data_9IHT
# 
_entry.id   9IHT 
# 
_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   9IHT         pdb_00009iht 10.2210/pdb9iht/pdb 
WWPDB D_1300048760 ?            ?                   
# 
_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                        9IHT 
_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 ? 
'Yu, F.'     3 ? 
# 
_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 branched    syn 
;4,6-dideoxy-4-{[(1S,4R,5S,6S)-4,5,6-trihydroxy-3-(hydroxymethyl)cyclohex-2-en-1-yl]amino}-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose
;
645.606   2   ? ? ? ? 
3 non-polymer syn GLYCEROL 92.094    2   ? ? ? ? 
4 water       nat water 18.015    485 ? ? ? ? 
# 
_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         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 GLYCEROL GOL 
4 water    HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   LYS n 
1 3   LYS n 
1 4   LEU n 
1 5   PHE n 
1 6   LEU n 
1 7   VAL n 
1 8   PHE n 
1 9   TRP n 
1 10  TRP n 
1 11  HIS n 
1 12  MET n 
1 13  HIS n 
1 14  GLN n 
1 15  PRO n 
1 16  LEU n 
1 17  TYR n 
1 18  ARG n 
1 19  GLU n 
1 20  PRO n 
1 21  TYR n 
1 22  THR n 
1 23  GLY n 
1 24  GLU n 
1 25  TYR n 
1 26  LEU n 
1 27  LEU n 
1 28  PRO n 
1 29  TRP n 
1 30  THR n 
1 31  PHE n 
1 32  PHE n 
1 33  HIS n 
1 34  ALA n 
1 35  VAL n 
1 36  LYS n 
1 37  ASP n 
1 38  TYR n 
1 39  TYR n 
1 40  ASP n 
1 41  MET n 
1 42  PRO n 
1 43  ALA n 
1 44  TYR n 
1 45  LEU n 
1 46  LYS n 
1 47  ASP n 
1 48  PHE n 
1 49  GLU n 
1 50  ILE n 
1 51  LYS n 
1 52  LEU n 
1 53  ASN n 
1 54  PHE n 
1 55  ASN n 
1 56  LEU n 
1 57  THR n 
1 58  PRO n 
1 59  VAL n 
1 60  LEU n 
1 61  ILE n 
1 62  ASP n 
1 63  GLN n 
1 64  ILE n 
1 65  GLN n 
1 66  GLU n 
1 67  TYR n 
1 68  ALA n 
1 69  GLN n 
1 70  GLY n 
1 71  LYS n 
1 72  ALA n 
1 73  LYS n 
1 74  ASP n 
1 75  VAL n 
1 76  PHE n 
1 77  LEU n 
1 78  GLU n 
1 79  ALA n 
1 80  ILE n 
1 81  ARG n 
1 82  LYS n 
1 83  ASP n 
1 84  PRO n 
1 85  ASP n 
1 86  ASP n 
1 87  LEU n 
1 88  GLU n 
1 89  LYS n 
1 90  GLU n 
1 91  GLU n 
1 92  VAL n 
1 93  GLU n 
1 94  LYS n 
1 95  LEU n 
1 96  ILE n 
1 97  GLU n 
1 98  PHE n 
1 99  THR n 
1 100 LYS n 
1 101 LEU n 
1 102 ASN n 
1 103 TYR n 
1 104 GLU n 
1 105 LYS n 
1 106 PRO n 
1 107 ILE n 
1 108 TYR n 
1 109 ARG n 
1 110 PHE n 
1 111 GLU n 
1 112 ARG n 
1 113 ILE n 
1 114 ARG n 
1 115 GLU n 
1 116 LEU n 
1 117 MET n 
1 118 ASN n 
1 119 LYS n 
1 120 GLU n 
1 121 LYS n 
1 122 LEU n 
1 123 ASN n 
1 124 ARG n 
1 125 GLU n 
1 126 GLU n 
1 127 LEU n 
1 128 LEU n 
1 129 ASP n 
1 130 LEU n 
1 131 GLN n 
1 132 THR n 
1 133 LEU n 
1 134 ASN n 
1 135 LEU n 
1 136 LEU n 
1 137 ALA n 
1 138 TRP n 
1 139 CYS n 
1 140 GLY n 
1 141 ARG n 
1 142 THR n 
1 143 LEU n 
1 144 ARG n 
1 145 LYS n 
1 146 ASP n 
1 147 LEU n 
1 148 LYS n 
1 149 ASP n 
1 150 LEU n 
1 151 LEU n 
1 152 ASN n 
1 153 LYS n 
1 154 GLY n 
1 155 ARG n 
1 156 ASN n 
1 157 TYR n 
1 158 THR n 
1 159 GLN n 
1 160 GLU n 
1 161 GLU n 
1 162 LYS n 
1 163 GLU n 
1 164 TYR n 
1 165 VAL n 
1 166 LEU n 
1 167 ASN n 
1 168 LYS n 
1 169 TYR n 
1 170 PHE n 
1 171 GLU n 
1 172 ILE n 
1 173 ILE n 
1 174 LYS n 
1 175 LYS n 
1 176 THR n 
1 177 LEU n 
1 178 SER n 
1 179 ILE n 
1 180 TYR n 
1 181 ARG n 
1 182 GLU n 
1 183 ILE n 
1 184 LYS n 
1 185 GLU n 
1 186 GLU n 
1 187 GLY n 
1 188 LYS n 
1 189 GLY n 
1 190 SER n 
1 191 VAL n 
1 192 SER n 
1 193 THR n 
1 194 SER n 
1 195 PRO n 
1 196 TYR n 
1 197 TYR n 
1 198 HIS n 
1 199 PRO n 
1 200 LEU n 
1 201 ILE n 
1 202 PRO n 
1 203 ILE n 
1 204 LEU n 
1 205 LEU n 
1 206 ASN n 
1 207 PRO n 
1 208 ASN n 
1 209 CYS n 
1 210 VAL n 
1 211 TYR n 
1 212 GLU n 
1 213 THR n 
1 214 THR n 
1 215 PRO n 
1 216 ASN n 
1 217 VAL n 
1 218 LYS n 
1 219 ILE n 
1 220 PRO n 
1 221 ASP n 
1 222 PHE n 
1 223 ALA n 
1 224 VAL n 
1 225 SER n 
1 226 PHE n 
1 227 ARG n 
1 228 GLU n 
1 229 ASP n 
1 230 ALA n 
1 231 SER n 
1 232 LYS n 
1 233 HIS n 
1 234 VAL n 
1 235 GLU n 
1 236 LEU n 
1 237 ALA n 
1 238 LYS n 
1 239 GLU n 
1 240 LYS n 
1 241 TYR n 
1 242 PHE n 
1 243 GLU n 
1 244 ILE n 
1 245 PHE n 
1 246 GLY n 
1 247 GLU n 
1 248 HIS n 
1 249 PRO n 
1 250 VAL n 
1 251 TYR n 
1 252 MET n 
1 253 TRP n 
1 254 PRO n 
1 255 PRO n 
1 256 GLU n 
1 257 ALA n 
1 258 SER n 
1 259 VAL n 
1 260 SER n 
1 261 ASN n 
1 262 GLU n 
1 263 ALA n 
1 264 LEU n 
1 265 GLU n 
1 266 LEU n 
1 267 TYR n 
1 268 TYR n 
1 269 GLU n 
1 270 LYS n 
1 271 GLY n 
1 272 ILE n 
1 273 ASN n 
1 274 MET n 
1 275 LEU n 
1 276 ALA n 
1 277 THR n 
1 278 ASP n 
1 279 GLU n 
1 280 VAL n 
1 281 ILE n 
1 282 LEU n 
1 283 LYS n 
1 284 ASN n 
1 285 SER n 
1 286 VAL n 
1 287 GLU n 
1 288 ARG n 
1 289 ALA n 
1 290 SER n 
1 291 PRO n 
1 292 TYR n 
1 293 LEU n 
1 294 ARG n 
1 295 TYR n 
1 296 TYR n 
1 297 PHE n 
1 298 ARG n 
1 299 GLU n 
1 300 LEU n 
1 301 ILE n 
1 302 SER n 
1 303 VAL n 
1 304 PHE n 
1 305 PHE n 
1 306 ARG n 
1 307 ASP n 
1 308 LYS n 
1 309 THR n 
1 310 LEU n 
1 311 SER n 
1 312 ASP n 
1 313 LEU n 
1 314 ILE n 
1 315 GLY n 
1 316 PHE n 
1 317 SER n 
1 318 TYR n 
1 319 HIS n 
1 320 ALA n 
1 321 TRP n 
1 322 ASN n 
1 323 ALA n 
1 324 GLU n 
1 325 ASP n 
1 326 ALA n 
1 327 VAL n 
1 328 ARG n 
1 329 ASP n 
1 330 PHE n 
1 331 ILE n 
1 332 GLY n 
1 333 ARG n 
1 334 LEU n 
1 335 LYS n 
1 336 LYS n 
1 337 ILE n 
1 338 HIS n 
1 339 GLU n 
1 340 SER n 
1 341 VAL n 
1 342 ASP n 
1 343 PHE n 
1 344 GLN n 
1 345 PRO n 
1 346 VAL n 
1 347 VAL n 
1 348 PHE n 
1 349 VAL n 
1 350 VAL n 
1 351 LEU n 
1 352 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 VF5' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     224324 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
_pdbx_entity_branch.entity_id   2 
_pdbx_entity_branch.type        oligosaccharide 
# 
loop_
_pdbx_entity_branch_descriptor.ordinal 
_pdbx_entity_branch_descriptor.entity_id 
_pdbx_entity_branch_descriptor.descriptor 
_pdbx_entity_branch_descriptor.type 
_pdbx_entity_branch_descriptor.program 
_pdbx_entity_branch_descriptor.program_version 
1 2 'WURCS=2.0/2,3,2/[a2122h-1a_1-5][a2122m-1a_1-5_4*NC^SC^SC^SC^RCCO/7=^ZC$3/6O/5O/4O]/1-1-2/a4-b1_b4-c1' WURCS  PDB2Glycan 1.1.0 
2 2 '[][a-D-Glcp]{[(4+1)][a-D-Glcp]{[(4+1)][a-D-6-deoxy-Glcp4N]{[(4+1)][&lt;C7O4&gt;]{}}}}'                LINUCS PDB-CARE   ?     
# 
loop_
_pdbx_entity_branch_link.link_id 
_pdbx_entity_branch_link.entity_id 
_pdbx_entity_branch_link.entity_branch_list_num_1 
_pdbx_entity_branch_link.comp_id_1 
_pdbx_entity_branch_link.atom_id_1 
_pdbx_entity_branch_link.leaving_atom_id_1 
_pdbx_entity_branch_link.entity_branch_list_num_2 
_pdbx_entity_branch_link.comp_id_2 
_pdbx_entity_branch_link.atom_id_2 
_pdbx_entity_branch_link.leaving_atom_id_2 
_pdbx_entity_branch_link.value_order 
_pdbx_entity_branch_link.details 
1 2 2 GLC C1 O1 1 GLC O4 HO4 sing ? 
2 2 3 AC1 C1 O1 2 GLC O4 HO4 sing ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
AC1 D-saccharide                  . 
'4,6-dideoxy-4-{[(1S,4R,5S,6S)-4,5,6-trihydroxy-3-(hydroxymethyl)cyclohex-2-en-1-yl]amino}-alpha-D-glucopyranose' 
;6-METHYL-5-(4,5,6-TRIHYDROXY-3-HYDROXYMETHYL-CYCLOHEX-2-ENYLAMINO)-TETRAHYDRO-PYRAN-2,3,4-TRIOL; 4,6-dideoxy-4-{[(1S,4R,5S,6S)-4,5,6-trihydroxy-3-(hydroxymethyl)cyclohex-2-en-1-yl]amino}-alpha-D-glucose; 4,6-dideoxy-4-{[(1S,4R,5S,6S)-4,5,6-trihydroxy-3-(hydroxymethyl)cyclohex-2-en-1-yl]amino}-D-glucose; 4,6-dideoxy-4-{[(1S,4R,5S,6S)-4,5,6-trihydroxy-3-(hydroxymethyl)cyclohex-2-en-1-yl]amino}-glucose
;
'C13 H23 N O8'   321.324 
ALA 'L-peptide linking'           y ALANINE ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking'           y ARGININE ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking'           y ASPARAGINE ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking'           y 'ASPARTIC ACID' ? 'C4 H7 N O4'     133.103 
CYS 'L-peptide linking'           y CYSTEINE ? 'C3 H7 N O2 S'   121.158 
GLC 'D-saccharide, alpha linking' . alpha-D-glucopyranose 'alpha-D-glucose; D-glucose; glucose' 'C6 H12 O6'      180.156 
GLN 'L-peptide linking'           y GLUTAMINE ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking'           y 'GLUTAMIC ACID' ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'             y GLYCINE ? 'C2 H5 N O2'     75.067  
GOL non-polymer                   . GLYCEROL 'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3'       92.094  
HIS 'L-peptide linking'           y HISTIDINE ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer                   . WATER ? 'H2 O'           18.015  
ILE 'L-peptide linking'           y ISOLEUCINE ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking'           y LEUCINE ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking'           y LYSINE ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking'           y METHIONINE ? 'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking'           y PHENYLALANINE ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking'           y PROLINE ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking'           y SERINE ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking'           y THREONINE ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking'           y TRYPTOPHAN ? 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking'           y TYROSINE ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking'           y VALINE ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_chem_comp_identifier.comp_id 
_pdbx_chem_comp_identifier.type 
_pdbx_chem_comp_identifier.program 
_pdbx_chem_comp_identifier.program_version 
_pdbx_chem_comp_identifier.identifier 
GLC 'CONDENSED IUPAC CARBOHYDRATE SYMBOL' GMML     1.0 DGlcpa            
GLC 'COMMON NAME'                         GMML     1.0 a-D-glucopyranose 
GLC 'IUPAC CARBOHYDRATE SYMBOL'           PDB-CARE 1.0 a-D-Glcp          
GLC 'SNFG CARBOHYDRATE SYMBOL'            GMML     1.0 Glc               
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   ?   ?   ?   A . n 
A 1 2   LYS 2   2   2   LYS LYS A . n 
A 1 3   LYS 3   3   3   LYS LYS A . n 
A 1 4   LEU 4   4   4   LEU LEU A . n 
A 1 5   PHE 5   5   5   PHE PHE A . n 
A 1 6   LEU 6   6   6   LEU LEU A . n 
A 1 7   VAL 7   7   7   VAL VAL A . n 
A 1 8   PHE 8   8   8   PHE PHE A . n 
A 1 9   TRP 9   9   9   TRP TRP A . n 
A 1 10  TRP 10  10  10  TRP TRP A . n 
A 1 11  HIS 11  11  11  HIS HIS A . n 
A 1 12  MET 12  12  12  MET MET A . n 
A 1 13  HIS 13  13  13  HIS HIS A . n 
A 1 14  GLN 14  14  14  GLN GLN A . n 
A 1 15  PRO 15  15  15  PRO PRO A . n 
A 1 16  LEU 16  16  16  LEU LEU A . n 
A 1 17  TYR 17  17  17  TYR TYR A . n 
A 1 18  ARG 18  18  18  ARG ARG A . n 
A 1 19  GLU 19  19  19  GLU GLU A . n 
A 1 20  PRO 20  20  20  PRO PRO A . n 
A 1 21  TYR 21  21  21  TYR TYR A . n 
A 1 22  THR 22  22  22  THR THR A . n 
A 1 23  GLY 23  23  23  GLY GLY A . n 
A 1 24  GLU 24  24  24  GLU GLU A . n 
A 1 25  TYR 25  25  25  TYR TYR A . n 
A 1 26  LEU 26  26  26  LEU LEU A . n 
A 1 27  LEU 27  27  27  LEU LEU A . n 
A 1 28  PRO 28  28  28  PRO PRO A . n 
A 1 29  TRP 29  29  29  TRP TRP A . n 
A 1 30  THR 30  30  30  THR THR A . n 
A 1 31  PHE 31  31  31  PHE PHE A . n 
A 1 32  PHE 32  32  32  PHE PHE A . n 
A 1 33  HIS 33  33  33  HIS HIS A . n 
A 1 34  ALA 34  34  34  ALA ALA A . n 
A 1 35  VAL 35  35  35  VAL VAL A . n 
A 1 36  LYS 36  36  36  LYS LYS A . n 
A 1 37  ASP 37  37  37  ASP ASP A . n 
A 1 38  TYR 38  38  38  TYR TYR A . n 
A 1 39  TYR 39  39  39  TYR TYR A . n 
A 1 40  ASP 40  40  40  ASP ASP A . n 
A 1 41  MET 41  41  41  MET MET A . n 
A 1 42  PRO 42  42  42  PRO PRO A . n 
A 1 43  ALA 43  43  43  ALA ALA A . n 
A 1 44  TYR 44  44  44  TYR TYR A . n 
A 1 45  LEU 45  45  45  LEU LEU A . n 
A 1 46  LYS 46  46  46  LYS LYS A . n 
A 1 47  ASP 47  47  47  ASP ASP A . n 
A 1 48  PHE 48  48  48  PHE PHE A . n 
A 1 49  GLU 49  49  49  GLU GLU A . n 
A 1 50  ILE 50  50  50  ILE ILE A . n 
A 1 51  LYS 51  51  51  LYS LYS A . n 
A 1 52  LEU 52  52  52  LEU LEU A . n 
A 1 53  ASN 53  53  53  ASN ASN A . n 
A 1 54  PHE 54  54  54  PHE PHE A . n 
A 1 55  ASN 55  55  55  ASN ASN A . n 
A 1 56  LEU 56  56  56  LEU LEU A . n 
A 1 57  THR 57  57  57  THR THR A . n 
A 1 58  PRO 58  58  58  PRO PRO A . n 
A 1 59  VAL 59  59  59  VAL VAL A . n 
A 1 60  LEU 60  60  60  LEU LEU A . n 
A 1 61  ILE 61  61  61  ILE ILE A . n 
A 1 62  ASP 62  62  62  ASP ASP A . n 
A 1 63  GLN 63  63  63  GLN GLN A . n 
A 1 64  ILE 64  64  64  ILE ILE A . n 
A 1 65  GLN 65  65  65  GLN GLN A . n 
A 1 66  GLU 66  66  66  GLU GLU A . n 
A 1 67  TYR 67  67  67  TYR TYR A . n 
A 1 68  ALA 68  68  68  ALA ALA A . n 
A 1 69  GLN 69  69  69  GLN GLN A . n 
A 1 70  GLY 70  70  70  GLY GLY A . n 
A 1 71  LYS 71  71  71  LYS LYS A . n 
A 1 72  ALA 72  72  72  ALA ALA A . n 
A 1 73  LYS 73  73  73  LYS LYS A . n 
A 1 74  ASP 74  74  74  ASP ASP A . n 
A 1 75  VAL 75  75  75  VAL VAL A . n 
A 1 76  PHE 76  76  76  PHE PHE A . n 
A 1 77  LEU 77  77  77  LEU LEU A . n 
A 1 78  GLU 78  78  78  GLU GLU A . n 
A 1 79  ALA 79  79  79  ALA ALA A . n 
A 1 80  ILE 80  80  80  ILE ILE A . n 
A 1 81  ARG 81  81  81  ARG ARG A . n 
A 1 82  LYS 82  82  82  LYS LYS A . n 
A 1 83  ASP 83  83  83  ASP ASP A . n 
A 1 84  PRO 84  84  84  PRO PRO A . n 
A 1 85  ASP 85  85  85  ASP ASP A . n 
A 1 86  ASP 86  86  86  ASP ASP A . n 
A 1 87  LEU 87  87  87  LEU LEU A . n 
A 1 88  GLU 88  88  88  GLU GLU A . n 
A 1 89  LYS 89  89  89  LYS LYS A . n 
A 1 90  GLU 90  90  90  GLU GLU A . n 
A 1 91  GLU 91  91  91  GLU GLU A . n 
A 1 92  VAL 92  92  92  VAL VAL A . n 
A 1 93  GLU 93  93  93  GLU GLU A . n 
A 1 94  LYS 94  94  94  LYS LYS A . n 
A 1 95  LEU 95  95  95  LEU LEU A . n 
A 1 96  ILE 96  96  96  ILE ILE A . n 
A 1 97  GLU 97  97  97  GLU GLU A . n 
A 1 98  PHE 98  98  98  PHE PHE A . n 
A 1 99  THR 99  99  99  THR THR A . n 
A 1 100 LYS 100 100 100 LYS LYS A . n 
A 1 101 LEU 101 101 101 LEU LEU A . n 
A 1 102 ASN 102 102 102 ASN ASN A . n 
A 1 103 TYR 103 103 103 TYR TYR A . n 
A 1 104 GLU 104 104 104 GLU GLU A . n 
A 1 105 LYS 105 105 105 LYS LYS A . n 
A 1 106 PRO 106 106 106 PRO PRO A . n 
A 1 107 ILE 107 107 107 ILE ILE A . n 
A 1 108 TYR 108 108 108 TYR TYR A . n 
A 1 109 ARG 109 109 109 ARG ARG A . n 
A 1 110 PHE 110 110 110 PHE PHE A . n 
A 1 111 GLU 111 111 111 GLU GLU A . n 
A 1 112 ARG 112 112 112 ARG ARG A . n 
A 1 113 ILE 113 113 113 ILE ILE A . n 
A 1 114 ARG 114 114 114 ARG ARG A . n 
A 1 115 GLU 115 115 115 GLU GLU A . n 
A 1 116 LEU 116 116 116 LEU LEU A . n 
A 1 117 MET 117 117 117 MET MET A . n 
A 1 118 ASN 118 118 118 ASN ASN A . n 
A 1 119 LYS 119 119 119 LYS LYS A . n 
A 1 120 GLU 120 120 120 GLU GLU A . n 
A 1 121 LYS 121 121 121 LYS LYS A . n 
A 1 122 LEU 122 122 122 LEU LEU A . n 
A 1 123 ASN 123 123 123 ASN ASN A . n 
A 1 124 ARG 124 124 124 ARG ARG A . n 
A 1 125 GLU 125 125 125 GLU GLU A . n 
A 1 126 GLU 126 126 126 GLU GLU A . n 
A 1 127 LEU 127 127 127 LEU LEU A . n 
A 1 128 LEU 128 128 128 LEU LEU A . n 
A 1 129 ASP 129 129 129 ASP ASP A . n 
A 1 130 LEU 130 130 130 LEU LEU A . n 
A 1 131 GLN 131 131 131 GLN GLN A . n 
A 1 132 THR 132 132 132 THR THR A . n 
A 1 133 LEU 133 133 133 LEU LEU A . n 
A 1 134 ASN 134 134 134 ASN ASN A . n 
A 1 135 LEU 135 135 135 LEU LEU A . n 
A 1 136 LEU 136 136 136 LEU LEU A . n 
A 1 137 ALA 137 137 137 ALA ALA A . n 
A 1 138 TRP 138 138 138 TRP TRP A . n 
A 1 139 CYS 139 139 139 CYS CYS A . n 
A 1 140 GLY 140 140 140 GLY GLY A . n 
A 1 141 ARG 141 141 141 ARG ARG A . n 
A 1 142 THR 142 142 142 THR THR A . n 
A 1 143 LEU 143 143 143 LEU LEU A . n 
A 1 144 ARG 144 144 144 ARG ARG A . n 
A 1 145 LYS 145 145 145 LYS LYS A . n 
A 1 146 ASP 146 146 146 ASP ASP A . n 
A 1 147 LEU 147 147 147 LEU LEU A . n 
A 1 148 LYS 148 148 148 LYS LYS A . n 
A 1 149 ASP 149 149 149 ASP ASP A . n 
A 1 150 LEU 150 150 150 LEU LEU A . n 
A 1 151 LEU 151 151 151 LEU LEU A . n 
A 1 152 ASN 152 152 152 ASN ASN A . n 
A 1 153 LYS 153 153 153 LYS LYS A . n 
A 1 154 GLY 154 154 154 GLY GLY A . n 
A 1 155 ARG 155 155 155 ARG ARG A . n 
A 1 156 ASN 156 156 156 ASN ASN A . n 
A 1 157 TYR 157 157 157 TYR TYR A . n 
A 1 158 THR 158 158 158 THR THR A . n 
A 1 159 GLN 159 159 159 GLN GLN A . n 
A 1 160 GLU 160 160 160 GLU GLU A . n 
A 1 161 GLU 161 161 161 GLU GLU A . n 
A 1 162 LYS 162 162 162 LYS LYS A . n 
A 1 163 GLU 163 163 163 GLU GLU A . n 
A 1 164 TYR 164 164 164 TYR TYR A . n 
A 1 165 VAL 165 165 165 VAL VAL A . n 
A 1 166 LEU 166 166 166 LEU LEU A . n 
A 1 167 ASN 167 167 167 ASN ASN A . n 
A 1 168 LYS 168 168 168 LYS LYS A . n 
A 1 169 TYR 169 169 169 TYR TYR A . n 
A 1 170 PHE 170 170 170 PHE PHE A . n 
A 1 171 GLU 171 171 171 GLU GLU A . n 
A 1 172 ILE 172 172 172 ILE ILE A . n 
A 1 173 ILE 173 173 173 ILE ILE A . n 
A 1 174 LYS 174 174 174 LYS LYS A . n 
A 1 175 LYS 175 175 175 LYS LYS A . n 
A 1 176 THR 176 176 176 THR THR A . n 
A 1 177 LEU 177 177 177 LEU LEU A . n 
A 1 178 SER 178 178 178 SER SER A . n 
A 1 179 ILE 179 179 179 ILE ILE A . n 
A 1 180 TYR 180 180 180 TYR TYR A . n 
A 1 181 ARG 181 181 181 ARG ARG A . n 
A 1 182 GLU 182 182 182 GLU GLU A . n 
A 1 183 ILE 183 183 183 ILE ILE A . n 
A 1 184 LYS 184 184 184 LYS LYS A . n 
A 1 185 GLU 185 185 185 GLU GLU A . n 
A 1 186 GLU 186 186 186 GLU GLU A . n 
A 1 187 GLY 187 187 187 GLY GLY A . n 
A 1 188 LYS 188 188 188 LYS LYS A . n 
A 1 189 GLY 189 189 189 GLY GLY A . n 
A 1 190 SER 190 190 190 SER SER A . n 
A 1 191 VAL 191 191 191 VAL VAL A . n 
A 1 192 SER 192 192 192 SER SER A . n 
A 1 193 THR 193 193 193 THR THR A . n 
A 1 194 SER 194 194 194 SER SER A . n 
A 1 195 PRO 195 195 195 PRO PRO A . n 
A 1 196 TYR 196 196 196 TYR TYR A . n 
A 1 197 TYR 197 197 197 TYR TYR A . n 
A 1 198 HIS 198 198 198 HIS HIS A . n 
A 1 199 PRO 199 199 199 PRO PRO A . n 
A 1 200 LEU 200 200 200 LEU LEU A . n 
A 1 201 ILE 201 201 201 ILE ILE A . n 
A 1 202 PRO 202 202 202 PRO PRO A . n 
A 1 203 ILE 203 203 203 ILE ILE A . n 
A 1 204 LEU 204 204 204 LEU LEU A . n 
A 1 205 LEU 205 205 205 LEU LEU A . n 
A 1 206 ASN 206 206 206 ASN ASN A . n 
A 1 207 PRO 207 207 207 PRO PRO A . n 
A 1 208 ASN 208 208 208 ASN ASN A . n 
A 1 209 CYS 209 209 209 CYS CYS A . n 
A 1 210 VAL 210 210 210 VAL VAL A . n 
A 1 211 TYR 211 211 211 TYR TYR A . n 
A 1 212 GLU 212 212 212 GLU GLU A . n 
A 1 213 THR 213 213 213 THR THR A . n 
A 1 214 THR 214 214 214 THR THR A . n 
A 1 215 PRO 215 215 215 PRO PRO A . n 
A 1 216 ASN 216 216 216 ASN ASN A . n 
A 1 217 VAL 217 217 217 VAL VAL A . n 
A 1 218 LYS 218 218 218 LYS LYS A . n 
A 1 219 ILE 219 219 219 ILE ILE A . n 
A 1 220 PRO 220 220 220 PRO PRO A . n 
A 1 221 ASP 221 221 221 ASP ASP A . n 
A 1 222 PHE 222 222 222 PHE PHE A . n 
A 1 223 ALA 223 223 223 ALA ALA A . n 
A 1 224 VAL 224 224 224 VAL VAL A . n 
A 1 225 SER 225 225 225 SER SER A . n 
A 1 226 PHE 226 226 226 PHE PHE A . n 
A 1 227 ARG 227 227 227 ARG ARG A . n 
A 1 228 GLU 228 228 228 GLU GLU A . n 
A 1 229 ASP 229 229 229 ASP ASP A . n 
A 1 230 ALA 230 230 230 ALA ALA A . n 
A 1 231 SER 231 231 231 SER SER A . n 
A 1 232 LYS 232 232 232 LYS LYS A . n 
A 1 233 HIS 233 233 233 HIS HIS A . n 
A 1 234 VAL 234 234 234 VAL VAL A . n 
A 1 235 GLU 235 235 235 GLU GLU A . n 
A 1 236 LEU 236 236 236 LEU LEU A . n 
A 1 237 ALA 237 237 237 ALA ALA A . n 
A 1 238 LYS 238 238 238 LYS LYS A . n 
A 1 239 GLU 239 239 239 GLU GLU A . n 
A 1 240 LYS 240 240 240 LYS LYS A . n 
A 1 241 TYR 241 241 241 TYR TYR A . n 
A 1 242 PHE 242 242 242 PHE PHE A . n 
A 1 243 GLU 243 243 243 GLU GLU A . n 
A 1 244 ILE 244 244 244 ILE ILE A . n 
A 1 245 PHE 245 245 245 PHE PHE A . n 
A 1 246 GLY 246 246 246 GLY GLY A . n 
A 1 247 GLU 247 247 247 GLU GLU A . n 
A 1 248 HIS 248 248 248 HIS HIS A . n 
A 1 249 PRO 249 249 249 PRO PRO A . n 
A 1 250 VAL 250 250 250 VAL VAL A . n 
A 1 251 TYR 251 251 251 TYR TYR A . n 
A 1 252 MET 252 252 252 MET MET A . n 
A 1 253 TRP 253 253 253 TRP TRP A . n 
A 1 254 PRO 254 254 254 PRO PRO A . n 
A 1 255 PRO 255 255 255 PRO PRO A . n 
A 1 256 GLU 256 256 256 GLU GLU A . n 
A 1 257 ALA 257 257 257 ALA ALA A . n 
A 1 258 SER 258 258 258 SER SER A . n 
A 1 259 VAL 259 259 259 VAL VAL A . n 
A 1 260 SER 260 260 260 SER SER A . n 
A 1 261 ASN 261 261 261 ASN ASN A . n 
A 1 262 GLU 262 262 262 GLU GLU A . n 
A 1 263 ALA 263 263 263 ALA ALA A . n 
A 1 264 LEU 264 264 264 LEU LEU A . n 
A 1 265 GLU 265 265 265 GLU GLU A . n 
A 1 266 LEU 266 266 266 LEU LEU A . n 
A 1 267 TYR 267 267 267 TYR TYR A . n 
A 1 268 TYR 268 268 268 TYR TYR A . n 
A 1 269 GLU 269 269 269 GLU GLU A . n 
A 1 270 LYS 270 270 270 LYS LYS A . n 
A 1 271 GLY 271 271 271 GLY GLY A . n 
A 1 272 ILE 272 272 272 ILE ILE A . n 
A 1 273 ASN 273 273 273 ASN ASN A . n 
A 1 274 MET 274 274 274 MET MET A . n 
A 1 275 LEU 275 275 275 LEU LEU A . n 
A 1 276 ALA 276 276 276 ALA ALA A . n 
A 1 277 THR 277 277 277 THR THR A . n 
A 1 278 ASP 278 278 278 ASP ASP A . n 
A 1 279 GLU 279 279 279 GLU GLU A . n 
A 1 280 VAL 280 280 280 VAL VAL A . n 
A 1 281 ILE 281 281 281 ILE ILE A . n 
A 1 282 LEU 282 282 282 LEU LEU A . n 
A 1 283 LYS 283 283 283 LYS LYS A . n 
A 1 284 ASN 284 284 284 ASN ASN A . n 
A 1 285 SER 285 285 285 SER SER A . n 
A 1 286 VAL 286 286 286 VAL VAL A . n 
A 1 287 GLU 287 287 287 GLU GLU A . n 
A 1 288 ARG 288 288 288 ARG ARG A . n 
A 1 289 ALA 289 289 289 ALA ALA A . n 
A 1 290 SER 290 290 290 SER SER A . n 
A 1 291 PRO 291 291 291 PRO PRO A . n 
A 1 292 TYR 292 292 292 TYR TYR A . n 
A 1 293 LEU 293 293 293 LEU LEU A . n 
A 1 294 ARG 294 294 294 ARG ARG A . n 
A 1 295 TYR 295 295 295 TYR TYR A . n 
A 1 296 TYR 296 296 296 TYR TYR A . n 
A 1 297 PHE 297 297 297 PHE PHE A . n 
A 1 298 ARG 298 298 298 ARG ARG A . n 
A 1 299 GLU 299 299 299 GLU GLU A . n 
A 1 300 LEU 300 300 300 LEU LEU A . n 
A 1 301 ILE 301 301 301 ILE ILE A . n 
A 1 302 SER 302 302 302 SER SER A . n 
A 1 303 VAL 303 303 303 VAL VAL A . n 
A 1 304 PHE 304 304 304 PHE PHE A . n 
A 1 305 PHE 305 305 305 PHE PHE A . n 
A 1 306 ARG 306 306 306 ARG ARG A . n 
A 1 307 ASP 307 307 307 ASP ASP A . n 
A 1 308 LYS 308 308 308 LYS LYS A . n 
A 1 309 THR 309 309 309 THR THR A . n 
A 1 310 LEU 310 310 310 LEU LEU A . n 
A 1 311 SER 311 311 311 SER SER A . n 
A 1 312 ASP 312 312 312 ASP ASP A . n 
A 1 313 LEU 313 313 313 LEU LEU A . n 
A 1 314 ILE 314 314 314 ILE ILE A . n 
A 1 315 GLY 315 315 315 GLY GLY A . n 
A 1 316 PHE 316 316 316 PHE PHE A . n 
A 1 317 SER 317 317 317 SER SER A . n 
A 1 318 TYR 318 318 318 TYR TYR A . n 
A 1 319 HIS 319 319 319 HIS HIS A . n 
A 1 320 ALA 320 320 320 ALA ALA A . n 
A 1 321 TRP 321 321 321 TRP TRP A . n 
A 1 322 ASN 322 322 322 ASN ASN A . n 
A 1 323 ALA 323 323 323 ALA ALA A . n 
A 1 324 GLU 324 324 324 GLU GLU A . n 
A 1 325 ASP 325 325 325 ASP ASP A . n 
A 1 326 ALA 326 326 326 ALA ALA A . n 
A 1 327 VAL 327 327 327 VAL VAL A . n 
A 1 328 ARG 328 328 328 ARG ARG A . n 
A 1 329 ASP 329 329 329 ASP ASP A . n 
A 1 330 PHE 330 330 330 PHE PHE A . n 
A 1 331 ILE 331 331 331 ILE ILE A . n 
A 1 332 GLY 332 332 332 GLY GLY A . n 
A 1 333 ARG 333 333 333 ARG ARG A . n 
A 1 334 LEU 334 334 334 LEU LEU A . n 
A 1 335 LYS 335 335 335 LYS LYS A . n 
A 1 336 LYS 336 336 336 LYS LYS A . n 
A 1 337 ILE 337 337 337 ILE ILE A . n 
A 1 338 HIS 338 338 338 HIS HIS A . n 
A 1 339 GLU 339 339 339 GLU GLU A . n 
A 1 340 SER 340 340 340 SER SER A . n 
A 1 341 VAL 341 341 341 VAL VAL A . n 
A 1 342 ASP 342 342 342 ASP ASP A . n 
A 1 343 PHE 343 343 343 PHE PHE A . n 
A 1 344 GLN 344 344 344 GLN GLN A . n 
A 1 345 PRO 345 345 345 PRO PRO A . n 
A 1 346 VAL 346 346 346 VAL VAL A . n 
A 1 347 VAL 347 347 347 VAL VAL A . n 
A 1 348 PHE 348 348 348 PHE PHE A . n 
A 1 349 VAL 349 349 349 VAL VAL A . n 
A 1 350 VAL 350 350 350 VAL VAL A . n 
A 1 351 LEU 351 351 351 LEU LEU A . n 
A 1 352 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   ?   ?   ?   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_branch_scheme.asym_id 
_pdbx_branch_scheme.entity_id 
_pdbx_branch_scheme.mon_id 
_pdbx_branch_scheme.num 
_pdbx_branch_scheme.pdb_asym_id 
_pdbx_branch_scheme.pdb_mon_id 
_pdbx_branch_scheme.pdb_seq_num 
_pdbx_branch_scheme.auth_asym_id 
_pdbx_branch_scheme.auth_mon_id 
_pdbx_branch_scheme.auth_seq_num 
_pdbx_branch_scheme.hetero 
C 2 GLC 1 C GLC 1 A GLC 491 n 
C 2 GLC 2 C GLC 2 A GLC 492 n 
C 2 AC1 3 C AC1 3 A AC1 493 n 
D 2 GLC 1 D GLC 1 B GLC 491 n 
D 2 GLC 2 D GLC 2 B GLC 492 n 
D 2 AC1 3 D AC1 3 B AC1 493 n 
# 
loop_
_pdbx_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 AC1 ? ? AC1 ? ? 'SUBJECT OF INVESTIGATION' ? 
2 GLC ? ? GLC ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
E 3 GOL 1   501 501 GOL GOL A . 
F 3 GOL 1   501 501 GOL GOL B . 
G 4 HOH 1   601 463 HOH HOH A . 
G 4 HOH 2   602 419 HOH HOH A . 
G 4 HOH 3   603 319 HOH HOH A . 
G 4 HOH 4   604 438 HOH HOH A . 
G 4 HOH 5   605 495 HOH HOH A . 
G 4 HOH 6   606 256 HOH HOH A . 
G 4 HOH 7   607 254 HOH HOH A . 
G 4 HOH 8   608 255 HOH HOH A . 
G 4 HOH 9   609 499 HOH HOH A . 
G 4 HOH 10  610 430 HOH HOH A . 
G 4 HOH 11  611 406 HOH HOH A . 
G 4 HOH 12  612 171 HOH HOH A . 
G 4 HOH 13  613 62  HOH HOH A . 
G 4 HOH 14  614 154 HOH HOH A . 
G 4 HOH 15  615 100 HOH HOH A . 
G 4 HOH 16  616 17  HOH HOH A . 
G 4 HOH 17  617 358 HOH HOH A . 
G 4 HOH 18  618 385 HOH HOH A . 
G 4 HOH 19  619 38  HOH HOH A . 
G 4 HOH 20  620 384 HOH HOH A . 
G 4 HOH 21  621 337 HOH HOH A . 
G 4 HOH 22  622 332 HOH HOH A . 
G 4 HOH 23  623 7   HOH HOH A . 
G 4 HOH 24  624 375 HOH HOH A . 
G 4 HOH 25  625 329 HOH HOH A . 
G 4 HOH 26  626 219 HOH HOH A . 
G 4 HOH 27  627 36  HOH HOH A . 
G 4 HOH 28  628 208 HOH HOH A . 
G 4 HOH 29  629 183 HOH HOH A . 
G 4 HOH 30  630 251 HOH HOH A . 
G 4 HOH 31  631 4   HOH HOH A . 
G 4 HOH 32  632 140 HOH HOH A . 
G 4 HOH 33  633 470 HOH HOH A . 
G 4 HOH 34  634 111 HOH HOH A . 
G 4 HOH 35  635 79  HOH HOH A . 
G 4 HOH 36  636 168 HOH HOH A . 
G 4 HOH 37  637 273 HOH HOH A . 
G 4 HOH 38  638 489 HOH HOH A . 
G 4 HOH 39  639 264 HOH HOH A . 
G 4 HOH 40  640 353 HOH HOH A . 
G 4 HOH 41  641 282 HOH HOH A . 
G 4 HOH 42  642 67  HOH HOH A . 
G 4 HOH 43  643 34  HOH HOH A . 
G 4 HOH 44  644 335 HOH HOH A . 
G 4 HOH 45  645 227 HOH HOH A . 
G 4 HOH 46  646 46  HOH HOH A . 
G 4 HOH 47  647 349 HOH HOH A . 
G 4 HOH 48  648 177 HOH HOH A . 
G 4 HOH 49  649 328 HOH HOH A . 
G 4 HOH 50  650 280 HOH HOH A . 
G 4 HOH 51  651 161 HOH HOH A . 
G 4 HOH 52  652 90  HOH HOH A . 
G 4 HOH 53  653 324 HOH HOH A . 
G 4 HOH 54  654 18  HOH HOH A . 
G 4 HOH 55  655 83  HOH HOH A . 
G 4 HOH 56  656 296 HOH HOH A . 
G 4 HOH 57  657 380 HOH HOH A . 
G 4 HOH 58  658 331 HOH HOH A . 
G 4 HOH 59  659 348 HOH HOH A . 
G 4 HOH 60  660 31  HOH HOH A . 
G 4 HOH 61  661 106 HOH HOH A . 
G 4 HOH 62  662 131 HOH HOH A . 
G 4 HOH 63  663 81  HOH HOH A . 
G 4 HOH 64  664 117 HOH HOH A . 
G 4 HOH 65  665 95  HOH HOH A . 
G 4 HOH 66  666 402 HOH HOH A . 
G 4 HOH 67  667 341 HOH HOH A . 
G 4 HOH 68  668 27  HOH HOH A . 
G 4 HOH 69  669 11  HOH HOH A . 
G 4 HOH 70  670 50  HOH HOH A . 
G 4 HOH 71  671 364 HOH HOH A . 
G 4 HOH 72  672 41  HOH HOH A . 
G 4 HOH 73  673 423 HOH HOH A . 
G 4 HOH 74  674 20  HOH HOH A . 
G 4 HOH 75  675 136 HOH HOH A . 
G 4 HOH 76  676 174 HOH HOH A . 
G 4 HOH 77  677 220 HOH HOH A . 
G 4 HOH 78  678 248 HOH HOH A . 
G 4 HOH 79  679 43  HOH HOH A . 
G 4 HOH 80  680 232 HOH HOH A . 
G 4 HOH 81  681 10  HOH HOH A . 
G 4 HOH 82  682 318 HOH HOH A . 
G 4 HOH 83  683 426 HOH HOH A . 
G 4 HOH 84  684 9   HOH HOH A . 
G 4 HOH 85  685 147 HOH HOH A . 
G 4 HOH 86  686 184 HOH HOH A . 
G 4 HOH 87  687 88  HOH HOH A . 
G 4 HOH 88  688 32  HOH HOH A . 
G 4 HOH 89  689 169 HOH HOH A . 
G 4 HOH 90  690 224 HOH HOH A . 
G 4 HOH 91  691 73  HOH HOH A . 
G 4 HOH 92  692 52  HOH HOH A . 
G 4 HOH 93  693 15  HOH HOH A . 
G 4 HOH 94  694 93  HOH HOH A . 
G 4 HOH 95  695 442 HOH HOH A . 
G 4 HOH 96  696 369 HOH HOH A . 
G 4 HOH 97  697 170 HOH HOH A . 
G 4 HOH 98  698 474 HOH HOH A . 
G 4 HOH 99  699 57  HOH HOH A . 
G 4 HOH 100 700 91  HOH HOH A . 
G 4 HOH 101 701 105 HOH HOH A . 
G 4 HOH 102 702 65  HOH HOH A . 
G 4 HOH 103 703 245 HOH HOH A . 
G 4 HOH 104 704 12  HOH HOH A . 
G 4 HOH 105 705 377 HOH HOH A . 
G 4 HOH 106 706 210 HOH HOH A . 
G 4 HOH 107 707 163 HOH HOH A . 
G 4 HOH 108 708 167 HOH HOH A . 
G 4 HOH 109 709 287 HOH HOH A . 
G 4 HOH 110 710 497 HOH HOH A . 
G 4 HOH 111 711 271 HOH HOH A . 
G 4 HOH 112 712 8   HOH HOH A . 
G 4 HOH 113 713 350 HOH HOH A . 
G 4 HOH 114 714 114 HOH HOH A . 
G 4 HOH 115 715 176 HOH HOH A . 
G 4 HOH 116 716 473 HOH HOH A . 
G 4 HOH 117 717 155 HOH HOH A . 
G 4 HOH 118 718 128 HOH HOH A . 
G 4 HOH 119 719 2   HOH HOH A . 
G 4 HOH 120 720 149 HOH HOH A . 
G 4 HOH 121 721 98  HOH HOH A . 
G 4 HOH 122 722 146 HOH HOH A . 
G 4 HOH 123 723 44  HOH HOH A . 
G 4 HOH 124 724 274 HOH HOH A . 
G 4 HOH 125 725 82  HOH HOH A . 
G 4 HOH 126 726 48  HOH HOH A . 
G 4 HOH 127 727 33  HOH HOH A . 
G 4 HOH 128 728 54  HOH HOH A . 
G 4 HOH 129 729 143 HOH HOH A . 
G 4 HOH 130 730 175 HOH HOH A . 
G 4 HOH 131 731 320 HOH HOH A . 
G 4 HOH 132 732 137 HOH HOH A . 
G 4 HOH 133 733 1   HOH HOH A . 
G 4 HOH 134 734 265 HOH HOH A . 
G 4 HOH 135 735 160 HOH HOH A . 
G 4 HOH 136 736 127 HOH HOH A . 
G 4 HOH 137 737 39  HOH HOH A . 
G 4 HOH 138 738 102 HOH HOH A . 
G 4 HOH 139 739 198 HOH HOH A . 
G 4 HOH 140 740 129 HOH HOH A . 
G 4 HOH 141 741 68  HOH HOH A . 
G 4 HOH 142 742 252 HOH HOH A . 
G 4 HOH 143 743 122 HOH HOH A . 
G 4 HOH 144 744 101 HOH HOH A . 
G 4 HOH 145 745 243 HOH HOH A . 
G 4 HOH 146 746 148 HOH HOH A . 
G 4 HOH 147 747 260 HOH HOH A . 
G 4 HOH 148 748 215 HOH HOH A . 
G 4 HOH 149 749 306 HOH HOH A . 
G 4 HOH 150 750 415 HOH HOH A . 
G 4 HOH 151 751 13  HOH HOH A . 
G 4 HOH 152 752 191 HOH HOH A . 
G 4 HOH 153 753 211 HOH HOH A . 
G 4 HOH 154 754 443 HOH HOH A . 
G 4 HOH 155 755 493 HOH HOH A . 
G 4 HOH 156 756 222 HOH HOH A . 
G 4 HOH 157 757 250 HOH HOH A . 
G 4 HOH 158 758 144 HOH HOH A . 
G 4 HOH 159 759 281 HOH HOH A . 
G 4 HOH 160 760 223 HOH HOH A . 
G 4 HOH 161 761 365 HOH HOH A . 
G 4 HOH 162 762 466 HOH HOH A . 
G 4 HOH 163 763 108 HOH HOH A . 
G 4 HOH 164 764 135 HOH HOH A . 
G 4 HOH 165 765 159 HOH HOH A . 
G 4 HOH 166 766 413 HOH HOH A . 
G 4 HOH 167 767 84  HOH HOH A . 
G 4 HOH 168 768 290 HOH HOH A . 
G 4 HOH 169 769 69  HOH HOH A . 
G 4 HOH 170 770 503 HOH HOH A . 
G 4 HOH 171 771 61  HOH HOH A . 
G 4 HOH 172 772 376 HOH HOH A . 
G 4 HOH 173 773 238 HOH HOH A . 
G 4 HOH 174 774 92  HOH HOH A . 
G 4 HOH 175 775 412 HOH HOH A . 
G 4 HOH 176 776 451 HOH HOH A . 
G 4 HOH 177 777 249 HOH HOH A . 
G 4 HOH 178 778 302 HOH HOH A . 
G 4 HOH 179 779 351 HOH HOH A . 
G 4 HOH 180 780 371 HOH HOH A . 
G 4 HOH 181 781 321 HOH HOH A . 
G 4 HOH 182 782 120 HOH HOH A . 
G 4 HOH 183 783 40  HOH HOH A . 
G 4 HOH 184 784 214 HOH HOH A . 
G 4 HOH 185 785 261 HOH HOH A . 
G 4 HOH 186 786 76  HOH HOH A . 
G 4 HOH 187 787 299 HOH HOH A . 
G 4 HOH 188 788 266 HOH HOH A . 
G 4 HOH 189 789 80  HOH HOH A . 
G 4 HOH 190 790 276 HOH HOH A . 
G 4 HOH 191 791 373 HOH HOH A . 
G 4 HOH 192 792 192 HOH HOH A . 
G 4 HOH 193 793 404 HOH HOH A . 
G 4 HOH 194 794 247 HOH HOH A . 
G 4 HOH 195 795 326 HOH HOH A . 
G 4 HOH 196 796 195 HOH HOH A . 
G 4 HOH 197 797 60  HOH HOH A . 
G 4 HOH 198 798 187 HOH HOH A . 
G 4 HOH 199 799 399 HOH HOH A . 
G 4 HOH 200 800 465 HOH HOH A . 
G 4 HOH 201 801 378 HOH HOH A . 
G 4 HOH 202 802 29  HOH HOH A . 
G 4 HOH 203 803 311 HOH HOH A . 
G 4 HOH 204 804 231 HOH HOH A . 
G 4 HOH 205 805 205 HOH HOH A . 
G 4 HOH 206 806 494 HOH HOH A . 
G 4 HOH 207 807 475 HOH HOH A . 
G 4 HOH 208 808 124 HOH HOH A . 
G 4 HOH 209 809 194 HOH HOH A . 
G 4 HOH 210 810 461 HOH HOH A . 
G 4 HOH 211 811 196 HOH HOH A . 
G 4 HOH 212 812 403 HOH HOH A . 
G 4 HOH 213 813 71  HOH HOH A . 
G 4 HOH 214 814 428 HOH HOH A . 
G 4 HOH 215 815 200 HOH HOH A . 
G 4 HOH 216 816 237 HOH HOH A . 
G 4 HOH 217 817 217 HOH HOH A . 
G 4 HOH 218 818 270 HOH HOH A . 
G 4 HOH 219 819 126 HOH HOH A . 
G 4 HOH 220 820 26  HOH HOH A . 
G 4 HOH 221 821 308 HOH HOH A . 
G 4 HOH 222 822 99  HOH HOH A . 
G 4 HOH 223 823 383 HOH HOH A . 
G 4 HOH 224 824 357 HOH HOH A . 
G 4 HOH 225 825 225 HOH HOH A . 
G 4 HOH 226 826 484 HOH HOH A . 
G 4 HOH 227 827 193 HOH HOH A . 
G 4 HOH 228 828 152 HOH HOH A . 
G 4 HOH 229 829 185 HOH HOH A . 
G 4 HOH 230 830 272 HOH HOH A . 
G 4 HOH 231 831 397 HOH HOH A . 
G 4 HOH 232 832 414 HOH HOH A . 
G 4 HOH 233 833 316 HOH HOH A . 
G 4 HOH 234 834 151 HOH HOH A . 
G 4 HOH 235 835 340 HOH HOH A . 
G 4 HOH 236 836 362 HOH HOH A . 
G 4 HOH 237 837 480 HOH HOH A . 
G 4 HOH 238 838 344 HOH HOH A . 
G 4 HOH 239 839 446 HOH HOH A . 
G 4 HOH 240 840 283 HOH HOH A . 
G 4 HOH 241 841 180 HOH HOH A . 
G 4 HOH 242 842 345 HOH HOH A . 
G 4 HOH 243 843 367 HOH HOH A . 
G 4 HOH 244 844 457 HOH HOH A . 
G 4 HOH 245 845 469 HOH HOH A . 
G 4 HOH 246 846 288 HOH HOH A . 
G 4 HOH 247 847 464 HOH HOH A . 
G 4 HOH 248 848 165 HOH HOH A . 
G 4 HOH 249 849 173 HOH HOH A . 
G 4 HOH 250 850 134 HOH HOH A . 
G 4 HOH 251 851 505 HOH HOH A . 
G 4 HOH 252 852 449 HOH HOH A . 
G 4 HOH 253 853 338 HOH HOH A . 
G 4 HOH 254 854 500 HOH HOH A . 
G 4 HOH 255 855 434 HOH HOH A . 
G 4 HOH 256 856 294 HOH HOH A . 
G 4 HOH 257 857 437 HOH HOH A . 
G 4 HOH 258 858 197 HOH HOH A . 
G 4 HOH 259 859 277 HOH HOH A . 
G 4 HOH 260 860 501 HOH HOH A . 
G 4 HOH 261 861 433 HOH HOH A . 
G 4 HOH 262 862 479 HOH HOH A . 
G 4 HOH 263 863 209 HOH HOH A . 
G 4 HOH 264 864 312 HOH HOH A . 
G 4 HOH 265 865 172 HOH HOH A . 
G 4 HOH 266 866 386 HOH HOH A . 
G 4 HOH 267 867 486 HOH HOH A . 
G 4 HOH 268 868 509 HOH HOH A . 
H 4 HOH 1   601 459 HOH HOH B . 
H 4 HOH 2   602 138 HOH HOH B . 
H 4 HOH 3   603 411 HOH HOH B . 
H 4 HOH 4   604 25  HOH HOH B . 
H 4 HOH 5   605 85  HOH HOH B . 
H 4 HOH 6   606 342 HOH HOH B . 
H 4 HOH 7   607 156 HOH HOH B . 
H 4 HOH 8   608 339 HOH HOH B . 
H 4 HOH 9   609 323 HOH HOH B . 
H 4 HOH 10  610 298 HOH HOH B . 
H 4 HOH 11  611 182 HOH HOH B . 
H 4 HOH 12  612 142 HOH HOH B . 
H 4 HOH 13  613 347 HOH HOH B . 
H 4 HOH 14  614 455 HOH HOH B . 
H 4 HOH 15  615 24  HOH HOH B . 
H 4 HOH 16  616 123 HOH HOH B . 
H 4 HOH 17  617 86  HOH HOH B . 
H 4 HOH 18  618 336 HOH HOH B . 
H 4 HOH 19  619 285 HOH HOH B . 
H 4 HOH 20  620 242 HOH HOH B . 
H 4 HOH 21  621 190 HOH HOH B . 
H 4 HOH 22  622 300 HOH HOH B . 
H 4 HOH 23  623 229 HOH HOH B . 
H 4 HOH 24  624 113 HOH HOH B . 
H 4 HOH 25  625 77  HOH HOH B . 
H 4 HOH 26  626 42  HOH HOH B . 
H 4 HOH 27  627 75  HOH HOH B . 
H 4 HOH 28  628 30  HOH HOH B . 
H 4 HOH 29  629 6   HOH HOH B . 
H 4 HOH 30  630 444 HOH HOH B . 
H 4 HOH 31  631 233 HOH HOH B . 
H 4 HOH 32  632 206 HOH HOH B . 
H 4 HOH 33  633 96  HOH HOH B . 
H 4 HOH 34  634 424 HOH HOH B . 
H 4 HOH 35  635 19  HOH HOH B . 
H 4 HOH 36  636 150 HOH HOH B . 
H 4 HOH 37  637 66  HOH HOH B . 
H 4 HOH 38  638 49  HOH HOH B . 
H 4 HOH 39  639 506 HOH HOH B . 
H 4 HOH 40  640 267 HOH HOH B . 
H 4 HOH 41  641 241 HOH HOH B . 
H 4 HOH 42  642 322 HOH HOH B . 
H 4 HOH 43  643 21  HOH HOH B . 
H 4 HOH 44  644 104 HOH HOH B . 
H 4 HOH 45  645 289 HOH HOH B . 
H 4 HOH 46  646 178 HOH HOH B . 
H 4 HOH 47  647 166 HOH HOH B . 
H 4 HOH 48  648 258 HOH HOH B . 
H 4 HOH 49  649 452 HOH HOH B . 
H 4 HOH 50  650 153 HOH HOH B . 
H 4 HOH 51  651 303 HOH HOH B . 
H 4 HOH 52  652 304 HOH HOH B . 
H 4 HOH 53  653 435 HOH HOH B . 
H 4 HOH 54  654 164 HOH HOH B . 
H 4 HOH 55  655 125 HOH HOH B . 
H 4 HOH 56  656 103 HOH HOH B . 
H 4 HOH 57  657 56  HOH HOH B . 
H 4 HOH 58  658 510 HOH HOH B . 
H 4 HOH 59  659 405 HOH HOH B . 
H 4 HOH 60  660 63  HOH HOH B . 
H 4 HOH 61  661 35  HOH HOH B . 
H 4 HOH 62  662 478 HOH HOH B . 
H 4 HOH 63  663 94  HOH HOH B . 
H 4 HOH 64  664 488 HOH HOH B . 
H 4 HOH 65  665 203 HOH HOH B . 
H 4 HOH 66  666 53  HOH HOH B . 
H 4 HOH 67  667 391 HOH HOH B . 
H 4 HOH 68  668 109 HOH HOH B . 
H 4 HOH 69  669 3   HOH HOH B . 
H 4 HOH 70  670 55  HOH HOH B . 
H 4 HOH 71  671 279 HOH HOH B . 
H 4 HOH 72  672 45  HOH HOH B . 
H 4 HOH 73  673 230 HOH HOH B . 
H 4 HOH 74  674 381 HOH HOH B . 
H 4 HOH 75  675 317 HOH HOH B . 
H 4 HOH 76  676 368 HOH HOH B . 
H 4 HOH 77  677 78  HOH HOH B . 
H 4 HOH 78  678 107 HOH HOH B . 
H 4 HOH 79  679 409 HOH HOH B . 
H 4 HOH 80  680 58  HOH HOH B . 
H 4 HOH 81  681 286 HOH HOH B . 
H 4 HOH 82  682 204 HOH HOH B . 
H 4 HOH 83  683 145 HOH HOH B . 
H 4 HOH 84  684 346 HOH HOH B . 
H 4 HOH 85  685 16  HOH HOH B . 
H 4 HOH 86  686 445 HOH HOH B . 
H 4 HOH 87  687 47  HOH HOH B . 
H 4 HOH 88  688 112 HOH HOH B . 
H 4 HOH 89  689 425 HOH HOH B . 
H 4 HOH 90  690 181 HOH HOH B . 
H 4 HOH 91  691 179 HOH HOH B . 
H 4 HOH 92  692 28  HOH HOH B . 
H 4 HOH 93  693 327 HOH HOH B . 
H 4 HOH 94  694 216 HOH HOH B . 
H 4 HOH 95  695 97  HOH HOH B . 
H 4 HOH 96  696 421 HOH HOH B . 
H 4 HOH 97  697 118 HOH HOH B . 
H 4 HOH 98  698 189 HOH HOH B . 
H 4 HOH 99  699 133 HOH HOH B . 
H 4 HOH 100 700 51  HOH HOH B . 
H 4 HOH 101 701 427 HOH HOH B . 
H 4 HOH 102 702 235 HOH HOH B . 
H 4 HOH 103 703 268 HOH HOH B . 
H 4 HOH 104 704 186 HOH HOH B . 
H 4 HOH 105 705 121 HOH HOH B . 
H 4 HOH 106 706 253 HOH HOH B . 
H 4 HOH 107 707 310 HOH HOH B . 
H 4 HOH 108 708 309 HOH HOH B . 
H 4 HOH 109 709 244 HOH HOH B . 
H 4 HOH 110 710 207 HOH HOH B . 
H 4 HOH 111 711 410 HOH HOH B . 
H 4 HOH 112 712 87  HOH HOH B . 
H 4 HOH 113 713 22  HOH HOH B . 
H 4 HOH 114 714 307 HOH HOH B . 
H 4 HOH 115 715 330 HOH HOH B . 
H 4 HOH 116 716 130 HOH HOH B . 
H 4 HOH 117 717 314 HOH HOH B . 
H 4 HOH 118 718 5   HOH HOH B . 
H 4 HOH 119 719 360 HOH HOH B . 
H 4 HOH 120 720 199 HOH HOH B . 
H 4 HOH 121 721 37  HOH HOH B . 
H 4 HOH 122 722 201 HOH HOH B . 
H 4 HOH 123 723 263 HOH HOH B . 
H 4 HOH 124 724 292 HOH HOH B . 
H 4 HOH 125 725 119 HOH HOH B . 
H 4 HOH 126 726 202 HOH HOH B . 
H 4 HOH 127 727 400 HOH HOH B . 
H 4 HOH 128 728 74  HOH HOH B . 
H 4 HOH 129 729 441 HOH HOH B . 
H 4 HOH 130 730 226 HOH HOH B . 
H 4 HOH 131 731 132 HOH HOH B . 
H 4 HOH 132 732 14  HOH HOH B . 
H 4 HOH 133 733 454 HOH HOH B . 
H 4 HOH 134 734 239 HOH HOH B . 
H 4 HOH 135 735 218 HOH HOH B . 
H 4 HOH 136 736 492 HOH HOH B . 
H 4 HOH 137 737 334 HOH HOH B . 
H 4 HOH 138 738 141 HOH HOH B . 
H 4 HOH 139 739 305 HOH HOH B . 
H 4 HOH 140 740 139 HOH HOH B . 
H 4 HOH 141 741 293 HOH HOH B . 
H 4 HOH 142 742 89  HOH HOH B . 
H 4 HOH 143 743 70  HOH HOH B . 
H 4 HOH 144 744 275 HOH HOH B . 
H 4 HOH 145 745 366 HOH HOH B . 
H 4 HOH 146 746 259 HOH HOH B . 
H 4 HOH 147 747 460 HOH HOH B . 
H 4 HOH 148 748 115 HOH HOH B . 
H 4 HOH 149 749 64  HOH HOH B . 
H 4 HOH 150 750 157 HOH HOH B . 
H 4 HOH 151 751 291 HOH HOH B . 
H 4 HOH 152 752 352 HOH HOH B . 
H 4 HOH 153 753 116 HOH HOH B . 
H 4 HOH 154 754 417 HOH HOH B . 
H 4 HOH 155 755 23  HOH HOH B . 
H 4 HOH 156 756 315 HOH HOH B . 
H 4 HOH 157 757 394 HOH HOH B . 
H 4 HOH 158 758 448 HOH HOH B . 
H 4 HOH 159 759 458 HOH HOH B . 
H 4 HOH 160 760 498 HOH HOH B . 
H 4 HOH 161 761 213 HOH HOH B . 
H 4 HOH 162 762 388 HOH HOH B . 
H 4 HOH 163 763 313 HOH HOH B . 
H 4 HOH 164 764 262 HOH HOH B . 
H 4 HOH 165 765 72  HOH HOH B . 
H 4 HOH 166 766 374 HOH HOH B . 
H 4 HOH 167 767 468 HOH HOH B . 
H 4 HOH 168 768 398 HOH HOH B . 
H 4 HOH 169 769 269 HOH HOH B . 
H 4 HOH 170 770 297 HOH HOH B . 
H 4 HOH 171 771 420 HOH HOH B . 
H 4 HOH 172 772 447 HOH HOH B . 
H 4 HOH 173 773 382 HOH HOH B . 
H 4 HOH 174 774 361 HOH HOH B . 
H 4 HOH 175 775 246 HOH HOH B . 
H 4 HOH 176 776 482 HOH HOH B . 
H 4 HOH 177 777 490 HOH HOH B . 
H 4 HOH 178 778 467 HOH HOH B . 
H 4 HOH 179 779 301 HOH HOH B . 
H 4 HOH 180 780 188 HOH HOH B . 
H 4 HOH 181 781 59  HOH HOH B . 
H 4 HOH 182 782 504 HOH HOH B . 
H 4 HOH 183 783 477 HOH HOH B . 
H 4 HOH 184 784 278 HOH HOH B . 
H 4 HOH 185 785 240 HOH HOH B . 
H 4 HOH 186 786 408 HOH HOH B . 
H 4 HOH 187 787 343 HOH HOH B . 
H 4 HOH 188 788 333 HOH HOH B . 
H 4 HOH 189 789 390 HOH HOH B . 
H 4 HOH 190 790 158 HOH HOH B . 
H 4 HOH 191 791 401 HOH HOH B . 
H 4 HOH 192 792 456 HOH HOH B . 
H 4 HOH 193 793 110 HOH HOH B . 
H 4 HOH 194 794 453 HOH HOH B . 
H 4 HOH 195 795 370 HOH HOH B . 
H 4 HOH 196 796 431 HOH HOH B . 
H 4 HOH 197 797 379 HOH HOH B . 
H 4 HOH 198 798 234 HOH HOH B . 
H 4 HOH 199 799 436 HOH HOH B . 
H 4 HOH 200 800 429 HOH HOH B . 
H 4 HOH 201 801 450 HOH HOH B . 
H 4 HOH 202 802 407 HOH HOH B . 
H 4 HOH 203 803 257 HOH HOH B . 
H 4 HOH 204 804 440 HOH HOH B . 
H 4 HOH 205 805 439 HOH HOH B . 
H 4 HOH 206 806 392 HOH HOH B . 
H 4 HOH 207 807 508 HOH HOH B . 
H 4 HOH 208 808 476 HOH HOH B . 
H 4 HOH 209 809 162 HOH HOH B . 
H 4 HOH 210 810 502 HOH HOH B . 
H 4 HOH 211 811 507 HOH HOH B . 
H 4 HOH 212 812 221 HOH HOH B . 
H 4 HOH 213 813 295 HOH HOH B . 
H 4 HOH 214 814 355 HOH HOH B . 
H 4 HOH 215 815 462 HOH HOH B . 
H 4 HOH 216 816 471 HOH HOH B . 
H 4 HOH 217 817 496 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' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .                  3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? .                  4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   95.80 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9IHT 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     60.931 
_cell.length_a_esd                 ? 
_cell.length_b                     40.109 
_cell.length_b_esd                 ? 
_cell.length_c                     195.144 
_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                         9IHT 
_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                   9IHT 
_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             2.07 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          40.63 
_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    '0.1 M Sodium citrate, pH 4.2, 20% PEG 3350' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            338 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2024-01-23 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.97918 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'SSRF BEAMLINE BL10U2' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97918 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL10U2 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9IHT 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.69 
_reflns.d_resolution_low                               97.07 
_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                                     105855 
_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                                5.2 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          9.2 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               0.88 
_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                                0.124 
_reflns.pdbx_Rpim_I_all                                0.052 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       550396 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.996 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.112 
_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                                    1.69 
_reflns_shell.d_res_low                                     1.78 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           71034 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             15318 
_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                               4.6 
_reflns_shell.pdbx_chi_squared                              0.73 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     1.4 
_reflns_shell.pdbx_Rrim_I_all                               1.768 
_reflns_shell.pdbx_Rpim_I_all                               0.780 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.470 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  1.580 
_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                                 9IHT 
_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                            1.692 
_refine.ls_d_res_low                             60.619 
_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                     105119 
_refine.ls_number_reflns_R_free                  5113 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.29 
_refine.ls_percent_reflns_R_free                 4.86 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1723 
_refine.ls_R_factor_R_free                       0.2002 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1709 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.35 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.11 
_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                 18.96 
_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                            0.20 
_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                       1.692 
_refine_hist.d_res_low                        60.619 
_refine_hist.number_atoms_solvent             485 
_refine_hist.number_atoms_total               8673 
_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        8188 
_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 ? 8469  ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.950 ? 11465 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 5.862 ? 7082  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.056 ? 1209  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.006 ? 1436  ? 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' 1.692  1.7109 . . 155 2962 90.00  . . . . 0.3020 . . . . . . . . . . . 0.3379 
'X-RAY DIFFRACTION' 1.7109 1.7311 . . 159 3185 94.00  . . . . 0.2958 . . . . . . . . . . . 0.3214 
'X-RAY DIFFRACTION' 1.7311 1.7522 . . 168 3199 97.00  . . . . 0.2758 . . . . . . . . . . . 0.2983 
'X-RAY DIFFRACTION' 1.7522 1.7743 . . 177 3263 99.00  . . . . 0.2740 . . . . . . . . . . . 0.3117 
'X-RAY DIFFRACTION' 1.7743 1.7977 . . 183 3316 100.00 . . . . 0.2646 . . . . . . . . . . . 0.3018 
'X-RAY DIFFRACTION' 1.7977 1.8223 . . 184 3369 100.00 . . . . 0.2338 . . . . . . . . . . . 0.2700 
'X-RAY DIFFRACTION' 1.8223 1.8484 . . 163 3269 100.00 . . . . 0.2243 . . . . . . . . . . . 0.3029 
'X-RAY DIFFRACTION' 1.8484 1.8760 . . 184 3309 100.00 . . . . 0.2105 . . . . . . . . . . . 0.2586 
'X-RAY DIFFRACTION' 1.8760 1.9053 . . 172 3383 100.00 . . . . 0.1962 . . . . . . . . . . . 0.2465 
'X-RAY DIFFRACTION' 1.9053 1.9365 . . 162 3273 100.00 . . . . 0.1952 . . . . . . . . . . . 0.2228 
'X-RAY DIFFRACTION' 1.9365 1.9699 . . 179 3378 100.00 . . . . 0.1862 . . . . . . . . . . . 0.2391 
'X-RAY DIFFRACTION' 1.9699 2.0057 . . 180 3309 100.00 . . . . 0.1818 . . . . . . . . . . . 0.2088 
'X-RAY DIFFRACTION' 2.0057 2.0443 . . 181 3292 100.00 . . . . 0.1740 . . . . . . . . . . . 0.1927 
'X-RAY DIFFRACTION' 2.0443 2.0860 . . 161 3374 100.00 . . . . 0.1807 . . . . . . . . . . . 0.2204 
'X-RAY DIFFRACTION' 2.0860 2.1314 . . 172 3309 100.00 . . . . 0.1632 . . . . . . . . . . . 0.1998 
'X-RAY DIFFRACTION' 2.1314 2.1810 . . 181 3342 100.00 . . . . 0.1608 . . . . . . . . . . . 0.1882 
'X-RAY DIFFRACTION' 2.1810 2.2355 . . 173 3362 100.00 . . . . 0.1575 . . . . . . . . . . . 0.1883 
'X-RAY DIFFRACTION' 2.2355 2.2960 . . 177 3320 100.00 . . . . 0.1572 . . . . . . . . . . . 0.1916 
'X-RAY DIFFRACTION' 2.2960 2.3635 . . 183 3381 100.00 . . . . 0.1626 . . . . . . . . . . . 0.2055 
'X-RAY DIFFRACTION' 2.3635 2.4398 . . 153 3338 100.00 . . . . 0.1675 . . . . . . . . . . . 0.1812 
'X-RAY DIFFRACTION' 2.4398 2.5270 . . 173 3382 100.00 . . . . 0.1608 . . . . . . . . . . . 0.1981 
'X-RAY DIFFRACTION' 2.5270 2.6282 . . 171 3326 100.00 . . . . 0.1593 . . . . . . . . . . . 0.2125 
'X-RAY DIFFRACTION' 2.6282 2.7478 . . 149 3362 100.00 . . . . 0.1599 . . . . . . . . . . . 0.1957 
'X-RAY DIFFRACTION' 2.7478 2.8927 . . 146 3443 100.00 . . . . 0.1596 . . . . . . . . . . . 0.1965 
'X-RAY DIFFRACTION' 2.8927 3.0739 . . 173 3372 100.00 . . . . 0.1562 . . . . . . . . . . . 0.2039 
'X-RAY DIFFRACTION' 3.0739 3.3112 . . 184 3362 100.00 . . . . 0.1542 . . . . . . . . . . . 0.1798 
'X-RAY DIFFRACTION' 3.3112 3.6444 . . 158 3440 100.00 . . . . 0.1462 . . . . . . . . . . . 0.1726 
'X-RAY DIFFRACTION' 3.6444 4.1717 . . 182 3352 100.00 . . . . 0.1356 . . . . . . . . . . . 0.1595 
'X-RAY DIFFRACTION' 4.1717 5.2554 . . 186 3441 100.00 . . . . 0.1463 . . . . . . . . . . . 0.1525 
'X-RAY DIFFRACTION' 5.2554 60.619 . . 144 3593 99.00  . . . . 0.1795 . . . . . . . . . . . 0.1768 
# 
_struct.entry_id                     9IHT 
_struct.title                        
'Crystal structure of GH57 family amylopullulanase from Aquifex aeolicus in complex with acarbose' 
_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        9IHT 
_struct_keywords.text            'GH57 family, amylopullulanase, Aquifex aeolicus, complex, 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 ? 
E N N 3 ? 
F N N 3 ? 
G N N 4 ? 
H N N 4 ? 
# 
_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 9IHT A 1 ? 477 ? O66934 1 ? 477 ? 1 477 
2 1 9IHT 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,E,G 
2 1 B,D,F,H 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 PRO A 28  ? ASP A 37  ? PRO A 28  ASP A 37  1 ? 10 
HELX_P HELX_P2  AA2 TYR A 39  ? TYR A 44  ? TYR A 39  TYR A 44  1 ? 6  
HELX_P HELX_P3  AA3 LEU A 45  ? ASP A 47  ? LEU A 45  ASP A 47  5 ? 3  
HELX_P HELX_P4  AA4 THR A 57  ? GLN A 69  ? THR A 57  GLN A 69  1 ? 13 
HELX_P HELX_P5  AA5 VAL A 75  ? LYS A 82  ? VAL A 75  LYS A 82  1 ? 8  
HELX_P HELX_P6  AA6 ASP A 83  ? LEU A 87  ? ASP A 83  LEU A 87  5 ? 5  
HELX_P HELX_P7  AA7 GLU A 88  ? TYR A 103 ? GLU A 88  TYR A 103 1 ? 16 
HELX_P HELX_P8  AA8 LYS A 105 ? ARG A 109 ? LYS A 105 ARG A 109 5 ? 5  
HELX_P HELX_P9  AA9 PHE A 110 ? LYS A 119 ? PHE A 110 LYS A 119 1 ? 10 
HELX_P HELX_P10 AB1 ASN A 123 ? TRP A 138 ? ASN A 123 TRP A 138 1 ? 16 
HELX_P HELX_P11 AB2 GLY A 140 ? LEU A 147 ? GLY A 140 LEU A 147 1 ? 8  
HELX_P HELX_P12 AB3 LEU A 147 ? GLY A 154 ? LEU A 147 GLY A 154 1 ? 8  
HELX_P HELX_P13 AB4 THR A 158 ? LYS A 175 ? THR A 158 LYS A 175 1 ? 18 
HELX_P HELX_P14 AB5 LYS A 175 ? GLU A 186 ? LYS A 175 GLU A 186 1 ? 12 
HELX_P HELX_P15 AB6 LEU A 200 ? ASN A 206 ? LEU A 200 ASN A 206 1 ? 7  
HELX_P HELX_P16 AB7 PRO A 207 ? THR A 213 ? PRO A 207 THR A 213 5 ? 7  
HELX_P HELX_P17 AB8 PHE A 226 ? GLY A 246 ? PHE A 226 GLY A 246 1 ? 21 
HELX_P HELX_P18 AB9 PRO A 254 ? SER A 258 ? PRO A 254 SER A 258 5 ? 5  
HELX_P HELX_P19 AC1 SER A 260 ? LYS A 270 ? SER A 260 LYS A 270 1 ? 11 
HELX_P HELX_P20 AC2 ASP A 278 ? VAL A 286 ? ASP A 278 VAL A 286 1 ? 9  
HELX_P HELX_P21 AC3 ASP A 307 ? SER A 317 ? ASP A 307 SER A 317 1 ? 11 
HELX_P HELX_P22 AC4 TYR A 318 ? TRP A 321 ? TYR A 318 TRP A 321 5 ? 4  
HELX_P HELX_P23 AC5 ASN A 322 ? VAL A 341 ? ASN A 322 VAL A 341 1 ? 20 
HELX_P HELX_P24 AC6 CYS A 356 ? ASN A 363 ? CYS A 356 ASN A 363 5 ? 8  
HELX_P HELX_P25 AC7 GLY A 364 ? GLU A 378 ? GLY A 364 GLU A 378 1 ? 15 
HELX_P HELX_P26 AC8 THR A 385 ? LYS A 392 ? THR A 385 LYS A 392 1 ? 8  
HELX_P HELX_P27 AC9 ASN A 419 ? LYS A 435 ? ASN A 419 LYS A 435 1 ? 17 
HELX_P HELX_P28 AD1 ASP A 439 ? GLU A 445 ? ASP A 439 GLU A 445 1 ? 7  
HELX_P HELX_P29 AD2 GLY A 446 ? GLN A 453 ? GLY A 446 GLN A 453 1 ? 8  
HELX_P HELX_P30 AD3 PHE A 460 ? GLN A 476 ? PHE A 460 GLN A 476 1 ? 17 
HELX_P HELX_P31 AD4 PRO B 28  ? ASP B 37  ? PRO B 28  ASP B 37  1 ? 10 
HELX_P HELX_P32 AD5 TYR B 39  ? TYR B 44  ? TYR B 39  TYR B 44  1 ? 6  
HELX_P HELX_P33 AD6 LEU B 45  ? ASP B 47  ? LEU B 45  ASP B 47  5 ? 3  
HELX_P HELX_P34 AD7 THR B 57  ? GLN B 69  ? THR B 57  GLN B 69  1 ? 13 
HELX_P HELX_P35 AD8 VAL B 75  ? LYS B 82  ? VAL B 75  LYS B 82  1 ? 8  
HELX_P HELX_P36 AD9 ASP B 83  ? LEU B 87  ? ASP B 83  LEU B 87  5 ? 5  
HELX_P HELX_P37 AE1 GLU B 88  ? TYR B 103 ? GLU B 88  TYR B 103 1 ? 16 
HELX_P HELX_P38 AE2 LYS B 105 ? ARG B 109 ? LYS B 105 ARG B 109 5 ? 5  
HELX_P HELX_P39 AE3 PHE B 110 ? ASN B 118 ? PHE B 110 ASN B 118 1 ? 9  
HELX_P HELX_P40 AE4 ASN B 123 ? TRP B 138 ? ASN B 123 TRP B 138 1 ? 16 
HELX_P HELX_P41 AE5 GLY B 140 ? LEU B 147 ? GLY B 140 LEU B 147 1 ? 8  
HELX_P HELX_P42 AE6 LEU B 147 ? GLY B 154 ? LEU B 147 GLY B 154 1 ? 8  
HELX_P HELX_P43 AE7 THR B 158 ? LYS B 175 ? THR B 158 LYS B 175 1 ? 18 
HELX_P HELX_P44 AE8 LYS B 175 ? GLU B 186 ? LYS B 175 GLU B 186 1 ? 12 
HELX_P HELX_P45 AE9 LEU B 200 ? ASN B 206 ? LEU B 200 ASN B 206 1 ? 7  
HELX_P HELX_P46 AF1 PRO B 207 ? THR B 213 ? PRO B 207 THR B 213 5 ? 7  
HELX_P HELX_P47 AF2 PHE B 226 ? GLY B 246 ? PHE B 226 GLY B 246 1 ? 21 
HELX_P HELX_P48 AF3 PRO B 254 ? SER B 258 ? PRO B 254 SER B 258 5 ? 5  
HELX_P HELX_P49 AF4 SER B 260 ? LYS B 270 ? SER B 260 LYS B 270 1 ? 11 
HELX_P HELX_P50 AF5 ASP B 278 ? VAL B 286 ? ASP B 278 VAL B 286 1 ? 9  
HELX_P HELX_P51 AF6 ASP B 307 ? SER B 317 ? ASP B 307 SER B 317 1 ? 11 
HELX_P HELX_P52 AF7 TYR B 318 ? TRP B 321 ? TYR B 318 TRP B 321 5 ? 4  
HELX_P HELX_P53 AF8 ASN B 322 ? VAL B 341 ? ASN B 322 VAL B 341 1 ? 20 
HELX_P HELX_P54 AF9 CYS B 356 ? ASN B 363 ? CYS B 356 ASN B 363 5 ? 8  
HELX_P HELX_P55 AG1 GLY B 364 ? LYS B 377 ? GLY B 364 LYS B 377 1 ? 14 
HELX_P HELX_P56 AG2 THR B 385 ? LYS B 392 ? THR B 385 LYS B 392 1 ? 8  
HELX_P HELX_P57 AG3 ASN B 419 ? LYS B 434 ? ASN B 419 LYS B 434 1 ? 16 
HELX_P HELX_P58 AG4 ASP B 439 ? GLU B 445 ? ASP B 439 GLU B 445 1 ? 7  
HELX_P HELX_P59 AG5 GLY B 446 ? GLN B 453 ? GLY B 446 GLN B 453 1 ? 8  
HELX_P HELX_P60 AG6 PHE B 460 ? GLN B 476 ? PHE B 460 GLN B 476 1 ? 17 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
covale1 covale both ? C GLC . O4 ? ? ? 1_555 C GLC . C1 ? ? C GLC 1 C GLC 2 1_555 ? ? ? ? ? ? ? 1.425 ? ? 
covale2 covale both ? C GLC . O4 ? ? ? 1_555 C AC1 . C1 ? ? C GLC 2 C AC1 3 1_555 ? ? ? ? ? ? ? 1.375 ? ? 
covale3 covale both ? D GLC . O4 ? ? ? 1_555 D GLC . C1 ? ? D GLC 1 D GLC 2 1_555 ? ? ? ? ? ? ? 1.428 ? ? 
covale4 covale both ? D GLC . O4 ? ? ? 1_555 D AC1 . C1 ? ? D GLC 2 D AC1 3 1_555 ? ? ? ? ? ? ? 1.376 ? ? 
# 
_struct_conn_type.id          covale 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 4 ? 
AA3 ? 2 ? 
AA4 ? 5 ? 
AA5 ? 4 ? 
AA6 ? 4 ? 
AA7 ? 2 ? 
AA8 ? 5 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? parallel      
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA2 1 2 ? parallel      
AA2 2 3 ? parallel      
AA2 3 4 ? parallel      
AA3 1 2 ? parallel      
AA4 1 2 ? parallel      
AA4 2 3 ? parallel      
AA4 3 4 ? anti-parallel 
AA4 4 5 ? parallel      
AA5 1 2 ? parallel      
AA5 2 3 ? parallel      
AA5 3 4 ? parallel      
AA6 1 2 ? parallel      
AA6 2 3 ? parallel      
AA6 3 4 ? parallel      
AA7 1 2 ? parallel      
AA8 1 2 ? parallel      
AA8 2 3 ? parallel      
AA8 3 4 ? anti-parallel 
AA8 4 5 ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 VAL A 191 ? SER A 192 ? VAL A 191 SER A 192 
AA1 2 ASN A 53  ? LEU A 56  ? ASN A 53  LEU A 56  
AA1 3 LEU A 4   ? MET A 12  ? LEU A 4   MET A 12  
AA1 4 VAL A 346 ? ASP A 352 ? VAL A 346 ASP A 352 
AA2 1 VAL A 191 ? SER A 192 ? VAL A 191 SER A 192 
AA2 2 ASN A 53  ? LEU A 56  ? ASN A 53  LEU A 56  
AA2 3 LEU A 4   ? MET A 12  ? LEU A 4   MET A 12  
AA2 4 ILE A 381 ? THR A 383 ? ILE A 381 THR A 383 
AA3 1 GLU A 24  ? TYR A 25  ? GLU A 24  TYR A 25  
AA3 2 LYS A 73  ? ASP A 74  ? LYS A 73  ASP A 74  
AA4 1 TYR A 251 ? MET A 252 ? TYR A 251 MET A 252 
AA4 2 MET A 274 ? THR A 277 ? MET A 274 THR A 277 
AA4 3 ILE A 301 ? PHE A 305 ? ILE A 301 PHE A 305 
AA4 4 ARG A 294 ? PHE A 297 ? ARG A 294 PHE A 297 
AA4 5 THR A 397 ? ILE A 400 ? THR A 397 ILE A 400 
AA5 1 VAL B 191 ? SER B 192 ? VAL B 191 SER B 192 
AA5 2 ASN B 53  ? LEU B 56  ? ASN B 53  LEU B 56  
AA5 3 LEU B 4   ? MET B 12  ? LEU B 4   MET B 12  
AA5 4 VAL B 346 ? 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 ? THR B 277 ? MET B 274 THR B 277 
AA8 3 ILE B 301 ? PHE B 305 ? ILE B 301 PHE B 305 
AA8 4 ARG B 294 ? PHE B 297 ? ARG B 294 PHE B 297 
AA8 5 THR B 397 ? ILE B 400 ? THR B 397 ILE B 400 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O SER A 192 ? O SER A 192 N PHE A 54  ? N PHE A 54  
AA1 2 3 O ASN A 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 PHE A 304 ? O PHE A 304 
AA4 3 4 O VAL A 303 ? O VAL A 303 N TYR A 295 ? N TYR A 295 
AA4 4 5 N TYR A 296 ? N TYR A 296 O ILE A 400 ? O ILE A 400 
AA5 1 2 O SER B 192 ? O SER B 192 N PHE B 54  ? N PHE B 54  
AA5 2 3 O ASN B 53  ? O ASN B 53  N TRP B 10  ? N TRP B 10  
AA5 3 4 N PHE B 5   ? N PHE B 5   O VAL B 347 ? O VAL B 347 
AA6 1 2 O SER B 192 ? O SER B 192 N PHE B 54  ? N PHE B 54  
AA6 2 3 O ASN B 53  ? O ASN B 53  N TRP B 10  ? N TRP B 10  
AA6 3 4 N LEU B 4   ? N LEU B 4   O GLU B 382 ? O GLU B 382 
AA7 1 2 N TYR B 25  ? N TYR B 25  O LYS B 73  ? O LYS B 73  
AA8 1 2 N MET B 252 ? N MET B 252 O MET B 274 ? O MET B 274 
AA8 2 3 N THR B 277 ? N THR B 277 O PHE B 304 ? O PHE B 304 
AA8 3 4 O ILE B 301 ? O ILE B 301 N PHE B 297 ? N PHE B 297 
AA8 4 5 N TYR B 296 ? N TYR B 296 O GLU B 398 ? O GLU B 398 
# 
_pdbx_entry_details.entry_id                   9IHT 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 OE2 B GLU 88  ? ? O B HOH 601 ? ? 2.06 
2 1 O   B HOH 765 ? ? O B HOH 789 ? ? 2.09 
3 1 O   A HOH 841 ? ? O A HOH 858 ? ? 2.09 
4 1 OE1 A GLU 97  ? ? O A HOH 601 ? ? 2.13 
5 1 O   B HOH 770 ? ? O B HOH 788 ? ? 2.16 
6 1 O   B HOH 745 ? ? O B HOH 792 ? ? 2.18 
7 1 NZ  B LYS 427 ? ? O B HOH 602 ? ? 2.18 
8 1 NH1 A ARG 328 ? ? O B GLU 376 ? ? 2.19 
9 1 O   B HOH 727 ? ? O B HOH 775 ? ? 2.19 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    O 
_pdbx_validate_symm_contact.auth_asym_id_1    A 
_pdbx_validate_symm_contact.auth_comp_id_1    HOH 
_pdbx_validate_symm_contact.auth_seq_id_1     617 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    O 
_pdbx_validate_symm_contact.auth_asym_id_2    A 
_pdbx_validate_symm_contact.auth_comp_id_2    HOH 
_pdbx_validate_symm_contact.auth_seq_id_2     849 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   1_455 
_pdbx_validate_symm_contact.dist              2.13 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 GLU A 299 ? ? 57.89   19.78 
2 1 ASP A 394 ? ? -94.78  50.38 
3 1 LYS A 457 ? ? 49.07   18.30 
4 1 ASN B 206 ? ? -160.38 94.75 
5 1 ALA B 458 ? ? -158.20 85.98 
# 
loop_
_pdbx_validate_peptide_omega.id 
_pdbx_validate_peptide_omega.PDB_model_num 
_pdbx_validate_peptide_omega.auth_comp_id_1 
_pdbx_validate_peptide_omega.auth_asym_id_1 
_pdbx_validate_peptide_omega.auth_seq_id_1 
_pdbx_validate_peptide_omega.PDB_ins_code_1 
_pdbx_validate_peptide_omega.label_alt_id_1 
_pdbx_validate_peptide_omega.auth_comp_id_2 
_pdbx_validate_peptide_omega.auth_asym_id_2 
_pdbx_validate_peptide_omega.auth_seq_id_2 
_pdbx_validate_peptide_omega.PDB_ins_code_2 
_pdbx_validate_peptide_omega.label_alt_id_2 
_pdbx_validate_peptide_omega.omega 
1 1 PRO A 195 ? ? TYR A 196 ? ? -147.54 
2 1 PRO B 195 ? ? TYR B 196 ? ? -147.49 
# 
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 -23.3010 35.4584 45.0041 0.2187 ? -0.0948 ? -0.0469 ? 0.1705 ? 0.0108  ? 0.1347 ? 1.3651 ? 0.1273 
? -0.5371 ? 0.6219 ? 0.2408  ? 1.9946 ? 0.3244  ? -0.4654 ? -0.0854 ? 0.3390  ? -0.2113 ? -0.1367 ? -0.0107 ? 0.2003  ? -0.1417 ? 
2  'X-RAY DIFFRACTION' ? refined -48.7254 35.3819 24.1990 0.0894 ? -0.0120 ? 0.0183  ? 0.2674 ? 0.0308  ? 0.1902 ? 1.5012 ? 0.0987 
? 0.2398  ? 1.3643 ? 0.0284  ? 2.4399 ? 0.1030  ? 0.3210  ? 0.2868  ? -0.1040 ? -0.1179 ? 0.2440  ? -0.0740 ? -0.5218 ? 0.0623  ? 
3  'X-RAY DIFFRACTION' ? refined -40.4591 30.3946 12.7615 0.1252 ? -0.0016 ? -0.0284 ? 0.2829 ? -0.0090 ? 0.1204 ? 3.3212 ? 0.6459 
? -0.0749 ? 2.6512 ? -0.0458 ? 3.5261 ? -0.0679 ? 0.5516  ? 0.0288  ? -0.2849 ? 0.0604  ? 0.2160  ? 0.0637  ? -0.0961 ? -0.0420 ? 
4  'X-RAY DIFFRACTION' ? refined -10.0630 11.9820 69.0881 0.0882 ? -0.0432 ? -0.0076 ? 0.0843 ? 0.0156  ? 0.0967 ? 1.0140 ? 0.1581 
? -0.1398 ? 0.5319 ? 0.1543  ? 0.8155 ? -0.0793 ? 0.0210  ? -0.0495 ? -0.1031 ? 0.0849  ? 0.0745  ? 0.0193  ? 0.0038  ? 0.0133  ? 
5  'X-RAY DIFFRACTION' ? refined -17.1597 9.7033  85.4903 0.1344 ? -0.0035 ? 0.0004  ? 0.1717 ? 0.0231  ? 0.1280 ? 2.0481 ? 
-1.1855 ? -1.8388 ? 1.0409 ? 1.2855  ? 1.9412 ? -0.1769 ? -0.2206 ? -0.1925 ? 0.1334  ? 0.0276  ? 0.1433  ? 0.2014  ? -0.1297 ? 
0.0707  ? 
6  'X-RAY DIFFRACTION' ? refined -24.1460 19.6894 79.0240 0.0809 ? -0.0087 ? -0.0213 ? 0.1264 ? 0.0197  ? 0.1413 ? 1.4197 ? 
-0.1999 ? -1.0917 ? 0.9661 ? 0.4369  ? 1.7918 ? 0.0569  ? -0.0005 ? 0.1599  ? 0.0315  ? -0.0271 ? 0.1166  ? -0.1222 ? -0.1556 ? 
-0.0049 ? 
7  'X-RAY DIFFRACTION' ? refined 4.4241   14.3524 63.1760 0.1543 ? -0.0748 ? 0.0167  ? 0.1100 ? -0.0110 ? 0.1103 ? 0.9650 ? 0.0356 
? 0.2287  ? 0.6010 ? -0.1701 ? 0.8791 ? -0.1157 ? 0.1370  ? -0.0353 ? -0.1708 ? 0.1083  ? -0.0533 ? 0.0039  ? 0.1043  ? 0.0155  ? 
8  'X-RAY DIFFRACTION' ? refined -9.5837  15.4972 51.6688 0.2166 ? -0.1051 ? -0.0550 ? 0.1661 ? 0.0192  ? 0.1223 ? 1.5976 ? 
-0.1113 ? -0.3509 ? 0.8837 ? -0.1347 ? 2.0702 ? -0.0468 ? 0.3103  ? 0.0035  ? -0.3024 ? 0.1017  ? -0.0404 ? -0.0412 ? -0.0646 ? 
-0.0460 ? 
9  'X-RAY DIFFRACTION' ? refined 12.3285  17.6697 76.2499 0.0631 ? -0.0367 ? -0.0041 ? 0.1324 ? -0.0027 ? 0.1372 ? 1.4234 ? 0.0463 
? 0.0784  ? 1.1958 ? -0.0605 ? 2.3121 ? -0.1161 ? -0.0754 ? 0.1107  ? -0.0275 ? 0.0482  ? -0.0764 ? -0.2216 ? 0.1221  ? 0.0177  ? 
10 'X-RAY DIFFRACTION' ? refined 2.1938   13.8947 86.7640 0.0458 ? -0.0005 ? -0.0156 ? 0.1735 ? -0.0040 ? 0.0860 ? 3.6702 ? 
-0.2600 ? -0.1734 ? 2.4506 ? -0.0913 ? 3.3065 ? -0.1256 ? -0.2917 ? 0.1343  ? 0.0703  ? 0.0363  ? -0.0097 ? -0.0981 ? -0.1177 ? 
0.0592  ? 
11 'X-RAY DIFFRACTION' ? refined -25.3728 30.2412 28.0727 0.1016 ? 0.0100  ? -0.0141 ? 0.0645 ? -0.0171 ? 0.1107 ? 1.5439 ? 0.4165 
? -0.2726 ? 0.9493 ? 0.0211  ? 1.0304 ? 0.0795  ? 0.0927  ? -0.1780 ? 0.0536  ? -0.0684 ? -0.0887 ? 0.2216  ? 0.0153  ? -0.0323 ? 
12 'X-RAY DIFFRACTION' ? refined -21.1486 26.2903 10.9217 0.1933 ? 0.0187  ? -0.0043 ? 0.3386 ? -0.1049 ? 0.1850 ? 1.3056 ? 0.4448 
? -1.4991 ? 0.4045 ? -0.9493 ? 2.5568 ? -0.1503 ? 0.6672  ? -0.4047 ? -0.2270 ? -0.0650 ? -0.1060 ? 0.5094  ? 0.0749  ? 0.0478  ? 
13 'X-RAY DIFFRACTION' ? refined -12.4254 41.2836 12.1046 0.1408 ? 0.0075  ? 0.0207  ? 0.2719 ? 0.0212  ? 0.1706 ? 1.6410 ? 0.0452 
? -0.6445 ? 1.2034 ? 0.4684  ? 3.0417 ? 0.0704  ? 0.4448  ? 0.1828  ? -0.1432 ? -0.0327 ? -0.0953 ? -0.3488 ? 0.2820  ? -0.1185 ? 
14 'X-RAY DIFFRACTION' ? refined -32.9162 28.1413 25.0988 0.1686 ? -0.0071 ? -0.0315 ? 0.0562 ? -0.0434 ? 0.1448 ? 1.2973 ? 0.3870 
? -0.2801 ? 0.6763 ? -0.1368 ? 1.4441 ? -0.0003 ? 0.1740  ? -0.2536 ? 0.0525  ? 0.0312  ? 0.0014  ? 0.2293  ? -0.1054 ? -0.0226 ? 
15 'X-RAY DIFFRACTION' ? refined -41.3224 22.5523 33.7412 0.2289 ? -0.0746 ? 0.0072  ? 0.1147 ? -0.0126 ? 0.2303 ? 1.5149 ? 
-0.3352 ? -0.3541 ? 1.4868 ? 0.0716  ? 1.6857 ? 0.0047  ? 0.0582  ? -0.4598 ? 0.1973  ? -0.0260 ? -0.1579 ? 0.4684  ? -0.2577 ? 
-0.0170 ? 
16 'X-RAY DIFFRACTION' ? refined -38.5356 39.9957 41.4160 0.2192 ? -0.0343 ? 0.0858  ? 0.0987 ? -0.0501 ? 0.2292 ? 1.6253 ? 1.3687 
? 0.1415  ? 1.6303 ? -0.5228 ? 1.0433 ? 0.1644  ? -0.2812 ? 0.3006  ? 0.1243  ? -0.1324 ? 0.0962  ? -0.1323 ? -0.2196 ? -0.0704 ? 
17 'X-RAY DIFFRACTION' ? refined -27.2112 43.2824 42.0946 0.3038 ? -0.1269 ? 0.0720  ? 0.1463 ? -0.1097 ? 0.1937 ? 1.0746 ? 0.4135 
? -0.4377 ? 0.9451 ? -0.1055 ? 1.0341 ? 0.4285  ? -0.3514 ? 0.4508  ? 0.3802  ? -0.2601 ? 0.0473  ? -0.3621 ? 0.0870  ? -0.1086 ? 
# 
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 'B' and (resid 361 through 396 )
;
2  'X-RAY DIFFRACTION' 2  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 397 through 435 )
;
3  'X-RAY DIFFRACTION' 3  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 436 through 477 )
;
4  'X-RAY DIFFRACTION' 4  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 2 through 57 )
;
5  'X-RAY DIFFRACTION' 5  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 58 through 88 )
;
6  'X-RAY DIFFRACTION' 6  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 89 through 185 )
;
7  'X-RAY DIFFRACTION' 7  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 186 through 360 )
;
8  'X-RAY DIFFRACTION' 8  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 361 through 396 )
;
9  'X-RAY DIFFRACTION' 9  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 397 through 435 )
;
10 'X-RAY DIFFRACTION' 10 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 436 through 477 )
;
11 'X-RAY DIFFRACTION' 11 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 2 through 57 )
;
12 'X-RAY DIFFRACTION' 12 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 58 through 88 )
;
13 'X-RAY DIFFRACTION' 13 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 89 through 158 )
;
14 'X-RAY DIFFRACTION' 14 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 159 through 226 )
;
15 'X-RAY DIFFRACTION' 15 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 227 through 278 )
;
16 'X-RAY DIFFRACTION' 16 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 279 through 322 )
;
17 'X-RAY DIFFRACTION' 17 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 323 through 360 )
;
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A MET 1 ? A MET 1 
2 1 Y 1 B MET 1 ? B MET 1 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
AC1 C1   C N S 1   
AC1 O2   O N N 2   
AC1 C2   C N R 3   
AC1 C4A  C N R 4   
AC1 C3   C N S 5   
AC1 O3   O N N 6   
AC1 C4   C N S 7   
AC1 N4A  N N N 8   
AC1 C5   C N R 9   
AC1 O5   O N N 10  
AC1 C6   C N N 11  
AC1 C1B  C N S 12  
AC1 C2B  C N S 13  
AC1 O2B  O N N 14  
AC1 C3B  C N S 15  
AC1 O3B  O N N 16  
AC1 O4   O N N 17  
AC1 C5B  C N N 18  
AC1 C7B  C N N 19  
AC1 C6B  C N N 20  
AC1 O6B  O N N 21  
AC1 O1   O N N 22  
AC1 H1   H N N 23  
AC1 HO2  H N N 24  
AC1 H2   H N N 25  
AC1 HC4  H N N 26  
AC1 H3   H N N 27  
AC1 HO3  H N N 28  
AC1 H4   H N N 29  
AC1 HN4  H N N 30  
AC1 H5   H N N 31  
AC1 H61  H N N 32  
AC1 H62  H N N 33  
AC1 H63  H N N 34  
AC1 HCB1 H N N 35  
AC1 HCB2 H N N 36  
AC1 HO2B H N N 37  
AC1 HCB3 H N N 38  
AC1 HOB3 H N N 39  
AC1 HO4  H N N 40  
AC1 HC7  H N N 41  
AC1 HC61 H N N 42  
AC1 HC62 H N N 43  
AC1 HO6B H N N 44  
AC1 HO1  H N N 45  
ALA N    N N N 46  
ALA CA   C N S 47  
ALA C    C N N 48  
ALA O    O N N 49  
ALA CB   C N N 50  
ALA OXT  O N N 51  
ALA H    H N N 52  
ALA H2   H N N 53  
ALA HA   H N N 54  
ALA HB1  H N N 55  
ALA HB2  H N N 56  
ALA HB3  H N N 57  
ALA HXT  H N N 58  
ARG N    N N N 59  
ARG CA   C N S 60  
ARG C    C N N 61  
ARG O    O N N 62  
ARG CB   C N N 63  
ARG CG   C N N 64  
ARG CD   C N N 65  
ARG NE   N N N 66  
ARG CZ   C N N 67  
ARG NH1  N N N 68  
ARG NH2  N N N 69  
ARG OXT  O N N 70  
ARG H    H N N 71  
ARG H2   H N N 72  
ARG HA   H N N 73  
ARG HB2  H N N 74  
ARG HB3  H N N 75  
ARG HG2  H N N 76  
ARG HG3  H N N 77  
ARG HD2  H N N 78  
ARG HD3  H N N 79  
ARG HE   H N N 80  
ARG HH11 H N N 81  
ARG HH12 H N N 82  
ARG HH21 H N N 83  
ARG HH22 H N N 84  
ARG HXT  H N N 85  
ASN N    N N N 86  
ASN CA   C N S 87  
ASN C    C N N 88  
ASN O    O N N 89  
ASN CB   C N N 90  
ASN CG   C N N 91  
ASN OD1  O N N 92  
ASN ND2  N N N 93  
ASN OXT  O N N 94  
ASN H    H N N 95  
ASN H2   H N N 96  
ASN HA   H N N 97  
ASN HB2  H N N 98  
ASN HB3  H N N 99  
ASN HD21 H N N 100 
ASN HD22 H N N 101 
ASN HXT  H N N 102 
ASP N    N N N 103 
ASP CA   C N S 104 
ASP C    C N N 105 
ASP O    O N N 106 
ASP CB   C N N 107 
ASP CG   C N N 108 
ASP OD1  O N N 109 
ASP OD2  O N N 110 
ASP OXT  O N N 111 
ASP H    H N N 112 
ASP H2   H N N 113 
ASP HA   H N N 114 
ASP HB2  H N N 115 
ASP HB3  H N N 116 
ASP HD2  H N N 117 
ASP HXT  H N N 118 
CYS N    N N N 119 
CYS CA   C N R 120 
CYS C    C N N 121 
CYS O    O N N 122 
CYS CB   C N N 123 
CYS SG   S N N 124 
CYS OXT  O N N 125 
CYS H    H N N 126 
CYS H2   H N N 127 
CYS HA   H N N 128 
CYS HB2  H N N 129 
CYS HB3  H N N 130 
CYS HG   H N N 131 
CYS HXT  H N N 132 
GLC C1   C N S 133 
GLC C2   C N R 134 
GLC C3   C N S 135 
GLC C4   C N S 136 
GLC C5   C N R 137 
GLC C6   C N N 138 
GLC O1   O N N 139 
GLC O2   O N N 140 
GLC O3   O N N 141 
GLC O4   O N N 142 
GLC O5   O N N 143 
GLC O6   O N N 144 
GLC H1   H N N 145 
GLC H2   H N N 146 
GLC H3   H N N 147 
GLC H4   H N N 148 
GLC H5   H N N 149 
GLC H61  H N N 150 
GLC H62  H N N 151 
GLC HO1  H N N 152 
GLC HO2  H N N 153 
GLC HO3  H N N 154 
GLC HO4  H N N 155 
GLC HO6  H N N 156 
GLN N    N N N 157 
GLN CA   C N S 158 
GLN C    C N N 159 
GLN O    O N N 160 
GLN CB   C N N 161 
GLN CG   C N N 162 
GLN CD   C N N 163 
GLN OE1  O N N 164 
GLN NE2  N N N 165 
GLN OXT  O N N 166 
GLN H    H N N 167 
GLN H2   H N N 168 
GLN HA   H N N 169 
GLN HB2  H N N 170 
GLN HB3  H N N 171 
GLN HG2  H N N 172 
GLN HG3  H N N 173 
GLN HE21 H N N 174 
GLN HE22 H N N 175 
GLN HXT  H N N 176 
GLU N    N N N 177 
GLU CA   C N S 178 
GLU C    C N N 179 
GLU O    O N N 180 
GLU CB   C N N 181 
GLU CG   C N N 182 
GLU CD   C N N 183 
GLU OE1  O N N 184 
GLU OE2  O N N 185 
GLU OXT  O N N 186 
GLU H    H N N 187 
GLU H2   H N N 188 
GLU HA   H N N 189 
GLU HB2  H N N 190 
GLU HB3  H N N 191 
GLU HG2  H N N 192 
GLU HG3  H N N 193 
GLU HE2  H N N 194 
GLU HXT  H N N 195 
GLY N    N N N 196 
GLY CA   C N N 197 
GLY C    C N N 198 
GLY O    O N N 199 
GLY OXT  O N N 200 
GLY H    H N N 201 
GLY H2   H N N 202 
GLY HA2  H N N 203 
GLY HA3  H N N 204 
GLY HXT  H N N 205 
GOL C1   C N N 206 
GOL O1   O N N 207 
GOL C2   C N N 208 
GOL O2   O N N 209 
GOL C3   C N N 210 
GOL O3   O N N 211 
GOL H11  H N N 212 
GOL H12  H N N 213 
GOL HO1  H N N 214 
GOL H2   H N N 215 
GOL HO2  H N N 216 
GOL H31  H N N 217 
GOL H32  H N N 218 
GOL HO3  H N N 219 
HIS N    N N N 220 
HIS CA   C N S 221 
HIS C    C N N 222 
HIS O    O N N 223 
HIS CB   C N N 224 
HIS CG   C Y N 225 
HIS ND1  N Y N 226 
HIS CD2  C Y N 227 
HIS CE1  C Y N 228 
HIS NE2  N Y N 229 
HIS OXT  O N N 230 
HIS H    H N N 231 
HIS H2   H N N 232 
HIS HA   H N N 233 
HIS HB2  H N N 234 
HIS HB3  H N N 235 
HIS HD1  H N N 236 
HIS HD2  H N N 237 
HIS HE1  H N N 238 
HIS HE2  H N N 239 
HIS HXT  H N N 240 
HOH O    O N N 241 
HOH H1   H N N 242 
HOH H2   H N N 243 
ILE N    N N N 244 
ILE CA   C N S 245 
ILE C    C N N 246 
ILE O    O N N 247 
ILE CB   C N S 248 
ILE CG1  C N N 249 
ILE CG2  C N N 250 
ILE CD1  C N N 251 
ILE OXT  O N N 252 
ILE H    H N N 253 
ILE H2   H N N 254 
ILE HA   H N N 255 
ILE HB   H N N 256 
ILE HG12 H N N 257 
ILE HG13 H N N 258 
ILE HG21 H N N 259 
ILE HG22 H N N 260 
ILE HG23 H N N 261 
ILE HD11 H N N 262 
ILE HD12 H N N 263 
ILE HD13 H N N 264 
ILE HXT  H N N 265 
LEU N    N N N 266 
LEU CA   C N S 267 
LEU C    C N N 268 
LEU O    O N N 269 
LEU CB   C N N 270 
LEU CG   C N N 271 
LEU CD1  C N N 272 
LEU CD2  C N N 273 
LEU OXT  O N N 274 
LEU H    H N N 275 
LEU H2   H N N 276 
LEU HA   H N N 277 
LEU HB2  H N N 278 
LEU HB3  H N N 279 
LEU HG   H N N 280 
LEU HD11 H N N 281 
LEU HD12 H N N 282 
LEU HD13 H N N 283 
LEU HD21 H N N 284 
LEU HD22 H N N 285 
LEU HD23 H N N 286 
LEU HXT  H N N 287 
LYS N    N N N 288 
LYS CA   C N S 289 
LYS C    C N N 290 
LYS O    O N N 291 
LYS CB   C N N 292 
LYS CG   C N N 293 
LYS CD   C N N 294 
LYS CE   C N N 295 
LYS NZ   N N N 296 
LYS OXT  O N N 297 
LYS H    H N N 298 
LYS H2   H N N 299 
LYS HA   H N N 300 
LYS HB2  H N N 301 
LYS HB3  H N N 302 
LYS HG2  H N N 303 
LYS HG3  H N N 304 
LYS HD2  H N N 305 
LYS HD3  H N N 306 
LYS HE2  H N N 307 
LYS HE3  H N N 308 
LYS HZ1  H N N 309 
LYS HZ2  H N N 310 
LYS HZ3  H N N 311 
LYS HXT  H N N 312 
MET N    N N N 313 
MET CA   C N S 314 
MET C    C N N 315 
MET O    O N N 316 
MET CB   C N N 317 
MET CG   C N N 318 
MET SD   S N N 319 
MET CE   C N N 320 
MET OXT  O N N 321 
MET H    H N N 322 
MET H2   H N N 323 
MET HA   H N N 324 
MET HB2  H N N 325 
MET HB3  H N N 326 
MET HG2  H N N 327 
MET HG3  H N N 328 
MET HE1  H N N 329 
MET HE2  H N N 330 
MET HE3  H N N 331 
MET HXT  H N N 332 
PHE N    N N N 333 
PHE CA   C N S 334 
PHE C    C N N 335 
PHE O    O N N 336 
PHE CB   C N N 337 
PHE CG   C Y N 338 
PHE CD1  C Y N 339 
PHE CD2  C Y N 340 
PHE CE1  C Y N 341 
PHE CE2  C Y N 342 
PHE CZ   C Y N 343 
PHE OXT  O N N 344 
PHE H    H N N 345 
PHE H2   H N N 346 
PHE HA   H N N 347 
PHE HB2  H N N 348 
PHE HB3  H N N 349 
PHE HD1  H N N 350 
PHE HD2  H N N 351 
PHE HE1  H N N 352 
PHE HE2  H N N 353 
PHE HZ   H N N 354 
PHE HXT  H N N 355 
PRO N    N N N 356 
PRO CA   C N S 357 
PRO C    C N N 358 
PRO O    O N N 359 
PRO CB   C N N 360 
PRO CG   C N N 361 
PRO CD   C N N 362 
PRO OXT  O N N 363 
PRO H    H N N 364 
PRO HA   H N N 365 
PRO HB2  H N N 366 
PRO HB3  H N N 367 
PRO HG2  H N N 368 
PRO HG3  H N N 369 
PRO HD2  H N N 370 
PRO HD3  H N N 371 
PRO HXT  H N N 372 
SER N    N N N 373 
SER CA   C N S 374 
SER C    C N N 375 
SER O    O N N 376 
SER CB   C N N 377 
SER OG   O N N 378 
SER OXT  O N N 379 
SER H    H N N 380 
SER H2   H N N 381 
SER HA   H N N 382 
SER HB2  H N N 383 
SER HB3  H N N 384 
SER HG   H N N 385 
SER HXT  H N N 386 
THR N    N N N 387 
THR CA   C N S 388 
THR C    C N N 389 
THR O    O N N 390 
THR CB   C N R 391 
THR OG1  O N N 392 
THR CG2  C N N 393 
THR OXT  O N N 394 
THR H    H N N 395 
THR H2   H N N 396 
THR HA   H N N 397 
THR HB   H N N 398 
THR HG1  H N N 399 
THR HG21 H N N 400 
THR HG22 H N N 401 
THR HG23 H N N 402 
THR HXT  H N N 403 
TRP N    N N N 404 
TRP CA   C N S 405 
TRP C    C N N 406 
TRP O    O N N 407 
TRP CB   C N N 408 
TRP CG   C Y N 409 
TRP CD1  C Y N 410 
TRP CD2  C Y N 411 
TRP NE1  N Y N 412 
TRP CE2  C Y N 413 
TRP CE3  C Y N 414 
TRP CZ2  C Y N 415 
TRP CZ3  C Y N 416 
TRP CH2  C Y N 417 
TRP OXT  O N N 418 
TRP H    H N N 419 
TRP H2   H N N 420 
TRP HA   H N N 421 
TRP HB2  H N N 422 
TRP HB3  H N N 423 
TRP HD1  H N N 424 
TRP HE1  H N N 425 
TRP HE3  H N N 426 
TRP HZ2  H N N 427 
TRP HZ3  H N N 428 
TRP HH2  H N N 429 
TRP HXT  H N N 430 
TYR N    N N N 431 
TYR CA   C N S 432 
TYR C    C N N 433 
TYR O    O N N 434 
TYR CB   C N N 435 
TYR CG   C Y N 436 
TYR CD1  C Y N 437 
TYR CD2  C Y N 438 
TYR CE1  C Y N 439 
TYR CE2  C Y N 440 
TYR CZ   C Y N 441 
TYR OH   O N N 442 
TYR OXT  O N N 443 
TYR H    H N N 444 
TYR H2   H N N 445 
TYR HA   H N N 446 
TYR HB2  H N N 447 
TYR HB3  H N N 448 
TYR HD1  H N N 449 
TYR HD2  H N N 450 
TYR HE1  H N N 451 
TYR HE2  H N N 452 
TYR HH   H N N 453 
TYR HXT  H N N 454 
VAL N    N N N 455 
VAL CA   C N S 456 
VAL C    C N N 457 
VAL O    O N N 458 
VAL CB   C N N 459 
VAL CG1  C N N 460 
VAL CG2  C N N 461 
VAL OXT  O N N 462 
VAL H    H N N 463 
VAL H2   H N N 464 
VAL HA   H N N 465 
VAL HB   H N N 466 
VAL HG11 H N N 467 
VAL HG12 H N N 468 
VAL HG13 H N N 469 
VAL HG21 H N N 470 
VAL HG22 H N N 471 
VAL HG23 H N N 472 
VAL HXT  H N N 473 
# 
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 
AC1 C1  C2   sing N N 1   
AC1 C1  O5   sing N N 2   
AC1 C1  O1   sing N N 3   
AC1 C1  H1   sing N N 4   
AC1 O2  C2   sing N N 5   
AC1 O2  HO2  sing N N 6   
AC1 C2  C3   sing N N 7   
AC1 C2  H2   sing N N 8   
AC1 C4A C3B  sing N N 9   
AC1 C4A O4   sing N N 10  
AC1 C4A C5B  sing N N 11  
AC1 C4A HC4  sing N N 12  
AC1 C3  O3   sing N N 13  
AC1 C3  C4   sing N N 14  
AC1 C3  H3   sing N N 15  
AC1 O3  HO3  sing N N 16  
AC1 C4  N4A  sing N N 17  
AC1 C4  C5   sing N N 18  
AC1 C4  H4   sing N N 19  
AC1 N4A C1B  sing N N 20  
AC1 N4A HN4  sing N N 21  
AC1 C5  O5   sing N N 22  
AC1 C5  C6   sing N N 23  
AC1 C5  H5   sing N N 24  
AC1 C6  H61  sing N N 25  
AC1 C6  H62  sing N N 26  
AC1 C6  H63  sing N N 27  
AC1 C1B C2B  sing N N 28  
AC1 C1B C7B  sing N N 29  
AC1 C1B HCB1 sing N N 30  
AC1 C2B O2B  sing N N 31  
AC1 C2B C3B  sing N N 32  
AC1 C2B HCB2 sing N N 33  
AC1 O2B HO2B sing N N 34  
AC1 C3B O3B  sing N N 35  
AC1 C3B HCB3 sing N N 36  
AC1 O3B HOB3 sing N N 37  
AC1 O4  HO4  sing N N 38  
AC1 C5B C7B  doub N N 39  
AC1 C5B C6B  sing N N 40  
AC1 C7B HC7  sing N N 41  
AC1 C6B O6B  sing N N 42  
AC1 C6B HC61 sing N N 43  
AC1 C6B HC62 sing N N 44  
AC1 O6B HO6B sing N N 45  
AC1 O1  HO1  sing N N 46  
ALA N   CA   sing N N 47  
ALA N   H    sing N N 48  
ALA N   H2   sing N N 49  
ALA CA  C    sing N N 50  
ALA CA  CB   sing N N 51  
ALA CA  HA   sing N N 52  
ALA C   O    doub N N 53  
ALA C   OXT  sing N N 54  
ALA CB  HB1  sing N N 55  
ALA CB  HB2  sing N N 56  
ALA CB  HB3  sing N N 57  
ALA OXT HXT  sing N N 58  
ARG N   CA   sing N N 59  
ARG N   H    sing N N 60  
ARG N   H2   sing N N 61  
ARG CA  C    sing N N 62  
ARG CA  CB   sing N N 63  
ARG CA  HA   sing N N 64  
ARG C   O    doub N N 65  
ARG C   OXT  sing N N 66  
ARG CB  CG   sing N N 67  
ARG CB  HB2  sing N N 68  
ARG CB  HB3  sing N N 69  
ARG CG  CD   sing N N 70  
ARG CG  HG2  sing N N 71  
ARG CG  HG3  sing N N 72  
ARG CD  NE   sing N N 73  
ARG CD  HD2  sing N N 74  
ARG CD  HD3  sing N N 75  
ARG NE  CZ   sing N N 76  
ARG NE  HE   sing N N 77  
ARG CZ  NH1  sing N N 78  
ARG CZ  NH2  doub N N 79  
ARG NH1 HH11 sing N N 80  
ARG NH1 HH12 sing N N 81  
ARG NH2 HH21 sing N N 82  
ARG NH2 HH22 sing N N 83  
ARG OXT HXT  sing N N 84  
ASN N   CA   sing N N 85  
ASN N   H    sing N N 86  
ASN N   H2   sing N N 87  
ASN CA  C    sing N N 88  
ASN CA  CB   sing N N 89  
ASN CA  HA   sing N N 90  
ASN C   O    doub N N 91  
ASN C   OXT  sing N N 92  
ASN CB  CG   sing N N 93  
ASN CB  HB2  sing N N 94  
ASN CB  HB3  sing N N 95  
ASN CG  OD1  doub N N 96  
ASN CG  ND2  sing N N 97  
ASN ND2 HD21 sing N N 98  
ASN ND2 HD22 sing N N 99  
ASN OXT HXT  sing N N 100 
ASP N   CA   sing N N 101 
ASP N   H    sing N N 102 
ASP N   H2   sing N N 103 
ASP CA  C    sing N N 104 
ASP CA  CB   sing N N 105 
ASP CA  HA   sing N N 106 
ASP C   O    doub N N 107 
ASP C   OXT  sing N N 108 
ASP CB  CG   sing N N 109 
ASP CB  HB2  sing N N 110 
ASP CB  HB3  sing N N 111 
ASP CG  OD1  doub N N 112 
ASP CG  OD2  sing N N 113 
ASP OD2 HD2  sing N N 114 
ASP OXT HXT  sing N N 115 
CYS N   CA   sing N N 116 
CYS N   H    sing N N 117 
CYS N   H2   sing N N 118 
CYS CA  C    sing N N 119 
CYS CA  CB   sing N N 120 
CYS CA  HA   sing N N 121 
CYS C   O    doub N N 122 
CYS C   OXT  sing N N 123 
CYS CB  SG   sing N N 124 
CYS CB  HB2  sing N N 125 
CYS CB  HB3  sing N N 126 
CYS SG  HG   sing N N 127 
CYS OXT HXT  sing N N 128 
GLC C1  C2   sing N N 129 
GLC C1  O1   sing N N 130 
GLC C1  O5   sing N N 131 
GLC C1  H1   sing N N 132 
GLC C2  C3   sing N N 133 
GLC C2  O2   sing N N 134 
GLC C2  H2   sing N N 135 
GLC C3  C4   sing N N 136 
GLC C3  O3   sing N N 137 
GLC C3  H3   sing N N 138 
GLC C4  C5   sing N N 139 
GLC C4  O4   sing N N 140 
GLC C4  H4   sing N N 141 
GLC C5  C6   sing N N 142 
GLC C5  O5   sing N N 143 
GLC C5  H5   sing N N 144 
GLC C6  O6   sing N N 145 
GLC C6  H61  sing N N 146 
GLC C6  H62  sing N N 147 
GLC O1  HO1  sing N N 148 
GLC O2  HO2  sing N N 149 
GLC O3  HO3  sing N N 150 
GLC O4  HO4  sing N N 151 
GLC O6  HO6  sing N N 152 
GLN N   CA   sing N N 153 
GLN N   H    sing N N 154 
GLN N   H2   sing N N 155 
GLN CA  C    sing N N 156 
GLN CA  CB   sing N N 157 
GLN CA  HA   sing N N 158 
GLN C   O    doub N N 159 
GLN C   OXT  sing N N 160 
GLN CB  CG   sing N N 161 
GLN CB  HB2  sing N N 162 
GLN CB  HB3  sing N N 163 
GLN CG  CD   sing N N 164 
GLN CG  HG2  sing N N 165 
GLN CG  HG3  sing N N 166 
GLN CD  OE1  doub N N 167 
GLN CD  NE2  sing N N 168 
GLN NE2 HE21 sing N N 169 
GLN NE2 HE22 sing N N 170 
GLN OXT HXT  sing N N 171 
GLU N   CA   sing N N 172 
GLU N   H    sing N N 173 
GLU N   H2   sing N N 174 
GLU CA  C    sing N N 175 
GLU CA  CB   sing N N 176 
GLU CA  HA   sing N N 177 
GLU C   O    doub N N 178 
GLU C   OXT  sing N N 179 
GLU CB  CG   sing N N 180 
GLU CB  HB2  sing N N 181 
GLU CB  HB3  sing N N 182 
GLU CG  CD   sing N N 183 
GLU CG  HG2  sing N N 184 
GLU CG  HG3  sing N N 185 
GLU CD  OE1  doub N N 186 
GLU CD  OE2  sing N N 187 
GLU OE2 HE2  sing N N 188 
GLU OXT HXT  sing N N 189 
GLY N   CA   sing N N 190 
GLY N   H    sing N N 191 
GLY N   H2   sing N N 192 
GLY CA  C    sing N N 193 
GLY CA  HA2  sing N N 194 
GLY CA  HA3  sing N N 195 
GLY C   O    doub N N 196 
GLY C   OXT  sing N N 197 
GLY OXT HXT  sing N N 198 
GOL C1  O1   sing N N 199 
GOL C1  C2   sing N N 200 
GOL C1  H11  sing N N 201 
GOL C1  H12  sing N N 202 
GOL O1  HO1  sing N N 203 
GOL C2  O2   sing N N 204 
GOL C2  C3   sing N N 205 
GOL C2  H2   sing N N 206 
GOL O2  HO2  sing N N 207 
GOL C3  O3   sing N N 208 
GOL C3  H31  sing N N 209 
GOL C3  H32  sing N N 210 
GOL O3  HO3  sing N N 211 
HIS N   CA   sing N N 212 
HIS N   H    sing N N 213 
HIS N   H2   sing N N 214 
HIS CA  C    sing N N 215 
HIS CA  CB   sing N N 216 
HIS CA  HA   sing N N 217 
HIS C   O    doub N N 218 
HIS C   OXT  sing N N 219 
HIS CB  CG   sing N N 220 
HIS CB  HB2  sing N N 221 
HIS CB  HB3  sing N N 222 
HIS CG  ND1  sing Y N 223 
HIS CG  CD2  doub Y N 224 
HIS ND1 CE1  doub Y N 225 
HIS ND1 HD1  sing N N 226 
HIS CD2 NE2  sing Y N 227 
HIS CD2 HD2  sing N N 228 
HIS CE1 NE2  sing Y N 229 
HIS CE1 HE1  sing N N 230 
HIS NE2 HE2  sing N N 231 
HIS OXT HXT  sing N N 232 
HOH O   H1   sing N N 233 
HOH O   H2   sing N N 234 
ILE N   CA   sing N N 235 
ILE N   H    sing N N 236 
ILE N   H2   sing N N 237 
ILE CA  C    sing N N 238 
ILE CA  CB   sing N N 239 
ILE CA  HA   sing N N 240 
ILE C   O    doub N N 241 
ILE C   OXT  sing N N 242 
ILE CB  CG1  sing N N 243 
ILE CB  CG2  sing N N 244 
ILE CB  HB   sing N N 245 
ILE CG1 CD1  sing N N 246 
ILE CG1 HG12 sing N N 247 
ILE CG1 HG13 sing N N 248 
ILE CG2 HG21 sing N N 249 
ILE CG2 HG22 sing N N 250 
ILE CG2 HG23 sing N N 251 
ILE CD1 HD11 sing N N 252 
ILE CD1 HD12 sing N N 253 
ILE CD1 HD13 sing N N 254 
ILE OXT HXT  sing N N 255 
LEU N   CA   sing N N 256 
LEU N   H    sing N N 257 
LEU N   H2   sing N N 258 
LEU CA  C    sing N N 259 
LEU CA  CB   sing N N 260 
LEU CA  HA   sing N N 261 
LEU C   O    doub N N 262 
LEU C   OXT  sing N N 263 
LEU CB  CG   sing N N 264 
LEU CB  HB2  sing N N 265 
LEU CB  HB3  sing N N 266 
LEU CG  CD1  sing N N 267 
LEU CG  CD2  sing N N 268 
LEU CG  HG   sing N N 269 
LEU CD1 HD11 sing N N 270 
LEU CD1 HD12 sing N N 271 
LEU CD1 HD13 sing N N 272 
LEU CD2 HD21 sing N N 273 
LEU CD2 HD22 sing N N 274 
LEU CD2 HD23 sing N N 275 
LEU OXT HXT  sing N N 276 
LYS N   CA   sing N N 277 
LYS N   H    sing N N 278 
LYS N   H2   sing N N 279 
LYS CA  C    sing N N 280 
LYS CA  CB   sing N N 281 
LYS CA  HA   sing N N 282 
LYS C   O    doub N N 283 
LYS C   OXT  sing N N 284 
LYS CB  CG   sing N N 285 
LYS CB  HB2  sing N N 286 
LYS CB  HB3  sing N N 287 
LYS CG  CD   sing N N 288 
LYS CG  HG2  sing N N 289 
LYS CG  HG3  sing N N 290 
LYS CD  CE   sing N N 291 
LYS CD  HD2  sing N N 292 
LYS CD  HD3  sing N N 293 
LYS CE  NZ   sing N N 294 
LYS CE  HE2  sing N N 295 
LYS CE  HE3  sing N N 296 
LYS NZ  HZ1  sing N N 297 
LYS NZ  HZ2  sing N N 298 
LYS NZ  HZ3  sing N N 299 
LYS OXT HXT  sing N N 300 
MET N   CA   sing N N 301 
MET N   H    sing N N 302 
MET N   H2   sing N N 303 
MET CA  C    sing N N 304 
MET CA  CB   sing N N 305 
MET CA  HA   sing N N 306 
MET C   O    doub N N 307 
MET C   OXT  sing N N 308 
MET CB  CG   sing N N 309 
MET CB  HB2  sing N N 310 
MET CB  HB3  sing N N 311 
MET CG  SD   sing N N 312 
MET CG  HG2  sing N N 313 
MET CG  HG3  sing N N 314 
MET SD  CE   sing N N 315 
MET CE  HE1  sing N N 316 
MET CE  HE2  sing N N 317 
MET CE  HE3  sing N N 318 
MET OXT HXT  sing N N 319 
PHE N   CA   sing N N 320 
PHE N   H    sing N N 321 
PHE N   H2   sing N N 322 
PHE CA  C    sing N N 323 
PHE CA  CB   sing N N 324 
PHE CA  HA   sing N N 325 
PHE C   O    doub N N 326 
PHE C   OXT  sing N N 327 
PHE CB  CG   sing N N 328 
PHE CB  HB2  sing N N 329 
PHE CB  HB3  sing N N 330 
PHE CG  CD1  doub Y N 331 
PHE CG  CD2  sing Y N 332 
PHE CD1 CE1  sing Y N 333 
PHE CD1 HD1  sing N N 334 
PHE CD2 CE2  doub Y N 335 
PHE CD2 HD2  sing N N 336 
PHE CE1 CZ   doub Y N 337 
PHE CE1 HE1  sing N N 338 
PHE CE2 CZ   sing Y N 339 
PHE CE2 HE2  sing N N 340 
PHE CZ  HZ   sing N N 341 
PHE OXT HXT  sing N N 342 
PRO N   CA   sing N N 343 
PRO N   CD   sing N N 344 
PRO N   H    sing N N 345 
PRO CA  C    sing N N 346 
PRO CA  CB   sing N N 347 
PRO CA  HA   sing N N 348 
PRO C   O    doub N N 349 
PRO C   OXT  sing N N 350 
PRO CB  CG   sing N N 351 
PRO CB  HB2  sing N N 352 
PRO CB  HB3  sing N N 353 
PRO CG  CD   sing N N 354 
PRO CG  HG2  sing N N 355 
PRO CG  HG3  sing N N 356 
PRO CD  HD2  sing N N 357 
PRO CD  HD3  sing N N 358 
PRO OXT HXT  sing N N 359 
SER N   CA   sing N N 360 
SER N   H    sing N N 361 
SER N   H2   sing N N 362 
SER CA  C    sing N N 363 
SER CA  CB   sing N N 364 
SER CA  HA   sing N N 365 
SER C   O    doub N N 366 
SER C   OXT  sing N N 367 
SER CB  OG   sing N N 368 
SER CB  HB2  sing N N 369 
SER CB  HB3  sing N N 370 
SER OG  HG   sing N N 371 
SER OXT HXT  sing N N 372 
THR N   CA   sing N N 373 
THR N   H    sing N N 374 
THR N   H2   sing N N 375 
THR CA  C    sing N N 376 
THR CA  CB   sing N N 377 
THR CA  HA   sing N N 378 
THR C   O    doub N N 379 
THR C   OXT  sing N N 380 
THR CB  OG1  sing N N 381 
THR CB  CG2  sing N N 382 
THR CB  HB   sing N N 383 
THR OG1 HG1  sing N N 384 
THR CG2 HG21 sing N N 385 
THR CG2 HG22 sing N N 386 
THR CG2 HG23 sing N N 387 
THR OXT HXT  sing N N 388 
TRP N   CA   sing N N 389 
TRP N   H    sing N N 390 
TRP N   H2   sing N N 391 
TRP CA  C    sing N N 392 
TRP CA  CB   sing N N 393 
TRP CA  HA   sing N N 394 
TRP C   O    doub N N 395 
TRP C   OXT  sing N N 396 
TRP CB  CG   sing N N 397 
TRP CB  HB2  sing N N 398 
TRP CB  HB3  sing N N 399 
TRP CG  CD1  doub Y N 400 
TRP CG  CD2  sing Y N 401 
TRP CD1 NE1  sing Y N 402 
TRP CD1 HD1  sing N N 403 
TRP CD2 CE2  doub Y N 404 
TRP CD2 CE3  sing Y N 405 
TRP NE1 CE2  sing Y N 406 
TRP NE1 HE1  sing N N 407 
TRP CE2 CZ2  sing Y N 408 
TRP CE3 CZ3  doub Y N 409 
TRP CE3 HE3  sing N N 410 
TRP CZ2 CH2  doub Y N 411 
TRP CZ2 HZ2  sing N N 412 
TRP CZ3 CH2  sing Y N 413 
TRP CZ3 HZ3  sing N N 414 
TRP CH2 HH2  sing N N 415 
TRP OXT HXT  sing N N 416 
TYR N   CA   sing N N 417 
TYR N   H    sing N N 418 
TYR N   H2   sing N N 419 
TYR CA  C    sing N N 420 
TYR CA  CB   sing N N 421 
TYR CA  HA   sing N N 422 
TYR C   O    doub N N 423 
TYR C   OXT  sing N N 424 
TYR CB  CG   sing N N 425 
TYR CB  HB2  sing N N 426 
TYR CB  HB3  sing N N 427 
TYR CG  CD1  doub Y N 428 
TYR CG  CD2  sing Y N 429 
TYR CD1 CE1  sing Y N 430 
TYR CD1 HD1  sing N N 431 
TYR CD2 CE2  doub Y N 432 
TYR CD2 HD2  sing N N 433 
TYR CE1 CZ   doub Y N 434 
TYR CE1 HE1  sing N N 435 
TYR CE2 CZ   sing Y N 436 
TYR CE2 HE2  sing N N 437 
TYR CZ  OH   sing N N 438 
TYR OH  HH   sing N N 439 
TYR OXT HXT  sing N N 440 
VAL N   CA   sing N N 441 
VAL N   H    sing N N 442 
VAL N   H2   sing N N 443 
VAL CA  C    sing N N 444 
VAL CA  CB   sing N N 445 
VAL CA  HA   sing N N 446 
VAL C   O    doub N N 447 
VAL C   OXT  sing N N 448 
VAL CB  CG1  sing N N 449 
VAL CB  CG2  sing N N 450 
VAL CB  HB   sing N N 451 
VAL CG1 HG11 sing N N 452 
VAL CG1 HG12 sing N N 453 
VAL CG1 HG13 sing N N 454 
VAL CG2 HG21 sing N N 455 
VAL CG2 HG22 sing N N 456 
VAL CG2 HG23 sing N N 457 
VAL OXT HXT  sing N N 458 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'Other government' China 2021YFC2301405 1 
'Other government' China 21ZR1471800    2 
# 
loop_
_pdbx_entity_branch_list.entity_id 
_pdbx_entity_branch_list.comp_id 
_pdbx_entity_branch_list.num 
_pdbx_entity_branch_list.hetero 
2 GLC 1 n 
2 GLC 2 n 
2 AC1 3 n 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'in silico model' 
_pdbx_initial_refinement_model.source_name      AlphaFold 
_pdbx_initial_refinement_model.accession_code   ? 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9IHT 
_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]   0.016412 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.001667 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.024932 
_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]   0.005151 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
H 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . LYS A 1 2   ? -3.542  16.262 36.759  1.00 35.06 ? 2   LYS A N   1 
ATOM   2    C CA  . LYS A 1 2   ? -2.621  16.606 37.844  1.00 29.92 ? 2   LYS A CA  1 
ATOM   3    C C   . LYS A 1 2   ? -3.387  16.918 39.121  1.00 29.07 ? 2   LYS A C   1 
ATOM   4    O O   . LYS A 1 2   ? -4.044  17.951 39.217  1.00 35.36 ? 2   LYS A O   1 
ATOM   5    C CB  . LYS A 1 2   ? -1.749  17.799 37.459  1.00 31.69 ? 2   LYS A CB  1 
ATOM   6    C CG  . LYS A 1 2   ? -0.706  18.159 38.503  1.00 34.84 ? 2   LYS A CG  1 
ATOM   7    C CD  . LYS A 1 2   ? 0.064   19.418 38.108  1.00 42.27 ? 2   LYS A CD  1 
ATOM   8    C CE  . LYS A 1 2   ? -0.806  20.662 38.282  1.00 43.24 ? 2   LYS A CE  1 
ATOM   9    N NZ  . LYS A 1 2   ? -0.052  21.925 38.052  1.00 39.39 ? 2   LYS A NZ  1 
ATOM   10   N N   . LYS A 1 3   ? -3.297  16.026 40.098  1.00 24.98 ? 3   LYS A N   1 
ATOM   11   C CA  . LYS A 1 3   ? -4.039  16.145 41.342  1.00 22.84 ? 3   LYS A CA  1 
ATOM   12   C C   . LYS A 1 3   ? -3.169  16.757 42.435  1.00 27.12 ? 3   LYS A C   1 
ATOM   13   O O   . LYS A 1 3   ? -1.940  16.651 42.413  1.00 23.05 ? 3   LYS A O   1 
ATOM   14   C CB  . LYS A 1 3   ? -4.537  14.778 41.813  1.00 29.95 ? 3   LYS A CB  1 
ATOM   15   C CG  . LYS A 1 3   ? -5.476  14.067 40.846  1.00 36.01 ? 3   LYS A CG  1 
ATOM   16   C CD  . LYS A 1 3   ? -6.847  14.697 40.832  1.00 37.51 ? 3   LYS A CD  1 
ATOM   17   C CE  . LYS A 1 3   ? -7.779  13.952 39.880  1.00 43.62 ? 3   LYS A CE  1 
ATOM   18   N NZ  . LYS A 1 3   ? -8.149  12.608 40.390  1.00 48.74 ? 3   LYS A NZ  1 
ATOM   19   N N   . LEU A 1 4   ? -3.822  17.399 43.394  1.00 20.86 ? 4   LEU A N   1 
ATOM   20   C CA  . LEU A 1 4   ? -3.209  17.701 44.681  1.00 20.21 ? 4   LEU A CA  1 
ATOM   21   C C   . LEU A 1 4   ? -3.633  16.607 45.653  1.00 21.32 ? 4   LEU A C   1 
ATOM   22   O O   . LEU A 1 4   ? -4.826  16.314 45.767  1.00 23.65 ? 4   LEU A O   1 
ATOM   23   C CB  . LEU A 1 4   ? -3.644  19.074 45.201  1.00 21.02 ? 4   LEU A CB  1 
ATOM   24   C CG  . LEU A 1 4   ? -3.083  19.534 46.554  1.00 20.66 ? 4   LEU A CG  1 
ATOM   25   C CD1 . LEU A 1 4   ? -2.860  21.037 46.535  1.00 20.43 ? 4   LEU A CD1 1 
ATOM   26   C CD2 . LEU A 1 4   ? -4.003  19.136 47.731  1.00 18.49 ? 4   LEU A CD2 1 
ATOM   27   N N   . PHE A 1 5   ? -2.672  16.003 46.344  1.00 18.88 ? 5   PHE A N   1 
ATOM   28   C CA  . PHE A 1 5   ? -2.973  14.963 47.319  1.00 22.45 ? 5   PHE A CA  1 
ATOM   29   C C   . PHE A 1 5   ? -3.049  15.582 48.708  1.00 23.67 ? 5   PHE A C   1 
ATOM   30   O O   . PHE A 1 5   ? -2.082  16.190 49.178  1.00 22.26 ? 5   PHE A O   1 
ATOM   31   C CB  . PHE A 1 5   ? -1.935  13.846 47.272  1.00 15.25 ? 5   PHE A CB  1 
ATOM   32   C CG  . PHE A 1 5   ? -1.897  13.117 45.962  1.00 19.47 ? 5   PHE A CG  1 
ATOM   33   C CD1 . PHE A 1 5   ? -3.038  12.519 45.462  1.00 21.32 ? 5   PHE A CD1 1 
ATOM   34   C CD2 . PHE A 1 5   ? -0.711  12.982 45.258  1.00 22.14 ? 5   PHE A CD2 1 
ATOM   35   C CE1 . PHE A 1 5   ? -3.015  11.835 44.263  1.00 20.77 ? 5   PHE A CE1 1 
ATOM   36   C CE2 . PHE A 1 5   ? -0.676  12.289 44.065  1.00 19.97 ? 5   PHE A CE2 1 
ATOM   37   C CZ  . PHE A 1 5   ? -1.830  11.718 43.561  1.00 22.37 ? 5   PHE A CZ  1 
ATOM   38   N N   . LEU A 1 6   ? -4.202  15.438 49.357  1.00 17.86 ? 6   LEU A N   1 
ATOM   39   C CA  . LEU A 1 6   ? -4.457  16.055 50.645  1.00 16.21 ? 6   LEU A CA  1 
ATOM   40   C C   . LEU A 1 6   ? -4.577  14.954 51.690  1.00 18.71 ? 6   LEU A C   1 
ATOM   41   O O   . LEU A 1 6   ? -5.303  13.979 51.485  1.00 17.24 ? 6   LEU A O   1 
ATOM   42   C CB  . LEU A 1 6   ? -5.733  16.898 50.588  1.00 17.11 ? 6   LEU A CB  1 
ATOM   43   C CG  . LEU A 1 6   ? -6.158  17.685 51.820  1.00 16.33 ? 6   LEU A CG  1 
ATOM   44   C CD1 . LEU A 1 6   ? -5.067  18.672 52.218  1.00 18.67 ? 6   LEU A CD1 1 
ATOM   45   C CD2 . LEU A 1 6   ? -7.453  18.413 51.488  1.00 16.23 ? 6   LEU A CD2 1 
ATOM   46   N N   . VAL A 1 7   ? -3.861  15.099 52.801  1.00 14.56 ? 7   VAL A N   1 
ATOM   47   C CA  . VAL A 1 7   ? -3.816  14.060 53.831  1.00 15.00 ? 7   VAL A CA  1 
ATOM   48   C C   . VAL A 1 7   ? -4.121  14.714 55.169  1.00 15.95 ? 7   VAL A C   1 
ATOM   49   O O   . VAL A 1 7   ? -3.296  15.474 55.689  1.00 17.31 ? 7   VAL A O   1 
ATOM   50   C CB  . VAL A 1 7   ? -2.456  13.349 53.879  1.00 17.45 ? 7   VAL A CB  1 
ATOM   51   C CG1 . VAL A 1 7   ? -2.509  12.170 54.855  1.00 16.98 ? 7   VAL A CG1 1 
ATOM   52   C CG2 . VAL A 1 7   ? -2.027  12.892 52.485  1.00 24.66 ? 7   VAL A CG2 1 
ATOM   53   N N   . PHE A 1 8   ? -5.305  14.429 55.724  1.00 14.82 ? 8   PHE A N   1 
ATOM   54   C CA  . PHE A 1 8   ? -5.629  14.831 57.095  1.00 12.82 ? 8   PHE A CA  1 
ATOM   55   C C   . PHE A 1 8   ? -5.182  13.748 58.065  1.00 11.54 ? 8   PHE A C   1 
ATOM   56   O O   . PHE A 1 8   ? -5.425  12.562 57.833  1.00 15.89 ? 8   PHE A O   1 
ATOM   57   C CB  . PHE A 1 8   ? -7.138  15.062 57.283  1.00 13.03 ? 8   PHE A CB  1 
ATOM   58   C CG  . PHE A 1 8   ? -7.664  16.256 56.548  1.00 11.16 ? 8   PHE A CG  1 
ATOM   59   C CD1 . PHE A 1 8   ? -7.628  17.521 57.133  1.00 16.22 ? 8   PHE A CD1 1 
ATOM   60   C CD2 . PHE A 1 8   ? -8.174  16.120 55.280  1.00 12.55 ? 8   PHE A CD2 1 
ATOM   61   C CE1 . PHE A 1 8   ? -8.110  18.621 56.444  1.00 18.35 ? 8   PHE A CE1 1 
ATOM   62   C CE2 . PHE A 1 8   ? -8.647  17.213 54.583  1.00 19.08 ? 8   PHE A CE2 1 
ATOM   63   C CZ  . PHE A 1 8   ? -8.611  18.470 55.170  1.00 14.46 ? 8   PHE A CZ  1 
ATOM   64   N N   . TRP A 1 9   ? -4.566  14.168 59.176  1.00 14.86 ? 9   TRP A N   1 
ATOM   65   C CA  . TRP A 1 9   ? -4.135  13.224 60.204  1.00 13.77 ? 9   TRP A CA  1 
ATOM   66   C C   . TRP A 1 9   ? -4.474  13.894 61.530  1.00 13.19 ? 9   TRP A C   1 
ATOM   67   O O   . TRP A 1 9   ? -3.803  14.841 61.936  1.00 11.63 ? 9   TRP A O   1 
ATOM   68   C CB  . TRP A 1 9   ? -2.651  12.901 60.042  1.00 13.31 ? 9   TRP A CB  1 
ATOM   69   C CG  . TRP A 1 9   ? -2.149  11.714 60.832  1.00 11.24 ? 9   TRP A CG  1 
ATOM   70   C CD1 . TRP A 1 9   ? -2.844  10.944 61.736  1.00 11.45 ? 9   TRP A CD1 1 
ATOM   71   C CD2 . TRP A 1 9   ? -0.856  11.130 60.710  1.00 13.15 ? 9   TRP A CD2 1 
ATOM   72   N NE1 . TRP A 1 9   ? -2.021  9.942  62.223  1.00 13.28 ? 9   TRP A NE1 1 
ATOM   73   C CE2 . TRP A 1 9   ? -0.795  10.042 61.605  1.00 10.57 ? 9   TRP A CE2 1 
ATOM   74   C CE3 . TRP A 1 9   ? 0.281   11.453 59.956  1.00 16.57 ? 9   TRP A CE3 1 
ATOM   75   C CZ2 . TRP A 1 9   ? 0.340   9.255  61.739  1.00 13.92 ? 9   TRP A CZ2 1 
ATOM   76   C CZ3 . TRP A 1 9   ? 1.406   10.673 60.093  1.00 16.16 ? 9   TRP A CZ3 1 
ATOM   77   C CH2 . TRP A 1 9   ? 1.435   9.590  60.991  1.00 14.42 ? 9   TRP A CH2 1 
ATOM   78   N N   . TRP A 1 10  ? -5.559  13.438 62.149  1.00 11.13 ? 10  TRP A N   1 
ATOM   79   C CA  . TRP A 1 10  ? -6.130  14.043 63.343  1.00 11.51 ? 10  TRP A CA  1 
ATOM   80   C C   . TRP A 1 10  ? -5.594  13.302 64.562  1.00 13.16 ? 10  TRP A C   1 
ATOM   81   O O   . TRP A 1 10  ? -5.859  12.112 64.723  1.00 10.65 ? 10  TRP A O   1 
ATOM   82   C CB  . TRP A 1 10  ? -7.662  13.950 63.308  1.00 10.37 ? 10  TRP A CB  1 
ATOM   83   C CG  . TRP A 1 10  ? -8.361  14.726 62.196  1.00 9.61  ? 10  TRP A CG  1 
ATOM   84   C CD1 . TRP A 1 10  ? -9.058  14.198 61.139  1.00 12.50 ? 10  TRP A CD1 1 
ATOM   85   C CD2 . TRP A 1 10  ? -8.414  16.156 62.034  1.00 10.93 ? 10  TRP A CD2 1 
ATOM   86   N NE1 . TRP A 1 10  ? -9.550  15.207 60.340  1.00 12.29 ? 10  TRP A NE1 1 
ATOM   87   C CE2 . TRP A 1 10  ? -9.163  16.416 60.866  1.00 12.37 ? 10  TRP A CE2 1 
ATOM   88   C CE3 . TRP A 1 10  ? -7.913  17.238 62.776  1.00 9.26  ? 10  TRP A CE3 1 
ATOM   89   C CZ2 . TRP A 1 10  ? -9.427  17.710 60.418  1.00 10.55 ? 10  TRP A CZ2 1 
ATOM   90   C CZ3 . TRP A 1 10  ? -8.171  18.536 62.324  1.00 12.51 ? 10  TRP A CZ3 1 
ATOM   91   C CH2 . TRP A 1 10  ? -8.921  18.757 61.151  1.00 10.21 ? 10  TRP A CH2 1 
ATOM   92   N N   . HIS A 1 11  ? -4.861  13.998 65.424  1.00 9.43  ? 11  HIS A N   1 
ATOM   93   C CA  . HIS A 1 11  ? -4.189  13.339 66.551  1.00 8.15  ? 11  HIS A CA  1 
ATOM   94   C C   . HIS A 1 11  ? -5.043  13.434 67.813  1.00 10.86 ? 11  HIS A C   1 
ATOM   95   O O   . HIS A 1 11  ? -5.397  14.534 68.245  1.00 9.84  ? 11  HIS A O   1 
ATOM   96   C CB  . HIS A 1 11  ? -2.819  13.979 66.782  1.00 9.02  ? 11  HIS A CB  1 
ATOM   97   C CG  . HIS A 1 11  ? -2.263  13.736 68.146  1.00 8.81  ? 11  HIS A CG  1 
ATOM   98   N ND1 . HIS A 1 11  ? -1.939  12.476 68.607  1.00 9.63  ? 11  HIS A ND1 1 
ATOM   99   C CD2 . HIS A 1 11  ? -2.001  14.591 69.163  1.00 9.84  ? 11  HIS A CD2 1 
ATOM   100  C CE1 . HIS A 1 11  ? -1.471  12.572 69.839  1.00 10.43 ? 11  HIS A CE1 1 
ATOM   101  N NE2 . HIS A 1 11  ? -1.511  13.843 70.205  1.00 10.40 ? 11  HIS A NE2 1 
ATOM   102  N N   . MET A 1 12  ? -5.349  12.282 68.421  1.00 7.63  ? 12  MET A N   1 
ATOM   103  C CA  . MET A 1 12  ? -6.252  12.202 69.565  1.00 8.01  ? 12  MET A CA  1 
ATOM   104  C C   . MET A 1 12  ? -5.487  11.667 70.763  1.00 10.87 ? 12  MET A C   1 
ATOM   105  O O   . MET A 1 12  ? -4.877  10.589 70.674  1.00 10.15 ? 12  MET A O   1 
ATOM   106  C CB  . MET A 1 12  ? -7.432  11.258 69.269  1.00 7.82  ? 12  MET A CB  1 
ATOM   107  C CG  . MET A 1 12  ? -8.212  11.550 67.987  1.00 7.56  ? 12  MET A CG  1 
ATOM   108  S SD  . MET A 1 12  ? -8.878  13.227 67.960  1.00 10.88 ? 12  MET A SD  1 
ATOM   109  C CE  . MET A 1 12  ? -10.012 13.046 66.569  1.00 11.17 ? 12  MET A CE  1 
ATOM   110  N N   . HIS A 1 13  ? -5.562  12.377 71.896  1.00 7.53  ? 13  HIS A N   1 
ATOM   111  C CA  . HIS A 1 13  ? -4.782  11.997 73.066  1.00 8.06  ? 13  HIS A CA  1 
ATOM   112  C C   . HIS A 1 13  ? -5.364  12.625 74.329  1.00 8.41  ? 13  HIS A C   1 
ATOM   113  O O   . HIS A 1 13  ? -5.830  13.766 74.301  1.00 9.33  ? 13  HIS A O   1 
ATOM   114  C CB  . HIS A 1 13  ? -3.311  12.425 72.904  1.00 9.96  ? 13  HIS A CB  1 
ATOM   115  C CG  . HIS A 1 13  ? -2.505  12.295 74.161  1.00 9.78  ? 13  HIS A CG  1 
ATOM   116  N ND1 . HIS A 1 13  ? -2.351  11.094 74.826  1.00 8.56  ? 13  HIS A ND1 1 
ATOM   117  C CD2 . HIS A 1 13  ? -1.801  13.213 74.873  1.00 8.46  ? 13  HIS A CD2 1 
ATOM   118  C CE1 . HIS A 1 13  ? -1.591  11.279 75.894  1.00 11.36 ? 13  HIS A CE1 1 
ATOM   119  N NE2 . HIS A 1 13  ? -1.252  12.557 75.949  1.00 9.91  ? 13  HIS A NE2 1 
ATOM   120  N N   . GLN A 1 14  ? -5.310  11.880 75.437  1.00 7.57  ? 14  GLN A N   1 
ATOM   121  C CA  . GLN A 1 14  ? -5.462  12.447 76.770  1.00 8.12  ? 14  GLN A CA  1 
ATOM   122  C C   . GLN A 1 14  ? -4.453  11.753 77.670  1.00 10.87 ? 14  GLN A C   1 
ATOM   123  O O   . GLN A 1 14  ? -4.265  10.528 77.557  1.00 10.64 ? 14  GLN A O   1 
ATOM   124  C CB  . GLN A 1 14  ? -6.879  12.237 77.359  1.00 7.75  ? 14  GLN A CB  1 
ATOM   125  C CG  . GLN A 1 14  ? -8.034  12.931 76.617  1.00 9.14  ? 14  GLN A CG  1 
ATOM   126  C CD  . GLN A 1 14  ? -7.953  14.445 76.698  1.00 10.82 ? 14  GLN A CD  1 
ATOM   127  O OE1 . GLN A 1 14  ? -7.393  15.004 77.643  1.00 9.62  ? 14  GLN A OE1 1 
ATOM   128  N NE2 . GLN A 1 14  ? -8.536  15.119 75.710  1.00 11.20 ? 14  GLN A NE2 1 
ATOM   129  N N   . PRO A 1 15  ? -3.811  12.480 78.580  1.00 10.36 ? 15  PRO A N   1 
ATOM   130  C CA  . PRO A 1 15  ? -2.994  11.814 79.606  1.00 8.40  ? 15  PRO A CA  1 
ATOM   131  C C   . PRO A 1 15  ? -3.893  11.060 80.580  1.00 8.88  ? 15  PRO A C   1 
ATOM   132  O O   . PRO A 1 15  ? -5.119  11.220 80.595  1.00 10.41 ? 15  PRO A O   1 
ATOM   133  C CB  . PRO A 1 15  ? -2.259  12.974 80.285  1.00 10.30 ? 15  PRO A CB  1 
ATOM   134  C CG  . PRO A 1 15  ? -3.283  14.131 80.198  1.00 9.02  ? 15  PRO A CG  1 
ATOM   135  C CD  . PRO A 1 15  ? -3.989  13.926 78.838  1.00 7.68  ? 15  PRO A CD  1 
ATOM   136  N N   . LEU A 1 16  ? -3.281  10.229 81.427  1.00 9.52  ? 16  LEU A N   1 
ATOM   137  C CA  . LEU A 1 16  ? -4.070  9.379  82.322  1.00 11.72 ? 16  LEU A CA  1 
ATOM   138  C C   . LEU A 1 16  ? -4.601  10.200 83.499  1.00 13.17 ? 16  LEU A C   1 
ATOM   139  O O   . LEU A 1 16  ? -3.829  10.601 84.380  1.00 12.66 ? 16  LEU A O   1 
ATOM   140  C CB  . LEU A 1 16  ? -3.216  8.214  82.826  1.00 10.65 ? 16  LEU A CB  1 
ATOM   141  C CG  . LEU A 1 16  ? -3.978  7.168  83.640  1.00 12.52 ? 16  LEU A CG  1 
ATOM   142  C CD1 . LEU A 1 16  ? -5.168  6.648  82.804  1.00 10.98 ? 16  LEU A CD1 1 
ATOM   143  C CD2 . LEU A 1 16  ? -3.053  6.039  84.054  1.00 10.08 ? 16  LEU A CD2 1 
ATOM   144  N N   . TYR A 1 17  ? -5.923  10.423 83.544  1.00 12.03 ? 17  TYR A N   1 
ATOM   145  C CA  . TYR A 1 17  ? -6.559  11.161 84.636  1.00 10.75 ? 17  TYR A CA  1 
ATOM   146  C C   . TYR A 1 17  ? -6.953  10.282 85.811  1.00 10.97 ? 17  TYR A C   1 
ATOM   147  O O   . TYR A 1 17  ? -7.444  10.807 86.817  1.00 11.01 ? 17  TYR A O   1 
ATOM   148  C CB  . TYR A 1 17  ? -7.814  11.899 84.142  1.00 12.24 ? 17  TYR A CB  1 
ATOM   149  C CG  . TYR A 1 17  ? -7.519  12.923 83.070  1.00 13.07 ? 17  TYR A CG  1 
ATOM   150  C CD1 . TYR A 1 17  ? -6.705  14.011 83.344  1.00 11.96 ? 17  TYR A CD1 1 
ATOM   151  C CD2 . TYR A 1 17  ? -8.051  12.801 81.783  1.00 10.66 ? 17  TYR A CD2 1 
ATOM   152  C CE1 . TYR A 1 17  ? -6.414  14.962 82.361  1.00 11.91 ? 17  TYR A CE1 1 
ATOM   153  C CE2 . TYR A 1 17  ? -7.772  13.760 80.791  1.00 10.47 ? 17  TYR A CE2 1 
ATOM   154  C CZ  . TYR A 1 17  ? -6.962  14.834 81.094  1.00 11.64 ? 17  TYR A CZ  1 
ATOM   155  O OH  . TYR A 1 17  ? -6.669  15.775 80.133  1.00 10.45 ? 17  TYR A OH  1 
ATOM   156  N N   . ARG A 1 18  ? -6.750  8.972  85.708  1.00 11.55 ? 18  ARG A N   1 
ATOM   157  C CA  . ARG A 1 18  ? -7.154  8.025  86.742  1.00 11.30 ? 18  ARG A CA  1 
ATOM   158  C C   . ARG A 1 18  ? -6.100  7.984  87.841  1.00 16.14 ? 18  ARG A C   1 
ATOM   159  O O   . ARG A 1 18  ? -4.991  7.466  87.633  1.00 13.26 ? 18  ARG A O   1 
ATOM   160  C CB  . ARG A 1 18  ? -7.335  6.644  86.122  1.00 17.46 ? 18  ARG A CB  1 
ATOM   161  C CG  . ARG A 1 18  ? -7.974  5.615  87.040  1.00 16.13 ? 18  ARG A CG  1 
ATOM   162  C CD  . ARG A 1 18  ? -7.936  4.254  86.359  1.00 23.87 ? 18  ARG A CD  1 
ATOM   163  N NE  . ARG A 1 18  ? -8.626  3.229  87.125  1.00 26.31 ? 18  ARG A NE  1 
ATOM   164  C CZ  . ARG A 1 18  ? -8.085  2.566  88.143  1.00 27.45 ? 18  ARG A CZ  1 
ATOM   165  N NH1 . ARG A 1 18  ? -6.842  2.830  88.532  1.00 23.70 ? 18  ARG A NH1 1 
ATOM   166  N NH2 . ARG A 1 18  ? -8.795  1.643  88.783  1.00 34.96 ? 18  ARG A NH2 1 
ATOM   167  N N   . GLU A 1 19  ? -6.450  8.515  89.001  1.00 15.81 ? 19  GLU A N   1 
ATOM   168  C CA  . GLU A 1 19  ? -5.545  8.517  90.144  1.00 16.32 ? 19  GLU A CA  1 
ATOM   169  C C   . GLU A 1 19  ? -5.337  7.080  90.613  1.00 14.00 ? 19  GLU A C   1 
ATOM   170  O O   . GLU A 1 19  ? -6.316  6.352  90.804  1.00 16.60 ? 19  GLU A O   1 
ATOM   171  C CB  . GLU A 1 19  ? -6.140  9.378  91.263  1.00 20.39 ? 19  GLU A CB  1 
ATOM   172  C CG  . GLU A 1 19  ? -5.115  9.950  92.230  1.00 30.62 ? 19  GLU A CG  1 
ATOM   173  C CD  . GLU A 1 19  ? -4.702  8.957  93.306  1.00 33.01 ? 19  GLU A CD  1 
ATOM   174  O OE1 . GLU A 1 19  ? -5.527  8.101  93.679  1.00 29.29 ? 19  GLU A OE1 1 
ATOM   175  O OE2 . GLU A 1 19  ? -3.547  9.029  93.767  1.00 35.43 ? 19  GLU A OE2 1 
ATOM   176  N N   . PRO A 1 20  ? -4.092  6.630  90.792  1.00 16.28 ? 20  PRO A N   1 
ATOM   177  C CA  . PRO A 1 20  ? -3.841  5.184  90.931  1.00 22.71 ? 20  PRO A CA  1 
ATOM   178  C C   . PRO A 1 20  ? -4.235  4.590  92.271  1.00 26.25 ? 20  PRO A C   1 
ATOM   179  O O   . PRO A 1 20  ? -4.503  3.383  92.332  1.00 32.43 ? 20  PRO A O   1 
ATOM   180  C CB  . PRO A 1 20  ? -2.318  5.069  90.711  1.00 22.42 ? 20  PRO A CB  1 
ATOM   181  C CG  . PRO A 1 20  ? -1.778  6.427  91.061  1.00 21.09 ? 20  PRO A CG  1 
ATOM   182  C CD  . PRO A 1 20  ? -2.845  7.397  90.599  1.00 16.11 ? 20  PRO A CD  1 
ATOM   183  N N   . TYR A 1 21  ? -4.278  5.382  93.339  1.00 19.32 ? 21  TYR A N   1 
ATOM   184  C CA  . TYR A 1 21  ? -4.630  4.839  94.645  1.00 20.70 ? 21  TYR A CA  1 
ATOM   185  C C   . TYR A 1 21  ? -6.143  4.760  94.842  1.00 21.97 ? 21  TYR A C   1 
ATOM   186  O O   . TYR A 1 21  ? -6.633  3.832  95.492  1.00 25.06 ? 21  TYR A O   1 
ATOM   187  C CB  . TYR A 1 21  ? -3.975  5.676  95.743  1.00 21.39 ? 21  TYR A CB  1 
ATOM   188  C CG  . TYR A 1 21  ? -2.461  5.545  95.750  1.00 26.19 ? 21  TYR A CG  1 
ATOM   189  C CD1 . TYR A 1 21  ? -1.842  4.486  96.411  1.00 32.50 ? 21  TYR A CD1 1 
ATOM   190  C CD2 . TYR A 1 21  ? -1.655  6.455  95.072  1.00 21.22 ? 21  TYR A CD2 1 
ATOM   191  C CE1 . TYR A 1 21  ? -0.465  4.339  96.415  1.00 29.45 ? 21  TYR A CE1 1 
ATOM   192  C CE2 . TYR A 1 21  ? -0.261  6.315  95.067  1.00 23.86 ? 21  TYR A CE2 1 
ATOM   193  C CZ  . TYR A 1 21  ? 0.319   5.256  95.746  1.00 30.48 ? 21  TYR A CZ  1 
ATOM   194  O OH  . TYR A 1 21  ? 1.689   5.092  95.761  1.00 28.47 ? 21  TYR A OH  1 
ATOM   195  N N   . THR A 1 22  ? -6.902  5.713  94.298  1.00 17.95 ? 22  THR A N   1 
ATOM   196  C CA  . THR A 1 22  ? -8.353  5.716  94.485  1.00 21.49 ? 22  THR A CA  1 
ATOM   197  C C   . THR A 1 22  ? -9.110  5.214  93.266  1.00 23.61 ? 22  THR A C   1 
ATOM   198  O O   . THR A 1 22  ? -10.291 4.868  93.390  1.00 22.84 ? 22  THR A O   1 
ATOM   199  C CB  . THR A 1 22  ? -8.866  7.126  94.821  1.00 19.77 ? 22  THR A CB  1 
ATOM   200  O OG1 . THR A 1 22  ? -8.623  8.014  93.714  1.00 21.00 ? 22  THR A OG1 1 
ATOM   201  C CG2 . THR A 1 22  ? -8.209  7.668  96.097  1.00 22.43 ? 22  THR A CG2 1 
ATOM   202  N N   . GLY A 1 23  ? -8.460  5.168  92.104  1.00 20.33 ? 23  GLY A N   1 
ATOM   203  C CA  . GLY A 1 23  ? -9.130  4.830  90.869  1.00 18.54 ? 23  GLY A CA  1 
ATOM   204  C C   . GLY A 1 23  ? -10.009 5.926  90.305  1.00 20.15 ? 23  GLY A C   1 
ATOM   205  O O   . GLY A 1 23  ? -10.701 5.694  89.311  1.00 26.57 ? 23  GLY A O   1 
ATOM   206  N N   . GLU A 1 24  ? -9.983  7.124  90.883  1.00 19.02 ? 24  GLU A N   1 
ATOM   207  C CA  . GLU A 1 24  ? -10.875 8.197  90.459  1.00 17.80 ? 24  GLU A CA  1 
ATOM   208  C C   . GLU A 1 24  ? -10.276 8.983  89.297  1.00 16.52 ? 24  GLU A C   1 
ATOM   209  O O   . GLU A 1 24  ? -9.102  9.376  89.347  1.00 13.86 ? 24  GLU A O   1 
ATOM   210  C CB  . GLU A 1 24  ? -11.178 9.137  91.625  1.00 17.56 ? 24  GLU A CB  1 
ATOM   211  C CG  . GLU A 1 24  ? -12.041 8.484  92.719  1.00 25.37 ? 24  GLU A CG  1 
ATOM   212  C CD  . GLU A 1 24  ? -12.145 9.331  93.972  1.00 36.12 ? 24  GLU A CD  1 
ATOM   213  O OE1 . GLU A 1 24  ? -11.489 10.393 94.037  1.00 42.40 ? 24  GLU A OE1 1 
ATOM   214  O OE2 . GLU A 1 24  ? -12.856 8.917  94.912  1.00 44.52 ? 24  GLU A OE2 1 
ATOM   215  N N   . TYR A 1 25  ? -11.094 9.225  88.261  1.00 14.46 ? 25  TYR A N   1 
ATOM   216  C CA  . TYR A 1 25  ? -10.715 10.148 87.198  1.00 13.45 ? 25  TYR A CA  1 
ATOM   217  C C   . TYR A 1 25  ? -10.872 11.568 87.732  1.00 15.69 ? 25  TYR A C   1 
ATOM   218  O O   . TYR A 1 25  ? -11.995 12.017 87.998  1.00 13.83 ? 25  TYR A O   1 
ATOM   219  C CB  . TYR A 1 25  ? -11.556 9.937  85.937  1.00 13.12 ? 25  TYR A CB  1 
ATOM   220  C CG  . TYR A 1 25  ? -11.115 8.753  85.119  1.00 13.22 ? 25  TYR A CG  1 
ATOM   221  C CD1 . TYR A 1 25  ? -11.297 7.443  85.559  1.00 13.67 ? 25  TYR A CD1 1 
ATOM   222  C CD2 . TYR A 1 25  ? -10.407 8.954  83.940  1.00 15.35 ? 25  TYR A CD2 1 
ATOM   223  C CE1 . TYR A 1 25  ? -10.846 6.366  84.787  1.00 18.67 ? 25  TYR A CE1 1 
ATOM   224  C CE2 . TYR A 1 25  ? -9.955  7.893  83.178  1.00 11.49 ? 25  TYR A CE2 1 
ATOM   225  C CZ  . TYR A 1 25  ? -10.169 6.609  83.606  1.00 17.78 ? 25  TYR A CZ  1 
ATOM   226  O OH  . TYR A 1 25  ? -9.705  5.571  82.827  1.00 16.98 ? 25  TYR A OH  1 
ATOM   227  N N   . LEU A 1 26  ? -9.747  12.258 87.941  1.00 12.67 ? 26  LEU A N   1 
ATOM   228  C CA  . LEU A 1 26  ? -9.792  13.514 88.664  1.00 15.41 ? 26  LEU A CA  1 
ATOM   229  C C   . LEU A 1 26  ? -10.157 14.691 87.775  1.00 13.55 ? 26  LEU A C   1 
ATOM   230  O O   . LEU A 1 26  ? -10.469 15.765 88.302  1.00 15.22 ? 26  LEU A O   1 
ATOM   231  C CB  . LEU A 1 26  ? -8.450  13.772 89.356  1.00 11.61 ? 26  LEU A CB  1 
ATOM   232  C CG  . LEU A 1 26  ? -8.048  12.705 90.382  1.00 16.62 ? 26  LEU A CG  1 
ATOM   233  C CD1 . LEU A 1 26  ? -6.744  13.107 91.092  1.00 17.69 ? 26  LEU A CD1 1 
ATOM   234  C CD2 . LEU A 1 26  ? -9.173  12.435 91.379  1.00 19.44 ? 26  LEU A CD2 1 
ATOM   235  N N   . LEU A 1 27  ? -10.123 14.515 86.455  1.00 12.72 ? 27  LEU A N   1 
ATOM   236  C CA  . LEU A 1 27  ? -10.599 15.499 85.498  1.00 13.73 ? 27  LEU A CA  1 
ATOM   237  C C   . LEU A 1 27  ? -11.483 14.790 84.484  1.00 12.68 ? 27  LEU A C   1 
ATOM   238  O O   . LEU A 1 27  ? -11.287 13.597 84.220  1.00 14.50 ? 27  LEU A O   1 
ATOM   239  C CB  . LEU A 1 27  ? -9.434  16.200 84.783  1.00 13.25 ? 27  LEU A CB  1 
ATOM   240  C CG  . LEU A 1 27  ? -8.567  17.093 85.675  1.00 15.83 ? 27  LEU A CG  1 
ATOM   241  C CD1 . LEU A 1 27  ? -7.292  17.555 84.948  1.00 14.71 ? 27  LEU A CD1 1 
ATOM   242  C CD2 . LEU A 1 27  ? -9.364  18.278 86.215  1.00 20.34 ? 27  LEU A CD2 1 
ATOM   243  N N   . PRO A 1 28  ? -12.496 15.470 83.951  1.00 13.00 ? 28  PRO A N   1 
ATOM   244  C CA  . PRO A 1 28  ? -13.432 14.819 83.021  1.00 11.42 ? 28  PRO A CA  1 
ATOM   245  C C   . PRO A 1 28  ? -13.060 14.958 81.554  1.00 10.24 ? 28  PRO A C   1 
ATOM   246  O O   . PRO A 1 28  ? -13.912 14.701 80.697  1.00 11.71 ? 28  PRO A O   1 
ATOM   247  C CB  . PRO A 1 28  ? -14.733 15.577 83.302  1.00 11.16 ? 28  PRO A CB  1 
ATOM   248  C CG  . PRO A 1 28  ? -14.238 16.998 83.478  1.00 16.35 ? 28  PRO A CG  1 
ATOM   249  C CD  . PRO A 1 28  ? -12.907 16.862 84.228  1.00 16.21 ? 28  PRO A CD  1 
ATOM   250  N N   . TRP A 1 29  ? -11.842 15.378 81.234  1.00 10.68 ? 29  TRP A N   1 
ATOM   251  C CA  . TRP A 1 29  ? -11.564 15.754 79.853  1.00 10.22 ? 29  TRP A CA  1 
ATOM   252  C C   . TRP A 1 29  ? -11.634 14.571 78.892  1.00 12.78 ? 29  TRP A C   1 
ATOM   253  O O   . TRP A 1 29  ? -11.996 14.748 77.722  1.00 11.76 ? 29  TRP A O   1 
ATOM   254  C CB  . TRP A 1 29  ? -10.214 16.431 79.767  1.00 11.15 ? 29  TRP A CB  1 
ATOM   255  C CG  . TRP A 1 29  ? -10.117 17.719 80.559  1.00 13.58 ? 29  TRP A CG  1 
ATOM   256  C CD1 . TRP A 1 29  ? -9.209  18.000 81.549  1.00 14.45 ? 29  TRP A CD1 1 
ATOM   257  C CD2 . TRP A 1 29  ? -10.904 18.913 80.393  1.00 15.96 ? 29  TRP A CD2 1 
ATOM   258  N NE1 . TRP A 1 29  ? -9.390  19.279 82.009  1.00 19.73 ? 29  TRP A NE1 1 
ATOM   259  C CE2 . TRP A 1 29  ? -10.419 19.862 81.317  1.00 16.23 ? 29  TRP A CE2 1 
ATOM   260  C CE3 . TRP A 1 29  ? -11.953 19.273 79.547  1.00 16.73 ? 29  TRP A CE3 1 
ATOM   261  C CZ2 . TRP A 1 29  ? -10.952 21.141 81.422  1.00 21.64 ? 29  TRP A CZ2 1 
ATOM   262  C CZ3 . TRP A 1 29  ? -12.485 20.549 79.656  1.00 15.47 ? 29  TRP A CZ3 1 
ATOM   263  C CH2 . TRP A 1 29  ? -11.984 21.463 80.581  1.00 19.24 ? 29  TRP A CH2 1 
ATOM   264  N N   . THR A 1 30  ? -11.312 13.360 79.339  1.00 9.92  ? 30  THR A N   1 
ATOM   265  C CA  . THR A 1 30  ? -11.503 12.223 78.445  1.00 10.63 ? 30  THR A CA  1 
ATOM   266  C C   . THR A 1 30  ? -12.983 12.005 78.156  1.00 13.39 ? 30  THR A C   1 
ATOM   267  O O   . THR A 1 30  ? -13.377 11.806 77.001  1.00 12.24 ? 30  THR A O   1 
ATOM   268  C CB  . THR A 1 30  ? -10.864 10.965 79.033  1.00 10.21 ? 30  THR A CB  1 
ATOM   269  O OG1 . THR A 1 30  ? -9.452  11.175 79.144  1.00 12.46 ? 30  THR A OG1 1 
ATOM   270  C CG2 . THR A 1 30  ? -11.112 9.772  78.132  1.00 14.02 ? 30  THR A CG2 1 
ATOM   271  N N   . PHE A 1 31  ? -13.831 12.076 79.185  1.00 9.00  ? 31  PHE A N   1 
ATOM   272  C CA  . PHE A 1 31  ? -15.264 11.922 78.947  1.00 11.17 ? 31  PHE A CA  1 
ATOM   273  C C   . PHE A 1 31  ? -15.771 12.984 77.972  1.00 11.05 ? 31  PHE A C   1 
ATOM   274  O O   . PHE A 1 31  ? -16.440 12.674 76.981  1.00 10.24 ? 31  PHE A O   1 
ATOM   275  C CB  . PHE A 1 31  ? -16.036 11.996 80.264  1.00 10.05 ? 31  PHE A CB  1 
ATOM   276  C CG  . PHE A 1 31  ? -17.523 11.981 80.085  1.00 12.15 ? 31  PHE A CG  1 
ATOM   277  C CD1 . PHE A 1 31  ? -18.204 10.782 79.913  1.00 12.79 ? 31  PHE A CD1 1 
ATOM   278  C CD2 . PHE A 1 31  ? -18.241 13.166 80.073  1.00 13.29 ? 31  PHE A CD2 1 
ATOM   279  C CE1 . PHE A 1 31  ? -19.599 10.767 79.765  1.00 14.48 ? 31  PHE A CE1 1 
ATOM   280  C CE2 . PHE A 1 31  ? -19.633 13.162 79.916  1.00 16.23 ? 31  PHE A CE2 1 
ATOM   281  C CZ  . PHE A 1 31  ? -20.304 11.967 79.756  1.00 15.71 ? 31  PHE A CZ  1 
ATOM   282  N N   . PHE A 1 32  ? -15.435 14.249 78.215  1.00 9.39  ? 32  PHE A N   1 
ATOM   283  C CA  . PHE A 1 32  ? -16.011 15.301 77.380  1.00 9.61  ? 32  PHE A CA  1 
ATOM   284  C C   . PHE A 1 32  ? -15.492 15.252 75.945  1.00 10.08 ? 32  PHE A C   1 
ATOM   285  O O   . PHE A 1 32  ? -16.258 15.483 75.002  1.00 11.68 ? 32  PHE A O   1 
ATOM   286  C CB  . PHE A 1 32  ? -15.758 16.672 77.992  1.00 10.32 ? 32  PHE A CB  1 
ATOM   287  C CG  . PHE A 1 32  ? -16.662 16.973 79.149  1.00 10.00 ? 32  PHE A CG  1 
ATOM   288  C CD1 . PHE A 1 32  ? -18.027 16.806 79.018  1.00 11.36 ? 32  PHE A CD1 1 
ATOM   289  C CD2 . PHE A 1 32  ? -16.154 17.417 80.348  1.00 13.68 ? 32  PHE A CD2 1 
ATOM   290  C CE1 . PHE A 1 32  ? -18.885 17.085 80.067  1.00 17.40 ? 32  PHE A CE1 1 
ATOM   291  C CE2 . PHE A 1 32  ? -17.005 17.699 81.407  1.00 16.68 ? 32  PHE A CE2 1 
ATOM   292  C CZ  . PHE A 1 32  ? -18.370 17.533 81.263  1.00 15.20 ? 32  PHE A CZ  1 
ATOM   293  N N   . HIS A 1 33  ? -14.198 14.990 75.743  1.00 9.10  ? 33  HIS A N   1 
ATOM   294  C CA  . HIS A 1 33  ? -13.736 14.888 74.361  1.00 9.58  ? 33  HIS A CA  1 
ATOM   295  C C   . HIS A 1 33  ? -14.188 13.591 73.685  1.00 9.01  ? 33  HIS A C   1 
ATOM   296  O O   . HIS A 1 33  ? -14.301 13.552 72.448  1.00 10.99 ? 33  HIS A O   1 
ATOM   297  C CB  . HIS A 1 33  ? -12.214 15.068 74.296  1.00 8.76  ? 33  HIS A CB  1 
ATOM   298  C CG  . HIS A 1 33  ? -11.794 16.495 74.519  1.00 8.49  ? 33  HIS A CG  1 
ATOM   299  N ND1 . HIS A 1 33  ? -12.063 17.488 73.601  1.00 8.19  ? 33  HIS A ND1 1 
ATOM   300  C CD2 . HIS A 1 33  ? -11.174 17.096 75.562  1.00 10.29 ? 33  HIS A CD2 1 
ATOM   301  C CE1 . HIS A 1 33  ? -11.612 18.642 74.063  1.00 7.53  ? 33  HIS A CE1 1 
ATOM   302  N NE2 . HIS A 1 33  ? -11.073 18.434 75.254  1.00 9.14  ? 33  HIS A NE2 1 
ATOM   303  N N   . ALA A 1 34  ? -14.476 12.541 74.455  1.00 9.96  ? 34  ALA A N   1 
ATOM   304  C CA  . ALA A 1 34  ? -15.060 11.345 73.856  1.00 12.83 ? 34  ALA A CA  1 
ATOM   305  C C   . ALA A 1 34  ? -16.466 11.626 73.323  1.00 13.44 ? 34  ALA A C   1 
ATOM   306  O O   . ALA A 1 34  ? -16.787 11.263 72.184  1.00 11.70 ? 34  ALA A O   1 
ATOM   307  C CB  . ALA A 1 34  ? -15.072 10.194 74.870  1.00 11.99 ? 34  ALA A CB  1 
ATOM   308  N N   . VAL A 1 35  ? -17.315 12.303 74.112  1.00 11.99 ? 35  VAL A N   1 
ATOM   309  C CA  . VAL A 1 35  ? -18.680 12.545 73.647  1.00 13.40 ? 35  VAL A CA  1 
ATOM   310  C C   . VAL A 1 35  ? -18.748 13.649 72.597  1.00 11.35 ? 35  VAL A C   1 
ATOM   311  O O   . VAL A 1 35  ? -19.692 13.666 71.788  1.00 11.82 ? 35  VAL A O   1 
ATOM   312  C CB  . VAL A 1 35  ? -19.637 12.866 74.812  1.00 11.40 ? 35  VAL A CB  1 
ATOM   313  C CG1 . VAL A 1 35  ? -19.587 11.760 75.860  1.00 12.36 ? 35  VAL A CG1 1 
ATOM   314  C CG2 . VAL A 1 35  ? -19.300 14.198 75.457  1.00 12.04 ? 35  VAL A CG2 1 
ATOM   315  N N   . LYS A 1 36  ? -17.760 14.549 72.559  1.00 8.22  ? 36  LYS A N   1 
ATOM   316  C CA  . LYS A 1 36  ? -17.775 15.660 71.611  1.00 12.46 ? 36  LYS A CA  1 
ATOM   317  C C   . LYS A 1 36  ? -17.025 15.342 70.314  1.00 13.32 ? 36  LYS A C   1 
ATOM   318  O O   . LYS A 1 36  ? -17.491 15.704 69.224  1.00 13.43 ? 36  LYS A O   1 
ATOM   319  C CB  . LYS A 1 36  ? -17.167 16.909 72.259  1.00 7.90  ? 36  LYS A CB  1 
ATOM   320  C CG  . LYS A 1 36  ? -17.470 18.224 71.494  1.00 9.63  ? 36  LYS A CG  1 
ATOM   321  C CD  . LYS A 1 36  ? -17.034 19.472 72.269  1.00 11.92 ? 36  LYS A CD  1 
ATOM   322  C CE  . LYS A 1 36  ? -15.543 19.680 72.246  1.00 11.26 ? 36  LYS A CE  1 
ATOM   323  N NZ  . LYS A 1 36  ? -14.992 19.931 70.865  1.00 11.79 ? 36  LYS A NZ  1 
ATOM   324  N N   . ASP A 1 37  ? -15.862 14.691 70.416  1.00 10.37 ? 37  ASP A N   1 
ATOM   325  C CA  . ASP A 1 37  ? -14.899 14.629 69.312  1.00 10.47 ? 37  ASP A CA  1 
ATOM   326  C C   . ASP A 1 37  ? -14.488 13.226 68.904  1.00 10.05 ? 37  ASP A C   1 
ATOM   327  O O   . ASP A 1 37  ? -14.348 12.957 67.705  1.00 11.77 ? 37  ASP A O   1 
ATOM   328  C CB  . ASP A 1 37  ? -13.635 15.406 69.705  1.00 10.43 ? 37  ASP A CB  1 
ATOM   329  C CG  . ASP A 1 37  ? -13.945 16.807 70.188  1.00 11.52 ? 37  ASP A CG  1 
ATOM   330  O OD1 . ASP A 1 37  ? -14.523 17.618 69.424  1.00 11.34 ? 37  ASP A OD1 1 
ATOM   331  O OD2 . ASP A 1 37  ? -13.695 17.061 71.380  1.00 10.92 ? 37  ASP A OD2 1 
ATOM   332  N N   . TYR A 1 38  ? -14.245 12.321 69.861  1.00 9.62  ? 38  TYR A N   1 
ATOM   333  C CA  . TYR A 1 38  ? -13.534 11.105 69.480  1.00 11.92 ? 38  TYR A CA  1 
ATOM   334  C C   . TYR A 1 38  ? -14.397 10.179 68.639  1.00 11.55 ? 38  TYR A C   1 
ATOM   335  O O   . TYR A 1 38  ? -13.858 9.467  67.793  1.00 12.16 ? 38  TYR A O   1 
ATOM   336  C CB  . TYR A 1 38  ? -12.994 10.374 70.709  1.00 9.64  ? 38  TYR A CB  1 
ATOM   337  C CG  . TYR A 1 38  ? -11.917 11.156 71.434  1.00 9.38  ? 38  TYR A CG  1 
ATOM   338  C CD1 . TYR A 1 38  ? -11.026 11.978 70.730  1.00 10.49 ? 38  TYR A CD1 1 
ATOM   339  C CD2 . TYR A 1 38  ? -11.789 11.093 72.825  1.00 7.75  ? 38  TYR A CD2 1 
ATOM   340  C CE1 . TYR A 1 38  ? -10.033 12.706 71.402  1.00 9.28  ? 38  TYR A CE1 1 
ATOM   341  C CE2 . TYR A 1 38  ? -10.803 11.829 73.488  1.00 11.58 ? 38  TYR A CE2 1 
ATOM   342  C CZ  . TYR A 1 38  ? -9.934  12.627 72.771  1.00 9.36  ? 38  TYR A CZ  1 
ATOM   343  O OH  . TYR A 1 38  ? -8.943  13.352 73.430  1.00 10.56 ? 38  TYR A OH  1 
ATOM   344  N N   . TYR A 1 39  ? -15.716 10.143 68.871  1.00 8.28  ? 39  TYR A N   1 
ATOM   345  C CA  . TYR A 1 39  ? -16.604 9.428  67.949  1.00 8.87  ? 39  TYR A CA  1 
ATOM   346  C C   . TYR A 1 39  ? -16.927 10.267 66.722  1.00 12.08 ? 39  TYR A C   1 
ATOM   347  O O   . TYR A 1 39  ? -16.917 9.763  65.595  1.00 12.26 ? 39  TYR A O   1 
ATOM   348  C CB  . TYR A 1 39  ? -17.909 9.036  68.658  1.00 8.57  ? 39  TYR A CB  1 
ATOM   349  C CG  . TYR A 1 39  ? -18.927 8.431  67.720  1.00 12.84 ? 39  TYR A CG  1 
ATOM   350  C CD1 . TYR A 1 39  ? -18.853 7.091  67.366  1.00 14.40 ? 39  TYR A CD1 1 
ATOM   351  C CD2 . TYR A 1 39  ? -19.952 9.206  67.169  1.00 12.06 ? 39  TYR A CD2 1 
ATOM   352  C CE1 . TYR A 1 39  ? -19.799 6.512  66.516  1.00 14.83 ? 39  TYR A CE1 1 
ATOM   353  C CE2 . TYR A 1 39  ? -20.885 8.650  66.296  1.00 13.66 ? 39  TYR A CE2 1 
ATOM   354  C CZ  . TYR A 1 39  ? -20.799 7.305  65.975  1.00 14.11 ? 39  TYR A CZ  1 
ATOM   355  O OH  . TYR A 1 39  ? -21.721 6.736  65.126  1.00 18.87 ? 39  TYR A OH  1 
ATOM   356  N N   . ASP A 1 40  ? -17.234 11.547 66.928  1.00 12.68 ? 40  ASP A N   1 
ATOM   357  C CA  . ASP A 1 40  ? -17.810 12.343 65.854  1.00 12.88 ? 40  ASP A CA  1 
ATOM   358  C C   . ASP A 1 40  ? -16.790 12.674 64.773  1.00 12.49 ? 40  ASP A C   1 
ATOM   359  O O   . ASP A 1 40  ? -17.165 12.773 63.603  1.00 11.14 ? 40  ASP A O   1 
ATOM   360  C CB  . ASP A 1 40  ? -18.456 13.587 66.452  1.00 13.70 ? 40  ASP A CB  1 
ATOM   361  C CG  . ASP A 1 40  ? -19.861 13.289 66.966  1.00 12.59 ? 40  ASP A CG  1 
ATOM   362  O OD1 . ASP A 1 40  ? -20.761 13.061 66.124  1.00 14.13 ? 40  ASP A OD1 1 
ATOM   363  O OD2 . ASP A 1 40  ? -20.049 13.169 68.198  1.00 14.67 ? 40  ASP A OD2 1 
ATOM   364  N N   . MET A 1 41  ? -15.506 12.817 65.120  1.00 12.04 ? 41  MET A N   1 
ATOM   365  C CA  . MET A 1 41  ? -14.533 13.169 64.085  1.00 10.33 ? 41  MET A CA  1 
ATOM   366  C C   . MET A 1 41  ? -14.414 12.075 63.037  1.00 12.31 ? 41  MET A C   1 
ATOM   367  O O   . MET A 1 41  ? -14.555 12.385 61.840  1.00 13.14 ? 41  MET A O   1 
ATOM   368  C CB  . MET A 1 41  ? -13.173 13.528 64.711  1.00 11.07 ? 41  MET A CB  1 
ATOM   369  C CG  . MET A 1 41  ? -13.113 14.922 65.345  1.00 12.02 ? 41  MET A CG  1 
ATOM   370  S SD  . MET A 1 41  ? -13.235 16.243 64.095  1.00 11.82 ? 41  MET A SD  1 
ATOM   371  C CE  . MET A 1 41  ? -11.545 16.217 63.503  1.00 9.00  ? 41  MET A CE  1 
ATOM   372  N N   . PRO A 1 42  ? -14.219 10.792 63.387  1.00 12.30 ? 42  PRO A N   1 
ATOM   373  C CA  . PRO A 1 42  ? -14.295 9.760  62.341  1.00 10.20 ? 42  PRO A CA  1 
ATOM   374  C C   . PRO A 1 42  ? -15.682 9.590  61.762  1.00 13.01 ? 42  PRO A C   1 
ATOM   375  O O   . PRO A 1 42  ? -15.803 9.159  60.612  1.00 13.99 ? 42  PRO A O   1 
ATOM   376  C CB  . PRO A 1 42  ? -13.838 8.481  63.057  1.00 12.14 ? 42  PRO A CB  1 
ATOM   377  C CG  . PRO A 1 42  ? -14.031 8.751  64.518  1.00 12.21 ? 42  PRO A CG  1 
ATOM   378  C CD  . PRO A 1 42  ? -13.753 10.227 64.675  1.00 10.24 ? 42  PRO A CD  1 
ATOM   379  N N   . ALA A 1 43  ? -16.738 9.888  62.520  1.00 11.06 ? 43  ALA A N   1 
ATOM   380  C CA  . ALA A 1 43  ? -18.084 9.661  62.004  1.00 13.58 ? 43  ALA A CA  1 
ATOM   381  C C   . ALA A 1 43  ? -18.447 10.609 60.860  1.00 17.14 ? 43  ALA A C   1 
ATOM   382  O O   . ALA A 1 43  ? -19.413 10.336 60.135  1.00 15.43 ? 43  ALA A O   1 
ATOM   383  C CB  . ALA A 1 43  ? -19.101 9.775  63.146  1.00 11.30 ? 43  ALA A CB  1 
ATOM   384  N N   . TYR A 1 44  ? -17.683 11.686 60.647  1.00 10.68 ? 44  TYR A N   1 
ATOM   385  C CA  . TYR A 1 44  ? -17.902 12.485 59.437  1.00 12.79 ? 44  TYR A CA  1 
ATOM   386  C C   . TYR A 1 44  ? -17.770 11.632 58.183  1.00 13.05 ? 44  TYR A C   1 
ATOM   387  O O   . TYR A 1 44  ? -18.395 11.935 57.156  1.00 15.35 ? 44  TYR A O   1 
ATOM   388  C CB  . TYR A 1 44  ? -16.909 13.642 59.353  1.00 12.64 ? 44  TYR A CB  1 
ATOM   389  C CG  . TYR A 1 44  ? -17.274 14.865 60.159  1.00 11.86 ? 44  TYR A CG  1 
ATOM   390  C CD1 . TYR A 1 44  ? -18.090 15.868 59.625  1.00 13.31 ? 44  TYR A CD1 1 
ATOM   391  C CD2 . TYR A 1 44  ? -16.795 15.018 61.462  1.00 10.47 ? 44  TYR A CD2 1 
ATOM   392  C CE1 . TYR A 1 44  ? -18.412 17.007 60.375  1.00 14.03 ? 44  TYR A CE1 1 
ATOM   393  C CE2 . TYR A 1 44  ? -17.125 16.135 62.213  1.00 11.81 ? 44  TYR A CE2 1 
ATOM   394  C CZ  . TYR A 1 44  ? -17.914 17.128 61.668  1.00 14.15 ? 44  TYR A CZ  1 
ATOM   395  O OH  . TYR A 1 44  ? -18.191 18.244 62.449  1.00 15.89 ? 44  TYR A OH  1 
ATOM   396  N N   . LEU A 1 45  ? -16.967 10.562 58.253  1.00 14.33 ? 45  LEU A N   1 
ATOM   397  C CA  . LEU A 1 45  ? -16.733 9.696  57.102  1.00 17.53 ? 45  LEU A CA  1 
ATOM   398  C C   . LEU A 1 45  ? -17.968 8.895  56.704  1.00 18.80 ? 45  LEU A C   1 
ATOM   399  O O   . LEU A 1 45  ? -18.011 8.362  55.589  1.00 17.82 ? 45  LEU A O   1 
ATOM   400  C CB  . LEU A 1 45  ? -15.571 8.747  57.399  1.00 16.36 ? 45  LEU A CB  1 
ATOM   401  C CG  . LEU A 1 45  ? -14.196 9.413  57.498  1.00 11.92 ? 45  LEU A CG  1 
ATOM   402  C CD1 . LEU A 1 45  ? -13.192 8.457  58.158  1.00 13.00 ? 45  LEU A CD1 1 
ATOM   403  C CD2 . LEU A 1 45  ? -13.701 9.839  56.123  1.00 13.20 ? 45  LEU A CD2 1 
ATOM   404  N N   . LYS A 1 46  ? -18.966 8.800  57.585  1.00 14.16 ? 46  LYS A N   1 
ATOM   405  C CA  . LYS A 1 46  ? -20.250 8.215  57.196  1.00 18.19 ? 46  LYS A CA  1 
ATOM   406  C C   . LYS A 1 46  ? -20.984 9.089  56.194  1.00 21.30 ? 46  LYS A C   1 
ATOM   407  O O   . LYS A 1 46  ? -21.761 8.583  55.371  1.00 20.00 ? 46  LYS A O   1 
ATOM   408  C CB  . LYS A 1 46  ? -21.136 8.023  58.422  1.00 17.45 ? 46  LYS A CB  1 
ATOM   409  C CG  . LYS A 1 46  ? -20.682 6.941  59.384  1.00 22.86 ? 46  LYS A CG  1 
ATOM   410  C CD  . LYS A 1 46  ? -21.702 6.829  60.516  1.00 36.76 ? 46  LYS A CD  1 
ATOM   411  C CE  . LYS A 1 46  ? -21.360 5.714  61.482  1.00 48.32 ? 46  LYS A CE  1 
ATOM   412  N NZ  . LYS A 1 46  ? -21.499 4.371  60.843  1.00 56.79 ? 46  LYS A NZ  1 
ATOM   413  N N   . ASP A 1 47  ? -20.771 10.400 56.255  1.00 19.69 ? 47  ASP A N   1 
ATOM   414  C CA  . ASP A 1 47  ? -21.543 11.337 55.459  1.00 19.11 ? 47  ASP A CA  1 
ATOM   415  C C   . ASP A 1 47  ? -20.786 11.931 54.286  1.00 19.67 ? 47  ASP A C   1 
ATOM   416  O O   . ASP A 1 47  ? -21.430 12.463 53.376  1.00 21.27 ? 47  ASP A O   1 
ATOM   417  C CB  . ASP A 1 47  ? -22.049 12.483 56.342  1.00 20.43 ? 47  ASP A CB  1 
ATOM   418  C CG  . ASP A 1 47  ? -22.984 12.000 57.414  1.00 26.41 ? 47  ASP A CG  1 
ATOM   419  O OD1 . ASP A 1 47  ? -23.677 10.990 57.164  1.00 26.67 ? 47  ASP A OD1 1 
ATOM   420  O OD2 . ASP A 1 47  ? -23.017 12.605 58.502  1.00 28.97 ? 47  ASP A OD2 1 
ATOM   421  N N   . PHE A 1 48  ? -19.455 11.864 54.275  1.00 17.37 ? 48  PHE A N   1 
ATOM   422  C CA  . PHE A 1 48  ? -18.662 12.544 53.255  1.00 18.39 ? 48  PHE A CA  1 
ATOM   423  C C   . PHE A 1 48  ? -17.691 11.557 52.628  1.00 15.51 ? 48  PHE A C   1 
ATOM   424  O O   . PHE A 1 48  ? -16.987 10.835 53.345  1.00 19.69 ? 48  PHE A O   1 
ATOM   425  C CB  . PHE A 1 48  ? -17.912 13.751 53.848  1.00 17.77 ? 48  PHE A CB  1 
ATOM   426  C CG  . PHE A 1 48  ? -18.830 14.802 54.390  1.00 18.39 ? 48  PHE A CG  1 
ATOM   427  C CD1 . PHE A 1 48  ? -19.502 15.658 53.528  1.00 19.67 ? 48  PHE A CD1 1 
ATOM   428  C CD2 . PHE A 1 48  ? -19.073 14.891 55.744  1.00 20.33 ? 48  PHE A CD2 1 
ATOM   429  C CE1 . PHE A 1 48  ? -20.378 16.599 54.015  1.00 24.52 ? 48  PHE A CE1 1 
ATOM   430  C CE2 . PHE A 1 48  ? -19.946 15.828 56.247  1.00 17.83 ? 48  PHE A CE2 1 
ATOM   431  C CZ  . PHE A 1 48  ? -20.600 16.693 55.378  1.00 23.54 ? 48  PHE A CZ  1 
ATOM   432  N N   . GLU A 1 49  ? -17.663 11.523 51.294  1.00 16.83 ? 49  GLU A N   1 
ATOM   433  C CA  . GLU A 1 49  ? -16.834 10.576 50.543  1.00 18.44 ? 49  GLU A CA  1 
ATOM   434  C C   . GLU A 1 49  ? -15.421 11.142 50.380  1.00 19.78 ? 49  GLU A C   1 
ATOM   435  O O   . GLU A 1 49  ? -14.980 11.540 49.296  1.00 21.44 ? 49  GLU A O   1 
ATOM   436  C CB  . GLU A 1 49  ? -17.476 10.241 49.199  1.00 25.05 ? 49  GLU A CB  1 
ATOM   437  C CG  . GLU A 1 49  ? -18.684 9.313  49.339  1.00 35.39 ? 49  GLU A CG  1 
ATOM   438  C CD  . GLU A 1 49  ? -18.293 7.890  49.759  1.00 48.07 ? 49  GLU A CD  1 
ATOM   439  O OE1 . GLU A 1 49  ? -17.301 7.347  49.221  1.00 51.48 ? 49  GLU A OE1 1 
ATOM   440  O OE2 . GLU A 1 49  ? -18.962 7.324  50.653  1.00 51.74 ? 49  GLU A OE2 1 
ATOM   441  N N   . ILE A 1 50  ? -14.714 11.191 51.509  1.00 16.94 ? 50  ILE A N   1 
ATOM   442  C CA  . ILE A 1 50  ? -13.315 11.586 51.567  1.00 15.63 ? 50  ILE A CA  1 
ATOM   443  C C   . ILE A 1 50  ? -12.570 10.576 52.435  1.00 15.84 ? 50  ILE A C   1 
ATOM   444  O O   . ILE A 1 50  ? -13.162 9.671  53.026  1.00 17.44 ? 50  ILE A O   1 
ATOM   445  C CB  . ILE A 1 50  ? -13.127 13.013 52.126  1.00 17.74 ? 50  ILE A CB  1 
ATOM   446  C CG1 . ILE A 1 50  ? -13.769 13.138 53.519  1.00 19.54 ? 50  ILE A CG1 1 
ATOM   447  C CG2 . ILE A 1 50  ? -13.706 14.049 51.174  1.00 20.58 ? 50  ILE A CG2 1 
ATOM   448  C CD1 . ILE A 1 50  ? -13.430 14.451 54.204  1.00 19.24 ? 50  ILE A CD1 1 
ATOM   449  N N   . LYS A 1 51  ? -11.253 10.744 52.495  1.00 15.55 ? 51  LYS A N   1 
ATOM   450  C CA  . LYS A 1 51  ? -10.385 9.987  53.387  1.00 14.81 ? 51  LYS A CA  1 
ATOM   451  C C   . LYS A 1 51  ? -9.926  10.897 54.513  1.00 15.63 ? 51  LYS A C   1 
ATOM   452  O O   . LYS A 1 51  ? -9.561  12.056 54.266  1.00 16.77 ? 51  LYS A O   1 
ATOM   453  C CB  . LYS A 1 51  ? -9.150  9.444  52.655  1.00 14.26 ? 51  LYS A CB  1 
ATOM   454  C CG  . LYS A 1 51  ? -9.437  8.652  51.388  1.00 17.77 ? 51  LYS A CG  1 
ATOM   455  C CD  . LYS A 1 51  ? -10.302 7.449  51.683  1.00 19.64 ? 51  LYS A CD  1 
ATOM   456  C CE  . LYS A 1 51  ? -10.257 6.489  50.505  1.00 28.47 ? 51  LYS A CE  1 
ATOM   457  N NZ  . LYS A 1 51  ? -10.758 7.164  49.295  1.00 31.86 ? 51  LYS A NZ  1 
ATOM   458  N N   . LEU A 1 52  ? -9.947  10.369 55.747  1.00 11.76 ? 52  LEU A N   1 
ATOM   459  C CA  . LEU A 1 52  ? -9.425  11.062 56.921  1.00 11.24 ? 52  LEU A CA  1 
ATOM   460  C C   . LEU A 1 52  ? -8.665  10.068 57.786  1.00 16.47 ? 52  LEU A C   1 
ATOM   461  O O   . LEU A 1 52  ? -9.136  8.952  57.994  1.00 14.77 ? 52  LEU A O   1 
ATOM   462  C CB  . LEU A 1 52  ? -10.546 11.673 57.770  1.00 12.21 ? 52  LEU A CB  1 
ATOM   463  C CG  . LEU A 1 52  ? -11.455 12.698 57.109  1.00 13.94 ? 52  LEU A CG  1 
ATOM   464  C CD1 . LEU A 1 52  ? -12.584 12.990 58.062  1.00 13.51 ? 52  LEU A CD1 1 
ATOM   465  C CD2 . LEU A 1 52  ? -10.667 13.974 56.788  1.00 13.95 ? 52  LEU A CD2 1 
ATOM   466  N N   . ASN A 1 53  ? -7.528  10.479 58.334  1.00 13.73 ? 53  ASN A N   1 
ATOM   467  C CA  . ASN A 1 53  ? -6.714  9.574  59.136  1.00 14.79 ? 53  ASN A CA  1 
ATOM   468  C C   . ASN A 1 53  ? -6.679  10.046 60.579  1.00 12.90 ? 53  ASN A C   1 
ATOM   469  O O   . ASN A 1 53  ? -6.886  11.222 60.872  1.00 10.35 ? 53  ASN A O   1 
ATOM   470  C CB  . ASN A 1 53  ? -5.296  9.503  58.581  1.00 11.84 ? 53  ASN A CB  1 
ATOM   471  C CG  . ASN A 1 53  ? -5.287  9.192  57.123  1.00 13.71 ? 53  ASN A CG  1 
ATOM   472  O OD1 . ASN A 1 53  ? -5.591  8.077  56.722  1.00 14.39 ? 53  ASN A OD1 1 
ATOM   473  N ND2 . ASN A 1 53  ? -5.045  10.214 56.303  1.00 14.68 ? 53  ASN A ND2 1 
ATOM   474  N N   . PHE A 1 54  ? -6.397  9.109  61.480  1.00 8.79  ? 54  PHE A N   1 
ATOM   475  C CA  . PHE A 1 54  ? -6.455  9.380  62.910  1.00 10.09 ? 54  PHE A CA  1 
ATOM   476  C C   . PHE A 1 54  ? -5.295  8.707  63.620  1.00 11.64 ? 54  PHE A C   1 
ATOM   477  O O   . PHE A 1 54  ? -4.887  7.594  63.262  1.00 14.05 ? 54  PHE A O   1 
ATOM   478  C CB  . PHE A 1 54  ? -7.793  8.881  63.505  1.00 12.95 ? 54  PHE A CB  1 
ATOM   479  C CG  . PHE A 1 54  ? -8.978  9.522  62.876  1.00 12.53 ? 54  PHE A CG  1 
ATOM   480  C CD1 . PHE A 1 54  ? -9.457  10.737 63.359  1.00 11.50 ? 54  PHE A CD1 1 
ATOM   481  C CD2 . PHE A 1 54  ? -9.566  8.967  61.748  1.00 11.05 ? 54  PHE A CD2 1 
ATOM   482  C CE1 . PHE A 1 54  ? -10.529 11.356 62.742  1.00 13.47 ? 54  PHE A CE1 1 
ATOM   483  C CE2 . PHE A 1 54  ? -10.633 9.598  61.126  1.00 11.56 ? 54  PHE A CE2 1 
ATOM   484  C CZ  . PHE A 1 54  ? -11.113 10.788 61.634  1.00 10.51 ? 54  PHE A CZ  1 
ATOM   485  N N   . ASN A 1 55  ? -4.785  9.398  64.633  1.00 11.42 ? 55  ASN A N   1 
ATOM   486  C CA  . ASN A 1 55  ? -3.866  8.850  65.627  1.00 7.96  ? 55  ASN A CA  1 
ATOM   487  C C   . ASN A 1 55  ? -4.614  8.696  66.940  1.00 10.07 ? 55  ASN A C   1 
ATOM   488  O O   . ASN A 1 55  ? -5.282  9.630  67.378  1.00 11.73 ? 55  ASN A O   1 
ATOM   489  C CB  . ASN A 1 55  ? -2.666  9.778  65.879  1.00 10.35 ? 55  ASN A CB  1 
ATOM   490  C CG  . ASN A 1 55  ? -1.594  9.111  66.721  1.00 12.51 ? 55  ASN A CG  1 
ATOM   491  O OD1 . ASN A 1 55  ? -1.060  8.073  66.338  1.00 13.42 ? 55  ASN A OD1 1 
ATOM   492  N ND2 . ASN A 1 55  ? -1.344  9.648  67.899  1.00 7.74  ? 55  ASN A ND2 1 
ATOM   493  N N   . LEU A 1 56  ? -4.507  7.524  67.566  1.00 8.90  ? 56  LEU A N   1 
ATOM   494  C CA  . LEU A 1 56  ? -5.073  7.298  68.891  1.00 9.41  ? 56  LEU A CA  1 
ATOM   495  C C   . LEU A 1 56  ? -3.954  6.867  69.825  1.00 11.55 ? 56  LEU A C   1 
ATOM   496  O O   . LEU A 1 56  ? -3.351  5.812  69.608  1.00 10.86 ? 56  LEU A O   1 
ATOM   497  C CB  . LEU A 1 56  ? -6.141  6.204  68.865  1.00 9.11  ? 56  LEU A CB  1 
ATOM   498  C CG  . LEU A 1 56  ? -7.363  6.398  67.975  1.00 12.19 ? 56  LEU A CG  1 
ATOM   499  C CD1 . LEU A 1 56  ? -8.210  5.124  68.038  1.00 12.79 ? 56  LEU A CD1 1 
ATOM   500  C CD2 . LEU A 1 56  ? -8.164  7.597  68.459  1.00 17.73 ? 56  LEU A CD2 1 
ATOM   501  N N   . THR A 1 57  ? -3.685  7.650  70.880  1.00 9.26  ? 57  THR A N   1 
ATOM   502  C CA  . THR A 1 57  ? -2.642  7.201  71.796  1.00 8.67  ? 57  THR A CA  1 
ATOM   503  C C   . THR A 1 57  ? -3.155  6.033  72.635  1.00 10.51 ? 57  THR A C   1 
ATOM   504  O O   . THR A 1 57  ? -4.356  5.924  72.912  1.00 9.75  ? 57  THR A O   1 
ATOM   505  C CB  . THR A 1 57  ? -2.143  8.316  72.716  1.00 8.59  ? 57  THR A CB  1 
ATOM   506  O OG1 . THR A 1 57  ? -3.181  8.727  73.610  1.00 7.41  ? 57  THR A OG1 1 
ATOM   507  C CG2 . THR A 1 57  ? -1.635  9.523  71.908  1.00 9.17  ? 57  THR A CG2 1 
ATOM   508  N N   . PRO A 1 58  ? -2.269  5.119  73.021  1.00 8.59  ? 58  PRO A N   1 
ATOM   509  C CA  . PRO A 1 58  ? -2.739  3.965  73.800  1.00 10.37 ? 58  PRO A CA  1 
ATOM   510  C C   . PRO A 1 58  ? -3.341  4.357  75.137  1.00 15.01 ? 58  PRO A C   1 
ATOM   511  O O   . PRO A 1 58  ? -4.333  3.744  75.555  1.00 13.31 ? 58  PRO A O   1 
ATOM   512  C CB  . PRO A 1 58  ? -1.469  3.122  73.951  1.00 9.59  ? 58  PRO A CB  1 
ATOM   513  C CG  . PRO A 1 58  ? -0.701  3.424  72.701  1.00 8.52  ? 58  PRO A CG  1 
ATOM   514  C CD  . PRO A 1 58  ? -0.895  4.922  72.519  1.00 9.33  ? 58  PRO A CD  1 
ATOM   515  N N   . VAL A 1 59  ? -2.783  5.368  75.815  1.00 11.86 ? 59  VAL A N   1 
ATOM   516  C CA  . VAL A 1 59  ? -3.351  5.773  77.097  1.00 11.31 ? 59  VAL A CA  1 
ATOM   517  C C   . VAL A 1 59  ? -4.749  6.370  76.894  1.00 12.51 ? 59  VAL A C   1 
ATOM   518  O O   . VAL A 1 59  ? -5.624  6.215  77.760  1.00 11.18 ? 59  VAL A O   1 
ATOM   519  C CB  . VAL A 1 59  ? -2.385  6.728  77.846  1.00 10.17 ? 59  VAL A CB  1 
ATOM   520  C CG1 . VAL A 1 59  ? -2.081  8.004  77.023  1.00 9.27  ? 59  VAL A CG1 1 
ATOM   521  C CG2 . VAL A 1 59  ? -2.943  7.112  79.226  1.00 11.87 ? 59  VAL A CG2 1 
ATOM   522  N N   . LEU A 1 60  ? -5.007  7.037  75.758  1.00 7.96  ? 60  LEU A N   1 
ATOM   523  C CA  . LEU A 1 60  ? -6.378  7.481  75.489  1.00 9.18  ? 60  LEU A CA  1 
ATOM   524  C C   . LEU A 1 60  ? -7.296  6.280  75.303  1.00 14.21 ? 60  LEU A C   1 
ATOM   525  O O   . LEU A 1 60  ? -8.394  6.221  75.877  1.00 11.67 ? 60  LEU A O   1 
ATOM   526  C CB  . LEU A 1 60  ? -6.439  8.381  74.248  1.00 7.92  ? 60  LEU A CB  1 
ATOM   527  C CG  . LEU A 1 60  ? -7.877  8.739  73.837  1.00 12.03 ? 60  LEU A CG  1 
ATOM   528  C CD1 . LEU A 1 60  ? -8.620  9.470  74.964  1.00 11.43 ? 60  LEU A CD1 1 
ATOM   529  C CD2 . LEU A 1 60  ? -7.911  9.577  72.534  1.00 8.99  ? 60  LEU A CD2 1 
ATOM   530  N N   . ILE A 1 61  ? -6.851  5.299  74.511  1.00 10.90 ? 61  ILE A N   1 
ATOM   531  C CA  . ILE A 1 61  ? -7.679  4.119  74.267  1.00 9.69  ? 61  ILE A CA  1 
ATOM   532  C C   . ILE A 1 61  ? -8.026  3.428  75.577  1.00 11.29 ? 61  ILE A C   1 
ATOM   533  O O   . ILE A 1 61  ? -9.174  3.020  75.783  1.00 10.94 ? 61  ILE A O   1 
ATOM   534  C CB  . ILE A 1 61  ? -6.983  3.147  73.304  1.00 12.31 ? 61  ILE A CB  1 
ATOM   535  C CG1 . ILE A 1 61  ? -6.861  3.776  71.915  1.00 12.71 ? 61  ILE A CG1 1 
ATOM   536  C CG2 . ILE A 1 61  ? -7.780  1.826  73.225  1.00 13.83 ? 61  ILE A CG2 1 
ATOM   537  C CD1 . ILE A 1 61  ? -5.944  2.970  70.967  1.00 13.87 ? 61  ILE A CD1 1 
ATOM   538  N N   . ASP A 1 62  ? -7.051  3.292  76.488  1.00 10.05 ? 62  ASP A N   1 
ATOM   539  C CA  . ASP A 1 62  ? -7.343  2.655  77.776  1.00 11.96 ? 62  ASP A CA  1 
ATOM   540  C C   . ASP A 1 62  ? -8.497  3.343  78.493  1.00 11.76 ? 62  ASP A C   1 
ATOM   541  O O   . ASP A 1 62  ? -9.352  2.679  79.099  1.00 12.92 ? 62  ASP A O   1 
ATOM   542  C CB  . ASP A 1 62  ? -6.121  2.673  78.695  1.00 11.01 ? 62  ASP A CB  1 
ATOM   543  C CG  . ASP A 1 62  ? -5.064  1.688  78.295  1.00 19.12 ? 62  ASP A CG  1 
ATOM   544  O OD1 . ASP A 1 62  ? -5.403  0.674  77.653  1.00 17.95 ? 62  ASP A OD1 1 
ATOM   545  O OD2 . ASP A 1 62  ? -3.889  1.917  78.651  1.00 21.48 ? 62  ASP A OD2 1 
ATOM   546  N N   . GLN A 1 63  ? -8.509  4.671  78.485  1.00 11.10 ? 63  GLN A N   1 
ATOM   547  C CA  . GLN A 1 63  ? -9.542  5.387  79.226  1.00 11.51 ? 63  GLN A CA  1 
ATOM   548  C C   . GLN A 1 63  ? -10.879 5.317  78.510  1.00 12.85 ? 63  GLN A C   1 
ATOM   549  O O   . GLN A 1 63  ? -11.919 5.159  79.162  1.00 12.85 ? 63  GLN A O   1 
ATOM   550  C CB  . GLN A 1 63  ? -9.130  6.846  79.467  1.00 11.26 ? 63  GLN A CB  1 
ATOM   551  C CG  . GLN A 1 63  ? -7.747  7.025  80.068  1.00 12.01 ? 63  GLN A CG  1 
ATOM   552  C CD  . GLN A 1 63  ? -7.362  8.487  80.126  1.00 15.45 ? 63  GLN A CD  1 
ATOM   553  O OE1 . GLN A 1 63  ? -8.025  9.296  80.777  1.00 16.64 ? 63  GLN A OE1 1 
ATOM   554  N NE2 . GLN A 1 63  ? -6.353  8.855  79.336  1.00 10.75 ? 63  GLN A NE2 1 
ATOM   555  N N   . ILE A 1 64  ? -10.880 5.438  77.179  1.00 13.83 ? 64  ILE A N   1 
ATOM   556  C CA  . ILE A 1 64  ? -12.123 5.268  76.440  1.00 10.27 ? 64  ILE A CA  1 
ATOM   557  C C   . ILE A 1 64  ? -12.745 3.923  76.788  1.00 12.11 ? 64  ILE A C   1 
ATOM   558  O O   . ILE A 1 64  ? -13.955 3.821  77.029  1.00 12.08 ? 64  ILE A O   1 
ATOM   559  C CB  . ILE A 1 64  ? -11.876 5.418  74.927  1.00 12.39 ? 64  ILE A CB  1 
ATOM   560  C CG1 . ILE A 1 64  ? -11.529 6.871  74.581  1.00 11.35 ? 64  ILE A CG1 1 
ATOM   561  C CG2 . ILE A 1 64  ? -13.099 4.987  74.145  1.00 13.38 ? 64  ILE A CG2 1 
ATOM   562  C CD1 . ILE A 1 64  ? -11.199 7.123  73.120  1.00 12.15 ? 64  ILE A CD1 1 
ATOM   563  N N   . GLN A 1 65  ? -11.917 2.878  76.866  1.00 14.39 ? 65  GLN A N   1 
ATOM   564  C CA  . GLN A 1 65  ? -12.434 1.553  77.195  1.00 13.20 ? 65  GLN A CA  1 
ATOM   565  C C   . GLN A 1 65  ? -13.049 1.524  78.589  1.00 17.11 ? 65  GLN A C   1 
ATOM   566  O O   . GLN A 1 65  ? -14.102 0.907  78.802  1.00 15.40 ? 65  GLN A O   1 
ATOM   567  C CB  . GLN A 1 65  ? -11.317 0.522  77.100  1.00 17.23 ? 65  GLN A CB  1 
ATOM   568  C CG  . GLN A 1 65  ? -11.071 0.028  75.692  1.00 20.24 ? 65  GLN A CG  1 
ATOM   569  C CD  . GLN A 1 65  ? -9.837  -0.839 75.612  1.00 26.96 ? 65  GLN A CD  1 
ATOM   570  O OE1 . GLN A 1 65  ? -8.806  -0.537 76.218  1.00 24.80 ? 65  GLN A OE1 1 
ATOM   571  N NE2 . GLN A 1 65  ? -9.969  -1.979 74.950  1.00 34.73 ? 65  GLN A NE2 1 
ATOM   572  N N   . GLU A 1 66  ? -12.400 2.181  79.554  1.00 15.99 ? 66  GLU A N   1 
ATOM   573  C CA  . GLU A 1 66  ? -12.902 2.147  80.922  1.00 15.65 ? 66  GLU A CA  1 
ATOM   574  C C   . GLU A 1 66  ? -14.242 2.868  81.029  1.00 14.83 ? 66  GLU A C   1 
ATOM   575  O O   . GLU A 1 66  ? -15.160 2.382  81.702  1.00 15.87 ? 66  GLU A O   1 
ATOM   576  C CB  . GLU A 1 66  ? -11.854 2.744  81.874  1.00 16.17 ? 66  GLU A CB  1 
ATOM   577  C CG  . GLU A 1 66  ? -12.197 2.574  83.350  1.00 25.28 ? 66  GLU A CG  1 
ATOM   578  C CD  . GLU A 1 66  ? -11.030 2.870  84.293  1.00 26.27 ? 66  GLU A CD  1 
ATOM   579  O OE1 . GLU A 1 66  ? -9.898  3.103  83.809  1.00 23.04 ? 66  GLU A OE1 1 
ATOM   580  O OE2 . GLU A 1 66  ? -11.253 2.867  85.525  1.00 27.78 ? 66  GLU A OE2 1 
ATOM   581  N N   . TYR A 1 67  ? -14.390 3.996  80.330  1.00 12.93 ? 67  TYR A N   1 
ATOM   582  C CA  . TYR A 1 67  ? -15.677 4.685  80.295  1.00 14.19 ? 67  TYR A CA  1 
ATOM   583  C C   . TYR A 1 67  ? -16.740 3.828  79.613  1.00 16.63 ? 67  TYR A C   1 
ATOM   584  O O   . TYR A 1 67  ? -17.869 3.714  80.104  1.00 17.03 ? 67  TYR A O   1 
ATOM   585  C CB  . TYR A 1 67  ? -15.545 6.034  79.576  1.00 12.47 ? 67  TYR A CB  1 
ATOM   586  C CG  . TYR A 1 67  ? -15.076 7.158  80.463  1.00 11.85 ? 67  TYR A CG  1 
ATOM   587  C CD1 . TYR A 1 67  ? -15.961 7.863  81.273  1.00 10.68 ? 67  TYR A CD1 1 
ATOM   588  C CD2 . TYR A 1 67  ? -13.735 7.509  80.491  1.00 12.35 ? 67  TYR A CD2 1 
ATOM   589  C CE1 . TYR A 1 67  ? -15.505 8.905  82.105  1.00 11.90 ? 67  TYR A CE1 1 
ATOM   590  C CE2 . TYR A 1 67  ? -13.275 8.527  81.294  1.00 16.96 ? 67  TYR A CE2 1 
ATOM   591  C CZ  . TYR A 1 67  ? -14.150 9.226  82.093  1.00 15.57 ? 67  TYR A CZ  1 
ATOM   592  O OH  . TYR A 1 67  ? -13.624 10.246 82.862  1.00 14.95 ? 67  TYR A OH  1 
ATOM   593  N N   . ALA A 1 68  ? -16.392 3.225  78.469  1.00 12.68 ? 68  ALA A N   1 
ATOM   594  C CA  . ALA A 1 68  ? -17.341 2.399  77.717  1.00 16.76 ? 68  ALA A CA  1 
ATOM   595  C C   . ALA A 1 68  ? -17.819 1.196  78.527  1.00 22.61 ? 68  ALA A C   1 
ATOM   596  O O   . ALA A 1 68  ? -18.963 0.746  78.362  1.00 19.79 ? 68  ALA A O   1 
ATOM   597  C CB  . ALA A 1 68  ? -16.697 1.932  76.406  1.00 14.18 ? 68  ALA A CB  1 
ATOM   598  N N   . GLN A 1 69  ? -16.964 0.657  79.393  1.00 17.74 ? 69  GLN A N   1 
ATOM   599  C CA  . GLN A 1 69  ? -17.295 -0.515 80.192  1.00 20.50 ? 69  GLN A CA  1 
ATOM   600  C C   . GLN A 1 69  ? -18.051 -0.159 81.460  1.00 25.76 ? 69  GLN A C   1 
ATOM   601  O O   . GLN A 1 69  ? -18.462 -1.068 82.189  1.00 29.37 ? 69  GLN A O   1 
ATOM   602  C CB  . GLN A 1 69  ? -16.012 -1.287 80.532  1.00 26.26 ? 69  GLN A CB  1 
ATOM   603  C CG  . GLN A 1 69  ? -15.326 -1.897 79.297  1.00 28.69 ? 69  GLN A CG  1 
ATOM   604  C CD  . GLN A 1 69  ? -13.893 -2.371 79.557  1.00 35.37 ? 69  GLN A CD  1 
ATOM   605  O OE1 . GLN A 1 69  ? -13.391 -2.293 80.674  1.00 39.27 ? 69  GLN A OE1 1 
ATOM   606  N NE2 . GLN A 1 69  ? -13.223 -2.829 78.507  1.00 35.24 ? 69  GLN A NE2 1 
ATOM   607  N N   . GLY A 1 70  ? -18.256 1.132  81.725  1.00 22.57 ? 70  GLY A N   1 
ATOM   608  C CA  . GLY A 1 70  ? -18.966 1.569  82.913  1.00 26.80 ? 70  GLY A CA  1 
ATOM   609  C C   . GLY A 1 70  ? -18.141 1.593  84.178  1.00 32.42 ? 70  GLY A C   1 
ATOM   610  O O   . GLY A 1 70  ? -18.703 1.673  85.273  1.00 33.03 ? 70  GLY A O   1 
ATOM   611  N N   . LYS A 1 71  ? -16.813 1.546  84.063  1.00 31.58 ? 71  LYS A N   1 
ATOM   612  C CA  . LYS A 1 71  ? -15.943 1.376  85.214  1.00 31.74 ? 71  LYS A CA  1 
ATOM   613  C C   . LYS A 1 71  ? -15.219 2.649  85.622  1.00 30.88 ? 71  LYS A C   1 
ATOM   614  O O   . LYS A 1 71  ? -14.546 2.648  86.657  1.00 32.41 ? 71  LYS A O   1 
ATOM   615  C CB  . LYS A 1 71  ? -14.914 0.270  84.931  1.00 35.98 ? 71  LYS A CB  1 
ATOM   616  C CG  . LYS A 1 71  ? -15.536 -0.974 84.300  1.00 42.27 ? 71  LYS A CG  1 
ATOM   617  C CD  . LYS A 1 71  ? -14.659 -2.204 84.425  1.00 43.61 ? 71  LYS A CD  1 
ATOM   618  C CE  . LYS A 1 71  ? -13.336 -2.031 83.717  1.00 42.93 ? 71  LYS A CE  1 
ATOM   619  N NZ  . LYS A 1 71  ? -12.561 -3.312 83.683  1.00 47.55 ? 71  LYS A NZ  1 
ATOM   620  N N   . ALA A 1 72  ? -15.339 3.728  84.853  1.00 21.42 ? 72  ALA A N   1 
ATOM   621  C CA  . ALA A 1 72  ? -14.635 4.962  85.170  1.00 17.97 ? 72  ALA A CA  1 
ATOM   622  C C   . ALA A 1 72  ? -15.377 5.723  86.266  1.00 25.80 ? 72  ALA A C   1 
ATOM   623  O O   . ALA A 1 72  ? -16.555 6.056  86.107  1.00 23.20 ? 72  ALA A O   1 
ATOM   624  C CB  . ALA A 1 72  ? -14.489 5.827  83.916  1.00 16.45 ? 72  ALA A CB  1 
ATOM   625  N N   . LYS A 1 73  ? -14.691 5.988  87.382  1.00 17.84 ? 73  LYS A N   1 
ATOM   626  C CA  . LYS A 1 73  ? -15.249 6.795  88.469  1.00 19.75 ? 73  LYS A CA  1 
ATOM   627  C C   . LYS A 1 73  ? -14.789 8.236  88.264  1.00 21.48 ? 73  LYS A C   1 
ATOM   628  O O   . LYS A 1 73  ? -13.713 8.640  88.710  1.00 22.72 ? 73  LYS A O   1 
ATOM   629  C CB  . LYS A 1 73  ? -14.800 6.264  89.825  1.00 23.23 ? 73  LYS A CB  1 
ATOM   630  C CG  . LYS A 1 73  ? -15.238 4.846  90.124  1.00 33.01 ? 73  LYS A CG  1 
ATOM   631  C CD  . LYS A 1 73  ? -14.930 4.462  91.566  1.00 42.53 ? 73  LYS A CD  1 
ATOM   632  C CE  . LYS A 1 73  ? -13.444 4.176  91.773  1.00 45.95 ? 73  LYS A CE  1 
ATOM   633  N NZ  . LYS A 1 73  ? -13.175 3.745  93.182  1.00 50.13 ? 73  LYS A NZ  1 
ATOM   634  N N   . ASP A 1 74  ? -15.623 9.026  87.603  1.00 15.08 ? 74  ASP A N   1 
ATOM   635  C CA  . ASP A 1 74  ? -15.264 10.377 87.184  1.00 12.70 ? 74  ASP A CA  1 
ATOM   636  C C   . ASP A 1 74  ? -15.889 11.368 88.164  1.00 16.19 ? 74  ASP A C   1 
ATOM   637  O O   . ASP A 1 74  ? -17.115 11.508 88.209  1.00 16.89 ? 74  ASP A O   1 
ATOM   638  C CB  . ASP A 1 74  ? -15.739 10.587 85.747  1.00 16.49 ? 74  ASP A CB  1 
ATOM   639  C CG  . ASP A 1 74  ? -15.381 11.943 85.187  1.00 19.56 ? 74  ASP A CG  1 
ATOM   640  O OD1 . ASP A 1 74  ? -15.414 12.954 85.926  1.00 17.49 ? 74  ASP A OD1 1 
ATOM   641  O OD2 . ASP A 1 74  ? -15.023 11.976 83.989  1.00 17.38 ? 74  ASP A OD2 1 
ATOM   642  N N   . VAL A 1 75  ? -15.045 12.070 88.931  1.00 13.11 ? 75  VAL A N   1 
ATOM   643  C CA  . VAL A 1 75  ? -15.554 12.858 90.057  1.00 19.30 ? 75  VAL A CA  1 
ATOM   644  C C   . VAL A 1 75  ? -16.370 14.052 89.569  1.00 19.08 ? 75  VAL A C   1 
ATOM   645  O O   . VAL A 1 75  ? -17.416 14.384 90.150  1.00 16.66 ? 75  VAL A O   1 
ATOM   646  C CB  . VAL A 1 75  ? -14.411 13.281 91.007  1.00 27.55 ? 75  VAL A CB  1 
ATOM   647  C CG1 . VAL A 1 75  ? -13.664 12.044 91.505  1.00 29.10 ? 75  VAL A CG1 1 
ATOM   648  C CG2 . VAL A 1 75  ? -13.447 14.274 90.360  1.00 30.43 ? 75  VAL A CG2 1 
ATOM   649  N N   A PHE A 1 76  ? -15.918 14.718 88.501  0.56 18.14 ? 76  PHE A N   1 
ATOM   650  N N   B PHE A 1 76  ? -15.926 14.703 88.496  0.44 18.23 ? 76  PHE A N   1 
ATOM   651  C CA  A PHE A 1 76  ? -16.684 15.834 87.957  0.56 19.22 ? 76  PHE A CA  1 
ATOM   652  C CA  B PHE A 1 76  ? -16.702 15.823 87.988  0.44 19.17 ? 76  PHE A CA  1 
ATOM   653  C C   A PHE A 1 76  ? -18.005 15.352 87.378  0.56 20.94 ? 76  PHE A C   1 
ATOM   654  C C   B PHE A 1 76  ? -18.011 15.350 87.379  0.44 20.58 ? 76  PHE A C   1 
ATOM   655  O O   A PHE A 1 76  ? -19.052 15.980 87.585  0.56 20.82 ? 76  PHE A O   1 
ATOM   656  O O   B PHE A 1 76  ? -19.054 15.992 87.552  0.44 20.74 ? 76  PHE A O   1 
ATOM   657  C CB  A PHE A 1 76  ? -15.876 16.579 86.888  0.56 20.73 ? 76  PHE A CB  1 
ATOM   658  C CB  B PHE A 1 76  ? -15.904 16.621 86.961  0.44 20.64 ? 76  PHE A CB  1 
ATOM   659  C CG  A PHE A 1 76  ? -14.910 17.585 87.448  0.56 18.00 ? 76  PHE A CG  1 
ATOM   660  C CG  B PHE A 1 76  ? -16.575 17.886 86.587  0.44 19.70 ? 76  PHE A CG  1 
ATOM   661  C CD1 A PHE A 1 76  ? -13.667 17.187 87.920  0.56 17.93 ? 76  PHE A CD1 1 
ATOM   662  C CD1 B PHE A 1 76  ? -16.467 18.992 87.405  0.44 19.22 ? 76  PHE A CD1 1 
ATOM   663  C CD2 A PHE A 1 76  ? -15.249 18.928 87.517  0.56 20.93 ? 76  PHE A CD2 1 
ATOM   664  C CD2 B PHE A 1 76  ? -17.378 17.956 85.458  0.44 17.29 ? 76  PHE A CD2 1 
ATOM   665  C CE1 A PHE A 1 76  ? -12.777 18.105 88.440  0.56 15.74 ? 76  PHE A CE1 1 
ATOM   666  C CE1 B PHE A 1 76  ? -17.115 20.152 87.088  0.44 17.14 ? 76  PHE A CE1 1 
ATOM   667  C CE2 A PHE A 1 76  ? -14.362 19.859 88.039  0.56 21.47 ? 76  PHE A CE2 1 
ATOM   668  C CE2 B PHE A 1 76  ? -18.025 19.118 85.135  0.44 18.33 ? 76  PHE A CE2 1 
ATOM   669  C CZ  A PHE A 1 76  ? -13.124 19.448 88.502  0.56 20.38 ? 76  PHE A CZ  1 
ATOM   670  C CZ  B PHE A 1 76  ? -17.898 20.217 85.954  0.44 21.30 ? 76  PHE A CZ  1 
ATOM   671  N N   . LEU A 1 77  ? -17.976 14.225 86.666  1.00 14.50 ? 77  LEU A N   1 
ATOM   672  C CA  . LEU A 1 77  ? -19.198 13.691 86.087  1.00 22.95 ? 77  LEU A CA  1 
ATOM   673  C C   . LEU A 1 77  ? -20.180 13.275 87.170  1.00 21.51 ? 77  LEU A C   1 
ATOM   674  O O   . LEU A 1 77  ? -21.397 13.413 86.995  1.00 18.85 ? 77  LEU A O   1 
ATOM   675  C CB  . LEU A 1 77  ? -18.841 12.532 85.167  1.00 14.78 ? 77  LEU A CB  1 
ATOM   676  C CG  . LEU A 1 77  ? -19.932 11.968 84.280  1.00 24.19 ? 77  LEU A CG  1 
ATOM   677  C CD1 . LEU A 1 77  ? -20.547 13.092 83.448  1.00 26.55 ? 77  LEU A CD1 1 
ATOM   678  C CD2 . LEU A 1 77  ? -19.316 10.911 83.386  1.00 24.12 ? 77  LEU A CD2 1 
ATOM   679  N N   . GLU A 1 78  ? -19.692 12.830 88.336  1.00 18.19 ? 78  GLU A N   1 
ATOM   680  C CA  . GLU A 1 78  ? -20.615 12.489 89.431  1.00 23.10 ? 78  GLU A CA  1 
ATOM   681  C C   . GLU A 1 78  ? -21.279 13.750 89.949  1.00 18.51 ? 78  GLU A C   1 
ATOM   682  O O   . GLU A 1 78  ? -22.380 13.693 90.366  1.00 20.28 ? 78  GLU A O   1 
ATOM   683  C CB  . GLU A 1 78  ? -19.989 11.804 90.647  1.00 37.13 ? 78  GLU A CB  1 
ATOM   684  C CG  . GLU A 1 78  ? -19.264 10.505 90.466  1.00 55.70 ? 78  GLU A CG  1 
ATOM   685  C CD  . GLU A 1 78  ? -20.084 9.379  89.911  1.00 68.69 ? 78  GLU A CD  1 
ATOM   686  O OE1 . GLU A 1 78  ? -21.319 9.501  89.861  1.00 69.92 ? 78  GLU A OE1 1 
ATOM   687  O OE2 . GLU A 1 78  ? -19.453 8.386  89.477  1.00 73.84 ? 78  GLU A OE2 1 
ATOM   688  N N   . ALA A 1 79  ? -20.582 14.873 89.938  1.00 18.07 ? 79  ALA A N   1 
ATOM   689  C CA  . ALA A 1 79  ? -21.213 16.126 90.344  1.00 19.90 ? 79  ALA A CA  1 
ATOM   690  C C   . ALA A 1 79  ? -22.262 16.583 89.333  1.00 21.35 ? 79  ALA A C   1 
ATOM   691  O O   . ALA A 1 79  ? -23.178 17.340 89.683  1.00 22.33 ? 79  ALA A O   1 
ATOM   692  C CB  . ALA A 1 79  ? -20.162 17.220 90.522  1.00 20.25 ? 79  ALA A CB  1 
ATOM   693  N N   . ILE A 1 80  ? -22.145 16.122 88.125  1.00 15.33 ? 80  ILE A N   1 
ATOM   694  C CA  . ILE A 1 80  ? -23.143 16.468 87.159  1.00 18.78 ? 80  ILE A CA  1 
ATOM   695  C C   . ILE A 1 80  ? -24.368 15.561 87.290  1.00 17.26 ? 80  ILE A C   1 
ATOM   696  O O   . ILE A 1 80  ? -25.469 16.014 87.168  1.00 15.36 ? 80  ILE A O   1 
ATOM   697  C CB  . ILE A 1 80  ? -22.592 16.391 85.717  1.00 13.97 ? 80  ILE A CB  1 
ATOM   698  C CG1 . ILE A 1 80  ? -21.741 17.607 85.435  1.00 20.25 ? 80  ILE A CG1 1 
ATOM   699  C CG2 . ILE A 1 80  ? -23.706 16.314 84.646  1.00 13.64 ? 80  ILE A CG2 1 
ATOM   700  C CD1 . ILE A 1 80  ? -20.801 17.402 84.302  1.00 29.35 ? 80  ILE A CD1 1 
ATOM   701  N N   . ARG A 1 81  ? -24.120 14.288 87.507  1.00 15.65 ? 81  ARG A N   1 
ATOM   702  C CA  . ARG A 1 81  ? -25.198 13.305 87.489  1.00 19.50 ? 81  ARG A CA  1 
ATOM   703  C C   . ARG A 1 81  ? -26.150 13.480 88.669  1.00 20.22 ? 81  ARG A C   1 
ATOM   704  O O   . ARG A 1 81  ? -27.365 13.287 88.527  1.00 19.45 ? 81  ARG A O   1 
ATOM   705  C CB  . ARG A 1 81  ? -24.596 11.899 87.501  1.00 19.78 ? 81  ARG A CB  1 
ATOM   706  C CG  . ARG A 1 81  ? -25.624 10.800 87.669  1.00 27.92 ? 81  ARG A CG  1 
ATOM   707  C CD  . ARG A 1 81  ? -24.992 9.416  87.672  1.00 39.65 ? 81  ARG A CD  1 
ATOM   708  N NE  . ARG A 1 81  ? -24.618 8.979  86.332  1.00 49.69 ? 81  ARG A NE  1 
ATOM   709  C CZ  . ARG A 1 81  ? -25.478 8.514  85.427  1.00 57.11 ? 81  ARG A CZ  1 
ATOM   710  N NH1 . ARG A 1 81  ? -26.776 8.435  85.709  1.00 54.48 ? 81  ARG A NH1 1 
ATOM   711  N NH2 . ARG A 1 81  ? -25.040 8.135  84.233  1.00 58.52 ? 81  ARG A NH2 1 
ATOM   712  N N   . LYS A 1 82  ? -25.611 13.810 89.847  1.00 16.30 ? 82  LYS A N   1 
ATOM   713  C CA  . LYS A 1 82  ? -26.402 13.823 91.073  1.00 14.71 ? 82  LYS A CA  1 
ATOM   714  C C   . LYS A 1 82  ? -27.544 14.822 90.985  1.00 20.14 ? 82  LYS A C   1 
ATOM   715  O O   . LYS A 1 82  ? -27.429 15.881 90.361  1.00 14.55 ? 82  LYS A O   1 
ATOM   716  C CB  . LYS A 1 82  ? -25.542 14.198 92.283  1.00 17.56 ? 82  LYS A CB  1 
ATOM   717  C CG  . LYS A 1 82  ? -24.526 13.187 92.744  1.00 26.30 ? 82  LYS A CG  1 
ATOM   718  C CD  . LYS A 1 82  ? -23.795 13.784 93.951  1.00 26.76 ? 82  LYS A CD  1 
ATOM   719  C CE  . LYS A 1 82  ? -22.688 12.897 94.475  1.00 34.53 ? 82  LYS A CE  1 
ATOM   720  N NZ  . LYS A 1 82  ? -22.115 13.492 95.710  1.00 34.44 ? 82  LYS A NZ  1 
ATOM   721  N N   . ASP A 1 83  ? -28.643 14.481 91.648  1.00 19.18 ? 83  ASP A N   1 
ATOM   722  C CA  . ASP A 1 83  ? -29.655 15.476 91.965  1.00 17.42 ? 83  ASP A CA  1 
ATOM   723  C C   . ASP A 1 83  ? -28.992 16.595 92.764  1.00 15.32 ? 83  ASP A C   1 
ATOM   724  O O   . ASP A 1 83  ? -28.168 16.316 93.645  1.00 15.25 ? 83  ASP A O   1 
ATOM   725  C CB  . ASP A 1 83  ? -30.797 14.821 92.752  1.00 21.58 ? 83  ASP A CB  1 
ATOM   726  C CG  . ASP A 1 83  ? -31.960 15.767 93.045  1.00 28.15 ? 83  ASP A CG  1 
ATOM   727  O OD1 . ASP A 1 83  ? -31.785 16.862 93.619  1.00 24.86 ? 83  ASP A OD1 1 
ATOM   728  O OD2 . ASP A 1 83  ? -33.076 15.422 92.602  1.00 32.39 ? 83  ASP A OD2 1 
ATOM   729  N N   . PRO A 1 84  ? -29.271 17.866 92.450  1.00 18.92 ? 84  PRO A N   1 
ATOM   730  C CA  . PRO A 1 84  ? -28.564 18.956 93.147  1.00 17.80 ? 84  PRO A CA  1 
ATOM   731  C C   . PRO A 1 84  ? -28.729 18.934 94.656  1.00 16.90 ? 84  PRO A C   1 
ATOM   732  O O   . PRO A 1 84  ? -27.844 19.432 95.363  1.00 18.01 ? 84  PRO A O   1 
ATOM   733  C CB  . PRO A 1 84  ? -29.174 20.222 92.528  1.00 19.88 ? 84  PRO A CB  1 
ATOM   734  C CG  . PRO A 1 84  ? -29.601 19.787 91.155  1.00 18.31 ? 84  PRO A CG  1 
ATOM   735  C CD  . PRO A 1 84  ? -30.088 18.363 91.326  1.00 23.06 ? 84  PRO A CD  1 
ATOM   736  N N   . ASP A 1 85  ? -29.827 18.357 95.168  1.00 17.07 ? 85  ASP A N   1 
ATOM   737  C CA  . ASP A 1 85  ? -30.026 18.233 96.611  1.00 20.47 ? 85  ASP A CA  1 
ATOM   738  C C   . ASP A 1 85  ? -28.980 17.338 97.261  1.00 16.81 ? 85  ASP A C   1 
ATOM   739  O O   . ASP A 1 85  ? -28.775 17.426 98.479  1.00 20.83 ? 85  ASP A O   1 
ATOM   740  C CB  . ASP A 1 85  ? -31.414 17.664 96.929  1.00 21.56 ? 85  ASP A CB  1 
ATOM   741  C CG  . ASP A 1 85  ? -32.535 18.653 96.667  1.00 31.68 ? 85  ASP A CG  1 
ATOM   742  O OD1 . ASP A 1 85  ? -32.272 19.874 96.675  1.00 32.77 ? 85  ASP A OD1 1 
ATOM   743  O OD2 . ASP A 1 85  ? -33.687 18.206 96.475  1.00 35.55 ? 85  ASP A OD2 1 
ATOM   744  N N   . ASP A 1 86  ? -28.334 16.471 96.478  1.00 16.20 ? 86  ASP A N   1 
ATOM   745  C CA  . ASP A 1 86  ? -27.302 15.560 96.963  1.00 21.84 ? 86  ASP A CA  1 
ATOM   746  C C   . ASP A 1 86  ? -25.890 16.079 96.733  1.00 18.39 ? 86  ASP A C   1 
ATOM   747  O O   . ASP A 1 86  ? -24.923 15.393 97.096  1.00 22.25 ? 86  ASP A O   1 
ATOM   748  C CB  . ASP A 1 86  ? -27.463 14.193 96.292  1.00 22.49 ? 86  ASP A CB  1 
ATOM   749  C CG  . ASP A 1 86  ? -28.774 13.511 96.680  1.00 28.33 ? 86  ASP A CG  1 
ATOM   750  O OD1 . ASP A 1 86  ? -29.183 13.640 97.850  1.00 34.57 ? 86  ASP A OD1 1 
ATOM   751  O OD2 . ASP A 1 86  ? -29.409 12.891 95.808  1.00 33.92 ? 86  ASP A OD2 1 
ATOM   752  N N   . LEU A 1 87  ? -25.739 17.258 96.138  1.00 15.46 ? 87  LEU A N   1 
ATOM   753  C CA  . LEU A 1 87  ? -24.402 17.777 95.860  1.00 17.71 ? 87  LEU A CA  1 
ATOM   754  C C   . LEU A 1 87  ? -23.693 18.193 97.147  1.00 15.13 ? 87  LEU A C   1 
ATOM   755  O O   . LEU A 1 87  ? -24.260 18.895 97.991  1.00 16.36 ? 87  LEU A O   1 
ATOM   756  C CB  . LEU A 1 87  ? -24.483 18.972 94.911  1.00 17.35 ? 87  LEU A CB  1 
ATOM   757  C CG  . LEU A 1 87  ? -24.816 18.671 93.455  1.00 17.48 ? 87  LEU A CG  1 
ATOM   758  C CD1 . LEU A 1 87  ? -25.083 19.973 92.713  1.00 19.18 ? 87  LEU A CD1 1 
ATOM   759  C CD2 . LEU A 1 87  ? -23.664 17.903 92.837  1.00 17.57 ? 87  LEU A CD2 1 
ATOM   760  N N   . GLU A 1 88  ? -22.449 17.748 97.290  1.00 15.26 ? 88  GLU A N   1 
ATOM   761  C CA  . GLU A 1 88  ? -21.550 18.271 98.307  1.00 16.06 ? 88  GLU A CA  1 
ATOM   762  C C   . GLU A 1 88  ? -21.226 19.736 98.025  1.00 18.24 ? 88  GLU A C   1 
ATOM   763  O O   . GLU A 1 88  ? -21.210 20.177 96.872  1.00 18.82 ? 88  GLU A O   1 
ATOM   764  C CB  . GLU A 1 88  ? -20.250 17.461 98.308  1.00 18.29 ? 88  GLU A CB  1 
ATOM   765  C CG  . GLU A 1 88  ? -20.354 16.103 98.962  1.00 25.58 ? 88  GLU A CG  1 
ATOM   766  C CD  . GLU A 1 88  ? -19.431 15.083 98.320  1.00 38.30 ? 88  GLU A CD  1 
ATOM   767  O OE1 . GLU A 1 88  ? -18.296 15.450 97.953  1.00 37.87 ? 88  GLU A OE1 1 
ATOM   768  O OE2 . GLU A 1 88  ? -19.822 13.905 98.227  1.00 45.42 ? 88  GLU A OE2 1 
ATOM   769  N N   . LYS A 1 89  ? -20.936 20.484 99.094  1.00 18.99 ? 89  LYS A N   1 
ATOM   770  C CA  . LYS A 1 89  ? -20.425 21.847 98.938  1.00 19.57 ? 89  LYS A CA  1 
ATOM   771  C C   . LYS A 1 89  ? -19.241 21.875 97.972  1.00 23.43 ? 89  LYS A C   1 
ATOM   772  O O   . LYS A 1 89  ? -19.191 22.707 97.058  1.00 22.48 ? 89  LYS A O   1 
ATOM   773  C CB  . LYS A 1 89  ? -20.022 22.414 100.299 1.00 24.70 ? 89  LYS A CB  1 
ATOM   774  C CG  . LYS A 1 89  ? -21.192 22.701 101.237 1.00 31.21 ? 89  LYS A CG  1 
ATOM   775  C CD  . LYS A 1 89  ? -20.703 23.147 102.615 1.00 35.79 ? 89  LYS A CD  1 
ATOM   776  C CE  . LYS A 1 89  ? -21.851 23.620 103.502 1.00 45.46 ? 89  LYS A CE  1 
ATOM   777  N NZ  . LYS A 1 89  ? -22.800 22.525 103.809 1.00 48.25 ? 89  LYS A NZ  1 
ATOM   778  N N   . GLU A 1 90  ? -18.290 20.946 98.150  1.00 22.15 ? 90  GLU A N   1 
ATOM   779  C CA  . GLU A 1 90  ? -17.138 20.858 97.247  1.00 22.30 ? 90  GLU A CA  1 
ATOM   780  C C   . GLU A 1 90  ? -17.554 20.636 95.799  1.00 22.43 ? 90  GLU A C   1 
ATOM   781  O O   . GLU A 1 90  ? -16.856 21.085 94.878  1.00 22.55 ? 90  GLU A O   1 
ATOM   782  C CB  . GLU A 1 90  ? -16.209 19.713 97.650  1.00 29.12 ? 90  GLU A CB  1 
ATOM   783  C CG  . GLU A 1 90  ? -15.505 19.845 98.962  1.00 44.94 ? 90  GLU A CG  1 
ATOM   784  C CD  . GLU A 1 90  ? -14.485 18.739 99.184  1.00 57.17 ? 90  GLU A CD  1 
ATOM   785  O OE1 . GLU A 1 90  ? -14.310 17.891 98.278  1.00 54.61 ? 90  GLU A OE1 1 
ATOM   786  O OE2 . GLU A 1 90  ? -13.870 18.716 100.274 1.00 63.91 ? 90  GLU A OE2 1 
ATOM   787  N N   . GLU A 1 91  ? -18.651 19.906 95.574  1.00 17.94 ? 91  GLU A N   1 
ATOM   788  C CA  . GLU A 1 91  ? -19.069 19.600 94.211  1.00 17.99 ? 91  GLU A CA  1 
ATOM   789  C C   . GLU A 1 91  ? -19.699 20.816 93.542  1.00 17.12 ? 91  GLU A C   1 
ATOM   790  O O   . GLU A 1 91  ? -19.493 21.049 92.343  1.00 15.84 ? 91  GLU A O   1 
ATOM   791  C CB  . GLU A 1 91  ? -20.036 18.410 94.218  1.00 17.79 ? 91  GLU A CB  1 
ATOM   792  C CG  . GLU A 1 91  ? -19.321 17.058 94.306  1.00 21.97 ? 91  GLU A CG  1 
ATOM   793  C CD  . GLU A 1 91  ? -20.268 15.886 94.556  1.00 23.36 ? 91  GLU A CD  1 
ATOM   794  O OE1 . GLU A 1 91  ? -21.266 16.033 95.309  1.00 19.66 ? 91  GLU A OE1 1 
ATOM   795  O OE2 . GLU A 1 91  ? -20.021 14.808 93.971  1.00 20.93 ? 91  GLU A OE2 1 
ATOM   796  N N   . VAL A 1 92  ? -20.480 21.594 94.293  1.00 18.01 ? 92  VAL A N   1 
ATOM   797  C CA  . VAL A 1 92  ? -21.034 22.831 93.748  1.00 19.08 ? 92  VAL A CA  1 
ATOM   798  C C   . VAL A 1 92  ? -19.907 23.767 93.338  1.00 20.29 ? 92  VAL A C   1 
ATOM   799  O O   . VAL A 1 92  ? -19.948 24.391 92.271  1.00 21.20 ? 92  VAL A O   1 
ATOM   800  C CB  . VAL A 1 92  ? -21.974 23.484 94.773  1.00 19.24 ? 92  VAL A CB  1 
ATOM   801  C CG1 . VAL A 1 92  ? -22.444 24.858 94.275  1.00 21.92 ? 92  VAL A CG1 1 
ATOM   802  C CG2 . VAL A 1 92  ? -23.147 22.563 95.039  1.00 20.36 ? 92  VAL A CG2 1 
ATOM   803  N N   . GLU A 1 93  ? -18.863 23.841 94.163  1.00 18.06 ? 93  GLU A N   1 
ATOM   804  C CA  . GLU A 1 93  ? -17.711 24.678 93.849  1.00 20.08 ? 93  GLU A CA  1 
ATOM   805  C C   . GLU A 1 93  ? -17.002 24.214 92.589  1.00 20.52 ? 93  GLU A C   1 
ATOM   806  O O   . GLU A 1 93  ? -16.629 25.033 91.741  1.00 25.53 ? 93  GLU A O   1 
ATOM   807  C CB  . GLU A 1 93  ? -16.746 24.676 95.029  1.00 24.79 ? 93  GLU A CB  1 
ATOM   808  C CG  . GLU A 1 93  ? -17.411 25.196 96.264  1.00 30.17 ? 93  GLU A CG  1 
ATOM   809  C CD  . GLU A 1 93  ? -16.520 25.159 97.478  1.00 41.84 ? 93  GLU A CD  1 
ATOM   810  O OE1 . GLU A 1 93  ? -15.358 24.711 97.375  1.00 46.15 ? 93  GLU A OE1 1 
ATOM   811  O OE2 . GLU A 1 93  ? -16.979 25.593 98.552  1.00 42.88 ? 93  GLU A OE2 1 
ATOM   812  N N   . LYS A 1 94  ? -16.758 22.906 92.467  1.00 19.44 ? 94  LYS A N   1 
ATOM   813  C CA  . LYS A 1 94  ? -16.112 22.393 91.261  1.00 21.89 ? 94  LYS A CA  1 
ATOM   814  C C   . LYS A 1 94  ? -16.949 22.685 90.021  1.00 22.21 ? 94  LYS A C   1 
ATOM   815  O O   . LYS A 1 94  ? -16.409 23.047 88.963  1.00 17.37 ? 94  LYS A O   1 
ATOM   816  C CB  . LYS A 1 94  ? -15.867 20.890 91.388  1.00 25.86 ? 94  LYS A CB  1 
ATOM   817  C CG  . LYS A 1 94  ? -14.802 20.544 92.407  1.00 36.30 ? 94  LYS A CG  1 
ATOM   818  C CD  . LYS A 1 94  ? -14.537 19.049 92.469  1.00 44.48 ? 94  LYS A CD  1 
ATOM   819  C CE  . LYS A 1 94  ? -13.494 18.746 93.541  1.00 53.47 ? 94  LYS A CE  1 
ATOM   820  N NZ  . LYS A 1 94  ? -13.205 17.295 93.657  1.00 58.19 ? 94  LYS A NZ  1 
ATOM   821  N N   . LEU A 1 95  ? -18.265 22.574 90.129  1.00 15.47 ? 95  LEU A N   1 
ATOM   822  C CA  . LEU A 1 95  ? -19.120 22.864 88.997  1.00 16.36 ? 95  LEU A CA  1 
ATOM   823  C C   . LEU A 1 95  ? -19.035 24.289 88.567  1.00 17.98 ? 95  LEU A C   1 
ATOM   824  O O   . LEU A 1 95  ? -18.996 24.567 87.418  1.00 17.79 ? 95  LEU A O   1 
ATOM   825  C CB  . LEU A 1 95  ? -20.569 22.655 89.338  1.00 19.65 ? 95  LEU A CB  1 
ATOM   826  C CG  . LEU A 1 95  ? -21.220 21.305 89.291  1.00 34.98 ? 95  LEU A CG  1 
ATOM   827  C CD1 . LEU A 1 95  ? -22.701 21.470 89.607  1.00 38.35 ? 95  LEU A CD1 1 
ATOM   828  C CD2 . LEU A 1 95  ? -21.112 20.640 87.927  1.00 31.13 ? 95  LEU A CD2 1 
ATOM   829  N N   . ILE A 1 96  ? -19.087 25.179 89.541  1.00 17.41 ? 96  ILE A N   1 
ATOM   830  C CA  . ILE A 1 96  ? -19.006 26.602 89.233  1.00 18.56 ? 96  ILE A CA  1 
ATOM   831  C C   . ILE A 1 96  ? -17.646 26.936 88.639  1.00 21.28 ? 96  ILE A C   1 
ATOM   832  O O   . ILE A 1 96  ? -17.553 27.642 87.629  1.00 17.59 ? 96  ILE A O   1 
ATOM   833  C CB  . ILE A 1 96  ? -19.310 27.431 90.495  1.00 19.10 ? 96  ILE A CB  1 
ATOM   834  C CG1 . ILE A 1 96  ? -20.817 27.415 90.773  1.00 18.24 ? 96  ILE A CG1 1 
ATOM   835  C CG2 . ILE A 1 96  ? -18.788 28.860 90.350  1.00 22.96 ? 96  ILE A CG2 1 
ATOM   836  C CD1 . ILE A 1 96  ? -21.164 27.810 92.185  1.00 30.09 ? 96  ILE A CD1 1 
ATOM   837  N N   . GLU A 1 97  ? -16.575 26.380 89.210  1.00 17.42 ? 97  GLU A N   1 
ATOM   838  C CA  . GLU A 1 97  ? -15.241 26.687 88.702  1.00 23.92 ? 97  GLU A CA  1 
ATOM   839  C C   . GLU A 1 97  ? -15.032 26.112 87.303  1.00 22.02 ? 97  GLU A C   1 
ATOM   840  O O   . GLU A 1 97  ? -14.362 26.724 86.464  1.00 21.17 ? 97  GLU A O   1 
ATOM   841  C CB  . GLU A 1 97  ? -14.177 26.167 89.670  1.00 31.22 ? 97  GLU A CB  1 
ATOM   842  C CG  . GLU A 1 97  ? -12.806 26.695 89.350  1.00 46.84 ? 97  GLU A CG  1 
ATOM   843  C CD  . GLU A 1 97  ? -12.731 28.206 89.521  1.00 60.79 ? 97  GLU A CD  1 
ATOM   844  O OE1 . GLU A 1 97  ? -13.386 28.740 90.442  1.00 62.71 ? 97  GLU A OE1 1 
ATOM   845  O OE2 . GLU A 1 97  ? -12.031 28.864 88.724  1.00 66.23 ? 97  GLU A OE2 1 
ATOM   846  N N   . PHE A 1 98  ? -15.572 24.928 87.035  1.00 19.10 ? 98  PHE A N   1 
ATOM   847  C CA  . PHE A 1 98  ? -15.480 24.383 85.687  1.00 18.50 ? 98  PHE A CA  1 
ATOM   848  C C   . PHE A 1 98  ? -16.243 25.249 84.690  1.00 17.33 ? 98  PHE A C   1 
ATOM   849  O O   . PHE A 1 98  ? -15.779 25.473 83.565  1.00 16.46 ? 98  PHE A O   1 
ATOM   850  C CB  . PHE A 1 98  ? -16.014 22.960 85.679  1.00 13.86 ? 98  PHE A CB  1 
ATOM   851  C CG  . PHE A 1 98  ? -15.737 22.209 84.412  1.00 17.25 ? 98  PHE A CG  1 
ATOM   852  C CD1 . PHE A 1 98  ? -14.497 21.627 84.192  1.00 15.75 ? 98  PHE A CD1 1 
ATOM   853  C CD2 . PHE A 1 98  ? -16.720 22.074 83.437  1.00 16.28 ? 98  PHE A CD2 1 
ATOM   854  C CE1 . PHE A 1 98  ? -14.250 20.917 83.020  1.00 14.17 ? 98  PHE A CE1 1 
ATOM   855  C CE2 . PHE A 1 98  ? -16.471 21.371 82.267  1.00 18.94 ? 98  PHE A CE2 1 
ATOM   856  C CZ  . PHE A 1 98  ? -15.231 20.800 82.062  1.00 17.17 ? 98  PHE A CZ  1 
ATOM   857  N N   . THR A 1 99  ? -17.422 25.731 85.085  1.00 13.00 ? 99  THR A N   1 
ATOM   858  C CA  . THR A 1 99  ? -18.166 26.650 84.236  1.00 19.43 ? 99  THR A CA  1 
ATOM   859  C C   . THR A 1 99  ? -17.354 27.906 83.939  1.00 17.44 ? 99  THR A C   1 
ATOM   860  O O   . THR A 1 99  ? -17.248 28.328 82.779  1.00 18.68 ? 99  THR A O   1 
ATOM   861  C CB  . THR A 1 99  ? -19.491 27.014 84.902  1.00 17.64 ? 99  THR A CB  1 
ATOM   862  O OG1 . THR A 1 99  ? -20.207 25.814 85.228  1.00 16.37 ? 99  THR A OG1 1 
ATOM   863  C CG2 . THR A 1 99  ? -20.339 27.864 83.963  1.00 18.40 ? 99  THR A CG2 1 
ATOM   864  N N   . LYS A 1 100 ? -16.776 28.520 84.986  1.00 17.96 ? 100 LYS A N   1 
ATOM   865  C CA  . LYS A 1 100 ? -15.965 29.729 84.827  1.00 19.39 ? 100 LYS A CA  1 
ATOM   866  C C   . LYS A 1 100 ? -14.854 29.534 83.806  1.00 22.06 ? 100 LYS A C   1 
ATOM   867  O O   . LYS A 1 100 ? -14.541 30.448 83.028  1.00 25.08 ? 100 LYS A O   1 
ATOM   868  C CB  . LYS A 1 100 ? -15.331 30.134 86.169  1.00 20.47 ? 100 LYS A CB  1 
ATOM   869  C CG  . LYS A 1 100 ? -16.258 30.562 87.285  1.00 40.23 ? 100 LYS A CG  1 
ATOM   870  C CD  . LYS A 1 100 ? -17.394 31.408 86.791  1.00 50.91 ? 100 LYS A CD  1 
ATOM   871  C CE  . LYS A 1 100 ? -17.590 32.584 87.729  1.00 60.14 ? 100 LYS A CE  1 
ATOM   872  N NZ  . LYS A 1 100 ? -17.016 33.838 87.152  1.00 64.51 ? 100 LYS A NZ  1 
ATOM   873  N N   . LEU A 1 101 ? -14.189 28.379 83.858  1.00 18.25 ? 101 LEU A N   1 
ATOM   874  C CA  . LEU A 1 101 ? -13.067 28.111 82.967  1.00 19.43 ? 101 LEU A CA  1 
ATOM   875  C C   . LEU A 1 101 ? -13.512 28.033 81.514  1.00 18.53 ? 101 LEU A C   1 
ATOM   876  O O   . LEU A 1 101 ? -12.750 28.395 80.611  1.00 22.81 ? 101 LEU A O   1 
ATOM   877  C CB  . LEU A 1 101 ? -12.392 26.798 83.369  1.00 22.01 ? 101 LEU A CB  1 
ATOM   878  C CG  . LEU A 1 101 ? -11.371 26.230 82.375  1.00 34.96 ? 101 LEU A CG  1 
ATOM   879  C CD1 . LEU A 1 101 ? -10.217 27.199 82.225  1.00 32.73 ? 101 LEU A CD1 1 
ATOM   880  C CD2 . LEU A 1 101 ? -10.870 24.846 82.778  1.00 40.98 ? 101 LEU A CD2 1 
ATOM   881  N N   . ASN A 1 102 ? -14.729 27.559 81.268  1.00 16.35 ? 102 ASN A N   1 
ATOM   882  C CA  . ASN A 1 102 ? -15.210 27.281 79.915  1.00 16.92 ? 102 ASN A CA  1 
ATOM   883  C C   . ASN A 1 102 ? -16.158 28.350 79.379  1.00 21.44 ? 102 ASN A C   1 
ATOM   884  O O   . ASN A 1 102 ? -16.528 28.299 78.193  1.00 17.88 ? 102 ASN A O   1 
ATOM   885  C CB  . ASN A 1 102 ? -15.905 25.923 79.896  1.00 13.77 ? 102 ASN A CB  1 
ATOM   886  C CG  . ASN A 1 102 ? -14.924 24.769 80.000  1.00 21.51 ? 102 ASN A CG  1 
ATOM   887  O OD1 . ASN A 1 102 ? -14.043 24.609 79.155  1.00 19.04 ? 102 ASN A OD1 1 
ATOM   888  N ND2 . ASN A 1 102 ? -15.050 23.982 81.055  1.00 23.78 ? 102 ASN A ND2 1 
ATOM   889  N N   . TYR A 1 103 ? -16.497 29.332 80.224  1.00 25.54 ? 103 TYR A N   1 
ATOM   890  C CA  . TYR A 1 103 ? -17.614 30.263 80.041  1.00 32.86 ? 103 TYR A CA  1 
ATOM   891  C C   . TYR A 1 103 ? -17.579 31.013 78.709  1.00 25.79 ? 103 TYR A C   1 
ATOM   892  O O   . TYR A 1 103 ? -18.635 31.309 78.132  1.00 18.41 ? 103 TYR A O   1 
ATOM   893  C CB  . TYR A 1 103 ? -17.582 31.253 81.219  1.00 40.18 ? 103 TYR A CB  1 
ATOM   894  C CG  . TYR A 1 103 ? -18.601 32.361 81.200  1.00 48.17 ? 103 TYR A CG  1 
ATOM   895  C CD1 . TYR A 1 103 ? -19.919 32.125 81.559  1.00 53.28 ? 103 TYR A CD1 1 
ATOM   896  C CD2 . TYR A 1 103 ? -18.239 33.655 80.852  1.00 56.63 ? 103 TYR A CD2 1 
ATOM   897  C CE1 . TYR A 1 103 ? -20.859 33.146 81.551  1.00 61.36 ? 103 TYR A CE1 1 
ATOM   898  C CE2 . TYR A 1 103 ? -19.168 34.685 80.840  1.00 62.83 ? 103 TYR A CE2 1 
ATOM   899  C CZ  . TYR A 1 103 ? -20.479 34.424 81.191  1.00 64.08 ? 103 TYR A CZ  1 
ATOM   900  O OH  . TYR A 1 103 ? -21.416 35.435 81.186  1.00 61.43 ? 103 TYR A OH  1 
ATOM   901  N N   . GLU A 1 104 ? -16.396 31.364 78.225  1.00 23.09 ? 104 GLU A N   1 
ATOM   902  C CA  . GLU A 1 104 ? -16.289 32.229 77.057  1.00 23.73 ? 104 GLU A CA  1 
ATOM   903  C C   . GLU A 1 104 ? -16.215 31.466 75.741  1.00 24.37 ? 104 GLU A C   1 
ATOM   904  O O   . GLU A 1 104 ? -16.205 32.093 74.674  1.00 25.75 ? 104 GLU A O   1 
ATOM   905  C CB  . GLU A 1 104 ? -15.060 33.131 77.193  1.00 32.87 ? 104 GLU A CB  1 
ATOM   906  C CG  . GLU A 1 104 ? -15.232 34.192 78.252  1.00 48.07 ? 104 GLU A CG  1 
ATOM   907  C CD  . GLU A 1 104 ? -16.372 35.136 77.923  1.00 59.86 ? 104 GLU A CD  1 
ATOM   908  O OE1 . GLU A 1 104 ? -16.628 35.368 76.720  1.00 63.27 ? 104 GLU A OE1 1 
ATOM   909  O OE2 . GLU A 1 104 ? -17.018 35.641 78.863  1.00 65.10 ? 104 GLU A OE2 1 
ATOM   910  N N   . LYS A 1 105 ? -16.154 30.143 75.788  1.00 16.27 ? 105 LYS A N   1 
ATOM   911  C CA  . LYS A 1 105 ? -16.063 29.364 74.564  1.00 16.48 ? 105 LYS A CA  1 
ATOM   912  C C   . LYS A 1 105 ? -17.411 29.371 73.846  1.00 17.61 ? 105 LYS A C   1 
ATOM   913  O O   . LYS A 1 105 ? -18.459 29.303 74.495  1.00 16.87 ? 105 LYS A O   1 
ATOM   914  C CB  . LYS A 1 105 ? -15.650 27.923 74.880  1.00 17.05 ? 105 LYS A CB  1 
ATOM   915  C CG  . LYS A 1 105 ? -14.270 27.828 75.487  1.00 18.87 ? 105 LYS A CG  1 
ATOM   916  C CD  . LYS A 1 105 ? -13.970 26.459 76.045  1.00 18.66 ? 105 LYS A CD  1 
ATOM   917  C CE  . LYS A 1 105 ? -12.585 26.472 76.664  1.00 19.42 ? 105 LYS A CE  1 
ATOM   918  N NZ  . LYS A 1 105 ? -12.240 25.155 77.231  1.00 17.74 ? 105 LYS A NZ  1 
ATOM   919  N N   . PRO A 1 106 ? -17.413 29.452 72.516  1.00 19.30 ? 106 PRO A N   1 
ATOM   920  C CA  . PRO A 1 106 ? -18.681 29.404 71.769  1.00 21.33 ? 106 PRO A CA  1 
ATOM   921  C C   . PRO A 1 106 ? -19.570 28.216 72.096  1.00 17.66 ? 106 PRO A C   1 
ATOM   922  O O   . PRO A 1 106 ? -20.799 28.371 72.096  1.00 19.62 ? 106 PRO A O   1 
ATOM   923  C CB  . PRO A 1 106 ? -18.209 29.372 70.309  1.00 19.82 ? 106 PRO A CB  1 
ATOM   924  C CG  . PRO A 1 106 ? -16.906 30.096 70.339  1.00 20.34 ? 106 PRO A CG  1 
ATOM   925  C CD  . PRO A 1 106 ? -16.260 29.708 71.632  1.00 18.77 ? 106 PRO A CD  1 
ATOM   926  N N   . ILE A 1 107 ? -19.016 27.036 72.400  1.00 14.87 ? 107 ILE A N   1 
ATOM   927  C CA  . ILE A 1 107 ? -19.891 25.921 72.735  1.00 17.96 ? 107 ILE A CA  1 
ATOM   928  C C   . ILE A 1 107 ? -20.626 26.143 74.050  1.00 19.48 ? 107 ILE A C   1 
ATOM   929  O O   . ILE A 1 107 ? -21.593 25.417 74.325  1.00 19.27 ? 107 ILE A O   1 
ATOM   930  C CB  . ILE A 1 107 ? -19.135 24.582 72.794  1.00 13.19 ? 107 ILE A CB  1 
ATOM   931  C CG1 . ILE A 1 107 ? -17.961 24.665 73.770  1.00 13.44 ? 107 ILE A CG1 1 
ATOM   932  C CG2 . ILE A 1 107 ? -18.695 24.159 71.374  1.00 17.69 ? 107 ILE A CG2 1 
ATOM   933  C CD1 . ILE A 1 107 ? -17.351 23.291 74.078  1.00 12.87 ? 107 ILE A CD1 1 
ATOM   934  N N   . TYR A 1 108 ? -20.196 27.107 74.875  1.00 14.29 ? 108 TYR A N   1 
ATOM   935  C CA  . TYR A 1 108 ? -20.916 27.478 76.086  1.00 19.38 ? 108 TYR A CA  1 
ATOM   936  C C   . TYR A 1 108 ? -21.854 28.674 75.902  1.00 17.67 ? 108 TYR A C   1 
ATOM   937  O O   . TYR A 1 108 ? -22.322 29.239 76.900  1.00 21.78 ? 108 TYR A O   1 
ATOM   938  C CB  . TYR A 1 108 ? -19.949 27.780 77.240  1.00 17.41 ? 108 TYR A CB  1 
ATOM   939  C CG  . TYR A 1 108 ? -19.553 26.560 78.044  1.00 13.35 ? 108 TYR A CG  1 
ATOM   940  C CD1 . TYR A 1 108 ? -18.744 25.567 77.511  1.00 12.52 ? 108 TYR A CD1 1 
ATOM   941  C CD2 . TYR A 1 108 ? -20.070 26.364 79.322  1.00 21.11 ? 108 TYR A CD2 1 
ATOM   942  C CE1 . TYR A 1 108 ? -18.410 24.451 78.250  1.00 17.86 ? 108 TYR A CE1 1 
ATOM   943  C CE2 . TYR A 1 108 ? -19.756 25.239 80.069  1.00 17.93 ? 108 TYR A CE2 1 
ATOM   944  C CZ  . TYR A 1 108 ? -18.922 24.283 79.521  1.00 17.17 ? 108 TYR A CZ  1 
ATOM   945  O OH  . TYR A 1 108 ? -18.584 23.159 80.230  1.00 16.86 ? 108 TYR A OH  1 
ATOM   946  N N   . ARG A 1 109 ? -22.151 29.073 74.662  1.00 18.54 ? 109 ARG A N   1 
ATOM   947  C CA  . ARG A 1 109 ? -22.991 30.248 74.415  1.00 20.94 ? 109 ARG A CA  1 
ATOM   948  C C   . ARG A 1 109 ? -24.456 29.892 74.657  1.00 24.49 ? 109 ARG A C   1 
ATOM   949  O O   . ARG A 1 109 ? -25.241 29.658 73.735  1.00 29.32 ? 109 ARG A O   1 
ATOM   950  C CB  . ARG A 1 109 ? -22.787 30.780 73.002  1.00 23.75 ? 109 ARG A CB  1 
ATOM   951  C CG  . ARG A 1 109 ? -23.598 32.023 72.687  1.00 32.15 ? 109 ARG A CG  1 
ATOM   952  C CD  . ARG A 1 109 ? -23.216 32.546 71.336  1.00 44.11 ? 109 ARG A CD  1 
ATOM   953  N NE  . ARG A 1 109 ? -21.781 32.786 71.331  1.00 48.12 ? 109 ARG A NE  1 
ATOM   954  C CZ  . ARG A 1 109 ? -21.040 32.823 70.235  1.00 52.85 ? 109 ARG A CZ  1 
ATOM   955  N NH1 . ARG A 1 109 ? -21.612 32.634 69.055  1.00 55.96 ? 109 ARG A NH1 1 
ATOM   956  N NH2 . ARG A 1 109 ? -19.731 33.034 70.321  1.00 48.93 ? 109 ARG A NH2 1 
ATOM   957  N N   . PHE A 1 110 ? -24.822 29.844 75.933  1.00 25.68 ? 110 PHE A N   1 
ATOM   958  C CA  . PHE A 1 110 ? -26.209 29.767 76.366  1.00 24.87 ? 110 PHE A CA  1 
ATOM   959  C C   . PHE A 1 110 ? -26.465 30.980 77.245  1.00 20.15 ? 110 PHE A C   1 
ATOM   960  O O   . PHE A 1 110 ? -25.740 31.191 78.223  1.00 19.96 ? 110 PHE A O   1 
ATOM   961  C CB  . PHE A 1 110 ? -26.481 28.493 77.169  1.00 20.50 ? 110 PHE A CB  1 
ATOM   962  C CG  . PHE A 1 110 ? -26.202 27.221 76.431  1.00 19.62 ? 110 PHE A CG  1 
ATOM   963  C CD1 . PHE A 1 110 ? -27.162 26.654 75.599  1.00 23.62 ? 110 PHE A CD1 1 
ATOM   964  C CD2 . PHE A 1 110 ? -24.994 26.563 76.603  1.00 22.36 ? 110 PHE A CD2 1 
ATOM   965  C CE1 . PHE A 1 110 ? -26.905 25.454 74.936  1.00 22.49 ? 110 PHE A CE1 1 
ATOM   966  C CE2 . PHE A 1 110 ? -24.724 25.373 75.948  1.00 24.31 ? 110 PHE A CE2 1 
ATOM   967  C CZ  . PHE A 1 110 ? -25.684 24.813 75.109  1.00 26.03 ? 110 PHE A CZ  1 
ATOM   968  N N   . GLU A 1 111 ? -27.485 31.779 76.907  1.00 23.78 ? 111 GLU A N   1 
ATOM   969  C CA  . GLU A 1 111 ? -27.794 32.926 77.758  1.00 28.45 ? 111 GLU A CA  1 
ATOM   970  C C   . GLU A 1 111 ? -28.041 32.493 79.195  1.00 26.57 ? 111 GLU A C   1 
ATOM   971  O O   . GLU A 1 111 ? -27.682 33.218 80.132  1.00 26.07 ? 111 GLU A O   1 
ATOM   972  C CB  . GLU A 1 111 ? -29.000 33.708 77.227  1.00 34.76 ? 111 GLU A CB  1 
ATOM   973  C CG  . GLU A 1 111 ? -29.331 34.913 78.108  1.00 48.29 ? 111 GLU A CG  1 
ATOM   974  C CD  . GLU A 1 111 ? -28.702 36.212 77.629  1.00 67.13 ? 111 GLU A CD  1 
ATOM   975  O OE1 . GLU A 1 111 ? -28.559 37.151 78.450  1.00 71.80 ? 111 GLU A OE1 1 
ATOM   976  O OE2 . GLU A 1 111 ? -28.375 36.300 76.425  1.00 74.63 ? 111 GLU A OE2 1 
ATOM   977  N N   . ARG A 1 112 ? -28.591 31.287 79.385  1.00 21.95 ? 112 ARG A N   1 
ATOM   978  C CA  . ARG A 1 112 ? -28.858 30.795 80.733  1.00 23.16 ? 112 ARG A CA  1 
ATOM   979  C C   . ARG A 1 112 ? -27.580 30.645 81.547  1.00 20.30 ? 112 ARG A C   1 
ATOM   980  O O   . ARG A 1 112 ? -27.593 30.875 82.760  1.00 20.78 ? 112 ARG A O   1 
ATOM   981  C CB  . ARG A 1 112 ? -29.606 29.463 80.667  1.00 19.78 ? 112 ARG A CB  1 
ATOM   982  C CG  . ARG A 1 112 ? -29.907 28.837 82.021  1.00 24.18 ? 112 ARG A CG  1 
ATOM   983  C CD  . ARG A 1 112 ? -30.760 29.762 82.892  1.00 21.35 ? 112 ARG A CD  1 
ATOM   984  N NE  . ARG A 1 112 ? -31.422 29.003 83.951  1.00 22.65 ? 112 ARG A NE  1 
ATOM   985  C CZ  . ARG A 1 112 ? -32.059 29.550 84.985  1.00 26.68 ? 112 ARG A CZ  1 
ATOM   986  N NH1 . ARG A 1 112 ? -32.111 30.863 85.105  1.00 25.88 ? 112 ARG A NH1 1 
ATOM   987  N NH2 . ARG A 1 112 ? -32.643 28.784 85.900  1.00 24.57 ? 112 ARG A NH2 1 
ATOM   988  N N   . ILE A 1 113 ? -26.470 30.258 80.909  1.00 19.87 ? 113 ILE A N   1 
ATOM   989  C CA  . ILE A 1 113 ? -25.207 30.174 81.641  1.00 20.35 ? 113 ILE A CA  1 
ATOM   990  C C   . ILE A 1 113 ? -24.782 31.555 82.105  1.00 24.63 ? 113 ILE A C   1 
ATOM   991  O O   . ILE A 1 113 ? -24.291 31.723 83.226  1.00 24.53 ? 113 ILE A O   1 
ATOM   992  C CB  . ILE A 1 113 ? -24.127 29.504 80.777  1.00 25.76 ? 113 ILE A CB  1 
ATOM   993  C CG1 . ILE A 1 113 ? -24.374 28.000 80.731  1.00 22.66 ? 113 ILE A CG1 1 
ATOM   994  C CG2 . ILE A 1 113 ? -22.729 29.803 81.324  1.00 32.49 ? 113 ILE A CG2 1 
ATOM   995  C CD1 . ILE A 1 113 ? -23.479 27.283 79.807  1.00 23.76 ? 113 ILE A CD1 1 
ATOM   996  N N   . ARG A 1 114 ? -24.975 32.561 81.250  1.00 25.38 ? 114 ARG A N   1 
ATOM   997  C CA  . ARG A 1 114 ? -24.690 33.938 81.626  1.00 34.43 ? 114 ARG A CA  1 
ATOM   998  C C   . ARG A 1 114 ? -25.546 34.362 82.822  1.00 32.05 ? 114 ARG A C   1 
ATOM   999  O O   . ARG A 1 114 ? -25.052 35.012 83.751  1.00 33.34 ? 114 ARG A O   1 
ATOM   1000 C CB  . ARG A 1 114 ? -24.921 34.855 80.416  1.00 38.48 ? 114 ARG A CB  1 
ATOM   1001 C CG  . ARG A 1 114 ? -24.269 34.395 79.085  1.00 47.35 ? 114 ARG A CG  1 
ATOM   1002 C CD  . ARG A 1 114 ? -24.429 35.478 77.998  1.00 57.15 ? 114 ARG A CD  1 
ATOM   1003 N NE  . ARG A 1 114 ? -23.901 35.109 76.680  1.00 62.78 ? 114 ARG A NE  1 
ATOM   1004 C CZ  . ARG A 1 114 ? -24.641 34.817 75.609  1.00 63.31 ? 114 ARG A CZ  1 
ATOM   1005 N NH1 . ARG A 1 114 ? -25.965 34.849 75.666  1.00 62.93 ? 114 ARG A NH1 1 
ATOM   1006 N NH2 . ARG A 1 114 ? -24.049 34.514 74.462  1.00 64.48 ? 114 ARG A NH2 1 
ATOM   1007 N N   . GLU A 1 115 ? -26.828 33.985 82.825  1.00 29.91 ? 115 GLU A N   1 
ATOM   1008 C CA  . GLU A 1 115 ? -27.688 34.297 83.964  1.00 31.49 ? 115 GLU A CA  1 
ATOM   1009 C C   . GLU A 1 115 ? -27.182 33.625 85.237  1.00 34.58 ? 115 GLU A C   1 
ATOM   1010 O O   . GLU A 1 115 ? -27.037 34.273 86.283  1.00 32.57 ? 115 GLU A O   1 
ATOM   1011 C CB  . GLU A 1 115 ? -29.126 33.865 83.673  1.00 35.89 ? 115 GLU A CB  1 
ATOM   1012 C CG  . GLU A 1 115 ? -29.710 34.441 82.398  1.00 42.97 ? 115 GLU A CG  1 
ATOM   1013 C CD  . GLU A 1 115 ? -31.106 33.917 82.093  1.00 47.69 ? 115 GLU A CD  1 
ATOM   1014 O OE1 . GLU A 1 115 ? -31.631 33.088 82.872  1.00 47.50 ? 115 GLU A OE1 1 
ATOM   1015 O OE2 . GLU A 1 115 ? -31.678 34.340 81.065  1.00 50.02 ? 115 GLU A OE2 1 
ATOM   1016 N N   . LEU A 1 116 ? -26.902 32.320 85.160  1.00 30.42 ? 116 LEU A N   1 
ATOM   1017 C CA  . LEU A 1 116 ? -26.540 31.552 86.348  1.00 26.48 ? 116 LEU A CA  1 
ATOM   1018 C C   . LEU A 1 116 ? -25.243 32.051 86.973  1.00 34.91 ? 116 LEU A C   1 
ATOM   1019 O O   . LEU A 1 116 ? -25.100 32.054 88.202  1.00 36.61 ? 116 LEU A O   1 
ATOM   1020 C CB  . LEU A 1 116 ? -26.422 30.070 85.992  1.00 26.62 ? 116 LEU A CB  1 
ATOM   1021 C CG  . LEU A 1 116 ? -27.697 29.358 85.529  1.00 25.13 ? 116 LEU A CG  1 
ATOM   1022 C CD1 . LEU A 1 116 ? -27.361 27.957 85.016  1.00 24.47 ? 116 LEU A CD1 1 
ATOM   1023 C CD2 . LEU A 1 116 ? -28.707 29.291 86.662  1.00 27.49 ? 116 LEU A CD2 1 
ATOM   1024 N N   . MET A 1 117 ? -24.278 32.470 86.152  1.00 32.32 ? 117 MET A N   1 
ATOM   1025 C CA  . MET A 1 117 ? -23.036 32.976 86.717  1.00 32.19 ? 117 MET A CA  1 
ATOM   1026 C C   . MET A 1 117 ? -23.183 34.378 87.297  1.00 41.38 ? 117 MET A C   1 
ATOM   1027 O O   . MET A 1 117 ? -22.272 34.833 87.996  1.00 45.28 ? 117 MET A O   1 
ATOM   1028 C CB  . MET A 1 117 ? -21.916 32.950 85.671  1.00 28.10 ? 117 MET A CB  1 
ATOM   1029 C CG  . MET A 1 117 ? -21.524 31.544 85.213  1.00 29.11 ? 117 MET A CG  1 
ATOM   1030 S SD  . MET A 1 117 ? -20.851 30.464 86.517  1.00 34.93 ? 117 MET A SD  1 
ATOM   1031 C CE  . MET A 1 117 ? -22.311 29.529 86.945  1.00 34.15 ? 117 MET A CE  1 
ATOM   1032 N N   . ASN A 1 118 ? -24.299 35.062 87.029  1.00 44.32 ? 118 ASN A N   1 
ATOM   1033 C CA  . ASN A 1 118 ? -24.596 36.352 87.643  1.00 52.49 ? 118 ASN A CA  1 
ATOM   1034 C C   . ASN A 1 118 ? -25.284 36.226 88.991  1.00 53.17 ? 118 ASN A C   1 
ATOM   1035 O O   . ASN A 1 118 ? -25.420 37.232 89.696  1.00 57.80 ? 118 ASN A O   1 
ATOM   1036 C CB  . ASN A 1 118 ? -25.491 37.198 86.733  1.00 57.90 ? 118 ASN A CB  1 
ATOM   1037 C CG  . ASN A 1 118 ? -24.709 38.005 85.733  1.00 63.48 ? 118 ASN A CG  1 
ATOM   1038 O OD1 . ASN A 1 118 ? -23.577 38.410 86.002  1.00 65.51 ? 118 ASN A OD1 1 
ATOM   1039 N ND2 . ASN A 1 118 ? -25.319 38.284 84.583  1.00 66.15 ? 118 ASN A ND2 1 
ATOM   1040 N N   . LYS A 1 119 ? -25.732 35.032 89.358  1.00 44.90 ? 119 LYS A N   1 
ATOM   1041 C CA  . LYS A 1 119 ? -26.516 34.855 90.569  1.00 43.27 ? 119 LYS A CA  1 
ATOM   1042 C C   . LYS A 1 119 ? -25.605 34.559 91.750  1.00 45.03 ? 119 LYS A C   1 
ATOM   1043 O O   . LYS A 1 119 ? -24.593 33.861 91.619  1.00 41.01 ? 119 LYS A O   1 
ATOM   1044 C CB  . LYS A 1 119 ? -27.539 33.736 90.376  1.00 41.15 ? 119 LYS A CB  1 
ATOM   1045 C CG  . LYS A 1 119 ? -28.728 34.173 89.535  1.00 45.61 ? 119 LYS A CG  1 
ATOM   1046 C CD  . LYS A 1 119 ? -29.772 33.081 89.398  1.00 49.41 ? 119 LYS A CD  1 
ATOM   1047 C CE  . LYS A 1 119 ? -30.953 33.556 88.554  1.00 51.53 ? 119 LYS A CE  1 
ATOM   1048 N NZ  . LYS A 1 119 ? -32.182 33.807 89.372  1.00 53.56 ? 119 LYS A NZ  1 
ATOM   1049 N N   . GLU A 1 120 ? -25.962 35.115 92.906  1.00 50.43 ? 120 GLU A N   1 
ATOM   1050 C CA  . GLU A 1 120 ? -25.132 34.958 94.093  1.00 49.43 ? 120 GLU A CA  1 
ATOM   1051 C C   . GLU A 1 120 ? -25.251 33.558 94.679  1.00 45.20 ? 120 GLU A C   1 
ATOM   1052 O O   . GLU A 1 120 ? -24.267 33.012 95.188  1.00 44.52 ? 120 GLU A O   1 
ATOM   1053 C CB  . GLU A 1 120 ? -25.520 36.022 95.119  1.00 51.40 ? 120 GLU A CB  1 
ATOM   1054 C CG  . GLU A 1 120 ? -25.481 37.446 94.553  1.00 54.97 ? 120 GLU A CG  1 
ATOM   1055 C CD  . GLU A 1 120 ? -26.124 38.483 95.468  1.00 61.69 ? 120 GLU A CD  1 
ATOM   1056 O OE1 . GLU A 1 120 ? -26.651 38.103 96.536  1.00 59.13 ? 120 GLU A OE1 1 
ATOM   1057 O OE2 . GLU A 1 120 ? -26.108 39.683 95.113  1.00 64.15 ? 120 GLU A OE2 1 
ATOM   1058 N N   . LYS A 1 121 ? -26.433 32.956 94.588  1.00 44.76 ? 121 LYS A N   1 
ATOM   1059 C CA  . LYS A 1 121 ? -26.696 31.641 95.158  1.00 44.84 ? 121 LYS A CA  1 
ATOM   1060 C C   . LYS A 1 121 ? -27.684 30.932 94.243  1.00 38.44 ? 121 LYS A C   1 
ATOM   1061 O O   . LYS A 1 121 ? -28.660 31.539 93.794  1.00 39.45 ? 121 LYS A O   1 
ATOM   1062 C CB  . LYS A 1 121 ? -27.246 31.771 96.588  1.00 49.36 ? 121 LYS A CB  1 
ATOM   1063 C CG  . LYS A 1 121 ? -27.712 30.473 97.234  1.00 51.88 ? 121 LYS A CG  1 
ATOM   1064 C CD  . LYS A 1 121 ? -29.129 30.632 97.775  1.00 57.80 ? 121 LYS A CD  1 
ATOM   1065 C CE  . LYS A 1 121 ? -30.156 30.017 96.830  1.00 60.15 ? 121 LYS A CE  1 
ATOM   1066 N NZ  . LYS A 1 121 ? -31.566 30.235 97.283  1.00 58.24 ? 121 LYS A NZ  1 
ATOM   1067 N N   . LEU A 1 122 ? -27.411 29.670 93.937  1.00 34.24 ? 122 LEU A N   1 
ATOM   1068 C CA  . LEU A 1 122 ? -28.226 28.911 92.994  1.00 27.14 ? 122 LEU A CA  1 
ATOM   1069 C C   . LEU A 1 122 ? -29.125 27.940 93.746  1.00 29.82 ? 122 LEU A C   1 
ATOM   1070 O O   . LEU A 1 122 ? -28.666 27.231 94.647  1.00 32.29 ? 122 LEU A O   1 
ATOM   1071 C CB  . LEU A 1 122 ? -27.348 28.144 92.003  1.00 24.88 ? 122 LEU A CB  1 
ATOM   1072 C CG  . LEU A 1 122 ? -26.351 28.986 91.215  1.00 28.03 ? 122 LEU A CG  1 
ATOM   1073 C CD1 . LEU A 1 122 ? -25.444 28.098 90.367  1.00 30.68 ? 122 LEU A CD1 1 
ATOM   1074 C CD2 . LEU A 1 122 ? -27.082 29.993 90.349  1.00 32.23 ? 122 LEU A CD2 1 
ATOM   1075 N N   . ASN A 1 123 ? -30.401 27.900 93.369  1.00 27.47 ? 123 ASN A N   1 
ATOM   1076 C CA  . ASN A 1 123 ? -31.323 26.943 93.965  1.00 24.04 ? 123 ASN A CA  1 
ATOM   1077 C C   . ASN A 1 123 ? -31.233 25.619 93.198  1.00 20.38 ? 123 ASN A C   1 
ATOM   1078 O O   . ASN A 1 123 ? -30.361 25.429 92.345  1.00 19.80 ? 123 ASN A O   1 
ATOM   1079 C CB  . ASN A 1 123 ? -32.733 27.536 94.029  1.00 32.95 ? 123 ASN A CB  1 
ATOM   1080 C CG  . ASN A 1 123 ? -33.316 27.869 92.652  1.00 32.26 ? 123 ASN A CG  1 
ATOM   1081 O OD1 . ASN A 1 123 ? -32.909 27.316 91.631  1.00 26.44 ? 123 ASN A OD1 1 
ATOM   1082 N ND2 . ASN A 1 123 ? -34.271 28.800 92.629  1.00 28.96 ? 123 ASN A ND2 1 
ATOM   1083 N N   . ARG A 1 124 ? -32.127 24.680 93.504  1.00 21.62 ? 124 ARG A N   1 
ATOM   1084 C CA  . ARG A 1 124 ? -32.039 23.360 92.889  1.00 22.87 ? 124 ARG A CA  1 
ATOM   1085 C C   . ARG A 1 124 ? -32.252 23.423 91.380  1.00 25.52 ? 124 ARG A C   1 
ATOM   1086 O O   . ARG A 1 124 ? -31.544 22.751 90.617  1.00 21.83 ? 124 ARG A O   1 
ATOM   1087 C CB  . ARG A 1 124 ? -33.061 22.417 93.526  1.00 23.49 ? 124 ARG A CB  1 
ATOM   1088 C CG  . ARG A 1 124 ? -33.004 21.013 92.958  1.00 23.26 ? 124 ARG A CG  1 
ATOM   1089 C CD  . ARG A 1 124 ? -34.019 20.089 93.582  1.00 24.94 ? 124 ARG A CD  1 
ATOM   1090 N NE  . ARG A 1 124 ? -34.026 18.794 92.904  1.00 24.70 ? 124 ARG A NE  1 
ATOM   1091 C CZ  . ARG A 1 124 ? -34.711 18.540 91.793  1.00 30.21 ? 124 ARG A CZ  1 
ATOM   1092 N NH1 . ARG A 1 124 ? -35.436 19.502 91.231  1.00 27.80 ? 124 ARG A NH1 1 
ATOM   1093 N NH2 . ARG A 1 124 ? -34.674 17.331 91.246  1.00 28.90 ? 124 ARG A NH2 1 
ATOM   1094 N N   . GLU A 1 125 ? -33.243 24.201 90.930  1.00 19.36 ? 125 GLU A N   1 
ATOM   1095 C CA  . GLU A 1 125 ? -33.516 24.283 89.495  1.00 21.84 ? 125 GLU A CA  1 
ATOM   1096 C C   . GLU A 1 125 ? -32.379 24.980 88.749  1.00 22.52 ? 125 GLU A C   1 
ATOM   1097 O O   . GLU A 1 125 ? -32.047 24.614 87.614  1.00 19.05 ? 125 GLU A O   1 
ATOM   1098 C CB  . GLU A 1 125 ? -34.851 24.996 89.271  1.00 27.31 ? 125 GLU A CB  1 
ATOM   1099 C CG  . GLU A 1 125 ? -36.035 24.218 89.841  1.00 41.98 ? 125 GLU A CG  1 
ATOM   1100 C CD  . GLU A 1 125 ? -37.386 24.741 89.378  1.00 58.90 ? 125 GLU A CD  1 
ATOM   1101 O OE1 . GLU A 1 125 ? -37.467 25.918 88.960  1.00 62.51 ? 125 GLU A OE1 1 
ATOM   1102 O OE2 . GLU A 1 125 ? -38.372 23.972 89.442  1.00 63.20 ? 125 GLU A OE2 1 
ATOM   1103 N N   . GLU A 1 126 ? -31.767 25.985 89.370  1.00 18.64 ? 126 GLU A N   1 
ATOM   1104 C CA  . GLU A 1 126 ? -30.650 26.658 88.728  1.00 20.66 ? 126 GLU A CA  1 
ATOM   1105 C C   . GLU A 1 126 ? -29.437 25.738 88.645  1.00 21.86 ? 126 GLU A C   1 
ATOM   1106 O O   . GLU A 1 126 ? -28.715 25.742 87.639  1.00 20.66 ? 126 GLU A O   1 
ATOM   1107 C CB  . GLU A 1 126 ? -30.352 27.955 89.485  1.00 21.62 ? 126 GLU A CB  1 
ATOM   1108 C CG  . GLU A 1 126 ? -31.496 28.960 89.279  1.00 24.98 ? 126 GLU A CG  1 
ATOM   1109 C CD  . GLU A 1 126 ? -31.554 30.078 90.308  1.00 32.74 ? 126 GLU A CD  1 
ATOM   1110 O OE1 . GLU A 1 126 ? -30.834 30.013 91.329  1.00 30.82 ? 126 GLU A OE1 1 
ATOM   1111 O OE2 . GLU A 1 126 ? -32.354 31.018 90.094  1.00 37.31 ? 126 GLU A OE2 1 
ATOM   1112 N N   . LEU A 1 127 ? -29.220 24.914 89.680  1.00 19.68 ? 127 LEU A N   1 
ATOM   1113 C CA  . LEU A 1 127 ? -28.103 23.972 89.651  1.00 17.85 ? 127 LEU A CA  1 
ATOM   1114 C C   . LEU A 1 127 ? -28.336 22.861 88.626  1.00 17.30 ? 127 LEU A C   1 
ATOM   1115 O O   . LEU A 1 127 ? -27.385 22.406 87.981  1.00 15.32 ? 127 LEU A O   1 
ATOM   1116 C CB  . LEU A 1 127 ? -27.869 23.374 91.041  1.00 19.06 ? 127 LEU A CB  1 
ATOM   1117 C CG  . LEU A 1 127 ? -27.192 24.284 92.076  1.00 24.68 ? 127 LEU A CG  1 
ATOM   1118 C CD1 . LEU A 1 127 ? -27.218 23.642 93.453  1.00 22.41 ? 127 LEU A CD1 1 
ATOM   1119 C CD2 . LEU A 1 127 ? -25.759 24.614 91.667  1.00 21.18 ? 127 LEU A CD2 1 
ATOM   1120 N N   . LEU A 1 128 ? -29.586 22.402 88.467  1.00 17.14 ? 128 LEU A N   1 
ATOM   1121 C CA  . LEU A 1 128 ? -29.882 21.444 87.398  1.00 15.35 ? 128 LEU A CA  1 
ATOM   1122 C C   . LEU A 1 128 ? -29.536 22.024 86.031  1.00 13.05 ? 128 LEU A C   1 
ATOM   1123 O O   . LEU A 1 128 ? -28.989 21.324 85.166  1.00 15.53 ? 128 LEU A O   1 
ATOM   1124 C CB  . LEU A 1 128 ? -31.357 21.026 87.431  1.00 15.22 ? 128 LEU A CB  1 
ATOM   1125 C CG  . LEU A 1 128 ? -31.774 19.793 88.237  1.00 19.86 ? 128 LEU A CG  1 
ATOM   1126 C CD1 . LEU A 1 128 ? -33.296 19.684 88.302  1.00 23.73 ? 128 LEU A CD1 1 
ATOM   1127 C CD2 . LEU A 1 128 ? -31.179 18.537 87.639  1.00 18.98 ? 128 LEU A CD2 1 
ATOM   1128 N N   . ASP A 1 129 ? -29.860 23.297 85.809  1.00 14.47 ? 129 ASP A N   1 
ATOM   1129 C CA  . ASP A 1 129 ? -29.493 23.924 84.546  1.00 17.70 ? 129 ASP A CA  1 
ATOM   1130 C C   . ASP A 1 129 ? -27.984 24.029 84.404  1.00 14.76 ? 129 ASP A C   1 
ATOM   1131 O O   . ASP A 1 129 ? -27.440 23.742 83.334  1.00 16.27 ? 129 ASP A O   1 
ATOM   1132 C CB  . ASP A 1 129 ? -30.129 25.306 84.411  1.00 16.52 ? 129 ASP A CB  1 
ATOM   1133 C CG  . ASP A 1 129 ? -31.590 25.224 84.093  1.00 24.67 ? 129 ASP A CG  1 
ATOM   1134 O OD1 . ASP A 1 129 ? -32.071 24.081 83.951  1.00 22.77 ? 129 ASP A OD1 1 
ATOM   1135 O OD2 . ASP A 1 129 ? -32.230 26.280 83.897  1.00 25.20 ? 129 ASP A OD2 1 
ATOM   1136 N N   . LEU A 1 130 ? -27.288 24.425 85.474  1.00 16.51 ? 130 LEU A N   1 
ATOM   1137 C CA  . LEU A 1 130 ? -25.827 24.481 85.410  1.00 13.96 ? 130 LEU A CA  1 
ATOM   1138 C C   . LEU A 1 130 ? -25.241 23.115 85.073  1.00 14.87 ? 130 LEU A C   1 
ATOM   1139 O O   . LEU A 1 130 ? -24.341 23.000 84.223  1.00 13.87 ? 130 LEU A O   1 
ATOM   1140 C CB  . LEU A 1 130 ? -25.263 24.982 86.736  1.00 12.58 ? 130 LEU A CB  1 
ATOM   1141 C CG  . LEU A 1 130 ? -23.769 25.296 86.706  1.00 16.18 ? 130 LEU A CG  1 
ATOM   1142 C CD1 . LEU A 1 130 ? -23.554 26.389 85.692  1.00 20.51 ? 130 LEU A CD1 1 
ATOM   1143 C CD2 . LEU A 1 130 ? -23.308 25.762 88.069  1.00 23.16 ? 130 LEU A CD2 1 
ATOM   1144 N N   . GLN A 1 131 ? -25.742 22.070 85.728  1.00 12.71 ? 131 GLN A N   1 
ATOM   1145 C CA  . GLN A 1 131 ? -25.265 20.715 85.458  1.00 15.17 ? 131 GLN A CA  1 
ATOM   1146 C C   . GLN A 1 131 ? -25.544 20.316 84.015  1.00 17.98 ? 131 GLN A C   1 
ATOM   1147 O O   . GLN A 1 131 ? -24.671 19.787 83.316  1.00 13.64 ? 131 GLN A O   1 
ATOM   1148 C CB  . GLN A 1 131 ? -25.955 19.727 86.393  1.00 14.48 ? 131 GLN A CB  1 
ATOM   1149 C CG  . GLN A 1 131 ? -25.489 19.699 87.834  1.00 12.74 ? 131 GLN A CG  1 
ATOM   1150 C CD  . GLN A 1 131 ? -26.421 18.839 88.670  1.00 19.03 ? 131 GLN A CD  1 
ATOM   1151 O OE1 . GLN A 1 131 ? -27.632 18.819 88.438  1.00 15.15 ? 131 GLN A OE1 1 
ATOM   1152 N NE2 . GLN A 1 131 ? -25.860 18.062 89.587  1.00 15.24 ? 131 GLN A NE2 1 
ATOM   1153 N N   . THR A 1 132 ? -26.778 20.527 83.565  1.00 14.00 ? 132 THR A N   1 
ATOM   1154 C CA  . THR A 1 132 ? -27.170 19.982 82.272  1.00 12.75 ? 132 THR A CA  1 
ATOM   1155 C C   . THR A 1 132 ? -26.573 20.798 81.133  1.00 16.11 ? 132 THR A C   1 
ATOM   1156 O O   . THR A 1 132 ? -26.210 20.243 80.093  1.00 15.04 ? 132 THR A O   1 
ATOM   1157 C CB  . THR A 1 132 ? -28.699 19.929 82.161  1.00 12.05 ? 132 THR A CB  1 
ATOM   1158 O OG1 . THR A 1 132 ? -29.246 19.261 83.312  1.00 14.35 ? 132 THR A OG1 1 
ATOM   1159 C CG2 . THR A 1 132 ? -29.117 19.167 80.897  1.00 13.90 ? 132 THR A CG2 1 
ATOM   1160 N N   . LEU A 1 133 ? -26.444 22.114 81.319  1.00 14.16 ? 133 LEU A N   1 
ATOM   1161 C CA  . LEU A 1 133 ? -25.836 22.937 80.279  1.00 15.68 ? 133 LEU A CA  1 
ATOM   1162 C C   . LEU A 1 133 ? -24.353 22.634 80.124  1.00 15.62 ? 133 LEU A C   1 
ATOM   1163 O O   . LEU A 1 133 ? -23.830 22.667 79.003  1.00 14.99 ? 133 LEU A O   1 
ATOM   1164 C CB  . LEU A 1 133 ? -26.060 24.420 80.580  1.00 16.43 ? 133 LEU A CB  1 
ATOM   1165 C CG  . LEU A 1 133 ? -27.475 24.912 80.281  1.00 21.12 ? 133 LEU A CG  1 
ATOM   1166 C CD1 . LEU A 1 133 ? -27.747 26.262 80.941  1.00 20.48 ? 133 LEU A CD1 1 
ATOM   1167 C CD2 . LEU A 1 133 ? -27.677 24.989 78.771  1.00 21.19 ? 133 LEU A CD2 1 
ATOM   1168 N N   . ASN A 1 134 ? -23.651 22.345 81.233  1.00 11.69 ? 134 ASN A N   1 
ATOM   1169 C CA  . ASN A 1 134 ? -22.268 21.870 81.111  1.00 11.42 ? 134 ASN A CA  1 
ATOM   1170 C C   . ASN A 1 134 ? -22.207 20.589 80.280  1.00 18.16 ? 134 ASN A C   1 
ATOM   1171 O O   . ASN A 1 134 ? -21.341 20.443 79.410  1.00 17.71 ? 134 ASN A O   1 
ATOM   1172 C CB  . ASN A 1 134 ? -21.642 21.652 82.494  1.00 10.55 ? 134 ASN A CB  1 
ATOM   1173 C CG  . ASN A 1 134 ? -20.946 22.887 83.012  1.00 14.32 ? 134 ASN A CG  1 
ATOM   1174 O OD1 . ASN A 1 134 ? -19.823 23.191 82.601  1.00 16.55 ? 134 ASN A OD1 1 
ATOM   1175 N ND2 . ASN A 1 134 ? -21.629 23.646 83.856  1.00 15.88 ? 134 ASN A ND2 1 
ATOM   1176 N N   . LEU A 1 135 ? -23.116 19.638 80.540  1.00 13.96 ? 135 LEU A N   1 
ATOM   1177 C CA  . LEU A 1 135 ? -23.169 18.429 79.716  1.00 17.01 ? 135 LEU A CA  1 
ATOM   1178 C C   . LEU A 1 135 ? -23.406 18.771 78.258  1.00 17.11 ? 135 LEU A C   1 
ATOM   1179 O O   . LEU A 1 135 ? -22.667 18.329 77.372  1.00 17.25 ? 135 LEU A O   1 
ATOM   1180 C CB  . LEU A 1 135 ? -24.275 17.483 80.169  1.00 20.75 ? 135 LEU A CB  1 
ATOM   1181 C CG  . LEU A 1 135 ? -24.056 16.286 81.059  1.00 24.17 ? 135 LEU A CG  1 
ATOM   1182 C CD1 . LEU A 1 135 ? -25.375 15.488 81.062  1.00 20.04 ? 135 LEU A CD1 1 
ATOM   1183 C CD2 . LEU A 1 135 ? -22.876 15.446 80.561  1.00 15.75 ? 135 LEU A CD2 1 
ATOM   1184 N N   . LEU A 1 136 ? -24.471 19.533 77.989  1.00 13.65 ? 136 LEU A N   1 
ATOM   1185 C CA  . LEU A 1 136 ? -24.893 19.782 76.614  1.00 11.51 ? 136 LEU A CA  1 
ATOM   1186 C C   . LEU A 1 136 ? -23.885 20.638 75.859  1.00 12.58 ? 136 LEU A C   1 
ATOM   1187 O O   . LEU A 1 136 ? -23.819 20.572 74.627  1.00 14.02 ? 136 LEU A O   1 
ATOM   1188 C CB  . LEU A 1 136 ? -26.265 20.454 76.604  1.00 17.13 ? 136 LEU A CB  1 
ATOM   1189 C CG  . LEU A 1 136 ? -27.435 19.527 76.917  1.00 15.93 ? 136 LEU A CG  1 
ATOM   1190 C CD1 . LEU A 1 136 ? -28.706 20.348 77.084  1.00 14.79 ? 136 LEU A CD1 1 
ATOM   1191 C CD2 . LEU A 1 136 ? -27.595 18.514 75.793  1.00 16.88 ? 136 LEU A CD2 1 
ATOM   1192 N N   . ALA A 1 137 ? -23.107 21.458 76.570  1.00 14.95 ? 137 ALA A N   1 
ATOM   1193 C CA  . ALA A 1 137 ? -22.089 22.253 75.891  1.00 16.45 ? 137 ALA A CA  1 
ATOM   1194 C C   . ALA A 1 137 ? -21.114 21.373 75.116  1.00 14.11 ? 137 ALA A C   1 
ATOM   1195 O O   . ALA A 1 137 ? -20.587 21.788 74.079  1.00 14.70 ? 137 ALA A O   1 
ATOM   1196 C CB  . ALA A 1 137 ? -21.330 23.119 76.904  1.00 17.75 ? 137 ALA A CB  1 
ATOM   1197 N N   . TRP A 1 138 ? -20.884 20.149 75.579  1.00 10.83 ? 138 TRP A N   1 
ATOM   1198 C CA  . TRP A 1 138 ? -19.920 19.269 74.936  1.00 13.90 ? 138 TRP A CA  1 
ATOM   1199 C C   . TRP A 1 138 ? -20.590 18.297 73.985  1.00 13.03 ? 138 TRP A C   1 
ATOM   1200 O O   . TRP A 1 138 ? -19.983 17.296 73.605  1.00 13.58 ? 138 TRP A O   1 
ATOM   1201 C CB  . TRP A 1 138 ? -19.095 18.524 75.994  1.00 15.12 ? 138 TRP A CB  1 
ATOM   1202 C CG  . TRP A 1 138 ? -18.315 19.481 76.822  1.00 14.78 ? 138 TRP A CG  1 
ATOM   1203 C CD1 . TRP A 1 138 ? -18.734 20.105 77.966  1.00 17.92 ? 138 TRP A CD1 1 
