data_9II1
# 
_entry.id   9II1 
# 
_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   9II1         pdb_00009ii1 10.2210/pdb9ii1/pdb 
WWPDB D_1300048792 ?            ?                   
# 
_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                        9II1 
_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' 57237.281 2   ? E256L ? ? 
2 branched    man 
;alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose
;
828.719   2   ? ?     ? ? 
3 branched    man 'alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose' 
666.578   1   ? ?     ? ? 
4 branched    man 'alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-beta-D-glucopyranose' 504.438   1   ? ?     ? ? 
5 non-polymer syn GLYCEROL 92.094    5   ? ?     ? ? 
6 water       nat water 18.015    549 ? ?     ? ? 
# 
_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
YFEIFGEHPVYMWPPLASVSNEALELYYEKGINMLATDEVILKNSVERASPYLRYYFRELISVFFRDKTLSDLIGFSYHA
WNAEDAVRDFIGRLKKIHESVDFQPVVFVVLDGENCWEYYEENGIPFLEKLYSTLEKEEWIETLTLEEAMRKEDVKTEVI
ESVKAGTWFDGNFLKWIGNKEKNEYWKILIEAKKKAKNDYILVAEGSDWFWWQGEEKAPFVEVFDKLFRSFVRRAQE
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MKKLFLVFWWHMHQPLYREPYTGEYLLPWTFFHAVKDYYDMPAYLKDFEIKLNFNLTPVLIDQIQEYAQGKAKDVFLEAI
RKDPDDLEKEEVEKLIEFTKLNYEKPIYRFERIRELMNKEKLNREELLDLQTLNLLAWCGRTLRKDLKDLLNKGRNYTQE
EKEYVLNKYFEIIKKTLSIYREIKEEGKGSVSTSPYYHPLIPILLNPNCVYETTPNVKIPDFAVSFREDASKHVELAKEK
YFEIFGEHPVYMWPPLASVSNEALELYYEKGINMLATDEVILKNSVERASPYLRYYFRELISVFFRDKTLSDLIGFSYHA
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 
5 GLYCEROL GOL 
6 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 LEU n 
1 257 ALA n 
1 258 SER n 
1 259 VAL n 
1 260 SER n 
1 261 ASN n 
1 262 GLU n 
1 263 ALA n 
1 264 LEU n 
1 265 GLU n 
1 266 LEU n 
1 267 TYR n 
1 268 TYR n 
1 269 GLU n 
1 270 LYS n 
1 271 GLY n 
1 272 ILE n 
1 273 ASN n 
1 274 MET n 
1 275 LEU n 
1 276 ALA n 
1 277 THR n 
1 278 ASP n 
1 279 GLU n 
1 280 VAL n 
1 281 ILE n 
1 282 LEU n 
1 283 LYS n 
1 284 ASN n 
1 285 SER n 
1 286 VAL n 
1 287 GLU n 
1 288 ARG n 
1 289 ALA n 
1 290 SER n 
1 291 PRO n 
1 292 TYR n 
1 293 LEU n 
1 294 ARG n 
1 295 TYR n 
1 296 TYR n 
1 297 PHE n 
1 298 ARG n 
1 299 GLU n 
1 300 LEU n 
1 301 ILE n 
1 302 SER n 
1 303 VAL n 
1 304 PHE n 
1 305 PHE n 
1 306 ARG n 
1 307 ASP n 
1 308 LYS n 
1 309 THR n 
1 310 LEU n 
1 311 SER n 
1 312 ASP n 
1 313 LEU n 
1 314 ILE n 
1 315 GLY n 
1 316 PHE n 
1 317 SER n 
1 318 TYR n 
1 319 HIS n 
1 320 ALA n 
1 321 TRP n 
1 322 ASN n 
1 323 ALA n 
1 324 GLU n 
1 325 ASP n 
1 326 ALA n 
1 327 VAL n 
1 328 ARG n 
1 329 ASP n 
1 330 PHE n 
1 331 ILE n 
1 332 GLY n 
1 333 ARG n 
1 334 LEU n 
1 335 LYS n 
1 336 LYS n 
1 337 ILE n 
1 338 HIS n 
1 339 GLU n 
1 340 SER n 
1 341 VAL n 
1 342 ASP n 
1 343 PHE n 
1 344 GLN n 
1 345 PRO n 
1 346 VAL n 
1 347 VAL n 
1 348 PHE n 
1 349 VAL n 
1 350 VAL n 
1 351 LEU n 
1 352 ASP n 
1 353 GLY n 
1 354 GLU n 
1 355 ASN n 
1 356 CYS n 
1 357 TRP n 
1 358 GLU n 
1 359 TYR n 
1 360 TYR n 
1 361 GLU n 
1 362 GLU n 
1 363 ASN n 
1 364 GLY n 
1 365 ILE n 
1 366 PRO n 
1 367 PHE n 
1 368 LEU n 
1 369 GLU n 
1 370 LYS n 
1 371 LEU n 
1 372 TYR n 
1 373 SER n 
1 374 THR n 
1 375 LEU n 
1 376 GLU n 
1 377 LYS n 
1 378 GLU n 
1 379 GLU n 
1 380 TRP n 
1 381 ILE n 
1 382 GLU n 
1 383 THR n 
1 384 LEU n 
1 385 THR n 
1 386 LEU n 
1 387 GLU n 
1 388 GLU n 
1 389 ALA n 
1 390 MET n 
1 391 ARG n 
1 392 LYS n 
1 393 GLU n 
1 394 ASP n 
1 395 VAL n 
1 396 LYS n 
1 397 THR n 
1 398 GLU n 
1 399 VAL n 
1 400 ILE n 
1 401 GLU n 
1 402 SER n 
1 403 VAL n 
1 404 LYS n 
1 405 ALA n 
1 406 GLY n 
1 407 THR n 
1 408 TRP n 
1 409 PHE n 
1 410 ASP n 
1 411 GLY n 
1 412 ASN n 
1 413 PHE n 
1 414 LEU n 
1 415 LYS n 
1 416 TRP n 
1 417 ILE n 
1 418 GLY n 
1 419 ASN n 
1 420 LYS n 
1 421 GLU n 
1 422 LYS n 
1 423 ASN n 
1 424 GLU n 
1 425 TYR n 
1 426 TRP n 
1 427 LYS n 
1 428 ILE n 
1 429 LEU n 
1 430 ILE n 
1 431 GLU n 
1 432 ALA n 
1 433 LYS n 
1 434 LYS n 
1 435 LYS n 
1 436 ALA n 
1 437 LYS n 
1 438 ASN n 
1 439 ASP n 
1 440 TYR n 
1 441 ILE n 
1 442 LEU n 
1 443 VAL n 
1 444 ALA n 
1 445 GLU n 
1 446 GLY n 
1 447 SER n 
1 448 ASP n 
1 449 TRP n 
1 450 PHE n 
1 451 TRP n 
1 452 TRP n 
1 453 GLN n 
1 454 GLY n 
1 455 GLU n 
1 456 GLU n 
1 457 LYS n 
1 458 ALA n 
1 459 PRO n 
1 460 PHE n 
1 461 VAL n 
1 462 GLU n 
1 463 VAL n 
1 464 PHE n 
1 465 ASP n 
1 466 LYS n 
1 467 LEU n 
1 468 PHE n 
1 469 ARG n 
1 470 SER n 
1 471 PHE n 
1 472 VAL n 
1 473 ARG n 
1 474 ARG n 
1 475 ALA n 
1 476 GLN n 
1 477 GLU n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   477 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 aq_720 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Aquifex aeolicus (strain VF5)' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     224324 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_pdbx_entity_branch.entity_id 
_pdbx_entity_branch.type 
2 oligosaccharide 
3 oligosaccharide 
4 oligosaccharide 
# 
loop_
_pdbx_entity_branch_descriptor.ordinal 
_pdbx_entity_branch_descriptor.entity_id 
_pdbx_entity_branch_descriptor.descriptor 
_pdbx_entity_branch_descriptor.type 
_pdbx_entity_branch_descriptor.program 
_pdbx_entity_branch_descriptor.program_version 
1 2 DGlcpa1-4DGlcpa1-4DGlcpa1-4DGlcpa1-4DGlcpa1-ROH                                              'Glycam Condensed Sequence' GMML 
1.0   
2 2 'WURCS=2.0/1,5,4/[a2122h-1a_1-5]/1-1-1-1-1/a4-b1_b4-c1_c4-d1_d4-e1'                          WURCS                       
PDB2Glycan 1.1.0 
3 2 '[][a-D-Glcp]{[(4+1)][a-D-Glcp]{[(4+1)][a-D-Glcp]{[(4+1)][a-D-Glcp]{[(4+1)][a-D-Glcp]{}}}}}' LINUCS                      
PDB-CARE   ?     
4 3 DGlcpa1-4DGlcpa1-4DGlcpa1-4DGlcpa1-ROH                                                       'Glycam Condensed Sequence' GMML 
1.0   
5 3 'WURCS=2.0/1,4,3/[a2122h-1a_1-5]/1-1-1-1/a4-b1_b4-c1_c4-d1'                                  WURCS                       
PDB2Glycan 1.1.0 
6 3 '[][a-D-Glcp]{[(4+1)][a-D-Glcp]{[(4+1)][a-D-Glcp]{[(4+1)][a-D-Glcp]{}}}}'                    LINUCS                      
PDB-CARE   ?     
7 4 DGlcpa1-4DGlcpa1-4DGlcpb1-ROH                                                                'Glycam Condensed Sequence' GMML 
1.0   
8 4 'WURCS=2.0/2,3,2/[a2122h-1b_1-5][a2122h-1a_1-5]/1-2-2/a4-b1_b4-c1'                           WURCS                       
PDB2Glycan 1.1.0 
9 4 '[][b-D-Glcp]{[(4+1)][a-D-Glcp]{[(4+1)][a-D-Glcp]{}}}'                                       LINUCS                      
PDB-CARE   ?     
# 
loop_
_pdbx_entity_branch_link.link_id 
_pdbx_entity_branch_link.entity_id 
_pdbx_entity_branch_link.entity_branch_list_num_1 
_pdbx_entity_branch_link.comp_id_1 
_pdbx_entity_branch_link.atom_id_1 
_pdbx_entity_branch_link.leaving_atom_id_1 
_pdbx_entity_branch_link.entity_branch_list_num_2 
_pdbx_entity_branch_link.comp_id_2 
_pdbx_entity_branch_link.atom_id_2 
_pdbx_entity_branch_link.leaving_atom_id_2 
_pdbx_entity_branch_link.value_order 
_pdbx_entity_branch_link.details 
1 2 2 GLC C1 O1 1 GLC O4 HO4 sing ? 
2 2 3 GLC C1 O1 2 GLC O4 HO4 sing ? 
3 2 4 GLC C1 O1 3 GLC O4 HO4 sing ? 
4 2 5 GLC C1 O1 4 GLC O4 HO4 sing ? 
5 3 2 GLC C1 O1 1 GLC O4 HO4 sing ? 
6 3 3 GLC C1 O1 2 GLC O4 HO4 sing ? 
7 3 4 GLC C1 O1 3 GLC O4 HO4 sing ? 
8 4 2 GLC C1 O1 1 BGC O4 HO4 sing ? 
9 4 3 GLC 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 
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 
BGC 'D-saccharide, beta linking'  . beta-D-glucopyranose  'beta-D-glucose; D-glucose; glucose'  'C6 H12 O6'      180.156 
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 
BGC 'CONDENSED IUPAC CARBOHYDRATE SYMBOL' GMML     1.0 DGlcpb            
BGC 'COMMON NAME'                         GMML     1.0 b-D-glucopyranose 
BGC 'IUPAC CARBOHYDRATE SYMBOL'           PDB-CARE 1.0 b-D-Glcp          
BGC 'SNFG CARBOHYDRATE SYMBOL'            GMML     1.0 Glc               
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 LEU 256 256 256 LEU LEU 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 LEU 256 256 256 LEU LEU 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 C GLC 1 n 
C 2 GLC 2 C GLC 2 C GLC 2 n 
C 2 GLC 3 C GLC 3 C GLC 3 n 
C 2 GLC 4 C GLC 4 C GLC 4 n 
C 2 GLC 5 C GLC 5 C GLC 5 n 
D 3 GLC 1 D GLC 1 D GLC 1 n 
D 3 GLC 2 D GLC 2 D GLC 2 n 
D 3 GLC 3 D GLC 3 D GLC 3 n 
D 3 GLC 4 D GLC 4 D GLC 4 n 
E 2 GLC 1 E GLC 1 E GLC 1 n 
E 2 GLC 2 E GLC 2 E GLC 2 n 
E 2 GLC 3 E GLC 3 E GLC 3 n 
E 2 GLC 4 E GLC 4 E GLC 4 n 
E 2 GLC 5 E GLC 5 E GLC 5 n 
F 4 BGC 1 G BGC 1 F GLC 1 n 
F 4 GLC 2 G GLC 2 F GLC 2 n 
F 4 GLC 3 G GLC 3 F GLC 3 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 GOL ? ? GOL ? ? '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 
G 5 GOL 1   501 1   GOL GOL A . 
H 5 GOL 1   502 2   GOL GOL A . 
I 5 GOL 1   503 3   GOL GOL A . 
J 5 GOL 1   504 5   GOL GOL A . 
K 5 GOL 1   501 4   GOL GOL B . 
L 6 HOH 1   601 472 HOH HOH A . 
L 6 HOH 2   602 360 HOH HOH A . 
L 6 HOH 3   603 240 HOH HOH A . 
L 6 HOH 4   604 438 HOH HOH A . 
L 6 HOH 5   605 138 HOH HOH A . 
L 6 HOH 6   606 451 HOH HOH A . 
L 6 HOH 7   607 39  HOH HOH A . 
L 6 HOH 8   608 169 HOH HOH A . 
L 6 HOH 9   609 491 HOH HOH A . 
L 6 HOH 10  610 188 HOH HOH A . 
L 6 HOH 11  611 405 HOH HOH A . 
L 6 HOH 12  612 385 HOH HOH A . 
L 6 HOH 13  613 80  HOH HOH A . 
L 6 HOH 14  614 235 HOH HOH A . 
L 6 HOH 15  615 165 HOH HOH A . 
L 6 HOH 16  616 168 HOH HOH A . 
L 6 HOH 17  617 218 HOH HOH A . 
L 6 HOH 18  618 514 HOH HOH A . 
L 6 HOH 19  619 321 HOH HOH A . 
L 6 HOH 20  620 239 HOH HOH A . 
L 6 HOH 21  621 155 HOH HOH A . 
L 6 HOH 22  622 199 HOH HOH A . 
L 6 HOH 23  623 185 HOH HOH A . 
L 6 HOH 24  624 133 HOH HOH A . 
L 6 HOH 25  625 142 HOH HOH A . 
L 6 HOH 26  626 307 HOH HOH A . 
L 6 HOH 27  627 323 HOH HOH A . 
L 6 HOH 28  628 47  HOH HOH A . 
L 6 HOH 29  629 375 HOH HOH A . 
L 6 HOH 30  630 117 HOH HOH A . 
L 6 HOH 31  631 141 HOH HOH A . 
L 6 HOH 32  632 8   HOH HOH A . 
L 6 HOH 33  633 325 HOH HOH A . 
L 6 HOH 34  634 462 HOH HOH A . 
L 6 HOH 35  635 179 HOH HOH A . 
L 6 HOH 36  636 209 HOH HOH A . 
L 6 HOH 37  637 447 HOH HOH A . 
L 6 HOH 38  638 23  HOH HOH A . 
L 6 HOH 39  639 508 HOH HOH A . 
L 6 HOH 40  640 126 HOH HOH A . 
L 6 HOH 41  641 374 HOH HOH A . 
L 6 HOH 42  642 125 HOH HOH A . 
L 6 HOH 43  643 507 HOH HOH A . 
L 6 HOH 44  644 13  HOH HOH A . 
L 6 HOH 45  645 145 HOH HOH A . 
L 6 HOH 46  646 467 HOH HOH A . 
L 6 HOH 47  647 115 HOH HOH A . 
L 6 HOH 48  648 267 HOH HOH A . 
L 6 HOH 49  649 78  HOH HOH A . 
L 6 HOH 50  650 399 HOH HOH A . 
L 6 HOH 51  651 522 HOH HOH A . 
L 6 HOH 52  652 53  HOH HOH A . 
L 6 HOH 53  653 96  HOH HOH A . 
L 6 HOH 54  654 120 HOH HOH A . 
L 6 HOH 55  655 183 HOH HOH A . 
L 6 HOH 56  656 252 HOH HOH A . 
L 6 HOH 57  657 229 HOH HOH A . 
L 6 HOH 58  658 300 HOH HOH A . 
L 6 HOH 59  659 489 HOH HOH A . 
L 6 HOH 60  660 109 HOH HOH A . 
L 6 HOH 61  661 212 HOH HOH A . 
L 6 HOH 62  662 242 HOH HOH A . 
L 6 HOH 63  663 537 HOH HOH A . 
L 6 HOH 64  664 36  HOH HOH A . 
L 6 HOH 65  665 61  HOH HOH A . 
L 6 HOH 66  666 487 HOH HOH A . 
L 6 HOH 67  667 343 HOH HOH A . 
L 6 HOH 68  668 431 HOH HOH A . 
L 6 HOH 69  669 131 HOH HOH A . 
L 6 HOH 70  670 520 HOH HOH A . 
L 6 HOH 71  671 435 HOH HOH A . 
L 6 HOH 72  672 205 HOH HOH A . 
L 6 HOH 73  673 154 HOH HOH A . 
L 6 HOH 74  674 135 HOH HOH A . 
L 6 HOH 75  675 192 HOH HOH A . 
L 6 HOH 76  676 305 HOH HOH A . 
L 6 HOH 77  677 3   HOH HOH A . 
L 6 HOH 78  678 49  HOH HOH A . 
L 6 HOH 79  679 68  HOH HOH A . 
L 6 HOH 80  680 28  HOH HOH A . 
L 6 HOH 81  681 25  HOH HOH A . 
L 6 HOH 82  682 228 HOH HOH A . 
L 6 HOH 83  683 4   HOH HOH A . 
L 6 HOH 84  684 340 HOH HOH A . 
L 6 HOH 85  685 224 HOH HOH A . 
L 6 HOH 86  686 24  HOH HOH A . 
L 6 HOH 87  687 130 HOH HOH A . 
L 6 HOH 88  688 64  HOH HOH A . 
L 6 HOH 89  689 7   HOH HOH A . 
L 6 HOH 90  690 544 HOH HOH A . 
L 6 HOH 91  691 22  HOH HOH A . 
L 6 HOH 92  692 107 HOH HOH A . 
L 6 HOH 93  693 44  HOH HOH A . 
L 6 HOH 94  694 6   HOH HOH A . 
L 6 HOH 95  695 281 HOH HOH A . 
L 6 HOH 96  696 503 HOH HOH A . 
L 6 HOH 97  697 226 HOH HOH A . 
L 6 HOH 98  698 440 HOH HOH A . 
L 6 HOH 99  699 525 HOH HOH A . 
L 6 HOH 100 700 72  HOH HOH A . 
L 6 HOH 101 701 81  HOH HOH A . 
L 6 HOH 102 702 241 HOH HOH A . 
L 6 HOH 103 703 90  HOH HOH A . 
L 6 HOH 104 704 71  HOH HOH A . 
L 6 HOH 105 705 79  HOH HOH A . 
L 6 HOH 106 706 17  HOH HOH A . 
L 6 HOH 107 707 234 HOH HOH A . 
L 6 HOH 108 708 27  HOH HOH A . 
L 6 HOH 109 709 112 HOH HOH A . 
L 6 HOH 110 710 87  HOH HOH A . 
L 6 HOH 111 711 279 HOH HOH A . 
L 6 HOH 112 712 1   HOH HOH A . 
L 6 HOH 113 713 425 HOH HOH A . 
L 6 HOH 114 714 153 HOH HOH A . 
L 6 HOH 115 715 410 HOH HOH A . 
L 6 HOH 116 716 86  HOH HOH A . 
L 6 HOH 117 717 511 HOH HOH A . 
L 6 HOH 118 718 46  HOH HOH A . 
L 6 HOH 119 719 346 HOH HOH A . 
L 6 HOH 120 720 369 HOH HOH A . 
L 6 HOH 121 721 294 HOH HOH A . 
L 6 HOH 122 722 388 HOH HOH A . 
L 6 HOH 123 723 414 HOH HOH A . 
L 6 HOH 124 724 251 HOH HOH A . 
L 6 HOH 125 725 63  HOH HOH A . 
L 6 HOH 126 726 62  HOH HOH A . 
L 6 HOH 127 727 513 HOH HOH A . 
L 6 HOH 128 728 95  HOH HOH A . 
L 6 HOH 129 729 210 HOH HOH A . 
L 6 HOH 130 730 76  HOH HOH A . 
L 6 HOH 131 731 355 HOH HOH A . 
L 6 HOH 132 732 144 HOH HOH A . 
L 6 HOH 133 733 140 HOH HOH A . 
L 6 HOH 134 734 197 HOH HOH A . 
L 6 HOH 135 735 123 HOH HOH A . 
L 6 HOH 136 736 11  HOH HOH A . 
L 6 HOH 137 737 160 HOH HOH A . 
L 6 HOH 138 738 148 HOH HOH A . 
L 6 HOH 139 739 5   HOH HOH A . 
L 6 HOH 140 740 253 HOH HOH A . 
L 6 HOH 141 741 132 HOH HOH A . 
L 6 HOH 142 742 171 HOH HOH A . 
L 6 HOH 143 743 266 HOH HOH A . 
L 6 HOH 144 744 453 HOH HOH A . 
L 6 HOH 145 745 93  HOH HOH A . 
L 6 HOH 146 746 166 HOH HOH A . 
L 6 HOH 147 747 111 HOH HOH A . 
L 6 HOH 148 748 134 HOH HOH A . 
L 6 HOH 149 749 246 HOH HOH A . 
L 6 HOH 150 750 89  HOH HOH A . 
L 6 HOH 151 751 116 HOH HOH A . 
L 6 HOH 152 752 466 HOH HOH A . 
L 6 HOH 153 753 14  HOH HOH A . 
L 6 HOH 154 754 531 HOH HOH A . 
L 6 HOH 155 755 350 HOH HOH A . 
L 6 HOH 156 756 190 HOH HOH A . 
L 6 HOH 157 757 376 HOH HOH A . 
L 6 HOH 158 758 211 HOH HOH A . 
L 6 HOH 159 759 232 HOH HOH A . 
L 6 HOH 160 760 180 HOH HOH A . 
L 6 HOH 161 761 398 HOH HOH A . 
L 6 HOH 162 762 175 HOH HOH A . 
L 6 HOH 163 763 261 HOH HOH A . 
L 6 HOH 164 764 83  HOH HOH A . 
L 6 HOH 165 765 339 HOH HOH A . 
L 6 HOH 166 766 20  HOH HOH A . 
L 6 HOH 167 767 113 HOH HOH A . 
L 6 HOH 168 768 70  HOH HOH A . 
L 6 HOH 169 769 282 HOH HOH A . 
L 6 HOH 170 770 391 HOH HOH A . 
L 6 HOH 171 771 233 HOH HOH A . 
L 6 HOH 172 772 191 HOH HOH A . 
L 6 HOH 173 773 314 HOH HOH A . 
L 6 HOH 174 774 274 HOH HOH A . 
L 6 HOH 175 775 352 HOH HOH A . 
L 6 HOH 176 776 301 HOH HOH A . 
L 6 HOH 177 777 216 HOH HOH A . 
L 6 HOH 178 778 67  HOH HOH A . 
L 6 HOH 179 779 2   HOH HOH A . 
L 6 HOH 180 780 225 HOH HOH A . 
L 6 HOH 181 781 485 HOH HOH A . 
L 6 HOH 182 782 73  HOH HOH A . 
L 6 HOH 183 783 335 HOH HOH A . 
L 6 HOH 184 784 459 HOH HOH A . 
L 6 HOH 185 785 162 HOH HOH A . 
L 6 HOH 186 786 12  HOH HOH A . 
L 6 HOH 187 787 104 HOH HOH A . 
L 6 HOH 188 788 193 HOH HOH A . 
L 6 HOH 189 789 331 HOH HOH A . 
L 6 HOH 190 790 100 HOH HOH A . 
L 6 HOH 191 791 270 HOH HOH A . 
L 6 HOH 192 792 395 HOH HOH A . 
L 6 HOH 193 793 439 HOH HOH A . 
L 6 HOH 194 794 159 HOH HOH A . 
L 6 HOH 195 795 455 HOH HOH A . 
L 6 HOH 196 796 48  HOH HOH A . 
L 6 HOH 197 797 315 HOH HOH A . 
L 6 HOH 198 798 257 HOH HOH A . 
L 6 HOH 199 799 157 HOH HOH A . 
L 6 HOH 200 800 289 HOH HOH A . 
L 6 HOH 201 801 476 HOH HOH A . 
L 6 HOH 202 802 215 HOH HOH A . 
L 6 HOH 203 803 436 HOH HOH A . 
L 6 HOH 204 804 303 HOH HOH A . 
L 6 HOH 205 805 392 HOH HOH A . 
L 6 HOH 206 806 29  HOH HOH A . 
L 6 HOH 207 807 94  HOH HOH A . 
L 6 HOH 208 808 247 HOH HOH A . 
L 6 HOH 209 809 161 HOH HOH A . 
L 6 HOH 210 810 265 HOH HOH A . 
L 6 HOH 211 811 186 HOH HOH A . 
L 6 HOH 212 812 156 HOH HOH A . 
L 6 HOH 213 813 291 HOH HOH A . 
L 6 HOH 214 814 416 HOH HOH A . 
L 6 HOH 215 815 231 HOH HOH A . 
L 6 HOH 216 816 382 HOH HOH A . 
L 6 HOH 217 817 319 HOH HOH A . 
L 6 HOH 218 818 18  HOH HOH A . 
L 6 HOH 219 819 184 HOH HOH A . 
L 6 HOH 220 820 535 HOH HOH A . 
L 6 HOH 221 821 345 HOH HOH A . 
L 6 HOH 222 822 534 HOH HOH A . 
L 6 HOH 223 823 418 HOH HOH A . 
L 6 HOH 224 824 313 HOH HOH A . 
L 6 HOH 225 825 295 HOH HOH A . 
L 6 HOH 226 826 429 HOH HOH A . 
L 6 HOH 227 827 469 HOH HOH A . 
L 6 HOH 228 828 349 HOH HOH A . 
L 6 HOH 229 829 164 HOH HOH A . 
L 6 HOH 230 830 516 HOH HOH A . 
L 6 HOH 231 831 299 HOH HOH A . 
L 6 HOH 232 832 34  HOH HOH A . 
L 6 HOH 233 833 452 HOH HOH A . 
L 6 HOH 234 834 377 HOH HOH A . 
L 6 HOH 235 835 458 HOH HOH A . 
L 6 HOH 236 836 370 HOH HOH A . 
L 6 HOH 237 837 493 HOH HOH A . 
L 6 HOH 238 838 286 HOH HOH A . 
L 6 HOH 239 839 322 HOH HOH A . 
L 6 HOH 240 840 309 HOH HOH A . 
L 6 HOH 241 841 483 HOH HOH A . 
L 6 HOH 242 842 368 HOH HOH A . 
L 6 HOH 243 843 498 HOH HOH A . 
L 6 HOH 244 844 417 HOH HOH A . 
L 6 HOH 245 845 428 HOH HOH A . 
L 6 HOH 246 846 214 HOH HOH A . 
L 6 HOH 247 847 207 HOH HOH A . 
L 6 HOH 248 848 426 HOH HOH A . 
L 6 HOH 249 849 542 HOH HOH A . 
L 6 HOH 250 850 35  HOH HOH A . 
L 6 HOH 251 851 238 HOH HOH A . 
L 6 HOH 252 852 545 HOH HOH A . 
L 6 HOH 253 853 541 HOH HOH A . 
L 6 HOH 254 854 320 HOH HOH A . 
L 6 HOH 255 855 538 HOH HOH A . 
L 6 HOH 256 856 328 HOH HOH A . 
L 6 HOH 257 857 502 HOH HOH A . 
L 6 HOH 258 858 423 HOH HOH A . 
L 6 HOH 259 859 481 HOH HOH A . 
L 6 HOH 260 860 490 HOH HOH A . 
L 6 HOH 261 861 530 HOH HOH A . 
L 6 HOH 262 862 103 HOH HOH A . 
L 6 HOH 263 863 519 HOH HOH A . 
L 6 HOH 264 864 427 HOH HOH A . 
L 6 HOH 265 865 397 HOH HOH A . 
L 6 HOH 266 866 486 HOH HOH A . 
L 6 HOH 267 867 378 HOH HOH A . 
L 6 HOH 268 868 549 HOH HOH A . 
L 6 HOH 269 869 480 HOH HOH A . 
L 6 HOH 270 870 311 HOH HOH A . 
L 6 HOH 271 871 353 HOH HOH A . 
L 6 HOH 272 872 536 HOH HOH A . 
L 6 HOH 273 873 448 HOH HOH A . 
L 6 HOH 274 874 505 HOH HOH A . 
L 6 HOH 275 875 278 HOH HOH A . 
L 6 HOH 276 876 404 HOH HOH A . 
L 6 HOH 277 877 449 HOH HOH A . 
L 6 HOH 278 878 237 HOH HOH A . 
L 6 HOH 279 879 504 HOH HOH A . 
L 6 HOH 280 880 381 HOH HOH A . 
L 6 HOH 281 881 450 HOH HOH A . 
L 6 HOH 282 882 406 HOH HOH A . 
L 6 HOH 283 883 527 HOH HOH A . 
L 6 HOH 284 884 499 HOH HOH A . 
L 6 HOH 285 885 367 HOH HOH A . 
L 6 HOH 286 886 518 HOH HOH A . 
L 6 HOH 287 887 338 HOH HOH A . 
L 6 HOH 288 888 411 HOH HOH A . 
L 6 HOH 289 889 532 HOH HOH A . 
L 6 HOH 290 890 260 HOH HOH A . 
L 6 HOH 291 891 533 HOH HOH A . 
L 6 HOH 292 892 195 HOH HOH A . 
L 6 HOH 293 893 543 HOH HOH A . 
L 6 HOH 294 894 393 HOH HOH A . 
M 6 HOH 1   601 219 HOH HOH B . 
M 6 HOH 2   602 433 HOH HOH B . 
M 6 HOH 3   603 342 HOH HOH B . 
M 6 HOH 4   604 280 HOH HOH B . 
M 6 HOH 5   605 333 HOH HOH B . 
M 6 HOH 6   606 442 HOH HOH B . 
M 6 HOH 7   607 254 HOH HOH B . 
M 6 HOH 8   608 383 HOH HOH B . 
M 6 HOH 9   609 220 HOH HOH B . 
M 6 HOH 10  610 84  HOH HOH B . 
M 6 HOH 11  611 122 HOH HOH B . 
M 6 HOH 12  612 163 HOH HOH B . 
M 6 HOH 13  613 92  HOH HOH B . 
M 6 HOH 14  614 341 HOH HOH B . 
M 6 HOH 15  615 528 HOH HOH B . 
M 6 HOH 16  616 302 HOH HOH B . 
M 6 HOH 17  617 150 HOH HOH B . 
M 6 HOH 18  618 524 HOH HOH B . 
M 6 HOH 19  619 151 HOH HOH B . 
M 6 HOH 20  620 102 HOH HOH B . 
M 6 HOH 21  621 98  HOH HOH B . 
M 6 HOH 22  622 222 HOH HOH B . 
M 6 HOH 23  623 60  HOH HOH B . 
M 6 HOH 24  624 110 HOH HOH B . 
M 6 HOH 25  625 263 HOH HOH B . 
M 6 HOH 26  626 510 HOH HOH B . 
M 6 HOH 27  627 196 HOH HOH B . 
M 6 HOH 28  628 517 HOH HOH B . 
M 6 HOH 29  629 318 HOH HOH B . 
M 6 HOH 30  630 500 HOH HOH B . 
M 6 HOH 31  631 15  HOH HOH B . 
M 6 HOH 32  632 316 HOH HOH B . 
M 6 HOH 33  633 152 HOH HOH B . 
M 6 HOH 34  634 129 HOH HOH B . 
M 6 HOH 35  635 420 HOH HOH B . 
M 6 HOH 36  636 32  HOH HOH B . 
M 6 HOH 37  637 213 HOH HOH B . 
M 6 HOH 38  638 363 HOH HOH B . 
M 6 HOH 39  639 99  HOH HOH B . 
M 6 HOH 40  640 475 HOH HOH B . 
M 6 HOH 41  641 137 HOH HOH B . 
M 6 HOH 42  642 460 HOH HOH B . 
M 6 HOH 43  643 101 HOH HOH B . 
M 6 HOH 44  644 200 HOH HOH B . 
M 6 HOH 45  645 362 HOH HOH B . 
M 6 HOH 46  646 143 HOH HOH B . 
M 6 HOH 47  647 268 HOH HOH B . 
M 6 HOH 48  648 419 HOH HOH B . 
M 6 HOH 49  649 548 HOH HOH B . 
M 6 HOH 50  650 371 HOH HOH B . 
M 6 HOH 51  651 444 HOH HOH B . 
M 6 HOH 52  652 172 HOH HOH B . 
M 6 HOH 53  653 492 HOH HOH B . 
M 6 HOH 54  654 304 HOH HOH B . 
M 6 HOH 55  655 57  HOH HOH B . 
M 6 HOH 56  656 114 HOH HOH B . 
M 6 HOH 57  657 54  HOH HOH B . 
M 6 HOH 58  658 167 HOH HOH B . 
M 6 HOH 59  659 75  HOH HOH B . 
M 6 HOH 60  660 244 HOH HOH B . 
M 6 HOH 61  661 74  HOH HOH B . 
M 6 HOH 62  662 293 HOH HOH B . 
M 6 HOH 63  663 421 HOH HOH B . 
M 6 HOH 64  664 26  HOH HOH B . 
M 6 HOH 65  665 264 HOH HOH B . 
M 6 HOH 66  666 292 HOH HOH B . 
M 6 HOH 67  667 127 HOH HOH B . 
M 6 HOH 68  668 217 HOH HOH B . 
M 6 HOH 69  669 50  HOH HOH B . 
M 6 HOH 70  670 336 HOH HOH B . 
M 6 HOH 71  671 146 HOH HOH B . 
M 6 HOH 72  672 465 HOH HOH B . 
M 6 HOH 73  673 66  HOH HOH B . 
M 6 HOH 74  674 243 HOH HOH B . 
M 6 HOH 75  675 82  HOH HOH B . 
M 6 HOH 76  676 121 HOH HOH B . 
M 6 HOH 77  677 40  HOH HOH B . 
M 6 HOH 78  678 275 HOH HOH B . 
M 6 HOH 79  679 330 HOH HOH B . 
M 6 HOH 80  680 337 HOH HOH B . 
M 6 HOH 81  681 108 HOH HOH B . 
M 6 HOH 82  682 42  HOH HOH B . 
M 6 HOH 83  683 249 HOH HOH B . 
M 6 HOH 84  684 91  HOH HOH B . 
M 6 HOH 85  685 262 HOH HOH B . 
M 6 HOH 86  686 357 HOH HOH B . 
M 6 HOH 87  687 139 HOH HOH B . 
M 6 HOH 88  688 344 HOH HOH B . 
M 6 HOH 89  689 41  HOH HOH B . 
M 6 HOH 90  690 43  HOH HOH B . 
M 6 HOH 91  691 69  HOH HOH B . 
M 6 HOH 92  692 312 HOH HOH B . 
M 6 HOH 93  693 407 HOH HOH B . 
M 6 HOH 94  694 474 HOH HOH B . 
M 6 HOH 95  695 359 HOH HOH B . 
M 6 HOH 96  696 10  HOH HOH B . 
M 6 HOH 97  697 354 HOH HOH B . 
M 6 HOH 98  698 189 HOH HOH B . 
M 6 HOH 99  699 19  HOH HOH B . 
M 6 HOH 100 700 77  HOH HOH B . 
M 6 HOH 101 701 509 HOH HOH B . 
M 6 HOH 102 702 173 HOH HOH B . 
M 6 HOH 103 703 31  HOH HOH B . 
M 6 HOH 104 704 326 HOH HOH B . 
M 6 HOH 105 705 128 HOH HOH B . 
M 6 HOH 106 706 400 HOH HOH B . 
M 6 HOH 107 707 464 HOH HOH B . 
M 6 HOH 108 708 52  HOH HOH B . 
M 6 HOH 109 709 415 HOH HOH B . 
M 6 HOH 110 710 394 HOH HOH B . 
M 6 HOH 111 711 206 HOH HOH B . 