ATOM   1204 C CD2 . TRP A 1 138 ? -16.987 19.968 76.568  1.00 12.24 ? 138 TRP A CD2 1 
ATOM   1205 N NE1 . TRP A 1 138 ? -17.746 20.925 78.446  1.00 17.95 ? 138 TRP A NE1 1 
ATOM   1206 C CE2 . TRP A 1 138 ? -16.664 20.864 77.608  1.00 17.33 ? 138 TRP A CE2 1 
ATOM   1207 C CE3 . TRP A 1 138 ? -16.031 19.715 75.580  1.00 16.04 ? 138 TRP A CE3 1 
ATOM   1208 C CZ2 . TRP A 1 138 ? -15.431 21.526 77.676  1.00 17.76 ? 138 TRP A CZ2 1 
ATOM   1209 C CZ3 . TRP A 1 138 ? -14.804 20.384 75.651  1.00 15.86 ? 138 TRP A CZ3 1 
ATOM   1210 C CH2 . TRP A 1 138 ? -14.521 21.270 76.690  1.00 20.51 ? 138 TRP A CH2 1 
ATOM   1211 N N   . CYS A 1 139 ? -21.813 18.597 73.561  1.00 14.35 ? 139 CYS A N   1 
ATOM   1212 C CA  . CYS A 1 139 ? -22.533 17.679 72.693  1.00 13.55 ? 139 CYS A CA  1 
ATOM   1213 C C   . CYS A 1 139 ? -21.838 17.612 71.341  1.00 15.04 ? 139 CYS A C   1 
ATOM   1214 O O   . CYS A 1 139 ? -21.456 18.641 70.774  1.00 14.11 ? 139 CYS A O   1 
ATOM   1215 C CB  . CYS A 1 139 ? -23.979 18.126 72.543  1.00 14.43 ? 139 CYS A CB  1 
ATOM   1216 S SG  . CYS A 1 139 ? -25.027 16.909 71.717  1.00 17.30 ? 139 CYS A SG  1 
ATOM   1217 N N   . GLY A 1 140 ? -21.650 16.397 70.831  1.00 13.46 ? 140 GLY A N   1 
ATOM   1218 C CA  . GLY A 1 140 ? -21.034 16.224 69.534  1.00 14.77 ? 140 GLY A CA  1 
ATOM   1219 C C   . GLY A 1 140 ? -22.037 16.323 68.394  1.00 14.35 ? 140 GLY A C   1 
ATOM   1220 O O   . GLY A 1 140 ? -23.245 16.464 68.582  1.00 15.37 ? 140 GLY A O   1 
ATOM   1221 N N   . ARG A 1 141 ? -21.496 16.252 67.178  1.00 10.50 ? 141 ARG A N   1 
ATOM   1222 C CA  . ARG A 1 141 ? -22.293 16.475 65.971  1.00 15.67 ? 141 ARG A CA  1 
ATOM   1223 C C   . ARG A 1 141 ? -23.469 15.512 65.883  1.00 15.74 ? 141 ARG A C   1 
ATOM   1224 O O   . ARG A 1 141 ? -24.593 15.916 65.551  1.00 14.53 ? 141 ARG A O   1 
ATOM   1225 C CB  . ARG A 1 141 ? -21.403 16.341 64.736  1.00 13.62 ? 141 ARG A CB  1 
ATOM   1226 C CG  . ARG A 1 141 ? -22.135 16.446 63.415  1.00 14.42 ? 141 ARG A CG  1 
ATOM   1227 C CD  . ARG A 1 141 ? -21.124 16.449 62.270  1.00 11.63 ? 141 ARG A CD  1 
ATOM   1228 N NE  . ARG A 1 141 ? -21.765 16.306 60.972  1.00 20.16 ? 141 ARG A NE  1 
ATOM   1229 C CZ  . ARG A 1 141 ? -21.883 15.163 60.295  1.00 19.27 ? 141 ARG A CZ  1 
ATOM   1230 N NH1 . ARG A 1 141 ? -22.508 15.170 59.127  1.00 20.65 ? 141 ARG A NH1 1 
ATOM   1231 N NH2 . ARG A 1 141 ? -21.380 14.020 60.773  1.00 20.95 ? 141 ARG A NH2 1 
ATOM   1232 N N   . THR A 1 142 ? -23.224 14.227 66.146  1.00 14.00 ? 142 THR A N   1 
ATOM   1233 C CA  . THR A 1 142 ? -24.278 13.225 65.979  1.00 16.33 ? 142 THR A CA  1 
ATOM   1234 C C   . THR A 1 142 ? -25.462 13.513 66.888  1.00 16.90 ? 142 THR A C   1 
ATOM   1235 O O   . THR A 1 142 ? -26.617 13.527 66.440  1.00 19.53 ? 142 THR A O   1 
ATOM   1236 C CB  . THR A 1 142 ? -23.725 11.826 66.267  1.00 14.44 ? 142 THR A CB  1 
ATOM   1237 O OG1 . THR A 1 142 ? -22.702 11.514 65.314  1.00 18.51 ? 142 THR A OG1 1 
ATOM   1238 C CG2 . THR A 1 142 ? -24.835 10.764 66.222  1.00 16.48 ? 142 THR A CG2 1 
ATOM   1239 N N   . LEU A 1 143 ? -25.197 13.747 68.175  1.00 14.33 ? 143 LEU A N   1 
ATOM   1240 C CA  . LEU A 1 143 ? -26.303 13.961 69.102  1.00 15.99 ? 143 LEU A CA  1 
ATOM   1241 C C   . LEU A 1 143 ? -26.810 15.393 69.069  1.00 18.88 ? 143 LEU A C   1 
ATOM   1242 O O   . LEU A 1 143 ? -27.910 15.668 69.558  1.00 20.43 ? 143 LEU A O   1 
ATOM   1243 C CB  . LEU A 1 143 ? -25.884 13.570 70.513  1.00 16.63 ? 143 LEU A CB  1 
ATOM   1244 C CG  . LEU A 1 143 ? -25.713 12.066 70.729  1.00 18.54 ? 143 LEU A CG  1 
ATOM   1245 C CD1 . LEU A 1 143 ? -25.277 11.799 72.156  1.00 14.76 ? 143 LEU A CD1 1 
ATOM   1246 C CD2 . LEU A 1 143 ? -27.008 11.333 70.402  1.00 17.22 ? 143 LEU A CD2 1 
ATOM   1247 N N   . ARG A 1 144 ? -26.068 16.298 68.436  1.00 15.44 ? 144 ARG A N   1 
ATOM   1248 C CA  . ARG A 1 144 ? -26.545 17.662 68.263  1.00 15.69 ? 144 ARG A CA  1 
ATOM   1249 C C   . ARG A 1 144 ? -27.764 17.605 67.334  1.00 21.99 ? 144 ARG A C   1 
ATOM   1250 O O   . ARG A 1 144 ? -28.640 18.398 67.427  1.00 17.76 ? 144 ARG A O   1 
ATOM   1251 C CB  . ARG A 1 144 ? -25.506 18.585 67.654  1.00 31.06 ? 144 ARG A CB  1 
ATOM   1252 C CG  . ARG A 1 144 ? -24.869 19.521 68.658  1.00 44.00 ? 144 ARG A CG  1 
ATOM   1253 C CD  . ARG A 1 144 ? -23.558 20.132 68.222  1.00 41.08 ? 144 ARG A CD  1 
ATOM   1254 N NE  . ARG A 1 144 ? -22.858 20.765 69.314  1.00 32.12 ? 144 ARG A NE  1 
ATOM   1255 C CZ  . ARG A 1 144 ? -23.025 22.022 69.682  1.00 30.29 ? 144 ARG A CZ  1 
ATOM   1256 N NH1 . ARG A 1 144 ? -23.888 22.808 69.074  1.00 24.96 ? 144 ARG A NH1 1 
ATOM   1257 N NH2 . ARG A 1 144 ? -22.363 22.470 70.693  1.00 27.74 ? 144 ARG A NH2 1 
ATOM   1258 N N   . LYS A 1 145 ? -27.749 16.644 66.432  1.00 20.70 ? 145 LYS A N   1 
ATOM   1259 C CA  . LYS A 1 145 ? -28.918 16.467 65.584  1.00 23.83 ? 145 LYS A CA  1 
ATOM   1260 C C   . LYS A 1 145 ? -30.033 15.740 66.332  1.00 24.16 ? 145 LYS A C   1 
ATOM   1261 O O   . LYS A 1 145 ? -31.181 16.195 66.332  1.00 26.20 ? 145 LYS A O   1 
ATOM   1262 C CB  . LYS A 1 145 ? -28.523 15.717 64.310  1.00 27.72 ? 145 LYS A CB  1 
ATOM   1263 C CG  . LYS A 1 145 ? -27.413 16.405 63.519  1.00 36.93 ? 145 LYS A CG  1 
ATOM   1264 C CD  . LYS A 1 145 ? -27.068 15.638 62.240  1.00 45.01 ? 145 LYS A CD  1 
ATOM   1265 C CE  . LYS A 1 145 ? -25.768 16.135 61.612  1.00 47.45 ? 145 LYS A CE  1 
ATOM   1266 N NZ  . LYS A 1 145 ? -25.842 17.559 61.167  1.00 49.34 ? 145 LYS A NZ  1 
ATOM   1267 N N   . ASP A 1 146 ? -29.707 14.630 67.004  1.00 26.81 ? 146 ASP A N   1 
ATOM   1268 C CA  . ASP A 1 146 ? -30.732 13.851 67.701  1.00 29.13 ? 146 ASP A CA  1 
ATOM   1269 C C   . ASP A 1 146 ? -31.345 14.609 68.875  1.00 30.61 ? 146 ASP A C   1 
ATOM   1270 O O   . ASP A 1 146 ? -32.531 14.437 69.166  1.00 36.09 ? 146 ASP A O   1 
ATOM   1271 C CB  . ASP A 1 146 ? -30.160 12.522 68.207  1.00 32.45 ? 146 ASP A CB  1 
ATOM   1272 C CG  . ASP A 1 146 ? -29.567 11.665 67.096  1.00 45.57 ? 146 ASP A CG  1 
ATOM   1273 O OD1 . ASP A 1 146 ? -29.772 11.978 65.906  1.00 51.89 ? 146 ASP A OD1 1 
ATOM   1274 O OD2 . ASP A 1 146 ? -28.903 10.658 67.419  1.00 49.16 ? 146 ASP A OD2 1 
ATOM   1275 N N   . LEU A 1 147 ? -30.565 15.437 69.567  1.00 23.28 ? 147 LEU A N   1 
ATOM   1276 C CA  . LEU A 1 147 ? -31.016 16.122 70.771  1.00 25.00 ? 147 LEU A CA  1 
ATOM   1277 C C   . LEU A 1 147 ? -31.277 17.602 70.528  1.00 20.77 ? 147 LEU A C   1 
ATOM   1278 O O   . LEU A 1 147 ? -31.273 18.387 71.479  1.00 23.59 ? 147 LEU A O   1 
ATOM   1279 C CB  . LEU A 1 147 ? -29.987 15.953 71.890  1.00 24.27 ? 147 LEU A CB  1 
ATOM   1280 C CG  . LEU A 1 147 ? -29.645 14.509 72.270  1.00 30.78 ? 147 LEU A CG  1 
ATOM   1281 C CD1 . LEU A 1 147 ? -28.529 14.475 73.304  1.00 27.52 ? 147 LEU A CD1 1 
ATOM   1282 C CD2 . LEU A 1 147 ? -30.873 13.790 72.783  1.00 37.72 ? 147 LEU A CD2 1 
ATOM   1283 N N   . LYS A 1 148 ? -31.478 17.993 69.266  1.00 20.00 ? 148 LYS A N   1 
ATOM   1284 C CA  . LYS A 1 148 ? -31.569 19.407 68.890  1.00 22.66 ? 148 LYS A CA  1 
ATOM   1285 C C   . LYS A 1 148 ? -32.587 20.173 69.732  1.00 29.73 ? 148 LYS A C   1 
ATOM   1286 O O   . LYS A 1 148 ? -32.356 21.331 70.111  1.00 27.77 ? 148 LYS A O   1 
ATOM   1287 C CB  . LYS A 1 148 ? -31.927 19.507 67.402  1.00 29.15 ? 148 LYS A CB  1 
ATOM   1288 C CG  . LYS A 1 148 ? -32.545 20.830 66.985  1.00 39.27 ? 148 LYS A CG  1 
ATOM   1289 C CD  . LYS A 1 148 ? -32.676 20.936 65.469  1.00 48.09 ? 148 LYS A CD  1 
ATOM   1290 C CE  . LYS A 1 148 ? -33.636 19.889 64.921  1.00 55.20 ? 148 LYS A CE  1 
ATOM   1291 N NZ  . LYS A 1 148 ? -33.836 20.027 63.445  1.00 59.70 ? 148 LYS A NZ  1 
ATOM   1292 N N   . ASP A 1 149 ? -33.720 19.542 70.035  1.00 25.34 ? 149 ASP A N   1 
ATOM   1293 C CA  . ASP A 1 149 ? -34.780 20.244 70.748  1.00 30.85 ? 149 ASP A CA  1 
ATOM   1294 C C   . ASP A 1 149 ? -34.405 20.516 72.203  1.00 27.54 ? 149 ASP A C   1 
ATOM   1295 O O   . ASP A 1 149 ? -34.729 21.585 72.733  1.00 24.43 ? 149 ASP A O   1 
ATOM   1296 C CB  . ASP A 1 149 ? -36.065 19.441 70.647  1.00 35.84 ? 149 ASP A CB  1 
ATOM   1297 C CG  . ASP A 1 149 ? -36.525 19.277 69.211  1.00 39.14 ? 149 ASP A CG  1 
ATOM   1298 O OD1 . ASP A 1 149 ? -36.454 20.261 68.430  1.00 35.22 ? 149 ASP A OD1 1 
ATOM   1299 O OD2 . ASP A 1 149 ? -36.907 18.144 68.854  1.00 41.81 ? 149 ASP A OD2 1 
ATOM   1300 N N   . LEU A 1 150 ? -33.732 19.565 72.871  1.00 24.27 ? 150 LEU A N   1 
ATOM   1301 C CA  . LEU A 1 150 ? -33.255 19.825 74.229  1.00 25.88 ? 150 LEU A CA  1 
ATOM   1302 C C   . LEU A 1 150 ? -32.190 20.913 74.243  1.00 26.42 ? 150 LEU A C   1 
ATOM   1303 O O   . LEU A 1 150 ? -32.160 21.743 75.158  1.00 25.42 ? 150 LEU A O   1 
ATOM   1304 C CB  . LEU A 1 150 ? -32.689 18.558 74.878  1.00 26.54 ? 150 LEU A CB  1 
ATOM   1305 C CG  . LEU A 1 150 ? -33.626 17.459 75.379  1.00 31.64 ? 150 LEU A CG  1 
ATOM   1306 C CD1 . LEU A 1 150 ? -32.800 16.276 75.885  1.00 23.39 ? 150 LEU A CD1 1 
ATOM   1307 C CD2 . LEU A 1 150 ? -34.556 17.986 76.472  1.00 29.80 ? 150 LEU A CD2 1 
ATOM   1308 N N   . LEU A 1 151 ? -31.292 20.908 73.250  1.00 26.44 ? 151 LEU A N   1 
ATOM   1309 C CA  . LEU A 1 151 ? -30.278 21.954 73.146  1.00 27.72 ? 151 LEU A CA  1 
ATOM   1310 C C   . LEU A 1 151 ? -30.905 23.335 73.011  1.00 29.50 ? 151 LEU A C   1 
ATOM   1311 O O   . LEU A 1 151 ? -30.493 24.282 73.689  1.00 26.65 ? 151 LEU A O   1 
ATOM   1312 C CB  . LEU A 1 151 ? -29.359 21.678 71.957  1.00 33.77 ? 151 LEU A CB  1 
ATOM   1313 C CG  . LEU A 1 151 ? -28.130 20.817 72.220  1.00 33.09 ? 151 LEU A CG  1 
ATOM   1314 C CD1 . LEU A 1 151 ? -27.525 20.359 70.902  1.00 42.87 ? 151 LEU A CD1 1 
ATOM   1315 C CD2 . LEU A 1 151 ? -27.113 21.604 73.034  1.00 26.27 ? 151 LEU A CD2 1 
ATOM   1316 N N   . ASN A 1 152 ? -31.893 23.480 72.118  1.00 27.61 ? 152 ASN A N   1 
ATOM   1317 C CA  . ASN A 1 152 ? -32.519 24.787 71.906  1.00 30.14 ? 152 ASN A CA  1 
ATOM   1318 C C   . ASN A 1 152 ? -33.331 25.252 73.103  1.00 29.00 ? 152 ASN A C   1 
ATOM   1319 O O   . ASN A 1 152 ? -33.568 26.455 73.252  1.00 34.44 ? 152 ASN A O   1 
ATOM   1320 C CB  . ASN A 1 152 ? -33.424 24.757 70.675  1.00 37.72 ? 152 ASN A CB  1 
ATOM   1321 C CG  . ASN A 1 152 ? -32.646 24.813 69.386  1.00 49.90 ? 152 ASN A CG  1 
ATOM   1322 O OD1 . ASN A 1 152 ? -31.523 25.319 69.351  1.00 50.11 ? 152 ASN A OD1 1 
ATOM   1323 N ND2 . ASN A 1 152 ? -33.244 24.315 68.307  1.00 57.63 ? 152 ASN A ND2 1 
ATOM   1324 N N   . LYS A 1 153 ? -33.788 24.326 73.941  1.00 28.13 ? 153 LYS A N   1 
ATOM   1325 C CA  . LYS A 1 153 ? -34.464 24.699 75.177  1.00 28.56 ? 153 LYS A CA  1 
ATOM   1326 C C   . LYS A 1 153 ? -33.615 25.688 75.977  1.00 30.04 ? 153 LYS A C   1 
ATOM   1327 O O   . LYS A 1 153 ? -34.087 26.760 76.374  1.00 26.31 ? 153 LYS A O   1 
ATOM   1328 C CB  . LYS A 1 153 ? -34.750 23.427 75.974  1.00 32.20 ? 153 LYS A CB  1 
ATOM   1329 C CG  . LYS A 1 153 ? -35.568 23.596 77.204  1.00 38.53 ? 153 LYS A CG  1 
ATOM   1330 C CD  . LYS A 1 153 ? -35.707 22.265 77.924  1.00 32.25 ? 153 LYS A CD  1 
ATOM   1331 C CE  . LYS A 1 153 ? -36.510 22.446 79.193  1.00 31.66 ? 153 LYS A CE  1 
ATOM   1332 N NZ  . LYS A 1 153 ? -36.663 21.161 79.921  1.00 42.90 ? 153 LYS A NZ  1 
ATOM   1333 N N   . GLY A 1 154 ? -32.351 25.340 76.216  1.00 28.28 ? 154 GLY A N   1 
ATOM   1334 C CA  . GLY A 1 154 ? -31.397 26.242 76.823  1.00 24.58 ? 154 GLY A CA  1 
ATOM   1335 C C   . GLY A 1 154 ? -31.575 26.524 78.297  1.00 23.44 ? 154 GLY A C   1 
ATOM   1336 O O   . GLY A 1 154 ? -30.756 27.253 78.861  1.00 27.55 ? 154 GLY A O   1 
ATOM   1337 N N   . ARG A 1 155 ? -32.598 25.978 78.950  1.00 22.79 ? 155 ARG A N   1 
ATOM   1338 C CA  . ARG A 1 155 ? -32.890 26.317 80.338  1.00 22.00 ? 155 ARG A CA  1 
ATOM   1339 C C   . ARG A 1 155 ? -33.954 25.354 80.842  1.00 18.50 ? 155 ARG A C   1 
ATOM   1340 O O   . ARG A 1 155 ? -34.557 24.616 80.062  1.00 25.39 ? 155 ARG A O   1 
ATOM   1341 C CB  . ARG A 1 155 ? -33.381 27.761 80.467  1.00 23.14 ? 155 ARG A CB  1 
ATOM   1342 C CG  . ARG A 1 155 ? -34.660 28.005 79.660  1.00 33.37 ? 155 ARG A CG  1 
ATOM   1343 C CD  . ARG A 1 155 ? -35.144 29.442 79.735  1.00 39.96 ? 155 ARG A CD  1 
ATOM   1344 N NE  . ARG A 1 155 ? -34.166 30.382 79.195  1.00 42.34 ? 155 ARG A NE  1 
ATOM   1345 C CZ  . ARG A 1 155 ? -33.482 31.253 79.931  1.00 38.12 ? 155 ARG A CZ  1 
ATOM   1346 N NH1 . ARG A 1 155 ? -32.606 32.072 79.353  1.00 42.33 ? 155 ARG A NH1 1 
ATOM   1347 N NH2 . ARG A 1 155 ? -33.670 31.306 81.241  1.00 31.19 ? 155 ARG A NH2 1 
ATOM   1348 N N   . ASN A 1 156 ? -34.176 25.371 82.157  1.00 19.42 ? 156 ASN A N   1 
ATOM   1349 C CA  . ASN A 1 156 ? -35.302 24.658 82.772  1.00 21.27 ? 156 ASN A CA  1 
ATOM   1350 C C   . ASN A 1 156 ? -35.207 23.149 82.548  1.00 24.38 ? 156 ASN A C   1 
ATOM   1351 O O   . ASN A 1 156 ? -36.208 22.481 82.270  1.00 21.71 ? 156 ASN A O   1 
ATOM   1352 C CB  . ASN A 1 156 ? -36.639 25.183 82.243  1.00 25.08 ? 156 ASN A CB  1 
ATOM   1353 C CG  . ASN A 1 156 ? -36.835 26.657 82.518  1.00 32.81 ? 156 ASN A CG  1 
ATOM   1354 O OD1 . ASN A 1 156 ? -36.463 27.156 83.584  1.00 31.47 ? 156 ASN A OD1 1 
ATOM   1355 N ND2 . ASN A 1 156 ? -37.415 27.367 81.552  1.00 37.50 ? 156 ASN A ND2 1 
ATOM   1356 N N   . TYR A 1 157 ? -34.003 22.608 82.663  1.00 18.97 ? 157 TYR A N   1 
ATOM   1357 C CA  . TYR A 1 157 ? -33.807 21.178 82.496  1.00 18.84 ? 157 TYR A CA  1 
ATOM   1358 C C   . TYR A 1 157 ? -34.227 20.416 83.753  1.00 20.93 ? 157 TYR A C   1 
ATOM   1359 O O   . TYR A 1 157 ? -34.132 20.921 84.876  1.00 18.90 ? 157 TYR A O   1 
ATOM   1360 C CB  . TYR A 1 157 ? -32.345 20.886 82.160  1.00 18.18 ? 157 TYR A CB  1 
ATOM   1361 C CG  . TYR A 1 157 ? -31.941 21.445 80.813  1.00 17.58 ? 157 TYR A CG  1 
ATOM   1362 C CD1 . TYR A 1 157 ? -32.325 20.805 79.636  1.00 19.60 ? 157 TYR A CD1 1 
ATOM   1363 C CD2 . TYR A 1 157 ? -31.197 22.612 80.715  1.00 14.93 ? 157 TYR A CD2 1 
ATOM   1364 C CE1 . TYR A 1 157 ? -31.969 21.316 78.390  1.00 20.13 ? 157 TYR A CE1 1 
ATOM   1365 C CE2 . TYR A 1 157 ? -30.832 23.127 79.483  1.00 19.00 ? 157 TYR A CE2 1 
ATOM   1366 C CZ  . TYR A 1 157 ? -31.216 22.478 78.326  1.00 22.84 ? 157 TYR A CZ  1 
ATOM   1367 O OH  . TYR A 1 157 ? -30.844 22.997 77.109  1.00 20.90 ? 157 TYR A OH  1 
ATOM   1368 N N   . THR A 1 158 ? -34.715 19.199 83.550  1.00 13.89 ? 158 THR A N   1 
ATOM   1369 C CA  . THR A 1 158 ? -35.106 18.313 84.639  1.00 14.64 ? 158 THR A CA  1 
ATOM   1370 C C   . THR A 1 158 ? -34.058 17.227 84.825  1.00 15.09 ? 158 THR A C   1 
ATOM   1371 O O   . THR A 1 158 ? -33.217 16.990 83.959  1.00 16.06 ? 158 THR A O   1 
ATOM   1372 C CB  . THR A 1 158 ? -36.462 17.660 84.366  1.00 14.90 ? 158 THR A CB  1 
ATOM   1373 O OG1 . THR A 1 158 ? -36.355 16.805 83.217  1.00 14.75 ? 158 THR A OG1 1 
ATOM   1374 C CG2 . THR A 1 158 ? -37.540 18.717 84.136  1.00 15.79 ? 158 THR A CG2 1 
ATOM   1375 N N   . GLN A 1 159 ? -34.141 16.539 85.970  1.00 14.53 ? 159 GLN A N   1 
ATOM   1376 C CA  . GLN A 1 159 ? -33.207 15.454 86.246  1.00 16.58 ? 159 GLN A CA  1 
ATOM   1377 C C   . GLN A 1 159 ? -33.331 14.355 85.195  1.00 17.25 ? 159 GLN A C   1 
ATOM   1378 O O   . GLN A 1 159 ? -32.324 13.805 84.733  1.00 14.84 ? 159 GLN A O   1 
ATOM   1379 C CB  . GLN A 1 159 ? -33.470 14.905 87.649  1.00 15.69 ? 159 GLN A CB  1 
ATOM   1380 C CG  . GLN A 1 159 ? -32.618 13.713 88.067  1.00 14.79 ? 159 GLN A CG  1 
ATOM   1381 C CD  . GLN A 1 159 ? -31.143 14.049 88.271  1.00 17.33 ? 159 GLN A CD  1 
ATOM   1382 O OE1 . GLN A 1 159 ? -30.781 15.183 88.607  1.00 19.67 ? 159 GLN A OE1 1 
ATOM   1383 N NE2 . GLN A 1 159 ? -30.285 13.043 88.097  1.00 16.19 ? 159 GLN A NE2 1 
ATOM   1384 N N   . GLU A 1 160 ? -34.565 14.046 84.785  1.00 14.93 ? 160 GLU A N   1 
ATOM   1385 C CA  . GLU A 1 160 ? -34.793 13.023 83.766  1.00 17.17 ? 160 GLU A CA  1 
ATOM   1386 C C   . GLU A 1 160 ? -34.150 13.405 82.441  1.00 17.03 ? 160 GLU A C   1 
ATOM   1387 O O   . GLU A 1 160 ? -33.547 12.561 81.768  1.00 15.46 ? 160 GLU A O   1 
ATOM   1388 C CB  . GLU A 1 160 ? -36.295 12.797 83.586  1.00 19.09 ? 160 GLU A CB  1 
ATOM   1389 C CG  . GLU A 1 160 ? -36.679 12.021 82.346  1.00 27.07 ? 160 GLU A CG  1 
ATOM   1390 C CD  . GLU A 1 160 ? -36.114 10.628 82.338  1.00 47.23 ? 160 GLU A CD  1 
ATOM   1391 O OE1 . GLU A 1 160 ? -35.927 10.061 83.437  1.00 49.95 ? 160 GLU A OE1 1 
ATOM   1392 O OE2 . GLU A 1 160 ? -35.859 10.102 81.229  1.00 60.13 ? 160 GLU A OE2 1 
ATOM   1393 N N   . GLU A 1 161 ? -34.290 14.670 82.032  1.00 13.33 ? 161 GLU A N   1 
ATOM   1394 C CA  . GLU A 1 161 ? -33.664 15.105 80.787  1.00 13.34 ? 161 GLU A CA  1 
ATOM   1395 C C   . GLU A 1 161 ? -32.147 15.011 80.875  1.00 16.32 ? 161 GLU A C   1 
ATOM   1396 O O   . GLU A 1 161 ? -31.485 14.572 79.927  1.00 14.53 ? 161 GLU A O   1 
ATOM   1397 C CB  . GLU A 1 161 ? -34.093 16.532 80.459  1.00 15.42 ? 161 GLU A CB  1 
ATOM   1398 C CG  . GLU A 1 161 ? -35.530 16.617 79.995  1.00 14.32 ? 161 GLU A CG  1 
ATOM   1399 C CD  . GLU A 1 161 ? -36.065 18.036 79.949  1.00 21.54 ? 161 GLU A CD  1 
ATOM   1400 O OE1 . GLU A 1 161 ? -35.425 18.954 80.504  1.00 17.31 ? 161 GLU A OE1 1 
ATOM   1401 O OE2 . GLU A 1 161 ? -37.140 18.228 79.365  1.00 24.92 ? 161 GLU A OE2 1 
ATOM   1402 N N   . LYS A 1 162 ? -31.578 15.408 82.013  1.00 11.68 ? 162 LYS A N   1 
ATOM   1403 C CA  . LYS A 1 162 ? -30.137 15.271 82.204  1.00 10.96 ? 162 LYS A CA  1 
ATOM   1404 C C   . LYS A 1 162 ? -29.691 13.814 82.088  1.00 11.59 ? 162 LYS A C   1 
ATOM   1405 O O   . LYS A 1 162 ? -28.696 13.503 81.419  1.00 11.79 ? 162 LYS A O   1 
ATOM   1406 C CB  . LYS A 1 162 ? -29.754 15.861 83.561  1.00 10.93 ? 162 LYS A CB  1 
ATOM   1407 C CG  . LYS A 1 162 ? -28.282 15.854 83.856  1.00 15.33 ? 162 LYS A CG  1 
ATOM   1408 C CD  . LYS A 1 162 ? -28.027 16.566 85.206  1.00 18.07 ? 162 LYS A CD  1 
ATOM   1409 C CE  . LYS A 1 162 ? -28.649 15.779 86.334  1.00 16.61 ? 162 LYS A CE  1 
ATOM   1410 N NZ  . LYS A 1 162 ? -28.263 16.294 87.700  1.00 16.26 ? 162 LYS A NZ  1 
ATOM   1411 N N   . GLU A 1 163 ? -30.407 12.906 82.752  1.00 11.88 ? 163 GLU A N   1 
ATOM   1412 C CA  . GLU A 1 163 ? -30.048 11.491 82.712  1.00 11.38 ? 163 GLU A CA  1 
ATOM   1413 C C   . GLU A 1 163 ? -30.225 10.911 81.313  1.00 18.45 ? 163 GLU A C   1 
ATOM   1414 O O   . GLU A 1 163 ? -29.459 10.029 80.902  1.00 16.79 ? 163 GLU A O   1 
ATOM   1415 C CB  . GLU A 1 163 ? -30.901 10.726 83.737  1.00 16.46 ? 163 GLU A CB  1 
ATOM   1416 C CG  . GLU A 1 163 ? -30.472 10.966 85.183  1.00 27.06 ? 163 GLU A CG  1 
ATOM   1417 C CD  . GLU A 1 163 ? -31.422 10.351 86.204  1.00 36.03 ? 163 GLU A CD  1 
ATOM   1418 O OE1 . GLU A 1 163 ? -32.367 9.653  85.789  1.00 39.20 ? 163 GLU A OE1 1 
ATOM   1419 O OE2 . GLU A 1 163 ? -31.223 10.567 87.419  1.00 39.93 ? 163 GLU A OE2 1 
ATOM   1420 N N   . TYR A 1 164 ? -31.217 11.403 80.569  1.00 14.20 ? 164 TYR A N   1 
ATOM   1421 C CA  . TYR A 1 164 ? -31.385 11.009 79.171  1.00 12.44 ? 164 TYR A CA  1 
ATOM   1422 C C   . TYR A 1 164 ? -30.162 11.389 78.344  1.00 16.11 ? 164 TYR A C   1 
ATOM   1423 O O   . TYR A 1 164 ? -29.649 10.581 77.564  1.00 15.52 ? 164 TYR A O   1 
ATOM   1424 C CB  . TYR A 1 164 ? -32.633 11.677 78.602  1.00 16.74 ? 164 TYR A CB  1 
ATOM   1425 C CG  . TYR A 1 164 ? -32.918 11.289 77.170  1.00 16.78 ? 164 TYR A CG  1 
ATOM   1426 C CD1 . TYR A 1 164 ? -33.374 10.021 76.868  1.00 25.42 ? 164 TYR A CD1 1 
ATOM   1427 C CD2 . TYR A 1 164 ? -32.723 12.188 76.128  1.00 24.44 ? 164 TYR A CD2 1 
ATOM   1428 C CE1 . TYR A 1 164 ? -33.642 9.650  75.562  1.00 32.21 ? 164 TYR A CE1 1 
ATOM   1429 C CE2 . TYR A 1 164 ? -32.987 11.824 74.811  1.00 30.31 ? 164 TYR A CE2 1 
ATOM   1430 C CZ  . TYR A 1 164 ? -33.445 10.548 74.540  1.00 34.16 ? 164 TYR A CZ  1 
ATOM   1431 O OH  . TYR A 1 164 ? -33.716 10.159 73.245  1.00 40.97 ? 164 TYR A OH  1 
ATOM   1432 N N   . VAL A 1 165 ? -29.698 12.633 78.491  1.00 14.09 ? 165 VAL A N   1 
ATOM   1433 C CA  . VAL A 1 165 ? -28.508 13.081 77.772  1.00 12.97 ? 165 VAL A CA  1 
ATOM   1434 C C   . VAL A 1 165 ? -27.304 12.220 78.154  1.00 16.56 ? 165 VAL A C   1 
ATOM   1435 O O   . VAL A 1 165 ? -26.532 11.783 77.291  1.00 15.34 ? 165 VAL A O   1 
ATOM   1436 C CB  . VAL A 1 165 ? -28.244 14.576 78.049  1.00 17.40 ? 165 VAL A CB  1 
ATOM   1437 C CG1 . VAL A 1 165 ? -26.886 15.019 77.451  1.00 16.77 ? 165 VAL A CG1 1 
ATOM   1438 C CG2 . VAL A 1 165 ? -29.376 15.441 77.513  1.00 16.02 ? 165 VAL A CG2 1 
ATOM   1439 N N   . LEU A 1 166 ? -27.118 11.978 79.457  1.00 16.08 ? 166 LEU A N   1 
ATOM   1440 C CA  . LEU A 1 166 ? -26.001 11.154 79.915  1.00 14.14 ? 166 LEU A CA  1 
ATOM   1441 C C   . LEU A 1 166 ? -26.035 9.775  79.276  1.00 14.00 ? 166 LEU A C   1 
ATOM   1442 O O   . LEU A 1 166 ? -24.997 9.245  78.860  1.00 15.30 ? 166 LEU A O   1 
ATOM   1443 C CB  . LEU A 1 166 ? -26.028 11.016 81.439  1.00 16.81 ? 166 LEU A CB  1 
ATOM   1444 C CG  . LEU A 1 166 ? -25.402 12.149 82.251  1.00 25.14 ? 166 LEU A CG  1 
ATOM   1445 C CD1 . LEU A 1 166 ? -25.751 12.015 83.727  1.00 29.48 ? 166 LEU A CD1 1 
ATOM   1446 C CD2 . LEU A 1 166 ? -23.869 12.195 82.053  1.00 22.08 ? 166 LEU A CD2 1 
ATOM   1447 N N   . ASN A 1 167 ? -27.218 9.169  79.205  1.00 11.59 ? 167 ASN A N   1 
ATOM   1448 C CA  . ASN A 1 167 ? -27.290 7.830  78.636  1.00 17.36 ? 167 ASN A CA  1 
ATOM   1449 C C   . ASN A 1 167 ? -26.929 7.849  77.157  1.00 17.78 ? 167 ASN A C   1 
ATOM   1450 O O   . ASN A 1 167 ? -26.212 6.963  76.682  1.00 18.07 ? 167 ASN A O   1 
ATOM   1451 C CB  . ASN A 1 167 ? -28.673 7.230  78.846  1.00 19.19 ? 167 ASN A CB  1 
ATOM   1452 C CG  . ASN A 1 167 ? -28.880 6.745  80.270  1.00 39.04 ? 167 ASN A CG  1 
ATOM   1453 O OD1 . ASN A 1 167 ? -27.935 6.295  80.924  1.00 47.37 ? 167 ASN A OD1 1 
ATOM   1454 N ND2 . ASN A 1 167 ? -30.119 6.808  80.751  1.00 39.76 ? 167 ASN A ND2 1 
ATOM   1455 N N   . LYS A 1 168 ? -27.393 8.864  76.417  1.00 14.01 ? 168 LYS A N   1 
ATOM   1456 C CA  . LYS A 1 168 ? -27.024 8.970  75.006  1.00 11.61 ? 168 LYS A CA  1 
ATOM   1457 C C   . LYS A 1 168 ? -25.527 9.201  74.847  1.00 13.77 ? 168 LYS A C   1 
ATOM   1458 O O   . LYS A 1 168 ? -24.914 8.698  73.898  1.00 12.78 ? 168 LYS A O   1 
ATOM   1459 C CB  . LYS A 1 168 ? -27.796 10.102 74.328  1.00 13.65 ? 168 LYS A CB  1 
ATOM   1460 C CG  . LYS A 1 168 ? -29.309 9.897  74.324  1.00 15.03 ? 168 LYS A CG  1 
ATOM   1461 C CD  . LYS A 1 168 ? -29.729 8.709  73.476  1.00 25.25 ? 168 LYS A CD  1 
ATOM   1462 C CE  . LYS A 1 168 ? -29.726 9.033  71.998  1.00 37.93 ? 168 LYS A CE  1 
ATOM   1463 N NZ  . LYS A 1 168 ? -30.269 7.881  71.216  1.00 46.69 ? 168 LYS A NZ  1 
ATOM   1464 N N   . TYR A 1 169 ? -24.930 9.978  75.757  1.00 10.71 ? 169 TYR A N   1 
ATOM   1465 C CA  . TYR A 1 169 ? -23.494 10.220 75.709  1.00 12.10 ? 169 TYR A CA  1 
ATOM   1466 C C   . TYR A 1 169 ? -22.715 8.926  75.907  1.00 13.96 ? 169 TYR A C   1 
ATOM   1467 O O   . TYR A 1 169 ? -21.756 8.646  75.171  1.00 12.91 ? 169 TYR A O   1 
ATOM   1468 C CB  . TYR A 1 169 ? -23.086 11.244 76.774  1.00 11.30 ? 169 TYR A CB  1 
ATOM   1469 C CG  . TYR A 1 169 ? -23.281 12.708 76.394  1.00 8.94  ? 169 TYR A CG  1 
ATOM   1470 C CD1 . TYR A 1 169 ? -24.062 13.073 75.311  1.00 11.83 ? 169 TYR A CD1 1 
ATOM   1471 C CD2 . TYR A 1 169 ? -22.671 13.719 77.137  1.00 12.12 ? 169 TYR A CD2 1 
ATOM   1472 C CE1 . TYR A 1 169 ? -24.234 14.411 74.973  1.00 13.47 ? 169 TYR A CE1 1 
ATOM   1473 C CE2 . TYR A 1 169 ? -22.834 15.049 76.816  1.00 12.64 ? 169 TYR A CE2 1 
ATOM   1474 C CZ  . TYR A 1 169 ? -23.615 15.390 75.736  1.00 11.00 ? 169 TYR A CZ  1 
ATOM   1475 O OH  . TYR A 1 169 ? -23.778 16.723 75.417  1.00 12.73 ? 169 TYR A OH  1 
ATOM   1476 N N   . PHE A 1 170 ? -23.134 8.100  76.866  1.00 11.90 ? 170 PHE A N   1 
ATOM   1477 C CA  . PHE A 1 170 ? -22.447 6.829  77.039  1.00 12.28 ? 170 PHE A CA  1 
ATOM   1478 C C   . PHE A 1 170 ? -22.666 5.892  75.858  1.00 16.10 ? 170 PHE A C   1 
ATOM   1479 O O   . PHE A 1 170 ? -21.769 5.102  75.538  1.00 14.17 ? 170 PHE A O   1 
ATOM   1480 C CB  . PHE A 1 170 ? -22.849 6.190  78.363  1.00 13.91 ? 170 PHE A CB  1 
ATOM   1481 C CG  . PHE A 1 170 ? -22.034 6.706  79.518  1.00 19.40 ? 170 PHE A CG  1 
ATOM   1482 C CD1 . PHE A 1 170 ? -20.750 6.225  79.744  1.00 21.35 ? 170 PHE A CD1 1 
ATOM   1483 C CD2 . PHE A 1 170 ? -22.524 7.720  80.333  1.00 23.19 ? 170 PHE A CD2 1 
ATOM   1484 C CE1 . PHE A 1 170 ? -19.986 6.713  80.794  1.00 20.50 ? 170 PHE A CE1 1 
ATOM   1485 C CE2 . PHE A 1 170 ? -21.764 8.215  81.378  1.00 26.23 ? 170 PHE A CE2 1 
ATOM   1486 C CZ  . PHE A 1 170 ? -20.494 7.708  81.611  1.00 24.45 ? 170 PHE A CZ  1 
ATOM   1487 N N   . GLU A 1 171 ? -23.813 5.978  75.170  1.00 13.55 ? 171 GLU A N   1 
ATOM   1488 C CA  . GLU A 1 171 ? -23.972 5.201  73.936  1.00 16.81 ? 171 GLU A CA  1 
ATOM   1489 C C   . GLU A 1 171 ? -22.923 5.591  72.903  1.00 16.28 ? 171 GLU A C   1 
ATOM   1490 O O   . GLU A 1 171 ? -22.371 4.732  72.212  1.00 15.14 ? 171 GLU A O   1 
ATOM   1491 C CB  . GLU A 1 171 ? -25.371 5.390  73.342  1.00 20.59 ? 171 GLU A CB  1 
ATOM   1492 C CG  . GLU A 1 171 ? -26.508 4.770  74.133  1.00 33.24 ? 171 GLU A CG  1 
ATOM   1493 C CD  . GLU A 1 171 ? -27.871 4.990  73.470  1.00 42.55 ? 171 GLU A CD  1 
ATOM   1494 O OE1 . GLU A 1 171 ? -27.941 5.673  72.422  1.00 43.31 ? 171 GLU A OE1 1 
ATOM   1495 O OE2 . GLU A 1 171 ? -28.880 4.487  74.007  1.00 47.83 ? 171 GLU A OE2 1 
ATOM   1496 N N   . ILE A 1 172 ? -22.653 6.890  72.776  1.00 10.52 ? 172 ILE A N   1 
ATOM   1497 C CA  . ILE A 1 172 ? -21.627 7.367  71.859  1.00 12.45 ? 172 ILE A CA  1 
ATOM   1498 C C   . ILE A 1 172 ? -20.265 6.794  72.241  1.00 15.13 ? 172 ILE A C   1 
ATOM   1499 O O   . ILE A 1 172 ? -19.498 6.346  71.380  1.00 14.34 ? 172 ILE A O   1 
ATOM   1500 C CB  . ILE A 1 172 ? -21.603 8.908  71.839  1.00 14.82 ? 172 ILE A CB  1 
ATOM   1501 C CG1 . ILE A 1 172 ? -22.834 9.473  71.117  1.00 16.81 ? 172 ILE A CG1 1 
ATOM   1502 C CG2 . ILE A 1 172 ? -20.315 9.433  71.204  1.00 19.52 ? 172 ILE A CG2 1 
ATOM   1503 C CD1 . ILE A 1 172 ? -22.920 9.138  69.632  1.00 13.46 ? 172 ILE A CD1 1 
ATOM   1504 N N   . ILE A 1 173 ? -19.929 6.825  73.534  1.00 10.28 ? 173 ILE A N   1 
ATOM   1505 C CA  . ILE A 1 173 ? -18.634 6.293  73.962  1.00 8.76  ? 173 ILE A CA  1 
ATOM   1506 C C   . ILE A 1 173 ? -18.533 4.809  73.639  1.00 16.82 ? 173 ILE A C   1 
ATOM   1507 O O   . ILE A 1 173 ? -17.484 4.324  73.192  1.00 13.15 ? 173 ILE A O   1 
ATOM   1508 C CB  . ILE A 1 173 ? -18.407 6.554  75.458  1.00 13.99 ? 173 ILE A CB  1 
ATOM   1509 C CG1 . ILE A 1 173 ? -18.411 8.062  75.746  1.00 11.94 ? 173 ILE A CG1 1 
ATOM   1510 C CG2 . ILE A 1 173 ? -17.086 5.934  75.900  1.00 12.99 ? 173 ILE A CG2 1 
ATOM   1511 C CD1 . ILE A 1 173 ? -18.263 8.417  77.241  1.00 16.36 ? 173 ILE A CD1 1 
ATOM   1512 N N   . LYS A 1 174 ? -19.617 4.061  73.863  1.00 12.37 ? 174 LYS A N   1 
ATOM   1513 C CA  . LYS A 1 174 ? -19.568 2.622  73.623  1.00 10.64 ? 174 LYS A CA  1 
ATOM   1514 C C   . LYS A 1 174 ? -19.336 2.276  72.154  1.00 13.99 ? 174 LYS A C   1 
ATOM   1515 O O   . LYS A 1 174 ? -18.867 1.172  71.868  1.00 15.52 ? 174 LYS A O   1 
ATOM   1516 C CB  . LYS A 1 174 ? -20.855 1.947  74.120  1.00 16.80 ? 174 LYS A CB  1 
ATOM   1517 C CG  . LYS A 1 174 ? -20.969 1.899  75.627  1.00 24.56 ? 174 LYS A CG  1 
ATOM   1518 C CD  . LYS A 1 174 ? -22.326 1.352  76.051  1.00 33.56 ? 174 LYS A CD  1 
ATOM   1519 C CE  . LYS A 1 174 ? -22.459 1.299  77.563  1.00 40.47 ? 174 LYS A CE  1 
ATOM   1520 N NZ  . LYS A 1 174 ? -21.670 0.181  78.149  1.00 52.12 ? 174 LYS A NZ  1 
ATOM   1521 N N   . LYS A 1 175 ? -19.648 3.177  71.218  1.00 13.25 ? 175 LYS A N   1 
ATOM   1522 C CA  . LYS A 1 175 ? -19.440 2.896  69.798  1.00 16.99 ? 175 LYS A CA  1 
ATOM   1523 C C   . LYS A 1 175 ? -18.167 3.508  69.250  1.00 14.21 ? 175 LYS A C   1 
ATOM   1524 O O   . LYS A 1 175 ? -17.940 3.445  68.046  1.00 15.56 ? 175 LYS A O   1 
ATOM   1525 C CB  . LYS A 1 175 ? -20.610 3.385  68.949  1.00 19.91 ? 175 LYS A CB  1 
ATOM   1526 C CG  . LYS A 1 175 ? -21.955 3.226  69.579  1.00 31.15 ? 175 LYS A CG  1 
ATOM   1527 C CD  . LYS A 1 175 ? -23.057 3.195  68.541  1.00 45.53 ? 175 LYS A CD  1 
ATOM   1528 C CE  . LYS A 1 175 ? -22.953 4.352  67.556  1.00 52.62 ? 175 LYS A CE  1 
ATOM   1529 N NZ  . LYS A 1 175 ? -22.508 5.629  68.196  1.00 58.99 ? 175 LYS A NZ  1 
ATOM   1530 N N   . THR A 1 176 ? -17.321 4.077  70.102  1.00 13.43 ? 176 THR A N   1 
ATOM   1531 C CA  . THR A 1 176 ? -16.203 4.859  69.588  1.00 13.61 ? 176 THR A CA  1 
ATOM   1532 C C   . THR A 1 176 ? -15.113 3.976  68.974  1.00 14.59 ? 176 THR A C   1 
ATOM   1533 O O   . THR A 1 176 ? -14.693 4.203  67.833  1.00 13.34 ? 176 THR A O   1 
ATOM   1534 C CB  . THR A 1 176 ? -15.668 5.760  70.700  1.00 16.17 ? 176 THR A CB  1 
ATOM   1535 O OG1 . THR A 1 176 ? -16.663 6.747  70.993  1.00 16.75 ? 176 THR A OG1 1 
ATOM   1536 C CG2 . THR A 1 176 ? -14.398 6.472  70.259  1.00 14.97 ? 176 THR A CG2 1 
ATOM   1537 N N   . LEU A 1 177 ? -14.629 2.965  69.695  1.00 13.15 ? 177 LEU A N   1 
ATOM   1538 C CA  . LEU A 1 177 ? -13.593 2.149  69.069  1.00 17.17 ? 177 LEU A CA  1 
ATOM   1539 C C   . LEU A 1 177 ? -14.132 1.430  67.833  1.00 15.05 ? 177 LEU A C   1 
ATOM   1540 O O   . LEU A 1 177 ? -13.400 1.258  66.849  1.00 14.92 ? 177 LEU A O   1 
ATOM   1541 C CB  . LEU A 1 177 ? -12.999 1.168  70.078  1.00 15.06 ? 177 LEU A CB  1 
ATOM   1542 C CG  . LEU A 1 177 ? -12.332 1.825  71.291  1.00 20.27 ? 177 LEU A CG  1 
ATOM   1543 C CD1 . LEU A 1 177 ? -11.748 0.750  72.199  1.00 23.33 ? 177 LEU A CD1 1 
ATOM   1544 C CD2 . LEU A 1 177 ? -11.262 2.807  70.884  1.00 24.04 ? 177 LEU A CD2 1 
ATOM   1545 N N   . SER A 1 178 ? -15.423 1.078  67.832  1.00 15.10 ? 178 SER A N   1 
ATOM   1546 C CA  . SER A 1 178 ? -16.020 0.412  66.675  1.00 13.61 ? 178 SER A CA  1 
ATOM   1547 C C   . SER A 1 178 ? -15.958 1.278  65.421  1.00 14.08 ? 178 SER A C   1 
ATOM   1548 O O   . SER A 1 178 ? -15.754 0.758  64.316  1.00 15.72 ? 178 SER A O   1 
ATOM   1549 C CB  . SER A 1 178 ? -17.472 0.034  66.968  1.00 19.84 ? 178 SER A CB  1 
ATOM   1550 O OG  . SER A 1 178 ? -17.524 -1.113 67.800  1.00 27.51 ? 178 SER A OG  1 
ATOM   1551 N N   . ILE A 1 179 ? -16.148 2.594  65.552  1.00 14.75 ? 179 ILE A N   1 
ATOM   1552 C CA  . ILE A 1 179 ? -16.142 3.393  64.326  1.00 12.57 ? 179 ILE A CA  1 
ATOM   1553 C C   . ILE A 1 179 ? -14.733 3.533  63.756  1.00 18.06 ? 179 ILE A C   1 
ATOM   1554 O O   . ILE A 1 179 ? -14.565 3.590  62.531  1.00 13.86 ? 179 ILE A O   1 
ATOM   1555 C CB  . ILE A 1 179 ? -16.825 4.762  64.525  1.00 17.68 ? 179 ILE A CB  1 
ATOM   1556 C CG1 . ILE A 1 179 ? -17.140 5.347  63.138  1.00 29.35 ? 179 ILE A CG1 1 
ATOM   1557 C CG2 . ILE A 1 179 ? -15.958 5.726  65.321  1.00 15.71 ? 179 ILE A CG2 1 
ATOM   1558 C CD1 . ILE A 1 179 ? -18.276 6.323  63.114  1.00 30.04 ? 179 ILE A CD1 1 
ATOM   1559 N N   . TYR A 1 180 ? -13.694 3.548  64.603  1.00 12.25 ? 180 TYR A N   1 
ATOM   1560 C CA  . TYR A 1 180 ? -12.339 3.520  64.055  1.00 12.37 ? 180 TYR A CA  1 
ATOM   1561 C C   . TYR A 1 180 ? -12.046 2.189  63.373  1.00 11.44 ? 180 TYR A C   1 
ATOM   1562 O O   . TYR A 1 180 ? -11.372 2.159  62.344  1.00 13.63 ? 180 TYR A O   1 
ATOM   1563 C CB  . TYR A 1 180 ? -11.299 3.790  65.144  1.00 12.17 ? 180 TYR A CB  1 
ATOM   1564 C CG  . TYR A 1 180 ? -11.315 5.219  65.624  1.00 14.69 ? 180 TYR A CG  1 
ATOM   1565 C CD1 . TYR A 1 180 ? -10.646 6.209  64.917  1.00 14.77 ? 180 TYR A CD1 1 
ATOM   1566 C CD2 . TYR A 1 180 ? -12.001 5.573  66.781  1.00 13.54 ? 180 TYR A CD2 1 
ATOM   1567 C CE1 . TYR A 1 180 ? -10.662 7.533  65.351  1.00 13.04 ? 180 TYR A CE1 1 
ATOM   1568 C CE2 . TYR A 1 180 ? -12.014 6.887  67.229  1.00 10.31 ? 180 TYR A CE2 1 
ATOM   1569 C CZ  . TYR A 1 180 ? -11.339 7.856  66.505  1.00 11.07 ? 180 TYR A CZ  1 
ATOM   1570 O OH  . TYR A 1 180 ? -11.353 9.169  66.926  1.00 11.69 ? 180 TYR A OH  1 
ATOM   1571 N N   . ARG A 1 181 ? -12.538 1.071  63.924  1.00 11.54 ? 181 ARG A N   1 
ATOM   1572 C CA  . ARG A 1 181 ? -12.345 -0.202 63.235  1.00 12.43 ? 181 ARG A CA  1 
ATOM   1573 C C   . ARG A 1 181 ? -13.074 -0.208 61.897  1.00 16.40 ? 181 ARG A C   1 
ATOM   1574 O O   . ARG A 1 181 ? -12.571 -0.749 60.904  1.00 16.41 ? 181 ARG A O   1 
ATOM   1575 C CB  . ARG A 1 181 ? -12.853 -1.358 64.095  1.00 13.03 ? 181 ARG A CB  1 
ATOM   1576 C CG  . ARG A 1 181 ? -12.112 -1.557 65.399  1.00 16.39 ? 181 ARG A CG  1 
ATOM   1577 C CD  . ARG A 1 181 ? -12.604 -2.820 66.095  1.00 20.29 ? 181 ARG A CD  1 
ATOM   1578 N NE  . ARG A 1 181 ? -12.114 -2.904 67.464  1.00 33.69 ? 181 ARG A NE  1 
ATOM   1579 C CZ  . ARG A 1 181 ? -12.845 -2.651 68.546  1.00 35.69 ? 181 ARG A CZ  1 
ATOM   1580 N NH1 . ARG A 1 181 ? -14.125 -2.319 68.436  1.00 29.13 ? 181 ARG A NH1 1 
ATOM   1581 N NH2 . ARG A 1 181 ? -12.293 -2.745 69.748  1.00 46.82 ? 181 ARG A NH2 1 
ATOM   1582 N N   . GLU A 1 182 ? -14.277 0.373  61.867  1.00 13.71 ? 182 GLU A N   1 
ATOM   1583 C CA  . GLU A 1 182 ? -15.080 0.399  60.648  1.00 17.43 ? 182 GLU A CA  1 
ATOM   1584 C C   . GLU A 1 182 ? -14.406 1.218  59.553  1.00 17.78 ? 182 GLU A C   1 
ATOM   1585 O O   . GLU A 1 182 ? -14.215 0.734  58.431  1.00 18.10 ? 182 GLU A O   1 
ATOM   1586 C CB  . GLU A 1 182 ? -16.467 0.959  60.952  1.00 15.35 ? 182 GLU A CB  1 
ATOM   1587 C CG  . GLU A 1 182 ? -17.385 1.038  59.735  1.00 27.12 ? 182 GLU A CG  1 
ATOM   1588 C CD  . GLU A 1 182 ? -18.802 1.491  60.082  1.00 45.52 ? 182 GLU A CD  1 
ATOM   1589 O OE1 . GLU A 1 182 ? -19.089 1.713  61.281  1.00 47.63 ? 182 GLU A OE1 1 
ATOM   1590 O OE2 . GLU A 1 182 ? -19.629 1.619  59.149  1.00 51.49 ? 182 GLU A OE2 1 
ATOM   1591 N N   . ILE A 1 183 ? -14.051 2.473  59.847  1.00 15.32 ? 183 ILE A N   1 
ATOM   1592 C CA  . ILE A 1 183 ? -13.505 3.298  58.772  1.00 14.94 ? 183 ILE A CA  1 
ATOM   1593 C C   . ILE A 1 183 ? -12.170 2.738  58.311  1.00 16.80 ? 183 ILE A C   1 
ATOM   1594 O O   . ILE A 1 183 ? -11.801 2.872  57.140  1.00 18.06 ? 183 ILE A O   1 
ATOM   1595 C CB  . ILE A 1 183 ? -13.408 4.782  59.192  1.00 15.62 ? 183 ILE A CB  1 
ATOM   1596 C CG1 . ILE A 1 183 ? -12.465 4.998  60.381  1.00 17.34 ? 183 ILE A CG1 1 
ATOM   1597 C CG2 . ILE A 1 183 ? -14.803 5.353  59.470  1.00 19.15 ? 183 ILE A CG2 1 
ATOM   1598 C CD1 . ILE A 1 183 ? -11.088 5.474  59.979  1.00 19.63 ? 183 ILE A CD1 1 
ATOM   1599 N N   . LYS A 1 184 ? -11.447 2.064  59.202  1.00 13.00 ? 184 LYS A N   1 
ATOM   1600 C CA  . LYS A 1 184 ? -10.204 1.416  58.805  1.00 18.83 ? 184 LYS A CA  1 
ATOM   1601 C C   . LYS A 1 184 ? -10.453 0.269  57.827  1.00 23.95 ? 184 LYS A C   1 
ATOM   1602 O O   . LYS A 1 184 ? -9.821  0.192  56.766  1.00 22.03 ? 184 LYS A O   1 
ATOM   1603 C CB  . LYS A 1 184 ? -9.482  0.920  60.052  1.00 20.46 ? 184 LYS A CB  1 
ATOM   1604 C CG  . LYS A 1 184 ? -8.118  0.346  59.813  1.00 22.18 ? 184 LYS A CG  1 
ATOM   1605 C CD  . LYS A 1 184 ? -7.473  0.011  61.147  1.00 24.29 ? 184 LYS A CD  1 
ATOM   1606 C CE  . LYS A 1 184 ? -6.057  -0.423 60.944  1.00 29.55 ? 184 LYS A CE  1 
ATOM   1607 N NZ  . LYS A 1 184 ? -6.030  -1.660 60.132  1.00 41.12 ? 184 LYS A NZ  1 
ATOM   1608 N N   . GLU A 1 185 ? -11.358 -0.645 58.165  1.00 17.50 ? 185 GLU A N   1 
ATOM   1609 C CA  . GLU A 1 185 ? -11.537 -1.794 57.283  1.00 19.92 ? 185 GLU A CA  1 
ATOM   1610 C C   . GLU A 1 185 ? -12.240 -1.402 55.987  1.00 22.63 ? 185 GLU A C   1 
ATOM   1611 O O   . GLU A 1 185 ? -12.116 -2.116 54.981  1.00 21.66 ? 185 GLU A O   1 
ATOM   1612 C CB  . GLU A 1 185 ? -12.309 -2.899 58.003  1.00 29.06 ? 185 GLU A CB  1 
ATOM   1613 C CG  . GLU A 1 185 ? -13.780 -2.939 57.689  1.00 34.44 ? 185 GLU A CG  1 
ATOM   1614 C CD  . GLU A 1 185 ? -14.483 -4.043 58.444  1.00 40.99 ? 185 GLU A CD  1 
ATOM   1615 O OE1 . GLU A 1 185 ? -14.310 -4.107 59.682  1.00 44.73 ? 185 GLU A OE1 1 
ATOM   1616 O OE2 . GLU A 1 185 ? -15.204 -4.836 57.808  1.00 40.45 ? 185 GLU A OE2 1 
ATOM   1617 N N   . GLU A 1 186 ? -12.944 -0.275 55.981  1.00 16.98 ? 186 GLU A N   1 
ATOM   1618 C CA  . GLU A 1 186 ? -13.544 0.257  54.762  1.00 20.52 ? 186 GLU A CA  1 
ATOM   1619 C C   . GLU A 1 186 ? -12.551 1.035  53.903  1.00 21.80 ? 186 GLU A C   1 
ATOM   1620 O O   . GLU A 1 186 ? -12.927 1.513  52.825  1.00 23.16 ? 186 GLU A O   1 
ATOM   1621 C CB  . GLU A 1 186 ? -14.722 1.165  55.116  1.00 21.13 ? 186 GLU A CB  1 
ATOM   1622 C CG  . GLU A 1 186 ? -15.996 0.418  55.534  1.00 21.86 ? 186 GLU A CG  1 
ATOM   1623 C CD  . GLU A 1 186 ? -17.130 1.369  55.872  1.00 30.12 ? 186 GLU A CD  1 
ATOM   1624 O OE1 . GLU A 1 186 ? -16.856 2.478  56.383  1.00 28.52 ? 186 GLU A OE1 1 
ATOM   1625 O OE2 . GLU A 1 186 ? -18.294 1.033  55.584  1.00 29.25 ? 186 GLU A OE2 1 
ATOM   1626 N N   . GLY A 1 187 ? -11.311 1.190  54.361  1.00 19.60 ? 187 GLY A N   1 
ATOM   1627 C CA  . GLY A 1 187 ? -10.351 1.982  53.616  1.00 20.40 ? 187 GLY A CA  1 
ATOM   1628 C C   . GLY A 1 187 ? -10.658 3.463  53.569  1.00 20.96 ? 187 GLY A C   1 
ATOM   1629 O O   . GLY A 1 187 ? -10.165 4.163  52.681  1.00 19.36 ? 187 GLY A O   1 
ATOM   1630 N N   . LYS A 1 188 ? -11.474 3.963  54.492  1.00 15.57 ? 188 LYS A N   1 
ATOM   1631 C CA  . LYS A 1 188 ? -11.809 5.378  54.518  1.00 15.15 ? 188 LYS A CA  1 
ATOM   1632 C C   . LYS A 1 188 ? -10.802 6.176  55.320  1.00 15.98 ? 188 LYS A C   1 
ATOM   1633 O O   . LYS A 1 188 ? -10.791 7.407  55.237  1.00 15.89 ? 188 LYS A O   1 
ATOM   1634 C CB  . LYS A 1 188 ? -13.213 5.587  55.104  1.00 17.48 ? 188 LYS A CB  1 
ATOM   1635 C CG  . LYS A 1 188 ? -14.352 5.021  54.228  1.00 20.75 ? 188 LYS A CG  1 
ATOM   1636 C CD  . LYS A 1 188 ? -15.702 5.209  54.914  1.00 22.53 ? 188 LYS A CD  1 
ATOM   1637 C CE  . LYS A 1 188 ? -16.861 4.655  54.061  1.00 28.02 ? 188 LYS A CE  1 
ATOM   1638 N NZ  . LYS A 1 188 ? -17.102 5.530  52.894  1.00 34.65 ? 188 LYS A NZ  1 
ATOM   1639 N N   . GLY A 1 189 ? -9.959  5.503  56.084  1.00 15.21 ? 189 GLY A N   1 
ATOM   1640 C CA  . GLY A 1 189 ? -8.884  6.174  56.783  1.00 14.45 ? 189 GLY A CA  1 
ATOM   1641 C C   . GLY A 1 189 ? -7.942  5.155  57.371  1.00 15.23 ? 189 GLY A C   1 
ATOM   1642 O O   . GLY A 1 189 ? -8.304  3.993  57.576  1.00 16.59 ? 189 GLY A O   1 
ATOM   1643 N N   . SER A 1 190 ? -6.708  5.594  57.587  1.00 12.99 ? 190 SER A N   1 
ATOM   1644 C CA  . SER A 1 190 ? -5.745  4.819  58.347  1.00 12.85 ? 190 SER A CA  1 
ATOM   1645 C C   . SER A 1 190 ? -5.776  5.267  59.798  1.00 13.57 ? 190 SER A C   1 
ATOM   1646 O O   . SER A 1 190 ? -6.072  6.429  60.098  1.00 12.09 ? 190 SER A O   1 
ATOM   1647 C CB  . SER A 1 190 ? -4.329  5.001  57.792  1.00 14.53 ? 190 SER A CB  1 
ATOM   1648 O OG  . SER A 1 190 ? -4.217  4.503  56.467  1.00 16.40 ? 190 SER A OG  1 
ATOM   1649 N N   . VAL A 1 191 ? -5.446  4.346  60.701  1.00 14.98 ? 191 VAL A N   1 
ATOM   1650 C CA  . VAL A 1 191 ? -5.342  4.653  62.123  1.00 15.87 ? 191 VAL A CA  1 
ATOM   1651 C C   . VAL A 1 191 ? -3.922  4.352  62.580  1.00 13.83 ? 191 VAL A C   1 
ATOM   1652 O O   . VAL A 1 191 ? -3.415  3.242  62.373  1.00 15.76 ? 191 VAL A O   1 
ATOM   1653 C CB  . VAL A 1 191 ? -6.373  3.869  62.958  1.00 14.75 ? 191 VAL A CB  1 
ATOM   1654 C CG1 . VAL A 1 191 ? -6.304  4.300  64.436  1.00 14.09 ? 191 VAL A CG1 1 
ATOM   1655 C CG2 . VAL A 1 191 ? -7.772  4.098  62.395  1.00 11.93 ? 191 VAL A CG2 1 
ATOM   1656 N N   . SER A 1 192 ? -3.284  5.345  63.193  1.00 12.83 ? 192 SER A N   1 
ATOM   1657 C CA  . SER A 1 192 ? -1.947  5.220  63.750  1.00 16.66 ? 192 SER A CA  1 
ATOM   1658 C C   . SER A 1 192 ? -2.023  5.238  65.270  1.00 17.24 ? 192 SER A C   1 
ATOM   1659 O O   . SER A 1 192 ? -3.079  5.457  65.865  1.00 11.76 ? 192 SER A O   1 
ATOM   1660 C CB  . SER A 1 192 ? -1.051  6.368  63.281  1.00 13.33 ? 192 SER A CB  1 
ATOM   1661 O OG  . SER A 1 192 ? -1.530  7.606  63.794  1.00 13.65 ? 192 SER A OG  1 
ATOM   1662 N N   . THR A 1 193 ? -0.881  5.018  65.913  1.00 14.15 ? 193 THR A N   1 
ATOM   1663 C CA  . THR A 1 193 ? -0.813  5.247  67.344  1.00 12.05 ? 193 THR A CA  1 
ATOM   1664 C C   . THR A 1 193 ? 0.496   5.961  67.653  1.00 9.75  ? 193 THR A C   1 
ATOM   1665 O O   . THR A 1 193 ? 1.289   6.263  66.753  1.00 10.00 ? 193 THR A O   1 
ATOM   1666 C CB  . THR A 1 193 ? -0.970  3.946  68.133  1.00 14.23 ? 193 THR A CB  1 
ATOM   1667 O OG1 . THR A 1 193 ? -1.266  4.278  69.496  1.00 14.64 ? 193 THR A OG1 1 
ATOM   1668 C CG2 . THR A 1 193 ? 0.292   3.073  68.056  1.00 11.59 ? 193 THR A CG2 1 
ATOM   1669 N N   . SER A 1 194 ? 0.711   6.260  68.923  1.00 10.34 ? 194 SER A N   1 
ATOM   1670 C CA  . SER A 1 194 ? 1.931   6.904  69.390  1.00 9.67  ? 194 SER A CA  1 
ATOM   1671 C C   . SER A 1 194 ? 2.539   6.029  70.477  1.00 11.37 ? 194 SER A C   1 
ATOM   1672 O O   . SER A 1 194 ? 1.839   5.202  71.071  1.00 11.98 ? 194 SER A O   1 
ATOM   1673 C CB  . SER A 1 194 ? 1.648   8.297  69.979  1.00 12.04 ? 194 SER A CB  1 
ATOM   1674 O OG  . SER A 1 194 ? 1.178   9.243  69.039  1.00 9.97  ? 194 SER A OG  1 
ATOM   1675 N N   . PRO A 1 195 ? 3.825   6.213  70.796  1.00 10.40 ? 195 PRO A N   1 
ATOM   1676 C CA  . PRO A 1 195 ? 4.377   5.611  72.024  1.00 10.21 ? 195 PRO A CA  1 
ATOM   1677 C C   . PRO A 1 195 ? 3.447   5.849  73.209  1.00 12.54 ? 195 PRO A C   1 
ATOM   1678 O O   . PRO A 1 195 ? 2.858   6.923  73.339  1.00 13.24 ? 195 PRO A O   1 
ATOM   1679 C CB  . PRO A 1 195 ? 5.715   6.335  72.200  1.00 14.08 ? 195 PRO A CB  1 
ATOM   1680 C CG  . PRO A 1 195 ? 6.103   6.738  70.812  1.00 23.15 ? 195 PRO A CG  1 
ATOM   1681 C CD  . PRO A 1 195 ? 4.815   7.056  70.096  1.00 13.78 ? 195 PRO A CD  1 
ATOM   1682 N N   . TYR A 1 196 ? 3.387   4.855  74.109  1.00 11.24 ? 196 TYR A N   1 
ATOM   1683 C CA  . TYR A 1 196 ? 2.165   4.550  74.862  1.00 11.67 ? 196 TYR A CA  1 
ATOM   1684 C C   . TYR A 1 196 ? 1.623   5.752  75.633  1.00 12.77 ? 196 TYR A C   1 
ATOM   1685 O O   . TYR A 1 196 ? 0.436   6.083  75.506  1.00 11.74 ? 196 TYR A O   1 
ATOM   1686 C CB  . TYR A 1 196 ? 2.438   3.355  75.780  1.00 9.93  ? 196 TYR A CB  1 
ATOM   1687 C CG  . TYR A 1 196 ? 1.215   2.629  76.301  1.00 10.14 ? 196 TYR A CG  1 
ATOM   1688 C CD1 . TYR A 1 196 ? 0.290   3.222  77.166  1.00 10.63 ? 196 TYR A CD1 1 
ATOM   1689 C CD2 . TYR A 1 196 ? 0.921   1.376  75.803  1.00 11.72 ? 196 TYR A CD2 1 
ATOM   1690 C CE1 . TYR A 1 196 ? -0.854  2.499  77.584  1.00 13.77 ? 196 TYR A CE1 1 
ATOM   1691 C CE2 . TYR A 1 196 ? -0.204  0.670  76.198  1.00 11.93 ? 196 TYR A CE2 1 
ATOM   1692 C CZ  . TYR A 1 196 ? -1.092  1.231  77.086  1.00 16.01 ? 196 TYR A CZ  1 
ATOM   1693 O OH  . TYR A 1 196 ? -2.218  0.520  77.473  1.00 16.45 ? 196 TYR A OH  1 
ATOM   1694 N N   . TYR A 1 197 ? 2.465   6.426  76.428  1.00 12.43 ? 197 TYR A N   1 
ATOM   1695 C CA  . TYR A 1 197 ? 1.995   7.516  77.277  1.00 14.50 ? 197 TYR A CA  1 
ATOM   1696 C C   . TYR A 1 197 ? 2.372   8.876  76.714  1.00 13.70 ? 197 TYR A C   1 
ATOM   1697 O O   . TYR A 1 197 ? 2.447   9.861  77.453  1.00 11.71 ? 197 TYR A O   1 
ATOM   1698 C CB  . TYR A 1 197 ? 2.517   7.341  78.705  1.00 12.95 ? 197 TYR A CB  1 
ATOM   1699 C CG  . TYR A 1 197 ? 1.881   6.139  79.349  1.00 14.09 ? 197 TYR A CG  1 
ATOM   1700 C CD1 . TYR A 1 197 ? 0.550   6.178  79.755  1.00 11.90 ? 197 TYR A CD1 1 
ATOM   1701 C CD2 . TYR A 1 197 ? 2.582   4.947  79.491  1.00 12.13 ? 197 TYR A CD2 1 
ATOM   1702 C CE1 . TYR A 1 197 ? -0.055  5.070  80.312  1.00 14.66 ? 197 TYR A CE1 1 
ATOM   1703 C CE2 . TYR A 1 197 ? 1.979   3.833  80.054  1.00 13.51 ? 197 TYR A CE2 1 
ATOM   1704 C CZ  . TYR A 1 197 ? 0.663   3.906  80.455  1.00 14.54 ? 197 TYR A CZ  1 
ATOM   1705 O OH  . TYR A 1 197 ? 0.056   2.802  81.004  1.00 17.95 ? 197 TYR A OH  1 
ATOM   1706 N N   . HIS A 1 198 ? 2.563   8.950  75.409  1.00 12.88 ? 198 HIS A N   1 
ATOM   1707 C CA  . HIS A 1 198 ? 2.836   10.233 74.757  1.00 10.51 ? 198 HIS A CA  1 
ATOM   1708 C C   . HIS A 1 198 ? 4.061   10.930 75.358  1.00 11.11 ? 198 HIS A C   1 
ATOM   1709 O O   . HIS A 1 198 ? 3.990   12.129 75.671  1.00 11.35 ? 198 HIS A O   1 
ATOM   1710 C CB  . HIS A 1 198 ? 1.594   11.130 74.869  1.00 9.28  ? 198 HIS A CB  1 
ATOM   1711 C CG  . HIS A 1 198 ? 1.522   12.241 73.860  1.00 8.14  ? 198 HIS A CG  1 
ATOM   1712 N ND1 . HIS A 1 198 ? 1.936   13.531 74.137  1.00 8.99  ? 198 HIS A ND1 1 
ATOM   1713 C CD2 . HIS A 1 198 ? 1.022   12.267 72.599  1.00 9.40  ? 198 HIS A CD2 1 
ATOM   1714 C CE1 . HIS A 1 198 ? 1.727   14.294 73.077  1.00 9.66  ? 198 HIS A CE1 1 
ATOM   1715 N NE2 . HIS A 1 198 ? 1.161   13.554 72.134  1.00 11.80 ? 198 HIS A NE2 1 
ATOM   1716 N N   . PRO A 1 199 ? 5.197   10.245 75.528  1.00 12.01 ? 199 PRO A N   1 
ATOM   1717 C CA  . PRO A 1 199 ? 6.406   10.916 76.019  1.00 11.62 ? 199 PRO A CA  1 
ATOM   1718 C C   . PRO A 1 199 ? 7.148   11.612 74.887  1.00 12.85 ? 199 PRO A C   1 
ATOM   1719 O O   . PRO A 1 199 ? 6.906   11.363 73.704  1.00 13.07 ? 199 PRO A O   1 
ATOM   1720 C CB  . PRO A 1 199 ? 7.253   9.760  76.537  1.00 10.82 ? 199 PRO A CB  1 
ATOM   1721 C CG  . PRO A 1 199 ? 6.967   8.680  75.503  1.00 11.45 ? 199 PRO A CG  1 
ATOM   1722 C CD  . PRO A 1 199 ? 5.462   8.823  75.223  1.00 12.26 ? 199 PRO A CD  1 
ATOM   1723 N N   . LEU A 1 200 ? 8.136   12.429 75.280  1.00 11.32 ? 200 LEU A N   1 
ATOM   1724 C CA  . LEU A 1 200 ? 9.142   12.987 74.368  1.00 10.18 ? 200 LEU A CA  1 
ATOM   1725 C C   . LEU A 1 200 ? 10.260  11.970 74.161  1.00 11.14 ? 200 LEU A C   1 
ATOM   1726 O O   . LEU A 1 200 ? 11.254  11.943 74.896  1.00 12.58 ? 200 LEU A O   1 
ATOM   1727 C CB  . LEU A 1 200 ? 9.699   14.290 74.922  1.00 15.21 ? 200 LEU A CB  1 
ATOM   1728 C CG  . LEU A 1 200 ? 8.655   15.406 75.030  1.00 16.97 ? 200 LEU A CG  1 
ATOM   1729 C CD1 . LEU A 1 200 ? 9.200   16.500 75.911  1.00 11.17 ? 200 LEU A CD1 1 
ATOM   1730 C CD2 . LEU A 1 200 ? 8.296   15.961 73.644  1.00 21.06 ? 200 LEU A CD2 1 
ATOM   1731 N N   . ILE A 1 201 ? 10.099  11.148 73.126  1.00 11.58 ? 201 ILE A N   1 
ATOM   1732 C CA  . ILE A 1 201 ? 11.078  10.084 72.856  1.00 9.88  ? 201 ILE A CA  1 
ATOM   1733 C C   . ILE A 1 201 ? 12.495  10.618 72.674  1.00 15.37 ? 201 ILE A C   1 
ATOM   1734 O O   . ILE A 1 201 ? 13.429  10.007 73.209  1.00 13.78 ? 201 ILE A O   1 
ATOM   1735 C CB  . ILE A 1 201 ? 10.602  9.226  71.674  1.00 12.03 ? 201 ILE A CB  1 
ATOM   1736 C CG1 . ILE A 1 201 ? 9.336   8.453  72.048  1.00 12.28 ? 201 ILE A CG1 1 
ATOM   1737 C CG2 . ILE A 1 201 ? 11.714  8.288  71.172  1.00 12.28 ? 201 ILE A CG2 1 
ATOM   1738 C CD1 . ILE A 1 201 ? 9.562   7.287  73.009  1.00 11.48 ? 201 ILE A CD1 1 
ATOM   1739 N N   . PRO A 1 202 ? 12.747  11.713 71.935  1.00 15.39 ? 202 PRO A N   1 
ATOM   1740 C CA  . PRO A 1 202 ? 14.148  12.161 71.789  1.00 11.57 ? 202 PRO A CA  1 
ATOM   1741 C C   . PRO A 1 202 ? 14.823  12.468 73.114  1.00 11.01 ? 202 PRO A C   1 
ATOM   1742 O O   . PRO A 1 202 ? 16.019  12.206 73.270  1.00 12.39 ? 202 PRO A O   1 
ATOM   1743 C CB  . PRO A 1 202 ? 14.034  13.420 70.913  1.00 14.40 ? 202 PRO A CB  1 
ATOM   1744 C CG  . PRO A 1 202 ? 12.826  13.195 70.100  1.00 13.32 ? 202 PRO A CG  1 
ATOM   1745 C CD  . PRO A 1 202 ? 11.852  12.479 71.041  1.00 14.81 ? 202 PRO A CD  1 
ATOM   1746 N N   . ILE A 1 203 ? 14.080  12.998 74.088  1.00 12.25 ? 203 ILE A N   1 
ATOM   1747 C CA  . ILE A 1 203 ? 14.680  13.312 75.381  1.00 12.24 ? 203 ILE A CA  1 
ATOM   1748 C C   . ILE A 1 203 ? 14.958  12.036 76.168  1.00 10.74 ? 203 ILE A C   1 
ATOM   1749 O O   . ILE A 1 203 ? 16.026  11.889 76.775  1.00 11.77 ? 203 ILE A O   1 
ATOM   1750 C CB  . ILE A 1 203 ? 13.784  14.285 76.171  1.00 13.03 ? 203 ILE A CB  1 
ATOM   1751 C CG1 . ILE A 1 203 ? 13.897  15.693 75.580  1.00 15.64 ? 203 ILE A CG1 1 
ATOM   1752 C CG2 . ILE A 1 203 ? 14.199  14.328 77.655  1.00 13.86 ? 203 ILE A CG2 1 
ATOM   1753 C CD1 . ILE A 1 203 ? 12.969  16.694 76.250  1.00 17.71 ? 203 ILE A CD1 1 
ATOM   1754 N N   . LEU A 1 204 ? 14.008  11.093 76.170  1.00 12.19 ? 204 LEU A N   1 
ATOM   1755 C CA  . LEU A 1 204 ? 14.245  9.822  76.852  1.00 12.42 ? 204 LEU A CA  1 
ATOM   1756 C C   . LEU A 1 204 ? 15.465  9.116  76.276  1.00 12.54 ? 204 LEU A C   1 
ATOM   1757 O O   . LEU A 1 204 ? 16.252  8.506  77.016  1.00 12.49 ? 204 LEU A O   1 
ATOM   1758 C CB  . LEU A 1 204 ? 13.013  8.912  76.754  1.00 10.48 ? 204 LEU A CB  1 
ATOM   1759 C CG  . LEU A 1 204 ? 11.668  9.364  77.364  1.00 13.66 ? 204 LEU A CG  1 
ATOM   1760 C CD1 . LEU A 1 204 ? 10.640  8.221  77.311  1.00 13.33 ? 204 LEU A CD1 1 
ATOM   1761 C CD2 . LEU A 1 204 ? 11.811  9.928  78.781  1.00 19.41 ? 204 LEU A CD2 1 
ATOM   1762 N N   . LEU A 1 205 ? 15.635  9.171  74.952  1.00 11.35 ? 205 LEU A N   1 
ATOM   1763 C CA  . LEU A 1 205 ? 16.807  8.544  74.344  1.00 11.95 ? 205 LEU A CA  1 
ATOM   1764 C C   . LEU A 1 205 ? 18.079  9.312  74.661  1.00 14.75 ? 205 LEU A C   1 
ATOM   1765 O O   . LEU A 1 205 ? 19.130  8.709  74.917  1.00 18.22 ? 205 LEU A O   1 
ATOM   1766 C CB  . LEU A 1 205 ? 16.625  8.438  72.835  1.00 12.02 ? 205 LEU A CB  1 
ATOM   1767 C CG  . LEU A 1 205 ? 15.617  7.371  72.419  1.00 11.89 ? 205 LEU A CG  1 
ATOM   1768 C CD1 . LEU A 1 205 ? 15.342  7.492  70.935  1.00 14.86 ? 205 LEU A CD1 1 
ATOM   1769 C CD2 . LEU A 1 205 ? 16.144  5.955  72.782  1.00 15.67 ? 205 LEU A CD2 1 
ATOM   1770 N N   . ASN A 1 206 ? 18.021  10.633 74.603  1.00 12.92 ? 206 ASN A N   1 
ATOM   1771 C CA  . ASN A 1 206 ? 19.239  11.413 74.761  1.00 14.61 ? 206 ASN A CA  1 
ATOM   1772 C C   . ASN A 1 206 ? 18.878  12.832 75.165  1.00 15.18 ? 206 ASN A C   1 
ATOM   1773 O O   . ASN A 1 206 ? 18.622  13.676 74.298  1.00 13.59 ? 206 ASN A O   1 
ATOM   1774 C CB  . ASN A 1 206 ? 20.066  11.399 73.465  1.00 17.58 ? 206 ASN A CB  1 
ATOM   1775 C CG  . ASN A 1 206 ? 21.436  12.038 73.637  1.00 28.93 ? 206 ASN A CG  1 
ATOM   1776 O OD1 . ASN A 1 206 ? 21.693  12.721 74.625  1.00 18.54 ? 206 ASN A OD1 1 
ATOM   1777 N ND2 . ASN A 1 206 ? 22.336  11.782 72.692  1.00 36.59 ? 206 ASN A ND2 1 
ATOM   1778 N N   . PRO A 1 207 ? 18.837  13.129 76.464  1.00 15.17 ? 207 PRO A N   1 
ATOM   1779 C CA  . PRO A 1 207 ? 18.476  14.486 76.899  1.00 12.92 ? 207 PRO A CA  1 
ATOM   1780 C C   . PRO A 1 207 ? 19.345  15.562 76.291  1.00 19.65 ? 207 PRO A C   1 
ATOM   1781 O O   . PRO A 1 207 ? 18.918  16.721 76.216  1.00 19.42 ? 207 PRO A O   1 
ATOM   1782 C CB  . PRO A 1 207 ? 18.648  14.420 78.423  1.00 17.01 ? 207 PRO A CB  1 
ATOM   1783 C CG  . PRO A 1 207 ? 18.401  12.986 78.759  1.00 19.28 ? 207 PRO A CG  1 
ATOM   1784 C CD  . PRO A 1 207 ? 19.012  12.206 77.599  1.00 18.36 ? 207 PRO A CD  1 
ATOM   1785 N N   . ASN A 1 208 ? 20.548  15.222 75.833  1.00 15.84 ? 208 ASN A N   1 
ATOM   1786 C CA  . ASN A 1 208 ? 21.390  16.254 75.260  1.00 13.43 ? 208 ASN A CA  1 
ATOM   1787 C C   . ASN A 1 208 ? 20.874  16.736 73.913  1.00 13.26 ? 208 ASN A C   1 
ATOM   1788 O O   . ASN A 1 208 ? 21.399  17.731 73.401  1.00 17.29 ? 208 ASN A O   1 
ATOM   1789 C CB  . ASN A 1 208 ? 22.820  15.753 75.105  1.00 18.11 ? 208 ASN A CB  1 
ATOM   1790 C CG  . ASN A 1 208 ? 23.456  15.373 76.437  1.00 24.87 ? 208 ASN A CG  1 
ATOM   1791 O OD1 . ASN A 1 208 ? 23.151  15.957 77.486  1.00 20.84 ? 208 ASN A OD1 1 
ATOM   1792 N ND2 . ASN A 1 208 ? 24.338  14.384 76.396  1.00 27.57 ? 208 ASN A ND2 1 
ATOM   1793 N N   . CYS A 1 209 ? 19.852  16.085 73.335  1.00 16.59 ? 209 CYS A N   1 
ATOM   1794 C CA  . CYS A 1 209 ? 19.379  16.551 72.035  1.00 16.30 ? 209 CYS A CA  1 
ATOM   1795 C C   . CYS A 1 209 ? 18.743  17.937 72.132  1.00 15.81 ? 209 CYS A C   1 
ATOM   1796 O O   . CYS A 1 209 ? 18.560  18.597 71.102  1.00 15.16 ? 209 CYS A O   1 
ATOM   1797 C CB  . CYS A 1 209 ? 18.383  15.561 71.416  1.00 20.11 ? 209 CYS A CB  1 
ATOM   1798 S SG  . CYS A 1 209 ? 16.813  15.466 72.277  1.00 20.13 ? 209 CYS A SG  1 
ATOM   1799 N N   . VAL A 1 210 ? 18.423  18.398 73.344  1.00 16.95 ? 210 VAL A N   1 
ATOM   1800 C CA  . VAL A 1 210 ? 17.837  19.725 73.489  1.00 18.26 ? 210 VAL A CA  1 
ATOM   1801 C C   . VAL A 1 210 ? 18.826  20.793 73.058  1.00 18.66 ? 210 VAL A C   1 
ATOM   1802 O O   . VAL A 1 210 ? 18.424  21.876 72.613  1.00 16.77 ? 210 VAL A O   1 
ATOM   1803 C CB  . VAL A 1 210 ? 17.352  19.960 74.935  1.00 20.97 ? 210 VAL A CB  1 
ATOM   1804 C CG1 . VAL A 1 210 ? 16.348  18.879 75.340  1.00 16.43 ? 210 VAL A CG1 1 
ATOM   1805 C CG2 . VAL A 1 210 ? 18.526  19.997 75.904  1.00 17.73 ? 210 VAL A CG2 1 
ATOM   1806 N N   . TYR A 1 211 ? 20.132  20.515 73.162  1.00 15.31 ? 211 TYR A N   1 
ATOM   1807 C CA  . TYR A 1 211 ? 21.116  21.523 72.800  1.00 15.45 ? 211 TYR A CA  1 
ATOM   1808 C C   . TYR A 1 211 ? 21.298  21.664 71.299  1.00 15.84 ? 211 TYR A C   1 
ATOM   1809 O O   . TYR A 1 211 ? 22.066  22.530 70.867  1.00 17.73 ? 211 TYR A O   1 
ATOM   1810 C CB  . TYR A 1 211 ? 22.464  21.208 73.456  1.00 16.79 ? 211 TYR A CB  1 
ATOM   1811 C CG  . TYR A 1 211 ? 22.334  21.040 74.948  1.00 16.93 ? 211 TYR A CG  1 
ATOM   1812 C CD1 . TYR A 1 211 ? 21.936  22.101 75.755  1.00 23.77 ? 211 TYR A CD1 1 
ATOM   1813 C CD2 . TYR A 1 211 ? 22.608  19.821 75.548  1.00 25.78 ? 211 TYR A CD2 1 
ATOM   1814 C CE1 . TYR A 1 211 ? 21.811  21.944 77.121  1.00 27.17 ? 211 TYR A CE1 1 
ATOM   1815 C CE2 . TYR A 1 211 ? 22.487  19.656 76.891  1.00 31.69 ? 211 TYR A CE2 1 
ATOM   1816 C CZ  . TYR A 1 211 ? 22.094  20.707 77.676  1.00 33.09 ? 211 TYR A CZ  1 
ATOM   1817 O OH  . TYR A 1 211 ? 21.996  20.502 79.028  1.00 40.85 ? 211 TYR A OH  1 
ATOM   1818 N N   . GLU A 1 212 ? 20.620  20.843 70.500  1.00 14.66 ? 212 GLU A N   1 
ATOM   1819 C CA  . GLU A 1 212 ? 20.691  21.023 69.055  1.00 18.97 ? 212 GLU A CA  1 
ATOM   1820 C C   . GLU A 1 212 ? 20.005  22.307 68.618  1.00 22.32 ? 212 GLU A C   1 
ATOM   1821 O O   . GLU A 1 212 ? 20.416  22.915 67.628  1.00 24.17 ? 212 GLU A O   1 
ATOM   1822 C CB  . GLU A 1 212 ? 20.111  19.800 68.349  1.00 18.44 ? 212 GLU A CB  1 
ATOM   1823 C CG  . GLU A 1 212 ? 20.915  18.526 68.658  1.00 21.46 ? 212 GLU A CG  1 
ATOM   1824 C CD  . GLU A 1 212 ? 20.469  17.320 67.858  1.00 30.91 ? 212 GLU A CD  1 
ATOM   1825 O OE1 . GLU A 1 212 ? 20.721  16.184 68.305  1.00 38.65 ? 212 GLU A OE1 1 
ATOM   1826 O OE2 . GLU A 1 212 ? 19.846  17.508 66.793  1.00 39.77 ? 212 GLU A OE2 1 
ATOM   1827 N N   . THR A 1 213 ? 19.012  22.776 69.376  1.00 17.70 ? 213 THR A N   1 
ATOM   1828 C CA  . THR A 1 213 ? 18.321  24.014 69.041  1.00 20.46 ? 213 THR A CA  1 
ATOM   1829 C C   . THR A 1 213 ? 18.430  25.103 70.096  1.00 24.71 ? 213 THR A C   1 
ATOM   1830 O O   . THR A 1 213 ? 18.372  26.284 69.736  1.00 23.34 ? 213 THR A O   1 
ATOM   1831 C CB  . THR A 1 213 ? 16.839  23.741 68.790  1.00 20.53 ? 213 THR A CB  1 
ATOM   1832 O OG1 . THR A 1 213 ? 16.300  23.075 69.935  1.00 24.21 ? 213 THR A OG1 1 
ATOM   1833 C CG2 . THR A 1 213 ? 16.685  22.869 67.567  1.00 19.32 ? 213 THR A CG2 1 
ATOM   1834 N N   . THR A 1 214 ? 18.568  24.755 71.377  1.00 20.90 ? 214 THR A N   1 
ATOM   1835 C CA  . THR A 1 214 ? 18.609  25.733 72.469  1.00 15.70 ? 214 THR A CA  1 
ATOM   1836 C C   . THR A 1 214 ? 19.850  25.473 73.314  1.00 19.96 ? 214 THR A C   1 
ATOM   1837 O O   . THR A 1 214 ? 19.769  24.878 74.396  1.00 20.78 ? 214 THR A O   1 
ATOM   1838 C CB  . THR A 1 214 ? 17.333  25.673 73.321  1.00 17.44 ? 214 THR A CB  1 
ATOM   1839 O OG1 . THR A 1 214 ? 17.167  24.354 73.863  1.00 19.94 ? 214 THR A OG1 1 
ATOM   1840 C CG2 . THR A 1 214 ? 16.105  26.008 72.472  1.00 16.70 ? 214 THR A CG2 1 
ATOM   1841 N N   . PRO A 1 215 ? 21.020  25.929 72.858  1.00 20.81 ? 215 PRO A N   1 
ATOM   1842 C CA  . PRO A 1 215 ? 22.260  25.635 73.601  1.00 22.95 ? 215 PRO A CA  1 
ATOM   1843 C C   . PRO A 1 215 ? 22.340  26.256 74.990  1.00 25.14 ? 215 PRO A C   1 
ATOM   1844 O O   . PRO A 1 215 ? 23.130  25.769 75.808  1.00 24.64 ? 215 PRO A O   1 
ATOM   1845 C CB  . PRO A 1 215 ? 23.363  26.190 72.680  1.00 27.56 ? 215 PRO A CB  1 
ATOM   1846 C CG  . PRO A 1 215 ? 22.676  27.184 71.800  1.00 29.78 ? 215 PRO A CG  1 
ATOM   1847 C CD  . PRO A 1 215 ? 21.285  26.644 71.598  1.00 25.78 ? 215 PRO A CD  1 
ATOM   1848 N N   . ASN A 1 216 ? 21.561  27.294 75.299  1.00 24.95 ? 216 ASN A N   1 
ATOM   1849 C CA  . ASN A 1 216 ? 21.678  27.966 76.588  1.00 33.11 ? 216 ASN A CA  1 
ATOM   1850 C C   . ASN A 1 216 ? 20.773  27.383 77.666  1.00 32.06 ? 216 ASN A C   1 
ATOM   1851 O O   . ASN A 1 216 ? 20.805  27.858 78.805  1.00 36.22 ? 216 ASN A O   1 
ATOM   1852 C CB  . ASN A 1 216 ? 21.384  29.461 76.433  1.00 34.69 ? 216 ASN A CB  1 
ATOM   1853 C CG  . ASN A 1 216 ? 22.431  30.169 75.606  1.00 40.64 ? 216 ASN A CG  1 
ATOM   1854 O OD1 . ASN A 1 216 ? 22.127  30.770 74.577  1.00 44.77 ? 216 ASN A OD1 1 
ATOM   1855 N ND2 . ASN A 1 216 ? 23.684  30.075 76.039  1.00 43.63 ? 216 ASN A ND2 1 
ATOM   1856 N N   . VAL A 1 217 ? 19.980  26.366 77.350  1.00 30.45 ? 217 VAL A N   1 
ATOM   1857 C CA  . VAL A 1 217 ? 19.005  25.866 78.308  1.00 24.52 ? 217 VAL A CA  1 
ATOM   1858 C C   . VAL A 1 217 ? 19.723  25.103 79.417  1.00 25.25 ? 217 VAL A C   1 
ATOM   1859 O O   . VAL A 1 217 ? 20.756  24.453 79.191  1.00 20.69 ? 217 VAL A O   1 
ATOM   1860 C CB  . VAL A 1 217 ? 17.962  24.999 77.577  1.00 23.81 ? 217 VAL A CB  1 
ATOM   1861 C CG1 . VAL A 1 217 ? 18.561  23.683 77.137  1.00 22.77 ? 217 VAL A CG1 1 
ATOM   1862 C CG2 . VAL A 1 217 ? 16.746  24.761 78.435  1.00 22.71 ? 217 VAL A CG2 1 
ATOM   1863 N N   . LYS A 1 218 ? 19.211  25.222 80.638  1.00 18.57 ? 218 LYS A N   1 
ATOM   1864 C CA  . LYS A 1 218 ? 19.665  24.402 81.747  1.00 20.88 ? 218 LYS A CA  1 
ATOM   1865 C C   . LYS A 1 218 ? 18.755  23.184 81.853  1.00 20.99 ? 218 LYS A C   1 
ATOM   1866 O O   . LYS A 1 218 ? 17.530  23.324 81.814  1.00 20.55 ? 218 LYS A O   1 
ATOM   1867 C CB  . LYS A 1 218 ? 19.633  25.184 83.057  1.00 23.36 ? 218 LYS A CB  1 
ATOM   1868 C CG  . LYS A 1 218 ? 20.592  26.358 83.107  1.00 34.45 ? 218 LYS A CG  1 
ATOM   1869 C CD  . LYS A 1 218 ? 20.483  27.094 84.436  1.00 43.46 ? 218 LYS A CD  1 
ATOM   1870 C CE  . LYS A 1 218 ? 21.025  26.243 85.572  1.00 48.18 ? 218 LYS A CE  1 
ATOM   1871 N NZ  . LYS A 1 218 ? 21.064  26.984 86.866  1.00 53.80 ? 218 LYS A NZ  1 
ATOM   1872 N N   . ILE A 1 219 ? 19.347  22.002 81.994  1.00 17.84 ? 219 ILE A N   1 
ATOM   1873 C CA  . ILE A 1 219 ? 18.567  20.795 82.269  1.00 13.94 ? 219 ILE A CA  1 
ATOM   1874 C C   . ILE A 1 219 ? 19.143  20.123 83.505  1.00 17.52 ? 219 ILE A C   1 
ATOM   1875 O O   . ILE A 1 219 ? 20.305  20.352 83.871  1.00 16.53 ? 219 ILE A O   1 
ATOM   1876 C CB  . ILE A 1 219 ? 18.571  19.822 81.069  1.00 17.07 ? 219 ILE A CB  1 
ATOM   1877 C CG1 . ILE A 1 219 ? 19.953  19.186 80.913  1.00 18.31 ? 219 ILE A CG1 1 
ATOM   1878 C CG2 . ILE A 1 219 ? 18.088  20.525 79.801  1.00 16.88 ? 219 ILE A CG2 1 
ATOM   1879 C CD1 . ILE A 1 219 ? 19.982  18.083 79.864  1.00 26.39 ? 219 ILE A CD1 1 
ATOM   1880 N N   . PRO A 1 220 ? 18.348  19.303 84.188  1.00 20.10 ? 220 PRO A N   1 
ATOM   1881 C CA  . PRO A 1 220 ? 18.879  18.601 85.366  1.00 22.60 ? 220 PRO A CA  1 
ATOM   1882 C C   . PRO A 1 220 ? 19.854  17.483 85.012  1.00 17.71 ? 220 PRO A C   1 
ATOM   1883 O O   . PRO A 1 220 ? 20.103  17.181 83.845  1.00 15.89 ? 220 PRO A O   1 
ATOM   1884 C CB  . PRO A 1 220 ? 17.623  18.055 86.052  1.00 20.56 ? 220 PRO A CB  1 
ATOM   1885 C CG  . PRO A 1 220 ? 16.589  17.985 84.981  1.00 19.45 ? 220 PRO A CG  1 
ATOM   1886 C CD  . PRO A 1 220 ? 16.896  19.087 84.012  1.00 18.21 ? 220 PRO A CD  1 
ATOM   1887 N N   . ASP A 1 221 ? 20.423  16.885 86.061  1.00 19.16 ? 221 ASP A N   1 
ATOM   1888 C CA  . ASP A 1 221 ? 21.377  15.781 85.970  1.00 17.42 ? 221 ASP A CA  1 
ATOM   1889 C C   . ASP A 1 221 ? 20.622  14.486 85.670  1.00 18.49 ? 221 ASP A C   1 
ATOM   1890 O O   . ASP A 1 221 ? 20.023  13.886 86.564  1.00 17.88 ? 221 ASP A O   1 
ATOM   1891 C CB  . ASP A 1 221 ? 22.150  15.664 87.281  1.00 15.84 ? 221 ASP A CB  1 
ATOM   1892 C CG  . ASP A 1 221 ? 23.326  14.734 87.183  1.00 22.11 ? 221 ASP A CG  1 
ATOM   1893 O OD1 . ASP A 1 221 ? 23.769  14.467 86.053  1.00 18.72 ? 221 ASP A OD1 1 
ATOM   1894 O OD2 . ASP A 1 221 ? 23.789  14.244 88.235  1.00 26.18 ? 221 ASP A OD2 1 
ATOM   1895 N N   . PHE A 1 222 ? 20.643  14.037 84.409  1.00 13.72 ? 222 PHE A N   1 
ATOM   1896 C CA  . PHE A 1 222 ? 19.978  12.783 84.056  1.00 13.38 ? 222 PHE A CA  1 
ATOM   1897 C C   . PHE A 1 222 ? 20.872  11.616 84.475  1.00 13.92 ? 222 PHE A C   1 
ATOM   1898 O O   . PHE A 1 222 ? 21.546  10.969 83.665  1.00 15.55 ? 222 PHE A O   1 
ATOM   1899 C CB  . PHE A 1 222 ? 19.621  12.711 82.581  1.00 14.40 ? 222 PHE A CB  1 
ATOM   1900 C CG  . PHE A 1 222 ? 18.389  13.502 82.208  1.00 13.49 ? 222 PHE A CG  1 
ATOM   1901 C CD1 . PHE A 1 222 ? 18.406  14.892 82.169  1.00 13.84 ? 222 PHE A CD1 1 
ATOM   1902 C CD2 . PHE A 1 222 ? 17.192  12.844 81.977  1.00 14.42 ? 222 PHE A CD2 1 
ATOM   1903 C CE1 . PHE A 1 222 ? 17.246  15.618 81.828  1.00 15.38 ? 222 PHE A CE1 1 
ATOM   1904 C CE2 . PHE A 1 222 ? 16.034  13.540 81.655  1.00 15.11 ? 222 PHE A CE2 1 
ATOM   1905 C CZ  . PHE A 1 222 ? 16.051  14.932 81.581  1.00 16.85 ? 222 PHE A CZ  1 
ATOM   1906 N N   . ALA A 1 223 ? 20.858  11.335 85.779  1.00 15.18 ? 223 ALA A N   1 
ATOM   1907 C CA  . ALA A 1 223 ? 21.700  10.299 86.362  1.00 21.19 ? 223 ALA A CA  1 
ATOM   1908 C C   . ALA A 1 223 ? 21.183  8.884  86.117  1.00 20.28 ? 223 ALA A C   1 
ATOM   1909 O O   . ALA A 1 223 ? 21.802  7.935  86.601  1.00 24.69 ? 223 ALA A O   1 
ATOM   1910 C CB  . ALA A 1 223 ? 21.845  10.539 87.871  1.00 21.75 ? 223 ALA A CB  1 
ATOM   1911 N N   . VAL A 1 224 ? 20.069  8.720  85.396  1.00 16.96 ? 224 VAL A N   1 
ATOM   1912 C CA  . VAL A 1 224 ? 19.526  7.412  85.036  1.00 23.01 ? 224 VAL A CA  1 
ATOM   1913 C C   . VAL A 1 224 ? 19.303  7.403  83.533  1.00 17.11 ? 224 VAL A C   1 
ATOM   1914 O O   . VAL A 1 224 ? 19.085  8.446  82.914  1.00 18.92 ? 224 VAL A O   1 
ATOM   1915 C CB  . VAL A 1 224 ? 18.177  7.095  85.730  1.00 30.89 ? 224 VAL A CB  1 
ATOM   1916 C CG1 . VAL A 1 224 ? 17.918  5.600  85.762  1.00 33.85 ? 224 VAL A CG1 1 
ATOM   1917 C CG2 . VAL A 1 224 ? 18.110  7.685  87.082  1.00 36.42 ? 224 VAL A CG2 1 
ATOM   1918 N N   . SER A 1 225 ? 19.308  6.202  82.957  1.00 15.94 ? 225 SER A N   1 
ATOM   1919 C CA  . SER A 1 225 ? 19.008  6.021  81.547  1.00 16.40 ? 225 SER A CA  1 
ATOM   1920 C C   . SER A 1 225 ? 17.511  5.792  81.365  1.00 15.12 ? 225 SER A C   1 
ATOM   1921 O O   . SER A 1 225 ? 16.916  4.965  82.065  1.00 16.19 ? 225 SER A O   1 
ATOM   1922 C CB  . SER A 1 225 ? 19.786  4.835  80.973  1.00 19.16 ? 225 SER A CB  1 
ATOM   1923 O OG  . SER A 1 225 ? 19.350  4.547  79.655  1.00 15.99 ? 225 SER A OG  1 
ATOM   1924 N N   . PHE A 1 226 ? 16.910  6.528  80.426  1.00 14.02 ? 226 PHE A N   1 
ATOM   1925 C CA  . PHE A 1 226 ? 15.535  6.302  80.009  1.00 11.97 ? 226 PHE A CA  1 
ATOM   1926 C C   . PHE A 1 226 ? 15.463  5.616  78.651  1.00 14.88 ? 226 PHE A C   1 
ATOM   1927 O O   . PHE A 1 226 ? 14.379  5.540  78.062  1.00 13.58 ? 226 PHE A O   1 
ATOM   1928 C CB  . PHE A 1 226 ? 14.768  7.627  79.960  1.00 12.62 ? 226 PHE A CB  1 
ATOM   1929 C CG  . PHE A 1 226 ? 14.492  8.236  81.316  1.00 11.36 ? 226 PHE A CG  1 
ATOM   1930 C CD1 . PHE A 1 226 ? 13.437  7.773  82.093  1.00 11.22 ? 226 PHE A CD1 1 
ATOM   1931 C CD2 . PHE A 1 226 ? 15.256  9.293  81.790  1.00 18.73 ? 226 PHE A CD2 1 
ATOM   1932 C CE1 . PHE A 1 226 ? 13.157  8.340  83.325  1.00 13.12 ? 226 PHE A CE1 1 
ATOM   1933 C CE2 . PHE A 1 226 ? 14.989  9.865  83.034  1.00 14.96 ? 226 PHE A CE2 1 
ATOM   1934 C CZ  . PHE A 1 226 ? 13.933  9.387  83.801  1.00 14.65 ? 226 PHE A CZ  1 
ATOM   1935 N N   . ARG A 1 227 ? 16.596  5.125  78.129  1.00 16.34 ? 227 ARG A N   1 
ATOM   1936 C CA  . ARG A 1 227 ? 16.595  4.594  76.769  1.00 13.38 ? 227 ARG A CA  1 
ATOM   1937 C C   . ARG A 1 227 ? 15.727  3.348  76.659  1.00 15.83 ? 227 ARG A C   1 
ATOM   1938 O O   . ARG A 1 227 ? 14.999  3.173  75.670  1.00 19.12 ? 227 ARG A O   1 
ATOM   1939 C CB  . ARG A 1 227 ? 18.019  4.294  76.315  1.00 17.93 ? 227 ARG A CB  1 
ATOM   1940 C CG  . ARG A 1 227 ? 18.866  5.528  76.159  1.00 22.67 ? 227 ARG A CG  1 
ATOM   1941 C CD  . ARG A 1 227 ? 20.249  5.162  75.663  1.00 28.16 ? 227 ARG A CD  1 
ATOM   1942 N NE  . ARG A 1 227 ? 20.215  4.507  74.358  1.00 28.72 ? 227 ARG A NE  1 
ATOM   1943 C CZ  . ARG A 1 227 ? 20.142  5.153  73.198  1.00 32.09 ? 227 ARG A CZ  1 
ATOM   1944 N NH1 . ARG A 1 227 ? 20.072  6.481  73.174  1.00 26.44 ? 227 ARG A NH1 1 
ATOM   1945 N NH2 . ARG A 1 227 ? 20.133  4.473  72.060  1.00 34.36 ? 227 ARG A NH2 1 
ATOM   1946 N N   . GLU A 1 228 ? 15.778  2.470  77.664  1.00 16.28 ? 228 GLU A N   1 
ATOM   1947 C CA  . GLU A 1 228 ? 14.948  1.272  77.614  1.00 16.01 ? 228 GLU A CA  1 
ATOM   1948 C C   . GLU A 1 228 ? 13.467  1.621  77.729  1.00 16.96 ? 228 GLU A C   1 
ATOM   1949 O O   . GLU A 1 228 ? 12.628  1.010  77.057  1.00 16.18 ? 228 GLU A O   1 
ATOM   1950 C CB  . GLU A 1 228 ? 15.355  0.291  78.714  1.00 23.93 ? 228 GLU A CB  1 
ATOM   1951 C CG  . GLU A 1 228 ? 14.418  -0.903 78.856  1.00 38.29 ? 228 GLU A CG  1 
ATOM   1952 C CD  . GLU A 1 228 ? 14.296  -1.737 77.584  1.00 56.45 ? 228 GLU A CD  1 
ATOM   1953 O OE1 . GLU A 1 228 ? 15.252  -1.759 76.775  1.00 62.84 ? 228 GLU A OE1 1 
ATOM   1954 O OE2 . GLU A 1 228 ? 13.236  -2.375 77.397  1.00 62.40 ? 228 GLU A OE2 1 
ATOM   1955 N N   . ASP A 1 229 ? 13.125  2.608  78.560  1.00 15.75 ? 229 ASP A N   1 
ATOM   1956 C CA  . ASP A 1 229 ? 11.729  3.031  78.645  1.00 13.22 ? 229 ASP A CA  1 
ATOM   1957 C C   . ASP A 1 229 ? 11.228  3.571  77.311  1.00 14.65 ? 229 ASP A C   1 
ATOM   1958 O O   . ASP A 1 229 ? 10.068  3.351  76.946  1.00 12.25 ? 229 ASP A O   1 
ATOM   1959 C CB  . ASP A 1 229 ? 11.541  4.086  79.733  1.00 11.32 ? 229 ASP A CB  1 
ATOM   1960 C CG  . ASP A 1 229 ? 11.546  3.494  81.141  1.00 18.86 ? 229 ASP A CG  1 
ATOM   1961 O OD1 . ASP A 1 229 ? 11.573  2.253  81.268  1.00 19.29 ? 229 ASP A OD1 1 
ATOM   1962 O OD2 . ASP A 1 229 ? 11.493  4.273  82.119  1.00 18.37 ? 229 ASP A OD2 1 
ATOM   1963 N N   . ALA A 1 230 ? 12.073  4.316  76.592  1.00 12.28 ? 230 ALA A N   1 
ATOM   1964 C CA  . ALA A 1 230 ? 11.683  4.808  75.272  1.00 13.33 ? 230 ALA A CA  1 
ATOM   1965 C C   . ALA A 1 230 ? 11.255  3.653  74.377  1.00 14.18 ? 230 ALA A C   1 
ATOM   1966 O O   . ALA A 1 230 ? 10.216  3.710  73.712  1.00 13.02 ? 230 ALA A O   1 
ATOM   1967 C CB  . ALA A 1 230 ? 12.840  5.574  74.630  1.00 14.62 ? 230 ALA A CB  1 
ATOM   1968 N N   . SER A 1 231 ? 12.058  2.593  74.354  1.00 12.62 ? 231 SER A N   1 
ATOM   1969 C CA  . SER A 1 231 ? 11.713  1.395  73.603  1.00 12.82 ? 231 SER A CA  1 
ATOM   1970 C C   . SER A 1 231 ? 10.414  0.758  74.114  1.00 15.47 ? 231 SER A C   1 
ATOM   1971 O O   . SER A 1 231 ? 9.558   0.350  73.311  1.00 19.41 ? 231 SER A O   1 
ATOM   1972 C CB  . SER A 1 231 ? 12.889  0.420  73.679  1.00 22.94 ? 231 SER A CB  1 
ATOM   1973 O OG  . SER A 1 231 ? 12.589  -0.793 73.037  1.00 32.53 ? 231 SER A OG  1 
ATOM   1974 N N   . LYS A 1 232 ? 10.229  0.697  75.441  1.00 13.37 ? 232 LYS A N   1 
ATOM   1975 C CA  . LYS A 1 232 ? 8.995   0.132  75.996  1.00 14.62 ? 232 LYS A CA  1 
ATOM   1976 C C   . LYS A 1 232 ? 7.761   0.927  75.585  1.00 14.59 ? 232 LYS A C   1 
ATOM   1977 O O   . LYS A 1 232 ? 6.714   0.333  75.301  1.00 13.99 ? 232 LYS A O   1 
ATOM   1978 C CB  . LYS A 1 232 ? 9.053   0.041  77.527  1.00 16.54 ? 232 LYS A CB  1 
ATOM   1979 C CG  . LYS A 1 232 ? 9.937   -1.056 78.067  1.00 33.34 ? 232 LYS A CG  1 
ATOM   1980 C CD  . LYS A 1 232 ? 9.888   -1.102 79.586  1.00 39.85 ? 232 LYS A CD  1 
ATOM   1981 C CE  . LYS A 1 232 ? 8.528   -1.602 80.063  1.00 49.34 ? 232 LYS A CE  1 
ATOM   1982 N NZ  . LYS A 1 232 ? 8.479   -1.812 81.544  1.00 57.25 ? 232 LYS A NZ  1 
ATOM   1983 N N   . HIS A 1 233 ? 7.830   2.270  75.586  1.00 16.63 ? 233 HIS A N   1 
ATOM   1984 C CA  . HIS A 1 233 ? 6.656   3.029  75.144  1.00 12.79 ? 233 HIS A CA  1 
ATOM   1985 C C   . HIS A 1 233 ? 6.250   2.613  73.734  1.00 12.92 ? 233 HIS A C   1 
ATOM   1986 O O   . HIS A 1 233 ? 5.059   2.489  73.436  1.00 13.29 ? 233 HIS A O   1 
ATOM   1987 C CB  . HIS A 1 233 ? 6.900   4.543  75.147  1.00 10.45 ? 233 HIS A CB  1 
ATOM   1988 C CG  . HIS A 1 233 ? 6.876   5.196  76.495  1.00 10.52 ? 233 HIS A CG  1 
ATOM   1989 N ND1 . HIS A 1 233 ? 5.718   5.669  77.084  1.00 10.76 ? 233 HIS A ND1 1 
ATOM   1990 C CD2 . HIS A 1 233 ? 7.882   5.500  77.349  1.00 11.40 ? 233 HIS A CD2 1 
ATOM   1991 C CE1 . HIS A 1 233 ? 6.012   6.216  78.251  1.00 12.44 ? 233 HIS A CE1 1 
ATOM   1992 N NE2 . HIS A 1 233 ? 7.319   6.133  78.432  1.00 12.15 ? 233 HIS A NE2 1 
ATOM   1993 N N   . VAL A 1 234 ? 7.227   2.444  72.837  1.00 13.41 ? 234 VAL A N   1 
ATOM   1994 C CA  . VAL A 1 234 ? 6.891   2.093  71.460  1.00 13.11 ? 234 VAL A CA  1 
ATOM   1995 C C   . VAL A 1 234 ? 6.373   0.669  71.388  1.00 14.81 ? 234 VAL A C   1 
ATOM   1996 O O   . VAL A 1 234 ? 5.398   0.380  70.683  1.00 14.22 ? 234 VAL A O   1 
ATOM   1997 C CB  . VAL A 1 234 ? 8.107   2.283  70.541  1.00 13.15 ? 234 VAL A CB  1 
ATOM   1998 C CG1 . VAL A 1 234 ? 7.751   1.867  69.114  1.00 13.53 ? 234 VAL A CG1 1 
ATOM   1999 C CG2 . VAL A 1 234 ? 8.591   3.752  70.593  1.00 12.74 ? 234 VAL A CG2 1 
ATOM   2000 N N   . GLU A 1 235 ? 7.024   -0.244 72.110  1.00 14.73 ? 235 GLU A N   1 
ATOM   2001 C CA  . GLU A 1 235 ? 6.649   -1.650 72.010  1.00 14.25 ? 235 GLU A CA  1 
ATOM   2002 C C   . GLU A 1 235 ? 5.280   -1.901 72.626  1.00 18.10 ? 235 GLU A C   1 
ATOM   2003 O O   . GLU A 1 235 ? 4.470   -2.638 72.055  1.00 18.81 ? 235 GLU A O   1 
ATOM   2004 C CB  . GLU A 1 235 ? 7.713   -2.526 72.673  1.00 22.95 ? 235 GLU A CB  1 
ATOM   2005 C CG  . GLU A 1 235 ? 7.527   -4.007 72.396  1.00 40.49 ? 235 GLU A CG  1 
ATOM   2006 C CD  . GLU A 1 235 ? 7.740   -4.358 70.926  1.00 51.84 ? 235 GLU A CD  1 
ATOM   2007 O OE1 . GLU A 1 235 ? 8.596   -3.724 70.266  1.00 52.75 ? 235 GLU A OE1 1 
ATOM   2008 O OE2 . GLU A 1 235 ? 7.031   -5.258 70.427  1.00 53.37 ? 235 GLU A OE2 1 
ATOM   2009 N N   . LEU A 1 236 ? 4.998   -1.289 73.785  1.00 13.77 ? 236 LEU A N   1 
ATOM   2010 C CA  . LEU A 1 236 ? 3.687   -1.459 74.414  1.00 13.38 ? 236 LEU A CA  1 
ATOM   2011 C C   . LEU A 1 236 ? 2.572   -0.848 73.575  1.00 11.64 ? 236 LEU A C   1 
ATOM   2012 O O   . LEU A 1 236 ? 1.437   -1.346 73.595  1.00 13.99 ? 236 LEU A O   1 
ATOM   2013 C CB  . LEU A 1 236 ? 3.693   -0.841 75.811  1.00 16.68 ? 236 LEU A CB  1 
ATOM   2014 C CG  . LEU A 1 236 ? 4.593   -1.587 76.797  1.00 14.83 ? 236 LEU A CG  1 
ATOM   2015 C CD1 . LEU A 1 236 ? 4.716   -0.814 78.119  1.00 15.73 ? 236 LEU A CD1 1 
ATOM   2016 C CD2 . LEU A 1 236 ? 4.103   -3.022 77.019  1.00 21.79 ? 236 LEU A CD2 1 
ATOM   2017 N N   . ALA A 1 237 ? 2.874   0.241  72.868  1.00 14.48 ? 237 ALA A N   1 
ATOM   2018 C CA  . ALA A 1 237 ? 1.910   0.861  71.961  1.00 17.77 ? 237 ALA A CA  1 
ATOM   2019 C C   . ALA A 1 237 ? 1.589   -0.047 70.783  1.00 15.21 ? 237 ALA A C   1 
ATOM   2020 O O   . ALA A 1 237 ? 0.421   -0.168 70.376  1.00 13.13 ? 237 ALA A O   1 
ATOM   2021 C CB  . ALA A 1 237 ? 2.457   2.200  71.465  1.00 13.81 ? 237 ALA A CB  1 
ATOM   2022 N N   . LYS A 1 238 ? 2.609   -0.687 70.208  1.00 11.90 ? 238 LYS A N   1 
ATOM   2023 C CA  . LYS A 1 238 ? 2.349   -1.682 69.173  1.00 13.76 ? 238 LYS A CA  1 
ATOM   2024 C C   . LYS A 1 238 ? 1.420   -2.773 69.687  1.00 18.25 ? 238 LYS A C   1 
ATOM   2025 O O   . LYS A 1 238 ? 0.508   -3.207 68.972  1.00 18.32 ? 238 LYS A O   1 
ATOM   2026 C CB  . LYS A 1 238 ? 3.662   -2.295 68.672  1.00 15.61 ? 238 LYS A CB  1 
ATOM   2027 C CG  . LYS A 1 238 ? 4.519   -1.333 67.836  1.00 18.39 ? 238 LYS A CG  1 
ATOM   2028 C CD  . LYS A 1 238 ? 5.892   -1.932 67.513  1.00 17.60 ? 238 LYS A CD  1 
ATOM   2029 C CE  . LYS A 1 238 ? 5.772   -3.125 66.580  1.00 27.69 ? 238 LYS A CE  1 
ATOM   2030 N NZ  . LYS A 1 238 ? 7.107   -3.751 66.323  1.00 31.93 ? 238 LYS A NZ  1 
ATOM   2031 N N   . GLU A 1 239 ? 1.641   -3.231 70.926  1.00 14.19 ? 239 GLU A N   1 
ATOM   2032 C CA  . GLU A 1 239 ? 0.822   -4.299 71.483  1.00 21.80 ? 239 GLU A CA  1 
ATOM   2033 C C   . GLU A 1 239 ? -0.614  -3.833 71.727  1.00 15.22 ? 239 GLU A C   1 
ATOM   2034 O O   . GLU A 1 239 ? -1.559  -4.586 71.469  1.00 18.13 ? 239 GLU A O   1 
ATOM   2035 C CB  . GLU A 1 239 ? 1.444   -4.829 72.779  1.00 29.03 ? 239 GLU A CB  1 
ATOM   2036 C CG  . GLU A 1 239 ? 2.812   -5.489 72.588  1.00 49.90 ? 239 GLU A CG  1 
ATOM   2037 C CD  . GLU A 1 239 ? 3.554   -5.722 73.902  1.00 66.65 ? 239 GLU A CD  1 
ATOM   2038 O OE1 . GLU A 1 239 ? 2.946   -5.514 74.974  1.00 71.24 ? 239 GLU A OE1 1 
ATOM   2039 O OE2 . GLU A 1 239 ? 4.748   -6.104 73.860  1.00 70.33 ? 239 GLU A OE2 1 
ATOM   2040 N N   . LYS A 1 240 ? -0.800  -2.606 72.225  1.00 17.08 ? 240 LYS A N   1 
ATOM   2041 C CA  . LYS A 1 240 ? -2.158  -2.131 72.477  1.00 18.02 ? 240 LYS A CA  1 
ATOM   2042 C C   . LYS A 1 240 ? -2.912  -1.948 71.173  1.00 18.36 ? 240 LYS A C   1 
ATOM   2043 O O   . LYS A 1 240 ? -4.091  -2.317 71.059  1.00 18.20 ? 240 LYS A O   1 
ATOM   2044 C CB  . LYS A 1 240 ? -2.145  -0.810 73.254  1.00 17.22 ? 240 LYS A CB  1 
ATOM   2045 C CG  . LYS A 1 240 ? -3.551  -0.272 73.552  1.00 13.97 ? 240 LYS A CG  1 
ATOM   2046 C CD  . LYS A 1 240 ? -4.264  -1.136 74.606  1.00 15.90 ? 240 LYS A CD  1 
ATOM   2047 C CE  . LYS A 1 240 ? -5.639  -0.604 74.904  1.00 21.27 ? 240 LYS A CE  1 
ATOM   2048 N NZ  . LYS A 1 240 ? -6.368  -1.473 75.869  1.00 24.73 ? 240 LYS A NZ  1 
ATOM   2049 N N   . TYR A 1 241 ? -2.247  -1.378 70.176  1.00 13.81 ? 241 TYR A N   1 
ATOM   2050 C CA  . TYR A 1 241 ? -2.862  -1.224 68.868  1.00 17.18 ? 241 TYR A CA  1 
ATOM   2051 C C   . TYR A 1 241 ? -3.188  -2.582 68.256  1.00 22.37 ? 241 TYR A C   1 
ATOM   2052 O O   . TYR A 1 241 ? -4.268  -2.759 67.676  1.00 18.21 ? 241 TYR A O   1 
ATOM   2053 C CB  . TYR A 1 241 ? -1.927  -0.400 67.992  1.00 16.69 ? 241 TYR A CB  1 
ATOM   2054 C CG  . TYR A 1 241 ? -2.425  -0.065 66.611  1.00 25.11 ? 241 TYR A CG  1 
ATOM   2055 C CD1 . TYR A 1 241 ? -2.483  -1.041 65.619  1.00 25.37 ? 241 TYR A CD1 1 
ATOM   2056 C CD2 . TYR A 1 241 ? -2.783  1.221  66.274  1.00 25.17 ? 241 TYR A CD2 1 
ATOM   2057 C CE1 . TYR A 1 241 ? -2.916  -0.727 64.359  1.00 30.45 ? 241 TYR A CE1 1 
ATOM   2058 C CE2 . TYR A 1 241 ? -3.216  1.535  65.023  1.00 28.88 ? 241 TYR A CE2 1 
ATOM   2059 C CZ  . TYR A 1 241 ? -3.277  0.558  64.066  1.00 34.39 ? 241 TYR A CZ  1 
ATOM   2060 O OH  . TYR A 1 241 ? -3.708  0.896  62.809  1.00 40.19 ? 241 TYR A OH  1 
ATOM   2061 N N   . PHE A 1 242 ? -2.273  -3.552 68.397  1.00 20.22 ? 242 PHE A N   1 
ATOM   2062 C CA  . PHE A 1 242 ? -2.514  -4.908 67.921  1.00 20.55 ? 242 PHE A CA  1 
ATOM   2063 C C   . PHE A 1 242 ? -3.782  -5.480 68.545  1.00 24.15 ? 242 PHE A C   1 
ATOM   2064 O O   . PHE A 1 242 ? -4.579  -6.140 67.867  1.00 21.09 ? 242 PHE A O   1 
ATOM   2065 C CB  . PHE A 1 242 ? -1.304  -5.768 68.236  1.00 22.54 ? 242 PHE A CB  1 
ATOM   2066 C CG  . PHE A 1 242 ? -1.408  -7.184 67.725  1.00 28.48 ? 242 PHE A CG  1 
ATOM   2067 C CD1 . PHE A 1 242 ? -1.216  -7.476 66.391  1.00 29.12 ? 242 PHE A CD1 1 
ATOM   2068 C CD2 . PHE A 1 242 ? -1.618  -8.225 68.607  1.00 28.43 ? 242 PHE A CD2 1 
ATOM   2069 C CE1 . PHE A 1 242 ? -1.273  -8.781 65.943  1.00 33.71 ? 242 PHE A CE1 1 
ATOM   2070 C CE2 . PHE A 1 242 ? -1.676  -9.528 68.171  1.00 27.46 ? 242 PHE A CE2 1 
ATOM   2071 C CZ  . PHE A 1 242 ? -1.504  -9.806 66.841  1.00 25.42 ? 242 PHE A CZ  1 
ATOM   2072 N N   . GLU A 1 243 ? -3.986  -5.241 69.843  1.00 19.55 ? 243 GLU A N   1 
ATOM   2073 C CA  . GLU A 1 243 ? -5.155  -5.804 70.518  1.00 26.01 ? 243 GLU A CA  1 
ATOM   2074 C C   . GLU A 1 243 ? -6.456  -5.196 70.000  1.00 21.14 ? 243 GLU A C   1 
ATOM   2075 O O   . GLU A 1 243 ? -7.462  -5.907 69.851  1.00 25.06 ? 243 GLU A O   1 
ATOM   2076 C CB  . GLU A 1 243 ? -5.028  -5.607 72.029  1.00 30.14 ? 243 GLU A CB  1 
ATOM   2077 C CG  . GLU A 1 243 ? -3.934  -6.459 72.665  1.00 38.97 ? 243 GLU A CG  1 
ATOM   2078 C CD  . GLU A 1 243 ? -3.607  -6.034 74.089  1.00 46.67 ? 243 GLU A CD  1 
ATOM   2079 O OE1 . GLU A 1 243 ? -4.157  -5.008 74.548  1.00 47.37 ? 243 GLU A OE1 1 
ATOM   2080 O OE2 . GLU A 1 243 ? -2.779  -6.712 74.737  1.00 48.78 ? 243 GLU A OE2 1 
ATOM   2081 N N   . ILE A 1 244 ? -6.452  -3.895 69.706  1.00 21.23 ? 244 ILE A N   1 
ATOM   2082 C CA  . ILE A 1 244 ? -7.677  -3.193 69.332  1.00 20.91 ? 244 ILE A CA  1 
ATOM   2083 C C   . ILE A 1 244 ? -8.025  -3.441 67.868  1.00 22.97 ? 244 ILE A C   1 
ATOM   2084 O O   . ILE A 1 244 ? -9.179  -3.733 67.530  1.00 21.68 ? 244 ILE A O   1 
ATOM   2085 C CB  . ILE A 1 244 ? -7.528  -1.686 69.617  1.00 20.20 ? 244 ILE A CB  1 
ATOM   2086 C CG1 . ILE A 1 244 ? -7.217  -1.431 71.099  1.00 22.48 ? 244 ILE A CG1 1 
ATOM   2087 C CG2 . ILE A 1 244 ? -8.785  -0.929 69.137  1.00 19.69 ? 244 ILE A CG2 1 
ATOM   2088 C CD1 . ILE A 1 244 ? -8.335  -1.812 72.058  1.00 20.64 ? 244 ILE A CD1 1 
ATOM   2089 N N   . PHE A 1 245 ? -7.036  -3.328 66.976  1.00 19.66 ? 245 PHE A N   1 
ATOM   2090 C CA  . PHE A 1 245 ? -7.280  -3.376 65.539  1.00 24.25 ? 245 PHE A CA  1 
ATOM   2091 C C   . PHE A 1 245 ? -6.802  -4.658 64.877  1.00 25.11 ? 245 PHE A C   1 
ATOM   2092 O O   . PHE A 1 245 ? -7.147  -4.898 63.714  1.00 25.85 ? 245 PHE A O   1 
ATOM   2093 C CB  . PHE A 1 245 ? -6.635  -2.166 64.845  1.00 25.80 ? 245 PHE A CB  1 
ATOM   2094 C CG  . PHE A 1 245 ? -7.199  -0.862 65.307  1.00 23.04 ? 245 PHE A CG  1 
ATOM   2095 C CD1 . PHE A 1 245 ? -8.430  -0.438 64.836  1.00 18.73 ? 245 PHE A CD1 1 
ATOM   2096 C CD2 . PHE A 1 245 ? -6.512  -0.069 66.221  1.00 21.96 ? 245 PHE A CD2 1 
ATOM   2097 C CE1 . PHE A 1 245 ? -8.987  0.742  65.267  1.00 21.98 ? 245 PHE A CE1 1 
ATOM   2098 C CE2 . PHE A 1 245 ? -7.056  1.117  66.656  1.00 22.70 ? 245 PHE A CE2 1 
ATOM   2099 C CZ  . PHE A 1 245 ? -8.297  1.533  66.178  1.00 16.91 ? 245 PHE A CZ  1 
ATOM   2100 N N   . GLY A 1 246 ? -6.034  -5.486 65.571  1.00 19.19 ? 246 GLY A N   1 
ATOM   2101 C CA  . GLY A 1 246 ? -5.722  -6.806 65.065  1.00 27.94 ? 246 GLY A CA  1 
ATOM   2102 C C   . GLY A 1 246 ? -4.446  -6.914 64.264  1.00 26.42 ? 246 GLY A C   1 
ATOM   2103 O O   . GLY A 1 246 ? -4.100  -8.023 63.834  1.00 23.72 ? 246 GLY A O   1 
ATOM   2104 N N   . GLU A 1 247 ? -3.737  -5.809 64.047  1.00 23.71 ? 247 GLU A N   1 
ATOM   2105 C CA  . GLU A 1 247 ? -2.457  -5.846 63.364  1.00 24.35 ? 247 GLU A CA  1 
ATOM   2106 C C   . GLU A 1 247 ? -1.506  -4.878 64.050  1.00 27.49 ? 247 GLU A C   1 
ATOM   2107 O O   . GLU A 1 247 ? -1.922  -3.997 64.815  1.00 23.02 ? 247 GLU A O   1 
ATOM   2108 C CB  . GLU A 1 247 ? -2.608  -5.495 61.879  1.00 34.39 ? 247 GLU A CB  1 
ATOM   2109 C CG  . GLU A 1 247 ? -3.153  -4.099 61.647  1.00 44.00 ? 247 GLU A CG  1 
ATOM   2110 C CD  . GLU A 1 247 ? -3.191  -3.728 60.183  1.00 55.34 ? 247 GLU A CD  1 
ATOM   2111 O OE1 . GLU A 1 247 ? -2.772  -4.558 59.349  1.00 61.78 ? 247 GLU A OE1 1 
ATOM   2112 O OE2 . GLU A 1 247 ? -3.622  -2.601 59.868  1.00 58.42 ? 247 GLU A OE2 1 
ATOM   2113 N N   . HIS A 1 248 ? -0.223  -5.053 63.774  1.00 18.10 ? 248 HIS A N   1 
ATOM   2114 C CA  . HIS A 1 248 ? 0.727   -4.106 64.340  1.00 21.18 ? 248 HIS A CA  1 
ATOM   2115 C C   . HIS A 1 248 ? 0.696   -2.805 63.545  1.00 21.91 ? 248 HIS A C   1 
ATOM   2116 O O   . HIS A 1 248 ? 0.529   -2.827 62.325  1.00 25.88 ? 248 HIS A O   1 
ATOM   2117 C CB  . HIS A 1 248 ? 2.143   -4.692 64.346  1.00 24.86 ? 248 HIS A CB  1 
ATOM   2118 C CG  . HIS A 1 248 ? 2.292   -5.839 65.295  1.00 34.92 ? 248 HIS A CG  1 
ATOM   2119 N ND1 . HIS A 1 248 ? 2.303   -5.670 66.664  1.00 37.00 ? 248 HIS A ND1 1 
ATOM   2120 C CD2 . HIS A 1 248 ? 2.377   -7.172 65.077  1.00 36.08 ? 248 HIS A CD2 1 
ATOM   2121 C CE1 . HIS A 1 248 ? 2.410   -6.850 67.248  1.00 37.85 ? 248 HIS A CE1 1 
ATOM   2122 N NE2 . HIS A 1 248 ? 2.457   -7.777 66.308  1.00 37.82 ? 248 HIS A NE2 1 
ATOM   2123 N N   . PRO A 1 249 ? 0.832   -1.663 64.209  1.00 18.44 ? 249 PRO A N   1 
ATOM   2124 C CA  . PRO A 1 249 ? 0.821   -0.395 63.476  1.00 16.87 ? 249 PRO A CA  1 
ATOM   2125 C C   . PRO A 1 249 ? 2.119   -0.224 62.706  1.00 21.11 ? 249 PRO A C   1 
ATOM   2126 O O   . PRO A 1 249 ? 3.202   -0.516 63.213  1.00 26.69 ? 249 PRO A O   1 
ATOM   2127 C CB  . PRO A 1 249 ? 0.696   0.655  64.584  1.00 19.80 ? 249 PRO A CB  1 
ATOM   2128 C CG  . PRO A 1 249 ? 1.442   0.002  65.749  1.00 19.83 ? 249 PRO A CG  1 
ATOM   2129 C CD  . PRO A 1 249 ? 1.177   -1.488 65.631  1.00 18.32 ? 249 PRO A CD  1 
ATOM   2130 N N   . VAL A 1 250 ? 2.006   0.247  61.465  1.00 20.54 ? 250 VAL A N   1 
ATOM   2131 C CA  . VAL A 1 250 ? 3.181   0.612  60.684  1.00 21.86 ? 250 VAL A CA  1 
ATOM   2132 C C   . VAL A 1 250 ? 3.312   2.111  60.522  1.00 19.40 ? 250 VAL A C   1 
ATOM   2133 O O   . VAL A 1 250 ? 4.312   2.566  59.961  1.00 19.93 ? 250 VAL A O   1 
ATOM   2134 C CB  . VAL A 1 250 ? 3.199   -0.085 59.309  1.00 26.37 ? 250 VAL A CB  1 
ATOM   2135 C CG1 . VAL A 1 250 ? 3.205   -1.596 59.487  1.00 30.66 ? 250 VAL A CG1 1 
ATOM   2136 C CG2 . VAL A 1 250 ? 2.028   0.373  58.446  1.00 23.61 ? 250 VAL A CG2 1 
ATOM   2137 N N   . TYR A 1 251 ? 2.342   2.892  61.018  1.00 18.44 ? 251 TYR A N   1 
ATOM   2138 C CA  . TYR A 1 251 ? 2.374   4.352  61.032  1.00 22.87 ? 251 TYR A CA  1 
ATOM   2139 C C   . TYR A 1 251 ? 2.335   4.795  62.479  1.00 18.71 ? 251 TYR A C   1 
ATOM   2140 O O   . TYR A 1 251 ? 1.535   4.273  63.261  1.00 15.69 ? 251 TYR A O   1 
ATOM   2141 C CB  . TYR A 1 251 ? 1.165   4.964  60.320  1.00 28.15 ? 251 TYR A CB  1 
ATOM   2142 C CG  . TYR A 1 251 ? 0.865   4.303  59.020  1.00 32.35 ? 251 TYR A CG  1 
ATOM   2143 C CD1 . TYR A 1 251 ? 1.879   4.043  58.123  1.00 41.57 ? 251 TYR A CD1 1 
ATOM   2144 C CD2 . TYR A 1 251 ? -0.415  3.855  58.723  1.00 38.89 ? 251 TYR A CD2 1 
ATOM   2145 C CE1 . TYR A 1 251 ? 1.622   3.413  56.940  1.00 45.97 ? 251 TYR A CE1 1 
ATOM   2146 C CE2 . TYR A 1 251 ? -0.680  3.210  57.537  1.00 38.16 ? 251 TYR A CE2 1 
ATOM   2147 C CZ  . TYR A 1 251 ? 0.352   2.993  56.648  1.00 46.91 ? 251 TYR A CZ  1 
ATOM   2148 O OH  . TYR A 1 251 ? 0.151   2.349  55.450  1.00 54.09 ? 251 TYR A OH  1 
ATOM   2149 N N   . MET A 1 252 ? 3.164   5.764  62.835  1.00 13.33 ? 252 MET A N   1 
ATOM   2150 C CA  . MET A 1 252 ? 3.083   6.313  64.177  1.00 13.25 ? 252 MET A CA  1 
ATOM   2151 C C   . MET A 1 252 ? 3.185   7.822  64.103  1.00 11.05 ? 252 MET A C   1 
ATOM   2152 O O   . MET A 1 252 ? 3.904   8.358  63.255  1.00 11.52 ? 252 MET A O   1 
ATOM   2153 C CB  . MET A 1 252 ? 4.175   5.765  65.113  1.00 17.35 ? 252 MET A CB  1 
ATOM   2154 C CG  . MET A 1 252 ? 3.879   4.366  65.670  1.00 14.50 ? 252 MET A CG  1 
ATOM   2155 S SD  . MET A 1 252 ? 4.842   4.074  67.185  1.00 18.87 ? 252 MET A SD  1 
ATOM   2156 C CE  . MET A 1 252 ? 4.207   2.451  67.668  1.00 23.99 ? 252 MET A CE  1 
ATOM   2157 N N   . TRP A 1 253 ? 2.414   8.492  64.964  1.00 12.18 ? 253 TRP A N   1 
ATOM   2158 C CA  . TRP A 1 253 ? 2.580   9.914  65.189  1.00 9.55  ? 253 TRP A CA  1 
ATOM   2159 C C   . TRP A 1 253 ? 3.533   10.120 66.358  1.00 10.42 ? 253 TRP A C   1 
ATOM   2160 O O   . TRP A 1 253 ? 3.215   9.701  67.485  1.00 11.75 ? 253 TRP A O   1 
ATOM   2161 C CB  . TRP A 1 253 ? 1.243   10.590 65.475  1.00 9.28  ? 253 TRP A CB  1 
ATOM   2162 C CG  . TRP A 1 253 ? 1.412   12.020 65.932  1.00 9.02  ? 253 TRP A CG  1 
ATOM   2163 C CD1 . TRP A 1 253 ? 1.130   12.526 67.177  1.00 10.21 ? 253 TRP A CD1 1 
ATOM   2164 C CD2 . TRP A 1 253 ? 1.922   13.122 65.158  1.00 9.30  ? 253 TRP A CD2 1 
ATOM   2165 N NE1 . TRP A 1 253 ? 1.442   13.876 67.219  1.00 11.24 ? 253 TRP A NE1 1 
ATOM   2166 C CE2 . TRP A 1 253 ? 1.932   14.256 65.995  1.00 11.61 ? 253 TRP A CE2 1 
ATOM   2167 C CE3 . TRP A 1 253 ? 2.384   13.252 63.842  1.00 12.44 ? 253 TRP A CE3 1 
ATOM   2168 C CZ2 . TRP A 1 253 ? 2.370   15.507 65.555  1.00 12.69 ? 253 TRP A CZ2 1 
ATOM   2169 C CZ3 . TRP A 1 253 ? 2.836   14.500 63.413  1.00 12.54 ? 253 TRP A CZ3 1 
ATOM   2170 C CH2 . TRP A 1 253 ? 2.813   15.606 64.269  1.00 13.93 ? 253 TRP A CH2 1 
ATOM   2171 N N   . PRO A 1 254 ? 4.695   10.733 66.146  1.00 10.31 ? 254 PRO A N   1 
ATOM   2172 C CA  . PRO A 1 254 ? 5.590   11.040 67.261  1.00 13.03 ? 254 PRO A CA  1 
ATOM   2173 C C   . PRO A 1 254 ? 5.004   12.155 68.103  1.00 11.17 ? 254 PRO A C   1 
ATOM   2174 O O   . PRO A 1 254 ? 4.645   13.214 67.569  1.00 11.39 ? 254 PRO A O   1 
ATOM   2175 C CB  . PRO A 1 254 ? 6.887   11.489 66.570  1.00 13.68 ? 254 PRO A CB  1 
ATOM   2176 C CG  . PRO A 1 254 ? 6.435   12.026 65.246  1.00 15.07 ? 254 PRO A CG  1 
ATOM   2177 C CD  . PRO A 1 254 ? 5.226   11.196 64.846  1.00 10.69 ? 254 PRO A CD  1 
ATOM   2178 N N   . PRO A 1 255 ? 4.883   11.950 69.411  1.00 11.51 ? 255 PRO A N   1 
ATOM   2179 C CA  . PRO A 1 255 ? 4.291   12.978 70.280  1.00 11.16 ? 255 PRO A CA  1 
ATOM   2180 C C   . PRO A 1 255 ? 4.975   14.330 70.134  1.00 11.84 ? 255 PRO A C   1 
ATOM   2181 O O   . PRO A 1 255 ? 6.202   14.436 70.132  1.00 11.25 ? 255 PRO A O   1 
ATOM   2182 C CB  . PRO A 1 255 ? 4.489   12.408 71.686  1.00 12.11 ? 255 PRO A CB  1 
ATOM   2183 C CG  . PRO A 1 255 ? 4.470   10.903 71.468  1.00 12.79 ? 255 PRO A CG  1 
ATOM   2184 C CD  . PRO A 1 255 ? 5.178   10.700 70.128  1.00 10.25 ? 255 PRO A CD  1 
ATOM   2185 N N   . GLU A 1 256 ? 4.159   15.368 70.010  1.00 9.69  ? 256 GLU A N   1 
ATOM   2186 C CA  . GLU A 1 256 ? 4.623   16.741 69.793  1.00 9.13  ? 256 GLU A CA  1 
ATOM   2187 C C   . GLU A 1 256 ? 5.446   16.864 68.517  1.00 11.99 ? 256 GLU A C   1 
ATOM   2188 O O   . GLU A 1 256 ? 6.273   17.778 68.389  1.00 12.39 ? 256 GLU A O   1 
ATOM   2189 C CB  . GLU A 1 256 ? 5.393   17.281 71.017  1.00 8.67  ? 256 GLU A CB  1 
ATOM   2190 C CG  . GLU A 1 256 ? 4.550   16.958 72.278  1.00 11.46 ? 256 GLU A CG  1 
ATOM   2191 C CD  . GLU A 1 256 ? 3.355   17.884 72.430  1.00 15.94 ? 256 GLU A CD  1 
ATOM   2192 O OE1 . GLU A 1 256 ? 3.056   18.653 71.508  1.00 31.44 ? 256 GLU A OE1 1 
ATOM   2193 O OE2 . GLU A 1 256 ? 2.592   17.704 73.397  1.00 20.45 ? 256 GLU A OE2 1 
ATOM   2194 N N   . ALA A 1 257 ? 5.194   15.971 67.557  1.00 11.73 ? 257 ALA A N   1 
ATOM   2195 C CA  . ALA A 1 257 ? 5.957   15.909 66.308  1.00 12.97 ? 257 ALA A CA  1 
ATOM   2196 C C   . ALA A 1 257 ? 7.447   15.665 66.560  1.00 12.59 ? 257 ALA A C   1 
ATOM   2197 O O   . ALA A 1 257 ? 8.284   15.956 65.693  1.00 14.65 ? 257 ALA A O   1 
ATOM   2198 C CB  . ALA A 1 257 ? 5.769   17.197 65.475  1.00 10.88 ? 257 ALA A CB  1 
ATOM   2199 N N   . SER A 1 258 ? 7.806   15.114 67.722  1.00 11.21 ? 258 SER A N   1 
ATOM   2200 C CA  . SER A 1 258 ? 9.184   15.222 68.197  1.00 9.62  ? 258 SER A CA  1 
ATOM   2201 C C   . SER A 1 258 ? 10.035  14.132 67.562  1.00 9.96  ? 258 SER A C   1 
ATOM   2202 O O   . SER A 1 258 ? 9.726   12.938 67.668  1.00 12.41 ? 258 SER A O   1 
ATOM   2203 C CB  . SER A 1 258 ? 9.253   15.155 69.720  1.00 12.49 ? 258 SER A CB  1 
ATOM   2204 O OG  . SER A 1 258 ? 10.593  15.448 70.112  1.00 18.87 ? 258 SER A OG  1 
ATOM   2205 N N   . VAL A 1 259 ? 11.097  14.549 66.875  1.00 10.81 ? 259 VAL A N   1 
ATOM   2206 C CA  . VAL A 1 259 ? 12.000  13.617 66.231  1.00 10.84 ? 259 VAL A CA  1 
ATOM   2207 C C   . VAL A 1 259 ? 13.425  14.037 66.556  1.00 13.54 ? 259 VAL A C   1 
ATOM   2208 O O   . VAL A 1 259 ? 13.702  15.161 66.987  1.00 15.95 ? 259 VAL A O   1 
ATOM   2209 C CB  . VAL A 1 259 ? 11.805  13.522 64.696  1.00 12.60 ? 259 VAL A CB  1 
ATOM   2210 C CG1 . VAL A 1 259 ? 10.424  12.939 64.370  1.00 16.01 ? 259 VAL A CG1 1 
ATOM   2211 C CG2 . VAL A 1 259 ? 12.006  14.889 64.043  1.00 16.31 ? 259 VAL A CG2 1 
ATOM   2212 N N   . SER A 1 260 ? 14.320  13.087 66.363  1.00 13.43 ? 260 SER A N   1 
ATOM   2213 C CA  . SER A 1 260 ? 15.756  13.278 66.444  1.00 12.15 ? 260 SER A CA  1 
ATOM   2214 C C   . SER A 1 260 ? 16.328  12.155 65.604  1.00 12.70 ? 260 SER A C   1 
ATOM   2215 O O   . SER A 1 260 ? 15.603  11.228 65.229  1.00 13.71 ? 260 SER A O   1 
ATOM   2216 C CB  . SER A 1 260 ? 16.255  13.201 67.889  1.00 13.91 ? 260 SER A CB  1 
ATOM   2217 O OG  . SER A 1 260 ? 16.084  11.871 68.376  1.00 15.72 ? 260 SER A OG  1 
ATOM   2218 N N   . ASN A 1 261 ? 17.629  12.225 65.315  1.00 14.18 ? 261 ASN A N   1 
ATOM   2219 C CA  . ASN A 1 261 ? 18.250  11.122 64.585  1.00 20.76 ? 261 ASN A CA  1 
ATOM   2220 C C   . ASN A 1 261 ? 18.100  9.806  65.343  1.00 20.10 ? 261 ASN A C   1 
ATOM   2221 O O   . ASN A 1 261 ? 17.785  8.768  64.746  1.00 14.10 ? 261 ASN A O   1 
ATOM   2222 C CB  . ASN A 1 261 ? 19.724  11.420 64.303  1.00 14.74 ? 261 ASN A CB  1 
ATOM   2223 C CG  . ASN A 1 261 ? 19.895  12.516 63.280  1.00 16.60 ? 261 ASN A CG  1 
ATOM   2224 O OD1 . ASN A 1 261 ? 19.063  12.660 62.380  1.00 18.40 ? 261 ASN A OD1 1 
ATOM   2225 N ND2 . ASN A 1 261 ? 20.970  13.293 63.398  1.00 19.33 ? 261 ASN A ND2 1 
ATOM   2226 N N   . GLU A 1 262 ? 18.299  9.835  66.661  1.00 15.94 ? 262 GLU A N   1 
ATOM   2227 C CA  . GLU A 1 262 ? 18.184  8.612  67.448  1.00 16.54 ? 262 GLU A CA  1 
ATOM   2228 C C   . GLU A 1 262 ? 16.739  8.135  67.556  1.00 16.19 ? 262 GLU A C   1 
ATOM   2229 O O   . GLU A 1 262 ? 16.484  6.922  67.552  1.00 15.22 ? 262 GLU A O   1 
ATOM   2230 C CB  . GLU A 1 262 ? 18.798  8.825  68.836  1.00 21.95 ? 262 GLU A CB  1 
ATOM   2231 C CG  . GLU A 1 262 ? 20.266  9.263  68.755  1.00 26.90 ? 262 GLU A CG  1 
ATOM   2232 C CD  . GLU A 1 262 ? 20.941  9.332  70.113  1.00 40.26 ? 262 GLU A CD  1 
ATOM   2233 O OE1 . GLU A 1 262 ? 21.627  10.339 70.390  1.00 45.29 ? 262 GLU A OE1 1 
ATOM   2234 O OE2 . GLU A 1 262 ? 20.769  8.389  70.909  1.00 45.06 ? 262 GLU A OE2 1 
ATOM   2235 N N   . ALA A 1 263 ? 15.777  9.062  67.652  1.00 13.32 ? 263 ALA A N   1 
ATOM   2236 C CA  . ALA A 1 263 ? 14.370  8.651  67.706  1.00 14.35 ? 263 ALA A CA  1 
ATOM   2237 C C   . ALA A 1 263 ? 13.933  8.016  66.390  1.00 15.07 ? 263 ALA A C   1 
ATOM   2238 O O   . ALA A 1 263 ? 13.177  7.034  66.381  1.00 13.88 ? 263 ALA A O   1 
ATOM   2239 C CB  . ALA A 1 263 ? 13.485  9.850  68.048  1.00 11.44 ? 263 ALA A CB  1 
ATOM   2240 N N   . LEU A 1 264 ? 14.380  8.575  65.262  1.00 15.27 ? 264 LEU A N   1 
ATOM   2241 C CA  . LEU A 1 264 ? 14.035  7.978  63.975  1.00 15.71 ? 264 LEU A CA  1 
ATOM   2242 C C   . LEU A 1 264 ? 14.612  6.574  63.859  1.00 17.78 ? 264 LEU A C   1 
ATOM   2243 O O   . LEU A 1 264 ? 13.939  5.658  63.370  1.00 14.78 ? 264 LEU A O   1 
ATOM   2244 C CB  . LEU A 1 264 ? 14.527  8.870  62.832  1.00 16.86 ? 264 LEU A CB  1 
ATOM   2245 C CG  . LEU A 1 264 ? 13.725  10.167 62.705  1.00 16.86 ? 264 LEU A CG  1 
ATOM   2246 C CD1 . LEU A 1 264 ? 14.396  11.136 61.732  1.00 15.62 ? 264 LEU A CD1 1 
ATOM   2247 C CD2 . LEU A 1 264 ? 12.292  9.856  62.267  1.00 21.47 ? 264 LEU A CD2 1 
ATOM   2248 N N   . GLU A 1 265 ? 15.856  6.383  64.318  1.00 15.13 ? 265 GLU A N   1 
ATOM   2249 C CA  . GLU A 1 265 ? 16.431  5.042  64.346  1.00 20.72 ? 265 GLU A CA  1 
ATOM   2250 C C   . GLU A 1 265 ? 15.583  4.093  65.182  1.00 15.49 ? 265 GLU A C   1 
ATOM   2251 O O   . GLU A 1 265 ? 15.354  2.944  64.789  1.00 18.76 ? 265 GLU A O   1 
ATOM   2252 C CB  . GLU A 1 265 ? 17.870  5.074  64.866  1.00 22.85 ? 265 GLU A CB  1 
ATOM   2253 C CG  . GLU A 1 265 ? 18.436  3.665  65.069  1.00 45.98 ? 265 GLU A CG  1 
ATOM   2254 C CD  . GLU A 1 265 ? 18.906  3.003  63.777  1.00 58.27 ? 265 GLU A CD  1 
ATOM   2255 O OE1 . GLU A 1 265 ? 19.394  1.853  63.848  1.00 62.96 ? 265 GLU A OE1 1 
ATOM   2256 O OE2 . GLU A 1 265 ? 18.808  3.633  62.699  1.00 60.69 ? 265 GLU A OE2 1 
ATOM   2257 N N   . LEU A 1 266 ? 15.112  4.550  66.346  1.00 16.73 ? 266 LEU A N   1 
ATOM   2258 C CA  . LEU A 1 266 ? 14.302  3.676  67.198  1.00 14.18 ? 266 LEU A CA  1 
ATOM   2259 C C   . LEU A 1 266 ? 12.999  3.272  66.505  1.00 14.83 ? 266 LEU A C   1 
ATOM   2260 O O   . LEU A 1 266 ? 12.612  2.092  66.526  1.00 15.10 ? 266 LEU A O   1 
ATOM   2261 C CB  . LEU A 1 266 ? 14.011  4.366  68.530  1.00 14.54 ? 266 LEU A CB  1 
ATOM   2262 C CG  . LEU A 1 266 ? 13.068  3.592  69.448  1.00 12.49 ? 266 LEU A CG  1 
ATOM   2263 C CD1 . LEU A 1 266 ? 13.659  2.217  69.817  1.00 13.12 ? 266 LEU A CD1 1 
ATOM   2264 C CD2 . LEU A 1 266 ? 12.739  4.427  70.708  1.00 14.67 ? 266 LEU A CD2 1 
ATOM   2265 N N   . TYR A 1 267 ? 12.290  4.245  65.913  1.00 15.32 ? 267 TYR A N   1 
ATOM   2266 C CA  . TYR A 1 267 ? 11.055  3.924  65.197  1.00 16.38 ? 267 TYR A CA  1 
ATOM   2267 C C   . TYR A 1 267 ? 11.309  2.927  64.072  1.00 17.21 ? 267 TYR A C   1 
ATOM   2268 O O   . TYR A 1 267 ? 10.530  1.986  63.880  1.00 16.27 ? 267 TYR A O   1 
ATOM   2269 C CB  . TYR A 1 267 ? 10.404  5.192  64.634  1.00 13.38 ? 267 TYR A CB  1 
ATOM   2270 C CG  . TYR A 1 267 ? 9.717   6.063  65.671  1.00 13.28 ? 267 TYR A CG  1 
ATOM   2271 C CD1 . TYR A 1 267 ? 8.608   5.593  66.376  1.00 16.55 ? 267 TYR A CD1 1 
ATOM   2272 C CD2 . TYR A 1 267 ? 10.154  7.364  65.921  1.00 13.62 ? 267 TYR A CD2 1 
ATOM   2273 C CE1 . TYR A 1 267 ? 7.957   6.388  67.331  1.00 16.59 ? 267 TYR A CE1 1 
ATOM   2274 C CE2 . TYR A 1 267 ? 9.507   8.178  66.882  1.00 13.20 ? 267 TYR A CE2 1 
ATOM   2275 C CZ  . TYR A 1 267 ? 8.413   7.679  67.578  1.00 18.49 ? 267 TYR A CZ  1 
ATOM   2276 O OH  . TYR A 1 267 ? 7.780   8.471  68.511  1.00 13.15 ? 267 TYR A OH  1 
ATOM   2277 N N   . TYR A 1 268 ? 12.394  3.119  63.315  1.00 15.50 ? 268 TYR A N   1 
ATOM   2278 C CA  . TYR A 1 268 ? 12.767  2.155  62.280  1.00 16.69 ? 268 TYR A CA  1 
ATOM   2279 C C   . TYR A 1 268 ? 13.002  0.767  62.867  1.00 18.18 ? 268 TYR A C   1 
ATOM   2280 O O   . TYR A 1 268 ? 12.523  -0.245 62.331  1.00 16.87 ? 268 TYR A O   1 
ATOM   2281 C CB  . TYR A 1 268 ? 14.021  2.642  61.558  1.00 20.24 ? 268 TYR A CB  1 
ATOM   2282 C CG  . TYR A 1 268 ? 14.716  1.533  60.827  1.00 18.72 ? 268 TYR A CG  1 
ATOM   2283 C CD1 . TYR A 1 268 ? 14.154  0.986  59.690  1.00 22.06 ? 268 TYR A CD1 1 
ATOM   2284 C CD2 . TYR A 1 268 ? 15.917  1.013  61.290  1.00 23.32 ? 268 TYR A CD2 1 
ATOM   2285 C CE1 . TYR A 1 268 ? 14.777  -0.030 59.019  1.00 26.67 ? 268 TYR A CE1 1 
ATOM   2286 C CE2 . TYR A 1 268 ? 16.548  -0.015 60.624  1.00 23.40 ? 268 TYR A CE2 1 
ATOM   2287 C CZ  . TYR A 1 268 ? 15.966  -0.530 59.493  1.00 27.53 ? 268 TYR A CZ  1 
ATOM   2288 O OH  . TYR A 1 268 ? 16.567  -1.553 58.817  1.00 31.62 ? 268 TYR A OH  1 
ATOM   2289 N N   . GLU A 1 269 ? 13.757  0.701  63.966  1.00 17.71 ? 269 GLU A N   1 
ATOM   2290 C CA  . GLU A 1 269 ? 14.078  -0.582 64.578  1.00 22.76 ? 269 GLU A CA  1 
ATOM   2291 C C   . GLU A 1 269 ? 12.832  -1.291 65.076  1.00 20.53 ? 269 GLU A C   1 
ATOM   2292 O O   . GLU A 1 269 ? 12.807  -2.525 65.144  1.00 23.16 ? 269 GLU A O   1 
ATOM   2293 C CB  . GLU A 1 269 ? 15.051  -0.378 65.739  1.00 24.72 ? 269 GLU A CB  1 
ATOM   2294 C CG  . GLU A 1 269 ? 16.453  0.036  65.314  1.00 28.35 ? 269 GLU A CG  1 
ATOM   2295 C CD  . GLU A 1 269 ? 17.324  0.426  66.496  1.00 38.40 ? 269 GLU A CD  1 
ATOM   2296 O OE1 . GLU A 1 269 ? 16.785  0.614  67.611  1.00 40.21 ? 269 GLU A OE1 1 
ATOM   2297 O OE2 . GLU A 1 269 ? 18.551  0.546  66.311  1.00 39.81 ? 269 GLU A OE2 1 
ATOM   2298 N N   . LYS A 1 270 ? 11.809  -0.531 65.459  1.00 18.26 ? 270 LYS A N   1 
ATOM   2299 C CA  . LYS A 1 270 ? 10.553  -1.091 65.929  1.00 18.19 ? 270 LYS A CA  1 
ATOM   2300 C C   . LYS A 1 270 ? 9.552   -1.330 64.805  1.00 22.87 ? 270 LYS A C   1 
ATOM   2301 O O   . LYS A 1 270 ? 8.375   -1.588 65.079  1.00 21.84 ? 270 LYS A O   1 
ATOM   2302 C CB  . LYS A 1 270 ? 9.960   -0.181 67.001  1.00 17.24 ? 270 LYS A CB  1 
ATOM   2303 C CG  . LYS A 1 270 ? 10.855  -0.099 68.227  1.00 17.28 ? 270 LYS A CG  1 
ATOM   2304 C CD  . LYS A 1 270 ? 10.904  -1.459 68.898  1.00 28.21 ? 270 LYS A CD  1 
ATOM   2305 C CE  . LYS A 1 270 ? 11.777  -1.453 70.133  1.00 41.30 ? 270 LYS A CE  1 
ATOM   2306 N NZ  . LYS A 1 270 ? 11.707  -2.766 70.836  1.00 49.03 ? 270 LYS A NZ  1 
ATOM   2307 N N   . GLY A 1 271 ? 9.982   -1.234 63.553  1.00 19.56 ? 271 GLY A N   1 
ATOM   2308 C CA  . GLY A 1 271 ? 9.139   -1.643 62.448  1.00 18.06 ? 271 GLY A CA  1 
ATOM   2309 C C   . GLY A 1 271 ? 8.154   -0.609 61.954  1.00 20.26 ? 271 GLY A C   1 
ATOM   2310 O O   . GLY A 1 271 ? 7.236   -0.965 61.204  1.00 23.51 ? 271 GLY A O   1 
ATOM   2311 N N   . ILE A 1 272 ? 8.318   0.655  62.337  1.00 16.25 ? 272 ILE A N   1 
ATOM   2312 C CA  . ILE A 1 272 ? 7.459   1.730  61.856  1.00 16.05 ? 272 ILE A CA  1 
ATOM   2313 C C   . ILE A 1 272 ? 7.920   2.131  60.461  1.00 21.49 ? 272 ILE A C   1 
ATOM   2314 O O   . ILE A 1 272 ? 9.112   2.359  60.240  1.00 22.97 ? 272 ILE A O   1 
ATOM   2315 C CB  . ILE A 1 272 ? 7.502   2.924  62.825  1.00 17.28 ? 272 ILE A CB  1 
ATOM   2316 C CG1 . ILE A 1 272 ? 7.123   2.464  64.243  1.00 18.74 ? 272 ILE A CG1 1 
ATOM   2317 C CG2 . ILE A 1 272 ? 6.635   4.065  62.324  1.00 17.81 ? 272 ILE A CG2 1 
ATOM   2318 C CD1 . ILE A 1 272 ? 5.850   1.635  64.313  1.00 21.95 ? 272 ILE A CD1 1 
ATOM   2319 N N   . ASN A 1 273 ? 6.978   2.217  59.512  1.00 20.02 ? 273 ASN A N   1 
ATOM   2320 C CA  . ASN A 1 273 ? 7.336   2.476  58.119  1.00 23.64 ? 273 ASN A CA  1 
ATOM   2321 C C   . ASN A 1 273 ? 7.246   3.945  57.746  1.00 24.65 ? 273 ASN A C   1 
ATOM   2322 O O   . ASN A 1 273 ? 7.957   4.393  56.836  1.00 21.58 ? 273 ASN A O   1 
ATOM   2323 C CB  . ASN A 1 273 ? 6.442   1.666  57.177  1.00 27.95 ? 273 ASN A CB  1 
ATOM   2324 C CG  . ASN A 1 273 ? 6.727   0.182  57.246  1.00 44.04 ? 273 ASN A CG  1 
ATOM   2325 O OD1 . ASN A 1 273 ? 7.882   -0.232 57.391  1.00 47.90 ? 273 ASN A OD1 1 
ATOM   2326 N ND2 . ASN A 1 273 ? 5.684   -0.629 57.136  1.00 47.07 ? 273 ASN A ND2 1 
ATOM   2327 N N   A MET A 1 274 ? 6.377   4.699  58.408  0.59 20.94 ? 274 MET A N   1 
ATOM   2328 N N   B MET A 1 274 ? 6.396   4.707  58.427  0.41 21.25 ? 274 MET A N   1 
ATOM   2329 C CA  A MET A 1 274 ? 6.230   6.113  58.103  0.59 20.51 ? 274 MET A CA  1 
ATOM   2330 C CA  B MET A 1 274 ? 6.201   6.107  58.095  0.41 20.80 ? 274 MET A CA  1 
ATOM   2331 C C   A MET A 1 274 ? 5.787   6.857  59.351  0.59 19.94 ? 274 MET A C   1 
ATOM   2332 C C   B MET A 1 274 ? 5.764   6.864  59.339  0.41 19.71 ? 274 MET A C   1 
ATOM   2333 O O   A MET A 1 274 ? 5.005   6.344  60.156  0.59 18.52 ? 274 MET A O   1 
ATOM   2334 O O   B MET A 1 274 ? 4.979   6.358  60.144  0.41 18.49 ? 274 MET A O   1 
ATOM   2335 C CB  A MET A 1 274 ? 5.224   6.345  56.967  0.59 22.97 ? 274 MET A CB  1 
ATOM   2336 C CB  B MET A 1 274 ? 5.158   6.266  56.977  0.41 22.67 ? 274 MET A CB  1 
ATOM   2337 C CG  A MET A 1 274 ? 5.076   7.808  56.573  0.59 22.58 ? 274 MET A CG  1 
ATOM   2338 C CG  B MET A 1 274 ? 4.938   7.693  56.516  0.41 22.97 ? 274 MET A CG  1 
ATOM   2339 S SD  A MET A 1 274 ? 3.823   8.662  57.555  0.59 22.90 ? 274 MET A SD  1 
ATOM   2340 S SD  B MET A 1 274 ? 3.495   7.843  55.444  0.41 24.78 ? 274 MET A SD  1 
ATOM   2341 C CE  A MET A 1 274 ? 2.339   8.175  56.669  0.59 22.22 ? 274 MET A CE  1 
ATOM   2342 C CE  B MET A 1 274 ? 2.207   8.176  56.643  0.41 22.23 ? 274 MET A CE  1 
ATOM   2343 N N   . LEU A 1 275 ? 6.287   8.074  59.498  1.00 12.28 ? 275 LEU A N   1 
ATOM   2344 C CA  . LEU A 1 275 ? 5.793   8.986  60.505  1.00 14.97 ? 275 LEU A CA  1 
ATOM   2345 C C   . LEU A 1 275 ? 5.723   10.351 59.856  1.00 16.28 ? 275 LEU A C   1 
ATOM   2346 O O   . LEU A 1 275 ? 6.150   10.540 58.712  1.00 17.15 ? 275 LEU A O   1 
ATOM   2347 C CB  . LEU A 1 275 ? 6.674   8.997  61.757  1.00 19.83 ? 275 LEU A CB  1 
ATOM   2348 C CG  . LEU A 1 275 ? 8.187   9.147  61.671  1.00 29.24 ? 275 LEU A CG  1 
ATOM   2349 C CD1 . LEU A 1 275 ? 8.600   10.617 61.563  1.00 34.30 ? 275 LEU A CD1 1 
ATOM   2350 C CD2 . LEU A 1 275 ? 8.812   8.507  62.908  1.00 27.17 ? 275 LEU A CD2 1 
ATOM   2351 N N   . ALA A 1 276 ? 5.149   11.296 60.577  1.00 14.28 ? 276 ALA A N   1 
ATOM   2352 C CA  . ALA A 1 276 ? 5.187   12.681 60.149  1.00 14.35 ? 276 ALA A CA  1 
ATOM   2353 C C   . ALA A 1 276 ? 5.752   13.527 61.276  1.00 16.46 ? 276 ALA A C   1 
ATOM   2354 O O   . ALA A 1 276 ? 5.796   13.111 62.438  1.00 13.91 ? 276 ALA A O   1 
ATOM   2355 C CB  . ALA A 1 276 ? 3.799   13.188 59.738  1.00 13.60 ? 276 ALA A CB  1 
ATOM   2356 N N   . THR A 1 277 ? 6.191   14.723 60.916  1.00 10.86 ? 277 THR A N   1 
ATOM   2357 C CA  . THR A 1 277 ? 6.682   15.685 61.908  1.00 12.05 ? 277 THR A CA  1 
ATOM   2358 C C   . THR A 1 277 ? 6.416   17.079 61.347  1.00 14.42 ? 277 THR A C   1 
ATOM   2359 O O   . THR A 1 277 ? 5.578   17.244 60.454  1.00 15.47 ? 277 THR A O   1 
ATOM   2360 C CB  . THR A 1 277 ? 8.155   15.395 62.272  1.00 16.43 ? 277 THR A CB  1 
ATOM   2361 O OG1 . THR A 1 277 ? 8.617   16.368 63.217  1.00 15.88 ? 277 THR A OG1 1 
ATOM   2362 C CG2 . THR A 1 277 ? 9.051   15.425 61.037  1.00 19.46 ? 277 THR A CG2 1 
ATOM   2363 N N   . ASP A 1 278 ? 7.079   18.096 61.894  1.00 12.46 ? 278 ASP A N   1 
ATOM   2364 C CA  . ASP A 1 278 ? 6.705   19.473 61.607  1.00 14.82 ? 278 ASP A CA  1 
ATOM   2365 C C   . ASP A 1 278 ? 7.612   20.142 60.572  1.00 15.46 ? 278 ASP A C   1 
ATOM   2366 O O   . ASP A 1 278 ? 8.802   19.835 60.447  1.00 16.82 ? 278 ASP A O   1 
ATOM   2367 C CB  . ASP A 1 278 ? 6.720   20.290 62.901  1.00 14.68 ? 278 ASP A CB  1 
ATOM   2368 C CG  . ASP A 1 278 ? 6.209   21.690 62.705  1.00 17.90 ? 278 ASP A CG  1 
ATOM   2369 O OD1 . ASP A 1 278 ? 5.096   21.842 62.160  1.00 17.28 ? 278 ASP A OD1 1 
ATOM   2370 O OD2 . ASP A 1 278 ? 6.894   22.644 63.135  1.00 20.20 ? 278 ASP A OD2 1 
ATOM   2371 N N   . GLU A 1 279 ? 7.025   21.101 59.849  1.00 12.72 ? 279 GLU A N   1 
ATOM   2372 C CA  . GLU A 1 279 ? 7.762   21.848 58.838  1.00 13.32 ? 279 GLU A CA  1 
ATOM   2373 C C   . GLU A 1 279 ? 8.929   22.643 59.429  1.00 14.86 ? 279 GLU A C   1 
ATOM   2374 O O   . GLU A 1 279 ? 9.945   22.841 58.747  1.00 18.38 ? 279 GLU A O   1 
ATOM   2375 C CB  . GLU A 1 279 ? 6.784   22.770 58.105  1.00 17.43 ? 279 GLU A CB  1 
ATOM   2376 C CG  . GLU A 1 279 ? 7.352   23.441 56.882  1.00 22.97 ? 279 GLU A CG  1 
ATOM   2377 C CD  . GLU A 1 279 ? 6.290   24.152 56.051  1.00 27.64 ? 279 GLU A CD  1 
ATOM   2378 O OE1 . GLU A 1 279 ? 5.089   24.140 56.422  1.00 19.87 ? 279 GLU A OE1 1 
ATOM   2379 O OE2 . GLU A 1 279 ? 6.665   24.742 55.018  1.00 26.07 ? 279 GLU A OE2 1 
ATOM   2380 N N   . VAL A 1 280 ? 8.817   23.116 60.679  1.00 15.55 ? 280 VAL A N   1 
ATOM   2381 C CA  . VAL A 1 280 ? 9.938   23.844 61.278  1.00 17.34 ? 280 VAL A CA  1 
ATOM   2382 C C   . VAL A 1 280 ? 11.163  22.940 61.380  1.00 19.49 ? 280 VAL A C   1 
ATOM   2383 O O   . VAL A 1 280 ? 12.299  23.372 61.136  1.00 20.35 ? 280 VAL A O   1 
ATOM   2384 C CB  . VAL A 1 280 ? 9.548   24.412 62.656  1.00 24.53 ? 280 VAL A CB  1 
ATOM   2385 C CG1 . VAL A 1 280 ? 10.787  24.928 63.384  1.00 23.73 ? 280 VAL A CG1 1 
ATOM   2386 C CG2 . VAL A 1 280 ? 8.498   25.523 62.512  1.00 23.40 ? 280 VAL A CG2 1 
ATOM   2387 N N   . ILE A 1 281 ? 10.949  21.671 61.749  1.00 18.46 ? 281 ILE A N   1 
ATOM   2388 C CA  . ILE A 1 281 ? 12.039  20.697 61.802  1.00 15.65 ? 281 ILE A CA  1 
ATOM   2389 C C   . ILE A 1 281 ? 12.703  20.565 60.436  1.00 19.81 ? 281 ILE A C   1 
ATOM   2390 O O   . ILE A 1 281 ? 13.938  20.517 60.329  1.00 18.01 ? 281 ILE A O   1 
ATOM   2391 C CB  . ILE A 1 281 ? 11.514  19.332 62.292  1.00 14.75 ? 281 ILE A CB  1 
ATOM   2392 C CG1 . ILE A 1 281 ? 10.804  19.462 63.646  1.00 26.72 ? 281 ILE A CG1 1 
ATOM   2393 C CG2 . ILE A 1 281 ? 12.636  18.298 62.334  1.00 18.14 ? 281 ILE A CG2 1 
ATOM   2394 C CD1 . ILE A 1 281 ? 11.649  20.027 64.735  1.00 32.13 ? 281 ILE A CD1 1 
ATOM   2395 N N   . LEU A 1 282 ? 11.895  20.495 59.374  1.00 15.65 ? 282 LEU A N   1 
ATOM   2396 C CA  . LEU A 1 282 ? 12.449  20.371 58.031  1.00 17.72 ? 282 LEU A CA  1 
ATOM   2397 C C   . LEU A 1 282 ? 13.294  21.583 57.688  1.00 16.10 ? 282 LEU A C   1 
ATOM   2398 O O   . LEU A 1 282 ? 14.413  21.458 57.168  1.00 16.12 ? 282 LEU A O   1 
ATOM   2399 C CB  . LEU A 1 282 ? 11.321  20.190 57.001  1.00 15.69 ? 282 LEU A CB  1 
ATOM   2400 C CG  . LEU A 1 282 ? 11.794  19.977 55.552  1.00 17.60 ? 282 LEU A CG  1 
ATOM   2401 C CD1 . LEU A 1 282 ? 12.684  18.745 55.399  1.00 17.93 ? 282 LEU A CD1 1 
ATOM   2402 C CD2 . LEU A 1 282 ? 10.615  19.915 54.560  1.00 17.36 ? 282 LEU A CD2 1 
ATOM   2403 N N   . LYS A 1 283 ? 12.768  22.775 57.972  1.00 15.44 ? 283 LYS A N   1 
ATOM   2404 C CA  . LYS A 1 283 ? 13.515  23.995 57.682  1.00 18.44 ? 283 LYS A CA  1 
ATOM   2405 C C   . LYS A 1 283 ? 14.815  24.054 58.476  1.00 17.82 ? 283 LYS A C   1 
ATOM   2406 O O   . LYS A 1 283 ? 15.831  24.556 57.973  1.00 18.34 ? 283 LYS A O   1 
ATOM   2407 C CB  . LYS A 1 283 ? 12.647  25.224 57.973  1.00 18.98 ? 283 LYS A CB  1 
ATOM   2408 C CG  . LYS A 1 283 ? 11.449  25.392 57.022  1.00 29.15 ? 283 LYS A CG  1 
ATOM   2409 C CD  . LYS A 1 283 ? 10.442  26.411 57.559  1.00 38.39 ? 283 LYS A CD  1 
ATOM   2410 C CE  . LYS A 1 283 ? 10.926  27.838 57.391  1.00 48.56 ? 283 LYS A CE  1 
ATOM   2411 N NZ  . LYS A 1 283 ? 10.847  28.285 55.974  1.00 55.05 ? 283 LYS A NZ  1 
ATOM   2412 N N   . ASN A 1 284 ? 14.810  23.539 59.703  1.00 16.34 ? 284 ASN A N   1 
ATOM   2413 C CA  . ASN A 1 284 ? 16.019  23.516 60.519  1.00 17.00 ? 284 ASN A CA  1 
ATOM   2414 C C   . ASN A 1 284 ? 17.021  22.469 60.064  1.00 22.13 ? 284 ASN A C   1 
ATOM   2415 O O   . ASN A 1 284 ? 18.183  22.532 60.477  1.00 22.50 ? 284 ASN A O   1 
ATOM   2416 C CB  . ASN A 1 284 ? 15.688  23.246 61.990  1.00 18.02 ? 284 ASN A CB  1 
ATOM   2417 C CG  . ASN A 1 284 ? 14.994  24.405 62.660  1.00 24.37 ? 284 ASN A CG  1 
ATOM   2418 O OD1 . ASN A 1 284 ? 15.012  25.528 62.153  1.00 20.86 ? 284 ASN A OD1 1 
ATOM   2419 N ND2 . ASN A 1 284 ? 14.432  24.156 63.846  1.00 22.09 ? 284 ASN A ND2 1 
ATOM   2420 N N   . SER A 1 285 ? 16.603  21.521 59.224  1.00 19.14 ? 285 SER A N   1 
ATOM   2421 C CA  . SER A 1 285 ? 17.400  20.343 58.904  1.00 19.47 ? 285 SER A CA  1 
ATOM   2422 C C   . SER A 1 285 ? 17.925  20.316 57.480  1.00 25.76 ? 285 SER A C   1 
ATOM   2423 O O   . SER A 1 285 ? 18.957  19.687 57.236  1.00 27.33 ? 285 SER A O   1 
ATOM   2424 C CB  . SER A 1 285 ? 16.571  19.069 59.131  1.00 24.00 ? 285 SER A CB  1 
ATOM   2425 O OG  . SER A 1 285 ? 16.102  18.987 60.469  1.00 22.66 ? 285 SER A OG  1 
ATOM   2426 N N   . VAL A 1 286 ? 17.238  20.949 56.524  1.00 22.25 ? 286 VAL A N   1 
ATOM   2427 C CA  . VAL A 1 286 ? 17.686  20.946 55.132  1.00 22.46 ? 286 VAL A CA  1 
ATOM   2428 C C   . VAL A 1 286 ? 17.554  22.346 54.556  1.00 22.30 ? 286 VAL A C   1 
ATOM   2429 O O   . VAL A 1 286 ? 16.832  23.194 55.080  1.00 23.37 ? 286 VAL A O   1 
ATOM   2430 C CB  . VAL A 1 286 ? 16.905  19.959 54.234  1.00 25.37 ? 286 VAL A CB  1 
ATOM   2431 C CG1 . VAL A 1 286 ? 16.874  18.553 54.844  1.00 23.91 ? 286 VAL A CG1 1 
ATOM   2432 C CG2 . VAL A 1 286 ? 15.498  20.477 53.961  1.00 25.81 ? 286 VAL A CG2 1 
ATOM   2433 N N   . GLU A 1 287 ? 18.240  22.570 53.432  1.00 23.90 ? 287 GLU A N   1 
ATOM   2434 C CA  . GLU A 1 287 ? 18.181  23.879 52.793  1.00 24.55 ? 287 GLU A CA  1 
ATOM   2435 C C   . GLU A 1 287 ? 16.873  24.073 52.031  1.00 25.19 ? 287 GLU A C   1 
ATOM   2436 O O   . GLU A 1 287 ? 16.131  25.028 52.291  1.00 27.69 ? 287 GLU A O   1 
ATOM   2437 C CB  . GLU A 1 287 ? 19.389  24.059 51.870  1.00 26.87 ? 287 GLU A CB  1 
ATOM   2438 C CG  . GLU A 1 287 ? 20.707  23.978 52.615  1.00 28.40 ? 287 GLU A CG  1 
ATOM   2439 C CD  . GLU A 1 287 ? 21.870  24.384 51.743  1.00 39.90 ? 287 GLU A CD  1 
ATOM   2440 O OE1 . GLU A 1 287 ? 21.622  24.740 50.571  1.00 38.11 ? 287 GLU A OE1 1 
ATOM   2441 O OE2 . GLU A 1 287 ? 23.019  24.346 52.229  1.00 47.21 ? 287 GLU A OE2 1 
ATOM   2442 N N   . ARG A 1 288 ? 16.560  23.165 51.102  1.00 21.20 ? 288 ARG A N   1 
ATOM   2443 C CA  . ARG A 1 288 ? 15.383  23.297 50.235  1.00 21.66 ? 288 ARG A CA  1 
ATOM   2444 C C   . ARG A 1 288 ? 14.236  22.534 50.891  1.00 20.83 ? 288 ARG A C   1 
ATOM   2445 O O   . ARG A 1 288 ? 14.031  21.342 50.655  1.00 25.63 ? 288 ARG A O   1 
ATOM   2446 C CB  . ARG A 1 288 ? 15.696  22.787 48.832  1.00 23.55 ? 288 ARG A CB  1 
ATOM   2447 C CG  . ARG A 1 288 ? 16.848  23.543 48.159  1.00 23.54 ? 288 ARG A CG  1 
ATOM   2448 C CD  . ARG A 1 288 ? 17.277  22.882 46.848  1.00 30.46 ? 288 ARG A CD  1 
ATOM   2449 N NE  . ARG A 1 288 ? 17.837  21.551 47.086  1.00 33.16 ? 288 ARG A NE  1 
ATOM   2450 C CZ  . ARG A 1 288 ? 17.181  20.415 46.857  1.00 33.19 ? 288 ARG A CZ  1 
ATOM   2451 N NH1 . ARG A 1 288 ? 17.746  19.241 47.115  1.00 34.66 ? 288 ARG A NH1 1 
ATOM   2452 N NH2 . ARG A 1 288 ? 15.949  20.458 46.377  1.00 35.61 ? 288 ARG A NH2 1 
ATOM   2453 N N   . ALA A 1 289 ? 13.484  23.229 51.736  1.00 17.93 ? 289 ALA A N   1 
ATOM   2454 C CA  . ALA A 1 289 ? 12.610  22.576 52.710  1.00 21.67 ? 289 ALA A CA  1 
ATOM   2455 C C   . ALA A 1 289 ? 11.159  22.524 52.228  1.00 25.14 ? 289 ALA A C   1 
ATOM   2456 O O   . ALA A 1 289 ? 10.253  23.027 52.895  1.00 24.73 ? 289 ALA A O   1 
ATOM   2457 C CB  . ALA A 1 289 ? 12.713  23.295 54.056  1.00 20.58 ? 289 ALA A CB  1 
ATOM   2458 N N   . SER A 1 290 ? 10.911  21.857 51.095  1.00 21.21 ? 290 SER A N   1 
ATOM   2459 C CA  . SER A 1 290 ? 9.520   21.749 50.629  1.00 23.39 ? 290 SER A CA  1 
ATOM   2460 C C   . SER A 1 290 ? 8.781   20.638 51.369  1.00 20.88 ? 290 SER A C   1 
ATOM   2461 O O   . SER A 1 290 ? 9.228   19.486 51.359  1.00 18.24 ? 290 SER A O   1 
ATOM   2462 C CB  . SER A 1 290 ? 9.429   21.477 49.136  1.00 18.57 ? 290 SER A CB  1 
ATOM   2463 O OG  . SER A 1 290 ? 8.058   21.330 48.778  1.00 17.65 ? 290 SER A OG  1 
ATOM   2464 N N   . PRO A 1 291 ? 7.631   20.931 51.980  1.00 16.71 ? 291 PRO A N   1 
ATOM   2465 C CA  . PRO A 1 291 ? 6.860   19.885 52.655  1.00 17.34 ? 291 PRO A CA  1 
ATOM   2466 C C   . PRO A 1 291 ? 5.992   19.042 51.726  1.00 19.13 ? 291 PRO A C   1 
ATOM   2467 O O   . PRO A 1 291 ? 5.249   18.191 52.221  1.00 20.29 ? 291 PRO A O   1 
ATOM   2468 C CB  . PRO A 1 291 ? 5.995   20.695 53.628  1.00 16.97 ? 291 PRO A CB  1 
ATOM   2469 C CG  . PRO A 1 291 ? 5.718   21.965 52.883  1.00 20.60 ? 291 PRO A CG  1 
ATOM   2470 C CD  . PRO A 1 291 ? 6.985   22.252 52.080  1.00 18.93 ? 291 PRO A CD  1 
ATOM   2471 N N   . TYR A 1 292 ? 6.051   19.235 50.409  1.00 16.48 ? 292 TYR A N   1 
ATOM   2472 C CA  . TYR A 1 292 ? 5.113   18.580 49.499  1.00 17.80 ? 292 TYR A CA  1 
ATOM   2473 C C   . TYR A 1 292 ? 5.661   17.278 48.927  1.00 17.54 ? 292 TYR A C   1 
ATOM   2474 O O   . TYR A 1 292 ? 5.036   16.701 48.034  1.00 17.84 ? 292 TYR A O   1 
ATOM   2475 C CB  . TYR A 1 292 ? 4.712   19.562 48.377  1.00 18.90 ? 292 TYR A CB  1 
ATOM   2476 C CG  . TYR A 1 292 ? 4.067   20.796 48.982  1.00 19.01 ? 292 TYR A CG  1 
ATOM   2477 C CD1 . TYR A 1 292 ? 3.199   20.676 50.056  1.00 22.30 ? 292 TYR A CD1 1 
ATOM   2478 C CD2 . TYR A 1 292 ? 4.415   22.074 48.562  1.00 26.81 ? 292 TYR A CD2 1 
ATOM   2479 C CE1 . TYR A 1 292 ? 2.654   21.790 50.667  1.00 25.52 ? 292 TYR A CE1 1 
ATOM   2480 C CE2 . TYR A 1 292 ? 3.866   23.196 49.164  1.00 26.45 ? 292 TYR A CE2 1 
ATOM   2481 C CZ  . TYR A 1 292 ? 2.989   23.045 50.217  1.00 27.85 ? 292 TYR A CZ  1 
ATOM   2482 O OH  . TYR A 1 292 ? 2.441   24.146 50.840  1.00 26.68 ? 292 TYR A OH  1 
ATOM   2483 N N   . LEU A 1 293 ? 6.794   16.801 49.445  1.00 16.73 ? 293 LEU A N   1 
ATOM   2484 C CA  . LEU A 1 293 ? 7.483   15.595 49.004  1.00 19.03 ? 293 LEU A CA  1 
ATOM   2485 C C   . LEU A 1 293 ? 7.412   14.537 50.095  1.00 17.89 ? 293 LEU A C   1 
ATOM   2486 O O   . LEU A 1 293 ? 7.310   14.869 51.276  1.00 21.89 ? 293 LEU A O   1 
ATOM   2487 C CB  . LEU A 1 293 ? 8.967   15.877 48.715  1.00 23.30 ? 293 LEU A CB  1 
ATOM   2488 C CG  . LEU A 1 293 ? 9.413   16.557 47.415  1.00 31.96 ? 293 LEU A CG  1 
ATOM   2489 C CD1 . LEU A 1 293 ? 8.916   17.972 47.368  1.00 29.71 ? 293 LEU A CD1 1 
ATOM   2490 C CD2 . LEU A 1 293 ? 10.932  16.535 47.307  1.00 38.11 ? 293 LEU A CD2 1 
ATOM   2491 N N   . ARG A 1 294 ? 7.506   13.263 49.697  1.00 19.61 ? 294 ARG A N   1 
ATOM   2492 C CA  . ARG A 1 294 ? 7.757   12.176 50.644  1.00 21.16 ? 294 ARG A CA  1 
ATOM   2493 C C   . ARG A 1 294 ? 9.263   12.076 50.892  1.00 20.33 ? 294 ARG A C   1 
ATOM   2494 O O   . ARG A 1 294 ? 10.036  11.922 49.941  1.00 22.19 ? 294 ARG A O   1 
ATOM   2495 C CB  . ARG A 1 294 ? 7.216   10.847 50.102  1.00 17.99 ? 294 ARG A CB  1 
ATOM   2496 C CG  . ARG A 1 294 ? 7.345   9.678  51.094  1.00 18.28 ? 294 ARG A CG  1 
ATOM   2497 C CD  . ARG A 1 294 ? 6.549   8.443  50.638  1.00 19.40 ? 294 ARG A CD  1 
ATOM   2498 N NE  . ARG A 1 294 ? 6.991   7.963  49.340  1.00 26.09 ? 294 ARG A NE  1 
ATOM   2499 C CZ  . ARG A 1 294 ? 6.199   7.761  48.291  1.00 28.63 ? 294 ARG A CZ  1 
ATOM   2500 N NH1 . ARG A 1 294 ? 4.885   7.956  48.376  1.00 24.87 ? 294 ARG A NH1 1 
ATOM   2501 N NH2 . ARG A 1 294 ? 6.726   7.339  47.151  1.00 32.59 ? 294 ARG A NH2 1 
ATOM   2502 N N   . TYR A 1 295 ? 9.690   12.173 52.150  1.00 20.35 ? 295 TYR A N   1 
ATOM   2503 C CA  . TYR A 1 295 ? 11.107  12.082 52.464  1.00 21.50 ? 295 TYR A CA  1 
ATOM   2504 C C   . TYR A 1 295 ? 11.451  10.689 52.974  1.00 21.30 ? 295 TYR A C   1 
ATOM   2505 O O   . TYR A 1 295 ? 10.626  10.012 53.589  1.00 20.17 ? 295 TYR A O   1 
ATOM   2506 C CB  . TYR A 1 295 ? 11.534  13.136 53.497  1.00 15.76 ? 295 TYR A CB  1 
ATOM   2507 C CG  . TYR A 1 295 ? 11.530  14.545 52.940  1.00 16.58 ? 295 TYR A CG  1 
ATOM   2508 C CD1 . TYR A 1 295 ? 10.347  15.265 52.779  1.00 17.64 ? 295 TYR A CD1 1 
ATOM   2509 C CD2 . TYR A 1 295 ? 12.706  15.128 52.495  1.00 19.59 ? 295 TYR A CD2 1 
ATOM   2510 C CE1 . TYR A 1 295 ? 10.357  16.558 52.250  1.00 18.84 ? 295 TYR A CE1 1 
ATOM   2511 C CE2 . TYR A 1 295 ? 12.725  16.397 51.960  1.00 22.79 ? 295 TYR A CE2 1 
ATOM   2512 C CZ  . TYR A 1 295 ? 11.552  17.110 51.823  1.00 22.49 ? 295 TYR A CZ  1 
ATOM   2513 O OH  . TYR A 1 295 ? 11.593  18.384 51.284  1.00 24.27 ? 295 TYR A OH  1 
ATOM   2514 N N   . TYR A 1 296 ? 12.673  10.255 52.682  1.00 22.34 ? 296 TYR A N   1 
ATOM   2515 C CA  . TYR A 1 296 ? 13.189  8.992  53.188  1.00 20.90 ? 296 TYR A CA  1 
ATOM   2516 C C   . TYR A 1 296 ? 14.384  9.316  54.074  1.00 18.79 ? 296 TYR A C   1 
ATOM   2517 O O   . TYR A 1 296 ? 15.411  9.790  53.585  1.00 21.72 ? 296 TYR A O   1 
ATOM   2518 C CB  . TYR A 1 296 ? 13.586  8.043  52.053  1.00 20.96 ? 296 TYR A CB  1 
ATOM   2519 C CG  . TYR A 1 296 ? 12.484  7.746  51.050  1.00 24.60 ? 296 TYR A CG  1 
ATOM   2520 C CD1 . TYR A 1 296 ? 11.308  7.119  51.442  1.00 29.50 ? 296 TYR A CD1 1 
ATOM   2521 C CD2 . TYR A 1 296 ? 12.636  8.064  49.706  1.00 31.53 ? 296 TYR A CD2 1 
ATOM   2522 C CE1 . TYR A 1 296 ? 10.303  6.838  50.531  1.00 30.55 ? 296 TYR A CE1 1 
ATOM   2523 C CE2 . TYR A 1 296 ? 11.632  7.782  48.779  1.00 35.50 ? 296 TYR A CE2 1 
ATOM   2524 C CZ  . TYR A 1 296 ? 10.468  7.172  49.208  1.00 29.51 ? 296 TYR A CZ  1 
ATOM   2525 O OH  . TYR A 1 296 ? 9.471   6.891  48.302  1.00 29.82 ? 296 TYR A OH  1 
ATOM   2526 N N   . PHE A 1 297 ? 14.248  9.079  55.376  1.00 20.48 ? 297 PHE A N   1 
ATOM   2527 C CA  . PHE A 1 297 ? 15.352  9.313  56.300  1.00 16.91 ? 297 PHE A CA  1 
ATOM   2528 C C   . PHE A 1 297 ? 16.333  8.159  56.181  1.00 18.12 ? 297 PHE A C   1 
ATOM   2529 O O   . PHE A 1 297 ? 16.051  7.045  56.638  1.00 19.14 ? 297 PHE A O   1 
ATOM   2530 C CB  . PHE A 1 297 ? 14.850  9.459  57.731  1.00 16.67 ? 297 PHE A CB  1 
ATOM   2531 C CG  . PHE A 1 297 ? 15.946  9.683  58.736  1.00 17.62 ? 297 PHE A CG  1 
ATOM   2532 C CD1 . PHE A 1 297 ? 16.541  10.931 58.869  1.00 18.96 ? 297 PHE A CD1 1 
ATOM   2533 C CD2 . PHE A 1 297 ? 16.368  8.648  59.556  1.00 20.65 ? 297 PHE A CD2 1 
ATOM   2534 C CE1 . PHE A 1 297 ? 17.535  11.143 59.810  1.00 21.36 ? 297 PHE A CE1 1 
ATOM   2535 C CE2 . PHE A 1 297 ? 17.366  8.854  60.498  1.00 18.37 ? 297 PHE A CE2 1 
ATOM   2536 C CZ  . PHE A 1 297 ? 17.952  10.094 60.621  1.00 19.18 ? 297 PHE A CZ  1 
ATOM   2537 N N   . ARG A 1 298 ? 17.475  8.431  55.551  1.00 19.27 ? 298 ARG A N   1 
ATOM   2538 C CA  . ARG A 1 298 ? 18.567  7.471  55.409  1.00 28.36 ? 298 ARG A CA  1 
ATOM   2539 C C   . ARG A 1 298 ? 18.118  6.175  54.739  1.00 22.80 ? 298 ARG A C   1 
ATOM   2540 O O   . ARG A 1 298 ? 18.672  5.113  55.014  1.00 27.19 ? 298 ARG A O   1 
ATOM   2541 C CB  . ARG A 1 298 ? 19.210  7.161  56.764  1.00 25.30 ? 298 ARG A CB  1 
ATOM   2542 C CG  . ARG A 1 298 ? 19.860  8.356  57.411  1.00 23.55 ? 298 ARG A CG  1 
ATOM   2543 C CD  . ARG A 1 298 ? 20.447  8.013  58.756  1.00 24.92 ? 298 ARG A CD  1 
ATOM   2544 N NE  . ARG A 1 298 ? 20.965  9.208  59.398  1.00 30.45 ? 298 ARG A NE  1 
ATOM   2545 C CZ  . ARG A 1 298 ? 21.354  9.274  60.667  1.00 39.68 ? 298 ARG A CZ  1 
ATOM   2546 N NH1 . ARG A 1 298 ? 21.280  8.200  61.445  1.00 41.98 ? 298 ARG A NH1 1 
ATOM   2547 N NH2 . ARG A 1 298 ? 21.811  10.423 61.160  1.00 39.00 ? 298 ARG A NH2 1 
ATOM   2548 N N   . GLU A 1 299 ? 17.112  6.246  53.865  1.00 25.89 ? 299 GLU A N   1 
ATOM   2549 C CA  . GLU A 1 299 ? 16.507  5.075  53.223  1.00 27.35 ? 299 GLU A CA  1 
ATOM   2550 C C   . GLU A 1 299 ? 15.948  4.063  54.234  1.00 29.88 ? 299 GLU A C   1 
ATOM   2551 O O   . GLU A 1 299 ? 15.747  2.891  53.896  1.00 27.94 ? 299 GLU A O   1 
ATOM   2552 C CB  . GLU A 1 299 ? 17.506  4.372  52.294  1.00 32.50 ? 299 GLU A CB  1 
ATOM   2553 C CG  . GLU A 1 299 ? 18.141  5.220  51.189  1.00 39.32 ? 299 GLU A CG  1 
ATOM   2554 C CD  . GLU A 1 299 ? 17.154  5.747  50.165  1.00 53.10 ? 299 GLU A CD  1 
ATOM   2555 O OE1 . GLU A 1 299 ? 15.958  5.381  50.214  1.00 54.67 ? 299 GLU A OE1 1 
ATOM   2556 O OE2 . GLU A 1 299 ? 17.601  6.484  49.260  1.00 56.91 ? 299 GLU A OE2 1 
ATOM   2557 N N   . LEU A 1 300 ? 15.693  4.488  55.475  1.00 25.79 ? 300 LEU A N   1 
ATOM   2558 C CA  . LEU A 1 300 ? 15.205  3.604  56.528  1.00 24.11 ? 300 LEU A CA  1 
ATOM   2559 C C   . LEU A 1 300 ? 13.706  3.731  56.751  1.00 23.83 ? 300 LEU A C   1 
ATOM   2560 O O   . LEU A 1 300 ? 13.004  2.720  56.854  1.00 24.35 ? 300 LEU A O   1 
ATOM   2561 C CB  . LEU A 1 300 ? 15.920  3.894  57.859  1.00 23.94 ? 300 LEU A CB  1 
ATOM   2562 C CG  . LEU A 1 300 ? 17.432  3.672  57.884  1.00 27.16 ? 300 LEU A CG  1 
ATOM   2563 C CD1 . LEU A 1 300 ? 18.013  4.015  59.233  1.00 21.54 ? 300 LEU A CD1 1 
ATOM   2564 C CD2 . LEU A 1 300 ? 17.744  2.244  57.516  1.00 25.19 ? 300 LEU A CD2 1 
ATOM   2565 N N   . ILE A 1 301 ? 13.209  4.959  56.846  1.00 20.59 ? 301 ILE A N   1 
ATOM   2566 C CA  . ILE A 1 301 ? 11.837  5.217  57.267  1.00 21.05 ? 301 ILE A CA  1 
ATOM   2567 C C   . ILE A 1 301 ? 11.342  6.437  56.499  1.00 23.30 ? 301 ILE A C   1 
ATOM   2568 O O   . ILE A 1 301 ? 12.108  7.369  56.235  1.00 24.32 ? 301 ILE A O   1 
ATOM   2569 C CB  . ILE A 1 301 ? 11.768  5.394  58.801  1.00 18.67 ? 301 ILE A CB  1 
ATOM   2570 C CG1 . ILE A 1 301 ? 10.334  5.585  59.306  1.00 16.71 ? 301 ILE A CG1 1 
ATOM   2571 C CG2 . ILE A 1 301 ? 12.670  6.554  59.270  1.00 25.50 ? 301 ILE A CG2 1 
ATOM   2572 C CD1 . ILE A 1 301 ? 10.251  5.574  60.827  1.00 15.43 ? 301 ILE A CD1 1 
ATOM   2573 N N   . SER A 1 302 ? 10.081  6.389  56.067  1.00 24.17 ? 302 SER A N   1 
ATOM   2574 C CA  . SER A 1 302 ? 9.483   7.501  55.337  1.00 17.92 ? 302 SER A CA  1 
ATOM   2575 C C   . SER A 1 302 ? 9.013   8.567  56.314  1.00 18.31 ? 302 SER A C   1 
ATOM   2576 O O   . SER A 1 302 ? 8.517   8.259  57.399  1.00 19.60 ? 302 SER A O   1 
ATOM   2577 C CB  . SER A 1 302 ? 8.312   7.013  54.481  1.00 20.91 ? 302 SER A CB  1 
ATOM   2578 O OG  . SER A 1 302 ? 8.785   6.132  53.476  1.00 24.78 ? 302 SER A OG  1 
ATOM   2579 N N   . VAL A 1 303 ? 9.188   9.828  55.930  1.00 22.08 ? 303 VAL A N   1 
ATOM   2580 C CA  . VAL A 1 303 ? 8.817   10.957 56.772  1.00 20.43 ? 303 VAL A CA  1 
ATOM   2581 C C   . VAL A 1 303 ? 8.077   11.975 55.917  1.00 20.13 ? 303 VAL A C   1 
ATOM   2582 O O   . VAL A 1 303 ? 8.589   12.409 54.881  1.00 20.38 ? 303 VAL A O   1 
ATOM   2583 C CB  . VAL A 1 303 ? 10.047  11.615 57.428  1.00 20.04 ? 303 VAL A CB  1 
ATOM   2584 C CG1 . VAL A 1 303 ? 9.596   12.767 58.339  1.00 18.20 ? 303 VAL A CG1 1 
ATOM   2585 C CG2 . VAL A 1 303 ? 10.854  10.589 58.219  1.00 18.86 ? 303 VAL A CG2 1 
ATOM   2586 N N   . PHE A 1 304 ? 6.882   12.359 56.342  1.00 17.02 ? 304 PHE A N   1 
ATOM   2587 C CA  . PHE A 1 304 ? 6.224   13.517 55.765  1.00 17.95 ? 304 PHE A CA  1 
ATOM   2588 C C   . PHE A 1 304 ? 6.331   14.678 56.743  1.00 17.56 ? 304 PHE A C   1 
ATOM   2589 O O   . PHE A 1 304 ? 6.277   14.493 57.964  1.00 17.88 ? 304 PHE A O   1 
ATOM   2590 C CB  . PHE A 1 304 ? 4.756   13.231 55.439  1.00 15.61 ? 304 PHE A CB  1 
ATOM   2591 C CG  . PHE A 1 304 ? 4.555   12.396 54.200  1.00 16.76 ? 304 PHE A CG  1 
ATOM   2592 C CD1 . PHE A 1 304 ? 4.606   12.974 52.943  1.00 17.98 ? 304 PHE A CD1 1 
ATOM   2593 C CD2 . PHE A 1 304 ? 4.301   11.034 54.296  1.00 19.02 ? 304 PHE A CD2 1 
ATOM   2594 C CE1 . PHE A 1 304 ? 4.411   12.222 51.796  1.00 21.12 ? 304 PHE A CE1 1 
ATOM   2595 C CE2 . PHE A 1 304 ? 4.110   10.280 53.146  1.00 18.11 ? 304 PHE A CE2 1 
ATOM   2596 C CZ  . PHE A 1 304 ? 4.169   10.872 51.902  1.00 19.40 ? 304 PHE A CZ  1 
ATOM   2597 N N   . PHE A 1 305 ? 6.490   15.875 56.205  1.00 13.97 ? 305 PHE A N   1 
ATOM   2598 C CA  . PHE A 1 305 ? 6.500   17.080 57.013  1.00 17.64 ? 305 PHE A CA  1 
ATOM   2599 C C   . PHE A 1 305 ? 5.182   17.802 56.784  1.00 15.24 ? 305 PHE A C   1 
ATOM   2600 O O   . PHE A 1 305 ? 4.826   18.112 55.642  1.00 14.22 ? 305 PHE A O   1 
ATOM   2601 C CB  . PHE A 1 305 ? 7.707   17.943 56.661  1.00 15.63 ? 305 PHE A CB  1 
ATOM   2602 C CG  . PHE A 1 305 ? 9.019   17.324 57.076  1.00 13.28 ? 305 PHE A CG  1 
ATOM   2603 C CD1 . PHE A 1 305 ? 9.689   16.389 56.277  1.00 17.42 ? 305 PHE A CD1 1 
ATOM   2604 C CD2 . PHE A 1 305 ? 9.548   17.632 58.316  1.00 17.06 ? 305 PHE A CD2 1 
ATOM   2605 C CE1 . PHE A 1 305 ? 10.899  15.822 56.734  1.00 21.34 ? 305 PHE A CE1 1 
ATOM   2606 C CE2 . PHE A 1 305 ? 10.724  17.087 58.753  1.00 26.09 ? 305 PHE A CE2 1 
ATOM   2607 C CZ  . PHE A 1 305 ? 11.395  16.182 57.981  1.00 19.64 ? 305 PHE A CZ  1 
ATOM   2608 N N   . ARG A 1 306 ? 4.436   18.024 57.835  1.00 11.73 ? 306 ARG A N   1 
ATOM   2609 C CA  . ARG A 1 306 ? 3.169   18.637 57.658  1.00 15.89 ? 306 ARG A CA  1 
ATOM   2610 C C   . ARG A 1 306 ? 3.265   20.036 57.106  1.00 16.22 ? 306 ARG A C   1 
ATOM   2611 O O   . ARG A 1 306 ? 4.224   20.689 57.323  1.00 16.91 ? 306 ARG A O   1 
ATOM   2612 C CB  . ARG A 1 306 ? 2.375   18.712 58.983  1.00 18.96 ? 306 ARG A CB  1 
ATOM   2613 C CG  . ARG A 1 306 ? 2.869   19.743 59.957  1.00 25.34 ? 306 ARG A CG  1 
ATOM   2614 C CD  . ARG A 1 306 ? 2.002   19.899 61.191  1.00 29.19 ? 306 ARG A CD  1 
ATOM   2615 N NE  . ARG A 1 306 ? 2.499   20.965 62.047  1.00 24.85 ? 306 ARG A NE  1 
ATOM   2616 C CZ  . ARG A 1 306 ? 1.793   21.584 62.953  1.00 30.43 ? 306 ARG A CZ  1 
ATOM   2617 N NH1 . ARG A 1 306 ? 0.579   21.204 63.186  1.00 28.64 ? 306 ARG A NH1 1 
ATOM   2618 N NH2 . ARG A 1 306 ? 2.329   22.570 63.645  1.00 43.91 ? 306 ARG A NH2 1 
ATOM   2619 N N   . ASP A 1 307 ? 2.245   20.466 56.387  1.00 18.65 ? 307 ASP A N   1 
ATOM   2620 C CA  . ASP A 1 307 ? 2.133   21.870 56.001  1.00 16.15 ? 307 ASP A CA  1 
ATOM   2621 C C   . ASP A 1 307 ? 1.676   22.639 57.230  1.00 15.25 ? 307 ASP A C   1 
ATOM   2622 O O   . ASP A 1 307 ? 0.514   22.544 57.641  1.00 15.81 ? 307 ASP A O   1 
ATOM   2623 C CB  . ASP A 1 307 ? 1.167   22.024 54.828  1.00 16.68 ? 307 ASP A CB  1 
ATOM   2624 C CG  . ASP A 1 307 ? 1.058   23.465 54.324  1.00 20.85 ? 307 ASP A CG  1 
ATOM   2625 O OD1 . ASP A 1 307 ? 1.129   24.421 55.126  1.00 21.88 ? 307 ASP A OD1 1 
ATOM   2626 O OD2 . ASP A 1 307 ? 0.941   23.637 53.094  1.00 24.25 ? 307 ASP A OD2 1 
ATOM   2627 N N   . LYS A 1 308 ? 2.604   23.373 57.846  1.00 15.76 ? 308 LYS A N   1 
ATOM   2628 C CA  . LYS A 1 308 ? 2.316   24.019 59.123  1.00 14.18 ? 308 LYS A CA  1 
ATOM   2629 C C   . LYS A 1 308 ? 1.288   25.133 58.975  1.00 15.06 ? 308 LYS A C   1 
ATOM   2630 O O   . LYS A 1 308 ? 0.428   25.307 59.847  1.00 14.13 ? 308 LYS A O   1 
ATOM   2631 C CB  . LYS A 1 308 ? 3.612   24.559 59.735  1.00 14.23 ? 308 LYS A CB  1 
ATOM   2632 C CG  . LYS A 1 308 ? 3.435   25.332 61.029  1.00 14.95 ? 308 LYS A CG  1 
ATOM   2633 C CD  . LYS A 1 308 ? 4.670   26.192 61.343  1.00 21.48 ? 308 LYS A CD  1 
ATOM   2634 C CE  . LYS A 1 308 ? 4.781   26.505 62.815  1.00 27.83 ? 308 LYS A CE  1 
ATOM   2635 N NZ  . LYS A 1 308 ? 3.511   26.879 63.488  1.00 28.14 ? 308 LYS A NZ  1 
ATOM   2636 N N   . THR A 1 309 ? 1.365   25.901 57.887  1.00 13.65 ? 309 THR A N   1 
ATOM   2637 C CA  . THR A 1 309 ? 0.414   26.988 57.673  1.00 15.34 ? 309 THR A CA  1 
ATOM   2638 C C   . THR A 1 309 ? -1.018  26.475 57.637  1.00 17.73 ? 309 THR A C   1 
ATOM   2639 O O   . THR A 1 309 ? -1.898  27.005 58.327  1.00 17.17 ? 309 THR A O   1 
ATOM   2640 C CB  . THR A 1 309 ? 0.750   27.711 56.377  1.00 24.35 ? 309 THR A CB  1 
ATOM   2641 O OG1 . THR A 1 309 ? 2.069   28.243 56.490  1.00 21.69 ? 309 THR A OG1 1 
ATOM   2642 C CG2 . THR A 1 309 ? -0.243  28.845 56.103  1.00 23.79 ? 309 THR A CG2 1 
ATOM   2643 N N   . LEU A 1 310 ? -1.278  25.463 56.805  1.00 15.34 ? 310 LEU A N   1 
ATOM   2644 C CA  . LEU A 1 310 ? -2.633  24.940 56.694  1.00 15.30 ? 310 LEU A CA  1 
ATOM   2645 C C   . LEU A 1 310 ? -3.085  24.296 57.997  1.00 12.11 ? 310 LEU A C   1 
ATOM   2646 O O   . LEU A 1 310 ? -4.255  24.419 58.389  1.00 14.90 ? 310 LEU A O   1 
ATOM   2647 C CB  . LEU A 1 310 ? -2.713  23.922 55.560  1.00 15.24 ? 310 LEU A CB  1 
ATOM   2648 C CG  . LEU A 1 310 ? -2.393  24.482 54.174  1.00 22.57 ? 310 LEU A CG  1 
ATOM   2649 C CD1 . LEU A 1 310 ? -2.534  23.389 53.132  1.00 19.63 ? 310 LEU A CD1 1 
ATOM   2650 C CD2 . LEU A 1 310 ? -3.290  25.678 53.850  1.00 20.52 ? 310 LEU A CD2 1 
ATOM   2651 N N   . SER A 1 311 ? -2.186  23.568 58.654  1.00 11.69 ? 311 SER A N   1 
ATOM   2652 C CA  . SER A 1 311 ? -2.545  22.917 59.908  1.00 14.90 ? 311 SER A CA  1 
ATOM   2653 C C   . SER A 1 311 ? -2.867  23.953 60.976  1.00 16.58 ? 311 SER A C   1 
ATOM   2654 O O   . SER A 1 311 ? -3.846  23.812 61.718  1.00 14.77 ? 311 SER A O   1 
ATOM   2655 C CB  . SER A 1 311 ? -1.410  22.001 60.360  1.00 12.99 ? 311 SER A CB  1 
ATOM   2656 O OG  . SER A 1 311 ? -1.062  21.092 59.336  1.00 15.37 ? 311 SER A OG  1 
ATOM   2657 N N   . ASP A 1 312 ? -2.058  25.006 61.055  1.00 14.89 ? 312 ASP A N   1 
ATOM   2658 C CA  . ASP A 1 312 ? -2.310  26.074 62.014  1.00 14.19 ? 312 ASP A CA  1 
ATOM   2659 C C   . ASP A 1 312 ? -3.550  26.896 61.676  1.00 17.20 ? 312 ASP A C   1 
ATOM   2660 O O   . ASP A 1 312 ? -4.186  27.434 62.586  1.00 16.06 ? 312 ASP A O   1 
ATOM   2661 C CB  . ASP A 1 312 ? -1.094  27.003 62.122  1.00 16.64 ? 312 ASP A CB  1 
ATOM   2662 C CG  . ASP A 1 312 ? 0.039   26.397 62.949  1.00 22.07 ? 312 ASP A CG  1 
ATOM   2663 O OD1 . ASP A 1 312 ? -0.216  25.404 63.676  1.00 22.16 ? 312 ASP A OD1 1 
ATOM   2664 O OD2 . ASP A 1 312 ? 1.170   26.932 62.910  1.00 21.19 ? 312 ASP A OD2 1 
ATOM   2665 N N   . LEU A 1 313 ? -3.906  27.039 60.391  1.00 15.18 ? 313 LEU A N   1 
ATOM   2666 C CA  . LEU A 1 313 ? -5.128  27.778 60.072  1.00 14.25 ? 313 LEU A CA  1 
ATOM   2667 C C   . LEU A 1 313 ? -6.349  27.082 60.673  1.00 12.86 ? 313 LEU A C   1 
ATOM   2668 O O   . LEU A 1 313 ? -7.221  27.729 61.265  1.00 14.05 ? 313 LEU A O   1 
ATOM   2669 C CB  . LEU A 1 313 ? -5.283  27.923 58.559  1.00 14.63 ? 313 LEU A CB  1 
ATOM   2670 C CG  . LEU A 1 313 ? -4.360  28.975 57.933  1.00 21.88 ? 313 LEU A CG  1 
ATOM   2671 C CD1 . LEU A 1 313 ? -4.222  28.719 56.458  1.00 24.16 ? 313 LEU A CD1 1 
ATOM   2672 C CD2 . LEU A 1 313 ? -4.905  30.368 58.188  1.00 25.29 ? 313 LEU A CD2 1 
ATOM   2673 N N   . ILE A 1 314 ? -6.416  25.759 60.549  1.00 15.23 ? 314 ILE A N   1 
ATOM   2674 C CA  . ILE A 1 314 ? -7.530  25.032 61.157  1.00 14.17 ? 314 ILE A CA  1 
ATOM   2675 C C   . ILE A 1 314 ? -7.397  25.036 62.673  1.00 15.77 ? 314 ILE A C   1 
ATOM   2676 O O   . ILE A 1 314 ? -8.347  25.350 63.403  1.00 14.04 ? 314 ILE A O   1 
ATOM   2677 C CB  . ILE A 1 314 ? -7.599  23.602 60.598  1.00 12.14 ? 314 ILE A CB  1 
ATOM   2678 C CG1 . ILE A 1 314 ? -7.912  23.641 59.096  1.00 14.32 ? 314 ILE A CG1 1 
ATOM   2679 C CG2 . ILE A 1 314 ? -8.587  22.726 61.414  1.00 11.19 ? 314 ILE A CG2 1 
ATOM   2680 C CD1 . ILE A 1 314 ? -7.885  22.261 58.437  1.00 15.07 ? 314 ILE A CD1 1 
ATOM   2681 N N   . GLY A 1 315 ? -6.208  24.695 63.167  1.00 14.66 ? 315 GLY A N   1 
ATOM   2682 C CA  . GLY A 1 315 ? -6.018  24.551 64.600  1.00 14.56 ? 315 GLY A CA  1 
ATOM   2683 C C   . GLY A 1 315 ? -6.179  25.839 65.381  1.00 16.30 ? 315 GLY A C   1 
ATOM   2684 O O   . GLY A 1 315 ? -6.589  25.808 66.546  1.00 18.88 ? 315 GLY A O   1 
ATOM   2685 N N   . PHE A 1 316 ? -5.852  26.987 64.768  1.00 14.25 ? 316 PHE A N   1 
ATOM   2686 C CA  . PHE A 1 316 ? -5.804  28.240 65.526  1.00 18.36 ? 316 PHE A CA  1 
ATOM   2687 C C   . PHE A 1 316 ? -6.502  29.422 64.870  1.00 20.40 ? 316 PHE A C   1 
ATOM   2688 O O   . PHE A 1 316 ? -6.950  30.322 65.588  1.00 20.45 ? 316 PHE A O   1 
ATOM   2689 C CB  . PHE A 1 316 ? -4.342  28.634 65.806  1.00 21.27 ? 316 PHE A CB  1 
ATOM   2690 C CG  . PHE A 1 316 ? -3.590  27.624 66.615  1.00 18.71 ? 316 PHE A CG  1 
ATOM   2691 C CD1 . PHE A 1 316 ? -3.832  27.478 67.975  1.00 26.03 ? 316 PHE A CD1 1 
ATOM   2692 C CD2 . PHE A 1 316 ? -2.639  26.826 66.026  1.00 19.72 ? 316 PHE A CD2 1 
ATOM   2693 C CE1 . PHE A 1 316 ? -3.131  26.536 68.721  1.00 18.94 ? 316 PHE A CE1 1 
ATOM   2694 C CE2 . PHE A 1 316 ? -1.940  25.883 66.767  1.00 27.46 ? 316 PHE A CE2 1 
ATOM   2695 C CZ  . PHE A 1 316 ? -2.184  25.745 68.112  1.00 24.59 ? 316 PHE A CZ  1 
ATOM   2696 N N   . SER A 1 317 ? -6.620  29.467 63.551  1.00 15.31 ? 317 SER A N   1 
ATOM   2697 C CA  . SER A 1 317 ? -7.119  30.680 62.916  1.00 18.19 ? 317 SER A CA  1 
ATOM   2698 C C   . SER A 1 317 ? -8.620  30.647 62.660  1.00 19.86 ? 317 SER A C   1 
ATOM   2699 O O   . SER A 1 317 ? -9.320  31.611 62.979  1.00 19.67 ? 317 SER A O   1 
ATOM   2700 C CB  . SER A 1 317 ? -6.368  30.928 61.606  1.00 23.19 ? 317 SER A CB  1 
ATOM   2701 O OG  . SER A 1 317 ? -6.927  32.029 60.908  1.00 37.23 ? 317 SER A OG  1 
ATOM   2702 N N   . TYR A 1 318 ? -9.134  29.556 62.079  1.00 16.92 ? 318 TYR A N   1 
ATOM   2703 C CA  . TYR A 1 318 ? -10.465 29.602 61.486  1.00 13.70 ? 318 TYR A CA  1 
ATOM   2704 C C   . TYR A 1 318 ? -11.594 29.648 62.505  1.00 13.76 ? 318 TYR A C   1 
ATOM   2705 O O   . TYR A 1 318 ? -12.741 29.888 62.111  1.00 16.79 ? 318 TYR A O   1 
ATOM   2706 C CB  . TYR A 1 318 ? -10.666 28.402 60.558  1.00 13.49 ? 318 TYR A CB  1 
ATOM   2707 C CG  . TYR A 1 318 ? -9.918  28.493 59.251  1.00 13.73 ? 318 TYR A CG  1 
ATOM   2708 C CD1 . TYR A 1 318 ? -9.614  29.730 58.667  1.00 17.82 ? 318 TYR A CD1 1 
ATOM   2709 C CD2 . TYR A 1 318 ? -9.530  27.347 58.587  1.00 13.45 ? 318 TYR A CD2 1 
ATOM   2710 C CE1 . TYR A 1 318 ? -8.933  29.799 57.455  1.00 19.32 ? 318 TYR A CE1 1 
ATOM   2711 C CE2 . TYR A 1 318 ? -8.850  27.409 57.384  1.00 14.72 ? 318 TYR A CE2 1 
ATOM   2712 C CZ  . TYR A 1 318 ? -8.555  28.619 56.822  1.00 17.67 ? 318 TYR A CZ  1 
ATOM   2713 O OH  . TYR A 1 318 ? -7.887  28.640 55.613  1.00 16.73 ? 318 TYR A OH  1 
ATOM   2714 N N   . HIS A 1 319 ? -11.324 29.407 63.789  1.00 18.08 ? 319 HIS A N   1 
ATOM   2715 C CA  . HIS A 1 319 ? -12.364 29.669 64.776  1.00 20.29 ? 319 HIS A CA  1 
ATOM   2716 C C   . HIS A 1 319 ? -12.796 31.131 64.735  1.00 26.18 ? 319 HIS A C   1 
ATOM   2717 O O   . HIS A 1 319 ? -13.969 31.432 64.969  1.00 23.26 ? 319 HIS A O   1 
ATOM   2718 C CB  . HIS A 1 319 ? -11.887 29.299 66.176  1.00 21.06 ? 319 HIS A CB  1 
ATOM   2719 C CG  . HIS A 1 319 ? -11.043 30.351 66.821  1.00 21.08 ? 319 HIS A CG  1 
ATOM   2720 N ND1 . HIS A 1 319 ? -9.672  30.394 66.681  1.00 24.80 ? 319 HIS A ND1 1 
ATOM   2721 C CD2 . HIS A 1 319 ? -11.376 31.406 67.600  1.00 21.63 ? 319 HIS A CD2 1 
ATOM   2722 C CE1 . HIS A 1 319 ? -9.194  31.420 67.364  1.00 22.48 ? 319 HIS A CE1 1 
ATOM   2723 N NE2 . HIS A 1 319 ? -10.210 32.056 67.921  1.00 24.75 ? 319 HIS A NE2 1 
ATOM   2724 N N   . ALA A 1 320 ? -11.871 32.045 64.414  1.00 24.61 ? 320 ALA A N   1 
ATOM   2725 C CA  . ALA A 1 320 ? -12.162 33.473 64.321  1.00 22.39 ? 320 ALA A CA  1 
ATOM   2726 C C   . ALA A 1 320 ? -12.720 33.889 62.955  1.00 28.78 ? 320 ALA A C   1 
ATOM   2727 O O   . ALA A 1 320 ? -12.777 35.092 62.660  1.00 28.65 ? 320 ALA A O   1 
ATOM   2728 C CB  . ALA A 1 320 ? -10.899 34.286 64.647  1.00 19.96 ? 320 ALA A CB  1 
ATOM   2729 N N   . TRP A 1 321 ? -13.165 32.931 62.142  1.00 23.49 ? 321 TRP A N   1 
ATOM   2730 C CA  . TRP A 1 321 ? -13.719 33.173 60.811  1.00 26.01 ? 321 TRP A CA  1 
ATOM   2731 C C   . TRP A 1 321 ? -15.142 32.628 60.708  1.00 24.88 ? 321 TRP A C   1 
ATOM   2732 O O   . TRP A 1 321 ? -15.504 31.665 61.386  1.00 25.66 ? 321 TRP A O   1 
ATOM   2733 C CB  . TRP A 1 321 ? -12.898 32.475 59.729  1.00 19.61 ? 321 TRP A CB  1 
ATOM   2734 C CG  . TRP A 1 321 ? -11.539 32.973 59.482  1.00 22.37 ? 321 TRP A CG  1 
ATOM   2735 C CD1 . TRP A 1 321 ? -10.519 33.084 60.387  1.00 17.84 ? 321 TRP A CD1 1 
ATOM   2736 C CD2 . TRP A 1 321 ? -10.993 33.331 58.212  1.00 27.57 ? 321 TRP A CD2 1 
ATOM   2737 N NE1 . TRP A 1 321 ? -9.381  33.541 59.756  1.00 20.70 ? 321 TRP A NE1 1 
ATOM   2738 C CE2 . TRP A 1 321 ? -9.648  33.690 58.421  1.00 21.20 ? 321 TRP A CE2 1 
ATOM   2739 C CE3 . TRP A 1 321 ? -11.519 33.398 56.917  1.00 27.37 ? 321 TRP A CE3 1 
ATOM   2740 C CZ2 . TRP A 1 321 ? -8.824  34.107 57.388  1.00 26.89 ? 321 TRP A CZ2 1 
ATOM   2741 C CZ3 . TRP A 1 321 ? -10.698 33.811 55.895  1.00 29.42 ? 321 TRP A CZ3 1 
ATOM   2742 C CH2 . TRP A 1 321 ? -9.363  34.164 56.135  1.00 26.07 ? 321 TRP A CH2 1 
ATOM   2743 N N   . ASN A 1 322 ? -15.940 33.223 59.825  1.00 24.01 ? 322 ASN A N   1 
ATOM   2744 C CA  . ASN A 1 322 ? -17.183 32.578 59.424  1.00 28.77 ? 322 ASN A CA  1 
ATOM   2745 C C   . ASN A 1 322 ? -16.863 31.344 58.575  1.00 30.18 ? 322 ASN A C   1 
ATOM   2746 O O   . ASN A 1 322 ? -15.852 31.297 57.872  1.00 26.99 ? 322 ASN A O   1 
ATOM   2747 C CB  . ASN A 1 322 ? -18.085 33.587 58.694  1.00 36.11 ? 322 ASN A CB  1 
ATOM   2748 C CG  . ASN A 1 322 ? -19.060 32.942 57.719  1.00 52.31 ? 322 ASN A CG  1 
ATOM   2749 O OD1 . ASN A 1 322 ? -18.710 32.645 56.577  1.00 55.85 ? 322 ASN A OD1 1 
ATOM   2750 N ND2 . ASN A 1 322 ? -20.293 32.719 58.173  1.00 56.98 ? 322 ASN A ND2 1 
ATOM   2751 N N   . ALA A 1 323 ? -17.713 30.315 58.689  1.00 28.06 ? 323 ALA A N   1 
ATOM   2752 C CA  . ALA A 1 323 ? -17.373 29.003 58.139  1.00 24.34 ? 323 ALA A CA  1 
ATOM   2753 C C   . ALA A 1 323 ? -17.180 29.049 56.625  1.00 23.96 ? 323 ALA A C   1 
ATOM   2754 O O   . ALA A 1 323 ? -16.216 28.478 56.100  1.00 22.24 ? 323 ALA A O   1 
ATOM   2755 C CB  . ALA A 1 323 ? -18.446 27.975 58.518  1.00 23.63 ? 323 ALA A CB  1 
ATOM   2756 N N   . GLU A 1 324 ? -18.088 29.717 55.902  1.00 22.93 ? 324 GLU A N   1 
ATOM   2757 C CA  . GLU A 1 324 ? -17.969 29.801 54.445  1.00 28.82 ? 324 GLU A CA  1 
ATOM   2758 C C   . GLU A 1 324 ? -16.662 30.471 54.033  1.00 27.57 ? 324 GLU A C   1 
ATOM   2759 O O   . GLU A 1 324 ? -15.952 29.987 53.140  1.00 23.14 ? 324 GLU A O   1 
ATOM   2760 C CB  . GLU A 1 324 ? -19.155 30.569 53.849  1.00 38.95 ? 324 GLU A CB  1 
ATOM   2761 C CG  . GLU A 1 324 ? -20.458 29.791 53.727  1.00 54.85 ? 324 GLU A CG  1 
ATOM   2762 C CD  . GLU A 1 324 ? -21.299 29.824 54.991  1.00 69.05 ? 324 GLU A CD  1 
ATOM   2763 O OE1 . GLU A 1 324 ? -20.814 30.323 56.033  1.00 69.35 ? 324 GLU A OE1 1 
ATOM   2764 O OE2 . GLU A 1 324 ? -22.460 29.362 54.931  1.00 75.92 ? 324 GLU A OE2 1 
ATOM   2765 N N   . ASP A 1 325 ? -16.331 31.594 54.673  1.00 25.18 ? 325 ASP A N   1 
ATOM   2766 C CA  . ASP A 1 325 ? -15.115 32.312 54.314  1.00 22.67 ? 325 ASP A CA  1 
ATOM   2767 C C   . ASP A 1 325 ? -13.877 31.477 54.610  1.00 22.06 ? 325 ASP A C   1 
ATOM   2768 O O   . ASP A 1 325 ? -12.905 31.511 53.846  1.00 22.32 ? 325 ASP A O   1 
ATOM   2769 C CB  . ASP A 1 325 ? -15.052 33.651 55.053  1.00 29.69 ? 325 ASP A CB  1 
ATOM   2770 C CG  . ASP A 1 325 ? -16.117 34.627 54.584  1.00 45.53 ? 325 ASP A CG  1 
ATOM   2771 O OD1 . ASP A 1 325 ? -16.601 34.478 53.443  1.00 51.20 ? 325 ASP A OD1 1 
ATOM   2772 O OD2 . ASP A 1 325 ? -16.467 35.547 55.351  1.00 50.12 ? 325 ASP A OD2 1 
ATOM   2773 N N   . ALA A 1 326 ? -13.887 30.731 55.722  1.00 20.84 ? 326 ALA A N   1 
ATOM   2774 C CA  . ALA A 1 326 ? -12.729 29.913 56.082  1.00 22.10 ? 326 ALA A CA  1 
ATOM   2775 C C   . ALA A 1 326 ? -12.479 28.833 55.039  1.00 20.78 ? 326 ALA A C   1 
ATOM   2776 O O   . ALA A 1 326 ? -11.338 28.618 54.616  1.00 18.73 ? 326 ALA A O   1 
ATOM   2777 C CB  . ALA A 1 326 ? -12.920 29.286 57.470  1.00 18.08 ? 326 ALA A CB  1 
ATOM   2778 N N   . VAL A 1 327 ? -13.541 28.140 54.612  1.00 20.82 ? 327 VAL A N   1 
ATOM   2779 C CA  . VAL A 1 327 ? -13.390 27.110 53.587  1.00 20.81 ? 327 VAL A CA  1 
ATOM   2780 C C   . VAL A 1 327 ? -12.922 27.723 52.275  1.00 25.73 ? 327 VAL A C   1 
ATOM   2781 O O   . VAL A 1 327 ? -12.019 27.191 51.613  1.00 19.99 ? 327 VAL A O   1 
ATOM   2782 C CB  . VAL A 1 327 ? -14.706 26.329 53.430  1.00 22.53 ? 327 VAL A CB  1 
ATOM   2783 C CG1 . VAL A 1 327 ? -14.625 25.387 52.226  1.00 25.12 ? 327 VAL A CG1 1 
ATOM   2784 C CG2 . VAL A 1 327 ? -15.004 25.573 54.739  1.00 15.53 ? 327 VAL A CG2 1 
ATOM   2785 N N   . ARG A 1 328 ? -13.509 28.865 51.893  1.00 24.11 ? 328 ARG A N   1 
ATOM   2786 C CA  . ARG A 1 328 ? -13.052 29.609 50.720  1.00 25.98 ? 328 ARG A CA  1 
ATOM   2787 C C   . ARG A 1 328 ? -11.554 29.907 50.814  1.00 21.40 ? 328 ARG A C   1 
ATOM   2788 O O   . ARG A 1 328 ? -10.804 29.705 49.853  1.00 23.84 ? 328 ARG A O   1 
ATOM   2789 C CB  . ARG A 1 328 ? -13.873 30.905 50.602  1.00 27.03 ? 328 ARG A CB  1 
ATOM   2790 C CG  . ARG A 1 328 ? -14.143 31.365 49.188  1.00 45.87 ? 328 ARG A CG  1 
ATOM   2791 C CD  . ARG A 1 328 ? -15.103 32.576 49.067  1.00 46.41 ? 328 ARG A CD  1 
ATOM   2792 N NE  . ARG A 1 328 ? -16.442 32.390 49.636  1.00 44.20 ? 328 ARG A NE  1 
ATOM   2793 C CZ  . ARG A 1 328 ? -16.926 33.134 50.629  1.00 51.04 ? 328 ARG A CZ  1 
ATOM   2794 N NH1 . ARG A 1 328 ? -16.172 34.085 51.162  1.00 50.55 ? 328 ARG A NH1 1 
ATOM   2795 N NH2 . ARG A 1 328 ? -18.150 32.931 51.099  1.00 52.64 ? 328 ARG A NH2 1 
ATOM   2796 N N   . ASP A 1 329 ? -11.102 30.348 51.985  1.00 18.19 ? 329 ASP A N   1 
ATOM   2797 C CA  . ASP A 1 329 ? -9.687  30.643 52.185  1.00 22.87 ? 329 ASP A CA  1 
ATOM   2798 C C   . ASP A 1 329 ? -8.827  29.390 52.059  1.00 19.01 ? 329 ASP A C   1 
ATOM   2799 O O   . ASP A 1 329 ? -7.774  29.400 51.403  1.00 19.70 ? 329 ASP A O   1 
ATOM   2800 C CB  . ASP A 1 329 ? -9.484  31.279 53.558  1.00 23.32 ? 329 ASP A CB  1 
ATOM   2801 C CG  . ASP A 1 329 ? -8.058  31.699 53.784  1.00 25.41 ? 329 ASP A CG  1 
ATOM   2802 O OD1 . ASP A 1 329 ? -7.676  32.749 53.232  1.00 26.15 ? 329 ASP A OD1 1 
ATOM   2803 O OD2 . ASP A 1 329 ? -7.314  30.964 54.469  1.00 21.22 ? 329 ASP A OD2 1 
ATOM   2804 N N   . PHE A 1 330 ? -9.254  28.303 52.699  1.00 16.80 ? 330 PHE A N   1 
ATOM   2805 C CA  . PHE A 1 330 ? -8.493  27.058 52.682  1.00 18.81 ? 330 PHE A CA  1 
ATOM   2806 C C   . PHE A 1 330 ? -8.407  26.475 51.273  1.00 24.41 ? 330 PHE A C   1 
ATOM   2807 O O   . PHE A 1 330 ? -7.331  26.053 50.829  1.00 18.39 ? 330 PHE A O   1 
ATOM   2808 C CB  . PHE A 1 330 ? -9.160  26.063 53.631  1.00 15.69 ? 330 PHE A CB  1 
ATOM   2809 C CG  . PHE A 1 330 ? -8.345  24.842 53.922  1.00 16.97 ? 330 PHE A CG  1 
ATOM   2810 C CD1 . PHE A 1 330 ? -7.338  24.877 54.885  1.00 20.99 ? 330 PHE A CD1 1 
ATOM   2811 C CD2 . PHE A 1 330 ? -8.610  23.646 53.273  1.00 19.92 ? 330 PHE A CD2 1 
ATOM   2812 C CE1 . PHE A 1 330 ? -6.599  23.745 55.183  1.00 21.88 ? 330 PHE A CE1 1 
ATOM   2813 C CE2 . PHE A 1 330 ? -7.865  22.501 53.561  1.00 20.76 ? 330 PHE A CE2 1 
ATOM   2814 C CZ  . PHE A 1 330 ? -6.864  22.554 54.512  1.00 20.32 ? 330 PHE A CZ  1 
ATOM   2815 N N   . ILE A 1 331 ? -9.547  26.397 50.574  1.00 20.04 ? 331 ILE A N   1 
ATOM   2816 C CA  . ILE A 1 331 ? -9.549  25.917 49.196  1.00 23.29 ? 331 ILE A CA  1 
ATOM   2817 C C   . ILE A 1 331 ? -8.678  26.813 48.326  1.00 22.17 ? 331 ILE A C   1 
ATOM   2818 O O   . ILE A 1 331 ? -7.887  26.331 47.504  1.00 21.33 ? 331 ILE A O   1 
ATOM   2819 C CB  . ILE A 1 331 ? -10.986 25.840 48.649  1.00 30.20 ? 331 ILE A CB  1 
ATOM   2820 C CG1 . ILE A 1 331 ? -11.808 24.827 49.450  1.00 28.65 ? 331 ILE A CG1 1 
ATOM   2821 C CG2 . ILE A 1 331 ? -10.978 25.507 47.150  1.00 33.83 ? 331 ILE A CG2 1 
ATOM   2822 C CD1 . ILE A 1 331 ? -11.217 23.432 49.466  1.00 27.25 ? 331 ILE A CD1 1 
ATOM   2823 N N   . GLY A 1 332 ? -8.797  28.127 48.508  1.00 22.15 ? 332 GLY A N   1 
ATOM   2824 C CA  . GLY A 1 332 ? -7.964  29.046 47.749  1.00 22.06 ? 332 GLY A CA  1 
ATOM   2825 C C   . GLY A 1 332 ? -6.484  28.782 47.939  1.00 23.58 ? 332 GLY A C   1 
ATOM   2826 O O   . GLY A 1 332 ? -5.693  28.916 47.001  1.00 23.40 ? 332 GLY A O   1 
ATOM   2827 N N   . ARG A 1 333 ? -6.081  28.413 49.158  1.00 20.75 ? 333 ARG A N   1 
ATOM   2828 C CA  . ARG A 1 333 ? -4.669  28.137 49.393  1.00 18.03 ? 333 ARG A CA  1 
ATOM   2829 C C   . ARG A 1 333 ? -4.253  26.822 48.750  1.00 22.85 ? 333 ARG A C   1 
ATOM   2830 O O   . ARG A 1 333 ? -3.139  26.708 48.226  1.00 21.74 ? 333 ARG A O   1 
ATOM   2831 C CB  . ARG A 1 333 ? -4.386  28.126 50.888  1.00 19.15 ? 333 ARG A CB  1 
ATOM   2832 C CG  . ARG A 1 333 ? -4.439  29.500 51.509  1.00 19.30 ? 333 ARG A CG  1 
ATOM   2833 C CD  . ARG A 1 333 ? -4.421  29.357 53.007  1.00 21.05 ? 333 ARG A CD  1 
ATOM   2834 N NE  . ARG A 1 333 ? -4.405  30.649 53.677  1.00 20.90 ? 333 ARG A NE  1 
ATOM   2835 C CZ  . ARG A 1 333 ? -3.290  31.280 54.022  1.00 23.99 ? 333 ARG A CZ  1 
ATOM   2836 N NH1 . ARG A 1 333 ? -2.112  30.738 53.737  1.00 26.36 ? 333 ARG A NH1 1 
ATOM   2837 N NH2 . ARG A 1 333 ? -3.353  32.442 54.658  1.00 25.88 ? 333 ARG A NH2 1 
ATOM   2838 N N   . LEU A 1 334 ? -5.138  25.819 48.767  1.00 17.72 ? 334 LEU A N   1 
ATOM   2839 C CA  . LEU A 1 334 ? -4.845  24.578 48.047  1.00 19.24 ? 334 LEU A CA  1 
ATOM   2840 C C   . LEU A 1 334 ? -4.739  24.818 46.549  1.00 20.59 ? 334 LEU A C   1 
ATOM   2841 O O   . LEU A 1 334 ? -3.916  24.191 45.872  1.00 20.16 ? 334 LEU A O   1 
ATOM   2842 C CB  . LEU A 1 334 ? -5.911  23.518 48.327  1.00 20.03 ? 334 LEU A CB  1 
ATOM   2843 C CG  . LEU A 1 334 ? -6.000  23.031 49.767  1.00 19.93 ? 334 LEU A CG  1 
ATOM   2844 C CD1 . LEU A 1 334 ? -7.152  22.044 49.921  1.00 22.69 ? 334 LEU A CD1 1 
ATOM   2845 C CD2 . LEU A 1 334 ? -4.678  22.378 50.194  1.00 18.23 ? 334 LEU A CD2 1 
ATOM   2846 N N   . LYS A 1 335 ? -5.588  25.691 46.002  1.00 21.36 ? 335 LYS A N   1 
ATOM   2847 C CA  . LYS A 1 335 ? -5.469  26.001 44.585  1.00 25.75 ? 335 LYS A CA  1 
ATOM   2848 C C   . LYS A 1 335 ? -4.102  26.616 44.287  1.00 27.10 ? 335 LYS A C   1 
ATOM   2849 O O   . LYS A 1 335 ? -3.438  26.232 43.317  1.00 29.94 ? 335 LYS A O   1 
ATOM   2850 C CB  . LYS A 1 335 ? -6.621  26.913 44.159  1.00 29.45 ? 335 LYS A CB  1 
ATOM   2851 C CG  . LYS A 1 335 ? -6.611  27.331 42.709  1.00 39.62 ? 335 LYS A CG  1 
ATOM   2852 C CD  . LYS A 1 335 ? -8.008  27.235 42.088  1.00 53.76 ? 335 LYS A CD  1 
ATOM   2853 C CE  . LYS A 1 335 ? -8.174  26.026 41.160  1.00 62.19 ? 335 LYS A CE  1 
ATOM   2854 N NZ  . LYS A 1 335 ? -9.368  26.141 40.251  1.00 65.12 ? 335 LYS A NZ  1 
ATOM   2855 N N   . LYS A 1 336 ? -3.631  27.520 45.154  1.00 23.36 ? 336 LYS A N   1 
ATOM   2856 C CA  . LYS A 1 336 ? -2.302  28.109 44.970  1.00 24.44 ? 336 LYS A CA  1 
ATOM   2857 C C   . LYS A 1 336 ? -1.218  27.032 44.966  1.00 25.55 ? 336 LYS A C   1 
ATOM   2858 O O   . LYS A 1 336 ? -0.301  27.060 44.138  1.00 27.76 ? 336 LYS A O   1 
ATOM   2859 C CB  . LYS A 1 336 ? -2.006  29.131 46.072  1.00 26.94 ? 336 LYS A CB  1 
ATOM   2860 C CG  . LYS A 1 336 ? -3.007  30.287 46.248  1.00 45.27 ? 336 LYS A CG  1 
ATOM   2861 C CD  . LYS A 1 336 ? -2.782  31.438 45.275  1.00 55.75 ? 336 LYS A CD  1 
ATOM   2862 C CE  . LYS A 1 336 ? -3.724  32.615 45.569  1.00 60.19 ? 336 LYS A CE  1 
ATOM   2863 N NZ  . LYS A 1 336 ? -3.435  33.298 46.869  1.00 59.18 ? 336 LYS A NZ  1 
ATOM   2864 N N   . ILE A 1 337 ? -1.276  26.104 45.925  1.00 25.21 ? 337 ILE A N   1 
ATOM   2865 C CA  . ILE A 1 337 ? -0.283  25.032 45.983  1.00 19.82 ? 337 ILE A CA  1 
ATOM   2866 C C   . ILE A 1 337 ? -0.337  24.184 44.722  1.00 25.16 ? 337 ILE A C   1 
ATOM   2867 O O   . ILE A 1 337 ? 0.700   23.825 44.153  1.00 25.39 ? 337 ILE A O   1 
ATOM   2868 C CB  . ILE A 1 337 ? -0.500  24.165 47.236  1.00 21.39 ? 337 ILE A CB  1 
ATOM   2869 C CG1 . ILE A 1 337 ? -0.283  24.993 48.513  1.00 17.92 ? 337 ILE A CG1 1 
ATOM   2870 C CG2 . ILE A 1 337 ? 0.452   22.974 47.217  1.00 22.28 ? 337 ILE A CG2 1 
ATOM   2871 C CD1 . ILE A 1 337 ? -0.752  24.261 49.776  1.00 17.62 ? 337 ILE A CD1 1 
ATOM   2872 N N   . HIS A 1 338 ? -1.552  23.822 44.289  1.00 22.39 ? 338 HIS A N   1 
ATOM   2873 C CA  . HIS A 1 338 ? -1.729  22.981 43.112  1.00 21.38 ? 338 HIS A CA  1 
ATOM   2874 C C   . HIS A 1 338 ? -1.059  23.593 41.892  1.00 29.21 ? 338 HIS A C   1 
ATOM   2875 O O   . HIS A 1 338 ? -0.335  22.906 41.161  1.00 29.65 ? 338 HIS A O   1 
ATOM   2876 C CB  . HIS A 1 338 ? -3.222  22.766 42.889  1.00 23.55 ? 338 HIS A CB  1 
ATOM   2877 C CG  . HIS A 1 338 ? -3.563  21.922 41.701  1.00 26.36 ? 338 HIS A CG  1 
ATOM   2878 N ND1 . HIS A 1 338 ? -4.231  22.422 40.604  1.00 31.17 ? 338 HIS A ND1 1 
ATOM   2879 C CD2 . HIS A 1 338 ? -3.353  20.609 41.450  1.00 28.04 ? 338 HIS A CD2 1 
ATOM   2880 C CE1 . HIS A 1 338 ? -4.417  21.451 39.726  1.00 34.24 ? 338 HIS A CE1 1 
ATOM   2881 N NE2 . HIS A 1 338 ? -3.890  20.342 40.214  1.00 30.09 ? 338 HIS A NE2 1 
ATOM   2882 N N   . GLU A 1 339 ? -1.238  24.889 41.676  1.00 32.35 ? 339 GLU A N   1 
ATOM   2883 C CA  . GLU A 1 339 ? -0.665  25.495 40.482  1.00 32.87 ? 339 GLU A CA  1 
ATOM   2884 C C   . GLU A 1 339 ? 0.714   26.087 40.720  1.00 29.08 ? 339 GLU A C   1 
ATOM   2885 O O   . GLU A 1 339 ? 1.280   26.691 39.805  1.00 31.46 ? 339 GLU A O   1 
ATOM   2886 C CB  . GLU A 1 339 ? -1.636  26.528 39.898  1.00 38.74 ? 339 GLU A CB  1 
ATOM   2887 C CG  . GLU A 1 339 ? -2.261  27.506 40.850  1.00 45.16 ? 339 GLU A CG  1 
ATOM   2888 C CD  . GLU A 1 339 ? -3.576  28.041 40.300  1.00 54.62 ? 339 GLU A CD  1 
ATOM   2889 O OE1 . GLU A 1 339 ? -3.862  27.792 39.110  1.00 59.33 ? 339 GLU A OE1 1 
ATOM   2890 O OE2 . GLU A 1 339 ? -4.331  28.696 41.048  1.00 59.15 ? 339 GLU A OE2 1 
ATOM   2891 N N   . SER A 1 340 ? 1.307   25.875 41.905  1.00 35.62 ? 340 SER A N   1 
ATOM   2892 C CA  . SER A 1 340 ? 2.673   26.312 42.178  1.00 33.80 ? 340 SER A CA  1 
ATOM   2893 C C   . SER A 1 340 ? 3.720   25.276 41.787  1.00 33.55 ? 340 SER A C   1 
ATOM   2894 O O   . SER A 1 340 ? 4.906   25.619 41.720  1.00 31.34 ? 340 SER A O   1 
ATOM   2895 C CB  . SER A 1 340 ? 2.870   26.647 43.665  1.00 33.73 ? 340 SER A CB  1 
ATOM   2896 O OG  . SER A 1 340 ? 3.042   25.464 44.451  1.00 29.96 ? 340 SER A OG  1 
ATOM   2897 N N   . VAL A 1 341 ? 3.330   24.026 41.540  1.00 28.28 ? 341 VAL A N   1 
ATOM   2898 C CA  . VAL A 1 341 ? 4.273   22.981 41.166  1.00 25.53 ? 341 VAL A CA  1 
ATOM   2899 C C   . VAL A 1 341 ? 3.703   22.201 39.990  1.00 24.87 ? 341 VAL A C   1 
ATOM   2900 O O   . VAL A 1 341 ? 2.485   22.089 39.828  1.00 29.24 ? 341 VAL A O   1 
ATOM   2901 C CB  . VAL A 1 341 ? 4.587   22.027 42.348  1.00 30.69 ? 341 VAL A CB  1 
ATOM   2902 C CG1 . VAL A 1 341 ? 5.358   22.750 43.440  1.00 29.66 ? 341 VAL A CG1 1 
ATOM   2903 C CG2 . VAL A 1 341 ? 3.307   21.430 42.904  1.00 25.03 ? 341 VAL A CG2 1 
ATOM   2904 N N   . ASP A 1 342 ? 4.592   21.672 39.152  1.00 27.17 ? 342 ASP A N   1 
ATOM   2905 C CA  . ASP A 1 342 ? 4.141   20.870 38.025  1.00 31.78 ? 342 ASP A CA  1 
ATOM   2906 C C   . ASP A 1 342 ? 3.986   19.399 38.386  1.00 33.71 ? 342 ASP A C   1 
ATOM   2907 O O   . ASP A 1 342 ? 3.425   18.638 37.591  1.00 35.99 ? 342 ASP A O   1 
ATOM   2908 C CB  . ASP A 1 342 ? 5.088   21.020 36.822  1.00 39.59 ? 342 ASP A CB  1 
ATOM   2909 C CG  . ASP A 1 342 ? 6.483   20.484 37.091  1.00 49.45 ? 342 ASP A CG  1 
ATOM   2910 O OD1 . ASP A 1 342 ? 6.818   20.223 38.263  1.00 53.92 ? 342 ASP A OD1 1 
ATOM   2911 O OD2 . ASP A 1 342 ? 7.245   20.322 36.113  1.00 56.00 ? 342 ASP A OD2 1 
ATOM   2912 N N   . PHE A 1 343 ? 4.455   18.985 39.560  1.00 29.75 ? 343 PHE A N   1 
ATOM   2913 C CA  . PHE A 1 343 ? 4.199   17.636 40.035  1.00 25.67 ? 343 PHE A CA  1 
ATOM   2914 C C   . PHE A 1 343 ? 2.961   17.630 40.926  1.00 23.49 ? 343 PHE A C   1 
ATOM   2915 O O   . PHE A 1 343 ? 2.309   18.658 41.129  1.00 25.11 ? 343 PHE A O   1 
ATOM   2916 C CB  . PHE A 1 343 ? 5.418   17.064 40.764  1.00 24.90 ? 343 PHE A CB  1 
ATOM   2917 C CG  . PHE A 1 343 ? 5.886   17.878 41.967  1.00 27.44 ? 343 PHE A CG  1 
ATOM   2918 C CD1 . PHE A 1 343 ? 6.855   18.866 41.821  1.00 28.42 ? 343 PHE A CD1 1 
ATOM   2919 C CD2 . PHE A 1 343 ? 5.411   17.605 43.245  1.00 22.23 ? 343 PHE A CD2 1 
ATOM   2920 C CE1 . PHE A 1 343 ? 7.311   19.595 42.923  1.00 25.64 ? 343 PHE A CE1 1 
ATOM   2921 C CE2 . PHE A 1 343 ? 5.869   18.333 44.359  1.00 28.20 ? 343 PHE A CE2 1 
ATOM   2922 C CZ  . PHE A 1 343 ? 6.816   19.330 44.191  1.00 28.34 ? 343 PHE A CZ  1 
ATOM   2923 N N   . GLN A 1 344 ? 2.622   16.457 41.467  1.00 21.42 ? 344 GLN A N   1 
ATOM   2924 C CA  . GLN A 1 344 ? 1.480   16.381 42.361  1.00 20.51 ? 344 GLN A CA  1 
ATOM   2925 C C   . GLN A 1 344 ? 1.978   16.491 43.793  1.00 22.24 ? 344 GLN A C   1 
ATOM   2926 O O   . GLN A 1 344 ? 2.645   15.564 44.288  1.00 20.80 ? 344 GLN A O   1 
ATOM   2927 C CB  . GLN A 1 344 ? 0.699   15.085 42.149  1.00 21.14 ? 344 GLN A CB  1 
ATOM   2928 C CG  . GLN A 1 344 ? 0.738   14.555 40.725  1.00 23.25 ? 344 GLN A CG  1 
ATOM   2929 C CD  . GLN A 1 344 ? -0.347  13.522 40.411  1.00 29.51 ? 344 GLN A CD  1 
ATOM   2930 O OE1 . GLN A 1 344 ? -1.536  13.822 40.234  1.00 27.51 ? 344 GLN A OE1 1 
ATOM   2931 N NE2 . GLN A 1 344 ? 0.052   12.284 40.492  1.00 22.47 ? 344 GLN A NE2 1 
ATOM   2932 N N   . PRO A 1 345 ? 1.704   17.593 44.480  1.00 20.18 ? 345 PRO A N   1 
ATOM   2933 C CA  . PRO A 1 345 ? 2.188   17.755 45.850  1.00 18.77 ? 345 PRO A CA  1 
ATOM   2934 C C   . PRO A 1 345 ? 1.375   16.919 46.824  1.00 21.54 ? 345 PRO A C   1 
ATOM   2935 O O   . PRO A 1 345 ? 0.176   16.696 46.642  1.00 21.54 ? 345 PRO A O   1 
ATOM   2936 C CB  . PRO A 1 345 ? 1.984   19.250 46.111  1.00 23.65 ? 345 PRO A CB  1 
ATOM   2937 C CG  . PRO A 1 345 ? 0.761   19.593 45.282  1.00 20.80 ? 345 PRO A CG  1 
ATOM   2938 C CD  . PRO A 1 345 ? 0.851   18.717 44.046  1.00 21.83 ? 345 PRO A CD  1 
ATOM   2939 N N   . VAL A 1 346 ? 2.049   16.445 47.867  1.00 17.60 ? 346 VAL A N   1 
ATOM   2940 C CA  . VAL A 1 346 ? 1.387   15.761 48.973  1.00 19.04 ? 346 VAL A CA  1 
ATOM   2941 C C   . VAL A 1 346 ? 1.303   16.750 50.126  1.00 22.32 ? 346 VAL A C   1 
ATOM   2942 O O   . VAL A 1 346 ? 2.327   17.261 50.591  1.00 16.92 ? 346 VAL A O   1 
ATOM   2943 C CB  . VAL A 1 346 ? 2.127   14.481 49.387  1.00 19.09 ? 346 VAL A CB  1 
ATOM   2944 C CG1 . VAL A 1 346 ? 1.307   13.752 50.457  1.00 21.17 ? 346 VAL A CG1 1 
ATOM   2945 C CG2 . VAL A 1 346 ? 2.336   13.572 48.192  1.00 19.85 ? 346 VAL A CG2 1 
ATOM   2946 N N   . VAL A 1 347 ? 0.092   17.017 50.598  1.00 15.09 ? 347 VAL A N   1 
ATOM   2947 C CA  . VAL A 1 347 ? -0.147  18.121 51.520  1.00 14.22 ? 347 VAL A CA  1 
ATOM   2948 C C   . VAL A 1 347 ? -0.675  17.509 52.811  1.00 19.38 ? 347 VAL A C   1 
ATOM   2949 O O   . VAL A 1 347 ? -1.849  17.125 52.877  1.00 17.89 ? 347 VAL A O   1 
ATOM   2950 C CB  . VAL A 1 347 ? -1.122  19.149 50.944  1.00 20.80 ? 347 VAL A CB  1 
ATOM   2951 C CG1 . VAL A 1 347 ? -1.421  20.229 51.971  1.00 19.12 ? 347 VAL A CG1 1 
ATOM   2952 C CG2 . VAL A 1 347 ? -0.521  19.767 49.661  1.00 17.35 ? 347 VAL A CG2 1 
ATOM   2953 N N   . PHE A 1 348 ? 0.188   17.394 53.832  1.00 17.47 ? 348 PHE A N   1 
ATOM   2954 C CA  . PHE A 1 348 ? -0.214  16.825 55.114  1.00 17.54 ? 348 PHE A CA  1 
ATOM   2955 C C   . PHE A 1 348 ? -0.763  17.915 56.020  1.00 18.47 ? 348 PHE A C   1 
ATOM   2956 O O   . PHE A 1 348 ? -0.074  18.897 56.318  1.00 17.16 ? 348 PHE A O   1 
ATOM   2957 C CB  . PHE A 1 348 ? 0.930   16.113 55.837  1.00 15.68 ? 348 PHE A CB  1 
ATOM   2958 C CG  . PHE A 1 348 ? 1.044   14.649 55.519  1.00 14.82 ? 348 PHE A CG  1 
ATOM   2959 C CD1 . PHE A 1 348 ? 1.236   14.199 54.218  1.00 16.93 ? 348 PHE A CD1 1 
ATOM   2960 C CD2 . PHE A 1 348 ? 0.848   13.703 56.532  1.00 19.53 ? 348 PHE A CD2 1 
ATOM   2961 C CE1 . PHE A 1 348 ? 1.312   12.818 53.950  1.00 17.82 ? 348 PHE A CE1 1 
ATOM   2962 C CE2 . PHE A 1 348 ? 0.903   12.336 56.269  1.00 17.79 ? 348 PHE A CE2 1 
ATOM   2963 C CZ  . PHE A 1 348 ? 1.142   11.888 54.985  1.00 14.16 ? 348 PHE A CZ  1 
ATOM   2964 N N   . VAL A 1 349 ? -1.990  17.721 56.496  1.00 13.80 ? 349 VAL A N   1 
ATOM   2965 C CA  . VAL A 1 349 ? -2.604  18.610 57.465  1.00 11.82 ? 349 VAL A CA  1 
ATOM   2966 C C   . VAL A 1 349 ? -2.684  17.807 58.752  1.00 15.09 ? 349 VAL A C   1 
ATOM   2967 O O   . VAL A 1 349 ? -3.443  16.838 58.829  1.00 12.69 ? 349 VAL A O   1 
ATOM   2968 C CB  . VAL A 1 349 ? -3.983  19.092 56.991  1.00 15.81 ? 349 VAL A CB  1 
ATOM   2969 C CG1 . VAL A 1 349 ? -4.653  19.979 58.041  1.00 14.72 ? 349 VAL A CG1 1 
ATOM   2970 C CG2 . VAL A 1 349 ? -3.835  19.827 55.661  1.00 18.16 ? 349 VAL A CG2 1 
ATOM   2971 N N   . VAL A 1 350 ? -1.859  18.152 59.736  1.00 12.42 ? 350 VAL A N   1 
ATOM   2972 C CA  . VAL A 1 350 ? -1.686  17.320 60.921  1.00 15.86 ? 350 VAL A CA  1 
ATOM   2973 C C   . VAL A 1 350 ? -1.812  18.220 62.144  1.00 13.81 ? 350 VAL A C   1 
ATOM   2974 O O   . VAL A 1 350 ? -1.094  19.221 62.256  1.00 13.51 ? 350 VAL A O   1 
ATOM   2975 C CB  . VAL A 1 350 ? -0.329  16.581 60.926  1.00 10.79 ? 350 VAL A CB  1 
ATOM   2976 C CG1 . VAL A 1 350 ? -0.234  15.630 62.121  1.00 11.78 ? 350 VAL A CG1 1 
ATOM   2977 C CG2 . VAL A 1 350 ? -0.092  15.819 59.638  1.00 12.67 ? 350 VAL A CG2 1 
ATOM   2978 N N   . LEU A 1 351 ? -2.721  17.871 63.055  1.00 10.56 ? 351 LEU A N   1 
ATOM   2979 C CA  . LEU A 1 351 ? -2.924  18.660 64.261  1.00 11.98 ? 351 LEU A CA  1 
ATOM   2980 C C   . LEU A 1 351 ? -3.727  17.819 65.245  1.00 11.28 ? 351 LEU A C   1 
ATOM   2981 O O   . LEU A 1 351 ? -4.222  16.733 64.915  1.00 12.15 ? 351 LEU A O   1 
ATOM   2982 C CB  . LEU A 1 351 ? -3.633  19.995 63.957  1.00 11.93 ? 351 LEU A CB  1 
ATOM   2983 C CG  . LEU A 1 351 ? -5.034  19.960 63.307  1.00 11.81 ? 351 LEU A CG  1 
ATOM   2984 C CD1 . LEU A 1 351 ? -5.832  21.190 63.690  1.00 17.97 ? 351 LEU A CD1 1 
ATOM   2985 C CD2 . LEU A 1 351 ? -4.954  19.848 61.778  1.00 13.18 ? 351 LEU A CD2 1 
ATOM   2986 N N   . ASP A 1 352 ? -3.854  18.339 66.466  1.00 12.35 ? 352 ASP A N   1 
ATOM   2987 C CA  . ASP A 1 352 ? -4.776  17.738 67.414  1.00 12.00 ? 352 ASP A CA  1 
ATOM   2988 C C   . ASP A 1 352 ? -6.164  17.650 66.802  1.00 10.67 ? 352 ASP A C   1 
ATOM   2989 O O   . ASP A 1 352 ? -6.638  18.585 66.145  1.00 13.45 ? 352 ASP A O   1 
ATOM   2990 C CB  . ASP A 1 352 ? -4.865  18.537 68.712  1.00 11.19 ? 352 ASP A CB  1 
ATOM   2991 C CG  . ASP A 1 352 ? -3.554  18.597 69.464  1.00 14.98 ? 352 ASP A CG  1 
ATOM   2992 O OD1 . ASP A 1 352 ? -2.568  17.935 69.057  1.00 13.16 ? 352 ASP A OD1 1 
ATOM   2993 O OD2 . ASP A 1 352 ? -3.539  19.291 70.504  1.00 13.68 ? 352 ASP A OD2 1 
ATOM   2994 N N   . GLY A 1 353 ? -6.840  16.541 67.057  1.00 9.26  ? 353 GLY A N   1 
ATOM   2995 C CA  . GLY A 1 353 ? -8.149  16.372 66.477  1.00 10.01 ? 353 GLY A CA  1 
ATOM   2996 C C   . GLY A 1 353 ? -9.291  16.746 67.386  1.00 10.28 ? 353 GLY A C   1 
ATOM   2997 O O   . GLY A 1 353 ? -10.448 16.646 66.966  1.00 13.55 ? 353 GLY A O   1 
ATOM   2998 N N   . GLU A 1 354 ? -9.034  17.184 68.604  1.00 9.24  ? 354 GLU A N   1 
ATOM   2999 C CA  . GLU A 1 354 ? -10.129 17.475 69.484  1.00 9.42  ? 354 GLU A CA  1 
ATOM   3000 C C   . GLU A 1 354 ? -10.115 18.768 70.255  1.00 11.17 ? 354 GLU A C   1 
ATOM   3001 O O   . GLU A 1 354 ? -10.993 18.985 71.021  1.00 9.75  ? 354 GLU A O   1 
ATOM   3002 C CB  . GLU A 1 354 ? -10.219 16.344 70.528  1.00 9.31  ? 354 GLU A CB  1 
ATOM   3003 C CG  . GLU A 1 354 ? -9.207  16.453 71.655  1.00 13.18 ? 354 GLU A CG  1 
ATOM   3004 C CD  . GLU A 1 354 ? -7.836  15.898 71.295  1.00 34.95 ? 354 GLU A CD  1 
ATOM   3005 O OE1 . GLU A 1 354 ? -7.167  16.519 70.528  1.00 52.06 ? 354 GLU A OE1 1 
ATOM   3006 O OE2 . GLU A 1 354 ? -7.435  14.883 71.810  1.00 23.13 ? 354 GLU A OE2 1 
ATOM   3007 N N   . ASN A 1 355 ? -9.085  19.576 70.047  1.00 11.16 ? 355 ASN A N   1 
ATOM   3008 C CA  . ASN A 1 355 ? -8.921  20.716 70.929  1.00 12.96 ? 355 ASN A CA  1 
ATOM   3009 C C   . ASN A 1 355 ? -9.352  22.039 70.321  1.00 11.14 ? 355 ASN A C   1 
ATOM   3010 O O   . ASN A 1 355 ? -9.670  22.966 71.078  1.00 13.56 ? 355 ASN A O   1 
ATOM   3011 C CB  . ASN A 1 355 ? -7.466  20.797 71.408  1.00 11.58 ? 355 ASN A CB  1 
ATOM   3012 C CG  . ASN A 1 355 ? -7.136  19.664 72.352  1.00 10.92 ? 355 ASN A CG  1 
ATOM   3013 O OD1 . ASN A 1 355 ? -7.960  19.318 73.214  1.00 11.74 ? 355 ASN A OD1 1 
ATOM   3014 N ND2 . ASN A 1 355 ? -5.978  19.043 72.166  1.00 9.62  ? 355 ASN A ND2 1 
ATOM   3015 N N   . CYS A 1 356 ? -9.395  22.155 68.993  1.00 10.75 ? 356 CYS A N   1 
ATOM   3016 C CA  . CYS A 1 356 ? -9.708  23.454 68.396  1.00 12.78 ? 356 CYS A CA  1 
ATOM   3017 C C   . CYS A 1 356 ? -11.204 23.721 68.267  1.00 13.41 ? 356 CYS A C   1 
ATOM   3018 O O   . CYS A 1 356 ? -11.621 24.892 68.268  1.00 11.96 ? 356 CYS A O   1 
ATOM   3019 C CB  . CYS A 1 356 ? -9.035  23.571 67.019  1.00 13.82 ? 356 CYS A CB  1 
ATOM   3020 S SG  . CYS A 1 356 ? -9.434  22.240 65.856  1.00 12.91 ? 356 CYS A SG  1 
ATOM   3021 N N   . TRP A 1 357 ? -12.025 22.667 68.190  1.00 12.99 ? 357 TRP A N   1 
ATOM   3022 C CA  . TRP A 1 357 ? -13.426 22.833 67.809  1.00 12.21 ? 357 TRP A CA  1 
ATOM   3023 C C   . TRP A 1 357 ? -14.243 23.607 68.838  1.00 11.65 ? 357 TRP A C   1 
ATOM   3024 O O   . TRP A 1 357 ? -15.165 24.331 68.441  1.00 13.42 ? 357 TRP A O   1 
ATOM   3025 C CB  . TRP A 1 357 ? -14.064 21.464 67.532  1.00 11.19 ? 357 TRP A CB  1 
ATOM   3026 C CG  . TRP A 1 357 ? -13.176 20.654 66.646  1.00 10.86 ? 357 TRP A CG  1 
ATOM   3027 C CD1 . TRP A 1 357 ? -12.589 19.454 66.951  1.00 12.95 ? 357 TRP A CD1 1 
ATOM   3028 C CD2 . TRP A 1 357 ? -12.731 21.001 65.328  1.00 16.40 ? 357 TRP A CD2 1 
ATOM   3029 N NE1 . TRP A 1 357 ? -11.803 19.032 65.903  1.00 11.37 ? 357 TRP A NE1 1 
ATOM   3030 C CE2 . TRP A 1 357 ? -11.877 19.959 64.890  1.00 10.97 ? 357 TRP A CE2 1 
ATOM   3031 C CE3 . TRP A 1 357 ? -12.976 22.090 64.469  1.00 13.54 ? 357 TRP A CE3 1 
ATOM   3032 C CZ2 . TRP A 1 357 ? -11.266 19.969 63.638  1.00 12.17 ? 357 TRP A CZ2 1 
ATOM   3033 C CZ3 . TRP A 1 357 ? -12.362 22.105 63.219  1.00 13.01 ? 357 TRP A CZ3 1 
ATOM   3034 C CH2 . TRP A 1 357 ? -11.515 21.041 62.814  1.00 13.48 ? 357 TRP A CH2 1 
ATOM   3035 N N   . GLU A 1 358 ? -13.911 23.511 70.138  1.00 11.48 ? 358 GLU A N   1 
ATOM   3036 C CA  . GLU A 1 358 ? -14.688 24.204 71.166  1.00 11.93 ? 358 GLU A CA  1 
ATOM   3037 C C   . GLU A 1 358 ? -14.626 25.711 71.007  1.00 14.12 ? 358 GLU A C   1 
ATOM   3038 O O   . GLU A 1 358 ? -15.465 26.418 71.579  1.00 15.14 ? 358 GLU A O   1 
ATOM   3039 C CB  . GLU A 1 358 ? -14.191 23.865 72.577  1.00 11.71 ? 358 GLU A CB  1 
ATOM   3040 C CG  . GLU A 1 358 ? -12.687 23.899 72.638  1.00 16.25 ? 358 GLU A CG  1 
ATOM   3041 C CD  . GLU A 1 358 ? -12.100 23.182 73.817  1.00 18.86 ? 358 GLU A CD  1 
ATOM   3042 O OE1 . GLU A 1 358 ? -11.858 23.737 74.913  1.00 19.20 ? 358 GLU A OE1 1 
ATOM   3043 O OE2 . GLU A 1 358 ? -12.004 21.964 73.642  1.00 15.01 ? 358 GLU A OE2 1 
ATOM   3044 N N   . TYR A 1 359 ? -13.647 26.225 70.257  1.00 13.00 ? 359 TYR A N   1 
ATOM   3045 C CA  . TYR A 1 359 ? -13.551 27.657 70.012  1.00 13.62 ? 359 TYR A CA  1 
ATOM   3046 C C   . TYR A 1 359 ? -14.249 28.084 68.728  1.00 16.68 ? 359 TYR A C   1 
ATOM   3047 O O   . TYR A 1 359 ? -14.357 29.293 68.479  1.00 17.49 ? 359 TYR A O   1 
ATOM   3048 C CB  . TYR A 1 359 ? -12.080 28.097 69.984  1.00 17.17 ? 359 TYR A CB  1 
ATOM   3049 C CG  . TYR A 1 359 ? -11.348 27.711 71.252  1.00 14.79 ? 359 TYR A CG  1 
ATOM   3050 C CD1 . TYR A 1 359 ? -11.483 28.473 72.412  1.00 22.68 ? 359 TYR A CD1 1 
ATOM   3051 C CD2 . TYR A 1 359 ? -10.565 26.565 71.303  1.00 16.76 ? 359 TYR A CD2 1 
ATOM   3052 C CE1 . TYR A 1 359 ? -10.827 28.119 73.585  1.00 21.37 ? 359 TYR A CE1 1 
ATOM   3053 C CE2 . TYR A 1 359 ? -9.906  26.200 72.469  1.00 20.32 ? 359 TYR A CE2 1 
ATOM   3054 C CZ  . TYR A 1 359 ? -10.044 26.982 73.605  1.00 24.85 ? 359 TYR A CZ  1 
ATOM   3055 O OH  . TYR A 1 359 ? -9.396  26.616 74.763  1.00 29.13 ? 359 TYR A OH  1 
ATOM   3056 N N   . TYR A 1 360 ? -14.739 27.139 67.923  1.00 13.15 ? 360 TYR A N   1 
ATOM   3057 C CA  . TYR A 1 360 ? -15.557 27.483 66.778  1.00 14.94 ? 360 TYR A CA  1 
ATOM   3058 C C   . TYR A 1 360 ? -17.029 27.594 67.168  1.00 18.99 ? 360 TYR A C   1 
ATOM   3059 O O   . TYR A 1 360 ? -17.521 26.907 68.063  1.00 18.68 ? 360 TYR A O   1 
ATOM   3060 C CB  . TYR A 1 360 ? -15.475 26.442 65.650  1.00 15.45 ? 360 TYR A CB  1 
ATOM   3061 C CG  . TYR A 1 360 ? -14.185 26.267 64.843  1.00 17.19 ? 360 TYR A CG  1 
ATOM   3062 C CD1 . TYR A 1 360 ? -12.966 25.890 65.429  1.00 15.23 ? 360 TYR A CD1 1 
ATOM   3063 C CD2 . TYR A 1 360 ? -14.215 26.456 63.457  1.00 16.78 ? 360 TYR A CD2 1 
ATOM   3064 C CE1 . TYR A 1 360 ? -11.826 25.712 64.634  1.00 16.45 ? 360 TYR A CE1 1 
ATOM   3065 C CE2 . TYR A 1 360 ? -13.102 26.291 62.680  1.00 14.89 ? 360 TYR A CE2 1 
ATOM   3066 C CZ  . TYR A 1 360 ? -11.912 25.920 63.261  1.00 16.11 ? 360 TYR A CZ  1 
ATOM   3067 O OH  . TYR A 1 360 ? -10.820 25.750 62.436  1.00 16.31 ? 360 TYR A OH  1 
ATOM   3068 N N   . GLU A 1 361 ? -17.735 28.348 66.355  1.00 18.74 ? 361 GLU A N   1 
ATOM   3069 C CA  . GLU A 1 361 ? -19.141 28.412 66.462  1.00 23.37 ? 361 GLU A CA  1 
ATOM   3070 C C   . GLU A 1 361 ? -19.714 26.980 66.232  1.00 21.25 ? 361 GLU A C   1 
ATOM   3071 O O   . GLU A 1 361 ? -19.266 26.295 65.361  1.00 20.24 ? 361 GLU A O   1 
ATOM   3072 C CB  . GLU A 1 361 ? -19.647 29.323 65.329  1.00 32.56 ? 361 GLU A CB  1 
ATOM   3073 C CG  . GLU A 1 361 ? -21.146 29.451 65.238  1.00 51.51 ? 361 GLU A CG  1 
ATOM   3074 C CD  . GLU A 1 361 ? -21.780 28.955 63.926  1.00 60.10 ? 361 GLU A CD  1 
ATOM   3075 O OE1 . GLU A 1 361 ? -21.219 29.145 62.830  1.00 53.69 ? 361 GLU A OE1 1 
ATOM   3076 O OE2 . GLU A 1 361 ? -22.878 28.374 64.001  1.00 59.32 ? 361 GLU A OE2 1 
ATOM   3077 N N   . GLU A 1 362 ? -20.684 26.568 67.039  1.00 20.32 ? 362 GLU A N   1 
ATOM   3078 C CA  . GLU A 1 362 ? -21.358 25.273 66.860  1.00 21.39 ? 362 GLU A CA  1 
ATOM   3079 C C   . GLU A 1 362 ? -20.367 24.113 66.785  1.00 20.01 ? 362 GLU A C   1 
ATOM   3080 O O   . GLU A 1 362 ? -20.523 23.175 65.995  1.00 16.43 ? 362 GLU A O   1 
ATOM   3081 C CB  . GLU A 1 362 ? -22.268 25.293 65.634  1.00 23.16 ? 362 GLU A CB  1 
ATOM   3082 C CG  . GLU A 1 362 ? -23.732 25.468 65.978  1.00 32.53 ? 362 GLU A CG  1 
ATOM   3083 C CD  . GLU A 1 362 ? -24.550 25.897 64.786  1.00 45.15 ? 362 GLU A CD  1 
ATOM   3084 O OE1 . GLU A 1 362 ? -24.284 26.986 64.236  1.00 50.49 ? 362 GLU A OE1 1 
ATOM   3085 O OE2 . GLU A 1 362 ? -25.446 25.129 64.390  1.00 50.66 ? 362 GLU A OE2 1 
ATOM   3086 N N   . ASN A 1 363 ? -19.340 24.187 67.627  1.00 17.57 ? 363 ASN A N   1 
ATOM   3087 C CA  . ASN A 1 363 ? -18.349 23.121 67.774  1.00 15.69 ? 363 ASN A CA  1 
ATOM   3088 C C   . ASN A 1 363 ? -17.650 22.813 66.454  1.00 14.35 ? 363 ASN A C   1 
ATOM   3089 O O   . ASN A 1 363 ? -17.219 21.683 66.212  1.00 16.06 ? 363 ASN A O   1 
ATOM   3090 C CB  . ASN A 1 363 ? -18.964 21.834 68.347  1.00 14.23 ? 363 ASN A CB  1 
ATOM   3091 C CG  . ASN A 1 363 ? -17.912 20.872 68.870  1.00 18.17 ? 363 ASN A CG  1 
ATOM   3092 O OD1 . ASN A 1 363 ? -16.883 21.283 69.405  1.00 15.36 ? 363 ASN A OD1 1 
ATOM   3093 N ND2 . ASN A 1 363 ? -18.134 19.587 68.643  1.00 17.42 ? 363 ASN A ND2 1 
ATOM   3094 N N   . GLY A 1 364 ? -17.517 23.806 65.586  1.00 15.83 ? 364 GLY A N   1 
ATOM   3095 C CA  . GLY A 1 364 ? -16.839 23.571 64.322  1.00 14.46 ? 364 GLY A CA  1 
ATOM   3096 C C   . GLY A 1 364 ? -17.623 22.783 63.296  1.00 17.76 ? 364 GLY A C   1 
ATOM   3097 O O   . GLY A 1 364 ? -17.075 22.456 62.236  1.00 13.27 ? 364 GLY A O   1 
ATOM   3098 N N   . ILE A 1 365 ? -18.881 22.465 63.567  1.00 15.49 ? 365 ILE A N   1 
ATOM   3099 C CA  . ILE A 1 365 ? -19.645 21.589 62.685  1.00 16.70 ? 365 ILE A CA  1 
ATOM   3100 C C   . ILE A 1 365 ? -19.956 22.296 61.369  1.00 17.46 ? 365 ILE A C   1 
ATOM   3101 O O   . ILE A 1 365 ? -19.703 21.706 60.314  1.00 17.30 ? 365 ILE A O   1 
ATOM   3102 C CB  . ILE A 1 365 ? -20.890 21.058 63.410  1.00 17.19 ? 365 ILE A CB  1 
ATOM   3103 C CG1 . ILE A 1 365 ? -20.399 20.156 64.554  1.00 15.78 ? 365 ILE A CG1 1 
ATOM   3104 C CG2 . ILE A 1 365 ? -21.802 20.295 62.462  1.00 17.36 ? 365 ILE A CG2 1 
ATOM   3105 C CD1 . ILE A 1 365 ? -21.440 19.858 65.625  1.00 18.68 ? 365 ILE A CD1 1 
ATOM   3106 N N   . PRO A 1 366 ? -20.461 23.544 61.347  1.00 18.24 ? 366 PRO A N   1 
ATOM   3107 C CA  . PRO A 1 366 ? -20.606 24.221 60.040  1.00 20.54 ? 366 PRO A CA  1 
ATOM   3108 C C   . PRO A 1 366 ? -19.308 24.271 59.247  1.00 16.30 ? 366 PRO A C   1 
ATOM   3109 O O   . PRO A 1 366 ? -19.337 24.098 58.026  1.00 17.06 ? 366 PRO A O   1 
ATOM   3110 C CB  . PRO A 1 366 ? -21.095 25.627 60.422  1.00 18.65 ? 366 PRO A CB  1 
ATOM   3111 C CG  . PRO A 1 366 ? -21.782 25.436 61.727  1.00 21.46 ? 366 PRO A CG  1 
ATOM   3112 C CD  . PRO A 1 366 ? -20.979 24.381 62.447  1.00 24.93 ? 366 PRO A CD  1 
ATOM   3113 N N   . PHE A 1 367 ? -18.166 24.487 59.910  1.00 16.73 ? 367 PHE A N   1 
ATOM   3114 C CA  . PHE A 1 367 ? -16.894 24.530 59.193  1.00 18.20 ? 367 PHE A CA  1 
ATOM   3115 C C   . PHE A 1 367 ? -16.551 23.176 58.575  1.00 19.42 ? 367 PHE A C   1 
ATOM   3116 O O   . PHE A 1 367 ? -16.223 23.092 57.385  1.00 17.06 ? 367 PHE A O   1 
ATOM   3117 C CB  . PHE A 1 367 ? -15.753 24.975 60.109  1.00 14.74 ? 367 PHE A CB  1 
ATOM   3118 C CG  . PHE A 1 367 ? -14.390 24.869 59.451  1.00 13.80 ? 367 PHE A CG  1 
ATOM   3119 C CD1 . PHE A 1 367 ? -14.016 25.769 58.454  1.00 14.37 ? 367 PHE A CD1 1 
ATOM   3120 C CD2 . PHE A 1 367 ? -13.504 23.869 59.805  1.00 16.34 ? 367 PHE A CD2 1 
ATOM   3121 C CE1 . PHE A 1 367 ? -12.781 25.668 57.831  1.00 15.53 ? 367 PHE A CE1 1 
ATOM   3122 C CE2 . PHE A 1 367 ? -12.261 23.761 59.189  1.00 16.45 ? 367 PHE A CE2 1 
ATOM   3123 C CZ  . PHE A 1 367 ? -11.897 24.666 58.200  1.00 13.70 ? 367 PHE A CZ  1 
ATOM   3124 N N   . LEU A 1 368 ? -16.576 22.110 59.374  1.00 15.18 ? 368 LEU A N   1 
ATOM   3125 C CA  . LEU A 1 368 ? -16.146 20.822 58.844  1.00 12.25 ? 368 LEU A CA  1 
ATOM   3126 C C   . LEU A 1 368 ? -17.141 20.282 57.829  1.00 15.09 ? 368 LEU A C   1 
ATOM   3127 O O   . LEU A 1 368 ? -16.741 19.668 56.835  1.00 16.92 ? 368 LEU A O   1 
ATOM   3128 C CB  . LEU A 1 368 ? -15.938 19.814 59.974  1.00 11.54 ? 368 LEU A CB  1 
ATOM   3129 C CG  . LEU A 1 368 ? -14.681 20.061 60.816  1.00 11.49 ? 368 LEU A CG  1 
ATOM   3130 C CD1 . LEU A 1 368 ? -14.611 19.018 61.937  1.00 13.64 ? 368 LEU A CD1 1 
ATOM   3131 C CD2 . LEU A 1 368 ? -13.392 20.029 59.962  1.00 13.07 ? 368 LEU A CD2 1 
ATOM   3132 N N   . GLU A 1 369 ? -18.440 20.489 58.063  1.00 14.35 ? 369 GLU A N   1 
ATOM   3133 C CA  . GLU A 1 369 ? -19.422 20.054 57.073  1.00 15.05 ? 369 GLU A CA  1 
ATOM   3134 C C   . GLU A 1 369 ? -19.210 20.764 55.742  1.00 16.99 ? 369 GLU A C   1 
ATOM   3135 O O   . GLU A 1 369 ? -19.244 20.127 54.683  1.00 17.72 ? 369 GLU A O   1 
ATOM   3136 C CB  . GLU A 1 369 ? -20.838 20.274 57.596  1.00 18.13 ? 369 GLU A CB  1 
ATOM   3137 C CG  . GLU A 1 369 ? -21.194 19.285 58.693  1.00 14.50 ? 369 GLU A CG  1 
ATOM   3138 C CD  . GLU A 1 369 ? -22.650 19.344 59.082  1.00 20.66 ? 369 GLU A CD  1 
ATOM   3139 O OE1 . GLU A 1 369 ? -23.347 20.276 58.640  1.00 27.04 ? 369 GLU A OE1 1 
ATOM   3140 O OE2 . GLU A 1 369 ? -23.101 18.452 59.829  1.00 23.68 ? 369 GLU A OE2 1 
ATOM   3141 N N   . LYS A 1 370 ? -18.951 22.074 55.766  1.00 17.30 ? 370 LYS A N   1 
ATOM   3142 C CA  . LYS A 1 370 ? -18.706 22.762 54.505  1.00 17.12 ? 370 LYS A CA  1 
ATOM   3143 C C   . LYS A 1 370 ? -17.363 22.362 53.911  1.00 15.51 ? 370 LYS A C   1 
ATOM   3144 O O   . LYS A 1 370 ? -17.256 22.165 52.694  1.00 17.04 ? 370 LYS A O   1 
ATOM   3145 C CB  . LYS A 1 370 ? -18.782 24.280 54.677  1.00 23.44 ? 370 LYS A CB  1 
ATOM   3146 C CG  . LYS A 1 370 ? -18.635 25.003 53.343  1.00 44.90 ? 370 LYS A CG  1 
ATOM   3147 C CD  . LYS A 1 370 ? -18.998 26.474 53.407  1.00 57.85 ? 370 LYS A CD  1 
ATOM   3148 C CE  . LYS A 1 370 ? -19.010 27.097 52.008  1.00 61.24 ? 370 LYS A CE  1 
ATOM   3149 N NZ  . LYS A 1 370 ? -17.651 27.333 51.442  1.00 63.16 ? 370 LYS A NZ  1 
ATOM   3150 N N   . LEU A 1 371 ? -16.333 22.223 54.753  1.00 14.42 ? 371 LEU A N   1 
ATOM   3151 C CA  . LEU A 1 371 ? -15.011 21.846 54.260  1.00 15.37 ? 371 LEU A CA  1 
ATOM   3152 C C   . LEU A 1 371 ? -15.049 20.480 53.597  1.00 17.55 ? 371 LEU A C   1 
ATOM   3153 O O   . LEU A 1 371 ? -14.552 20.300 52.478  1.00 15.67 ? 371 LEU A O   1 
ATOM   3154 C CB  . LEU A 1 371 ? -13.996 21.825 55.407  1.00 14.48 ? 371 LEU A CB  1 
ATOM   3155 C CG  . LEU A 1 371 ? -12.589 21.360 54.996  1.00 18.31 ? 371 LEU A CG  1 
ATOM   3156 C CD1 . LEU A 1 371 ? -11.948 22.374 54.051  1.00 16.95 ? 371 LEU A CD1 1 
ATOM   3157 C CD2 . LEU A 1 371 ? -11.688 21.100 56.204  1.00 18.83 ? 371 LEU A CD2 1 
ATOM   3158 N N   . TYR A 1 372 ? -15.628 19.497 54.289  1.00 14.10 ? 372 TYR A N   1 
ATOM   3159 C CA  . TYR A 1 372 ? -15.655 18.135 53.771  1.00 15.82 ? 372 TYR A CA  1 
ATOM   3160 C C   . TYR A 1 372 ? -16.594 18.014 52.571  1.00 19.93 ? 372 TYR A C   1 
ATOM   3161 O O   . TYR A 1 372 ? -16.271 17.330 51.590  1.00 19.10 ? 372 TYR A O   1 
ATOM   3162 C CB  . TYR A 1 372 ? -16.077 17.183 54.888  1.00 15.42 ? 372 TYR A CB  1 
ATOM   3163 C CG  . TYR A 1 372 ? -15.060 16.991 55.997  1.00 17.87 ? 372 TYR A CG  1 
ATOM   3164 C CD1 . TYR A 1 372 ? -13.718 17.335 55.830  1.00 14.74 ? 372 TYR A CD1 1 
ATOM   3165 C CD2 . TYR A 1 372 ? -15.452 16.456 57.219  1.00 12.50 ? 372 TYR A CD2 1 
ATOM   3166 C CE1 . TYR A 1 372 ? -12.789 17.129 56.856  1.00 15.64 ? 372 TYR A CE1 1 
ATOM   3167 C CE2 . TYR A 1 372 ? -14.545 16.260 58.245  1.00 11.75 ? 372 TYR A CE2 1 
ATOM   3168 C CZ  . TYR A 1 372 ? -13.217 16.581 58.061  1.00 13.71 ? 372 TYR A CZ  1 
ATOM   3169 O OH  . TYR A 1 372 ? -12.321 16.367 59.079  1.00 13.70 ? 372 TYR A OH  1 
ATOM   3170 N N   . SER A 1 373 ? -17.758 18.678 52.625  1.00 15.63 ? 373 SER A N   1 
ATOM   3171 C CA  . SER A 1 373 ? -18.641 18.734 51.456  1.00 17.27 ? 373 SER A CA  1 
ATOM   3172 C C   . SER A 1 373 ? -17.919 19.302 50.239  1.00 22.38 ? 373 SER A C   1 
ATOM   3173 O O   . SER A 1 373 ? -18.063 18.790 49.119  1.00 26.35 ? 373 SER A O   1 
ATOM   3174 C CB  . SER A 1 373 ? -19.885 19.569 51.775  1.00 20.24 ? 373 SER A CB  1 
ATOM   3175 O OG  . SER A 1 373 ? -20.745 19.642 50.654  1.00 30.85 ? 373 SER A OG  1 
ATOM   3176 N N   . THR A 1 374 ? -17.129 20.356 50.440  1.00 19.52 ? 374 THR A N   1 
ATOM   3177 C CA  . THR A 1 374 ? -16.412 20.971 49.330  1.00 20.17 ? 374 THR A CA  1 
ATOM   3178 C C   . THR A 1 374 ? -15.326 20.045 48.800  1.00 21.34 ? 374 THR A C   1 
ATOM   3179 O O   . THR A 1 374 ? -15.248 19.801 47.590  1.00 22.28 ? 374 THR A O   1 
ATOM   3180 C CB  . THR A 1 374 ? -15.830 22.314 49.774  1.00 20.32 ? 374 THR A CB  1 
ATOM   3181 O OG1 . THR A 1 374 ? -16.899 23.179 50.194  1.00 22.19 ? 374 THR A OG1 1 
ATOM   3182 C CG2 . THR A 1 374 ? -15.056 22.985 48.638  1.00 22.22 ? 374 THR A CG2 1 
ATOM   3183 N N   . LEU A 1 375 ? -14.499 19.491 49.695  1.00 22.77 ? 375 LEU A N   1 
ATOM   3184 C CA  . LEU A 1 375 ? -13.401 18.619 49.271  1.00 21.27 ? 375 LEU A CA  1 
ATOM   3185 C C   . LEU A 1 375 ? -13.910 17.387 48.540  1.00 20.48 ? 375 LEU A C   1 
ATOM   3186 O O   . LEU A 1 375 ? -13.296 16.934 47.570  1.00 22.02 ? 375 LEU A O   1 
ATOM   3187 C CB  . LEU A 1 375 ? -12.567 18.192 50.485  1.00 19.32 ? 375 LEU A CB  1 
ATOM   3188 C CG  . LEU A 1 375 ? -11.765 19.292 51.170  1.00 15.83 ? 375 LEU A CG  1 
ATOM   3189 C CD1 . LEU A 1 375 ? -11.123 18.773 52.453  1.00 16.81 ? 375 LEU A CD1 1 
ATOM   3190 C CD2 . LEU A 1 375 ? -10.716 19.865 50.230  1.00 24.75 ? 375 LEU A CD2 1 
ATOM   3191 N N   . GLU A 1 376 ? -15.023 16.825 49.017  1.00 20.74 ? 376 GLU A N   1 
ATOM   3192 C CA  . GLU A 1 376 ? -15.671 15.667 48.414  1.00 23.83 ? 376 GLU A CA  1 
ATOM   3193 C C   . GLU A 1 376 ? -15.925 15.851 46.926  1.00 24.07 ? 376 GLU A C   1 
ATOM   3194 O O   . GLU A 1 376 ? -15.923 14.876 46.163  1.00 27.45 ? 376 GLU A O   1 
ATOM   3195 C CB  . GLU A 1 376 ? -17.000 15.446 49.126  1.00 26.22 ? 376 GLU A CB  1 
ATOM   3196 C CG  . GLU A 1 376 ? -17.675 14.136 48.935  1.00 35.70 ? 376 GLU A CG  1 
ATOM   3197 C CD  . GLU A 1 376 ? -19.074 14.160 49.532  1.00 38.09 ? 376 GLU A CD  1 
ATOM   3198 O OE1 . GLU A 1 376 ? -19.676 15.256 49.639  1.00 35.83 ? 376 GLU A OE1 1 
ATOM   3199 O OE2 . GLU A 1 376 ? -19.559 13.086 49.923  1.00 38.71 ? 376 GLU A OE2 1 
ATOM   3200 N N   . LYS A 1 377 ? -16.178 17.084 46.500  1.00 21.06 ? 377 LYS A N   1 
ATOM   3201 C CA  . LYS A 1 377 ? -16.616 17.342 45.138  1.00 22.38 ? 377 LYS A CA  1 
ATOM   3202 C C   . LYS A 1 377 ? -15.540 17.986 44.275  1.00 23.54 ? 377 LYS A C   1 
ATOM   3203 O O   . LYS A 1 377 ? -15.740 18.112 43.061  1.00 24.12 ? 377 LYS A O   1 
ATOM   3204 C CB  . LYS A 1 377 ? -17.872 18.225 45.158  1.00 24.64 ? 377 LYS A CB  1 
ATOM   3205 C CG  . LYS A 1 377 ? -19.042 17.596 45.919  1.00 24.89 ? 377 LYS A CG  1 
ATOM   3206 C CD  . LYS A 1 377 ? -20.187 18.582 46.086  1.00 31.71 ? 377 LYS A CD  1 
ATOM   3207 C CE  . LYS A 1 377 ? -21.316 18.013 46.923  1.00 34.25 ? 377 LYS A CE  1 
ATOM   3208 N NZ  . LYS A 1 377 ? -20.857 17.749 48.307  1.00 33.76 ? 377 LYS A NZ  1 
ATOM   3209 N N   . GLU A 1 378 ? -14.407 18.370 44.859  1.00 22.00 ? 378 GLU A N   1 
ATOM   3210 C CA  . GLU A 1 378 ? -13.354 19.045 44.107  1.00 28.17 ? 378 GLU A CA  1 
ATOM   3211 C C   . GLU A 1 378 ? -12.620 18.035 43.245  1.00 29.01 ? 378 GLU A C   1 
ATOM   3212 O O   . GLU A 1 378 ? -12.064 17.060 43.749  1.00 34.33 ? 378 GLU A O   1 
ATOM   3213 C CB  . GLU A 1 378 ? -12.358 19.729 45.048  1.00 33.82 ? 378 GLU A CB  1 
ATOM   3214 C CG  . GLU A 1 378 ? -12.826 21.004 45.740  1.00 40.41 ? 378 GLU A CG  1 
ATOM   3215 C CD  . GLU A 1 378 ? -13.072 22.173 44.798  1.00 46.75 ? 378 GLU A CD  1 
ATOM   3216 O OE1 . GLU A 1 378 ? -12.863 22.039 43.573  1.00 47.06 ? 378 GLU A OE1 1 
ATOM   3217 O OE2 . GLU A 1 378 ? -13.450 23.252 45.304  1.00 47.92 ? 378 GLU A OE2 1 
ATOM   3218 N N   . GLU A 1 379 ? -12.564 18.285 41.955  1.00 29.45 ? 379 GLU A N   1 
ATOM   3219 C CA  . GLU A 1 379 ? -12.067 17.232 41.089  1.00 32.15 ? 379 GLU A CA  1 
ATOM   3220 C C   . GLU A 1 379 ? -10.544 17.163 41.018  1.00 29.50 ? 379 GLU A C   1 
ATOM   3221 O O   . GLU A 1 379 ? -10.002 16.101 40.707  1.00 32.25 ? 379 GLU A O   1 
ATOM   3222 C CB  . GLU A 1 379 ? -12.710 17.421 39.721  1.00 43.12 ? 379 GLU A CB  1 
ATOM   3223 C CG  . GLU A 1 379 ? -14.210 17.209 39.913  1.00 53.67 ? 379 GLU A CG  1 
ATOM   3224 C CD  . GLU A 1 379 ? -15.043 17.541 38.723  1.00 57.54 ? 379 GLU A CD  1 
ATOM   3225 O OE1 . GLU A 1 379 ? -15.999 16.786 38.457  1.00 51.99 ? 379 GLU A OE1 1 
ATOM   3226 O OE2 . GLU A 1 379 ? -14.754 18.565 38.075  1.00 65.85 ? 379 GLU A OE2 1 
ATOM   3227 N N   . TRP A 1 380 ? -9.843  18.238 41.362  1.00 24.33 ? 380 TRP A N   1 
ATOM   3228 C CA  . TRP A 1 380 ? -8.390  18.233 41.315  1.00 28.12 ? 380 TRP A CA  1 
ATOM   3229 C C   . TRP A 1 380 ? -7.757  17.887 42.660  1.00 24.76 ? 380 TRP A C   1 
ATOM   3230 O O   . TRP A 1 380 ? -6.528  17.848 42.753  1.00 29.36 ? 380 TRP A O   1 
ATOM   3231 C CB  . TRP A 1 380 ? -7.879  19.595 40.822  1.00 24.21 ? 380 TRP A CB  1 
ATOM   3232 C CG  . TRP A 1 380 ? -8.505  20.727 41.560  1.00 25.88 ? 380 TRP A CG  1 
ATOM   3233 C CD1 . TRP A 1 380 ? -9.710  21.307 41.294  1.00 32.40 ? 380 TRP A CD1 1 
ATOM   3234 C CD2 . TRP A 1 380 ? -7.970  21.415 42.695  1.00 23.63 ? 380 TRP A CD2 1 
ATOM   3235 N NE1 . TRP A 1 380 ? -9.961  22.313 42.196  1.00 30.77 ? 380 TRP A NE1 1 
ATOM   3236 C CE2 . TRP A 1 380 ? -8.909  22.398 43.067  1.00 28.45 ? 380 TRP A CE2 1 
ATOM   3237 C CE3 . TRP A 1 380 ? -6.787  21.295 43.441  1.00 23.31 ? 380 TRP A CE3 1 
ATOM   3238 C CZ2 . TRP A 1 380 ? -8.703  23.256 44.144  1.00 31.73 ? 380 TRP A CZ2 1 
ATOM   3239 C CZ3 . TRP A 1 380 ? -6.587  22.145 44.503  1.00 23.50 ? 380 TRP A CZ3 1 
ATOM   3240 C CH2 . TRP A 1 380 ? -7.539  23.113 44.850  1.00 29.65 ? 380 TRP A CH2 1 
ATOM   3241 N N   . ILE A 1 381 ? -8.552  17.620 43.696  1.00 19.54 ? 381 ILE A N   1 
ATOM   3242 C CA  . ILE A 1 381 ? -8.042  17.209 45.005  1.00 19.23 ? 381 ILE A CA  1 
ATOM   3243 C C   . ILE A 1 381 ? -8.405  15.749 45.220  1.00 26.66 ? 381 ILE A C   1 
ATOM   3244 O O   . ILE A 1 381 ? -9.555  15.352 45.002  1.00 24.38 ? 381 ILE A O   1 
ATOM   3245 C CB  . ILE A 1 381 ? -8.622  18.069 46.140  1.00 22.29 ? 381 ILE A CB  1 
ATOM   3246 C CG1 . ILE A 1 381 ? -8.265  19.539 45.952  1.00 24.57 ? 381 ILE A CG1 1 
ATOM   3247 C CG2 . ILE A 1 381 ? -8.140  17.580 47.518  1.00 23.65 ? 381 ILE A CG2 1 
ATOM   3248 C CD1 . ILE A 1 381 ? -8.989  20.463 46.913  1.00 23.23 ? 381 ILE A CD1 1 
ATOM   3249 N N   . GLU A 1 382 ? -7.435  14.950 45.653  1.00 17.38 ? 382 GLU A N   1 
ATOM   3250 C CA  . GLU A 1 382 ? -7.713  13.600 46.131  1.00 25.76 ? 382 GLU A CA  1 
ATOM   3251 C C   . GLU A 1 382 ? -7.222  13.495 47.564  1.00 21.31 ? 382 GLU A C   1 
ATOM   3252 O O   . GLU A 1 382 ? -6.019  13.608 47.814  1.00 19.00 ? 382 GLU A O   1 
ATOM   3253 C CB  . GLU A 1 382 ? -7.022  12.537 45.276  1.00 32.77 ? 382 GLU A CB  1 
ATOM   3254 C CG  . GLU A 1 382 ? -7.476  11.121 45.581  1.00 45.83 ? 382 GLU A CG  1 
ATOM   3255 C CD  . GLU A 1 382 ? -6.819  10.097 44.678  1.00 63.06 ? 382 GLU A CD  1 
ATOM   3256 O OE1 . GLU A 1 382 ? -6.652  8.936  45.118  1.00 67.61 ? 382 GLU A OE1 1 
ATOM   3257 O OE2 . GLU A 1 382 ? -6.461  10.457 43.534  1.00 67.88 ? 382 GLU A OE2 1 
ATOM   3258 N N   . THR A 1 383 ? -8.138  13.275 48.500  1.00 20.61 ? 383 THR A N   1 
ATOM   3259 C CA  . THR A 1 383 ? -7.706  12.969 49.857  1.00 14.48 ? 383 THR A CA  1 
ATOM   3260 C C   . THR A 1 383 ? -7.261  11.515 49.935  1.00 17.28 ? 383 THR A C   1 
ATOM   3261 O O   . THR A 1 383 ? -7.814  10.637 49.260  1.00 17.30 ? 383 THR A O   1 
ATOM   3262 C CB  . THR A 1 383 ? -8.823  13.239 50.877  1.00 13.80 ? 383 THR A CB  1 
ATOM   3263 O OG1 . THR A 1 383 ? -9.990  12.484 50.528  1.00 14.13 ? 383 THR A OG1 1 
ATOM   3264 C CG2 . THR A 1 383 ? -9.165  14.727 50.893  1.00 18.13 ? 383 THR A CG2 1 
ATOM   3265 N N   . LEU A 1 384 ? -6.252  11.264 50.774  1.00 18.41 ? 384 LEU A N   1 
ATOM   3266 C CA  . LEU A 1 384 ? -5.589  9.971  50.840  1.00 16.82 ? 384 LEU A CA  1 
ATOM   3267 C C   . LEU A 1 384 ? -5.588  9.432  52.259  1.00 14.05 ? 384 LEU A C   1 
ATOM   3268 O O   . LEU A 1 384 ? -5.547  10.191 53.231  1.00 15.88 ? 384 LEU A O   1 
ATOM   3269 C CB  . LEU A 1 384 ? -4.122  10.059 50.382  1.00 17.26 ? 384 LEU A CB  1 
ATOM   3270 C CG  . LEU A 1 384 ? -3.818  10.595 48.992  1.00 16.98 ? 384 LEU A CG  1 
ATOM   3271 C CD1 . LEU A 1 384 ? -2.310  10.562 48.767  1.00 16.54 ? 384 LEU A CD1 1 
ATOM   3272 C CD2 . LEU A 1 384 ? -4.537  9.759  47.955  1.00 17.25 ? 384 LEU A CD2 1 
ATOM   3273 N N   . THR A 1 385 ? -5.601  8.105  52.372  1.00 14.45 ? 385 THR A N   1 
ATOM   3274 C CA  . THR A 1 385 ? -5.241  7.505  53.650  1.00 14.10 ? 385 THR A CA  1 
ATOM   3275 C C   . THR A 1 385 ? -3.731  7.566  53.836  1.00 20.44 ? 385 THR A C   1 
ATOM   3276 O O   . THR A 1 385 ? -2.980  7.846  52.900  1.00 19.10 ? 385 THR A O   1 
ATOM   3277 C CB  . THR A 1 385 ? -5.674  6.049  53.711  1.00 16.12 ? 385 THR A CB  1 
ATOM   3278 O OG1 . THR A 1 385 ? -4.931  5.313  52.727  1.00 16.36 ? 385 THR A OG1 1 
ATOM   3279 C CG2 . THR A 1 385 ? -7.188  5.917  53.453  1.00 16.38 ? 385 THR A CG2 1 
ATOM   3280 N N   . LEU A 1 386 ? -3.280  7.278  55.061  1.00 17.36 ? 386 LEU A N   1 
ATOM   3281 C CA  . LEU A 1 386 ? -1.842  7.208  55.296  1.00 16.69 ? 386 LEU A CA  1 
ATOM   3282 C C   . LEU A 1 386 ? -1.209  6.125  54.444  1.00 16.16 ? 386 LEU A C   1 
ATOM   3283 O O   . LEU A 1 386 ? -0.098  6.296  53.930  1.00 19.48 ? 386 LEU A O   1 
ATOM   3284 C CB  . LEU A 1 386 ? -1.548  6.949  56.767  1.00 14.10 ? 386 LEU A CB  1 
ATOM   3285 C CG  . LEU A 1 386 ? -2.102  7.970  57.753  1.00 13.17 ? 386 LEU A CG  1 
ATOM   3286 C CD1 . LEU A 1 386 ? -1.713  7.575  59.170  1.00 13.09 ? 386 LEU A CD1 1 
ATOM   3287 C CD2 . LEU A 1 386 ? -1.600  9.391  57.436  1.00 14.23 ? 386 LEU A CD2 1 
ATOM   3288 N N   . GLU A 1 387 ? -1.911  5.007  54.269  1.00 18.74 ? 387 GLU A N   1 
ATOM   3289 C CA  . GLU A 1 387 ? -1.387  3.943  53.426  1.00 19.11 ? 387 GLU A CA  1 
ATOM   3290 C C   . GLU A 1 387 ? -1.244  4.409  51.988  1.00 20.44 ? 387 GLU A C   1 
ATOM   3291 O O   . GLU A 1 387 ? -0.241  4.114  51.329  1.00 21.91 ? 387 GLU A O   1 
ATOM   3292 C CB  . GLU A 1 387 ? -2.289  2.711  53.505  1.00 19.99 ? 387 GLU A CB  1 
ATOM   3293 C CG  . GLU A 1 387 ? -1.722  1.508  52.781  1.00 29.69 ? 387 GLU A CG  1 
ATOM   3294 C CD  . GLU A 1 387 ? -2.559  0.270  52.968  1.00 50.72 ? 387 GLU A CD  1 
ATOM   3295 O OE1 . GLU A 1 387 ? -3.634  0.371  53.594  1.00 56.51 ? 387 GLU A OE1 1 
ATOM   3296 O OE2 . GLU A 1 387 ? -2.138  -0.808 52.493  1.00 60.10 ? 387 GLU A OE2 1 
ATOM   3297 N N   . GLU A 1 388 ? -2.245  5.129  51.478  1.00 20.64 ? 388 GLU A N   1 
ATOM   3298 C CA  . GLU A 1 388 ? -2.181  5.613  50.103  1.00 19.46 ? 388 GLU A CA  1 
ATOM   3299 C C   . GLU A 1 388 ? -1.067  6.636  49.934  1.00 22.64 ? 388 GLU A C   1 
ATOM   3300 O O   . GLU A 1 388 ? -0.353  6.621  48.926  1.00 24.49 ? 388 GLU A O   1 
ATOM   3301 C CB  . GLU A 1 388 ? -3.529  6.200  49.698  1.00 21.18 ? 388 GLU A CB  1 
ATOM   3302 C CG  . GLU A 1 388 ? -4.561  5.129  49.434  1.00 21.04 ? 388 GLU A CG  1 
ATOM   3303 C CD  . GLU A 1 388 ? -5.975  5.669  49.334  1.00 27.28 ? 388 GLU A CD  1 
ATOM   3304 O OE1 . GLU A 1 388 ? -6.239  6.806  49.787  1.00 17.28 ? 388 GLU A OE1 1 
ATOM   3305 O OE2 . GLU A 1 388 ? -6.831  4.935  48.798  1.00 35.15 ? 388 GLU A OE2 1 
ATOM   3306 N N   . ALA A 1 389 ? -0.903  7.534  50.912  1.00 20.69 ? 389 ALA A N   1 
ATOM   3307 C CA  . ALA A 1 389 ? 0.178   8.512  50.842  1.00 23.49 ? 389 ALA A CA  1 
ATOM   3308 C C   . ALA A 1 389 ? 1.530   7.821  50.887  1.00 25.48 ? 389 ALA A C   1 
ATOM   3309 O O   . ALA A 1 389 ? 2.470   8.225  50.187  1.00 23.21 ? 389 ALA A O   1 
ATOM   3310 C CB  . ALA A 1 389 ? 0.055   9.517  51.987  1.00 22.96 ? 389 ALA A CB  1 
ATOM   3311 N N   . MET A 1 390 ? 1.634   6.759  51.692  1.00 25.54 ? 390 MET A N   1 
ATOM   3312 C CA  . MET A 1 390 ? 2.903   6.070  51.874  1.00 29.56 ? 390 MET A CA  1 
ATOM   3313 C C   . MET A 1 390 ? 3.323   5.326  50.620  1.00 36.01 ? 390 MET A C   1 
ATOM   3314 O O   . MET A 1 390 ? 4.521   5.246  50.331  1.00 34.95 ? 390 MET A O   1 
ATOM   3315 C CB  . MET A 1 390 ? 2.816   5.100  53.057  1.00 31.79 ? 390 MET A CB  1 
ATOM   3316 C CG  . MET A 1 390 ? 4.123   4.393  53.383  1.00 46.76 ? 390 MET A CG  1 
ATOM   3317 S SD  . MET A 1 390 ? 4.010   3.265  54.793  1.00 52.04 ? 390 MET A SD  1 
ATOM   3318 C CE  . MET A 1 390 ? 3.007   1.946  54.108  1.00 53.64 ? 390 MET A CE  1 
ATOM   3319 N N   . ARG A 1 391 ? 2.366   4.786  49.865  1.00 29.03 ? 391 ARG A N   1 
ATOM   3320 C CA  . ARG A 1 391 ? 2.671   3.934  48.730  1.00 34.97 ? 391 ARG A CA  1 
ATOM   3321 C C   . ARG A 1 391 ? 2.411   4.597  47.379  1.00 31.57 ? 391 ARG A C   1 
ATOM   3322 O O   . ARG A 1 391 ? 2.600   3.955  46.342  1.00 33.10 ? 391 ARG A O   1 
ATOM   3323 C CB  . ARG A 1 391 ? 1.882   2.618  48.843  1.00 41.35 ? 391 ARG A CB  1 
ATOM   3324 C CG  . ARG A 1 391 ? 2.614   1.567  49.676  1.00 51.94 ? 391 ARG A CG  1 
ATOM   3325 C CD  . ARG A 1 391 ? 1.681   0.755  50.560  1.00 58.63 ? 391 ARG A CD  1 
ATOM   3326 N NE  . ARG A 1 391 ? 2.423   -0.051 51.530  1.00 64.88 ? 391 ARG A NE  1 
ATOM   3327 C CZ  . ARG A 1 391 ? 2.009   -1.219 52.012  1.00 66.90 ? 391 ARG A CZ  1 
ATOM   3328 N NH1 . ARG A 1 391 ? 0.851   -1.728 51.612  1.00 67.63 ? 391 ARG A NH1 1 
ATOM   3329 N NH2 . ARG A 1 391 ? 2.752   -1.879 52.893  1.00 66.05 ? 391 ARG A NH2 1 
ATOM   3330 N N   . LYS A 1 392 ? 2.007   5.861  47.359  1.00 30.74 ? 392 LYS A N   1 
ATOM   3331 C CA  . LYS A 1 392 ? 1.674   6.518  46.106  1.00 28.61 ? 392 LYS A CA  1 
ATOM   3332 C C   . LYS A 1 392 ? 2.939   6.729  45.274  1.00 26.43 ? 392 LYS A C   1 
ATOM   3333 O O   . LYS A 1 392 ? 3.976   7.158  45.787  1.00 24.13 ? 392 LYS A O   1 
ATOM   3334 C CB  . LYS A 1 392 ? 0.955   7.837  46.385  1.00 34.80 ? 392 LYS A CB  1 
ATOM   3335 C CG  . LYS A 1 392 ? 0.387   8.485  45.161  1.00 39.60 ? 392 LYS A CG  1 
ATOM   3336 C CD  . LYS A 1 392 ? -0.843  7.769  44.627  1.00 44.96 ? 392 LYS A CD  1 
ATOM   3337 C CE  . LYS A 1 392 ? -2.130  8.261  45.235  1.00 44.85 ? 392 LYS A CE  1 
ATOM   3338 N NZ  . LYS A 1 392 ? -3.267  7.689  44.449  1.00 47.51 ? 392 LYS A NZ  1 
ATOM   3339 N N   . GLU A 1 393 ? 2.863   6.386  43.990  1.00 25.85 ? 393 GLU A N   1 
ATOM   3340 C CA  . GLU A 1 393 ? 4.022   6.340  43.114  1.00 33.54 ? 393 GLU A CA  1 
ATOM   3341 C C   . GLU A 1 393 ? 4.253   7.633  42.348  1.00 30.47 ? 393 GLU A C   1 
ATOM   3342 O O   . GLU A 1 393 ? 5.399   7.938  42.005  1.00 37.74 ? 393 GLU A O   1 
ATOM   3343 C CB  . GLU A 1 393 ? 3.875   5.178  42.118  1.00 49.59 ? 393 GLU A CB  1 
ATOM   3344 C CG  . GLU A 1 393 ? 2.546   5.170  41.342  1.00 66.62 ? 393 GLU A CG  1 
ATOM   3345 C CD  . GLU A 1 393 ? 1.314   4.996  42.238  1.00 77.78 ? 393 GLU A CD  1 
ATOM   3346 O OE1 . GLU A 1 393 ? 0.374   5.815  42.126  1.00 80.44 ? 393 GLU A OE1 1 
ATOM   3347 O OE2 . GLU A 1 393 ? 1.305   4.070  43.078  1.00 80.93 ? 393 GLU A OE2 1 
ATOM   3348 N N   . ASP A 1 394 ? 3.199   8.390  42.057  1.00 29.55 ? 394 ASP A N   1 
ATOM   3349 C CA  . ASP A 1 394 ? 3.306   9.594  41.231  1.00 32.97 ? 394 ASP A CA  1 
ATOM   3350 C C   . ASP A 1 394 ? 3.467   10.851 42.082  1.00 29.38 ? 394 ASP A C   1 
ATOM   3351 O O   . ASP A 1 394 ? 2.774   11.847 41.904  1.00 29.90 ? 394 ASP A O   1 
ATOM   3352 C CB  . ASP A 1 394 ? 2.095   9.698  40.305  1.00 38.68 ? 394 ASP A CB  1 
ATOM   3353 C CG  . ASP A 1 394 ? 0.777   9.412  41.024  1.00 49.95 ? 394 ASP A CG  1 
ATOM   3354 O OD1 . ASP A 1 394 ? 0.817   8.979  42.191  1.00 50.98 ? 394 ASP A OD1 1 
ATOM   3355 O OD2 . ASP A 1 394 ? -0.303  9.625  40.424  1.00 51.25 ? 394 ASP A OD2 1 
ATOM   3356 N N   . VAL A 1 395 ? 4.416   10.808 43.014  1.00 27.05 ? 395 VAL A N   1 
ATOM   3357 C CA  . VAL A 1 395 ? 4.741   11.938 43.876  1.00 26.59 ? 395 VAL A CA  1 
ATOM   3358 C C   . VAL A 1 395 ? 6.248   12.156 43.818  1.00 30.92 ? 395 VAL A C   1 
ATOM   3359 O O   . VAL A 1 395 ? 7.000   11.318 43.320  1.00 34.24 ? 395 VAL A O   1 
ATOM   3360 C CB  . VAL A 1 395 ? 4.279   11.723 45.329  1.00 24.58 ? 395 VAL A CB  1 
ATOM   3361 C CG1 . VAL A 1 395 ? 2.792   11.359 45.382  1.00 23.50 ? 395 VAL A CG1 1 
ATOM   3362 C CG2 . VAL A 1 395 ? 5.127   10.663 46.007  1.00 29.41 ? 395 VAL A CG2 1 
ATOM   3363 N N   . LYS A 1 396 ? 6.688   13.310 44.312  1.00 23.77 ? 396 LYS A N   1 
ATOM   3364 C CA  . LYS A 1 396 ? 8.114   13.589 44.373  1.00 24.75 ? 396 LYS A CA  1 
ATOM   3365 C C   . LYS A 1 396 ? 8.677   13.156 45.716  1.00 28.91 ? 396 LYS A C   1 
ATOM   3366 O O   . LYS A 1 396 ? 7.993   13.197 46.747  1.00 24.01 ? 396 LYS A O   1 
ATOM   3367 C CB  . LYS A 1 396 ? 8.404   15.070 44.137  1.00 29.36 ? 396 LYS A CB  1 
ATOM   3368 C CG  . LYS A 1 396 ? 7.970   15.536 42.774  1.00 39.56 ? 396 LYS A CG  1 
ATOM   3369 C CD  . LYS A 1 396 ? 8.782   14.938 41.636  1.00 44.46 ? 396 LYS A CD  1 
ATOM   3370 C CE  . LYS A 1 396 ? 10.096  15.662 41.429  1.00 49.22 ? 396 LYS A CE  1 
ATOM   3371 N NZ  . LYS A 1 396 ? 10.751  15.190 40.175  1.00 52.92 ? 396 LYS A NZ  1 
ATOM   3372 N N   . THR A 1 397 ? 9.928   12.707 45.690  1.00 26.01 ? 397 THR A N   1 
ATOM   3373 C CA  . THR A 1 397 ? 10.583  12.194 46.879  1.00 24.66 ? 397 THR A CA  1 
ATOM   3374 C C   . THR A 1 397 ? 11.972  12.806 47.015  1.00 27.50 ? 397 THR A C   1 
ATOM   3375 O O   . THR A 1 397 ? 12.550  13.317 46.048  1.00 27.07 ? 397 THR A O   1 
ATOM   3376 C CB  . THR A 1 397 ? 10.686  10.665 46.851  1.00 26.62 ? 397 THR A CB  1 
ATOM   3377 O OG1 . THR A 1 397 ? 11.504  10.277 45.749  1.00 28.76 ? 397 THR A OG1 1 
ATOM   3378 C CG2 . THR A 1 397 ? 9.306   10.024 46.698  1.00 29.14 ? 397 THR A CG2 1 
ATOM   3379 N N   . GLU A 1 398 ? 12.497  12.748 48.240  1.00 25.72 ? 398 GLU A N   1 
ATOM   3380 C CA  . GLU A 1 398 ? 13.821  13.272 48.559  1.00 29.90 ? 398 GLU A CA  1 
ATOM   3381 C C   . GLU A 1 398 ? 14.394  12.470 49.715  1.00 26.08 ? 398 GLU A C   1 
ATOM   3382 O O   . GLU A 1 398 ? 13.655  11.981 50.573  1.00 23.34 ? 398 GLU A O   1 
ATOM   3383 C CB  . GLU A 1 398 ? 13.765  14.762 48.931  1.00 33.08 ? 398 GLU A CB  1 
ATOM   3384 C CG  . GLU A 1 398 ? 15.120  15.415 49.152  1.00 41.81 ? 398 GLU A CG  1 
ATOM   3385 C CD  . GLU A 1 398 ? 15.903  15.589 47.867  1.00 49.58 ? 398 GLU A CD  1 
ATOM   3386 O OE1 . GLU A 1 398 ? 15.281  15.830 46.812  1.00 53.36 ? 398 GLU A OE1 1 
ATOM   3387 O OE2 . GLU A 1 398 ? 17.143  15.469 47.910  1.00 53.85 ? 398 GLU A OE2 1 
ATOM   3388 N N   . VAL A 1 399 ? 15.715  12.339 49.743  1.00 26.28 ? 399 VAL A N   1 
ATOM   3389 C CA  . VAL A 1 399 ? 16.398  11.660 50.837  1.00 29.61 ? 399 VAL A CA  1 
ATOM   3390 C C   . VAL A 1 399 ? 16.894  12.707 51.830  1.00 29.00 ? 399 VAL A C   1 
ATOM   3391 O O   . VAL A 1 399 ? 17.309  13.803 51.440  1.00 34.15 ? 399 VAL A O   1 
ATOM   3392 C CB  . VAL A 1 399 ? 17.545  10.781 50.304  1.00 33.65 ? 399 VAL A CB  1 
ATOM   3393 C CG1 . VAL A 1 399 ? 18.379  10.217 51.442  1.00 33.32 ? 399 VAL A CG1 1 
ATOM   3394 C CG2 . VAL A 1 399 ? 16.977  9.648  49.450  1.00 34.42 ? 399 VAL A CG2 1 
ATOM   3395 N N   . ILE A 1 400 ? 16.822  12.385 53.120  1.00 22.98 ? 400 ILE A N   1 
ATOM   3396 C CA  . ILE A 1 400 ? 17.332  13.253 54.175  1.00 25.30 ? 400 ILE A CA  1 
ATOM   3397 C C   . ILE A 1 400 ? 18.235  12.411 55.070  1.00 28.04 ? 400 ILE A C   1 
ATOM   3398 O O   . ILE A 1 400 ? 17.915  11.259 55.384  1.00 27.33 ? 400 ILE A O   1 
ATOM   3399 C CB  . ILE A 1 400 ? 16.183  13.937 54.962  1.00 26.04 ? 400 ILE A CB  1 
ATOM   3400 C CG1 . ILE A 1 400 ? 16.711  14.879 56.037  1.00 29.54 ? 400 ILE A CG1 1 
ATOM   3401 C CG2 . ILE A 1 400 ? 15.240  12.936 55.602  1.00 23.27 ? 400 ILE A CG2 1 
ATOM   3402 C CD1 . ILE A 1 400 ? 15.609  15.727 56.658  1.00 30.48 ? 400 ILE A CD1 1 
ATOM   3403 N N   . GLU A 1 401 ? 19.390  12.970 55.442  1.00 19.96 ? 401 GLU A N   1 
ATOM   3404 C CA  . GLU A 1 401 ? 20.403  12.227 56.182  1.00 20.74 ? 401 GLU A CA  1 
ATOM   3405 C C   . GLU A 1 401 ? 20.440  12.560 57.664  1.00 24.81 ? 401 GLU A C   1 
ATOM   3406 O O   . GLU A 1 401 ? 21.018  11.791 58.445  1.00 24.05 ? 401 GLU A O   1 
ATOM   3407 C CB  . GLU A 1 401 ? 21.794  12.493 55.585  1.00 22.80 ? 401 GLU A CB  1 
ATOM   3408 C CG  . GLU A 1 401 ? 21.967  11.951 54.177  1.00 34.78 ? 401 GLU A CG  1 
ATOM   3409 C CD  . GLU A 1 401 ? 21.921  10.431 54.134  1.00 47.61 ? 401 GLU A CD  1 
ATOM   3410 O OE1 . GLU A 1 401 ? 22.394  9.788  55.097  1.00 49.94 ? 401 GLU A OE1 1 
ATOM   3411 O OE2 . GLU A 1 401 ? 21.408  9.878  53.137  1.00 51.65 ? 401 GLU A OE2 1 
ATOM   3412 N N   . SER A 1 402 ? 19.841  13.675 58.066  1.00 18.32 ? 402 SER A N   1 