M 6 HOH 112 712 38  HOH HOH B . 
M 6 HOH 113 713 256 HOH HOH B . 
M 6 HOH 114 714 21  HOH HOH B . 
M 6 HOH 115 715 16  HOH HOH B . 
M 6 HOH 116 716 283 HOH HOH B . 
M 6 HOH 117 717 45  HOH HOH B . 
M 6 HOH 118 718 290 HOH HOH B . 
M 6 HOH 119 719 245 HOH HOH B . 
M 6 HOH 120 720 106 HOH HOH B . 
M 6 HOH 121 721 468 HOH HOH B . 
M 6 HOH 122 722 149 HOH HOH B . 
M 6 HOH 123 723 422 HOH HOH B . 
M 6 HOH 124 724 396 HOH HOH B . 
M 6 HOH 125 725 58  HOH HOH B . 
M 6 HOH 126 726 124 HOH HOH B . 
M 6 HOH 127 727 259 HOH HOH B . 
M 6 HOH 128 728 356 HOH HOH B . 
M 6 HOH 129 729 118 HOH HOH B . 
M 6 HOH 130 730 177 HOH HOH B . 
M 6 HOH 131 731 387 HOH HOH B . 
M 6 HOH 132 732 269 HOH HOH B . 
M 6 HOH 133 733 221 HOH HOH B . 
M 6 HOH 134 734 287 HOH HOH B . 
M 6 HOH 135 735 176 HOH HOH B . 
M 6 HOH 136 736 65  HOH HOH B . 
M 6 HOH 137 737 178 HOH HOH B . 
M 6 HOH 138 738 51  HOH HOH B . 
M 6 HOH 139 739 482 HOH HOH B . 
M 6 HOH 140 740 9   HOH HOH B . 
M 6 HOH 141 741 408 HOH HOH B . 
M 6 HOH 142 742 332 HOH HOH B . 
M 6 HOH 143 743 136 HOH HOH B . 
M 6 HOH 144 744 203 HOH HOH B . 
M 6 HOH 145 745 547 HOH HOH B . 
M 6 HOH 146 746 358 HOH HOH B . 
M 6 HOH 147 747 284 HOH HOH B . 
M 6 HOH 148 748 230 HOH HOH B . 
M 6 HOH 149 749 402 HOH HOH B . 
M 6 HOH 150 750 236 HOH HOH B . 
M 6 HOH 151 751 105 HOH HOH B . 
M 6 HOH 152 752 471 HOH HOH B . 
M 6 HOH 153 753 310 HOH HOH B . 
M 6 HOH 154 754 285 HOH HOH B . 
M 6 HOH 155 755 202 HOH HOH B . 
M 6 HOH 156 756 187 HOH HOH B . 
M 6 HOH 157 757 324 HOH HOH B . 
M 6 HOH 158 758 473 HOH HOH B . 
M 6 HOH 159 759 351 HOH HOH B . 
M 6 HOH 160 760 208 HOH HOH B . 
M 6 HOH 161 761 201 HOH HOH B . 
M 6 HOH 162 762 30  HOH HOH B . 
M 6 HOH 163 763 389 HOH HOH B . 
M 6 HOH 164 764 56  HOH HOH B . 
M 6 HOH 165 765 119 HOH HOH B . 
M 6 HOH 166 766 424 HOH HOH B . 
M 6 HOH 167 767 494 HOH HOH B . 
M 6 HOH 168 768 204 HOH HOH B . 
M 6 HOH 169 769 170 HOH HOH B . 
M 6 HOH 170 770 347 HOH HOH B . 
M 6 HOH 171 771 512 HOH HOH B . 
M 6 HOH 172 772 276 HOH HOH B . 
M 6 HOH 173 773 457 HOH HOH B . 
M 6 HOH 174 774 484 HOH HOH B . 
M 6 HOH 175 775 297 HOH HOH B . 
M 6 HOH 176 776 255 HOH HOH B . 
M 6 HOH 177 777 248 HOH HOH B . 
M 6 HOH 178 778 298 HOH HOH B . 
M 6 HOH 179 779 364 HOH HOH B . 
M 6 HOH 180 780 85  HOH HOH B . 
M 6 HOH 181 781 250 HOH HOH B . 
M 6 HOH 182 782 446 HOH HOH B . 
M 6 HOH 183 783 88  HOH HOH B . 
M 6 HOH 184 784 412 HOH HOH B . 
M 6 HOH 185 785 33  HOH HOH B . 
M 6 HOH 186 786 296 HOH HOH B . 
M 6 HOH 187 787 37  HOH HOH B . 
M 6 HOH 188 788 272 HOH HOH B . 
M 6 HOH 189 789 174 HOH HOH B . 
M 6 HOH 190 790 441 HOH HOH B . 
M 6 HOH 191 791 308 HOH HOH B . 
M 6 HOH 192 792 470 HOH HOH B . 
M 6 HOH 193 793 59  HOH HOH B . 
M 6 HOH 194 794 495 HOH HOH B . 
M 6 HOH 195 795 386 HOH HOH B . 
M 6 HOH 196 796 526 HOH HOH B . 
M 6 HOH 197 797 380 HOH HOH B . 
M 6 HOH 198 798 403 HOH HOH B . 
M 6 HOH 199 799 373 HOH HOH B . 
M 6 HOH 200 800 329 HOH HOH B . 
M 6 HOH 201 801 501 HOH HOH B . 
M 6 HOH 202 802 273 HOH HOH B . 
M 6 HOH 203 803 523 HOH HOH B . 
M 6 HOH 204 804 365 HOH HOH B . 
M 6 HOH 205 805 443 HOH HOH B . 
M 6 HOH 206 806 327 HOH HOH B . 
M 6 HOH 207 807 258 HOH HOH B . 
M 6 HOH 208 808 454 HOH HOH B . 
M 6 HOH 209 809 182 HOH HOH B . 
M 6 HOH 210 810 227 HOH HOH B . 
M 6 HOH 211 811 55  HOH HOH B . 
M 6 HOH 212 812 277 HOH HOH B . 
M 6 HOH 213 813 390 HOH HOH B . 
M 6 HOH 214 814 379 HOH HOH B . 
M 6 HOH 215 815 223 HOH HOH B . 
M 6 HOH 216 816 97  HOH HOH B . 
M 6 HOH 217 817 434 HOH HOH B . 
M 6 HOH 218 818 361 HOH HOH B . 
M 6 HOH 219 819 488 HOH HOH B . 
M 6 HOH 220 820 306 HOH HOH B . 
M 6 HOH 221 821 432 HOH HOH B . 
M 6 HOH 222 822 456 HOH HOH B . 
M 6 HOH 223 823 194 HOH HOH B . 
M 6 HOH 224 824 288 HOH HOH B . 
M 6 HOH 225 825 461 HOH HOH B . 
M 6 HOH 226 826 271 HOH HOH B . 
M 6 HOH 227 827 445 HOH HOH B . 
M 6 HOH 228 828 496 HOH HOH B . 
M 6 HOH 229 829 478 HOH HOH B . 
M 6 HOH 230 830 479 HOH HOH B . 
M 6 HOH 231 831 384 HOH HOH B . 
M 6 HOH 232 832 515 HOH HOH B . 
M 6 HOH 233 833 463 HOH HOH B . 
M 6 HOH 234 834 334 HOH HOH B . 
M 6 HOH 235 835 437 HOH HOH B . 
M 6 HOH 236 836 506 HOH HOH B . 
M 6 HOH 237 837 409 HOH HOH B . 
M 6 HOH 238 838 198 HOH HOH B . 
M 6 HOH 239 839 413 HOH HOH B . 
M 6 HOH 240 840 317 HOH HOH B . 
M 6 HOH 241 841 147 HOH HOH B . 
M 6 HOH 242 842 366 HOH HOH B . 
M 6 HOH 243 843 158 HOH HOH B . 
M 6 HOH 244 844 348 HOH HOH B . 
M 6 HOH 245 845 521 HOH HOH B . 
M 6 HOH 246 846 372 HOH HOH B . 
M 6 HOH 247 847 477 HOH HOH B . 
M 6 HOH 248 848 430 HOH HOH B . 
M 6 HOH 249 849 529 HOH HOH B . 
M 6 HOH 250 850 497 HOH HOH B . 
M 6 HOH 251 851 540 HOH HOH B . 
M 6 HOH 252 852 546 HOH HOH B . 
M 6 HOH 253 853 539 HOH HOH B . 
M 6 HOH 254 854 401 HOH HOH B . 
M 6 HOH 255 855 181 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          ? ? ? ? ? ? ? ? ? ? ? PHASER  ? ? ? .                  4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   95.76 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9II1 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     60.831 
_cell.length_a_esd                 ? 
_cell.length_b                     39.638 
_cell.length_b_esd                 ? 
_cell.length_c                     193.778 
_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                         9II1 
_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                   9II1 
_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             2.03 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          39.42 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.1M Sodium citrate, pH 4.2, 20% PEG 3350' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            338 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER2 S 9M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-06-09 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.9792 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'SSRF BEAMLINE BL02U1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9792 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL02U1 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9II1 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.50 
_reflns.d_resolution_low                               96.40 
_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                                     147906 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           100.0 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.2 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          5.6 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               0.79 
_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                                0.142 
_reflns.pdbx_Rpim_I_all                                0.056 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       922301 
_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                              0.131 
_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                                    1.50 
_reflns_shell.d_res_low                                     1.58 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           124942 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             21482 
_reflns_shell.percent_possible_obs                          99.8 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               5.8 
_reflns_shell.pdbx_chi_squared                              0.61 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     1.2 
_reflns_shell.pdbx_Rrim_I_all                               1.804 
_reflns_shell.pdbx_Rpim_I_all                               0.730 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.450 
_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                                  1.645 
_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                                 9II1 
_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                            1.501 
_refine.ls_d_res_low                             56.158 
_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                     147732 
_refine.ls_number_reflns_R_free                  7221 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.80 
_refine.ls_percent_reflns_R_free                 4.89 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1724 
_refine.ls_R_factor_R_free                       0.2001 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1710 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.36 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.11 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 20.29 
_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                            0.19 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        8086 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         221 
_refine_hist.number_atoms_solvent             549 
_refine_hist.number_atoms_total               8856 
_refine_hist.d_res_high                       1.501 
_refine_hist.d_res_low                        56.158 
# 
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' ? 0.009 ? 8541  ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.081 ? 11571 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 6.246 ? 5083  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.099 ? 1255  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.007 ? 1422  ? 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' 1.5013 1.5184 . . 236 4632 98.00  . . . . 0.3312 . . . . . . . . . . . 0.3456 
'X-RAY DIFFRACTION' 1.5184 1.5362 . . 237 4554 99.00  . . . . 0.3178 . . . . . . . . . . . 0.3155 
'X-RAY DIFFRACTION' 1.5362 1.5550 . . 261 4556 99.00  . . . . 0.3036 . . . . . . . . . . . 0.3231 
'X-RAY DIFFRACTION' 1.5550 1.5746 . . 264 4671 100.00 . . . . 0.2844 . . . . . . . . . . . 0.3188 
'X-RAY DIFFRACTION' 1.5746 1.5954 . . 232 4653 100.00 . . . . 0.2777 . . . . . . . . . . . 0.2848 
'X-RAY DIFFRACTION' 1.5954 1.6172 . . 216 4612 100.00 . . . . 0.2625 . . . . . . . . . . . 0.3135 
'X-RAY DIFFRACTION' 1.6172 1.6403 . . 240 4665 100.00 . . . . 0.2521 . . . . . . . . . . . 0.2901 
'X-RAY DIFFRACTION' 1.6403 1.6648 . . 239 4640 100.00 . . . . 0.2421 . . . . . . . . . . . 0.2785 
'X-RAY DIFFRACTION' 1.6648 1.6908 . . 249 4681 100.00 . . . . 0.2320 . . . . . . . . . . . 0.2556 
'X-RAY DIFFRACTION' 1.6908 1.7186 . . 261 4638 100.00 . . . . 0.2218 . . . . . . . . . . . 0.2551 
'X-RAY DIFFRACTION' 1.7186 1.7482 . . 229 4621 100.00 . . . . 0.2115 . . . . . . . . . . . 0.2555 
'X-RAY DIFFRACTION' 1.7482 1.7800 . . 217 4701 100.00 . . . . 0.2104 . . . . . . . . . . . 0.2335 
'X-RAY DIFFRACTION' 1.7800 1.8142 . . 248 4705 100.00 . . . . 0.2105 . . . . . . . . . . . 0.2662 
'X-RAY DIFFRACTION' 1.8142 1.8513 . . 283 4595 100.00 . . . . 0.1973 . . . . . . . . . . . 0.2402 
'X-RAY DIFFRACTION' 1.8513 1.8915 . . 249 4654 100.00 . . . . 0.1821 . . . . . . . . . . . 0.2388 
'X-RAY DIFFRACTION' 1.8915 1.9355 . . 230 4652 100.00 . . . . 0.1635 . . . . . . . . . . . 0.1958 
'X-RAY DIFFRACTION' 1.9355 1.9839 . . 229 4698 100.00 . . . . 0.1619 . . . . . . . . . . . 0.2078 
'X-RAY DIFFRACTION' 1.9839 2.0376 . . 267 4655 100.00 . . . . 0.1570 . . . . . . . . . . . 0.1932 
'X-RAY DIFFRACTION' 2.0376 2.0975 . . 216 4747 100.00 . . . . 0.1583 . . . . . . . . . . . 0.1974 
'X-RAY DIFFRACTION' 2.0975 2.1652 . . 213 4666 100.00 . . . . 0.1636 . . . . . . . . . . . 0.2042 
'X-RAY DIFFRACTION' 2.1652 2.2426 . . 234 4687 100.00 . . . . 0.1647 . . . . . . . . . . . 0.1835 
'X-RAY DIFFRACTION' 2.2426 2.3324 . . 241 4753 100.00 . . . . 0.1542 . . . . . . . . . . . 0.1912 
'X-RAY DIFFRACTION' 2.3324 2.4386 . . 246 4651 100.00 . . . . 0.1568 . . . . . . . . . . . 0.1985 
'X-RAY DIFFRACTION' 2.4386 2.5671 . . 236 4710 100.00 . . . . 0.1573 . . . . . . . . . . . 0.1811 
'X-RAY DIFFRACTION' 2.5671 2.7280 . . 231 4708 100.00 . . . . 0.1540 . . . . . . . . . . . 0.1782 
'X-RAY DIFFRACTION' 2.7280 2.9386 . . 237 4742 100.00 . . . . 0.1525 . . . . . . . . . . . 0.1929 
'X-RAY DIFFRACTION' 2.9386 3.2343 . . 236 4742 100.00 . . . . 0.1505 . . . . . . . . . . . 0.1746 
'X-RAY DIFFRACTION' 3.2343 3.7022 . . 284 4721 100.00 . . . . 0.1372 . . . . . . . . . . . 0.1474 
'X-RAY DIFFRACTION' 3.7022 4.6640 . . 224 4817 100.00 . . . . 0.1246 . . . . . . . . . . . 0.1509 
'X-RAY DIFFRACTION' 4.6640 56.158 . . 236 4984 100.00 . . . . 0.1599 . . . . . . . . . . . 0.1808 
# 
_struct.entry_id                     9II1 
_struct.title                        'GH57 family Amylopullulanase mutant E256L from Aquifex aeolicus in complex with maltohexaose' 
_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        9II1 
_struct_keywords.text            'Amylopullulanase mutant E256L, Aquifex aeolicus, maltohexaose, HYDROLASE' 
_struct_keywords.pdbx_keywords   HYDROLASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 2 ? 
F N N 4 ? 
G N N 5 ? 
H N N 5 ? 
I N N 5 ? 
J N N 5 ? 
K N N 5 ? 
L N N 6 ? 
M N N 6 ? 
# 
_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 9II1 A 1 ? 477 ? O66934 1 ? 477 ? 1 477 
2 1 9II1 B 1 ? 477 ? O66934 1 ? 477 ? 1 477 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 9II1 LEU A 256 ? UNP O66934 GLU 256 'engineered mutation' 256 1 
2 9II1 LEU B 256 ? UNP O66934 GLU 256 'engineered mutation' 256 2 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,G,H,I,J,L 
2 1 B,E,F,K,M       
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 PRO A 28  ? ASP A 37  ? PRO A 28  ASP A 37  1 ? 10 
HELX_P HELX_P2  AA2 TYR A 39  ? TYR A 44  ? TYR A 39  TYR A 44  1 ? 6  
HELX_P HELX_P3  AA3 LEU A 45  ? ASP A 47  ? LEU A 45  ASP A 47  5 ? 3  
HELX_P HELX_P4  AA4 THR A 57  ? GLN A 69  ? THR A 57  GLN A 69  1 ? 13 
HELX_P HELX_P5  AA5 VAL A 75  ? LYS A 82  ? VAL A 75  LYS A 82  1 ? 8  
HELX_P HELX_P6  AA6 ASP A 83  ? LEU A 87  ? ASP A 83  LEU A 87  5 ? 5  
HELX_P HELX_P7  AA7 GLU A 88  ? TYR A 103 ? GLU A 88  TYR A 103 1 ? 16 
HELX_P HELX_P8  AA8 LYS A 105 ? ARG A 109 ? LYS A 105 ARG A 109 5 ? 5  
HELX_P HELX_P9  AA9 PHE A 110 ? ASN A 118 ? PHE A 110 ASN A 118 1 ? 9  
HELX_P HELX_P10 AB1 ASN A 123 ? TRP A 138 ? ASN A 123 TRP A 138 1 ? 16 
HELX_P HELX_P11 AB2 GLY A 140 ? LEU A 147 ? GLY A 140 LEU A 147 1 ? 8  
HELX_P HELX_P12 AB3 LEU A 147 ? GLY A 154 ? LEU A 147 GLY A 154 1 ? 8  
HELX_P HELX_P13 AB4 THR A 158 ? LYS A 175 ? THR A 158 LYS A 175 1 ? 18 
HELX_P HELX_P14 AB5 LYS A 175 ? GLU A 186 ? LYS A 175 GLU A 186 1 ? 12 
HELX_P HELX_P15 AB6 LEU A 200 ? ASN A 206 ? LEU A 200 ASN A 206 1 ? 7  
HELX_P HELX_P16 AB7 PRO A 207 ? THR A 213 ? PRO A 207 THR A 213 5 ? 7  
HELX_P HELX_P17 AB8 PHE A 226 ? GLY A 246 ? PHE A 226 GLY A 246 1 ? 21 
HELX_P HELX_P18 AB9 PRO A 254 ? SER A 258 ? PRO A 254 SER A 258 5 ? 5  
HELX_P HELX_P19 AC1 SER A 260 ? LYS A 270 ? SER A 260 LYS A 270 1 ? 11 
HELX_P HELX_P20 AC2 GLU A 279 ? VAL A 286 ? GLU A 279 VAL A 286 1 ? 8  
HELX_P HELX_P21 AC3 ASP A 307 ? SER A 317 ? ASP A 307 SER A 317 1 ? 11 
HELX_P HELX_P22 AC4 TYR A 318 ? TRP A 321 ? TYR A 318 TRP A 321 5 ? 4  
HELX_P HELX_P23 AC5 ASN A 322 ? VAL A 341 ? ASN A 322 VAL A 341 1 ? 20 
HELX_P HELX_P24 AC6 CYS A 356 ? ASN A 363 ? CYS A 356 ASN A 363 5 ? 8  
HELX_P HELX_P25 AC7 GLY A 364 ? GLU A 376 ? GLY A 364 GLU A 376 1 ? 13 
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 ? ALA A 444 ? ASP A 439 ALA A 444 1 ? 6  
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  ? PHE B 48  ? TYR B 39  PHE B 48  1 ? 10 
HELX_P HELX_P33 AD6 THR B 57  ? GLN B 69  ? THR B 57  GLN B 69  1 ? 13 
HELX_P HELX_P34 AD7 VAL B 75  ? LYS B 82  ? VAL B 75  LYS B 82  1 ? 8  
HELX_P HELX_P35 AD8 ASP B 83  ? LEU B 87  ? ASP B 83  LEU B 87  5 ? 5  
HELX_P HELX_P36 AD9 GLU B 88  ? TYR B 103 ? GLU B 88  TYR B 103 1 ? 16 
HELX_P HELX_P37 AE1 LYS B 105 ? ARG B 109 ? LYS B 105 ARG B 109 5 ? 5  
HELX_P HELX_P38 AE2 PHE B 110 ? LYS B 119 ? PHE B 110 LYS B 119 1 ? 10 
HELX_P HELX_P39 AE3 ASN B 123 ? TRP B 138 ? ASN B 123 TRP B 138 1 ? 16 
HELX_P HELX_P40 AE4 GLY B 140 ? LEU B 147 ? GLY B 140 LEU B 147 1 ? 8  
HELX_P HELX_P41 AE5 LEU B 147 ? GLY B 154 ? LEU B 147 GLY B 154 1 ? 8  
HELX_P HELX_P42 AE6 THR B 158 ? LYS B 175 ? THR B 158 LYS B 175 1 ? 18 
HELX_P HELX_P43 AE7 LYS B 175 ? GLU B 186 ? LYS B 175 GLU B 186 1 ? 12 
HELX_P HELX_P44 AE8 LEU B 200 ? ASN B 206 ? LEU B 200 ASN B 206 1 ? 7  
HELX_P HELX_P45 AE9 PRO B 207 ? THR B 213 ? PRO B 207 THR B 213 5 ? 7  
HELX_P HELX_P46 AF1 PHE B 226 ? GLY B 246 ? PHE B 226 GLY B 246 1 ? 21 
HELX_P HELX_P47 AF2 PRO B 254 ? SER B 258 ? PRO B 254 SER B 258 5 ? 5  
HELX_P HELX_P48 AF3 SER B 260 ? LYS B 270 ? SER B 260 LYS B 270 1 ? 11 
HELX_P HELX_P49 AF4 GLU B 279 ? VAL B 286 ? GLU B 279 VAL B 286 1 ? 8  
HELX_P HELX_P50 AF5 ASP B 307 ? SER B 317 ? ASP B 307 SER B 317 1 ? 11 
HELX_P HELX_P51 AF6 TYR B 318 ? TRP B 321 ? TYR B 318 TRP B 321 5 ? 4  
HELX_P HELX_P52 AF7 ASN B 322 ? VAL B 341 ? ASN B 322 VAL B 341 1 ? 20 
HELX_P HELX_P53 AF8 CYS B 356 ? ASN B 363 ? CYS B 356 ASN B 363 5 ? 8  
HELX_P HELX_P54 AF9 GLY B 364 ? GLU B 378 ? GLY B 364 GLU B 378 1 ? 15 
HELX_P HELX_P55 AG1 THR B 385 ? LYS B 392 ? THR B 385 LYS B 392 1 ? 8  
HELX_P HELX_P56 AG2 ASN B 419 ? LYS B 435 ? ASN B 419 LYS B 435 1 ? 17 
HELX_P HELX_P57 AG3 ASP B 439 ? GLU B 445 ? ASP B 439 GLU B 445 1 ? 7  
HELX_P HELX_P58 AG4 GLY B 446 ? GLN B 453 ? GLY B 446 GLN B 453 1 ? 8  
HELX_P HELX_P59 AG5 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 ? ? ? ? ? ? ? 1.401 ? ? 
covale2  covale both ? C GLC . O4 ? ? ? 1_555 C GLC . C1 ? ? C GLC 2 C GLC 3 1_555 ? ? ? ? ? ? ? 1.435 ? ? 
covale3  covale both ? C GLC . O4 ? ? ? 1_555 C GLC . C1 ? ? C GLC 3 C GLC 4 1_555 ? ? ? ? ? ? ? 1.440 ? ? 
covale4  covale both ? C GLC . O4 ? ? ? 1_555 C GLC . C1 ? ? C GLC 4 C GLC 5 1_555 ? ? ? ? ? ? ? 1.449 ? ? 
covale5  covale both ? D GLC . O4 ? ? ? 1_555 D GLC . C1 ? ? D GLC 1 D GLC 2 1_555 ? ? ? ? ? ? ? 1.415 ? ? 
covale6  covale both ? D GLC . O4 ? ? ? 1_555 D GLC . C1 ? ? D GLC 2 D GLC 3 1_555 ? ? ? ? ? ? ? 1.399 ? ? 
covale7  covale both ? D GLC . O4 ? ? ? 1_555 D GLC . C1 ? ? D GLC 3 D GLC 4 1_555 ? ? ? ? ? ? ? 1.399 ? ? 
covale8  covale both ? E GLC . O4 ? ? ? 1_555 E GLC . C1 ? ? E GLC 1 E GLC 2 1_555 ? ? ? ? ? ? ? 1.405 ? ? 
covale9  covale both ? E GLC . O4 ? ? ? 1_555 E GLC . C1 ? ? E GLC 2 E GLC 3 1_555 ? ? ? ? ? ? ? 1.445 ? ? 
covale10 covale both ? E GLC . O4 ? ? ? 1_555 E GLC . C1 ? ? E GLC 3 E GLC 4 1_555 ? ? ? ? ? ? ? 1.440 ? ? 
covale11 covale both ? E GLC . O4 ? ? ? 1_555 E GLC . C1 ? ? E GLC 4 E GLC 5 1_555 ? ? ? ? ? ? ? 1.447 ? ? 
covale12 covale both ? F BGC . O4 ? ? ? 1_555 F GLC . C1 ? ? G BGC 1 G GLC 2 1_555 ? ? ? ? ? ? ? 1.452 ? ? 
covale13 covale both ? F GLC . O4 ? ? ? 1_555 F GLC . C1 ? ? G GLC 2 G GLC 3 1_555 ? ? ? ? ? ? ? 1.442 ? ? 
# 
_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 ? ASP A 278 ? MET A 274 ASP A 278 
AA4 3 ILE A 301 ? ARG A 306 ? ILE A 301 ARG A 306 
AA4 4 ARG A 294 ? PHE A 297 ? ARG A 294 PHE A 297 
AA4 5 THR A 397 ? ILE A 400 ? THR A 397 ILE A 400 
AA5 1 VAL B 191 ? SER B 192 ? VAL B 191 SER B 192 
AA5 2 ASN B 53  ? LEU B 56  ? ASN B 53  LEU B 56  
AA5 3 LEU B 4   ? MET B 12  ? LEU B 4   MET B 12  
AA5 4 VAL B 346 ? ASP B 352 ? VAL B 346 ASP B 352 
AA6 1 VAL B 191 ? SER B 192 ? VAL B 191 SER B 192 
AA6 2 ASN B 53  ? LEU B 56  ? ASN B 53  LEU B 56  
AA6 3 LEU B 4   ? MET B 12  ? LEU B 4   MET B 12  
AA6 4 ILE B 381 ? THR B 383 ? ILE B 381 THR B 383 
AA7 1 GLU B 24  ? TYR B 25  ? GLU B 24  TYR B 25  
AA7 2 LYS B 73  ? ASP B 74  ? LYS B 73  ASP B 74  
AA8 1 TYR B 251 ? MET B 252 ? TYR B 251 MET B 252 
AA8 2 MET B 274 ? ASP B 278 ? MET B 274 ASP B 278 
AA8 3 ILE B 301 ? ARG B 306 ? ILE B 301 ARG B 306 
AA8 4 ARG B 294 ? PHE B 297 ? ARG B 294 PHE B 297 
AA8 5 THR B 397 ? ILE B 400 ? THR B 397 ILE B 400 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O SER A 192 ? O SER A 192 N PHE A 54  ? N PHE A 54  
AA1 2 3 O ASN A 53  ? O ASN A 53  N TRP A 10  ? N TRP A 10  
AA1 3 4 N PHE A 5   ? N PHE A 5   O VAL A 347 ? O VAL A 347 
AA2 1 2 O SER A 192 ? O SER A 192 N PHE A 54  ? N PHE A 54  
AA2 2 3 O ASN A 53  ? O ASN A 53  N TRP A 10  ? N TRP A 10  
AA2 3 4 N LEU A 4   ? N LEU A 4   O GLU A 382 ? O GLU A 382 
AA3 1 2 N TYR A 25  ? N TYR A 25  O LYS A 73  ? O LYS A 73  
AA4 1 2 N MET A 252 ? N MET A 252 O MET A 274 ? O MET A 274 
AA4 2 3 N THR A 277 ? N THR A 277 O ARG A 306 ? O ARG A 306 
AA4 3 4 O VAL A 303 ? O VAL A 303 N TYR A 295 ? N TYR A 295 
AA4 4 5 N TYR A 296 ? N TYR A 296 O GLU A 398 ? O GLU A 398 
AA5 1 2 O SER B 192 ? O SER B 192 N PHE B 54  ? N PHE B 54  
AA5 2 3 O ASN B 53  ? O ASN B 53  N TRP B 10  ? N TRP B 10  
AA5 3 4 N VAL B 7   ? N VAL B 7   O VAL B 349 ? O VAL B 349 
AA6 1 2 O SER B 192 ? O SER B 192 N PHE B 54  ? N PHE B 54  
AA6 2 3 O ASN B 53  ? O ASN B 53  N TRP B 10  ? N TRP B 10  
AA6 3 4 N LEU B 4   ? N LEU B 4   O GLU B 382 ? O GLU B 382 
AA7 1 2 N TYR B 25  ? N TYR B 25  O LYS B 73  ? O LYS B 73  
AA8 1 2 N MET B 252 ? N MET B 252 O MET B 274 ? O MET B 274 
AA8 2 3 N THR B 277 ? N THR B 277 O ARG B 306 ? O ARG B 306 
AA8 3 4 O VAL B 303 ? O VAL B 303 N TYR B 295 ? N TYR B 295 
AA8 4 5 N TYR B 296 ? N TYR B 296 O ILE B 400 ? O ILE B 400 
# 
_pdbx_entry_details.entry_id                   9II1 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1  1 O   B HOH 778 ? ? O  B HOH 833 ? ? 2.01 
2  1 OE1 A GLU 287 ? ? O  A HOH 601 ? ? 2.03 
3  1 O   B HOH 804 ? ? O  B HOH 826 ? ? 2.07 
4  1 O   A HOH 646 ? ? O  A HOH 848 ? ? 2.09 
5  1 O   B HOH 613 ? ? O  B HOH 824 ? ? 2.09 
6  1 NZ  A LYS 308 ? ? O2 D GLC 1   ? ? 2.14 
7  1 OE2 A GLU 362 ? ? O  A HOH 602 ? ? 2.16 
8  1 NZ  B LYS 145 ? ? O  B HOH 601 ? ? 2.16 
9  1 NZ  A LYS 377 ? ? O  A HOH 603 ? ? 2.18 
10 1 OE2 B GLU 185 ? ? O  B HOH 602 ? ? 2.18 
11 1 O   B HOH 743 ? ? O  B HOH 816 ? ? 2.19 
12 1 O   A HOH 854 ? ? O  A HOH 878 ? ? 2.19 
# 
loop_
_pdbx_validate_symm_contact.id 
_pdbx_validate_symm_contact.PDB_model_num 
_pdbx_validate_symm_contact.auth_atom_id_1 
_pdbx_validate_symm_contact.auth_asym_id_1 
_pdbx_validate_symm_contact.auth_comp_id_1 
_pdbx_validate_symm_contact.auth_seq_id_1 
_pdbx_validate_symm_contact.PDB_ins_code_1 
_pdbx_validate_symm_contact.label_alt_id_1 
_pdbx_validate_symm_contact.site_symmetry_1 
_pdbx_validate_symm_contact.auth_atom_id_2 
_pdbx_validate_symm_contact.auth_asym_id_2 
_pdbx_validate_symm_contact.auth_comp_id_2 
_pdbx_validate_symm_contact.auth_seq_id_2 
_pdbx_validate_symm_contact.PDB_ins_code_2 
_pdbx_validate_symm_contact.label_alt_id_2 
_pdbx_validate_symm_contact.site_symmetry_2 
_pdbx_validate_symm_contact.dist 
1 1 O   A HOH 793 ? ? 1_555 O  B HOH 771 ? ? 1_655 2.11 
2 1 OE2 A GLU 160 ? ? 1_555 NZ A LYS 434 ? ? 1_455 2.16 
3 1 O   A HOH 847 ? ? 1_555 O  B HOH 824 ? ? 1_565 2.17 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 GLU A 49  ? ? -92.02  59.63 
2 1 ASN A 206 ? ? -161.46 87.91 
3 1 ASP A 394 ? ? -90.56  48.98 
4 1 ASP A 410 ? ? 58.35   17.62 
5 1 PHE A 460 ? ? 68.90   -5.75 
6 1 ASN B 206 ? ? -160.81 91.46 
7 1 ALA B 289 ? ? -99.94  58.18 
8 1 GLU B 299 ? ? 56.31   19.95 
9 1 ASP B 410 ? ? 57.39   16.19 
# 
_pdbx_validate_peptide_omega.id               1 
_pdbx_validate_peptide_omega.PDB_model_num    1 
_pdbx_validate_peptide_omega.auth_comp_id_1   PRO 
_pdbx_validate_peptide_omega.auth_asym_id_1   A 
_pdbx_validate_peptide_omega.auth_seq_id_1    195 
_pdbx_validate_peptide_omega.PDB_ins_code_1   ? 
_pdbx_validate_peptide_omega.label_alt_id_1   ? 
_pdbx_validate_peptide_omega.auth_comp_id_2   TYR 
_pdbx_validate_peptide_omega.auth_asym_id_2   A 
_pdbx_validate_peptide_omega.auth_seq_id_2    196 
_pdbx_validate_peptide_omega.PDB_ins_code_2   ? 
_pdbx_validate_peptide_omega.label_alt_id_2   ? 
_pdbx_validate_peptide_omega.omega            -149.44 
# 
loop_
_pdbx_molecule_features.prd_id 
_pdbx_molecule_features.name 
_pdbx_molecule_features.type 
_pdbx_molecule_features.class 
_pdbx_molecule_features.details 
PRD_900010 alpha-maltotetraose Oligosaccharide 'Substrate analog' oligosaccharide 
PRD_900030 alpha-maltopentaose Oligosaccharide 'Substrate analog' oligosaccharide 
PRD_900065 beta-maltotriose    Oligosaccharide Nutrient           oligosaccharide 
# 
loop_
_pdbx_molecule.instance_id 
_pdbx_molecule.prd_id 
_pdbx_molecule.asym_id 
1 PRD_900030 C 
2 PRD_900010 D 
3 PRD_900030 E 
4 PRD_900065 F 
# 
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 15.7853  12.9211 70.1298 0.0848 ? -0.0005 ? 0.0047  ? 0.0194 ? -0.0048 ? 0.1159 ? 1.0510 ? 
-0.1068 ? 0.1836  ? 0.6588 ? -0.1558 ? 1.9230 ? 0.0605  ? -0.0473 ? -0.0974 ? -0.0519 ? -0.0041 ? 0.0355  ? 0.1198  ? 0.0102  ? 
-0.0500 ? 
2  'X-RAY DIFFRACTION' ? refined 9.6740   18.8584 91.1137 0.1257 ? -0.0005 ? -0.0249 ? 0.2392 ? 0.0098  ? 0.1295 ? 0.8888 ? 
-0.5970 ? -1.0167 ? 1.1033 ? 0.8223  ? 3.2769 ? -0.0035 ? -0.2408 ? -0.0394 ? 0.1278  ? 0.0322  ? 0.0238  ? 0.0390  ? 0.0570  ? 
-0.0393 ? 
3  'X-RAY DIFFRACTION' ? refined 0.0967   26.1926 82.5718 0.1401 ? 0.0362  ? 0.0303  ? 0.1788 ? -0.0164 ? 0.1857 ? 2.1829 ? 
-0.4547 ? -0.8971 ? 1.1465 ? -0.1764 ? 3.3890 ? 0.1097  ? -0.1897 ? 0.2508  ? 0.1118  ? -0.0037 ? 0.1011  ? -0.5035 ? -0.4033 ? 
-0.0455 ? 
4  'X-RAY DIFFRACTION' ? refined 4.3364   8.5734  74.7209 0.1366 ? -0.0300 ? -0.0122 ? 0.0944 ? 0.0257  ? 0.1589 ? 1.9872 ? 
-1.3107 ? -2.0634 ? 2.0814 ? 2.7541  ? 5.1490 ? -0.1176 ? -0.0839 ? -0.3091 ? 0.0665  ? -0.0863 ? 0.1604  ? 0.4318  ? -0.3220 ? 
0.2190  ? 
5  'X-RAY DIFFRACTION' ? refined 34.8586  10.6956 69.5039 0.0984 ? 0.0354  ? 0.0182  ? 0.1240 ? -0.0200 ? 0.1129 ? 2.1205 ? 0.4205 
? 0.9289  ? 1.3201 ? 0.1774  ? 1.6467 ? 0.0548  ? -0.0311 ? -0.0820 ? 0.0121  ? -0.0121 ? -0.1559 ? 0.1135  ? 0.2456  ? -0.0532 ? 