ATOM   3413 C CA  . SER A 1 402 ? 19.942  14.116 59.446  1.00 19.37 ? 402 SER A CA  1 
ATOM   3414 C C   . SER A 1 402 ? 18.832  15.117 59.716  1.00 19.41 ? 402 SER A C   1 
ATOM   3415 O O   . SER A 1 402 ? 18.483  15.914 58.840  1.00 20.47 ? 402 SER A O   1 
ATOM   3416 C CB  . SER A 1 402 ? 21.316  14.751 59.708  1.00 22.69 ? 402 SER A CB  1 
ATOM   3417 O OG  . SER A 1 402 ? 21.424  15.184 61.057  1.00 26.09 ? 402 SER A OG  1 
ATOM   3418 N N   . VAL A 1 403 ? 18.271  15.062 60.919  1.00 17.50 ? 403 VAL A N   1 
ATOM   3419 C CA  . VAL A 1 403 ? 17.324  16.072 61.361  1.00 19.24 ? 403 VAL A CA  1 
ATOM   3420 C C   . VAL A 1 403 ? 17.890  16.751 62.596  1.00 21.42 ? 403 VAL A C   1 
ATOM   3421 O O   . VAL A 1 403 ? 18.684  16.173 63.346  1.00 18.07 ? 403 VAL A O   1 
ATOM   3422 C CB  . VAL A 1 403 ? 15.920  15.496 61.650  1.00 16.10 ? 403 VAL A CB  1 
ATOM   3423 C CG1 . VAL A 1 403 ? 15.331  14.869 60.372  1.00 14.77 ? 403 VAL A CG1 1 
ATOM   3424 C CG2 . VAL A 1 403 ? 15.959  14.504 62.829  1.00 19.51 ? 403 VAL A CG2 1 
ATOM   3425 N N   . LYS A 1 404 ? 17.496  18.006 62.783  1.00 15.94 ? 404 LYS A N   1 
ATOM   3426 C CA  . LYS A 1 404 ? 17.797  18.737 64.002  1.00 16.32 ? 404 LYS A CA  1 
ATOM   3427 C C   . LYS A 1 404 ? 16.660  18.482 64.986  1.00 14.76 ? 404 LYS A C   1 
ATOM   3428 O O   . LYS A 1 404 ? 15.490  18.756 64.683  1.00 14.78 ? 404 LYS A O   1 
ATOM   3429 C CB  . LYS A 1 404 ? 17.979  20.224 63.700  1.00 18.84 ? 404 LYS A CB  1 
ATOM   3430 C CG  . LYS A 1 404 ? 18.436  21.047 64.884  1.00 28.99 ? 404 LYS A CG  1 
ATOM   3431 C CD  . LYS A 1 404 ? 18.657  22.492 64.486  1.00 31.29 ? 404 LYS A CD  1 
ATOM   3432 C CE  . LYS A 1 404 ? 19.914  22.648 63.650  1.00 37.27 ? 404 LYS A CE  1 
ATOM   3433 N NZ  . LYS A 1 404 ? 20.127  24.082 63.328  1.00 45.55 ? 404 LYS A NZ  1 
ATOM   3434 N N   . ALA A 1 405 ? 17.001  17.930 66.143  1.00 12.39 ? 405 ALA A N   1 
ATOM   3435 C CA  . ALA A 1 405 ? 15.983  17.442 67.063  1.00 15.21 ? 405 ALA A CA  1 
ATOM   3436 C C   . ALA A 1 405 ? 15.063  18.576 67.507  1.00 13.56 ? 405 ALA A C   1 
ATOM   3437 O O   . ALA A 1 405 ? 15.521  19.678 67.787  1.00 13.93 ? 405 ALA A O   1 
ATOM   3438 C CB  . ALA A 1 405 ? 16.656  16.795 68.280  1.00 13.97 ? 405 ALA A CB  1 
ATOM   3439 N N   . GLY A 1 406 ? 13.765  18.310 67.577  1.00 11.79 ? 406 GLY A N   1 
ATOM   3440 C CA  . GLY A 1 406 ? 12.854  19.329 68.062  1.00 16.40 ? 406 GLY A CA  1 
ATOM   3441 C C   . GLY A 1 406 ? 11.432  18.821 68.167  1.00 16.55 ? 406 GLY A C   1 
ATOM   3442 O O   . GLY A 1 406 ? 11.191  17.618 68.140  1.00 13.04 ? 406 GLY A O   1 
ATOM   3443 N N   . THR A 1 407 ? 10.490  19.765 68.279  1.00 12.53 ? 407 THR A N   1 
ATOM   3444 C CA  . THR A 1 407 ? 9.055   19.485 68.356  1.00 13.10 ? 407 THR A CA  1 
ATOM   3445 C C   . THR A 1 407 ? 8.321   20.469 67.455  1.00 15.27 ? 407 THR A C   1 
ATOM   3446 O O   . THR A 1 407 ? 8.913   21.421 66.938  1.00 15.70 ? 407 THR A O   1 
ATOM   3447 C CB  . THR A 1 407 ? 8.504   19.643 69.786  1.00 10.03 ? 407 THR A CB  1 
ATOM   3448 O OG1 . THR A 1 407 ? 8.426   21.051 70.083  1.00 11.57 ? 407 THR A OG1 1 
ATOM   3449 C CG2 . THR A 1 407 ? 9.400   18.977 70.810  1.00 9.27  ? 407 THR A CG2 1 
ATOM   3450 N N   . TRP A 1 408 ? 6.991   20.272 67.305  1.00 13.65 ? 408 TRP A N   1 
ATOM   3451 C CA  . TRP A 1 408 ? 6.275   21.274 66.531  1.00 12.71 ? 408 TRP A CA  1 
ATOM   3452 C C   . TRP A 1 408 ? 6.044   22.551 67.311  1.00 14.91 ? 408 TRP A C   1 
ATOM   3453 O O   . TRP A 1 408 ? 5.355   23.480 66.855  1.00 17.76 ? 408 TRP A O   1 
ATOM   3454 C CB  . TRP A 1 408 ? 4.919   20.780 66.032  1.00 11.82 ? 408 TRP A CB  1 
ATOM   3455 C CG  . TRP A 1 408 ? 3.972   20.185 67.041  1.00 15.08 ? 408 TRP A CG  1 
ATOM   3456 C CD1 . TRP A 1 408 ? 4.034   20.244 68.408  1.00 16.61 ? 408 TRP A CD1 1 
ATOM   3457 C CD2 . TRP A 1 408 ? 2.730   19.552 66.723  1.00 14.73 ? 408 TRP A CD2 1 
ATOM   3458 N NE1 . TRP A 1 408 ? 2.934   19.628 68.957  1.00 15.24 ? 408 TRP A NE1 1 
ATOM   3459 C CE2 . TRP A 1 408 ? 2.112   19.204 67.941  1.00 14.74 ? 408 TRP A CE2 1 
ATOM   3460 C CE3 . TRP A 1 408 ? 2.089   19.233 65.524  1.00 15.72 ? 408 TRP A CE3 1 
ATOM   3461 C CZ2 . TRP A 1 408 ? 0.884   18.549 67.990  1.00 14.17 ? 408 TRP A CZ2 1 
ATOM   3462 C CZ3 . TRP A 1 408 ? 0.868   18.578 65.572  1.00 13.61 ? 408 TRP A CZ3 1 
ATOM   3463 C CH2 . TRP A 1 408 ? 0.282   18.242 66.799  1.00 12.65 ? 408 TRP A CH2 1 
ATOM   3464 N N   . PHE A 1 409 ? 6.584   22.712 68.506  1.00 13.70 ? 409 PHE A N   1 
ATOM   3465 C CA  . PHE A 1 409 ? 6.459   23.970 69.205  1.00 19.11 ? 409 PHE A CA  1 
ATOM   3466 C C   . PHE A 1 409 ? 7.809   24.684 69.086  1.00 18.26 ? 409 PHE A C   1 
ATOM   3467 O O   . PHE A 1 409 ? 8.761   24.360 69.801  1.00 17.88 ? 409 PHE A O   1 
ATOM   3468 C CB  . PHE A 1 409 ? 5.992   23.751 70.636  1.00 24.82 ? 409 PHE A CB  1 
ATOM   3469 C CG  . PHE A 1 409 ? 5.255   24.906 71.204  1.00 37.66 ? 409 PHE A CG  1 
ATOM   3470 C CD1 . PHE A 1 409 ? 5.900   26.114 71.431  1.00 44.72 ? 409 PHE A CD1 1 
ATOM   3471 C CD2 . PHE A 1 409 ? 3.893   24.827 71.408  1.00 43.02 ? 409 PHE A CD2 1 
ATOM   3472 C CE1 . PHE A 1 409 ? 5.201   27.202 71.945  1.00 50.73 ? 409 PHE A CE1 1 
ATOM   3473 C CE2 . PHE A 1 409 ? 3.188   25.895 71.889  1.00 47.99 ? 409 PHE A CE2 1 
ATOM   3474 C CZ  . PHE A 1 409 ? 3.829   27.089 72.159  1.00 49.41 ? 409 PHE A CZ  1 
ATOM   3475 N N   . ASP A 1 410 ? 7.897   25.615 68.124  1.00 17.89 ? 410 ASP A N   1 
ATOM   3476 C CA  . ASP A 1 410 ? 9.083   26.417 67.843  1.00 25.01 ? 410 ASP A CA  1 
ATOM   3477 C C   . ASP A 1 410 ? 10.289  25.577 67.435  1.00 25.29 ? 410 ASP A C   1 
ATOM   3478 O O   . ASP A 1 410 ? 11.419  26.085 67.436  1.00 25.06 ? 410 ASP A O   1 
ATOM   3479 C CB  . ASP A 1 410 ? 9.462   27.310 69.034  1.00 27.75 ? 410 ASP A CB  1 
ATOM   3480 C CG  . ASP A 1 410 ? 8.376   28.308 69.394  1.00 39.16 ? 410 ASP A CG  1 
ATOM   3481 O OD1 . ASP A 1 410 ? 7.570   28.667 68.501  1.00 39.39 ? 410 ASP A OD1 1 
ATOM   3482 O OD2 . ASP A 1 410 ? 8.329   28.740 70.563  1.00 40.56 ? 410 ASP A OD2 1 
ATOM   3483 N N   . GLY A 1 411 ? 10.096  24.304 67.112  1.00 18.50 ? 411 GLY A N   1 
ATOM   3484 C CA  . GLY A 1 411 ? 11.205  23.443 66.748  1.00 16.30 ? 411 GLY A CA  1 
ATOM   3485 C C   . GLY A 1 411 ? 12.141  23.083 67.888  1.00 15.20 ? 411 GLY A C   1 
ATOM   3486 O O   . GLY A 1 411 ? 13.267  22.655 67.633  1.00 19.23 ? 411 GLY A O   1 
ATOM   3487 N N   . ASN A 1 412 ? 11.709  23.236 69.144  1.00 14.65 ? 412 ASN A N   1 
ATOM   3488 C CA  . ASN A 1 412 ? 12.581  22.973 70.286  1.00 14.92 ? 412 ASN A CA  1 
ATOM   3489 C C   . ASN A 1 412 ? 11.756  22.403 71.436  1.00 15.88 ? 412 ASN A C   1 
ATOM   3490 O O   . ASN A 1 412 ? 10.557  22.133 71.295  1.00 13.96 ? 412 ASN A O   1 
ATOM   3491 C CB  . ASN A 1 412 ? 13.356  24.237 70.659  1.00 13.52 ? 412 ASN A CB  1 
ATOM   3492 C CG  . ASN A 1 412 ? 12.483  25.349 71.235  1.00 21.13 ? 412 ASN A CG  1 
ATOM   3493 O OD1 . ASN A 1 412 ? 11.581  25.120 72.049  1.00 16.53 ? 412 ASN A OD1 1 
ATOM   3494 N ND2 . ASN A 1 412 ? 12.758  26.585 70.798  1.00 19.07 ? 412 ASN A ND2 1 
ATOM   3495 N N   . PHE A 1 413 ? 12.415  22.215 72.584  1.00 12.50 ? 413 PHE A N   1 
ATOM   3496 C CA  . PHE A 1 413 ? 11.847  21.467 73.707  1.00 15.38 ? 413 PHE A CA  1 
ATOM   3497 C C   . PHE A 1 413 ? 11.507  22.341 74.917  1.00 13.84 ? 413 PHE A C   1 
ATOM   3498 O O   . PHE A 1 413 ? 11.212  21.800 75.993  1.00 11.47 ? 413 PHE A O   1 
ATOM   3499 C CB  . PHE A 1 413 ? 12.823  20.360 74.132  1.00 10.87 ? 413 PHE A CB  1 
ATOM   3500 C CG  . PHE A 1 413 ? 12.990  19.272 73.108  1.00 13.49 ? 413 PHE A CG  1 
ATOM   3501 C CD1 . PHE A 1 413 ? 12.096  18.213 73.052  1.00 15.75 ? 413 PHE A CD1 1 
ATOM   3502 C CD2 . PHE A 1 413 ? 14.045  19.314 72.191  1.00 13.85 ? 413 PHE A CD2 1 
ATOM   3503 C CE1 . PHE A 1 413 ? 12.242  17.214 72.095  1.00 12.64 ? 413 PHE A CE1 1 
ATOM   3504 C CE2 . PHE A 1 413 ? 14.210  18.313 71.240  1.00 12.38 ? 413 PHE A CE2 1 
ATOM   3505 C CZ  . PHE A 1 413 ? 13.294  17.261 71.183  1.00 11.23 ? 413 PHE A CZ  1 
ATOM   3506 N N   . LEU A 1 414 ? 11.521  23.673 74.772  1.00 13.42 ? 414 LEU A N   1 
ATOM   3507 C CA  . LEU A 1 414 ? 11.379  24.564 75.928  1.00 14.66 ? 414 LEU A CA  1 
ATOM   3508 C C   . LEU A 1 414 ? 10.001  24.500 76.600  1.00 15.94 ? 414 LEU A C   1 
ATOM   3509 O O   . LEU A 1 414 ? 9.872   24.941 77.745  1.00 14.20 ? 414 LEU A O   1 
ATOM   3510 C CB  . LEU A 1 414 ? 11.678  26.010 75.528  1.00 15.58 ? 414 LEU A CB  1 
ATOM   3511 C CG  . LEU A 1 414 ? 13.103  26.294 75.048  1.00 18.85 ? 414 LEU A CG  1 
ATOM   3512 C CD1 . LEU A 1 414 ? 13.266  27.776 74.661  1.00 24.57 ? 414 LEU A CD1 1 
ATOM   3513 C CD2 . LEU A 1 414 ? 14.103  25.914 76.119  1.00 21.05 ? 414 LEU A CD2 1 
ATOM   3514 N N   . LYS A 1 415 ? 8.995   23.959 75.941  1.00 15.22 ? 415 LYS A N   1 
ATOM   3515 C CA  . LYS A 1 415 ? 7.692   23.871 76.575  1.00 12.56 ? 415 LYS A CA  1 
ATOM   3516 C C   . LYS A 1 415 ? 7.635   22.762 77.654  1.00 16.53 ? 415 LYS A C   1 
ATOM   3517 O O   . LYS A 1 415 ? 6.713   22.722 78.412  1.00 12.87 ? 415 LYS A O   1 
ATOM   3518 C CB  . LYS A 1 415 ? 6.601   23.609 75.532  1.00 16.28 ? 415 LYS A CB  1 
ATOM   3519 C CG  . LYS A 1 415 ? 6.028   24.820 74.879  1.00 26.34 ? 415 LYS A CG  1 
ATOM   3520 C CD  . LYS A 1 415 ? 5.553   25.839 75.899  1.00 41.71 ? 415 LYS A CD  1 
ATOM   3521 C CE  . LYS A 1 415 ? 4.047   25.821 76.057  1.00 31.45 ? 415 LYS A CE  1 
ATOM   3522 N NZ  . LYS A 1 415 ? 3.448   26.596 77.196  1.00 28.41 ? 415 LYS A NZ  1 
ATOM   3523 N N   . TRP A 1 416 ? 8.658   21.906 77.705  1.00 14.38 ? 416 TRP A N   1 
ATOM   3524 C CA  . TRP A 1 416 ? 8.678   20.762 78.602  1.00 12.92 ? 416 TRP A CA  1 
ATOM   3525 C C   . TRP A 1 416 ? 9.913   20.688 79.479  1.00 10.06 ? 416 TRP A C   1 
ATOM   3526 O O   . TRP A 1 416 ? 9.950   19.843 80.379  1.00 11.50 ? 416 TRP A O   1 
ATOM   3527 C CB  . TRP A 1 416 ? 8.588   19.448 77.806  1.00 9.24  ? 416 TRP A CB  1 
ATOM   3528 C CG  . TRP A 1 416 ? 7.371   19.398 76.927  1.00 11.74 ? 416 TRP A CG  1 
ATOM   3529 C CD1 . TRP A 1 416 ? 6.129   18.923 77.258  1.00 11.00 ? 416 TRP A CD1 1 
ATOM   3530 C CD2 . TRP A 1 416 ? 7.283   19.866 75.582  1.00 11.02 ? 416 TRP A CD2 1 
ATOM   3531 N NE1 . TRP A 1 416 ? 5.274   19.066 76.185  1.00 9.83  ? 416 TRP A NE1 1 
ATOM   3532 C CE2 . TRP A 1 416 ? 5.959   19.643 75.146  1.00 12.12 ? 416 TRP A CE2 1 
ATOM   3533 C CE3 . TRP A 1 416 ? 8.202   20.437 74.694  1.00 15.72 ? 416 TRP A CE3 1 
ATOM   3534 C CZ2 . TRP A 1 416 ? 5.525   19.976 73.859  1.00 13.39 ? 416 TRP A CZ2 1 
ATOM   3535 C CZ3 . TRP A 1 416 ? 7.762   20.780 73.408  1.00 14.79 ? 416 TRP A CZ3 1 
ATOM   3536 C CH2 . TRP A 1 416 ? 6.440   20.538 73.008  1.00 16.60 ? 416 TRP A CH2 1 
ATOM   3537 N N   . ILE A 1 417 ? 10.938  21.494 79.221  1.00 11.20 ? 417 ILE A N   1 
ATOM   3538 C CA  . ILE A 1 417 ? 12.175  21.398 79.979  1.00 13.30 ? 417 ILE A CA  1 
ATOM   3539 C C   . ILE A 1 417 ? 12.854  22.751 79.888  1.00 16.18 ? 417 ILE A C   1 
ATOM   3540 O O   . ILE A 1 417 ? 12.637  23.507 78.933  1.00 16.13 ? 417 ILE A O   1 
ATOM   3541 C CB  . ILE A 1 417 ? 13.064  20.240 79.445  1.00 11.38 ? 417 ILE A CB  1 
ATOM   3542 C CG1 . ILE A 1 417 ? 14.137  19.849 80.467  1.00 14.67 ? 417 ILE A CG1 1 
ATOM   3543 C CG2 . ILE A 1 417 ? 13.707  20.584 78.089  1.00 12.40 ? 417 ILE A CG2 1 
ATOM   3544 C CD1 . ILE A 1 417 ? 14.758  18.482 80.168  1.00 14.52 ? 417 ILE A CD1 1 
ATOM   3545 N N   . GLY A 1 418 ? 13.638  23.086 80.909  1.00 16.45 ? 418 GLY A N   1 
ATOM   3546 C CA  . GLY A 1 418 ? 14.493  24.256 80.824  1.00 17.68 ? 418 GLY A CA  1 
ATOM   3547 C C   . GLY A 1 418 ? 14.141  25.442 81.696  1.00 28.73 ? 418 GLY A C   1 
ATOM   3548 O O   . GLY A 1 418 ? 14.867  26.440 81.653  1.00 38.27 ? 418 GLY A O   1 
ATOM   3549 N N   . ASN A 1 419 ? 13.063  25.402 82.470  1.00 28.10 ? 419 ASN A N   1 
ATOM   3550 C CA  . ASN A 1 419 ? 12.922  26.374 83.545  1.00 27.47 ? 419 ASN A CA  1 
ATOM   3551 C C   . ASN A 1 419 ? 12.905  25.619 84.867  1.00 26.46 ? 419 ASN A C   1 
ATOM   3552 O O   . ASN A 1 419 ? 12.843  24.387 84.892  1.00 22.49 ? 419 ASN A O   1 
ATOM   3553 C CB  . ASN A 1 419 ? 11.689  27.286 83.355  1.00 26.42 ? 419 ASN A CB  1 
ATOM   3554 C CG  . ASN A 1 419 ? 10.340  26.583 83.568  1.00 26.27 ? 419 ASN A CG  1 
ATOM   3555 O OD1 . ASN A 1 419 ? 10.249  25.473 84.081  1.00 29.58 ? 419 ASN A OD1 1 
ATOM   3556 N ND2 . ASN A 1 419 ? 9.273   27.273 83.176  1.00 28.02 ? 419 ASN A ND2 1 
ATOM   3557 N N   . LYS A 1 420 ? 12.991  26.364 85.972  1.00 20.07 ? 420 LYS A N   1 
ATOM   3558 C CA  . LYS A 1 420 ? 13.180  25.716 87.266  1.00 19.18 ? 420 LYS A CA  1 
ATOM   3559 C C   . LYS A 1 420 ? 12.041  24.754 87.594  1.00 24.63 ? 420 LYS A C   1 
ATOM   3560 O O   . LYS A 1 420 ? 12.281  23.655 88.108  1.00 20.50 ? 420 LYS A O   1 
ATOM   3561 C CB  . LYS A 1 420 ? 13.337  26.766 88.378  1.00 33.62 ? 420 LYS A CB  1 
ATOM   3562 C CG  . LYS A 1 420 ? 13.611  26.155 89.757  1.00 43.25 ? 420 LYS A CG  1 
ATOM   3563 C CD  . LYS A 1 420 ? 14.224  27.155 90.744  1.00 53.13 ? 420 LYS A CD  1 
ATOM   3564 C CE  . LYS A 1 420 ? 15.114  26.447 91.765  1.00 58.24 ? 420 LYS A CE  1 
ATOM   3565 N NZ  . LYS A 1 420 ? 15.388  25.025 91.387  1.00 56.51 ? 420 LYS A NZ  1 
ATOM   3566 N N   . GLU A 1 421 ? 10.796  25.133 87.282  1.00 21.60 ? 421 GLU A N   1 
ATOM   3567 C CA  . GLU A 1 421 ? 9.653   24.304 87.655  1.00 20.44 ? 421 GLU A CA  1 
ATOM   3568 C C   . GLU A 1 421 ? 9.571   23.051 86.789  1.00 19.94 ? 421 GLU A C   1 
ATOM   3569 O O   . GLU A 1 421 ? 9.373   21.940 87.299  1.00 18.33 ? 421 GLU A O   1 
ATOM   3570 C CB  . GLU A 1 421 ? 8.360   25.119 87.562  1.00 30.04 ? 421 GLU A CB  1 
ATOM   3571 C CG  . GLU A 1 421 ? 8.236   26.212 88.621  1.00 38.59 ? 421 GLU A CG  1 
ATOM   3572 C CD  . GLU A 1 421 ? 8.990   27.478 88.243  1.00 54.12 ? 421 GLU A CD  1 
ATOM   3573 O OE1 . GLU A 1 421 ? 9.429   27.593 87.075  1.00 56.66 ? 421 GLU A OE1 1 
ATOM   3574 O OE2 . GLU A 1 421 ? 9.161   28.351 89.120  1.00 61.46 ? 421 GLU A OE2 1 
ATOM   3575 N N   . LYS A 1 422 ? 9.710   23.206 85.471  1.00 19.54 ? 422 LYS A N   1 
ATOM   3576 C CA  . LYS A 1 422 ? 9.736   22.023 84.614  1.00 18.10 ? 422 LYS A CA  1 
ATOM   3577 C C   . LYS A 1 422 ? 10.931  21.137 84.955  1.00 18.22 ? 422 LYS A C   1 
ATOM   3578 O O   . LYS A 1 422 ? 10.810  19.905 84.983  1.00 15.10 ? 422 LYS A O   1 
ATOM   3579 C CB  . LYS A 1 422 ? 9.764   22.427 83.134  1.00 20.99 ? 422 LYS A CB  1 
ATOM   3580 C CG  . LYS A 1 422 ? 8.507   23.171 82.665  1.00 19.73 ? 422 LYS A CG  1 
ATOM   3581 C CD  . LYS A 1 422 ? 8.598   23.583 81.187  1.00 14.91 ? 422 LYS A CD  1 
ATOM   3582 C CE  . LYS A 1 422 ? 7.482   24.547 80.823  1.00 18.06 ? 422 LYS A CE  1 
ATOM   3583 N NZ  . LYS A 1 422 ? 6.128   23.918 80.956  1.00 17.30 ? 422 LYS A NZ  1 
ATOM   3584 N N   . ASN A 1 423 ? 12.097  21.743 85.220  1.00 19.85 ? 423 ASN A N   1 
ATOM   3585 C CA  . ASN A 1 423 ? 13.255  20.924 85.563  1.00 20.16 ? 423 ASN A CA  1 
ATOM   3586 C C   . ASN A 1 423 ? 13.040  20.180 86.874  1.00 20.64 ? 423 ASN A C   1 
ATOM   3587 O O   . ASN A 1 423 ? 13.566  19.073 87.049  1.00 16.82 ? 423 ASN A O   1 
ATOM   3588 C CB  . ASN A 1 423 ? 14.533  21.767 85.636  1.00 18.39 ? 423 ASN A CB  1 
ATOM   3589 C CG  . ASN A 1 423 ? 15.003  22.238 84.269  1.00 19.41 ? 423 ASN A CG  1 
ATOM   3590 O OD1 . ASN A 1 423 ? 14.498  21.784 83.243  1.00 18.88 ? 423 ASN A OD1 1 
ATOM   3591 N ND2 . ASN A 1 423 ? 16.025  23.099 84.252  1.00 19.90 ? 423 ASN A ND2 1 
ATOM   3592 N N   . GLU A 1 424 ? 12.267  20.757 87.801  1.00 18.25 ? 424 GLU A N   1 
ATOM   3593 C CA  . GLU A 1 424 ? 11.993  20.059 89.051  1.00 19.72 ? 424 GLU A CA  1 
ATOM   3594 C C   . GLU A 1 424 ? 11.213  18.771 88.802  1.00 13.04 ? 424 GLU A C   1 
ATOM   3595 O O   . GLU A 1 424 ? 11.489  17.745 89.436  1.00 17.27 ? 424 GLU A O   1 
ATOM   3596 C CB  . GLU A 1 424 ? 11.241  20.965 90.026  1.00 18.83 ? 424 GLU A CB  1 
ATOM   3597 C CG  . GLU A 1 424 ? 10.909  20.293 91.351  1.00 30.78 ? 424 GLU A CG  1 
ATOM   3598 C CD  . GLU A 1 424 ? 12.142  19.796 92.106  1.00 37.73 ? 424 GLU A CD  1 
ATOM   3599 O OE1 . GLU A 1 424 ? 13.257  20.329 91.889  1.00 36.89 ? 424 GLU A OE1 1 
ATOM   3600 O OE2 . GLU A 1 424 ? 11.989  18.866 92.927  1.00 38.69 ? 424 GLU A OE2 1 
ATOM   3601 N N   . TYR A 1 425 ? 10.243  18.799 87.873  1.00 14.19 ? 425 TYR A N   1 
ATOM   3602 C CA  . TYR A 1 425 ? 9.541   17.576 87.501  1.00 13.20 ? 425 TYR A CA  1 
ATOM   3603 C C   . TYR A 1 425 ? 10.493  16.528 86.938  1.00 14.11 ? 425 TYR A C   1 
ATOM   3604 O O   . TYR A 1 425 ? 10.380  15.335 87.260  1.00 13.42 ? 425 TYR A O   1 
ATOM   3605 C CB  . TYR A 1 425 ? 8.437   17.858 86.474  1.00 11.23 ? 425 TYR A CB  1 
ATOM   3606 C CG  . TYR A 1 425 ? 7.062   18.097 87.053  1.00 13.77 ? 425 TYR A CG  1 
ATOM   3607 C CD1 . TYR A 1 425 ? 6.888   18.580 88.348  1.00 14.11 ? 425 TYR A CD1 1 
ATOM   3608 C CD2 . TYR A 1 425 ? 5.924   17.778 86.314  1.00 16.16 ? 425 TYR A CD2 1 
ATOM   3609 C CE1 . TYR A 1 425 ? 5.614   18.783 88.875  1.00 15.65 ? 425 TYR A CE1 1 
ATOM   3610 C CE2 . TYR A 1 425 ? 4.653   17.982 86.831  1.00 14.70 ? 425 TYR A CE2 1 
ATOM   3611 C CZ  . TYR A 1 425 ? 4.505   18.477 88.109  1.00 18.87 ? 425 TYR A CZ  1 
ATOM   3612 O OH  . TYR A 1 425 ? 3.225   18.654 88.603  1.00 19.73 ? 425 TYR A OH  1 
ATOM   3613 N N   . TRP A 1 426 ? 11.412  16.934 86.056  1.00 12.43 ? 426 TRP A N   1 
ATOM   3614 C CA  . TRP A 1 426 ? 12.383  15.973 85.541  1.00 13.64 ? 426 TRP A CA  1 
ATOM   3615 C C   . TRP A 1 426 ? 13.259  15.432 86.668  1.00 14.77 ? 426 TRP A C   1 
ATOM   3616 O O   . TRP A 1 426 ? 13.565  14.234 86.709  1.00 12.62 ? 426 TRP A O   1 
ATOM   3617 C CB  . TRP A 1 426 ? 13.244  16.621 84.454  1.00 12.41 ? 426 TRP A CB  1 
ATOM   3618 C CG  . TRP A 1 426 ? 12.514  16.806 83.171  1.00 14.25 ? 426 TRP A CG  1 
ATOM   3619 C CD1 . TRP A 1 426 ? 12.002  17.971 82.667  1.00 9.95  ? 426 TRP A CD1 1 
ATOM   3620 C CD2 . TRP A 1 426 ? 12.196  15.779 82.222  1.00 13.86 ? 426 TRP A CD2 1 
ATOM   3621 N NE1 . TRP A 1 426 ? 11.390  17.728 81.453  1.00 11.88 ? 426 TRP A NE1 1 
ATOM   3622 C CE2 . TRP A 1 426 ? 11.502  16.393 81.158  1.00 12.37 ? 426 TRP A CE2 1 
ATOM   3623 C CE3 . TRP A 1 426 ? 12.452  14.403 82.161  1.00 15.71 ? 426 TRP A CE3 1 
ATOM   3624 C CZ2 . TRP A 1 426 ? 11.030  15.674 80.057  1.00 14.78 ? 426 TRP A CZ2 1 
ATOM   3625 C CZ3 . TRP A 1 426 ? 11.986  13.686 81.055  1.00 15.55 ? 426 TRP A CZ3 1 
ATOM   3626 C CH2 . TRP A 1 426 ? 11.284  14.327 80.026  1.00 16.44 ? 426 TRP A CH2 1 
ATOM   3627 N N   . LYS A 1 427 ? 13.672  16.300 87.598  1.00 11.86 ? 427 LYS A N   1 
ATOM   3628 C CA  . LYS A 1 427 ? 14.437  15.823 88.745  1.00 15.07 ? 427 LYS A CA  1 
ATOM   3629 C C   . LYS A 1 427 ? 13.663  14.785 89.544  1.00 14.69 ? 427 LYS A C   1 
ATOM   3630 O O   . LYS A 1 427 ? 14.221  13.753 89.935  1.00 15.13 ? 427 LYS A O   1 
ATOM   3631 C CB  . LYS A 1 427 ? 14.814  16.997 89.639  1.00 20.40 ? 427 LYS A CB  1 
ATOM   3632 C CG  . LYS A 1 427 ? 15.932  16.659 90.605  1.00 36.92 ? 427 LYS A CG  1 
ATOM   3633 C CD  . LYS A 1 427 ? 16.288  17.842 91.516  1.00 47.14 ? 427 LYS A CD  1 
ATOM   3634 C CE  . LYS A 1 427 ? 16.099  19.241 90.882  1.00 54.21 ? 427 LYS A CE  1 
ATOM   3635 N NZ  . LYS A 1 427 ? 16.534  19.439 89.461  1.00 58.60 ? 427 LYS A NZ  1 
ATOM   3636 N N   . ILE A 1 428 ? 12.376  15.045 89.794  1.00 13.48 ? 428 ILE A N   1 
ATOM   3637 C CA  . ILE A 1 428 ? 11.532  14.082 90.499  1.00 16.73 ? 428 ILE A CA  1 
ATOM   3638 C C   . ILE A 1 428 ? 11.455  12.768 89.729  1.00 16.49 ? 428 ILE A C   1 
ATOM   3639 O O   . ILE A 1 428 ? 11.575  11.678 90.309  1.00 15.25 ? 428 ILE A O   1 
ATOM   3640 C CB  . ILE A 1 428 ? 10.139  14.688 90.730  1.00 16.08 ? 428 ILE A CB  1 
ATOM   3641 C CG1 . ILE A 1 428 ? 10.225  15.814 91.759  1.00 19.69 ? 428 ILE A CG1 1 
ATOM   3642 C CG2 . ILE A 1 428 ? 9.118   13.621 91.133  1.00 19.25 ? 428 ILE A CG2 1 
ATOM   3643 C CD1 . ILE A 1 428 ? 8.983   16.674 91.799  1.00 19.83 ? 428 ILE A CD1 1 
ATOM   3644 N N   . LEU A 1 429 ? 11.248  12.855 88.412  1.00 13.67 ? 429 LEU A N   1 
ATOM   3645 C CA  . LEU A 1 429 ? 11.178  11.660 87.578  1.00 12.31 ? 429 LEU A CA  1 
ATOM   3646 C C   . LEU A 1 429 ? 12.496  10.892 87.593  1.00 14.46 ? 429 LEU A C   1 
ATOM   3647 O O   . LEU A 1 429 ? 12.509  9.656  87.690  1.00 15.06 ? 429 LEU A O   1 
ATOM   3648 C CB  . LEU A 1 429 ? 10.817  12.061 86.147  1.00 12.99 ? 429 LEU A CB  1 
ATOM   3649 C CG  . LEU A 1 429 ? 10.686  10.900 85.170  1.00 13.69 ? 429 LEU A CG  1 
ATOM   3650 C CD1 . LEU A 1 429 ? 9.415   10.143 85.466  1.00 16.88 ? 429 LEU A CD1 1 
ATOM   3651 C CD2 . LEU A 1 429 ? 10.684  11.406 83.712  1.00 15.52 ? 429 LEU A CD2 1 
ATOM   3652 N N   . ILE A 1 430 ? 13.615  11.608 87.483  1.00 15.94 ? 430 ILE A N   1 
ATOM   3653 C CA  . ILE A 1 430 ? 14.922  10.958 87.486  1.00 16.00 ? 430 ILE A CA  1 
ATOM   3654 C C   . ILE A 1 430 ? 15.129  10.195 88.789  1.00 16.90 ? 430 ILE A C   1 
ATOM   3655 O O   . ILE A 1 430 ? 15.557  9.032  88.788  1.00 15.83 ? 430 ILE A O   1 
ATOM   3656 C CB  . ILE A 1 430 ? 16.034  11.995 87.249  1.00 14.14 ? 430 ILE A CB  1 
ATOM   3657 C CG1 . ILE A 1 430 ? 16.025  12.465 85.792  1.00 11.65 ? 430 ILE A CG1 1 
ATOM   3658 C CG2 . ILE A 1 430 ? 17.385  11.437 87.642  1.00 18.32 ? 430 ILE A CG2 1 
ATOM   3659 C CD1 . ILE A 1 430 ? 16.714  13.823 85.613  1.00 16.65 ? 430 ILE A CD1 1 
ATOM   3660 N N   . GLU A 1 431 ? 14.830  10.842 89.920  1.00 14.94 ? 431 GLU A N   1 
ATOM   3661 C CA  . GLU A 1 431 ? 14.969  10.193 91.222  1.00 20.87 ? 431 GLU A CA  1 
ATOM   3662 C C   . GLU A 1 431 ? 14.060  8.976  91.333  1.00 21.68 ? 431 GLU A C   1 
ATOM   3663 O O   . GLU A 1 431 ? 14.475  7.915  91.824  1.00 19.41 ? 431 GLU A O   1 
ATOM   3664 C CB  . GLU A 1 431 ? 14.659  11.189 92.340  1.00 25.35 ? 431 GLU A CB  1 
ATOM   3665 C CG  . GLU A 1 431 ? 15.878  11.860 92.873  1.00 39.99 ? 431 GLU A CG  1 
ATOM   3666 C CD  . GLU A 1 431 ? 16.782  10.871 93.578  1.00 49.12 ? 431 GLU A CD  1 
ATOM   3667 O OE1 . GLU A 1 431 ? 16.264  9.878  94.127  1.00 54.91 ? 431 GLU A OE1 1 
ATOM   3668 O OE2 . GLU A 1 431 ? 18.010  11.076 93.567  1.00 55.82 ? 431 GLU A OE2 1 
ATOM   3669 N N   . ALA A 1 432 ? 12.805  9.119  90.903  1.00 18.39 ? 432 ALA A N   1 
ATOM   3670 C CA  . ALA A 1 432 ? 11.862  8.009  90.995  1.00 18.01 ? 432 ALA A CA  1 
ATOM   3671 C C   . ALA A 1 432 ? 12.296  6.852  90.111  1.00 14.31 ? 432 ALA A C   1 
ATOM   3672 O O   . ALA A 1 432 ? 12.149  5.686  90.489  1.00 18.18 ? 432 ALA A O   1 
ATOM   3673 C CB  . ALA A 1 432 ? 10.461  8.481  90.603  1.00 17.99 ? 432 ALA A CB  1 
ATOM   3674 N N   . LYS A 1 433 ? 12.855  7.158  88.933  1.00 16.83 ? 433 LYS A N   1 
ATOM   3675 C CA  . LYS A 1 433 ? 13.266  6.108  88.006  1.00 21.07 ? 433 LYS A CA  1 
ATOM   3676 C C   . LYS A 1 433 ? 14.326  5.204  88.627  1.00 22.64 ? 433 LYS A C   1 
ATOM   3677 O O   . LYS A 1 433 ? 14.297  3.982  88.438  1.00 18.92 ? 433 LYS A O   1 
ATOM   3678 C CB  . LYS A 1 433 ? 13.764  6.735  86.699  1.00 21.68 ? 433 LYS A CB  1 
ATOM   3679 C CG  . LYS A 1 433 ? 14.398  5.756  85.705  1.00 17.90 ? 433 LYS A CG  1 
ATOM   3680 C CD  . LYS A 1 433 ? 13.388  4.748  85.158  1.00 16.64 ? 433 LYS A CD  1 
ATOM   3681 C CE  . LYS A 1 433 ? 14.068  3.736  84.234  1.00 24.12 ? 433 LYS A CE  1 
ATOM   3682 N NZ  . LYS A 1 433 ? 13.113  2.692  83.772  1.00 20.37 ? 433 LYS A NZ  1 
ATOM   3683 N N   . LYS A 1 434 ? 15.254  5.781  89.399  1.00 20.77 ? 434 LYS A N   1 
ATOM   3684 C CA  . LYS A 1 434 ? 16.268  4.972  90.082  1.00 22.84 ? 434 LYS A CA  1 
ATOM   3685 C C   . LYS A 1 434 ? 15.651  3.871  90.931  1.00 25.31 ? 434 LYS A C   1 
ATOM   3686 O O   . LYS A 1 434 ? 16.272  2.824  91.141  1.00 27.64 ? 434 LYS A O   1 
ATOM   3687 C CB  . LYS A 1 434 ? 17.139  5.845  90.990  1.00 25.36 ? 434 LYS A CB  1 
ATOM   3688 C CG  . LYS A 1 434 ? 18.032  6.832  90.279  1.00 33.86 ? 434 LYS A CG  1 
ATOM   3689 C CD  . LYS A 1 434 ? 18.754  7.731  91.274  1.00 40.12 ? 434 LYS A CD  1 
ATOM   3690 C CE  . LYS A 1 434 ? 19.576  8.796  90.570  1.00 45.28 ? 434 LYS A CE  1 
ATOM   3691 N NZ  . LYS A 1 434 ? 20.217  9.716  91.549  1.00 47.35 ? 434 LYS A NZ  1 
ATOM   3692 N N   . LYS A 1 435 ? 14.447  4.100  91.443  1.00 21.33 ? 435 LYS A N   1 
ATOM   3693 C CA  . LYS A 1 435 ? 13.802  3.207  92.390  1.00 26.04 ? 435 LYS A CA  1 
ATOM   3694 C C   . LYS A 1 435 ? 12.518  2.621  91.828  1.00 24.39 ? 435 LYS A C   1 
ATOM   3695 O O   . LYS A 1 435 ? 11.723  2.064  92.591  1.00 25.07 ? 435 LYS A O   1 
ATOM   3696 C CB  . LYS A 1 435 ? 13.512  3.967  93.684  1.00 28.87 ? 435 LYS A CB  1 
ATOM   3697 C CG  . LYS A 1 435 ? 14.763  4.479  94.371  1.00 33.43 ? 435 LYS A CG  1 
ATOM   3698 C CD  . LYS A 1 435 ? 14.425  5.483  95.463  1.00 43.67 ? 435 LYS A CD  1 
ATOM   3699 C CE  . LYS A 1 435 ? 14.181  6.871  94.879  1.00 50.26 ? 435 LYS A CE  1 
ATOM   3700 N NZ  . LYS A 1 435 ? 15.450  7.476  94.361  1.00 57.33 ? 435 LYS A NZ  1 
ATOM   3701 N N   . ALA A 1 436 ? 12.278  2.763  90.526  1.00 20.91 ? 436 ALA A N   1 
ATOM   3702 C CA  . ALA A 1 436 ? 10.991  2.384  89.965  1.00 22.22 ? 436 ALA A CA  1 
ATOM   3703 C C   . ALA A 1 436 ? 10.845  0.868  89.933  1.00 22.86 ? 436 ALA A C   1 
ATOM   3704 O O   . ALA A 1 436 ? 11.812  0.134  89.709  1.00 23.45 ? 436 ALA A O   1 
ATOM   3705 C CB  . ALA A 1 436 ? 10.823  2.966  88.562  1.00 21.98 ? 436 ALA A CB  1 
ATOM   3706 N N   . LYS A 1 437 ? 9.627   0.396  90.181  1.00 19.69 ? 437 LYS A N   1 
ATOM   3707 C CA  . LYS A 1 437 ? 9.371   -1.033 90.251  1.00 26.54 ? 437 LYS A CA  1 
ATOM   3708 C C   . LYS A 1 437 ? 8.245   -1.485 89.330  1.00 24.94 ? 437 LYS A C   1 
ATOM   3709 O O   . LYS A 1 437 ? 8.004   -2.691 89.231  1.00 28.83 ? 437 LYS A O   1 
ATOM   3710 C CB  . LYS A 1 437 ? 9.062   -1.452 91.703  1.00 31.54 ? 437 LYS A CB  1 
ATOM   3711 C CG  . LYS A 1 437 ? 10.220  -1.241 92.688  1.00 39.79 ? 437 LYS A CG  1 
ATOM   3712 C CD  . LYS A 1 437 ? 11.265  -2.344 92.572  1.00 48.16 ? 437 LYS A CD  1 
ATOM   3713 C CE  . LYS A 1 437 ? 12.657  -1.887 93.019  1.00 55.13 ? 437 LYS A CE  1 
ATOM   3714 N NZ  . LYS A 1 437 ? 12.740  -1.469 94.444  1.00 58.06 ? 437 LYS A NZ  1 
ATOM   3715 N N   . ASN A 1 438 ? 7.575   -0.572 88.627  1.00 18.92 ? 438 ASN A N   1 
ATOM   3716 C CA  . ASN A 1 438 ? 6.431   -0.941 87.799  1.00 23.14 ? 438 ASN A CA  1 
ATOM   3717 C C   . ASN A 1 438 ? 6.208   0.129  86.740  1.00 25.60 ? 438 ASN A C   1 
ATOM   3718 O O   . ASN A 1 438 ? 6.867   1.175  86.736  1.00 20.29 ? 438 ASN A O   1 
ATOM   3719 C CB  . ASN A 1 438 ? 5.195   -1.162 88.670  1.00 20.70 ? 438 ASN A CB  1 
ATOM   3720 C CG  . ASN A 1 438 ? 4.715   0.102  89.352  1.00 23.83 ? 438 ASN A CG  1 
ATOM   3721 O OD1 . ASN A 1 438 ? 4.500   1.126  88.713  1.00 20.51 ? 438 ASN A OD1 1 
ATOM   3722 N ND2 . ASN A 1 438 ? 4.628   0.055  90.679  1.00 22.01 ? 438 ASN A ND2 1 
ATOM   3723 N N   . ASP A 1 439 ? 5.267   -0.146 85.834  1.00 21.67 ? 439 ASP A N   1 
ATOM   3724 C CA  . ASP A 1 439 ? 5.099   0.702  84.653  1.00 25.26 ? 439 ASP A CA  1 
ATOM   3725 C C   . ASP A 1 439 ? 4.430   2.045  84.942  1.00 21.09 ? 439 ASP A C   1 
ATOM   3726 O O   . ASP A 1 439 ? 4.245   2.847  84.014  1.00 18.78 ? 439 ASP A O   1 
ATOM   3727 C CB  . ASP A 1 439 ? 4.313   -0.041 83.565  1.00 26.02 ? 439 ASP A CB  1 
ATOM   3728 C CG  . ASP A 1 439 ? 5.153   -1.089 82.859  1.00 33.82 ? 439 ASP A CG  1 
ATOM   3729 O OD1 . ASP A 1 439 ? 6.396   -1.026 82.984  1.00 33.81 ? 439 ASP A OD1 1 
ATOM   3730 O OD2 . ASP A 1 439 ? 4.578   -1.947 82.156  1.00 34.97 ? 439 ASP A OD2 1 
ATOM   3731 N N   . TYR A 1 440 ? 4.073   2.348  86.191  1.00 15.87 ? 440 TYR A N   1 
ATOM   3732 C CA  . TYR A 1 440 ? 3.622   3.709  86.436  1.00 13.28 ? 440 TYR A CA  1 
ATOM   3733 C C   . TYR A 1 440 ? 4.730   4.723  86.168  1.00 16.90 ? 440 TYR A C   1 
ATOM   3734 O O   . TYR A 1 440 ? 4.433   5.893  85.913  1.00 15.20 ? 440 TYR A O   1 
ATOM   3735 C CB  . TYR A 1 440 ? 3.059   3.849  87.859  1.00 13.52 ? 440 TYR A CB  1 
ATOM   3736 C CG  . TYR A 1 440 ? 1.590   3.488  87.929  1.00 19.42 ? 440 TYR A CG  1 
ATOM   3737 C CD1 . TYR A 1 440 ? 0.632   4.341  87.384  1.00 20.80 ? 440 TYR A CD1 1 
ATOM   3738 C CD2 . TYR A 1 440 ? 1.158   2.293  88.492  1.00 26.08 ? 440 TYR A CD2 1 
ATOM   3739 C CE1 . TYR A 1 440 ? -0.708  4.034  87.423  1.00 24.04 ? 440 TYR A CE1 1 
ATOM   3740 C CE2 . TYR A 1 440 ? -0.199  1.973  88.531  1.00 26.96 ? 440 TYR A CE2 1 
ATOM   3741 C CZ  . TYR A 1 440 ? -1.122  2.859  87.986  1.00 27.65 ? 440 TYR A CZ  1 
ATOM   3742 O OH  . TYR A 1 440 ? -2.476  2.601  88.001  1.00 29.11 ? 440 TYR A OH  1 
ATOM   3743 N N   . ILE A 1 441 ? 5.999   4.299  86.152  1.00 12.43 ? 441 ILE A N   1 
ATOM   3744 C CA  . ILE A 1 441 ? 7.043   5.245  85.769  1.00 12.74 ? 441 ILE A CA  1 
ATOM   3745 C C   . ILE A 1 441 ? 6.861   5.668  84.319  1.00 16.79 ? 441 ILE A C   1 
ATOM   3746 O O   . ILE A 1 441 ? 7.185   6.803  83.954  1.00 13.66 ? 441 ILE A O   1 
ATOM   3747 C CB  . ILE A 1 441 ? 8.449   4.656  86.027  1.00 11.56 ? 441 ILE A CB  1 
ATOM   3748 C CG1 . ILE A 1 441 ? 9.492   5.781  86.063  1.00 16.92 ? 441 ILE A CG1 1 
ATOM   3749 C CG2 . ILE A 1 441 ? 8.825   3.596  84.978  1.00 12.73 ? 441 ILE A CG2 1 
ATOM   3750 C CD1 . ILE A 1 441 ? 9.324   6.727  87.266  1.00 15.23 ? 441 ILE A CD1 1 
ATOM   3751 N N   . LEU A 1 442 ? 6.311   4.785  83.474  1.00 12.34 ? 442 LEU A N   1 
ATOM   3752 C CA  . LEU A 1 442 ? 6.044   5.163  82.089  1.00 12.31 ? 442 LEU A CA  1 
ATOM   3753 C C   . LEU A 1 442 ? 4.933   6.194  82.009  1.00 13.00 ? 442 LEU A C   1 
ATOM   3754 O O   . LEU A 1 442 ? 4.994   7.115  81.185  1.00 13.24 ? 442 LEU A O   1 
ATOM   3755 C CB  . LEU A 1 442 ? 5.664   3.933  81.265  1.00 13.04 ? 442 LEU A CB  1 
ATOM   3756 C CG  . LEU A 1 442 ? 6.690   2.802  81.268  1.00 15.64 ? 442 LEU A CG  1 
ATOM   3757 C CD1 . LEU A 1 442 ? 6.187   1.680  80.366  1.00 13.95 ? 442 LEU A CD1 1 
ATOM   3758 C CD2 . LEU A 1 442 ? 8.072   3.289  80.831  1.00 16.91 ? 442 LEU A CD2 1 
ATOM   3759 N N   . VAL A 1 443 ? 3.897   6.035  82.839  1.00 12.98 ? 443 VAL A N   1 
ATOM   3760 C CA  . VAL A 1 443 ? 2.815   7.015  82.885  1.00 8.63  ? 443 VAL A CA  1 
ATOM   3761 C C   . VAL A 1 443 ? 3.372   8.396  83.186  1.00 13.57 ? 443 VAL A C   1 
ATOM   3762 O O   . VAL A 1 443 ? 2.976   9.394  82.561  1.00 11.36 ? 443 VAL A O   1 
ATOM   3763 C CB  . VAL A 1 443 ? 1.760   6.610  83.931  1.00 10.62 ? 443 VAL A CB  1 
ATOM   3764 C CG1 . VAL A 1 443 ? 0.620   7.647  83.958  1.00 14.24 ? 443 VAL A CG1 1 
ATOM   3765 C CG2 . VAL A 1 443 ? 1.238   5.216  83.651  1.00 11.46 ? 443 VAL A CG2 1 
ATOM   3766 N N   . ALA A 1 444 ? 4.301   8.476  84.143  1.00 13.62 ? 444 ALA A N   1 
ATOM   3767 C CA  . ALA A 1 444 ? 4.864   9.755  84.546  1.00 16.11 ? 444 ALA A CA  1 
ATOM   3768 C C   . ALA A 1 444 ? 5.791   10.344 83.502  1.00 15.42 ? 444 ALA A C   1 
ATOM   3769 O O   . ALA A 1 444 ? 6.124   11.526 83.611  1.00 13.26 ? 444 ALA A O   1 
ATOM   3770 C CB  . ALA A 1 444 ? 5.618   9.635  85.876  1.00 13.19 ? 444 ALA A CB  1 
ATOM   3771 N N   . GLU A 1 445 ? 6.226   9.562  82.511  1.00 10.74 ? 445 GLU A N   1 
ATOM   3772 C CA  . GLU A 1 445 ? 7.062   10.086 81.437  1.00 11.05 ? 445 GLU A CA  1 
ATOM   3773 C C   . GLU A 1 445 ? 6.237   10.791 80.356  1.00 10.82 ? 445 GLU A C   1 
ATOM   3774 O O   . GLU A 1 445 ? 6.817   11.328 79.411  1.00 13.21 ? 445 GLU A O   1 
ATOM   3775 C CB  . GLU A 1 445 ? 7.904   8.943  80.847  1.00 12.74 ? 445 GLU A CB  1 
ATOM   3776 C CG  . GLU A 1 445 ? 8.924   8.399  81.881  1.00 12.58 ? 445 GLU A CG  1 
ATOM   3777 C CD  . GLU A 1 445 ? 9.554   7.062  81.519  1.00 18.77 ? 445 GLU A CD  1 
ATOM   3778 O OE1 . GLU A 1 445 ? 9.227   6.482  80.455  1.00 14.94 ? 445 GLU A OE1 1 
ATOM   3779 O OE2 . GLU A 1 445 ? 10.379  6.588  82.336  1.00 16.20 ? 445 GLU A OE2 1 
ATOM   3780 N N   . GLY A 1 446 ? 4.909   10.832 80.497  1.00 10.22 ? 446 GLY A N   1 
ATOM   3781 C CA  . GLY A 1 446 ? 4.093   11.510 79.504  1.00 14.29 ? 446 GLY A CA  1 
ATOM   3782 C C   . GLY A 1 446 ? 4.416   12.991 79.424  1.00 12.90 ? 446 GLY A C   1 
ATOM   3783 O O   . GLY A 1 446 ? 4.760   13.632 80.422  1.00 12.13 ? 446 GLY A O   1 
ATOM   3784 N N   . SER A 1 447 ? 4.327   13.534 78.202  1.00 10.27 ? 447 SER A N   1 
ATOM   3785 C CA  . SER A 1 447 ? 4.702   14.929 77.988  1.00 14.39 ? 447 SER A CA  1 
ATOM   3786 C C   . SER A 1 447 ? 3.781   15.880 78.743  1.00 12.95 ? 447 SER A C   1 
ATOM   3787 O O   . SER A 1 447 ? 4.212   16.976 79.123  1.00 12.79 ? 447 SER A O   1 
ATOM   3788 C CB  . SER A 1 447 ? 4.695   15.265 76.489  1.00 10.70 ? 447 SER A CB  1 
ATOM   3789 O OG  . SER A 1 447 ? 3.363   15.245 75.960  1.00 12.99 ? 447 SER A OG  1 
ATOM   3790 N N   . ASP A 1 448 ? 2.531   15.463 78.995  1.00 10.86 ? 448 ASP A N   1 
ATOM   3791 C CA  . ASP A 1 448 ? 1.524   16.392 79.495  1.00 11.96 ? 448 ASP A CA  1 
ATOM   3792 C C   . ASP A 1 448 ? 1.910   16.978 80.846  1.00 8.98  ? 448 ASP A C   1 
ATOM   3793 O O   . ASP A 1 448 ? 1.667   18.161 81.100  1.00 13.13 ? 448 ASP A O   1 
ATOM   3794 C CB  . ASP A 1 448 ? 0.156   15.713 79.602  1.00 11.79 ? 448 ASP A CB  1 
ATOM   3795 C CG  . ASP A 1 448 ? -0.269  15.065 78.295  1.00 10.70 ? 448 ASP A CG  1 
ATOM   3796 O OD1 . ASP A 1 448 ? 0.211   13.958 77.959  1.00 14.08 ? 448 ASP A OD1 1 
ATOM   3797 O OD2 . ASP A 1 448 ? -1.005  15.735 77.545  1.00 13.43 ? 448 ASP A OD2 1 
ATOM   3798 N N   . TRP A 1 449 ? 2.516   16.174 81.728  1.00 9.58  ? 449 TRP A N   1 
ATOM   3799 C CA  . TRP A 1 449 ? 2.818   16.674 83.069  1.00 9.11  ? 449 TRP A CA  1 
ATOM   3800 C C   . TRP A 1 449 ? 3.790   17.835 83.011  1.00 11.94 ? 449 TRP A C   1 
ATOM   3801 O O   . TRP A 1 449 ? 3.678   18.787 83.797  1.00 13.97 ? 449 TRP A O   1 
ATOM   3802 C CB  . TRP A 1 449 ? 3.375   15.543 83.942  1.00 11.33 ? 449 TRP A CB  1 
ATOM   3803 C CG  . TRP A 1 449 ? 2.639   14.262 83.720  1.00 12.69 ? 449 TRP A CG  1 
ATOM   3804 C CD1 . TRP A 1 449 ? 3.157   13.098 83.213  1.00 13.13 ? 449 TRP A CD1 1 
ATOM   3805 C CD2 . TRP A 1 449 ? 1.242   14.007 83.963  1.00 10.69 ? 449 TRP A CD2 1 
ATOM   3806 N NE1 . TRP A 1 449 ? 2.170   12.139 83.130  1.00 11.66 ? 449 TRP A NE1 1 
ATOM   3807 C CE2 . TRP A 1 449 ? 0.990   12.669 83.580  1.00 8.98  ? 449 TRP A CE2 1 
ATOM   3808 C CE3 . TRP A 1 449 ? 0.180   14.778 84.456  1.00 12.56 ? 449 TRP A CE3 1 
ATOM   3809 C CZ2 . TRP A 1 449 ? -0.268  12.095 83.669  1.00 8.87  ? 449 TRP A CZ2 1 
ATOM   3810 C CZ3 . TRP A 1 449 ? -1.064  14.198 84.563  1.00 11.87 ? 449 TRP A CZ3 1 
ATOM   3811 C CH2 . TRP A 1 449 ? -1.283  12.868 84.167  1.00 12.62 ? 449 TRP A CH2 1 
ATOM   3812 N N   . PHE A 1 450 ? 4.734   17.788 82.065  1.00 10.64 ? 450 PHE A N   1 
ATOM   3813 C CA  . PHE A 1 450 ? 5.780   18.799 81.956  1.00 15.15 ? 450 PHE A CA  1 
ATOM   3814 C C   . PHE A 1 450 ? 5.283   20.050 81.265  1.00 16.10 ? 450 PHE A C   1 
ATOM   3815 O O   . PHE A 1 450 ? 5.815   21.140 81.496  1.00 13.81 ? 450 PHE A O   1 
ATOM   3816 C CB  . PHE A 1 450 ? 6.977   18.213 81.208  1.00 12.70 ? 450 PHE A CB  1 
ATOM   3817 C CG  . PHE A 1 450 ? 7.516   16.988 81.874  1.00 12.13 ? 450 PHE A CG  1 
ATOM   3818 C CD1 . PHE A 1 450 ? 8.461   17.086 82.888  1.00 13.19 ? 450 PHE A CD1 1 
ATOM   3819 C CD2 . PHE A 1 450 ? 7.022   15.740 81.537  1.00 11.92 ? 450 PHE A CD2 1 
ATOM   3820 C CE1 . PHE A 1 450 ? 8.925   15.951 83.528  1.00 13.17 ? 450 PHE A CE1 1 
ATOM   3821 C CE2 . PHE A 1 450 ? 7.480   14.599 82.169  1.00 12.07 ? 450 PHE A CE2 1 
ATOM   3822 C CZ  . PHE A 1 450 ? 8.429   14.708 83.172  1.00 13.19 ? 450 PHE A CZ  1 
ATOM   3823 N N   . TRP A 1 451 ? 4.271   19.899 80.412  1.00 13.09 ? 451 TRP A N   1 
ATOM   3824 C CA  . TRP A 1 451 ? 3.674   21.035 79.728  1.00 12.40 ? 451 TRP A CA  1 
ATOM   3825 C C   . TRP A 1 451 ? 3.012   21.975 80.730  1.00 13.87 ? 451 TRP A C   1 
ATOM   3826 O O   . TRP A 1 451 ? 3.226   23.192 80.694  1.00 16.63 ? 451 TRP A O   1 
ATOM   3827 C CB  . TRP A 1 451 ? 2.665   20.498 78.703  1.00 15.03 ? 451 TRP A CB  1 
ATOM   3828 C CG  . TRP A 1 451 ? 1.828   21.496 78.032  1.00 16.76 ? 451 TRP A CG  1 
ATOM   3829 C CD1 . TRP A 1 451 ? 0.607   21.956 78.447  1.00 15.84 ? 451 TRP A CD1 1 
ATOM   3830 C CD2 . TRP A 1 451 ? 2.103   22.139 76.788  1.00 22.62 ? 451 TRP A CD2 1 
ATOM   3831 N NE1 . TRP A 1 451 ? 0.116   22.867 77.539  1.00 24.96 ? 451 TRP A NE1 1 
ATOM   3832 C CE2 . TRP A 1 451 ? 1.014   22.995 76.511  1.00 27.41 ? 451 TRP A CE2 1 
ATOM   3833 C CE3 . TRP A 1 451 ? 3.170   22.086 75.883  1.00 21.23 ? 451 TRP A CE3 1 
ATOM   3834 C CZ2 . TRP A 1 451 ? 0.964   23.791 75.370  1.00 29.27 ? 451 TRP A CZ2 1 
ATOM   3835 C CZ3 . TRP A 1 451 ? 3.120   22.879 74.752  1.00 25.67 ? 451 TRP A CZ3 1 
ATOM   3836 C CH2 . TRP A 1 451 ? 2.025   23.724 74.506  1.00 27.91 ? 451 TRP A CH2 1 
ATOM   3837 N N   . TRP A 1 452 ? 2.207   21.419 81.645  1.00 12.34 ? 452 TRP A N   1 
ATOM   3838 C CA  . TRP A 1 452 ? 1.444   22.239 82.580  1.00 19.07 ? 452 TRP A CA  1 
ATOM   3839 C C   . TRP A 1 452 ? 2.285   22.759 83.736  1.00 23.60 ? 452 TRP A C   1 
ATOM   3840 O O   . TRP A 1 452 ? 1.903   23.756 84.359  1.00 19.05 ? 452 TRP A O   1 
ATOM   3841 C CB  . TRP A 1 452 ? 0.251   21.451 83.116  1.00 17.55 ? 452 TRP A CB  1 
ATOM   3842 C CG  . TRP A 1 452 ? -0.673  21.046 82.006  1.00 19.54 ? 452 TRP A CG  1 
ATOM   3843 C CD1 . TRP A 1 452 ? -0.900  19.777 81.551  1.00 17.51 ? 452 TRP A CD1 1 
ATOM   3844 C CD2 . TRP A 1 452 ? -1.455  21.917 81.172  1.00 13.87 ? 452 TRP A CD2 1 
ATOM   3845 N NE1 . TRP A 1 452 ? -1.778  19.801 80.501  1.00 17.34 ? 452 TRP A NE1 1 
ATOM   3846 C CE2 . TRP A 1 452 ? -2.132  21.101 80.240  1.00 15.26 ? 452 TRP A CE2 1 
ATOM   3847 C CE3 . TRP A 1 452 ? -1.640  23.301 81.119  1.00 19.08 ? 452 TRP A CE3 1 
ATOM   3848 C CZ2 . TRP A 1 452 ? -2.989  21.621 79.275  1.00 20.29 ? 452 TRP A CZ2 1 
ATOM   3849 C CZ3 . TRP A 1 452 ? -2.498  23.821 80.155  1.00 18.35 ? 452 TRP A CZ3 1 
ATOM   3850 C CH2 . TRP A 1 452 ? -3.165  22.978 79.248  1.00 19.71 ? 452 TRP A CH2 1 
ATOM   3851 N N   . GLN A 1 453 ? 3.421   22.124 84.018  1.00 20.87 ? 453 GLN A N   1 
ATOM   3852 C CA  . GLN A 1 453 ? 4.278   22.550 85.120  1.00 20.74 ? 453 GLN A CA  1 
ATOM   3853 C C   . GLN A 1 453 ? 4.951   23.884 84.801  1.00 25.84 ? 453 GLN A C   1 
ATOM   3854 O O   . GLN A 1 453 ? 5.433   24.113 83.689  1.00 22.90 ? 453 GLN A O   1 
ATOM   3855 C CB  . GLN A 1 453 ? 5.313   21.457 85.403  1.00 18.49 ? 453 GLN A CB  1 
ATOM   3856 C CG  . GLN A 1 453 ? 6.365   21.714 86.490  1.00 25.78 ? 453 GLN A CG  1 
ATOM   3857 C CD  . GLN A 1 453 ? 5.825   22.014 87.891  1.00 29.03 ? 453 GLN A CD  1 
ATOM   3858 O OE1 . GLN A 1 453 ? 4.626   21.953 88.145  1.00 32.37 ? 453 GLN A OE1 1 
ATOM   3859 N NE2 . GLN A 1 453 ? 6.743   22.252 88.827  1.00 29.61 ? 453 GLN A NE2 1 
ATOM   3860 N N   . GLY A 1 454 ? 4.946   24.788 85.780  1.00 27.83 ? 454 GLY A N   1 
ATOM   3861 C CA  . GLY A 1 454 ? 5.627   26.062 85.635  1.00 35.57 ? 454 GLY A CA  1 
ATOM   3862 C C   . GLY A 1 454 ? 5.097   26.978 84.554  1.00 37.89 ? 454 GLY A C   1 
ATOM   3863 O O   . GLY A 1 454 ? 5.881   27.523 83.768  1.00 37.67 ? 454 GLY A O   1 
ATOM   3864 N N   . GLU A 1 455 ? 3.794   27.111 84.497  1.00 34.27 ? 455 GLU A N   1 
ATOM   3865 C CA  . GLU A 1 455 ? 3.157   27.934 83.510  1.00 42.61 ? 455 GLU A CA  1 
ATOM   3866 C C   . GLU A 1 455 ? 2.205   28.888 84.218  1.00 51.97 ? 455 GLU A C   1 
ATOM   3867 O O   . GLU A 1 455 ? 1.662   28.574 85.268  1.00 50.70 ? 455 GLU A O   1 
ATOM   3868 C CB  . GLU A 1 455 ? 2.358   27.098 82.520  1.00 38.74 ? 455 GLU A CB  1 
ATOM   3869 C CG  . GLU A 1 455 ? 3.157   26.198 81.612  1.00 37.72 ? 455 GLU A CG  1 
ATOM   3870 C CD  . GLU A 1 455 ? 3.988   26.964 80.596  1.00 43.76 ? 455 GLU A CD  1 
ATOM   3871 O OE1 . GLU A 1 455 ? 3.701   28.149 80.393  1.00 47.21 ? 455 GLU A OE1 1 
ATOM   3872 O OE2 . GLU A 1 455 ? 4.910   26.388 80.000  1.00 42.69 ? 455 GLU A OE2 1 
ATOM   3873 N N   . GLU A 1 456 ? 2.028   30.053 83.608  1.00 60.59 ? 456 GLU A N   1 
ATOM   3874 C CA  . GLU A 1 456 ? 1.151   31.076 84.115  1.00 67.13 ? 456 GLU A CA  1 
ATOM   3875 C C   . GLU A 1 456 ? -0.279  30.615 84.069  1.00 67.03 ? 456 GLU A C   1 
ATOM   3876 O O   . GLU A 1 456 ? -0.802  30.318 83.023  1.00 66.51 ? 456 GLU A O   1 
ATOM   3877 C CB  . GLU A 1 456 ? 1.288   32.360 83.287  1.00 75.15 ? 456 GLU A CB  1 
ATOM   3878 C CG  . GLU A 1 456 ? 0.625   32.321 81.910  1.00 80.36 ? 456 GLU A CG  1 
ATOM   3879 C CD  . GLU A 1 456 ? -0.079  33.605 81.505  1.00 85.38 ? 456 GLU A CD  1 
ATOM   3880 O OE1 . GLU A 1 456 ? 0.513   34.694 81.624  1.00 87.39 ? 456 GLU A OE1 1 
ATOM   3881 O OE2 . GLU A 1 456 ? -1.227  33.514 81.024  1.00 86.92 ? 456 GLU A OE2 1 
ATOM   3882 N N   . LYS A 1 457 ? -0.877  30.565 85.243  1.00 69.74 ? 457 LYS A N   1 
ATOM   3883 C CA  . LYS A 1 457 ? -2.267  30.209 85.467  1.00 71.17 ? 457 LYS A CA  1 
ATOM   3884 C C   . LYS A 1 457 ? -2.883  28.957 84.841  1.00 69.34 ? 457 LYS A C   1 
ATOM   3885 O O   . LYS A 1 457 ? -4.107  28.874 84.777  1.00 72.13 ? 457 LYS A O   1 
ATOM   3886 C CB  . LYS A 1 457 ? -3.147  31.388 85.080  1.00 71.21 ? 457 LYS A CB  1 
ATOM   3887 C CG  . LYS A 1 457 ? -3.418  32.337 86.215  1.00 71.64 ? 457 LYS A CG  1 
ATOM   3888 C CD  . LYS A 1 457 ? -2.107  32.852 86.770  1.00 69.27 ? 457 LYS A CD  1 
ATOM   3889 C CE  . LYS A 1 457 ? -2.330  33.526 88.089  1.00 70.97 ? 457 LYS A CE  1 
ATOM   3890 N NZ  . LYS A 1 457 ? -2.672  34.942 87.821  1.00 74.73 ? 457 LYS A NZ  1 
ATOM   3891 N N   . ALA A 1 458 ? -2.081  28.001 84.395  1.00 58.89 ? 458 ALA A N   1 
ATOM   3892 C CA  . ALA A 1 458 ? -2.630  26.783 83.810  1.00 48.50 ? 458 ALA A CA  1 
ATOM   3893 C C   . ALA A 1 458 ? -3.832  26.202 84.617  1.00 46.79 ? 458 ALA A C   1 
ATOM   3894 O O   . ALA A 1 458 ? -3.753  25.936 85.786  1.00 40.63 ? 458 ALA A O   1 
ATOM   3895 C CB  . ALA A 1 458 ? -1.554  25.745 83.649  1.00 47.05 ? 458 ALA A CB  1 
ATOM   3896 N N   . PRO A 1 459 ? -4.984  26.026 83.873  1.00 48.00 ? 459 PRO A N   1 
ATOM   3897 C CA  . PRO A 1 459 ? -6.155  25.557 84.629  1.00 42.18 ? 459 PRO A CA  1 
ATOM   3898 C C   . PRO A 1 459 ? -6.048  24.187 85.256  1.00 36.26 ? 459 PRO A C   1 
ATOM   3899 O O   . PRO A 1 459 ? -5.641  23.254 84.624  1.00 31.21 ? 459 PRO A O   1 
ATOM   3900 C CB  . PRO A 1 459 ? -7.293  25.587 83.600  1.00 37.25 ? 459 PRO A CB  1 
ATOM   3901 C CG  . PRO A 1 459 ? -6.842  26.463 82.529  1.00 44.13 ? 459 PRO A CG  1 
ATOM   3902 C CD  . PRO A 1 459 ? -5.411  26.133 82.408  1.00 46.70 ? 459 PRO A CD  1 
ATOM   3903 N N   . PHE A 1 460 ? -6.451  24.079 86.501  1.00 33.34 ? 460 PHE A N   1 
ATOM   3904 C CA  . PHE A 1 460 ? -6.410  22.822 87.199  1.00 31.31 ? 460 PHE A CA  1 
ATOM   3905 C C   . PHE A 1 460 ? -5.012  22.233 87.306  1.00 32.96 ? 460 PHE A C   1 
ATOM   3906 O O   . PHE A 1 460 ? -4.863  21.072 87.434  1.00 26.23 ? 460 PHE A O   1 
ATOM   3907 C CB  . PHE A 1 460 ? -7.350  21.799 86.574  1.00 34.72 ? 460 PHE A CB  1 
ATOM   3908 C CG  . PHE A 1 460 ? -8.817  22.135 86.728  1.00 34.34 ? 460 PHE A CG  1 
ATOM   3909 C CD1 . PHE A 1 460 ? -9.373  22.300 87.960  1.00 40.44 ? 460 PHE A CD1 1 
ATOM   3910 C CD2 . PHE A 1 460 ? -9.613  22.263 85.639  1.00 37.07 ? 460 PHE A CD2 1 
ATOM   3911 C CE1 . PHE A 1 460 ? -10.701 22.600 88.106  1.00 43.20 ? 460 PHE A CE1 1 
ATOM   3912 C CE2 . PHE A 1 460 ? -10.943 22.566 85.764  1.00 39.45 ? 460 PHE A CE2 1 
ATOM   3913 C CZ  . PHE A 1 460 ? -11.495 22.739 87.003  1.00 41.86 ? 460 PHE A CZ  1 
ATOM   3914 N N   . VAL A 1 461 ? -4.008  23.075 87.241  1.00 27.77 ? 461 VAL A N   1 
ATOM   3915 C CA  . VAL A 1 461 ? -2.641  22.581 87.339  1.00 28.25 ? 461 VAL A CA  1 
ATOM   3916 C C   . VAL A 1 461 ? -2.436  21.827 88.648  1.00 27.46 ? 461 VAL A C   1 
ATOM   3917 O O   . VAL A 1 461 ? -1.612  20.907 88.726  1.00 27.56 ? 461 VAL A O   1 
ATOM   3918 C CB  . VAL A 1 461 ? -1.623  23.728 87.186  1.00 29.29 ? 461 VAL A CB  1 
ATOM   3919 C CG1 . VAL A 1 461 ? -1.655  24.652 88.402  1.00 34.87 ? 461 VAL A CG1 1 
ATOM   3920 C CG2 . VAL A 1 461 ? -0.216  23.172 86.938  1.00 32.14 ? 461 VAL A CG2 1 
ATOM   3921 N N   . GLU A 1 462 ? -3.181  22.184 89.691  1.00 19.18 ? 462 GLU A N   1 
ATOM   3922 C CA  . GLU A 1 462 ? -3.096  21.427 90.931  1.00 26.80 ? 462 GLU A CA  1 
ATOM   3923 C C   . GLU A 1 462 ? -3.475  19.973 90.712  1.00 24.23 ? 462 GLU A C   1 
ATOM   3924 O O   . GLU A 1 462 ? -2.927  19.087 91.369  1.00 20.46 ? 462 GLU A O   1 
ATOM   3925 C CB  . GLU A 1 462 ? -4.012  22.048 91.967  1.00 43.59 ? 462 GLU A CB  1 
ATOM   3926 C CG  . GLU A 1 462 ? -3.331  22.477 93.229  1.00 59.54 ? 462 GLU A CG  1 
ATOM   3927 C CD  . GLU A 1 462 ? -4.249  23.421 93.955  1.00 73.75 ? 462 GLU A CD  1 
ATOM   3928 O OE1 . GLU A 1 462 ? -4.261  24.606 93.562  1.00 78.53 ? 462 GLU A OE1 1 
ATOM   3929 O OE2 . GLU A 1 462 ? -5.035  22.960 94.817  1.00 77.15 ? 462 GLU A OE2 1 
ATOM   3930 N N   . VAL A 1 463 ? -4.403  19.710 89.789  1.00 16.47 ? 463 VAL A N   1 
ATOM   3931 C CA  . VAL A 1 463 ? -4.826  18.339 89.555  1.00 16.12 ? 463 VAL A CA  1 
ATOM   3932 C C   . VAL A 1 463 ? -3.785  17.584 88.737  1.00 18.71 ? 463 VAL A C   1 
ATOM   3933 O O   . VAL A 1 463 ? -3.454  16.435 89.049  1.00 16.64 ? 463 VAL A O   1 
ATOM   3934 C CB  . VAL A 1 463 ? -6.213  18.286 88.887  1.00 17.59 ? 463 VAL A CB  1 
ATOM   3935 C CG1 . VAL A 1 463 ? -6.631  16.843 88.694  1.00 18.04 ? 463 VAL A CG1 1 
ATOM   3936 C CG2 . VAL A 1 463 ? -7.243  19.016 89.724  1.00 19.09 ? 463 VAL A CG2 1 
ATOM   3937 N N   . PHE A 1 464 ? -3.255  18.208 87.676  1.00 14.60 ? 464 PHE A N   1 
ATOM   3938 C CA  . PHE A 1 464 ? -2.155  17.594 86.936  1.00 12.18 ? 464 PHE A CA  1 
ATOM   3939 C C   . PHE A 1 464 ? -0.978  17.298 87.855  1.00 13.82 ? 464 PHE A C   1 
ATOM   3940 O O   . PHE A 1 464 ? -0.298  16.269 87.719  1.00 13.85 ? 464 PHE A O   1 
ATOM   3941 C CB  . PHE A 1 464 ? -1.725  18.494 85.776  1.00 12.38 ? 464 PHE A CB  1 
ATOM   3942 C CG  . PHE A 1 464 ? -2.723  18.519 84.626  1.00 12.34 ? 464 PHE A CG  1 
ATOM   3943 C CD1 . PHE A 1 464 ? -2.709  17.533 83.647  1.00 14.55 ? 464 PHE A CD1 1 
ATOM   3944 C CD2 . PHE A 1 464 ? -3.689  19.501 84.555  1.00 15.12 ? 464 PHE A CD2 1 
ATOM   3945 C CE1 . PHE A 1 464 ? -3.640  17.556 82.597  1.00 13.43 ? 464 PHE A CE1 1 
ATOM   3946 C CE2 . PHE A 1 464 ? -4.610  19.531 83.497  1.00 16.01 ? 464 PHE A CE2 1 
ATOM   3947 C CZ  . PHE A 1 464 ? -4.579  18.554 82.532  1.00 12.61 ? 464 PHE A CZ  1 
ATOM   3948 N N   . ASP A 1 465 ? -0.708  18.202 88.788  1.00 14.44 ? 465 ASP A N   1 
ATOM   3949 C CA  . ASP A 1 465 ? 0.402   17.998 89.712  1.00 16.01 ? 465 ASP A CA  1 
ATOM   3950 C C   . ASP A 1 465 ? 0.144   16.810 90.626  1.00 16.91 ? 465 ASP A C   1 
ATOM   3951 O O   . ASP A 1 465 ? 1.041   15.995 90.875  1.00 16.72 ? 465 ASP A O   1 
ATOM   3952 C CB  . ASP A 1 465 ? 0.615   19.262 90.524  1.00 12.99 ? 465 ASP A CB  1 
ATOM   3953 C CG  . ASP A 1 465 ? 1.695   19.099 91.582  1.00 21.74 ? 465 ASP A CG  1 
ATOM   3954 O OD1 . ASP A 1 465 ? 2.899   19.094 91.226  1.00 19.01 ? 465 ASP A OD1 1 
ATOM   3955 O OD2 . ASP A 1 465 ? 1.330   18.967 92.768  1.00 17.74 ? 465 ASP A OD2 1 
ATOM   3956 N N   . LYS A 1 466 ? -1.069  16.720 91.164  1.00 15.52 ? 466 LYS A N   1 
ATOM   3957 C CA  . LYS A 1 466 ? -1.444  15.575 91.983  1.00 12.53 ? 466 LYS A CA  1 
ATOM   3958 C C   . LYS A 1 466 ? -1.303  14.270 91.211  1.00 15.61 ? 466 LYS A C   1 
ATOM   3959 O O   . LYS A 1 466 ? -0.820  13.269 91.751  1.00 15.79 ? 466 LYS A O   1 
ATOM   3960 C CB  . LYS A 1 466 ? -2.876  15.747 92.469  1.00 13.90 ? 466 LYS A CB  1 
ATOM   3961 C CG  . LYS A 1 466 ? -3.361  14.655 93.365  1.00 19.85 ? 466 LYS A CG  1 
ATOM   3962 C CD  . LYS A 1 466 ? -4.802  14.954 93.755  1.00 26.27 ? 466 LYS A CD  1 
ATOM   3963 C CE  . LYS A 1 466 ? -5.155  14.344 95.089  1.00 41.32 ? 466 LYS A CE  1 
ATOM   3964 N NZ  . LYS A 1 466 ? -4.943  12.884 95.070  1.00 48.67 ? 466 LYS A NZ  1 
ATOM   3965 N N   . LEU A 1 467 ? -1.766  14.249 89.959  1.00 13.73 ? 467 LEU A N   1 
ATOM   3966 C CA  . LEU A 1 467 ? -1.668  13.037 89.144  1.00 13.18 ? 467 LEU A CA  1 
ATOM   3967 C C   . LEU A 1 467 ? -0.212  12.637 88.923  1.00 17.63 ? 467 LEU A C   1 
ATOM   3968 O O   . LEU A 1 467 ? 0.187   11.495 89.199  1.00 11.86 ? 467 LEU A O   1 
ATOM   3969 C CB  . LEU A 1 467 ? -2.384  13.255 87.804  1.00 10.98 ? 467 LEU A CB  1 
ATOM   3970 C CG  . LEU A 1 467 ? -3.918  13.267 87.940  1.00 13.86 ? 467 LEU A CG  1 
ATOM   3971 C CD1 . LEU A 1 467 ? -4.544  13.784 86.646  1.00 10.74 ? 467 LEU A CD1 1 
ATOM   3972 C CD2 . LEU A 1 467 ? -4.411  11.870 88.255  1.00 14.51 ? 467 LEU A CD2 1 
ATOM   3973 N N   . PHE A 1 468 ? 0.602   13.571 88.431  1.00 14.41 ? 468 PHE A N   1 
ATOM   3974 C CA  . PHE A 1 468 ? 2.011   13.264 88.180  1.00 12.52 ? 468 PHE A CA  1 
ATOM   3975 C C   . PHE A 1 468 ? 2.683   12.704 89.428  1.00 13.63 ? 468 PHE A C   1 
ATOM   3976 O O   . PHE A 1 468 ? 3.341   11.656 89.386  1.00 14.98 ? 468 PHE A O   1 
ATOM   3977 C CB  . PHE A 1 468 ? 2.739   14.520 87.699  1.00 10.08 ? 468 PHE A CB  1 
ATOM   3978 C CG  . PHE A 1 468 ? 4.235   14.367 87.597  1.00 9.22  ? 468 PHE A CG  1 
ATOM   3979 C CD1 . PHE A 1 468 ? 4.813   13.651 86.556  1.00 8.51  ? 468 PHE A CD1 1 
ATOM   3980 C CD2 . PHE A 1 468 ? 5.068   14.957 88.539  1.00 11.96 ? 468 PHE A CD2 1 
ATOM   3981 C CE1 . PHE A 1 468 ? 6.195   13.525 86.460  1.00 14.22 ? 468 PHE A CE1 1 
ATOM   3982 C CE2 . PHE A 1 468 ? 6.444   14.828 88.437  1.00 15.25 ? 468 PHE A CE2 1 
ATOM   3983 C CZ  . PHE A 1 468 ? 7.006   14.113 87.401  1.00 17.03 ? 468 PHE A CZ  1 
ATOM   3984 N N   . ARG A 1 469 ? 2.540   13.406 90.553  1.00 11.67 ? 469 ARG A N   1 
ATOM   3985 C CA  . ARG A 1 469 ? 3.231   12.973 91.759  1.00 11.17 ? 469 ARG A CA  1 
ATOM   3986 C C   . ARG A 1 469 ? 2.640   11.678 92.301  1.00 16.36 ? 469 ARG A C   1 
ATOM   3987 O O   . ARG A 1 469 ? 3.363   10.875 92.909  1.00 13.65 ? 469 ARG A O   1 
ATOM   3988 C CB  . ARG A 1 469 ? 3.188   14.093 92.804  1.00 16.31 ? 469 ARG A CB  1 
ATOM   3989 C CG  . ARG A 1 469 ? 3.973   15.334 92.358  1.00 14.97 ? 469 ARG A CG  1 
ATOM   3990 C CD  . ARG A 1 469 ? 3.855   16.453 93.391  1.00 18.21 ? 469 ARG A CD  1 
ATOM   3991 N NE  . ARG A 1 469 ? 4.595   17.675 93.052  1.00 17.31 ? 469 ARG A NE  1 
ATOM   3992 C CZ  . ARG A 1 469 ? 5.853   17.922 93.409  1.00 19.75 ? 469 ARG A CZ  1 
ATOM   3993 N NH1 . ARG A 1 469 ? 6.549   17.015 94.090  1.00 16.68 ? 469 ARG A NH1 1 
ATOM   3994 N NH2 . ARG A 1 469 ? 6.424   19.081 93.093  1.00 17.60 ? 469 ARG A NH2 1 
ATOM   3995 N N   . SER A 1 470 ? 1.339   11.444 92.080  1.00 15.23 ? 470 SER A N   1 
ATOM   3996 C CA  . SER A 1 470 ? 0.766   10.164 92.488  1.00 16.65 ? 470 SER A CA  1 
ATOM   3997 C C   . SER A 1 470 ? 1.323   9.024  91.645  1.00 13.92 ? 470 SER A C   1 
ATOM   3998 O O   . SER A 1 470 ? 1.626   7.950  92.175  1.00 15.29 ? 470 SER A O   1 
ATOM   3999 C CB  . SER A 1 470 ? -0.762  10.195 92.395  1.00 19.08 ? 470 SER A CB  1 
ATOM   4000 O OG  . SER A 1 470 ? -1.277  11.130 93.321  1.00 23.43 ? 470 SER A OG  1 
ATOM   4001 N N   . PHE A 1 471 ? 1.465   9.231  90.328  1.00 15.60 ? 471 PHE A N   1 
ATOM   4002 C CA  . PHE A 1 471 ? 2.056   8.191  89.488  1.00 11.55 ? 471 PHE A CA  1 
ATOM   4003 C C   . PHE A 1 471 ? 3.513   7.931  89.867  1.00 19.25 ? 471 PHE A C   1 
ATOM   4004 O O   . PHE A 1 471 ? 3.961   6.776  89.902  1.00 15.01 ? 471 PHE A O   1 
ATOM   4005 C CB  . PHE A 1 471 ? 1.939   8.564  88.002  1.00 14.23 ? 471 PHE A CB  1 
ATOM   4006 C CG  . PHE A 1 471 ? 0.515   8.661  87.513  1.00 11.74 ? 471 PHE A CG  1 
ATOM   4007 C CD1 . PHE A 1 471 ? -0.377  7.643  87.762  1.00 14.78 ? 471 PHE A CD1 1 
ATOM   4008 C CD2 . PHE A 1 471 ? 0.092   9.744  86.748  1.00 16.09 ? 471 PHE A CD2 1 
ATOM   4009 C CE1 . PHE A 1 471 ? -1.689  7.713  87.300  1.00 17.97 ? 471 PHE A CE1 1 
ATOM   4010 C CE2 . PHE A 1 471 ? -1.219  9.808  86.286  1.00 14.13 ? 471 PHE A CE2 1 
ATOM   4011 C CZ  . PHE A 1 471 ? -2.097  8.792  86.563  1.00 15.77 ? 471 PHE A CZ  1 
ATOM   4012 N N   . VAL A 1 472 ? 4.258   8.990  90.174  1.00 14.29 ? 472 VAL A N   1 
ATOM   4013 C CA  . VAL A 1 472 ? 5.653   8.836  90.578  1.00 15.73 ? 472 VAL A CA  1 
ATOM   4014 C C   . VAL A 1 472 ? 5.751   8.042  91.877  1.00 16.12 ? 472 VAL A C   1 
ATOM   4015 O O   . VAL A 1 472 ? 6.624   7.176  92.033  1.00 15.54 ? 472 VAL A O   1 
ATOM   4016 C CB  . VAL A 1 472 ? 6.307   10.226 90.689  1.00 17.46 ? 472 VAL A CB  1 
ATOM   4017 C CG1 . VAL A 1 472 ? 7.563   10.179 91.510  1.00 24.48 ? 472 VAL A CG1 1 
ATOM   4018 C CG2 . VAL A 1 472 ? 6.581   10.787 89.276  1.00 21.82 ? 472 VAL A CG2 1 
ATOM   4019 N N   . ARG A 1 473 ? 4.857   8.328  92.832  1.00 15.58 ? 473 ARG A N   1 
ATOM   4020 C CA  . ARG A 1 473 ? 4.813   7.593  94.096  1.00 20.83 ? 473 ARG A CA  1 
ATOM   4021 C C   . ARG A 1 473 ? 4.511   6.120  93.859  1.00 22.78 ? 473 ARG A C   1 
ATOM   4022 O O   . ARG A 1 473 ? 5.206   5.229  94.370  1.00 20.44 ? 473 ARG A O   1 
ATOM   4023 C CB  . ARG A 1 473 ? 3.746   8.217  94.999  1.00 20.58 ? 473 ARG A CB  1 
ATOM   4024 C CG  . ARG A 1 473 ? 3.806   7.842  96.475  1.00 32.62 ? 473 ARG A CG  1 
ATOM   4025 C CD  . ARG A 1 473 ? 2.599   8.468  97.205  1.00 45.39 ? 473 ARG A CD  1 
ATOM   4026 N NE  . ARG A 1 473 ? 2.406   9.868  96.816  1.00 58.41 ? 473 ARG A NE  1 
ATOM   4027 C CZ  . ARG A 1 473 ? 1.277   10.379 96.327  1.00 62.41 ? 473 ARG A CZ  1 
ATOM   4028 N NH1 . ARG A 1 473 ? 0.203   9.616  96.169  1.00 61.73 ? 473 ARG A NH1 1 
ATOM   4029 N NH2 . ARG A 1 473 ? 1.221   11.663 95.999  1.00 62.29 ? 473 ARG A NH2 1 
ATOM   4030 N N   . ARG A 1 474 ? 3.478   5.855  93.061  1.00 16.81 ? 474 ARG A N   1 
ATOM   4031 C CA  . ARG A 1 474 ? 3.030   4.495  92.806  1.00 22.51 ? 474 ARG A CA  1 
ATOM   4032 C C   . ARG A 1 474 ? 4.075   3.693  92.041  1.00 17.47 ? 474 ARG A C   1 
ATOM   4033 O O   . ARG A 1 474 ? 4.195   2.477  92.254  1.00 20.09 ? 474 ARG A O   1 
ATOM   4034 C CB  . ARG A 1 474 ? 1.711   4.539  92.032  1.00 19.44 ? 474 ARG A CB  1 
ATOM   4035 C CG  . ARG A 1 474 ? 1.088   3.193  91.718  1.00 23.98 ? 474 ARG A CG  1 
ATOM   4036 C CD  . ARG A 1 474 ? 0.596   2.432  92.941  1.00 38.14 ? 474 ARG A CD  1 
ATOM   4037 N NE  . ARG A 1 474 ? -0.347  1.394  92.522  1.00 48.75 ? 474 ARG A NE  1 
ATOM   4038 C CZ  . ARG A 1 474 ? 0.005   0.236  91.965  1.00 60.68 ? 474 ARG A CZ  1 
ATOM   4039 N NH1 . ARG A 1 474 ? 1.287   -0.053 91.770  1.00 61.84 ? 474 ARG A NH1 1 
ATOM   4040 N NH2 . ARG A 1 474 ? -0.927  -0.636 91.600  1.00 66.57 ? 474 ARG A NH2 1 
ATOM   4041 N N   . ALA A 1 475 ? 4.839   4.355  91.167  1.00 15.51 ? 475 ALA A N   1 
ATOM   4042 C CA  . ALA A 1 475 ? 5.888   3.691  90.397  1.00 13.63 ? 475 ALA A CA  1 
ATOM   4043 C C   . ALA A 1 475 ? 6.957   3.058  91.276  1.00 19.92 ? 475 ALA A C   1 
ATOM   4044 O O   . ALA A 1 475 ? 7.661   2.152  90.820  1.00 23.67 ? 475 ALA A O   1 
ATOM   4045 C CB  . ALA A 1 475 ? 6.561   4.685  89.441  1.00 14.60 ? 475 ALA A CB  1 
ATOM   4046 N N   . GLN A 1 476 ? 7.117   3.511  92.511  1.00 18.91 ? 476 GLN A N   1 
ATOM   4047 C CA  . GLN A 1 476 ? 8.166   2.970  93.363  1.00 18.77 ? 476 GLN A CA  1 
ATOM   4048 C C   . GLN A 1 476 ? 7.649   1.889  94.297  1.00 26.22 ? 476 GLN A C   1 
ATOM   4049 O O   . GLN A 1 476 ? 8.438   1.288  95.035  1.00 27.62 ? 476 GLN A O   1 
ATOM   4050 C CB  . GLN A 1 476 ? 8.841   4.111  94.140  1.00 21.97 ? 476 GLN A CB  1 
ATOM   4051 C CG  . GLN A 1 476 ? 9.057   5.344  93.241  1.00 24.39 ? 476 GLN A CG  1 
ATOM   4052 C CD  . GLN A 1 476 ? 9.771   6.500  93.900  1.00 27.29 ? 476 GLN A CD  1 
ATOM   4053 O OE1 . GLN A 1 476 ? 10.798  6.338  94.571  1.00 32.34 ? 476 GLN A OE1 1 
ATOM   4054 N NE2 . GLN A 1 476 ? 9.171   7.681  93.784  1.00 24.09 ? 476 GLN A NE2 1 
ATOM   4055 N N   . GLU A 1 477 ? 6.358   1.584  94.230  1.00 28.47 ? 477 GLU A N   1 
ATOM   4056 C CA  . GLU A 1 477 ? 5.749   0.568  95.066  1.00 32.37 ? 477 GLU A CA  1 
ATOM   4057 C C   . GLU A 1 477 ? 5.458   -0.685 94.244  1.00 35.76 ? 477 GLU A C   1 
ATOM   4058 O O   . GLU A 1 477 ? 5.559   -1.808 94.754  1.00 44.81 ? 477 GLU A O   1 
ATOM   4059 C CB  . GLU A 1 477 ? 4.469   1.111  95.701  1.00 33.67 ? 477 GLU A CB  1 
ATOM   4060 C CG  . GLU A 1 477 ? 4.703   2.333  96.577  1.00 46.49 ? 477 GLU A CG  1 
ATOM   4061 C CD  . GLU A 1 477 ? 3.410   3.004  97.025  1.00 57.99 ? 477 GLU A CD  1 
ATOM   4062 O OE1 . GLU A 1 477 ? 2.323   2.577  96.578  1.00 57.92 ? 477 GLU A OE1 1 
ATOM   4063 O OE2 . GLU A 1 477 ? 3.483   3.967  97.822  1.00 60.25 ? 477 GLU A OE2 1 
ATOM   4064 N N   . LYS B 1 2   ? -27.339 37.826 60.599  1.00 36.38 ? 2   LYS B N   1 
ATOM   4065 C CA  . LYS B 1 2   ? -28.375 37.966 59.586  1.00 38.85 ? 2   LYS B CA  1 
ATOM   4066 C C   . LYS B 1 2   ? -27.758 38.086 58.198  1.00 33.23 ? 2   LYS B C   1 
ATOM   4067 O O   . LYS B 1 2   ? -27.002 39.018 57.929  1.00 37.18 ? 2   LYS B O   1 
ATOM   4068 C CB  . LYS B 1 2   ? -29.252 39.189 59.869  1.00 42.83 ? 2   LYS B CB  1 
ATOM   4069 C CG  . LYS B 1 2   ? -30.431 39.314 58.919  1.00 44.09 ? 2   LYS B CG  1 
ATOM   4070 C CD  . LYS B 1 2   ? -31.263 40.551 59.203  1.00 49.00 ? 2   LYS B CD  1 
ATOM   4071 C CE  . LYS B 1 2   ? -30.623 41.806 58.635  1.00 53.24 ? 2   LYS B CE  1 
ATOM   4072 N NZ  . LYS B 1 2   ? -31.524 42.989 58.764  1.00 53.42 ? 2   LYS B NZ  1 
ATOM   4073 N N   . LYS B 1 3   ? -28.076 37.140 57.318  1.00 29.77 ? 3   LYS B N   1 
ATOM   4074 C CA  . LYS B 1 3   ? -27.537 37.134 55.967  1.00 33.04 ? 3   LYS B CA  1 
ATOM   4075 C C   . LYS B 1 3   ? -28.552 37.695 54.973  1.00 28.14 ? 3   LYS B C   1 
ATOM   4076 O O   . LYS B 1 3   ? -29.763 37.693 55.207  1.00 29.86 ? 3   LYS B O   1 
ATOM   4077 C CB  . LYS B 1 3   ? -27.139 35.716 55.530  1.00 40.37 ? 3   LYS B CB  1 
ATOM   4078 C CG  . LYS B 1 3   ? -26.358 34.886 56.545  1.00 49.54 ? 3   LYS B CG  1 
ATOM   4079 C CD  . LYS B 1 3   ? -25.063 35.561 56.948  1.00 56.17 ? 3   LYS B CD  1 
ATOM   4080 C CE  . LYS B 1 3   ? -23.854 34.707 56.595  1.00 61.62 ? 3   LYS B CE  1 
ATOM   4081 N NZ  . LYS B 1 3   ? -23.974 33.290 57.034  1.00 68.85 ? 3   LYS B NZ  1 
ATOM   4082 N N   . LEU B 1 4   ? -28.034 38.194 53.858  1.00 20.33 ? 4   LEU B N   1 
ATOM   4083 C CA  . LEU B 1 4   ? -28.809 38.348 52.633  1.00 23.14 ? 4   LEU B CA  1 
ATOM   4084 C C   . LEU B 1 4   ? -28.465 37.172 51.729  1.00 21.45 ? 4   LEU B C   1 
ATOM   4085 O O   . LEU B 1 4   ? -27.286 36.860 51.538  1.00 21.23 ? 4   LEU B O   1 
ATOM   4086 C CB  . LEU B 1 4   ? -28.506 39.675 51.932  1.00 22.42 ? 4   LEU B CB  1 
ATOM   4087 C CG  . LEU B 1 4   ? -29.215 39.951 50.596  1.00 19.67 ? 4   LEU B CG  1 
ATOM   4088 C CD1 . LEU B 1 4   ? -29.522 41.446 50.480  1.00 23.06 ? 4   LEU B CD1 1 
ATOM   4089 C CD2 . LEU B 1 4   ? -28.365 39.488 49.395  1.00 15.00 ? 4   LEU B CD2 1 
ATOM   4090 N N   . PHE B 1 5   ? -29.486 36.511 51.189  1.00 20.62 ? 5   PHE B N   1 
ATOM   4091 C CA  . PHE B 1 5   ? -29.279 35.375 50.303  1.00 18.47 ? 5   PHE B CA  1 
ATOM   4092 C C   . PHE B 1 5   ? -29.416 35.857 48.870  1.00 22.13 ? 5   PHE B C   1 
ATOM   4093 O O   . PHE B 1 5   ? -30.448 36.426 48.497  1.00 24.54 ? 5   PHE B O   1 
ATOM   4094 C CB  . PHE B 1 5   ? -30.263 34.241 50.595  1.00 17.85 ? 5   PHE B CB  1 
ATOM   4095 C CG  . PHE B 1 5   ? -30.132 33.677 51.981  1.00 21.86 ? 5   PHE B CG  1 
ATOM   4096 C CD1 . PHE B 1 5   ? -28.938 33.096 52.390  1.00 27.51 ? 5   PHE B CD1 1 
ATOM   4097 C CD2 . PHE B 1 5   ? -31.197 33.727 52.875  1.00 25.05 ? 5   PHE B CD2 1 
ATOM   4098 C CE1 . PHE B 1 5   ? -28.801 32.575 53.670  1.00 29.09 ? 5   PHE B CE1 1 
ATOM   4099 C CE2 . PHE B 1 5   ? -31.068 33.200 54.163  1.00 28.33 ? 5   PHE B CE2 1 
ATOM   4100 C CZ  . PHE B 1 5   ? -29.867 32.627 54.557  1.00 30.32 ? 5   PHE B CZ  1 
ATOM   4101 N N   . LEU B 1 6   ? -28.368 35.646 48.081  1.00 16.32 ? 6   LEU B N   1 
ATOM   4102 C CA  . LEU B 1 6   ? -28.291 36.116 46.709  1.00 17.62 ? 6   LEU B CA  1 
ATOM   4103 C C   . LEU B 1 6   ? -28.280 34.910 45.765  1.00 12.50 ? 6   LEU B C   1 
ATOM   4104 O O   . LEU B 1 6   ? -27.530 33.954 45.983  1.00 14.70 ? 6   LEU B O   1 
ATOM   4105 C CB  . LEU B 1 6   ? -27.033 36.975 46.545  1.00 15.65 ? 6   LEU B CB  1 
ATOM   4106 C CG  . LEU B 1 6   ? -26.731 37.595 45.183  1.00 16.40 ? 6   LEU B CG  1 
ATOM   4107 C CD1 . LEU B 1 6   ? -27.856 38.511 44.704  1.00 14.65 ? 6   LEU B CD1 1 
ATOM   4108 C CD2 . LEU B 1 6   ? -25.409 38.379 45.277  1.00 13.48 ? 6   LEU B CD2 1 
ATOM   4109 N N   . VAL B 1 7   ? -29.128 34.936 44.742  1.00 10.65 ? 7   VAL B N   1 
ATOM   4110 C CA  . VAL B 1 7   ? -29.266 33.809 43.816  1.00 11.06 ? 7   VAL B CA  1 
ATOM   4111 C C   . VAL B 1 7   ? -29.146 34.359 42.399  1.00 15.38 ? 7   VAL B C   1 
ATOM   4112 O O   . VAL B 1 7   ? -30.046 35.062 41.925  1.00 18.49 ? 7   VAL B O   1 
ATOM   4113 C CB  . VAL B 1 7   ? -30.598 33.059 43.994  1.00 11.69 ? 7   VAL B CB  1 
ATOM   4114 C CG1 . VAL B 1 7   ? -30.626 31.804 43.125  1.00 20.08 ? 7   VAL B CG1 1 
ATOM   4115 C CG2 . VAL B 1 7   ? -30.852 32.706 45.470  1.00 15.13 ? 7   VAL B CG2 1 
ATOM   4116 N N   . PHE B 1 8   ? -28.033 34.063 41.732  1.00 9.17  ? 8   PHE B N   1 
ATOM   4117 C CA  . PHE B 1 8   ? -27.878 34.380 40.314  1.00 8.45  ? 8   PHE B CA  1 
ATOM   4118 C C   . PHE B 1 8   ? -28.440 33.225 39.500  1.00 10.48 ? 8   PHE B C   1 
ATOM   4119 O O   . PHE B 1 8   ? -28.128 32.066 39.785  1.00 12.82 ? 8   PHE B O   1 
ATOM   4120 C CB  . PHE B 1 8   ? -26.408 34.570 39.940  1.00 9.44  ? 8   PHE B CB  1 
ATOM   4121 C CG  . PHE B 1 8   ? -25.801 35.817 40.475  1.00 11.80 ? 8   PHE B CG  1 
ATOM   4122 C CD1 . PHE B 1 8   ? -25.918 37.008 39.769  1.00 12.92 ? 8   PHE B CD1 1 
ATOM   4123 C CD2 . PHE B 1 8   ? -25.115 35.802 41.680  1.00 14.58 ? 8   PHE B CD2 1 
ATOM   4124 C CE1 . PHE B 1 8   ? -25.347 38.185 40.257  1.00 14.83 ? 8   PHE B CE1 1 
ATOM   4125 C CE2 . PHE B 1 8   ? -24.541 36.963 42.187  1.00 16.64 ? 8   PHE B CE2 1 
ATOM   4126 C CZ  . PHE B 1 8   ? -24.662 38.164 41.472  1.00 16.47 ? 8   PHE B CZ  1 
ATOM   4127 N N   . TRP B 1 9   ? -29.233 33.537 38.474  1.00 8.81  ? 9   TRP B N   1 
ATOM   4128 C CA  . TRP B 1 9   ? -29.763 32.494 37.588  1.00 8.50  ? 9   TRP B CA  1 
ATOM   4129 C C   . TRP B 1 9   ? -29.618 33.013 36.165  1.00 11.02 ? 9   TRP B C   1 
ATOM   4130 O O   . TRP B 1 9   ? -30.405 33.853 35.719  1.00 9.85  ? 9   TRP B O   1 
ATOM   4131 C CB  . TRP B 1 9   ? -31.212 32.167 37.954  1.00 10.43 ? 9   TRP B CB  1 
ATOM   4132 C CG  . TRP B 1 9   ? -31.806 30.896 37.377  1.00 10.08 ? 9   TRP B CG  1 
ATOM   4133 C CD1 . TRP B 1 9   ? -31.221 30.007 36.515  1.00 12.41 ? 9   TRP B CD1 1 
ATOM   4134 C CD2 . TRP B 1 9   ? -33.084 30.348 37.720  1.00 10.42 ? 9   TRP B CD2 1 
ATOM   4135 N NE1 . TRP B 1 9   ? -32.096 28.946 36.266  1.00 9.99  ? 9   TRP B NE1 1 
ATOM   4136 C CE2 . TRP B 1 9   ? -33.235 29.135 37.009  1.00 9.94  ? 9   TRP B CE2 1 
ATOM   4137 C CE3 . TRP B 1 9   ? -34.118 30.764 38.575  1.00 14.43 ? 9   TRP B CE3 1 
ATOM   4138 C CZ2 . TRP B 1 9   ? -34.395 28.351 37.098  1.00 11.41 ? 9   TRP B CZ2 1 
ATOM   4139 C CZ3 . TRP B 1 9   ? -35.263 29.967 38.676  1.00 13.78 ? 9   TRP B CZ3 1 
ATOM   4140 C CH2 . TRP B 1 9   ? -35.391 28.784 37.931  1.00 15.00 ? 9   TRP B CH2 1 
ATOM   4141 N N   . TRP B 1 10  ? -28.588 32.531 35.480  1.00 10.69 ? 10  TRP B N   1 
ATOM   4142 C CA  . TRP B 1 10  ? -28.253 32.980 34.136  1.00 10.54 ? 10  TRP B CA  1 
ATOM   4143 C C   . TRP B 1 10  ? -28.951 32.093 33.111  1.00 10.24 ? 10  TRP B C   1 
ATOM   4144 O O   . TRP B 1 10  ? -28.663 30.891 33.021  1.00 10.07 ? 10  TRP B O   1 
ATOM   4145 C CB  . TRP B 1 10  ? -26.741 32.940 33.930  1.00 7.83  ? 10  TRP B CB  1 
ATOM   4146 C CG  . TRP B 1 10  ? -25.901 33.777 34.893  1.00 9.59  ? 10  TRP B CG  1 
ATOM   4147 C CD1 . TRP B 1 10  ? -25.058 33.306 35.876  1.00 8.12  ? 10  TRP B CD1 1 
ATOM   4148 C CD2 . TRP B 1 10  ? -25.765 35.209 34.908  1.00 12.21 ? 10  TRP B CD2 1 
ATOM   4149 N NE1 . TRP B 1 10  ? -24.433 34.361 36.514  1.00 10.84 ? 10  TRP B NE1 1 
ATOM   4150 C CE2 . TRP B 1 10  ? -24.843 35.534 35.934  1.00 9.83  ? 10  TRP B CE2 1 
ATOM   4151 C CE3 . TRP B 1 10  ? -26.340 36.249 34.155  1.00 9.58  ? 10  TRP B CE3 1 
ATOM   4152 C CZ2 . TRP B 1 10  ? -24.497 36.848 36.239  1.00 10.42 ? 10  TRP B CZ2 1 
ATOM   4153 C CZ3 . TRP B 1 10  ? -25.996 37.551 34.461  1.00 10.43 ? 10  TRP B CZ3 1 
ATOM   4154 C CH2 . TRP B 1 10  ? -25.078 37.842 35.492  1.00 9.17  ? 10  TRP B CH2 1 
ATOM   4155 N N   . HIS B 1 11  ? -29.819 32.691 32.300  1.00 7.23  ? 11  HIS B N   1 
ATOM   4156 C CA  . HIS B 1 11  ? -30.647 31.953 31.342  1.00 7.82  ? 11  HIS B CA  1 
ATOM   4157 C C   . HIS B 1 11  ? -30.009 31.941 29.954  1.00 9.85  ? 11  HIS B C   1 
ATOM   4158 O O   . HIS B 1 11  ? -29.769 32.999 29.364  1.00 9.78  ? 11  HIS B O   1 
ATOM   4159 C CB  . HIS B 1 11  ? -32.050 32.571 31.288  1.00 9.84  ? 11  HIS B CB  1 
ATOM   4160 C CG  . HIS B 1 11  ? -32.816 32.197 30.061  1.00 9.70  ? 11  HIS B CG  1 
ATOM   4161 N ND1 . HIS B 1 11  ? -33.196 30.900 29.790  1.00 9.99  ? 11  HIS B ND1 1 
ATOM   4162 C CD2 . HIS B 1 11  ? -33.255 32.943 29.018  1.00 8.68  ? 11  HIS B CD2 1 
ATOM   4163 C CE1 . HIS B 1 11  ? -33.843 30.861 28.638  1.00 12.01 ? 11  HIS B CE1 1 
ATOM   4164 N NE2 . HIS B 1 11  ? -33.898 32.089 28.151  1.00 9.61  ? 11  HIS B NE2 1 
ATOM   4165 N N   . MET B 1 12  ? -29.757 30.738 29.429  1.00 6.97  ? 12  MET B N   1 
ATOM   4166 C CA  . MET B 1 12  ? -29.082 30.551 28.154  1.00 8.00  ? 12  MET B CA  1 
ATOM   4167 C C   . MET B 1 12  ? -30.066 29.937 27.170  1.00 12.51 ? 12  MET B C   1 
ATOM   4168 O O   . MET B 1 12  ? -30.677 28.908 27.473  1.00 8.56  ? 12  MET B O   1 
ATOM   4169 C CB  . MET B 1 12  ? -27.869 29.632 28.304  1.00 9.51  ? 12  MET B CB  1 
ATOM   4170 C CG  . MET B 1 12  ? -26.907 30.002 29.431  1.00 7.24  ? 12  MET B CG  1 
ATOM   4171 S SD  . MET B 1 12  ? -26.222 31.648 29.206  1.00 10.54 ? 12  MET B SD  1 
ATOM   4172 C CE  . MET B 1 12  ? -24.949 31.571 30.488  1.00 9.72  ? 12  MET B CE  1 
ATOM   4173 N N   . HIS B 1 13  ? -30.186 30.529 25.988  1.00 8.19  ? 13  HIS B N   1 
ATOM   4174 C CA  . HIS B 1 13  ? -31.145 29.992 25.030  1.00 8.87  ? 13  HIS B CA  1 
ATOM   4175 C C   . HIS B 1 13  ? -30.799 30.468 23.628  1.00 12.59 ? 13  HIS B C   1 
ATOM   4176 O O   . HIS B 1 13  ? -30.274 31.565 23.452  1.00 10.10 ? 13  HIS B O   1 
ATOM   4177 C CB  . HIS B 1 13  ? -32.581 30.426 25.394  1.00 9.48  ? 13  HIS B CB  1 
ATOM   4178 C CG  . HIS B 1 13  ? -33.576 30.213 24.293  1.00 8.56  ? 13  HIS B CG  1 
ATOM   4179 N ND1 . HIS B 1 13  ? -33.851 28.969 23.763  1.00 9.85  ? 13  HIS B ND1 1 
ATOM   4180 C CD2 . HIS B 1 13  ? -34.340 31.092 23.602  1.00 12.29 ? 13  HIS B CD2 1 
ATOM   4181 C CE1 . HIS B 1 13  ? -34.753 29.086 22.804  1.00 13.79 ? 13  HIS B CE1 1 
ATOM   4182 N NE2 . HIS B 1 13  ? -35.073 30.363 22.690  1.00 11.29 ? 13  HIS B NE2 1 
ATOM   4183 N N   . GLN B 1 14  ? -31.088 29.621 22.637  1.00 11.06 ? 14  GLN B N   1 
ATOM   4184 C CA  . GLN B 1 14  ? -31.096 29.998 21.228  1.00 11.73 ? 14  GLN B CA  1 
ATOM   4185 C C   . GLN B 1 14  ? -32.238 29.237 20.567  1.00 10.74 ? 14  GLN B C   1 
ATOM   4186 O O   . GLN B 1 14  ? -32.382 28.018 20.783  1.00 12.45 ? 14  GLN B O   1 
ATOM   4187 C CB  . GLN B 1 14  ? -29.784 29.663 20.481  1.00 12.73 ? 14  GLN B CB  1 
ATOM   4188 C CG  . GLN B 1 14  ? -28.530 30.436 20.934  1.00 8.45  ? 14  GLN B CG  1 
ATOM   4189 C CD  . GLN B 1 14  ? -28.620 31.948 20.690  1.00 10.52 ? 14  GLN B CD  1 
ATOM   4190 O OE1 . GLN B 1 14  ? -29.361 32.406 19.828  1.00 11.45 ? 14  GLN B OE1 1 
ATOM   4191 N NE2 . GLN B 1 14  ? -27.869 32.724 21.470  1.00 11.38 ? 14  GLN B NE2 1 
ATOM   4192 N N   . PRO B 1 15  ? -33.023 29.894 19.716  1.00 10.84 ? 15  PRO B N   1 
ATOM   4193 C CA  . PRO B 1 15  ? -33.990 29.153 18.893  1.00 11.86 ? 15  PRO B CA  1 
ATOM   4194 C C   . PRO B 1 15  ? -33.262 28.237 17.914  1.00 15.18 ? 15  PRO B C   1 
ATOM   4195 O O   . PRO B 1 15  ? -32.051 28.348 17.697  1.00 13.92 ? 15  PRO B O   1 
ATOM   4196 C CB  . PRO B 1 15  ? -34.770 30.257 18.164  1.00 10.51 ? 15  PRO B CB  1 
ATOM   4197 C CG  . PRO B 1 15  ? -33.775 31.425 18.102  1.00 12.17 ? 15  PRO B CG  1 
ATOM   4198 C CD  . PRO B 1 15  ? -32.967 31.334 19.379  1.00 9.27  ? 15  PRO B CD  1 
ATOM   4199 N N   . LEU B 1 16  ? -34.017 27.323 17.295  1.00 13.80 ? 16  LEU B N   1 
ATOM   4200 C CA  . LEU B 1 16  ? -33.411 26.365 16.369  1.00 14.82 ? 16  LEU B CA  1 
ATOM   4201 C C   . LEU B 1 16  ? -33.115 27.056 15.040  1.00 17.99 ? 16  LEU B C   1 
ATOM   4202 O O   . LEU B 1 16  ? -34.032 27.361 14.272  1.00 19.13 ? 16  LEU B O   1 
ATOM   4203 C CB  . LEU B 1 16  ? -34.315 25.150 16.167  1.00 17.48 ? 16  LEU B CB  1 
ATOM   4204 C CG  . LEU B 1 16  ? -33.741 24.043 15.268  1.00 17.68 ? 16  LEU B CG  1 
ATOM   4205 C CD1 . LEU B 1 16  ? -32.374 23.609 15.777  1.00 19.24 ? 16  LEU B CD1 1 
ATOM   4206 C CD2 . LEU B 1 16  ? -34.704 22.856 15.153  1.00 19.47 ? 16  LEU B CD2 1 
ATOM   4207 N N   . TYR B 1 17  ? -31.832 27.291 14.760  1.00 17.90 ? 17  TYR B N   1 
ATOM   4208 C CA  . TYR B 1 17  ? -31.403 27.921 13.511  1.00 19.93 ? 17  TYR B CA  1 
ATOM   4209 C C   . TYR B 1 17  ? -31.242 26.939 12.358  1.00 17.57 ? 17  TYR B C   1 
ATOM   4210 O O   . TYR B 1 17  ? -30.891 27.367 11.255  1.00 18.14 ? 17  TYR B O   1 
ATOM   4211 C CB  . TYR B 1 17  ? -30.066 28.656 13.705  1.00 17.90 ? 17  TYR B CB  1 
ATOM   4212 C CG  . TYR B 1 17  ? -30.136 29.803 14.694  1.00 16.08 ? 17  TYR B CG  1 
ATOM   4213 C CD1 . TYR B 1 17  ? -30.949 30.905 14.447  1.00 18.92 ? 17  TYR B CD1 1 
ATOM   4214 C CD2 . TYR B 1 17  ? -29.378 29.789 15.860  1.00 12.11 ? 17  TYR B CD2 1 
ATOM   4215 C CE1 . TYR B 1 17  ? -31.025 31.958 15.336  1.00 14.54 ? 17  TYR B CE1 1 
ATOM   4216 C CE2 . TYR B 1 17  ? -29.443 30.843 16.765  1.00 12.96 ? 17  TYR B CE2 1 
ATOM   4217 C CZ  . TYR B 1 17  ? -30.267 31.929 16.499  1.00 12.91 ? 17  TYR B CZ  1 
ATOM   4218 O OH  . TYR B 1 17  ? -30.331 32.970 17.410  1.00 10.60 ? 17  TYR B OH  1 
ATOM   4219 N N   . ARG B 1 18  ? -31.461 25.645 12.585  1.00 18.56 ? 18  ARG B N   1 
ATOM   4220 C CA  . ARG B 1 18  ? -31.162 24.609 11.601  1.00 16.17 ? 18  ARG B CA  1 
ATOM   4221 C C   . ARG B 1 18  ? -32.385 24.400 10.717  1.00 24.71 ? 18  ARG B C   1 
ATOM   4222 O O   . ARG B 1 18  ? -33.391 23.841 11.162  1.00 19.48 ? 18  ARG B O   1 
ATOM   4223 C CB  . ARG B 1 18  ? -30.765 23.307 12.297  1.00 20.32 ? 18  ARG B CB  1 
ATOM   4224 C CG  . ARG B 1 18  ? -30.317 22.176 11.351  1.00 24.82 ? 18  ARG B CG  1 
ATOM   4225 C CD  . ARG B 1 18  ? -30.242 20.849 12.116  1.00 27.65 ? 18  ARG B CD  1 
ATOM   4226 N NE  . ARG B 1 18  ? -29.714 19.744 11.316  1.00 33.09 ? 18  ARG B NE  1 
ATOM   4227 C CZ  . ARG B 1 18  ? -30.426 19.014 10.463  1.00 31.25 ? 18  ARG B CZ  1 
ATOM   4228 N NH1 . ARG B 1 18  ? -31.719 19.260 10.273  1.00 31.68 ? 18  ARG B NH1 1 
ATOM   4229 N NH2 . ARG B 1 18  ? -29.840 18.028 9.793   1.00 35.15 ? 18  ARG B NH2 1 
ATOM   4230 N N   . GLU B 1 19  ? -32.293 24.849 9.475   1.00 25.45 ? 19  GLU B N   1 
ATOM   4231 C CA  . GLU B 1 19  ? -33.395 24.698 8.533   1.00 27.13 ? 19  GLU B CA  1 
ATOM   4232 C C   . GLU B 1 19  ? -33.625 23.216 8.249   1.00 30.20 ? 19  GLU B C   1 
ATOM   4233 O O   . GLU B 1 19  ? -32.669 22.492 7.946   1.00 27.45 ? 19  GLU B O   1 
ATOM   4234 C CB  . GLU B 1 19  ? -33.075 25.460 7.252   1.00 29.97 ? 19  GLU B CB  1 
ATOM   4235 C CG  . GLU B 1 19  ? -34.286 25.914 6.456   1.00 37.59 ? 19  GLU B CG  1 
ATOM   4236 C CD  . GLU B 1 19  ? -34.760 24.860 5.494   1.00 45.15 ? 19  GLU B CD  1 
ATOM   4237 O OE1 . GLU B 1 19  ? -33.952 23.976 5.142   1.00 48.58 ? 19  GLU B OE1 1 
ATOM   4238 O OE2 . GLU B 1 19  ? -35.936 24.918 5.082   1.00 51.59 ? 19  GLU B OE2 1 
ATOM   4239 N N   . PRO B 1 20  ? -34.868 22.725 8.339   1.00 25.34 ? 20  PRO B N   1 
ATOM   4240 C CA  . PRO B 1 20  ? -35.082 21.268 8.342   1.00 30.02 ? 20  PRO B CA  1 
ATOM   4241 C C   . PRO B 1 20  ? -34.930 20.596 6.983   1.00 31.74 ? 20  PRO B C   1 
ATOM   4242 O O   . PRO B 1 20  ? -34.753 19.371 6.943   1.00 38.37 ? 20  PRO B O   1 
ATOM   4243 C CB  . PRO B 1 20  ? -36.518 21.128 8.872   1.00 31.07 ? 20  PRO B CB  1 
ATOM   4244 C CG  . PRO B 1 20  ? -37.188 22.403 8.478   1.00 29.54 ? 20  PRO B CG  1 
ATOM   4245 C CD  . PRO B 1 20  ? -36.123 23.476 8.532   1.00 25.65 ? 20  PRO B CD  1 
ATOM   4246 N N   . TYR B 1 21  ? -34.990 21.336 5.878   1.00 26.00 ? 21  TYR B N   1 
ATOM   4247 C CA  . TYR B 1 21  ? -34.873 20.723 4.560   1.00 31.18 ? 21  TYR B CA  1 
ATOM   4248 C C   . TYR B 1 21  ? -33.428 20.629 4.091   1.00 36.30 ? 21  TYR B C   1 
ATOM   4249 O O   . TYR B 1 21  ? -33.039 19.623 3.490   1.00 35.66 ? 21  TYR B O   1 
ATOM   4250 C CB  . TYR B 1 21  ? -35.729 21.494 3.553   1.00 26.12 ? 21  TYR B CB  1 
ATOM   4251 C CG  . TYR B 1 21  ? -37.198 21.284 3.837   1.00 33.15 ? 21  TYR B CG  1 
ATOM   4252 C CD1 . TYR B 1 21  ? -37.867 20.164 3.349   1.00 33.64 ? 21  TYR B CD1 1 
ATOM   4253 C CD2 . TYR B 1 21  ? -37.900 22.166 4.645   1.00 31.34 ? 21  TYR B CD2 1 
ATOM   4254 C CE1 . TYR B 1 21  ? -39.199 19.954 3.630   1.00 36.53 ? 21  TYR B CE1 1 
ATOM   4255 C CE2 . TYR B 1 21  ? -39.236 21.963 4.937   1.00 34.66 ? 21  TYR B CE2 1 
ATOM   4256 C CZ  . TYR B 1 21  ? -39.878 20.857 4.430   1.00 34.81 ? 21  TYR B CZ  1 
ATOM   4257 O OH  . TYR B 1 21  ? -41.205 20.655 4.722   1.00 39.86 ? 21  TYR B OH  1 
ATOM   4258 N N   . THR B 1 22  ? -32.618 21.647 4.370   1.00 32.29 ? 22  THR B N   1 
ATOM   4259 C CA  . THR B 1 22  ? -31.212 21.630 3.989   1.00 32.09 ? 22  THR B CA  1 
ATOM   4260 C C   . THR B 1 22  ? -30.293 21.194 5.122   1.00 33.10 ? 22  THR B C   1 
ATOM   4261 O O   . THR B 1 22  ? -29.146 20.823 4.862   1.00 28.17 ? 22  THR B O   1 
ATOM   4262 C CB  . THR B 1 22  ? -30.774 23.023 3.514   1.00 34.58 ? 22  THR B CB  1 
ATOM   4263 O OG1 . THR B 1 22  ? -30.806 23.937 4.622   1.00 32.79 ? 22  THR B OG1 1 
ATOM   4264 C CG2 . THR B 1 22  ? -31.700 23.531 2.420   1.00 35.62 ? 22  THR B CG2 1 
ATOM   4265 N N   . GLY B 1 23  ? -30.761 21.240 6.364   1.00 29.03 ? 23  GLY B N   1 
ATOM   4266 C CA  . GLY B 1 23  ? -29.879 20.994 7.484   1.00 34.51 ? 23  GLY B CA  1 
ATOM   4267 C C   . GLY B 1 23  ? -28.878 22.095 7.757   1.00 33.78 ? 23  GLY B C   1 
ATOM   4268 O O   . GLY B 1 23  ? -27.970 21.894 8.564   1.00 36.91 ? 23  GLY B O   1 
ATOM   4269 N N   . GLU B 1 24  ? -29.012 23.254 7.115   1.00 25.36 ? 24  GLU B N   1 
ATOM   4270 C CA  . GLU B 1 24  ? -28.069 24.347 7.326   1.00 25.06 ? 24  GLU B CA  1 
ATOM   4271 C C   . GLU B 1 24  ? -28.477 25.185 8.526   1.00 25.25 ? 24  GLU B C   1 
ATOM   4272 O O   . GLU B 1 24  ? -29.658 25.511 8.689   1.00 21.15 ? 24  GLU B O   1 
ATOM   4273 C CB  . GLU B 1 24  ? -28.010 25.265 6.104   1.00 33.51 ? 24  GLU B CB  1 
ATOM   4274 C CG  . GLU B 1 24  ? -27.247 24.735 4.900   1.00 46.51 ? 24  GLU B CG  1 
ATOM   4275 C CD  . GLU B 1 24  ? -27.567 25.513 3.639   1.00 59.00 ? 24  GLU B CD  1 
ATOM   4276 O OE1 . GLU B 1 24  ? -28.435 26.413 3.697   1.00 63.20 ? 24  GLU B OE1 1 
ATOM   4277 O OE2 . GLU B 1 24  ? -26.937 25.239 2.596   1.00 65.68 ? 24  GLU B OE2 1 
ATOM   4278 N N   . TYR B 1 25  ? -27.492 25.562 9.348   1.00 22.67 ? 25  TYR B N   1 
ATOM   4279 C CA  . TYR B 1 25  ? -27.721 26.599 10.339  1.00 20.97 ? 25  TYR B CA  1 
ATOM   4280 C C   . TYR B 1 25  ? -27.649 27.954 9.646   1.00 18.81 ? 25  TYR B C   1 
ATOM   4281 O O   . TYR B 1 25  ? -26.586 28.342 9.140   1.00 22.99 ? 25  TYR B O   1 
ATOM   4282 C CB  . TYR B 1 25  ? -26.718 26.523 11.486  1.00 18.72 ? 25  TYR B CB  1 
ATOM   4283 C CG  . TYR B 1 25  ? -27.010 25.419 12.479  1.00 20.51 ? 25  TYR B CG  1 
ATOM   4284 C CD1 . TYR B 1 25  ? -26.904 24.069 12.136  1.00 21.93 ? 25  TYR B CD1 1 
ATOM   4285 C CD2 . TYR B 1 25  ? -27.492 25.735 13.740  1.00 20.34 ? 25  TYR B CD2 1 
ATOM   4286 C CE1 . TYR B 1 25  ? -27.211 23.075 13.075  1.00 27.12 ? 25  TYR B CE1 1 
ATOM   4287 C CE2 . TYR B 1 25  ? -27.800 24.767 14.660  1.00 18.04 ? 25  TYR B CE2 1 
ATOM   4288 C CZ  . TYR B 1 25  ? -27.657 23.443 14.336  1.00 24.56 ? 25  TYR B CZ  1 
ATOM   4289 O OH  . TYR B 1 25  ? -27.974 22.508 15.300  1.00 18.98 ? 25  TYR B OH  1 
ATOM   4290 N N   . LEU B 1 26  ? -28.773 28.659 9.614   1.00 19.39 ? 26  LEU B N   1 
ATOM   4291 C CA  . LEU B 1 26  ? -28.910 29.854 8.798   1.00 21.72 ? 26  LEU B CA  1 
ATOM   4292 C C   . LEU B 1 26  ? -28.440 31.118 9.495   1.00 21.07 ? 26  LEU B C   1 
ATOM   4293 O O   . LEU B 1 26  ? -28.306 32.159 8.842   1.00 19.05 ? 26  LEU B O   1 
ATOM   4294 C CB  . LEU B 1 26  ? -30.363 30.027 8.359   1.00 25.52 ? 26  LEU B CB  1 
ATOM   4295 C CG  . LEU B 1 26  ? -30.902 28.872 7.540   1.00 21.79 ? 26  LEU B CG  1 
ATOM   4296 C CD1 . LEU B 1 26  ? -32.312 29.231 7.079   1.00 25.23 ? 26  LEU B CD1 1 
ATOM   4297 C CD2 . LEU B 1 26  ? -29.971 28.587 6.368   1.00 23.78 ? 26  LEU B CD2 1 
ATOM   4298 N N   . LEU B 1 27  ? -28.177 31.046 10.790  1.00 19.29 ? 27  LEU B N   1 
ATOM   4299 C CA  . LEU B 1 27  ? -27.584 32.125 11.553  1.00 16.99 ? 27  LEU B CA  1 
ATOM   4300 C C   . LEU B 1 27  ? -26.560 31.487 12.472  1.00 14.12 ? 27  LEU B C   1 
ATOM   4301 O O   . LEU B 1 27  ? -26.729 30.327 12.879  1.00 18.25 ? 27  LEU B O   1 
ATOM   4302 C CB  . LEU B 1 27  ? -28.635 32.897 12.370  1.00 25.03 ? 27  LEU B CB  1 
ATOM   4303 C CG  . LEU B 1 27  ? -29.588 33.732 11.504  1.00 21.53 ? 27  LEU B CG  1 
ATOM   4304 C CD1 . LEU B 1 27  ? -30.724 34.294 12.346  1.00 22.45 ? 27  LEU B CD1 1 
ATOM   4305 C CD2 . LEU B 1 27  ? -28.835 34.847 10.808  1.00 22.64 ? 27  LEU B CD2 1 
ATOM   4306 N N   . PRO B 1 28  ? -25.467 32.188 12.768  1.00 16.95 ? 28  PRO B N   1 
ATOM   4307 C CA  . PRO B 1 28  ? -24.367 31.595 13.548  1.00 11.61 ? 28  PRO B CA  1 
ATOM   4308 C C   . PRO B 1 28  ? -24.413 31.883 15.045  1.00 18.65 ? 28  PRO B C   1 
ATOM   4309 O O   . PRO B 1 28  ? -23.395 31.667 15.709  1.00 16.62 ? 28  PRO B O   1 
ATOM   4310 C CB  . PRO B 1 28  ? -23.146 32.272 12.917  1.00 13.04 ? 28  PRO B CB  1 
ATOM   4311 C CG  . PRO B 1 28  ? -23.662 33.707 12.687  1.00 13.63 ? 28  PRO B CG  1 
ATOM   4312 C CD  . PRO B 1 28  ? -25.124 33.540 12.285  1.00 17.06 ? 28  PRO B CD  1 
ATOM   4313 N N   . TRP B 1 29  ? -25.529 32.398 15.571  1.00 13.64 ? 29  TRP B N   1 
ATOM   4314 C CA  . TRP B 1 29  ? -25.534 32.920 16.934  1.00 12.35 ? 29  TRP B CA  1 
ATOM   4315 C C   . TRP B 1 29  ? -25.278 31.841 17.979  1.00 14.93 ? 29  TRP B C   1 
ATOM   4316 O O   . TRP B 1 29  ? -24.735 32.145 19.052  1.00 14.06 ? 29  TRP B O   1 
ATOM   4317 C CB  . TRP B 1 29  ? -26.867 33.621 17.218  1.00 10.93 ? 29  TRP B CB  1 
ATOM   4318 C CG  . TRP B 1 29  ? -27.134 34.818 16.315  1.00 13.76 ? 29  TRP B CG  1 
ATOM   4319 C CD1 . TRP B 1 29  ? -28.182 34.985 15.443  1.00 15.81 ? 29  TRP B CD1 1 
ATOM   4320 C CD2 . TRP B 1 29  ? -26.340 36.005 16.221  1.00 14.07 ? 29  TRP B CD2 1 
ATOM   4321 N NE1 . TRP B 1 29  ? -28.087 36.212 14.822  1.00 20.74 ? 29  TRP B NE1 1 
ATOM   4322 C CE2 . TRP B 1 29  ? -26.958 36.849 15.276  1.00 16.65 ? 29  TRP B CE2 1 
ATOM   4323 C CE3 . TRP B 1 29  ? -25.168 36.438 16.853  1.00 19.61 ? 29  TRP B CE3 1 
ATOM   4324 C CZ2 . TRP B 1 29  ? -26.454 38.105 14.962  1.00 21.64 ? 29  TRP B CZ2 1 
ATOM   4325 C CZ3 . TRP B 1 29  ? -24.662 37.681 16.528  1.00 22.05 ? 29  TRP B CZ3 1 
ATOM   4326 C CH2 . TRP B 1 29  ? -25.302 38.499 15.594  1.00 24.56 ? 29  TRP B CH2 1 
ATOM   4327 N N   . THR B 1 30  ? -25.671 30.591 17.716  1.00 14.97 ? 30  THR B N   1 
ATOM   4328 C CA  . THR B 1 30  ? -25.339 29.530 18.662  1.00 13.03 ? 30  THR B CA  1 
ATOM   4329 C C   . THR B 1 30  ? -23.836 29.332 18.723  1.00 13.64 ? 30  THR B C   1 
ATOM   4330 O O   . THR B 1 30  ? -23.253 29.250 19.812  1.00 13.66 ? 30  THR B O   1 
ATOM   4331 C CB  . THR B 1 30  ? -26.036 28.223 18.282  1.00 14.33 ? 30  THR B CB  1 
ATOM   4332 O OG1 . THR B 1 30  ? -27.458 28.394 18.406  1.00 16.15 ? 30  THR B OG1 1 
ATOM   4333 C CG2 . THR B 1 30  ? -25.580 27.080 19.213  1.00 19.38 ? 30  THR B CG2 1 
ATOM   4334 N N   . PHE B 1 31  ? -23.188 29.278 17.557  1.00 14.73 ? 31  PHE B N   1 
ATOM   4335 C CA  . PHE B 1 31  ? -21.737 29.145 17.534  1.00 13.69 ? 31  PHE B CA  1 
ATOM   4336 C C   . PHE B 1 31  ? -21.062 30.286 18.294  1.00 12.30 ? 31  PHE B C   1 
ATOM   4337 O O   . PHE B 1 31  ? -20.215 30.051 19.165  1.00 14.91 ? 31  PHE B O   1 
ATOM   4338 C CB  . PHE B 1 31  ? -21.241 29.085 16.089  1.00 11.84 ? 31  PHE B CB  1 
ATOM   4339 C CG  . PHE B 1 31  ? -19.740 29.077 15.972  1.00 14.64 ? 31  PHE B CG  1 
ATOM   4340 C CD1 . PHE B 1 31  ? -19.015 27.899 16.102  1.00 14.82 ? 31  PHE B CD1 1 
ATOM   4341 C CD2 . PHE B 1 31  ? -19.051 30.267 15.777  1.00 14.50 ? 31  PHE B CD2 1 
ATOM   4342 C CE1 . PHE B 1 31  ? -17.628 27.902 16.003  1.00 16.58 ? 31  PHE B CE1 1 
ATOM   4343 C CE2 . PHE B 1 31  ? -17.646 30.279 15.682  1.00 15.39 ? 31  PHE B CE2 1 
ATOM   4344 C CZ  . PHE B 1 31  ? -16.943 29.103 15.793  1.00 16.38 ? 31  PHE B CZ  1 
ATOM   4345 N N   . PHE B 1 32  ? -21.420 31.536 17.978  1.00 13.41 ? 32  PHE B N   1 
ATOM   4346 C CA  . PHE B 1 32  ? -20.706 32.672 18.559  1.00 13.33 ? 32  PHE B CA  1 
ATOM   4347 C C   . PHE B 1 32  ? -20.960 32.815 20.062  1.00 15.36 ? 32  PHE B C   1 
ATOM   4348 O O   . PHE B 1 32  ? -20.042 33.166 20.824  1.00 11.38 ? 32  PHE B O   1 
ATOM   4349 C CB  . PHE B 1 32  ? -21.076 33.958 17.816  1.00 10.53 ? 32  PHE B CB  1 
ATOM   4350 C CG  . PHE B 1 32  ? -20.376 34.085 16.483  1.00 14.84 ? 32  PHE B CG  1 
ATOM   4351 C CD1 . PHE B 1 32  ? -18.992 34.074 16.421  1.00 18.48 ? 32  PHE B CD1 1 
ATOM   4352 C CD2 . PHE B 1 32  ? -21.097 34.217 15.303  1.00 17.93 ? 32  PHE B CD2 1 
ATOM   4353 C CE1 . PHE B 1 32  ? -18.322 34.177 15.200  1.00 17.04 ? 32  PHE B CE1 1 
ATOM   4354 C CE2 . PHE B 1 32  ? -20.439 34.329 14.089  1.00 20.37 ? 32  PHE B CE2 1 
ATOM   4355 C CZ  . PHE B 1 32  ? -19.050 34.310 14.041  1.00 21.42 ? 32  PHE B CZ  1 
ATOM   4356 N N   . HIS B 1 33  ? -22.185 32.554 20.518  1.00 9.89  ? 33  HIS B N   1 
ATOM   4357 C CA  . HIS B 1 33  ? -22.418 32.617 21.959  1.00 10.49 ? 33  HIS B CA  1 
ATOM   4358 C C   . HIS B 1 33  ? -21.867 31.394 22.688  1.00 11.35 ? 33  HIS B C   1 
ATOM   4359 O O   . HIS B 1 33  ? -21.497 31.503 23.858  1.00 11.70 ? 33  HIS B O   1 
ATOM   4360 C CB  . HIS B 1 33  ? -23.907 32.820 22.263  1.00 8.88  ? 33  HIS B CB  1 
ATOM   4361 C CG  . HIS B 1 33  ? -24.374 34.214 21.987  1.00 10.81 ? 33  HIS B CG  1 
ATOM   4362 N ND1 . HIS B 1 33  ? -23.962 35.295 22.737  1.00 10.63 ? 33  HIS B ND1 1 
ATOM   4363 C CD2 . HIS B 1 33  ? -25.186 34.708 21.022  1.00 10.44 ? 33  HIS B CD2 1 
ATOM   4364 C CE1 . HIS B 1 33  ? -24.514 36.396 22.255  1.00 10.82 ? 33  HIS B CE1 1 
ATOM   4365 N NE2 . HIS B 1 33  ? -25.270 36.066 21.219  1.00 10.61 ? 33  HIS B NE2 1 
ATOM   4366 N N   . ALA B 1 34  ? -21.747 30.246 22.019  1.00 11.09 ? 34  ALA B N   1 
ATOM   4367 C CA  . ALA B 1 34  ? -21.033 29.124 22.630  1.00 13.25 ? 34  ALA B CA  1 
ATOM   4368 C C   . ALA B 1 34  ? -19.563 29.462 22.866  1.00 14.54 ? 34  ALA B C   1 
ATOM   4369 O O   . ALA B 1 34  ? -19.027 29.210 23.952  1.00 15.55 ? 34  ALA B O   1 
ATOM   4370 C CB  . ALA B 1 34  ? -21.167 27.866 21.767  1.00 11.67 ? 34  ALA B CB  1 
ATOM   4371 N N   . VAL B 1 35  ? -18.888 30.044 21.864  1.00 12.82 ? 35  VAL B N   1 
ATOM   4372 C CA  . VAL B 1 35  ? -17.452 30.282 22.021  1.00 14.44 ? 35  VAL B CA  1 
ATOM   4373 C C   . VAL B 1 35  ? -17.205 31.445 22.971  1.00 14.12 ? 35  VAL B C   1 
ATOM   4374 O O   . VAL B 1 35  ? -16.170 31.497 23.653  1.00 13.22 ? 35  VAL B O   1 
ATOM   4375 C CB  . VAL B 1 35  ? -16.747 30.498 20.661  1.00 14.68 ? 35  VAL B CB  1 
ATOM   4376 C CG1 . VAL B 1 35  ? -17.047 29.335 19.712  1.00 17.07 ? 35  VAL B CG1 1 
ATOM   4377 C CG2 . VAL B 1 35  ? -17.123 31.836 20.003  1.00 16.83 ? 35  VAL B CG2 1 
ATOM   4378 N N   . LYS B 1 36  ? -18.144 32.377 23.057  1.00 12.40 ? 36  LYS B N   1 
ATOM   4379 C CA  . LYS B 1 36  ? -17.940 33.558 23.886  1.00 10.75 ? 36  LYS B CA  1 
ATOM   4380 C C   . LYS B 1 36  ? -18.492 33.395 25.299  1.00 9.46  ? 36  LYS B C   1 
ATOM   4381 O O   . LYS B 1 36  ? -17.824 33.789 26.269  1.00 11.65 ? 36  LYS B O   1 
ATOM   4382 C CB  . LYS B 1 36  ? -18.575 34.782 23.220  1.00 12.05 ? 36  LYS B CB  1 
ATOM   4383 C CG  . LYS B 1 36  ? -18.188 36.092 23.905  1.00 11.41 ? 36  LYS B CG  1 
ATOM   4384 C CD  . LYS B 1 36  ? -18.648 37.339 23.145  1.00 12.72 ? 36  LYS B CD  1 
ATOM   4385 C CE  . LYS B 1 36  ? -20.150 37.642 23.332  1.00 12.00 ? 36  LYS B CE  1 
ATOM   4386 N NZ  . LYS B 1 36  ? -20.533 38.044 24.727  1.00 10.52 ? 36  LYS B NZ  1 
ATOM   4387 N N   . ASP B 1 37  ? -19.682 32.800 25.447  1.00 9.33  ? 37  ASP B N   1 
ATOM   4388 C CA  . ASP B 1 37  ? -20.392 32.889 26.726  1.00 10.84 ? 37  ASP B CA  1 
ATOM   4389 C C   . ASP B 1 37  ? -20.761 31.549 27.346  1.00 10.04 ? 37  ASP B C   1 
ATOM   4390 O O   . ASP B 1 37  ? -20.680 31.405 28.573  1.00 9.14  ? 37  ASP B O   1 
ATOM   4391 C CB  . ASP B 1 37  ? -21.671 33.682 26.534  1.00 8.16  ? 37  ASP B CB  1 
ATOM   4392 C CG  . ASP B 1 37  ? -21.436 35.012 25.870  1.00 12.32 ? 37  ASP B CG  1 
ATOM   4393 O OD1 . ASP B 1 37  ? -20.719 35.873 26.434  1.00 11.75 ? 37  ASP B OD1 1 
ATOM   4394 O OD2 . ASP B 1 37  ? -21.919 35.148 24.735  1.00 11.33 ? 37  ASP B OD2 1 
ATOM   4395 N N   . TYR B 1 38  ? -21.210 30.576 26.546  1.00 11.23 ? 38  TYR B N   1 
ATOM   4396 C CA  . TYR B 1 38  ? -21.846 29.405 27.142  1.00 8.20  ? 38  TYR B CA  1 
ATOM   4397 C C   . TYR B 1 38  ? -20.855 28.540 27.899  1.00 11.00 ? 38  TYR B C   1 
ATOM   4398 O O   . TYR B 1 38  ? -21.232 27.931 28.902  1.00 11.58 ? 38  TYR B O   1 
ATOM   4399 C CB  . TYR B 1 38  ? -22.565 28.574 26.083  1.00 8.51  ? 38  TYR B CB  1 
ATOM   4400 C CG  . TYR B 1 38  ? -23.773 29.275 25.496  1.00 10.64 ? 38  TYR B CG  1 
ATOM   4401 C CD1 . TYR B 1 38  ? -24.547 30.146 26.273  1.00 10.25 ? 38  TYR B CD1 1 
ATOM   4402 C CD2 . TYR B 1 38  ? -24.128 29.098 24.152  1.00 12.39 ? 38  TYR B CD2 1 
ATOM   4403 C CE1 . TYR B 1 38  ? -25.658 30.807 25.725  1.00 12.32 ? 38  TYR B CE1 1 
ATOM   4404 C CE2 . TYR B 1 38  ? -25.228 29.777 23.602  1.00 12.70 ? 38  TYR B CE2 1 
ATOM   4405 C CZ  . TYR B 1 38  ? -25.982 30.606 24.392  1.00 10.26 ? 38  TYR B CZ  1 
ATOM   4406 O OH  . TYR B 1 38  ? -27.066 31.274 23.853  1.00 9.77  ? 38  TYR B OH  1 
ATOM   4407 N N   . TYR B 1 39  ? -19.608 28.452 27.445  1.00 9.29  ? 39  TYR B N   1 
ATOM   4408 C CA  . TYR B 1 39  ? -18.605 27.766 28.260  1.00 9.81  ? 39  TYR B CA  1 
ATOM   4409 C C   . TYR B 1 39  ? -18.077 28.678 29.367  1.00 10.78 ? 39  TYR B C   1 
ATOM   4410 O O   . TYR B 1 39  ? -17.904 28.250 30.517  1.00 12.44 ? 39  TYR B O   1 
ATOM   4411 C CB  . TYR B 1 39  ? -17.448 27.278 27.377  1.00 14.38 ? 39  TYR B CB  1 
ATOM   4412 C CG  . TYR B 1 39  ? -16.284 26.701 28.169  1.00 18.29 ? 39  TYR B CG  1 
ATOM   4413 C CD1 . TYR B 1 39  ? -16.278 25.368 28.565  1.00 15.08 ? 39  TYR B CD1 1 
ATOM   4414 C CD2 . TYR B 1 39  ? -15.211 27.495 28.549  1.00 11.75 ? 39  TYR B CD2 1 
ATOM   4415 C CE1 . TYR B 1 39  ? -15.228 24.844 29.304  1.00 17.65 ? 39  TYR B CE1 1 
ATOM   4416 C CE2 . TYR B 1 39  ? -14.147 26.974 29.301  1.00 14.97 ? 39  TYR B CE2 1 
ATOM   4417 C CZ  . TYR B 1 39  ? -14.166 25.651 29.665  1.00 17.24 ? 39  TYR B CZ  1 
ATOM   4418 O OH  . TYR B 1 39  ? -13.132 25.117 30.401  1.00 20.58 ? 39  TYR B OH  1 
ATOM   4419 N N   . ASP B 1 40  ? -17.835 29.941 29.040  1.00 9.91  ? 40  ASP B N   1 
ATOM   4420 C CA  . ASP B 1 40  ? -17.082 30.810 29.938  1.00 10.76 ? 40  ASP B CA  1 
ATOM   4421 C C   . ASP B 1 40  ? -17.899 31.284 31.130  1.00 11.00 ? 40  ASP B C   1 
ATOM   4422 O O   . ASP B 1 40  ? -17.331 31.494 32.212  1.00 11.04 ? 40  ASP B O   1 
ATOM   4423 C CB  . ASP B 1 40  ? -16.522 31.977 29.136  1.00 10.26 ? 40  ASP B CB  1 
ATOM   4424 C CG  . ASP B 1 40  ? -15.205 31.621 28.486  1.00 15.11 ? 40  ASP B CG  1 
ATOM   4425 O OD1 . ASP B 1 40  ? -14.229 31.392 29.241  1.00 14.53 ? 40  ASP B OD1 1 
ATOM   4426 O OD2 . ASP B 1 40  ? -15.171 31.478 27.236  1.00 15.10 ? 40  ASP B OD2 1 
ATOM   4427 N N   . MET B 1 41  ? -19.215 31.433 30.981  1.00 9.08  ? 41  MET B N   1 
ATOM   4428 C CA  . MET B 1 41  ? -20.019 31.870 32.120  1.00 9.36  ? 41  MET B CA  1 
ATOM   4429 C C   . MET B 1 41  ? -19.961 30.886 33.281  1.00 10.02 ? 41  MET B C   1 
ATOM   4430 O O   . MET B 1 41  ? -19.632 31.313 34.402  1.00 9.04  ? 41  MET B O   1 
ATOM   4431 C CB  . MET B 1 41  ? -21.450 32.181 31.657  1.00 7.79  ? 41  MET B CB  1 
ATOM   4432 C CG  . MET B 1 41  ? -21.553 33.558 30.963  1.00 8.61  ? 41  MET B CG  1 
ATOM   4433 S SD  . MET B 1 41  ? -21.338 34.962 32.090  1.00 9.68  ? 41  MET B SD  1 
ATOM   4434 C CE  . MET B 1 41  ? -22.922 34.977 32.906  1.00 7.04  ? 41  MET B CE  1 
ATOM   4435 N N   . PRO B 1 42  ? -20.206 29.579 33.102  1.00 11.78 ? 42  PRO B N   1 
ATOM   4436 C CA  . PRO B 1 42  ? -19.992 28.664 34.230  1.00 11.25 ? 42  PRO B CA  1 
ATOM   4437 C C   . PRO B 1 42  ? -18.530 28.503 34.588  1.00 14.61 ? 42  PRO B C   1 
ATOM   4438 O O   . PRO B 1 42  ? -18.204 28.237 35.752  1.00 14.60 ? 42  PRO B O   1 
ATOM   4439 C CB  . PRO B 1 42  ? -20.609 27.341 33.746  1.00 11.45 ? 42  PRO B CB  1 
ATOM   4440 C CG  . PRO B 1 42  ? -20.574 27.421 32.252  1.00 14.16 ? 42  PRO B CG  1 
ATOM   4441 C CD  . PRO B 1 42  ? -20.785 28.894 31.928  1.00 10.09 ? 42  PRO B CD  1 
ATOM   4442 N N   . ALA B 1 43  ? -17.630 28.668 33.621  1.00 13.23 ? 43  ALA B N   1 
ATOM   4443 C CA  . ALA B 1 43  ? -16.217 28.480 33.899  1.00 13.54 ? 43  ALA B CA  1 
ATOM   4444 C C   . ALA B 1 43  ? -15.679 29.501 34.896  1.00 16.99 ? 43  ALA B C   1 
ATOM   4445 O O   . ALA B 1 43  ? -14.625 29.259 35.483  1.00 15.44 ? 43  ALA B O   1 
ATOM   4446 C CB  . ALA B 1 43  ? -15.414 28.529 32.596  1.00 14.38 ? 43  ALA B CB  1 
ATOM   4447 N N   . TYR B 1 44  ? -16.384 30.620 35.119  1.00 13.99 ? 44  TYR B N   1 
ATOM   4448 C CA  . TYR B 1 44  ? -15.985 31.538 36.189  1.00 19.36 ? 44  TYR B CA  1 
ATOM   4449 C C   . TYR B 1 44  ? -15.899 30.832 37.538  1.00 16.26 ? 44  TYR B C   1 
ATOM   4450 O O   . TYR B 1 44  ? -15.090 31.218 38.394  1.00 16.03 ? 44  TYR B O   1 
ATOM   4451 C CB  . TYR B 1 44  ? -16.967 32.706 36.307  1.00 12.12 ? 44  TYR B CB  1 
ATOM   4452 C CG  . TYR B 1 44  ? -16.711 33.872 35.375  1.00 14.00 ? 44  TYR B CG  1 
ATOM   4453 C CD1 . TYR B 1 44  ? -15.862 34.913 35.747  1.00 17.65 ? 44  TYR B CD1 1 
ATOM   4454 C CD2 . TYR B 1 44  ? -17.336 33.938 34.133  1.00 11.24 ? 44  TYR B CD2 1 
ATOM   4455 C CE1 . TYR B 1 44  ? -15.636 35.993 34.892  1.00 16.15 ? 44  TYR B CE1 1 
ATOM   4456 C CE2 . TYR B 1 44  ? -17.111 34.993 33.268  1.00 11.44 ? 44  TYR B CE2 1 
ATOM   4457 C CZ  . TYR B 1 44  ? -16.271 36.026 33.658  1.00 12.48 ? 44  TYR B CZ  1 
ATOM   4458 O OH  . TYR B 1 44  ? -16.071 37.087 32.796  1.00 15.00 ? 44  TYR B OH  1 
ATOM   4459 N N   . LEU B 1 45  ? -16.720 29.799 37.750  1.00 15.64 ? 45  LEU B N   1 
ATOM   4460 C CA  . LEU B 1 45  ? -16.762 29.110 39.036  1.00 15.08 ? 45  LEU B CA  1 
ATOM   4461 C C   . LEU B 1 45  ? -15.485 28.323 39.338  1.00 14.47 ? 45  LEU B C   1 
ATOM   4462 O O   . LEU B 1 45  ? -15.275 27.932 40.495  1.00 17.18 ? 45  LEU B O   1 
ATOM   4463 C CB  . LEU B 1 45  ? -17.994 28.191 39.083  1.00 17.01 ? 45  LEU B CB  1 
ATOM   4464 C CG  . LEU B 1 45  ? -19.347 28.912 39.132  1.00 15.67 ? 45  LEU B CG  1 
ATOM   4465 C CD1 . LEU B 1 45  ? -20.498 27.958 38.792  1.00 14.78 ? 45  LEU B CD1 1 
ATOM   4466 C CD2 . LEU B 1 45  ? -19.587 29.574 40.487  1.00 15.52 ? 45  LEU B CD2 1 
ATOM   4467 N N   . LYS B 1 46  ? -14.615 28.105 38.343  1.00 17.08 ? 46  LYS B N   1 
ATOM   4468 C CA  . LYS B 1 46  ? -13.310 27.506 38.623  1.00 18.99 ? 46  LYS B CA  1 
ATOM   4469 C C   . LYS B 1 46  ? -12.428 28.462 39.404  1.00 21.47 ? 46  LYS B C   1 
ATOM   4470 O O   . LYS B 1 46  ? -11.525 28.030 40.129  1.00 21.99 ? 46  LYS B O   1 
ATOM   4471 C CB  . LYS B 1 46  ? -12.605 27.122 37.319  1.00 23.39 ? 46  LYS B CB  1 
ATOM   4472 C CG  . LYS B 1 46  ? -13.116 25.854 36.647  1.00 31.37 ? 46  LYS B CG  1 
ATOM   4473 C CD  . LYS B 1 46  ? -12.314 25.587 35.390  1.00 39.98 ? 46  LYS B CD  1 
ATOM   4474 C CE  . LYS B 1 46  ? -12.640 24.238 34.792  1.00 49.73 ? 46  LYS B CE  1 
ATOM   4475 N NZ  . LYS B 1 46  ? -11.811 23.991 33.583  1.00 50.45 ? 46  LYS B NZ  1 
ATOM   4476 N N   . ASP B 1 47  ? -12.662 29.766 39.254  1.00 17.49 ? 47  ASP B N   1 
ATOM   4477 C CA  . ASP B 1 47  ? -11.783 30.765 39.834  1.00 20.21 ? 47  ASP B CA  1 
ATOM   4478 C C   . ASP B 1 47  ? -12.401 31.513 40.998  1.00 23.32 ? 47  ASP B C   1 
ATOM   4479 O O   . ASP B 1 47  ? -11.665 32.118 41.786  1.00 22.02 ? 47  ASP B O   1 
ATOM   4480 C CB  . ASP B 1 47  ? -11.361 31.764 38.748  1.00 25.10 ? 47  ASP B CB  1 
ATOM   4481 C CG  . ASP B 1 47  ? -10.548 31.105 37.653  1.00 33.36 ? 47  ASP B CG  1 
ATOM   4482 O OD1 . ASP B 1 47  ? -9.811  30.136 37.964  1.00 29.89 ? 47  ASP B OD1 1 
ATOM   4483 O OD2 . ASP B 1 47  ? -10.660 31.537 36.486  1.00 35.17 ? 47  ASP B OD2 1 
ATOM   4484 N N   . PHE B 1 48  ? -13.723 31.479 41.136  1.00 19.00 ? 48  PHE B N   1 
ATOM   4485 C CA  . PHE B 1 48  ? -14.401 32.221 42.186  1.00 22.56 ? 48  PHE B CA  1 
ATOM   4486 C C   . PHE B 1 48  ? -15.275 31.260 42.974  1.00 24.64 ? 48  PHE B C   1 
ATOM   4487 O O   . PHE B 1 48  ? -16.094 30.539 42.398  1.00 24.83 ? 48  PHE B O   1 
ATOM   4488 C CB  . PHE B 1 48  ? -15.205 33.379 41.588  1.00 21.79 ? 48  PHE B CB  1 
ATOM   4489 C CG  . PHE B 1 48  ? -14.349 34.373 40.855  1.00 20.12 ? 48  PHE B CG  1 
ATOM   4490 C CD1 . PHE B 1 48  ? -13.677 35.367 41.545  1.00 24.42 ? 48  PHE B CD1 1 
ATOM   4491 C CD2 . PHE B 1 48  ? -14.178 34.285 39.482  1.00 17.71 ? 48  PHE B CD2 1 
ATOM   4492 C CE1 . PHE B 1 48  ? -12.868 36.275 40.874  1.00 27.41 ? 48  PHE B CE1 1 
ATOM   4493 C CE2 . PHE B 1 48  ? -13.377 35.186 38.804  1.00 20.50 ? 48  PHE B CE2 1 
ATOM   4494 C CZ  . PHE B 1 48  ? -12.714 36.179 39.502  1.00 22.55 ? 48  PHE B CZ  1 
ATOM   4495 N N   . GLU B 1 49  ? -15.074 31.233 44.288  1.00 19.70 ? 49  GLU B N   1 
ATOM   4496 C CA  . GLU B 1 49  ? -15.738 30.262 45.159  1.00 26.05 ? 49  GLU B CA  1 
ATOM   4497 C C   . GLU B 1 49  ? -17.045 30.862 45.678  1.00 24.74 ? 49  GLU B C   1 
ATOM   4498 O O   . GLU B 1 49  ? -17.205 31.191 46.853  1.00 27.10 ? 49  GLU B O   1 
ATOM   4499 C CB  . GLU B 1 49  ? -14.814 29.860 46.299  1.00 33.84 ? 49  GLU B CB  1 
ATOM   4500 C CG  . GLU B 1 49  ? -13.546 29.161 45.850  1.00 48.21 ? 49  GLU B CG  1 
ATOM   4501 C CD  . GLU B 1 49  ? -13.819 27.738 45.423  1.00 55.45 ? 49  GLU B CD  1 
ATOM   4502 O OE1 . GLU B 1 49  ? -14.621 27.067 46.110  1.00 52.00 ? 49  GLU B OE1 1 
ATOM   4503 O OE2 . GLU B 1 49  ? -13.248 27.300 44.400  1.00 61.90 ? 49  GLU B OE2 1 
ATOM   4504 N N   . ILE B 1 50  ? -17.969 31.049 44.747  1.00 19.16 ? 50  ILE B N   1 
ATOM   4505 C CA  . ILE B 1 50  ? -19.328 31.470 45.024  1.00 19.69 ? 50  ILE B CA  1 
ATOM   4506 C C   . ILE B 1 50  ? -20.258 30.482 44.323  1.00 25.60 ? 50  ILE B C   1 
ATOM   4507 O O   . ILE B 1 50  ? -19.797 29.544 43.675  1.00 19.99 ? 50  ILE B O   1 
ATOM   4508 C CB  . ILE B 1 50  ? -19.596 32.910 44.552  1.00 19.42 ? 50  ILE B CB  1 
ATOM   4509 C CG1 . ILE B 1 50  ? -19.395 32.990 43.030  1.00 24.95 ? 50  ILE B CG1 1 
ATOM   4510 C CG2 . ILE B 1 50  ? -18.697 33.900 45.294  1.00 22.32 ? 50  ILE B CG2 1 
ATOM   4511 C CD1 . ILE B 1 50  ? -19.920 34.241 42.424  1.00 24.09 ? 50  ILE B CD1 1 
ATOM   4512 N N   . LYS B 1 51  ? -21.567 30.699 44.456  1.00 15.10 ? 51  LYS B N   1 
ATOM   4513 C CA  . LYS B 1 51  ? -22.584 29.894 43.777  1.00 16.95 ? 51  LYS B CA  1 
ATOM   4514 C C   . LYS B 1 51  ? -23.234 30.702 42.662  1.00 15.89 ? 51  LYS B C   1 
ATOM   4515 O O   . LYS B 1 51  ? -23.643 31.845 42.880  1.00 14.86 ? 51  LYS B O   1 
ATOM   4516 C CB  . LYS B 1 51  ? -23.700 29.433 44.725  1.00 16.86 ? 51  LYS B CB  1 
ATOM   4517 C CG  . LYS B 1 51  ? -23.270 28.764 46.036  1.00 20.27 ? 51  LYS B CG  1 
ATOM   4518 C CD  . LYS B 1 51  ? -22.553 27.467 45.818  1.00 19.99 ? 51  LYS B CD  1 
ATOM   4519 C CE  . LYS B 1 51  ? -22.179 26.839 47.164  1.00 25.06 ? 51  LYS B CE  1 
ATOM   4520 N NZ  . LYS B 1 51  ? -21.376 25.612 46.957  1.00 30.84 ? 51  LYS B NZ  1 
ATOM   4521 N N   . LEU B 1 52  ? -23.372 30.088 41.490  1.00 10.83 ? 52  LEU B N   1 
ATOM   4522 C CA  . LEU B 1 52  ? -24.053 30.690 40.348  1.00 9.91  ? 52  LEU B CA  1 
ATOM   4523 C C   . LEU B 1 52  ? -24.891 29.621 39.675  1.00 15.66 ? 52  LEU B C   1 
ATOM   4524 O O   . LEU B 1 52  ? -24.424 28.496 39.510  1.00 13.42 ? 52  LEU B O   1 
ATOM   4525 C CB  . LEU B 1 52  ? -23.051 31.237 39.313  1.00 11.07 ? 52  LEU B CB  1 
ATOM   4526 C CG  . LEU B 1 52  ? -22.045 32.302 39.741  1.00 15.13 ? 52  LEU B CG  1 
ATOM   4527 C CD1 . LEU B 1 52  ? -21.030 32.490 38.617  1.00 16.37 ? 52  LEU B CD1 1 
ATOM   4528 C CD2 . LEU B 1 52  ? -22.780 33.607 40.068  1.00 16.19 ? 52  LEU B CD2 1 
ATOM   4529 N N   . ASN B 1 53  ? -26.100 29.970 39.248  1.00 11.25 ? 53  ASN B N   1 
ATOM   4530 C CA  . ASN B 1 53  ? -26.996 28.989 38.645  1.00 12.64 ? 53  ASN B CA  1 
ATOM   4531 C C   . ASN B 1 53  ? -27.227 29.318 37.177  1.00 13.33 ? 53  ASN B C   1 
ATOM   4532 O O   . ASN B 1 53  ? -27.046 30.460 36.734  1.00 10.74 ? 53  ASN B O   1 
ATOM   4533 C CB  . ASN B 1 53  ? -28.324 28.948 39.405  1.00 9.64  ? 53  ASN B CB  1 
ATOM   4534 C CG  . ASN B 1 53  ? -28.116 28.754 40.892  1.00 14.68 ? 53  ASN B CG  1 
ATOM   4535 O OD1 . ASN B 1 53  ? -27.790 27.662 41.334  1.00 14.47 ? 53  ASN B OD1 1 
ATOM   4536 N ND2 . ASN B 1 53  ? -28.188 29.838 41.650  1.00 13.68 ? 53  ASN B ND2 1 
ATOM   4537 N N   . PHE B 1 54  ? -27.626 28.294 36.419  1.00 11.62 ? 54  PHE B N   1 
ATOM   4538 C CA  . PHE B 1 54  ? -27.743 28.411 34.972  1.00 13.97 ? 54  PHE B CA  1 
ATOM   4539 C C   . PHE B 1 54  ? -28.991 27.690 34.485  1.00 12.36 ? 54  PHE B C   1 
ATOM   4540 O O   . PHE B 1 54  ? -29.357 26.635 35.006  1.00 16.21 ? 54  PHE B O   1 
ATOM   4541 C CB  . PHE B 1 54  ? -26.505 27.829 34.270  1.00 12.03 ? 54  PHE B CB  1 
ATOM   4542 C CG  . PHE B 1 54  ? -25.243 28.516 34.667  1.00 12.48 ? 54  PHE B CG  1 
ATOM   4543 C CD1 . PHE B 1 54  ? -24.803 29.636 33.975  1.00 10.38 ? 54  PHE B CD1 1 
ATOM   4544 C CD2 . PHE B 1 54  ? -24.524 28.081 35.779  1.00 12.74 ? 54  PHE B CD2 1 
ATOM   4545 C CE1 . PHE B 1 54  ? -23.655 30.306 34.368  1.00 13.45 ? 54  PHE B CE1 1 
ATOM   4546 C CE2 . PHE B 1 54  ? -23.365 28.758 36.176  1.00 15.64 ? 54  PHE B CE2 1 
ATOM   4547 C CZ  . PHE B 1 54  ? -22.943 29.877 35.457  1.00 14.78 ? 54  PHE B CZ  1 
ATOM   4548 N N   . ASN B 1 55  ? -29.632 28.271 33.482  1.00 9.76  ? 55  ASN B N   1 
ATOM   4549 C CA  . ASN B 1 55  ? -30.709 27.628 32.736  1.00 10.31 ? 55  ASN B CA  1 
ATOM   4550 C C   . ASN B 1 55  ? -30.218 27.355 31.320  1.00 13.06 ? 55  ASN B C   1 
ATOM   4551 O O   . ASN B 1 55  ? -29.639 28.246 30.693  1.00 11.99 ? 55  ASN B O   1 
ATOM   4552 C CB  . ASN B 1 55  ? -31.953 28.524 32.654  1.00 9.99  ? 55  ASN B CB  1 
ATOM   4553 C CG  . ASN B 1 55  ? -33.156 27.795 32.088  1.00 16.07 ? 55  ASN B CG  1 
ATOM   4554 O OD1 . ASN B 1 55  ? -33.564 26.756 32.617  1.00 13.78 ? 55  ASN B OD1 1 
ATOM   4555 N ND2 . ASN B 1 55  ? -33.683 28.291 30.967  1.00 9.98  ? 55  ASN B ND2 1 
ATOM   4556 N N   . LEU B 1 56  ? -30.431 26.128 30.829  1.00 11.48 ? 56  LEU B N   1 
ATOM   4557 C CA  . LEU B 1 56  ? -30.141 25.762 29.444  1.00 12.76 ? 56  LEU B CA  1 
ATOM   4558 C C   . LEU B 1 56  ? -31.417 25.228 28.821  1.00 15.17 ? 56  LEU B C   1 
ATOM   4559 O O   . LEU B 1 56  ? -31.969 24.228 29.295  1.00 17.04 ? 56  LEU B O   1 
ATOM   4560 C CB  . LEU B 1 56  ? -29.058 24.681 29.331  1.00 15.24 ? 56  LEU B CB  1 
ATOM   4561 C CG  . LEU B 1 56  ? -27.665 24.938 29.895  1.00 21.18 ? 56  LEU B CG  1 
ATOM   4562 C CD1 . LEU B 1 56  ? -26.808 23.700 29.657  1.00 29.24 ? 56  LEU B CD1 1 
ATOM   4563 C CD2 . LEU B 1 56  ? -27.050 26.161 29.238  1.00 23.12 ? 56  LEU B CD2 1 
ATOM   4564 N N   . THR B 1 57  ? -31.876 25.859 27.748  1.00 11.78 ? 57  THR B N   1 
ATOM   4565 C CA  . THR B 1 57  ? -33.039 25.298 27.085  1.00 9.64  ? 57  THR B CA  1 
ATOM   4566 C C   . THR B 1 57  ? -32.631 24.038 26.316  1.00 10.38 ? 57  THR B C   1 
ATOM   4567 O O   . THR B 1 57  ? -31.495 23.925 25.835  1.00 14.84 ? 57  THR B O   1 
ATOM   4568 C CB  . THR B 1 57  ? -33.701 26.316 26.146  1.00 15.41 ? 57  THR B CB  1 
ATOM   4569 O OG1 . THR B 1 57  ? -32.808 26.660 25.087  1.00 12.72 ? 57  THR B OG1 1 
ATOM   4570 C CG2 . THR B 1 57  ? -34.102 27.594 26.908  1.00 12.61 ? 57  THR B CG2 1 
ATOM   4571 N N   . PRO B 1 58  ? -33.534 23.062 26.210  1.00 11.69 ? 58  PRO B N   1 
ATOM   4572 C CA  . PRO B 1 58  ? -33.192 21.842 25.460  1.00 12.96 ? 58  PRO B CA  1 
ATOM   4573 C C   . PRO B 1 58  ? -32.829 22.119 24.011  1.00 15.89 ? 58  PRO B C   1 
ATOM   4574 O O   . PRO B 1 58  ? -31.886 21.503 23.485  1.00 13.58 ? 58  PRO B O   1 
ATOM   4575 C CB  . PRO B 1 58  ? -34.462 20.989 25.603  1.00 16.36 ? 58  PRO B CB  1 
ATOM   4576 C CG  . PRO B 1 58  ? -35.083 21.464 26.911  1.00 12.78 ? 58  PRO B CG  1 
ATOM   4577 C CD  . PRO B 1 58  ? -34.841 22.956 26.887  1.00 13.43 ? 58  PRO B CD  1 
ATOM   4578 N N   . VAL B 1 59  ? -33.515 23.063 23.359  1.00 13.88 ? 59  VAL B N   1 
ATOM   4579 C CA  . VAL B 1 59  ? -33.199 23.348 21.960  1.00 15.42 ? 59  VAL B CA  1 
ATOM   4580 C C   . VAL B 1 59  ? -31.804 23.936 21.833  1.00 14.51 ? 59  VAL B C   1 
ATOM   4581 O O   . VAL B 1 59  ? -31.091 23.655 20.857  1.00 14.40 ? 59  VAL B O   1 
ATOM   4582 C CB  . VAL B 1 59  ? -34.271 24.250 21.308  1.00 14.44 ? 59  VAL B CB  1 
ATOM   4583 C CG1 . VAL B 1 59  ? -34.448 25.579 22.048  1.00 16.74 ? 59  VAL B CG1 1 
ATOM   4584 C CG2 . VAL B 1 59  ? -33.950 24.488 19.836  1.00 12.86 ? 59  VAL B CG2 1 
ATOM   4585 N N   . LEU B 1 60  ? -31.366 24.729 22.816  1.00 12.25 ? 60  LEU B N   1 
ATOM   4586 C CA  . LEU B 1 60  ? -29.973 25.154 22.824  1.00 10.11 ? 60  LEU B CA  1 
ATOM   4587 C C   . LEU B 1 60  ? -29.039 23.960 23.002  1.00 12.31 ? 60  LEU B C   1 
ATOM   4588 O O   . LEU B 1 60  ? -28.015 23.850 22.312  1.00 14.08 ? 60  LEU B O   1 
ATOM   4589 C CB  . LEU B 1 60  ? -29.731 26.188 23.925  1.00 10.80 ? 60  LEU B CB  1 
ATOM   4590 C CG  . LEU B 1 60  ? -28.257 26.554 24.068  1.00 10.90 ? 60  LEU B CG  1 
ATOM   4591 C CD1 . LEU B 1 60  ? -27.655 27.115 22.747  1.00 12.65 ? 60  LEU B CD1 1 
ATOM   4592 C CD2 . LEU B 1 60  ? -28.064 27.530 25.258  1.00 11.88 ? 60  LEU B CD2 1 
ATOM   4593 N N   . ILE B 1 61  ? -29.370 23.051 23.923  1.00 11.80 ? 61  ILE B N   1 
ATOM   4594 C CA  . ILE B 1 61  ? -28.484 21.911 24.152  1.00 18.14 ? 61  ILE B CA  1 
ATOM   4595 C C   . ILE B 1 61  ? -28.334 21.093 22.874  1.00 23.19 ? 61  ILE B C   1 
ATOM   4596 O O   . ILE B 1 61  ? -27.227 20.648 22.529  1.00 15.34 ? 61  ILE B O   1 
ATOM   4597 C CB  . ILE B 1 61  ? -28.992 21.041 25.313  1.00 13.98 ? 61  ILE B CB  1 
ATOM   4598 C CG1 . ILE B 1 61  ? -28.893 21.801 26.637  1.00 11.12 ? 61  ILE B CG1 1 
ATOM   4599 C CG2 . ILE B 1 61  ? -28.153 19.773 25.405  1.00 13.67 ? 61  ILE B CG2 1 
ATOM   4600 C CD1 . ILE B 1 61  ? -29.618 21.135 27.790  1.00 16.37 ? 61  ILE B CD1 1 
ATOM   4601 N N   . ASP B 1 62  ? -29.437 20.900 22.140  1.00 13.58 ? 62  ASP B N   1 
ATOM   4602 C CA  . ASP B 1 62  ? -29.372 20.112 20.906  1.00 18.71 ? 62  ASP B CA  1 
ATOM   4603 C C   . ASP B 1 62  ? -28.363 20.700 19.922  1.00 21.80 ? 62  ASP B C   1 
ATOM   4604 O O   . ASP B 1 62  ? -27.608 19.957 19.271  1.00 17.71 ? 62  ASP B O   1 
ATOM   4605 C CB  . ASP B 1 62  ? -30.746 20.033 20.239  1.00 19.05 ? 62  ASP B CB  1 
ATOM   4606 C CG  . ASP B 1 62  ? -31.678 19.051 20.912  1.00 24.43 ? 62  ASP B CG  1 
ATOM   4607 O OD1 . ASP B 1 62  ? -31.187 18.122 21.596  1.00 24.56 ? 62  ASP B OD1 1 
ATOM   4608 O OD2 . ASP B 1 62  ? -32.907 19.196 20.723  1.00 24.31 ? 62  ASP B OD2 1 
ATOM   4609 N N   . GLN B 1 63  ? -28.360 22.028 19.775  1.00 17.70 ? 63  GLN B N   1 
ATOM   4610 C CA  . GLN B 1 63  ? -27.476 22.659 18.797  1.00 20.97 ? 63  GLN B CA  1 
ATOM   4611 C C   . GLN B 1 63  ? -26.027 22.643 19.267  1.00 15.48 ? 63  GLN B C   1 
ATOM   4612 O O   . GLN B 1 63  ? -25.120 22.415 18.463  1.00 19.42 ? 63  GLN B O   1 
ATOM   4613 C CB  . GLN B 1 63  ? -27.914 24.098 18.498  1.00 14.54 ? 63  GLN B CB  1 
ATOM   4614 C CG  . GLN B 1 63  ? -29.394 24.268 18.256  1.00 18.10 ? 63  GLN B CG  1 
ATOM   4615 C CD  . GLN B 1 63  ? -29.793 25.718 18.062  1.00 24.58 ? 63  GLN B CD  1 
ATOM   4616 O OE1 . GLN B 1 63  ? -29.227 26.448 17.247  1.00 25.13 ? 63  GLN B OE1 1 
ATOM   4617 N NE2 . GLN B 1 63  ? -30.703 26.174 18.908  1.00 15.93 ? 63  GLN B NE2 1 
ATOM   4618 N N   . ILE B 1 64  ? -25.782 22.893 20.559  1.00 16.10 ? 64  ILE B N   1 
ATOM   4619 C CA  . ILE B 1 64  ? -24.420 22.779 21.065  1.00 13.56 ? 64  ILE B CA  1 
ATOM   4620 C C   . ILE B 1 64  ? -23.872 21.386 20.780  1.00 16.13 ? 64  ILE B C   1 
ATOM   4621 O O   . ILE B 1 64  ? -22.720 21.231 20.358  1.00 20.05 ? 64  ILE B O   1 
ATOM   4622 C CB  . ILE B 1 64  ? -24.372 23.106 22.566  1.00 21.43 ? 64  ILE B CB  1 
ATOM   4623 C CG1 . ILE B 1 64  ? -24.653 24.600 22.780  1.00 15.88 ? 64  ILE B CG1 1 
ATOM   4624 C CG2 . ILE B 1 64  ? -23.015 22.677 23.174  1.00 14.78 ? 64  ILE B CG2 1 
ATOM   4625 C CD1 . ILE B 1 64  ? -24.816 25.004 24.252  1.00 13.44 ? 64  ILE B CD1 1 
ATOM   4626 N N   . GLN B 1 65  ? -24.698 20.357 20.991  1.00 16.67 ? 65  GLN B N   1 
ATOM   4627 C CA  . GLN B 1 65  ? -24.278 18.985 20.711  1.00 21.00 ? 65  GLN B CA  1 
ATOM   4628 C C   . GLN B 1 65  ? -23.918 18.805 19.246  1.00 23.55 ? 65  GLN B C   1 
ATOM   4629 O O   . GLN B 1 65  ? -22.913 18.159 18.920  1.00 20.72 ? 65  GLN B O   1 
ATOM   4630 C CB  . GLN B 1 65  ? -25.385 18.010 21.109  1.00 22.77 ? 65  GLN B CB  1 
ATOM   4631 C CG  . GLN B 1 65  ? -25.334 17.619 22.574  1.00 31.92 ? 65  GLN B CG  1 
ATOM   4632 C CD  . GLN B 1 65  ? -26.552 16.827 23.029  1.00 41.43 ? 65  GLN B CD  1 
ATOM   4633 O OE1 . GLN B 1 65  ? -27.635 16.925 22.449  1.00 40.22 ? 65  GLN B OE1 1 
ATOM   4634 N NE2 . GLN B 1 65  ? -26.366 16.013 24.061  1.00 48.04 ? 65  GLN B NE2 1 
ATOM   4635 N N   . GLU B 1 66  ? -24.726 19.368 18.345  1.00 20.18 ? 66  GLU B N   1 
ATOM   4636 C CA  . GLU B 1 66  ? -24.456 19.216 16.917  1.00 22.00 ? 66  GLU B CA  1 
ATOM   4637 C C   . GLU B 1 66  ? -23.141 19.885 16.527  1.00 20.89 ? 66  GLU B C   1 
ATOM   4638 O O   . GLU B 1 66  ? -22.334 19.299 15.793  1.00 22.77 ? 66  GLU B O   1 
ATOM   4639 C CB  . GLU B 1 66  ? -25.623 19.784 16.103  1.00 24.58 ? 66  GLU B CB  1 
ATOM   4640 C CG  . GLU B 1 66  ? -25.501 19.541 14.611  1.00 32.81 ? 66  GLU B CG  1 
ATOM   4641 C CD  . GLU B 1 66  ? -26.794 19.822 13.853  1.00 39.98 ? 66  GLU B CD  1 
ATOM   4642 O OE1 . GLU B 1 66  ? -27.795 20.224 14.492  1.00 28.56 ? 66  GLU B OE1 1 
ATOM   4643 O OE2 . GLU B 1 66  ? -26.811 19.625 12.614  1.00 47.26 ? 66  GLU B OE2 1 
ATOM   4644 N N   . TYR B 1 67  ? -22.900 21.113 17.006  1.00 18.53 ? 67  TYR B N   1 
ATOM   4645 C CA  . TYR B 1 67  ? -21.619 21.761 16.721  1.00 18.45 ? 67  TYR B CA  1 
ATOM   4646 C C   . TYR B 1 67  ? -20.463 20.961 17.308  1.00 20.25 ? 67  TYR B C   1 
ATOM   4647 O O   . TYR B 1 67  ? -19.404 20.830 16.679  1.00 20.84 ? 67  TYR B O   1 
ATOM   4648 C CB  . TYR B 1 67  ? -21.597 23.191 17.279  1.00 19.12 ? 67  TYR B CB  1 
ATOM   4649 C CG  . TYR B 1 67  ? -22.266 24.248 16.406  1.00 18.17 ? 67  TYR B CG  1 
ATOM   4650 C CD1 . TYR B 1 67  ? -21.565 24.900 15.388  1.00 17.42 ? 67  TYR B CD1 1 
ATOM   4651 C CD2 . TYR B 1 67  ? -23.582 24.596 16.611  1.00 19.21 ? 67  TYR B CD2 1 
ATOM   4652 C CE1 . TYR B 1 67  ? -22.174 25.870 14.609  1.00 17.03 ? 67  TYR B CE1 1 
ATOM   4653 C CE2 . TYR B 1 67  ? -24.192 25.563 15.844  1.00 15.07 ? 67  TYR B CE2 1 
ATOM   4654 C CZ  . TYR B 1 67  ? -23.499 26.191 14.847  1.00 22.22 ? 67  TYR B CZ  1 
ATOM   4655 O OH  . TYR B 1 67  ? -24.158 27.150 14.111  1.00 16.89 ? 67  TYR B OH  1 
ATOM   4656 N N   . ALA B 1 68  ? -20.648 20.425 18.518  1.00 20.00 ? 68  ALA B N   1 
ATOM   4657 C CA  . ALA B 1 68  ? -19.572 19.690 19.182  1.00 19.79 ? 68  ALA B CA  1 
ATOM   4658 C C   . ALA B 1 68  ? -19.180 18.442 18.404  1.00 25.62 ? 68  ALA B C   1 
ATOM   4659 O O   . ALA B 1 68  ? -18.020 18.010 18.456  1.00 24.79 ? 68  ALA B O   1 
ATOM   4660 C CB  . ALA B 1 68  ? -19.989 19.307 20.603  1.00 19.09 ? 68  ALA B CB  1 
ATOM   4661 N N   . GLN B 1 69  ? -20.128 17.850 17.691  1.00 27.81 ? 69  GLN B N   1 
ATOM   4662 C CA  . GLN B 1 69  ? -19.878 16.662 16.892  1.00 25.05 ? 69  GLN B CA  1 
ATOM   4663 C C   . GLN B 1 69  ? -19.370 16.978 15.492  1.00 31.97 ? 69  GLN B C   1 
ATOM   4664 O O   . GLN B 1 69  ? -19.108 16.048 14.722  1.00 37.44 ? 69  GLN B O   1 
ATOM   4665 C CB  . GLN B 1 69  ? -21.153 15.822 16.799  1.00 38.30 ? 69  GLN B CB  1 
ATOM   4666 C CG  . GLN B 1 69  ? -21.634 15.307 18.138  1.00 43.01 ? 69  GLN B CG  1 
ATOM   4667 C CD  . GLN B 1 69  ? -22.918 14.518 18.033  1.00 52.53 ? 69  GLN B CD  1 
ATOM   4668 O OE1 . GLN B 1 69  ? -23.451 14.318 16.944  1.00 56.14 ? 69  GLN B OE1 1 
ATOM   4669 N NE2 . GLN B 1 69  ? -23.432 14.073 19.173  1.00 61.31 ? 69  GLN B NE2 1 
ATOM   4670 N N   . GLY B 1 70  ? -19.201 18.253 15.149  1.00 30.11 ? 70  GLY B N   1 
ATOM   4671 C CA  . GLY B 1 70  ? -18.792 18.595 13.801  1.00 30.93 ? 70  GLY B CA  1 
ATOM   4672 C C   . GLY B 1 70  ? -19.873 18.418 12.763  1.00 36.74 ? 70  GLY B C   1 
ATOM   4673 O O   . GLY B 1 70  ? -19.582 18.480 11.565  1.00 38.00 ? 70  GLY B O   1 
ATOM   4674 N N   . LYS B 1 71  ? -21.119 18.205 13.190  1.00 35.36 ? 71  LYS B N   1 
ATOM   4675 C CA  . LYS B 1 71  ? -22.233 17.976 12.278  1.00 38.30 ? 71  LYS B CA  1 
ATOM   4676 C C   . LYS B 1 71  ? -22.899 19.258 11.801  1.00 39.47 ? 71  LYS B C   1 
ATOM   4677 O O   . LYS B 1 71  ? -23.610 19.230 10.792  1.00 40.22 ? 71  LYS B O   1 
ATOM   4678 C CB  . LYS B 1 71  ? -23.291 17.093 12.949  1.00 42.57 ? 71  LYS B CB  1 
ATOM   4679 C CG  . LYS B 1 71  ? -22.940 15.619 12.992  1.00 51.72 ? 71  LYS B CG  1 
ATOM   4680 C CD  . LYS B 1 71  ? -23.923 14.843 13.857  1.00 57.05 ? 71  LYS B CD  1 
ATOM   4681 C CE  . LYS B 1 71  ? -25.308 14.764 13.228  1.00 60.63 ? 71  LYS B CE  1 
ATOM   4682 N NZ  . LYS B 1 71  ? -25.357 13.841 12.062  1.00 66.56 ? 71  LYS B NZ  1 
ATOM   4683 N N   . ALA B 1 72  ? -22.684 20.375 12.486  1.00 33.75 ? 72  ALA B N   1 
ATOM   4684 C CA  . ALA B 1 72  ? -23.435 21.586 12.187  1.00 27.96 ? 72  ALA B CA  1 
ATOM   4685 C C   . ALA B 1 72  ? -22.928 22.236 10.903  1.00 30.07 ? 72  ALA B C   1 
ATOM   4686 O O   . ALA B 1 72  ? -21.738 22.532 10.770  1.00 30.62 ? 72  ALA B O   1 
ATOM   4687 C CB  . ALA B 1 72  ? -23.341 22.558 13.362  1.00 26.13 ? 72  ALA B CB  1 
ATOM   4688 N N   . LYS B 1 73  ? -23.838 22.434 9.948   1.00 26.17 ? 73  LYS B N   1 
ATOM   4689 C CA  . LYS B 1 73  ? -23.551 23.088 8.666   1.00 25.35 ? 73  LYS B CA  1 
ATOM   4690 C C   . LYS B 1 73  ? -24.003 24.545 8.780   1.00 22.14 ? 73  LYS B C   1 
ATOM   4691 O O   . LYS B 1 73  ? -25.159 24.879 8.531   1.00 30.67 ? 73  LYS B O   1 
ATOM   4692 C CB  . LYS B 1 73  ? -24.264 22.366 7.522   1.00 29.06 ? 73  LYS B CB  1 
ATOM   4693 C CG  . LYS B 1 73  ? -23.909 20.894 7.376   1.00 38.86 ? 73  LYS B CG  1 
ATOM   4694 C CD  . LYS B 1 73  ? -24.650 20.240 6.204   1.00 42.72 ? 73  LYS B CD  1 
ATOM   4695 C CE  . LYS B 1 73  ? -26.125 20.020 6.533   1.00 46.56 ? 73  LYS B CE  1 
ATOM   4696 N NZ  . LYS B 1 73  ? -26.828 19.282 5.445   1.00 55.27 ? 73  LYS B NZ  1 
ATOM   4697 N N   . ASP B 1 74  ? -23.075 25.420 9.152   1.00 22.32 ? 74  ASP B N   1 
ATOM   4698 C CA  . ASP B 1 74  ? -23.365 26.806 9.509   1.00 19.81 ? 74  ASP B CA  1 
ATOM   4699 C C   . ASP B 1 74  ? -22.904 27.693 8.354   1.00 21.84 ? 74  ASP B C   1 
ATOM   4700 O O   . ASP B 1 74  ? -21.705 27.756 8.056   1.00 22.97 ? 74  ASP B O   1 
ATOM   4701 C CB  . ASP B 1 74  ? -22.672 27.121 10.842  1.00 18.07 ? 74  ASP B CB  1 
ATOM   4702 C CG  . ASP B 1 74  ? -22.853 28.559 11.320  1.00 26.67 ? 74  ASP B CG  1 
ATOM   4703 O OD1 . ASP B 1 74  ? -22.975 29.501 10.506  1.00 23.80 ? 74  ASP B OD1 1 
ATOM   4704 O OD2 . ASP B 1 74  ? -22.869 28.735 12.564  1.00 28.46 ? 74  ASP B OD2 1 
ATOM   4705 N N   . VAL B 1 75  ? -23.858 28.369 7.700   1.00 21.70 ? 75  VAL B N   1 
ATOM   4706 C CA  . VAL B 1 75  ? -23.565 29.047 6.435   1.00 21.20 ? 75  VAL B CA  1 
ATOM   4707 C C   . VAL B 1 75  ? -22.632 30.238 6.652   1.00 26.14 ? 75  VAL B C   1 
ATOM   4708 O O   . VAL B 1 75  ? -21.678 30.440 5.883   1.00 24.60 ? 75  VAL B O   1 
ATOM   4709 C CB  . VAL B 1 75  ? -24.872 29.445 5.707   1.00 27.85 ? 75  VAL B CB  1 
ATOM   4710 C CG1 . VAL B 1 75  ? -25.701 28.199 5.391   1.00 31.07 ? 75  VAL B CG1 1 
ATOM   4711 C CG2 . VAL B 1 75  ? -25.703 30.444 6.501   1.00 32.03 ? 75  VAL B CG2 1 
ATOM   4712 N N   A PHE B 1 76  ? -22.884 31.044 7.693   0.53 23.58 ? 76  PHE B N   1 
ATOM   4713 N N   B PHE B 1 76  ? -22.872 31.023 7.701   0.47 23.75 ? 76  PHE B N   1 
ATOM   4714 C CA  A PHE B 1 76  ? -22.009 32.175 7.991   0.53 24.95 ? 76  PHE B CA  1 
ATOM   4715 C CA  B PHE B 1 76  ? -22.002 32.159 7.966   0.47 24.93 ? 76  PHE B CA  1 
ATOM   4716 C C   A PHE B 1 76  ? -20.611 31.700 8.369   0.53 26.26 ? 76  PHE B C   1 
ATOM   4717 C C   B PHE B 1 76  ? -20.609 31.704 8.378   0.47 26.21 ? 76  PHE B C   1 
ATOM   4718 O O   A PHE B 1 76  ? -19.608 32.308 7.970   0.53 26.12 ? 76  PHE B O   1 
ATOM   4719 O O   B PHE B 1 76  ? -19.608 32.334 8.013   0.47 26.04 ? 76  PHE B O   1 
ATOM   4720 C CB  A PHE B 1 76  ? -22.590 33.025 9.125   0.53 23.75 ? 76  PHE B CB  1 
ATOM   4721 C CB  B PHE B 1 76  ? -22.602 33.054 9.043   0.47 23.91 ? 76  PHE B CB  1 
ATOM   4722 C CG  A PHE B 1 76  ? -23.636 34.013 8.685   0.53 25.12 ? 76  PHE B CG  1 
ATOM   4723 C CG  B PHE B 1 76  ? -21.852 34.318 9.216   0.47 23.29 ? 76  PHE B CG  1 
ATOM   4724 C CD1 A PHE B 1 76  ? -24.903 33.585 8.305   0.53 22.82 ? 76  PHE B CD1 1 
ATOM   4725 C CD1 B PHE B 1 76  ? -22.091 35.384 8.373   0.47 22.13 ? 76  PHE B CD1 1 
ATOM   4726 C CD2 A PHE B 1 76  ? -23.353 35.373 8.650   0.53 22.66 ? 76  PHE B CD2 1 
ATOM   4727 C CD2 B PHE B 1 76  ? -20.865 34.430 10.179  0.47 21.10 ? 76  PHE B CD2 1 
ATOM   4728 C CE1 A PHE B 1 76  ? -25.867 34.496 7.897   0.53 25.43 ? 76  PHE B CE1 1 
ATOM   4729 C CE1 B PHE B 1 76  ? -21.383 36.544 8.502   0.47 22.48 ? 76  PHE B CE1 1 
ATOM   4730 C CE2 A PHE B 1 76  ? -24.314 36.287 8.244   0.53 24.45 ? 76  PHE B CE2 1 
ATOM   4731 C CE2 B PHE B 1 76  ? -20.154 35.596 10.315  0.47 22.88 ? 76  PHE B CE2 1 
ATOM   4732 C CZ  A PHE B 1 76  ? -25.571 35.847 7.870   0.53 24.95 ? 76  PHE B CZ  1 
ATOM   4733 C CZ  B PHE B 1 76  ? -20.409 36.651 9.470   0.47 19.60 ? 76  PHE B CZ  1 
ATOM   4734 N N   . LEU B 1 77  ? -20.524 30.616 9.144   1.00 23.10 ? 77  LEU B N   1 
ATOM   4735 C CA  . LEU B 1 77  ? -19.223 30.116 9.557   1.00 19.60 ? 77  LEU B CA  1 
ATOM   4736 C C   . LEU B 1 77  ? -18.440 29.594 8.365   1.00 24.41 ? 77  LEU B C   1 
ATOM   4737 O O   . LEU B 1 77  ? -17.209 29.690 8.345   1.00 25.69 ? 77  LEU B O   1 
ATOM   4738 C CB  . LEU B 1 77  ? -19.394 29.044 10.631  1.00 25.84 ? 77  LEU B CB  1 
ATOM   4739 C CG  . LEU B 1 77  ? -18.181 28.688 11.476  1.00 31.44 ? 77  LEU B CG  1 
ATOM   4740 C CD1 . LEU B 1 77  ? -17.616 29.941 12.124  1.00 30.06 ? 77  LEU B CD1 1 
ATOM   4741 C CD2 . LEU B 1 77  ? -18.613 27.693 12.533  1.00 35.20 ? 77  LEU B CD2 1 
ATOM   4742 N N   . GLU B 1 78  ? -19.132 29.067 7.349   1.00 27.68 ? 78  GLU B N   1 
ATOM   4743 C CA  . GLU B 1 78  ? -18.443 28.701 6.115   1.00 28.37 ? 78  GLU B CA  1 
ATOM   4744 C C   . GLU B 1 78  ? -17.893 29.927 5.399   1.00 28.84 ? 78  GLU B C   1 
ATOM   4745 O O   . GLU B 1 78  ? -16.808 29.867 4.806   1.00 31.99 ? 78  GLU B O   1 
ATOM   4746 C CB  . GLU B 1 78  ? -19.372 27.907 5.198   1.00 36.38 ? 78  GLU B CB  1 
ATOM   4747 C CG  . GLU B 1 78  ? -19.230 26.432 5.428   1.00 53.02 ? 78  GLU B CG  1 
ATOM   4748 C CD  . GLU B 1 78  ? -17.814 25.965 5.128   1.00 67.29 ? 78  GLU B CD  1 
ATOM   4749 O OE1 . GLU B 1 78  ? -17.222 26.439 4.134   1.00 70.57 ? 78  GLU B OE1 1 
ATOM   4750 O OE2 . GLU B 1 78  ? -17.275 25.153 5.909   1.00 72.73 ? 78  GLU B OE2 1 
ATOM   4751 N N   . ALA B 1 79  ? -18.616 31.047 5.445   1.00 26.89 ? 79  ALA B N   1 
ATOM   4752 C CA  . ALA B 1 79  ? -18.080 32.274 4.861   1.00 27.81 ? 79  ALA B CA  1 
ATOM   4753 C C   . ALA B 1 79  ? -16.819 32.737 5.590   1.00 28.57 ? 79  ALA B C   1 
ATOM   4754 O O   . ALA B 1 79  ? -15.958 33.391 4.989   1.00 30.70 ? 79  ALA B O   1 
ATOM   4755 C CB  . ALA B 1 79  ? -19.141 33.375 4.874   1.00 25.39 ? 79  ALA B CB  1 
ATOM   4756 N N   . ILE B 1 80  ? -16.680 32.403 6.876   1.00 21.06 ? 80  ILE B N   1 
ATOM   4757 C CA  . ILE B 1 80  ? -15.445 32.740 7.590   1.00 20.04 ? 80  ILE B CA  1 
ATOM   4758 C C   . ILE B 1 80  ? -14.351 31.709 7.329   1.00 20.83 ? 80  ILE B C   1 
ATOM   4759 O O   . ILE B 1 80  ? -13.177 32.064 7.199   1.00 25.72 ? 80  ILE B O   1 
ATOM   4760 C CB  . ILE B 1 80  ? -15.740 32.887 9.092   1.00 21.46 ? 80  ILE B CB  1 
ATOM   4761 C CG1 . ILE B 1 80  ? -16.505 34.190 9.341   1.00 19.11 ? 80  ILE B CG1 1 
ATOM   4762 C CG2 . ILE B 1 80  ? -14.454 32.819 9.926   1.00 23.06 ? 80  ILE B CG2 1 
ATOM   4763 C CD1 . ILE B 1 80  ? -17.096 34.264 10.725  1.00 29.23 ? 80  ILE B CD1 1 
ATOM   4764 N N   . ARG B 1 81  ? -14.700 30.418 7.259   1.00 24.34 ? 81  ARG B N   1 
ATOM   4765 C CA  . ARG B 1 81  ? -13.663 29.395 7.121   1.00 27.19 ? 81  ARG B CA  1 
ATOM   4766 C C   . ARG B 1 81  ? -12.955 29.479 5.772   1.00 28.60 ? 81  ARG B C   1 
ATOM   4767 O O   . ARG B 1 81  ? -11.740 29.255 5.691   1.00 31.38 ? 81  ARG B O   1 
ATOM   4768 C CB  . ARG B 1 81  ? -14.252 27.996 7.314   1.00 29.56 ? 81  ARG B CB  1 
ATOM   4769 C CG  . ARG B 1 81  ? -13.208 26.874 7.230   1.00 34.66 ? 81  ARG B CG  1 
ATOM   4770 C CD  . ARG B 1 81  ? -13.809 25.495 7.469   1.00 45.84 ? 81  ARG B CD  1 
ATOM   4771 N NE  . ARG B 1 81  ? -14.253 25.309 8.854   1.00 54.75 ? 81  ARG B NE  1 
ATOM   4772 C CZ  . ARG B 1 81  ? -13.462 24.919 9.854   1.00 58.37 ? 81  ARG B CZ  1 
ATOM   4773 N NH1 . ARG B 1 81  ? -12.177 24.671 9.634   1.00 60.77 ? 81  ARG B NH1 1 
ATOM   4774 N NH2 . ARG B 1 81  ? -13.957 24.775 11.077  1.00 58.09 ? 81  ARG B NH2 1 
ATOM   4775 N N   . LYS B 1 82  ? -13.697 29.795 4.709   1.00 26.01 ? 82  LYS B N   1 
ATOM   4776 C CA  . LYS B 1 82  ? -13.171 29.748 3.350   1.00 28.35 ? 82  LYS B CA  1 
ATOM   4777 C C   . LYS B 1 82  ? -11.992 30.690 3.158   1.00 23.97 ? 82  LYS B C   1 
ATOM   4778 O O   . LYS B 1 82  ? -11.959 31.800 3.704   1.00 24.33 ? 82  LYS B O   1 
ATOM   4779 C CB  . LYS B 1 82  ? -14.258 30.140 2.343   1.00 27.95 ? 82  LYS B CB  1 
ATOM   4780 C CG  . LYS B 1 82  ? -15.251 29.070 1.940   1.00 39.78 ? 82  LYS B CG  1 
ATOM   4781 C CD  . LYS B 1 82  ? -16.161 29.653 0.871   1.00 40.67 ? 82  LYS B CD  1 
ATOM   4782 C CE  . LYS B 1 82  ? -17.156 28.659 0.319   1.00 49.66 ? 82  LYS B CE  1 
ATOM   4783 N NZ  . LYS B 1 82  ? -18.061 29.341 -0.647  1.00 52.84 ? 82  LYS B NZ  1 
ATOM   4784 N N   . ASP B 1 83  ? -11.046 30.253 2.332   1.00 26.98 ? 83  ASP B N   1 
ATOM   4785 C CA  . ASP B 1 83  ? -10.075 31.181 1.784   1.00 31.36 ? 83  ASP B CA  1 
ATOM   4786 C C   . ASP B 1 83  ? -10.849 32.248 1.018   1.00 28.10 ? 83  ASP B C   1 
ATOM   4787 O O   . ASP B 1 83  ? -11.802 31.911 0.294   1.00 28.92 ? 83  ASP B O   1 
ATOM   4788 C CB  . ASP B 1 83  ? -9.076  30.441 0.886   1.00 28.72 ? 83  ASP B CB  1 
ATOM   4789 C CG  . ASP B 1 83  ? -7.937  31.330 0.386   1.00 35.32 ? 83  ASP B CG  1 
ATOM   4790 O OD1 . ASP B 1 83  ? -8.171  32.416 -0.180  1.00 32.47 ? 83  ASP B OD1 1 
ATOM   4791 O OD2 . ASP B 1 83  ? -6.772  30.964 0.658   1.00 36.13 ? 83  ASP B OD2 1 
ATOM   4792 N N   . PRO B 1 84  ? -10.549 33.534 1.220   1.00 25.99 ? 84  PRO B N   1 
ATOM   4793 C CA  . PRO B 1 84  ? -11.332 34.579 0.544   1.00 26.12 ? 84  PRO B CA  1 
ATOM   4794 C C   . PRO B 1 84  ? -11.414 34.404 -0.956  1.00 28.99 ? 84  PRO B C   1 
ATOM   4795 O O   . PRO B 1 84  ? -12.406 34.833 -1.552  1.00 28.29 ? 84  PRO B O   1 
ATOM   4796 C CB  . PRO B 1 84  ? -10.589 35.868 0.924   1.00 25.90 ? 84  PRO B CB  1 
ATOM   4797 C CG  . PRO B 1 84  ? -9.997  35.557 2.225   1.00 22.44 ? 84  PRO B CG  1 
ATOM   4798 C CD  . PRO B 1 84  ? -9.596  34.107 2.179   1.00 25.75 ? 84  PRO B CD  1 
ATOM   4799 N N   . ASP B 1 85  ? -10.407 33.786 -1.589  1.00 27.41 ? 85  ASP B N   1 
ATOM   4800 C CA  . ASP B 1 85  ? -10.482 33.552 -3.029  1.00 28.15 ? 85  ASP B CA  1 
ATOM   4801 C C   . ASP B 1 85  ? -11.695 32.715 -3.404  1.00 32.30 ? 85  ASP B C   1 
ATOM   4802 O O   . ASP B 1 85  ? -12.191 32.810 -4.535  1.00 30.24 ? 85  ASP B O   1 
ATOM   4803 C CB  . ASP B 1 85  ? -9.214  32.862 -3.529  1.00 33.94 ? 85  ASP B CB  1 
ATOM   4804 C CG  . ASP B 1 85  ? -8.015  33.781 -3.547  1.00 44.72 ? 85  ASP B CG  1 
ATOM   4805 O OD1 . ASP B 1 85  ? -8.215  35.015 -3.549  1.00 44.24 ? 85  ASP B OD1 1 
ATOM   4806 O OD2 . ASP B 1 85  ? -6.876  33.265 -3.586  1.00 46.95 ? 85  ASP B OD2 1 
ATOM   4807 N N   . ASP B 1 86  ? -12.175 31.888 -2.481  1.00 30.31 ? 86  ASP B N   1 
ATOM   4808 C CA  . ASP B 1 86  ? -13.288 30.987 -2.733  1.00 33.55 ? 86  ASP B CA  1 
ATOM   4809 C C   . ASP B 1 86  ? -14.636 31.579 -2.343  1.00 33.58 ? 86  ASP B C   1 
ATOM   4810 O O   . ASP B 1 86  ? -15.666 30.945 -2.595  1.00 30.65 ? 86  ASP B O   1 
ATOM   4811 C CB  . ASP B 1 86  ? -13.070 29.668 -1.980  1.00 34.87 ? 86  ASP B CB  1 
ATOM   4812 C CG  . ASP B 1 86  ? -11.793 28.964 -2.402  1.00 39.17 ? 86  ASP B CG  1 
ATOM   4813 O OD1 . ASP B 1 86  ? -11.393 29.125 -3.573  1.00 37.14 ? 86  ASP B OD1 1 
ATOM   4814 O OD2 . ASP B 1 86  ? -11.183 28.264 -1.562  1.00 43.61 ? 86  ASP B OD2 1 
ATOM   4815 N N   . LEU B 1 87  ? -14.663 32.766 -1.741  1.00 25.88 ? 87  LEU B N   1 
ATOM   4816 C CA  . LEU B 1 87  ? -15.927 33.336 -1.283  1.00 24.97 ? 87  LEU B CA  1 
ATOM   4817 C C   . LEU B 1 87  ? -16.810 33.737 -2.455  1.00 27.35 ? 87  LEU B C   1 
ATOM   4818 O O   . LEU B 1 87  ? -16.359 34.402 -3.396  1.00 30.35 ? 87  LEU B O   1 
ATOM   4819 C CB  . LEU B 1 87  ? -15.674 34.561 -0.417  1.00 24.18 ? 87  LEU B CB  1 
ATOM   4820 C CG  . LEU B 1 87  ? -15.040 34.335 0.948   1.00 22.54 ? 87  LEU B CG  1 
ATOM   4821 C CD1 . LEU B 1 87  ? -14.650 35.671 1.543   1.00 23.30 ? 87  LEU B CD1 1 
ATOM   4822 C CD2 . LEU B 1 87  ? -16.037 33.615 1.839   1.00 27.09 ? 87  LEU B CD2 1 
ATOM   4823 N N   . GLU B 1 88  ? -18.080 33.371 -2.382  1.00 25.99 ? 88  GLU B N   1 
ATOM   4824 C CA  . GLU B 1 88  ? -18.988 33.957 -3.344  1.00 26.70 ? 88  GLU B CA  1 
ATOM   4825 C C   . GLU B 1 88  ? -19.379 35.365 -2.902  1.00 28.01 ? 88  GLU B C   1 
ATOM   4826 O O   . GLU B 1 88  ? -19.164 35.776 -1.751  1.00 30.63 ? 88  GLU B O   1 
ATOM   4827 C CB  . GLU B 1 88  ? -20.197 33.049 -3.566  1.00 36.33 ? 88  GLU B CB  1 
ATOM   4828 C CG  . GLU B 1 88  ? -21.041 32.742 -2.395  1.00 45.12 ? 88  GLU B CG  1 
ATOM   4829 C CD  . GLU B 1 88  ? -21.761 31.425 -2.587  1.00 50.65 ? 88  GLU B CD  1 
ATOM   4830 O OE1 . GLU B 1 88  ? -21.364 30.655 -3.486  1.00 56.98 ? 88  GLU B OE1 1 
ATOM   4831 O OE2 . GLU B 1 88  ? -22.732 31.165 -1.864  1.00 56.50 ? 88  GLU B OE2 1 
ATOM   4832 N N   . LYS B 1 89  ? -19.870 36.134 -3.872  1.00 28.17 ? 89  LYS B N   1 
ATOM   4833 C CA  . LYS B 1 89  ? -20.261 37.516 -3.621  1.00 28.36 ? 89  LYS B CA  1 
ATOM   4834 C C   . LYS B 1 89  ? -21.279 37.599 -2.492  1.00 28.36 ? 89  LYS B C   1 
ATOM   4835 O O   . LYS B 1 89  ? -21.168 38.457 -1.609  1.00 30.71 ? 89  LYS B O   1 
ATOM   4836 C CB  . LYS B 1 89  ? -20.827 38.126 -4.903  1.00 30.51 ? 89  LYS B CB  1 
ATOM   4837 C CG  . LYS B 1 89  ? -19.768 38.373 -5.961  1.00 35.07 ? 89  LYS B CG  1 
ATOM   4838 C CD  . LYS B 1 89  ? -20.381 38.880 -7.253  1.00 38.24 ? 89  LYS B CD  1 
ATOM   4839 C CE  . LYS B 1 89  ? -19.305 39.351 -8.220  1.00 43.96 ? 89  LYS B CE  1 
ATOM   4840 N NZ  . LYS B 1 89  ? -18.346 38.253 -8.529  1.00 49.76 ? 89  LYS B NZ  1 
ATOM   4841 N N   . GLU B 1 90  ? -22.266 36.703 -2.493  1.00 27.48 ? 90  GLU B N   1 
ATOM   4842 C CA  . GLU B 1 90  ? -23.240 36.664 -1.405  1.00 26.59 ? 90  GLU B CA  1 
ATOM   4843 C C   . GLU B 1 90  ? -22.560 36.458 -0.048  1.00 24.58 ? 90  GLU B C   1 
ATOM   4844 O O   . GLU B 1 90  ? -23.002 37.013 0.968   1.00 27.68 ? 90  GLU B O   1 
ATOM   4845 C CB  . GLU B 1 90  ? -24.256 35.557 -1.680  1.00 31.80 ? 90  GLU B CB  1 
ATOM   4846 C CG  . GLU B 1 90  ? -25.009 35.078 -0.461  1.00 55.51 ? 90  GLU B CG  1 
ATOM   4847 C CD  . GLU B 1 90  ? -26.167 34.169 -0.820  1.00 72.29 ? 90  GLU B CD  1 
ATOM   4848 O OE1 . GLU B 1 90  ? -26.976 33.862 0.082   1.00 77.79 ? 90  GLU B OE1 1 
ATOM   4849 O OE2 . GLU B 1 90  ? -26.250 33.746 -1.997  1.00 73.68 ? 90  GLU B OE2 1 
ATOM   4850 N N   . GLU B 1 91  ? -21.483 35.668 -0.008  1.00 23.92 ? 91  GLU B N   1 
ATOM   4851 C CA  . GLU B 1 91  ? -20.816 35.392 1.259   1.00 22.93 ? 91  GLU B CA  1 
ATOM   4852 C C   . GLU B 1 91  ? -20.017 36.601 1.743   1.00 21.68 ? 91  GLU B C   1 
ATOM   4853 O O   . GLU B 1 91  ? -19.942 36.866 2.951   1.00 22.28 ? 91  GLU B O   1 
ATOM   4854 C CB  . GLU B 1 91  ? -19.911 34.169 1.107   1.00 23.30 ? 91  GLU B CB  1 
ATOM   4855 C CG  . GLU B 1 91  ? -20.654 32.848 1.173   1.00 27.89 ? 91  GLU B CG  1 
ATOM   4856 C CD  . GLU B 1 91  ? -19.791 31.675 0.784   1.00 31.91 ? 91  GLU B CD  1 
ATOM   4857 O OE1 . GLU B 1 91  ? -18.914 31.820 -0.109  1.00 30.11 ? 91  GLU B OE1 1 
ATOM   4858 O OE2 . GLU B 1 91  ? -19.942 30.618 1.435   1.00 30.90 ? 91  GLU B OE2 1 
ATOM   4859 N N   . VAL B 1 92  ? -19.398 37.334 0.816   1.00 25.45 ? 92  VAL B N   1 
ATOM   4860 C CA  . VAL B 1 92  ? -18.733 38.582 1.183   1.00 25.09 ? 92  VAL B CA  1 
ATOM   4861 C C   . VAL B 1 92  ? -19.753 39.586 1.701   1.00 27.66 ? 92  VAL B C   1 
ATOM   4862 O O   . VAL B 1 92  ? -19.513 40.274 2.700   1.00 22.91 ? 92  VAL B O   1 
ATOM   4863 C CB  . VAL B 1 92  ? -17.933 39.137 -0.011  1.00 28.18 ? 92  VAL B CB  1 
ATOM   4864 C CG1 . VAL B 1 92  ? -17.355 40.514 0.317   1.00 27.35 ? 92  VAL B CG1 1 
ATOM   4865 C CG2 . VAL B 1 92  ? -16.818 38.154 -0.414  1.00 25.06 ? 92  VAL B CG2 1 
ATOM   4866 N N   . GLU B 1 93  ? -20.923 39.658 1.052   1.00 29.29 ? 93  GLU B N   1 
ATOM   4867 C CA  . GLU B 1 93  ? -21.998 40.531 1.527   1.00 28.60 ? 93  GLU B CA  1 
ATOM   4868 C C   . GLU B 1 93  ? -22.420 40.185 2.950   1.00 26.82 ? 93  GLU B C   1 
ATOM   4869 O O   . GLU B 1 93  ? -22.596 41.076 3.788   1.00 27.60 ? 93  GLU B O   1 
ATOM   4870 C CB  . GLU B 1 93  ? -23.198 40.445 0.588   1.00 33.78 ? 93  GLU B CB  1 
ATOM   4871 C CG  . GLU B 1 93  ? -22.889 40.970 -0.788  1.00 42.64 ? 93  GLU B CG  1 
ATOM   4872 C CD  . GLU B 1 93  ? -24.001 40.707 -1.783  1.00 50.08 ? 93  GLU B CD  1 
ATOM   4873 O OE1 . GLU B 1 93  ? -24.990 40.025 -1.427  1.00 51.39 ? 93  GLU B OE1 1 
ATOM   4874 O OE2 . GLU B 1 93  ? -23.860 41.174 -2.931  1.00 49.58 ? 93  GLU B OE2 1 
ATOM   4875 N N   . LYS B 1 94  ? -22.617 38.895 3.241   1.00 23.32 ? 94  LYS B N   1 
ATOM   4876 C CA  . LYS B 1 94  ? -23.040 38.532 4.591   1.00 24.92 ? 94  LYS B CA  1 
ATOM   4877 C C   . LYS B 1 94  ? -21.961 38.855 5.620   1.00 23.86 ? 94  LYS B C   1 
ATOM   4878 O O   . LYS B 1 94  ? -22.282 39.261 6.740   1.00 20.84 ? 94  LYS B O   1 
ATOM   4879 C CB  . LYS B 1 94  ? -23.407 37.045 4.674   1.00 32.92 ? 94  LYS B CB  1 
ATOM   4880 C CG  . LYS B 1 94  ? -24.590 36.618 3.817   1.00 38.38 ? 94  LYS B CG  1 
ATOM   4881 C CD  . LYS B 1 94  ? -25.050 35.210 4.186   1.00 41.98 ? 94  LYS B CD  1 
ATOM   4882 C CE  . LYS B 1 94  ? -25.942 34.625 3.092   1.00 47.13 ? 94  LYS B CE  1 
ATOM   4883 N NZ  . LYS B 1 94  ? -27.108 35.493 2.804   1.00 50.84 ? 94  LYS B NZ  1 
ATOM   4884 N N   . LEU B 1 95  ? -20.687 38.698 5.248   1.00 20.62 ? 95  LEU B N   1 
ATOM   4885 C CA  . LEU B 1 95  ? -19.590 39.013 6.159   1.00 23.94 ? 95  LEU B CA  1 
ATOM   4886 C C   . LEU B 1 95  ? -19.568 40.502 6.499   1.00 20.59 ? 95  LEU B C   1 
ATOM   4887 O O   . LEU B 1 95  ? -19.419 40.876 7.669   1.00 21.19 ? 95  LEU B O   1 
ATOM   4888 C CB  . LEU B 1 95  ? -18.270 38.569 5.532   1.00 23.57 ? 95  LEU B CB  1 
ATOM   4889 C CG  . LEU B 1 95  ? -16.963 38.764 6.295   1.00 28.71 ? 95  LEU B CG  1 
ATOM   4890 C CD1 . LEU B 1 95  ? -17.023 38.124 7.669   1.00 33.08 ? 95  LEU B CD1 1 
ATOM   4891 C CD2 . LEU B 1 95  ? -15.801 38.191 5.477   1.00 37.07 ? 95  LEU B CD2 1 
ATOM   4892 N N   . ILE B 1 96  ? -19.743 41.365 5.494   1.00 19.75 ? 96  ILE B N   1 
ATOM   4893 C CA  . ILE B 1 96  ? -19.767 42.804 5.746   1.00 21.93 ? 96  ILE B CA  1 
ATOM   4894 C C   . ILE B 1 96  ? -21.020 43.191 6.526   1.00 23.06 ? 96  ILE B C   1 
ATOM   4895 O O   . ILE B 1 96  ? -20.961 44.003 7.456   1.00 26.71 ? 96  ILE B O   1 
ATOM   4896 C CB  . ILE B 1 96  ? -19.660 43.581 4.423   1.00 25.49 ? 96  ILE B CB  1 
ATOM   4897 C CG1 . ILE B 1 96  ? -18.305 43.314 3.759   1.00 24.99 ? 96  ILE B CG1 1 
ATOM   4898 C CG2 . ILE B 1 96  ? -19.831 45.082 4.658   1.00 29.26 ? 96  ILE B CG2 1 
ATOM   4899 C CD1 . ILE B 1 96  ? -18.231 43.804 2.309   1.00 29.65 ? 96  ILE B CD1 1 
ATOM   4900 N N   . GLU B 1 97  ? -22.174 42.634 6.144   1.00 21.48 ? 97  GLU B N   1 
ATOM   4901 C CA  . GLU B 1 97  ? -23.419 42.853 6.880   1.00 26.18 ? 97  GLU B CA  1 
ATOM   4902 C C   . GLU B 1 97  ? -23.239 42.547 8.361   1.00 25.13 ? 97  GLU B C   1 
ATOM   4903 O O   . GLU B 1 97  ? -23.600 43.349 9.233   1.00 22.88 ? 97  GLU B O   1 
ATOM   4904 C CB  . GLU B 1 97  ? -24.523 41.956 6.310   1.00 35.56 ? 97  GLU B CB  1 
ATOM   4905 C CG  . GLU B 1 97  ? -25.493 42.583 5.337   1.00 51.92 ? 97  GLU B CG  1 
ATOM   4906 C CD  . GLU B 1 97  ? -26.282 41.523 4.582   1.00 63.99 ? 97  GLU B CD  1 
ATOM   4907 O OE1 . GLU B 1 97  ? -25.689 40.489 4.211   1.00 67.81 ? 97  GLU B OE1 1 
ATOM   4908 O OE2 . GLU B 1 97  ? -27.501 41.704 4.388   1.00 69.53 ? 97  GLU B OE2 1 
ATOM   4909 N N   . PHE B 1 98  ? -22.711 41.358 8.655   1.00 18.36 ? 98  PHE B N   1 
ATOM   4910 C CA  . PHE B 1 98  ? -22.554 40.911 10.033  1.00 16.58 ? 98  PHE B CA  1 
ATOM   4911 C C   . PHE B 1 98  ? -21.590 41.810 10.793  1.00 18.35 ? 98  PHE B C   1 
ATOM   4912 O O   . PHE B 1 98  ? -21.823 42.131 11.963  1.00 18.66 ? 98  PHE B O   1 
ATOM   4913 C CB  . PHE B 1 98  ? -22.054 39.473 10.036  1.00 16.17 ? 98  PHE B CB  1 
ATOM   4914 C CG  . PHE B 1 98  ? -22.087 38.811 11.387  1.00 21.20 ? 98  PHE B CG  1 
ATOM   4915 C CD1 . PHE B 1 98  ? -23.277 38.317 11.897  1.00 20.54 ? 98  PHE B CD1 1 
ATOM   4916 C CD2 . PHE B 1 98  ? -20.925 38.655 12.130  1.00 23.22 ? 98  PHE B CD2 1 
ATOM   4917 C CE1 . PHE B 1 98  ? -23.314 37.683 13.126  1.00 21.04 ? 98  PHE B CE1 1 
ATOM   4918 C CE2 . PHE B 1 98  ? -20.957 38.025 13.370  1.00 17.27 ? 98  PHE B CE2 1 
ATOM   4919 C CZ  . PHE B 1 98  ? -22.164 37.539 13.862  1.00 18.62 ? 98  PHE B CZ  1 
ATOM   4920 N N   . THR B 1 99  ? -20.481 42.198 10.148  1.00 20.76 ? 99  THR B N   1 
ATOM   4921 C CA  . THR B 1 99  ? -19.556 43.144 10.764  1.00 18.28 ? 99  THR B CA  1 
ATOM   4922 C C   . THR B 1 99  ? -20.263 44.455 11.103  1.00 17.42 ? 99  THR B C   1 
ATOM   4923 O O   . THR B 1 99  ? -20.119 44.984 12.212  1.00 17.53 ? 99  THR B O   1 
ATOM   4924 C CB  . THR B 1 99  ? -18.364 43.391 9.830   1.00 24.78 ? 99  THR B CB  1 
ATOM   4925 O OG1 . THR B 1 99  ? -17.758 42.135 9.487   1.00 19.40 ? 99  THR B OG1 1 
ATOM   4926 C CG2 . THR B 1 99  ? -17.321 44.278 10.504  1.00 20.83 ? 99  THR B CG2 1 
ATOM   4927 N N   . LYS B 1 100 ? -21.046 44.986 10.165  1.00 18.60 ? 100 LYS B N   1 
ATOM   4928 C CA  . LYS B 1 100 ? -21.706 46.268 10.393  1.00 20.58 ? 100 LYS B CA  1 
ATOM   4929 C C   . LYS B 1 100 ? -22.714 46.185 11.534  1.00 19.12 ? 100 LYS B C   1 
ATOM   4930 O O   . LYS B 1 100 ? -22.896 47.157 12.280  1.00 21.43 ? 100 LYS B O   1 
ATOM   4931 C CB  . LYS B 1 100 ? -22.401 46.743 9.112   1.00 28.77 ? 100 LYS B CB  1 
ATOM   4932 C CG  . LYS B 1 100 ? -21.449 47.224 8.027   1.00 39.47 ? 100 LYS B CG  1 
ATOM   4933 C CD  . LYS B 1 100 ? -22.219 47.802 6.844   1.00 48.07 ? 100 LYS B CD  1 
ATOM   4934 C CE  . LYS B 1 100 ? -21.279 48.353 5.782   1.00 52.68 ? 100 LYS B CE  1 
ATOM   4935 N NZ  . LYS B 1 100 ? -22.015 48.797 4.560   1.00 56.72 ? 100 LYS B NZ  1 
ATOM   4936 N N   . LEU B 1 101 ? -23.401 45.049 11.671  1.00 20.58 ? 101 LEU B N   1 
ATOM   4937 C CA  . LEU B 1 101 ? -24.365 44.903 12.760  1.00 19.39 ? 101 LEU B CA  1 
ATOM   4938 C C   . LEU B 1 101 ? -23.682 44.944 14.127  1.00 19.94 ? 101 LEU B C   1 
ATOM   4939 O O   . LEU B 1 101 ? -24.273 45.410 15.109  1.00 21.05 ? 101 LEU B O   1 
ATOM   4940 C CB  . LEU B 1 101 ? -25.138 43.594 12.595  1.00 24.29 ? 101 LEU B CB  1 
ATOM   4941 C CG  . LEU B 1 101 ? -26.081 43.200 13.739  1.00 30.43 ? 101 LEU B CG  1 
ATOM   4942 C CD1 . LEU B 1 101 ? -27.272 44.145 13.820  1.00 32.25 ? 101 LEU B CD1 1 
ATOM   4943 C CD2 . LEU B 1 101 ? -26.546 41.755 13.596  1.00 33.91 ? 101 LEU B CD2 1 
ATOM   4944 N N   . ASN B 1 102 ? -22.451 44.458 14.215  1.00 15.94 ? 102 ASN B N   1 
ATOM   4945 C CA  . ASN B 1 102 ? -21.757 44.317 15.490  1.00 16.62 ? 102 ASN B CA  1 
ATOM   4946 C C   . ASN B 1 102 ? -20.699 45.384 15.697  1.00 18.26 ? 102 ASN B C   1 
ATOM   4947 O O   . ASN B 1 102 ? -20.023 45.383 16.736  1.00 16.97 ? 102 ASN B O   1 
ATOM   4948 C CB  . ASN B 1 102 ? -21.107 42.933 15.570  1.00 16.70 ? 102 ASN B CB  1 
ATOM   4949 C CG  . ASN B 1 102 ? -22.123 41.813 15.666  1.00 22.54 ? 102 ASN B CG  1 
ATOM   4950 O OD1 . ASN B 1 102 ? -22.991 41.814 16.536  1.00 23.07 ? 102 ASN B OD1 1 
ATOM   4951 N ND2 . ASN B 1 102 ? -22.034 40.856 14.742  1.00 22.79 ? 102 ASN B ND2 1 
ATOM   4952 N N   . TYR B 1 103 ? -20.575 46.301 14.737  1.00 18.12 ? 103 TYR B N   1 
ATOM   4953 C CA  . TYR B 1 103 ? -19.410 47.174 14.593  1.00 23.13 ? 103 TYR B CA  1 
ATOM   4954 C C   . TYR B 1 103 ? -19.184 48.070 15.811  1.00 23.11 ? 103 TYR B C   1 
ATOM   4955 O O   . TYR B 1 103 ? -18.034 48.336 16.185  1.00 22.17 ? 103 TYR B O   1 
ATOM   4956 C CB  . TYR B 1 103 ? -19.605 48.017 13.327  1.00 26.20 ? 103 TYR B CB  1 
ATOM   4957 C CG  . TYR B 1 103 ? -18.536 49.044 13.052  1.00 28.86 ? 103 TYR B CG  1 
ATOM   4958 C CD1 . TYR B 1 103 ? -17.393 48.712 12.329  1.00 29.82 ? 103 TYR B CD1 1 
ATOM   4959 C CD2 . TYR B 1 103 ? -18.679 50.353 13.493  1.00 32.89 ? 103 TYR B CD2 1 
ATOM   4960 C CE1 . TYR B 1 103 ? -16.420 49.663 12.063  1.00 37.10 ? 103 TYR B CE1 1 
ATOM   4961 C CE2 . TYR B 1 103 ? -17.717 51.304 13.241  1.00 37.30 ? 103 TYR B CE2 1 
ATOM   4962 C CZ  . TYR B 1 103 ? -16.588 50.954 12.523  1.00 41.56 ? 103 TYR B CZ  1 
ATOM   4963 O OH  . TYR B 1 103 ? -15.628 51.901 12.269  1.00 40.61 ? 103 TYR B OH  1 
ATOM   4964 N N   . GLU B 1 104 ? -20.258 48.575 16.417  1.00 17.92 ? 104 GLU B N   1 
ATOM   4965 C CA  . GLU B 1 104 ? -20.158 49.509 17.535  1.00 18.28 ? 104 GLU B CA  1 
ATOM   4966 C C   . GLU B 1 104 ? -20.022 48.816 18.896  1.00 20.65 ? 104 GLU B C   1 
ATOM   4967 O O   . GLU B 1 104 ? -19.870 49.501 19.909  1.00 23.89 ? 104 GLU B O   1 
ATOM   4968 C CB  . GLU B 1 104 ? -21.379 50.443 17.556  1.00 20.22 ? 104 GLU B CB  1 
ATOM   4969 C CG  . GLU B 1 104 ? -21.605 51.269 16.282  1.00 27.46 ? 104 GLU B CG  1 
ATOM   4970 C CD  . GLU B 1 104 ? -20.530 52.319 16.048  1.00 36.87 ? 104 GLU B CD  1 
ATOM   4971 O OE1 . GLU B 1 104 ? -19.868 52.722 17.028  1.00 40.68 ? 104 GLU B OE1 1 
ATOM   4972 O OE2 . GLU B 1 104 ? -20.372 52.771 14.891  1.00 42.17 ? 104 GLU B OE2 1 
ATOM   4973 N N   . LYS B 1 105 ? -20.065 47.485 18.953  1.00 15.71 ? 105 LYS B N   1 
ATOM   4974 C CA  . LYS B 1 105 ? -19.925 46.821 20.250  1.00 14.69 ? 105 LYS B CA  1 
ATOM   4975 C C   . LYS B 1 105 ? -18.459 46.812 20.697  1.00 19.89 ? 105 LYS B C   1 
ATOM   4976 O O   . LYS B 1 105 ? -17.561 46.631 19.873  1.00 18.32 ? 105 LYS B O   1 
ATOM   4977 C CB  . LYS B 1 105 ? -20.461 45.404 20.159  1.00 16.16 ? 105 LYS B CB  1 
ATOM   4978 C CG  . LYS B 1 105 ? -21.928 45.385 19.743  1.00 20.48 ? 105 LYS B CG  1 
ATOM   4979 C CD  . LYS B 1 105 ? -22.408 43.973 19.457  1.00 14.31 ? 105 LYS B CD  1 
ATOM   4980 C CE  . LYS B 1 105 ? -23.843 44.006 18.930  1.00 16.41 ? 105 LYS B CE  1 
ATOM   4981 N NZ  . LYS B 1 105 ? -24.331 42.614 18.666  1.00 17.99 ? 105 LYS B NZ  1 
ATOM   4982 N N   . PRO B 1 106 ? -18.188 47.024 21.992  1.00 16.07 ? 106 PRO B N   1 
ATOM   4983 C CA  . PRO B 1 106 ? -16.792 47.047 22.463  1.00 17.77 ? 106 PRO B CA  1 
ATOM   4984 C C   . PRO B 1 106 ? -15.986 45.809 22.124  1.00 17.87 ? 106 PRO B C   1 
ATOM   4985 O O   . PRO B 1 106 ? -14.771 45.929 21.909  1.00 19.56 ? 106 PRO B O   1 
ATOM   4986 C CB  . PRO B 1 106 ? -16.942 47.221 23.980  1.00 18.68 ? 106 PRO B CB  1 
ATOM   4987 C CG  . PRO B 1 106 ? -18.247 47.961 24.135  1.00 19.27 ? 106 PRO B CG  1 
ATOM   4988 C CD  . PRO B 1 106 ? -19.136 47.431 23.050  1.00 16.46 ? 106 PRO B CD  1 
ATOM   4989 N N   . ILE B 1 107 ? -16.605 44.626 22.033  1.00 15.60 ? 107 ILE B N   1 
ATOM   4990 C CA  . ILE B 1 107 ? -15.841 43.444 21.656  1.00 13.13 ? 107 ILE B CA  1 
ATOM   4991 C C   . ILE B 1 107 ? -15.361 43.516 20.204  1.00 14.24 ? 107 ILE B C   1 
ATOM   4992 O O   . ILE B 1 107 ? -14.456 42.759 19.819  1.00 14.28 ? 107 ILE B O   1 
ATOM   4993 C CB  . ILE B 1 107 ? -16.665 42.161 21.900  1.00 15.27 ? 107 ILE B CB  1 
ATOM   4994 C CG1 . ILE B 1 107 ? -17.947 42.173 21.065  1.00 15.21 ? 107 ILE B CG1 1 
ATOM   4995 C CG2 . ILE B 1 107 ? -16.988 42.025 23.396  1.00 14.32 ? 107 ILE B CG2 1 
ATOM   4996 C CD1 . ILE B 1 107 ? -18.624 40.805 20.974  1.00 15.49 ? 107 ILE B CD1 1 
ATOM   4997 N N   . TYR B 1 108 ? -15.914 44.427 19.395  1.00 17.14 ? 108 TYR B N   1 
ATOM   4998 C CA  . TYR B 1 108 ? -15.450 44.660 18.038  1.00 17.41 ? 108 TYR B CA  1 
ATOM   4999 C C   . TYR B 1 108 ? -14.472 45.834 17.926  1.00 19.10 ? 108 TYR B C   1 
ATOM   5000 O O   . TYR B 1 108 ? -14.213 46.300 16.807  1.00 20.96 ? 108 TYR B O   1 
ATOM   5001 C CB  . TYR B 1 108 ? -16.632 44.892 17.085  1.00 14.65 ? 108 TYR B CB  1 
ATOM   5002 C CG  . TYR B 1 108 ? -17.185 43.620 16.473  1.00 15.82 ? 108 TYR B CG  1 
ATOM   5003 C CD1 . TYR B 1 108 ? -17.901 42.682 17.227  1.00 13.01 ? 108 TYR B CD1 1 
ATOM   5004 C CD2 . TYR B 1 108 ? -16.910 43.315 15.141  1.00 15.77 ? 108 TYR B CD2 1 
ATOM   5005 C CE1 . TYR B 1 108 ? -18.361 41.504 16.642  1.00 15.62 ? 108 TYR B CE1 1 
ATOM   5006 C CE2 . TYR B 1 108 ? -17.354 42.153 14.566  1.00 20.48 ? 108 TYR B CE2 1 
ATOM   5007 C CZ  . TYR B 1 108 ? -18.081 41.253 15.313  1.00 18.84 ? 108 TYR B CZ  1 
ATOM   5008 O OH  . TYR B 1 108 ? -18.507 40.095 14.714  1.00 18.95 ? 108 TYR B OH  1 
ATOM   5009 N N   . ARG B 1 109 ? -13.914 46.316 19.038  1.00 17.12 ? 109 ARG B N   1 
ATOM   5010 C CA  . ARG B 1 109 ? -13.008 47.473 19.009  1.00 25.43 ? 109 ARG B CA  1 
ATOM   5011 C C   . ARG B 1 109 ? -11.617 47.010 18.564  1.00 23.64 ? 109 ARG B C   1 
ATOM   5012 O O   . ARG B 1 109 ? -10.733 46.698 19.365  1.00 22.54 ? 109 ARG B O   1 
ATOM   5013 C CB  . ARG B 1 109 ? -12.968 48.176 20.370  1.00 28.95 ? 109 ARG B CB  1 
ATOM   5014 C CG  . ARG B 1 109 ? -11.831 49.214 20.506  1.00 41.69 ? 109 ARG B CG  1 
ATOM   5015 C CD  . ARG B 1 109 ? -11.946 50.126 21.719  1.00 47.72 ? 109 ARG B CD  1 
ATOM   5016 N NE  . ARG B 1 109 ? -13.287 50.130 22.287  1.00 49.45 ? 109 ARG B NE  1 
ATOM   5017 C CZ  . ARG B 1 109 ? -13.509 50.130 23.594  1.00 49.16 ? 109 ARG B CZ  1 
ATOM   5018 N NH1 . ARG B 1 109 ? -12.474 50.117 24.425  1.00 55.15 ? 109 ARG B NH1 1 
ATOM   5019 N NH2 . ARG B 1 109 ? -14.749 50.128 24.072  1.00 46.97 ? 109 ARG B NH2 1 
ATOM   5020 N N   . PHE B 1 110 ? -11.454 46.901 17.249  1.00 21.57 ? 110 PHE B N   1 
ATOM   5021 C CA  . PHE B 1 110 ? -10.168 46.651 16.609  1.00 23.20 ? 110 PHE B CA  1 
ATOM   5022 C C   . PHE B 1 110 ? -9.972  47.754 15.584  1.00 21.50 ? 110 PHE B C   1 
ATOM   5023 O O   . PHE B 1 110 ? -10.864 47.994 14.768  1.00 21.66 ? 110 PHE B O   1 
ATOM   5024 C CB  . PHE B 1 110 ? -10.122 45.291 15.897  1.00 25.76 ? 110 PHE B CB  1 
ATOM   5025 C CG  . PHE B 1 110 ? -10.246 44.099 16.806  1.00 22.26 ? 110 PHE B CG  1 
ATOM   5026 C CD1 . PHE B 1 110 ? -9.131  43.549 17.420  1.00 21.77 ? 110 PHE B CD1 1 
ATOM   5027 C CD2 . PHE B 1 110 ? -11.480 43.518 17.027  1.00 24.10 ? 110 PHE B CD2 1 
ATOM   5028 C CE1 . PHE B 1 110 ? -9.254  42.452 18.242  1.00 21.30 ? 110 PHE B CE1 1 
ATOM   5029 C CE2 . PHE B 1 110 ? -11.609 42.426 17.844  1.00 22.79 ? 110 PHE B CE2 1 
ATOM   5030 C CZ  . PHE B 1 110 ? -10.490 41.889 18.451  1.00 17.33 ? 110 PHE B CZ  1 
ATOM   5031 N N   . GLU B 1 111 ? -8.815  48.420 15.612  1.00 25.51 ? 111 GLU B N   1 
ATOM   5032 C CA  . GLU B 1 111 ? -8.590  49.477 14.631  1.00 28.53 ? 111 GLU B CA  1 
ATOM   5033 C C   . GLU B 1 111 ? -8.652  48.930 13.209  1.00 26.33 ? 111 GLU B C   1 
ATOM   5034 O O   . GLU B 1 111 ? -9.169  49.604 12.305  1.00 26.94 ? 111 GLU B O   1 
ATOM   5035 C CB  . GLU B 1 111 ? -7.262  50.192 14.891  1.00 39.56 ? 111 GLU B CB  1 
ATOM   5036 C CG  . GLU B 1 111 ? -6.755  50.942 13.655  1.00 56.93 ? 111 GLU B CG  1 
ATOM   5037 C CD  . GLU B 1 111 ? -7.320  52.353 13.529  1.00 74.80 ? 111 GLU B CD  1 
ATOM   5038 O OE1 . GLU B 1 111 ? -6.917  53.083 12.596  1.00 81.58 ? 111 GLU B OE1 1 
ATOM   5039 O OE2 . GLU B 1 111 ? -8.184  52.723 14.351  1.00 79.23 ? 111 GLU B OE2 1 
ATOM   5040 N N   . ARG B 1 112 ? -8.208  47.685 13.009  1.00 26.31 ? 112 ARG B N   1 
ATOM   5041 C CA  . ARG B 1 112 ? -8.219  47.096 11.673  1.00 25.61 ? 112 ARG B CA  1 
ATOM   5042 C C   . ARG B 1 112 ? -9.640  46.961 11.138  1.00 26.73 ? 112 ARG B C   1 
ATOM   5043 O O   . ARG B 1 112 ? -9.876  47.165 9.941   1.00 27.76 ? 112 ARG B O   1 
ATOM   5044 C CB  . ARG B 1 112 ? -7.517  45.740 11.693  1.00 21.85 ? 112 ARG B CB  1 
ATOM   5045 C CG  . ARG B 1 112 ? -7.435  45.037 10.336  1.00 21.26 ? 112 ARG B CG  1 
ATOM   5046 C CD  . ARG B 1 112 ? -6.633  45.834 9.310   1.00 26.39 ? 112 ARG B CD  1 
ATOM   5047 N NE  . ARG B 1 112 ? -6.247  45.006 8.170   1.00 27.33 ? 112 ARG B NE  1 
ATOM   5048 C CZ  . ARG B 1 112 ? -5.818  45.486 7.006   1.00 33.69 ? 112 ARG B CZ  1 
ATOM   5049 N NH1 . ARG B 1 112 ? -5.723  46.795 6.819   1.00 31.16 ? 112 ARG B NH1 1 
ATOM   5050 N NH2 . ARG B 1 112 ? -5.484  44.656 6.026   1.00 35.78 ? 112 ARG B NH2 1 
ATOM   5051 N N   . ILE B 1 113 ? -10.606 46.633 12.009  1.00 21.23 ? 113 ILE B N   1 
ATOM   5052 C CA  . ILE B 1 113 ? -11.988 46.535 11.555  1.00 22.23 ? 113 ILE B CA  1 
ATOM   5053 C C   . ILE B 1 113 ? -12.468 47.887 11.056  1.00 27.89 ? 113 ILE B C   1 
ATOM   5054 O O   . ILE B 1 113 ? -13.099 47.994 9.994   1.00 27.07 ? 113 ILE B O   1 
ATOM   5055 C CB  . ILE B 1 113 ? -12.904 45.992 12.667  1.00 22.35 ? 113 ILE B CB  1 
ATOM   5056 C CG1 . ILE B 1 113 ? -12.680 44.493 12.887  1.00 22.49 ? 113 ILE B CG1 1 
ATOM   5057 C CG2 . ILE B 1 113 ? -14.360 46.264 12.305  1.00 20.62 ? 113 ILE B CG2 1 
ATOM   5058 C CD1 . ILE B 1 113 ? -13.510 43.916 14.015  1.00 23.95 ? 113 ILE B CD1 1 
ATOM   5059 N N   . ARG B 1 114 ? -12.156 48.946 11.804  1.00 27.70 ? 114 ARG B N   1 
ATOM   5060 C CA  . ARG B 1 114 ? -12.537 50.292 11.395  1.00 31.89 ? 114 ARG B CA  1 
ATOM   5061 C C   . ARG B 1 114 ? -11.879 50.666 10.068  1.00 32.46 ? 114 ARG B C   1 
ATOM   5062 O O   . ARG B 1 114 ? -12.475 51.384 9.258   1.00 35.44 ? 114 ARG B O   1 
ATOM   5063 C CB  . ARG B 1 114 ? -12.189 51.277 12.517  1.00 37.26 ? 114 ARG B CB  1 
ATOM   5064 C CG  . ARG B 1 114 ? -12.491 50.736 13.958  1.00 49.94 ? 114 ARG B CG  1 
ATOM   5065 C CD  . ARG B 1 114 ? -12.103 51.736 15.068  1.00 57.31 ? 114 ARG B CD  1 
ATOM   5066 N NE  . ARG B 1 114 ? -11.765 51.141 16.366  1.00 57.89 ? 114 ARG B NE  1 
ATOM   5067 C CZ  . ARG B 1 114 ? -10.622 51.380 17.007  1.00 57.70 ? 114 ARG B CZ  1 
ATOM   5068 N NH1 . ARG B 1 114 ? -9.717  52.173 16.449  1.00 57.57 ? 114 ARG B NH1 1 
ATOM   5069 N NH2 . ARG B 1 114 ? -10.369 50.831 18.187  1.00 58.13 ? 114 ARG B NH2 1 
ATOM   5070 N N   . GLU B 1 115 ? -10.673 50.155 9.806   1.00 30.90 ? 115 GLU B N   1 
ATOM   5071 C CA  . GLU B 1 115 ? -10.028 50.406 8.521   1.00 34.39 ? 115 GLU B CA  1 
ATOM   5072 C C   . GLU B 1 115 ? -10.740 49.676 7.393   1.00 33.71 ? 115 GLU B C   1 
ATOM   5073 O O   . GLU B 1 115 ? -11.022 50.263 6.341   1.00 35.63 ? 115 GLU B O   1 
ATOM   5074 C CB  . GLU B 1 115 ? -8.566  49.963 8.560   1.00 37.17 ? 115 GLU B CB  1 
ATOM   5075 C CG  . GLU B 1 115 ? -7.673  50.732 9.488   1.00 41.90 ? 115 GLU B CG  1 
ATOM   5076 C CD  . GLU B 1 115 ? -6.236  50.247 9.404   1.00 47.05 ? 115 GLU B CD  1 
ATOM   5077 O OE1 . GLU B 1 115 ? -5.966  49.309 8.617   1.00 46.07 ? 115 GLU B OE1 1 
ATOM   5078 O OE2 . GLU B 1 115 ? -5.382  50.795 10.131  1.00 46.70 ? 115 GLU B OE2 1 
ATOM   5079 N N   . LEU B 1 116 ? -10.988 48.376 7.574   1.00 26.95 ? 116 LEU B N   1 
ATOM   5080 C CA  . LEU B 1 116 ? -11.586 47.562 6.518   1.00 29.56 ? 116 LEU B CA  1 
ATOM   5081 C C   . LEU B 1 116 ? -12.976 48.055 6.138   1.00 28.54 ? 116 LEU B C   1 
ATOM   5082 O O   . LEU B 1 116 ? -13.366 47.982 4.967   1.00 32.53 ? 116 LEU B O   1 
ATOM   5083 C CB  . LEU B 1 116 ? -11.659 46.101 6.970   1.00 26.10 ? 116 LEU B CB  1 
ATOM   5084 C CG  . LEU B 1 116 ? -10.330 45.416 7.298   1.00 22.71 ? 116 LEU B CG  1 
ATOM   5085 C CD1 . LEU B 1 116 ? -10.598 44.068 7.988   1.00 26.00 ? 116 LEU B CD1 1 
ATOM   5086 C CD2 . LEU B 1 116 ? -9.443  45.242 6.068   1.00 26.66 ? 116 LEU B CD2 1 
ATOM   5087 N N   . MET B 1 117 ? -13.739 48.554 7.108   1.00 28.72 ? 117 MET B N   1 
ATOM   5088 C CA  . MET B 1 117 ? -15.089 49.019 6.823   1.00 31.49 ? 117 MET B CA  1 
ATOM   5089 C C   . MET B 1 117 ? -15.105 50.373 6.124   1.00 38.57 ? 117 MET B C   1 
ATOM   5090 O O   . MET B 1 117 ? -16.137 50.752 5.555   1.00 39.36 ? 117 MET B O   1 
ATOM   5091 C CB  . MET B 1 117 ? -15.904 49.069 8.116   1.00 31.93 ? 117 MET B CB  1 
ATOM   5092 C CG  . MET B 1 117 ? -16.136 47.698 8.749   1.00 29.20 ? 117 MET B CG  1 
ATOM   5093 S SD  . MET B 1 117 ? -17.122 46.581 7.710   1.00 37.25 ? 117 MET B SD  1 
ATOM   5094 C CE  . MET B 1 117 ? -15.839 45.596 6.957   1.00 41.87 ? 117 MET B CE  1 
ATOM   5095 N N   . ASN B 1 118 ? -13.988 51.099 6.139   1.00 41.93 ? 118 ASN B N   1 
ATOM   5096 C CA  . ASN B 1 118 ? -13.868 52.357 5.412   1.00 46.26 ? 118 ASN B CA  1 
ATOM   5097 C C   . ASN B 1 118 ? -13.372 52.175 3.986   1.00 47.73 ? 118 ASN B C   1 
ATOM   5098 O O   . ASN B 1 118 ? -13.239 53.166 3.261   1.00 52.90 ? 118 ASN B O   1 
ATOM   5099 C CB  . ASN B 1 118 ? -12.929 53.313 6.151   1.00 50.86 ? 118 ASN B CB  1 
ATOM   5100 C CG  . ASN B 1 118 ? -13.575 53.933 7.363   1.00 58.58 ? 118 ASN B CG  1 
ATOM   5101 O OD1 . ASN B 1 118 ? -14.755 54.281 7.339   1.00 64.83 ? 118 ASN B OD1 1 
ATOM   5102 N ND2 . ASN B 1 118 ? -12.805 54.085 8.434   1.00 60.70 ? 118 ASN B ND2 1 
ATOM   5103 N N   . LYS B 1 119 ? -13.105 50.955 3.570   1.00 45.19 ? 119 LYS B N   1 
ATOM   5104 C CA  . LYS B 1 119 ? -12.617 50.687 2.247   1.00 49.23 ? 119 LYS B CA  1 
ATOM   5105 C C   . LYS B 1 119 ? -13.743 50.464 1.245   1.00 52.29 ? 119 LYS B C   1 
ATOM   5106 O O   . LYS B 1 119 ? -14.804 50.056 1.619   1.00 50.52 ? 119 LYS B O   1 
ATOM   5107 C CB  . LYS B 1 119 ? -11.710 49.486 2.306   1.00 47.61 ? 119 LYS B CB  1 
ATOM   5108 C CG  . LYS B 1 119 ? -10.276 49.878 2.353   1.00 51.11 ? 119 LYS B CG  1 
ATOM   5109 C CD  . LYS B 1 119 ? -9.458  49.001 3.231   1.00 52.68 ? 119 LYS B CD  1 
ATOM   5110 C CE  . LYS B 1 119 ? -8.178  49.706 3.519   1.00 55.16 ? 119 LYS B CE  1 
ATOM   5111 N NZ  . LYS B 1 119 ? -7.053  48.838 3.177   1.00 58.13 ? 119 LYS B NZ  1 
ATOM   5112 N N   . GLU B 1 120 ? -13.502 50.739 -0.032  1.00 53.95 ? 120 GLU B N   1 
ATOM   5113 C CA  . GLU B 1 120 ? -14.528 50.582 -1.049  1.00 58.27 ? 120 GLU B CA  1 
ATOM   5114 C C   . GLU B 1 120 ? -14.536 49.186 -1.625  1.00 56.83 ? 120 GLU B C   1 
ATOM   5115 O O   . GLU B 1 120 ? -15.541 48.724 -2.137  1.00 59.39 ? 120 GLU B O   1 
ATOM   5116 C CB  . GLU B 1 120 ? -14.336 51.582 -2.191  1.00 66.28 ? 120 GLU B CB  1 
ATOM   5117 C CG  . GLU B 1 120 ? -14.157 53.069 -1.817  1.00 71.29 ? 120 GLU B CG  1 
ATOM   5118 C CD  . GLU B 1 120 ? -14.154 53.988 -3.057  1.00 73.94 ? 120 GLU B CD  1 
ATOM   5119 O OE1 . GLU B 1 120 ? -14.857 53.639 -3.998  1.00 71.98 ? 120 GLU B OE1 1 
ATOM   5120 O OE2 . GLU B 1 120 ? -13.480 55.042 -3.060  1.00 76.06 ? 120 GLU B OE2 1 
ATOM   5121 N N   . LYS B 1 121 ? -13.399 48.528 -1.552  1.00 48.40 ? 121 LYS B N   1 
ATOM   5122 C CA  . LYS B 1 121 ? -13.263 47.181 -2.048  1.00 50.39 ? 121 LYS B CA  1 
ATOM   5123 C C   . LYS B 1 121 ? -12.192 46.541 -1.205  1.00 46.77 ? 121 LYS B C   1 
ATOM   5124 O O   . LYS B 1 121 ? -11.256 47.207 -0.831  1.00 49.60 ? 121 LYS B O   1 
ATOM   5125 C CB  . LYS B 1 121 ? -12.823 47.191 -3.512  1.00 57.43 ? 121 LYS B CB  1 
ATOM   5126 C CG  . LYS B 1 121 ? -13.211 45.962 -4.322  1.00 64.73 ? 121 LYS B CG  1 
ATOM   5127 C CD  . LYS B 1 121 ? -14.317 45.114 -3.698  1.00 69.49 ? 121 LYS B CD  1 
ATOM   5128 C CE  . LYS B 1 121 ? -13.948 43.630 -3.580  1.00 70.63 ? 121 LYS B CE  1 
ATOM   5129 N NZ  . LYS B 1 121 ? -14.863 42.903 -2.656  1.00 69.31 ? 121 LYS B NZ  1 
ATOM   5130 N N   . LEU B 1 122 ? -12.345 45.252 -0.918  1.00 41.71 ? 122 LEU B N   1 
ATOM   5131 C CA  . LEU B 1 122 ? -11.420 44.475 -0.102  1.00 34.31 ? 122 LEU B CA  1 
ATOM   5132 C C   . LEU B 1 122 ? -10.721 43.417 -0.948  1.00 36.12 ? 122 LEU B C   1 
ATOM   5133 O O   . LEU B 1 122 ? -11.362 42.725 -1.744  1.00 40.52 ? 122 LEU B O   1 
ATOM   5134 C CB  . LEU B 1 122 ? -12.154 43.803 1.068   1.00 34.08 ? 122 LEU B CB  1 
ATOM   5135 C CG  . LEU B 1 122 ? -12.926 44.699 2.045   1.00 33.74 ? 122 LEU B CG  1 
ATOM   5136 C CD1 . LEU B 1 122 ? -13.570 43.848 3.124   1.00 32.89 ? 122 LEU B CD1 1 
ATOM   5137 C CD2 . LEU B 1 122 ? -12.040 45.766 2.658   1.00 29.15 ? 122 LEU B CD2 1 
ATOM   5138 N N   . ASN B 1 123 ? -9.407  43.288 -0.769  1.00 34.23 ? 123 ASN B N   1 
ATOM   5139 C CA  . ASN B 1 123 ? -8.639  42.242 -1.429  1.00 29.98 ? 123 ASN B CA  1 
ATOM   5140 C C   . ASN B 1 123 ? -8.547  41.013 -0.525  1.00 27.01 ? 123 ASN B C   1 
ATOM   5141 O O   . ASN B 1 123 ? -9.179  40.946 0.531   1.00 29.04 ? 123 ASN B O   1 
ATOM   5142 C CB  . ASN B 1 123 ? -7.265  42.769 -1.843  1.00 30.23 ? 123 ASN B CB  1 
ATOM   5143 C CG  . ASN B 1 123 ? -6.417  43.230 -0.668  1.00 33.38 ? 123 ASN B CG  1 
ATOM   5144 O OD1 . ASN B 1 123 ? -6.620  42.827 0.471   1.00 31.71 ? 123 ASN B OD1 1 
ATOM   5145 N ND2 . ASN B 1 123 ? -5.464  44.109 -0.949  1.00 36.68 ? 123 ASN B ND2 1 
ATOM   5146 N N   . ARG B 1 124 ? -7.767  40.015 -0.952  1.00 30.19 ? 124 ARG B N   1 
ATOM   5147 C CA  . ARG B 1 124 ? -7.757  38.736 -0.241  1.00 28.49 ? 124 ARG B CA  1 
ATOM   5148 C C   . ARG B 1 124 ? -7.284  38.898 1.190   1.00 28.27 ? 124 ARG B C   1 
ATOM   5149 O O   . ARG B 1 124 ? -7.889  38.370 2.127   1.00 26.25 ? 124 ARG B O   1 
ATOM   5150 C CB  . ARG B 1 124 ? -6.865  37.724 -0.959  1.00 32.52 ? 124 ARG B CB  1 
ATOM   5151 C CG  . ARG B 1 124 ? -6.751  36.411 -0.187  1.00 27.60 ? 124 ARG B CG  1 
ATOM   5152 C CD  . ARG B 1 124 ? -5.886  35.370 -0.874  1.00 30.96 ? 124 ARG B CD  1 
ATOM   5153 N NE  . ARG B 1 124 ? -5.867  34.147 -0.078  1.00 28.86 ? 124 ARG B NE  1 
ATOM   5154 C CZ  . ARG B 1 124 ? -5.013  33.923 0.914   1.00 32.36 ? 124 ARG B CZ  1 
ATOM   5155 N NH1 . ARG B 1 124 ? -4.098  34.838 1.223   1.00 32.67 ? 124 ARG B NH1 1 
ATOM   5156 N NH2 . ARG B 1 124 ? -5.072  32.791 1.600   1.00 33.20 ? 124 ARG B NH2 1 
ATOM   5157 N N   . GLU B 1 125 ? -6.172  39.594 1.377   1.00 27.34 ? 125 GLU B N   1 
ATOM   5158 C CA  . GLU B 1 125 ? -5.606  39.676 2.716   1.00 27.73 ? 125 GLU B CA  1 
ATOM   5159 C C   . GLU B 1 125 ? -6.448  40.576 3.623   1.00 27.32 ? 125 GLU B C   1 
ATOM   5160 O O   . GLU B 1 125 ? -6.500  40.345 4.835   1.00 25.62 ? 125 GLU B O   1 
ATOM   5161 C CB  . GLU B 1 125 ? -4.149  40.109 2.591   1.00 40.30 ? 125 GLU B CB  1 
ATOM   5162 C CG  . GLU B 1 125 ? -3.282  39.005 1.913   1.00 52.46 ? 125 GLU B CG  1 
ATOM   5163 C CD  . GLU B 1 125 ? -3.503  38.875 0.392   1.00 58.65 ? 125 GLU B CD  1 
ATOM   5164 O OE1 . GLU B 1 125 ? -3.774  39.908 -0.268  1.00 56.48 ? 125 GLU B OE1 1 
ATOM   5165 O OE2 . GLU B 1 125 ? -3.433  37.732 -0.128  1.00 59.82 ? 125 GLU B OE2 1 
ATOM   5166 N N   . GLU B 1 126 ? -7.168  41.544 3.051   1.00 27.02 ? 126 GLU B N   1 
ATOM   5167 C CA  . GLU B 1 126 ? -8.103  42.336 3.843   1.00 26.22 ? 126 GLU B CA  1 
ATOM   5168 C C   . GLU B 1 126 ? -9.315  41.509 4.256   1.00 25.40 ? 126 GLU B C   1 
ATOM   5169 O O   . GLU B 1 126 ? -9.775  41.596 5.402   1.00 24.21 ? 126 GLU B O   1 
ATOM   5170 C CB  . GLU B 1 126 ? -8.526  43.575 3.044   1.00 27.39 ? 126 GLU B CB  1 
ATOM   5171 C CG  . GLU B 1 126 ? -7.411  44.620 2.954   1.00 31.01 ? 126 GLU B CG  1 
ATOM   5172 C CD  . GLU B 1 126 ? -7.609  45.630 1.836   1.00 38.58 ? 126 GLU B CD  1 
ATOM   5173 O OE1 . GLU B 1 126 ? -8.452  45.403 0.934   1.00 36.28 ? 126 GLU B OE1 1 
ATOM   5174 O OE2 . GLU B 1 126 ? -6.905  46.662 1.860   1.00 41.27 ? 126 GLU B OE2 1 
ATOM   5175 N N   . LEU B 1 127 ? -9.834  40.687 3.340   1.00 23.07 ? 127 LEU B N   1 
ATOM   5176 C CA  . LEU B 1 127 ? -10.927 39.790 3.691   1.00 21.24 ? 127 LEU B CA  1 
ATOM   5177 C C   . LEU B 1 127 ? -10.488 38.776 4.738   1.00 20.58 ? 127 LEU B C   1 
ATOM   5178 O O   . LEU B 1 127 ? -11.261 38.434 5.643   1.00 19.53 ? 127 LEU B O   1 
ATOM   5179 C CB  . LEU B 1 127 ? -11.449 39.083 2.440   1.00 21.92 ? 127 LEU B CB  1 
ATOM   5180 C CG  . LEU B 1 127 ? -12.337 39.938 1.534   1.00 28.75 ? 127 LEU B CG  1 
ATOM   5181 C CD1 . LEU B 1 127 ? -12.559 39.237 0.210   1.00 26.87 ? 127 LEU B CD1 1 
ATOM   5182 C CD2 . LEU B 1 127 ? -13.674 40.225 2.230   1.00 28.03 ? 127 LEU B CD2 1 
ATOM   5183 N N   . LEU B 1 128 ? -9.242  38.289 4.644   1.00 21.83 ? 128 LEU B N   1 
ATOM   5184 C CA  . LEU B 1 128 ? -8.731  37.402 5.686   1.00 22.91 ? 128 LEU B CA  1 
ATOM   5185 C C   . LEU B 1 128 ? -8.774  38.078 7.049   1.00 20.89 ? 128 LEU B C   1 
ATOM   5186 O O   . LEU B 1 128 ? -9.166  37.454 8.040   1.00 17.85 ? 128 LEU B O   1 
ATOM   5187 C CB  . LEU B 1 128 ? -7.304  36.951 5.389   1.00 23.05 ? 128 LEU B CB  1 
ATOM   5188 C CG  . LEU B 1 128 ? -7.078  35.639 4.636   1.00 28.86 ? 128 LEU B CG  1 
ATOM   5189 C CD1 . LEU B 1 128 ? -5.600  35.509 4.264   1.00 25.54 ? 128 LEU B CD1 1 
ATOM   5190 C CD2 . LEU B 1 128 ? -7.533  34.442 5.467   1.00 23.76 ? 128 LEU B CD2 1 
ATOM   5191 N N   . ASP B 1 129 ? -8.371  39.354 7.118   1.00 20.30 ? 129 ASP B N   1 
ATOM   5192 C CA  . ASP B 1 129 ? -8.443  40.070 8.388   1.00 22.22 ? 129 ASP B CA  1 
ATOM   5193 C C   . ASP B 1 129 ? -9.880  40.235 8.854   1.00 21.43 ? 129 ASP B C   1 
ATOM   5194 O O   . ASP B 1 129 ? -10.168 40.083 10.047  1.00 16.92 ? 129 ASP B O   1 
ATOM   5195 C CB  . ASP B 1 129 ? -7.761  41.434 8.289   1.00 25.24 ? 129 ASP B CB  1 
ATOM   5196 C CG  . ASP B 1 129 ? -6.247  41.330 8.285   1.00 27.20 ? 129 ASP B CG  1 
ATOM   5197 O OD1 . ASP B 1 129 ? -5.740  40.193 8.400   1.00 26.94 ? 129 ASP B OD1 1 
ATOM   5198 O OD2 . ASP B 1 129 ? -5.569  42.384 8.221   1.00 24.82 ? 129 ASP B OD2 1 
ATOM   5199 N N   . LEU B 1 130 ? -10.799 40.555 7.933   1.00 22.10 ? 130 LEU B N   1 
ATOM   5200 C CA  . LEU B 1 130 ? -12.203 40.691 8.307   1.00 20.58 ? 130 LEU B CA  1 
ATOM   5201 C C   . LEU B 1 130 ? -12.759 39.386 8.872   1.00 20.62 ? 130 LEU B C   1 
ATOM   5202 O O   . LEU B 1 130 ? -13.482 39.394 9.872   1.00 22.13 ? 130 LEU B O   1 
ATOM   5203 C CB  . LEU B 1 130 ? -13.025 41.145 7.098   1.00 24.03 ? 130 LEU B CB  1 
ATOM   5204 C CG  . LEU B 1 130 ? -14.475 41.529 7.391   1.00 28.22 ? 130 LEU B CG  1 
ATOM   5205 C CD1 . LEU B 1 130 ? -14.530 42.697 8.382   1.00 22.83 ? 130 LEU B CD1 1 
ATOM   5206 C CD2 . LEU B 1 130 ? -15.218 41.861 6.101   1.00 28.33 ? 130 LEU B CD2 1 
ATOM   5207 N N   . GLN B 1 131 ? -12.445 38.256 8.231   1.00 18.24 ? 131 GLN B N   1 
ATOM   5208 C CA  . GLN B 1 131 ? -12.904 36.958 8.722   1.00 16.97 ? 131 GLN B CA  1 
ATOM   5209 C C   . GLN B 1 131 ? -12.349 36.683 10.115  1.00 21.26 ? 131 GLN B C   1 
ATOM   5210 O O   . GLN B 1 131 ? -13.083 36.318 11.042  1.00 15.22 ? 131 GLN B O   1 
ATOM   5211 C CB  . GLN B 1 131 ? -12.448 35.858 7.768   1.00 16.39 ? 131 GLN B CB  1 
ATOM   5212 C CG  . GLN B 1 131 ? -13.215 35.747 6.463   1.00 21.63 ? 131 GLN B CG  1 
ATOM   5213 C CD  . GLN B 1 131 ? -12.463 34.915 5.465   1.00 23.41 ? 131 GLN B CD  1 
ATOM   5214 O OE1 . GLN B 1 131 ? -11.234 34.853 5.499   1.00 21.09 ? 131 GLN B OE1 1 
ATOM   5215 N NE2 . GLN B 1 131 ? -13.191 34.211 4.611   1.00 23.08 ? 131 GLN B NE2 1 
ATOM   5216 N N   . THR B 1 132 ? -11.040 36.838 10.267  1.00 19.86 ? 132 THR B N   1 
ATOM   5217 C CA  . THR B 1 132 ? -10.395 36.439 11.511  1.00 19.43 ? 132 THR B CA  1 
ATOM   5218 C C   . THR B 1 132 ? -10.767 37.375 12.657  1.00 15.53 ? 132 THR B C   1 
ATOM   5219 O O   . THR B 1 132 ? -10.900 36.939 13.806  1.00 18.77 ? 132 THR B O   1 
ATOM   5220 C CB  . THR B 1 132 ? -8.882  36.399 11.310  1.00 15.91 ? 132 THR B CB  1 
ATOM   5221 O OG1 . THR B 1 132 ? -8.584  35.606 10.154  1.00 19.41 ? 132 THR B OG1 1 
ATOM   5222 C CG2 . THR B 1 132 ? -8.204  35.781 12.531  1.00 17.92 ? 132 THR B CG2 1 
ATOM   5223 N N   . LEU B 1 133 ? -10.920 38.667 12.372  1.00 16.41 ? 133 LEU B N   1 
ATOM   5224 C CA  . LEU B 1 133 ? -11.296 39.597 13.431  1.00 14.43 ? 133 LEU B CA  1 
ATOM   5225 C C   . LEU B 1 133 ? -12.735 39.398 13.875  1.00 17.59 ? 133 LEU B C   1 
ATOM   5226 O O   . LEU B 1 133 ? -13.049 39.605 15.053  1.00 19.39 ? 133 LEU B O   1 
ATOM   5227 C CB  . LEU B 1 133 ? -11.062 41.039 12.969  1.00 15.33 ? 133 LEU B CB  1 
ATOM   5228 C CG  . LEU B 1 133 ? -9.564  41.381 12.927  1.00 21.87 ? 133 LEU B CG  1 
ATOM   5229 C CD1 . LEU B 1 133 ? -9.348  42.672 12.172  1.00 26.60 ? 133 LEU B CD1 1 
ATOM   5230 C CD2 . LEU B 1 133 ? -8.978  41.475 14.342  1.00 23.25 ? 133 LEU B CD2 1 
ATOM   5231 N N   . ASN B 1 134 ? -13.623 39.001 12.961  1.00 15.70 ? 134 ASN B N   1 
ATOM   5232 C CA  . ASN B 1 134 ? -14.961 38.610 13.393  1.00 16.17 ? 134 ASN B CA  1 
ATOM   5233 C C   . ASN B 1 134 ? -14.889 37.429 14.355  1.00 17.10 ? 134 ASN B C   1 
ATOM   5234 O O   . ASN B 1 134 ? -15.578 37.413 15.381  1.00 18.94 ? 134 ASN B O   1 
ATOM   5235 C CB  . ASN B 1 134 ? -15.829 38.301 12.174  1.00 16.72 ? 134 ASN B CB  1 
ATOM   5236 C CG  . ASN B 1 134 ? -16.569 39.534 11.658  1.00 18.88 ? 134 ASN B CG  1 
ATOM   5237 O OD1 . ASN B 1 134 ? -17.567 39.953 12.236  1.00 19.71 ? 134 ASN B OD1 1 
ATOM   5238 N ND2 . ASN B 1 134 ? -16.044 40.151 10.604  1.00 18.78 ? 134 ASN B ND2 1 
ATOM   5239 N N   . LEU B 1 135 ? -14.037 36.439 14.059  1.00 14.06 ? 135 LEU B N   1 
ATOM   5240 C CA  . LEU B 1 135 ? -13.854 35.339 15.002  1.00 16.31 ? 135 LEU B CA  1 
ATOM   5241 C C   . LEU B 1 135 ? -13.306 35.848 16.322  1.00 16.34 ? 135 LEU B C   1 
ATOM   5242 O O   . LEU B 1 135 ? -13.841 35.535 17.388  1.00 15.58 ? 135 LEU B O   1 
ATOM   5243 C CB  . LEU B 1 135 ? -12.903 34.285 14.440  1.00 16.83 ? 135 LEU B CB  1 
ATOM   5244 C CG  . LEU B 1 135 ? -13.404 33.364 13.338  1.00 20.49 ? 135 LEU B CG  1 
ATOM   5245 C CD1 . LEU B 1 135 ? -12.278 32.410 12.939  1.00 19.77 ? 135 LEU B CD1 1 
ATOM   5246 C CD2 . LEU B 1 135 ? -14.651 32.605 13.788  1.00 18.58 ? 135 LEU B CD2 1 
ATOM   5247 N N   . LEU B 1 136 ? -12.213 36.619 16.268  1.00 13.90 ? 136 LEU B N   1 
ATOM   5248 C CA  . LEU B 1 136 ? -11.549 37.017 17.507  1.00 13.99 ? 136 LEU B CA  1 
ATOM   5249 C C   . LEU B 1 136 ? -12.411 37.956 18.345  1.00 14.66 ? 136 LEU B C   1 
ATOM   5250 O O   . LEU B 1 136 ? -12.234 38.022 19.568  1.00 14.35 ? 136 LEU B O   1 
ATOM   5251 C CB  . LEU B 1 136 ? -10.200 37.669 17.200  1.00 17.90 ? 136 LEU B CB  1 
ATOM   5252 C CG  . LEU B 1 136 ? -9.120  36.726 16.649  1.00 16.29 ? 136 LEU B CG  1 
ATOM   5253 C CD1 . LEU B 1 136 ? -7.887  37.526 16.225  1.00 14.80 ? 136 LEU B CD1 1 
ATOM   5254 C CD2 . LEU B 1 136 ? -8.735  35.654 17.679  1.00 17.85 ? 136 LEU B CD2 1 
ATOM   5255 N N   . ALA B 1 137 ? -13.342 38.691 17.721  1.00 17.61 ? 137 ALA B N   1 
ATOM   5256 C CA  . ALA B 1 137 ? -14.197 39.583 18.496  1.00 14.94 ? 137 ALA B CA  1 
ATOM   5257 C C   . ALA B 1 137 ? -15.055 38.813 19.494  1.00 12.07 ? 137 ALA B C   1 
ATOM   5258 O O   . ALA B 1 137 ? -15.416 39.350 20.544  1.00 13.81 ? 137 ALA B O   1 
ATOM   5259 C CB  . ALA B 1 137 ? -15.091 40.408 17.567  1.00 14.05 ? 137 ALA B CB  1 
ATOM   5260 N N   . TRP B 1 138 ? -15.383 37.558 19.193  1.00 12.78 ? 138 TRP B N   1 
ATOM   5261 C CA  . TRP B 1 138 ? -16.205 36.721 20.064  1.00 11.65 ? 138 TRP B CA  1 
ATOM   5262 C C   . TRP B 1 138 ? -15.369 35.806 20.961  1.00 13.36 ? 138 TRP B C   1 
ATOM   5263 O O   . TRP B 1 138 ? -15.902 34.843 21.529  1.00 13.84 ? 138 TRP B O   1 
ATOM   5264 C CB  . TRP B 1 138 ? -17.173 35.899 19.215  1.00 10.16 ? 138 TRP B CB  1 
ATOM   5265 C CG  . TRP B 1 138 ? -18.169 36.776 18.490  1.00 11.40 ? 138 TRP B CG  1 
ATOM   5266 C CD1 . TRP B 1 138 ? -17.986 37.401 17.289  1.00 16.75 ? 138 TRP B CD1 1 
ATOM   5267 C CD2 . TRP B 1 138 ? -19.477 37.138 18.934  1.00 11.71 ? 138 TRP B CD2 1 
ATOM   5268 N NE1 . TRP B 1 138 ? -19.097 38.129 16.959  1.00 13.16 ? 138 TRP B NE1 1 
ATOM   5269 C CE2 . TRP B 1 138 ? -20.035 37.979 17.949  1.00 15.47 ? 138 TRP B CE2 1 
ATOM   5270 C CE3 . TRP B 1 138 ? -20.236 36.832 20.067  1.00 14.88 ? 138 TRP B CE3 1 
ATOM   5271 C CZ2 . TRP B 1 138 ? -21.309 38.522 18.067  1.00 18.92 ? 138 TRP B CZ2 1 
ATOM   5272 C CZ3 . TRP B 1 138 ? -21.508 37.372 20.178  1.00 19.64 ? 138 TRP B CZ3 1 
ATOM   5273 C CH2 . TRP B 1 138 ? -22.033 38.201 19.186  1.00 21.82 ? 138 TRP B CH2 1 
ATOM   5274 N N   . CYS B 1 139 ? -14.078 36.090 21.110  1.00 14.32 ? 139 CYS B N   1 
ATOM   5275 C CA  . CYS B 1 139 ? -13.231 35.274 21.978  1.00 10.76 ? 139 CYS B CA  1 
ATOM   5276 C C   . CYS B 1 139 ? -13.704 35.352 23.429  1.00 11.23 ? 139 CYS B C   1 
ATOM   5277 O O   . CYS B 1 139 ? -13.986 36.438 23.955  1.00 13.91 ? 139 CYS B O   1 
ATOM   5278 C CB  . CYS B 1 139 ? -11.776 35.722 21.870  1.00 12.16 ? 139 CYS B CB  1 
ATOM   5279 S SG  . CYS B 1 139 ? -10.601 34.606 22.687  1.00 18.51 ? 139 CYS B SG  1 
ATOM   5280 N N   . GLY B 1 140 ? -13.794 34.185 24.080  1.00 11.72 ? 140 GLY B N   1 
ATOM   5281 C CA  . GLY B 1 140 ? -14.254 34.132 25.450  1.00 14.53 ? 140 GLY B CA  1 
ATOM   5282 C C   . GLY B 1 140 ? -13.124 34.336 26.438  1.00 13.22 ? 140 GLY B C   1 
ATOM   5283 O O   . GLY B 1 140 ? -11.960 34.376 26.062  1.00 13.49 ? 140 GLY B O   1 
ATOM   5284 N N   . ARG B 1 141 ? -13.502 34.453 27.711  1.00 11.18 ? 141 ARG B N   1 
ATOM   5285 C CA  . ARG B 1 141 ? -12.537 34.704 28.779  1.00 11.86 ? 141 ARG B CA  1 
ATOM   5286 C C   . ARG B 1 141 ? -11.397 33.696 28.768  1.00 12.66 ? 141 ARG B C   1 
ATOM   5287 O O   . ARG B 1 141 ? -10.223 34.070 28.882  1.00 14.16 ? 141 ARG B O   1 
ATOM   5288 C CB  . ARG B 1 141 ? -13.259 34.668 30.124  1.00 12.31 ? 141 ARG B CB  1 
ATOM   5289 C CG  . ARG B 1 141 ? -12.359 34.885 31.340  1.00 15.16 ? 141 ARG B CG  1 
ATOM   5290 C CD  . ARG B 1 141 ? -13.226 35.095 32.586  1.00 15.38 ? 141 ARG B CD  1 
ATOM   5291 N NE  . ARG B 1 141 ? -12.421 35.120 33.799  1.00 15.95 ? 141 ARG B NE  1 
ATOM   5292 C CZ  . ARG B 1 141 ? -12.171 34.052 34.549  1.00 17.83 ? 141 ARG B CZ  1 
ATOM   5293 N NH1 . ARG B 1 141 ? -12.662 32.856 34.225  1.00 15.60 ? 141 ARG B NH1 1 
ATOM   5294 N NH2 . ARG B 1 141 ? -11.426 34.184 35.626  1.00 20.59 ? 141 ARG B NH2 1 
ATOM   5295 N N   . THR B 1 142 ? -11.723 32.411 28.616  1.00 12.76 ? 142 THR B N   1 
ATOM   5296 C CA  . THR B 1 142 ? -10.709 31.363 28.721  1.00 17.17 ? 142 THR B CA  1 
ATOM   5297 C C   . THR B 1 142 ? -9.655  31.490 27.625  1.00 20.35 ? 142 THR B C   1 
ATOM   5298 O O   . THR B 1 142 ? -8.446  31.425 27.889  1.00 21.15 ? 142 THR B O   1 
ATOM   5299 C CB  . THR B 1 142 ? -11.375 29.987 28.654  1.00 13.96 ? 142 THR B CB  1 
ATOM   5300 O OG1 . THR B 1 142 ? -12.250 29.817 29.774  1.00 16.85 ? 142 THR B OG1 1 
ATOM   5301 C CG2 . THR B 1 142 ? -10.325 28.875 28.658  1.00 20.20 ? 142 THR B CG2 1 
ATOM   5302 N N   . LEU B 1 143 ? -10.092 31.632 26.380  1.00 13.46 ? 143 LEU B N   1 
ATOM   5303 C CA  . LEU B 1 143 ? -9.143  31.650 25.279  1.00 17.10 ? 143 LEU B CA  1 
ATOM   5304 C C   . LEU B 1 143 ? -8.469  32.997 25.091  1.00 18.61 ? 143 LEU B C   1 
ATOM   5305 O O   . LEU B 1 143 ? -7.520  33.085 24.308  1.00 21.18 ? 143 LEU B O   1 
ATOM   5306 C CB  . LEU B 1 143 ? -9.824  31.253 23.972  1.00 20.05 ? 143 LEU B CB  1 
ATOM   5307 C CG  . LEU B 1 143 ? -10.156 29.777 23.828  1.00 20.47 ? 143 LEU B CG  1 
ATOM   5308 C CD1 . LEU B 1 143 ? -10.842 29.551 22.471  1.00 16.52 ? 143 LEU B CD1 1 
ATOM   5309 C CD2 . LEU B 1 143 ? -8.895  28.933 23.971  1.00 21.38 ? 143 LEU B CD2 1 
ATOM   5310 N N   . ARG B 1 144 ? -8.893  34.008 25.827  1.00 24.12 ? 144 ARG B N   1 
ATOM   5311 C CA  . ARG B 1 144 ? -8.247  35.300 25.762  1.00 28.04 ? 144 ARG B CA  1 
ATOM   5312 C C   . ARG B 1 144 ? -6.756  35.128 26.157  1.00 31.79 ? 144 ARG B C   1 
ATOM   5313 O O   . ARG B 1 144 ? -5.899  35.843 25.696  1.00 25.90 ? 144 ARG B O   1 
ATOM   5314 C CB  . ARG B 1 144 ? -9.024  36.383 26.567  1.00 28.60 ? 144 ARG B CB  1 
ATOM   5315 C CG  . ARG B 1 144 ? -9.928  37.281 25.683  1.00 40.14 ? 144 ARG B CG  1 
ATOM   5316 C CD  . ARG B 1 144 ? -11.245 37.821 26.271  1.00 45.70 ? 144 ARG B CD  1 
ATOM   5317 N NE  . ARG B 1 144 ? -12.205 38.517 25.399  1.00 39.05 ? 144 ARG B NE  1 
ATOM   5318 C CZ  . ARG B 1 144 ? -12.097 39.786 25.006  1.00 41.49 ? 144 ARG B CZ  1 
ATOM   5319 N NH1 . ARG B 1 144 ? -11.012 40.466 25.330  1.00 43.67 ? 144 ARG B NH1 1 
ATOM   5320 N NH2 . ARG B 1 144 ? -13.043 40.370 24.263  1.00 33.80 ? 144 ARG B NH2 1 
ATOM   5321 N N   . LYS B 1 145 ? -6.474  34.141 26.993  1.00 30.95 ? 145 LYS B N   1 
ATOM   5322 C CA  . LYS B 1 145 ? -5.104  33.847 27.382  1.00 34.67 ? 145 LYS B CA  1 
ATOM   5323 C C   . LYS B 1 145 ? -4.352  33.130 26.263  1.00 34.12 ? 145 LYS B C   1 
ATOM   5324 O O   . LYS B 1 145 ? -3.253  33.547 25.873  1.00 32.75 ? 145 LYS B O   1 
ATOM   5325 C CB  . LYS B 1 145 ? -5.096  33.023 28.676  1.00 44.54 ? 145 LYS B CB  1 
ATOM   5326 C CG  . LYS B 1 145 ? -4.163  31.818 28.683  1.00 53.93 ? 145 LYS B CG  1 
ATOM   5327 C CD  . LYS B 1 145 ? -2.733  32.209 29.023  1.00 63.35 ? 145 LYS B CD  1 
ATOM   5328 C CE  . LYS B 1 145 ? -1.962  31.066 29.678  1.00 66.67 ? 145 LYS B CE  1 
ATOM   5329 N NZ  . LYS B 1 145 ? -0.479  31.297 29.600  1.00 66.52 ? 145 LYS B NZ  1 
ATOM   5330 N N   . ASP B 1 146 ? -4.928  32.049 25.727  1.00 33.48 ? 146 ASP B N   1 
ATOM   5331 C CA  . ASP B 1 146 ? -4.218  31.273 24.716  1.00 35.04 ? 146 ASP B CA  1 
ATOM   5332 C C   . ASP B 1 146 ? -4.043  32.073 23.441  1.00 33.76 ? 146 ASP B C   1 
ATOM   5333 O O   . ASP B 1 146 ? -3.023  31.944 22.758  1.00 34.36 ? 146 ASP B O   1 
ATOM   5334 C CB  . ASP B 1 146 ? -4.954  29.968 24.404  1.00 47.03 ? 146 ASP B CB  1 
ATOM   5335 C CG  . ASP B 1 146 ? -5.341  29.198 25.647  1.00 65.05 ? 146 ASP B CG  1 
ATOM   5336 O OD1 . ASP B 1 146 ? -5.943  29.793 26.568  1.00 67.04 ? 146 ASP B OD1 1 
ATOM   5337 O OD2 . ASP B 1 146 ? -5.065  27.979 25.678  1.00 72.03 ? 146 ASP B OD2 1 
ATOM   5338 N N   . LEU B 1 147 ? -5.032  32.893 23.094  1.00 17.56 ? 147 LEU B N   1 
ATOM   5339 C CA  . LEU B 1 147 ? -5.026  33.599 21.822  1.00 20.24 ? 147 LEU B CA  1 
ATOM   5340 C C   . LEU B 1 147 ? -4.494  35.022 21.943  1.00 20.08 ? 147 LEU B C   1 
ATOM   5341 O O   . LEU B 1 147 ? -4.639  35.808 21.001  1.00 18.76 ? 147 LEU B O   1 
ATOM   5342 C CB  . LEU B 1 147 ? -6.428  33.607 21.215  1.00 18.86 ? 147 LEU B CB  1 
ATOM   5343 C CG  . LEU B 1 147 ? -6.973  32.226 20.838  1.00 21.15 ? 147 LEU B CG  1 
ATOM   5344 C CD1 . LEU B 1 147 ? -8.364  32.346 20.211  1.00 21.60 ? 147 LEU B CD1 1 
ATOM   5345 C CD2 . LEU B 1 147 ? -5.987  31.490 19.913  1.00 29.58 ? 147 LEU B CD2 1 
ATOM   5346 N N   . LYS B 1 148 ? -3.860  35.360 23.068  1.00 22.09 ? 148 LYS B N   1 
ATOM   5347 C CA  . LYS B 1 148 ? -3.411  36.731 23.273  1.00 18.46 ? 148 LYS B CA  1 
ATOM   5348 C C   . LYS B 1 148 ? -2.469  37.177 22.155  1.00 19.05 ? 148 LYS B C   1 
ATOM   5349 O O   . LYS B 1 148 ? -2.564  38.317 21.683  1.00 25.38 ? 148 LYS B O   1 
ATOM   5350 C CB  . LYS B 1 148 ? -2.742  36.866 24.642  1.00 24.25 ? 148 LYS B CB  1 
ATOM   5351 C CG  . LYS B 1 148 ? -2.256  38.268 24.950  1.00 27.06 ? 148 LYS B CG  1 
ATOM   5352 C CD  . LYS B 1 148 ? -1.836  38.396 26.407  1.00 34.92 ? 148 LYS B CD  1 
ATOM   5353 C CE  . LYS B 1 148 ? -1.083  39.690 26.650  1.00 43.21 ? 148 LYS B CE  1 
ATOM   5354 N NZ  . LYS B 1 148 ? -1.904  40.893 26.343  1.00 46.30 ? 148 LYS B NZ  1 
ATOM   5355 N N   . ASP B 1 149 ? -1.587  36.281 21.691  1.00 19.99 ? 149 ASP B N   1 
ATOM   5356 C CA  . ASP B 1 149 ? -0.713  36.591 20.554  1.00 26.42 ? 149 ASP B CA  1 
ATOM   5357 C C   . ASP B 1 149 ? -1.504  37.115 19.362  1.00 26.22 ? 149 ASP B C   1 
ATOM   5358 O O   . ASP B 1 149 ? -1.139  38.124 18.742  1.00 23.04 ? 149 ASP B O   1 
ATOM   5359 C CB  . ASP B 1 149 ? 0.072   35.349 20.106  1.00 38.93 ? 149 ASP B CB  1 
ATOM   5360 C CG  . ASP B 1 149 ? 1.087   34.876 21.127  1.00 52.79 ? 149 ASP B CG  1 
ATOM   5361 O OD1 . ASP B 1 149 ? 1.453   35.664 22.024  1.00 56.44 ? 149 ASP B OD1 1 
ATOM   5362 O OD2 . ASP B 1 149 ? 1.537   33.711 21.012  1.00 54.30 ? 149 ASP B OD2 1 
ATOM   5363 N N   . LEU B 1 150 ? -2.565  36.402 18.992  1.00 19.38 ? 150 LEU B N   1 
ATOM   5364 C CA  . LEU B 1 150 ? -3.322  36.787 17.806  1.00 22.51 ? 150 LEU B CA  1 
ATOM   5365 C C   . LEU B 1 150 ? -4.178  38.014 18.069  1.00 21.96 ? 150 LEU B C   1 
ATOM   5366 O O   . LEU B 1 150 ? -4.327  38.858 17.179  1.00 23.42 ? 150 LEU B O   1 
ATOM   5367 C CB  . LEU B 1 150 ? -4.185  35.621 17.323  1.00 19.85 ? 150 LEU B CB  1 
ATOM   5368 C CG  . LEU B 1 150 ? -3.402  34.456 16.717  1.00 29.72 ? 150 LEU B CG  1 
ATOM   5369 C CD1 . LEU B 1 150 ? -4.330  33.296 16.413  1.00 30.04 ? 150 LEU B CD1 1 
ATOM   5370 C CD2 . LEU B 1 150 ? -2.670  34.904 15.467  1.00 28.42 ? 150 LEU B CD2 1 
ATOM   5371 N N   . LEU B 1 151 ? -4.722  38.147 19.288  1.00 20.70 ? 151 LEU B N   1 
ATOM   5372 C CA  . LEU B 1 151 ? -5.497  39.334 19.645  1.00 24.92 ? 151 LEU B CA  1 
ATOM   5373 C C   . LEU B 1 151 ? -4.647  40.596 19.567  1.00 24.49 ? 151 LEU B C   1 
ATOM   5374 O O   . LEU B 1 151 ? -5.104  41.625 19.058  1.00 32.81 ? 151 LEU B O   1 
ATOM   5375 C CB  . LEU B 1 151 ? -6.086  39.176 21.050  1.00 23.10 ? 151 LEU B CB  1 
ATOM   5376 C CG  . LEU B 1 151 ? -7.230  38.161 21.124  1.00 24.78 ? 151 LEU B CG  1 
ATOM   5377 C CD1 . LEU B 1 151 ? -7.519  37.744 22.566  1.00 20.94 ? 151 LEU B CD1 1 
ATOM   5378 C CD2 . LEU B 1 151 ? -8.478  38.723 20.453  1.00 22.43 ? 151 LEU B CD2 1 
ATOM   5379 N N   . ASN B 1 152 ? -3.414  40.542 20.080  1.00 23.93 ? 152 ASN B N   1 
ATOM   5380 C CA  . ASN B 1 152 ? -2.531  41.703 20.033  1.00 25.18 ? 152 ASN B CA  1 
ATOM   5381 C C   . ASN B 1 152 ? -1.989  41.973 18.637  1.00 30.34 ? 152 ASN B C   1 
ATOM   5382 O O   . ASN B 1 152 ? -1.555  43.099 18.366  1.00 32.91 ? 152 ASN B O   1 
ATOM   5383 C CB  . ASN B 1 152 ? -1.349  41.537 20.988  1.00 34.93 ? 152 ASN B CB  1 
ATOM   5384 C CG  . ASN B 1 152 ? -1.770  41.531 22.440  1.00 41.57 ? 152 ASN B CG  1 
ATOM   5385 O OD1 . ASN B 1 152 ? -2.822  42.062 22.798  1.00 40.27 ? 152 ASN B OD1 1 
ATOM   5386 N ND2 . ASN B 1 152 ? -0.927  40.960 23.294  1.00 49.00 ? 152 ASN B ND2 1 
ATOM   5387 N N   . LYS B 1 153 ? -1.969  40.963 17.762  1.00 29.07 ? 153 LYS B N   1 
ATOM   5388 C CA  . LYS B 1 153 ? -1.455  41.161 16.409  1.00 27.52 ? 153 LYS B CA  1 
ATOM   5389 C C   . LYS B 1 153 ? -2.278  42.208 15.664  1.00 25.72 ? 153 LYS B C   1 
ATOM   5390 O O   . LYS B 1 153 ? -1.726  43.126 15.047  1.00 27.59 ? 153 LYS B O   1 
ATOM   5391 C CB  . LYS B 1 153 ? -1.450  39.832 15.653  1.00 31.70 ? 153 LYS B CB  1 
ATOM   5392 C CG  . LYS B 1 153 ? -0.788  39.880 14.283  1.00 34.43 ? 153 LYS B CG  1 
ATOM   5393 C CD  . LYS B 1 153 ? -0.810  38.508 13.611  1.00 33.81 ? 153 LYS B CD  1 
ATOM   5394 C CE  . LYS B 1 153 ? -0.148  38.553 12.244  1.00 39.28 ? 153 LYS B CE  1 
ATOM   5395 N NZ  . LYS B 1 153 ? -0.135  37.209 11.609  1.00 40.39 ? 153 LYS B NZ  1 
ATOM   5396 N N   . GLY B 1 154 ? -3.606  42.072 15.698  1.00 28.14 ? 154 GLY B N   1 
ATOM   5397 C CA  . GLY B 1 154 ? -4.512  43.097 15.227  1.00 27.51 ? 154 GLY B CA  1 
ATOM   5398 C C   . GLY B 1 154 ? -4.802  43.104 13.744  1.00 25.15 ? 154 GLY B C   1 
ATOM   5399 O O   . GLY B 1 154 ? -5.818  43.674 13.335  1.00 29.63 ? 154 GLY B O   1 
ATOM   5400 N N   . ARG B 1 155 ? -3.961  42.485 12.922  1.00 27.01 ? 155 ARG B N   1 
ATOM   5401 C CA  . ARG B 1 155 ? -4.080  42.599 11.474  1.00 26.07 ? 155 ARG B CA  1 
ATOM   5402 C C   . ARG B 1 155 ? -3.177  41.555 10.837  1.00 27.11 ? 155 ARG B C   1 
ATOM   5403 O O   . ARG B 1 155 ? -2.405  40.878 11.521  1.00 31.31 ? 155 ARG B O   1 
ATOM   5404 C CB  . ARG B 1 155 ? -3.690  43.999 10.995  1.00 29.08 ? 155 ARG B CB  1 
ATOM   5405 C CG  . ARG B 1 155 ? -2.248  44.348 11.323  1.00 40.39 ? 155 ARG B CG  1 
ATOM   5406 C CD  . ARG B 1 155 ? -1.919  45.776 10.931  1.00 43.71 ? 155 ARG B CD  1 
ATOM   5407 N NE  . ARG B 1 155 ? -2.785  46.730 11.619  1.00 45.64 ? 155 ARG B NE  1 
ATOM   5408 C CZ  . ARG B 1 155 ? -3.588  47.594 11.005  1.00 45.57 ? 155 ARG B CZ  1 
ATOM   5409 N NH1 . ARG B 1 155 ? -4.343  48.422 11.718  1.00 49.46 ? 155 ARG B NH1 1 
ATOM   5410 N NH2 . ARG B 1 155 ? -3.619  47.647 9.681   1.00 41.64 ? 155 ARG B NH2 1 
ATOM   5411 N N   . ASN B 1 156 ? -3.276  41.447 9.512   1.00 23.72 ? 156 ASN B N   1 
ATOM   5412 C CA  . ASN B 1 156 ? -2.354  40.636 8.716   1.00 25.89 ? 156 ASN B CA  1 
ATOM   5413 C C   . ASN B 1 156 ? -2.419  39.168 9.121   1.00 26.68 ? 156 ASN B C   1 
ATOM   5414 O O   . ASN B 1 156 ? -1.395  38.499 9.273   1.00 27.67 ? 156 ASN B O   1 
ATOM   5415 C CB  . ASN B 1 156 ? -0.922  41.163 8.821   1.00 33.11 ? 156 ASN B CB  1 
ATOM   5416 C CG  . ASN B 1 156 ? -0.743  42.484 8.119   1.00 42.33 ? 156 ASN B CG  1 
ATOM   5417 O OD1 . ASN B 1 156 ? -1.293  42.699 7.041   1.00 49.20 ? 156 ASN B OD1 1 
ATOM   5418 N ND2 . ASN B 1 156 ? 0.036   43.379 8.721   1.00 45.19 ? 156 ASN B ND2 1 
ATOM   5419 N N   . TYR B 1 157 ? -3.632  38.666 9.303   1.00 21.41 ? 157 TYR B N   1 
ATOM   5420 C CA  . TYR B 1 157 ? -3.833  37.270 9.649   1.00 20.68 ? 157 TYR B CA  1 
ATOM   5421 C C   . TYR B 1 157 ? -3.734  36.382 8.417   1.00 25.73 ? 157 TYR B C   1 
ATOM   5422 O O   . TYR B 1 157 ? -4.147  36.764 7.318   1.00 31.59 ? 157 TYR B O   1 
ATOM   5423 C CB  . TYR B 1 157 ? -5.196  37.090 10.309  1.00 19.12 ? 157 TYR B CB  1 
ATOM   5424 C CG  . TYR B 1 157 ? -5.324  37.857 11.601  1.00 18.80 ? 157 TYR B CG  1 
ATOM   5425 C CD1 . TYR B 1 157 ? -4.707  37.403 12.761  1.00 19.43 ? 157 TYR B CD1 1 
ATOM   5426 C CD2 . TYR B 1 157 ? -6.060  39.042 11.662  1.00 18.25 ? 157 TYR B CD2 1 
ATOM   5427 C CE1 . TYR B 1 157 ? -4.826  38.114 13.959  1.00 21.47 ? 157 TYR B CE1 1 
ATOM   5428 C CE2 . TYR B 1 157 ? -6.182  39.750 12.837  1.00 18.06 ? 157 TYR B CE2 1 
ATOM   5429 C CZ  . TYR B 1 157 ? -5.571  39.282 13.983  1.00 21.27 ? 157 TYR B CZ  1 
ATOM   5430 O OH  . TYR B 1 157 ? -5.705  39.983 15.157  1.00 17.58 ? 157 TYR B OH  1 
ATOM   5431 N N   . THR B 1 158 ? -3.190  35.188 8.607   1.00 25.50 ? 158 THR B N   1 
ATOM   5432 C CA  . THR B 1 158 ? -3.120  34.189 7.549   1.00 29.24 ? 158 THR B CA  1 
ATOM   5433 C C   . THR B 1 158 ? -4.304  33.230 7.645   1.00 21.18 ? 158 THR B C   1 
ATOM   5434 O O   . THR B 1 158 ? -5.020  33.182 8.654   1.00 20.00 ? 158 THR B O   1 
ATOM   5435 C CB  . THR B 1 158 ? -1.815  33.398 7.637   1.00 25.53 ? 158 THR B CB  1 
ATOM   5436 O OG1 . THR B 1 158 ? -1.800  32.674 8.874   1.00 26.00 ? 158 THR B OG1 1 
ATOM   5437 C CG2 . THR B 1 158 ? -0.598  34.327 7.574   1.00 28.39 ? 158 THR B CG2 1 
ATOM   5438 N N   . GLN B 1 159 ? -4.516  32.472 6.563   1.00 26.08 ? 159 GLN B N   1 
ATOM   5439 C CA  . GLN B 1 159 ? -5.529  31.416 6.584   1.00 28.86 ? 159 GLN B CA  1 
ATOM   5440 C C   . GLN B 1 159 ? -5.228  30.399 7.681   1.00 26.53 ? 159 GLN B C   1 
ATOM   5441 O O   . GLN B 1 159 ? -6.136  29.914 8.371   1.00 24.16 ? 159 GLN B O   1 
ATOM   5442 C CB  . GLN B 1 159 ? -5.588  30.731 5.212   1.00 28.88 ? 159 GLN B CB  1 
ATOM   5443 C CG  . GLN B 1 159 ? -6.508  29.516 5.095   1.00 29.10 ? 159 GLN B CG  1 
ATOM   5444 C CD  . GLN B 1 159 ? -7.988  29.881 5.143   1.00 30.55 ? 159 GLN B CD  1 
ATOM   5445 O OE1 . GLN B 1 159 ? -8.379  30.977 4.742   1.00 25.91 ? 159 GLN B OE1 1 
ATOM   5446 N NE2 . GLN B 1 159 ? -8.817  28.946 5.599   1.00 28.47 ? 159 GLN B NE2 1 
ATOM   5447 N N   . GLU B 1 160 ? -3.947  30.089 7.868   1.00 24.33 ? 160 GLU B N   1 
ATOM   5448 C CA  . GLU B 1 160 ? -3.531  29.130 8.882   1.00 24.72 ? 160 GLU B CA  1 
ATOM   5449 C C   . GLU B 1 160 ? -3.849  29.628 10.294  1.00 27.02 ? 160 GLU B C   1 
ATOM   5450 O O   . GLU B 1 160 ? -4.282  28.846 11.149  1.00 26.10 ? 160 GLU B O   1 
ATOM   5451 C CB  . GLU B 1 160 ? -2.036  28.845 8.702   1.00 32.38 ? 160 GLU B CB  1 
ATOM   5452 C CG  . GLU B 1 160 ? -1.725  28.104 7.383   1.00 45.16 ? 160 GLU B CG  1 
ATOM   5453 C CD  . GLU B 1 160 ? -1.837  28.970 6.102   1.00 47.07 ? 160 GLU B CD  1 
ATOM   5454 O OE1 . GLU B 1 160 ? -1.871  30.218 6.176   1.00 40.98 ? 160 GLU B OE1 1 
ATOM   5455 O OE2 . GLU B 1 160 ? -1.929  28.378 5.003   1.00 53.05 ? 160 GLU B OE2 1 
ATOM   5456 N N   . GLU B 1 161 ? -3.658  30.926 10.559  1.00 22.81 ? 161 GLU B N   1 
ATOM   5457 C CA  . GLU B 1 161 ? -3.982  31.446 11.885  1.00 25.70 ? 161 GLU B CA  1 
ATOM   5458 C C   . GLU B 1 161 ? -5.484  31.403 12.127  1.00 28.25 ? 161 GLU B C   1 
ATOM   5459 O O   . GLU B 1 161 ? -5.935  31.060 13.227  1.00 21.97 ? 161 GLU B O   1 
ATOM   5460 C CB  . GLU B 1 161 ? -3.434  32.869 12.041  1.00 22.65 ? 161 GLU B CB  1 
ATOM   5461 C CG  . GLU B 1 161 ? -1.902  32.916 12.119  1.00 22.67 ? 161 GLU B CG  1 
ATOM   5462 C CD  . GLU B 1 161 ? -1.323  34.308 11.908  1.00 33.12 ? 161 GLU B CD  1 
ATOM   5463 O OE1 . GLU B 1 161 ? -2.080  35.219 11.520  1.00 30.84 ? 161 GLU B OE1 1 
ATOM   5464 O OE2 . GLU B 1 161 ? -0.097  34.484 12.104  1.00 40.14 ? 161 GLU B OE2 1 
ATOM   5465 N N   . LYS B 1 162 ? -6.272  31.726 11.096  1.00 24.80 ? 162 LYS B N   1 
ATOM   5466 C CA  . LYS B 1 162 ? -7.724  31.685 11.217  1.00 22.47 ? 162 LYS B CA  1 
ATOM   5467 C C   . LYS B 1 162 ? -8.207  30.281 11.568  1.00 19.35 ? 162 LYS B C   1 
ATOM   5468 O O   . LYS B 1 162 ? -9.054  30.111 12.448  1.00 19.40 ? 162 LYS B O   1 
ATOM   5469 C CB  . LYS B 1 162 ? -8.359  32.163 9.909   1.00 19.07 ? 162 LYS B CB  1 
ATOM   5470 C CG  . LYS B 1 162 ? -9.876  32.071 9.877   1.00 21.27 ? 162 LYS B CG  1 
ATOM   5471 C CD  . LYS B 1 162 ? -10.448 32.665 8.574   1.00 20.25 ? 162 LYS B CD  1 
ATOM   5472 C CE  . LYS B 1 162 ? -9.974  31.889 7.363   1.00 23.12 ? 162 LYS B CE  1 
ATOM   5473 N NZ  . LYS B 1 162 ? -10.669 32.303 6.091   1.00 24.44 ? 162 LYS B NZ  1 
ATOM   5474 N N   . GLU B 1 163 ? -7.676  29.264 10.884  1.00 20.57 ? 163 GLU B N   1 
ATOM   5475 C CA  . GLU B 1 163 ? -8.063  27.884 11.152  1.00 26.98 ? 163 GLU B CA  1 
ATOM   5476 C C   . GLU B 1 163 ? -7.633  27.444 12.550  1.00 26.36 ? 163 GLU B C   1 
ATOM   5477 O O   . GLU B 1 163 ? -8.315  26.633 13.185  1.00 27.70 ? 163 GLU B O   1 
ATOM   5478 C CB  . GLU B 1 163 ? -7.464  26.957 10.092  1.00 26.66 ? 163 GLU B CB  1 
ATOM   5479 C CG  . GLU B 1 163 ? -7.967  27.249 8.686   1.00 27.28 ? 163 GLU B CG  1 
ATOM   5480 C CD  . GLU B 1 163 ? -7.317  26.388 7.617   1.00 39.13 ? 163 GLU B CD  1 
ATOM   5481 O OE1 . GLU B 1 163 ? -6.081  26.207 7.673   1.00 39.10 ? 163 GLU B OE1 1 
ATOM   5482 O OE2 . GLU B 1 163 ? -8.037  25.931 6.703   1.00 41.53 ? 163 GLU B OE2 1 
ATOM   5483 N N   . TYR B 1 164 ? -6.505  27.957 13.030  1.00 24.16 ? 164 TYR B N   1 
ATOM   5484 C CA  . TYR B 1 164 ? -6.097  27.712 14.406  1.00 23.44 ? 164 TYR B CA  1 
ATOM   5485 C C   . TYR B 1 164 ? -7.136  28.241 15.387  1.00 23.66 ? 164 TYR B C   1 
ATOM   5486 O O   . TYR B 1 164 ? -7.512  27.552 16.344  1.00 20.83 ? 164 TYR B O   1 
ATOM   5487 C CB  . TYR B 1 164 ? -4.741  28.360 14.660  1.00 29.84 ? 164 TYR B CB  1 
ATOM   5488 C CG  . TYR B 1 164 ? -4.206  28.180 16.057  1.00 33.28 ? 164 TYR B CG  1 
ATOM   5489 C CD1 . TYR B 1 164 ? -3.657  26.970 16.465  1.00 38.40 ? 164 TYR B CD1 1 
ATOM   5490 C CD2 . TYR B 1 164 ? -4.228  29.228 16.965  1.00 30.73 ? 164 TYR B CD2 1 
ATOM   5491 C CE1 . TYR B 1 164 ? -3.155  26.809 17.742  1.00 39.74 ? 164 TYR B CE1 1 
ATOM   5492 C CE2 . TYR B 1 164 ? -3.723  29.078 18.244  1.00 34.78 ? 164 TYR B CE2 1 
ATOM   5493 C CZ  . TYR B 1 164 ? -3.192  27.865 18.628  1.00 41.23 ? 164 TYR B CZ  1 
ATOM   5494 O OH  . TYR B 1 164 ? -2.689  27.708 19.898  1.00 47.71 ? 164 TYR B OH  1 
ATOM   5495 N N   . VAL B 1 165 ? -7.606  29.474 15.168  1.00 19.66 ? 165 VAL B N   1 
ATOM   5496 C CA  . VAL B 1 165 ? -8.648  30.040 16.022  1.00 21.42 ? 165 VAL B CA  1 
ATOM   5497 C C   . VAL B 1 165 ? -9.906  29.176 15.972  1.00 22.05 ? 165 VAL B C   1 
ATOM   5498 O O   . VAL B 1 165 ? -10.536 28.901 17.003  1.00 20.78 ? 165 VAL B O   1 
ATOM   5499 C CB  . VAL B 1 165 ? -8.957  31.495 15.619  1.00 19.59 ? 165 VAL B CB  1 
ATOM   5500 C CG1 . VAL B 1 165 ? -10.157 32.004 16.420  1.00 15.57 ? 165 VAL B CG1 1 
ATOM   5501 C CG2 . VAL B 1 165 ? -7.771  32.396 15.853  1.00 22.42 ? 165 VAL B CG2 1 
ATOM   5502 N N   . LEU B 1 166 ? -10.313 28.767 14.768  1.00 18.76 ? 166 LEU B N   1 
ATOM   5503 C CA  . LEU B 1 166 ? -11.491 27.915 14.642  1.00 22.95 ? 166 LEU B CA  1 
ATOM   5504 C C   . LEU B 1 166 ? -11.319 26.616 15.418  1.00 25.32 ? 166 LEU B C   1 
ATOM   5505 O O   . LEU B 1 166 ? -12.255 26.156 16.081  1.00 19.36 ? 166 LEU B O   1 
ATOM   5506 C CB  . LEU B 1 166 ? -11.777 27.611 13.167  1.00 22.58 ? 166 LEU B CB  1 
ATOM   5507 C CG  . LEU B 1 166 ? -12.415 28.745 12.367  1.00 22.60 ? 166 LEU B CG  1 
ATOM   5508 C CD1 . LEU B 1 166 ? -12.357 28.429 10.882  1.00 24.18 ? 166 LEU B CD1 1 
ATOM   5509 C CD2 . LEU B 1 166 ? -13.860 28.971 12.811  1.00 25.41 ? 166 LEU B CD2 1 
ATOM   5510 N N   . ASN B 1 167 ? -10.136 25.995 15.329  1.00 20.49 ? 167 ASN B N   1 
ATOM   5511 C CA  . ASN B 1 167 ? -9.922  24.738 16.039  1.00 23.87 ? 167 ASN B CA  1 
ATOM   5512 C C   . ASN B 1 167 ? -10.041 24.925 17.543  1.00 22.23 ? 167 ASN B C   1 
ATOM   5513 O O   . ASN B 1 167 ? -10.681 24.117 18.224  1.00 21.69 ? 167 ASN B O   1 
ATOM   5514 C CB  . ASN B 1 167 ? -8.563  24.149 15.683  1.00 23.27 ? 167 ASN B CB  1 
ATOM   5515 C CG  . ASN B 1 167 ? -8.578  23.455 14.336  1.00 34.93 ? 167 ASN B CG  1 
ATOM   5516 O OD1 . ASN B 1 167 ? -9.607  22.912 13.927  1.00 40.48 ? 167 ASN B OD1 1 
ATOM   5517 N ND2 . ASN B 1 167 ? -7.445  23.446 13.653  1.00 40.75 ? 167 ASN B ND2 1 
ATOM   5518 N N   . LYS B 1 168 ? -9.437  25.990 18.075  1.00 19.02 ? 168 LYS B N   1 
ATOM   5519 C CA  . LYS B 1 168 ? -9.564  26.298 19.499  1.00 18.42 ? 168 LYS B CA  1 
ATOM   5520 C C   . LYS B 1 168 ? -11.024 26.543 19.892  1.00 23.30 ? 168 LYS B C   1 
ATOM   5521 O O   . LYS B 1 168 ? -11.469 26.110 20.964  1.00 17.06 ? 168 LYS B O   1 
ATOM   5522 C CB  . LYS B 1 168 ? -8.720  27.524 19.845  1.00 22.60 ? 168 LYS B CB  1 
ATOM   5523 C CG  . LYS B 1 168 ? -7.217  27.315 19.754  1.00 27.66 ? 168 LYS B CG  1 
ATOM   5524 C CD  . LYS B 1 168 ? -6.793  26.092 20.540  1.00 34.91 ? 168 LYS B CD  1 
ATOM   5525 C CE  . LYS B 1 168 ? -5.331  25.769 20.292  1.00 47.83 ? 168 LYS B CE  1 
ATOM   5526 N NZ  . LYS B 1 168 ? -4.433  26.592 21.163  1.00 54.04 ? 168 LYS B NZ  1 
ATOM   5527 N N   . TYR B 1 169 ? -11.777 27.248 19.047  1.00 16.47 ? 169 TYR B N   1 
ATOM   5528 C CA  . TYR B 1 169 ? -13.180 27.514 19.356  1.00 16.16 ? 169 TYR B CA  1 
ATOM   5529 C C   . TYR B 1 169 ? -13.995 26.223 19.415  1.00 18.72 ? 169 TYR B C   1 
ATOM   5530 O O   . TYR B 1 169 ? -14.840 26.050 20.305  1.00 15.61 ? 169 TYR B O   1 
ATOM   5531 C CB  . TYR B 1 169 ? -13.785 28.463 18.323  1.00 14.79 ? 169 TYR B CB  1 
ATOM   5532 C CG  . TYR B 1 169 ? -13.430 29.927 18.532  1.00 16.21 ? 169 TYR B CG  1 
ATOM   5533 C CD1 . TYR B 1 169 ? -12.481 30.312 19.475  1.00 18.00 ? 169 TYR B CD1 1 
ATOM   5534 C CD2 . TYR B 1 169 ? -14.075 30.922 17.801  1.00 17.28 ? 169 TYR B CD2 1 
ATOM   5535 C CE1 . TYR B 1 169 ? -12.177 31.665 19.670  1.00 13.79 ? 169 TYR B CE1 1 
ATOM   5536 C CE2 . TYR B 1 169 ? -13.779 32.265 17.989  1.00 14.38 ? 169 TYR B CE2 1 
ATOM   5537 C CZ  . TYR B 1 169 ? -12.827 32.623 18.919  1.00 13.19 ? 169 TYR B CZ  1 
ATOM   5538 O OH  . TYR B 1 169 ? -12.544 33.961 19.099  1.00 13.85 ? 169 TYR B OH  1 
ATOM   5539 N N   . PHE B 1 170 ? -13.763 25.300 18.478  1.00 23.46 ? 170 PHE B N   1 
ATOM   5540 C CA  . PHE B 1 170 ? -14.495 24.041 18.532  1.00 22.18 ? 170 PHE B CA  1 
ATOM   5541 C C   . PHE B 1 170 ? -14.056 23.179 19.710  1.00 21.76 ? 170 PHE B C   1 
ATOM   5542 O O   . PHE B 1 170 ? -14.862 22.393 20.219  1.00 23.54 ? 170 PHE B O   1 
ATOM   5543 C CB  . PHE B 1 170 ? -14.373 23.290 17.205  1.00 21.08 ? 170 PHE B CB  1 
ATOM   5544 C CG  . PHE B 1 170 ? -15.382 23.743 16.182  1.00 28.06 ? 170 PHE B CG  1 
ATOM   5545 C CD1 . PHE B 1 170 ? -16.703 23.316 16.258  1.00 25.74 ? 170 PHE B CD1 1 
ATOM   5546 C CD2 . PHE B 1 170 ? -15.031 24.644 15.185  1.00 32.17 ? 170 PHE B CD2 1 
ATOM   5547 C CE1 . PHE B 1 170 ? -17.649 23.741 15.336  1.00 27.67 ? 170 PHE B CE1 1 
ATOM   5548 C CE2 . PHE B 1 170 ? -15.968 25.073 14.257  1.00 31.59 ? 170 PHE B CE2 1 
ATOM   5549 C CZ  . PHE B 1 170 ? -17.286 24.621 14.336  1.00 28.58 ? 170 PHE B CZ  1 
ATOM   5550 N N   . GLU B 1 171 ? -12.809 23.323 20.175  1.00 19.96 ? 171 GLU B N   1 
ATOM   5551 C CA  . GLU B 1 171 ? -12.432 22.676 21.432  1.00 19.37 ? 171 GLU B CA  1 
ATOM   5552 C C   . GLU B 1 171 ? -13.287 23.193 22.588  1.00 21.31 ? 171 GLU B C   1 
ATOM   5553 O O   . GLU B 1 171 ? -13.717 22.415 23.448  1.00 20.71 ? 171 GLU B O   1 
ATOM   5554 C CB  . GLU B 1 171 ? -10.952 22.902 21.742  1.00 23.19 ? 171 GLU B CB  1 
ATOM   5555 C CG  . GLU B 1 171 ? -9.982  22.274 20.774  1.00 34.49 ? 171 GLU B CG  1 
ATOM   5556 C CD  . GLU B 1 171 ? -8.536  22.585 21.136  1.00 47.46 ? 171 GLU B CD  1 
ATOM   5557 O OE1 . GLU B 1 171 ? -8.313  23.337 22.114  1.00 48.89 ? 171 GLU B OE1 1 
ATOM   5558 O OE2 . GLU B 1 171 ? -7.627  22.078 20.442  1.00 52.61 ? 171 GLU B OE2 1 
ATOM   5559 N N   . ILE B 1 172 ? -13.540 24.507 22.620  1.00 19.06 ? 172 ILE B N   1 
ATOM   5560 C CA  . ILE B 1 172 ? -14.366 25.097 23.676  1.00 16.09 ? 172 ILE B CA  1 
ATOM   5561 C C   . ILE B 1 172 ? -15.792 24.567 23.594  1.00 19.21 ? 172 ILE B C   1 
ATOM   5562 O O   . ILE B 1 172 ? -16.408 24.222 24.615  1.00 15.25 ? 172 ILE B O   1 
ATOM   5563 C CB  . ILE B 1 172 ? -14.331 26.638 23.591  1.00 15.48 ? 172 ILE B CB  1 
ATOM   5564 C CG1 . ILE B 1 172 ? -13.010 27.204 24.111  1.00 17.01 ? 172 ILE B CG1 1 
ATOM   5565 C CG2 . ILE B 1 172 ? -15.514 27.261 24.332  1.00 21.64 ? 172 ILE B CG2 1 
ATOM   5566 C CD1 . ILE B 1 172 ? -12.785 27.053 25.607  1.00 18.30 ? 172 ILE B CD1 1 
ATOM   5567 N N   . ILE B 1 173 ? -16.337 24.476 22.382  1.00 15.89 ? 173 ILE B N   1 
ATOM   5568 C CA  . ILE B 1 173 ? -17.703 23.979 22.236  1.00 17.81 ? 173 ILE B CA  1 
ATOM   5569 C C   . ILE B 1 173 ? -17.801 22.530 22.695  1.00 20.57 ? 173 ILE B C   1 
ATOM   5570 O O   . ILE B 1 173 ? -18.765 22.144 23.366  1.00 19.95 ? 173 ILE B O   1 
ATOM   5571 C CB  . ILE B 1 173 ? -18.179 24.142 20.787  1.00 20.53 ? 173 ILE B CB  1 
ATOM   5572 C CG1 . ILE B 1 173 ? -18.300 25.633 20.454  1.00 15.03 ? 173 ILE B CG1 1 
ATOM   5573 C CG2 . ILE B 1 173 ? -19.497 23.403 20.597  1.00 19.96 ? 173 ILE B CG2 1 
ATOM   5574 C CD1 . ILE B 1 173 ? -18.527 25.915 18.986  1.00 20.50 ? 173 ILE B CD1 1 
ATOM   5575 N N   . LYS B 1 174 ? -16.800 21.709 22.350  1.00 17.23 ? 174 LYS B N   1 
ATOM   5576 C CA  . LYS B 1 174 ? -16.804 20.305 22.760  1.00 18.39 ? 174 LYS B CA  1 
ATOM   5577 C C   . LYS B 1 174 ? -16.786 20.128 24.273  1.00 24.30 ? 174 LYS B C   1 
ATOM   5578 O O   . LYS B 1 174 ? -17.203 19.074 24.762  1.00 21.82 ? 174 LYS B O   1 
ATOM   5579 C CB  . LYS B 1 174 ? -15.609 19.581 22.140  1.00 20.73 ? 174 LYS B CB  1 
ATOM   5580 C CG  . LYS B 1 174 ? -15.676 19.429 20.630  1.00 22.90 ? 174 LYS B CG  1 
ATOM   5581 C CD  . LYS B 1 174 ? -14.378 18.815 20.106  1.00 29.79 ? 174 LYS B CD  1 
ATOM   5582 C CE  . LYS B 1 174 ? -14.336 18.808 18.585  1.00 46.55 ? 174 LYS B CE  1 
ATOM   5583 N NZ  . LYS B 1 174 ? -15.275 17.818 17.991  1.00 52.86 ? 174 LYS B NZ  1 
ATOM   5584 N N   . LYS B 1 175 ? -16.316 21.129 25.025  1.00 17.70 ? 175 LYS B N   1 
ATOM   5585 C CA  . LYS B 1 175 ? -16.249 21.073 26.481  1.00 17.74 ? 175 LYS B CA  1 
ATOM   5586 C C   . LYS B 1 175 ? -17.419 21.784 27.147  1.00 16.56 ? 175 LYS B C   1 
ATOM   5587 O O   . LYS B 1 175 ? -17.464 21.857 28.377  1.00 19.71 ? 175 LYS B O   1 
ATOM   5588 C CB  . LYS B 1 175 ? -14.938 21.703 26.976  1.00 21.39 ? 175 LYS B CB  1 
ATOM   5589 C CG  . LYS B 1 175 ? -13.662 21.030 26.463  1.00 37.43 ? 175 LYS B CG  1 
ATOM   5590 C CD  . LYS B 1 175 ? -12.431 21.637 27.111  1.00 42.63 ? 175 LYS B CD  1 
ATOM   5591 C CE  . LYS B 1 175 ? -12.221 23.076 26.661  1.00 46.17 ? 175 LYS B CE  1 
ATOM   5592 N NZ  . LYS B 1 175 ? -10.959 23.653 27.218  1.00 54.51 ? 175 LYS B NZ  1 
ATOM   5593 N N   . THR B 1 176 ? -18.356 22.321 26.367  1.00 16.92 ? 176 THR B N   1 
ATOM   5594 C CA  . THR B 1 176 ? -19.341 23.243 26.930  1.00 14.58 ? 176 THR B CA  1 
ATOM   5595 C C   . THR B 1 176 ? -20.377 22.520 27.786  1.00 16.63 ? 176 THR B C   1 
ATOM   5596 O O   . THR B 1 176 ? -20.681 22.955 28.902  1.00 20.87 ? 176 THR B O   1 
ATOM   5597 C CB  . THR B 1 176 ? -20.011 24.043 25.814  1.00 18.90 ? 176 THR B CB  1 
ATOM   5598 O OG1 . THR B 1 176 ? -19.047 24.948 25.254  1.00 17.80 ? 176 THR B OG1 1 
ATOM   5599 C CG2 . THR B 1 176 ? -21.158 24.864 26.374  1.00 20.81 ? 176 THR B CG2 1 
ATOM   5600 N N   . LEU B 1 177 ? -20.944 21.415 27.297  1.00 15.39 ? 177 LEU B N   1 
ATOM   5601 C CA  . LEU B 1 177 ? -21.907 20.736 28.161  1.00 15.61 ? 177 LEU B CA  1 
ATOM   5602 C C   . LEU B 1 177 ? -21.223 20.149 29.392  1.00 17.54 ? 177 LEU B C   1 
ATOM   5603 O O   . LEU B 1 177 ? -21.824 20.090 30.473  1.00 17.48 ? 177 LEU B O   1 
ATOM   5604 C CB  . LEU B 1 177 ? -22.650 19.646 27.381  1.00 18.72 ? 177 LEU B CB  1 
ATOM   5605 C CG  . LEU B 1 177 ? -23.590 20.213 26.322  1.00 25.52 ? 177 LEU B CG  1 
ATOM   5606 C CD1 . LEU B 1 177 ? -24.270 19.068 25.582  1.00 22.78 ? 177 LEU B CD1 1 
ATOM   5607 C CD2 . LEU B 1 177 ? -24.625 21.124 26.982  1.00 23.00 ? 177 LEU B CD2 1 
ATOM   5608 N N   . SER B 1 178 ? -19.959 19.752 29.256  1.00 17.23 ? 178 SER B N   1 
ATOM   5609 C CA  . SER B 1 178 ? -19.243 19.159 30.385  1.00 18.16 ? 178 SER B CA  1 
ATOM   5610 C C   . SER B 1 178 ? -19.001 20.155 31.506  1.00 17.87 ? 178 SER B C   1 
ATOM   5611 O O   . SER B 1 178 ? -18.994 19.765 32.681  1.00 19.18 ? 178 SER B O   1 
ATOM   5612 C CB  . SER B 1 178 ? -17.908 18.573 29.923  1.00 24.27 ? 178 SER B CB  1 
ATOM   5613 O OG  . SER B 1 178 ? -18.126 17.364 29.239  1.00 30.68 ? 178 SER B OG  1 
ATOM   5614 N N   . ILE B 1 179 ? -18.785 21.430 31.185  1.00 18.45 ? 179 ILE B N   1 
ATOM   5615 C CA  . ILE B 1 179 ? -18.553 22.367 32.278  1.00 18.10 ? 179 ILE B CA  1 
ATOM   5616 C C   . ILE B 1 179 ? -19.842 22.588 33.072  1.00 15.43 ? 179 ILE B C   1 
ATOM   5617 O O   . ILE B 1 179 ? -19.792 22.794 34.289  1.00 21.66 ? 179 ILE B O   1 
ATOM   5618 C CB  . ILE B 1 179 ? -17.932 23.687 31.762  1.00 19.48 ? 179 ILE B CB  1 
ATOM   5619 C CG1 . ILE B 1 179 ? -17.361 24.508 32.928  1.00 23.72 ? 179 ILE B CG1 1 
ATOM   5620 C CG2 . ILE B 1 179 ? -18.934 24.555 30.982  1.00 16.10 ? 179 ILE B CG2 1 