6  'X-RAY DIFFRACTION' ? refined 25.6510  20.3193 56.0575 0.1253 ? -0.0105 ? 0.0255  ? 0.0775 ? -0.0075 ? 0.1289 ? 1.6754 ? 
-0.8176 ? -0.0141 ? 1.1893 ? 0.0802  ? 1.3451 ? 0.1004  ? 0.1735  ? 0.1083  ? -0.1745 ? -0.0724 ? -0.1172 ? -0.0453 ? 0.1738  ? 
-0.0224 ? 
7  'X-RAY DIFFRACTION' ? refined 12.9876  18.0870 51.6893 0.1551 ? 0.0118  ? -0.0310 ? 0.0674 ? -0.0073 ? 0.1163 ? 3.0234 ? 
-0.3971 ? -1.1168 ? 1.6378 ? 0.2383  ? 3.1698 ? 0.1298  ? 0.3606  ? -0.1204 ? -0.3475 ? -0.0871 ? 0.1113  ? -0.0703 ? -0.0390 ? 
-0.0378 ? 
8  'X-RAY DIFFRACTION' ? refined 38.8537  20.3058 72.0710 0.0369 ? -0.0240 ? 0.0236  ? 0.1588 ? -0.0184 ? 0.1831 ? 1.2886 ? 
-0.1247 ? 0.5535  ? 1.6856 ? 0.1693  ? 3.6424 ? -0.0235 ? -0.0618 ? 0.1481  ? 0.0299  ? -0.0209 ? -0.1771 ? -0.2727 ? 0.3303  ? 
0.0242  ? 
9  'X-RAY DIFFRACTION' ? refined 30.5979  15.8678 84.2937 0.0413 ? -0.0159 ? -0.0160 ? 0.1490 ? -0.0143 ? 0.0745 ? 5.0563 ? 
-0.9126 ? 0.1582  ? 3.8967 ? -0.2203 ? 4.8124 ? -0.0224 ? -0.2867 ? 0.0465  ? 0.1625  ? 0.0214  ? -0.0081 ? -0.0806 ? 0.0772  ? 
-0.0198 ? 
10 'X-RAY DIFFRACTION' ? refined 0.1113   -4.9197 27.8908 0.0801 ? 0.0204  ? -0.0137 ? 0.0862 ? -0.0256 ? 0.1128 ? 1.3755 ? 
-0.0146 ? -0.3121 ? 0.6333 ? -0.1724 ? 2.4848 ? -0.0261 ? 0.1868  ? -0.1062 ? 0.0393  ? 0.0001  ? -0.0421 ? 0.0416  ? -0.0043 ? 
0.0167  ? 
11 'X-RAY DIFFRACTION' ? refined 12.5362  0.4576  16.3598 0.1097 ? 0.0137  ? -0.0149 ? 0.2471 ? -0.0010 ? 0.1566 ? 1.7695 ? 0.2703 
? -0.9963 ? 0.7377 ? -0.4529 ? 2.4965 ? 0.0418  ? 0.2295  ? 0.1360  ? -0.0376 ? -0.0363 ? -0.0733 ? -0.1199 ? 0.2983  ? 0.0215  ? 
12 'X-RAY DIFFRACTION' ? refined -14.4143 -2.3139 33.7890 0.1484 ? 0.0552  ? 0.0005  ? 0.1289 ? -0.0128 ? 0.1275 ? 1.4364 ? 0.1650 
? 0.4571  ? 0.4193 ? 0.0016  ? 1.5930 ? 0.0009  ? 0.0130  ? -0.0358 ? 0.1129  ? 0.0533  ? 0.0675  ? -0.0679 ? -0.2391 ? -0.0316 ? 
13 'X-RAY DIFFRACTION' ? refined -11.8102 -1.1605 24.3969 0.0994 ? 0.0277  ? -0.0013 ? 0.1399 ? -0.0224 ? 0.1298 ? 1.6385 ? 0.1072 
? 0.7016  ? 0.5475 ? 0.0132  ? 2.0153 ? -0.0376 ? 0.1959  ? 0.0104  ? 0.0370  ? 0.0343  ? 0.0542  ? -0.1024 ? -0.1504 ? 0.0002  ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1  'X-RAY DIFFRACTION' 1  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 2 through 68 )
;
2  'X-RAY DIFFRACTION' 2  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 69 through 102 )
;
3  'X-RAY DIFFRACTION' 3  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 103 through 158 )
;
4  'X-RAY DIFFRACTION' 4  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 159 through 185 )
;
5  'X-RAY DIFFRACTION' 5  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 186 through 245 )
;
6  'X-RAY DIFFRACTION' 6  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 246 through 360 )
;
7  'X-RAY DIFFRACTION' 7  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 361 through 396 )
;
8  'X-RAY DIFFRACTION' 8  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 397 through 435 )
;
9  'X-RAY DIFFRACTION' 9  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 436 through 477 )
;
10 'X-RAY DIFFRACTION' 10 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 2 through 57 )
;
11 'X-RAY DIFFRACTION' 11 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 58 through 185 )
;
12 'X-RAY DIFFRACTION' 12 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 186 through 360 )
;
13 'X-RAY DIFFRACTION' 13 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 361 through 477 )
;
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A MET 1 ? A MET 1 
2 1 Y 1 B MET 1 ? B MET 1 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
BGC C2   C N R 74  
BGC C3   C N S 75  
BGC C4   C N S 76  
BGC C5   C N R 77  
BGC C6   C N N 78  
BGC C1   C N R 79  
BGC O1   O N N 80  
BGC O2   O N N 81  
BGC O3   O N N 82  
BGC O4   O N N 83  
BGC O5   O N N 84  
BGC O6   O N N 85  
BGC H2   H N N 86  
BGC H3   H N N 87  
BGC H4   H N N 88  
BGC H5   H N N 89  
BGC H61  H N N 90  
BGC H62  H N N 91  
BGC H1   H N N 92  
BGC HO1  H N N 93  
BGC HO2  H N N 94  
BGC HO3  H N N 95  
BGC HO4  H N N 96  
BGC HO6  H N N 97  
CYS N    N N N 98  
CYS CA   C N R 99  
CYS C    C N N 100 
CYS O    O N N 101 
CYS CB   C N N 102 
CYS SG   S N N 103 
CYS OXT  O N N 104 
CYS H    H N N 105 
CYS H2   H N N 106 
CYS HA   H N N 107 
CYS HB2  H N N 108 
CYS HB3  H N N 109 
CYS HG   H N N 110 
CYS HXT  H N N 111 
GLC C1   C N S 112 
GLC C2   C N R 113 
GLC C3   C N S 114 
GLC C4   C N S 115 
GLC C5   C N R 116 
GLC C6   C N N 117 
GLC O1   O N N 118 
GLC O2   O N N 119 
GLC O3   O N N 120 
GLC O4   O N N 121 
GLC O5   O N N 122 
GLC O6   O N N 123 
GLC H1   H N N 124 
GLC H2   H N N 125 
GLC H3   H N N 126 
GLC H4   H N N 127 
GLC H5   H N N 128 
GLC H61  H N N 129 
GLC H62  H N N 130 
GLC HO1  H N N 131 
GLC HO2  H N N 132 
GLC HO3  H N N 133 
GLC HO4  H N N 134 
GLC HO6  H N N 135 
GLN N    N N N 136 
GLN CA   C N S 137 
GLN C    C N N 138 
GLN O    O N N 139 
GLN CB   C N N 140 
GLN CG   C N N 141 
GLN CD   C N N 142 
GLN OE1  O N N 143 
GLN NE2  N N N 144 
GLN OXT  O N N 145 
GLN H    H N N 146 
GLN H2   H N N 147 
GLN HA   H N N 148 
GLN HB2  H N N 149 
GLN HB3  H N N 150 
GLN HG2  H N N 151 
GLN HG3  H N N 152 
GLN HE21 H N N 153 
GLN HE22 H N N 154 
GLN HXT  H N N 155 
GLU N    N N N 156 
GLU CA   C N S 157 
GLU C    C N N 158 
GLU O    O N N 159 
GLU CB   C N N 160 
GLU CG   C N N 161 
GLU CD   C N N 162 
GLU OE1  O N N 163 
GLU OE2  O N N 164 
GLU OXT  O N N 165 
GLU H    H N N 166 
GLU H2   H N N 167 
GLU HA   H N N 168 
GLU HB2  H N N 169 
GLU HB3  H N N 170 
GLU HG2  H N N 171 
GLU HG3  H N N 172 
GLU HE2  H N N 173 
GLU HXT  H N N 174 
GLY N    N N N 175 
GLY CA   C N N 176 
GLY C    C N N 177 
GLY O    O N N 178 
GLY OXT  O N N 179 
GLY H    H N N 180 
GLY H2   H N N 181 
GLY HA2  H N N 182 
GLY HA3  H N N 183 
GLY HXT  H N N 184 
GOL C1   C N N 185 
GOL O1   O N N 186 
GOL C2   C N N 187 
GOL O2   O N N 188 
GOL C3   C N N 189 
GOL O3   O N N 190 
GOL H11  H N N 191 
GOL H12  H N N 192 
GOL HO1  H N N 193 
GOL H2   H N N 194 
GOL HO2  H N N 195 
GOL H31  H N N 196 
GOL H32  H N N 197 
GOL HO3  H N N 198 
HIS N    N N N 199 
HIS CA   C N S 200 
HIS C    C N N 201 
HIS O    O N N 202 
HIS CB   C N N 203 
HIS CG   C Y N 204 
HIS ND1  N Y N 205 
HIS CD2  C Y N 206 
HIS CE1  C Y N 207 
HIS NE2  N Y N 208 
HIS OXT  O N N 209 
HIS H    H N N 210 
HIS H2   H N N 211 
HIS HA   H N N 212 
HIS HB2  H N N 213 
HIS HB3  H N N 214 
HIS HD1  H N N 215 
HIS HD2  H N N 216 
HIS HE1  H N N 217 
HIS HE2  H N N 218 
HIS HXT  H N N 219 
HOH O    O N N 220 
HOH H1   H N N 221 
HOH H2   H N N 222 
ILE N    N N N 223 
ILE CA   C N S 224 
ILE C    C N N 225 
ILE O    O N N 226 
ILE CB   C N S 227 
ILE CG1  C N N 228 
ILE CG2  C N N 229 
ILE CD1  C N N 230 
ILE OXT  O N N 231 
ILE H    H N N 232 
ILE H2   H N N 233 
ILE HA   H N N 234 
ILE HB   H N N 235 
ILE HG12 H N N 236 
ILE HG13 H N N 237 
ILE HG21 H N N 238 
ILE HG22 H N N 239 
ILE HG23 H N N 240 
ILE HD11 H N N 241 
ILE HD12 H N N 242 
ILE HD13 H N N 243 
ILE HXT  H N N 244 
LEU N    N N N 245 
LEU CA   C N S 246 
LEU C    C N N 247 
LEU O    O N N 248 
LEU CB   C N N 249 
LEU CG   C N N 250 
LEU CD1  C N N 251 
LEU CD2  C N N 252 
LEU OXT  O N N 253 
LEU H    H N N 254 
LEU H2   H N N 255 
LEU HA   H N N 256 
LEU HB2  H N N 257 
LEU HB3  H N N 258 
LEU HG   H N N 259 
LEU HD11 H N N 260 
LEU HD12 H N N 261 
LEU HD13 H N N 262 
LEU HD21 H N N 263 
LEU HD22 H N N 264 
LEU HD23 H N N 265 
LEU HXT  H N N 266 
LYS N    N N N 267 
LYS CA   C N S 268 
LYS C    C N N 269 
LYS O    O N N 270 
LYS CB   C N N 271 
LYS CG   C N N 272 
LYS CD   C N N 273 
LYS CE   C N N 274 
LYS NZ   N N N 275 
LYS OXT  O N N 276 
LYS H    H N N 277 
LYS H2   H N N 278 
LYS HA   H N N 279 
LYS HB2  H N N 280 
LYS HB3  H N N 281 
LYS HG2  H N N 282 
LYS HG3  H N N 283 
LYS HD2  H N N 284 
LYS HD3  H N N 285 
LYS HE2  H N N 286 
LYS HE3  H N N 287 
LYS HZ1  H N N 288 
LYS HZ2  H N N 289 
LYS HZ3  H N N 290 
LYS HXT  H N N 291 
MET N    N N N 292 
MET CA   C N S 293 
MET C    C N N 294 
MET O    O N N 295 
MET CB   C N N 296 
MET CG   C N N 297 
MET SD   S N N 298 
MET CE   C N N 299 
MET OXT  O N N 300 
MET H    H N N 301 
MET H2   H N N 302 
MET HA   H N N 303 
MET HB2  H N N 304 
MET HB3  H N N 305 
MET HG2  H N N 306 
MET HG3  H N N 307 
MET HE1  H N N 308 
MET HE2  H N N 309 
MET HE3  H N N 310 
MET HXT  H N N 311 
PHE N    N N N 312 
PHE CA   C N S 313 
PHE C    C N N 314 
PHE O    O N N 315 
PHE CB   C N N 316 
PHE CG   C Y N 317 
PHE CD1  C Y N 318 
PHE CD2  C Y N 319 
PHE CE1  C Y N 320 
PHE CE2  C Y N 321 
PHE CZ   C Y N 322 
PHE OXT  O N N 323 
PHE H    H N N 324 
PHE H2   H N N 325 
PHE HA   H N N 326 
PHE HB2  H N N 327 
PHE HB3  H N N 328 
PHE HD1  H N N 329 
PHE HD2  H N N 330 
PHE HE1  H N N 331 
PHE HE2  H N N 332 
PHE HZ   H N N 333 
PHE HXT  H N N 334 
PRO N    N N N 335 
PRO CA   C N S 336 
PRO C    C N N 337 
PRO O    O N N 338 
PRO CB   C N N 339 
PRO CG   C N N 340 
PRO CD   C N N 341 
PRO OXT  O N N 342 
PRO H    H N N 343 
PRO HA   H N N 344 
PRO HB2  H N N 345 
PRO HB3  H N N 346 
PRO HG2  H N N 347 
PRO HG3  H N N 348 
PRO HD2  H N N 349 
PRO HD3  H N N 350 
PRO HXT  H N N 351 
SER N    N N N 352 
SER CA   C N S 353 
SER C    C N N 354 
SER O    O N N 355 
SER CB   C N N 356 
SER OG   O N N 357 
SER OXT  O N N 358 
SER H    H N N 359 
SER H2   H N N 360 
SER HA   H N N 361 
SER HB2  H N N 362 
SER HB3  H N N 363 
SER HG   H N N 364 
SER HXT  H N N 365 
THR N    N N N 366 
THR CA   C N S 367 
THR C    C N N 368 
THR O    O N N 369 
THR CB   C N R 370 
THR OG1  O N N 371 
THR CG2  C N N 372 
THR OXT  O N N 373 
THR H    H N N 374 
THR H2   H N N 375 
THR HA   H N N 376 
THR HB   H N N 377 
THR HG1  H N N 378 
THR HG21 H N N 379 
THR HG22 H N N 380 
THR HG23 H N N 381 
THR HXT  H N N 382 
TRP N    N N N 383 
TRP CA   C N S 384 
TRP C    C N N 385 
TRP O    O N N 386 
TRP CB   C N N 387 
TRP CG   C Y N 388 
TRP CD1  C Y N 389 
TRP CD2  C Y N 390 
TRP NE1  N Y N 391 
TRP CE2  C Y N 392 
TRP CE3  C Y N 393 
TRP CZ2  C Y N 394 
TRP CZ3  C Y N 395 
TRP CH2  C Y N 396 
TRP OXT  O N N 397 
TRP H    H N N 398 
TRP H2   H N N 399 
TRP HA   H N N 400 
TRP HB2  H N N 401 
TRP HB3  H N N 402 
TRP HD1  H N N 403 
TRP HE1  H N N 404 
TRP HE3  H N N 405 
TRP HZ2  H N N 406 
TRP HZ3  H N N 407 
TRP HH2  H N N 408 
TRP HXT  H N N 409 
TYR N    N N N 410 
TYR CA   C N S 411 
TYR C    C N N 412 
TYR O    O N N 413 
TYR CB   C N N 414 
TYR CG   C Y N 415 
TYR CD1  C Y N 416 
TYR CD2  C Y N 417 
TYR CE1  C Y N 418 
TYR CE2  C Y N 419 
TYR CZ   C Y N 420 
TYR OH   O N N 421 
TYR OXT  O N N 422 
TYR H    H N N 423 
TYR H2   H N N 424 
TYR HA   H N N 425 
TYR HB2  H N N 426 
TYR HB3  H N N 427 
TYR HD1  H N N 428 
TYR HD2  H N N 429 
TYR HE1  H N N 430 
TYR HE2  H N N 431 
TYR HH   H N N 432 
TYR HXT  H N N 433 
VAL N    N N N 434 
VAL CA   C N S 435 
VAL C    C N N 436 
VAL O    O N N 437 
VAL CB   C N N 438 
VAL CG1  C N N 439 
VAL CG2  C N N 440 
VAL OXT  O N N 441 
VAL H    H N N 442 
VAL H2   H N N 443 
VAL HA   H N N 444 
VAL HB   H N N 445 
VAL HG11 H N N 446 
VAL HG12 H N N 447 
VAL HG13 H N N 448 
VAL HG21 H N N 449 
VAL HG22 H N N 450 
VAL HG23 H N N 451 
VAL HXT  H N N 452 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
BGC C2  C3   sing N N 70  
BGC C2  C1   sing N N 71  
BGC C2  O2   sing N N 72  
BGC C2  H2   sing N N 73  
BGC C3  C4   sing N N 74  
BGC C3  O3   sing N N 75  
BGC C3  H3   sing N N 76  
BGC C4  C5   sing N N 77  
BGC C4  O4   sing N N 78  
BGC C4  H4   sing N N 79  
BGC C5  C6   sing N N 80  
BGC C5  O5   sing N N 81  
BGC C5  H5   sing N N 82  
BGC C6  O6   sing N N 83  
BGC C6  H61  sing N N 84  
BGC C6  H62  sing N N 85  
BGC C1  O1   sing N N 86  
BGC C1  O5   sing N N 87  
BGC C1  H1   sing N N 88  
BGC O1  HO1  sing N N 89  
BGC O2  HO2  sing N N 90  
BGC O3  HO3  sing N N 91  
BGC O4  HO4  sing N N 92  
BGC O6  HO6  sing N N 93  
CYS N   CA   sing N N 94  
CYS N   H    sing N N 95  
CYS N   H2   sing N N 96  
CYS CA  C    sing N N 97  
CYS CA  CB   sing N N 98  
CYS CA  HA   sing N N 99  
CYS C   O    doub N N 100 
CYS C   OXT  sing N N 101 
CYS CB  SG   sing N N 102 
CYS CB  HB2  sing N N 103 
CYS CB  HB3  sing N N 104 
CYS SG  HG   sing N N 105 
CYS OXT HXT  sing N N 106 
GLC C1  C2   sing N N 107 
GLC C1  O1   sing N N 108 
GLC C1  O5   sing N N 109 
GLC C1  H1   sing N N 110 
GLC C2  C3   sing N N 111 
GLC C2  O2   sing N N 112 
GLC C2  H2   sing N N 113 
GLC C3  C4   sing N N 114 
GLC C3  O3   sing N N 115 
GLC C3  H3   sing N N 116 
GLC C4  C5   sing N N 117 
GLC C4  O4   sing N N 118 
GLC C4  H4   sing N N 119 
GLC C5  C6   sing N N 120 
GLC C5  O5   sing N N 121 
GLC C5  H5   sing N N 122 
GLC C6  O6   sing N N 123 
GLC C6  H61  sing N N 124 
GLC C6  H62  sing N N 125 
GLC O1  HO1  sing N N 126 
GLC O2  HO2  sing N N 127 
GLC O3  HO3  sing N N 128 
GLC O4  HO4  sing N N 129 
GLC O6  HO6  sing N N 130 
GLN N   CA   sing N N 131 
GLN N   H    sing N N 132 
GLN N   H2   sing N N 133 
GLN CA  C    sing N N 134 
GLN CA  CB   sing N N 135 
GLN CA  HA   sing N N 136 
GLN C   O    doub N N 137 
GLN C   OXT  sing N N 138 
GLN CB  CG   sing N N 139 
GLN CB  HB2  sing N N 140 
GLN CB  HB3  sing N N 141 
GLN CG  CD   sing N N 142 
GLN CG  HG2  sing N N 143 
GLN CG  HG3  sing N N 144 
GLN CD  OE1  doub N N 145 
GLN CD  NE2  sing N N 146 
GLN NE2 HE21 sing N N 147 
GLN NE2 HE22 sing N N 148 
GLN OXT HXT  sing N N 149 
GLU N   CA   sing N N 150 
GLU N   H    sing N N 151 
GLU N   H2   sing N N 152 
GLU CA  C    sing N N 153 
GLU CA  CB   sing N N 154 
GLU CA  HA   sing N N 155 
GLU C   O    doub N N 156 
GLU C   OXT  sing N N 157 
GLU CB  CG   sing N N 158 
GLU CB  HB2  sing N N 159 
GLU CB  HB3  sing N N 160 
GLU CG  CD   sing N N 161 
GLU CG  HG2  sing N N 162 
GLU CG  HG3  sing N N 163 
GLU CD  OE1  doub N N 164 
GLU CD  OE2  sing N N 165 
GLU OE2 HE2  sing N N 166 
GLU OXT HXT  sing N N 167 
GLY N   CA   sing N N 168 
GLY N   H    sing N N 169 
GLY N   H2   sing N N 170 
GLY CA  C    sing N N 171 
GLY CA  HA2  sing N N 172 
GLY CA  HA3  sing N N 173 
GLY C   O    doub N N 174 
GLY C   OXT  sing N N 175 
GLY OXT HXT  sing N N 176 
GOL C1  O1   sing N N 177 
GOL C1  C2   sing N N 178 
GOL C1  H11  sing N N 179 
GOL C1  H12  sing N N 180 
GOL O1  HO1  sing N N 181 
GOL C2  O2   sing N N 182 
GOL C2  C3   sing N N 183 
GOL C2  H2   sing N N 184 
GOL O2  HO2  sing N N 185 
GOL C3  O3   sing N N 186 
GOL C3  H31  sing N N 187 
GOL C3  H32  sing N N 188 
GOL O3  HO3  sing N N 189 
HIS N   CA   sing N N 190 
HIS N   H    sing N N 191 
HIS N   H2   sing N N 192 
HIS CA  C    sing N N 193 
HIS CA  CB   sing N N 194 
HIS CA  HA   sing N N 195 
HIS C   O    doub N N 196 
HIS C   OXT  sing N N 197 
HIS CB  CG   sing N N 198 
HIS CB  HB2  sing N N 199 
HIS CB  HB3  sing N N 200 
HIS CG  ND1  sing Y N 201 
HIS CG  CD2  doub Y N 202 
HIS ND1 CE1  doub Y N 203 
HIS ND1 HD1  sing N N 204 
HIS CD2 NE2  sing Y N 205 
HIS CD2 HD2  sing N N 206 
HIS CE1 NE2  sing Y N 207 
HIS CE1 HE1  sing N N 208 
HIS NE2 HE2  sing N N 209 
HIS OXT HXT  sing N N 210 
HOH O   H1   sing N N 211 
HOH O   H2   sing N N 212 
ILE N   CA   sing N N 213 
ILE N   H    sing N N 214 
ILE N   H2   sing N N 215 
ILE CA  C    sing N N 216 
ILE CA  CB   sing N N 217 
ILE CA  HA   sing N N 218 
ILE C   O    doub N N 219 
ILE C   OXT  sing N N 220 
ILE CB  CG1  sing N N 221 
ILE CB  CG2  sing N N 222 
ILE CB  HB   sing N N 223 
ILE CG1 CD1  sing N N 224 
ILE CG1 HG12 sing N N 225 
ILE CG1 HG13 sing N N 226 
ILE CG2 HG21 sing N N 227 
ILE CG2 HG22 sing N N 228 
ILE CG2 HG23 sing N N 229 
ILE CD1 HD11 sing N N 230 
ILE CD1 HD12 sing N N 231 
ILE CD1 HD13 sing N N 232 
ILE OXT HXT  sing N N 233 
LEU N   CA   sing N N 234 
LEU N   H    sing N N 235 
LEU N   H2   sing N N 236 
LEU CA  C    sing N N 237 
LEU CA  CB   sing N N 238 
LEU CA  HA   sing N N 239 
LEU C   O    doub N N 240 
LEU C   OXT  sing N N 241 
LEU CB  CG   sing N N 242 
LEU CB  HB2  sing N N 243 
LEU CB  HB3  sing N N 244 
LEU CG  CD1  sing N N 245 
LEU CG  CD2  sing N N 246 
LEU CG  HG   sing N N 247 
LEU CD1 HD11 sing N N 248 
LEU CD1 HD12 sing N N 249 
LEU CD1 HD13 sing N N 250 
LEU CD2 HD21 sing N N 251 
LEU CD2 HD22 sing N N 252 
LEU CD2 HD23 sing N N 253 
LEU OXT HXT  sing N N 254 
LYS N   CA   sing N N 255 
LYS N   H    sing N N 256 
LYS N   H2   sing N N 257 
LYS CA  C    sing N N 258 
LYS CA  CB   sing N N 259 
LYS CA  HA   sing N N 260 
LYS C   O    doub N N 261 
LYS C   OXT  sing N N 262 
LYS CB  CG   sing N N 263 
LYS CB  HB2  sing N N 264 
LYS CB  HB3  sing N N 265 
LYS CG  CD   sing N N 266 
LYS CG  HG2  sing N N 267 
LYS CG  HG3  sing N N 268 
LYS CD  CE   sing N N 269 
LYS CD  HD2  sing N N 270 
LYS CD  HD3  sing N N 271 
LYS CE  NZ   sing N N 272 
LYS CE  HE2  sing N N 273 
LYS CE  HE3  sing N N 274 
LYS NZ  HZ1  sing N N 275 
LYS NZ  HZ2  sing N N 276 
LYS NZ  HZ3  sing N N 277 
LYS OXT HXT  sing N N 278 
MET N   CA   sing N N 279 
MET N   H    sing N N 280 
MET N   H2   sing N N 281 
MET CA  C    sing N N 282 
MET CA  CB   sing N N 283 
MET CA  HA   sing N N 284 
MET C   O    doub N N 285 
MET C   OXT  sing N N 286 
MET CB  CG   sing N N 287 
MET CB  HB2  sing N N 288 
MET CB  HB3  sing N N 289 
MET CG  SD   sing N N 290 
MET CG  HG2  sing N N 291 
MET CG  HG3  sing N N 292 
MET SD  CE   sing N N 293 
MET CE  HE1  sing N N 294 
MET CE  HE2  sing N N 295 
MET CE  HE3  sing N N 296 
MET OXT HXT  sing N N 297 
PHE N   CA   sing N N 298 
PHE N   H    sing N N 299 
PHE N   H2   sing N N 300 
PHE CA  C    sing N N 301 
PHE CA  CB   sing N N 302 
PHE CA  HA   sing N N 303 
PHE C   O    doub N N 304 
PHE C   OXT  sing N N 305 
PHE CB  CG   sing N N 306 
PHE CB  HB2  sing N N 307 
PHE CB  HB3  sing N N 308 
PHE CG  CD1  doub Y N 309 
PHE CG  CD2  sing Y N 310 
PHE CD1 CE1  sing Y N 311 
PHE CD1 HD1  sing N N 312 
PHE CD2 CE2  doub Y N 313 
PHE CD2 HD2  sing N N 314 
PHE CE1 CZ   doub Y N 315 
PHE CE1 HE1  sing N N 316 
PHE CE2 CZ   sing Y N 317 
PHE CE2 HE2  sing N N 318 
PHE CZ  HZ   sing N N 319 
PHE OXT HXT  sing N N 320 
PRO N   CA   sing N N 321 
PRO N   CD   sing N N 322 
PRO N   H    sing N N 323 
PRO CA  C    sing N N 324 
PRO CA  CB   sing N N 325 
PRO CA  HA   sing N N 326 
PRO C   O    doub N N 327 
PRO C   OXT  sing N N 328 
PRO CB  CG   sing N N 329 
PRO CB  HB2  sing N N 330 
PRO CB  HB3  sing N N 331 
PRO CG  CD   sing N N 332 
PRO CG  HG2  sing N N 333 
PRO CG  HG3  sing N N 334 
PRO CD  HD2  sing N N 335 
PRO CD  HD3  sing N N 336 
PRO OXT HXT  sing N N 337 
SER N   CA   sing N N 338 
SER N   H    sing N N 339 
SER N   H2   sing N N 340 
SER CA  C    sing N N 341 
SER CA  CB   sing N N 342 
SER CA  HA   sing N N 343 
SER C   O    doub N N 344 
SER C   OXT  sing N N 345 
SER CB  OG   sing N N 346 
SER CB  HB2  sing N N 347 
SER CB  HB3  sing N N 348 
SER OG  HG   sing N N 349 
SER OXT HXT  sing N N 350 
THR N   CA   sing N N 351 
THR N   H    sing N N 352 
THR N   H2   sing N N 353 
THR CA  C    sing N N 354 
THR CA  CB   sing N N 355 
THR CA  HA   sing N N 356 
THR C   O    doub N N 357 
THR C   OXT  sing N N 358 
THR CB  OG1  sing N N 359 
THR CB  CG2  sing N N 360 
THR CB  HB   sing N N 361 
THR OG1 HG1  sing N N 362 
THR CG2 HG21 sing N N 363 
THR CG2 HG22 sing N N 364 
THR CG2 HG23 sing N N 365 
THR OXT HXT  sing N N 366 
TRP N   CA   sing N N 367 
TRP N   H    sing N N 368 
TRP N   H2   sing N N 369 
TRP CA  C    sing N N 370 
TRP CA  CB   sing N N 371 
TRP CA  HA   sing N N 372 
TRP C   O    doub N N 373 
TRP C   OXT  sing N N 374 
TRP CB  CG   sing N N 375 
TRP CB  HB2  sing N N 376 
TRP CB  HB3  sing N N 377 
TRP CG  CD1  doub Y N 378 
TRP CG  CD2  sing Y N 379 
TRP CD1 NE1  sing Y N 380 
TRP CD1 HD1  sing N N 381 
TRP CD2 CE2  doub Y N 382 
TRP CD2 CE3  sing Y N 383 
TRP NE1 CE2  sing Y N 384 
TRP NE1 HE1  sing N N 385 
TRP CE2 CZ2  sing Y N 386 
TRP CE3 CZ3  doub Y N 387 
TRP CE3 HE3  sing N N 388 
TRP CZ2 CH2  doub Y N 389 
TRP CZ2 HZ2  sing N N 390 
TRP CZ3 CH2  sing Y N 391 
TRP CZ3 HZ3  sing N N 392 
TRP CH2 HH2  sing N N 393 
TRP OXT HXT  sing N N 394 
TYR N   CA   sing N N 395 
TYR N   H    sing N N 396 
TYR N   H2   sing N N 397 
TYR CA  C    sing N N 398 
TYR CA  CB   sing N N 399 
TYR CA  HA   sing N N 400 
TYR C   O    doub N N 401 
TYR C   OXT  sing N N 402 
TYR CB  CG   sing N N 403 
TYR CB  HB2  sing N N 404 
TYR CB  HB3  sing N N 405 
TYR CG  CD1  doub Y N 406 
TYR CG  CD2  sing Y N 407 
TYR CD1 CE1  sing Y N 408 
TYR CD1 HD1  sing N N 409 
TYR CD2 CE2  doub Y N 410 
TYR CD2 HD2  sing N N 411 
TYR CE1 CZ   doub Y N 412 
TYR CE1 HE1  sing N N 413 
TYR CE2 CZ   sing Y N 414 
TYR CE2 HE2  sing N N 415 
TYR CZ  OH   sing N N 416 
TYR OH  HH   sing N N 417 
TYR OXT HXT  sing N N 418 
VAL N   CA   sing N N 419 
VAL N   H    sing N N 420 
VAL N   H2   sing N N 421 
VAL CA  C    sing N N 422 
VAL CA  CB   sing N N 423 
VAL CA  HA   sing N N 424 
VAL C   O    doub N N 425 
VAL C   OXT  sing N N 426 
VAL CB  CG1  sing N N 427 
VAL CB  CG2  sing N N 428 
VAL CB  HB   sing N N 429 
VAL CG1 HG11 sing N N 430 
VAL CG1 HG12 sing N N 431 
VAL CG1 HG13 sing N N 432 
VAL CG2 HG21 sing N N 433 
VAL CG2 HG22 sing N N 434 
VAL CG2 HG23 sing N N 435 
VAL OXT HXT  sing N N 436 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'National Basic Research Program of China (973 Program)' China 2021YFC2301405 1 
'National Science Foundation (NSF, China)'               China 21ZR1471800    2 
# 
loop_
_pdbx_entity_branch_list.entity_id 
_pdbx_entity_branch_list.comp_id 
_pdbx_entity_branch_list.num 
_pdbx_entity_branch_list.hetero 
2 GLC 1 n 
2 GLC 2 n 
2 GLC 3 n 
2 GLC 4 n 
2 GLC 5 n 
3 GLC 1 n 
3 GLC 2 n 
3 GLC 3 n 
3 GLC 4 n 
4 BGC 1 n 
4 GLC 2 n 
4 GLC 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                    9II1 
_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]   0.016439 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.001658 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.025228 
_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]   0.005187 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . LYS A 1 2   ? 17.068  19.891  35.808  1.00 30.75 ? 2   LYS A N   1 
ATOM   2    C CA  . LYS A 1 2   ? 18.069  20.144  36.842  1.00 27.81 ? 2   LYS A CA  1 
ATOM   3    C C   . LYS A 1 2   ? 17.405  20.270  38.196  1.00 25.49 ? 2   LYS A C   1 
ATOM   4    O O   . LYS A 1 2   ? 16.548  21.135  38.398  1.00 26.10 ? 2   LYS A O   1 
ATOM   5    C CB  . LYS A 1 2   ? 18.860  21.416  36.548  1.00 34.71 ? 2   LYS A CB  1 
ATOM   6    C CG  . LYS A 1 2   ? 20.118  21.559  37.395  1.00 39.67 ? 2   LYS A CG  1 
ATOM   7    C CD  . LYS A 1 2   ? 20.373  22.994  37.833  1.00 44.94 ? 2   LYS A CD  1 
ATOM   8    C CE  . LYS A 1 2   ? 20.428  23.956  36.665  1.00 52.25 ? 2   LYS A CE  1 
ATOM   9    N NZ  . LYS A 1 2   ? 20.522  25.371  37.136  1.00 53.29 ? 2   LYS A NZ  1 
ATOM   10   N N   . LYS A 1 3   ? 17.798  19.423  39.138  1.00 21.49 ? 3   LYS A N   1 
ATOM   11   C CA  . LYS A 1 3   ? 17.197  19.445  40.461  1.00 19.81 ? 3   LYS A CA  1 
ATOM   12   C C   . LYS A 1 3   ? 18.164  20.040  41.480  1.00 19.54 ? 3   LYS A C   1 
ATOM   13   O O   . LYS A 1 3   ? 19.377  20.089  41.269  1.00 22.05 ? 3   LYS A O   1 
ATOM   14   C CB  . LYS A 1 3   ? 16.800  18.031  40.912  1.00 24.60 ? 3   LYS A CB  1 
ATOM   15   C CG  . LYS A 1 3   ? 15.870  17.297  39.964  1.00 33.53 ? 3   LYS A CG  1 
ATOM   16   C CD  . LYS A 1 3   ? 14.416  17.628  40.259  1.00 40.49 ? 3   LYS A CD  1 
ATOM   17   C CE  . LYS A 1 3   ? 13.482  17.009  39.219  1.00 44.77 ? 3   LYS A CE  1 
ATOM   18   N NZ  . LYS A 1 3   ? 12.827  18.030  38.333  1.00 47.98 ? 3   LYS A NZ  1 
ATOM   19   N N   . LEU A 1 4   ? 17.609  20.479  42.599  1.00 15.83 ? 4   LEU A N   1 
ATOM   20   C CA  . LEU A 1 4   ? 18.382  20.760  43.800  1.00 15.11 ? 4   LEU A CA  1 
ATOM   21   C C   . LEU A 1 4   ? 18.084  19.641  44.785  1.00 17.82 ? 4   LEU A C   1 
ATOM   22   O O   . LEU A 1 4   ? 16.912  19.311  45.017  1.00 16.96 ? 4   LEU A O   1 
ATOM   23   C CB  . LEU A 1 4   ? 18.026  22.132  44.397  1.00 14.83 ? 4   LEU A CB  1 
ATOM   24   C CG  . LEU A 1 4   ? 18.666  22.429  45.775  1.00 16.49 ? 4   LEU A CG  1 
ATOM   25   C CD1 . LEU A 1 4   ? 18.981  23.952  45.855  1.00 17.69 ? 4   LEU A CD1 1 
ATOM   26   C CD2 . LEU A 1 4   ? 17.824  21.985  46.991  1.00 13.39 ? 4   LEU A CD2 1 
ATOM   27   N N   . PHE A 1 5   ? 19.126  19.055  45.361  1.00 14.05 ? 5   PHE A N   1 
ATOM   28   C CA  . PHE A 1 5   ? 18.949  17.972  46.318  1.00 14.91 ? 5   PHE A CA  1 
ATOM   29   C C   . PHE A 1 5   ? 19.057  18.550  47.714  1.00 13.39 ? 5   PHE A C   1 
ATOM   30   O O   . PHE A 1 5   ? 20.024  19.257  48.026  1.00 17.99 ? 5   PHE A O   1 
ATOM   31   C CB  . PHE A 1 5   ? 19.979  16.871  46.092  1.00 15.79 ? 5   PHE A CB  1 
ATOM   32   C CG  . PHE A 1 5   ? 19.817  16.173  44.772  1.00 18.50 ? 5   PHE A CG  1 
ATOM   33   C CD1 . PHE A 1 5   ? 18.622  15.535  44.457  1.00 16.98 ? 5   PHE A CD1 1 
ATOM   34   C CD2 . PHE A 1 5   ? 20.839  16.182  43.835  1.00 17.90 ? 5   PHE A CD2 1 
ATOM   35   C CE1 . PHE A 1 5   ? 18.449  14.908  43.226  1.00 17.52 ? 5   PHE A CE1 1 
ATOM   36   C CE2 . PHE A 1 5   ? 20.686  15.531  42.594  1.00 21.65 ? 5   PHE A CE2 1 
ATOM   37   C CZ  . PHE A 1 5   ? 19.493  14.909  42.288  1.00 23.19 ? 5   PHE A CZ  1 
ATOM   38   N N   . LEU A 1 6   ? 18.045  18.297  48.528  1.00 11.83 ? 6   LEU A N   1 
ATOM   39   C CA  . LEU A 1 6   ? 17.951  18.882  49.855  1.00 12.84 ? 6   LEU A CA  1 
ATOM   40   C C   . LEU A 1 6   ? 18.005  17.750  50.863  1.00 12.88 ? 6   LEU A C   1 
ATOM   41   O O   . LEU A 1 6   ? 17.276  16.766  50.719  1.00 13.21 ? 6   LEU A O   1 
ATOM   42   C CB  . LEU A 1 6   ? 16.642  19.645  49.996  1.00 15.66 ? 6   LEU A CB  1 
ATOM   43   C CG  . LEU A 1 6   ? 16.390  20.334  51.333  1.00 13.66 ? 6   LEU A CG  1 
ATOM   44   C CD1 . LEU A 1 6   ? 17.505  21.347  51.622  1.00 12.57 ? 6   LEU A CD1 1 
ATOM   45   C CD2 . LEU A 1 6   ? 15.048  21.028  51.282  1.00 12.94 ? 6   LEU A CD2 1 
ATOM   46   N N   . VAL A 1 7   ? 18.862  17.880  51.875  1.00 10.89 ? 7   VAL A N   1 
ATOM   47   C CA  . VAL A 1 7   ? 19.068  16.795  52.838  1.00 9.72  ? 7   VAL A CA  1 
ATOM   48   C C   . VAL A 1 7   ? 18.956  17.396  54.232  1.00 11.26 ? 7   VAL A C   1 
ATOM   49   O O   . VAL A 1 7   ? 19.845  18.143  54.654  1.00 13.64 ? 7   VAL A O   1 
ATOM   50   C CB  . VAL A 1 7   ? 20.446  16.123  52.651  1.00 11.25 ? 7   VAL A CB  1 
ATOM   51   C CG1 . VAL A 1 7   ? 20.493  14.851  53.494  1.00 18.75 ? 7   VAL A CG1 1 
ATOM   52   C CG2 . VAL A 1 7   ? 20.723  15.744  51.173  1.00 12.87 ? 7   VAL A CG2 1 
ATOM   53   N N   . PHE A 1 8   ? 17.890  17.065  54.956  1.00 9.40  ? 8   PHE A N   1 
ATOM   54   C CA  . PHE A 1 8   ? 17.771  17.489  56.356  1.00 9.16  ? 8   PHE A CA  1 
ATOM   55   C C   . PHE A 1 8   ? 18.381  16.417  57.236  1.00 8.19  ? 8   PHE A C   1 
ATOM   56   O O   . PHE A 1 8   ? 18.102  15.239  57.051  1.00 10.56 ? 8   PHE A O   1 
ATOM   57   C CB  . PHE A 1 8   ? 16.307  17.665  56.780  1.00 8.95  ? 8   PHE A CB  1 
ATOM   58   C CG  . PHE A 1 8   ? 15.634  18.883  56.212  1.00 9.61  ? 8   PHE A CG  1 
ATOM   59   C CD1 . PHE A 1 8   ? 15.711  20.101  56.863  1.00 11.92 ? 8   PHE A CD1 1 
ATOM   60   C CD2 . PHE A 1 8   ? 14.882  18.785  55.054  1.00 11.86 ? 8   PHE A CD2 1 
ATOM   61   C CE1 . PHE A 1 8   ? 15.075  21.222  56.348  1.00 14.20 ? 8   PHE A CE1 1 
ATOM   62   C CE2 . PHE A 1 8   ? 14.237  19.906  54.521  1.00 13.18 ? 8   PHE A CE2 1 
ATOM   63   C CZ  . PHE A 1 8   ? 14.326  21.130  55.176  1.00 15.61 ? 8   PHE A CZ  1 
ATOM   64   N N   . TRP A 1 9   ? 19.165  16.817  58.232  1.00 7.68  ? 9   TRP A N   1 
ATOM   65   C CA  . TRP A 1 9   ? 19.751  15.847  59.166  1.00 7.76  ? 9   TRP A CA  1 
ATOM   66   C C   . TRP A 1 9   ? 19.600  16.450  60.557  1.00 8.67  ? 9   TRP A C   1 
ATOM   67   O O   . TRP A 1 9   ? 20.309  17.391  60.927  1.00 11.59 ? 9   TRP A O   1 
ATOM   68   C CB  . TRP A 1 9   ? 21.206  15.573  58.801  1.00 9.24  ? 9   TRP A CB  1 
ATOM   69   C CG  . TRP A 1 9   ? 21.831  14.286  59.392  1.00 8.62  ? 9   TRP A CG  1 
ATOM   70   C CD1 . TRP A 1 9   ? 21.298  13.425  60.321  1.00 11.81 ? 9   TRP A CD1 1 
ATOM   71   C CD2 . TRP A 1 9   ? 23.125  13.779  59.074  1.00 8.54  ? 9   TRP A CD2 1 
ATOM   72   N NE1 . TRP A 1 9   ? 22.201  12.406  60.600  1.00 10.68 ? 9   TRP A NE1 1 
ATOM   73   C CE2 . TRP A 1 9   ? 23.328  12.612  59.850  1.00 10.80 ? 9   TRP A CE2 1 
ATOM   74   C CE3 . TRP A 1 9   ? 24.137  14.207  58.208  1.00 10.53 ? 9   TRP A CE3 1 
ATOM   75   C CZ2 . TRP A 1 9   ? 24.501  11.851  59.763  1.00 11.19 ? 9   TRP A CZ2 1 
ATOM   76   C CZ3 . TRP A 1 9   ? 25.295  13.462  58.119  1.00 15.26 ? 9   TRP A CZ3 1 
ATOM   77   C CH2 . TRP A 1 9   ? 25.471  12.301  58.913  1.00 15.32 ? 9   TRP A CH2 1 
ATOM   78   N N   . TRP A 1 10  ? 18.592  15.975  61.285  1.00 9.19  ? 10  TRP A N   1 
ATOM   79   C CA  . TRP A 1 10  ? 18.209  16.545  62.574  1.00 6.90  ? 10  TRP A CA  1 
ATOM   80   C C   . TRP A 1 10  ? 18.927  15.754  63.664  1.00 11.52 ? 10  TRP A C   1 
ATOM   81   O O   . TRP A 1 10  ? 18.667  14.555  63.826  1.00 9.66  ? 10  TRP A O   1 
ATOM   82   C CB  . TRP A 1 10  ? 16.702  16.407  62.767  1.00 6.15  ? 10  TRP A CB  1 
ATOM   83   C CG  . TRP A 1 10  ? 15.818  17.135  61.800  1.00 8.35  ? 10  TRP A CG  1 
ATOM   84   C CD1 . TRP A 1 10  ? 14.923  16.601  60.897  1.00 10.98 ? 10  TRP A CD1 1 
ATOM   85   C CD2 . TRP A 1 10  ? 15.694  18.559  61.675  1.00 7.22  ? 10  TRP A CD2 1 
ATOM   86   N NE1 . TRP A 1 10  ? 14.279  17.596  60.217  1.00 9.67  ? 10  TRP A NE1 1 
ATOM   87   C CE2 . TRP A 1 10  ? 14.705  18.805  60.696  1.00 6.70  ? 10  TRP A CE2 1 
ATOM   88   C CE3 . TRP A 1 10  ? 16.277  19.658  62.342  1.00 9.74  ? 10  TRP A CE3 1 
ATOM   89   C CZ2 . TRP A 1 10  ? 14.329  20.088  60.321  1.00 7.98  ? 10  TRP A CZ2 1 
ATOM   90   C CZ3 . TRP A 1 10  ? 15.888  20.971  61.961  1.00 11.90 ? 10  TRP A CZ3 1 
ATOM   91   C CH2 . TRP A 1 10  ? 14.905  21.155  60.973  1.00 9.62  ? 10  TRP A CH2 1 
ATOM   92   N N   . HIS A 1 11  ? 19.789  16.401  64.444  1.00 8.75  ? 11  HIS A N   1 
ATOM   93   C CA  . HIS A 1 11  ? 20.615  15.670  65.405  1.00 10.10 ? 11  HIS A CA  1 
ATOM   94   C C   . HIS A 1 11  ? 20.025  15.727  66.818  1.00 7.43  ? 11  HIS A C   1 
ATOM   95   O O   . HIS A 1 11  ? 19.795  16.800  67.359  1.00 7.47  ? 11  HIS A O   1 
ATOM   96   C CB  . HIS A 1 11  ? 22.041  16.235  65.347  1.00 10.39 ? 11  HIS A CB  1 
ATOM   97   C CG  . HIS A 1 11  ? 22.834  16.042  66.599  1.00 9.68  ? 11  HIS A CG  1 
ATOM   98   N ND1 . HIS A 1 11  ? 23.290  14.810  67.028  1.00 8.30  ? 11  HIS A ND1 1 
ATOM   99   C CD2 . HIS A 1 11  ? 23.185  16.929  67.551  1.00 10.77 ? 11  HIS A CD2 1 
ATOM   100  C CE1 . HIS A 1 11  ? 23.933  14.966  68.174  1.00 7.33  ? 11  HIS A CE1 1 
ATOM   101  N NE2 . HIS A 1 11  ? 23.858  16.241  68.531  1.00 11.25 ? 11  HIS A NE2 1 
ATOM   102  N N   . MET A 1 12  ? 19.868  14.576  67.456  1.00 7.50  ? 12  MET A N   1 
ATOM   103  C CA  . MET A 1 12  ? 19.191  14.446  68.744  1.00 9.40  ? 12  MET A CA  1 
ATOM   104  C C   . MET A 1 12  ? 20.190  13.913  69.766  1.00 8.95  ? 12  MET A C   1 
ATOM   105  O O   . MET A 1 12  ? 20.765  12.830  69.551  1.00 8.04  ? 12  MET A O   1 
ATOM   106  C CB  . MET A 1 12  ? 18.018  13.451  68.628  1.00 7.53  ? 12  MET A CB  1 
ATOM   107  C CG  . MET A 1 12  ? 16.994  13.740  67.465  1.00 6.04  ? 12  MET A CG  1 
ATOM   108  S SD  . MET A 1 12  ? 16.294  15.385  67.623  1.00 9.47  ? 12  MET A SD  1 
ATOM   109  C CE  . MET A 1 12  ? 14.971  15.185  66.421  1.00 9.26  ? 12  MET A CE  1 
ATOM   110  N N   . HIS A 1 13  ? 20.347  14.606  70.897  1.00 8.25  ? 13  HIS A N   1 
ATOM   111  C CA  . HIS A 1 13  ? 21.312  14.148  71.891  1.00 9.24  ? 13  HIS A CA  1 
ATOM   112  C C   . HIS A 1 13  ? 20.937  14.664  73.273  1.00 10.48 ? 13  HIS A C   1 
ATOM   113  O O   . HIS A 1 13  ? 20.420  15.774  73.401  1.00 11.05 ? 13  HIS A O   1 
ATOM   114  C CB  . HIS A 1 13  ? 22.717  14.616  71.488  1.00 6.37  ? 13  HIS A CB  1 
ATOM   115  C CG  . HIS A 1 13  ? 23.733  14.511  72.579  1.00 6.88  ? 13  HIS A CG  1 
ATOM   116  N ND1 . HIS A 1 13  ? 24.096  13.317  73.163  1.00 8.91  ? 13  HIS A ND1 1 
ATOM   117  C CD2 . HIS A 1 13  ? 24.454  15.472  73.203  1.00 8.08  ? 13  HIS A CD2 1 
ATOM   118  C CE1 . HIS A 1 13  ? 25.005  13.544  74.097  1.00 9.22  ? 13  HIS A CE1 1 
ATOM   119  N NE2 . HIS A 1 13  ? 25.245  14.846  74.138  1.00 9.51  ? 13  HIS A NE2 1 
ATOM   120  N N   . GLN A 1 14  ? 21.213  13.866  74.312  1.00 8.15  ? 14  GLN A N   1 
ATOM   121  C CA  . GLN A 1 14  ? 21.272  14.421  75.684  1.00 9.11  ? 14  GLN A CA  1 
ATOM   122  C C   . GLN A 1 14  ? 22.450  13.740  76.355  1.00 7.75  ? 14  GLN A C   1 
ATOM   123  O O   . GLN A 1 14  ? 22.600  12.502  76.233  1.00 10.14 ? 14  GLN A O   1 
ATOM   124  C CB  . GLN A 1 14  ? 20.020  14.173  76.558  1.00 10.28 ? 14  GLN A CB  1 
ATOM   125  C CG  . GLN A 1 14  ? 18.715  14.829  76.015  1.00 9.93  ? 14  GLN A CG  1 
ATOM   126  C CD  . GLN A 1 14  ? 18.729  16.327  76.143  1.00 8.48  ? 14  GLN A CD  1 
ATOM   127  O OE1 . GLN A 1 14  ? 19.454  16.875  76.965  1.00 11.08 ? 14  GLN A OE1 1 
ATOM   128  N NE2 . GLN A 1 14  ? 17.973  16.998  75.302  1.00 8.91  ? 14  GLN A NE2 1 
ATOM   129  N N   . PRO A 1 15  ? 23.234  14.472  77.144  1.00 9.40  ? 15  PRO A N   1 
ATOM   130  C CA  . PRO A 1 15  ? 24.257  13.821  77.990  1.00 11.76 ? 15  PRO A CA  1 
ATOM   131  C C   . PRO A 1 15  ? 23.577  13.010  79.087  1.00 9.72  ? 15  PRO A C   1 
ATOM   132  O O   . PRO A 1 15  ? 22.386  13.167  79.345  1.00 10.74 ? 15  PRO A O   1 
ATOM   133  C CB  . PRO A 1 15  ? 25.059  14.998  78.576  1.00 12.47 ? 15  PRO A CB  1 
ATOM   134  C CG  . PRO A 1 15  ? 24.027  16.146  78.668  1.00 10.30 ? 15  PRO A CG  1 
ATOM   135  C CD  . PRO A 1 15  ? 23.101  15.924  77.410  1.00 6.98  ? 15  PRO A CD  1 
ATOM   136  N N   . LEU A 1 16  ? 24.349  12.160  79.770  1.00 11.24 ? 16  LEU A N   1 
ATOM   137  C CA  . LEU A 1 16  ? 23.755  11.267  80.768  1.00 12.60 ? 16  LEU A CA  1 
ATOM   138  C C   . LEU A 1 16  ? 23.411  12.054  82.028  1.00 9.23  ? 16  LEU A C   1 
ATOM   139  O O   . LEU A 1 16  ? 24.309  12.492  82.759  1.00 11.57 ? 16  LEU A O   1 
ATOM   140  C CB  . LEU A 1 16  ? 24.710  10.126  81.091  1.00 12.82 ? 16  LEU A CB  1 
ATOM   141  C CG  . LEU A 1 16  ? 24.119  9.016   81.982  1.00 11.91 ? 16  LEU A CG  1 
ATOM   142  C CD1 . LEU A 1 16  ? 22.770  8.462   81.440  1.00 14.31 ? 16  LEU A CD1 1 
ATOM   143  C CD2 . LEU A 1 16  ? 25.126  7.911   82.047  1.00 15.41 ? 16  LEU A CD2 1 
ATOM   144  N N   . TYR A 1 17  ? 22.114  12.172  82.337  1.00 9.88  ? 17  TYR A N   1 
ATOM   145  C CA  . TYR A 1 17  ? 21.676  12.898  83.521  1.00 11.64 ? 17  TYR A CA  1 
ATOM   146  C C   . TYR A 1 17  ? 21.570  12.016  84.763  1.00 11.79 ? 17  TYR A C   1 
ATOM   147  O O   . TYR A 1 17  ? 21.237  12.516  85.844  1.00 12.95 ? 17  TYR A O   1 
ATOM   148  C CB  . TYR A 1 17  ? 20.315  13.552  83.258  1.00 13.04 ? 17  TYR A CB  1 
ATOM   149  C CG  . TYR A 1 17  ? 20.377  14.647  82.209  1.00 10.31 ? 17  TYR A CG  1 
ATOM   150  C CD1 . TYR A 1 17  ? 21.205  15.759  82.370  1.00 12.46 ? 17  TYR A CD1 1 
ATOM   151  C CD2 . TYR A 1 17  ? 19.606  14.574  81.042  1.00 11.10 ? 17  TYR A CD2 1 
ATOM   152  C CE1 . TYR A 1 17  ? 21.269  16.777  81.377  1.00 11.24 ? 17  TYR A CE1 1 
ATOM   153  C CE2 . TYR A 1 17  ? 19.670  15.559  80.071  1.00 10.57 ? 17  TYR A CE2 1 
ATOM   154  C CZ  . TYR A 1 17  ? 20.495  16.646  80.226  1.00 11.16 ? 17  TYR A CZ  1 
ATOM   155  O OH  . TYR A 1 17  ? 20.539  17.637  79.252  1.00 10.56 ? 17  TYR A OH  1 
ATOM   156  N N   . ARG A 1 18  ? 21.828  10.721  84.622  1.00 10.93 ? 18  ARG A N   1 
ATOM   157  C CA  . ARG A 1 18  ? 21.622  9.731   85.678  1.00 13.84 ? 18  ARG A CA  1 
ATOM   158  C C   . ARG A 1 18  ? 22.856  9.676   86.577  1.00 13.29 ? 18  ARG A C   1 
ATOM   159  O O   . ARG A 1 18  ? 23.912  9.176   86.173  1.00 16.41 ? 18  ARG A O   1 
ATOM   160  C CB  . ARG A 1 18  ? 21.353  8.371   85.042  1.00 15.40 ? 18  ARG A CB  1 
ATOM   161  C CG  . ARG A 1 18  ? 21.008  7.314   86.021  1.00 16.71 ? 18  ARG A CG  1 
ATOM   162  C CD  . ARG A 1 18  ? 20.993  5.952   85.309  1.00 22.02 ? 18  ARG A CD  1 
ATOM   163  N NE  . ARG A 1 18  ? 20.399  4.918   86.146  1.00 26.34 ? 18  ARG A NE  1 
ATOM   164  C CZ  . ARG A 1 18  ? 21.014  4.319   87.160  1.00 26.31 ? 18  ARG A CZ  1 
ATOM   165  N NH1 . ARG A 1 18  ? 22.264  4.633   87.484  1.00 27.07 ? 18  ARG A NH1 1 
ATOM   166  N NH2 . ARG A 1 18  ? 20.368  3.395   87.855  1.00 34.50 ? 18  ARG A NH2 1 
ATOM   167  N N   . GLU A 1 19  ? 22.717  10.169  87.779  1.00 13.14 ? 19  GLU A N   1 
ATOM   168  C CA  . GLU A 1 19  ? 23.817  10.163  88.737  1.00 13.66 ? 19  GLU A CA  1 
ATOM   169  C C   . GLU A 1 19  ? 24.147  8.726   89.120  1.00 16.88 ? 19  GLU A C   1 
ATOM   170  O O   . GLU A 1 19  ? 23.240  7.966   89.458  1.00 18.62 ? 19  GLU A O   1 
ATOM   171  C CB  . GLU A 1 19  ? 23.402  10.974  89.960  1.00 22.62 ? 19  GLU A CB  1 
ATOM   172  C CG  . GLU A 1 19  ? 24.556  11.606  90.715  1.00 28.86 ? 19  GLU A CG  1 
ATOM   173  C CD  . GLU A 1 19  ? 25.120  10.694  91.777  1.00 32.52 ? 19  GLU A CD  1 
ATOM   174  O OE1 . GLU A 1 19  ? 24.470  9.695   92.122  1.00 30.15 ? 19  GLU A OE1 1 
ATOM   175  O OE2 . GLU A 1 19  ? 26.230  10.977  92.251  1.00 39.21 ? 19  GLU A OE2 1 
ATOM   176  N N   . PRO A 1 20  ? 25.422  8.321   89.101  1.00 19.72 ? 20  PRO A N   1 
ATOM   177  C CA  . PRO A 1 20  ? 25.732  6.883   89.154  1.00 19.98 ? 20  PRO A CA  1 
ATOM   178  C C   . PRO A 1 20  ? 25.610  6.270   90.534  1.00 25.90 ? 20  PRO A C   1 
ATOM   179  O O   . PRO A 1 20  ? 25.497  5.039   90.640  1.00 32.84 ? 20  PRO A O   1 
ATOM   180  C CB  . PRO A 1 20  ? 27.178  6.815   88.623  1.00 19.02 ? 20  PRO A CB  1 
ATOM   181  C CG  . PRO A 1 20  ? 27.745  8.173   88.875  1.00 22.86 ? 20  PRO A CG  1 
ATOM   182  C CD  . PRO A 1 20  ? 26.603  9.133   88.738  1.00 19.67 ? 20  PRO A CD  1 
ATOM   183  N N   . TYR A 1 21  ? 25.610  7.069   91.594  1.00 21.28 ? 21  TYR A N   1 
ATOM   184  C CA  . TYR A 1 21  ? 25.565  6.475   92.920  1.00 23.45 ? 21  TYR A CA  1 
ATOM   185  C C   . TYR A 1 21  ? 24.133  6.342   93.420  1.00 26.59 ? 21  TYR A C   1 
ATOM   186  O O   . TYR A 1 21  ? 23.785  5.331   94.036  1.00 32.99 ? 21  TYR A O   1 
ATOM   187  C CB  . TYR A 1 21  ? 26.432  7.292   93.888  1.00 24.71 ? 21  TYR A CB  1 
ATOM   188  C CG  . TYR A 1 21  ? 27.918  7.196   93.563  1.00 27.86 ? 21  TYR A CG  1 
ATOM   189  C CD1 . TYR A 1 21  ? 28.698  6.182   94.095  1.00 26.82 ? 21  TYR A CD1 1 
ATOM   190  C CD2 . TYR A 1 21  ? 28.529  8.102   92.693  1.00 31.43 ? 21  TYR A CD2 1 
ATOM   191  C CE1 . TYR A 1 21  ? 30.049  6.075   93.791  1.00 25.87 ? 21  TYR A CE1 1 
ATOM   192  C CE2 . TYR A 1 21  ? 29.885  8.004   92.375  1.00 30.23 ? 21  TYR A CE2 1 
ATOM   193  C CZ  . TYR A 1 21  ? 30.641  6.986   92.934  1.00 32.28 ? 21  TYR A CZ  1 
ATOM   194  O OH  . TYR A 1 21  ? 31.990  6.857   92.649  1.00 30.29 ? 21  TYR A OH  1 
ATOM   195  N N   . THR A 1 22  ? 23.285  7.327   93.133  1.00 19.79 ? 22  THR A N   1 
ATOM   196  C CA  . THR A 1 22  ? 21.882  7.290   93.522  1.00 20.01 ? 22  THR A CA  1 
ATOM   197  C C   . THR A 1 22  ? 20.966  6.775   92.423  1.00 26.22 ? 22  THR A C   1 
ATOM   198  O O   . THR A 1 22  ? 19.825  6.389   92.715  1.00 24.84 ? 22  THR A O   1 
ATOM   199  C CB  . THR A 1 22  ? 21.401  8.692   93.928  1.00 20.50 ? 22  THR A CB  1 
ATOM   200  O OG1 . THR A 1 22  ? 21.495  9.590   92.806  1.00 22.89 ? 22  THR A OG1 1 
ATOM   201  C CG2 . THR A 1 22  ? 22.216  9.248   95.081  1.00 21.86 ? 22  THR A CG2 1 
ATOM   202  N N   . GLY A 1 23  ? 21.411  6.799   91.167  1.00 19.84 ? 23  GLY A N   1 
ATOM   203  C CA  . GLY A 1 23  ? 20.543  6.424   90.081  1.00 17.03 ? 23  GLY A CA  1 
ATOM   204  C C   . GLY A 1 23  ? 19.530  7.471   89.706  1.00 20.40 ? 23  GLY A C   1 
ATOM   205  O O   . GLY A 1 23  ? 18.689  7.215   88.839  1.00 25.17 ? 23  GLY A O   1 
ATOM   206  N N   . GLU A 1 24  ? 19.592  8.652   90.308  1.00 21.26 ? 24  GLU A N   1 
ATOM   207  C CA  . GLU A 1 24  ? 18.588  9.676   90.073  1.00 19.98 ? 24  GLU A CA  1 
ATOM   208  C C   . GLU A 1 24  ? 18.935  10.494  88.839  1.00 14.41 ? 24  GLU A C   1 
ATOM   209  O O   . GLU A 1 24  ? 20.100  10.806  88.613  1.00 15.02 ? 24  GLU A O   1 
ATOM   210  C CB  . GLU A 1 24  ? 18.493  10.593  91.289  1.00 20.44 ? 24  GLU A CB  1 
ATOM   211  C CG  . GLU A 1 24  ? 17.836  9.892   92.457  1.00 25.38 ? 24  GLU A CG  1 
ATOM   212  C CD  . GLU A 1 24  ? 17.961  10.660  93.747  1.00 32.96 ? 24  GLU A CD  1 
ATOM   213  O OE1 . GLU A 1 24  ? 17.413  10.185  94.760  1.00 42.79 ? 24  GLU A OE1 1 
ATOM   214  O OE2 . GLU A 1 24  ? 18.616  11.720  93.753  1.00 37.92 ? 24  GLU A OE2 1 
ATOM   215  N N   . TYR A 1 25  ? 17.926  10.802  88.021  1.00 15.22 ? 25  TYR A N   1 
ATOM   216  C CA  . TYR A 1 25  ? 18.110  11.709  86.884  1.00 11.95 ? 25  TYR A CA  1 
ATOM   217  C C   . TYR A 1 25  ? 18.026  13.130  87.425  1.00 12.45 ? 25  TYR A C   1 
ATOM   218  O O   . TYR A 1 25  ? 16.966  13.553  87.893  1.00 14.09 ? 25  TYR A O   1 
ATOM   219  C CB  . TYR A 1 25  ? 17.040  11.457  85.816  1.00 15.33 ? 25  TYR A CB  1 
ATOM   220  C CG  . TYR A 1 25  ? 17.377  10.317  84.873  1.00 14.09 ? 25  TYR A CG  1 
ATOM   221  C CD1 . TYR A 1 25  ? 17.304  8.992   85.280  1.00 17.28 ? 25  TYR A CD1 1 
ATOM   222  C CD2 . TYR A 1 25  ? 17.793  10.590  83.568  1.00 15.71 ? 25  TYR A CD2 1 
ATOM   223  C CE1 . TYR A 1 25  ? 17.633  7.963   84.402  1.00 21.01 ? 25  TYR A CE1 1 
ATOM   224  C CE2 . TYR A 1 25  ? 18.127  9.596   82.709  1.00 16.15 ? 25  TYR A CE2 1 
ATOM   225  C CZ  . TYR A 1 25  ? 18.052  8.292   83.115  1.00 17.38 ? 25  TYR A CZ  1 
ATOM   226  O OH  . TYR A 1 25  ? 18.396  7.309   82.200  1.00 19.14 ? 25  TYR A OH  1 
ATOM   227  N N   . LEU A 1 26  ? 19.144  13.867  87.381  1.00 12.34 ? 26  LEU A N   1 
ATOM   228  C CA  . LEU A 1 26  ? 19.224  15.130  88.113  1.00 13.26 ? 26  LEU A CA  1 
ATOM   229  C C   . LEU A 1 26  ? 18.639  16.301  87.354  1.00 11.53 ? 26  LEU A C   1 
ATOM   230  O O   . LEU A 1 26  ? 18.400  17.355  87.962  1.00 14.88 ? 26  LEU A O   1 
ATOM   231  C CB  . LEU A 1 26  ? 20.675  15.442  88.463  1.00 12.77 ? 26  LEU A CB  1 
ATOM   232  C CG  . LEU A 1 26  ? 21.271  14.394  89.392  1.00 17.64 ? 26  LEU A CG  1 
ATOM   233  C CD1 . LEU A 1 26  ? 22.708  14.830  89.792  1.00 18.88 ? 26  LEU A CD1 1 
ATOM   234  C CD2 . LEU A 1 26  ? 20.381  14.163  90.607  1.00 17.29 ? 26  LEU A CD2 1 
ATOM   235  N N   . LEU A 1 27  ? 18.426  16.157  86.050  1.00 12.79 ? 27  LEU A N   1 
ATOM   236  C CA  . LEU A 1 27  ? 17.732  17.155  85.256  1.00 11.19 ? 27  LEU A CA  1 
ATOM   237  C C   . LEU A 1 27  ? 16.726  16.424  84.385  1.00 11.00 ? 27  LEU A C   1 
ATOM   238  O O   . LEU A 1 27  ? 16.945  15.249  84.048  1.00 13.07 ? 27  LEU A O   1 
ATOM   239  C CB  . LEU A 1 27  ? 18.688  17.965  84.362  1.00 14.83 ? 27  LEU A CB  1 
ATOM   240  C CG  . LEU A 1 27  ? 19.634  18.939  85.092  1.00 15.11 ? 27  LEU A CG  1 
ATOM   241  C CD1 . LEU A 1 27  ? 20.767  19.403  84.181  1.00 15.22 ? 27  LEU A CD1 1 
ATOM   242  C CD2 . LEU A 1 27  ? 18.863  20.127  85.649  1.00 18.65 ? 27  LEU A CD2 1 
ATOM   243  N N   . PRO A 1 28  ? 15.609  17.070  84.052  1.00 12.78 ? 28  PRO A N   1 
ATOM   244  C CA  . PRO A 1 28  ? 14.510  16.402  83.340  1.00 11.42 ? 28  PRO A CA  1 
ATOM   245  C C   . PRO A 1 28  ? 14.551  16.556  81.827  1.00 11.01 ? 28  PRO A C   1 
ATOM   246  O O   . PRO A 1 28  ? 13.561  16.228  81.169  1.00 12.03 ? 28  PRO A O   1 
ATOM   247  C CB  . PRO A 1 28  ? 13.278  17.121  83.910  1.00 10.89 ? 28  PRO A CB  1 
ATOM   248  C CG  . PRO A 1 28  ? 13.751  18.561  84.042  1.00 14.67 ? 28  PRO A CG  1 
ATOM   249  C CD  . PRO A 1 28  ? 15.233  18.435  84.489  1.00 14.19 ? 28  PRO A CD  1 
ATOM   250  N N   . TRP A 1 29  ? 15.653  17.053  81.263  1.00 9.21  ? 29  TRP A N   1 
ATOM   251  C CA  . TRP A 1 29  ? 15.618  17.473  79.863  1.00 10.04 ? 29  TRP A CA  1 
ATOM   252  C C   . TRP A 1 29  ? 15.383  16.318  78.895  1.00 10.19 ? 29  TRP A C   1 
ATOM   253  O O   . TRP A 1 29  ? 14.787  16.539  77.829  1.00 11.28 ? 29  TRP A O   1 
ATOM   254  C CB  . TRP A 1 29  ? 16.917  18.182  79.521  1.00 9.69  ? 29  TRP A CB  1 
ATOM   255  C CG  . TRP A 1 29  ? 17.187  19.451  80.349  1.00 11.90 ? 29  TRP A CG  1 
ATOM   256  C CD1 . TRP A 1 29  ? 18.309  19.705  81.077  1.00 9.89  ? 29  TRP A CD1 1 
ATOM   257  C CD2 . TRP A 1 29  ? 16.354  20.619  80.475  1.00 15.32 ? 29  TRP A CD2 1 
ATOM   258  N NE1 . TRP A 1 29  ? 18.231  20.963  81.662  1.00 10.76 ? 29  TRP A NE1 1 
ATOM   259  C CE2 . TRP A 1 29  ? 17.033  21.529  81.312  1.00 12.53 ? 29  TRP A CE2 1 
ATOM   260  C CE3 . TRP A 1 29  ? 15.102  20.982  79.955  1.00 13.51 ? 29  TRP A CE3 1 
ATOM   261  C CZ2 . TRP A 1 29  ? 16.525  22.780  81.627  1.00 14.04 ? 29  TRP A CZ2 1 
ATOM   262  C CZ3 . TRP A 1 29  ? 14.591  22.251  80.283  1.00 15.65 ? 29  TRP A CZ3 1 
ATOM   263  C CH2 . TRP A 1 29  ? 15.300  23.118  81.107  1.00 16.38 ? 29  TRP A CH2 1 
ATOM   264  N N   . THR A 1 30  ? 15.805  15.091  79.231  1.00 9.33  ? 30  THR A N   1 
ATOM   265  C CA  . THR A 1 30  ? 15.502  13.969  78.340  1.00 11.56 ? 30  THR A CA  1 
ATOM   266  C C   . THR A 1 30  ? 14.004  13.706  78.302  1.00 10.11 ? 30  THR A C   1 
ATOM   267  O O   . THR A 1 30  ? 13.435  13.461  77.226  1.00 11.92 ? 30  THR A O   1 
ATOM   268  C CB  . THR A 1 30  ? 16.260  12.694  78.752  1.00 12.67 ? 30  THR A CB  1 
ATOM   269  O OG1 . THR A 1 30  ? 17.663  12.954  78.700  1.00 13.81 ? 30  THR A OG1 1 