ATOM   5621 C CD1 . ILE B 1 179 ? -16.183 23.853 33.608  1.00 32.02 ? 179 ILE B CD1 1 
ATOM   5622 N N   . TYR B 1 180 ? -21.014 22.520 32.422  1.00 16.39 ? 180 TYR B N   1 
ATOM   5623 C CA  . TYR B 1 180 ? -22.267 22.599 33.178  1.00 14.53 ? 180 TYR B CA  1 
ATOM   5624 C C   . TYR B 1 180 ? -22.446 21.378 34.070  1.00 18.15 ? 180 TYR B C   1 
ATOM   5625 O O   . TYR B 1 180 ? -22.852 21.506 35.230  1.00 19.11 ? 180 TYR B O   1 
ATOM   5626 C CB  . TYR B 1 180 ? -23.474 22.758 32.246  1.00 16.03 ? 180 TYR B CB  1 
ATOM   5627 C CG  . TYR B 1 180 ? -23.536 24.135 31.648  1.00 14.37 ? 180 TYR B CG  1 
ATOM   5628 C CD1 . TYR B 1 180 ? -24.030 25.212 32.387  1.00 17.33 ? 180 TYR B CD1 1 
ATOM   5629 C CD2 . TYR B 1 180 ? -23.058 24.378 30.367  1.00 13.14 ? 180 TYR B CD2 1 
ATOM   5630 C CE1 . TYR B 1 180 ? -24.069 26.497 31.855  1.00 13.26 ? 180 TYR B CE1 1 
ATOM   5631 C CE2 . TYR B 1 180 ? -23.103 25.671 29.819  1.00 12.37 ? 180 TYR B CE2 1 
ATOM   5632 C CZ  . TYR B 1 180 ? -23.597 26.716 30.571  1.00 14.45 ? 180 TYR B CZ  1 
ATOM   5633 O OH  . TYR B 1 180 ? -23.619 27.994 30.061  1.00 12.82 ? 180 TYR B OH  1 
ATOM   5634 N N   . ARG B 1 181 ? -22.126 20.182 33.564  1.00 19.42 ? 181 ARG B N   1 
ATOM   5635 C CA  . ARG B 1 181 ? -22.147 19.018 34.446  1.00 18.56 ? 181 ARG B CA  1 
ATOM   5636 C C   . ARG B 1 181 ? -21.152 19.181 35.590  1.00 21.38 ? 181 ARG B C   1 
ATOM   5637 O O   . ARG B 1 181 ? -21.459 18.846 36.741  1.00 22.98 ? 181 ARG B O   1 
ATOM   5638 C CB  . ARG B 1 181 ? -21.847 17.734 33.670  1.00 18.87 ? 181 ARG B CB  1 
ATOM   5639 C CG  . ARG B 1 181 ? -22.881 17.361 32.624  1.00 19.21 ? 181 ARG B CG  1 
ATOM   5640 C CD  . ARG B 1 181 ? -22.653 15.906 32.149  1.00 20.59 ? 181 ARG B CD  1 
ATOM   5641 N NE  . ARG B 1 181 ? -23.409 15.655 30.932  1.00 31.44 ? 181 ARG B NE  1 
ATOM   5642 C CZ  . ARG B 1 181 ? -22.937 15.885 29.712  1.00 35.27 ? 181 ARG B CZ  1 
ATOM   5643 N NH1 . ARG B 1 181 ? -21.707 16.353 29.559  1.00 33.96 ? 181 ARG B NH1 1 
ATOM   5644 N NH2 . ARG B 1 181 ? -23.682 15.627 28.647  1.00 46.69 ? 181 ARG B NH2 1 
ATOM   5645 N N   . GLU B 1 182 ? -19.954 19.691 35.289  1.00 19.49 ? 182 GLU B N   1 
ATOM   5646 C CA  . GLU B 1 182 ? -18.911 19.817 36.306  1.00 24.13 ? 182 GLU B CA  1 
ATOM   5647 C C   . GLU B 1 182 ? -19.327 20.758 37.433  1.00 22.91 ? 182 GLU B C   1 
ATOM   5648 O O   . GLU B 1 182 ? -19.188 20.419 38.615  1.00 23.08 ? 182 GLU B O   1 
ATOM   5649 C CB  . GLU B 1 182 ? -17.605 20.296 35.672  1.00 24.24 ? 182 GLU B CB  1 
ATOM   5650 C CG  . GLU B 1 182 ? -16.516 20.584 36.689  1.00 30.33 ? 182 GLU B CG  1 
ATOM   5651 C CD  . GLU B 1 182 ? -15.172 20.940 36.068  1.00 37.48 ? 182 GLU B CD  1 
ATOM   5652 O OE1 . GLU B 1 182 ? -15.046 20.944 34.826  1.00 36.33 ? 182 GLU B OE1 1 
ATOM   5653 O OE2 . GLU B 1 182 ? -14.225 21.194 36.839  1.00 42.90 ? 182 GLU B OE2 1 
ATOM   5654 N N   . ILE B 1 183 ? -19.824 21.954 37.099  1.00 16.93 ? 183 ILE B N   1 
ATOM   5655 C CA  . ILE B 1 183 ? -20.134 22.875 38.188  1.00 17.57 ? 183 ILE B CA  1 
ATOM   5656 C C   . ILE B 1 183 ? -21.332 22.365 38.987  1.00 23.30 ? 183 ILE B C   1 
ATOM   5657 O O   . ILE B 1 183 ? -21.443 22.625 40.192  1.00 23.36 ? 183 ILE B O   1 
ATOM   5658 C CB  . ILE B 1 183 ? -20.323 24.324 37.679  1.00 20.75 ? 183 ILE B CB  1 
ATOM   5659 C CG1 . ILE B 1 183 ? -21.566 24.494 36.801  1.00 17.91 ? 183 ILE B CG1 1 
ATOM   5660 C CG2 . ILE B 1 183 ? -19.066 24.798 36.962  1.00 27.36 ? 183 ILE B CG2 1 
ATOM   5661 C CD1 . ILE B 1 183 ? -22.758 25.010 37.553  1.00 22.23 ? 183 ILE B CD1 1 
ATOM   5662 N N   . LYS B 1 184 ? -22.207 21.580 38.363  1.00 17.63 ? 184 LYS B N   1 
ATOM   5663 C CA  . LYS B 1 184 ? -23.312 21.004 39.115  1.00 16.99 ? 184 LYS B CA  1 
ATOM   5664 C C   . LYS B 1 184 ? -22.803 19.920 40.059  1.00 22.75 ? 184 LYS B C   1 
ATOM   5665 O O   . LYS B 1 184 ? -23.186 19.876 41.235  1.00 23.90 ? 184 LYS B O   1 
ATOM   5666 C CB  . LYS B 1 184 ? -24.363 20.445 38.161  1.00 19.83 ? 184 LYS B CB  1 
ATOM   5667 C CG  . LYS B 1 184 ? -25.517 19.743 38.853  1.00 34.64 ? 184 LYS B CG  1 
ATOM   5668 C CD  . LYS B 1 184 ? -26.544 19.225 37.855  1.00 39.45 ? 184 LYS B CD  1 
ATOM   5669 C CE  . LYS B 1 184 ? -27.652 18.482 38.587  1.00 43.65 ? 184 LYS B CE  1 
ATOM   5670 N NZ  . LYS B 1 184 ? -28.706 18.010 37.659  1.00 52.56 ? 184 LYS B NZ  1 
ATOM   5671 N N   . GLU B 1 185 ? -21.906 19.065 39.572  1.00 22.13 ? 185 GLU B N   1 
ATOM   5672 C CA  . GLU B 1 185 ? -21.392 17.990 40.419  1.00 24.26 ? 185 GLU B CA  1 
ATOM   5673 C C   . GLU B 1 185 ? -20.492 18.524 41.524  1.00 29.03 ? 185 GLU B C   1 
ATOM   5674 O O   . GLU B 1 185 ? -20.417 17.924 42.604  1.00 31.46 ? 185 GLU B O   1 
ATOM   5675 C CB  . GLU B 1 185 ? -20.662 16.953 39.566  1.00 30.28 ? 185 GLU B CB  1 
ATOM   5676 C CG  . GLU B 1 185 ? -21.592 16.288 38.581  1.00 32.72 ? 185 GLU B CG  1 
ATOM   5677 C CD  . GLU B 1 185 ? -22.784 15.673 39.284  1.00 46.64 ? 185 GLU B CD  1 
ATOM   5678 O OE1 . GLU B 1 185 ? -22.585 14.980 40.308  1.00 53.76 ? 185 GLU B OE1 1 
ATOM   5679 O OE2 . GLU B 1 185 ? -23.926 15.918 38.842  1.00 50.52 ? 185 GLU B OE2 1 
ATOM   5680 N N   . GLU B 1 186 ? -19.814 19.640 41.285  1.00 27.64 ? 186 GLU B N   1 
ATOM   5681 C CA  . GLU B 1 186 ? -18.994 20.257 42.316  1.00 26.20 ? 186 GLU B CA  1 
ATOM   5682 C C   . GLU B 1 186 ? -19.822 21.030 43.334  1.00 27.60 ? 186 GLU B C   1 
ATOM   5683 O O   . GLU B 1 186 ? -19.249 21.591 44.275  1.00 26.42 ? 186 GLU B O   1 
ATOM   5684 C CB  . GLU B 1 186 ? -17.950 21.173 41.669  1.00 26.13 ? 186 GLU B CB  1 
ATOM   5685 C CG  . GLU B 1 186 ? -16.794 20.411 41.039  1.00 30.48 ? 186 GLU B CG  1 
ATOM   5686 C CD  . GLU B 1 186 ? -15.792 21.313 40.346  1.00 49.75 ? 186 GLU B CD  1 
ATOM   5687 O OE1 . GLU B 1 186 ? -16.161 22.442 39.954  1.00 53.23 ? 186 GLU B OE1 1 
ATOM   5688 O OE2 . GLU B 1 186 ? -14.619 20.897 40.225  1.00 59.07 ? 186 GLU B OE2 1 
ATOM   5689 N N   . GLY B 1 187 ? -21.147 21.054 43.179  1.00 30.29 ? 187 GLY B N   1 
ATOM   5690 C CA  . GLY B 1 187 ? -22.012 21.825 44.055  1.00 26.32 ? 187 GLY B CA  1 
ATOM   5691 C C   . GLY B 1 187 ? -21.832 23.323 43.970  1.00 24.72 ? 187 GLY B C   1 
ATOM   5692 O O   . GLY B 1 187 ? -22.192 24.035 44.910  1.00 23.49 ? 187 GLY B O   1 
ATOM   5693 N N   . LYS B 1 188 ? -21.253 23.825 42.880  1.00 19.74 ? 188 LYS B N   1 
ATOM   5694 C CA  . LYS B 1 188 ? -21.013 25.251 42.709  1.00 19.25 ? 188 LYS B CA  1 
ATOM   5695 C C   . LYS B 1 188 ? -22.209 25.977 42.105  1.00 18.11 ? 188 LYS B C   1 
ATOM   5696 O O   . LYS B 1 188 ? -22.231 27.215 42.097  1.00 15.03 ? 188 LYS B O   1 
ATOM   5697 C CB  . LYS B 1 188 ? -19.773 25.467 41.834  1.00 21.87 ? 188 LYS B CB  1 
ATOM   5698 C CG  . LYS B 1 188 ? -18.448 25.008 42.477  1.00 25.77 ? 188 LYS B CG  1 
ATOM   5699 C CD  . LYS B 1 188 ? -17.297 25.066 41.460  1.00 29.44 ? 188 LYS B CD  1 
ATOM   5700 C CE  . LYS B 1 188 ? -15.925 24.831 42.112  1.00 35.59 ? 188 LYS B CE  1 
ATOM   5701 N NZ  . LYS B 1 188 ? -15.442 26.062 42.807  1.00 36.24 ? 188 LYS B NZ  1 
ATOM   5702 N N   . GLY B 1 189 ? -23.197 25.243 41.611  1.00 17.48 ? 189 GLY B N   1 
ATOM   5703 C CA  . GLY B 1 189 ? -24.382 25.870 41.054  1.00 18.49 ? 189 GLY B CA  1 
ATOM   5704 C C   . GLY B 1 189 ? -25.366 24.800 40.633  1.00 16.88 ? 189 GLY B C   1 
ATOM   5705 O O   . GLY B 1 189 ? -25.004 23.636 40.433  1.00 24.00 ? 189 GLY B O   1 
ATOM   5706 N N   . SER B 1 190 ? -26.625 25.213 40.521  1.00 17.36 ? 190 SER B N   1 
ATOM   5707 C CA  . SER B 1 190 ? -27.651 24.339 39.969  1.00 16.71 ? 190 SER B CA  1 
ATOM   5708 C C   . SER B 1 190 ? -27.795 24.629 38.482  1.00 20.02 ? 190 SER B C   1 
ATOM   5709 O O   . SER B 1 190 ? -27.565 25.752 38.036  1.00 17.17 ? 190 SER B O   1 
ATOM   5710 C CB  . SER B 1 190 ? -28.993 24.553 40.672  1.00 17.58 ? 190 SER B CB  1 
ATOM   5711 O OG  . SER B 1 190 ? -28.901 24.291 42.063  1.00 22.85 ? 190 SER B OG  1 
ATOM   5712 N N   . VAL B 1 191 ? -28.180 23.610 37.716  1.00 16.80 ? 191 VAL B N   1 
ATOM   5713 C CA  . VAL B 1 191 ? -28.532 23.773 36.308  1.00 15.57 ? 191 VAL B CA  1 
ATOM   5714 C C   . VAL B 1 191 ? -30.003 23.411 36.135  1.00 16.91 ? 191 VAL B C   1 
ATOM   5715 O O   . VAL B 1 191 ? -30.442 22.344 36.582  1.00 19.09 ? 191 VAL B O   1 
ATOM   5716 C CB  . VAL B 1 191 ? -27.649 22.906 35.392  1.00 22.20 ? 191 VAL B CB  1 
ATOM   5717 C CG1 . VAL B 1 191 ? -28.021 23.144 33.920  1.00 20.46 ? 191 VAL B CG1 1 
ATOM   5718 C CG2 . VAL B 1 191 ? -26.167 23.194 35.647  1.00 22.09 ? 191 VAL B CG2 1 
ATOM   5719 N N   . SER B 1 192 ? -30.762 24.294 35.497  1.00 12.24 ? 192 SER B N   1 
ATOM   5720 C CA  . SER B 1 192 ? -32.175 24.090 35.226  1.00 14.96 ? 192 SER B CA  1 
ATOM   5721 C C   . SER B 1 192 ? -32.409 23.982 33.721  1.00 13.85 ? 192 SER B C   1 
ATOM   5722 O O   . SER B 1 192 ? -31.515 24.205 32.910  1.00 11.82 ? 192 SER B O   1 
ATOM   5723 C CB  . SER B 1 192 ? -33.001 25.254 35.785  1.00 13.57 ? 192 SER B CB  1 
ATOM   5724 O OG  . SER B 1 192 ? -32.705 26.464 35.071  1.00 13.87 ? 192 SER B OG  1 
ATOM   5725 N N   . THR B 1 193 ? -33.638 23.662 33.348  1.00 12.72 ? 193 THR B N   1 
ATOM   5726 C CA  . THR B 1 193 ? -34.029 23.761 31.946  1.00 14.66 ? 193 THR B CA  1 
ATOM   5727 C C   . THR B 1 193 ? -35.383 24.458 31.851  1.00 17.10 ? 193 THR B C   1 
ATOM   5728 O O   . THR B 1 193 ? -35.993 24.822 32.863  1.00 15.28 ? 193 THR B O   1 
ATOM   5729 C CB  . THR B 1 193 ? -34.043 22.386 31.260  1.00 19.13 ? 193 THR B CB  1 
ATOM   5730 O OG1 . THR B 1 193 ? -34.073 22.576 29.844  1.00 18.55 ? 193 THR B OG1 1 
ATOM   5731 C CG2 . THR B 1 193 ? -35.259 21.550 31.670  1.00 14.21 ? 193 THR B CG2 1 
ATOM   5732 N N   . SER B 1 194 ? -35.838 24.652 30.617  1.00 16.23 ? 194 SER B N   1 
ATOM   5733 C CA  . SER B 1 194 ? -37.122 25.235 30.267  1.00 15.98 ? 194 SER B CA  1 
ATOM   5734 C C   . SER B 1 194 ? -37.892 24.252 29.399  1.00 12.68 ? 194 SER B C   1 
ATOM   5735 O O   . SER B 1 194 ? -37.290 23.381 28.767  1.00 13.07 ? 194 SER B O   1 
ATOM   5736 C CB  . SER B 1 194 ? -36.958 26.546 29.485  1.00 10.85 ? 194 SER B CB  1 
ATOM   5737 O OG  . SER B 1 194 ? -36.412 27.573 30.301  1.00 11.20 ? 194 SER B OG  1 
ATOM   5738 N N   . PRO B 1 195 ? -39.216 24.385 29.318  1.00 13.50 ? 195 PRO B N   1 
ATOM   5739 C CA  . PRO B 1 195 ? -39.980 23.665 28.277  1.00 13.51 ? 195 PRO B CA  1 
ATOM   5740 C C   . PRO B 1 195 ? -39.276 23.773 26.925  1.00 17.00 ? 195 PRO B C   1 
ATOM   5741 O O   . PRO B 1 195 ? -38.765 24.834 26.568  1.00 16.25 ? 195 PRO B O   1 
ATOM   5742 C CB  . PRO B 1 195 ? -41.333 24.387 28.272  1.00 20.60 ? 195 PRO B CB  1 
ATOM   5743 C CG  . PRO B 1 195 ? -41.464 24.932 29.685  1.00 25.85 ? 195 PRO B CG  1 
ATOM   5744 C CD  . PRO B 1 195 ? -40.069 25.259 30.149  1.00 15.18 ? 195 PRO B CD  1 
ATOM   5745 N N   . TYR B 1 196 ? -39.353 22.683 26.141  1.00 13.78 ? 196 TYR B N   1 
ATOM   5746 C CA  . TYR B 1 196 ? -38.281 22.283 25.214  1.00 14.79 ? 196 TYR B CA  1 
ATOM   5747 C C   . TYR B 1 196 ? -37.879 23.394 24.243  1.00 18.98 ? 196 TYR B C   1 
ATOM   5748 O O   . TYR B 1 196 ? -36.693 23.753 24.163  1.00 12.75 ? 196 TYR B O   1 
ATOM   5749 C CB  . TYR B 1 196 ? -38.709 20.999 24.478  1.00 15.00 ? 196 TYR B CB  1 
ATOM   5750 C CG  . TYR B 1 196 ? -37.564 20.225 23.839  1.00 15.43 ? 196 TYR B CG  1 
ATOM   5751 C CD1 . TYR B 1 196 ? -36.802 20.739 22.779  1.00 16.41 ? 196 TYR B CD1 1 
ATOM   5752 C CD2 . TYR B 1 196 ? -37.132 19.044 24.430  1.00 17.10 ? 196 TYR B CD2 1 
ATOM   5753 C CE1 . TYR B 1 196 ? -35.710 19.997 22.272  1.00 15.59 ? 196 TYR B CE1 1 
ATOM   5754 C CE2 . TYR B 1 196 ? -36.050 18.337 23.959  1.00 18.55 ? 196 TYR B CE2 1 
ATOM   5755 C CZ  . TYR B 1 196 ? -35.342 18.800 22.877  1.00 21.23 ? 196 TYR B CZ  1 
ATOM   5756 O OH  . TYR B 1 196 ? -34.266 18.061 22.420  1.00 18.98 ? 196 TYR B OH  1 
ATOM   5757 N N   . TYR B 1 197 ? -38.834 23.964 23.499  1.00 14.05 ? 197 TYR B N   1 
ATOM   5758 C CA  . TYR B 1 197 ? -38.507 24.983 22.495  1.00 12.80 ? 197 TYR B CA  1 
ATOM   5759 C C   . TYR B 1 197 ? -38.800 26.411 22.959  1.00 14.12 ? 197 TYR B C   1 
ATOM   5760 O O   . TYR B 1 197 ? -38.973 27.312 22.127  1.00 14.90 ? 197 TYR B O   1 
ATOM   5761 C CB  . TYR B 1 197 ? -39.230 24.670 21.176  1.00 13.65 ? 197 TYR B CB  1 
ATOM   5762 C CG  . TYR B 1 197 ? -38.699 23.394 20.576  1.00 15.42 ? 197 TYR B CG  1 
ATOM   5763 C CD1 . TYR B 1 197 ? -37.436 23.362 19.981  1.00 19.92 ? 197 TYR B CD1 1 
ATOM   5764 C CD2 . TYR B 1 197 ? -39.416 22.204 20.653  1.00 18.06 ? 197 TYR B CD2 1 
ATOM   5765 C CE1 . TYR B 1 197 ? -36.922 22.186 19.457  1.00 15.32 ? 197 TYR B CE1 1 
ATOM   5766 C CE2 . TYR B 1 197 ? -38.903 21.027 20.133  1.00 20.11 ? 197 TYR B CE2 1 
ATOM   5767 C CZ  . TYR B 1 197 ? -37.652 21.025 19.543  1.00 21.93 ? 197 TYR B CZ  1 
ATOM   5768 O OH  . TYR B 1 197 ? -37.137 19.852 19.026  1.00 23.54 ? 197 TYR B OH  1 
ATOM   5769 N N   . HIS B 1 198 ? -38.802 26.652 24.271  1.00 14.76 ? 198 HIS B N   1 
ATOM   5770 C CA  . HIS B 1 198 ? -38.973 27.993 24.836  1.00 11.04 ? 198 HIS B CA  1 
ATOM   5771 C C   . HIS B 1 198 ? -40.282 28.635 24.368  1.00 15.02 ? 198 HIS B C   1 
ATOM   5772 O O   . HIS B 1 198 ? -40.256 29.776 23.895  1.00 15.58 ? 198 HIS B O   1 
ATOM   5773 C CB  . HIS B 1 198 ? -37.743 28.853 24.464  1.00 10.74 ? 198 HIS B CB  1 
ATOM   5774 C CG  . HIS B 1 198 ? -37.541 30.098 25.281  1.00 9.79  ? 198 HIS B CG  1 
ATOM   5775 N ND1 . HIS B 1 198 ? -37.999 31.336 24.875  1.00 10.72 ? 198 HIS B ND1 1 
ATOM   5776 C CD2 . HIS B 1 198 ? -36.842 30.319 26.425  1.00 11.51 ? 198 HIS B CD2 1 
ATOM   5777 C CE1 . HIS B 1 198 ? -37.638 32.252 25.760  1.00 12.52 ? 198 HIS B CE1 1 
ATOM   5778 N NE2 . HIS B 1 198 ? -36.930 31.661 26.706  1.00 11.14 ? 198 HIS B NE2 1 
ATOM   5779 N N   . PRO B 1 199 ? -41.434 27.959 24.471  1.00 13.87 ? 199 PRO B N   1 
ATOM   5780 C CA  . PRO B 1 199 ? -42.707 28.584 24.087  1.00 14.53 ? 199 PRO B CA  1 
ATOM   5781 C C   . PRO B 1 199 ? -43.287 29.421 25.229  1.00 18.12 ? 199 PRO B C   1 
ATOM   5782 O O   . PRO B 1 199 ? -42.816 29.376 26.366  1.00 16.68 ? 199 PRO B O   1 
ATOM   5783 C CB  . PRO B 1 199 ? -43.601 27.377 23.827  1.00 14.84 ? 199 PRO B CB  1 
ATOM   5784 C CG  . PRO B 1 199 ? -43.173 26.431 24.943  1.00 16.91 ? 199 PRO B CG  1 
ATOM   5785 C CD  . PRO B 1 199 ? -41.660 26.622 25.059  1.00 18.39 ? 199 PRO B CD  1 
ATOM   5786 N N   . LEU B 1 200 ? -44.373 30.140 24.918  1.00 17.88 ? 200 LEU B N   1 
ATOM   5787 C CA  . LEU B 1 200 ? -45.181 30.842 25.925  1.00 17.29 ? 200 LEU B CA  1 
ATOM   5788 C C   . LEU B 1 200 ? -46.262 29.891 26.432  1.00 15.95 ? 200 LEU B C   1 
ATOM   5789 O O   . LEU B 1 200 ? -47.361 29.810 25.880  1.00 19.55 ? 200 LEU B O   1 
ATOM   5790 C CB  . LEU B 1 200 ? -45.779 32.116 25.340  1.00 20.50 ? 200 LEU B CB  1 
ATOM   5791 C CG  . LEU B 1 200 ? -44.771 33.219 24.996  1.00 19.75 ? 200 LEU B CG  1 
ATOM   5792 C CD1 . LEU B 1 200 ? -45.417 34.243 24.067  1.00 19.52 ? 200 LEU B CD1 1 
ATOM   5793 C CD2 . LEU B 1 200 ? -44.207 33.898 26.257  1.00 18.32 ? 200 LEU B CD2 1 
ATOM   5794 N N   . ILE B 1 201 ? -45.934 29.162 27.499  1.00 17.71 ? 201 ILE B N   1 
ATOM   5795 C CA  . ILE B 1 201 ? -46.845 28.137 28.018  1.00 17.94 ? 201 ILE B CA  1 
ATOM   5796 C C   . ILE B 1 201 ? -48.231 28.697 28.342  1.00 16.34 ? 201 ILE B C   1 
ATOM   5797 O O   . ILE B 1 201 ? -49.230 28.055 27.978  1.00 15.55 ? 201 ILE B O   1 
ATOM   5798 C CB  . ILE B 1 201 ? -46.201 27.426 29.220  1.00 15.50 ? 201 ILE B CB  1 
ATOM   5799 C CG1 . ILE B 1 201 ? -44.943 26.654 28.784  1.00 16.02 ? 201 ILE B CG1 1 
ATOM   5800 C CG2 . ILE B 1 201 ? -47.193 26.468 29.861  1.00 14.87 ? 201 ILE B CG2 1 
ATOM   5801 C CD1 . ILE B 1 201 ? -45.231 25.452 27.914  1.00 16.51 ? 201 ILE B CD1 1 
ATOM   5802 N N   . PRO B 1 202 ? -48.372 29.855 29.009  1.00 15.16 ? 202 PRO B N   1 
ATOM   5803 C CA  . PRO B 1 202 ? -49.735 30.343 29.316  1.00 15.06 ? 202 PRO B CA  1 
ATOM   5804 C C   . PRO B 1 202 ? -50.610 30.535 28.091  1.00 16.62 ? 202 PRO B C   1 
ATOM   5805 O O   . PRO B 1 202 ? -51.829 30.340 28.181  1.00 16.89 ? 202 PRO B O   1 
ATOM   5806 C CB  . PRO B 1 202 ? -49.485 31.676 30.041  1.00 16.13 ? 202 PRO B CB  1 
ATOM   5807 C CG  . PRO B 1 202 ? -48.125 31.503 30.681  1.00 17.67 ? 202 PRO B CG  1 
ATOM   5808 C CD  . PRO B 1 202 ? -47.339 30.698 29.650  1.00 13.47 ? 202 PRO B CD  1 
ATOM   5809 N N   . ILE B 1 203 ? -50.039 30.926 26.950  1.00 17.20 ? 203 ILE B N   1 
ATOM   5810 C CA  . ILE B 1 203 ? -50.858 31.122 25.760  1.00 16.05 ? 203 ILE B CA  1 
ATOM   5811 C C   . ILE B 1 203 ? -51.265 29.780 25.155  1.00 19.11 ? 203 ILE B C   1 
ATOM   5812 O O   . ILE B 1 203 ? -52.428 29.589 24.771  1.00 20.23 ? 203 ILE B O   1 
ATOM   5813 C CB  . ILE B 1 203 ? -50.126 32.013 24.742  1.00 21.24 ? 203 ILE B CB  1 
ATOM   5814 C CG1 . ILE B 1 203 ? -49.963 33.426 25.304  1.00 19.91 ? 203 ILE B CG1 1 
ATOM   5815 C CG2 . ILE B 1 203 ? -50.897 32.059 23.400  1.00 21.29 ? 203 ILE B CG2 1 
ATOM   5816 C CD1 . ILE B 1 203 ? -49.318 34.363 24.333  1.00 18.61 ? 203 ILE B CD1 1 
ATOM   5817 N N   . LEU B 1 204 ? -50.327 28.827 25.076  1.00 19.31 ? 204 LEU B N   1 
ATOM   5818 C CA  . LEU B 1 204 ? -50.670 27.479 24.626  1.00 17.15 ? 204 LEU B CA  1 
ATOM   5819 C C   . LEU B 1 204 ? -51.788 26.868 25.467  1.00 18.01 ? 204 LEU B C   1 
ATOM   5820 O O   . LEU B 1 204 ? -52.669 26.177 24.939  1.00 19.24 ? 204 LEU B O   1 
ATOM   5821 C CB  . LEU B 1 204 ? -49.447 26.576 24.681  1.00 17.34 ? 204 LEU B CB  1 
ATOM   5822 C CG  . LEU B 1 204 ? -48.265 26.974 23.796  1.00 22.82 ? 204 LEU B CG  1 
ATOM   5823 C CD1 . LEU B 1 204 ? -47.209 25.886 23.888  1.00 19.58 ? 204 LEU B CD1 1 
ATOM   5824 C CD2 . LEU B 1 204 ? -48.721 27.188 22.356  1.00 24.40 ? 204 LEU B CD2 1 
ATOM   5825 N N   . LEU B 1 205 ? -51.749 27.083 26.783  1.00 18.33 ? 205 LEU B N   1 
ATOM   5826 C CA  . LEU B 1 205 ? -52.763 26.493 27.656  1.00 20.17 ? 205 LEU B CA  1 
ATOM   5827 C C   . LEU B 1 205 ? -54.102 27.206 27.523  1.00 19.33 ? 205 LEU B C   1 
ATOM   5828 O O   . LEU B 1 205 ? -55.158 26.564 27.560  1.00 20.42 ? 205 LEU B O   1 
ATOM   5829 C CB  . LEU B 1 205 ? -52.293 26.523 29.118  1.00 19.26 ? 205 LEU B CB  1 
ATOM   5830 C CG  . LEU B 1 205 ? -51.165 25.557 29.502  1.00 22.08 ? 205 LEU B CG  1 
ATOM   5831 C CD1 . LEU B 1 205 ? -50.692 25.813 30.908  1.00 17.13 ? 205 LEU B CD1 1 
ATOM   5832 C CD2 . LEU B 1 205 ? -51.620 24.106 29.371  1.00 20.55 ? 205 LEU B CD2 1 
ATOM   5833 N N   . ASN B 1 206 ? -54.084 28.529 27.430  1.00 19.28 ? 206 ASN B N   1 
ATOM   5834 C CA  . ASN B 1 206 ? -55.316 29.309 27.413  1.00 19.73 ? 206 ASN B CA  1 
ATOM   5835 C C   . ASN B 1 206 ? -55.036 30.682 26.826  1.00 19.27 ? 206 ASN B C   1 
ATOM   5836 O O   . ASN B 1 206 ? -54.626 31.591 27.558  1.00 19.95 ? 206 ASN B O   1 
ATOM   5837 C CB  . ASN B 1 206 ? -55.904 29.454 28.821  1.00 23.52 ? 206 ASN B CB  1 
ATOM   5838 C CG  . ASN B 1 206 ? -57.298 30.062 28.806  1.00 34.30 ? 206 ASN B CG  1 
ATOM   5839 O OD1 . ASN B 1 206 ? -57.784 30.514 27.763  1.00 27.89 ? 206 ASN B OD1 1 
ATOM   5840 N ND2 . ASN B 1 206 ? -57.954 30.062 29.958  1.00 42.87 ? 206 ASN B ND2 1 
ATOM   5841 N N   . PRO B 1 207 ? -55.252 30.883 25.526  1.00 21.88 ? 207 PRO B N   1 
ATOM   5842 C CA  . PRO B 1 207 ? -54.957 32.197 24.936  1.00 26.74 ? 207 PRO B CA  1 
ATOM   5843 C C   . PRO B 1 207 ? -55.707 33.342 25.593  1.00 19.72 ? 207 PRO B C   1 
ATOM   5844 O O   . PRO B 1 207 ? -55.227 34.478 25.548  1.00 22.35 ? 207 PRO B O   1 
ATOM   5845 C CB  . PRO B 1 207 ? -55.369 32.020 23.467  1.00 28.12 ? 207 PRO B CB  1 
ATOM   5846 C CG  . PRO B 1 207 ? -55.272 30.549 23.234  1.00 29.61 ? 207 PRO B CG  1 
ATOM   5847 C CD  . PRO B 1 207 ? -55.736 29.924 24.519  1.00 25.49 ? 207 PRO B CD  1 
ATOM   5848 N N   . ASN B 1 208 ? -56.850 33.083 26.230  1.00 21.29 ? 208 ASN B N   1 
ATOM   5849 C CA  . ASN B 1 208 ? -57.590 34.158 26.880  1.00 26.30 ? 208 ASN B CA  1 
ATOM   5850 C C   . ASN B 1 208 ? -56.829 34.793 28.039  1.00 26.53 ? 208 ASN B C   1 
ATOM   5851 O O   . ASN B 1 208 ? -57.237 35.864 28.502  1.00 25.40 ? 208 ASN B O   1 
ATOM   5852 C CB  . ASN B 1 208 ? -58.937 33.635 27.370  1.00 27.17 ? 208 ASN B CB  1 
ATOM   5853 C CG  . ASN B 1 208 ? -59.851 33.247 26.225  1.00 36.71 ? 208 ASN B CG  1 
ATOM   5854 O OD1 . ASN B 1 208 ? -59.956 33.965 25.233  1.00 33.51 ? 208 ASN B OD1 1 
ATOM   5855 N ND2 . ASN B 1 208 ? -60.497 32.095 26.347  1.00 46.45 ? 208 ASN B ND2 1 
ATOM   5856 N N   . CYS B 1 209 ? -55.728 34.189 28.504  1.00 26.63 ? 209 CYS B N   1 
ATOM   5857 C CA  . CYS B 1 209 ? -54.983 34.801 29.598  1.00 24.86 ? 209 CYS B CA  1 
ATOM   5858 C C   . CYS B 1 209 ? -54.405 36.156 29.208  1.00 26.10 ? 209 CYS B C   1 
ATOM   5859 O O   . CYS B 1 209 ? -54.012 36.920 30.099  1.00 23.08 ? 209 CYS B O   1 
ATOM   5860 C CB  . CYS B 1 209 ? -53.859 33.878 30.092  1.00 20.51 ? 209 CYS B CB  1 
ATOM   5861 S SG  . CYS B 1 209 ? -52.487 33.672 28.959  1.00 25.54 ? 209 CYS B SG  1 
ATOM   5862 N N   . VAL B 1 210 ? -54.364 36.482 27.907  1.00 21.78 ? 210 VAL B N   1 
ATOM   5863 C CA  . VAL B 1 210 ? -53.828 37.776 27.484  1.00 19.85 ? 210 VAL B CA  1 
ATOM   5864 C C   . VAL B 1 210 ? -54.713 38.909 27.988  1.00 22.41 ? 210 VAL B C   1 
ATOM   5865 O O   . VAL B 1 210 ? -54.244 40.036 28.190  1.00 20.33 ? 210 VAL B O   1 
ATOM   5866 C CB  . VAL B 1 210 ? -53.672 37.840 25.947  1.00 23.06 ? 210 VAL B CB  1 
ATOM   5867 C CG1 . VAL B 1 210 ? -52.694 36.763 25.444  1.00 17.12 ? 210 VAL B CG1 1 
ATOM   5868 C CG2 . VAL B 1 210 ? -55.033 37.716 25.249  1.00 23.01 ? 210 VAL B CG2 1 
ATOM   5869 N N   . TYR B 1 211 ? -55.995 38.634 28.210  1.00 22.24 ? 211 TYR B N   1 
ATOM   5870 C CA  . TYR B 1 211 ? -56.911 39.692 28.602  1.00 26.53 ? 211 TYR B CA  1 
ATOM   5871 C C   . TYR B 1 211 ? -56.752 40.092 30.062  1.00 25.60 ? 211 TYR B C   1 
ATOM   5872 O O   . TYR B 1 211 ? -57.240 41.157 30.450  1.00 30.44 ? 211 TYR B O   1 
ATOM   5873 C CB  . TYR B 1 211 ? -58.357 39.266 28.346  1.00 22.28 ? 211 TYR B CB  1 
ATOM   5874 C CG  . TYR B 1 211 ? -58.652 38.893 26.906  1.00 31.06 ? 211 TYR B CG  1 
ATOM   5875 C CD1 . TYR B 1 211 ? -58.541 39.834 25.887  1.00 37.67 ? 211 TYR B CD1 1 
ATOM   5876 C CD2 . TYR B 1 211 ? -59.084 37.616 26.574  1.00 30.86 ? 211 TYR B CD2 1 
ATOM   5877 C CE1 . TYR B 1 211 ? -58.827 39.507 24.571  1.00 32.60 ? 211 TYR B CE1 1 
ATOM   5878 C CE2 . TYR B 1 211 ? -59.375 37.275 25.255  1.00 30.08 ? 211 TYR B CE2 1 
ATOM   5879 C CZ  . TYR B 1 211 ? -59.241 38.227 24.258  1.00 31.90 ? 211 TYR B CZ  1 
ATOM   5880 O OH  . TYR B 1 211 ? -59.528 37.897 22.944  1.00 32.44 ? 211 TYR B OH  1 
ATOM   5881 N N   . GLU B 1 212 ? -56.085 39.269 30.875  1.00 23.35 ? 212 GLU B N   1 
ATOM   5882 C CA  . GLU B 1 212 ? -55.929 39.613 32.285  1.00 25.24 ? 212 GLU B CA  1 
ATOM   5883 C C   . GLU B 1 212 ? -55.146 40.911 32.476  1.00 26.52 ? 212 GLU B C   1 
ATOM   5884 O O   . GLU B 1 212 ? -55.432 41.666 33.411  1.00 29.17 ? 212 GLU B O   1 
ATOM   5885 C CB  . GLU B 1 212 ? -55.269 38.454 33.043  1.00 22.66 ? 212 GLU B CB  1 
ATOM   5886 C CG  . GLU B 1 212 ? -56.068 37.154 32.949  1.00 26.04 ? 212 GLU B CG  1 
ATOM   5887 C CD  . GLU B 1 212 ? -55.402 35.990 33.649  1.00 34.52 ? 212 GLU B CD  1 
ATOM   5888 O OE1 . GLU B 1 212 ? -54.517 36.224 34.493  1.00 34.94 ? 212 GLU B OE1 1 
ATOM   5889 O OE2 . GLU B 1 212 ? -55.768 34.835 33.350  1.00 41.03 ? 212 GLU B OE2 1 
ATOM   5890 N N   . THR B 1 213 ? -54.173 41.202 31.607  1.00 29.17 ? 213 THR B N   1 
ATOM   5891 C CA  . THR B 1 213 ? -53.411 42.447 31.701  1.00 32.90 ? 213 THR B CA  1 
ATOM   5892 C C   . THR B 1 213 ? -53.647 43.412 30.545  1.00 32.50 ? 213 THR B C   1 
ATOM   5893 O O   . THR B 1 213 ? -53.469 44.620 30.725  1.00 40.83 ? 213 THR B O   1 
ATOM   5894 C CB  . THR B 1 213 ? -51.907 42.154 31.804  1.00 32.19 ? 213 THR B CB  1 
ATOM   5895 O OG1 . THR B 1 213 ? -51.493 41.373 30.681  1.00 41.44 ? 213 THR B OG1 1 
ATOM   5896 C CG2 . THR B 1 213 ? -51.602 41.401 33.088  1.00 31.88 ? 213 THR B CG2 1 
ATOM   5897 N N   . THR B 1 214 ? -54.038 42.925 29.368  1.00 32.43 ? 214 THR B N   1 
ATOM   5898 C CA  . THR B 1 214 ? -54.363 43.778 28.222  1.00 28.92 ? 214 THR B CA  1 
ATOM   5899 C C   . THR B 1 214 ? -55.744 43.378 27.727  1.00 33.64 ? 214 THR B C   1 
ATOM   5900 O O   . THR B 1 214 ? -55.885 42.678 26.715  1.00 34.24 ? 214 THR B O   1 
ATOM   5901 C CB  . THR B 1 214 ? -53.314 43.671 27.108  1.00 28.60 ? 214 THR B CB  1 
ATOM   5902 O OG1 . THR B 1 214 ? -53.230 42.316 26.642  1.00 29.10 ? 214 THR B OG1 1 
ATOM   5903 C CG2 . THR B 1 214 ? -51.935 44.128 27.597  1.00 24.71 ? 214 THR B CG2 1 
ATOM   5904 N N   . PRO B 1 215 ? -56.796 43.817 28.420  1.00 38.69 ? 215 PRO B N   1 
ATOM   5905 C CA  . PRO B 1 215 ? -58.149 43.351 28.078  1.00 36.71 ? 215 PRO B CA  1 
ATOM   5906 C C   . PRO B 1 215 ? -58.645 43.798 26.708  1.00 41.98 ? 215 PRO B C   1 
ATOM   5907 O O   . PRO B 1 215 ? -59.584 43.188 26.182  1.00 39.58 ? 215 PRO B O   1 
ATOM   5908 C CB  . PRO B 1 215 ? -59.013 43.937 29.206  1.00 35.73 ? 215 PRO B CB  1 
ATOM   5909 C CG  . PRO B 1 215 ? -58.239 45.102 29.725  1.00 35.64 ? 215 PRO B CG  1 
ATOM   5910 C CD  . PRO B 1 215 ? -56.789 44.711 29.590  1.00 37.82 ? 215 PRO B CD  1 
ATOM   5911 N N   . ASN B 1 216 ? -58.058 44.831 26.111  1.00 43.92 ? 216 ASN B N   1 
ATOM   5912 C CA  . ASN B 1 216 ? -58.535 45.341 24.832  1.00 49.62 ? 216 ASN B CA  1 
ATOM   5913 C C   . ASN B 1 216 ? -57.775 44.775 23.639  1.00 44.61 ? 216 ASN B C   1 
ATOM   5914 O O   . ASN B 1 216 ? -58.100 45.120 22.500  1.00 38.37 ? 216 ASN B O   1 
ATOM   5915 C CB  . ASN B 1 216 ? -58.458 46.872 24.810  1.00 55.02 ? 216 ASN B CB  1 
ATOM   5916 C CG  . ASN B 1 216 ? -59.151 47.507 26.004  1.00 55.66 ? 216 ASN B CG  1 
ATOM   5917 O OD1 . ASN B 1 216 ? -58.527 48.231 26.784  1.00 59.07 ? 216 ASN B OD1 1 
ATOM   5918 N ND2 . ASN B 1 216 ? -60.439 47.223 26.163  1.00 46.76 ? 216 ASN B ND2 1 
ATOM   5919 N N   . VAL B 1 217 ? -56.779 43.916 23.873  1.00 42.59 ? 217 VAL B N   1 
ATOM   5920 C CA  . VAL B 1 217 ? -55.966 43.400 22.782  1.00 36.53 ? 217 VAL B CA  1 
ATOM   5921 C C   . VAL B 1 217 ? -56.827 42.577 21.823  1.00 31.67 ? 217 VAL B C   1 
ATOM   5922 O O   . VAL B 1 217 ? -57.854 42.002 22.205  1.00 34.50 ? 217 VAL B O   1 
ATOM   5923 C CB  . VAL B 1 217 ? -54.796 42.569 23.341  1.00 33.22 ? 217 VAL B CB  1 
ATOM   5924 C CG1 . VAL B 1 217 ? -55.282 41.201 23.855  1.00 27.78 ? 217 VAL B CG1 1 
ATOM   5925 C CG2 . VAL B 1 217 ? -53.699 42.421 22.310  1.00 29.73 ? 217 VAL B CG2 1 
ATOM   5926 N N   . LYS B 1 218 ? -56.417 42.541 20.560  1.00 29.04 ? 218 LYS B N   1 
ATOM   5927 C CA  . LYS B 1 218 ? -57.051 41.709 19.550  1.00 28.61 ? 218 LYS B CA  1 
ATOM   5928 C C   . LYS B 1 218 ? -56.130 40.546 19.214  1.00 29.62 ? 218 LYS B C   1 
ATOM   5929 O O   . LYS B 1 218 ? -54.967 40.755 18.863  1.00 29.57 ? 218 LYS B O   1 
ATOM   5930 C CB  . LYS B 1 218 ? -57.355 42.514 18.284  1.00 34.85 ? 218 LYS B CB  1 
ATOM   5931 C CG  . LYS B 1 218 ? -58.499 43.497 18.435  1.00 42.81 ? 218 LYS B CG  1 
ATOM   5932 C CD  . LYS B 1 218 ? -58.796 44.200 17.114  1.00 49.64 ? 218 LYS B CD  1 
ATOM   5933 C CE  . LYS B 1 218 ? -60.064 45.021 17.219  1.00 53.52 ? 218 LYS B CE  1 
ATOM   5934 N NZ  . LYS B 1 218 ? -59.914 46.098 18.239  1.00 55.40 ? 218 LYS B NZ  1 
ATOM   5935 N N   . ILE B 1 219 ? -56.648 39.327 19.311  1.00 28.76 ? 219 ILE B N   1 
ATOM   5936 C CA  . ILE B 1 219 ? -55.851 38.146 18.984  1.00 30.79 ? 219 ILE B CA  1 
ATOM   5937 C C   . ILE B 1 219 ? -56.666 37.255 18.058  1.00 31.40 ? 219 ILE B C   1 
ATOM   5938 O O   . ILE B 1 219 ? -57.900 37.362 17.994  1.00 29.27 ? 219 ILE B O   1 
ATOM   5939 C CB  . ILE B 1 219 ? -55.415 37.382 20.256  1.00 29.60 ? 219 ILE B CB  1 
ATOM   5940 C CG1 . ILE B 1 219 ? -56.631 36.817 20.990  1.00 30.70 ? 219 ILE B CG1 1 
ATOM   5941 C CG2 . ILE B 1 219 ? -54.619 38.290 21.174  1.00 25.69 ? 219 ILE B CG2 1 
ATOM   5942 C CD1 . ILE B 1 219 ? -56.263 35.923 22.167  1.00 33.43 ? 219 ILE B CD1 1 
ATOM   5943 N N   . PRO B 1 220 ? -56.004 36.368 17.318  1.00 33.09 ? 220 PRO B N   1 
ATOM   5944 C CA  . PRO B 1 220 ? -56.735 35.467 16.422  1.00 35.11 ? 220 PRO B CA  1 
ATOM   5945 C C   . PRO B 1 220 ? -57.607 34.474 17.186  1.00 30.00 ? 220 PRO B C   1 
ATOM   5946 O O   . PRO B 1 220 ? -57.577 34.360 18.414  1.00 27.19 ? 220 PRO B O   1 
ATOM   5947 C CB  . PRO B 1 220 ? -55.622 34.759 15.635  1.00 27.75 ? 220 PRO B CB  1 
ATOM   5948 C CG  . PRO B 1 220 ? -54.385 34.948 16.435  1.00 29.53 ? 220 PRO B CG  1 
ATOM   5949 C CD  . PRO B 1 220 ? -54.544 36.273 17.115  1.00 28.77 ? 220 PRO B CD  1 
ATOM   5950 N N   . ASP B 1 221 ? -58.432 33.777 16.407  1.00 27.82 ? 221 ASP B N   1 
ATOM   5951 C CA  . ASP B 1 221 ? -59.337 32.746 16.901  1.00 34.79 ? 221 ASP B CA  1 
ATOM   5952 C C   . ASP B 1 221 ? -58.565 31.440 17.069  1.00 37.76 ? 221 ASP B C   1 
ATOM   5953 O O   . ASP B 1 221 ? -58.231 30.779 16.081  1.00 35.14 ? 221 ASP B O   1 
ATOM   5954 C CB  . ASP B 1 221 ? -60.498 32.571 15.924  1.00 37.50 ? 221 ASP B CB  1 
ATOM   5955 C CG  . ASP B 1 221 ? -61.524 31.572 16.404  1.00 46.45 ? 221 ASP B CG  1 
ATOM   5956 O OD1 . ASP B 1 221 ? -61.455 31.143 17.578  1.00 50.82 ? 221 ASP B OD1 1 
ATOM   5957 O OD2 . ASP B 1 221 ? -62.391 31.195 15.590  1.00 52.11 ? 221 ASP B OD2 1 
ATOM   5958 N N   . PHE B 1 222 ? -58.282 31.054 18.315  1.00 30.27 ? 222 PHE B N   1 
ATOM   5959 C CA  . PHE B 1 222 ? -57.615 29.777 18.565  1.00 33.43 ? 222 PHE B CA  1 
ATOM   5960 C C   . PHE B 1 222 ? -58.675 28.681 18.519  1.00 35.77 ? 222 PHE B C   1 
ATOM   5961 O O   . PHE B 1 222 ? -59.217 28.263 19.546  1.00 35.63 ? 222 PHE B O   1 
ATOM   5962 C CB  . PHE B 1 222 ? -56.861 29.774 19.892  1.00 26.00 ? 222 PHE B CB  1 
ATOM   5963 C CG  . PHE B 1 222 ? -55.585 30.582 19.880  1.00 26.26 ? 222 PHE B CG  1 
ATOM   5964 C CD1 . PHE B 1 222 ? -55.602 31.963 19.743  1.00 26.17 ? 222 PHE B CD1 1 
ATOM   5965 C CD2 . PHE B 1 222 ? -54.362 29.943 19.960  1.00 22.46 ? 222 PHE B CD2 1 
ATOM   5966 C CE1 . PHE B 1 222 ? -54.406 32.688 19.728  1.00 27.11 ? 222 PHE B CE1 1 
ATOM   5967 C CE2 . PHE B 1 222 ? -53.174 30.658 19.935  1.00 28.33 ? 222 PHE B CE2 1 
ATOM   5968 C CZ  . PHE B 1 222 ? -53.193 32.023 19.820  1.00 19.27 ? 222 PHE B CZ  1 
ATOM   5969 N N   . ALA B 1 223 ? -58.959 28.209 17.307  1.00 30.16 ? 223 ALA B N   1 
ATOM   5970 C CA  . ALA B 1 223 ? -59.956 27.179 17.058  1.00 37.56 ? 223 ALA B CA  1 
ATOM   5971 C C   . ALA B 1 223 ? -59.439 25.768 17.317  1.00 42.46 ? 223 ALA B C   1 
ATOM   5972 O O   . ALA B 1 223 ? -60.185 24.801 17.118  1.00 43.75 ? 223 ALA B O   1 
ATOM   5973 C CB  . ALA B 1 223 ? -60.467 27.288 15.617  1.00 35.42 ? 223 ALA B CB  1 
ATOM   5974 N N   . VAL B 1 224 ? -58.196 25.633 17.774  1.00 37.04 ? 224 VAL B N   1 
ATOM   5975 C CA  . VAL B 1 224 ? -57.571 24.347 18.042  1.00 31.99 ? 224 VAL B CA  1 
ATOM   5976 C C   . VAL B 1 224 ? -56.883 24.430 19.400  1.00 27.07 ? 224 VAL B C   1 
ATOM   5977 O O   . VAL B 1 224 ? -56.497 25.512 19.849  1.00 27.49 ? 224 VAL B O   1 
ATOM   5978 C CB  . VAL B 1 224 ? -56.575 23.976 16.912  1.00 34.54 ? 224 VAL B CB  1 
ATOM   5979 C CG1 . VAL B 1 224 ? -55.368 24.901 16.937  1.00 36.22 ? 224 VAL B CG1 1 
ATOM   5980 C CG2 . VAL B 1 224 ? -56.160 22.515 16.996  1.00 41.19 ? 224 VAL B CG2 1 
ATOM   5981 N N   . SER B 1 225 ? -56.732 23.280 20.061  1.00 25.64 ? 225 SER B N   1 
ATOM   5982 C CA  . SER B 1 225 ? -56.107 23.225 21.381  1.00 26.50 ? 225 SER B CA  1 
ATOM   5983 C C   . SER B 1 225 ? -54.602 22.991 21.279  1.00 24.34 ? 225 SER B C   1 
ATOM   5984 O O   . SER B 1 225 ? -54.152 22.059 20.599  1.00 25.19 ? 225 SER B O   1 
ATOM   5985 C CB  . SER B 1 225 ? -56.737 22.126 22.237  1.00 30.35 ? 225 SER B CB  1 
ATOM   5986 O OG  . SER B 1 225 ? -56.023 21.962 23.457  1.00 26.87 ? 225 SER B OG  1 
ATOM   5987 N N   . PHE B 1 226 ? -53.834 23.822 21.988  1.00 25.85 ? 226 PHE B N   1 
ATOM   5988 C CA  . PHE B 1 226 ? -52.396 23.651 22.160  1.00 24.43 ? 226 PHE B CA  1 
ATOM   5989 C C   . PHE B 1 226 ? -52.047 23.074 23.524  1.00 21.79 ? 226 PHE B C   1 
ATOM   5990 O O   . PHE B 1 226 ? -50.880 23.100 23.927  1.00 21.33 ? 226 PHE B O   1 
ATOM   5991 C CB  . PHE B 1 226 ? -51.675 24.984 21.964  1.00 22.13 ? 226 PHE B CB  1 
ATOM   5992 C CG  . PHE B 1 226 ? -51.618 25.435 20.530  1.00 27.11 ? 226 PHE B CG  1 
ATOM   5993 C CD1 . PHE B 1 226 ? -50.657 24.925 19.667  1.00 29.58 ? 226 PHE B CD1 1 
ATOM   5994 C CD2 . PHE B 1 226 ? -52.520 26.371 20.048  1.00 26.70 ? 226 PHE B CD2 1 
ATOM   5995 C CE1 . PHE B 1 226 ? -50.599 25.336 18.335  1.00 28.77 ? 226 PHE B CE1 1 
ATOM   5996 C CE2 . PHE B 1 226 ? -52.474 26.787 18.723  1.00 35.29 ? 226 PHE B CE2 1 
ATOM   5997 C CZ  . PHE B 1 226 ? -51.513 26.270 17.864  1.00 32.98 ? 226 PHE B CZ  1 
ATOM   5998 N N   . ARG B 1 227 ? -53.034 22.530 24.234  1.00 25.08 ? 227 ARG B N   1 
ATOM   5999 C CA  . ARG B 1 227 ? -52.809 22.164 25.628  1.00 25.83 ? 227 ARG B CA  1 
ATOM   6000 C C   . ARG B 1 227 ? -51.884 20.956 25.758  1.00 21.48 ? 227 ARG B C   1 
ATOM   6001 O O   . ARG B 1 227 ? -50.991 20.961 26.608  1.00 20.57 ? 227 ARG B O   1 
ATOM   6002 C CB  . ARG B 1 227 ? -54.154 21.922 26.313  1.00 27.06 ? 227 ARG B CB  1 
ATOM   6003 C CG  . ARG B 1 227 ? -54.931 23.215 26.519  1.00 29.73 ? 227 ARG B CG  1 
ATOM   6004 C CD  . ARG B 1 227 ? -56.285 22.975 27.166  1.00 32.25 ? 227 ARG B CD  1 
ATOM   6005 N NE  . ARG B 1 227 ? -56.157 22.374 28.486  1.00 34.02 ? 227 ARG B NE  1 
ATOM   6006 C CZ  . ARG B 1 227 ? -55.854 23.062 29.583  1.00 43.14 ? 227 ARG B CZ  1 
ATOM   6007 N NH1 . ARG B 1 227 ? -55.626 24.369 29.503  1.00 39.04 ? 227 ARG B NH1 1 
ATOM   6008 N NH2 . ARG B 1 227 ? -55.765 22.447 30.757  1.00 47.06 ? 227 ARG B NH2 1 
ATOM   6009 N N   . GLU B 1 228 ? -52.084 19.899 24.953  1.00 22.88 ? 228 GLU B N   1 
ATOM   6010 C CA  . GLU B 1 228 ? -51.165 18.768 25.057  1.00 31.16 ? 228 GLU B CA  1 
ATOM   6011 C C   . GLU B 1 228 ? -49.753 19.148 24.625  1.00 29.86 ? 228 GLU B C   1 
ATOM   6012 O O   . GLU B 1 228 ? -48.772 18.638 25.176  1.00 23.96 ? 228 GLU B O   1 
ATOM   6013 C CB  . GLU B 1 228 ? -51.659 17.563 24.256  1.00 43.26 ? 228 GLU B CB  1 
ATOM   6014 C CG  . GLU B 1 228 ? -50.979 16.282 24.741  1.00 58.72 ? 228 GLU B CG  1 
ATOM   6015 C CD  . GLU B 1 228 ? -51.323 15.933 26.200  1.00 69.34 ? 228 GLU B CD  1 
ATOM   6016 O OE1 . GLU B 1 228 ? -50.643 15.056 26.780  1.00 73.79 ? 228 GLU B OE1 1 
ATOM   6017 O OE2 . GLU B 1 228 ? -52.281 16.514 26.763  1.00 71.57 ? 228 GLU B OE2 1 
ATOM   6018 N N   . ASP B 1 229 ? -49.631 20.032 23.635  1.00 21.66 ? 229 ASP B N   1 
ATOM   6019 C CA  . ASP B 1 229 ? -48.312 20.528 23.243  1.00 27.05 ? 229 ASP B CA  1 
ATOM   6020 C C   . ASP B 1 229 ? -47.597 21.194 24.410  1.00 19.16 ? 229 ASP B C   1 
ATOM   6021 O O   . ASP B 1 229 ? -46.394 20.983 24.613  1.00 18.86 ? 229 ASP B O   1 
ATOM   6022 C CB  . ASP B 1 229 ? -48.424 21.503 22.061  1.00 21.67 ? 229 ASP B CB  1 
ATOM   6023 C CG  . ASP B 1 229 ? -48.671 20.789 20.733  1.00 28.69 ? 229 ASP B CG  1 
ATOM   6024 O OD1 . ASP B 1 229 ? -48.686 19.536 20.712  1.00 29.63 ? 229 ASP B OD1 1 
ATOM   6025 O OD2 . ASP B 1 229 ? -48.788 21.468 19.697  1.00 26.16 ? 229 ASP B OD2 1 
ATOM   6026 N N   . ALA B 1 230 ? -48.311 22.025 25.175  1.00 20.26 ? 230 ALA B N   1 
ATOM   6027 C CA  . ALA B 1 230 ? -47.686 22.637 26.339  1.00 20.62 ? 230 ALA B CA  1 
ATOM   6028 C C   . ALA B 1 230 ? -47.144 21.567 27.279  1.00 18.84 ? 230 ALA B C   1 
ATOM   6029 O O   . ALA B 1 230 ? -46.018 21.679 27.778  1.00 19.84 ? 230 ALA B O   1 
ATOM   6030 C CB  . ALA B 1 230 ? -48.689 23.548 27.056  1.00 20.29 ? 230 ALA B CB  1 
ATOM   6031 N N   . SER B 1 231 ? -47.919 20.499 27.504  1.00 19.11 ? 231 SER B N   1 
ATOM   6032 C CA  . SER B 1 231 ? -47.421 19.396 28.319  1.00 22.08 ? 231 SER B CA  1 
ATOM   6033 C C   . SER B 1 231 ? -46.213 18.725 27.677  1.00 21.05 ? 231 SER B C   1 
ATOM   6034 O O   . SER B 1 231 ? -45.268 18.350 28.376  1.00 23.05 ? 231 SER B O   1 
ATOM   6035 C CB  . SER B 1 231 ? -48.523 18.365 28.558  1.00 28.01 ? 231 SER B CB  1 
ATOM   6036 O OG  . SER B 1 231 ? -49.520 18.897 29.398  1.00 40.40 ? 231 SER B OG  1 
ATOM   6037 N N   . LYS B 1 232 ? -46.232 18.544 26.349  1.00 22.82 ? 232 LYS B N   1 
ATOM   6038 C CA  . LYS B 1 232 ? -45.121 17.853 25.691  1.00 25.82 ? 232 LYS B CA  1 
ATOM   6039 C C   . LYS B 1 232 ? -43.823 18.647 25.770  1.00 22.55 ? 232 LYS B C   1 
ATOM   6040 O O   . LYS B 1 232 ? -42.752 18.051 25.930  1.00 20.18 ? 232 LYS B O   1 
ATOM   6041 C CB  . LYS B 1 232 ? -45.454 17.537 24.232  1.00 26.68 ? 232 LYS B CB  1 
ATOM   6042 C CG  . LYS B 1 232 ? -46.697 16.704 24.067  1.00 42.81 ? 232 LYS B CG  1 
ATOM   6043 C CD  . LYS B 1 232 ? -46.976 16.359 22.619  1.00 51.53 ? 232 LYS B CD  1 
ATOM   6044 C CE  . LYS B 1 232 ? -47.764 15.068 22.531  1.00 60.31 ? 232 LYS B CE  1 
ATOM   6045 N NZ  . LYS B 1 232 ? -47.801 14.549 21.143  1.00 64.11 ? 232 LYS B NZ  1 
ATOM   6046 N N   . HIS B 1 233 ? -43.886 19.984 25.637  1.00 18.54 ? 233 HIS B N   1 
ATOM   6047 C CA  . HIS B 1 233 ? -42.696 20.812 25.833  1.00 17.40 ? 233 HIS B CA  1 
ATOM   6048 C C   . HIS B 1 233 ? -42.057 20.529 27.184  1.00 22.35 ? 233 HIS B C   1 
ATOM   6049 O O   . HIS B 1 233 ? -40.829 20.421 27.303  1.00 17.14 ? 233 HIS B O   1 
ATOM   6050 C CB  . HIS B 1 233 ? -43.042 22.304 25.753  1.00 16.15 ? 233 HIS B CB  1 
ATOM   6051 C CG  . HIS B 1 233 ? -43.231 22.833 24.364  1.00 18.82 ? 233 HIS B CG  1 
ATOM   6052 N ND1 . HIS B 1 233 ? -42.181 23.231 23.563  1.00 18.03 ? 233 HIS B ND1 1 
ATOM   6053 C CD2 . HIS B 1 233 ? -44.361 23.077 23.653  1.00 17.23 ? 233 HIS B CD2 1 
ATOM   6054 C CE1 . HIS B 1 233 ? -42.654 23.678 22.412  1.00 19.71 ? 233 HIS B CE1 1 
ATOM   6055 N NE2 . HIS B 1 233 ? -43.973 23.587 22.439  1.00 18.62 ? 233 HIS B NE2 1 
ATOM   6056 N N   . VAL B 1 234 ? -42.882 20.451 28.225  1.00 17.30 ? 234 VAL B N   1 
ATOM   6057 C CA  . VAL B 1 234 ? -42.364 20.237 29.571  1.00 21.46 ? 234 VAL B CA  1 
ATOM   6058 C C   . VAL B 1 234 ? -41.824 18.821 29.708  1.00 18.58 ? 234 VAL B C   1 
ATOM   6059 O O   . VAL B 1 234 ? -40.717 18.608 30.221  1.00 18.87 ? 234 VAL B O   1 
ATOM   6060 C CB  . VAL B 1 234 ? -43.458 20.534 30.614  1.00 21.58 ? 234 VAL B CB  1 
ATOM   6061 C CG1 . VAL B 1 234 ? -42.955 20.239 32.024  1.00 24.11 ? 234 VAL B CG1 1 
ATOM   6062 C CG2 . VAL B 1 234 ? -43.899 21.989 30.504  1.00 18.03 ? 234 VAL B CG2 1 
ATOM   6063 N N   . GLU B 1 235 ? -42.592 17.828 29.242  1.00 19.82 ? 235 GLU B N   1 
ATOM   6064 C CA  . GLU B 1 235 ? -42.178 16.442 29.432  1.00 21.29 ? 235 GLU B CA  1 
ATOM   6065 C C   . GLU B 1 235 ? -40.908 16.126 28.654  1.00 29.28 ? 235 GLU B C   1 
ATOM   6066 O O   . GLU B 1 235 ? -40.007 15.456 29.172  1.00 22.17 ? 235 GLU B O   1 
ATOM   6067 C CB  . GLU B 1 235 ? -43.306 15.484 29.028  1.00 22.72 ? 235 GLU B CB  1 
ATOM   6068 C CG  . GLU B 1 235 ? -43.258 14.195 29.812  1.00 52.26 ? 235 GLU B CG  1 
ATOM   6069 C CD  . GLU B 1 235 ? -43.699 14.403 31.253  1.00 60.22 ? 235 GLU B CD  1 
ATOM   6070 O OE1 . GLU B 1 235 ? -44.709 15.103 31.470  1.00 65.45 ? 235 GLU B OE1 1 
ATOM   6071 O OE2 . GLU B 1 235 ? -43.018 13.897 32.170  1.00 64.62 ? 235 GLU B OE2 1 
ATOM   6072 N N   . LEU B 1 236 ? -40.815 16.597 27.409  1.00 21.13 ? 236 LEU B N   1 
ATOM   6073 C CA  . LEU B 1 236 ? -39.608 16.360 26.629  1.00 25.02 ? 236 LEU B CA  1 
ATOM   6074 C C   . LEU B 1 236 ? -38.401 17.052 27.254  1.00 23.58 ? 236 LEU B C   1 
ATOM   6075 O O   . LEU B 1 236 ? -37.286 16.520 27.210  1.00 21.10 ? 236 LEU B O   1 
ATOM   6076 C CB  . LEU B 1 236 ? -39.816 16.823 25.183  1.00 25.15 ? 236 LEU B CB  1 
ATOM   6077 C CG  . LEU B 1 236 ? -40.768 15.943 24.356  1.00 22.62 ? 236 LEU B CG  1 
ATOM   6078 C CD1 . LEU B 1 236 ? -41.076 16.592 23.018  1.00 22.56 ? 236 LEU B CD1 1 
ATOM   6079 C CD2 . LEU B 1 236 ? -40.195 14.547 24.156  1.00 24.30 ? 236 LEU B CD2 1 
ATOM   6080 N N   . ALA B 1 237 ? -38.602 18.239 27.840  1.00 19.33 ? 237 ALA B N   1 
ATOM   6081 C CA  . ALA B 1 237 ? -37.511 18.914 28.540  1.00 18.35 ? 237 ALA B CA  1 
ATOM   6082 C C   . ALA B 1 237 ? -37.043 18.109 29.745  1.00 19.98 ? 237 ALA B C   1 
ATOM   6083 O O   . ALA B 1 237 ? -35.839 18.018 30.014  1.00 19.73 ? 237 ALA B O   1 
ATOM   6084 C CB  . ALA B 1 237 ? -37.948 20.314 28.979  1.00 16.92 ? 237 ALA B CB  1 
ATOM   6085 N N   . LYS B 1 238 ? -37.981 17.529 30.491  1.00 19.68 ? 238 LYS B N   1 
ATOM   6086 C CA  . LYS B 1 238 ? -37.607 16.673 31.622  1.00 24.57 ? 238 LYS B CA  1 
ATOM   6087 C C   . LYS B 1 238 ? -36.708 15.516 31.185  1.00 23.78 ? 238 LYS B C   1 
ATOM   6088 O O   . LYS B 1 238 ? -35.698 15.220 31.836  1.00 23.25 ? 238 LYS B O   1 
ATOM   6089 C CB  . LYS B 1 238 ? -38.866 16.144 32.304  1.00 24.45 ? 238 LYS B CB  1 
ATOM   6090 C CG  . LYS B 1 238 ? -39.645 17.214 33.076  1.00 23.41 ? 238 LYS B CG  1 
ATOM   6091 C CD  . LYS B 1 238 ? -40.983 16.655 33.525  1.00 23.42 ? 238 LYS B CD  1 
ATOM   6092 C CE  . LYS B 1 238 ? -40.799 15.540 34.541  1.00 30.29 ? 238 LYS B CE  1 
ATOM   6093 N NZ  . LYS B 1 238 ? -42.127 15.015 34.975  1.00 32.81 ? 238 LYS B NZ  1 
ATOM   6094 N N   . GLU B 1 239 ? -37.081 14.822 30.104  1.00 22.86 ? 239 GLU B N   1 
ATOM   6095 C CA  . GLU B 1 239 ? -36.319 13.656 29.669  1.00 26.19 ? 239 GLU B CA  1 
ATOM   6096 C C   . GLU B 1 239 ? -34.911 14.048 29.227  1.00 30.27 ? 239 GLU B C   1 
ATOM   6097 O O   . GLU B 1 239 ? -33.928 13.371 29.566  1.00 25.11 ? 239 GLU B O   1 
ATOM   6098 C CB  . GLU B 1 239 ? -37.064 12.939 28.539  1.00 27.50 ? 239 GLU B CB  1 
ATOM   6099 C CG  . GLU B 1 239 ? -38.543 12.682 28.819  1.00 40.66 ? 239 GLU B CG  1 
ATOM   6100 C CD  . GLU B 1 239 ? -39.322 12.351 27.558  1.00 50.59 ? 239 GLU B CD  1 
ATOM   6101 O OE1 . GLU B 1 239 ? -40.565 12.476 27.577  1.00 53.46 ? 239 GLU B OE1 1 
ATOM   6102 O OE2 . GLU B 1 239 ? -38.690 11.981 26.545  1.00 53.65 ? 239 GLU B OE2 1 
ATOM   6103 N N   . LYS B 1 240 ? -34.804 15.125 28.438  1.00 22.84 ? 240 LYS B N   1 
ATOM   6104 C CA  . LYS B 1 240 ? -33.508 15.627 27.980  1.00 26.73 ? 240 LYS B CA  1 
ATOM   6105 C C   . LYS B 1 240 ? -32.619 16.018 29.158  1.00 23.39 ? 240 LYS B C   1 
ATOM   6106 O O   . LYS B 1 240 ? -31.417 15.715 29.167  1.00 22.99 ? 240 LYS B O   1 
ATOM   6107 C CB  . LYS B 1 240 ? -33.711 16.822 27.045  1.00 24.54 ? 240 LYS B CB  1 
ATOM   6108 C CG  . LYS B 1 240 ? -32.434 17.316 26.367  1.00 27.84 ? 240 LYS B CG  1 
ATOM   6109 C CD  . LYS B 1 240 ? -31.966 16.356 25.268  1.00 36.63 ? 240 LYS B CD  1 
ATOM   6110 C CE  . LYS B 1 240 ? -30.775 16.931 24.515  1.00 40.53 ? 240 LYS B CE  1 
ATOM   6111 N NZ  . LYS B 1 240 ? -30.264 16.036 23.446  1.00 46.78 ? 240 LYS B NZ  1 
ATOM   6112 N N   . TYR B 1 241 ? -33.185 16.680 30.152  1.00 21.35 ? 241 TYR B N   1 
ATOM   6113 C CA  . TYR B 1 241 ? -32.445 17.102 31.321  1.00 30.72 ? 241 TYR B CA  1 
ATOM   6114 C C   . TYR B 1 241 ? -31.907 15.914 32.104  1.00 33.57 ? 241 TYR B C   1 
ATOM   6115 O O   . TYR B 1 241 ? -30.780 15.885 32.448  1.00 23.20 ? 241 TYR B O   1 
ATOM   6116 C CB  . TYR B 1 241 ? -33.282 17.981 32.209  1.00 25.18 ? 241 TYR B CB  1 
ATOM   6117 C CG  . TYR B 1 241 ? -32.573 18.521 33.397  1.00 32.40 ? 241 TYR B CG  1 
ATOM   6118 C CD1 . TYR B 1 241 ? -32.480 17.800 34.550  1.00 39.61 ? 241 TYR B CD1 1 
ATOM   6119 C CD2 . TYR B 1 241 ? -32.041 19.779 33.390  1.00 29.71 ? 241 TYR B CD2 1 
ATOM   6120 C CE1 . TYR B 1 241 ? -31.871 18.314 35.658  1.00 40.66 ? 241 TYR B CE1 1 
ATOM   6121 C CE2 . TYR B 1 241 ? -31.400 20.273 34.491  1.00 40.01 ? 241 TYR B CE2 1 
ATOM   6122 C CZ  . TYR B 1 241 ? -31.319 19.539 35.622  1.00 38.94 ? 241 TYR B CZ  1 
ATOM   6123 O OH  . TYR B 1 241 ? -30.707 20.023 36.732  1.00 46.55 ? 241 TYR B OH  1 
ATOM   6124 N N   . PHE B 1 242 ? -32.777 14.954 32.357  1.00 23.58 ? 242 PHE B N   1 
ATOM   6125 C CA  . PHE B 1 242 ? -32.319 13.734 33.030  1.00 25.31 ? 242 PHE B CA  1 
ATOM   6126 C C   . PHE B 1 242 ? -31.149 13.102 32.282  1.00 30.92 ? 242 PHE B C   1 
ATOM   6127 O O   . PHE B 1 242 ? -30.146 12.715 32.895  1.00 32.97 ? 242 PHE B O   1 
ATOM   6128 C CB  . PHE B 1 242 ? -33.461 12.729 33.178  1.00 26.30 ? 242 PHE B CB  1 
ATOM   6129 C CG  . PHE B 1 242 ? -33.096 11.540 34.052  1.00 28.15 ? 242 PHE B CG  1 
ATOM   6130 C CD1 . PHE B 1 242 ? -33.277 11.587 35.429  1.00 28.36 ? 242 PHE B CD1 1 
ATOM   6131 C CD2 . PHE B 1 242 ? -32.526 10.405 33.497  1.00 30.09 ? 242 PHE B CD2 1 
ATOM   6132 C CE1 . PHE B 1 242 ? -32.930 10.513 36.238  1.00 33.72 ? 242 PHE B CE1 1 
ATOM   6133 C CE2 . PHE B 1 242 ? -32.165 9.321  34.298  1.00 31.64 ? 242 PHE B CE2 1 
ATOM   6134 C CZ  . PHE B 1 242 ? -32.370 9.379  35.671  1.00 31.84 ? 242 PHE B CZ  1 
ATOM   6135 N N   . GLU B 1 243 ? -31.269 12.978 30.952  1.00 26.40 ? 243 GLU B N   1 
ATOM   6136 C CA  . GLU B 1 243 ? -30.187 12.421 30.148  1.00 27.49 ? 243 GLU B CA  1 
ATOM   6137 C C   . GLU B 1 243 ? -28.876 13.171 30.377  1.00 37.28 ? 243 GLU B C   1 
ATOM   6138 O O   . GLU B 1 243 ? -27.821 12.557 30.578  1.00 33.15 ? 243 GLU B O   1 
ATOM   6139 C CB  . GLU B 1 243 ? -30.565 12.450 28.659  1.00 34.64 ? 243 GLU B CB  1 
ATOM   6140 C CG  . GLU B 1 243 ? -29.409 12.804 27.707  1.00 46.07 ? 243 GLU B CG  1 
ATOM   6141 C CD  . GLU B 1 243 ? -29.856 13.031 26.253  1.00 60.57 ? 243 GLU B CD  1 
ATOM   6142 O OE1 . GLU B 1 243 ? -28.993 13.368 25.409  1.00 64.14 ? 243 GLU B OE1 1 
ATOM   6143 O OE2 . GLU B 1 243 ? -31.061 12.872 25.950  1.00 64.69 ? 243 GLU B OE2 1 
ATOM   6144 N N   . ILE B 1 244 ? -28.926 14.504 30.346  1.00 28.29 ? 244 ILE B N   1 
ATOM   6145 C CA  . ILE B 1 244 ? -27.707 15.313 30.389  1.00 34.74 ? 244 ILE B CA  1 
ATOM   6146 C C   . ILE B 1 244 ? -27.167 15.409 31.813  1.00 32.14 ? 244 ILE B C   1 
ATOM   6147 O O   . ILE B 1 244 ? -25.959 15.279 32.038  1.00 37.99 ? 244 ILE B O   1 
ATOM   6148 C CB  . ILE B 1 244 ? -27.966 16.718 29.791  1.00 34.90 ? 244 ILE B CB  1 
ATOM   6149 C CG1 . ILE B 1 244 ? -28.579 16.634 28.386  1.00 29.65 ? 244 ILE B CG1 1 
ATOM   6150 C CG2 . ILE B 1 244 ? -26.678 17.519 29.698  1.00 30.08 ? 244 ILE B CG2 1 
ATOM   6151 C CD1 . ILE B 1 244 ? -27.678 16.000 27.352  1.00 25.80 ? 244 ILE B CD1 1 
ATOM   6152 N N   . PHE B 1 245 ? -28.040 15.606 32.802  1.00 25.44 ? 245 PHE B N   1 
ATOM   6153 C CA  . PHE B 1 245 ? -27.582 15.997 34.125  1.00 31.10 ? 245 PHE B CA  1 
ATOM   6154 C C   . PHE B 1 245 ? -27.921 15.022 35.249  1.00 36.98 ? 245 PHE B C   1 
ATOM   6155 O O   . PHE B 1 245 ? -27.454 15.234 36.374  1.00 38.37 ? 245 PHE B O   1 
ATOM   6156 C CB  . PHE B 1 245 ? -28.123 17.397 34.470  1.00 28.04 ? 245 PHE B CB  1 
ATOM   6157 C CG  . PHE B 1 245 ? -27.640 18.468 33.532  1.00 33.41 ? 245 PHE B CG  1 
ATOM   6158 C CD1 . PHE B 1 245 ? -26.307 18.850 33.532  1.00 36.64 ? 245 PHE B CD1 1 
ATOM   6159 C CD2 . PHE B 1 245 ? -28.514 19.097 32.657  1.00 29.22 ? 245 PHE B CD2 1 
ATOM   6160 C CE1 . PHE B 1 245 ? -25.848 19.829 32.673  1.00 39.92 ? 245 PHE B CE1 1 
ATOM   6161 C CE2 . PHE B 1 245 ? -28.058 20.078 31.793  1.00 36.16 ? 245 PHE B CE2 1 
ATOM   6162 C CZ  . PHE B 1 245 ? -26.728 20.450 31.803  1.00 38.23 ? 245 PHE B CZ  1 
ATOM   6163 N N   . GLY B 1 246 ? -28.708 13.979 34.994  1.00 29.51 ? 246 GLY B N   1 
ATOM   6164 C CA  . GLY B 1 246 ? -28.925 12.934 35.987  1.00 35.50 ? 246 GLY B CA  1 
ATOM   6165 C C   . GLY B 1 246 ? -29.743 13.293 37.213  1.00 39.89 ? 246 GLY B C   1 
ATOM   6166 O O   . GLY B 1 246 ? -29.377 12.916 38.335  1.00 42.72 ? 246 GLY B O   1 
ATOM   6167 N N   . GLU B 1 247 ? -30.852 14.002 37.022  1.00 38.26 ? 247 GLU B N   1 
ATOM   6168 C CA  . GLU B 1 247 ? -31.793 14.289 38.092  1.00 43.24 ? 247 GLU B CA  1 
ATOM   6169 C C   . GLU B 1 247 ? -33.127 14.612 37.445  1.00 31.19 ? 247 GLU B C   1 
ATOM   6170 O O   . GLU B 1 247 ? -33.170 15.110 36.321  1.00 27.16 ? 247 GLU B O   1 
ATOM   6171 C CB  . GLU B 1 247 ? -31.327 15.464 38.970  1.00 54.47 ? 247 GLU B CB  1 
ATOM   6172 C CG  . GLU B 1 247 ? -31.562 15.271 40.468  1.00 68.51 ? 247 GLU B CG  1 
ATOM   6173 C CD  . GLU B 1 247 ? -31.254 16.513 41.285  1.00 77.30 ? 247 GLU B CD  1 
ATOM   6174 O OE1 . GLU B 1 247 ? -30.375 17.299 40.865  1.00 80.18 ? 247 GLU B OE1 1 
ATOM   6175 O OE2 . GLU B 1 247 ? -31.888 16.694 42.351  1.00 79.89 ? 247 GLU B OE2 1 
ATOM   6176 N N   . HIS B 1 248 ? -34.209 14.325 38.152  1.00 32.17 ? 248 HIS B N   1 
ATOM   6177 C CA  . HIS B 1 248 ? -35.503 14.807 37.695  1.00 42.17 ? 248 HIS B CA  1 
ATOM   6178 C C   . HIS B 1 248 ? -35.513 16.302 37.936  1.00 37.97 ? 248 HIS B C   1 
ATOM   6179 O O   . HIS B 1 248 ? -35.262 16.731 39.068  1.00 41.19 ? 248 HIS B O   1 
ATOM   6180 C CB  . HIS B 1 248 ? -36.653 14.151 38.445  1.00 50.67 ? 248 HIS B CB  1 
ATOM   6181 C CG  . HIS B 1 248 ? -36.527 12.668 38.564  1.00 59.74 ? 248 HIS B CG  1 
ATOM   6182 N ND1 . HIS B 1 248 ? -35.826 12.062 39.584  1.00 62.06 ? 248 HIS B ND1 1 
ATOM   6183 C CD2 . HIS B 1 248 ? -37.010 11.670 37.789  1.00 61.89 ? 248 HIS B CD2 1 
ATOM   6184 C CE1 . HIS B 1 248 ? -35.888 10.752 39.435  1.00 64.45 ? 248 HIS B CE1 1 
ATOM   6185 N NE2 . HIS B 1 248 ? -36.598 10.487 38.353  1.00 64.98 ? 248 HIS B NE2 1 
ATOM   6186 N N   . PRO B 1 249 ? -35.745 17.129 36.921  1.00 41.44 ? 249 PRO B N   1 
ATOM   6187 C CA  . PRO B 1 249 ? -35.772 18.574 37.170  1.00 35.05 ? 249 PRO B CA  1 
ATOM   6188 C C   . PRO B 1 249 ? -36.932 18.971 38.077  1.00 38.99 ? 249 PRO B C   1 
ATOM   6189 O O   . PRO B 1 249 ? -38.094 18.788 37.710  1.00 45.86 ? 249 PRO B O   1 
ATOM   6190 C CB  . PRO B 1 249 ? -35.915 19.173 35.765  1.00 36.61 ? 249 PRO B CB  1 
ATOM   6191 C CG  . PRO B 1 249 ? -36.464 18.082 34.935  1.00 34.21 ? 249 PRO B CG  1 
ATOM   6192 C CD  . PRO B 1 249 ? -35.918 16.808 35.496  1.00 36.06 ? 249 PRO B CD  1 
ATOM   6193 N N   . VAL B 1 250 ? -36.634 19.482 39.275  1.00 31.37 ? 250 VAL B N   1 
ATOM   6194 C CA  . VAL B 1 250 ? -37.676 19.976 40.168  1.00 26.22 ? 250 VAL B CA  1 
ATOM   6195 C C   . VAL B 1 250 ? -37.787 21.485 40.133  1.00 25.61 ? 250 VAL B C   1 
ATOM   6196 O O   . VAL B 1 250 ? -38.656 22.053 40.817  1.00 21.75 ? 250 VAL B O   1 
ATOM   6197 C CB  . VAL B 1 250 ? -37.464 19.482 41.619  1.00 32.40 ? 250 VAL B CB  1 
ATOM   6198 C CG1 . VAL B 1 250 ? -37.525 17.952 41.676  1.00 34.26 ? 250 VAL B CG1 1 
ATOM   6199 C CG2 . VAL B 1 250 ? -36.152 20.020 42.144  1.00 38.63 ? 250 VAL B CG2 1 
ATOM   6200 N N   . TYR B 1 251 ? -36.941 22.162 39.350  1.00 17.14 ? 251 TYR B N   1 
ATOM   6201 C CA  . TYR B 1 251 ? -37.082 23.587 39.095  1.00 16.00 ? 251 TYR B CA  1 
ATOM   6202 C C   . TYR B 1 251 ? -36.860 23.836 37.615  1.00 18.92 ? 251 TYR B C   1 
ATOM   6203 O O   . TYR B 1 251 ? -36.136 23.091 36.946  1.00 25.76 ? 251 TYR B O   1 
ATOM   6204 C CB  . TYR B 1 251 ? -36.142 24.400 40.016  1.00 18.87 ? 251 TYR B CB  1 
ATOM   6205 C CG  . TYR B 1 251 ? -34.755 23.855 40.179  1.00 23.85 ? 251 TYR B CG  1 
ATOM   6206 C CD1 . TYR B 1 251 ? -33.945 23.574 39.092  1.00 28.11 ? 251 TYR B CD1 1 
ATOM   6207 C CD2 . TYR B 1 251 ? -34.344 23.403 41.425  1.00 22.83 ? 251 TYR B CD2 1 
ATOM   6208 C CE1 . TYR B 1 251 ? -32.683 23.003 39.277  1.00 29.98 ? 251 TYR B CE1 1 
ATOM   6209 C CE2 . TYR B 1 251 ? -33.119 22.817 41.614  1.00 27.08 ? 251 TYR B CE2 1 
ATOM   6210 C CZ  . TYR B 1 251 ? -32.283 22.611 40.538  1.00 31.88 ? 251 TYR B CZ  1 
ATOM   6211 O OH  . TYR B 1 251 ? -31.041 22.028 40.716  1.00 28.03 ? 251 TYR B OH  1 
ATOM   6212 N N   . MET B 1 252 ? -37.590 24.817 37.096  1.00 16.41 ? 252 MET B N   1 
ATOM   6213 C CA  . MET B 1 252 ? -37.499 25.209 35.694  1.00 13.48 ? 252 MET B CA  1 
ATOM   6214 C C   . MET B 1 252 ? -37.609 26.719 35.592  1.00 14.47 ? 252 MET B C   1 
ATOM   6215 O O   . MET B 1 252 ? -38.219 27.383 36.443  1.00 14.84 ? 252 MET B O   1 
ATOM   6216 C CB  . MET B 1 252 ? -38.601 24.565 34.833  1.00 16.44 ? 252 MET B CB  1 
ATOM   6217 C CG  . MET B 1 252 ? -38.345 23.144 34.431  1.00 21.89 ? 252 MET B CG  1 
ATOM   6218 S SD  . MET B 1 252 ? -39.538 22.658 33.153  1.00 19.84 ? 252 MET B SD  1 
ATOM   6219 C CE  . MET B 1 252 ? -39.027 20.972 32.855  1.00 19.19 ? 252 MET B CE  1 
ATOM   6220 N N   . TRP B 1 253 ? -36.981 27.263 34.550  1.00 11.98 ? 253 TRP B N   1 
ATOM   6221 C CA  . TRP B 1 253 ? -37.163 28.659 34.211  1.00 11.27 ? 253 TRP B CA  1 
ATOM   6222 C C   . TRP B 1 253 ? -38.288 28.778 33.196  1.00 13.15 ? 253 TRP B C   1 
ATOM   6223 O O   . TRP B 1 253 ? -38.152 28.249 32.081  1.00 12.73 ? 253 TRP B O   1 
ATOM   6224 C CB  . TRP B 1 253 ? -35.886 29.249 33.622  1.00 11.91 ? 253 TRP B CB  1 
ATOM   6225 C CG  . TRP B 1 253 ? -36.119 30.619 33.056  1.00 12.11 ? 253 TRP B CG  1 
ATOM   6226 C CD1 . TRP B 1 253 ? -36.042 30.990 31.746  1.00 11.98 ? 253 TRP B CD1 1 
ATOM   6227 C CD2 . TRP B 1 253 ? -36.511 31.794 33.784  1.00 11.26 ? 253 TRP B CD2 1 
ATOM   6228 N NE1 . TRP B 1 253 ? -36.339 32.325 31.616  1.00 11.22 ? 253 TRP B NE1 1 
ATOM   6229 C CE2 . TRP B 1 253 ? -36.650 32.839 32.846  1.00 16.99 ? 253 TRP B CE2 1 
ATOM   6230 C CE3 . TRP B 1 253 ? -36.761 32.062 35.138  1.00 11.01 ? 253 TRP B CE3 1 
ATOM   6231 C CZ2 . TRP B 1 253 ? -37.019 34.132 33.215  1.00 11.40 ? 253 TRP B CZ2 1 
ATOM   6232 C CZ3 . TRP B 1 253 ? -37.115 33.345 35.508  1.00 11.35 ? 253 TRP B CZ3 1 
ATOM   6233 C CH2 . TRP B 1 253 ? -37.243 34.367 34.549  1.00 13.14 ? 253 TRP B CH2 1 
ATOM   6234 N N   . PRO B 1 254 ? -39.399 29.438 33.517  1.00 10.92 ? 254 PRO B N   1 
ATOM   6235 C CA  . PRO B 1 254 ? -40.466 29.612 32.522  1.00 12.99 ? 254 PRO B CA  1 
ATOM   6236 C C   . PRO B 1 254 ? -40.041 30.630 31.479  1.00 11.24 ? 254 PRO B C   1 
ATOM   6237 O O   . PRO B 1 254 ? -39.580 31.730 31.827  1.00 14.30 ? 254 PRO B O   1 
ATOM   6238 C CB  . PRO B 1 254 ? -41.662 30.108 33.356  1.00 13.05 ? 254 PRO B CB  1 
ATOM   6239 C CG  . PRO B 1 254 ? -41.018 30.797 34.545  1.00 16.59 ? 254 PRO B CG  1 
ATOM   6240 C CD  . PRO B 1 254 ? -39.721 30.080 34.810  1.00 15.61 ? 254 PRO B CD  1 
ATOM   6241 N N   . PRO B 1 255 ? -40.135 30.280 30.197  1.00 12.32 ? 255 PRO B N   1 
ATOM   6242 C CA  . PRO B 1 255 ? -39.675 31.192 29.146  1.00 11.50 ? 255 PRO B CA  1 
ATOM   6243 C C   . PRO B 1 255 ? -40.315 32.560 29.279  1.00 9.64  ? 255 PRO B C   1 
ATOM   6244 O O   . PRO B 1 255 ? -41.515 32.689 29.544  1.00 13.10 ? 255 PRO B O   1 
ATOM   6245 C CB  . PRO B 1 255 ? -40.094 30.480 27.853  1.00 14.79 ? 255 PRO B CB  1 
ATOM   6246 C CG  . PRO B 1 255 ? -40.014 29.016 28.223  1.00 15.11 ? 255 PRO B CG  1 
ATOM   6247 C CD  . PRO B 1 255 ? -40.518 28.962 29.661  1.00 11.80 ? 255 PRO B CD  1 
ATOM   6248 N N   . GLU B 1 256 ? -39.485 33.587 29.135  1.00 10.37 ? 256 GLU B N   1 
ATOM   6249 C CA  . GLU B 1 256 ? -39.901 34.985 29.271  1.00 13.02 ? 256 GLU B CA  1 
ATOM   6250 C C   . GLU B 1 256 ? -40.517 35.259 30.640  1.00 12.00 ? 256 GLU B C   1 
ATOM   6251 O O   . GLU B 1 256 ? -41.371 36.140 30.787  1.00 10.63 ? 256 GLU B O   1 
ATOM   6252 C CB  . GLU B 1 256 ? -40.852 35.392 28.128  1.00 15.06 ? 256 GLU B CB  1 
ATOM   6253 C CG  . GLU B 1 256 ? -40.268 34.965 26.783  1.00 17.41 ? 256 GLU B CG  1 
ATOM   6254 C CD  . GLU B 1 256 ? -39.098 35.839 26.337  1.00 26.04 ? 256 GLU B CD  1 
ATOM   6255 O OE1 . GLU B 1 256 ? -38.712 36.775 27.072  1.00 38.33 ? 256 GLU B OE1 1 
ATOM   6256 O OE2 . GLU B 1 256 ? -38.492 35.513 25.298  1.00 33.54 ? 256 GLU B OE2 1 
ATOM   6257 N N   . ALA B 1 257 ? -40.076 34.503 31.653  1.00 10.72 ? 257 ALA B N   1 
ATOM   6258 C CA  . ALA B 1 257 ? -40.663 34.540 33.001  1.00 10.84 ? 257 ALA B CA  1 
ATOM   6259 C C   . ALA B 1 257 ? -42.182 34.334 32.975  1.00 14.46 ? 257 ALA B C   1 
ATOM   6260 O O   . ALA B 1 257 ? -42.897 34.759 33.896  1.00 14.58 ? 257 ALA B O   1 
ATOM   6261 C CB  . ALA B 1 257 ? -40.315 35.859 33.725  1.00 8.31  ? 257 ALA B CB  1 
ATOM   6262 N N   . SER B 1 258 ? -42.721 33.673 31.948  1.00 13.94 ? 258 SER B N   1 
ATOM   6263 C CA  . SER B 1 258 ? -44.160 33.756 31.731  1.00 10.90 ? 258 SER B CA  1 
ATOM   6264 C C   . SER B 1 258 ? -44.905 32.762 32.614  1.00 13.96 ? 258 SER B C   1 
ATOM   6265 O O   . SER B 1 258 ? -44.627 31.558 32.596  1.00 16.14 ? 258 SER B O   1 
ATOM   6266 C CB  . SER B 1 258 ? -44.511 33.524 30.265  1.00 15.99 ? 258 SER B CB  1 
ATOM   6267 O OG  . SER B 1 258 ? -45.895 33.765 30.094  1.00 20.94 ? 258 SER B OG  1 
ATOM   6268 N N   . VAL B 1 259 ? -45.864 33.269 33.381  1.00 14.48 ? 259 VAL B N   1 
ATOM   6269 C CA  . VAL B 1 259 ? -46.680 32.420 34.234  1.00 13.76 ? 259 VAL B CA  1 
ATOM   6270 C C   . VAL B 1 259 ? -48.136 32.835 34.104  1.00 17.36 ? 259 VAL B C   1 
ATOM   6271 O O   . VAL B 1 259 ? -48.471 33.930 33.638  1.00 17.53 ? 259 VAL B O   1 
ATOM   6272 C CB  . VAL B 1 259 ? -46.262 32.453 35.723  1.00 16.10 ? 259 VAL B CB  1 
ATOM   6273 C CG1 . VAL B 1 259 ? -44.865 31.857 35.914  1.00 18.56 ? 259 VAL B CG1 1 
ATOM   6274 C CG2 . VAL B 1 259 ? -46.345 33.873 36.274  1.00 16.40 ? 259 VAL B CG2 1 
ATOM   6275 N N   . SER B 1 260 ? -48.993 31.912 34.513  1.00 14.77 ? 260 SER B N   1 
ATOM   6276 C CA  . SER B 1 260 ? -50.425 32.104 34.623  1.00 14.55 ? 260 SER B CA  1 
ATOM   6277 C C   . SER B 1 260 ? -50.867 31.095 35.660  1.00 14.11 ? 260 SER B C   1 
ATOM   6278 O O   . SER B 1 260 ? -50.103 30.190 36.010  1.00 16.39 ? 260 SER B O   1 
ATOM   6279 C CB  . SER B 1 260 ? -51.131 31.876 33.290  1.00 15.20 ? 260 SER B CB  1 
ATOM   6280 O OG  . SER B 1 260 ? -51.089 30.501 32.923  1.00 18.52 ? 260 SER B OG  1 
ATOM   6281 N N   . ASN B 1 261 ? -52.088 31.259 36.181  1.00 13.34 ? 261 ASN B N   1 
ATOM   6282 C CA  . ASN B 1 261 ? -52.596 30.256 37.108  1.00 16.29 ? 261 ASN B CA  1 
ATOM   6283 C C   . ASN B 1 261 ? -52.548 28.866 36.480  1.00 18.29 ? 261 ASN B C   1 
ATOM   6284 O O   . ASN B 1 261 ? -52.134 27.894 37.127  1.00 19.15 ? 261 ASN B O   1 
ATOM   6285 C CB  . ASN B 1 261 ? -54.024 30.605 37.551  1.00 19.60 ? 261 ASN B CB  1 
ATOM   6286 C CG  . ASN B 1 261 ? -54.078 31.870 38.401  1.00 22.44 ? 261 ASN B CG  1 
ATOM   6287 O OD1 . ASN B 1 261 ? -53.146 32.156 39.155  1.00 17.81 ? 261 ASN B OD1 1 
ATOM   6288 N ND2 . ASN B 1 261 ? -55.186 32.623 38.295  1.00 20.70 ? 261 ASN B ND2 1 
ATOM   6289 N N   . GLU B 1 262 ? -52.959 28.753 35.215  1.00 17.07 ? 262 GLU B N   1 
ATOM   6290 C CA  . GLU B 1 262 ? -52.975 27.445 34.565  1.00 19.48 ? 262 GLU B CA  1 
ATOM   6291 C C   . GLU B 1 262 ? -51.566 26.937 34.296  1.00 18.03 ? 262 GLU B C   1 
ATOM   6292 O O   . GLU B 1 262 ? -51.303 25.735 34.424  1.00 18.15 ? 262 GLU B O   1 
ATOM   6293 C CB  . GLU B 1 262 ? -53.775 27.498 33.264  1.00 22.05 ? 262 GLU B CB  1 
ATOM   6294 C CG  . GLU B 1 262 ? -55.218 27.916 33.476  1.00 23.59 ? 262 GLU B CG  1 
ATOM   6295 C CD  . GLU B 1 262 ? -56.108 27.618 32.280  1.00 33.80 ? 262 GLU B CD  1 
ATOM   6296 O OE1 . GLU B 1 262 ? -55.678 26.874 31.371  1.00 36.54 ? 262 GLU B OE1 1 
ATOM   6297 O OE2 . GLU B 1 262 ? -57.233 28.153 32.243  1.00 40.17 ? 262 GLU B OE2 1 
ATOM   6298 N N   . ALA B 1 263 ? -50.647 27.831 33.926  1.00 14.30 ? 263 ALA B N   1 
ATOM   6299 C CA  . ALA B 1 263 ? -49.269 27.408 33.691  1.00 14.75 ? 263 ALA B CA  1 
ATOM   6300 C C   . ALA B 1 263 ? -48.614 26.910 34.980  1.00 17.07 ? 263 ALA B C   1 
ATOM   6301 O O   . ALA B 1 263 ? -47.904 25.899 34.968  1.00 16.35 ? 263 ALA B O   1 
ATOM   6302 C CB  . ALA B 1 263 ? -48.456 28.546 33.079  1.00 14.25 ? 263 ALA B CB  1 
ATOM   6303 N N   . LEU B 1 264 ? -48.852 27.593 36.102  1.00 14.05 ? 264 LEU B N   1 
ATOM   6304 C CA  . LEU B 1 264 ? -48.310 27.117 37.377  1.00 14.28 ? 264 LEU B CA  1 
ATOM   6305 C C   . LEU B 1 264 ? -48.861 25.744 37.729  1.00 19.22 ? 264 LEU B C   1 
ATOM   6306 O O   . LEU B 1 264 ? -48.132 24.893 38.253  1.00 19.62 ? 264 LEU B O   1 
ATOM   6307 C CB  . LEU B 1 264 ? -48.604 28.123 38.493  1.00 13.87 ? 264 LEU B CB  1 
ATOM   6308 C CG  . LEU B 1 264 ? -47.817 29.439 38.353  1.00 19.32 ? 264 LEU B CG  1 
ATOM   6309 C CD1 . LEU B 1 264 ? -48.422 30.571 39.198  1.00 19.32 ? 264 LEU B CD1 1 
ATOM   6310 C CD2 . LEU B 1 264 ? -46.356 29.224 38.727  1.00 27.41 ? 264 LEU B CD2 1 
ATOM   6311 N N   . GLU B 1 265 ? -50.146 25.506 37.435  1.00 20.72 ? 265 GLU B N   1 
ATOM   6312 C CA  . GLU B 1 265 ? -50.734 24.190 37.664  1.00 21.37 ? 265 GLU B CA  1 
ATOM   6313 C C   . GLU B 1 265 ? -50.074 23.128 36.792  1.00 17.81 ? 265 GLU B C   1 
ATOM   6314 O O   . GLU B 1 265 ? -49.882 21.988 37.232  1.00 20.06 ? 265 GLU B O   1 
ATOM   6315 C CB  . GLU B 1 265 ? -52.244 24.232 37.402  1.00 25.89 ? 265 GLU B CB  1 
ATOM   6316 C CG  . GLU B 1 265 ? -53.031 24.989 38.461  1.00 28.08 ? 265 GLU B CG  1 
ATOM   6317 C CD  . GLU B 1 265 ? -54.511 25.086 38.130  1.00 37.96 ? 265 GLU B CD  1 
ATOM   6318 O OE1 . GLU B 1 265 ? -54.892 24.790 36.977  1.00 43.66 ? 265 GLU B OE1 1 
ATOM   6319 O OE2 . GLU B 1 265 ? -55.293 25.447 39.024  1.00 40.85 ? 265 GLU B OE2 1 
ATOM   6320 N N   . LEU B 1 266 ? -49.755 23.471 35.542  1.00 17.11 ? 266 LEU B N   1 
ATOM   6321 C CA  . LEU B 1 266 ? -49.088 22.513 34.661  1.00 21.59 ? 266 LEU B CA  1 
ATOM   6322 C C   . LEU B 1 266 ? -47.703 22.147 35.196  1.00 20.91 ? 266 LEU B C   1 
ATOM   6323 O O   . LEU B 1 266 ? -47.351 20.964 35.283  1.00 23.04 ? 266 LEU B O   1 
ATOM   6324 C CB  . LEU B 1 266 ? -48.982 23.077 33.241  1.00 18.18 ? 266 LEU B CB  1 
ATOM   6325 C CG  . LEU B 1 266 ? -48.193 22.183 32.271  1.00 18.22 ? 266 LEU B CG  1 
ATOM   6326 C CD1 . LEU B 1 266 ? -48.869 20.826 32.162  1.00 19.73 ? 266 LEU B CD1 1 
ATOM   6327 C CD2 . LEU B 1 266 ? -47.999 22.804 30.888  1.00 18.41 ? 266 LEU B CD2 1 
ATOM   6328 N N   . TYR B 1 267 ? -46.899 23.153 35.562  1.00 16.14 ? 267 TYR B N   1 
ATOM   6329 C CA  . TYR B 1 267 ? -45.575 22.873 36.109  1.00 16.06 ? 267 TYR B CA  1 
ATOM   6330 C C   . TYR B 1 267 ? -45.666 21.979 37.342  1.00 21.58 ? 267 TYR B C   1 
ATOM   6331 O O   . TYR B 1 267 ? -44.912 21.004 37.470  1.00 18.55 ? 267 TYR B O   1 
ATOM   6332 C CB  . TYR B 1 267 ? -44.859 24.181 36.440  1.00 14.86 ? 267 TYR B CB  1 
ATOM   6333 C CG  . TYR B 1 267 ? -44.321 24.916 35.226  1.00 18.65 ? 267 TYR B CG  1 
ATOM   6334 C CD1 . TYR B 1 267 ? -43.282 24.386 34.469  1.00 17.25 ? 267 TYR B CD1 1 
ATOM   6335 C CD2 . TYR B 1 267 ? -44.840 26.153 34.850  1.00 14.73 ? 267 TYR B CD2 1 
ATOM   6336 C CE1 . TYR B 1 267 ? -42.770 25.067 33.360  1.00 16.77 ? 267 TYR B CE1 1 
ATOM   6337 C CE2 . TYR B 1 267 ? -44.339 26.842 33.737  1.00 15.32 ? 267 TYR B CE2 1 
ATOM   6338 C CZ  . TYR B 1 267 ? -43.312 26.296 33.001  1.00 20.22 ? 267 TYR B CZ  1 
ATOM   6339 O OH  . TYR B 1 267 ? -42.837 26.998 31.906  1.00 17.45 ? 267 TYR B OH  1 
ATOM   6340 N N   . TYR B 1 268 ? -46.601 22.279 38.248  1.00 17.47 ? 268 TYR B N   1 
ATOM   6341 C CA  . TYR B 1 268 ? -46.812 21.424 39.414  1.00 18.73 ? 268 TYR B CA  1 
ATOM   6342 C C   . TYR B 1 268 ? -47.138 19.994 38.998  1.00 21.69 ? 268 TYR B C   1 
ATOM   6343 O O   . TYR B 1 268 ? -46.594 19.029 39.551  1.00 21.12 ? 268 TYR B O   1 
ATOM   6344 C CB  . TYR B 1 268 ? -47.939 21.979 40.283  1.00 22.52 ? 268 TYR B CB  1 
ATOM   6345 C CG  . TYR B 1 268 ? -48.304 21.017 41.372  1.00 26.19 ? 268 TYR B CG  1 
ATOM   6346 C CD1 . TYR B 1 268 ? -47.426 20.787 42.422  1.00 28.50 ? 268 TYR B CD1 1 
ATOM   6347 C CD2 . TYR B 1 268 ? -49.497 20.304 41.336  1.00 27.91 ? 268 TYR B CD2 1 
ATOM   6348 C CE1 . TYR B 1 268 ? -47.723 19.887 43.422  1.00 34.04 ? 268 TYR B CE1 1 
ATOM   6349 C CE2 . TYR B 1 268 ? -49.810 19.390 42.344  1.00 35.88 ? 268 TYR B CE2 1 
ATOM   6350 C CZ  . TYR B 1 268 ? -48.912 19.196 43.386  1.00 33.94 ? 268 TYR B CZ  1 
ATOM   6351 O OH  . TYR B 1 268 ? -49.180 18.310 44.409  1.00 38.86 ? 268 TYR B OH  1 
ATOM   6352 N N   . GLU B 1 269 ? -48.046 19.839 38.033  1.00 20.42 ? 269 GLU B N   1 
ATOM   6353 C CA  . GLU B 1 269 ? -48.479 18.499 37.639  1.00 21.82 ? 269 GLU B CA  1 
ATOM   6354 C C   . GLU B 1 269 ? -47.337 17.704 37.029  1.00 22.06 ? 269 GLU B C   1 
ATOM   6355 O O   . GLU B 1 269 ? -47.347 16.469 37.075  1.00 23.52 ? 269 GLU B O   1 
ATOM   6356 C CB  . GLU B 1 269 ? -49.633 18.583 36.642  1.00 22.04 ? 269 GLU B CB  1 
ATOM   6357 C CG  . GLU B 1 269 ? -50.951 18.996 37.244  1.00 30.24 ? 269 GLU B CG  1 
ATOM   6358 C CD  . GLU B 1 269 ? -51.475 17.973 38.233  1.00 40.65 ? 269 GLU B CD  1 
ATOM   6359 O OE1 . GLU B 1 269 ? -51.198 16.769 38.052  1.00 42.37 ? 269 GLU B OE1 1 
ATOM   6360 O OE2 . GLU B 1 269 ? -52.164 18.381 39.191  1.00 39.68 ? 269 GLU B OE2 1 
ATOM   6361 N N   . LYS B 1 270 ? -46.351 18.387 36.458  1.00 21.47 ? 270 LYS B N   1 
ATOM   6362 C CA  . LYS B 1 270 ? -45.191 17.740 35.861  1.00 25.97 ? 270 LYS B CA  1 
ATOM   6363 C C   . LYS B 1 270 ? -44.018 17.612 36.829  1.00 23.95 ? 270 LYS B C   1 
ATOM   6364 O O   . LYS B 1 270 ? -42.902 17.294 36.401  1.00 24.78 ? 270 LYS B O   1 
ATOM   6365 C CB  . LYS B 1 270 ? -44.762 18.506 34.605  1.00 23.58 ? 270 LYS B CB  1 
ATOM   6366 C CG  . LYS B 1 270 ? -45.858 18.548 33.537  1.00 22.38 ? 270 LYS B CG  1 
ATOM   6367 C CD  . LYS B 1 270 ? -46.277 17.137 33.146  1.00 31.78 ? 270 LYS B CD  1 
ATOM   6368 C CE  . LYS B 1 270 ? -47.375 17.129 32.087  1.00 39.04 ? 270 LYS B CE  1 
ATOM   6369 N NZ  . LYS B 1 270 ? -47.913 15.752 31.811  1.00 43.59 ? 270 LYS B NZ  1 
ATOM   6370 N N   . GLY B 1 271 ? -44.241 17.851 38.117  1.00 23.28 ? 271 GLY B N   1 
ATOM   6371 C CA  . GLY B 1 271 ? -43.231 17.603 39.122  1.00 21.63 ? 271 GLY B CA  1 
ATOM   6372 C C   . GLY B 1 271 ? -42.277 18.742 39.374  1.00 24.17 ? 271 GLY B C   1 
ATOM   6373 O O   . GLY B 1 271 ? -41.256 18.529 40.039  1.00 21.82 ? 271 GLY B O   1 
ATOM   6374 N N   . ILE B 1 272 ? -42.564 19.935 38.856  1.00 18.95 ? 272 ILE B N   1 
ATOM   6375 C CA  . ILE B 1 272 ? -41.734 21.110 39.115  1.00 17.81 ? 272 ILE B CA  1 
ATOM   6376 C C   . ILE B 1 272 ? -42.132 21.684 40.469  1.00 21.55 ? 272 ILE B C   1 
ATOM   6377 O O   . ILE B 1 272 ? -43.292 22.051 40.679  1.00 23.96 ? 272 ILE B O   1 
ATOM   6378 C CB  . ILE B 1 272 ? -41.886 22.163 38.003  1.00 20.25 ? 272 ILE B CB  1 
ATOM   6379 C CG1 . ILE B 1 272 ? -41.635 21.544 36.621  1.00 26.35 ? 272 ILE B CG1 1 
ATOM   6380 C CG2 . ILE B 1 272 ? -41.002 23.384 38.279  1.00 20.51 ? 272 ILE B CG2 1 
ATOM   6381 C CD1 . ILE B 1 272 ? -40.362 20.758 36.514  1.00 33.76 ? 272 ILE B CD1 1 
ATOM   6382 N N   . ASN B 1 273 ? -41.174 21.748 41.397  1.00 19.54 ? 273 ASN B N   1 
ATOM   6383 C CA  . ASN B 1 273 ? -41.449 22.227 42.743  1.00 24.30 ? 273 ASN B CA  1 
ATOM   6384 C C   . ASN B 1 273 ? -41.133 23.701 42.932  1.00 20.20 ? 273 ASN B C   1 
ATOM   6385 O O   . ASN B 1 273 ? -41.553 24.284 43.940  1.00 20.03 ? 273 ASN B O   1 
ATOM   6386 C CB  . ASN B 1 273 ? -40.649 21.422 43.776  1.00 27.18 ? 273 ASN B CB  1 
ATOM   6387 C CG  . ASN B 1 273 ? -41.130 19.996 43.907  1.00 38.28 ? 273 ASN B CG  1 
ATOM   6388 O OD1 . ASN B 1 273 ? -42.327 19.718 43.800  1.00 38.03 ? 273 ASN B OD1 1 
ATOM   6389 N ND2 . ASN B 1 273 ? -40.202 19.082 44.157  1.00 40.88 ? 273 ASN B ND2 1 
ATOM   6390 N N   A MET B 1 274 ? -40.386 24.314 42.014  0.61 18.66 ? 274 MET B N   1 
ATOM   6391 N N   B MET B 1 274 ? -40.417 24.317 41.995  0.39 18.63 ? 274 MET B N   1 
ATOM   6392 C CA  A MET B 1 274 ? -39.985 25.706 42.165  0.61 16.14 ? 274 MET B CA  1 
ATOM   6393 C CA  B MET B 1 274 ? -40.020 25.701 42.159  0.39 16.40 ? 274 MET B CA  1 
ATOM   6394 C C   A MET B 1 274 ? -39.743 26.324 40.796  0.61 15.93 ? 274 MET B C   1 
ATOM   6395 C C   B MET B 1 274 ? -39.753 26.320 40.797  0.39 15.91 ? 274 MET B C   1 
ATOM   6396 O O   A MET B 1 274 ? -39.190 25.678 39.903  0.61 16.64 ? 274 MET B O   1 
ATOM   6397 O O   B MET B 1 274 ? -39.212 25.666 39.904  0.39 16.72 ? 274 MET B O   1 
ATOM   6398 C CB  A MET B 1 274 ? -38.712 25.847 43.014  0.61 17.32 ? 274 MET B CB  1 
ATOM   6399 C CB  B MET B 1 274 ? -38.775 25.813 43.044  0.39 17.39 ? 274 MET B CB  1 
ATOM   6400 C CG  A MET B 1 274 ? -38.318 27.298 43.299  0.61 17.03 ? 274 MET B CG  1 
ATOM   6401 C CG  B MET B 1 274 ? -38.372 27.236 43.343  0.39 17.73 ? 274 MET B CG  1 
ATOM   6402 S SD  A MET B 1 274 ? -37.270 28.088 42.041  0.61 17.59 ? 274 MET B SD  1 
ATOM   6403 S SD  B MET B 1 274 ? -36.726 27.331 44.050  0.39 24.75 ? 274 MET B SD  1 
ATOM   6404 C CE  A MET B 1 274 ? -35.661 27.509 42.579  0.61 21.68 ? 274 MET B CE  1 
ATOM   6405 C CE  B MET B 1 274 ? -35.727 27.505 42.576  0.39 21.63 ? 274 MET B CE  1 
ATOM   6406 N N   . LEU B 1 275 ? -40.149 27.578 40.642  1.00 13.46 ? 275 LEU B N   1 
ATOM   6407 C CA  . LEU B 1 275 ? -39.737 28.377 39.499  1.00 13.26 ? 275 LEU B CA  1 
ATOM   6408 C C   . LEU B 1 275 ? -39.539 29.807 39.968  1.00 17.08 ? 275 LEU B C   1 
ATOM   6409 O O   . LEU B 1 275 ? -39.827 30.155 41.114  1.00 14.16 ? 275 LEU B O   1 
ATOM   6410 C CB  . LEU B 1 275 ? -40.739 28.311 38.349  1.00 18.95 ? 275 LEU B CB  1 
ATOM   6411 C CG  . LEU B 1 275 ? -42.219 28.504 38.648  1.00 19.53 ? 275 LEU B CG  1 
ATOM   6412 C CD1 . LEU B 1 275 ? -42.600 29.990 38.763  1.00 26.00 ? 275 LEU B CD1 1 
ATOM   6413 C CD2 . LEU B 1 275 ? -42.994 27.835 37.541  1.00 20.90 ? 275 LEU B CD2 1 
ATOM   6414 N N   . ALA B 1 276 ? -39.006 30.628 39.078  1.00 12.82 ? 276 ALA B N   1 
ATOM   6415 C CA  . ALA B 1 276 ? -38.944 32.056 39.322  1.00 12.10 ? 276 ALA B CA  1 
ATOM   6416 C C   . ALA B 1 276 ? -39.697 32.778 38.222  1.00 12.20 ? 276 ALA B C   1 
ATOM   6417 O O   . ALA B 1 276 ? -39.888 32.255 37.119  1.00 16.42 ? 276 ALA B O   1 
ATOM   6418 C CB  . ALA B 1 276 ? -37.500 32.578 39.377  1.00 12.96 ? 276 ALA B CB  1 
ATOM   6419 N N   . THR B 1 277 ? -40.121 33.994 38.529  1.00 9.84  ? 277 THR B N   1 
ATOM   6420 C CA  . THR B 1 277 ? -40.766 34.822 37.526  1.00 10.42 ? 277 THR B CA  1 
ATOM   6421 C C   . THR B 1 277 ? -40.416 36.266 37.862  1.00 14.21 ? 277 THR B C   1 
ATOM   6422 O O   . THR B 1 277 ? -39.429 36.528 38.557  1.00 13.58 ? 277 THR B O   1 
ATOM   6423 C CB  . THR B 1 277 ? -42.278 34.531 37.456  1.00 14.42 ? 277 THR B CB  1 
ATOM   6424 O OG1 . THR B 1 277 ? -42.900 35.393 36.492  1.00 15.35 ? 277 THR B OG1 1 
ATOM   6425 C CG2 . THR B 1 277 ? -42.945 34.704 38.824  1.00 15.58 ? 277 THR B CG2 1 
ATOM   6426 N N   . ASP B 1 278 ? -41.192 37.207 37.346  1.00 13.93 ? 278 ASP B N   1 
ATOM   6427 C CA  . ASP B 1 278 ? -40.770 38.598 37.373  1.00 15.60 ? 278 ASP B CA  1 
ATOM   6428 C C   . ASP B 1 278 ? -41.504 39.430 38.425  1.00 16.87 ? 278 ASP B C   1 
ATOM   6429 O O   . ASP B 1 278 ? -42.655 39.166 38.768  1.00 14.83 ? 278 ASP B O   1 
ATOM   6430 C CB  . ASP B 1 278 ? -40.971 39.226 36.008  1.00 15.18 ? 278 ASP B CB  1 
ATOM   6431 C CG  . ASP B 1 278 ? -40.457 40.635 35.959  1.00 24.72 ? 278 ASP B CG  1 
ATOM   6432 O OD1 . ASP B 1 278 ? -39.250 40.840 36.264  1.00 19.03 ? 278 ASP B OD1 1 
ATOM   6433 O OD2 . ASP B 1 278 ? -41.259 41.521 35.607  1.00 20.85 ? 278 ASP B OD2 1 
ATOM   6434 N N   . GLU B 1 279 ? -40.828 40.494 38.875  1.00 16.73 ? 279 GLU B N   1 
ATOM   6435 C CA  . GLU B 1 279 ? -41.380 41.395 39.880  1.00 17.21 ? 279 GLU B CA  1 
ATOM   6436 C C   . GLU B 1 279 ? -42.618 42.153 39.392  1.00 16.39 ? 279 GLU B C   1 
ATOM   6437 O O   . GLU B 1 279 ? -43.501 42.469 40.194  1.00 17.30 ? 279 GLU B O   1 
ATOM   6438 C CB  . GLU B 1 279 ? -40.297 42.384 40.312  1.00 18.20 ? 279 GLU B CB  1 
ATOM   6439 C CG  . GLU B 1 279 ? -40.683 43.195 41.521  1.00 20.27 ? 279 GLU B CG  1 
ATOM   6440 C CD  . GLU B 1 279 ? -39.546 44.037 42.066  1.00 27.40 ? 279 GLU B CD  1 
ATOM   6441 O OE1 . GLU B 1 279 ? -38.426 43.999 41.507  1.00 24.87 ? 279 GLU B OE1 1 
ATOM   6442 O OE2 . GLU B 1 279 ? -39.791 44.759 43.056  1.00 29.06 ? 279 GLU B OE2 1 
ATOM   6443 N N   . VAL B 1 280 ? -42.715 42.464 38.099  1.00 17.25 ? 280 VAL B N   1 
ATOM   6444 C CA  . VAL B 1 280 ? -43.925 43.146 37.639  1.00 17.24 ? 280 VAL B CA  1 
ATOM   6445 C C   . VAL B 1 280 ? -45.131 42.228 37.792  1.00 17.43 ? 280 VAL B C   1 
ATOM   6446 O O   . VAL B 1 280 ? -46.233 42.673 38.136  1.00 20.25 ? 280 VAL B O   1 
ATOM   6447 C CB  . VAL B 1 280 ? -43.758 43.638 36.190  1.00 25.03 ? 280 VAL B CB  1 
ATOM   6448 C CG1 . VAL B 1 280 ? -45.062 44.229 35.670  1.00 18.86 ? 280 VAL B CG1 1 
ATOM   6449 C CG2 . VAL B 1 280 ? -42.662 44.677 36.126  1.00 26.95 ? 280 VAL B CG2 1 
ATOM   6450 N N   . ILE B 1 281 ? -44.936 40.927 37.573  1.00 18.87 ? 281 ILE B N   1 
ATOM   6451 C CA  . ILE B 1 281 ? -46.023 39.975 37.776  1.00 19.40 ? 281 ILE B CA  1 
ATOM   6452 C C   . ILE B 1 281 ? -46.417 39.933 39.247  1.00 18.68 ? 281 ILE B C   1 
ATOM   6453 O O   . ILE B 1 281 ? -47.611 39.901 39.587  1.00 19.29 ? 281 ILE B O   1 
ATOM   6454 C CB  . ILE B 1 281 ? -45.620 38.591 37.230  1.00 15.91 ? 281 ILE B CB  1 
ATOM   6455 C CG1 . ILE B 1 281 ? -45.511 38.670 35.701  1.00 20.26 ? 281 ILE B CG1 1 
ATOM   6456 C CG2 . ILE B 1 281 ? -46.621 37.506 37.651  1.00 19.11 ? 281 ILE B CG2 1 
ATOM   6457 C CD1 . ILE B 1 281 ? -45.003 37.412 35.032  1.00 21.10 ? 281 ILE B CD1 1 
ATOM   6458 N N   . LEU B 1 282 ? -45.427 39.975 40.143  1.00 18.13 ? 282 LEU B N   1 
ATOM   6459 C CA  . LEU B 1 282 ? -45.715 40.042 41.573  1.00 19.90 ? 282 LEU B CA  1 
ATOM   6460 C C   . LEU B 1 282 ? -46.568 41.256 41.904  1.00 21.26 ? 282 LEU B C   1 
ATOM   6461 O O   . LEU B 1 282 ? -47.600 41.138 42.574  1.00 22.82 ? 282 LEU B O   1 
ATOM   6462 C CB  . LEU B 1 282 ? -44.416 40.080 42.377  1.00 20.70 ? 282 LEU B CB  1 
ATOM   6463 C CG  . LEU B 1 282 ? -44.572 40.097 43.905  1.00 24.30 ? 282 LEU B CG  1 
ATOM   6464 C CD1 . LEU B 1 282 ? -45.256 38.831 44.405  1.00 25.80 ? 282 LEU B CD1 1 
ATOM   6465 C CD2 . LEU B 1 282 ? -43.207 40.265 44.557  1.00 22.76 ? 282 LEU B CD2 1 
ATOM   6466 N N   . LYS B 1 283 ? -46.143 42.438 41.443  1.00 22.74 ? 283 LYS B N   1 
ATOM   6467 C CA  . LYS B 1 283 ? -46.861 43.674 41.750  1.00 22.56 ? 283 LYS B CA  1 
ATOM   6468 C C   . LYS B 1 283 ? -48.271 43.662 41.165  1.00 24.62 ? 283 LYS B C   1 
ATOM   6469 O O   . LYS B 1 283 ? -49.204 44.214 41.763  1.00 27.32 ? 283 LYS B O   1 
ATOM   6470 C CB  . LYS B 1 283 ? -46.073 44.874 41.220  1.00 23.50 ? 283 LYS B CB  1 
ATOM   6471 C CG  . LYS B 1 283 ? -44.663 45.028 41.783  1.00 35.15 ? 283 LYS B CG  1 
ATOM   6472 C CD  . LYS B 1 283 ? -44.661 45.740 43.115  1.00 45.83 ? 283 LYS B CD  1 
ATOM   6473 C CE  . LYS B 1 283 ? -43.239 46.088 43.545  1.00 47.09 ? 283 LYS B CE  1 
ATOM   6474 N NZ  . LYS B 1 283 ? -42.496 44.893 44.028  1.00 38.99 ? 283 LYS B NZ  1 
ATOM   6475 N N   . ASN B 1 284 ? -48.449 43.046 39.990  1.00 21.95 ? 284 ASN B N   1 
ATOM   6476 C CA  . ASN B 1 284 ? -49.788 42.941 39.416  1.00 23.62 ? 284 ASN B CA  1 
ATOM   6477 C C   . ASN B 1 284 ? -50.679 41.979 40.187  1.00 27.88 ? 284 ASN B C   1 
ATOM   6478 O O   . ASN B 1 284 ? -51.903 42.034 40.032  1.00 30.01 ? 284 ASN B O   1 
ATOM   6479 C CB  . ASN B 1 284 ? -49.744 42.460 37.962  1.00 20.93 ? 284 ASN B CB  1 
ATOM   6480 C CG  . ASN B 1 284 ? -49.168 43.478 37.021  1.00 28.04 ? 284 ASN B CG  1 
ATOM   6481 O OD1 . ASN B 1 284 ? -49.205 44.679 37.285  1.00 27.00 ? 284 ASN B OD1 1 
ATOM   6482 N ND2 . ASN B 1 284 ? -48.677 43.007 35.875  1.00 26.51 ? 284 ASN B ND2 1 
ATOM   6483 N N   . SER B 1 285 ? -50.098 41.083 40.980  1.00 27.09 ? 285 SER B N   1 
ATOM   6484 C CA  . SER B 1 285 ? -50.831 39.943 41.521  1.00 30.76 ? 285 SER B CA  1 
ATOM   6485 C C   . SER B 1 285 ? -51.134 40.044 43.008  1.00 37.98 ? 285 SER B C   1 
ATOM   6486 O O   . SER B 1 285 ? -52.219 39.642 43.437  1.00 36.30 ? 285 SER B O   1 
ATOM   6487 C CB  . SER B 1 285 ? -50.052 38.659 41.263  1.00 26.36 ? 285 SER B CB  1 
ATOM   6488 O OG  . SER B 1 285 ? -49.811 38.504 39.879  1.00 24.55 ? 285 SER B OG  1 
ATOM   6489 N N   . VAL B 1 286 ? -50.194 40.538 43.818  1.00 38.07 ? 286 VAL B N   1 
ATOM   6490 C CA  . VAL B 1 286 ? -50.390 40.611 45.260  1.00 42.23 ? 286 VAL B CA  1 
ATOM   6491 C C   . VAL B 1 286 ? -50.117 42.031 45.732  1.00 44.37 ? 286 VAL B C   1 
ATOM   6492 O O   . VAL B 1 286 ? -49.381 42.798 45.104  1.00 43.52 ? 286 VAL B O   1 
ATOM   6493 C CB  . VAL B 1 286 ? -49.505 39.614 46.043  1.00 48.56 ? 286 VAL B CB  1 
ATOM   6494 C CG1 . VAL B 1 286 ? -49.552 38.227 45.417  1.00 47.74 ? 286 VAL B CG1 1 
ATOM   6495 C CG2 . VAL B 1 286 ? -48.084 40.125 46.157  1.00 49.43 ? 286 VAL B CG2 1 
ATOM   6496 N N   . GLU B 1 287 ? -50.708 42.360 46.882  1.00 40.80 ? 287 GLU B N   1 
ATOM   6497 C CA  . GLU B 1 287 ? -50.661 43.723 47.398  1.00 46.70 ? 287 GLU B CA  1 
ATOM   6498 C C   . GLU B 1 287 ? -49.313 44.050 48.027  1.00 46.73 ? 287 GLU B C   1 
ATOM   6499 O O   . GLU B 1 287 ? -48.628 44.986 47.602  1.00 46.31 ? 287 GLU B O   1 
ATOM   6500 C CB  . GLU B 1 287 ? -51.771 43.919 48.420  1.00 44.11 ? 287 GLU B CB  1 
ATOM   6501 C CG  . GLU B 1 287 ? -53.101 43.837 47.791  1.00 51.24 ? 287 GLU B CG  1 
ATOM   6502 C CD  . GLU B 1 287 ? -54.192 44.144 48.755  1.00 60.20 ? 287 GLU B CD  1 
ATOM   6503 O OE1 . GLU B 1 287 ? -53.917 44.273 49.972  1.00 60.31 ? 287 GLU B OE1 1 
ATOM   6504 O OE2 . GLU B 1 287 ? -55.325 44.272 48.272  1.00 67.06 ? 287 GLU B OE2 1 
ATOM   6505 N N   . ARG B 1 288 ? -48.937 43.299 49.062  1.00 44.41 ? 288 ARG B N   1 
ATOM   6506 C CA  . ARG B 1 288 ? -47.677 43.514 49.764  1.00 49.33 ? 288 ARG B CA  1 
ATOM   6507 C C   . ARG B 1 288 ? -46.599 42.766 48.981  1.00 47.84 ? 288 ARG B C   1 
ATOM   6508 O O   . ARG B 1 288 ? -46.144 41.676 49.333  1.00 54.38 ? 288 ARG B O   1 
ATOM   6509 C CB  . ARG B 1 288 ? -47.801 43.083 51.221  1.00 53.03 ? 288 ARG B CB  1 
ATOM   6510 C CG  . ARG B 1 288 ? -48.817 43.963 51.956  1.00 52.56 ? 288 ARG B CG  1 
ATOM   6511 C CD  . ARG B 1 288 ? -48.774 43.879 53.477  1.00 51.50 ? 288 ARG B CD  1 
ATOM   6512 N NE  . ARG B 1 288 ? -49.504 42.724 53.992  1.00 57.42 ? 288 ARG B NE  1 
ATOM   6513 C CZ  . ARG B 1 288 ? -50.758 42.755 54.445  1.00 54.44 ? 288 ARG B CZ  1 
ATOM   6514 N NH1 . ARG B 1 288 ? -51.313 41.641 54.896  1.00 54.30 ? 288 ARG B NH1 1 
ATOM   6515 N NH2 . ARG B 1 288 ? -51.452 43.890 54.462  1.00 40.99 ? 288 ARG B NH2 1 
ATOM   6516 N N   . ALA B 1 289 ? -46.207 43.379 47.869  1.00 35.34 ? 289 ALA B N   1 
ATOM   6517 C CA  . ALA B 1 289 ? -45.377 42.731 46.865  1.00 40.85 ? 289 ALA B CA  1 
ATOM   6518 C C   . ALA B 1 289 ? -43.897 42.872 47.222  1.00 37.68 ? 289 ALA B C   1 
ATOM   6519 O O   . ALA B 1 289 ? -43.150 43.641 46.618  1.00 44.78 ? 289 ALA B O   1 
ATOM   6520 C CB  . ALA B 1 289 ? -45.672 43.320 45.491  1.00 42.86 ? 289 ALA B CB  1 
ATOM   6521 N N   . SER B 1 290 ? -43.462 42.099 48.220  1.00 26.76 ? 290 SER B N   1 
ATOM   6522 C CA  . SER B 1 290 ? -42.029 42.011 48.492  1.00 27.75 ? 290 SER B CA  1 
ATOM   6523 C C   . SER B 1 290 ? -41.418 40.890 47.665  1.00 21.99 ? 290 SER B C   1 
ATOM   6524 O O   . SER B 1 290 ? -41.833 39.733 47.815  1.00 19.35 ? 290 SER B O   1 
ATOM   6525 C CB  . SER B 1 290 ? -41.744 41.760 49.959  1.00 26.01 ? 290 SER B CB  1 
ATOM   6526 O OG  . SER B 1 290 ? -40.359 41.482 50.129  1.00 26.16 ? 290 SER B OG  1 
ATOM   6527 N N   . PRO B 1 291 ? -40.434 41.167 46.808  1.00 22.11 ? 291 PRO B N   1 
ATOM   6528 C CA  . PRO B 1 291 ? -39.786 40.092 46.052  1.00 22.00 ? 291 PRO B CA  1 
ATOM   6529 C C   . PRO B 1 291 ? -38.753 39.308 46.842  1.00 19.91 ? 291 PRO B C   1 
ATOM   6530 O O   . PRO B 1 291 ? -38.051 38.489 46.249  1.00 19.86 ? 291 PRO B O   1 
ATOM   6531 C CB  . PRO B 1 291 ? -39.121 40.853 44.895  1.00 22.25 ? 291 PRO B CB  1 
ATOM   6532 C CG  . PRO B 1 291 ? -38.746 42.178 45.517  1.00 20.50 ? 291 PRO B CG  1 
ATOM   6533 C CD  . PRO B 1 291 ? -39.867 42.493 46.489  1.00 21.62 ? 291 PRO B CD  1 
ATOM   6534 N N   . TYR B 1 292 ? -38.628 39.517 48.153  1.00 17.91 ? 292 TYR B N   1 
ATOM   6535 C CA  . TYR B 1 292 ? -37.558 38.890 48.915  1.00 17.92 ? 292 TYR B CA  1 
ATOM   6536 C C   . TYR B 1 292 ? -38.029 37.695 49.732  1.00 18.21 ? 292 TYR B C   1 
ATOM   6537 O O   . TYR B 1 292 ? -37.290 37.229 50.601  1.00 18.59 ? 292 TYR B O   1 
ATOM   6538 C CB  . TYR B 1 292 ? -36.878 39.937 49.812  1.00 18.89 ? 292 TYR B CB  1 
ATOM   6539 C CG  . TYR B 1 292 ? -36.435 41.119 48.984  1.00 23.77 ? 292 TYR B CG  1 
ATOM   6540 C CD1 . TYR B 1 292 ? -35.595 40.932 47.892  1.00 25.10 ? 292 TYR B CD1 1 
ATOM   6541 C CD2 . TYR B 1 292 ? -36.867 42.410 49.268  1.00 23.81 ? 292 TYR B CD2 1 
ATOM   6542 C CE1 . TYR B 1 292 ? -35.190 41.994 47.103  1.00 26.59 ? 292 TYR B CE1 1 
ATOM   6543 C CE2 . TYR B 1 292 ? -36.459 43.492 48.479  1.00 27.59 ? 292 TYR B CE2 1 
ATOM   6544 C CZ  . TYR B 1 292 ? -35.619 43.275 47.405  1.00 28.51 ? 292 TYR B CZ  1 
ATOM   6545 O OH  . TYR B 1 292 ? -35.220 44.327 46.610  1.00 29.46 ? 292 TYR B OH  1 
ATOM   6546 N N   . LEU B 1 293 ? -39.222 37.180 49.455  1.00 18.12 ? 293 LEU B N   1 
ATOM   6547 C CA  . LEU B 1 293 ? -39.788 36.026 50.136  1.00 19.54 ? 293 LEU B CA  1 
ATOM   6548 C C   . LEU B 1 293 ? -39.794 34.821 49.204  1.00 18.90 ? 293 LEU B C   1 
ATOM   6549 O O   . LEU B 1 293 ? -39.778 34.963 47.978  1.00 17.95 ? 293 LEU B O   1 
ATOM   6550 C CB  . LEU B 1 293 ? -41.226 36.312 50.596  1.00 21.94 ? 293 LEU B CB  1 
ATOM   6551 C CG  . LEU B 1 293 ? -41.452 37.123 51.878  1.00 34.73 ? 293 LEU B CG  1 
ATOM   6552 C CD1 . LEU B 1 293 ? -40.928 38.538 51.763  1.00 38.30 ? 293 LEU B CD1 1 
ATOM   6553 C CD2 . LEU B 1 293 ? -42.937 37.142 52.244  1.00 40.04 ? 293 LEU B CD2 1 
ATOM   6554 N N   . ARG B 1 294 ? -39.836 33.624 49.790  1.00 19.37 ? 294 ARG B N   1 
ATOM   6555 C CA  . ARG B 1 294 ? -40.219 32.436 49.034  1.00 18.15 ? 294 ARG B CA  1 
ATOM   6556 C C   . ARG B 1 294 ? -41.743 32.344 49.065  1.00 17.68 ? 294 ARG B C   1 
ATOM   6557 O O   . ARG B 1 294 ? -42.342 32.285 50.145  1.00 21.20 ? 294 ARG B O   1 
ATOM   6558 C CB  . ARG B 1 294 ? -39.591 31.159 49.599  1.00 16.89 ? 294 ARG B CB  1 
ATOM   6559 C CG  . ARG B 1 294 ? -39.961 29.905 48.810  1.00 18.03 ? 294 ARG B CG  1 
ATOM   6560 C CD  . ARG B 1 294 ? -39.144 28.673 49.207  1.00 17.67 ? 294 ARG B CD  1 
ATOM   6561 N NE  . ARG B 1 294 ? -39.289 28.314 50.611  1.00 20.65 ? 294 ARG B NE  1 
ATOM   6562 C CZ  . ARG B 1 294 ? -38.271 28.160 51.456  1.00 21.99 ? 294 ARG B CZ  1 
ATOM   6563 N NH1 . ARG B 1 294 ? -37.019 28.317 51.038  1.00 21.02 ? 294 ARG B NH1 1 
ATOM   6564 N NH2 . ARG B 1 294 ? -38.505 27.834 52.723  1.00 26.72 ? 294 ARG B NH2 1 
ATOM   6565 N N   . TYR B 1 295 ? -42.374 32.367 47.897  1.00 16.71 ? 295 TYR B N   1 
ATOM   6566 C CA  . TYR B 1 295 ? -43.823 32.267 47.850  1.00 16.98 ? 295 TYR B CA  1 
ATOM   6567 C C   . TYR B 1 295 ? -44.240 30.837 47.536  1.00 18.12 ? 295 TYR B C   1 
ATOM   6568 O O   . TYR B 1 295 ? -43.514 30.098 46.872  1.00 16.17 ? 295 TYR B O   1 
ATOM   6569 C CB  . TYR B 1 295 ? -44.424 33.214 46.806  1.00 16.79 ? 295 TYR B CB  1 
ATOM   6570 C CG  . TYR B 1 295 ? -44.311 34.685 47.178  1.00 17.44 ? 295 TYR B CG  1 
ATOM   6571 C CD1 . TYR B 1 295 ? -43.164 35.438 46.899  1.00 17.05 ? 295 TYR B CD1 1 
ATOM   6572 C CD2 . TYR B 1 295 ? -45.341 35.312 47.859  1.00 23.02 ? 295 TYR B CD2 1 
ATOM   6573 C CE1 . TYR B 1 295 ? -43.089 36.789 47.261  1.00 20.21 ? 295 TYR B CE1 1 
ATOM   6574 C CE2 . TYR B 1 295 ? -45.275 36.624 48.221  1.00 21.78 ? 295 TYR B CE2 1 
ATOM   6575 C CZ  . TYR B 1 295 ? -44.157 37.369 47.927  1.00 21.07 ? 295 TYR B CZ  1 
ATOM   6576 O OH  . TYR B 1 295 ? -44.157 38.692 48.332  1.00 20.05 ? 295 TYR B OH  1 
ATOM   6577 N N   . TYR B 1 296 ? -45.420 30.446 48.033  1.00 17.54 ? 296 TYR B N   1 
ATOM   6578 C CA  . TYR B 1 296 ? -46.009 29.159 47.695  1.00 19.49 ? 296 TYR B CA  1 
ATOM   6579 C C   . TYR B 1 296 ? -47.311 29.432 46.954  1.00 17.23 ? 296 TYR B C   1 
ATOM   6580 O O   . TYR B 1 296 ? -48.286 29.910 47.548  1.00 18.94 ? 296 TYR B O   1 
ATOM   6581 C CB  . TYR B 1 296 ? -46.258 28.292 48.933  1.00 19.95 ? 296 TYR B CB  1 
ATOM   6582 C CG  . TYR B 1 296 ? -45.032 28.045 49.780  1.00 19.35 ? 296 TYR B CG  1 
ATOM   6583 C CD1 . TYR B 1 296 ? -43.901 27.451 49.236  1.00 20.24 ? 296 TYR B CD1 1 
ATOM   6584 C CD2 . TYR B 1 296 ? -45.013 28.374 51.129  1.00 23.27 ? 296 TYR B CD2 1 
ATOM   6585 C CE1 . TYR B 1 296 ? -42.772 27.217 50.011  1.00 18.01 ? 296 TYR B CE1 1 
ATOM   6586 C CE2 . TYR B 1 296 ? -43.892 28.136 51.912  1.00 22.28 ? 296 TYR B CE2 1 
ATOM   6587 C CZ  . TYR B 1 296 ? -42.776 27.558 51.341  1.00 22.91 ? 296 TYR B CZ  1 
ATOM   6588 O OH  . TYR B 1 296 ? -41.660 27.319 52.104  1.00 26.05 ? 296 TYR B OH  1 
ATOM   6589 N N   . PHE B 1 297 ? -47.327 29.144 45.660  1.00 16.81 ? 297 PHE B N   1 
ATOM   6590 C CA  . PHE B 1 297 ? -48.552 29.316 44.887  1.00 16.68 ? 297 PHE B CA  1 
ATOM   6591 C C   . PHE B 1 297 ? -49.506 28.184 45.233  1.00 17.64 ? 297 PHE B C   1 
ATOM   6592 O O   . PHE B 1 297 ? -49.241 27.027 44.898  1.00 19.55 ? 297 PHE B O   1 
ATOM   6593 C CB  . PHE B 1 297 ? -48.258 29.351 43.388  1.00 17.71 ? 297 PHE B CB  1 
ATOM   6594 C CG  . PHE B 1 297 ? -49.499 29.432 42.535  1.00 18.74 ? 297 PHE B CG  1 
ATOM   6595 C CD1 . PHE B 1 297 ? -50.181 30.630 42.393  1.00 16.78 ? 297 PHE B CD1 1 
ATOM   6596 C CD2 . PHE B 1 297 ? -49.996 28.305 41.898  1.00 17.78 ? 297 PHE B CD2 1 
ATOM   6597 C CE1 . PHE B 1 297 ? -51.320 30.707 41.598  1.00 17.22 ? 297 PHE B CE1 1 
ATOM   6598 C CE2 . PHE B 1 297 ? -51.129 28.372 41.107  1.00 17.33 ? 297 PHE B CE2 1 
ATOM   6599 C CZ  . PHE B 1 297 ? -51.792 29.575 40.950  1.00 22.60 ? 297 PHE B CZ  1 
ATOM   6600 N N   . ARG B 1 298 ? -50.596 28.525 45.930  1.00 18.14 ? 298 ARG B N   1 
ATOM   6601 C CA  . ARG B 1 298 ? -51.650 27.589 46.318  1.00 18.77 ? 298 ARG B CA  1 
ATOM   6602 C C   . ARG B 1 298 ? -51.096 26.415 47.122  1.00 22.64 ? 298 ARG B C   1 
ATOM   6603 O O   . ARG B 1 298 ? -51.645 25.307 47.084  1.00 22.22 ? 298 ARG B O   1 
ATOM   6604 C CB  . ARG B 1 298 ? -52.442 27.100 45.095  1.00 22.91 ? 298 ARG B CB  1 
ATOM   6605 C CG  . ARG B 1 298 ? -53.214 28.249 44.434  1.00 20.40 ? 298 ARG B CG  1 
ATOM   6606 C CD  . ARG B 1 298 ? -54.040 27.857 43.221  1.00 20.28 ? 298 ARG B CD  1 
ATOM   6607 N NE  . ARG B 1 298 ? -54.611 29.066 42.627  1.00 20.80 ? 298 ARG B NE  1 
ATOM   6608 C CZ  . ARG B 1 298 ? -55.229 29.131 41.455  1.00 24.61 ? 298 ARG B CZ  1 
ATOM   6609 N NH1 . ARG B 1 298 ? -55.384 28.040 40.718  1.00 23.55 ? 298 ARG B NH1 1 
ATOM   6610 N NH2 . ARG B 1 298 ? -55.680 30.305 41.017  1.00 21.88 ? 298 ARG B NH2 1 
ATOM   6611 N N   . GLU B 1 299 ? -50.016 26.679 47.866  1.00 20.39 ? 299 GLU B N   1 
ATOM   6612 C CA  . GLU B 1 299 ? -49.321 25.701 48.701  1.00 24.05 ? 299 GLU B CA  1 
ATOM   6613 C C   . GLU B 1 299 ? -48.827 24.501 47.902  1.00 25.21 ? 299 GLU B C   1 
ATOM   6614 O O   . GLU B 1 299 ? -48.645 23.416 48.471  1.00 24.56 ? 299 GLU B O   1 
ATOM   6615 C CB  . GLU B 1 299 ? -50.211 25.219 49.860  1.00 23.83 ? 299 GLU B CB  1 
ATOM   6616 C CG  . GLU B 1 299 ? -50.423 26.184 51.017  1.00 41.17 ? 299 GLU B CG  1 
ATOM   6617 C CD  . GLU B 1 299 ? -49.164 26.486 51.828  1.00 48.94 ? 299 GLU B CD  1 
ATOM   6618 O OE1 . GLU B 1 299 ? -48.052 26.016 51.483  1.00 41.04 ? 299 GLU B OE1 1 
ATOM   6619 O OE2 . GLU B 1 299 ? -49.308 27.150 52.876  1.00 51.62 ? 299 GLU B OE2 1 
ATOM   6620 N N   . LEU B 1 300 ? -48.588 24.667 46.600  1.00 20.39 ? 300 LEU B N   1 
ATOM   6621 C CA  . LEU B 1 300 ? -48.253 23.562 45.702  1.00 17.62 ? 300 LEU B CA  1 
ATOM   6622 C C   . LEU B 1 300 ? -46.907 23.713 45.010  1.00 22.30 ? 300 LEU B C   1 
ATOM   6623 O O   . LEU B 1 300 ? -46.218 22.713 44.794  1.00 26.04 ? 300 LEU B O   1 
ATOM   6624 C CB  . LEU B 1 300 ? -49.342 23.392 44.632  1.00 23.12 ? 300 LEU B CB  1 
ATOM   6625 C CG  . LEU B 1 300 ? -50.677 22.845 45.141  1.00 31.08 ? 300 LEU B CG  1 
ATOM   6626 C CD1 . LEU B 1 300 ? -51.683 22.810 44.015  1.00 36.85 ? 300 LEU B CD1 1 
ATOM   6627 C CD2 . LEU B 1 300 ? -50.487 21.459 45.735  1.00 28.79 ? 300 LEU B CD2 1 
ATOM   6628 N N   . ILE B 1 301 ? -46.506 24.926 44.649  1.00 18.21 ? 301 ILE B N   1 
ATOM   6629 C CA  . ILE B 1 301 ? -45.236 25.135 43.958  1.00 15.38 ? 301 ILE B CA  1 
ATOM   6630 C C   . ILE B 1 301 ? -44.598 26.405 44.503  1.00 17.66 ? 301 ILE B C   1 
ATOM   6631 O O   . ILE B 1 301 ? -45.282 27.411 44.721  1.00 20.02 ? 301 ILE B O   1 
ATOM   6632 C CB  . ILE B 1 301 ? -45.432 25.189 42.424  1.00 21.21 ? 301 ILE B CB  1 
ATOM   6633 C CG1 . ILE B 1 301 ? -44.107 25.426 41.692  1.00 16.94 ? 301 ILE B CG1 1 
ATOM   6634 C CG2 . ILE B 1 301 ? -46.468 26.229 42.015  1.00 20.43 ? 301 ILE B CG2 1 
ATOM   6635 C CD1 . ILE B 1 301 ? -44.248 25.265 40.166  1.00 19.72 ? 301 ILE B CD1 1 
ATOM   6636 N N   . SER B 1 302 ? -43.298 26.340 44.781  1.00 15.29 ? 302 SER B N   1 
ATOM   6637 C CA  . SER B 1 302 ? -42.567 27.504 45.268  1.00 14.64 ? 302 SER B CA  1 
ATOM   6638 C C   . SER B 1 302 ? -42.268 28.454 44.115  1.00 15.69 ? 302 SER B C   1 
ATOM   6639 O O   . SER B 1 302 ? -41.931 28.023 43.012  1.00 15.15 ? 302 SER B O   1 
ATOM   6640 C CB  . SER B 1 302 ? -41.265 27.070 45.940  1.00 17.85 ? 302 SER B CB  1 
ATOM   6641 O OG  . SER B 1 302 ? -41.544 26.323 47.110  1.00 21.52 ? 302 SER B OG  1 
ATOM   6642 N N   . VAL B 1 303 ? -42.393 29.754 44.379  1.00 14.81 ? 303 VAL B N   1 
ATOM   6643 C CA  . VAL B 1 303 ? -42.201 30.787 43.368  1.00 16.27 ? 303 VAL B CA  1 
ATOM   6644 C C   . VAL B 1 303 ? -41.333 31.887 43.969  1.00 14.46 ? 303 VAL B C   1 
ATOM   6645 O O   . VAL B 1 303 ? -41.664 32.434 45.025  1.00 14.99 ? 303 VAL B O   1 
ATOM   6646 C CB  . VAL B 1 303 ? -43.546 31.362 42.880  1.00 17.69 ? 303 VAL B CB  1 
ATOM   6647 C CG1 . VAL B 1 303 ? -43.326 32.432 41.817  1.00 15.58 ? 303 VAL B CG1 1 
ATOM   6648 C CG2 . VAL B 1 303 ? -44.451 30.253 42.335  1.00 16.57 ? 303 VAL B CG2 1 
ATOM   6649 N N   . PHE B 1 304 ? -40.219 32.199 43.316  1.00 13.55 ? 304 PHE B N   1 
ATOM   6650 C CA  . PHE B 1 304 ? -39.441 33.379 43.661  1.00 13.70 ? 304 PHE B CA  1 
ATOM   6651 C C   . PHE B 1 304 ? -39.648 34.415 42.576  1.00 18.21 ? 304 PHE B C   1 
ATOM   6652 O O   . PHE B 1 304 ? -39.757 34.072 41.393  1.00 15.14 ? 304 PHE B O   1 
ATOM   6653 C CB  . PHE B 1 304 ? -37.946 33.078 43.778  1.00 13.48 ? 304 PHE B CB  1 
ATOM   6654 C CG  . PHE B 1 304 ? -37.585 32.254 44.971  1.00 15.58 ? 304 PHE B CG  1 
ATOM   6655 C CD1 . PHE B 1 304 ? -37.360 32.859 46.205  1.00 19.39 ? 304 PHE B CD1 1 
ATOM   6656 C CD2 . PHE B 1 304 ? -37.444 30.885 44.854  1.00 15.80 ? 304 PHE B CD2 1 
ATOM   6657 C CE1 . PHE B 1 304 ? -37.002 32.107 47.310  1.00 17.28 ? 304 PHE B CE1 1 
ATOM   6658 C CE2 . PHE B 1 304 ? -37.092 30.113 45.965  1.00 21.17 ? 304 PHE B CE2 1 
ATOM   6659 C CZ  . PHE B 1 304 ? -36.869 30.728 47.189  1.00 15.74 ? 304 PHE B CZ  1 
ATOM   6660 N N   . PHE B 1 305 ? -39.683 35.678 42.969  1.00 16.96 ? 305 PHE B N   1 
ATOM   6661 C CA  . PHE B 1 305 ? -39.801 36.766 42.015  1.00 17.77 ? 305 PHE B CA  1 
ATOM   6662 C C   . PHE B 1 305 ? -38.467 37.484 41.943  1.00 15.88 ? 305 PHE B C   1 
ATOM   6663 O O   . PHE B 1 305 ? -37.908 37.859 42.975  1.00 15.02 ? 305 PHE B O   1 
ATOM   6664 C CB  . PHE B 1 305 ? -40.934 37.709 42.406  1.00 14.68 ? 305 PHE B CB  1 
ATOM   6665 C CG  . PHE B 1 305 ? -42.308 37.076 42.324  1.00 14.92 ? 305 PHE B CG  1 
ATOM   6666 C CD1 . PHE B 1 305 ? -42.812 36.276 43.355  1.00 21.91 ? 305 PHE B CD1 1 
ATOM   6667 C CD2 . PHE B 1 305 ? -43.064 37.226 41.178  1.00 17.50 ? 305 PHE B CD2 1 
ATOM   6668 C CE1 . PHE B 1 305 ? -44.093 35.685 43.236  1.00 22.71 ? 305 PHE B CE1 1 
ATOM   6669 C CE2 . PHE B 1 305 ? -44.317 36.655 41.058  1.00 18.04 ? 305 PHE B CE2 1 
ATOM   6670 C CZ  . PHE B 1 305 ? -44.829 35.881 42.075  1.00 22.48 ? 305 PHE B CZ  1 
ATOM   6671 N N   . ARG B 1 306 ? -37.929 37.653 40.747  1.00 15.45 ? 306 ARG B N   1 
ATOM   6672 C CA  . ARG B 1 306 ? -36.640 38.289 40.661  1.00 13.11 ? 306 ARG B CA  1 
ATOM   6673 C C   . ARG B 1 306 ? -36.702 39.755 41.026  1.00 13.70 ? 306 ARG B C   1 
ATOM   6674 O O   . ARG B 1 306 ? -37.693 40.349 40.881  1.00 15.77 ? 306 ARG B O   1 
ATOM   6675 C CB  . ARG B 1 306 ? -36.034 38.177 39.266  1.00 19.03 ? 306 ARG B CB  1 
ATOM   6676 C CG  . ARG B 1 306 ? -36.685 39.061 38.260  1.00 30.25 ? 306 ARG B CG  1 
ATOM   6677 C CD  . ARG B 1 306 ? -36.082 38.994 36.873  1.00 40.12 ? 306 ARG B CD  1 
ATOM   6678 N NE  . ARG B 1 306 ? -36.702 39.972 36.042  1.00 37.79 ? 306 ARG B NE  1 
ATOM   6679 C CZ  . ARG B 1 306 ? -36.134 40.530 35.007  1.00 28.84 ? 306 ARG B CZ  1 
ATOM   6680 N NH1 . ARG B 1 306 ? -34.937 40.167 34.616  1.00 20.10 ? 306 ARG B NH1 1 
ATOM   6681 N NH2 . ARG B 1 306 ? -36.808 41.403 34.343  1.00 30.04 ? 306 ARG B NH2 1 
ATOM   6682 N N   . ASP B 1 307 ? -35.571 40.258 41.495  1.00 13.85 ? 307 ASP B N   1 
ATOM   6683 C CA  . ASP B 1 307 ? -35.422 41.695 41.700  1.00 14.44 ? 307 ASP B CA  1 
ATOM   6684 C C   . ASP B 1 307 ? -35.169 42.310 40.330  1.00 14.14 ? 307 ASP B C   1 
ATOM   6685 O O   . ASP B 1 307 ? -34.075 42.194 39.769  1.00 13.74 ? 307 ASP B O   1 
ATOM   6686 C CB  . ASP B 1 307 ? -34.306 41.983 42.697  1.00 22.20 ? 307 ASP B CB  1 
ATOM   6687 C CG  . ASP B 1 307 ? -34.168 43.462 43.014  1.00 23.58 ? 307 ASP B CG  1 
ATOM   6688 O OD1 . ASP B 1 307 ? -34.299 44.309 42.108  1.00 25.12 ? 307 ASP B OD1 1 
ATOM   6689 O OD2 . ASP B 1 307 ? -33.991 43.777 44.204  1.00 26.15 ? 307 ASP B OD2 1 
ATOM   6690 N N   . LYS B 1 308 ? -36.202 42.954 39.779  1.00 14.48 ? 308 LYS B N   1 
ATOM   6691 C CA  . LYS B 1 308 ? -36.134 43.427 38.400  1.00 15.73 ? 308 LYS B CA  1 
ATOM   6692 C C   . LYS B 1 308 ? -35.060 44.494 38.224  1.00 17.14 ? 308 LYS B C   1 
ATOM   6693 O O   . LYS B 1 308 ? -34.326 44.484 37.228  1.00 15.91 ? 308 LYS B O   1 
ATOM   6694 C CB  . LYS B 1 308 ? -37.504 43.960 37.960  1.00 17.94 ? 308 LYS B CB  1 
ATOM   6695 C CG  . LYS B 1 308 ? -37.495 44.640 36.599  1.00 20.03 ? 308 LYS B CG  1 
ATOM   6696 C CD  . LYS B 1 308 ? -38.896 45.059 36.153  1.00 24.55 ? 308 LYS B CD  1 
ATOM   6697 C CE  . LYS B 1 308 ? -38.827 46.031 34.967  1.00 23.77 ? 308 LYS B CE  1 
ATOM   6698 N NZ  . LYS B 1 308 ? -38.190 45.392 33.777  1.00 23.45 ? 308 LYS B NZ  1 
ATOM   6699 N N   . THR B 1 309 ? -34.949 45.420 39.180  1.00 16.99 ? 309 THR B N   1 
ATOM   6700 C CA  . THR B 1 309 ? -33.974 46.499 39.047  1.00 18.81 ? 309 THR B CA  1 
ATOM   6701 C C   . THR B 1 309 ? -32.551 45.960 39.008  1.00 20.59 ? 309 THR B C   1 
ATOM   6702 O O   . THR B 1 309 ? -31.767 46.322 38.123  1.00 18.64 ? 309 THR B O   1 
ATOM   6703 C CB  . THR B 1 309 ? -34.138 47.496 40.187  1.00 22.87 ? 309 THR B CB  1 
ATOM   6704 O OG1 . THR B 1 309 ? -35.444 48.064 40.108  1.00 21.18 ? 309 THR B OG1 1 
ATOM   6705 C CG2 . THR B 1 309 ? -33.107 48.600 40.065  1.00 24.75 ? 309 THR B CG2 1 
ATOM   6706 N N   . LEU B 1 310 ? -32.195 45.088 39.958  1.00 14.76 ? 310 LEU B N   1 
ATOM   6707 C CA  . LEU B 1 310 ? -30.846 44.526 39.953  1.00 14.39 ? 310 LEU B CA  1 
ATOM   6708 C C   . LEU B 1 310 ? -30.594 43.719 38.688  1.00 15.03 ? 310 LEU B C   1 
ATOM   6709 O O   . LEU B 1 310 ? -29.513 43.793 38.089  1.00 14.60 ? 310 LEU B O   1 
ATOM   6710 C CB  . LEU B 1 310 ? -30.631 43.649 41.188  1.00 17.54 ? 310 LEU B CB  1 
ATOM   6711 C CG  . LEU B 1 310 ? -30.652 44.336 42.555  1.00 17.14 ? 310 LEU B CG  1 
ATOM   6712 C CD1 . LEU B 1 310 ? -30.548 43.296 43.649  1.00 19.20 ? 310 LEU B CD1 1 
ATOM   6713 C CD2 . LEU B 1 310 ? -29.528 45.357 42.679  1.00 19.68 ? 310 LEU B CD2 1 
ATOM   6714 N N   . SER B 1 311 ? -31.577 42.930 38.267  1.00 13.38 ? 311 SER B N   1 
ATOM   6715 C CA  . SER B 1 311 ? -31.401 42.148 37.050  1.00 12.90 ? 311 SER B CA  1 
ATOM   6716 C C   . SER B 1 311 ? -31.204 43.058 35.834  1.00 13.93 ? 311 SER B C   1 
ATOM   6717 O O   . SER B 1 311 ? -30.305 42.823 35.008  1.00 12.90 ? 311 SER B O   1 
ATOM   6718 C CB  . SER B 1 311 ? -32.602 41.223 36.886  1.00 12.66 ? 311 SER B CB  1 
ATOM   6719 O OG  . SER B 1 311 ? -32.668 40.337 38.009  1.00 15.60 ? 311 SER B OG  1 
ATOM   6720 N N   . ASP B 1 312 ? -32.002 44.134 35.733  1.00 13.71 ? 312 ASP B N   1 
ATOM   6721 C CA  . ASP B 1 312 ? -31.917 45.021 34.574  1.00 15.90 ? 312 ASP B CA  1 
ATOM   6722 C C   . ASP B 1 312 ? -30.702 45.942 34.608  1.00 15.73 ? 312 ASP B C   1 
ATOM   6723 O O   . ASP B 1 312 ? -30.281 46.434 33.552  1.00 14.15 ? 312 ASP B O   1 
ATOM   6724 C CB  . ASP B 1 312 ? -33.169 45.899 34.456  1.00 14.39 ? 312 ASP B CB  1 
ATOM   6725 C CG  . ASP B 1 312 ? -34.373 45.164 33.909  1.00 22.63 ? 312 ASP B CG  1 
ATOM   6726 O OD1 . ASP B 1 312 ? -34.194 44.104 33.281  1.00 23.13 ? 312 ASP B OD1 1 
ATOM   6727 O OD2 . ASP B 1 312 ? -35.500 45.686 34.069  1.00 25.62 ? 312 ASP B OD2 1 
ATOM   6728 N N   . LEU B 1 313 ? -30.150 46.218 35.789  1.00 14.53 ? 313 LEU B N   1 
ATOM   6729 C CA  . LEU B 1 313 ? -28.903 46.970 35.842  1.00 15.50 ? 313 LEU B CA  1 
ATOM   6730 C C   . LEU B 1 313 ? -27.794 46.218 35.127  1.00 14.11 ? 313 LEU B C   1 
ATOM   6731 O O   . LEU B 1 313 ? -27.041 46.790 34.333  1.00 14.32 ? 313 LEU B O   1 
ATOM   6732 C CB  . LEU B 1 313 ? -28.500 47.239 37.294  1.00 14.81 ? 313 LEU B CB  1 
ATOM   6733 C CG  . LEU B 1 313 ? -29.272 48.335 38.026  1.00 18.15 ? 313 LEU B CG  1 
ATOM   6734 C CD1 . LEU B 1 313 ? -28.855 48.350 39.489  1.00 17.37 ? 313 LEU B CD1 1 
ATOM   6735 C CD2 . LEU B 1 313 ? -29.035 49.707 37.367  1.00 19.49 ? 313 LEU B CD2 1 
ATOM   6736 N N   . ILE B 1 314 ? -27.650 44.932 35.432  1.00 13.69 ? 314 ILE B N   1 
ATOM   6737 C CA  . ILE B 1 314 ? -26.622 44.152 34.765  1.00 13.96 ? 314 ILE B CA  1 
ATOM   6738 C C   . ILE B 1 314 ? -26.941 44.025 33.278  1.00 14.00 ? 314 ILE B C   1 
ATOM   6739 O O   . ILE B 1 314 ? -26.065 44.180 32.412  1.00 13.71 ? 314 ILE B O   1 
ATOM   6740 C CB  . ILE B 1 314 ? -26.510 42.779 35.440  1.00 13.28 ? 314 ILE B CB  1 
ATOM   6741 C CG1 . ILE B 1 314 ? -26.053 42.930 36.896  1.00 13.53 ? 314 ILE B CG1 1 
ATOM   6742 C CG2 . ILE B 1 314 ? -25.573 41.871 34.660  1.00 13.30 ? 314 ILE B CG2 1 
ATOM   6743 C CD1 . ILE B 1 314 ? -26.030 41.595 37.615  1.00 15.20 ? 314 ILE B CD1 1 
ATOM   6744 N N   . GLY B 1 315 ? -28.201 43.732 32.959  1.00 13.28 ? 315 GLY B N   1 
ATOM   6745 C CA  . GLY B 1 315 ? -28.547 43.430 31.584  1.00 13.31 ? 315 GLY B CA  1 
ATOM   6746 C C   . GLY B 1 315 ? -28.541 44.640 30.674  1.00 17.20 ? 315 GLY B C   1 
ATOM   6747 O O   . GLY B 1 315 ? -28.315 44.508 29.468  1.00 18.08 ? 315 GLY B O   1 
ATOM   6748 N N   . PHE B 1 316 ? -28.776 45.829 31.223  1.00 14.58 ? 316 PHE B N   1 
ATOM   6749 C CA  . PHE B 1 316 ? -29.003 46.995 30.375  1.00 15.31 ? 316 PHE B CA  1 
ATOM   6750 C C   . PHE B 1 316 ? -28.179 48.233 30.693  1.00 18.97 ? 316 PHE B C   1 
ATOM   6751 O O   . PHE B 1 316 ? -27.990 49.057 29.786  1.00 25.24 ? 316 PHE B O   1 
ATOM   6752 C CB  . PHE B 1 316 ? -30.489 47.389 30.403  1.00 21.12 ? 316 PHE B CB  1 
ATOM   6753 C CG  . PHE B 1 316 ? -31.389 46.360 29.791  1.00 23.41 ? 316 PHE B CG  1 
ATOM   6754 C CD1 . PHE B 1 316 ? -31.437 46.191 28.415  1.00 27.29 ? 316 PHE B CD1 1 
ATOM   6755 C CD2 . PHE B 1 316 ? -32.181 45.546 30.589  1.00 19.35 ? 316 PHE B CD2 1 
ATOM   6756 C CE1 . PHE B 1 316 ? -32.266 45.228 27.850  1.00 31.42 ? 316 PHE B CE1 1 
ATOM   6757 C CE2 . PHE B 1 316 ? -33.006 44.594 30.034  1.00 27.22 ? 316 PHE B CE2 1 
ATOM   6758 C CZ  . PHE B 1 316 ? -33.051 44.431 28.663  1.00 28.44 ? 316 PHE B CZ  1 
ATOM   6759 N N   A SER B 1 317 ? -27.665 48.402 31.909  0.53 15.01 ? 317 SER B N   1 
ATOM   6760 N N   B SER B 1 317 ? -27.709 48.415 31.926  0.47 15.05 ? 317 SER B N   1 
ATOM   6761 C CA  A SER B 1 317 ? -27.065 49.683 32.263  0.53 15.59 ? 317 SER B CA  1 
ATOM   6762 C CA  B SER B 1 317 ? -27.095 49.678 32.339  0.47 15.58 ? 317 SER B CA  1 
ATOM   6763 C C   A SER B 1 317 ? -25.573 49.603 32.544  0.53 15.60 ? 317 SER B C   1 
ATOM   6764 C C   B SER B 1 317 ? -25.589 49.585 32.527  0.47 15.59 ? 317 SER B C   1 
ATOM   6765 O O   A SER B 1 317 ? -24.815 50.477 32.092  0.53 17.83 ? 317 SER B O   1 
ATOM   6766 O O   B SER B 1 317 ? -24.844 50.409 31.988  0.47 17.68 ? 317 SER B O   1 
ATOM   6767 C CB  A SER B 1 317 ? -27.786 50.287 33.485  0.53 16.47 ? 317 SER B CB  1 
ATOM   6768 C CB  B SER B 1 317 ? -27.737 50.187 33.645  0.47 15.83 ? 317 SER B CB  1 
ATOM   6769 O OG  A SER B 1 317 ? -27.451 51.656 33.632  0.53 19.59 ? 317 SER B OG  1 
ATOM   6770 O OG  B SER B 1 317 ? -29.152 50.198 33.585  0.47 15.93 ? 317 SER B OG  1 
ATOM   6771 N N   . TYR B 1 318 ? -25.124 48.591 33.288  1.00 15.19 ? 318 TYR B N   1 
ATOM   6772 C CA  . TYR B 1 318 ? -23.740 48.558 33.754  1.00 15.38 ? 318 TYR B CA  1 
ATOM   6773 C C   . TYR B 1 318 ? -22.718 48.395 32.634  1.00 16.60 ? 318 TYR B C   1 
ATOM   6774 O O   . TYR B 1 318 ? -21.531 48.590 32.894  1.00 16.89 ? 318 TYR B O   1 
ATOM   6775 C CB  . TYR B 1 318 ? -23.535 47.411 34.755  1.00 15.04 ? 318 TYR B CB  1 
ATOM   6776 C CG  . TYR B 1 318 ? -24.112 47.641 36.159  1.00 16.42 ? 318 TYR B CG  1 
ATOM   6777 C CD1 . TYR B 1 318 ? -24.391 48.925 36.643  1.00 16.47 ? 318 TYR B CD1 1 
ATOM   6778 C CD2 . TYR B 1 318 ? -24.350 46.561 37.001  1.00 14.85 ? 318 TYR B CD2 1 
ATOM   6779 C CE1 . TYR B 1 318 ? -24.908 49.107 37.947  1.00 15.97 ? 318 TYR B CE1 1 
ATOM   6780 C CE2 . TYR B 1 318 ? -24.855 46.729 38.283  1.00 20.88 ? 318 TYR B CE2 1 
ATOM   6781 C CZ  . TYR B 1 318 ? -25.135 47.992 38.756  1.00 19.91 ? 318 TYR B CZ  1 
ATOM   6782 O OH  . TYR B 1 318 ? -25.644 48.110 40.043  1.00 18.68 ? 318 TYR B OH  1 
ATOM   6783 N N   . HIS B 1 319 ? -23.133 48.027 31.415  1.00 16.36 ? 319 HIS B N   1 
ATOM   6784 C CA  . HIS B 1 319 ? -22.172 47.928 30.315  1.00 15.80 ? 319 HIS B CA  1 
ATOM   6785 C C   . HIS B 1 319 ? -21.433 49.237 30.103  1.00 21.15 ? 319 HIS B C   1 
ATOM   6786 O O   . HIS B 1 319 ? -20.278 49.233 29.669  1.00 16.85 ? 319 HIS B O   1 
ATOM   6787 C CB  . HIS B 1 319 ? -22.880 47.548 29.019  1.00 16.66 ? 319 HIS B CB  1 
ATOM   6788 C CG  . HIS B 1 319 ? -23.754 48.638 28.489  1.00 18.27 ? 319 HIS B CG  1 
ATOM   6789 N ND1 . HIS B 1 319 ? -25.017 48.884 28.984  1.00 19.41 ? 319 HIS B ND1 1 
ATOM   6790 C CD2 . HIS B 1 319 ? -23.530 49.576 27.540  1.00 18.07 ? 319 HIS B CD2 1 
ATOM   6791 C CE1 . HIS B 1 319 ? -25.545 49.912 28.343  1.00 19.86 ? 319 HIS B CE1 1 
ATOM   6792 N NE2 . HIS B 1 319 ? -24.662 50.354 27.467  1.00 22.07 ? 319 HIS B NE2 1 
ATOM   6793 N N   . ALA B 1 320 ? -22.085 50.365 30.387  1.00 20.00 ? 320 ALA B N   1 
ATOM   6794 C CA  . ALA B 1 320 ? -21.495 51.669 30.129  1.00 23.03 ? 320 ALA B CA  1 
ATOM   6795 C C   . ALA B 1 320 ? -20.717 52.224 31.316  1.00 23.54 ? 320 ALA B C   1 
ATOM   6796 O O   . ALA B 1 320 ? -20.077 53.278 31.175  1.00 22.46 ? 320 ALA B O   1 
ATOM   6797 C CB  . ALA B 1 320 ? -22.585 52.666 29.724  1.00 25.26 ? 320 ALA B CB  1 
ATOM   6798 N N   . TRP B 1 321 ? -20.763 51.550 32.463  1.00 17.21 ? 321 TRP B N   1 
ATOM   6799 C CA  . TRP B 1 321 ? -20.105 51.988 33.681  1.00 17.56 ? 321 TRP B CA  1 
ATOM   6800 C C   . TRP B 1 321 ? -18.720 51.377 33.809  1.00 22.75 ? 321 TRP B C   1 
ATOM   6801 O O   . TRP B 1 321 ? -18.436 50.299 33.293  1.00 20.43 ? 321 TRP B O   1 
ATOM   6802 C CB  . TRP B 1 321 ? -20.877 51.592 34.939  1.00 21.21 ? 321 TRP B CB  1 
ATOM   6803 C CG  . TRP B 1 321 ? -22.292 52.049 35.077  1.00 20.87 ? 321 TRP B CG  1 
ATOM   6804 C CD1 . TRP B 1 321 ? -23.205 52.282 34.089  1.00 24.12 ? 321 TRP B CD1 1 
ATOM   6805 C CD2 . TRP B 1 321 ? -22.952 52.339 36.314  1.00 18.69 ? 321 TRP B CD2 1 
ATOM   6806 N NE1 . TRP B 1 321 ? -24.409 52.684 34.646  1.00 24.93 ? 321 TRP B NE1 1 
ATOM   6807 C CE2 . TRP B 1 321 ? -24.273 52.725 36.009  1.00 25.61 ? 321 TRP B CE2 1 
ATOM   6808 C CE3 . TRP B 1 321 ? -22.551 52.304 37.647  1.00 19.38 ? 321 TRP B CE3 1 
ATOM   6809 C CZ2 . TRP B 1 321 ? -25.194 53.083 36.998  1.00 29.43 ? 321 TRP B CZ2 1 
ATOM   6810 C CZ3 . TRP B 1 321 ? -23.471 52.662 38.632  1.00 26.27 ? 321 TRP B CZ3 1 
ATOM   6811 C CH2 . TRP B 1 321 ? -24.771 53.044 38.299  1.00 27.28 ? 321 TRP B CH2 1 
ATOM   6812 N N   . ASN B 1 322 ? -17.874 52.060 34.568  1.00 21.73 ? 322 ASN B N   1 
ATOM   6813 C CA  . ASN B 1 322 ? -16.631 51.454 35.008  1.00 19.96 ? 322 ASN B CA  1 
ATOM   6814 C C   . ASN B 1 322 ? -16.937 50.328 36.000  1.00 25.65 ? 322 ASN B C   1 
ATOM   6815 O O   . ASN B 1 322 ? -17.887 50.416 36.783  1.00 27.25 ? 322 ASN B O   1 
ATOM   6816 C CB  . ASN B 1 322 ? -15.729 52.539 35.604  1.00 34.55 ? 322 ASN B CB  1 
ATOM   6817 C CG  . ASN B 1 322 ? -14.744 52.004 36.598  1.00 51.06 ? 322 ASN B CG  1 
ATOM   6818 O OD1 . ASN B 1 322 ? -15.077 51.806 37.764  1.00 54.15 ? 322 ASN B OD1 1 
ATOM   6819 N ND2 . ASN B 1 322 ? -13.519 51.748 36.143  1.00 62.07 ? 322 ASN B ND2 1 
ATOM   6820 N N   . ALA B 1 323 ? -16.162 49.237 35.927  1.00 21.99 ? 323 ALA B N   1 
ATOM   6821 C CA  . ALA B 1 323 ? -16.519 48.031 36.676  1.00 19.31 ? 323 ALA B CA  1 
ATOM   6822 C C   . ALA B 1 323 ? -16.568 48.289 38.182  1.00 20.32 ? 323 ALA B C   1 
ATOM   6823 O O   . ALA B 1 323 ? -17.442 47.760 38.881  1.00 23.65 ? 323 ALA B O   1 
ATOM   6824 C CB  . ALA B 1 323 ? -15.537 46.896 36.365  1.00 20.11 ? 323 ALA B CB  1 
ATOM   6825 N N   . GLU B 1 324 ? -15.638 49.101 38.696  1.00 21.90 ? 324 GLU B N   1 
ATOM   6826 C CA  . GLU B 1 324 ? -15.604 49.409 40.123  1.00 23.45 ? 324 GLU B CA  1 
ATOM   6827 C C   . GLU B 1 324 ? -16.854 50.167 40.565  1.00 24.21 ? 324 GLU B C   1 
ATOM   6828 O O   . GLU B 1 324 ? -17.465 49.828 41.586  1.00 24.56 ? 324 GLU B O   1 
ATOM   6829 C CB  . GLU B 1 324 ? -14.337 50.211 40.438  1.00 33.14 ? 324 GLU B CB  1 
ATOM   6830 C CG  . GLU B 1 324 ? -14.217 50.692 41.868  1.00 50.87 ? 324 GLU B CG  1 
ATOM   6831 C CD  . GLU B 1 324 ? -12.796 51.115 42.224  1.00 66.54 ? 324 GLU B CD  1 
ATOM   6832 O OE1 . GLU B 1 324 ? -11.901 50.973 41.361  1.00 69.77 ? 324 GLU B OE1 1 
ATOM   6833 O OE2 . GLU B 1 324 ? -12.575 51.584 43.364  1.00 70.66 ? 324 GLU B OE2 1 
ATOM   6834 N N   . ASP B 1 325 ? -17.261 51.186 39.806  1.00 23.67 ? 325 ASP B N   1 
ATOM   6835 C CA  . ASP B 1 325 ? -18.502 51.891 40.130  1.00 28.08 ? 325 ASP B CA  1 
ATOM   6836 C C   . ASP B 1 325 ? -19.700 50.946 40.084  1.00 26.24 ? 325 ASP B C   1 
ATOM   6837 O O   . ASP B 1 325 ? -20.557 50.968 40.973  1.00 23.49 ? 325 ASP B O   1 
ATOM   6838 C CB  . ASP B 1 325 ? -18.721 53.050 39.161  1.00 24.70 ? 325 ASP B CB  1 
ATOM   6839 C CG  . ASP B 1 325 ? -17.673 54.115 39.285  1.00 33.72 ? 325 ASP B CG  1 
ATOM   6840 O OD1 . ASP B 1 325 ? -17.165 54.327 40.405  1.00 34.39 ? 325 ASP B OD1 1 
ATOM   6841 O OD2 . ASP B 1 325 ? -17.352 54.722 38.245  1.00 27.81 ? 325 ASP B OD2 1 
ATOM   6842 N N   . ALA B 1 326 ? -19.795 50.134 39.026  1.00 21.55 ? 326 ALA B N   1 
ATOM   6843 C CA  . ALA B 1 326 ? -20.941 49.240 38.880  1.00 20.43 ? 326 ALA B CA  1 
ATOM   6844 C C   . ALA B 1 326 ? -21.045 48.284 40.059  1.00 20.32 ? 326 ALA B C   1 
ATOM   6845 O O   . ALA B 1 326 ? -22.139 48.046 40.588  1.00 20.76 ? 326 ALA B O   1 
ATOM   6846 C CB  . ALA B 1 326 ? -20.843 48.445 37.572  1.00 18.96 ? 326 ALA B CB  1 
ATOM   6847 N N   . VAL B 1 327 ? -19.921 47.699 40.469  1.00 20.32 ? 327 VAL B N   1 
ATOM   6848 C CA  . VAL B 1 327 ? -19.975 46.739 41.569  1.00 23.24 ? 327 VAL B CA  1 
ATOM   6849 C C   . VAL B 1 327 ? -20.312 47.451 42.876  1.00 23.52 ? 327 VAL B C   1 
ATOM   6850 O O   . VAL B 1 327 ? -21.097 46.943 43.693  1.00 22.30 ? 327 VAL B O   1 
ATOM   6851 C CB  . VAL B 1 327 ? -18.657 45.945 41.654  1.00 21.51 ? 327 VAL B CB  1 
ATOM   6852 C CG1 . VAL B 1 327 ? -18.666 45.022 42.868  1.00 24.05 ? 327 VAL B CG1 1 
ATOM   6853 C CG2 . VAL B 1 327 ? -18.478 45.112 40.377  1.00 18.57 ? 327 VAL B CG2 1 
ATOM   6854 N N   . ARG B 1 328 ? -19.756 48.650 43.084  1.00 23.07 ? 328 ARG B N   1 
ATOM   6855 C CA  . ARG B 1 328 ? -20.097 49.408 44.286  1.00 24.61 ? 328 ARG B CA  1 
ATOM   6856 C C   . ARG B 1 328 ? -21.584 49.741 44.330  1.00 24.63 ? 328 ARG B C   1 
ATOM   6857 O O   . ARG B 1 328 ? -22.209 49.686 45.396  1.00 25.33 ? 328 ARG B O   1 
ATOM   6858 C CB  . ARG B 1 328 ? -19.268 50.691 44.363  1.00 26.07 ? 328 ARG B CB  1 
ATOM   6859 C CG  . ARG B 1 328 ? -19.519 51.456 45.664  1.00 27.83 ? 328 ARG B CG  1 
ATOM   6860 C CD  . ARG B 1 328 ? -18.725 52.759 45.717  1.00 31.91 ? 328 ARG B CD  1 
ATOM   6861 N NE  . ARG B 1 328 ? -19.220 53.719 44.733  1.00 36.70 ? 328 ARG B NE  1 
ATOM   6862 C CZ  . ARG B 1 328 ? -18.546 54.124 43.662  1.00 39.57 ? 328 ARG B CZ  1 
ATOM   6863 N NH1 . ARG B 1 328 ? -17.321 53.659 43.413  1.00 43.36 ? 328 ARG B NH1 1 
ATOM   6864 N NH2 . ARG B 1 328 ? -19.099 55.006 42.840  1.00 37.25 ? 328 ARG B NH2 1 
ATOM   6865 N N   . ASP B 1 329 ? -22.163 50.110 43.183  1.00 23.99 ? 329 ASP B N   1 
ATOM   6866 C CA  . ASP B 1 329 ? -23.598 50.375 43.117  1.00 29.74 ? 329 ASP B CA  1 
ATOM   6867 C C   . ASP B 1 329 ? -24.397 49.124 43.470  1.00 23.00 ? 329 ASP B C   1 
ATOM   6868 O O   . ASP B 1 329 ? -25.337 49.173 44.277  1.00 23.58 ? 329 ASP B O   1 
ATOM   6869 C CB  . ASP B 1 329 ? -23.959 50.874 41.712  1.00 27.20 ? 329 ASP B CB  1 
ATOM   6870 C CG  . ASP B 1 329 ? -25.415 51.287 41.588  1.00 27.71 ? 329 ASP B CG  1 
ATOM   6871 O OD1 . ASP B 1 329 ? -25.774 52.387 42.068  1.00 29.48 ? 329 ASP B OD1 1 
ATOM   6872 O OD2 . ASP B 1 329 ? -26.201 50.508 41.014  1.00 23.31 ? 329 ASP B OD2 1 
ATOM   6873 N N   . PHE B 1 330 ? -24.013 47.986 42.888  1.00 21.58 ? 330 PHE B N   1 
ATOM   6874 C CA  . PHE B 1 330 ? -24.699 46.723 43.129  1.00 20.59 ? 330 PHE B CA  1 
ATOM   6875 C C   . PHE B 1 330 ? -24.633 46.325 44.596  1.00 21.36 ? 330 PHE B C   1 
ATOM   6876 O O   . PHE B 1 330 ? -25.667 46.069 45.229  1.00 21.54 ? 330 PHE B O   1 
ATOM   6877 C CB  . PHE B 1 330 ? -24.072 45.641 42.243  1.00 19.12 ? 330 PHE B CB  1 
ATOM   6878 C CG  . PHE B 1 330 ? -24.865 44.364 42.160  1.00 17.97 ? 330 PHE B CG  1 
ATOM   6879 C CD1 . PHE B 1 330 ? -25.907 44.243 41.255  1.00 17.18 ? 330 PHE B CD1 1 
ATOM   6880 C CD2 . PHE B 1 330 ? -24.537 43.275 42.957  1.00 17.76 ? 330 PHE B CD2 1 
ATOM   6881 C CE1 . PHE B 1 330 ? -26.629 43.044 41.148  1.00 16.17 ? 330 PHE B CE1 1 
ATOM   6882 C CE2 . PHE B 1 330 ? -25.255 42.072 42.854  1.00 17.95 ? 330 PHE B CE2 1 
ATOM   6883 C CZ  . PHE B 1 330 ? -26.296 41.967 41.955  1.00 20.70 ? 330 PHE B CZ  1 
ATOM   6884 N N   . ILE B 1 331 ? -23.419 46.251 45.149  1.00 22.53 ? 331 ILE B N   1 
ATOM   6885 C CA  . ILE B 1 331 ? -23.270 45.913 46.563  1.00 23.04 ? 331 ILE B CA  1 
ATOM   6886 C C   . ILE B 1 331 ? -24.031 46.910 47.423  1.00 24.27 ? 331 ILE B C   1 
ATOM   6887 O O   . ILE B 1 331 ? -24.715 46.533 48.381  1.00 24.70 ? 331 ILE B O   1 
ATOM   6888 C CB  . ILE B 1 331 ? -21.784 45.862 46.962  1.00 24.38 ? 331 ILE B CB  1 
ATOM   6889 C CG1 . ILE B 1 331 ? -21.030 44.800 46.155  1.00 23.11 ? 331 ILE B CG1 1 
ATOM   6890 C CG2 . ILE B 1 331 ? -21.652 45.576 48.447  1.00 24.87 ? 331 ILE B CG2 1 
ATOM   6891 C CD1 . ILE B 1 331 ? -21.439 43.386 46.491  1.00 25.92 ? 331 ILE B CD1 1 
ATOM   6892 N N   . GLY B 1 332 ? -23.928 48.196 47.082  1.00 26.62 ? 332 GLY B N   1 
ATOM   6893 C CA  . GLY B 1 332 ? -24.693 49.206 47.791  1.00 31.03 ? 332 GLY B CA  1 
ATOM   6894 C C   . GLY B 1 332 ? -26.175 48.897 47.821  1.00 28.39 ? 332 GLY B C   1 
ATOM   6895 O O   . GLY B 1 332 ? -26.815 48.999 48.870  1.00 28.22 ? 332 GLY B O   1 
ATOM   6896 N N   . ARG B 1 333 ? -26.739 48.473 46.678  1.00 24.76 ? 333 ARG B N   1 
ATOM   6897 C CA  . ARG B 1 333 ? -28.170 48.185 46.631  1.00 24.41 ? 333 ARG B CA  1 
ATOM   6898 C C   . ARG B 1 333 ? -28.526 46.969 47.479  1.00 28.40 ? 333 ARG B C   1 
ATOM   6899 O O   . ARG B 1 333 ? -29.573 46.956 48.134  1.00 24.56 ? 333 ARG B O   1 
ATOM   6900 C CB  . ARG B 1 333 ? -28.614 47.998 45.189  1.00 24.58 ? 333 ARG B CB  1 
ATOM   6901 C CG  . ARG B 1 333 ? -28.578 49.291 44.420  1.00 30.98 ? 333 ARG B CG  1 
ATOM   6902 C CD  . ARG B 1 333 ? -28.814 49.053 42.954  1.00 25.03 ? 333 ARG B CD  1 
ATOM   6903 N NE  . ARG B 1 333 ? -28.832 50.314 42.225  1.00 28.78 ? 333 ARG B NE  1 
ATOM   6904 C CZ  . ARG B 1 333 ? -29.935 51.026 42.029  1.00 33.53 ? 333 ARG B CZ  1 
ATOM   6905 N NH1 . ARG B 1 333 ? -31.089 50.602 42.535  1.00 27.93 ? 333 ARG B NH1 1 
ATOM   6906 N NH2 . ARG B 1 333 ? -29.881 52.164 41.346  1.00 36.60 ? 333 ARG B NH2 1 
ATOM   6907 N N   . LEU B 1 334 ? -27.668 45.942 47.484  1.00 23.14 ? 334 LEU B N   1 
ATOM   6908 C CA  . LEU B 1 334 ? -27.898 44.799 48.365  1.00 22.94 ? 334 LEU B CA  1 
ATOM   6909 C C   . LEU B 1 334 ? -27.846 45.209 49.834  1.00 24.60 ? 334 LEU B C   1 
ATOM   6910 O O   . LEU B 1 334 ? -28.634 44.715 50.649  1.00 29.45 ? 334 LEU B O   1 
ATOM   6911 C CB  . LEU B 1 334 ? -26.872 43.699 48.093  1.00 21.90 ? 334 LEU B CB  1 
ATOM   6912 C CG  . LEU B 1 334 ? -26.906 43.109 46.687  1.00 20.26 ? 334 LEU B CG  1 
ATOM   6913 C CD1 . LEU B 1 334 ? -25.700 42.196 46.482  1.00 23.83 ? 334 LEU B CD1 1 
ATOM   6914 C CD2 . LEU B 1 334 ? -28.211 42.348 46.474  1.00 19.98 ? 334 LEU B CD2 1 
ATOM   6915 N N   . LYS B 1 335 ? -26.924 46.112 50.195  1.00 26.46 ? 335 LYS B N   1 
ATOM   6916 C CA  . LYS B 1 335 ? -26.880 46.580 51.578  1.00 27.50 ? 335 LYS B CA  1 
ATOM   6917 C C   . LYS B 1 335 ? -28.189 47.255 51.969  1.00 28.40 ? 335 LYS B C   1 
ATOM   6918 O O   . LYS B 1 335 ? -28.687 47.061 53.086  1.00 31.96 ? 335 LYS B O   1 
ATOM   6919 C CB  . LYS B 1 335 ? -25.701 47.539 51.787  1.00 28.91 ? 335 LYS B CB  1 
ATOM   6920 C CG  . LYS B 1 335 ? -25.473 47.944 53.258  1.00 43.37 ? 335 LYS B CG  1 
ATOM   6921 C CD  . LYS B 1 335 ? -24.980 46.750 54.081  1.00 49.73 ? 335 LYS B CD  1 
ATOM   6922 C CE  . LYS B 1 335 ? -24.591 47.130 55.505  1.00 56.93 ? 335 LYS B CE  1 
ATOM   6923 N NZ  . LYS B 1 335 ? -24.185 45.921 56.287  1.00 55.14 ? 335 LYS B NZ  1 
ATOM   6924 N N   . LYS B 1 336 ? -28.774 48.037 51.058  1.00 28.21 ? 336 LYS B N   1 
ATOM   6925 C CA  . LYS B 1 336 ? -30.023 48.726 51.379  1.00 32.71 ? 336 LYS B CA  1 
ATOM   6926 C C   . LYS B 1 336 ? -31.159 47.726 51.559  1.00 33.70 ? 336 LYS B C   1 
ATOM   6927 O O   . LYS B 1 336 ? -32.004 47.892 52.452  1.00 34.51 ? 336 LYS B O   1 
ATOM   6928 C CB  . LYS B 1 336 ? -30.371 49.762 50.301  1.00 36.75 ? 336 LYS B CB  1 
ATOM   6929 C CG  . LYS B 1 336 ? -29.579 51.117 50.366  1.00 48.00 ? 336 LYS B CG  1 
ATOM   6930 C CD  . LYS B 1 336 ? -28.081 50.862 50.492  1.00 54.20 ? 336 LYS B CD  1 
ATOM   6931 C CE  . LYS B 1 336 ? -27.147 51.992 50.131  1.00 53.95 ? 336 LYS B CE  1 
ATOM   6932 N NZ  . LYS B 1 336 ? -25.760 51.523 50.377  1.00 52.55 ? 336 LYS B NZ  1 
ATOM   6933 N N   . ILE B 1 337 ? -31.188 46.671 50.736  1.00 31.94 ? 337 ILE B N   1 
ATOM   6934 C CA  . ILE B 1 337 ? -32.157 45.598 50.944  1.00 31.15 ? 337 ILE B CA  1 
ATOM   6935 C C   . ILE B 1 337 ? -31.922 44.926 52.291  1.00 31.06 ? 337 ILE B C   1 
ATOM   6936 O O   . ILE B 1 337 ? -32.854 44.734 53.085  1.00 34.12 ? 337 ILE B O   1 
ATOM   6937 C CB  . ILE B 1 337 ? -32.084 44.577 49.797  1.00 24.07 ? 337 ILE B CB  1 
ATOM   6938 C CG1 . ILE B 1 337 ? -32.385 45.240 48.458  1.00 23.50 ? 337 ILE B CG1 1 
ATOM   6939 C CG2 . ILE B 1 337 ? -33.064 43.443 50.079  1.00 23.47 ? 337 ILE B CG2 1 
ATOM   6940 C CD1 . ILE B 1 337 ? -32.006 44.386 47.243  1.00 23.73 ? 337 ILE B CD1 1 
ATOM   6941 N N   . HIS B 1 338 ? -30.669 44.551 52.560  1.00 27.59 ? 338 HIS B N   1 
ATOM   6942 C CA  . HIS B 1 338 ? -30.324 43.858 53.798  1.00 31.49 ? 338 HIS B CA  1 
ATOM   6943 C C   . HIS B 1 338 ? -30.760 44.650 55.028  1.00 37.81 ? 338 HIS B C   1 
ATOM   6944 O O   . HIS B 1 338 ? -31.234 44.072 56.016  1.00 36.85 ? 338 HIS B O   1 
ATOM   6945 C CB  . HIS B 1 338 ? -28.815 43.593 53.825  1.00 32.22 ? 338 HIS B CB  1 
ATOM   6946 C CG  . HIS B 1 338 ? -28.329 42.900 55.064  1.00 42.58 ? 338 HIS B CG  1 
ATOM   6947 N ND1 . HIS B 1 338 ? -27.815 43.582 56.147  1.00 47.23 ? 338 HIS B ND1 1 
ATOM   6948 C CD2 . HIS B 1 338 ? -28.262 41.585 55.382  1.00 46.09 ? 338 HIS B CD2 1 
ATOM   6949 C CE1 . HIS B 1 338 ? -27.458 42.717 57.080  1.00 47.30 ? 338 HIS B CE1 1 
ATOM   6950 N NE2 . HIS B 1 338 ? -27.717 41.498 56.640  1.00 44.32 ? 338 HIS B NE2 1 
ATOM   6951 N N   . GLU B 1 339 ? -30.622 45.971 54.988  1.00 40.22 ? 339 GLU B N   1 
ATOM   6952 C CA  . GLU B 1 339 ? -30.967 46.788 56.142  1.00 44.43 ? 339 GLU B CA  1 
ATOM   6953 C C   . GLU B 1 339 ? -32.443 47.174 56.187  1.00 43.38 ? 339 GLU B C   1 
ATOM   6954 O O   . GLU B 1 339 ? -32.904 47.647 57.229  1.00 43.72 ? 339 GLU B O   1 
ATOM   6955 C CB  . GLU B 1 339 ? -30.095 48.050 56.180  1.00 49.59 ? 339 GLU B CB  1 
ATOM   6956 C CG  . GLU B 1 339 ? -30.595 49.176 55.301  1.00 58.58 ? 339 GLU B CG  1 
ATOM   6957 C CD  . GLU B 1 339 ? -29.645 50.356 55.279  1.00 72.14 ? 339 GLU B CD  1 
ATOM   6958 O OE1 . GLU B 1 339 ? -29.944 51.348 54.579  1.00 75.30 ? 339 GLU B OE1 1 
ATOM   6959 O OE2 . GLU B 1 339 ? -28.599 50.290 55.961  1.00 76.28 ? 339 GLU B OE2 1 
ATOM   6960 N N   . SER B 1 340 ? -33.199 46.957 55.105  1.00 42.79 ? 340 SER B N   1 
ATOM   6961 C CA  . SER B 1 340 ? -34.595 47.374 55.029  1.00 41.63 ? 340 SER B CA  1 
ATOM   6962 C C   . SER B 1 340 ? -35.569 46.356 55.612  1.00 41.69 ? 340 SER B C   1 
ATOM   6963 O O   . SER B 1 340 ? -36.746 46.688 55.791  1.00 44.54 ? 340 SER B O   1 
ATOM   6964 C CB  . SER B 1 340 ? -35.009 47.647 53.576  1.00 38.29 ? 340 SER B CB  1 
ATOM   6965 O OG  . SER B 1 340 ? -35.280 46.432 52.871  1.00 34.90 ? 340 SER B OG  1 
ATOM   6966 N N   . VAL B 1 341 ? -35.123 45.132 55.903  1.00 37.09 ? 341 VAL B N   1 
ATOM   6967 C CA  . VAL B 1 341 ? -36.007 44.083 56.391  1.00 37.23 ? 341 VAL B CA  1 
ATOM   6968 C C   . VAL B 1 341 ? -35.404 43.468 57.640  1.00 40.68 ? 341 VAL B C   1 
ATOM   6969 O O   . VAL B 1 341 ? -34.203 43.563 57.894  1.00 39.98 ? 341 VAL B O   1 
ATOM   6970 C CB  . VAL B 1 341 ? -36.270 42.975 55.339  1.00 37.68 ? 341 VAL B CB  1 
ATOM   6971 C CG1 . VAL B 1 341 ? -36.997 43.537 54.141  1.00 31.84 ? 341 VAL B CG1 1 
ATOM   6972 C CG2 . VAL B 1 341 ? -34.968 42.311 54.919  1.00 38.92 ? 341 VAL B CG2 1 
ATOM   6973 N N   . ASP B 1 342 ? -36.262 42.804 58.410  1.00 42.23 ? 342 ASP B N   1 
ATOM   6974 C CA  . ASP B 1 342 ? -35.848 42.208 59.667  1.00 45.13 ? 342 ASP B CA  1 
ATOM   6975 C C   . ASP B 1 342 ? -35.535 40.726 59.543  1.00 37.48 ? 342 ASP B C   1 
ATOM   6976 O O   . ASP B 1 342 ? -34.907 40.165 60.446  1.00 47.04 ? 342 ASP B O   1 
ATOM   6977 C CB  . ASP B 1 342 ? -36.938 42.436 60.713  1.00 53.89 ? 342 ASP B CB  1 
ATOM   6978 C CG  . ASP B 1 342 ? -37.289 43.907 60.855  1.00 62.46 ? 342 ASP B CG  1 
ATOM   6979 O OD1 . ASP B 1 342 ? -36.362 44.747 60.880  1.00 62.46 ? 342 ASP B OD1 1 
ATOM   6980 O OD2 . ASP B 1 342 ? -38.494 44.233 60.883  1.00 66.08 ? 342 ASP B OD2 1 
ATOM   6981 N N   . PHE B 1 343 ? -35.926 40.093 58.442  1.00 29.67 ? 343 PHE B N   1 
ATOM   6982 C CA  . PHE B 1 343 ? -35.624 38.701 58.161  1.00 28.34 ? 343 PHE B CA  1 
ATOM   6983 C C   . PHE B 1 343 ? -34.466 38.632 57.161  1.00 27.73 ? 343 PHE B C   1 
ATOM   6984 O O   . PHE B 1 343 ? -33.905 39.654 56.757  1.00 30.70 ? 343 PHE B O   1 
ATOM   6985 C CB  . PHE B 1 343 ? -36.870 38.000 57.620  1.00 33.72 ? 343 PHE B CB  1 
ATOM   6986 C CG  . PHE B 1 343 ? -37.450 38.676 56.412  1.00 32.51 ? 343 PHE B CG  1 
ATOM   6987 C CD1 . PHE B 1 343 ? -38.374 39.700 56.553  1.00 32.58 ? 343 PHE B CD1 1 
ATOM   6988 C CD2 . PHE B 1 343 ? -37.050 38.309 55.132  1.00 30.62 ? 343 PHE B CD2 1 
ATOM   6989 C CE1 . PHE B 1 343 ? -38.896 40.344 55.440  1.00 31.04 ? 343 PHE B CE1 1 
ATOM   6990 C CE2 . PHE B 1 343 ? -37.572 38.946 54.009  1.00 28.47 ? 343 PHE B CE2 1 
ATOM   6991 C CZ  . PHE B 1 343 ? -38.493 39.962 54.160  1.00 26.78 ? 343 PHE B CZ  1 
ATOM   6992 N N   . GLN B 1 344 ? -34.096 37.414 56.763  1.00 26.81 ? 344 GLN B N   1 
ATOM   6993 C CA  . GLN B 1 344 ? -33.041 37.243 55.772  1.00 26.50 ? 344 GLN B CA  1 
ATOM   6994 C C   . GLN B 1 344 ? -33.683 37.231 54.390  1.00 27.13 ? 344 GLN B C   1 
ATOM   6995 O O   . GLN B 1 344 ? -34.364 36.252 54.044  1.00 24.14 ? 344 GLN B O   1 
ATOM   6996 C CB  . GLN B 1 344 ? -32.259 35.959 55.999  1.00 32.25 ? 344 GLN B CB  1 
ATOM   6997 C CG  . GLN B 1 344 ? -32.193 35.449 57.433  1.00 44.46 ? 344 GLN B CG  1 
ATOM   6998 C CD  . GLN B 1 344 ? -30.997 34.539 57.677  1.00 46.91 ? 344 GLN B CD  1 
ATOM   6999 O OE1 . GLN B 1 344 ? -29.839 34.931 57.513  1.00 50.08 ? 344 GLN B OE1 1 
ATOM   7000 N NE2 . GLN B 1 344 ? -31.285 33.281 57.959  1.00 36.05 ? 344 GLN B NE2 1 
ATOM   7001 N N   . PRO B 1 345 ? -33.493 38.263 53.576  1.00 25.54 ? 345 PRO B N   1 
ATOM   7002 C CA  . PRO B 1 345 ? -34.151 38.316 52.268  1.00 25.15 ? 345 PRO B CA  1 
ATOM   7003 C C   . PRO B 1 345 ? -33.470 37.403 51.264  1.00 24.33 ? 345 PRO B C   1 
ATOM   7004 O O   . PRO B 1 345 ? -32.260 37.173 51.327  1.00 21.83 ? 345 PRO B O   1 
ATOM   7005 C CB  . PRO B 1 345 ? -33.983 39.786 51.862  1.00 26.63 ? 345 PRO B CB  1 
ATOM   7006 C CG  . PRO B 1 345 ? -32.678 40.185 52.499  1.00 30.50 ? 345 PRO B CG  1 
ATOM   7007 C CD  . PRO B 1 345 ? -32.583 39.402 53.795  1.00 23.99 ? 345 PRO B CD  1 
ATOM   7008 N N   . VAL B 1 346 ? -34.268 36.886 50.319  1.00 19.22 ? 346 VAL B N   1 
ATOM   7009 C CA  . VAL B 1 346 ? -33.761 36.148 49.163  1.00 18.51 ? 346 VAL B CA  1 
ATOM   7010 C C   . VAL B 1 346 ? -33.868 37.050 47.938  1.00 19.17 ? 346 VAL B C   1 
ATOM   7011 O O   . VAL B 1 346 ? -34.967 37.492 47.578  1.00 18.97 ? 346 VAL B O   1 
ATOM   7012 C CB  . VAL B 1 346 ? -34.529 34.839 48.930  1.00 20.29 ? 346 VAL B CB  1 
ATOM   7013 C CG1 . VAL B 1 346 ? -33.876 34.027 47.823  1.00 17.08 ? 346 VAL B CG1 1 
ATOM   7014 C CG2 . VAL B 1 346 ? -34.564 34.039 50.178  1.00 21.69 ? 346 VAL B CG2 1 
ATOM   7015 N N   . VAL B 1 347 ? -32.740 37.285 47.276  1.00 16.80 ? 347 VAL B N   1 
ATOM   7016 C CA  . VAL B 1 347 ? -32.654 38.213 46.158  1.00 16.49 ? 347 VAL B CA  1 
ATOM   7017 C C   . VAL B 1 347 ? -32.314 37.402 44.915  1.00 15.06 ? 347 VAL B C   1 
ATOM   7018 O O   . VAL B 1 347 ? -31.166 36.974 44.746  1.00 17.04 ? 347 VAL B O   1 
ATOM   7019 C CB  . VAL B 1 347 ? -31.609 39.304 46.403  1.00 18.66 ? 347 VAL B CB  1 
ATOM   7020 C CG1 . VAL B 1 347 ? -31.597 40.280 45.226  1.00 17.06 ? 347 VAL B CG1 1 
ATOM   7021 C CG2 . VAL B 1 347 ? -31.920 40.037 47.712  1.00 25.46 ? 347 VAL B CG2 1 
ATOM   7022 N N   . PHE B 1 348 ? -33.299 37.206 44.033  1.00 14.41 ? 348 PHE B N   1 
ATOM   7023 C CA  . PHE B 1 348 ? -33.065 36.520 42.772  1.00 13.16 ? 348 PHE B CA  1 
ATOM   7024 C C   . PHE B 1 348 ? -32.639 37.524 41.711  1.00 14.15 ? 348 PHE B C   1 
ATOM   7025 O O   . PHE B 1 348 ? -33.331 38.518 41.464  1.00 15.45 ? 348 PHE B O   1 
ATOM   7026 C CB  . PHE B 1 348 ? -34.292 35.752 42.290  1.00 12.58 ? 348 PHE B CB  1 
ATOM   7027 C CG  . PHE B 1 348 ? -34.346 34.335 42.763  1.00 15.84 ? 348 PHE B CG  1 
ATOM   7028 C CD1 . PHE B 1 348 ? -34.332 34.026 44.121  1.00 15.90 ? 348 PHE B CD1 1 
ATOM   7029 C CD2 . PHE B 1 348 ? -34.275 33.311 41.847  1.00 13.51 ? 348 PHE B CD2 1 
ATOM   7030 C CE1 . PHE B 1 348 ? -34.350 32.694 44.538  1.00 15.45 ? 348 PHE B CE1 1 
ATOM   7031 C CE2 . PHE B 1 348 ? -34.273 31.982 42.244  1.00 14.67 ? 348 PHE B CE2 1 
ATOM   7032 C CZ  . PHE B 1 348 ? -34.311 31.674 43.597  1.00 11.81 ? 348 PHE B CZ  1 
ATOM   7033 N N   . VAL B 1 349 ? -31.499 37.257 41.084  1.00 12.40 ? 349 VAL B N   1 
ATOM   7034 C CA  . VAL B 1 349 ? -31.015 38.056 39.975  1.00 12.19 ? 349 VAL B CA  1 
ATOM   7035 C C   . VAL B 1 349 ? -31.068 37.156 38.759  1.00 16.73 ? 349 VAL B C   1 
ATOM   7036 O O   . VAL B 1 349 ? -30.276 36.211 38.657  1.00 14.68 ? 349 VAL B O   1 
ATOM   7037 C CB  . VAL B 1 349 ? -29.596 38.574 40.233  1.00 12.58 ? 349 VAL B CB  1 
ATOM   7038 C CG1 . VAL B 1 349 ? -29.089 39.345 39.007  1.00 12.85 ? 349 VAL B CG1 1 
ATOM   7039 C CG2 . VAL B 1 349 ? -29.577 39.449 41.503  1.00 16.73 ? 349 VAL B CG2 1 
ATOM   7040 N N   . VAL B 1 350 ? -32.035 37.394 37.868  1.00 10.77 ? 350 VAL B N   1 
ATOM   7041 C CA  . VAL B 1 350 ? -32.337 36.472 36.777  1.00 9.78  ? 350 VAL B CA  1 
ATOM   7042 C C   . VAL B 1 350 ? -32.386 37.276 35.487  1.00 9.67  ? 350 VAL B C   1 
ATOM   7043 O O   . VAL B 1 350 ? -33.133 38.258 35.396  1.00 13.36 ? 350 VAL B O   1 
ATOM   7044 C CB  . VAL B 1 350 ? -33.669 35.717 36.980  1.00 9.65  ? 350 VAL B CB  1 
ATOM   7045 C CG1 . VAL B 1 350 ? -33.838 34.613 35.908  1.00 8.65  ? 350 VAL B CG1 1 
ATOM   7046 C CG2 . VAL B 1 350 ? -33.763 35.107 38.387  1.00 12.59 ? 350 VAL B CG2 1 
ATOM   7047 N N   . LEU B 1 351 ? -31.580 36.876 34.504  1.00 8.96  ? 351 LEU B N   1 
ATOM   7048 C CA  . LEU B 1 351 ? -31.558 37.554 33.216  1.00 12.33 ? 351 LEU B CA  1 
ATOM   7049 C C   . LEU B 1 351 ? -30.886 36.635 32.217  1.00 13.02 ? 351 LEU B C   1 
ATOM   7050 O O   . LEU B 1 351 ? -30.323 35.601 32.587  1.00 10.48 ? 351 LEU B O   1 
ATOM   7051 C CB  . LEU B 1 351 ? -30.824 38.892 33.310  1.00 12.66 ? 351 LEU B CB  1 
ATOM   7052 C CG  . LEU B 1 351 ? -29.342 38.876 33.699  1.00 11.23 ? 351 LEU B CG  1 
ATOM   7053 C CD1 . LEU B 1 351 ? -28.574 39.991 32.955  1.00 13.33 ? 351 LEU B CD1 1 
ATOM   7054 C CD2 . LEU B 1 351 ? -29.172 39.046 35.200  1.00 13.03 ? 351 LEU B CD2 1 
ATOM   7055 N N   . ASP B 1 352 ? -30.960 37.016 30.939  1.00 10.86 ? 352 ASP B N   1 
ATOM   7056 C CA  . ASP B 1 352 ? -30.237 36.268 29.919  1.00 10.99 ? 352 ASP B CA  1 
ATOM   7057 C C   . ASP B 1 352 ? -28.769 36.229 30.294  1.00 9.88  ? 352 ASP B C   1 
ATOM   7058 O O   . ASP B 1 352 ? -28.203 37.233 30.730  1.00 11.49 ? 352 ASP B O   1 
ATOM   7059 C CB  . ASP B 1 352 ? -30.375 36.913 28.536  1.00 11.75 ? 352 ASP B CB  1 
ATOM   7060 C CG  . ASP B 1 352 ? -31.794 36.898 28.000  1.00 16.65 ? 352 ASP B CG  1 
ATOM   7061 O OD1 . ASP B 1 352 ? -32.691 36.256 28.595  1.00 13.62 ? 352 ASP B OD1 1 
ATOM   7062 O OD2 . ASP B 1 352 ? -31.999 37.551 26.948  1.00 14.88 ? 352 ASP B OD2 1 
ATOM   7063 N N   . GLY B 1 353 ? -28.149 35.060 30.134  1.00 10.81 ? 353 GLY B N   1 
ATOM   7064 C CA  . GLY B 1 353 ? -26.764 34.929 30.500  1.00 10.63 ? 353 GLY B CA  1 
ATOM   7065 C C   . GLY B 1 353 ? -25.754 35.187 29.412  1.00 9.79  ? 353 GLY B C   1 
ATOM   7066 O O   . GLY B 1 353 ? -24.558 35.134 29.699  1.00 8.91  ? 353 GLY B O   1 
ATOM   7067 N N   . GLU B 1 354 ? -26.171 35.512 28.194  1.00 6.11  ? 354 GLU B N   1 
ATOM   7068 C CA  . GLU B 1 354 ? -25.190 35.690 27.163  1.00 7.60  ? 354 GLU B CA  1 
ATOM   7069 C C   . GLU B 1 354 ? -25.317 36.884 26.262  1.00 11.78 ? 354 GLU B C   1 
ATOM   7070 O O   . GLU B 1 354 ? -24.545 37.019 25.378  1.00 12.21 ? 354 GLU B O   1 
ATOM   7071 C CB  . GLU B 1 354 ? -25.261 34.474 26.243  1.00 11.94 ? 354 GLU B CB  1 
ATOM   7072 C CG  . GLU B 1 354 ? -26.411 34.451 25.261  1.00 18.57 ? 354 GLU B CG  1 
ATOM   7073 C CD  . GLU B 1 354 ? -27.732 33.933 25.825  1.00 37.93 ? 354 GLU B CD  1 
ATOM   7074 O OE1 . GLU B 1 354 ? -28.227 32.905 25.397  1.00 54.43 ? 354 GLU B OE1 1 
ATOM   7075 O OE2 . GLU B 1 354 ? -28.297 34.596 26.652  1.00 37.43 ? 354 GLU B OE2 1 
ATOM   7076 N N   . ASN B 1 355 ? -26.309 37.710 26.517  1.00 8.49  ? 355 ASN B N   1 
ATOM   7077 C CA  . ASN B 1 355 ? -26.624 38.761 25.565  1.00 8.83  ? 355 ASN B CA  1 
ATOM   7078 C C   . ASN B 1 355 ? -26.081 40.124 25.958  1.00 14.33 ? 355 ASN B C   1 
ATOM   7079 O O   . ASN B 1 355 ? -25.876 40.958 25.076  1.00 13.55 ? 355 ASN B O   1 
ATOM   7080 C CB  . ASN B 1 355 ? -28.145 38.832 25.346  1.00 11.23 ? 355 ASN B CB  1 
ATOM   7081 C CG  . ASN B 1 355 ? -28.639 37.637 24.573  1.00 10.70 ? 355 ASN B CG  1 
ATOM   7082 O OD1 . ASN B 1 355 ? -27.960 37.181 23.660  1.00 11.82 ? 355 ASN B OD1 1 
ATOM   7083 N ND2 . ASN B 1 355 ? -29.749 37.060 25.002  1.00 10.19 ? 355 ASN B ND2 1 
ATOM   7084 N N   . CYS B 1 356 ? -25.784 40.354 27.233  1.00 9.33  ? 356 CYS B N   1 
ATOM   7085 C CA  . CYS B 1 356 ? -25.382 41.699 27.639  1.00 9.46  ? 356 CYS B CA  1 
ATOM   7086 C C   . CYS B 1 356 ? -23.885 41.934 27.558  1.00 11.95 ? 356 CYS B C   1 
ATOM   7087 O O   . CYS B 1 356 ? -23.462 43.089 27.418  1.00 12.17 ? 356 CYS B O   1 
ATOM   7088 C CB  . CYS B 1 356 ? -25.860 41.992 29.070  1.00 11.96 ? 356 CYS B CB  1 
ATOM   7089 S SG  . CYS B 1 356 ? -25.312 40.761 30.329  1.00 13.40 ? 356 CYS B SG  1 
ATOM   7090 N N   . TRP B 1 357 ? -23.074 40.875 27.619  1.00 11.02 ? 357 TRP B N   1 
ATOM   7091 C CA  . TRP B 1 357 ? -21.635 41.063 27.810  1.00 11.39 ? 357 TRP B CA  1 
ATOM   7092 C C   . TRP B 1 357 ? -20.952 41.708 26.612  1.00 13.18 ? 357 TRP B C   1 
ATOM   7093 O O   . TRP B 1 357 ? -19.923 42.360 26.792  1.00 10.36 ? 357 TRP B O   1 
ATOM   7094 C CB  . TRP B 1 357 ? -20.971 39.721 28.126  1.00 9.93  ? 357 TRP B CB  1 
ATOM   7095 C CG  . TRP B 1 357 ? -21.731 39.010 29.164  1.00 8.51  ? 357 TRP B CG  1 
ATOM   7096 C CD1 . TRP B 1 357 ? -22.359 37.796 29.044  1.00 9.19  ? 357 TRP B CD1 1 
ATOM   7097 C CD2 . TRP B 1 357 ? -22.005 39.480 30.485  1.00 10.98 ? 357 TRP B CD2 1 
ATOM   7098 N NE1 . TRP B 1 357 ? -22.990 37.483 30.220  1.00 9.32  ? 357 TRP B NE1 1 
ATOM   7099 C CE2 . TRP B 1 357 ? -22.795 38.503 31.118  1.00 10.54 ? 357 TRP B CE2 1 
ATOM   7100 C CE3 . TRP B 1 357 ? -21.662 40.642 31.197  1.00 10.10 ? 357 TRP B CE3 1 
ATOM   7101 C CZ2 . TRP B 1 357 ? -23.258 38.651 32.431  1.00 11.53 ? 357 TRP B CZ2 1 
ATOM   7102 C CZ3 . TRP B 1 357 ? -22.102 40.780 32.508  1.00 14.38 ? 357 TRP B CZ3 1 
ATOM   7103 C CH2 . TRP B 1 357 ? -22.895 39.789 33.106  1.00 11.94 ? 357 TRP B CH2 1 
ATOM   7104 N N   . GLU B 1 358 ? -21.477 41.516 25.396  1.00 11.93 ? 358 GLU B N   1 
ATOM   7105 C CA  . GLU B 1 358 ? -20.870 42.093 24.199  1.00 13.02 ? 358 GLU B CA  1 
ATOM   7106 C C   . GLU B 1 358 ? -20.827 43.603 24.252  1.00 12.64 ? 358 GLU B C   1 
ATOM   7107 O O   . GLU B 1 358 ? -20.027 44.209 23.532  1.00 11.32 ? 358 GLU B O   1 
ATOM   7108 C CB  . GLU B 1 358 ? -21.646 41.689 22.939  1.00 17.04 ? 358 GLU B CB  1 
ATOM   7109 C CG  . GLU B 1 358 ? -23.141 41.700 23.168  1.00 17.92 ? 358 GLU B CG  1 
ATOM   7110 C CD  . GLU B 1 358 ? -23.927 40.946 22.126  1.00 22.41 ? 358 GLU B CD  1 
ATOM   7111 O OE1 . GLU B 1 358 ? -24.336 41.461 21.060  1.00 18.56 ? 358 GLU B OE1 1 
ATOM   7112 O OE2 . GLU B 1 358 ? -24.011 39.736 22.355  1.00 16.28 ? 358 GLU B OE2 1 
ATOM   7113 N N   . TYR B 1 359 ? -21.678 44.226 25.078  1.00 10.88 ? 359 TYR B N   1 
ATOM   7114 C CA  . TYR B 1 359 ? -21.708 45.677 25.190  1.00 11.97 ? 359 TYR B CA  1 
ATOM   7115 C C   . TYR B 1 359 ? -20.807 46.214 26.295  1.00 12.77 ? 359 TYR B C   1 
ATOM   7116 O O   . TYR B 1 359 ? -20.693 47.436 26.419  1.00 13.68 ? 359 TYR B O   1 
ATOM   7117 C CB  . TYR B 1 359 ? -23.146 46.182 25.425  1.00 12.32 ? 359 TYR B CB  1 
ATOM   7118 C CG  . TYR B 1 359 ? -24.095 45.758 24.323  1.00 16.81 ? 359 TYR B CG  1 
ATOM   7119 C CD1 . TYR B 1 359 ? -24.186 46.482 23.133  1.00 24.28 ? 359 TYR B CD1 1 
ATOM   7120 C CD2 . TYR B 1 359 ? -24.863 44.608 24.454  1.00 17.99 ? 359 TYR B CD2 1 
ATOM   7121 C CE1 . TYR B 1 359 ? -25.044 46.076 22.106  1.00 22.13 ? 359 TYR B CE1 1 
ATOM   7122 C CE2 . TYR B 1 359 ? -25.722 44.202 23.437  1.00 20.34 ? 359 TYR B CE2 1 
ATOM   7123 C CZ  . TYR B 1 359 ? -25.806 44.935 22.274  1.00 21.17 ? 359 TYR B CZ  1 
ATOM   7124 O OH  . TYR B 1 359 ? -26.661 44.518 21.273  1.00 29.95 ? 359 TYR B OH  1 
ATOM   7125 N N   . TYR B 1 360 ? -20.193 45.350 27.103  1.00 12.27 ? 360 TYR B N   1 
ATOM   7126 C CA  . TYR B 1 360 ? -19.263 45.749 28.153  1.00 12.99 ? 360 TYR B CA  1 
ATOM   7127 C C   . TYR B 1 360 ? -17.843 45.777 27.615  1.00 13.14 ? 360 TYR B C   1 
ATOM   7128 O O   . TYR B 1 360 ? -17.481 44.976 26.755  1.00 12.41 ? 360 TYR B O   1 
ATOM   7129 C CB  . TYR B 1 360 ? -19.254 44.749 29.303  1.00 12.60 ? 360 TYR B CB  1 
ATOM   7130 C CG  . TYR B 1 360 ? -20.412 44.749 30.262  1.00 12.71 ? 360 TYR B CG  1 
ATOM   7131 C CD1 . TYR B 1 360 ? -21.686 44.348 29.863  1.00 12.11 ? 360 TYR B CD1 1 
ATOM   7132 C CD2 . TYR B 1 360 ? -20.210 45.050 31.597  1.00 13.45 ? 360 TYR B CD2 1 
ATOM   7133 C CE1 . TYR B 1 360 ? -22.750 44.308 30.763  1.00 12.26 ? 360 TYR B CE1 1 
ATOM   7134 C CE2 . TYR B 1 360 ? -21.261 45.010 32.503  1.00 13.88 ? 360 TYR B CE2 1 
ATOM   7135 C CZ  . TYR B 1 360 ? -22.518 44.633 32.092  1.00 13.71 ? 360 TYR B CZ  1 
ATOM   7136 O OH  . TYR B 1 360 ? -23.531 44.608 33.038  1.00 14.97 ? 360 TYR B OH  1 
ATOM   7137 N N   . GLU B 1 361 ? -17.018 46.651 28.193  1.00 14.34 ? 361 GLU B N   1 
ATOM   7138 C CA  . GLU B 1 361 ? -15.583 46.597 27.944  1.00 16.14 ? 361 GLU B CA  1 
ATOM   7139 C C   . GLU B 1 361 ? -15.049 45.197 28.218  1.00 14.64 ? 361 GLU B C   1 
ATOM   7140 O O   . GLU B 1 361 ? -15.396 44.575 29.223  1.00 16.92 ? 361 GLU B O   1 
ATOM   7141 C CB  . GLU B 1 361 ? -14.854 47.609 28.833  1.00 28.77 ? 361 GLU B CB  1 
ATOM   7142 C CG  . GLU B 1 361 ? -15.189 49.028 28.486  1.00 47.32 ? 361 GLU B CG  1 
ATOM   7143 C CD  . GLU B 1 361 ? -14.853 49.335 27.038  1.00 60.44 ? 361 GLU B CD  1 
ATOM   7144 O OE1 . GLU B 1 361 ? -13.774 48.902 26.571  1.00 64.83 ? 361 GLU B OE1 1 
ATOM   7145 O OE2 . GLU B 1 361 ? -15.676 49.987 26.361  1.00 59.93 ? 361 GLU B OE2 1 
ATOM   7146 N N   . GLU B 1 362 ? -14.211 44.705 27.308  1.00 13.59 ? 362 GLU B N   1 
ATOM   7147 C CA  . GLU B 1 362 ? -13.568 43.390 27.442  1.00 15.68 ? 362 GLU B CA  1 
ATOM   7148 C C   . GLU B 1 362 ? -14.589 42.300 27.772  1.00 16.40 ? 362 GLU B C   1 
ATOM   7149 O O   . GLU B 1 362 ? -14.318 41.379 28.554  1.00 14.22 ? 362 GLU B O   1 
ATOM   7150 C CB  . GLU B 1 362 ? -12.462 43.410 28.498  1.00 18.00 ? 362 GLU B CB  1 
ATOM   7151 C CG  . GLU B 1 362 ? -11.368 44.441 28.312  1.00 32.97 ? 362 GLU B CG  1 
ATOM   7152 C CD  . GLU B 1 362 ? -10.222 44.240 29.297  1.00 45.06 ? 362 GLU B CD  1 
ATOM   7153 O OE1 . GLU B 1 362 ? -10.151 43.160 29.924  1.00 48.81 ? 362 GLU B OE1 1 
ATOM   7154 O OE2 . GLU B 1 362 ? -9.414  45.175 29.471  1.00 54.16 ? 362 GLU B OE2 1 
ATOM   7155 N N   . ASN B 1 363 ? -15.766 42.396 27.156  1.00 14.86 ? 363 ASN B N   1 
ATOM   7156 C CA  . ASN B 1 363 ? -16.752 41.306 27.182  1.00 8.44  ? 363 ASN B CA  1 
ATOM   7157 C C   . ASN B 1 363 ? -17.222 41.018 28.606  1.00 12.43 ? 363 ASN B C   1 
ATOM   7158 O O   . ASN B 1 363 ? -17.543 39.877 28.943  1.00 10.10 ? 363 ASN B O   1 
ATOM   7159 C CB  . ASN B 1 363 ? -16.205 40.015 26.553  1.00 13.68 ? 363 ASN B CB  1 
ATOM   7160 C CG  . ASN B 1 363 ? -17.291 39.001 26.247  1.00 13.46 ? 363 ASN B CG  1 
ATOM   7161 O OD1 . ASN B 1 363 ? -18.424 39.352 25.892  1.00 13.86 ? 363 ASN B OD1 1 
ATOM   7162 N ND2 . ASN B 1 363 ? -16.959 37.722 26.429  1.00 16.52 ? 363 ASN B ND2 1 
ATOM   7163 N N   . GLY B 1 364 ? -17.260 42.046 29.453  1.00 11.53 ? 364 GLY B N   1 
ATOM   7164 C CA  . GLY B 1 364 ? -17.787 41.868 30.797  1.00 11.90 ? 364 GLY B CA  1 
ATOM   7165 C C   . GLY B 1 364 ? -16.821 41.253 31.787  1.00 15.29 ? 364 GLY B C   1 
ATOM   7166 O O   . GLY B 1 364 ? -17.189 41.057 32.954  1.00 11.80 ? 364 GLY B O   1 
ATOM   7167 N N   . ILE B 1 365 ? -15.606 40.931 31.366  1.00 12.49 ? 365 ILE B N   1 
ATOM   7168 C CA  . ILE B 1 365 ? -14.679 40.189 32.219  1.00 11.49 ? 365 ILE B CA  1 
ATOM   7169 C C   . ILE B 1 365 ? -14.200 41.068 33.373  1.00 15.05 ? 365 ILE B C   1 
ATOM   7170 O O   . ILE B 1 365 ? -14.215 40.596 34.522  1.00 16.38 ? 365 ILE B O   1 
ATOM   7171 C CB  . ILE B 1 365 ? -13.530 39.600 31.384  1.00 13.49 ? 365 ILE B CB  1 
ATOM   7172 C CG1 . ILE B 1 365 ? -14.097 38.524 30.442  1.00 14.31 ? 365 ILE B CG1 1 
ATOM   7173 C CG2 . ILE B 1 365 ? -12.457 38.989 32.274  1.00 16.90 ? 365 ILE B CG2 1 
ATOM   7174 C CD1 . ILE B 1 365 ? -13.166 38.192 29.314  1.00 16.44 ? 365 ILE B CD1 1 
ATOM   7175 N N   . PRO B 1 366 ? -13.812 42.338 33.165  1.00 13.30 ? 366 PRO B N   1 
ATOM   7176 C CA  . PRO B 1 366 ? -13.512 43.176 34.342  1.00 17.74 ? 366 PRO B CA  1 
ATOM   7177 C C   . PRO B 1 366 ? -14.673 43.276 35.311  1.00 13.81 ? 366 PRO B C   1 
ATOM   7178 O O   . PRO B 1 366 ? -14.457 43.224 36.530  1.00 14.30 ? 366 PRO B O   1 
ATOM   7179 C CB  . PRO B 1 366 ? -13.175 44.540 33.731  1.00 14.27 ? 366 PRO B CB  1 
ATOM   7180 C CG  . PRO B 1 366 ? -12.628 44.203 32.386  1.00 18.81 ? 366 PRO B CG  1 
ATOM   7181 C CD  . PRO B 1 366 ? -13.397 43.007 31.912  1.00 13.32 ? 366 PRO B CD  1 
ATOM   7182 N N   . PHE B 1 367 ? -15.899 43.437 34.802  1.00 15.75 ? 367 PHE B N   1 
ATOM   7183 C CA  . PHE B 1 367 ? -17.049 43.596 35.690  1.00 11.95 ? 367 PHE B CA  1 
ATOM   7184 C C   . PHE B 1 367 ? -17.312 42.315 36.475  1.00 14.12 ? 367 PHE B C   1 
ATOM   7185 O O   . PHE B 1 367 ? -17.422 42.336 37.711  1.00 14.52 ? 367 PHE B O   1 
ATOM   7186 C CB  . PHE B 1 367 ? -18.297 43.989 34.891  1.00 13.10 ? 367 PHE B CB  1 
ATOM   7187 C CG  . PHE B 1 367 ? -19.573 43.903 35.691  1.00 15.77 ? 367 PHE B CG  1 
ATOM   7188 C CD1 . PHE B 1 367 ? -19.899 44.887 36.612  1.00 17.87 ? 367 PHE B CD1 1 
ATOM   7189 C CD2 . PHE B 1 367 ? -20.422 42.822 35.544  1.00 14.61 ? 367 PHE B CD2 1 
ATOM   7190 C CE1 . PHE B 1 367 ? -21.078 44.814 37.369  1.00 19.09 ? 367 PHE B CE1 1 
ATOM   7191 C CE2 . PHE B 1 367 ? -21.601 42.738 36.286  1.00 17.44 ? 367 PHE B CE2 1 
ATOM   7192 C CZ  . PHE B 1 367 ? -21.929 43.734 37.200  1.00 18.87 ? 367 PHE B CZ  1 
ATOM   7193 N N   . LEU B 1 368 ? -17.403 41.183 35.773  1.00 12.28 ? 368 LEU B N   1 
ATOM   7194 C CA  . LEU B 1 368 ? -17.752 39.946 36.461  1.00 11.83 ? 368 LEU B CA  1 
ATOM   7195 C C   . LEU B 1 368 ? -16.653 39.517 37.417  1.00 11.88 ? 368 LEU B C   1 
ATOM   7196 O O   . LEU B 1 368 ? -16.939 39.024 38.515  1.00 12.27 ? 368 LEU B O   1 
ATOM   7197 C CB  . LEU B 1 368 ? -18.053 38.831 35.463  1.00 11.92 ? 368 LEU B CB  1 
ATOM   7198 C CG  . LEU B 1 368 ? -19.428 38.948 34.794  1.00 10.84 ? 368 LEU B CG  1 
ATOM   7199 C CD1 . LEU B 1 368 ? -19.662 37.784 33.813  1.00 12.34 ? 368 LEU B CD1 1 
ATOM   7200 C CD2 . LEU B 1 368 ? -20.552 39.006 35.835  1.00 11.61 ? 368 LEU B CD2 1 
ATOM   7201 N N   . GLU B 1 369 ? -15.388 39.682 37.029  1.00 12.38 ? 369 GLU B N   1 
ATOM   7202 C CA  . GLU B 1 369 ? -14.329 39.320 37.967  1.00 13.47 ? 369 GLU B CA  1 
ATOM   7203 C C   . GLU B 1 369 ? -14.371 40.201 39.211  1.00 16.10 ? 369 GLU B C   1 
ATOM   7204 O O   . GLU B 1 369 ? -14.149 39.718 40.326  1.00 17.52 ? 369 GLU B O   1 
ATOM   7205 C CB  . GLU B 1 369 ? -12.959 39.390 37.288  1.00 18.13 ? 369 GLU B CB  1 
ATOM   7206 C CG  . GLU B 1 369 ? -12.769 38.256 36.277  1.00 14.32 ? 369 GLU B CG  1 
ATOM   7207 C CD  . GLU B 1 369 ? -11.391 38.248 35.637  1.00 21.70 ? 369 GLU B CD  1 
ATOM   7208 O OE1 . GLU B 1 369 ? -10.630 39.222 35.813  1.00 21.22 ? 369 GLU B OE1 1 
ATOM   7209 O OE2 . GLU B 1 369 ? -11.068 37.256 34.953  1.00 22.59 ? 369 GLU B OE2 1 
ATOM   7210 N N   . LYS B 1 370 ? -14.637 41.500 39.044  1.00 15.93 ? 370 LYS B N   1 
ATOM   7211 C CA  . LYS B 1 370 ? -14.722 42.382 40.205  1.00 16.37 ? 370 LYS B CA  1 
ATOM   7212 C C   . LYS B 1 370 ? -15.945 42.055 41.052  1.00 17.46 ? 370 LYS B C   1 
ATOM   7213 O O   . LYS B 1 370 ? -15.871 42.068 42.288  1.00 17.80 ? 370 LYS B O   1 
ATOM   7214 C CB  . LYS B 1 370 ? -14.757 43.847 39.765  1.00 19.08 ? 370 LYS B CB  1 
ATOM   7215 C CG  . LYS B 1 370 ? -14.736 44.833 40.934  1.00 25.58 ? 370 LYS B CG  1 
ATOM   7216 C CD  . LYS B 1 370 ? -13.371 44.839 41.619  1.00 41.92 ? 370 LYS B CD  1 
ATOM   7217 C CE  . LYS B 1 370 ? -13.303 45.863 42.748  1.00 52.72 ? 370 LYS B CE  1 
ATOM   7218 N NZ  . LYS B 1 370 ? -11.984 45.865 43.455  1.00 57.22 ? 370 LYS B NZ  1 
ATOM   7219 N N   . LEU B 1 371 ? -17.070 41.735 40.400  1.00 15.18 ? 371 LEU B N   1 
ATOM   7220 C CA  . LEU B 1 371 ? -18.304 41.415 41.116  1.00 13.63 ? 371 LEU B CA  1 
ATOM   7221 C C   . LEU B 1 371 ? -18.157 40.137 41.929  1.00 18.17 ? 371 LEU B C   1 
ATOM   7222 O O   . LEU B 1 371 ? -18.470 40.108 43.125  1.00 19.82 ? 371 LEU B O   1 
ATOM   7223 C CB  . LEU B 1 371 ? -19.460 41.273 40.126  1.00 12.47 ? 371 LEU B CB  1 
ATOM   7224 C CG  . LEU B 1 371 ? -20.788 40.838 40.755  1.00 16.05 ? 371 LEU B CG  1 
ATOM   7225 C CD1 . LEU B 1 371 ? -21.332 41.946 41.683  1.00 18.35 ? 371 LEU B CD1 1 
ATOM   7226 C CD2 . LEU B 1 371 ? -21.797 40.482 39.677  1.00 17.04 ? 371 LEU B CD2 1 
ATOM   7227 N N   . TYR B 1 372 ? -17.721 39.059 41.279  1.00 16.01 ? 372 TYR B N   1 
ATOM   7228 C CA  . TYR B 1 372 ? -17.569 37.779 41.961  1.00 14.19 ? 372 TYR B CA  1 
ATOM   7229 C C   . TYR B 1 372 ? -16.497 37.843 43.044  1.00 17.85 ? 372 TYR B C   1 
ATOM   7230 O O   . TYR B 1 372 ? -16.659 37.257 44.123  1.00 17.82 ? 372 TYR B O   1 
ATOM   7231 C CB  . TYR B 1 372 ? -17.228 36.701 40.942  1.00 13.45 ? 372 TYR B CB  1 
ATOM   7232 C CG  . TYR B 1 372 ? -18.332 36.426 39.949  1.00 17.06 ? 372 TYR B CG  1 
ATOM   7233 C CD1 . TYR B 1 372 ? -19.660 36.782 40.212  1.00 13.18 ? 372 TYR B CD1 1 
ATOM   7234 C CD2 . TYR B 1 372 ? -18.052 35.795 38.745  1.00 15.88 ? 372 TYR B CD2 1 
ATOM   7235 C CE1 . TYR B 1 372 ? -20.676 36.511 39.283  1.00 13.86 ? 372 TYR B CE1 1 
ATOM   7236 C CE2 . TYR B 1 372 ? -19.042 35.528 37.829  1.00 12.01 ? 372 TYR B CE2 1 
ATOM   7237 C CZ  . TYR B 1 372 ? -20.355 35.883 38.097  1.00 12.24 ? 372 TYR B CZ  1 
ATOM   7238 O OH  . TYR B 1 372 ? -21.331 35.595 37.176  1.00 13.53 ? 372 TYR B OH  1 
ATOM   7239 N N   . SER B 1 373 ? -15.386 38.531 42.770  1.00 19.12 ? 373 SER B N   1 
ATOM   7240 C CA  . SER B 1 373 ? -14.339 38.626 43.781  1.00 23.07 ? 373 SER B CA  1 
ATOM   7241 C C   . SER B 1 373 ? -14.809 39.447 44.978  1.00 23.64 ? 373 SER B C   1 
ATOM   7242 O O   . SER B 1 373 ? -14.478 39.123 46.125  1.00 23.62 ? 373 SER B O   1 
ATOM   7243 C CB  . SER B 1 373 ? -13.058 39.210 43.182  1.00 27.89 ? 373 SER B CB  1 
ATOM   7244 O OG  . SER B 1 373 ? -13.192 40.587 42.897  1.00 31.47 ? 373 SER B OG  1 
ATOM   7245 N N   . THR B 1 374 ? -15.603 40.491 44.732  1.00 20.17 ? 374 THR B N   1 
ATOM   7246 C CA  . THR B 1 374 ? -16.144 41.278 45.836  1.00 21.80 ? 374 THR B CA  1 
ATOM   7247 C C   . THR B 1 374 ? -17.163 40.478 46.638  1.00 25.84 ? 374 THR B C   1 
ATOM   7248 O O   . THR B 1 374 ? -17.165 40.535 47.873  1.00 23.00 ? 374 THR B O   1 
ATOM   7249 C CB  . THR B 1 374 ? -16.767 42.572 45.305  1.00 23.19 ? 374 THR B CB  1 
ATOM   7250 O OG1 . THR B 1 374 ? -15.753 43.360 44.657  1.00 18.07 ? 374 THR B OG1 1 
ATOM   7251 C CG2 . THR B 1 374 ? -17.373 43.378 46.445  1.00 24.89 ? 374 THR B CG2 1 
ATOM   7252 N N   . LEU B 1 375 ? -18.036 39.723 45.956  1.00 22.33 ? 375 LEU B N   1 
ATOM   7253 C CA  . LEU B 1 375 ? -19.021 38.902 46.662  1.00 22.57 ? 375 LEU B CA  1 
ATOM   7254 C C   . LEU B 1 375 ? -18.357 37.839 47.531  1.00 25.68 ? 375 LEU B C   1 
ATOM   7255 O O   . LEU B 1 375 ? -18.877 37.494 48.600  1.00 27.48 ? 375 LEU B O   1 
ATOM   7256 C CB  . LEU B 1 375 ? -19.972 38.245 45.664  1.00 18.66 ? 375 LEU B CB  1 
ATOM   7257 C CG  . LEU B 1 375 ? -20.966 39.183 44.989  1.00 20.43 ? 375 LEU B CG  1 
ATOM   7258 C CD1 . LEU B 1 375 ? -21.658 38.451 43.843  1.00 19.07 ? 375 LEU B CD1 1 
ATOM   7259 C CD2 . LEU B 1 375 ? -21.994 39.693 45.987  1.00 23.38 ? 375 LEU B CD2 1 
ATOM   7260 N N   . GLU B 1 376 ? -17.210 37.313 47.092  1.00 26.74 ? 376 GLU B N   1 
ATOM   7261 C CA  . GLU B 1 376 ? -16.482 36.330 47.882  1.00 29.78 ? 376 GLU B CA  1 
ATOM   7262 C C   . GLU B 1 376 ? -16.167 36.845 49.281  1.00 35.85 ? 376 GLU B C   1 
ATOM   7263 O O   . GLU B 1 376 ? -16.025 36.050 50.214  1.00 39.35 ? 376 GLU B O   1 
ATOM   7264 C CB  . GLU B 1 376 ? -15.174 35.945 47.180  1.00 28.46 ? 376 GLU B CB  1 
ATOM   7265 C CG  . GLU B 1 376 ? -15.261 34.807 46.186  1.00 34.68 ? 376 GLU B CG  1 
ATOM   7266 C CD  . GLU B 1 376 ? -13.919 34.527 45.532  1.00 42.82 ? 376 GLU B CD  1 
ATOM   7267 O OE1 . GLU B 1 376 ? -13.075 35.446 45.492  1.00 44.90 ? 376 GLU B OE1 1 
ATOM   7268 O OE2 . GLU B 1 376 ? -13.686 33.384 45.092  1.00 46.79 ? 376 GLU B OE2 1 
ATOM   7269 N N   . LYS B 1 377 ? -16.070 38.165 49.448  1.00 29.46 ? 377 LYS B N   1 
ATOM   7270 C CA  . LYS B 1 377 ? -15.534 38.755 50.672  1.00 33.82 ? 377 LYS B CA  1 
ATOM   7271 C C   . LYS B 1 377 ? -16.603 39.380 51.564  1.00 37.38 ? 377 LYS B C   1 
ATOM   7272 O O   . LYS B 1 377 ? -16.255 40.016 52.562  1.00 43.66 ? 377 LYS B O   1 
ATOM   7273 C CB  . LYS B 1 377 ? -14.483 39.810 50.329  1.00 33.79 ? 377 LYS B CB  1 
ATOM   7274 C CG  . LYS B 1 377 ? -13.206 39.282 49.693  1.00 39.93 ? 377 LYS B CG  1 
ATOM   7275 C CD  . LYS B 1 377 ? -12.206 40.422 49.598  1.00 53.44 ? 377 LYS B CD  1 
ATOM   7276 C CE  . LYS B 1 377 ? -10.861 39.979 49.057  1.00 62.05 ? 377 LYS B CE  1 
ATOM   7277 N NZ  . LYS B 1 377 ? -9.860  41.085 49.159  1.00 65.52 ? 377 LYS B NZ  1 
ATOM   7278 N N   . GLU B 1 378 ? -17.887 39.247 51.226  1.00 30.67 ? 378 GLU B N   1 
ATOM   7279 C CA  . GLU B 1 378 ? -18.961 39.797 52.045  1.00 33.39 ? 378 GLU B CA  1 
ATOM   7280 C C   . GLU B 1 378 ? -19.506 38.673 52.917  1.00 35.52 ? 378 GLU B C   1 
ATOM   7281 O O   . GLU B 1 378 ? -20.142 37.741 52.411  1.00 36.27 ? 378 GLU B O   1 
ATOM   7282 C CB  . GLU B 1 378 ? -20.072 40.409 51.201  1.00 36.01 ? 378 GLU B CB  1 
ATOM   7283 C CG  . GLU B 1 378 ? -19.649 41.464 50.185  1.00 35.96 ? 378 GLU B CG  1 
ATOM   7284 C CD  . GLU B 1 378 ? -19.207 42.787 50.788  1.00 45.88 ? 378 GLU B CD  1 
ATOM   7285 O OE1 . GLU B 1 378 ? -19.505 43.062 51.971  1.00 44.24 ? 378 GLU B OE1 1 
ATOM   7286 O OE2 . GLU B 1 378 ? -18.601 43.582 50.036  1.00 47.31 ? 378 GLU B OE2 1 
ATOM   7287 N N   . GLU B 1 379 ? -19.239 38.765 54.225  1.00 33.30 ? 379 GLU B N   1 
ATOM   7288 C CA  . GLU B 1 379 ? -19.766 37.800 55.184  1.00 31.93 ? 379 GLU B CA  1 
ATOM   7289 C C   . GLU B 1 379 ? -21.287 37.777 55.197  1.00 29.26 ? 379 GLU B C   1 
ATOM   7290 O O   . GLU B 1 379 ? -21.898 36.734 55.470  1.00 29.81 ? 379 GLU B O   1 
ATOM   7291 C CB  . GLU B 1 379 ? -19.288 38.138 56.593  1.00 37.11 ? 379 GLU B CB  1 
ATOM   7292 C CG  . GLU B 1 379 ? -18.728 36.987 57.350  1.00 47.26 ? 379 GLU B CG  1 
ATOM   7293 C CD  . GLU B 1 379 ? -18.088 37.428 58.649  1.00 59.43 ? 379 GLU B CD  1 
ATOM   7294 O OE1 . GLU B 1 379 ? -18.829 37.627 59.634  1.00 63.71 ? 379 GLU B OE1 1 
ATOM   7295 O OE2 . GLU B 1 379 ? -16.855 37.603 58.685  1.00 61.02 ? 379 GLU B OE2 1 
ATOM   7296 N N   . TRP B 1 380 ? -21.915 38.929 54.998  1.00 27.22 ? 380 TRP B N   1 
ATOM   7297 C CA  . TRP B 1 380 ? -23.354 39.094 55.180  1.00 22.90 ? 380 TRP B CA  1 
ATOM   7298 C C   . TRP B 1 380 ? -24.151 38.753 53.922  1.00 21.29 ? 380 TRP B C   1 
ATOM   7299 O O   . TRP B 1 380 ? -25.383 38.812 53.948  1.00 26.93 ? 380 TRP B O   1 
ATOM   7300 C CB  . TRP B 1 380 ? -23.654 40.532 55.613  1.00 25.62 ? 380 TRP B CB  1 
ATOM   7301 C CG  . TRP B 1 380 ? -23.111 41.533 54.626  1.00 28.24 ? 380 TRP B CG  1 
ATOM   7302 C CD1 . TRP B 1 380 ? -21.812 41.965 54.517  1.00 28.32 ? 380 TRP B CD1 1 
ATOM   7303 C CD2 . TRP B 1 380 ? -23.844 42.204 53.595  1.00 30.62 ? 380 TRP B CD2 1 
ATOM   7304 N NE1 . TRP B 1 380 ? -21.700 42.873 53.488  1.00 28.69 ? 380 TRP B NE1 1 
ATOM   7305 C CE2 . TRP B 1 380 ? -22.930 43.034 52.902  1.00 30.09 ? 380 TRP B CE2 1 
ATOM   7306 C CE3 . TRP B 1 380 ? -25.188 42.194 53.194  1.00 24.97 ? 380 TRP B CE3 1 
ATOM   7307 C CZ2 . TRP B 1 380 ? -23.316 43.841 51.832  1.00 30.39 ? 380 TRP B CZ2 1 
ATOM   7308 C CZ3 . TRP B 1 380 ? -25.567 42.994 52.124  1.00 28.13 ? 380 TRP B CZ3 1 
ATOM   7309 C CH2 . TRP B 1 380 ? -24.635 43.809 51.459  1.00 25.23 ? 380 TRP B CH2 1 
ATOM   7310 N N   . ILE B 1 381 ? -23.472 38.422 52.827  1.00 20.42 ? 381 ILE B N   1 
ATOM   7311 C CA  . ILE B 1 381 ? -24.091 37.896 51.613  1.00 24.42 ? 381 ILE B CA  1 
ATOM   7312 C C   . ILE B 1 381 ? -23.701 36.432 51.493  1.00 22.43 ? 381 ILE B C   1 
ATOM   7313 O O   . ILE B 1 381 ? -22.515 36.094 51.573  1.00 28.64 ? 381 ILE B O   1 
ATOM   7314 C CB  . ILE B 1 381 ? -23.647 38.669 50.359  1.00 18.07 ? 381 ILE B CB  1 
ATOM   7315 C CG1 . ILE B 1 381 ? -24.044 40.141 50.440  1.00 25.52 ? 381 ILE B CG1 1 
ATOM   7316 C CG2 . ILE B 1 381 ? -24.248 38.017 49.087  1.00 16.86 ? 381 ILE B CG2 1 
ATOM   7317 C CD1 . ILE B 1 381 ? -23.363 41.002 49.376  1.00 22.64 ? 381 ILE B CD1 1 
ATOM   7318 N N   . GLU B 1 382 ? -24.688 35.563 51.303  1.00 21.02 ? 382 GLU B N   1 
ATOM   7319 C CA  . GLU B 1 382 ? -24.432 34.164 50.985  1.00 23.87 ? 382 GLU B CA  1 
ATOM   7320 C C   . GLU B 1 382 ? -25.101 33.870 49.650  1.00 22.73 ? 382 GLU B C   1 
ATOM   7321 O O   . GLU B 1 382 ? -26.329 33.957 49.543  1.00 19.36 ? 382 GLU B O   1 
ATOM   7322 C CB  . GLU B 1 382 ? -24.956 33.233 52.081  1.00 25.34 ? 382 GLU B CB  1 
ATOM   7323 C CG  . GLU B 1 382 ? -24.735 31.755 51.780  1.00 35.24 ? 382 GLU B CG  1 
ATOM   7324 C CD  . GLU B 1 382 ? -25.195 30.854 52.911  1.00 50.90 ? 382 GLU B CD  1 
ATOM   7325 O OE1 . GLU B 1 382 ? -25.664 31.384 53.941  1.00 55.39 ? 382 GLU B OE1 1 
ATOM   7326 O OE2 . GLU B 1 382 ? -25.083 29.617 52.768  1.00 56.26 ? 382 GLU B OE2 1 
ATOM   7327 N N   . THR B 1 383 ? -24.300 33.571 48.624  1.00 22.87 ? 383 THR B N   1 
ATOM   7328 C CA  . THR B 1 383 ? -24.871 33.145 47.355  1.00 19.94 ? 383 THR B CA  1 
ATOM   7329 C C   . THR B 1 383 ? -25.360 31.713 47.493  1.00 16.58 ? 383 THR B C   1 
ATOM   7330 O O   . THR B 1 383 ? -24.757 30.904 48.207  1.00 20.89 ? 383 THR B O   1 
ATOM   7331 C CB  . THR B 1 383 ? -23.859 33.253 46.212  1.00 18.75 ? 383 THR B CB  1 
ATOM   7332 O OG1 . THR B 1 383 ? -22.660 32.543 46.546  1.00 19.77 ? 383 THR B OG1 1 
ATOM   7333 C CG2 . THR B 1 383 ? -23.538 34.734 45.907  1.00 16.87 ? 383 THR B CG2 1 
ATOM   7334 N N   . LEU B 1 384 ? -26.476 31.411 46.834  1.00 19.38 ? 384 LEU B N   1 
ATOM   7335 C CA  . LEU B 1 384 ? -27.111 30.111 46.952  1.00 15.48 ? 384 LEU B CA  1 
ATOM   7336 C C   . LEU B 1 384 ? -27.261 29.425 45.597  1.00 14.67 ? 384 LEU B C   1 
ATOM   7337 O O   . LEU B 1 384 ? -27.423 30.070 44.561  1.00 13.66 ? 384 LEU B O   1 
ATOM   7338 C CB  . LEU B 1 384 ? -28.503 30.218 47.597  1.00 15.75 ? 384 LEU B CB  1 
ATOM   7339 C CG  . LEU B 1 384 ? -28.676 30.817 48.994  1.00 21.20 ? 384 LEU B CG  1 
ATOM   7340 C CD1 . LEU B 1 384 ? -30.144 30.704 49.401  1.00 19.01 ? 384 LEU B CD1 1 
ATOM   7341 C CD2 . LEU B 1 384 ? -27.774 30.108 50.007  1.00 20.30 ? 384 LEU B CD2 1 
ATOM   7342 N N   . THR B 1 385 ? -27.249 28.095 45.624  1.00 16.58 ? 385 THR B N   1 
ATOM   7343 C CA  . THR B 1 385 ? -27.740 27.343 44.480  1.00 14.70 ? 385 THR B CA  1 
ATOM   7344 C C   . THR B 1 385 ? -29.262 27.354 44.491  1.00 14.73 ? 385 THR B C   1 
ATOM   7345 O O   . THR B 1 385 ? -29.888 27.714 45.490  1.00 15.05 ? 385 THR B O   1 
ATOM   7346 C CB  . THR B 1 385 ? -27.238 25.903 44.517  1.00 19.87 ? 385 THR B CB  1 
ATOM   7347 O OG1 . THR B 1 385 ? -27.864 25.206 45.609  1.00 24.06 ? 385 THR B OG1 1 
ATOM   7348 C CG2 . THR B 1 385 ? -25.721 25.867 44.683  1.00 23.56 ? 385 THR B CG2 1 
ATOM   7349 N N   . LEU B 1 386 ? -29.870 26.941 43.370  1.00 14.94 ? 386 LEU B N   1 
ATOM   7350 C CA  . LEU B 1 386 ? -31.333 26.869 43.327  1.00 17.32 ? 386 LEU B CA  1 
ATOM   7351 C C   . LEU B 1 386 ? -31.878 25.891 44.372  1.00 21.32 ? 386 LEU B C   1 
ATOM   7352 O O   . LEU B 1 386 ? -32.888 26.182 45.030  1.00 17.69 ? 386 LEU B O   1 
ATOM   7353 C CB  . LEU B 1 386 ? -31.802 26.479 41.923  1.00 14.74 ? 386 LEU B CB  1 
ATOM   7354 C CG  . LEU B 1 386 ? -31.426 27.479 40.817  1.00 15.23 ? 386 LEU B CG  1 
ATOM   7355 C CD1 . LEU B 1 386 ? -31.890 26.963 39.467  1.00 13.05 ? 386 LEU B CD1 1 
ATOM   7356 C CD2 . LEU B 1 386 ? -31.990 28.889 41.097  1.00 15.16 ? 386 LEU B CD2 1 
ATOM   7357 N N   . GLU B 1 387 ? -31.244 24.717 44.522  1.00 22.88 ? 387 GLU B N   1 
ATOM   7358 C CA  . GLU B 1 387 ? -31.686 23.785 45.558  1.00 25.09 ? 387 GLU B CA  1 
ATOM   7359 C C   . GLU B 1 387 ? -31.662 24.427 46.929  1.00 23.96 ? 387 GLU B C   1 
ATOM   7360 O O   . GLU B 1 387 ? -32.589 24.245 47.728  1.00 21.63 ? 387 GLU B O   1 
ATOM   7361 C CB  . GLU B 1 387 ? -30.838 22.509 45.603  1.00 36.85 ? 387 GLU B CB  1 
ATOM   7362 C CG  . GLU B 1 387 ? -30.352 21.970 44.301  1.00 53.84 ? 387 GLU B CG  1 
ATOM   7363 C CD  . GLU B 1 387 ? -31.291 20.897 43.761  1.00 70.62 ? 387 GLU B CD  1 
ATOM   7364 O OE1 . GLU B 1 387 ? -32.357 20.660 44.380  1.00 75.55 ? 387 GLU B OE1 1 
ATOM   7365 O OE2 . GLU B 1 387 ? -30.946 20.260 42.741  1.00 73.17 ? 387 GLU B OE2 1 
ATOM   7366 N N   . GLU B 1 388 ? -30.590 25.150 47.233  1.00 21.92 ? 388 GLU B N   1 
ATOM   7367 C CA  . GLU B 1 388 ? -30.459 25.767 48.549  1.00 21.64 ? 388 GLU B CA  1 
ATOM   7368 C C   . GLU B 1 388 ? -31.547 26.811 48.774  1.00 24.86 ? 388 GLU B C   1 
ATOM   7369 O O   . GLU B 1 388 ? -32.140 26.881 49.859  1.00 22.11 ? 388 GLU B O   1 
ATOM   7370 C CB  . GLU B 1 388 ? -29.060 26.367 48.677  1.00 21.16 ? 388 GLU B CB  1 
ATOM   7371 C CG  . GLU B 1 388 ? -27.999 25.286 48.788  1.00 24.88 ? 388 GLU B CG  1 
ATOM   7372 C CD  . GLU B 1 388 ? -26.585 25.827 48.695  1.00 30.37 ? 388 GLU B CD  1 
ATOM   7373 O OE1 . GLU B 1 388 ? -26.397 26.980 48.244  1.00 23.15 ? 388 GLU B OE1 1 
ATOM   7374 O OE2 . GLU B 1 388 ? -25.655 25.097 49.094  1.00 32.97 ? 388 GLU B OE2 1 
ATOM   7375 N N   . ALA B 1 389 ? -31.843 27.614 47.747  1.00 20.24 ? 389 ALA B N   1 
ATOM   7376 C CA  . ALA B 1 389 ? -32.919 28.593 47.866  1.00 21.31 ? 389 ALA B CA  1 
ATOM   7377 C C   . ALA B 1 389 ? -34.262 27.902 48.027  1.00 20.61 ? 389 ALA B C   1 
ATOM   7378 O O   . ALA B 1 389 ? -35.108 28.355 48.802  1.00 21.73 ? 389 ALA B O   1 
ATOM   7379 C CB  . ALA B 1 389 ? -32.943 29.521 46.645  1.00 17.95 ? 389 ALA B CB  1 
ATOM   7380 N N   . MET B 1 390 ? -34.454 26.784 47.331  1.00 20.19 ? 390 MET B N   1 
ATOM   7381 C CA  . MET B 1 390 ? -35.714 26.056 47.402  1.00 24.02 ? 390 MET B CA  1 
ATOM   7382 C C   . MET B 1 390 ? -35.940 25.480 48.791  1.00 26.61 ? 390 MET B C   1 
ATOM   7383 O O   . MET B 1 390 ? -37.087 25.389 49.242  1.00 27.48 ? 390 MET B O   1 
ATOM   7384 C CB  . MET B 1 390 ? -35.726 24.957 46.335  1.00 22.20 ? 390 MET B CB  1 
ATOM   7385 C CG  . MET B 1 390 ? -36.914 24.012 46.382  1.00 34.19 ? 390 MET B CG  1 
ATOM   7386 S SD  . MET B 1 390 ? -36.937 22.959 44.912  1.00 37.12 ? 390 MET B SD  1 
ATOM   7387 C CE  . MET B 1 390 ? -35.285 22.275 44.980  1.00 43.63 ? 390 MET B CE  1 
ATOM   7388 N N   . ARG B 1 391 ? -34.863 25.168 49.516  1.00 23.03 ? 391 ARG B N   1 
ATOM   7389 C CA  . ARG B 1 391 ? -34.952 24.443 50.778  1.00 29.88 ? 391 ARG B CA  1 
ATOM   7390 C C   . ARG B 1 391 ? -34.512 25.231 52.007  1.00 30.30 ? 391 ARG B C   1 
ATOM   7391 O O   . ARG B 1 391 ? -34.639 24.712 53.123  1.00 29.93 ? 391 ARG B O   1 
ATOM   7392 C CB  . ARG B 1 391 ? -34.130 23.154 50.678  1.00 32.90 ? 391 ARG B CB  1 
ATOM   7393 C CG  . ARG B 1 391 ? -34.816 22.106 49.817  1.00 40.01 ? 391 ARG B CG  1 
ATOM   7394 C CD  . ARG B 1 391 ? -34.089 20.790 49.799  1.00 50.22 ? 391 ARG B CD  1 
ATOM   7395 N NE  . ARG B 1 391 ? -34.013 20.255 48.442  1.00 58.76 ? 391 ARG B NE  1 
ATOM   7396 C CZ  . ARG B 1 391 ? -32.912 19.749 47.897  1.00 65.44 ? 391 ARG B CZ  1 
ATOM   7397 N NH1 . ARG B 1 391 ? -31.785 19.702 48.596  1.00 69.46 ? 391 ARG B NH1 1 
ATOM   7398 N NH2 . ARG B 1 391 ? -32.940 19.280 46.655  1.00 65.10 ? 391 ARG B NH2 1 
ATOM   7399 N N   . LYS B 1 392 ? -33.999 26.451 51.854  1.00 31.02 ? 392 LYS B N   1 
ATOM   7400 C CA  . LYS B 1 392 ? -33.544 27.211 53.021  1.00 36.81 ? 392 LYS B CA  1 
ATOM   7401 C C   . LYS B 1 392 ? -34.696 27.415 54.004  1.00 34.87 ? 392 LYS B C   1 
ATOM   7402 O O   . LYS B 1 392 ? -35.778 27.874 53.627  1.00 32.41 ? 392 LYS B O   1 
ATOM   7403 C CB  . LYS B 1 392 ? -32.966 28.565 52.599  1.00 40.29 ? 392 LYS B CB  1 
ATOM   7404 C CG  . LYS B 1 392 ? -31.438 28.605 52.469  1.00 49.54 ? 392 LYS B CG  1 
ATOM   7405 C CD  . LYS B 1 392 ? -30.764 28.901 53.803  1.00 53.36 ? 392 LYS B CD  1 
ATOM   7406 C CE  . LYS B 1 392 ? -29.247 28.852 53.684  1.00 53.59 ? 392 LYS B CE  1 
ATOM   7407 N NZ  . LYS B 1 392 ? -28.832 27.607 52.962  1.00 58.70 ? 392 LYS B NZ  1 
ATOM   7408 N N   . GLU B 1 393 ? -34.469 27.061 55.269  1.00 38.40 ? 393 GLU B N   1 
ATOM   7409 C CA  . GLU B 1 393 ? -35.549 27.156 56.247  1.00 39.97 ? 393 GLU B CA  1 
ATOM   7410 C C   . GLU B 1 393 ? -35.638 28.537 56.880  1.00 35.46 ? 393 GLU B C   1 
ATOM   7411 O O   . GLU B 1 393 ? -36.743 29.012 57.162  1.00 37.24 ? 393 GLU B O   1 
ATOM   7412 C CB  . GLU B 1 393 ? -35.386 26.114 57.358  1.00 46.15 ? 393 GLU B CB  1 
ATOM   7413 C CG  . GLU B 1 393 ? -34.813 24.775 56.920  1.00 56.31 ? 393 GLU B CG  1 
ATOM   7414 C CD  . GLU B 1 393 ? -35.422 23.595 57.661  1.00 67.30 ? 393 GLU B CD  1 
ATOM   7415 O OE1 . GLU B 1 393 ? -34.735 22.558 57.800  1.00 70.06 ? 393 GLU B OE1 1 
ATOM   7416 O OE2 . GLU B 1 393 ? -36.600 23.689 58.069  1.00 70.63 ? 393 GLU B OE2 1 
ATOM   7417 N N   . ASP B 1 394 ? -34.500 29.186 57.095  1.00 32.67 ? 394 ASP B N   1 
ATOM   7418 C CA  . ASP B 1 394 ? -34.441 30.435 57.845  1.00 33.10 ? 394 ASP B CA  1 
ATOM   7419 C C   . ASP B 1 394 ? -34.795 31.603 56.939  1.00 38.14 ? 394 ASP B C   1 
ATOM   7420 O O   . ASP B 1 394 ? -34.041 32.570 56.811  1.00 36.40 ? 394 ASP B O   1 
ATOM   7421 C CB  . ASP B 1 394 ? -33.048 30.613 58.453  1.00 36.84 ? 394 ASP B CB  1 
ATOM   7422 C CG  . ASP B 1 394 ? -31.938 30.400 57.435  1.00 44.65 ? 394 ASP B CG  1 
ATOM   7423 O OD1 . ASP B 1 394 ? -32.237 29.887 56.336  1.00 45.90 ? 394 ASP B OD1 1 
ATOM   7424 O OD2 . ASP B 1 394 ? -30.770 30.752 57.726  1.00 45.85 ? 394 ASP B OD2 1 
ATOM   7425 N N   . VAL B 1 395 ? -35.956 31.517 56.302  1.00 38.04 ? 395 VAL B N   1 
ATOM   7426 C CA  . VAL B 1 395 ? -36.333 32.463 55.272  1.00 28.93 ? 395 VAL B CA  1 
ATOM   7427 C C   . VAL B 1 395 ? -37.813 32.772 55.436  1.00 34.53 ? 395 VAL B C   1 
ATOM   7428 O O   . VAL B 1 395 ? -38.563 32.006 56.041  1.00 33.82 ? 395 VAL B O   1 
ATOM   7429 C CB  . VAL B 1 395 ? -36.010 31.894 53.876  1.00 31.10 ? 395 VAL B CB  1 
ATOM   7430 C CG1 . VAL B 1 395 ? -37.143 31.020 53.330  1.00 29.71 ? 395 VAL B CG1 1 
ATOM   7431 C CG2 . VAL B 1 395 ? -35.675 32.961 52.993  1.00 36.73 ? 395 VAL B CG2 1 
ATOM   7432 N N   . LYS B 1 396 ? -38.236 33.920 54.920  1.00 25.82 ? 396 LYS B N   1 
ATOM   7433 C CA  . LYS B 1 396 ? -39.628 34.312 55.082  1.00 24.35 ? 396 LYS B CA  1 
ATOM   7434 C C   . LYS B 1 396 ? -40.470 33.847 53.902  1.00 21.36 ? 396 LYS B C   1 
ATOM   7435 O O   . LYS B 1 396 ? -40.053 33.973 52.750  1.00 21.48 ? 396 LYS B O   1 
ATOM   7436 C CB  . LYS B 1 396 ? -39.761 35.822 55.232  1.00 30.03 ? 396 LYS B CB  1 
ATOM   7437 C CG  . LYS B 1 396 ? -41.171 36.195 55.595  1.00 36.69 ? 396 LYS B CG  1 
ATOM   7438 C CD  . LYS B 1 396 ? -41.327 37.667 55.828  1.00 43.54 ? 396 LYS B CD  1 
ATOM   7439 C CE  . LYS B 1 396 ? -42.730 37.928 56.300  1.00 46.54 ? 396 LYS B CE  1 
ATOM   7440 N NZ  . LYS B 1 396 ? -43.003 39.366 56.484  1.00 44.67 ? 396 LYS B NZ  1 
ATOM   7441 N N   . THR B 1 397 ? -41.674 33.337 54.188  1.00 25.73 ? 397 THR B N   1 
ATOM   7442 C CA  . THR B 1 397 ? -42.536 32.765 53.155  1.00 23.90 ? 397 THR B CA  1 
ATOM   7443 C C   . THR B 1 397 ? -43.940 33.367 53.214  1.00 23.32 ? 397 THR B C   1 
ATOM   7444 O O   . THR B 1 397 ? -44.356 33.935 54.226  1.00 27.60 ? 397 THR B O   1 
ATOM   7445 C CB  . THR B 1 397 ? -42.648 31.236 53.285  1.00 24.31 ? 397 THR B CB  1 
ATOM   7446 O OG1 . THR B 1 397 ? -43.399 30.904 54.462  1.00 27.81 ? 397 THR B OG1 1 
ATOM   7447 C CG2 . THR B 1 397 ? -41.272 30.594 53.369  1.00 25.90 ? 397 THR B CG2 1 
ATOM   7448 N N   . GLU B 1 398 ? -44.684 33.205 52.120  1.00 22.21 ? 398 GLU B N   1 
ATOM   7449 C CA  . GLU B 1 398 ? -46.057 33.686 52.016  1.00 22.16 ? 398 GLU B CA  1 
ATOM   7450 C C   . GLU B 1 398 ? -46.792 32.833 50.985  1.00 24.07 ? 398 GLU B C   1 
ATOM   7451 O O   . GLU B 1 398 ? -46.183 32.351 50.030  1.00 20.95 ? 398 GLU B O   1 
ATOM   7452 C CB  . GLU B 1 398 ? -46.089 35.168 51.626  1.00 29.59 ? 398 GLU B CB  1 
ATOM   7453 C CG  . GLU B 1 398 ? -47.471 35.766 51.425  1.00 41.55 ? 398 GLU B CG  1 
ATOM   7454 C CD  . GLU B 1 398 ? -47.415 37.255 51.104  1.00 51.99 ? 398 GLU B CD  1 
ATOM   7455 O OE1 . GLU B 1 398 ? -46.311 37.836 51.162  1.00 54.25 ? 398 GLU B OE1 1 
ATOM   7456 O OE2 . GLU B 1 398 ? -48.467 37.846 50.780  1.00 55.06 ? 398 GLU B OE2 1 
ATOM   7457 N N   . VAL B 1 399 ? -48.107 32.627 51.195  1.00 20.02 ? 399 VAL B N   1 
ATOM   7458 C CA  . VAL B 1 399 ? -48.933 31.899 50.231  1.00 24.54 ? 399 VAL B CA  1 
ATOM   7459 C C   . VAL B 1 399 ? -49.548 32.904 49.266  1.00 26.46 ? 399 VAL B C   1 
ATOM   7460 O O   . VAL B 1 399 ? -49.950 34.002 49.674  1.00 28.14 ? 399 VAL B O   1 
ATOM   7461 C CB  . VAL B 1 399 ? -50.016 31.073 50.951  1.00 25.47 ? 399 VAL B CB  1 
ATOM   7462 C CG1 . VAL B 1 399 ? -50.993 30.437 49.960  1.00 22.42 ? 399 VAL B CG1 1 
ATOM   7463 C CG2 . VAL B 1 399 ? -49.370 30.016 51.835  1.00 27.90 ? 399 VAL B CG2 1 
ATOM   7464 N N   . ILE B 1 400 ? -49.647 32.523 48.010  1.00 26.05 ? 400 ILE B N   1 
ATOM   7465 C CA  . ILE B 1 400 ? -50.270 33.371 47.003  1.00 26.32 ? 400 ILE B CA  1 
ATOM   7466 C C   . ILE B 1 400 ? -51.320 32.484 46.298  1.00 25.86 ? 400 ILE B C   1 
ATOM   7467 O O   . ILE B 1 400 ? -51.019 31.376 45.964  1.00 25.58 ? 400 ILE B O   1 
ATOM   7468 C CB  . ILE B 1 400 ? -49.232 33.984 46.075  1.00 28.20 ? 400 ILE B CB  1 
ATOM   7469 C CG1 . ILE B 1 400 ? -49.877 34.741 44.971  1.00 36.14 ? 400 ILE B CG1 1 
ATOM   7470 C CG2 . ILE B 1 400 ? -48.482 32.923 45.379  1.00 39.84 ? 400 ILE B CG2 1 
ATOM   7471 C CD1 . ILE B 1 400 ? -48.856 35.458 44.122  1.00 45.98 ? 400 ILE B CD1 1 
ATOM   7472 N N   . GLU B 1 401 ? -52.522 32.996 46.115  1.00 21.70 ? 401 GLU B N   1 
ATOM   7473 C CA  . GLU B 1 401 ? -53.608 32.202 45.564  1.00 21.97 ? 401 GLU B CA  1 
ATOM   7474 C C   . GLU B 1 401 ? -53.831 32.419 44.075  1.00 23.38 ? 401 GLU B C   1 
ATOM   7475 O O   . GLU B 1 401 ? -54.518 31.606 43.448  1.00 22.35 ? 401 GLU B O   1 
ATOM   7476 C CB  . GLU B 1 401 ? -54.913 32.488 46.323  1.00 26.25 ? 401 GLU B CB  1 
ATOM   7477 C CG  . GLU B 1 401 ? -54.861 32.101 47.797  1.00 38.65 ? 401 GLU B CG  1 
ATOM   7478 C CD  . GLU B 1 401 ? -54.616 30.615 48.004  1.00 48.71 ? 401 GLU B CD  1 
ATOM   7479 O OE1 . GLU B 1 401 ? -54.970 29.819 47.107  1.00 55.56 ? 401 GLU B OE1 1 
ATOM   7480 O OE2 . GLU B 1 401 ? -54.080 30.240 49.069  1.00 54.68 ? 401 GLU B OE2 1 
ATOM   7481 N N   . SER B 1 402 ? -53.262 33.470 43.489  1.00 24.20 ? 402 SER B N   1 
ATOM   7482 C CA  . SER B 1 402 ? -53.563 33.766 42.097  1.00 24.10 ? 402 SER B CA  1 
ATOM   7483 C C   . SER B 1 402 ? -52.549 34.758 41.543  1.00 24.00 ? 402 SER B C   1 
ATOM   7484 O O   . SER B 1 402 ? -52.086 35.659 42.256  1.00 22.19 ? 402 SER B O   1 
ATOM   7485 C CB  . SER B 1 402 ? -54.979 34.327 41.962  1.00 28.48 ? 402 SER B CB  1 
ATOM   7486 O OG  . SER B 1 402 ? -55.257 34.670 40.625  1.00 32.84 ? 402 SER B OG  1 
ATOM   7487 N N   . VAL B 1 403 ? -52.220 34.592 40.261  1.00 20.00 ? 403 VAL B N   1 
ATOM   7488 C CA  . VAL B 1 403 ? -51.362 35.540 39.561  1.00 18.37 ? 403 VAL B CA  1 
ATOM   7489 C C   . VAL B 1 403 ? -52.112 36.092 38.355  1.00 23.10 ? 403 VAL B C   1 
ATOM   7490 O O   . VAL B 1 403 ? -53.011 35.444 37.809  1.00 22.11 ? 403 VAL B O   1 
ATOM   7491 C CB  . VAL B 1 403 ? -50.012 34.935 39.110  1.00 19.75 ? 403 VAL B CB  1 
ATOM   7492 C CG1 . VAL B 1 403 ? -49.198 34.453 40.314  1.00 20.11 ? 403 VAL B CG1 1 
ATOM   7493 C CG2 . VAL B 1 403 ? -50.222 33.815 38.055  1.00 16.82 ? 403 VAL B CG2 1 
ATOM   7494 N N   . LYS B 1 404 ? -51.746 37.311 37.957  1.00 19.87 ? 404 LYS B N   1 
ATOM   7495 C CA  . LYS B 1 404 ? -52.154 37.873 36.681  1.00 20.98 ? 404 LYS B CA  1 
ATOM   7496 C C   . LYS B 1 404 ? -51.151 37.420 35.626  1.00 18.77 ? 404 LYS B C   1 
ATOM   7497 O O   . LYS B 1 404 ? -49.961 37.711 35.745  1.00 18.98 ? 404 LYS B O   1 
ATOM   7498 C CB  . LYS B 1 404 ? -52.195 39.401 36.730  1.00 26.18 ? 404 LYS B CB  1 
ATOM   7499 C CG  . LYS B 1 404 ? -53.273 39.999 37.608  1.00 40.91 ? 404 LYS B CG  1 
ATOM   7500 C CD  . LYS B 1 404 ? -53.840 41.244 36.936  1.00 50.66 ? 404 LYS B CD  1 
ATOM   7501 C CE  . LYS B 1 404 ? -54.829 41.961 37.838  1.00 53.56 ? 404 LYS B CE  1 
ATOM   7502 N NZ  . LYS B 1 404 ? -54.919 41.308 39.172  1.00 55.54 ? 404 LYS B NZ  1 
ATOM   7503 N N   . ALA B 1 405 ? -51.630 36.708 34.607  1.00 17.55 ? 405 ALA B N   1 
ATOM   7504 C CA  . ALA B 1 405 ? -50.740 36.158 33.595  1.00 14.65 ? 405 ALA B CA  1 
ATOM   7505 C C   . ALA B 1 405 ? -49.933 37.256 32.918  1.00 17.09 ? 405 ALA B C   1 
ATOM   7506 O O   . ALA B 1 405 ? -50.449 38.334 32.615  1.00 17.65 ? 405 ALA B O   1 
ATOM   7507 C CB  . ALA B 1 405 ? -51.541 35.391 32.541  1.00 15.54 ? 405 ALA B CB  1 
ATOM   7508 N N   . GLY B 1 406 ? -48.662 36.971 32.658  1.00 17.72 ? 406 GLY B N   1 
ATOM   7509 C CA  . GLY B 1 406 ? -47.841 37.921 31.932  1.00 17.98 ? 406 GLY B CA  1 
ATOM   7510 C C   . GLY B 1 406 ? -46.456 37.376 31.690  1.00 17.25 ? 406 GLY B C   1 
ATOM   7511 O O   . GLY B 1 406 ? -46.224 36.171 31.794  1.00 13.25 ? 406 GLY B O   1 
ATOM   7512 N N   . THR B 1 407 ? -45.537 38.285 31.359  1.00 14.77 ? 407 THR B N   1 
ATOM   7513 C CA  . THR B 1 407 ? -44.142 37.964 31.102  1.00 15.53 ? 407 THR B CA  1 
ATOM   7514 C C   . THR B 1 407 ? -43.284 39.032 31.781  1.00 20.25 ? 407 THR B C   1 
ATOM   7515 O O   . THR B 1 407 ? -43.801 40.012 32.325  1.00 20.09 ? 407 THR B O   1 
ATOM   7516 C CB  . THR B 1 407 ? -43.832 37.922 29.602  1.00 11.35 ? 407 THR B CB  1 
ATOM   7517 O OG1 . THR B 1 407 ? -43.798 39.266 29.094  1.00 15.36 ? 407 THR B OG1 1 
ATOM   7518 C CG2 . THR B 1 407 ? -44.878 37.118 28.837  1.00 13.09 ? 407 THR B CG2 1 
ATOM   7519 N N   . TRP B 1 408 ? -41.955 38.874 31.721  1.00 14.73 ? 408 TRP B N   1 
ATOM   7520 C CA  . TRP B 1 408 ? -41.119 39.927 32.278  1.00 11.67 ? 408 TRP B CA  1 
ATOM   7521 C C   . TRP B 1 408 ? -41.043 41.159 31.381  1.00 17.63 ? 408 TRP B C   1 
ATOM   7522 O O   . TRP B 1 408 ? -40.340 42.119 31.725  1.00 22.61 ? 408 TRP B O   1 
ATOM   7523 C CB  . TRP B 1 408 ? -39.688 39.463 32.579  1.00 16.36 ? 408 TRP B CB  1 
ATOM   7524 C CG  . TRP B 1 408 ? -38.909 38.771 31.492  1.00 17.70 ? 408 TRP B CG  1 
ATOM   7525 C CD1 . TRP B 1 408 ? -39.190 38.710 30.149  1.00 17.94 ? 408 TRP B CD1 1 
ATOM   7526 C CD2 . TRP B 1 408 ? -37.639 38.121 31.669  1.00 11.80 ? 408 TRP B CD2 1 
ATOM   7527 N NE1 . TRP B 1 408 ? -38.189 38.003 29.491  1.00 16.37 ? 408 TRP B NE1 1 
ATOM   7528 C CE2 . TRP B 1 408 ? -37.226 37.647 30.401  1.00 14.26 ? 408 TRP B CE2 1 
ATOM   7529 C CE3 . TRP B 1 408 ? -36.829 37.876 32.778  1.00 13.98 ? 408 TRP B CE3 1 
ATOM   7530 C CZ2 . TRP B 1 408 ? -36.026 36.960 30.213  1.00 14.41 ? 408 TRP B CZ2 1 
ATOM   7531 C CZ3 . TRP B 1 408 ? -35.624 37.192 32.585  1.00 15.45 ? 408 TRP B CZ3 1 
ATOM   7532 C CH2 . TRP B 1 408 ? -35.244 36.742 31.311  1.00 16.01 ? 408 TRP B CH2 1 
ATOM   7533 N N   . PHE B 1 409 ? -41.749 41.180 30.253  1.00 17.87 ? 409 PHE B N   1 
ATOM   7534 C CA  . PHE B 1 409 ? -41.790 42.378 29.429  1.00 19.62 ? 409 PHE B CA  1 
ATOM   7535 C C   . PHE B 1 409 ? -43.132 43.066 29.694  1.00 24.20 ? 409 PHE B C   1 
ATOM   7536 O O   . PHE B 1 409 ? -44.171 42.666 29.160  1.00 21.88 ? 409 PHE B O   1 
ATOM   7537 C CB  . PHE B 1 409 ? -41.559 42.040 27.961  1.00 29.70 ? 409 PHE B CB  1 
ATOM   7538 C CG  . PHE B 1 409 ? -41.142 43.207 27.128  1.00 39.25 ? 409 PHE B CG  1 
ATOM   7539 C CD1 . PHE B 1 409 ? -41.935 44.350 27.028  1.00 43.67 ? 409 PHE B CD1 1 
ATOM   7540 C CD2 . PHE B 1 409 ? -39.901 43.209 26.531  1.00 40.26 ? 409 PHE B CD2 1 
ATOM   7541 C CE1 . PHE B 1 409 ? -41.505 45.442 26.254  1.00 46.95 ? 409 PHE B CE1 1 
ATOM   7542 C CE2 . PHE B 1 409 ? -39.470 44.275 25.788  1.00 46.98 ? 409 PHE B CE2 1 
ATOM   7543 C CZ  . PHE B 1 409 ? -40.259 45.393 25.641  1.00 47.09 ? 409 PHE B CZ  1 
ATOM   7544 N N   . ASP B 1 410 ? -43.096 44.077 30.571  1.00 26.18 ? 410 ASP B N   1 
ATOM   7545 C CA  . ASP B 1 410 ? -44.229 44.905 30.974  1.00 23.69 ? 410 ASP B CA  1 
ATOM   7546 C C   . ASP B 1 410 ? -45.336 44.123 31.664  1.00 26.00 ? 410 ASP B C   1 
ATOM   7547 O O   . ASP B 1 410 ? -46.444 44.654 31.842  1.00 24.97 ? 410 ASP B O   1 
ATOM   7548 C CB  . ASP B 1 410 ? -44.812 45.686 29.791  1.00 31.36 ? 410 ASP B CB  1 
ATOM   7549 C CG  . ASP B 1 410 ? -43.819 46.642 29.169  1.00 38.94 ? 410 ASP B CG  1 
ATOM   7550 O OD1 . ASP B 1 410 ? -42.902 47.102 29.882  1.00 44.40 ? 410 ASP B OD1 1 
ATOM   7551 O OD2 . ASP B 1 410 ? -43.960 46.940 27.963  1.00 45.89 ? 410 ASP B OD2 1 
ATOM   7552 N N   . GLY B 1 411 ? -45.078 42.886 32.072  1.00 20.27 ? 411 GLY B N   1 
ATOM   7553 C CA  . GLY B 1 411 ? -46.110 42.075 32.682  1.00 18.55 ? 411 GLY B CA  1 
ATOM   7554 C C   . GLY B 1 411 ? -47.215 41.627 31.744  1.00 20.59 ? 411 GLY B C   1 
ATOM   7555 O O   . GLY B 1 411 ? -48.300 41.280 32.216  1.00 22.24 ? 411 GLY B O   1 
ATOM   7556 N N   . ASN B 1 412 ? -46.979 41.619 30.426  1.00 17.63 ? 412 ASN B N   1 
ATOM   7557 C CA  . ASN B 1 412 ? -48.031 41.276 29.476  1.00 20.26 ? 412 ASN B CA  1 
ATOM   7558 C C   . ASN B 1 412 ? -47.413 40.561 28.276  1.00 17.35 ? 412 ASN B C   1 
ATOM   7559 O O   . ASN B 1 412 ? -46.212 40.275 28.244  1.00 17.24 ? 412 ASN B O   1 
ATOM   7560 C CB  . ASN B 1 412 ? -48.846 42.532 29.104  1.00 21.32 ? 412 ASN B CB  1 
ATOM   7561 C CG  . ASN B 1 412 ? -48.061 43.553 28.282  1.00 26.72 ? 412 ASN B CG  1 
ATOM   7562 O OD1 . ASN B 1 412 ? -47.293 43.214 27.378  1.00 22.78 ? 412 ASN B OD1 1 
ATOM   7563 N ND2 . ASN B 1 412 ? -48.227 44.825 28.635  1.00 26.76 ? 412 ASN B ND2 1 
ATOM   7564 N N   . PHE B 1 413 ? -48.254 40.243 27.291  1.00 16.78 ? 413 PHE B N   1 
ATOM   7565 C CA  . PHE B 1 413 ? -47.844 39.381 26.181  1.00 16.25 ? 413 PHE B CA  1 
ATOM   7566 C C   . PHE B 1 413 ? -47.653 40.125 24.865  1.00 20.83 ? 413 PHE B C   1 
ATOM   7567 O O   . PHE B 1 413 ? -47.500 39.481 23.817  1.00 19.49 ? 413 PHE B O   1 
ATOM   7568 C CB  . PHE B 1 413 ? -48.866 38.257 26.000  1.00 15.08 ? 413 PHE B CB  1 
ATOM   7569 C CG  . PHE B 1 413 ? -48.858 37.266 27.129  1.00 18.96 ? 413 PHE B CG  1 
ATOM   7570 C CD1 . PHE B 1 413 ? -47.892 36.279 27.180  1.00 20.29 ? 413 PHE B CD1 1 
ATOM   7571 C CD2 . PHE B 1 413 ? -49.797 37.343 28.149  1.00 17.29 ? 413 PHE B CD2 1 
ATOM   7572 C CE1 . PHE B 1 413 ? -47.853 35.370 28.226  1.00 18.71 ? 413 PHE B CE1 1 
ATOM   7573 C CE2 . PHE B 1 413 ? -49.772 36.432 29.201  1.00 18.66 ? 413 PHE B CE2 1 
ATOM   7574 C CZ  . PHE B 1 413 ? -48.795 35.446 29.237  1.00 14.33 ? 413 PHE B CZ  1 
ATOM   7575 N N   . LEU B 1 414 ? -47.634 41.459 24.888  1.00 20.73 ? 414 LEU B N   1 
ATOM   7576 C CA  . LEU B 1 414 ? -47.687 42.219 23.644  1.00 20.27 ? 414 LEU B CA  1 
ATOM   7577 C C   . LEU B 1 414 ? -46.426 42.084 22.794  1.00 21.44 ? 414 LEU B C   1 
ATOM   7578 O O   . LEU B 1 414 ? -46.473 42.413 21.606  1.00 18.66 ? 414 LEU B O   1 
ATOM   7579 C CB  . LEU B 1 414 ? -47.961 43.699 23.944  1.00 21.21 ? 414 LEU B CB  1 
ATOM   7580 C CG  . LEU B 1 414 ? -49.325 43.988 24.583  1.00 24.41 ? 414 LEU B CG  1 
ATOM   7581 C CD1 . LEU B 1 414 ? -49.485 45.469 24.840  1.00 25.15 ? 414 LEU B CD1 1 
ATOM   7582 C CD2 . LEU B 1 414 ? -50.455 43.470 23.699  1.00 22.65 ? 414 LEU B CD2 1 
ATOM   7583 N N   . LYS B 1 415 ? -45.316 41.588 23.341  1.00 20.12 ? 415 LYS B N   1 
ATOM   7584 C CA  . LYS B 1 415 ? -44.159 41.396 22.473  1.00 16.94 ? 415 LYS B CA  1 
ATOM   7585 C C   . LYS B 1 415 ? -44.293 40.182 21.567  1.00 18.85 ? 415 LYS B C   1 
ATOM   7586 O O   . LYS B 1 415 ? -43.451 39.995 20.686  1.00 15.56 ? 415 LYS B O   1 
ATOM   7587 C CB  . LYS B 1 415 ? -42.864 41.273 23.292  1.00 21.11 ? 415 LYS B CB  1 
ATOM   7588 C CG  . LYS B 1 415 ? -42.448 42.534 24.014  1.00 31.71 ? 415 LYS B CG  1 
ATOM   7589 C CD  . LYS B 1 415 ? -42.492 43.751 23.097  1.00 42.47 ? 415 LYS B CD  1 
ATOM   7590 C CE  . LYS B 1 415 ? -41.510 43.647 21.940  1.00 47.79 ? 415 LYS B CE  1 
ATOM   7591 N NZ  . LYS B 1 415 ? -40.108 43.773 22.394  1.00 50.72 ? 415 LYS B NZ  1 
ATOM   7592 N N   . TRP B 1 416 ? -45.319 39.354 21.755  1.00 16.00 ? 416 TRP B N   1 
ATOM   7593 C CA  . TRP B 1 416 ? -45.476 38.139 20.962  1.00 20.35 ? 416 TRP B CA  1 
ATOM   7594 C C   . TRP B 1 416 ? -46.844 37.994 20.317  1.00 18.77 ? 416 TRP B C   1 
ATOM   7595 O O   . TRP B 1 416 ? -47.048 37.046 19.547  1.00 20.02 ? 416 TRP B O   1 
ATOM   7596 C CB  . TRP B 1 416 ? -45.211 36.900 21.827  1.00 13.96 ? 416 TRP B CB  1 
ATOM   7597 C CG  . TRP B 1 416 ? -43.876 36.980 22.525  1.00 15.76 ? 416 TRP B CG  1 
ATOM   7598 C CD1 . TRP B 1 416 ? -42.680 36.522 22.064  1.00 13.53 ? 416 TRP B CD1 1 
ATOM   7599 C CD2 . TRP B 1 416 ? -43.613 37.595 23.789  1.00 16.57 ? 416 TRP B CD2 1 
ATOM   7600 N NE1 . TRP B 1 416 ? -41.683 36.806 22.969  1.00 17.17 ? 416 TRP B NE1 1 
ATOM   7601 C CE2 . TRP B 1 416 ? -42.228 37.470 24.035  1.00 17.79 ? 416 TRP B CE2 1 
ATOM   7602 C CE3 . TRP B 1 416 ? -44.408 38.258 24.726  1.00 16.20 ? 416 TRP B CE3 1 
ATOM   7603 C CZ2 . TRP B 1 416 ? -41.625 37.962 25.194  1.00 15.70 ? 416 TRP B CZ2 1 
ATOM   7604 C CZ3 . TRP B 1 416 ? -43.814 38.742 25.878  1.00 15.16 ? 416 TRP B CZ3 1 
ATOM   7605 C CH2 . TRP B 1 416 ? -42.434 38.595 26.100  1.00 20.08 ? 416 TRP B CH2 1 
ATOM   7606 N N   . ILE B 1 417 ? -47.795 38.872 20.621  1.00 21.13 ? 417 ILE B N   1 
ATOM   7607 C CA  . ILE B 1 417 ? -49.158 38.722 20.127  1.00 22.73 ? 417 ILE B CA  1 
ATOM   7608 C C   . ILE B 1 417 ? -49.828 40.077 20.261  1.00 25.15 ? 417 ILE B C   1 
ATOM   7609 O O   . ILE B 1 417 ? -49.406 40.915 21.056  1.00 24.39 ? 417 ILE B O   1 
ATOM   7610 C CB  . ILE B 1 417 ? -49.925 37.625 20.912  1.00 21.95 ? 417 ILE B CB  1 
ATOM   7611 C CG1 . ILE B 1 417 ? -51.144 37.141 20.117  1.00 18.91 ? 417 ILE B CG1 1 
ATOM   7612 C CG2 . ILE B 1 417 ? -50.336 38.141 22.295  1.00 20.58 ? 417 ILE B CG2 1 
ATOM   7613 C CD1 . ILE B 1 417 ? -51.638 35.772 20.532  1.00 22.13 ? 417 ILE B CD1 1 
ATOM   7614 N N   . GLY B 1 418 ? -50.868 40.304 19.460  1.00 29.54 ? 418 GLY B N   1 
ATOM   7615 C CA  . GLY B 1 418 ? -51.695 41.484 19.610  1.00 27.38 ? 418 GLY B CA  1 
ATOM   7616 C C   . GLY B 1 418 ? -51.526 42.561 18.558  1.00 34.98 ? 418 GLY B C   1 
ATOM   7617 O O   . GLY B 1 418 ? -52.208 43.587 18.649  1.00 38.48 ? 418 GLY B O   1 
ATOM   7618 N N   . ASN B 1 419 ? -50.644 42.387 17.574  1.00 36.70 ? 419 ASN B N   1 
ATOM   7619 C CA  . ASN B 1 419 ? -50.671 43.229 16.389  1.00 36.92 ? 419 ASN B CA  1 
ATOM   7620 C C   . ASN B 1 419 ? -50.752 42.334 15.158  1.00 36.19 ? 419 ASN B C   1 
ATOM   7621 O O   . ASN B 1 419 ? -50.581 41.113 15.241  1.00 34.94 ? 419 ASN B O   1 
ATOM   7622 C CB  . ASN B 1 419 ? -49.482 44.219 16.341  1.00 33.53 ? 419 ASN B CB  1 
ATOM   7623 C CG  . ASN B 1 419 ? -48.136 43.578 15.964  1.00 35.37 ? 419 ASN B CG  1 
ATOM   7624 O OD1 . ASN B 1 419 ? -48.048 42.467 15.442  1.00 35.09 ? 419 ASN B OD1 1 
ATOM   7625 N ND2 . ASN B 1 419 ? -47.073 44.316 16.232  1.00 37.17 ? 419 ASN B ND2 1 
ATOM   7626 N N   . LYS B 1 420 ? -51.008 42.964 14.002  1.00 38.10 ? 420 LYS B N   1 
ATOM   7627 C CA  . LYS B 1 420 ? -51.458 42.202 12.843  1.00 39.05 ? 420 LYS B CA  1 
ATOM   7628 C C   . LYS B 1 420 ? -50.373 41.250 12.343  1.00 33.34 ? 420 LYS B C   1 
ATOM   7629 O O   . LYS B 1 420 ? -50.663 40.117 11.944  1.00 34.58 ? 420 LYS B O   1 
ATOM   7630 C CB  . LYS B 1 420 ? -51.936 43.156 11.740  1.00 48.17 ? 420 LYS B CB  1 
ATOM   7631 C CG  . LYS B 1 420 ? -52.887 44.283 12.220  1.00 61.20 ? 420 LYS B CG  1 
ATOM   7632 C CD  . LYS B 1 420 ? -53.756 43.843 13.417  1.00 67.82 ? 420 LYS B CD  1 
ATOM   7633 C CE  . LYS B 1 420 ? -53.997 44.989 14.403  1.00 71.14 ? 420 LYS B CE  1 
ATOM   7634 N NZ  . LYS B 1 420 ? -54.864 44.624 15.561  1.00 70.10 ? 420 LYS B NZ  1 
ATOM   7635 N N   . GLU B 1 421 ? -49.115 41.672 12.404  1.00 32.99 ? 421 GLU B N   1 
ATOM   7636 C CA  . GLU B 1 421 ? -48.008 40.809 11.992  1.00 28.00 ? 421 GLU B CA  1 
ATOM   7637 C C   . GLU B 1 421 ? -47.827 39.635 12.950  1.00 26.17 ? 421 GLU B C   1 
ATOM   7638 O O   . GLU B 1 421 ? -47.737 38.476 12.522  1.00 27.35 ? 421 GLU B O   1 
ATOM   7639 C CB  . GLU B 1 421 ? -46.721 41.635 11.901  1.00 38.05 ? 421 GLU B CB  1 
ATOM   7640 C CG  . GLU B 1 421 ? -46.679 42.623 10.742  1.00 46.72 ? 421 GLU B CG  1 
ATOM   7641 C CD  . GLU B 1 421 ? -46.438 41.933 9.411   1.00 61.12 ? 421 GLU B CD  1 
ATOM   7642 O OE1 . GLU B 1 421 ? -47.412 41.388 8.845   1.00 66.29 ? 421 GLU B OE1 1 
ATOM   7643 O OE2 . GLU B 1 421 ? -45.278 41.919 8.937   1.00 65.91 ? 421 GLU B OE2 1 
ATOM   7644 N N   . LYS B 1 422 ? -47.746 39.917 14.254  1.00 25.07 ? 422 LYS B N   1 
ATOM   7645 C CA  . LYS B 1 422 ? -47.602 38.832 15.224  1.00 21.71 ? 422 LYS B CA  1 
ATOM   7646 C C   . LYS B 1 422 ? -48.817 37.919 15.193  1.00 25.40 ? 422 LYS B C   1 
ATOM   7647 O O   . LYS B 1 422 ? -48.686 36.693 15.319  1.00 22.29 ? 422 LYS B O   1 
ATOM   7648 C CB  . LYS B 1 422 ? -47.375 39.395 16.633  1.00 20.69 ? 422 LYS B CB  1 
ATOM   7649 C CG  . LYS B 1 422 ? -46.028 40.118 16.784  1.00 19.32 ? 422 LYS B CG  1 
ATOM   7650 C CD  . LYS B 1 422 ? -45.821 40.713 18.173  1.00 21.84 ? 422 LYS B CD  1 
ATOM   7651 C CE  . LYS B 1 422 ? -44.637 41.686 18.183  1.00 22.43 ? 422 LYS B CE  1 
ATOM   7652 N NZ  . LYS B 1 422 ? -43.328 40.991 17.982  1.00 20.50 ? 422 LYS B NZ  1 
ATOM   7653 N N   . ASN B 1 423 ? -50.007 38.492 14.984  1.00 24.77 ? 423 ASN B N   1 
ATOM   7654 C CA  . ASN B 1 423 ? -51.207 37.672 14.885  1.00 24.39 ? 423 ASN B CA  1 
ATOM   7655 C C   . ASN B 1 423 ? -51.186 36.775 13.652  1.00 25.71 ? 423 ASN B C   1 
ATOM   7656 O O   . ASN B 1 423 ? -51.710 35.656 13.702  1.00 26.17 ? 423 ASN B O   1 
ATOM   7657 C CB  . ASN B 1 423 ? -52.460 38.547 14.883  1.00 27.05 ? 423 ASN B CB  1 
ATOM   7658 C CG  . ASN B 1 423 ? -52.758 39.132 16.251  1.00 27.45 ? 423 ASN B CG  1 
ATOM   7659 O OD1 . ASN B 1 423 ? -52.190 38.702 17.259  1.00 24.33 ? 423 ASN B OD1 1 
ATOM   7660 N ND2 . ASN B 1 423 ? -53.703 40.068 16.304  1.00 27.61 ? 423 ASN B ND2 1 
ATOM   7661 N N   . GLU B 1 424 ? -50.583 37.232 12.549  1.00 26.70 ? 424 GLU B N   1 
ATOM   7662 C CA  . GLU B 1 424 ? -50.481 36.385 11.367  1.00 28.45 ? 424 GLU B CA  1 
ATOM   7663 C C   . GLU B 1 424 ? -49.694 35.112 11.663  1.00 27.52 ? 424 GLU B C   1 
ATOM   7664 O O   . GLU B 1 424 ? -50.063 34.026 11.188  1.00 25.82 ? 424 GLU B O   1 
ATOM   7665 C CB  . GLU B 1 424 ? -49.838 37.147 10.208  1.00 38.10 ? 424 GLU B CB  1 
ATOM   7666 C CG  . GLU B 1 424 ? -49.635 36.305 8.952   1.00 51.20 ? 424 GLU B CG  1 
ATOM   7667 C CD  . GLU B 1 424 ? -50.940 35.889 8.284   1.00 65.20 ? 424 GLU B CD  1 
ATOM   7668 O OE1 . GLU B 1 424 ? -50.882 35.126 7.296   1.00 67.70 ? 424 GLU B OE1 1 
ATOM   7669 O OE2 . GLU B 1 424 ? -52.020 36.341 8.722   1.00 69.41 ? 424 GLU B OE2 1 
ATOM   7670 N N   . TYR B 1 425 ? -48.605 35.222 12.441  1.00 22.03 ? 425 TYR B N   1 
ATOM   7671 C CA  . TYR B 1 425 ? -47.850 34.036 12.809  1.00 20.88 ? 425 TYR B CA  1 
ATOM   7672 C C   . TYR B 1 425 ? -48.692 33.065 13.625  1.00 20.46 ? 425 TYR B C   1 
ATOM   7673 O O   . TYR B 1 425 ? -48.648 31.847 13.395  1.00 26.58 ? 425 TYR B O   1 
ATOM   7674 C CB  . TYR B 1 425 ? -46.587 34.404 13.595  1.00 21.35 ? 425 TYR B CB  1 
ATOM   7675 C CG  . TYR B 1 425 ? -45.326 34.562 12.764  1.00 19.73 ? 425 TYR B CG  1 
ATOM   7676 C CD1 . TYR B 1 425 ? -45.381 34.809 11.399  1.00 22.86 ? 425 TYR B CD1 1 
ATOM   7677 C CD2 . TYR B 1 425 ? -44.074 34.408 13.356  1.00 18.62 ? 425 TYR B CD2 1 
ATOM   7678 C CE1 . TYR B 1 425 ? -44.216 34.943 10.647  1.00 24.55 ? 425 TYR B CE1 1 
ATOM   7679 C CE2 . TYR B 1 425 ? -42.919 34.532 12.619  1.00 19.18 ? 425 TYR B CE2 1 
ATOM   7680 C CZ  . TYR B 1 425 ? -42.998 34.797 11.274  1.00 25.66 ? 425 TYR B CZ  1 
ATOM   7681 O OH  . TYR B 1 425 ? -41.839 34.910 10.579  1.00 23.09 ? 425 TYR B OH  1 
ATOM   7682 N N   . TRP B 1 426 ? -49.443 33.572 14.610  1.00 21.49 ? 426 TRP B N   1 
ATOM   7683 C CA  . TRP B 1 426 ? -50.298 32.681 15.384  1.00 21.63 ? 426 TRP B CA  1 
ATOM   7684 C C   . TRP B 1 426 ? -51.342 32.022 14.488  1.00 22.03 ? 426 TRP B C   1 
ATOM   7685 O O   . TRP B 1 426 ? -51.649 30.838 14.658  1.00 24.04 ? 426 TRP B O   1 
ATOM   7686 C CB  . TRP B 1 426 ? -50.959 33.433 16.545  1.00 23.50 ? 426 TRP B CB  1 
ATOM   7687 C CG  . TRP B 1 426 ? -49.991 33.774 17.635  1.00 18.40 ? 426 TRP B CG  1 
ATOM   7688 C CD1 . TRP B 1 426 ? -49.387 34.982 17.845  1.00 20.01 ? 426 TRP B CD1 1 
ATOM   7689 C CD2 . TRP B 1 426 ? -49.490 32.891 18.653  1.00 21.50 ? 426 TRP B CD2 1 
ATOM   7690 N NE1 . TRP B 1 426 ? -48.545 34.908 18.936  1.00 18.39 ? 426 TRP B NE1 1 
ATOM   7691 C CE2 . TRP B 1 426 ? -48.591 33.637 19.448  1.00 21.26 ? 426 TRP B CE2 1 
ATOM   7692 C CE3 . TRP B 1 426 ? -49.713 31.545 18.969  1.00 26.43 ? 426 TRP B CE3 1 
ATOM   7693 C CZ2 . TRP B 1 426 ? -47.916 33.081 20.542  1.00 19.73 ? 426 TRP B CZ2 1 
ATOM   7694 C CZ3 . TRP B 1 426 ? -49.048 30.997 20.062  1.00 23.91 ? 426 TRP B CZ3 1 
ATOM   7695 C CH2 . TRP B 1 426 ? -48.148 31.765 20.826  1.00 17.89 ? 426 TRP B CH2 1 
ATOM   7696 N N   . LYS B 1 427 ? -51.881 32.764 13.516  1.00 22.91 ? 427 LYS B N   1 
ATOM   7697 C CA  . LYS B 1 427 ? -52.820 32.172 12.561  1.00 24.49 ? 427 LYS B CA  1 
ATOM   7698 C C   . LYS B 1 427 ? -52.169 31.048 11.766  1.00 26.32 ? 427 LYS B C   1 
ATOM   7699 O O   . LYS B 1 427 ? -52.776 29.989 11.557  1.00 28.30 ? 427 LYS B O   1 
ATOM   7700 C CB  . LYS B 1 427 ? -53.361 33.228 11.598  1.00 26.06 ? 427 LYS B CB  1 
ATOM   7701 C CG  . LYS B 1 427 ? -54.067 34.398 12.233  1.00 42.98 ? 427 LYS B CG  1 
ATOM   7702 C CD  . LYS B 1 427 ? -54.398 35.430 11.165  1.00 55.44 ? 427 LYS B CD  1 
ATOM   7703 C CE  . LYS B 1 427 ? -55.300 36.528 11.693  1.00 60.27 ? 427 LYS B CE  1 
ATOM   7704 N NZ  . LYS B 1 427 ? -54.582 37.833 11.701  1.00 65.42 ? 427 LYS B NZ  1 
ATOM   7705 N N   . ILE B 1 428 ? -50.946 31.278 11.276  1.00 24.87 ? 428 ILE B N   1 
ATOM   7706 C CA  . ILE B 1 428 ? -50.218 30.239 10.551  1.00 24.13 ? 428 ILE B CA  1 
ATOM   7707 C C   . ILE B 1 428 ? -50.060 29.002 11.428  1.00 24.78 ? 428 ILE B C   1 
ATOM   7708 O O   . ILE B 1 428 ? -50.288 27.867 10.986  1.00 27.42 ? 428 ILE B O   1 
ATOM   7709 C CB  . ILE B 1 428 ? -48.850 30.775 10.093  1.00 29.29 ? 428 ILE B CB  1 
ATOM   7710 C CG1 . ILE B 1 428 ? -49.022 31.900 9.066   1.00 33.86 ? 428 ILE B CG1 1 
ATOM   7711 C CG2 . ILE B 1 428 ? -47.975 29.638 9.553   1.00 29.43 ? 428 ILE B CG2 1 
ATOM   7712 C CD1 . ILE B 1 428 ? -47.762 32.723 8.855   1.00 34.58 ? 428 ILE B CD1 1 
ATOM   7713 N N   . LEU B 1 429 ? -49.678 29.215 12.690  1.00 21.71 ? 429 LEU B N   1 
ATOM   7714 C CA  . LEU B 1 429 ? -49.482 28.106 13.618  1.00 23.83 ? 429 LEU B CA  1 
ATOM   7715 C C   . LEU B 1 429 ? -50.791 27.379 13.890  1.00 26.24 ? 429 LEU B C   1 
ATOM   7716 O O   . LEU B 1 429 ? -50.838 26.142 13.899  1.00 32.26 ? 429 LEU B O   1 
ATOM   7717 C CB  . LEU B 1 429 ? -48.880 28.628 14.925  1.00 22.46 ? 429 LEU B CB  1 
ATOM   7718 C CG  . LEU B 1 429 ? -48.548 27.564 15.983  1.00 25.78 ? 429 LEU B CG  1 
ATOM   7719 C CD1 . LEU B 1 429 ? -47.331 26.752 15.543  1.00 26.31 ? 429 LEU B CD1 1 
ATOM   7720 C CD2 . LEU B 1 429 ? -48.315 28.184 17.365  1.00 23.44 ? 429 LEU B CD2 1 
ATOM   7721 N N   . ILE B 1 430 ? -51.865 28.134 14.127  1.00 24.53 ? 430 ILE B N   1 
ATOM   7722 C CA  . ILE B 1 430 ? -53.161 27.521 14.413  1.00 26.95 ? 430 ILE B CA  1 
ATOM   7723 C C   . ILE B 1 430 ? -53.586 26.624 13.256  1.00 31.87 ? 430 ILE B C   1 
ATOM   7724 O O   . ILE B 1 430 ? -53.983 25.468 13.451  1.00 33.47 ? 430 ILE B O   1 
ATOM   7725 C CB  . ILE B 1 430 ? -54.217 28.607 14.701  1.00 29.15 ? 430 ILE B CB  1 
ATOM   7726 C CG1 . ILE B 1 430 ? -53.924 29.294 16.042  1.00 25.47 ? 430 ILE B CG1 1 
ATOM   7727 C CG2 . ILE B 1 430 ? -55.623 28.019 14.674  1.00 28.85 ? 430 ILE B CG2 1 
ATOM   7728 C CD1 . ILE B 1 430 ? -54.646 30.618 16.204  1.00 31.21 ? 430 ILE B CD1 1 
ATOM   7729 N N   . GLU B 1 431 ? -53.498 27.135 12.029  1.00 28.43 ? 431 GLU B N   1 
ATOM   7730 C CA  . GLU B 1 431 ? -53.932 26.311 10.909  1.00 32.85 ? 431 GLU B CA  1 
ATOM   7731 C C   . GLU B 1 431 ? -52.981 25.139 10.664  1.00 36.08 ? 431 GLU B C   1 
ATOM   7732 O O   . GLU B 1 431 ? -53.440 24.039 10.337  1.00 33.34 ? 431 GLU B O   1 
ATOM   7733 C CB  . GLU B 1 431 ? -54.106 27.181 9.665   1.00 37.29 ? 431 GLU B CB  1 
ATOM   7734 C CG  . GLU B 1 431 ? -55.510 27.781 9.616   1.00 48.31 ? 431 GLU B CG  1 
ATOM   7735 C CD  . GLU B 1 431 ? -56.567 26.714 9.378   1.00 59.07 ? 431 GLU B CD  1 
ATOM   7736 O OE1 . GLU B 1 431 ? -56.472 25.998 8.355   1.00 64.32 ? 431 GLU B OE1 1 
ATOM   7737 O OE2 . GLU B 1 431 ? -57.466 26.562 10.235  1.00 63.61 ? 431 GLU B OE2 1 
ATOM   7738 N N   . ALA B 1 432 ? -51.671 25.330 10.880  1.00 31.79 ? 432 ALA B N   1 
ATOM   7739 C CA  . ALA B 1 432 ? -50.733 24.220 10.725  1.00 28.03 ? 432 ALA B CA  1 
ATOM   7740 C C   . ALA B 1 432 ? -50.936 23.163 11.806  1.00 31.35 ? 432 ALA B C   1 
ATOM   7741 O O   . ALA B 1 432 ? -50.764 21.964 11.550  1.00 29.59 ? 432 ALA B O   1 
ATOM   7742 C CB  . ALA B 1 432 ? -49.297 24.731 10.748  1.00 34.77 ? 432 ALA B CB  1 
ATOM   7743 N N   . LYS B 1 433 ? -51.294 23.592 13.023  1.00 29.58 ? 433 LYS B N   1 
ATOM   7744 C CA  . LYS B 1 433 ? -51.557 22.649 14.108  1.00 29.85 ? 433 LYS B CA  1 
ATOM   7745 C C   . LYS B 1 433 ? -52.719 21.718 13.766  1.00 34.79 ? 433 LYS B C   1 
ATOM   7746 O O   . LYS B 1 433 ? -52.709 20.535 14.128  1.00 35.01 ? 433 LYS B O   1 
ATOM   7747 C CB  . LYS B 1 433 ? -51.837 23.416 15.405  1.00 31.41 ? 433 LYS B CB  1 
ATOM   7748 C CG  . LYS B 1 433 ? -52.217 22.537 16.583  1.00 30.68 ? 433 LYS B CG  1 
ATOM   7749 C CD  . LYS B 1 433 ? -51.062 21.634 17.005  1.00 29.54 ? 433 LYS B CD  1 
ATOM   7750 C CE  . LYS B 1 433 ? -51.486 20.681 18.119  1.00 30.10 ? 433 LYS B CE  1 
ATOM   7751 N NZ  . LYS B 1 433 ? -50.425 19.695 18.453  1.00 28.99 ? 433 LYS B NZ  1 
ATOM   7752 N N   . LYS B 1 434 ? -53.722 22.226 13.051  1.00 31.52 ? 434 LYS B N   1 
ATOM   7753 C CA  . LYS B 1 434 ? -54.822 21.368 12.627  1.00 31.62 ? 434 LYS B CA  1 
ATOM   7754 C C   . LYS B 1 434 ? -54.355 20.242 11.707  1.00 36.23 ? 434 LYS B C   1 
ATOM   7755 O O   . LYS B 1 434 ? -55.045 19.224 11.588  1.00 38.27 ? 434 LYS B O   1 
ATOM   7756 C CB  . LYS B 1 434 ? -55.896 22.223 11.949  1.00 37.07 ? 434 LYS B CB  1 
ATOM   7757 C CG  . LYS B 1 434 ? -56.643 23.113 12.941  1.00 43.46 ? 434 LYS B CG  1 
ATOM   7758 C CD  . LYS B 1 434 ? -57.505 24.154 12.247  1.00 47.36 ? 434 LYS B CD  1 
ATOM   7759 C CE  . LYS B 1 434 ? -58.718 23.527 11.595  1.00 54.63 ? 434 LYS B CE  1 
ATOM   7760 N NZ  . LYS B 1 434 ? -59.690 23.012 12.598  1.00 59.74 ? 434 LYS B NZ  1 
ATOM   7761 N N   . LYS B 1 435 ? -53.180 20.378 11.087  1.00 34.04 ? 435 LYS B N   1 
ATOM   7762 C CA  . LYS B 1 435 ? -52.693 19.380 10.143  1.00 34.39 ? 435 LYS B CA  1 
ATOM   7763 C C   . LYS B 1 435 ? -51.312 18.839 10.520  1.00 34.79 ? 435 LYS B C   1 
ATOM   7764 O O   . LYS B 1 435 ? -50.627 18.270 9.663   1.00 36.63 ? 435 LYS B O   1 
ATOM   7765 C CB  . LYS B 1 435 ? -52.661 19.964 8.721   1.00 36.84 ? 435 LYS B CB  1 
ATOM   7766 C CG  . LYS B 1 435 ? -53.992 20.561 8.204   1.00 44.67 ? 435 LYS B CG  1 
ATOM   7767 C CD  . LYS B 1 435 ? -53.787 21.335 6.884   1.00 53.81 ? 435 LYS B CD  1 
ATOM   7768 C CE  . LYS B 1 435 ? -53.294 22.778 7.118   1.00 58.78 ? 435 LYS B CE  1 
ATOM   7769 N NZ  . LYS B 1 435 ? -52.409 23.369 6.049   1.00 62.46 ? 435 LYS B NZ  1 
ATOM   7770 N N   . ALA B 1 436 ? -50.889 18.986 11.778  1.00 30.16 ? 436 ALA B N   1 
ATOM   7771 C CA  . ALA B 1 436 ? -49.529 18.628 12.169  1.00 31.19 ? 436 ALA B CA  1 
ATOM   7772 C C   . ALA B 1 436 ? -49.377 17.117 12.320  1.00 34.03 ? 436 ALA B C   1 
ATOM   7773 O O   . ALA B 1 436 ? -50.284 16.432 12.795  1.00 31.80 ? 436 ALA B O   1 
ATOM   7774 C CB  . ALA B 1 436 ? -49.145 19.325 13.480  1.00 25.68 ? 436 ALA B CB  1 
ATOM   7775 N N   . LYS B 1 437 ? -48.207 16.604 11.927  1.00 32.22 ? 437 LYS B N   1 
ATOM   7776 C CA  . LYS B 1 437 ? -47.925 15.177 11.959  1.00 35.20 ? 437 LYS B CA  1 
ATOM   7777 C C   . LYS B 1 437 ? -46.660 14.810 12.723  1.00 38.87 ? 437 LYS B C   1 
ATOM   7778 O O   . LYS B 1 437 ? -46.356 13.618 12.835  1.00 41.71 ? 437 LYS B O   1 
ATOM   7779 C CB  . LYS B 1 437 ? -47.825 14.630 10.525  1.00 38.57 ? 437 LYS B CB  1 
ATOM   7780 C CG  . LYS B 1 437 ? -49.119 14.762 9.750   1.00 49.68 ? 437 LYS B CG  1 
ATOM   7781 C CD  . LYS B 1 437 ? -48.984 14.259 8.325   1.00 63.50 ? 437 LYS B CD  1 
ATOM   7782 C CE  . LYS B 1 437 ? -50.304 14.388 7.589   1.00 70.27 ? 437 LYS B CE  1 
ATOM   7783 N NZ  . LYS B 1 437 ? -50.695 15.819 7.474   1.00 71.51 ? 437 LYS B NZ  1 
ATOM   7784 N N   . ASN B 1 438 ? -45.921 15.780 13.254  1.00 31.21 ? 438 ASN B N   1 
ATOM   7785 C CA  . ASN B 1 438 ? -44.645 15.495 13.902  1.00 31.27 ? 438 ASN B CA  1 
ATOM   7786 C C   . ASN B 1 438 ? -44.265 16.668 14.789  1.00 33.02 ? 438 ASN B C   1 
ATOM   7787 O O   . ASN B 1 438 ? -44.878 17.735 14.744  1.00 30.74 ? 438 ASN B O   1 
ATOM   7788 C CB  . ASN B 1 438 ? -43.568 15.192 12.856  1.00 31.46 ? 438 ASN B CB  1 
ATOM   7789 C CG  . ASN B 1 438 ? -43.288 16.369 11.937  1.00 29.59 ? 438 ASN B CG  1 
ATOM   7790 O OD1 . ASN B 1 438 ? -42.986 17.470 12.386  1.00 29.43 ? 438 ASN B OD1 1 
ATOM   7791 N ND2 . ASN B 1 438 ? -43.513 16.161 10.638  1.00 29.12 ? 438 ASN B ND2 1 
ATOM   7792 N N   . ASP B 1 439 ? -43.237 16.457 15.594  1.00 30.78 ? 439 ASP B N   1 
ATOM   7793 C CA  . ASP B 1 439 ? -42.902 17.466 16.587  1.00 28.03 ? 439 ASP B CA  1 
ATOM   7794 C C   . ASP B 1 439 ? -42.267 18.702 16.010  1.00 26.16 ? 439 ASP B C   1 
ATOM   7795 O O   . ASP B 1 439 ? -41.816 19.534 16.813  1.00 22.84 ? 439 ASP B O   1 
ATOM   7796 C CB  . ASP B 1 439 ? -41.988 16.868 17.650  1.00 24.64 ? 439 ASP B CB  1 
ATOM   7797 C CG  . ASP B 1 439 ? -42.720 15.901 18.547  1.00 29.00 ? 439 ASP B CG  1 
ATOM   7798 O OD1 . ASP B 1 439 ? -43.966 15.969 18.595  1.00 30.59 ? 439 ASP B OD1 1 
ATOM   7799 O OD2 . ASP B 1 439 ? -42.047 15.092 19.215  1.00 38.80 ? 439 ASP B OD2 1 
ATOM   7800 N N   . TYR B 1 440 ? -42.181 18.923 14.697  1.00 25.92 ? 440 TYR B N   1 
ATOM   7801 C CA  . TYR B 1 440 ? -41.727 20.232 14.245  1.00 23.16 ? 440 TYR B CA  1 
ATOM   7802 C C   . TYR B 1 440 ? -42.734 21.320 14.573  1.00 21.12 ? 440 TYR B C   1 
ATOM   7803 O O   . TYR B 1 440 ? -42.376 22.505 14.567  1.00 21.75 ? 440 TYR B O   1 
ATOM   7804 C CB  . TYR B 1 440 ? -41.422 20.199 12.748  1.00 23.80 ? 440 TYR B CB  1 
ATOM   7805 C CG  . TYR B 1 440 ? -39.968 19.895 12.481  1.00 24.89 ? 440 TYR B CG  1 
ATOM   7806 C CD1 . TYR B 1 440 ? -39.004 20.870 12.666  1.00 28.50 ? 440 TYR B CD1 1 
ATOM   7807 C CD2 . TYR B 1 440 ? -39.557 18.629 12.086  1.00 27.33 ? 440 TYR B CD2 1 
ATOM   7808 C CE1 . TYR B 1 440 ? -37.674 20.615 12.438  1.00 32.85 ? 440 TYR B CE1 1 
ATOM   7809 C CE2 . TYR B 1 440 ? -38.223 18.358 11.843  1.00 30.94 ? 440 TYR B CE2 1 
ATOM   7810 C CZ  . TYR B 1 440 ? -37.283 19.359 12.030  1.00 38.26 ? 440 TYR B CZ  1 
ATOM   7811 O OH  . TYR B 1 440 ? -35.948 19.118 11.804  1.00 42.10 ? 440 TYR B OH  1 
ATOM   7812 N N   . ILE B 1 441 ? -43.985 20.949 14.858  1.00 20.90 ? 441 ILE B N   1 
ATOM   7813 C CA  . ILE B 1 441 ? -44.947 21.939 15.319  1.00 21.59 ? 441 ILE B CA  1 
ATOM   7814 C C   . ILE B 1 441 ? -44.529 22.493 16.678  1.00 18.05 ? 441 ILE B C   1 
ATOM   7815 O O   . ILE B 1 441 ? -44.807 23.656 16.988  1.00 19.82 ? 441 ILE B O   1 
ATOM   7816 C CB  . ILE B 1 441 ? -46.368 21.349 15.353  1.00 23.77 ? 441 ILE B CB  1 
ATOM   7817 C CG1 . ILE B 1 441 ? -47.403 22.469 15.365  1.00 23.75 ? 441 ILE B CG1 1 
ATOM   7818 C CG2 . ILE B 1 441 ? -46.555 20.435 16.563  1.00 26.40 ? 441 ILE B CG2 1 
ATOM   7819 C CD1 . ILE B 1 441 ? -47.362 23.337 14.110  1.00 29.84 ? 441 ILE B CD1 1 
ATOM   7820 N N   . LEU B 1 442 ? -43.845 21.685 17.501  1.00 16.97 ? 442 LEU B N   1 
ATOM   7821 C CA  . LEU B 1 442 ? -43.338 22.198 18.774  1.00 15.91 ? 442 LEU B CA  1 
ATOM   7822 C C   . LEU B 1 442 ? -42.247 23.240 18.555  1.00 19.27 ? 442 LEU B C   1 
ATOM   7823 O O   . LEU B 1 442 ? -42.184 24.234 19.286  1.00 17.97 ? 442 LEU B O   1 
ATOM   7824 C CB  . LEU B 1 442 ? -42.810 21.052 19.645  1.00 16.63 ? 442 LEU B CB  1 
ATOM   7825 C CG  . LEU B 1 442 ? -43.763 19.915 20.021  1.00 19.39 ? 442 LEU B CG  1 
ATOM   7826 C CD1 . LEU B 1 442 ? -43.025 18.841 20.857  1.00 21.09 ? 442 LEU B CD1 1 
ATOM   7827 C CD2 . LEU B 1 442 ? -44.992 20.435 20.757  1.00 20.54 ? 442 LEU B CD2 1 
ATOM   7828 N N   . VAL B 1 443 ? -41.380 23.024 17.553  1.00 14.75 ? 443 VAL B N   1 
ATOM   7829 C CA  . VAL B 1 443 ? -40.313 23.973 17.230  1.00 15.75 ? 443 VAL B CA  1 