ATOM   270  C CG2 . THR A 1 30  ? 15.923  11.509  77.769  1.00 12.62 ? 30  THR A CG2 1 
ATOM   271  N N   . PHE A 1 31  ? 13.351  13.749  79.468  1.00 9.75  ? 31  PHE A N   1 
ATOM   272  C CA  . PHE A 1 31  ? 11.906  13.559  79.509  1.00 9.74  ? 31  PHE A CA  1 
ATOM   273  C C   . PHE A 1 31  ? 11.203  14.628  78.693  1.00 11.17 ? 31  PHE A C   1 
ATOM   274  O O   . PHE A 1 31  ? 10.357  14.327  77.835  1.00 12.28 ? 31  PHE A O   1 
ATOM   275  C CB  . PHE A 1 31  ? 11.420  13.594  80.962  1.00 10.14 ? 31  PHE A CB  1 
ATOM   276  C CG  . PHE A 1 31  ? 9.922   13.546  81.094  1.00 10.63 ? 31  PHE A CG  1 
ATOM   277  C CD1 . PHE A 1 31  ? 9.253   12.336  81.100  1.00 12.14 ? 31  PHE A CD1 1 
ATOM   278  C CD2 . PHE A 1 31  ? 9.186   14.717  81.214  1.00 11.85 ? 31  PHE A CD2 1 
ATOM   279  C CE1 . PHE A 1 31  ? 7.864   12.298  81.226  1.00 13.72 ? 31  PHE A CE1 1 
ATOM   280  C CE2 . PHE A 1 31  ? 7.786   14.687  81.361  1.00 12.81 ? 31  PHE A CE2 1 
ATOM   281  C CZ  . PHE A 1 31  ? 7.137   13.497  81.342  1.00 12.65 ? 31  PHE A CZ  1 
ATOM   282  N N   . PHE A 1 32  ? 11.540  15.900  78.958  1.00 8.67  ? 32  PHE A N   1 
ATOM   283  C CA  . PHE A 1 32  ? 10.823  16.994  78.301  1.00 12.35 ? 32  PHE A CA  1 
ATOM   284  C C   . PHE A 1 32  ? 11.069  17.026  76.791  1.00 10.28 ? 32  PHE A C   1 
ATOM   285  O O   . PHE A 1 32  ? 10.126  17.244  76.011  1.00 10.14 ? 32  PHE A O   1 
ATOM   286  C CB  . PHE A 1 32  ? 11.182  18.328  78.946  1.00 11.28 ? 32  PHE A CB  1 
ATOM   287  C CG  . PHE A 1 32  ? 10.448  18.577  80.244  1.00 13.36 ? 32  PHE A CG  1 
ATOM   288  C CD1 . PHE A 1 32  ? 9.058   18.492  80.300  1.00 16.01 ? 32  PHE A CD1 1 
ATOM   289  C CD2 . PHE A 1 32  ? 11.135  18.838  81.407  1.00 14.89 ? 32  PHE A CD2 1 
ATOM   290  C CE1 . PHE A 1 32  ? 8.364   18.712  81.502  1.00 20.54 ? 32  PHE A CE1 1 
ATOM   291  C CE2 . PHE A 1 32  ? 10.445  19.046  82.609  1.00 15.42 ? 32  PHE A CE2 1 
ATOM   292  C CZ  . PHE A 1 32  ? 9.074   18.976  82.653  1.00 17.53 ? 32  PHE A CZ  1 
ATOM   293  N N   . HIS A 1 33  ? 12.296  16.741  76.336  1.00 9.22  ? 33  HIS A N   1 
ATOM   294  C CA  . HIS A 1 33  ? 12.479  16.721  74.886  1.00 7.77  ? 33  HIS A CA  1 
ATOM   295  C C   . HIS A 1 33  ? 11.926  15.476  74.235  1.00 8.02  ? 33  HIS A C   1 
ATOM   296  O O   . HIS A 1 33  ? 11.571  15.533  73.052  1.00 8.74  ? 33  HIS A O   1 
ATOM   297  C CB  . HIS A 1 33  ? 13.966  16.933  74.533  1.00 6.38  ? 33  HIS A CB  1 
ATOM   298  C CG  . HIS A 1 33  ? 14.368  18.385  74.670  1.00 6.31  ? 33  HIS A CG  1 
ATOM   299  N ND1 . HIS A 1 33  ? 13.912  19.370  73.816  1.00 11.96 ? 33  HIS A ND1 1 
ATOM   300  C CD2 . HIS A 1 33  ? 15.153  19.005  75.584  1.00 9.35  ? 33  HIS A CD2 1 
ATOM   301  C CE1 . HIS A 1 33  ? 14.420  20.532  74.190  1.00 9.63  ? 33  HIS A CE1 1 
ATOM   302  N NE2 . HIS A 1 33  ? 15.185  20.343  75.259  1.00 9.06  ? 33  HIS A NE2 1 
ATOM   303  N N   . ALA A 1 34  ? 11.813  14.378  74.978  1.00 7.52  ? 34  ALA A N   1 
ATOM   304  C CA  . ALA A 1 34  ? 11.191  13.199  74.399  1.00 10.91 ? 34  ALA A CA  1 
ATOM   305  C C   . ALA A 1 34  ? 9.713   13.470  74.144  1.00 14.78 ? 34  ALA A C   1 
ATOM   306  O O   . ALA A 1 34  ? 9.195   13.178  73.053  1.00 11.48 ? 34  ALA A O   1 
ATOM   307  C CB  . ALA A 1 34  ? 11.387  11.995  75.325  1.00 13.27 ? 34  ALA A CB  1 
ATOM   308  N N   . VAL A 1 35  ? 9.027   14.067  75.129  1.00 10.53 ? 35  VAL A N   1 
ATOM   309  C CA  . VAL A 1 35  ? 7.587   14.277  74.968  1.00 8.47  ? 35  VAL A CA  1 
ATOM   310  C C   . VAL A 1 35  ? 7.317   15.367  73.957  1.00 10.34 ? 35  VAL A C   1 
ATOM   311  O O   . VAL A 1 35  ? 6.279   15.345  73.269  1.00 10.51 ? 35  VAL A O   1 
ATOM   312  C CB  . VAL A 1 35  ? 6.875   14.569  76.307  1.00 12.15 ? 35  VAL A CB  1 
ATOM   313  C CG1 . VAL A 1 35  ? 7.204   13.490  77.350  1.00 10.62 ? 35  VAL A CG1 1 
ATOM   314  C CG2 . VAL A 1 35  ? 7.212   15.939  76.861  1.00 15.79 ? 35  VAL A CG2 1 
ATOM   315  N N   . LYS A 1 36  ? 8.241   16.316  73.822  1.00 11.07 ? 36  LYS A N   1 
ATOM   316  C CA  . LYS A 1 36  ? 8.001   17.471  72.963  1.00 10.07 ? 36  LYS A CA  1 
ATOM   317  C C   . LYS A 1 36  ? 8.530   17.260  71.545  1.00 9.80  ? 36  LYS A C   1 
ATOM   318  O O   . LYS A 1 36  ? 7.860   17.638  70.577  1.00 12.37 ? 36  LYS A O   1 
ATOM   319  C CB  . LYS A 1 36  ? 8.635   18.715  73.573  1.00 13.05 ? 36  LYS A CB  1 
ATOM   320  C CG  . LYS A 1 36  ? 8.253   19.962  72.817  1.00 9.82  ? 36  LYS A CG  1 
ATOM   321  C CD  . LYS A 1 36  ? 8.653   21.296  73.495  1.00 10.83 ? 36  LYS A CD  1 
ATOM   322  C CE  . LYS A 1 36  ? 10.160  21.590  73.307  1.00 11.22 ? 36  LYS A CE  1 
ATOM   323  N NZ  . LYS A 1 36  ? 10.507  21.944  71.880  1.00 9.55  ? 36  LYS A NZ  1 
ATOM   324  N N   . ASP A 1 37  ? 9.705   16.646  71.402  1.00 9.25  ? 37  ASP A N   1 
ATOM   325  C CA  . ASP A 1 37  ? 10.426  16.640  70.125  1.00 15.71 ? 37  ASP A CA  1 
ATOM   326  C C   . ASP A 1 37  ? 10.807  15.260  69.603  1.00 9.98  ? 37  ASP A C   1 
ATOM   327  O O   . ASP A 1 37  ? 10.727  15.041  68.395  1.00 9.98  ? 37  ASP A O   1 
ATOM   328  C CB  . ASP A 1 37  ? 11.712  17.509  70.231  1.00 9.25  ? 37  ASP A CB  1 
ATOM   329  C CG  . ASP A 1 37  ? 11.443  18.888  70.816  1.00 9.10  ? 37  ASP A CG  1 
ATOM   330  O OD1 . ASP A 1 37  ? 10.719  19.686  70.174  1.00 11.45 ? 37  ASP A OD1 1 
ATOM   331  O OD2 . ASP A 1 37  ? 11.952  19.137  71.931  1.00 8.00  ? 37  ASP A OD2 1 
ATOM   332  N N   . TYR A 1 38  ? 11.264  14.337  70.460  1.00 6.08  ? 38  TYR A N   1 
ATOM   333  C CA  . TYR A 1 38  ? 11.925  13.146  69.900  1.00 8.33  ? 38  TYR A CA  1 
ATOM   334  C C   . TYR A 1 38  ? 10.959  12.193  69.201  1.00 12.73 ? 38  TYR A C   1 
ATOM   335  O O   . TYR A 1 38  ? 11.347  11.556  68.223  1.00 10.79 ? 38  TYR A O   1 
ATOM   336  C CB  . TYR A 1 38  ? 12.706  12.397  70.990  1.00 7.89  ? 38  TYR A CB  1 
ATOM   337  C CG  . TYR A 1 38  ? 13.886  13.168  71.530  1.00 8.50  ? 38  TYR A CG  1 
ATOM   338  C CD1 . TYR A 1 38  ? 14.628  14.036  70.700  1.00 8.75  ? 38  TYR A CD1 1 
ATOM   339  C CD2 . TYR A 1 38  ? 14.248  13.064  72.874  1.00 8.75  ? 38  TYR A CD2 1 
ATOM   340  C CE1 . TYR A 1 38  ? 15.721  14.740  71.205  1.00 9.35  ? 38  TYR A CE1 1 
ATOM   341  C CE2 . TYR A 1 38  ? 15.327  13.780  73.380  1.00 7.76  ? 38  TYR A CE2 1 
ATOM   342  C CZ  . TYR A 1 38  ? 16.057  14.615  72.546  1.00 12.06 ? 38  TYR A CZ  1 
ATOM   343  O OH  . TYR A 1 38  ? 17.138  15.330  73.037  1.00 9.79  ? 38  TYR A OH  1 
ATOM   344  N N   . TYR A 1 39  ? 9.723   12.041  69.691  1.00 9.03  ? 39  TYR A N   1 
ATOM   345  C CA  . TYR A 1 39  ? 8.706   11.327  68.914  1.00 10.40 ? 39  TYR A CA  1 
ATOM   346  C C   . TYR A 1 39  ? 8.203   12.182  67.754  1.00 9.15  ? 39  TYR A C   1 
ATOM   347  O O   . TYR A 1 39  ? 8.066   11.708  66.618  1.00 10.02 ? 39  TYR A O   1 
ATOM   348  C CB  . TYR A 1 39  ? 7.544   10.924  69.830  1.00 7.92  ? 39  TYR A CB  1 
ATOM   349  C CG  . TYR A 1 39  ? 6.406   10.296  69.065  1.00 9.02  ? 39  TYR A CG  1 
ATOM   350  C CD1 . TYR A 1 39  ? 6.432   8.923   68.771  1.00 11.08 ? 39  TYR A CD1 1 
ATOM   351  C CD2 . TYR A 1 39  ? 5.322   11.048  68.629  1.00 11.25 ? 39  TYR A CD2 1 
ATOM   352  C CE1 . TYR A 1 39  ? 5.410   8.326   68.049  1.00 14.51 ? 39  TYR A CE1 1 
ATOM   353  C CE2 . TYR A 1 39  ? 4.301   10.462  67.894  1.00 13.42 ? 39  TYR A CE2 1 
ATOM   354  C CZ  . TYR A 1 39  ? 4.349   9.097   67.617  1.00 15.73 ? 39  TYR A CZ  1 
ATOM   355  O OH  . TYR A 1 39  ? 3.307   8.503   66.917  1.00 19.05 ? 39  TYR A OH  1 
ATOM   356  N N   . ASP A 1 40  ? 7.951   13.459  68.017  1.00 7.77  ? 40  ASP A N   1 
ATOM   357  C CA  . ASP A 1 40  ? 7.176   14.233  67.059  1.00 9.66  ? 40  ASP A CA  1 
ATOM   358  C C   . ASP A 1 40  ? 7.970   14.656  65.838  1.00 8.51  ? 40  ASP A C   1 
ATOM   359  O O   . ASP A 1 40  ? 7.388   14.754  64.760  1.00 10.01 ? 40  ASP A O   1 
ATOM   360  C CB  . ASP A 1 40  ? 6.587   15.454  67.757  1.00 9.48  ? 40  ASP A CB  1 
ATOM   361  C CG  . ASP A 1 40  ? 5.315   15.081  68.496  1.00 12.81 ? 40  ASP A CG  1 
ATOM   362  O OD1 . ASP A 1 40  ? 4.328   14.796  67.795  1.00 13.19 ? 40  ASP A OD1 1 
ATOM   363  O OD2 . ASP A 1 40  ? 5.304   15.022  69.753  1.00 15.78 ? 40  ASP A OD2 1 
ATOM   364  N N   . MET A 1 41  ? 9.281   14.828  65.951  1.00 8.30  ? 41  MET A N   1 
ATOM   365  C CA  . MET A 1 41  ? 10.053  15.210  64.768  1.00 7.85  ? 41  MET A CA  1 
ATOM   366  C C   . MET A 1 41  ? 10.020  14.143  63.682  1.00 6.86  ? 41  MET A C   1 
ATOM   367  O O   . MET A 1 41  ? 9.652   14.485  62.536  1.00 10.37 ? 41  MET A O   1 
ATOM   368  C CB  . MET A 1 41  ? 11.488  15.584  65.171  1.00 8.01  ? 41  MET A CB  1 
ATOM   369  C CG  . MET A 1 41  ? 11.530  16.993  65.787  1.00 6.76  ? 41  MET A CG  1 
ATOM   370  S SD  . MET A 1 41  ? 11.241  18.363  64.600  1.00 9.32  ? 41  MET A SD  1 
ATOM   371  C CE  . MET A 1 41  ? 12.841  18.435  63.801  1.00 7.77  ? 41  MET A CE  1 
ATOM   372  N N   . PRO A 1 42  ? 10.281  12.851  63.955  1.00 8.83  ? 42  PRO A N   1 
ATOM   373  C CA  . PRO A 1 42  ? 10.107  11.852  62.890  1.00 10.81 ? 42  PRO A CA  1 
ATOM   374  C C   . PRO A 1 42  ? 8.637   11.582  62.539  1.00 10.94 ? 42  PRO A C   1 
ATOM   375  O O   . PRO A 1 42  ? 8.330   11.181  61.401  1.00 10.68 ? 42  PRO A O   1 
ATOM   376  C CB  . PRO A 1 42  ? 10.785  10.603  63.477  1.00 13.32 ? 42  PRO A CB  1 
ATOM   377  C CG  . PRO A 1 42  ? 10.815  10.829  64.997  1.00 11.26 ? 42  PRO A CG  1 
ATOM   378  C CD  . PRO A 1 42  ? 10.994  12.307  65.141  1.00 8.03  ? 42  PRO A CD  1 
ATOM   379  N N   . ALA A 1 43  ? 7.720   11.799  63.487  1.00 8.09  ? 43  ALA A N   1 
ATOM   380  C CA  . ALA A 1 43  ? 6.299   11.578  63.224  1.00 8.72  ? 43  ALA A CA  1 
ATOM   381  C C   . ALA A 1 43  ? 5.714   12.523  62.178  1.00 12.06 ? 43  ALA A C   1 
ATOM   382  O O   . ALA A 1 43  ? 4.641   12.226  61.616  1.00 12.87 ? 43  ALA A O   1 
ATOM   383  C CB  . ALA A 1 43  ? 5.488   11.685  64.524  1.00 11.03 ? 43  ALA A CB  1 
ATOM   384  N N   . TYR A 1 44  ? 6.357   13.668  61.920  1.00 9.82  ? 44  TYR A N   1 
ATOM   385  C CA  . TYR A 1 44  ? 5.931   14.472  60.772  1.00 13.46 ? 44  TYR A CA  1 
ATOM   386  C C   . TYR A 1 44  ? 5.908   13.662  59.480  1.00 12.68 ? 44  TYR A C   1 
ATOM   387  O O   . TYR A 1 44  ? 5.121   13.971  58.572  1.00 12.15 ? 44  TYR A O   1 
ATOM   388  C CB  . TYR A 1 44  ? 6.853   15.669  60.564  1.00 12.28 ? 44  TYR A CB  1 
ATOM   389  C CG  . TYR A 1 44  ? 6.596   16.859  61.462  1.00 10.41 ? 44  TYR A CG  1 
ATOM   390  C CD1 . TYR A 1 44  ? 5.671   17.857  61.105  1.00 11.93 ? 44  TYR A CD1 1 
ATOM   391  C CD2 . TYR A 1 44  ? 7.330   17.036  62.642  1.00 8.97  ? 44  TYR A CD2 1 
ATOM   392  C CE1 . TYR A 1 44  ? 5.462   18.981  61.925  1.00 11.28 ? 44  TYR A CE1 1 
ATOM   393  C CE2 . TYR A 1 44  ? 7.106   18.136  63.468  1.00 9.98  ? 44  TYR A CE2 1 
ATOM   394  C CZ  . TYR A 1 44  ? 6.199   19.102  63.101  1.00 11.76 ? 44  TYR A CZ  1 
ATOM   395  O OH  . TYR A 1 44  ? 6.034   20.177  63.934  1.00 11.69 ? 44  TYR A OH  1 
ATOM   396  N N   . LEU A 1 45  ? 6.774   12.633  59.372  1.00 9.85  ? 45  LEU A N   1 
ATOM   397  C CA  . LEU A 1 45  ? 6.847   11.835  58.141  1.00 11.55 ? 45  LEU A CA  1 
ATOM   398  C C   . LEU A 1 45  ? 5.598   10.994  57.896  1.00 16.24 ? 45  LEU A C   1 
ATOM   399  O O   . LEU A 1 45  ? 5.389   10.541  56.763  1.00 16.95 ? 45  LEU A O   1 
ATOM   400  C CB  . LEU A 1 45  ? 8.095   10.955  58.178  1.00 12.77 ? 45  LEU A CB  1 
ATOM   401  C CG  . LEU A 1 45  ? 9.410   11.730  58.048  1.00 13.34 ? 45  LEU A CG  1 
ATOM   402  C CD1 . LEU A 1 45  ? 10.606  10.898  58.425  1.00 13.49 ? 45  LEU A CD1 1 
ATOM   403  C CD2 . LEU A 1 45  ? 9.579   12.293  56.627  1.00 13.07 ? 45  LEU A CD2 1 
ATOM   404  N N   . LYS A 1 46  ? 4.751   10.781  58.913  1.00 11.36 ? 46  LYS A N   1 
ATOM   405  C CA  . LYS A 1 46  ? 3.469   10.133  58.659  1.00 20.94 ? 46  LYS A CA  1 
ATOM   406  C C   . LYS A 1 46  ? 2.525   11.019  57.857  1.00 21.43 ? 46  LYS A C   1 
ATOM   407  O O   . LYS A 1 46  ? 1.620   10.505  57.183  1.00 20.36 ? 46  LYS A O   1 
ATOM   408  C CB  . LYS A 1 46  ? 2.802   9.752   59.979  1.00 20.72 ? 46  LYS A CB  1 
ATOM   409  C CG  . LYS A 1 46  ? 3.607   8.790   60.822  1.00 23.60 ? 46  LYS A CG  1 
ATOM   410  C CD  . LYS A 1 46  ? 3.211   8.916   62.282  1.00 35.11 ? 46  LYS A CD  1 
ATOM   411  C CE  . LYS A 1 46  ? 2.420   7.721   62.733  1.00 49.85 ? 46  LYS A CE  1 
ATOM   412  N NZ  . LYS A 1 46  ? 1.629   8.038   63.954  1.00 58.14 ? 46  LYS A NZ  1 
ATOM   413  N N   . ASP A 1 47  ? 2.686   12.348  57.954  1.00 15.17 ? 47  ASP A N   1 
ATOM   414  C CA  . ASP A 1 47  ? 1.760   13.297  57.346  1.00 18.72 ? 47  ASP A CA  1 
ATOM   415  C C   . ASP A 1 47  ? 2.320   14.038  56.136  1.00 16.42 ? 47  ASP A C   1 
ATOM   416  O O   . ASP A 1 47  ? 1.539   14.636  55.387  1.00 18.89 ? 47  ASP A O   1 
ATOM   417  C CB  . ASP A 1 47  ? 1.315   14.335  58.385  1.00 18.39 ? 47  ASP A CB  1 
ATOM   418  C CG  . ASP A 1 47  ? 0.502   13.726  59.509  1.00 26.13 ? 47  ASP A CG  1 
ATOM   419  O OD1 . ASP A 1 47  ? -0.229  12.746  59.262  1.00 24.45 ? 47  ASP A OD1 1 
ATOM   420  O OD2 . ASP A 1 47  ? 0.591   14.244  60.642  1.00 27.53 ? 47  ASP A OD2 1 
ATOM   421  N N   . PHE A 1 48  ? 3.627   13.997  55.903  1.00 13.96 ? 48  PHE A N   1 
ATOM   422  C CA  . PHE A 1 48  ? 4.230   14.716  54.791  1.00 17.66 ? 48  PHE A CA  1 
ATOM   423  C C   . PHE A 1 48  ? 5.140   13.771  54.029  1.00 12.77 ? 48  PHE A C   1 
ATOM   424  O O   . PHE A 1 48  ? 5.978   13.092  54.627  1.00 18.76 ? 48  PHE A O   1 
ATOM   425  C CB  . PHE A 1 48  ? 4.998   15.947  55.280  1.00 20.63 ? 48  PHE A CB  1 
ATOM   426  C CG  . PHE A 1 48  ? 4.128   16.924  56.002  1.00 16.43 ? 48  PHE A CG  1 
ATOM   427  C CD1 . PHE A 1 48  ? 3.340   17.837  55.304  1.00 16.11 ? 48  PHE A CD1 1 
ATOM   428  C CD2 . PHE A 1 48  ? 4.051   16.901  57.379  1.00 13.89 ? 48  PHE A CD2 1 
ATOM   429  C CE1 . PHE A 1 48  ? 2.501   18.700  55.983  1.00 18.78 ? 48  PHE A CE1 1 
ATOM   430  C CE2 . PHE A 1 48  ? 3.229   17.789  58.072  1.00 19.13 ? 48  PHE A CE2 1 
ATOM   431  C CZ  . PHE A 1 48  ? 2.448   18.682  57.376  1.00 17.50 ? 48  PHE A CZ  1 
ATOM   432  N N   . GLU A 1 49  ? 4.993   13.758  52.710  1.00 15.81 ? 49  GLU A N   1 
ATOM   433  C CA  . GLU A 1 49  ? 5.671   12.774  51.862  1.00 21.30 ? 49  GLU A CA  1 
ATOM   434  C C   . GLU A 1 49  ? 7.021   13.302  51.366  1.00 18.67 ? 49  GLU A C   1 
ATOM   435  O O   . GLU A 1 49  ? 7.271   13.419  50.170  1.00 23.15 ? 49  GLU A O   1 
ATOM   436  C CB  . GLU A 1 49  ? 4.772   12.392  50.688  1.00 25.94 ? 49  GLU A CB  1 
ATOM   437  C CG  . GLU A 1 49  ? 3.548   11.572  51.087  1.00 48.84 ? 49  GLU A CG  1 
ATOM   438  C CD  . GLU A 1 49  ? 3.916   10.289  51.822  1.00 67.94 ? 49  GLU A CD  1 
ATOM   439  O OE1 . GLU A 1 49  ? 3.560   10.165  53.016  1.00 74.09 ? 49  GLU A OE1 1 
ATOM   440  O OE2 . GLU A 1 49  ? 4.558   9.403   51.212  1.00 73.94 ? 49  GLU A OE2 1 
ATOM   441  N N   . ILE A 1 50  ? 7.901   13.620  52.311  1.00 16.16 ? 50  ILE A N   1 
ATOM   442  C CA  . ILE A 1 50  ? 9.265   14.032  52.000  1.00 13.77 ? 50  ILE A CA  1 
ATOM   443  C C   . ILE A 1 50  ? 10.225  13.116  52.751  1.00 16.93 ? 50  ILE A C   1 
ATOM   444  O O   . ILE A 1 50  ? 9.793   12.213  53.474  1.00 17.68 ? 50  ILE A O   1 
ATOM   445  C CB  . ILE A 1 50  ? 9.507   15.499  52.391  1.00 16.86 ? 50  ILE A CB  1 
ATOM   446  C CG1 . ILE A 1 50  ? 9.287   15.684  53.893  1.00 20.20 ? 50  ILE A CG1 1 
ATOM   447  C CG2 . ILE A 1 50  ? 8.627   16.422  51.539  1.00 22.44 ? 50  ILE A CG2 1 
ATOM   448  C CD1 . ILE A 1 50  ? 9.746   17.003  54.366  1.00 21.49 ? 50  ILE A CD1 1 
ATOM   449  N N   . LYS A 1 51  ? 11.527  13.303  52.544  1.00 10.27 ? 51  LYS A N   1 
ATOM   450  C CA  . LYS A 1 51  ? 12.553  12.557  53.277  1.00 11.57 ? 51  LYS A CA  1 
ATOM   451  C C   . LYS A 1 51  ? 13.162  13.444  54.357  1.00 10.60 ? 51  LYS A C   1 
ATOM   452  O O   . LYS A 1 51  ? 13.458  14.614  54.102  1.00 10.24 ? 51  LYS A O   1 
ATOM   453  C CB  . LYS A 1 51  ? 13.669  12.051  52.341  1.00 11.40 ? 51  LYS A CB  1 
ATOM   454  C CG  . LYS A 1 51  ? 13.184  11.335  51.104  1.00 14.91 ? 51  LYS A CG  1 
ATOM   455  C CD  . LYS A 1 51  ? 12.445  10.059  51.440  1.00 15.92 ? 51  LYS A CD  1 
ATOM   456  C CE  . LYS A 1 51  ? 12.243  9.233   50.163  1.00 24.54 ? 51  LYS A CE  1 
ATOM   457  N NZ  . LYS A 1 51  ? 11.398  8.065   50.492  1.00 34.92 ? 51  LYS A NZ  1 
ATOM   458  N N   . LEU A 1 52  ? 13.311  12.905  55.571  1.00 9.38  ? 52  LEU A N   1 
ATOM   459  C CA  . LEU A 1 52  ? 13.987  13.609  56.666  1.00 8.22  ? 52  LEU A CA  1 
ATOM   460  C C   . LEU A 1 52  ? 14.875  12.624  57.385  1.00 11.53 ? 52  LEU A C   1 
ATOM   461  O O   . LEU A 1 52  ? 14.476  11.475  57.598  1.00 13.17 ? 52  LEU A O   1 
ATOM   462  C CB  . LEU A 1 52  ? 13.021  14.190  57.704  1.00 11.16 ? 52  LEU A CB  1 
ATOM   463  C CG  . LEU A 1 52  ? 11.993  15.188  57.203  1.00 11.18 ? 52  LEU A CG  1 
ATOM   464  C CD1 . LEU A 1 52  ? 10.933  15.392  58.316  1.00 10.35 ? 52  LEU A CD1 1 
ATOM   465  C CD2 . LEU A 1 52  ? 12.606  16.552  56.756  1.00 14.49 ? 52  LEU A CD2 1 
ATOM   466  N N   . ASN A 1 53  ? 16.080  13.053  57.759  1.00 9.72  ? 53  ASN A N   1 
ATOM   467  C CA  . ASN A 1 53  ? 17.022  12.128  58.387  1.00 7.97  ? 53  ASN A CA  1 
ATOM   468  C C   . ASN A 1 53  ? 17.291  12.565  59.823  1.00 7.43  ? 53  ASN A C   1 
ATOM   469  O O   . ASN A 1 53  ? 17.089  13.739  60.187  1.00 8.43  ? 53  ASN A O   1 
ATOM   470  C CB  . ASN A 1 53  ? 18.341  12.080  57.606  1.00 8.37  ? 53  ASN A CB  1 
ATOM   471  C CG  . ASN A 1 53  ? 18.102  11.813  56.145  1.00 8.97  ? 53  ASN A CG  1 
ATOM   472  O OD1 . ASN A 1 53  ? 17.857  10.679  55.767  1.00 10.37 ? 53  ASN A OD1 1 
ATOM   473  N ND2 . ASN A 1 53  ? 18.162  12.851  55.301  1.00 9.10  ? 53  ASN A ND2 1 
ATOM   474  N N   . PHE A 1 54  ? 17.745  11.621  60.647  1.00 8.98  ? 54  PHE A N   1 
ATOM   475  C CA  . PHE A 1 54  ? 17.911  11.872  62.064  1.00 7.07  ? 54  PHE A CA  1 
ATOM   476  C C   . PHE A 1 54  ? 19.196  11.232  62.547  1.00 10.54 ? 54  PHE A C   1 
ATOM   477  O O   . PHE A 1 54  ? 19.570  10.150  62.090  1.00 9.53  ? 54  PHE A O   1 
ATOM   478  C CB  . PHE A 1 54  ? 16.707  11.313  62.857  1.00 9.83  ? 54  PHE A CB  1 
ATOM   479  C CG  . PHE A 1 54  ? 15.401  11.916  62.435  1.00 6.89  ? 54  PHE A CG  1 
ATOM   480  C CD1 . PHE A 1 54  ? 14.695  11.396  61.346  1.00 9.40  ? 54  PHE A CD1 1 
ATOM   481  C CD2 . PHE A 1 54  ? 14.955  13.104  63.038  1.00 9.11  ? 54  PHE A CD2 1 
ATOM   482  C CE1 . PHE A 1 54  ? 13.494  11.989  60.918  1.00 10.86 ? 54  PHE A CE1 1 
ATOM   483  C CE2 . PHE A 1 54  ? 13.756  13.677  62.640  1.00 12.24 ? 54  PHE A CE2 1 
ATOM   484  C CZ  . PHE A 1 54  ? 13.061  13.183  61.569  1.00 11.14 ? 54  PHE A CZ  1 
ATOM   485  N N   . ASN A 1 55  ? 19.825  11.861  63.516  1.00 8.51  ? 55  ASN A N   1 
ATOM   486  C CA  . ASN A 1 55  ? 20.920  11.263  64.268  1.00 11.15 ? 55  ASN A CA  1 
ATOM   487  C C   . ASN A 1 55  ? 20.434  11.031  65.691  1.00 8.97  ? 55  ASN A C   1 
ATOM   488  O O   . ASN A 1 55  ? 19.807  11.919  66.278  1.00 9.12  ? 55  ASN A O   1 
ATOM   489  C CB  . ASN A 1 55  ? 22.131  12.190  64.305  1.00 12.40 ? 55  ASN A CB  1 
ATOM   490  C CG  . ASN A 1 55  ? 23.332  11.511  64.957  1.00 11.82 ? 55  ASN A CG  1 
ATOM   491  O OD1 . ASN A 1 55  ? 23.805  10.500  64.461  1.00 12.00 ? 55  ASN A OD1 1 
ATOM   492  N ND2 . ASN A 1 55  ? 23.824  12.067  66.065  1.00 9.90  ? 55  ASN A ND2 1 
ATOM   493  N N   . LEU A 1 56  ? 20.709  9.854   66.245  1.00 8.74  ? 56  LEU A N   1 
ATOM   494  C CA  . LEU A 1 56  ? 20.428  9.574   67.656  1.00 11.99 ? 56  LEU A CA  1 
ATOM   495  C C   . LEU A 1 56  ? 21.733  9.189   68.330  1.00 10.16 ? 56  LEU A C   1 
ATOM   496  O O   . LEU A 1 56  ? 22.340  8.192   67.945  1.00 12.61 ? 56  LEU A O   1 
ATOM   497  C CB  . LEU A 1 56  ? 19.437  8.421   67.803  1.00 15.15 ? 56  LEU A CB  1 
ATOM   498  C CG  . LEU A 1 56  ? 18.041  8.631   67.202  1.00 14.25 ? 56  LEU A CG  1 
ATOM   499  C CD1 . LEU A 1 56  ? 17.278  7.272   67.238  1.00 15.19 ? 56  LEU A CD1 1 
ATOM   500  C CD2 . LEU A 1 56  ? 17.308  9.714   68.002  1.00 15.06 ? 56  LEU A CD2 1 
ATOM   501  N N   . THR A 1 57  ? 22.131  9.914   69.366  1.00 9.01  ? 57  THR A N   1 
ATOM   502  C CA  . THR A 1 57  ? 23.318  9.464   70.078  1.00 9.19  ? 57  THR A CA  1 
ATOM   503  C C   . THR A 1 57  ? 22.983  8.235   70.934  1.00 10.69 ? 57  THR A C   1 
ATOM   504  O O   . THR A 1 57  ? 21.865  8.102   71.450  1.00 9.81  ? 57  THR A O   1 
ATOM   505  C CB  . THR A 1 57  ? 23.943  10.572  70.940  1.00 7.67  ? 57  THR A CB  1 
ATOM   506  O OG1 . THR A 1 57  ? 23.071  10.919  72.020  1.00 8.87  ? 57  THR A OG1 1 
ATOM   507  C CG2 . THR A 1 57  ? 24.272  11.837  70.076  1.00 10.36 ? 57  THR A CG2 1 
ATOM   508  N N   . PRO A 1 58  ? 23.928  7.329   71.110  1.00 8.85  ? 58  PRO A N   1 
ATOM   509  C CA  . PRO A 1 58  ? 23.631  6.135   71.927  1.00 9.86  ? 58  PRO A CA  1 
ATOM   510  C C   . PRO A 1 58  ? 23.267  6.492   73.360  1.00 13.11 ? 58  PRO A C   1 
ATOM   511  O O   . PRO A 1 58  ? 22.404  5.821   73.954  1.00 11.27 ? 58  PRO A O   1 
ATOM   512  C CB  . PRO A 1 58  ? 24.927  5.328   71.832  1.00 14.25 ? 58  PRO A CB  1 
ATOM   513  C CG  . PRO A 1 58  ? 25.506  5.766   70.488  1.00 11.76 ? 58  PRO A CG  1 
ATOM   514  C CD  . PRO A 1 58  ? 25.261  7.228   70.482  1.00 9.23  ? 58  PRO A CD  1 
ATOM   515  N N   . VAL A 1 59  ? 23.913  7.516   73.938  1.00 11.90 ? 59  VAL A N   1 
ATOM   516  C CA  . VAL A 1 59  ? 23.612  7.885   75.328  1.00 11.71 ? 59  VAL A CA  1 
ATOM   517  C C   . VAL A 1 59  ? 22.184  8.424   75.436  1.00 13.31 ? 59  VAL A C   1 
ATOM   518  O O   . VAL A 1 59  ? 21.481  8.152   76.421  1.00 10.96 ? 59  VAL A O   1 
ATOM   519  C CB  . VAL A 1 59  ? 24.678  8.868   75.881  1.00 9.33  ? 59  VAL A CB  1 
ATOM   520  C CG1 . VAL A 1 59  ? 24.766  10.166  75.053  1.00 9.95  ? 59  VAL A CG1 1 
ATOM   521  C CG2 . VAL A 1 59  ? 24.384  9.203   77.372  1.00 10.86 ? 59  VAL A CG2 1 
ATOM   522  N N   . LEU A 1 60  ? 21.694  9.131   74.405  1.00 8.74  ? 60  LEU A N   1 
ATOM   523  C CA  . LEU A 1 60  ? 20.281  9.514   74.393  1.00 9.72  ? 60  LEU A CA  1 
ATOM   524  C C   . LEU A 1 60  ? 19.371  8.300   74.338  1.00 12.83 ? 60  LEU A C   1 
ATOM   525  O O   . LEU A 1 60  ? 18.383  8.217   75.085  1.00 10.95 ? 60  LEU A O   1 
ATOM   526  C CB  . LEU A 1 60  ? 19.993  10.432  73.195  1.00 6.75  ? 60  LEU A CB  1 
ATOM   527  C CG  . LEU A 1 60  ? 18.489  10.727  73.032  1.00 8.28  ? 60  LEU A CG  1 
ATOM   528  C CD1 . LEU A 1 60  ? 17.863  11.482  74.225  1.00 10.10 ? 60  LEU A CD1 1 
ATOM   529  C CD2 . LEU A 1 60  ? 18.289  11.641  71.784  1.00 8.00  ? 60  LEU A CD2 1 
ATOM   530  N N   . ILE A 1 61  ? 19.678  7.345   73.452  1.00 9.94  ? 61  ILE A N   1 
ATOM   531  C CA  . ILE A 1 61  ? 18.866  6.141   73.332  1.00 10.78 ? 61  ILE A CA  1 
ATOM   532  C C   . ILE A 1 61  ? 18.759  5.419   74.674  1.00 9.41  ? 61  ILE A C   1 
ATOM   533  O O   . ILE A 1 61  ? 17.663  5.037   75.101  1.00 10.30 ? 61  ILE A O   1 
ATOM   534  C CB  . ILE A 1 61  ? 19.448  5.231   72.244  1.00 8.87  ? 61  ILE A CB  1 
ATOM   535  C CG1 . ILE A 1 61  ? 19.323  5.894   70.870  1.00 11.34 ? 61  ILE A CG1 1 
ATOM   536  C CG2 . ILE A 1 61  ? 18.751  3.861   72.264  1.00 11.58 ? 61  ILE A CG2 1 
ATOM   537  C CD1 . ILE A 1 61  ? 20.085  5.113   69.798  1.00 12.00 ? 61  ILE A CD1 1 
ATOM   538  N N   . ASP A 1 62  ? 19.893  5.259   75.379  1.00 10.79 ? 62  ASP A N   1 
ATOM   539  C CA  . ASP A 1 62  ? 19.886  4.585   76.690  1.00 11.65 ? 62  ASP A CA  1 
ATOM   540  C C   . ASP A 1 62  ? 18.879  5.221   77.637  1.00 11.13 ? 62  ASP A C   1 
ATOM   541  O O   . ASP A 1 62  ? 18.160  4.531   78.363  1.00 14.11 ? 62  ASP A O   1 
ATOM   542  C CB  . ASP A 1 62  ? 21.272  4.678   77.345  1.00 13.14 ? 62  ASP A CB  1 
ATOM   543  C CG  . ASP A 1 62  ? 22.282  3.699   76.762  1.00 19.25 ? 62  ASP A CG  1 
ATOM   544  O OD1 . ASP A 1 62  ? 21.881  2.696   76.127  1.00 22.67 ? 62  ASP A OD1 1 
ATOM   545  O OD2 . ASP A 1 62  ? 23.499  3.937   76.952  1.00 18.07 ? 62  ASP A OD2 1 
ATOM   546  N N   . GLN A 1 63  ? 18.838  6.546   77.656  1.00 8.84  ? 63  GLN A N   1 
ATOM   547  C CA  . GLN A 1 63  ? 17.949  7.247   78.574  1.00 10.00 ? 63  GLN A CA  1 
ATOM   548  C C   . GLN A 1 63  ? 16.493  7.149   78.145  1.00 9.69  ? 63  GLN A C   1 
ATOM   549  O O   . GLN A 1 63  ? 15.596  6.973   78.986  1.00 11.55 ? 63  GLN A O   1 
ATOM   550  C CB  . GLN A 1 63  ? 18.363  8.706   78.631  1.00 7.92  ? 63  GLN A CB  1 
ATOM   551  C CG  . GLN A 1 63  ? 19.754  8.929   79.218  1.00 8.40  ? 63  GLN A CG  1 
ATOM   552  C CD  . GLN A 1 63  ? 20.129  10.404  79.207  1.00 15.76 ? 63  GLN A CD  1 
ATOM   553  O OE1 . GLN A 1 63  ? 19.678  11.205  80.038  1.00 19.81 ? 63  GLN A OE1 1 
ATOM   554  N NE2 . GLN A 1 63  ? 20.949  10.774  78.248  1.00 11.02 ? 63  GLN A NE2 1 
ATOM   555  N N   . ILE A 1 64  ? 16.219  7.283   76.845  1.00 10.93 ? 64  ILE A N   1 
ATOM   556  C CA  . ILE A 1 64  ? 14.839  7.074   76.391  1.00 9.35  ? 64  ILE A CA  1 
ATOM   557  C C   . ILE A 1 64  ? 14.356  5.679   76.796  1.00 11.22 ? 64  ILE A C   1 
ATOM   558  O O   . ILE A 1 64  ? 13.217  5.513   77.267  1.00 12.17 ? 64  ILE A O   1 
ATOM   559  C CB  . ILE A 1 64  ? 14.733  7.299   74.871  1.00 8.49  ? 64  ILE A CB  1 
ATOM   560  C CG1 . ILE A 1 64  ? 15.027  8.777   74.529  1.00 10.09 ? 64  ILE A CG1 1 
ATOM   561  C CG2 . ILE A 1 64  ? 13.324  6.899   74.362  1.00 11.33 ? 64  ILE A CG2 1 
ATOM   562  C CD1 . ILE A 1 64  ? 15.172  8.979   73.024  1.00 11.26 ? 64  ILE A CD1 1 
ATOM   563  N N   . GLN A 1 65  ? 15.204  4.661   76.625  1.00 11.79 ? 65  GLN A N   1 
ATOM   564  C CA  . GLN A 1 65  ? 14.826  3.310   77.030  1.00 13.81 ? 65  GLN A CA  1 
ATOM   565  C C   . GLN A 1 65  ? 14.514  3.234   78.521  1.00 14.99 ? 65  GLN A C   1 
ATOM   566  O O   . GLN A 1 65  ? 13.543  2.575   78.926  1.00 15.76 ? 65  GLN A O   1 
ATOM   567  C CB  . GLN A 1 65  ? 15.947  2.332   76.666  1.00 13.79 ? 65  GLN A CB  1 
ATOM   568  C CG  . GLN A 1 65  ? 16.080  2.136   75.161  1.00 16.79 ? 65  GLN A CG  1 
ATOM   569  C CD  . GLN A 1 65  ? 17.214  1.185   74.800  1.00 21.31 ? 65  GLN A CD  1 
ATOM   570  O OE1 . GLN A 1 65  ? 18.357  1.367   75.223  1.00 23.05 ? 65  GLN A OE1 1 
ATOM   571  N NE2 . GLN A 1 65  ? 16.896  0.149   74.027  1.00 27.56 ? 65  GLN A NE2 1 
ATOM   572  N N   . GLU A 1 66  ? 15.319  3.897   79.350  1.00 14.83 ? 66  GLU A N   1 
ATOM   573  C CA  . GLU A 1 66  ? 15.070  3.840   80.790  1.00 17.39 ? 66  GLU A CA  1 
ATOM   574  C C   . GLU A 1 66  ? 13.747  4.517   81.153  1.00 13.60 ? 66  GLU A C   1 
ATOM   575  O O   . GLU A 1 66  ? 12.985  3.987   81.971  1.00 16.36 ? 66  GLU A O   1 
ATOM   576  C CB  . GLU A 1 66  ? 16.246  4.450   81.559  1.00 18.19 ? 66  GLU A CB  1 
ATOM   577  C CG  . GLU A 1 66  ? 16.187  4.140   83.063  1.00 26.78 ? 66  GLU A CG  1 
ATOM   578  C CD  . GLU A 1 66  ? 17.482  4.456   83.813  1.00 26.20 ? 66  GLU A CD  1 
ATOM   579  O OE1 . GLU A 1 66  ? 18.449  4.916   83.174  1.00 26.63 ? 66  GLU A OE1 1 
ATOM   580  O OE2 . GLU A 1 66  ? 17.512  4.274   85.053  1.00 28.96 ? 66  GLU A OE2 1 
ATOM   581  N N   . TYR A 1 67  ? 13.449  5.686   80.559  1.00 12.47 ? 67  TYR A N   1 
ATOM   582  C CA  . TYR A 1 67  ? 12.147  6.300   80.818  1.00 12.74 ? 67  TYR A CA  1 
ATOM   583  C C   . TYR A 1 67  ? 11.010  5.416   80.324  1.00 19.20 ? 67  TYR A C   1 
ATOM   584  O O   . TYR A 1 67  ? 9.986   5.260   81.008  1.00 15.73 ? 67  TYR A O   1 
ATOM   585  C CB  . TYR A 1 67  ? 12.054  7.683   80.152  1.00 10.75 ? 67  TYR A CB  1 
ATOM   586  C CG  . TYR A 1 67  ? 12.707  8.812   80.941  1.00 14.02 ? 67  TYR A CG  1 
ATOM   587  C CD1 . TYR A 1 67  ? 12.004  9.483   81.928  1.00 14.18 ? 67  TYR A CD1 1 
ATOM   588  C CD2 . TYR A 1 67  ? 14.020  9.192   80.697  1.00 11.88 ? 67  TYR A CD2 1 
ATOM   589  C CE1 . TYR A 1 67  ? 12.571  10.522  82.644  1.00 10.43 ? 67  TYR A CE1 1 
ATOM   590  C CE2 . TYR A 1 67  ? 14.625  10.256  81.427  1.00 13.08 ? 67  TYR A CE2 1 
ATOM   591  C CZ  . TYR A 1 67  ? 13.886  10.884  82.410  1.00 12.84 ? 67  TYR A CZ  1 
ATOM   592  O OH  . TYR A 1 67  ? 14.429  11.938  83.137  1.00 15.73 ? 67  TYR A OH  1 
ATOM   593  N N   . ALA A 1 68  ? 11.161  4.843   79.124  1.00 19.12 ? 68  ALA A N   1 
ATOM   594  C CA  . ALA A 1 68  ? 10.095  4.024   78.562  1.00 15.49 ? 68  ALA A CA  1 
ATOM   595  C C   . ALA A 1 68  ? 9.836   2.779   79.410  1.00 15.53 ? 68  ALA A C   1 
ATOM   596  O O   . ALA A 1 68  ? 8.705   2.264   79.442  1.00 19.87 ? 68  ALA A O   1 
ATOM   597  C CB  . ALA A 1 68  ? 10.455  3.654   77.121  1.00 14.93 ? 68  ALA A CB  1 
ATOM   598  N N   . GLN A 1 69  ? 10.855  2.290   80.111  1.00 18.86 ? 69  GLN A N   1 
ATOM   599  C CA  . GLN A 1 69  ? 10.715  1.103   80.950  1.00 20.37 ? 69  GLN A CA  1 
ATOM   600  C C   . GLN A 1 69  ? 10.180  1.408   82.344  1.00 22.65 ? 69  GLN A C   1 
ATOM   601  O O   . GLN A 1 69  ? 10.042  0.482   83.158  1.00 28.16 ? 69  GLN A O   1 
ATOM   602  C CB  . GLN A 1 69  ? 12.060  0.382   81.073  1.00 24.77 ? 69  GLN A CB  1 
ATOM   603  C CG  . GLN A 1 69  ? 12.492  -0.306  79.781  1.00 30.56 ? 69  GLN A CG  1 
ATOM   604  C CD  . GLN A 1 69  ? 13.982  -0.632  79.756  1.00 39.33 ? 69  GLN A CD  1 
ATOM   605  O OE1 . GLN A 1 69  ? 14.675  -0.527  80.773  1.00 43.85 ? 69  GLN A OE1 1 
ATOM   606  N NE2 . GLN A 1 69  ? 14.485  -1.003  78.583  1.00 40.29 ? 69  GLN A NE2 1 
ATOM   607  N N   . GLY A 1 70  ? 9.880   2.665   82.645  1.00 19.35 ? 70  GLY A N   1 
ATOM   608  C CA  . GLY A 1 70  ? 9.463   2.995   83.994  1.00 20.99 ? 70  GLY A CA  1 
ATOM   609  C C   . GLY A 1 70  ? 10.572  2.909   85.012  1.00 28.94 ? 70  GLY A C   1 
ATOM   610  O O   . GLY A 1 70  ? 10.288  2.769   86.199  1.00 34.87 ? 70  GLY A O   1 
ATOM   611  N N   . LYS A 1 71  ? 11.837  3.000   84.584  1.00 21.74 ? 71  LYS A N   1 
ATOM   612  C CA  . LYS A 1 71  ? 12.970  2.864   85.499  1.00 24.13 ? 71  LYS A CA  1 
ATOM   613  C C   . LYS A 1 71  ? 13.617  4.190   85.896  1.00 25.55 ? 71  LYS A C   1 
ATOM   614  O O   . LYS A 1 71  ? 14.407  4.209   86.845  1.00 27.31 ? 71  LYS A O   1 
ATOM   615  C CB  . LYS A 1 71  ? 14.049  1.962   84.879  1.00 27.89 ? 71  LYS A CB  1 
ATOM   616  C CG  . LYS A 1 71  ? 13.667  0.483   84.773  1.00 32.91 ? 71  LYS A CG  1 
ATOM   617  C CD  . LYS A 1 71  ? 14.732  -0.314  84.033  1.00 35.75 ? 71  LYS A CD  1 
ATOM   618  C CE  . LYS A 1 71  ? 14.322  -1.772  83.877  1.00 46.10 ? 71  LYS A CE  1 
ATOM   619  N NZ  . LYS A 1 71  ? 15.283  -2.554  83.038  1.00 51.09 ? 71  LYS A NZ  1 
ATOM   620  N N   . ALA A 1 72  ? 13.333  5.282   85.194  1.00 19.24 ? 72  ALA A N   1 
ATOM   621  C CA  . ALA A 1 72  ? 14.048  6.532   85.435  1.00 19.34 ? 72  ALA A CA  1 
ATOM   622  C C   . ALA A 1 72  ? 13.482  7.239   86.669  1.00 22.06 ? 72  ALA A C   1 
ATOM   623  O O   . ALA A 1 72  ? 12.289  7.550   86.724  1.00 25.56 ? 72  ALA A O   1 
ATOM   624  C CB  . ALA A 1 72  ? 13.970  7.433   84.197  1.00 17.19 ? 72  ALA A CB  1 
ATOM   625  N N   . LYS A 1 73  ? 14.338  7.474   87.664  1.00 19.46 ? 73  LYS A N   1 
ATOM   626  C CA  . LYS A 1 73  ? 13.972  8.240   88.852  1.00 20.22 ? 73  LYS A CA  1 
ATOM   627  C C   . LYS A 1 73  ? 14.352  9.694   88.588  1.00 21.02 ? 73  LYS A C   1 
ATOM   628  O O   . LYS A 1 73  ? 15.481  10.112  88.824  1.00 24.01 ? 73  LYS A O   1 
ATOM   629  C CB  . LYS A 1 73  ? 14.680  7.699   90.088  1.00 25.79 ? 73  LYS A CB  1 
ATOM   630  C CG  . LYS A 1 73  ? 14.328  6.266   90.450  1.00 34.85 ? 73  LYS A CG  1 
ATOM   631  C CD  . LYS A 1 73  ? 14.709  5.967   91.892  1.00 45.32 ? 73  LYS A CD  1 
ATOM   632  C CE  . LYS A 1 73  ? 16.214  6.000   92.064  1.00 51.45 ? 73  LYS A CE  1 
ATOM   633  N NZ  . LYS A 1 73  ? 16.860  4.953   91.237  1.00 55.18 ? 73  LYS A NZ  1 
ATOM   634  N N   . ASP A 1 74  ? 13.399  10.469  88.114  1.00 19.18 ? 74  ASP A N   1 
ATOM   635  C CA  . ASP A 1 74  ? 13.617  11.847  87.676  1.00 14.05 ? 74  ASP A CA  1 
ATOM   636  C C   . ASP A 1 74  ? 13.178  12.795  88.792  1.00 16.21 ? 74  ASP A C   1 
ATOM   637  O O   . ASP A 1 74  ? 11.982  12.919  89.067  1.00 16.71 ? 74  ASP A O   1 
ATOM   638  C CB  . ASP A 1 74  ? 12.834  12.079  86.381  1.00 13.56 ? 74  ASP A CB  1 
ATOM   639  C CG  . ASP A 1 74  ? 13.028  13.472  85.794  1.00 19.21 ? 74  ASP A CG  1 
ATOM   640  O OD1 . ASP A 1 74  ? 12.998  14.479  86.545  1.00 18.52 ? 74  ASP A OD1 1 
ATOM   641  O OD2 . ASP A 1 74  ? 13.191  13.574  84.557  1.00 18.89 ? 74  ASP A OD2 1 
ATOM   642  N N   . VAL A 1 75  ? 14.143  13.463  89.439  1.00 18.49 ? 75  VAL A N   1 
ATOM   643  C CA  . VAL A 1 75  ? 13.810  14.218  90.653  1.00 20.03 ? 75  VAL A CA  1 
ATOM   644  C C   . VAL A 1 75  ? 12.894  15.400  90.343  1.00 21.92 ? 75  VAL A C   1 
ATOM   645  O O   . VAL A 1 75  ? 11.966  15.697  91.111  1.00 18.80 ? 75  VAL A O   1 
ATOM   646  C CB  . VAL A 1 75  ? 15.087  14.655  91.399  1.00 24.58 ? 75  VAL A CB  1 
ATOM   647  C CG1 . VAL A 1 75  ? 15.899  13.442  91.795  1.00 22.13 ? 75  VAL A CG1 1 
ATOM   648  C CG2 . VAL A 1 75  ? 15.913  15.591  90.567  1.00 26.32 ? 75  VAL A CG2 1 
ATOM   649  N N   . PHE A 1 76  ? 13.102  16.085  89.216  1.00 18.51 ? 76  PHE A N   1 
ATOM   650  C CA  . PHE A 1 76  ? 12.206  17.187  88.891  1.00 19.61 ? 76  PHE A CA  1 
ATOM   651  C C   . PHE A 1 76  ? 10.806  16.689  88.552  1.00 18.74 ? 76  PHE A C   1 
ATOM   652  O O   . PHE A 1 76  ? 9.800   17.307  88.930  1.00 17.03 ? 76  PHE A O   1 
ATOM   653  C CB  . PHE A 1 76  ? 12.766  18.006  87.732  1.00 20.57 ? 76  PHE A CB  1 
ATOM   654  C CG  . PHE A 1 76  ? 12.002  19.245  87.477  1.00 26.68 ? 76  PHE A CG  1 
ATOM   655  C CD1 . PHE A 1 76  ? 12.273  20.393  88.205  1.00 29.19 ? 76  PHE A CD1 1 
ATOM   656  C CD2 . PHE A 1 76  ? 10.998  19.275  86.520  1.00 29.65 ? 76  PHE A CD2 1 
ATOM   657  C CE1 . PHE A 1 76  ? 11.553  21.547  87.983  1.00 31.28 ? 76  PHE A CE1 1 
ATOM   658  C CE2 . PHE A 1 76  ? 10.271  20.433  86.289  1.00 27.30 ? 76  PHE A CE2 1 
ATOM   659  C CZ  . PHE A 1 76  ? 10.546  21.567  87.024  1.00 32.34 ? 76  PHE A CZ  1 
ATOM   660  N N   . LEU A 1 77  ? 10.712  15.570  87.836  1.00 17.02 ? 77  LEU A N   1 
ATOM   661  C CA  . LEU A 1 77  ? 9.396   15.063  87.496  1.00 18.33 ? 77  LEU A CA  1 
ATOM   662  C C   . LEU A 1 77  ? 8.666   14.578  88.742  1.00 20.56 ? 77  LEU A C   1 
ATOM   663  O O   . LEU A 1 77  ? 7.439   14.674  88.812  1.00 22.03 ? 77  LEU A O   1 
ATOM   664  C CB  . LEU A 1 77  ? 9.526   13.946  86.462  1.00 19.49 ? 77  LEU A CB  1 
ATOM   665  C CG  . LEU A 1 77  ? 8.313   13.527  85.655  1.00 31.09 ? 77  LEU A CG  1 
ATOM   666  C CD1 . LEU A 1 77  ? 7.656   14.732  84.983  1.00 25.70 ? 77  LEU A CD1 1 
ATOM   667  C CD2 . LEU A 1 77  ? 8.781   12.488  84.639  1.00 32.98 ? 77  LEU A CD2 1 
ATOM   668  N N   . GLU A 1 78  ? 9.402   14.080  89.744  1.00 18.05 ? 78  GLU A N   1 
ATOM   669  C CA  . GLU A 1 78  ? 8.762   13.684  91.000  1.00 19.36 ? 78  GLU A CA  1 
ATOM   670  C C   . GLU A 1 78  ? 8.077   14.874  91.660  1.00 20.96 ? 78  GLU A C   1 
ATOM   671  O O   . GLU A 1 78  ? 6.984   14.729  92.232  1.00 25.08 ? 78  GLU A O   1 
ATOM   672  C CB  . GLU A 1 78  ? 9.784   13.062  91.960  1.00 24.68 ? 78  GLU A CB  1 
ATOM   673  C CG  . GLU A 1 78  ? 10.194  11.637  91.607  1.00 37.02 ? 78  GLU A CG  1 
ATOM   674  C CD  . GLU A 1 78  ? 11.386  11.147  92.427  1.00 52.42 ? 78  GLU A CD  1 
ATOM   675  O OE1 . GLU A 1 78  ? 11.869  11.902  93.303  1.00 53.66 ? 78  GLU A OE1 1 
ATOM   676  O OE2 . GLU A 1 78  ? 11.845  10.007  92.185  1.00 57.10 ? 78  GLU A OE2 1 
ATOM   677  N N   . ALA A 1 79  ? 8.692   16.061  91.562  1.00 18.54 ? 79  ALA A N   1 
ATOM   678  C CA  . ALA A 1 79  ? 8.118   17.293  92.102  1.00 20.88 ? 79  ALA A CA  1 
ATOM   679  C C   . ALA A 1 79  ? 6.884   17.758  91.325  1.00 20.10 ? 79  ALA A C   1 
ATOM   680  O O   . ALA A 1 79  ? 5.976   18.358  91.911  1.00 24.45 ? 79  ALA A O   1 
ATOM   681  C CB  . ALA A 1 79  ? 9.164   18.398  92.110  1.00 19.19 ? 79  ALA A CB  1 
ATOM   682  N N   . ILE A 1 80  ? 6.834   17.507  90.020  1.00 14.49 ? 80  ILE A N   1 
ATOM   683  C CA  . ILE A 1 80  ? 5.617   17.783  89.250  1.00 13.15 ? 80  ILE A CA  1 
ATOM   684  C C   . ILE A 1 80  ? 4.502   16.833  89.630  1.00 18.31 ? 80  ILE A C   1 
ATOM   685  O O   . ILE A 1 80  ? 3.325   17.222  89.717  1.00 18.85 ? 80  ILE A O   1 
ATOM   686  C CB  . ILE A 1 80  ? 5.920   17.680  87.742  1.00 16.37 ? 80  ILE A CB  1 
ATOM   687  C CG1 . ILE A 1 80  ? 6.934   18.743  87.322  1.00 24.45 ? 80  ILE A CG1 1 
ATOM   688  C CG2 . ILE A 1 80  ? 4.622   17.743  86.917  1.00 16.27 ? 80  ILE A CG2 1 
ATOM   689  C CD1 . ILE A 1 80  ? 6.420   20.114  87.371  1.00 27.99 ? 80  ILE A CD1 1 
ATOM   690  N N   . ARG A 1 81  ? 4.829   15.557  89.801  1.00 16.53 ? 81  ARG A N   1 
ATOM   691  C CA  . ARG A 1 81  ? 3.784   14.563  89.993  1.00 17.24 ? 81  ARG A CA  1 
ATOM   692  C C   . ARG A 1 81  ? 3.100   14.689  91.359  1.00 18.95 ? 81  ARG A C   1 
ATOM   693  O O   . ARG A 1 81  ? 1.882   14.498  91.451  1.00 22.51 ? 81  ARG A O   1 
ATOM   694  C CB  . ARG A 1 81  ? 4.368   13.161  89.809  1.00 24.36 ? 81  ARG A CB  1 
ATOM   695  C CG  . ARG A 1 81  ? 3.349   12.047  90.067  1.00 27.30 ? 81  ARG A CG  1 
ATOM   696  C CD  . ARG A 1 81  ? 3.997   10.671  90.000  1.00 36.20 ? 81  ARG A CD  1 
ATOM   697  N NE  . ARG A 1 81  ? 4.372   10.286  88.639  1.00 43.65 ? 81  ARG A NE  1 
ATOM   698  C CZ  . ARG A 1 81  ? 3.512   9.853   87.716  1.00 43.95 ? 81  ARG A CZ  1 
ATOM   699  N NH1 . ARG A 1 81  ? 2.212   9.758   87.996  1.00 38.23 ? 81  ARG A NH1 1 
ATOM   700  N NH2 . ARG A 1 81  ? 3.951   9.525   86.506  1.00 43.61 ? 81  ARG A NH2 1 
ATOM   701  N N   . LYS A 1 82  ? 3.855   14.998  92.425  1.00 16.91 ? 82  LYS A N   1 
ATOM   702  C CA  . LYS A 1 82  ? 3.302   15.003  93.785  1.00 20.27 ? 82  LYS A CA  1 
ATOM   703  C C   . LYS A 1 82  ? 2.113   15.953  93.919  1.00 16.33 ? 82  LYS A C   1 
ATOM   704  O O   . LYS A 1 82  ? 2.049   16.999  93.274  1.00 17.39 ? 82  LYS A O   1 
ATOM   705  C CB  . LYS A 1 82  ? 4.355   15.463  94.806  1.00 22.48 ? 82  LYS A CB  1 
ATOM   706  C CG  . LYS A 1 82  ? 5.515   14.574  95.026  1.00 32.41 ? 82  LYS A CG  1 
ATOM   707  C CD  . LYS A 1 82  ? 6.492   15.305  95.949  1.00 24.63 ? 82  LYS A CD  1 
ATOM   708  C CE  . LYS A 1 82  ? 7.719   14.492  96.219  1.00 36.14 ? 82  LYS A CE  1 
ATOM   709  N NZ  . LYS A 1 82  ? 8.460   15.149  97.319  1.00 37.07 ? 82  LYS A NZ  1 
ATOM   710  N N   . ASP A 1 83  ? 1.209   15.620  94.845  1.00 18.78 ? 83  ASP A N   1 
ATOM   711  C CA  . ASP A 1 83  ? 0.253   16.605  95.314  1.00 18.64 ? 83  ASP A CA  1 
ATOM   712  C C   . ASP A 1 83  ? 1.027   17.778  95.915  1.00 18.38 ? 83  ASP A C   1 
ATOM   713  O O   . ASP A 1 83  ? 2.031   17.563  96.605  1.00 17.97 ? 83  ASP A O   1 
ATOM   714  C CB  . ASP A 1 83  ? -0.670  15.984  96.368  1.00 24.80 ? 83  ASP A CB  1 
ATOM   715  C CG  . ASP A 1 83  ? -1.866  16.871  96.705  1.00 32.56 ? 83  ASP A CG  1 
ATOM   716  O OD1 . ASP A 1 83  ? -1.677  17.998  97.229  1.00 25.45 ? 83  ASP A OD1 1 
ATOM   717  O OD2 . ASP A 1 83  ? -3.013  16.425  96.464  1.00 33.42 ? 83  ASP A OD2 1 
ATOM   718  N N   . PRO A 1 84  ? 0.615   19.021  95.656  1.00 16.78 ? 84  PRO A N   1 
ATOM   719  C CA  . PRO A 1 84  ? 1.377   20.165  96.190  1.00 18.23 ? 84  PRO A CA  1 
ATOM   720  C C   . PRO A 1 84  ? 1.465   20.203  97.697  1.00 16.91 ? 84  PRO A C   1 
ATOM   721  O O   . PRO A 1 84  ? 2.448   20.748  98.228  1.00 19.99 ? 84  PRO A O   1 
ATOM   722  C CB  . PRO A 1 84  ? 0.620   21.384  95.645  1.00 19.20 ? 84  PRO A CB  1 
ATOM   723  C CG  . PRO A 1 84  ? -0.025  20.880  94.383  1.00 18.98 ? 84  PRO A CG  1 
ATOM   724  C CD  . PRO A 1 84  ? -0.431  19.444  94.704  1.00 20.46 ? 84  PRO A CD  1 
ATOM   725  N N   . ASP A 1 85  ? 0.483   19.630  98.413  1.00 17.75 ? 85  ASP A N   1 
ATOM   726  C CA  . ASP A 1 85  ? 0.591   19.533  99.870  1.00 23.19 ? 85  ASP A CA  1 
ATOM   727  C C   . ASP A 1 85  ? 1.840   18.775  100.307 1.00 22.80 ? 85  ASP A C   1 
ATOM   728  O O   . ASP A 1 85  ? 2.265   18.928  101.458 1.00 23.59 ? 85  ASP A O   1 
ATOM   729  C CB  . ASP A 1 85  ? -0.626  18.835  100.483 1.00 23.01 ? 85  ASP A CB  1 
ATOM   730  C CG  . ASP A 1 85  ? -1.894  19.686  100.423 1.00 28.76 ? 85  ASP A CG  1 
ATOM   731  O OD1 . ASP A 1 85  ? -1.771  20.926  100.296 1.00 33.44 ? 85  ASP A OD1 1 
ATOM   732  O OD2 . ASP A 1 85  ? -3.004  19.117  100.537 1.00 34.07 ? 85  ASP A OD2 1 
ATOM   733  N N   . ASP A 1 86  ? 2.412   17.949  99.431  1.00 17.84 ? 86  ASP A N   1 
ATOM   734  C CA  . ASP A 1 86  ? 3.588   17.155  99.759  1.00 20.71 ? 86  ASP A CA  1 
ATOM   735  C C   . ASP A 1 86  ? 4.886   17.733  99.206  1.00 20.77 ? 86  ASP A C   1 
ATOM   736  O O   . ASP A 1 86  ? 5.948   17.138  99.407  1.00 19.30 ? 86  ASP A O   1 
ATOM   737  C CB  . ASP A 1 86  ? 3.393   15.728  99.247  1.00 20.80 ? 86  ASP A CB  1 
ATOM   738  C CG  . ASP A 1 86  ? 2.225   15.034  99.937  1.00 29.08 ? 86  ASP A CG  1 
ATOM   739  O OD1 . ASP A 1 86  ? 1.998   15.335  101.130 1.00 40.42 ? 86  ASP A OD1 1 
ATOM   740  O OD2 . ASP A 1 86  ? 1.536   14.224  99.292  1.00 33.43 ? 86  ASP A OD2 1 
ATOM   741  N N   . LEU A 1 87  ? 4.843   18.892  98.569  1.00 16.50 ? 87  LEU A N   1 
ATOM   742  C CA  . LEU A 1 87  ? 6.059   19.455  97.991  1.00 15.93 ? 87  LEU A CA  1 
ATOM   743  C C   . LEU A 1 87  ? 6.986   19.957  99.092  1.00 16.37 ? 87  LEU A C   1 
ATOM   744  O O   . LEU A 1 87  ? 6.548   20.676  99.995  1.00 17.42 ? 87  LEU A O   1 
ATOM   745  C CB  . LEU A 1 87  ? 5.713   20.607  97.060  1.00 15.53 ? 87  LEU A CB  1 
ATOM   746  C CG  . LEU A 1 87  ? 5.187   20.198  95.684  1.00 17.30 ? 87  LEU A CG  1 
ATOM   747  C CD1 . LEU A 1 87  ? 4.615   21.413  94.915  1.00 18.97 ? 87  LEU A CD1 1 
ATOM   748  C CD2 . LEU A 1 87  ? 6.345   19.545  94.902  1.00 20.12 ? 87  LEU A CD2 1 
ATOM   749  N N   . GLU A 1 88  ? 8.264   19.599  98.991  1.00 16.39 ? 88  GLU A N   1 
ATOM   750  C CA  . GLU A 1 88  ? 9.297   20.146  99.863  1.00 16.95 ? 88  GLU A CA  1 
ATOM   751  C C   . GLU A 1 88  ? 9.560   21.593  99.478  1.00 18.25 ? 88  GLU A C   1 
ATOM   752  O O   . GLU A 1 88  ? 9.318   21.993  98.339  1.00 16.58 ? 88  GLU A O   1 
ATOM   753  C CB  . GLU A 1 88  ? 10.595  19.340  99.726  1.00 21.64 ? 88  GLU A CB  1 
ATOM   754  C CG  . GLU A 1 88  ? 10.393  17.862  99.979  1.00 23.69 ? 88  GLU A CG  1 
ATOM   755  C CD  . GLU A 1 88  ? 11.484  16.985  99.372  1.00 31.69 ? 88  GLU A CD  1 
ATOM   756  O OE1 . GLU A 1 88  ? 11.359  15.739  99.457  1.00 37.83 ? 88  GLU A OE1 1 
ATOM   757  O OE2 . GLU A 1 88  ? 12.465  17.542  98.825  1.00 28.28 ? 88  GLU A OE2 1 
ATOM   758  N N   . LYS A 1 89  ? 10.070  22.373  100.443 1.00 18.86 ? 89  LYS A N   1 
ATOM   759  C CA  . LYS A 1 89  ? 10.472  23.751  100.157 1.00 19.76 ? 89  LYS A CA  1 
ATOM   760  C C   . LYS A 1 89  ? 11.448  23.795  98.991  1.00 21.17 ? 89  LYS A C   1 
ATOM   761  O O   . LYS A 1 89  ? 11.309  24.619  98.076  1.00 21.85 ? 89  LYS A O   1 
ATOM   762  C CB  . LYS A 1 89  ? 11.106  24.391  101.398 1.00 20.08 ? 89  LYS A CB  1 
ATOM   763  C CG  . LYS A 1 89  ? 10.146  24.540  102.555 1.00 24.76 ? 89  LYS A CG  1 
ATOM   764  C CD  . LYS A 1 89  ? 10.862  24.994  103.828 1.00 28.40 ? 89  LYS A CD  1 
ATOM   765  C CE  . LYS A 1 89  ? 9.891   25.078  105.011 1.00 29.09 ? 89  LYS A CE  1 
ATOM   766  N NZ  . LYS A 1 89  ? 10.537  25.615  106.259 1.00 33.67 ? 89  LYS A NZ  1 
ATOM   767  N N   . GLU A 1 90  ? 12.440  22.900  99.011  1.00 18.72 ? 90  GLU A N   1 
ATOM   768  C CA  . GLU A 1 90  ? 13.418  22.810  97.926  1.00 22.85 ? 90  GLU A CA  1 
ATOM   769  C C   . GLU A 1 90  ? 12.752  22.517  96.579  1.00 22.09 ? 90  GLU A C   1 
ATOM   770  O O   . GLU A 1 90  ? 13.210  23.003  95.533  1.00 19.88 ? 90  GLU A O   1 
ATOM   771  C CB  . GLU A 1 90  ? 14.439  21.720  98.240  1.00 25.99 ? 90  GLU A CB  1 
ATOM   772  C CG  . GLU A 1 90  ? 15.370  22.032  99.399  1.00 50.91 ? 90  GLU A CG  1 
ATOM   773  C CD  . GLU A 1 90  ? 16.315  20.877  99.714  1.00 69.60 ? 90  GLU A CD  1 
ATOM   774  O OE1 . GLU A 1 90  ? 17.008  20.931  100.757 1.00 72.60 ? 90  GLU A OE1 1 
ATOM   775  O OE2 . GLU A 1 90  ? 16.361  19.916  98.910  1.00 73.96 ? 90  GLU A OE2 1 
ATOM   776  N N   . GLU A 1 91  ? 11.688  21.702  96.579  1.00 16.30 ? 91  GLU A N   1 
ATOM   777  C CA  . GLU A 1 91  ? 11.000  21.360  95.335  1.00 16.36 ? 91  GLU A CA  1 
ATOM   778  C C   . GLU A 1 91  ? 10.172  22.530  94.803  1.00 18.60 ? 91  GLU A C   1 
ATOM   779  O O   . GLU A 1 91  ? 10.066  22.719  93.581  1.00 17.64 ? 91  GLU A O   1 
ATOM   780  C CB  . GLU A 1 91  ? 10.109  20.136  95.555  1.00 19.84 ? 91  GLU A CB  1 
ATOM   781  C CG  . GLU A 1 91  ? 10.885  18.839  95.815  1.00 21.02 ? 91  GLU A CG  1 
ATOM   782  C CD  . GLU A 1 91  ? 9.976   17.644  96.084  1.00 23.69 ? 91  GLU A CD  1 
ATOM   783  O OE1 . GLU A 1 91  ? 9.072   17.735  96.965  1.00 18.18 ? 91  GLU A OE1 1 
ATOM   784  O OE2 . GLU A 1 91  ? 10.172  16.599  95.412  1.00 24.23 ? 91  GLU A OE2 1 
ATOM   785  N N   . VAL A 1 92  ? 9.521   23.285  95.692  1.00 15.44 ? 92  VAL A N   1 
ATOM   786  C CA  . VAL A 1 92  ? 8.822   24.495  95.254  1.00 18.67 ? 92  VAL A CA  1 
ATOM   787  C C   . VAL A 1 92  ? 9.806   25.482  94.635  1.00 18.78 ? 92  VAL A C   1 
ATOM   788  O O   . VAL A 1 92  ? 9.540   26.059  93.572  1.00 17.68 ? 92  VAL A O   1 