ATOM   7830 C C   . VAL B 1 443 ? -40.905 25.329 16.876  1.00 17.60 ? 443 VAL B C   1 
ATOM   7831 O O   . VAL B 1 443 ? -40.392 26.380 17.288  1.00 17.19 ? 443 VAL B O   1 
ATOM   7832 C CB  . VAL B 1 443 ? -39.446 23.437 16.068  1.00 17.22 ? 443 VAL B CB  1 
ATOM   7833 C CG1 . VAL B 1 443 ? -38.309 24.420 15.758  1.00 18.65 ? 443 VAL B CG1 1 
ATOM   7834 C CG2 . VAL B 1 443 ? -38.885 22.070 16.402  1.00 16.89 ? 443 VAL B CG2 1 
ATOM   7835 N N   . ALA B 1 444 ? -42.006 25.322 16.120  1.00 19.28 ? 444 ALA B N   1 
ATOM   7836 C CA  . ALA B 1 444 ? -42.650 26.548 15.660  1.00 17.69 ? 444 ALA B CA  1 
ATOM   7837 C C   . ALA B 1 444 ? -43.388 27.280 16.769  1.00 18.18 ? 444 ALA B C   1 
ATOM   7838 O O   . ALA B 1 444 ? -43.732 28.456 16.596  1.00 16.35 ? 444 ALA B O   1 
ATOM   7839 C CB  . ALA B 1 444 ? -43.617 26.218 14.515  1.00 20.39 ? 444 ALA B CB  1 
ATOM   7840 N N   . GLU B 1 445 ? -43.650 26.619 17.897  1.00 17.12 ? 445 GLU B N   1 
ATOM   7841 C CA  . GLU B 1 445 ? -44.274 27.274 19.041  1.00 16.09 ? 445 GLU B CA  1 
ATOM   7842 C C   . GLU B 1 445 ? -43.263 28.036 19.890  1.00 16.79 ? 445 GLU B C   1 
ATOM   7843 O O   . GLU B 1 445 ? -43.666 28.685 20.859  1.00 15.16 ? 445 GLU B O   1 
ATOM   7844 C CB  . GLU B 1 445 ? -45.029 26.228 19.875  1.00 17.98 ? 445 GLU B CB  1 
ATOM   7845 C CG  . GLU B 1 445 ? -46.226 25.646 19.106  1.00 17.01 ? 445 GLU B CG  1 
ATOM   7846 C CD  . GLU B 1 445 ? -46.709 24.315 19.636  1.00 26.03 ? 445 GLU B CD  1 
ATOM   7847 O OE1 . GLU B 1 445 ? -46.111 23.820 20.611  1.00 23.61 ? 445 GLU B OE1 1 
ATOM   7848 O OE2 . GLU B 1 445 ? -47.677 23.754 19.054  1.00 26.09 ? 445 GLU B OE2 1 
ATOM   7849 N N   . GLY B 1 446 ? -41.982 27.999 19.524  1.00 16.30 ? 446 GLY B N   1 
ATOM   7850 C CA  . GLY B 1 446 ? -40.979 28.736 20.281  1.00 12.06 ? 446 GLY B CA  1 
ATOM   7851 C C   . GLY B 1 446 ? -41.238 30.232 20.232  1.00 17.30 ? 446 GLY B C   1 
ATOM   7852 O O   . GLY B 1 446 ? -41.717 30.767 19.228  1.00 16.32 ? 446 GLY B O   1 
ATOM   7853 N N   . SER B 1 447 ? -40.944 30.908 21.353  1.00 14.48 ? 447 SER B N   1 
ATOM   7854 C CA  . SER B 1 447 ? -41.316 32.317 21.500  1.00 12.12 ? 447 SER B CA  1 
ATOM   7855 C C   . SER B 1 447 ? -40.550 33.211 20.533  1.00 14.52 ? 447 SER B C   1 
ATOM   7856 O O   . SER B 1 447 ? -41.047 34.278 20.152  1.00 16.63 ? 447 SER B O   1 
ATOM   7857 C CB  . SER B 1 447 ? -41.076 32.787 22.938  1.00 14.44 ? 447 SER B CB  1 
ATOM   7858 O OG  . SER B 1 447 ? -39.677 32.866 23.207  1.00 16.18 ? 447 SER B OG  1 
ATOM   7859 N N   . ASP B 1 448 ? -39.346 32.806 20.134  1.00 12.09 ? 448 ASP B N   1 
ATOM   7860 C CA  . ASP B 1 448 ? -38.501 33.714 19.359  1.00 15.08 ? 448 ASP B CA  1 
ATOM   7861 C C   . ASP B 1 448 ? -39.131 34.109 18.034  1.00 14.66 ? 448 ASP B C   1 
ATOM   7862 O O   . ASP B 1 448 ? -38.970 35.255 17.598  1.00 15.77 ? 448 ASP B O   1 
ATOM   7863 C CB  . ASP B 1 448 ? -37.130 33.103 19.099  1.00 12.87 ? 448 ASP B CB  1 
ATOM   7864 C CG  . ASP B 1 448 ? -36.484 32.588 20.360  1.00 12.82 ? 448 ASP B CG  1 
ATOM   7865 O OD1 . ASP B 1 448 ? -36.911 31.535 20.878  1.00 17.62 ? 448 ASP B OD1 1 
ATOM   7866 O OD2 . ASP B 1 448 ? -35.608 33.315 20.885  1.00 16.95 ? 448 ASP B OD2 1 
ATOM   7867 N N   . TRP B 1 449 ? -39.841 33.190 17.373  1.00 13.03 ? 449 TRP B N   1 
ATOM   7868 C CA  . TRP B 1 449 ? -40.391 33.514 16.062  1.00 16.09 ? 449 TRP B CA  1 
ATOM   7869 C C   . TRP B 1 449 ? -41.344 34.687 16.176  1.00 19.47 ? 449 TRP B C   1 
ATOM   7870 O O   . TRP B 1 449 ? -41.338 35.598 15.336  1.00 17.30 ? 449 TRP B O   1 
ATOM   7871 C CB  . TRP B 1 449 ? -41.086 32.292 15.465  1.00 14.12 ? 449 TRP B CB  1 
ATOM   7872 C CG  . TRP B 1 449 ? -40.281 31.019 15.681  1.00 12.03 ? 449 TRP B CG  1 
ATOM   7873 C CD1 . TRP B 1 449 ? -40.676 29.906 16.371  1.00 19.28 ? 449 TRP B CD1 1 
ATOM   7874 C CD2 . TRP B 1 449 ? -38.949 30.763 15.232  1.00 11.98 ? 449 TRP B CD2 1 
ATOM   7875 N NE1 . TRP B 1 449 ? -39.669 28.967 16.375  1.00 15.62 ? 449 TRP B NE1 1 
ATOM   7876 C CE2 . TRP B 1 449 ? -38.595 29.470 15.687  1.00 15.11 ? 449 TRP B CE2 1 
ATOM   7877 C CE3 . TRP B 1 449 ? -38.015 31.500 14.494  1.00 13.97 ? 449 TRP B CE3 1 
ATOM   7878 C CZ2 . TRP B 1 449 ? -37.356 28.902 15.429  1.00 14.66 ? 449 TRP B CZ2 1 
ATOM   7879 C CZ3 . TRP B 1 449 ? -36.777 30.931 14.230  1.00 12.49 ? 449 TRP B CZ3 1 
ATOM   7880 C CH2 . TRP B 1 449 ? -36.454 29.645 14.702  1.00 17.86 ? 449 TRP B CH2 1 
ATOM   7881 N N   . PHE B 1 450 ? -42.120 34.679 17.235  1.00 17.04 ? 450 PHE B N   1 
ATOM   7882 C CA  . PHE B 1 450 ? -43.079 35.726 17.457  1.00 16.30 ? 450 PHE B CA  1 
ATOM   7883 C C   . PHE B 1 450 ? -42.478 37.039 17.905  1.00 18.98 ? 450 PHE B C   1 
ATOM   7884 O O   . PHE B 1 450 ? -42.989 38.066 17.600  1.00 18.98 ? 450 PHE B O   1 
ATOM   7885 C CB  . PHE B 1 450 ? -44.194 35.254 18.395  1.00 16.31 ? 450 PHE B CB  1 
ATOM   7886 C CG  . PHE B 1 450 ? -44.824 33.991 17.971  1.00 14.93 ? 450 PHE B CG  1 
ATOM   7887 C CD1 . PHE B 1 450 ? -44.303 32.801 18.338  1.00 16.54 ? 450 PHE B CD1 1 
ATOM   7888 C CD2 . PHE B 1 450 ? -45.931 33.997 17.182  1.00 19.03 ? 450 PHE B CD2 1 
ATOM   7889 C CE1 . PHE B 1 450 ? -44.864 31.632 17.942  1.00 25.95 ? 450 PHE B CE1 1 
ATOM   7890 C CE2 . PHE B 1 450 ? -46.477 32.840 16.769  1.00 26.77 ? 450 PHE B CE2 1 
ATOM   7891 C CZ  . PHE B 1 450 ? -45.973 31.657 17.162  1.00 19.35 ? 450 PHE B CZ  1 
ATOM   7892 N N   . TRP B 1 451 ? -41.380 36.973 18.660  1.00 19.02 ? 451 TRP B N   1 
ATOM   7893 C CA  . TRP B 1 451 ? -40.655 38.161 19.099  1.00 14.13 ? 451 TRP B CA  1 
ATOM   7894 C C   . TRP B 1 451 ? -40.226 39.028 17.915  1.00 18.38 ? 451 TRP B C   1 
ATOM   7895 O O   . TRP B 1 451 ? -40.427 40.247 17.918  1.00 19.63 ? 451 TRP B O   1 
ATOM   7896 C CB  . TRP B 1 451 ? -39.438 37.727 19.915  1.00 16.72 ? 451 TRP B CB  1 
ATOM   7897 C CG  . TRP B 1 451 ? -38.544 38.843 20.345  1.00 19.01 ? 451 TRP B CG  1 
ATOM   7898 C CD1 . TRP B 1 451 ? -37.426 39.294 19.705  1.00 19.37 ? 451 TRP B CD1 1 
ATOM   7899 C CD2 . TRP B 1 451 ? -38.671 39.630 21.533  1.00 20.44 ? 451 TRP B CD2 1 
ATOM   7900 N NE1 . TRP B 1 451 ? -36.860 40.327 20.413  1.00 24.48 ? 451 TRP B NE1 1 
ATOM   7901 C CE2 . TRP B 1 451 ? -37.604 40.549 21.542  1.00 26.37 ? 451 TRP B CE2 1 
ATOM   7902 C CE3 . TRP B 1 451 ? -39.589 39.647 22.592  1.00 23.39 ? 451 TRP B CE3 1 
ATOM   7903 C CZ2 . TRP B 1 451 ? -37.427 41.478 22.566  1.00 30.11 ? 451 TRP B CZ2 1 
ATOM   7904 C CZ3 . TRP B 1 451 ? -39.414 40.574 23.606  1.00 29.83 ? 451 TRP B CZ3 1 
ATOM   7905 C CH2 . TRP B 1 451 ? -38.341 41.476 23.585  1.00 32.09 ? 451 TRP B CH2 1 
ATOM   7906 N N   . TRP B 1 452 ? -39.593 38.420 16.906  1.00 20.61 ? 452 TRP B N   1 
ATOM   7907 C CA  . TRP B 1 452 ? -39.021 39.192 15.805  1.00 21.32 ? 452 TRP B CA  1 
ATOM   7908 C C   . TRP B 1 452 ? -40.050 39.589 14.757  1.00 22.87 ? 452 TRP B C   1 
ATOM   7909 O O   . TRP B 1 452 ? -39.806 40.541 14.002  1.00 19.81 ? 452 TRP B O   1 
ATOM   7910 C CB  . TRP B 1 452 ? -37.889 38.409 15.128  1.00 19.47 ? 452 TRP B CB  1 
ATOM   7911 C CG  . TRP B 1 452 ? -36.788 38.097 16.078  1.00 16.20 ? 452 TRP B CG  1 
ATOM   7912 C CD1 . TRP B 1 452 ? -36.457 36.871 16.574  1.00 15.46 ? 452 TRP B CD1 1 
ATOM   7913 C CD2 . TRP B 1 452 ? -35.881 39.032 16.674  1.00 15.16 ? 452 TRP B CD2 1 
ATOM   7914 N NE1 . TRP B 1 452 ? -35.405 36.983 17.453  1.00 16.55 ? 452 TRP B NE1 1 
ATOM   7915 C CE2 . TRP B 1 452 ? -35.034 38.301 17.535  1.00 14.03 ? 452 TRP B CE2 1 
ATOM   7916 C CE3 . TRP B 1 452 ? -35.706 40.418 16.572  1.00 17.00 ? 452 TRP B CE3 1 
ATOM   7917 C CZ2 . TRP B 1 452 ? -34.025 38.906 18.283  1.00 18.51 ? 452 TRP B CZ2 1 
ATOM   7918 C CZ3 . TRP B 1 452 ? -34.704 41.014 17.312  1.00 19.19 ? 452 TRP B CZ3 1 
ATOM   7919 C CH2 . TRP B 1 452 ? -33.878 40.261 18.161  1.00 21.05 ? 452 TRP B CH2 1 
ATOM   7920 N N   . GLN B 1 453 ? -41.174 38.878 14.688  1.00 20.72 ? 453 GLN B N   1 
ATOM   7921 C CA  . GLN B 1 453 ? -42.214 39.192 13.718  1.00 22.98 ? 453 GLN B CA  1 
ATOM   7922 C C   . GLN B 1 453 ? -42.870 40.526 14.057  1.00 22.46 ? 453 GLN B C   1 
ATOM   7923 O O   . GLN B 1 453 ? -43.106 40.848 15.224  1.00 26.97 ? 453 GLN B O   1 
ATOM   7924 C CB  . GLN B 1 453 ? -43.250 38.070 13.701  1.00 19.64 ? 453 GLN B CB  1 
ATOM   7925 C CG  . GLN B 1 453 ? -44.530 38.281 12.876  1.00 26.74 ? 453 GLN B CG  1 
ATOM   7926 C CD  . GLN B 1 453 ? -44.310 38.352 11.372  1.00 33.85 ? 453 GLN B CD  1 
ATOM   7927 O OE1 . GLN B 1 453 ? -43.216 38.079 10.863  1.00 35.51 ? 453 GLN B OE1 1 
ATOM   7928 N NE2 . GLN B 1 453 ? -45.386 38.632 10.647  1.00 35.68 ? 453 GLN B NE2 1 
ATOM   7929 N N   . GLY B 1 454 ? -43.147 41.315 13.025  1.00 34.81 ? 454 GLY B N   1 
ATOM   7930 C CA  . GLY B 1 454 ? -43.809 42.595 13.226  1.00 43.67 ? 454 GLY B CA  1 
ATOM   7931 C C   . GLY B 1 454 ? -43.021 43.579 14.055  1.00 47.83 ? 454 GLY B C   1 
ATOM   7932 O O   . GLY B 1 454 ? -43.592 44.268 14.912  1.00 50.70 ? 454 GLY B O   1 
ATOM   7933 N N   . GLU B 1 455 ? -41.715 43.661 13.818  1.00 47.85 ? 455 GLU B N   1 
ATOM   7934 C CA  . GLU B 1 455 ? -40.831 44.551 14.556  1.00 47.88 ? 455 GLU B CA  1 
ATOM   7935 C C   . GLU B 1 455 ? -40.083 45.431 13.570  1.00 56.25 ? 455 GLU B C   1 
ATOM   7936 O O   . GLU B 1 455 ? -39.556 44.944 12.563  1.00 52.81 ? 455 GLU B O   1 
ATOM   7937 C CB  . GLU B 1 455 ? -39.840 43.761 15.425  1.00 41.41 ? 455 GLU B CB  1 
ATOM   7938 C CG  . GLU B 1 455 ? -40.476 43.038 16.601  1.00 39.53 ? 455 GLU B CG  1 
ATOM   7939 C CD  . GLU B 1 455 ? -41.132 43.989 17.593  1.00 45.41 ? 455 GLU B CD  1 
ATOM   7940 O OE1 . GLU B 1 455 ? -40.768 45.185 17.609  1.00 49.15 ? 455 GLU B OE1 1 
ATOM   7941 O OE2 . GLU B 1 455 ? -42.000 43.539 18.371  1.00 42.75 ? 455 GLU B OE2 1 
ATOM   7942 N N   . GLU B 1 456 ? -40.061 46.732 13.857  1.00 62.37 ? 456 GLU B N   1 
ATOM   7943 C CA  . GLU B 1 456 ? -39.273 47.668 13.060  1.00 72.39 ? 456 GLU B CA  1 
ATOM   7944 C C   . GLU B 1 456 ? -37.792 47.304 13.114  1.00 73.70 ? 456 GLU B C   1 
ATOM   7945 O O   . GLU B 1 456 ? -37.139 47.116 12.082  1.00 75.40 ? 456 GLU B O   1 
ATOM   7946 C CB  . GLU B 1 456 ? -39.512 49.083 13.581  1.00 78.11 ? 456 GLU B CB  1 
ATOM   7947 C CG  . GLU B 1 456 ? -40.830 49.704 13.145  1.00 84.63 ? 456 GLU B CG  1 
ATOM   7948 C CD  . GLU B 1 456 ? -41.495 50.494 14.268  1.00 88.93 ? 456 GLU B CD  1 
ATOM   7949 O OE1 . GLU B 1 456 ? -41.725 49.903 15.348  1.00 89.01 ? 456 GLU B OE1 1 
ATOM   7950 O OE2 . GLU B 1 456 ? -41.780 51.699 14.077  1.00 91.30 ? 456 GLU B OE2 1 
ATOM   7951 N N   . LYS B 1 457 ? -37.250 47.193 14.324  1.00 72.39 ? 457 LYS B N   1 
ATOM   7952 C CA  . LYS B 1 457 ? -35.850 46.840 14.538  1.00 72.42 ? 457 LYS B CA  1 
ATOM   7953 C C   . LYS B 1 457 ? -35.733 45.320 14.537  1.00 68.81 ? 457 LYS B C   1 
ATOM   7954 O O   . LYS B 1 457 ? -36.084 44.662 15.519  1.00 68.04 ? 457 LYS B O   1 
ATOM   7955 C CB  . LYS B 1 457 ? -35.350 47.430 15.856  1.00 72.34 ? 457 LYS B CB  1 
ATOM   7956 C CG  . LYS B 1 457 ? -34.639 48.776 15.727  1.00 75.42 ? 457 LYS B CG  1 
ATOM   7957 C CD  . LYS B 1 457 ? -34.331 49.417 17.088  1.00 76.50 ? 457 LYS B CD  1 
ATOM   7958 C CE  . LYS B 1 457 ? -35.520 50.184 17.658  1.00 77.73 ? 457 LYS B CE  1 
ATOM   7959 N NZ  . LYS B 1 457 ? -35.144 50.941 18.889  1.00 79.46 ? 457 LYS B NZ  1 
ATOM   7960 N N   . ALA B 1 458 ? -35.234 44.749 13.438  1.00 60.65 ? 458 ALA B N   1 
ATOM   7961 C CA  . ALA B 1 458 ? -35.136 43.296 13.372  1.00 52.99 ? 458 ALA B CA  1 
ATOM   7962 C C   . ALA B 1 458 ? -34.101 42.847 12.346  1.00 52.53 ? 458 ALA B C   1 
ATOM   7963 O O   . ALA B 1 458 ? -34.452 42.554 11.194  1.00 48.62 ? 458 ALA B O   1 
ATOM   7964 C CB  . ALA B 1 458 ? -36.499 42.679 13.047  1.00 49.03 ? 458 ALA B CB  1 
ATOM   7965 N N   . PRO B 1 459 ? -32.826 42.756 12.725  1.00 50.85 ? 459 PRO B N   1 
ATOM   7966 C CA  . PRO B 1 459 ? -31.813 42.303 11.766  1.00 46.27 ? 459 PRO B CA  1 
ATOM   7967 C C   . PRO B 1 459 ? -31.977 40.823 11.456  1.00 41.13 ? 459 PRO B C   1 
ATOM   7968 O O   . PRO B 1 459 ? -32.240 40.005 12.343  1.00 39.01 ? 459 PRO B O   1 
ATOM   7969 C CB  . PRO B 1 459 ? -30.492 42.582 12.486  1.00 48.67 ? 459 PRO B CB  1 
ATOM   7970 C CG  . PRO B 1 459 ? -30.839 42.447 13.917  1.00 45.73 ? 459 PRO B CG  1 
ATOM   7971 C CD  . PRO B 1 459 ? -32.257 42.960 14.068  1.00 49.89 ? 459 PRO B CD  1 
ATOM   7972 N N   . PHE B 1 460 ? -31.819 40.491 10.175  1.00 39.09 ? 460 PHE B N   1 
ATOM   7973 C CA  . PHE B 1 460 ? -31.972 39.129 9.672   1.00 37.67 ? 460 PHE B CA  1 
ATOM   7974 C C   . PHE B 1 460 ? -33.365 38.572 9.946   1.00 32.74 ? 460 PHE B C   1 
ATOM   7975 O O   . PHE B 1 460 ? -33.547 37.357 10.049  1.00 36.35 ? 460 PHE B O   1 
ATOM   7976 C CB  . PHE B 1 460 ? -30.902 38.191 10.241  1.00 39.07 ? 460 PHE B CB  1 
ATOM   7977 C CG  . PHE B 1 460 ? -29.488 38.636 9.964   1.00 37.75 ? 460 PHE B CG  1 
ATOM   7978 C CD1 . PHE B 1 460 ? -28.992 38.666 8.670   1.00 45.41 ? 460 PHE B CD1 1 
ATOM   7979 C CD2 . PHE B 1 460 ? -28.651 39.000 11.005  1.00 41.51 ? 460 PHE B CD2 1 
ATOM   7980 C CE1 . PHE B 1 460 ? -27.686 39.068 8.416   1.00 47.68 ? 460 PHE B CE1 1 
ATOM   7981 C CE2 . PHE B 1 460 ? -27.345 39.399 10.763  1.00 42.37 ? 460 PHE B CE2 1 
ATOM   7982 C CZ  . PHE B 1 460 ? -26.862 39.433 9.465   1.00 44.77 ? 460 PHE B CZ  1 
ATOM   7983 N N   . VAL B 1 461 ? -34.362 39.453 10.058  1.00 27.87 ? 461 VAL B N   1 
ATOM   7984 C CA  . VAL B 1 461 ? -35.734 39.004 10.274  1.00 26.44 ? 461 VAL B CA  1 
ATOM   7985 C C   . VAL B 1 461 ? -36.196 38.068 9.158   1.00 29.62 ? 461 VAL B C   1 
ATOM   7986 O O   . VAL B 1 461 ? -36.981 37.142 9.407   1.00 29.62 ? 461 VAL B O   1 
ATOM   7987 C CB  . VAL B 1 461 ? -36.677 40.215 10.420  1.00 31.65 ? 461 VAL B CB  1 
ATOM   7988 C CG1 . VAL B 1 461 ? -36.740 41.015 9.129   1.00 36.17 ? 461 VAL B CG1 1 
ATOM   7989 C CG2 . VAL B 1 461 ? -38.075 39.751 10.832  1.00 31.98 ? 461 VAL B CG2 1 
ATOM   7990 N N   . GLU B 1 462 ? -35.722 38.280 7.920   1.00 24.25 ? 462 GLU B N   1 
ATOM   7991 C CA  . GLU B 1 462 ? -36.048 37.347 6.843   1.00 26.98 ? 462 GLU B CA  1 
ATOM   7992 C C   . GLU B 1 462 ? -35.614 35.931 7.189   1.00 31.52 ? 462 GLU B C   1 
ATOM   7993 O O   . GLU B 1 462 ? -36.251 34.963 6.757   1.00 26.03 ? 462 GLU B O   1 
ATOM   7994 C CB  . GLU B 1 462 ? -35.381 37.770 5.533   1.00 32.85 ? 462 GLU B CB  1 
ATOM   7995 C CG  . GLU B 1 462 ? -35.901 39.050 4.936   1.00 44.18 ? 462 GLU B CG  1 
ATOM   7996 C CD  . GLU B 1 462 ? -35.241 40.276 5.530   1.00 56.10 ? 462 GLU B CD  1 
ATOM   7997 O OE1 . GLU B 1 462 ? -34.388 40.124 6.438   1.00 57.54 ? 462 GLU B OE1 1 
ATOM   7998 O OE2 . GLU B 1 462 ? -35.571 41.395 5.080   1.00 57.14 ? 462 GLU B OE2 1 
ATOM   7999 N N   . VAL B 1 463 ? -34.520 35.789 7.945   1.00 22.29 ? 463 VAL B N   1 
ATOM   8000 C CA  . VAL B 1 463 ? -34.021 34.459 8.267   1.00 21.83 ? 463 VAL B CA  1 
ATOM   8001 C C   . VAL B 1 463 ? -34.882 33.807 9.344   1.00 19.04 ? 463 VAL B C   1 
ATOM   8002 O O   . VAL B 1 463 ? -35.221 32.620 9.245   1.00 22.69 ? 463 VAL B O   1 
ATOM   8003 C CB  . VAL B 1 463 ? -32.542 34.521 8.686   1.00 26.63 ? 463 VAL B CB  1 
ATOM   8004 C CG1 . VAL B 1 463 ? -32.069 33.138 9.082   1.00 30.08 ? 463 VAL B CG1 1 
ATOM   8005 C CG2 . VAL B 1 463 ? -31.686 35.090 7.568   1.00 25.45 ? 463 VAL B CG2 1 
ATOM   8006 N N   . PHE B 1 464 ? -35.231 34.552 10.399  1.00 22.98 ? 464 PHE B N   1 
ATOM   8007 C CA  . PHE B 1 464 ? -36.152 34.019 11.407  1.00 19.08 ? 464 PHE B CA  1 
ATOM   8008 C C   . PHE B 1 464 ? -37.476 33.618 10.774  1.00 21.38 ? 464 PHE B C   1 
ATOM   8009 O O   . PHE B 1 464 ? -38.072 32.600 11.147  1.00 18.05 ? 464 PHE B O   1 
ATOM   8010 C CB  . PHE B 1 464 ? -36.397 35.048 12.515  1.00 14.85 ? 464 PHE B CB  1 
ATOM   8011 C CG  . PHE B 1 464 ? -35.222 35.236 13.434  1.00 18.00 ? 464 PHE B CG  1 
ATOM   8012 C CD1 . PHE B 1 464 ? -35.014 34.382 14.503  1.00 16.98 ? 464 PHE B CD1 1 
ATOM   8013 C CD2 . PHE B 1 464 ? -34.305 36.252 13.209  1.00 19.37 ? 464 PHE B CD2 1 
ATOM   8014 C CE1 . PHE B 1 464 ? -33.925 34.550 15.342  1.00 15.61 ? 464 PHE B CE1 1 
ATOM   8015 C CE2 . PHE B 1 464 ? -33.205 36.414 14.041  1.00 19.26 ? 464 PHE B CE2 1 
ATOM   8016 C CZ  . PHE B 1 464 ? -33.025 35.562 15.115  1.00 17.76 ? 464 PHE B CZ  1 
ATOM   8017 N N   . ASP B 1 465 ? -37.942 34.406 9.806   1.00 18.25 ? 465 ASP B N   1 
ATOM   8018 C CA  . ASP B 1 465 ? -39.206 34.107 9.138   1.00 17.70 ? 465 ASP B CA  1 
ATOM   8019 C C   . ASP B 1 465 ? -39.096 32.854 8.277   1.00 21.32 ? 465 ASP B C   1 
ATOM   8020 O O   . ASP B 1 465 ? -40.014 32.025 8.259   1.00 19.92 ? 465 ASP B O   1 
ATOM   8021 C CB  . ASP B 1 465 ? -39.639 35.306 8.306   1.00 19.19 ? 465 ASP B CB  1 
ATOM   8022 C CG  . ASP B 1 465 ? -40.874 35.020 7.456   1.00 21.63 ? 465 ASP B CG  1 
ATOM   8023 O OD1 . ASP B 1 465 ? -42.017 35.125 7.975   1.00 22.78 ? 465 ASP B OD1 1 
ATOM   8024 O OD2 . ASP B 1 465 ? -40.697 34.673 6.270   1.00 24.34 ? 465 ASP B OD2 1 
ATOM   8025 N N   . LYS B 1 466 ? -37.990 32.710 7.539   1.00 21.07 ? 466 LYS B N   1 
ATOM   8026 C CA  . LYS B 1 466 ? -37.780 31.495 6.755   1.00 19.82 ? 466 LYS B CA  1 
ATOM   8027 C C   . LYS B 1 466 ? -37.752 30.259 7.652   1.00 19.14 ? 466 LYS B C   1 
ATOM   8028 O O   . LYS B 1 466 ? -38.337 29.221 7.312   1.00 22.33 ? 466 LYS B O   1 
ATOM   8029 C CB  . LYS B 1 466 ? -36.479 31.612 5.957   1.00 20.95 ? 466 LYS B CB  1 
ATOM   8030 C CG  . LYS B 1 466 ? -36.212 30.462 5.005   1.00 36.20 ? 466 LYS B CG  1 
ATOM   8031 C CD  . LYS B 1 466 ? -34.939 30.701 4.191   1.00 42.43 ? 466 LYS B CD  1 
ATOM   8032 C CE  . LYS B 1 466 ? -34.832 29.706 3.053   1.00 53.02 ? 466 LYS B CE  1 
ATOM   8033 N NZ  . LYS B 1 466 ? -34.701 28.311 3.560   1.00 57.60 ? 466 LYS B NZ  1 
ATOM   8034 N N   . LEU B 1 467 ? -37.069 30.351 8.800   1.00 17.35 ? 467 LEU B N   1 
ATOM   8035 C CA  . LEU B 1 467 ? -37.001 29.221 9.726   1.00 16.43 ? 467 LEU B CA  1 
ATOM   8036 C C   . LEU B 1 467 ? -38.386 28.868 10.249  1.00 18.30 ? 467 LEU B C   1 
ATOM   8037 O O   . LEU B 1 467 ? -38.797 27.700 10.213  1.00 21.59 ? 467 LEU B O   1 
ATOM   8038 C CB  . LEU B 1 467 ? -36.050 29.546 10.892  1.00 15.31 ? 467 LEU B CB  1 
ATOM   8039 C CG  . LEU B 1 467 ? -34.568 29.530 10.508  1.00 17.70 ? 467 LEU B CG  1 
ATOM   8040 C CD1 . LEU B 1 467 ? -33.691 30.223 11.540  1.00 18.12 ? 467 LEU B CD1 1 
ATOM   8041 C CD2 . LEU B 1 467 ? -34.099 28.095 10.276  1.00 21.74 ? 467 LEU B CD2 1 
ATOM   8042 N N   . PHE B 1 468 ? -39.117 29.871 10.754  1.00 18.06 ? 468 PHE B N   1 
ATOM   8043 C CA  . PHE B 1 468 ? -40.458 29.635 11.287  1.00 21.39 ? 468 PHE B CA  1 
ATOM   8044 C C   . PHE B 1 468 ? -41.340 28.939 10.260  1.00 19.75 ? 468 PHE B C   1 
ATOM   8045 O O   . PHE B 1 468 ? -41.972 27.913 10.543  1.00 20.39 ? 468 PHE B O   1 
ATOM   8046 C CB  . PHE B 1 468 ? -41.100 30.960 11.712  1.00 20.38 ? 468 PHE B CB  1 
ATOM   8047 C CG  . PHE B 1 468 ? -42.548 30.827 12.109  1.00 18.36 ? 468 PHE B CG  1 
ATOM   8048 C CD1 . PHE B 1 468 ? -42.900 30.220 13.306  1.00 17.60 ? 468 PHE B CD1 1 
ATOM   8049 C CD2 . PHE B 1 468 ? -43.559 31.304 11.281  1.00 16.57 ? 468 PHE B CD2 1 
ATOM   8050 C CE1 . PHE B 1 468 ? -44.234 30.094 13.667  1.00 20.67 ? 468 PHE B CE1 1 
ATOM   8051 C CE2 . PHE B 1 468 ? -44.891 31.182 11.642  1.00 25.39 ? 468 PHE B CE2 1 
ATOM   8052 C CZ  . PHE B 1 468 ? -45.229 30.574 12.834  1.00 24.09 ? 468 PHE B CZ  1 
ATOM   8053 N N   . ARG B 1 469 ? -41.387 29.482 9.051   1.00 17.80 ? 469 ARG B N   1 
ATOM   8054 C CA  . ARG B 1 469 ? -42.261 28.902 8.041   1.00 19.44 ? 469 ARG B CA  1 
ATOM   8055 C C   . ARG B 1 469 ? -41.768 27.536 7.580   1.00 26.95 ? 469 ARG B C   1 
ATOM   8056 O O   . ARG B 1 469 ? -42.582 26.675 7.221   1.00 22.45 ? 469 ARG B O   1 
ATOM   8057 C CB  . ARG B 1 469 ? -42.390 29.870 6.867   1.00 24.29 ? 469 ARG B CB  1 
ATOM   8058 C CG  . ARG B 1 469 ? -43.073 31.164 7.279   1.00 22.87 ? 469 ARG B CG  1 
ATOM   8059 C CD  . ARG B 1 469 ? -43.128 32.134 6.129   1.00 22.40 ? 469 ARG B CD  1 
ATOM   8060 N NE  . ARG B 1 469 ? -43.800 33.382 6.475   1.00 26.27 ? 469 ARG B NE  1 
ATOM   8061 C CZ  . ARG B 1 469 ? -45.109 33.589 6.323   1.00 25.80 ? 469 ARG B CZ  1 
ATOM   8062 N NH1 . ARG B 1 469 ? -45.893 32.627 5.848   1.00 24.90 ? 469 ARG B NH1 1 
ATOM   8063 N NH2 . ARG B 1 469 ? -45.636 34.764 6.631   1.00 25.05 ? 469 ARG B NH2 1 
ATOM   8064 N N   . SER B 1 470 ? -40.452 27.307 7.602   1.00 19.78 ? 470 SER B N   1 
ATOM   8065 C CA  . SER B 1 470 ? -39.944 25.984 7.251   1.00 26.90 ? 470 SER B CA  1 
ATOM   8066 C C   . SER B 1 470 ? -40.366 24.944 8.281   1.00 22.81 ? 470 SER B C   1 
ATOM   8067 O O   . SER B 1 470 ? -40.775 23.838 7.913   1.00 24.34 ? 470 SER B O   1 
ATOM   8068 C CB  . SER B 1 470 ? -38.422 26.012 7.121   1.00 31.32 ? 470 SER B CB  1 
ATOM   8069 O OG  . SER B 1 470 ? -38.040 26.859 6.054   1.00 39.42 ? 470 SER B OG  1 
ATOM   8070 N N   . PHE B 1 471 ? -40.266 25.277 9.576   1.00 18.41 ? 471 PHE B N   1 
ATOM   8071 C CA  . PHE B 1 471 ? -40.699 24.336 10.606  1.00 22.07 ? 471 PHE B CA  1 
ATOM   8072 C C   . PHE B 1 471 ? -42.197 24.081 10.513  1.00 25.21 ? 471 PHE B C   1 
ATOM   8073 O O   . PHE B 1 471 ? -42.654 22.945 10.706  1.00 21.54 ? 471 PHE B O   1 
ATOM   8074 C CB  . PHE B 1 471 ? -40.323 24.843 12.007  1.00 20.34 ? 471 PHE B CB  1 
ATOM   8075 C CG  . PHE B 1 471 ? -38.845 25.037 12.200  1.00 18.38 ? 471 PHE B CG  1 
ATOM   8076 C CD1 . PHE B 1 471 ? -37.958 24.032 11.866  1.00 24.93 ? 471 PHE B CD1 1 
ATOM   8077 C CD2 . PHE B 1 471 ? -38.343 26.206 12.759  1.00 21.52 ? 471 PHE B CD2 1 
ATOM   8078 C CE1 . PHE B 1 471 ? -36.597 24.193 12.044  1.00 23.49 ? 471 PHE B CE1 1 
ATOM   8079 C CE2 . PHE B 1 471 ? -36.975 26.367 12.954  1.00 18.72 ? 471 PHE B CE2 1 
ATOM   8080 C CZ  . PHE B 1 471 ? -36.106 25.359 12.589  1.00 20.42 ? 471 PHE B CZ  1 
ATOM   8081 N N   . VAL B 1 472 ? -42.975 25.127 10.216  1.00 19.87 ? 472 VAL B N   1 
ATOM   8082 C CA  . VAL B 1 472 ? -44.420 24.976 10.038  1.00 22.59 ? 472 VAL B CA  1 
ATOM   8083 C C   . VAL B 1 472 ? -44.721 24.051 8.864   1.00 24.57 ? 472 VAL B C   1 
ATOM   8084 O O   . VAL B 1 472 ? -45.625 23.205 8.931   1.00 24.85 ? 472 VAL B O   1 
ATOM   8085 C CB  . VAL B 1 472 ? -45.067 26.363 9.858   1.00 27.71 ? 472 VAL B CB  1 
ATOM   8086 C CG1 . VAL B 1 472 ? -46.467 26.249 9.279   1.00 33.97 ? 472 VAL B CG1 1 
ATOM   8087 C CG2 . VAL B 1 472 ? -45.074 27.123 11.189  1.00 22.21 ? 472 VAL B CG2 1 
ATOM   8088 N N   . ARG B 1 473 ? -43.964 24.182 7.773   1.00 25.16 ? 473 ARG B N   1 
ATOM   8089 C CA  . ARG B 1 473 ? -44.219 23.323 6.627   1.00 26.58 ? 473 ARG B CA  1 
ATOM   8090 C C   . ARG B 1 473 ? -43.832 21.878 6.928   1.00 28.55 ? 473 ARG B C   1 
ATOM   8091 O O   . ARG B 1 473 ? -44.588 20.954 6.603   1.00 27.35 ? 473 ARG B O   1 
ATOM   8092 C CB  . ARG B 1 473 ? -43.480 23.852 5.395   1.00 31.23 ? 473 ARG B CB  1 
ATOM   8093 C CG  . ARG B 1 473 ? -43.205 22.801 4.317   1.00 37.35 ? 473 ARG B CG  1 
ATOM   8094 C CD  . ARG B 1 473 ? -42.667 23.435 3.028   1.00 45.12 ? 473 ARG B CD  1 
ATOM   8095 N NE  . ARG B 1 473 ? -41.292 23.926 3.175   1.00 55.37 ? 473 ARG B NE  1 
ATOM   8096 C CZ  . ARG B 1 473 ? -40.948 25.215 3.210   1.00 60.67 ? 473 ARG B CZ  1 
ATOM   8097 N NH1 . ARG B 1 473 ? -41.879 26.152 3.085   1.00 64.07 ? 473 ARG B NH1 1 
ATOM   8098 N NH2 . ARG B 1 473 ? -39.675 25.573 3.351   1.00 58.70 ? 473 ARG B NH2 1 
ATOM   8099 N N   . ARG B 1 474 ? -42.673 21.659 7.562   1.00 24.40 ? 474 ARG B N   1 
ATOM   8100 C CA  . ARG B 1 474 ? -42.240 20.294 7.886   1.00 30.46 ? 474 ARG B CA  1 
ATOM   8101 C C   . ARG B 1 474 ? -43.159 19.628 8.909   1.00 27.20 ? 474 ARG B C   1 
ATOM   8102 O O   . ARG B 1 474 ? -43.319 18.401 8.893   1.00 32.01 ? 474 ARG B O   1 
ATOM   8103 C CB  . ARG B 1 474 ? -40.780 20.291 8.376   1.00 27.73 ? 474 ARG B CB  1 
ATOM   8104 C CG  . ARG B 1 474 ? -40.311 18.907 8.881   1.00 39.26 ? 474 ARG B CG  1 
ATOM   8105 C CD  . ARG B 1 474 ? -39.956 17.874 7.805   1.00 48.73 ? 474 ARG B CD  1 
ATOM   8106 N NE  . ARG B 1 474 ? -39.207 16.742 8.367   1.00 58.33 ? 474 ARG B NE  1 
ATOM   8107 C CZ  . ARG B 1 474 ? -39.752 15.716 9.026   1.00 64.60 ? 474 ARG B CZ  1 
ATOM   8108 N NH1 . ARG B 1 474 ? -41.068 15.645 9.179   1.00 63.92 ? 474 ARG B NH1 1 
ATOM   8109 N NH2 . ARG B 1 474 ? -38.986 14.737 9.500   1.00 65.52 ? 474 ARG B NH2 1 
ATOM   8110 N N   . ALA B 1 475 ? -43.769 20.416 9.799   1.00 23.58 ? 475 ALA B N   1 
ATOM   8111 C CA  . ALA B 1 475 ? -44.670 19.862 10.809  1.00 23.67 ? 475 ALA B CA  1 
ATOM   8112 C C   . ALA B 1 475 ? -45.866 19.129 10.203  1.00 29.45 ? 475 ALA B C   1 
ATOM   8113 O O   . ALA B 1 475 ? -46.442 18.261 10.867  1.00 30.09 ? 475 ALA B O   1 
ATOM   8114 C CB  . ALA B 1 475 ? -45.157 20.981 11.735  1.00 22.85 ? 475 ALA B CB  1 
ATOM   8115 N N   . GLN B 1 476 ? -46.243 19.451 8.961   1.00 30.54 ? 476 GLN B N   1 
ATOM   8116 C CA  . GLN B 1 476 ? -47.444 18.921 8.324   1.00 30.19 ? 476 GLN B CA  1 
ATOM   8117 C C   . GLN B 1 476 ? -47.154 17.810 7.322   1.00 36.07 ? 476 GLN B C   1 
ATOM   8118 O O   . GLN B 1 476 ? -48.085 17.340 6.658   1.00 38.09 ? 476 GLN B O   1 
ATOM   8119 C CB  . GLN B 1 476 ? -48.206 20.050 7.615   1.00 29.79 ? 476 GLN B CB  1 
ATOM   8120 C CG  . GLN B 1 476 ? -48.143 21.386 8.323   1.00 32.79 ? 476 GLN B CG  1 
ATOM   8121 C CD  . GLN B 1 476 ? -49.009 22.456 7.688   1.00 32.14 ? 476 GLN B CD  1 
ATOM   8122 O OE1 . GLN B 1 476 ? -50.075 22.177 7.144   1.00 33.87 ? 476 GLN B OE1 1 
ATOM   8123 N NE2 . GLN B 1 476 ? -48.523 23.686 7.710   1.00 28.67 ? 476 GLN B NE2 1 
ATOM   8124 N N   . GLU B 1 477 ? -45.898 17.387 7.186   1.00 37.20 ? 477 GLU B N   1 
ATOM   8125 C CA  . GLU B 1 477 ? -45.535 16.432 6.137   1.00 47.83 ? 477 GLU B CA  1 
ATOM   8126 C C   . GLU B 1 477 ? -45.198 15.042 6.678   1.00 50.02 ? 477 GLU B C   1 
ATOM   8127 O O   . GLU B 1 477 ? -44.637 14.907 7.766   1.00 52.20 ? 477 GLU B O   1 
ATOM   8128 C CB  . GLU B 1 477 ? -44.359 16.977 5.327   1.00 49.04 ? 477 GLU B CB  1 
ATOM   8129 C CG  . GLU B 1 477 ? -44.703 18.234 4.544   1.00 53.19 ? 477 GLU B CG  1 
ATOM   8130 C CD  . GLU B 1 477 ? -43.535 18.759 3.736   1.00 57.88 ? 477 GLU B CD  1 
ATOM   8131 O OE1 . GLU B 1 477 ? -42.415 18.235 3.910   1.00 58.27 ? 477 GLU B OE1 1 
ATOM   8132 O OE2 . GLU B 1 477 ? -43.736 19.691 2.927   1.00 58.27 ? 477 GLU B OE2 1 
HETATM 8133 C C1  . GLC C 2 .   ? -0.117  18.742 72.444  1.00 27.77 ? 1   GLC C C1  1 
HETATM 8134 C C2  . GLC C 2 .   ? -0.607  17.323 72.151  1.00 18.12 ? 1   GLC C C2  1 
HETATM 8135 C C3  . GLC C 2 .   ? -1.970  17.123 72.809  1.00 19.61 ? 1   GLC C C3  1 
HETATM 8136 C C4  . GLC C 2 .   ? -2.032  17.529 74.310  1.00 17.89 ? 1   GLC C C4  1 
HETATM 8137 C C5  . GLC C 2 .   ? -1.270  18.868 74.564  1.00 17.18 ? 1   GLC C C5  1 
HETATM 8138 C C6  . GLC C 2 .   ? -0.882  19.134 76.029  1.00 15.25 ? 1   GLC C C6  1 
HETATM 8139 O O1  . GLC C 2 .   ? -0.907  19.615 71.697  1.00 37.16 ? 1   GLC C O1  1 
HETATM 8140 O O2  . GLC C 2 .   ? -0.658  17.089 70.769  1.00 15.00 ? 1   GLC C O2  1 
HETATM 8141 O O3  . GLC C 2 .   ? -2.452  15.819 72.487  1.00 11.85 ? 1   GLC C O3  1 
HETATM 8142 O O4  . GLC C 2 .   ? -3.384  17.701 74.679  1.00 10.02 ? 1   GLC C O4  1 
HETATM 8143 O O5  . GLC C 2 .   ? -0.094  18.991 73.842  1.00 16.62 ? 1   GLC C O5  1 
HETATM 8144 O O6  . GLC C 2 .   ? -0.060  18.164 76.606  1.00 17.34 ? 1   GLC C O6  1 
HETATM 8145 C C1  . GLC C 2 .   ? -3.985  16.583 75.327  1.00 10.15 ? 2   GLC C C1  1 
HETATM 8146 C C2  . GLC C 2 .   ? -5.495  16.635 75.011  1.00 9.57  ? 2   GLC C C2  1 
HETATM 8147 C C3  . GLC C 2 .   ? -6.084  17.900 75.580  1.00 11.18 ? 2   GLC C C3  1 
HETATM 8148 C C4  . GLC C 2 .   ? -5.824  17.988 77.083  1.00 11.36 ? 2   GLC C C4  1 
HETATM 8149 C C5  . GLC C 2 .   ? -4.319  17.829 77.365  1.00 10.01 ? 2   GLC C C5  1 
HETATM 8150 C C6  . GLC C 2 .   ? -3.995  17.794 78.861  1.00 9.03  ? 2   GLC C C6  1 
HETATM 8151 O O2  . GLC C 2 .   ? -5.713  16.546 73.601  1.00 12.28 ? 2   GLC C O2  1 
HETATM 8152 O O3  . GLC C 2 .   ? -7.469  17.911 75.364  1.00 11.22 ? 2   GLC C O3  1 
HETATM 8153 O O4  . GLC C 2 .   ? -6.351  19.202 77.606  1.00 11.00 ? 2   GLC C O4  1 
HETATM 8154 O O5  . GLC C 2 .   ? -3.815  16.660 76.739  1.00 12.02 ? 2   GLC C O5  1 
HETATM 8155 O O6  . GLC C 2 .   ? -2.599  17.628 79.026  1.00 12.43 ? 2   GLC C O6  1 
HETATM 8156 C C1  . AC1 C 2 .   ? -7.273  19.145 78.625  1.00 9.84  ? 3   AC1 C C1  1 
HETATM 8157 O O2  . AC1 C 2 .   ? -9.130  19.046 77.159  1.00 11.20 ? 3   AC1 C O2  1 
HETATM 8158 C C2  . AC1 C 2 .   ? -8.592  19.787 78.277  1.00 10.57 ? 3   AC1 C C2  1 
HETATM 8159 C C4A . AC1 C 2 .   ? -7.186  27.184 78.337  1.00 38.48 ? 3   AC1 C C4A 1 
HETATM 8160 C C3  . AC1 C 2 .   ? -8.342  21.235 77.944  1.00 11.26 ? 3   AC1 C C3  1 
HETATM 8161 O O3  . AC1 C 2 .   ? -9.553  21.896 77.534  1.00 17.07 ? 3   AC1 C O3  1 
HETATM 8162 C C4  . AC1 C 2 .   ? -7.781  21.985 79.130  1.00 11.37 ? 3   AC1 C C4  1 
HETATM 8163 N N4A . AC1 C 2 .   ? -7.412  23.344 78.605  1.00 11.45 ? 3   AC1 C N4A 1 
HETATM 8164 C C5  . AC1 C 2 .   ? -6.495  21.314 79.620  1.00 14.90 ? 3   AC1 C C5  1 
HETATM 8165 O O5  . AC1 C 2 .   ? -6.658  19.859 79.783  1.00 11.36 ? 3   AC1 C O5  1 
HETATM 8166 C C6  . AC1 C 2 .   ? -6.039  21.827 80.958  1.00 18.52 ? 3   AC1 C C6  1 
HETATM 8167 C C1B . AC1 C 2 .   ? -7.633  24.426 79.545  1.00 24.20 ? 3   AC1 C C1B 1 
HETATM 8168 C C2B . AC1 C 2 .   ? -8.853  25.392 78.900  1.00 27.82 ? 3   AC1 C C2B 1 
HETATM 8169 O O2B . AC1 C 2 .   ? -9.960  24.474 78.518  1.00 19.64 ? 3   AC1 C O2B 1 
HETATM 8170 C C3B . AC1 C 2 .   ? -8.388  26.077 77.875  1.00 32.69 ? 3   AC1 C C3B 1 
HETATM 8171 O O3B . AC1 C 2 .   ? -9.429  26.859 77.285  1.00 32.14 ? 3   AC1 C O3B 1 
HETATM 8172 O O4  . AC1 C 2 .   ? -6.574  27.724 77.201  1.00 43.37 ? 3   AC1 C O4  1 
HETATM 8173 C C5B . AC1 C 2 .   ? -6.174  26.595 79.139  1.00 37.36 ? 3   AC1 C C5B 1 
HETATM 8174 C C7B . AC1 C 2 .   ? -6.365  25.073 79.629  1.00 29.09 ? 3   AC1 C C7B 1 
HETATM 8175 C C6B . AC1 C 2 .   ? -4.804  27.305 79.273  1.00 46.03 ? 3   AC1 C C6B 1 
HETATM 8176 O O6B . AC1 C 2 .   ? -3.860  26.681 78.460  1.00 48.64 ? 3   AC1 C O6B 1 
HETATM 8177 C C1  . GLC D 2 .   ? -35.706 36.653 25.691  1.00 24.19 ? 1   GLC D C1  1 
HETATM 8178 C C2  . GLC D 2 .   ? -35.070 35.314 26.028  1.00 17.23 ? 1   GLC D C2  1 
HETATM 8179 C C3  . GLC D 2 .   ? -33.766 35.169 25.239  1.00 17.53 ? 1   GLC D C3  1 
HETATM 8180 C C4  . GLC D 2 .   ? -34.013 35.395 23.734  1.00 15.35 ? 1   GLC D C4  1 
HETATM 8181 C C5  . GLC D 2 .   ? -34.891 36.642 23.439  1.00 16.96 ? 1   GLC D C5  1 
HETATM 8182 C C6  . GLC D 2 .   ? -35.484 36.729 22.024  1.00 16.38 ? 1   GLC D C6  1 
HETATM 8183 O O1  . GLC D 2 .   ? -34.815 37.566 26.249  1.00 42.02 ? 1   GLC D O1  1 
HETATM 8184 O O2  . GLC D 2 .   ? -34.888 35.164 27.418  1.00 13.58 ? 1   GLC D O2  1 
HETATM 8185 O O3  . GLC D 2 .   ? -33.234 33.894 25.458  1.00 14.75 ? 1   GLC D O3  1 
HETATM 8186 O O4  . GLC D 2 .   ? -32.775 35.513 23.078  1.00 11.96 ? 1   GLC D O4  1 
HETATM 8187 O O5  . GLC D 2 .   ? -35.956 36.773 24.306  1.00 19.88 ? 1   GLC D O5  1 
HETATM 8188 O O6  . GLC D 2 .   ? -36.487 35.787 21.664  1.00 16.16 ? 1   GLC D O6  1 
HETATM 8189 C C1  . GLC D 2 .   ? -32.245 34.339 22.462  1.00 12.30 ? 2   GLC D C1  1 
HETATM 8190 C C2  . GLC D 2 .   ? -30.714 34.412 22.538  1.00 9.72  ? 2   GLC D C2  1 
HETATM 8191 C C3  . GLC D 2 .   ? -30.169 35.591 21.735  1.00 12.09 ? 2   GLC D C3  1 
HETATM 8192 C C4  . GLC D 2 .   ? -30.715 35.500 20.315  1.00 12.49 ? 2   GLC D C4  1 
HETATM 8193 C C5  . GLC D 2 .   ? -32.245 35.320 20.320  1.00 12.72 ? 2   GLC D C5  1 
HETATM 8194 C C6  . GLC D 2 .   ? -32.821 35.152 18.912  1.00 11.70 ? 2   GLC D C6  1 
HETATM 8195 O O2  . GLC D 2 .   ? -30.263 34.481 23.883  1.00 10.93 ? 2   GLC D O2  1 
HETATM 8196 O O3  . GLC D 2 .   ? -28.740 35.604 21.712  1.00 9.41  ? 2   GLC D O3  1 
HETATM 8197 O O4  . GLC D 2 .   ? -30.364 36.695 19.638  1.00 11.05 ? 2   GLC D O4  1 
HETATM 8198 O O5  . GLC D 2 .   ? -32.661 34.209 21.113  1.00 14.09 ? 2   GLC D O5  1 
HETATM 8199 O O6  . GLC D 2 .   ? -34.228 34.932 19.029  1.00 11.37 ? 2   GLC D O6  1 
HETATM 8200 C C1  . AC1 D 2 .   ? -29.619 36.470 18.503  1.00 11.10 ? 3   AC1 D C1  1 
HETATM 8201 O O2  . AC1 D 2 .   ? -27.511 36.469 19.632  1.00 12.69 ? 3   AC1 D O2  1 
HETATM 8202 C C2  . AC1 D 2 .   ? -28.259 37.127 18.584  1.00 10.01 ? 3   AC1 D C2  1 
HETATM 8203 C C4A . AC1 D 2 .   ? -29.555 44.485 18.314  1.00 39.18 ? 3   AC1 D C4A 1 
HETATM 8204 C C3  . AC1 D 2 .   ? -28.431 38.595 18.832  1.00 11.50 ? 3   AC1 D C3  1 
HETATM 8205 O O3  . AC1 D 2 .   ? -27.155 39.240 18.941  1.00 13.82 ? 3   AC1 D O3  1 
HETATM 8206 C C4  . AC1 D 2 .   ? -29.186 39.241 17.703  1.00 16.27 ? 3   AC1 D C4  1 
HETATM 8207 N N4A . AC1 D 2 .   ? -29.461 40.647 18.161  1.00 15.75 ? 3   AC1 D N4A 1 
HETATM 8208 C C5  . AC1 D 2 .   ? -30.513 38.515 17.452  1.00 10.22 ? 3   AC1 D C5  1 
HETATM 8209 O O5  . AC1 D 2 .   ? -30.338 37.056 17.343  1.00 12.82 ? 3   AC1 D O5  1 
HETATM 8210 C C6  . AC1 D 2 .   ? -31.202 38.988 16.194  1.00 16.41 ? 3   AC1 D C6  1 
HETATM 8211 C C1B . AC1 D 2 .   ? -29.415 41.679 17.140  1.00 26.69 ? 3   AC1 D C1B 1 
HETATM 8212 C C2B . AC1 D 2 .   ? -28.071 42.654 17.430  1.00 24.07 ? 3   AC1 D C2B 1 
HETATM 8213 O O2B . AC1 D 2 .   ? -26.896 41.771 17.616  1.00 19.09 ? 3   AC1 D O2B 1 
HETATM 8214 C C3B . AC1 D 2 .   ? -28.252 43.408 18.489  1.00 29.86 ? 3   AC1 D C3B 1 
HETATM 8215 O O3B . AC1 D 2 .   ? -27.087 44.210 18.707  1.00 30.76 ? 3   AC1 D O3B 1 
HETATM 8216 O O4  . AC1 D 2 .   ? -29.773 45.154 19.531  1.00 39.67 ? 3   AC1 D O4  1 
HETATM 8217 C C5B . AC1 D 2 .   ? -30.757 43.842 17.900  1.00 39.09 ? 3   AC1 D C5B 1 
HETATM 8218 C C7B . AC1 D 2 .   ? -30.663 42.388 17.216  1.00 27.56 ? 3   AC1 D C7B 1 
HETATM 8219 C C6B . AC1 D 2 .   ? -32.134 44.436 18.288  1.00 47.61 ? 3   AC1 D C6B 1 
HETATM 8220 O O6B . AC1 D 2 .   ? -32.421 45.521 17.463  1.00 53.14 ? 3   AC1 D O6B 1 
HETATM 8221 C C1  . GOL E 3 .   ? 23.477  10.254 76.893  1.00 38.06 ? 501 GOL A C1  1 
HETATM 8222 O O1  . GOL E 3 .   ? 22.742  11.428 76.731  1.00 36.68 ? 501 GOL A O1  1 
HETATM 8223 C C2  . GOL E 3 .   ? 22.540  9.067  76.523  1.00 35.04 ? 501 GOL A C2  1 
HETATM 8224 O O2  . GOL E 3 .   ? 22.043  9.186  75.232  1.00 33.92 ? 501 GOL A O2  1 
HETATM 8225 C C3  . GOL E 3 .   ? 21.397  9.094  77.582  1.00 36.06 ? 501 GOL A C3  1 
HETATM 8226 O O3  . GOL E 3 .   ? 20.760  7.843  77.534  1.00 30.23 ? 501 GOL A O3  1 
HETATM 8227 C C1  . GOL F 3 .   ? -18.610 37.190 30.356  1.00 29.11 ? 501 GOL B C1  1 
HETATM 8228 O O1  . GOL F 3 .   ? -17.433 37.774 30.722  1.00 27.45 ? 501 GOL B O1  1 
HETATM 8229 C C2  . GOL F 3 .   ? -18.329 36.370 29.096  1.00 26.12 ? 501 GOL B C2  1 
HETATM 8230 O O2  . GOL F 3 .   ? -19.411 35.506 28.853  1.00 17.99 ? 501 GOL B O2  1 
HETATM 8231 C C3  . GOL F 3 .   ? -16.954 35.647 29.381  1.00 24.22 ? 501 GOL B C3  1 
HETATM 8232 O O3  . GOL F 3 .   ? -16.340 35.287 28.151  1.00 11.14 ? 501 GOL B O3  1 
HETATM 8233 O O   . HOH G 4 .   ? -15.115 29.594 91.344  1.00 44.76 ? 601 HOH A O   1 
HETATM 8234 O O   . HOH G 4 .   ? -19.125 7.728  52.910  1.00 47.05 ? 602 HOH A O   1 
HETATM 8235 O O   . HOH G 4 .   ? -21.446 11.864 49.414  1.00 43.58 ? 603 HOH A O   1 
HETATM 8236 O O   . HOH G 4 .   ? 12.325  14.607 38.512  1.00 47.97 ? 604 HOH A O   1 
HETATM 8237 O O   . HOH G 4 .   ? -36.332 16.438 67.297  1.00 49.89 ? 605 HOH A O   1 
HETATM 8238 O O   . HOH G 4 .   ? -6.855  34.354 61.433  1.00 40.68 ? 606 HOH A O   1 
HETATM 8239 O O   . HOH G 4 .   ? -31.013 31.683 93.338  1.00 35.76 ? 607 HOH A O   1 
HETATM 8240 O O   . HOH G 4 .   ? -6.384  -4.149 74.925  1.00 34.91 ? 608 HOH A O   1 
HETATM 8241 O O   . HOH G 4 .   ? -8.991  25.688 37.896  1.00 50.66 ? 609 HOH A O   1 
HETATM 8242 O O   . HOH G 4 .   ? 0.070   20.511 41.308  1.00 47.97 ? 610 HOH A O   1 
HETATM 8243 O O   . HOH G 4 .   ? -15.785 8.683  72.183  1.00 32.53 ? 611 HOH A O   1 
HETATM 8244 O O   . HOH G 4 .   ? -18.581 8.570  87.182  1.00 38.30 ? 612 HOH A O   1 
HETATM 8245 O O   . HOH G 4 .   ? -12.240 4.657  87.691  1.00 21.55 ? 613 HOH A O   1 
HETATM 8246 O O   . HOH G 4 .   ? -25.754 7.041  81.821  1.00 33.81 ? 614 HOH A O   1 
HETATM 8247 O O   . HOH G 4 .   ? 17.197  27.152 81.226  1.00 22.98 ? 615 HOH A O   1 
HETATM 8248 O O   . HOH G 4 .   ? 2.516   17.864 75.890  1.00 14.91 ? 616 HOH A O   1 
HETATM 8249 O O   . HOH G 4 .   ? -38.042 16.389 70.238  1.00 42.92 ? 617 HOH A O   1 
HETATM 8250 O O   . HOH G 4 .   ? -3.463  0.770  89.403  1.00 50.01 ? 618 HOH A O   1 
HETATM 8251 O O   . HOH G 4 .   ? 5.062   24.062 64.430  1.00 21.36 ? 619 HOH A O   1 
HETATM 8252 O O   . HOH G 4 .   ? -11.604 25.391 41.120  1.00 43.49 ? 620 HOH A O   1 
HETATM 8253 O O   . HOH G 4 .   ? 25.221  12.215 87.847  1.00 38.92 ? 621 HOH A O   1 
HETATM 8254 O O   . HOH G 4 .   ? -11.633 0.825  86.945  1.00 43.30 ? 622 HOH A O   1 
HETATM 8255 O O   . HOH G 4 .   ? -13.427 14.226 86.807  1.00 16.89 ? 623 HOH A O   1 
HETATM 8256 O O   . HOH G 4 .   ? -27.825 38.110 84.294  1.00 45.76 ? 624 HOH A O   1 
HETATM 8257 O O   . HOH G 4 .   ? -5.616  1.725  90.763  1.00 42.31 ? 625 HOH A O   1 
HETATM 8258 O O   . HOH G 4 .   ? -28.548 20.931 67.265  1.00 38.43 ? 626 HOH A O   1 
HETATM 8259 O O   . HOH G 4 .   ? -22.209 13.849 72.133  1.00 12.77 ? 627 HOH A O   1 
HETATM 8260 O O   . HOH G 4 .   ? 23.086  25.263 78.517  1.00 35.31 ? 628 HOH A O   1 
HETATM 8261 O O   . HOH G 4 .   ? -11.609 15.159 46.832  1.00 32.57 ? 629 HOH A O   1 
HETATM 8262 O O   . HOH G 4 .   ? -33.797 13.246 91.460  1.00 37.04 ? 630 HOH A O   1 
HETATM 8263 O O   . HOH G 4 .   ? -12.590 21.197 71.265  1.00 12.28 ? 631 HOH A O   1 
HETATM 8264 O O   . HOH G 4 .   ? -1.603  23.289 64.131  1.00 33.47 ? 632 HOH A O   1 
HETATM 8265 O O   . HOH G 4 .   ? -28.473 8.832  87.599  1.00 43.36 ? 633 HOH A O   1 
HETATM 8266 O O   . HOH G 4 .   ? -23.072 10.317 63.069  1.00 23.07 ? 634 HOH A O   1 
HETATM 8267 O O   . HOH G 4 .   ? 7.363   23.655 47.906  1.00 22.41 ? 635 HOH A O   1 
HETATM 8268 O O   . HOH G 4 .   ? 11.502  25.997 79.454  1.00 29.35 ? 636 HOH A O   1 
HETATM 8269 O O   . HOH G 4 .   ? 3.473   25.927 55.442  1.00 35.53 ? 637 HOH A O   1 
HETATM 8270 O O   . HOH G 4 .   ? -12.708 5.304  95.211  1.00 43.53 ? 638 HOH A O   1 
HETATM 8271 O O   . HOH G 4 .   ? -19.524 30.127 61.105  1.00 35.19 ? 639 HOH A O   1 
HETATM 8272 O O   . HOH G 4 .   ? -2.672  8.695  41.004  1.00 46.14 ? 640 HOH A O   1 
HETATM 8273 O O   . HOH G 4 .   ? 15.724  -1.206 69.187  1.00 45.79 ? 641 HOH A O   1 
HETATM 8274 O O   . HOH G 4 .   ? -23.217 24.767 72.350  1.00 22.11 ? 642 HOH A O   1 
HETATM 8275 O O   . HOH G 4 .   ? 6.711   16.219 53.465  1.00 17.08 ? 643 HOH A O   1 
HETATM 8276 O O   . HOH G 4 .   ? 9.362   24.797 54.641  1.00 39.44 ? 644 HOH A O   1 
HETATM 8277 O O   . HOH G 4 .   ? 19.848  16.829 56.768  1.00 32.22 ? 645 HOH A O   1 
HETATM 8278 O O   . HOH G 4 .   ? -9.733  21.206 74.767  1.00 20.35 ? 646 HOH A O   1 
HETATM 8279 O O   . HOH G 4 .   ? 2.160   25.739 86.093  1.00 57.13 ? 647 HOH A O   1 
HETATM 8280 O O   . HOH G 4 .   ? 13.258  19.260 49.213  1.00 28.55 ? 648 HOH A O   1 
HETATM 8281 O O   . HOH G 4 .   ? -14.906 7.910  52.089  1.00 47.01 ? 649 HOH A O   1 
HETATM 8282 O O   . HOH G 4 .   ? -23.986 12.982 97.681  1.00 40.38 ? 650 HOH A O   1 
HETATM 8283 O O   . HOH G 4 .   ? -21.939 10.832 60.775  1.00 30.90 ? 651 HOH A O   1 
HETATM 8284 O O   . HOH G 4 .   ? 8.235   13.188 78.159  1.00 21.26 ? 652 HOH A O   1 
HETATM 8285 O O   . HOH G 4 .   ? -8.128  10.534 94.392  1.00 41.67 ? 653 HOH A O   1 
HETATM 8286 O O   . HOH G 4 .   ? 16.736  20.458 70.065  1.00 16.19 ? 654 HOH A O   1 
HETATM 8287 O O   . HOH G 4 .   ? -17.678 14.372 92.794  1.00 23.34 ? 655 HOH A O   1 
HETATM 8288 O O   . HOH G 4 .   ? -38.762 21.957 82.822  1.00 31.31 ? 656 HOH A O   1 
HETATM 8289 O O   . HOH G 4 .   ? 1.511   24.220 65.574  1.00 33.34 ? 657 HOH A O   1 
HETATM 8290 O O   . HOH G 4 .   ? -23.615 8.086  63.815  1.00 33.17 ? 658 HOH A O   1 
HETATM 8291 O O   . HOH G 4 .   ? -6.067  30.594 44.958  1.00 41.96 ? 659 HOH A O   1 
HETATM 8292 O O   . HOH G 4 .   ? -20.326 20.952 71.529  1.00 16.13 ? 660 HOH A O   1 
HETATM 8293 O O   . HOH G 4 .   ? 19.040  9.794  80.602  1.00 24.14 ? 661 HOH A O   1 
HETATM 8294 O O   . HOH G 4 .   ? 22.264  12.211 79.247  1.00 26.45 ? 662 HOH A O   1 
HETATM 8295 O O   . HOH G 4 .   ? -29.890 29.377 77.472  1.00 24.05 ? 663 HOH A O   1 
HETATM 8296 O O   . HOH G 4 .   ? 17.967  2.253  79.525  1.00 24.63 ? 664 HOH A O   1 
HETATM 8297 O O   . HOH G 4 .   ? 13.991  18.639 46.673  1.00 26.02 ? 665 HOH A O   1 
HETATM 8298 O O   . HOH G 4 .   ? 17.128  0.798  52.921  1.00 41.56 ? 666 HOH A O   1 
HETATM 8299 O O   . HOH G 4 .   ? -23.516 22.905 58.090  1.00 48.39 ? 667 HOH A O   1 
HETATM 8300 O O   . HOH G 4 .   ? -6.898  12.456 54.347  1.00 15.76 ? 668 HOH A O   1 
HETATM 8301 O O   . HOH G 4 .   ? 9.002   10.805 69.155  1.00 14.01 ? 669 HOH A O   1 
HETATM 8302 O O   . HOH G 4 .   ? -38.734 15.759 82.478  1.00 14.85 ? 670 HOH A O   1 
HETATM 8303 O O   . HOH G 4 .   ? 9.693   10.156 94.741  1.00 45.21 ? 671 HOH A O   1 
HETATM 8304 O O   . HOH G 4 .   ? 18.347  8.259  78.709  1.00 16.86 ? 672 HOH A O   1 
HETATM 8305 O O   . HOH G 4 .   ? 3.760   28.675 65.503  1.00 43.78 ? 673 HOH A O   1 
HETATM 8306 O O   . HOH G 4 .   ? -22.548 13.126 69.250  1.00 11.68 ? 674 HOH A O   1 
HETATM 8307 O O   . HOH G 4 .   ? -15.516 12.084 46.694  1.00 31.42 ? 675 HOH A O   1 
HETATM 8308 O O   . HOH G 4 .   ? -21.525 31.301 78.471  1.00 31.95 ? 676 HOH A O   1 
HETATM 8309 O O   . HOH G 4 .   ? -9.449  34.616 52.374  1.00 36.55 ? 677 HOH A O   1 
HETATM 8310 O O   . HOH G 4 .   ? -5.694  2.817  51.967  1.00 29.25 ? 678 HOH A O   1 
HETATM 8311 O O   . HOH G 4 .   ? -16.864 0.363  70.217  1.00 18.04 ? 679 HOH A O   1 
HETATM 8312 O O   . HOH G 4 .   ? 11.964  1.107  85.660  1.00 33.72 ? 680 HOH A O   1 
HETATM 8313 O O   . HOH G 4 .   ? 17.371  11.763 70.772  1.00 10.68 ? 681 HOH A O   1 
HETATM 8314 O O   . HOH G 4 .   ? -19.209 3.724  56.950  1.00 37.83 ? 682 HOH A O   1 
HETATM 8315 O O   . HOH G 4 .   ? -2.036  -3.777 75.732  1.00 44.70 ? 683 HOH A O   1 
HETATM 8316 O O   . HOH G 4 .   ? -4.591  15.666 70.789  1.00 12.34 ? 684 HOH A O   1 
HETATM 8317 O O   . HOH G 4 .   ? -7.457  26.832 68.919  1.00 25.91 ? 685 HOH A O   1 
HETATM 8318 O O   . HOH G 4 .   ? -4.899  1.862  56.557  1.00 28.10 ? 686 HOH A O   1 
HETATM 8319 O O   . HOH G 4 .   ? -34.182 23.344 86.135  1.00 23.21 ? 687 HOH A O   1 
HETATM 8320 O O   . HOH G 4 .   ? -7.207  20.612 67.888  1.00 14.56 ? 688 HOH A O   1 
HETATM 8321 O O   . HOH G 4 .   ? 4.033   13.990 40.759  1.00 31.00 ? 689 HOH A O   1 
HETATM 8322 O O   . HOH G 4 .   ? 21.088  17.885 61.395  1.00 43.05 ? 690 HOH A O   1 
HETATM 8323 O O   . HOH G 4 .   ? 4.940   15.063 45.714  1.00 21.03 ? 691 HOH A O   1 
HETATM 8324 O O   . HOH G 4 .   ? 0.402   11.347 78.806  1.00 14.67 ? 692 HOH A O   1 
HETATM 8325 O O   . HOH G 4 .   ? -11.689 12.081 81.958  1.00 12.54 ? 693 HOH A O   1 
HETATM 8326 O O   . HOH G 4 .   ? -11.147 12.981 48.074  1.00 22.43 ? 694 HOH A O   1 
HETATM 8327 O O   . HOH G 4 .   ? -28.708 39.926 96.775  1.00 47.58 ? 695 HOH A O   1 
HETATM 8328 O O   . HOH G 4 .   ? -18.541 6.700  84.303  1.00 47.30 ? 696 HOH A O   1 
HETATM 8329 O O   . HOH G 4 .   ? -5.910  -8.528 68.241  1.00 33.79 ? 697 HOH A O   1 
HETATM 8330 O O   . HOH G 4 .   ? -1.629  -2.160 77.773  1.00 49.56 ? 698 HOH A O   1 
HETATM 8331 O O   . HOH G 4 .   ? -1.286  19.314 93.587  1.00 17.00 ? 699 HOH A O   1 
HETATM 8332 O O   . HOH G 4 .   ? 8.851   19.859 94.163  1.00 28.17 ? 700 HOH A O   1 
HETATM 8333 O O   . HOH G 4 .   ? 22.162  14.903 79.843  1.00 23.24 ? 701 HOH A O   1 
HETATM 8334 O O   . HOH G 4 .   ? 15.350  22.539 72.838  1.00 16.04 ? 702 HOH A O   1 
HETATM 8335 O O   . HOH G 4 .   ? -13.558 31.609 69.766  1.00 39.78 ? 703 HOH A O   1 
HETATM 8336 O O   . HOH G 4 .   ? -18.631 17.031 67.079  1.00 13.47 ? 704 HOH A O   1 
HETATM 8337 O O   . HOH G 4 .   ? -1.148  29.527 59.195  1.00 51.77 ? 705 HOH A O   1 
HETATM 8338 O O   . HOH G 4 .   ? 15.705  2.501  73.074  1.00 35.31 ? 706 HOH A O   1 
HETATM 8339 O O   . HOH G 4 .   ? -8.428  3.312  50.687  1.00 34.79 ? 707 HOH A O   1 
HETATM 8340 O O   . HOH G 4 .   ? 11.109  -0.409 59.942  1.00 28.47 ? 708 HOH A O   1 
HETATM 8341 O O   . HOH G 4 .   ? -13.972 -3.492 53.432  1.00 38.95 ? 709 HOH A O   1 
HETATM 8342 O O   . HOH G 4 .   ? -5.466  6.226  45.329  1.00 53.62 ? 710 HOH A O   1 
HETATM 8343 O O   . HOH G 4 .   ? -8.220  8.144  48.088  1.00 33.24 ? 711 HOH A O   1 
HETATM 8344 O O   . HOH G 4 .   ? -13.298 14.776 61.145  1.00 12.09 ? 712 HOH A O   1 
HETATM 8345 O O   . HOH G 4 .   ? 20.777  12.434 91.293  1.00 48.29 ? 713 HOH A O   1 
HETATM 8346 O O   . HOH G 4 .   ? -19.866 31.517 75.441  1.00 25.94 ? 714 HOH A O   1 
HETATM 8347 O O   . HOH G 4 .   ? 4.845   21.258 92.353  1.00 31.32 ? 715 HOH A O   1 
HETATM 8348 O O   . HOH G 4 .   ? 10.751  1.633  58.090  1.00 45.06 ? 716 HOH A O   1 
HETATM 8349 O O   . HOH G 4 .   ? 18.142  5.040  68.777  1.00 27.68 ? 717 HOH A O   1 
HETATM 8350 O O   . HOH G 4 .   ? -2.979  3.193  80.961  1.00 22.50 ? 718 HOH A O   1 
HETATM 8351 O O   . HOH G 4 .   ? 1.371   15.247 69.848  1.00 10.92 ? 719 HOH A O   1 
HETATM 8352 O O   . HOH G 4 .   ? -26.727 20.379 97.748  1.00 29.78 ? 720 HOH A O   1 
HETATM 8353 O O   . HOH G 4 .   ? -7.578  1.714  56.058  1.00 29.76 ? 721 HOH A O   1 
HETATM 8354 O O   . HOH G 4 .   ? 14.631  0.879  82.260  1.00 27.08 ? 722 HOH A O   1 
HETATM 8355 O O   . HOH G 4 .   ? -15.319 17.232 66.760  1.00 16.09 ? 723 HOH A O   1 
HETATM 8356 O O   . HOH G 4 .   ? -30.317 22.898 68.588  1.00 43.07 ? 724 HOH A O   1 
HETATM 8357 O O   . HOH G 4 .   ? -4.729  4.669  87.553  1.00 21.74 ? 725 HOH A O   1 
HETATM 8358 O O   . HOH G 4 .   ? 2.829   18.373 53.640  1.00 16.66 ? 726 HOH A O   1 
HETATM 8359 O O   . HOH G 4 .   ? 18.725  14.833 65.820  1.00 15.85 ? 727 HOH A O   1 
HETATM 8360 O O   . HOH G 4 .   ? -15.632 2.329  72.476  1.00 14.87 ? 728 HOH A O   1 
HETATM 8361 O O   . HOH G 4 .   ? -28.333 8.338  82.853  1.00 30.68 ? 729 HOH A O   1 
HETATM 8362 O O   . HOH G 4 .   ? -10.481 16.637 90.981  1.00 31.34 ? 730 HOH A O   1 
HETATM 8363 O O   . HOH G 4 .   ? -18.189 33.158 72.980  1.00 48.79 ? 731 HOH A O   1 
HETATM 8364 O O   . HOH G 4 .   ? 19.884  12.535 70.037  1.00 26.80 ? 732 HOH A O   1 
HETATM 8365 O O   . HOH G 4 .   ? -17.786 12.291 69.647  1.00 9.10  ? 733 HOH A O   1 
HETATM 8366 O O   . HOH G 4 .   ? -8.995  0.013  79.971  1.00 36.03 ? 734 HOH A O   1 
HETATM 8367 O O   . HOH G 4 .   ? -13.656 30.500 78.943  1.00 26.75 ? 735 HOH A O   1 
HETATM 8368 O O   . HOH G 4 .   ? 5.551   11.898 94.394  1.00 27.43 ? 736 HOH A O   1 
HETATM 8369 O O   . HOH G 4 .   ? -19.922 13.372 63.314  1.00 15.27 ? 737 HOH A O   1 
HETATM 8370 O O   . HOH G 4 .   ? -11.055 36.878 61.282  1.00 29.99 ? 738 HOH A O   1 
HETATM 8371 O O   . HOH G 4 .   ? -28.656 12.016 93.060  1.00 33.50 ? 739 HOH A O   1 
HETATM 8372 O O   . HOH G 4 .   ? 1.775   19.167 85.875  1.00 21.55 ? 740 HOH A O   1 
HETATM 8373 O O   . HOH G 4 .   ? 7.902   12.234 71.186  1.00 15.75 ? 741 HOH A O   1 
HETATM 8374 O O   . HOH G 4 .   ? -8.532  23.937 75.178  1.00 38.31 ? 742 HOH A O   1 
HETATM 8375 O O   . HOH G 4 .   ? -28.993 31.388 74.526  1.00 30.92 ? 743 HOH A O   1 
HETATM 8376 O O   . HOH G 4 .   ? 13.551  26.269 65.536  1.00 31.17 ? 744 HOH A O   1 
HETATM 8377 O O   . HOH G 4 .   ? -16.143 21.437 45.435  1.00 32.10 ? 745 HOH A O   1 
HETATM 8378 O O   . HOH G 4 .   ? 15.781  25.843 55.160  1.00 25.54 ? 746 HOH A O   1 
HETATM 8379 O O   . HOH G 4 .   ? 6.088   26.790 66.258  1.00 32.51 ? 747 HOH A O   1 
HETATM 8380 O O   . HOH G 4 .   ? 1.798   24.955 78.854  1.00 43.19 ? 748 HOH A O   1 
HETATM 8381 O O   . HOH G 4 .   ? -8.855  -3.141 62.244  1.00 37.71 ? 749 HOH A O   1 
HETATM 8382 O O   . HOH G 4 .   ? -21.395 9.472  87.000  1.00 50.85 ? 750 HOH A O   1 
HETATM 8383 O O   . HOH G 4 .   ? -9.219  27.829 64.932  1.00 13.62 ? 751 HOH A O   1 
HETATM 8384 O O   . HOH G 4 .   ? -1.190  28.441 49.449  1.00 30.98 ? 752 HOH A O   1 
HETATM 8385 O O   . HOH G 4 .   ? 4.364   25.246 88.566  1.00 40.91 ? 753 HOH A O   1 
HETATM 8386 O O   . HOH G 4 .   ? 22.490  21.986 65.852  1.00 38.54 ? 754 HOH A O   1 
HETATM 8387 O O   . HOH G 4 .   ? 1.240   -5.003 60.568  1.00 50.31 ? 755 HOH A O   1 
HETATM 8388 O O   . HOH G 4 .   ? 13.263  29.220 85.653  1.00 38.56 ? 756 HOH A O   1 
HETATM 8389 O O   . HOH G 4 .   ? 11.214  12.132 43.163  1.00 36.23 ? 757 HOH A O   1 
HETATM 8390 O O   . HOH G 4 .   ? -23.702 2.172  71.968  1.00 33.28 ? 758 HOH A O   1 
HETATM 8391 O O   . HOH G 4 .   ? 21.376  30.113 80.538  1.00 46.33 ? 759 HOH A O   1 
HETATM 8392 O O   . HOH G 4 .   ? 1.385   0.227  81.217  1.00 34.34 ? 760 HOH A O   1 
HETATM 8393 O O   . HOH G 4 .   ? -2.291  5.219  43.266  1.00 41.99 ? 761 HOH A O   1 
HETATM 8394 O O   . HOH G 4 .   ? 14.250  -3.087 96.334  1.00 53.44 ? 762 HOH A O   1 
HETATM 8395 O O   . HOH G 4 .   ? -17.013 18.530 65.096  1.00 26.58 ? 763 HOH A O   1 
HETATM 8396 O O   . HOH G 4 .   ? 19.407  28.696 73.925  1.00 25.29 ? 764 HOH A O   1 
HETATM 8397 O O   . HOH G 4 .   ? -34.530 16.612 69.566  1.00 33.58 ? 765 HOH A O   1 
HETATM 8398 O O   . HOH G 4 .   ? 6.190   5.199  97.117  1.00 40.93 ? 766 HOH A O   1 
HETATM 8399 O O   . HOH G 4 .   ? 11.245  11.470 93.203  1.00 21.29 ? 767 HOH A O   1 
HETATM 8400 O O   . HOH G 4 .   ? -7.874  26.216 87.897  1.00 39.50 ? 768 HOH A O   1 
HETATM 8401 O O   . HOH G 4 .   ? -9.682  26.923 67.452  1.00 15.64 ? 769 HOH A O   1 
HETATM 8402 O O   . HOH G 4 .   ? -16.636 -1.944 63.627  1.00 44.25 ? 770 HOH A O   1 
HETATM 8403 O O   . HOH G 4 .   ? 14.992  3.068  80.766  1.00 17.65 ? 771 HOH A O   1 
HETATM 8404 O O   . HOH G 4 .   ? -2.065  -9.640 62.489  1.00 48.57 ? 772 HOH A O   1 
HETATM 8405 O O   . HOH G 4 .   ? 10.253  6.795  45.482  1.00 33.02 ? 773 HOH A O   1 
HETATM 8406 O O   . HOH G 4 .   ? 6.835   14.101 94.085  1.00 21.00 ? 774 HOH A O   1 
HETATM 8407 O O   . HOH G 4 .   ? -24.444 16.705 57.553  1.00 40.56 ? 775 HOH A O   1 
HETATM 8408 O O   . HOH G 4 .   ? -25.510 9.685  59.042  1.00 47.85 ? 776 HOH A O   1 
HETATM 8409 O O   . HOH G 4 .   ? -27.384 12.265 63.899  1.00 34.74 ? 777 HOH A O   1 
HETATM 8410 O O   . HOH G 4 .   ? 17.612  2.722  83.832  1.00 43.15 ? 778 HOH A O   1 
HETATM 8411 O O   . HOH G 4 .   ? 23.726  9.127  58.379  1.00 46.17 ? 779 HOH A O   1 
HETATM 8412 O O   . HOH G 4 .   ? -21.334 3.923  64.329  1.00 38.45 ? 780 HOH A O   1 
HETATM 8413 O O   . HOH G 4 .   ? -12.629 32.207 81.612  1.00 43.80 ? 781 HOH A O   1 
HETATM 8414 O O   . HOH G 4 .   ? -25.008 18.500 64.156  1.00 25.69 ? 782 HOH A O   1 
HETATM 8415 O O   . HOH G 4 .   ? 14.338  21.478 65.121  1.00 18.66 ? 783 HOH A O   1 
HETATM 8416 O O   . HOH G 4 .   ? -25.781 4.232  77.767  1.00 40.82 ? 784 HOH A O   1 
HETATM 8417 O O   . HOH G 4 .   ? 15.101  -1.482 71.608  1.00 40.87 ? 785 HOH A O   1 
HETATM 8418 O O   . HOH G 4 .   ? -18.090 26.152 62.636  1.00 19.66 ? 786 HOH A O   1 
HETATM 8419 O O   . HOH G 4 .   ? 11.022  28.938 71.805  1.00 37.77 ? 787 HOH A O   1 
HETATM 8420 O O   . HOH G 4 .   ? -33.728 24.996 95.989  1.00 34.50 ? 788 HOH A O   1 
HETATM 8421 O O   . HOH G 4 .   ? -4.477  1.848  59.410  1.00 22.00 ? 789 HOH A O   1 
HETATM 8422 O O   . HOH G 4 .   ? 1.615   29.143 60.970  1.00 38.26 ? 790 HOH A O   1 
HETATM 8423 O O   . HOH G 4 .   ? -12.808 33.972 52.173  1.00 36.27 ? 791 HOH A O   1 
HETATM 8424 O O   . HOH G 4 .   ? 0.405   26.550 52.686  1.00 38.04 ? 792 HOH A O   1 
HETATM 8425 O O   . HOH G 4 .   ? -6.390  1.520  53.753  1.00 46.27 ? 793 HOH A O   1 
HETATM 8426 O O   . HOH G 4 .   ? 0.250   -3.106 75.701  1.00 36.61 ? 794 HOH A O   1 
HETATM 8427 O O   . HOH G 4 .   ? -24.333 21.679 99.087  1.00 45.21 ? 795 HOH A O   1 
HETATM 8428 O O   . HOH G 4 .   ? 20.328  3.733  84.319  1.00 35.61 ? 796 HOH A O   1 
HETATM 8429 O O   . HOH G 4 .   ? -2.833  21.036 67.289  1.00 18.88 ? 797 HOH A O   1 
HETATM 8430 O O   . HOH G 4 .   ? -22.023 28.091 69.249  1.00 26.71 ? 798 HOH A O   1 
HETATM 8431 O O   . HOH G 4 .   ? 20.203  5.606  69.281  1.00 38.21 ? 799 HOH A O   1 
HETATM 8432 O O   . HOH G 4 .   ? 6.088   -5.012 63.790  1.00 47.14 ? 800 HOH A O   1 
HETATM 8433 O O   . HOH G 4 .   ? -20.957 8.894  52.285  1.00 42.29 ? 801 HOH A O   1 
HETATM 8434 O O   . HOH G 4 .   ? -36.006 17.629 88.079  1.00 15.79 ? 802 HOH A O   1 
HETATM 8435 O O   . HOH G 4 .   ? 25.019  12.868 78.925  1.00 40.71 ? 803 HOH A O   1 
HETATM 8436 O O   . HOH G 4 .   ? 21.636  10.247 80.717  1.00 28.56 ? 804 HOH A O   1 
HETATM 8437 O O   . HOH G 4 .   ? 21.589  17.218 64.314  1.00 43.17 ? 805 HOH A O   1 
HETATM 8438 O O   . HOH G 4 .   ? -7.265  2.441  82.427  1.00 56.26 ? 806 HOH A O   1 
HETATM 8439 O O   . HOH G 4 .   ? -28.176 29.444 72.930  1.00 47.52 ? 807 HOH A O   1 
HETATM 8440 O O   . HOH G 4 .   ? -1.003  28.397 52.120  1.00 25.36 ? 808 HOH A O   1 
HETATM 8441 O O   . HOH G 4 .   ? 20.254  15.782 54.622  1.00 33.19 ? 809 HOH A O   1 
HETATM 8442 O O   . HOH G 4 .   ? -31.669 13.534 99.630  1.00 48.83 ? 810 HOH A O   1 
HETATM 8443 O O   . HOH G 4 .   ? -22.173 14.806 51.351  1.00 36.01 ? 811 HOH A O   1 
HETATM 8444 O O   . HOH G 4 .   ? 16.884  24.185 86.982  1.00 36.16 ? 812 HOH A O   1 
HETATM 8445 O O   . HOH G 4 .   ? 19.779  12.290 67.785  1.00 21.12 ? 813 HOH A O   1 
HETATM 8446 O O   . HOH G 4 .   ? -35.144 28.737 87.701  1.00 46.25 ? 814 HOH A O   1 
HETATM 8447 O O   . HOH G 4 .   ? 0.808   -7.223 61.835  1.00 44.53 ? 815 HOH A O   1 
HETATM 8448 O O   . HOH G 4 .   ? 5.430   25.104 46.382  1.00 39.47 ? 816 HOH A O   1 
HETATM 8449 O O   . HOH G 4 .   ? -12.868 3.398  50.372  1.00 39.95 ? 817 HOH A O   1 
HETATM 8450 O O   . HOH G 4 .   ? 18.261  20.621 50.639  1.00 33.13 ? 818 HOH A O   1 
HETATM 8451 O O   . HOH G 4 .   ? -15.155 -1.754 71.331  1.00 33.41 ? 819 HOH A O   1 
HETATM 8452 O O   . HOH G 4 .   ? -0.193  9.804  80.938  1.00 14.27 ? 820 HOH A O   1 
HETATM 8453 O O   . HOH G 4 .   ? -0.744  1.808  61.446  1.00 43.03 ? 821 HOH A O   1 
HETATM 8454 O O   . HOH G 4 .   ? -24.622 25.735 70.046  1.00 30.13 ? 822 HOH A O   1 
HETATM 8455 O O   . HOH G 4 .   ? 2.397   21.752 71.673  1.00 49.95 ? 823 HOH A O   1 
HETATM 8456 O O   . HOH G 4 .   ? -29.627 27.285 73.134  1.00 39.26 ? 824 HOH A O   1 
HETATM 8457 O O   . HOH G 4 .   ? 20.124  20.194 52.446  1.00 45.25 ? 825 HOH A O   1 
HETATM 8458 O O   . HOH G 4 .   ? -3.868  22.485 70.488  1.00 42.20 ? 826 HOH A O   1 
HETATM 8459 O O   . HOH G 4 .   ? 21.841  13.631 66.690  1.00 36.29 ? 827 HOH A O   1 
HETATM 8460 O O   . HOH G 4 .   ? -17.921 4.704  83.177  1.00 29.77 ? 828 HOH A O   1 
HETATM 8461 O O   . HOH G 4 .   ? -19.807 2.295  65.668  1.00 33.82 ? 829 HOH A O   1 
HETATM 8462 O O   . HOH G 4 .   ? 16.240  18.962 50.691  1.00 34.94 ? 830 HOH A O   1 
HETATM 8463 O O   . HOH G 4 .   ? -35.894 29.428 89.870  1.00 51.90 ? 831 HOH A O   1 
HETATM 8464 O O   . HOH G 4 .   ? -13.106 -2.178 73.879  1.00 46.59 ? 832 HOH A O   1 
HETATM 8465 O O   . HOH G 4 .   ? -9.269  -3.031 59.247  1.00 41.52 ? 833 HOH A O   1 
HETATM 8466 O O   . HOH G 4 .   ? 25.098  13.660 73.203  1.00 39.66 ? 834 HOH A O   1 
HETATM 8467 O O   . HOH G 4 .   ? 11.954  9.515  94.687  1.00 38.80 ? 835 HOH A O   1 
HETATM 8468 O O   . HOH G 4 .   ? 13.315  28.282 79.265  1.00 49.97 ? 836 HOH A O   1 
HETATM 8469 O O   . HOH G 4 .   ? -38.476 7.876  80.887  1.00 44.39 ? 837 HOH A O   1 
HETATM 8470 O O   . HOH G 4 .   ? 7.387   10.232 95.307  1.00 41.01 ? 838 HOH A O   1 
HETATM 8471 O O   . HOH G 4 .   ? 2.352   24.268 68.399  1.00 47.68 ? 839 HOH A O   1 
HETATM 8472 O O   . HOH G 4 .   ? -2.023  0.560  59.779  1.00 40.76 ? 840 HOH A O   1 
HETATM 8473 O O   . HOH G 4 .   ? -0.885  22.107 66.221  1.00 36.00 ? 841 HOH A O   1 
HETATM 8474 O O   . HOH G 4 .   ? 3.104   26.234 66.925  1.00 45.04 ? 842 HOH A O   1 
HETATM 8475 O O   . HOH G 4 .   ? -11.215 10.747 47.666  1.00 41.89 ? 843 HOH A O   1 
HETATM 8476 O O   . HOH G 4 .   ? -21.395 7.958  85.096  1.00 43.45 ? 844 HOH A O   1 
HETATM 8477 O O   . HOH G 4 .   ? 21.402  20.163 54.609  1.00 54.90 ? 845 HOH A O   1 
HETATM 8478 O O   . HOH G 4 .   ? -7.895  -4.444 77.336  1.00 50.87 ? 846 HOH A O   1 
HETATM 8479 O O   . HOH G 4 .   ? 7.837   28.567 64.830  1.00 43.29 ? 847 HOH A O   1 
HETATM 8480 O O   . HOH G 4 .   ? -0.005  -1.045 80.028  1.00 42.68 ? 848 HOH A O   1 
HETATM 8481 O O   . HOH G 4 .   ? 23.774  15.068 71.654  1.00 39.86 ? 849 HOH A O   1 
HETATM 8482 O O   . HOH G 4 .   ? -5.229  22.579 68.076  1.00 31.45 ? 850 HOH A O   1 
HETATM 8483 O O   . HOH G 4 .   ? 14.583  -3.888 68.258  1.00 50.29 ? 851 HOH A O   1 
HETATM 8484 O O   . HOH G 4 .   ? 25.717  11.503 90.109  1.00 49.06 ? 852 HOH A O   1 
HETATM 8485 O O   . HOH G 4 .   ? -22.407 -0.223 71.208  1.00 47.81 ? 853 HOH A O   1 
HETATM 8486 O O   . HOH G 4 .   ? -21.204 -0.001 67.077  1.00 47.11 ? 854 HOH A O   1 
HETATM 8487 O O   . HOH G 4 .   ? 10.788  24.577 91.654  1.00 48.35 ? 855 HOH A O   1 
HETATM 8488 O O   . HOH G 4 .   ? -25.345 21.197 64.923  1.00 39.73 ? 856 HOH A O   1 
HETATM 8489 O O   . HOH G 4 .   ? 17.219  2.553  86.152  1.00 45.56 ? 857 HOH A O   1 
HETATM 8490 O O   . HOH G 4 .   ? 0.648   22.579 67.567  1.00 41.31 ? 858 HOH A O   1 
HETATM 8491 O O   . HOH G 4 .   ? -10.759 19.517 91.322  1.00 46.92 ? 859 HOH A O   1 
HETATM 8492 O O   . HOH G 4 .   ? -24.009 29.370 68.839  1.00 44.07 ? 860 HOH A O   1 
HETATM 8493 O O   . HOH G 4 .   ? -26.190 10.394 95.250  1.00 45.76 ? 861 HOH A O   1 
HETATM 8494 O O   . HOH G 4 .   ? 21.642  3.775  86.570  1.00 52.08 ? 862 HOH A O   1 
HETATM 8495 O O   . HOH G 4 .   ? -30.728 29.087 74.838  1.00 44.77 ? 863 HOH A O   1 
HETATM 8496 O O   . HOH G 4 .   ? 0.025   21.921 70.906  1.00 45.26 ? 864 HOH A O   1 
HETATM 8497 O O   . HOH G 4 .   ? -15.272 -0.436 73.666  1.00 35.65 ? 865 HOH A O   1 
HETATM 8498 O O   . HOH G 4 .   ? 17.224  29.006 75.210  1.00 45.90 ? 866 HOH A O   1 
HETATM 8499 O O   . HOH G 4 .   ? -25.236 1.379  73.729  1.00 44.39 ? 867 HOH A O   1 
HETATM 8500 O O   . HOH G 4 .   ? 15.751  29.499 78.157  1.00 55.40 ? 868 HOH A O   1 
HETATM 8501 O O   . HOH H 4 .   ? -24.119 30.733 -0.400  1.00 39.05 ? 601 HOH B O   1 
HETATM 8502 O O   . HOH H 4 .   ? -53.241 39.509 11.330  1.00 38.46 ? 602 HOH B O   1 
HETATM 8503 O O   . HOH H 4 .   ? -50.846 17.933 6.687   1.00 41.86 ? 603 HOH B O   1 
HETATM 8504 O O   . HOH H 4 .   ? -24.989 30.535 9.829   1.00 20.00 ? 604 HOH B O   1 
HETATM 8505 O O   . HOH H 4 .   ? -26.293 21.140 10.059  1.00 23.44 ? 605 HOH B O   1 
HETATM 8506 O O   . HOH H 4 .   ? -8.737  28.653 39.484  1.00 53.40 ? 606 HOH B O   1 
HETATM 8507 O O   . HOH H 4 .   ? -45.235 39.932 50.806  1.00 29.96 ? 607 HOH B O   1 
HETATM 8508 O O   . HOH H 4 .   ? -12.750 25.185 43.412  1.00 40.43 ? 608 HOH B O   1 
HETATM 8509 O O   . HOH H 4 .   ? -21.529 13.701 42.040  1.00 42.55 ? 609 HOH B O   1 
HETATM 8510 O O   . HOH H 4 .   ? -6.181  28.762 1.484   1.00 38.08 ? 610 HOH B O   1 
HETATM 8511 O O   . HOH H 4 .   ? -16.692 37.307 -7.009  1.00 33.60 ? 611 HOH B O   1 
HETATM 8512 O O   . HOH H 4 .   ? -12.805 49.861 37.512  1.00 39.65 ? 612 HOH B O   1 
HETATM 8513 O O   . HOH H 4 .   ? -24.185 14.336 42.042  1.00 34.16 ? 613 HOH B O   1 
HETATM 8514 O O   . HOH H 4 .   ? -32.137 39.168 6.523   1.00 50.43 ? 614 HOH B O   1 
HETATM 8515 O O   . HOH H 4 .   ? -38.952 35.468 22.862  1.00 16.12 ? 615 HOH B O   1 
HETATM 8516 O O   . HOH H 4 .   ? -54.450 44.294 19.460  1.00 33.11 ? 616 HOH B O   1 
HETATM 8517 O O   . HOH H 4 .   ? -39.622 42.944 33.969  1.00 28.91 ? 617 HOH B O   1 
HETATM 8518 O O   . HOH H 4 .   ? -20.795 36.061 49.359  1.00 39.99 ? 618 HOH B O   1 
HETATM 8519 O O   . HOH H 4 .   ? -41.087 16.521 41.540  1.00 39.56 ? 619 HOH B O   1 
HETATM 8520 O O   . HOH H 4 .   ? -48.352 44.964 33.453  1.00 31.92 ? 620 HOH B O   1 
HETATM 8521 O O   . HOH H 4 .   ? -34.725 21.994 35.156  1.00 32.23 ? 621 HOH B O   1 
HETATM 8522 O O   . HOH H 4 .   ? -54.803 19.745 23.467  1.00 42.40 ? 622 HOH B O   1 
HETATM 8523 O O   . HOH H 4 .   ? -51.526 20.440 29.322  1.00 32.23 ? 623 HOH B O   1 
HETATM 8524 O O   . HOH H 4 .   ? -54.886 25.789 23.729  1.00 25.59 ? 624 HOH B O   1 
HETATM 8525 O O   . HOH H 4 .   ? -21.781 30.455 3.215   1.00 24.84 ? 625 HOH B O   1 
HETATM 8526 O O   . HOH H 4 .   ? -26.329 38.912 21.604  1.00 18.03 ? 626 HOH B O   1 
HETATM 8527 O O   . HOH H 4 .   ? -13.673 31.470 23.003  1.00 17.86 ? 627 HOH B O   1 
HETATM 8528 O O   . HOH H 4 .   ? -26.195 32.216 43.063  1.00 13.60 ? 628 HOH B O   1 
HETATM 8529 O O   . HOH H 4 .   ? -23.064 39.079 24.671  1.00 12.21 ? 629 HOH B O   1 
HETATM 8530 O O   . HOH H 4 .   ? -45.196 39.324 55.099  1.00 48.22 ? 630 HOH B O   1 
HETATM 8531 O O   . HOH H 4 .   ? -11.219 26.336 31.691  1.00 35.30 ? 631 HOH B O   1 
HETATM 8532 O O   . HOH H 4 .   ? -44.872 30.676 22.046  1.00 33.94 ? 632 HOH B O   1 
HETATM 8533 O O   . HOH H 4 .   ? -21.466 33.640 48.597  1.00 25.40 ? 633 HOH B O   1 
HETATM 8534 O O   . HOH H 4 .   ? 0.914   39.760 18.804  1.00 30.53 ? 634 HOH B O   1 
HETATM 8535 O O   . HOH H 4 .   ? -27.720 39.011 28.856  1.00 10.47 ? 635 HOH B O   1 
HETATM 8536 O O   . HOH H 4 .   ? -12.152 29.723 34.710  1.00 29.95 ? 636 HOH B O   1 
HETATM 8537 O O   . HOH H 4 .   ? -18.955 18.610 26.675  1.00 21.94 ? 637 HOH B O   1 
HETATM 8538 O O   . HOH H 4 .   ? -52.240 38.845 30.593  1.00 18.75 ? 638 HOH B O   1 
HETATM 8539 O O   . HOH H 4 .   ? -20.068 48.423 2.807   1.00 59.76 ? 639 HOH B O   1 
HETATM 8540 O O   . HOH H 4 .   ? -40.239 42.260 12.035  1.00 38.56 ? 640 HOH B O   1 
HETATM 8541 O O   . HOH H 4 .   ? -32.622 42.009 32.886  1.00 41.65 ? 641 HOH B O   1 
HETATM 8542 O O   . HOH H 4 .   ? -11.061 34.125 43.408  1.00 40.39 ? 642 HOH B O   1 
HETATM 8543 O O   . HOH H 4 .   ? -44.053 29.243 31.180  1.00 13.19 ? 643 HOH B O   1 
HETATM 8544 O O   . HOH H 4 .   ? -28.876 21.311 39.354  1.00 20.90 ? 644 HOH B O   1 
HETATM 8545 O O   . HOH H 4 .   ? -25.766 22.628 50.071  1.00 39.76 ? 645 HOH B O   1 
HETATM 8546 O O   . HOH H 4 .   ? -34.230 20.195 18.645  1.00 31.66 ? 646 HOH B O   1 
HETATM 8547 O O   . HOH H 4 .   ? -26.811 22.815 46.104  1.00 30.51 ? 647 HOH B O   1 
HETATM 8548 O O   . HOH H 4 .   ? -55.800 46.190 26.484  1.00 49.92 ? 648 HOH B O   1 
HETATM 8549 O O   . HOH H 4 .   ? -11.852 30.407 -5.860  1.00 43.98 ? 649 HOH B O   1 
HETATM 8550 O O   . HOH H 4 .   ? -11.968 43.509 37.443  1.00 26.26 ? 650 HOH B O   1 
HETATM 8551 O O   . HOH H 4 .   ? -26.383 45.646 16.729  1.00 40.73 ? 651 HOH B O   1 
HETATM 8552 O O   . HOH H 4 .   ? 1.976   31.954 22.978  1.00 42.45 ? 652 HOH B O   1 
HETATM 8553 O O   . HOH H 4 .   ? -27.756 45.502 27.050  1.00 40.67 ? 653 HOH B O   1 
HETATM 8554 O O   . HOH H 4 .   ? -11.468 27.560 1.012   1.00 30.85 ? 654 HOH B O   1 
HETATM 8555 O O   . HOH H 4 .   ? -12.492 42.288 21.589  1.00 27.25 ? 655 HOH B O   1 
HETATM 8556 O O   . HOH H 4 .   ? -36.563 45.926 41.704  1.00 25.21 ? 656 HOH B O   1 
HETATM 8557 O O   . HOH H 4 .   ? -12.964 31.002 25.775  1.00 17.82 ? 657 HOH B O   1 
HETATM 8558 O O   . HOH H 4 .   ? -10.499 24.843 6.818   1.00 43.58 ? 658 HOH B O   1 
HETATM 8559 O O   . HOH H 4 .   ? -13.775 36.024 -3.549  1.00 35.19 ? 659 HOH B O   1 
HETATM 8560 O O   . HOH H 4 .   ? -19.279 47.845 34.188  1.00 19.07 ? 660 HOH B O   1 
HETATM 8561 O O   . HOH H 4 .   ? -52.733 30.167 30.801  1.00 17.35 ? 661 HOH B O   1 
HETATM 8562 O O   . HOH H 4 .   ? -33.030 42.268 7.379   1.00 56.37 ? 662 HOH B O   1 
HETATM 8563 O O   . HOH H 4 .   ? -36.791 35.712 52.973  1.00 24.32 ? 663 HOH B O   1 
HETATM 8564 O O   . HOH H 4 .   ? -39.476 16.460 37.697  1.00 47.57 ? 664 HOH B O   1 
HETATM 8565 O O   . HOH H 4 .   ? -48.562 43.403 20.196  1.00 33.39 ? 665 HOH B O   1 
HETATM 8566 O O   . HOH H 4 .   ? -39.648 36.358 45.656  1.00 18.92 ? 666 HOH B O   1 
HETATM 8567 O O   . HOH H 4 .   ? -36.257 43.007 31.896  1.00 29.86 ? 667 HOH B O   1 
HETATM 8568 O O   . HOH H 4 .   ? -11.589 28.999 32.279  1.00 28.21 ? 668 HOH B O   1 
HETATM 8569 O O   . HOH H 4 .   ? -30.917 33.900 26.898  1.00 12.19 ? 669 HOH B O   1 
HETATM 8570 O O   . HOH H 4 .   ? -35.747 38.502 44.510  1.00 19.43 ? 670 HOH B O   1 
HETATM 8571 O O   . HOH H 4 .   ? -12.230 20.140 23.692  1.00 37.09 ? 671 HOH B O   1 
HETATM 8572 O O   . HOH H 4 .   ? -15.221 38.758 23.209  1.00 18.55 ? 672 HOH B O   1 
HETATM 8573 O O   . HOH H 4 .   ? -56.139 27.147 22.010  1.00 40.41 ? 673 HOH B O   1 
HETATM 8574 O O   . HOH H 4 .   ? -31.602 26.424 3.813   1.00 45.65 ? 674 HOH B O   1 
HETATM 8575 O O   . HOH H 4 .   ? -16.586 24.750 10.316  1.00 45.52 ? 675 HOH B O   1 
HETATM 8576 O O   . HOH H 4 .   ? -20.998 34.443 53.153  1.00 43.78 ? 676 HOH B O   1 
HETATM 8577 O O   . HOH H 4 .   ? -43.345 30.393 28.859  1.00 18.46 ? 677 HOH B O   1 
HETATM 8578 O O   . HOH H 4 .   ? -4.243  39.122 5.805   1.00 22.70 ? 678 HOH B O   1 
HETATM 8579 O O   . HOH H 4 .   ? -11.971 23.881 12.918  1.00 35.31 ? 679 HOH B O   1 
HETATM 8580 O O   . HOH H 4 .   ? -53.230 33.695 35.619  1.00 17.13 ? 680 HOH B O   1 
HETATM 8581 O O   . HOH H 4 .   ? -24.205 28.571 49.556  1.00 32.26 ? 681 HOH B O   1 
HETATM 8582 O O   . HOH H 4 .   ? -15.240 48.298 15.209  1.00 31.58 ? 682 HOH B O   1 
HETATM 8583 O O   . HOH H 4 .   ? -0.881  33.636 23.146  1.00 25.23 ? 683 HOH B O   1 
HETATM 8584 O O   . HOH H 4 .   ? -4.341  47.530 14.327  1.00 37.46 ? 684 HOH B O   1 
HETATM 8585 O O   . HOH H 4 .   ? -20.704 33.822 35.154  1.00 13.58 ? 685 HOH B O   1 
HETATM 8586 O O   . HOH H 4 .   ? -30.839 42.608 8.694   1.00 45.23 ? 686 HOH B O   1 
HETATM 8587 O O   . HOH H 4 .   ? -37.311 28.657 20.375  1.00 12.47 ? 687 HOH B O   1 
HETATM 8588 O O   . HOH H 4 .   ? -18.726 54.833 35.847  1.00 30.67 ? 688 HOH B O   1 
HETATM 8589 O O   . HOH H 4 .   ? -58.243 21.107 19.256  1.00 41.52 ? 689 HOH B O   1 
HETATM 8590 O O   . HOH H 4 .   ? -48.759 45.480 44.826  1.00 37.25 ? 690 HOH B O   1 
HETATM 8591 O O   . HOH H 4 .   ? -17.322 28.076 43.109  1.00 37.66 ? 691 HOH B O   1 
HETATM 8592 O O   . HOH H 4 .   ? -25.910 29.007 15.194  1.00 12.94 ? 692 HOH B O   1 
HETATM 8593 O O   . HOH H 4 .   ? -38.372 39.498 26.658  1.00 39.74 ? 693 HOH B O   1 
HETATM 8594 O O   . HOH H 4 .   ? -11.646 39.517 21.833  1.00 27.48 ? 694 HOH B O   1 
HETATM 8595 O O   . HOH H 4 .   ? 0.637   31.501 9.505   1.00 28.26 ? 695 HOH B O   1 
HETATM 8596 O O   . HOH H 4 .   ? -50.288 27.292 8.265   1.00 34.57 ? 696 HOH B O   1 
HETATM 8597 O O   . HOH H 4 .   ? -38.349 35.062 4.820   1.00 23.30 ? 697 HOH B O   1 
HETATM 8598 O O   . HOH H 4 .   ? -44.838 19.088 41.718  1.00 29.68 ? 698 HOH B O   1 
HETATM 8599 O O   . HOH H 4 .   ? -42.349 27.114 54.805  1.00 29.89 ? 699 HOH B O   1 
HETATM 8600 O O   . HOH H 4 .   ? -20.519 20.325 24.561  1.00 18.75 ? 700 HOH B O   1 
HETATM 8601 O O   . HOH H 4 .   ? -8.308  40.216 25.997  1.00 38.18 ? 701 HOH B O   1 
HETATM 8602 O O   . HOH H 4 .   ? -60.108 36.564 16.473  1.00 31.18 ? 702 HOH B O   1 
HETATM 8603 O O   . HOH H 4 .   ? -58.864 42.167 32.493  1.00 40.12 ? 703 HOH B O   1 
HETATM 8604 O O   . HOH H 4 .   ? -28.409 17.311 18.782  1.00 34.13 ? 704 HOH B O   1 
HETATM 8605 O O   . HOH H 4 .   ? -16.249 48.765 18.595  1.00 25.96 ? 705 HOH B O   1 
HETATM 8606 O O   . HOH H 4 .   ? -3.733  26.116 11.570  1.00 33.10 ? 706 HOH B O   1 
HETATM 8607 O O   . HOH H 4 .   ? -7.038  47.952 17.751  1.00 29.07 ? 707 HOH B O   1 
HETATM 8608 O O   . HOH H 4 .   ? -42.209 29.613 56.670  1.00 45.13 ? 708 HOH B O   1 
HETATM 8609 O O   . HOH H 4 .   ? -38.205 46.060 44.995  1.00 42.46 ? 709 HOH B O   1 
HETATM 8610 O O   . HOH H 4 .   ? -33.524 21.086 11.765  1.00 27.65 ? 710 HOH B O   1 
HETATM 8611 O O   . HOH H 4 .   ? -46.840 27.301 54.248  1.00 39.97 ? 711 HOH B O   1 
HETATM 8612 O O   . HOH H 4 .   ? -6.649  45.914 14.859  1.00 26.01 ? 712 HOH B O   1 
HETATM 8613 O O   . HOH H 4 .   ? -14.548 32.019 32.041  1.00 13.27 ? 713 HOH B O   1 
HETATM 8614 O O   . HOH H 4 .   ? -49.313 33.254 53.690  1.00 35.38 ? 714 HOH B O   1 
HETATM 8615 O O   . HOH H 4 .   ? -21.712 24.019 49.287  1.00 46.06 ? 715 HOH B O   1 
HETATM 8616 O O   . HOH H 4 .   ? -3.100  32.808 4.118   1.00 25.77 ? 716 HOH B O   1 
HETATM 8617 O O   . HOH H 4 .   ? -32.002 48.462 44.178  1.00 46.42 ? 717 HOH B O   1 
HETATM 8618 O O   . HOH H 4 .   ? -36.634 33.443 28.913  1.00 10.59 ? 718 HOH B O   1 
HETATM 8619 O O   . HOH H 4 .   ? -11.688 42.829 43.817  1.00 38.63 ? 719 HOH B O   1 
HETATM 8620 O O   . HOH H 4 .   ? -25.136 21.575 42.439  1.00 32.20 ? 720 HOH B O   1 
HETATM 8621 O O   . HOH H 4 .   ? -25.580 46.388 30.656  1.00 14.16 ? 721 HOH B O   1 
HETATM 8622 O O   . HOH H 4 .   ? -9.859  24.746 11.679  1.00 38.24 ? 722 HOH B O   1 
HETATM 8623 O O   . HOH H 4 .   ? -8.614  31.592 34.478  1.00 35.52 ? 723 HOH B O   1 
HETATM 8624 O O   . HOH H 4 .   ? -48.374 35.696 6.024   1.00 37.36 ? 724 HOH B O   1 
HETATM 8625 O O   . HOH H 4 .   ? -6.072  38.701 25.886  1.00 33.56 ? 725 HOH B O   1 
HETATM 8626 O O   . HOH H 4 .   ? -40.636 45.403 31.234  1.00 35.82 ? 726 HOH B O   1 
HETATM 8627 O O   . HOH H 4 .   ? -52.989 35.630 47.162  1.00 43.44 ? 727 HOH B O   1 
HETATM 8628 O O   . HOH H 4 .   ? -48.812 40.297 34.927  1.00 20.42 ? 728 HOH B O   1 
HETATM 8629 O O   . HOH H 4 .   ? -51.517 17.766 20.285  1.00 40.97 ? 729 HOH B O   1 
HETATM 8630 O O   . HOH H 4 .   ? -46.147 30.077 54.244  1.00 36.77 ? 730 HOH B O   1 
HETATM 8631 O O   . HOH H 4 .   ? -23.033 47.567 16.556  1.00 27.95 ? 731 HOH B O   1 
HETATM 8632 O O   . HOH H 4 .   ? -17.730 30.485 26.184  1.00 13.57 ? 732 HOH B O   1 
HETATM 8633 O O   . HOH H 4 .   ? -28.698 32.632 6.027   1.00 37.69 ? 733 HOH B O   1 
HETATM 8634 O O   . HOH H 4 .   ? -31.755 48.390 46.909  1.00 36.78 ? 734 HOH B O   1 
HETATM 8635 O O   . HOH H 4 .   ? -24.169 23.416 46.922  1.00 32.90 ? 735 HOH B O   1 
HETATM 8636 O O   . HOH H 4 .   ? -11.847 37.852 46.526  1.00 44.93 ? 736 HOH B O   1 
HETATM 8637 O O   . HOH H 4 .   ? -22.085 30.342 49.177  1.00 35.41 ? 737 HOH B O   1 
HETATM 8638 O O   . HOH H 4 .   ? -51.132 40.642 27.737  1.00 26.08 ? 738 HOH B O   1 
HETATM 8639 O O   . HOH H 4 .   ? -21.415 49.785 24.865  1.00 42.91 ? 739 HOH B O   1 
HETATM 8640 O O   . HOH H 4 .   ? -13.456 46.004 24.810  1.00 26.62 ? 740 HOH B O   1 
HETATM 8641 O O   . HOH H 4 .   ? -50.037 45.540 30.807  1.00 38.94 ? 741 HOH B O   1 
HETATM 8642 O O   . HOH H 4 .   ? -44.875 42.068 26.209  1.00 27.39 ? 742 HOH B O   1 
HETATM 8643 O O   . HOH H 4 .   ? -32.307 39.474 30.069  1.00 23.16 ? 743 HOH B O   1 
HETATM 8644 O O   . HOH H 4 .   ? -47.278 16.366 40.581  1.00 38.22 ? 744 HOH B O   1 
HETATM 8645 O O   . HOH H 4 .   ? -35.777 48.132 35.679  1.00 39.73 ? 745 HOH B O   1 
HETATM 8646 O O   . HOH H 4 .   ? -13.471 22.260 31.035  1.00 35.71 ? 746 HOH B O   1 
HETATM 8647 O O   . HOH H 4 .   ? -55.813 36.292 37.453  1.00 41.33 ? 747 HOH B O   1 
HETATM 8648 O O   . HOH H 4 .   ? -9.421  36.749 29.833  1.00 24.65 ? 748 HOH B O   1 
HETATM 8649 O O   . HOH H 4 .   ? -25.266 45.298 28.187  1.00 17.85 ? 749 HOH B O   1 
HETATM 8650 O O   . HOH H 4 .   ? -39.809 35.593 12.795  1.00 24.72 ? 750 HOH B O   1 
HETATM 8651 O O   . HOH H 4 .   ? -26.878 17.351 10.706  1.00 45.63 ? 751 HOH B O   1 
HETATM 8652 O O   . HOH H 4 .   ? -10.185 42.111 36.428  1.00 51.70 ? 752 HOH B O   1 
HETATM 8653 O O   . HOH H 4 .   ? -51.848 20.378 21.663  1.00 27.97 ? 753 HOH B O   1 
HETATM 8654 O O   . HOH H 4 .   ? -6.628  39.796 -3.708  1.00 36.70 ? 754 HOH B O   1 
HETATM 8655 O O   . HOH H 4 .   ? -16.390 44.595 32.045  1.00 14.04 ? 755 HOH B O   1 
HETATM 8656 O O   . HOH H 4 .   ? -53.096 23.522 33.463  1.00 35.33 ? 756 HOH B O   1 
HETATM 8657 O O   . HOH H 4 .   ? -20.089 21.642 13.355  1.00 33.11 ? 757 HOH B O   1 
HETATM 8658 O O   . HOH H 4 .   ? -45.122 44.823 26.036  1.00 68.22 ? 758 HOH B O   1 
HETATM 8659 O O   . HOH H 4 .   ? -55.347 23.951 33.346  1.00 46.26 ? 759 HOH B O   1 
HETATM 8660 O O   . HOH H 4 .   ? -2.336  45.915 7.553   1.00 54.91 ? 760 HOH B O   1 
HETATM 8661 O O   . HOH H 4 .   ? -14.746 48.481 33.355  1.00 28.82 ? 761 HOH B O   1 
HETATM 8662 O O   . HOH H 4 .   ? -4.481  46.719 3.687   1.00 47.27 ? 762 HOH B O   1 
HETATM 8663 O O   . HOH H 4 .   ? -16.472 37.317 -4.241  1.00 34.90 ? 763 HOH B O   1 
HETATM 8664 O O   . HOH H 4 .   ? -57.034 28.876 38.303  1.00 38.76 ? 764 HOH B O   1 
HETATM 8665 O O   . HOH H 4 .   ? -54.619 31.029 34.042  1.00 22.11 ? 765 HOH B O   1 
HETATM 8666 O O   . HOH H 4 .   ? -44.927 13.803 35.128  1.00 48.08 ? 766 HOH B O   1 
HETATM 8667 O O   . HOH H 4 .   ? -47.087 47.182 27.059  1.00 44.35 ? 767 HOH B O   1 
HETATM 8668 O O   . HOH H 4 .   ? -42.214 32.997 57.181  1.00 31.42 ? 768 HOH B O   1 
HETATM 8669 O O   . HOH H 4 .   ? -9.131  36.957 32.588  1.00 39.05 ? 769 HOH B O   1 
HETATM 8670 O O   . HOH H 4 .   ? -16.207 48.159 43.842  1.00 43.25 ? 770 HOH B O   1 
HETATM 8671 O O   . HOH H 4 .   ? -24.104 52.787 25.670  1.00 45.03 ? 771 HOH B O   1 
HETATM 8672 O O   . HOH H 4 .   ? -54.559 37.637 40.203  1.00 44.96 ? 772 HOH B O   1 
HETATM 8673 O O   . HOH H 4 .   ? -56.531 32.592 35.322  1.00 41.44 ? 773 HOH B O   1 
HETATM 8674 O O   . HOH H 4 .   ? -39.778 26.829 55.352  1.00 41.71 ? 774 HOH B O   1 
HETATM 8675 O O   . HOH H 4 .   ? -53.113 36.369 45.100  1.00 43.19 ? 775 HOH B O   1 
HETATM 8676 O O   . HOH H 4 .   ? -12.902 23.387 39.508  1.00 44.92 ? 776 HOH B O   1 
HETATM 8677 O O   . HOH H 4 .   ? -25.984 51.904 45.616  1.00 46.97 ? 777 HOH B O   1 
HETATM 8678 O O   . HOH H 4 .   ? -45.883 36.563 54.932  1.00 42.63 ? 778 HOH B O   1 
HETATM 8679 O O   . HOH H 4 .   ? -15.223 21.075 30.413  1.00 32.64 ? 779 HOH B O   1 
HETATM 8680 O O   . HOH H 4 .   ? -39.254 43.545 57.841  1.00 26.91 ? 780 HOH B O   1 
HETATM 8681 O O   . HOH H 4 .   ? -36.932 26.908 18.397  1.00 15.27 ? 781 HOH B O   1 
HETATM 8682 O O   . HOH H 4 .   ? -4.501  24.460 9.757   1.00 49.31 ? 782 HOH B O   1 
HETATM 8683 O O   . HOH H 4 .   ? -4.566  22.550 19.786  1.00 45.15 ? 783 HOH B O   1 
HETATM 8684 O O   . HOH H 4 .   ? -44.065 14.084 37.322  1.00 44.82 ? 784 HOH B O   1 
HETATM 8685 O O   . HOH H 4 .   ? -2.220  37.012 4.586   1.00 41.68 ? 785 HOH B O   1 
HETATM 8686 O O   . HOH H 4 .   ? -20.919 45.026 55.986  1.00 43.90 ? 786 HOH B O   1 
HETATM 8687 O O   . HOH H 4 .   ? -17.121 50.825 21.403  1.00 43.28 ? 787 HOH B O   1 
HETATM 8688 O O   . HOH H 4 .   ? -14.103 48.614 44.069  1.00 47.04 ? 788 HOH B O   1 
HETATM 8689 O O   . HOH H 4 .   ? -55.122 30.901 32.015  1.00 25.09 ? 789 HOH B O   1 
HETATM 8690 O O   . HOH H 4 .   ? -27.702 21.047 41.740  1.00 42.87 ? 790 HOH B O   1 
HETATM 8691 O O   . HOH H 4 .   ? -20.894 16.282 26.141  1.00 46.65 ? 791 HOH B O   1 
HETATM 8692 O O   . HOH H 4 .   ? -36.330 49.095 33.807  1.00 44.70 ? 792 HOH B O   1 
HETATM 8693 O O   . HOH H 4 .   ? -17.048 47.100 32.805  1.00 21.36 ? 793 HOH B O   1 
HETATM 8694 O O   . HOH H 4 .   ? -10.101 36.319 43.649  1.00 46.00 ? 794 HOH B O   1 
HETATM 8695 O O   . HOH H 4 .   ? -34.396 40.715 31.032  1.00 44.24 ? 795 HOH B O   1 
HETATM 8696 O O   . HOH H 4 .   ? -20.013 29.460 48.467  1.00 46.51 ? 796 HOH B O   1 
HETATM 8697 O O   . HOH H 4 .   ? -35.904 18.867 15.675  1.00 43.73 ? 797 HOH B O   1 
HETATM 8698 O O   . HOH H 4 .   ? -40.402 46.108 46.966  1.00 41.47 ? 798 HOH B O   1 
HETATM 8699 O O   . HOH H 4 .   ? -57.072 37.987 36.634  1.00 42.45 ? 799 HOH B O   1 
HETATM 8700 O O   . HOH H 4 .   ? -22.575 25.421 5.210   1.00 46.10 ? 800 HOH B O   1 
HETATM 8701 O O   . HOH H 4 .   ? -12.612 48.500 34.355  1.00 44.22 ? 801 HOH B O   1 
HETATM 8702 O O   . HOH H 4 .   ? -18.075 16.162 33.558  1.00 51.24 ? 802 HOH B O   1 
HETATM 8703 O O   . HOH H 4 .   ? -57.288 30.448 35.753  1.00 42.84 ? 803 HOH B O   1 
HETATM 8704 O O   . HOH H 4 .   ? -0.005  35.199 30.021  1.00 47.60 ? 804 HOH B O   1 
HETATM 8705 O O   . HOH H 4 .   ? -28.036 21.267 48.509  1.00 41.75 ? 805 HOH B O   1 
HETATM 8706 O O   . HOH H 4 .   ? -29.837 40.892 28.370  1.00 30.90 ? 806 HOH B O   1 
HETATM 8707 O O   . HOH H 4 .   ? -22.180 27.292 3.342   1.00 44.38 ? 807 HOH B O   1 
HETATM 8708 O O   . HOH H 4 .   ? -54.109 46.989 24.246  1.00 50.78 ? 808 HOH B O   1 
HETATM 8709 O O   . HOH H 4 .   ? -37.766 17.583 15.646  1.00 44.34 ? 809 HOH B O   1 
HETATM 8710 O O   . HOH H 4 .   ? -19.462 47.386 -2.090  1.00 47.56 ? 810 HOH B O   1 
HETATM 8711 O O   . HOH H 4 .   ? -7.978  39.188 52.435  1.00 44.85 ? 811 HOH B O   1 
HETATM 8712 O O   . HOH H 4 .   ? -32.963 39.967 22.141  1.00 45.12 ? 812 HOH B O   1 
HETATM 8713 O O   . HOH H 4 .   ? -5.730  45.668 17.527  1.00 40.60 ? 813 HOH B O   1 
HETATM 8714 O O   . HOH H 4 .   ? -61.246 42.764 31.758  1.00 52.29 ? 814 HOH B O   1 
HETATM 8715 O O   . HOH H 4 .   ? -24.522 48.368 18.898  1.00 40.73 ? 815 HOH B O   1 
HETATM 8716 O O   . HOH H 4 .   ? -21.662 17.511 23.551  1.00 45.71 ? 816 HOH B O   1 
HETATM 8717 O O   . HOH H 4 .   ? -10.344 47.314 33.747  1.00 45.48 ? 817 HOH B O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . LYS A 2   ? 0.5092 0.5399 0.2831 -0.1677 -0.0101 0.0073  2   LYS A N   
2    C CA  . LYS A 2   ? 0.4433 0.4685 0.2250 -0.1655 -0.0060 0.0063  2   LYS A CA  
3    C C   . LYS A 2   ? 0.4322 0.4501 0.2223 -0.1594 -0.0105 0.0110  2   LYS A C   
4    O O   . LYS A 2   ? 0.5142 0.5270 0.3022 -0.1577 -0.0164 0.0202  2   LYS A O   
5    C CB  . LYS A 2   ? 0.4685 0.4914 0.2440 -0.1689 -0.0044 0.0114  2   LYS A CB  
6    C CG  . LYS A 2   ? 0.5072 0.5259 0.2905 -0.1672 0.0002  0.0095  2   LYS A CG  
7    C CD  . LYS A 2   ? 0.6045 0.6202 0.3815 -0.1707 0.0013  0.0150  2   LYS A CD  
8    C CE  . LYS A 2   ? 0.6205 0.6277 0.3946 -0.1681 -0.0057 0.0266  2   LYS A CE  
9    N NZ  . LYS A 2   ? 0.5750 0.5775 0.3441 -0.1707 -0.0043 0.0321  2   LYS A NZ  
10   N N   . LYS A 3   ? 0.3772 0.3946 0.1772 -0.1557 -0.0076 0.0047  3   LYS A N   
11   C CA  . LYS A 3   ? 0.3494 0.3608 0.1577 -0.1500 -0.0114 0.0079  3   LYS A CA  
12   C C   . LYS A 3   ? 0.4033 0.4094 0.2177 -0.1478 -0.0083 0.0087  3   LYS A C   
13   O O   . LYS A 3   ? 0.3507 0.3591 0.1659 -0.1499 -0.0020 0.0036  3   LYS A O   
14   C CB  . LYS A 3   ? 0.4364 0.4501 0.2517 -0.1469 -0.0104 0.0008  3   LYS A CB  
15   C CG  . LYS A 3   ? 0.5128 0.5320 0.3235 -0.1486 -0.0136 -0.0011 3   LYS A CG  
16   C CD  . LYS A 3   ? 0.5326 0.5502 0.3422 -0.1467 -0.0224 0.0073  3   LYS A CD  
17   C CE  . LYS A 3   ? 0.6091 0.6334 0.4147 -0.1485 -0.0257 0.0047  3   LYS A CE  
18   N NZ  . LYS A 3   ? 0.6708 0.6965 0.4845 -0.1460 -0.0239 -0.0036 3   LYS A NZ  
19   N N   . LEU A 4   ? 0.3246 0.3243 0.1438 -0.1435 -0.0129 0.0147  4   LEU A N   
20   C CA  . LEU A 4   ? 0.3152 0.3104 0.1423 -0.1402 -0.0103 0.0139  4   LEU A CA  
21   C C   . LEU A 4   ? 0.3262 0.3219 0.1618 -0.1358 -0.0096 0.0090  4   LEU A C   
22   O O   . LEU A 4   ? 0.3554 0.3506 0.1925 -0.1335 -0.0148 0.0114  4   LEU A O   
23   C CB  . LEU A 4   ? 0.3278 0.3153 0.1556 -0.1375 -0.0153 0.0230  4   LEU A CB  
24   C CG  . LEU A 4   ? 0.3221 0.3048 0.1581 -0.1337 -0.0130 0.0226  4   LEU A CG  
25   C CD1 . LEU A 4   ? 0.3220 0.2983 0.1558 -0.1334 -0.0147 0.0296  4   LEU A CD1 
26   C CD2 . LEU A 4   ? 0.2927 0.2730 0.1369 -0.1281 -0.0163 0.0233  4   LEU A CD2 
27   N N   . PHE A 5   ? 0.2928 0.2902 0.1344 -0.1345 -0.0034 0.0022  5   PHE A N   
28   C CA  . PHE A 5   ? 0.3352 0.3327 0.1852 -0.1298 -0.0023 -0.0025 5   PHE A CA  
29   C C   . PHE A 5   ? 0.3504 0.3426 0.2066 -0.1257 -0.0039 0.0012  5   PHE A C   
30   O O   . PHE A 5   ? 0.3322 0.3236 0.1901 -0.1258 -0.0006 0.0010  5   PHE A O   
31   C CB  . PHE A 5   ? 0.2410 0.2436 0.0948 -0.1296 0.0053  -0.0122 5   PHE A CB  
32   C CG  . PHE A 5   ? 0.2945 0.3024 0.1430 -0.1332 0.0072  -0.0169 5   PHE A CG  
33   C CD1 . PHE A 5   ? 0.3185 0.3268 0.1649 -0.1331 0.0031  -0.0169 5   PHE A CD1 
34   C CD2 . PHE A 5   ? 0.3274 0.3404 0.1735 -0.1367 0.0131  -0.0219 5   PHE A CD2 
35   C CE1 . PHE A 5   ? 0.3115 0.3250 0.1527 -0.1367 0.0048  -0.0218 5   PHE A CE1 
36   C CE2 . PHE A 5   ? 0.2999 0.3180 0.1410 -0.1401 0.0150  -0.0267 5   PHE A CE2 
37   C CZ  . PHE A 5   ? 0.3311 0.3494 0.1694 -0.1402 0.0109  -0.0267 5   PHE A CZ  
38   N N   . LEU A 6   ? 0.2764 0.2656 0.1365 -0.1219 -0.0092 0.0042  6   LEU A N   
39   C CA  . LEU A 6   ? 0.2552 0.2397 0.1209 -0.1179 -0.0117 0.0081  6   LEU A CA  
40   C C   . LEU A 6   ? 0.2822 0.2679 0.1607 -0.1123 -0.0100 0.0023  6   LEU A C   
41   O O   . LEU A 6   ? 0.2622 0.2495 0.1432 -0.1112 -0.0116 -0.0007 6   LEU A O   
42   C CB  . LEU A 6   ? 0.2685 0.2490 0.1328 -0.1167 -0.0195 0.0170  6   LEU A CB  
43   C CG  . LEU A 6   ? 0.2567 0.2321 0.1316 -0.1106 -0.0217 0.0221  6   LEU A CG  
44   C CD1 . LEU A 6   ? 0.2874 0.2595 0.1623 -0.1112 -0.0175 0.0236  6   LEU A CD1 
45   C CD2 . LEU A 6   ? 0.2570 0.2297 0.1298 -0.1096 -0.0295 0.0304  6   LEU A CD2 
46   N N   . VAL A 7   ? 0.2268 0.2118 0.1145 -0.1082 -0.0064 0.0011  7   VAL A N   
47   C CA  . VAL A 7   ? 0.2279 0.2142 0.1277 -0.1025 -0.0041 -0.0038 7   VAL A CA  
48   C C   . VAL A 7   ? 0.2375 0.2211 0.1473 -0.0969 -0.0058 0.0006  7   VAL A C   
49   O O   . VAL A 7   ? 0.2542 0.2378 0.1657 -0.0963 -0.0032 0.0016  7   VAL A O   
50   C CB  . VAL A 7   ? 0.2570 0.2475 0.1586 -0.1026 0.0029  -0.0113 7   VAL A CB  
51   C CG1 . VAL A 7   ? 0.2469 0.2379 0.1604 -0.0965 0.0046  -0.0156 7   VAL A CG1 
52   C CG2 . VAL A 7   ? 0.3507 0.3445 0.2417 -0.1085 0.0055  -0.0160 7   VAL A CG2 
53   N N   . PHE A 8   ? 0.2216 0.2036 0.1380 -0.0931 -0.0100 0.0029  8   PHE A N   
54   C CA  . PHE A 8   ? 0.1932 0.1737 0.1200 -0.0874 -0.0109 0.0058  8   PHE A CA  
55   C C   . PHE A 8   ? 0.1731 0.1561 0.1092 -0.0830 -0.0071 0.0010  8   PHE A C   
56   O O   . PHE A 8   ? 0.2275 0.2112 0.1650 -0.0829 -0.0063 -0.0028 8   PHE A O   
57   C CB  . PHE A 8   ? 0.1954 0.1740 0.1257 -0.0853 -0.0169 0.0107  8   PHE A CB  
58   C CG  . PHE A 8   ? 0.1751 0.1508 0.0983 -0.0879 -0.0215 0.0170  8   PHE A CG  
59   C CD1 . PHE A 8   ? 0.2396 0.2116 0.1651 -0.0858 -0.0224 0.0217  8   PHE A CD1 
60   C CD2 . PHE A 8   ? 0.1953 0.1720 0.1095 -0.0923 -0.0249 0.0181  8   PHE A CD2 
61   C CE1 . PHE A 8   ? 0.2699 0.2380 0.1891 -0.0877 -0.0266 0.0281  8   PHE A CE1 
62   C CE2 . PHE A 8   ? 0.2812 0.2552 0.1884 -0.0943 -0.0294 0.0248  8   PHE A CE2 
63   C CZ  . PHE A 8   ? 0.2234 0.1925 0.1333 -0.0918 -0.0302 0.0301  8   PHE A CZ  
64   N N   . TRP A 9   ? 0.2128 0.1968 0.1552 -0.0793 -0.0048 0.0013  9   TRP A N   
65   C CA  . TRP A 9   ? 0.1951 0.1818 0.1462 -0.0744 -0.0016 -0.0020 9   TRP A CA  
66   C C   . TRP A 9   ? 0.1853 0.1721 0.1437 -0.0699 -0.0030 0.0015  9   TRP A C   
67   O O   . TRP A 9   ? 0.1653 0.1531 0.1237 -0.0699 -0.0018 0.0022  9   TRP A O   
68   C CB  . TRP A 9   ? 0.1883 0.1791 0.1383 -0.0751 0.0036  -0.0071 9   TRP A CB  
69   C CG  . TRP A 9   ? 0.1585 0.1520 0.1165 -0.0701 0.0069  -0.0108 9   TRP A CG  
70   C CD1 . TRP A 9   ? 0.1591 0.1512 0.1247 -0.0653 0.0059  -0.0095 9   TRP A CD1 
71   C CD2 . TRP A 9   ? 0.1808 0.1789 0.1400 -0.0694 0.0117  -0.0160 9   TRP A CD2 
72   N NE1 . TRP A 9   ? 0.1796 0.1743 0.1507 -0.0614 0.0096  -0.0131 9   TRP A NE1 
73   C CE2 . TRP A 9   ? 0.1451 0.1438 0.1128 -0.0635 0.0131  -0.0173 9   TRP A CE2 
74   C CE3 . TRP A 9   ? 0.2244 0.2265 0.1785 -0.0732 0.0151  -0.0196 9   TRP A CE3 
75   C CZ2 . TRP A 9   ? 0.1848 0.1877 0.1565 -0.0606 0.0174  -0.0219 9   TRP A CZ2 
76   C CZ3 . TRP A 9   ? 0.2160 0.2234 0.1746 -0.0705 0.0197  -0.0249 9   TRP A CZ3 
77   C CH2 . TRP A 9   ? 0.1909 0.1987 0.1585 -0.0639 0.0206  -0.0259 9   TRP A CH2 
78   N N   . TRP A 10  ? 0.1576 0.1434 0.1220 -0.0667 -0.0054 0.0034  10  TRP A N   
79   C CA  . TRP A 10  ? 0.1600 0.1462 0.1310 -0.0626 -0.0070 0.0067  10  TRP A CA  
80   C C   . TRP A 10  ? 0.1773 0.1672 0.1554 -0.0579 -0.0038 0.0048  10  TRP A C   
81   O O   . TRP A 10  ? 0.1445 0.1343 0.1259 -0.0562 -0.0029 0.0037  10  TRP A O   
82   C CB  . TRP A 10  ? 0.1454 0.1297 0.1190 -0.0620 -0.0112 0.0099  10  TRP A CB  
83   C CG  . TRP A 10  ? 0.1387 0.1202 0.1061 -0.0658 -0.0155 0.0129  10  TRP A CG  
84   C CD1 . TRP A 10  ? 0.1769 0.1578 0.1402 -0.0690 -0.0182 0.0129  10  TRP A CD1 
85   C CD2 . TRP A 10  ? 0.1573 0.1361 0.1218 -0.0665 -0.0176 0.0166  10  TRP A CD2 
86   N NE1 . TRP A 10  ? 0.1768 0.1557 0.1346 -0.0714 -0.0223 0.0169  10  TRP A NE1 
87   C CE2 . TRP A 10  ? 0.1782 0.1550 0.1367 -0.0698 -0.0219 0.0194  10  TRP A CE2 
88   C CE3 . TRP A 10  ? 0.1359 0.1136 0.1023 -0.0649 -0.0164 0.0176  10  TRP A CE3 
89   C CZ2 . TRP A 10  ? 0.1578 0.1308 0.1123 -0.0709 -0.0250 0.0241  10  TRP A CZ2 
90   C CZ3 . TRP A 10  ? 0.1799 0.1530 0.1427 -0.0664 -0.0190 0.0216  10  TRP A CZ3 
91   C CH2 . TRP A 10  ? 0.1535 0.1239 0.1103 -0.0691 -0.0233 0.0252  10  TRP A CH2 
92   N N   . HIS A 11  ? 0.1283 0.1214 0.1088 -0.0559 -0.0022 0.0046  11  HIS A N   
93   C CA  . HIS A 11  ? 0.1084 0.1064 0.0947 -0.0514 0.0007  0.0030  11  HIS A CA  
94   C C   . HIS A 11  ? 0.1403 0.1397 0.1327 -0.0474 -0.0007 0.0059  11  HIS A C   
95   O O   . HIS A 11  ? 0.1271 0.1265 0.1203 -0.0473 -0.0022 0.0074  11  HIS A O   
96   C CB  . HIS A 11  ? 0.1182 0.1209 0.1035 -0.0519 0.0032  0.0005  11  HIS A CB  
97   C CG  . HIS A 11  ? 0.1113 0.1206 0.1027 -0.0471 0.0049  -0.0001 11  HIS A CG  
98   N ND1 . HIS A 11  ? 0.1195 0.1316 0.1149 -0.0431 0.0066  -0.0008 11  HIS A ND1 
99   C CD2 . HIS A 11  ? 0.1221 0.1358 0.1161 -0.0456 0.0049  -0.0001 11  HIS A CD2 
100  C CE1 . HIS A 11  ? 0.1260 0.1447 0.1257 -0.0392 0.0073  -0.0006 11  HIS A CE1 
101  N NE2 . HIS A 11  ? 0.1253 0.1455 0.1242 -0.0409 0.0063  -0.0005 11  HIS A NE2 
102  N N   . MET A 12  ? 0.0976 0.0979 0.0945 -0.0441 0.0002  0.0065  12  MET A N   
103  C CA  . MET A 12  ? 0.1001 0.1020 0.1024 -0.0407 -0.0006 0.0094  12  MET A CA  
104  C C   . MET A 12  ? 0.1332 0.1407 0.1392 -0.0362 0.0019  0.0093  12  MET A C   
105  O O   . MET A 12  ? 0.1239 0.1313 0.1306 -0.0347 0.0039  0.0084  12  MET A O   
106  C CB  . MET A 12  ? 0.0981 0.0962 0.1026 -0.0412 -0.0018 0.0112  12  MET A CB  
107  C CG  . MET A 12  ? 0.0976 0.0913 0.0983 -0.0457 -0.0048 0.0112  12  MET A CG  
108  S SD  . MET A 12  ? 0.1399 0.1337 0.1398 -0.0465 -0.0082 0.0135  12  MET A SD  
109  C CE  . MET A 12  ? 0.1458 0.1358 0.1428 -0.0507 -0.0122 0.0146  12  MET A CE  
110  N N   . HIS A 13  ? 0.0884 0.1008 0.0969 -0.0339 0.0018  0.0103  13  HIS A N   
111  C CA  . HIS A 13  ? 0.0920 0.1112 0.1030 -0.0298 0.0037  0.0104  13  HIS A CA  
112  C C   . HIS A 13  ? 0.0939 0.1179 0.1076 -0.0277 0.0032  0.0119  13  HIS A C   
113  O O   . HIS A 13  ? 0.1061 0.1293 0.1193 -0.0295 0.0019  0.0111  13  HIS A O   
114  C CB  . HIS A 13  ? 0.1151 0.1391 0.1242 -0.0303 0.0050  0.0069  13  HIS A CB  
115  C CG  . HIS A 13  ? 0.1089 0.1421 0.1207 -0.0262 0.0062  0.0068  13  HIS A CG  
116  N ND1 . HIS A 13  ? 0.0917 0.1273 0.1062 -0.0217 0.0072  0.0093  13  HIS A ND1 
117  C CD2 . HIS A 13  ? 0.0896 0.1304 0.1015 -0.0261 0.0064  0.0045  13  HIS A CD2 
118  C CE1 . HIS A 13  ? 0.1235 0.1687 0.1395 -0.0186 0.0076  0.0090  13  HIS A CE1 
119  N NE2 . HIS A 13  ? 0.1044 0.1533 0.1189 -0.0215 0.0071  0.0057  13  HIS A NE2 
120  N N   . GLN A 14  ? 0.0809 0.1098 0.0971 -0.0238 0.0044  0.0142  14  GLN A N   
121  C CA  . GLN A 14  ? 0.0848 0.1211 0.1025 -0.0215 0.0047  0.0147  14  GLN A CA  
122  C C   . GLN A 14  ? 0.1170 0.1609 0.1352 -0.0176 0.0060  0.0156  14  GLN A C   
123  O O   . GLN A 14  ? 0.1145 0.1561 0.1336 -0.0154 0.0069  0.0182  14  GLN A O   
124  C CB  . GLN A 14  ? 0.0796 0.1150 0.1000 -0.0208 0.0045  0.0179  14  GLN A CB  
125  C CG  . GLN A 14  ? 0.0988 0.1284 0.1201 -0.0238 0.0027  0.0175  14  GLN A CG  
126  C CD  . GLN A 14  ? 0.1198 0.1509 0.1406 -0.0250 0.0018  0.0143  14  GLN A CD  
127  O OE1 . GLN A 14  ? 0.1024 0.1401 0.1231 -0.0235 0.0028  0.0123  14  GLN A OE1 
128  N NE2 . GLN A 14  ? 0.1268 0.1516 0.1472 -0.0276 -0.0002 0.0138  14  GLN A NE2 
129  N N   . PRO A 15  ? 0.1076 0.1605 0.1254 -0.0164 0.0062  0.0136  15  PRO A N   
130  C CA  . PRO A 15  ? 0.0797 0.1416 0.0980 -0.0121 0.0069  0.0153  15  PRO A CA  
131  C C   . PRO A 15  ? 0.0851 0.1481 0.1043 -0.0093 0.0074  0.0206  15  PRO A C   
132  O O   . PRO A 15  ? 0.1057 0.1643 0.1256 -0.0109 0.0075  0.0219  15  PRO A O   
133  C CB  . PRO A 15  ? 0.1007 0.1724 0.1181 -0.0129 0.0065  0.0109  15  PRO A CB  
134  C CG  . PRO A 15  ? 0.0861 0.1535 0.1033 -0.0163 0.0061  0.0088  15  PRO A CG  
135  C CD  . PRO A 15  ? 0.0731 0.1283 0.0903 -0.0189 0.0056  0.0099  15  PRO A CD  
136  N N   . LEU A 16  ? 0.0911 0.1604 0.1103 -0.0050 0.0079  0.0240  16  LEU A N   
137  C CA  . LEU A 16  ? 0.1188 0.1883 0.1382 -0.0024 0.0088  0.0301  16  LEU A CA  
138  C C   . LEU A 16  ? 0.1347 0.2130 0.1526 -0.0027 0.0090  0.0295  16  LEU A C   
139  O O   . LEU A 16  ? 0.1251 0.2146 0.1413 -0.0009 0.0085  0.0281  16  LEU A O   
140  C CB  . LEU A 16  ? 0.1041 0.1769 0.1237 0.0027  0.0091  0.0347  16  LEU A CB  
141  C CG  . LEU A 16  ? 0.1285 0.1993 0.1479 0.0051  0.0104  0.0422  16  LEU A CG  
142  C CD1 . LEU A 16  ? 0.1126 0.1704 0.1341 0.0018  0.0115  0.0436  16  LEU A CD1 
143  C CD2 . LEU A 16  ? 0.0968 0.1696 0.1166 0.0107  0.0104  0.0473  16  LEU A CD2 
144  N N   . TYR A 17  ? 0.1213 0.1956 0.1402 -0.0050 0.0097  0.0303  17  TYR A N   
145  C CA  . TYR A 17  ? 0.1027 0.1851 0.1208 -0.0052 0.0105  0.0293  17  TYR A CA  
146  C C   . TYR A 17  ? 0.1042 0.1920 0.1208 -0.0026 0.0120  0.0356  17  TYR A C   
147  O O   . TYR A 17  ? 0.1023 0.1983 0.1176 -0.0027 0.0131  0.0349  17  TYR A O   
148  C CB  . TYR A 17  ? 0.1224 0.1992 0.1433 -0.0085 0.0106  0.0268  17  TYR A CB  
149  C CG  . TYR A 17  ? 0.1345 0.2060 0.1561 -0.0112 0.0090  0.0213  17  TYR A CG  
150  C CD1 . TYR A 17  ? 0.1190 0.1962 0.1391 -0.0118 0.0085  0.0159  17  TYR A CD1 
151  C CD2 . TYR A 17  ? 0.1069 0.1678 0.1304 -0.0136 0.0080  0.0215  17  TYR A CD2 
152  C CE1 . TYR A 17  ? 0.1202 0.1917 0.1407 -0.0147 0.0074  0.0114  17  TYR A CE1 
153  C CE2 . TYR A 17  ? 0.1061 0.1622 0.1294 -0.0162 0.0065  0.0172  17  TYR A CE2 
154  C CZ  . TYR A 17  ? 0.1199 0.1807 0.1416 -0.0168 0.0063  0.0125  17  TYR A CZ  
155  O OH  . TYR A 17  ? 0.1070 0.1621 0.1281 -0.0197 0.0052  0.0090  17  TYR A OH  
156  N N   . ARG A 18  ? 0.1130 0.1962 0.1297 -0.0003 0.0125  0.0417  18  ARG A N   
157  C CA  . ARG A 18  ? 0.1094 0.1956 0.1244 0.0019  0.0142  0.0490  18  ARG A CA  
158  C C   . ARG A 18  ? 0.1679 0.2664 0.1788 0.0058  0.0134  0.0508  18  ARG A C   
159  O O   . ARG A 18  ? 0.1314 0.2302 0.1422 0.0091  0.0120  0.0521  18  ARG A O   
160  C CB  . ARG A 18  ? 0.1906 0.2651 0.2077 0.0026  0.0150  0.0547  18  ARG A CB  
161  C CG  . ARG A 18  ? 0.1742 0.2485 0.1900 0.0038  0.0173  0.0630  18  ARG A CG  
162  C CD  . ARG A 18  ? 0.2757 0.3371 0.2941 0.0047  0.0181  0.0678  18  ARG A CD  
163  N NE  . ARG A 18  ? 0.3078 0.3665 0.3253 0.0050  0.0206  0.0762  18  ARG A NE  
164  C CZ  . ARG A 18  ? 0.3219 0.3851 0.3358 0.0093  0.0210  0.0834  18  ARG A CZ  
165  N NH1 . ARG A 18  ? 0.2724 0.3444 0.2838 0.0139  0.0188  0.0827  18  ARG A NH1 
166  N NH2 . ARG A 18  ? 0.4186 0.4782 0.4316 0.0088  0.0237  0.0914  18  ARG A NH2 
167  N N   . GLU A 19  ? 0.1612 0.2706 0.1689 0.0057  0.0142  0.0506  19  GLU A N   
168  C CA  . GLU A 19  ? 0.1647 0.2878 0.1677 0.0090  0.0133  0.0522  19  GLU A CA  
169  C C   . GLU A 19  ? 0.1364 0.2579 0.1376 0.0131  0.0136  0.0624  19  GLU A C   
170  O O   . GLU A 19  ? 0.1714 0.2868 0.1726 0.0122  0.0160  0.0683  19  GLU A O   
171  C CB  . GLU A 19  ? 0.2135 0.3482 0.2131 0.0073  0.0146  0.0494  19  GLU A CB  
172  C CG  . GLU A 19  ? 0.3392 0.4899 0.3342 0.0090  0.0129  0.0464  19  GLU A CG  
173  C CD  . GLU A 19  ? 0.3684 0.5277 0.3582 0.0132  0.0125  0.0552  19  GLU A CD  
174  O OE1 . GLU A 19  ? 0.3231 0.4784 0.3114 0.0136  0.0147  0.0629  19  GLU A OE1 
175  O OE2 . GLU A 19  ? 0.3962 0.5666 0.3834 0.0160  0.0100  0.0547  19  GLU A OE2 
176  N N   . PRO A 20  ? 0.1640 0.2905 0.1640 0.0177  0.0114  0.0648  20  PRO A N   
177  C CA  . PRO A 20  ? 0.2474 0.3681 0.2473 0.0222  0.0116  0.0746  20  PRO A CA  
178  C C   . PRO A 20  ? 0.2918 0.4193 0.2861 0.0242  0.0127  0.0834  20  PRO A C   
179  O O   . PRO A 20  ? 0.3730 0.4916 0.3675 0.0263  0.0141  0.0923  20  PRO A O   
180  C CB  . PRO A 20  ? 0.2413 0.3677 0.2428 0.0269  0.0086  0.0732  20  PRO A CB  
181  C CG  . PRO A 20  ? 0.2203 0.3611 0.2199 0.0249  0.0068  0.0647  20  PRO A CG  
182  C CD  . PRO A 20  ? 0.1587 0.2940 0.1594 0.0186  0.0087  0.0580  20  PRO A CD  
183  N N   . TYR A 21  ? 0.2007 0.3434 0.1898 0.0233  0.0125  0.0813  21  TYR A N   
184  C CA  . TYR A 21  ? 0.2178 0.3670 0.2017 0.0246  0.0135  0.0884  21  TYR A CA  
185  C C   . TYR A 21  ? 0.2359 0.3787 0.2201 0.0200  0.0173  0.0894  21  TYR A C   
186  O O   . TYR A 21  ? 0.2768 0.4156 0.2597 0.0205  0.0187  0.0963  21  TYR A O   
187  C CB  . TYR A 21  ? 0.2218 0.3895 0.2015 0.0253  0.0113  0.0836  21  TYR A CB  
188  C CG  . TYR A 21  ? 0.2797 0.4553 0.2600 0.0302  0.0075  0.0835  21  TYR A CG  
189  C CD1 . TYR A 21  ? 0.3594 0.5363 0.3390 0.0353  0.0062  0.0913  21  TYR A CD1 
190  C CD2 . TYR A 21  ? 0.2145 0.3956 0.1963 0.0297  0.0053  0.0755  21  TYR A CD2 
191  C CE1 . TYR A 21  ? 0.3179 0.5023 0.2990 0.0401  0.0029  0.0910  21  TYR A CE1 
192  C CE2 . TYR A 21  ? 0.2446 0.4338 0.2283 0.0340  0.0019  0.0749  21  TYR A CE2 
193  C CZ  . TYR A 21  ? 0.3278 0.5188 0.3114 0.0394  0.0008  0.0826  21  TYR A CZ  
194  O OH  . TYR A 21  ? 0.2989 0.4980 0.2849 0.0438  -0.0023 0.0818  21  TYR A OH  
195  N N   . THR A 22  ? 0.1847 0.3265 0.1709 0.0153  0.0190  0.0825  22  THR A N   
196  C CA  . THR A 22  ? 0.2304 0.3680 0.2181 0.0110  0.0224  0.0825  22  THR A CA  
197  C C   . THR A 22  ? 0.2604 0.3823 0.2542 0.0084  0.0242  0.0841  22  THR A C   
198  O O   . THR A 22  ? 0.2517 0.3686 0.2476 0.0052  0.0268  0.0858  22  THR A O   
199  C CB  . THR A 22  ? 0.2054 0.3530 0.1927 0.0077  0.0233  0.0732  22  THR A CB  
200  O OG1 . THR A 22  ? 0.2207 0.3644 0.2127 0.0062  0.0221  0.0652  22  THR A OG1 
201  C CG2 . THR A 22  ? 0.2358 0.3991 0.2172 0.0094  0.0216  0.0704  22  THR A CG2 
202  N N   . GLY A 23  ? 0.2205 0.3335 0.2185 0.0094  0.0220  0.0810  23  GLY A N   
203  C CA  . GLY A 23  ? 0.2006 0.2987 0.2050 0.0064  0.0227  0.0797  23  GLY A CA  
204  C C   . GLY A 23  ? 0.2198 0.3176 0.2281 0.0020  0.0231  0.0714  23  GLY A C   
205  O O   . GLY A 23  ? 0.3030 0.3900 0.3164 -0.0009 0.0235  0.0703  23  GLY A O   
206  N N   . GLU A 24  ? 0.2022 0.3116 0.2086 0.0014  0.0228  0.0654  24  GLU A N   
207  C CA  . GLU A 24  ? 0.1855 0.2948 0.1961 -0.0021 0.0233  0.0580  24  GLU A CA  
208  C C   . GLU A 24  ? 0.1701 0.2738 0.1837 -0.0026 0.0204  0.0508  24  GLU A C   
209  O O   . GLU A 24  ? 0.1358 0.2439 0.1468 -0.0006 0.0183  0.0480  24  GLU A O   
210  C CB  . GLU A 24  ? 0.1787 0.3021 0.1863 -0.0025 0.0249  0.0542  24  GLU A CB  
211  C CG  . GLU A 24  ? 0.2766 0.4059 0.2814 -0.0032 0.0286  0.0607  24  GLU A CG  
212  C CD  . GLU A 24  ? 0.4091 0.5535 0.4095 -0.0032 0.0300  0.0566  24  GLU A CD  
213  O OE1 . GLU A 24  ? 0.4869 0.6378 0.4862 -0.0026 0.0284  0.0492  24  GLU A OE1 
214  O OE2 . GLU A 24  ? 0.5153 0.6630 0.5134 -0.0038 0.0320  0.0597  24  GLU A OE2 
215  N N   . TYR A 25  ? 0.1452 0.2400 0.1642 -0.0055 0.0202  0.0480  25  TYR A N   
216  C CA  . TYR A 25  ? 0.1333 0.2233 0.1545 -0.0066 0.0177  0.0413  25  TYR A CA  
217  C C   . TYR A 25  ? 0.1588 0.2571 0.1800 -0.0072 0.0179  0.0345  25  TYR A C   
218  O O   . TYR A 25  ? 0.1336 0.2340 0.1579 -0.0086 0.0195  0.0329  25  TYR A O   
219  C CB  . TYR A 25  ? 0.1312 0.2099 0.1575 -0.0094 0.0170  0.0410  25  TYR A CB  
220  C CG  . TYR A 25  ? 0.1358 0.2046 0.1621 -0.0092 0.0164  0.0449  25  TYR A CG  
221  C CD1 . TYR A 25  ? 0.1425 0.2089 0.1682 -0.0083 0.0183  0.0519  25  TYR A CD1 
222  C CD2 . TYR A 25  ? 0.1649 0.2269 0.1914 -0.0097 0.0141  0.0415  25  TYR A CD2 
223  C CE1 . TYR A 25  ? 0.2089 0.2653 0.2352 -0.0079 0.0180  0.0548  25  TYR A CE1 
224  C CE2 . TYR A 25  ? 0.1188 0.1722 0.1455 -0.0094 0.0139  0.0440  25  TYR A CE2 
225  C CZ  . TYR A 25  ? 0.1994 0.2498 0.2263 -0.0083 0.0158  0.0504  25  TYR A CZ  
226  O OH  . TYR A 25  ? 0.1922 0.2331 0.2198 -0.0078 0.0158  0.0521  25  TYR A OH  
227  N N   . LEU A 26  ? 0.1199 0.2234 0.1380 -0.0062 0.0165  0.0302  26  LEU A N   
228  C CA  . LEU A 26  ? 0.1519 0.2642 0.1694 -0.0067 0.0171  0.0236  26  LEU A CA  
229  C C   . LEU A 26  ? 0.1291 0.2347 0.1509 -0.0088 0.0161  0.0172  26  LEU A C   
230  O O   . LEU A 26  ? 0.1483 0.2588 0.1711 -0.0094 0.0171  0.0115  26  LEU A O   
231  C CB  . LEU A 26  ? 0.1022 0.2242 0.1148 -0.0052 0.0161  0.0214  26  LEU A CB  
232  C CG  . LEU A 26  ? 0.1644 0.2949 0.1721 -0.0024 0.0167  0.0282  26  LEU A CG  
233  C CD1 . LEU A 26  ? 0.1755 0.3179 0.1787 -0.0010 0.0152  0.0250  26  LEU A CD1 
234  C CD2 . LEU A 26  ? 0.1986 0.3348 0.2051 -0.0026 0.0197  0.0314  26  LEU A CD2 
235  N N   . LEU A 27  ? 0.1216 0.2159 0.1457 -0.0100 0.0142  0.0180  27  LEU A N   
236  C CA  . LEU A 27  ? 0.1357 0.2224 0.1637 -0.0119 0.0129  0.0138  27  LEU A CA  
237  C C   . LEU A 27  ? 0.1243 0.2018 0.1558 -0.0130 0.0121  0.0179  27  LEU A C   
238  O O   . LEU A 27  ? 0.1488 0.2232 0.1790 -0.0128 0.0120  0.0228  27  LEU A O   
239  C CB  . LEU A 27  ? 0.1315 0.2144 0.1576 -0.0132 0.0110  0.0096  27  LEU A CB  
240  C CG  . LEU A 27  ? 0.1620 0.2539 0.1855 -0.0131 0.0117  0.0040  27  LEU A CG  
241  C CD1 . LEU A 27  ? 0.1494 0.2383 0.1711 -0.0148 0.0101  0.0008  27  LEU A CD1 
242  C CD2 . LEU A 27  ? 0.2174 0.3115 0.2438 -0.0135 0.0130  -0.0013 27  LEU A CD2 
243  N N   . PRO A 28  ? 0.1282 0.2016 0.1644 -0.0141 0.0114  0.0159  28  PRO A N   
244  C CA  . PRO A 28  ? 0.1091 0.1756 0.1490 -0.0154 0.0102  0.0194  28  PRO A CA  
245  C C   . PRO A 28  ? 0.0977 0.1543 0.1369 -0.0173 0.0072  0.0189  28  PRO A C   
246  O O   . PRO A 28  ? 0.1171 0.1685 0.1595 -0.0187 0.0057  0.0206  28  PRO A O   
247  C CB  . PRO A 28  ? 0.1028 0.1724 0.1488 -0.0151 0.0109  0.0173  28  PRO A CB  
248  C CG  . PRO A 28  ? 0.1685 0.2389 0.2140 -0.0144 0.0105  0.0114  28  PRO A CG  
249  C CD  . PRO A 28  ? 0.1671 0.2426 0.2063 -0.0138 0.0116  0.0103  28  PRO A CD  
250  N N   . TRP A 29  ? 0.1054 0.1600 0.1404 -0.0176 0.0064  0.0165  29  TRP A N   
251  C CA  . TRP A 29  ? 0.1028 0.1486 0.1368 -0.0198 0.0038  0.0155  29  TRP A CA  
252  C C   . TRP A 29  ? 0.1375 0.1774 0.1707 -0.0212 0.0028  0.0190  29  TRP A C   
253  O O   . TRP A 29  ? 0.1268 0.1600 0.1602 -0.0233 0.0006  0.0190  29  TRP A O   
254  C CB  . TRP A 29  ? 0.1160 0.1618 0.1459 -0.0204 0.0037  0.0120  29  TRP A CB  
255  C CG  . TRP A 29  ? 0.1451 0.1952 0.1758 -0.0198 0.0045  0.0074  29  TRP A CG  
256  C CD1 . TRP A 29  ? 0.1543 0.2122 0.1828 -0.0190 0.0061  0.0043  29  TRP A CD1 
257  C CD2 . TRP A 29  ? 0.1752 0.2218 0.2095 -0.0200 0.0038  0.0048  29  TRP A CD2 
258  N NE1 . TRP A 29  ? 0.2201 0.2793 0.2503 -0.0193 0.0067  -0.0005 29  TRP A NE1 
259  C CE2 . TRP A 29  ? 0.1770 0.2286 0.2110 -0.0196 0.0054  -0.0002 29  TRP A CE2 
260  C CE3 . TRP A 29  ? 0.1859 0.2259 0.2239 -0.0204 0.0017  0.0062  29  TRP A CE3 
261  C CZ2 . TRP A 29  ? 0.2453 0.2942 0.2828 -0.0194 0.0055  -0.0041 29  TRP A CZ2 
262  C CZ3 . TRP A 29  ? 0.1695 0.2073 0.2111 -0.0196 0.0015  0.0031  29  TRP A CZ3 
263  C CH2 . TRP A 29  ? 0.2160 0.2576 0.2575 -0.0190 0.0035  -0.0021 29  TRP A CH2 
264  N N   . THR A 30  ? 0.1010 0.1428 0.1330 -0.0202 0.0045  0.0220  30  THR A N   
265  C CA  . THR A 30  ? 0.1122 0.1475 0.1442 -0.0217 0.0040  0.0246  30  THR A CA  
266  C C   . THR A 30  ? 0.1461 0.1797 0.1829 -0.0234 0.0032  0.0263  30  THR A C   
267  O O   . THR A 30  ? 0.1334 0.1611 0.1706 -0.0260 0.0012  0.0263  30  THR A O   
268  C CB  . THR A 30  ? 0.1069 0.1435 0.1374 -0.0198 0.0061  0.0278  30  THR A CB  
269  O OG1 . THR A 30  ? 0.1358 0.1748 0.1628 -0.0182 0.0063  0.0259  30  THR A OG1 
270  C CG2 . THR A 30  ? 0.1576 0.1863 0.1888 -0.0216 0.0060  0.0299  30  THR A CG2 
271  N N   . PHE A 31  ? 0.0872 0.1271 0.1277 -0.0222 0.0049  0.0276  31  PHE A N   
272  C CA  . PHE A 31  ? 0.1126 0.1528 0.1588 -0.0238 0.0043  0.0288  31  PHE A CA  
273  C C   . PHE A 31  ? 0.1113 0.1488 0.1596 -0.0249 0.0009  0.0262  31  PHE A C   
274  O O   . PHE A 31  ? 0.1018 0.1355 0.1520 -0.0273 -0.0014 0.0269  31  PHE A O   
275  C CB  . PHE A 31  ? 0.0944 0.1432 0.1442 -0.0223 0.0070  0.0298  31  PHE A CB  
276  C CG  . PHE A 31  ? 0.1179 0.1691 0.1748 -0.0239 0.0066  0.0303  31  PHE A CG  
277  C CD1 . PHE A 31  ? 0.1255 0.1753 0.1851 -0.0265 0.0076  0.0336  31  PHE A CD1 
278  C CD2 . PHE A 31  ? 0.1295 0.1844 0.1911 -0.0227 0.0053  0.0274  31  PHE A CD2 
279  C CE1 . PHE A 31  ? 0.1432 0.1968 0.2102 -0.0283 0.0072  0.0338  31  PHE A CE1 
280  C CE2 . PHE A 31  ? 0.1629 0.2215 0.2322 -0.0237 0.0047  0.0278  31  PHE A CE2 
281  C CZ  . PHE A 31  ? 0.1553 0.2141 0.2274 -0.0267 0.0056  0.0309  31  PHE A CZ  
282  N N   . PHE A 32  ? 0.0901 0.1290 0.1376 -0.0232 0.0003  0.0232  32  PHE A N   
283  C CA  . PHE A 32  ? 0.0931 0.1290 0.1432 -0.0235 -0.0029 0.0217  32  PHE A CA  
284  C C   . PHE A 32  ? 0.1032 0.1309 0.1487 -0.0261 -0.0059 0.0220  32  PHE A C   
285  O O   . PHE A 32  ? 0.1238 0.1488 0.1713 -0.0275 -0.0091 0.0228  32  PHE A O   
286  C CB  . PHE A 32  ? 0.1012 0.1391 0.1519 -0.0212 -0.0024 0.0183  32  PHE A CB  
287  C CG  . PHE A 32  ? 0.0924 0.1384 0.1491 -0.0189 -0.0001 0.0172  32  PHE A CG  
288  C CD1 . PHE A 32  ? 0.1062 0.1552 0.1700 -0.0187 -0.0009 0.0186  32  PHE A CD1 
289  C CD2 . PHE A 32  ? 0.1376 0.1892 0.1929 -0.0170 0.0029  0.0144  32  PHE A CD2 
290  C CE1 . PHE A 32  ? 0.1779 0.2354 0.2478 -0.0166 0.0017  0.0172  32  PHE A CE1 
291  C CE2 . PHE A 32  ? 0.1711 0.2309 0.2316 -0.0151 0.0054  0.0129  32  PHE A CE2 
292  C CZ  . PHE A 32  ? 0.1490 0.2116 0.2169 -0.0148 0.0050  0.0143  32  PHE A CZ  
293  N N   . HIS A 33  ? 0.0939 0.1186 0.1332 -0.0269 -0.0050 0.0212  33  HIS A N   
294  C CA  . HIS A 33  ? 0.1039 0.1217 0.1385 -0.0298 -0.0073 0.0212  33  HIS A CA  
295  C C   . HIS A 33  ? 0.0972 0.1128 0.1322 -0.0321 -0.0078 0.0230  33  HIS A C   
296  O O   . HIS A 33  ? 0.1248 0.1358 0.1571 -0.0349 -0.0105 0.0229  33  HIS A O   
297  C CB  . HIS A 33  ? 0.0960 0.1121 0.1247 -0.0301 -0.0059 0.0192  33  HIS A CB  
298  C CG  . HIS A 33  ? 0.0929 0.1089 0.1207 -0.0295 -0.0062 0.0169  33  HIS A CG  
299  N ND1 . HIS A 33  ? 0.0913 0.1018 0.1180 -0.0310 -0.0089 0.0169  33  HIS A ND1 
300  C CD2 . HIS A 33  ? 0.1143 0.1347 0.1422 -0.0277 -0.0041 0.0145  33  HIS A CD2 
301  C CE1 . HIS A 33  ? 0.0831 0.0934 0.1097 -0.0303 -0.0082 0.0145  33  HIS A CE1 
302  N NE2 . HIS A 33  ? 0.1011 0.1178 0.1285 -0.0285 -0.0053 0.0126  33  HIS A NE2 
303  N N   . ALA A 34  ? 0.1074 0.1259 0.1452 -0.0313 -0.0054 0.0246  34  ALA A N   
304  C CA  . ALA A 34  ? 0.1442 0.1600 0.1833 -0.0340 -0.0056 0.0259  34  ALA A CA  
305  C C   . ALA A 34  ? 0.1496 0.1671 0.1938 -0.0358 -0.0087 0.0264  34  ALA A C   
306  O O   . ALA A 34  ? 0.1291 0.1432 0.1722 -0.0391 -0.0112 0.0260  34  ALA A O   
307  C CB  . ALA A 34  ? 0.1323 0.1500 0.1735 -0.0329 -0.0020 0.0281  34  ALA A CB  
308  N N   . VAL A 35  ? 0.1274 0.1509 0.1773 -0.0337 -0.0086 0.0269  35  VAL A N   
309  C CA  . VAL A 35  ? 0.1421 0.1688 0.1983 -0.0348 -0.0116 0.0274  35  VAL A CA  
310  C C   . VAL A 35  ? 0.1177 0.1416 0.1720 -0.0348 -0.0161 0.0268  35  VAL A C   
311  O O   . VAL A 35  ? 0.1221 0.1474 0.1796 -0.0365 -0.0197 0.0275  35  VAL A O   
312  C CB  . VAL A 35  ? 0.1114 0.1464 0.1754 -0.0323 -0.0097 0.0279  35  VAL A CB  
313  C CG1 . VAL A 35  ? 0.1224 0.1601 0.1872 -0.0327 -0.0051 0.0294  35  VAL A CG1 
314  C CG2 . VAL A 35  ? 0.1189 0.1558 0.1829 -0.0284 -0.0093 0.0262  35  VAL A CG2 
315  N N   . LYS A 36  ? 0.0810 0.1011 0.1301 -0.0333 -0.0161 0.0257  36  LYS A N   
316  C CA  . LYS A 36  ? 0.1368 0.1531 0.1836 -0.0334 -0.0200 0.0259  36  LYS A CA  
317  C C   . LYS A 36  ? 0.1526 0.1626 0.1910 -0.0371 -0.0218 0.0259  36  LYS A C   
318  O O   . LYS A 36  ? 0.1551 0.1633 0.1920 -0.0388 -0.0261 0.0272  36  LYS A O   
319  C CB  . LYS A 36  ? 0.0796 0.0947 0.1257 -0.0303 -0.0188 0.0246  36  LYS A CB  
320  C CG  . LYS A 36  ? 0.1030 0.1139 0.1490 -0.0295 -0.0227 0.0256  36  LYS A CG  
321  C CD  . LYS A 36  ? 0.1321 0.1414 0.1792 -0.0265 -0.0209 0.0236  36  LYS A CD  
322  C CE  . LYS A 36  ? 0.1280 0.1327 0.1672 -0.0284 -0.0187 0.0219  36  LYS A CE  
323  N NZ  . LYS A 36  ? 0.1397 0.1369 0.1714 -0.0317 -0.0214 0.0236  36  LYS A NZ  
324  N N   . ASP A 37  ? 0.1179 0.1253 0.1509 -0.0382 -0.0188 0.0245  37  ASP A N   
325  C CA  . ASP A 37  ? 0.1237 0.1256 0.1483 -0.0413 -0.0195 0.0236  37  ASP A CA  
326  C C   . ASP A 37  ? 0.1199 0.1203 0.1417 -0.0439 -0.0177 0.0223  37  ASP A C   
327  O O   . ASP A 37  ? 0.1444 0.1416 0.1611 -0.0474 -0.0195 0.0216  37  ASP A O   
328  C CB  . ASP A 37  ? 0.1253 0.1253 0.1458 -0.0400 -0.0172 0.0222  37  ASP A CB  
329  C CG  . ASP A 37  ? 0.1380 0.1382 0.1614 -0.0375 -0.0183 0.0227  37  ASP A CG  
330  O OD1 . ASP A 37  ? 0.1368 0.1342 0.1599 -0.0380 -0.0219 0.0245  37  ASP A OD1 
331  O OD2 . ASP A 37  ? 0.1283 0.1319 0.1548 -0.0347 -0.0155 0.0214  37  ASP A OD2 
332  N N   . TYR A 38  ? 0.1129 0.1150 0.1376 -0.0422 -0.0140 0.0220  38  TYR A N   
333  C CA  . TYR A 38  ? 0.1441 0.1430 0.1657 -0.0440 -0.0118 0.0205  38  TYR A CA  
334  C C   . TYR A 38  ? 0.1397 0.1369 0.1623 -0.0477 -0.0134 0.0201  38  TYR A C   
335  O O   . TYR A 38  ? 0.1502 0.1434 0.1685 -0.0504 -0.0128 0.0177  38  TYR A O   
336  C CB  . TYR A 38  ? 0.1140 0.1145 0.1381 -0.0408 -0.0077 0.0210  38  TYR A CB  
337  C CG  . TYR A 38  ? 0.1104 0.1134 0.1325 -0.0378 -0.0061 0.0204  38  TYR A CG  
338  C CD1 . TYR A 38  ? 0.1269 0.1280 0.1435 -0.0390 -0.0069 0.0184  38  TYR A CD1 
339  C CD2 . TYR A 38  ? 0.0872 0.0949 0.1124 -0.0342 -0.0037 0.0218  38  TYR A CD2 
340  C CE1 . TYR A 38  ? 0.1111 0.1152 0.1265 -0.0369 -0.0053 0.0173  38  TYR A CE1 
341  C CE2 . TYR A 38  ? 0.1352 0.1463 0.1585 -0.0319 -0.0025 0.0206  38  TYR A CE2 
342  C CZ  . TYR A 38  ? 0.1092 0.1185 0.1280 -0.0334 -0.0033 0.0181  38  TYR A CZ  
343  O OH  . TYR A 38  ? 0.1235 0.1367 0.1409 -0.0318 -0.0020 0.0164  38  TYR A OH  
344  N N   . TYR A 39  ? 0.0950 0.0958 0.1238 -0.0481 -0.0152 0.0217  39  TYR A N   
345  C CA  . TYR A 39  ? 0.1022 0.1026 0.1321 -0.0525 -0.0175 0.0208  39  TYR A CA  
346  C C   . TYR A 39  ? 0.1441 0.1449 0.1699 -0.0548 -0.0225 0.0206  39  TYR A C   
347  O O   . TYR A 39  ? 0.1486 0.1473 0.1699 -0.0589 -0.0241 0.0185  39  TYR A O   
348  C CB  . TYR A 39  ? 0.0938 0.0992 0.1326 -0.0525 -0.0175 0.0225  39  TYR A CB  
349  C CG  . TYR A 39  ? 0.1469 0.1535 0.1875 -0.0569 -0.0202 0.0210  39  TYR A CG  
350  C CD1 . TYR A 39  ? 0.1684 0.1708 0.2079 -0.0595 -0.0177 0.0182  39  TYR A CD1 
351  C CD2 . TYR A 39  ? 0.1341 0.1465 0.1777 -0.0578 -0.0253 0.0219  39  TYR A CD2 
352  C CE1 . TYR A 39  ? 0.1728 0.1769 0.2138 -0.0633 -0.0197 0.0158  39  TYR A CE1 
353  C CE2 . TYR A 39  ? 0.1530 0.1680 0.1978 -0.0613 -0.0279 0.0201  39  TYR A CE2 
354  C CZ  . TYR A 39  ? 0.1607 0.1716 0.2039 -0.0642 -0.0249 0.0167  39  TYR A CZ  
355  O OH  . TYR A 39  ? 0.2195 0.2334 0.2642 -0.0681 -0.0272 0.0142  39  TYR A OH  
356  N N   . ASP A 40  ? 0.1503 0.1538 0.1775 -0.0521 -0.0250 0.0228  40  ASP A N   
357  C CA  . ASP A 40  ? 0.1533 0.1578 0.1781 -0.0537 -0.0304 0.0241  40  ASP A CA  
358  C C   . ASP A 40  ? 0.1536 0.1529 0.1679 -0.0561 -0.0312 0.0232  40  ASP A C   
359  O O   . ASP A 40  ? 0.1379 0.1375 0.1478 -0.0594 -0.0352 0.0235  40  ASP A O   
360  C CB  . ASP A 40  ? 0.1607 0.1686 0.1912 -0.0494 -0.0325 0.0268  40  ASP A CB  
361  C CG  . ASP A 40  ? 0.1408 0.1560 0.1817 -0.0486 -0.0337 0.0276  40  ASP A CG  
362  O OD1 . ASP A 40  ? 0.1586 0.1773 0.2011 -0.0513 -0.0378 0.0280  40  ASP A OD1 
363  O OD2 . ASP A 40  ? 0.1640 0.1822 0.2112 -0.0458 -0.0302 0.0276  40  ASP A OD2 
364  N N   . MET A 41  ? 0.1506 0.1462 0.1605 -0.0549 -0.0274 0.0220  41  MET A N   
365  C CA  . MET A 41  ? 0.1335 0.1251 0.1337 -0.0577 -0.0277 0.0210  41  MET A CA  
366  C C   . MET A 41  ? 0.1607 0.1512 0.1558 -0.0624 -0.0277 0.0179  41  MET A C   
367  O O   . MET A 41  ? 0.1736 0.1637 0.1619 -0.0659 -0.0311 0.0182  41  MET A O   
368  C CB  . MET A 41  ? 0.1445 0.1338 0.1422 -0.0557 -0.0235 0.0198  41  MET A CB  
369  C CG  . MET A 41  ? 0.1561 0.1452 0.1556 -0.0526 -0.0241 0.0222  41  MET A CG  
370  S SD  . MET A 41  ? 0.1572 0.1424 0.1495 -0.0551 -0.0287 0.0253  41  MET A SD  
371  C CE  . MET A 41  ? 0.1258 0.1077 0.1084 -0.0585 -0.0249 0.0226  41  MET A CE  
372  N N   . PRO A 42  ? 0.1599 0.1497 0.1578 -0.0628 -0.0241 0.0149  42  PRO A N   
373  C CA  . PRO A 42  ? 0.1350 0.1236 0.1289 -0.0665 -0.0240 0.0110  42  PRO A CA  
374  C C   . PRO A 42  ? 0.1686 0.1610 0.1649 -0.0688 -0.0283 0.0116  42  PRO A C   
375  O O   . PRO A 42  ? 0.1828 0.1753 0.1735 -0.0726 -0.0298 0.0089  42  PRO A O   
376  C CB  . PRO A 42  ? 0.1591 0.1451 0.1573 -0.0652 -0.0189 0.0083  42  PRO A CB  
377  C CG  . PRO A 42  ? 0.1569 0.1445 0.1626 -0.0612 -0.0176 0.0118  42  PRO A CG  
378  C CD  . PRO A 42  ? 0.1321 0.1214 0.1355 -0.0591 -0.0195 0.0145  42  PRO A CD  
379  N N   . ALA A 43  ? 0.1397 0.1361 0.1443 -0.0668 -0.0304 0.0147  43  ALA A N   
380  C CA  . ALA A 43  ? 0.1688 0.1702 0.1770 -0.0690 -0.0345 0.0149  43  ALA A CA  
381  C C   . ALA A 43  ? 0.2149 0.2191 0.2172 -0.0713 -0.0408 0.0171  43  ALA A C   
382  O O   . ALA A 43  ? 0.1915 0.2004 0.1945 -0.0738 -0.0445 0.0165  43  ALA A O   
383  C CB  . ALA A 43  ? 0.1345 0.1407 0.1540 -0.0662 -0.0348 0.0175  43  ALA A CB  
384  N N   . TYR A 44  ? 0.1362 0.1374 0.1323 -0.0709 -0.0420 0.0198  44  TYR A N   
385  C CA  . TYR A 44  ? 0.1650 0.1676 0.1534 -0.0733 -0.0475 0.0223  44  TYR A CA  
386  C C   . TYR A 44  ? 0.1709 0.1740 0.1510 -0.0783 -0.0476 0.0182  44  TYR A C   
387  O O   . TYR A 44  ? 0.2002 0.2072 0.1757 -0.0809 -0.0529 0.0198  44  TYR A O   
388  C CB  . TYR A 44  ? 0.1671 0.1645 0.1486 -0.0714 -0.0467 0.0251  44  TYR A CB  
389  C CG  . TYR A 44  ? 0.1553 0.1524 0.1430 -0.0660 -0.0481 0.0299  44  TYR A CG  
390  C CD1 . TYR A 44  ? 0.1730 0.1719 0.1606 -0.0647 -0.0542 0.0349  44  TYR A CD1 
391  C CD2 . TYR A 44  ? 0.1364 0.1315 0.1301 -0.0618 -0.0435 0.0291  44  TYR A CD2 
392  C CE1 . TYR A 44  ? 0.1804 0.1781 0.1744 -0.0593 -0.0552 0.0387  44  TYR A CE1 
393  C CE2 . TYR A 44  ? 0.1515 0.1463 0.1509 -0.0570 -0.0444 0.0324  44  TYR A CE2 
394  C CZ  . TYR A 44  ? 0.1808 0.1762 0.1806 -0.0557 -0.0500 0.0369  44  TYR A CZ  
395  O OH  . TYR A 44  ? 0.2012 0.1952 0.2073 -0.0505 -0.0503 0.0395  44  TYR A OH  
396  N N   . LEU A 45  ? 0.1889 0.1883 0.1672 -0.0790 -0.0416 0.0128  45  LEU A N   
397  C CA  . LEU A 45  ? 0.2320 0.2313 0.2028 -0.0832 -0.0406 0.0079  45  LEU A CA  
398  C C   . LEU A 45  ? 0.2448 0.2492 0.2201 -0.0853 -0.0430 0.0056  45  LEU A C   
399  O O   . LEU A 45  ? 0.2341 0.2400 0.2031 -0.0892 -0.0436 0.0018  45  LEU A O   
400  C CB  . LEU A 45  ? 0.2192 0.2131 0.1893 -0.0828 -0.0336 0.0027  45  LEU A CB  
401  C CG  . LEU A 45  ? 0.1663 0.1564 0.1303 -0.0818 -0.0307 0.0034  45  LEU A CG  
402  C CD1 . LEU A 45  ? 0.1802 0.1662 0.1474 -0.0799 -0.0242 -0.0010 45  LEU A CD1 
403  C CD2 . LEU A 45  ? 0.1865 0.1771 0.1380 -0.0863 -0.0321 0.0027  45  LEU A CD2 
404  N N   . LYS A 46  ? 0.1814 0.1891 0.1677 -0.0830 -0.0442 0.0073  46  LYS A N   
405  C CA  . LYS A 46  ? 0.2286 0.2426 0.2198 -0.0852 -0.0471 0.0056  46  LYS A CA  
406  C C   . LYS A 46  ? 0.2672 0.2880 0.2541 -0.0868 -0.0544 0.0090  46  LYS A C   
407  O O   . LYS A 46  ? 0.2491 0.2754 0.2354 -0.0899 -0.0570 0.0064  46  LYS A O   
408  C CB  . LYS A 46  ? 0.2139 0.2309 0.2182 -0.0824 -0.0464 0.0072  46  LYS A CB  
409  C CG  . LYS A 46  ? 0.2825 0.2938 0.2921 -0.0813 -0.0396 0.0041  46  LYS A CG  
410  C CD  . LYS A 46  ? 0.4532 0.4688 0.4749 -0.0792 -0.0392 0.0062  46  LYS A CD  
411  C CE  . LYS A 46  ? 0.5998 0.6097 0.6266 -0.0785 -0.0327 0.0040  46  LYS A CE  
412  N NZ  . LYS A 46  ? 0.7079 0.7151 0.7346 -0.0826 -0.0306 -0.0016 46  LYS A NZ  
413  N N   . ASP A 47  ? 0.2479 0.2684 0.2319 -0.0845 -0.0578 0.0150  47  ASP A N   
414  C CA  . ASP A 47  ? 0.2394 0.2660 0.2208 -0.0847 -0.0652 0.0198  47  ASP A CA  
415  C C   . ASP A 47  ? 0.2521 0.2762 0.2193 -0.0874 -0.0670 0.0216  47  ASP A C   
416  O O   . ASP A 47  ? 0.2719 0.3012 0.2350 -0.0882 -0.0728 0.0250  47  ASP A O   
417  C CB  . ASP A 47  ? 0.2526 0.2811 0.2425 -0.0797 -0.0688 0.0263  47  ASP A CB  
418  C CG  . ASP A 47  ? 0.3221 0.3553 0.3262 -0.0771 -0.0674 0.0250  47  ASP A CG  
419  O OD1 . ASP A 47  ? 0.3226 0.3605 0.3301 -0.0797 -0.0667 0.0207  47  ASP A OD1 
420  O OD2 . ASP A 47  ? 0.3520 0.3845 0.3640 -0.0730 -0.0668 0.0280  47  ASP A OD2 
421  N N   . PHE A 48  ? 0.2280 0.2446 0.1875 -0.0886 -0.0621 0.0197  48  PHE A N   
422  C CA  . PHE A 48  ? 0.2462 0.2603 0.1921 -0.0914 -0.0632 0.0219  48  PHE A CA  
423  C C   . PHE A 48  ? 0.2133 0.2247 0.1514 -0.0952 -0.0573 0.0149  48  PHE A C   
424  O O   . PHE A 48  ? 0.2664 0.2734 0.2083 -0.0941 -0.0512 0.0104  48  PHE A O   
425  C CB  . PHE A 48  ? 0.2409 0.2491 0.1851 -0.0890 -0.0634 0.0273  48  PHE A CB  
426  C CG  . PHE A 48  ? 0.2454 0.2559 0.1974 -0.0847 -0.0695 0.0342  48  PHE A CG  
427  C CD1 . PHE A 48  ? 0.2620 0.2756 0.2097 -0.0841 -0.0760 0.0403  48  PHE A CD1 
428  C CD2 . PHE A 48  ? 0.2662 0.2756 0.2307 -0.0794 -0.0671 0.0345  48  PHE A CD2 
429  C CE1 . PHE A 48  ? 0.3200 0.3357 0.2761 -0.0788 -0.0813 0.0465  48  PHE A CE1 
430  C CE2 . PHE A 48  ? 0.2310 0.2425 0.2040 -0.0740 -0.0711 0.0399  48  PHE A CE2 
431  C CZ  . PHE A 48  ? 0.3036 0.3181 0.2728 -0.0735 -0.0783 0.0460  48  PHE A CZ  
432  N N   . GLU A 49  ? 0.2325 0.2469 0.1601 -0.0993 -0.0589 0.0141  49  GLU A N   
433  C CA  . GLU A 49  ? 0.2558 0.2689 0.1760 -0.1032 -0.0536 0.0069  49  GLU A CA  
434  C C   . GLU A 49  ? 0.2776 0.2853 0.1887 -0.1043 -0.0496 0.0078  49  GLU A C   
435  O O   . GLU A 49  ? 0.3020 0.3108 0.2018 -0.1079 -0.0499 0.0088  49  GLU A O   
436  C CB  . GLU A 49  ? 0.3393 0.3592 0.2531 -0.1072 -0.0568 0.0050  49  GLU A CB  
437  C CG  . GLU A 49  ? 0.4655 0.4906 0.3887 -0.1072 -0.0587 0.0012  49  GLU A CG  
438  C CD  . GLU A 49  ? 0.6256 0.6468 0.5542 -0.1078 -0.0522 -0.0074 49  GLU A CD  
439  O OE1 . GLU A 49  ? 0.6721 0.6902 0.5939 -0.1102 -0.0472 -0.0126 49  GLU A OE1 
440  O OE2 . GLU A 49  ? 0.6682 0.6894 0.6084 -0.1056 -0.0518 -0.0088 49  GLU A OE2 
441  N N   . ILE A 50  ? 0.2416 0.2439 0.1583 -0.1011 -0.0456 0.0073  50  ILE A N   
442  C CA  . ILE A 50  ? 0.2286 0.2263 0.1392 -0.1018 -0.0409 0.0068  50  ILE A CA  
443  C C   . ILE A 50  ? 0.2299 0.2243 0.1477 -0.0992 -0.0342 0.0005  50  ILE A C   
444  O O   . ILE A 50  ? 0.2470 0.2416 0.1741 -0.0970 -0.0334 -0.0024 50  ILE A O   
445  C CB  . ILE A 50  ? 0.2565 0.2510 0.1665 -0.1001 -0.0438 0.0143  50  ILE A CB  
446  C CG1 . ILE A 50  ? 0.2752 0.2686 0.1985 -0.0949 -0.0454 0.0165  50  ILE A CG1 
447  C CG2 . ILE A 50  ? 0.2946 0.2911 0.1962 -0.1022 -0.0503 0.0213  50  ILE A CG2 
448  C CD1 . ILE A 50  ? 0.2723 0.2616 0.1971 -0.0918 -0.0462 0.0226  50  ILE A CD1 
449  N N   . LYS A 51  ? 0.2286 0.2202 0.1422 -0.0996 -0.0292 -0.0013 51  LYS A N   
450  C CA  . LYS A 51  ? 0.2178 0.2065 0.1383 -0.0964 -0.0230 -0.0062 51  LYS A CA  
451  C C   . LYS A 51  ? 0.2276 0.2137 0.1527 -0.0929 -0.0226 -0.0018 51  LYS A C   
452  O O   . LYS A 51  ? 0.2443 0.2298 0.1632 -0.0947 -0.0241 0.0024  51  LYS A O   
453  C CB  . LYS A 51  ? 0.2131 0.2019 0.1269 -0.0992 -0.0172 -0.0124 51  LYS A CB  
454  C CG  . LYS A 51  ? 0.2586 0.2504 0.1664 -0.1033 -0.0170 -0.0173 51  LYS A CG  
455  C CD  . LYS A 51  ? 0.2796 0.2707 0.1958 -0.1017 -0.0174 -0.0212 51  LYS A CD  
456  C CE  . LYS A 51  ? 0.3925 0.3858 0.3036 -0.1056 -0.0153 -0.0282 51  LYS A CE  
457  N NZ  . LYS A 51  ? 0.4371 0.4355 0.3380 -0.1101 -0.0195 -0.0252 51  LYS A NZ  
458  N N   . LEU A 52  ? 0.1753 0.1599 0.1114 -0.0881 -0.0203 -0.0028 52  LEU A N   
459  C CA  . LEU A 52  ? 0.1674 0.1504 0.1091 -0.0842 -0.0188 0.0002  52  LEU A CA  
460  C C   . LEU A 52  ? 0.2317 0.2136 0.1804 -0.0809 -0.0134 -0.0043 52  LEU A C   
461  O O   . LEU A 52  ? 0.2087 0.1897 0.1626 -0.0800 -0.0125 -0.0070 52  LEU A O   
462  C CB  . LEU A 52  ? 0.1772 0.1604 0.1264 -0.0809 -0.0232 0.0057  52  LEU A CB  
463  C CG  . LEU A 52  ? 0.2002 0.1844 0.1449 -0.0835 -0.0297 0.0112  52  LEU A CG  
464  C CD1 . LEU A 52  ? 0.1910 0.1763 0.1459 -0.0792 -0.0328 0.0150  52  LEU A CD1 
465  C CD2 . LEU A 52  ? 0.2036 0.1854 0.1410 -0.0844 -0.0295 0.0146  52  LEU A CD2 
466  N N   . ASN A 53  ? 0.1968 0.1787 0.1460 -0.0794 -0.0099 -0.0046 53  ASN A N   
467  C CA  . ASN A 53  ? 0.2082 0.1899 0.1639 -0.0758 -0.0050 -0.0083 53  ASN A CA  
468  C C   . ASN A 53  ? 0.1813 0.1638 0.1450 -0.0702 -0.0047 -0.0045 53  ASN A C   
469  O O   . ASN A 53  ? 0.1490 0.1321 0.1121 -0.0698 -0.0071 -0.0003 53  ASN A O   
470  C CB  . ASN A 53  ? 0.1719 0.1553 0.1226 -0.0774 -0.0004 -0.0129 53  ASN A CB  
471  C CG  . ASN A 53  ? 0.1987 0.1823 0.1401 -0.0834 -0.0004 -0.0168 53  ASN A CG  
472  O OD1 . ASN A 53  ? 0.2075 0.1896 0.1496 -0.0846 0.0005  -0.0213 53  ASN A OD1 
473  N ND2 . ASN A 53  ? 0.2136 0.1987 0.1457 -0.0877 -0.0017 -0.0149 53  ASN A ND2 
474  N N   . PHE A 54  ? 0.1268 0.1092 0.0979 -0.0660 -0.0017 -0.0061 54  PHE A N   
475  C CA  . PHE A 54  ? 0.1404 0.1243 0.1188 -0.0608 -0.0015 -0.0026 54  PHE A CA  
476  C C   . PHE A 54  ? 0.1580 0.1437 0.1406 -0.0566 0.0029  -0.0050 54  PHE A C   
477  O O   . PHE A 54  ? 0.1889 0.1727 0.1722 -0.0564 0.0057  -0.0088 54  PHE A O   
478  C CB  . PHE A 54  ? 0.1751 0.1574 0.1595 -0.0593 -0.0038 0.0002  54  PHE A CB  
479  C CG  . PHE A 54  ? 0.1707 0.1528 0.1527 -0.0626 -0.0086 0.0027  54  PHE A CG  
480  C CD1 . PHE A 54  ? 0.1566 0.1405 0.1399 -0.0612 -0.0114 0.0069  54  PHE A CD1 
481  C CD2 . PHE A 54  ? 0.1537 0.1343 0.1318 -0.0672 -0.0104 0.0004  54  PHE A CD2 
482  C CE1 . PHE A 54  ? 0.1821 0.1661 0.1636 -0.0635 -0.0161 0.0095  54  PHE A CE1 
483  C CE2 . PHE A 54  ? 0.1606 0.1424 0.1363 -0.0696 -0.0153 0.0031  54  PHE A CE2 
484  C CZ  . PHE A 54  ? 0.1460 0.1295 0.1237 -0.0677 -0.0183 0.0079  54  PHE A CZ  
485  N N   . ASN A 55  ? 0.1529 0.1424 0.1385 -0.0532 0.0035  -0.0029 55  ASN A N   
486  C CA  . ASN A 55  ? 0.1061 0.0990 0.0971 -0.0480 0.0066  -0.0037 55  ASN A CA  
487  C C   . ASN A 55  ? 0.1307 0.1242 0.1279 -0.0439 0.0055  0.0006  55  ASN A C   
488  O O   . ASN A 55  ? 0.1512 0.1458 0.1486 -0.0442 0.0031  0.0035  55  ASN A O   
489  C CB  . ASN A 55  ? 0.1348 0.1338 0.1246 -0.0476 0.0080  -0.0048 55  ASN A CB  
490  C CG  . ASN A 55  ? 0.1587 0.1628 0.1539 -0.0424 0.0111  -0.0062 55  ASN A CG  
491  O OD1 . ASN A 55  ? 0.1701 0.1732 0.1666 -0.0410 0.0136  -0.0092 55  ASN A OD1 
492  N ND2 . ASN A 55  ? 0.0953 0.1048 0.0940 -0.0391 0.0107  -0.0041 55  ASN A ND2 
493  N N   . LEU A 56  ? 0.1145 0.1070 0.1166 -0.0400 0.0076  0.0010  56  LEU A N   
494  C CA  . LEU A 56  ? 0.1188 0.1125 0.1262 -0.0360 0.0072  0.0054  56  LEU A CA  
495  C C   . LEU A 56  ? 0.1432 0.1416 0.1540 -0.0306 0.0097  0.0057  56  LEU A C   
496  O O   . LEU A 56  ? 0.1346 0.1307 0.1473 -0.0285 0.0121  0.0040  56  LEU A O   
497  C CB  . LEU A 56  ? 0.1160 0.1037 0.1264 -0.0366 0.0072  0.0069  56  LEU A CB  
498  C CG  . LEU A 56  ? 0.1569 0.1410 0.1652 -0.0418 0.0044  0.0066  56  LEU A CG  
499  C CD1 . LEU A 56  ? 0.1650 0.1436 0.1773 -0.0424 0.0053  0.0073  56  LEU A CD1 
500  C CD2 . LEU A 56  ? 0.2257 0.2136 0.2344 -0.0422 0.0014  0.0098  56  LEU A CD2 
501  N N   . THR A 57  ? 0.1115 0.1168 0.1236 -0.0280 0.0091  0.0077  57  THR A N   
502  C CA  . THR A 57  ? 0.1009 0.1121 0.1162 -0.0227 0.0109  0.0084  57  THR A CA  
503  C C   . THR A 57  ? 0.1239 0.1320 0.1433 -0.0187 0.0117  0.0128  57  THR A C   
504  O O   . THR A 57  ? 0.1153 0.1199 0.1354 -0.0200 0.0108  0.0158  57  THR A O   
505  C CB  . THR A 57  ? 0.0969 0.1174 0.1121 -0.0214 0.0100  0.0087  57  THR A CB  
506  O OG1 . THR A 57  ? 0.0814 0.1026 0.0975 -0.0210 0.0085  0.0122  57  THR A OG1 
507  C CG2 . THR A 57  ? 0.1049 0.1272 0.1162 -0.0259 0.0095  0.0047  57  THR A CG2 
508  N N   . PRO A 58  ? 0.1388 0.0543 0.1333 -0.0122 -0.0122 0.0115  58  PRO A N   
509  C CA  . PRO A 58  ? 0.1633 0.0759 0.1550 -0.0116 -0.0122 0.0189  58  PRO A CA  
510  C C   . PRO A 58  ? 0.2214 0.1390 0.2099 -0.0087 -0.0148 0.0220  58  PRO A C   
511  O O   . PRO A 58  ? 0.2006 0.1178 0.1876 -0.0096 -0.0114 0.0274  58  PRO A O   
512  C CB  . PRO A 58  ? 0.1553 0.0639 0.1453 -0.0080 -0.0118 0.0211  58  PRO A CB  
513  C CG  . PRO A 58  ? 0.1389 0.0512 0.1338 -0.0101 -0.0091 0.0140  58  PRO A CG  
514  C CD  . PRO A 58  ? 0.1474 0.0627 0.1442 -0.0114 -0.0102 0.0080  58  PRO A CD  
515  N N   . VAL A 59  ? 0.1773 0.1064 0.1670 -0.0047 -0.0175 0.0159  59  VAL A N   
516  C CA  . VAL A 59  ? 0.1664 0.1092 0.1541 -0.0002 -0.0181 0.0164  59  VAL A CA  
517  C C   . VAL A 59  ? 0.1816 0.1232 0.1704 -0.0048 -0.0175 0.0170  59  VAL A C   
518  O O   . VAL A 59  ? 0.1634 0.1114 0.1499 -0.0031 -0.0163 0.0209  59  VAL A O   
519  C CB  . VAL A 59  ? 0.1453 0.1045 0.1366 0.0045  -0.0208 0.0061  59  VAL A CB  
520  C CG1 . VAL A 59  ? 0.1329 0.0872 0.1322 -0.0016 -0.0193 -0.0043 59  VAL A CG1 
521  C CG2 . VAL A 59  ? 0.1621 0.1382 0.1509 0.0102  -0.0219 0.0058  59  VAL A CG2 
522  N N   . LEU A 60  ? 0.1257 0.0596 0.1170 -0.0091 -0.0176 0.0134  60  LEU A N   
523  C CA  . LEU A 60  ? 0.1408 0.0763 0.1317 -0.0108 -0.0175 0.0140  60  LEU A CA  
524  C C   . LEU A 60  ? 0.2045 0.1392 0.1964 -0.0144 -0.0159 0.0184  60  LEU A C   
525  O O   . LEU A 60  ? 0.1694 0.1116 0.1624 -0.0152 -0.0148 0.0194  60  LEU A O   
526  C CB  . LEU A 60  ? 0.1279 0.0554 0.1176 -0.0105 -0.0169 0.0104  60  LEU A CB  
527  C CG  . LEU A 60  ? 0.1789 0.1115 0.1666 -0.0090 -0.0176 0.0108  60  LEU A CG  
528  C CD1 . LEU A 60  ? 0.1676 0.1108 0.1559 -0.0070 -0.0176 0.0103  60  LEU A CD1 
529  C CD2 . LEU A 60  ? 0.1452 0.0694 0.1271 -0.0041 -0.0159 0.0092  60  LEU A CD2 
530  N N   . ILE A 61  ? 0.1652 0.0908 0.1581 -0.0175 -0.0145 0.0196  61  ILE A N   
531  C CA  . ILE A 61  ? 0.1490 0.0732 0.1461 -0.0229 -0.0101 0.0209  61  ILE A CA  
532  C C   . ILE A 61  ? 0.1693 0.0944 0.1653 -0.0219 -0.0041 0.0267  61  ILE A C   
533  O O   . ILE A 61  ? 0.1620 0.0908 0.1629 -0.0264 0.0009  0.0257  61  ILE A O   
534  C CB  . ILE A 61  ? 0.1846 0.0996 0.1837 -0.0256 -0.0074 0.0202  61  ILE A CB  
535  C CG1 . ILE A 61  ? 0.1889 0.1062 0.1880 -0.0248 -0.0112 0.0142  61  ILE A CG1 
536  C CG2 . ILE A 61  ? 0.2025 0.1148 0.2083 -0.0324 0.0008  0.0197  61  ILE A CG2 
537  C CD1 . ILE A 61  ? 0.2031 0.1198 0.2040 -0.0240 -0.0066 0.0119  61  ILE A CD1 
538  N N   . ASP A 62  ? 0.1564 0.0796 0.1457 -0.0150 -0.0035 0.0322  62  ASP A N   
539  C CA  . ASP A 62  ? 0.1824 0.1057 0.1665 -0.0102 0.0035  0.0397  62  ASP A CA  
540  C C   . ASP A 62  ? 0.1757 0.1101 0.1612 -0.0109 0.0032  0.0381  62  ASP A C   
541  O O   . ASP A 62  ? 0.1912 0.1229 0.1768 -0.0123 0.0120  0.0422  62  ASP A O   
542  C CB  . ASP A 62  ? 0.1721 0.0996 0.1468 0.0015  0.0016  0.0439  62  ASP A CB  
543  C CG  . ASP A 62  ? 0.2796 0.1959 0.2509 0.0048  0.0047  0.0480  62  ASP A CG  
544  O OD1 . ASP A 62  ? 0.2689 0.1701 0.2431 -0.0014 0.0126  0.0510  62  ASP A OD1 
545  O OD2 . ASP A 62  ? 0.3084 0.2326 0.2751 0.0137  -0.0002 0.0468  62  ASP A OD2 
546  N N   . GLN A 63  ? 0.1633 0.1087 0.1498 -0.0095 -0.0050 0.0323  63  GLN A N   
547  C CA  . GLN A 63  ? 0.1645 0.1209 0.1518 -0.0091 -0.0055 0.0310  63  GLN A CA  
548  C C   . GLN A 63  ? 0.1783 0.1368 0.1733 -0.0167 -0.0039 0.0266  63  GLN A C   
549  O O   . GLN A 63  ? 0.1756 0.1396 0.1731 -0.0185 0.0006  0.0271  63  GLN A O   
550  C CB  . GLN A 63  ? 0.1583 0.1245 0.1450 -0.0052 -0.0124 0.0253  63  GLN A CB  
551  C CG  . GLN A 63  ? 0.1675 0.1381 0.1506 0.0015  -0.0147 0.0240  63  GLN A CG  
552  C CD  . GLN A 63  ? 0.2070 0.1860 0.1941 0.0022  -0.0184 0.0146  63  GLN A CD  
553  O OE1 . GLN A 63  ? 0.2187 0.2067 0.2067 0.0031  -0.0187 0.0120  63  GLN A OE1 
554  N NE2 . GLN A 63  ? 0.1482 0.1216 0.1386 0.0007  -0.0193 0.0089  63  GLN A NE2 
555  N N   . ILE A 64  ? 0.1899 0.1465 0.1891 -0.0203 -0.0073 0.0213  64  ILE A N   
556  C CA  . ILE A 64  ? 0.1395 0.1041 0.1467 -0.0257 -0.0065 0.0145  64  ILE A CA  
557  C C   . ILE A 64  ? 0.1614 0.1229 0.1759 -0.0329 0.0040  0.0147  64  ILE A C   
558  O O   . ILE A 64  ? 0.1551 0.1269 0.1772 -0.0373 0.0079  0.0094  64  ILE A O   
559  C CB  . ILE A 64  ? 0.1663 0.1301 0.1744 -0.0259 -0.0111 0.0090  64  ILE A CB  
560  C CG1 . ILE A 64  ? 0.1553 0.1199 0.1559 -0.0180 -0.0173 0.0088  64  ILE A CG1 
561  C CG2 . ILE A 64  ? 0.1709 0.1485 0.1888 -0.0306 -0.0103 -0.0007 64  ILE A CG2 
562  C CD1 . ILE A 64  ? 0.1678 0.1286 0.1652 -0.0150 -0.0202 0.0056  64  ILE A CD1 
563  N N   . GLN A 65  ? 0.1960 0.1423 0.2083 -0.0340 0.0107  0.0205  65  GLN A N   
564  C CA  . GLN A 65  ? 0.1819 0.1193 0.2005 -0.0406 0.0252  0.0215  65  GLN A CA  
565  C C   . GLN A 65  ? 0.2325 0.1701 0.2475 -0.0379 0.0331  0.0274  65  GLN A C   
566  O O   . GLN A 65  ? 0.2076 0.1455 0.2322 -0.0455 0.0447  0.0231  65  GLN A O   
567  C CB  . GLN A 65  ? 0.2410 0.1591 0.2544 -0.0389 0.0320  0.0290  65  GLN A CB  
568  C CG  . GLN A 65  ? 0.2773 0.1926 0.2991 -0.0460 0.0309  0.0213  65  GLN A CG  
569  C CD  . GLN A 65  ? 0.3690 0.2724 0.3828 -0.0404 0.0322  0.0281  65  GLN A CD  
570  O OE1 . GLN A 65  ? 0.3471 0.2459 0.3492 -0.0311 0.0283  0.0366  65  GLN A OE1 
571  N NE2 . GLN A 65  ? 0.4658 0.3676 0.4863 -0.0451 0.0380  0.0230  65  GLN A NE2 
572  N N   . GLU A 66  ? 0.2223 0.1611 0.2243 -0.0272 0.0278  0.0358  66  GLU A N   
573  C CA  . GLU A 66  ? 0.2196 0.1592 0.2156 -0.0224 0.0352  0.0423  66  GLU A CA  
574  C C   . GLU A 66  ? 0.2011 0.1564 0.2061 -0.0279 0.0328  0.0342  66  GLU A C   
575  O O   . GLU A 66  ? 0.2137 0.1672 0.2222 -0.0313 0.0446  0.0349  66  GLU A O   
576  C CB  . GLU A 66  ? 0.2299 0.1734 0.2110 -0.0086 0.0283  0.0500  66  GLU A CB  
577  C CG  . GLU A 66  ? 0.3485 0.2926 0.3194 0.0000  0.0366  0.0584  66  GLU A CG  
578  C CD  . GLU A 66  ? 0.3638 0.3149 0.3193 0.0161  0.0312  0.0648  66  GLU A CD  
579  O OE1 . GLU A 66  ? 0.3223 0.2764 0.2766 0.0194  0.0224  0.0620  66  GLU A OE1 
580  O OE2 . GLU A 66  ? 0.3850 0.3406 0.3300 0.0260  0.0360  0.0712  66  GLU A OE2 
581  N N   . TYR A 67  ? 0.1711 0.1404 0.1797 -0.0283 0.0195  0.0263  67  TYR A N   
582  C CA  . TYR A 67  ? 0.1788 0.1647 0.1955 -0.0317 0.0168  0.0180  67  TYR A CA  
583  C C   . TYR A 67  ? 0.2029 0.1936 0.2354 -0.0427 0.0249  0.0076  67  TYR A C   
584  O O   . TYR A 67  ? 0.2023 0.2018 0.2431 -0.0474 0.0316  0.0025  67  TYR A O   
585  C CB  . TYR A 67  ? 0.1541 0.1509 0.1689 -0.0270 0.0032  0.0130  67  TYR A CB  
586  C CG  . TYR A 67  ? 0.1484 0.1478 0.1539 -0.0189 -0.0023 0.0176  67  TYR A CG  
587  C CD1 . TYR A 67  ? 0.1297 0.1405 0.1357 -0.0171 -0.0026 0.0163  67  TYR A CD1 
588  C CD2 . TYR A 67  ? 0.1596 0.1519 0.1578 -0.0137 -0.0064 0.0210  67  TYR A CD2 
589  C CE1 . TYR A 67  ? 0.1461 0.1606 0.1453 -0.0104 -0.0067 0.0184  67  TYR A CE1 
590  C CE2 . TYR A 67  ? 0.2178 0.2155 0.2109 -0.0076 -0.0101 0.0213  67  TYR A CE2 
591  C CZ  . TYR A 67  ? 0.1965 0.2050 0.1901 -0.0061 -0.0102 0.0199  67  TYR A CZ  
592  O OH  . TYR A 67  ? 0.1876 0.2024 0.1779 -0.0007 -0.0131 0.0180  67  TYR A OH  
593  N N   . ALA A 68  ? 0.1521 0.1392 0.1905 -0.0474 0.0248  0.0022  68  ALA A N   
594  C CA  . ALA A 68  ? 0.1947 0.1909 0.2512 -0.0587 0.0324  -0.0119 68  ALA A CA  
595  C C   . ALA A 68  ? 0.2706 0.2537 0.3348 -0.0672 0.0529  -0.0108 68  ALA A C   
596  O O   . ALA A 68  ? 0.2248 0.2200 0.3070 -0.0775 0.0619  -0.0250 68  ALA A O   
597  C CB  . ALA A 68  ? 0.1620 0.1552 0.2217 -0.0612 0.0291  -0.0171 68  ALA A CB  
598  N N   . GLN A 69  ? 0.2214 0.1805 0.2724 -0.0620 0.0618  0.0049  69  GLN A N   
599  C CA  . GLN A 69  ? 0.2618 0.2018 0.3154 -0.0668 0.0849  0.0096  69  GLN A CA  
600  C C   . GLN A 69  ? 0.3289 0.2717 0.3784 -0.0636 0.0910  0.0143  69  GLN A C   
601  O O   . GLN A 69  ? 0.3796 0.3070 0.4292 -0.0650 0.1101  0.0179  69  GLN A O   
602  C CB  . GLN A 69  ? 0.3486 0.2636 0.3854 -0.0570 0.0906  0.0252  69  GLN A CB  
603  C CG  . GLN A 69  ? 0.3790 0.2912 0.4200 -0.0595 0.0857  0.0193  69  GLN A CG  
604  C CD  . GLN A 69  ? 0.4750 0.3708 0.4982 -0.0471 0.0844  0.0332  69  GLN A CD  
605  O OE1 . GLN A 69  ? 0.5322 0.4203 0.5394 -0.0352 0.0869  0.0465  69  GLN A OE1 
606  N NE2 . GLN A 69  ? 0.4728 0.3672 0.4990 -0.0488 0.0795  0.0289  69  GLN A NE2 
607  N N   . GLY A 70  ? 0.2838 0.2458 0.3280 -0.0571 0.0742  0.0138  70  GLY A N   
608  C CA  . GLY A 70  ? 0.3370 0.3039 0.3772 -0.0537 0.0783  0.0177  70  GLY A CA  
609  C C   . GLY A 70  ? 0.4203 0.3730 0.4384 -0.0396 0.0813  0.0359  70  GLY A C   
610  O O   . GLY A 70  ? 0.4300 0.3821 0.4429 -0.0361 0.0894  0.0410  70  GLY A O   
611  N N   . LYS A 71  ? 0.4171 0.3610 0.4217 -0.0302 0.0746  0.0449  71  LYS A N   
612  C CA  . LYS A 71  ? 0.4296 0.3633 0.4130 -0.0145 0.0784  0.0606  71  LYS A CA  
613  C C   . LYS A 71  ? 0.4162 0.3678 0.3894 -0.0035 0.0592  0.0616  71  LYS A C   
614  O O   . LYS A 71  ? 0.4412 0.3925 0.3976 0.0110  0.0601  0.0715  71  LYS A O   
615  C CB  . LYS A 71  ? 0.4932 0.4054 0.4684 -0.0098 0.0875  0.0694  71  LYS A CB  
616  C CG  . LYS A 71  ? 0.5733 0.4697 0.5629 -0.0226 0.1048  0.0633  71  LYS A CG  
617  C CD  . LYS A 71  ? 0.5994 0.4784 0.5791 -0.0130 0.1123  0.0695  71  LYS A CD  
618  C CE  . LYS A 71  ? 0.5920 0.4729 0.5661 -0.0080 0.0988  0.0716  71  LYS A CE  
619  N NZ  . LYS A 71  ? 0.6575 0.5234 0.6257 -0.0007 0.1074  0.0753  71  LYS A NZ  
620  N N   . ALA A 72  ? 0.2878 0.2555 0.2705 -0.0089 0.0433  0.0507  72  ALA A N   
621  C CA  . ALA A 72  ? 0.2415 0.2238 0.2177 -0.0006 0.0283  0.0492  72  ALA A CA  
622  C C   . ALA A 72  ? 0.3372 0.3325 0.3107 0.0032  0.0276  0.0490  72  ALA A C   
623  O O   . ALA A 72  ? 0.2987 0.3006 0.2823 -0.0046 0.0286  0.0429  72  ALA A O   
624  C CB  . ALA A 72  ? 0.2167 0.2060 0.2023 -0.0066 0.0158  0.0392  72  ALA A CB  
625  N N   . LYS A 73  ? 0.2385 0.2404 0.1989 0.0160  0.0257  0.0545  73  LYS A N   
626  C CA  . LYS A 73  ? 0.2589 0.2756 0.2160 0.0208  0.0238  0.0534  73  LYS A CA  
627  C C   . LYS A 73  ? 0.2736 0.3068 0.2356 0.0211  0.0094  0.0431  73  LYS A C   
628  O O   . LYS A 73  ? 0.2879 0.3312 0.2441 0.0298  0.0034  0.0409  73  LYS A O   
629  C CB  . LYS A 73  ? 0.3086 0.3260 0.2478 0.0364  0.0309  0.0639  73  LYS A CB  
630  C CG  . LYS A 73  ? 0.4423 0.4380 0.3739 0.0381  0.0500  0.0761  73  LYS A CG  
631  C CD  . LYS A 73  ? 0.5696 0.5667 0.4795 0.0575  0.0583  0.0881  73  LYS A CD  
632  C CE  . LYS A 73  ? 0.6164 0.6182 0.5112 0.0744  0.0531  0.0928  73  LYS A CE  
633  N NZ  . LYS A 73  ? 0.6735 0.6799 0.5513 0.0946  0.0596  0.1000  73  LYS A NZ  
634  N N   . ASP A 74  ? 0.1876 0.2246 0.1609 0.0122  0.0053  0.0355  74  ASP A N   
635  C CA  . ASP A 74  ? 0.1527 0.1985 0.1312 0.0116  -0.0043 0.0263  74  ASP A CA  
636  C C   . ASP A 74  ? 0.1922 0.2523 0.1708 0.0144  -0.0057 0.0226  74  ASP A C   
637  O O   . ASP A 74  ? 0.1989 0.2612 0.1818 0.0103  -0.0031 0.0223  74  ASP A O   
638  C CB  . ASP A 74  ? 0.2001 0.2392 0.1873 0.0037  -0.0066 0.0219  74  ASP A CB  
639  C CG  . ASP A 74  ? 0.2370 0.2788 0.2273 0.0046  -0.0125 0.0144  74  ASP A CG  
640  O OD1 . ASP A 74  ? 0.2078 0.2588 0.1980 0.0077  -0.0137 0.0103  74  ASP A OD1 
641  O OD2 . ASP A 74  ? 0.2116 0.2447 0.2039 0.0024  -0.0142 0.0127  74  ASP A OD2 
642  N N   . VAL A 75  ? 0.1501 0.2223 0.1256 0.0211  -0.0096 0.0178  75  VAL A N   
643  C CA  . VAL A 75  ? 0.2237 0.3113 0.1984 0.0249  -0.0099 0.0143  75  VAL A CA  
644  C C   . VAL A 75  ? 0.2175 0.3059 0.2014 0.0190  -0.0115 0.0074  75  VAL A C   
645  O O   . VAL A 75  ? 0.1845 0.2795 0.1691 0.0187  -0.0097 0.0077  75  VAL A O   
646  C CB  . VAL A 75  ? 0.3235 0.4289 0.2944 0.0340  -0.0135 0.0075  75  VAL A CB  
647  C CG1 . VAL A 75  ? 0.3472 0.4530 0.3055 0.0441  -0.0115 0.0160  75  VAL A CG1 
648  C CG2 . VAL A 75  ? 0.3557 0.4638 0.3366 0.0304  -0.0175 -0.0055 75  VAL A CG2 
649  N N   A PHE A 76  ? 0.2062 0.2871 0.1958 0.0155  -0.0136 0.0017  76  PHE A N   
650  N N   B PHE A 76  ? 0.2075 0.2882 0.1970 0.0155  -0.0136 0.0019  76  PHE A N   
651  C CA  A PHE A 76  ? 0.2189 0.2975 0.2138 0.0133  -0.0131 -0.0027 76  PHE A CA  
652  C CA  B PHE A 76  ? 0.2183 0.2972 0.2131 0.0133  -0.0131 -0.0027 76  PHE A CA  
653  C C   A PHE A 76  ? 0.2414 0.3171 0.2372 0.0105  -0.0124 0.0023  76  PHE A C   
654  C C   B PHE A 76  ? 0.2369 0.3126 0.2326 0.0105  -0.0124 0.0023  76  PHE A C   
655  O O   A PHE A 76  ? 0.2370 0.3193 0.2349 0.0112  -0.0118 0.0005  76  PHE A O   
656  O O   B PHE A 76  ? 0.2360 0.3181 0.2340 0.0112  -0.0118 0.0004  76  PHE A O   
657  C CB  A PHE A 76  ? 0.2409 0.3080 0.2389 0.0123  -0.0124 -0.0081 76  PHE A CB  
658  C CB  B PHE A 76  ? 0.2394 0.3074 0.2375 0.0125  -0.0123 -0.0084 76  PHE A CB  
659  C CG  A PHE A 76  ? 0.2028 0.2756 0.2057 0.0132  -0.0101 -0.0190 76  PHE A CG  
660  C CG  B PHE A 76  ? 0.2279 0.2921 0.2284 0.0138  -0.0089 -0.0121 76  PHE A CG  
661  C CD1 A PHE A 76  ? 0.1987 0.2797 0.2027 0.0142  -0.0119 -0.0239 76  PHE A CD1 
662  C CD1 B PHE A 76  ? 0.2182 0.2892 0.2226 0.0148  -0.0053 -0.0201 76  PHE A CD1 
663  C CD2 A PHE A 76  ? 0.2387 0.3104 0.2461 0.0134  -0.0049 -0.0259 76  PHE A CD2 
664  C CD2 B PHE A 76  ? 0.2010 0.2567 0.1991 0.0155  -0.0086 -0.0080 76  PHE A CD2 
665  C CE1 A PHE A 76  ? 0.1648 0.2564 0.1769 0.0140  -0.0094 -0.0383 76  PHE A CE1 
666  C CE1 B PHE A 76  ? 0.1937 0.2585 0.1990 0.0173  0.0001  -0.0223 76  PHE A CE1 
667  C CE2 A PHE A 76  ? 0.2409 0.3185 0.2563 0.0122  -0.0003 -0.0391 76  PHE A CE2 
668  C CE2 B PHE A 76  ? 0.2158 0.2679 0.2128 0.0203  -0.0045 -0.0099 76  PHE A CE2 
669  C CZ  A PHE A 76  ? 0.2219 0.3114 0.2410 0.0118  -0.0028 -0.0468 76  PHE A CZ  
670  C CZ  B PHE A 76  ? 0.2516 0.3060 0.2519 0.0211  0.0006  -0.0161 76  PHE A CZ  
671  N N   . LEU A 77  ? 0.1625 0.2306 0.1579 0.0074  -0.0121 0.0068  77  LEU A N   
672  C CA  . LEU A 77  ? 0.2673 0.3373 0.2672 0.0036  -0.0108 0.0073  77  LEU A CA  
673  C C   . LEU A 77  ? 0.2458 0.3246 0.2470 0.0020  -0.0063 0.0092  77  LEU A C   
674  O O   . LEU A 77  ? 0.2071 0.2946 0.2144 -0.0002 -0.0055 0.0055  77  LEU A O   
675  C CB  . LEU A 77  ? 0.1666 0.2272 0.1679 -0.0006 -0.0098 0.0095  77  LEU A CB  
676  C CG  . LEU A 77  ? 0.2814 0.3470 0.2906 -0.0054 -0.0087 0.0055  77  LEU A CG  
677  C CD1 . LEU A 77  ? 0.3083 0.3821 0.3183 -0.0002 -0.0139 -0.0002 77  LEU A CD1 
678  C CD2 . LEU A 77  ? 0.2834 0.3388 0.2942 -0.0095 -0.0074 0.0064  77  LEU A CD2 
679  N N   . GLU A 78  ? 0.2059 0.2844 0.2008 0.0046  -0.0029 0.0143  78  GLU A N   
680  C CA  . GLU A 78  ? 0.2664 0.3511 0.2604 0.0045  0.0033  0.0172  78  GLU A CA  
681  C C   . GLU A 78  ? 0.2031 0.3009 0.1993 0.0068  0.0002  0.0120  78  GLU A C   
682  O O   . GLU A 78  ? 0.2219 0.3265 0.2220 0.0044  0.0042  0.0113  78  GLU A O   
683  C CB  . GLU A 78  ? 0.4490 0.5302 0.4317 0.0109  0.0084  0.0253  78  GLU A CB  
684  C CG  . GLU A 78  ? 0.6846 0.7680 0.6637 0.0121  0.0180  0.0303  78  GLU A CG  
685  C CD  . GLU A 78  ? 0.8485 0.9241 0.8373 0.0022  0.0277  0.0298  78  GLU A CD  
686  O OE1 . GLU A 78  ? 0.8593 0.9427 0.8547 -0.0017 0.0319  0.0262  78  GLU A OE1 
687  O OE2 . GLU A 78  ? 0.9167 0.9803 0.9086 -0.0024 0.0315  0.0310  78  GLU A OE2 
688  N N   . ALA A 79  ? 0.1969 0.2976 0.1920 0.0108  -0.0054 0.0074  79  ALA A N   
689  C CA  . ALA A 79  ? 0.2159 0.3264 0.2138 0.0128  -0.0067 0.0019  79  ALA A CA  
690  C C   . ALA A 79  ? 0.2322 0.3433 0.2359 0.0114  -0.0079 -0.0012 79  ALA A C   
691  O O   . ALA A 79  ? 0.2408 0.3608 0.2469 0.0133  -0.0075 -0.0043 79  ALA A O   
692  C CB  . ALA A 79  ? 0.2202 0.3316 0.2176 0.0163  -0.0089 -0.0043 79  ALA A CB  
693  N N   . ILE A 80  ? 0.1578 0.2615 0.1631 0.0099  -0.0095 -0.0011 80  ILE A N   
694  C CA  . ILE A 80  ? 0.1983 0.3077 0.2077 0.0115  -0.0113 -0.0049 80  ILE A CA  
695  C C   . ILE A 80  ? 0.1724 0.2940 0.1896 0.0061  -0.0088 -0.0073 80  ILE A C   
696  O O   . ILE A 80  ? 0.1419 0.2776 0.1641 0.0083  -0.0097 -0.0126 80  ILE A O   
697  C CB  . ILE A 80  ? 0.1411 0.2411 0.1487 0.0131  -0.0139 -0.0050 80  ILE A CB  
698  C CG1 . ILE A 80  ? 0.2271 0.3136 0.2285 0.0181  -0.0134 -0.0042 80  ILE A CG1 
699  C CG2 . ILE A 80  ? 0.1316 0.2437 0.1428 0.0170  -0.0165 -0.0101 80  ILE A CG2 
700  C CD1 . ILE A 80  ? 0.3431 0.4304 0.3418 0.0259  -0.0113 -0.0064 80  ILE A CD1 
701  N N   . ARG A 81  ? 0.1531 0.2692 0.1724 -0.0007 -0.0041 -0.0043 81  ARG A N   
702  C CA  . ARG A 81  ? 0.1956 0.3200 0.2255 -0.0083 0.0020  -0.0089 81  ARG A CA  
703  C C   . ARG A 81  ? 0.2006 0.3346 0.2332 -0.0094 0.0072  -0.0096 81  ARG A C   
704  O O   . ARG A 81  ? 0.1822 0.3307 0.2263 -0.0137 0.0101  -0.0180 81  ARG A O   
705  C CB  . ARG A 81  ? 0.2038 0.3140 0.2339 -0.0147 0.0097  -0.0042 81  ARG A CB  
706  C CG  . ARG A 81  ? 0.3014 0.4156 0.3439 -0.0244 0.0213  -0.0094 81  ARG A CG  
707  C CD  . ARG A 81  ? 0.4565 0.5519 0.4980 -0.0299 0.0323  -0.0038 81  ARG A CD  
708  N NE  . ARG A 81  ? 0.5822 0.6760 0.6298 -0.0334 0.0286  -0.0093 81  ARG A NE  
709  C CZ  . ARG A 81  ? 0.6662 0.7732 0.7304 -0.0414 0.0309  -0.0230 81  ARG A CZ  
710  N NH1 . ARG A 81  ? 0.6227 0.7464 0.7009 -0.0473 0.0370  -0.0338 81  ARG A NH1 
711  N NH2 . ARG A 81  ? 0.6831 0.7895 0.7511 -0.0432 0.0269  -0.0278 81  ARG A NH2 
712  N N   . LYS A 82  ? 0.1560 0.2845 0.1789 -0.0054 0.0087  -0.0024 82  LYS A N   
713  C CA  . LYS A 82  ? 0.1334 0.2687 0.1567 -0.0061 0.0151  -0.0014 82  LYS A CA  
714  C C   . LYS A 82  ? 0.1941 0.3466 0.2246 -0.0046 0.0110  -0.0096 82  LYS A C   
715  O O   . LYS A 82  ? 0.1224 0.2789 0.1514 0.0014  0.0028  -0.0126 82  LYS A O   
716  C CB  . LYS A 82  ? 0.1753 0.3066 0.1855 0.0010  0.0149  0.0060  82  LYS A CB  
717  C CG  . LYS A 82  ? 0.2938 0.4119 0.2936 0.0035  0.0204  0.0151  82  LYS A CG  
718  C CD  . LYS A 82  ? 0.3016 0.4256 0.2894 0.0131  0.0178  0.0184  82  LYS A CD  
719  C CE  . LYS A 82  ? 0.4073 0.5230 0.3818 0.0204  0.0217  0.0272  82  LYS A CE  
720  N NZ  . LYS A 82  ? 0.4052 0.5342 0.3690 0.0314  0.0187  0.0274  82  LYS A NZ  
721  N N   . ASP A 83  ? 0.1765 0.3380 0.2142 -0.0091 0.0184  -0.0127 83  ASP A N   
722  C CA  . ASP A 83  ? 0.1472 0.3254 0.1893 -0.0061 0.0154  -0.0187 83  ASP A CA  
723  C C   . ASP A 83  ? 0.1255 0.3006 0.1560 0.0020  0.0107  -0.0134 83  ASP A C   
724  O O   . ASP A 83  ? 0.1307 0.2969 0.1517 0.0036  0.0137  -0.0062 83  ASP A O   
725  C CB  . ASP A 83  ? 0.1943 0.3801 0.2456 -0.0132 0.0265  -0.0223 83  ASP A CB  
726  C CG  . ASP A 83  ? 0.2687 0.4745 0.3265 -0.0106 0.0236  -0.0300 83  ASP A CG  
727  O OD1 . ASP A 83  ? 0.2292 0.4366 0.2787 -0.0031 0.0184  -0.0267 83  ASP A OD1 
728  O OD2 . ASP A 83  ? 0.3117 0.5339 0.3850 -0.0162 0.0266  -0.0415 83  ASP A OD2 
729  N N   . PRO A 84  ? 0.1684 0.3513 0.1991 0.0083  0.0043  -0.0177 84  PRO A N   
730  C CA  . PRO A 84  ? 0.1583 0.3374 0.1807 0.0144  0.0021  -0.0155 84  PRO A CA  
731  C C   . PRO A 84  ? 0.1461 0.3305 0.1654 0.0140  0.0067  -0.0133 84  PRO A C   
732  O O   . PRO A 84  ? 0.1631 0.3456 0.1756 0.0177  0.0056  -0.0122 84  PRO A O   
733  C CB  . PRO A 84  ? 0.1819 0.3672 0.2063 0.0212  -0.0014 -0.0206 84  PRO A CB  
734  C CG  . PRO A 84  ? 0.1594 0.3481 0.1882 0.0220  -0.0043 -0.0236 84  PRO A CG  
735  C CD  . PRO A 84  ? 0.2149 0.4093 0.2519 0.0121  -0.0004 -0.0251 84  PRO A CD  
736  N N   . ASP A 85  ? 0.1439 0.3363 0.1684 0.0098  0.0125  -0.0140 85  ASP A N   
737  C CA  . ASP A 85  ? 0.1874 0.3835 0.2068 0.0107  0.0185  -0.0105 85  ASP A CA  
738  C C   . ASP A 85  ? 0.1485 0.3339 0.1561 0.0128  0.0228  -0.0018 85  ASP A C   
739  O O   . ASP A 85  ? 0.2011 0.3906 0.1996 0.0182  0.0258  0.0017  85  ASP A O   
740  C CB  . ASP A 85  ? 0.1956 0.3996 0.2240 0.0047  0.0267  -0.0133 85  ASP A CB  
741  C CG  . ASP A 85  ? 0.3151 0.5354 0.3531 0.0057  0.0225  -0.0223 85  ASP A CG  
742  O OD1 . ASP A 85  ? 0.3292 0.5524 0.3636 0.0125  0.0159  -0.0238 85  ASP A OD1 
743  O OD2 . ASP A 85  ? 0.3566 0.5874 0.4066 0.0001  0.0272  -0.0288 85  ASP A OD2 
744  N N   . ASP A 86  ? 0.1452 0.3185 0.1519 0.0103  0.0235  0.0017  86  ASP A N   
745  C CA  . ASP A 86  ? 0.2243 0.3867 0.2187 0.0145  0.0279  0.0107  86  ASP A CA  
746  C C   . ASP A 86  ? 0.1830 0.3447 0.1711 0.0203  0.0187  0.0099  86  ASP A C   
747  O O   . ASP A 86  ? 0.2373 0.3936 0.2146 0.0260  0.0206  0.0162  86  ASP A O   
748  C CB  . ASP A 86  ? 0.2361 0.3843 0.2341 0.0077  0.0368  0.0145  86  ASP A CB  
749  C CG  . ASP A 86  ? 0.3076 0.4556 0.3133 0.0008  0.0504  0.0137  86  ASP A CG  
750  O OD1 . ASP A 86  ? 0.3875 0.5393 0.3867 0.0050  0.0566  0.0172  86  ASP A OD1 
751  O OD2 . ASP A 86  ? 0.3745 0.5205 0.3939 -0.0089 0.0552  0.0077  86  ASP A OD2 
752  N N   . LEU A 87  ? 0.1420 0.3088 0.1366 0.0199  0.0105  0.0019  87  LEU A N   
753  C CA  . LEU A 87  ? 0.1719 0.3372 0.1639 0.0234  0.0044  -0.0014 87  LEU A CA  
754  C C   . LEU A 87  ? 0.1373 0.3157 0.1220 0.0309  0.0035  -0.0041 87  LEU A C   
755  O O   . LEU A 87  ? 0.1485 0.3388 0.1342 0.0328  0.0043  -0.0082 87  LEU A O   
756  C CB  . LEU A 87  ? 0.1652 0.3287 0.1654 0.0216  0.0001  -0.0090 87  LEU A CB  
757  C CG  . LEU A 87  ? 0.1686 0.3220 0.1736 0.0179  -0.0012 -0.0079 87  LEU A CG  
758  C CD1 . LEU A 87  ? 0.1893 0.3413 0.1981 0.0207  -0.0030 -0.0136 87  LEU A CD1 
759  C CD2 . LEU A 87  ? 0.1746 0.3167 0.1761 0.0170  -0.0026 -0.0046 87  LEU A CD2 
760  N N   . GLU A 88  ? 0.1409 0.3200 0.1189 0.0360  0.0015  -0.0032 88  GLU A N   
761  C CA  . GLU A 88  ? 0.1463 0.3440 0.1200 0.0442  -0.0016 -0.0108 88  GLU A CA  
762  C C   . GLU A 88  ? 0.1676 0.3717 0.1539 0.0401  -0.0048 -0.0257 88  GLU A C   
763  O O   . GLU A 88  ? 0.1768 0.3669 0.1712 0.0336  -0.0050 -0.0279 88  GLU A O   
764  C CB  . GLU A 88  ? 0.1770 0.3758 0.1422 0.0512  -0.0036 -0.0083 88  GLU A CB  
765  C CG  . GLU A 88  ? 0.2763 0.4708 0.2248 0.0603  0.0025  0.0062  88  GLU A CG  
766  C CD  . GLU A 88  ? 0.4435 0.6257 0.3859 0.0631  0.0029  0.0130  88  GLU A CD  
767  O OE1 . GLU A 88  ? 0.4342 0.6240 0.3808 0.0643  -0.0040 0.0041  88  GLU A OE1 
768  O OE2 . GLU A 88  ? 0.5422 0.7072 0.4762 0.0640  0.0114  0.0265  88  GLU A OE2 
769  N N   . LYS A 89  ? 0.2318 0.3428 0.1471 -0.0164 -0.0004 -0.0496 89  LYS A N   
770  C CA  . LYS A 89  ? 0.2343 0.3495 0.1598 -0.0246 -0.0014 -0.0637 89  LYS A CA  
771  C C   . LYS A 89  ? 0.2775 0.3996 0.2132 -0.0264 -0.0090 -0.0638 89  LYS A C   
772  O O   . LYS A 89  ? 0.2631 0.3767 0.2143 -0.0320 -0.0073 -0.0682 89  LYS A O   
773  C CB  . LYS A 89  ? 0.2989 0.4290 0.2105 -0.0274 -0.0015 -0.0764 89  LYS A CB  
774  C CG  . LYS A 89  ? 0.3868 0.5089 0.2900 -0.0277 0.0077  -0.0796 89  LYS A CG  
775  C CD  . LYS A 89  ? 0.4448 0.5839 0.3313 -0.0301 0.0068  -0.0921 89  LYS A CD  
776  C CE  . LYS A 89  ? 0.5725 0.7026 0.4521 -0.0317 0.0172  -0.0975 89  LYS A CE  
777  N NZ  . LYS A 89  ? 0.6140 0.7357 0.4834 -0.0238 0.0218  -0.0835 89  LYS A NZ  
778  N N   . GLU A 90  ? 0.2593 0.3962 0.1861 -0.0206 -0.0166 -0.0582 90  GLU A N   
779  C CA  . GLU A 90  ? 0.2550 0.4004 0.1917 -0.0215 -0.0236 -0.0578 90  GLU A CA  
780  C C   . GLU A 90  ? 0.2578 0.3853 0.2091 -0.0216 -0.0217 -0.0489 90  GLU A C   
781  O O   . GLU A 90  ? 0.2549 0.3832 0.2187 -0.0259 -0.0243 -0.0520 90  GLU A O   
782  C CB  . GLU A 90  ? 0.3398 0.5027 0.2640 -0.0123 -0.0312 -0.0504 90  GLU A CB  
783  C CG  . GLU A 90  ? 0.5369 0.7244 0.4464 -0.0105 -0.0359 -0.0586 90  GLU A CG  
784  C CD  . GLU A 90  ? 0.6897 0.8880 0.5945 0.0007  -0.0417 -0.0478 90  GLU A CD  
785  O OE1 . GLU A 90  ? 0.6582 0.8501 0.5668 0.0061  -0.0433 -0.0368 90  GLU A OE1 
786  O OE2 . GLU A 90  ? 0.7726 0.9855 0.6701 0.0044  -0.0441 -0.0506 90  GLU A OE2 
787  N N   . GLU A 91  ? 0.2064 0.3191 0.1560 -0.0171 -0.0171 -0.0383 91  GLU A N   
788  C CA  . GLU A 91  ? 0.2075 0.3063 0.1698 -0.0170 -0.0160 -0.0304 91  GLU A CA  
789  C C   . GLU A 91  ? 0.1955 0.2829 0.1720 -0.0231 -0.0114 -0.0364 91  GLU A C   
790  O O   . GLU A 91  ? 0.1774 0.2588 0.1656 -0.0248 -0.0126 -0.0343 91  GLU A O   
791  C CB  . GLU A 91  ? 0.2102 0.2990 0.1666 -0.0115 -0.0119 -0.0188 91  GLU A CB  
792  C CG  . GLU A 91  ? 0.2651 0.3587 0.2107 -0.0042 -0.0155 -0.0092 91  GLU A CG  
793  C CD  . GLU A 91  ? 0.2896 0.3715 0.2264 0.0004  -0.0089 0.0009  91  GLU A CD  
794  O OE1 . GLU A 91  ? 0.2461 0.3232 0.1778 -0.0007 -0.0024 -0.0006 91  GLU A OE1 
795  O OE2 . GLU A 91  ? 0.2611 0.3377 0.1966 0.0044  -0.0090 0.0100  91  GLU A OE2 
796  N N   . VAL A 92  ? 0.2087 0.2923 0.1835 -0.0255 -0.0055 -0.0432 92  VAL A N   
797  C CA  . VAL A 92  ? 0.2219 0.2939 0.2091 -0.0298 0.0000  -0.0489 92  VAL A CA  
798  C C   . VAL A 92  ? 0.2343 0.3089 0.2278 -0.0359 -0.0019 -0.0576 92  VAL A C   
799  O O   . VAL A 92  ? 0.2455 0.3093 0.2505 -0.0377 0.0003  -0.0568 92  VAL A O   
800  C CB  . VAL A 92  ? 0.2266 0.2948 0.2096 -0.0308 0.0075  -0.0557 92  VAL A CB  
801  C CG1 . VAL A 92  ? 0.2609 0.3160 0.2559 -0.0340 0.0143  -0.0620 92  VAL A CG1 
802  C CG2 . VAL A 92  ? 0.2432 0.3081 0.2222 -0.0256 0.0107  -0.0471 92  VAL A CG2 
803  N N   . GLU A 93  ? 0.2034 0.2936 0.1893 -0.0391 -0.0058 -0.0660 93  GLU A N   
804  C CA  . GLU A 93  ? 0.2248 0.3206 0.2176 -0.0466 -0.0071 -0.0761 93  GLU A CA  
805  C C   . GLU A 93  ? 0.2275 0.3232 0.2288 -0.0454 -0.0119 -0.0686 93  GLU A C   
806  O O   . GLU A 93  ? 0.2903 0.3777 0.3020 -0.0508 -0.0089 -0.0723 93  GLU A O   
807  C CB  . GLU A 93  ? 0.2802 0.3987 0.2631 -0.0497 -0.0118 -0.0867 93  GLU A CB  
808  C CG  . GLU A 93  ? 0.3514 0.4700 0.3250 -0.0516 -0.0065 -0.0953 93  GLU A CG  
809  C CD  . GLU A 93  ? 0.4947 0.6385 0.4565 -0.0540 -0.0117 -0.1061 93  GLU A CD  
810  O OE1 . GLU A 93  ? 0.5429 0.7061 0.5046 -0.0534 -0.0200 -0.1067 93  GLU A OE1 
811  O OE2 . GLU A 93  ? 0.5104 0.6562 0.4627 -0.0561 -0.0075 -0.1145 93  GLU A OE2 
812  N N   . LYS A 94  ? 0.2130 0.3168 0.2089 -0.0385 -0.0184 -0.0582 94  LYS A N   
813  C CA  . LYS A 94  ? 0.2417 0.3450 0.2451 -0.0370 -0.0223 -0.0510 94  LYS A CA  
814  C C   . LYS A 94  ? 0.2492 0.3324 0.2622 -0.0368 -0.0178 -0.0445 94  LYS A C   
815  O O   . LYS A 94  ? 0.1865 0.2651 0.2082 -0.0396 -0.0177 -0.0442 94  LYS A O   
816  C CB  . LYS A 94  ? 0.2919 0.4038 0.2868 -0.0286 -0.0281 -0.0403 94  LYS A CB  
817  C CG  . LYS A 94  ? 0.4195 0.5544 0.4053 -0.0265 -0.0341 -0.0450 94  LYS A CG  
818  C CD  . LYS A 94  ? 0.5244 0.6647 0.5010 -0.0162 -0.0384 -0.0327 94  LYS A CD  
819  C CE  . LYS A 94  ? 0.6332 0.7990 0.5994 -0.0118 -0.0448 -0.0366 94  LYS A CE  
820  N NZ  . LYS A 94  ? 0.6953 0.8647 0.6510 0.0004  -0.0477 -0.0235 94  LYS A NZ  
821  N N   . LEU A 95  ? 0.1679 0.2407 0.1793 -0.0332 -0.0138 -0.0395 95  LEU A N   
822  C CA  . LEU A 95  ? 0.1811 0.2390 0.2015 -0.0316 -0.0103 -0.0335 95  LEU A CA  
823  C C   . LEU A 95  ? 0.2026 0.2499 0.2307 -0.0363 -0.0046 -0.0403 95  LEU A C   
824  O O   . LEU A 95  ? 0.2008 0.2393 0.2360 -0.0360 -0.0037 -0.0361 95  LEU A O   
825  C CB  . LEU A 95  ? 0.2250 0.2781 0.2433 -0.0273 -0.0068 -0.0290 95  LEU A CB  
826  C CG  . LEU A 95  ? 0.4196 0.4629 0.4467 -0.0241 -0.0042 -0.0224 95  LEU A CG  
827  C CD1 . LEU A 95  ? 0.4627 0.5066 0.4878 -0.0210 -0.0009 -0.0198 95  LEU A CD1 
828  C CD2 . LEU A 95  ? 0.3696 0.4133 0.3998 -0.0227 -0.0091 -0.0146 95  LEU A CD2 
829  N N   . ILE A 96  ? 0.1962 0.2431 0.2221 -0.0405 0.0002  -0.0508 96  ILE A N   
830  C CA  . ILE A 96  ? 0.2131 0.2466 0.2453 -0.0453 0.0080  -0.0582 96  ILE A CA  
831  C C   . ILE A 96  ? 0.2453 0.2815 0.2818 -0.0519 0.0068  -0.0628 96  ILE A C   
832  O O   . ILE A 96  ? 0.2011 0.2230 0.2442 -0.0531 0.0118  -0.0610 96  ILE A O   
833  C CB  . ILE A 96  ? 0.2217 0.2544 0.2496 -0.0493 0.0143  -0.0700 96  ILE A CB  
834  C CG1 . ILE A 96  ? 0.2137 0.2383 0.2410 -0.0426 0.0187  -0.0650 96  ILE A CG1 
835  C CG2 . ILE A 96  ? 0.2729 0.2935 0.3059 -0.0573 0.0230  -0.0811 96  ILE A CG2 
836  C CD1 . ILE A 96  ? 0.3651 0.3929 0.3852 -0.0452 0.0232  -0.0751 96  ILE A CD1 
837  N N   . GLU A 97  ? 0.1912 0.2467 0.2240 -0.0553 0.0002  -0.0678 97  GLU A N   
838  C CA  . GLU A 97  ? 0.2695 0.3313 0.3082 -0.0622 -0.0008 -0.0737 97  GLU A CA  
839  C C   . GLU A 97  ? 0.2456 0.3020 0.2892 -0.0582 -0.0037 -0.0621 97  GLU A C   
840  O O   . GLU A 97  ? 0.2348 0.2844 0.2851 -0.0632 0.0001  -0.0643 97  GLU A O   
841  C CB  . GLU A 97  ? 0.3546 0.4428 0.3887 -0.0651 -0.0082 -0.0816 97  GLU A CB  
842  C CG  . GLU A 97  ? 0.5465 0.6447 0.5885 -0.0743 -0.0079 -0.0917 97  GLU A CG  
843  C CD  . GLU A 97  ? 0.7256 0.8117 0.7725 -0.0854 0.0030  -0.1059 97  GLU A CD  
844  O OE1 . GLU A 97  ? 0.7530 0.8348 0.7948 -0.0870 0.0075  -0.1128 97  GLU A OE1 
845  O OE2 . GLU A 97  ? 0.7949 0.8724 0.8491 -0.0899 0.0088  -0.1073 97  GLU A OE2 
846  N N   . PHE A 98  ? 0.2089 0.2678 0.2488 -0.0499 -0.0094 -0.0502 98  PHE A N   
847  C CA  . PHE A 98  ? 0.2020 0.2551 0.2458 -0.0464 -0.0116 -0.0400 98  PHE A CA  
848  C C   . PHE A 98  ? 0.1924 0.2250 0.2409 -0.0453 -0.0047 -0.0359 98  PHE A C   
849  O O   . PHE A 98  ? 0.1824 0.2080 0.2351 -0.0463 -0.0031 -0.0326 98  PHE A O   
850  C CB  . PHE A 98  ? 0.1433 0.2017 0.1819 -0.0387 -0.0174 -0.0297 98  PHE A CB  
851  C CG  . PHE A 98  ? 0.1859 0.2421 0.2273 -0.0359 -0.0204 -0.0209 98  PHE A CG  
852  C CD1 . PHE A 98  ? 0.1629 0.2305 0.2050 -0.0368 -0.0247 -0.0212 98  PHE A CD1 
853  C CD2 . PHE A 98  ? 0.1769 0.2215 0.2203 -0.0321 -0.0188 -0.0128 98  PHE A CD2 
854  C CE1 . PHE A 98  ? 0.1432 0.2079 0.1873 -0.0343 -0.0266 -0.0136 98  PHE A CE1 
855  C CE2 . PHE A 98  ? 0.2105 0.2538 0.2553 -0.0301 -0.0214 -0.0058 98  PHE A CE2 
856  C CZ  . PHE A 98  ? 0.1851 0.2371 0.2300 -0.0315 -0.0248 -0.0062 98  PHE A CZ  
857  N N   . THR A 99  ? 0.1411 0.1645 0.1885 -0.0422 -0.0002 -0.0355 99  THR A N   
858  C CA  . THR A 99  ? 0.2273 0.2322 0.2786 -0.0391 0.0068  -0.0314 99  THR A CA  
859  C C   . THR A 99  ? 0.2050 0.1980 0.2596 -0.0460 0.0150  -0.0387 99  THR A C   
860  O O   . THR A 99  ? 0.2243 0.2045 0.2812 -0.0444 0.0188  -0.0330 99  THR A O   
861  C CB  . THR A 99  ? 0.2067 0.2064 0.2572 -0.0345 0.0109  -0.0315 99  THR A CB  
862  O OG1 . THR A 99  ? 0.1878 0.1988 0.2355 -0.0297 0.0046  -0.0259 99  THR A OG1 
863  C CG2 . THR A 99  ? 0.2207 0.2034 0.2750 -0.0282 0.0174  -0.0253 99  THR A CG2 
864  N N   . LYS A 100 ? 0.2106 0.2072 0.2647 -0.0541 0.0186  -0.0517 100 LYS A N   
865  C CA  . LYS A 100 ? 0.2312 0.2165 0.2891 -0.0632 0.0281  -0.0613 100 LYS A CA  
866  C C   . LYS A 100 ? 0.2631 0.2505 0.3248 -0.0670 0.0267  -0.0592 100 LYS A C   
867  O O   . LYS A 100 ? 0.3063 0.2759 0.3708 -0.0704 0.0362  -0.0597 100 LYS A O   
868  C CB  . LYS A 100 ? 0.2412 0.2383 0.2982 -0.0731 0.0297  -0.0779 100 LYS A CB  
869  C CG  . LYS A 100 ? 0.4940 0.4876 0.5468 -0.0719 0.0337  -0.0835 100 LYS A CG  
870  C CD  . LYS A 100 ? 0.6375 0.6054 0.6913 -0.0654 0.0438  -0.0774 100 LYS A CD  
871  C CE  . LYS A 100 ? 0.7586 0.7151 0.8114 -0.0716 0.0553  -0.0909 100 LYS A CE  
872  N NZ  . LYS A 100 ? 0.8200 0.7544 0.8768 -0.0789 0.0687  -0.0971 100 LYS A NZ  
873  N N   . LEU A 101 ? 0.2078 0.2163 0.2693 -0.0667 0.0161  -0.0575 101 LEU A N   
874  C CA  . LEU A 101 ? 0.2196 0.2331 0.2854 -0.0704 0.0145  -0.0563 101 LEU A CA  
875  C C   . LEU A 101 ? 0.2138 0.2111 0.2792 -0.0638 0.0165  -0.0430 101 LEU A C   
876  O O   . LEU A 101 ? 0.2693 0.2596 0.3377 -0.0678 0.0211  -0.0428 101 LEU A O   
877  C CB  . LEU A 101 ? 0.2440 0.2833 0.3090 -0.0687 0.0029  -0.0557 101 LEU A CB  
878  C CG  . LEU A 101 ? 0.4042 0.4505 0.4735 -0.0696 -0.0002 -0.0520 101 LEU A CG  
879  C CD1 . LEU A 101 ? 0.3732 0.4202 0.4501 -0.0812 0.0070  -0.0637 101 LEU A CD1 
880  C CD2 . LEU A 101 ? 0.4734 0.5428 0.5407 -0.0648 -0.0110 -0.0491 101 LEU A CD2 
881  N N   . ASN A 102 ? 0.1892 0.1816 0.2505 -0.0539 0.0132  -0.0325 102 ASN A N   
882  C CA  . ASN A 102 ? 0.2000 0.1831 0.2599 -0.0466 0.0125  -0.0199 102 ASN A CA  
883  C C   . ASN A 102 ? 0.2650 0.2264 0.3234 -0.0411 0.0213  -0.0148 102 ASN A C   
884  O O   . ASN A 102 ? 0.2231 0.1767 0.2794 -0.0345 0.0215  -0.0045 102 ASN A O   
885  C CB  . ASN A 102 ? 0.1568 0.1523 0.2140 -0.0394 0.0027  -0.0121 102 ASN A CB  
886  C CG  . ASN A 102 ? 0.2492 0.2617 0.3065 -0.0419 -0.0048 -0.0131 102 ASN A CG  
887  O OD1 . ASN A 102 ? 0.2170 0.2301 0.2762 -0.0442 -0.0049 -0.0117 102 ASN A OD1 
888  N ND2 . ASN A 102 ? 0.2742 0.3001 0.3291 -0.0409 -0.0103 -0.0154 102 ASN A ND2 
889  N N   . TYR A 103 ? 0.3198 0.2719 0.3788 -0.0433 0.0289  -0.0220 103 TYR A N   
890  C CA  . TYR A 103 ? 0.4191 0.3527 0.4766 -0.0357 0.0369  -0.0173 103 TYR A CA  
891  C C   . TYR A 103 ? 0.3372 0.2504 0.3924 -0.0311 0.0450  -0.0087 103 TYR A C   
892  O O   . TYR A 103 ? 0.2476 0.1516 0.3004 -0.0197 0.0469  0.0012  103 TYR A O   
893  C CB  . TYR A 103 ? 0.5141 0.4398 0.5727 -0.0421 0.0458  -0.0297 103 TYR A CB  
894  C CG  . TYR A 103 ? 0.6229 0.5271 0.6804 -0.0349 0.0568  -0.0269 103 TYR A CG  
895  C CD1 . TYR A 103 ? 0.6861 0.5946 0.7435 -0.0250 0.0537  -0.0219 103 TYR A CD1 
896  C CD2 . TYR A 103 ? 0.7386 0.6176 0.7954 -0.0379 0.0714  -0.0296 103 TYR A CD2 
897  C CE1 . TYR A 103 ? 0.7947 0.6848 0.8519 -0.0168 0.0640  -0.0190 103 TYR A CE1 
898  C CE2 . TYR A 103 ? 0.8250 0.6821 0.8801 -0.0296 0.0828  -0.0262 103 TYR A CE2 
899  C CZ  . TYR A 103 ? 0.8384 0.7022 0.8940 -0.0184 0.0785  -0.0207 103 TYR A CZ  
900  O OH  . TYR A 103 ? 0.8119 0.6555 0.8666 -0.0086 0.0898  -0.0170 103 TYR A OH  
901  N N   . GLU A 104 ? 0.3051 0.2115 0.3608 -0.0394 0.0502  -0.0123 104 GLU A N   
902  C CA  . GLU A 104 ? 0.3222 0.2053 0.3740 -0.0359 0.0608  -0.0047 104 GLU A CA  
903  C C   . GLU A 104 ? 0.3299 0.2182 0.3779 -0.0297 0.0540  0.0072  104 GLU A C   
904  O O   . GLU A 104 ? 0.3553 0.2253 0.3978 -0.0248 0.0620  0.0156  104 GLU A O   
905  C CB  . GLU A 104 ? 0.4415 0.3117 0.4959 -0.0493 0.0731  -0.0157 104 GLU A CB  
906  C CG  . GLU A 104 ? 0.6377 0.4949 0.6940 -0.0549 0.0840  -0.0271 104 GLU A CG  
907  C CD  . GLU A 104 ? 0.7972 0.6291 0.8479 -0.0425 0.0942  -0.0178 104 GLU A CD  
908  O OE1 . GLU A 104 ? 0.8465 0.6666 0.8908 -0.0324 0.0970  -0.0045 104 GLU A OE1 
909  O OE2 . GLU A 104 ? 0.8649 0.6918 0.9167 -0.0415 0.0987  -0.0237 104 GLU A OE2 
910  N N   . LYS A 105 ? 0.2190 0.1306 0.2688 -0.0297 0.0407  0.0081  105 LYS A N   
911  C CA  . LYS A 105 ? 0.2210 0.1381 0.2670 -0.0250 0.0346  0.0178  105 LYS A CA  
912  C C   . LYS A 105 ? 0.2381 0.1521 0.2790 -0.0111 0.0323  0.0298  105 LYS A C   
913  O O   . LYS A 105 ? 0.2261 0.1459 0.2691 -0.0056 0.0291  0.0298  105 LYS A O   
914  C CB  . LYS A 105 ? 0.2192 0.1602 0.2684 -0.0288 0.0223  0.0148  105 LYS A CB  
915  C CG  . LYS A 105 ? 0.2379 0.1868 0.2924 -0.0406 0.0231  0.0038  105 LYS A CG  
916  C CD  . LYS A 105 ? 0.2268 0.1986 0.2837 -0.0420 0.0118  0.0013  105 LYS A CD  
917  C CE  . LYS A 105 ? 0.2308 0.2134 0.2935 -0.0522 0.0125  -0.0097 105 LYS A CE  
918  N NZ  . LYS A 105 ? 0.2020 0.2062 0.2659 -0.0515 0.0022  -0.0109 105 LYS A NZ  
919  N N   . PRO A 106 ? 0.2640 0.1709 0.2982 -0.0050 0.0337  0.0397  106 PRO A N   
920  C CA  . PRO A 106 ? 0.2906 0.1999 0.3199 0.0091  0.0300  0.0508  106 PRO A CA  
921  C C   . PRO A 106 ? 0.2347 0.1681 0.2682 0.0119  0.0173  0.0504  106 PRO A C   
922  O O   . PRO A 106 ? 0.2578 0.1958 0.2919 0.0219  0.0153  0.0550  106 PRO A O   
923  C CB  . PRO A 106 ? 0.2765 0.1796 0.2971 0.0122  0.0315  0.0594  106 PRO A CB  
924  C CG  . PRO A 106 ? 0.2891 0.1744 0.3094 0.0021  0.0428  0.0543  106 PRO A CG  
925  C CD  . PRO A 106 ? 0.2621 0.1584 0.2926 -0.0104 0.0400  0.0408  106 PRO A CD  
926  N N   . ILE A 107 ? 0.1931 0.1420 0.2300 0.0038  0.0094  0.0449  107 ILE A N   
927  C CA  . ILE A 107 ? 0.2245 0.1931 0.2648 0.0058  -0.0003 0.0443  107 ILE A CA  
928  C C   . ILE A 107 ? 0.2409 0.2124 0.2868 0.0061  0.0004  0.0391  107 ILE A C   
929  O O   . ILE A 107 ? 0.2323 0.2182 0.2814 0.0091  -0.0056 0.0392  107 ILE A O   
930  C CB  . ILE A 107 ? 0.1594 0.1408 0.2009 -0.0020 -0.0071 0.0404  107 ILE A CB  
931  C CG1 . ILE A 107 ? 0.1623 0.1413 0.2070 -0.0114 -0.0044 0.0319  107 ILE A CG1 
932  C CG2 . ILE A 107 ? 0.2183 0.2000 0.2540 -0.0008 -0.0089 0.0460  107 ILE A CG2 
933  C CD1 . ILE A 107 ? 0.1500 0.1430 0.1961 -0.0165 -0.0111 0.0286  107 ILE A CD1 
934  N N   . TYR A 108 ? 0.1789 0.1377 0.2263 0.0023  0.0082  0.0335  108 TYR A N   
935  C CA  . TYR A 108 ? 0.2419 0.2012 0.2933 0.0030  0.0104  0.0283  108 TYR A CA  
936  C C   . TYR A 108 ? 0.2248 0.1709 0.2758 0.0132  0.0181  0.0332  108 TYR A C   
937  O O   . TYR A 108 ? 0.2772 0.2191 0.3312 0.0135  0.0228  0.0282  108 TYR A O   
938  C CB  . TYR A 108 ? 0.2176 0.1733 0.2707 -0.0076 0.0144  0.0174  108 TYR A CB  
939  C CG  . TYR A 108 ? 0.1597 0.1332 0.2142 -0.0139 0.0062  0.0120  108 TYR A CG  
940  C CD1 . TYR A 108 ? 0.1466 0.1290 0.2000 -0.0173 0.0002  0.0135  108 TYR A CD1 
941  C CD2 . TYR A 108 ? 0.2552 0.2359 0.3111 -0.0150 0.0051  0.0064  108 TYR A CD2 
942  C CE1 . TYR A 108 ? 0.2094 0.2061 0.2630 -0.0211 -0.0061 0.0099  108 TYR A CE1 
943  C CE2 . TYR A 108 ? 0.2103 0.2056 0.2654 -0.0190 -0.0014 0.0030  108 TYR A CE2 
944  C CZ  . TYR A 108 ? 0.1986 0.2014 0.2523 -0.0215 -0.0069 0.0052  108 TYR A CZ  
945  O OH  . TYR A 108 ? 0.1911 0.2065 0.2429 -0.0238 -0.0123 0.0032  108 TYR A OH  
946  N N   . ARG A 109 ? 0.2395 0.1790 0.2860 0.0224  0.0198  0.0431  109 ARG A N   
947  C CA  . ARG A 109 ? 0.2750 0.2006 0.3198 0.0344  0.0279  0.0495  109 ARG A CA  
948  C C   . ARG A 109 ? 0.3123 0.2556 0.3626 0.0440  0.0219  0.0520  109 ARG A C   
949  O O   . ARG A 109 ? 0.3700 0.3248 0.4193 0.0545  0.0167  0.0603  109 ARG A O   
950  C CB  . ARG A 109 ? 0.3178 0.2308 0.3539 0.0425  0.0319  0.0604  109 ARG A CB  
951  C CG  . ARG A 109 ? 0.4309 0.3273 0.4634 0.0573  0.0414  0.0689  109 ARG A CG  
952  C CD  . ARG A 109 ? 0.5911 0.4724 0.6124 0.0645  0.0467  0.0800  109 ARG A CD  
953  N NE  . ARG A 109 ? 0.6487 0.5126 0.6670 0.0509  0.0542  0.0745  109 ARG A NE  
954  C CZ  . ARG A 109 ? 0.7141 0.5704 0.7237 0.0501  0.0564  0.0800  109 ARG A CZ  
955  N NH1 . ARG A 109 ? 0.7525 0.6198 0.7540 0.0610  0.0501  0.0893  109 ARG A NH1 
956  N NH2 . ARG A 109 ? 0.6690 0.5123 0.6780 0.0365  0.0635  0.0732  109 ARG A NH2 
957  N N   . PHE A 110 ? 0.3240 0.2715 0.3804 0.0399  0.0228  0.0439  110 PHE A N   
958  C CA  . PHE A 110 ? 0.3070 0.2680 0.3700 0.0484  0.0207  0.0447  110 PHE A CA  
959  C C   . PHE A 110 ? 0.2527 0.1959 0.3171 0.0513  0.0324  0.0411  110 PHE A C   
960  O O   . PHE A 110 ? 0.2536 0.1873 0.3175 0.0404  0.0371  0.0315  110 PHE A O   
961  C CB  . PHE A 110 ? 0.2427 0.2251 0.3112 0.0404  0.0123  0.0378  110 PHE A CB  
962  C CG  . PHE A 110 ? 0.2267 0.2247 0.2941 0.0360  0.0024  0.0396  110 PHE A CG  
963  C CD1 . PHE A 110 ? 0.2701 0.2867 0.3407 0.0432  -0.0043 0.0448  110 PHE A CD1 
964  C CD2 . PHE A 110 ? 0.2634 0.2592 0.3270 0.0247  0.0000  0.0353  110 PHE A CD2 
965  C CE1 . PHE A 110 ? 0.2518 0.2818 0.3210 0.0379  -0.0123 0.0449  110 PHE A CE1 
966  C CE2 . PHE A 110 ? 0.2844 0.2926 0.3467 0.0209  -0.0078 0.0367  110 PHE A CE2 
967  C CZ  . PHE A 110 ? 0.3001 0.3242 0.3648 0.0270  -0.0135 0.0412  110 PHE A CZ  
968  N N   . GLU A 111 ? 0.2994 0.2387 0.3654 0.0662  0.0372  0.0482  111 GLU A N   
969  C CA  . GLU A 111 ? 0.3643 0.2851 0.4317 0.0696  0.0497  0.0445  111 GLU A CA  
970  C C   . GLU A 111 ? 0.3351 0.2660 0.4085 0.0606  0.0485  0.0329  111 GLU A C   
971  O O   . GLU A 111 ? 0.3347 0.2490 0.4069 0.0547  0.0581  0.0246  111 GLU A O   
972  C CB  . GLU A 111 ? 0.4440 0.3632 0.5134 0.0893  0.0542  0.0546  111 GLU A CB  
973  C CG  . GLU A 111 ? 0.6221 0.5197 0.6928 0.0935  0.0688  0.0507  111 GLU A CG  
974  C CD  . GLU A 111 ? 0.8756 0.7377 0.9372 0.0977  0.0837  0.0555  111 GLU A CD  
975  O OE1 . GLU A 111 ? 0.9423 0.7831 1.0028 0.0937  0.0965  0.0481  111 GLU A OE1 
976  O OE2 . GLU A 111 ? 0.9743 0.8341 1.0274 0.1015  0.0811  0.0646  111 GLU A OE2 
977  N N   . ARG A 112 ? 0.2660 0.2233 0.3448 0.0583  0.0375  0.0316  112 ARG A N   
978  C CA  . ARG A 112 ? 0.2768 0.2436 0.3595 0.0504  0.0368  0.0217  112 ARG A CA  
979  C C   . ARG A 112 ? 0.2454 0.2035 0.3222 0.0353  0.0381  0.0122  112 ARG A C   
980  O O   . ARG A 112 ? 0.2525 0.2078 0.3293 0.0299  0.0428  0.0032  112 ARG A O   
981  C CB  . ARG A 112 ? 0.2228 0.2174 0.3115 0.0499  0.0262  0.0226  112 ARG A CB  
982  C CG  . ARG A 112 ? 0.2745 0.2786 0.3657 0.0420  0.0260  0.0138  112 ARG A CG  
983  C CD  . ARG A 112 ? 0.2391 0.2374 0.3347 0.0480  0.0355  0.0101  112 ARG A CD  
984  N NE  . ARG A 112 ? 0.2493 0.2626 0.3488 0.0434  0.0344  0.0040  112 ARG A NE  
985  C CZ  . ARG A 112 ? 0.3004 0.3107 0.4026 0.0452  0.0424  -0.0016 112 ARG A CZ  
986  N NH1 . ARG A 112 ? 0.2964 0.2885 0.3982 0.0515  0.0522  -0.0023 112 ARG A NH1 
987  N NH2 . ARG A 112 ? 0.2683 0.2924 0.3730 0.0406  0.0417  -0.0066 112 ARG A NH2 
988  N N   . ILE A 113 ? 0.2424 0.1983 0.3143 0.0286  0.0338  0.0135  113 ILE A N   
989  C CA  . ILE A 113 ? 0.2516 0.2024 0.3192 0.0152  0.0347  0.0042  113 ILE A CA  
990  C C   . ILE A 113 ? 0.3140 0.2422 0.3795 0.0127  0.0474  -0.0023 113 ILE A C   
991  O O   . ILE A 113 ? 0.3137 0.2406 0.3776 0.0033  0.0506  -0.0134 113 ILE A O   
992  C CB  . ILE A 113 ? 0.3201 0.2743 0.3843 0.0098  0.0281  0.0072  113 ILE A CB  
993  C CG1 . ILE A 113 ? 0.2733 0.2490 0.3386 0.0083  0.0168  0.0093  113 ILE A CG1 
994  C CG2 . ILE A 113 ? 0.4090 0.3556 0.4698 -0.0024 0.0315  -0.0022 113 ILE A CG2 
995  C CD1 . ILE A 113 ? 0.2869 0.2664 0.3494 0.0048  0.0108  0.0130  113 ILE A CD1 
996  N N   . ARG A 114 ? 0.3299 0.2397 0.3945 0.0212  0.0556  0.0045  114 ARG A N   
997  C CA  . ARG A 114 ? 0.4538 0.3380 0.5164 0.0195  0.0705  -0.0011 114 ARG A CA  
998  C C   . ARG A 114 ? 0.4230 0.3063 0.4885 0.0215  0.0764  -0.0082 114 ARG A C   
999  O O   . ARG A 114 ? 0.4437 0.3156 0.5075 0.0122  0.0851  -0.0202 114 ARG A O   
1000 C CB  . ARG A 114 ? 0.5129 0.3764 0.5727 0.0315  0.0789  0.0104  114 ARG A CB  
1001 C CG  . ARG A 114 ? 0.6258 0.4915 0.6816 0.0321  0.0728  0.0196  114 ARG A CG  
1002 C CD  . ARG A 114 ? 0.7601 0.6010 0.8103 0.0443  0.0839  0.0309  114 ARG A CD  
1003 N NE  . ARG A 114 ? 0.8328 0.6749 0.8775 0.0463  0.0791  0.0404  114 ARG A NE  
1004 C CZ  . ARG A 114 ? 0.8372 0.6888 0.8794 0.0607  0.0727  0.0538  114 ARG A CZ  
1005 N NH1 . ARG A 114 ? 0.8274 0.6902 0.8736 0.0748  0.0699  0.0594  114 ARG A NH1 
1006 N NH2 . ARG A 114 ? 0.8542 0.7056 0.8900 0.0610  0.0693  0.0610  114 ARG A NH2 
1007 N N   . GLU A 115 ? 0.3896 0.2868 0.4602 0.0327  0.0721  -0.0020 115 GLU A N   
1008 C CA  . GLU A 115 ? 0.4080 0.3065 0.4819 0.0347  0.0776  -0.0087 115 GLU A CA  
1009 C C   . GLU A 115 ? 0.4438 0.3546 0.5154 0.0207  0.0733  -0.0211 115 GLU A C   
1010 O O   . GLU A 115 ? 0.4223 0.3235 0.4916 0.0147  0.0820  -0.0322 115 GLU A O   
1011 C CB  . GLU A 115 ? 0.4554 0.3715 0.5368 0.0485  0.0726  -0.0001 115 GLU A CB  
1012 C CG  . GLU A 115 ? 0.5466 0.4563 0.6298 0.0648  0.0749  0.0132  115 GLU A CG  
1013 C CD  . GLU A 115 ? 0.5952 0.5292 0.6875 0.0776  0.0681  0.0202  115 GLU A CD  
1014 O OE1 . GLU A 115 ? 0.5844 0.5385 0.6820 0.0727  0.0626  0.0145  115 GLU A OE1 
1015 O OE2 . GLU A 115 ? 0.6243 0.5582 0.7181 0.0927  0.0686  0.0313  115 GLU A OE2 
1016 N N   . LEU A 116 ? 0.3844 0.3161 0.4554 0.0158  0.0605  -0.0194 116 LEU A N   
1017 C CA  . LEU A 116 ? 0.3311 0.2764 0.3985 0.0055  0.0558  -0.0286 116 LEU A CA  
1018 C C   . LEU A 116 ? 0.4428 0.3794 0.5042 -0.0070 0.0598  -0.0402 116 LEU A C   
1019 O O   . LEU A 116 ? 0.4642 0.4054 0.5217 -0.0138 0.0616  -0.0508 116 LEU A O   
1020 C CB  . LEU A 116 ? 0.3263 0.2919 0.3934 0.0039  0.0428  -0.0229 116 LEU A CB  
1021 C CG  . LEU A 116 ? 0.3005 0.2802 0.3742 0.0130  0.0380  -0.0145 116 LEU A CG  
1022 C CD1 . LEU A 116 ? 0.2875 0.2824 0.3600 0.0095  0.0270  -0.0098 116 LEU A CD1 
1023 C CD2 . LEU A 116 ? 0.3273 0.3139 0.4033 0.0144  0.0419  -0.0193 116 LEU A CD2 
1024 N N   . MET A 117 ? 0.4140 0.3395 0.4746 -0.0105 0.0615  -0.0391 117 MET A N   
1025 C CA  . MET A 117 ? 0.4154 0.3353 0.4723 -0.0235 0.0658  -0.0518 117 MET A CA  
1026 C C   . MET A 117 ? 0.5391 0.4376 0.5956 -0.0258 0.0811  -0.0615 117 MET A C   
1027 O O   . MET A 117 ? 0.5901 0.4864 0.6440 -0.0382 0.0857  -0.0753 117 MET A O   
1028 C CB  . MET A 117 ? 0.3649 0.2808 0.4220 -0.0279 0.0638  -0.0486 117 MET A CB  
1029 C CG  . MET A 117 ? 0.3708 0.3075 0.4275 -0.0280 0.0494  -0.0418 117 MET A CG  
1030 S SD  . MET A 117 ? 0.4376 0.3995 0.4899 -0.0369 0.0396  -0.0512 117 MET A SD  
1031 C CE  . MET A 117 ? 0.4242 0.3974 0.4760 -0.0275 0.0343  -0.0437 117 MET A CE  
1032 N N   . ASN A 118 ? 0.5802 0.4642 0.6396 -0.0142 0.0895  -0.0552 118 ASN A N   
1033 C CA  . ASN A 118 ? 0.6911 0.5533 0.7500 -0.0147 0.1054  -0.0639 118 ASN A CA  
1034 C C   . ASN A 118 ? 0.6969 0.5688 0.7545 -0.0159 0.1064  -0.0728 118 ASN A C   
1035 O O   . ASN A 118 ? 0.7614 0.6170 0.8177 -0.0189 0.1196  -0.0831 118 ASN A O   
1036 C CB  . ASN A 118 ? 0.7658 0.6065 0.8277 0.0007  0.1153  -0.0521 118 ASN A CB  
1037 C CG  . ASN A 118 ? 0.8452 0.6619 0.9050 -0.0005 0.1242  -0.0487 118 ASN A CG  
1038 O OD1 . ASN A 118 ? 0.8746 0.6827 0.9319 -0.0150 0.1298  -0.0603 118 ASN A OD1 
1039 N ND2 . ASN A 118 ? 0.8822 0.6883 0.9428 0.0147  0.1265  -0.0332 118 ASN A ND2 
1040 N N   . LYS A 119 ? 0.5839 0.4804 0.6415 -0.0139 0.0941  -0.0691 119 LYS A N   
1041 C CA  . LYS A 119 ? 0.5608 0.4665 0.6168 -0.0135 0.0956  -0.0754 119 LYS A CA  
1042 C C   . LYS A 119 ? 0.5821 0.4993 0.6297 -0.0275 0.0925  -0.0897 119 LYS A C   
1043 O O   . LYS A 119 ? 0.5278 0.4580 0.5723 -0.0347 0.0828  -0.0904 119 LYS A O   
1044 C CB  . LYS A 119 ? 0.5261 0.4512 0.5862 -0.0042 0.0858  -0.0643 119 LYS A CB  
1045 C CG  . LYS A 119 ? 0.5819 0.5000 0.6509 0.0110  0.0904  -0.0532 119 LYS A CG  
1046 C CD  . LYS A 119 ? 0.6208 0.5610 0.6955 0.0182  0.0815  -0.0448 119 LYS A CD  
1047 C CE  . LYS A 119 ? 0.6450 0.5830 0.7297 0.0340  0.0853  -0.0347 119 LYS A CE  
1048 N NZ  . LYS A 119 ? 0.6673 0.6100 0.7577 0.0404  0.0923  -0.0379 119 LYS A NZ  
1049 N N   . GLU A 120 ? 0.6530 0.5664 0.6968 -0.0308 0.1011  -0.1013 120 GLU A N   
1050 C CA  . GLU A 120 ? 0.6394 0.5649 0.6738 -0.0436 0.0989  -0.1162 120 GLU A CA  
1051 C C   . GLU A 120 ? 0.5793 0.5306 0.6077 -0.0428 0.0860  -0.1120 120 GLU A C   
1052 O O   . GLU A 120 ? 0.5678 0.5350 0.5886 -0.0510 0.0781  -0.1181 120 GLU A O   
1053 C CB  . GLU A 120 ? 0.6697 0.5822 0.7010 -0.0473 0.1132  -0.1305 120 GLU A CB  
1054 C CG  . GLU A 120 ? 0.7233 0.6054 0.7599 -0.0472 0.1289  -0.1341 120 GLU A CG  
1055 C CD  . GLU A 120 ? 0.8139 0.6816 0.8485 -0.0477 0.1437  -0.1444 120 GLU A CD  
1056 O OE1 . GLU A 120 ? 0.7791 0.6593 0.8083 -0.0481 0.1427  -0.1504 120 GLU A OE1 
1057 O OE2 . GLU A 120 ? 0.8509 0.6976 0.8889 -0.0473 0.1548  -0.1428 120 GLU A OE2 
1058 N N   . LYS A 121 ? 0.5709 0.5270 0.6026 -0.0327 0.0841  -0.1015 121 LYS A N   
1059 C CA  . LYS A 121 ? 0.5671 0.5437 0.5927 -0.0315 0.0749  -0.0970 121 LYS A CA  
1060 C C   . LYS A 121 ? 0.4819 0.4619 0.5167 -0.0211 0.0708  -0.0819 121 LYS A C   
1061 O O   . LYS A 121 ? 0.4948 0.4653 0.5390 -0.0131 0.0777  -0.0780 121 LYS A O   
1062 C CB  . LYS A 121 ? 0.6260 0.6063 0.6431 -0.0336 0.0811  -0.1066 121 LYS A CB  
1063 C CG  . LYS A 121 ? 0.6546 0.6522 0.6643 -0.0312 0.0748  -0.1010 121 LYS A CG  
1064 C CD  . LYS A 121 ? 0.7295 0.7244 0.7423 -0.0253 0.0837  -0.1008 121 LYS A CD  
1065 C CE  . LYS A 121 ? 0.7539 0.7519 0.7795 -0.0161 0.0814  -0.0870 121 LYS A CE  
1066 N NZ  . LYS A 121 ? 0.7279 0.7256 0.7596 -0.0100 0.0906  -0.0874 121 LYS A NZ  
1067 N N   . LEU A 122 ? 0.4247 0.4188 0.4573 -0.0211 0.0600  -0.0739 122 LEU A N   
1068 C CA  . LEU A 122 ? 0.3302 0.3295 0.3716 -0.0134 0.0555  -0.0612 122 LEU A CA  
1069 C C   . LEU A 122 ? 0.3611 0.3725 0.3996 -0.0118 0.0552  -0.0590 122 LEU A C   
1070 O O   . LEU A 122 ? 0.3937 0.4130 0.4202 -0.0166 0.0524  -0.0618 122 LEU A O   
1071 C CB  . LEU A 122 ? 0.2998 0.3041 0.3414 -0.0149 0.0454  -0.0538 122 LEU A CB  
1072 C CG  . LEU A 122 ? 0.3428 0.3358 0.3866 -0.0176 0.0458  -0.0556 122 LEU A CG  
1073 C CD1 . LEU A 122 ? 0.3742 0.3744 0.4172 -0.0196 0.0358  -0.0490 122 LEU A CD1 
1074 C CD2 . LEU A 122 ? 0.3973 0.3761 0.4510 -0.0099 0.0529  -0.0514 122 LEU A CD2 
1075 N N   . ASN A 123 ? 0.3268 0.3405 0.3762 -0.0046 0.0586  -0.0538 123 ASN A N   
1076 C CA  . ASN A 123 ? 0.2798 0.3050 0.3286 -0.0039 0.0596  -0.0516 123 ASN A CA  
1077 C C   . ASN A 123 ? 0.2296 0.2646 0.2801 -0.0044 0.0510  -0.0426 123 ASN A C   
1078 O O   . ASN A 123 ? 0.2229 0.2563 0.2730 -0.0055 0.0438  -0.0386 123 ASN A O   
1079 C CB  . ASN A 123 ? 0.3884 0.4143 0.4492 0.0031  0.0681  -0.0524 123 ASN A CB  
1080 C CG  . ASN A 123 ? 0.3739 0.4013 0.4505 0.0117  0.0661  -0.0449 123 ASN A CG  
1081 O OD1 . ASN A 123 ? 0.2981 0.3294 0.3771 0.0117  0.0578  -0.0380 123 ASN A OD1 
1082 N ND2 . ASN A 123 ? 0.3297 0.3543 0.4165 0.0198  0.0741  -0.0461 123 ASN A ND2 
1083 N N   . ARG A 124 ? 0.2416 0.2861 0.2939 -0.0042 0.0527  -0.0399 124 ARG A N   
1084 C CA  . ARG A 124 ? 0.2550 0.3067 0.3074 -0.0062 0.0465  -0.0327 124 ARG A CA  
1085 C C   . ARG A 124 ? 0.2827 0.3381 0.3490 -0.0022 0.0412  -0.0270 124 ARG A C   
1086 O O   . ARG A 124 ? 0.2365 0.2924 0.3005 -0.0042 0.0342  -0.0222 124 ARG A O   
1087 C CB  . ARG A 124 ? 0.2601 0.3198 0.3128 -0.0078 0.0521  -0.0321 124 ARG A CB  
1088 C CG  . ARG A 124 ? 0.2557 0.3202 0.3079 -0.0109 0.0482  -0.0258 124 ARG A CG  
1089 C CD  . ARG A 124 ? 0.2749 0.3450 0.3275 -0.0139 0.0558  -0.0259 124 ARG A CD  
1090 N NE  . ARG A 124 ? 0.2706 0.3436 0.3245 -0.0176 0.0536  -0.0208 124 ARG A NE  
1091 C CZ  . ARG A 124 ? 0.3315 0.4146 0.4017 -0.0178 0.0514  -0.0198 124 ARG A CZ  
1092 N NH1 . ARG A 124 ? 0.2926 0.3850 0.3787 -0.0127 0.0505  -0.0222 124 ARG A NH1 
1093 N NH2 . ARG A 124 ? 0.3145 0.3990 0.3847 -0.0225 0.0506  -0.0166 124 ARG A NH2 
1094 N N   . GLU A 125 ? 0.1990 0.2578 0.2790 0.0043  0.0447  -0.0272 125 GLU A N   
1095 C CA  . GLU A 125 ? 0.2244 0.2890 0.3163 0.0096  0.0394  -0.0214 125 GLU A CA  
1096 C C   . GLU A 125 ? 0.2385 0.2910 0.3261 0.0108  0.0350  -0.0190 125 GLU A C   
1097 O O   . GLU A 125 ? 0.1928 0.2482 0.2829 0.0116  0.0283  -0.0135 125 GLU A O   
1098 C CB  . GLU A 125 ? 0.2858 0.3590 0.3928 0.0183  0.0443  -0.0217 125 GLU A CB  
1099 C CG  . GLU A 125 ? 0.4641 0.5528 0.5783 0.0162  0.0486  -0.0243 125 GLU A CG  
1100 C CD  . GLU A 125 ? 0.6671 0.7712 0.7997 0.0255  0.0514  -0.0240 125 GLU A CD  
1101 O OE1 . GLU A 125 ? 0.7132 0.8116 0.8503 0.0352  0.0527  -0.0222 125 GLU A OE1 
1102 O OE2 . GLU A 125 ? 0.7123 0.8343 0.8548 0.0233  0.0531  -0.0257 125 GLU A OE2 
1103 N N   . GLU A 126 ? 0.1962 0.2349 0.2772 0.0101  0.0395  -0.0240 126 GLU A N   
1104 C CA  . GLU A 126 ? 0.2271 0.2534 0.3043 0.0095  0.0371  -0.0231 126 GLU A CA  
1105 C C   . GLU A 126 ? 0.2450 0.2728 0.3128 0.0019  0.0297  -0.0221 126 GLU A C   
1106 O O   . GLU A 126 ? 0.2307 0.2553 0.2989 0.0019  0.0248  -0.0180 126 GLU A O   
1107 C CB  . GLU A 126 ? 0.2455 0.2570 0.3188 0.0090  0.0457  -0.0308 126 GLU A CB  
1108 C CG  . GLU A 126 ? 0.2862 0.2933 0.3697 0.0191  0.0536  -0.0297 126 GLU A CG  
1109 C CD  . GLU A 126 ? 0.3901 0.3836 0.4702 0.0185  0.0646  -0.0389 126 GLU A CD  
1110 O OE1 . GLU A 126 ? 0.3702 0.3610 0.4399 0.0093  0.0658  -0.0474 126 GLU A OE1 
1111 O OE2 . GLU A 126 ? 0.4477 0.4342 0.5356 0.0278  0.0723  -0.0377 126 GLU A OE2 
1112 N N   . LEU A 127 ? 0.2186 0.2517 0.2776 -0.0036 0.0292  -0.0253 127 LEU A N   
1113 C CA  . LEU A 127 ? 0.1976 0.2332 0.2475 -0.0088 0.0224  -0.0234 127 LEU A CA  
1114 C C   . LEU A 127 ? 0.1868 0.2294 0.2413 -0.0078 0.0169  -0.0156 127 LEU A C   
1115 O O   . LEU A 127 ? 0.1630 0.2048 0.2144 -0.0098 0.0112  -0.0124 127 LEU A O   
1116 C CB  . LEU A 127 ? 0.2158 0.2550 0.2532 -0.0127 0.0239  -0.0274 127 LEU A CB  
1117 C CG  . LEU A 127 ? 0.2912 0.3262 0.3203 -0.0160 0.0271  -0.0368 127 LEU A CG  
1118 C CD1 . LEU A 127 ? 0.2649 0.3058 0.2806 -0.0181 0.0289  -0.0397 127 LEU A CD1 
1119 C CD2 . LEU A 127 ? 0.2485 0.2814 0.2747 -0.0197 0.0220  -0.0390 127 LEU A CD2 
1120 N N   . LEU A 128 ? 0.1794 0.2298 0.2418 -0.0054 0.0191  -0.0134 128 LEU A N   
1121 C CA  . LEU A 128 ? 0.1523 0.2104 0.2206 -0.0055 0.0145  -0.0079 128 LEU A CA  
1122 C C   . LEU A 128 ? 0.1218 0.1780 0.1959 -0.0017 0.0097  -0.0041 128 LEU A C   
1123 O O   . LEU A 128 ? 0.1531 0.2109 0.2259 -0.0036 0.0043  -0.0003 128 LEU A O   
1124 C CB  . LEU A 128 ? 0.1433 0.2131 0.2218 -0.0042 0.0183  -0.0084 128 LEU A CB  
1125 C CG  . LEU A 128 ? 0.2023 0.2759 0.2762 -0.0097 0.0223  -0.0093 128 LEU A CG  
1126 C CD1 . LEU A 128 ? 0.2428 0.3291 0.3296 -0.0088 0.0276  -0.0118 128 LEU A CD1 
1127 C CD2 . LEU A 128 ? 0.1930 0.2660 0.2620 -0.0141 0.0183  -0.0053 128 LEU A CD2 
1128 N N   . ASP A 129 ? 0.1395 0.1912 0.2191 0.0041  0.0126  -0.0047 129 ASP A N   
1129 C CA  . ASP A 129 ? 0.1809 0.2281 0.2635 0.0087  0.0095  -0.0001 129 ASP A CA  
1130 C C   . ASP A 129 ? 0.1502 0.1866 0.2240 0.0038  0.0070  -0.0005 129 ASP A C   
1131 O O   . ASP A 129 ? 0.1696 0.2058 0.2429 0.0038  0.0022  0.0041  129 ASP A O   
1132 C CB  . ASP A 129 ? 0.1659 0.2072 0.2546 0.0172  0.0151  0.0002  129 ASP A CB  
1133 C CG  . ASP A 129 ? 0.2602 0.3166 0.3604 0.0245  0.0156  0.0023  129 ASP A CG  
1134 O OD1 . ASP A 129 ? 0.2300 0.3015 0.3338 0.0210  0.0117  0.0025  129 ASP A OD1 
1135 O OD2 . ASP A 129 ? 0.2659 0.3196 0.3720 0.0339  0.0200  0.0039  129 ASP A OD2 
1136 N N   . LEU A 130 ? 0.1772 0.2062 0.2440 -0.0008 0.0103  -0.0066 130 LEU A N   
1137 C CA  . LEU A 130 ? 0.1492 0.1722 0.2091 -0.0062 0.0077  -0.0084 130 LEU A CA  
1138 C C   . LEU A 130 ? 0.1594 0.1902 0.2155 -0.0094 0.0009  -0.0047 130 LEU A C   
1139 O O   . LEU A 130 ? 0.1477 0.1762 0.2029 -0.0107 -0.0028 -0.0020 130 LEU A O   
1140 C CB  . LEU A 130 ? 0.1350 0.1545 0.1883 -0.0111 0.0116  -0.0172 130 LEU A CB  
1141 C CG  . LEU A 130 ? 0.1834 0.1992 0.2321 -0.0170 0.0099  -0.0214 130 LEU A CG  
1142 C CD1 . LEU A 130 ? 0.2408 0.2438 0.2947 -0.0153 0.0137  -0.0200 130 LEU A CD1 
1143 C CD2 . LEU A 130 ? 0.2738 0.2903 0.3161 -0.0223 0.0132  -0.0317 130 LEU A CD2 
1144 N N   . GLN A 131 ? 0.1304 0.1688 0.1838 -0.0105 0.0004  -0.0043 131 GLN A N   
1145 C CA  . GLN A 131 ? 0.1614 0.2045 0.2104 -0.0129 -0.0041 -0.0005 131 GLN A CA  
1146 C C   . GLN A 131 ? 0.1941 0.2396 0.2495 -0.0113 -0.0076 0.0049  131 GLN A C   
1147 O O   . GLN A 131 ? 0.1403 0.1850 0.1931 -0.0129 -0.0115 0.0076  131 GLN A O   
1148 C CB  . GLN A 131 ? 0.1525 0.2002 0.1973 -0.0140 -0.0014 -0.0005 131 GLN A CB  
1149 C CG  . GLN A 131 ? 0.1343 0.1815 0.1683 -0.0156 0.0009  -0.0044 131 GLN A CG  
1150 C CD  . GLN A 131 ? 0.2144 0.2641 0.2445 -0.0158 0.0057  -0.0036 131 GLN A CD  
1151 O OE1 . GLN A 131 ? 0.1615 0.2140 0.2002 -0.0153 0.0093  -0.0035 131 GLN A OE1 
1152 N NE2 . GLN A 131 ? 0.1709 0.2202 0.1880 -0.0163 0.0063  -0.0025 131 GLN A NE2 
1153 N N   . THR A 132 ? 0.1391 0.1898 0.2030 -0.0078 -0.0061 0.0060  132 THR A N   
1154 C CA  . THR A 132 ? 0.1192 0.1766 0.1885 -0.0067 -0.0098 0.0100  132 THR A CA  
1155 C C   . THR A 132 ? 0.1633 0.2154 0.2334 -0.0033 -0.0126 0.0133  132 THR A C   
1156 O O   . THR A 132 ? 0.1493 0.2035 0.2186 -0.0041 -0.0166 0.0165  132 THR A O   
1157 C CB  . THR A 132 ? 0.1031 0.1724 0.1823 -0.0039 -0.0080 0.0093  132 THR A CB  
1158 O OG1 . THR A 132 ? 0.1317 0.2038 0.2096 -0.0076 -0.0035 0.0059  132 THR A OG1 
1159 C CG2 . THR A 132 ? 0.1213 0.2014 0.2055 -0.0043 -0.0123 0.0115  132 THR A CG2 
1160 N N   . LEU A 133 ? 0.1412 0.1848 0.2119 0.0003  -0.0093 0.0124  133 LEU A N   
1161 C CA  . LEU A 133 ? 0.1635 0.1988 0.2334 0.0034  -0.0098 0.0160  133 LEU A CA  
1162 C C   . LEU A 133 ? 0.1670 0.1961 0.2304 -0.0025 -0.0118 0.0154  133 LEU A C   
1163 O O   . LEU A 133 ? 0.1603 0.1866 0.2225 -0.0017 -0.0139 0.0194  133 LEU A O   
1164 C CB  . LEU A 133 ? 0.1762 0.2004 0.2477 0.0082  -0.0033 0.0149  133 LEU A CB  
1165 C CG  . LEU A 133 ? 0.2311 0.2614 0.3099 0.0176  -0.0014 0.0180  133 LEU A CG  
1166 C CD1 . LEU A 133 ? 0.2268 0.2446 0.3068 0.0221  0.0070  0.0155  133 LEU A CD1 
1167 C CD2 . LEU A 133 ? 0.2304 0.2645 0.3103 0.0244  -0.0052 0.0256  133 LEU A CD2 
1168 N N   . ASN A 134 ? 0.1188 0.1472 0.1779 -0.0080 -0.0112 0.0104  134 ASN A N   
1169 C CA  . ASN A 134 ? 0.1173 0.1449 0.1717 -0.0128 -0.0141 0.0097  134 ASN A CA  
1170 C C   . ASN A 134 ? 0.2010 0.2346 0.2544 -0.0131 -0.0187 0.0143  134 ASN A C   
1171 O O   . ASN A 134 ? 0.1964 0.2279 0.2486 -0.0143 -0.0208 0.0165  134 ASN A O   
1172 C CB  . ASN A 134 ? 0.1071 0.1375 0.1564 -0.0168 -0.0137 0.0039  134 ASN A CB  
1173 C CG  . ASN A 134 ? 0.1569 0.1812 0.2059 -0.0198 -0.0099 -0.0027 134 ASN A CG  
1174 O OD1 . ASN A 134 ? 0.1859 0.2080 0.2349 -0.0232 -0.0103 -0.0044 134 ASN A OD1 
1175 N ND2 . ASN A 134 ? 0.1776 0.1987 0.2272 -0.0191 -0.0051 -0.0071 134 ASN A ND2 
1176 N N   . LEU A 135 ? 0.1453 0.1858 0.1994 -0.0128 -0.0193 0.0152  135 LEU A N   
1177 C CA  . LEU A 135 ? 0.1826 0.2275 0.2363 -0.0141 -0.0221 0.0183  135 LEU A CA  
1178 C C   . LEU A 135 ? 0.1823 0.2284 0.2394 -0.0115 -0.0244 0.0217  135 LEU A C   
1179 O O   . LEU A 135 ? 0.1855 0.2301 0.2399 -0.0129 -0.0266 0.0238  135 LEU A O   
1180 C CB  . LEU A 135 ? 0.2273 0.2785 0.2825 -0.0153 -0.0204 0.0175  135 LEU A CB  
1181 C CG  . LEU A 135 ? 0.2732 0.3231 0.3221 -0.0183 -0.0182 0.0171  135 LEU A CG  
1182 C CD1 . LEU A 135 ? 0.2175 0.2733 0.2708 -0.0205 -0.0150 0.0160  135 LEU A CD1 
1183 C CD2 . LEU A 135 ? 0.1696 0.2157 0.2130 -0.0196 -0.0202 0.0196  135 LEU A CD2 
1184 N N   . LEU A 136 ? 0.1355 0.1850 0.1979 -0.0069 -0.0236 0.0224  136 LEU A N   
1185 C CA  . LEU A 136 ? 0.1062 0.1603 0.1709 -0.0026 -0.0262 0.0264  136 LEU A CA  
1186 C C   . LEU A 136 ? 0.1249 0.1680 0.1852 -0.0006 -0.0257 0.0297  136 LEU A C   
1187 O O   . LEU A 136 ? 0.1431 0.1881 0.2014 0.0016  -0.0281 0.0336  136 LEU A O   
1188 C CB  . LEU A 136 ? 0.1724 0.2347 0.2440 0.0040  -0.0253 0.0269  136 LEU A CB  
1189 C CG  . LEU A 136 ? 0.1499 0.2275 0.2279 0.0018  -0.0260 0.0235  136 LEU A CG  
1190 C CD1 . LEU A 136 ? 0.1297 0.2165 0.2159 0.0092  -0.0245 0.0235  136 LEU A CD1 
1191 C CD2 . LEU A 136 ? 0.1583 0.2467 0.2365 -0.0011 -0.0303 0.0236  136 LEU A CD2 
1192 N N   . ALA A 137 ? 0.1592 0.1910 0.2177 -0.0020 -0.0219 0.0277  137 ALA A N   
1193 C CA  . ALA A 137 ? 0.1831 0.2036 0.2382 -0.0020 -0.0197 0.0298  137 ALA A CA  
1194 C C   . ALA A 137 ? 0.1542 0.1763 0.2056 -0.0061 -0.0229 0.0311  137 ALA A C   
1195 O O   . ALA A 137 ? 0.1647 0.1807 0.2130 -0.0048 -0.0219 0.0347  137 ALA A O   
1196 C CB  . ALA A 137 ? 0.2031 0.2136 0.2578 -0.0056 -0.0146 0.0247  137 ALA A CB  
1197 N N   . TRP A 138 ? 0.1105 0.1396 0.1615 -0.0104 -0.0257 0.0286  138 TRP A N   
1198 C CA  . TRP A 138 ? 0.1502 0.1800 0.1980 -0.0137 -0.0278 0.0294  138 TRP A CA  
1199 C C   . TRP A 138 ? 0.1371 0.1740 0.1841 -0.0131 -0.0308 0.0316  138 TRP A C   
1200 O O   . TRP A 138 ? 0.1446 0.1824 0.1889 -0.0162 -0.0318 0.0314  138 TRP A O   
1201 C CB  . TRP A 138 ? 0.1655 0.1971 0.2121 -0.0176 -0.0281 0.0258  138 TRP A CB  
1202 C CG  . TRP A 138 ? 0.1621 0.1900 0.2095 -0.0193 -0.0257 0.0220  138 TRP A CG  
1203 C CD1 . TRP A 138 ? 0.2015 0.2292 0.2501 -0.0193 -0.0237 0.0182  138 TRP A CD1 
1204 C CD2 . TRP A 138 ? 0.1307 0.1557 0.1785 -0.0224 -0.0243 0.0200  138 TRP A CD2 
1205 N NE1 . TRP A 138 ? 0.2026 0.2277 0.2519 -0.0227 -0.0214 0.0134  138 TRP A NE1 
1206 C CE2 . TRP A 138 ? 0.1950 0.2190 0.2444 -0.0249 -0.0217 0.0142  138 TRP A CE2 
1207 C CE3 . TRP A 138 ? 0.1795 0.2035 0.2266 -0.0239 -0.0245 0.0218  138 TRP A CE3 
1208 C CZ2 . TRP A 138 ? 0.2000 0.2232 0.2516 -0.0296 -0.0192 0.0093  138 TRP A CZ2 
1209 C CZ3 . TRP A 138 ? 0.1768 0.1996 0.2263 -0.0280 -0.0218 0.0178  138 TRP A CZ3 
1210 C CH2 . TRP A 138 ? 0.2347 0.2578 0.2868 -0.0312 -0.0193 0.0113  138 TRP A CH2 
1211 N N   . CYS A 139 ? 0.1510 0.1940 0.2004 -0.0091 -0.0319 0.0331  139 CYS A N   
1212 C CA  . CYS A 139 ? 0.1372 0.1908 0.1869 -0.0097 -0.0350 0.0331  139 CYS A CA  
1213 C C   . CYS A 139 ? 0.1586 0.2100 0.2027 -0.0094 -0.0363 0.0361  139 CYS A C   
1214 O O   . CYS A 139 ? 0.1502 0.1948 0.1913 -0.0053 -0.0352 0.0402  139 CYS A O   
1215 C CB  . CYS A 139 ? 0.1428 0.2076 0.1977 -0.0046 -0.0365 0.0335  139 CYS A CB  
1216 S SG  . CYS A 139 ? 0.1721 0.2555 0.2299 -0.0076 -0.0401 0.0300  139 CYS A SG  
1217 N N   . GLY A 140 ? 0.1381 0.1933 0.1800 -0.0140 -0.0375 0.0339  140 GLY A N   
1218 C CA  . GLY A 140 ? 0.1570 0.2110 0.1931 -0.0143 -0.0383 0.0359  140 GLY A CA  
1219 C C   . GLY A 140 ? 0.1481 0.2146 0.1827 -0.0108 -0.0420 0.0369  140 GLY A C   
1220 O O   . GLY A 140 ? 0.1554 0.2336 0.1950 -0.0083 -0.0442 0.0357  140 GLY A O   
1221 N N   . ARG A 141 ? 0.1021 0.1675 0.1295 -0.0105 -0.0426 0.0390  141 ARG A N   
1222 C CA  . ARG A 141 ? 0.1647 0.2429 0.1879 -0.0058 -0.0466 0.0409  141 ARG A CA  
1223 C C   . ARG A 141 ? 0.1576 0.2548 0.1858 -0.0096 -0.0501 0.0340  141 ARG A C   
1224 O O   . ARG A 141 ? 0.1369 0.2481 0.1672 -0.0040 -0.0531 0.0336  141 ARG A O   
1225 C CB  . ARG A 141 ? 0.1437 0.2169 0.1567 -0.0063 -0.0458 0.0432  141 ARG A CB  
1226 C CG  . ARG A 141 ? 0.1513 0.2393 0.1574 -0.0015 -0.0503 0.0448  141 ARG A CG  
1227 C CD  . ARG A 141 ? 0.1225 0.2024 0.1170 -0.0017 -0.0482 0.0480  141 ARG A CD  
1228 N NE  . ARG A 141 ? 0.2280 0.3241 0.2139 0.0017  -0.0528 0.0481  141 ARG A NE  
1229 C CZ  . ARG A 141 ? 0.2139 0.3212 0.1970 -0.0052 -0.0548 0.0405  141 ARG A CZ  
1230 N NH1 . ARG A 141 ? 0.2297 0.3496 0.2052 -0.0012 -0.0576 0.0388  141 ARG A NH1 
1231 N NH2 . ARG A 141 ? 0.2357 0.3367 0.2237 -0.0155 -0.0514 0.0330  141 ARG A NH2 
1232 N N   . THR A 142 ? 0.1354 0.2311 0.1653 -0.0187 -0.0478 0.0275  142 THR A N   
1233 C CA  . THR A 142 ? 0.1581 0.2698 0.1925 -0.0246 -0.0490 0.0192  142 THR A CA  
1234 C C   . THR A 142 ? 0.1596 0.2791 0.2033 -0.0223 -0.0488 0.0167  142 THR A C   
1235 O O   . THR A 142 ? 0.1870 0.3215 0.2337 -0.0203 -0.0509 0.0124  142 THR A O   
1236 C CB  . THR A 142 ? 0.1375 0.2400 0.1713 -0.0346 -0.0438 0.0133  142 THR A CB  
1237 O OG1 . THR A 142 ? 0.1946 0.2893 0.2196 -0.0359 -0.0427 0.0143  142 THR A OG1 
1238 C CG2 . THR A 142 ? 0.1572 0.2725 0.1963 -0.0423 -0.0422 0.0034  142 THR A CG2 
1239 N N   . LEU A 143 ? 0.1287 0.2389 0.1769 -0.0227 -0.0463 0.0191  143 LEU A N   
1240 C CA  . LEU A 143 ? 0.1442 0.2620 0.2012 -0.0214 -0.0454 0.0165  143 LEU A CA  
1241 C C   . LEU A 143 ? 0.1787 0.3010 0.2375 -0.0106 -0.0483 0.0220  143 LEU A C   
1242 O O   . LEU A 143 ? 0.1923 0.3250 0.2588 -0.0079 -0.0483 0.0196  143 LEU A O   
1243 C CB  . LEU A 143 ? 0.1557 0.2610 0.2151 -0.0258 -0.0406 0.0162  143 LEU A CB  
1244 C CG  . LEU A 143 ? 0.1820 0.2822 0.2401 -0.0355 -0.0356 0.0105  143 LEU A CG  
1245 C CD1 . LEU A 143 ? 0.1393 0.2249 0.1965 -0.0366 -0.0303 0.0119  143 LEU A CD1 
1246 C CD2 . LEU A 143 ? 0.1578 0.2743 0.2223 -0.0412 -0.0347 0.0021  143 LEU A CD2 
1247 N N   . ARG A 144 ? 0.1402 0.2542 0.1923 -0.0042 -0.0497 0.0296  144 ARG A N   
1248 C CA  . ARG A 144 ? 0.1427 0.2588 0.1947 0.0071  -0.0510 0.0356  144 ARG A CA  
1249 C C   . ARG A 144 ? 0.2167 0.3502 0.2687 0.0118  -0.0544 0.0325  144 ARG A C   
1250 O O   . ARG A 144 ? 0.1593 0.3001 0.2153 0.0204  -0.0552 0.0346  144 ARG A O   
1251 C CB  . ARG A 144 ? 0.3458 0.4454 0.3888 0.0115  -0.0495 0.0438  144 ARG A CB  
1252 C CG  . ARG A 144 ? 0.5133 0.6032 0.5554 0.0215  -0.0467 0.0508  144 ARG A CG  
1253 C CD  . ARG A 144 ? 0.4867 0.5539 0.5203 0.0211  -0.0417 0.0555  144 ARG A CD  
1254 N NE  . ARG A 144 ? 0.3774 0.4288 0.4141 0.0154  -0.0367 0.0527  144 ARG A NE  
1255 C CZ  . ARG A 144 ? 0.3580 0.3969 0.3958 0.0198  -0.0315 0.0552  144 ARG A CZ  
1256 N NH1 . ARG A 144 ? 0.2912 0.3302 0.3272 0.0308  -0.0304 0.0615  144 ARG A NH1 
1257 N NH2 . ARG A 144 ? 0.3289 0.3560 0.3692 0.0141  -0.0272 0.0513  144 ARG A NH2 
1258 N N   . LYS A 145 ? 0.1990 0.3402 0.2474 0.0060  -0.0561 0.0270  145 LYS A N   
1259 C CA  . LYS A 145 ? 0.2318 0.3919 0.2816 0.0083  -0.0596 0.0226  145 LYS A CA  
1260 C C   . LYS A 145 ? 0.2278 0.4007 0.2895 0.0021  -0.0585 0.0139  145 LYS A C   
1261 O O   . LYS A 145 ? 0.2469 0.4340 0.3147 0.0077  -0.0604 0.0131  145 LYS A O   
1262 C CB  . LYS A 145 ? 0.2827 0.4467 0.3239 0.0040  -0.0613 0.0197  145 LYS A CB  
1263 C CG  . LYS A 145 ? 0.4078 0.5590 0.4365 0.0097  -0.0616 0.0284  145 LYS A CG  
1264 C CD  . LYS A 145 ? 0.5111 0.6679 0.5311 0.0053  -0.0631 0.0250  145 LYS A CD  
1265 C CE  . LYS A 145 ? 0.5511 0.6926 0.5589 0.0084  -0.0618 0.0332  145 LYS A CE  
1266 N NZ  . LYS A 145 ? 0.5793 0.7154 0.5801 0.0215  -0.0620 0.0434  145 LYS A NZ  
1267 N N   . ASP A 146 ? 0.2623 0.4294 0.3271 -0.0091 -0.0547 0.0079  146 ASP A N   
1268 C CA  . ASP A 146 ? 0.2849 0.4619 0.3600 -0.0161 -0.0519 -0.0003 146 ASP A CA  
1269 C C   . ASP A 146 ? 0.3002 0.4787 0.3841 -0.0113 -0.0505 0.0019  146 ASP A C   
1270 O O   . ASP A 146 ? 0.3619 0.5546 0.4548 -0.0125 -0.0498 -0.0033 146 ASP A O   
1271 C CB  . ASP A 146 ? 0.3307 0.4969 0.4053 -0.0285 -0.0462 -0.0058 146 ASP A CB  
1272 C CG  . ASP A 146 ? 0.5002 0.6647 0.5668 -0.0342 -0.0462 -0.0092 146 ASP A CG  
1273 O OD1 . ASP A 146 ? 0.5782 0.7532 0.6403 -0.0298 -0.0508 -0.0088 146 ASP A OD1 
1274 O OD2 . ASP A 146 ? 0.5503 0.7028 0.6147 -0.0429 -0.0411 -0.0122 146 ASP A OD2 
1275 N N   . LEU A 147 ? 0.2126 0.3775 0.2944 -0.0064 -0.0497 0.0091  147 LEU A N   
1276 C CA  . LEU A 147 ? 0.2316 0.3967 0.3214 -0.0026 -0.0475 0.0109  147 LEU A CA  
1277 C C   . LEU A 147 ? 0.1775 0.3444 0.2671 0.0110  -0.0500 0.0184  147 LEU A C   
1278 O O   . LEU A 147 ? 0.2135 0.3755 0.3074 0.0157  -0.0475 0.0221  147 LEU A O   
1279 C CB  . LEU A 147 ? 0.2285 0.3772 0.3166 -0.0077 -0.0435 0.0133  147 LEU A CB  
1280 C CG  . LEU A 147 ? 0.3132 0.4562 0.4001 -0.0199 -0.0394 0.0075  147 LEU A CG  
1281 C CD1 . LEU A 147 ? 0.2805 0.4031 0.3619 -0.0222 -0.0356 0.0113  147 LEU A CD1 
1282 C CD2 . LEU A 147 ? 0.3943 0.5488 0.4902 -0.0257 -0.0356 -0.0005 147 LEU A CD2 
1283 N N   . LYS A 148 ? 0.1677 0.3405 0.2515 0.0177  -0.0539 0.0211  148 LYS A N   
1284 C CA  . LYS A 148 ? 0.2037 0.3734 0.2838 0.0316  -0.0549 0.0299  148 LYS A CA  
1285 C C   . LYS A 148 ? 0.2873 0.4644 0.3777 0.0389  -0.0531 0.0305  148 LYS A C   
1286 O O   . LYS A 148 ? 0.2668 0.4326 0.3559 0.0484  -0.0503 0.0378  148 LYS A O   
1287 C CB  . LYS A 148 ? 0.2850 0.4647 0.3579 0.0369  -0.0593 0.0314  148 LYS A CB  
1288 C CG  . LYS A 148 ? 0.4129 0.5954 0.4838 0.0519  -0.0599 0.0390  148 LYS A CG  
1289 C CD  . LYS A 148 ? 0.5253 0.7159 0.5862 0.0573  -0.0638 0.0418  148 LYS A CD  
1290 C CE  . LYS A 148 ? 0.6051 0.8208 0.6715 0.0508  -0.0681 0.0323  148 LYS A CE  
1291 N NZ  . LYS A 148 ? 0.6615 0.8885 0.7182 0.0568  -0.0722 0.0348  148 LYS A NZ  
1292 N N   . ASP A 149 ? 0.2223 0.4174 0.3231 0.0345  -0.0536 0.0227  149 ASP A N   
1293 C CA  . ASP A 149 ? 0.2854 0.4901 0.3967 0.0418  -0.0517 0.0228  149 ASP A CA  
1294 C C   . ASP A 149 ? 0.2454 0.4389 0.3622 0.0402  -0.0462 0.0233  149 ASP A C   
1295 O O   . ASP A 149 ? 0.2056 0.3964 0.3263 0.0503  -0.0433 0.0277  149 ASP A O   
1296 C CB  . ASP A 149 ? 0.3376 0.5655 0.4588 0.0363  -0.0531 0.0139  149 ASP A CB  
1297 C CG  . ASP A 149 ? 0.3761 0.6188 0.4924 0.0391  -0.0586 0.0133  149 ASP A CG  
1298 O OD1 . ASP A 149 ? 0.3293 0.5704 0.4384 0.0514  -0.0611 0.0213  149 ASP A OD1 
1299 O OD2 . ASP A 149 ? 0.4050 0.6599 0.5236 0.0289  -0.0596 0.0048  149 ASP A OD2 
1300 N N   . LEU A 150 ? 0.2064 0.3929 0.3229 0.0279  -0.0439 0.0191  150 LEU A N   
1301 C CA  . LEU A 150 ? 0.2288 0.4054 0.3490 0.0262  -0.0388 0.0204  150 LEU A CA  
1302 C C   . LEU A 150 ? 0.2478 0.3987 0.3573 0.0326  -0.0365 0.0282  150 LEU A C   
1303 O O   . LEU A 150 ? 0.2394 0.3772 0.3493 0.0363  -0.0311 0.0293  150 LEU A O   
1304 C CB  . LEU A 150 ? 0.2413 0.4089 0.3583 0.0115  -0.0358 0.0145  150 LEU A CB  
1305 C CG  . LEU A 150 ? 0.2975 0.4807 0.4240 0.0020  -0.0330 0.0057  150 LEU A CG  
1306 C CD1 . LEU A 150 ? 0.2009 0.3682 0.3198 -0.0104 -0.0290 0.0028  150 LEU A CD1 
1307 C CD2 . LEU A 150 ? 0.2688 0.4583 0.4052 0.0055  -0.0281 0.0035  150 LEU A CD2 
1308 N N   . LEU A 151 ? 0.2541 0.3968 0.3537 0.0330  -0.0397 0.0327  151 LEU A N   
1309 C CA  . LEU A 151 ? 0.2816 0.4001 0.3716 0.0381  -0.0364 0.0395  151 LEU A CA  
1310 C C   . LEU A 151 ? 0.3039 0.4211 0.3958 0.0528  -0.0338 0.0459  151 LEU A C   
1311 O O   . LEU A 151 ? 0.2756 0.3723 0.3649 0.0555  -0.0271 0.0477  151 LEU A O   
1312 C CB  . LEU A 151 ? 0.3633 0.4767 0.4432 0.0365  -0.0399 0.0433  151 LEU A CB  
1313 C CG  . LEU A 151 ? 0.3611 0.4612 0.4351 0.0243  -0.0389 0.0399  151 LEU A CG  
1314 C CD1 . LEU A 151 ? 0.4869 0.5887 0.5531 0.0230  -0.0429 0.0424  151 LEU A CD1 
1315 C CD2 . LEU A 151 ? 0.2841 0.3606 0.3536 0.0231  -0.0330 0.0411  151 LEU A CD2 
1316 N N   . ASN A 152 ? 0.2720 0.4097 0.3673 0.0625  -0.0384 0.0486  152 ASN A N   
1317 C CA  . ASN A 152 ? 0.3059 0.4390 0.4001 0.0772  -0.0351 0.0546  152 ASN A CA  
1318 C C   . ASN A 152 ? 0.2862 0.4233 0.3925 0.0816  -0.0301 0.0522  152 ASN A C   
1319 O O   . ASN A 152 ? 0.3595 0.4844 0.4645 0.0932  -0.0243 0.0576  152 ASN A O   
1320 C CB  . ASN A 152 ? 0.3975 0.5471 0.4887 0.0829  -0.0406 0.0548  152 ASN A CB  
1321 C CG  . ASN A 152 ? 0.5595 0.7002 0.6363 0.0839  -0.0429 0.0601  152 ASN A CG  
1322 O OD1 . ASN A 152 ? 0.5725 0.6905 0.6407 0.0845  -0.0386 0.0659  152 ASN A OD1 
1323 N ND2 . ASN A 152 ? 0.6522 0.8110 0.7267 0.0840  -0.0490 0.0579  152 ASN A ND2 
1324 N N   . LYS A 153 ? 0.2664 0.4189 0.3834 0.0723  -0.0311 0.0440  153 LYS A N   
1325 C CA  . LYS A 153 ? 0.2690 0.4211 0.3950 0.0734  -0.0249 0.0398  153 LYS A CA  
1326 C C   . LYS A 153 ? 0.3012 0.4208 0.4192 0.0738  -0.0162 0.0417  153 LYS A C   
1327 O O   . LYS A 153 ? 0.2554 0.3678 0.3764 0.0842  -0.0099 0.0442  153 LYS A O   
1328 C CB  . LYS A 153 ? 0.3088 0.4729 0.4416 0.0589  -0.0255 0.0298  153 LYS A CB  
1329 C CG  . LYS A 153 ? 0.3845 0.5527 0.5270 0.0587  -0.0194 0.0245  153 LYS A CG  
1330 C CD  . LYS A 153 ? 0.3011 0.4769 0.4471 0.0436  -0.0186 0.0158  153 LYS A CD  
1331 C CE  . LYS A 153 ? 0.2899 0.4687 0.4442 0.0431  -0.0114 0.0107  153 LYS A CE  
1332 N NZ  . LYS A 153 ? 0.4301 0.6137 0.5862 0.0289  -0.0089 0.0031  153 LYS A NZ  
1333 N N   . GLY A 154 ? 0.2886 0.3892 0.3970 0.0624  -0.0153 0.0398  154 GLY A N   
1334 C CA  . GLY A 154 ? 0.2537 0.3258 0.3543 0.0610  -0.0077 0.0402  154 GLY A CA  
1335 C C   . GLY A 154 ? 0.2408 0.3053 0.3446 0.0569  -0.0009 0.0333  154 GLY A C   
1336 O O   . GLY A 154 ? 0.3023 0.3447 0.3997 0.0541  0.0056  0.0316  154 GLY A O   
1337 N N   . ARG A 155 ? 0.2235 0.3059 0.3366 0.0558  -0.0014 0.0285  155 ARG A N   
1338 C CA  . ARG A 155 ? 0.2147 0.2908 0.3304 0.0534  0.0060  0.0224  155 ARG A CA  
1339 C C   . ARG A 155 ? 0.1594 0.2585 0.2850 0.0497  0.0043  0.0173  155 ARG A C   
1340 O O   . ARG A 155 ? 0.2374 0.3576 0.3695 0.0503  -0.0019 0.0183  155 ARG A O   
1341 C CB  . ARG A 155 ? 0.2319 0.2971 0.3501 0.0660  0.0139  0.0252  155 ARG A CB  
1342 C CG  . ARG A 155 ? 0.3510 0.4371 0.4799 0.0805  0.0114  0.0308  155 ARG A CG  
1343 C CD  . ARG A 155 ? 0.4380 0.5117 0.5687 0.0955  0.0202  0.0352  155 ARG A CD  
1344 N NE  . ARG A 155 ? 0.4812 0.5271 0.6004 0.0991  0.0249  0.0411  155 ARG A NE  
1345 C CZ  . ARG A 155 ? 0.4393 0.4572 0.5519 0.0957  0.0351  0.0378  155 ARG A CZ  
1346 N NH1 . ARG A 155 ? 0.5042 0.4972 0.6070 0.0980  0.0404  0.0428  155 ARG A NH1 
1347 N NH2 . ARG A 155 ? 0.3516 0.3664 0.4671 0.0893  0.0408  0.0287  155 ARG A NH2 
1348 N N   . ASN A 156 ? 0.1723 0.2672 0.2985 0.0452  0.0105  0.0111  156 ASN A N   
1349 C CA  . ASN A 156 ? 0.1859 0.3004 0.3221 0.0425  0.0120  0.0061  156 ASN A CA  
1350 C C   . ASN A 156 ? 0.2214 0.3478 0.3571 0.0316  0.0068  0.0039  156 ASN A C   
1351 O O   . ASN A 156 ? 0.1765 0.3252 0.3233 0.0307  0.0052  0.0015  156 ASN A O   
1352 C CB  . ASN A 156 ? 0.2225 0.3572 0.3734 0.0550  0.0121  0.0081  156 ASN A CB  
1353 C CG  . ASN A 156 ? 0.3247 0.4458 0.4762 0.0672  0.0193  0.0106  156 ASN A CG  
1354 O OD1 . ASN A 156 ? 0.3159 0.4185 0.4614 0.0639  0.0268  0.0065  156 ASN A OD1 
1355 N ND2 . ASN A 156 ? 0.3790 0.5089 0.5369 0.0818  0.0175  0.0173  156 ASN A ND2 
1356 N N   . TYR A 157 ? 0.1618 0.2737 0.2853 0.0231  0.0049  0.0042  157 TYR A N   
1357 C CA  . TYR A 157 ? 0.1587 0.2771 0.2800 0.0133  0.0017  0.0026  157 TYR A CA  
1358 C C   . TYR A 157 ? 0.1851 0.3046 0.3056 0.0057  0.0080  -0.0027 157 TYR A C   
1359 O O   . TYR A 157 ? 0.1643 0.2739 0.2801 0.0060  0.0136  -0.0049 157 TYR A O   
1360 C CB  . TYR A 157 ? 0.1599 0.2626 0.2683 0.0088  -0.0021 0.0056  157 TYR A CB  
1361 C CG  . TYR A 157 ? 0.1525 0.2545 0.2608 0.0149  -0.0076 0.0110  157 TYR A CG  
1362 C CD1 . TYR A 157 ? 0.1714 0.2887 0.2844 0.0150  -0.0132 0.0125  157 TYR A CD1 
1363 C CD2 . TYR A 157 ? 0.1262 0.2121 0.2290 0.0200  -0.0063 0.0141  157 TYR A CD2 
1364 C CE1 . TYR A 157 ? 0.1791 0.2959 0.2900 0.0213  -0.0180 0.0180  157 TYR A CE1 
1365 C CE2 . TYR A 157 ? 0.1792 0.2623 0.2803 0.0259  -0.0098 0.0199  157 TYR A CE2 
1366 C CZ  . TYR A 157 ? 0.2216 0.3203 0.3260 0.0271  -0.0160 0.0224  157 TYR A CZ  
1367 O OH  . TYR A 157 ? 0.1992 0.2950 0.2999 0.0335  -0.0192 0.0287  157 TYR A OH  
1368 N N   . THR A 158 ? 0.0905 0.2220 0.2152 -0.0013 0.0080  -0.0052 158 THR A N   
1369 C CA  . THR A 158 ? 0.1009 0.2317 0.2236 -0.0092 0.0153  -0.0094 158 THR A CA  
1370 C C   . THR A 158 ? 0.1160 0.2325 0.2247 -0.0169 0.0153  -0.0075 158 THR A C   
1371 O O   . THR A 158 ? 0.1314 0.2434 0.2355 -0.0173 0.0093  -0.0043 158 THR A O   
1372 C CB  . THR A 158 ? 0.0916 0.2448 0.2296 -0.0128 0.0180  -0.0144 158 THR A CB  
1373 O OG1 . THR A 158 ? 0.0861 0.2478 0.2267 -0.0176 0.0128  -0.0146 158 THR A OG1 
1374 C CG2 . THR A 158 ? 0.0919 0.2630 0.2452 -0.0032 0.0175  -0.0158 158 THR A CG2 
1375 N N   . GLN A 159 ? 0.1137 0.2233 0.2152 -0.0223 0.0228  -0.0093 159 GLN A N   
1376 C CA  . GLN A 159 ? 0.1491 0.2447 0.2362 -0.0277 0.0242  -0.0065 159 GLN A CA  
1377 C C   . GLN A 159 ? 0.1543 0.2551 0.2459 -0.0336 0.0229  -0.0069 159 GLN A C   
1378 O O   . GLN A 159 ? 0.1300 0.2210 0.2128 -0.0349 0.0196  -0.0034 159 GLN A O   
1379 C CB  . GLN A 159 ? 0.1433 0.2314 0.2215 -0.0312 0.0339  -0.0076 159 GLN A CB  
1380 C CG  . GLN A 159 ? 0.1424 0.2153 0.2043 -0.0350 0.0372  -0.0035 159 GLN A CG  
1381 C CD  . GLN A 159 ? 0.1829 0.2447 0.2308 -0.0302 0.0309  0.0011  159 GLN A CD  
1382 O OE1 . GLN A 159 ? 0.2127 0.2750 0.2595 -0.0256 0.0271  0.0000  159 GLN A OE1 
1383 N NE2 . GLN A 159 ? 0.1751 0.2273 0.2126 -0.0315 0.0307  0.0056  159 GLN A NE2 
1384 N N   . GLU A 160 ? 0.1144 0.2323 0.2206 -0.0375 0.0257  -0.0122 160 GLU A N   
1385 C CA  . GLU A 160 ? 0.1384 0.2638 0.2501 -0.0446 0.0251  -0.0149 160 GLU A CA  
1386 C C   . GLU A 160 ? 0.1350 0.2643 0.2476 -0.0404 0.0145  -0.0122 160 GLU A C   
1387 O O   . GLU A 160 ? 0.1189 0.2422 0.2262 -0.0450 0.0133  -0.0115 160 GLU A O   
1388 C CB  . GLU A 160 ? 0.1491 0.2974 0.2787 -0.0495 0.0294  -0.0229 160 GLU A CB  
1389 C CG  . GLU A 160 ? 0.2420 0.4055 0.3810 -0.0565 0.0269  -0.0282 160 GLU A CG  
1390 C CD  . GLU A 160 ? 0.5072 0.6524 0.6349 -0.0660 0.0333  -0.0284 160 GLU A CD  
1391 O OE1 . GLU A 160 ? 0.5507 0.6785 0.6687 -0.0697 0.0434  -0.0266 160 GLU A OE1 
1392 O OE2 . GLU A 160 ? 0.6712 0.8166 0.7971 -0.0680 0.0284  -0.0293 160 GLU A OE2 
1393 N N   . GLU A 161 ? 0.0832 0.2214 0.2020 -0.0314 0.0078  -0.0104 161 GLU A N   
1394 C CA  . GLU A 161 ? 0.0830 0.2230 0.2007 -0.0266 -0.0012 -0.0068 161 GLU A CA  
1395 C C   . GLU A 161 ? 0.1331 0.2514 0.2355 -0.0263 -0.0031 -0.0014 161 GLU A C   
1396 O O   . GLU A 161 ? 0.1125 0.2284 0.2111 -0.0280 -0.0072 0.0003  161 GLU A O   
1397 C CB  . GLU A 161 ? 0.1037 0.2533 0.2289 -0.0155 -0.0057 -0.0046 161 GLU A CB  
1398 C CG  . GLU A 161 ? 0.0751 0.2521 0.2170 -0.0137 -0.0065 -0.0094 161 GLU A CG  
1399 C CD  . GLU A 161 ? 0.1616 0.3464 0.3106 -0.0008 -0.0085 -0.0065 161 GLU A CD  
1400 O OE1 . GLU A 161 ? 0.1167 0.2831 0.2580 0.0050  -0.0069 -0.0021 161 GLU A OE1 
1401 O OE2 . GLU A 161 ? 0.1914 0.4014 0.3541 0.0038  -0.0111 -0.0089 161 GLU A OE2 
1402 N N   . LYS A 162 ? 0.0820 0.1861 0.1758 -0.0244 0.0000  0.0007  162 LYS A N   
1403 C CA  . LYS A 162 ? 0.0829 0.1703 0.1633 -0.0242 -0.0018 0.0048  162 LYS A CA  
1404 C C   . LYS A 162 ? 0.0955 0.1760 0.1689 -0.0308 0.0010  0.0053  162 LYS A C   
1405 O O   . LYS A 162 ? 0.1021 0.1762 0.1698 -0.0308 -0.0027 0.0082  162 LYS A O   
1406 C CB  . LYS A 162 ? 0.0882 0.1661 0.1610 -0.0218 0.0015  0.0050  162 LYS A CB  
1407 C CG  . LYS A 162 ? 0.1522 0.2176 0.2126 -0.0211 -0.0010 0.0081  162 LYS A CG  
1408 C CD  . LYS A 162 ? 0.1908 0.2512 0.2446 -0.0190 0.0018  0.0064  162 LYS A CD  
1409 C CE  . LYS A 162 ? 0.1743 0.2337 0.2230 -0.0216 0.0090  0.0053  162 LYS A CE  
1410 N NZ  . LYS A 162 ? 0.1748 0.2296 0.2134 -0.0198 0.0115  0.0037  162 LYS A NZ  
1411 N N   . GLU A 163 ? 0.0991 0.1795 0.1727 -0.0362 0.0088  0.0026  163 GLU A N   
1412 C CA  . GLU A 163 ? 0.0987 0.1690 0.1648 -0.0422 0.0141  0.0034  163 GLU A CA  
1413 C C   . GLU A 163 ? 0.1835 0.2613 0.2564 -0.0469 0.0114  0.0005  163 GLU A C   
1414 O O   . GLU A 163 ? 0.1685 0.2356 0.2339 -0.0494 0.0127  0.0024  163 GLU A O   
1415 C CB  . GLU A 163 ? 0.1645 0.2315 0.2293 -0.0474 0.0251  0.0009  163 GLU A CB  
1416 C CG  . GLU A 163 ? 0.3066 0.3624 0.3590 -0.0430 0.0289  0.0048  163 GLU A CG  
1417 C CD  . GLU A 163 ? 0.4217 0.4747 0.4725 -0.0476 0.0407  0.0026  163 GLU A CD  
1418 O OE1 . GLU A 163 ? 0.4568 0.5157 0.5170 -0.0554 0.0468  -0.0024 163 GLU A OE1 
1419 O OE2 . GLU A 163 ? 0.4772 0.5228 0.5172 -0.0440 0.0443  0.0053  163 GLU A OE2 
1420 N N   . TYR A 164 ? 0.1186 0.2157 0.2052 -0.0474 0.0078  -0.0042 164 TYR A N   
1421 C CA  . TYR A 164 ? 0.0906 0.1988 0.1831 -0.0510 0.0036  -0.0076 164 TYR A CA  
1422 C C   . TYR A 164 ? 0.1421 0.2429 0.2271 -0.0459 -0.0039 -0.0022 164 TYR A C   
1423 O O   . TYR A 164 ? 0.1375 0.2338 0.2185 -0.0501 -0.0040 -0.0029 164 TYR A O   
1424 C CB  . TYR A 164 ? 0.1314 0.2653 0.2394 -0.0495 -0.0005 -0.0126 164 TYR A CB  
1425 C CG  . TYR A 164 ? 0.1256 0.2736 0.2384 -0.0524 -0.0054 -0.0168 164 TYR A CG  
1426 C CD1 . TYR A 164 ? 0.2362 0.3816 0.3481 -0.0612 0.0003  -0.0231 164 TYR A CD1 
1427 C CD2 . TYR A 164 ? 0.2198 0.3760 0.3329 -0.0439 -0.0150 -0.0134 164 TYR A CD2 
1428 C CE1 . TYR A 164 ? 0.3193 0.4731 0.4314 -0.0624 -0.0040 -0.0272 164 TYR A CE1 
1429 C CE2 . TYR A 164 ? 0.2919 0.4555 0.4041 -0.0445 -0.0191 -0.0166 164 TYR A CE2 
1430 C CZ  . TYR A 164 ? 0.3408 0.5044 0.4529 -0.0541 -0.0139 -0.0239 164 TYR A CZ  
1431 O OH  . TYR A 164 ? 0.4243 0.5970 0.5352 -0.0555 -0.0176 -0.0281 164 TYR A OH  
1432 N N   . VAL A 165 ? 0.1176 0.2166 0.2010 -0.0374 -0.0094 0.0025  165 VAL A N   
1433 C CA  . VAL A 165 ? 0.1082 0.1995 0.1849 -0.0331 -0.0152 0.0074  165 VAL A CA  
1434 C C   . VAL A 165 ? 0.1632 0.2374 0.2286 -0.0356 -0.0122 0.0102  165 VAL A C   
1435 O O   . VAL A 165 ? 0.1506 0.2205 0.2119 -0.0366 -0.0143 0.0115  165 VAL A O   
1436 C CB  . VAL A 165 ? 0.1648 0.2545 0.2418 -0.0249 -0.0188 0.0110  165 VAL A CB  
1437 C CG1 . VAL A 165 ? 0.1627 0.2421 0.2324 -0.0219 -0.0228 0.0155  165 VAL A CG1 
1438 C CG2 . VAL A 165 ? 0.1384 0.2444 0.2259 -0.0199 -0.0217 0.0099  165 VAL A CG2 
1439 N N   . LEU A 166 ? 0.1622 0.2270 0.2218 -0.0355 -0.0071 0.0114  166 LEU A N   
1440 C CA  . LEU A 166 ? 0.1463 0.1965 0.1945 -0.0355 -0.0041 0.0150  166 LEU A CA  
1441 C C   . LEU A 166 ? 0.1468 0.1920 0.1931 -0.0414 0.0007  0.0135  166 LEU A C   
1442 O O   . LEU A 166 ? 0.1684 0.2047 0.2081 -0.0404 0.0003  0.0165  166 LEU A O   
1443 C CB  . LEU A 166 ? 0.1848 0.2280 0.2260 -0.0339 0.0013  0.0165  166 LEU A CB  
1444 C CG  . LEU A 166 ? 0.2915 0.3346 0.3292 -0.0282 -0.0026 0.0182  166 LEU A CG  
1445 C CD1 . LEU A 166 ? 0.3498 0.3894 0.3809 -0.0274 0.0032  0.0183  166 LEU A CD1 
1446 C CD2 . LEU A 166 ? 0.2567 0.2946 0.2875 -0.0247 -0.0071 0.0217  166 LEU A CD2 
1447 N N   . ASN A 167 ? 0.1123 0.1631 0.1648 -0.0480 0.0062  0.0083  167 ASN A N   
1448 C CA  . ASN A 167 ? 0.1882 0.2325 0.2389 -0.0553 0.0128  0.0052  167 ASN A CA  
1449 C C   . ASN A 167 ? 0.1905 0.2412 0.2439 -0.0566 0.0066  0.0033  167 ASN A C   
1450 O O   . ASN A 167 ? 0.2000 0.2394 0.2470 -0.0587 0.0099  0.0039  167 ASN A O   
1451 C CB  . ASN A 167 ? 0.2066 0.2576 0.2651 -0.0640 0.0207  -0.0020 167 ASN A CB  
1452 C CG  . ASN A 167 ? 0.4646 0.5025 0.5162 -0.0643 0.0308  0.0005  167 ASN A CG  
1453 O OD1 . ASN A 167 ? 0.5805 0.6006 0.6189 -0.0597 0.0344  0.0073  167 ASN A OD1 
1454 N ND2 . ASN A 167 ? 0.4677 0.5153 0.5279 -0.0692 0.0358  -0.0048 167 ASN A ND2 
1455 N N   . LYS A 168 ? 0.1341 0.2021 0.1960 -0.0544 -0.0018 0.0014  168 LYS A N   
1456 C CA  . LYS A 168 ? 0.1015 0.1759 0.1639 -0.0544 -0.0078 0.0004  168 LYS A CA  
1457 C C   . LYS A 168 ? 0.1362 0.1974 0.1894 -0.0487 -0.0108 0.0071  168 LYS A C   
1458 O O   . LYS A 168 ? 0.1261 0.1838 0.1756 -0.0506 -0.0113 0.0066  168 LYS A O   
1459 C CB  . LYS A 168 ? 0.1175 0.2124 0.1886 -0.0505 -0.0159 -0.0009 168 LYS A CB  
1460 C CG  . LYS A 168 ? 0.1248 0.2389 0.2075 -0.0557 -0.0142 -0.0086 168 LYS A CG  
1461 C CD  . LYS A 168 ? 0.2537 0.3697 0.3361 -0.0635 -0.0105 -0.0164 168 LYS A CD  
1462 C CE  . LYS A 168 ? 0.4111 0.5379 0.4922 -0.0600 -0.0181 -0.0176 168 LYS A CE  
1463 N NZ  . LYS A 168 ? 0.5209 0.6513 0.6016 -0.0679 -0.0142 -0.0264 168 LYS A NZ  
1464 N N   . TYR A 169 ? 0.1005 0.1558 0.1507 -0.0423 -0.0125 0.0124  169 TYR A N   
1465 C CA  . TYR A 169 ? 0.1236 0.1693 0.1668 -0.0376 -0.0150 0.0175  169 TYR A CA  
1466 C C   . TYR A 169 ? 0.1543 0.1865 0.1898 -0.0391 -0.0090 0.0190  169 TYR A C   
1467 O O   . TYR A 169 ? 0.1436 0.1712 0.1756 -0.0382 -0.0100 0.0206  169 TYR A O   
1468 C CB  . TYR A 169 ? 0.1143 0.1584 0.1565 -0.0320 -0.0172 0.0207  169 TYR A CB  
1469 C CG  . TYR A 169 ? 0.0802 0.1318 0.1276 -0.0283 -0.0228 0.0211  169 TYR A CG  
1470 C CD1 . TYR A 169 ? 0.1116 0.1733 0.1645 -0.0284 -0.0259 0.0197  169 TYR A CD1 
1471 C CD2 . TYR A 169 ? 0.1220 0.1705 0.1682 -0.0244 -0.0242 0.0228  169 TYR A CD2 
1472 C CE1 . TYR A 169 ? 0.1299 0.1958 0.1860 -0.0232 -0.0296 0.0216  169 TYR A CE1 
1473 C CE2 . TYR A 169 ? 0.1263 0.1776 0.1764 -0.0210 -0.0270 0.0233  169 TYR A CE2 
1474 C CZ  . TYR A 169 ? 0.1015 0.1602 0.1561 -0.0197 -0.0293 0.0236  169 TYR A CZ  
1475 O OH  . TYR A 169 ? 0.1225 0.1816 0.1794 -0.0146 -0.0308 0.0255  169 TYR A OH  
1476 N N   . PHE A 170 ? 0.1316 0.1565 0.1639 -0.0411 -0.0016 0.0188  170 PHE A N   
1477 C CA  . PHE A 170 ? 0.1443 0.1541 0.1682 -0.0411 0.0058  0.0213  170 PHE A CA  
1478 C C   . PHE A 170 ? 0.1932 0.2002 0.2182 -0.0481 0.0098  0.0164  170 PHE A C   
1479 O O   . PHE A 170 ? 0.1749 0.1701 0.1935 -0.0466 0.0137  0.0187  170 PHE A O   
1480 C CB  . PHE A 170 ? 0.1702 0.1703 0.1882 -0.0406 0.0142  0.0234  170 PHE A CB  
1481 C CG  . PHE A 170 ? 0.2425 0.2409 0.2538 -0.0319 0.0114  0.0295  170 PHE A CG  
1482 C CD1 . PHE A 170 ? 0.2727 0.2629 0.2754 -0.0250 0.0120  0.0353  170 PHE A CD1 
1483 C CD2 . PHE A 170 ? 0.2867 0.2937 0.3008 -0.0304 0.0077  0.0288  170 PHE A CD2 
1484 C CE1 . PHE A 170 ? 0.2630 0.2561 0.2598 -0.0171 0.0084  0.0398  170 PHE A CE1 
1485 C CE2 . PHE A 170 ? 0.3272 0.3347 0.3348 -0.0234 0.0049  0.0328  170 PHE A CE2 
1486 C CZ  . PHE A 170 ? 0.3094 0.3113 0.3084 -0.0169 0.0048  0.0380  170 PHE A CZ  
1487 N N   . GLU A 171 ? 0.1543 0.1734 0.1874 -0.0553 0.0090  0.0093  171 GLU A N   
1488 C CA  . GLU A 171 ? 0.1948 0.2148 0.2290 -0.0626 0.0115  0.0030  171 GLU A CA  
1489 C C   . GLU A 171 ? 0.1887 0.2098 0.2200 -0.0586 0.0050  0.0055  171 GLU A C   
1490 O O   . GLU A 171 ? 0.1788 0.1910 0.2056 -0.0613 0.0094  0.0038  171 GLU A O   
1491 C CB  . GLU A 171 ? 0.2329 0.2722 0.2773 -0.0703 0.0095  -0.0059 171 GLU A CB  
1492 C CG  . GLU A 171 ? 0.3916 0.4308 0.4405 -0.0775 0.0183  -0.0112 171 GLU A CG  
1493 C CD  . GLU A 171 ? 0.4984 0.5603 0.5581 -0.0822 0.0147  -0.0203 171 GLU A CD  
1494 O OE1 . GLU A 171 ? 0.5017 0.5793 0.5645 -0.0794 0.0052  -0.0217 171 GLU A OE1 
1495 O OE2 . GLU A 171 ? 0.5638 0.6265 0.6271 -0.0863 0.0212  -0.0253 171 GLU A OE2 
1496 N N   . ILE A 172 ? 0.1116 0.1426 0.1455 -0.0525 -0.0044 0.0092  172 ILE A N   
1497 C CA  . ILE A 172 ? 0.1369 0.1682 0.1680 -0.0487 -0.0096 0.0120  172 ILE A CA  
1498 C C   . ILE A 172 ? 0.1781 0.1945 0.2024 -0.0445 -0.0057 0.0169  172 ILE A C   
1499 O O   . ILE A 172 ? 0.1708 0.1824 0.1917 -0.0449 -0.0044 0.0167  172 ILE A O   
1500 C CB  . ILE A 172 ? 0.1625 0.2037 0.1971 -0.0429 -0.0180 0.0156  172 ILE A CB  
1501 C CG1 . ILE A 172 ? 0.1802 0.2379 0.2207 -0.0447 -0.0225 0.0117  172 ILE A CG1 
1502 C CG2 . ILE A 172 ? 0.2245 0.2619 0.2554 -0.0387 -0.0212 0.0196  172 ILE A CG2 
1503 C CD1 . ILE A 172 ? 0.1359 0.2009 0.1745 -0.0482 -0.0244 0.0079  172 ILE A CD1 
1504 N N   . ILE A 173 ? 0.1194 0.1298 0.1416 -0.0397 -0.0040 0.0214  173 ILE A N   
1505 C CA  . ILE A 173 ? 0.1056 0.1055 0.1217 -0.0338 -0.0010 0.0265  173 ILE A CA  
1506 C C   . ILE A 173 ? 0.2141 0.2001 0.2248 -0.0365 0.0086  0.0253  173 ILE A C   
1507 O O   . ILE A 173 ? 0.1710 0.1503 0.1782 -0.0331 0.0108  0.0275  173 ILE A O   
1508 C CB  . ILE A 173 ? 0.1731 0.1718 0.1865 -0.0277 -0.0011 0.0311  173 ILE A CB  
1509 C CG1 . ILE A 173 ? 0.1414 0.1522 0.1600 -0.0258 -0.0094 0.0311  173 ILE A CG1 
1510 C CG2 . ILE A 173 ? 0.1650 0.1563 0.1720 -0.0201 0.0015  0.0366  173 ILE A CG2 
1511 C CD1 . ILE A 173 ? 0.1979 0.2099 0.2137 -0.0209 -0.0100 0.0338  173 ILE A CD1 
1512 N N   . LYS A 174 ? 0.1596 0.1403 0.1701 -0.0429 0.0158  0.0213  174 LYS A N   
1513 C CA  . LYS A 174 ? 0.1452 0.1091 0.1500 -0.0464 0.0275  0.0195  174 LYS A CA  
1514 C C   . LYS A 174 ? 0.1871 0.1518 0.1928 -0.0517 0.0278  0.0138  174 LYS A C   
1515 O O   . LYS A 174 ? 0.2136 0.1624 0.2136 -0.0523 0.0372  0.0133  174 LYS A O   
1516 C CB  . LYS A 174 ? 0.2247 0.1832 0.2303 -0.0544 0.0364  0.0147  174 LYS A CB  
1517 C CG  . LYS A 174 ? 0.3271 0.2782 0.3278 -0.0488 0.0403  0.0211  174 LYS A CG  
1518 C CD  . LYS A 174 ? 0.4416 0.3891 0.4444 -0.0581 0.0495  0.0155  174 LYS A CD  
1519 C CE  . LYS A 174 ? 0.5342 0.4733 0.5303 -0.0523 0.0544  0.0223  174 LYS A CE  
1520 N NZ  . LYS A 174 ? 0.6942 0.6093 0.6769 -0.0452 0.0657  0.0302  174 LYS A NZ  
1521 N N   . LYS A 175 ? 0.1702 0.1518 0.1815 -0.0550 0.0186  0.0098  175 LYS A N   
1522 C CA  . LYS A 175 ? 0.2171 0.2009 0.2275 -0.0598 0.0185  0.0043  175 LYS A CA  
1523 C C   . LYS A 175 ? 0.1818 0.1675 0.1904 -0.0528 0.0128  0.0094  175 LYS A C   
1524 O O   . LYS A 175 ? 0.1985 0.1873 0.2055 -0.0559 0.0119  0.0056  175 LYS A O   
1525 C CB  . LYS A 175 ? 0.2459 0.2485 0.2620 -0.0674 0.0128  -0.0036 175 LYS A CB  
1526 C CG  . LYS A 175 ? 0.3844 0.3931 0.4061 -0.0736 0.0153  -0.0086 175 LYS A CG  
1527 C CD  . LYS A 175 ? 0.5586 0.5857 0.5854 -0.0829 0.0127  -0.0192 175 LYS A CD  
1528 C CE  . LYS A 175 ? 0.6422 0.6874 0.6699 -0.0784 0.0006  -0.0176 175 LYS A CE  
1529 N NZ  . LYS A 175 ? 0.7219 0.7687 0.7507 -0.0678 -0.0069 -0.0075 175 LYS A NZ  
1530 N N   . THR A 176 ? 0.1723 0.1570 0.1810 -0.0440 0.0094  0.0171  176 THR A N   
1531 C CA  . THR A 176 ? 0.1726 0.1626 0.1819 -0.0388 0.0037  0.0206  176 THR A CA  
1532 C C   . THR A 176 ? 0.1899 0.1696 0.1950 -0.0368 0.0098  0.0210  176 THR A C   
1533 O O   . THR A 176 ? 0.1730 0.1563 0.1774 -0.0387 0.0081  0.0189  176 THR A O   
1534 C CB  . THR A 176 ? 0.2026 0.1973 0.2145 -0.0316 -0.0015 0.0265  176 THR A CB  
1535 O OG1 . THR A 176 ? 0.2052 0.2097 0.2214 -0.0338 -0.0072 0.0253  176 THR A OG1 
1536 C CG2 . THR A 176 ? 0.1852 0.1848 0.1989 -0.0274 -0.0055 0.0291  176 THR A CG2 
1537 N N   . LEU A 177 ? 0.1773 0.1438 0.1787 -0.0322 0.0176  0.0242  177 LEU A N   
1538 C CA  . LEU A 177 ? 0.2325 0.1895 0.2305 -0.0292 0.0240  0.0247  177 LEU A CA  
1539 C C   . LEU A 177 ? 0.2086 0.1597 0.2035 -0.0386 0.0298  0.0165  177 LEU A C   
1540 O O   . LEU A 177 ? 0.2080 0.1578 0.2013 -0.0387 0.0315  0.0147  177 LEU A O   
1541 C CB  . LEU A 177 ? 0.2119 0.1550 0.2055 -0.0204 0.0322  0.0308  177 LEU A CB  
1542 C CG  . LEU A 177 ? 0.2742 0.2263 0.2698 -0.0103 0.0259  0.0383  177 LEU A CG  
1543 C CD1 . LEU A 177 ? 0.3194 0.2585 0.3086 0.0002  0.0344  0.0452  177 LEU A CD1 
1544 C CD2 . LEU A 177 ? 0.3147 0.2821 0.3165 -0.0070 0.0178  0.0391  177 LEU A CD2 
1545 N N   . SER A 178 ? 0.2097 0.1596 0.2044 -0.0474 0.0326  0.0104  178 SER A N   
1546 C CA  . SER A 178 ? 0.1924 0.1402 0.1846 -0.0580 0.0377  0.0004  178 SER A CA  
1547 C C   . SER A 178 ? 0.1927 0.1567 0.1856 -0.0608 0.0288  -0.0029 178 SER A C   
1548 O O   . SER A 178 ? 0.2157 0.1771 0.2044 -0.0656 0.0329  -0.0090 178 SER A O   
1549 C CB  . SER A 178 ? 0.2701 0.2194 0.2644 -0.0677 0.0410  -0.0067 178 SER A CB  
1550 O OG  . SER A 178 ? 0.3755 0.3038 0.3660 -0.0675 0.0539  -0.0056 178 SER A OG  
1551 N N   . ILE A 179 ? 0.1945 0.1742 0.1916 -0.0577 0.0177  0.0009  179 ILE A N   
1552 C CA  . ILE A 179 ? 0.1630 0.1558 0.1586 -0.0594 0.0107  -0.0011 179 ILE A CA  
1553 C C   . ILE A 179 ? 0.2352 0.2232 0.2278 -0.0542 0.0118  0.0028  179 ILE A C   
1554 O O   . ILE A 179 ? 0.1823 0.1741 0.1702 -0.0572 0.0115  -0.0008 179 ILE A O   
1555 C CB  . ILE A 179 ? 0.2211 0.2299 0.2209 -0.0572 0.0002  0.0020  179 ILE A CB  
1556 C CG1 . ILE A 179 ? 0.3658 0.3877 0.3616 -0.0596 -0.0053 -0.0011 179 ILE A CG1 
1557 C CG2 . ILE A 179 ? 0.1952 0.2031 0.1984 -0.0487 -0.0039 0.0108  179 ILE A CG2 
1558 C CD1 . ILE A 179 ? 0.3679 0.4065 0.3668 -0.0591 -0.0137 -0.0009 179 ILE A CD1 
1559 N N   . TYR A 180 ? 0.1630 0.1441 0.1583 -0.0464 0.0135  0.0096  180 TYR A N   
1560 C CA  . TYR A 180 ? 0.1660 0.1438 0.1602 -0.0420 0.0160  0.0120  180 TYR A CA  
1561 C C   . TYR A 180 ? 0.1603 0.1253 0.1491 -0.0449 0.0264  0.0069  180 TYR A C   
1562 O O   . TYR A 180 ? 0.1892 0.1540 0.1747 -0.0455 0.0285  0.0050  180 TYR A O   
1563 C CB  . TYR A 180 ? 0.1618 0.1393 0.1614 -0.0328 0.0152  0.0193  180 TYR A CB  
1564 C CG  . TYR A 180 ? 0.1879 0.1776 0.1926 -0.0308 0.0062  0.0230  180 TYR A CG  
1565 C CD1 . TYR A 180 ? 0.1861 0.1828 0.1923 -0.0305 0.0028  0.0241  180 TYR A CD1 
1566 C CD2 . TYR A 180 ? 0.1714 0.1640 0.1791 -0.0295 0.0024  0.0251  180 TYR A CD2 
1567 C CE1 . TYR A 180 ? 0.1600 0.1649 0.1705 -0.0294 -0.0035 0.0269  180 TYR A CE1 
1568 C CE2 . TYR A 180 ? 0.1258 0.1279 0.1380 -0.0280 -0.0046 0.0276  180 TYR A CE2 
1569 C CZ  . TYR A 180 ? 0.1331 0.1406 0.1468 -0.0281 -0.0072 0.0284  180 TYR A CZ  
1570 O OH  . TYR A 180 ? 0.1374 0.1515 0.1552 -0.0273 -0.0122 0.0303  180 TYR A OH  
1571 N N   . ARG A 181 ? 0.1664 0.1187 0.1534 -0.0468 0.0344  0.0044  181 ARG A N   
1572 C CA  . ARG A 181 ? 0.1844 0.1219 0.1658 -0.0506 0.0460  -0.0016 181 ARG A CA  
1573 C C   . ARG A 181 ? 0.2339 0.1786 0.2106 -0.0617 0.0450  -0.0118 181 ARG A C   
1574 O O   . ARG A 181 ? 0.2377 0.1767 0.2092 -0.0643 0.0511  -0.0167 181 ARG A O   
1575 C CB  . ARG A 181 ? 0.1985 0.1187 0.1780 -0.0517 0.0564  -0.0026 181 ARG A CB  
1576 C CG  . ARG A 181 ? 0.2432 0.1550 0.2244 -0.0393 0.0589  0.0078  181 ARG A CG  
1577 C CD  . ARG A 181 ? 0.3014 0.1917 0.2778 -0.0401 0.0720  0.0073  181 ARG A CD  
1578 N NE  . ARG A 181 ? 0.4730 0.3579 0.4493 -0.0276 0.0729  0.0182  181 ARG A NE  
1579 C CZ  . ARG A 181 ? 0.4975 0.3843 0.4743 -0.0272 0.0703  0.0215  181 ARG A CZ  
1580 N NH1 . ARG A 181 ? 0.4113 0.3051 0.3904 -0.0387 0.0671  0.0146  181 ARG A NH1 
1581 N NH2 . ARG A 181 ? 0.6404 0.5234 0.6152 -0.0147 0.0710  0.0316  181 ARG A NH2 
1582 N N   . GLU A 182 ? 0.1946 0.1532 0.1730 -0.0678 0.0374  -0.0153 182 GLU A N   
1583 C CA  . GLU A 182 ? 0.2393 0.2097 0.2133 -0.0775 0.0350  -0.0252 182 GLU A CA  
1584 C C   . GLU A 182 ? 0.2420 0.2220 0.2114 -0.0746 0.0292  -0.0231 182 GLU A C   
1585 O O   . GLU A 182 ? 0.2489 0.2278 0.2110 -0.0796 0.0335  -0.0301 182 GLU A O   
1586 C CB  . GLU A 182 ? 0.2059 0.1928 0.1843 -0.0821 0.0271  -0.0281 182 GLU A CB  
1587 C CG  . GLU A 182 ? 0.3504 0.3552 0.3249 -0.0910 0.0228  -0.0384 182 GLU A CG  
1588 C CD  . GLU A 182 ? 0.5752 0.5986 0.5559 -0.0949 0.0156  -0.0419 182 GLU A CD  
1589 O OE1 . GLU A 182 ? 0.6006 0.6208 0.5883 -0.0915 0.0149  -0.0365 182 GLU A OE1 
1590 O OE2 . GLU A 182 ? 0.6450 0.6880 0.6235 -0.1010 0.0107  -0.0503 182 GLU A OE2 
1591 N N   . ILE A 183 ? 0.2070 0.1956 0.1796 -0.0671 0.0203  -0.0139 183 ILE A N   
1592 C CA  . ILE A 183 ? 0.2013 0.1977 0.1684 -0.0651 0.0161  -0.0117 183 ILE A CA  
1593 C C   . ILE A 183 ? 0.2300 0.2143 0.1942 -0.0627 0.0244  -0.0113 183 ILE A C   
1594 O O   . ILE A 183 ? 0.2475 0.2346 0.2041 -0.0645 0.0254  -0.0137 183 ILE A O   
1595 C CB  . ILE A 183 ? 0.2057 0.2110 0.1768 -0.0583 0.0071  -0.0024 183 ILE A CB  
1596 C CG1 . ILE A 183 ? 0.2272 0.2248 0.2066 -0.0514 0.0084  0.0050  183 ILE A CG1 
1597 C CG2 . ILE A 183 ? 0.2453 0.2637 0.2185 -0.0600 -0.0007 -0.0033 183 ILE A CG2 
1598 C CD1 . ILE A 183 ? 0.2570 0.2523 0.2364 -0.0469 0.0104  0.0094  183 ILE A CD1 
1599 N N   . LYS A 184 ? 0.1842 0.1557 0.1539 -0.0582 0.0310  -0.0083 184 LYS A N   
1600 C CA  . LYS A 184 ? 0.2622 0.2230 0.2304 -0.0548 0.0398  -0.0082 184 LYS A CA  
1601 C C   . LYS A 184 ? 0.3327 0.2847 0.2925 -0.0626 0.0490  -0.0185 184 LYS A C   
1602 O O   . LYS A 184 ? 0.3106 0.2620 0.2645 -0.0637 0.0526  -0.0214 184 LYS A O   
1603 C CB  . LYS A 184 ? 0.2836 0.2346 0.2592 -0.0464 0.0443  -0.0021 184 LYS A CB  
1604 C CG  . LYS A 184 ? 0.3077 0.2506 0.2843 -0.0401 0.0526  -0.0004 184 LYS A CG  
1605 C CD  . LYS A 184 ? 0.3336 0.2718 0.3175 -0.0296 0.0547  0.0070  184 LYS A CD  
1606 C CE  . LYS A 184 ? 0.4003 0.3351 0.3872 -0.0213 0.0617  0.0095  184 LYS A CE  
1607 N NZ  . LYS A 184 ? 0.5549 0.4729 0.5344 -0.0244 0.0742  0.0031  184 LYS A NZ  
1608 N N   . GLU A 185 ? 0.2538 0.1983 0.2127 -0.0687 0.0540  -0.0250 185 GLU A N   
1609 C CA  . GLU A 185 ? 0.2903 0.2247 0.2418 -0.0772 0.0646  -0.0365 185 GLU A CA  
1610 C C   . GLU A 185 ? 0.3220 0.2726 0.2654 -0.0863 0.0589  -0.0452 185 GLU A C   
1611 O O   . GLU A 185 ? 0.3140 0.2597 0.2493 -0.0928 0.0665  -0.0548 185 GLU A O   
1612 C CB  . GLU A 185 ? 0.4104 0.3307 0.3632 -0.0826 0.0736  -0.0420 185 GLU A CB  
1613 C CG  . GLU A 185 ? 0.4750 0.4073 0.4265 -0.0952 0.0700  -0.0527 185 GLU A CG  
1614 C CD  . GLU A 185 ? 0.5625 0.4789 0.5161 -0.1015 0.0811  -0.0584 185 GLU A CD  
1615 O OE1 . GLU A 185 ? 0.6117 0.5176 0.5702 -0.0938 0.0830  -0.0491 185 GLU A OE1 
1616 O OE2 . GLU A 185 ? 0.5576 0.4720 0.5073 -0.1144 0.0884  -0.0725 185 GLU A OE2 
1617 N N   . GLU A 186 ? 0.2640 0.1715 0.2097 -0.1145 -0.0369 -0.0125 186 GLU A N   
1618 C CA  . GLU A 186 ? 0.3112 0.2213 0.2472 -0.1192 -0.0410 -0.0127 186 GLU A CA  
1619 C C   . GLU A 186 ? 0.3322 0.2406 0.2555 -0.1187 -0.0382 -0.0168 186 GLU A C   
1620 O O   . GLU A 186 ? 0.3521 0.2622 0.2658 -0.1227 -0.0412 -0.0170 186 GLU A O   
1621 C CB  . GLU A 186 ? 0.3134 0.2348 0.2547 -0.1201 -0.0449 -0.0040 186 GLU A CB  
1622 C CG  . GLU A 186 ? 0.3183 0.2429 0.2694 -0.1231 -0.0492 0.0002  186 GLU A CG  
1623 C CD  . GLU A 186 ? 0.4170 0.3539 0.3735 -0.1236 -0.0529 0.0087  186 GLU A CD  
1624 O OE1 . GLU A 186 ? 0.3944 0.3371 0.3521 -0.1196 -0.0509 0.0121  186 GLU A OE1 
1625 O OE2 . GLU A 186 ? 0.4038 0.3445 0.3633 -0.1281 -0.0580 0.0118  186 GLU A OE2 
1626 N N   . GLY A 187 ? 0.3052 0.2110 0.2283 -0.1142 -0.0325 -0.0197 187 GLY A N   
1627 C CA  . GLY A 187 ? 0.3193 0.2247 0.2310 -0.1140 -0.0293 -0.0229 187 GLY A CA  
1628 C C   . GLY A 187 ? 0.3242 0.2383 0.2337 -0.1143 -0.0307 -0.0166 187 GLY A C   
1629 O O   . GLY A 187 ? 0.3075 0.2219 0.2061 -0.1163 -0.0297 -0.0181 187 GLY A O   
1630 N N   . LYS A 188 ? 0.2504 0.1714 0.1700 -0.1125 -0.0330 -0.0094 188 LYS A N   
1631 C CA  . LYS A 188 ? 0.2429 0.1714 0.1615 -0.1122 -0.0349 -0.0034 188 LYS A CA  
1632 C C   . LYS A 188 ? 0.2519 0.1820 0.1732 -0.1072 -0.0301 -0.0028 188 LYS A C   
1633 O O   . LYS A 188 ? 0.2502 0.1845 0.1691 -0.1069 -0.0310 0.0010  188 LYS A O   
1634 C CB  . LYS A 188 ? 0.2666 0.2026 0.1949 -0.1125 -0.0399 0.0037  188 LYS A CB  
1635 C CG  . LYS A 188 ? 0.3088 0.2451 0.2344 -0.1182 -0.0457 0.0044  188 LYS A CG  
1636 C CD  . LYS A 188 ? 0.3249 0.2698 0.2615 -0.1184 -0.0501 0.0118  188 LYS A CD  
1637 C CE  . LYS A 188 ? 0.3946 0.3408 0.3294 -0.1244 -0.0562 0.0129  188 LYS A CE  
1638 N NZ  . LYS A 188 ? 0.4813 0.4294 0.4057 -0.1281 -0.0600 0.0144  188 LYS A NZ  
1639 N N   . GLY A 189 ? 0.2417 0.1681 0.1681 -0.1034 -0.0255 -0.0062 189 GLY A N   
1640 C CA  . GLY A 189 ? 0.2311 0.1586 0.1594 -0.0991 -0.0209 -0.0064 189 GLY A CA  
1641 C C   . GLY A 189 ? 0.2414 0.1635 0.1738 -0.0961 -0.0163 -0.0111 189 GLY A C   
1642 O O   . GLY A 189 ? 0.2584 0.1766 0.1953 -0.0964 -0.0172 -0.0126 189 GLY A O   
1643 N N   . SER A 190 ? 0.2139 0.1353 0.1444 -0.0935 -0.0116 -0.0135 190 SER A N   
1644 C CA  . SER A 190 ? 0.2117 0.1292 0.1474 -0.0899 -0.0072 -0.0170 190 SER A CA  
1645 C C   . SER A 190 ? 0.2155 0.1382 0.1620 -0.0853 -0.0066 -0.0118 190 SER A C   
1646 O O   . SER A 190 ? 0.1944 0.1232 0.1420 -0.0843 -0.0079 -0.0074 190 SER A O   
1647 C CB  . SER A 190 ? 0.2364 0.1511 0.1644 -0.0900 -0.0020 -0.0227 190 SER A CB  
1648 O OG  . SER A 190 ? 0.2653 0.1752 0.1826 -0.0942 -0.0018 -0.0284 190 SER A OG  
1649 N N   . VAL A 191 ? 0.2319 0.1515 0.1858 -0.0825 -0.0046 -0.0125 191 VAL A N   
1650 C CA  . VAL A 191 ? 0.2385 0.1626 0.2018 -0.0782 -0.0035 -0.0081 191 VAL A CA  
1651 C C   . VAL A 191 ? 0.2136 0.1340 0.1777 -0.0754 0.0015  -0.0119 191 VAL A C   
1652 O O   . VAL A 191 ? 0.2408 0.1537 0.2045 -0.0755 0.0034  -0.0163 191 VAL A O   
1653 C CB  . VAL A 191 ? 0.2210 0.1461 0.1933 -0.0779 -0.0060 -0.0036 191 VAL A CB  
1654 C CG1 . VAL A 191 ? 0.2080 0.1388 0.1884 -0.0739 -0.0046 0.0015  191 VAL A CG1 
1655 C CG2 . VAL A 191 ? 0.1843 0.1133 0.1556 -0.0813 -0.0107 -0.0004 191 VAL A CG2 
1656 N N   . SER A 192 ? 0.1989 0.1242 0.1644 -0.0728 0.0036  -0.0103 192 SER A N   
1657 C CA  . SER A 192 ? 0.2473 0.1709 0.2147 -0.0701 0.0083  -0.0132 192 SER A CA  
1658 C C   . SER A 192 ? 0.2507 0.1775 0.2269 -0.0666 0.0085  -0.0084 192 SER A C   
1659 O O   . SER A 192 ? 0.1785 0.1096 0.1588 -0.0663 0.0053  -0.0030 192 SER A O   
1660 C CB  . SER A 192 ? 0.2058 0.1329 0.1679 -0.0707 0.0107  -0.0153 192 SER A CB  
1661 O OG  . SER A 192 ? 0.2070 0.1407 0.1710 -0.0696 0.0081  -0.0102 192 SER A OG  
1662 N N   . THR A 193 ? 0.2098 0.1378 0.1901 -0.0618 0.0121  -0.0100 193 THR A N   
1663 C CA  . THR A 193 ? 0.1785 0.1128 0.1665 -0.0567 0.0121  -0.0053 193 THR A CA  
1664 C C   . THR A 193 ? 0.1474 0.0867 0.1362 -0.0530 0.0150  -0.0074 193 THR A C   
1665 O O   . THR A 193 ? 0.1525 0.0909 0.1365 -0.0546 0.0173  -0.0119 193 THR A O   
1666 C CB  . THR A 193 ? 0.2050 0.1360 0.1998 -0.0543 0.0122  -0.0030 193 THR A CB  
1667 O OG1 . THR A 193 ? 0.2056 0.1441 0.2064 -0.0504 0.0114  0.0028  193 THR A OG1 
1668 C CG2 . THR A 193 ? 0.1725 0.0990 0.1691 -0.0509 0.0159  -0.0076 193 THR A CG2 
1669 N N   . SER A 194 ? 0.1510 0.0964 0.1456 -0.0483 0.0149  -0.0040 194 SER A N   
1670 C CA  . SER A 194 ? 0.1400 0.0909 0.1365 -0.0449 0.0170  -0.0055 194 SER A CA  
1671 C C   . SER A 194 ? 0.1585 0.1113 0.1623 -0.0395 0.0184  -0.0041 194 SER A C   
1672 O O   . SER A 194 ? 0.1657 0.1166 0.1730 -0.0384 0.0172  -0.0004 194 SER A O   
1673 C CB  . SER A 194 ? 0.1682 0.1252 0.1640 -0.0442 0.0147  -0.0029 194 SER A CB  
1674 O OG  . SER A 194 ? 0.1446 0.1000 0.1342 -0.0487 0.0130  -0.0036 194 SER A OG  
1675 N N   . PRO A 195 ? 0.1438 0.1010 0.1505 -0.0362 0.0206  -0.0062 195 PRO A N   
1676 C CA  . PRO A 195 ? 0.1377 0.0987 0.1517 -0.0306 0.0210  -0.0036 195 PRO A CA  
1677 C C   . PRO A 195 ? 0.1653 0.1303 0.1809 -0.0289 0.0181  0.0022  195 PRO A C   
1678 O O   . PRO A 195 ? 0.1741 0.1424 0.1865 -0.0303 0.0162  0.0032  195 PRO A O   
1679 C CB  . PRO A 195 ? 0.1838 0.1518 0.1996 -0.0285 0.0225  -0.0061 195 PRO A CB  
1680 C CG  . PRO A 195 ? 0.3011 0.2668 0.3118 -0.0328 0.0246  -0.0110 195 PRO A CG  
1681 C CD  . PRO A 195 ? 0.1865 0.1467 0.1904 -0.0378 0.0225  -0.0102 195 PRO A CD  
1682 N N   . TYR A 196 ? 0.1470 0.1122 0.1679 -0.0254 0.0180  0.0060  196 TYR A N   
1683 C CA  . TYR A 196 ? 0.1518 0.1180 0.1738 -0.0254 0.0159  0.0119  196 TYR A CA  
1684 C C   . TYR A 196 ? 0.1636 0.1380 0.1836 -0.0244 0.0141  0.0143  196 TYR A C   
1685 O O   . TYR A 196 ? 0.1511 0.1259 0.1690 -0.0268 0.0125  0.0164  196 TYR A O   
1686 C CB  . TYR A 196 ? 0.1278 0.0937 0.1560 -0.0215 0.0162  0.0162  196 TYR A CB  
1687 C CG  . TYR A 196 ? 0.1301 0.0948 0.1603 -0.0228 0.0146  0.0226  196 TYR A CG  
1688 C CD1 . TYR A 196 ? 0.1339 0.1067 0.1635 -0.0224 0.0132  0.0275  196 TYR A CD1 
1689 C CD2 . TYR A 196 ? 0.1526 0.1076 0.1851 -0.0250 0.0146  0.0234  196 TYR A CD2 
1690 C CE1 . TYR A 196 ? 0.1727 0.1457 0.2049 -0.0242 0.0121  0.0340  196 TYR A CE1 
1691 C CE2 . TYR A 196 ? 0.1550 0.1085 0.1899 -0.0273 0.0130  0.0297  196 TYR A CE2 
1692 C CZ  . TYR A 196 ? 0.2033 0.1666 0.2384 -0.0271 0.0118  0.0354  196 TYR A CZ  
1693 O OH  . TYR A 196 ? 0.2078 0.1712 0.2460 -0.0298 0.0105  0.0422  196 TYR A OH  
1694 N N   . TYR A 197 ? 0.1568 0.1380 0.1776 -0.0207 0.0140  0.0136  197 TYR A N   
1695 C CA  . TYR A 197 ? 0.1814 0.1697 0.1999 -0.0189 0.0121  0.0151  197 TYR A CA  
1696 C C   . TYR A 197 ? 0.1726 0.1609 0.1869 -0.0207 0.0114  0.0104  197 TYR A C   
1697 O O   . TYR A 197 ? 0.1462 0.1397 0.1589 -0.0185 0.0098  0.0099  197 TYR A O   
1698 C CB  . TYR A 197 ? 0.1582 0.1542 0.1797 -0.0136 0.0118  0.0180  197 TYR A CB  
1699 C CG  . TYR A 197 ? 0.1712 0.1678 0.1963 -0.0123 0.0120  0.0242  197 TYR A CG  
1700 C CD1 . TYR A 197 ? 0.1428 0.1424 0.1670 -0.0129 0.0113  0.0286  197 TYR A CD1 
1701 C CD2 . TYR A 197 ? 0.1458 0.1395 0.1756 -0.0106 0.0130  0.0260  197 TYR A CD2 
1702 C CE1 . TYR A 197 ? 0.1763 0.1766 0.2041 -0.0126 0.0115  0.0351  197 TYR A CE1 
1703 C CE2 . TYR A 197 ? 0.1624 0.1553 0.1957 -0.0100 0.0129  0.0324  197 TYR A CE2 
1704 C CZ  . TYR A 197 ? 0.1747 0.1710 0.2068 -0.0114 0.0122  0.0371  197 TYR A CZ  
1705 O OH  . TYR A 197 ? 0.2167 0.2127 0.2525 -0.0116 0.0120  0.0443  197 TYR A OH  
1706 N N   . HIS A 198 ? 0.1650 0.1473 0.1770 -0.0250 0.0123  0.0070  198 HIS A N   
1707 C CA  . HIS A 198 ? 0.1368 0.1182 0.1445 -0.0277 0.0114  0.0035  198 HIS A CA  
1708 C C   . HIS A 198 ? 0.1421 0.1286 0.1513 -0.0255 0.0111  0.0013  198 HIS A C   
1709 O O   . HIS A 198 ? 0.1455 0.1337 0.1521 -0.0255 0.0088  0.0003  198 HIS A O   
1710 C CB  . HIS A 198 ? 0.1222 0.1039 0.1265 -0.0282 0.0088  0.0053  198 HIS A CB  
1711 C CG  . HIS A 198 ? 0.1107 0.0884 0.1102 -0.0322 0.0074  0.0028  198 HIS A CG  
1712 N ND1 . HIS A 198 ? 0.1216 0.1005 0.1193 -0.0316 0.0056  0.0010  198 HIS A ND1 
1713 C CD2 . HIS A 198 ? 0.1296 0.1020 0.1256 -0.0369 0.0072  0.0023  198 HIS A CD2 
1714 C CE1 . HIS A 198 ? 0.1331 0.1072 0.1266 -0.0359 0.0044  0.0000  198 HIS A CE1 
1715 N NE2 . HIS A 198 ? 0.1618 0.1324 0.1540 -0.0390 0.0054  0.0009  198 HIS A NE2 
1716 N N   . PRO A 199 ? 0.1513 0.1403 0.1648 -0.0238 0.0130  0.0003  199 PRO A N   
1717 C CA  . PRO A 199 ? 0.1437 0.1384 0.1593 -0.0225 0.0124  -0.0018 199 PRO A CA  
1718 C C   . PRO A 199 ? 0.1604 0.1535 0.1742 -0.0272 0.0135  -0.0055 199 PRO A C   
1719 O O   . PRO A 199 ? 0.1659 0.1537 0.1770 -0.0307 0.0154  -0.0067 199 PRO A O   
1720 C CB  . PRO A 199 ? 0.1303 0.1288 0.1522 -0.0187 0.0142  -0.0008 199 PRO A CB  
1721 C CG  . PRO A 199 ? 0.1404 0.1319 0.1626 -0.0203 0.0170  -0.0012 199 PRO A CG  
1722 C CD  . PRO A 199 ? 0.1541 0.1403 0.1713 -0.0228 0.0156  0.0008  199 PRO A CD  
1723 N N   . LEU A 200 ? 0.1387 0.1370 0.1543 -0.0273 0.0123  -0.0071 200 LEU A N   
1724 C CA  . LEU A 200 ? 0.1238 0.1232 0.1398 -0.0316 0.0136  -0.0099 200 LEU A CA  
1725 C C   . LEU A 200 ? 0.1322 0.1365 0.1545 -0.0298 0.0173  -0.0110 200 LEU A C   
1726 O O   . LEU A 200 ? 0.1460 0.1580 0.1741 -0.0273 0.0168  -0.0111 200 LEU A O   
1727 C CB  . LEU A 200 ? 0.1864 0.1893 0.2022 -0.0330 0.0103  -0.0109 200 LEU A CB  
1728 C CG  . LEU A 200 ? 0.2127 0.2097 0.2223 -0.0345 0.0067  -0.0105 200 LEU A CG  
1729 C CD1 . LEU A 200 ? 0.1381 0.1380 0.1481 -0.0343 0.0028  -0.0119 200 LEU A CD1 
1730 C CD2 . LEU A 200 ? 0.2684 0.2588 0.2731 -0.0403 0.0073  -0.0108 200 LEU A CD2 
1731 N N   . ILE A 201 ? 0.1397 0.1396 0.1608 -0.0310 0.0208  -0.0121 201 ILE A N   
1732 C CA  . ILE A 201 ? 0.1149 0.1183 0.1420 -0.0283 0.0247  -0.0138 201 ILE A CA  
1733 C C   . ILE A 201 ? 0.1799 0.1923 0.2117 -0.0296 0.0261  -0.0157 201 ILE A C   
1734 O O   . ILE A 201 ? 0.1548 0.1743 0.1944 -0.0253 0.0272  -0.0158 201 ILE A O   
1735 C CB  . ILE A 201 ? 0.1459 0.1418 0.1694 -0.0298 0.0279  -0.0157 201 ILE A CB  
1736 C CG1 . ILE A 201 ? 0.1523 0.1407 0.1738 -0.0280 0.0263  -0.0132 201 ILE A CG1 
1737 C CG2 . ILE A 201 ? 0.1462 0.1453 0.1750 -0.0272 0.0325  -0.0188 201 ILE A CG2 
1738 C CD1 . ILE A 201 ? 0.1395 0.1290 0.1678 -0.0219 0.0264  -0.0111 201 ILE A CD1 
1739 N N   . PRO A 202 ? 0.1810 0.1943 0.2093 -0.0355 0.0261  -0.0169 202 PRO A N   
1740 C CA  . PRO A 202 ? 0.1273 0.1507 0.1614 -0.0372 0.0276  -0.0182 202 PRO A CA  
1741 C C   . PRO A 202 ? 0.1153 0.1468 0.1561 -0.0342 0.0241  -0.0168 202 PRO A C   
1742 O O   . PRO A 202 ? 0.1267 0.1682 0.1757 -0.0326 0.0258  -0.0174 202 PRO A O   
1743 C CB  . PRO A 202 ? 0.1660 0.1871 0.1939 -0.0448 0.0269  -0.0183 202 PRO A CB  
1744 C CG  . PRO A 202 ? 0.1586 0.1694 0.1780 -0.0465 0.0275  -0.0183 202 PRO A CG  
1745 C CD  . PRO A 202 ? 0.1792 0.1850 0.1986 -0.0411 0.0252  -0.0168 202 PRO A CD  
1746 N N   . ILE A 203 ? 0.1333 0.1613 0.1710 -0.0332 0.0193  -0.0151 203 ILE A N   
1747 C CA  . ILE A 203 ? 0.1290 0.1645 0.1715 -0.0306 0.0156  -0.0142 203 ILE A CA  
1748 C C   . ILE A 203 ? 0.1064 0.1465 0.1552 -0.0235 0.0165  -0.0127 203 ILE A C   
1749 O O   . ILE A 203 ? 0.1135 0.1636 0.1699 -0.0212 0.0157  -0.0124 203 ILE A O   
1750 C CB  . ILE A 203 ? 0.1429 0.1732 0.1790 -0.0312 0.0104  -0.0135 203 ILE A CB  
1751 C CG1 . ILE A 203 ? 0.1782 0.2056 0.2106 -0.0381 0.0084  -0.0149 203 ILE A CG1 
1752 C CG2 . ILE A 203 ? 0.1498 0.1872 0.1895 -0.0270 0.0065  -0.0128 203 ILE A CG2 
1753 C CD1 . ILE A 203 ? 0.2087 0.2295 0.2346 -0.0382 0.0034  -0.0150 203 ILE A CD1 
1754 N N   . LEU A 204 ? 0.1281 0.1610 0.1742 -0.0202 0.0178  -0.0113 204 LEU A N   
1755 C CA  . LEU A 204 ? 0.1280 0.1637 0.1801 -0.0138 0.0186  -0.0091 204 LEU A CA  
1756 C C   . LEU A 204 ? 0.1248 0.1667 0.1851 -0.0119 0.0225  -0.0108 204 LEU A C   
1757 O O   . LEU A 204 ? 0.1190 0.1684 0.1873 -0.0069 0.0220  -0.0093 204 LEU A O   
1758 C CB  . LEU A 204 ? 0.1081 0.1340 0.1562 -0.0118 0.0196  -0.0072 204 LEU A CB  
1759 C CG  . LEU A 204 ? 0.1523 0.1731 0.1934 -0.0125 0.0164  -0.0048 204 LEU A CG  
1760 C CD1 . LEU A 204 ? 0.1512 0.1645 0.1910 -0.0105 0.0176  -0.0021 204 LEU A CD1 
1761 C CD2 . LEU A 204 ? 0.2227 0.2505 0.2641 -0.0099 0.0122  -0.0029 204 LEU A CD2 
1762 N N   . LEU A 205 ? 0.1111 0.1505 0.1697 -0.0156 0.0266  -0.0140 205 LEU A N   
1763 C CA  . LEU A 205 ? 0.1137 0.1601 0.1801 -0.0134 0.0311  -0.0163 205 LEU A CA  
1764 C C   . LEU A 205 ? 0.1422 0.2024 0.2158 -0.0149 0.0300  -0.0164 205 LEU A C   
1765 O O   . LEU A 205 ? 0.1797 0.2494 0.2631 -0.0104 0.0315  -0.0164 205 LEU A O   
1766 C CB  . LEU A 205 ? 0.1181 0.1591 0.1794 -0.0172 0.0359  -0.0199 205 LEU A CB  
1767 C CG  . LEU A 205 ? 0.1222 0.1508 0.1787 -0.0150 0.0375  -0.0205 205 LEU A CG  
1768 C CD1 . LEU A 205 ? 0.1640 0.1873 0.2132 -0.0199 0.0413  -0.0243 205 LEU A CD1 
1769 C CD2 . LEU A 205 ? 0.1671 0.1964 0.2320 -0.0072 0.0394  -0.0206 205 LEU A CD2 
1770 N N   . ASN A 206 ? 0.1202 0.1813 0.1895 -0.0213 0.0273  -0.0165 206 ASN A N   
1771 C CA  . ASN A 206 ? 0.1350 0.2089 0.2112 -0.0242 0.0263  -0.0167 206 ASN A CA  
1772 C C   . ASN A 206 ? 0.1451 0.2163 0.2155 -0.0301 0.0210  -0.0161 206 ASN A C   
1773 O O   . ASN A 206 ? 0.1283 0.1950 0.1930 -0.0366 0.0216  -0.0170 206 ASN A O   
1774 C CB  . ASN A 206 ? 0.1695 0.2495 0.2489 -0.0273 0.0321  -0.0191 206 ASN A CB  
1775 C CG  . ASN A 206 ? 0.3049 0.4004 0.3939 -0.0300 0.0315  -0.0187 206 ASN A CG  
1776 O OD1 . ASN A 206 ? 0.1711 0.2710 0.2625 -0.0313 0.0259  -0.0171 206 ASN A OD1 
1777 N ND2 . ASN A 206 ? 0.3970 0.5017 0.4917 -0.0308 0.0372  -0.0203 206 ASN A ND2 
1778 N N   . PRO A 207 ? 0.1439 0.2174 0.2151 -0.0278 0.0155  -0.0147 207 PRO A N   
1779 C CA  . PRO A 207 ? 0.1187 0.1884 0.1839 -0.0328 0.0101  -0.0150 207 PRO A CA  
1780 C C   . PRO A 207 ? 0.2012 0.2762 0.2691 -0.0404 0.0097  -0.0160 207 PRO A C   
1781 O O   . PRO A 207 ? 0.2027 0.2709 0.2644 -0.0458 0.0062  -0.0166 207 PRO A O   
1782 C CB  . PRO A 207 ? 0.1679 0.2430 0.2356 -0.0282 0.0050  -0.0139 207 PRO A CB  
1783 C CG  . PRO A 207 ? 0.1957 0.2710 0.2660 -0.0207 0.0076  -0.0118 207 PRO A CG  
1784 C CD  . PRO A 207 ? 0.1810 0.2592 0.2573 -0.0204 0.0138  -0.0127 207 PRO A CD  
1785 N N   . ASN A 208 ? 0.1459 0.2329 0.2232 -0.0411 0.0131  -0.0161 208 ASN A N   
1786 C CA  . ASN A 208 ? 0.1121 0.2054 0.1926 -0.0491 0.0127  -0.0162 208 ASN A CA  
1787 C C   . ASN A 208 ? 0.1153 0.2003 0.1883 -0.0551 0.0161  -0.0165 208 ASN A C   
1788 O O   . ASN A 208 ? 0.1650 0.2529 0.2389 -0.0629 0.0154  -0.0158 208 ASN A O   
1789 C CB  . ASN A 208 ? 0.1614 0.2719 0.2549 -0.0481 0.0160  -0.0159 208 ASN A CB  
1790 C CG  . ASN A 208 ? 0.2409 0.3613 0.3426 -0.0427 0.0118  -0.0150 208 ASN A CG  
1791 O OD1 . ASN A 208 ? 0.1922 0.3094 0.2903 -0.0430 0.0052  -0.0149 208 ASN A OD1 
1792 N ND2 . ASN A 208 ? 0.2676 0.4002 0.3799 -0.0374 0.0155  -0.0145 208 ASN A ND2 
1793 N N   . CYS A 209 ? 0.1633 0.2380 0.2290 -0.0523 0.0194  -0.0170 209 CYS A N   
1794 C CA  . CYS A 209 ? 0.1645 0.2322 0.2227 -0.0583 0.0222  -0.0170 209 CYS A CA  
1795 C C   . CYS A 209 ? 0.1639 0.2219 0.2147 -0.0643 0.0167  -0.0160 209 CYS A C   
1796 O O   . CYS A 209 ? 0.1589 0.2125 0.2046 -0.0707 0.0178  -0.0150 209 CYS A O   
1797 C CB  . CYS A 209 ? 0.2179 0.2765 0.2695 -0.0543 0.0261  -0.0180 209 CYS A CB  
1798 S SG  . CYS A 209 ? 0.2254 0.2702 0.2691 -0.0501 0.0214  -0.0174 209 CYS A SG  
1799 N N   . VAL A 210 ? 0.1798 0.2344 0.2299 -0.0622 0.0106  -0.0161 210 VAL A N   
1800 C CA  . VAL A 210 ? 0.2019 0.2465 0.2453 -0.0671 0.0051  -0.0158 210 VAL A CA  
1801 C C   . VAL A 210 ? 0.2041 0.2536 0.2513 -0.0757 0.0035  -0.0148 210 VAL A C   
1802 O O   . VAL A 210 ? 0.1852 0.2254 0.2266 -0.0817 0.0007  -0.0138 210 VAL A O   
1803 C CB  . VAL A 210 ? 0.2380 0.2790 0.2797 -0.0623 -0.0008 -0.0171 210 VAL A CB  
1804 C CG1 . VAL A 210 ? 0.1830 0.2201 0.2213 -0.0544 0.0010  -0.0171 210 VAL A CG1 
1805 C CG2 . VAL A 210 ? 0.1901 0.2431 0.2404 -0.0617 -0.0037 -0.0178 210 VAL A CG2 
1806 N N   . TYR A 211 ? 0.1534 0.2176 0.2108 -0.0767 0.0053  -0.0146 211 TYR A N   
1807 C CA  . TYR A 211 ? 0.1515 0.2218 0.2137 -0.0856 0.0036  -0.0131 211 TYR A CA  
1808 C C   . TYR A 211 ? 0.1566 0.2283 0.2170 -0.0919 0.0092  -0.0108 211 TYR A C   
1809 O O   . TYR A 211 ? 0.1778 0.2544 0.2417 -0.1003 0.0083  -0.0086 211 TYR A O   
1810 C CB  . TYR A 211 ? 0.1586 0.2461 0.2334 -0.0848 0.0033  -0.0132 211 TYR A CB  
1811 C CG  . TYR A 211 ? 0.1600 0.2474 0.2359 -0.0787 -0.0023 -0.0152 211 TYR A CG  
1812 C CD1 . TYR A 211 ? 0.2514 0.3296 0.3222 -0.0812 -0.0099 -0.0165 211 TYR A CD1 
1813 C CD2 . TYR A 211 ? 0.2672 0.3635 0.3489 -0.0703 -0.0001 -0.0157 211 TYR A CD2 
1814 C CE1 . TYR A 211 ? 0.2943 0.3731 0.3649 -0.0755 -0.0149 -0.0185 211 TYR A CE1 
1815 C CE2 . TYR A 211 ? 0.3417 0.4386 0.4236 -0.0650 -0.0051 -0.0168 211 TYR A CE2 
1816 C CZ  . TYR A 211 ? 0.3641 0.4530 0.4402 -0.0676 -0.0123 -0.0183 211 TYR A CZ  
1817 O OH  . TYR A 211 ? 0.4620 0.5526 0.5375 -0.0621 -0.0171 -0.0196 211 TYR A OH  
1818 N N   . GLU A 212 ? 0.1449 0.2125 0.1996 -0.0884 0.0146  -0.0112 212 GLU A N   
1819 C CA  . GLU A 212 ? 0.2005 0.2687 0.2514 -0.0945 0.0196  -0.0093 212 GLU A CA  
1820 C C   . GLU A 212 ? 0.2507 0.3050 0.2925 -0.1006 0.0149  -0.0065 212 GLU A C   
1821 O O   . GLU A 212 ? 0.2746 0.3295 0.3144 -0.1049 0.0162  -0.0033 212 GLU A O   
1822 C CB  . GLU A 212 ? 0.1960 0.2623 0.2422 -0.0888 0.0259  -0.0111 212 GLU A CB  
1823 C CG  . GLU A 212 ? 0.2268 0.3061 0.2825 -0.0817 0.0307  -0.0135 212 GLU A CG  
1824 C CD  . GLU A 212 ? 0.3487 0.4258 0.4001 -0.0767 0.0371  -0.0159 212 GLU A CD  
1825 O OE1 . GLU A 212 ? 0.4432 0.5250 0.5004 -0.0689 0.0396  -0.0182 212 GLU A OE1 
1826 O OE2 . GLU A 212 ? 0.4663 0.5363 0.5083 -0.0806 0.0392  -0.0154 212 GLU A OE2 
1827 N N   . THR A 213 ? 0.1983 0.2394 0.2347 -0.0986 0.0089  -0.0074 213 THR A N   
1828 C CA  . THR A 213 ? 0.2408 0.2674 0.2691 -0.1005 0.0039  -0.0049 213 THR A CA  
1829 C C   . THR A 213 ? 0.2960 0.3167 0.3261 -0.1012 -0.0037 -0.0055 213 THR A C   
1830 O O   . THR A 213 ? 0.2824 0.2949 0.3095 -0.1042 -0.0073 -0.0031 213 THR A O   
1831 C CB  . THR A 213 ? 0.2491 0.2633 0.2678 -0.0967 0.0038  -0.0053 213 THR A CB  
1832 O OG1 . THR A 213 ? 0.2955 0.3087 0.3154 -0.0917 0.0023  -0.0088 213 THR A OG1 
1833 C CG2 . THR A 213 ? 0.2338 0.2514 0.2488 -0.0970 0.0105  -0.0047 213 THR A CG2 
1834 N N   . THR A 214 ? 0.2449 0.2696 0.2795 -0.0985 -0.0065 -0.0090 214 THR A N   
1835 C CA  . THR A 214 ? 0.1809 0.1996 0.2160 -0.0986 -0.0141 -0.0108 214 THR A CA  
1836 C C   . THR A 214 ? 0.2266 0.2599 0.2719 -0.1000 -0.0154 -0.0123 214 THR A C   
1837 O O   . THR A 214 ? 0.2351 0.2724 0.2822 -0.0943 -0.0169 -0.0153 214 THR A O   
1838 C CB  . THR A 214 ? 0.2089 0.2166 0.2370 -0.0933 -0.0177 -0.0139 214 THR A CB  
1839 O OG1 . THR A 214 ? 0.2375 0.2528 0.2675 -0.0853 -0.0141 -0.0156 214 THR A OG1 
1840 C CG2 . THR A 214 ? 0.2070 0.2013 0.2261 -0.0917 -0.0170 -0.0119 214 THR A CG2 
1841 N N   . PRO A 215 ? 0.2324 0.2739 0.2845 -0.1050 -0.0147 -0.0098 215 PRO A N   
1842 C CA  . PRO A 215 ? 0.2504 0.3079 0.3136 -0.1061 -0.0157 -0.0108 215 PRO A CA  
1843 C C   . PRO A 215 ? 0.2791 0.3332 0.3428 -0.1054 -0.0240 -0.0141 215 PRO A C   
1844 O O   . PRO A 215 ? 0.2655 0.3334 0.3373 -0.1046 -0.0254 -0.0155 215 PRO A O   
1845 C CB  . PRO A 215 ? 0.3045 0.3690 0.3734 -0.1121 -0.0134 -0.0068 215 PRO A CB  
1846 C CG  . PRO A 215 ? 0.3410 0.3898 0.4009 -0.1148 -0.0143 -0.0043 215 PRO A CG  
1847 C CD  . PRO A 215 ? 0.2970 0.3353 0.3473 -0.1098 -0.0125 -0.0056 215 PRO A CD  
1848 N N   . ASN A 216 ? 0.2851 0.3223 0.3406 -0.1052 -0.0295 -0.0156 216 ASN A N   
1849 C CA  . ASN A 216 ? 0.3898 0.4232 0.4449 -0.1045 -0.0373 -0.0196 216 ASN A CA  
1850 C C   . ASN A 216 ? 0.3795 0.4101 0.4287 -0.0982 -0.0399 -0.0238 216 ASN A C   
1851 O O   . ASN A 216 ? 0.4336 0.4616 0.4810 -0.0967 -0.0465 -0.0278 216 ASN A O   
1852 C CB  . ASN A 216 ? 0.4169 0.4342 0.4669 -0.1070 -0.0419 -0.0200 216 ASN A CB  
1853 C CG  . ASN A 216 ? 0.4888 0.5102 0.5451 -0.1141 -0.0408 -0.0161 216 ASN A CG  
1854 O OD1 . ASN A 216 ? 0.5450 0.5582 0.5978 -0.1166 -0.0388 -0.0127 216 ASN A OD1 
1855 N ND2 . ASN A 216 ? 0.5189 0.5540 0.5849 -0.1173 -0.0421 -0.0161 216 ASN A ND2 
1856 N N   . VAL A 217 ? 0.3601 0.3908 0.4060 -0.0919 -0.0342 -0.0230 217 VAL A N   
1857 C CA  . VAL A 217 ? 0.2887 0.3149 0.3282 -0.0823 -0.0351 -0.0259 217 VAL A CA  
1858 C C   . VAL A 217 ? 0.2912 0.3315 0.3367 -0.0774 -0.0361 -0.0273 217 VAL A C   
1859 O O   . VAL A 217 ? 0.2255 0.2802 0.2805 -0.0787 -0.0330 -0.0251 217 VAL A O   
1860 C CB  . VAL A 217 ? 0.2825 0.3046 0.3174 -0.0772 -0.0286 -0.0239 217 VAL A CB  
1861 C CG1 . VAL A 217 ? 0.2624 0.2981 0.3046 -0.0748 -0.0218 -0.0216 217 VAL A CG1 
1862 C CG2 . VAL A 217 ? 0.2736 0.2883 0.3008 -0.0688 -0.0300 -0.0262 217 VAL A CG2 
1863 N N   . LYS A 218 ? 0.2097 0.2463 0.2495 -0.0718 -0.0406 -0.0307 218 LYS A N   
1864 C CA  . LYS A 218 ? 0.2336 0.2827 0.2770 -0.0658 -0.0415 -0.0314 218 LYS A CA  
1865 C C   . LYS A 218 ? 0.2359 0.2853 0.2761 -0.0569 -0.0361 -0.0297 218 LYS A C   
1866 O O   . LYS A 218 ? 0.2370 0.2752 0.2687 -0.0536 -0.0355 -0.0305 218 LYS A O   
1867 C CB  . LYS A 218 ? 0.2679 0.3138 0.3060 -0.0648 -0.0495 -0.0362 218 LYS A CB  
1868 C CG  . LYS A 218 ? 0.4073 0.4527 0.4489 -0.0739 -0.0560 -0.0382 218 LYS A CG  
1869 C CD  . LYS A 218 ? 0.5252 0.5662 0.5601 -0.0723 -0.0641 -0.0440 218 LYS A CD  
1870 C CE  . LYS A 218 ? 0.5788 0.6351 0.6166 -0.0667 -0.0655 -0.0442 218 LYS A CE  
1871 N NZ  . LYS A 218 ? 0.6532 0.7068 0.6840 -0.0660 -0.0738 -0.0502 218 LYS A NZ  
1872 N N   . ILE A 219 ? 0.1893 0.2517 0.2369 -0.0530 -0.0326 -0.0272 219 ILE A N   
1873 C CA  . ILE A 219 ? 0.1404 0.2035 0.1857 -0.0447 -0.0285 -0.0252 219 ILE A CA  
1874 C C   . ILE A 219 ? 0.1805 0.2556 0.2296 -0.0393 -0.0310 -0.0247 219 ILE A C   
1875 O O   . ILE A 219 ? 0.1622 0.2476 0.2183 -0.0422 -0.0344 -0.0251 219 ILE A O   
1876 C CB  . ILE A 219 ? 0.1780 0.2427 0.2280 -0.0443 -0.0209 -0.0221 219 ILE A CB  
1877 C CG1 . ILE A 219 ? 0.1847 0.2644 0.2466 -0.0450 -0.0189 -0.0203 219 ILE A CG1 
1878 C CG2 . ILE A 219 ? 0.1805 0.2345 0.2264 -0.0503 -0.0188 -0.0222 219 ILE A CG2 
1879 C CD1 . ILE A 219 ? 0.2848 0.3667 0.3512 -0.0429 -0.0113 -0.0181 219 ILE A CD1 
1880 N N   . PRO A 220 ? 0.2148 0.2894 0.2596 -0.0318 -0.0297 -0.0233 220 PRO A N   
1881 C CA  . PRO A 220 ? 0.2415 0.3278 0.2895 -0.0266 -0.0321 -0.0217 220 PRO A CA  
1882 C C   . PRO A 220 ? 0.1717 0.2697 0.2316 -0.0248 -0.0285 -0.0179 220 PRO A C   
1883 O O   . PRO A 220 ? 0.1470 0.2444 0.2123 -0.0273 -0.0234 -0.0169 220 PRO A O   
1884 C CB  . PRO A 220 ? 0.2201 0.3015 0.2596 -0.0197 -0.0310 -0.0205 220 PRO A CB  
1885 C CG  . PRO A 220 ? 0.2111 0.2809 0.2469 -0.0205 -0.0260 -0.0199 220 PRO A CG  
1886 C CD  . PRO A 220 ? 0.1974 0.2610 0.2337 -0.0282 -0.0268 -0.0228 220 PRO A CD  
1887 N N   . ASP A 221 ? 0.1851 0.2942 0.2488 -0.0203 -0.0313 -0.0160 221 ASP A N   
1888 C CA  . ASP A 221 ? 0.1550 0.2763 0.2305 -0.0170 -0.0288 -0.0122 221 ASP A CA  
1889 C C   . ASP A 221 ? 0.1703 0.2868 0.2455 -0.0107 -0.0230 -0.0085 221 ASP A C   
1890 O O   . ASP A 221 ? 0.1642 0.2803 0.2349 -0.0051 -0.0241 -0.0059 221 ASP A O   
1891 C CB  . ASP A 221 ? 0.1297 0.2638 0.2084 -0.0142 -0.0349 -0.0110 221 ASP A CB  
1892 C CG  . ASP A 221 ? 0.1997 0.3479 0.2924 -0.0114 -0.0335 -0.0073 221 ASP A CG  
1893 O OD1 . ASP A 221 ? 0.1537 0.3031 0.2543 -0.0132 -0.0283 -0.0071 221 ASP A OD1 
1894 O OD2 . ASP A 221 ? 0.2469 0.4053 0.3425 -0.0068 -0.0374 -0.0045 221 ASP A OD2 
1895 N N   . PHE A 222 ? 0.1096 0.2225 0.1892 -0.0119 -0.0169 -0.0082 222 PHE A N   
1896 C CA  . PHE A 222 ? 0.1071 0.2145 0.1867 -0.0065 -0.0117 -0.0053 222 PHE A CA  
1897 C C   . PHE A 222 ? 0.1067 0.2250 0.1970 -0.0005 -0.0112 -0.0015 222 PHE A C   
1898 O O   . PHE A 222 ? 0.1232 0.2452 0.2224 0.0006  -0.0068 -0.0013 222 PHE A O   
1899 C CB  . PHE A 222 ? 0.1231 0.2218 0.2021 -0.0098 -0.0058 -0.0069 222 PHE A CB  
1900 C CG  . PHE A 222 ? 0.1197 0.2054 0.1874 -0.0135 -0.0058 -0.0090 222 PHE A CG  
1901 C CD1 . PHE A 222 ? 0.1265 0.2097 0.1897 -0.0195 -0.0094 -0.0121 222 PHE A CD1 
1902 C CD2 . PHE A 222 ? 0.1366 0.2125 0.1987 -0.0107 -0.0029 -0.0074 222 PHE A CD2 
1903 C CE1 . PHE A 222 ? 0.1534 0.2243 0.2067 -0.0221 -0.0096 -0.0137 222 PHE A CE1 
1904 C CE2 . PHE A 222 ? 0.1521 0.2172 0.2047 -0.0136 -0.0031 -0.0089 222 PHE A CE2 
1905 C CZ  . PHE A 222 ? 0.1765 0.2390 0.2247 -0.0189 -0.0064 -0.0121 222 PHE A CZ  
1906 N N   . ALA A 223 ? 0.1215 0.2451 0.2104 0.0040  -0.0157 0.0014  223 ALA A N   
1907 C CA  . ALA A 223 ? 0.1907 0.3251 0.2894 0.0101  -0.0165 0.0058  223 ALA A CA  
1908 C C   . ALA A 223 ? 0.1806 0.3086 0.2814 0.0162  -0.0120 0.0098  223 ALA A C   
1909 O O   . ALA A 223 ? 0.2313 0.3666 0.3402 0.0220  -0.0127 0.0140  223 ALA A O   
1910 C CB  . ALA A 223 ? 0.1962 0.3388 0.2915 0.0122  -0.0235 0.0079  223 ALA A CB  
1911 N N   . VAL A 224 ? 0.1454 0.2598 0.2393 0.0150  -0.0079 0.0088  224 VAL A N   
1912 C CA  . VAL A 224 ? 0.2241 0.3305 0.3197 0.0196  -0.0037 0.0120  224 VAL A CA  
1913 C C   . VAL A 224 ? 0.1523 0.2500 0.2478 0.0161  0.0021  0.0079  224 VAL A C   
1914 O O   . VAL A 224 ? 0.1779 0.2726 0.2683 0.0100  0.0025  0.0038  224 VAL A O   
1915 C CB  . VAL A 224 ? 0.3299 0.4280 0.4159 0.0213  -0.0048 0.0157  224 VAL A CB  
1916 C CG1 . VAL A 224 ? 0.3676 0.4606 0.4579 0.0269  -0.0024 0.0209  224 VAL A CG1 
1917 C CG2 . VAL A 224 ? 0.3992 0.5046 0.4798 0.0220  -0.0104 0.0175  224 VAL A CG2 
1918 N N   . SER A 225 ? 0.1375 0.2301 0.2380 0.0202  0.0062  0.0091  225 SER A N   
1919 C CA  . SER A 225 ? 0.1468 0.2304 0.2460 0.0176  0.0117  0.0052  225 SER A CA  
1920 C C   . SER A 225 ? 0.1386 0.2081 0.2280 0.0161  0.0126  0.0061  225 SER A C   
1921 O O   . SER A 225 ? 0.1538 0.2192 0.2424 0.0200  0.0113  0.0108  225 SER A O   
1922 C CB  . SER A 225 ? 0.1779 0.2627 0.2874 0.0230  0.0158  0.0050  225 SER A CB  
1923 O OG  . SER A 225 ? 0.1422 0.2168 0.2484 0.0208  0.0210  0.0010  225 SER A OG  
1924 N N   . PHE A 226 ? 0.1292 0.1920 0.2116 0.0102  0.0146  0.0022  226 PHE A N   
1925 C CA  . PHE A 226 ? 0.1102 0.1602 0.1845 0.0082  0.0159  0.0026  226 PHE A CA  
1926 C C   . PHE A 226 ? 0.1495 0.1913 0.2244 0.0074  0.0209  -0.0006 226 PHE A C   
1927 O O   . PHE A 226 ? 0.1389 0.1704 0.2069 0.0044  0.0220  -0.0012 226 PHE A O   
1928 C CB  . PHE A 226 ? 0.1223 0.1698 0.1874 0.0025  0.0138  0.0008  226 PHE A CB  
1929 C CG  . PHE A 226 ? 0.1058 0.1583 0.1675 0.0037  0.0089  0.0034  226 PHE A CG  
1930 C CD1 . PHE A 226 ? 0.1066 0.1555 0.1641 0.0063  0.0076  0.0076  226 PHE A CD1 
1931 C CD2 . PHE A 226 ? 0.1962 0.2572 0.2585 0.0019  0.0057  0.0015  226 PHE A CD2 
1932 C CE1 . PHE A 226 ? 0.1304 0.1846 0.1836 0.0077  0.0036  0.0095  226 PHE A CE1 
1933 C CE2 . PHE A 226 ? 0.1484 0.2136 0.2064 0.0031  0.0010  0.0029  226 PHE A CE2 
1934 C CZ  . PHE A 226 ? 0.1472 0.2092 0.2003 0.0063  0.0002  0.0067  226 PHE A CZ  
1935 N N   . ARG A 227 ? 0.1636 0.2105 0.2466 0.0099  0.0240  -0.0029 227 ARG A N   
1936 C CA  . ARG A 227 ? 0.1286 0.1686 0.2111 0.0090  0.0291  -0.0072 227 ARG A CA  
1937 C C   . ARG A 227 ? 0.1644 0.1917 0.2452 0.0119  0.0300  -0.0057 227 ARG A C   
1938 O O   . ARG A 227 ? 0.2115 0.2288 0.2861 0.0086  0.0323  -0.0086 227 ARG A O   
1939 C CB  . ARG A 227 ? 0.1798 0.2295 0.2720 0.0121  0.0325  -0.0100 227 ARG A CB  
1940 C CG  . ARG A 227 ? 0.2352 0.2970 0.3292 0.0077  0.0322  -0.0119 227 ARG A CG  
1941 C CD  . ARG A 227 ? 0.2976 0.3704 0.4021 0.0109  0.0362  -0.0144 227 ARG A CD  
1942 N NE  . ARG A 227 ? 0.3073 0.3738 0.4102 0.0114  0.0423  -0.0191 227 ARG A NE  
1943 C CZ  . ARG A 227 ? 0.3523 0.4180 0.4491 0.0053  0.0458  -0.0229 227 ARG A CZ  
1944 N NH1 . ARG A 227 ? 0.2809 0.3507 0.3732 -0.0020 0.0435  -0.0223 227 ARG A NH1 
1945 N NH2 . ARG A 227 ? 0.3835 0.4438 0.4783 0.0064  0.0512  -0.0275 227 ARG A NH2 
1946 N N   . GLU A 228 ? 0.1684 0.1958 0.2545 0.0176  0.0278  -0.0008 228 GLU A N   
1947 C CA  . GLU A 228 ? 0.1696 0.1841 0.2547 0.0198  0.0281  0.0014  228 GLU A CA  
1948 C C   . GLU A 228 ? 0.1873 0.1942 0.2630 0.0148  0.0260  0.0037  228 GLU A C   
1949 O O   . GLU A 228 ? 0.1825 0.1776 0.2544 0.0128  0.0273  0.0028  228 GLU A O   
1950 C CB  . GLU A 228 ? 0.2664 0.2831 0.3596 0.0269  0.0258  0.0073  228 GLU A CB  
1951 C CG  . GLU A 228 ? 0.4532 0.4563 0.5454 0.0284  0.0251  0.0112  228 GLU A CG  
1952 C CD  . GLU A 228 ? 0.6875 0.6779 0.7795 0.0283  0.0289  0.0057  228 GLU A CD  
1953 O OE1 . GLU A 228 ? 0.7662 0.7597 0.8620 0.0303  0.0326  -0.0003 228 GLU A OE1 
1954 O OE2 . GLU A 228 ? 0.7684 0.7461 0.8563 0.0261  0.0283  0.0073  228 GLU A OE2 
1955 N N   . ASP A 229 ? 0.1710 0.1846 0.2429 0.0126  0.0228  0.0065  229 ASP A N   
1956 C CA  . ASP A 229 ? 0.1436 0.1515 0.2071 0.0083  0.0212  0.0083  229 ASP A CA  
1957 C C   . ASP A 229 ? 0.1661 0.1675 0.2232 0.0025  0.0234  0.0031  229 ASP A C   
1958 O O   . ASP A 229 ? 0.1402 0.1332 0.1922 -0.0005 0.0233  0.0040  229 ASP A O   
1959 C CB  . ASP A 229 ? 0.1178 0.1344 0.1781 0.0078  0.0176  0.0109  229 ASP A CB  
1960 C CG  . ASP A 229 ? 0.2105 0.2320 0.2740 0.0127  0.0148  0.0176  229 ASP A CG  
1961 O OD1 . ASP A 229 ? 0.2160 0.2328 0.2842 0.0162  0.0154  0.0210  229 ASP A OD1 
1962 O OD2 . ASP A 229 ? 0.2027 0.2322 0.2633 0.0131  0.0118  0.0193  229 ASP A OD2 
1963 N N   . ALA A 230 ? 0.1343 0.1406 0.1916 0.0004  0.0253  -0.0018 230 ALA A N   
1964 C CA  . ALA A 230 ? 0.1516 0.1523 0.2024 -0.0052 0.0275  -0.0063 230 ALA A CA  
1965 C C   . ALA A 230 ? 0.1664 0.1562 0.2162 -0.0051 0.0301  -0.0083 230 ALA A C   
1966 O O   . ALA A 230 ? 0.1566 0.1384 0.1996 -0.0095 0.0299  -0.0091 230 ALA A O   
1967 C CB  . ALA A 230 ? 0.1649 0.1733 0.2174 -0.0071 0.0297  -0.0106 230 ALA A CB  
1968 N N   . SER A 231 ? 0.1445 0.1337 0.2012 0.0000  0.0323  -0.0093 231 SER A N   
1969 C CA  . SER A 231 ? 0.1512 0.1286 0.2074 0.0009  0.0344  -0.0117 231 SER A CA  
1970 C C   . SER A 231 ? 0.1885 0.1567 0.2424 -0.0001 0.0313  -0.0067 231 SER A C   
1971 O O   . SER A 231 ? 0.2437 0.2015 0.2924 -0.0037 0.0317  -0.0086 231 SER A O   
1972 C CB  . SER A 231 ? 0.2757 0.2548 0.3410 0.0078  0.0368  -0.0133 231 SER A CB  
1973 O OG  . SER A 231 ? 0.4015 0.3680 0.4667 0.0094  0.0385  -0.0159 231 SER A OG  
1974 N N   . LYS A 232 ? 0.1593 0.1319 0.2168 0.0027  0.0282  -0.0001 232 LYS A N   
1975 C CA  . LYS A 232 ? 0.1779 0.1437 0.2337 0.0015  0.0255  0.0056  232 LYS A CA  
1976 C C   . LYS A 232 ? 0.1809 0.1448 0.2286 -0.0050 0.0243  0.0056  232 LYS A C   
1977 O O   . LYS A 232 ? 0.1770 0.1322 0.2224 -0.0079 0.0234  0.0072  232 LYS A O   
1978 C CB  . LYS A 232 ? 0.1984 0.1716 0.2586 0.0055  0.0227  0.0131  232 LYS A CB  
1979 C CG  . LYS A 232 ? 0.4085 0.3812 0.4772 0.0120  0.0227  0.0156  232 LYS A CG  
1980 C CD  . LYS A 232 ? 0.4874 0.4678 0.5588 0.0153  0.0195  0.0237  232 LYS A CD  
1981 C CE  . LYS A 232 ? 0.6105 0.5850 0.6792 0.0127  0.0176  0.0303  232 LYS A CE  
1982 N NZ  . LYS A 232 ? 0.7074 0.6895 0.7784 0.0161  0.0148  0.0389  232 LYS A NZ  
1983 N N   . HIS A 233 ? 0.2055 0.1772 0.2492 -0.0073 0.0239  0.0040  233 HIS A N   
1984 C CA  . HIS A 233 ? 0.1599 0.1295 0.1965 -0.0128 0.0226  0.0040  233 HIS A CA  
1985 C C   . HIS A 233 ? 0.1662 0.1259 0.1986 -0.0171 0.0242  -0.0004 233 HIS A C   
1986 O O   . HIS A 233 ? 0.1741 0.1283 0.2027 -0.0209 0.0226  0.0012  233 HIS A O   
1987 C CB  . HIS A 233 ? 0.1290 0.1062 0.1618 -0.0147 0.0219  0.0020  233 HIS A CB  
1988 C CG  . HIS A 233 ? 0.1266 0.1126 0.1606 -0.0119 0.0193  0.0060  233 HIS A CG  
1989 N ND1 . HIS A 233 ? 0.1304 0.1177 0.1609 -0.0129 0.0170  0.0095  233 HIS A ND1 
1990 C CD2 . HIS A 233 ? 0.1337 0.1281 0.1715 -0.0082 0.0186  0.0064  233 HIS A CD2 
1991 C CE1 . HIS A 233 ? 0.1486 0.1442 0.1799 -0.0097 0.0152  0.0116  233 HIS A CE1 
1992 N NE2 . HIS A 233 ? 0.1420 0.1419 0.1776 -0.0071 0.0159  0.0098  233 HIS A NE2 
1993 N N   . VAL A 234 ? 0.1729 0.1312 0.2055 -0.0166 0.0273  -0.0062 234 VAL A N   
1994 C CA  . VAL A 234 ? 0.1739 0.1233 0.2010 -0.0207 0.0289  -0.0113 234 VAL A CA  
1995 C C   . VAL A 234 ? 0.1984 0.1367 0.2275 -0.0198 0.0285  -0.0105 234 VAL A C   
1996 O O   . VAL A 234 ? 0.1953 0.1255 0.2193 -0.0245 0.0273  -0.0115 234 VAL A O   
1997 C CB  . VAL A 234 ? 0.1736 0.1258 0.2002 -0.0200 0.0330  -0.0178 234 VAL A CB  
1998 C CG1 . VAL A 234 ? 0.1839 0.1270 0.2034 -0.0240 0.0348  -0.0233 234 VAL A CG1 
1999 C CG2 . VAL A 234 ? 0.1656 0.1282 0.1904 -0.0220 0.0329  -0.0178 234 VAL A CG2 
2000 N N   . GLU A 235 ? 0.1952 0.1328 0.2319 -0.0141 0.0290  -0.0087 235 GLU A N   
2001 C CA  . GLU A 235 ? 0.1924 0.1177 0.2315 -0.0131 0.0284  -0.0082 235 GLU A CA  
2002 C C   . GLU A 235 ? 0.2424 0.1643 0.2811 -0.0165 0.0246  -0.0012 235 GLU A C   
2003 O O   . GLU A 235 ? 0.2558 0.1668 0.2922 -0.0203 0.0233  -0.0019 235 GLU A O   
2004 C CB  . GLU A 235 ? 0.2996 0.2250 0.3476 -0.0056 0.0295  -0.0071 235 GLU A CB  
2005 C CG  . GLU A 235 ? 0.5257 0.4363 0.5764 -0.0040 0.0292  -0.0081 235 GLU A CG  
2006 C CD  . GLU A 235 ? 0.6742 0.5758 0.7196 -0.0056 0.0321  -0.0176 235 GLU A CD  
2007 O OE1 . GLU A 235 ? 0.6841 0.5927 0.7274 -0.0046 0.0357  -0.0235 235 GLU A OE1 
2008 O OE2 . GLU A 235 ? 0.6990 0.5868 0.7421 -0.0083 0.0307  -0.0192 235 GLU A OE2 
2009 N N   . LEU A 236 ? 0.1837 0.1152 0.2244 -0.0154 0.0227  0.0054  236 LEU A N   
2010 C CA  . LEU A 236 ? 0.1789 0.1098 0.2196 -0.0185 0.0196  0.0124  236 LEU A CA  
2011 C C   . LEU A 236 ? 0.1597 0.0889 0.1935 -0.0253 0.0184  0.0107  236 LEU A C   
2012 O O   . LEU A 236 ? 0.1911 0.1157 0.2250 -0.0291 0.0162  0.0146  236 LEU A O   
2013 C CB  . LEU A 236 ? 0.2159 0.1589 0.2590 -0.0153 0.0184  0.0189  236 LEU A CB  
2014 C CG  . LEU A 236 ? 0.1894 0.1343 0.2396 -0.0090 0.0184  0.0227  236 LEU A CG  
2015 C CD1 . LEU A 236 ? 0.1960 0.1544 0.2471 -0.0059 0.0172  0.0278  236 LEU A CD1 
2016 C CD2 . LEU A 236 ? 0.2796 0.2140 0.3342 -0.0091 0.0171  0.0276  236 LEU A CD2 
2017 N N   . ALA A 237 ? 0.1961 0.1296 0.2246 -0.0269 0.0196  0.0057  237 ALA A N   
2018 C CA  . ALA A 237 ? 0.2405 0.1724 0.2623 -0.0330 0.0183  0.0039  237 ALA A CA  
2019 C C   . ALA A 237 ? 0.2132 0.1329 0.2318 -0.0371 0.0183  -0.0005 237 ALA A C   
2020 O O   . ALA A 237 ? 0.1890 0.1050 0.2049 -0.0423 0.0157  0.0011  237 ALA A O   
2021 C CB  . ALA A 237 ? 0.1897 0.1282 0.2068 -0.0337 0.0196  -0.0002 237 ALA A CB  
2022 N N   . LYS A 238 ? 0.1731 0.0869 0.1920 -0.0345 0.0211  -0.0064 238 LYS A N   
2023 C CA  . LYS A 238 ? 0.2020 0.1030 0.2177 -0.0376 0.0210  -0.0113 238 LYS A CA  
2024 C C   . LYS A 238 ? 0.2602 0.1531 0.2802 -0.0393 0.0178  -0.0060 238 LYS A C   
2025 O O   . LYS A 238 ? 0.2650 0.1498 0.2813 -0.0451 0.0154  -0.0073 238 LYS A O   
2026 C CB  . LYS A 238 ? 0.2267 0.1231 0.2433 -0.0329 0.0249  -0.0183 238 LYS A CB  
2027 C CG  . LYS A 238 ? 0.2614 0.1648 0.2727 -0.0329 0.0284  -0.0244 238 LYS A CG  
2028 C CD  . LYS A 238 ? 0.2509 0.1528 0.2650 -0.0271 0.0329  -0.0306 238 LYS A CD  
2029 C CE  . LYS A 238 ? 0.3846 0.2722 0.3954 -0.0277 0.0336  -0.0371 238 LYS A CE  
2030 N NZ  . LYS A 238 ? 0.4373 0.3240 0.4520 -0.0208 0.0382  -0.0432 238 LYS A NZ  
2031 N N   . GLU A 239 ? 0.2053 0.1006 0.2332 -0.0347 0.0174  0.0003  239 GLU A N   
2032 C CA  . GLU A 239 ? 0.3026 0.1905 0.3353 -0.0365 0.0144  0.0065  239 GLU A CA  
2033 C C   . GLU A 239 ? 0.2177 0.1111 0.2493 -0.0425 0.0112  0.0126  239 GLU A C   
2034 O O   . GLU A 239 ? 0.2571 0.1425 0.2893 -0.0477 0.0084  0.0147  239 GLU A O   
2035 C CB  . GLU A 239 ? 0.3904 0.2811 0.4314 -0.0301 0.0148  0.0126  239 GLU A CB  
2036 C CG  . GLU A 239 ? 0.6557 0.5404 0.6998 -0.0237 0.0174  0.0073  239 GLU A CG  
2037 C CD  . GLU A 239 ? 0.8632 0.7542 0.9151 -0.0168 0.0177  0.0136  239 GLU A CD  
2038 O OE1 . GLU A 239 ? 0.9180 0.8165 0.9722 -0.0173 0.0156  0.0223  239 GLU A OE1 
2039 O OE2 . GLU A 239 ? 0.9090 0.7984 0.9646 -0.0106 0.0199  0.0099  239 GLU A OE2 
2040 N N   . LYS A 240 ? 0.2372 0.1441 0.2676 -0.0417 0.0115  0.0154  240 LYS A N   
2041 C CA  . LYS A 240 ? 0.2471 0.1603 0.2771 -0.0463 0.0088  0.0211  240 LYS A CA  
2042 C C   . LYS A 240 ? 0.2552 0.1634 0.2791 -0.0531 0.0070  0.0167  240 LYS A C   
2043 O O   . LYS A 240 ? 0.2533 0.1599 0.2785 -0.0585 0.0040  0.0205  240 LYS A O   
2044 C CB  . LYS A 240 ? 0.2323 0.1601 0.2618 -0.0432 0.0096  0.0239  240 LYS A CB  
2045 C CG  . LYS A 240 ? 0.1884 0.1242 0.2182 -0.0468 0.0073  0.0296  240 LYS A CG  
2046 C CD  . LYS A 240 ? 0.2098 0.1478 0.2464 -0.0471 0.0060  0.0386  240 LYS A CD  
2047 C CE  . LYS A 240 ? 0.2741 0.2220 0.3119 -0.0502 0.0042  0.0442  240 LYS A CE  
2048 N NZ  . LYS A 240 ? 0.3147 0.2658 0.3592 -0.0514 0.0033  0.0535  240 LYS A NZ  
2049 N N   . TYR A 241 ? 0.2003 0.1068 0.2177 -0.0531 0.0088  0.0089  241 TYR A N   
2050 C CA  . TYR A 241 ? 0.2470 0.1485 0.2573 -0.0594 0.0070  0.0044  241 TYR A CA  
2051 C C   . TYR A 241 ? 0.3174 0.2049 0.3276 -0.0634 0.0052  0.0019  241 TYR A C   
2052 O O   . TYR A 241 ? 0.2645 0.1528 0.2744 -0.0676 0.0015  0.0026  241 TYR A O   
2053 C CB  . TYR A 241 ? 0.2427 0.1456 0.2460 -0.0582 0.0098  -0.0029 241 TYR A CB  
2054 C CG  . TYR A 241 ? 0.3535 0.2529 0.3479 -0.0643 0.0082  -0.0077 241 TYR A CG  
2055 C CD1 . TYR A 241 ? 0.3612 0.2507 0.3520 -0.0667 0.0072  -0.0131 241 TYR A CD1 
2056 C CD2 . TYR A 241 ? 0.3528 0.2606 0.3429 -0.0661 0.0072  -0.0068 241 TYR A CD2 
2057 C CE1 . TYR A 241 ? 0.4278 0.3180 0.4111 -0.0702 0.0053  -0.0169 241 TYR A CE1 
2058 C CE2 . TYR A 241 ? 0.4021 0.3101 0.3852 -0.0693 0.0052  -0.0100 241 TYR A CE2 
2059 C CZ  . TYR A 241 ? 0.4759 0.3755 0.4553 -0.0716 0.0043  -0.0150 241 TYR A CZ  
2060 O OH  . TYR A 241 ? 0.5518 0.4520 0.5232 -0.0751 0.0024  -0.0180 241 TYR A OH  
2061 N N   . PHE A 242 ? 0.2922 0.1709 0.3052 -0.0593 0.0072  -0.0010 242 PHE A N   
2062 C CA  . PHE A 242 ? 0.3010 0.1650 0.3147 -0.0621 0.0051  -0.0035 242 PHE A CA  
2063 C C   . PHE A 242 ? 0.3433 0.2097 0.3645 -0.0653 0.0012  0.0048  242 PHE A C   
2064 O O   . PHE A 242 ? 0.3056 0.1683 0.3272 -0.0690 -0.0010 0.0029  242 PHE A O   
2065 C CB  . PHE A 242 ? 0.3277 0.1835 0.3452 -0.0554 0.0082  -0.0066 242 PHE A CB  
2066 C CG  . PHE A 242 ? 0.4084 0.2478 0.4261 -0.0569 0.0057  -0.0101 242 PHE A CG  
2067 C CD1 . PHE A 242 ? 0.4214 0.2537 0.4315 -0.0581 0.0053  -0.0197 242 PHE A CD1 
2068 C CD2 . PHE A 242 ? 0.4075 0.2405 0.4320 -0.0557 0.0034  -0.0036 242 PHE A CD2 
2069 C CE1 . PHE A 242 ? 0.4841 0.3023 0.4944 -0.0583 0.0023  -0.0234 242 PHE A CE1 
2070 C CE2 . PHE A 242 ? 0.4011 0.2188 0.4234 -0.0566 0.0007  -0.0067 242 PHE A CE2 
2071 C CZ  . PHE A 242 ? 0.3798 0.1898 0.3963 -0.0576 -0.0006 -0.0168 242 PHE A CZ  
2072 N N   . GLU A 243 ? 0.2809 0.1552 0.3068 -0.0635 0.0018  0.0135  243 GLU A N   
2073 C CA  . GLU A 243 ? 0.3598 0.2386 0.3900 -0.0657 -0.0001 0.0211  243 GLU A CA  
2074 C C   . GLU A 243 ? 0.2953 0.1838 0.3240 -0.0702 -0.0020 0.0218  243 GLU A C   
2075 O O   . GLU A 243 ? 0.3447 0.2321 0.3753 -0.0740 -0.0042 0.0238  243 GLU A O   
2076 C CB  . GLU A 243 ? 0.4068 0.2951 0.4433 -0.0615 0.0004  0.0303  243 GLU A CB  
2077 C CG  . GLU A 243 ? 0.5198 0.3998 0.5613 -0.0563 0.0015  0.0316  243 GLU A CG  
2078 C CD  . GLU A 243 ? 0.6112 0.5028 0.6593 -0.0512 0.0027  0.0399  243 GLU A CD  
2079 O OE1 . GLU A 243 ? 0.6156 0.5211 0.6633 -0.0517 0.0029  0.0437  243 GLU A OE1 
2080 O OE2 . GLU A 243 ? 0.6377 0.5246 0.6909 -0.0464 0.0036  0.0424  243 GLU A OE2 
2081 N N   . ILE A 244 ? 0.2945 0.1922 0.3198 -0.0697 -0.0017 0.0203  244 ILE A N   
2082 C CA  . ILE A 244 ? 0.2875 0.1954 0.3118 -0.0728 -0.0040 0.0220  244 ILE A CA  
2083 C C   . ILE A 244 ? 0.3171 0.2191 0.3368 -0.0768 -0.0063 0.0153  244 ILE A C   
2084 O O   . ILE A 244 ? 0.2995 0.2040 0.3203 -0.0808 -0.0092 0.0171  244 ILE A O   
2085 C CB  . ILE A 244 ? 0.2755 0.1945 0.2975 -0.0703 -0.0031 0.0233  244 ILE A CB  
2086 C CG1 . ILE A 244 ? 0.3004 0.2264 0.3273 -0.0662 -0.0014 0.0301  244 ILE A CG1 
2087 C CG2 . ILE A 244 ? 0.2664 0.1947 0.2871 -0.0731 -0.0058 0.0248  244 ILE A CG2 
2088 C CD1 . ILE A 244 ? 0.2723 0.2067 0.3052 -0.0667 -0.0026 0.0383  244 ILE A CD1 
2089 N N   . PHE A 245 ? 0.2794 0.1742 0.2933 -0.0760 -0.0054 0.0077  245 PHE A N   
2090 C CA  . PHE A 245 ? 0.3412 0.2320 0.3483 -0.0794 -0.0077 0.0011  245 PHE A CA  
2091 C C   . PHE A 245 ? 0.3572 0.2338 0.3631 -0.0803 -0.0082 -0.0052 245 PHE A C   
2092 O O   . PHE A 245 ? 0.3697 0.2424 0.3700 -0.0837 -0.0106 -0.0105 245 PHE A O   
2093 C CB  . PHE A 245 ? 0.3624 0.2572 0.3608 -0.0783 -0.0064 -0.0031 245 PHE A CB  
2094 C CG  . PHE A 245 ? 0.3229 0.2305 0.3219 -0.0776 -0.0067 0.0022  245 PHE A CG  
2095 C CD1 . PHE A 245 ? 0.2665 0.1805 0.2645 -0.0808 -0.0102 0.0047  245 PHE A CD1 
2096 C CD2 . PHE A 245 ? 0.3071 0.2198 0.3076 -0.0737 -0.0039 0.0047  245 PHE A CD2 
2097 C CE1 . PHE A 245 ? 0.3038 0.2287 0.3027 -0.0798 -0.0108 0.0094  245 PHE A CE1 
2098 C CE2 . PHE A 245 ? 0.3126 0.2361 0.3137 -0.0728 -0.0045 0.0091  245 PHE A CE2 
2099 C CZ  . PHE A 245 ? 0.2375 0.1669 0.2380 -0.0756 -0.0079 0.0115  245 PHE A CZ  
2100 N N   . GLY A 246 ? 0.2833 0.1517 0.2941 -0.0773 -0.0062 -0.0050 246 GLY A N   
2101 C CA  . GLY A 246 ? 0.3987 0.2528 0.4101 -0.0777 -0.0071 -0.0105 246 GLY A CA  
2102 C C   . GLY A 246 ? 0.3853 0.2301 0.3886 -0.0746 -0.0055 -0.0198 246 GLY A C   
2103 O O   . GLY A 246 ? 0.3553 0.1872 0.3585 -0.0739 -0.0063 -0.0253 246 GLY A O   
2104 N N   . GLU A 247 ? 0.3512 0.2022 0.3474 -0.0726 -0.0022 -0.0223 247 GLU A N   
2105 C CA  . GLU A 247 ? 0.3641 0.2086 0.3525 -0.0692 0.0019  -0.0313 247 GLU A CA  
2106 C C   . GLU A 247 ? 0.4013 0.2531 0.3900 -0.0651 0.0073  -0.0299 247 GLU A C   
2107 O O   . GLU A 247 ? 0.3401 0.2023 0.3322 -0.0657 0.0068  -0.0228 247 GLU A O   
2108 C CB  . GLU A 247 ? 0.4948 0.3399 0.4720 -0.0725 0.0014  -0.0385 247 GLU A CB  
2109 C CG  . GLU A 247 ? 0.6134 0.4719 0.5866 -0.0755 0.0008  -0.0348 247 GLU A CG  
2110 C CD  . GLU A 247 ? 0.7609 0.6197 0.7221 -0.0787 0.0006  -0.0413 247 GLU A CD  
2111 O OE1 . GLU A 247 ? 0.8474 0.6967 0.8032 -0.0785 0.0013  -0.0492 247 GLU A OE1 
2112 O OE2 . GLU A 247 ? 0.7980 0.6665 0.7551 -0.0811 -0.0002 -0.0384 247 GLU A OE2 
2113 N N   . HIS A 248 ? 0.2850 0.1318 0.2711 -0.0607 0.0126  -0.0371 248 HIS A N   
2114 C CA  . HIS A 248 ? 0.3201 0.1765 0.3083 -0.0564 0.0175  -0.0362 248 HIS A CA  
2115 C C   . HIS A 248 ? 0.3290 0.1949 0.3085 -0.0598 0.0185  -0.0382 248 HIS A C   
2116 O O   . HIS A 248 ? 0.3835 0.2460 0.3538 -0.0635 0.0180  -0.0441 248 HIS A O   
2117 C CB  . HIS A 248 ? 0.3668 0.2200 0.3579 -0.0487 0.0225  -0.0420 248 HIS A CB  
2118 C CG  . HIS A 248 ? 0.4935 0.3387 0.4945 -0.0442 0.0215  -0.0384 248 HIS A CG  
2119 N ND1 . HIS A 248 ? 0.5143 0.3671 0.5245 -0.0408 0.0206  -0.0293 248 HIS A ND1 
2120 C CD2 . HIS A 248 ? 0.5129 0.3426 0.5155 -0.0427 0.0208  -0.0424 248 HIS A CD2 
2121 C CE1 . HIS A 248 ? 0.5260 0.3688 0.5432 -0.0376 0.0195  -0.0271 248 HIS A CE1 
2122 N NE2 . HIS A 248 ? 0.5318 0.3600 0.5451 -0.0386 0.0195  -0.0350 248 HIS A NE2 
2123 N N   . PRO A 249 ? 0.2799 0.1586 0.2623 -0.0582 0.0191  -0.0328 249 PRO A N   
2124 C CA  . PRO A 249 ? 0.2599 0.1466 0.2345 -0.0614 0.0196  -0.0341 249 PRO A CA  
2125 C C   . PRO A 249 ? 0.3146 0.2029 0.2845 -0.0588 0.0249  -0.0415 249 PRO A C   
2126 O O   . PRO A 249 ? 0.3825 0.2730 0.3585 -0.0525 0.0286  -0.0429 249 PRO A O   
2127 C CB  . PRO A 249 ? 0.2912 0.1895 0.2717 -0.0593 0.0187  -0.0264 249 PRO A CB  
2128 C CG  . PRO A 249 ? 0.2882 0.1869 0.2784 -0.0525 0.0207  -0.0243 249 PRO A CG  
2129 C CD  . PRO A 249 ? 0.2726 0.1586 0.2649 -0.0527 0.0197  -0.0262 249 PRO A CD  
2130 N N   . VAL A 250 ? 0.3109 0.1993 0.2701 -0.0636 0.0253  -0.0459 250 VAL A N   
2131 C CA  . VAL A 250 ? 0.3279 0.2208 0.2820 -0.0620 0.0306  -0.0519 250 VAL A CA  
2132 C C   . VAL A 250 ? 0.2941 0.1981 0.2448 -0.0645 0.0308  -0.0484 250 VAL A C   
2133 O O   . VAL A 250 ? 0.3000 0.2098 0.2473 -0.0637 0.0353  -0.0520 250 VAL A O   
2134 C CB  . VAL A 250 ? 0.3914 0.2759 0.3347 -0.0649 0.0320  -0.0608 250 VAL A CB  
2135 C CG1 . VAL A 250 ? 0.4487 0.3205 0.3959 -0.0617 0.0319  -0.0651 250 VAL A CG1 
2136 C CG2 . VAL A 250 ? 0.3604 0.2431 0.2936 -0.0731 0.0273  -0.0597 250 VAL A CG2 
2137 N N   . TYR A 251 ? 0.2804 0.1877 0.2326 -0.0674 0.0262  -0.0414 251 TYR A N   
2138 C CA  . TYR A 251 ? 0.3342 0.2504 0.2844 -0.0693 0.0255  -0.0372 251 TYR A CA  
2139 C C   . TYR A 251 ? 0.2763 0.1980 0.2367 -0.0652 0.0241  -0.0309 251 TYR A C   
2140 O O   . TYR A 251 ? 0.2371 0.1560 0.2029 -0.0641 0.0211  -0.0272 251 TYR A O   
2141 C CB  . TYR A 251 ? 0.4039 0.3191 0.3465 -0.0759 0.0207  -0.0346 251 TYR A CB  
2142 C CG  . TYR A 251 ? 0.4627 0.3712 0.3951 -0.0804 0.0204  -0.0402 251 TYR A CG  
2143 C CD1 . TYR A 251 ? 0.5819 0.4898 0.5077 -0.0802 0.0254  -0.0473 251 TYR A CD1 
2144 C CD2 . TYR A 251 ? 0.5467 0.4527 0.4782 -0.0821 0.0149  -0.0376 251 TYR A CD2 
2145 C CE1 . TYR A 251 ? 0.6432 0.5449 0.5587 -0.0840 0.0252  -0.0532 251 TYR A CE1 
2146 C CE2 . TYR A 251 ? 0.5421 0.4430 0.4649 -0.0853 0.0142  -0.0426 251 TYR A CE2 
2147 C CZ  . TYR A 251 ? 0.6565 0.5549 0.5708 -0.0860 0.0193  -0.0505 251 TYR A CZ  
2148 O OH  . TYR A 251 ? 0.7522 0.6459 0.6570 -0.0887 0.0188  -0.0561 251 TYR A OH  
2149 N N   . MET A 252 ? 0.2047 0.1344 0.1674 -0.0632 0.0260  -0.0295 252 MET A N   
2150 C CA  . MET A 252 ? 0.1992 0.1343 0.1699 -0.0597 0.0241  -0.0240 252 MET A CA  
2151 C C   . MET A 252 ? 0.1702 0.1114 0.1383 -0.0619 0.0229  -0.0214 252 MET A C   
2152 O O   . MET A 252 ? 0.1770 0.1205 0.1400 -0.0644 0.0253  -0.0240 252 MET A O   
2153 C CB  . MET A 252 ? 0.2471 0.1854 0.2265 -0.0533 0.0273  -0.0249 252 MET A CB  
2154 C CG  . MET A 252 ? 0.2114 0.1434 0.1962 -0.0500 0.0270  -0.0247 252 MET A CG  
2155 S SD  . MET A 252 ? 0.2609 0.1990 0.2571 -0.0423 0.0284  -0.0220 252 MET A SD  
2156 C CE  . MET A 252 ? 0.3274 0.2559 0.3283 -0.0401 0.0270  -0.0204 252 MET A CE  
2157 N N   . TRP A 253 ? 0.1827 0.1261 0.1539 -0.0610 0.0192  -0.0163 253 TRP A N   
2158 C CA  . TRP A 253 ? 0.1480 0.0962 0.1186 -0.0616 0.0176  -0.0138 253 TRP A CA  
2159 C C   . TRP A 253 ? 0.1547 0.1086 0.1327 -0.0566 0.0191  -0.0133 253 TRP A C   
2160 O O   . TRP A 253 ? 0.1692 0.1243 0.1531 -0.0524 0.0180  -0.0110 253 TRP A O   
2161 C CB  . TRP A 253 ? 0.1450 0.0927 0.1148 -0.0626 0.0128  -0.0091 253 TRP A CB  
2162 C CG  . TRP A 253 ? 0.1404 0.0916 0.1107 -0.0619 0.0109  -0.0068 253 TRP A CG  
2163 C CD1 . TRP A 253 ? 0.1527 0.1071 0.1281 -0.0576 0.0089  -0.0041 253 TRP A CD1 
2164 C CD2 . TRP A 253 ? 0.1457 0.0970 0.1108 -0.0657 0.0106  -0.0071 253 TRP A CD2 
2165 N NE1 . TRP A 253 ? 0.1659 0.1214 0.1398 -0.0583 0.0072  -0.0034 253 TRP A NE1 
2166 C CE2 . TRP A 253 ? 0.1733 0.1267 0.1413 -0.0635 0.0081  -0.0048 253 TRP A CE2 
2167 C CE3 . TRP A 253 ? 0.1882 0.1382 0.1464 -0.0707 0.0124  -0.0090 253 TRP A CE3 
2168 C CZ2 . TRP A 253 ? 0.1882 0.1411 0.1528 -0.0667 0.0068  -0.0040 253 TRP A CZ2 
2169 C CZ3 . TRP A 253 ? 0.1898 0.1416 0.1450 -0.0727 0.0113  -0.0075 253 TRP A CZ3 
2170 C CH2 . TRP A 253 ? 0.2059 0.1587 0.1647 -0.0705 0.0083  -0.0048 253 TRP A CH2 
2171 N N   . PRO A 254 ? 0.1519 0.1100 0.1299 -0.0572 0.0214  -0.0152 254 PRO A N   
2172 C CA  . PRO A 254 ? 0.1819 0.1462 0.1670 -0.0530 0.0219  -0.0146 254 PRO A CA  
2173 C C   . PRO A 254 ? 0.1577 0.1232 0.1435 -0.0523 0.0176  -0.0111 254 PRO A C   
2174 O O   . PRO A 254 ? 0.1628 0.1264 0.1436 -0.0560 0.0154  -0.0099 254 PRO A O   
2175 C CB  . PRO A 254 ? 0.1889 0.1576 0.1732 -0.0554 0.0252  -0.0173 254 PRO A CB  
2176 C CG  . PRO A 254 ? 0.2108 0.1759 0.1861 -0.0616 0.0248  -0.0175 254 PRO A CG  
2177 C CD  . PRO A 254 ? 0.1588 0.1171 0.1302 -0.0622 0.0234  -0.0175 254 PRO A CD  
2178 N N   . PRO A 255 ? 0.1593 0.1276 0.1506 -0.0473 0.0164  -0.0093 255 PRO A N   
2179 C CA  . PRO A 255 ? 0.1544 0.1240 0.1458 -0.0457 0.0126  -0.0068 255 PRO A CA  
2180 C C   . PRO A 255 ? 0.1632 0.1340 0.1529 -0.0482 0.0112  -0.0076 255 PRO A C   
2181 O O   . PRO A 255 ? 0.1535 0.1282 0.1458 -0.0488 0.0131  -0.0095 255 PRO A O   
2182 C CB  . PRO A 255 ? 0.1628 0.1371 0.1603 -0.0399 0.0126  -0.0056 255 PRO A CB  
2183 C CG  . PRO A 255 ? 0.1712 0.1437 0.1712 -0.0388 0.0153  -0.0058 255 PRO A CG  
2184 C CD  . PRO A 255 ? 0.1409 0.1108 0.1380 -0.0427 0.0183  -0.0094 255 PRO A CD  
2185 N N   . GLU A 256 ? 0.1383 0.1056 0.1242 -0.0498 0.0077  -0.0060 256 GLU A N   
2186 C CA  . GLU A 256 ? 0.1324 0.0984 0.1161 -0.0528 0.0055  -0.0061 256 GLU A CA  
2187 C C   . GLU A 256 ? 0.1698 0.1353 0.1504 -0.0587 0.0079  -0.0071 256 GLU A C   
2188 O O   . GLU A 256 ? 0.1745 0.1410 0.1552 -0.0617 0.0073  -0.0074 256 GLU A O   
2189 C CB  . GLU A 256 ? 0.1238 0.0939 0.1118 -0.0496 0.0041  -0.0073 256 GLU A CB  
2190 C CG  . GLU A 256 ? 0.1578 0.1297 0.1480 -0.0433 0.0026  -0.0063 256 GLU A CG  
2191 C CD  . GLU A 256 ? 0.2171 0.1847 0.2040 -0.0422 -0.0012 -0.0049 256 GLU A CD  
2192 O OE1 . GLU A 256 ? 0.4165 0.3786 0.3994 -0.0462 -0.0029 -0.0041 256 GLU A OE1 
2193 O OE2 . GLU A 256 ? 0.2729 0.2429 0.2611 -0.0372 -0.0021 -0.0040 256 GLU A OE2 
2194 N N   . ALA A 257 ? 0.1679 0.1321 0.1456 -0.0607 0.0106  -0.0077 257 ALA A N   
2195 C CA  . ALA A 257 ? 0.1847 0.1497 0.1586 -0.0659 0.0139  -0.0091 257 ALA A CA  
2196 C C   . ALA A 257 ? 0.1756 0.1477 0.1550 -0.0651 0.0176  -0.0115 257 ALA A C   
2197 O O   . ALA A 257 ? 0.2013 0.1764 0.1788 -0.0695 0.0202  -0.0123 257 ALA A O   
2198 C CB  . ALA A 257 ? 0.1614 0.1228 0.1292 -0.0716 0.0112  -0.0067 257 ALA A CB  
2199 N N   . SER A 258 ? 0.1545 0.1306 0.1410 -0.0596 0.0180  -0.0124 258 SER A N   
2200 C CA  . SER A 258 ? 0.1296 0.1134 0.1224 -0.0587 0.0197  -0.0138 258 SER A CA  
2201 C C   . SER A 258 ? 0.1316 0.1201 0.1268 -0.0580 0.0254  -0.0166 258 SER A C   
2202 O O   . SER A 258 ? 0.1628 0.1494 0.1593 -0.0541 0.0272  -0.0179 258 SER A O   
2203 C CB  . SER A 258 ? 0.1629 0.1499 0.1619 -0.0531 0.0173  -0.0133 258 SER A CB  
2204 O OG  . SER A 258 ? 0.2391 0.2340 0.2440 -0.0532 0.0181  -0.0143 258 SER A OG  
2205 N N   . VAL A 259 ? 0.1402 0.1344 0.1360 -0.0619 0.0281  -0.0175 259 VAL A N   
2206 C CA  . VAL A 259 ? 0.1378 0.1378 0.1361 -0.0609 0.0340  -0.0207 259 VAL A CA  
2207 C C   . VAL A 259 ? 0.1657 0.1768 0.1718 -0.0614 0.0356  -0.0209 259 VAL A C   
2208 O O   . VAL A 259 ? 0.1950 0.2083 0.2027 -0.0645 0.0322  -0.0186 259 VAL A O   
2209 C CB  . VAL A 259 ? 0.1639 0.1613 0.1535 -0.0658 0.0373  -0.0221 259 VAL A CB  
2210 C CG1 . VAL A 259 ? 0.2128 0.1999 0.1954 -0.0653 0.0355  -0.0223 259 VAL A CG1 
2211 C CG2 . VAL A 259 ? 0.2120 0.2108 0.1970 -0.0732 0.0359  -0.0193 259 VAL A CG2 
2212 N N   . SER A 260 ? 0.1602 0.1784 0.1717 -0.0580 0.0407  -0.0237 260 SER A N   
2213 C CA  . SER A 260 ? 0.1369 0.1680 0.1568 -0.0583 0.0435  -0.0243 260 SER A CA  
2214 C C   . SER A 260 ? 0.1420 0.1773 0.1631 -0.0554 0.0503  -0.0283 260 SER A C   
2215 O O   . SER A 260 ? 0.1592 0.1864 0.1755 -0.0526 0.0517  -0.0307 260 SER A O   
2216 C CB  . SER A 260 ? 0.1541 0.1906 0.1839 -0.0533 0.0404  -0.0232 260 SER A CB  
2217 O OG  . SER A 260 ? 0.1764 0.2110 0.2099 -0.0457 0.0418  -0.0248 260 SER A OG  
2218 N N   . ASN A 261 ? 0.1542 0.2027 0.1821 -0.0559 0.0546  -0.0293 261 ASN A N   
2219 C CA  . ASN A 261 ? 0.2351 0.2886 0.2651 -0.0518 0.0615  -0.0338 261 ASN A CA  
2220 C C   . ASN A 261 ? 0.2262 0.2756 0.2619 -0.0427 0.0615  -0.0360 261 ASN A C   
2221 O O   . ASN A 261 ? 0.1536 0.1967 0.1855 -0.0393 0.0648  -0.0400 261 ASN A O   
2222 C CB  . ASN A 261 ? 0.1502 0.2209 0.1888 -0.0531 0.0661  -0.0341 261 ASN A CB  
2223 C CG  . ASN A 261 ? 0.1746 0.2495 0.2066 -0.0624 0.0676  -0.0321 261 ASN A CG  
2224 O OD1 . ASN A 261 ? 0.2044 0.2703 0.2243 -0.0665 0.0679  -0.0324 261 ASN A OD1 
2225 N ND2 . ASN A 261 ? 0.2021 0.2906 0.2419 -0.0663 0.0682  -0.0294 261 ASN A ND2 
2226 N N   . GLU A 262 ? 0.1698 0.2218 0.2139 -0.0389 0.0573  -0.0333 262 GLU A N   
2227 C CA  . GLU A 262 ? 0.1768 0.2250 0.2266 -0.0305 0.0568  -0.0342 262 GLU A CA  
2228 C C   . GLU A 262 ? 0.1803 0.2128 0.2219 -0.0299 0.0538  -0.0337 262 GLU A C   
2229 O O   . GLU A 262 ? 0.1699 0.1959 0.2125 -0.0245 0.0553  -0.0359 262 GLU A O   
2230 C CB  . GLU A 262 ? 0.2391 0.2956 0.2993 -0.0271 0.0529  -0.0308 262 GLU A CB  
2231 C CG  . GLU A 262 ? 0.2929 0.3665 0.3628 -0.0279 0.0555  -0.0309 262 GLU A CG  
2232 C CD  . GLU A 262 ? 0.4554 0.5380 0.5362 -0.0241 0.0515  -0.0280 262 GLU A CD  
2233 O OE1 . GLU A 262 ? 0.5145 0.6071 0.5994 -0.0286 0.0493  -0.0260 262 GLU A OE1 
2234 O OE2 . GLU A 262 ? 0.5160 0.5953 0.6009 -0.0169 0.0500  -0.0273 262 GLU A OE2 
2235 N N   . ALA A 263 ? 0.1487 0.1748 0.1827 -0.0353 0.0493  -0.0309 263 ALA A N   
2236 C CA  . ALA A 263 ? 0.1685 0.1814 0.1954 -0.0352 0.0465  -0.0301 263 ALA A CA  
2237 C C   . ALA A 263 ? 0.1827 0.1884 0.2016 -0.0370 0.0502  -0.0341 263 ALA A C   
2238 O O   . ALA A 263 ? 0.1715 0.1676 0.1883 -0.0343 0.0497  -0.0352 263 ALA A O   
2239 C CB  . ALA A 263 ? 0.1348 0.1438 0.1560 -0.0400 0.0412  -0.0264 263 ALA A CB  
2240 N N   . LEU A 264 ? 0.1854 0.1954 0.1994 -0.0420 0.0536  -0.0361 264 LEU A N   
2241 C CA  . LEU A 264 ? 0.1959 0.2000 0.2012 -0.0437 0.0572  -0.0406 264 LEU A CA  
2242 C C   . LEU A 264 ? 0.2205 0.2242 0.2308 -0.0367 0.0617  -0.0456 264 LEU A C   
2243 O O   . LEU A 264 ? 0.1879 0.1811 0.1928 -0.0356 0.0622  -0.0490 264 LEU A O   
2244 C CB  . LEU A 264 ? 0.2102 0.2211 0.2094 -0.0503 0.0603  -0.0413 264 LEU A CB  
2245 C CG  . LEU A 264 ? 0.2138 0.2210 0.2057 -0.0576 0.0555  -0.0365 264 LEU A CG  
2246 C CD1 . LEU A 264 ? 0.1968 0.2122 0.1846 -0.0642 0.0583  -0.0357 264 LEU A CD1 
2247 C CD2 . LEU A 264 ? 0.2798 0.2742 0.2620 -0.0595 0.0524  -0.0367 264 LEU A CD2 
2248 N N   . GLU A 265 ? 0.1797 0.1944 0.2007 -0.0319 0.0646  -0.0462 265 GLU A N   
2249 C CA  . GLU A 265 ? 0.2486 0.2628 0.2761 -0.0240 0.0685  -0.0506 265 GLU A CA  
2250 C C   . GLU A 265 ? 0.1858 0.1876 0.2152 -0.0194 0.0644  -0.0492 265 GLU A C   
2251 O O   . GLU A 265 ? 0.2307 0.2234 0.2586 -0.0158 0.0663  -0.0534 265 GLU A O   
2252 C CB  . GLU A 265 ? 0.2661 0.2956 0.3065 -0.0192 0.0713  -0.0503 265 GLU A CB  
2253 C CG  . GLU A 265 ? 0.5567 0.5849 0.6054 -0.0097 0.0744  -0.0541 265 GLU A CG  
2254 C CD  . GLU A 265 ? 0.7135 0.7422 0.7584 -0.0077 0.0816  -0.0617 265 GLU A CD  
2255 O OE1 . GLU A 265 ? 0.7713 0.7982 0.8228 0.0006  0.0844  -0.0657 265 GLU A OE1 
2256 O OE2 . GLU A 265 ? 0.7465 0.7776 0.7818 -0.0141 0.0844  -0.0638 265 GLU A OE2 
2257 N N   . LEU A 266 ? 0.2006 0.2020 0.2332 -0.0198 0.0589  -0.0432 266 LEU A N   
2258 C CA  . LEU A 266 ? 0.1710 0.1622 0.2057 -0.0159 0.0551  -0.0407 266 LEU A CA  
2259 C C   . LEU A 266 ? 0.1873 0.1645 0.2118 -0.0197 0.0537  -0.0422 266 LEU A C   
2260 O O   . LEU A 266 ? 0.1937 0.1609 0.2190 -0.0163 0.0536  -0.0438 266 LEU A O   
2261 C CB  . LEU A 266 ? 0.1730 0.1680 0.2115 -0.0160 0.0498  -0.0341 266 LEU A CB  
2262 C CG  . LEU A 266 ? 0.1496 0.1355 0.1894 -0.0131 0.0458  -0.0302 266 LEU A CG  
2263 C CD1 . LEU A 266 ? 0.1555 0.1391 0.2038 -0.0053 0.0476  -0.0312 266 LEU A CD1 
2264 C CD2 . LEU A 266 ? 0.1750 0.1658 0.2166 -0.0136 0.0409  -0.0242 266 LEU A CD2 
2265 N N   . TYR A 267 ? 0.1969 0.1730 0.2122 -0.0269 0.0521  -0.0413 267 TYR A N   
2266 C CA  . TYR A 267 ? 0.2175 0.1816 0.2231 -0.0311 0.0503  -0.0425 267 TYR A CA  
2267 C C   . TYR A 267 ? 0.2315 0.1897 0.2329 -0.0299 0.0547  -0.0498 267 TYR A C   
2268 O O   . TYR A 267 ? 0.2245 0.1709 0.2229 -0.0297 0.0532  -0.0516 267 TYR A O   
2269 C CB  . TYR A 267 ? 0.1821 0.1475 0.1789 -0.0387 0.0481  -0.0405 267 TYR A CB  
2270 C CG  . TYR A 267 ? 0.1797 0.1465 0.1784 -0.0400 0.0428  -0.0340 267 TYR A CG  
2271 C CD1 . TYR A 267 ? 0.2231 0.1829 0.2226 -0.0389 0.0388  -0.0306 267 TYR A CD1 
2272 C CD2 . TYR A 267 ? 0.1810 0.1561 0.1805 -0.0424 0.0418  -0.0314 267 TYR A CD2 
2273 C CE1 . TYR A 267 ? 0.2224 0.1844 0.2233 -0.0395 0.0345  -0.0251 267 TYR A CE1 
2274 C CE2 . TYR A 267 ? 0.1751 0.1508 0.1757 -0.0430 0.0369  -0.0263 267 TYR A CE2 
2275 C CZ  . TYR A 267 ? 0.2439 0.2135 0.2451 -0.0412 0.0336  -0.0235 267 TYR A CZ  
2276 O OH  . TYR A 267 ? 0.1755 0.1465 0.1775 -0.0411 0.0294  -0.0190 267 TYR A OH  
2277 N N   . TYR A 268 ? 0.2071 0.1736 0.2081 -0.0294 0.0601  -0.0543 268 TYR A N   
2278 C CA  . TYR A 268 ? 0.2250 0.1871 0.2221 -0.0271 0.0650  -0.0622 268 TYR A CA  
2279 C C   . TYR A 268 ? 0.2436 0.1984 0.2489 -0.0190 0.0655  -0.0643 268 TYR A C   
2280 O O   . TYR A 268 ? 0.2326 0.1750 0.2334 -0.0181 0.0657  -0.0692 268 TYR A O   
2281 C CB  . TYR A 268 ? 0.2653 0.2409 0.2628 -0.0269 0.0713  -0.0657 268 TYR A CB  
2282 C CG  . TYR A 268 ? 0.2467 0.2205 0.2443 -0.0213 0.0773  -0.0740 268 TYR A CG  
2283 C CD1 . TYR A 268 ? 0.2961 0.2600 0.2819 -0.0237 0.0787  -0.0804 268 TYR A CD1 
2284 C CD2 . TYR A 268 ? 0.2982 0.2802 0.3079 -0.0132 0.0812  -0.0757 268 TYR A CD2 
2285 C CE1 . TYR A 268 ? 0.3555 0.3170 0.3407 -0.0180 0.0842  -0.0890 268 TYR A CE1 
2286 C CE2 . TYR A 268 ? 0.2996 0.2798 0.3098 -0.0070 0.0868  -0.0839 268 TYR A CE2 
2287 C CZ  . TYR A 268 ? 0.3597 0.3291 0.3573 -0.0094 0.0884  -0.0908 268 TYR A CZ  
2288 O OH  . TYR A 268 ? 0.4125 0.3791 0.4097 -0.0029 0.0940  -0.0998 268 TYR A OH  
2289 N N   . GLU A 269 ? 0.2310 0.1932 0.2486 -0.0132 0.0653  -0.0607 269 GLU A N   
2290 C CA  . GLU A 269 ? 0.2941 0.2502 0.3206 -0.0050 0.0655  -0.0617 269 GLU A CA  
2291 C C   . GLU A 269 ? 0.2714 0.2124 0.2961 -0.0060 0.0601  -0.0586 269 GLU A C   
2292 O O   . GLU A 269 ? 0.3072 0.2375 0.3352 -0.0011 0.0602  -0.0612 269 GLU A O   
2293 C CB  . GLU A 269 ? 0.3105 0.2788 0.3501 0.0006  0.0652  -0.0570 269 GLU A CB  
2294 C CG  . GLU A 269 ? 0.3495 0.3335 0.3943 0.0031  0.0709  -0.0603 269 GLU A CG  
2295 C CD  . GLU A 269 ? 0.4682 0.4655 0.5255 0.0070  0.0694  -0.0548 269 GLU A CD  
2296 O OE1 . GLU A 269 ? 0.4909 0.4861 0.5507 0.0066  0.0639  -0.0483 269 GLU A OE1 
2297 O OE2 . GLU A 269 ? 0.4791 0.4898 0.5436 0.0104  0.0738  -0.0570 269 GLU A OE2 
2298 N N   . LYS A 270 ? 0.2444 0.1846 0.2648 -0.0121 0.0554  -0.0528 270 LYS A N   
2299 C CA  . LYS A 270 ? 0.2480 0.1762 0.2670 -0.0140 0.0503  -0.0490 270 LYS A CA  
2300 C C   . LYS A 270 ? 0.3148 0.2319 0.3224 -0.0202 0.0494  -0.0531 270 LYS A C   
2301 O O   . LYS A 270 ? 0.3052 0.2140 0.3108 -0.0237 0.0448  -0.0495 270 LYS A O   
2302 C CB  . LYS A 270 ? 0.2332 0.1677 0.2542 -0.0165 0.0458  -0.0406 270 LYS A CB  
2303 C CG  . LYS A 270 ? 0.2269 0.1710 0.2588 -0.0104 0.0457  -0.0363 270 LYS A CG  
2304 C CD  . LYS A 270 ? 0.3655 0.3014 0.4048 -0.0043 0.0448  -0.0346 270 LYS A CD  
2305 C CE  . LYS A 270 ? 0.5246 0.4703 0.5745 0.0020  0.0442  -0.0299 270 LYS A CE  
2306 N NZ  . LYS A 270 ? 0.6230 0.5599 0.6799 0.0076  0.0425  -0.0268 270 LYS A NZ  
2307 N N   . GLY A 271 ? 0.2750 0.1928 0.2752 -0.0218 0.0535  -0.0605 271 GLY A N   
2308 C CA  . GLY A 271 ? 0.2636 0.1701 0.2526 -0.0270 0.0526  -0.0655 271 GLY A CA  
2309 C C   . GLY A 271 ? 0.2940 0.2024 0.2735 -0.0356 0.0494  -0.0627 271 GLY A C   
2310 O O   . GLY A 271 ? 0.3411 0.2400 0.3121 -0.0405 0.0471  -0.0653 271 GLY A O   
2311 N N   . ILE A 272 ? 0.2388 0.1589 0.2196 -0.0376 0.0489  -0.0575 272 ILE A N   
2312 C CA  . ILE A 272 ? 0.2384 0.1607 0.2107 -0.0451 0.0459  -0.0545 272 ILE A CA  
2313 C C   . ILE A 272 ? 0.3097 0.2352 0.2717 -0.0487 0.0498  -0.0602 272 ILE A C   
2314 O O   . ILE A 272 ? 0.3248 0.2590 0.2890 -0.0459 0.0550  -0.0630 272 ILE A O   
2315 C CB  . ILE A 272 ? 0.2489 0.1811 0.2265 -0.0453 0.0437  -0.0471 272 ILE A CB  
2316 C CG1 . ILE A 272 ? 0.2648 0.1950 0.2521 -0.0412 0.0404  -0.0416 272 ILE A CG1 
2317 C CG2 . ILE A 272 ? 0.2578 0.1915 0.2272 -0.0524 0.0404  -0.0439 272 ILE A CG2 
2318 C CD1 . ILE A 272 ? 0.3097 0.2288 0.2954 -0.0433 0.0364  -0.0401 272 ILE A CD1 
2319 N N   . ASN A 273 ? 0.2967 0.2162 0.2476 -0.0551 0.0473  -0.0617 273 ASN A N   
2320 C CA  . ASN A 273 ? 0.3457 0.2675 0.2850 -0.0588 0.0509  -0.0674 273 ASN A CA  
2321 C C   . ASN A 273 ? 0.3572 0.2880 0.2912 -0.0646 0.0499  -0.0626 273 ASN A C   
2322 O O   . ASN A 273 ? 0.3183 0.2558 0.2457 -0.0666 0.0542  -0.0655 273 ASN A O   
2323 C CB  . ASN A 273 ? 0.4077 0.3176 0.3366 -0.0626 0.0487  -0.0726 273 ASN A CB  
2324 C CG  . ASN A 273 ? 0.6137 0.5135 0.5460 -0.0571 0.0506  -0.0794 273 ASN A CG  
2325 O OD1 . ASN A 273 ? 0.6595 0.5629 0.5974 -0.0505 0.0561  -0.0834 273 ASN A OD1 
2326 N ND2 . ASN A 273 ? 0.6574 0.5445 0.5867 -0.0596 0.0460  -0.0807 273 ASN A ND2 
2327 N N   A MET A 274 ? 0.3094 0.2404 0.2458 -0.0672 0.0444  -0.0552 274 MET A N   
2328 N N   B MET A 274 ? 0.3132 0.2443 0.2498 -0.0671 0.0444  -0.0551 274 MET A N   
2329 C CA  A MET A 274 ? 0.3033 0.2409 0.2351 -0.0724 0.0427  -0.0502 274 MET A CA  
2330 C CA  B MET A 274 ? 0.3071 0.2445 0.2388 -0.0725 0.0426  -0.0502 274 MET A CA  
2331 C C   A MET A 274 ? 0.2924 0.2323 0.2328 -0.0711 0.0383  -0.0428 274 MET A C   
2332 C C   B MET A 274 ? 0.2897 0.2295 0.2298 -0.0712 0.0382  -0.0427 274 MET A C   
2333 O O   A MET A 274 ? 0.2744 0.2092 0.2200 -0.0690 0.0348  -0.0405 274 MET A O   
2334 O O   B MET A 274 ? 0.2742 0.2089 0.2195 -0.0691 0.0347  -0.0404 274 MET A O   
2335 C CB  A MET A 274 ? 0.3403 0.2732 0.2592 -0.0794 0.0394  -0.0504 274 MET A CB  
2336 C CB  B MET A 274 ? 0.3367 0.2689 0.2557 -0.0793 0.0392  -0.0506 274 MET A CB  
2337 C CG  A MET A 274 ? 0.3351 0.2740 0.2489 -0.0847 0.0373  -0.0449 274 MET A CG  
2338 C CG  B MET A 274 ? 0.3406 0.2783 0.2537 -0.0849 0.0369  -0.0452 274 MET A CG  
2339 S SD  A MET A 274 ? 0.3378 0.2750 0.2572 -0.0856 0.0296  -0.0361 274 MET A SD  
2340 S SD  B MET A 274 ? 0.3699 0.3014 0.2702 -0.0923 0.0311  -0.0439 274 MET A SD  
2341 C CE  A MET A 274 ? 0.3352 0.2643 0.2449 -0.0909 0.0244  -0.0366 274 MET A CE  
2342 C CE  B MET A 274 ? 0.3356 0.2642 0.2449 -0.0913 0.0238  -0.0364 274 MET A CE  
2343 N N   . LEU A 275 ? 0.1925 0.1402 0.1340 -0.0726 0.0385  -0.0390 275 LEU A N   
2344 C CA  . LEU A 275 ? 0.2242 0.1735 0.1711 -0.0723 0.0340  -0.0325 275 LEU A CA  
2345 C C   . LEU A 275 ? 0.2418 0.1943 0.1823 -0.0779 0.0323  -0.0291 275 LEU A C   
2346 O O   . LEU A 275 ? 0.2548 0.2094 0.1873 -0.0820 0.0351  -0.0313 275 LEU A O   
2347 C CB  . LEU A 275 ? 0.2800 0.2350 0.2384 -0.0665 0.0355  -0.0315 275 LEU A CB  
2348 C CG  . LEU A 275 ? 0.3950 0.3586 0.3573 -0.0648 0.0407  -0.0340 275 LEU A CG  
2349 C CD1 . LEU A 275 ? 0.4574 0.4273 0.4184 -0.0691 0.0398  -0.0303 275 LEU A CD1 
2350 C CD2 . LEU A 275 ? 0.3640 0.3305 0.3378 -0.0578 0.0418  -0.0341 275 LEU A CD2 
2351 N N   . ALA A 276 ? 0.2155 0.1681 0.1590 -0.0781 0.0277  -0.0237 276 ALA A N   
2352 C CA  . ALA A 276 ? 0.2171 0.1719 0.1563 -0.0828 0.0257  -0.0198 276 ALA A CA  
2353 C C   . ALA A 276 ? 0.2396 0.1986 0.1871 -0.0801 0.0247  -0.0169 276 ALA A C   
2354 O O   . ALA A 276 ? 0.2044 0.1641 0.1601 -0.0747 0.0243  -0.0171 276 ALA A O   
2355 C CB  . ALA A 276 ? 0.2114 0.1609 0.1446 -0.0863 0.0200  -0.0159 276 ALA A CB  
2356 N N   . THR A 277 ? 0.1686 0.1301 0.1138 -0.0842 0.0239  -0.0142 277 THR A N   
2357 C CA  . THR A 277 ? 0.1805 0.1447 0.1325 -0.0828 0.0220  -0.0116 277 THR A CA  
2358 C C   . THR A 277 ? 0.2127 0.1755 0.1598 -0.0856 0.0178  -0.0071 277 THR A C   
2359 O O   . THR A 277 ? 0.2298 0.1889 0.1693 -0.0877 0.0155  -0.0053 277 THR A O   
2360 C CB  . THR A 277 ? 0.2310 0.2034 0.1898 -0.0809 0.0267  -0.0144 277 THR A CB  
2361 O OG1 . THR A 277 ? 0.2213 0.1961 0.1862 -0.0802 0.0241  -0.0120 277 THR A OG1 
2362 C CG2 . THR A 277 ? 0.2693 0.2470 0.2232 -0.0858 0.0316  -0.0159 277 THR A CG2 
2363 N N   . ASP A 278 ? 0.1856 0.1507 0.1372 -0.0853 0.0161  -0.0051 278 ASP A N   
2364 C CA  . ASP A 278 ? 0.2175 0.1793 0.1661 -0.0866 0.0111  -0.0006 278 ASP A CA  
2365 C C   . ASP A 278 ? 0.2259 0.1912 0.1704 -0.0923 0.0129  0.0011  278 ASP A C   
2366 O O   . ASP A 278 ? 0.2399 0.2121 0.1870 -0.0947 0.0177  -0.0009 278 ASP A O   
2367 C CB  . ASP A 278 ? 0.2140 0.1742 0.1697 -0.0829 0.0073  0.0005  278 ASP A CB  
2368 C CG  . ASP A 278 ? 0.2573 0.2121 0.2105 -0.0837 0.0020  0.0045  278 ASP A CG  
2369 O OD1 . ASP A 278 ? 0.2527 0.2030 0.2009 -0.0835 -0.0008 0.0067  278 ASP A OD1 
2370 O OD2 . ASP A 278 ? 0.2853 0.2401 0.2420 -0.0845 0.0002  0.0055  278 ASP A OD2 
2371 N N   . GLU A 279 ? 0.1945 0.1556 0.1333 -0.0946 0.0088  0.0053  279 GLU A N   
2372 C CA  . GLU A 279 ? 0.2027 0.1665 0.1370 -0.1003 0.0097  0.0081  279 GLU A CA  
2373 C C   . GLU A 279 ? 0.2186 0.1861 0.1601 -0.1012 0.0097  0.0090  279 GLU A C   
2374 O O   . GLU A 279 ? 0.2614 0.2351 0.2019 -0.1059 0.0129  0.0099  279 GLU A O   
2375 C CB  . GLU A 279 ? 0.2590 0.2165 0.1866 -0.1021 0.0043  0.0129  279 GLU A CB  
2376 C CG  . GLU A 279 ? 0.3305 0.2904 0.2517 -0.1086 0.0048  0.0164  279 GLU A CG  
2377 C CD  . GLU A 279 ? 0.3943 0.3481 0.3079 -0.1106 -0.0004 0.0211  279 GLU A CD  
2378 O OE1 . GLU A 279 ? 0.2977 0.2457 0.2114 -0.1069 -0.0045 0.0217  279 GLU A OE1 
2379 O OE2 . GLU A 279 ? 0.3757 0.3312 0.2835 -0.1161 -0.0006 0.0246  279 GLU A OE2 
2380 N N   . VAL A 280 ? 0.2260 0.1902 0.1747 -0.0970 0.0063  0.0088  280 VAL A N   
2381 C CA  . VAL A 280 ? 0.2453 0.2129 0.2009 -0.0984 0.0059  0.0093  280 VAL A CA  
2382 C C   . VAL A 280 ? 0.2673 0.2454 0.2277 -0.0997 0.0120  0.0060  280 VAL A C   
2383 O O   . VAL A 280 ? 0.2750 0.2597 0.2385 -0.1036 0.0138  0.0073  280 VAL A O   
2384 C CB  . VAL A 280 ? 0.3362 0.2982 0.2977 -0.0938 0.0011  0.0087  280 VAL A CB  
2385 C CG1 . VAL A 280 ? 0.3221 0.2885 0.2911 -0.0954 0.0009  0.0080  280 VAL A CG1 
2386 C CG2 . VAL A 280 ? 0.3264 0.2785 0.2841 -0.0930 -0.0048 0.0121  280 VAL A CG2 
2387 N N   . ILE A 281 ? 0.2531 0.2334 0.2148 -0.0965 0.0154  0.0020  281 ILE A N   
2388 C CA  . ILE A 281 ? 0.2125 0.2030 0.1792 -0.0973 0.0219  -0.0016 281 ILE A CA  
2389 C C   . ILE A 281 ? 0.2647 0.2618 0.2263 -0.1025 0.0270  -0.0011 281 ILE A C   
2390 O O   . ILE A 281 ? 0.2366 0.2442 0.2035 -0.1047 0.0311  -0.0017 281 ILE A O   
2391 C CB  . ILE A 281 ? 0.2009 0.1905 0.1689 -0.0931 0.0246  -0.0059 281 ILE A CB  
2392 C CG1 . ILE A 281 ? 0.3530 0.3368 0.3254 -0.0880 0.0197  -0.0060 281 ILE A CG1 
2393 C CG2 . ILE A 281 ? 0.2382 0.2385 0.2124 -0.0932 0.0319  -0.0099 281 ILE A CG2 
2394 C CD1 . ILE A 281 ? 0.4173 0.4053 0.3980 -0.0874 0.0178  -0.0060 281 ILE A CD1 
2395 N N   . LEU A 282 ? 0.2170 0.2094 0.1685 -0.1045 0.0267  -0.0001 282 LEU A N   
2396 C CA  . LEU A 282 ? 0.2431 0.2419 0.1881 -0.1096 0.0315  0.0002  282 LEU A CA  
2397 C C   . LEU A 282 ? 0.2206 0.2237 0.1674 -0.1138 0.0300  0.0049  282 LEU A C   
2398 O O   . LEU A 282 ? 0.2167 0.2306 0.1654 -0.1168 0.0352  0.0046  282 LEU A O   
2399 C CB  . LEU A 282 ? 0.2237 0.2158 0.1567 -0.1115 0.0301  0.0009  282 LEU A CB  
2400 C CG  . LEU A 282 ? 0.2486 0.2472 0.1729 -0.1169 0.0352  0.0006  282 LEU A CG  
2401 C CD1 . LEU A 282 ? 0.2487 0.2572 0.1753 -0.1161 0.0442  -0.0055 282 LEU A CD1 
2402 C CD2 . LEU A 282 ? 0.2521 0.2436 0.1639 -0.1194 0.0325  0.0018  282 LEU A CD2 
2403 N N   . LYS A 283 ? 0.2151 0.2099 0.1616 -0.1139 0.0230  0.0094  283 LYS A N   
2404 C CA  . LYS A 283 ? 0.2518 0.2488 0.2001 -0.1183 0.0210  0.0142  283 LYS A CA  
2405 C C   . LYS A 283 ? 0.2373 0.2431 0.1967 -0.1184 0.0231  0.0131  283 LYS A C   
2406 O O   . LYS A 283 ? 0.2406 0.2542 0.2022 -0.1230 0.0250  0.0158  283 LYS A O   
2407 C CB  . LYS A 283 ? 0.2631 0.2482 0.2100 -0.1176 0.0131  0.0184  283 LYS A CB  
2408 C CG  . LYS A 283 ? 0.3978 0.3757 0.3341 -0.1185 0.0103  0.0209  283 LYS A CG  
2409 C CD  . LYS A 283 ? 0.5185 0.4848 0.4553 -0.1158 0.0029  0.0238  283 LYS A CD  
2410 C CE  . LYS A 283 ? 0.6477 0.6112 0.5861 -0.1196 -0.0008 0.0289  283 LYS A CE  
2411 N NZ  . LYS A 283 ? 0.7327 0.6966 0.6625 -0.1254 -0.0011 0.0338  283 LYS A NZ  
2412 N N   . ASN A 284 ? 0.2162 0.2218 0.1829 -0.1137 0.0226  0.0095  284 ASN A N   
2413 C CA  . ASN A 284 ? 0.2178 0.2327 0.1955 -0.1137 0.0242  0.0082  284 ASN A CA  
2414 C C   . ASN A 284 ? 0.2768 0.3060 0.2579 -0.1144 0.0324  0.0053  284 ASN A C   
2415 O O   . ASN A 284 ? 0.2748 0.3146 0.2654 -0.1154 0.0343  0.0052  284 ASN A O   
2416 C CB  . ASN A 284 ? 0.2299 0.2409 0.2140 -0.1084 0.0211  0.0052  284 ASN A CB  
2417 C CG  . ASN A 284 ? 0.3145 0.3136 0.2979 -0.1073 0.0134  0.0074  284 ASN A CG  
2418 O OD1 . ASN A 284 ? 0.2723 0.2671 0.2530 -0.1109 0.0102  0.0115  284 ASN A OD1 
2419 N ND2 . ASN A 284 ? 0.2862 0.2806 0.2726 -0.1023 0.0105  0.0047  284 ASN A ND2 
2420 N N   . SER A 285 ? 0.2411 0.2713 0.2151 -0.1138 0.0373  0.0026  285 SER A N   
2421 C CA  . SER A 285 ? 0.2398 0.2826 0.2171 -0.1125 0.0457  -0.0018 285 SER A CA  
2422 C C   . SER A 285 ? 0.3190 0.3698 0.2900 -0.1166 0.0510  -0.0009 285 SER A C   
2423 O O   . SER A 285 ? 0.3326 0.3969 0.3090 -0.1157 0.0578  -0.0036 285 SER A O   
2424 C CB  . SER A 285 ? 0.2998 0.3377 0.2743 -0.1079 0.0484  -0.0072 285 SER A CB  
2425 O OG  . SER A 285 ? 0.2829 0.3147 0.2635 -0.1038 0.0440  -0.0081 285 SER A OG  
2426 N N   . VAL A 286 ? 0.2806 0.3242 0.2407 -0.1205 0.0482  0.0026  286 VAL A N   
2427 C CA  . VAL A 286 ? 0.2830 0.3343 0.2360 -0.1246 0.0529  0.0037  286 VAL A CA  
2428 C C   . VAL A 286 ? 0.2840 0.3308 0.2324 -0.1302 0.0475  0.0109  286 VAL A C   
2429 O O   . VAL A 286 ? 0.3016 0.3368 0.2496 -0.1302 0.0401  0.0143  286 VAL A O   
2430 C CB  . VAL A 286 ? 0.3247 0.3730 0.2661 -0.1238 0.0566  -0.0006 286 VAL A CB  
2431 C CG1 . VAL A 286 ? 0.3043 0.3542 0.2498 -0.1178 0.0616  -0.0081 286 VAL A CG1 
2432 C CG2 . VAL A 286 ? 0.3386 0.3723 0.2699 -0.1255 0.0497  0.0024  286 VAL A CG2 
2433 N N   . GLU A 287 ? 0.3024 0.3585 0.2471 -0.1346 0.0514  0.0133  287 GLU A N   
2434 C CA  . GLU A 287 ? 0.3133 0.3658 0.2536 -0.1404 0.0468  0.0207  287 GLU A CA  
2435 C C   . GLU A 287 ? 0.3296 0.3708 0.2568 -0.1419 0.0427  0.0224  287 GLU A C   
2436 O O   . GLU A 287 ? 0.3656 0.3953 0.2913 -0.1427 0.0353  0.0267  287 GLU A O   
2437 C CB  . GLU A 287 ? 0.3374 0.4048 0.2788 -0.1449 0.0524  0.0232  287 GLU A CB  
2438 C CG  . GLU A 287 ? 0.3479 0.4276 0.3034 -0.1438 0.0558  0.0224  287 GLU A CG  
2439 C CD  . GLU A 287 ? 0.4883 0.5822 0.4457 -0.1487 0.0604  0.0263  287 GLU A CD  
2440 O OE1 . GLU A 287 ? 0.4691 0.5628 0.4163 -0.1529 0.0609  0.0297  287 GLU A OE1 
2441 O OE2 . GLU A 287 ? 0.5729 0.6786 0.5422 -0.1483 0.0633  0.0262  287 GLU A OE2 
2442 N N   . ARG A 288 ? 0.2811 0.3254 0.1989 -0.1419 0.0474  0.0188  288 ARG A N   
2443 C CA  . ARG A 288 ? 0.2942 0.3297 0.1990 -0.1441 0.0438  0.0205  288 ARG A CA  
2444 C C   . ARG A 288 ? 0.2878 0.3129 0.1908 -0.1393 0.0414  0.0158  288 ARG A C   
2445 O O   . ARG A 288 ? 0.3493 0.3763 0.2480 -0.1372 0.0461  0.0097  288 ARG A O   
2446 C CB  . ARG A 288 ? 0.3183 0.3631 0.2134 -0.1473 0.0498  0.0192  288 ARG A CB  
2447 C CG  . ARG A 288 ? 0.3136 0.3700 0.2110 -0.1521 0.0525  0.0244  288 ARG A CG  
2448 C CD  . ARG A 288 ? 0.4003 0.4680 0.2889 -0.1539 0.0598  0.0219  288 ARG A CD  
2449 N NE  . ARG A 288 ? 0.4305 0.5066 0.3228 -0.1485 0.0677  0.0133  288 ARG A NE  
2450 C CZ  . ARG A 288 ? 0.4346 0.5071 0.3196 -0.1450 0.0703  0.0062  288 ARG A CZ  
2451 N NH1 . ARG A 288 ? 0.4493 0.5288 0.3386 -0.1394 0.0774  -0.0017 288 ARG A NH1 
2452 N NH2 . ARG A 288 ? 0.4726 0.5342 0.3463 -0.1470 0.0654  0.0069  288 ARG A NH2 
2453 N N   . ALA A 289 ? 0.2536 0.2675 0.1600 -0.1373 0.0340  0.0187  289 ALA A N   
2454 C CA  . ALA A 289 ? 0.3030 0.3087 0.2118 -0.1318 0.0319  0.0147  289 ALA A CA  
2455 C C   . ALA A 289 ? 0.3536 0.3492 0.2524 -0.1319 0.0272  0.0156  289 ALA A C   
2456 O O   . ALA A 289 ? 0.3508 0.3369 0.2518 -0.1290 0.0208  0.0178  289 ALA A O   
2457 C CB  . ALA A 289 ? 0.2870 0.2880 0.2068 -0.1283 0.0272  0.0164  289 ALA A CB  
2458 N N   . SER A 290 ? 0.3065 0.3048 0.1947 -0.1350 0.0304  0.0136  290 SER A N   
2459 C CA  . SER A 290 ? 0.3401 0.3296 0.2190 -0.1357 0.0256  0.0145  290 SER A CA  
2460 C C   . SER A 290 ? 0.3096 0.2938 0.1899 -0.1312 0.0262  0.0090  290 SER A C   
2461 O O   . SER A 290 ? 0.2747 0.2635 0.1547 -0.1303 0.0329  0.0027  290 SER A O   
2462 C CB  . SER A 290 ? 0.2819 0.2755 0.1481 -0.1410 0.0279  0.0145  290 SER A CB  
2463 O OG  . SER A 290 ? 0.2758 0.2610 0.1338 -0.1417 0.0227  0.0153  290 SER A OG  
2464 N N   . PRO A 291 ? 0.2594 0.2342 0.1413 -0.1281 0.0195  0.0111  291 PRO A N   
2465 C CA  . PRO A 291 ? 0.2684 0.2384 0.1520 -0.1241 0.0197  0.0066  291 PRO A CA  
2466 C C   . PRO A 291 ? 0.2959 0.2631 0.1677 -0.1275 0.0200  0.0043  291 PRO A C   
2467 O O   . PRO A 291 ? 0.3118 0.2743 0.1848 -0.1249 0.0195  0.0012  291 PRO A O   
2468 C CB  . PRO A 291 ? 0.2637 0.2265 0.1544 -0.1191 0.0123  0.0106  291 PRO A CB  
2469 C CG  . PRO A 291 ? 0.3121 0.2729 0.1980 -0.1226 0.0071  0.0171  291 PRO A CG  
2470 C CD  . PRO A 291 ? 0.2891 0.2578 0.1722 -0.1278 0.0117  0.0179  291 PRO A CD  
2471 N N   . TYR A 292 ? 0.2650 0.2353 0.1259 -0.1332 0.0206  0.0058  292 TYR A N   
2472 C CA  . TYR A 292 ? 0.2869 0.2539 0.1356 -0.1369 0.0194  0.0043  292 TYR A CA  
2473 C C   . TYR A 292 ? 0.2845 0.2559 0.1259 -0.1381 0.0276  -0.0037 292 TYR A C   
2474 O O   . TYR A 292 ? 0.2928 0.2623 0.1228 -0.1409 0.0271  -0.0061 292 TYR A O   
2475 C CB  . TYR A 292 ? 0.3034 0.2707 0.1439 -0.1417 0.0142  0.0105  292 TYR A CB  
2476 C CG  . TYR A 292 ? 0.3044 0.2662 0.1519 -0.1391 0.0061  0.0176  292 TYR A CG  
2477 C CD1 . TYR A 292 ? 0.3457 0.3012 0.2005 -0.1337 0.0022  0.0175  292 TYR A CD1 
2478 C CD2 . TYR A 292 ? 0.4024 0.3657 0.2504 -0.1413 0.0031  0.0239  292 TYR A CD2 
2479 C CE1 . TYR A 292 ? 0.3857 0.3367 0.2474 -0.1301 -0.0044 0.0231  292 TYR A CE1 
2480 C CE2 . TYR A 292 ? 0.3976 0.3551 0.2522 -0.1382 -0.0037 0.0296  292 TYR A CE2 
2481 C CZ  . TYR A 292 ? 0.4151 0.3666 0.2764 -0.1324 -0.0072 0.0288  292 TYR A CZ  
2482 O OH  . TYR A 292 ? 0.4000 0.3459 0.2679 -0.1287 -0.0134 0.0337  292 TYR A OH  
2483 N N   . LEU A 293 ? 0.2699 0.2472 0.1184 -0.1350 0.0348  -0.0082 293 LEU A N   
2484 C CA  . LEU A 293 ? 0.2989 0.2813 0.1428 -0.1336 0.0431  -0.0169 293 LEU A CA  
2485 C C   . LEU A 293 ? 0.2826 0.2607 0.1365 -0.1262 0.0445  -0.0231 293 LEU A C   
2486 O O   . LEU A 293 ? 0.3301 0.3055 0.1961 -0.1226 0.0414  -0.0202 293 LEU A O   
2487 C CB  . LEU A 293 ? 0.3474 0.3418 0.1962 -0.1332 0.0494  -0.0175 293 LEU A CB  
2488 C CG  . LEU A 293 ? 0.4569 0.4588 0.2985 -0.1379 0.0497  -0.0141 293 LEU A CG  
2489 C CD1 . LEU A 293 ? 0.4294 0.4277 0.2716 -0.1417 0.0417  -0.0045 293 LEU A CD1 
2490 C CD2 . LEU A 293 ? 0.5284 0.5431 0.3764 -0.1363 0.0572  -0.0160 293 LEU A CD2 
2491 N N   . ARG A 294 ? 0.3060 0.2834 0.1556 -0.1232 0.0486  -0.0318 294 ARG A N   
2492 C CA  . ARG A 294 ? 0.3229 0.2976 0.1835 -0.1153 0.0509  -0.0382 294 ARG A CA  
2493 C C   . ARG A 294 ? 0.3062 0.2916 0.1746 -0.1120 0.0588  -0.0409 294 ARG A C   
2494 O O   . ARG A 294 ? 0.3296 0.3229 0.1906 -0.1139 0.0652  -0.0444 294 ARG A O   
2495 C CB  . ARG A 294 ? 0.2875 0.2554 0.1405 -0.1134 0.0515  -0.0465 294 ARG A CB  
2496 C CG  . ARG A 294 ? 0.2891 0.2521 0.1534 -0.1054 0.0529  -0.0522 294 ARG A CG  
2497 C CD  . ARG A 294 ? 0.3090 0.2620 0.1662 -0.1047 0.0513  -0.0593 294 ARG A CD  
2498 N NE  . ARG A 294 ? 0.3973 0.3529 0.2410 -0.1067 0.0564  -0.0665 294 ARG A NE  
2499 C CZ  . ARG A 294 ? 0.4355 0.3867 0.2657 -0.1115 0.0533  -0.0684 294 ARG A CZ  
2500 N NH1 . ARG A 294 ? 0.3909 0.3348 0.2192 -0.1151 0.0450  -0.0637 294 ARG A NH1 
2501 N NH2 . ARG A 294 ? 0.4866 0.4423 0.3093 -0.1111 0.0576  -0.0734 294 ARG A NH2 
2502 N N   . TYR A 295 ? 0.3011 0.2879 0.1843 -0.1071 0.0585  -0.0393 295 TYR A N   
2503 C CA  . TYR A 295 ? 0.3090 0.3068 0.2012 -0.1038 0.0652  -0.0414 295 TYR A CA  
2504 C C   . TYR A 295 ? 0.3047 0.3006 0.2039 -0.0954 0.0689  -0.0494 295 TYR A C   
2505 O O   . TYR A 295 ? 0.2929 0.2786 0.1950 -0.0917 0.0648  -0.0510 295 TYR A O   
2506 C CB  . TYR A 295 ? 0.2310 0.2328 0.1349 -0.1042 0.0626  -0.0346 295 TYR A CB  
2507 C CG  . TYR A 295 ? 0.2422 0.2471 0.1404 -0.1125 0.0602  -0.0268 295 TYR A CG  
2508 C CD1 . TYR A 295 ? 0.2610 0.2568 0.1525 -0.1168 0.0529  -0.0213 295 TYR A CD1 
2509 C CD2 . TYR A 295 ? 0.2760 0.2933 0.1752 -0.1163 0.0654  -0.0248 295 TYR A CD2 
2510 C CE1 . TYR A 295 ? 0.2771 0.2744 0.1644 -0.1230 0.0495  -0.0141 295 TYR A CE1 
2511 C CE2 . TYR A 295 ? 0.3171 0.3355 0.2135 -0.1215 0.0606  -0.0176 295 TYR A CE2 
2512 C CZ  . TYR A 295 ? 0.3187 0.3268 0.2089 -0.1245 0.0527  -0.0124 295 TYR A CZ  
2513 O OH  . TYR A 295 ? 0.3419 0.3507 0.2296 -0.1288 0.0480  -0.0054 295 TYR A OH  
2514 N N   . TYR A 296 ? 0.3135 0.3197 0.2157 -0.0924 0.0767  -0.0542 296 TYR A N   
2515 C CA  . TYR A 296 ? 0.2926 0.2982 0.2033 -0.0837 0.0807  -0.0614 296 TYR A CA  
2516 C C   . TYR A 296 ? 0.2570 0.2743 0.1828 -0.0801 0.0836  -0.0590 296 TYR A C   
2517 O O   . TYR A 296 ? 0.2893 0.3201 0.2159 -0.0823 0.0891  -0.0584 296 TYR A O   
2518 C CB  . TYR A 296 ? 0.2958 0.3033 0.1972 -0.0818 0.0875  -0.0705 296 TYR A CB  
2519 C CG  . TYR A 296 ? 0.3509 0.3480 0.2358 -0.0863 0.0847  -0.0734 296 TYR A CG  
2520 C CD1 . TYR A 296 ? 0.4182 0.4005 0.3021 -0.0851 0.0783  -0.0745 296 TYR A CD1 
2521 C CD2 . TYR A 296 ? 0.4415 0.4445 0.3119 -0.0919 0.0883  -0.0750 296 TYR A CD2 
2522 C CE1 . TYR A 296 ? 0.4393 0.4128 0.3087 -0.0895 0.0751  -0.0771 296 TYR A CE1 
2523 C CE2 . TYR A 296 ? 0.4996 0.4936 0.3558 -0.0957 0.0844  -0.0772 296 TYR A CE2 
2524 C CZ  . TYR A 296 ? 0.4291 0.4083 0.2838 -0.0950 0.0783  -0.0789 296 TYR A CZ  
2525 O OH  . TYR A 296 ? 0.4398 0.4110 0.2820 -0.0989 0.0738  -0.0805 296 TYR A OH  
2526 N N   . PHE A 297 ? 0.2759 0.2889 0.2135 -0.0749 0.0798  -0.0572 297 PHE A N   
2527 C CA  . PHE A 297 ? 0.2222 0.2461 0.1745 -0.0712 0.0817  -0.0552 297 PHE A CA  
2528 C C   . PHE A 297 ? 0.2333 0.2635 0.1917 -0.0635 0.0889  -0.0625 297 PHE A C   
2529 O O   . PHE A 297 ? 0.2479 0.2695 0.2098 -0.0567 0.0883  -0.0667 297 PHE A O   
2530 C CB  . PHE A 297 ? 0.2181 0.2357 0.1798 -0.0683 0.0750  -0.0508 297 PHE A CB  
2531 C CG  . PHE A 297 ? 0.2215 0.2501 0.1979 -0.0645 0.0761  -0.0487 297 PHE A CG  
2532 C CD1 . PHE A 297 ? 0.2341 0.2723 0.2139 -0.0699 0.0752  -0.0433 297 PHE A CD1 
2533 C CD2 . PHE A 297 ? 0.2563 0.2852 0.2431 -0.0559 0.0773  -0.0518 297 PHE A CD2 
2534 C CE1 . PHE A 297 ? 0.2566 0.3051 0.2499 -0.0670 0.0755  -0.0415 297 PHE A CE1 
2535 C CE2 . PHE A 297 ? 0.2193 0.2590 0.2196 -0.0525 0.0777  -0.0496 297 PHE A CE2 
2536 C CZ  . PHE A 297 ? 0.2251 0.2750 0.2286 -0.0582 0.0767  -0.0447 297 PHE A CZ  
2537 N N   . ARG A 298 ? 0.2425 0.2877 0.2022 -0.0645 0.0957  -0.0637 298 ARG A N   
2538 C CA  . ARG A 298 ? 0.3521 0.4065 0.3191 -0.0568 0.1033  -0.0704 298 ARG A CA  
2539 C C   . ARG A 298 ? 0.2881 0.3317 0.2466 -0.0519 0.1060  -0.0795 298 ARG A C   
2540 O O   . ARG A 298 ? 0.3409 0.3848 0.3072 -0.0431 0.1096  -0.0853 298 ARG A O   
2541 C CB  . ARG A 298 ? 0.3060 0.3646 0.2905 -0.0496 0.1020  -0.0688 298 ARG A CB  
2542 C CG  . ARG A 298 ? 0.2767 0.3476 0.2705 -0.0539 0.0999  -0.0613 298 ARG A CG  
2543 C CD  . ARG A 298 ? 0.2873 0.3623 0.2974 -0.0468 0.0979  -0.0599 298 ARG A CD  
2544 N NE  . ARG A 298 ? 0.3513 0.4365 0.3692 -0.0518 0.0948  -0.0529 298 ARG A NE  
2545 C CZ  . ARG A 298 ? 0.4627 0.5515 0.4934 -0.0481 0.0910  -0.0498 298 ARG A CZ  
2546 N NH1 . ARG A 298 ? 0.4915 0.5748 0.5288 -0.0392 0.0900  -0.0524 298 ARG A NH1 
2547 N NH2 . ARG A 298 ? 0.4494 0.5468 0.4857 -0.0537 0.0878  -0.0440 298 ARG A NH2 
2548 N N   . GLU A 299 ? 0.3358 0.3693 0.2785 -0.0576 0.1038  -0.0807 299 GLU A N   
2549 C CA  . GLU A 299 ? 0.3618 0.3826 0.2948 -0.0543 0.1047  -0.0893 299 GLU A CA  
2550 C C   . GLU A 299 ? 0.3960 0.4026 0.3369 -0.0476 0.1001  -0.0909 299 GLU A C   
2551 O O   . GLU A 299 ? 0.3759 0.3726 0.3132 -0.0427 0.1017  -0.0988 299 GLU A O   
2552 C CB  . GLU A 299 ? 0.4249 0.4548 0.3551 -0.0496 0.1143  -0.0983 299 GLU A CB  
2553 C CG  . GLU A 299 ? 0.5085 0.5531 0.4324 -0.0549 0.1174  -0.0950 299 GLU A CG  
2554 C CD  . GLU A 299 ? 0.6911 0.7290 0.5974 -0.0637 0.1135  -0.0931 299 GLU A CD  
2555 O OE1 . GLU A 299 ? 0.7189 0.7410 0.6172 -0.0656 0.1085  -0.0949 299 GLU A OE1 
2556 O OE2 . GLU A 299 ? 0.7375 0.7865 0.6383 -0.0685 0.1155  -0.0896 299 GLU A OE2 
2557 N N   . LEU A 300 ? 0.3412 0.3462 0.2926 -0.0472 0.0943  -0.0836 300 LEU A N   
2558 C CA  . LEU A 300 ? 0.3211 0.3143 0.2806 -0.0412 0.0900  -0.0836 300 LEU A CA  
2559 C C   . LEU A 300 ? 0.3245 0.3035 0.2773 -0.0461 0.0821  -0.0798 300 LEU A C   
2560 O O   . LEU A 300 ? 0.3361 0.3017 0.2873 -0.0435 0.0796  -0.0831 300 LEU A O   
2561 C CB  . LEU A 300 ? 0.3107 0.3125 0.2866 -0.0368 0.0888  -0.0780 300 LEU A CB  
2562 C CG  . LEU A 300 ? 0.3429 0.3598 0.3293 -0.0307 0.0958  -0.0810 300 LEU A CG  
2563 C CD1 . LEU A 300 ? 0.2639 0.2888 0.2656 -0.0274 0.0932  -0.0748 300 LEU A CD1 
2564 C CD2 . LEU A 300 ? 0.3197 0.3307 0.3068 -0.0224 0.1004  -0.0899 300 LEU A CD2 
2565 N N   . ILE A 301 ? 0.2836 0.2655 0.2332 -0.0531 0.0779  -0.0726 301 ILE A N   
2566 C CA  . ILE A 301 ? 0.2941 0.2653 0.2404 -0.0569 0.0702  -0.0677 301 ILE A CA  
2567 C C   . ILE A 301 ? 0.3253 0.2991 0.2610 -0.0657 0.0680  -0.0636 301 ILE A C   
2568 O O   . ILE A 301 ? 0.3343 0.3193 0.2703 -0.0687 0.0707  -0.0610 301 ILE A O   
2569 C CB  . ILE A 301 ? 0.2596 0.2311 0.2188 -0.0532 0.0660  -0.0617 301 ILE A CB  
2570 C CG1 . ILE A 301 ? 0.2389 0.2004 0.1957 -0.0563 0.0586  -0.0568 301 ILE A CG1 
2571 C CG2 . ILE A 301 ? 0.3392 0.3242 0.3053 -0.0544 0.0670  -0.0568 301 ILE A CG2 
2572 C CD1 . ILE A 301 ? 0.2187 0.1804 0.1873 -0.0518 0.0551  -0.0517 301 ILE A CD1 
2573 N N   . SER A 302 ? 0.3428 0.3064 0.2690 -0.0701 0.0632  -0.0629 302 SER A N   
2574 C CA  . SER A 302 ? 0.2666 0.2315 0.1826 -0.0782 0.0602  -0.0584 302 SER A CA  
2575 C C   . SER A 302 ? 0.2692 0.2348 0.1917 -0.0797 0.0544  -0.0499 302 SER A C   
2576 O O   . SER A 302 ? 0.2845 0.2452 0.2151 -0.0760 0.0508  -0.0478 302 SER A O   
2577 C CB  . SER A 302 ? 0.3120 0.2667 0.2158 -0.0821 0.0567  -0.0611 302 SER A CB  
2578 O OG  . SER A 302 ? 0.3639 0.3179 0.2597 -0.0811 0.0621  -0.0697 302 SER A OG  
2579 N N   . VAL A 303 ? 0.3161 0.2878 0.2349 -0.0852 0.0537  -0.0450 303 VAL A N   
2580 C CA  . VAL A 303 ? 0.2934 0.2653 0.2175 -0.0868 0.0484  -0.0375 303 VAL A CA  
2581 C C   . VAL A 303 ? 0.2938 0.2637 0.2073 -0.0942 0.0445  -0.0329 303 VAL A C   
2582 O O   . VAL A 303 ? 0.2978 0.2730 0.2034 -0.0990 0.0476  -0.0329 303 VAL A O   
2583 C CB  . VAL A 303 ? 0.2819 0.2639 0.2158 -0.0853 0.0510  -0.0354 303 VAL A CB  
2584 C CG1 . VAL A 303 ? 0.2576 0.2379 0.1962 -0.0867 0.0449  -0.0286 303 VAL A CG1 
2585 C CG2 . VAL A 303 ? 0.2623 0.2474 0.2068 -0.0777 0.0549  -0.0397 303 VAL A CG2 
2586 N N   . PHE A 304 ? 0.2568 0.2197 0.1701 -0.0950 0.0379  -0.0285 304 PHE A N   
2587 C CA  . PHE A 304 ? 0.2715 0.2328 0.1775 -0.1012 0.0333  -0.0226 304 PHE A CA  
2588 C C   . PHE A 304 ? 0.2636 0.2260 0.1777 -0.1005 0.0298  -0.0168 304 PHE A C   
2589 O O   . PHE A 304 ? 0.2646 0.2262 0.1885 -0.0952 0.0285  -0.0168 304 PHE A O   
2590 C CB  . PHE A 304 ? 0.2466 0.1999 0.1465 -0.1027 0.0278  -0.0216 304 PHE A CB  
2591 C CG  . PHE A 304 ? 0.2656 0.2171 0.1540 -0.1058 0.0298  -0.0266 304 PHE A CG  
2592 C CD1 . PHE A 304 ? 0.2844 0.2383 0.1606 -0.1122 0.0301  -0.0251 304 PHE A CD1 
2593 C CD2 . PHE A 304 ? 0.2956 0.2424 0.1848 -0.1024 0.0310  -0.0328 304 PHE A CD2 
2594 C CE1 . PHE A 304 ? 0.3285 0.2810 0.1929 -0.1151 0.0317  -0.0302 304 PHE A CE1 
2595 C CE2 . PHE A 304 ? 0.2887 0.2328 0.1665 -0.1053 0.0325  -0.0382 304 PHE A CE2 
2596 C CZ  . PHE A 304 ? 0.3082 0.2555 0.1733 -0.1115 0.0329  -0.0372 304 PHE A CZ  
2597 N N   . PHE A 305 ? 0.2191 0.1832 0.1286 -0.1060 0.0282  -0.0119 305 PHE A N   
2598 C CA  . PHE A 305 ? 0.2633 0.2272 0.1796 -0.1036 0.0234  -0.0068 305 PHE A CA  
2599 C C   . PHE A 305 ? 0.2364 0.1943 0.1485 -0.1030 0.0161  -0.0020 305 PHE A C   
2600 O O   . PHE A 305 ? 0.2270 0.1839 0.1293 -0.1080 0.0147  0.0001  305 PHE A O   
2601 C CB  . PHE A 305 ? 0.2353 0.2061 0.1523 -0.1068 0.0257  -0.0047 305 PHE A CB  
2602 C CG  . PHE A 305 ? 0.2005 0.1795 0.1246 -0.1061 0.0327  -0.0088 305 PHE A CG  
2603 C CD1 . PHE A 305 ? 0.2523 0.2373 0.1724 -0.1076 0.0401  -0.0137 305 PHE A CD1 
2604 C CD2 . PHE A 305 ? 0.2439 0.2250 0.1792 -0.1020 0.0315  -0.0084 305 PHE A CD2 
2605 C CE1 . PHE A 305 ? 0.2961 0.2899 0.2250 -0.1037 0.0457  -0.0177 305 PHE A CE1 
2606 C CE2 . PHE A 305 ? 0.3528 0.3425 0.2959 -0.1008 0.0373  -0.0118 305 PHE A CE2 
2607 C CZ  . PHE A 305 ? 0.2697 0.2660 0.2105 -0.1004 0.0440  -0.0163 305 PHE A CZ  
2608 N N   . ARG A 306 ? 0.1907 0.1452 0.1100 -0.0971 0.0116  -0.0003 306 ARG A N   
2609 C CA  . ARG A 306 ? 0.2458 0.1957 0.1625 -0.0962 0.0053  0.0038  306 ARG A CA  
2610 C C   . ARG A 306 ? 0.2514 0.2004 0.1647 -0.0991 0.0019  0.0089  306 ARG A C   
2611 O O   . ARG A 306 ? 0.2581 0.2096 0.1747 -0.0998 0.0031  0.0097  306 ARG A O   
2612 C CB  . ARG A 306 ? 0.2822 0.2302 0.2080 -0.0894 0.0023  0.0042  306 ARG A CB  
2613 C CG  . ARG A 306 ? 0.3601 0.3086 0.2942 -0.0856 0.0011  0.0052  306 ARG A CG  
2614 C CD  . ARG A 306 ? 0.4089 0.3536 0.3467 -0.0816 -0.0042 0.0082  306 ARG A CD  
2615 N NE  . ARG A 306 ? 0.3518 0.2959 0.2963 -0.0786 -0.0054 0.0082  306 ARG A NE  
2616 C CZ  . ARG A 306 ? 0.4216 0.3635 0.3712 -0.0743 -0.0082 0.0085  306 ARG A CZ  
2617 N NH1 . ARG A 306 ? 0.3992 0.3398 0.3491 -0.0722 -0.0102 0.0095  306 ARG A NH1 
2618 N NH2 . ARG A 306 ? 0.5913 0.5320 0.5451 -0.0727 -0.0093 0.0080  306 ARG A NH2 
2619 N N   . ASP A 307 ? 0.2854 0.2310 0.1921 -0.1014 -0.0026 0.0125  307 ASP A N   
2620 C CA  . ASP A 307 ? 0.2553 0.1984 0.1600 -0.1033 -0.0072 0.0181  307 ASP A CA  
2621 C C   . ASP A 307 ? 0.2420 0.1816 0.1559 -0.0973 -0.0111 0.0198  307 ASP A C   
2622 O O   . ASP A 307 ? 0.2493 0.1860 0.1653 -0.0940 -0.0146 0.0207  307 ASP A O   
2623 C CB  . ASP A 307 ? 0.2660 0.2068 0.1611 -0.1076 -0.0112 0.0216  307 ASP A CB  
2624 C CG  . ASP A 307 ? 0.3205 0.2584 0.2134 -0.1100 -0.0161 0.0278  307 ASP A CG  
2625 O OD1 . ASP A 307 ? 0.3322 0.2670 0.2322 -0.1064 -0.0187 0.0299  307 ASP A OD1 
2626 O OD2 . ASP A 307 ? 0.3665 0.3050 0.2500 -0.1158 -0.0174 0.0306  307 ASP A OD2 
2627 N N   . LYS A 308 ? 0.2465 0.1864 0.1658 -0.0963 -0.0104 0.0199  308 LYS A N   
2628 C CA  . LYS A 308 ? 0.2250 0.1614 0.1526 -0.0911 -0.0134 0.0201  308 LYS A CA  
2629 C C   . LYS A 308 ? 0.2388 0.1684 0.1650 -0.0906 -0.0198 0.0249  308 LYS A C   
2630 O O   . LYS A 308 ? 0.2267 0.1528 0.1574 -0.0860 -0.0228 0.0249  308 LYS A O   
2631 C CB  . LYS A 308 ? 0.2232 0.1613 0.1561 -0.0912 -0.0115 0.0190  308 LYS A CB  
2632 C CG  . LYS A 308 ? 0.2316 0.1651 0.1715 -0.0868 -0.0149 0.0187  308 LYS A CG  
2633 C CD  . LYS A 308 ? 0.3129 0.2468 0.2564 -0.0888 -0.0147 0.0189  308 LYS A CD  
2634 C CE  . LYS A 308 ? 0.3918 0.3233 0.3424 -0.0845 -0.0164 0.0162  308 LYS A CE  
2635 N NZ  . LYS A 308 ? 0.3977 0.3223 0.3491 -0.0800 -0.0208 0.0165  308 LYS A NZ  
2636 N N   . THR A 309 ? 0.2236 0.1514 0.1437 -0.0953 -0.0221 0.0292  309 THR A N   
2637 C CA  . THR A 309 ? 0.2477 0.1686 0.1666 -0.0951 -0.0286 0.0342  309 THR A CA  
2638 C C   . THR A 309 ? 0.2787 0.1985 0.1966 -0.0929 -0.0315 0.0351  309 THR A C   
2639 O O   . THR A 309 ? 0.2717 0.1866 0.1941 -0.0889 -0.0358 0.0367  309 THR A O   
2640 C CB  . THR A 309 ? 0.3644 0.2846 0.2761 -0.1013 -0.0303 0.0389  309 THR A CB  
2641 O OG1 . THR A 309 ? 0.3295 0.2511 0.2434 -0.1035 -0.0278 0.0386  309 THR A OG1 
2642 C CG2 . THR A 309 ? 0.3602 0.2728 0.2710 -0.1010 -0.0375 0.0447  309 THR A CG2 
2643 N N   . LEU A 310 ? 0.2489 0.1731 0.1609 -0.0959 -0.0296 0.0343  310 LEU A N   
2644 C CA  . LEU A 310 ? 0.2488 0.1726 0.1599 -0.0948 -0.0327 0.0355  310 LEU A CA  
2645 C C   . LEU A 310 ? 0.2052 0.1301 0.1247 -0.0889 -0.0315 0.0321  310 LEU A C   
2646 O O   . LEU A 310 ? 0.2402 0.1631 0.1630 -0.0862 -0.0356 0.0344  310 LEU A O   
2647 C CB  . LEU A 310 ? 0.2495 0.1775 0.1520 -0.1000 -0.0308 0.0344  310 LEU A CB  
2648 C CG  . LEU A 310 ? 0.3457 0.2735 0.2384 -0.1067 -0.0324 0.0381  310 LEU A CG  
2649 C CD1 . LEU A 310 ? 0.3105 0.2418 0.1936 -0.1121 -0.0304 0.0362  310 LEU A CD1 
2650 C CD2 . LEU A 310 ? 0.3214 0.2443 0.2139 -0.1069 -0.0398 0.0449  310 LEU A CD2 
2651 N N   . SER A 311 ? 0.1976 0.1260 0.1206 -0.0871 -0.0259 0.0270  311 SER A N   
2652 C CA  . SER A 311 ? 0.2353 0.1651 0.1658 -0.0819 -0.0246 0.0241  311 SER A CA  
2653 C C   . SER A 311 ? 0.2561 0.1812 0.1926 -0.0777 -0.0282 0.0255  311 SER A C   
2654 O O   . SER A 311 ? 0.2320 0.1562 0.1729 -0.0744 -0.0304 0.0261  311 SER A O   
2655 C CB  . SER A 311 ? 0.2088 0.1431 0.1418 -0.0811 -0.0184 0.0189  311 SER A CB  
2656 O OG  . SER A 311 ? 0.2400 0.1772 0.1667 -0.0851 -0.0152 0.0171  311 SER A OG  
2657 N N   . ASP A 312 ? 0.2359 0.1574 0.1725 -0.0783 -0.0289 0.0261  312 ASP A N   
2658 C CA  . ASP A 312 ? 0.2277 0.1427 0.1689 -0.0747 -0.0328 0.0270  312 ASP A CA  
2659 C C   . ASP A 312 ? 0.2683 0.1769 0.2083 -0.0740 -0.0392 0.0320  312 ASP A C   
2660 O O   . ASP A 312 ? 0.2542 0.1573 0.1986 -0.0697 -0.0427 0.0324  312 ASP A O   
2661 C CB  . ASP A 312 ? 0.2594 0.1718 0.2010 -0.0761 -0.0323 0.0263  312 ASP A CB  
2662 C CG  . ASP A 312 ? 0.3252 0.2426 0.2708 -0.0751 -0.0274 0.0213  312 ASP A CG  
2663 O OD1 . ASP A 312 ? 0.3240 0.2452 0.2726 -0.0722 -0.0250 0.0183  312 ASP A OD1 
2664 O OD2 . ASP A 312 ? 0.3138 0.2314 0.2600 -0.0773 -0.0263 0.0208  312 ASP A OD2 
2665 N N   . LEU A 313 ? 0.2445 0.1534 0.1788 -0.0781 -0.0413 0.0362  313 LEU A N   
2666 C CA  . LEU A 313 ? 0.2347 0.1381 0.1687 -0.0772 -0.0479 0.0416  313 LEU A CA  
2667 C C   . LEU A 313 ? 0.2150 0.1205 0.1534 -0.0738 -0.0494 0.0420  313 LEU A C   
2668 O O   . LEU A 313 ? 0.2299 0.1310 0.1731 -0.0686 -0.0538 0.0442  313 LEU A O   
2669 C CB  . LEU A 313 ? 0.2416 0.1463 0.1681 -0.0828 -0.0500 0.0461  313 LEU A CB  
2670 C CG  . LEU A 313 ? 0.3358 0.2367 0.2587 -0.0862 -0.0508 0.0482  313 LEU A CG  
2671 C CD1 . LEU A 313 ? 0.3663 0.2711 0.2805 -0.0927 -0.0507 0.0510  313 LEU A CD1 
2672 C CD2 . LEU A 313 ? 0.3813 0.2725 0.3073 -0.0833 -0.0573 0.0524  313 LEU A CD2 
2673 N N   . ILE A 314 ? 0.2425 0.1558 0.1803 -0.0754 -0.0454 0.0395  314 ILE A N   
2674 C CA  . ILE A 314 ? 0.2257 0.1438 0.1691 -0.0715 -0.0460 0.0395  314 ILE A CA  
2675 C C   . ILE A 314 ? 0.2427 0.1628 0.1939 -0.0638 -0.0436 0.0351  314 ILE A C   
2676 O O   . ILE A 314 ? 0.2179 0.1402 0.1752 -0.0568 -0.0458 0.0358  314 ILE A O   
2677 C CB  . ILE A 314 ? 0.1987 0.1234 0.1392 -0.0760 -0.0428 0.0378  314 ILE A CB  
2678 C CG1 . ILE A 314 ? 0.2288 0.1539 0.1613 -0.0817 -0.0456 0.0413  314 ILE A CG1 
2679 C CG2 . ILE A 314 ? 0.1815 0.1140 0.1298 -0.0708 -0.0421 0.0366  314 ILE A CG2 
2680 C CD1 . ILE A 314 ? 0.2378 0.1688 0.1661 -0.0855 -0.0424 0.0382  314 ILE A CD1 
2681 N N   . GLY A 315 ? 0.2289 0.1488 0.1796 -0.0649 -0.0390 0.0307  315 GLY A N   
2682 C CA  . GLY A 315 ? 0.2245 0.1472 0.1815 -0.0582 -0.0365 0.0265  315 GLY A CA  
2683 C C   . GLY A 315 ? 0.2474 0.1645 0.2074 -0.0522 -0.0400 0.0261  315 GLY A C   
2684 O O   . GLY A 315 ? 0.2770 0.1979 0.2424 -0.0449 -0.0393 0.0236  315 GLY A O   
2685 N N   . PHE A 316 ? 0.2257 0.1335 0.1820 -0.0552 -0.0438 0.0286  316 PHE A N   
2686 C CA  . PHE A 316 ? 0.2797 0.1797 0.2383 -0.0500 -0.0472 0.0273  316 PHE A CA  
2687 C C   . PHE A 316 ? 0.3088 0.2001 0.2662 -0.0495 -0.0535 0.0323  316 PHE A C   
2688 O O   . PHE A 316 ? 0.3100 0.1960 0.2710 -0.0425 -0.0567 0.0311  316 PHE A O   
2689 C CB  . PHE A 316 ? 0.3189 0.2136 0.2755 -0.0538 -0.0457 0.0242  316 PHE A CB  
2690 C CG  . PHE A 316 ? 0.2832 0.1859 0.2420 -0.0531 -0.0401 0.0192  316 PHE A CG  
2691 C CD1 . PHE A 316 ? 0.3730 0.2797 0.3364 -0.0452 -0.0391 0.0149  316 PHE A CD1 
2692 C CD2 . PHE A 316 ? 0.2955 0.2022 0.2516 -0.0598 -0.0360 0.0188  316 PHE A CD2 
2693 C CE1 . PHE A 316 ? 0.2801 0.1942 0.2454 -0.0446 -0.0344 0.0111  316 PHE A CE1 
2694 C CE2 . PHE A 316 ? 0.3902 0.3040 0.3490 -0.0586 -0.0312 0.0146  316 PHE A CE2 
2695 C CZ  . PHE A 316 ? 0.3512 0.2685 0.3146 -0.0511 -0.0307 0.0111  316 PHE A CZ  
2696 N N   . SER A 317 ? 0.2466 0.1360 0.1990 -0.0563 -0.0555 0.0378  317 SER A N   
2697 C CA  . SER A 317 ? 0.2868 0.1666 0.2378 -0.0563 -0.0620 0.0433  317 SER A CA  
2698 C C   . SER A 317 ? 0.3054 0.1896 0.2597 -0.0513 -0.0656 0.0472  317 SER A C   
2699 O O   . SER A 317 ? 0.3036 0.1820 0.2618 -0.0447 -0.0702 0.0486  317 SER A O   
2700 C CB  . SER A 317 ? 0.3531 0.2311 0.2969 -0.0652 -0.0621 0.0470  317 SER A CB  
2701 O OG  . SER A 317 ? 0.5336 0.4048 0.4763 -0.0649 -0.0682 0.0526  317 SER A OG  
2702 N N   . TYR A 318 ? 0.2652 0.1593 0.2185 -0.0544 -0.0637 0.0488  318 TYR A N   
2703 C CA  . TYR A 318 ? 0.2225 0.1205 0.1777 -0.0525 -0.0682 0.0542  318 TYR A CA  
2704 C C   . TYR A 318 ? 0.2179 0.1222 0.1827 -0.0420 -0.0690 0.0527  318 TYR A C   
2705 O O   . TYR A 318 ? 0.2540 0.1615 0.2222 -0.0391 -0.0734 0.0575  318 TYR A O   
2706 C CB  . TYR A 318 ? 0.2183 0.1250 0.1693 -0.0595 -0.0665 0.0558  318 TYR A CB  
2707 C CG  . TYR A 318 ? 0.2264 0.1283 0.1671 -0.0695 -0.0671 0.0591  318 TYR A CG  
2708 C CD1 . TYR A 318 ? 0.2827 0.1750 0.2196 -0.0714 -0.0714 0.0634  318 TYR A CD1 
2709 C CD2 . TYR A 318 ? 0.2228 0.1305 0.1576 -0.0764 -0.0633 0.0575  318 TYR A CD2 
2710 C CE1 . TYR A 318 ? 0.3037 0.1977 0.2328 -0.0785 -0.0704 0.0643  318 TYR A CE1 
2711 C CE2 . TYR A 318 ? 0.2417 0.1498 0.1678 -0.0830 -0.0626 0.0581  318 TYR A CE2 
2712 C CZ  . TYR A 318 ? 0.2819 0.1840 0.2053 -0.0841 -0.0660 0.0616  318 TYR A CZ  
2713 O OH  . TYR A 318 ? 0.2722 0.1763 0.1872 -0.0906 -0.0650 0.0624  318 TYR A OH  
2714 N N   . HIS A 319 ? 0.2702 0.1774 0.2395 -0.0362 -0.0648 0.0466  319 HIS A N   
2715 C CA  . HIS A 319 ? 0.2935 0.2061 0.2713 -0.0256 -0.0656 0.0454  319 HIS A CA  
2716 C C   . HIS A 319 ? 0.3710 0.2733 0.3506 -0.0198 -0.0716 0.0477  319 HIS A C   
2717 O O   . HIS A 319 ? 0.3300 0.2373 0.3164 -0.0122 -0.0742 0.0496  319 HIS A O   
2718 C CB  . HIS A 319 ? 0.3011 0.2174 0.2818 -0.0205 -0.0603 0.0384  319 HIS A CB  
2719 C CG  . HIS A 319 ? 0.3059 0.2104 0.2847 -0.0176 -0.0613 0.0341  319 HIS A CG  
2720 N ND1 . HIS A 319 ? 0.3574 0.2547 0.3304 -0.0243 -0.0596 0.0318  319 HIS A ND1 
2721 C CD2 . HIS A 319 ? 0.3137 0.2123 0.2957 -0.0088 -0.0639 0.0316  319 HIS A CD2 
2722 C CE1 . HIS A 319 ? 0.3313 0.2187 0.3042 -0.0204 -0.0615 0.0282  319 HIS A CE1 
2723 N NE2 . HIS A 319 ? 0.3585 0.2457 0.3363 -0.0109 -0.0642 0.0276  319 HIS A NE2 
2724 N N   . ALA A 320 ? 0.3575 0.2457 0.3317 -0.0235 -0.0740 0.0478  320 ALA A N   
2725 C CA  . ALA A 320 ? 0.3333 0.2087 0.3086 -0.0188 -0.0802 0.0501  320 ALA A CA  
2726 C C   . ALA A 320 ? 0.4162 0.2882 0.3891 -0.0232 -0.0862 0.0590  320 ALA A C   
2727 O O   . ALA A 320 ? 0.4191 0.2782 0.3915 -0.0214 -0.0919 0.0623  320 ALA A O   
2728 C CB  . ALA A 320 ? 0.3088 0.1699 0.2798 -0.0214 -0.0806 0.0466  320 ALA A CB  
2729 N N   . TRP A 321 ? 0.3461 0.2289 0.3174 -0.0286 -0.0854 0.0629  321 TRP A N   
2730 C CA  . TRP A 321 ? 0.3794 0.2613 0.3475 -0.0334 -0.0910 0.0713  321 TRP A CA  
2731 C C   . TRP A 321 ? 0.3583 0.2539 0.3333 -0.0290 -0.0927 0.0743  321 TRP A C   
2732 O O   . TRP A 321 ? 0.3624 0.2703 0.3423 -0.0263 -0.0881 0.0704  321 TRP A O   
2733 C CB  . TRP A 321 ? 0.3014 0.1842 0.2594 -0.0459 -0.0889 0.0734  321 TRP A CB  
2734 C CG  . TRP A 321 ? 0.3425 0.2140 0.2932 -0.0526 -0.0878 0.0727  321 TRP A CG  
2735 C CD1 . TRP A 321 ? 0.2867 0.1534 0.2378 -0.0517 -0.0837 0.0663  321 TRP A CD1 
2736 C CD2 . TRP A 321 ? 0.4110 0.2819 0.3547 -0.0606 -0.0884 0.0756  321 TRP A CD2 
2737 N NE1 . TRP A 321 ? 0.3261 0.1889 0.2714 -0.0588 -0.0823 0.0659  321 TRP A NE1 
2738 C CE2 . TRP A 321 ? 0.3330 0.1988 0.2737 -0.0640 -0.0848 0.0715  321 TRP A CE2 
2739 C CE3 . TRP A 321 ? 0.4084 0.2834 0.3482 -0.0651 -0.0918 0.0813  321 TRP A CE3 
2740 C CZ2 . TRP A 321 ? 0.4074 0.2726 0.3418 -0.0713 -0.0844 0.0735  321 TRP A CZ2 
2741 C CZ3 . TRP A 321 ? 0.4372 0.3105 0.3699 -0.0725 -0.0915 0.0830  321 TRP A CZ3 
2742 C CH2 . TRP A 321 ? 0.3973 0.2659 0.3275 -0.0754 -0.0877 0.0793  321 TRP A CH2 
2743 N N   . ASN A 322 ? 0.3475 0.2415 0.3230 -0.0288 -0.0995 0.0820  322 ASN A N   
2744 C CA  . ASN A 322 ? 0.4014 0.3097 0.3820 -0.0277 -0.1017 0.0860  322 ASN A CA  
2745 C C   . ASN A 322 ? 0.4193 0.3351 0.3922 -0.0390 -0.0992 0.0866  322 ASN A C   
2746 O O   . ASN A 322 ? 0.3849 0.2933 0.3473 -0.0479 -0.0981 0.0869  322 ASN A O   
2747 C CB  . ASN A 322 ? 0.4944 0.3997 0.4781 -0.0243 -0.1097 0.0937  322 ASN A CB  
2748 C CG  . ASN A 322 ? 0.6947 0.6136 0.6794 -0.0286 -0.1123 0.0987  322 ASN A CG  
2749 O OD1 . ASN A 322 ? 0.7425 0.6613 0.7183 -0.0386 -0.1128 0.1010  322 ASN A OD1 
2750 N ND2 . ASN A 322 ? 0.7459 0.6774 0.7418 -0.0210 -0.1139 0.1001  322 ASN A ND2 
2751 N N   . ALA A 323 ? 0.3858 0.3164 0.3641 -0.0386 -0.0979 0.0863  323 ALA A N   
2752 C CA  . ALA A 323 ? 0.3386 0.2758 0.3105 -0.0482 -0.0944 0.0846  323 ALA A CA  
2753 C C   . ALA A 323 ? 0.3388 0.2721 0.2995 -0.0581 -0.0988 0.0900  323 ALA A C   
2754 O O   . ALA A 323 ? 0.3215 0.2517 0.2721 -0.0665 -0.0952 0.0875  323 ALA A O   
2755 C CB  . ALA A 323 ? 0.3213 0.2745 0.3020 -0.0461 -0.0934 0.0842  323 ALA A CB  
2756 N N   . GLU A 324 ? 0.3245 0.2594 0.2874 -0.0567 -0.1056 0.0967  324 GLU A N   
2757 C CA  . GLU A 324 ? 0.4023 0.3364 0.3563 -0.0654 -0.1079 0.0996  324 GLU A CA  
2758 C C   . GLU A 324 ? 0.3937 0.3155 0.3383 -0.0700 -0.1058 0.0982  324 GLU A C   
2759 O O   . GLU A 324 ? 0.3410 0.2629 0.2753 -0.0791 -0.1036 0.0969  324 GLU A O   
2760 C CB  . GLU A 324 ? 0.5272 0.4652 0.4873 -0.0617 -0.1144 0.1057  324 GLU A CB  
2761 C CG  . GLU A 324 ? 0.7212 0.6742 0.6887 -0.0609 -0.1170 0.1079  324 GLU A CG  
2762 C CD  . GLU A 324 ? 0.8938 0.8542 0.8755 -0.0500 -0.1169 0.1074  324 GLU A CD  
2763 O OE1 . GLU A 324 ? 0.8990 0.8524 0.8838 -0.0431 -0.1144 0.1045  324 GLU A OE1 
2764 O OE2 . GLU A 324 ? 0.9737 0.9475 0.9636 -0.0484 -0.1192 0.1098  324 GLU A OE2 
2765 N N   . ASP A 325 ? 0.3654 0.2773 0.3138 -0.0638 -0.1063 0.0981  325 ASP A N   
2766 C CA  . ASP A 325 ? 0.3397 0.2410 0.2808 -0.0682 -0.1046 0.0970  325 ASP A CA  
2767 C C   . ASP A 325 ? 0.3342 0.2350 0.2689 -0.0736 -0.0976 0.0909  325 ASP A C   
2768 O O   . ASP A 325 ? 0.3410 0.2398 0.2673 -0.0809 -0.0952 0.0900  325 ASP A O   
2769 C CB  . ASP A 325 ? 0.4302 0.3204 0.3775 -0.0602 -0.1068 0.0974  325 ASP A CB  
2770 C CG  . ASP A 325 ? 0.6293 0.5186 0.5819 -0.0552 -0.1135 0.1035  325 ASP A CG  
2771 O OD1 . ASP A 325 ? 0.7003 0.5954 0.6494 -0.0603 -0.1164 0.1081  325 ASP A OD1 
2772 O OD2 . ASP A 325 ? 0.6872 0.5697 0.6474 -0.0460 -0.1157 0.1034  325 ASP A OD2 
2773 N N   . ALA A 326 ? 0.3164 0.2197 0.2556 -0.0698 -0.0939 0.0867  326 ALA A N   
2774 C CA  . ALA A 326 ? 0.3340 0.2372 0.2684 -0.0742 -0.0868 0.0805  326 ALA A CA  
2775 C C   . ALA A 326 ? 0.3177 0.2282 0.2435 -0.0831 -0.0844 0.0794  326 ALA A C   
2776 O O   . ALA A 326 ? 0.2945 0.2039 0.2132 -0.0885 -0.0799 0.0758  326 ALA A O   
2777 C CB  . ALA A 326 ? 0.2790 0.1863 0.2218 -0.0675 -0.0830 0.0754  326 ALA A CB  
2778 N N   . VAL A 327 ? 0.3153 0.2338 0.2418 -0.0843 -0.0875 0.0822  327 VAL A N   
2779 C CA  . VAL A 327 ? 0.3163 0.2405 0.2338 -0.0928 -0.0860 0.0807  327 VAL A CA  
2780 C C   . VAL A 327 ? 0.3824 0.3043 0.2910 -0.0988 -0.0877 0.0830  327 VAL A C   
2781 O O   . VAL A 327 ? 0.3125 0.2352 0.2118 -0.1053 -0.0837 0.0795  327 VAL A O   
2782 C CB  . VAL A 327 ? 0.3339 0.2673 0.2548 -0.0929 -0.0899 0.0834  327 VAL A CB  
2783 C CG1 . VAL A 327 ? 0.3688 0.3065 0.2792 -0.1022 -0.0897 0.0820  327 VAL A CG1 
2784 C CG2 . VAL A 327 ? 0.2401 0.1787 0.1712 -0.0870 -0.0860 0.0788  327 VAL A CG2 
2785 N N   . ARG A 328 ? 0.3617 0.2809 0.2734 -0.0962 -0.0936 0.0890  328 ARG A N   
2786 C CA  . ARG A 328 ? 0.3889 0.3052 0.2930 -0.1015 -0.0955 0.0922  328 ARG A CA  
2787 C C   . ARG A 328 ? 0.3343 0.2453 0.2335 -0.1039 -0.0901 0.0884  328 ARG A C   
2788 O O   . ARG A 328 ? 0.3678 0.2806 0.2576 -0.1109 -0.0879 0.0877  328 ARG A O   
2789 C CB  . ARG A 328 ? 0.4013 0.3137 0.3119 -0.0965 -0.1022 0.0989  328 ARG A CB  
2790 C CG  . ARG A 328 ? 0.6416 0.5553 0.5459 -0.1019 -0.1066 0.1045  328 ARG A CG  
2791 C CD  . ARG A 328 ? 0.6471 0.5576 0.5586 -0.0963 -0.1135 0.1116  328 ARG A CD  
2792 N NE  . ARG A 328 ? 0.6140 0.5298 0.5357 -0.0892 -0.1170 0.1132  328 ARG A NE  
2793 C CZ  . ARG A 328 ? 0.6985 0.6101 0.6308 -0.0796 -0.1188 0.1140  328 ARG A CZ  
2794 N NH1 . ARG A 328 ? 0.6956 0.5961 0.6289 -0.0764 -0.1178 0.1131  328 ARG A NH1 
2795 N NH2 . ARG A 328 ? 0.7132 0.6319 0.6552 -0.0729 -0.1216 0.1155  328 ARG A NH2 
2796 N N   . ASP A 329 ? 0.2934 0.1987 0.1992 -0.0982 -0.0878 0.0858  329 ASP A N   
2797 C CA  . ASP A 329 ? 0.3549 0.2562 0.2577 -0.1000 -0.0827 0.0821  329 ASP A CA  
2798 C C   . ASP A 329 ? 0.3061 0.2135 0.2028 -0.1045 -0.0757 0.0759  329 ASP A C   
2799 O O   . ASP A 329 ? 0.3167 0.2252 0.2065 -0.1096 -0.0723 0.0746  329 ASP A O   
2800 C CB  . ASP A 329 ? 0.3600 0.2543 0.2716 -0.0927 -0.0820 0.0799  329 ASP A CB  
2801 C CG  . ASP A 329 ? 0.3884 0.2791 0.2982 -0.0945 -0.0776 0.0766  329 ASP A CG  
2802 O OD1 . ASP A 329 ? 0.4001 0.2858 0.3079 -0.0966 -0.0802 0.0804  329 ASP A OD1 
2803 O OD2 . ASP A 329 ? 0.3340 0.2275 0.2447 -0.0939 -0.0716 0.0706  329 ASP A OD2 
2804 N N   . PHE A 330 ? 0.2757 0.1872 0.1753 -0.1024 -0.0734 0.0721  330 PHE A N   
2805 C CA  . PHE A 330 ? 0.3012 0.2176 0.1961 -0.1056 -0.0667 0.0657  330 PHE A CA  
2806 C C   . PHE A 330 ? 0.3743 0.2952 0.2578 -0.1136 -0.0667 0.0662  330 PHE A C   
2807 O O   . PHE A 330 ? 0.2998 0.2224 0.1764 -0.1176 -0.0614 0.0623  330 PHE A O   
2808 C CB  . PHE A 330 ? 0.2585 0.1780 0.1598 -0.1018 -0.0652 0.0627  330 PHE A CB  
2809 C CG  . PHE A 330 ? 0.2741 0.1974 0.1735 -0.1030 -0.0578 0.0554  330 PHE A CG  
2810 C CD1 . PHE A 330 ? 0.3238 0.2459 0.2280 -0.0990 -0.0524 0.0506  330 PHE A CD1 
2811 C CD2 . PHE A 330 ? 0.3119 0.2396 0.2052 -0.1076 -0.0567 0.0532  330 PHE A CD2 
2812 C CE1 . PHE A 330 ? 0.3338 0.2597 0.2376 -0.0991 -0.0457 0.0441  330 PHE A CE1 
2813 C CE2 . PHE A 330 ? 0.3220 0.2523 0.2143 -0.1078 -0.0498 0.0461  330 PHE A CE2 
2814 C CZ  . PHE A 330 ? 0.3149 0.2445 0.2128 -0.1031 -0.0443 0.0418  330 PHE A CZ  
2815 N N   . ILE A 331 ? 0.3190 0.2420 0.2005 -0.1159 -0.0726 0.0707  331 ILE A N   
2816 C CA  . ILE A 331 ? 0.3626 0.2895 0.2329 -0.1238 -0.0733 0.0712  331 ILE A CA  
2817 C C   . ILE A 331 ? 0.3510 0.2761 0.2151 -0.1276 -0.0729 0.0737  331 ILE A C   
2818 O O   . ILE A 331 ? 0.3426 0.2705 0.1972 -0.1335 -0.0689 0.0709  331 ILE A O   
2819 C CB  . ILE A 331 ? 0.4488 0.3788 0.3200 -0.1250 -0.0804 0.0762  331 ILE A CB  
2820 C CG1 . ILE A 331 ? 0.4262 0.3593 0.3031 -0.1223 -0.0806 0.0740  331 ILE A CG1 
2821 C CG2 . ILE A 331 ? 0.4976 0.4310 0.3570 -0.1333 -0.0814 0.0771  331 ILE A CG2 
2822 C CD1 . ILE A 331 ? 0.4101 0.3450 0.2803 -0.1263 -0.0747 0.0669  331 ILE A CD1 
2823 N N   . GLY A 332 ? 0.3505 0.2708 0.2202 -0.1242 -0.0768 0.0789  332 GLY A N   
2824 C CA  . GLY A 332 ? 0.3516 0.2700 0.2165 -0.1279 -0.0766 0.0821  332 GLY A CA  
2825 C C   . GLY A 332 ? 0.3716 0.2909 0.2334 -0.1297 -0.0691 0.0768  332 GLY A C   
2826 O O   . GLY A 332 ? 0.3711 0.2928 0.2251 -0.1354 -0.0669 0.0776  332 GLY A O   
2827 N N   . ARG A 333 ? 0.3341 0.2521 0.2025 -0.1246 -0.0649 0.0716  333 ARG A N   
2828 C CA  . ARG A 333 ? 0.2994 0.2193 0.1664 -0.1257 -0.0576 0.0667  333 ARG A CA  
2829 C C   . ARG A 333 ? 0.3612 0.2874 0.2194 -0.1306 -0.0524 0.0616  333 ARG A C   
2830 O O   . ARG A 333 ? 0.3479 0.2773 0.2008 -0.1346 -0.0474 0.0597  333 ARG A O   
2831 C CB  . ARG A 333 ? 0.3111 0.2282 0.1882 -0.1186 -0.0549 0.0627  333 ARG A CB  
2832 C CG  . ARG A 333 ? 0.3130 0.2229 0.1975 -0.1146 -0.0588 0.0665  333 ARG A CG  
2833 C CD  . ARG A 333 ? 0.3328 0.2403 0.2268 -0.1076 -0.0568 0.0622  333 ARG A CD  
2834 N NE  . ARG A 333 ? 0.3314 0.2309 0.2319 -0.1038 -0.0603 0.0648  333 ARG A NE  
2835 C CZ  . ARG A 333 ? 0.3706 0.2677 0.2732 -0.1042 -0.0580 0.0636  333 ARG A CZ  
2836 N NH1 . ARG A 333 ? 0.3998 0.3028 0.2990 -0.1080 -0.0520 0.0605  333 ARG A NH1 
2837 N NH2 . ARG A 333 ? 0.3955 0.2841 0.3036 -0.1008 -0.0618 0.0656  333 ARG A NH2 
2838 N N   . LEU A 334 ? 0.2963 0.2242 0.1529 -0.1306 -0.0533 0.0594  334 LEU A N   
2839 C CA  . LEU A 334 ? 0.3172 0.2497 0.1642 -0.1360 -0.0490 0.0545  334 LEU A CA  
2840 C C   . LEU A 334 ? 0.3369 0.2722 0.1732 -0.1435 -0.0504 0.0576  334 LEU A C   
2841 O O   . LEU A 334 ? 0.3329 0.2721 0.1610 -0.1481 -0.0449 0.0536  334 LEU A O   
2842 C CB  . LEU A 334 ? 0.3269 0.2598 0.1743 -0.1353 -0.0508 0.0522  334 LEU A CB  
2843 C CG  . LEU A 334 ? 0.3226 0.2542 0.1803 -0.1281 -0.0482 0.0485  334 LEU A CG  
2844 C CD1 . LEU A 334 ? 0.3571 0.2896 0.2154 -0.1283 -0.0509 0.0476  334 LEU A CD1 
2845 C CD2 . LEU A 334 ? 0.3006 0.2336 0.1585 -0.1272 -0.0397 0.0416  334 LEU A CD2 
2846 N N   . LYS A 335 ? 0.3471 0.2810 0.1836 -0.1444 -0.0575 0.0646  335 LYS A N   
2847 C CA  . LYS A 335 ? 0.4049 0.3418 0.2318 -0.1511 -0.0588 0.0682  335 LYS A CA  
2848 C C   . LYS A 335 ? 0.4222 0.3606 0.2468 -0.1532 -0.0542 0.0687  335 LYS A C   
2849 O O   . LYS A 335 ? 0.4595 0.4030 0.2749 -0.1588 -0.0500 0.0670  335 LYS A O   
2850 C CB  . LYS A 335 ? 0.4516 0.3866 0.2809 -0.1507 -0.0674 0.0763  335 LYS A CB  
2851 C CG  . LYS A 335 ? 0.5825 0.5206 0.4025 -0.1571 -0.0695 0.0811  335 LYS A CG  
2852 C CD  . LYS A 335 ? 0.7615 0.7010 0.5801 -0.1584 -0.0764 0.0853  335 LYS A CD  
2853 C CE  . LYS A 335 ? 0.8700 0.8150 0.6780 -0.1641 -0.0741 0.0810  335 LYS A CE  
2854 N NZ  . LYS A 335 ? 0.9074 0.8547 0.7123 -0.1665 -0.0809 0.0863  335 LYS A NZ  
2855 N N   . LYS A 336 ? 0.3733 0.3076 0.2066 -0.1487 -0.0543 0.0705  336 LYS A N   
2856 C CA  . LYS A 336 ? 0.3867 0.3227 0.2193 -0.1509 -0.0500 0.0712  336 LYS A CA  
2857 C C   . LYS A 336 ? 0.4001 0.3420 0.2288 -0.1527 -0.0412 0.0637  336 LYS A C   
2858 O O   . LYS A 336 ? 0.4283 0.3757 0.2509 -0.1577 -0.0371 0.0639  336 LYS A O   
2859 C CB  . LYS A 336 ? 0.4168 0.3466 0.2603 -0.1454 -0.0515 0.0733  336 LYS A CB  
2860 C CG  . LYS A 336 ? 0.6495 0.5721 0.4984 -0.1424 -0.0598 0.0802  336 LYS A CG  
2861 C CD  . LYS A 336 ? 0.7839 0.7053 0.6292 -0.1471 -0.0632 0.0878  336 LYS A CD  
2862 C CE  . LYS A 336 ? 0.8407 0.7536 0.6925 -0.1432 -0.0712 0.0943  336 LYS A CE  
2863 N NZ  . LYS A 336 ? 0.8270 0.7326 0.6891 -0.1371 -0.0714 0.0930  336 LYS A NZ  
2864 N N   . ILE A 337 ? 0.3946 0.3358 0.2276 -0.1485 -0.0381 0.0573  337 ILE A N   
2865 C CA  . ILE A 337 ? 0.3255 0.2718 0.1558 -0.1496 -0.0297 0.0500  337 ILE A CA  
2866 C C   . ILE A 337 ? 0.3956 0.3470 0.2136 -0.1558 -0.0272 0.0476  337 ILE A C   
2867 O O   . ILE A 337 ? 0.3981 0.3556 0.2111 -0.1590 -0.0207 0.0445  337 ILE A O   
2868 C CB  . ILE A 337 ? 0.3439 0.2878 0.1811 -0.1438 -0.0275 0.0442  337 ILE A CB  
2869 C CG1 . ILE A 337 ? 0.2972 0.2371 0.1468 -0.1372 -0.0287 0.0458  337 ILE A CG1 
2870 C CG2 . ILE A 337 ? 0.3546 0.3033 0.1885 -0.1451 -0.0188 0.0365  337 ILE A CG2 
2871 C CD1 . ILE A 337 ? 0.2915 0.2290 0.1490 -0.1307 -0.0279 0.0413  337 ILE A CD1 
2872 N N   . HIS A 338 ? 0.3627 0.3121 0.1761 -0.1573 -0.0323 0.0486  338 HIS A N   
2873 C CA  . HIS A 338 ? 0.3523 0.3058 0.1542 -0.1628 -0.0304 0.0459  338 HIS A CA  
2874 C C   . HIS A 338 ? 0.4521 0.4112 0.2466 -0.1678 -0.0290 0.0495  338 HIS A C   
2875 O O   . HIS A 338 ? 0.4583 0.4233 0.2449 -0.1709 -0.0226 0.0448  338 HIS A O   
2876 C CB  . HIS A 338 ? 0.3814 0.3318 0.1818 -0.1633 -0.0376 0.0483  338 HIS A CB  
2877 C CG  . HIS A 338 ? 0.4195 0.3735 0.2085 -0.1683 -0.0368 0.0456  338 HIS A CG  
2878 N ND1 . HIS A 338 ? 0.4818 0.4377 0.2649 -0.1721 -0.0421 0.0513  338 HIS A ND1 
2879 C CD2 . HIS A 338 ? 0.4423 0.3980 0.2250 -0.1693 -0.0313 0.0376  338 HIS A CD2 
2880 C CE1 . HIS A 338 ? 0.5229 0.4819 0.2962 -0.1754 -0.0400 0.0468  338 HIS A CE1 
2881 N NE2 . HIS A 338 ? 0.4707 0.4292 0.2436 -0.1735 -0.0335 0.0382  338 HIS A NE2 
2882 N N   . GLU A 339 ? 0.4915 0.4490 0.2885 -0.1684 -0.0345 0.0578  339 GLU A N   
2883 C CA  . GLU A 339 ? 0.4987 0.4617 0.2884 -0.1737 -0.0335 0.0622  339 GLU A CA  
2884 C C   . GLU A 339 ? 0.4483 0.4144 0.2419 -0.1737 -0.0284 0.0630  339 GLU A C   
2885 O O   . GLU A 339 ? 0.4786 0.4496 0.2672 -0.1782 -0.0274 0.0675  339 GLU A O   
2886 C CB  . GLU A 339 ? 0.5743 0.5343 0.3632 -0.1754 -0.0423 0.0713  339 GLU A CB  
2887 C CG  . GLU A 339 ? 0.6547 0.6068 0.4545 -0.1705 -0.0489 0.0764  339 GLU A CG  
2888 C CD  . GLU A 339 ? 0.7757 0.7252 0.5745 -0.1713 -0.0576 0.0832  339 GLU A CD  
2889 O OE1 . GLU A 339 ? 0.8371 0.7911 0.6261 -0.1763 -0.0584 0.0848  339 GLU A OE1 
2890 O OE2 . GLU A 339 ? 0.8321 0.7753 0.6399 -0.1665 -0.0634 0.0869  339 GLU A OE2 
2891 N N   . SER A 340 ? 0.5288 0.4931 0.3313 -0.1691 -0.0247 0.0587  340 SER A N   
2892 C CA  . SER A 340 ? 0.5030 0.4713 0.3100 -0.1692 -0.0194 0.0588  340 SER A CA  
2893 C C   . SER A 340 ? 0.4984 0.4758 0.3006 -0.1709 -0.0100 0.0517  340 SER A C   
2894 O O   . SER A 340 ? 0.4675 0.4509 0.2722 -0.1721 -0.0051 0.0525  340 SER A O   
2895 C CB  . SER A 340 ? 0.4998 0.4625 0.3194 -0.1630 -0.0200 0.0577  340 SER A CB  
2896 O OG  . SER A 340 ? 0.4507 0.4142 0.2732 -0.1594 -0.0150 0.0494  340 SER A OG  
2897 N N   . VAL A 341 ? 0.4334 0.4120 0.2294 -0.1708 -0.0071 0.0449  341 VAL A N   
2898 C CA  . VAL A 341 ? 0.3973 0.3840 0.1887 -0.1714 0.0020  0.0374  341 VAL A CA  
2899 C C   . VAL A 341 ? 0.3924 0.3816 0.1710 -0.1746 0.0025  0.0344  341 VAL A C   
2900 O O   . VAL A 341 ? 0.4507 0.4341 0.2260 -0.1752 -0.0038 0.0358  341 VAL A O   
2901 C CB  . VAL A 341 ? 0.4608 0.4456 0.2596 -0.1661 0.0068  0.0295  341 VAL A CB  
2902 C CG1 . VAL A 341 ? 0.4439 0.4281 0.2550 -0.1629 0.0075  0.0318  341 VAL A CG1 
2903 C CG2 . VAL A 341 ? 0.3920 0.3681 0.1910 -0.1637 0.0020  0.0273  341 VAL A CG2 
2904 N N   . ASP A 342 ? 0.4207 0.4190 0.1925 -0.1764 0.0098  0.0303  342 ASP A N   
2905 C CA  . ASP A 342 ? 0.4825 0.4835 0.2416 -0.1786 0.0108  0.0263  342 ASP A CA  
2906 C C   . ASP A 342 ? 0.5082 0.5067 0.2660 -0.1748 0.0150  0.0156  342 ASP A C   
2907 O O   . ASP A 342 ? 0.5404 0.5386 0.2884 -0.1759 0.0147  0.0114  342 ASP A O   
2908 C CB  . ASP A 342 ? 0.5804 0.5926 0.3312 -0.1820 0.0164  0.0270  342 ASP A CB  
2909 C CG  . ASP A 342 ? 0.7012 0.7216 0.4560 -0.1790 0.0264  0.0207  342 ASP A CG  
2910 O OD1 . ASP A 342 ? 0.7553 0.7727 0.5205 -0.1748 0.0284  0.0174  342 ASP A OD1 
2911 O OD2 . ASP A 342 ? 0.7833 0.8137 0.5306 -0.1806 0.0322  0.0192  342 ASP A OD2 
2912 N N   . PHE A 343 ? 0.4555 0.4517 0.2230 -0.1703 0.0186  0.0112  343 PHE A N   
2913 C CA  . PHE A 343 ? 0.4053 0.3973 0.1728 -0.1663 0.0215  0.0018  343 PHE A CA  
2914 C C   . PHE A 343 ? 0.3796 0.3610 0.1520 -0.1651 0.0142  0.0039  343 PHE A C   
2915 O O   . PHE A 343 ? 0.4001 0.3780 0.1758 -0.1668 0.0070  0.0123  343 PHE A O   
2916 C CB  . PHE A 343 ? 0.3917 0.3879 0.1666 -0.1616 0.0301  -0.0047 343 PHE A CB  
2917 C CG  . PHE A 343 ? 0.4198 0.4151 0.2076 -0.1599 0.0294  0.0001  343 PHE A CG  
2918 C CD1 . PHE A 343 ? 0.4285 0.4312 0.2203 -0.1616 0.0313  0.0056  343 PHE A CD1 
2919 C CD2 . PHE A 343 ? 0.3537 0.3411 0.1497 -0.1562 0.0272  -0.0012 343 PHE A CD2 
2920 C CE1 . PHE A 343 ? 0.3895 0.3911 0.1936 -0.1595 0.0303  0.0094  343 PHE A CE1 
2921 C CE2 . PHE A 343 ? 0.4257 0.4123 0.2336 -0.1539 0.0266  0.0026  343 PHE A CE2 
2922 C CZ  . PHE A 343 ? 0.4237 0.4172 0.2357 -0.1555 0.0279  0.0078  343 PHE A CZ  
2923 N N   . GLN A 344 ? 0.3546 0.3310 0.1281 -0.1616 0.0158  -0.0037 344 GLN A N   
2924 C CA  . GLN A 344 ? 0.3444 0.3119 0.1231 -0.1602 0.0093  -0.0016 344 GLN A CA  
2925 C C   . GLN A 344 ? 0.3633 0.3285 0.1534 -0.1559 0.0117  -0.0020 344 GLN A C   
2926 O O   . GLN A 344 ? 0.3439 0.3097 0.1367 -0.1521 0.0181  -0.0097 344 GLN A O   
2927 C CB  . GLN A 344 ? 0.3555 0.3182 0.1295 -0.1589 0.0085  -0.0087 344 GLN A CB  
2928 C CG  . GLN A 344 ? 0.3848 0.3515 0.1469 -0.1613 0.0102  -0.0129 344 GLN A CG  
2929 C CD  . GLN A 344 ? 0.4676 0.4284 0.2254 -0.1610 0.0062  -0.0175 344 GLN A CD  
2930 O OE1 . GLN A 344 ? 0.4436 0.4013 0.2004 -0.1635 -0.0015 -0.0121 344 GLN A OE1 
2931 N NE2 . GLN A 344 ? 0.3793 0.3381 0.1365 -0.1570 0.0113  -0.0275 344 GLN A NE2 
2932 N N   . PRO A 345 ? 0.3355 0.2982 0.1329 -0.1558 0.0065  0.0058  345 PRO A N   
2933 C CA  . PRO A 345 ? 0.3145 0.2754 0.1233 -0.1513 0.0085  0.0057  345 PRO A CA  
2934 C C   . PRO A 345 ? 0.3509 0.3048 0.1629 -0.1481 0.0069  0.0025  345 PRO A C   
2935 O O   . PRO A 345 ? 0.3537 0.3029 0.1619 -0.1493 0.0009  0.0039  345 PRO A O   
2936 C CB  . PRO A 345 ? 0.3746 0.3343 0.1898 -0.1512 0.0021  0.0148  345 PRO A CB  
2937 C CG  . PRO A 345 ? 0.3418 0.2987 0.1500 -0.1548 -0.0055 0.0196  345 PRO A CG  
2938 C CD  . PRO A 345 ? 0.3574 0.3183 0.1537 -0.1587 -0.0019 0.0147  345 PRO A CD  
2939 N N   . VAL A 346 ? 0.2984 0.2521 0.1181 -0.1439 0.0123  -0.0015 346 VAL A N   
2940 C CA  . VAL A 346 ? 0.3146 0.2630 0.1457 -0.1377 0.0098  -0.0045 346 VAL A CA  
2941 C C   . VAL A 346 ? 0.3524 0.2991 0.1963 -0.1345 0.0066  0.0018  346 VAL A C   
2942 O O   . VAL A 346 ? 0.2808 0.2312 0.1310 -0.1327 0.0101  0.0025  346 VAL A O   
2943 C CB  . VAL A 346 ? 0.3135 0.2627 0.1492 -0.1328 0.0166  -0.0140 346 VAL A CB  
2944 C CG1 . VAL A 346 ? 0.3383 0.2815 0.1846 -0.1274 0.0132  -0.0160 346 VAL A CG1 
2945 C CG2 . VAL A 346 ? 0.3272 0.2778 0.1493 -0.1357 0.0203  -0.0212 346 VAL A CG2 
2946 N N   . VAL A 347 ? 0.2609 0.2030 0.1095 -0.1323 -0.0006 0.0057  347 VAL A N   
2947 C CA  . VAL A 347 ? 0.2462 0.1881 0.1059 -0.1256 -0.0052 0.0111  347 VAL A CA  
2948 C C   . VAL A 347 ? 0.3080 0.2483 0.1799 -0.1178 -0.0058 0.0088  347 VAL A C   
2949 O O   . VAL A 347 ? 0.2896 0.2278 0.1623 -0.1166 -0.0101 0.0097  347 VAL A O   
2950 C CB  . VAL A 347 ? 0.3315 0.2716 0.1872 -0.1276 -0.0129 0.0183  347 VAL A CB  
2951 C CG1 . VAL A 347 ? 0.3068 0.2455 0.1743 -0.1207 -0.0171 0.0227  347 VAL A CG1 
2952 C CG2 . VAL A 347 ? 0.2905 0.2334 0.1354 -0.1346 -0.0123 0.0208  347 VAL A CG2 
2953 N N   . PHE A 348 ? 0.2800 0.2221 0.1616 -0.1127 -0.0017 0.0060  348 PHE A N   
2954 C CA  . PHE A 348 ? 0.2774 0.2189 0.1704 -0.1053 -0.0020 0.0042  348 PHE A CA  
2955 C C   . PHE A 348 ? 0.2864 0.2274 0.1878 -0.1000 -0.0068 0.0092  348 PHE A C   
2956 O O   . PHE A 348 ? 0.2687 0.2104 0.1729 -0.0991 -0.0067 0.0112  348 PHE A O   
2957 C CB  . PHE A 348 ? 0.2510 0.1946 0.1502 -0.1026 0.0043  -0.0010 348 PHE A CB  
2958 C CG  . PHE A 348 ? 0.2416 0.1837 0.1377 -0.1043 0.0083  -0.0074 348 PHE A CG  
2959 C CD1 . PHE A 348 ? 0.2727 0.2138 0.1567 -0.1117 0.0106  -0.0108 348 PHE A CD1 
2960 C CD2 . PHE A 348 ? 0.2986 0.2396 0.2037 -0.0987 0.0091  -0.0102 348 PHE A CD2 
2961 C CE1 . PHE A 348 ? 0.2855 0.2246 0.1670 -0.1109 0.0138  -0.0179 348 PHE A CE1 
2962 C CE2 . PHE A 348 ? 0.2782 0.2163 0.1813 -0.0994 0.0120  -0.0162 348 PHE A CE2 
2963 C CZ  . PHE A 348 ? 0.2367 0.1732 0.1280 -0.1054 0.0143  -0.0207 348 PHE A CZ  
2964 N N   . VAL A 349 ? 0.2263 0.1661 0.1321 -0.0968 -0.0109 0.0109  349 VAL A N   
2965 C CA  . VAL A 349 ? 0.1986 0.1378 0.1126 -0.0919 -0.0148 0.0146  349 VAL A CA  
2966 C C   . VAL A 349 ? 0.2362 0.1771 0.1599 -0.0863 -0.0127 0.0117  349 VAL A C   
2967 O O   . VAL A 349 ? 0.2052 0.1467 0.1303 -0.0857 -0.0131 0.0107  349 VAL A O   
2968 C CB  . VAL A 349 ? 0.2506 0.1882 0.1621 -0.0934 -0.0213 0.0196  349 VAL A CB  
2969 C CG1 . VAL A 349 ? 0.2342 0.1707 0.1543 -0.0884 -0.0251 0.0230  349 VAL A CG1 
2970 C CG2 . VAL A 349 ? 0.2843 0.2203 0.1853 -0.0997 -0.0236 0.0229  349 VAL A CG2 
2971 N N   . VAL A 350 ? 0.2001 0.1418 0.1299 -0.0827 -0.0104 0.0105  350 VAL A N   
2972 C CA  . VAL A 350 ? 0.2404 0.1840 0.1782 -0.0782 -0.0077 0.0076  350 VAL A CA  
2973 C C   . VAL A 350 ? 0.2124 0.1555 0.1569 -0.0741 -0.0098 0.0095  350 VAL A C   
2974 O O   . VAL A 350 ? 0.2089 0.1509 0.1534 -0.0743 -0.0101 0.0100  350 VAL A O   
2975 C CB  . VAL A 350 ? 0.1757 0.1209 0.1135 -0.0789 -0.0019 0.0030  350 VAL A CB  
2976 C CG1 . VAL A 350 ? 0.1852 0.1317 0.1309 -0.0747 0.0003  0.0007  350 VAL A CG1 
2977 C CG2 . VAL A 350 ? 0.2025 0.1470 0.1320 -0.0840 0.0005  0.0005  350 VAL A CG2 
2978 N N   . LEU A 351 ? 0.1691 0.1129 0.1191 -0.0709 -0.0113 0.0104  351 LEU A N   
2979 C CA  . LEU A 351 ? 0.1857 0.1285 0.1409 -0.0675 -0.0133 0.0117  351 LEU A CA  
2980 C C   . LEU A 351 ? 0.1741 0.1196 0.1350 -0.0646 -0.0132 0.0121  351 LEU A C   
2981 O O   . LEU A 351 ? 0.1844 0.1317 0.1455 -0.0659 -0.0123 0.0120  351 LEU A O   
2982 C CB  . LEU A 351 ? 0.1871 0.1258 0.1403 -0.0681 -0.0186 0.0157  351 LEU A CB  
2983 C CG  . LEU A 351 ? 0.1862 0.1249 0.1378 -0.0697 -0.0227 0.0196  351 LEU A CG  
2984 C CD1 . LEU A 351 ? 0.2644 0.2002 0.2184 -0.0666 -0.0277 0.0232  351 LEU A CD1 
2985 C CD2 . LEU A 351 ? 0.2061 0.1446 0.1500 -0.0744 -0.0230 0.0203  351 LEU A CD2 
2986 N N   . ASP A 352 ? 0.1851 0.1327 0.1513 -0.0587 -0.0139 0.0122  352 ASP A N   
2987 C CA  . ASP A 352 ? 0.1769 0.1300 0.1490 -0.0538 -0.0139 0.0135  352 ASP A CA  
2988 C C   . ASP A 352 ? 0.1596 0.1140 0.1318 -0.0553 -0.0171 0.0172  352 ASP A C   
2989 O O   . ASP A 352 ? 0.1966 0.1482 0.1661 -0.0566 -0.0208 0.0195  352 ASP A O   
2990 C CB  . ASP A 352 ? 0.1645 0.1199 0.1407 -0.0470 -0.0147 0.0132  352 ASP A CB  
2991 C CG  . ASP A 352 ? 0.2124 0.1677 0.1892 -0.0453 -0.0121 0.0096  352 ASP A CG  
2992 O OD1 . ASP A 352 ? 0.1899 0.1446 0.1654 -0.0488 -0.0092 0.0077  352 ASP A OD1 
2993 O OD2 . ASP A 352 ? 0.1947 0.1514 0.1736 -0.0401 -0.0131 0.0086  352 ASP A OD2 
2994 N N   . GLY A 353 ? 0.1389 0.0979 0.1149 -0.0550 -0.0162 0.0183  353 GLY A N   
2995 C CA  . GLY A 353 ? 0.1473 0.1088 0.1243 -0.0571 -0.0195 0.0220  353 GLY A CA  
2996 C C   . GLY A 353 ? 0.1459 0.1147 0.1299 -0.0513 -0.0213 0.0253  353 GLY A C   
2997 O O   . GLY A 353 ? 0.1854 0.1580 0.1716 -0.0526 -0.0243 0.0289  353 GLY A O   
2998 N N   . GLU A 354 ? 0.1305 0.1023 0.1181 -0.0448 -0.0195 0.0242  354 GLU A N   
2999 C CA  . GLU A 354 ? 0.1279 0.1081 0.1220 -0.0388 -0.0204 0.0270  354 GLU A CA  
3000 C C   . GLU A 354 ? 0.1501 0.1298 0.1446 -0.0320 -0.0215 0.0257  354 GLU A C   
3001 O O   . GLU A 354 ? 0.1279 0.1151 0.1276 -0.0261 -0.0220 0.0275  354 GLU A O   
3002 C CB  . GLU A 354 ? 0.1223 0.1099 0.1216 -0.0365 -0.0167 0.0277  354 GLU A CB  
3003 C CG  . GLU A 354 ? 0.1718 0.1588 0.1704 -0.0321 -0.0136 0.0242  354 GLU A CG  
3004 C CD  . GLU A 354 ? 0.4511 0.4312 0.4456 -0.0364 -0.0115 0.0209  354 GLU A CD  
3005 O OE1 . GLU A 354 ? 0.6719 0.6448 0.6612 -0.0394 -0.0126 0.0186  354 GLU A OE1 
3006 O OE2 . GLU A 354 ? 0.2999 0.2822 0.2966 -0.0366 -0.0086 0.0210  354 GLU A OE2 
3007 N N   . ASN A 355 ? 0.1545 0.1257 0.1439 -0.0326 -0.0221 0.0225  355 ASN A N   
3008 C CA  . ASN A 355 ? 0.1776 0.1474 0.1674 -0.0260 -0.0229 0.0202  355 ASN A CA  
3009 C C   . ASN A 355 ? 0.1572 0.1208 0.1453 -0.0250 -0.0276 0.0213  355 ASN A C   
3010 O O   . ASN A 355 ? 0.1872 0.1507 0.1771 -0.0182 -0.0289 0.0199  355 ASN A O   
3011 C CB  . ASN A 355 ? 0.1626 0.1279 0.1493 -0.0266 -0.0207 0.0158  355 ASN A CB  
3012 C CG  . ASN A 355 ? 0.1511 0.1234 0.1405 -0.0249 -0.0166 0.0149  355 ASN A CG  
3013 O OD1 . ASN A 355 ? 0.1571 0.1379 0.1509 -0.0201 -0.0155 0.0165  355 ASN A OD1 
3014 N ND2 . ASN A 355 ? 0.1362 0.1059 0.1236 -0.0289 -0.0142 0.0129  355 ASN A ND2 
3015 N N   . CYS A 356 ? 0.1553 0.1136 0.1397 -0.0313 -0.0301 0.0237  356 CYS A N   
3016 C CA  . CYS A 356 ? 0.1840 0.1352 0.1664 -0.0306 -0.0349 0.0255  356 CYS A CA  
3017 C C   . CYS A 356 ? 0.1884 0.1453 0.1759 -0.0266 -0.0382 0.0296  356 CYS A C   
3018 O O   . CYS A 356 ? 0.1712 0.1237 0.1595 -0.0221 -0.0420 0.0305  356 CYS A O   
3019 C CB  . CYS A 356 ? 0.2021 0.1454 0.1776 -0.0392 -0.0365 0.0269  356 CYS A CB  
3020 S SG  . CYS A 356 ? 0.1897 0.1377 0.1629 -0.0470 -0.0357 0.0296  356 CYS A SG  
3021 N N   . TRP A 357 ? 0.1784 0.1450 0.1700 -0.0279 -0.0371 0.0323  357 TRP A N   
3022 C CA  . TRP A 357 ? 0.1648 0.1379 0.1614 -0.0260 -0.0407 0.0371  357 TRP A CA  
3023 C C   . TRP A 357 ? 0.1536 0.1324 0.1569 -0.0157 -0.0412 0.0370  357 TRP A C   
3024 O O   . TRP A 357 ? 0.1744 0.1544 0.1810 -0.0126 -0.0454 0.0403  357 TRP A O   
3025 C CB  . TRP A 357 ? 0.1476 0.1301 0.1475 -0.0306 -0.0394 0.0398  357 TRP A CB  
3026 C CG  . TRP A 357 ? 0.1479 0.1243 0.1406 -0.0396 -0.0382 0.0384  357 TRP A CG  
3027 C CD1 . TRP A 357 ? 0.1739 0.1518 0.1662 -0.0427 -0.0339 0.0361  357 TRP A CD1 
3028 C CD2 . TRP A 357 ? 0.2235 0.1912 0.2083 -0.0462 -0.0410 0.0391  357 TRP A CD2 
3029 N NE1 . TRP A 357 ? 0.1589 0.1296 0.1436 -0.0503 -0.0336 0.0346  357 TRP A NE1 
3030 C CE2 . TRP A 357 ? 0.1574 0.1224 0.1371 -0.0528 -0.0378 0.0364  357 TRP A CE2 
3031 C CE3 . TRP A 357 ? 0.1903 0.1525 0.1718 -0.0471 -0.0460 0.0421  357 TRP A CE3 
3032 C CZ2 . TRP A 357 ? 0.1778 0.1358 0.1487 -0.0601 -0.0389 0.0361  357 TRP A CZ2 
3033 C CZ3 . TRP A 357 ? 0.1889 0.1439 0.1614 -0.0549 -0.0474 0.0425  357 TRP A CZ3 
3034 C CH2 . TRP A 357 ? 0.1972 0.1508 0.1643 -0.0613 -0.0435 0.0393  357 TRP A CH2 
3035 N N   . GLU A 358 ? 0.1495 0.1319 0.1548 -0.0100 -0.0372 0.0331  358 GLU A N   
3036 C CA  . GLU A 358 ? 0.1512 0.1400 0.1621 0.0004  -0.0371 0.0321  358 GLU A CA  
3037 C C   . GLU A 358 ? 0.1832 0.1612 0.1921 0.0051  -0.0413 0.0305  358 GLU A C   
3038 O O   . GLU A 358 ? 0.1931 0.1754 0.2070 0.0140  -0.0424 0.0302  358 GLU A O   
3039 C CB  . GLU A 358 ? 0.1467 0.1404 0.1579 0.0052  -0.0321 0.0277  358 GLU A CB  
3040 C CG  . GLU A 358 ? 0.2102 0.1930 0.2141 0.0012  -0.0309 0.0233  358 GLU A CG  
3041 C CD  . GLU A 358 ? 0.2414 0.2301 0.2451 0.0031  -0.0261 0.0202  358 GLU A CD  
3042 O OE1 . GLU A 358 ? 0.2458 0.2351 0.2487 0.0099  -0.0250 0.0160  358 GLU A OE1 
3043 O OE2 . GLU A 358 ? 0.1906 0.1844 0.1954 -0.0021 -0.0236 0.0226  358 GLU A OE2 
3044 N N   . TYR A 359 ? 0.1760 0.1401 0.1778 -0.0005 -0.0437 0.0294  359 TYR A N   
3045 C CA  . TYR A 359 ? 0.1886 0.1406 0.1883 0.0028  -0.0483 0.0287  359 TYR A CA  
3046 C C   . TYR A 359 ? 0.2283 0.1772 0.2284 -0.0003 -0.0537 0.0348  359 TYR A C   
3047 O O   . TYR A 359 ? 0.2421 0.1811 0.2415 0.0030  -0.0583 0.0354  359 TYR A O   
3048 C CB  . TYR A 359 ? 0.2404 0.1792 0.2327 -0.0017 -0.0482 0.0247  359 TYR A CB  
3049 C CG  . TYR A 359 ? 0.2093 0.1515 0.2011 0.0013  -0.0436 0.0188  359 TYR A CG  
3050 C CD1 . TYR A 359 ? 0.3091 0.2503 0.3023 0.0105  -0.0436 0.0140  359 TYR A CD1 
3051 C CD2 . TYR A 359 ? 0.2335 0.1800 0.2233 -0.0047 -0.0393 0.0180  359 TYR A CD2 
3052 C CE1 . TYR A 359 ? 0.2916 0.2366 0.2836 0.0131  -0.0398 0.0088  359 TYR A CE1 
3053 C CE2 . TYR A 359 ? 0.2775 0.2276 0.2670 -0.0019 -0.0355 0.0133  359 TYR A CE2 
3054 C CZ  . TYR A 359 ? 0.3348 0.2845 0.3251 0.0068  -0.0359 0.0089  359 TYR A CZ  
3055 O OH  . TYR A 359 ? 0.3879 0.3418 0.3771 0.0094  -0.0325 0.0044  359 TYR A OH  
3056 N N   . TYR A 360 ? 0.1807 0.1373 0.1817 -0.0065 -0.0537 0.0394  360 TYR A N   
3057 C CA  . TYR A 360 ? 0.2032 0.1594 0.2051 -0.0088 -0.0592 0.0455  360 TYR A CA  
3058 C C   . TYR A 360 ? 0.2470 0.2155 0.2589 -0.0007 -0.0607 0.0485  360 TYR A C   
3059 O O   . TYR A 360 ? 0.2368 0.2180 0.2549 0.0034  -0.0567 0.0472  360 TYR A O   
3060 C CB  . TYR A 360 ? 0.2101 0.1691 0.2079 -0.0195 -0.0593 0.0489  360 TYR A CB  
3061 C CG  . TYR A 360 ? 0.2390 0.1877 0.2266 -0.0289 -0.0585 0.0476  360 TYR A CG  
3062 C CD1 . TYR A 360 ? 0.2165 0.1616 0.2005 -0.0306 -0.0535 0.0422  360 TYR A CD1 
3063 C CD2 . TYR A 360 ? 0.2373 0.1812 0.2190 -0.0360 -0.0627 0.0522  360 TYR A CD2 
3064 C CE1 . TYR A 360 ? 0.2373 0.1749 0.2129 -0.0390 -0.0524 0.0414  360 TYR A CE1 
3065 C CE2 . TYR A 360 ? 0.2191 0.1554 0.1915 -0.0445 -0.0615 0.0513  360 TYR A CE2 
3066 C CZ  . TYR A 360 ? 0.2363 0.1698 0.2061 -0.0458 -0.0562 0.0458  360 TYR A CZ  
3067 O OH  . TYR A 360 ? 0.2437 0.1713 0.2049 -0.0541 -0.0548 0.0452  360 TYR A OH  
3068 N N   . GLU A 361 ? 0.2931 0.1805 0.2384 0.0120  -0.0584 0.0358  361 GLU A N   
3069 C CA  . GLU A 361 ? 0.3453 0.2482 0.2944 0.0257  -0.0596 0.0435  361 GLU A CA  
3070 C C   . GLU A 361 ? 0.3046 0.2385 0.2644 0.0216  -0.0642 0.0485  361 GLU A C   
3071 O O   . GLU A 361 ? 0.2900 0.2279 0.2512 0.0109  -0.0668 0.0508  361 GLU A O   
3072 C CB  . GLU A 361 ? 0.4692 0.3568 0.4112 0.0330  -0.0590 0.0528  361 GLU A CB  
3073 C CG  . GLU A 361 ? 0.7117 0.5949 0.6506 0.0216  -0.0612 0.0583  361 GLU A CG  
3074 C CD  . GLU A 361 ? 0.8299 0.6908 0.7627 0.0078  -0.0584 0.0514  361 GLU A CD  
3075 O OE1 . GLU A 361 ? 0.7544 0.6008 0.6849 0.0057  -0.0551 0.0418  361 GLU A OE1 
3076 O OE2 . GLU A 361 ? 0.8210 0.6812 0.7516 -0.0016 -0.0595 0.0553  361 GLU A OE2 
3077 N N   . GLU A 362 ? 0.2830 0.2386 0.2503 0.0295  -0.0645 0.0497  362 GLU A N   
3078 C CA  . GLU A 362 ? 0.2833 0.2680 0.2614 0.0256  -0.0684 0.0551  362 GLU A CA  
3079 C C   . GLU A 362 ? 0.2639 0.2517 0.2447 0.0106  -0.0701 0.0512  362 GLU A C   
3080 O O   . GLU A 362 ? 0.2132 0.2127 0.1984 0.0031  -0.0735 0.0554  362 GLU A O   
3081 C CB  . GLU A 362 ? 0.3020 0.2964 0.2817 0.0288  -0.0720 0.0653  362 GLU A CB  
3082 C CG  . GLU A 362 ? 0.4110 0.4271 0.3978 0.0423  -0.0723 0.0717  362 GLU A CG  
3083 C CD  . GLU A 362 ? 0.5692 0.5911 0.5552 0.0488  -0.0756 0.0817  362 GLU A CD  
3084 O OE1 . GLU A 362 ? 0.6479 0.6466 0.6238 0.0549  -0.0739 0.0837  362 GLU A OE1 
3085 O OE2 . GLU A 362 ? 0.6280 0.6748 0.6221 0.0463  -0.0777 0.0839  362 GLU A OE2 
3086 N N   . ASN A 363 ? 0.2373 0.2150 0.2153 0.0067  -0.0677 0.0427  363 ASN A N   
3087 C CA  . ASN A 363 ? 0.2110 0.1928 0.1922 -0.0049 -0.0687 0.0388  363 ASN A CA  
3088 C C   . ASN A 363 ? 0.1977 0.1712 0.1765 -0.0148 -0.0704 0.0403  363 ASN A C   
3089 O O   . ASN A 363 ? 0.2153 0.1966 0.1983 -0.0231 -0.0718 0.0401  363 ASN A O   
3090 C CB  . ASN A 363 ? 0.1815 0.1870 0.1721 -0.0060 -0.0701 0.0419  363 ASN A CB  
3091 C CG  . ASN A 363 ? 0.2302 0.2376 0.2229 -0.0143 -0.0700 0.0375  363 ASN A CG  
3092 O OD1 . ASN A 363 ? 0.1991 0.1966 0.1877 -0.0158 -0.0685 0.0305  363 ASN A OD1 
3093 N ND2 . ASN A 363 ? 0.2143 0.2340 0.2134 -0.0200 -0.0716 0.0415  363 ASN A ND2 
3094 N N   . GLY A 364 ? 0.2245 0.1812 0.1959 -0.0137 -0.0696 0.0421  364 GLY A N   
3095 C CA  . GLY A 364 ? 0.2107 0.1603 0.1784 -0.0228 -0.0704 0.0438  364 GLY A CA  
3096 C C   . GLY A 364 ? 0.2470 0.2107 0.2170 -0.0247 -0.0742 0.0507  364 GLY A C   
3097 O O   . GLY A 364 ? 0.1929 0.1525 0.1589 -0.0325 -0.0749 0.0514  364 GLY A O   
3098 N N   . ILE A 365 ? 0.2105 0.1918 0.1865 -0.0184 -0.0766 0.0555  365 ILE A N   
3099 C CA  . ILE A 365 ? 0.2189 0.2169 0.1986 -0.0222 -0.0801 0.0602  365 ILE A CA  
3100 C C   . ILE A 365 ? 0.2329 0.2256 0.2050 -0.0199 -0.0812 0.0656  365 ILE A C   
3101 O O   . ILE A 365 ? 0.2312 0.2255 0.2007 -0.0278 -0.0815 0.0648  365 ILE A O   
3102 C CB  . ILE A 365 ? 0.2143 0.2342 0.2046 -0.0169 -0.0787 0.0611  365 ILE A CB  
3103 C CG1 . ILE A 365 ? 0.1934 0.2169 0.1895 -0.0213 -0.0766 0.0561  365 ILE A CG1 
3104 C CG2 . ILE A 365 ? 0.2099 0.2453 0.2044 -0.0206 -0.0789 0.0628  365 ILE A CG2 
3105 C CD1 . ILE A 365 ? 0.2212 0.2628 0.2257 -0.0152 -0.0747 0.0576  365 ILE A CD1 
3106 N N   . PRO A 366 ? 0.2469 0.2320 0.2140 -0.0088 -0.0814 0.0713  366 PRO A N   
3107 C CA  . PRO A 366 ? 0.2813 0.2594 0.2396 -0.0065 -0.0815 0.0771  366 PRO A CA  
3108 C C   . PRO A 366 ? 0.2373 0.1965 0.1856 -0.0169 -0.0808 0.0757  366 PRO A C   
3109 O O   . PRO A 366 ? 0.2473 0.2101 0.1908 -0.0206 -0.0811 0.0780  366 PRO A O   
3110 C CB  . PRO A 366 ? 0.2633 0.2285 0.2170 0.0080  -0.0804 0.0830  366 PRO A CB  
3111 C CG  . PRO A 366 ? 0.2908 0.2698 0.2546 0.0151  -0.0799 0.0803  366 PRO A CG  
3112 C CD  . PRO A 366 ? 0.3318 0.3145 0.3011 0.0036  -0.0791 0.0715  366 PRO A CD  
3113 N N   . PHE A 367 ? 0.2485 0.1912 0.1959 -0.0215 -0.0765 0.0684  367 PHE A N   
3114 C CA  . PHE A 367 ? 0.2744 0.2025 0.2147 -0.0317 -0.0737 0.0656  367 PHE A CA  
3115 C C   . PHE A 367 ? 0.2847 0.2261 0.2271 -0.0419 -0.0759 0.0629  367 PHE A C   
3116 O O   . PHE A 367 ? 0.2584 0.1972 0.1928 -0.0472 -0.0760 0.0654  367 PHE A O   
3117 C CB  . PHE A 367 ? 0.2354 0.1480 0.1766 -0.0353 -0.0689 0.0575  367 PHE A CB  
3118 C CG  . PHE A 367 ? 0.2281 0.1312 0.1651 -0.0468 -0.0657 0.0541  367 PHE A CG  
3119 C CD1 . PHE A 367 ? 0.2444 0.1309 0.1708 -0.0487 -0.0628 0.0593  367 PHE A CD1 
3120 C CD2 . PHE A 367 ? 0.2553 0.1668 0.1987 -0.0548 -0.0651 0.0468  367 PHE A CD2 
3121 C CE1 . PHE A 367 ? 0.2622 0.1426 0.1853 -0.0595 -0.0592 0.0567  367 PHE A CE1 
3122 C CE2 . PHE A 367 ? 0.2594 0.1653 0.2002 -0.0644 -0.0617 0.0439  367 PHE A CE2 
3123 C CZ  . PHE A 367 ? 0.2329 0.1241 0.1637 -0.0672 -0.0586 0.0486  367 PHE A CZ  
3124 N N   . LEU A 368 ? 0.2236 0.1776 0.1756 -0.0448 -0.0770 0.0576  368 LEU A N   
3125 C CA  . LEU A 368 ? 0.1834 0.1453 0.1367 -0.0542 -0.0781 0.0540  368 LEU A CA  
3126 C C   . LEU A 368 ? 0.2152 0.1906 0.1675 -0.0549 -0.0812 0.0576  368 LEU A C   
3127 O O   . LEU A 368 ? 0.2400 0.2155 0.1872 -0.0620 -0.0808 0.0556  368 LEU A O   
3128 C CB  . LEU A 368 ? 0.1684 0.1382 0.1319 -0.0562 -0.0777 0.0483  368 LEU A CB  
3129 C CG  . LEU A 368 ? 0.1704 0.1303 0.1359 -0.0577 -0.0734 0.0421  368 LEU A CG  
3130 C CD1 . LEU A 368 ? 0.1912 0.1611 0.1660 -0.0580 -0.0735 0.0384  368 LEU A CD1 
3131 C CD2 . LEU A 368 ? 0.1952 0.1458 0.1553 -0.0653 -0.0702 0.0388  368 LEU A CD2 
3132 N N   . GLU A 369 ? 0.1996 0.1878 0.1581 -0.0471 -0.0820 0.0610  369 GLU A N   
3133 C CA  . GLU A 369 ? 0.2033 0.2062 0.1623 -0.0474 -0.0834 0.0629  369 GLU A CA  
3134 C C   . GLU A 369 ? 0.2343 0.2306 0.1808 -0.0473 -0.0844 0.0674  369 GLU A C   
3135 O O   . GLU A 369 ? 0.2430 0.2451 0.1851 -0.0533 -0.0854 0.0660  369 GLU A O   
3136 C CB  . GLU A 369 ? 0.2340 0.2534 0.2015 -0.0383 -0.0843 0.0663  369 GLU A CB  
3137 C CG  . GLU A 369 ? 0.1809 0.2103 0.1599 -0.0406 -0.0827 0.0623  369 GLU A CG  
3138 C CD  . GLU A 369 ? 0.2497 0.2984 0.2371 -0.0334 -0.0835 0.0656  369 GLU A CD  
3139 O OE1 . GLU A 369 ? 0.3297 0.3833 0.3143 -0.0245 -0.0853 0.0708  369 GLU A OE1 
3140 O OE2 . GLU A 369 ? 0.2816 0.3405 0.2779 -0.0364 -0.0822 0.0635  369 GLU A OE2 
3141 N N   . LYS A 370 ? 0.2453 0.2275 0.1846 -0.0405 -0.0835 0.0729  370 LYS A N   
3142 C CA  . LYS A 370 ? 0.2498 0.2242 0.1765 -0.0401 -0.0830 0.0782  370 LYS A CA  
3143 C C   . LYS A 370 ? 0.2362 0.1990 0.1543 -0.0516 -0.0812 0.0746  370 LYS A C   
3144 O O   . LYS A 370 ? 0.2574 0.2233 0.1668 -0.0555 -0.0814 0.0758  370 LYS A O   
3145 C CB  . LYS A 370 ? 0.3373 0.2956 0.2579 -0.0297 -0.0806 0.0856  370 LYS A CB  
3146 C CG  . LYS A 370 ? 0.6159 0.5667 0.5235 -0.0281 -0.0790 0.0925  370 LYS A CG  
3147 C CD  . LYS A 370 ? 0.7868 0.7226 0.6886 -0.0154 -0.0761 0.1011  370 LYS A CD  
3148 C CE  . LYS A 370 ? 0.8354 0.7672 0.7242 -0.0126 -0.0744 0.1092  370 LYS A CE  
3149 N NZ  . LYS A 370 ? 0.8691 0.7821 0.7484 -0.0228 -0.0695 0.1086  370 LYS A NZ  
3150 N N   . LEU A 371 ? 0.2258 0.1767 0.1455 -0.0568 -0.0793 0.0702  371 LEU A N   
3151 C CA  . LEU A 371 ? 0.2427 0.1848 0.1564 -0.0666 -0.0756 0.0656  371 LEU A CA  
3152 C C   . LEU A 371 ? 0.2663 0.2214 0.1790 -0.0739 -0.0782 0.0608  371 LEU A C   
3153 O O   . LEU A 371 ? 0.2466 0.2001 0.1487 -0.0792 -0.0767 0.0605  371 LEU A O   
3154 C CB  . LEU A 371 ? 0.2312 0.1651 0.1537 -0.0689 -0.0710 0.0581  371 LEU A CB  
3155 C CG  . LEU A 371 ? 0.2818 0.2114 0.2024 -0.0779 -0.0659 0.0520  371 LEU A CG  
3156 C CD1 . LEU A 371 ? 0.2728 0.1894 0.1820 -0.0806 -0.0615 0.0569  371 LEU A CD1 
3157 C CD2 . LEU A 371 ? 0.2853 0.2135 0.2167 -0.0797 -0.0630 0.0444  371 LEU A CD2 
3158 N N   . TYR A 372 ? 0.2148 0.1817 0.1392 -0.0739 -0.0801 0.0559  372 TYR A N   
3159 C CA  . TYR A 372 ? 0.2333 0.2080 0.1596 -0.0797 -0.0788 0.0495  372 TYR A CA  
3160 C C   . TYR A 372 ? 0.2836 0.2692 0.2044 -0.0796 -0.0812 0.0519  372 TYR A C   
3161 O O   . TYR A 372 ? 0.2754 0.2618 0.1886 -0.0854 -0.0802 0.0480  372 TYR A O   
3162 C CB  . TYR A 372 ? 0.2216 0.2025 0.1619 -0.0778 -0.0770 0.0453  372 TYR A CB  
3163 C CG  . TYR A 372 ? 0.2533 0.2263 0.1994 -0.0771 -0.0730 0.0412  372 TYR A CG  
3164 C CD1 . TYR A 372 ? 0.2187 0.1815 0.1597 -0.0799 -0.0700 0.0386  372 TYR A CD1 
3165 C CD2 . TYR A 372 ? 0.1800 0.1579 0.1370 -0.0729 -0.0714 0.0399  372 TYR A CD2 
3166 C CE1 . TYR A 372 ? 0.2285 0.1886 0.1771 -0.0768 -0.0649 0.0341  372 TYR A CE1 
3167 C CE2 . TYR A 372 ? 0.1702 0.1437 0.1324 -0.0704 -0.0675 0.0363  372 TYR A CE2 
3168 C CZ  . TYR A 372 ? 0.1989 0.1646 0.1575 -0.0717 -0.0642 0.0331  372 TYR A CZ  
3169 O OH  . TYR A 372 ? 0.1967 0.1621 0.1618 -0.0683 -0.0601 0.0291  372 TYR A OH  
3170 N N   . SER A 373 ? 0.2247 0.2200 0.1493 -0.0721 -0.0841 0.0579  373 SER A N   
3171 C CA  . SER A 373 ? 0.2431 0.2508 0.1622 -0.0707 -0.0869 0.0608  373 SER A CA  
3172 C C   . SER A 373 ? 0.3158 0.3156 0.2189 -0.0727 -0.0861 0.0639  373 SER A C   
3173 O O   . SER A 373 ? 0.3663 0.3735 0.2616 -0.0768 -0.0872 0.0618  373 SER A O   
3174 C CB  . SER A 373 ? 0.2750 0.2937 0.2002 -0.0598 -0.0894 0.0677  373 SER A CB  
3175 O OG  . SER A 373 ? 0.4065 0.4390 0.3265 -0.0575 -0.0927 0.0708  373 SER A OG  
3176 N N   . THR A 374 ? 0.2868 0.2710 0.1840 -0.0701 -0.0835 0.0687  374 THR A N   
3177 C CA  . THR A 374 ? 0.3032 0.2785 0.1848 -0.0719 -0.0809 0.0729  374 THR A CA  
3178 C C   . THR A 374 ? 0.3217 0.2935 0.1957 -0.0828 -0.0784 0.0655  374 THR A C   
3179 O O   . THR A 374 ? 0.3357 0.3124 0.1985 -0.0859 -0.0781 0.0651  374 THR A O   
3180 C CB  . THR A 374 ? 0.3122 0.2689 0.1908 -0.0672 -0.0769 0.0796  374 THR A CB  
3181 O OG1 . THR A 374 ? 0.3333 0.2925 0.2173 -0.0553 -0.0786 0.0861  374 THR A OG1 
3182 C CG2 . THR A 374 ? 0.3447 0.2912 0.2082 -0.0695 -0.0722 0.0846  374 THR A CG2 
3183 N N   . LEU A 375 ? 0.3404 0.3049 0.2198 -0.0879 -0.0766 0.0593  375 LEU A N   
3184 C CA  . LEU A 375 ? 0.3248 0.2860 0.1973 -0.0967 -0.0733 0.0517  375 LEU A CA  
3185 C C   . LEU A 375 ? 0.3111 0.2835 0.1835 -0.0997 -0.0743 0.0444  375 LEU A C   
3186 O O   . LEU A 375 ? 0.3348 0.3064 0.1955 -0.1048 -0.0715 0.0400  375 LEU A O   
3187 C CB  . LEU A 375 ? 0.2977 0.2527 0.1838 -0.0977 -0.0693 0.0446  375 LEU A CB  
3188 C CG  . LEU A 375 ? 0.2557 0.1991 0.1468 -0.0952 -0.0640 0.0477  375 LEU A CG  
3189 C CD1 . LEU A 375 ? 0.2635 0.2059 0.1694 -0.0953 -0.0616 0.0405  375 LEU A CD1 
3190 C CD2 . LEU A 375 ? 0.3745 0.3108 0.2549 -0.0993 -0.0573 0.0496  375 LEU A CD2 
3191 N N   . GLU A 376 ? 0.3071 0.2892 0.1917 -0.0967 -0.0773 0.0428  376 GLU A N   
3192 C CA  . GLU A 376 ? 0.3431 0.3346 0.2280 -0.0996 -0.0782 0.0365  376 GLU A CA  
3193 C C   . GLU A 376 ? 0.3485 0.3472 0.2189 -0.1013 -0.0801 0.0378  376 GLU A C   
3194 O O   . GLU A 376 ? 0.3922 0.3940 0.2568 -0.1062 -0.0795 0.0303  376 GLU A O   
3195 C CB  . GLU A 376 ? 0.3649 0.3676 0.2636 -0.0956 -0.0816 0.0383  376 GLU A CB  
3196 C CG  . GLU A 376 ? 0.4813 0.4913 0.3839 -0.0995 -0.0822 0.0314  376 GLU A CG  
3197 C CD  . GLU A 376 ? 0.5030 0.5268 0.4176 -0.0960 -0.0859 0.0351  376 GLU A CD  
3198 O OE1 . GLU A 376 ? 0.4711 0.5024 0.3879 -0.0897 -0.0890 0.0429  376 GLU A OE1 
3199 O OE2 . GLU A 376 ? 0.5075 0.5342 0.4292 -0.0991 -0.0854 0.0303  376 GLU A OE2 
3200 N N   . LYS A 377 ? 0.3117 0.3127 0.1759 -0.0963 -0.0820 0.0473  377 LYS A N   
3201 C CA  . LYS A 377 ? 0.3295 0.3400 0.1810 -0.0954 -0.0842 0.0503  377 LYS A CA  
3202 C C   . LYS A 377 ? 0.3527 0.3542 0.1875 -0.0969 -0.0797 0.0538  377 LYS A C   
3203 O O   . LYS A 377 ? 0.3618 0.3707 0.1840 -0.0964 -0.0805 0.0556  377 LYS A O   
3204 C CB  . LYS A 377 ? 0.3526 0.3747 0.2090 -0.0860 -0.0890 0.0595  377 LYS A CB  
3205 C CG  . LYS A 377 ? 0.3463 0.3809 0.2187 -0.0847 -0.0929 0.0565  377 LYS A CG  
3206 C CD  . LYS A 377 ? 0.4272 0.4727 0.3049 -0.0738 -0.0967 0.0658  377 LYS A CD  
3207 C CE  . LYS A 377 ? 0.4495 0.5084 0.3434 -0.0728 -0.0996 0.0634  377 LYS A CE  
3208 N NZ  . LYS A 377 ? 0.4430 0.4913 0.3484 -0.0742 -0.0961 0.0604  377 LYS A NZ  
3209 N N   . GLU A 378 ? 0.3384 0.3249 0.1724 -0.0990 -0.0748 0.0547  378 GLU A N   
3210 C CA  . GLU A 378 ? 0.4245 0.4023 0.2437 -0.1010 -0.0688 0.0590  378 GLU A CA  
3211 C C   . GLU A 378 ? 0.4381 0.4182 0.2460 -0.1085 -0.0652 0.0494  378 GLU A C   
3212 O O   . GLU A 378 ? 0.5052 0.4818 0.3175 -0.1134 -0.0633 0.0394  378 GLU A O   
3213 C CB  . GLU A 378 ? 0.5000 0.4619 0.3231 -0.1021 -0.0638 0.0623  378 GLU A CB  
3214 C CG  . GLU A 378 ? 0.5835 0.5378 0.4141 -0.0941 -0.0647 0.0722  378 GLU A CG  
3215 C CD  . GLU A 378 ? 0.6678 0.6197 0.4886 -0.0879 -0.0627 0.0830  378 GLU A CD  
3216 O OE1 . GLU A 378 ? 0.6744 0.6319 0.4819 -0.0901 -0.0608 0.0838  378 GLU A OE1 
3217 O OE2 . GLU A 378 ? 0.6839 0.6272 0.5095 -0.0802 -0.0624 0.0908  378 GLU A OE2 
3218 N N   . GLU A 379 ? 0.4469 0.4322 0.2398 -0.1083 -0.0636 0.0522  379 GLU A N   
3219 C CA  . GLU A 379 ? 0.4833 0.4727 0.2655 -0.1141 -0.0606 0.0415  379 GLU A CA  
3220 C C   . GLU A 379 ? 0.4556 0.4356 0.2299 -0.1193 -0.0512 0.0381  379 GLU A C   
3221 O O   . GLU A 379 ? 0.4917 0.4724 0.2612 -0.1235 -0.0478 0.0264  379 GLU A O   
3222 C CB  . GLU A 379 ? 0.6226 0.6240 0.3916 -0.1115 -0.0633 0.0447  379 GLU A CB  
3223 C CG  . GLU A 379 ? 0.7489 0.7623 0.5280 -0.1075 -0.0724 0.0452  379 GLU A CG  
3224 C CD  . GLU A 379 ? 0.7970 0.8243 0.5651 -0.1032 -0.0768 0.0500  379 GLU A CD  
3225 O OE1 . GLU A 379 ? 0.7215 0.7613 0.4925 -0.1043 -0.0828 0.0438  379 GLU A OE1 
3226 O OE2 . GLU A 379 ? 0.9066 0.9321 0.6634 -0.0987 -0.0740 0.0603  379 GLU A OE2 
3227 N N   . TRP A 380 ? 0.3930 0.3640 0.1675 -0.1188 -0.0461 0.0474  380 TRP A N   
3228 C CA  . TRP A 380 ? 0.4447 0.4098 0.2139 -0.1241 -0.0359 0.0449  380 TRP A CA  
3229 C C   . TRP A 380 ? 0.3972 0.3560 0.1875 -0.1241 -0.0331 0.0384  380 TRP A C   
3230 O O   . TRP A 380 ? 0.4543 0.4116 0.2496 -0.1263 -0.0239 0.0348  380 TRP A O   
3231 C CB  . TRP A 380 ? 0.3985 0.3585 0.1628 -0.1230 -0.0294 0.0576  380 TRP A CB  
3232 C CG  . TRP A 380 ? 0.4189 0.3705 0.1939 -0.1175 -0.0334 0.0682  380 TRP A CG  
3233 C CD1 . TRP A 380 ? 0.5007 0.4551 0.2751 -0.1098 -0.0403 0.0758  380 TRP A CD1 
3234 C CD2 . TRP A 380 ? 0.3901 0.3293 0.1784 -0.1185 -0.0300 0.0713  380 TRP A CD2 
3235 N NE1 . TRP A 380 ? 0.4803 0.4234 0.2656 -0.1051 -0.0411 0.0833  380 TRP A NE1 
3236 C CE2 . TRP A 380 ? 0.4513 0.3844 0.2454 -0.1106 -0.0351 0.0801  380 TRP A CE2 
3237 C CE3 . TRP A 380 ? 0.3839 0.3185 0.1832 -0.1238 -0.0229 0.0660  380 TRP A CE3 
3238 C CZ2 . TRP A 380 ? 0.4929 0.4128 0.2998 -0.1090 -0.0334 0.0832  380 TRP A CZ2 
3239 C CZ3 . TRP A 380 ? 0.3854 0.3089 0.1985 -0.1232 -0.0219 0.0696  380 TRP A CZ3 
3240 C CH2 . TRP A 380 ? 0.4651 0.3802 0.2812 -0.1159 -0.0271 0.0774  380 TRP A CH2 
3241 N N   . ILE A 381 ? 0.3268 0.2844 0.1311 -0.1212 -0.0404 0.0366  381 ILE A N   
3242 C CA  . ILE A 381 ? 0.3175 0.2710 0.1422 -0.1201 -0.0386 0.0303  381 ILE A CA  
3243 C C   . ILE A 381 ? 0.4093 0.3660 0.2376 -0.1207 -0.0421 0.0188  381 ILE A C   
3244 O O   . ILE A 381 ? 0.3805 0.3416 0.2041 -0.1212 -0.0501 0.0182  381 ILE A O   
3245 C CB  . ILE A 381 ? 0.3537 0.3019 0.1914 -0.1160 -0.0431 0.0377  381 ILE A CB  
3246 C CG1 . ILE A 381 ? 0.3866 0.3271 0.2201 -0.1158 -0.0391 0.0488  381 ILE A CG1 
3247 C CG2 . ILE A 381 ? 0.3649 0.3111 0.2224 -0.1147 -0.0419 0.0309  381 ILE A CG2 
3248 C CD1 . ILE A 381 ? 0.3690 0.3022 0.2114 -0.1107 -0.0437 0.0560  381 ILE A CD1 
3249 N N   . GLU A 382 ? 0.2895 0.2442 0.1266 -0.1207 -0.0360 0.0098  382 GLU A N   
3250 C CA  . GLU A 382 ? 0.3940 0.3471 0.2375 -0.1204 -0.0385 -0.0001 382 GLU A CA  
3251 C C   . GLU A 382 ? 0.3320 0.2821 0.1957 -0.1166 -0.0370 -0.0008 382 GLU A C   
3252 O O   . GLU A 382 ? 0.3003 0.2510 0.1707 -0.1153 -0.0296 -0.0024 382 GLU A O   
3253 C CB  . GLU A 382 ? 0.4866 0.4388 0.3198 -0.1221 -0.0324 -0.0111 382 GLU A CB  
3254 C CG  . GLU A 382 ? 0.6529 0.5995 0.4888 -0.1226 -0.0352 -0.0213 382 GLU A CG  
3255 C CD  . GLU A 382 ? 0.8765 0.8193 0.7001 -0.1235 -0.0286 -0.0330 382 GLU A CD  
3256 O OE1 . GLU A 382 ? 0.9352 0.8694 0.7643 -0.1218 -0.0267 -0.0419 382 GLU A OE1 
3257 O OE2 . GLU A 382 ? 0.9412 0.8889 0.7488 -0.1253 -0.0247 -0.0332 382 GLU A OE2 
3258 N N   . THR A 383 ? 0.3201 0.2692 0.1937 -0.1151 -0.0438 0.0005  383 THR A N   
3259 C CA  . THR A 383 ? 0.2367 0.1846 0.1289 -0.1094 -0.0416 -0.0005 383 THR A CA  
3260 C C   . THR A 383 ? 0.2724 0.2168 0.1674 -0.1077 -0.0379 -0.0098 383 THR A C   
3261 O O   . THR A 383 ? 0.2762 0.2179 0.1633 -0.1091 -0.0388 -0.0148 383 THR A O   
3262 C CB  . THR A 383 ? 0.2233 0.1738 0.1272 -0.1031 -0.0465 0.0057  383 THR A CB  
3263 O OG1 . THR A 383 ? 0.2276 0.1802 0.1289 -0.1029 -0.0502 0.0045  383 THR A OG1 
3264 C CG2 . THR A 383 ? 0.2792 0.2299 0.1798 -0.1047 -0.0501 0.0143  383 THR A CG2 
3265 N N   . LEU A 384 ? 0.2833 0.2270 0.1894 -0.1050 -0.0338 -0.0123 384 LEU A N   
3266 C CA  . LEU A 384 ? 0.2643 0.2028 0.1720 -0.1028 -0.0292 -0.0207 384 LEU A CA  
3267 C C   . LEU A 384 ? 0.2246 0.1614 0.1478 -0.0977 -0.0308 -0.0197 384 LEU A C   
3268 O O   . LEU A 384 ? 0.2416 0.1853 0.1763 -0.0941 -0.0324 -0.0135 384 LEU A O   
3269 C CB  . LEU A 384 ? 0.2680 0.2118 0.1758 -0.1002 -0.0200 -0.0239 384 LEU A CB  
3270 C CG  . LEU A 384 ? 0.2684 0.2157 0.1610 -0.1044 -0.0159 -0.0245 384 LEU A CG  
3271 C CD1 . LEU A 384 ? 0.2589 0.2141 0.1556 -0.1012 -0.0060 -0.0275 384 LEU A CD1 
3272 C CD2 . LEU A 384 ? 0.2798 0.2198 0.1557 -0.1076 -0.0175 -0.0311 384 LEU A CD2 
3273 N N   . THR A 385 ? 0.2327 0.1603 0.1559 -0.0955 -0.0290 -0.0256 385 THR A N   
3274 C CA  . THR A 385 ? 0.2242 0.1505 0.1613 -0.0888 -0.0281 -0.0242 385 THR A CA  
3275 C C   . THR A 385 ? 0.2994 0.2336 0.2438 -0.0819 -0.0210 -0.0256 385 THR A C   
3276 O O   . THR A 385 ? 0.2829 0.2216 0.2213 -0.0827 -0.0156 -0.0289 385 THR A O   
3277 C CB  . THR A 385 ? 0.2555 0.1668 0.1900 -0.0881 -0.0276 -0.0291 385 THR A CB  
3278 O OG1 . THR A 385 ? 0.2643 0.1681 0.1894 -0.0863 -0.0205 -0.0378 385 THR A OG1 
3279 C CG2 . THR A 385 ? 0.2600 0.1708 0.1915 -0.0920 -0.0330 -0.0271 385 THR A CG2 
3280 N N   . LEU A 386 ? 0.2546 0.1926 0.2125 -0.0750 -0.0207 -0.0228 386 LEU A N   
3281 C CA  . LEU A 386 ? 0.2395 0.1883 0.2062 -0.0677 -0.0144 -0.0241 386 LEU A CA  
3282 C C   . LEU A 386 ? 0.2376 0.1786 0.1978 -0.0629 -0.0068 -0.0315 386 LEU A C   
3283 O O   . LEU A 386 ? 0.2757 0.2271 0.2372 -0.0599 -0.0003 -0.0343 386 LEU A O   
3284 C CB  . LEU A 386 ? 0.2000 0.1549 0.1809 -0.0602 -0.0163 -0.0196 386 LEU A CB  
3285 C CG  . LEU A 386 ? 0.1835 0.1463 0.1708 -0.0634 -0.0232 -0.0134 386 LEU A CG  
3286 C CD1 . LEU A 386 ? 0.1759 0.1461 0.1754 -0.0551 -0.0245 -0.0096 386 LEU A CD1 
3287 C CD2 . LEU A 386 ? 0.1924 0.1677 0.1807 -0.0691 -0.0230 -0.0127 386 LEU A CD2 
3288 N N   . GLU A 387 ? 0.2790 0.2012 0.2318 -0.0626 -0.0072 -0.0352 387 GLU A N   
3289 C CA  . GLU A 387 ? 0.2903 0.2010 0.2346 -0.0581 0.0004  -0.0437 387 GLU A CA  
3290 C C   . GLU A 387 ? 0.3108 0.2246 0.2412 -0.0642 0.0036  -0.0493 387 GLU A C   
3291 O O   . GLU A 387 ? 0.3293 0.2465 0.2568 -0.0588 0.0119  -0.0548 387 GLU A O   
3292 C CB  . GLU A 387 ? 0.3116 0.1986 0.2494 -0.0591 -0.0011 -0.0470 387 GLU A CB  
3293 C CG  . GLU A 387 ? 0.4429 0.3135 0.3718 -0.0530 0.0073  -0.0566 387 GLU A CG  
3294 C CD  . GLU A 387 ? 0.7200 0.5640 0.6432 -0.0547 0.0064  -0.0598 387 GLU A CD  
3295 O OE1 . GLU A 387 ? 0.7934 0.6343 0.7196 -0.0619 -0.0010 -0.0543 387 GLU A OE1 
3296 O OE2 . GLU A 387 ? 0.8474 0.6732 0.7631 -0.0490 0.0136  -0.0680 387 GLU A OE2 
3297 N N   . GLU A 388 ? 0.3164 0.2300 0.2378 -0.0748 -0.0027 -0.0476 388 GLU A N   
3298 C CA  . GLU A 388 ? 0.3052 0.2224 0.2116 -0.0806 -0.0002 -0.0516 388 GLU A CA  
3299 C C   . GLU A 388 ? 0.3374 0.2734 0.2495 -0.0791 0.0049  -0.0479 388 GLU A C   
3300 O O   . GLU A 388 ? 0.3621 0.3026 0.2656 -0.0785 0.0122  -0.0527 388 GLU A O   
3301 C CB  . GLU A 388 ? 0.3309 0.2461 0.2277 -0.0909 -0.0088 -0.0486 388 GLU A CB  
3302 C CG  . GLU A 388 ? 0.3379 0.2365 0.2253 -0.0952 -0.0125 -0.0549 388 GLU A CG  
3303 C CD  . GLU A 388 ? 0.4176 0.3185 0.3005 -0.1044 -0.0224 -0.0504 388 GLU A CD  
3304 O OE1 . GLU A 388 ? 0.2845 0.1973 0.1748 -0.1048 -0.0267 -0.0409 388 GLU A OE1 
3305 O OE2 . GLU A 388 ? 0.5212 0.4164 0.3980 -0.1069 -0.0247 -0.0543 388 GLU A OE2 
3306 N N   . ALA A 389 ? 0.3042 0.2515 0.2305 -0.0791 0.0014  -0.0399 389 ALA A N   
3307 C CA  . ALA A 389 ? 0.3314 0.2965 0.2648 -0.0794 0.0061  -0.0366 389 ALA A CA  
3308 C C   . ALA A 389 ? 0.3508 0.3250 0.2924 -0.0703 0.0151  -0.0412 389 ALA A C   
3309 O O   . ALA A 389 ? 0.3180 0.3053 0.2587 -0.0709 0.0223  -0.0424 389 ALA A O   
3310 C CB  . ALA A 389 ? 0.3175 0.2907 0.2641 -0.0815 0.0002  -0.0288 389 ALA A CB  
3311 N N   . MET A 390 ? 0.3509 0.3189 0.3004 -0.0612 0.0151  -0.0431 390 MET A N   
3312 C CA  . MET A 390 ? 0.3954 0.3732 0.3546 -0.0499 0.0231  -0.0462 390 MET A CA  
3313 C C   . MET A 390 ? 0.4835 0.4551 0.4296 -0.0464 0.0321  -0.0550 390 MET A C   
3314 O O   . MET A 390 ? 0.4629 0.4501 0.4149 -0.0397 0.0407  -0.0572 390 MET A O   
3315 C CB  . MET A 390 ? 0.4228 0.3930 0.3921 -0.0400 0.0207  -0.0446 390 MET A CB  
3316 C CG  . MET A 390 ? 0.6045 0.5866 0.5856 -0.0259 0.0283  -0.0461 390 MET A CG  
3317 S SD  . MET A 390 ? 0.6712 0.6433 0.6626 -0.0131 0.0255  -0.0419 390 MET A SD  
3318 C CE  . MET A 390 ? 0.7102 0.6449 0.6830 -0.0131 0.0273  -0.0490 390 MET A CE  
3319 N N   . ARG A 391 ? 0.4080 0.3587 0.3364 -0.0508 0.0305  -0.0605 391 ARG A N   
3320 C CA  . ARG A 391 ? 0.4913 0.4324 0.4050 -0.0471 0.0388  -0.0708 391 ARG A CA  
3321 C C   . ARG A 391 ? 0.4532 0.3975 0.3489 -0.0570 0.0401  -0.0735 391 ARG A C   
3322 O O   . ARG A 391 ? 0.4801 0.4171 0.3606 -0.0550 0.0468  -0.0829 391 ARG A O   
3323 C CB  . ARG A 391 ? 0.5842 0.4974 0.4896 -0.0444 0.0370  -0.0772 391 ARG A CB  
3324 C CG  . ARG A 391 ? 0.7162 0.6237 0.6337 -0.0294 0.0421  -0.0779 391 ARG A CG  
3325 C CD  . ARG A 391 ? 0.8078 0.6927 0.7271 -0.0292 0.0360  -0.0760 391 ARG A CD  
3326 N NE  . ARG A 391 ? 0.8832 0.7660 0.8160 -0.0141 0.0402  -0.0730 391 ARG A NE  
3327 C CZ  . ARG A 391 ? 0.9179 0.7751 0.8489 -0.0088 0.0405  -0.0742 391 ARG A CZ  
3328 N NH1 . ARG A 391 ? 0.9402 0.7723 0.8570 -0.0189 0.0369  -0.0794 391 ARG A NH1 
3329 N NH2 . ARG A 391 ? 0.9031 0.7603 0.8463 0.0065  0.0445  -0.0697 391 ARG A NH2 
3330 N N   . LYS A 392 ? 0.4391 0.3936 0.3352 -0.0668 0.0344  -0.0655 392 LYS A N   
3331 C CA  . LYS A 392 ? 0.4174 0.3744 0.2954 -0.0757 0.0350  -0.0661 392 LYS A CA  
3332 C C   . LYS A 392 ? 0.3851 0.3583 0.2606 -0.0727 0.0467  -0.0686 392 LYS A C   
3333 O O   . LYS A 392 ? 0.3445 0.3356 0.2367 -0.0690 0.0514  -0.0642 392 LYS A O   
3334 C CB  . LYS A 392 ? 0.4933 0.4554 0.3734 -0.0852 0.0265  -0.0554 392 LYS A CB  
3335 C CG  . LYS A 392 ? 0.5607 0.5229 0.4209 -0.0938 0.0253  -0.0541 392 LYS A CG  
3336 C CD  . LYS A 392 ? 0.6394 0.5859 0.4828 -0.0974 0.0189  -0.0602 392 LYS A CD  
3337 C CE  . LYS A 392 ? 0.6386 0.5804 0.4852 -0.1029 0.0070  -0.0530 392 LYS A CE  
3338 N NZ  . LYS A 392 ? 0.6814 0.6136 0.5101 -0.1085 0.0012  -0.0589 392 LYS A NZ  
3339 N N   . GLU A 393 ? 0.3863 0.3550 0.2410 -0.0743 0.0517  -0.0761 393 GLU A N   
3340 C CA  . GLU A 393 ? 0.4805 0.4634 0.3304 -0.0699 0.0643  -0.0804 393 GLU A CA  
3341 C C   . GLU A 393 ? 0.4385 0.4378 0.2816 -0.0791 0.0668  -0.0725 393 GLU A C   
3342 O O   . GLU A 393 ? 0.5226 0.5408 0.3708 -0.0767 0.0771  -0.0715 393 GLU A O   
3343 C CB  . GLU A 393 ? 0.6957 0.6638 0.5246 -0.0658 0.0697  -0.0943 393 GLU A CB  
3344 C CG  . GLU A 393 ? 0.9241 0.8772 0.7299 -0.0759 0.0615  -0.0975 393 GLU A CG  
3345 C CD  . GLU A 393 ? 1.0688 1.0060 0.8804 -0.0804 0.0485  -0.0945 393 GLU A CD  
3346 O OE1 . GLU A 393 ? 1.1037 1.0427 0.9101 -0.0900 0.0393  -0.0873 393 GLU A OE1 
3347 O OE2 . GLU A 393 ? 1.1095 1.0337 0.9318 -0.0738 0.0478  -0.0984 393 GLU A OE2 
3348 N N   . ASP A 394 ? 0.4326 0.4256 0.2644 -0.0891 0.0581  -0.0664 394 ASP A N   
3349 C CA  . ASP A 394 ? 0.4755 0.4800 0.2971 -0.0975 0.0605  -0.0579 394 ASP A CA  
3350 C C   . ASP A 394 ? 0.4213 0.4342 0.2607 -0.1029 0.0570  -0.0451 394 ASP A C   
3351 O O   . ASP A 394 ? 0.4313 0.4409 0.2638 -0.1106 0.0511  -0.0360 394 ASP A O   
3352 C CB  . ASP A 394 ? 0.5596 0.5534 0.3566 -0.1040 0.0537  -0.0582 394 ASP A CB  
3353 C CG  . ASP A 394 ? 0.7069 0.6848 0.5063 -0.1058 0.0404  -0.0581 394 ASP A CG  
3354 O OD1 . ASP A 394 ? 0.7154 0.6883 0.5335 -0.1013 0.0374  -0.0590 394 ASP A OD1 
3355 O OD2 . ASP A 394 ? 0.7306 0.7032 0.5136 -0.1117 0.0329  -0.0566 394 ASP A OD2 
3356 N N   . VAL A 395 ? 0.3806 0.4045 0.2426 -0.0983 0.0606  -0.0446 395 VAL A N   
3357 C CA  . VAL A 395 ? 0.3658 0.3988 0.2455 -0.1038 0.0582  -0.0346 395 VAL A CA  
3358 C C   . VAL A 395 ? 0.4084 0.4649 0.3015 -0.1029 0.0696  -0.0343 395 VAL A C   
3359 O O   . VAL A 395 ? 0.4479 0.5135 0.3396 -0.0954 0.0786  -0.0419 395 VAL A O   
3360 C CB  . VAL A 395 ? 0.3372 0.3629 0.2339 -0.1004 0.0486  -0.0340 395 VAL A CB  
3361 C CG1 . VAL A 395 ? 0.3343 0.3393 0.2191 -0.1009 0.0382  -0.0350 395 VAL A CG1 
3362 C CG2 . VAL A 395 ? 0.3905 0.4240 0.3028 -0.0894 0.0529  -0.0409 395 VAL A CG2 
3363 N N   . LYS A 396 ? 0.3100 0.3768 0.2162 -0.1109 0.0694  -0.0258 396 LYS A N   
3364 C CA  . LYS A 396 ? 0.3086 0.4010 0.2308 -0.1120 0.0793  -0.0250 396 LYS A CA  
3365 C C   . LYS A 396 ? 0.3493 0.4528 0.2964 -0.1052 0.0764  -0.0279 396 LYS A C   
3366 O O   . LYS A 396 ? 0.2888 0.3807 0.2426 -0.1045 0.0660  -0.0266 396 LYS A O   
3367 C CB  . LYS A 396 ? 0.3645 0.4632 0.2877 -0.1261 0.0819  -0.0147 396 LYS A CB  
3368 C CG  . LYS A 396 ? 0.5047 0.5952 0.4030 -0.1321 0.0859  -0.0100 396 LYS A CG  
3369 C CD  . LYS A 396 ? 0.5647 0.6709 0.4537 -0.1281 0.0988  -0.0150 396 LYS A CD  
3370 C CE  . LYS A 396 ? 0.6122 0.7440 0.5138 -0.1357 0.1103  -0.0099 396 LYS A CE  
3371 N NZ  . LYS A 396 ? 0.6586 0.8051 0.5471 -0.1323 0.1234  -0.0135 396 LYS A NZ  
3372 N N   . THR A 397 ? 0.4110 0.4392 0.1382 -0.1166 0.0242  -0.0022 397 THR A N   
3373 C CA  . THR A 397 ? 0.3865 0.4163 0.1340 -0.1140 0.0329  -0.0078 397 THR A CA  
3374 C C   . THR A 397 ? 0.4177 0.4530 0.1740 -0.1129 0.0450  -0.0015 397 THR A C   
3375 O O   . THR A 397 ? 0.4156 0.4531 0.1599 -0.1144 0.0494  0.0037  397 THR A O   
3376 C CB  . THR A 397 ? 0.4128 0.4399 0.1589 -0.1116 0.0389  -0.0244 397 THR A CB  
3377 O OG1 . THR A 397 ? 0.4445 0.4726 0.1757 -0.1099 0.0486  -0.0293 397 THR A OG1 
3378 C CG2 . THR A 397 ? 0.4487 0.4704 0.1882 -0.1142 0.0262  -0.0312 397 THR A CG2 
3379 N N   . GLU A 398 ? 0.3867 0.4252 0.1653 -0.1105 0.0501  -0.0020 398 GLU A N   
3380 C CA  . GLU A 398 ? 0.4323 0.4784 0.2252 -0.1094 0.0603  0.0031  398 GLU A CA  
3381 C C   . GLU A 398 ? 0.3749 0.4261 0.1899 -0.1040 0.0675  -0.0047 398 GLU A C   
3382 O O   . GLU A 398 ? 0.3392 0.3860 0.1616 -0.1028 0.0626  -0.0091 398 GLU A O   
3383 C CB  . GLU A 398 ? 0.4714 0.5149 0.2707 -0.1133 0.0540  0.0179  398 GLU A CB  
3384 C CG  . GLU A 398 ? 0.5748 0.6258 0.3880 -0.1140 0.0629  0.0234  398 GLU A CG  
3385 C CD  . GLU A 398 ? 0.6765 0.7325 0.4750 -0.1162 0.0706  0.0255  398 GLU A CD  
3386 O OE1 . GLU A 398 ? 0.7339 0.7837 0.5099 -0.1189 0.0657  0.0287  398 GLU A OE1 
3387 O OE2 . GLU A 398 ? 0.7229 0.7906 0.5325 -0.1147 0.0813  0.0240  398 GLU A OE2 
3388 N N   . VAL A 399 ? 0.3703 0.4317 0.1965 -0.1003 0.0788  -0.0059 399 VAL A N   
3389 C CA  . VAL A 399 ? 0.4027 0.4707 0.2516 -0.0936 0.0852  -0.0117 399 VAL A CA  
3390 C C   . VAL A 399 ? 0.3858 0.4598 0.2564 -0.0952 0.0830  -0.0018 399 VAL A C   
3391 O O   . VAL A 399 ? 0.4510 0.5271 0.3196 -0.1003 0.0822  0.0077  399 VAL A O   
3392 C CB  . VAL A 399 ? 0.4507 0.5278 0.2999 -0.0864 0.0979  -0.0197 399 VAL A CB  
3393 C CG1 . VAL A 399 ? 0.4353 0.5210 0.3097 -0.0780 0.1038  -0.0233 399 VAL A CG1 
3394 C CG2 . VAL A 399 ? 0.4710 0.5380 0.2988 -0.0839 0.0991  -0.0316 399 VAL A CG2 
3395 N N   . ILE A 400 ? 0.3027 0.3776 0.1929 -0.0913 0.0815  -0.0041 400 ILE A N   
3396 C CA  . ILE A 400 ? 0.3232 0.4032 0.2349 -0.0917 0.0787  0.0032  400 ILE A CA  
3397 C C   . ILE A 400 ? 0.3472 0.4382 0.2801 -0.0830 0.0852  -0.0028 400 ILE A C   
3398 O O   . ILE A 400 ? 0.3388 0.4269 0.2728 -0.0771 0.0876  -0.0115 400 ILE A O   
3399 C CB  . ILE A 400 ? 0.3352 0.4046 0.2496 -0.0953 0.0673  0.0086  400 ILE A CB  
3400 C CG1 . ILE A 400 ? 0.3720 0.4440 0.3065 -0.0954 0.0638  0.0150  400 ILE A CG1 
3401 C CG2 . ILE A 400 ? 0.3008 0.3638 0.2196 -0.0899 0.0631  0.0011  400 ILE A CG2 
3402 C CD1 . ILE A 400 ? 0.3879 0.4478 0.3224 -0.0985 0.0527  0.0210  400 ILE A CD1 
3403 N N   . GLU A 401 ? 0.2356 0.3384 0.1842 -0.0822 0.0880  0.0019  401 GLU A N   
3404 C CA  . GLU A 401 ? 0.2346 0.3506 0.2026 -0.0732 0.0939  -0.0023 401 GLU A CA  
3405 C C   . GLU A 401 ? 0.2789 0.3962 0.2674 -0.0713 0.0873  0.0006  401 GLU A C   
3406 O O   . GLU A 401 ? 0.2615 0.3872 0.2651 -0.0627 0.0902  -0.0031 401 GLU A O   
3407 C CB  . GLU A 401 ? 0.2540 0.3860 0.2263 -0.0729 0.1022  0.0004  401 GLU A CB  
3408 C CG  . GLU A 401 ? 0.4115 0.5450 0.3650 -0.0718 0.1108  -0.0038 401 GLU A CG  
3409 C CD  . GLU A 401 ? 0.5752 0.7074 0.5263 -0.0606 0.1170  -0.0151 401 GLU A CD  
3410 O OE1 . GLU A 401 ? 0.5966 0.7352 0.5657 -0.0517 0.1186  -0.0180 401 GLU A OE1 
3411 O OE2 . GLU A 401 ? 0.6363 0.7597 0.5663 -0.0604 0.1198  -0.0211 401 GLU A OE2 
3412 N N   . SER A 402 ? 0.1999 0.3082 0.1880 -0.0783 0.0783  0.0070  402 SER A N   
3413 C CA  . SER A 402 ? 0.2072 0.3161 0.2128 -0.0766 0.0719  0.0094  402 SER A CA  
3414 C C   . SER A 402 ? 0.2149 0.3085 0.2140 -0.0827 0.0621  0.0142  402 SER A C   
3415 O O   . SER A 402 ? 0.2359 0.3216 0.2203 -0.0898 0.0603  0.0190  402 SER A O   
3416 C CB  . SER A 402 ? 0.2405 0.3626 0.2592 -0.0781 0.0743  0.0132  402 SER A CB  
3417 O OG  . SER A 402 ? 0.2787 0.4007 0.3120 -0.0770 0.0676  0.0146  402 SER A OG  
3418 N N   . VAL A 403 ? 0.1888 0.2780 0.1982 -0.0790 0.0558  0.0131  403 VAL A N   
3419 C CA  . VAL A 403 ? 0.2163 0.2923 0.2224 -0.0829 0.0466  0.0174  403 VAL A CA  
3420 C C   . VAL A 403 ? 0.2384 0.3163 0.2591 -0.0817 0.0426  0.0188  403 VAL A C   
3421 O O   . VAL A 403 ? 0.1877 0.2768 0.2221 -0.0764 0.0451  0.0158  403 VAL A O   
3422 C CB  . VAL A 403 ? 0.1803 0.2484 0.1831 -0.0805 0.0421  0.0146  403 VAL A CB  
3423 C CG1 . VAL A 403 ? 0.1700 0.2356 0.1555 -0.0836 0.0455  0.0127  403 VAL A CG1 
3424 C CG2 . VAL A 403 ? 0.2166 0.2903 0.2344 -0.0723 0.0426  0.0093  403 VAL A CG2 
3425 N N   . LYS A 404 ? 0.1743 0.2405 0.1907 -0.0870 0.0362  0.0235  404 LYS A N   
3426 C CA  . LYS A 404 ? 0.1763 0.2407 0.2032 -0.0868 0.0314  0.0237  404 LYS A CA  
3427 C C   . LYS A 404 ? 0.1574 0.2155 0.1878 -0.0813 0.0255  0.0210  404 LYS A C   
3428 O O   . LYS A 404 ? 0.1644 0.2114 0.1857 -0.0825 0.0212  0.0230  404 LYS A O   
3429 C CB  . LYS A 404 ? 0.2146 0.2674 0.2337 -0.0956 0.0281  0.0294  404 LYS A CB  
3430 C CG  . LYS A 404 ? 0.3409 0.3913 0.3691 -0.0973 0.0238  0.0287  404 LYS A CG  
3431 C CD  . LYS A 404 ? 0.3779 0.4140 0.3968 -0.1069 0.0211  0.0343  404 LYS A CD  
3432 C CE  . LYS A 404 ? 0.4500 0.4969 0.4693 -0.1135 0.0276  0.0370  404 LYS A CE  
3433 N NZ  . LYS A 404 ? 0.5631 0.5945 0.5731 -0.1236 0.0249  0.0429  404 LYS A NZ  
3434 N N   . ALA A 405 ? 0.1204 0.1867 0.1638 -0.0753 0.0253  0.0171  405 ALA A N   
3435 C CA  . ALA A 405 ? 0.1557 0.2192 0.2030 -0.0693 0.0213  0.0143  405 ALA A CA  
3436 C C   . ALA A 405 ? 0.1405 0.1911 0.1834 -0.0722 0.0140  0.0163  405 ALA A C   
3437 O O   . ALA A 405 ? 0.1475 0.1921 0.1895 -0.0771 0.0112  0.0181  405 ALA A O   
3438 C CB  . ALA A 405 ? 0.1322 0.2062 0.1925 -0.0631 0.0220  0.0112  405 ALA A CB  
3439 N N   . GLY A 406 ? 0.1206 0.1667 0.1609 -0.0697 0.0105  0.0159  406 GLY A N   
3440 C CA  . GLY A 406 ? 0.1845 0.2174 0.2211 -0.0676 0.0031  0.0170  406 GLY A CA  
3441 C C   . GLY A 406 ? 0.1871 0.2187 0.2230 -0.0594 -0.0002 0.0152  406 GLY A C   
3442 O O   . GLY A 406 ? 0.1382 0.1789 0.1781 -0.0566 0.0030  0.0126  406 GLY A O   
3443 N N   . THR A 407 ? 0.1417 0.1618 0.1726 -0.0558 -0.0067 0.0168  407 THR A N   
3444 C CA  . THR A 407 ? 0.1481 0.1698 0.1798 -0.0481 -0.0105 0.0157  407 THR A CA  
3445 C C   . THR A 407 ? 0.1833 0.1926 0.2041 -0.0468 -0.0164 0.0205  407 THR A C   
3446 O O   . THR A 407 ? 0.1961 0.1924 0.2081 -0.0518 -0.0175 0.0247  407 THR A O   
3447 C CB  . THR A 407 ? 0.1057 0.1299 0.1454 -0.0407 -0.0128 0.0119  407 THR A CB  
3448 O OG1 . THR A 407 ? 0.1320 0.1412 0.1663 -0.0387 -0.0177 0.0128  407 THR A OG1 
3449 C CG2 . THR A 407 ? 0.0902 0.1237 0.1384 -0.0420 -0.0083 0.0085  407 THR A CG2 
3450 N N   . TRP A 408 ? 0.1610 0.1747 0.1828 -0.0400 -0.0207 0.0203  408 TRP A N   
3451 C CA  . TRP A 408 ? 0.1563 0.1586 0.1682 -0.0367 -0.0274 0.0254  408 TRP A CA  
3452 C C   . TRP A 408 ? 0.1891 0.1772 0.2002 -0.0300 -0.0319 0.0257  408 TRP A C   
3453 O O   . TRP A 408 ? 0.2317 0.2080 0.2351 -0.0243 -0.0382 0.0299  408 TRP A O   
3454 C CB  . TRP A 408 ? 0.1407 0.1542 0.1542 -0.0314 -0.0318 0.0257  408 TRP A CB  
3455 C CG  . TRP A 408 ? 0.1722 0.2010 0.1996 -0.0245 -0.0320 0.0208  408 TRP A CG  
3456 C CD1 . TRP A 408 ? 0.1877 0.2192 0.2243 -0.0201 -0.0296 0.0167  408 TRP A CD1 
3457 C CD2 . TRP A 408 ? 0.1608 0.2053 0.1935 -0.0216 -0.0353 0.0203  408 TRP A CD2 
3458 N NE1 . TRP A 408 ? 0.1613 0.2095 0.2084 -0.0149 -0.0300 0.0139  408 TRP A NE1 
3459 C CE2 . TRP A 408 ? 0.1523 0.2093 0.1983 -0.0161 -0.0337 0.0161  408 TRP A CE2 
3460 C CE3 . TRP A 408 ? 0.1733 0.2238 0.2004 -0.0240 -0.0397 0.0228  408 TRP A CE3 
3461 C CZ2 . TRP A 408 ? 0.1356 0.2117 0.1909 -0.0138 -0.0357 0.0148  408 TRP A CZ2 
3462 C CZ3 . TRP A 408 ? 0.1371 0.2065 0.1735 -0.0217 -0.0428 0.0209  408 TRP A CZ3 
3463 C CH2 . TRP A 408 ? 0.1157 0.1981 0.1669 -0.0171 -0.0405 0.0171  408 TRP A CH2 
3464 N N   . PHE A 409 ? 0.1721 0.1589 0.1894 -0.0296 -0.0295 0.0211  409 PHE A N   
3465 C CA  . PHE A 409 ? 0.2476 0.2172 0.2612 -0.0241 -0.0337 0.0202  409 PHE A CA  
3466 C C   . PHE A 409 ? 0.2448 0.1983 0.2509 -0.0349 -0.0323 0.0222  409 PHE A C   
3467 O O   . PHE A 409 ? 0.2358 0.1957 0.2479 -0.0409 -0.0283 0.0184  409 PHE A O   
3468 C CB  . PHE A 409 ? 0.3135 0.2925 0.3371 -0.0160 -0.0328 0.0131  409 PHE A CB  
3469 C CG  . PHE A 409 ? 0.4821 0.4468 0.5019 -0.0051 -0.0378 0.0111  409 PHE A CG  
3470 C CD1 . PHE A 409 ? 0.5831 0.5229 0.5930 -0.0073 -0.0404 0.0108  409 PHE A CD1 
3471 C CD2 . PHE A 409 ? 0.5445 0.5200 0.5701 0.0074  -0.0401 0.0098  409 PHE A CD2 
3472 C CE1 . PHE A 409 ? 0.6667 0.5895 0.6712 0.0042  -0.0450 0.0082  409 PHE A CE1 
3473 C CE2 . PHE A 409 ? 0.6128 0.5757 0.6350 0.0197  -0.0443 0.0076  409 PHE A CE2 
3474 C CZ  . PHE A 409 ? 0.6439 0.5787 0.6548 0.0189  -0.0468 0.0065  409 PHE A CZ  
3475 N N   . ASP A 410 ? 0.2507 0.1851 0.2438 -0.0381 -0.0358 0.0291  410 ASP A N   
3476 C CA  . ASP A 410 ? 0.3495 0.2668 0.3338 -0.0502 -0.0348 0.0327  410 ASP A CA  
3477 C C   . ASP A 410 ? 0.3462 0.2799 0.3350 -0.0627 -0.0274 0.0334  410 ASP A C   
3478 O O   . ASP A 410 ? 0.3463 0.2733 0.3326 -0.0740 -0.0253 0.0351  410 ASP A O   
3479 C CB  . ASP A 410 ? 0.3894 0.2914 0.3737 -0.0502 -0.0370 0.0275  410 ASP A CB  
3480 C CG  . ASP A 410 ? 0.5430 0.4245 0.5206 -0.0370 -0.0438 0.0265  410 ASP A CG  
3481 O OD1 . ASP A 410 ? 0.5516 0.4240 0.5212 -0.0307 -0.0479 0.0328  410 ASP A OD1 
3482 O OD2 . ASP A 410 ? 0.5624 0.4370 0.5419 -0.0323 -0.0452 0.0192  410 ASP A OD2 
3483 N N   . GLY A 411 ? 0.2507 0.2059 0.2465 -0.0610 -0.0233 0.0318  411 GLY A N   
3484 C CA  . GLY A 411 ? 0.2161 0.1869 0.2164 -0.0701 -0.0158 0.0315  411 GLY A CA  
3485 C C   . GLY A 411 ? 0.1941 0.1764 0.2069 -0.0729 -0.0123 0.0259  411 GLY A C   
3486 O O   . GLY A 411 ? 0.2399 0.2339 0.2569 -0.0809 -0.0065 0.0264  411 GLY A O   
3487 N N   . ASN A 412 ? 0.1855 0.1668 0.2045 -0.0659 -0.0156 0.0206  412 ASN A N   
3488 C CA  . ASN A 412 ? 0.1820 0.1738 0.2110 -0.0683 -0.0136 0.0157  412 ASN A CA  
3489 C C   . ASN A 412 ? 0.1892 0.1889 0.2253 -0.0574 -0.0149 0.0101  412 ASN A C   
3490 O O   . ASN A 412 ? 0.1652 0.1649 0.2003 -0.0490 -0.0165 0.0100  412 ASN A O   
3491 C CB  . ASN A 412 ? 0.1707 0.1476 0.1952 -0.0767 -0.0168 0.0159  412 ASN A CB  
3492 C CG  . ASN A 412 ? 0.2775 0.2317 0.2937 -0.0701 -0.0236 0.0137  412 ASN A CG  
3493 O OD1 . ASN A 412 ? 0.2173 0.1741 0.2365 -0.0589 -0.0256 0.0089  412 ASN A OD1 
3494 N ND2 . ASN A 412 ? 0.2630 0.1936 0.2678 -0.0772 -0.0270 0.0174  412 ASN A ND2 
3495 N N   . PHE A 413 ? 0.1411 0.1494 0.1844 -0.0581 -0.0143 0.0057  413 PHE A N   
3496 C CA  . PHE A 413 ? 0.1717 0.1911 0.2215 -0.0493 -0.0140 0.0012  413 PHE A CA  
3497 C C   . PHE A 413 ? 0.1564 0.1666 0.2029 -0.0448 -0.0186 -0.0039 413 PHE A C   
3498 O O   . PHE A 413 ? 0.1215 0.1420 0.1723 -0.0387 -0.0180 -0.0076 413 PHE A O   
3499 C CB  . PHE A 413 ? 0.1049 0.1435 0.1645 -0.0515 -0.0095 0.0005  413 PHE A CB  
3500 C CG  . PHE A 413 ? 0.1341 0.1819 0.1967 -0.0527 -0.0041 0.0037  413 PHE A CG  
3501 C CD1 . PHE A 413 ? 0.1603 0.2134 0.2248 -0.0463 -0.0020 0.0035  413 PHE A CD1 
3502 C CD2 . PHE A 413 ? 0.1374 0.1886 0.2003 -0.0607 -0.0008 0.0065  413 PHE A CD2 
3503 C CE1 . PHE A 413 ? 0.1189 0.1773 0.1840 -0.0476 0.0028  0.0051  413 PHE A CE1 
3504 C CE2 . PHE A 413 ? 0.1165 0.1742 0.1797 -0.0597 0.0048  0.0080  413 PHE A CE2 
3505 C CZ  . PHE A 413 ? 0.1006 0.1614 0.1648 -0.0540 0.0063  0.0070  413 PHE A CZ  
3506 N N   . LEU A 414 ? 0.1610 0.1505 0.1983 -0.0475 -0.0231 -0.0042 414 LEU A N   
3507 C CA  . LEU A 414 ? 0.1823 0.1603 0.2145 -0.0441 -0.0274 -0.0106 414 LEU A CA  
3508 C C   . LEU A 414 ? 0.1985 0.1772 0.2299 -0.0300 -0.0281 -0.0145 414 LEU A C   
3509 O O   . LEU A 414 ? 0.1789 0.1538 0.2068 -0.0255 -0.0300 -0.0211 414 LEU A O   
3510 C CB  . LEU A 414 ? 0.2067 0.1576 0.2275 -0.0504 -0.0320 -0.0100 414 LEU A CB  
3511 C CG  . LEU A 414 ? 0.2483 0.1984 0.2696 -0.0665 -0.0315 -0.0068 414 LEU A CG  
3512 C CD1 . LEU A 414 ? 0.3355 0.2544 0.3435 -0.0735 -0.0362 -0.0054 414 LEU A CD1 
3513 C CD2 . LEU A 414 ? 0.2679 0.2348 0.2970 -0.0718 -0.0313 -0.0118 414 LEU A CD2 
3514 N N   . LYS A 415 ? 0.1861 0.1716 0.2207 -0.0233 -0.0264 -0.0110 415 LYS A N   
3515 C CA  . LYS A 415 ? 0.1499 0.1411 0.1861 -0.0105 -0.0264 -0.0143 415 LYS A CA  
3516 C C   . LYS A 415 ? 0.1905 0.2031 0.2345 -0.0083 -0.0222 -0.0170 415 LYS A C   
3517 O O   . LYS A 415 ? 0.1414 0.1609 0.1866 0.0011  -0.0212 -0.0204 415 LYS A O   
3518 C CB  . LYS A 415 ? 0.1953 0.1896 0.2336 -0.0051 -0.0268 -0.0095 415 LYS A CB  
3519 C CG  . LYS A 415 ? 0.3336 0.3050 0.3621 -0.0020 -0.0322 -0.0070 415 LYS A CG  
3520 C CD  . LYS A 415 ? 0.5357 0.4921 0.5572 -0.0151 -0.0331 -0.0028 415 LYS A CD  
3521 C CE  . LYS A 415 ? 0.3976 0.3716 0.4257 -0.0243 -0.0283 0.0016  415 LYS A CE  
3522 N NZ  . LYS A 415 ? 0.3638 0.3289 0.3868 -0.0367 -0.0277 0.0056  415 LYS A NZ  
3523 N N   . TRP A 416 ? 0.1582 0.1813 0.2069 -0.0162 -0.0195 -0.0152 416 TRP A N   
3524 C CA  . TRP A 416 ? 0.1316 0.1729 0.1864 -0.0142 -0.0157 -0.0159 416 TRP A CA  
3525 C C   . TRP A 416 ? 0.0940 0.1396 0.1487 -0.0192 -0.0163 -0.0181 416 TRP A C   
3526 O O   . TRP A 416 ? 0.1068 0.1659 0.1644 -0.0165 -0.0140 -0.0184 416 TRP A O   
3527 C CB  . TRP A 416 ? 0.0786 0.1317 0.1407 -0.0168 -0.0114 -0.0105 416 TRP A CB  
3528 C CG  . TRP A 416 ? 0.1102 0.1628 0.1732 -0.0132 -0.0116 -0.0083 416 TRP A CG  
3529 C CD1 . TRP A 416 ? 0.0960 0.1590 0.1629 -0.0069 -0.0100 -0.0085 416 TRP A CD1 
3530 C CD2 . TRP A 416 ? 0.1054 0.1482 0.1650 -0.0161 -0.0138 -0.0051 416 TRP A CD2 
3531 N NE1 . TRP A 416 ? 0.0814 0.1432 0.1490 -0.0057 -0.0119 -0.0061 416 TRP A NE1 
3532 C CE2 . TRP A 416 ? 0.1166 0.1652 0.1787 -0.0108 -0.0144 -0.0038 416 TRP A CE2 
3533 C CE3 . TRP A 416 ? 0.1705 0.2018 0.2251 -0.0233 -0.0152 -0.0027 416 TRP A CE3 
3534 C CZ2 . TRP A 416 ? 0.1359 0.1784 0.1945 -0.0116 -0.0174 -0.0003 416 TRP A CZ2 
3535 C CZ3 . TRP A 416 ? 0.1628 0.1864 0.2126 -0.0244 -0.0173 0.0012  416 TRP A CZ3 
3536 C CH2 . TRP A 416 ? 0.1834 0.2125 0.2349 -0.0182 -0.0187 0.0023  416 TRP A CH2 
3537 N N   . ILE A 417 ? 0.1126 0.1485 0.1643 -0.0270 -0.0196 -0.0190 417 ILE A N   
3538 C CA  . ILE A 417 ? 0.1360 0.1799 0.1895 -0.0328 -0.0210 -0.0209 417 ILE A CA  
3539 C C   . ILE A 417 ? 0.1802 0.2076 0.2270 -0.0408 -0.0261 -0.0241 417 ILE A C   
3540 O O   . ILE A 417 ? 0.1864 0.1974 0.2288 -0.0437 -0.0272 -0.0222 417 ILE A O   
3541 C CB  . ILE A 417 ? 0.1030 0.1629 0.1664 -0.0372 -0.0172 -0.0155 417 ILE A CB  
3542 C CG1 . ILE A 417 ? 0.1384 0.2132 0.2059 -0.0392 -0.0187 -0.0168 417 ILE A CG1 
3543 C CG2 . ILE A 417 ? 0.1172 0.1717 0.1822 -0.0458 -0.0163 -0.0118 417 ILE A CG2 
3544 C CD1 . ILE A 417 ? 0.1276 0.2192 0.2049 -0.0383 -0.0142 -0.0116 417 ILE A CD1 
3545 N N   . GLY A 418 ? 0.1833 0.2139 0.2280 -0.0448 -0.0297 -0.0290 418 GLY A N   
3546 C CA  . GLY A 418 ? 0.2053 0.2218 0.2448 -0.0558 -0.0348 -0.0319 418 GLY A CA  
3547 C C   . GLY A 418 ? 0.3565 0.3527 0.3826 -0.0542 -0.0401 -0.0406 418 GLY A C   
3548 O O   . GLY A 418 ? 0.4840 0.4657 0.5046 -0.0649 -0.0448 -0.0435 418 GLY A O   
3549 N N   . ASN A 419 ? 0.3512 0.3451 0.3713 -0.0417 -0.0394 -0.0453 419 ASN A N   
3550 C CA  . ASN A 419 ? 0.3527 0.3314 0.3594 -0.0396 -0.0441 -0.0554 419 ASN A CA  
3551 C C   . ASN A 419 ? 0.3333 0.3326 0.3396 -0.0339 -0.0433 -0.0591 419 ASN A C   
3552 O O   . ASN A 419 ? 0.2722 0.2940 0.2883 -0.0304 -0.0389 -0.0531 419 ASN A O   
3553 C CB  . ASN A 419 ? 0.3512 0.3052 0.3475 -0.0290 -0.0442 -0.0591 419 ASN A CB  
3554 C CG  . ASN A 419 ? 0.3438 0.3107 0.3435 -0.0135 -0.0388 -0.0581 419 ASN A CG  
3555 O OD1 . ASN A 419 ? 0.3753 0.3664 0.3821 -0.0105 -0.0349 -0.0558 419 ASN A OD1 
3556 N ND2 . ASN A 419 ? 0.3732 0.3236 0.3679 -0.0035 -0.0386 -0.0594 419 ASN A ND2 
3557 N N   . LYS A 420 ? 0.2597 0.2497 0.2532 -0.0334 -0.0477 -0.0691 420 LYS A N   
3558 C CA  . LYS A 420 ? 0.2428 0.2526 0.2336 -0.0302 -0.0480 -0.0724 420 LYS A CA  
3559 C C   . LYS A 420 ? 0.3058 0.3307 0.2992 -0.0166 -0.0409 -0.0690 420 LYS A C   
3560 O O   . LYS A 420 ? 0.2443 0.2916 0.2429 -0.0154 -0.0388 -0.0643 420 LYS A O   
3561 C CB  . LYS A 420 ? 0.4365 0.4313 0.4097 -0.0314 -0.0540 -0.0852 420 LYS A CB  
3562 C CG  . LYS A 420 ? 0.5533 0.5690 0.5210 -0.0289 -0.0553 -0.0887 420 LYS A CG  
3563 C CD  . LYS A 420 ? 0.6881 0.6915 0.6392 -0.0356 -0.0635 -0.1012 420 LYS A CD  
3564 C CE  . LYS A 420 ? 0.7441 0.7739 0.6950 -0.0399 -0.0677 -0.1010 420 LYS A CE  
3565 N NZ  . LYS A 420 ? 0.7068 0.7647 0.6756 -0.0381 -0.0634 -0.0875 420 LYS A NZ  
3566 N N   . GLU A 421 ? 0.2723 0.2856 0.2627 -0.0065 -0.0373 -0.0705 421 GLU A N   
3567 C CA  . GLU A 421 ? 0.2514 0.2807 0.2446 0.0052  -0.0304 -0.0679 421 GLU A CA  
3568 C C   . GLU A 421 ? 0.2344 0.2801 0.2431 0.0035  -0.0258 -0.0563 421 GLU A C   
3569 O O   . GLU A 421 ? 0.2063 0.2712 0.2189 0.0062  -0.0216 -0.0517 421 GLU A O   
3570 C CB  . GLU A 421 ? 0.3796 0.3949 0.3669 0.0170  -0.0282 -0.0733 421 GLU A CB  
3571 C CG  . GLU A 421 ? 0.4990 0.4987 0.4686 0.0223  -0.0311 -0.0863 421 GLU A CG  
3572 C CD  . GLU A 421 ? 0.7085 0.6784 0.6694 0.0142  -0.0386 -0.0921 421 GLU A CD  
3573 O OE1 . GLU A 421 ? 0.7409 0.7022 0.7097 0.0061  -0.0406 -0.0852 421 GLU A OE1 
3574 O OE2 . GLU A 421 ? 0.8119 0.7664 0.7568 0.0152  -0.0424 -0.1035 421 GLU A OE2 
3575 N N   . LYS A 422 ? 0.2297 0.2666 0.2460 -0.0013 -0.0264 -0.0514 422 LYS A N   
3576 C CA  . LYS A 422 ? 0.2027 0.2532 0.2318 -0.0038 -0.0223 -0.0417 422 LYS A CA  
3577 C C   . LYS A 422 ? 0.1976 0.2630 0.2317 -0.0105 -0.0228 -0.0379 422 LYS A C   
3578 O O   . LYS A 422 ? 0.1509 0.2310 0.1917 -0.0085 -0.0186 -0.0317 422 LYS A O   
3579 C CB  . LYS A 422 ? 0.2421 0.2799 0.2756 -0.0082 -0.0232 -0.0377 422 LYS A CB  
3580 C CG  . LYS A 422 ? 0.2314 0.2566 0.2615 0.0002  -0.0230 -0.0395 422 LYS A CG  
3581 C CD  . LYS A 422 ? 0.1741 0.1861 0.2063 -0.0045 -0.0247 -0.0345 422 LYS A CD  
3582 C CE  . LYS A 422 ? 0.2210 0.2174 0.2477 0.0048  -0.0266 -0.0366 422 LYS A CE  
3583 N NZ  . LYS A 422 ? 0.2037 0.2166 0.2369 0.0157  -0.0226 -0.0355 422 LYS A NZ  
3584 N N   . ASN A 423 ? 0.2205 0.2822 0.2516 -0.0183 -0.0283 -0.0413 423 ASN A N   
3585 C CA  . ASN A 423 ? 0.2164 0.2955 0.2539 -0.0233 -0.0295 -0.0376 423 ASN A CA  
3586 C C   . ASN A 423 ? 0.2194 0.3128 0.2521 -0.0167 -0.0285 -0.0377 423 ASN A C   
3587 O O   . ASN A 423 ? 0.1636 0.2727 0.2028 -0.0163 -0.0271 -0.0313 423 ASN A O   
3588 C CB  . ASN A 423 ? 0.1954 0.2714 0.2319 -0.0341 -0.0363 -0.0415 423 ASN A CB  
3589 C CG  . ASN A 423 ? 0.2093 0.2758 0.2523 -0.0428 -0.0362 -0.0384 423 ASN A CG  
3590 O OD1 . ASN A 423 ? 0.2013 0.2661 0.2499 -0.0404 -0.0313 -0.0328 423 ASN A OD1 
3591 N ND2 . ASN A 423 ? 0.2174 0.2794 0.2594 -0.0542 -0.0416 -0.0417 423 ASN A ND2 
3592 N N   . GLU A 424 ? 0.1950 0.2829 0.2155 -0.0108 -0.0289 -0.0446 424 GLU A N   
3593 C CA  . GLU A 424 ? 0.2112 0.3130 0.2251 -0.0048 -0.0271 -0.0440 424 GLU A CA  
3594 C C   . GLU A 424 ? 0.1207 0.2329 0.1418 0.0005  -0.0196 -0.0350 424 GLU A C   
3595 O O   . GLU A 424 ? 0.1699 0.2954 0.1909 0.0020  -0.0183 -0.0291 424 GLU A O   
3596 C CB  . GLU A 424 ? 0.2076 0.3016 0.2060 0.0012  -0.0276 -0.0540 424 GLU A CB  
3597 C CG  . GLU A 424 ? 0.3572 0.4663 0.3462 0.0072  -0.0251 -0.0533 424 GLU A CG  
3598 C CD  . GLU A 424 ? 0.4417 0.5639 0.4282 0.0025  -0.0307 -0.0508 424 GLU A CD  
3599 O OE1 . GLU A 424 ? 0.4312 0.5503 0.4201 -0.0056 -0.0379 -0.0538 424 GLU A OE1 
3600 O OE2 . GLU A 424 ? 0.4505 0.5869 0.4326 0.0068  -0.0280 -0.0453 424 GLU A OE2 
3601 N N   . TYR A 425 ? 0.1356 0.2412 0.1624 0.0028  -0.0152 -0.0333 425 TYR A N   
3602 C CA  . TYR A 425 ? 0.1176 0.2318 0.1520 0.0051  -0.0087 -0.0251 425 TYR A CA  
3603 C C   . TYR A 425 ? 0.1244 0.2438 0.1678 0.0004  -0.0086 -0.0173 425 TYR A C   
3604 O O   . TYR A 425 ? 0.1123 0.2401 0.1573 0.0022  -0.0050 -0.0105 425 TYR A O   
3605 C CB  . TYR A 425 ? 0.0930 0.2006 0.1330 0.0071  -0.0056 -0.0252 425 TYR A CB  
3606 C CG  . TYR A 425 ? 0.1249 0.2373 0.1611 0.0148  -0.0016 -0.0283 425 TYR A CG  
3607 C CD1 . TYR A 425 ? 0.1320 0.2476 0.1566 0.0200  -0.0015 -0.0344 425 TYR A CD1 
3608 C CD2 . TYR A 425 ? 0.1512 0.2674 0.1953 0.0169  0.0026  -0.0251 425 TYR A CD2 
3609 C CE1 . TYR A 425 ? 0.1500 0.2729 0.1717 0.0280  0.0035  -0.0375 425 TYR A CE1 
3610 C CE2 . TYR A 425 ? 0.1302 0.2552 0.1733 0.0243  0.0068  -0.0277 425 TYR A CE2 
3611 C CZ  . TYR A 425 ? 0.1853 0.3141 0.2174 0.0302  0.0078  -0.0338 425 TYR A CZ  
3612 O OH  . TYR A 425 ? 0.1924 0.3328 0.2243 0.0383  0.0132  -0.0365 425 TYR A OH  