ATOM   789  C CB  . VAL A 1 92  ? 8.054   25.133  96.423  1.00 16.78 ? 92  VAL A CB  1 
ATOM   790  C CG1 . VAL A 1 92  ? 7.349   26.399  95.963  1.00 20.68 ? 92  VAL A CG1 1 
ATOM   791  C CG2 . VAL A 1 92  ? 7.052   24.144  96.983  1.00 19.13 ? 92  VAL A CG2 1 
ATOM   792  N N   . GLU A 1 93  ? 10.958  25.682  95.289  1.00 19.71 ? 93  GLU A N   1 
ATOM   793  C CA  . GLU A 1 93  ? 11.978  26.584  94.756  1.00 18.19 ? 93  GLU A CA  1 
ATOM   794  C C   . GLU A 1 93  ? 12.425  26.156  93.368  1.00 19.51 ? 93  GLU A C   1 
ATOM   795  O O   . GLU A 1 93  ? 12.575  26.997  92.463  1.00 19.25 ? 93  GLU A O   1 
ATOM   796  C CB  . GLU A 1 93  ? 13.184  26.630  95.694  1.00 19.64 ? 93  GLU A CB  1 
ATOM   797  C CG  . GLU A 1 93  ? 12.899  27.382  96.992  1.00 26.99 ? 93  GLU A CG  1 
ATOM   798  C CD  . GLU A 1 93  ? 13.896  27.072  98.101  1.00 42.06 ? 93  GLU A CD  1 
ATOM   799  O OE1 . GLU A 1 93  ? 13.564  27.353  99.268  1.00 51.42 ? 93  GLU A OE1 1 
ATOM   800  O OE2 . GLU A 1 93  ? 14.999  26.555  97.821  1.00 45.83 ? 93  GLU A OE2 1 
ATOM   801  N N   . LYS A 1 94  ? 12.667  24.852  93.179  1.00 17.47 ? 94  LYS A N   1 
ATOM   802  C CA  . LYS A 1 94  ? 13.121  24.380  91.869  1.00 19.46 ? 94  LYS A CA  1 
ATOM   803  C C   . LYS A 1 94  ? 12.030  24.504  90.800  1.00 18.41 ? 94  LYS A C   1 
ATOM   804  O O   . LYS A 1 94  ? 12.329  24.829  89.645  1.00 19.34 ? 94  LYS A O   1 
ATOM   805  C CB  . LYS A 1 94  ? 13.624  22.945  91.976  1.00 25.60 ? 94  LYS A CB  1 
ATOM   806  C CG  . LYS A 1 94  ? 14.929  22.872  92.765  1.00 38.39 ? 94  LYS A CG  1 
ATOM   807  C CD  . LYS A 1 94  ? 15.535  21.479  92.774  1.00 48.34 ? 94  LYS A CD  1 
ATOM   808  C CE  . LYS A 1 94  ? 16.803  21.457  93.625  1.00 55.10 ? 94  LYS A CE  1 
ATOM   809  N NZ  . LYS A 1 94  ? 17.593  22.716  93.503  1.00 59.05 ? 94  LYS A NZ  1 
ATOM   810  N N   . LEU A 1 95  ? 10.763  24.277  91.163  1.00 14.33 ? 95  LEU A N   1 
ATOM   811  C CA  . LEU A 1 95  ? 9.671   24.493  90.219  1.00 14.74 ? 95  LEU A CA  1 
ATOM   812  C C   . LEU A 1 95  ? 9.609   25.950  89.780  1.00 16.16 ? 95  LEU A C   1 
ATOM   813  O O   . LEU A 1 95  ? 9.421   26.236  88.596  1.00 15.85 ? 95  LEU A O   1 
ATOM   814  C CB  . LEU A 1 95  ? 8.347   24.063  90.851  1.00 18.14 ? 95  LEU A CB  1 
ATOM   815  C CG  . LEU A 1 95  ? 7.094   24.184  90.014  1.00 25.62 ? 95  LEU A CG  1 
ATOM   816  C CD1 . LEU A 1 95  ? 7.207   23.357  88.734  1.00 27.49 ? 95  LEU A CD1 1 
ATOM   817  C CD2 . LEU A 1 95  ? 5.881   23.751  90.834  1.00 30.74 ? 95  LEU A CD2 1 
ATOM   818  N N   . ILE A 1 96  ? 9.744   26.880  90.727  1.00 17.80 ? 96  ILE A N   1 
ATOM   819  C CA  . ILE A 1 96  ? 9.715   28.302  90.379  1.00 17.08 ? 96  ILE A CA  1 
ATOM   820  C C   . ILE A 1 96  ? 10.928  28.673  89.526  1.00 15.41 ? 96  ILE A C   1 
ATOM   821  O O   . ILE A 1 96  ? 10.805  29.392  88.521  1.00 17.35 ? 96  ILE A O   1 
ATOM   822  C CB  . ILE A 1 96  ? 9.633   29.157  91.658  1.00 21.17 ? 96  ILE A CB  1 
ATOM   823  C CG1 . ILE A 1 96  ? 8.238   29.040  92.286  1.00 22.29 ? 96  ILE A CG1 1 
ATOM   824  C CG2 . ILE A 1 96  ? 9.982   30.611  91.358  1.00 19.97 ? 96  ILE A CG2 1 
ATOM   825  C CD1 . ILE A 1 96  ? 8.169   29.558  93.711  1.00 26.37 ? 96  ILE A CD1 1 
ATOM   826  N N   . GLU A 1 97  ? 12.111  28.179  89.896  1.00 16.31 ? 97  GLU A N   1 
ATOM   827  C CA  . GLU A 1 97  ? 13.311  28.480  89.109  1.00 18.03 ? 97  GLU A CA  1 
ATOM   828  C C   . GLU A 1 97  ? 13.196  27.920  87.696  1.00 18.25 ? 97  GLU A C   1 
ATOM   829  O O   . GLU A 1 97  ? 13.566  28.584  86.719  1.00 19.70 ? 97  GLU A O   1 
ATOM   830  C CB  . GLU A 1 97  ? 14.542  27.919  89.825  1.00 24.06 ? 97  GLU A CB  1 
ATOM   831  C CG  . GLU A 1 97  ? 15.875  28.146  89.131  1.00 31.46 ? 97  GLU A CG  1 
ATOM   832  C CD  . GLU A 1 97  ? 17.018  27.450  89.866  1.00 49.04 ? 97  GLU A CD  1 
ATOM   833  O OE1 . GLU A 1 97  ? 18.125  27.342  89.299  1.00 55.30 ? 97  GLU A OE1 1 
ATOM   834  O OE2 . GLU A 1 97  ? 16.805  27.011  91.017  1.00 54.01 ? 97  GLU A OE2 1 
ATOM   835  N N   . PHE A 1 98  ? 12.666  26.703  87.563  1.00 15.59 ? 98  PHE A N   1 
ATOM   836  C CA  . PHE A 1 98  ? 12.451  26.126  86.242  1.00 17.41 ? 98  PHE A CA  1 
ATOM   837  C C   . PHE A 1 98  ? 11.465  26.956  85.420  1.00 15.95 ? 98  PHE A C   1 
ATOM   838  O O   . PHE A 1 98  ? 11.650  27.152  84.208  1.00 16.43 ? 98  PHE A O   1 
ATOM   839  C CB  . PHE A 1 98  ? 11.951  24.691  86.408  1.00 14.93 ? 98  PHE A CB  1 
ATOM   840  C CG  . PHE A 1 98  ? 11.920  23.896  85.130  1.00 15.17 ? 98  PHE A CG  1 
ATOM   841  C CD1 . PHE A 1 98  ? 13.086  23.344  84.619  1.00 17.00 ? 98  PHE A CD1 1 
ATOM   842  C CD2 . PHE A 1 98  ? 10.717  23.688  84.455  1.00 16.99 ? 98  PHE A CD2 1 
ATOM   843  C CE1 . PHE A 1 98  ? 13.047  22.607  83.451  1.00 18.94 ? 98  PHE A CE1 1 
ATOM   844  C CE2 . PHE A 1 98  ? 10.671  22.938  83.279  1.00 14.68 ? 98  PHE A CE2 1 
ATOM   845  C CZ  . PHE A 1 98  ? 11.847  22.414  82.785  1.00 16.87 ? 98  PHE A CZ  1 
ATOM   846  N N   . THR A 1 99  ? 10.395  27.442  86.060  1.00 14.16 ? 99  THR A N   1 
ATOM   847  C CA  . THR A 1 99  ? 9.443   28.283  85.343  1.00 15.81 ? 99  THR A CA  1 
ATOM   848  C C   . THR A 1 99  ? 10.098  29.586  84.895  1.00 15.49 ? 99  THR A C   1 
ATOM   849  O O   . THR A 1 99  ? 9.940   30.011  83.747  1.00 16.48 ? 99  THR A O   1 
ATOM   850  C CB  . THR A 1 99  ? 8.231   28.560  86.240  1.00 20.36 ? 99  THR A CB  1 
ATOM   851  O OG1 . THR A 1 99  ? 7.705   27.324  86.736  1.00 15.86 ? 99  THR A OG1 1 
ATOM   852  C CG2 . THR A 1 99  ? 7.157   29.261  85.456  1.00 16.44 ? 99  THR A CG2 1 
ATOM   853  N N   . LYS A 1 100 ? 10.856  30.232  85.797  1.00 17.27 ? 100 LYS A N   1 
ATOM   854  C CA  . LYS A 1 100 ? 11.531  31.477  85.427  1.00 22.77 ? 100 LYS A CA  1 
ATOM   855  C C   . LYS A 1 100 ? 12.521  31.278  84.285  1.00 18.33 ? 100 LYS A C   1 
ATOM   856  O O   . LYS A 1 100 ? 12.690  32.176  83.447  1.00 21.68 ? 100 LYS A O   1 
ATOM   857  C CB  . LYS A 1 100 ? 12.255  32.062  86.639  1.00 20.48 ? 100 LYS A CB  1 
ATOM   858  C CG  . LYS A 1 100 ? 11.446  33.064  87.418  1.00 33.71 ? 100 LYS A CG  1 
ATOM   859  C CD  . LYS A 1 100 ? 11.940  33.203  88.840  1.00 38.22 ? 100 LYS A CD  1 
ATOM   860  C CE  . LYS A 1 100 ? 11.038  34.137  89.643  1.00 46.31 ? 100 LYS A CE  1 
ATOM   861  N NZ  . LYS A 1 100 ? 11.543  34.346  91.027  1.00 50.07 ? 100 LYS A NZ  1 
ATOM   862  N N   . LEU A 1 101 ? 13.180  30.121  84.233  1.00 17.73 ? 101 LEU A N   1 
ATOM   863  C CA  . LEU A 1 101 ? 14.141  29.835  83.164  1.00 18.81 ? 101 LEU A CA  1 
ATOM   864  C C   . LEU A 1 101 ? 13.479  29.779  81.789  1.00 16.23 ? 101 LEU A C   1 
ATOM   865  O O   . LEU A 1 101 ? 14.103  30.123  80.777  1.00 19.27 ? 101 LEU A O   1 
ATOM   866  C CB  . LEU A 1 101 ? 14.835  28.505  83.461  1.00 18.46 ? 101 LEU A CB  1 
ATOM   867  C CG  . LEU A 1 101 ? 15.905  28.018  82.477  1.00 23.87 ? 101 LEU A CG  1 
ATOM   868  C CD1 . LEU A 1 101 ? 17.089  28.952  82.450  1.00 22.94 ? 101 LEU A CD1 1 
ATOM   869  C CD2 . LEU A 1 101 ? 16.346  26.610  82.854  1.00 26.86 ? 101 LEU A CD2 1 
ATOM   870  N N   . ASN A 1 102 ? 12.207  29.389  81.743  1.00 15.66 ? 102 ASN A N   1 
ATOM   871  C CA  . ASN A 1 102 ? 11.492  29.065  80.515  1.00 15.42 ? 102 ASN A CA  1 
ATOM   872  C C   . ASN A 1 102 ? 10.374  30.042  80.184  1.00 16.19 ? 102 ASN A C   1 
ATOM   873  O O   . ASN A 1 102 ? 9.807   29.968  79.078  1.00 16.54 ? 102 ASN A O   1 
ATOM   874  C CB  . ASN A 1 102 ? 10.906  27.657  80.645  1.00 15.77 ? 102 ASN A CB  1 
ATOM   875  C CG  . ASN A 1 102 ? 11.959  26.591  80.596  1.00 17.74 ? 102 ASN A CG  1 
ATOM   876  O OD1 . ASN A 1 102 ? 12.739  26.530  79.666  1.00 21.15 ? 102 ASN A OD1 1 
ATOM   877  N ND2 . ASN A 1 102 ? 11.997  25.745  81.615  1.00 19.62 ? 102 ASN A ND2 1 
ATOM   878  N N   . TYR A 1 103 ? 10.135  31.000  81.074  1.00 18.44 ? 103 TYR A N   1 
ATOM   879  C CA  . TYR A 1 103 ? 8.965   31.878  81.116  1.00 27.61 ? 103 TYR A CA  1 
ATOM   880  C C   . TYR A 1 103 ? 8.778   32.713  79.848  1.00 21.32 ? 103 TYR A C   1 
ATOM   881  O O   . TYR A 1 103 ? 7.634   33.027  79.475  1.00 20.49 ? 103 TYR A O   1 
ATOM   882  C CB  . TYR A 1 103 ? 9.134   32.779  82.355  1.00 29.89 ? 103 TYR A CB  1 
ATOM   883  C CG  . TYR A 1 103 ? 8.127   33.868  82.560  1.00 35.06 ? 103 TYR A CG  1 
ATOM   884  C CD1 . TYR A 1 103 ? 6.983   33.637  83.307  1.00 39.97 ? 103 TYR A CD1 1 
ATOM   885  C CD2 . TYR A 1 103 ? 8.340   35.146  82.051  1.00 40.82 ? 103 TYR A CD2 1 
ATOM   886  C CE1 . TYR A 1 103 ? 6.059   34.635  83.522  1.00 43.59 ? 103 TYR A CE1 1 
ATOM   887  C CE2 . TYR A 1 103 ? 7.418   36.154  82.251  1.00 44.40 ? 103 TYR A CE2 1 
ATOM   888  C CZ  . TYR A 1 103 ? 6.275   35.890  82.991  1.00 48.78 ? 103 TYR A CZ  1 
ATOM   889  O OH  . TYR A 1 103 ? 5.346   36.880  83.209  1.00 49.82 ? 103 TYR A OH  1 
ATOM   890  N N   . GLU A 1 104 ? 9.862   33.088  79.184  1.00 18.44 ? 104 GLU A N   1 
ATOM   891  C CA  . GLU A 1 104 ? 9.753   33.948  78.008  1.00 21.86 ? 104 GLU A CA  1 
ATOM   892  C C   . GLU A 1 104 ? 9.654   33.170  76.706  1.00 19.27 ? 104 GLU A C   1 
ATOM   893  O O   . GLU A 1 104 ? 9.504   33.779  75.648  1.00 23.07 ? 104 GLU A O   1 
ATOM   894  C CB  . GLU A 1 104 ? 10.945  34.901  77.926  1.00 27.69 ? 104 GLU A CB  1 
ATOM   895  C CG  . GLU A 1 104 ? 10.986  35.942  79.045  1.00 36.80 ? 104 GLU A CG  1 
ATOM   896  C CD  . GLU A 1 104 ? 9.797   36.912  79.003  1.00 45.09 ? 104 GLU A CD  1 
ATOM   897  O OE1 . GLU A 1 104 ? 9.228   37.132  77.911  1.00 45.00 ? 104 GLU A OE1 1 
ATOM   898  O OE2 . GLU A 1 104 ? 9.434   37.460  80.065  1.00 45.48 ? 104 GLU A OE2 1 
ATOM   899  N N   . LYS A 1 105 ? 9.755   31.863  76.756  1.00 16.35 ? 105 LYS A N   1 
ATOM   900  C CA  . LYS A 1 105 ? 9.642   31.068  75.545  1.00 15.26 ? 105 LYS A CA  1 
ATOM   901  C C   . LYS A 1 105 ? 8.174   30.982  75.119  1.00 14.99 ? 105 LYS A C   1 
ATOM   902  O O   . LYS A 1 105 ? 7.288   30.925  75.975  1.00 14.92 ? 105 LYS A O   1 
ATOM   903  C CB  . LYS A 1 105 ? 10.202  29.673  75.804  1.00 13.82 ? 105 LYS A CB  1 
ATOM   904  C CG  . LYS A 1 105 ? 11.725  29.677  76.137  1.00 14.25 ? 105 LYS A CG  1 
ATOM   905  C CD  . LYS A 1 105 ? 12.218  28.302  76.600  1.00 16.40 ? 105 LYS A CD  1 
ATOM   906  C CE  . LYS A 1 105 ? 13.717  28.343  77.055  1.00 15.06 ? 105 LYS A CE  1 
ATOM   907  N NZ  . LYS A 1 105 ? 14.085  27.009  77.604  1.00 17.31 ? 105 LYS A NZ  1 
ATOM   908  N N   . PRO A 1 106 ? 7.868   30.999  73.814  1.00 15.04 ? 106 PRO A N   1 
ATOM   909  C CA  . PRO A 1 106 ? 6.441   30.987  73.423  1.00 16.34 ? 106 PRO A CA  1 
ATOM   910  C C   . PRO A 1 106 ? 5.673   29.743  73.858  1.00 14.49 ? 106 PRO A C   1 
ATOM   911  O O   . PRO A 1 106 ? 4.437   29.804  74.020  1.00 16.46 ? 106 PRO A O   1 
ATOM   912  C CB  . PRO A 1 106 ? 6.488   31.119  71.885  1.00 18.89 ? 106 PRO A CB  1 
ATOM   913  C CG  . PRO A 1 106 ? 7.782   31.844  71.609  1.00 18.14 ? 106 PRO A CG  1 
ATOM   914  C CD  . PRO A 1 106 ? 8.754   31.298  72.670  1.00 15.52 ? 106 PRO A CD  1 
ATOM   915  N N   . ILE A 1 107 ? 6.336   28.607  74.055  1.00 12.60 ? 107 ILE A N   1 
ATOM   916  C CA  . ILE A 1 107 ? 5.607   27.448  74.552  1.00 14.14 ? 107 ILE A CA  1 
ATOM   917  C C   . ILE A 1 107 ? 5.120   27.639  75.984  1.00 14.88 ? 107 ILE A C   1 
ATOM   918  O O   . ILE A 1 107 ? 4.245   26.894  76.436  1.00 14.73 ? 107 ILE A O   1 
ATOM   919  C CB  . ILE A 1 107 ? 6.436   26.148  74.442  1.00 13.68 ? 107 ILE A CB  1 
ATOM   920  C CG1 . ILE A 1 107 ? 7.744   26.220  75.238  1.00 12.83 ? 107 ILE A CG1 1 
ATOM   921  C CG2 . ILE A 1 107 ? 6.768   25.829  72.962  1.00 15.05 ? 107 ILE A CG2 1 
ATOM   922  C CD1 . ILE A 1 107 ? 8.434   24.852  75.411  1.00 12.02 ? 107 ILE A CD1 1 
ATOM   923  N N   . TYR A 1 108 ? 5.632   28.648  76.697  1.00 15.29 ? 108 TYR A N   1 
ATOM   924  C CA  . TYR A 1 108 ? 5.152   28.981  78.041  1.00 15.29 ? 108 TYR A CA  1 
ATOM   925  C C   . TYR A 1 108 ? 4.120   30.099  78.038  1.00 19.17 ? 108 TYR A C   1 
ATOM   926  O O   . TYR A 1 108 ? 3.805   30.630  79.105  1.00 19.22 ? 108 TYR A O   1 
ATOM   927  C CB  . TYR A 1 108 ? 6.321   29.373  78.973  1.00 13.60 ? 108 TYR A CB  1 
ATOM   928  C CG  . TYR A 1 108 ? 6.891   28.155  79.675  1.00 15.40 ? 108 TYR A CG  1 
ATOM   929  C CD1 . TYR A 1 108 ? 7.653   27.220  78.977  1.00 14.05 ? 108 TYR A CD1 1 
ATOM   930  C CD2 . TYR A 1 108 ? 6.634   27.917  81.018  1.00 17.27 ? 108 TYR A CD2 1 
ATOM   931  C CE1 . TYR A 1 108 ? 8.143   26.064  79.614  1.00 11.12 ? 108 TYR A CE1 1 
ATOM   932  C CE2 . TYR A 1 108 ? 7.116   26.775  81.652  1.00 16.70 ? 108 TYR A CE2 1 
ATOM   933  C CZ  . TYR A 1 108 ? 7.881   25.863  80.949  1.00 13.96 ? 108 TYR A CZ  1 
ATOM   934  O OH  . TYR A 1 108 ? 8.326   24.740  81.618  1.00 15.28 ? 108 TYR A OH  1 
ATOM   935  N N   . ARG A 1 109 ? 3.575   30.466  76.871  1.00 18.77 ? 109 ARG A N   1 
ATOM   936  C CA  . ARG A 1 109 ? 2.667   31.613  76.777  1.00 18.90 ? 109 ARG A CA  1 
ATOM   937  C C   . ARG A 1 109 ? 1.293   31.227  77.324  1.00 26.72 ? 109 ARG A C   1 
ATOM   938  O O   . ARG A 1 109 ? 0.344   30.959  76.583  1.00 26.12 ? 109 ARG A O   1 
ATOM   939  C CB  . ARG A 1 109 ? 2.546   32.116  75.339  1.00 18.24 ? 109 ARG A CB  1 
ATOM   940  C CG  . ARG A 1 109 ? 2.087   33.576  75.284  1.00 35.81 ? 109 ARG A CG  1 
ATOM   941  C CD  . ARG A 1 109 ? 1.744   34.070  73.876  1.00 49.51 ? 109 ARG A CD  1 
ATOM   942  N NE  . ARG A 1 109 ? 2.798   33.895  72.864  1.00 55.93 ? 109 ARG A NE  1 
ATOM   943  C CZ  . ARG A 1 109 ? 4.045   34.359  72.950  1.00 56.86 ? 109 ARG A CZ  1 
ATOM   944  N NH1 . ARG A 1 109 ? 4.458   35.029  74.019  1.00 62.93 ? 109 ARG A NH1 1 
ATOM   945  N NH2 . ARG A 1 109 ? 4.890   34.149  71.952  1.00 52.36 ? 109 ARG A NH2 1 
ATOM   946  N N   . PHE A 1 110 ? 1.184   31.213  78.650  1.00 20.06 ? 110 PHE A N   1 
ATOM   947  C CA  . PHE A 1 110 ? -0.082  30.997  79.339  1.00 17.07 ? 110 PHE A CA  1 
ATOM   948  C C   . PHE A 1 110 ? -0.281  32.157  80.293  1.00 21.86 ? 110 PHE A C   1 
ATOM   949  O O   . PHE A 1 110 ? 0.613   32.454  81.092  1.00 25.74 ? 110 PHE A O   1 
ATOM   950  C CB  . PHE A 1 110 ? -0.090  29.700  80.154  1.00 19.89 ? 110 PHE A CB  1 
ATOM   951  C CG  . PHE A 1 110 ? 0.039   28.460  79.345  1.00 23.21 ? 110 PHE A CG  1 
ATOM   952  C CD1 . PHE A 1 110 ? -1.080  27.854  78.787  1.00 23.82 ? 110 PHE A CD1 1 
ATOM   953  C CD2 . PHE A 1 110 ? 1.275   27.863  79.177  1.00 20.77 ? 110 PHE A CD2 1 
ATOM   954  C CE1 . PHE A 1 110 ? -0.947  26.678  78.057  1.00 20.80 ? 110 PHE A CE1 1 
ATOM   955  C CE2 . PHE A 1 110 ? 1.410   26.689  78.454  1.00 18.64 ? 110 PHE A CE2 1 
ATOM   956  C CZ  . PHE A 1 110 ? 0.298   26.102  77.886  1.00 20.43 ? 110 PHE A CZ  1 
ATOM   957  N N   . GLU A 1 111 ? -1.440  32.817  80.204  1.00 22.14 ? 111 GLU A N   1 
ATOM   958  C CA  . GLU A 1 111 ? -1.706  33.937  81.095  1.00 25.42 ? 111 GLU A CA  1 
ATOM   959  C C   . GLU A 1 111 ? -1.608  33.518  82.556  1.00 25.26 ? 111 GLU A C   1 
ATOM   960  O O   . GLU A 1 111 ? -1.136  34.297  83.394  1.00 23.78 ? 111 GLU A O   1 
ATOM   961  C CB  . GLU A 1 111 ? -3.085  34.524  80.794  1.00 35.26 ? 111 GLU A CB  1 
ATOM   962  C CG  . GLU A 1 111 ? -3.542  35.598  81.776  1.00 50.33 ? 111 GLU A CG  1 
ATOM   963  C CD  . GLU A 1 111 ? -4.861  36.232  81.368  1.00 70.17 ? 111 GLU A CD  1 
ATOM   964  O OE1 . GLU A 1 111 ? -4.959  37.480  81.381  1.00 78.64 ? 111 GLU A OE1 1 
ATOM   965  O OE2 . GLU A 1 111 ? -5.802  35.482  81.028  1.00 75.11 ? 111 GLU A OE2 1 
ATOM   966  N N   . ARG A 1 112 ? -1.998  32.281  82.871  1.00 24.73 ? 112 ARG A N   1 
ATOM   967  C CA  . ARG A 1 112 ? -1.978  31.828  84.260  1.00 24.58 ? 112 ARG A CA  1 
ATOM   968  C C   . ARG A 1 112 ? -0.554  31.774  84.805  1.00 25.62 ? 112 ARG A C   1 
ATOM   969  O O   . ARG A 1 112 ? -0.321  32.114  85.971  1.00 26.47 ? 112 ARG A O   1 
ATOM   970  C CB  . ARG A 1 112 ? -2.655  30.464  84.365  1.00 20.30 ? 112 ARG A CB  1 
ATOM   971  C CG  . ARG A 1 112 ? -2.695  29.863  85.765  1.00 20.09 ? 112 ARG A CG  1 
ATOM   972  C CD  . ARG A 1 112 ? -3.431  30.740  86.764  1.00 21.26 ? 112 ARG A CD  1 
ATOM   973  N NE  . ARG A 1 112 ? -3.794  29.947  87.937  1.00 26.14 ? 112 ARG A NE  1 
ATOM   974  C CZ  . ARG A 1 112 ? -4.197  30.446  89.102  1.00 31.69 ? 112 ARG A CZ  1 
ATOM   975  N NH1 . ARG A 1 112 ? -4.306  31.759  89.279  1.00 28.99 ? 112 ARG A NH1 1 
ATOM   976  N NH2 . ARG A 1 112 ? -4.494  29.621  90.094  1.00 30.59 ? 112 ARG A NH2 1 
ATOM   977  N N   . ILE A 1 113 ? 0.414   31.381  83.968  1.00 20.41 ? 113 ILE A N   1 
ATOM   978  C CA  . ILE A 1 113 ? 1.812   31.413  84.395  1.00 18.16 ? 113 ILE A CA  1 
ATOM   979  C C   . ILE A 1 113 ? 2.214   32.822  84.806  1.00 25.42 ? 113 ILE A C   1 
ATOM   980  O O   . ILE A 1 113 ? 2.899   33.018  85.817  1.00 27.49 ? 113 ILE A O   1 
ATOM   981  C CB  . ILE A 1 113 ? 2.732   30.872  83.282  1.00 18.38 ? 113 ILE A CB  1 
ATOM   982  C CG1 . ILE A 1 113 ? 2.630   29.343  83.224  1.00 22.35 ? 113 ILE A CG1 1 
ATOM   983  C CG2 . ILE A 1 113 ? 4.182   31.338  83.526  1.00 25.43 ? 113 ILE A CG2 1 
ATOM   984  C CD1 . ILE A 1 113 ? 3.214   28.770  81.990  1.00 30.16 ? 113 ILE A CD1 1 
ATOM   985  N N   . ARG A 1 114 ? 1.799   33.827  84.027  1.00 23.20 ? 114 ARG A N   1 
ATOM   986  C CA  . ARG A 1 114 ? 2.103   35.215  84.371  1.00 29.67 ? 114 ARG A CA  1 
ATOM   987  C C   . ARG A 1 114 ? 1.533   35.580  85.739  1.00 29.68 ? 114 ARG A C   1 
ATOM   988  O O   . ARG A 1 114 ? 2.231   36.148  86.589  1.00 31.60 ? 114 ARG A O   1 
ATOM   989  C CB  . ARG A 1 114 ? 1.554   36.141  83.283  1.00 33.94 ? 114 ARG A CB  1 
ATOM   990  C CG  . ARG A 1 114 ? 1.718   37.636  83.541  1.00 44.91 ? 114 ARG A CG  1 
ATOM   991  C CD  . ARG A 1 114 ? 3.135   37.985  83.949  1.00 58.73 ? 114 ARG A CD  1 
ATOM   992  N NE  . ARG A 1 114 ? 3.695   39.076  83.150  1.00 66.42 ? 114 ARG A NE  1 
ATOM   993  C CZ  . ARG A 1 114 ? 3.379   40.358  83.308  1.00 69.94 ? 114 ARG A CZ  1 
ATOM   994  N NH1 . ARG A 1 114 ? 2.504   40.717  84.236  1.00 71.00 ? 114 ARG A NH1 1 
ATOM   995  N NH2 . ARG A 1 114 ? 3.938   41.283  82.539  1.00 71.67 ? 114 ARG A NH2 1 
ATOM   996  N N   . GLU A 1 115 ? 0.263   35.251  85.970  1.00 28.02 ? 115 GLU A N   1 
ATOM   997  C CA  . GLU A 1 115 ? -0.349  35.517  87.268  1.00 29.31 ? 115 GLU A CA  1 
ATOM   998  C C   . GLU A 1 115 ? 0.406   34.830  88.398  1.00 27.48 ? 115 GLU A C   1 
ATOM   999  O O   . GLU A 1 115 ? 0.665   35.442  89.442  1.00 33.47 ? 115 GLU A O   1 
ATOM   1000 C CB  . GLU A 1 115 ? -1.807  35.062  87.260  1.00 32.33 ? 115 GLU A CB  1 
ATOM   1001 C CG  . GLU A 1 115 ? -2.602  35.550  86.074  1.00 40.30 ? 115 GLU A CG  1 
ATOM   1002 C CD  . GLU A 1 115 ? -4.031  35.033  86.073  1.00 49.28 ? 115 GLU A CD  1 
ATOM   1003 O OE1 . GLU A 1 115 ? -4.385  34.217  86.960  1.00 46.55 ? 115 GLU A OE1 1 
ATOM   1004 O OE2 . GLU A 1 115 ? -4.802  35.450  85.179  1.00 52.68 ? 115 GLU A OE2 1 
ATOM   1005 N N   . LEU A 1 116 ? 0.769   33.556  88.211  1.00 24.01 ? 116 LEU A N   1 
ATOM   1006 C CA  . LEU A 1 116 ? 1.414   32.805  89.286  1.00 24.48 ? 116 LEU A CA  1 
ATOM   1007 C C   . LEU A 1 116 ? 2.782   33.380  89.621  1.00 28.47 ? 116 LEU A C   1 
ATOM   1008 O O   . LEU A 1 116 ? 3.141   33.485  90.797  1.00 34.81 ? 116 LEU A O   1 
ATOM   1009 C CB  . LEU A 1 116 ? 1.539   31.326  88.902  1.00 26.48 ? 116 LEU A CB  1 
ATOM   1010 C CG  . LEU A 1 116 ? 0.230   30.551  88.698  1.00 27.54 ? 116 LEU A CG  1 
ATOM   1011 C CD1 . LEU A 1 116 ? 0.483   29.130  88.154  1.00 25.25 ? 116 LEU A CD1 1 
ATOM   1012 C CD2 . LEU A 1 116 ? -0.549  30.489  89.983  1.00 27.41 ? 116 LEU A CD2 1 
ATOM   1013 N N   . MET A 1 117 ? 3.556   33.775  88.607  1.00 27.79 ? 117 MET A N   1 
ATOM   1014 C CA  . MET A 1 117 ? 4.877   34.334  88.885  1.00 28.80 ? 117 MET A CA  1 
ATOM   1015 C C   . MET A 1 117 ? 4.806   35.721  89.513  1.00 36.36 ? 117 MET A C   1 
ATOM   1016 O O   . MET A 1 117 ? 5.829   36.218  89.995  1.00 38.03 ? 117 MET A O   1 
ATOM   1017 C CB  . MET A 1 117 ? 5.724   34.369  87.608  1.00 35.35 ? 117 MET A CB  1 
ATOM   1018 C CG  . MET A 1 117 ? 6.027   32.995  87.028  1.00 37.38 ? 117 MET A CG  1 
ATOM   1019 S SD  . MET A 1 117 ? 6.615   31.810  88.265  1.00 41.63 ? 117 MET A SD  1 
ATOM   1020 C CE  . MET A 1 117 ? 8.361   32.091  88.168  1.00 36.91 ? 117 MET A CE  1 
ATOM   1021 N N   . ASN A 1 118 ? 3.631   36.342  89.541  1.00 37.09 ? 118 ASN A N   1 
ATOM   1022 C CA  . ASN A 1 118 ? 3.442   37.623  90.204  1.00 39.36 ? 118 ASN A CA  1 
ATOM   1023 C C   . ASN A 1 118 ? 2.934   37.470  91.630  1.00 42.94 ? 118 ASN A C   1 
ATOM   1024 O O   . ASN A 1 118 ? 2.720   38.477  92.312  1.00 47.04 ? 118 ASN A O   1 
ATOM   1025 C CB  . ASN A 1 118 ? 2.461   38.497  89.413  1.00 45.29 ? 118 ASN A CB  1 
ATOM   1026 C CG  . ASN A 1 118 ? 3.096   39.133  88.190  1.00 55.40 ? 118 ASN A CG  1 
ATOM   1027 O OD1 . ASN A 1 118 ? 4.321   39.161  88.049  1.00 56.92 ? 118 ASN A OD1 1 
ATOM   1028 N ND2 . ASN A 1 118 ? 2.258   39.652  87.294  1.00 57.20 ? 118 ASN A ND2 1 
ATOM   1029 N N   . LYS A 1 119 ? 2.733   36.246  92.097  1.00 40.84 ? 119 LYS A N   1 
ATOM   1030 C CA  . LYS A 1 119 ? 2.212   36.036  93.437  1.00 41.80 ? 119 LYS A CA  1 
ATOM   1031 C C   . LYS A 1 119 ? 3.350   35.823  94.425  1.00 45.96 ? 119 LYS A C   1 
ATOM   1032 O O   . LYS A 1 119 ? 4.397   35.260  94.093  1.00 44.75 ? 119 LYS A O   1 
ATOM   1033 C CB  . LYS A 1 119 ? 1.250   34.847  93.462  1.00 40.62 ? 119 LYS A CB  1 
ATOM   1034 C CG  . LYS A 1 119 ? -0.101  35.177  92.859  1.00 44.15 ? 119 LYS A CG  1 
ATOM   1035 C CD  . LYS A 1 119 ? -1.000  33.960  92.782  1.00 47.94 ? 119 LYS A CD  1 
ATOM   1036 C CE  . LYS A 1 119 ? -2.287  34.277  92.025  1.00 50.61 ? 119 LYS A CE  1 
ATOM   1037 N NZ  . LYS A 1 119 ? -2.985  35.460  92.597  1.00 52.93 ? 119 LYS A NZ  1 
ATOM   1038 N N   . GLU A 1 120 ? 3.132   36.288  95.654  1.00 51.15 ? 120 GLU A N   1 
ATOM   1039 C CA  . GLU A 1 120 ? 4.163   36.200  96.679  1.00 56.93 ? 120 GLU A CA  1 
ATOM   1040 C C   . GLU A 1 120 ? 4.268   34.792  97.251  1.00 53.31 ? 120 GLU A C   1 
ATOM   1041 O O   . GLU A 1 120 ? 5.374   34.298  97.485  1.00 50.63 ? 120 GLU A O   1 
ATOM   1042 C CB  . GLU A 1 120 ? 3.878   37.212  97.786  1.00 61.23 ? 120 GLU A CB  1 
ATOM   1043 C CG  . GLU A 1 120 ? 3.874   38.646  97.303  1.00 62.36 ? 120 GLU A CG  1 
ATOM   1044 C CD  . GLU A 1 120 ? 3.929   39.642  98.444  1.00 63.94 ? 120 GLU A CD  1 
ATOM   1045 O OE1 . GLU A 1 120 ? 4.799   40.532  98.400  1.00 66.26 ? 120 GLU A OE1 1 
ATOM   1046 O OE2 . GLU A 1 120 ? 3.104   39.538  99.377  1.00 63.06 ? 120 GLU A OE2 1 
ATOM   1047 N N   . LYS A 1 121 ? 3.133   34.139  97.492  1.00 54.02 ? 121 LYS A N   1 