3613 N N   . TRP A 426 ? 0.1031 0.2169 0.1523 -0.0053 -0.0121 -0.0179 426 TRP A N   
3614 C CA  . TRP A 426 ? 0.1132 0.2337 0.1712 -0.0082 -0.0115 -0.0115 426 TRP A CA  
3615 C C   . TRP A 426 ? 0.1242 0.2572 0.1797 -0.0065 -0.0143 -0.0093 426 TRP A C   
3616 O O   . TRP A 426 ? 0.0934 0.2331 0.1530 -0.0038 -0.0118 -0.0022 426 TRP A O   
3617 C CB  . TRP A 426 ? 0.0974 0.2125 0.1616 -0.0151 -0.0141 -0.0130 426 TRP A CB  
3618 C CG  . TRP A 426 ? 0.1232 0.2278 0.1903 -0.0165 -0.0110 -0.0122 426 TRP A CG  
3619 C CD1 . TRP A 426 ? 0.0744 0.1659 0.1375 -0.0181 -0.0130 -0.0165 426 TRP A CD1 
3620 C CD2 . TRP A 426 ? 0.1161 0.2212 0.1892 -0.0160 -0.0060 -0.0069 426 TRP A CD2 
3621 N NE1 . TRP A 426 ? 0.0994 0.1856 0.1661 -0.0185 -0.0099 -0.0133 426 TRP A NE1 
3622 C CE2 . TRP A 426 ? 0.1009 0.1955 0.1736 -0.0179 -0.0056 -0.0081 426 TRP A CE2 
3623 C CE3 . TRP A 426 ? 0.1358 0.2476 0.2135 -0.0140 -0.0022 -0.0014 426 TRP A CE3 
3624 C CZ2 . TRP A 426 ? 0.1308 0.2235 0.2072 -0.0186 -0.0018 -0.0045 426 TRP A CZ2 
3625 C CZ3 . TRP A 426 ? 0.1342 0.2414 0.2153 -0.0148 0.0021  0.0015  426 TRP A CZ3 
3626 C CH2 . TRP A 426 ? 0.1486 0.2473 0.2289 -0.0176 0.0021  -0.0004 426 TRP A CH2 
3627 N N   . LYS A 427 ? 0.0893 0.2244 0.1370 -0.0076 -0.0199 -0.0154 427 LYS A N   
3628 C CA  . LYS A 427 ? 0.1269 0.2754 0.1704 -0.0056 -0.0237 -0.0133 427 LYS A CA  
3629 C C   . LYS A 427 ? 0.1226 0.2758 0.1596 0.0014  -0.0190 -0.0073 427 LYS A C   
3630 O O   . LYS A 427 ? 0.1248 0.2870 0.1632 0.0044  -0.0193 0.0002  427 LYS A O   
3631 C CB  . LYS A 427 ? 0.1978 0.3462 0.2312 -0.0087 -0.0308 -0.0224 427 LYS A CB  
3632 C CG  . LYS A 427 ? 0.4022 0.5670 0.4335 -0.0090 -0.0373 -0.0207 427 LYS A CG  
3633 C CD  . LYS A 427 ? 0.5360 0.6998 0.5553 -0.0134 -0.0451 -0.0310 427 LYS A CD  
3634 C CE  . LYS A 427 ? 0.6323 0.7777 0.6499 -0.0204 -0.0468 -0.0405 427 LYS A CE  
3635 N NZ  . LYS A 427 ? 0.6849 0.8246 0.7169 -0.0270 -0.0455 -0.0379 427 LYS A NZ  
3636 N N   . ILE A 428 ? 0.1116 0.2591 0.1415 0.0042  -0.0146 -0.0100 428 ILE A N   
3637 C CA  . ILE A 428 ? 0.1530 0.3057 0.1770 0.0090  -0.0089 -0.0037 428 ILE A CA  
3638 C C   . ILE A 428 ? 0.1474 0.2985 0.1809 0.0088  -0.0040 0.0060  428 ILE A C   
3639 O O   . ILE A 428 ? 0.1313 0.2866 0.1614 0.0115  -0.0022 0.0143  428 ILE A O   
3640 C CB  . ILE A 428 ? 0.1478 0.2976 0.1658 0.0116  -0.0043 -0.0090 428 ILE A CB  
3641 C CG1 . ILE A 428 ? 0.1978 0.3482 0.2023 0.0136  -0.0085 -0.0187 428 ILE A CG1 
3642 C CG2 . ILE A 428 ? 0.1865 0.3424 0.2024 0.0142  0.0035  -0.0013 428 ILE A CG2 
3643 C CD1 . ILE A 428 ? 0.2026 0.3481 0.2026 0.0177  -0.0046 -0.0263 428 ILE A CD1 
3644 N N   . LEU A 429 ? 0.1109 0.2540 0.1546 0.0057  -0.0020 0.0051  429 LEU A N   
3645 C CA  . LEU A 429 ? 0.0925 0.2315 0.1438 0.0049  0.0024  0.0125  429 LEU A CA  
3646 C C   . LEU A 429 ? 0.1172 0.2597 0.1724 0.0067  -0.0002 0.0177  429 LEU A C   
3647 O O   . LEU A 429 ? 0.1257 0.2660 0.1806 0.0094  0.0029  0.0256  429 LEU A O   
3648 C CB  . LEU A 429 ? 0.1011 0.2318 0.1607 0.0011  0.0038  0.0092  429 LEU A CB  
3649 C CG  . LEU A 429 ? 0.1099 0.2346 0.1758 -0.0005 0.0082  0.0147  429 LEU A CG  
3650 C CD1 . LEU A 429 ? 0.1515 0.2754 0.2144 -0.0008 0.0134  0.0188  429 LEU A CD1 
3651 C CD2 . LEU A 429 ? 0.1331 0.2510 0.2056 -0.0045 0.0080  0.0110  429 LEU A CD2 
3652 N N   . ILE A 430 ? 0.1329 0.2808 0.1920 0.0052  -0.0059 0.0136  430 ILE A N   
3653 C CA  . ILE A 430 ? 0.1290 0.2848 0.1942 0.0079  -0.0087 0.0182  430 ILE A CA  
3654 C C   . ILE A 430 ? 0.1408 0.3037 0.1977 0.0140  -0.0105 0.0247  430 ILE A C   
3655 O O   . ILE A 430 ? 0.1266 0.2892 0.1858 0.0192  -0.0091 0.0326  430 ILE A O   
3656 C CB  . ILE A 430 ? 0.1006 0.2647 0.1721 0.0034  -0.0149 0.0122  430 ILE A CB  
3657 C CG1 . ILE A 430 ? 0.0686 0.2252 0.1487 -0.0021 -0.0122 0.0088  430 ILE A CG1 
3658 C CG2 . ILE A 430 ? 0.1463 0.3257 0.2239 0.0073  -0.0192 0.0166  430 ILE A CG2 
3659 C CD1 . ILE A 430 ? 0.1301 0.2899 0.2125 -0.0096 -0.0176 0.0020  430 ILE A CD1 
3660 N N   . GLU A 431 ? 0.1179 0.2860 0.1636 0.0139  -0.0138 0.0214  431 GLU A N   
3661 C CA  . GLU A 431 ? 0.1943 0.3697 0.2291 0.0193  -0.0157 0.0279  431 GLU A CA  
3662 C C   . GLU A 431 ? 0.2092 0.3755 0.2389 0.0221  -0.0083 0.0371  431 GLU A C   
3663 O O   . GLU A 431 ? 0.1815 0.3484 0.2077 0.0275  -0.0087 0.0467  431 GLU A O   
3664 C CB  . GLU A 431 ? 0.2535 0.4349 0.2748 0.0180  -0.0195 0.0210  431 GLU A CB  
3665 C CG  . GLU A 431 ? 0.4349 0.6289 0.4557 0.0168  -0.0292 0.0165  431 GLU A CG  
3666 C CD  . GLU A 431 ? 0.5470 0.7529 0.5663 0.0231  -0.0335 0.0261  431 GLU A CD  
3667 O OE1 . GLU A 431 ? 0.6244 0.8270 0.6350 0.0284  -0.0295 0.0353  431 GLU A OE1 
3668 O OE2 . GLU A 431 ? 0.6248 0.8439 0.6521 0.0226  -0.0411 0.0251  431 GLU A OE2 
3669 N N   . ALA A 432 ? 0.1706 0.3284 0.1998 0.0184  -0.0019 0.0348  432 ALA A N   
3670 C CA  . ALA A 432 ? 0.1698 0.3198 0.1948 0.0184  0.0052  0.0432  432 ALA A CA  
3671 C C   . ALA A 432 ? 0.1239 0.2629 0.1568 0.0197  0.0074  0.0498  432 ALA A C   
3672 O O   . ALA A 432 ? 0.1773 0.3090 0.2044 0.0219  0.0104  0.0595  432 ALA A O   
3673 C CB  . ALA A 432 ? 0.1700 0.3173 0.1961 0.0136  0.0110  0.0383  432 ALA A CB  
3674 N N   . LYS A 433 ? 0.1527 0.2892 0.1976 0.0183  0.0062  0.0446  433 LYS A N   
3675 C CA  . LYS A 433 ? 0.2078 0.3332 0.2594 0.0202  0.0089  0.0490  433 LYS A CA  
3676 C C   . LYS A 433 ? 0.2279 0.3550 0.2773 0.0288  0.0060  0.0572  433 LYS A C   
3677 O O   . LYS A 433 ? 0.1860 0.2994 0.2334 0.0322  0.0095  0.0646  433 LYS A O   
3678 C CB  . LYS A 433 ? 0.2115 0.3373 0.2749 0.0175  0.0081  0.0414  433 LYS A CB  
3679 C CG  . LYS A 433 ? 0.1645 0.2811 0.2346 0.0208  0.0109  0.0441  433 LYS A CG  
3680 C CD  . LYS A 433 ? 0.1560 0.2542 0.2223 0.0179  0.0172  0.0472  433 LYS A CD  
3681 C CE  . LYS A 433 ? 0.2532 0.3396 0.3236 0.0224  0.0200  0.0487  433 LYS A CE  
3682 N NZ  . LYS A 433 ? 0.2146 0.2803 0.2793 0.0184  0.0255  0.0514  433 LYS A NZ  
3683 N N   . LYS A 434 ? 0.1989 0.3422 0.2480 0.0326  -0.0010 0.0562  434 LYS A N   
3684 C CA  . LYS A 434 ? 0.2241 0.3725 0.2712 0.0421  -0.0051 0.0647  434 LYS A CA  
3685 C C   . LYS A 434 ? 0.2640 0.4006 0.2971 0.0454  -0.0021 0.0759  434 LYS A C   
3686 O O   . LYS A 434 ? 0.2961 0.4269 0.3273 0.0541  -0.0031 0.0850  434 LYS A O   
3687 C CB  . LYS A 434 ? 0.2491 0.4192 0.2953 0.0437  -0.0140 0.0617  434 LYS A CB  
3688 C CG  . LYS A 434 ? 0.3476 0.5310 0.4080 0.0402  -0.0182 0.0526  434 LYS A CG  
3689 C CD  . LYS A 434 ? 0.4212 0.6247 0.4786 0.0391  -0.0276 0.0489  434 LYS A CD  
3690 C CE  . LYS A 434 ? 0.4778 0.6935 0.5489 0.0327  -0.0315 0.0398  434 LYS A CE  
3691 N NZ  . LYS A 434 ? 0.5012 0.7311 0.5670 0.0289  -0.0404 0.0345  434 LYS A NZ  
3692 N N   . LYS A 435 ? 0.2181 0.3514 0.2410 0.0390  0.0018  0.0758  435 LYS A N   
3693 C CA  . LYS A 435 ? 0.2854 0.4105 0.2933 0.0400  0.0050  0.0868  435 LYS A CA  
3694 C C   . LYS A 435 ? 0.2706 0.3789 0.2773 0.0322  0.0138  0.0887  435 LYS A C   
3695 O O   . LYS A 435 ? 0.2849 0.3881 0.2794 0.0294  0.0180  0.0968  435 LYS A O   
3696 C CB  . LYS A 435 ? 0.3204 0.4610 0.3156 0.0389  0.0022  0.0856  435 LYS A CB  
3697 C CG  . LYS A 435 ? 0.3727 0.5306 0.3668 0.0454  -0.0077 0.0841  435 LYS A CG  
3698 C CD  . LYS A 435 ? 0.5019 0.6742 0.4834 0.0427  -0.0106 0.0785  435 LYS A CD  
3699 C CE  . LYS A 435 ? 0.5807 0.7584 0.5705 0.0363  -0.0112 0.0635  435 LYS A CE  
3700 N NZ  . LYS A 435 ? 0.6628 0.8498 0.6656 0.0372  -0.0191 0.0571  435 LYS A NZ  
3701 N N   . ALA A 436 ? 0.1927 0.3296 0.2724 0.0812  -0.0012 0.1015  436 ALA A N   
3702 C CA  . ALA A 436 ? 0.2212 0.3303 0.2928 0.0738  0.0079  0.1017  436 ALA A CA  
3703 C C   . ALA A 436 ? 0.2412 0.3159 0.3117 0.0826  0.0170  0.1149  436 ALA A C   
3704 O O   . ALA A 436 ? 0.2461 0.3151 0.3298 0.0984  0.0194  0.1207  436 ALA A O   
3705 C CB  . ALA A 436 ? 0.2185 0.3207 0.2959 0.0632  0.0134  0.0832  436 ALA A CB  
3706 N N   . LYS A 437 ? 0.2134 0.2649 0.2700 0.0724  0.0224  0.1200  437 LYS A N   
3707 C CA  . LYS A 437 ? 0.3131 0.3269 0.3683 0.0773  0.0311  0.1338  437 LYS A CA  
3708 C C   . LYS A 437 ? 0.3050 0.2852 0.3575 0.0607  0.0408  0.1227  437 LYS A C   
3709 O O   . LYS A 437 ? 0.3664 0.3091 0.4197 0.0617  0.0488  0.1307  437 LYS A O   
3710 C CB  . LYS A 437 ? 0.3797 0.3974 0.4211 0.0801  0.0286  0.1556  437 LYS A CB  
3711 C CG  . LYS A 437 ? 0.4740 0.5228 0.5150 0.0930  0.0177  0.1598  437 LYS A CG  
3712 C CD  . LYS A 437 ? 0.5821 0.6136 0.6341 0.1093  0.0194  0.1668  437 LYS A CD  
3713 C CE  . LYS A 437 ? 0.6558 0.7228 0.7160 0.1207  0.0082  0.1641  437 LYS A CE  
3714 N NZ  . LYS A 437 ? 0.6887 0.7835 0.7338 0.1200  -0.0021 0.1712  437 LYS A NZ  
3715 N N   . ASN A 438 ? 0.2255 0.2173 0.2760 0.0456  0.0396  0.1045  438 ASN A N   
3716 C CA  . ASN A 438 ? 0.2879 0.2551 0.3361 0.0287  0.0459  0.0937  438 ASN A CA  
3717 C C   . ASN A 438 ? 0.3136 0.2971 0.3620 0.0199  0.0427  0.0728  438 ASN A C   
3718 O O   . ASN A 438 ? 0.2365 0.2473 0.2870 0.0251  0.0366  0.0685  438 ASN A O   
3719 C CB  . ASN A 438 ? 0.2599 0.2259 0.3009 0.0159  0.0481  0.1052  438 ASN A CB  
3720 C CG  . ASN A 438 ? 0.2887 0.2933 0.3233 0.0114  0.0415  0.1039  438 ASN A CG  
3721 O OD1 . ASN A 438 ? 0.2407 0.2621 0.2766 0.0059  0.0371  0.0877  438 ASN A OD1 
3722 N ND2 . ASN A 438 ? 0.2641 0.2823 0.2899 0.0157  0.0408  0.1213  438 ASN A ND2 
3723 N N   . ASP A 439 ? 0.2702 0.2365 0.3166 0.0057  0.0461  0.0607  439 ASP A N   
3724 C CA  . ASP A 439 ? 0.3127 0.2900 0.3570 -0.0009 0.0433  0.0424  439 ASP A CA  
3725 C C   . ASP A 439 ? 0.2505 0.2587 0.2923 -0.0079 0.0358  0.0404  439 ASP A C   
3726 O O   . ASP A 439 ? 0.2188 0.2365 0.2582 -0.0125 0.0326  0.0284  439 ASP A O   
3727 C CB  . ASP A 439 ? 0.3320 0.2835 0.3732 -0.0134 0.0472  0.0288  439 ASP A CB  
3728 C CG  . ASP A 439 ? 0.4409 0.3615 0.4825 -0.0043 0.0547  0.0223  439 ASP A CG  
3729 O OD1 . ASP A 439 ? 0.4373 0.3637 0.4834 0.0127  0.0567  0.0267  439 ASP A OD1 
3730 O OD2 . ASP A 439 ? 0.4661 0.3582 0.5045 -0.0140 0.0583  0.0111  439 ASP A OD2 
3731 N N   . TYR A 440 ? 0.1793 0.2033 0.2203 -0.0075 0.0334  0.0518  440 TYR A N   
3732 C CA  . TYR A 440 ? 0.1380 0.1895 0.1770 -0.0103 0.0268  0.0471  440 TYR A CA  
3733 C C   . TYR A 440 ? 0.1787 0.2442 0.2194 -0.0022 0.0215  0.0418  440 TYR A C   
3734 O O   . TYR A 440 ? 0.1526 0.2322 0.1926 -0.0054 0.0165  0.0344  440 TYR A O   
3735 C CB  . TYR A 440 ? 0.1371 0.2044 0.1723 -0.0102 0.0265  0.0581  440 TYR A CB  
3736 C CG  . TYR A 440 ? 0.2113 0.2785 0.2482 -0.0231 0.0310  0.0590  440 TYR A CG  
3737 C CD1 . TYR A 440 ? 0.2225 0.3050 0.2628 -0.0304 0.0276  0.0477  440 TYR A CD1 
3738 C CD2 . TYR A 440 ? 0.3003 0.3529 0.3377 -0.0285 0.0385  0.0720  440 TYR A CD2 
3739 C CE1 . TYR A 440 ? 0.2590 0.3484 0.3058 -0.0424 0.0311  0.0481  440 TYR A CE1 
3740 C CE2 . TYR A 440 ? 0.3082 0.3647 0.3515 -0.0432 0.0432  0.0729  440 TYR A CE2 
3741 C CZ  . TYR A 440 ? 0.3079 0.3857 0.3571 -0.0500 0.0391  0.0600  440 TYR A CZ  
3742 O OH  . TYR A 440 ? 0.3191 0.4082 0.3787 -0.0642 0.0429  0.0600  440 TYR A OH  
3743 N N   . ILE A 441 ? 0.1217 0.1833 0.1671 0.0081  0.0229  0.0457  441 ILE A N   
3744 C CA  . ILE A 441 ? 0.1184 0.1959 0.1697 0.0126  0.0191  0.0405  441 ILE A CA  
3745 C C   . ILE A 441 ? 0.1724 0.2439 0.2218 0.0061  0.0215  0.0290  441 ILE A C   
3746 O O   . ILE A 441 ? 0.1277 0.2122 0.1790 0.0040  0.0178  0.0247  441 ILE A O   
3747 C CB  . ILE A 441 ? 0.0991 0.1799 0.1603 0.0257  0.0205  0.0474  441 ILE A CB  
3748 C CG1 . ILE A 441 ? 0.1551 0.2618 0.2261 0.0278  0.0144  0.0443  441 ILE A CG1 
3749 C CG2 . ILE A 441 ? 0.1204 0.1787 0.1845 0.0303  0.0300  0.0439  441 ILE A CG2 
3750 C CD1 . ILE A 441 ? 0.1280 0.2550 0.1958 0.0255  0.0042  0.0457  441 ILE A CD1 
3751 N N   . LEU A 442 ? 0.1245 0.1755 0.1688 0.0018  0.0272  0.0239  442 LEU A N   
3752 C CA  . LEU A 442 ? 0.1275 0.1753 0.1650 -0.0043 0.0283  0.0129  442 LEU A CA  
3753 C C   . LEU A 442 ? 0.1341 0.1930 0.1670 -0.0130 0.0212  0.0103  442 LEU A C   
3754 O O   . LEU A 442 ? 0.1362 0.2019 0.1650 -0.0150 0.0189  0.0063  442 LEU A O   
3755 C CB  . LEU A 442 ? 0.1470 0.1704 0.1781 -0.0076 0.0345  0.0052  442 LEU A CB  
3756 C CG  . LEU A 442 ? 0.1840 0.1904 0.2200 0.0035  0.0429  0.0065  442 LEU A CG  
3757 C CD1 . LEU A 442 ? 0.1749 0.1525 0.2025 -0.0016 0.0485  -0.0055 442 LEU A CD1 
3758 C CD2 . LEU A 442 ? 0.1931 0.2145 0.2350 0.0141  0.0466  0.0060  442 LEU A CD2 
3759 N N   . VAL A 443 ? 0.1327 0.1940 0.1668 -0.0174 0.0186  0.0136  443 VAL A N   
3760 C CA  . VAL A 443 ? 0.0731 0.1484 0.1065 -0.0225 0.0124  0.0113  443 VAL A CA  
3761 C C   . VAL A 443 ? 0.1307 0.2189 0.1658 -0.0173 0.0075  0.0122  443 VAL A C   
3762 O O   . VAL A 443 ? 0.1020 0.1948 0.1350 -0.0190 0.0031  0.0088  443 VAL A O   
3763 C CB  . VAL A 443 ? 0.0950 0.1762 0.1321 -0.0264 0.0128  0.0160  443 VAL A CB  
3764 C CG1 . VAL A 443 ? 0.1340 0.2335 0.1735 -0.0289 0.0073  0.0125  443 VAL A CG1 
3765 C CG2 . VAL A 443 ? 0.1108 0.1756 0.1489 -0.0346 0.0180  0.0157  443 VAL A CG2 
3766 N N   . ALA A 444 ? 0.1282 0.2217 0.1675 -0.0112 0.0074  0.0170  444 ALA A N   
3767 C CA  . ALA A 444 ? 0.1551 0.2595 0.1977 -0.0087 0.0019  0.0157  444 ALA A CA  
3768 C C   . ALA A 444 ? 0.1460 0.2483 0.1914 -0.0098 0.0027  0.0141  444 ALA A C   
3769 O O   . ALA A 444 ? 0.1159 0.2231 0.1649 -0.0109 -0.0018 0.0126  444 ALA A O   
3770 C CB  . ALA A 444 ? 0.1136 0.2283 0.1594 -0.0030 -0.0004 0.0200  444 ALA A CB  
3771 N N   . GLU A 445 ? 0.0901 0.1846 0.1335 -0.0098 0.0092  0.0139  445 GLU A N   
3772 C CA  . GLU A 445 ? 0.0934 0.1889 0.1375 -0.0112 0.0126  0.0134  445 GLU A CA  
3773 C C   . GLU A 445 ? 0.0960 0.1864 0.1288 -0.0164 0.0107  0.0115  445 GLU A C   
3774 O O   . GLU A 445 ? 0.1270 0.2180 0.1569 -0.0183 0.0141  0.0134  445 GLU A O   
3775 C CB  . GLU A 445 ? 0.1158 0.2072 0.1610 -0.0066 0.0219  0.0127  445 GLU A CB  
3776 C CG  . GLU A 445 ? 0.1061 0.2064 0.1656 0.0015  0.0226  0.0174  445 GLU A CG  
3777 C CD  . GLU A 445 ? 0.1864 0.2784 0.2484 0.0100  0.0317  0.0170  445 GLU A CD  
3778 O OE1 . GLU A 445 ? 0.1464 0.2238 0.1975 0.0088  0.0384  0.0104  445 GLU A OE1 
3779 O OE2 . GLU A 445 ? 0.1469 0.2471 0.2214 0.0190  0.0314  0.0229  445 GLU A OE2 
3780 N N   . GLY A 446 ? 0.0908 0.1791 0.1183 -0.0182 0.0055  0.0093  446 GLY A N   
3781 C CA  . GLY A 446 ? 0.1460 0.2330 0.1639 -0.0210 0.0015  0.0090  446 GLY A CA  
3782 C C   . GLY A 446 ? 0.1275 0.2146 0.1482 -0.0206 -0.0020 0.0140  446 GLY A C   
3783 O O   . GLY A 446 ? 0.1137 0.2025 0.1447 -0.0192 -0.0047 0.0142  446 GLY A O   
3784 N N   . SER A 447 ? 0.0990 0.1826 0.1088 -0.0222 -0.0020 0.0180  447 SER A N   
3785 C CA  . SER A 447 ? 0.1521 0.2302 0.1642 -0.0229 -0.0040 0.0255  447 SER A CA  
3786 C C   . SER A 447 ? 0.1330 0.2074 0.1515 -0.0187 -0.0128 0.0249  447 SER A C   
3787 O O   . SER A 447 ? 0.1313 0.1971 0.1576 -0.0192 -0.0147 0.0274  447 SER A O   
3788 C CB  . SER A 447 ? 0.1121 0.1871 0.1074 -0.0247 -0.0018 0.0332  447 SER A CB  
3789 O OG  . SER A 447 ? 0.1441 0.2213 0.1280 -0.0215 -0.0097 0.0328  447 SER A OG  
3790 N N   . ASP A 448 ? 0.1047 0.1860 0.1220 -0.0149 -0.0176 0.0203  448 ASP A N   
3791 C CA  . ASP A 448 ? 0.1168 0.1978 0.1400 -0.0081 -0.0248 0.0197  448 ASP A CA  
3792 C C   . ASP A 448 ? 0.0766 0.1539 0.1109 -0.0059 -0.0251 0.0142  448 ASP A C   
3793 O O   . ASP A 448 ? 0.1311 0.1981 0.1696 -0.0009 -0.0293 0.0140  448 ASP A O   
3794 C CB  . ASP A 448 ? 0.1089 0.2056 0.1336 -0.0055 -0.0283 0.0154  448 ASP A CB  
3795 C CG  . ASP A 448 ? 0.0971 0.1996 0.1099 -0.0093 -0.0302 0.0174  448 ASP A CG  
3796 O OD1 . ASP A 448 ? 0.1421 0.2444 0.1484 -0.0161 -0.0249 0.0138  448 ASP A OD1 
3797 O OD2 . ASP A 448 ? 0.1319 0.2378 0.1406 -0.0046 -0.0374 0.0225  448 ASP A OD2 
3798 N N   . TRP A 449 ? 0.0805 0.1649 0.1185 -0.0087 -0.0214 0.0094  449 TRP A N   
3799 C CA  . TRP A 449 ? 0.0721 0.1572 0.1169 -0.0064 -0.0233 0.0027  449 TRP A CA  
3800 C C   . TRP A 449 ? 0.1110 0.1820 0.1608 -0.0101 -0.0255 0.0030  449 TRP A C   
3801 O O   . TRP A 449 ? 0.1378 0.2015 0.1916 -0.0071 -0.0298 -0.0043 449 TRP A O   
3802 C CB  . TRP A 449 ? 0.0960 0.1930 0.1416 -0.0081 -0.0198 0.0007  449 TRP A CB  
3803 C CG  . TRP A 449 ? 0.1121 0.2166 0.1537 -0.0085 -0.0159 0.0030  449 TRP A CG  
3804 C CD1 . TRP A 449 ? 0.1187 0.2222 0.1580 -0.0121 -0.0109 0.0064  449 TRP A CD1 
3805 C CD2 . TRP A 449 ? 0.0840 0.1969 0.1254 -0.0059 -0.0163 0.0013  449 TRP A CD2 
3806 N NE1 . TRP A 449 ? 0.0996 0.2068 0.1366 -0.0137 -0.0088 0.0063  449 TRP A NE1 
3807 C CE2 . TRP A 449 ? 0.0627 0.1770 0.1016 -0.0108 -0.0119 0.0038  449 TRP A CE2 
3808 C CE3 . TRP A 449 ? 0.1048 0.2235 0.1491 0.0004  -0.0189 -0.0028 449 TRP A CE3 
3809 C CZ2 . TRP A 449 ? 0.0587 0.1796 0.0987 -0.0124 -0.0107 0.0031  449 TRP A CZ2 
3810 C CZ3 . TRP A 449 ? 0.0928 0.2200 0.1380 0.0006  -0.0163 -0.0027 449 TRP A CZ3 
3811 C CH2 . TRP A 449 ? 0.1026 0.2308 0.1460 -0.0069 -0.0126 0.0005  449 TRP A CH2 
3812 N N   . PHE A 450 ? 0.0958 0.1626 0.1459 -0.0171 -0.0217 0.0106  450 PHE A N   
3813 C CA  . PHE A 450 ? 0.1538 0.2096 0.2122 -0.0244 -0.0221 0.0128  450 PHE A CA  
3814 C C   . PHE A 450 ? 0.1739 0.2081 0.2300 -0.0232 -0.0247 0.0188  450 PHE A C   
3815 O O   . PHE A 450 ? 0.1473 0.1654 0.2119 -0.0284 -0.0271 0.0180  450 PHE A O   
3816 C CB  . PHE A 450 ? 0.1188 0.1834 0.1804 -0.0319 -0.0146 0.0199  450 PHE A CB  
3817 C CG  . PHE A 450 ? 0.1040 0.1873 0.1697 -0.0303 -0.0123 0.0155  450 PHE A CG  
3818 C CD1 . PHE A 450 ? 0.1094 0.2035 0.1883 -0.0333 -0.0155 0.0104  450 PHE A CD1 
3819 C CD2 . PHE A 450 ? 0.1024 0.1917 0.1587 -0.0254 -0.0081 0.0163  450 PHE A CD2 
3820 C CE1 . PHE A 450 ? 0.1023 0.2137 0.1843 -0.0291 -0.0144 0.0090  450 PHE A CE1 
3821 C CE2 . PHE A 450 ? 0.0992 0.2004 0.1592 -0.0224 -0.0057 0.0142  450 PHE A CE2 
3822 C CZ  . PHE A 450 ? 0.1053 0.2179 0.1778 -0.0230 -0.0089 0.0119  450 PHE A CZ  
3823 N N   . TRP A 451 ? 0.1396 0.1728 0.1848 -0.0167 -0.0252 0.0254  451 TRP A N   
3824 C CA  . TRP A 451 ? 0.1385 0.1523 0.1803 -0.0121 -0.0289 0.0340  451 TRP A CA  
3825 C C   . TRP A 451 ? 0.1588 0.1595 0.2086 -0.0035 -0.0351 0.0243  451 TRP A C   
3826 O O   . TRP A 451 ? 0.2008 0.1757 0.2555 -0.0040 -0.0373 0.0269  451 TRP A O   
3827 C CB  . TRP A 451 ? 0.1729 0.1968 0.2013 -0.0056 -0.0304 0.0414  451 TRP A CB  
3828 C CG  . TRP A 451 ? 0.2010 0.2110 0.2249 0.0033  -0.0362 0.0515  451 TRP A CG  
3829 C CD1 . TRP A 451 ? 0.1873 0.1976 0.2167 0.0168  -0.0433 0.0476  451 TRP A CD1 
3830 C CD2 . TRP A 451 ? 0.2836 0.2795 0.2963 0.0013  -0.0353 0.0692  451 TRP A CD2 
3831 N NE1 . TRP A 451 ? 0.3096 0.3054 0.3333 0.0247  -0.0482 0.0621  451 TRP A NE1 
3832 C CE2 . TRP A 451 ? 0.3480 0.3337 0.3597 0.0149  -0.0436 0.0766  451 TRP A CE2 
3833 C CE3 . TRP A 451 ? 0.2701 0.2629 0.2737 -0.0098 -0.0274 0.0808  451 TRP A CE3 
3834 C CZ2 . TRP A 451 ? 0.3809 0.3506 0.3805 0.0178  -0.0453 0.0968  451 TRP A CZ2 
3835 C CZ3 . TRP A 451 ? 0.3355 0.3138 0.3260 -0.0086 -0.0276 0.1004  451 TRP A CZ3 
3836 C CH2 . TRP A 451 ? 0.3691 0.3346 0.3567 0.0052  -0.0371 0.1092  451 TRP A CH2 
3837 N N   . TRP A 452 ? 0.1335 0.1507 0.1846 0.0044  -0.0369 0.0128  452 TRP A N   
3838 C CA  . TRP A 452 ? 0.2196 0.2287 0.2763 0.0155  -0.0410 0.0018  452 TRP A CA  
3839 C C   . TRP A 452 ? 0.2784 0.2777 0.3407 0.0103  -0.0420 -0.0120 452 TRP A C   
3840 O O   . TRP A 452 ? 0.2252 0.2074 0.2910 0.0180  -0.0453 -0.0222 452 TRP A O   
3841 C CB  . TRP A 452 ? 0.1918 0.2270 0.2482 0.0251  -0.0407 -0.0046 452 TRP A CB  
3842 C CG  . TRP A 452 ? 0.2141 0.2608 0.2675 0.0295  -0.0424 0.0064  452 TRP A CG  
3843 C CD1 . TRP A 452 ? 0.1827 0.2509 0.2315 0.0238  -0.0403 0.0096  452 TRP A CD1 
3844 C CD2 . TRP A 452 ? 0.1453 0.1821 0.1996 0.0401  -0.0478 0.0153  452 TRP A CD2 
3845 N NE1 . TRP A 452 ? 0.1790 0.2544 0.2253 0.0287  -0.0450 0.0180  452 TRP A NE1 
3846 C CE2 . TRP A 452 ? 0.1573 0.2157 0.2068 0.0397  -0.0500 0.0231  452 TRP A CE2 
3847 C CE3 . TRP A 452 ? 0.2186 0.2290 0.2774 0.0504  -0.0515 0.0178  452 TRP A CE3 
3848 C CZ2 . TRP A 452 ? 0.2210 0.2807 0.2692 0.0498  -0.0571 0.0339  452 TRP A CZ2 
3849 C CZ3 . TRP A 452 ? 0.2103 0.2183 0.2687 0.0622  -0.0574 0.0306  452 TRP A CZ3 
3850 C CH2 . TRP A 452 ? 0.2203 0.2556 0.2730 0.0620  -0.0608 0.0389  452 TRP A CH2 
3851 N N   . GLN A 453 ? 0.2396 0.2499 0.3032 -0.0018 -0.0399 -0.0133 453 GLN A N   
3852 C CA  . GLN A 453 ? 0.2372 0.2444 0.3062 -0.0081 -0.0432 -0.0269 453 GLN A CA  
3853 C C   . GLN A 453 ? 0.3093 0.2854 0.3872 -0.0165 -0.0461 -0.0266 453 GLN A C   
3854 O O   . GLN A 453 ? 0.2746 0.2399 0.3557 -0.0244 -0.0429 -0.0114 453 GLN A O   
3855 C CB  . GLN A 453 ? 0.2002 0.2317 0.2708 -0.0171 -0.0412 -0.0256 453 GLN A CB  
3856 C CG  . GLN A 453 ? 0.2883 0.3260 0.3654 -0.0251 -0.0467 -0.0381 453 GLN A CG  
3857 C CD  . GLN A 453 ? 0.3309 0.3719 0.4002 -0.0171 -0.0518 -0.0564 453 GLN A CD  
3858 O OE1 . GLN A 453 ? 0.3759 0.4177 0.4364 -0.0045 -0.0496 -0.0596 453 GLN A OE1 
3859 N NE2 . GLN A 453 ? 0.3348 0.3833 0.4071 -0.0245 -0.0586 -0.0686 453 GLN A NE2 
3860 N N   . GLY A 454 ? 0.3388 0.2991 0.4195 -0.0151 -0.0514 -0.0438 454 GLY A N   
3861 C CA  . GLY A 454 ? 0.4445 0.3713 0.5356 -0.0258 -0.0546 -0.0463 454 GLY A CA  
3862 C C   . GLY A 454 ? 0.4848 0.3776 0.5772 -0.0210 -0.0528 -0.0317 454 GLY A C   
3863 O O   . GLY A 454 ? 0.4858 0.3596 0.5860 -0.0348 -0.0509 -0.0187 454 GLY A O   
3864 N N   . GLU A 455 ? 0.4432 0.3300 0.5288 -0.0014 -0.0532 -0.0322 455 GLU A N   
3865 C CA  . GLU A 455 ? 0.5586 0.4165 0.6440 0.0085  -0.0531 -0.0167 455 GLU A CA  
3866 C C   . GLU A 455 ? 0.6844 0.5184 0.7719 0.0271  -0.0566 -0.0318 455 GLU A C   
3867 O O   . GLU A 455 ? 0.6631 0.5158 0.7477 0.0372  -0.0571 -0.0514 455 GLU A O   
3868 C CB  . GLU A 455 ? 0.5042 0.3870 0.5808 0.0174  -0.0507 0.0014  455 GLU A CB  
3869 C CG  . GLU A 455 ? 0.4862 0.3887 0.5581 0.0023  -0.0458 0.0166  455 GLU A CG  
3870 C CD  . GLU A 455 ? 0.5711 0.4464 0.6451 -0.0100 -0.0430 0.0347  455 GLU A CD  
3871 O OE1 . GLU A 455 ? 0.6260 0.4655 0.7023 -0.0038 -0.0456 0.0414  455 GLU A OE1 
3872 O OE2 . GLU A 455 ? 0.5529 0.4423 0.6268 -0.0251 -0.0373 0.0433  455 GLU A OE2 
3873 N N   . GLU A 456 ? 0.8062 0.5976 0.8983 0.0325  -0.0581 -0.0221 456 GLU A N   
3874 C CA  . GLU A 456 ? 0.8971 0.6608 0.9928 0.0538  -0.0608 -0.0351 456 GLU A CA  
3875 C C   . GLU A 456 ? 0.8850 0.6845 0.9775 0.0770  -0.0600 -0.0363 456 GLU A C   
3876 O O   . GLU A 456 ? 0.8724 0.6929 0.9618 0.0814  -0.0600 -0.0156 456 GLU A O   
3877 C CB  . GLU A 456 ? 1.0145 0.7253 1.1158 0.0578  -0.0623 -0.0181 456 GLU A CB  
3878 C CG  . GLU A 456 ? 1.0808 0.7937 1.1790 0.0806  -0.0631 0.0039  456 GLU A CG  
3879 C CD  . GLU A 456 ? 1.1599 0.8305 1.2537 0.0814  -0.0596 0.0251  456 GLU A CD  
3880 O OE1 . GLU A 456 ? 1.1976 0.8303 1.2926 0.0669  -0.0561 0.0202  456 GLU A OE1 
3881 O OE2 . GLU A 456 ? 1.1790 0.8567 1.2668 0.0969  -0.0604 0.0467  456 GLU A OE2 
3882 N N   . LYS A 457 ? 0.9150 0.7275 1.0074 0.0890  -0.0589 -0.0613 457 LYS A N   
3883 C CA  . LYS A 457 ? 0.9234 0.7619 1.0186 0.1144  -0.0570 -0.0658 457 LYS A CA  
3884 C C   . LYS A 457 ? 0.8850 0.7706 0.9790 0.1150  -0.0560 -0.0477 457 LYS A C   
3885 O O   . LYS A 457 ? 0.9111 0.8170 1.0123 0.1348  -0.0562 -0.0438 457 LYS A O   
3886 C CB  . LYS A 457 ? 0.9330 0.7367 1.0358 0.1353  -0.0580 -0.0608 457 LYS A CB  
3887 C CG  . LYS A 457 ? 0.9464 0.7284 1.0471 0.1426  -0.0530 -0.0850 457 LYS A CG  
3888 C CD  . LYS A 457 ? 0.9293 0.6780 1.0247 0.1206  -0.0549 -0.0997 457 LYS A CD  
3889 C CE  . LYS A 457 ? 0.9595 0.6871 1.0497 0.1279  -0.0505 -0.1245 457 LYS A CE  
3890 N NZ  . LYS A 457 ? 1.0190 0.7061 1.1142 0.1429  -0.0472 -0.1150 457 LYS A NZ  
3891 N N   . ALA A 458 ? 0.7490 0.6529 0.8357 0.0940  -0.0553 -0.0375 458 ALA A N   
3892 C CA  . ALA A 458 ? 0.6053 0.5478 0.6896 0.0924  -0.0548 -0.0226 458 ALA A CA  
3893 C C   . ALA A 458 ? 0.5686 0.5514 0.6579 0.1054  -0.0516 -0.0335 458 ALA A C   
3894 O O   . ALA A 458 ? 0.4872 0.4831 0.5736 0.1032  -0.0470 -0.0508 458 ALA A O   
3895 C CB  . ALA A 458 ? 0.5856 0.5408 0.6613 0.0693  -0.0524 -0.0170 458 ALA A CB  
3896 N N   . PRO A 459 ? 0.5736 0.5795 0.6707 0.1184  -0.0540 -0.0233 459 PRO A N   
3897 C CA  . PRO A 459 ? 0.4835 0.5281 0.5912 0.1322  -0.0500 -0.0335 459 PRO A CA  
3898 C C   . PRO A 459 ? 0.3984 0.4784 0.5009 0.1169  -0.0439 -0.0379 459 PRO A C   
3899 O O   . PRO A 459 ? 0.3337 0.4225 0.4297 0.1006  -0.0452 -0.0269 459 PRO A O   
3900 C CB  . PRO A 459 ? 0.4125 0.4739 0.5289 0.1407  -0.0542 -0.0166 459 PRO A CB  
3901 C CG  . PRO A 459 ? 0.5142 0.5362 0.6263 0.1445  -0.0624 -0.0019 459 PRO A CG  
3902 C CD  . PRO A 459 ? 0.5594 0.5580 0.6570 0.1227  -0.0610 -0.0018 459 PRO A CD  
3903 N N   . PHE A 460 ? 0.3544 0.4535 0.4586 0.1231  -0.0364 -0.0538 460 PHE A N   
3904 C CA  . PHE A 460 ? 0.3205 0.4506 0.4184 0.1097  -0.0291 -0.0561 460 PHE A CA  
3905 C C   . PHE A 460 ? 0.3511 0.4663 0.4347 0.0908  -0.0302 -0.0543 460 PHE A C   
3906 O O   . PHE A 460 ? 0.2606 0.3961 0.3398 0.0781  -0.0268 -0.0488 460 PHE A O   
3907 C CB  . PHE A 460 ? 0.3525 0.5113 0.4555 0.1002  -0.0269 -0.0421 460 PHE A CB  
3908 C CG  . PHE A 460 ? 0.3376 0.5139 0.4533 0.1116  -0.0237 -0.0420 460 PHE A CG  
3909 C CD1 . PHE A 460 ? 0.4098 0.6008 0.5260 0.1189  -0.0145 -0.0533 460 PHE A CD1 
3910 C CD2 . PHE A 460 ? 0.3668 0.5479 0.4939 0.1148  -0.0302 -0.0302 460 PHE A CD2 
3911 C CE1 . PHE A 460 ? 0.4334 0.6437 0.5643 0.1298  -0.0110 -0.0531 460 PHE A CE1 
3912 C CE2 . PHE A 460 ? 0.3849 0.5862 0.5278 0.1259  -0.0281 -0.0300 460 PHE A CE2 
3913 C CZ  . PHE A 460 ? 0.4093 0.6255 0.5556 0.1336  -0.0180 -0.0415 460 PHE A CZ  
3914 N N   . VAL A 461 ? 0.2997 0.3786 0.3769 0.0875  -0.0346 -0.0582 461 VAL A N   
3915 C CA  . VAL A 461 ? 0.3125 0.3818 0.3792 0.0693  -0.0355 -0.0565 461 VAL A CA  
3916 C C   . VAL A 461 ? 0.2979 0.3898 0.3556 0.0657  -0.0304 -0.0666 461 VAL A C   
3917 O O   . VAL A 461 ? 0.2988 0.3982 0.3501 0.0526  -0.0298 -0.0608 461 VAL A O   
3918 C CB  . VAL A 461 ? 0.3391 0.3691 0.4047 0.0650  -0.0409 -0.0607 461 VAL A CB  
3919 C CG1 . VAL A 461 ? 0.4150 0.4320 0.4777 0.0739  -0.0410 -0.0828 461 VAL A CG1 
3920 C CG2 . VAL A 461 ? 0.3780 0.4042 0.4389 0.0456  -0.0421 -0.0543 461 VAL A CG2 
3921 N N   . GLU A 462 ? 0.1895 0.2936 0.2455 0.0787  -0.0259 -0.0808 462 GLU A N   
3922 C CA  . GLU A 462 ? 0.2817 0.4110 0.3256 0.0762  -0.0200 -0.0875 462 GLU A CA  
3923 C C   . GLU A 462 ? 0.2390 0.3969 0.2849 0.0681  -0.0144 -0.0718 462 GLU A C   
3924 O O   . GLU A 462 ? 0.1909 0.3608 0.2258 0.0598  -0.0117 -0.0687 462 GLU A O   
3925 C CB  . GLU A 462 ? 0.4912 0.6328 0.5323 0.0933  -0.0138 -0.1046 462 GLU A CB  
3926 C CG  . GLU A 462 ? 0.7012 0.8375 0.7237 0.0939  -0.0147 -0.1238 462 GLU A CG  
3927 C CD  . GLU A 462 ? 0.8822 1.0169 0.9032 0.1098  -0.0101 -0.1388 462 GLU A CD  
3928 O OE1 . GLU A 462 ? 0.9509 1.0536 0.9794 0.1178  -0.0148 -0.1480 462 GLU A OE1 
3929 O OE2 . GLU A 462 ? 0.9181 1.0807 0.9324 0.1125  -0.0015 -0.1366 462 GLU A OE2 
3930 N N   . VAL A 463 ? 0.1324 0.3008 0.1927 0.0702  -0.0135 -0.0616 463 VAL A N   
3931 C CA  . VAL A 463 ? 0.1208 0.3093 0.1824 0.0590  -0.0086 -0.0482 463 VAL A CA  
3932 C C   . VAL A 463 ? 0.1587 0.3347 0.2175 0.0451  -0.0128 -0.0378 463 VAL A C   
3933 O O   . VAL A 463 ? 0.1335 0.3141 0.1846 0.0347  -0.0085 -0.0308 463 VAL A O   
3934 C CB  . VAL A 463 ? 0.1328 0.3298 0.2057 0.0609  -0.0073 -0.0414 463 VAL A CB  
3935 C CG1 . VAL A 463 ? 0.1351 0.3430 0.2073 0.0461  -0.0028 -0.0299 463 VAL A CG1 
3936 C CG2 . VAL A 463 ? 0.1462 0.3562 0.2231 0.0749  -0.0023 -0.0506 463 VAL A CG2 
3937 N N   . PHE A 464 ? 0.1135 0.2666 0.1747 0.0439  -0.0203 -0.0351 464 PHE A N   
3938 C CA  . PHE A 464 ? 0.0892 0.2286 0.1452 0.0312  -0.0225 -0.0265 464 PHE A CA  
3939 C C   . PHE A 464 ? 0.1142 0.2500 0.1609 0.0258  -0.0215 -0.0298 464 PHE A C   
3940 O O   . PHE A 464 ? 0.1151 0.2528 0.1586 0.0173  -0.0196 -0.0225 464 PHE A O   
3941 C CB  . PHE A 464 ? 0.0990 0.2146 0.1566 0.0312  -0.0288 -0.0226 464 PHE A CB  
3942 C CG  . PHE A 464 ? 0.0946 0.2163 0.1581 0.0348  -0.0319 -0.0150 464 PHE A CG  
3943 C CD1 . PHE A 464 ? 0.1213 0.2494 0.1821 0.0254  -0.0321 -0.0067 464 PHE A CD1 
3944 C CD2 . PHE A 464 ? 0.1266 0.2493 0.1984 0.0487  -0.0352 -0.0173 464 PHE A CD2 
3945 C CE1 . PHE A 464 ? 0.1038 0.2390 0.1673 0.0277  -0.0366 -0.0010 464 PHE A CE1 
3946 C CE2 . PHE A 464 ? 0.1324 0.2655 0.2105 0.0533  -0.0403 -0.0092 464 PHE A CE2 
3947 C CZ  . PHE A 464 ? 0.0893 0.2284 0.1617 0.0412  -0.0412 -0.0012 464 PHE A CZ  
3948 N N   . ASP A 465 ? 0.1252 0.2559 0.1677 0.0316  -0.0236 -0.0417 465 ASP A N   
3949 C CA  . ASP A 465 ? 0.1476 0.2797 0.1811 0.0269  -0.0252 -0.0461 465 ASP A CA  
3950 C C   . ASP A 465 ? 0.1538 0.3096 0.1789 0.0267  -0.0191 -0.0413 465 ASP A C   
3951 O O   . ASP A 465 ? 0.1520 0.3112 0.1723 0.0208  -0.0196 -0.0345 465 ASP A O   
3952 C CB  . ASP A 465 ? 0.1141 0.2360 0.1433 0.0326  -0.0299 -0.0632 465 ASP A CB  
3953 C CG  . ASP A 465 ? 0.2261 0.3552 0.2449 0.0278  -0.0340 -0.0699 465 ASP A CG  
3954 O OD1 . ASP A 465 ? 0.1924 0.3136 0.2162 0.0181  -0.0396 -0.0667 465 ASP A OD1 
3955 O OD2 . ASP A 465 ? 0.1740 0.3203 0.1797 0.0341  -0.0317 -0.0781 465 ASP A OD2 
3956 N N   . LYS A 466 ? 0.1308 0.3040 0.1549 0.0338  -0.0126 -0.0437 466 LYS A N   
3957 C CA  . LYS A 466 ? 0.0880 0.2834 0.1047 0.0323  -0.0046 -0.0358 466 LYS A CA  
3958 C C   . LYS A 466 ? 0.1259 0.3188 0.1485 0.0220  -0.0020 -0.0198 466 LYS A C   
3959 O O   . LYS A 466 ? 0.1292 0.3266 0.1441 0.0181  0.0010  -0.0105 466 LYS A O   
3960 C CB  . LYS A 466 ? 0.0969 0.3141 0.1169 0.0404  0.0039  -0.0398 466 LYS A CB  
3961 C CG  . LYS A 466 ? 0.1704 0.4027 0.1811 0.0360  0.0118  -0.0288 466 LYS A CG  
3962 C CD  . LYS A 466 ? 0.2459 0.4907 0.2614 0.0413  0.0177  -0.0317 466 LYS A CD  
3963 C CE  . LYS A 466 ? 0.4351 0.6963 0.4385 0.0410  0.0252  -0.0261 466 LYS A CE  
3964 N NZ  . LYS A 466 ? 0.5292 0.7883 0.5318 0.0292  0.0286  -0.0079 466 LYS A NZ  
3965 N N   . LEU A 467 ? 0.1020 0.2841 0.1355 0.0182  -0.0032 -0.0165 467 LEU A N   
3966 C CA  . LEU A 467 ? 0.0980 0.2697 0.1332 0.0081  -0.0010 -0.0054 467 LEU A CA  
3967 C C   . LEU A 467 ? 0.1595 0.3191 0.1914 0.0046  -0.0040 -0.0014 467 LEU A C   
3968 O O   . LEU A 467 ? 0.0862 0.2482 0.1163 0.0009  -0.0003 0.0074  467 LEU A O   
3969 C CB  . LEU A 467 ? 0.0706 0.2329 0.1137 0.0057  -0.0036 -0.0055 467 LEU A CB  
3970 C CG  . LEU A 467 ? 0.0997 0.2772 0.1499 0.0075  -0.0006 -0.0064 467 LEU A CG  
3971 C CD1 . LEU A 467 ? 0.0591 0.2318 0.1173 0.0083  -0.0061 -0.0074 467 LEU A CD1 
3972 C CD2 . LEU A 467 ? 0.1051 0.2896 0.1564 -0.0018 0.0057  0.0012  467 LEU A CD2 
3973 N N   . PHE A 468 ? 0.1225 0.2694 0.1555 0.0059  -0.0101 -0.0068 468 PHE A N   
3974 C CA  . PHE A 468 ? 0.1020 0.2392 0.1345 0.0025  -0.0122 -0.0032 468 PHE A CA  
3975 C C   . PHE A 468 ? 0.1143 0.2632 0.1404 0.0049  -0.0123 -0.0003 468 PHE A C   
3976 O O   . PHE A 468 ? 0.1310 0.2802 0.1581 0.0036  -0.0104 0.0087  468 PHE A O   
3977 C CB  . PHE A 468 ? 0.0730 0.2001 0.1100 0.0021  -0.0185 -0.0094 468 PHE A CB  
3978 C CG  . PHE A 468 ? 0.0624 0.1855 0.1025 -0.0016 -0.0203 -0.0067 468 PHE A CG  
3979 C CD1 . PHE A 468 ? 0.0539 0.1716 0.0979 -0.0052 -0.0167 0.0003  468 PHE A CD1 
3980 C CD2 . PHE A 468 ? 0.0956 0.2234 0.1356 -0.0012 -0.0258 -0.0127 468 PHE A CD2 
3981 C CE1 . PHE A 468 ? 0.1236 0.2427 0.1740 -0.0071 -0.0171 0.0026  468 PHE A CE1 
3982 C CE2 . PHE A 468 ? 0.1348 0.2630 0.1816 -0.0048 -0.0278 -0.0099 468 PHE A CE2 
3983 C CZ  . PHE A 468 ? 0.1563 0.2813 0.2096 -0.0070 -0.0229 -0.0018 468 PHE A CZ  
3984 N N   . ARG A 469 ? 0.0879 0.2484 0.1070 0.0098  -0.0152 -0.0080 469 ARG A N   
3985 C CA  . ARG A 469 ? 0.0811 0.2534 0.0900 0.0127  -0.0168 -0.0052 469 ARG A CA  
3986 C C   . ARG A 469 ? 0.1451 0.3290 0.1474 0.0138  -0.0094 0.0083  469 ARG A C   
3987 O O   . ARG A 469 ? 0.1113 0.3001 0.1073 0.0160  -0.0101 0.0184  469 ARG A O   
3988 C CB  . ARG A 469 ? 0.1469 0.3266 0.1464 0.0174  -0.0214 -0.0196 469 ARG A CB  
3989 C CG  . ARG A 469 ? 0.1322 0.2968 0.1398 0.0140  -0.0295 -0.0314 469 ARG A CG  
3990 C CD  . ARG A 469 ? 0.1749 0.3438 0.1731 0.0183  -0.0348 -0.0490 469 ARG A CD  
3991 N NE  . ARG A 469 ? 0.1658 0.3191 0.1728 0.0131  -0.0435 -0.0613 469 ARG A NE  
3992 C CZ  . ARG A 469 ? 0.1965 0.3481 0.2060 0.0068  -0.0503 -0.0635 469 ARG A CZ  
3993 N NH1 . ARG A 469 ? 0.1550 0.3199 0.1588 0.0074  -0.0504 -0.0542 469 ARG A NH1 
3994 N NH2 . ARG A 469 ? 0.1708 0.3079 0.1902 -0.0002 -0.0577 -0.0748 469 ARG A NH2 
3995 N N   . SER A 470 ? 0.1292 0.3154 0.1342 0.0119  -0.0016 0.0101  470 SER A N   
3996 C CA  . SER A 470 ? 0.1466 0.3378 0.1482 0.0090  0.0075  0.0246  470 SER A CA  
3997 C C   . SER A 470 ? 0.1158 0.2881 0.1250 0.0037  0.0091  0.0353  470 SER A C   
3998 O O   . SER A 470 ? 0.1359 0.3052 0.1397 0.0042  0.0130  0.0491  470 SER A O   
3999 C CB  . SER A 470 ? 0.1722 0.3729 0.1800 0.0059  0.0149  0.0230  470 SER A CB  
4000 O OG  . SER A 470 ? 0.2247 0.4412 0.2244 0.0134  0.0149  0.0132  470 SER A OG  
4001 N N   . PHE A 471 ? 0.1382 0.2964 0.1583 -0.0003 0.0064  0.0293  471 PHE A N   
4002 C CA  . PHE A 471 ? 0.0913 0.2310 0.1166 -0.0037 0.0087  0.0359  471 PHE A CA  
4003 C C   . PHE A 471 ? 0.1901 0.3278 0.2134 0.0033  0.0051  0.0411  471 PHE A C   
4004 O O   . PHE A 471 ? 0.1399 0.2666 0.1638 0.0052  0.0090  0.0518  471 PHE A O   
4005 C CB  . PHE A 471 ? 0.1262 0.2552 0.1592 -0.0084 0.0067  0.0273  471 PHE A CB  
4006 C CG  . PHE A 471 ? 0.0915 0.2254 0.1290 -0.0149 0.0084  0.0234  471 PHE A CG  
4007 C CD1 . PHE A 471 ? 0.1287 0.2639 0.1691 -0.0219 0.0148  0.0296  471 PHE A CD1 
4008 C CD2 . PHE A 471 ? 0.1447 0.2814 0.1851 -0.0142 0.0031  0.0147  471 PHE A CD2 
4009 C CE1 . PHE A 471 ? 0.1646 0.3062 0.2118 -0.0281 0.0147  0.0250  471 PHE A CE1 
4010 C CE2 . PHE A 471 ? 0.1177 0.2577 0.1616 -0.0177 0.0028  0.0116  471 PHE A CE2 
4011 C CZ  . PHE A 471 ? 0.1354 0.2801 0.1839 -0.0248 0.0080  0.0158  471 PHE A CZ  
4012 N N   . VAL A 472 ? 0.1239 0.2723 0.1467 0.0073  -0.0027 0.0337  472 VAL A N   
4013 C CA  . VAL A 472 ? 0.1395 0.2939 0.1643 0.0134  -0.0080 0.0378  472 VAL A CA  
4014 C C   . VAL A 472 ? 0.1450 0.3092 0.1585 0.0199  -0.0077 0.0506  472 VAL A C   
4015 O O   . VAL A 472 ? 0.1372 0.2995 0.1537 0.0264  -0.0082 0.0618  472 VAL A O   
4016 C CB  . VAL A 472 ? 0.1586 0.3193 0.1854 0.0122  -0.0163 0.0247  472 VAL A CB  
4017 C CG1 . VAL A 472 ? 0.2452 0.4139 0.2712 0.0165  -0.0219 0.0263  472 VAL A CG1 
4018 C CG2 . VAL A 472 ? 0.2149 0.3615 0.2527 0.0066  -0.0153 0.0184  472 VAL A CG2 
4019 N N   . ARG A 473 ? 0.1386 0.3146 0.1386 0.0198  -0.0064 0.0500  473 ARG A N   
4020 C CA  . ARG A 473 ? 0.2068 0.3933 0.1914 0.0255  -0.0045 0.0644  473 ARG A CA  
4021 C C   . ARG A 473 ? 0.2369 0.4046 0.2240 0.0242  0.0053  0.0826  473 ARG A C   
4022 O O   . ARG A 473 ? 0.2095 0.3733 0.1936 0.0314  0.0048  0.0974  473 ARG A O   
4023 C CB  . ARG A 473 ? 0.2031 0.4026 0.1761 0.0241  -0.0010 0.0568  473 ARG A CB  
4024 C CG  . ARG A 473 ? 0.3568 0.5670 0.3157 0.0295  -0.0001 0.0641  473 ARG A CG  
4025 C CD  . ARG A 473 ? 0.5171 0.7405 0.4672 0.0286  0.0051  0.0557  473 ARG A CD  
4026 N NE  . ARG A 473 ? 0.6792 0.9070 0.6330 0.0283  0.0007  0.0345  473 ARG A NE  
4027 C CZ  . ARG A 473 ? 0.7275 0.9569 0.6870 0.0257  0.0058  0.0266  473 ARG A CZ  
4028 N NH1 . ARG A 473 ? 0.7176 0.9458 0.6821 0.0209  0.0154  0.0368  473 ARG A NH1 
4029 N NH2 . ARG A 473 ? 0.7248 0.9548 0.6872 0.0275  0.0009  0.0080  473 ARG A NH2 
4030 N N   . ARG A 474 ? 0.1634 0.3170 0.1584 0.0145  0.0135  0.0799  474 ARG A N   
4031 C CA  . ARG A 474 ? 0.2415 0.3736 0.2402 0.0095  0.0232  0.0940  474 ARG A CA  
4032 C C   . ARG A 474 ? 0.1822 0.2910 0.1905 0.0143  0.0223  0.0978  474 ARG A C   
4033 O O   . ARG A 474 ? 0.2219 0.3116 0.2297 0.0165  0.0281  0.1136  474 ARG A O   
4034 C CB  . ARG A 474 ? 0.2011 0.3285 0.2090 -0.0037 0.0294  0.0859  474 ARG A CB  
4035 C CG  . ARG A 474 ? 0.2640 0.3686 0.2783 -0.0137 0.0390  0.0970  474 ARG A CG  
4036 C CD  . ARG A 474 ? 0.4466 0.5506 0.4519 -0.0143 0.0450  0.1118  474 ARG A CD  
4037 N NE  . ARG A 474 ? 0.5848 0.6680 0.5994 -0.0287 0.0535  0.1155  474 ARG A NE  
4038 C CZ  . ARG A 474 ? 0.7450 0.7951 0.7654 -0.0325 0.0575  0.1233  474 ARG A CZ  
4039 N NH1 . ARG A 474 ? 0.7653 0.8000 0.7842 -0.0200 0.0547  0.1296  474 ARG A NH1 
4040 N NH2 . ARG A 474 ? 0.8228 0.8545 0.8519 -0.0483 0.0643  0.1235  474 ARG A NH2 
4041 N N   . ALA A 475 ? 0.1540 0.2638 0.1714 0.0166  0.0163  0.0842  475 ALA A N   
4042 C CA  . ALA A 475 ? 0.1325 0.2253 0.1600 0.0230  0.0169  0.0856  475 ALA A CA  
4043 C C   . ALA A 475 ? 0.2111 0.3084 0.2374 0.0374  0.0139  0.1013  475 ALA A C   
4044 O O   . ALA A 475 ? 0.2617 0.3409 0.2967 0.0453  0.0173  0.1070  475 ALA A O   
4045 C CB  . ALA A 475 ? 0.1390 0.2401 0.1757 0.0227  0.0119  0.0699  475 ALA A CB  
4046 N N   . GLN A 476 ? 0.1939 0.3157 0.2091 0.0424  0.0070  0.1078  476 GLN A N   
4047 C CA  . GLN A 476 ? 0.1896 0.3204 0.2032 0.0566  0.0016  0.1220  476 GLN A CA  
4048 C C   . GLN A 476 ? 0.2926 0.4094 0.2940 0.0579  0.0081  0.1392  476 GLN A C   
4049 O O   . GLN A 476 ? 0.3104 0.4290 0.3100 0.0682  0.0048  0.1491  476 GLN A O   
4050 C CB  . GLN A 476 ? 0.2214 0.3821 0.2313 0.0569  -0.0096 0.1088  476 GLN A CB  
4051 C CG  . GLN A 476 ? 0.2455 0.4148 0.2665 0.0497  -0.0141 0.0892  476 GLN A CG  
4052 C CD  . GLN A 476 ? 0.2768 0.4646 0.2955 0.0469  -0.0238 0.0746  476 GLN A CD  
4053 O OE1 . GLN A 476 ? 0.3367 0.5352 0.3567 0.0530  -0.0301 0.0775  476 GLN A OE1 
4054 N NE2 . GLN A 476 ? 0.2368 0.4271 0.2516 0.0379  -0.0254 0.0593  476 GLN A NE2 
4055 N N   . GLU A 477 ? 0.3279 0.4305 0.3231 0.0466  0.0175  0.1427  477 GLU A N   
4056 C CA  . GLU A 477 ? 0.3851 0.4735 0.3712 0.0445  0.0247  0.1580  477 GLU A CA  
4057 C C   . GLU A 477 ? 0.4385 0.4859 0.4344 0.0401  0.0347  0.1662  477 GLU A C   
4058 O O   . GLU A 477 ? 0.5611 0.5876 0.5539 0.0440  0.0385  0.1812  477 GLU A O   
4059 C CB  . GLU A 477 ? 0.4000 0.5040 0.3751 0.0331  0.0286  0.1534  477 GLU A CB  
4060 C CG  . GLU A 477 ? 0.5544 0.6935 0.5184 0.0377  0.0197  0.1425  477 GLU A CG  
4061 C CD  . GLU A 477 ? 0.6975 0.8518 0.6540 0.0287  0.0246  0.1339  477 GLU A CD  
4062 O OE1 . GLU A 477 ? 0.6990 0.8405 0.6614 0.0177  0.0341  0.1358  477 GLU A OE1 
4063 O OE2 . GLU A 477 ? 0.7213 0.9003 0.6675 0.0326  0.0189  0.1237  477 GLU A OE2 
4064 N N   . LYS B 2   ? 0.5345 0.5538 0.2938 -0.2008 0.0071  -0.0184 2   LYS B N   
4065 C CA  . LYS B 2   ? 0.5646 0.5754 0.3362 -0.1951 0.0155  -0.0237 2   LYS B CA  
4066 C C   . LYS B 2   ? 0.4902 0.4968 0.2758 -0.1830 0.0119  -0.0218 2   LYS B C   
4067 O O   . LYS B 2   ? 0.5363 0.5472 0.3289 -0.1803 0.0127  -0.0268 2   LYS B O   
4068 C CB  . LYS B 2   ? 0.6122 0.6256 0.3894 -0.2002 0.0298  -0.0384 2   LYS B CB  
4069 C CG  . LYS B 2   ? 0.6262 0.6323 0.4167 -0.1946 0.0385  -0.0438 2   LYS B CG  
4070 C CD  . LYS B 2   ? 0.6848 0.6937 0.4835 -0.1986 0.0523  -0.0579 2   LYS B CD  
4071 C CE  . LYS B 2   ? 0.7336 0.7444 0.5451 -0.1932 0.0565  -0.0647 2   LYS B CE  
4072 N NZ  . LYS B 2   ? 0.7317 0.7434 0.5544 -0.1953 0.0704  -0.0779 2   LYS B NZ  
4073 N N   . LYS B 3   ? 0.4479 0.4459 0.2372 -0.1760 0.0080  -0.0147 3   LYS B N   
4074 C CA  . LYS B 3   ? 0.4867 0.4804 0.2882 -0.1647 0.0042  -0.0124 3   LYS B CA  
4075 C C   . LYS B 3   ? 0.4221 0.4107 0.2365 -0.1601 0.0148  -0.0208 3   LYS B C   
4076 O O   . LYS B 3   ? 0.4446 0.4312 0.2588 -0.1643 0.0229  -0.0256 3   LYS B O   
4077 C CB  . LYS B 3   ? 0.5826 0.5700 0.3812 -0.1590 -0.0075 0.0011  3   LYS B CB  
4078 C CG  . LYS B 3   ? 0.7016 0.6927 0.4881 -0.1628 -0.0181 0.0118  3   LYS B CG  
4079 C CD  . LYS B 3   ? 0.7819 0.7835 0.5687 -0.1634 -0.0233 0.0111  3   LYS B CD  
4080 C CE  . LYS B 3   ? 0.8498 0.8518 0.6395 -0.1554 -0.0370 0.0233  3   LYS B CE  
4081 N NZ  . LYS B 3   ? 0.9459 0.9425 0.7276 -0.1553 -0.0444 0.0362  3   LYS B NZ  
4082 N N   . LEU B 4   ? 0.3194 0.3070 0.1461 -0.1509 0.0142  -0.0226 4   LEU B N   
4083 C CA  . LEU B 4   ? 0.3527 0.3346 0.1918 -0.1435 0.0203  -0.0262 4   LEU B CA  
4084 C C   . LEU B 4   ? 0.3337 0.3087 0.1725 -0.1366 0.0104  -0.0164 4   LEU B C   
4085 O O   . LEU B 4   ? 0.3306 0.3069 0.1691 -0.1326 0.0002  -0.0101 4   LEU B O   
4086 C CB  . LEU B 4   ? 0.3378 0.3226 0.1916 -0.1369 0.0263  -0.0345 4   LEU B CB  
4087 C CG  . LEU B 4   ? 0.2994 0.2798 0.1684 -0.1273 0.0320  -0.0380 4   LEU B CG  
4088 C CD1 . LEU B 4   ? 0.3368 0.3205 0.2186 -0.1249 0.0429  -0.0483 4   LEU B CD1 
4089 C CD2 . LEU B 4   ? 0.2387 0.2158 0.1153 -0.1175 0.0224  -0.0322 4   LEU B CD2 
4090 N N   . PHE B 5   ? 0.3250 0.2934 0.1650 -0.1353 0.0133  -0.0153 5   PHE B N   
4091 C CA  . PHE B 5   ? 0.3006 0.2612 0.1401 -0.1290 0.0051  -0.0064 5   PHE B CA  
4092 C C   . PHE B 5   ? 0.3412 0.3004 0.1994 -0.1188 0.0080  -0.0113 5   PHE B C   
4093 O O   . PHE B 5   ? 0.3685 0.3284 0.2356 -0.1182 0.0178  -0.0189 5   PHE B O   
4094 C CB  . PHE B 5   ? 0.2970 0.2512 0.1299 -0.1324 0.0057  -0.0011 5   PHE B CB  
4095 C CG  . PHE B 5   ? 0.3517 0.3075 0.1715 -0.1402 0.0015  0.0041  5   PHE B CG  
4096 C CD1 . PHE B 5   ? 0.4250 0.3812 0.2388 -0.1391 -0.0097 0.0141  5   PHE B CD1 
4097 C CD2 . PHE B 5   ? 0.3931 0.3510 0.2075 -0.1483 0.0085  -0.0008 5   PHE B CD2 
4098 C CE1 . PHE B 5   ? 0.4483 0.4069 0.2501 -0.1461 -0.0136 0.0197  5   PHE B CE1 
4099 C CE2 . PHE B 5   ? 0.4385 0.3983 0.2395 -0.1560 0.0048  0.0045  5   PHE B CE2 
4100 C CZ  . PHE B 5   ? 0.4658 0.4260 0.2603 -0.1550 -0.0063 0.0150  5   PHE B CZ  
4101 N N   . LEU B 6   ? 0.2646 0.2232 0.1322 -0.1097 -0.0003 -0.0064 6   LEU B N   
4102 C CA  . LEU B 6   ? 0.2745 0.2333 0.1618 -0.0991 0.0015  -0.0097 6   LEU B CA  
4103 C C   . LEU B 6   ? 0.2095 0.1617 0.1035 -0.0908 -0.0043 -0.0018 6   LEU B C   
4104 O O   . LEU B 6   ? 0.2405 0.1893 0.1288 -0.0895 -0.0132 0.0068  6   LEU B O   
4105 C CB  . LEU B 6   ? 0.2455 0.2103 0.1388 -0.0962 -0.0021 -0.0120 6   LEU B CB  
4106 C CG  . LEU B 6   ? 0.2482 0.2143 0.1608 -0.0860 -0.0005 -0.0147 6   LEU B CG  
4107 C CD1 . LEU B 6   ? 0.2227 0.1889 0.1451 -0.0850 0.0105  -0.0228 6   LEU B CD1 
4108 C CD2 . LEU B 6   ? 0.2079 0.1805 0.1238 -0.0858 -0.0043 -0.0165 6   LEU B CD2 
4109 N N   . VAL B 7   ? 0.1827 0.1333 0.0888 -0.0854 0.0008  -0.0049 7   VAL B N   
4110 C CA  . VAL B 7   ? 0.1880 0.1323 0.1000 -0.0788 -0.0033 0.0005  7   VAL B CA  
4111 C C   . VAL B 7   ? 0.2359 0.1836 0.1649 -0.0691 -0.0018 -0.0031 7   VAL B C   
4112 O O   . VAL B 7   ? 0.2714 0.2228 0.2085 -0.0683 0.0055  -0.0089 7   VAL B O   
4113 C CB  . VAL B 7   ? 0.1990 0.1384 0.1066 -0.0838 0.0009  0.0010  7   VAL B CB  
4114 C CG1 . VAL B 7   ? 0.3064 0.2379 0.2188 -0.0782 -0.0040 0.0063  7   VAL B CG1 
4115 C CG2 . VAL B 7   ? 0.2493 0.1866 0.1388 -0.0951 0.0015  0.0041  7   VAL B CG2 
4116 N N   . PHE B 8   ? 0.1554 0.1028 0.0902 -0.0616 -0.0084 0.0005  8   PHE B N   
4117 C CA  . PHE B 8   ? 0.1405 0.0909 0.0897 -0.0525 -0.0075 -0.0018 8   PHE B CA  
4118 C C   . PHE B 8   ? 0.1672 0.1117 0.1192 -0.0489 -0.0090 0.0003  8   PHE B C   
4119 O O   . PHE B 8   ? 0.2014 0.1383 0.1475 -0.0492 -0.0144 0.0057  8   PHE B O   
4120 C CB  . PHE B 8   ? 0.1501 0.1040 0.1047 -0.0466 -0.0130 0.0003  8   PHE B CB  
4121 C CG  . PHE B 8   ? 0.1775 0.1382 0.1325 -0.0497 -0.0112 -0.0030 8   PHE B CG  
4122 C CD1 . PHE B 8   ? 0.1866 0.1523 0.1521 -0.0469 -0.0053 -0.0081 8   PHE B CD1 
4123 C CD2 . PHE B 8   ? 0.2156 0.1777 0.1605 -0.0558 -0.0154 -0.0009 8   PHE B CD2 
4124 C CE1 . PHE B 8   ? 0.2087 0.1793 0.1753 -0.0504 -0.0030 -0.0119 8   PHE B CE1 
4125 C CE2 . PHE B 8   ? 0.2395 0.2081 0.1845 -0.0598 -0.0136 -0.0052 8   PHE B CE2 
4126 C CZ  . PHE B 8   ? 0.2325 0.2046 0.1888 -0.0572 -0.0070 -0.0112 8   PHE B CZ  
4127 N N   . TRP B 9   ? 0.1419 0.0898 0.1030 -0.0455 -0.0046 -0.0036 9   TRP B N   
4128 C CA  . TRP B 9   ? 0.1384 0.0820 0.1025 -0.0425 -0.0060 -0.0030 9   TRP B CA  
4129 C C   . TRP B 9   ? 0.1642 0.1146 0.1400 -0.0347 -0.0049 -0.0058 9   TRP B C   
4130 O O   . TRP B 9   ? 0.1448 0.1024 0.1270 -0.0344 0.0001  -0.0091 9   TRP B O   
4131 C CB  . TRP B 9   ? 0.1644 0.1065 0.1252 -0.0494 -0.0015 -0.0047 9   TRP B CB  
4132 C CG  . TRP B 9   ? 0.1621 0.0979 0.1231 -0.0496 -0.0033 -0.0040 9   TRP B CG  
4133 C CD1 . TRP B 9   ? 0.1925 0.1228 0.1563 -0.0439 -0.0080 -0.0028 9   TRP B CD1 
4134 C CD2 . TRP B 9   ? 0.1681 0.1017 0.1260 -0.0568 0.0000  -0.0050 9   TRP B CD2 
4135 N NE1 . TRP B 9   ? 0.1643 0.0883 0.1269 -0.0475 -0.0077 -0.0035 9   TRP B NE1 
4136 C CE2 . TRP B 9   ? 0.1641 0.0904 0.1232 -0.0556 -0.0031 -0.0044 9   TRP B CE2 
4137 C CE3 . TRP B 9   ? 0.2181 0.1567 0.1734 -0.0634 0.0058  -0.0066 9   TRP B CE3 
4138 C CZ2 . TRP B 9   ? 0.1833 0.1084 0.1419 -0.0607 -0.0008 -0.0053 9   TRP B CZ2 
4139 C CZ3 . TRP B 9   ? 0.2100 0.1485 0.1650 -0.0672 0.0080  -0.0070 9   TRP B CZ3 
4140 C CH2 . TRP B 9   ? 0.2270 0.1591 0.1839 -0.0661 0.0045  -0.0062 9   TRP B CH2 
4141 N N   . TRP B 10  ? 0.1594 0.1083 0.1383 -0.0283 -0.0095 -0.0041 10  TRP B N   
4142 C CA  . TRP B 10  ? 0.1522 0.1080 0.1404 -0.0212 -0.0087 -0.0062 10  TRP B CA  
4143 C C   . TRP B 10  ? 0.1482 0.1025 0.1383 -0.0193 -0.0090 -0.0083 10  TRP B C   
4144 O O   . TRP B 10  ? 0.1498 0.0958 0.1372 -0.0184 -0.0125 -0.0075 10  TRP B O   
4145 C CB  . TRP B 10  ? 0.1166 0.0732 0.1076 -0.0157 -0.0127 -0.0041 10  TRP B CB  
4146 C CG  . TRP B 10  ? 0.1385 0.0979 0.1279 -0.0179 -0.0134 -0.0024 10  TRP B CG  
4147 C CD1 . TRP B 10  ? 0.1229 0.0787 0.1070 -0.0197 -0.0185 0.0014  10  TRP B CD1 
4148 C CD2 . TRP B 10  ? 0.1676 0.1346 0.1616 -0.0186 -0.0093 -0.0044 10  TRP B CD2 
4149 N NE1 . TRP B 10  ? 0.1552 0.1171 0.1395 -0.0223 -0.0179 0.0010  10  TRP B NE1 
4150 C CE2 . TRP B 10  ? 0.1384 0.1061 0.1289 -0.0218 -0.0119 -0.0029 10  TRP B CE2 
4151 C CE3 . TRP B 10  ? 0.1300 0.1030 0.1311 -0.0170 -0.0038 -0.0069 10  TRP B CE3 
4152 C CZ2 . TRP B 10  ? 0.1430 0.1163 0.1366 -0.0241 -0.0086 -0.0052 10  TRP B CZ2 
4153 C CZ3 . TRP B 10  ? 0.1381 0.1153 0.1429 -0.0185 -0.0003 -0.0082 10  TRP B CZ3 
4154 C CH2 . TRP B 10  ? 0.1235 0.1004 0.1245 -0.0224 -0.0025 -0.0079 10  TRP B CH2 
4155 N N   . HIS B 11  ? 0.1055 0.0680 0.1011 -0.0186 -0.0054 -0.0110 11  HIS B N   
4156 C CA  . HIS B 11  ? 0.1122 0.0758 0.1092 -0.0184 -0.0056 -0.0137 11  HIS B CA  
4157 C C   . HIS B 11  ? 0.1345 0.1036 0.1360 -0.0115 -0.0068 -0.0153 11  HIS B C   
4158 O O   . HIS B 11  ? 0.1289 0.1073 0.1356 -0.0078 -0.0050 -0.0146 11  HIS B O   
4159 C CB  . HIS B 11  ? 0.1338 0.1054 0.1346 -0.0219 -0.0016 -0.0153 11  HIS B CB  
4160 C CG  . HIS B 11  ? 0.1285 0.1069 0.1331 -0.0208 -0.0021 -0.0181 11  HIS B CG  
4161 N ND1 . HIS B 11  ? 0.1354 0.1079 0.1363 -0.0238 -0.0043 -0.0208 11  HIS B ND1 
4162 C CD2 . HIS B 11  ? 0.1091 0.1001 0.1205 -0.0173 -0.0009 -0.0185 11  HIS B CD2 
4163 C CE1 . HIS B 11  ? 0.1565 0.1385 0.1614 -0.0228 -0.0046 -0.0237 11  HIS B CE1 
4164 N NE2 . HIS B 11  ? 0.1201 0.1140 0.1311 -0.0187 -0.0029 -0.0218 11  HIS B NE2 
4165 N N   . MET B 12  ? 0.1009 0.0637 0.1003 -0.0102 -0.0095 -0.0175 12  MET B N   
4166 C CA  . MET B 12  ? 0.1116 0.0787 0.1138 -0.0042 -0.0101 -0.0201 12  MET B CA  
4167 C C   . MET B 12  ? 0.1677 0.1381 0.1693 -0.0062 -0.0099 -0.0250 12  MET B C   
4168 O O   . MET B 12  ? 0.1217 0.0834 0.1200 -0.0109 -0.0109 -0.0272 12  MET B O   
4169 C CB  . MET B 12  ? 0.1341 0.0915 0.1356 -0.0005 -0.0129 -0.0201 12  MET B CB  
4170 C CG  . MET B 12  ? 0.1065 0.0606 0.1081 0.0003  -0.0145 -0.0150 12  MET B CG  
4171 S SD  . MET B 12  ? 0.1420 0.1093 0.1490 0.0035  -0.0122 -0.0130 12  MET B SD  
4172 C CE  . MET B 12  ? 0.1336 0.0955 0.1401 0.0039  -0.0158 -0.0085 12  MET B CE  
4173 N N   . HIS B 13  ? 0.1080 0.0909 0.1123 -0.0033 -0.0089 -0.0264 13  HIS B N   
4174 C CA  . HIS B 13  ? 0.1151 0.1036 0.1182 -0.0059 -0.0093 -0.0312 13  HIS B CA  
4175 C C   . HIS B 13  ? 0.1577 0.1589 0.1618 -0.0014 -0.0089 -0.0326 13  HIS B C   
4176 O O   . HIS B 13  ? 0.1226 0.1313 0.1298 0.0027  -0.0075 -0.0281 13  HIS B O   
4177 C CB  . HIS B 13  ? 0.1200 0.1150 0.1254 -0.0113 -0.0086 -0.0299 13  HIS B CB  
4178 C CG  . HIS B 13  ? 0.1042 0.1107 0.1102 -0.0136 -0.0096 -0.0337 13  HIS B CG  
4179 N ND1 . HIS B 13  ? 0.1234 0.1255 0.1254 -0.0172 -0.0112 -0.0404 13  HIS B ND1 
4180 C CD2 . HIS B 13  ? 0.1446 0.1673 0.1550 -0.0129 -0.0095 -0.0316 13  HIS B CD2 
4181 C CE1 . HIS B 13  ? 0.1682 0.1845 0.1713 -0.0194 -0.0123 -0.0428 13  HIS B CE1 
4182 N NE2 . HIS B 13  ? 0.1303 0.1599 0.1388 -0.0165 -0.0117 -0.0370 13  HIS B NE2 
4183 N N   . GLN B 14  ? 0.1387 0.1422 0.1394 -0.0028 -0.0098 -0.0389 14  GLN B N   
4184 C CA  . GLN B 14  ? 0.1427 0.1609 0.1421 -0.0006 -0.0096 -0.0407 14  GLN B CA  
4185 C C   . GLN B 14  ? 0.1296 0.1527 0.1258 -0.0065 -0.0114 -0.0468 14  GLN B C   
4186 O O   . GLN B 14  ? 0.1560 0.1674 0.1496 -0.0103 -0.0120 -0.0532 14  GLN B O   
4187 C CB  . GLN B 14  ? 0.1566 0.1735 0.1538 0.0045  -0.0082 -0.0442 14  GLN B CB  
4188 C CG  . GLN B 14  ? 0.1015 0.1168 0.1028 0.0102  -0.0065 -0.0387 14  GLN B CG  
4189 C CD  . GLN B 14  ? 0.1224 0.1505 0.1268 0.0121  -0.0052 -0.0312 14  GLN B CD  
4190 O OE1 . GLN B 14  ? 0.1305 0.1712 0.1336 0.0111  -0.0056 -0.0301 14  GLN B OE1 
4191 N NE2 . GLN B 14  ? 0.1329 0.1578 0.1419 0.0147  -0.0040 -0.0259 14  GLN B NE2 
4192 N N   . PRO B 15  ? 0.1250 0.1654 0.1216 -0.0074 -0.0126 -0.0452 15  PRO B N   
4193 C CA  . PRO B 15  ? 0.1365 0.1847 0.1295 -0.0132 -0.0150 -0.0520 15  PRO B CA  
4194 C C   . PRO B 15  ? 0.1818 0.2275 0.1675 -0.0129 -0.0143 -0.0610 15  PRO B C   
4195 O O   . PRO B 15  ? 0.1675 0.2094 0.1519 -0.0073 -0.0119 -0.0609 15  PRO B O   
4196 C CB  . PRO B 15  ? 0.1113 0.1809 0.1071 -0.0125 -0.0169 -0.0460 15  PRO B CB  
4197 C CG  . PRO B 15  ? 0.1309 0.2029 0.1287 -0.0050 -0.0146 -0.0381 15  PRO B CG  
4198 C CD  . PRO B 15  ? 0.0992 0.1532 0.0998 -0.0029 -0.0120 -0.0368 15  PRO B CD  
4199 N N   . LEU B 16  ? 0.1649 0.2133 0.1463 -0.0194 -0.0160 -0.0696 16  LEU B N   
4200 C CA  . LEU B 16  ? 0.1813 0.2263 0.1556 -0.0201 -0.0146 -0.0802 16  LEU B CA  
4201 C C   . LEU B 16  ? 0.2168 0.2811 0.1855 -0.0175 -0.0146 -0.0797 16  LEU B C   
4202 O O   . LEU B 16  ? 0.2262 0.3085 0.1920 -0.0215 -0.0178 -0.0794 16  LEU B O   
4203 C CB  . LEU B 16  ? 0.2174 0.2578 0.1890 -0.0288 -0.0159 -0.0900 16  LEU B CB  
4204 C CG  . LEU B 16  ? 0.2245 0.2567 0.1904 -0.0290 -0.0130 -0.0986 16  LEU B CG  
4205 C CD1 . LEU B 16  ? 0.2498 0.2636 0.2176 -0.0225 -0.0093 -0.1003 16  LEU B CD1 
4206 C CD2 . LEU B 16  ? 0.2500 0.2749 0.2150 -0.0369 -0.0138 -0.1039 16  LEU B CD2 
4207 N N   . TYR B 17  ? 0.2170 0.2789 0.1844 -0.0109 -0.0111 -0.0792 17  TYR B N   
4208 C CA  . TYR B 17  ? 0.2390 0.3182 0.2000 -0.0086 -0.0101 -0.0783 17  TYR B CA  
4209 C C   . TYR B 17  ? 0.2112 0.2932 0.1631 -0.0122 -0.0085 -0.0909 17  TYR B C   
4210 O O   . TYR B 17  ? 0.2159 0.3119 0.1616 -0.0111 -0.0071 -0.0899 17  TYR B O   
4211 C CB  . TYR B 17  ? 0.2130 0.2895 0.1775 -0.0005 -0.0063 -0.0720 17  TYR B CB  
4212 C CG  . TYR B 17  ? 0.1875 0.2629 0.1606 0.0029  -0.0073 -0.0592 17  TYR B CG  
4213 C CD1 . TYR B 17  ? 0.2179 0.3083 0.1925 0.0023  -0.0098 -0.0500 17  TYR B CD1 
4214 C CD2 . TYR B 17  ? 0.1401 0.2000 0.1202 0.0066  -0.0056 -0.0565 17  TYR B CD2 
4215 C CE1 . TYR B 17  ? 0.1604 0.2488 0.1434 0.0054  -0.0098 -0.0396 17  TYR B CE1 
4216 C CE2 . TYR B 17  ? 0.1488 0.2077 0.1358 0.0088  -0.0060 -0.0462 17  TYR B CE2 
4217 C CZ  . TYR B 17  ? 0.1432 0.2157 0.1318 0.0081  -0.0076 -0.0384 17  TYR B CZ  
4218 O OH  . TYR B 17  ? 0.1120 0.1822 0.1083 0.0103  -0.0071 -0.0295 17  TYR B OH  
4219 N N   . ARG B 18  ? 0.2288 0.2946 0.1817 -0.0161 -0.0076 -0.0988 18  ARG B N   
4220 C CA  . ARG B 18  ? 0.2016 0.2636 0.1492 -0.0184 -0.0046 -0.1081 18  ARG B CA  
4221 C C   . ARG B 18  ? 0.3072 0.3824 0.2494 -0.0262 -0.0080 -0.1102 18  ARG B C   
4222 O O   . ARG B 18  ? 0.2418 0.3116 0.1866 -0.0318 -0.0107 -0.1115 18  ARG B O   
4223 C CB  . ARG B 18  ? 0.2609 0.2981 0.2128 -0.0181 -0.0019 -0.1146 18  ARG B CB  
4224 C CG  . ARG B 18  ? 0.3215 0.3524 0.2690 -0.0194 0.0021  -0.1249 18  ARG B CG  
4225 C CD  . ARG B 18  ? 0.3641 0.3701 0.3163 -0.0201 0.0035  -0.1296 18  ARG B CD  
4226 N NE  . ARG B 18  ? 0.4368 0.4345 0.3861 -0.0202 0.0078  -0.1396 18  ARG B NE  
4227 C CZ  . ARG B 18  ? 0.4145 0.4149 0.3580 -0.0271 0.0077  -0.1474 18  ARG B CZ  
4228 N NH1 . ARG B 18  ? 0.4171 0.4294 0.3574 -0.0346 0.0030  -0.1458 18  ARG B NH1 
4229 N NH2 . ARG B 18  ? 0.4673 0.4592 0.4089 -0.0266 0.0123  -0.1570 18  ARG B NH2 
4230 N N   . GLU B 19  ? 0.3131 0.4060 0.2481 -0.0268 -0.0078 -0.1099 19  GLU B N   
4231 C CA  . GLU B 19  ? 0.3312 0.4387 0.2609 -0.0339 -0.0113 -0.1115 19  GLU B CA  
4232 C C   . GLU B 19  ? 0.3752 0.4698 0.3026 -0.0396 -0.0095 -0.1235 19  GLU B C   
4233 O O   . GLU B 19  ? 0.3448 0.4281 0.2700 -0.0374 -0.0044 -0.1312 19  GLU B O   
4234 C CB  . GLU B 19  ? 0.3631 0.4908 0.2848 -0.0330 -0.0110 -0.1082 19  GLU B CB  
4235 C CG  . GLU B 19  ? 0.4537 0.6025 0.3720 -0.0383 -0.0165 -0.1035 19  GLU B CG  
4236 C CD  . GLU B 19  ? 0.5511 0.7020 0.4626 -0.0458 -0.0164 -0.1141 19  GLU B CD  
4237 O OE1 . GLU B 19  ? 0.5997 0.7391 0.5071 -0.0459 -0.0113 -0.1243 19  GLU B OE1 
4238 O OE2 . GLU B 19  ? 0.6284 0.7927 0.5391 -0.0514 -0.0214 -0.1123 19  GLU B OE2 
4239 N N   . PRO B 20  ? 0.3126 0.4086 0.2414 -0.0466 -0.0132 -0.1253 20  PRO B N   
4240 C CA  . PRO B 20  ? 0.3776 0.4572 0.3059 -0.0518 -0.0112 -0.1361 20  PRO B CA  
4241 C C   . PRO B 20  ? 0.4003 0.4857 0.3198 -0.0557 -0.0089 -0.1461 20  PRO B C   
4242 O O   . PRO B 20  ? 0.4899 0.5591 0.4090 -0.0582 -0.0057 -0.1560 20  PRO B O   
4243 C CB  . PRO B 20  ? 0.3883 0.4708 0.3215 -0.0583 -0.0160 -0.1335 20  PRO B CB  
4244 C CG  . PRO B 20  ? 0.3606 0.4681 0.2936 -0.0582 -0.0208 -0.1242 20  PRO B CG  
4245 C CD  . PRO B 20  ? 0.3102 0.4218 0.2425 -0.0498 -0.0191 -0.1171 20  PRO B CD  
4246 N N   . TYR B 21  ? 0.3227 0.4300 0.2351 -0.0566 -0.0104 -0.1437 21  TYR B N   
4247 C CA  . TYR B 21  ? 0.3892 0.5034 0.2922 -0.0612 -0.0081 -0.1535 21  TYR B CA  
4248 C C   . TYR B 21  ? 0.4572 0.5657 0.3562 -0.0555 -0.0016 -0.1580 21  TYR B C   
4249 O O   . TYR B 21  ? 0.4532 0.5537 0.3481 -0.0579 0.0028  -0.1697 21  TYR B O   
4250 C CB  . TYR B 21  ? 0.3181 0.4595 0.2148 -0.0657 -0.0132 -0.1484 21  TYR B CB  
4251 C CG  . TYR B 21  ? 0.4039 0.5509 0.3048 -0.0725 -0.0190 -0.1472 21  TYR B CG  
4252 C CD1 . TYR B 21  ? 0.4119 0.5568 0.3097 -0.0809 -0.0191 -0.1581 21  TYR B CD1 
4253 C CD2 . TYR B 21  ? 0.3761 0.5297 0.2849 -0.0705 -0.0237 -0.1356 21  TYR B CD2 
4254 C CE1 . TYR B 21  ? 0.4450 0.5955 0.3475 -0.0873 -0.0241 -0.1572 21  TYR B CE1 
4255 C CE2 . TYR B 21  ? 0.4146 0.5738 0.3286 -0.0765 -0.0284 -0.1346 21  TYR B CE2 
4256 C CZ  . TYR B 21  ? 0.4180 0.5758 0.3288 -0.0850 -0.0286 -0.1453 21  TYR B CZ  
4257 O OH  . TYR B 21  ? 0.4779 0.6421 0.3944 -0.0912 -0.0331 -0.1443 21  TYR B OH  
4258 N N   . THR B 22  ? 0.4046 0.5170 0.3055 -0.0481 -0.0005 -0.1494 22  THR B N   
4259 C CA  . THR B 22  ? 0.4041 0.5122 0.3028 -0.0424 0.0061  -0.1528 22  THR B CA  
4260 C C   . THR B 22  ? 0.4215 0.5066 0.3297 -0.0354 0.0100  -0.1540 22  THR B C   
4261 O O   . THR B 22  ? 0.3615 0.4392 0.2698 -0.0309 0.0161  -0.1594 22  THR B O   
4262 C CB  . THR B 22  ? 0.4307 0.5578 0.3256 -0.0385 0.0055  -0.1425 22  THR B CB  
4263 O OG1 . THR B 22  ? 0.4058 0.5313 0.3087 -0.0334 0.0028  -0.1311 22  THR B OG1 
4264 C CG2 . THR B 22  ? 0.4389 0.5895 0.3251 -0.0449 0.0008  -0.1391 22  THR B CG2 
4265 N N   . GLY B 23  ? 0.3708 0.4453 0.2870 -0.0343 0.0068  -0.1486 23  GLY B N   
4266 C CA  . GLY B 23  ? 0.4438 0.4986 0.3689 -0.0273 0.0097  -0.1474 23  GLY B CA  
4267 C C   . GLY B 23  ? 0.4316 0.4924 0.3597 -0.0194 0.0115  -0.1394 23  GLY B C   
4268 O O   . GLY B 23  ? 0.4735 0.5197 0.4092 -0.0130 0.0144  -0.1388 23  GLY B O   
4269 N N   . GLU B 24  ? 0.3196 0.4017 0.2424 -0.0197 0.0097  -0.1326 24  GLU B N   
4270 C CA  . GLU B 24  ? 0.3127 0.4013 0.2381 -0.0126 0.0116  -0.1246 24  GLU B CA  
4271 C C   . GLU B 24  ? 0.3132 0.4009 0.2453 -0.0101 0.0074  -0.1146 24  GLU B C   
4272 O O   . GLU B 24  ? 0.2591 0.3541 0.1904 -0.0146 0.0019  -0.1102 24  GLU B O   
4273 C CB  . GLU B 24  ? 0.4152 0.5264 0.3316 -0.0140 0.0117  -0.1201 24  GLU B CB  
4274 C CG  . GLU B 24  ? 0.5811 0.6956 0.4906 -0.0149 0.0174  -0.1287 24  GLU B CG  
4275 C CD  . GLU B 24  ? 0.7352 0.8726 0.6340 -0.0188 0.0159  -0.1241 24  GLU B CD  
4276 O OE1 . GLU B 24  ? 0.7845 0.9346 0.6822 -0.0205 0.0101  -0.1139 24  GLU B OE1 
4277 O OE2 . GLU B 24  ? 0.8203 0.9630 0.7122 -0.0199 0.0206  -0.1301 24  GLU B OE2 
4278 N N   . TYR B 25  ? 0.2807 0.3606 0.2201 -0.0029 0.0100  -0.1109 25  TYR B N   
4279 C CA  . TYR B 25  ? 0.2565 0.3392 0.2010 0.0000  0.0067  -0.1010 25  TYR B CA  
4280 C C   . TYR B 25  ? 0.2238 0.3277 0.1634 0.0014  0.0063  -0.0918 25  TYR B C   
4281 O O   . TYR B 25  ? 0.2753 0.3843 0.2139 0.0055  0.0110  -0.0905 25  TYR B O   
4282 C CB  . TYR B 25  ? 0.2300 0.2972 0.1843 0.0070  0.0093  -0.1001 25  TYR B CB  
4283 C CG  . TYR B 25  ? 0.2578 0.3036 0.2180 0.0057  0.0078  -0.1046 25  TYR B CG  
4284 C CD1 . TYR B 25  ? 0.2802 0.3132 0.2397 0.0035  0.0101  -0.1135 25  TYR B CD1 
4285 C CD2 . TYR B 25  ? 0.2562 0.2944 0.2222 0.0059  0.0041  -0.0984 25  TYR B CD2 
4286 C CE1 . TYR B 25  ? 0.3510 0.3637 0.3156 0.0021  0.0088  -0.1155 25  TYR B CE1 
4287 C CE2 . TYR B 25  ? 0.2320 0.2511 0.2023 0.0039  0.0028  -0.1014 25  TYR B CE2 
4288 C CZ  . TYR B 25  ? 0.3191 0.3252 0.2889 0.0021  0.0050  -0.1089 25  TYR B CZ  
4289 O OH  . TYR B 25  ? 0.2536 0.2399 0.2275 0.0001  0.0037  -0.1091 25  TYR B OH  
4290 N N   . LEU B 26  ? 0.2278 0.3438 0.1651 -0.0019 0.0009  -0.0845 26  LEU B N   
4291 C CA  . LEU B 26  ? 0.2522 0.3885 0.1845 -0.0015 -0.0003 -0.0742 26  LEU B CA  
4292 C C   . LEU B 26  ? 0.2413 0.3787 0.1805 0.0047  0.0004  -0.0615 26  LEU B C   
4293 O O   . LEU B 26  ? 0.2120 0.3639 0.1480 0.0061  0.0007  -0.0518 26  LEU B O   
4294 C CB  . LEU B 26  ? 0.2970 0.4459 0.2267 -0.0073 -0.0067 -0.0703 26  LEU B CB  
4295 C CG  . LEU B 26  ? 0.2518 0.4002 0.1759 -0.0142 -0.0073 -0.0809 26  LEU B CG  
4296 C CD1 . LEU B 26  ? 0.2906 0.4545 0.2135 -0.0192 -0.0137 -0.0751 26  LEU B CD1 
4297 C CD2 . LEU B 26  ? 0.2783 0.4307 0.1945 -0.0142 -0.0022 -0.0864 26  LEU B CD2 
4298 N N   . LEU B 27  ? 0.2209 0.3410 0.1712 0.0079  0.0008  -0.0595 27  LEU B N   
4299 C CA  . LEU B 27  ? 0.1899 0.3061 0.1496 0.0132  0.0023  -0.0480 27  LEU B CA  
4300 C C   . LEU B 27  ? 0.1570 0.2555 0.1239 0.0167  0.0054  -0.0532 27  LEU B C   
4301 O O   . LEU B 27  ? 0.2133 0.2996 0.1806 0.0150  0.0047  -0.0623 27  LEU B O   
4302 C CB  . LEU B 27  ? 0.2895 0.4052 0.2565 0.0125  -0.0021 -0.0381 27  LEU B CB  
4303 C CG  . LEU B 27  ? 0.2401 0.3747 0.2031 0.0106  -0.0056 -0.0300 27  LEU B CG  
4304 C CD1 . LEU B 27  ? 0.2491 0.3826 0.2212 0.0102  -0.0095 -0.0225 27  LEU B CD1 
4305 C CD2 . LEU B 27  ? 0.2514 0.3962 0.2127 0.0142  -0.0026 -0.0206 27  LEU B CD2 
4306 N N   . PRO B 28  ? 0.1913 0.2884 0.1642 0.0215  0.0089  -0.0474 28  PRO B N   
4307 C CA  . PRO B 28  ? 0.1258 0.2092 0.1062 0.0254  0.0115  -0.0518 28  PRO B CA  
4308 C C   . PRO B 28  ? 0.2160 0.2865 0.2059 0.0266  0.0089  -0.0457 28  PRO B C   
4309 O O   . PRO B 28  ? 0.1909 0.2530 0.1877 0.0303  0.0105  -0.0463 28  PRO B O   
4310 C CB  . PRO B 28  ? 0.1403 0.2334 0.1219 0.0290  0.0167  -0.0489 28  PRO B CB  
4311 C CG  . PRO B 28  ? 0.1444 0.2486 0.1249 0.0278  0.0155  -0.0364 28  PRO B CG  
4312 C CD  . PRO B 28  ? 0.1884 0.2980 0.1616 0.0233  0.0108  -0.0367 28  PRO B CD  
4313 N N   . TRP B 29  ? 0.1525 0.2227 0.1431 0.0237  0.0052  -0.0397 29  TRP B N   
4314 C CA  . TRP B 29  ? 0.1367 0.1973 0.1352 0.0244  0.0038  -0.0333 29  TRP B CA  
4315 C C   . TRP B 29  ? 0.1739 0.2180 0.1753 0.0244  0.0024  -0.0384 29  TRP B C   
4316 O O   . TRP B 29  ? 0.1634 0.2000 0.1709 0.0260  0.0021  -0.0342 29  TRP B O   
4317 C CB  . TRP B 29  ? 0.1172 0.1816 0.1163 0.0212  0.0010  -0.0272 29  TRP B CB  
4318 C CG  . TRP B 29  ? 0.1483 0.2279 0.1465 0.0220  0.0019  -0.0194 29  TRP B CG  
4319 C CD1 . TRP B 29  ? 0.1717 0.2638 0.1653 0.0197  -0.0005 -0.0178 29  TRP B CD1 
4320 C CD2 . TRP B 29  ? 0.1494 0.2332 0.1518 0.0251  0.0050  -0.0116 29  TRP B CD2 
4321 N NE1 . TRP B 29  ? 0.2301 0.3333 0.2247 0.0218  0.0008  -0.0083 29  TRP B NE1 
4322 C CE2 . TRP B 29  ? 0.1784 0.2759 0.1783 0.0249  0.0046  -0.0046 29  TRP B CE2 
4323 C CE3 . TRP B 29  ? 0.2196 0.2973 0.2281 0.0276  0.0079  -0.0095 29  TRP B CE3 
4324 C CZ2 . TRP B 29  ? 0.2386 0.3418 0.2420 0.0271  0.0076  0.0048  29  TRP B CZ2 
4325 C CZ3 . TRP B 29  ? 0.2472 0.3315 0.2593 0.0291  0.0110  -0.0014 29  TRP B CZ3 
4326 C CH2 . TRP B 29  ? 0.2759 0.3718 0.2853 0.0290  0.0111  0.0058  29  TRP B CH2 
4327 N N   . THR B 30  ? 0.1778 0.2160 0.1749 0.0223  0.0014  -0.0470 30  THR B N   
4328 C CA  . THR B 30  ? 0.1578 0.1792 0.1581 0.0229  0.0003  -0.0507 30  THR B CA  
4329 C C   . THR B 30  ? 0.1645 0.1830 0.1705 0.0289  0.0028  -0.0518 30  THR B C   
4330 O O   . THR B 30  ? 0.1659 0.1752 0.1779 0.0311  0.0013  -0.0482 30  THR B O   
4331 C CB  . THR B 30  ? 0.1782 0.1927 0.1735 0.0191  -0.0005 -0.0601 30  THR B CB  
4332 O OG1 . THR B 30  ? 0.2013 0.2189 0.1932 0.0130  -0.0033 -0.0584 30  THR B OG1 
4333 C CG2 . THR B 30  ? 0.2473 0.2426 0.2466 0.0205  -0.0013 -0.0630 30  THR B CG2 
4334 N N   . PHE B 31  ? 0.1758 0.2037 0.1801 0.0316  0.0066  -0.0567 31  PHE B N   
4335 C CA  . PHE B 31  ? 0.1603 0.1882 0.1718 0.0376  0.0097  -0.0581 31  PHE B CA  
4336 C C   . PHE B 31  ? 0.1391 0.1707 0.1575 0.0395  0.0092  -0.0484 31  PHE B C   
4337 O O   . PHE B 31  ? 0.1718 0.1966 0.1983 0.0429  0.0081  -0.0467 31  PHE B O   
4338 C CB  . PHE B 31  ? 0.1339 0.1742 0.1415 0.0391  0.0149  -0.0646 31  PHE B CB  
4339 C CG  . PHE B 31  ? 0.1655 0.2091 0.1818 0.0453  0.0191  -0.0659 31  PHE B CG  
4340 C CD1 . PHE B 31  ? 0.1687 0.2027 0.1916 0.0499  0.0207  -0.0736 31  PHE B CD1 
4341 C CD2 . PHE B 31  ? 0.1584 0.2147 0.1779 0.0465  0.0215  -0.0590 31  PHE B CD2 
4342 C CE1 . PHE B 31  ? 0.1868 0.2243 0.2188 0.0544  0.0241  -0.0723 31  PHE B CE1 
4343 C CE2 . PHE B 31  ? 0.1649 0.2261 0.1939 0.0518  0.0256  -0.0602 31  PHE B CE2 
4344 C CZ  . PHE B 31  ? 0.1786 0.2302 0.2136 0.0551  0.0264  -0.0659 31  PHE B CZ  
4345 N N   . PHE B 32  ? 0.1503 0.1930 0.1663 0.0374  0.0100  -0.0419 32  PHE B N   
4346 C CA  . PHE B 32  ? 0.1457 0.1922 0.1686 0.0386  0.0106  -0.0339 32  PHE B CA  
4347 C C   . PHE B 32  ? 0.1738 0.2094 0.2004 0.0369  0.0065  -0.0293 32  PHE B C   
4348 O O   . PHE B 32  ? 0.1214 0.1559 0.1551 0.0386  0.0061  -0.0260 32  PHE B O   
4349 C CB  . PHE B 32  ? 0.1071 0.1662 0.1269 0.0367  0.0128  -0.0278 32  PHE B CB  
4350 C CG  . PHE B 32  ? 0.1582 0.2301 0.1756 0.0385  0.0177  -0.0301 32  PHE B CG  
4351 C CD1 . PHE B 32  ? 0.2008 0.2761 0.2253 0.0421  0.0213  -0.0315 32  PHE B CD1 
4352 C CD2 . PHE B 32  ? 0.1971 0.2789 0.2051 0.0363  0.0187  -0.0307 32  PHE B CD2 
4353 C CE1 . PHE B 32  ? 0.1792 0.2671 0.2013 0.0434  0.0268  -0.0340 32  PHE B CE1 
4354 C CE2 . PHE B 32  ? 0.2253 0.3195 0.2293 0.0373  0.0236  -0.0327 32  PHE B CE2 
4355 C CZ  . PHE B 32  ? 0.2353 0.3323 0.2463 0.0408  0.0281  -0.0346 32  PHE B CZ  
4356 N N   . HIS B 33  ? 0.1084 0.1371 0.1302 0.0330  0.0035  -0.0292 33  HIS B N   
4357 C CA  . HIS B 33  ? 0.1186 0.1373 0.1425 0.0308  0.0003  -0.0254 33  HIS B CA  
4358 C C   . HIS B 33  ? 0.1328 0.1395 0.1588 0.0327  -0.0024 -0.0284 33  HIS B C   
4359 O O   . HIS B 33  ? 0.1382 0.1392 0.1673 0.0321  -0.0050 -0.0244 33  HIS B O   
4360 C CB  . HIS B 33  ? 0.1006 0.1170 0.1197 0.0258  -0.0012 -0.0239 33  HIS B CB  
4361 C CG  . HIS B 33  ? 0.1214 0.1474 0.1418 0.0246  0.0007  -0.0184 33  HIS B CG  
4362 N ND1 . HIS B 33  ? 0.1175 0.1437 0.1428 0.0243  0.0018  -0.0130 33  HIS B ND1 
4363 C CD2 . HIS B 33  ? 0.1144 0.1501 0.1322 0.0238  0.0018  -0.0171 33  HIS B CD2 
4364 C CE1 . HIS B 33  ? 0.1168 0.1507 0.1434 0.0237  0.0039  -0.0086 33  HIS B CE1 
4365 N NE2 . HIS B 33  ? 0.1136 0.1539 0.1358 0.0238  0.0036  -0.0103 33  HIS B NE2 
4366 N N   . ALA B 34  ? 0.1312 0.1342 0.1561 0.0349  -0.0017 -0.0352 34  ALA B N   
4367 C CA  . ALA B 34  ? 0.1609 0.1524 0.1903 0.0383  -0.0038 -0.0371 34  ALA B CA  
4368 C C   . ALA B 34  ? 0.1722 0.1691 0.2110 0.0436  -0.0034 -0.0344 34  ALA B C   
4369 O O   . ALA B 34  ? 0.1857 0.1761 0.2292 0.0449  -0.0071 -0.0303 34  ALA B O   
4370 C CB  . ALA B 34  ? 0.1434 0.1292 0.1709 0.0399  -0.0020 -0.0461 34  ALA B CB  
4371 N N   . VAL B 35  ? 0.1451 0.1552 0.1870 0.0464  0.0010  -0.0361 35  VAL B N   
4372 C CA  . VAL B 35  ? 0.1598 0.1765 0.2122 0.0513  0.0018  -0.0343 35  VAL B CA  
4373 C C   . VAL B 35  ? 0.1535 0.1744 0.2087 0.0483  -0.0005 -0.0265 35  VAL B C   
4374 O O   . VAL B 35  ? 0.1385 0.1614 0.2024 0.0508  -0.0026 -0.0237 35  VAL B O   
4375 C CB  . VAL B 35  ? 0.1576 0.1876 0.2127 0.0546  0.0080  -0.0390 35  VAL B CB  
4376 C CG1 . VAL B 35  ? 0.1905 0.2163 0.2417 0.0565  0.0108  -0.0485 35  VAL B CG1 
4377 C CG2 . VAL B 35  ? 0.1825 0.2246 0.2324 0.0506  0.0111  -0.0353 35  VAL B CG2 
4378 N N   . LYS B 36  ? 0.1335 0.1558 0.1821 0.0430  -0.0001 -0.0232 36  LYS B N   
4379 C CA  . LYS B 36  ? 0.1106 0.1362 0.1617 0.0397  -0.0010 -0.0172 36  LYS B CA  
4380 C C   . LYS B 36  ? 0.0989 0.1139 0.1467 0.0358  -0.0058 -0.0142 36  LYS B C   
4381 O O   . LYS B 36  ? 0.1250 0.1408 0.1769 0.0346  -0.0084 -0.0108 36  LYS B O   
4382 C CB  . LYS B 36  ? 0.1257 0.1587 0.1735 0.0366  0.0029  -0.0147 36  LYS B CB  
4383 C CG  . LYS B 36  ? 0.1149 0.1515 0.1672 0.0335  0.0036  -0.0096 36  LYS B CG  
4384 C CD  . LYS B 36  ? 0.1295 0.1729 0.1808 0.0315  0.0081  -0.0062 36  LYS B CD  
4385 C CE  . LYS B 36  ? 0.1242 0.1623 0.1693 0.0283  0.0076  -0.0047 36  LYS B CE  
4386 N NZ  . LYS B 36  ? 0.1080 0.1382 0.1534 0.0241  0.0056  -0.0031 36  LYS B NZ  
4387 N N   . ASP B 37  ? 0.1028 0.1087 0.1429 0.0332  -0.0072 -0.0156 37  ASP B N   
4388 C CA  . ASP B 37  ? 0.1262 0.1239 0.1616 0.0280  -0.0103 -0.0125 37  ASP B CA  
4389 C C   . ASP B 37  ? 0.1217 0.1066 0.1531 0.0275  -0.0142 -0.0133 37  ASP B C   
4390 O O   . ASP B 37  ? 0.1130 0.0918 0.1426 0.0248  -0.0178 -0.0096 37  ASP B O   
4391 C CB  . ASP B 37  ? 0.0934 0.0928 0.1239 0.0235  -0.0077 -0.0120 37  ASP B CB  
4392 C CG  . ASP B 37  ? 0.1411 0.1513 0.1755 0.0240  -0.0036 -0.0101 37  ASP B CG  
4393 O OD1 . ASP B 37  ? 0.1315 0.1448 0.1703 0.0229  -0.0031 -0.0074 37  ASP B OD1 
4394 O OD2 . ASP B 37  ? 0.1272 0.1431 0.1602 0.0253  -0.0010 -0.0114 37  ASP B OD2 
4395 N N   . TYR B 38  ? 0.1391 0.1194 0.1684 0.0293  -0.0133 -0.0180 38  TYR B N   
4396 C CA  . TYR B 38  ? 0.1068 0.0732 0.1315 0.0270  -0.0162 -0.0185 38  TYR B CA  
4397 C C   . TYR B 38  ? 0.1434 0.1019 0.1725 0.0308  -0.0203 -0.0156 38  TYR B C   
4398 O O   . TYR B 38  ? 0.1559 0.1033 0.1808 0.0276  -0.0237 -0.0121 38  TYR B O   
4399 C CB  . TYR B 38  ? 0.1128 0.0759 0.1345 0.0271  -0.0140 -0.0251 38  TYR B CB  
4400 C CG  . TYR B 38  ? 0.1390 0.1095 0.1558 0.0226  -0.0115 -0.0267 38  TYR B CG  
4401 C CD1 . TYR B 38  ? 0.1343 0.1067 0.1485 0.0175  -0.0118 -0.0223 38  TYR B CD1 
4402 C CD2 . TYR B 38  ? 0.1596 0.1364 0.1747 0.0234  -0.0089 -0.0325 38  TYR B CD2 
4403 C CE1 . TYR B 38  ? 0.1586 0.1388 0.1706 0.0143  -0.0096 -0.0231 38  TYR B CE1 
4404 C CE2 . TYR B 38  ? 0.1617 0.1475 0.1733 0.0196  -0.0076 -0.0327 38  TYR B CE2 
4405 C CZ  . TYR B 38  ? 0.1306 0.1177 0.1415 0.0156  -0.0080 -0.0277 38  TYR B CZ  
4406 O OH  . TYR B 38  ? 0.1217 0.1182 0.1313 0.0128  -0.0069 -0.0272 38  TYR B OH  
4407 N N   . TYR B 39  ? 0.1169 0.0812 0.1550 0.0375  -0.0199 -0.0166 39  TYR B N   
4408 C CA  . TYR B 39  ? 0.1230 0.0821 0.1674 0.0417  -0.0246 -0.0123 39  TYR B CA  
4409 C C   . TYR B 39  ? 0.1329 0.0989 0.1780 0.0389  -0.0282 -0.0056 39  TYR B C   
4410 O O   . TYR B 39  ? 0.1567 0.1160 0.2000 0.0376  -0.0336 0.0002  39  TYR B O   
4411 C CB  . TYR B 39  ? 0.1755 0.1394 0.2313 0.0504  -0.0227 -0.0163 39  TYR B CB  
4412 C CG  . TYR B 39  ? 0.2224 0.1845 0.2881 0.0560  -0.0278 -0.0111 39  TYR B CG  
4413 C CD1 . TYR B 39  ? 0.1863 0.1346 0.2520 0.0579  -0.0298 -0.0091 39  TYR B CD1 
4414 C CD2 . TYR B 39  ? 0.1326 0.1083 0.2056 0.0574  -0.0295 -0.0070 39  TYR B CD2 
4415 C CE1 . TYR B 39  ? 0.2164 0.1652 0.2890 0.0618  -0.0336 -0.0027 39  TYR B CE1 
4416 C CE2 . TYR B 39  ? 0.1706 0.1477 0.2505 0.0607  -0.0337 -0.0011 39  TYR B CE2 
4417 C CZ  . TYR B 39  ? 0.2038 0.1677 0.2835 0.0633  -0.0358 0.0012  39  TYR B CZ  
4418 O OH  . TYR B 39  ? 0.2432 0.2090 0.3299 0.0673  -0.0401 0.0077  39  TYR B OH  
4419 N N   . ASP B 40  ? 0.1169 0.0958 0.1638 0.0374  -0.0252 -0.0062 40  ASP B N   
4420 C CA  . ASP B 40  ? 0.1240 0.1109 0.1739 0.0352  -0.0281 -0.0015 40  ASP B CA  
4421 C C   . ASP B 40  ? 0.1321 0.1142 0.1719 0.0270  -0.0302 0.0019  40  ASP B C   
4422 O O   . ASP B 40  ? 0.1319 0.1162 0.1715 0.0246  -0.0348 0.0063  40  ASP B O   
4423 C CB  . ASP B 40  ? 0.1109 0.1120 0.1670 0.0360  -0.0234 -0.0036 40  ASP B CB  
4424 C CG  . ASP B 40  ? 0.1653 0.1749 0.2338 0.0435  -0.0229 -0.0050 40  ASP B CG  
4425 O OD1 . ASP B 40  ? 0.1545 0.1673 0.2301 0.0456  -0.0279 -0.0013 40  ASP B OD1 
4426 O OD2 . ASP B 40  ? 0.1632 0.1763 0.2342 0.0473  -0.0178 -0.0098 40  ASP B OD2 
4427 N N   . MET B 41  ? 0.1124 0.0890 0.1438 0.0225  -0.0270 -0.0002 41  MET B N   
4428 C CA  . MET B 41  ? 0.1203 0.0928 0.1427 0.0146  -0.0279 0.0022  41  MET B CA  
4429 C C   . MET B 41  ? 0.1336 0.0966 0.1506 0.0127  -0.0338 0.0070  41  MET B C   
4430 O O   . MET B 41  ? 0.1216 0.0869 0.1349 0.0083  -0.0370 0.0107  41  MET B O   
4431 C CB  . MET B 41  ? 0.1029 0.0731 0.1199 0.0109  -0.0230 -0.0012 41  MET B CB  
4432 C CG  . MET B 41  ? 0.1086 0.0891 0.1296 0.0107  -0.0178 -0.0032 41  MET B CG  
4433 S SD  . MET B 41  ? 0.1209 0.1060 0.1411 0.0045  -0.0169 -0.0015 41  MET B SD  
4434 C CE  . MET B 41  ? 0.0931 0.0706 0.1038 -0.0027 -0.0149 -0.0023 41  MET B CE  
4435 N N   . PRO B 42  ? 0.1599 0.1119 0.1759 0.0155  -0.0357 0.0076  42  PRO B N   
4436 C CA  . PRO B 42  ? 0.1577 0.1004 0.1694 0.0142  -0.0418 0.0141  42  PRO B CA  
4437 C C   . PRO B 42  ? 0.1955 0.1441 0.2156 0.0197  -0.0475 0.0188  42  PRO B C   
4438 O O   . PRO B 42  ? 0.1974 0.1440 0.2132 0.0171  -0.0535 0.0257  42  PRO B O   
4439 C CB  . PRO B 42  ? 0.1652 0.0938 0.1759 0.0164  -0.0412 0.0127  42  PRO B CB  
4440 C CG  . PRO B 42  ? 0.1956 0.1290 0.2136 0.0217  -0.0362 0.0051  42  PRO B CG  
4441 C CD  . PRO B 42  ? 0.1396 0.0865 0.1572 0.0188  -0.0321 0.0023  42  PRO B CD  
4442 N N   . ALA B 43  ? 0.1712 0.1284 0.2033 0.0270  -0.0458 0.0155  43  ALA B N   
4443 C CA  . ALA B 43  ? 0.1690 0.1336 0.2117 0.0328  -0.0510 0.0197  43  ALA B CA  
4444 C C   . ALA B 43  ? 0.2095 0.1857 0.2502 0.0273  -0.0546 0.0233  43  ALA B C   
4445 O O   . ALA B 43  ? 0.1856 0.1679 0.2329 0.0302  -0.0611 0.0287  43  ALA B O   
4446 C CB  . ALA B 43  ? 0.1723 0.1455 0.2286 0.0410  -0.0470 0.0142  43  ALA B CB  
4447 N N   . TYR B 44  ? 0.1731 0.1527 0.2056 0.0193  -0.0507 0.0203  44  TYR B N   
4448 C CA  . TYR B 44  ? 0.2396 0.2280 0.2683 0.0125  -0.0538 0.0227  44  TYR B CA  
4449 C C   . TYR B 44  ? 0.2047 0.1882 0.2251 0.0091  -0.0618 0.0304  44  TYR B C   
4450 O O   . TYR B 44  ? 0.1983 0.1916 0.2190 0.0061  -0.0674 0.0340  44  TYR B O   
4451 C CB  . TYR B 44  ? 0.1504 0.1392 0.1707 0.0043  -0.0476 0.0179  44  TYR B CB  
4452 C CG  . TYR B 44  ? 0.1684 0.1667 0.1969 0.0053  -0.0414 0.0126  44  TYR B CG  
4453 C CD1 . TYR B 44  ? 0.2092 0.2190 0.2423 0.0018  -0.0419 0.0119  44  TYR B CD1 
4454 C CD2 . TYR B 44  ? 0.1333 0.1292 0.1646 0.0090  -0.0350 0.0085  44  TYR B CD2 
4455 C CE1 . TYR B 44  ? 0.1853 0.2024 0.2260 0.0022  -0.0357 0.0078  44  TYR B CE1 
4456 C CE2 . TYR B 44  ? 0.1307 0.1350 0.1688 0.0098  -0.0295 0.0051  44  TYR B CE2 
4457 C CZ  . TYR B 44  ? 0.1391 0.1532 0.1820 0.0064  -0.0296 0.0050  44  TYR B CZ  
4458 O OH  . TYR B 44  ? 0.1665 0.1874 0.2161 0.0068  -0.0235 0.0024  44  TYR B OH  
4459 N N   . LEU B 45  ? 0.2042 0.1732 0.2169 0.0088  -0.0626 0.0333  45  LEU B N   
4460 C CA  . LEU B 45  ? 0.2025 0.1655 0.2052 0.0048  -0.0697 0.0419  45  LEU B CA  
4461 C C   . LEU B 45  ? 0.1903 0.1569 0.2027 0.0121  -0.0785 0.0499  45  LEU B C   
4462 O O   . LEU B 45  ? 0.2274 0.1932 0.2323 0.0086  -0.0860 0.0585  45  LEU B O   
4463 C CB  . LEU B 45  ? 0.2358 0.1816 0.2290 0.0025  -0.0674 0.0430  45  LEU B CB  
4464 C CG  . LEU B 45  ? 0.2233 0.1666 0.2056 -0.0062 -0.0600 0.0369  45  LEU B CG  
4465 C CD1 . LEU B 45  ? 0.2186 0.1468 0.1963 -0.0069 -0.0567 0.0363  45  LEU B CD1 
4466 C CD2 . LEU B 45  ? 0.2244 0.1720 0.1932 -0.0167 -0.0616 0.0393  45  LEU B CD2 
4467 N N   . LYS B 46  ? 0.2159 0.1877 0.2451 0.0221  -0.0779 0.0476  46  LYS B N   
4468 C CA  . LYS B 46  ? 0.2339 0.2129 0.2746 0.0291  -0.0843 0.0537  46  LYS B CA  
4469 C C   . LYS B 46  ? 0.2589 0.2562 0.3005 0.0244  -0.0893 0.0558  46  LYS B C   
4470 O O   . LYS B 46  ? 0.2622 0.2664 0.3067 0.0263  -0.0946 0.0618  46  LYS B O   
4471 C CB  . LYS B 46  ? 0.2830 0.2652 0.3405 0.0398  -0.0789 0.0481  46  LYS B CB  
4472 C CG  . LYS B 46  ? 0.3892 0.3548 0.4478 0.0455  -0.0746 0.0465  46  LYS B CG  
4473 C CD  . LYS B 46  ? 0.4914 0.4628 0.5650 0.0547  -0.0688 0.0401  46  LYS B CD  
4474 C CE  . LYS B 46  ? 0.6194 0.5753 0.6947 0.0602  -0.0648 0.0382  46  LYS B CE  
4475 N NZ  . LYS B 46  ? 0.6220 0.5844 0.7104 0.0685  -0.0587 0.0317  46  LYS B NZ  
4476 N N   . ASP B 47  ? 0.2067 0.2125 0.2456 0.0178  -0.0858 0.0495  47  ASP B N   
4477 C CA  . ASP B 47  ? 0.2342 0.2579 0.2759 0.0128  -0.0895 0.0495  47  ASP B CA  
4478 C C   . ASP B 47  ? 0.2793 0.3037 0.3030 -0.0002 -0.0903 0.0491  47  ASP B C   
4479 O O   . ASP B 47  ? 0.2585 0.2967 0.2815 -0.0057 -0.0958 0.0506  47  ASP B O   
4480 C CB  . ASP B 47  ? 0.2885 0.3228 0.3423 0.0147  -0.0821 0.0408  47  ASP B CB  
4481 C CG  . ASP B 47  ? 0.3858 0.4235 0.4582 0.0270  -0.0813 0.0405  47  ASP B CG  
4482 O OD1 . ASP B 47  ? 0.3400 0.3783 0.4172 0.0330  -0.0851 0.0457  47  ASP B OD1 
4483 O OD2 . ASP B 47  ? 0.4063 0.4451 0.4849 0.0298  -0.0729 0.0334  47  ASP B OD2 
4484 N N   . PHE B 48  ? 0.2341 0.2446 0.2434 -0.0055 -0.0850 0.0467  48  PHE B N   
4485 C CA  . PHE B 48  ? 0.2846 0.2954 0.2770 -0.0179 -0.0838 0.0448  48  PHE B CA  
4486 C C   . PHE B 48  ? 0.3206 0.3179 0.2977 -0.0214 -0.0864 0.0514  48  PHE B C   
4487 O O   . PHE B 48  ? 0.3279 0.3112 0.3043 -0.0175 -0.0823 0.0512  48  PHE B O   
4488 C CB  . PHE B 48  ? 0.2758 0.2853 0.2670 -0.0222 -0.0729 0.0343  48  PHE B CB  
4489 C CG  . PHE B 48  ? 0.2457 0.2677 0.2510 -0.0199 -0.0700 0.0288  48  PHE B CG  
4490 C CD1 . PHE B 48  ? 0.2962 0.3308 0.3009 -0.0275 -0.0720 0.0264  48  PHE B CD1 
4491 C CD2 . PHE B 48  ? 0.2109 0.2324 0.2297 -0.0109 -0.0652 0.0260  48  PHE B CD2 
4492 C CE1 . PHE B 48  ? 0.3258 0.3716 0.3442 -0.0261 -0.0690 0.0216  48  PHE B CE1 
4493 C CE2 . PHE B 48  ? 0.2381 0.2713 0.2696 -0.0094 -0.0621 0.0217  48  PHE B CE2 
4494 C CZ  . PHE B 48  ? 0.2600 0.3051 0.2918 -0.0170 -0.0640 0.0198  48  PHE B CZ  
4495 N N   . GLU B 49  ? 0.2607 0.2626 0.2253 -0.0291 -0.0933 0.0573  49  GLU B N   
4496 C CA  . GLU B 49  ? 0.3500 0.3403 0.2994 -0.0329 -0.0970 0.0657  49  GLU B CA  
4497 C C   . GLU B 49  ? 0.3411 0.3257 0.2733 -0.0443 -0.0891 0.0595  49  GLU B C   
4498 O O   . GLU B 49  ? 0.3747 0.3637 0.2915 -0.0546 -0.0908 0.0607  49  GLU B O   
4499 C CB  . GLU B 49  ? 0.4463 0.4456 0.3938 -0.0339 -0.1037 0.0730  49  GLU B CB  
4500 C CG  . GLU B 49  ? 0.6203 0.6252 0.5863 -0.0217 -0.1089 0.0779  49  GLU B CG  
4501 C CD  . GLU B 49  ? 0.7156 0.7048 0.6865 -0.0129 -0.1089 0.0840  49  GLU B CD  
4502 O OE1 . GLU B 49  ? 0.6802 0.6578 0.6378 -0.0176 -0.1088 0.0891  49  GLU B OE1 
4503 O OE2 . GLU B 49  ? 0.7918 0.7802 0.7799 -0.0017 -0.1080 0.0829  49  GLU B OE2 
4504 N N   . ILE B 50  ? 0.2719 0.2480 0.2082 -0.0421 -0.0794 0.0519  50  ILE B N   
4505 C CA  . ILE B 50  ? 0.2849 0.2543 0.2090 -0.0505 -0.0708 0.0459  50  ILE B CA  
4506 C C   . ILE B 50  ? 0.3641 0.3185 0.2899 -0.0459 -0.0671 0.0473  50  ILE B C   
4507 O O   . ILE B 50  ? 0.2917 0.2405 0.2273 -0.0367 -0.0710 0.0521  50  ILE B O   
4508 C CB  . ILE B 50  ? 0.2775 0.2538 0.2066 -0.0532 -0.0620 0.0341  50  ILE B CB  
4509 C CG1 . ILE B 50  ? 0.3417 0.3175 0.2887 -0.0426 -0.0584 0.0302  50  ILE B CG1 
4510 C CG2 . ILE B 50  ? 0.3102 0.3005 0.2372 -0.0594 -0.0652 0.0316  50  ILE B CG2 
4511 C CD1 . ILE B 50  ? 0.3282 0.3071 0.2802 -0.0442 -0.0489 0.0203  50  ILE B CD1 
4512 N N   . LYS B 51  ? 0.2361 0.1845 0.1533 -0.0525 -0.0593 0.0425  51  LYS B N   
4513 C CA  . LYS B 51  ? 0.2631 0.1989 0.1821 -0.0499 -0.0549 0.0420  51  LYS B CA  
4514 C C   . LYS B 51  ? 0.2456 0.1839 0.1744 -0.0472 -0.0461 0.0318  51  LYS B C   
4515 O O   . LYS B 51  ? 0.2309 0.1760 0.1576 -0.0524 -0.0402 0.0250  51  LYS B O   
4516 C CB  . LYS B 51  ? 0.2700 0.1979 0.1728 -0.0597 -0.0524 0.0449  51  LYS B CB  
4517 C CG  . LYS B 51  ? 0.3185 0.2445 0.2070 -0.0653 -0.0603 0.0559  51  LYS B CG  
4518 C CD  . LYS B 51  ? 0.3161 0.2333 0.2103 -0.0572 -0.0687 0.0664  51  LYS B CD  
4519 C CE  . LYS B 51  ? 0.3841 0.3016 0.2666 -0.0622 -0.0755 0.0770  51  LYS B CE  
4520 N NZ  . LYS B 51  ? 0.4555 0.3672 0.3493 -0.0521 -0.0819 0.0852  51  LYS B NZ  
4521 N N   . LEU B 52  ? 0.1800 0.1126 0.1191 -0.0392 -0.0450 0.0307  52  LEU B N   
4522 C CA  . LEU B 52  ? 0.1646 0.0996 0.1125 -0.0363 -0.0376 0.0225  52  LEU B CA  
4523 C C   . LEU B 52  ? 0.2405 0.1648 0.1896 -0.0342 -0.0360 0.0225  52  LEU B C   
4524 O O   . LEU B 52  ? 0.2143 0.1304 0.1654 -0.0297 -0.0408 0.0274  52  LEU B O   
4525 C CB  . LEU B 52  ? 0.1719 0.1152 0.1335 -0.0278 -0.0381 0.0195  52  LEU B CB  
4526 C CG  . LEU B 52  ? 0.2188 0.1734 0.1826 -0.0289 -0.0398 0.0188  52  LEU B CG  
4527 C CD1 . LEU B 52  ? 0.2275 0.1887 0.2057 -0.0198 -0.0406 0.0173  52  LEU B CD1 
4528 C CD2 . LEU B 52  ? 0.2318 0.1913 0.1921 -0.0360 -0.0326 0.0124  52  LEU B CD2 
4529 N N   . ASN B 53  ? 0.1843 0.1091 0.1339 -0.0373 -0.0291 0.0168  53  ASN B N   
4530 C CA  . ASN B 53  ? 0.2046 0.1206 0.1550 -0.0370 -0.0275 0.0159  53  ASN B CA  
4531 C C   . ASN B 53  ? 0.2079 0.1291 0.1694 -0.0309 -0.0240 0.0094  53  ASN B C   
4532 O O   . ASN B 53  ? 0.1698 0.1013 0.1371 -0.0285 -0.0211 0.0057  53  ASN B O   
4533 C CB  . ASN B 53  ? 0.1706 0.0838 0.1119 -0.0468 -0.0229 0.0153  53  ASN B CB  
4534 C CG  . ASN B 53  ? 0.2399 0.1497 0.1680 -0.0541 -0.0257 0.0217  53  ASN B CG  
4535 O OD1 . ASN B 53  ? 0.2424 0.1422 0.1651 -0.0545 -0.0309 0.0289  53  ASN B OD1 
4536 N ND2 . ASN B 53  ? 0.2261 0.1445 0.1491 -0.0593 -0.0227 0.0192  53  ASN B ND2 
4537 N N   . PHE B 54  ? 0.1879 0.1016 0.1520 -0.0287 -0.0242 0.0082  54  PHE B N   
4538 C CA  . PHE B 54  ? 0.2130 0.1317 0.1862 -0.0229 -0.0220 0.0024  54  PHE B CA  
4539 C C   . PHE B 54  ? 0.1945 0.1084 0.1669 -0.0267 -0.0194 -0.0011 54  PHE B C   
4540 O O   . PHE B 54  ? 0.2489 0.1511 0.2160 -0.0310 -0.0208 0.0015  54  PHE B O   
4541 C CB  . PHE B 54  ? 0.1871 0.1033 0.1667 -0.0142 -0.0258 0.0030  54  PHE B CB  
4542 C CG  . PHE B 54  ? 0.1897 0.1126 0.1720 -0.0105 -0.0286 0.0062  54  PHE B CG  
4543 C CD1 . PHE B 54  ? 0.1567 0.0920 0.1458 -0.0068 -0.0261 0.0029  54  PHE B CD1 
4544 C CD2 . PHE B 54  ? 0.1961 0.1139 0.1742 -0.0115 -0.0338 0.0130  54  PHE B CD2 
4545 C CE1 . PHE B 54  ? 0.1923 0.1344 0.1844 -0.0046 -0.0284 0.0054  54  PHE B CE1 
4546 C CE2 . PHE B 54  ? 0.2290 0.1552 0.2101 -0.0090 -0.0369 0.0156  54  PHE B CE2 
4547 C CZ  . PHE B 54  ? 0.2116 0.1499 0.2000 -0.0058 -0.0339 0.0112  54  PHE B CZ  
4548 N N   . ASN B 55  ? 0.1565 0.0801 0.1344 -0.0255 -0.0159 -0.0065 55  ASN B N   
4549 C CA  . ASN B 55  ? 0.1633 0.0858 0.1425 -0.0282 -0.0141 -0.0110 55  ASN B CA  
4550 C C   . ASN B 55  ? 0.1953 0.1207 0.1804 -0.0214 -0.0150 -0.0155 55  ASN B C   
4551 O O   . ASN B 55  ? 0.1768 0.1124 0.1665 -0.0159 -0.0143 -0.0163 55  ASN B O   
4552 C CB  . ASN B 55  ? 0.1546 0.0887 0.1361 -0.0325 -0.0097 -0.0136 55  ASN B CB  
4553 C CG  . ASN B 55  ? 0.2313 0.1653 0.2139 -0.0372 -0.0085 -0.0177 55  ASN B CG  
4554 O OD1 . ASN B 55  ? 0.2075 0.1305 0.1854 -0.0429 -0.0090 -0.0169 55  ASN B OD1 
4555 N ND2 . ASN B 55  ? 0.1479 0.0945 0.1369 -0.0349 -0.0072 -0.0218 55  ASN B ND2 
4556 N N   . LEU B 56  ? 0.1786 0.0945 0.1630 -0.0222 -0.0160 -0.0186 56  LEU B N   
4557 C CA  . LEU B 56  ? 0.1925 0.1113 0.1812 -0.0172 -0.0159 -0.0248 56  LEU B CA  
4558 C C   . LEU B 56  ? 0.2228 0.1428 0.2108 -0.0232 -0.0144 -0.0305 56  LEU B C   
4559 O O   . LEU B 56  ? 0.2516 0.1594 0.2365 -0.0291 -0.0147 -0.0308 56  LEU B O   
4560 C CB  . LEU B 56  ? 0.2278 0.1333 0.2178 -0.0121 -0.0182 -0.0250 56  LEU B CB  
4561 C CG  . LEU B 56  ? 0.3028 0.2068 0.2951 -0.0056 -0.0207 -0.0194 56  LEU B CG  
4562 C CD1 . LEU B 56  ? 0.4082 0.2988 0.4040 -0.0003 -0.0226 -0.0204 56  LEU B CD1 
4563 C CD2 . LEU B 56  ? 0.3205 0.2405 0.3173 -0.0003 -0.0194 -0.0204 56  LEU B CD2 
4564 N N   . THR B 57  ? 0.1740 0.1088 0.1649 -0.0222 -0.0131 -0.0348 57  THR B N   
4565 C CA  . THR B 57  ? 0.1459 0.0838 0.1366 -0.0281 -0.0125 -0.0407 57  THR B CA  
4566 C C   . THR B 57  ? 0.1591 0.0864 0.1487 -0.0272 -0.0132 -0.0475 57  THR B C   
4567 O O   . THR B 57  ? 0.2161 0.1410 0.2069 -0.0200 -0.0135 -0.0488 57  THR B O   
4568 C CB  . THR B 57  ? 0.2110 0.1693 0.2051 -0.0274 -0.0117 -0.0425 57  THR B CB  
4569 O OG1 . THR B 57  ? 0.1743 0.1396 0.1693 -0.0203 -0.0120 -0.0444 57  THR B OG1 
4570 C CG2 . THR B 57  ? 0.1716 0.1390 0.1687 -0.0276 -0.0101 -0.0364 57  THR B CG2 
4571 N N   . PRO B 58  ? 0.1629 0.0904 0.1908 -0.0246 -0.0246 -0.0365 58  PRO B N   
4572 C CA  . PRO B 58  ? 0.1865 0.1010 0.2049 -0.0292 -0.0207 -0.0476 58  PRO B CA  
4573 C C   . PRO B 58  ? 0.2254 0.1438 0.2348 -0.0341 -0.0220 -0.0544 58  PRO B C   
4574 O O   . PRO B 58  ? 0.2005 0.1098 0.2054 -0.0318 -0.0195 -0.0608 58  PRO B O   
4575 C CB  . PRO B 58  ? 0.2346 0.1409 0.2459 -0.0363 -0.0204 -0.0521 58  PRO B CB  
4576 C CG  . PRO B 58  ? 0.1832 0.0966 0.2059 -0.0311 -0.0220 -0.0424 58  PRO B CG  
4577 C CD  . PRO B 58  ? 0.1843 0.1124 0.2136 -0.0262 -0.0259 -0.0337 58  PRO B CD  
4578 N N   . VAL B 59  ? 0.1957 0.1291 0.2025 -0.0400 -0.0260 -0.0526 59  VAL B N   
4579 C CA  . VAL B 59  ? 0.2150 0.1572 0.2137 -0.0448 -0.0301 -0.0578 59  VAL B CA  
4580 C C   . VAL B 59  ? 0.1994 0.1461 0.2059 -0.0372 -0.0287 -0.0570 59  VAL B C   
4581 O O   . VAL B 59  ? 0.1964 0.1471 0.2036 -0.0359 -0.0294 -0.0678 59  VAL B O   
4582 C CB  . VAL B 59  ? 0.1963 0.1588 0.1933 -0.0521 -0.0377 -0.0532 59  VAL B CB  
4583 C CG1 . VAL B 59  ? 0.2176 0.1940 0.2246 -0.0487 -0.0338 -0.0431 59  VAL B CG1 
4584 C CG2 . VAL B 59  ? 0.1685 0.1509 0.1691 -0.0522 -0.0435 -0.0626 59  VAL B CG2 
4585 N N   . LEU B 60  ? 0.1675 0.1155 0.1823 -0.0309 -0.0269 -0.0462 60  LEU B N   
4586 C CA  . LEU B 60  ? 0.1370 0.0866 0.1607 -0.0238 -0.0282 -0.0451 60  LEU B CA  
4587 C C   . LEU B 60  ? 0.1691 0.1046 0.1939 -0.0187 -0.0237 -0.0513 60  LEU B C   
4588 O O   . LEU B 60  ? 0.1889 0.1267 0.2194 -0.0145 -0.0241 -0.0597 60  LEU B O   
4589 C CB  . LEU B 60  ? 0.1434 0.0952 0.1715 -0.0195 -0.0281 -0.0310 60  LEU B CB  
4590 C CG  . LEU B 60  ? 0.1421 0.0943 0.1778 -0.0147 -0.0305 -0.0284 60  LEU B CG  
4591 C CD1 . LEU B 60  ? 0.1591 0.1228 0.1987 -0.0162 -0.0368 -0.0358 60  LEU B CD1 
4592 C CD2 . LEU B 60  ? 0.1540 0.1084 0.1890 -0.0129 -0.0297 -0.0148 60  LEU B CD2 
4593 N N   . ILE B 61  ? 0.1681 0.0907 0.1894 -0.0177 -0.0192 -0.0485 61  ILE B N   
4594 C CA  . ILE B 61  ? 0.2539 0.1611 0.2741 -0.0118 -0.0137 -0.0523 61  ILE B CA  
4595 C C   . ILE B 61  ? 0.3234 0.2221 0.3356 -0.0126 -0.0107 -0.0672 61  ILE B C   
4596 O O   . ILE B 61  ? 0.2241 0.1176 0.2409 -0.0047 -0.0059 -0.0734 61  ILE B O   
4597 C CB  . ILE B 61  ? 0.2032 0.1013 0.2268 -0.0105 -0.0118 -0.0495 61  ILE B CB  
4598 C CG1 . ILE B 61  ? 0.1585 0.0690 0.1948 -0.0076 -0.0158 -0.0374 61  ILE B CG1 
4599 C CG2 . ILE B 61  ? 0.2071 0.0862 0.2262 -0.0039 -0.0051 -0.0537 61  ILE B CG2 
4600 C CD1 . ILE B 61  ? 0.2251 0.1318 0.2650 -0.0076 -0.0156 -0.0348 61  ILE B CD1 
4601 N N   . ASP B 62  ? 0.2049 0.1045 0.2066 -0.0215 -0.0132 -0.0738 62  ASP B N   
4602 C CA  . ASP B 62  ? 0.2737 0.1692 0.2679 -0.0235 -0.0103 -0.0898 62  ASP B CA  
4603 C C   . ASP B 62  ? 0.3049 0.2170 0.3065 -0.0197 -0.0088 -0.0983 62  ASP B C   
4604 O O   . ASP B 62  ? 0.2572 0.1615 0.2544 -0.0149 -0.0007 -0.1093 62  ASP B O   
4605 C CB  . ASP B 62  ? 0.2786 0.1812 0.2640 -0.0349 -0.0158 -0.0947 62  ASP B CB  
4606 C CG  . ASP B 62  ? 0.3549 0.2399 0.3335 -0.0380 -0.0164 -0.0934 62  ASP B CG  
4607 O OD1 . ASP B 62  ? 0.3626 0.2286 0.3419 -0.0316 -0.0104 -0.0941 62  ASP B OD1 
4608 O OD2 . ASP B 62  ? 0.3500 0.2451 0.3284 -0.0466 -0.0221 -0.0940 62  ASP B OD2 
4609 N N   . GLN B 63  ? 0.2423 0.1775 0.2528 -0.0212 -0.0162 -0.0933 63  GLN B N   
4610 C CA  . GLN B 63  ? 0.2755 0.2313 0.2902 -0.0178 -0.0168 -0.1016 63  GLN B CA  
4611 C C   . GLN B 63  ? 0.2042 0.1538 0.2303 -0.0049 -0.0131 -0.1007 63  GLN B C   
4612 O O   . GLN B 63  ? 0.2525 0.2083 0.2770 0.0020  -0.0071 -0.1112 63  GLN B O   
4613 C CB  . GLN B 63  ? 0.1839 0.1670 0.2017 -0.0224 -0.0267 -0.0944 63  GLN B CB  
4614 C CG  . GLN B 63  ? 0.2289 0.2197 0.2392 -0.0324 -0.0306 -0.0902 63  GLN B CG  
4615 C CD  . GLN B 63  ? 0.3016 0.3175 0.3150 -0.0341 -0.0379 -0.0788 63  GLN B CD  
4616 O OE1 . GLN B 63  ? 0.3004 0.3405 0.3138 -0.0319 -0.0395 -0.0792 63  GLN B OE1 
4617 N NE2 . GLN B 63  ? 0.1938 0.2028 0.2087 -0.0367 -0.0409 -0.0663 63  GLN B NE2 
4618 N N   . ILE B 64  ? 0.2117 0.1516 0.2482 -0.0007 -0.0157 -0.0866 64  ILE B N   
4619 C CA  . ILE B 64  ? 0.1770 0.1127 0.2256 0.0123  -0.0120 -0.0827 64  ILE B CA  
4620 C C   . ILE B 64  ? 0.2169 0.1361 0.2600 0.0210  0.0019  -0.0901 64  ILE B C   
4621 O O   . ILE B 64  ? 0.2627 0.1894 0.3099 0.0332  0.0091  -0.0909 64  ILE B O   
4622 C CB  . ILE B 64  ? 0.2760 0.2050 0.3332 0.0124  -0.0163 -0.0647 64  ILE B CB  
4623 C CG1 . ILE B 64  ? 0.2001 0.1436 0.2597 0.0049  -0.0273 -0.0548 64  ILE B CG1 
4624 C CG2 . ILE B 64  ? 0.1886 0.1150 0.2581 0.0263  -0.0104 -0.0572 64  ILE B CG2 
4625 C CD1 . ILE B 64  ? 0.1699 0.1094 0.2312 0.0019  -0.0293 -0.0375 64  ILE B CD1 
4626 N N   . GLN B 65  ? 0.2350 0.1342 0.2641 0.0152  0.0065  -0.0910 65  GLN B N   
4627 C CA  . GLN B 65  ? 0.3005 0.1787 0.3187 0.0229  0.0191  -0.0972 65  GLN B CA  
4628 C C   . GLN B 65  ? 0.3336 0.2178 0.3435 0.0239  0.0262  -0.1128 65  GLN B C   
4629 O O   . GLN B 65  ? 0.3008 0.1777 0.3089 0.0370  0.0381  -0.1152 65  GLN B O   
4630 C CB  . GLN B 65  ? 0.3349 0.1925 0.3379 0.0155  0.0183  -0.0975 65  GLN B CB  
4631 C CG  . GLN B 65  ? 0.4535 0.3002 0.4592 0.0208  0.0170  -0.0835 65  GLN B CG  
4632 C CD  . GLN B 65  ? 0.5834 0.4153 0.5756 0.0132  0.0131  -0.0837 65  GLN B CD  
4633 O OE1 . GLN B 65  ? 0.5697 0.4042 0.5542 0.0018  0.0085  -0.0899 65  GLN B OE1 
4634 N NE2 . GLN B 65  ? 0.6700 0.4903 0.6652 0.0198  0.0153  -0.0782 65  GLN B NE2 
4635 N N   . GLU B 66  ? 0.2877 0.1882 0.2910 0.0109  0.0196  -0.1219 66  GLU B N   
4636 C CA  . GLU B 66  ? 0.3112 0.2216 0.3030 0.0094  0.0257  -0.1362 66  GLU B CA  
4637 C C   . GLU B 66  ? 0.2867 0.2182 0.2888 0.0226  0.0289  -0.1366 66  GLU B C   
4638 O O   . GLU B 66  ? 0.3142 0.2422 0.3088 0.0314  0.0412  -0.1427 66  GLU B O   
4639 C CB  . GLU B 66  ? 0.3395 0.2709 0.3234 -0.0073 0.0161  -0.1420 66  GLU B CB  
4640 C CG  . GLU B 66  ? 0.4447 0.3880 0.4140 -0.0118 0.0217  -0.1557 66  GLU B CG  
4641 C CD  . GLU B 66  ? 0.5317 0.4947 0.4927 -0.0287 0.0136  -0.1590 66  GLU B CD  
4642 O OE1 . GLU B 66  ? 0.3838 0.3508 0.3505 -0.0353 0.0043  -0.1503 66  GLU B OE1 
4643 O OE2 . GLU B 66  ? 0.6238 0.5993 0.5726 -0.0346 0.0173  -0.1691 66  GLU B OE2 
4644 N N   . TYR B 67  ? 0.2443 0.1997 0.2602 0.0243  0.0173  -0.1230 67  TYR B N   
4645 C CA  . TYR B 67  ? 0.2328 0.2133 0.2548 0.0356  0.0176  -0.1099 67  TYR B CA  
4646 C C   . TYR B 67  ? 0.2573 0.2246 0.2875 0.0529  0.0295  -0.1026 67  TYR B C   
4647 O O   . TYR B 67  ? 0.2608 0.2407 0.2903 0.0643  0.0377  -0.1002 67  TYR B O   
4648 C CB  . TYR B 67  ? 0.2303 0.2342 0.2618 0.0315  0.0037  -0.0915 67  TYR B CB  
4649 C CG  . TYR B 67  ? 0.2125 0.2411 0.2367 0.0206  -0.0053 -0.0925 67  TYR B CG  
4650 C CD1 . TYR B 67  ? 0.1948 0.2516 0.2155 0.0237  -0.0052 -0.0896 67  TYR B CD1 
4651 C CD2 . TYR B 67  ? 0.2276 0.2532 0.2493 0.0086  -0.0131 -0.0946 67  TYR B CD2 
4652 C CE1 . TYR B 67  ? 0.1839 0.2643 0.1987 0.0152  -0.0122 -0.0886 67  TYR B CE1 
4653 C CE2 . TYR B 67  ? 0.1685 0.2191 0.1847 0.0009  -0.0198 -0.0925 67  TYR B CE2 
4654 C CZ  . TYR B 67  ? 0.2514 0.3288 0.2641 0.0044  -0.0192 -0.0895 67  TYR B CZ  
4655 O OH  . TYR B 67  ? 0.1771 0.2797 0.1848 -0.0023 -0.0249 -0.0857 67  TYR B OH  
4656 N N   . ALA B 68  ? 0.2591 0.2031 0.2977 0.0558  0.0311  -0.0975 68  ALA B N   
4657 C CA  . ALA B 68  ? 0.2560 0.1913 0.3045 0.0736  0.0427  -0.0868 68  ALA B CA  
4658 C C   . ALA B 68  ? 0.3407 0.2547 0.3779 0.0844  0.0623  -0.0998 68  ALA B C   
4659 O O   . ALA B 68  ? 0.3268 0.2457 0.3694 0.1021  0.0732  -0.0893 68  ALA B O   
4660 C CB  . ALA B 68  ? 0.2512 0.1647 0.3096 0.0738  0.0411  -0.0797 68  ALA B CB  
4661 N N   . GLN B 69  ? 0.3823 0.2769 0.3976 0.0716  0.0632  -0.1154 69  GLN B N   
4662 C CA  . GLN B 69  ? 0.3597 0.2351 0.3570 0.0770  0.0764  -0.1248 69  GLN B CA  
4663 C C   . GLN B 69  ? 0.4446 0.3370 0.4331 0.0785  0.0831  -0.1349 69  GLN B C   
4664 O O   . GLN B 69  ? 0.5239 0.4016 0.4972 0.0827  0.0943  -0.1434 69  GLN B O   
4665 C CB  . GLN B 69  ? 0.5417 0.3919 0.5217 0.0612  0.0736  -0.1358 69  GLN B CB  
4666 C CG  . GLN B 69  ? 0.6045 0.4385 0.5911 0.0607  0.0683  -0.1261 69  GLN B CG  
4667 C CD  . GLN B 69  ? 0.7362 0.5514 0.7085 0.0454  0.0653  -0.1359 69  GLN B CD  
4668 O OE1 . GLN B 69  ? 0.7872 0.6011 0.7448 0.0344  0.0675  -0.1498 69  GLN B OE1 
4669 N NE2 . GLN B 69  ? 0.8496 0.6534 0.8267 0.0442  0.0601  -0.1279 69  GLN B NE2 
4670 N N   . GLY B 70  ? 0.4056 0.3330 0.4053 0.0754  0.0747  -0.1349 70  GLY B N   
4671 C CA  . GLY B 70  ? 0.4118 0.3616 0.4017 0.0751  0.0773  -0.1431 70  GLY B CA  
4672 C C   . GLY B 70  ? 0.4945 0.4390 0.4624 0.0556  0.0743  -0.1606 70  GLY B C   
4673 O O   . GLY B 70  ? 0.5100 0.4680 0.4659 0.0544  0.0785  -0.1684 70  GLY B O   
4674 N N   . LYS B 71  ? 0.4839 0.4127 0.4469 0.0399  0.0661  -0.1637 71  LYS B N   
4675 C CA  . LYS B 71  ? 0.5273 0.4559 0.4721 0.0205  0.0619  -0.1761 71  LYS B CA  
4676 C C   . LYS B 71  ? 0.5276 0.4955 0.4766 0.0075  0.0463  -0.1762 71  LYS B C   
4677 O O   . LYS B 71  ? 0.5375 0.5171 0.4735 -0.0064 0.0435  -0.1841 71  LYS B O   
4678 C CB  . LYS B 71  ? 0.5929 0.4923 0.5322 0.0110  0.0602  -0.1768 71  LYS B CB  
4679 C CG  . LYS B 71  ? 0.7244 0.5881 0.6525 0.0192  0.0747  -0.1811 71  LYS B CG  
4680 C CD  . LYS B 71  ? 0.7996 0.6407 0.7273 0.0116  0.0711  -0.1795 71  LYS B CD  
4681 C CE  . LYS B 71  ? 0.8464 0.6944 0.7629 -0.0105 0.0640  -0.1892 71  LYS B CE  
4682 N NZ  . LYS B 71  ? 0.9315 0.7687 0.8287 -0.0175 0.0752  -0.2047 71  LYS B NZ  
4683 N N   . ALA B 72  ? 0.4419 0.4320 0.4084 0.0125  0.0360  -0.1662 72  ALA B N   
4684 C CA  . ALA B 72  ? 0.3565 0.3807 0.3253 0.0014  0.0208  -0.1625 72  ALA B CA  
4685 C C   . ALA B 72  ? 0.3739 0.4324 0.3362 0.0025  0.0200  -0.1634 72  ALA B C   
4686 O O   . ALA B 72  ? 0.3756 0.4439 0.3439 0.0161  0.0235  -0.1538 72  ALA B O   
4687 C CB  . ALA B 72  ? 0.3251 0.3557 0.3119 0.0063  0.0098  -0.1413 72  ALA B CB  
4688 N N   . LYS B 73  ? 0.3216 0.3984 0.2741 -0.0119 0.0149  -0.1672 73  LYS B N   
4689 C CA  . LYS B 73  ? 0.3015 0.4132 0.2484 -0.0129 0.0130  -0.1664 73  LYS B CA  
4690 C C   . LYS B 73  ? 0.2464 0.3920 0.2027 -0.0151 -0.0006 -0.1506 73  LYS B C   
4691 O O   . LYS B 73  ? 0.3501 0.5084 0.3068 -0.0263 -0.0070 -0.1454 73  LYS B O   
4692 C CB  . LYS B 73  ? 0.3537 0.4648 0.2858 -0.0266 0.0171  -0.1772 73  LYS B CB  
4693 C CG  . LYS B 73  ? 0.4953 0.5674 0.4139 -0.0256 0.0319  -0.1914 73  LYS B CG  
4694 C CD  . LYS B 73  ? 0.5492 0.6231 0.4509 -0.0413 0.0351  -0.2026 73  LYS B CD  
4695 C CE  . LYS B 73  ? 0.5982 0.6706 0.5003 -0.0572 0.0282  -0.2021 73  LYS B CE  
4696 N NZ  . LYS B 73  ? 0.7130 0.7880 0.5989 -0.0734 0.0325  -0.2139 73  LYS B NZ  
4697 N N   . ASP B 74  ? 0.2416 0.3989 0.2074 -0.0033 -0.0034 -0.1369 74  ASP B N   
4698 C CA  . ASP B 74  ? 0.1999 0.3777 0.1750 -0.0037 -0.0138 -0.1171 74  ASP B CA  
4699 C C   . ASP B 74  ? 0.2148 0.4287 0.1863 -0.0012 -0.0149 -0.1113 74  ASP B C   
4700 O O   . ASP B 74  ? 0.2270 0.4456 0.2001 0.0086  -0.0101 -0.1085 74  ASP B O   
4701 C CB  . ASP B 74  ? 0.1796 0.3384 0.1685 0.0049  -0.0148 -0.1020 74  ASP B CB  
4702 C CG  . ASP B 74  ? 0.2819 0.4541 0.2776 0.0040  -0.0226 -0.0819 74  ASP B CG  
4703 O OD1 . ASP B 74  ? 0.2373 0.4374 0.2295 0.0026  -0.0251 -0.0752 74  ASP B OD1 
4704 O OD2 . ASP B 74  ? 0.3083 0.4608 0.3121 0.0046  -0.0249 -0.0725 74  ASP B OD2 
4705 N N   . VAL B 75  ? 0.2059 0.4407 0.1780 -0.0086 -0.0187 -0.1035 75  VAL B N   
4706 C CA  . VAL B 75  ? 0.1897 0.4544 0.1613 -0.0069 -0.0170 -0.0974 75  VAL B CA  
4707 C C   . VAL B 75  ? 0.2466 0.5221 0.2247 0.0026  -0.0180 -0.0803 75  VAL B C   
4708 O O   . VAL B 75  ? 0.2220 0.5138 0.1990 0.0084  -0.0151 -0.0799 75  VAL B O   
4709 C CB  . VAL B 75  ? 0.2675 0.5506 0.2401 -0.0157 -0.0181 -0.0916 75  VAL B CB  
4710 C CG1 . VAL B 75  ? 0.3139 0.5881 0.2784 -0.0273 -0.0165 -0.1086 75  VAL B CG1 
4711 C CG2 . VAL B 75  ? 0.3191 0.5994 0.2985 -0.0154 -0.0213 -0.0736 75  VAL B CG2 
4712 N N   A PHE B 76  ? 0.2158 0.4800 0.2001 0.0033  -0.0212 -0.0653 76  PHE B N   
4713 N N   B PHE B 76  ? 0.2181 0.4821 0.2024 0.0033  -0.0212 -0.0656 76  PHE B N   
4714 C CA  A PHE B 76  ? 0.2307 0.4979 0.2193 0.0091  -0.0202 -0.0486 76  PHE B CA  
4715 C CA  B PHE B 76  ? 0.2304 0.4980 0.2190 0.0092  -0.0201 -0.0489 76  PHE B CA  
4716 C C   A PHE B 76  ? 0.2474 0.5136 0.2365 0.0162  -0.0204 -0.0529 76  PHE B C   
4717 C C   B PHE B 76  ? 0.2468 0.5130 0.2360 0.0162  -0.0205 -0.0528 76  PHE B C   
4718 O O   A PHE B 76  ? 0.2407 0.5206 0.2312 0.0211  -0.0176 -0.0446 76  PHE B O   
4719 O O   B PHE B 76  ? 0.2398 0.5190 0.2305 0.0210  -0.0177 -0.0441 76  PHE B O   
4720 C CB  A PHE B 76  ? 0.2208 0.4687 0.2130 0.0065  -0.0218 -0.0335 76  PHE B CB  
4721 C CB  B PHE B 76  ? 0.2224 0.4718 0.2144 0.0065  -0.0215 -0.0334 76  PHE B CB  
4722 C CG  A PHE B 76  ? 0.2359 0.4916 0.2271 0.0040  -0.0190 -0.0221 76  PHE B CG  
4723 C CG  B PHE B 76  ? 0.2141 0.4637 0.2071 0.0090  -0.0180 -0.0171 76  PHE B CG  
4724 C CD1 A PHE B 76  ? 0.2049 0.4670 0.1950 -0.0008 -0.0201 -0.0272 76  PHE B CD1 
4725 C CD1 B PHE B 76  ? 0.1947 0.4596 0.1866 0.0095  -0.0130 -0.0073 76  PHE B CD1 
4726 C CD2 A PHE B 76  ? 0.2035 0.4622 0.1951 0.0061  -0.0145 -0.0059 76  PHE B CD2 
4727 C CD2 B PHE B 76  ? 0.1897 0.4268 0.1853 0.0100  -0.0190 -0.0120 76  PHE B CD2 
4728 C CE1 A PHE B 76  ? 0.2335 0.5085 0.2241 -0.0014 -0.0169 -0.0150 76  PHE B CE1 
4729 C CE1 B PHE B 76  ? 0.1989 0.4637 0.1916 0.0103  -0.0089 0.0059  76  PHE B CE1 
4730 C CE2 A PHE B 76  ? 0.2226 0.4917 0.2148 0.0058  -0.0107 0.0050  76  PHE B CE2 
4731 C CE2 B PHE B 76  ? 0.2124 0.4498 0.2073 0.0091  -0.0149 0.0018  76  PHE B CE2 
4732 C CZ  A PHE B 76  ? 0.2258 0.5045 0.2178 0.0029  -0.0120 0.0011  76  PHE B CZ  
4733 C CZ  B PHE B 76  ? 0.1671 0.4174 0.1603 0.0091  -0.0098 0.0099  76  PHE B CZ  
4734 N N   . LEU B 77  ? 0.2149 0.4561 0.2068 0.0173  -0.0192 -0.0623 77  LEU B N   
4735 C CA  . LEU B 77  ? 0.1718 0.4037 0.1694 0.0259  -0.0144 -0.0612 77  LEU B CA  
4736 C C   . LEU B 77  ? 0.2292 0.4771 0.2211 0.0327  -0.0078 -0.0708 77  LEU B C   
4737 O O   . LEU B 77  ? 0.2411 0.4974 0.2375 0.0411  -0.0041 -0.0638 77  LEU B O   
4738 C CB  . LEU B 77  ? 0.2598 0.4597 0.2624 0.0270  -0.0123 -0.0674 77  LEU B CB  
4739 C CG  . LEU B 77  ? 0.3308 0.5211 0.3428 0.0361  -0.0083 -0.0596 77  LEU B CG  
4740 C CD1 . LEU B 77  ? 0.3075 0.5095 0.3253 0.0337  -0.0134 -0.0401 77  LEU B CD1 
4741 C CD2 . LEU B 77  ? 0.3874 0.5461 0.4038 0.0365  -0.0065 -0.0649 77  LEU B CD2 
4742 N N   . GLU B 78  ? 0.2720 0.5266 0.2532 0.0282  -0.0059 -0.0864 78  GLU B N   
4743 C CA  . GLU B 78  ? 0.2778 0.5492 0.2510 0.0333  0.0008  -0.0956 78  GLU B CA  
4744 C C   . GLU B 78  ? 0.2723 0.5771 0.2465 0.0357  -0.0022 -0.0825 78  GLU B C   
4745 O O   . GLU B 78  ? 0.3080 0.6256 0.2817 0.0440  0.0031  -0.0818 78  GLU B O   
4746 C CB  . GLU B 78  ? 0.3839 0.6553 0.3432 0.0243  0.0033  -0.1155 78  GLU B CB  
4747 C CG  . GLU B 78  ? 0.6075 0.8467 0.5604 0.0265  0.0137  -0.1329 78  GLU B CG  
4748 C CD  . GLU B 78  ? 0.7891 1.0253 0.7424 0.0412  0.0247  -0.1330 78  GLU B CD  
4749 O OE1 . GLU B 78  ? 0.8231 1.0839 0.7743 0.0442  0.0251  -0.1292 78  GLU B OE1 
4750 O OE2 . GLU B 78  ? 0.8655 1.0742 0.8238 0.0502  0.0326  -0.1332 78  GLU B OE2 
4751 N N   . ALA B 79  ? 0.2426 0.5581 0.2210 0.0291  -0.0090 -0.0697 79  ALA B N   
4752 C CA  . ALA B 79  ? 0.2451 0.5809 0.2306 0.0311  -0.0086 -0.0539 79  ALA B CA  
4753 C C   . ALA B 79  ? 0.2534 0.5894 0.2427 0.0371  -0.0078 -0.0420 79  ALA B C   
4754 O O   . ALA B 79  ? 0.2734 0.6265 0.2667 0.0404  -0.0051 -0.0336 79  ALA B O   
4755 C CB  . ALA B 79  ? 0.2135 0.5480 0.2034 0.0244  -0.0088 -0.0412 79  ALA B CB  
4756 N N   . ILE B 80  ? 0.1640 0.4806 0.1556 0.0375  -0.0100 -0.0398 80  ILE B N   
4757 C CA  . ILE B 80  ? 0.1484 0.4655 0.1476 0.0412  -0.0089 -0.0269 80  ILE B CA  
4758 C C   . ILE B 80  ? 0.1563 0.4765 0.1587 0.0522  -0.0021 -0.0330 80  ILE B C   
4759 O O   . ILE B 80  ? 0.2108 0.5494 0.2170 0.0572  0.0000  -0.0231 80  ILE B O   
4760 C CB  . ILE B 80  ? 0.1725 0.4651 0.1777 0.0356  -0.0124 -0.0190 80  ILE B CB  
4761 C CG1 . ILE B 80  ? 0.1486 0.4284 0.1489 0.0253  -0.0124 -0.0079 80  ILE B CG1 
4762 C CG2 . ILE B 80  ? 0.1897 0.4835 0.2031 0.0389  -0.0108 -0.0085 80  ILE B CG2 
4763 C CD1 . ILE B 80  ? 0.2843 0.5386 0.2876 0.0191  -0.0160 -0.0032 80  ILE B CD1 
4764 N N   . ARG B 81  ? 0.2077 0.5095 0.2078 0.0564  0.0027  -0.0485 81  ARG B N   
4765 C CA  . ARG B 81  ? 0.2437 0.5430 0.2462 0.0691  0.0122  -0.0526 81  ARG B CA  
4766 C C   . ARG B 81  ? 0.2551 0.5802 0.2515 0.0755  0.0174  -0.0558 81  ARG B C   
4767 O O   . ARG B 81  ? 0.2850 0.6207 0.2864 0.0863  0.0234  -0.0488 81  ARG B O   
4768 C CB  . ARG B 81  ? 0.2855 0.5538 0.2839 0.0715  0.0190  -0.0694 81  ARG B CB  
4769 C CG  . ARG B 81  ? 0.3523 0.6125 0.3521 0.0870  0.0324  -0.0724 81  ARG B CG  
4770 C CD  . ARG B 81  ? 0.5083 0.7317 0.5018 0.0889  0.0418  -0.0890 81  ARG B CD  
4771 N NE  . ARG B 81  ? 0.6255 0.8264 0.6283 0.0861  0.0376  -0.0831 81  ARG B NE  
4772 C CZ  . ARG B 81  ? 0.6697 0.8636 0.6847 0.0970  0.0420  -0.0706 81  ARG B CZ  
4773 N NH1 . ARG B 81  ? 0.6932 0.9023 0.7134 0.1121  0.0511  -0.0615 81  ARG B NH1 
4774 N NH2 . ARG B 81  ? 0.6701 0.8445 0.6927 0.0931  0.0376  -0.0661 81  ARG B NH2 
4775 N N   . LYS B 82  ? 0.2218 0.5587 0.2076 0.0688  0.0151  -0.0650 82  LYS B N   
4776 C CA  . LYS B 82  ? 0.2489 0.5992 0.2290 0.0715  0.0172  -0.0683 82  LYS B CA  
4777 C C   . LYS B 82  ? 0.1842 0.5561 0.1705 0.0754  0.0138  -0.0506 82  LYS B C   
4778 O O   . LYS B 82  ? 0.1845 0.5645 0.1753 0.0697  0.0066  -0.0361 82  LYS B O   
4779 C CB  . LYS B 82  ? 0.2429 0.6027 0.2164 0.0604  0.0114  -0.0753 82  LYS B CB  
4780 C CG  . LYS B 82  ? 0.4020 0.7445 0.3649 0.0538  0.0153  -0.0953 82  LYS B CG  
4781 C CD  . LYS B 82  ? 0.4072 0.7691 0.3689 0.0429  0.0089  -0.0960 82  LYS B CD  
4782 C CE  . LYS B 82  ? 0.5288 0.8785 0.4794 0.0327  0.0120  -0.1143 82  LYS B CE  
4783 N NZ  . LYS B 82  ? 0.5594 0.9349 0.5133 0.0226  0.0060  -0.1106 82  LYS B NZ  
4784 N N   . ASP B 83  ? 0.2210 0.5992 0.2050 0.0839  0.0197  -0.0521 83  ASP B N   
4785 C CA  . ASP B 83  ? 0.2682 0.6688 0.2544 0.0852  0.0152  -0.0382 83  ASP B CA  
4786 C C   . ASP B 83  ? 0.2225 0.6380 0.2073 0.0752  0.0064  -0.0368 83  ASP B C   
4787 O O   . ASP B 83  ? 0.2345 0.6491 0.2152 0.0707  0.0069  -0.0496 83  ASP B O   
4788 C CB  . ASP B 83  ? 0.2346 0.6391 0.2176 0.0961  0.0239  -0.0421 83  ASP B CB  
4789 C CG  . ASP B 83  ? 0.3099 0.7374 0.2949 0.0983  0.0195  -0.0270 83  ASP B CG  
4790 O OD1 . ASP B 83  ? 0.2689 0.7119 0.2530 0.0907  0.0109  -0.0220 83  ASP B OD1 
4791 O OD2 . ASP B 83  ? 0.3181 0.7480 0.3065 0.1077  0.0248  -0.0184 83  ASP B OD2 
4792 N N   . PRO B 84  ? 0.1905 0.6177 0.1793 0.0705  -0.0009 -0.0210 84  PRO B N   
4793 C CA  . PRO B 84  ? 0.1901 0.6194 0.1830 0.0618  -0.0032 -0.0177 84  PRO B CA  
4794 C C   . PRO B 84  ? 0.2189 0.6708 0.2117 0.0646  -0.0039 -0.0256 84  PRO B C   
4795 O O   . PRO B 84  ? 0.2084 0.6627 0.2038 0.0584  -0.0039 -0.0274 84  PRO B O   
4796 C CB  . PRO B 84  ? 0.1905 0.6079 0.1856 0.0562  -0.0021 -0.0010 84  PRO B CB  
4797 C CG  . PRO B 84  ? 0.1510 0.5576 0.1437 0.0566  -0.0016 0.0042  84  PRO B CG  
4798 C CD  . PRO B 84  ? 0.1893 0.6109 0.1782 0.0692  -0.0012 -0.0054 84  PRO B CD  
4799 N N   . ASP B 85  ? 0.1978 0.6588 0.1851 0.0729  -0.0011 -0.0295 85  ASP B N   
4800 C CA  . ASP B 85  ? 0.2036 0.6785 0.1876 0.0739  0.0009  -0.0383 85  ASP B CA  
4801 C C   . ASP B 85  ? 0.2609 0.7275 0.2388 0.0680  0.0041  -0.0552 85  ASP B C   
4802 O O   . ASP B 85  ? 0.2302 0.7117 0.2071 0.0636  0.0035  -0.0606 85  ASP B O   
4803 C CB  . ASP B 85  ? 0.2786 0.7548 0.2561 0.0840  0.0076  -0.0405 85  ASP B CB  
4804 C CG  . ASP B 85  ? 0.4085 0.9001 0.3904 0.0878  0.0033  -0.0237 85  ASP B CG  
4805 O OD1 . ASP B 85  ? 0.3988 0.8954 0.3867 0.0808  -0.0026 -0.0130 85  ASP B OD1 
4806 O OD2 . ASP B 85  ? 0.4377 0.9295 0.4167 0.0969  0.0090  -0.0212 85  ASP B OD2 
4807 N N   . ASP B 86  ? 0.2450 0.6884 0.2183 0.0668  0.0076  -0.0635 86  ASP B N   
4808 C CA  . ASP B 86  ? 0.2930 0.7240 0.2576 0.0592  0.0110  -0.0806 86  ASP B CA  
4809 C C   . ASP B 86  ? 0.2902 0.7244 0.2613 0.0490  0.0043  -0.0772 86  ASP B C   
4810 O O   . ASP B 86  ? 0.2574 0.6853 0.2220 0.0404  0.0055  -0.0896 86  ASP B O   
4811 C CB  . ASP B 86  ? 0.3229 0.7232 0.2788 0.0640  0.0206  -0.0924 86  ASP B CB  
4812 C CG  . ASP B 86  ? 0.3811 0.7756 0.3317 0.0760  0.0313  -0.0950 86  ASP B CG  
4813 O OD1 . ASP B 86  ? 0.3513 0.7615 0.2984 0.0769  0.0322  -0.0960 86  ASP B OD1 
4814 O OD2 . ASP B 86  ? 0.4434 0.8186 0.3951 0.0855  0.0394  -0.0945 86  ASP B OD2 
4815 N N   . LEU B 87  ? 0.1859 0.6280 0.1695 0.0492  -0.0010 -0.0604 87  LEU B N   
4816 C CA  . LEU B 87  ? 0.1724 0.6133 0.1629 0.0415  -0.0033 -0.0553 87  LEU B CA  
4817 C C   . LEU B 87  ? 0.1941 0.6572 0.1878 0.0357  -0.0035 -0.0554 87  LEU B C   
4818 O O   . LEU B 87  ? 0.2230 0.7079 0.2222 0.0385  -0.0036 -0.0490 87  LEU B O   
4819 C CB  . LEU B 87  ? 0.1615 0.5961 0.1610 0.0427  -0.0036 -0.0369 87  LEU B CB  
4820 C CG  . LEU B 87  ? 0.1476 0.5628 0.1459 0.0456  -0.0037 -0.0337 87  LEU B CG  
4821 C CD1 . LEU B 87  ? 0.1631 0.5600 0.1621 0.0423  -0.0016 -0.0157 87  LEU B CD1 
4822 C CD2 . LEU B 87  ? 0.2121 0.6101 0.2070 0.0415  -0.0041 -0.0422 87  LEU B CD2 
4823 N N   . GLU B 88  ? 0.1790 0.6386 0.1700 0.0273  -0.0035 -0.0614 88  GLU B N   
4824 C CA  . GLU B 88  ? 0.1777 0.6628 0.1741 0.0222  -0.0030 -0.0567 88  GLU B CA  
4825 C C   . GLU B 88  ? 0.1942 0.6732 0.1970 0.0243  -0.0017 -0.0367 88  GLU B C   
4826 O O   . GLU B 88  ? 0.2363 0.6892 0.2384 0.0265  -0.0014 -0.0288 88  GLU B O   
4827 C CB  . GLU B 88  ? 0.3025 0.7870 0.2909 0.0111  -0.0032 -0.0694 88  GLU B CB  
4828 C CG  . GLU B 88  ? 0.4221 0.8839 0.4083 0.0067  -0.0041 -0.0703 88  GLU B CG  
4829 C CD  . GLU B 88  ? 0.4992 0.9520 0.4733 -0.0046 -0.0041 -0.0888 88  GLU B CD  
4830 O OE1 . GLU B 88  ? 0.5814 1.0378 0.5458 -0.0079 -0.0020 -0.1025 88  GLU B OE1 
4831 O OE2 . GLU B 88  ? 0.5778 1.0183 0.5507 -0.0108 -0.0054 -0.0897 88  GLU B OE2 
4832 N N   . LYS B 89  ? 0.2522 0.6509 0.1672 0.0653  -0.0105 -0.0205 89  LYS B N   
4833 C CA  . LYS B 89  ? 0.2603 0.6491 0.1680 0.0737  -0.0140 -0.0001 89  LYS B CA  
4834 C C   . LYS B 89  ? 0.2580 0.6405 0.1791 0.0776  -0.0197 -0.0031 89  LYS B C   
4835 O O   . LYS B 89  ? 0.2942 0.6569 0.2157 0.0815  -0.0198 0.0096  89  LYS B O   
4836 C CB  . LYS B 89  ? 0.2874 0.6911 0.1808 0.0804  -0.0183 0.0098  89  LYS B CB  
4837 C CG  . LYS B 89  ? 0.3503 0.7552 0.2270 0.0771  -0.0122 0.0178  89  LYS B CG  
4838 C CD  . LYS B 89  ? 0.3906 0.8107 0.2515 0.0838  -0.0169 0.0263  89  LYS B CD  
4839 C CE  . LYS B 89  ? 0.4709 0.8871 0.3122 0.0805  -0.0100 0.0378  89  LYS B CE  
4840 N NZ  . LYS B 89  ? 0.5396 0.9653 0.3857 0.0703  -0.0033 0.0220  89  LYS B NZ  
4841 N N   . GLU B 90  ? 0.2376 0.6361 0.1703 0.0755  -0.0237 -0.0203 90  GLU B N   
4842 C CA  . GLU B 90  ? 0.2231 0.6169 0.1704 0.0771  -0.0278 -0.0256 90  GLU B CA  
4843 C C   . GLU B 90  ? 0.2024 0.5733 0.1582 0.0726  -0.0243 -0.0282 90  GLU B C   
4844 O O   . GLU B 90  ? 0.2431 0.6011 0.2075 0.0766  -0.0272 -0.0225 90  GLU B O   
4845 C CB  . GLU B 90  ? 0.2785 0.6933 0.2362 0.0713  -0.0299 -0.0459 90  GLU B CB  
4846 C CG  . GLU B 90  ? 0.5757 0.9835 0.5500 0.0671  -0.0305 -0.0574 90  GLU B CG  
4847 C CD  . GLU B 90  ? 0.7780 1.2081 0.7608 0.0608  -0.0320 -0.0750 90  GLU B CD  
4848 O OE1 . GLU B 90  ? 0.8444 1.2715 0.8397 0.0571  -0.0321 -0.0837 90  GLU B OE1 
4849 O OE2 . GLU B 90  ? 0.7907 1.2411 0.7675 0.0585  -0.0324 -0.0806 90  GLU B OE2 
4850 N N   . GLU B 91  ? 0.1966 0.5615 0.1507 0.0649  -0.0177 -0.0369 91  GLU B N   
4851 C CA  . GLU B 91  ? 0.1891 0.5262 0.1557 0.0601  -0.0120 -0.0396 91  GLU B CA  
4852 C C   . GLU B 91  ? 0.1814 0.4960 0.1466 0.0627  -0.0087 -0.0198 91  GLU B C   
4853 O O   . GLU B 91  ? 0.1928 0.4840 0.1698 0.0614  -0.0073 -0.0171 91  GLU B O   
4854 C CB  . GLU B 91  ? 0.1944 0.5300 0.1611 0.0532  -0.0047 -0.0547 91  GLU B CB  
4855 C CG  . GLU B 91  ? 0.2485 0.5887 0.2223 0.0472  -0.0056 -0.0760 91  GLU B CG  
4856 C CD  . GLU B 91  ? 0.3020 0.6335 0.2768 0.0416  0.0004  -0.0872 91  GLU B CD  
4857 O OE1 . GLU B 91  ? 0.2797 0.6183 0.2462 0.0430  0.0032  -0.0821 91  GLU B OE1 
4858 O OE2 . GLU B 91  ? 0.2923 0.6066 0.2753 0.0361  0.0028  -0.1001 91  GLU B OE2 
4859 N N   . VAL B 92  ? 0.2323 0.5529 0.1818 0.0649  -0.0066 -0.0064 92  VAL B N   
4860 C CA  . VAL B 92  ? 0.2365 0.5348 0.1821 0.0654  -0.0030 0.0128  92  VAL B CA  
4861 C C   . VAL B 92  ? 0.2728 0.5584 0.2196 0.0736  -0.0089 0.0240  92  VAL B C   
4862 O O   . VAL B 92  ? 0.2194 0.4783 0.1726 0.0723  -0.0064 0.0316  92  VAL B O   
4863 C CB  . VAL B 92  ? 0.2791 0.5867 0.2049 0.0648  0.0015  0.0249  92  VAL B CB  
4864 C CG1 . VAL B 92  ? 0.2794 0.5613 0.1986 0.0636  0.0060  0.0453  92  VAL B CG1 
4865 C CG2 . VAL B 92  ? 0.2350 0.5552 0.1620 0.0574  0.0089  0.0129  92  VAL B CG2 
4866 N N   . GLU B 93  ? 0.2885 0.5949 0.2296 0.0825  -0.0169 0.0239  93  GLU B N   
4867 C CA  . GLU B 93  ? 0.2814 0.5801 0.2253 0.0932  -0.0229 0.0328  93  GLU B CA  
4868 C C   . GLU B 93  ? 0.2567 0.5406 0.2219 0.0900  -0.0227 0.0225  93  GLU B C   
4869 O O   . GLU B 93  ? 0.2734 0.5332 0.2421 0.0942  -0.0220 0.0321  93  GLU B O   
4870 C CB  . GLU B 93  ? 0.3385 0.6670 0.2778 0.1022  -0.0310 0.0302  93  GLU B CB  
4871 C CG  . GLU B 93  ? 0.4553 0.7904 0.3744 0.1056  -0.0298 0.0420  93  GLU B CG  
4872 C CD  . GLU B 93  ? 0.5405 0.9031 0.4593 0.1109  -0.0355 0.0354  93  GLU B CD  
4873 O OE1 . GLU B 93  ? 0.5468 0.9249 0.4810 0.1099  -0.0392 0.0201  93  GLU B OE1 
4874 O OE2 . GLU B 93  ? 0.5377 0.9065 0.4399 0.1151  -0.0357 0.0455  93  GLU B OE2 
4875 N N   . LYS B 94  ? 0.2041 0.5002 0.1818 0.0823  -0.0228 0.0029  94  LYS B N   
4876 C CA  . LYS B 94  ? 0.2233 0.5047 0.2188 0.0786  -0.0218 -0.0063 94  LYS B CA  
4877 C C   . LYS B 94  ? 0.2198 0.4680 0.2188 0.0728  -0.0149 -0.0007 94  LYS B C   
4878 O O   . LYS B 94  ? 0.1849 0.4140 0.1928 0.0736  -0.0144 0.0010  94  LYS B O   
4879 C CB  . LYS B 94  ? 0.3166 0.6129 0.3213 0.0701  -0.0217 -0.0280 94  LYS B CB  
4880 C CG  . LYS B 94  ? 0.3740 0.7061 0.3782 0.0727  -0.0288 -0.0377 94  LYS B CG  
4881 C CD  . LYS B 94  ? 0.4137 0.7527 0.4285 0.0614  -0.0269 -0.0601 94  LYS B CD  
4882 C CE  . LYS B 94  ? 0.4714 0.8380 0.4814 0.0587  -0.0290 -0.0712 94  LYS B CE  
4883 N NZ  . LYS B 94  ? 0.5140 0.8936 0.5242 0.0678  -0.0338 -0.0630 94  LYS B NZ  
4884 N N   . LEU B 95  ? 0.1823 0.4264 0.1748 0.0670  -0.0096 0.0017  95  LEU B N   
4885 C CA  . LEU B 95  ? 0.2314 0.4502 0.2279 0.0608  -0.0037 0.0065  95  LEU B CA  
4886 C C   . LEU B 95  ? 0.1982 0.3954 0.1888 0.0641  -0.0030 0.0236  95  LEU B C   
4887 O O   . LEU B 95  ? 0.2109 0.3853 0.2088 0.0612  -0.0011 0.0248  95  LEU B O   
4888 C CB  . LEU B 95  ? 0.2258 0.4524 0.2173 0.0549  0.0018  0.0052  95  LEU B CB  
4889 C CG  . LEU B 95  ? 0.2945 0.5050 0.2912 0.0478  0.0077  0.0084  95  LEU B CG  
4890 C CD1 . LEU B 95  ? 0.3501 0.5460 0.3607 0.0454  0.0074  -0.0014 95  LEU B CD1 
4891 C CD2 . LEU B 95  ? 0.3960 0.6235 0.3890 0.0441  0.0129  0.0050  95  LEU B CD2 
4892 N N   . ILE B 96  ? 0.1910 0.3929 0.1664 0.0705  -0.0043 0.0369  96  ILE B N   
4893 C CA  . ILE B 96  ? 0.2303 0.4063 0.1966 0.0745  -0.0026 0.0539  96  ILE B CA  
4894 C C   . ILE B 96  ? 0.2451 0.4121 0.2189 0.0841  -0.0073 0.0532  96  ILE B C   
4895 O O   . ILE B 96  ? 0.3004 0.4388 0.2756 0.0838  -0.0044 0.0589  96  ILE B O   
4896 C CB  . ILE B 96  ? 0.2809 0.4619 0.2257 0.0800  -0.0022 0.0695  96  ILE B CB  
4897 C CG1 . ILE B 96  ? 0.2745 0.4628 0.2122 0.0687  0.0046  0.0706  96  ILE B CG1 
4898 C CG2 . ILE B 96  ? 0.3436 0.4923 0.2759 0.0860  0.0000  0.0877  96  ILE B CG2 
4899 C CD1 . ILE B 96  ? 0.3373 0.5371 0.2521 0.0732  0.0052  0.0837  96  ILE B CD1 
4900 N N   . GLU B 97  ? 0.2148 0.4078 0.1937 0.0925  -0.0141 0.0454  97  GLU B N   
4901 C CA  . GLU B 97  ? 0.2710 0.4633 0.2604 0.1015  -0.0183 0.0420  97  GLU B CA  
4902 C C   . GLU B 97  ? 0.2596 0.4316 0.2636 0.0930  -0.0143 0.0328  97  GLU B C   
4903 O O   . GLU B 97  ? 0.2377 0.3876 0.2440 0.0975  -0.0129 0.0375  97  GLU B O   
4904 C CB  . GLU B 97  ? 0.3744 0.6053 0.3714 0.1061  -0.0255 0.0296  97  GLU B CB  
4905 C CG  . GLU B 97  ? 0.5772 0.8301 0.5653 0.1223  -0.0329 0.0386  97  GLU B CG  
4906 C CD  . GLU B 97  ? 0.7164 1.0058 0.7093 0.1186  -0.0372 0.0228  97  GLU B CD  
4907 O OE1 . GLU B 97  ? 0.7603 1.0628 0.7535 0.1079  -0.0360 0.0120  97  GLU B OE1 
4908 O OE2 . GLU B 97  ? 0.7809 1.0837 0.7771 0.1254  -0.0408 0.0199  97  GLU B OE2 
4909 N N   . PHE B 98  ? 0.1689 0.3476 0.1812 0.0816  -0.0123 0.0193  98  PHE B N   
4910 C CA  . PHE B 98  ? 0.1481 0.3097 0.1721 0.0740  -0.0090 0.0103  98  PHE B CA  
4911 C C   . PHE B 98  ? 0.1823 0.3129 0.2021 0.0693  -0.0041 0.0197  98  PHE B C   
4912 O O   . PHE B 98  ? 0.1907 0.3021 0.2160 0.0684  -0.0024 0.0181  98  PHE B O   
4913 C CB  . PHE B 98  ? 0.1375 0.3099 0.1671 0.0646  -0.0075 -0.0037 98  PHE B CB  
4914 C CG  . PHE B 98  ? 0.2027 0.3605 0.2425 0.0583  -0.0048 -0.0137 98  PHE B CG  
4915 C CD1 . PHE B 98  ? 0.1891 0.3537 0.2377 0.0589  -0.0062 -0.0236 98  PHE B CD1 
4916 C CD2 . PHE B 98  ? 0.2343 0.3739 0.2741 0.0514  -0.0009 -0.0132 98  PHE B CD2 
4917 C CE1 . PHE B 98  ? 0.1983 0.3479 0.2533 0.0524  -0.0028 -0.0320 98  PHE B CE1 
4918 C CE2 . PHE B 98  ? 0.1614 0.2872 0.2077 0.0467  0.0011  -0.0213 98  PHE B CE2 
4919 C CZ  . PHE B 98  ? 0.1752 0.3042 0.2280 0.0470  0.0005  -0.0303 98  PHE B CZ  
4920 N N   . THR B 99  ? 0.2174 0.3442 0.2271 0.0649  -0.0012 0.0285  99  THR B N   
4921 C CA  . THR B 99  ? 0.1968 0.2963 0.2016 0.0583  0.0039  0.0372  99  THR B CA  
4922 C C   . THR B 99  ? 0.1960 0.2718 0.1941 0.0661  0.0043  0.0475  99  THR B C   
4923 O O   . THR B 99  ? 0.2050 0.2561 0.2051 0.0621  0.0072  0.0472  99  THR B O   
4924 C CB  . THR B 99  ? 0.2810 0.3851 0.2756 0.0517  0.0077  0.0453  99  THR B CB  
4925 O OG1 . THR B 99  ? 0.2029 0.3302 0.2041 0.0470  0.0077  0.0347  99  THR B OG1 
4926 C CG2 . THR B 99  ? 0.2403 0.3195 0.2316 0.0410  0.0135  0.0519  99  THR B CG2 
4927 N N   . LYS B 100 ? 0.2117 0.2944 0.2006 0.0785  0.0013  0.0563  100 LYS B N   
4928 C CA  . LYS B 100 ? 0.2479 0.3059 0.2281 0.0893  0.0021  0.0674  100 LYS B CA  
4929 C C   . LYS B 100 ? 0.2265 0.2800 0.2199 0.0951  0.0005  0.0582  100 LYS B C   
4930 O O   . LYS B 100 ? 0.2670 0.2909 0.2564 0.0985  0.0040  0.0630  100 LYS B O   
4931 C CB  . LYS B 100 ? 0.3516 0.4224 0.3190 0.1045  -0.0021 0.0790  100 LYS B CB  
4932 C CG  . LYS B 100 ? 0.4953 0.5606 0.4436 0.0999  0.0016  0.0926  100 LYS B CG  
4933 C CD  . LYS B 100 ? 0.6066 0.6810 0.5387 0.1173  -0.0029 0.1061  100 LYS B CD  
4934 C CE  . LYS B 100 ? 0.6755 0.7408 0.5851 0.1122  0.0022  0.1212  100 LYS B CE  
4935 N NZ  . LYS B 100 ? 0.7288 0.8062 0.6201 0.1299  -0.0031 0.1348  100 LYS B NZ  
4936 N N   . LEU B 101 ? 0.2307 0.3124 0.2388 0.0958  -0.0038 0.0446  101 LEU B N   
4937 C CA  . LEU B 101 ? 0.2119 0.2921 0.2327 0.0996  -0.0041 0.0351  101 LEU B CA  
4938 C C   . LEU B 101 ? 0.2269 0.2800 0.2507 0.0878  0.0013  0.0301  101 LEU B C   
4939 O O   . LEU B 101 ? 0.2450 0.2826 0.2723 0.0915  0.0034  0.0275  101 LEU B O   
4940 C CB  . LEU B 101 ? 0.2576 0.3730 0.2922 0.0987  -0.0084 0.0207  101 LEU B CB  
4941 C CG  . LEU B 101 ? 0.3297 0.4477 0.3787 0.0986  -0.0073 0.0087  101 LEU B CG  
4942 C CD1 . LEU B 101 ? 0.3512 0.4717 0.4025 0.1154  -0.0089 0.0133  101 LEU B CD1 
4943 C CD2 . LEU B 101 ? 0.3603 0.5077 0.4205 0.0914  -0.0094 -0.0065 101 LEU B CD2 
4944 N N   . ASN B 102 ? 0.1779 0.2274 0.2003 0.0742  0.0034  0.0282  102 ASN B N   
4945 C CA  . ASN B 102 ? 0.1916 0.2225 0.2173 0.0628  0.0069  0.0223  102 ASN B CA  
4946 C C   . ASN B 102 ? 0.2250 0.2290 0.2399 0.0553  0.0113  0.0314  102 ASN B C   
4947 O O   . ASN B 102 ? 0.2127 0.2027 0.2291 0.0450  0.0137  0.0268  102 ASN B O   
4948 C CB  . ASN B 102 ? 0.1847 0.2325 0.2175 0.0537  0.0059  0.0125  102 ASN B CB  
4949 C CG  . ASN B 102 ? 0.2489 0.3161 0.2916 0.0568  0.0035  0.0009  102 ASN B CG  
4950 O OD1 . ASN B 102 ? 0.2555 0.3175 0.3037 0.0590  0.0044  -0.0046 102 ASN B OD1 
4951 N ND2 . ASN B 102 ? 0.2438 0.3338 0.2882 0.0560  0.0014  -0.0035 102 ASN B ND2 
4952 N N   . TYR B 103 ? 0.2297 0.2262 0.2325 0.0598  0.0126  0.0441  103 TYR B N   
4953 C CA  . TYR B 103 ? 0.3040 0.2796 0.2950 0.0492  0.0177  0.0531  103 TYR B CA  
4954 C C   . TYR B 103 ? 0.3165 0.2582 0.3036 0.0423  0.0225  0.0522  103 TYR B C   
4955 O O   . TYR B 103 ? 0.3088 0.2404 0.2931 0.0271  0.0261  0.0520  103 TYR B O   
4956 C CB  . TYR B 103 ? 0.3497 0.3201 0.3255 0.0577  0.0187  0.0681  103 TYR B CB  
4957 C CG  . TYR B 103 ? 0.3970 0.3422 0.3574 0.0464  0.0258  0.0792  103 TYR B CG  
4958 C CD1 . TYR B 103 ? 0.4045 0.3656 0.3629 0.0345  0.0279  0.0814  103 TYR B CD1 
4959 C CD2 . TYR B 103 ? 0.4658 0.3708 0.4129 0.0472  0.0313  0.0868  103 TYR B CD2 
4960 C CE1 . TYR B 103 ? 0.5084 0.4483 0.4530 0.0217  0.0355  0.0912  103 TYR B CE1 
4961 C CE2 . TYR B 103 ? 0.5356 0.4146 0.4671 0.0343  0.0390  0.0964  103 TYR B CE2 
4962 C CZ  . TYR B 103 ? 0.5835 0.4813 0.5142 0.0207  0.0411  0.0987  103 TYR B CZ  
4963 O OH  . TYR B 103 ? 0.5844 0.4583 0.5000 0.0055  0.0499  0.1077  103 TYR B OH  
4964 N N   . GLU B 104 ? 0.2562 0.1818 0.2429 0.0532  0.0228  0.0510  104 GLU B N   
4965 C CA  . GLU B 104 ? 0.2745 0.1651 0.2549 0.0480  0.0281  0.0494  104 GLU B CA  
4966 C C   . GLU B 104 ? 0.2996 0.1941 0.2907 0.0394  0.0272  0.0354  104 GLU B C   
4967 O O   . GLU B 104 ? 0.3514 0.2193 0.3370 0.0333  0.0313  0.0320  104 GLU B O   
4968 C CB  . GLU B 104 ? 0.3084 0.1780 0.2819 0.0659  0.0299  0.0547  104 GLU B CB  
4969 C CG  . GLU B 104 ? 0.4082 0.2683 0.3670 0.0777  0.0308  0.0707  104 GLU B CG  
4970 C CD  . GLU B 104 ? 0.5452 0.3706 0.4852 0.0649  0.0381  0.0810  104 GLU B CD  
4971 O OE1 . GLU B 104 ? 0.6021 0.4038 0.5396 0.0499  0.0432  0.0751  104 GLU B OE1 
4972 O OE2 . GLU B 104 ? 0.6182 0.4396 0.5446 0.0693  0.0393  0.0948  104 GLU B OE2 
4973 N N   . LYS B 105 ? 0.2228 0.1473 0.2267 0.0386  0.0224  0.0272  105 LYS B N   
4974 C CA  . LYS B 105 ? 0.2073 0.1329 0.2181 0.0312  0.0219  0.0156  105 LYS B CA  
4975 C C   . LYS B 105 ? 0.2750 0.1974 0.2834 0.0147  0.0226  0.0141  105 LYS B C   
4976 O O   . LYS B 105 ? 0.2505 0.1863 0.2591 0.0092  0.0219  0.0187  105 LYS B O   
4977 C CB  . LYS B 105 ? 0.2125 0.1663 0.2351 0.0357  0.0178  0.0080  105 LYS B CB  
4978 C CG  . LYS B 105 ? 0.2625 0.2260 0.2897 0.0502  0.0167  0.0076  105 LYS B CG  
4979 C CD  . LYS B 105 ? 0.1712 0.1635 0.2090 0.0516  0.0133  -0.0004 105 LYS B CD  
4980 C CE  . LYS B 105 ? 0.1904 0.1989 0.2343 0.0647  0.0118  -0.0013 105 LYS B CE  
4981 N NZ  . LYS B 105 ? 0.1979 0.2338 0.2516 0.0628  0.0094  -0.0110 105 LYS B NZ  
4982 N N   . PRO B 106 ? 0.2323 0.1397 0.2385 0.0065  0.0241  0.0073  106 PRO B N   
4983 C CA  . PRO B 106 ? 0.2536 0.1630 0.2586 -0.0093 0.0237  0.0050  106 PRO B CA  
4984 C C   . PRO B 106 ? 0.2413 0.1819 0.2557 -0.0116 0.0191  0.0028  106 PRO B C   
4985 O O   . PRO B 106 ? 0.2594 0.2095 0.2744 -0.0222 0.0190  0.0044  106 PRO B O   
4986 C CB  . PRO B 106 ? 0.2716 0.1651 0.2730 -0.0142 0.0246  -0.0039 106 PRO B CB  
4987 C CG  . PRO B 106 ? 0.2884 0.1591 0.2847 -0.0033 0.0287  -0.0032 106 PRO B CG  
4988 C CD  . PRO B 106 ? 0.2447 0.1327 0.2482 0.0113  0.0267  0.0016  106 PRO B CD  
4989 N N   . ILE B 107 ? 0.2048 0.1616 0.2264 -0.0023 0.0159  -0.0011 107 ILE B N   
4990 C CA  . ILE B 107 ? 0.1626 0.1449 0.1913 -0.0027 0.0124  -0.0032 107 ILE B CA  
4991 C C   . ILE B 107 ? 0.1711 0.1688 0.2011 -0.0020 0.0131  0.0036  107 ILE B C   
4992 O O   . ILE B 107 ? 0.1628 0.1816 0.1980 -0.0038 0.0115  0.0023  107 ILE B O   
4993 C CB  . ILE B 107 ? 0.1855 0.1759 0.2188 0.0058  0.0104  -0.0096 107 ILE B CB  
4994 C CG1 . ILE B 107 ? 0.1834 0.1760 0.2183 0.0154  0.0114  -0.0081 107 ILE B CG1 
4995 C CG2 . ILE B 107 ? 0.1794 0.1556 0.2093 0.0037  0.0105  -0.0159 107 ILE B CG2 
4996 C CD1 . ILE B 107 ? 0.1809 0.1865 0.2211 0.0208  0.0101  -0.0150 107 ILE B CD1 
4997 N N   . TYR B 108 ? 0.2132 0.2007 0.2373 0.0014  0.0158  0.0112  108 TYR B N   
4998 C CA  . TYR B 108 ? 0.2137 0.2127 0.2352 0.0011  0.0173  0.0192  108 TYR B CA  
4999 C C   . TYR B 108 ? 0.2418 0.2281 0.2557 -0.0117 0.0219  0.0259  108 TYR B C   
5000 O O   . TYR B 108 ? 0.2665 0.2555 0.2742 -0.0126 0.0249  0.0347  108 TYR B O   
5001 C CB  . TYR B 108 ? 0.1805 0.1784 0.1978 0.0136  0.0170  0.0248  108 TYR B CB  
5002 C CG  . TYR B 108 ? 0.1846 0.2076 0.2091 0.0222  0.0132  0.0194  108 TYR B CG  
5003 C CD1 . TYR B 108 ? 0.1452 0.1719 0.1772 0.0260  0.0108  0.0094  108 TYR B CD1 
5004 C CD2 . TYR B 108 ? 0.1780 0.2207 0.2006 0.0245  0.0128  0.0233  108 TYR B CD2 
5005 C CE1 . TYR B 108 ? 0.1696 0.2169 0.2068 0.0312  0.0084  0.0033  108 TYR B CE1 
5006 C CE2 . TYR B 108 ? 0.2287 0.2932 0.2565 0.0305  0.0099  0.0166  108 TYR B CE2 
5007 C CZ  . TYR B 108 ? 0.2049 0.2707 0.2400 0.0334  0.0078  0.0064  108 TYR B CZ  
5008 O OH  . TYR B 108 ? 0.1987 0.2837 0.2377 0.0372  0.0060  -0.0012 108 TYR B OH  
5009 N N   . ARG B 109 ? 0.2215 0.1946 0.2344 -0.0228 0.0231  0.0218  109 ARG B N   
5010 C CA  . ARG B 109 ? 0.3340 0.2931 0.3392 -0.0382 0.0285  0.0265  109 ARG B CA  
5011 C C   . ARG B 109 ? 0.2984 0.2882 0.3115 -0.0486 0.0284  0.0255  109 ARG B C   
5012 O O   . ARG B 109 ? 0.2772 0.2812 0.2978 -0.0577 0.0261  0.0182  109 ARG B O   
5013 C CB  . ARG B 109 ? 0.3882 0.3229 0.3888 -0.0473 0.0298  0.0205  109 ARG B CB  
5014 C CG  . ARG B 109 ? 0.5551 0.4795 0.5493 -0.0680 0.0352  0.0217  109 ARG B CG  
5015 C CD  . ARG B 109 ? 0.6449 0.5380 0.6302 -0.0775 0.0380  0.0158  109 ARG B CD  
5016 N NE  . ARG B 109 ? 0.6752 0.5471 0.6566 -0.0625 0.0370  0.0137  109 ARG B NE  
5017 C CZ  . ARG B 109 ? 0.6752 0.5372 0.6556 -0.0648 0.0355  0.0040  109 ARG B CZ  
5018 N NH1 . ARG B 109 ? 0.7470 0.6191 0.7292 -0.0810 0.0337  -0.0039 109 ARG B NH1 
5019 N NH2 . ARG B 109 ? 0.6539 0.4993 0.6315 -0.0511 0.0357  0.0018  109 ARG B NH2 
5020 N N   . PHE B 110 ? 0.2682 0.2717 0.2797 -0.0457 0.0307  0.0327  110 PHE B N   
5021 C CA  . PHE B 110 ? 0.2773 0.3095 0.2948 -0.0556 0.0329  0.0332  110 PHE B CA  
5022 C C   . PHE B 110 ? 0.2651 0.2831 0.2689 -0.0637 0.0409  0.0450  110 PHE B C   
5023 O O   . PHE B 110 ? 0.2749 0.2798 0.2683 -0.0526 0.0419  0.0534  110 PHE B O   
5024 C CB  . PHE B 110 ? 0.2957 0.3605 0.3228 -0.0436 0.0292  0.0299  110 PHE B CB  
5025 C CG  . PHE B 110 ? 0.2437 0.3203 0.2819 -0.0352 0.0225  0.0195  110 PHE B CG  
5026 C CD1 . PHE B 110 ? 0.2263 0.3257 0.2753 -0.0405 0.0202  0.0127  110 PHE B CD1 
5027 C CD2 . PHE B 110 ? 0.2709 0.3367 0.3080 -0.0219 0.0188  0.0168  110 PHE B CD2 
5028 C CE1 . PHE B 110 ? 0.2158 0.3220 0.2714 -0.0312 0.0144  0.0049  110 PHE B CE1 
5029 C CE2 . PHE B 110 ? 0.2499 0.3222 0.2940 -0.0154 0.0141  0.0082  110 PHE B CE2 
5030 C CZ  . PHE B 110 ? 0.1720 0.2624 0.2241 -0.0194 0.0119  0.0030  110 PHE B CZ  
5031 N N   . GLU B 111 ? 0.3149 0.3364 0.3180 -0.0831 0.0467  0.0458  111 GLU B N   
5032 C CA  . GLU B 111 ? 0.3641 0.3686 0.3513 -0.0926 0.0559  0.0579  111 GLU B CA  
5033 C C   . GLU B 111 ? 0.3295 0.3563 0.3146 -0.0829 0.0569  0.0648  111 GLU B C   
5034 O O   . GLU B 111 ? 0.3499 0.3561 0.3175 -0.0790 0.0614  0.0772  111 GLU B O   
5035 C CB  . GLU B 111 ? 0.5019 0.5110 0.4902 -0.1184 0.0630  0.0560  111 GLU B CB  
5036 C CG  . GLU B 111 ? 0.7281 0.7325 0.7025 -0.1298 0.0736  0.0680  111 GLU B CG  
5037 C CD  . GLU B 111 ? 0.9810 0.9308 0.9303 -0.1351 0.0816  0.0795  111 GLU B CD  
5038 O OE1 . GLU B 111 ? 1.0758 1.0141 1.0096 -0.1460 0.0916  0.0908  111 GLU B OE1 
5039 O OE2 . GLU B 111 ? 1.0497 0.9668 0.9936 -0.1274 0.0786  0.0776  111 GLU B OE2 
5040 N N   . ARG B 112 ? 0.3105 0.3775 0.3115 -0.0770 0.0524  0.0570  112 ARG B N   
5041 C CA  . ARG B 112 ? 0.2948 0.3848 0.2935 -0.0684 0.0536  0.0612  112 ARG B CA  
5042 C C   . ARG B 112 ? 0.3177 0.3921 0.3059 -0.0497 0.0495  0.0666  112 ARG B C   
5043 O O   . ARG B 112 ? 0.3344 0.4105 0.3097 -0.0453 0.0525  0.0759  112 ARG B O   
5044 C CB  . ARG B 112 ? 0.2269 0.3590 0.2444 -0.0638 0.0498  0.0498  112 ARG B CB  
5045 C CG  . ARG B 112 ? 0.2114 0.3696 0.2269 -0.0556 0.0518  0.0515  112 ARG B CG  
5046 C CD  . ARG B 112 ? 0.2775 0.4426 0.2825 -0.0695 0.0620  0.0611  112 ARG B CD  
5047 N NE  . ARG B 112 ? 0.2776 0.4765 0.2844 -0.0635 0.0644  0.0591  112 ARG B NE  
5048 C CZ  . ARG B 112 ? 0.3597 0.5666 0.3538 -0.0709 0.0731  0.0681  112 ARG B CZ  
5049 N NH1 . ARG B 112 ? 0.3418 0.5224 0.3196 -0.0849 0.0804  0.0807  112 ARG B NH1 
5050 N NH2 . ARG B 112 ? 0.3749 0.6139 0.3707 -0.0646 0.0753  0.0644  112 ARG B NH2 
5051 N N   . ILE B 113 ? 0.2508 0.3121 0.2439 -0.0387 0.0425  0.0607  113 ILE B N   
5052 C CA  . ILE B 113 ? 0.2693 0.3203 0.2548 -0.0217 0.0384  0.0646  113 ILE B CA  
5053 C C   . ILE B 113 ? 0.3584 0.3775 0.3237 -0.0213 0.0432  0.0793  113 ILE B C   
5054 O O   . ILE B 113 ? 0.3514 0.3722 0.3050 -0.0106 0.0427  0.0880  113 ILE B O   
5055 C CB  . ILE B 113 ? 0.2702 0.3137 0.2653 -0.0123 0.0316  0.0551  113 ILE B CB  
5056 C CG1 . ILE B 113 ? 0.2571 0.3297 0.2676 -0.0080 0.0268  0.0425  113 ILE B CG1 
5057 C CG2 . ILE B 113 ? 0.2555 0.2854 0.2424 0.0030  0.0286  0.0602  113 ILE B CG2 
5058 C CD1 . ILE B 113 ? 0.2759 0.3399 0.2941 -0.0010 0.0215  0.0335  113 ILE B CD1 
5059 N N   . ARG B 114 ? 0.3682 0.3569 0.3274 -0.0328 0.0481  0.0823  114 ARG B N   
5060 C CA  . ARG B 114 ? 0.4411 0.3921 0.3783 -0.0327 0.0542  0.0968  114 ARG B CA  
5061 C C   . ARG B 114 ? 0.4512 0.4083 0.3738 -0.0396 0.0613  0.1090  114 ARG B C   
5062 O O   . ARG B 114 ? 0.5028 0.4388 0.4050 -0.0308 0.0639  0.1232  114 ARG B O   
5063 C CB  . ARG B 114 ? 0.5221 0.4382 0.4554 -0.0469 0.0594  0.0949  114 ARG B CB  
5064 C CG  . ARG B 114 ? 0.6764 0.5949 0.6262 -0.0449 0.0530  0.0800  114 ARG B CG  
5065 C CD  . ARG B 114 ? 0.7828 0.6679 0.7270 -0.0605 0.0583  0.0767  114 ARG B CD  
5066 N NE  . ARG B 114 ? 0.7802 0.6788 0.7403 -0.0669 0.0534  0.0618  114 ARG B NE  
5067 C CZ  . ARG B 114 ? 0.7748 0.6784 0.7392 -0.0877 0.0561  0.0551  114 ARG B CZ  
5068 N NH1 . ARG B 114 ? 0.7784 0.6754 0.7337 -0.1056 0.0646  0.0613  114 ARG B NH1 
5069 N NH2 . ARG B 114 ? 0.7716 0.6885 0.7485 -0.0913 0.0506  0.0424  114 ARG B NH2 
5070 N N   . GLU B 115 ? 0.4180 0.4057 0.3502 -0.0538 0.0645  0.1039  115 GLU B N   
5071 C CA  . GLU B 115 ? 0.4630 0.4616 0.3821 -0.0608 0.0720  0.1143  115 GLU B CA  
5072 C C   . GLU B 115 ? 0.4484 0.4694 0.3629 -0.0424 0.0668  0.1177  115 GLU B C   
5073 O O   . GLU B 115 ? 0.4837 0.4935 0.3764 -0.0380 0.0706  0.1322  115 GLU B O   
5074 C CB  . GLU B 115 ? 0.4821 0.5144 0.4158 -0.0795 0.0768  0.1060  115 GLU B CB  
5075 C CG  . GLU B 115 ? 0.5457 0.5633 0.4829 -0.1019 0.0829  0.1026  115 GLU B CG  
5076 C CD  . GLU B 115 ? 0.5914 0.6513 0.5451 -0.1186 0.0870  0.0944  115 GLU B CD  
5077 O OE1 . GLU B 115 ? 0.5639 0.6613 0.5253 -0.1110 0.0857  0.0916  115 GLU B OE1 
5078 O OE2 . GLU B 115 ? 0.5859 0.6432 0.5452 -0.1391 0.0917  0.0897  115 GLU B OE2 
5079 N N   . LEU B 116 ? 0.3460 0.3989 0.2792 -0.0324 0.0585  0.1043  116 LEU B N   
5080 C CA  . LEU B 116 ? 0.3716 0.4498 0.3018 -0.0176 0.0537  0.1040  116 LEU B CA  
5081 C C   . LEU B 116 ? 0.3703 0.4287 0.2854 -0.0004 0.0487  0.1138  116 LEU B C   
5082 O O   . LEU B 116 ? 0.4214 0.4919 0.3227 0.0085  0.0476  0.1211  116 LEU B O   
5083 C CB  . LEU B 116 ? 0.3105 0.4185 0.2628 -0.0111 0.0464  0.0864  116 LEU B CB  
5084 C CG  . LEU B 116 ? 0.2535 0.3872 0.2223 -0.0229 0.0497  0.0759  116 LEU B CG  
5085 C CD1 . LEU B 116 ? 0.2833 0.4338 0.2709 -0.0137 0.0422  0.0599  116 LEU B CD1 
5086 C CD2 . LEU B 116 ? 0.2966 0.4571 0.2594 -0.0286 0.0567  0.0790  116 LEU B CD2 
5087 N N   . MET B 117 ? 0.3812 0.4116 0.2984 0.0052  0.0455  0.1136  117 MET B N   
5088 C CA  . MET B 117 ? 0.4253 0.4403 0.3308 0.0239  0.0405  0.1220  117 MET B CA  
5089 C C   . MET B 117 ? 0.5350 0.5176 0.4128 0.0248  0.0472  0.1422  117 MET B C   
5090 O O   . MET B 117 ? 0.5520 0.5274 0.4162 0.0429  0.0430  0.1522  117 MET B O   
5091 C CB  . MET B 117 ? 0.4325 0.4303 0.3504 0.0305  0.0358  0.1140  117 MET B CB  
5092 C CG  . MET B 117 ? 0.3804 0.4071 0.3219 0.0324  0.0289  0.0956  117 MET B CG  
5093 S SD  . MET B 117 ? 0.4685 0.5336 0.4132 0.0482  0.0203  0.0904  117 MET B SD  
5094 C CE  . MET B 117 ? 0.5152 0.6120 0.4637 0.0364  0.0237  0.0839  117 MET B CE  
5095 N N   . ASN B 118 ? 0.5870 0.5507 0.4554 0.0060  0.0577  0.1486  118 ASN B N   
5096 C CA  . ASN B 118 ? 0.6632 0.5926 0.5020 0.0039  0.0663  0.1686  118 ASN B CA  
5097 C C   . ASN B 118 ? 0.6792 0.6314 0.5029 0.0013  0.0702  0.1779  118 ASN B C   
5098 O O   . ASN B 118 ? 0.7633 0.6878 0.5590 -0.0006 0.0780  0.1962  118 ASN B O   
5099 C CB  . ASN B 118 ? 0.7349 0.6289 0.5687 -0.0183 0.0775  0.1706  118 ASN B CB  
5100 C CG  . ASN B 118 ? 0.8443 0.7010 0.6806 -0.0135 0.0761  0.1673  118 ASN B CG  
5101 O OD1 . ASN B 118 ? 0.9324 0.7707 0.7602 0.0077  0.0712  0.1738  118 ASN B OD1 
5102 N ND2 . ASN B 118 ? 0.8703 0.7177 0.7183 -0.0329 0.0803  0.1568  118 ASN B ND2 
5103 N N   . LYS B 119 ? 0.6263 0.6253 0.4654 0.0015  0.0656  0.1661  119 LYS B N   
5104 C CA  . LYS B 119 ? 0.6738 0.6973 0.4995 -0.0028 0.0703  0.1724  119 LYS B CA  
5105 C C   . LYS B 119 ? 0.7124 0.7507 0.5239 0.0190  0.0620  0.1792  119 LYS B C   
5106 O O   . LYS B 119 ? 0.6814 0.7330 0.5053 0.0351  0.0507  0.1704  119 LYS B O   
5107 C CB  . LYS B 119 ? 0.6313 0.6975 0.4800 -0.0144 0.0713  0.1553  119 LYS B CB  
5108 C CG  . LYS B 119 ? 0.6742 0.7326 0.5353 -0.0367 0.0797  0.1500  119 LYS B CG  
5109 C CD  . LYS B 119 ? 0.6751 0.7756 0.5509 -0.0488 0.0843  0.1392  119 LYS B CD  
5110 C CE  . LYS B 119 ? 0.7035 0.8003 0.5921 -0.0710 0.0920  0.1342  119 LYS B CE  
5111 N NZ  . LYS B 119 ? 0.7192 0.8621 0.6274 -0.0801 0.0952  0.1215  119 LYS B NZ  
5112 N N   . GLU B 120 ? 0.7428 0.7798 0.5272 0.0181  0.0679  0.1947  120 GLU B N   
5113 C CA  . GLU B 120 ? 0.7978 0.8474 0.5687 0.0367  0.0585  0.1980  120 GLU B CA  
5114 C C   . GLU B 120 ? 0.7571 0.8591 0.5432 0.0411  0.0517  0.1819  120 GLU B C   
5115 O O   . GLU B 120 ? 0.7832 0.9034 0.5701 0.0580  0.0405  0.1778  120 GLU B O   
5116 C CB  . GLU B 120 ? 0.9161 0.9451 0.6572 0.0309  0.0654  0.2124  120 GLU B CB  
5117 C CG  . GLU B 120 ? 1.0044 0.9773 0.7269 0.0234  0.0733  0.2272  120 GLU B CG  
5118 C CD  . GLU B 120 ? 1.0568 1.0065 0.7461 0.0245  0.0759  0.2433  120 GLU B CD  
5119 O OE1 . GLU B 120 ? 1.0260 1.0019 0.7069 0.0364  0.0692  0.2438  120 GLU B OE1 
5120 O OE2 . GLU B 120 ? 1.1041 1.0099 0.7757 0.0124  0.0843  0.2549  120 GLU B OE2 
5121 N N   . LYS B 121 ? 0.6377 0.7645 0.4369 0.0255  0.0584  0.1711  121 LYS B N   
5122 C CA  . LYS B 121 ? 0.6434 0.8150 0.4563 0.0280  0.0536  0.1537  121 LYS B CA  
5123 C C   . LYS B 121 ? 0.5843 0.7711 0.4215 0.0131  0.0596  0.1390  121 LYS B C   
5124 O O   . LYS B 121 ? 0.6245 0.7975 0.4625 -0.0029 0.0696  0.1439  121 LYS B O   
5125 C CB  . LYS B 121 ? 0.7330 0.9202 0.5288 0.0277  0.0554  0.1555  121 LYS B CB  
5126 C CG  . LYS B 121 ? 0.8068 1.0364 0.6161 0.0305  0.0509  0.1361  121 LYS B CG  
5127 C CD  . LYS B 121 ? 0.8589 1.1012 0.6804 0.0454  0.0381  0.1256  121 LYS B CD  
5128 C CE  . LYS B 121 ? 0.8559 1.1334 0.6942 0.0451  0.0352  0.1032  121 LYS B CE  
5129 N NZ  . LYS B 121 ? 0.8317 1.1167 0.6849 0.0546  0.0252  0.0912  121 LYS B NZ  
5130 N N   . LEU B 122 ? 0.5043 0.7178 0.3627 0.0183  0.0529  0.1193  122 LEU B N   
5131 C CA  . LEU B 122 ? 0.3979 0.6240 0.2818 0.0085  0.0560  0.1034  122 LEU B CA  
5132 C C   . LEU B 122 ? 0.4073 0.6712 0.2939 0.0067  0.0599  0.0917  122 LEU B C   
5133 O O   . LEU B 122 ? 0.4592 0.7411 0.3394 0.0165  0.0545  0.0854  122 LEU B O   
5134 C CB  . LEU B 122 ? 0.3896 0.6102 0.2953 0.0160  0.0465  0.0897  122 LEU B CB  
5135 C CG  . LEU B 122 ? 0.3967 0.5823 0.3031 0.0195  0.0423  0.0974  122 LEU B CG  
5136 C CD1 . LEU B 122 ? 0.3785 0.5649 0.3064 0.0256  0.0344  0.0819  122 LEU B CD1 
5137 C CD2 . LEU B 122 ? 0.3478 0.5074 0.2524 0.0050  0.0508  0.1069  122 LEU B CD2 
5138 N N   . ASN B 123 ? 0.3758 0.6514 0.2734 -0.0059 0.0688  0.0872  123 ASN B N   
5139 C CA  . ASN B 123 ? 0.3094 0.6128 0.2167 -0.0062 0.0707  0.0722  123 ASN B CA  
5140 C C   . ASN B 123 ? 0.2595 0.5754 0.1913 -0.0008 0.0664  0.0535  123 ASN B C   
5141 O O   . ASN B 123 ? 0.2866 0.5895 0.2273 0.0032  0.0611  0.0515  123 ASN B O   
5142 C CB  . ASN B 123 ? 0.3112 0.6193 0.2182 -0.0207 0.0813  0.0763  123 ASN B CB  
5143 C CG  . ASN B 123 ? 0.3478 0.6490 0.2715 -0.0331 0.0858  0.0766  123 ASN B CG  
5144 O OD1 . ASN B 123 ? 0.3215 0.6214 0.2620 -0.0299 0.0811  0.0694  123 ASN B OD1 
5145 N ND2 . ASN B 123 ? 0.3929 0.6894 0.3113 -0.0482 0.0952  0.0846  123 ASN B ND2 
5146 N N   . ARG B 124 ? 0.2896 0.6255 0.2318 0.0003  0.0679  0.0395  124 ARG B N   
5147 C CA  . ARG B 124 ? 0.2600 0.6014 0.2210 0.0081  0.0630  0.0220  124 ARG B CA  
5148 C C   . ARG B 124 ? 0.2538 0.5874 0.2329 0.0041  0.0631  0.0211  124 ARG B C   
5149 O O   . ARG B 124 ? 0.2281 0.5526 0.2167 0.0107  0.0576  0.0143  124 ARG B O   
5150 C CB  . ARG B 124 ? 0.3032 0.6628 0.2697 0.0104  0.0654  0.0093  124 ARG B CB  
5151 C CG  . ARG B 124 ? 0.2359 0.5937 0.2190 0.0189  0.0609  -0.0069 124 ARG B CG  
5152 C CD  . ARG B 124 ? 0.2726 0.6445 0.2591 0.0230  0.0637  -0.0188 124 ARG B CD  
5153 N NE  . ARG B 124 ? 0.2451 0.6078 0.2435 0.0320  0.0596  -0.0319 124 ARG B NE  
5154 C CZ  . ARG B 124 ? 0.2849 0.6462 0.2982 0.0334  0.0596  -0.0342 124 ARG B CZ  
5155 N NH1 . ARG B 124 ? 0.2831 0.6548 0.3034 0.0249  0.0632  -0.0260 124 ARG B NH1 
5156 N NH2 . ARG B 124 ? 0.2974 0.6464 0.3177 0.0426  0.0562  -0.0445 124 ARG B NH2 
5157 N N   . GLU B 125 ? 0.2388 0.5765 0.2234 -0.0074 0.0693  0.0269  125 GLU B N   
5158 C CA  . GLU B 125 ? 0.2388 0.5730 0.2418 -0.0118 0.0683  0.0241  125 GLU B CA  
5159 C C   . GLU B 125 ? 0.2422 0.5541 0.2420 -0.0157 0.0666  0.0343  125 GLU B C   
5160 O O   . GLU B 125 ? 0.2194 0.5206 0.2333 -0.0140 0.0611  0.0287  125 GLU B O   
5161 C CB  . GLU B 125 ? 0.3908 0.7394 0.4011 -0.0238 0.0748  0.0252  125 GLU B CB  
5162 C CG  . GLU B 125 ? 0.5351 0.9060 0.5521 -0.0166 0.0754  0.0129  125 GLU B CG  
5163 C CD  . GLU B 125 ? 0.6166 0.9951 0.6166 -0.0144 0.0791  0.0145  125 GLU B CD  
5164 O OE1 . GLU B 125 ? 0.5970 0.9687 0.5803 -0.0229 0.0839  0.0275  125 GLU B OE1 
5165 O OE2 . GLU B 125 ? 0.6277 1.0161 0.6292 -0.0039 0.0772  0.0029  125 GLU B OE2 
5166 N N   . GLU B 126 ? 0.2515 0.5437 0.2315 -0.0182 0.0670  0.0480  126 GLU B N   
5167 C CA  . GLU B 126 ? 0.2547 0.5114 0.2303 -0.0177 0.0611  0.0556  126 GLU B CA  
5168 C C   . GLU B 126 ? 0.2454 0.4941 0.2256 -0.0031 0.0510  0.0467  126 GLU B C   
5169 O O   . GLU B 126 ? 0.2340 0.4628 0.2229 -0.0016 0.0457  0.0444  126 GLU B O   
5170 C CB  . GLU B 126 ? 0.2840 0.5213 0.2353 -0.0216 0.0648  0.0735  126 GLU B CB  
5171 C CG  . GLU B 126 ? 0.3328 0.5664 0.2789 -0.0402 0.0757  0.0836  126 GLU B CG  
5172 C CD  . GLU B 126 ? 0.4427 0.6623 0.3606 -0.0439 0.0822  0.1015  126 GLU B CD  
5173 O OE1 . GLU B 126 ? 0.4177 0.6404 0.3204 -0.0311 0.0783  0.1054  126 GLU B OE1 
5174 O OE2 . GLU B 126 ? 0.4844 0.6897 0.3941 -0.0604 0.0916  0.1117  126 GLU B OE2 
5175 N N   . LEU B 127 ? 0.2126 0.4775 0.1864 0.0065  0.0489  0.0407  127 LEU B N   
5176 C CA  . LEU B 127 ? 0.1891 0.4498 0.1681 0.0177  0.0405  0.0300  127 LEU B CA  
5177 C C   . LEU B 127 ? 0.1736 0.4364 0.1719 0.0194  0.0391  0.0160  127 LEU B C   
5178 O O   . LEU B 127 ? 0.1634 0.4103 0.1684 0.0239  0.0331  0.0107  127 LEU B O   
5179 C CB  . LEU B 127 ? 0.1949 0.4754 0.1627 0.0249  0.0395  0.0244  127 LEU B CB  
5180 C CG  . LEU B 127 ? 0.2895 0.5660 0.2369 0.0282  0.0368  0.0374  127 LEU B CG  
5181 C CD1 . LEU B 127 ? 0.2611 0.5636 0.1963 0.0330  0.0369  0.0311  127 LEU B CD1 
5182 C CD2 . LEU B 127 ? 0.2861 0.5430 0.2359 0.0352  0.0280  0.0391  127 LEU B CD2 
5183 N N   . LEU B 128 ? 0.1799 0.4629 0.1866 0.0166  0.0448  0.0104  128 LEU B N   
5184 C CA  . LEU B 128 ? 0.1876 0.4718 0.2111 0.0201  0.0432  -0.0007 128 LEU B CA  
5185 C C   . LEU B 128 ? 0.1665 0.4294 0.1979 0.0148  0.0395  0.0042  128 LEU B C   
5186 O O   . LEU B 128 ? 0.1296 0.3800 0.1686 0.0202  0.0345  -0.0029 128 LEU B O   
5187 C CB  . LEU B 128 ? 0.1797 0.4852 0.2108 0.0186  0.0480  -0.0057 128 LEU B CB  
5188 C CG  . LEU B 128 ? 0.2522 0.5635 0.2808 0.0274  0.0471  -0.0177 128 LEU B CG  
5189 C CD1 . LEU B 128 ? 0.2020 0.5317 0.2366 0.0248  0.0514  -0.0194 128 LEU B CD1 
5190 C CD2 . LEU B 128 ? 0.1915 0.4858 0.2255 0.0370  0.0417  -0.0288 128 LEU B CD2 
5191 N N   . ASP B 129 ? 0.1621 0.4190 0.1900 0.0034  0.0426  0.0159  129 ASP B N   
5192 C CA  . ASP B 129 ? 0.1921 0.4270 0.2252 -0.0028 0.0396  0.0195  129 ASP B CA  
5193 C C   . ASP B 129 ? 0.1932 0.4005 0.2205 0.0035  0.0334  0.0210  129 ASP B C   
5194 O O   . ASP B 129 ? 0.1386 0.3310 0.1731 0.0047  0.0291  0.0167  129 ASP B O   
5195 C CB  . ASP B 129 ? 0.2337 0.4640 0.2616 -0.0181 0.0456  0.0309  129 ASP B CB  
5196 C CG  . ASP B 129 ? 0.2447 0.5043 0.2844 -0.0273 0.0513  0.0275  129 ASP B CG  
5197 O OD1 . ASP B 129 ? 0.2295 0.5123 0.2816 -0.0189 0.0498  0.0167  129 ASP B OD1 
5198 O OD2 . ASP B 129 ? 0.2159 0.4747 0.2525 -0.0428 0.0574  0.0351  129 ASP B OD2 
5199 N N   . LEU B 130 ? 0.2078 0.4102 0.2218 0.0080  0.0328  0.0269  130 LEU B N   
5200 C CA  . LEU B 130 ? 0.1964 0.3788 0.2067 0.0152  0.0268  0.0276  130 LEU B CA  
5201 C C   . LEU B 130 ? 0.1927 0.3780 0.2127 0.0229  0.0221  0.0136  130 LEU B C   
5202 O O   . LEU B 130 ? 0.2162 0.3840 0.2406 0.0248  0.0184  0.0111  130 LEU B O   
5203 C CB  . LEU B 130 ? 0.2446 0.4292 0.2394 0.0207  0.0262  0.0358  130 LEU B CB  
5204 C CG  . LEU B 130 ? 0.3044 0.4722 0.2955 0.0290  0.0203  0.0385  130 LEU B CG  
5205 C CD1 . LEU B 130 ? 0.2464 0.3845 0.2368 0.0247  0.0213  0.0469  130 LEU B CD1 
5206 C CD2 . LEU B 130 ? 0.3078 0.4849 0.2836 0.0365  0.0184  0.0462  130 LEU B CD2 
5207 N N   . GLN B 131 ? 0.1552 0.3606 0.1771 0.0269  0.0233  0.0042  131 GLN B N   
5208 C CA  . GLN B 131 ? 0.1375 0.3414 0.1660 0.0331  0.0205  -0.0093 131 GLN B CA  
5209 C C   . GLN B 131 ? 0.1922 0.3845 0.2311 0.0317  0.0198  -0.0127 131 GLN B C   
5210 O O   . GLN B 131 ? 0.1202 0.2960 0.1620 0.0339  0.0166  -0.0172 131 GLN B O   
5211 C CB  . GLN B 131 ? 0.1238 0.3484 0.1506 0.0371  0.0237  -0.0189 131 GLN B CB  
5212 C CG  . GLN B 131 ? 0.1898 0.4270 0.2051 0.0397  0.0231  -0.0202 131 GLN B CG  
5213 C CD  . GLN B 131 ? 0.2062 0.4649 0.2183 0.0419  0.0281  -0.0282 131 GLN B CD  
5214 O OE1 . GLN B 131 ? 0.1719 0.4404 0.1892 0.0408  0.0330  -0.0278 131 GLN B OE1 
5215 N NE2 . GLN B 131 ? 0.2017 0.4693 0.2058 0.0451  0.0271  -0.0373 131 GLN B NE2 
5216 N N   . THR B 132 ? 0.1689 0.3723 0.2135 0.0279  0.0229  -0.0108 132 THR B N   
5217 C CA  . THR B 132 ? 0.1618 0.3606 0.2160 0.0284  0.0213  -0.0148 132 THR B CA  
5218 C C   . THR B 132 ? 0.1194 0.2967 0.1741 0.0222  0.0183  -0.0091 132 THR B C   
5219 O O   . THR B 132 ? 0.1632 0.3283 0.2216 0.0244  0.0152  -0.0134 132 THR B O   
5220 C CB  . THR B 132 ? 0.1065 0.3299 0.1683 0.0262  0.0250  -0.0149 132 THR B CB  
5221 O OG1 . THR B 132 ? 0.1449 0.3880 0.2047 0.0325  0.0289  -0.0205 132 THR B OG1 
5222 C CG2 . THR B 132 ? 0.1286 0.3523 0.2001 0.0303  0.0221  -0.0200 132 THR B CG2 
5223 N N   . LEU B 133 ? 0.1345 0.3052 0.1837 0.0146  0.0197  0.0007  133 LEU B N   
5224 C CA  . LEU B 133 ? 0.1175 0.2650 0.1656 0.0089  0.0178  0.0051  133 LEU B CA  
5225 C C   . LEU B 133 ? 0.1649 0.2933 0.2099 0.0154  0.0144  0.0025  133 LEU B C   
5226 O O   . LEU B 133 ? 0.1930 0.3041 0.2396 0.0138  0.0124  0.0010  133 LEU B O   
5227 C CB  . LEU B 133 ? 0.1339 0.2744 0.1743 -0.0007 0.0217  0.0163  133 LEU B CB  
5228 C CG  . LEU B 133 ? 0.2090 0.3671 0.2547 -0.0119 0.0258  0.0178  133 LEU B CG  
5229 C CD1 . LEU B 133 ? 0.2750 0.4259 0.3100 -0.0222 0.0318  0.0292  133 LEU B CD1 
5230 C CD2 . LEU B 133 ? 0.2251 0.3791 0.2792 -0.0182 0.0232  0.0133  133 LEU B CD2 
5231 N N   . ASN B 134 ? 0.1407 0.2744 0.1814 0.0222  0.0137  0.0011  134 ASN B N   
5232 C CA  . ASN B 134 ? 0.1504 0.2728 0.1913 0.0277  0.0107  -0.0040 134 ASN B CA  
5233 C C   . ASN B 134 ? 0.1617 0.2797 0.2083 0.0294  0.0097  -0.0142 134 ASN B C   
5234 O O   . ASN B 134 ? 0.1901 0.2919 0.2376 0.0294  0.0084  -0.0167 134 ASN B O   
5235 C CB  . ASN B 134 ? 0.1545 0.2900 0.1907 0.0334  0.0097  -0.0054 134 ASN B CB  
5236 C CG  . ASN B 134 ? 0.1861 0.3164 0.2150 0.0355  0.0087  0.0051  134 ASN B CG  
5237 O OD1 . ASN B 134 ? 0.2005 0.3183 0.2303 0.0387  0.0067  0.0058  134 ASN B OD1 
5238 N ND2 . ASN B 134 ? 0.1846 0.3235 0.2053 0.0344  0.0109  0.0140  134 ASN B ND2 
5239 N N   . LEU B 135 ? 0.1181 0.2490 0.1671 0.0317  0.0110  -0.0197 135 LEU B N   
5240 C CA  . LEU B 135 ? 0.1486 0.2712 0.2000 0.0350  0.0105  -0.0275 135 LEU B CA  
5241 C C   . LEU B 135 ? 0.1517 0.2636 0.2057 0.0313  0.0088  -0.0240 135 LEU B C   
5242 O O   . LEU B 135 ? 0.1482 0.2431 0.2006 0.0319  0.0075  -0.0270 135 LEU B O   
5243 C CB  . LEU B 135 ? 0.1496 0.2871 0.2026 0.0405  0.0127  -0.0331 135 LEU B CB  
5244 C CG  . LEU B 135 ? 0.1951 0.3397 0.2437 0.0447  0.0150  -0.0409 135 LEU B CG  
5245 C CD1 . LEU B 135 ? 0.1814 0.3383 0.2314 0.0514  0.0181  -0.0464 135 LEU B CD1 
5246 C CD2 . LEU B 135 ? 0.1781 0.3048 0.2232 0.0451  0.0147  -0.0486 135 LEU B CD2 
5247 N N   . LEU B 136 ? 0.1159 0.2391 0.1732 0.0263  0.0090  -0.0184 136 LEU B N   
5248 C CA  . LEU B 136 ? 0.1179 0.2357 0.1778 0.0217  0.0068  -0.0170 136 LEU B CA  
5249 C C   . LEU B 136 ? 0.1355 0.2306 0.1910 0.0161  0.0059  -0.0142 136 LEU B C   
5250 O O   . LEU B 136 ? 0.1350 0.2203 0.1898 0.0137  0.0037  -0.0157 136 LEU B O   
5251 C CB  . LEU B 136 ? 0.1588 0.2973 0.2242 0.0149  0.0080  -0.0131 136 LEU B CB  
5252 C CG  . LEU B 136 ? 0.1273 0.2922 0.1993 0.0215  0.0089  -0.0170 136 LEU B CG  
5253 C CD1 . LEU B 136 ? 0.0981 0.2875 0.1768 0.0122  0.0114  -0.0131 136 LEU B CD1 
5254 C CD2 . LEU B 136 ? 0.1467 0.3106 0.2211 0.0306  0.0053  -0.0225 136 LEU B CD2 
5255 N N   . ALA B 137 ? 0.1768 0.2639 0.2283 0.0152  0.0075  -0.0102 137 ALA B N   
5256 C CA  . ALA B 137 ? 0.1516 0.2168 0.1991 0.0123  0.0074  -0.0080 137 ALA B CA  
5257 C C   . ALA B 137 ? 0.1197 0.1724 0.1666 0.0164  0.0062  -0.0148 137 ALA B C   
5258 O O   . ALA B 137 ? 0.1482 0.1843 0.1922 0.0133  0.0061  -0.0151 137 ALA B O   
5259 C CB  . ALA B 137 ? 0.1433 0.2041 0.1866 0.0145  0.0090  -0.0021 137 ALA B CB  
5260 N N   . TRP B 138 ? 0.1263 0.1851 0.1743 0.0224  0.0061  -0.0206 138 TRP B N   
5261 C CA  . TRP B 138 ? 0.1171 0.1629 0.1629 0.0246  0.0065  -0.0270 138 TRP B CA  
5262 C C   . TRP B 138 ? 0.1407 0.1829 0.1841 0.0262  0.0053  -0.0299 138 TRP B C   
5263 O O   . TRP B 138 ? 0.1521 0.1826 0.1911 0.0287  0.0067  -0.0348 138 TRP B O   
5264 C CB  . TRP B 138 ? 0.0960 0.1476 0.1425 0.0284  0.0080  -0.0325 138 TRP B CB  
5265 C CG  . TRP B 138 ? 0.1094 0.1662 0.1577 0.0290  0.0079  -0.0296 138 TRP B CG  
5266 C CD1 . TRP B 138 ? 0.1726 0.2428 0.2210 0.0306  0.0072  -0.0240 138 TRP B CD1 
5267 C CD2 . TRP B 138 ? 0.1152 0.1649 0.1647 0.0295  0.0087  -0.0315 138 TRP B CD2 
5268 N NE1 . TRP B 138 ? 0.1268 0.1976 0.1755 0.0334  0.0066  -0.0215 138 TRP B NE1 
5269 C CE2 . TRP B 138 ? 0.1590 0.2190 0.2098 0.0332  0.0075  -0.0266 138 TRP B CE2 
5270 C CE3 . TRP B 138 ? 0.1599 0.1966 0.2090 0.0276  0.0107  -0.0368 138 TRP B CE3 
5271 C CZ2 . TRP B 138 ? 0.2018 0.2616 0.2552 0.0369  0.0075  -0.0271 138 TRP B CZ2 
5272 C CZ3 . TRP B 138 ? 0.2188 0.2562 0.2712 0.0294  0.0117  -0.0381 138 TRP B CZ3 
5273 C CH2 . TRP B 138 ? 0.2412 0.2912 0.2967 0.0348  0.0098  -0.0335 138 TRP B CH2 
5274 N N   . CYS B 139 ? 0.1487 0.2011 0.1943 0.0249  0.0031  -0.0266 139 CYS B N   
5275 C CA  . CYS B 139 ? 0.1044 0.1568 0.1478 0.0289  0.0008  -0.0284 139 CYS B CA  
5276 C C   . CYS B 139 ? 0.1194 0.1521 0.1552 0.0264  -0.0002 -0.0292 139 CYS B C   
5277 O O   . CYS B 139 ? 0.1561 0.1817 0.1909 0.0192  -0.0004 -0.0275 139 CYS B O   
5278 C CB  . CYS B 139 ? 0.1128 0.1866 0.1625 0.0269  -0.0019 -0.0253 139 CYS B CB  
5279 S SG  . CYS B 139 ? 0.1905 0.2736 0.2393 0.0366  -0.0060 -0.0271 139 CYS B SG  
5280 N N   . GLY B 140 ? 0.1318 0.1532 0.1602 0.0326  0.0001  -0.0319 140 GLY B N   
5281 C CA  . GLY B 140 ? 0.1771 0.1794 0.1955 0.0305  0.0000  -0.0324 140 GLY B CA  
5282 C C   . GLY B 140 ? 0.1594 0.1681 0.1746 0.0309  -0.0055 -0.0298 140 GLY B C   
5283 O O   . GLY B 140 ? 0.1536 0.1834 0.1757 0.0337  -0.0092 -0.0281 140 GLY B O   
5284 N N   . ARG B 141 ? 0.1425 0.1352 0.1470 0.0279  -0.0059 -0.0301 141 ARG B N   
5285 C CA  . ARG B 141 ? 0.1506 0.1501 0.1499 0.0273  -0.0120 -0.0284 141 ARG B CA  
5286 C C   . ARG B 141 ? 0.1563 0.1698 0.1550 0.0392  -0.0166 -0.0262 141 ARG B C   
5287 O O   . ARG B 141 ? 0.1650 0.2028 0.1702 0.0393  -0.0226 -0.0251 141 ARG B O   
5288 C CB  . ARG B 141 ? 0.1689 0.1461 0.1528 0.0244  -0.0106 -0.0294 141 ARG B CB  
5289 C CG  . ARG B 141 ? 0.2057 0.1896 0.1808 0.0236  -0.0174 -0.0283 141 ARG B CG  
5290 C CD  . ARG B 141 ? 0.2212 0.1826 0.1805 0.0181  -0.0146 -0.0301 141 ARG B CD  
5291 N NE  . ARG B 141 ? 0.2305 0.1977 0.1776 0.0186  -0.0214 -0.0290 141 ARG B NE  
5292 C CZ  . ARG B 141 ? 0.2620 0.2220 0.1936 0.0286  -0.0240 -0.0250 141 ARG B CZ  
5293 N NH1 . ARG B 141 ? 0.2415 0.1842 0.1671 0.0379  -0.0190 -0.0221 141 ARG B NH1 
5294 N NH2 . ARG B 141 ? 0.2976 0.2668 0.2180 0.0291  -0.0314 -0.0240 141 ARG B NH2 
5295 N N   . THR B 142 ? 0.1649 0.1637 0.1560 0.0496  -0.0135 -0.0259 142 THR B N   
5296 C CA  . THR B 142 ? 0.2196 0.2259 0.2070 0.0644  -0.0172 -0.0233 142 THR B CA  
5297 C C   . THR B 142 ? 0.2435 0.2816 0.2479 0.0687  -0.0196 -0.0238 142 THR B C   
5298 O O   . THR B 142 ? 0.2442 0.3065 0.2530 0.0758  -0.0259 -0.0220 142 THR B O   
5299 C CB  . THR B 142 ? 0.1929 0.1704 0.1670 0.0733  -0.0111 -0.0236 142 THR B CB  
5300 O OG1 . THR B 142 ? 0.2446 0.1942 0.2015 0.0688  -0.0083 -0.0225 142 THR B OG1 
5301 C CG2 . THR B 142 ? 0.2723 0.2539 0.2414 0.0916  -0.0141 -0.0205 142 THR B CG2 
5302 N N   . LEU B 143 ? 0.1522 0.1932 0.1660 0.0650  -0.0145 -0.0265 143 LEU B N   
5303 C CA  . LEU B 143 ? 0.1840 0.2539 0.2119 0.0692  -0.0151 -0.0272 143 LEU B CA  
5304 C C   . LEU B 143 ? 0.1897 0.2868 0.2305 0.0573  -0.0182 -0.0262 143 LEU B C   
5305 O O   . LEU B 143 ? 0.2089 0.3344 0.2617 0.0594  -0.0187 -0.0265 143 LEU B O   
5306 C CB  . LEU B 143 ? 0.2224 0.2863 0.2531 0.0697  -0.0084 -0.0307 143 LEU B CB  
5307 C CG  . LEU B 143 ? 0.2385 0.2810 0.2584 0.0818  -0.0042 -0.0336 143 LEU B CG  
5308 C CD1 . LEU B 143 ? 0.1877 0.2289 0.2112 0.0789  0.0020  -0.0388 143 LEU B CD1 
5309 C CD2 . LEU B 143 ? 0.2459 0.3008 0.2656 0.0986  -0.0072 -0.0322 143 LEU B CD2 
5310 N N   . ARG B 144 ? 0.2636 0.3514 0.3014 0.0443  -0.0191 -0.0256 144 ARG B N   
5311 C CA  . ARG B 144 ? 0.3029 0.4121 0.3502 0.0315  -0.0215 -0.0251 144 ARG B CA  
5312 C C   . ARG B 144 ? 0.3374 0.4789 0.3915 0.0357  -0.0281 -0.0253 144 ARG B C   
5313 O O   . ARG B 144 ? 0.2495 0.4189 0.3159 0.0269  -0.0287 -0.0259 144 ARG B O   
5314 C CB  . ARG B 144 ? 0.3195 0.4084 0.3589 0.0188  -0.0213 -0.0256 144 ARG B CB  
5315 C CG  . ARG B 144 ? 0.4697 0.5446 0.5109 0.0098  -0.0152 -0.0249 144 ARG B CG  
5316 C CD  . ARG B 144 ? 0.5533 0.5988 0.5842 0.0052  -0.0128 -0.0261 144 ARG B CD  
5317 N NE  . ARG B 144 ? 0.4728 0.5057 0.5054 0.0019  -0.0073 -0.0250 144 ARG B NE  
5318 C CZ  . ARG B 144 ? 0.5022 0.5359 0.5381 -0.0071 -0.0052 -0.0226 144 ARG B CZ  
5319 N NH1 . ARG B 144 ? 0.5246 0.5713 0.5633 -0.0168 -0.0072 -0.0224 144 ARG B NH1 
5320 N NH2 . ARG B 144 ? 0.4090 0.4306 0.4446 -0.0067 -0.0009 -0.0205 144 ARG B NH2 
5321 N N   . LYS B 145 ? 0.3301 0.4695 0.3763 0.0495  -0.0327 -0.0246 145 LYS B N   
5322 C CA  . LYS B 145 ? 0.3634 0.5373 0.4167 0.0575  -0.0399 -0.0246 145 LYS B CA  
5323 C C   . LYS B 145 ? 0.3442 0.5424 0.4098 0.0702  -0.0379 -0.0251 145 LYS B C   
5324 O O   . LYS B 145 ? 0.3084 0.5460 0.3898 0.0670  -0.0400 -0.0267 145 LYS B O   
5325 C CB  . LYS B 145 ? 0.4979 0.6590 0.5353 0.0702  -0.0458 -0.0221 145 LYS B CB  
5326 C CG  . LYS B 145 ? 0.6105 0.7895 0.6490 0.0930  -0.0500 -0.0200 145 LYS B CG  
5327 C CD  . LYS B 145 ? 0.7088 0.9371 0.7610 0.0938  -0.0590 -0.0212 145 LYS B CD  
5328 C CE  . LYS B 145 ? 0.7519 0.9856 0.7956 0.1156  -0.0641 -0.0173 145 LYS B CE  
5329 N NZ  . LYS B 145 ? 0.7314 1.0066 0.7894 0.1134  -0.0667 -0.0194 145 LYS B NZ  
5330 N N   . ASP B 146 ? 0.3458 0.5217 0.4044 0.0836  -0.0330 -0.0248 146 ASP B N   
5331 C CA  . ASP B 146 ? 0.3556 0.5520 0.4237 0.0976  -0.0304 -0.0264 146 ASP B CA  
5332 C C   . ASP B 146 ? 0.3275 0.5451 0.4101 0.0852  -0.0252 -0.0286 146 ASP B C   
5333 O O   . ASP B 146 ? 0.3251 0.5654 0.4149 0.0864  -0.0234 -0.0293 146 ASP B O   
5334 C CB  . ASP B 146 ? 0.5232 0.6857 0.5779 0.1122  -0.0250 -0.0271 146 ASP B CB  
5335 C CG  . ASP B 146 ? 0.7679 0.8999 0.8036 0.1221  -0.0279 -0.0237 146 ASP B CG  
5336 O OD1 . ASP B 146 ? 0.8011 0.9175 0.8284 0.1107  -0.0302 -0.0217 146 ASP B OD1 
5337 O OD2 . ASP B 146 ? 0.8640 0.9827 0.8899 0.1388  -0.0264 -0.0226 146 ASP B OD2 
5338 N N   . LEU B 147 ? 0.1302 0.3276 0.2093 0.0695  -0.0210 -0.0281 147 LEU B N   
5339 C CA  . LEU B 147 ? 0.1567 0.3675 0.2448 0.0591  -0.0154 -0.0284 147 LEU B CA  
5340 C C   . LEU B 147 ? 0.1457 0.3754 0.2420 0.0402  -0.0165 -0.0269 147 LEU B C   
5341 O O   . LEU B 147 ? 0.1267 0.3597 0.2264 0.0289  -0.0112 -0.0254 147 LEU B O   
5342 C CB  . LEU B 147 ? 0.1529 0.3319 0.2317 0.0554  -0.0099 -0.0284 147 LEU B CB  
5343 C CG  . LEU B 147 ? 0.1906 0.3516 0.2615 0.0702  -0.0068 -0.0318 147 LEU B CG  
5344 C CD1 . LEU B 147 ? 0.2066 0.3434 0.2705 0.0638  -0.0021 -0.0330 147 LEU B CD1 
5345 C CD2 . LEU B 147 ? 0.2869 0.4723 0.3648 0.0814  -0.0043 -0.0346 147 LEU B CD2 
5346 N N   . LYS B 148 ? 0.1664 0.4084 0.2647 0.0363  -0.0230 -0.0273 148 LYS B N   
5347 C CA  . LYS B 148 ? 0.1140 0.3695 0.2179 0.0156  -0.0233 -0.0273 148 LYS B CA  
5348 C C   . LYS B 148 ? 0.1050 0.3955 0.2235 0.0079  -0.0187 -0.0277 148 LYS B C   
5349 O O   . LYS B 148 ? 0.1864 0.4730 0.3051 -0.0103 -0.0137 -0.0259 148 LYS B O   
5350 C CB  . LYS B 148 ? 0.1824 0.4522 0.2866 0.0134  -0.0318 -0.0296 148 LYS B CB  
5351 C CG  . LYS B 148 ? 0.2124 0.4947 0.3211 -0.0103 -0.0320 -0.0317 148 LYS B CG  
5352 C CD  . LYS B 148 ? 0.3102 0.6013 0.4152 -0.0133 -0.0409 -0.0351 148 LYS B CD  
5353 C CE  . LYS B 148 ? 0.4058 0.7181 0.5178 -0.0380 -0.0411 -0.0395 148 LYS B CE  
5354 N NZ  . LYS B 148 ? 0.4600 0.7362 0.5631 -0.0568 -0.0330 -0.0383 148 LYS B NZ  
5355 N N   . ASP B 149 ? 0.1097 0.4182 0.2318 0.0211  -0.0182 -0.0288 149 ASP B N   
5356 C CA  . ASP B 149 ? 0.1818 0.5117 0.3105 0.0147  -0.0120 -0.0288 149 ASP B CA  
5357 C C   . ASP B 149 ? 0.1840 0.5017 0.3105 0.0068  -0.0042 -0.0259 149 ASP B C   
5358 O O   . ASP B 149 ? 0.1391 0.4674 0.2688 -0.0098 0.0010  -0.0239 149 ASP B O   
5359 C CB  . ASP B 149 ? 0.3360 0.6780 0.4653 0.0332  -0.0116 -0.0309 149 ASP B CB  
5360 C CG  . ASP B 149 ? 0.5042 0.8651 0.6365 0.0416  -0.0186 -0.0329 149 ASP B CG  
5361 O OD1 . ASP B 149 ? 0.5454 0.9180 0.6811 0.0297  -0.0231 -0.0336 149 ASP B OD1 
5362 O OD2 . ASP B 149 ? 0.5229 0.8869 0.6533 0.0601  -0.0193 -0.0340 149 ASP B OD2 
5363 N N   . LEU B 150 ? 0.1072 0.4025 0.2267 0.0186  -0.0028 -0.0254 150 LEU B N   
5364 C CA  . LEU B 150 ? 0.1510 0.4373 0.2670 0.0136  0.0041  -0.0227 150 LEU B CA  
5365 C C   . LEU B 150 ? 0.1549 0.4158 0.2635 -0.0020 0.0052  -0.0179 150 LEU B C   
5366 O O   . LEU B 150 ? 0.1754 0.4337 0.2808 -0.0129 0.0110  -0.0133 150 LEU B O   
5367 C CB  . LEU B 150 ? 0.1267 0.3932 0.2344 0.0300  0.0052  -0.0249 150 LEU B CB  
5368 C CG  . LEU B 150 ? 0.2493 0.5244 0.3555 0.0433  0.0065  -0.0286 150 LEU B CG  
5369 C CD1 . LEU B 150 ? 0.2649 0.5152 0.3611 0.0565  0.0077  -0.0320 150 LEU B CD1 
5370 C CD2 . LEU B 150 ? 0.2246 0.5212 0.3339 0.0359  0.0123  -0.0276 150 LEU B CD2 
5371 N N   . LEU B 151 ? 0.1488 0.3863 0.2512 -0.0029 0.0000  -0.0184 151 LEU B N   
5372 C CA  . LEU B 151 ? 0.2151 0.4236 0.3083 -0.0166 0.0012  -0.0147 151 LEU B CA  
5373 C C   . LEU B 151 ? 0.2038 0.4256 0.3010 -0.0365 0.0044  -0.0129 151 LEU B C   
5374 O O   . LEU B 151 ? 0.3182 0.5207 0.4077 -0.0475 0.0098  -0.0076 151 LEU B O   
5375 C CB  . LEU B 151 ? 0.2018 0.3875 0.2882 -0.0138 -0.0044 -0.0172 151 LEU B CB  
5376 C CG  . LEU B 151 ? 0.2335 0.3960 0.3122 0.0011  -0.0052 -0.0182 151 LEU B CG  
5377 C CD1 . LEU B 151 ? 0.1921 0.3393 0.2644 0.0054  -0.0105 -0.0209 151 LEU B CD1 
5378 C CD2 . LEU B 151 ? 0.2144 0.3522 0.2856 -0.0017 -0.0007 -0.0148 151 LEU B CD2 
5379 N N   . ASN B 152 ? 0.1820 0.4366 0.2907 -0.0414 0.0013  -0.0171 152 ASN B N   
5380 C CA  . ASN B 152 ? 0.1908 0.4615 0.3044 -0.0633 0.0049  -0.0171 152 ASN B CA  
5381 C C   . ASN B 152 ? 0.2479 0.5388 0.3663 -0.0696 0.0134  -0.0135 152 ASN B C   
5382 O O   . ASN B 152 ? 0.2806 0.5723 0.3976 -0.0903 0.0195  -0.0111 152 ASN B O   
5383 C CB  . ASN B 152 ? 0.2980 0.6049 0.4242 -0.0673 -0.0016 -0.0240 152 ASN B CB  
5384 C CG  . ASN B 152 ? 0.3910 0.6786 0.5097 -0.0659 -0.0094 -0.0273 152 ASN B CG  
5385 O OD1 . ASN B 152 ? 0.3931 0.6395 0.4977 -0.0695 -0.0080 -0.0251 152 ASN B OD1 
5386 N ND2 . ASN B 152 ? 0.4735 0.7890 0.5993 -0.0596 -0.0173 -0.0323 152 ASN B ND2 
5387 N N   . LYS B 153 ? 0.2250 0.5316 0.3477 -0.0533 0.0146  -0.0135 153 LYS B N   
5388 C CA  . LYS B 153 ? 0.2008 0.5217 0.3233 -0.0574 0.0226  -0.0103 153 LYS B CA  
5389 C C   . LYS B 153 ? 0.1914 0.4851 0.3009 -0.0696 0.0302  -0.0015 153 LYS B C   
5390 O O   . LYS B 153 ? 0.2132 0.5142 0.3211 -0.0870 0.0380  0.0027  153 LYS B O   
5391 C CB  . LYS B 153 ? 0.2507 0.5801 0.3735 -0.0358 0.0220  -0.0129 153 LYS B CB  
5392 C CG  . LYS B 153 ? 0.2802 0.6263 0.4018 -0.0382 0.0292  -0.0113 153 LYS B CG  
5393 C CD  . LYS B 153 ? 0.2715 0.6218 0.3914 -0.0174 0.0284  -0.0155 153 LYS B CD  
5394 C CE  . LYS B 153 ? 0.3354 0.7036 0.4535 -0.0202 0.0355  -0.0148 153 LYS B CE  
5395 N NZ  . LYS B 153 ? 0.3496 0.7201 0.4651 -0.0013 0.0349  -0.0202 153 LYS B NZ  
5396 N N   . GLY B 154 ? 0.2386 0.4955 0.3353 -0.0592 0.0278  0.0016  154 GLY B N   
5397 C CA  . GLY B 154 ? 0.2478 0.4694 0.3283 -0.0663 0.0324  0.0104  154 GLY B CA  
5398 C C   . GLY B 154 ? 0.2199 0.4435 0.2921 -0.0625 0.0385  0.0171  154 GLY B C   
5399 O O   . GLY B 154 ? 0.2916 0.4851 0.3492 -0.0608 0.0401  0.0246  154 GLY B O   
5400 N N   . ARG B 155 ? 0.2287 0.4881 0.3093 -0.0601 0.0420  0.0146  155 ARG B N   
5401 C CA  . ARG B 155 ? 0.2183 0.4829 0.2893 -0.0594 0.0489  0.0209  155 ARG B CA  
5402 C C   . ARG B 155 ? 0.2132 0.5201 0.2965 -0.0518 0.0511  0.0139  155 ARG B C   
5403 O O   . ARG B 155 ? 0.2565 0.5802 0.3528 -0.0465 0.0461  0.0051  155 ARG B O   
5404 C CB  . ARG B 155 ? 0.2632 0.5182 0.3237 -0.0799 0.0578  0.0309  155 ARG B CB  
5405 C CG  . ARG B 155 ? 0.3916 0.6773 0.4659 -0.0977 0.0624  0.0268  155 ARG B CG  
5406 C CD  . ARG B 155 ? 0.4442 0.7116 0.5051 -0.1200 0.0719  0.0361  155 ARG B CD  
5407 N NE  . ARG B 155 ? 0.4887 0.7096 0.5358 -0.1260 0.0709  0.0419  155 ARG B NE  
5408 C CZ  . ARG B 155 ? 0.5080 0.6907 0.5329 -0.1271 0.0757  0.0542  155 ARG B CZ  
5409 N NH1 . ARG B 155 ? 0.5757 0.7148 0.5889 -0.1295 0.0743  0.0578  155 ARG B NH1 
5410 N NH2 . ARG B 155 ? 0.4602 0.6483 0.4734 -0.1251 0.0823  0.0629  155 ARG B NH2 
5411 N N   . ASN B 156 ? 0.1707 0.4855 0.2450 -0.0490 0.0569  0.0175  156 ASN B N   
5412 C CA  . ASN B 156 ? 0.1891 0.5273 0.2672 -0.0417 0.0578  0.0107  156 ASN B CA  
5413 C C   . ASN B 156 ? 0.1955 0.5371 0.2810 -0.0221 0.0503  -0.0004 156 ASN B C   
5414 O O   . ASN B 156 ? 0.1994 0.5582 0.2937 -0.0167 0.0484  -0.0075 156 ASN B O   
5415 C CB  . ASN B 156 ? 0.2712 0.6289 0.3578 -0.0554 0.0610  0.0093  156 ASN B CB  
5416 C CG  . ASN B 156 ? 0.3940 0.7450 0.4693 -0.0749 0.0704  0.0198  156 ASN B CG  
5417 O OD1 . ASN B 156 ? 0.4887 0.8318 0.5489 -0.0741 0.0756  0.0271  156 ASN B OD1 
5418 N ND2 . ASN B 156 ? 0.4282 0.7802 0.5085 -0.0925 0.0726  0.0205  156 ASN B ND2 
5419 N N   . TYR B 157 ? 0.1367 0.4598 0.2170 -0.0114 0.0466  -0.0015 157 TYR B N   
5420 C CA  . TYR B 157 ? 0.1285 0.4460 0.2114 0.0058  0.0407  -0.0112 157 TYR B CA  
5421 C C   . TYR B 157 ? 0.1924 0.5171 0.2682 0.0149  0.0432  -0.0163 157 TYR B C   
5422 O O   . TYR B 157 ? 0.2691 0.5963 0.3348 0.0113  0.0476  -0.0121 157 TYR B O   
5423 C CB  . TYR B 157 ? 0.1179 0.4114 0.1973 0.0117  0.0363  -0.0114 157 TYR B CB  
5424 C CG  . TYR B 157 ? 0.1153 0.3983 0.2006 0.0037  0.0330  -0.0077 157 TYR B CG  
5425 C CD1 . TYR B 157 ? 0.1187 0.4056 0.2140 0.0073  0.0280  -0.0129 157 TYR B CD1 
5426 C CD2 . TYR B 157 ? 0.1201 0.3779 0.1953 -0.0068 0.0331  0.0011  157 TYR B CD2 
5427 C CE1 . TYR B 157 ? 0.1482 0.4217 0.2457 -0.0011 0.0239  -0.0104 157 TYR B CE1 
5428 C CE2 . TYR B 157 ? 0.1237 0.3627 0.1999 -0.0146 0.0296  0.0034  157 TYR B CE2 
5429 C CZ  . TYR B 157 ? 0.1579 0.4053 0.2451 -0.0125 0.0250  -0.0029 157 TYR B CZ  
5430 O OH  . TYR B 157 ? 0.1174 0.3468 0.2039 -0.0209 0.0215  -0.0017 157 TYR B OH  
5431 N N   . THR B 158 ? 0.1872 0.5145 0.2670 0.0268  0.0406  -0.0248 158 THR B N   
5432 C CA  . THR B 158 ? 0.2354 0.5667 0.3090 0.0360  0.0430  -0.0314 158 THR B CA  
5433 C C   . THR B 158 ? 0.1440 0.4510 0.2097 0.0460  0.0398  -0.0372 158 THR B C   
5434 O O   . THR B 158 ? 0.1349 0.4231 0.2017 0.0477  0.0355  -0.0368 158 THR B O   
5435 C CB  . THR B 158 ? 0.1802 0.5279 0.2621 0.0436  0.0433  -0.0374 158 THR B CB  
5436 O OG1 . THR B 158 ? 0.1888 0.5235 0.2757 0.0532  0.0378  -0.0407 158 THR B OG1 
5437 C CG2 . THR B 158 ? 0.2043 0.5791 0.2953 0.0324  0.0465  -0.0332 158 THR B CG2 
5438 N N   . GLN B 159 ? 0.2136 0.4908 0.2866 0.0347  0.0342  -0.1421 159 GLN B N   
5439 C CA  . GLN B 159 ? 0.2584 0.5104 0.3278 0.0400  0.0331  -0.1470 159 GLN B CA  
5440 C C   . GLN B 159 ? 0.2288 0.4676 0.3116 0.0527  0.0308  -0.1478 159 GLN B C   
5441 O O   . GLN B 159 ? 0.2072 0.4229 0.2877 0.0561  0.0269  -0.1467 159 GLN B O   
5442 C CB  . GLN B 159 ? 0.2598 0.5132 0.3243 0.0385  0.0384  -0.1554 159 GLN B CB  
5443 C CG  . GLN B 159 ? 0.2719 0.5008 0.3332 0.0429  0.0384  -0.1613 159 GLN B CG  
5444 C CD  . GLN B 159 ? 0.2999 0.5130 0.3479 0.0357  0.0341  -0.1573 159 GLN B CD  
5445 O OE1 . GLN B 159 ? 0.2414 0.4636 0.2795 0.0262  0.0329  -0.1520 159 GLN B OE1 
5446 N NE2 . GLN B 159 ? 0.2818 0.4709 0.3291 0.0400  0.0320  -0.1592 159 GLN B NE2 
5447 N N   . GLU B 160 ? 0.1914 0.4448 0.2882 0.0596  0.0328  -0.1484 160 GLU B N   
5448 C CA  . GLU B 160 ? 0.1954 0.4383 0.3057 0.0722  0.0306  -0.1473 160 GLU B CA  
5449 C C   . GLU B 160 ? 0.2259 0.4619 0.3389 0.0730  0.0232  -0.1385 160 GLU B C   
5450 O O   . GLU B 160 ? 0.2200 0.4351 0.3364 0.0806  0.0195  -0.1368 160 GLU B O   
5451 C CB  . GLU B 160 ? 0.2805 0.5446 0.4052 0.0784  0.0345  -0.1485 160 GLU B CB  
5452 C CG  . GLU B 160 ? 0.4417 0.7092 0.5652 0.0800  0.0425  -0.1584 160 GLU B CG  
5453 C CD  . GLU B 160 ? 0.4646 0.7481 0.5757 0.0674  0.0462  -0.1615 160 GLU B CD  
5454 O OE1 . GLU B 160 ? 0.3851 0.6816 0.4905 0.0576  0.0436  -0.1553 160 GLU B OE1 
5455 O OE2 . GLU B 160 ? 0.5424 0.8244 0.6488 0.0669  0.0518  -0.1697 160 GLU B OE2 
5456 N N   . GLU B 161 ? 0.1677 0.4203 0.2786 0.0646  0.0209  -0.1324 161 GLU B N   
5457 C CA  . GLU B 161 ? 0.2054 0.4523 0.3187 0.0645  0.0140  -0.1242 161 GLU B CA  
5458 C C   . GLU B 161 ? 0.2529 0.4693 0.3511 0.0608  0.0103  -0.1221 161 GLU B C   
5459 O O   . GLU B 161 ? 0.1795 0.3765 0.2786 0.0647  0.0044  -0.1167 161 GLU B O   
5460 C CB  . GLU B 161 ? 0.1621 0.4266 0.2720 0.0523  0.0118  -0.1154 161 GLU B CB  
5461 C CG  . GLU B 161 ? 0.1469 0.4414 0.2732 0.0554  0.0135  -0.1151 161 GLU B CG  
5462 C CD  . GLU B 161 ? 0.2732 0.5892 0.3958 0.0415  0.0139  -0.1093 161 GLU B CD  
5463 O OE1 . GLU B 161 ? 0.2533 0.5592 0.3592 0.0297  0.0138  -0.1058 161 GLU B OE1 
5464 O OE2 . GLU B 161 ? 0.3521 0.6884 0.4846 0.0411  0.0137  -0.1063 161 GLU B OE2 
5465 N N   . LYS B 162 ? 0.2149 0.4281 0.2994 0.0531  0.0137  -0.1261 162 LYS B N   
5466 C CA  . LYS B 162 ? 0.1984 0.3860 0.2693 0.0494  0.0105  -0.1243 162 LYS B CA  
5467 C C   . LYS B 162 ? 0.1640 0.3314 0.2398 0.0598  0.0103  -0.1306 162 LYS B C   
5468 O O   . LYS B 162 ? 0.1733 0.3186 0.2451 0.0602  0.0050  -0.1253 162 LYS B O   
5469 C CB  . LYS B 162 ? 0.1581 0.3510 0.2154 0.0403  0.0147  -0.1281 162 LYS B CB  
5470 C CG  . LYS B 162 ? 0.1979 0.3683 0.2421 0.0365  0.0118  -0.1271 162 LYS B CG  
5471 C CD  . LYS B 162 ? 0.1865 0.3659 0.2172 0.0270  0.0151  -0.1290 162 LYS B CD  
5472 C CE  . LYS B 162 ? 0.2186 0.4078 0.2521 0.0278  0.0204  -0.1370 162 LYS B CE  
5473 N NZ  . LYS B 162 ? 0.2378 0.4323 0.2587 0.0181  0.0219  -0.1363 162 LYS B NZ  
5474 N N   . GLU B 163 ? 0.1769 0.3462 0.2587 0.0653  0.0149  -0.1376 163 GLU B N   
5475 C CA  . GLU B 163 ? 0.2651 0.4107 0.3494 0.0726  0.0146  -0.1401 163 GLU B CA  
5476 C C   . GLU B 163 ? 0.2562 0.3935 0.3521 0.0821  0.0099  -0.1339 163 GLU B C   
5477 O O   . GLU B 163 ? 0.2817 0.3948 0.3761 0.0856  0.0072  -0.1318 163 GLU B O   
5478 C CB  . GLU B 163 ? 0.2583 0.4084 0.3462 0.0760  0.0215  -0.1483 163 GLU B CB  
5479 C CG  . GLU B 163 ? 0.2680 0.4247 0.3437 0.0663  0.0256  -0.1541 163 GLU B CG  
5480 C CD  . GLU B 163 ? 0.4151 0.5776 0.4940 0.0694  0.0329  -0.1630 163 GLU B CD  
5481 O OE1 . GLU B 163 ? 0.4060 0.5826 0.4969 0.0765  0.0358  -0.1641 163 GLU B OE1 
5482 O OE2 . GLU B 163 ? 0.4514 0.6057 0.5207 0.0646  0.0357  -0.1687 163 GLU B OE2 
5483 N N   . TYR B 164 ? 0.2175 0.3757 0.3247 0.0855  0.0086  -0.1299 164 TYR B N   
5484 C CA  . TYR B 164 ? 0.2065 0.3602 0.3239 0.0931  0.0028  -0.1219 164 TYR B CA  
5485 C C   . TYR B 164 ? 0.2172 0.3551 0.3268 0.0891  -0.0040 -0.1157 164 TYR B C   
5486 O O   . TYR B 164 ? 0.1875 0.3055 0.2987 0.0945  -0.0083 -0.1110 164 TYR B O   
5487 C CB  . TYR B 164 ? 0.2737 0.4569 0.4033 0.0943  0.0020  -0.1178 164 TYR B CB  
5488 C CG  . TYR B 164 ? 0.3137 0.4969 0.4540 0.1010  -0.0048 -0.1083 164 TYR B CG  
5489 C CD1 . TYR B 164 ? 0.3778 0.5528 0.5284 0.1123  -0.0046 -0.1063 164 TYR B CD1 
5490 C CD2 . TYR B 164 ? 0.2799 0.4699 0.4179 0.0942  -0.0116 -0.0995 164 TYR B CD2 
5491 C CE1 . TYR B 164 ? 0.3913 0.5676 0.5509 0.1179  -0.0112 -0.0963 164 TYR B CE1 
5492 C CE2 . TYR B 164 ? 0.3278 0.5195 0.4743 0.0990  -0.0185 -0.0904 164 TYR B CE2 
5493 C CZ  . TYR B 164 ? 0.4078 0.5936 0.5654 0.1113  -0.0185 -0.0888 164 TYR B CZ  
5494 O OH  . TYR B 164 ? 0.4865 0.6746 0.6514 0.1155  -0.0256 -0.0783 164 TYR B OH  
5495 N N   . VAL B 165 ? 0.1695 0.3111 0.2663 0.0763  -0.0053 -0.1113 165 VAL B N   
5496 C CA  . VAL B 165 ? 0.2023 0.3246 0.2872 0.0692  -0.0112 -0.1026 165 VAL B CA  
5497 C C   . VAL B 165 ? 0.2211 0.3177 0.2991 0.0711  -0.0110 -0.1066 165 VAL B C   
5498 O O   . VAL B 165 ? 0.2122 0.2896 0.2876 0.0722  -0.0159 -0.1007 165 VAL B O   
5499 C CB  . VAL B 165 ? 0.1807 0.3104 0.2532 0.0559  -0.0113 -0.0983 165 VAL B CB  
5500 C CG1 . VAL B 165 ? 0.1411 0.2491 0.2014 0.0498  -0.0162 -0.0907 165 VAL B CG1 
5501 C CG2 . VAL B 165 ? 0.2072 0.3594 0.2854 0.0521  -0.0122 -0.0933 165 VAL B CG2 
5502 N N   . LEU B 166 ? 0.1808 0.2774 0.2548 0.0703  -0.0054 -0.1166 166 LEU B N   
5503 C CA  . LEU B 166 ? 0.2439 0.3172 0.3108 0.0699  -0.0051 -0.1201 166 LEU B CA  
5504 C C   . LEU B 166 ? 0.2771 0.3330 0.3517 0.0783  -0.0064 -0.1176 166 LEU B C   
5505 O O   . LEU B 166 ? 0.2108 0.2450 0.2800 0.0770  -0.0094 -0.1133 166 LEU B O   
5506 C CB  . LEU B 166 ? 0.2399 0.3175 0.3004 0.0647  0.0008  -0.1276 166 LEU B CB  
5507 C CG  . LEU B 166 ? 0.2408 0.3286 0.2892 0.0542  0.0014  -0.1277 166 LEU B CG  
5508 C CD1 . LEU B 166 ? 0.2588 0.3564 0.3034 0.0502  0.0071  -0.1348 166 LEU B CD1 
5509 C CD2 . LEU B 166 ? 0.2862 0.3556 0.3239 0.0483  -0.0028 -0.1223 166 LEU B CD2 
5510 N N   . ASN B 167 ? 0.2089 0.2742 0.2955 0.0867  -0.0037 -0.1195 167 ASN B N   
5511 C CA  . ASN B 167 ? 0.2550 0.3036 0.3484 0.0951  -0.0042 -0.1162 167 ASN B CA  
5512 C C   . ASN B 167 ? 0.2363 0.2762 0.3319 0.0977  -0.0117 -0.1058 167 ASN B C   
5513 O O   . ASN B 167 ? 0.2380 0.2556 0.3306 0.0988  -0.0135 -0.1014 167 ASN B O   
5514 C CB  . ASN B 167 ? 0.2384 0.3008 0.3450 0.1043  0.0002  -0.1192 167 ASN B CB  
5515 C CG  . ASN B 167 ? 0.3875 0.4486 0.4911 0.1034  0.0082  -0.1293 167 ASN B CG  
5516 O OD1 . ASN B 167 ? 0.4673 0.5101 0.5607 0.0986  0.0100  -0.1327 167 ASN B OD1 
5517 N ND2 . ASN B 167 ? 0.4516 0.5327 0.5639 0.1078  0.0131  -0.1339 167 ASN B ND2 
5518 N N   . LYS B 168 ? 0.1880 0.2464 0.2884 0.0978  -0.0160 -0.1016 168 LYS B N   
5519 C CA  . LYS B 168 ? 0.1822 0.2343 0.2835 0.0990  -0.0237 -0.0916 168 LYS B CA  
5520 C C   . LYS B 168 ? 0.2562 0.2863 0.3428 0.0909  -0.0264 -0.0888 168 LYS B C   
5521 O O   . LYS B 168 ? 0.1834 0.1965 0.2682 0.0925  -0.0309 -0.0817 168 LYS B O   
5522 C CB  . LYS B 168 ? 0.2265 0.3023 0.3299 0.0940  -0.0269 -0.0853 168 LYS B CB  
5523 C CG  . LYS B 168 ? 0.2767 0.3773 0.3970 0.1026  -0.0259 -0.0860 168 LYS B CG  
5524 C CD  . LYS B 168 ? 0.3685 0.4590 0.4987 0.1140  -0.0279 -0.0812 168 LYS B CD  
5525 C CE  . LYS B 168 ? 0.5196 0.6327 0.6650 0.1214  -0.0252 -0.0810 168 LYS B CE  
5526 N NZ  . LYS B 168 ? 0.5879 0.7246 0.7406 0.1202  -0.0318 -0.0723 168 LYS B NZ  
5527 N N   . TYR B 169 ? 0.1730 0.2044 0.2485 0.0814  -0.0237 -0.0928 169 TYR B N   
5528 C CA  . TYR B 169 ? 0.1795 0.1927 0.2419 0.0735  -0.0258 -0.0896 169 TYR B CA  
5529 C C   . TYR B 169 ? 0.2200 0.2111 0.2801 0.0750  -0.0243 -0.0909 169 TYR B C   
5530 O O   . TYR B 169 ? 0.1882 0.1627 0.2424 0.0721  -0.0276 -0.0843 169 TYR B O   
5531 C CB  . TYR B 169 ? 0.1629 0.1840 0.2150 0.0638  -0.0228 -0.0928 169 TYR B CB  
5532 C CG  . TYR B 169 ? 0.1777 0.2128 0.2254 0.0565  -0.0248 -0.0857 169 TYR B CG  
5533 C CD1 . TYR B 169 ? 0.1957 0.2390 0.2492 0.0581  -0.0284 -0.0789 169 TYR B CD1 
5534 C CD2 . TYR B 169 ? 0.1932 0.2325 0.2307 0.0475  -0.0231 -0.0855 169 TYR B CD2 
5535 C CE1 . TYR B 169 ? 0.1404 0.1945 0.1889 0.0501  -0.0298 -0.0732 169 TYR B CE1 
5536 C CE2 . TYR B 169 ? 0.1549 0.2038 0.1878 0.0406  -0.0243 -0.0790 169 TYR B CE2 
5537 C CZ  . TYR B 169 ? 0.1358 0.1913 0.1740 0.0415  -0.0274 -0.0734 169 TYR B CZ  
5538 O OH  . TYR B 169 ? 0.1433 0.2066 0.1761 0.0335  -0.0282 -0.0678 169 TYR B OH  
5539 N N   . PHE B 170 ? 0.2790 0.2702 0.3420 0.0771  -0.0187 -0.0974 170 PHE B N   
5540 C CA  . PHE B 170 ? 0.2710 0.2413 0.3304 0.0765  -0.0164 -0.0970 170 PHE B CA  
5541 C C   . PHE B 170 ? 0.2675 0.2259 0.3335 0.0841  -0.0187 -0.0898 170 PHE B C   
5542 O O   . PHE B 170 ? 0.2981 0.2373 0.3591 0.0821  -0.0186 -0.0860 170 PHE B O   
5543 C CB  . PHE B 170 ? 0.2564 0.2285 0.3159 0.0767  -0.0094 -0.1066 170 PHE B CB  
5544 C CG  . PHE B 170 ? 0.3476 0.3224 0.3963 0.0667  -0.0074 -0.1114 170 PHE B CG  
5545 C CD1 . PHE B 170 ? 0.3266 0.2853 0.3661 0.0600  -0.0075 -0.1096 170 PHE B CD1 
5546 C CD2 . PHE B 170 ? 0.3932 0.3882 0.4408 0.0636  -0.0057 -0.1166 170 PHE B CD2 
5547 C CE1 . PHE B 170 ? 0.3526 0.3158 0.3829 0.0511  -0.0063 -0.1129 170 PHE B CE1 
5548 C CE2 . PHE B 170 ? 0.3880 0.3867 0.4256 0.0545  -0.0043 -0.1195 170 PHE B CE2 
5549 C CZ  . PHE B 170 ? 0.3579 0.3409 0.3872 0.0486  -0.0049 -0.1175 170 PHE B CZ  
5550 N N   . GLU B 171 ? 0.2368 0.2077 0.3140 0.0925  -0.0209 -0.0870 171 GLU B N   
5551 C CA  . GLU B 171 ? 0.2306 0.1922 0.3133 0.0991  -0.0245 -0.0777 171 GLU B CA  
5552 C C   . GLU B 171 ? 0.2612 0.2128 0.3356 0.0933  -0.0307 -0.0691 171 GLU B C   
5553 O O   . GLU B 171 ? 0.2601 0.1949 0.3320 0.0938  -0.0318 -0.0624 171 GLU B O   
5554 C CB  . GLU B 171 ? 0.2678 0.2493 0.3642 0.1082  -0.0267 -0.0750 171 GLU B CB  
5555 C CG  . GLU B 171 ? 0.4042 0.3959 0.5105 0.1154  -0.0201 -0.0820 171 GLU B CG  
5556 C CD  . GLU B 171 ? 0.5558 0.5709 0.6765 0.1235  -0.0225 -0.0779 171 GLU B CD  
5557 O OE1 . GLU B 171 ? 0.5706 0.5946 0.6926 0.1225  -0.0297 -0.0699 171 GLU B OE1 
5558 O OE2 . GLU B 171 ? 0.6143 0.6398 0.7447 0.1304  -0.0170 -0.0825 171 GLU B OE2 
5559 N N   . ILE B 172 ? 0.2312 0.1925 0.3006 0.0876  -0.0341 -0.0692 172 ILE B N   
5560 C CA  . ILE B 172 ? 0.1997 0.1515 0.2601 0.0817  -0.0394 -0.0617 172 ILE B CA  
5561 C C   . ILE B 172 ? 0.2488 0.1823 0.2987 0.0742  -0.0365 -0.0615 172 ILE B C   
5562 O O   . ILE B 172 ? 0.2047 0.1249 0.2497 0.0719  -0.0387 -0.0541 172 ILE B O   
5563 C CB  . ILE B 172 ? 0.1888 0.1543 0.2451 0.0766  -0.0420 -0.0622 172 ILE B CB  
5564 C CG1 . ILE B 172 ? 0.1992 0.1845 0.2627 0.0791  -0.0453 -0.0567 172 ILE B CG1 
5565 C CG2 . ILE B 172 ? 0.2752 0.2285 0.3185 0.0676  -0.0444 -0.0562 172 ILE B CG2 
5566 C CD1 . ILE B 172 ? 0.2170 0.1974 0.2808 0.0809  -0.0517 -0.0461 172 ILE B CD1 
5567 N N   . ILE B 173 ? 0.2076 0.1421 0.2539 0.0698  -0.0313 -0.0693 173 ILE B N   
5568 C CA  . ILE B 173 ? 0.2396 0.1602 0.2770 0.0624  -0.0286 -0.0691 173 ILE B CA  
5569 C C   . ILE B 173 ? 0.2794 0.1836 0.3187 0.0657  -0.0264 -0.0666 173 ILE B C   
5570 O O   . ILE B 173 ? 0.2778 0.1690 0.3111 0.0611  -0.0266 -0.0616 173 ILE B O   
5571 C CB  . ILE B 173 ? 0.2730 0.2002 0.3067 0.0574  -0.0241 -0.0777 173 ILE B CB  
5572 C CG1 . ILE B 173 ? 0.2001 0.1413 0.2299 0.0530  -0.0261 -0.0783 173 ILE B CG1 
5573 C CG2 . ILE B 173 ? 0.2728 0.1865 0.2990 0.0508  -0.0211 -0.0780 173 ILE B CG2 
5574 C CD1 . ILE B 173 ? 0.2667 0.2187 0.2936 0.0489  -0.0222 -0.0862 173 ILE B CD1 
5575 N N   . LYS B 174 ? 0.2341 0.1388 0.2820 0.0740  -0.0237 -0.0699 174 LYS B N   
5576 C CA  . LYS B 174 ? 0.2539 0.1412 0.3036 0.0783  -0.0209 -0.0674 174 LYS B CA  
5577 C C   . LYS B 174 ? 0.3313 0.2106 0.3815 0.0805  -0.0256 -0.0561 174 LYS B C   
5578 O O   . LYS B 174 ? 0.3061 0.1685 0.3544 0.0810  -0.0235 -0.0525 174 LYS B O   
5579 C CB  . LYS B 174 ? 0.2790 0.1699 0.3387 0.0883  -0.0169 -0.0725 174 LYS B CB  
5580 C CG  . LYS B 174 ? 0.3058 0.2009 0.3636 0.0861  -0.0109 -0.0842 174 LYS B CG  
5581 C CD  . LYS B 174 ? 0.3875 0.2884 0.4560 0.0968  -0.0067 -0.0888 174 LYS B CD  
5582 C CE  . LYS B 174 ? 0.5979 0.5064 0.6641 0.0943  -0.0010 -0.1009 174 LYS B CE  
5583 N NZ  . LYS B 174 ? 0.6876 0.5770 0.7441 0.0894  0.0041  -0.1064 174 LYS B NZ  
5584 N N   . LYS B 175 ? 0.2433 0.1341 0.2953 0.0814  -0.0318 -0.0505 175 LYS B N   
5585 C CA  . LYS B 175 ? 0.2457 0.1312 0.2970 0.0828  -0.0370 -0.0394 175 LYS B CA  
5586 C C   . LYS B 175 ? 0.2361 0.1171 0.2761 0.0729  -0.0397 -0.0353 175 LYS B C   
5587 O O   . LYS B 175 ? 0.2781 0.1554 0.3155 0.0725  -0.0440 -0.0264 175 LYS B O   
5588 C CB  . LYS B 175 ? 0.2837 0.1855 0.3435 0.0899  -0.0426 -0.0352 175 LYS B CB  
5589 C CG  . LYS B 175 ? 0.4797 0.3896 0.5528 0.1009  -0.0400 -0.0377 175 LYS B CG  
5590 C CD  . LYS B 175 ? 0.5363 0.4651 0.6183 0.1071  -0.0462 -0.0317 175 LYS B CD  
5591 C CE  . LYS B 175 ? 0.5754 0.5226 0.6565 0.1029  -0.0489 -0.0366 175 LYS B CE  
5592 N NZ  . LYS B 175 ? 0.6705 0.6396 0.7611 0.1081  -0.0547 -0.0311 175 LYS B NZ  
5593 N N   . THR B 176 ? 0.2423 0.1248 0.2758 0.0651  -0.0370 -0.0412 176 THR B N   
5594 C CA  . THR B 176 ? 0.2158 0.0983 0.2400 0.0568  -0.0393 -0.0375 176 THR B CA  
5595 C C   . THR B 176 ? 0.2484 0.1167 0.2668 0.0522  -0.0381 -0.0317 176 THR B C   
5596 O O   . THR B 176 ? 0.3044 0.1708 0.3177 0.0494  -0.0416 -0.0247 176 THR B O   
5597 C CB  . THR B 176 ? 0.2693 0.1595 0.2893 0.0507  -0.0366 -0.0443 176 THR B CB  
5598 O OG1 . THR B 176 ? 0.2492 0.1536 0.2734 0.0542  -0.0385 -0.0483 176 THR B OG1 
5599 C CG2 . THR B 176 ? 0.2969 0.1859 0.3079 0.0427  -0.0375 -0.0401 176 THR B CG2 
5600 N N   . LEU B 177 ? 0.2362 0.0938 0.2546 0.0511  -0.0330 -0.0350 177 LEU B N   
5601 C CA  . LEU B 177 ? 0.2451 0.0897 0.2585 0.0467  -0.0319 -0.0295 177 LEU B CA  
5602 C C   . LEU B 177 ? 0.2708 0.1084 0.2870 0.0525  -0.0352 -0.0206 177 LEU B C   
5603 O O   . LEU B 177 ? 0.2738 0.1055 0.2848 0.0487  -0.0368 -0.0136 177 LEU B O   
5604 C CB  . LEU B 177 ? 0.2886 0.1218 0.3009 0.0437  -0.0257 -0.0352 177 LEU B CB  
5605 C CG  . LEU B 177 ? 0.3739 0.2140 0.3818 0.0363  -0.0232 -0.0423 177 LEU B CG  
5606 C CD1 . LEU B 177 ? 0.3441 0.1719 0.3496 0.0329  -0.0176 -0.0483 177 LEU B CD1 
5607 C CD2 . LEU B 177 ? 0.3421 0.1873 0.3443 0.0293  -0.0252 -0.0376 177 LEU B CD2 
5608 N N   . SER B 178 ? 0.2636 0.1032 0.2879 0.0618  -0.0362 -0.0205 178 SER B N   
5609 C CA  . SER B 178 ? 0.2759 0.1103 0.3037 0.0683  -0.0395 -0.0110 178 SER B CA  
5610 C C   . SER B 178 ? 0.2705 0.1138 0.2946 0.0668  -0.0465 -0.0033 178 SER B C   
5611 O O   . SER B 178 ? 0.2898 0.1272 0.3116 0.0675  -0.0493 0.0061  178 SER B O   
5612 C CB  . SER B 178 ? 0.3486 0.1862 0.3875 0.0796  -0.0387 -0.0124 178 SER B CB  
5613 O OG  . SER B 178 ? 0.4338 0.2573 0.4745 0.0819  -0.0318 -0.0171 178 SER B OG  
5614 N N   . ILE B 179 ? 0.2738 0.1307 0.2966 0.0645  -0.0494 -0.0068 179 ILE B N   
5615 C CA  . ILE B 179 ? 0.2688 0.1321 0.2866 0.0624  -0.0559 0.0002  179 ILE B CA  
5616 C C   . ILE B 179 ? 0.2416 0.0967 0.2480 0.0532  -0.0553 0.0038  179 ILE B C   
5617 O O   . ILE B 179 ? 0.3226 0.1767 0.3235 0.0516  -0.0596 0.0120  179 ILE B O   
5618 C CB  . ILE B 179 ? 0.2810 0.1592 0.3000 0.0626  -0.0590 -0.0044 179 ILE B CB  
5619 C CG1 . ILE B 179 ? 0.3337 0.2189 0.3488 0.0620  -0.0665 0.0035  179 ILE B CG1 
5620 C CG2 . ILE B 179 ? 0.2401 0.1192 0.2523 0.0548  -0.0555 -0.0116 179 ILE B CG2 
5621 C CD1 . ILE B 179 ? 0.4341 0.3253 0.4573 0.0702  -0.0708 0.0113  179 ILE B CD1 
5622 N N   . TYR B 180 ? 0.2564 0.1070 0.2592 0.0470  -0.0499 -0.0018 180 TYR B N   
5623 C CA  . TYR B 180 ? 0.2380 0.0823 0.2319 0.0391  -0.0486 0.0017  180 TYR B CA  
5624 C C   . TYR B 180 ? 0.2880 0.1199 0.2817 0.0403  -0.0482 0.0089  180 TYR B C   
5625 O O   . TYR B 180 ? 0.3036 0.1324 0.2903 0.0365  -0.0505 0.0159  180 TYR B O   
5626 C CB  . TYR B 180 ? 0.2574 0.1023 0.2493 0.0329  -0.0430 -0.0052 180 TYR B CB  
5627 C CG  . TYR B 180 ? 0.2333 0.0899 0.2229 0.0304  -0.0434 -0.0097 180 TYR B CG  
5628 C CD1 . TYR B 180 ? 0.2723 0.1321 0.2541 0.0255  -0.0449 -0.0066 180 TYR B CD1 
5629 C CD2 . TYR B 180 ? 0.2135 0.0775 0.2083 0.0330  -0.0420 -0.0169 180 TYR B CD2 
5630 C CE1 . TYR B 180 ? 0.2185 0.0874 0.1980 0.0235  -0.0447 -0.0101 180 TYR B CE1 
5631 C CE2 . TYR B 180 ? 0.2011 0.0754 0.1935 0.0307  -0.0423 -0.0202 180 TYR B CE2 
5632 C CZ  . TYR B 180 ? 0.2294 0.1054 0.2144 0.0262  -0.0435 -0.0165 180 TYR B CZ  
5633 O OH  . TYR B 180 ? 0.2067 0.0910 0.1892 0.0242  -0.0432 -0.0192 180 TYR B OH  
5634 N N   . ARG B 181 ? 0.3045 0.1284 0.3051 0.0455  -0.0452 0.0074  181 ARG B N   
5635 C CA  . ARG B 181 ? 0.2979 0.1089 0.2985 0.0477  -0.0449 0.0153  181 ARG B CA  
5636 C C   . ARG B 181 ? 0.3322 0.1474 0.3328 0.0528  -0.0514 0.0253  181 ARG B C   
5637 O O   . ARG B 181 ? 0.3563 0.1654 0.3513 0.0506  -0.0533 0.0340  181 ARG B O   
5638 C CB  . ARG B 181 ? 0.3030 0.1031 0.3110 0.0535  -0.0400 0.0119  181 ARG B CB  
5639 C CG  . ARG B 181 ? 0.3097 0.1036 0.3165 0.0476  -0.0334 0.0028  181 ARG B CG  
5640 C CD  . ARG B 181 ? 0.3311 0.1087 0.3425 0.0526  -0.0281 0.0009  181 ARG B CD  
5641 N NE  . ARG B 181 ? 0.4701 0.2441 0.4803 0.0473  -0.0223 -0.0096 181 ARG B NE  
5642 C CZ  . ARG B 181 ? 0.5154 0.2960 0.5287 0.0499  -0.0203 -0.0186 181 ARG B CZ  
5643 N NH1 . ARG B 181 ? 0.4932 0.2847 0.5124 0.0580  -0.0235 -0.0184 181 ARG B NH1 
5644 N NH2 . ARG B 181 ? 0.6622 0.4392 0.6725 0.0442  -0.0153 -0.0277 181 ARG B NH2 
5645 N N   . GLU B 182 ? 0.3023 0.1292 0.3090 0.0593  -0.0551 0.0243  182 GLU B N   
5646 C CA  . GLU B 182 ? 0.3582 0.1922 0.3662 0.0645  -0.0617 0.0340  182 GLU B CA  
5647 C C   . GLU B 182 ? 0.3452 0.1835 0.3417 0.0568  -0.0664 0.0396  182 GLU B C   
5648 O O   . GLU B 182 ? 0.3494 0.1858 0.3416 0.0569  -0.0698 0.0497  182 GLU B O   
5649 C CB  . GLU B 182 ? 0.3515 0.2003 0.3691 0.0721  -0.0646 0.0309  182 GLU B CB  
5650 C CG  . GLU B 182 ? 0.4240 0.2852 0.4433 0.0765  -0.0720 0.0409  182 GLU B CG  
5651 C CD  . GLU B 182 ? 0.5049 0.3833 0.5360 0.0846  -0.0746 0.0384  182 GLU B CD  
5652 O OE1 . GLU B 182 ? 0.4875 0.3675 0.5255 0.0873  -0.0703 0.0286  182 GLU B OE1 
5653 O OE2 . GLU B 182 ? 0.5681 0.4604 0.6017 0.0881  -0.0809 0.0465  182 GLU B OE2 
5654 N N   . ILE B 183 ? 0.2695 0.1136 0.2601 0.0501  -0.0664 0.0333  183 ILE B N   
5655 C CA  . ILE B 183 ? 0.2806 0.1278 0.2593 0.0430  -0.0704 0.0383  183 ILE B CA  
5656 C C   . ILE B 183 ? 0.3596 0.1956 0.3299 0.0366  -0.0675 0.0425  183 ILE B C   
5657 O O   . ILE B 183 ? 0.3634 0.1998 0.3244 0.0324  -0.0708 0.0499  183 ILE B O   
5658 C CB  . ILE B 183 ? 0.3199 0.1746 0.2938 0.0381  -0.0707 0.0313  183 ILE B CB  
5659 C CG1 . ILE B 183 ? 0.2862 0.1359 0.2585 0.0331  -0.0638 0.0228  183 ILE B CG1 
5660 C CG2 . ILE B 183 ? 0.3967 0.2635 0.3793 0.0445  -0.0741 0.0280  183 ILE B CG2 
5661 C CD1 . ILE B 183 ? 0.3461 0.1916 0.3068 0.0244  -0.0619 0.0245  183 ILE B CD1 
5662 N N   . LYS B 184 ? 0.2900 0.1165 0.2633 0.0354  -0.0613 0.0382  184 LYS B N   
5663 C CA  . LYS B 184 ? 0.2875 0.1041 0.2542 0.0296  -0.0587 0.0425  184 LYS B CA  
5664 C C   . LYS B 184 ? 0.3624 0.1720 0.3298 0.0339  -0.0610 0.0531  184 LYS B C   
5665 O O   . LYS B 184 ? 0.3808 0.1878 0.3394 0.0294  -0.0628 0.0609  184 LYS B O   
5666 C CB  . LYS B 184 ? 0.3245 0.1342 0.2946 0.0267  -0.0518 0.0352  184 LYS B CB  
5667 C CG  . LYS B 184 ? 0.5173 0.3166 0.4821 0.0206  -0.0489 0.0394  184 LYS B CG  
5668 C CD  . LYS B 184 ? 0.5788 0.3729 0.5475 0.0171  -0.0426 0.0319  184 LYS B CD  
5669 C CE  . LYS B 184 ? 0.6369 0.4207 0.6010 0.0108  -0.0401 0.0367  184 LYS B CE  
5670 N NZ  . LYS B 184 ? 0.7499 0.5294 0.7176 0.0062  -0.0345 0.0295  184 LYS B NZ  
5671 N N   . GLU B 185 ? 0.3520 0.1590 0.3296 0.0430  -0.0609 0.0539  185 GLU B N   
5672 C CA  . GLU B 185 ? 0.3810 0.1809 0.3600 0.0486  -0.0626 0.0648  185 GLU B CA  
5673 C C   . GLU B 185 ? 0.4389 0.2504 0.4137 0.0504  -0.0701 0.0743  185 GLU B C   
5674 O O   . GLU B 185 ? 0.4724 0.2800 0.4427 0.0511  -0.0722 0.0850  185 GLU B O   
5675 C CB  . GLU B 185 ? 0.4553 0.2489 0.4463 0.0588  -0.0595 0.0629  185 GLU B CB  
5676 C CG  . GLU B 185 ? 0.4897 0.2704 0.4830 0.0557  -0.0519 0.0542  185 GLU B CG  
5677 C CD  . GLU B 185 ? 0.6730 0.4405 0.6587 0.0483  -0.0491 0.0586  185 GLU B CD  
5678 O OE1 . GLU B 185 ? 0.7664 0.5268 0.7495 0.0507  -0.0508 0.0696  185 GLU B OE1 
5679 O OE2 . GLU B 185 ? 0.7237 0.4896 0.7062 0.0399  -0.0453 0.0517  185 GLU B OE2 
5680 N N   . GLU B 186 ? 0.4160 0.2424 0.3916 0.0507  -0.0742 0.0707  186 GLU B N   
5681 C CA  . GLU B 186 ? 0.3949 0.2347 0.3656 0.0506  -0.0814 0.0789  186 GLU B CA  
5682 C C   . GLU B 186 ? 0.4177 0.2580 0.3728 0.0394  -0.0828 0.0814  186 GLU B C   
5683 O O   . GLU B 186 ? 0.4013 0.2530 0.3497 0.0371  -0.0884 0.0877  186 GLU B O   
5684 C CB  . GLU B 186 ? 0.3866 0.2425 0.3638 0.0542  -0.0851 0.0740  186 GLU B CB  
5685 C CG  . GLU B 186 ? 0.4350 0.2957 0.4274 0.0667  -0.0855 0.0750  186 GLU B CG  
5686 C CD  . GLU B 186 ? 0.6706 0.5490 0.6705 0.0699  -0.0887 0.0696  186 GLU B CD  
5687 O OE1 . GLU B 186 ? 0.7152 0.5974 0.7097 0.0629  -0.0888 0.0622  186 GLU B OE1 
5688 O OE2 . GLU B 186 ? 0.7812 0.6705 0.7925 0.0797  -0.0911 0.0734  186 GLU B OE2 
5689 N N   . GLY B 187 ? 0.4573 0.2870 0.4067 0.0322  -0.0774 0.0765  187 GLY B N   
5690 C CA  . GLY B 187 ? 0.4117 0.2418 0.3466 0.0218  -0.0773 0.0776  187 GLY B CA  
5691 C C   . GLY B 187 ? 0.3901 0.2306 0.3185 0.0169  -0.0795 0.0722  187 GLY B C   
5692 O O   . GLY B 187 ? 0.3780 0.2214 0.2933 0.0091  -0.0806 0.0746  187 GLY B O   
5693 N N   . LYS B 188 ? 0.3224 0.1684 0.2591 0.0212  -0.0799 0.0649  188 LYS B N   
5694 C CA  . LYS B 188 ? 0.3154 0.1699 0.2460 0.0170  -0.0818 0.0598  188 LYS B CA  
5695 C C   . LYS B 188 ? 0.3049 0.1529 0.2304 0.0112  -0.0758 0.0510  188 LYS B C   
5696 O O   . LYS B 188 ? 0.2673 0.1189 0.1847 0.0065  -0.0762 0.0474  188 LYS B O   
5697 C CB  . LYS B 188 ? 0.3414 0.2063 0.2834 0.0245  -0.0853 0.0568  188 LYS B CB  
5698 C CG  . LYS B 188 ? 0.3849 0.2620 0.3323 0.0303  -0.0918 0.0656  188 LYS B CG  
5699 C CD  . LYS B 188 ? 0.4228 0.3111 0.3846 0.0388  -0.0939 0.0618  188 LYS B CD  
5700 C CE  . LYS B 188 ? 0.4931 0.3986 0.4606 0.0440  -0.1005 0.0704  188 LYS B CE  
5701 N NZ  . LYS B 188 ? 0.4993 0.4207 0.4569 0.0359  -0.1056 0.0715  188 LYS B NZ  
5702 N N   . GLY B 189 ? 0.2982 0.1375 0.2282 0.0113  -0.0700 0.0479  189 GLY B N   
5703 C CA  . GLY B 189 ? 0.3130 0.1497 0.2399 0.0063  -0.0640 0.0403  189 GLY B CA  
5704 C C   . GLY B 189 ? 0.2929 0.1227 0.2259 0.0063  -0.0587 0.0387  189 GLY B C   
5705 O O   . GLY B 189 ? 0.3818 0.2074 0.3228 0.0112  -0.0590 0.0412  189 GLY B O   
5706 N N   . SER B 190 ? 0.3007 0.1295 0.2295 0.0006  -0.0535 0.0349  190 SER B N   
5707 C CA  . SER B 190 ? 0.2919 0.1163 0.2266 -0.0006 -0.0485 0.0324  190 SER B CA  
5708 C C   . SER B 190 ? 0.3290 0.1591 0.2725 0.0018  -0.0452 0.0234  190 SER B C   
5709 O O   . SER B 190 ? 0.2908 0.1283 0.2332 0.0020  -0.0453 0.0191  190 SER B O   
5710 C CB  . SER B 190 ? 0.3065 0.1285 0.2330 -0.0080 -0.0448 0.0340  190 SER B CB  
5711 O OG  . SER B 190 ? 0.3779 0.1954 0.2950 -0.0111 -0.0474 0.0424  190 SER B OG  
5712 N N   . VAL B 191 ? 0.2869 0.1133 0.2383 0.0029  -0.0422 0.0207  191 VAL B N   
5713 C CA  . VAL B 191 ? 0.2672 0.0990 0.2255 0.0035  -0.0387 0.0125  191 VAL B CA  
5714 C C   . VAL B 191 ? 0.2850 0.1143 0.2432 -0.0024 -0.0343 0.0109  191 VAL B C   
5715 O O   . VAL B 191 ? 0.3157 0.1356 0.2740 -0.0046 -0.0333 0.0143  191 VAL B O   
5716 C CB  . VAL B 191 ? 0.3489 0.1785 0.3160 0.0094  -0.0388 0.0094  191 VAL B CB  
5717 C CG1 . VAL B 191 ? 0.3230 0.1591 0.2954 0.0090  -0.0353 0.0008  191 VAL B CG1 
5718 C CG2 . VAL B 191 ? 0.3462 0.1786 0.3144 0.0156  -0.0439 0.0118  191 VAL B CG2 
5719 N N   . SER B 192 ? 0.2231 0.0605 0.1815 -0.0049 -0.0318 0.0062  192 SER B N   
5720 C CA  . SER B 192 ? 0.2576 0.0944 0.2165 -0.0105 -0.0283 0.0044  192 SER B CA  
5721 C C   . SER B 192 ? 0.2395 0.0812 0.2054 -0.0101 -0.0263 -0.0030 192 SER B C   
5722 O O   . SER B 192 ? 0.2111 0.0574 0.1806 -0.0056 -0.0271 -0.0067 192 SER B O   
5723 C CB  . SER B 192 ? 0.2405 0.0823 0.1930 -0.0141 -0.0270 0.0058  192 SER B CB  
5724 O OG  . SER B 192 ? 0.2406 0.0920 0.1943 -0.0113 -0.0267 0.0018  192 SER B OG  
5725 N N   . THR B 193 ? 0.2250 0.0659 0.1923 -0.0156 -0.0240 -0.0053 193 THR B N   
5726 C CA  . THR B 193 ? 0.2461 0.0930 0.2181 -0.0166 -0.0227 -0.0124 193 THR B CA  
5727 C C   . THR B 193 ? 0.2759 0.1280 0.2460 -0.0220 -0.0218 -0.0129 193 THR B C   
5728 O O   . THR B 193 ? 0.2550 0.1054 0.2202 -0.0248 -0.0213 -0.0081 193 THR B O   
5729 C CB  . THR B 193 ? 0.3037 0.1430 0.2804 -0.0183 -0.0213 -0.0166 193 THR B CB  
5730 O OG1 . THR B 193 ? 0.2929 0.1390 0.2728 -0.0185 -0.0205 -0.0242 193 THR B OG1 
5731 C CG2 . THR B 193 ? 0.2438 0.0758 0.2201 -0.0259 -0.0199 -0.0154 193 THR B CG2 
5732 N N   . SER B 194 ? 0.2616 0.1200 0.2350 -0.0238 -0.0216 -0.0189 194 SER B N   
5733 C CA  . SER B 194 ? 0.2570 0.1207 0.2294 -0.0293 -0.0216 -0.0202 194 SER B CA  
5734 C C   . SER B 194 ? 0.2140 0.0775 0.1902 -0.0362 -0.0215 -0.0256 194 SER B C   
5735 O O   . SER B 194 ? 0.2188 0.0792 0.1985 -0.0350 -0.0209 -0.0302 194 SER B O   
5736 C CB  . SER B 194 ? 0.1889 0.0621 0.1611 -0.0257 -0.0228 -0.0224 194 SER B CB  
5737 O OG  . SER B 194 ? 0.1945 0.0681 0.1628 -0.0207 -0.0223 -0.0178 194 SER B OG  
5738 N N   . PRO B 195 ? 0.2234 0.0908 0.1988 -0.0443 -0.0217 -0.0257 195 PRO B N   
5739 C CA  . PRO B 195 ? 0.2207 0.0929 0.1998 -0.0522 -0.0223 -0.0321 195 PRO B CA  
5740 C C   . PRO B 195 ? 0.2619 0.1404 0.2437 -0.0483 -0.0237 -0.0394 195 PRO B C   
5741 O O   . PRO B 195 ? 0.2508 0.1355 0.2312 -0.0426 -0.0252 -0.0393 195 PRO B O   
5742 C CB  . PRO B 195 ? 0.3055 0.1922 0.2849 -0.0589 -0.0217 -0.0298 195 PRO B CB  
5743 C CG  . PRO B 195 ? 0.3743 0.2575 0.3503 -0.0564 -0.0192 -0.0217 195 PRO B CG  
5744 C CD  . PRO B 195 ? 0.2454 0.1150 0.2164 -0.0476 -0.0208 -0.0202 195 PRO B CD  
5745 N N   . TYR B 196 ? 0.2201 0.0977 0.2057 -0.0523 -0.0232 -0.0461 196 TYR B N   
5746 C CA  . TYR B 196 ? 0.2325 0.1092 0.2203 -0.0475 -0.0220 -0.0528 196 TYR B CA  
5747 C C   . TYR B 196 ? 0.2822 0.1713 0.2676 -0.0440 -0.0238 -0.0555 196 TYR B C   
5748 O O   . TYR B 196 ? 0.2046 0.0918 0.1880 -0.0363 -0.0228 -0.0545 196 TYR B O   
5749 C CB  . TYR B 196 ? 0.2341 0.1085 0.2273 -0.0535 -0.0225 -0.0605 196 TYR B CB  
5750 C CG  . TYR B 196 ? 0.2409 0.1098 0.2353 -0.0487 -0.0189 -0.0659 196 TYR B CG  
5751 C CD1 . TYR B 196 ? 0.2553 0.1290 0.2391 -0.0471 -0.0162 -0.0691 196 TYR B CD1 
5752 C CD2 . TYR B 196 ? 0.2668 0.1199 0.2632 -0.0477 -0.0157 -0.0651 196 TYR B CD2 
5753 C CE1 . TYR B 196 ? 0.2543 0.1124 0.2258 -0.0441 -0.0147 -0.0705 196 TYR B CE1 
5754 C CE2 . TYR B 196 ? 0.2898 0.1333 0.2816 -0.0445 -0.0104 -0.0685 196 TYR B CE2 
5755 C CZ  . TYR B 196 ? 0.3291 0.1727 0.3048 -0.0431 -0.0100 -0.0708 196 TYR B CZ  
5756 O OH  . TYR B 196 ? 0.3084 0.1371 0.2755 -0.0384 -0.0093 -0.0729 196 TYR B OH  
5757 N N   . TYR B 197 ? 0.2152 0.1182 0.2006 -0.0496 -0.0273 -0.0579 197 TYR B N   
5758 C CA  . TYR B 197 ? 0.1955 0.1115 0.1792 -0.0466 -0.0300 -0.0602 197 TYR B CA  
5759 C C   . TYR B 197 ? 0.2074 0.1363 0.1926 -0.0409 -0.0294 -0.0512 197 TYR B C   
5760 O O   . TYR B 197 ? 0.2107 0.1578 0.1977 -0.0387 -0.0300 -0.0503 197 TYR B O   
5761 C CB  . TYR B 197 ? 0.2004 0.1329 0.1854 -0.0542 -0.0311 -0.0667 197 TYR B CB  
5762 C CG  . TYR B 197 ? 0.2279 0.1483 0.2098 -0.0540 -0.0317 -0.0715 197 TYR B CG  
5763 C CD1 . TYR B 197 ? 0.2889 0.2032 0.2648 -0.0480 -0.0307 -0.0737 197 TYR B CD1 
5764 C CD2 . TYR B 197 ? 0.2627 0.1770 0.2464 -0.0608 -0.0318 -0.0739 197 TYR B CD2 
5765 C CE1 . TYR B 197 ? 0.2361 0.1381 0.2078 -0.0481 -0.0301 -0.0784 197 TYR B CE1 
5766 C CE2 . TYR B 197 ? 0.2941 0.1953 0.2746 -0.0605 -0.0321 -0.0789 197 TYR B CE2 
5767 C CZ  . TYR B 197 ? 0.3217 0.2160 0.2955 -0.0539 -0.0316 -0.0811 197 TYR B CZ  
5768 O OH  . TYR B 197 ? 0.3480 0.2288 0.3177 -0.0538 -0.0310 -0.0866 197 TYR B OH  
5769 N N   . HIS B 198 ? 0.2193 0.1383 0.2033 -0.0381 -0.0280 -0.0444 198 HIS B N   
5770 C CA  . HIS B 198 ? 0.1693 0.0965 0.1538 -0.0323 -0.0264 -0.0368 198 HIS B CA  
5771 C C   . HIS B 198 ? 0.2107 0.1599 0.2001 -0.0347 -0.0255 -0.0338 198 HIS B C   
5772 O O   . HIS B 198 ? 0.2131 0.1748 0.2042 -0.0292 -0.0253 -0.0307 198 HIS B O   
5773 C CB  . HIS B 198 ? 0.1662 0.0930 0.1488 -0.0241 -0.0272 -0.0370 198 HIS B CB  
5774 C CG  . HIS B 198 ? 0.1550 0.0814 0.1358 -0.0180 -0.0253 -0.0302 198 HIS B CG  
5775 N ND1 . HIS B 198 ? 0.1612 0.1020 0.1441 -0.0146 -0.0239 -0.0263 198 HIS B ND1 
5776 C CD2 . HIS B 198 ? 0.1827 0.0956 0.1592 -0.0146 -0.0245 -0.0270 198 HIS B CD2 
5777 C CE1 . HIS B 198 ? 0.1872 0.1215 0.1670 -0.0097 -0.0218 -0.0217 198 HIS B CE1 
5778 N NE2 . HIS B 198 ? 0.1764 0.0948 0.1520 -0.0101 -0.0223 -0.0224 198 HIS B NE2 
5779 N N   . PRO B 199 ? 0.1931 0.1484 0.1855 -0.0429 -0.0250 -0.0340 199 PRO B N   
5780 C CA  . PRO B 199 ? 0.1915 0.1706 0.1902 -0.0446 -0.0242 -0.0302 199 PRO B CA  
5781 C C   . PRO B 199 ? 0.2355 0.2168 0.2361 -0.0403 -0.0203 -0.0223 199 PRO B C   
5782 O O   . PRO B 199 ? 0.2246 0.1889 0.2204 -0.0382 -0.0183 -0.0203 199 PRO B O   
5783 C CB  . PRO B 199 ? 0.1932 0.1766 0.1941 -0.0564 -0.0251 -0.0345 199 PRO B CB  
5784 C CG  . PRO B 199 ? 0.2296 0.1877 0.2254 -0.0592 -0.0238 -0.0352 199 PRO B CG  
5785 C CD  . PRO B 199 ? 0.2559 0.1965 0.2464 -0.0508 -0.0247 -0.0366 199 PRO B CD  
5786 N N   . LEU B 200 ? 0.2227 0.2263 0.2304 -0.0394 -0.0191 -0.0179 200 LEU B N   
5787 C CA  . LEU B 200 ? 0.2123 0.2213 0.2235 -0.0361 -0.0144 -0.0112 200 LEU B CA  
5788 C C   . LEU B 200 ? 0.1925 0.2067 0.2069 -0.0460 -0.0131 -0.0113 200 LEU B C   
5789 O O   . LEU B 200 ? 0.2280 0.2646 0.2504 -0.0505 -0.0136 -0.0103 200 LEU B O   
5790 C CB  . LEU B 200 ? 0.2434 0.2735 0.2618 -0.0286 -0.0134 -0.0058 200 LEU B CB  
5791 C CG  . LEU B 200 ? 0.2374 0.2608 0.2521 -0.0188 -0.0135 -0.0042 200 LEU B CG  
5792 C CD1 . LEU B 200 ? 0.2245 0.2703 0.2468 -0.0131 -0.0139 0.0011  200 LEU B CD1 
5793 C CD2 . LEU B 200 ? 0.2274 0.2324 0.2364 -0.0127 -0.0090 -0.0019 200 LEU B CD2 
5794 N N   . ILE B 201 ? 0.2234 0.2177 0.2316 -0.0498 -0.0116 -0.0120 201 ILE B N   
5795 C CA  . ILE B 201 ? 0.2254 0.2211 0.2351 -0.0606 -0.0103 -0.0121 201 ILE B CA  
5796 C C   . ILE B 201 ? 0.1944 0.2136 0.2129 -0.0612 -0.0063 -0.0068 201 ILE B C   
5797 O O   . ILE B 201 ? 0.1771 0.2119 0.2017 -0.0706 -0.0069 -0.0077 201 ILE B O   
5798 C CB  . ILE B 201 ? 0.2062 0.1759 0.2070 -0.0630 -0.0090 -0.0117 201 ILE B CB  
5799 C CG1 . ILE B 201 ? 0.2217 0.1706 0.2162 -0.0631 -0.0132 -0.0171 201 ILE B CG1 
5800 C CG2 . ILE B 201 ? 0.1974 0.1682 0.1992 -0.0744 -0.0069 -0.0103 201 ILE B CG2 
5801 C CD1 . ILE B 201 ? 0.2275 0.1764 0.2236 -0.0732 -0.0161 -0.0234 201 ILE B CD1 
5802 N N   . PRO B 202 ? 0.1777 0.2007 0.1976 -0.0519 -0.0017 -0.0017 202 PRO B N   
5803 C CA  . PRO B 202 ? 0.1653 0.2118 0.1950 -0.0517 0.0029  0.0031  202 PRO B CA  
5804 C C   . PRO B 202 ? 0.1715 0.2470 0.2129 -0.0527 0.0001  0.0039  202 PRO B C   
5805 O O   . PRO B 202 ? 0.1649 0.2617 0.2152 -0.0580 0.0020  0.0063  202 PRO B O   
5806 C CB  . PRO B 202 ? 0.1809 0.2231 0.2091 -0.0394 0.0081  0.0070  202 PRO B CB  
5807 C CG  . PRO B 202 ? 0.2144 0.2273 0.2295 -0.0380 0.0072  0.0046  202 PRO B CG  
5808 C CD  . PRO B 202 ? 0.1646 0.1701 0.1770 -0.0421 0.0002  -0.0004 202 PRO B CD  
5809 N N   . ILE B 203 ? 0.1779 0.2565 0.2193 -0.0480 -0.0045 0.0023  203 ILE B N   
5810 C CA  . ILE B 203 ? 0.1501 0.2579 0.2017 -0.0493 -0.0078 0.0038  203 ILE B CA  
5811 C C   . ILE B 203 ? 0.1866 0.3011 0.2385 -0.0642 -0.0121 -0.0019 203 ILE B C   
5812 O O   . ILE B 203 ? 0.1887 0.3299 0.2502 -0.0705 -0.0129 -0.0001 203 ILE B O   
5813 C CB  . ILE B 203 ? 0.2157 0.3253 0.2662 -0.0399 -0.0110 0.0047  203 ILE B CB  
5814 C CG1 . ILE B 203 ? 0.1996 0.3055 0.2515 -0.0258 -0.0061 0.0110  203 ILE B CG1 
5815 C CG2 . ILE B 203 ? 0.2031 0.3434 0.2624 -0.0429 -0.0158 0.0062  203 ILE B CG2 
5816 C CD1 . ILE B 203 ? 0.1827 0.2905 0.2339 -0.0170 -0.0088 0.0132  203 ILE B CD1 
5817 N N   . LEU B 204 ? 0.2004 0.2909 0.2422 -0.0703 -0.0147 -0.0089 204 LEU B N   
5818 C CA  . LEU B 204 ? 0.1733 0.2645 0.2139 -0.0852 -0.0177 -0.0153 204 LEU B CA  
5819 C C   . LEU B 204 ? 0.1802 0.2789 0.2253 -0.0950 -0.0144 -0.0130 204 LEU B C   
5820 O O   . LEU B 204 ? 0.1882 0.3044 0.2383 -0.1071 -0.0163 -0.0155 204 LEU B O   
5821 C CB  . LEU B 204 ? 0.1901 0.2496 0.2192 -0.0881 -0.0194 -0.0224 204 LEU B CB  
5822 C CG  . LEU B 204 ? 0.2638 0.3155 0.2879 -0.0805 -0.0226 -0.0260 204 LEU B CG  
5823 C CD1 . LEU B 204 ? 0.2356 0.2579 0.2503 -0.0844 -0.0238 -0.0334 204 LEU B CD1 
5824 C CD2 . LEU B 204 ? 0.2735 0.3514 0.3024 -0.0832 -0.0268 -0.0281 204 LEU B CD2 
5825 N N   . LEU B 205 ? 0.1893 0.2751 0.2321 -0.0911 -0.0092 -0.0087 205 LEU B N   
5826 C CA  . LEU B 205 ? 0.2093 0.3015 0.2555 -0.1008 -0.0053 -0.0063 205 LEU B CA  
5827 C C   . LEU B 205 ? 0.1819 0.3104 0.2422 -0.0994 -0.0030 -0.0007 205 LEU B C   
5828 O O   . LEU B 205 ? 0.1878 0.3337 0.2545 -0.1112 -0.0023 -0.0005 205 LEU B O   
5829 C CB  . LEU B 205 ? 0.2084 0.2768 0.2466 -0.0973 -0.0003 -0.0032 205 LEU B CB  
5830 C CG  . LEU B 205 ? 0.2600 0.2937 0.2853 -0.1012 -0.0022 -0.0071 205 LEU B CG  
5831 C CD1 . LEU B 205 ? 0.2061 0.2210 0.2238 -0.0961 0.0021  -0.0027 205 LEU B CD1 
5832 C CD2 . LEU B 205 ? 0.2428 0.2711 0.2668 -0.1176 -0.0037 -0.0110 205 LEU B CD2 
5833 N N   . ASN B 206 ? 0.1757 0.3154 0.2414 -0.0849 -0.0012 0.0042  206 ASN B N   
5834 C CA  . ASN B 206 ? 0.1654 0.3385 0.2456 -0.0805 0.0019  0.0106  206 ASN B CA  
5835 C C   . ASN B 206 ? 0.1553 0.3370 0.2400 -0.0644 0.0015  0.0149  206 ASN B C   
5836 O O   . ASN B 206 ? 0.1689 0.3380 0.2510 -0.0526 0.0064  0.0179  206 ASN B O   
5837 C CB  . ASN B 206 ? 0.2130 0.3855 0.2950 -0.0799 0.0100  0.0145  206 ASN B CB  
5838 C CG  . ASN B 206 ? 0.3316 0.5414 0.4304 -0.0770 0.0137  0.0206  206 ASN B CG  
5839 O OD1 . ASN B 206 ? 0.2380 0.4741 0.3476 -0.0735 0.0100  0.0230  206 ASN B OD1 
5840 N ND2 . ASN B 206 ? 0.4378 0.6515 0.5394 -0.0785 0.0211  0.0233  206 ASN B ND2 
5841 N N   . PRO B 207 ? 0.1792 0.3820 0.2701 -0.0640 -0.0043 0.0154  207 PRO B N   
5842 C CA  . PRO B 207 ? 0.2373 0.4469 0.3319 -0.0487 -0.0048 0.0206  207 PRO B CA  
5843 C C   . PRO B 207 ? 0.1400 0.3637 0.2455 -0.0361 0.0021  0.0287  207 PRO B C   
5844 O O   . PRO B 207 ? 0.1760 0.3923 0.2809 -0.0222 0.0041  0.0325  207 PRO B O   
5845 C CB  . PRO B 207 ? 0.2437 0.4802 0.3443 -0.0537 -0.0123 0.0207  207 PRO B CB  
5846 C CG  . PRO B 207 ? 0.2673 0.4966 0.3610 -0.0713 -0.0161 0.0120  207 PRO B CG  
5847 C CD  . PRO B 207 ? 0.2182 0.4387 0.3118 -0.0781 -0.0105 0.0113  207 PRO B CD  
5848 N N   . ASN B 208 ? 0.1504 0.3930 0.2655 -0.0407 0.0064  0.0311  208 ASN B N   
5849 C CA  . ASN B 208 ? 0.2055 0.4620 0.3317 -0.0280 0.0140  0.0381  208 ASN B CA  
5850 C C   . ASN B 208 ? 0.2221 0.4477 0.3383 -0.0188 0.0212  0.0371  208 ASN B C   
5851 O O   . ASN B 208 ? 0.2033 0.4351 0.3268 -0.0059 0.0281  0.0420  208 ASN B O   
5852 C CB  . ASN B 208 ? 0.2034 0.4872 0.3418 -0.0362 0.0175  0.0400  208 ASN B CB  
5853 C CG  . ASN B 208 ? 0.3076 0.6285 0.4587 -0.0438 0.0108  0.0424  208 ASN B CG  
5854 O OD1 . ASN B 208 ? 0.2588 0.5974 0.4172 -0.0352 0.0067  0.0473  208 ASN B OD1 
5855 N ND2 . ASN B 208 ? 0.4265 0.7590 0.5793 -0.0607 0.0095  0.0390  208 ASN B ND2 
5856 N N   . CYS B 209 ? 0.2396 0.4327 0.3395 -0.0246 0.0200  0.0309  209 CYS B N   
5857 C CA  . CYS B 209 ? 0.2297 0.3953 0.3194 -0.0169 0.0263  0.0299  209 CYS B CA  
5858 C C   . CYS B 209 ? 0.2479 0.4064 0.3374 -0.0015 0.0273  0.0329  209 CYS B C   
5859 O O   . CYS B 209 ? 0.2174 0.3583 0.3011 0.0065  0.0338  0.0328  209 CYS B O   
5860 C CB  . CYS B 209 ? 0.1908 0.3248 0.2637 -0.0258 0.0236  0.0237  209 CYS B CB  
5861 S SG  . CYS B 209 ? 0.2634 0.3799 0.3270 -0.0260 0.0147  0.0195  209 CYS B SG  
5862 N N   . VAL B 210 ? 0.1868 0.3588 0.2820 0.0022  0.0212  0.0357  210 VAL B N   
5863 C CA  . VAL B 210 ? 0.1648 0.3298 0.2598 0.0163  0.0222  0.0395  210 VAL B CA  
5864 C C   . VAL B 210 ? 0.1892 0.3666 0.2957 0.0293  0.0306  0.0458  210 VAL B C   
5865 O O   . VAL B 210 ? 0.1690 0.3311 0.2726 0.0412  0.0350  0.0478  210 VAL B O   
5866 C CB  . VAL B 210 ? 0.1994 0.3789 0.2980 0.0166  0.0137  0.0421  210 VAL B CB  
5867 C CG1 . VAL B 210 ? 0.1332 0.2978 0.2196 0.0048  0.0064  0.0346  210 VAL B CG1 
5868 C CG2 . VAL B 210 ? 0.1801 0.3987 0.2954 0.0152  0.0114  0.0478  210 VAL B CG2 
5869 N N   . TYR B 211 ? 0.1735 0.3781 0.2934 0.0271  0.0335  0.0487  211 TYR B N   
5870 C CA  . TYR B 211 ? 0.2183 0.4381 0.3515 0.0405  0.0418  0.0549  211 TYR B CA  
5871 C C   . TYR B 211 ? 0.2162 0.4145 0.3421 0.0445  0.0523  0.0513  211 TYR B C   
5872 O O   . TYR B 211 ? 0.2736 0.4756 0.4073 0.0578  0.0605  0.0550  211 TYR B O   
5873 C CB  . TYR B 211 ? 0.1451 0.4048 0.2965 0.0369  0.0415  0.0594  211 TYR B CB  
5874 C CG  . TYR B 211 ? 0.2451 0.5307 0.4043 0.0323  0.0311  0.0632  211 TYR B CG  
5875 C CD1 . TYR B 211 ? 0.3242 0.6180 0.4891 0.0441  0.0276  0.0703  211 TYR B CD1 
5876 C CD2 . TYR B 211 ? 0.2366 0.5390 0.3972 0.0156  0.0252  0.0599  211 TYR B CD2 
5877 C CE1 . TYR B 211 ? 0.2494 0.5688 0.4205 0.0393  0.0181  0.0739  211 TYR B CE1 
5878 C CE2 . TYR B 211 ? 0.2163 0.5435 0.3830 0.0102  0.0158  0.0624  211 TYR B CE2 
5879 C CZ  . TYR B 211 ? 0.2346 0.5711 0.4064 0.0221  0.0122  0.0695  211 TYR B CZ  
5880 O OH  . TYR B 211 ? 0.2327 0.5923 0.4076 0.0161  0.0027  0.0717  211 TYR B OH  
5881 N N   . GLU B 212 ? 0.2001 0.3760 0.3109 0.0334  0.0523  0.0442  212 GLU B N   
5882 C CA  . GLU B 212 ? 0.2332 0.3902 0.3355 0.0357  0.0619  0.0407  212 GLU B CA  
5883 C C   . GLU B 212 ? 0.2597 0.3931 0.3550 0.0487  0.0665  0.0404  212 GLU B C   
5884 O O   . GLU B 212 ? 0.2954 0.4226 0.3904 0.0562  0.0767  0.0395  212 GLU B O   
5885 C CB  . GLU B 212 ? 0.2124 0.3497 0.2990 0.0211  0.0596  0.0345  212 GLU B CB  
5886 C CG  . GLU B 212 ? 0.2464 0.4040 0.3391 0.0072  0.0561  0.0346  212 GLU B CG  
5887 C CD  . GLU B 212 ? 0.3660 0.5022 0.4433 -0.0067 0.0536  0.0296  212 GLU B CD  
5888 O OE1 . GLU B 212 ? 0.3849 0.4946 0.4479 -0.0052 0.0564  0.0265  212 GLU B OE1 
5889 O OE2 . GLU B 212 ? 0.4445 0.5906 0.5240 -0.0193 0.0488  0.0290  212 GLU B OE2 
5890 N N   . THR B 213 ? 0.2997 0.4196 0.3890 0.0511  0.0598  0.0407  213 THR B N   
5891 C CA  . THR B 213 ? 0.3567 0.4540 0.4393 0.0622  0.0638  0.0407  213 THR B CA  
5892 C C   . THR B 213 ? 0.3440 0.4529 0.4380 0.0744  0.0619  0.0483  213 THR B C   
5893 O O   . THR B 213 ? 0.4542 0.5497 0.5475 0.0862  0.0683  0.0500  213 THR B O   
5894 C CB  . THR B 213 ? 0.3637 0.4315 0.4278 0.0554  0.0587  0.0350  213 THR B CB  
5895 O OG1 . THR B 213 ? 0.4786 0.5531 0.5428 0.0484  0.0480  0.0356  213 THR B OG1 
5896 C CG2 . THR B 213 ? 0.3688 0.4221 0.4205 0.0455  0.0615  0.0287  213 THR B CG2 
5897 N N   . THR B 214 ? 0.3320 0.4647 0.4355 0.0715  0.0535  0.0529  214 THR B N   
5898 C CA  . THR B 214 ? 0.2785 0.4266 0.3935 0.0825  0.0510  0.0617  214 THR B CA  
5899 C C   . THR B 214 ? 0.3189 0.5065 0.4526 0.0823  0.0490  0.0677  214 THR B C   
5900 O O   . THR B 214 ? 0.3188 0.5258 0.4562 0.0747  0.0397  0.0696  214 THR B O   
5901 C CB  . THR B 214 ? 0.2804 0.4195 0.3868 0.0788  0.0414  0.0620  214 THR B CB  
5902 O OG1 . THR B 214 ? 0.2840 0.4339 0.3878 0.0643  0.0329  0.0579  214 THR B OG1 
5903 C CG2 . THR B 214 ? 0.2493 0.3514 0.3383 0.0791  0.0435  0.0564  214 THR B CG2 
5904 N N   . PRO B 215 ? 0.3742 0.5758 0.5202 0.0902  0.0579  0.0706  215 PRO B N   
5905 C CA  . PRO B 215 ? 0.3294 0.5714 0.4942 0.0886  0.0564  0.0758  215 PRO B CA  
5906 C C   . PRO B 215 ? 0.3850 0.6496 0.5603 0.0944  0.0488  0.0850  215 PRO B C   
5907 O O   . PRO B 215 ? 0.3418 0.6358 0.5264 0.0875  0.0434  0.0874  215 PRO B O   
5908 C CB  . PRO B 215 ? 0.3128 0.5587 0.4860 0.0977  0.0689  0.0761  215 PRO B CB  
5909 C CG  . PRO B 215 ? 0.3270 0.5379 0.4894 0.1089  0.0760  0.0740  215 PRO B CG  
5910 C CD  . PRO B 215 ? 0.3707 0.5525 0.5138 0.1000  0.0701  0.0681  215 PRO B CD  
5911 N N   . ASN B 216 ? 0.4175 0.6642 0.5871 0.1039  0.0474  0.0890  216 ASN B N   
5912 C CA  . ASN B 216 ? 0.4829 0.7450 0.6574 0.1078  0.0403  0.0973  216 ASN B CA  
5913 C C   . ASN B 216 ? 0.4203 0.6866 0.5882 0.0993  0.0293  0.0978  216 ASN B C   
5914 O O   . ASN B 216 ? 0.3362 0.6155 0.5060 0.1008  0.0231  0.1045  216 ASN B O   
5915 C CB  . ASN B 216 ? 0.5588 0.8006 0.7311 0.1223  0.0456  0.1023  216 ASN B CB  
5916 C CG  . ASN B 216 ? 0.5675 0.8025 0.7450 0.1308  0.0570  0.1004  216 ASN B CG  
5917 O OD1 . ASN B 216 ? 0.6236 0.8286 0.7923 0.1365  0.0646  0.0964  216 ASN B OD1 
5918 N ND2 . ASN B 216 ? 0.4410 0.7038 0.6320 0.1307  0.0581  0.1027  216 ASN B ND2 
5919 N N   . VAL B 217 ? 0.4008 0.6567 0.5608 0.0904  0.0271  0.0909  217 VAL B N   
5920 C CA  . VAL B 217 ? 0.3261 0.5833 0.4785 0.0823  0.0171  0.0901  217 VAL B CA  
5921 C C   . VAL B 217 ? 0.2516 0.5416 0.4102 0.0717  0.0085  0.0915  217 VAL B C   
5922 O O   . VAL B 217 ? 0.2779 0.5878 0.4452 0.0664  0.0098  0.0905  217 VAL B O   
5923 C CB  . VAL B 217 ? 0.3010 0.5267 0.4344 0.0700  0.0162  0.0778  217 VAL B CB  
5924 C CG1 . VAL B 217 ? 0.2287 0.4644 0.3625 0.0552  0.0150  0.0705  217 VAL B CG1 
5925 C CG2 . VAL B 217 ? 0.2642 0.4796 0.3859 0.0651  0.0082  0.0760  217 VAL B CG2 
5926 N N   . LYS B 218 ? 0.2189 0.5131 0.3712 0.0679  0.0001  0.0934  218 LYS B N   
5927 C CA  . LYS B 218 ? 0.2042 0.5250 0.3580 0.0560  -0.0082 0.0930  218 LYS B CA  
5928 C C   . LYS B 218 ? 0.2217 0.5381 0.3657 0.0416  -0.0147 0.0837  218 LYS B C   
5929 O O   . LYS B 218 ? 0.2302 0.5289 0.3645 0.0429  -0.0170 0.0821  218 LYS B O   
5930 C CB  . LYS B 218 ? 0.2802 0.6107 0.4331 0.0615  -0.0123 0.1017  218 LYS B CB  
5931 C CG  . LYS B 218 ? 0.3736 0.7150 0.5378 0.0735  -0.0074 0.1110  218 LYS B CG  
5932 C CD  . LYS B 218 ? 0.4563 0.8097 0.6199 0.0775  -0.0121 0.1202  218 LYS B CD  
5933 C CE  . LYS B 218 ? 0.4960 0.8649 0.6725 0.0882  -0.0081 0.1294  218 LYS B CE  
5934 N NZ  . LYS B 218 ? 0.5265 0.8722 0.7062 0.1026  0.0015  0.1315  218 LYS B NZ  
5935 N N   . ILE B 219 ? 0.2052 0.5363 0.3512 0.0273  -0.0175 0.0773  219 ILE B N   
5936 C CA  . ILE B 219 ? 0.2369 0.5607 0.3723 0.0120  -0.0233 0.0670  219 ILE B CA  
5937 C C   . ILE B 219 ? 0.2373 0.5836 0.3721 -0.0015 -0.0295 0.0641  219 ILE B C   
5938 O O   . ILE B 219 ? 0.2005 0.5675 0.3441 -0.0007 -0.0286 0.0691  219 ILE B O   
5939 C CB  . ILE B 219 ? 0.2345 0.5290 0.3612 0.0051  -0.0178 0.0570  219 ILE B CB  
5940 C CG1 . ILE B 219 ? 0.2383 0.5521 0.3763 -0.0008 -0.0145 0.0570  219 ILE B CG1 
5941 C CG2 . ILE B 219 ? 0.1979 0.4602 0.3182 0.0175  -0.0106 0.0578  219 ILE B CG2 
5942 C CD1 . ILE B 219 ? 0.2847 0.5720 0.4134 -0.0099 -0.0101 0.0478  219 ILE B CD1 
5943 N N   . PRO B 220 ? 0.2644 0.6051 0.3878 -0.0139 -0.0354 0.0556  220 PRO B N   
5944 C CA  . PRO B 220 ? 0.2854 0.6429 0.4056 -0.0273 -0.0402 0.0515  220 PRO B CA  
5945 C C   . PRO B 220 ? 0.2164 0.5814 0.3420 -0.0385 -0.0382 0.0466  220 PRO B C   
5946 O O   . PRO B 220 ? 0.1818 0.5385 0.3127 -0.0377 -0.0331 0.0455  220 PRO B O   
5947 C CB  . PRO B 220 ? 0.2023 0.5445 0.3076 -0.0368 -0.0449 0.0417  220 PRO B CB  
5948 C CG  . PRO B 220 ? 0.2341 0.5518 0.3360 -0.0321 -0.0427 0.0386  220 PRO B CG  
5949 C CD  . PRO B 220 ? 0.2209 0.5395 0.3328 -0.0149 -0.0377 0.0498  220 PRO B CD  
5950 N N   . ASP B 221 ? 0.1837 0.5656 0.3076 -0.0493 -0.0418 0.0443  221 ASP B N   
5951 C CA  . ASP B 221 ? 0.2682 0.6585 0.3954 -0.0620 -0.0407 0.0396  221 ASP B CA  
5952 C C   . ASP B 221 ? 0.3172 0.6846 0.4327 -0.0770 -0.0418 0.0265  221 ASP B C   
5953 O O   . ASP B 221 ? 0.2891 0.6522 0.3937 -0.0858 -0.0458 0.0196  221 ASP B O   
5954 C CB  . ASP B 221 ? 0.2927 0.7102 0.4220 -0.0672 -0.0443 0.0427  221 ASP B CB  
5955 C CG  . ASP B 221 ? 0.4011 0.8293 0.5343 -0.0801 -0.0431 0.0387  221 ASP B CG  
5956 O OD1 . ASP B 221 ? 0.4597 0.8757 0.5956 -0.0835 -0.0387 0.0352  221 ASP B OD1 
5957 O OD2 . ASP B 221 ? 0.4660 0.9149 0.5989 -0.0876 -0.0465 0.0391  221 ASP B OD2 
5958 N N   . PHE B 222 ? 0.2271 0.5787 0.3443 -0.0798 -0.0374 0.0230  222 PHE B N   
5959 C CA  . PHE B 222 ? 0.2791 0.6060 0.3851 -0.0940 -0.0378 0.0112  222 PHE B CA  
5960 C C   . PHE B 222 ? 0.3057 0.6417 0.4116 -0.1084 -0.0379 0.0072  222 PHE B C   
5961 O O   . PHE B 222 ? 0.3028 0.6377 0.4135 -0.1135 -0.0338 0.0073  222 PHE B O   
5962 C CB  . PHE B 222 ? 0.1921 0.4971 0.2985 -0.0924 -0.0332 0.0097  222 PHE B CB  
5963 C CG  . PHE B 222 ? 0.2058 0.4874 0.3046 -0.0789 -0.0326 0.0106  222 PHE B CG  
5964 C CD1 . PHE B 222 ? 0.1990 0.4908 0.3044 -0.0624 -0.0314 0.0203  222 PHE B CD1 
5965 C CD2 . PHE B 222 ? 0.1741 0.4211 0.2583 -0.0824 -0.0329 0.0017  222 PHE B CD2 
5966 C CE1 . PHE B 222 ? 0.2223 0.4891 0.3189 -0.0509 -0.0303 0.0207  222 PHE B CE1 
5967 C CE2 . PHE B 222 ? 0.2584 0.4832 0.3348 -0.0704 -0.0321 0.0022  222 PHE B CE2 
5968 C CZ  . PHE B 222 ? 0.1385 0.3730 0.2206 -0.0554 -0.0309 0.0115  222 PHE B CZ  
5969 N N   . ALA B 223 ? 0.2339 0.5787 0.3334 -0.1153 -0.0423 0.0036  223 ALA B N   
5970 C CA  . ALA B 223 ? 0.3246 0.6796 0.4229 -0.1294 -0.0429 -0.0005 223 ALA B CA  
5971 C C   . ALA B 223 ? 0.4001 0.7262 0.4870 -0.1433 -0.0418 -0.0123 223 ALA B C   
5972 O O   . ALA B 223 ? 0.4158 0.7464 0.5003 -0.1560 -0.0420 -0.0167 223 ALA B O   
5973 C CB  . ALA B 223 ? 0.2908 0.6683 0.3867 -0.1312 -0.0476 0.0008  223 ALA B CB  
5974 N N   . VAL B 224 ? 0.3439 0.6399 0.4237 -0.1409 -0.0405 -0.0172 224 VAL B N   
5975 C CA  . VAL B 224 ? 0.2943 0.5582 0.3629 -0.1515 -0.0391 -0.0277 224 VAL B CA  
5976 C C   . VAL B 224 ? 0.2397 0.4801 0.3087 -0.1480 -0.0352 -0.0268 224 VAL B C   
5977 O O   . VAL B 224 ? 0.2415 0.4863 0.3165 -0.1367 -0.0344 -0.0205 224 VAL B O   
5978 C CB  . VAL B 224 ? 0.3358 0.5841 0.3923 -0.1520 -0.0420 -0.0360 224 VAL B CB  
5979 C CG1 . VAL B 224 ? 0.3613 0.5987 0.4162 -0.1393 -0.0427 -0.0343 224 VAL B CG1 
5980 C CG2 . VAL B 224 ? 0.4337 0.6518 0.4796 -0.1629 -0.0403 -0.0467 224 VAL B CG2 
5981 N N   . SER B 225 ? 0.2324 0.4470 0.2947 -0.1576 -0.0326 -0.0326 225 SER B N   
5982 C CA  . SER B 225 ? 0.2521 0.4420 0.3127 -0.1558 -0.0286 -0.0315 225 SER B CA  
5983 C C   . SER B 225 ? 0.2396 0.3962 0.2891 -0.1515 -0.0294 -0.0379 225 SER B C   
5984 O O   . SER B 225 ? 0.2593 0.3982 0.2997 -0.1559 -0.0308 -0.0460 225 SER B O   
5985 C CB  . SER B 225 ? 0.3055 0.4835 0.3643 -0.1672 -0.0250 -0.0326 225 SER B CB  
5986 O OG  . SER B 225 ? 0.2723 0.4220 0.3265 -0.1657 -0.0213 -0.0316 225 SER B OG  
5987 N N   . PHE B 226 ? 0.2612 0.4092 0.3117 -0.1427 -0.0282 -0.0341 226 PHE B N   
5988 C CA  . PHE B 226 ? 0.2578 0.3727 0.2979 -0.1379 -0.0283 -0.0391 226 PHE B CA  
5989 C C   . PHE B 226 ? 0.2363 0.3208 0.2708 -0.1387 -0.0238 -0.0377 226 PHE B C   
5990 O O   . PHE B 226 ? 0.2423 0.2990 0.2690 -0.1303 -0.0230 -0.0386 226 PHE B O   
5991 C CB  . PHE B 226 ? 0.2275 0.3451 0.2682 -0.1202 -0.0286 -0.0339 226 PHE B CB  
5992 C CG  . PHE B 226 ? 0.2830 0.4220 0.3252 -0.1188 -0.0335 -0.0361 226 PHE B CG  
5993 C CD1 . PHE B 226 ? 0.3221 0.4466 0.3552 -0.1211 -0.0364 -0.0453 226 PHE B CD1 
5994 C CD2 . PHE B 226 ? 0.2626 0.4367 0.3153 -0.1148 -0.0351 -0.0287 226 PHE B CD2 
5995 C CE1 . PHE B 226 ? 0.3063 0.4482 0.3387 -0.1178 -0.0398 -0.0462 226 PHE B CE1 
5996 C CE2 . PHE B 226 ? 0.3642 0.5589 0.4175 -0.1137 -0.0400 -0.0296 226 PHE B CE2 
5997 C CZ  . PHE B 226 ? 0.3450 0.5214 0.3868 -0.1145 -0.0418 -0.0381 226 PHE B CZ  
5998 N N   . ARG B 227 ? 0.2607 0.4158 0.2763 -0.1366 0.0256  -0.1020 227 ARG B N   
5999 C CA  . ARG B 227 ? 0.2787 0.4081 0.2948 -0.1414 0.0277  -0.0918 227 ARG B CA  
6000 C C   . ARG B 227 ? 0.2365 0.3274 0.2523 -0.1454 0.0275  -0.0941 227 ARG B C   
6001 O O   . ARG B 227 ? 0.2338 0.3001 0.2476 -0.1420 0.0284  -0.0860 227 ARG B O   
6002 C CB  . ARG B 227 ? 0.2887 0.4307 0.3086 -0.1506 0.0290  -0.0880 227 ARG B CB  
6003 C CG  . ARG B 227 ? 0.3120 0.4865 0.3311 -0.1438 0.0297  -0.0823 227 ARG B CG  
6004 C CD  . ARG B 227 ? 0.3378 0.5259 0.3617 -0.1523 0.0313  -0.0793 227 ARG B CD  
6005 N NE  . ARG B 227 ? 0.3691 0.5310 0.3926 -0.1592 0.0344  -0.0706 227 ARG B NE  
6006 C CZ  . ARG B 227 ? 0.4887 0.6435 0.5071 -0.1534 0.0367  -0.0593 227 ARG B CZ  
6007 N NH1 . ARG B 227 ? 0.4331 0.6031 0.4474 -0.1408 0.0361  -0.0556 227 ARG B NH1 
6008 N NH2 . ARG B 227 ? 0.5466 0.6780 0.5634 -0.1597 0.0396  -0.0514 227 ARG B NH2 
6009 N N   . GLU B 228 ? 0.2556 0.3403 0.2735 -0.1518 0.0260  -0.1048 228 GLU B N   
6010 C CA  . GLU B 228 ? 0.3732 0.4203 0.3905 -0.1536 0.0259  -0.1066 228 GLU B CA  
6011 C C   . GLU B 228 ? 0.3623 0.3962 0.3761 -0.1416 0.0258  -0.1082 228 GLU B C   
6012 O O   . GLU B 228 ? 0.2981 0.3009 0.3115 -0.1387 0.0261  -0.1037 228 GLU B O   
6013 C CB  . GLU B 228 ? 0.5273 0.5694 0.5471 -0.1628 0.0243  -0.1184 228 GLU B CB  
6014 C CG  . GLU B 228 ? 0.7365 0.7379 0.7566 -0.1664 0.0246  -0.1169 228 GLU B CG  
6015 C CD  . GLU B 228 ? 0.8753 0.8619 0.8976 -0.1730 0.0265  -0.1040 228 GLU B CD  
6016 O OE1 . GLU B 228 ? 0.9430 0.8960 0.9646 -0.1733 0.0267  -0.0994 228 GLU B OE1 
6017 O OE2 . GLU B 228 ? 0.8955 0.9042 0.9197 -0.1772 0.0280  -0.0982 228 GLU B OE2 
6018 N N   . ASP B 229 ? 0.2512 0.3090 0.2628 -0.1339 0.0254  -0.1144 229 ASP B N   
6019 C CA  . ASP B 229 ? 0.3235 0.3717 0.3327 -0.1223 0.0264  -0.1157 229 ASP B CA  
6020 C C   . ASP B 229 ? 0.2272 0.2630 0.2376 -0.1173 0.0275  -0.1032 229 ASP B C   
6021 O O   . ASP B 229 ? 0.2316 0.2422 0.2430 -0.1111 0.0281  -0.1016 229 ASP B O   
6022 C CB  . ASP B 229 ? 0.2461 0.3256 0.2515 -0.1142 0.0263  -0.1226 229 ASP B CB  
6023 C CG  . ASP B 229 ? 0.3343 0.4193 0.3366 -0.1156 0.0250  -0.1361 229 ASP B CG  
6024 O OD1 . ASP B 229 ? 0.3531 0.4161 0.3568 -0.1231 0.0244  -0.1412 229 ASP B OD1 
6025 O OD2 . ASP B 229 ? 0.2957 0.4051 0.2931 -0.1081 0.0246  -0.1410 229 ASP B OD2 
6026 N N   . ALA B 230 ? 0.2351 0.2890 0.2456 -0.1190 0.0276  -0.0943 230 ALA B N   
6027 C CA  . ALA B 230 ? 0.2437 0.2854 0.2542 -0.1149 0.0282  -0.0823 230 ALA B CA  
6028 C C   . ALA B 230 ? 0.2334 0.2387 0.2439 -0.1180 0.0275  -0.0762 230 ALA B C   
6029 O O   . ALA B 230 ? 0.2527 0.2373 0.2637 -0.1113 0.0269  -0.0709 230 ALA B O   
6030 C CB  . ALA B 230 ? 0.2318 0.2978 0.2414 -0.1166 0.0290  -0.0737 230 ALA B CB  
6031 N N   . SER B 231 ? 0.2392 0.2370 0.2498 -0.1278 0.0273  -0.0770 231 SER B N   
6032 C CA  . SER B 231 ? 0.2884 0.2519 0.2987 -0.1301 0.0265  -0.0712 231 SER B CA  
6033 C C   . SER B 231 ? 0.2825 0.2225 0.2946 -0.1233 0.0253  -0.0774 231 SER B C   
6034 O O   . SER B 231 ? 0.3166 0.2303 0.3288 -0.1181 0.0238  -0.0703 231 SER B O   
6035 C CB  . SER B 231 ? 0.3639 0.3250 0.3754 -0.1426 0.0272  -0.0721 231 SER B CB  
6036 O OG  . SER B 231 ? 0.5156 0.4938 0.5257 -0.1478 0.0292  -0.0642 231 SER B OG  
6037 N N   . LYS B 232 ? 0.3014 0.2510 0.3145 -0.1226 0.0259  -0.0905 232 LYS B N   
6038 C CA  . LYS B 232 ? 0.3464 0.2740 0.3606 -0.1157 0.0259  -0.0972 232 LYS B CA  
6039 C C   . LYS B 232 ? 0.3059 0.2282 0.3226 -0.1026 0.0265  -0.0936 232 LYS B C   
6040 O O   . LYS B 232 ? 0.2833 0.1805 0.3028 -0.0955 0.0259  -0.0919 232 LYS B O   
6041 C CB  . LYS B 232 ? 0.3535 0.2940 0.3663 -0.1173 0.0268  -0.1125 232 LYS B CB  
6042 C CG  . LYS B 232 ? 0.5561 0.5018 0.5685 -0.1304 0.0256  -0.1175 232 LYS B CG  
6043 C CD  . LYS B 232 ? 0.6636 0.6210 0.6735 -0.1317 0.0254  -0.1330 232 LYS B CD  
6044 C CE  . LYS B 232 ? 0.7782 0.7243 0.7892 -0.1441 0.0239  -0.1387 232 LYS B CE  
6045 N NZ  . LYS B 232 ? 0.8264 0.7760 0.8337 -0.1444 0.0231  -0.1544 232 LYS B NZ  
6046 N N   . HIS B 233 ? 0.2470 0.1935 0.2640 -0.0987 0.0278  -0.0927 233 HIS B N   
6047 C CA  . HIS B 233 ? 0.2322 0.1753 0.2534 -0.0855 0.0283  -0.0868 233 HIS B CA  
6048 C C   . HIS B 233 ? 0.3027 0.2206 0.3260 -0.0839 0.0253  -0.0747 233 HIS B C   
6049 O O   . HIS B 233 ? 0.2400 0.1419 0.2692 -0.0735 0.0244  -0.0720 233 HIS B O   
6050 C CB  . HIS B 233 ? 0.2068 0.1803 0.2263 -0.0791 0.0288  -0.0808 233 HIS B CB  
6051 C CG  . HIS B 233 ? 0.2335 0.2310 0.2506 -0.0740 0.0317  -0.0898 233 HIS B CG  
6052 N ND1 . HIS B 233 ? 0.2225 0.2204 0.2424 -0.0613 0.0348  -0.0920 233 HIS B ND1 
6053 C CD2 . HIS B 233 ? 0.2064 0.2299 0.2182 -0.0792 0.0320  -0.0963 233 HIS B CD2 
6054 C CE1 . HIS B 233 ? 0.2379 0.2591 0.2520 -0.0587 0.0372  -0.0990 233 HIS B CE1 
6055 N NE2 . HIS B 233 ? 0.2203 0.2577 0.2294 -0.0692 0.0348  -0.1020 233 HIS B NE2 
6056 N N   . VAL B 234 ? 0.2408 0.1574 0.2591 -0.0929 0.0237  -0.0666 234 VAL B N   
6057 C CA  . VAL B 234 ? 0.3012 0.1962 0.3180 -0.0906 0.0202  -0.0538 234 VAL B CA  
6058 C C   . VAL B 234 ? 0.2740 0.1400 0.2919 -0.0893 0.0178  -0.0533 234 VAL B C   
6059 O O   . VAL B 234 ? 0.2831 0.1299 0.3039 -0.0803 0.0145  -0.0473 234 VAL B O   
6060 C CB  . VAL B 234 ? 0.3024 0.2059 0.3116 -0.0994 0.0200  -0.0448 234 VAL B CB  
6061 C CG1 . VAL B 234 ? 0.3438 0.2239 0.3484 -0.0971 0.0163  -0.0318 234 VAL B CG1 
6062 C CG2 . VAL B 234 ? 0.2477 0.1815 0.2556 -0.0961 0.0212  -0.0433 234 VAL B CG2 
6063 N N   . GLU B 235 ? 0.2913 0.1543 0.3074 -0.0980 0.0190  -0.0596 235 GLU B N   
6064 C CA  . GLU B 235 ? 0.3195 0.1534 0.3359 -0.0979 0.0170  -0.0588 235 GLU B CA  
6065 C C   . GLU B 235 ? 0.4234 0.2447 0.4443 -0.0862 0.0168  -0.0651 235 GLU B C   
6066 O O   . GLU B 235 ? 0.3413 0.1382 0.3629 -0.0792 0.0136  -0.0593 235 GLU B O   
6067 C CB  . GLU B 235 ? 0.3382 0.1722 0.3528 -0.1105 0.0188  -0.0655 235 GLU B CB  
6068 C CG  . GLU B 235 ? 0.7225 0.5271 0.7362 -0.1140 0.0170  -0.0589 235 GLU B CG  
6069 C CD  . GLU B 235 ? 0.8249 0.6275 0.8356 -0.1180 0.0166  -0.0445 235 GLU B CD  
6070 O OE1 . GLU B 235 ? 0.8843 0.7097 0.8928 -0.1253 0.0193  -0.0431 235 GLU B OE1 
6071 O OE2 . GLU B 235 ? 0.8888 0.6679 0.8987 -0.1128 0.0140  -0.0345 235 GLU B OE2 
6072 N N   . LEU B 236 ? 0.3136 0.1521 0.3372 -0.0832 0.0205  -0.0767 236 LEU B N   
6073 C CA  . LEU B 236 ? 0.3641 0.1935 0.3929 -0.0712 0.0221  -0.0829 236 LEU B CA  
6074 C C   . LEU B 236 ? 0.3444 0.1708 0.3806 -0.0585 0.0202  -0.0738 236 LEU B C   
6075 O O   . LEU B 236 ? 0.3167 0.1272 0.3577 -0.0482 0.0194  -0.0728 236 LEU B O   
6076 C CB  . LEU B 236 ? 0.3584 0.2094 0.3877 -0.0704 0.0272  -0.0969 236 LEU B CB  
6077 C CG  . LEU B 236 ? 0.3282 0.1803 0.3510 -0.0807 0.0282  -0.1084 236 LEU B CG  
6078 C CD1 . LEU B 236 ? 0.3195 0.1978 0.3401 -0.0797 0.0320  -0.1210 236 LEU B CD1 
6079 C CD2 . LEU B 236 ? 0.3594 0.1823 0.3814 -0.0782 0.0276  -0.1121 236 LEU B CD2 
6080 N N   . ALA B 237 ? 0.2847 0.1273 0.3223 -0.0589 0.0193  -0.0671 237 ALA B N   
6081 C CA  . ALA B 237 ? 0.2703 0.1108 0.3159 -0.0479 0.0161  -0.0580 237 ALA B CA  
6082 C C   . ALA B 237 ? 0.3007 0.1161 0.3422 -0.0457 0.0099  -0.0469 237 ALA B C   
6083 O O   . ALA B 237 ? 0.2980 0.1052 0.3464 -0.0341 0.0070  -0.0426 237 ALA B O   
6084 C CB  . ALA B 237 ? 0.2451 0.1069 0.2908 -0.0498 0.0159  -0.0531 237 ALA B CB  
6085 N N   . LYS B 238 ? 0.3042 0.1090 0.3347 -0.0565 0.0079  -0.0419 238 LYS B N   
6086 C CA  . LYS B 238 ? 0.3772 0.1555 0.4008 -0.0550 0.0025  -0.0312 238 LYS B CA  
6087 C C   . LYS B 238 ? 0.3740 0.1306 0.3987 -0.0472 0.0026  -0.0348 238 LYS B C   
6088 O O   . LYS B 238 ? 0.3728 0.1142 0.3965 -0.0372 0.0001  -0.0276 238 LYS B O   
6089 C CB  . LYS B 238 ? 0.3793 0.1532 0.3966 -0.0683 0.0018  -0.0264 238 LYS B CB  
6090 C CG  . LYS B 238 ? 0.3608 0.1532 0.3753 -0.0740 0.0029  -0.0199 238 LYS B CG  
6091 C CD  . LYS B 238 ? 0.3627 0.1561 0.3712 -0.0873 0.0066  -0.0174 238 LYS B CD  
6092 C CE  . LYS B 238 ? 0.4588 0.2264 0.4658 -0.0870 0.0052  -0.0076 238 LYS B CE  
6093 N NZ  . LYS B 238 ? 0.4925 0.2611 0.4930 -0.1006 0.0100  -0.0048 238 LYS B NZ  
6094 N N   . GLU B 239 ? 0.3624 0.1178 0.3884 -0.0513 0.0064  -0.0462 239 GLU B N   
6095 C CA  . GLU B 239 ? 0.4120 0.1450 0.4380 -0.0444 0.0070  -0.0503 239 GLU B CA  
6096 C C   . GLU B 239 ? 0.4580 0.1970 0.4951 -0.0283 0.0086  -0.0519 239 GLU B C   
6097 O O   . GLU B 239 ? 0.3985 0.1194 0.4363 -0.0182 0.0070  -0.0477 239 GLU B O   
6098 C CB  . GLU B 239 ? 0.4290 0.1620 0.4540 -0.0527 0.0112  -0.0636 239 GLU B CB  
6099 C CG  . GLU B 239 ? 0.5962 0.3327 0.6161 -0.0692 0.0109  -0.0635 239 GLU B CG  
6100 C CD  . GLU B 239 ? 0.7186 0.4652 0.7382 -0.0774 0.0155  -0.0786 239 GLU B CD  
6101 O OE1 . GLU B 239 ? 0.7511 0.5116 0.7687 -0.0903 0.0164  -0.0804 239 GLU B OE1 
6102 O OE2 . GLU B 239 ? 0.7586 0.5004 0.7794 -0.0704 0.0182  -0.0888 239 GLU B OE2 
6103 N N   . LYS B 240 ? 0.3516 0.1173 0.3987 -0.0255 0.0122  -0.0581 240 LYS B N   
6104 C CA  . LYS B 240 ? 0.3924 0.1692 0.4542 -0.0110 0.0138  -0.0593 240 LYS B CA  
6105 C C   . LYS B 240 ? 0.3485 0.1241 0.4162 -0.0026 0.0076  -0.0465 240 LYS B C   
6106 O O   . LYS B 240 ? 0.3413 0.1132 0.4188 0.0096  0.0066  -0.0446 240 LYS B O   
6107 C CB  . LYS B 240 ? 0.3525 0.1578 0.4221 -0.0112 0.0189  -0.0666 240 LYS B CB  
6108 C CG  . LYS B 240 ? 0.3846 0.2032 0.4701 0.0025  0.0223  -0.0689 240 LYS B CG  
6109 C CD  . LYS B 240 ? 0.4989 0.3084 0.5844 0.0079  0.0279  -0.0791 240 LYS B CD  
6110 C CE  . LYS B 240 ? 0.5374 0.3639 0.6384 0.0205  0.0329  -0.0812 240 LYS B CE  
6111 N NZ  . LYS B 240 ? 0.6196 0.4380 0.7197 0.0269  0.0389  -0.0908 240 LYS B NZ  
6112 N N   . TYR B 241 ? 0.3230 0.1030 0.3851 -0.0088 0.0032  -0.0380 241 TYR B N   
6113 C CA  . TYR B 241 ? 0.4395 0.2210 0.5069 -0.0010 -0.0035 -0.0269 241 TYR B CA  
6114 C C   . TYR B 241 ? 0.4866 0.2420 0.5469 0.0037  -0.0067 -0.0197 241 TYR B C   
6115 O O   . TYR B 241 ? 0.3516 0.1078 0.4223 0.0156  -0.0110 -0.0147 241 TYR B O   
6116 C CB  . TYR B 241 ? 0.3675 0.1601 0.4290 -0.0086 -0.0069 -0.0207 241 TYR B CB  
6117 C CG  . TYR B 241 ? 0.4562 0.2531 0.5217 -0.0020 -0.0153 -0.0099 241 TYR B CG  
6118 C CD1 . TYR B 241 ? 0.5565 0.3353 0.6132 0.0005  -0.0207 -0.0001 241 TYR B CD1 
6119 C CD2 . TYR B 241 ? 0.4101 0.2296 0.4890 0.0026  -0.0180 -0.0102 241 TYR B CD2 
6120 C CE1 . TYR B 241 ? 0.5665 0.3517 0.6268 0.0069  -0.0301 0.0086  241 TYR B CE1 
6121 C CE2 . TYR B 241 ? 0.5375 0.3622 0.6206 0.0081  -0.0269 -0.0021 241 TYR B CE2 
6122 C CZ  . TYR B 241 ? 0.5326 0.3407 0.6061 0.0103  -0.0337 0.0069  241 TYR B CZ  
6123 O OH  . TYR B 241 ? 0.6257 0.4404 0.7027 0.0157  -0.0441 0.0140  241 TYR B OH  
6124 N N   . PHE B 242 ? 0.3735 0.1059 0.4167 -0.0055 -0.0044 -0.0191 242 PHE B N   
6125 C CA  . PHE B 242 ? 0.4074 0.1115 0.4428 -0.0004 -0.0053 -0.0126 242 PHE B CA  
6126 C C   . PHE B 242 ? 0.4765 0.1754 0.5229 0.0127  -0.0042 -0.0179 242 PHE B C   
6127 O O   . PHE B 242 ? 0.5034 0.1944 0.5548 0.0246  -0.0076 -0.0108 242 PHE B O   
6128 C CB  . PHE B 242 ? 0.4349 0.1139 0.4505 -0.0137 -0.0019 -0.0130 242 PHE B CB  
6129 C CG  . PHE B 242 ? 0.4723 0.1197 0.4775 -0.0090 -0.0010 -0.0041 242 PHE B CG  
6130 C CD1 . PHE B 242 ? 0.4779 0.1204 0.4792 -0.0094 -0.0003 0.0092  242 PHE B CD1 
6131 C CD2 . PHE B 242 ? 0.5049 0.1301 0.5082 -0.0024 -0.0004 -0.0087 242 PHE B CD2 
6132 C CE1 . PHE B 242 ? 0.5554 0.1735 0.5523 -0.0037 0.0016  0.0185  242 PHE B CE1 
6133 C CE2 . PHE B 242 ? 0.5368 0.1343 0.5312 0.0032  0.0009  0.0001  242 PHE B CE2 
6134 C CZ  . PHE B 242 ? 0.5409 0.1360 0.5329 0.0026  0.0030  0.0140  242 PHE B CZ  
6135 N N   . GLU B 243 ? 0.4158 0.1204 0.4667 0.0112  0.0008  -0.0305 243 GLU B N   
6136 C CA  . GLU B 243 ? 0.4271 0.1287 0.4887 0.0237  0.0035  -0.0365 243 GLU B CA  
6137 C C   . GLU B 243 ? 0.5377 0.2597 0.6190 0.0374  0.0003  -0.0317 243 GLU B C   
6138 O O   . GLU B 243 ? 0.4862 0.1995 0.5741 0.0497  -0.0012 -0.0285 243 GLU B O   
6139 C CB  . GLU B 243 ? 0.5135 0.2248 0.5779 0.0198  0.0102  -0.0512 243 GLU B CB  
6140 C CG  . GLU B 243 ? 0.6465 0.3755 0.7287 0.0327  0.0143  -0.0573 243 GLU B CG  
6141 C CD  . GLU B 243 ? 0.8255 0.5676 0.9084 0.0287  0.0219  -0.0713 243 GLU B CD  
6142 O OE1 . GLU B 243 ? 0.8614 0.6187 0.9569 0.0383  0.0267  -0.0763 243 GLU B OE1 
6143 O OE2 . GLU B 243 ? 0.8829 0.6212 0.9537 0.0160  0.0232  -0.0771 243 GLU B OE2 
6144 N N   . ILE B 244 ? 0.4112 0.1611 0.5026 0.0353  -0.0012 -0.0313 244 ILE B N   
6145 C CA  . ILE B 244 ? 0.4783 0.2510 0.5907 0.0462  -0.0042 -0.0286 244 ILE B CA  
6146 C C   . ILE B 244 ? 0.4456 0.2158 0.5598 0.0512  -0.0140 -0.0163 244 ILE B C   
6147 O O   . ILE B 244 ? 0.5132 0.2886 0.6417 0.0630  -0.0177 -0.0131 244 ILE B O   
6148 C CB  . ILE B 244 ? 0.4676 0.2690 0.5894 0.0416  -0.0016 -0.0329 244 ILE B CB  
6149 C CG1 . ILE B 244 ? 0.4012 0.2059 0.5193 0.0369  0.0080  -0.0451 244 ILE B CG1 
6150 C CG2 . ILE B 244 ? 0.3913 0.2159 0.5357 0.0514  -0.0034 -0.0313 244 ILE B CG2 
6151 C CD1 . ILE B 244 ? 0.3500 0.1536 0.4768 0.0466  0.0142  -0.0525 244 ILE B CD1 
6152 N N   . PHE B 245 ? 0.3679 0.1310 0.4677 0.0427  -0.0184 -0.0093 245 PHE B N   
6153 C CA  . PHE B 245 ? 0.4377 0.2046 0.5395 0.0469  -0.0285 0.0017  245 PHE B CA  
6154 C C   . PHE B 245 ? 0.5271 0.2671 0.6109 0.0465  -0.0316 0.0115  245 PHE B C   
6155 O O   . PHE B 245 ? 0.5438 0.2860 0.6282 0.0517  -0.0409 0.0210  245 PHE B O   
6156 C CB  . PHE B 245 ? 0.3920 0.1792 0.4944 0.0393  -0.0323 0.0031  245 PHE B CB  
6157 C CG  . PHE B 245 ? 0.4447 0.2588 0.5661 0.0411  -0.0294 -0.0042 245 PHE B CG  
6158 C CD1 . PHE B 245 ? 0.4731 0.3033 0.6157 0.0510  -0.0336 -0.0036 245 PHE B CD1 
6159 C CD2 . PHE B 245 ? 0.3893 0.2130 0.5078 0.0327  -0.0221 -0.0114 245 PHE B CD2 
6160 C CE1 . PHE B 245 ? 0.5009 0.3550 0.6611 0.0518  -0.0293 -0.0096 245 PHE B CE1 
6161 C CE2 . PHE B 245 ? 0.4639 0.3110 0.5989 0.0349  -0.0180 -0.0170 245 PHE B CE2 
6162 C CZ  . PHE B 245 ? 0.4784 0.3402 0.6341 0.0440  -0.0211 -0.0159 245 PHE B CZ  
6163 N N   . GLY B 246 ? 0.4461 0.1611 0.5139 0.0402  -0.0243 0.0095  246 GLY B N   
6164 C CA  . GLY B 246 ? 0.5366 0.2237 0.5888 0.0408  -0.0249 0.0192  246 GLY B CA  
6165 C C   . GLY B 246 ? 0.5972 0.2823 0.6360 0.0329  -0.0287 0.0294  246 GLY B C   
6166 O O   . GLY B 246 ? 0.6382 0.3131 0.6717 0.0393  -0.0344 0.0409  246 GLY B O   
6167 N N   . GLU B 247 ? 0.5753 0.2706 0.6080 0.0196  -0.0256 0.0258  247 GLU B N   
6168 C CA  . GLU B 247 ? 0.6436 0.3369 0.6625 0.0107  -0.0274 0.0346  247 GLU B CA  
6169 C C   . GLU B 247 ? 0.4909 0.1900 0.5042 -0.0049 -0.0192 0.0270  247 GLU B C   
6170 O O   . GLU B 247 ? 0.4324 0.1457 0.4537 -0.0070 -0.0164 0.0161  247 GLU B O   
6171 C CB  . GLU B 247 ? 0.7783 0.4914 0.8001 0.0158  -0.0392 0.0410  247 GLU B CB  
6172 C CG  . GLU B 247 ? 0.9651 0.6672 0.9706 0.0160  -0.0453 0.0547  247 GLU B CG  
6173 C CD  . GLU B 247 ? 1.0707 0.7917 1.0749 0.0189  -0.0572 0.0589  247 GLU B CD  
6174 O OE1 . GLU B 247 ? 1.0950 0.8351 1.1164 0.0254  -0.0629 0.0533  247 GLU B OE1 
6175 O OE2 . GLU B 247 ? 1.1110 0.8274 1.0968 0.0143  -0.0603 0.0675  247 GLU B OE2 
6176 N N   . HIS B 248 ? 0.5101 0.2006 0.5115 -0.0155 -0.0157 0.0331  248 HIS B N   
6177 C CA  . HIS B 248 ? 0.6333 0.3363 0.6328 -0.0302 -0.0098 0.0271  248 HIS B CA  
6178 C C   . HIS B 248 ? 0.5719 0.2993 0.5716 -0.0294 -0.0169 0.0281  248 HIS B C   
6179 O O   . HIS B 248 ? 0.6149 0.3432 0.6069 -0.0250 -0.0248 0.0382  248 HIS B O   
6180 C CB  . HIS B 248 ? 0.7469 0.4397 0.7387 -0.0414 -0.0056 0.0343  248 HIS B CB  
6181 C CG  . HIS B 248 ? 0.8695 0.5364 0.8639 -0.0406 -0.0006 0.0373  248 HIS B CG  
6182 N ND1 . HIS B 248 ? 0.9077 0.5558 0.8944 -0.0308 -0.0043 0.0496  248 HIS B ND1 
6183 C CD2 . HIS B 248 ? 0.8952 0.5543 0.9020 -0.0478 0.0053  0.0297  248 HIS B CD2 
6184 C CE1 . HIS B 248 ? 0.9432 0.5695 0.9360 -0.0321 0.0019  0.0502  248 HIS B CE1 
6185 N NE2 . HIS B 248 ? 0.9430 0.5771 0.9489 -0.0427 0.0064  0.0377  248 HIS B NE2 
6186 N N   . PRO B 249 ? 0.6070 0.3533 0.6142 -0.0328 -0.0147 0.0181  249 PRO B N   
6187 C CA  . PRO B 249 ? 0.5185 0.2863 0.5267 -0.0320 -0.0205 0.0195  249 PRO B CA  
6188 C C   . PRO B 249 ? 0.5729 0.3435 0.5652 -0.0420 -0.0204 0.0266  249 PRO B C   
6189 O O   . PRO B 249 ? 0.6600 0.4343 0.6484 -0.0539 -0.0132 0.0230  249 PRO B O   
6190 C CB  . PRO B 249 ? 0.5288 0.3139 0.5483 -0.0342 -0.0158 0.0072  249 PRO B CB  
6191 C CG  . PRO B 249 ? 0.5033 0.2763 0.5203 -0.0415 -0.0077 -0.0005 249 PRO B CG  
6192 C CD  . PRO B 249 ? 0.5365 0.2842 0.5495 -0.0366 -0.0076 0.0050  249 PRO B CD  
6193 N N   . VAL B 250 ? 0.4799 0.2498 0.4623 -0.0374 -0.0284 0.0364  250 VAL B N   
6194 C CA  . VAL B 250 ? 0.4197 0.1929 0.3838 -0.0458 -0.0278 0.0431  250 VAL B CA  
6195 C C   . VAL B 250 ? 0.4057 0.1984 0.3690 -0.0460 -0.0312 0.0410  250 VAL B C   
6196 O O   . VAL B 250 ? 0.3602 0.1586 0.3075 -0.0522 -0.0295 0.0455  250 VAL B O   
6197 C CB  . VAL B 250 ? 0.5087 0.2658 0.4565 -0.0419 -0.0332 0.0558  250 VAL B CB  
6198 C CG1 . VAL B 250 ? 0.5393 0.2752 0.4871 -0.0430 -0.0278 0.0590  250 VAL B CG1 
6199 C CG2 . VAL B 250 ? 0.5856 0.3447 0.5374 -0.0286 -0.0454 0.0588  250 VAL B CG2 
6200 N N   . TYR B 251 ? 0.2884 0.0936 0.2692 -0.0386 -0.0342 0.0339  251 TYR B N   
6201 C CA  . TYR B 251 ? 0.2642 0.0951 0.2486 -0.0376 -0.0331 0.0291  251 TYR B CA  
6202 C C   . TYR B 251 ? 0.2901 0.1356 0.2933 -0.0360 -0.0273 0.0183  251 TYR B C   
6203 O O   . TYR B 251 ? 0.3753 0.2120 0.3915 -0.0317 -0.0273 0.0145  251 TYR B O   
6204 C CB  . TYR B 251 ? 0.2999 0.1332 0.2838 -0.0287 -0.0438 0.0336  251 TYR B CB  
6205 C CG  . TYR B 251 ? 0.3626 0.1844 0.3591 -0.0186 -0.0532 0.0357  251 TYR B CG  
6206 C CD1 . TYR B 251 ? 0.4081 0.2330 0.4270 -0.0132 -0.0514 0.0289  251 TYR B CD1 
6207 C CD2 . TYR B 251 ? 0.3594 0.1648 0.3434 -0.0144 -0.0630 0.0454  251 TYR B CD2 
6208 C CE1 . TYR B 251 ? 0.4295 0.2493 0.4604 -0.0029 -0.0580 0.0305  251 TYR B CE1 
6209 C CE2 . TYR B 251 ? 0.4108 0.2118 0.4064 -0.0040 -0.0701 0.0469  251 TYR B CE2 
6210 C CZ  . TYR B 251 ? 0.4610 0.2695 0.4807 0.0017  -0.0675 0.0395  251 TYR B CZ  
6211 O OH  . TYR B 251 ? 0.4090 0.2150 0.4411 0.0123  -0.0741 0.0411  251 TYR B OH  
6212 N N   . MET B 252 ? 0.2513 0.1183 0.2539 -0.0394 -0.0213 0.0137  252 MET B N   
6213 C CA  . MET B 252 ? 0.2041 0.0872 0.2207 -0.0376 -0.0150 0.0043  252 MET B CA  
6214 C C   . MET B 252 ? 0.2094 0.1134 0.2270 -0.0347 -0.0136 0.0033  252 MET B C   
6215 O O   . MET B 252 ? 0.2169 0.1251 0.2217 -0.0371 -0.0146 0.0078  252 MET B O   
6216 C CB  . MET B 252 ? 0.2415 0.1285 0.2548 -0.0467 -0.0068 -0.0017 252 MET B CB  
6217 C CG  . MET B 252 ? 0.3156 0.1830 0.3330 -0.0488 -0.0060 -0.0048 252 MET B CG  
6218 S SD  . MET B 252 ? 0.2863 0.1644 0.3029 -0.0593 0.0031  -0.0157 252 MET B SD  
6219 C CE  . MET B 252 ? 0.2866 0.1349 0.3075 -0.0607 0.0032  -0.0196 252 MET B CE  
6220 N N   . TRP B 253 ? 0.1690 0.0848 0.2016 -0.0291 -0.0105 -0.0025 253 TRP B N   
6221 C CA  . TRP B 253 ? 0.1533 0.0876 0.1873 -0.0266 -0.0068 -0.0039 253 TRP B CA  
6222 C C   . TRP B 253 ? 0.1736 0.1230 0.2030 -0.0308 0.0021  -0.0087 253 TRP B C   
6223 O O   . TRP B 253 ? 0.1648 0.1170 0.2017 -0.0302 0.0064  -0.0148 253 TRP B O   
6224 C CB  . TRP B 253 ? 0.1536 0.0930 0.2062 -0.0186 -0.0071 -0.0064 253 TRP B CB  
6225 C CG  . TRP B 253 ? 0.1498 0.1062 0.2040 -0.0164 -0.0011 -0.0079 253 TRP B CG  
6226 C CD1 . TRP B 253 ? 0.1414 0.1102 0.2037 -0.0133 0.0072  -0.0123 253 TRP B CD1 
6227 C CD2 . TRP B 253 ? 0.1403 0.1016 0.1858 -0.0166 -0.0021 -0.0045 253 TRP B CD2 
6228 N NE1 . TRP B 253 ? 0.1287 0.1090 0.1884 -0.0113 0.0113  -0.0108 253 TRP B NE1 
6229 C CE2 . TRP B 253 ? 0.2067 0.1822 0.2565 -0.0133 0.0059  -0.0065 253 TRP B CE2 
6230 C CE3 . TRP B 253 ? 0.1438 0.0978 0.1769 -0.0186 -0.0087 0.0001  253 TRP B CE3 
6231 C CZ2 . TRP B 253 ? 0.1362 0.1172 0.1796 -0.0120 0.0077  -0.0043 253 TRP B CZ2 
6232 C CZ3 . TRP B 253 ? 0.1482 0.1085 0.1744 -0.0175 -0.0070 0.0011  253 TRP B CZ3 
6233 C CH2 . TRP B 253 ? 0.1647 0.1377 0.1967 -0.0142 0.0011  -0.0011 253 TRP B CH2 
6234 N N   . PRO B 254 ? 0.1457 0.1062 0.1631 -0.0344 0.0050  -0.0066 254 PRO B N   
6235 C CA  . PRO B 254 ? 0.1669 0.1454 0.1814 -0.0372 0.0124  -0.0111 254 PRO B CA  
6236 C C   . PRO B 254 ? 0.1373 0.1297 0.1601 -0.0294 0.0171  -0.0140 254 PRO B C   
6237 O O   . PRO B 254 ? 0.1748 0.1689 0.1996 -0.0240 0.0166  -0.0106 254 PRO B O   
6238 C CB  . PRO B 254 ? 0.1695 0.1560 0.1703 -0.0415 0.0136  -0.0067 254 PRO B CB  
6239 C CG  . PRO B 254 ? 0.2191 0.1953 0.2161 -0.0374 0.0081  -0.0009 254 PRO B CG  
6240 C CD  . PRO B 254 ? 0.2099 0.1678 0.2155 -0.0351 0.0013  -0.0003 254 PRO B CD  
6241 N N   . PRO B 255 ? 0.1466 0.1477 0.1738 -0.0288 0.0220  -0.0202 255 PRO B N   
6242 C CA  . PRO B 255 ? 0.1301 0.1432 0.1638 -0.0208 0.0275  -0.0219 255 PRO B CA  
6243 C C   . PRO B 255 ? 0.1043 0.1308 0.1313 -0.0174 0.0307  -0.0175 255 PRO B C   
6244 O O   . PRO B 255 ? 0.1482 0.1846 0.1649 -0.0209 0.0315  -0.0164 255 PRO B O   
6245 C CB  . PRO B 255 ? 0.1691 0.1912 0.2018 -0.0223 0.0319  -0.0296 255 PRO B CB  
6246 C CG  . PRO B 255 ? 0.1784 0.1839 0.2119 -0.0294 0.0276  -0.0330 255 PRO B CG  
6247 C CD  . PRO B 255 ? 0.1415 0.1388 0.1679 -0.0352 0.0225  -0.0264 255 PRO B CD  
6248 N N   . GLU B 256 ? 0.1113 0.1374 0.1454 -0.0104 0.0330  -0.0148 256 GLU B N   
6249 C CA  . GLU B 256 ? 0.1439 0.1781 0.1726 -0.0058 0.0366  -0.0104 256 GLU B CA  
6250 C C   . GLU B 256 ? 0.1360 0.1652 0.1549 -0.0093 0.0321  -0.0066 256 GLU B C   
6251 O O   . GLU B 256 ? 0.1185 0.1567 0.1285 -0.0067 0.0355  -0.0040 256 GLU B O   
6252 C CB  . GLU B 256 ? 0.1656 0.2191 0.1874 -0.0021 0.0438  -0.0114 256 GLU B CB  
6253 C CG  . GLU B 256 ? 0.1918 0.2496 0.2201 0.0010  0.0482  -0.0158 256 GLU B CG  
6254 C CD  . GLU B 256 ? 0.2991 0.3527 0.3377 0.0080  0.0533  -0.0130 256 GLU B CD  
6255 O OE1 . GLU B 256 ? 0.4560 0.5024 0.4979 0.0096  0.0527  -0.0082 256 GLU B OE1 
6256 O OE2 . GLU B 256 ? 0.3922 0.4473 0.4348 0.0111  0.0558  -0.0154 256 GLU B OE2 
6257 N N   . ALA B 257 ? 0.1245 0.1390 0.1440 -0.0141 0.0247  -0.0061 257 ALA B N   
6258 C CA  . ALA B 257 ? 0.1320 0.1404 0.1394 -0.0179 0.0203  -0.0026 257 ALA B CA  
6259 C C   . ALA B 257 ? 0.1772 0.1991 0.1731 -0.0219 0.0242  -0.0024 257 ALA B C   
6260 O O   . ALA B 257 ? 0.1820 0.2049 0.1668 -0.0230 0.0242  0.0009  257 ALA B O   
6261 C CB  . ALA B 257 ? 0.1022 0.1062 0.1072 -0.0133 0.0193  0.0002  257 ALA B CB  
6262 N N   . SER B 258 ? 0.1660 0.1994 0.1643 -0.0245 0.0276  -0.0063 258 SER B N   
6263 C CA  . SER B 258 ? 0.1236 0.1760 0.1144 -0.0270 0.0318  -0.0067 258 SER B CA  
6264 C C   . SER B 258 ? 0.1659 0.2143 0.1502 -0.0371 0.0295  -0.0057 258 SER B C   
6265 O O   . SER B 258 ? 0.1962 0.2335 0.1835 -0.0439 0.0266  -0.0081 258 SER B O   
6266 C CB  . SER B 258 ? 0.1811 0.2502 0.1762 -0.0259 0.0357  -0.0120 258 SER B CB  
6267 O OG  . SER B 258 ? 0.2388 0.3285 0.2283 -0.0268 0.0383  -0.0119 258 SER B OG  
6268 N N   . VAL B 259 ? 0.1727 0.2295 0.1479 -0.0378 0.0317  -0.0020 259 VAL B N   
6269 C CA  . VAL B 259 ? 0.1662 0.2215 0.1349 -0.0477 0.0315  0.0000  259 VAL B CA  
6270 C C   . VAL B 259 ? 0.2046 0.2842 0.1710 -0.0478 0.0364  0.0001  259 VAL B C   
6271 O O   . VAL B 259 ? 0.2031 0.2905 0.1725 -0.0361 0.0362  0.0001  259 VAL B O   
6272 C CB  . VAL B 259 ? 0.2060 0.2414 0.1645 -0.0483 0.0278  0.0059  259 VAL B CB  
6273 C CG1 . VAL B 259 ? 0.2435 0.2552 0.2064 -0.0478 0.0208  0.0061  259 VAL B CG1 
6274 C CG2 . VAL B 259 ? 0.2109 0.2501 0.1620 -0.0396 0.0296  0.0087  259 VAL B CG2 
6275 N N   . SER B 260 ? 0.1711 0.2538 0.1363 -0.0579 0.0371  0.0002  260 SER B N   
6276 C CA  . SER B 260 ? 0.1623 0.2609 0.1295 -0.0565 0.0378  0.0003  260 SER B CA  
6277 C C   . SER B 260 ? 0.1610 0.2522 0.1227 -0.0686 0.0395  0.0034  260 SER B C   
6278 O O   . SER B 260 ? 0.1974 0.2704 0.1549 -0.0780 0.0392  0.0051  260 SER B O   
6279 C CB  . SER B 260 ? 0.1607 0.2794 0.1373 -0.0573 0.0369  -0.0061 260 SER B CB  
6280 O OG  . SER B 260 ? 0.2019 0.3201 0.1815 -0.0716 0.0375  -0.0110 260 SER B OG  
6281 N N   . ASN B 261 ? 0.1475 0.2500 0.1093 -0.0682 0.0416  0.0052  261 ASN B N   
6282 C CA  . ASN B 261 ? 0.1885 0.2845 0.1458 -0.0798 0.0443  0.0086  261 ASN B CA  
6283 C C   . ASN B 261 ? 0.2130 0.3058 0.1761 -0.0941 0.0441  0.0044  261 ASN B C   
6284 O O   . ASN B 261 ? 0.2328 0.3044 0.1904 -0.1033 0.0446  0.0081  261 ASN B O   
6285 C CB  . ASN B 261 ? 0.2240 0.3371 0.1838 -0.0777 0.0477  0.0099  261 ASN B CB  
6286 C CG  . ASN B 261 ? 0.2636 0.3729 0.2162 -0.0645 0.0492  0.0141  261 ASN B CG  
6287 O OD1 . ASN B 261 ? 0.2148 0.3052 0.1565 -0.0608 0.0482  0.0177  261 ASN B OD1 
6288 N ND2 . ASN B 261 ? 0.2341 0.3605 0.1919 -0.0578 0.0514  0.0134  261 ASN B ND2 
6289 N N   . GLU B 262 ? 0.1880 0.2991 0.1615 -0.0954 0.0429  -0.0033 262 GLU B N   
6290 C CA  . GLU B 262 ? 0.2178 0.3248 0.1974 -0.1086 0.0426  -0.0093 262 GLU B CA  
6291 C C   . GLU B 262 ? 0.2078 0.2908 0.1865 -0.1106 0.0404  -0.0105 262 GLU B C   
6292 O O   . GLU B 262 ? 0.2158 0.2785 0.1953 -0.1203 0.0397  -0.0114 262 GLU B O   
6293 C CB  . GLU B 262 ? 0.2384 0.3721 0.2274 -0.1088 0.0412  -0.0183 262 GLU B CB  
6294 C CG  . GLU B 262 ? 0.2489 0.4065 0.2409 -0.1075 0.0425  -0.0174 262 GLU B CG  
6295 C CD  . GLU B 262 ? 0.3671 0.5497 0.3675 -0.1119 0.0406  -0.0265 262 GLU B CD  
6296 O OE1 . GLU B 262 ? 0.4019 0.5810 0.4053 -0.1182 0.0390  -0.0343 262 GLU B OE1 
6297 O OE2 . GLU B 262 ? 0.4388 0.6446 0.4429 -0.1085 0.0406  -0.0261 262 GLU B OE2 
6298 N N   . ALA B 263 ? 0.1609 0.2437 0.1388 -0.1004 0.0390  -0.0105 263 ALA B N   
6299 C CA  . ALA B 263 ? 0.1747 0.2322 0.1536 -0.0978 0.0348  -0.0118 263 ALA B CA  
6300 C C   . ALA B 263 ? 0.2171 0.2445 0.1872 -0.0995 0.0325  -0.0036 263 ALA B C   
6301 O O   . ALA B 263 ? 0.2153 0.2189 0.1869 -0.1031 0.0295  -0.0045 263 ALA B O   
6302 C CB  . ALA B 263 ? 0.1662 0.2285 0.1467 -0.0830 0.0330  -0.0129 263 ALA B CB  
6303 N N   . LEU B 264 ? 0.1822 0.2099 0.1419 -0.0963 0.0339  0.0044  264 LEU B N   
6304 C CA  . LEU B 264 ? 0.1979 0.1984 0.1463 -0.0977 0.0313  0.0127  264 LEU B CA  
6305 C C   . LEU B 264 ? 0.2650 0.2534 0.2120 -0.1120 0.0341  0.0149  264 LEU B C   
6306 O O   . LEU B 264 ? 0.2811 0.2412 0.2233 -0.1137 0.0306  0.0193  264 LEU B O   
6307 C CB  . LEU B 264 ? 0.1956 0.2008 0.1308 -0.0921 0.0330  0.0197  264 LEU B CB  
6308 C CG  . LEU B 264 ? 0.2636 0.2717 0.1987 -0.0781 0.0293  0.0183  264 LEU B CG  
6309 C CD1 . LEU B 264 ? 0.2640 0.2828 0.1874 -0.0728 0.0330  0.0222  264 LEU B CD1 
6310 C CD2 . LEU B 264 ? 0.3752 0.3573 0.3090 -0.0727 0.0209  0.0203  264 LEU B CD2 
6311 N N   . GLU B 265 ? 0.2751 0.2843 0.2277 -0.1191 0.0392  0.0115  265 GLU B N   
6312 C CA  . GLU B 265 ? 0.2862 0.2849 0.2408 -0.1296 0.0413  0.0119  265 GLU B CA  
6313 C C   . GLU B 265 ? 0.2441 0.2255 0.2071 -0.1335 0.0380  0.0053  265 GLU B C   
6314 O O   . GLU B 265 ? 0.2813 0.2385 0.2424 -0.1384 0.0377  0.0086  265 GLU B O   
6315 C CB  . GLU B 265 ? 0.3315 0.3587 0.2935 -0.1347 0.0460  0.0081  265 GLU B CB  
6316 C CG  . GLU B 265 ? 0.3576 0.3971 0.3122 -0.1307 0.0501  0.0151  265 GLU B CG  
6317 C CD  . GLU B 265 ? 0.4697 0.5384 0.4343 -0.1343 0.0540  0.0110  265 GLU B CD  
6318 O OE1 . GLU B 265 ? 0.5331 0.6165 0.5092 -0.1386 0.0525  0.0021  265 GLU B OE1 
6319 O OE2 . GLU B 265 ? 0.5047 0.5817 0.4656 -0.1325 0.0583  0.0165  265 GLU B OE2 
6320 N N   . LEU B 266 ? 0.2280 0.2217 0.2002 -0.1302 0.0359  -0.0042 266 LEU B N   
6321 C CA  . LEU B 266 ? 0.2878 0.2652 0.2673 -0.1316 0.0329  -0.0119 266 LEU B CA  
6322 C C   . LEU B 266 ? 0.2916 0.2362 0.2665 -0.1257 0.0285  -0.0064 266 LEU B C   
6323 O O   . LEU B 266 ? 0.3261 0.2470 0.3024 -0.1279 0.0272  -0.0061 266 LEU B O   
6324 C CB  . LEU B 266 ? 0.2348 0.2333 0.2227 -0.1276 0.0320  -0.0229 266 LEU B CB  
6325 C CG  . LEU B 266 ? 0.2388 0.2206 0.2328 -0.1269 0.0293  -0.0318 266 LEU B CG  
6326 C CD1 . LEU B 266 ? 0.2601 0.2327 0.2569 -0.1368 0.0304  -0.0353 266 LEU B CD1 
6327 C CD2 . LEU B 266 ? 0.2324 0.2348 0.2324 -0.1219 0.0290  -0.0424 266 LEU B CD2 
6328 N N   . TYR B 267 ? 0.2333 0.1765 0.2035 -0.1167 0.0256  -0.0018 267 TYR B N   
6329 C CA  . TYR B 267 ? 0.2426 0.1579 0.2097 -0.1082 0.0197  0.0036  267 TYR B CA  
6330 C C   . TYR B 267 ? 0.3241 0.2152 0.2805 -0.1130 0.0195  0.0138  267 TYR B C   
6331 O O   . TYR B 267 ? 0.2934 0.1600 0.2516 -0.1101 0.0162  0.0155  267 TYR B O   
6332 C CB  . TYR B 267 ? 0.2254 0.1488 0.1904 -0.0946 0.0155  0.0071  267 TYR B CB  
6333 C CG  . TYR B 267 ? 0.2642 0.2034 0.2411 -0.0859 0.0148  -0.0014 267 TYR B CG  
6334 C CD1 . TYR B 267 ? 0.2473 0.1742 0.2341 -0.0810 0.0122  -0.0067 267 TYR B CD1 
6335 C CD2 . TYR B 267 ? 0.2056 0.1710 0.1830 -0.0816 0.0177  -0.0033 267 TYR B CD2 
6336 C CE1 . TYR B 267 ? 0.2332 0.1744 0.2297 -0.0729 0.0129  -0.0136 267 TYR B CE1 
6337 C CE2 . TYR B 267 ? 0.2057 0.1840 0.1923 -0.0733 0.0180  -0.0096 267 TYR B CE2 
6338 C CZ  . TYR B 267 ? 0.2687 0.2352 0.2645 -0.0694 0.0160  -0.0146 267 TYR B CZ  
6339 O OH  . TYR B 267 ? 0.2265 0.2063 0.2303 -0.0612 0.0177  -0.0199 267 TYR B OH  
6340 N N   . TYR B 268 ? 0.2725 0.1727 0.2187 -0.1177 0.0234  0.0207  268 TYR B N   
6341 C CA  . TYR B 268 ? 0.2984 0.1792 0.2342 -0.1208 0.0245  0.0305  268 TYR B CA  
6342 C C   . TYR B 268 ? 0.3368 0.2059 0.2814 -0.1281 0.0272  0.0270  268 TYR B C   
6343 O O   . TYR B 268 ? 0.3395 0.1824 0.2808 -0.1264 0.0254  0.0330  268 TYR B O   
6344 C CB  . TYR B 268 ? 0.3442 0.2415 0.2698 -0.1249 0.0303  0.0363  268 TYR B CB  
6345 C CG  . TYR B 268 ? 0.3997 0.2795 0.3160 -0.1292 0.0333  0.0457  268 TYR B CG  
6346 C CD1 . TYR B 268 ? 0.4418 0.2967 0.3442 -0.1222 0.0284  0.0557  268 TYR B CD1 
6347 C CD2 . TYR B 268 ? 0.4167 0.3048 0.3388 -0.1398 0.0407  0.0446  268 TYR B CD2 
6348 C CE1 . TYR B 268 ? 0.5207 0.3591 0.4137 -0.1253 0.0317  0.0651  268 TYR B CE1 
6349 C CE2 . TYR B 268 ? 0.5262 0.3968 0.4404 -0.1441 0.0445  0.0541  268 TYR B CE2 
6350 C CZ  . TYR B 268 ? 0.5149 0.3606 0.4139 -0.1365 0.0403  0.0647  268 TYR B CZ  
6351 O OH  . TYR B 268 ? 0.5862 0.4143 0.4759 -0.1395 0.0443  0.0752  268 TYR B OH  
6352 N N   . GLU B 269 ? 0.3104 0.1993 0.2661 -0.1358 0.0313  0.0174  269 GLU B N   
6353 C CA  . GLU B 269 ? 0.3289 0.2076 0.2927 -0.1442 0.0337  0.0134  269 GLU B CA  
6354 C C   . GLU B 269 ? 0.3375 0.1929 0.3078 -0.1386 0.0290  0.0091  269 GLU B C   
6355 O O   . GLU B 269 ? 0.3615 0.1971 0.3350 -0.1429 0.0299  0.0096  269 GLU B O   
6356 C CB  . GLU B 269 ? 0.3189 0.2256 0.2930 -0.1527 0.0372  0.0026  269 GLU B CB  
6357 C CG  . GLU B 269 ? 0.4163 0.3450 0.3878 -0.1595 0.0429  0.0066  269 GLU B CG  
6358 C CD  . GLU B 269 ? 0.5549 0.4667 0.5228 -0.1676 0.0475  0.0152  269 GLU B CD  
6359 O OE1 . GLU B 269 ? 0.5828 0.4720 0.5551 -0.1717 0.0470  0.0141  269 GLU B OE1 
6360 O OE2 . GLU B 269 ? 0.5420 0.4629 0.5027 -0.1693 0.0521  0.0231  269 GLU B OE2 
6361 N N   . LYS B 270 ? 0.3285 0.1859 0.3015 -0.1288 0.0243  0.0048  270 LYS B N   
6362 C CA  . LYS B 270 ? 0.3895 0.2272 0.3699 -0.1215 0.0200  0.0004  270 LYS B CA  
6363 C C   . LYS B 270 ? 0.3738 0.1874 0.3487 -0.1112 0.0151  0.0108  270 LYS B C   
6364 O O   . LYS B 270 ? 0.3863 0.1866 0.3686 -0.1023 0.0111  0.0079  270 LYS B O   
6365 C CB  . LYS B 270 ? 0.3511 0.2057 0.3393 -0.1162 0.0185  -0.0107 270 LYS B CB  
6366 C CG  . LYS B 270 ? 0.3259 0.2050 0.3192 -0.1248 0.0224  -0.0219 270 LYS B CG  
6367 C CD  . LYS B 270 ? 0.4480 0.3138 0.4457 -0.1326 0.0236  -0.0270 270 LYS B CD  
6368 C CE  . LYS B 270 ? 0.5301 0.4206 0.5326 -0.1413 0.0263  -0.0386 270 LYS B CE  
6369 N NZ  . LYS B 270 ? 0.5908 0.4682 0.5972 -0.1510 0.0275  -0.0435 270 LYS B NZ  
6370 N N   . GLY B 271 ? 0.3713 0.1802 0.3330 -0.1116 0.0153  0.0227  271 GLY B N   
6371 C CA  . GLY B 271 ? 0.3605 0.1468 0.3146 -0.1020 0.0101  0.0332  271 GLY B CA  
6372 C C   . GLY B 271 ? 0.3923 0.1833 0.3428 -0.0910 0.0030  0.0355  271 GLY B C   
6373 O O   . GLY B 271 ? 0.3691 0.1435 0.3163 -0.0810 -0.0033 0.0424  271 GLY B O   
6374 N N   . ILE B 272 ? 0.3181 0.1317 0.2701 -0.0922 0.0034  0.0299  272 ILE B N   
6375 C CA  . ILE B 272 ? 0.3030 0.1215 0.2524 -0.0829 -0.0036 0.0321  272 ILE B CA  
6376 C C   . ILE B 272 ? 0.3566 0.1753 0.2871 -0.0835 -0.0051 0.0428  272 ILE B C   
6377 O O   . ILE B 272 ? 0.3848 0.2178 0.3076 -0.0919 0.0016  0.0436  272 ILE B O   
6378 C CB  . ILE B 272 ? 0.3209 0.1670 0.2816 -0.0813 -0.0012 0.0217  272 ILE B CB  
6379 C CG1 . ILE B 272 ? 0.3933 0.2390 0.3690 -0.0822 0.0014  0.0106  272 ILE B CG1 
6380 C CG2 . ILE B 272 ? 0.3199 0.1763 0.2830 -0.0690 -0.0076 0.0230  272 ILE B CG2 
6381 C CD1 . ILE B 272 ? 0.4924 0.3147 0.4757 -0.0740 -0.0036 0.0108  272 ILE B CD1 
6382 N N   . ASN B 273 ? 0.3383 0.1427 0.2613 -0.0738 -0.0139 0.0505  273 ASN B N   
6383 C CA  . ASN B 273 ? 0.4061 0.2087 0.3084 -0.0729 -0.0162 0.0603  273 ASN B CA  
6384 C C   . ASN B 273 ? 0.3481 0.1699 0.2497 -0.0654 -0.0208 0.0574  273 ASN B C   
6385 O O   . ASN B 273 ? 0.3508 0.1757 0.2346 -0.0653 -0.0210 0.0629  273 ASN B O   
6386 C CB  . ASN B 273 ? 0.4526 0.2337 0.3465 -0.0650 -0.0231 0.0695  273 ASN B CB  
6387 C CG  . ASN B 273 ? 0.5984 0.3645 0.4915 -0.0706 -0.0162 0.0734  273 ASN B CG  
6388 O OD1 . ASN B 273 ? 0.5939 0.3662 0.4849 -0.0818 -0.0064 0.0727  273 ASN B OD1 
6389 N ND2 . ASN B 273 ? 0.6366 0.3838 0.5329 -0.0627 -0.0212 0.0776  273 ASN B ND2 
6390 N N   A MET B 274 ? 0.3182 0.1523 0.2385 -0.0587 -0.0240 0.0486  274 MET B N   
6391 N N   B MET B 274 ? 0.3177 0.1522 0.2381 -0.0589 -0.0237 0.0485  274 MET B N   
6392 C CA  A MET B 274 ? 0.2804 0.1306 0.2023 -0.0515 -0.0282 0.0454  274 MET B CA  
6393 C CA  B MET B 274 ? 0.2837 0.1341 0.2054 -0.0518 -0.0279 0.0454  274 MET B CA  
6394 C C   A MET B 274 ? 0.2647 0.1330 0.2075 -0.0491 -0.0249 0.0350  274 MET B C   
6395 C C   B MET B 274 ? 0.2644 0.1328 0.2072 -0.0492 -0.0248 0.0350  274 MET B C   
6396 O O   A MET B 274 ? 0.2700 0.1340 0.2282 -0.0477 -0.0248 0.0307  274 MET B O   
6397 O O   B MET B 274 ? 0.2711 0.1351 0.2291 -0.0479 -0.0246 0.0307  274 MET B O   
6398 C CB  A MET B 274 ? 0.2999 0.1386 0.2195 -0.0418 -0.0410 0.0496  274 MET B CB  
6399 C CB  B MET B 274 ? 0.3013 0.1396 0.2199 -0.0422 -0.0407 0.0500  274 MET B CB  
6400 C CG  A MET B 274 ? 0.2913 0.1445 0.2113 -0.0360 -0.0458 0.0458  274 MET B CG  
6401 C CG  B MET B 274 ? 0.3009 0.1531 0.2196 -0.0364 -0.0455 0.0463  274 MET B CG  
6402 S SD  A MET B 274 ? 0.2836 0.1519 0.2330 -0.0297 -0.0474 0.0355  274 MET B SD  
6403 S SD  B MET B 274 ? 0.3911 0.2341 0.3151 -0.0257 -0.0620 0.0483  274 MET B SD  
6404 C CE  A MET B 274 ? 0.3369 0.1913 0.2957 -0.0208 -0.0620 0.0389  274 MET B CE  
6405 C CE  B MET B 274 ? 0.3365 0.1909 0.2945 -0.0212 -0.0615 0.0390  274 MET B CE  
6406 N N   . LEU B 275 ? 0.2273 0.1146 0.1696 -0.0478 -0.0217 0.0313  275 LEU B N   
6407 C CA  . LEU B 275 ? 0.2136 0.1166 0.1736 -0.0433 -0.0195 0.0233  275 LEU B CA  
6408 C C   . LEU B 275 ? 0.2602 0.1723 0.2165 -0.0380 -0.0219 0.0227  275 LEU B C   
6409 O O   . LEU B 275 ? 0.2304 0.1380 0.1697 -0.0382 -0.0247 0.0272  275 LEU B O   
6410 C CB  . LEU B 275 ? 0.2787 0.1974 0.2439 -0.0487 -0.0095 0.0178  275 LEU B CB  
6411 C CG  . LEU B 275 ? 0.2866 0.2167 0.2388 -0.0558 -0.0023 0.0196  275 LEU B CG  
6412 C CD1 . LEU B 275 ? 0.3643 0.3113 0.3124 -0.0510 0.0004  0.0186  275 LEU B CD1 
6413 C CD2 . LEU B 275 ? 0.2980 0.2380 0.2579 -0.0628 0.0046  0.0141  275 LEU B CD2 
6414 N N   . ALA B 276 ? 0.1973 0.1208 0.1690 -0.0332 -0.0204 0.0170  276 ALA B N   
6415 C CA  . ALA B 276 ? 0.1860 0.1180 0.1556 -0.0292 -0.0203 0.0154  276 ALA B CA  
6416 C C   . ALA B 276 ? 0.1798 0.1296 0.1544 -0.0290 -0.0100 0.0113  276 ALA B C   
6417 O O   . ALA B 276 ? 0.2277 0.1844 0.2117 -0.0304 -0.0049 0.0083  276 ALA B O   
6418 C CB  . ALA B 276 ? 0.1933 0.1217 0.1773 -0.0233 -0.0282 0.0132  276 ALA B CB  
6419 N N   . THR B 277 ? 0.1501 0.1068 0.1172 -0.0264 -0.0072 0.0110  277 THR B N   
6420 C CA  . THR B 277 ? 0.1505 0.1235 0.1218 -0.0239 0.0020  0.0083  277 THR B CA  
6421 C C   . THR B 277 ? 0.1992 0.1716 0.1692 -0.0183 0.0018  0.0073  277 THR B C   
6422 O O   . THR B 277 ? 0.1943 0.1552 0.1664 -0.0171 -0.0060 0.0068  277 THR B O   
6423 C CB  . THR B 277 ? 0.2008 0.1860 0.1612 -0.0281 0.0091  0.0096  277 THR B CB  
6424 O OG1 . THR B 277 ? 0.2054 0.2081 0.1695 -0.0239 0.0170  0.0074  277 THR B OG1 
6425 C CG2 . THR B 277 ? 0.2234 0.2038 0.1649 -0.0300 0.0082  0.0136  277 THR B CG2 
6426 N N   . ASP B 278 ? 0.1925 0.1768 0.1598 -0.0149 0.0102  0.0066  278 ASP B N   
6427 C CA  . ASP B 278 ? 0.2138 0.1957 0.1832 -0.0093 0.0117  0.0052  278 ASP B CA  
6428 C C   . ASP B 278 ? 0.2370 0.2158 0.1882 -0.0074 0.0130  0.0059  278 ASP B C   
6429 O O   . ASP B 278 ? 0.2129 0.1990 0.1514 -0.0086 0.0169  0.0080  278 ASP B O   
6430 C CB  . ASP B 278 ? 0.2012 0.1954 0.1801 -0.0045 0.0208  0.0046  278 ASP B CB  
6431 C CG  . ASP B 278 ? 0.3228 0.3114 0.3052 0.0008  0.0235  0.0038  278 ASP B CG  
6432 O OD1 . ASP B 278 ? 0.2511 0.2285 0.2435 -0.0004 0.0176  0.0019  278 ASP B OD1 
6433 O OD2 . ASP B 278 ? 0.2736 0.2691 0.2496 0.0062  0.0315  0.0052  278 ASP B OD2 
6434 N N   . GLU B 279 ? 0.2403 0.1226 0.2727 -0.0172 0.0850  -0.0394 279 GLU B N   
6435 C CA  . GLU B 279 ? 0.2412 0.1299 0.2828 -0.0149 0.0917  -0.0499 279 GLU B CA  
6436 C C   . GLU B 279 ? 0.2225 0.1167 0.2834 -0.0065 0.0940  -0.0494 279 GLU B C   
6437 O O   . GLU B 279 ? 0.2271 0.1328 0.2973 -0.0048 0.1004  -0.0572 279 GLU B O   
6438 C CB  . GLU B 279 ? 0.2568 0.1376 0.2971 -0.0149 0.0921  -0.0545 279 GLU B CB  
6439 C CG  . GLU B 279 ? 0.2799 0.1659 0.3244 -0.0156 0.0993  -0.0666 279 GLU B CG  
6440 C CD  . GLU B 279 ? 0.3739 0.2546 0.4126 -0.0185 0.0974  -0.0692 279 GLU B CD  
6441 O OE1 . GLU B 279 ? 0.3456 0.2205 0.3789 -0.0191 0.0904  -0.0614 279 GLU B OE1 
6442 O OE2 . GLU B 279 ? 0.3939 0.2767 0.4336 -0.0203 0.1033  -0.0792 279 GLU B OE2 
6443 N N   . VAL B 280 ? 0.2334 0.1204 0.3017 -0.0019 0.0889  -0.0400 280 VAL B N   
6444 C CA  . VAL B 280 ? 0.2239 0.1175 0.3138 0.0055  0.0892  -0.0370 280 VAL B CA  
6445 C C   . VAL B 280 ? 0.2194 0.1320 0.3111 0.0033  0.0886  -0.0334 280 VAL B C   
6446 O O   . VAL B 280 ? 0.2444 0.1697 0.3554 0.0084  0.0930  -0.0361 280 VAL B O   
6447 C CB  . VAL B 280 ? 0.3243 0.2065 0.4201 0.0083  0.0818  -0.0254 280 VAL B CB  
6448 C CG1 . VAL B 280 ? 0.2351 0.1259 0.3555 0.0148  0.0797  -0.0189 280 VAL B CG1 
6449 C CG2 . VAL B 280 ? 0.3532 0.2234 0.4475 0.0099  0.0808  -0.0283 280 VAL B CG2 
6450 N N   . ILE B 281 ? 0.2431 0.1580 0.3159 -0.0044 0.0837  -0.0275 281 ILE B N   
6451 C CA  . ILE B 281 ? 0.2443 0.1767 0.3161 -0.0081 0.0824  -0.0238 281 ILE B CA  
6452 C C   . ILE B 281 ? 0.2299 0.1764 0.3034 -0.0099 0.0906  -0.0353 281 ILE B C   
6453 O O   . ILE B 281 ? 0.2275 0.1916 0.3137 -0.0085 0.0938  -0.0360 281 ILE B O   
6454 C CB  . ILE B 281 ? 0.2088 0.1370 0.2588 -0.0166 0.0754  -0.0158 281 ILE B CB  
6455 C CG1 . ILE B 281 ? 0.2681 0.1849 0.3166 -0.0162 0.0686  -0.0049 281 ILE B CG1 
6456 C CG2 . ILE B 281 ? 0.2450 0.1905 0.2905 -0.0224 0.0738  -0.0130 281 ILE B CG2 
6457 C CD1 . ILE B 281 ? 0.2889 0.1972 0.3156 -0.0244 0.0637  0.0011  281 ILE B CD1 
6458 N N   . LEU B 282 ? 0.2294 0.1691 0.2905 -0.0140 0.0942  -0.0442 282 LEU B N   
6459 C CA  . LEU B 282 ? 0.2483 0.2000 0.3078 -0.0181 0.1024  -0.0560 282 LEU B CA  
6460 C C   . LEU B 282 ? 0.2557 0.2137 0.3383 -0.0097 0.1121  -0.0651 282 LEU B C   
6461 O O   . LEU B 282 ? 0.2668 0.2430 0.3574 -0.0105 0.1187  -0.0701 282 LEU B O   
6462 C CB  . LEU B 282 ? 0.2675 0.2084 0.3107 -0.0247 0.1034  -0.0628 282 LEU B CB  
6463 C CG  . LEU B 282 ? 0.3120 0.2637 0.3475 -0.0328 0.1111  -0.0749 282 LEU B CG  
6464 C CD1 . LEU B 282 ? 0.3284 0.2979 0.3539 -0.0419 0.1086  -0.0710 282 LEU B CD1 
6465 C CD2 . LEU B 282 ? 0.3018 0.2410 0.3221 -0.0401 0.1100  -0.0792 282 LEU B CD2 
6466 N N   . LYS B 283 ? 0.2752 0.2184 0.3702 -0.0016 0.1136  -0.0673 283 LYS B N   
6467 C CA  . LYS B 283 ? 0.2639 0.2096 0.3838 0.0075  0.1232  -0.0766 283 LYS B CA  
6468 C C   . LYS B 283 ? 0.2764 0.2381 0.4211 0.0144  0.1226  -0.0689 283 LYS B C   
6469 O O   . LYS B 283 ? 0.2994 0.2734 0.4651 0.0196  0.1328  -0.0774 283 LYS B O   
6470 C CB  . LYS B 283 ? 0.2801 0.2046 0.4081 0.0142  0.1221  -0.0776 283 LYS B CB  
6471 C CG  . LYS B 283 ? 0.4397 0.3522 0.5438 0.0061  0.1189  -0.0813 283 LYS B CG  
6472 C CD  . LYS B 283 ? 0.5747 0.4909 0.6756 0.0023  0.1260  -0.0942 283 LYS B CD  
6473 C CE  . LYS B 283 ? 0.6010 0.5049 0.6832 -0.0046 0.1220  -0.0958 283 LYS B CE  
6474 N NZ  . LYS B 283 ? 0.5057 0.4104 0.5653 -0.0157 0.1202  -0.0953 283 LYS B NZ  
6475 N N   . ASN B 284 ? 0.2429 0.2049 0.3862 0.0140  0.1110  -0.0526 284 ASN B N   
6476 C CA  . ASN B 284 ? 0.2511 0.2297 0.4167 0.0184  0.1082  -0.0428 284 ASN B CA  
6477 C C   . ASN B 284 ? 0.2986 0.3003 0.4603 0.0123  0.1121  -0.0448 284 ASN B C   
6478 O O   . ASN B 284 ? 0.3119 0.3316 0.4968 0.0164  0.1133  -0.0399 284 ASN B O   
6479 C CB  . ASN B 284 ? 0.2208 0.1932 0.3811 0.0162  0.0941  -0.0246 284 ASN B CB  
6480 C CG  . ASN B 284 ? 0.3140 0.2677 0.4836 0.0220  0.0892  -0.0193 284 ASN B CG  
6481 O OD1 . ASN B 284 ? 0.2955 0.2440 0.4864 0.0306  0.0951  -0.0262 284 ASN B OD1 
6482 N ND2 . ASN B 284 ? 0.3034 0.2466 0.4573 0.0166  0.0784  -0.0069 284 ASN B ND2 
6483 N N   . SER B 285 ? 0.2975 0.3000 0.4317 0.0019  0.1132  -0.0504 285 SER B N   
6484 C CA  . SER B 285 ? 0.3404 0.3631 0.4654 -0.0066 0.1130  -0.0484 285 SER B CA  
6485 C C   . SER B 285 ? 0.4276 0.4643 0.5513 -0.0109 0.1261  -0.0640 285 SER B C   
6486 O O   . SER B 285 ? 0.3960 0.4551 0.5282 -0.0134 0.1303  -0.0641 285 SER B O   
6487 C CB  . SER B 285 ? 0.2975 0.3119 0.3921 -0.0172 0.1026  -0.0405 285 SER B CB  
6488 O OG  . SER B 285 ? 0.2793 0.2811 0.3726 -0.0150 0.0922  -0.0275 285 SER B OG  
6489 N N   . VAL B 286 ? 0.4368 0.4614 0.5482 -0.0136 0.1325  -0.0768 286 VAL B N   
6490 C CA  . VAL B 286 ? 0.4880 0.5242 0.5925 -0.0210 0.1449  -0.0922 286 VAL B CA  
6491 C C   . VAL B 286 ? 0.5145 0.5398 0.6315 -0.0140 0.1572  -0.1079 286 VAL B C   
6492 O O   . VAL B 286 ? 0.5090 0.5138 0.6307 -0.0069 0.1535  -0.1064 286 VAL B O   
6493 C CB  . VAL B 286 ? 0.5802 0.6140 0.6509 -0.0366 0.1399  -0.0927 286 VAL B CB  
6494 C CG1 . VAL B 286 ? 0.5727 0.6104 0.6308 -0.0425 0.1261  -0.0765 286 VAL B CG1 
6495 C CG2 . VAL B 286 ? 0.6034 0.6141 0.6606 -0.0380 0.1379  -0.0971 286 VAL B CG2 
6496 N N   . GLU B 287 ? 0.4659 0.5019 0.5823 -0.0180 0.1651  -0.1188 287 GLU B N   
6497 C CA  . GLU B 287 ? 0.5413 0.5662 0.6668 -0.0128 0.1712  -0.1296 287 GLU B CA  
6498 C C   . GLU B 287 ? 0.5563 0.5624 0.6569 -0.0217 0.1691  -0.1360 287 GLU B C   
6499 O O   . GLU B 287 ? 0.5555 0.5428 0.6613 -0.0154 0.1664  -0.1358 287 GLU B O   
6500 C CB  . GLU B 287 ? 0.5001 0.5429 0.6331 -0.0149 0.1819  -0.1395 287 GLU B CB  
6501 C CG  . GLU B 287 ? 0.5741 0.6355 0.7374 -0.0045 0.1843  -0.1329 287 GLU B CG  
6502 C CD  . GLU B 287 ? 0.6785 0.7566 0.8521 -0.0051 0.1958  -0.1429 287 GLU B CD  
6503 O OE1 . GLU B 287 ? 0.6874 0.7634 0.8406 -0.0158 0.2022  -0.1553 287 GLU B OE1 
6504 O OE2 . GLU B 287 ? 0.7504 0.8438 0.9537 0.0049  0.1985  -0.1377 287 GLU B OE2 
6505 N N   . ARG B 288 ? 0.5338 0.5457 0.6077 -0.0374 0.1694  -0.1404 288 ARG B N   
6506 C CA  . ARG B 288 ? 0.6089 0.6061 0.6594 -0.0483 0.1670  -0.1452 288 ARG B CA  
6507 C C   . ARG B 288 ? 0.5978 0.5843 0.6357 -0.0503 0.1563  -0.1342 288 ARG B C   
6508 O O   . ARG B 288 ? 0.6860 0.6773 0.7028 -0.0627 0.1514  -0.1302 288 ARG B O   
6509 C CB  . ARG B 288 ? 0.6588 0.6676 0.6883 -0.0655 0.1716  -0.1538 288 ARG B CB  
6510 C CG  . ARG B 288 ? 0.6458 0.6622 0.6890 -0.0627 0.1840  -0.1663 288 ARG B CG  
6511 C CD  . ARG B 288 ? 0.6375 0.6602 0.6591 -0.0808 0.1900  -0.1772 288 ARG B CD  
6512 N NE  . ARG B 288 ? 0.7085 0.7527 0.7203 -0.0910 0.1894  -0.1749 288 ARG B NE  
6513 C CZ  . ARG B 288 ? 0.6614 0.7228 0.6844 -0.0896 0.1987  -0.1810 288 ARG B CZ  
6514 N NH1 . ARG B 288 ? 0.6570 0.7375 0.6687 -0.1003 0.1961  -0.1771 288 ARG B NH1 
6515 N NH2 . ARG B 288 ? 0.4841 0.5435 0.5299 -0.0780 0.2102  -0.1906 288 ARG B NH2 
6516 N N   . ALA B 289 ? 0.4397 0.4112 0.4917 -0.0379 0.1521  -0.1283 289 ALA B N   
6517 C CA  . ALA B 289 ? 0.5151 0.4759 0.5609 -0.0363 0.1430  -0.1172 289 ALA B CA  
6518 C C   . ALA B 289 ? 0.4868 0.4315 0.5136 -0.0445 0.1377  -0.1175 289 ALA B C   
6519 O O   . ALA B 289 ? 0.5800 0.5090 0.6124 -0.0382 0.1333  -0.1140 289 ALA B O   
6520 C CB  . ALA B 289 ? 0.5354 0.4883 0.6048 -0.0208 0.1400  -0.1095 289 ALA B CB  
6521 N N   . SER B 290 ? 0.3541 0.3043 0.3581 -0.0600 0.1372  -0.1203 290 SER B N   
6522 C CA  . SER B 290 ? 0.3772 0.3135 0.3637 -0.0691 0.1307  -0.1182 290 SER B CA  
6523 C C   . SER B 290 ? 0.3063 0.2401 0.2893 -0.0689 0.1173  -0.1014 290 SER B C   
6524 O O   . SER B 290 ? 0.2706 0.2174 0.2472 -0.0749 0.1125  -0.0944 290 SER B O   
6525 C CB  . SER B 290 ? 0.3601 0.3035 0.3247 -0.0876 0.1324  -0.1249 290 SER B CB  
6526 O OG  . SER B 290 ? 0.3709 0.3027 0.3204 -0.0972 0.1231  -0.1190 290 SER B OG  
6527 N N   . PRO B 291 ? 0.3117 0.2294 0.2989 -0.0629 0.1110  -0.0944 291 PRO B N   
6528 C CA  . PRO B 291 ? 0.3121 0.2270 0.2968 -0.0630 0.0997  -0.0795 291 PRO B CA  
6529 C C   . PRO B 291 ? 0.2905 0.2057 0.2601 -0.0768 0.0920  -0.0742 291 PRO B C   
6530 O O   . PRO B 291 ? 0.2912 0.2018 0.2615 -0.0764 0.0836  -0.0627 291 PRO B O   
6531 C CB  . PRO B 291 ? 0.3172 0.2154 0.3128 -0.0521 0.0982  -0.0759 291 PRO B CB  
6532 C CG  . PRO B 291 ? 0.2978 0.1877 0.2936 -0.0529 0.1043  -0.0870 291 PRO B CG  
6533 C CD  . PRO B 291 ? 0.3082 0.2100 0.3034 -0.0559 0.1142  -0.0996 291 PRO B CD  
6534 N N   . TYR B 292 ? 0.2678 0.1881 0.2245 -0.0898 0.0946  -0.0819 292 TYR B N   
6535 C CA  . TYR B 292 ? 0.2723 0.1923 0.2163 -0.1043 0.0855  -0.0751 292 TYR B CA  
6536 C C   . TYR B 292 ? 0.2746 0.2104 0.2070 -0.1173 0.0807  -0.0704 292 TYR B C   
6537 O O   . TYR B 292 ? 0.2825 0.2206 0.2034 -0.1323 0.0730  -0.0651 292 TYR B O   
6538 C CB  . TYR B 292 ? 0.2902 0.2030 0.2244 -0.1134 0.0890  -0.0845 292 TYR B CB  
6539 C CG  . TYR B 292 ? 0.3536 0.2501 0.2996 -0.1008 0.0930  -0.0884 292 TYR B CG  
6540 C CD1 . TYR B 292 ? 0.3700 0.2569 0.3269 -0.0922 0.0861  -0.0771 292 TYR B CD1 
6541 C CD2 . TYR B 292 ? 0.3549 0.2472 0.3026 -0.0969 0.1035  -0.1020 292 TYR B CD2 
6542 C CE1 . TYR B 292 ? 0.3885 0.2658 0.3561 -0.0798 0.0876  -0.0772 292 TYR B CE1 
6543 C CE2 . TYR B 292 ? 0.4017 0.2839 0.3628 -0.0836 0.1037  -0.1003 292 TYR B CE2 
6544 C CZ  . TYR B 292 ? 0.4129 0.2880 0.3824 -0.0760 0.0954  -0.0879 292 TYR B CZ  
6545 O OH  . TYR B 292 ? 0.4237 0.2913 0.4045 -0.0647 0.0943  -0.0853 292 TYR B OH  
6546 N N   . LEU B 293 ? 0.2685 0.2155 0.2045 -0.1128 0.0838  -0.0706 293 LEU B N   
6547 C CA  . LEU B 293 ? 0.2847 0.2473 0.2104 -0.1248 0.0791  -0.0655 293 LEU B CA  
6548 C C   . LEU B 293 ? 0.2747 0.2360 0.2075 -0.1191 0.0698  -0.0514 293 LEU B C   
6549 O O   . LEU B 293 ? 0.2616 0.2134 0.2069 -0.1048 0.0705  -0.0486 293 LEU B O   
6550 C CB  . LEU B 293 ? 0.3105 0.2886 0.2346 -0.1256 0.0905  -0.0769 293 LEU B CB  
6551 C CG  . LEU B 293 ? 0.4745 0.4591 0.3859 -0.1375 0.1008  -0.0922 293 LEU B CG  
6552 C CD1 . LEU B 293 ? 0.5232 0.4923 0.4396 -0.1304 0.1088  -0.1033 293 LEU B CD1 
6553 C CD2 . LEU B 293 ? 0.5350 0.5381 0.4482 -0.1378 0.1122  -0.1016 293 LEU B CD2 
6554 N N   . ARG B 294 ? 0.2807 0.2509 0.2045 -0.1315 0.0610  -0.0426 294 ARG B N   
6555 C CA  . ARG B 294 ? 0.2634 0.2345 0.1919 -0.1275 0.0542  -0.0318 294 ARG B CA  
6556 C C   . ARG B 294 ? 0.2527 0.2393 0.1798 -0.1266 0.0608  -0.0369 294 ARG B C   
6557 O O   . ARG B 294 ? 0.2957 0.2977 0.2122 -0.1390 0.0635  -0.0417 294 ARG B O   
6558 C CB  . ARG B 294 ? 0.2487 0.2217 0.1714 -0.1369 0.0398  -0.0188 294 ARG B CB  
6559 C CG  . ARG B 294 ? 0.2619 0.2334 0.1897 -0.1311 0.0327  -0.0087 294 ARG B CG  
6560 C CD  . ARG B 294 ? 0.2574 0.2275 0.1865 -0.1328 0.0180  0.0041  294 ARG B CD  
6561 N NE  . ARG B 294 ? 0.2954 0.2787 0.2107 -0.1460 0.0116  0.0061  294 ARG B NE  
6562 C CZ  . ARG B 294 ? 0.3129 0.2961 0.2266 -0.1512 0.0030  0.0122  294 ARG B CZ  
6563 N NH1 . ARG B 294 ? 0.2995 0.2716 0.2275 -0.1439 0.0000  0.0166  294 ARG B NH1 
6564 N NH2 . ARG B 294 ? 0.3741 0.3693 0.2717 -0.1643 -0.0027 0.0143  294 ARG B NH2 
6565 N N   . TYR B 295 ? 0.2377 0.2214 0.1757 -0.1132 0.0635  -0.0357 295 TYR B N   
6566 C CA  . TYR B 295 ? 0.2352 0.2347 0.1752 -0.1120 0.0687  -0.0386 295 TYR B CA  
6567 C C   . TYR B 295 ? 0.2499 0.2534 0.1854 -0.1170 0.0591  -0.0267 295 TYR B C   
6568 O O   . TYR B 295 ? 0.2297 0.2192 0.1656 -0.1151 0.0508  -0.0174 295 TYR B O   
6569 C CB  . TYR B 295 ? 0.2287 0.2249 0.1845 -0.0959 0.0766  -0.0433 295 TYR B CB  
6570 C CG  . TYR B 295 ? 0.2354 0.2295 0.1978 -0.0908 0.0875  -0.0565 295 TYR B CG  
6571 C CD1 . TYR B 295 ? 0.2355 0.2119 0.2002 -0.0857 0.0874  -0.0585 295 TYR B CD1 
6572 C CD2 . TYR B 295 ? 0.2995 0.3091 0.2661 -0.0917 0.0985  -0.0675 295 TYR B CD2 
6573 C CE1 . TYR B 295 ? 0.2750 0.2478 0.2450 -0.0818 0.0972  -0.0709 295 TYR B CE1 
6574 C CE2 . TYR B 295 ? 0.2828 0.2888 0.2560 -0.0871 0.1094  -0.0806 295 TYR B CE2 
6575 C CZ  . TYR B 295 ? 0.2799 0.2666 0.2540 -0.0824 0.1083  -0.0824 295 TYR B CZ  
6576 O OH  . TYR B 295 ? 0.2665 0.2486 0.2467 -0.0786 0.1195  -0.0963 295 TYR B OH  
6577 N N   . TYR B 296 ? 0.2374 0.2601 0.1689 -0.1239 0.0610  -0.0274 296 TYR B N   
6578 C CA  . TYR B 296 ? 0.2620 0.2893 0.1893 -0.1287 0.0524  -0.0165 296 TYR B CA  
6579 C C   . TYR B 296 ? 0.2265 0.2642 0.1640 -0.1202 0.0581  -0.0178 296 TYR B C   
6580 O O   . TYR B 296 ? 0.2405 0.2976 0.1816 -0.1223 0.0666  -0.0248 296 TYR B O   
6581 C CB  . TYR B 296 ? 0.2678 0.3088 0.1814 -0.1436 0.0452  -0.0135 296 TYR B CB  
6582 C CG  . TYR B 296 ? 0.2659 0.2985 0.1706 -0.1505 0.0368  -0.0110 296 TYR B CG  
6583 C CD1 . TYR B 296 ? 0.2823 0.2963 0.1906 -0.1452 0.0271  -0.0020 296 TYR B CD1 
6584 C CD2 . TYR B 296 ? 0.3156 0.3596 0.2089 -0.1619 0.0383  -0.0174 296 TYR B CD2 
6585 C CE1 . TYR B 296 ? 0.2572 0.2659 0.1612 -0.1497 0.0188  0.0021  296 TYR B CE1 
6586 C CE2 . TYR B 296 ? 0.3083 0.3456 0.1926 -0.1686 0.0292  -0.0131 296 TYR B CE2 
6587 C CZ  . TYR B 296 ? 0.3196 0.3401 0.2110 -0.1616 0.0192  -0.0024 296 TYR B CZ  
6588 O OH  . TYR B 296 ? 0.3624 0.3783 0.2491 -0.1664 0.0100  0.0037  296 TYR B OH  
6589 N N   . PHE B 297 ? 0.2236 0.2488 0.1663 -0.1114 0.0539  -0.0109 297 PHE B N   
6590 C CA  . PHE B 297 ? 0.2154 0.2504 0.1678 -0.1052 0.0567  -0.0090 297 PHE B CA  
6591 C C   . PHE B 297 ? 0.2249 0.2758 0.1693 -0.1165 0.0509  -0.0018 297 PHE B C   
6592 O O   . PHE B 297 ? 0.2559 0.2970 0.1898 -0.1225 0.0408  0.0075  297 PHE B O   
6593 C CB  . PHE B 297 ? 0.2332 0.2496 0.1902 -0.0952 0.0532  -0.0034 297 PHE B CB  
6594 C CG  . PHE B 297 ? 0.2401 0.2661 0.2060 -0.0911 0.0532  0.0015  297 PHE B CG  
6595 C CD1 . PHE B 297 ? 0.2057 0.2421 0.1898 -0.0820 0.0613  -0.0036 297 PHE B CD1 
6596 C CD2 . PHE B 297 ? 0.2313 0.2558 0.1883 -0.0972 0.0446  0.0118  297 PHE B CD2 
6597 C CE1 . PHE B 297 ? 0.2040 0.2507 0.1995 -0.0788 0.0599  0.0031  297 PHE B CE1 
6598 C CE2 . PHE B 297 ? 0.2199 0.2539 0.1847 -0.0952 0.0432  0.0179  297 PHE B CE2 
6599 C CZ  . PHE B 297 ? 0.2759 0.3218 0.2609 -0.0860 0.0504  0.0143  297 PHE B CZ  
6600 N N   . ARG B 298 ? 0.2213 0.2965 0.1713 -0.1198 0.0580  -0.0066 298 ARG B N   
6601 C CA  . ARG B 298 ? 0.2249 0.3188 0.1694 -0.1300 0.0534  -0.0004 298 ARG B CA  
6602 C C   . ARG B 298 ? 0.2820 0.3694 0.2086 -0.1397 0.0405  0.0038  298 ARG B C   
6603 O O   . ARG B 298 ? 0.2781 0.3686 0.1977 -0.1447 0.0301  0.0117  298 ARG B O   
6604 C CB  . ARG B 298 ? 0.2758 0.3697 0.2251 -0.1272 0.0479  0.0102  298 ARG B CB  
6605 C CG  . ARG B 298 ? 0.2337 0.3362 0.2053 -0.1141 0.0563  0.0068  298 ARG B CG  
6606 C CD  . ARG B 298 ? 0.2302 0.3334 0.2070 -0.1120 0.0493  0.0184  298 ARG B CD  
6607 N NE  . ARG B 298 ? 0.2264 0.3363 0.2274 -0.0993 0.0563  0.0161  298 ARG B NE  
6608 C CZ  . ARG B 298 ? 0.2719 0.3810 0.2821 -0.0951 0.0510  0.0259  298 ARG B CZ  
6609 N NH1 . ARG B 298 ? 0.2663 0.3674 0.2611 -0.1033 0.0396  0.0373  298 ARG B NH1 
6610 N NH2 . ARG B 298 ? 0.2271 0.3423 0.2621 -0.0836 0.0568  0.0244  298 ARG B NH2 
6611 N N   . GLU B 299 ? 0.2586 0.3375 0.1787 -0.1427 0.0409  -0.0012 299 GLU B N   
6612 C CA  . GLU B 299 ? 0.3116 0.3848 0.2174 -0.1519 0.0286  0.0033  299 GLU B CA  
6613 C C   . GLU B 299 ? 0.3336 0.3884 0.2358 -0.1496 0.0156  0.0145  299 GLU B C   
6614 O O   . GLU B 299 ? 0.3291 0.3828 0.2214 -0.1565 0.0040  0.0206  299 GLU B O   
6615 C CB  . GLU B 299 ? 0.3048 0.3989 0.2019 -0.1632 0.0256  0.0021  299 GLU B CB  
6616 C CG  . GLU B 299 ? 0.5197 0.6290 0.4154 -0.1688 0.0365  -0.0104 299 GLU B CG  
6617 C CD  . GLU B 299 ? 0.6247 0.7241 0.5105 -0.1749 0.0346  -0.0140 299 GLU B CD  
6618 O OE1 . GLU B 299 ? 0.5318 0.6129 0.4146 -0.1730 0.0255  -0.0062 299 GLU B OE1 
6619 O OE2 . GLU B 299 ? 0.6567 0.7672 0.5374 -0.1824 0.0419  -0.0246 299 GLU B OE2 
6620 N N   . LEU B 300 ? 0.2752 0.3148 0.1847 -0.1401 0.0176  0.0168  300 LEU B N   
6621 C CA  . LEU B 300 ? 0.2471 0.2687 0.1537 -0.1368 0.0077  0.0250  300 LEU B CA  
6622 C C   . LEU B 300 ? 0.3125 0.3108 0.2238 -0.1287 0.0083  0.0250  300 LEU B C   
6623 O O   . LEU B 300 ? 0.3651 0.3495 0.2749 -0.1272 0.0002  0.0300  300 LEU B O   
6624 C CB  . LEU B 300 ? 0.3152 0.3394 0.2238 -0.1339 0.0081  0.0283  300 LEU B CB  
6625 C CG  . LEU B 300 ? 0.4103 0.4555 0.3150 -0.1415 0.0041  0.0311  300 LEU B CG  
6626 C CD1 . LEU B 300 ? 0.4813 0.5290 0.3898 -0.1384 0.0043  0.0353  300 LEU B CD1 
6627 C CD2 . LEU B 300 ? 0.3861 0.4280 0.2798 -0.1489 -0.0090 0.0364  300 LEU B CD2 
6628 N N   . ILE B 301 ? 0.2598 0.2538 0.1784 -0.1231 0.0182  0.0192  301 ILE B N   
6629 C CA  . ILE B 301 ? 0.2293 0.2020 0.1532 -0.1151 0.0192  0.0188  301 ILE B CA  
6630 C C   . ILE B 301 ? 0.2560 0.2301 0.1849 -0.1144 0.0274  0.0115  301 ILE B C   
6631 O O   . ILE B 301 ? 0.2807 0.2674 0.2127 -0.1139 0.0363  0.0047  301 ILE B O   
6632 C CB  . ILE B 301 ? 0.3070 0.2661 0.2328 -0.1072 0.0217  0.0200  301 ILE B CB  
6633 C CG1 . ILE B 301 ? 0.2578 0.1964 0.1895 -0.0982 0.0237  0.0184  301 ILE B CG1 
6634 C CG2 . ILE B 301 ? 0.2923 0.2622 0.2216 -0.1063 0.0302  0.0172  301 ILE B CG2 
6635 C CD1 . ILE B 301 ? 0.2979 0.2232 0.2283 -0.0916 0.0249  0.0194  301 ILE B CD1 
6636 N N   . SER B 302 ? 0.2285 0.1917 0.1605 -0.1124 0.0240  0.0123  302 SER B N   
6637 C CA  . SER B 302 ? 0.2194 0.1816 0.1552 -0.1121 0.0304  0.0056  302 SER B CA  
6638 C C   . SER B 302 ? 0.2344 0.1834 0.1782 -0.1004 0.0383  0.0011  302 SER B C   
6639 O O   . SER B 302 ? 0.2316 0.1660 0.1779 -0.0942 0.0368  0.0051  302 SER B O   
6640 C CB  . SER B 302 ? 0.2611 0.2178 0.1992 -0.1133 0.0222  0.0101  302 SER B CB  
6641 O OG  . SER B 302 ? 0.3060 0.2757 0.2359 -0.1234 0.0142  0.0140  302 SER B OG  
6642 N N   . VAL B 303 ? 0.2200 0.1746 0.1682 -0.0957 0.0463  -0.0078 303 VAL B N   
6643 C CA  . VAL B 303 ? 0.2389 0.1834 0.1960 -0.0832 0.0525  -0.0121 303 VAL B CA  
6644 C C   . VAL B 303 ? 0.2159 0.1571 0.1765 -0.0818 0.0569  -0.0191 303 VAL B C   
6645 O O   . VAL B 303 ? 0.2197 0.1724 0.1775 -0.0871 0.0608  -0.0261 303 VAL B O   
6646 C CB  . VAL B 303 ? 0.2517 0.2065 0.2140 -0.0774 0.0578  -0.0152 303 VAL B CB  
6647 C CG1 . VAL B 303 ? 0.2255 0.1691 0.1976 -0.0657 0.0624  -0.0176 303 VAL B CG1 
6648 C CG2 . VAL B 303 ? 0.2378 0.1969 0.1949 -0.0809 0.0525  -0.0073 303 VAL B CG2 
6649 N N   . PHE B 304 ? 0.2079 0.1332 0.1736 -0.0759 0.0567  -0.0178 304 PHE B N   
6650 C CA  . PHE B 304 ? 0.2101 0.1306 0.1799 -0.0735 0.0609  -0.0241 304 PHE B CA  
6651 C C   . PHE B 304 ? 0.2670 0.1798 0.2452 -0.0617 0.0667  -0.0276 304 PHE B C   
6652 O O   . PHE B 304 ? 0.2299 0.1352 0.2101 -0.0564 0.0655  -0.0226 304 PHE B O   
6653 C CB  . PHE B 304 ? 0.2103 0.1201 0.1819 -0.0764 0.0559  -0.0190 304 PHE B CB  
6654 C CG  . PHE B 304 ? 0.2364 0.1535 0.2019 -0.0892 0.0486  -0.0143 304 PHE B CG  
6655 C CD1 . PHE B 304 ? 0.2843 0.2086 0.2438 -0.0984 0.0490  -0.0190 304 PHE B CD1 
6656 C CD2 . PHE B 304 ? 0.2382 0.1571 0.2049 -0.0897 0.0396  -0.0046 304 PHE B CD2 
6657 C CE1 . PHE B 304 ? 0.2566 0.1901 0.2100 -0.1092 0.0396  -0.0128 304 PHE B CE1 
6658 C CE2 . PHE B 304 ? 0.3043 0.2319 0.2683 -0.0988 0.0303  0.0016  304 PHE B CE2 
6659 C CZ  . PHE B 304 ? 0.2351 0.1706 0.1921 -0.1085 0.0297  -0.0018 304 PHE B CZ  
6660 N N   . PHE B 305 ? 0.2494 0.1629 0.2319 -0.0588 0.0726  -0.0361 305 PHE B N   
6661 C CA  . PHE B 305 ? 0.2592 0.1644 0.2515 -0.0483 0.0770  -0.0386 305 PHE B CA  
6662 C C   . PHE B 305 ? 0.2392 0.1310 0.2334 -0.0469 0.0771  -0.0398 305 PHE B C   
6663 O O   . PHE B 305 ? 0.2291 0.1218 0.2196 -0.0529 0.0779  -0.0447 305 PHE B O   
6664 C CB  . PHE B 305 ? 0.2144 0.1293 0.2141 -0.0445 0.0840  -0.0470 305 PHE B CB  
6665 C CG  . PHE B 305 ? 0.2120 0.1418 0.2133 -0.0449 0.0840  -0.0446 305 PHE B CG  
6666 C CD1 . PHE B 305 ? 0.2984 0.2429 0.2912 -0.0543 0.0836  -0.0458 305 PHE B CD1 
6667 C CD2 . PHE B 305 ? 0.2416 0.1710 0.2523 -0.0374 0.0832  -0.0393 305 PHE B CD2 
6668 C CE1 . PHE B 305 ? 0.3029 0.2622 0.2978 -0.0551 0.0833  -0.0426 305 PHE B CE1 
6669 C CE2 . PHE B 305 ? 0.2428 0.1866 0.2561 -0.0384 0.0822  -0.0356 305 PHE B CE2 
6670 C CZ  . PHE B 305 ? 0.2966 0.2553 0.3023 -0.0468 0.0826  -0.0374 305 PHE B CZ  
6671 N N   . ARG B 306 ? 0.2360 0.1163 0.2346 -0.0406 0.0760  -0.0348 306 ARG B N   
6672 C CA  . ARG B 306 ? 0.2061 0.0849 0.2070 -0.0374 0.0726  -0.0328 306 ARG B CA  
6673 C C   . ARG B 306 ? 0.2126 0.0894 0.2185 -0.0346 0.0768  -0.0401 306 ARG B C   
6674 O O   . ARG B 306 ? 0.2367 0.1139 0.2486 -0.0305 0.0816  -0.0450 306 ARG B O   
6675 C CB  . ARG B 306 ? 0.2806 0.1589 0.2836 -0.0308 0.0679  -0.0248 306 ARG B CB  
6676 C CG  . ARG B 306 ? 0.4221 0.2985 0.4286 -0.0249 0.0689  -0.0233 306 ARG B CG  
6677 C CD  . ARG B 306 ? 0.5460 0.4207 0.5578 -0.0205 0.0677  -0.0233 306 ARG B CD  
6678 N NE  . ARG B 306 ? 0.5164 0.3884 0.5310 -0.0164 0.0666  -0.0198 306 ARG B NE  
6679 C CZ  . ARG B 306 ? 0.4042 0.2747 0.4167 -0.0154 0.0632  -0.0150 306 ARG B CZ  
6680 N NH1 . ARG B 306 ? 0.2940 0.1663 0.3036 -0.0165 0.0615  -0.0133 306 ARG B NH1 
6681 N NH2 . ARG B 306 ? 0.4201 0.2864 0.4349 -0.0136 0.0620  -0.0119 306 ARG B NH2 
6682 N N   . ASP B 307 ? 0.2154 0.0906 0.2201 -0.0369 0.0747  -0.0406 307 ASP B N   
6683 C CA  . ASP B 307 ? 0.2226 0.0947 0.2312 -0.0341 0.0770  -0.0460 307 ASP B CA  
6684 C C   . ASP B 307 ? 0.2171 0.0876 0.2326 -0.0256 0.0733  -0.0396 307 ASP B C   
6685 O O   . ASP B 307 ? 0.2124 0.0824 0.2272 -0.0249 0.0684  -0.0335 307 ASP B O   
6686 C CB  . ASP B 307 ? 0.3238 0.1933 0.3266 -0.0416 0.0753  -0.0481 307 ASP B CB  
6687 C CG  . ASP B 307 ? 0.3421 0.2070 0.3468 -0.0401 0.0778  -0.0546 307 ASP B CG  
6688 O OD1 . ASP B 307 ? 0.3596 0.2225 0.3724 -0.0317 0.0768  -0.0525 307 ASP B OD1 
6689 O OD2 . ASP B 307 ? 0.3777 0.2409 0.3748 -0.0487 0.0805  -0.0620 307 ASP B OD2 
6690 N N   . LYS B 308 ? 0.2191 0.0893 0.2418 -0.0198 0.0755  -0.0411 308 LYS B N   
6691 C CA  . LYS B 308 ? 0.2341 0.1021 0.2614 -0.0141 0.0712  -0.0344 308 LYS B CA  
6692 C C   . LYS B 308 ? 0.2531 0.1170 0.2812 -0.0133 0.0678  -0.0335 308 LYS B C   
6693 O O   . LYS B 308 ? 0.2383 0.1014 0.2650 -0.0125 0.0633  -0.0272 308 LYS B O   
6694 C CB  . LYS B 308 ? 0.2590 0.1264 0.2964 -0.0090 0.0737  -0.0356 308 LYS B CB  
6695 C CG  . LYS B 308 ? 0.2854 0.1483 0.3275 -0.0048 0.0687  -0.0288 308 LYS B CG  
6696 C CD  . LYS B 308 ? 0.3384 0.2003 0.3939 0.0001  0.0703  -0.0279 308 LYS B CD  
6697 C CE  . LYS B 308 ? 0.3287 0.1842 0.3903 0.0030  0.0646  -0.0212 308 LYS B CE  
6698 N NZ  . LYS B 308 ? 0.3294 0.1825 0.3792 -0.0010 0.0594  -0.0131 308 LYS B NZ  
6699 N N   . THR B 309 ? 0.2517 0.1124 0.2813 -0.0144 0.0702  -0.0404 309 THR B N   
6700 C CA  . THR B 309 ? 0.2766 0.1315 0.3065 -0.0142 0.0668  -0.0397 309 THR B CA  
6701 C C   . THR B 309 ? 0.3008 0.1566 0.3248 -0.0184 0.0630  -0.0348 309 THR B C   
6702 O O   . THR B 309 ? 0.2765 0.1305 0.3013 -0.0171 0.0588  -0.0295 309 THR B O   
6703 C CB  . THR B 309 ? 0.3293 0.1795 0.3601 -0.0157 0.0709  -0.0490 309 THR B CB  
6704 O OG1 . THR B 309 ? 0.3047 0.1548 0.3451 -0.0102 0.0747  -0.0534 309 THR B OG1 
6705 C CG2 . THR B 309 ? 0.3561 0.1984 0.3861 -0.0163 0.0668  -0.0481 309 THR B CG2 
6706 N N   . LEU B 310 ? 0.2279 0.0863 0.2467 -0.0241 0.0644  -0.0364 310 LEU B N   
6707 C CA  . LEU B 310 ? 0.2234 0.0831 0.2403 -0.0278 0.0603  -0.0309 310 LEU B CA  
6708 C C   . LEU B 310 ? 0.2292 0.0936 0.2482 -0.0240 0.0580  -0.0236 310 LEU B C   
6709 O O   . LEU B 310 ? 0.2230 0.0877 0.2439 -0.0239 0.0553  -0.0191 310 LEU B O   
6710 C CB  . LEU B 310 ? 0.2643 0.1256 0.2764 -0.0355 0.0608  -0.0326 310 LEU B CB  
6711 C CG  . LEU B 310 ? 0.2629 0.1193 0.2689 -0.0432 0.0634  -0.0406 310 LEU B CG  
6712 C CD1 . LEU B 310 ? 0.2902 0.1498 0.2896 -0.0533 0.0624  -0.0407 310 LEU B CD1 
6713 C CD2 . LEU B 310 ? 0.2970 0.1474 0.3032 -0.0456 0.0599  -0.0397 310 LEU B CD2 
6714 N N   . SER B 311 ? 0.2074 0.0754 0.2256 -0.0218 0.0598  -0.0230 311 SER B N   
6715 C CA  . SER B 311 ? 0.2004 0.0715 0.2183 -0.0196 0.0585  -0.0176 311 SER B CA  
6716 C C   . SER B 311 ? 0.2140 0.0821 0.2332 -0.0168 0.0570  -0.0151 311 SER B C   
6717 O O   . SER B 311 ? 0.2007 0.0697 0.2198 -0.0171 0.0564  -0.0116 311 SER B O   
6718 C CB  . SER B 311 ? 0.1975 0.0708 0.2127 -0.0190 0.0603  -0.0177 311 SER B CB  
6719 O OG  . SER B 311 ? 0.2348 0.1101 0.2480 -0.0229 0.0610  -0.0194 311 SER B OG  
6720 N N   . ASP B 312 ? 0.2119 0.0756 0.2333 -0.0146 0.0569  -0.0172 312 ASP B N   
6721 C CA  . ASP B 312 ? 0.2408 0.0998 0.2635 -0.0129 0.0543  -0.0140 312 ASP B CA  
6722 C C   . ASP B 312 ? 0.2395 0.0949 0.2632 -0.0143 0.0520  -0.0134 312 ASP B C   
6723 O O   . ASP B 312 ? 0.2208 0.0728 0.2442 -0.0146 0.0499  -0.0096 312 ASP B O   
6724 C CB  . ASP B 312 ? 0.2216 0.0759 0.2493 -0.0097 0.0540  -0.0154 312 ASP B CB  
6725 C CG  . ASP B 312 ? 0.3254 0.1812 0.3532 -0.0087 0.0551  -0.0134 312 ASP B CG  
6726 O OD1 . ASP B 312 ? 0.3330 0.1915 0.3545 -0.0109 0.0553  -0.0102 312 ASP B OD1 
6727 O OD2 . ASP B 312 ? 0.3617 0.2151 0.3968 -0.0057 0.0561  -0.0150 312 ASP B OD2 
6728 N N   . LEU B 313 ? 0.2244 0.0792 0.2487 -0.0162 0.0524  -0.0168 313 LEU B N   
6729 C CA  . LEU B 313 ? 0.2377 0.0887 0.2625 -0.0186 0.0499  -0.0155 313 LEU B CA  
6730 C C   . LEU B 313 ? 0.2185 0.0740 0.2435 -0.0202 0.0500  -0.0105 313 LEU B C   
6731 O O   . LEU B 313 ? 0.2220 0.0747 0.2476 -0.0212 0.0486  -0.0074 313 LEU B O   
6732 C CB  . LEU B 313 ? 0.2300 0.0786 0.2540 -0.0223 0.0502  -0.0198 313 LEU B CB  
6733 C CG  . LEU B 313 ? 0.2746 0.1161 0.2988 -0.0215 0.0514  -0.0266 313 LEU B CG  
6734 C CD1 . LEU B 313 ? 0.2668 0.1059 0.2872 -0.0276 0.0529  -0.0317 313 LEU B CD1 
6735 C CD2 . LEU B 313 ? 0.2938 0.1268 0.3201 -0.0198 0.0478  -0.0254 313 LEU B CD2 
6736 N N   . ILE B 314 ? 0.2111 0.0729 0.2362 -0.0209 0.0520  -0.0099 314 ILE B N   
6737 C CA  . ILE B 314 ? 0.2124 0.0781 0.2398 -0.0216 0.0536  -0.0062 314 ILE B CA  
6738 C C   . ILE B 314 ? 0.2140 0.0793 0.2388 -0.0200 0.0560  -0.0045 314 ILE B C   
6739 O O   . ILE B 314 ? 0.2102 0.0745 0.2362 -0.0212 0.0579  -0.0021 314 ILE B O   
6740 C CB  . ILE B 314 ? 0.2013 0.0724 0.2308 -0.0223 0.0547  -0.0059 314 ILE B CB  
6741 C CG1 . ILE B 314 ? 0.2043 0.0742 0.2357 -0.0263 0.0515  -0.0064 314 ILE B CG1 
6742 C CG2 . ILE B 314 ? 0.1987 0.0734 0.2330 -0.0218 0.0580  -0.0029 314 ILE B CG2 
6743 C CD1 . ILE B 314 ? 0.2233 0.0974 0.2569 -0.0281 0.0508  -0.0049 314 ILE B CD1 
6744 N N   . GLY B 315 ? 0.2062 0.0713 0.2270 -0.0184 0.0563  -0.0054 315 GLY B N   
6745 C CA  . GLY B 315 ? 0.2087 0.0719 0.2250 -0.0187 0.0583  -0.0034 315 GLY B CA  
6746 C C   . GLY B 315 ? 0.2606 0.1170 0.2758 -0.0200 0.0558  -0.0010 315 GLY B C   
6747 O O   . GLY B 315 ? 0.2741 0.1277 0.2852 -0.0225 0.0580  0.0015  315 GLY B O   
6748 N N   . PHE B 316 ? 0.2278 0.0801 0.2460 -0.0191 0.0515  -0.0016 316 PHE B N   
6749 C CA  . PHE B 316 ? 0.2399 0.0841 0.2579 -0.0202 0.0475  0.0016  316 PHE B CA  
6750 C C   . PHE B 316 ? 0.2870 0.1260 0.3079 -0.0213 0.0441  0.0020  316 PHE B C   
6751 O O   . PHE B 316 ? 0.3690 0.2012 0.3889 -0.0239 0.0408  0.0061  316 PHE B O   
6752 C CB  . PHE B 316 ? 0.3142 0.1543 0.3338 -0.0177 0.0445  0.0016  316 PHE B CB  
6753 C CG  . PHE B 316 ? 0.3438 0.1861 0.3595 -0.0183 0.0463  0.0032  316 PHE B CG  
6754 C CD1 . PHE B 316 ? 0.3962 0.2346 0.4063 -0.0227 0.0456  0.0084  316 PHE B CD1 
6755 C CD2 . PHE B 316 ? 0.2904 0.1379 0.3068 -0.0158 0.0488  -0.0001 316 PHE B CD2 
6756 C CE1 . PHE B 316 ? 0.4501 0.2892 0.4547 -0.0246 0.0470  0.0101  316 PHE B CE1 
6757 C CE2 . PHE B 316 ? 0.3913 0.2396 0.4032 -0.0170 0.0500  0.0018  316 PHE B CE2 
6758 C CZ  . PHE B 316 ? 0.4104 0.2542 0.4160 -0.0215 0.0490  0.0068  316 PHE B CZ  
6759 N N   A SER B 317 ? 0.2354 0.0761 0.2588 -0.0206 0.0442  -0.0015 317 SER B N   
6760 N N   B SER B 317 ? 0.2360 0.0766 0.2594 -0.0205 0.0441  -0.0016 317 SER B N   
6761 C CA  A SER B 317 ? 0.2446 0.0780 0.2696 -0.0222 0.0403  -0.0015 317 SER B CA  
6762 C CA  B SER B 317 ? 0.2445 0.0780 0.2695 -0.0220 0.0403  -0.0018 317 SER B CA  
6763 C C   A SER B 317 ? 0.2437 0.0794 0.2696 -0.0258 0.0411  -0.0001 317 SER B C   
6764 C C   B SER B 317 ? 0.2436 0.0793 0.2694 -0.0258 0.0411  -0.0001 317 SER B C   
6765 O O   A SER B 317 ? 0.2738 0.1038 0.2997 -0.0290 0.0383  0.0030  317 SER B O   
6766 O O   B SER B 317 ? 0.2719 0.1023 0.2977 -0.0289 0.0385  0.0033  317 SER B O   
6767 C CB  A SER B 317 ? 0.2566 0.0861 0.2833 -0.0197 0.0393  -0.0072 317 SER B CB  
6768 C CB  B SER B 317 ? 0.2482 0.0786 0.2749 -0.0198 0.0398  -0.0077 317 SER B CB  
6769 O OG  A SER B 317 ? 0.2993 0.1185 0.3267 -0.0209 0.0353  -0.0075 317 SER B OG  
6770 O OG  B SER B 317 ? 0.2491 0.0785 0.2776 -0.0158 0.0404  -0.0097 317 SER B OG  
6771 N N   . TYR B 318 ? 0.2356 0.0786 0.2630 -0.0261 0.0442  -0.0014 318 TYR B N   
6772 C CA  . TYR B 318 ? 0.2364 0.0809 0.2670 -0.0299 0.0441  0.0006  318 TYR B CA  
6773 C C   . TYR B 318 ? 0.2504 0.0970 0.2835 -0.0320 0.0469  0.0052  318 TYR B C   
6774 O O   . TYR B 318 ? 0.2525 0.0995 0.2897 -0.0356 0.0464  0.0079  318 TYR B O   
6775 C CB  . TYR B 318 ? 0.2291 0.0803 0.2622 -0.0303 0.0459  -0.0005 318 TYR B CB  
6776 C CG  . TYR B 318 ? 0.2483 0.0966 0.2790 -0.0315 0.0437  -0.0048 318 TYR B CG  
6777 C CD1 . TYR B 318 ? 0.2530 0.0922 0.2807 -0.0328 0.0408  -0.0081 318 TYR B CD1 
6778 C CD2 . TYR B 318 ? 0.2266 0.0799 0.2577 -0.0322 0.0449  -0.0060 318 TYR B CD2 
6779 C CE1 . TYR B 318 ? 0.2486 0.0844 0.2736 -0.0349 0.0410  -0.0137 318 TYR B CE1 
6780 C CE2 . TYR B 318 ? 0.3051 0.1553 0.3329 -0.0352 0.0440  -0.0104 318 TYR B CE2 
6781 C CZ  . TYR B 318 ? 0.2969 0.1385 0.3213 -0.0367 0.0429  -0.0149 318 TYR B CZ  
6782 O OH  . TYR B 318 ? 0.2838 0.1221 0.3040 -0.0407 0.0442  -0.0211 318 TYR B OH  
6783 N N   . HIS B 319 ? 0.2477 0.0952 0.2785 -0.0307 0.0503  0.0062  319 HIS B N   
6784 C CA  . HIS B 319 ? 0.2398 0.0881 0.2724 -0.0338 0.0548  0.0096  319 HIS B CA  
6785 C C   . HIS B 319 ? 0.3097 0.1516 0.3424 -0.0383 0.0503  0.0132  319 HIS B C   
6786 O O   . HIS B 319 ? 0.2532 0.0970 0.2900 -0.0419 0.0538  0.0162  319 HIS B O   
6787 C CB  . HIS B 319 ? 0.2531 0.0999 0.2798 -0.0338 0.0584  0.0099  319 HIS B CB  
6788 C CG  . HIS B 319 ? 0.2781 0.1167 0.2995 -0.0353 0.0517  0.0122  319 HIS B CG  
6789 N ND1 . HIS B 319 ? 0.2938 0.1299 0.3138 -0.0318 0.0469  0.0103  319 HIS B ND1 
6790 C CD2 . HIS B 319 ? 0.2786 0.1105 0.2973 -0.0402 0.0486  0.0169  319 HIS B CD2 
6791 C CE1 . HIS B 319 ? 0.3030 0.1307 0.3210 -0.0338 0.0411  0.0138  319 HIS B CE1 
6792 N NE2 . HIS B 319 ? 0.3324 0.1573 0.3491 -0.0394 0.0412  0.0183  319 HIS B NE2 
6793 N N   . ALA B 320 ? 0.2991 0.1328 0.3280 -0.0384 0.0430  0.0129  320 ALA B N   
6794 C CA  . ALA B 320 ? 0.3405 0.1659 0.3684 -0.0431 0.0376  0.0167  320 ALA B CA  
6795 C C   . ALA B 320 ? 0.3472 0.1701 0.3771 -0.0455 0.0340  0.0161  320 ALA B C   
6796 O O   . ALA B 320 ? 0.3364 0.1520 0.3649 -0.0505 0.0293  0.0195  320 ALA B O   
6797 C CB  . ALA B 320 ? 0.3736 0.1888 0.3973 -0.0423 0.0312  0.0172  320 ALA B CB  
6798 N N   . TRP B 321 ? 0.2647 0.0924 0.2967 -0.0435 0.0353  0.0125  321 TRP B N   
6799 C CA  . TRP B 321 ? 0.2700 0.0945 0.3025 -0.0476 0.0314  0.0122  321 TRP B CA  
6800 C C   . TRP B 321 ? 0.3313 0.1632 0.3700 -0.0520 0.0337  0.0170  321 TRP B C   
6801 O O   . TRP B 321 ? 0.2968 0.1380 0.3415 -0.0497 0.0400  0.0182  321 TRP B O   
6802 C CB  . TRP B 321 ? 0.3166 0.1415 0.3476 -0.0453 0.0312  0.0066  321 TRP B CB  
6803 C CG  . TRP B 321 ? 0.3154 0.1347 0.3428 -0.0405 0.0307  0.0010  321 TRP B CG  
6804 C CD1 . TRP B 321 ? 0.3576 0.1750 0.3840 -0.0362 0.0310  0.0009  321 TRP B CD1 
6805 C CD2 . TRP B 321 ? 0.2902 0.1048 0.3153 -0.0404 0.0301  -0.0054 321 TRP B CD2 
6806 N NE1 . TRP B 321 ? 0.3698 0.1822 0.3950 -0.0324 0.0306  -0.0047 321 TRP B NE1 
6807 C CE2 . TRP B 321 ? 0.3793 0.1901 0.4036 -0.0346 0.0310  -0.0094 321 TRP B CE2 
6808 C CE3 . TRP B 321 ? 0.2999 0.1129 0.3237 -0.0456 0.0292  -0.0081 321 TRP B CE3 
6809 C CZ2 . TRP B 321 ? 0.4296 0.2357 0.4528 -0.0329 0.0326  -0.0170 321 TRP B CZ2 
6810 C CZ3 . TRP B 321 ? 0.3900 0.1975 0.4106 -0.0450 0.0308  -0.0162 321 TRP B CZ3 
6811 C CH2 . TRP B 321 ? 0.4038 0.2082 0.4245 -0.0382 0.0333  -0.0210 321 TRP B CH2 
6812 N N   . ASN B 322 ? 0.3201 0.1473 0.3581 -0.0587 0.0287  0.0195  322 ASN B N   
6813 C CA  . ASN B 322 ? 0.2929 0.1276 0.3377 -0.0638 0.0296  0.0245  322 ASN B CA  
6814 C C   . ASN B 322 ? 0.3620 0.2030 0.4097 -0.0622 0.0306  0.0226  322 ASN B C   
6815 O O   . ASN B 322 ? 0.3857 0.2221 0.4274 -0.0610 0.0280  0.0176  322 ASN B O   
6816 C CB  . ASN B 322 ? 0.4818 0.3088 0.5223 -0.0734 0.0229  0.0283  322 ASN B CB  
6817 C CG  . ASN B 322 ? 0.6879 0.5203 0.7317 -0.0806 0.0216  0.0326  322 ASN B CG  
6818 O OD1 . ASN B 322 ? 0.7294 0.5594 0.7687 -0.0838 0.0177  0.0307  322 ASN B OD1 
6819 N ND2 . ASN B 322 ? 0.8215 0.6623 0.8746 -0.0838 0.0253  0.0386  322 ASN B ND2 
6820 N N   . ALA B 323 ? 0.3269 0.1964 0.3121 -0.1096 0.0558  -0.0601 323 ALA B N   
6821 C CA  . ALA B 323 ? 0.2916 0.1725 0.2696 -0.1108 0.0464  -0.0599 323 ALA B CA  
6822 C C   . ALA B 323 ? 0.3081 0.1906 0.2732 -0.1216 0.0471  -0.0685 323 ALA B C   
6823 O O   . ALA B 323 ? 0.3526 0.2369 0.3090 -0.1209 0.0465  -0.0705 323 ALA B O   
6824 C CB  . ALA B 323 ? 0.2944 0.1914 0.2784 -0.1116 0.0331  -0.0528 323 ALA B CB  
6825 N N   . GLU B 324 ? 0.3289 0.2108 0.2923 -0.1320 0.0489  -0.0735 324 GLU B N   
6826 C CA  . GLU B 324 ? 0.3524 0.2356 0.3028 -0.1433 0.0501  -0.0817 324 GLU B CA  
6827 C C   . GLU B 324 ? 0.3693 0.2383 0.3124 -0.1420 0.0634  -0.0887 324 GLU B C   
6828 O O   . GLU B 324 ? 0.3765 0.2482 0.3085 -0.1457 0.0633  -0.0925 324 GLU B O   
6829 C CB  . GLU B 324 ? 0.4745 0.3590 0.4256 -0.1546 0.0502  -0.0856 324 GLU B CB  
6830 C CG  . GLU B 324 ? 0.7037 0.5884 0.6409 -0.1675 0.0527  -0.0946 324 GLU B CG  
6831 C CD  . GLU B 324 ? 0.8994 0.7913 0.8376 -0.1794 0.0483  -0.0968 324 GLU B CD  
6832 O OE1 . GLU B 324 ? 0.9341 0.8318 0.8849 -0.1773 0.0428  -0.0910 324 GLU B OE1 
6833 O OE2 . GLU B 324 ? 0.9553 0.8475 0.8819 -0.1912 0.0504  -0.1044 324 GLU B OE2 
6834 N N   . ASP B 325 ? 0.3652 0.2192 0.3150 -0.1363 0.0753  -0.0898 325 ASP B N   
6835 C CA  . ASP B 325 ? 0.4268 0.2676 0.3726 -0.1334 0.0886  -0.0954 325 ASP B CA  
6836 C C   . ASP B 325 ? 0.4025 0.2471 0.3472 -0.1245 0.0864  -0.0919 325 ASP B C   
6837 O O   . ASP B 325 ? 0.3711 0.2138 0.3075 -0.1271 0.0915  -0.0973 325 ASP B O   
6838 C CB  . ASP B 325 ? 0.3858 0.2111 0.3416 -0.1265 0.1009  -0.0947 325 ASP B CB  
6839 C CG  . ASP B 325 ? 0.5020 0.3212 0.4580 -0.1359 0.1055  -0.0994 325 ASP B CG  
6840 O OD1 . ASP B 325 ? 0.5128 0.3351 0.4587 -0.1488 0.1046  -0.1068 325 ASP B OD1 
6841 O OD2 . ASP B 325 ? 0.4262 0.2381 0.3923 -0.1306 0.1098  -0.0953 325 ASP B OD2 
6842 N N   . ALA B 326 ? 0.3386 0.1883 0.2920 -0.1142 0.0796  -0.0831 326 ALA B N   
6843 C CA  . ALA B 326 ? 0.3234 0.1764 0.2765 -0.1056 0.0776  -0.0796 326 ALA B CA  
6844 C C   . ALA B 326 ? 0.3222 0.1865 0.2633 -0.1127 0.0696  -0.0819 326 ALA B C   
6845 O O   . ALA B 326 ? 0.3300 0.1932 0.2657 -0.1111 0.0735  -0.0844 326 ALA B O   
6846 C CB  . ALA B 326 ? 0.2998 0.1575 0.2630 -0.0950 0.0704  -0.0697 326 ALA B CB  
6847 N N   . VAL B 327 ? 0.3195 0.1956 0.2570 -0.1202 0.0583  -0.0802 327 VAL B N   
6848 C CA  . VAL B 327 ? 0.3564 0.2441 0.2826 -0.1260 0.0501  -0.0806 327 VAL B CA  
6849 C C   . VAL B 327 ? 0.3655 0.2484 0.2796 -0.1360 0.0583  -0.0897 327 VAL B C   
6850 O O   . VAL B 327 ? 0.3521 0.2380 0.2571 -0.1376 0.0586  -0.0914 327 VAL B O   
6851 C CB  . VAL B 327 ? 0.3293 0.2316 0.2566 -0.1305 0.0361  -0.0754 327 VAL B CB  
6852 C CG1 . VAL B 327 ? 0.3615 0.2754 0.2769 -0.1365 0.0284  -0.0749 327 VAL B CG1 
6853 C CG2 . VAL B 327 ? 0.2864 0.1936 0.2256 -0.1204 0.0289  -0.0663 327 VAL B CG2 
6854 N N   . ARG B 328 ? 0.3627 0.2376 0.2762 -0.1431 0.0658  -0.0959 328 ARG B N   
6855 C CA  . ARG B 328 ? 0.3881 0.2569 0.2900 -0.1530 0.0752  -0.1053 328 ARG B CA  
6856 C C   . ARG B 328 ? 0.3918 0.2503 0.2939 -0.1471 0.0874  -0.1087 328 ARG B C   
6857 O O   . ARG B 328 ? 0.4041 0.2629 0.2956 -0.1531 0.0916  -0.1138 328 ARG B O   
6858 C CB  . ARG B 328 ? 0.4092 0.2696 0.3117 -0.1611 0.0822  -0.1114 328 ARG B CB  
6859 C CG  . ARG B 328 ? 0.4378 0.2923 0.3272 -0.1730 0.0918  -0.1217 328 ARG B CG  
6860 C CD  . ARG B 328 ? 0.4926 0.3376 0.3824 -0.1813 0.0997  -0.1284 328 ARG B CD  
6861 N NE  . ARG B 328 ? 0.5547 0.3838 0.4559 -0.1726 0.1120  -0.1289 328 ARG B NE  
6862 C CZ  . ARG B 328 ? 0.5885 0.4139 0.5012 -0.1680 0.1113  -0.1249 328 ARG B CZ  
6863 N NH1 . ARG B 328 ? 0.6318 0.4686 0.5470 -0.1716 0.0990  -0.1205 328 ARG B NH1 
6864 N NH2 . ARG B 328 ? 0.5608 0.3714 0.4831 -0.1597 0.1233  -0.1248 328 ARG B NH2 
6865 N N   . ASP B 329 ? 0.3825 0.2321 0.2970 -0.1355 0.0937  -0.1057 329 ASP B N   
6866 C CA  . ASP B 329 ? 0.4571 0.2983 0.3747 -0.1284 0.1047  -0.1076 329 ASP B CA  
6867 C C   . ASP B 329 ? 0.3699 0.2212 0.2828 -0.1255 0.0980  -0.1044 329 ASP B C   
6868 O O   . ASP B 329 ? 0.3798 0.2292 0.2868 -0.1282 0.1049  -0.1092 329 ASP B O   
6869 C CB  . ASP B 329 ? 0.4228 0.2550 0.3558 -0.1153 0.1104  -0.1025 329 ASP B CB  
6870 C CG  . ASP B 329 ? 0.4301 0.2538 0.3691 -0.1073 0.1224  -0.1037 329 ASP B CG  
6871 O OD1 . ASP B 329 ? 0.4563 0.2688 0.3950 -0.1110 0.1356  -0.1104 329 ASP B OD1 
6872 O OD2 . ASP B 329 ? 0.3710 0.1994 0.3155 -0.0976 0.1187  -0.0978 329 ASP B OD2 
6873 N N   . PHE B 330 ? 0.3474 0.2096 0.2629 -0.1206 0.0847  -0.0964 330 PHE B N   
6874 C CA  . PHE B 330 ? 0.3330 0.2048 0.2444 -0.1175 0.0775  -0.0925 330 PHE B CA  
6875 C C   . PHE B 330 ? 0.3454 0.2243 0.2419 -0.1289 0.0747  -0.0963 330 PHE B C   
6876 O O   . PHE B 330 ? 0.3493 0.2283 0.2407 -0.1296 0.0793  -0.0987 330 PHE B O   
6877 C CB  . PHE B 330 ? 0.3094 0.1910 0.2263 -0.1115 0.0638  -0.0834 330 PHE B CB  
6878 C CG  . PHE B 330 ? 0.2926 0.1821 0.2081 -0.1057 0.0573  -0.0784 330 PHE B CG  
6879 C CD1 . PHE B 330 ? 0.2812 0.1663 0.2053 -0.0948 0.0616  -0.0759 330 PHE B CD1 
6880 C CD2 . PHE B 330 ? 0.2889 0.1905 0.1952 -0.1109 0.0468  -0.0755 330 PHE B CD2 
6881 C CE1 . PHE B 330 ? 0.2664 0.1589 0.1891 -0.0901 0.0555  -0.0717 330 PHE B CE1 
6882 C CE2 . PHE B 330 ? 0.2894 0.1979 0.1947 -0.1056 0.0410  -0.0705 330 PHE B CE2 
6883 C CZ  . PHE B 330 ? 0.3232 0.2271 0.2363 -0.0957 0.0453  -0.0691 330 PHE B CZ  
6884 N N   . ILE B 331 ? 0.3602 0.2457 0.2502 -0.1379 0.0672  -0.0963 331 ILE B N   
6885 C CA  . ILE B 331 ? 0.3692 0.2615 0.2446 -0.1492 0.0645  -0.0991 331 ILE B CA  
6886 C C   . ILE B 331 ? 0.3905 0.2725 0.2591 -0.1560 0.0791  -0.1089 331 ILE B C   
6887 O O   . ILE B 331 ? 0.3982 0.2829 0.2573 -0.1608 0.0812  -0.1110 331 ILE B O   
6888 C CB  . ILE B 331 ? 0.3850 0.2854 0.2561 -0.1579 0.0552  -0.0978 331 ILE B CB  
6889 C CG1 . ILE B 331 ? 0.3625 0.2739 0.2416 -0.1512 0.0410  -0.0877 331 ILE B CG1 
6890 C CG2 . ILE B 331 ? 0.3942 0.3011 0.2498 -0.1699 0.0531  -0.1004 331 ILE B CG2 
6891 C CD1 . ILE B 331 ? 0.3961 0.3179 0.2709 -0.1480 0.0321  -0.0810 331 ILE B CD1 
6892 N N   . GLY B 332 ? 0.4225 0.2924 0.2964 -0.1566 0.0900  -0.1147 332 GLY B N   
6893 C CA  . GLY B 332 ? 0.4835 0.3421 0.3532 -0.1620 0.1054  -0.1240 332 GLY B CA  
6894 C C   . GLY B 332 ? 0.4501 0.3062 0.3226 -0.1555 0.1121  -0.1242 332 GLY B C   
6895 O O   . GLY B 332 ? 0.4513 0.3062 0.3149 -0.1628 0.1189  -0.1299 332 GLY B O   
6896 N N   . ARG B 333 ? 0.3998 0.2561 0.2848 -0.1421 0.1099  -0.1178 333 ARG B N   
6897 C CA  . ARG B 333 ? 0.3944 0.2492 0.2839 -0.1354 0.1160  -0.1178 333 ARG B CA  
6898 C C   . ARG B 333 ? 0.4446 0.3110 0.3235 -0.1398 0.1082  -0.1157 333 ARG B C   
6899 O O   . ARG B 333 ? 0.3974 0.2622 0.2736 -0.1419 0.1158  -0.1197 333 ARG B O   
6900 C CB  . ARG B 333 ? 0.3920 0.2450 0.2970 -0.1205 0.1147  -0.1110 333 ARG B CB  
6901 C CG  . ARG B 333 ? 0.4737 0.3133 0.3902 -0.1151 0.1254  -0.1126 333 ARG B CG  
6902 C CD  . ARG B 333 ? 0.3936 0.2329 0.3245 -0.1008 0.1222  -0.1043 333 ARG B CD  
6903 N NE  . ARG B 333 ? 0.4415 0.2680 0.3839 -0.0951 0.1328  -0.1045 333 ARG B NE  
6904 C CZ  . ARG B 333 ? 0.5014 0.3192 0.4534 -0.0883 0.1448  -0.1054 333 ARG B CZ  
6905 N NH1 . ARG B 333 ? 0.4296 0.2503 0.3812 -0.0871 0.1478  -0.1072 333 ARG B NH1 
6906 N NH2 . ARG B 333 ? 0.5406 0.3471 0.5032 -0.0828 0.1537  -0.1041 333 ARG B NH2 
6907 N N   . LEU B 334 ? 0.3759 0.2540 0.2495 -0.1412 0.0934  -0.1091 334 LEU B N   
6908 C CA  . LEU B 334 ? 0.3733 0.2621 0.2363 -0.1459 0.0859  -0.1062 334 LEU B CA  
6909 C C   . LEU B 334 ? 0.3994 0.2872 0.2482 -0.1600 0.0917  -0.1133 334 LEU B C   
6910 O O   . LEU B 334 ? 0.4622 0.3529 0.3040 -0.1640 0.0938  -0.1144 334 LEU B O   
6911 C CB  . LEU B 334 ? 0.3568 0.2573 0.2182 -0.1445 0.0695  -0.0972 334 LEU B CB  
6912 C CG  . LEU B 334 ? 0.3311 0.2338 0.2051 -0.1315 0.0628  -0.0898 334 LEU B CG  
6913 C CD1 . LEU B 334 ? 0.3729 0.2863 0.2461 -0.1314 0.0478  -0.0818 334 LEU B CD1 
6914 C CD2 . LEU B 334 ? 0.3259 0.2306 0.2028 -0.1245 0.0640  -0.0874 334 LEU B CD2 
6915 N N   . LYS B 335 ? 0.4259 0.3095 0.2700 -0.1683 0.0945  -0.1183 335 LYS B N   
6916 C CA  . LYS B 335 ? 0.4444 0.3262 0.2744 -0.1826 0.1009  -0.1258 335 LYS B CA  
6917 C C   . LYS B 335 ? 0.4587 0.3305 0.2898 -0.1835 0.1168  -0.1338 335 LYS B C   
6918 O O   . LYS B 335 ? 0.5070 0.3804 0.3272 -0.1924 0.1206  -0.1375 335 LYS B O   
6919 C CB  . LYS B 335 ? 0.4648 0.3429 0.2908 -0.1912 0.1022  -0.1307 335 LYS B CB  
6920 C CG  . LYS B 335 ? 0.6536 0.5315 0.4629 -0.2076 0.1070  -0.1382 335 LYS B CG  
6921 C CD  . LYS B 335 ? 0.7332 0.6255 0.5307 -0.2140 0.0936  -0.1318 335 LYS B CD  
6922 C CE  . LYS B 335 ? 0.8299 0.7230 0.6101 -0.2311 0.0968  -0.1384 335 LYS B CE  
6923 N NZ  . LYS B 335 ? 0.8061 0.7130 0.5758 -0.2364 0.0838  -0.1309 335 LYS B NZ  
6924 N N   . LYS B 336 ? 0.4552 0.3164 0.3002 -0.1742 0.1265  -0.1360 336 LYS B N   
6925 C CA  . LYS B 336 ? 0.5142 0.3655 0.3630 -0.1741 0.1422  -0.1431 336 LYS B CA  
6926 C C   . LYS B 336 ? 0.5243 0.3822 0.3739 -0.1701 0.1403  -0.1400 336 LYS B C   
6927 O O   . LYS B 336 ? 0.5371 0.3921 0.3818 -0.1764 0.1495  -0.1460 336 LYS B O   
6928 C CB  . LYS B 336 ? 0.5641 0.4027 0.4295 -0.1638 0.1524  -0.1445 336 LYS B CB  
6929 C CG  . LYS B 336 ? 0.7106 0.5378 0.5754 -0.1698 0.1610  -0.1511 336 LYS B CG  
6930 C CD  . LYS B 336 ? 0.7897 0.6244 0.6451 -0.1770 0.1488  -0.1488 336 LYS B CD  
6931 C CE  . LYS B 336 ? 0.7888 0.6142 0.6470 -0.1797 0.1535  -0.1524 336 LYS B CE  
6932 N NZ  . LYS B 336 ? 0.7705 0.6065 0.6195 -0.1873 0.1397  -0.1495 336 LYS B NZ  
6933 N N   . ILE B 337 ? 0.4971 0.3639 0.3526 -0.1603 0.1286  -0.1308 337 ILE B N   
6934 C CA  . ILE B 337 ? 0.4848 0.3591 0.3396 -0.1576 0.1252  -0.1274 337 ILE B CA  
6935 C C   . ILE B 337 ? 0.4869 0.3688 0.3246 -0.1703 0.1205  -0.1278 337 ILE B C   
6936 O O   . ILE B 337 ? 0.5270 0.4091 0.3603 -0.1752 0.1266  -0.1315 337 ILE B O   
6937 C CB  . ILE B 337 ? 0.3897 0.2719 0.2530 -0.1456 0.1129  -0.1175 337 ILE B CB  
6938 C CG1 . ILE B 337 ? 0.3794 0.2539 0.2595 -0.1331 0.1179  -0.1166 337 ILE B CG1 
6939 C CG2 . ILE B 337 ? 0.3801 0.2701 0.2417 -0.1440 0.1094  -0.1142 337 ILE B CG2 
6940 C CD1 . ILE B 337 ? 0.3779 0.2589 0.2650 -0.1225 0.1056  -0.1073 337 ILE B CD1 
6941 N N   . HIS B 338 ? 0.4437 0.3323 0.2723 -0.1758 0.1094  -0.1237 338 HIS B N   
6942 C CA  . HIS B 338 ? 0.4957 0.3922 0.3084 -0.1874 0.1034  -0.1224 338 HIS B CA  
6943 C C   . HIS B 338 ? 0.5814 0.4714 0.3837 -0.2003 0.1163  -0.1327 338 HIS B C   
6944 O O   . HIS B 338 ? 0.5713 0.4654 0.3635 -0.2079 0.1165  -0.1331 338 HIS B O   
6945 C CB  . HIS B 338 ? 0.5046 0.4079 0.3116 -0.1909 0.0909  -0.1172 338 HIS B CB  
6946 C CG  . HIS B 338 ? 0.6383 0.5499 0.4297 -0.2026 0.0839  -0.1148 338 HIS B CG  
6947 N ND1 . HIS B 338 ? 0.7023 0.6119 0.4806 -0.2168 0.0884  -0.1215 338 HIS B ND1 
6948 C CD2 . HIS B 338 ? 0.6809 0.6025 0.4678 -0.2023 0.0728  -0.1060 338 HIS B CD2 
6949 C CE1 . HIS B 338 ? 0.7041 0.6226 0.4704 -0.2248 0.0800  -0.1167 338 HIS B CE1 
6950 N NE2 . HIS B 338 ? 0.6623 0.5877 0.4339 -0.2159 0.0706  -0.1072 338 HIS B NE2 
6951 N N   . GLU B 339 ? 0.6148 0.4938 0.4194 -0.2032 0.1276  -0.1411 339 GLU B N   
6952 C CA  . GLU B 339 ? 0.6739 0.5457 0.4685 -0.2161 0.1406  -0.1515 339 GLU B CA  
6953 C C   . GLU B 339 ? 0.6606 0.5243 0.4632 -0.2128 0.1549  -0.1576 339 GLU B C   
6954 O O   . GLU B 339 ? 0.6696 0.5281 0.4635 -0.2236 0.1656  -0.1659 339 GLU B O   
6955 C CB  . GLU B 339 ? 0.7428 0.6059 0.5354 -0.2222 0.1470  -0.1584 339 GLU B CB  
6956 C CG  . GLU B 339 ? 0.8560 0.7055 0.6640 -0.2136 0.1598  -0.1633 339 GLU B CG  
6957 C CD  . GLU B 339 ? 1.0313 0.8722 0.8375 -0.2194 0.1652  -0.1693 339 GLU B CD  
6958 O OE1 . GLU B 339 ? 1.0712 0.8999 0.8899 -0.2129 0.1759  -0.1729 339 GLU B OE1 
6959 O OE2 . GLU B 339 ? 1.0864 0.9328 0.8790 -0.2307 0.1586  -0.1700 339 GLU B OE2 
6960 N N   . SER B 340 ? 0.6481 0.5109 0.4669 -0.1985 0.1550  -0.1535 340 SER B N   
6961 C CA  . SER B 340 ? 0.6324 0.4877 0.4617 -0.1937 0.1682  -0.1588 340 SER B CA  
6962 C C   . SER B 340 ? 0.6319 0.4947 0.4573 -0.1956 0.1664  -0.1573 340 SER B C   
6963 O O   . SER B 340 ? 0.6676 0.5248 0.4999 -0.1941 0.1778  -0.1628 340 SER B O   
6964 C CB  . SER B 340 ? 0.5848 0.4358 0.4341 -0.1772 0.1695  -0.1549 340 SER B CB  
6965 O OG  . SER B 340 ? 0.5366 0.3983 0.3912 -0.1678 0.1575  -0.1457 340 SER B OG  
6966 N N   . VAL B 341 ? 0.5728 0.4478 0.3885 -0.1984 0.1525  -0.1497 341 VAL B N   
6967 C CA  . VAL B 341 ? 0.5734 0.4555 0.3857 -0.1998 0.1499  -0.1472 341 VAL B CA  
6968 C C   . VAL B 341 ? 0.6214 0.5101 0.4143 -0.2138 0.1436  -0.1459 341 VAL B C   
6969 O O   . VAL B 341 ? 0.6148 0.5058 0.3985 -0.2196 0.1370  -0.1439 341 VAL B O   
6970 C CB  . VAL B 341 ? 0.5728 0.4635 0.3952 -0.1867 0.1385  -0.1372 341 VAL B CB  
6971 C CG1 . VAL B 341 ? 0.4945 0.3793 0.3359 -0.1731 0.1449  -0.1384 341 VAL B CG1 
6972 C CG2 . VAL B 341 ? 0.5875 0.4858 0.4056 -0.1846 0.1230  -0.1279 341 VAL B CG2 
6973 N N   . ASP B 342 ? 0.6417 0.5339 0.4289 -0.2192 0.1455  -0.1467 342 ASP B N   
6974 C CA  . ASP B 342 ? 0.6828 0.5804 0.4514 -0.2330 0.1407  -0.1454 342 ASP B CA  
6975 C C   . ASP B 342 ? 0.5832 0.4923 0.3487 -0.2297 0.1249  -0.1333 342 ASP B C   
6976 O O   . ASP B 342 ? 0.7073 0.6216 0.4583 -0.2396 0.1180  -0.1298 342 ASP B O   
6977 C CB  . ASP B 342 ? 0.7973 0.6905 0.5599 -0.2428 0.1534  -0.1544 342 ASP B CB  
6978 C CG  . ASP B 342 ? 0.9087 0.7892 0.6753 -0.2458 0.1701  -0.1666 342 ASP B CG  
6979 O OD1 . ASP B 342 ? 0.9116 0.7873 0.6742 -0.2498 0.1718  -0.1696 342 ASP B OD1 
6980 O OD2 . ASP B 342 ? 0.9536 0.8285 0.7286 -0.2435 0.1817  -0.1730 342 ASP B OD2 
6981 N N   . PHE B 343 ? 0.4785 0.3912 0.2575 -0.2160 0.1192  -0.1268 343 PHE B N   
6982 C CA  . PHE B 343 ? 0.4588 0.3810 0.2372 -0.2112 0.1047  -0.1152 343 PHE B CA  
6983 C C   . PHE B 343 ? 0.4481 0.3730 0.2326 -0.2023 0.0940  -0.1080 343 PHE B C   
6984 O O   . PHE B 343 ? 0.4863 0.4059 0.2744 -0.2009 0.0977  -0.1122 343 PHE B O   
6985 C CB  . PHE B 343 ? 0.5226 0.4472 0.3114 -0.2029 0.1058  -0.1133 343 PHE B CB  
6986 C CG  . PHE B 343 ? 0.5031 0.4232 0.3091 -0.1905 0.1119  -0.1166 343 PHE B CG  
6987 C CD1 . PHE B 343 ? 0.5047 0.4168 0.3165 -0.1915 0.1267  -0.1270 343 PHE B CD1 
6988 C CD2 . PHE B 343 ? 0.4745 0.3977 0.2911 -0.1778 0.1030  -0.1093 343 PHE B CD2 
6989 C CE1 . PHE B 343 ? 0.4811 0.3885 0.3097 -0.1796 0.1323  -0.1294 343 PHE B CE1 
6990 C CE2 . PHE B 343 ? 0.4436 0.3626 0.2757 -0.1667 0.1085  -0.1120 343 PHE B CE2 
6991 C CZ  . PHE B 343 ? 0.4226 0.3337 0.2611 -0.1673 0.1230  -0.1217 343 PHE B CZ  
6992 N N   . GLN B 344 ? 0.4334 0.3659 0.2194 -0.1964 0.0809  -0.0973 344 GLN B N   
6993 C CA  . GLN B 344 ? 0.4262 0.3616 0.2191 -0.1874 0.0706  -0.0903 344 GLN B CA  
6994 C C   . GLN B 344 ? 0.4292 0.3633 0.2383 -0.1733 0.0716  -0.0892 344 GLN B C   
6995 O O   . GLN B 344 ? 0.3884 0.3267 0.2020 -0.1676 0.0678  -0.0841 344 GLN B O   
6996 C CB  . GLN B 344 ? 0.4981 0.4415 0.2859 -0.1878 0.0565  -0.0794 344 GLN B CB  
6997 C CG  . GLN B 344 ? 0.6570 0.6031 0.4292 -0.2010 0.0552  -0.0786 344 GLN B CG  
6998 C CD  . GLN B 344 ? 0.6877 0.6404 0.4544 -0.2033 0.0418  -0.0687 344 GLN B CD  
6999 O OE1 . GLN B 344 ? 0.7275 0.6817 0.4937 -0.2040 0.0368  -0.0674 344 GLN B OE1 
7000 N NE2 . GLN B 344 ? 0.5499 0.5064 0.3136 -0.2041 0.0360  -0.0614 344 GLN B NE2 
7001 N N   . PRO B 345 ? 0.4082 0.3365 0.2259 -0.1677 0.0766  -0.0935 345 PRO B N   
7002 C CA  . PRO B 345 ? 0.3987 0.3254 0.2316 -0.1547 0.0782  -0.0927 345 PRO B CA  
7003 C C   . PRO B 345 ? 0.3843 0.3171 0.2229 -0.1452 0.0649  -0.0827 345 PRO B C   
7004 O O   . PRO B 345 ? 0.3530 0.2889 0.1875 -0.1470 0.0561  -0.0778 345 PRO B O   
7005 C CB  . PRO B 345 ? 0.4186 0.3358 0.2575 -0.1535 0.0880  -0.1003 345 PRO B CB  
7006 C CG  . PRO B 345 ? 0.4711 0.3882 0.2996 -0.1624 0.0845  -0.1009 345 PRO B CG  
7007 C CD  . PRO B 345 ? 0.3915 0.3145 0.2055 -0.1733 0.0803  -0.0988 345 PRO B CD  
7008 N N   . VAL B 346 ? 0.3156 0.2502 0.1645 -0.1353 0.0638  -0.0798 346 VAL B N   
7009 C CA  . VAL B 346 ? 0.3026 0.2415 0.1589 -0.1251 0.0531  -0.0716 346 VAL B CA  
7010 C C   . VAL B 346 ? 0.3091 0.2422 0.1773 -0.1163 0.0578  -0.0747 346 VAL B C   
7011 O O   . VAL B 346 ? 0.3052 0.2347 0.1808 -0.1122 0.0666  -0.0795 346 VAL B O   
7012 C CB  . VAL B 346 ? 0.3223 0.2675 0.1809 -0.1206 0.0479  -0.0657 346 VAL B CB  
7013 C CG1 . VAL B 346 ? 0.2782 0.2275 0.1434 -0.1113 0.0367  -0.0571 346 VAL B CG1 
7014 C CG2 . VAL B 346 ? 0.3426 0.2915 0.1901 -0.1297 0.0453  -0.0633 346 VAL B CG2 
7015 N N   . VAL B 347 ? 0.2783 0.2107 0.1493 -0.1130 0.0519  -0.0715 347 VAL B N   
7016 C CA  . VAL B 347 ? 0.2731 0.1988 0.1546 -0.1056 0.0564  -0.0741 347 VAL B CA  
7017 C C   . VAL B 347 ? 0.2512 0.1812 0.1398 -0.0960 0.0464  -0.0664 347 VAL B C   
7018 O O   . VAL B 347 ? 0.2755 0.2094 0.1625 -0.0961 0.0368  -0.0608 347 VAL B O   
7019 C CB  . VAL B 347 ? 0.3034 0.2232 0.1824 -0.1109 0.0593  -0.0780 347 VAL B CB  
7020 C CG1 . VAL B 347 ? 0.2819 0.1933 0.1731 -0.1029 0.0651  -0.0802 347 VAL B CG1 
7021 C CG2 . VAL B 347 ? 0.3938 0.3095 0.2642 -0.1218 0.0691  -0.0859 347 VAL B CG2 
7022 N N   . PHE B 348 ? 0.2403 0.1699 0.1374 -0.0876 0.0489  -0.0661 348 PHE B N   
7023 C CA  . PHE B 348 ? 0.2213 0.1540 0.1249 -0.0786 0.0408  -0.0597 348 PHE B CA  
7024 C C   . PHE B 348 ? 0.2335 0.1581 0.1460 -0.0726 0.0446  -0.0612 348 PHE B C   
7025 O O   . PHE B 348 ? 0.2502 0.1671 0.1698 -0.0692 0.0556  -0.0664 348 PHE B O   
7026 C CB  . PHE B 348 ? 0.2112 0.1481 0.1188 -0.0727 0.0409  -0.0584 348 PHE B CB  
7027 C CG  . PHE B 348 ? 0.2515 0.1974 0.1531 -0.0750 0.0320  -0.0522 348 PHE B CG  
7028 C CD1 . PHE B 348 ? 0.2544 0.2027 0.1469 -0.0839 0.0322  -0.0526 348 PHE B CD1 
7029 C CD2 . PHE B 348 ? 0.2190 0.1700 0.1242 -0.0683 0.0234  -0.0455 348 PHE B CD2 
7030 C CE1 . PHE B 348 ? 0.2478 0.2028 0.1364 -0.0852 0.0246  -0.0461 348 PHE B CE1 
7031 C CE2 . PHE B 348 ? 0.2325 0.1905 0.1345 -0.0694 0.0160  -0.0391 348 PHE B CE2 
7032 C CZ  . PHE B 348 ? 0.1984 0.1578 0.0924 -0.0776 0.0168  -0.0393 348 PHE B CZ  
7033 N N   . VAL B 349 ? 0.2105 0.1366 0.1241 -0.0708 0.0360  -0.0560 349 VAL B N   
7034 C CA  . VAL B 349 ? 0.2072 0.1258 0.1299 -0.0650 0.0385  -0.0559 349 VAL B CA  
7035 C C   . VAL B 349 ? 0.2622 0.1839 0.1895 -0.0567 0.0312  -0.0497 349 VAL B C   
7036 O O   . VAL B 349 ? 0.2348 0.1638 0.1591 -0.0578 0.0203  -0.0437 349 VAL B O   
7037 C CB  . VAL B 349 ? 0.2134 0.1308 0.1339 -0.0707 0.0353  -0.0557 349 VAL B CB  
7038 C CG1 . VAL B 349 ? 0.2160 0.1255 0.1470 -0.0644 0.0380  -0.0545 349 VAL B CG1 
7039 C CG2 . VAL B 349 ? 0.2692 0.1833 0.1830 -0.0800 0.0429  -0.0626 349 VAL B CG2 
7040 N N   . VAL B 350 ? 0.1856 0.1026 0.1210 -0.0477 0.0376  -0.0505 350 VAL B N   
7041 C CA  . VAL B 350 ? 0.1712 0.0911 0.1092 -0.0398 0.0320  -0.0454 350 VAL B CA  
7042 C C   . VAL B 350 ? 0.1666 0.0814 0.1194 -0.0274 0.0373  -0.0411 350 VAL B C   
7043 O O   . VAL B 350 ? 0.2129 0.1210 0.1737 -0.0221 0.0487  -0.0445 350 VAL B O   
7044 C CB  . VAL B 350 ? 0.1680 0.0947 0.1039 -0.0378 0.0331  -0.0466 350 VAL B CB  
7045 C CG1 . VAL B 350 ? 0.1502 0.0876 0.0910 -0.0289 0.0237  -0.0371 350 VAL B CG1 
7046 C CG2 . VAL B 350 ? 0.2058 0.1405 0.1321 -0.0478 0.0293  -0.0474 350 VAL B CG2 
7047 N N   . LEU B 351 ? 0.1547 0.0737 0.1120 -0.0220 0.0291  -0.0325 351 LEU B N   
7048 C CA  . LEU B 351 ? 0.1937 0.1101 0.1645 -0.0098 0.0327  -0.0261 351 LEU B CA  
7049 C C   . LEU B 351 ? 0.1991 0.1241 0.1715 -0.0048 0.0219  -0.0168 351 LEU B C   
7050 O O   . LEU B 351 ? 0.1676 0.0986 0.1318 -0.0109 0.0126  -0.0158 351 LEU B O   
7051 C CB  . LEU B 351 ? 0.2013 0.1043 0.1754 -0.0127 0.0408  -0.0297 351 LEU B CB  
7052 C CG  . LEU B 351 ? 0.1861 0.0868 0.1538 -0.0232 0.0351  -0.0310 351 LEU B CG  
7053 C CD1 . LEU B 351 ? 0.2128 0.1039 0.1896 -0.0198 0.0407  -0.0286 351 LEU B CD1 
7054 C CD2 . LEU B 351 ? 0.2130 0.1126 0.1694 -0.0371 0.0362  -0.0401 351 LEU B CD2 
7055 N N   . ASP B 352 ? 0.1682 0.0934 0.1512 0.0066  0.0236  -0.0098 352 ASP B N   
7056 C CA  . ASP B 352 ? 0.1671 0.0989 0.1516 0.0113  0.0150  -0.0016 352 ASP B CA  
7057 C C   . ASP B 352 ? 0.1554 0.0844 0.1357 0.0028  0.0106  -0.0024 352 ASP B C   
7058 O O   . ASP B 352 ? 0.1785 0.0984 0.1598 -0.0026 0.0163  -0.0066 352 ASP B O   
7059 C CB  . ASP B 352 ? 0.1735 0.1041 0.1687 0.0233  0.0187  0.0058  352 ASP B CB  
7060 C CG  . ASP B 352 ? 0.2313 0.1691 0.2323 0.0322  0.0210  0.0083  352 ASP B CG  
7061 O OD1 . ASP B 352 ? 0.1924 0.1354 0.1898 0.0305  0.0200  0.0050  352 ASP B OD1 
7062 O OD2 . ASP B 352 ? 0.2039 0.1492 0.2122 0.0361  0.0207  0.0123  352 ASP B OD2 
7063 N N   . GLY B 353 ? 0.1658 0.1028 0.1422 0.0013  0.0006  0.0016  353 GLY B N   
7064 C CA  . GLY B 353 ? 0.1643 0.1012 0.1384 -0.0062 -0.0044 0.0016  353 GLY B CA  
7065 C C   . GLY B 353 ? 0.1510 0.0879 0.1332 -0.0011 -0.0051 0.0078  353 GLY B C   
7066 O O   . GLY B 353 ? 0.1393 0.0775 0.1217 -0.0073 -0.0090 0.0080  353 GLY B O   
7067 N N   . GLU B 354 ? 0.1023 0.0386 0.0914 0.0098  -0.0015 0.0131  354 GLU B N   
7068 C CA  . GLU B 354 ? 0.1187 0.0558 0.1142 0.0145  -0.0023 0.0194  354 GLU B CA  
7069 C C   . GLU B 354 ? 0.1698 0.1059 0.1719 0.0183  0.0042  0.0192  354 GLU B C   
7070 O O   . GLU B 354 ? 0.1730 0.1131 0.1776 0.0192  0.0031  0.0213  354 GLU B O   
7071 C CB  . GLU B 354 ? 0.1652 0.1225 0.1659 0.0170  -0.0079 0.0223  354 GLU B CB  
7072 C CG  . GLU B 354 ? 0.2478 0.2094 0.2483 0.0202  -0.0091 0.0202  354 GLU B CG  
7073 C CD  . GLU B 354 ? 0.4952 0.4555 0.4906 0.0211  -0.0076 0.0196  354 GLU B CD  
7074 O OE1 . GLU B 354 ? 0.7012 0.6717 0.6952 0.0197  -0.0106 0.0198  354 GLU B OE1 
7075 O OE2 . GLU B 354 ? 0.4956 0.4413 0.4853 0.0222  -0.0021 0.0169  354 GLU B OE2 
7076 N N   . ASN B 355 ? 0.1293 0.0602 0.1330 0.0201  0.0113  0.0165  355 ASN B N   
7077 C CA  . ASN B 355 ? 0.1311 0.0644 0.1400 0.0245  0.0158  0.0180  355 ASN B CA  
7078 C C   . ASN B 355 ? 0.2037 0.1250 0.2158 0.0213  0.0242  0.0158  355 ASN B C   
7079 O O   . ASN B 355 ? 0.1922 0.1145 0.2082 0.0241  0.0272  0.0186  355 ASN B O   
7080 C CB  . ASN B 355 ? 0.1594 0.0977 0.1695 0.0295  0.0174  0.0180  355 ASN B CB  
7081 C CG  . ASN B 355 ? 0.1491 0.1004 0.1573 0.0312  0.0093  0.0198  355 ASN B CG  
7082 O OD1 . ASN B 355 ? 0.1615 0.1187 0.1690 0.0301  0.0045  0.0212  355 ASN B OD1 
7083 N ND2 . ASN B 355 ? 0.1418 0.0965 0.1489 0.0326  0.0086  0.0186  355 ASN B ND2 
7084 N N   . CYS B 356 ? 0.1450 0.0550 0.1545 0.0135  0.0281  0.0097  356 CYS B N   
7085 C CA  . CYS B 356 ? 0.1493 0.0490 0.1613 0.0086  0.0364  0.0055  356 CYS B CA  
7086 C C   . CYS B 356 ? 0.1813 0.0783 0.1946 0.0022  0.0352  0.0058  356 CYS B C   
7087 O O   . CYS B 356 ? 0.1849 0.0759 0.2017 0.0005  0.0416  0.0047  356 CYS B O   
7088 C CB  . CYS B 356 ? 0.1855 0.0765 0.1923 0.0005  0.0415  -0.0040 356 CYS B CB  
7089 S SG  . CYS B 356 ? 0.2074 0.0986 0.2031 -0.0126 0.0338  -0.0101 356 CYS B SG  
7090 N N   . TRP B 357 ? 0.1686 0.0702 0.1800 -0.0014 0.0274  0.0079  357 TRP B N   
7091 C CA  . TRP B 357 ? 0.1730 0.0731 0.1868 -0.0101 0.0262  0.0072  357 TRP B CA  
7092 C C   . TRP B 357 ? 0.1928 0.0949 0.2132 -0.0048 0.0287  0.0127  357 TRP B C   
7093 O O   . TRP B 357 ? 0.1573 0.0555 0.1807 -0.0121 0.0312  0.0108  357 TRP B O   
7094 C CB  . TRP B 357 ? 0.1519 0.0620 0.1635 -0.0145 0.0157  0.0090  357 TRP B CB  
7095 C CG  . TRP B 357 ? 0.1356 0.0496 0.1379 -0.0184 0.0110  0.0041  357 TRP B CG  
7096 C CD1 . TRP B 357 ? 0.1427 0.0656 0.1410 -0.0130 0.0040  0.0073  357 TRP B CD1 
7097 C CD2 . TRP B 357 ? 0.1713 0.0798 0.1663 -0.0292 0.0138  -0.0052 357 TRP B CD2 
7098 N NE1 . TRP B 357 ? 0.1471 0.0705 0.1364 -0.0197 0.0021  0.0010  357 TRP B NE1 
7099 C CE2 . TRP B 357 ? 0.1663 0.0811 0.1529 -0.0296 0.0081  -0.0068 357 TRP B CE2 
7100 C CE3 . TRP B 357 ? 0.1640 0.0620 0.1578 -0.0392 0.0211  -0.0129 357 TRP B CE3 
7101 C CZ2 . TRP B 357 ? 0.1831 0.0947 0.1600 -0.0395 0.0096  -0.0154 357 TRP B CZ2 
7102 C CZ3 . TRP B 357 ? 0.2209 0.1197 0.2056 -0.0473 0.0213  -0.0213 357 TRP B CZ3 
7103 C CH2 . TRP B 357 ? 0.1914 0.0950 0.1673 -0.0483 0.0164  -0.0227 357 TRP B CH2 
7104 N N   . GLU B 358 ? 0.1740 0.0837 0.1955 0.0061  0.0275  0.0186  358 GLU B N   
7105 C CA  . GLU B 358 ? 0.1856 0.0980 0.2113 0.0099  0.0299  0.0231  358 GLU B CA  
7106 C C   . GLU B 358 ? 0.1831 0.0853 0.2120 0.0080  0.0392  0.0210  358 GLU B C   
7107 O O   . GLU B 358 ? 0.1654 0.0666 0.1982 0.0080  0.0423  0.0238  358 GLU B O   
7108 C CB  . GLU B 358 ? 0.2334 0.1566 0.2572 0.0188  0.0268  0.0273  358 GLU B CB  
7109 C CG  . GLU B 358 ? 0.2452 0.1693 0.2665 0.0225  0.0272  0.0258  358 GLU B CG  
7110 C CD  . GLU B 358 ? 0.2990 0.2349 0.3174 0.0277  0.0217  0.0282  358 GLU B CD  
7111 O OE1 . GLU B 358 ? 0.2490 0.1877 0.2687 0.0316  0.0241  0.0313  358 GLU B OE1 
7112 O OE2 . GLU B 358 ? 0.2206 0.1627 0.2353 0.0268  0.0149  0.0269  358 GLU B OE2 
7113 N N   . TYR B 359 ? 0.1638 0.0583 0.1912 0.0065  0.0443  0.0161  359 TYR B N   
7114 C CA  . TYR B 359 ? 0.1801 0.0643 0.2103 0.0048  0.0538  0.0136  359 TYR B CA  
7115 C C   . TYR B 359 ? 0.1936 0.0688 0.2228 -0.0074 0.0569  0.0061  359 TYR B C   
7116 O O   . TYR B 359 ? 0.2076 0.0737 0.2387 -0.0098 0.0651  0.0033  359 TYR B O   
7117 C CB  . TYR B 359 ? 0.1857 0.0669 0.2156 0.0097  0.0589  0.0121  359 TYR B CB  
7118 C CG  . TYR B 359 ? 0.2388 0.1305 0.2695 0.0199  0.0551  0.0190  359 TYR B CG  
7119 C CD1 . TYR B 359 ? 0.3318 0.2249 0.3658 0.0254  0.0580  0.0249  359 TYR B CD1 
7120 C CD2 . TYR B 359 ? 0.2520 0.1525 0.2792 0.0226  0.0482  0.0193  359 TYR B CD2 
7121 C CE1 . TYR B 359 ? 0.3014 0.2047 0.3346 0.0325  0.0536  0.0302  359 TYR B CE1 
7122 C CE2 . TYR B 359 ? 0.2782 0.1893 0.3053 0.0297  0.0441  0.0243  359 TYR B CE2 
7123 C CZ  . TYR B 359 ? 0.2873 0.1998 0.3171 0.0341  0.0465  0.0294  359 TYR B CZ  
7124 O OH  . TYR B 359 ? 0.3956 0.3181 0.4242 0.0394  0.0420  0.0334  359 TYR B OH  
7125 N N   . TYR B 360 ? 0.1873 0.0658 0.2132 -0.0158 0.0504  0.0026  360 TYR B N   
7126 C CA  . TYR B 360 ? 0.1982 0.0731 0.2222 -0.0295 0.0507  -0.0048 360 TYR B CA  
7127 C C   . TYR B 360 ? 0.1970 0.0757 0.2266 -0.0337 0.0483  -0.0013 360 TYR B C   
7128 O O   . TYR B 360 ? 0.1840 0.0703 0.2173 -0.0283 0.0434  0.0059  360 TYR B O   
7129 C CB  . TYR B 360 ? 0.1935 0.0741 0.2110 -0.0380 0.0430  -0.0097 360 TYR B CB  
7130 C CG  . TYR B 360 ? 0.1986 0.0757 0.2087 -0.0390 0.0453  -0.0162 360 TYR B CG  
7131 C CD1 . TYR B 360 ? 0.1911 0.0682 0.2009 -0.0284 0.0466  -0.0131 360 TYR B CD1 
7132 C CD2 . TYR B 360 ? 0.2105 0.0870 0.2135 -0.0508 0.0454  -0.0251 360 TYR B CD2 
7133 C CE1 . TYR B 360 ? 0.1958 0.0706 0.1996 -0.0298 0.0492  -0.0191 360 TYR B CE1 
7134 C CE2 . TYR B 360 ? 0.2192 0.0936 0.2147 -0.0519 0.0480  -0.0311 360 TYR B CE2 
7135 C CZ  . TYR B 360 ? 0.2172 0.0903 0.2135 -0.0418 0.0502  -0.0282 360 TYR B CZ  
7136 O OH  . TYR B 360 ? 0.2359 0.1075 0.2254 -0.0439 0.0534  -0.0345 360 TYR B OH  
7137 N N   . GLU B 361 ? 0.2144 0.1115 0.2189 -0.0086 0.0683  -0.0264 361 GLU B N   
7138 C CA  . GLU B 361 ? 0.2333 0.1322 0.2478 -0.0165 0.0712  -0.0315 361 GLU B CA  
7139 C C   . GLU B 361 ? 0.2042 0.1159 0.2363 -0.0164 0.0593  -0.0341 361 GLU B C   
7140 O O   . GLU B 361 ? 0.2316 0.1475 0.2636 -0.0197 0.0505  -0.0346 361 GLU B O   
7141 C CB  . GLU B 361 ? 0.3989 0.2897 0.4044 -0.0342 0.0788  -0.0384 361 GLU B CB  
7142 C CG  . GLU B 361 ? 0.6438 0.5200 0.6343 -0.0340 0.0923  -0.0367 361 GLU B CG  
7143 C CD  . GLU B 361 ? 0.8096 0.6835 0.8034 -0.0272 0.0995  -0.0326 361 GLU B CD  
7144 O OE1 . GLU B 361 ? 0.8586 0.7396 0.8649 -0.0313 0.0990  -0.0359 361 GLU B OE1 
7145 O OE2 . GLU B 361 ? 0.8086 0.6750 0.7934 -0.0185 0.1050  -0.0257 361 GLU B OE2 
7146 N N   . GLU B 362 ? 0.1810 0.1073 0.2282 -0.0116 0.0564  -0.0331 362 GLU B N   
7147 C CA  . GLU B 362 ? 0.1930 0.1451 0.2577 -0.0088 0.0409  -0.0314 362 GLU B CA  
7148 C C   . GLU B 362 ? 0.2017 0.1542 0.2674 0.0013  0.0308  -0.0276 362 GLU B C   
7149 O O   . GLU B 362 ? 0.1672 0.1333 0.2398 -0.0011 0.0182  -0.0263 362 GLU B O   
7150 C CB  . GLU B 362 ? 0.2154 0.1840 0.2844 -0.0249 0.0345  -0.0349 362 GLU B CB  
7151 C CG  . GLU B 362 ? 0.4041 0.3757 0.4729 -0.0384 0.0439  -0.0399 362 GLU B CG  
7152 C CD  . GLU B 362 ? 0.5464 0.5425 0.6230 -0.0530 0.0349  -0.0435 362 GLU B CD  
7153 O OE1 . GLU B 362 ? 0.5857 0.5985 0.6704 -0.0491 0.0203  -0.0403 362 GLU B OE1 
7154 O OE2 . GLU B 362 ? 0.6619 0.6603 0.7355 -0.0686 0.0425  -0.0493 362 GLU B OE2 
7155 N N   . ASN B 363 ? 0.1889 0.1302 0.2454 0.0120  0.0350  -0.0245 363 ASN B N   
7156 C CA  . ASN B 363 ? 0.1065 0.0552 0.1590 0.0199  0.0239  -0.0194 363 ASN B CA  
7157 C C   . ASN B 363 ? 0.1598 0.1013 0.2113 0.0138  0.0204  -0.0214 363 ASN B C   
7158 O O   . ASN B 363 ? 0.1263 0.0743 0.1831 0.0174  0.0103  -0.0188 363 ASN B O   
7159 C CB  . ASN B 363 ? 0.1636 0.1285 0.2279 0.0266  0.0141  -0.0170 363 ASN B CB  
7160 C CG  . ASN B 363 ? 0.1646 0.1327 0.2142 0.0320  0.0078  -0.0124 363 ASN B CG  
7161 O OD1 . ASN B 363 ? 0.1762 0.1397 0.2106 0.0342  0.0095  -0.0116 363 ASN B OD1 
7162 N ND2 . ASN B 363 ? 0.1976 0.1744 0.2555 0.0330  0.0005  -0.0107 363 ASN B ND2 
7163 N N   . GLY B 364 ? 0.1563 0.0845 0.1974 0.0027  0.0284  -0.0256 364 GLY B N   
7164 C CA  . GLY B 364 ? 0.1648 0.0902 0.1973 -0.0056 0.0239  -0.0262 364 GLY B CA  
7165 C C   . GLY B 364 ? 0.2002 0.1422 0.2384 -0.0160 0.0120  -0.0255 364 GLY B C   
7166 O O   . GLY B 364 ? 0.1588 0.1006 0.1888 -0.0236 0.0074  -0.0253 364 GLY B O   
7167 N N   . ILE B 365 ? 0.1550 0.1129 0.2068 -0.0162 0.0069  -0.0250 365 ILE B N   
7168 C CA  . ILE B 365 ? 0.1333 0.1108 0.1927 -0.0227 -0.0061 -0.0231 365 ILE B CA  
7169 C C   . ILE B 365 ? 0.1811 0.1607 0.2299 -0.0407 -0.0038 -0.0279 365 ILE B C   
7170 O O   . ILE B 365 ? 0.1970 0.1840 0.2414 -0.0473 -0.0127 -0.0260 365 ILE B O   
7171 C CB  . ILE B 365 ? 0.1461 0.1422 0.2242 -0.0161 -0.0118 -0.0217 365 ILE B CB  
7172 C CG1 . ILE B 365 ? 0.1542 0.1482 0.2415 0.0010  -0.0160 -0.0175 365 ILE B CG1 
7173 C CG2 . ILE B 365 ? 0.1791 0.1979 0.2652 -0.0225 -0.0245 -0.0198 365 ILE B CG2 
7174 C CD1 . ILE B 365 ? 0.1710 0.1786 0.2748 0.0094  -0.0169 -0.0178 365 ILE B CD1 
7175 N N   . PRO B 366 ? 0.1635 0.1357 0.2062 -0.0500 0.0084  -0.0342 366 PRO B N   
7176 C CA  . PRO B 366 ? 0.2240 0.1958 0.2542 -0.0684 0.0114  -0.0402 366 PRO B CA  
7177 C C   . PRO B 366 ? 0.1845 0.1417 0.1984 -0.0715 0.0127  -0.0406 366 PRO B C   
7178 O O   . PRO B 366 ? 0.1899 0.1562 0.1970 -0.0836 0.0068  -0.0423 366 PRO B O   
7179 C CB  . PRO B 366 ? 0.1865 0.1445 0.2112 -0.0755 0.0273  -0.0468 366 PRO B CB  
7180 C CG  . PRO B 366 ? 0.2362 0.2022 0.2764 -0.0641 0.0274  -0.0437 366 PRO B CG  
7181 C CD  . PRO B 366 ? 0.1636 0.1309 0.2114 -0.0461 0.0189  -0.0364 366 PRO B CD  
7182 N N   . PHE B 367 ? 0.2181 0.1551 0.2253 -0.0608 0.0205  -0.0393 367 PHE B N   
7183 C CA  . PHE B 367 ? 0.1793 0.1036 0.1713 -0.0635 0.0231  -0.0404 367 PHE B CA  
7184 C C   . PHE B 367 ? 0.2013 0.1391 0.1960 -0.0621 0.0085  -0.0343 367 PHE B C   
7185 O O   . PHE B 367 ? 0.2089 0.1499 0.1931 -0.0733 0.0051  -0.0358 367 PHE B O   
7186 C CB  . PHE B 367 ? 0.2013 0.1082 0.1880 -0.0489 0.0331  -0.0386 367 PHE B CB  
7187 C CG  . PHE B 367 ? 0.2406 0.1424 0.2162 -0.0472 0.0335  -0.0377 367 PHE B CG  
7188 C CD1 . PHE B 367 ? 0.2737 0.1703 0.2350 -0.0547 0.0407  -0.0415 367 PHE B CD1 
7189 C CD2 . PHE B 367 ? 0.2243 0.1268 0.2040 -0.0388 0.0272  -0.0337 367 PHE B CD2 
7190 C CE1 . PHE B 367 ? 0.2936 0.1866 0.2453 -0.0539 0.0420  -0.0414 367 PHE B CE1 
7191 C CE2 . PHE B 367 ? 0.2645 0.1637 0.2343 -0.0387 0.0283  -0.0335 367 PHE B CE2 
7192 C CZ  . PHE B 367 ? 0.2887 0.1835 0.2447 -0.0462 0.0358  -0.0374 367 PHE B CZ  
7193 N N   . LEU B 368 ? 0.1711 0.1162 0.1791 -0.0488 0.0000  -0.0275 368 LEU B N   
7194 C CA  . LEU B 368 ? 0.1624 0.1154 0.1715 -0.0468 -0.0125 -0.0211 368 LEU B CA  
7195 C C   . LEU B 368 ? 0.1559 0.1279 0.1675 -0.0566 -0.0241 -0.0189 368 LEU B C   
7196 O O   . LEU B 368 ? 0.1623 0.1381 0.1656 -0.0625 -0.0312 -0.0156 368 LEU B O   
7197 C CB  . LEU B 368 ? 0.1587 0.1131 0.1810 -0.0311 -0.0181 -0.0153 368 LEU B CB  
7198 C CG  . LEU B 368 ? 0.1514 0.0911 0.1695 -0.0216 -0.0097 -0.0161 368 LEU B CG  
7199 C CD1 . LEU B 368 ? 0.1648 0.1077 0.1961 -0.0077 -0.0158 -0.0116 368 LEU B CD1 
7200 C CD2 . LEU B 368 ? 0.1685 0.1007 0.1718 -0.0277 -0.0079 -0.0166 368 LEU B CD2 
7201 N N   . GLU B 369 ? 0.1537 0.1400 0.1766 -0.0584 -0.0264 -0.0203 369 GLU B N   
7202 C CA  . GLU B 369 ? 0.1593 0.1677 0.1848 -0.0674 -0.0378 -0.0184 369 GLU B CA  
7203 C C   . GLU B 369 ? 0.1983 0.2066 0.2067 -0.0852 -0.0342 -0.0244 369 GLU B C   
7204 O O   . GLU B 369 ? 0.2137 0.2351 0.2168 -0.0921 -0.0442 -0.0210 369 GLU B O   
7205 C CB  . GLU B 369 ? 0.2067 0.2337 0.2486 -0.0663 -0.0402 -0.0199 369 GLU B CB  
7206 C CG  . GLU B 369 ? 0.1509 0.1830 0.2103 -0.0486 -0.0471 -0.0132 369 GLU B CG  
7207 C CD  . GLU B 369 ? 0.2314 0.2851 0.3081 -0.0467 -0.0499 -0.0147 369 GLU B CD  
7208 O OE1 . GLU B 369 ? 0.2225 0.2858 0.2981 -0.0595 -0.0447 -0.0215 369 GLU B OE1 
7209 O OE2 . GLU B 369 ? 0.2352 0.2964 0.3268 -0.0328 -0.0569 -0.0096 369 GLU B OE2 
7210 N N   . LYS B 370 ? 0.2045 0.1976 0.2033 -0.0929 -0.0196 -0.0334 370 LYS B N   
7211 C CA  . LYS B 370 ? 0.2165 0.2072 0.1985 -0.1070 -0.0142 -0.0396 370 LYS B CA  
7212 C C   . LYS B 370 ? 0.2382 0.2188 0.2064 -0.1063 -0.0149 -0.0369 370 LYS B C   
7213 O O   . LYS B 370 ? 0.2429 0.2324 0.2009 -0.1145 -0.0184 -0.0368 370 LYS B O   
7214 C CB  . LYS B 370 ? 0.2585 0.2326 0.2338 -0.1088 0.0027  -0.0472 370 LYS B CB  
7215 C CG  . LYS B 370 ? 0.3467 0.3194 0.3057 -0.1198 0.0092  -0.0529 370 LYS B CG  
7216 C CD  . LYS B 370 ? 0.5442 0.5415 0.5068 -0.1310 0.0018  -0.0547 370 LYS B CD  
7217 C CE  . LYS B 370 ? 0.6871 0.6829 0.6332 -0.1430 0.0094  -0.0614 370 LYS B CE  
7218 N NZ  . LYS B 370 ? 0.7345 0.7561 0.6836 -0.1540 0.0023  -0.0634 370 LYS B NZ  
7219 N N   . LEU B 371 ? 0.2152 0.1787 0.1829 -0.0967 -0.0112 -0.0346 371 LEU B N   
7220 C CA  . LEU B 371 ? 0.2025 0.1575 0.1581 -0.0957 -0.0109 -0.0323 371 LEU B CA  
7221 C C   . LEU B 371 ? 0.2547 0.2247 0.2110 -0.0972 -0.0265 -0.0235 371 LEU B C   
7222 O O   . LEU B 371 ? 0.2789 0.2524 0.2219 -0.1057 -0.0284 -0.0231 371 LEU B O   
7223 C CB  . LEU B 371 ? 0.1924 0.1308 0.1508 -0.0815 -0.0040 -0.0308 371 LEU B CB  
7224 C CG  . LEU B 371 ? 0.2432 0.1753 0.1913 -0.0803 -0.0037 -0.0285 371 LEU B CG  
7225 C CD1 . LEU B 371 ? 0.2800 0.2057 0.2115 -0.0883 0.0072  -0.0354 371 LEU B CD1 
7226 C CD2 . LEU B 371 ? 0.2566 0.1794 0.2116 -0.0648 0.0004  -0.0259 371 LEU B CD2 
7227 N N   . TYR B 372 ? 0.2194 0.1978 0.1913 -0.0857 -0.0365 -0.0152 372 TYR B N   
7228 C CA  . TYR B 372 ? 0.1922 0.1818 0.1652 -0.0841 -0.0510 -0.0051 372 TYR B CA  
7229 C C   . TYR B 372 ? 0.2330 0.2433 0.2017 -0.0963 -0.0598 -0.0044 372 TYR B C   
7230 O O   . TYR B 372 ? 0.2340 0.2505 0.1925 -0.1016 -0.0679 0.0015  372 TYR B O   
7231 C CB  . TYR B 372 ? 0.1759 0.1681 0.1670 -0.0685 -0.0584 0.0023  372 TYR B CB  
7232 C CG  . TYR B 372 ? 0.2261 0.2012 0.2210 -0.0568 -0.0518 0.0024  372 TYR B CG  
7233 C CD1 . TYR B 372 ? 0.1859 0.1470 0.1681 -0.0594 -0.0432 -0.0006 372 TYR B CD1 
7234 C CD2 . TYR B 372 ? 0.2056 0.1808 0.2170 -0.0431 -0.0542 0.0050  372 TYR B CD2 
7235 C CE1 . TYR B 372 ? 0.1968 0.1464 0.1833 -0.0486 -0.0378 -0.0008 372 TYR B CE1 
7236 C CE2 . TYR B 372 ? 0.1598 0.1222 0.1744 -0.0331 -0.0487 0.0045  372 TYR B CE2 
7237 C CZ  . TYR B 372 ? 0.1707 0.1213 0.1731 -0.0359 -0.0408 0.0017  372 TYR B CZ  
7238 O OH  . TYR B 372 ? 0.1885 0.1305 0.1950 -0.0260 -0.0360 0.0009  372 TYR B OH  
7239 N N   . SER B 373 ? 0.2426 0.2653 0.2187 -0.1013 -0.0585 -0.0103 373 SER B N   
7240 C CA  . SER B 373 ? 0.2860 0.3311 0.2596 -0.1098 -0.0649 -0.0103 373 SER B CA  
7241 C C   . SER B 373 ? 0.3013 0.3416 0.2553 -0.1214 -0.0567 -0.0160 373 SER B C   
7242 O O   . SER B 373 ? 0.2988 0.3532 0.2453 -0.1268 -0.0635 -0.0121 373 SER B O   
7243 C CB  . SER B 373 ? 0.3375 0.3975 0.3246 -0.1113 -0.0632 -0.0160 373 SER B CB  
7244 O OG  . SER B 373 ? 0.3894 0.4360 0.3704 -0.1184 -0.0476 -0.0271 373 SER B OG  
7245 N N   . THR B 374 ? 0.2668 0.2871 0.2123 -0.1241 -0.0417 -0.0246 374 THR B N   
7246 C CA  . THR B 374 ? 0.2954 0.3102 0.2227 -0.1336 -0.0333 -0.0299 374 THR B CA  
7247 C C   . THR B 374 ? 0.3516 0.3627 0.2675 -0.1335 -0.0379 -0.0232 374 THR B C   
7248 O O   . THR B 374 ? 0.3170 0.3365 0.2205 -0.1422 -0.0393 -0.0227 374 THR B O   
7249 C CB  . THR B 374 ? 0.3219 0.3156 0.2437 -0.1333 -0.0160 -0.0394 374 THR B CB  
7250 O OG1 . THR B 374 ? 0.2533 0.2500 0.1833 -0.1352 -0.0112 -0.0451 374 THR B OG1 
7251 C CG2 . THR B 374 ? 0.3515 0.3395 0.2549 -0.1423 -0.0070 -0.0449 374 THR B CG2 
7252 N N   . LEU B 375 ? 0.3097 0.3089 0.2297 -0.1245 -0.0400 -0.0180 375 LEU B N   
7253 C CA  . LEU B 375 ? 0.3177 0.3130 0.2271 -0.1250 -0.0442 -0.0111 375 LEU B CA  
7254 C C   . LEU B 375 ? 0.3516 0.3644 0.2598 -0.1272 -0.0593 -0.0003 375 LEU B C   
7255 O O   . LEU B 375 ? 0.3784 0.3927 0.2730 -0.1330 -0.0611 0.0040  375 LEU B O   
7256 C CB  . LEU B 375 ? 0.2710 0.2512 0.1869 -0.1149 -0.0442 -0.0076 375 LEU B CB  
7257 C CG  . LEU B 375 ? 0.3000 0.2623 0.2138 -0.1109 -0.0284 -0.0165 375 LEU B CG  
7258 C CD1 . LEU B 375 ? 0.2824 0.2347 0.2076 -0.0973 -0.0290 -0.0120 375 LEU B CD1 
7259 C CD2 . LEU B 375 ? 0.3449 0.3021 0.2415 -0.1173 -0.0196 -0.0205 375 LEU B CD2 
7260 N N   . GLU B 376 ? 0.3555 0.3823 0.2782 -0.1218 -0.0696 0.0047  376 GLU B N   
7261 C CA  . GLU B 376 ? 0.3882 0.4321 0.3112 -0.1207 -0.0832 0.0156  376 GLU B CA  
7262 C C   . GLU B 376 ? 0.4654 0.5222 0.3745 -0.1328 -0.0817 0.0129  376 GLU B C   
7263 O O   . GLU B 376 ? 0.5087 0.5750 0.4116 -0.1335 -0.0904 0.0224  376 GLU B O   
7264 C CB  . GLU B 376 ? 0.3599 0.4195 0.3021 -0.1121 -0.0918 0.0186  376 GLU B CB  
7265 C CG  . GLU B 376 ? 0.4362 0.4891 0.3925 -0.0972 -0.0997 0.0279  376 GLU B CG  
7266 C CD  . GLU B 376 ? 0.5270 0.5972 0.5028 -0.0879 -0.1062 0.0295  376 GLU B CD  
7267 O OE1 . GLU B 376 ? 0.5472 0.6315 0.5272 -0.0943 -0.1022 0.0206  376 GLU B OE1 
7268 O OE2 . GLU B 376 ? 0.5739 0.6435 0.5605 -0.0741 -0.1142 0.0390  376 GLU B OE2 
7269 N N   . LYS B 377 ? 0.3864 0.4426 0.2902 -0.1418 -0.0701 0.0005  377 LYS B N   
7270 C CA  . LYS B 377 ? 0.4401 0.5113 0.3336 -0.1535 -0.0688 -0.0034 377 LYS B CA  
7271 C C   . LYS B 377 ? 0.4951 0.5553 0.3698 -0.1630 -0.0584 -0.0086 377 LYS B C   
7272 O O   . LYS B 377 ? 0.5744 0.6450 0.4396 -0.1738 -0.0552 -0.0136 377 LYS B O   
7273 C CB  . LYS B 377 ? 0.4342 0.5146 0.3351 -0.1580 -0.0634 -0.0137 377 LYS B CB  
7274 C CG  . LYS B 377 ? 0.4998 0.5983 0.4191 -0.1508 -0.0738 -0.0097 377 LYS B CG  
7275 C CD  . LYS B 377 ? 0.6661 0.7750 0.5893 -0.1590 -0.0671 -0.0206 377 LYS B CD  
7276 C CE  . LYS B 377 ? 0.7617 0.8927 0.7034 -0.1530 -0.0767 -0.0177 377 LYS B CE  
7277 N NZ  . LYS B 377 ? 0.8010 0.9445 0.7442 -0.1636 -0.0703 -0.0283 377 LYS B NZ  
7278 N N   . GLU B 378 ? 0.4184 0.4588 0.2880 -0.1594 -0.0525 -0.0082 378 GLU B N   
7279 C CA  . GLU B 378 ? 0.4614 0.4927 0.3145 -0.1672 -0.0421 -0.0131 378 GLU B CA  
7280 C C   . GLU B 378 ? 0.4901 0.5253 0.3342 -0.1689 -0.0505 -0.0019 378 GLU B C   
7281 O O   . GLU B 378 ? 0.5018 0.5276 0.3488 -0.1616 -0.0552 0.0059  378 GLU B O   
7282 C CB  . GLU B 378 ? 0.5020 0.5113 0.3550 -0.1620 -0.0293 -0.0203 378 GLU B CB  
7283 C CG  . GLU B 378 ? 0.5010 0.5022 0.3631 -0.1582 -0.0202 -0.0298 378 GLU B CG  
7284 C CD  . GLU B 378 ? 0.6285 0.6318 0.4830 -0.1683 -0.0100 -0.0402 378 GLU B CD  
7285 O OE1 . GLU B 378 ? 0.6106 0.6185 0.4517 -0.1780 -0.0069 -0.0423 378 GLU B OE1 
7286 O OE2 . GLU B 378 ? 0.6455 0.6446 0.5074 -0.1666 -0.0042 -0.0465 378 GLU B OE2 
7287 N N   . GLU B 379 ? 0.4611 0.5100 0.2943 -0.1791 -0.0522 -0.0011 379 GLU B N   
7288 C CA  . GLU B 379 ? 0.4460 0.4984 0.2689 -0.1822 -0.0587 0.0093  379 GLU B CA  
7289 C C   . GLU B 379 ? 0.4208 0.4562 0.2349 -0.1832 -0.0499 0.0079  379 GLU B C   
7290 O O   . GLU B 379 ? 0.4302 0.4622 0.2400 -0.1820 -0.0556 0.0180  379 GLU B O   
7291 C CB  . GLU B 379 ? 0.5092 0.5793 0.3213 -0.1940 -0.0595 0.0079  379 GLU B CB  
7292 C CG  . GLU B 379 ? 0.6333 0.7185 0.4438 -0.1929 -0.0737 0.0214  379 GLU B CG  
7293 C CD  . GLU B 379 ? 0.7837 0.8895 0.5850 -0.2041 -0.0747 0.0187  379 GLU B CD  
7294 O OE1 . GLU B 379 ? 0.8426 0.9479 0.6301 -0.2135 -0.0693 0.0168  379 GLU B OE1 
7295 O OE2 . GLU B 379 ? 0.7956 0.9190 0.6039 -0.2038 -0.0806 0.0176  379 GLU B OE2 
7296 N N   . TRP B 380 ? 0.3994 0.4247 0.2103 -0.1859 -0.0355 -0.0046 380 TRP B N   
7297 C CA  . TRP B 380 ? 0.3516 0.3646 0.1539 -0.1877 -0.0255 -0.0081 380 TRP B CA  
7298 C C   . TRP B 380 ? 0.3339 0.3311 0.1440 -0.1767 -0.0231 -0.0074 380 TRP B C   
7299 O O   . TRP B 380 ? 0.4098 0.3984 0.2149 -0.1768 -0.0151 -0.0101 380 TRP B O   
7300 C CB  . TRP B 380 ? 0.3892 0.3992 0.1851 -0.1946 -0.0106 -0.0219 380 TRP B CB  
7301 C CG  . TRP B 380 ? 0.4220 0.4243 0.2267 -0.1892 -0.0038 -0.0309 380 TRP B CG  
7302 C CD1 . TRP B 380 ? 0.4181 0.4295 0.2283 -0.1912 -0.0071 -0.0335 380 TRP B CD1 
7303 C CD2 . TRP B 380 ? 0.4563 0.4411 0.2661 -0.1807 0.0074  -0.0380 380 TRP B CD2 
7304 N NE1 . TRP B 380 ? 0.4245 0.4234 0.2422 -0.1853 0.0019  -0.0417 380 TRP B NE1 
7305 C CE2 . TRP B 380 ? 0.4480 0.4300 0.2655 -0.1782 0.0108  -0.0442 380 TRP B CE2 
7306 C CE3 . TRP B 380 ? 0.3892 0.3613 0.1982 -0.1749 0.0152  -0.0398 380 TRP B CE3 
7307 C CZ2 . TRP B 380 ? 0.4552 0.4207 0.2789 -0.1696 0.0216  -0.0509 380 TRP B CZ2 
7308 C CZ3 . TRP B 380 ? 0.4318 0.3892 0.2478 -0.1655 0.0256  -0.0469 380 TRP B CZ3 
7309 C CH2 . TRP B 380 ? 0.3942 0.3475 0.2171 -0.1628 0.0287  -0.0518 380 TRP B CH2 
7310 N N   . ILE B 381 ? 0.3192 0.3142 0.1426 -0.1673 -0.0297 -0.0044 381 ILE B N   
7311 C CA  . ILE B 381 ? 0.3711 0.3534 0.2034 -0.1566 -0.0302 -0.0023 381 ILE B CA  
7312 C C   . ILE B 381 ? 0.3431 0.3290 0.1802 -0.1528 -0.0457 0.0119  381 ILE B C   
7313 O O   . ILE B 381 ? 0.4159 0.4127 0.2594 -0.1515 -0.0558 0.0174  381 ILE B O   
7314 C CB  . ILE B 381 ? 0.2885 0.2639 0.1343 -0.1480 -0.0250 -0.0101 381 ILE B CB  
7315 C CG1 . ILE B 381 ? 0.3869 0.3554 0.2275 -0.1504 -0.0089 -0.0230 381 ILE B CG1 
7316 C CG2 . ILE B 381 ? 0.2731 0.2372 0.1302 -0.1366 -0.0265 -0.0072 381 ILE B CG2 
7317 C CD1 . ILE B 381 ? 0.3485 0.3111 0.2006 -0.1438 -0.0037 -0.0298 381 ILE B CD1 
7318 N N   . GLU B 382 ? 0.3291 0.3061 0.1635 -0.1507 -0.0473 0.0178  382 GLU B N   
7319 C CA  . GLU B 382 ? 0.3641 0.3391 0.2038 -0.1451 -0.0608 0.0313  382 GLU B CA  
7320 C C   . GLU B 382 ? 0.3498 0.3115 0.2023 -0.1344 -0.0576 0.0296  382 GLU B C   
7321 O O   . GLU B 382 ? 0.3107 0.2652 0.1596 -0.1349 -0.0483 0.0255  382 GLU B O   
7322 C CB  . GLU B 382 ? 0.3868 0.3625 0.2134 -0.1519 -0.0649 0.0418  382 GLU B CB  
7323 C CG  . GLU B 382 ? 0.5125 0.4819 0.3445 -0.1444 -0.0768 0.0567  382 GLU B CG  
7324 C CD  . GLU B 382 ? 0.7147 0.6835 0.5357 -0.1507 -0.0794 0.0664  382 GLU B CD  
7325 O OE1 . GLU B 382 ? 0.7733 0.7489 0.5822 -0.1616 -0.0730 0.0617  382 GLU B OE1 
7326 O OE2 . GLU B 382 ? 0.7837 0.7446 0.6091 -0.1442 -0.0870 0.0781  382 GLU B OE2 
7327 N N   . THR B 383 ? 0.3458 0.3065 0.2164 -0.1227 -0.0629 0.0322  383 THR B N   
7328 C CA  . THR B 383 ? 0.3075 0.2570 0.1932 -0.1102 -0.0593 0.0318  383 THR B CA  
7329 C C   . THR B 383 ? 0.2678 0.2100 0.1521 -0.1084 -0.0658 0.0435  383 THR B C   
7330 O O   . THR B 383 ? 0.3236 0.2683 0.2018 -0.1110 -0.0765 0.0547  383 THR B O   
7331 C CB  . THR B 383 ? 0.2856 0.2366 0.1904 -0.0987 -0.0624 0.0304  383 THR B CB  
7332 O OG1 . THR B 383 ? 0.2946 0.2540 0.2027 -0.0973 -0.0758 0.0401  383 THR B OG1 
7333 C CG2 . THR B 383 ? 0.2602 0.2143 0.1665 -0.1007 -0.0531 0.0179  383 THR B CG2 
7334 N N   . LEU B 384 ? 0.3048 0.2379 0.1937 -0.1043 -0.0590 0.0410  384 LEU B N   
7335 C CA  . LEU B 384 ? 0.2594 0.1834 0.1455 -0.1050 -0.0627 0.0503  384 LEU B CA  
7336 C C   . LEU B 384 ? 0.2462 0.1613 0.1500 -0.0927 -0.0630 0.0503  384 LEU B C   
7337 O O   . LEU B 384 ? 0.2288 0.1454 0.1447 -0.0848 -0.0565 0.0411  384 LEU B O   
7338 C CB  . LEU B 384 ? 0.2674 0.1910 0.1399 -0.1154 -0.0538 0.0470  384 LEU B CB  
7339 C CG  . LEU B 384 ? 0.3404 0.2723 0.1928 -0.1292 -0.0514 0.0459  384 LEU B CG  
7340 C CD1 . LEU B 384 ? 0.3161 0.2474 0.1587 -0.1373 -0.0423 0.0430  384 LEU B CD1 
7341 C CD2 . LEU B 384 ? 0.3321 0.2659 0.1733 -0.1348 -0.0636 0.0590  384 LEU B CD2 
7342 N N   . THR B 385 ? 0.2737 0.1785 0.1778 -0.0913 -0.0700 0.0607  385 THR B N   
7343 C CA  . THR B 385 ? 0.2489 0.1438 0.1660 -0.0831 -0.0682 0.0593  385 THR B CA  
7344 C C   . THR B 385 ? 0.2513 0.1455 0.1630 -0.0904 -0.0585 0.0536  385 THR B C   
7345 O O   . THR B 385 ? 0.2586 0.1577 0.1556 -0.1017 -0.0542 0.0531  385 THR B O   
7346 C CB  . THR B 385 ? 0.3171 0.2011 0.2368 -0.0783 -0.0771 0.0700  385 THR B CB  
7347 O OG1 . THR B 385 ? 0.3762 0.2568 0.2812 -0.0880 -0.0769 0.0757  385 THR B OG1 
7348 C CG2 . THR B 385 ? 0.3609 0.2490 0.2852 -0.0715 -0.0873 0.0766  385 THR B CG2 
7349 N N   . LEU B 386 ? 0.2509 0.1417 0.1752 -0.0837 -0.0546 0.0484  386 LEU B N   
7350 C CA  . LEU B 386 ? 0.2807 0.1754 0.2020 -0.0897 -0.0455 0.0422  386 LEU B CA  
7351 C C   . LEU B 386 ? 0.3372 0.2276 0.2453 -0.0996 -0.0465 0.0492  386 LEU B C   
7352 O O   . LEU B 386 ? 0.2923 0.1899 0.1901 -0.1093 -0.0397 0.0459  386 LEU B O   
7353 C CB  . LEU B 386 ? 0.2432 0.1367 0.1803 -0.0811 -0.0425 0.0358  386 LEU B CB  
7354 C CG  . LEU B 386 ? 0.2424 0.1433 0.1928 -0.0693 -0.0398 0.0275  386 LEU B CG  
7355 C CD1 . LEU B 386 ? 0.2101 0.1109 0.1747 -0.0615 -0.0378 0.0218  386 LEU B CD1 
7356 C CD2 . LEU B 386 ? 0.2389 0.1531 0.1842 -0.0707 -0.0306 0.0192  386 LEU B CD2 
7357 N N   . GLU B 387 ? 0.3607 0.2397 0.2691 -0.0966 -0.0542 0.0581  387 GLU B N   
7358 C CA  . GLU B 387 ? 0.3950 0.2680 0.2901 -0.1057 -0.0551 0.0653  387 GLU B CA  
7359 C C   . GLU B 387 ? 0.3840 0.2647 0.2619 -0.1161 -0.0556 0.0685  387 GLU B C   
7360 O O   . GLU B 387 ? 0.3574 0.2409 0.2235 -0.1265 -0.0509 0.0684  387 GLU B O   
7361 C CB  . GLU B 387 ? 0.5481 0.4067 0.4454 -0.0996 -0.0631 0.0750  387 GLU B CB  
7362 C CG  . GLU B 387 ? 0.7598 0.6115 0.6745 -0.0869 -0.0647 0.0724  387 GLU B CG  
7363 C CD  . GLU B 387 ? 0.9745 0.8165 0.8923 -0.0889 -0.0591 0.0696  387 GLU B CD  
7364 O OE1 . GLU B 387 ? 1.0403 0.8825 0.9478 -0.1004 -0.0538 0.0694  387 GLU B OE1 
7365 O OE2 . GLU B 387 ? 1.0050 0.8399 0.9354 -0.0795 -0.0596 0.0673  387 GLU B OE2 
7366 N N   . GLU B 388 ? 0.3572 0.2423 0.2335 -0.1139 -0.0612 0.0712  388 GLU B N   
7367 C CA  . GLU B 388 ? 0.3563 0.2500 0.2158 -0.1243 -0.0620 0.0736  388 GLU B CA  
7368 C C   . GLU B 388 ? 0.3955 0.3005 0.2484 -0.1324 -0.0508 0.0629  388 GLU B C   
7369 O O   . GLU B 388 ? 0.3636 0.2743 0.2022 -0.1429 -0.0478 0.0629  388 GLU B O   
7370 C CB  . GLU B 388 ? 0.3484 0.2466 0.2091 -0.1204 -0.0699 0.0773  388 GLU B CB  
7371 C CG  . GLU B 388 ? 0.3963 0.2875 0.2617 -0.1127 -0.0808 0.0884  388 GLU B CG  
7372 C CD  . GLU B 388 ? 0.4611 0.3603 0.3323 -0.1063 -0.0887 0.0908  388 GLU B CD  
7373 O OE1 . GLU B 388 ? 0.3666 0.2729 0.2400 -0.1066 -0.0859 0.0837  388 GLU B OE1 
7374 O OE2 . GLU B 388 ? 0.4934 0.3926 0.3667 -0.1008 -0.0969 0.0995  388 GLU B OE2 
7375 N N   . ALA B 389 ? 0.3320 0.2407 0.1962 -0.1267 -0.0441 0.0532  389 ALA B N   
7376 C CA  . ALA B 389 ? 0.3434 0.2630 0.2034 -0.1318 -0.0324 0.0423  389 ALA B CA  
7377 C C   . ALA B 389 ? 0.3345 0.2566 0.1918 -0.1372 -0.0266 0.0406  389 ALA B C   
7378 O O   . ALA B 389 ? 0.3491 0.2809 0.1957 -0.1457 -0.0196 0.0358  389 ALA B O   
7379 C CB  . ALA B 389 ? 0.2947 0.2176 0.1696 -0.1221 -0.0265 0.0322  389 ALA B CB  
7380 N N   . MET B 390 ? 0.3290 0.2426 0.1957 -0.1330 -0.0294 0.0440  390 MET B N   
7381 C CA  . MET B 390 ? 0.3773 0.2931 0.2422 -0.1392 -0.0238 0.0420  390 MET B CA  
7382 C C   . MET B 390 ? 0.4164 0.3306 0.2642 -0.1504 -0.0256 0.0487  390 MET B C   
7383 O O   . MET B 390 ? 0.4269 0.3490 0.2683 -0.1589 -0.0187 0.0446  390 MET B O   
7384 C CB  . MET B 390 ? 0.3533 0.2586 0.2316 -0.1328 -0.0264 0.0437  390 MET B CB  
7385 C CG  . MET B 390 ? 0.5057 0.4110 0.3823 -0.1405 -0.0215 0.0424  390 MET B CG  
7386 S SD  . MET B 390 ? 0.5403 0.4353 0.4347 -0.1327 -0.0227 0.0405  390 MET B SD  
7387 C CE  . MET B 390 ? 0.6293 0.5042 0.5244 -0.1236 -0.0344 0.0521  390 MET B CE  
7388 N N   . ARG B 391 ? 0.3763 0.2824 0.2164 -0.1507 -0.0347 0.0585  391 ARG B N   
7389 C CA  . ARG B 391 ? 0.4692 0.3716 0.2944 -0.1601 -0.0378 0.0666  391 ARG B CA  
7390 C C   . ARG B 391 ? 0.4761 0.3878 0.2875 -0.1670 -0.0398 0.0677  391 ARG B C   
7391 O O   . ARG B 391 ? 0.4759 0.3867 0.2747 -0.1753 -0.0418 0.0740  391 ARG B O   
7392 C CB  . ARG B 391 ? 0.5124 0.3972 0.3402 -0.1548 -0.0467 0.0785  391 ARG B CB  
7393 C CG  . ARG B 391 ? 0.6032 0.4773 0.4398 -0.1526 -0.0431 0.0774  391 ARG B CG  
7394 C CD  . ARG B 391 ? 0.7385 0.5932 0.5762 -0.1476 -0.0500 0.0885  391 ARG B CD  
7395 N NE  . ARG B 391 ? 0.8442 0.6899 0.6983 -0.1381 -0.0493 0.0850  391 ARG B NE  
7396 C CZ  . ARG B 391 ? 0.9296 0.7640 0.7927 -0.1265 -0.0561 0.0902  391 ARG B CZ  
7397 N NH1 . ARG B 391 ? 0.9832 0.8150 0.8410 -0.1226 -0.0644 0.0997  391 ARG B NH1 
7398 N NH2 . ARG B 391 ? 0.9227 0.7502 0.8005 -0.1187 -0.0543 0.0854  391 ARG B NH2 
7399 N N   . LYS B 392 ? 0.4816 0.4020 0.2950 -0.1643 -0.0389 0.0617  392 LYS B N   
7400 C CA  . LYS B 392 ? 0.5560 0.4857 0.3569 -0.1717 -0.0403 0.0614  392 LYS B CA  
7401 C C   . LYS B 392 ? 0.5320 0.4713 0.3215 -0.1830 -0.0325 0.0559  392 LYS B C   
7402 O O   . LYS B 392 ? 0.4975 0.4437 0.2902 -0.1837 -0.0227 0.0458  392 LYS B O   
7403 C CB  . LYS B 392 ? 0.5965 0.5331 0.4012 -0.1679 -0.0378 0.0533  392 LYS B CB  
7404 C CG  . LYS B 392 ? 0.7135 0.6470 0.5216 -0.1626 -0.0481 0.0604  392 LYS B CG  
7405 C CD  . LYS B 392 ? 0.7629 0.7054 0.5591 -0.1709 -0.0526 0.0637  392 LYS B CD  
7406 C CE  . LYS B 392 ? 0.7640 0.7071 0.5650 -0.1648 -0.0632 0.0709  392 LYS B CE  
7407 N NZ  . LYS B 392 ? 0.8296 0.7598 0.6410 -0.1544 -0.0713 0.0815  392 LYS B NZ  
7408 N N   . GLU B 393 ? 0.5803 0.5213 0.3573 -0.1913 -0.0367 0.0626  393 GLU B N   
7409 C CA  . GLU B 393 ? 0.6008 0.5507 0.3674 -0.2023 -0.0297 0.0581  393 GLU B CA  
7410 C C   . GLU B 393 ? 0.5402 0.5045 0.3026 -0.2072 -0.0235 0.0473  393 GLU B C   
7411 O O   . GLU B 393 ? 0.5602 0.5337 0.3209 -0.2121 -0.0141 0.0378  393 GLU B O   
7412 C CB  . GLU B 393 ? 0.6847 0.6296 0.4391 -0.2094 -0.0357 0.0704  393 GLU B CB  
7413 C CG  . GLU B 393 ? 0.8181 0.7456 0.5759 -0.2029 -0.0438 0.0837  393 GLU B CG  
7414 C CD  . GLU B 393 ? 0.9635 0.8829 0.7107 -0.2102 -0.0434 0.0923  393 GLU B CD  
7415 O OE1 . GLU B 393 ? 1.0039 0.9093 0.7488 -0.2064 -0.0507 0.1054  393 GLU B OE1 
7416 O OE2 . GLU B 393 ? 1.0053 0.9318 0.7466 -0.2193 -0.0354 0.0860  393 GLU B OE2 
7417 N N   . ASP B 394 ? 0.5043 0.4710 0.2661 -0.2058 -0.0281 0.0481  394 ASP B N   
7418 C CA  . ASP B 394 ? 0.5073 0.4859 0.2645 -0.2114 -0.0223 0.0385  394 ASP B CA  
7419 C C   . ASP B 394 ? 0.5672 0.5480 0.3341 -0.2050 -0.0126 0.0251  394 ASP B C   
7420 O O   . ASP B 394 ? 0.5438 0.5263 0.3131 -0.2027 -0.0113 0.0201  394 ASP B O   
7421 C CB  . ASP B 394 ? 0.5550 0.5365 0.3081 -0.2130 -0.0307 0.0449  394 ASP B CB  
7422 C CG  . ASP B 394 ? 0.6534 0.6272 0.4160 -0.2028 -0.0387 0.0507  394 ASP B CG  
7423 O OD1 . ASP B 394 ? 0.6697 0.6335 0.4408 -0.1949 -0.0390 0.0521  394 ASP B OD1 
7424 O OD2 . ASP B 394 ? 0.6671 0.6458 0.4292 -0.2024 -0.0444 0.0535  394 ASP B OD2 
7425 N N   . VAL B 395 ? 0.5639 0.5450 0.3365 -0.2018 -0.0052 0.0193  395 VAL B N   
7426 C CA  . VAL B 395 ? 0.4446 0.4268 0.2278 -0.1929 0.0037  0.0084  395 VAL B CA  
7427 C C   . VAL B 395 ? 0.5114 0.5035 0.2969 -0.1945 0.0147  -0.0009 395 VAL B C   
7428 O O   . VAL B 395 ? 0.5030 0.4991 0.2831 -0.2018 0.0144  0.0022  395 VAL B O   
7429 C CB  . VAL B 395 ? 0.4720 0.4446 0.2650 -0.1829 -0.0005 0.0131  395 VAL B CB  
7430 C CG1 . VAL B 395 ? 0.4525 0.4256 0.2507 -0.1816 0.0025  0.0139  395 VAL B CG1 
7431 C CG2 . VAL B 395 ? 0.5411 0.5125 0.3419 -0.1741 0.0050  0.0052  395 VAL B CG2 
7432 N N   . LYS B 396 ? 0.3970 0.3933 0.1908 -0.1869 0.0248  -0.0121 396 LYS B N   
7433 C CA  . LYS B 396 ? 0.3730 0.3810 0.1711 -0.1862 0.0351  -0.0209 396 LYS B CA  
7434 C C   . LYS B 396 ? 0.3301 0.3414 0.1399 -0.1787 0.0383  -0.0221 396 LYS B C   
7435 O O   . LYS B 396 ? 0.3309 0.3363 0.1490 -0.1689 0.0378  -0.0220 396 LYS B O   
7436 C CB  . LYS B 396 ? 0.4426 0.4539 0.2443 -0.1801 0.0448  -0.0320 396 LYS B CB  
7437 C CG  . LYS B 396 ? 0.5215 0.5459 0.3267 -0.1793 0.0542  -0.0397 396 LYS B CG  
7438 C CD  . LYS B 396 ? 0.6072 0.6324 0.4146 -0.1722 0.0634  -0.0498 396 LYS B CD  
7439 C CE  . LYS B 396 ? 0.6398 0.6791 0.4495 -0.1716 0.0716  -0.0562 396 LYS B CE  
7440 N NZ  . LYS B 396 ? 0.6156 0.6545 0.4273 -0.1627 0.0809  -0.0658 396 LYS B NZ  
7441 N N   . THR B 397 ? 0.4217 0.3179 0.2380 -0.1480 0.0647  -0.0566 397 THR B N   
7442 C CA  . THR B 397 ? 0.3912 0.2997 0.2172 -0.1483 0.0708  -0.0548 397 THR B CA  
7443 C C   . THR B 397 ? 0.3761 0.2970 0.2130 -0.1544 0.0845  -0.0659 397 THR B C   
7444 O O   . THR B 397 ? 0.4327 0.3526 0.2635 -0.1573 0.0888  -0.0747 397 THR B O   
7445 C CB  . THR B 397 ? 0.4013 0.3076 0.2147 -0.1520 0.0648  -0.0468 397 THR B CB  
7446 O OG1 . THR B 397 ? 0.4500 0.3542 0.2524 -0.1652 0.0692  -0.0501 397 THR B OG1 
7447 C CG2 . THR B 397 ? 0.4304 0.3229 0.2308 -0.1493 0.0529  -0.0369 397 THR B CG2 
7448 N N   . GLU B 398 ? 0.3513 0.2860 0.2064 -0.1481 0.0853  -0.0674 398 GLU B N   
7449 C CA  . GLU B 398 ? 0.3413 0.2899 0.2106 -0.1527 0.0947  -0.0801 398 GLU B CA  
7450 C C   . GLU B 398 ? 0.3587 0.3196 0.2363 -0.1494 0.0901  -0.0792 398 GLU B C   
7451 O O   . GLU B 398 ? 0.3196 0.2777 0.1985 -0.1399 0.0820  -0.0711 398 GLU B O   
7452 C CB  . GLU B 398 ? 0.4293 0.3815 0.3136 -0.1397 0.1011  -0.0874 398 GLU B CB  
7453 C CG  . GLU B 398 ? 0.5678 0.5423 0.4688 -0.1308 0.1107  -0.0954 398 GLU B CG  
7454 C CD  . GLU B 398 ? 0.6968 0.6682 0.6102 -0.1161 0.1153  -0.1034 398 GLU B CD  
7455 O OE1 . GLU B 398 ? 0.7347 0.6846 0.6421 -0.1139 0.1093  -0.1035 398 GLU B OE1 
7456 O OE2 . GLU B 398 ? 0.7240 0.7140 0.6542 -0.1053 0.1228  -0.1084 398 GLU B OE2 
7457 N N   . VAL B 399 ? 0.2977 0.2797 0.1835 -0.1501 0.0963  -0.0807 399 VAL B N   
7458 C CA  . VAL B 399 ? 0.3450 0.3438 0.2437 -0.1467 0.0934  -0.0762 399 VAL B CA  
7459 C C   . VAL B 399 ? 0.3538 0.3719 0.2798 -0.1344 0.0989  -0.0785 399 VAL B C   
7460 O O   . VAL B 399 ? 0.3693 0.3962 0.3035 -0.1287 0.1084  -0.0853 399 VAL B O   
7461 C CB  . VAL B 399 ? 0.3545 0.3664 0.2468 -0.1556 0.0966  -0.0757 399 VAL B CB  
7462 C CG1 . VAL B 399 ? 0.3044 0.3358 0.2118 -0.1532 0.0948  -0.0715 399 VAL B CG1 
7463 C CG2 . VAL B 399 ? 0.4015 0.3923 0.2662 -0.1673 0.0903  -0.0722 399 VAL B CG2 
7464 N N   . ILE B 400 ? 0.3425 0.3662 0.2812 -0.1283 0.0926  -0.0726 400 ILE B N   
7465 C CA  . ILE B 400 ? 0.3305 0.3743 0.2953 -0.1171 0.0962  -0.0728 400 ILE B CA  
7466 C C   . ILE B 400 ? 0.3152 0.3787 0.2888 -0.1183 0.0931  -0.0679 400 ILE B C   
7467 O O   . ILE B 400 ? 0.3184 0.3724 0.2810 -0.1236 0.0848  -0.0623 400 ILE B O   
7468 C CB  . ILE B 400 ? 0.3553 0.3875 0.3287 -0.1088 0.0916  -0.0696 400 ILE B CB  
7469 C CG1 . ILE B 400 ? 0.4595 0.4846 0.4289 -0.1083 0.0798  -0.0605 400 ILE B CG1 
7470 C CG2 . ILE B 400 ? 0.5147 0.5242 0.4749 -0.1114 0.0933  -0.0737 400 ILE B CG2 
7471 C CD1 . ILE B 400 ? 0.5883 0.5983 0.5606 -0.1008 0.0737  -0.0558 400 ILE B CD1 
7472 N N   . GLU B 401 ? 0.2473 0.3378 0.2394 -0.1126 0.1001  -0.0704 401 GLU B N   
7473 C CA  . GLU B 401 ? 0.2409 0.3524 0.2416 -0.1155 0.0981  -0.0666 401 GLU B CA  
7474 C C   . GLU B 401 ? 0.2481 0.3717 0.2684 -0.1062 0.0935  -0.0619 401 GLU B C   
7475 O O   . GLU B 401 ? 0.2296 0.3656 0.2541 -0.1101 0.0896  -0.0581 401 GLU B O   
7476 C CB  . GLU B 401 ? 0.2836 0.4215 0.2923 -0.1160 0.1083  -0.0714 401 GLU B CB  
7477 C CG  . GLU B 401 ? 0.4505 0.5796 0.4385 -0.1272 0.1129  -0.0751 401 GLU B CG  
7478 C CD  . GLU B 401 ? 0.5895 0.7037 0.5576 -0.1418 0.1054  -0.0701 401 GLU B CD  
7479 O OE1 . GLU B 401 ? 0.6727 0.7925 0.6457 -0.1440 0.0994  -0.0652 401 GLU B OE1 
7480 O OE2 . GLU B 401 ? 0.6782 0.7746 0.6248 -0.1506 0.1057  -0.0713 401 GLU B OE2 
7481 N N   . SER B 402 ? 0.2562 0.3758 0.2875 -0.0949 0.0940  -0.0621 402 SER B N   
7482 C CA  . SER B 402 ? 0.2437 0.3776 0.2943 -0.0857 0.0904  -0.0573 402 SER B CA  
7483 C C   . SER B 402 ? 0.2452 0.3652 0.3015 -0.0761 0.0897  -0.0565 402 SER B C   
7484 O O   . SER B 402 ? 0.2264 0.3359 0.2807 -0.0725 0.0961  -0.0623 402 SER B O   
7485 C CB  . SER B 402 ? 0.2813 0.4483 0.3525 -0.0779 0.0969  -0.0595 402 SER B CB  
7486 O OG  . SER B 402 ? 0.3257 0.5068 0.4152 -0.0683 0.0929  -0.0547 402 SER B OG  
7487 N N   . VAL B 403 ? 0.1923 0.3122 0.2556 -0.0724 0.0824  -0.0496 403 VAL B N   
7488 C CA  . VAL B 403 ? 0.1720 0.2823 0.2438 -0.0634 0.0820  -0.0475 403 VAL B CA  
7489 C C   . VAL B 403 ? 0.2164 0.3507 0.3104 -0.0519 0.0815  -0.0437 403 VAL B C   
7490 O O   . VAL B 403 ? 0.1958 0.3493 0.2950 -0.0537 0.0780  -0.0408 403 VAL B O   
7491 C CB  . VAL B 403 ? 0.2022 0.2878 0.2605 -0.0682 0.0733  -0.0418 403 VAL B CB  
7492 C CG1 . VAL B 403 ? 0.2218 0.2840 0.2584 -0.0769 0.0726  -0.0450 403 VAL B CG1 
7493 C CG2 . VAL B 403 ? 0.1637 0.2554 0.2201 -0.0708 0.0645  -0.0353 403 VAL B CG2 
7494 N N   . LYS B 404 ? 0.1720 0.3038 0.2791 -0.0400 0.0852  -0.0443 404 LYS B N   
7495 C CA  . LYS B 404 ? 0.1736 0.3231 0.3003 -0.0276 0.0829  -0.0391 404 LYS B CA  
7496 C C   . LYS B 404 ? 0.1514 0.2886 0.2731 -0.0318 0.0749  -0.0309 404 LYS B C   
7497 O O   . LYS B 404 ? 0.1647 0.2770 0.2796 -0.0338 0.0751  -0.0298 404 LYS B O   
7498 C CB  . LYS B 404 ? 0.2352 0.3819 0.3778 -0.0103 0.0898  -0.0429 404 LYS B CB  
7499 C CG  . LYS B 404 ? 0.4145 0.5758 0.5640 -0.0013 0.0977  -0.0514 404 LYS B CG  
7500 C CD  . LYS B 404 ? 0.5276 0.6987 0.6985 0.0212  0.0988  -0.0505 404 LYS B CD  
7501 C CE  . LYS B 404 ? 0.5591 0.7408 0.7351 0.0331  0.1065  -0.0592 404 LYS B CE  
7502 N NZ  . LYS B 404 ? 0.5906 0.7702 0.7495 0.0185  0.1121  -0.0664 404 LYS B NZ  
7503 N N   . ALA B 405 ? 0.1297 0.2832 0.2540 -0.0333 0.0679  -0.0252 405 ALA B N   
7504 C CA  . ALA B 405 ? 0.0988 0.2419 0.2158 -0.0372 0.0605  -0.0183 405 ALA B CA  
7505 C C   . ALA B 405 ? 0.1306 0.2632 0.2557 -0.0265 0.0607  -0.0131 405 ALA B C   
7506 O O   . ALA B 405 ? 0.1311 0.2704 0.2691 -0.0120 0.0616  -0.0110 405 ALA B O   
7507 C CB  . ALA B 405 ? 0.1022 0.2655 0.2228 -0.0385 0.0539  -0.0149 405 ALA B CB  
7508 N N   . GLY B 406 ? 0.1502 0.2602 0.2628 -0.0315 0.0569  -0.0086 406 GLY B N   
7509 C CA  . GLY B 406 ? 0.1582 0.2527 0.2723 -0.0218 0.0540  -0.0003 406 GLY B CA  
7510 C C   . GLY B 406 ? 0.1594 0.2352 0.2606 -0.0295 0.0505  0.0037  406 GLY B C   
7511 O O   . GLY B 406 ? 0.1117 0.1886 0.2031 -0.0400 0.0487  0.0009  406 GLY B O   
7512 N N   . THR B 407 ? 0.1336 0.1923 0.2351 -0.0240 0.0496  0.0104  407 THR B N   
7513 C CA  . THR B 407 ? 0.1512 0.1951 0.2438 -0.0297 0.0470  0.0148  407 THR B CA  
7514 C C   . THR B 407 ? 0.2185 0.2395 0.3115 -0.0292 0.0490  0.0157  407 THR B C   
7515 O O   . THR B 407 ? 0.2168 0.2313 0.3154 -0.0234 0.0521  0.0129  407 THR B O   
7516 C CB  . THR B 407 ? 0.0954 0.1474 0.1885 -0.0249 0.0432  0.0245  407 THR B CB  
7517 O OG1 . THR B 407 ? 0.1457 0.1915 0.2462 -0.0152 0.0437  0.0327  407 THR B OG1 
7518 C CG2 . THR B 407 ? 0.1093 0.1849 0.2032 -0.0239 0.0404  0.0234  407 THR B CG2 
7519 N N   . TRP B 408 ? 0.1544 0.1635 0.2419 -0.0349 0.0469  0.0192  408 TRP B N   
7520 C CA  . TRP B 408 ? 0.1220 0.1106 0.2107 -0.0361 0.0479  0.0205  408 TRP B CA  
7521 C C   . TRP B 408 ? 0.1971 0.1798 0.2931 -0.0281 0.0480  0.0304  408 TRP B C   
7522 O O   . TRP B 408 ? 0.2662 0.2297 0.3632 -0.0300 0.0484  0.0325  408 TRP B O   
7523 C CB  . TRP B 408 ? 0.1887 0.1714 0.2614 -0.0406 0.0397  0.0191  408 TRP B CB  
7524 C CG  . TRP B 408 ? 0.2042 0.1965 0.2720 -0.0404 0.0357  0.0245  408 TRP B CG  
7525 C CD1 . TRP B 408 ? 0.2015 0.2049 0.2754 -0.0362 0.0377  0.0319  408 TRP B CD1 
7526 C CD2 . TRP B 408 ? 0.1331 0.1251 0.1902 -0.0440 0.0301  0.0232  408 TRP B CD2 
7527 N NE1 . TRP B 408 ? 0.1824 0.1910 0.2485 -0.0374 0.0346  0.0334  408 TRP B NE1 
7528 C CE2 . TRP B 408 ? 0.1608 0.1626 0.2183 -0.0420 0.0307  0.0279  408 TRP B CE2 
7529 C CE3 . TRP B 408 ? 0.1655 0.1511 0.2147 -0.0480 0.0251  0.0194  408 TRP B CE3 
7530 C CZ2 . TRP B 408 ? 0.1637 0.1683 0.2157 -0.0439 0.0284  0.0274  408 TRP B CZ2 
7531 C CZ3 . TRP B 408 ? 0.1845 0.1739 0.2285 -0.0501 0.0215  0.0206  408 TRP B CZ3 
7532 C CH2 . TRP B 408 ? 0.1879 0.1864 0.2339 -0.0480 0.0243  0.0235  408 TRP B CH2 
7533 N N   . PHE B 409 ? 0.1939 0.1912 0.2939 -0.0198 0.0471  0.0369  409 PHE B N   
7534 C CA  . PHE B 409 ? 0.2169 0.2068 0.3220 -0.0113 0.0468  0.0474  409 PHE B CA  
7535 C C   . PHE B 409 ? 0.2721 0.2636 0.3840 0.0000  0.0482  0.0438  409 PHE B C   
7536 O O   . PHE B 409 ? 0.2341 0.2471 0.3500 0.0067  0.0470  0.0437  409 PHE B O   
7537 C CB  . PHE B 409 ? 0.3403 0.3445 0.4436 -0.0090 0.0443  0.0583  409 PHE B CB  
7538 C CG  . PHE B 409 ? 0.4648 0.4570 0.5694 -0.0043 0.0441  0.0716  409 PHE B CG  
7539 C CD1 . PHE B 409 ? 0.5225 0.5047 0.6320 0.0065  0.0439  0.0756  409 PHE B CD1 
7540 C CD2 . PHE B 409 ? 0.4798 0.4691 0.5808 -0.0111 0.0444  0.0801  409 PHE B CD2 
7541 C CE1 . PHE B 409 ? 0.5695 0.5364 0.6780 0.0099  0.0433  0.0894  409 PHE B CE1 
7542 C CE2 . PHE B 409 ? 0.5688 0.5463 0.6698 -0.0092 0.0448  0.0933  409 PHE B CE2 
7543 C CZ  . PHE B 409 ? 0.5737 0.5380 0.6774 0.0008  0.0440  0.0986  409 PHE B CZ  
7544 N N   . ASP B 410 ? 0.3040 0.2735 0.4172 0.0021  0.0507  0.0397  410 ASP B N   
7545 C CA  . ASP B 410 ? 0.2713 0.2377 0.3911 0.0145  0.0530  0.0350  410 ASP B CA  
7546 C C   . ASP B 410 ? 0.2921 0.2807 0.4151 0.0157  0.0558  0.0232  410 ASP B C   
7547 O O   . ASP B 410 ? 0.2739 0.2696 0.4052 0.0279  0.0580  0.0194  410 ASP B O   
7548 C CB  . ASP B 410 ? 0.3654 0.3348 0.4914 0.0287  0.0503  0.0467  410 ASP B CB  
7549 C CG  . ASP B 410 ? 0.4713 0.4153 0.5931 0.0275  0.0484  0.0593  410 ASP B CG  
7550 O OD1 . ASP B 410 ? 0.5501 0.4696 0.6675 0.0187  0.0499  0.0567  410 ASP B OD1 
7551 O OD2 . ASP B 410 ? 0.5572 0.5064 0.6798 0.0345  0.0453  0.0722  410 ASP B OD2 
7552 N N   . GLY B 411 ? 0.2176 0.2177 0.3348 0.0036  0.0559  0.0176  411 GLY B N   
7553 C CA  . GLY B 411 ? 0.1881 0.2095 0.3072 0.0020  0.0588  0.0078  411 GLY B CA  
7554 C C   . GLY B 411 ? 0.2009 0.2523 0.3290 0.0086  0.0567  0.0110  411 GLY B C   
7555 O O   . GLY B 411 ? 0.2131 0.2847 0.3473 0.0099  0.0598  0.0033  411 GLY B O   
7556 N N   . ASN B 412 ? 0.1613 0.2183 0.2903 0.0122  0.0515  0.0219  412 ASN B N   
7557 C CA  . ASN B 412 ? 0.1824 0.2683 0.3192 0.0188  0.0480  0.0252  412 ASN B CA  
7558 C C   . ASN B 412 ? 0.1462 0.2377 0.2752 0.0138  0.0425  0.0334  412 ASN B C   
7559 O O   . ASN B 412 ? 0.1535 0.2289 0.2725 0.0056  0.0423  0.0359  412 ASN B O   
7560 C CB  . ASN B 412 ? 0.1910 0.2793 0.3398 0.0368  0.0475  0.0299  412 ASN B CB  
7561 C CG  . ASN B 412 ? 0.2683 0.3337 0.4133 0.0437  0.0445  0.0429  412 ASN B CG  
7562 O OD1 . ASN B 412 ? 0.2216 0.2853 0.3588 0.0384  0.0409  0.0516  412 ASN B OD1 
7563 N ND2 . ASN B 412 ? 0.2736 0.3197 0.4233 0.0552  0.0465  0.0439  412 ASN B ND2 
7564 N N   . PHE B 413 ? 0.1292 0.2457 0.2628 0.0188  0.0379  0.0370  413 PHE B N   
7565 C CA  . PHE B 413 ? 0.1226 0.2480 0.2469 0.0135  0.0329  0.0420  413 PHE B CA  
7566 C C   . PHE B 413 ? 0.1811 0.3064 0.3041 0.0237  0.0286  0.0554  413 PHE B C   
7567 O O   . PHE B 413 ? 0.1630 0.2997 0.2779 0.0213  0.0242  0.0595  413 PHE B O   
7568 C CB  . PHE B 413 ? 0.0977 0.2513 0.2240 0.0080  0.0298  0.0351  413 PHE B CB  
7569 C CG  . PHE B 413 ? 0.1490 0.3003 0.2712 -0.0057 0.0335  0.0238  413 PHE B CG  
7570 C CD1 . PHE B 413 ? 0.1751 0.3131 0.2827 -0.0170 0.0329  0.0217  413 PHE B CD1 
7571 C CD2 . PHE B 413 ? 0.1210 0.2829 0.2530 -0.0064 0.0379  0.0157  413 PHE B CD2 
7572 C CE1 . PHE B 413 ? 0.1590 0.2914 0.2605 -0.0292 0.0355  0.0127  413 PHE B CE1 
7573 C CE2 . PHE B 413 ? 0.1416 0.3000 0.2672 -0.0200 0.0416  0.0065  413 PHE B CE2 
7574 C CZ  . PHE B 413 ? 0.0975 0.2396 0.2072 -0.0315 0.0399  0.0056  413 PHE B CZ  
7575 N N   . LEU B 414 ? 0.1828 0.2934 0.3113 0.0346  0.0297  0.0625  414 LEU B N   
7576 C CA  . LEU B 414 ? 0.1771 0.2888 0.3043 0.0455  0.0251  0.0765  414 LEU B CA  
7577 C C   . LEU B 414 ? 0.2003 0.3007 0.3137 0.0392  0.0247  0.0860  414 LEU B C   
7578 O O   . LEU B 414 ? 0.1647 0.2710 0.2731 0.0457  0.0206  0.0976  414 LEU B O   
7579 C CB  . LEU B 414 ? 0.1923 0.2859 0.3275 0.0588  0.0264  0.0818  414 LEU B CB  
7580 C CG  . LEU B 414 ? 0.2226 0.3317 0.3731 0.0697  0.0268  0.0738  414 LEU B CG  
7581 C CD1 . LEU B 414 ? 0.2379 0.3238 0.3939 0.0845  0.0280  0.0788  414 LEU B CD1 
7582 C CD2 . LEU B 414 ? 0.1859 0.3317 0.3429 0.0759  0.0201  0.0754  414 LEU B CD2 
7583 N N   . LYS B 415 ? 0.1903 0.2771 0.2972 0.0272  0.0288  0.0815  415 LYS B N   
7584 C CA  . LYS B 415 ? 0.1553 0.2374 0.2509 0.0222  0.0290  0.0900  415 LYS B CA  
7585 C C   . LYS B 415 ? 0.1753 0.2793 0.2616 0.0191  0.0255  0.0879  415 LYS B C   
7586 O O   . LYS B 415 ? 0.1369 0.2413 0.2129 0.0169  0.0259  0.0948  415 LYS B O   
7587 C CB  . LYS B 415 ? 0.2151 0.2785 0.3083 0.0114  0.0339  0.0864  415 LYS B CB  
7588 C CG  . LYS B 415 ? 0.3560 0.3940 0.4548 0.0122  0.0370  0.0898  415 LYS B CG  
7589 C CD  . LYS B 415 ? 0.4955 0.5244 0.5937 0.0208  0.0357  0.1051  415 LYS B CD  
7590 C CE  . LYS B 415 ? 0.5649 0.5975 0.6535 0.0167  0.0362  0.1171  415 LYS B CE  
7591 N NZ  . LYS B 415 ? 0.6071 0.6252 0.6950 0.0051  0.0406  0.1179  415 LYS B NZ  
7592 N N   . TRP B 416 ? 0.1320 0.2545 0.2213 0.0182  0.0223  0.0782  416 TRP B N   
7593 C CA  . TRP B 416 ? 0.1846 0.3249 0.2637 0.0137  0.0183  0.0743  416 TRP B CA  
7594 C C   . TRP B 416 ? 0.1549 0.3204 0.2378 0.0194  0.0115  0.0739  416 TRP B C   
7595 O O   . TRP B 416 ? 0.1691 0.3494 0.2422 0.0155  0.0069  0.0707  416 TRP B O   
7596 C CB  . TRP B 416 ? 0.1060 0.2430 0.1814 0.0019  0.0201  0.0610  416 TRP B CB  
7597 C CG  . TRP B 416 ? 0.1370 0.2521 0.2097 -0.0034 0.0256  0.0607  416 TRP B CG  
7598 C CD1 . TRP B 416 ? 0.1140 0.2234 0.1765 -0.0068 0.0272  0.0628  416 TRP B CD1 
7599 C CD2 . TRP B 416 ? 0.1501 0.2485 0.2311 -0.0054 0.0298  0.0580  416 TRP B CD2 
7600 N NE1 . TRP B 416 ? 0.1648 0.2569 0.2305 -0.0111 0.0315  0.0621  416 TRP B NE1 
7601 C CE2 . TRP B 416 ? 0.1721 0.2559 0.2480 -0.0109 0.0328  0.0591  416 TRP B CE2 
7602 C CE3 . TRP B 416 ? 0.1427 0.2381 0.2346 -0.0025 0.0314  0.0544  416 TRP B CE3 
7603 C CZ2 . TRP B 416 ? 0.1500 0.2160 0.2307 -0.0149 0.0362  0.0566  416 TRP B CZ2 
7604 C CZ3 . TRP B 416 ? 0.1352 0.2109 0.2300 -0.0061 0.0356  0.0512  416 TRP B CZ3 
7605 C CH2 . TRP B 416 ? 0.2044 0.2653 0.2933 -0.0128 0.0374  0.0525  416 TRP B CH2 
7606 N N   . ILE B 417 ? 0.1781 0.3497 0.2751 0.0286  0.0103  0.0762  417 ILE B N   
7607 C CA  . ILE B 417 ? 0.1864 0.3865 0.2907 0.0343  0.0033  0.0750  417 ILE B CA  
7608 C C   . ILE B 417 ? 0.2124 0.4124 0.3309 0.0494  0.0027  0.0824  417 ILE B C   
7609 O O   . ILE B 417 ? 0.2087 0.3860 0.3322 0.0526  0.0085  0.0837  417 ILE B O   
7610 C CB  . ILE B 417 ? 0.1692 0.3852 0.2796 0.0238  0.0033  0.0603  417 ILE B CB  
7611 C CG1 . ILE B 417 ? 0.1181 0.3677 0.2325 0.0251  -0.0054 0.0587  417 ILE B CG1 
7612 C CG2 . ILE B 417 ? 0.1485 0.3591 0.2742 0.0254  0.0095  0.0542  417 ILE B CG2 
7613 C CD1 . ILE B 417 ? 0.1549 0.4179 0.2681 0.0099  -0.0065 0.0454  417 ILE B CD1 
7614 N N   . GLY B 418 ? 0.2578 0.4825 0.3821 0.0594  -0.0050 0.0873  418 GLY B N   
7615 C CA  . GLY B 418 ? 0.2241 0.4525 0.3637 0.0760  -0.0067 0.0928  418 GLY B CA  
7616 C C   . GLY B 418 ? 0.3256 0.5447 0.4589 0.0899  -0.0115 0.1102  418 GLY B C   
7617 O O   . GLY B 418 ? 0.3660 0.5850 0.5112 0.1058  -0.0136 0.1156  418 GLY B O   
7618 N N   . ASN B 419 ? 0.3566 0.5670 0.4710 0.0852  -0.0130 0.1193  419 ASN B N   
7619 C CA  . ASN B 419 ? 0.3628 0.5714 0.4686 0.0972  -0.0192 0.1366  419 ASN B CA  
7620 C C   . ASN B 419 ? 0.3507 0.5829 0.4413 0.0924  -0.0264 0.1385  419 ASN B C   
7621 O O   . ASN B 419 ? 0.3331 0.5762 0.4182 0.0790  -0.0254 0.1266  419 ASN B O   
7622 C CB  . ASN B 419 ? 0.3356 0.5070 0.4314 0.0978  -0.0133 0.1493  419 ASN B CB  
7623 C CG  . ASN B 419 ? 0.3682 0.5294 0.4463 0.0830  -0.0080 0.1503  419 ASN B CG  
7624 O OD1 . ASN B 419 ? 0.3617 0.5414 0.4302 0.0749  -0.0099 0.1444  419 ASN B OD1 
7625 N ND2 . ASN B 419 ? 0.4024 0.5336 0.4764 0.0797  -0.0013 0.1577  419 ASN B ND2 
7626 N N   . LYS B 420 ? 0.3785 0.6110 0.4581 0.1007  -0.0324 0.1500  420 LYS B N   
7627 C CA  . LYS B 420 ? 0.3870 0.6432 0.4534 0.0972  -0.0401 0.1480  420 LYS B CA  
7628 C C   . LYS B 420 ? 0.3218 0.5765 0.3683 0.0846  -0.0369 0.1469  420 LYS B C   
7629 O O   . LYS B 420 ? 0.3331 0.6082 0.3725 0.0767  -0.0412 0.1370  420 LYS B O   
7630 C CB  . LYS B 420 ? 0.5062 0.7595 0.5645 0.1085  -0.0468 0.1599  420 LYS B CB  
7631 C CG  . LYS B 420 ? 0.6668 0.9155 0.7431 0.1234  -0.0497 0.1623  420 LYS B CG  
7632 C CD  . LYS B 420 ? 0.7366 1.0034 0.8368 0.1233  -0.0487 0.1474  420 LYS B CD  
7633 C CE  . LYS B 420 ? 0.7796 1.0271 0.8963 0.1353  -0.0446 0.1483  420 LYS B CE  
7634 N NZ  . LYS B 420 ? 0.7527 1.0185 0.8921 0.1353  -0.0422 0.1332  420 LYS B NZ  
7635 N N   . GLU B 421 ? 0.3288 0.5584 0.3663 0.0819  -0.0289 0.1555  421 GLU B N   
7636 C CA  . GLU B 421 ? 0.2724 0.4997 0.2917 0.0708  -0.0242 0.1534  421 GLU B CA  
7637 C C   . GLU B 421 ? 0.2467 0.4756 0.2721 0.0587  -0.0200 0.1348  421 GLU B C   
7638 O O   . GLU B 421 ? 0.2617 0.5026 0.2749 0.0508  -0.0218 0.1252  421 GLU B O   
7639 C CB  . GLU B 421 ? 0.4117 0.6108 0.4234 0.0689  -0.0149 0.1649  421 GLU B CB  
7640 C CG  . GLU B 421 ? 0.5283 0.7186 0.5283 0.0747  -0.0166 0.1777  421 GLU B CG  
7641 C CD  . GLU B 421 ? 0.7131 0.9173 0.6919 0.0706  -0.0185 0.1766  421 GLU B CD  
7642 O OE1 . GLU B 421 ? 0.7725 0.9983 0.7478 0.0735  -0.0273 0.1712  421 GLU B OE1 
7643 O OE2 . GLU B 421 ? 0.7812 0.9755 0.7477 0.0642  -0.0111 0.1798  421 GLU B OE2 
7644 N N   . LYS B 422 ? 0.2321 0.4460 0.2745 0.0567  -0.0141 0.1289  422 LYS B N   
7645 C CA  . LYS B 422 ? 0.1883 0.4013 0.2354 0.0449  -0.0102 0.1118  422 LYS B CA  
7646 C C   . LYS B 422 ? 0.2247 0.4641 0.2765 0.0420  -0.0178 0.1003  422 LYS B C   
7647 O O   . LYS B 422 ? 0.1865 0.4295 0.2310 0.0308  -0.0178 0.0880  422 LYS B O   
7648 C CB  . LYS B 422 ? 0.1767 0.3698 0.2398 0.0439  -0.0031 0.1082  422 LYS B CB  
7649 C CG  . LYS B 422 ? 0.1698 0.3359 0.2283 0.0423  0.0046  0.1170  422 LYS B CG  
7650 C CD  . LYS B 422 ? 0.2039 0.3495 0.2765 0.0409  0.0105  0.1128  422 LYS B CD  
7651 C CE  . LYS B 422 ? 0.2209 0.3411 0.2902 0.0401  0.0162  0.1240  422 LYS B CE  
7652 N NZ  . LYS B 422 ? 0.2013 0.3178 0.2598 0.0296  0.0211  0.1227  422 LYS B NZ  
7653 N N   . ASN B 423 ? 0.2063 0.4648 0.2701 0.0519  -0.0250 0.1045  423 ASN B N   
7654 C CA  . ASN B 423 ? 0.1894 0.4777 0.2595 0.0482  -0.0330 0.0944  423 ASN B CA  
7655 C C   . ASN B 423 ? 0.2082 0.5110 0.2577 0.0429  -0.0404 0.0928  423 ASN B C   
7656 O O   . ASN B 423 ? 0.2095 0.5272 0.2576 0.0321  -0.0445 0.0800  423 ASN B O   
7657 C CB  . ASN B 423 ? 0.2097 0.5191 0.2991 0.0619  -0.0395 0.1000  423 ASN B CB  
7658 C CG  . ASN B 423 ? 0.2104 0.5114 0.3214 0.0654  -0.0325 0.0956  423 ASN B CG  
7659 O OD1 . ASN B 423 ? 0.1762 0.4601 0.2881 0.0551  -0.0240 0.0864  423 ASN B OD1 
7660 N ND2 . ASN B 423 ? 0.2052 0.5136 0.3303 0.0789  -0.0353 0.0993  423 ASN B ND2 
7661 N N   . GLU B 424 ? 0.2284 0.5259 0.2604 0.0492  -0.0418 0.1054  424 GLU B N   
7662 C CA  . GLU B 424 ? 0.2548 0.5622 0.2639 0.0440  -0.0471 0.1022  424 GLU B CA  
7663 C C   . GLU B 424 ? 0.2507 0.5475 0.2474 0.0305  -0.0422 0.0886  424 GLU B C   
7664 O O   . GLU B 424 ? 0.2289 0.5381 0.2139 0.0225  -0.0484 0.0778  424 GLU B O   
7665 C CB  . GLU B 424 ? 0.3865 0.6826 0.3783 0.0515  -0.0453 0.1161  424 GLU B CB  
7666 C CG  . GLU B 424 ? 0.5588 0.8602 0.5263 0.0461  -0.0482 0.1107  424 GLU B CG  
7667 C CD  . GLU B 424 ? 0.7288 1.0522 0.6964 0.0455  -0.0594 0.1042  424 GLU B CD  
7668 O OE1 . GLU B 424 ? 0.7655 1.0929 0.7137 0.0406  -0.0629 0.0980  424 GLU B OE1 
7669 O OE2 . GLU B 424 ? 0.7711 1.1076 0.7585 0.0501  -0.0646 0.1049  424 GLU B OE2 
7670 N N   . TYR B 425 ? 0.1891 0.4604 0.1876 0.0277  -0.0312 0.0881  425 TYR B N   
7671 C CA  . TYR B 425 ? 0.1823 0.4405 0.1705 0.0165  -0.0262 0.0749  425 TYR B CA  
7672 C C   . TYR B 425 ? 0.1718 0.4365 0.1692 0.0061  -0.0297 0.0596  425 TYR B C   
7673 O O   . TYR B 425 ? 0.2543 0.5182 0.2376 -0.0032 -0.0324 0.0477  425 TYR B O   
7674 C CB  . TYR B 425 ? 0.1954 0.4282 0.1874 0.0159  -0.0148 0.0777  425 TYR B CB  
7675 C CG  . TYR B 425 ? 0.1835 0.4077 0.1583 0.0187  -0.0091 0.0855  425 TYR B CG  
7676 C CD1 . TYR B 425 ? 0.2245 0.4613 0.1828 0.0244  -0.0131 0.0945  425 TYR B CD1 
7677 C CD2 . TYR B 425 ? 0.1756 0.3814 0.1506 0.0151  0.0002  0.0835  425 TYR B CD2 
7678 C CE1 . TYR B 425 ? 0.2531 0.4844 0.1953 0.0263  -0.0064 0.1017  425 TYR B CE1 
7679 C CE2 . TYR B 425 ? 0.1883 0.3906 0.1499 0.0172  0.0064  0.0903  425 TYR B CE2 
7680 C CZ  . TYR B 425 ? 0.2715 0.4866 0.2167 0.0225  0.0037  0.0993  425 TYR B CZ  
7681 O OH  . TYR B 425 ? 0.2439 0.4542 0.1793 0.0234  0.0109  0.1034  425 TYR B OH  
7682 N N   . TRP B 426 ? 0.1757 0.4452 0.1957 0.0070  -0.0292 0.0593  426 TRP B N   
7683 C CA  . TRP B 426 ? 0.1715 0.4499 0.2004 -0.0042 -0.0318 0.0459  426 TRP B CA  
7684 C C   . TRP B 426 ? 0.1695 0.4749 0.1928 -0.0086 -0.0433 0.0409  426 TRP B C   
7685 O O   . TRP B 426 ? 0.1965 0.5032 0.2136 -0.0221 -0.0463 0.0282  426 TRP B O   
7686 C CB  . TRP B 426 ? 0.1853 0.4680 0.2395 -0.0011 -0.0282 0.0469  426 TRP B CB  
7687 C CG  . TRP B 426 ? 0.1287 0.3837 0.1866 -0.0017 -0.0177 0.0472  426 TRP B CG  
7688 C CD1 . TRP B 426 ? 0.1520 0.3925 0.2158 0.0085  -0.0123 0.0578  426 TRP B CD1 
7689 C CD2 . TRP B 426 ? 0.1751 0.4122 0.2296 -0.0136 -0.0123 0.0367  426 TRP B CD2 
7690 N NE1 . TRP B 426 ? 0.1389 0.3559 0.2040 0.0031  -0.0041 0.0537  426 TRP B NE1 
7691 C CE2 . TRP B 426 ? 0.1778 0.3928 0.2372 -0.0097 -0.0041 0.0413  426 TRP B CE2 
7692 C CE3 . TRP B 426 ? 0.2405 0.4766 0.2872 -0.0277 -0.0143 0.0244  426 TRP B CE3 
7693 C CZ2 . TRP B 426 ? 0.1660 0.3606 0.2230 -0.0184 0.0017  0.0340  426 TRP B CZ2 
7694 C CZ3 . TRP B 426 ? 0.2172 0.4304 0.2609 -0.0358 -0.0080 0.0180  426 TRP B CZ3 
7695 C CH2 . TRP B 426 ? 0.1457 0.3396 0.1945 -0.0306 -0.0004 0.0229  426 TRP B CH2 
7696 N N   . LYS B 427 ? 0.1735 0.4993 0.1977 0.0022  -0.0506 0.0510  427 LYS B N   
7697 C CA  . LYS B 427 ? 0.1897 0.5344 0.2063 -0.0019 -0.0601 0.0456  427 LYS B CA  
7698 C C   . LYS B 427 ? 0.2262 0.5586 0.2151 -0.0104 -0.0615 0.0373  427 LYS B C   
7699 O O   . LYS B 427 ? 0.2524 0.5876 0.2354 -0.0219 -0.0662 0.0251  427 LYS B O   
7700 C CB  . LYS B 427 ? 0.2048 0.5620 0.2236 0.0122  -0.0651 0.0581  427 LYS B CB  
7701 C CG  . LYS B 427 ? 0.4078 0.7736 0.4517 0.0235  -0.0641 0.0660  427 LYS B CG  
7702 C CD  . LYS B 427 ? 0.5648 0.9363 0.6054 0.0380  -0.0693 0.0793  427 LYS B CD  
7703 C CE  . LYS B 427 ? 0.6151 0.9951 0.6798 0.0502  -0.0700 0.0850  427 LYS B CE  
7704 N NZ  . LYS B 427 ? 0.6870 1.0470 0.7516 0.0643  -0.0653 0.1002  427 LYS B NZ  
7705 N N   . ILE B 428 ? 0.2188 0.5356 0.1904 -0.0044 -0.0568 0.0438  428 ILE B N   
7706 C CA  . ILE B 428 ? 0.2232 0.5251 0.1686 -0.0102 -0.0558 0.0348  428 ILE B CA  
7707 C C   . ILE B 428 ? 0.2371 0.5245 0.1797 -0.0239 -0.0541 0.0194  428 ILE B C   
7708 O O   . ILE B 428 ? 0.2777 0.5577 0.2065 -0.0327 -0.0578 0.0071  428 ILE B O   
7709 C CB  . ILE B 428 ? 0.2981 0.5853 0.2296 -0.0012 -0.0476 0.0447  428 ILE B CB  
7710 C CG1 . ILE B 428 ? 0.3532 0.6500 0.2835 0.0105  -0.0495 0.0597  428 ILE B CG1 
7711 C CG2 . ILE B 428 ? 0.3137 0.5833 0.2212 -0.0060 -0.0443 0.0333  428 ILE B CG2 
7712 C CD1 . ILE B 428 ? 0.3691 0.6517 0.2931 0.0185  -0.0398 0.0726  428 ILE B CD1 
7713 N N   . LEU B 429 ? 0.1973 0.4734 0.1540 -0.0257 -0.0471 0.0199  429 LEU B N   
7714 C CA  . LEU B 429 ? 0.2315 0.4881 0.1859 -0.0383 -0.0442 0.0066  429 LEU B CA  
7715 C C   . LEU B 429 ? 0.2548 0.5258 0.2165 -0.0514 -0.0519 -0.0031 429 LEU B C   
7716 O O   . LEU B 429 ? 0.3410 0.5948 0.2900 -0.0625 -0.0530 -0.0151 429 LEU B O   
7717 C CB  . LEU B 429 ? 0.2146 0.4537 0.1852 -0.0364 -0.0339 0.0105  429 LEU B CB  
7718 C CG  . LEU B 429 ? 0.2655 0.4814 0.2326 -0.0481 -0.0303 -0.0010 429 LEU B CG  
7719 C CD1 . LEU B 429 ? 0.2877 0.4805 0.2316 -0.0470 -0.0276 -0.0064 429 LEU B CD1 
7720 C CD2 . LEU B 429 ? 0.2330 0.4387 0.2189 -0.0474 -0.0223 0.0028  429 LEU B CD2 
7721 N N   . ILE B 430 ? 0.2176 0.5127 0.2019 -0.0488 -0.0545 0.0025  430 ILE B N   
7722 C CA  . ILE B 430 ? 0.2414 0.5467 0.2360 -0.0600 -0.0580 -0.0053 430 ILE B CA  
7723 C C   . ILE B 430 ? 0.3095 0.6148 0.2867 -0.0655 -0.0655 -0.0123 430 ILE B C   
7724 O O   . ILE B 430 ? 0.3357 0.6295 0.3066 -0.0791 -0.0671 -0.0229 430 ILE B O   
7725 C CB  . ILE B 430 ? 0.2514 0.5840 0.2723 -0.0521 -0.0589 0.0026  430 ILE B CB  
7726 C CG1 . ILE B 430 ? 0.2003 0.5279 0.2395 -0.0490 -0.0503 0.0061  430 ILE B CG1 
7727 C CG2 . ILE B 430 ? 0.2396 0.5880 0.2686 -0.0618 -0.0636 -0.0043 430 ILE B CG2 
7728 C CD1 . ILE B 430 ? 0.2587 0.6063 0.3208 -0.0351 -0.0497 0.0157  430 ILE B CD1 
7729 N N   . GLU B 431 ? 0.2654 0.5812 0.2335 -0.0550 -0.0702 -0.0059 431 GLU B N   
7730 C CA  . GLU B 431 ? 0.3269 0.6430 0.2784 -0.0602 -0.0779 -0.0129 431 GLU B CA  
7731 C C   . GLU B 431 ? 0.3868 0.6714 0.3127 -0.0662 -0.0759 -0.0234 431 GLU B C   
7732 O O   . GLU B 431 ? 0.3586 0.6342 0.2739 -0.0767 -0.0811 -0.0340 431 GLU B O   
7733 C CB  . GLU B 431 ? 0.3785 0.7127 0.3257 -0.0474 -0.0833 -0.0030 431 GLU B CB  
7734 C CG  . GLU B 431 ? 0.5008 0.8654 0.4695 -0.0454 -0.0898 0.0016  431 GLU B CG  
7735 C CD  . GLU B 431 ? 0.6349 1.0068 0.6027 -0.0596 -0.0973 -0.0098 431 GLU B CD  
7736 O OE1 . GLU B 431 ? 0.7110 1.0753 0.6574 -0.0633 -0.1032 -0.0158 431 GLU B OE1 
7737 O OE2 . GLU B 431 ? 0.6820 1.0654 0.6695 -0.0674 -0.0968 -0.0130 431 GLU B OE2 
7738 N N   . ALA B 432 ? 0.3418 0.6081 0.2581 -0.0594 -0.0684 -0.0208 432 ALA B N   
7739 C CA  . ALA B 432 ? 0.3122 0.5474 0.2055 -0.0627 -0.0657 -0.0311 432 ALA B CA  
7740 C C   . ALA B 432 ? 0.3601 0.5748 0.2562 -0.0764 -0.0645 -0.0413 432 ALA B C   
7741 O O   . ALA B 432 ? 0.3518 0.5425 0.2301 -0.0823 -0.0668 -0.0520 432 ALA B O   
7742 C CB  . ALA B 432 ? 0.4042 0.6277 0.2892 -0.0514 -0.0571 -0.0252 432 ALA B CB  
7743 N N   . LYS B 433 ? 0.3283 0.5501 0.2456 -0.0808 -0.0608 -0.0376 433 LYS B N   
7744 C CA  . LYS B 433 ? 0.3371 0.5394 0.2575 -0.0940 -0.0587 -0.0452 433 LYS B CA  
7745 C C   . LYS B 433 ? 0.3996 0.6042 0.3182 -0.1059 -0.0658 -0.0524 433 LYS B C   
7746 O O   . LYS B 433 ? 0.4143 0.5930 0.3229 -0.1156 -0.0660 -0.0605 433 LYS B O   
7747 C CB  . LYS B 433 ? 0.3454 0.5588 0.2892 -0.0956 -0.0530 -0.0390 433 LYS B CB  
7748 C CG  . LYS B 433 ? 0.3410 0.5360 0.2886 -0.1089 -0.0496 -0.0445 433 LYS B CG  
7749 C CD  . LYS B 433 ? 0.3457 0.5017 0.2750 -0.1102 -0.0459 -0.0499 433 LYS B CD  
7750 C CE  . LYS B 433 ? 0.3592 0.4949 0.2897 -0.1224 -0.0431 -0.0534 433 LYS B CE  
7751 N NZ  . LYS B 433 ? 0.3642 0.4608 0.2764 -0.1219 -0.0412 -0.0581 433 LYS B NZ  
7752 N N   . LYS B 434 ? 0.3448 0.5800 0.2728 -0.1048 -0.0720 -0.0491 434 LYS B N   
7753 C CA  . LYS B 434 ? 0.3451 0.5852 0.2710 -0.1164 -0.0796 -0.0559 434 LYS B CA  
7754 C C   . LYS B 434 ? 0.4214 0.6355 0.3198 -0.1186 -0.0848 -0.0657 434 LYS B C   
7755 O O   . LYS B 434 ? 0.4516 0.6579 0.3446 -0.1305 -0.0903 -0.0736 434 LYS B O   
7756 C CB  . LYS B 434 ? 0.3961 0.6754 0.3369 -0.1123 -0.0860 -0.0499 434 LYS B CB  
7757 C CG  . LYS B 434 ? 0.4592 0.7635 0.4286 -0.1114 -0.0817 -0.0427 434 LYS B CG  
7758 C CD  . LYS B 434 ? 0.4912 0.8327 0.4756 -0.1018 -0.0877 -0.0350 434 LYS B CD  
7759 C CE  . LYS B 434 ? 0.5774 0.9357 0.5628 -0.1115 -0.0971 -0.0404 434 LYS B CE  
7760 N NZ  . LYS B 434 ? 0.6346 0.9995 0.6359 -0.1251 -0.0946 -0.0444 434 LYS B NZ  
7761 N N   . LYS B 435 ? 0.4044 0.6040 0.2848 -0.1070 -0.0828 -0.0657 435 LYS B N   
7762 C CA  . LYS B 435 ? 0.4262 0.6016 0.2789 -0.1061 -0.0873 -0.0755 435 LYS B CA  
7763 C C   . LYS B 435 ? 0.4484 0.5887 0.2850 -0.1002 -0.0805 -0.0799 435 LYS B C   
7764 O O   . LYS B 435 ? 0.4858 0.6077 0.2984 -0.0937 -0.0821 -0.0867 435 LYS B O   
7765 C CB  . LYS B 435 ? 0.4550 0.6482 0.2964 -0.0960 -0.0922 -0.0724 435 LYS B CB  
7766 C CG  . LYS B 435 ? 0.5370 0.7668 0.3933 -0.0991 -0.1003 -0.0673 435 LYS B CG  
7767 C CD  . LYS B 435 ? 0.6511 0.8973 0.4962 -0.0865 -0.1037 -0.0610 435 LYS B CD  
7768 C CE  . LYS B 435 ? 0.7035 0.9671 0.5627 -0.0732 -0.0967 -0.0463 435 LYS B CE  
7769 N NZ  . LYS B 435 ? 0.7563 1.0194 0.5976 -0.0593 -0.0944 -0.0398 435 LYS B NZ  
7770 N N   . ALA B 436 ? 0.3156 0.4585 0.3720 -0.1528 -0.0708 -0.1117 436 ALA B N   
7771 C CA  . ALA B 436 ? 0.3485 0.4535 0.3831 -0.1451 -0.0609 -0.1188 436 ALA B CA  
7772 C C   . ALA B 436 ? 0.4051 0.4615 0.4263 -0.1586 -0.0560 -0.1322 436 ALA B C   
7773 O O   . ALA B 436 ? 0.3742 0.4244 0.4098 -0.1755 -0.0551 -0.1301 436 ALA B O   
7774 C CB  . ALA B 436 ? 0.2745 0.3795 0.3219 -0.1313 -0.0494 -0.1023 436 ALA B CB  
7775 N N   . LYS B 437 ? 0.4030 0.4237 0.3976 -0.1492 -0.0519 -0.1450 437 LYS B N   
7776 C CA  . LYS B 437 ? 0.4634 0.4308 0.4432 -0.1565 -0.0471 -0.1581 437 LYS B CA  
7777 C C   . LYS B 437 ? 0.5277 0.4523 0.4968 -0.1385 -0.0348 -0.1556 437 LYS B C   
7778 O O   . LYS B 437 ? 0.5842 0.4586 0.5420 -0.1423 -0.0302 -0.1657 437 LYS B O   
7779 C CB  . LYS B 437 ? 0.5161 0.4758 0.4737 -0.1571 -0.0545 -0.1758 437 LYS B CB  
7780 C CG  . LYS B 437 ? 0.6417 0.6368 0.6091 -0.1729 -0.0681 -0.1754 437 LYS B CG  
7781 C CD  . LYS B 437 ? 0.8280 0.8153 0.7695 -0.1744 -0.0754 -0.1933 437 LYS B CD  
7782 C CE  . LYS B 437 ? 0.8982 0.9213 0.8503 -0.1906 -0.0904 -0.1925 437 LYS B CE  
7783 N NZ  . LYS B 437 ? 0.8911 0.9674 0.8587 -0.1823 -0.0968 -0.1748 437 LYS B NZ  
7784 N N   . ASN B 438 ? 0.4236 0.3652 0.3970 -0.1166 -0.0300 -0.1396 438 ASN B N   
7785 C CA  . ASN B 438 ? 0.4381 0.3469 0.4032 -0.0955 -0.0206 -0.1341 438 ASN B CA  
7786 C C   . ASN B 438 ? 0.4475 0.3829 0.4240 -0.0805 -0.0173 -0.1130 438 ASN B C   
7787 O O   . ASN B 438 ? 0.4012 0.3770 0.3898 -0.0834 -0.0212 -0.1052 438 ASN B O   
7788 C CB  . ASN B 438 ? 0.4516 0.3471 0.3968 -0.0810 -0.0189 -0.1521 438 ASN B CB  
7789 C CG  . ASN B 438 ? 0.4142 0.3551 0.3549 -0.0731 -0.0228 -0.1531 438 ASN B CG  
7790 O OD1 . ASN B 438 ? 0.3999 0.3681 0.3503 -0.0621 -0.0218 -0.1363 438 ASN B OD1 
7791 N ND2 . ASN B 438 ? 0.4110 0.3598 0.3355 -0.0819 -0.0281 -0.1723 438 ASN B ND2 
7792 N N   . ASP B 439 ? 0.4284 0.3400 0.4012 -0.0639 -0.0107 -0.1045 439 ASP B N   
7793 C CA  . ASP B 439 ? 0.3838 0.3161 0.3652 -0.0530 -0.0079 -0.0856 439 ASP B CA  
7794 C C   . ASP B 439 ? 0.3484 0.3155 0.3301 -0.0398 -0.0097 -0.0847 439 ASP B C   
7795 O O   . ASP B 439 ? 0.3003 0.2802 0.2872 -0.0302 -0.0073 -0.0713 439 ASP B O   
7796 C CB  . ASP B 439 ? 0.3534 0.2529 0.3299 -0.0403 -0.0029 -0.0753 439 ASP B CB  
7797 C CG  . ASP B 439 ? 0.4194 0.2869 0.3958 -0.0551 -0.0004 -0.0678 439 ASP B CG  
7798 O OD1 . ASP B 439 ? 0.4321 0.3132 0.4171 -0.0754 -0.0009 -0.0675 439 ASP B OD1 
7799 O OD2 . ASP B 439 ? 0.5582 0.3890 0.5271 -0.0465 0.0020  -0.0608 439 ASP B OD2 
7800 N N   . TYR B 440 ? 0.3425 0.3255 0.3169 -0.0398 -0.0135 -0.0975 440 TYR B N   
7801 C CA  . TYR B 440 ? 0.2959 0.3130 0.2710 -0.0306 -0.0150 -0.0918 440 TYR B CA  
7802 C C   . TYR B 440 ? 0.2555 0.3018 0.2453 -0.0377 -0.0193 -0.0798 440 TYR B C   
7803 O O   . TYR B 440 ? 0.2553 0.3230 0.2483 -0.0294 -0.0195 -0.0707 440 TYR B O   
7804 C CB  . TYR B 440 ? 0.3057 0.3333 0.2654 -0.0303 -0.0176 -0.1066 440 TYR B CB  
7805 C CG  . TYR B 440 ? 0.3262 0.3433 0.2762 -0.0138 -0.0099 -0.1133 440 TYR B CG  
7806 C CD1 . TYR B 440 ? 0.3639 0.4012 0.3179 -0.0013 -0.0064 -0.1026 440 TYR B CD1 
7807 C CD2 . TYR B 440 ? 0.3707 0.3575 0.3100 -0.0107 -0.0056 -0.1307 440 TYR B CD2 
7808 C CE1 . TYR B 440 ? 0.4209 0.4560 0.3712 0.0136  0.0010  -0.1082 440 TYR B CE1 
7809 C CE2 . TYR B 440 ? 0.4198 0.4012 0.3547 0.0072  0.0026  -0.1374 440 TYR B CE2 
7810 C CZ  . TYR B 440 ? 0.5009 0.5099 0.4429 0.0192  0.0059  -0.1255 440 TYR B CZ  
7811 O OH  . TYR B 440 ? 0.5486 0.5599 0.4913 0.0367  0.0145  -0.1316 440 TYR B OH  
7812 N N   . ILE B 441 ? 0.2487 0.2962 0.2491 -0.0527 -0.0219 -0.0798 441 ILE B N   
7813 C CA  . ILE B 441 ? 0.2416 0.3180 0.2609 -0.0564 -0.0238 -0.0685 441 ILE B CA  
7814 C C   . ILE B 441 ? 0.1967 0.2679 0.2213 -0.0472 -0.0157 -0.0556 441 ILE B C   
7815 O O   . ILE B 441 ? 0.2081 0.3012 0.2436 -0.0423 -0.0153 -0.0472 441 ILE B O   
7816 C CB  . ILE B 441 ? 0.2618 0.3459 0.2954 -0.0755 -0.0272 -0.0720 441 ILE B CB  
7817 C CG1 . ILE B 441 ? 0.2406 0.3651 0.2969 -0.0765 -0.0315 -0.0635 441 ILE B CG1 
7818 C CG2 . ILE B 441 ? 0.3034 0.3603 0.3395 -0.0834 -0.0186 -0.0683 441 ILE B CG2 
7819 C CD1 . ILE B 441 ? 0.3101 0.4606 0.3630 -0.0704 -0.0422 -0.0639 441 ILE B CD1 
7820 N N   . LEU B 442 ? 0.1959 0.2373 0.2116 -0.0443 -0.0097 -0.0540 442 LEU B N   
7821 C CA  . LEU B 442 ? 0.1837 0.2215 0.1993 -0.0362 -0.0038 -0.0423 442 LEU B CA  
7822 C C   . LEU B 442 ? 0.2235 0.2733 0.2351 -0.0218 -0.0048 -0.0395 442 LEU B C   
7823 O O   . LEU B 442 ? 0.2021 0.2629 0.2179 -0.0179 -0.0024 -0.0318 442 LEU B O   
7824 C CB  . LEU B 442 ? 0.2078 0.2114 0.2129 -0.0357 0.0003  -0.0388 442 LEU B CB  
7825 C CG  . LEU B 442 ? 0.2491 0.2324 0.2554 -0.0521 0.0028  -0.0389 442 LEU B CG  
7826 C CD1 . LEU B 442 ? 0.2882 0.2322 0.2810 -0.0480 0.0056  -0.0320 442 LEU B CD1 
7827 C CD2 . LEU B 442 ? 0.2517 0.2571 0.2716 -0.0642 0.0076  -0.0321 442 LEU B CD2 
7828 N N   . VAL B 443 ? 0.1699 0.2177 0.1729 -0.0152 -0.0075 -0.0468 443 VAL B N   
7829 C CA  . VAL B 443 ? 0.1788 0.2407 0.1790 -0.0044 -0.0076 -0.0441 443 VAL B CA  
7830 C C   . VAL B 443 ? 0.1916 0.2778 0.1993 -0.0066 -0.0105 -0.0388 443 VAL B C   
7831 O O   . VAL B 443 ? 0.1832 0.2769 0.1929 -0.0014 -0.0092 -0.0316 443 VAL B O   
7832 C CB  . VAL B 443 ? 0.2013 0.2614 0.1917 0.0012  -0.0078 -0.0545 443 VAL B CB  
7833 C CG1 . VAL B 443 ? 0.2136 0.2921 0.2028 0.0099  -0.0063 -0.0503 443 VAL B CG1 
7834 C CG2 . VAL B 443 ? 0.2080 0.2400 0.1936 0.0064  -0.0047 -0.0603 443 VAL B CG2 
7835 N N   . ALA B 444 ? 0.2074 0.3052 0.2199 -0.0145 -0.0154 -0.0421 444 ALA B N   
7836 C CA  . ALA B 444 ? 0.1768 0.2973 0.1981 -0.0143 -0.0201 -0.0356 444 ALA B CA  
7837 C C   . ALA B 444 ? 0.1762 0.3013 0.2134 -0.0136 -0.0166 -0.0281 444 ALA B C   
7838 O O   . ALA B 444 ? 0.1455 0.2842 0.1915 -0.0092 -0.0190 -0.0215 444 ALA B O   
7839 C CB  . ALA B 444 ? 0.2057 0.3409 0.2282 -0.0227 -0.0287 -0.0410 444 ALA B CB  
7840 N N   . GLU B 445 ? 0.1659 0.2788 0.2058 -0.0174 -0.0104 -0.0288 445 GLU B N   
7841 C CA  . GLU B 445 ? 0.1474 0.2651 0.1989 -0.0168 -0.0040 -0.0237 445 GLU B CA  
7842 C C   . GLU B 445 ? 0.1626 0.2704 0.2050 -0.0091 0.0005  -0.0197 445 GLU B C   
7843 O O   . GLU B 445 ? 0.1396 0.2493 0.1873 -0.0080 0.0067  -0.0177 445 GLU B O   
7844 C CB  . GLU B 445 ? 0.1723 0.2833 0.2275 -0.0270 0.0017  -0.0251 445 GLU B CB  
7845 C CG  . GLU B 445 ? 0.1502 0.2765 0.2196 -0.0379 -0.0031 -0.0295 445 GLU B CG  
7846 C CD  . GLU B 445 ? 0.2695 0.3817 0.3378 -0.0519 0.0012  -0.0317 445 GLU B CD  
7847 O OE1 . GLU B 445 ? 0.2512 0.3400 0.3060 -0.0516 0.0079  -0.0280 445 GLU B OE1 
7848 O OE2 . GLU B 445 ? 0.2623 0.3866 0.3427 -0.0643 -0.0030 -0.0365 445 GLU B OE2 
7849 N N   . GLY B 446 ? 0.1632 0.2633 0.1930 -0.0045 -0.0021 -0.0198 446 GLY B N   
7850 C CA  . GLY B 446 ? 0.1136 0.2083 0.1365 0.0002  0.0003  -0.0165 446 GLY B CA  
7851 C C   . GLY B 446 ? 0.1749 0.2771 0.2052 0.0030  0.0006  -0.0135 446 GLY B C   
7852 O O   . GLY B 446 ? 0.1567 0.2688 0.1945 0.0045  -0.0037 -0.0115 446 GLY B O   
7853 N N   . SER B 447 ? 0.1429 0.2380 0.1693 0.0037  0.0052  -0.0132 447 SER B N   
7854 C CA  . SER B 447 ? 0.1106 0.2056 0.1442 0.0067  0.0072  -0.0125 447 SER B CA  
7855 C C   . SER B 447 ? 0.1414 0.2365 0.1739 0.0084  0.0018  -0.0080 447 SER B C   
7856 O O   . SER B 447 ? 0.1657 0.2595 0.2067 0.0119  0.0010  -0.0047 447 SER B O   
7857 C CB  . SER B 447 ? 0.1463 0.2310 0.1713 0.0053  0.0138  -0.0164 447 SER B CB  
7858 O OG  . SER B 447 ? 0.1746 0.2539 0.1862 0.0026  0.0102  -0.0158 447 SER B OG  
7859 N N   . ASP B 448 ? 0.1132 0.2099 0.1363 0.0061  -0.0013 -0.0070 448 ASP B N   
7860 C CA  . ASP B 448 ? 0.1514 0.2495 0.1722 0.0047  -0.0041 -0.0019 448 ASP B CA  
7861 C C   . ASP B 448 ? 0.1423 0.2472 0.1675 0.0066  -0.0083 0.0043  448 ASP B C   
7862 O O   . ASP B 448 ? 0.1579 0.2577 0.1835 0.0061  -0.0099 0.0115  448 ASP B O   
7863 C CB  . ASP B 448 ? 0.1230 0.2292 0.1369 0.0026  -0.0051 -0.0025 448 ASP B CB  
7864 C CG  . ASP B 448 ? 0.1249 0.2278 0.1346 0.0020  -0.0040 -0.0063 448 ASP B CG  
7865 O OD1 . ASP B 448 ? 0.1875 0.2868 0.1953 0.0045  -0.0031 -0.0090 448 ASP B OD1 
7866 O OD2 . ASP B 448 ? 0.1778 0.2807 0.1855 -0.0024 -0.0046 -0.0057 448 ASP B OD2 
7867 N N   . TRP B 449 ? 0.1177 0.2327 0.1447 0.0078  -0.0112 0.0025  449 TRP B N   
7868 C CA  . TRP B 449 ? 0.1528 0.2779 0.1805 0.0085  -0.0176 0.0089  449 TRP B CA  
7869 C C   . TRP B 449 ? 0.1926 0.3138 0.2334 0.0138  -0.0198 0.0161  449 TRP B C   
7870 O O   . TRP B 449 ? 0.1658 0.2866 0.2050 0.0153  -0.0248 0.0267  449 TRP B O   
7871 C CB  . TRP B 449 ? 0.1241 0.2607 0.1515 0.0067  -0.0213 0.0030  449 TRP B CB  
7872 C CG  . TRP B 449 ? 0.1022 0.2348 0.1201 0.0044  -0.0174 -0.0064 449 TRP B CG  
7873 C CD1 . TRP B 449 ? 0.1952 0.3214 0.2158 0.0028  -0.0149 -0.0137 449 TRP B CD1 
7874 C CD2 . TRP B 449 ? 0.1050 0.2391 0.1112 0.0044  -0.0149 -0.0083 449 TRP B CD2 
7875 N NE1 . TRP B 449 ? 0.1543 0.2739 0.1652 0.0037  -0.0122 -0.0195 449 TRP B NE1 
7876 C CE2 . TRP B 449 ? 0.1478 0.2748 0.1516 0.0057  -0.0118 -0.0172 449 TRP B CE2 
7877 C CE3 . TRP B 449 ? 0.1301 0.2718 0.1289 0.0033  -0.0142 -0.0026 449 TRP B CE3 
7878 C CZ2 . TRP B 449 ? 0.1435 0.2725 0.1408 0.0089  -0.0083 -0.0217 449 TRP B CZ2 
7879 C CZ3 . TRP B 449 ? 0.1115 0.2593 0.1037 0.0041  -0.0095 -0.0076 449 TRP B CZ3 
7880 C CH2 . TRP B 449 ? 0.1811 0.3234 0.1741 0.0084  -0.0067 -0.0176 449 TRP B CH2 
7881 N N   . PHE B 450 ? 0.1590 0.2762 0.2124 0.0173  -0.0150 0.0109  450 PHE B N   
7882 C CA  . PHE B 450 ? 0.1448 0.2595 0.2149 0.0255  -0.0152 0.0154  450 PHE B CA  
7883 C C   . PHE B 450 ? 0.1875 0.2795 0.2540 0.0275  -0.0115 0.0182  450 PHE B C   
7884 O O   . PHE B 450 ? 0.1868 0.2710 0.2632 0.0351  -0.0143 0.0260  450 PHE B O   
7885 C CB  . PHE B 450 ? 0.1376 0.2593 0.2229 0.0281  -0.0086 0.0071  450 PHE B CB  
7886 C CG  . PHE B 450 ? 0.1110 0.2536 0.2027 0.0237  -0.0126 0.0047  450 PHE B CG  
7887 C CD1 . PHE B 450 ? 0.1361 0.2772 0.2153 0.0149  -0.0104 -0.0019 450 PHE B CD1 
7888 C CD2 . PHE B 450 ? 0.1500 0.3130 0.2599 0.0281  -0.0205 0.0100  450 PHE B CD2 
7889 C CE1 . PHE B 450 ? 0.2484 0.4044 0.3331 0.0087  -0.0146 -0.0051 450 PHE B CE1 
7890 C CE2 . PHE B 450 ? 0.2393 0.4225 0.3553 0.0213  -0.0258 0.0070  450 PHE B CE2 
7891 C CZ  . PHE B 450 ? 0.1515 0.3294 0.2542 0.0106  -0.0224 -0.0014 450 PHE B CZ  
7892 N N   . TRP B 451 ? 0.1962 0.2769 0.2494 0.0205  -0.0063 0.0120  451 TRP B N   
7893 C CA  . TRP B 451 ? 0.1436 0.2021 0.1914 0.0181  -0.0036 0.0127  451 TRP B CA  
7894 C C   . TRP B 451 ? 0.2006 0.2529 0.2450 0.0163  -0.0097 0.0265  451 TRP B C   
7895 O O   . TRP B 451 ? 0.2219 0.2531 0.2708 0.0198  -0.0097 0.0318  451 TRP B O   
7896 C CB  . TRP B 451 ? 0.1816 0.2382 0.2156 0.0085  -0.0004 0.0052  451 TRP B CB  
7897 C CG  . TRP B 451 ? 0.2192 0.2565 0.2466 0.0014  0.0009  0.0044  451 TRP B CG  
7898 C CD1 . TRP B 451 ? 0.2260 0.2625 0.2473 -0.0079 -0.0023 0.0115  451 TRP B CD1 
7899 C CD2 . TRP B 451 ? 0.2450 0.2615 0.2701 0.0006  0.0064  -0.0054 451 TRP B CD2 
7900 N NE1 . TRP B 451 ? 0.2992 0.3146 0.3162 -0.0158 -0.0002 0.0073  451 TRP B NE1 
7901 C CE2 . TRP B 451 ? 0.3277 0.3290 0.3454 -0.0104 0.0048  -0.0041 451 TRP B CE2 
7902 C CE3 . TRP B 451 ? 0.2836 0.2938 0.3113 0.0071  0.0137  -0.0162 451 TRP B CE3 
7903 C CZ2 . TRP B 451 ? 0.3852 0.3620 0.3967 -0.0156 0.0088  -0.0148 451 TRP B CZ2 
7904 C CZ3 . TRP B 451 ? 0.3754 0.3625 0.3956 0.0037  0.0191  -0.0271 451 TRP B CZ3 
7905 C CH2 . TRP B 451 ? 0.4130 0.3819 0.4243 -0.0077 0.0159  -0.0270 451 TRP B CH2 
7906 N N   . TRP B 452 ? 0.2267 0.2950 0.2615 0.0105  -0.0140 0.0323  452 TRP B N   
7907 C CA  . TRP B 452 ? 0.2396 0.3041 0.2662 0.0055  -0.0180 0.0463  452 TRP B CA  
7908 C C   . TRP B 452 ? 0.2566 0.3244 0.2879 0.0135  -0.0261 0.0596  452 TRP B C   
7909 O O   . TRP B 452 ? 0.2237 0.2801 0.2488 0.0112  -0.0297 0.0747  452 TRP B O   
7910 C CB  . TRP B 452 ? 0.2143 0.2981 0.2276 -0.0037 -0.0172 0.0462  452 TRP B CB  
7911 C CG  . TRP B 452 ? 0.1731 0.2576 0.1849 -0.0104 -0.0116 0.0362  452 TRP B CG  
7912 C CD1 . TRP B 452 ? 0.1592 0.2574 0.1707 -0.0092 -0.0095 0.0254  452 TRP B CD1 
7913 C CD2 . TRP B 452 ? 0.1650 0.2354 0.1758 -0.0197 -0.0089 0.0367  452 TRP B CD2 
7914 N NE1 . TRP B 452 ? 0.1735 0.2707 0.1847 -0.0155 -0.0068 0.0204  452 TRP B NE1 
7915 C CE2 . TRP B 452 ? 0.1468 0.2286 0.1576 -0.0234 -0.0065 0.0260  452 TRP B CE2 
7916 C CE3 . TRP B 452 ? 0.1961 0.2437 0.2062 -0.0261 -0.0091 0.0453  452 TRP B CE3 
7917 C CZ2 . TRP B 452 ? 0.2054 0.2821 0.2158 -0.0342 -0.0053 0.0230  452 TRP B CZ2 
7918 C CZ3 . TRP B 452 ? 0.2274 0.2655 0.2363 -0.0384 -0.0065 0.0409  452 TRP B CZ3 
7919 C CH2 . TRP B 452 ? 0.2450 0.3003 0.2544 -0.0428 -0.0052 0.0294  452 TRP B CH2 
7920 N N   . GLN B 453 ? 0.2202 0.3047 0.2622 0.0216  -0.0298 0.0557  453 GLN B N   
7921 C CA  . GLN B 453 ? 0.2433 0.3376 0.2924 0.0296  -0.0401 0.0683  453 GLN B CA  
7922 C C   . GLN B 453 ? 0.2387 0.3107 0.3038 0.0413  -0.0410 0.0768  453 GLN B C   
7923 O O   . GLN B 453 ? 0.2967 0.3539 0.3742 0.0466  -0.0328 0.0662  453 GLN B O   
7924 C CB  . GLN B 453 ? 0.1885 0.3087 0.2489 0.0330  -0.0436 0.0598  453 GLN B CB  
7925 C CG  . GLN B 453 ? 0.2676 0.4063 0.3422 0.0419  -0.0561 0.0705  453 GLN B CG  
7926 C CD  . GLN B 453 ? 0.3604 0.5105 0.4153 0.0371  -0.0679 0.0850  453 GLN B CD  
7927 O OE1 . GLN B 453 ? 0.3904 0.5382 0.4206 0.0263  -0.0648 0.0848  453 GLN B OE1 
7928 N NE2 . GLN B 453 ? 0.3741 0.5414 0.4402 0.0450  -0.0814 0.0968  453 GLN B NE2 
7929 N N   . GLY B 454 ? 0.3972 0.4653 0.4603 0.0458  -0.0509 0.0962  454 GLY B N   
7930 C CA  . GLY B 454 ? 0.5119 0.5556 0.5919 0.0600  -0.0530 0.1063  454 GLY B CA  
7931 C C   . GLY B 454 ? 0.5793 0.5829 0.6551 0.0562  -0.0431 0.1026  454 GLY B C   
7932 O O   . GLY B 454 ? 0.6167 0.5993 0.7101 0.0682  -0.0378 0.0960  454 GLY B O   
7933 N N   . GLU B 455 ? 0.5902 0.5841 0.6437 0.0390  -0.0400 0.1053  455 GLU B N   
7934 C CA  . GLU B 455 ? 0.6043 0.5628 0.6522 0.0302  -0.0319 0.1010  455 GLU B CA  
7935 C C   . GLU B 455 ? 0.7220 0.6614 0.7538 0.0194  -0.0360 0.1226  455 GLU B C   
7936 O O   . GLU B 455 ? 0.6761 0.6385 0.6918 0.0093  -0.0396 0.1329  455 GLU B O   
7937 C CB  . GLU B 455 ? 0.5215 0.4910 0.5608 0.0164  -0.0232 0.0819  455 GLU B CB  
7938 C CG  . GLU B 455 ? 0.4902 0.4702 0.5414 0.0244  -0.0174 0.0616  455 GLU B CG  
7939 C CD  . GLU B 455 ? 0.5705 0.5204 0.6344 0.0351  -0.0115 0.0532  455 GLU B CD  
7940 O OE1 . GLU B 455 ? 0.6308 0.5451 0.6915 0.0324  -0.0107 0.0585  455 GLU B OE1 
7941 O OE2 . GLU B 455 ? 0.5289 0.4897 0.6056 0.0453  -0.0065 0.0403  455 GLU B OE2 
7942 N N   . GLU B 456 ? 0.8130 0.7087 0.8482 0.0211  -0.0346 0.1292  456 GLU B N   
7943 C CA  . GLU B 456 ? 0.9537 0.8239 0.9729 0.0073  -0.0368 0.1504  456 GLU B CA  
7944 C C   . GLU B 456 ? 0.9712 0.8546 0.9742 -0.0181 -0.0297 0.1443  456 GLU B C   
7945 O O   . GLU B 456 ? 0.9920 0.8939 0.9789 -0.0308 -0.0312 0.1592  456 GLU B O   
7946 C CB  . GLU B 456 ? 1.0422 0.8561 1.0697 0.0132  -0.0351 0.1539  456 GLU B CB  
7947 C CG  . GLU B 456 ? 1.1248 0.9226 1.1683 0.0388  -0.0440 0.1696  456 GLU B CG  
7948 C CD  . GLU B 456 ? 1.1854 0.9440 1.2494 0.0556  -0.0376 0.1542  456 GLU B CD  
7949 O OE1 . GLU B 456 ? 1.1781 0.9520 1.2520 0.0596  -0.0290 0.1275  456 GLU B OE1 
7950 O OE2 . GLU B 456 ? 1.2296 0.9407 1.2986 0.0649  -0.0404 0.1686  456 GLU B OE2 
7951 N N   . LYS B 457 ? 0.9552 0.8328 0.9627 -0.0254 -0.0218 0.1223  457 LYS B N   
7952 C CA  . LYS B 457 ? 0.9529 0.8476 0.9512 -0.0477 -0.0162 0.1148  457 LYS B CA  
7953 C C   . LYS B 457 ? 0.8908 0.8343 0.8893 -0.0444 -0.0153 0.1030  457 LYS B C   
7954 O O   . LYS B 457 ? 0.8755 0.8275 0.8822 -0.0362 -0.0132 0.0843  457 LYS B O   
7955 C CB  . LYS B 457 ? 0.9599 0.8270 0.9618 -0.0572 -0.0107 0.0969  457 LYS B CB  
7956 C CG  . LYS B 457 ? 1.0147 0.8406 1.0103 -0.0758 -0.0094 0.1073  457 LYS B CG  
7957 C CD  . LYS B 457 ? 1.0384 0.8319 1.0362 -0.0843 -0.0052 0.0861  457 LYS B CD  
7958 C CE  . LYS B 457 ? 1.0666 0.8150 1.0718 -0.0642 -0.0043 0.0793  457 LYS B CE  
7959 N NZ  . LYS B 457 ? 1.1021 0.8131 1.1041 -0.0755 0.0007  0.0577  457 LYS B NZ  
7960 N N   . ALA B 458 ? 0.7810 0.7547 0.7688 -0.0511 -0.0160 0.1135  458 ALA B N   
7961 C CA  . ALA B 458 ? 0.6704 0.6849 0.6581 -0.0467 -0.0148 0.1015  458 ALA B CA  
7962 C C   . ALA B 458 ? 0.6586 0.7034 0.6337 -0.0595 -0.0112 0.1087  458 ALA B C   
7963 O O   . ALA B 458 ? 0.6081 0.6678 0.5714 -0.0564 -0.0142 0.1195  458 ALA B O   
7964 C CB  . ALA B 458 ? 0.6158 0.6395 0.6075 -0.0283 -0.0212 0.1012  458 ALA B CB  
7965 N N   . PRO B 459 ? 0.6320 0.6903 0.6096 -0.0738 -0.0045 0.1020  459 PRO B N   
7966 C CA  . PRO B 459 ? 0.5654 0.6579 0.5345 -0.0846 0.0016  0.1071  459 PRO B CA  
7967 C C   . PRO B 459 ? 0.4900 0.6153 0.4574 -0.0724 0.0027  0.0948  459 PRO B C   
7968 O O   . PRO B 459 ? 0.4586 0.5873 0.4364 -0.0620 0.0013  0.0786  459 PRO B O   
7969 C CB  . PRO B 459 ? 0.5894 0.6904 0.5692 -0.1010 0.0074  0.1007  459 PRO B CB  
7970 C CG  . PRO B 459 ? 0.5536 0.6388 0.5452 -0.0933 0.0034  0.0843  459 PRO B CG  
7971 C CD  . PRO B 459 ? 0.6193 0.6682 0.6082 -0.0800 -0.0025 0.0878  459 PRO B CD  
7972 N N   . PHE B 460 ? 0.4622 0.6092 0.4140 -0.0749 0.0056  0.1026  460 PHE B N   
7973 C CA  . PHE B 460 ? 0.4371 0.6113 0.3830 -0.0649 0.0072  0.0902  460 PHE B CA  
7974 C C   . PHE B 460 ? 0.3781 0.5399 0.3261 -0.0493 -0.0022 0.0833  460 PHE B C   
7975 O O   . PHE B 460 ? 0.4186 0.5942 0.3683 -0.0407 -0.0015 0.0680  460 PHE B O   
7976 C CB  . PHE B 460 ? 0.4418 0.6417 0.4011 -0.0640 0.0153  0.0732  460 PHE B CB  
7977 C CG  . PHE B 460 ? 0.4164 0.6387 0.3793 -0.0795 0.0253  0.0785  460 PHE B CG  
7978 C CD1 . PHE B 460 ? 0.5120 0.7526 0.4609 -0.0857 0.0320  0.0844  460 PHE B CD1 
7979 C CD2 . PHE B 460 ? 0.4569 0.6808 0.4393 -0.0871 0.0264  0.0746  460 PHE B CD2 
7980 C CE1 . PHE B 460 ? 0.5326 0.7897 0.4895 -0.0974 0.0397  0.0857  460 PHE B CE1 
7981 C CE2 . PHE B 460 ? 0.4575 0.7047 0.4477 -0.1019 0.0343  0.0782  460 PHE B CE2 
7982 C CZ  . PHE B 460 ? 0.4873 0.7482 0.4657 -0.1053 0.0405  0.0828  460 PHE B CZ  
7983 N N   . VAL B 461 ? 0.3246 0.4603 0.2741 -0.0456 -0.0106 0.0947  461 VAL B N   
7984 C CA  . VAL B 461 ? 0.3064 0.4361 0.2620 -0.0317 -0.0192 0.0895  461 VAL B CA  
7985 C C   . VAL B 461 ? 0.3440 0.4969 0.2844 -0.0289 -0.0230 0.0872  461 VAL B C   
7986 O O   . VAL B 461 ? 0.3401 0.4988 0.2867 -0.0206 -0.0269 0.0746  461 VAL B O   
7987 C CB  . VAL B 461 ? 0.3796 0.4813 0.3418 -0.0264 -0.0270 0.1041  461 VAL B CB  
7988 C CG1 . VAL B 461 ? 0.4435 0.5429 0.3878 -0.0317 -0.0322 0.1273  461 VAL B CG1 
7989 C CG2 . VAL B 461 ? 0.3792 0.4808 0.3553 -0.0118 -0.0343 0.0967  461 VAL B CG2 
7990 N N   . GLU B 462 ? 0.2788 0.4453 0.1972 -0.0374 -0.0216 0.0985  462 GLU B N   
7991 C CA  . GLU B 462 ? 0.3122 0.5016 0.2111 -0.0368 -0.0243 0.0929  462 GLU B CA  
7992 C C   . GLU B 462 ? 0.3634 0.5673 0.2668 -0.0332 -0.0165 0.0682  462 GLU B C   
7993 O O   . GLU B 462 ? 0.2935 0.5036 0.1921 -0.0290 -0.0204 0.0556  462 GLU B O   
7994 C CB  . GLU B 462 ? 0.3906 0.5870 0.2704 -0.0466 -0.0193 0.1018  462 GLU B CB  
7995 C CG  . GLU B 462 ? 0.5425 0.7219 0.4142 -0.0492 -0.0281 0.1262  462 GLU B CG  
7996 C CD  . GLU B 462 ? 0.6980 0.8572 0.5766 -0.0567 -0.0239 0.1424  462 GLU B CD  
7997 O OE1 . GLU B 462 ? 0.7113 0.8735 0.6015 -0.0613 -0.0145 0.1341  462 GLU B OE1 
7998 O OE2 . GLU B 462 ? 0.7199 0.8587 0.5926 -0.0586 -0.0301 0.1632  462 GLU B OE2 
7999 N N   . VAL B 463 ? 0.2419 0.4472 0.1579 -0.0347 -0.0059 0.0603  463 VAL B N   
8000 C CA  . VAL B 463 ? 0.2303 0.4473 0.1517 -0.0289 0.0011  0.0392  463 VAL B CA  
8001 C C   . VAL B 463 ? 0.1948 0.3959 0.1328 -0.0195 -0.0049 0.0284  463 VAL B C   
8002 O O   . VAL B 463 ? 0.2409 0.4448 0.1763 -0.0144 -0.0052 0.0137  463 VAL B O   
8003 C CB  . VAL B 463 ? 0.2833 0.5130 0.2154 -0.0325 0.0129  0.0362  463 VAL B CB  
8004 C CG1 . VAL B 463 ? 0.3210 0.5600 0.2618 -0.0226 0.0186  0.0161  463 VAL B CG1 
8005 C CG2 . VAL B 463 ? 0.2673 0.5130 0.1869 -0.0431 0.0203  0.0453  463 VAL B CG2 
8006 N N   . PHE B 464 ? 0.2455 0.4285 0.1994 -0.0181 -0.0086 0.0347  464 PHE B N   
8007 C CA  . PHE B 464 ? 0.1959 0.3658 0.1635 -0.0107 -0.0130 0.0263  464 PHE B CA  
8008 C C   . PHE B 464 ? 0.2256 0.3980 0.1887 -0.0082 -0.0217 0.0255  464 PHE B C   
8009 O O   . PHE B 464 ? 0.1822 0.3531 0.1507 -0.0049 -0.0231 0.0136  464 PHE B O   
8010 C CB  . PHE B 464 ? 0.1438 0.2949 0.1254 -0.0101 -0.0144 0.0329  464 PHE B CB  
8011 C CG  . PHE B 464 ? 0.1822 0.3313 0.1705 -0.0136 -0.0082 0.0296  464 PHE B CG  
8012 C CD1 . PHE B 464 ? 0.1671 0.3147 0.1632 -0.0091 -0.0062 0.0182  464 PHE B CD1 
8013 C CD2 . PHE B 464 ? 0.2000 0.3498 0.1862 -0.0228 -0.0052 0.0390  464 PHE B CD2 
8014 C CE1 . PHE B 464 ? 0.1470 0.2971 0.1490 -0.0125 -0.0031 0.0161  464 PHE B CE1 
8015 C CE2 . PHE B 464 ? 0.1949 0.3478 0.1890 -0.0281 -0.0012 0.0354  464 PHE B CE2 
8016 C CZ  . PHE B 464 ? 0.1727 0.3273 0.1749 -0.0222 -0.0010 0.0237  464 PHE B CZ  
8017 N N   . ASP B 465 ? 0.1877 0.3646 0.1409 -0.0108 -0.0284 0.0391  465 ASP B N   
8018 C CA  . ASP B 465 ? 0.1791 0.3643 0.1291 -0.0093 -0.0394 0.0400  465 ASP B CA  
8019 C C   . ASP B 465 ? 0.2260 0.4259 0.1581 -0.0132 -0.0389 0.0255  465 ASP B C   
8020 O O   . ASP B 465 ? 0.2059 0.4092 0.1417 -0.0130 -0.0451 0.0155  465 ASP B O   
8021 C CB  . ASP B 465 ? 0.2000 0.3866 0.1425 -0.0101 -0.0484 0.0611  465 ASP B CB  
8022 C CG  . ASP B 465 ? 0.2279 0.4264 0.1675 -0.0090 -0.0611 0.0625  465 ASP B CG  
8023 O OD1 . ASP B 465 ? 0.2352 0.4340 0.1962 -0.0023 -0.0689 0.0638  465 ASP B OD1 
8024 O OD2 . ASP B 465 ? 0.2667 0.4727 0.1853 -0.0151 -0.0613 0.0603  465 ASP B OD2 
8025 N N   . LYS B 466 ? 0.2263 0.4342 0.1401 -0.0176 -0.0304 0.0231  466 LYS B N   
8026 C CA  . LYS B 466 ? 0.2131 0.4264 0.1134 -0.0195 -0.0259 0.0055  466 LYS B CA  
8027 C C   . LYS B 466 ? 0.2036 0.4102 0.1135 -0.0147 -0.0223 -0.0134 466 LYS B C   
8028 O O   . LYS B 466 ? 0.2467 0.4499 0.1518 -0.0162 -0.0252 -0.0275 466 LYS B O   
8029 C CB  . LYS B 466 ? 0.2290 0.4518 0.1153 -0.0229 -0.0142 0.0053  466 LYS B CB  
8030 C CG  . LYS B 466 ? 0.4257 0.6533 0.2964 -0.0238 -0.0088 -0.0128 466 LYS B CG  
8031 C CD  . LYS B 466 ? 0.5040 0.7444 0.3637 -0.0269 0.0034  -0.0116 466 LYS B CD  
8032 C CE  . LYS B 466 ? 0.6437 0.8876 0.4834 -0.0281 0.0078  -0.0282 466 LYS B CE  
8033 N NZ  . LYS B 466 ? 0.7026 0.9367 0.5493 -0.0202 0.0128  -0.0509 466 LYS B NZ  
8034 N N   . LEU B 467 ? 0.1781 0.3761 0.1049 -0.0095 -0.0155 -0.0132 467 LEU B N   
8035 C CA  . LEU B 467 ? 0.1671 0.3514 0.1058 -0.0039 -0.0118 -0.0274 467 LEU B CA  
8036 C C   . LEU B 467 ? 0.1909 0.3646 0.1399 -0.0053 -0.0205 -0.0292 467 LEU B C   
8037 O O   . LEU B 467 ? 0.2360 0.4019 0.1827 -0.0065 -0.0212 -0.0429 467 LEU B O   
8038 C CB  . LEU B 467 ? 0.1494 0.3281 0.1042 0.0011  -0.0054 -0.0232 467 LEU B CB  
8039 C CG  . LEU B 467 ? 0.1758 0.3695 0.1271 0.0031  0.0047  -0.0256 467 LEU B CG  
8040 C CD1 . LEU B 467 ? 0.1753 0.3703 0.1430 0.0040  0.0076  -0.0175 467 LEU B CD1 
8041 C CD2 . LEU B 467 ? 0.2286 0.4210 0.1766 0.0107  0.0111  -0.0438 467 LEU B CD2 
8042 N N   . PHE B 468 ? 0.1838 0.3567 0.1456 -0.0055 -0.0262 -0.0159 468 PHE B N   
8043 C CA  . PHE B 468 ? 0.2224 0.3918 0.1986 -0.0066 -0.0327 -0.0167 468 PHE B CA  
8044 C C   . PHE B 468 ? 0.2009 0.3814 0.1680 -0.0133 -0.0413 -0.0242 468 PHE B C   
8045 O O   . PHE B 468 ? 0.2093 0.3840 0.1816 -0.0176 -0.0426 -0.0354 468 PHE B O   
8046 C CB  . PHE B 468 ? 0.2040 0.3752 0.1950 -0.0035 -0.0369 -0.0017 468 PHE B CB  
8047 C CG  . PHE B 468 ? 0.1707 0.3470 0.1800 -0.0037 -0.0429 -0.0020 468 PHE B CG  
8048 C CD1 . PHE B 468 ? 0.1597 0.3265 0.1825 -0.0039 -0.0372 -0.0088 468 PHE B CD1 
8049 C CD2 . PHE B 468 ? 0.1406 0.3345 0.1544 -0.0042 -0.0545 0.0058  468 PHE B CD2 
8050 C CE1 . PHE B 468 ? 0.1889 0.3654 0.2310 -0.0056 -0.0407 -0.0091 468 PHE B CE1 
8051 C CE2 . PHE B 468 ? 0.2410 0.4466 0.2772 -0.0042 -0.0598 0.0054  468 PHE B CE2 
8052 C CZ  . PHE B 468 ? 0.2222 0.4199 0.2733 -0.0055 -0.0518 -0.0027 468 PHE B CZ  
8053 N N   . ARG B 469 ? 0.1763 0.3725 0.1277 -0.0162 -0.0479 -0.0179 469 ARG B N   
8054 C CA  . ARG B 469 ? 0.1974 0.4017 0.1397 -0.0235 -0.0566 -0.0241 469 ARG B CA  
8055 C C   . ARG B 469 ? 0.3010 0.4970 0.2258 -0.0282 -0.0509 -0.0448 469 ARG B C   
8056 O O   . ARG B 469 ? 0.2452 0.4394 0.1682 -0.0358 -0.0568 -0.0557 469 ARG B O   
8057 C CB  . ARG B 469 ? 0.2597 0.4736 0.1896 -0.0242 -0.0627 -0.0094 469 ARG B CB  
8058 C CG  . ARG B 469 ? 0.2342 0.4518 0.1832 -0.0181 -0.0699 0.0101  469 ARG B CG  
8059 C CD  . ARG B 469 ? 0.2311 0.4542 0.1659 -0.0183 -0.0765 0.0261  469 ARG B CD  
8060 N NE  . ARG B 469 ? 0.2740 0.4967 0.2275 -0.0102 -0.0839 0.0448  469 ARG B NE  
8061 C CZ  . ARG B 469 ? 0.2594 0.4915 0.2294 -0.0068 -0.0958 0.0499  469 ARG B CZ  
8062 N NH1 . ARG B 469 ? 0.2443 0.4881 0.2135 -0.0134 -0.1024 0.0383  469 ARG B NH1 
8063 N NH2 . ARG B 469 ? 0.2446 0.4744 0.2328 0.0033  -0.1013 0.0664  469 ARG B NH2 
8064 N N   . SER B 470 ? 0.2160 0.4059 0.1297 -0.0234 -0.0393 -0.0512 470 SER B N   
8065 C CA  . SER B 470 ? 0.3146 0.4923 0.2150 -0.0241 -0.0321 -0.0722 470 SER B CA  
8066 C C   . SER B 470 ? 0.2649 0.4233 0.1786 -0.0246 -0.0318 -0.0841 470 SER B C   
8067 O O   . SER B 470 ? 0.2910 0.4380 0.1960 -0.0313 -0.0336 -0.1012 470 SER B O   
8068 C CB  . SER B 470 ? 0.3730 0.5513 0.2658 -0.0159 -0.0184 -0.0751 470 SER B CB  
8069 O OG  . SER B 470 ? 0.4749 0.6683 0.3546 -0.0186 -0.0172 -0.0643 470 SER B OG  
8070 N N   . PHE B 471 ? 0.2051 0.3539 0.1407 -0.0184 -0.0284 -0.0735 471 PHE B N   
8071 C CA  . PHE B 471 ? 0.2543 0.3806 0.2034 -0.0196 -0.0268 -0.0792 471 PHE B CA  
8072 C C   . PHE B 471 ? 0.2898 0.4214 0.2465 -0.0323 -0.0368 -0.0809 471 PHE B C   
8073 O O   . PHE B 471 ? 0.2491 0.3629 0.2065 -0.0399 -0.0368 -0.0926 471 PHE B O   
8074 C CB  . PHE B 471 ? 0.2292 0.3480 0.1957 -0.0118 -0.0216 -0.0665 471 PHE B CB  
8075 C CG  . PHE B 471 ? 0.2058 0.3233 0.1693 -0.0008 -0.0133 -0.0648 471 PHE B CG  
8076 C CD1 . PHE B 471 ? 0.2953 0.4018 0.2501 0.0054  -0.0069 -0.0779 471 PHE B CD1 
8077 C CD2 . PHE B 471 ? 0.2395 0.3667 0.2112 0.0033  -0.0118 -0.0511 471 PHE B CD2 
8078 C CE1 . PHE B 471 ? 0.2744 0.3865 0.2318 0.0163  0.0006  -0.0762 471 PHE B CE1 
8079 C CE2 . PHE B 471 ? 0.2028 0.3337 0.1749 0.0111  -0.0052 -0.0497 471 PHE B CE2 
8080 C CZ  . PHE B 471 ? 0.2276 0.3541 0.1942 0.0180  0.0009  -0.0617 471 PHE B CZ  
8081 N N   . VAL B 472 ? 0.2115 0.3678 0.1758 -0.0348 -0.0457 -0.0687 472 VAL B N   
8082 C CA  . VAL B 472 ? 0.2369 0.4081 0.2134 -0.0462 -0.0567 -0.0693 472 VAL B CA  
8083 C C   . VAL B 472 ? 0.2682 0.4399 0.2253 -0.0579 -0.0633 -0.0854 472 VAL B C   
8084 O O   . VAL B 472 ? 0.2709 0.4378 0.2355 -0.0701 -0.0676 -0.0939 472 VAL B O   
8085 C CB  . VAL B 472 ? 0.2882 0.4868 0.2780 -0.0420 -0.0653 -0.0515 472 VAL B CB  
8086 C CG1 . VAL B 472 ? 0.3585 0.5733 0.3591 -0.0505 -0.0768 -0.0500 472 VAL B CG1 
8087 C CG2 . VAL B 472 ? 0.2130 0.4056 0.2252 -0.0326 -0.0578 -0.0393 472 VAL B CG2 
8088 N N   . ARG B 473 ? 0.2840 0.4555 0.2166 -0.0540 -0.0614 -0.0877 473 ARG B N   
8089 C CA  . ARG B 473 ? 0.3104 0.4762 0.2232 -0.0632 -0.0651 -0.1017 473 ARG B CA  
8090 C C   . ARG B 473 ? 0.3483 0.4831 0.2535 -0.0670 -0.0575 -0.1235 473 ARG B C   
8091 O O   . ARG B 473 ? 0.3375 0.4618 0.2400 -0.0795 -0.0629 -0.1353 473 ARG B O   
8092 C CB  . ARG B 473 ? 0.3746 0.5491 0.2626 -0.0586 -0.0633 -0.0985 473 ARG B CB  
8093 C CG  . ARG B 473 ? 0.4655 0.6270 0.3267 -0.0645 -0.0609 -0.1182 473 ARG B CG  
8094 C CD  . ARG B 473 ? 0.5671 0.7431 0.4040 -0.0625 -0.0601 -0.1128 473 ARG B CD  
8095 N NE  . ARG B 473 ? 0.6982 0.8744 0.5310 -0.0511 -0.0460 -0.1082 473 ARG B NE  
8096 C CZ  . ARG B 473 ? 0.7584 0.9509 0.5960 -0.0461 -0.0456 -0.0877 473 ARG B CZ  
8097 N NH1 . ARG B 473 ? 0.7940 1.0009 0.6395 -0.0490 -0.0584 -0.0699 473 ARG B NH1 
8098 N NH2 . ARG B 473 ? 0.7336 0.9274 0.5694 -0.0381 -0.0325 -0.0849 473 ARG B NH2 
8099 N N   . ARG B 474 ? 0.3019 0.4200 0.2050 -0.0559 -0.0452 -0.1286 474 ARG B N   
8100 C CA  . ARG B 474 ? 0.3925 0.4748 0.2899 -0.0557 -0.0371 -0.1480 474 ARG B CA  
8101 C C   . ARG B 474 ? 0.3508 0.4151 0.2674 -0.0665 -0.0402 -0.1487 474 ARG B C   
8102 O O   . ARG B 474 ? 0.4243 0.4574 0.3346 -0.0745 -0.0384 -0.1653 474 ARG B O   
8103 C CB  . ARG B 474 ? 0.3621 0.4324 0.2591 -0.0370 -0.0234 -0.1484 474 ARG B CB  
8104 C CG  . ARG B 474 ? 0.5222 0.5500 0.4196 -0.0315 -0.0149 -0.1630 474 ARG B CG  
8105 C CD  . ARG B 474 ? 0.6563 0.6639 0.5311 -0.0316 -0.0102 -0.1858 474 ARG B CD  
8106 N NE  . ARG B 474 ? 0.7905 0.7573 0.6683 -0.0193 -0.0002 -0.1977 474 ARG B NE  
8107 C CZ  . ARG B 474 ? 0.8811 0.8087 0.7647 -0.0265 -0.0017 -0.2042 474 ARG B CZ  
8108 N NH1 . ARG B 474 ? 0.8709 0.7990 0.7588 -0.0483 -0.0121 -0.2014 474 ARG B NH1 
8109 N NH2 . ARG B 474 ? 0.9051 0.7928 0.7917 -0.0119 0.0071  -0.2114 474 ARG B NH2 
8110 N N   . ALA B 475 ? 0.2918 0.3721 0.2320 -0.0666 -0.0432 -0.1291 475 ALA B N   
8111 C CA  . ALA B 475 ? 0.2909 0.3579 0.2507 -0.0773 -0.0435 -0.1255 475 ALA B CA  
8112 C C   . ALA B 475 ? 0.3628 0.4336 0.3225 -0.0998 -0.0536 -0.1386 475 ALA B C   
8113 O O   . ALA B 475 ? 0.3748 0.4240 0.3446 -0.1122 -0.0516 -0.1416 475 ALA B O   
8114 C CB  . ALA B 475 ? 0.2646 0.3553 0.2484 -0.0729 -0.0438 -0.1043 475 ALA B CB  
8115 N N   . GLN B 476 ? 0.3727 0.4663 0.3216 -0.1031 -0.0632 -0.1406 476 GLN B N   
8116 C CA  . GLN B 476 ? 0.3648 0.4654 0.3169 -0.1197 -0.0738 -0.1452 476 GLN B CA  
8117 C C   . GLN B 476 ? 0.4576 0.5306 0.3824 -0.1255 -0.0742 -0.1656 476 GLN B C   
8118 O O   . GLN B 476 ? 0.4816 0.5603 0.4055 -0.1399 -0.0843 -0.1716 476 GLN B O   
8119 C CB  . GLN B 476 ? 0.3427 0.4863 0.3030 -0.1180 -0.0859 -0.1307 476 GLN B CB  
8120 C CG  . GLN B 476 ? 0.3660 0.5339 0.3459 -0.1049 -0.0842 -0.1107 476 GLN B CG  
8121 C CD  . GLN B 476 ? 0.3422 0.5457 0.3334 -0.1017 -0.0962 -0.0953 476 GLN B CD  
8122 O OE1 . GLN B 476 ? 0.3568 0.5747 0.3554 -0.1124 -0.1069 -0.0971 476 GLN B OE1 
8123 N NE2 . GLN B 476 ? 0.2940 0.5096 0.2859 -0.0867 -0.0949 -0.0804 476 GLN B NE2 
8124 N N   . GLU B 477 ? 0.4882 0.5330 0.3923 -0.1137 -0.0634 -0.1768 477 GLU B N   
8125 C CA  . GLU B 477 ? 0.6402 0.6602 0.5169 -0.1156 -0.0622 -0.1968 477 GLU B CA  
8126 C C   . GLU B 477 ? 0.6866 0.6543 0.5599 -0.1173 -0.0539 -0.2123 477 GLU B C   
8127 O O   . GLU B 477 ? 0.7174 0.6642 0.6018 -0.1087 -0.0445 -0.2081 477 GLU B O   
8128 C CB  . GLU B 477 ? 0.6598 0.6890 0.5145 -0.0990 -0.0551 -0.1983 477 GLU B CB  
8129 C CG  . GLU B 477 ? 0.6986 0.7718 0.5505 -0.0989 -0.0642 -0.1831 477 GLU B CG  
8130 C CD  . GLU B 477 ? 0.7626 0.8442 0.5925 -0.0855 -0.0557 -0.1829 477 GLU B CD  
8131 O OE1 . GLU B 477 ? 0.7777 0.8364 0.5997 -0.0739 -0.0418 -0.1935 477 GLU B OE1 
8132 O OE2 . GLU B 477 ? 0.7601 0.8715 0.5823 -0.0862 -0.0625 -0.1711 477 GLU B OE2 
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