ATOM   1048 C CA  . LYS A 1 121 ? 3.113   32.761  97.957  1.00 51.13 ? 121 LYS A CA  1 
ATOM   1049 C C   . LYS A 1 121 ? 2.009   32.012  97.227  1.00 43.57 ? 121 LYS A C   1 
ATOM   1050 O O   . LYS A 1 121 ? 0.934   32.562  96.972  1.00 44.31 ? 121 LYS A O   1 
ATOM   1051 C CB  . LYS A 1 121 ? 2.904   32.671  99.474  1.00 55.54 ? 121 LYS A CB  1 
ATOM   1052 C CG  . LYS A 1 121 ? 3.485   31.405  100.104 1.00 61.90 ? 121 LYS A CG  1 
ATOM   1053 C CD  . LYS A 1 121 ? 4.319   31.717  101.347 1.00 65.32 ? 121 LYS A CD  1 
ATOM   1054 C CE  . LYS A 1 121 ? 5.106   30.495  101.816 1.00 65.87 ? 121 LYS A CE  1 
ATOM   1055 N NZ  . LYS A 1 121 ? 4.213   29.363  102.206 1.00 66.96 ? 121 LYS A NZ  1 
ATOM   1056 N N   . LEU A 1 122 ? 2.287   30.762  96.883  1.00 33.19 ? 122 LEU A N   1 
ATOM   1057 C CA  . LEU A 1 122 ? 1.359   29.930  96.131  1.00 29.25 ? 122 LEU A CA  1 
ATOM   1058 C C   . LEU A 1 122 ? 0.661   28.962  97.079  1.00 31.31 ? 122 LEU A C   1 
ATOM   1059 O O   . LEU A 1 122 ? 1.311   28.352  97.936  1.00 31.09 ? 122 LEU A O   1 
ATOM   1060 C CB  . LEU A 1 122 ? 2.096   29.167  95.032  1.00 28.71 ? 122 LEU A CB  1 
ATOM   1061 C CG  . LEU A 1 122 ? 2.899   30.042  94.057  1.00 32.47 ? 122 LEU A CG  1 
ATOM   1062 C CD1 . LEU A 1 122 ? 3.525   29.194  92.954  1.00 35.09 ? 122 LEU A CD1 1 
ATOM   1063 C CD2 . LEU A 1 122 ? 2.006   31.129  93.470  1.00 32.85 ? 122 LEU A CD2 1 
ATOM   1064 N N   . ASN A 1 123 ? -0.663  28.856  96.946  1.00 26.69 ? 123 ASN A N   1 
ATOM   1065 C CA  . ASN A 1 123 ? -1.438  27.867  97.682  1.00 25.36 ? 123 ASN A CA  1 
ATOM   1066 C C   . ASN A 1 123 ? -1.495  26.570  96.856  1.00 23.47 ? 123 ASN A C   1 
ATOM   1067 O O   . ASN A 1 123 ? -0.843  26.440  95.814  1.00 22.10 ? 123 ASN A O   1 
ATOM   1068 C CB  . ASN A 1 123 ? -2.825  28.423  98.031  1.00 26.78 ? 123 ASN A CB  1 
ATOM   1069 C CG  . ASN A 1 123 ? -3.670  28.750  96.801  1.00 33.47 ? 123 ASN A CG  1 
ATOM   1070 O OD1 . ASN A 1 123 ? -3.531  28.133  95.746  1.00 29.11 ? 123 ASN A OD1 1 
ATOM   1071 N ND2 . ASN A 1 123 ? -4.568  29.711  96.946  1.00 38.99 ? 123 ASN A ND2 1 
ATOM   1072 N N   . ARG A 1 124 ? -2.269  25.582  97.321  1.00 26.20 ? 124 ARG A N   1 
ATOM   1073 C CA  . ARG A 1 124 ? -2.272  24.287  96.643  1.00 22.09 ? 124 ARG A CA  1 
ATOM   1074 C C   . ARG A 1 124 ? -2.852  24.399  95.235  1.00 21.39 ? 124 ARG A C   1 
ATOM   1075 O O   . ARG A 1 124 ? -2.288  23.849  94.280  1.00 22.98 ? 124 ARG A O   1 
ATOM   1076 C CB  . ARG A 1 124 ? -3.045  23.233  97.459  1.00 22.75 ? 124 ARG A CB  1 
ATOM   1077 C CG  . ARG A 1 124 ? -3.128  21.859  96.741  1.00 27.62 ? 124 ARG A CG  1 
ATOM   1078 C CD  . ARG A 1 124 ? -3.981  20.807  97.509  1.00 27.65 ? 124 ARG A CD  1 
ATOM   1079 N NE  . ARG A 1 124 ? -4.042  19.538  96.773  1.00 24.66 ? 124 ARG A NE  1 
ATOM   1080 C CZ  . ARG A 1 124 ? -4.973  19.260  95.860  1.00 27.97 ? 124 ARG A CZ  1 
ATOM   1081 N NH1 . ARG A 1 124 ? -5.920  20.154  95.588  1.00 25.73 ? 124 ARG A NH1 1 
ATOM   1082 N NH2 . ARG A 1 124 ? -4.959  18.100  95.219  1.00 26.07 ? 124 ARG A NH2 1 
ATOM   1083 N N   . GLU A 1 125 ? -3.963  25.121  95.083  1.00 23.56 ? 125 GLU A N   1 
ATOM   1084 C CA  . GLU A 1 125 ? -4.554  25.288  93.756  1.00 25.32 ? 125 GLU A CA  1 
ATOM   1085 C C   . GLU A 1 125 ? -3.559  25.931  92.793  1.00 21.25 ? 125 GLU A C   1 
ATOM   1086 O O   . GLU A 1 125 ? -3.393  25.482  91.640  1.00 20.94 ? 125 GLU A O   1 
ATOM   1087 C CB  . GLU A 1 125 ? -5.832  26.132  93.874  1.00 28.12 ? 125 GLU A CB  1 
ATOM   1088 C CG  . GLU A 1 125 ? -6.675  26.197  92.609  1.00 49.76 ? 125 GLU A CG  1 
ATOM   1089 C CD  . GLU A 1 125 ? -6.218  27.279  91.634  1.00 66.70 ? 125 GLU A CD  1 
ATOM   1090 O OE1 . GLU A 1 125 ? -6.403  27.093  90.407  1.00 68.17 ? 125 GLU A OE1 1 
ATOM   1091 O OE2 . GLU A 1 125 ? -5.677  28.311  92.092  1.00 71.97 ? 125 GLU A OE2 1 
ATOM   1092 N N   . GLU A 1 126 ? -2.862  26.962  93.263  1.00 23.84 ? 126 GLU A N   1 
ATOM   1093 C CA  . GLU A 1 126 ? -1.895  27.655  92.419  1.00 22.93 ? 126 GLU A CA  1 
ATOM   1094 C C   . GLU A 1 126 ? -0.731  26.745  92.044  1.00 25.02 ? 126 GLU A C   1 
ATOM   1095 O O   . GLU A 1 126 ? -0.301  26.719  90.880  1.00 21.38 ? 126 GLU A O   1 
ATOM   1096 C CB  . GLU A 1 126 ? -1.425  28.927  93.128  1.00 24.48 ? 126 GLU A CB  1 
ATOM   1097 C CG  . GLU A 1 126 ? -2.531  29.987  93.138  1.00 24.16 ? 126 GLU A CG  1 
ATOM   1098 C CD  . GLU A 1 126 ? -2.428  31.004  94.259  1.00 32.21 ? 126 GLU A CD  1 
ATOM   1099 O OE1 . GLU A 1 126 ? -1.613  30.827  95.204  1.00 29.68 ? 126 GLU A OE1 1 
ATOM   1100 O OE2 . GLU A 1 126 ? -3.196  31.991  94.193  1.00 38.19 ? 126 GLU A OE2 1 
ATOM   1101 N N   . LEU A 1 127 ? -0.216  25.977  93.010  1.00 19.03 ? 127 LEU A N   1 
ATOM   1102 C CA  . LEU A 1 127 ? 0.897   25.082  92.718  1.00 17.86 ? 127 LEU A CA  1 
ATOM   1103 C C   . LEU A 1 127 ? 0.490   23.982  91.750  1.00 19.73 ? 127 LEU A C   1 
ATOM   1104 O O   . LEU A 1 127 ? 1.300   23.563  90.915  1.00 18.11 ? 127 LEU A O   1 
ATOM   1105 C CB  . LEU A 1 127 ? 1.449   24.477  94.007  1.00 18.47 ? 127 LEU A CB  1 
ATOM   1106 C CG  . LEU A 1 127 ? 2.263   25.416  94.908  1.00 23.81 ? 127 LEU A CG  1 
ATOM   1107 C CD1 . LEU A 1 127 ? 2.456   24.797  96.276  1.00 23.46 ? 127 LEU A CD1 1 
ATOM   1108 C CD2 . LEU A 1 127 ? 3.608   25.712  94.233  1.00 26.37 ? 127 LEU A CD2 1 
ATOM   1109 N N   . LEU A 1 128 ? -0.746  23.475  91.863  1.00 16.86 ? 128 LEU A N   1 
ATOM   1110 C CA  . LEU A 1 128 ? -1.226  22.510  90.877  1.00 15.95 ? 128 LEU A CA  1 
ATOM   1111 C C   . LEU A 1 128 ? -1.220  23.113  89.481  1.00 16.26 ? 128 LEU A C   1 
ATOM   1112 O O   . LEU A 1 128 ? -0.848  22.451  88.508  1.00 18.07 ? 128 LEU A O   1 
ATOM   1113 C CB  . LEU A 1 128 ? -2.642  22.049  91.230  1.00 20.51 ? 128 LEU A CB  1 
ATOM   1114 C CG  . LEU A 1 128 ? -2.816  20.719  91.945  1.00 20.46 ? 128 LEU A CG  1 
ATOM   1115 C CD1 . LEU A 1 128 ? -4.293  20.562  92.321  1.00 23.06 ? 128 LEU A CD1 1 
ATOM   1116 C CD2 . LEU A 1 128 ? -2.355  19.557  91.115  1.00 21.15 ? 128 LEU A CD2 1 
ATOM   1117 N N   . ASP A 1 129 ? -1.625  24.376  89.368  1.00 17.37 ? 129 ASP A N   1 
ATOM   1118 C CA  . ASP A 1 129 ? -1.574  25.039  88.074  1.00 18.83 ? 129 ASP A CA  1 
ATOM   1119 C C   . ASP A 1 129 ? -0.141  25.200  87.612  1.00 18.61 ? 129 ASP A C   1 
ATOM   1120 O O   . ASP A 1 129 ? 0.157   24.996  86.433  1.00 16.55 ? 129 ASP A O   1 
ATOM   1121 C CB  . ASP A 1 129 ? -2.266  26.401  88.134  1.00 18.66 ? 129 ASP A CB  1 
ATOM   1122 C CG  . ASP A 1 129 ? -3.781  26.283  88.078  1.00 23.20 ? 129 ASP A CG  1 
ATOM   1123 O OD1 . ASP A 1 129 ? -4.272  25.137  88.027  1.00 22.48 ? 129 ASP A OD1 1 
ATOM   1124 O OD2 . ASP A 1 129 ? -4.468  27.328  88.107  1.00 27.49 ? 129 ASP A OD2 1 
ATOM   1125 N N   . LEU A 1 130 ? 0.775   25.522  88.529  1.00 16.08 ? 130 LEU A N   1 
ATOM   1126 C CA  . LEU A 1 130 ? 2.159   25.678  88.104  1.00 14.63 ? 130 LEU A CA  1 
ATOM   1127 C C   . LEU A 1 130 ? 2.737   24.349  87.619  1.00 14.85 ? 130 LEU A C   1 
ATOM   1128 O O   . LEU A 1 130 ? 3.409   24.298  86.574  1.00 15.86 ? 130 LEU A O   1 
ATOM   1129 C CB  . LEU A 1 130 ? 2.995   26.267  89.237  1.00 17.65 ? 130 LEU A CB  1 
ATOM   1130 C CG  . LEU A 1 130 ? 4.411   26.728  88.861  1.00 21.08 ? 130 LEU A CG  1 
ATOM   1131 C CD1 . LEU A 1 130 ? 4.329   27.781  87.759  1.00 25.74 ? 130 LEU A CD1 1 
ATOM   1132 C CD2 . LEU A 1 130 ? 5.121   27.294  90.093  1.00 27.44 ? 130 LEU A CD2 1 
ATOM   1133 N N   . GLN A 1 131 ? 2.508   23.264  88.368  1.00 13.44 ? 131 GLN A N   1 
ATOM   1134 C CA  . GLN A 1 131 ? 2.992   21.943  87.936  1.00 12.93 ? 131 GLN A CA  1 
ATOM   1135 C C   . GLN A 1 131 ? 2.401   21.533  86.588  1.00 14.60 ? 131 GLN A C   1 
ATOM   1136 O O   . GLN A 1 131 ? 3.116   21.065  85.686  1.00 14.87 ? 131 GLN A O   1 
ATOM   1137 C CB  . GLN A 1 131 ? 2.619   20.874  88.964  1.00 14.35 ? 131 GLN A CB  1 
ATOM   1138 C CG  . GLN A 1 131 ? 3.249   20.994  90.368  1.00 13.69 ? 131 GLN A CG  1 
ATOM   1139 C CD  . GLN A 1 131 ? 2.549   20.094  91.352  1.00 17.42 ? 131 GLN A CD  1 
ATOM   1140 O OE1 . GLN A 1 131 ? 1.303   20.015  91.375  1.00 16.61 ? 131 GLN A OE1 1 
ATOM   1141 N NE2 . GLN A 1 131 ? 3.329   19.389  92.177  1.00 18.11 ? 131 GLN A NE2 1 
ATOM   1142 N N   . THR A 1 132 ? 1.083   21.648  86.454  1.00 14.60 ? 132 THR A N   1 
ATOM   1143 C CA  . THR A 1 132 ? 0.426   21.174  85.241  1.00 13.47 ? 132 THR A CA  1 
ATOM   1144 C C   . THR A 1 132 ? 0.764   22.036  84.035  1.00 14.32 ? 132 THR A C   1 
ATOM   1145 O O   . THR A 1 132 ? 0.921   21.515  82.932  1.00 13.18 ? 132 THR A O   1 
ATOM   1146 C CB  . THR A 1 132 ? -1.076  21.113  85.452  1.00 13.49 ? 132 THR A CB  1 
ATOM   1147 O OG1 . THR A 1 132 ? -1.352  20.390  86.658  1.00 16.79 ? 132 THR A OG1 1 
ATOM   1148 C CG2 . THR A 1 132 ? -1.750  20.400  84.266  1.00 13.96 ? 132 THR A CG2 1 
ATOM   1149 N N   . LEU A 1 133 ? 0.874   23.352  84.209  1.00 14.04 ? 133 LEU A N   1 
ATOM   1150 C CA  . LEU A 1 133 ? 1.237   24.179  83.065  1.00 14.40 ? 133 LEU A CA  1 
ATOM   1151 C C   . LEU A 1 133 ? 2.683   23.967  82.658  1.00 16.97 ? 133 LEU A C   1 
ATOM   1152 O O   . LEU A 1 133 ? 3.010   24.093  81.472  1.00 15.34 ? 133 LEU A O   1 
ATOM   1153 C CB  . LEU A 1 133 ? 0.999   25.653  83.371  1.00 14.93 ? 133 LEU A CB  1 
ATOM   1154 C CG  . LEU A 1 133 ? -0.507  25.936  83.356  1.00 16.44 ? 133 LEU A CG  1 
ATOM   1155 C CD1 . LEU A 1 133 ? -0.824  27.315  83.979  1.00 19.92 ? 133 LEU A CD1 1 
ATOM   1156 C CD2 . LEU A 1 133 ? -1.043  25.817  81.931  1.00 22.10 ? 133 LEU A CD2 1 
ATOM   1157 N N   . ASN A 1 134 ? 3.568   23.665  83.612  1.00 15.68 ? 134 ASN A N   1 
ATOM   1158 C CA  . ASN A 1 134 ? 4.928   23.311  83.206  1.00 13.42 ? 134 ASN A CA  1 
ATOM   1159 C C   . ASN A 1 134 ? 4.920   22.050  82.359  1.00 21.01 ? 134 ASN A C   1 
ATOM   1160 O O   . ASN A 1 134 ? 5.647   21.963  81.362  1.00 19.86 ? 134 ASN A O   1 
ATOM   1161 C CB  . ASN A 1 134 ? 5.827   23.143  84.433  1.00 11.66 ? 134 ASN A CB  1 
ATOM   1162 C CG  . ASN A 1 134 ? 6.563   24.447  84.799  1.00 12.77 ? 134 ASN A CG  1 
ATOM   1163 O OD1 . ASN A 1 134 ? 7.597   24.792  84.202  1.00 15.71 ? 134 ASN A OD1 1 
ATOM   1164 N ND2 . ASN A 1 134 ? 6.025   25.180  85.765  1.00 14.07 ? 134 ASN A ND2 1 
ATOM   1165 N N   . LEU A 1 135 ? 4.107   21.057  82.735  1.00 15.79 ? 135 LEU A N   1 
ATOM   1166 C CA  . LEU A 1 135 ? 3.969   19.871  81.890  1.00 15.03 ? 135 LEU A CA  1 
ATOM   1167 C C   . LEU A 1 135 ? 3.408   20.233  80.525  1.00 16.38 ? 135 LEU A C   1 
ATOM   1168 O O   . LEU A 1 135 ? 3.965   19.854  79.485  1.00 15.14 ? 135 LEU A O   1 
ATOM   1169 C CB  . LEU A 1 135 ? 3.036   18.852  82.548  1.00 17.95 ? 135 LEU A CB  1 
ATOM   1170 C CG  . LEU A 1 135 ? 3.599   17.788  83.465  1.00 22.29 ? 135 LEU A CG  1 
ATOM   1171 C CD1 . LEU A 1 135 ? 2.451   16.897  83.883  1.00 19.32 ? 135 LEU A CD1 1 
ATOM   1172 C CD2 . LEU A 1 135 ? 4.719   16.981  82.789  1.00 19.12 ? 135 LEU A CD2 1 
ATOM   1173 N N   . LEU A 1 136 ? 2.266   20.931  80.511  1.00 12.03 ? 136 LEU A N   1 
ATOM   1174 C CA  . LEU A 1 136 ? 1.584   21.211  79.248  1.00 13.30 ? 136 LEU A CA  1 
ATOM   1175 C C   . LEU A 1 136 ? 2.421   22.062  78.299  1.00 13.28 ? 136 LEU A C   1 
ATOM   1176 O O   . LEU A 1 136 ? 2.231   21.983  77.079  1.00 13.10 ? 136 LEU A O   1 
ATOM   1177 C CB  . LEU A 1 136 ? 0.238   21.893  79.511  1.00 13.98 ? 136 LEU A CB  1 
ATOM   1178 C CG  . LEU A 1 136 ? -0.814  20.947  80.072  1.00 15.70 ? 136 LEU A CG  1 
ATOM   1179 C CD1 . LEU A 1 136 ? -2.059  21.747  80.490  1.00 14.90 ? 136 LEU A CD1 1 
ATOM   1180 C CD2 . LEU A 1 136 ? -1.188  19.902  79.023  1.00 18.72 ? 136 LEU A CD2 1 
ATOM   1181 N N   . ALA A 1 137 ? 3.325   22.895  78.827  1.00 12.13 ? 137 ALA A N   1 
ATOM   1182 C CA  . ALA A 1 137 ? 4.151   23.739  77.961  1.00 13.13 ? 137 ALA A CA  1 
ATOM   1183 C C   . ALA A 1 137 ? 4.982   22.902  77.003  1.00 11.39 ? 137 ALA A C   1 
ATOM   1184 O O   . ALA A 1 137 ? 5.351   23.375  75.918  1.00 14.00 ? 137 ALA A O   1 
ATOM   1185 C CB  . ALA A 1 137 ? 5.087   24.618  78.792  1.00 13.89 ? 137 ALA A CB  1 
ATOM   1186 N N   . TRP A 1 138 ? 5.318   21.678  77.397  1.00 12.70 ? 138 TRP A N   1 
ATOM   1187 C CA  . TRP A 1 138 ? 6.198   20.810  76.618  1.00 14.02 ? 138 TRP A CA  1 
ATOM   1188 C C   . TRP A 1 138 ? 5.416   19.833  75.754  1.00 12.52 ? 138 TRP A C   1 
ATOM   1189 O O   . TRP A 1 138 ? 5.993   18.884  75.224  1.00 14.44 ? 138 TRP A O   1 
ATOM   1190 C CB  . TRP A 1 138 ? 7.184   20.081  77.548  1.00 12.97 ? 138 TRP A CB  1 
ATOM   1191 C CG  . TRP A 1 138 ? 8.145   21.070  78.208  1.00 13.01 ? 138 TRP A CG  1 
ATOM   1192 C CD1 . TRP A 1 138 ? 7.916   21.824  79.331  1.00 16.71 ? 138 TRP A CD1 1 
ATOM   1193 C CD2 . TRP A 1 138 ? 9.458   21.444  77.746  1.00 13.24 ? 138 TRP A CD2 1 
ATOM   1194 N NE1 . TRP A 1 138 ? 8.990   22.620  79.596  1.00 12.55 ? 138 TRP A NE1 1 
ATOM   1195 C CE2 . TRP A 1 138 ? 9.964   22.415  78.654  1.00 14.43 ? 138 TRP A CE2 1 
ATOM   1196 C CE3 . TRP A 1 138 ? 10.253  21.048  76.666  1.00 13.02 ? 138 TRP A CE3 1 
ATOM   1197 C CZ2 . TRP A 1 138 ? 11.216  22.990  78.512  1.00 17.57 ? 138 TRP A CZ2 1 
ATOM   1198 C CZ3 . TRP A 1 138 ? 11.524  21.631  76.528  1.00 17.24 ? 138 TRP A CZ3 1 
ATOM   1199 C CH2 . TRP A 1 138 ? 11.987  22.584  77.445  1.00 21.04 ? 138 TRP A CH2 1 
ATOM   1200 N N   . CYS A 1 139 ? 4.121   20.071  75.560  1.00 10.73 ? 139 CYS A N   1 
ATOM   1201 C CA  . CYS A 1 139 ? 3.314   19.155  74.765  1.00 10.26 ? 139 CYS A CA  1 
ATOM   1202 C C   . CYS A 1 139 ? 3.790   19.134  73.309  1.00 11.85 ? 139 CYS A C   1 
ATOM   1203 O O   . CYS A 1 139 ? 4.010   20.183  72.700  1.00 13.36 ? 139 CYS A O   1 
ATOM   1204 C CB  . CYS A 1 139 ? 1.852   19.575  74.842  1.00 15.26 ? 139 CYS A CB  1 
ATOM   1205 S SG  . CYS A 1 139 ? 0.688   18.334  74.240  1.00 16.98 ? 139 CYS A SG  1 
ATOM   1206 N N   . GLY A 1 140 ? 3.966   17.926  72.753  1.00 11.66 ? 140 GLY A N   1 
ATOM   1207 C CA  . GLY A 1 140 ? 4.338   17.796  71.357  1.00 11.86 ? 140 GLY A CA  1 
ATOM   1208 C C   . GLY A 1 140 ? 3.143   17.895  70.407  1.00 10.57 ? 140 GLY A C   1 
ATOM   1209 O O   . GLY A 1 140 ? 1.969   17.934  70.800  1.00 13.46 ? 140 GLY A O   1 
ATOM   1210 N N   . ARG A 1 141 ? 3.469   17.935  69.112  1.00 10.21 ? 141 ARG A N   1 
ATOM   1211 C CA  . ARG A 1 141 ? 2.468   18.075  68.057  1.00 12.12 ? 141 ARG A CA  1 
ATOM   1212 C C   . ARG A 1 141 ? 1.359   17.037  68.162  1.00 13.30 ? 141 ARG A C   1 
ATOM   1213 O O   . ARG A 1 141 ? 0.169   17.369  68.050  1.00 15.14 ? 141 ARG A O   1 
ATOM   1214 C CB  . ARG A 1 141 ? 3.165   17.971  66.697  1.00 11.34 ? 141 ARG A CB  1 
ATOM   1215 C CG  . ARG A 1 141 ? 2.233   18.065  65.482  1.00 12.86 ? 141 ARG A CG  1 
ATOM   1216 C CD  . ARG A 1 141 ? 3.051   18.258  64.196  1.00 12.93 ? 141 ARG A CD  1 
ATOM   1217 N NE  . ARG A 1 141 ? 2.252   18.088  62.977  1.00 15.16 ? 141 ARG A NE  1 
ATOM   1218 C CZ  . ARG A 1 141 ? 2.080   16.927  62.338  1.00 17.07 ? 141 ARG A CZ  1 
ATOM   1219 N NH1 . ARG A 1 141 ? 2.643   15.801  62.776  1.00 17.34 ? 141 ARG A NH1 1 
ATOM   1220 N NH2 . ARG A 1 141 ? 1.321   16.893  61.282  1.00 17.46 ? 141 ARG A NH2 1 
ATOM   1221 N N   . THR A 1 142 ? 1.730   15.766  68.349  1.00 13.97 ? 142 THR A N   1 
ATOM   1222 C CA  . THR A 1 142 ? 0.724   14.710  68.339  1.00 14.90 ? 142 THR A CA  1 
ATOM   1223 C C   . THR A 1 142 ? -0.311  14.937  69.432  1.00 12.83 ? 142 THR A C   1 
ATOM   1224 O O   . THR A 1 142 ? -1.531  14.873  69.190  1.00 16.48 ? 142 THR A O   1 
ATOM   1225 C CB  . THR A 1 142 ? 1.400   13.348  68.531  1.00 15.18 ? 142 THR A CB  1 
ATOM   1226 O OG1 . THR A 1 142 ? 2.253   13.080  67.416  1.00 17.31 ? 142 THR A OG1 1 
ATOM   1227 C CG2 . THR A 1 142 ? 0.351   12.240  68.650  1.00 18.41 ? 142 THR A CG2 1 
ATOM   1228 N N   . LEU A 1 143 ? 0.157   15.188  70.642  1.00 15.04 ? 143 LEU A N   1 
ATOM   1229 C CA  . LEU A 1 143 ? -0.775  15.328  71.756  1.00 14.21 ? 143 LEU A CA  1 
ATOM   1230 C C   . LEU A 1 143 ? -1.419  16.704  71.828  1.00 17.98 ? 143 LEU A C   1 
ATOM   1231 O O   . LEU A 1 143 ? -2.414  16.858  72.543  1.00 16.00 ? 143 LEU A O   1 
ATOM   1232 C CB  . LEU A 1 143 ? -0.065  15.032  73.078  1.00 13.63 ? 143 LEU A CB  1 
ATOM   1233 C CG  . LEU A 1 143 ? 0.123   13.532  73.379  1.00 16.56 ? 143 LEU A CG  1 
ATOM   1234 C CD1 . LEU A 1 143 ? 0.862   13.414  74.712  1.00 12.24 ? 143 LEU A CD1 1 
ATOM   1235 C CD2 . LEU A 1 143 ? -1.196  12.767  73.378  1.00 19.58 ? 143 LEU A CD2 1 
ATOM   1236 N N   . ARG A 1 144 ? -0.881  17.707  71.129  1.00 19.09 ? 144 ARG A N   1 
ATOM   1237 C CA  . ARG A 1 144 ? -1.540  19.012  71.117  1.00 20.07 ? 144 ARG A CA  1 
ATOM   1238 C C   . ARG A 1 144 ? -2.952  18.925  70.532  1.00 26.26 ? 144 ARG A C   1 
ATOM   1239 O O   . ARG A 1 144 ? -3.819  19.735  70.884  1.00 23.26 ? 144 ARG A O   1 
ATOM   1240 C CB  . ARG A 1 144 ? -0.685  20.037  70.357  1.00 21.04 ? 144 ARG A CB  1 
ATOM   1241 C CG  . ARG A 1 144 ? 0.280   20.816  71.280  1.00 20.05 ? 144 ARG A CG  1 
ATOM   1242 C CD  . ARG A 1 144 ? 1.312   21.623  70.497  1.00 16.18 ? 144 ARG A CD  1 
ATOM   1243 N NE  . ARG A 1 144 ? 2.275   22.288  71.370  1.00 17.31 ? 144 ARG A NE  1 
ATOM   1244 C CZ  . ARG A 1 144 ? 2.157   23.561  71.752  1.00 26.75 ? 144 ARG A CZ  1 
ATOM   1245 N NH1 . ARG A 1 144 ? 1.105   24.265  71.347  1.00 24.50 ? 144 ARG A NH1 1 
ATOM   1246 N NH2 . ARG A 1 144 ? 3.071   24.119  72.545  1.00 21.39 ? 144 ARG A NH2 1 
ATOM   1247 N N   . LYS A 1 145 ? -3.220  17.926  69.681  1.00 25.85 ? 145 LYS A N   1 
ATOM   1248 C CA  . LYS A 1 145 ? -4.589  17.675  69.238  1.00 26.46 ? 145 LYS A CA  1 
ATOM   1249 C C   . LYS A 1 145 ? -5.427  17.020  70.337  1.00 30.06 ? 145 LYS A C   1 
ATOM   1250 O O   . LYS A 1 145 ? -6.549  17.454  70.620  1.00 35.08 ? 145 LYS A O   1 
ATOM   1251 C CB  . LYS A 1 145 ? -4.575  16.798  67.983  1.00 36.14 ? 145 LYS A CB  1 
ATOM   1252 C CG  . LYS A 1 145 ? -5.910  16.746  67.251  1.00 45.20 ? 145 LYS A CG  1 
ATOM   1253 C CD  . LYS A 1 145 ? -5.755  16.290  65.789  1.00 52.90 ? 145 LYS A CD  1 
ATOM   1254 C CE  . LYS A 1 145 ? -4.424  16.747  65.196  1.00 57.74 ? 145 LYS A CE  1 
ATOM   1255 N NZ  . LYS A 1 145 ? -4.448  16.799  63.708  1.00 65.45 ? 145 LYS A NZ  1 
ATOM   1256 N N   . ASP A 1 146 ? -4.888  15.982  70.983  1.00 30.50 ? 146 ASP A N   1 
ATOM   1257 C CA  . ASP A 1 146 ? -5.645  15.247  71.992  1.00 30.47 ? 146 ASP A CA  1 
ATOM   1258 C C   . ASP A 1 146 ? -5.869  16.072  73.256  1.00 31.25 ? 146 ASP A C   1 
ATOM   1259 O O   . ASP A 1 146 ? -6.917  15.952  73.904  1.00 35.68 ? 146 ASP A O   1 
ATOM   1260 C CB  . ASP A 1 146 ? -4.926  13.942  72.332  1.00 43.81 ? 146 ASP A CB  1 
ATOM   1261 C CG  . ASP A 1 146 ? -4.855  12.989  71.147  1.00 58.29 ? 146 ASP A CG  1 
ATOM   1262 O OD1 . ASP A 1 146 ? -3.998  13.196  70.253  1.00 57.15 ? 146 ASP A OD1 1 
ATOM   1263 O OD2 . ASP A 1 146 ? -5.664  12.035  71.111  1.00 66.29 ? 146 ASP A OD2 1 
ATOM   1264 N N   . LEU A 1 147 ? -4.892  16.886  73.645  1.00 20.29 ? 147 LEU A N   1 
ATOM   1265 C CA  . LEU A 1 147 ? -4.949  17.678  74.865  1.00 18.97 ? 147 LEU A CA  1 
ATOM   1266 C C   . LEU A 1 147 ? -5.376  19.127  74.618  1.00 19.79 ? 147 LEU A C   1 
ATOM   1267 O O   . LEU A 1 147 ? -5.168  19.978  75.495  1.00 18.30 ? 147 LEU A O   1 
ATOM   1268 C CB  . LEU A 1 147 ? -3.592  17.652  75.578  1.00 19.46 ? 147 LEU A CB  1 
ATOM   1269 C CG  . LEU A 1 147 ? -3.125  16.270  76.055  1.00 25.70 ? 147 LEU A CG  1 
ATOM   1270 C CD1 . LEU A 1 147 ? -1.746  16.353  76.691  1.00 28.06 ? 147 LEU A CD1 1 
ATOM   1271 C CD2 . LEU A 1 147 ? -4.141  15.643  77.015  1.00 29.02 ? 147 LEU A CD2 1 
ATOM   1272 N N   . LYS A 1 148 ? -5.931  19.435  73.439  1.00 19.01 ? 148 LYS A N   1 
ATOM   1273 C CA  . LYS A 1 148 ? -6.326  20.815  73.148  1.00 19.98 ? 148 LYS A CA  1 
ATOM   1274 C C   . LYS A 1 148 ? -7.235  21.396  74.234  1.00 18.70 ? 148 LYS A C   1 
ATOM   1275 O O   . LYS A 1 148 ? -7.056  22.547  74.646  1.00 21.14 ? 148 LYS A O   1 
ATOM   1276 C CB  . LYS A 1 148 ? -7.014  20.873  71.777  1.00 22.33 ? 148 LYS A CB  1 
ATOM   1277 C CG  . LYS A 1 148 ? -7.465  22.263  71.319  1.00 22.48 ? 148 LYS A CG  1 
ATOM   1278 C CD  . LYS A 1 148 ? -7.982  22.170  69.870  1.00 28.12 ? 148 LYS A CD  1 
ATOM   1279 C CE  . LYS A 1 148 ? -8.118  23.517  69.152  1.00 39.32 ? 148 LYS A CE  1 
ATOM   1280 N NZ  . LYS A 1 148 ? -8.708  24.598  69.987  1.00 45.21 ? 148 LYS A NZ  1 
ATOM   1281 N N   . ASP A 1 149 ? -8.201  20.611  74.729  1.00 20.83 ? 149 ASP A N   1 
ATOM   1282 C CA  . ASP A 1 149 ? -9.110  21.132  75.754  1.00 22.30 ? 149 ASP A CA  1 
ATOM   1283 C C   . ASP A 1 149 ? -8.368  21.502  77.030  1.00 19.94 ? 149 ASP A C   1 
ATOM   1284 O O   . ASP A 1 149 ? -8.684  22.524  77.654  1.00 22.64 ? 149 ASP A O   1 
ATOM   1285 C CB  . ASP A 1 149 ? -10.211 20.120  76.077  1.00 29.81 ? 149 ASP A CB  1 
ATOM   1286 C CG  . ASP A 1 149 ? -10.983 19.702  74.860  1.00 37.25 ? 149 ASP A CG  1 
ATOM   1287 O OD1 . ASP A 1 149 ? -11.066 20.520  73.923  1.00 34.54 ? 149 ASP A OD1 1 
ATOM   1288 O OD2 . ASP A 1 149 ? -11.486 18.555  74.838  1.00 47.71 ? 149 ASP A OD2 1 
ATOM   1289 N N   . LEU A 1 150 ? -7.403  20.673  77.455  1.00 18.44 ? 150 LEU A N   1 
ATOM   1290 C CA  . LEU A 1 150 ? -6.620  20.995  78.651  1.00 20.58 ? 150 LEU A CA  1 
ATOM   1291 C C   . LEU A 1 150 ? -5.728  22.205  78.420  1.00 25.15 ? 150 LEU A C   1 
ATOM   1292 O O   . LEU A 1 150 ? -5.616  23.076  79.291  1.00 27.13 ? 150 LEU A O   1 
ATOM   1293 C CB  . LEU A 1 150 ? -5.755  19.800  79.084  1.00 21.91 ? 150 LEU A CB  1 
ATOM   1294 C CG  . LEU A 1 150 ? -6.494  18.793  79.971  1.00 30.25 ? 150 LEU A CG  1 
ATOM   1295 C CD1 . LEU A 1 150 ? -5.684  17.504  80.151  1.00 26.46 ? 150 LEU A CD1 1 
ATOM   1296 C CD2 . LEU A 1 150 ? -6.865  19.422  81.323  1.00 22.64 ? 150 LEU A CD2 1 
ATOM   1297 N N   . LEU A 1 151 ? -5.069  22.264  77.256  1.00 21.91 ? 151 LEU A N   1 
ATOM   1298 C CA  . LEU A 1 151 ? -4.240  23.417  76.924  1.00 18.56 ? 151 LEU A CA  1 
ATOM   1299 C C   . LEU A 1 151 ? -5.044  24.700  76.951  1.00 21.85 ? 151 LEU A C   1 
ATOM   1300 O O   . LEU A 1 151 ? -4.556  25.732  77.417  1.00 27.49 ? 151 LEU A O   1 
ATOM   1301 C CB  . LEU A 1 151 ? -3.604  23.238  75.540  1.00 19.67 ? 151 LEU A CB  1 
ATOM   1302 C CG  . LEU A 1 151 ? -2.517  22.190  75.488  1.00 20.13 ? 151 LEU A CG  1 
ATOM   1303 C CD1 . LEU A 1 151 ? -2.277  21.772  74.035  1.00 19.61 ? 151 LEU A CD1 1 
ATOM   1304 C CD2 . LEU A 1 151 ? -1.238  22.746  76.118  1.00 18.79 ? 151 LEU A CD2 1 
ATOM   1305 N N   . ASN A 1 152 ? -6.276  24.664  76.425  1.00 20.60 ? 152 ASN A N   1 
ATOM   1306 C CA  . ASN A 1 152 ? -7.105  25.854  76.395  1.00 24.70 ? 152 ASN A CA  1 
ATOM   1307 C C   . ASN A 1 152 ? -7.760  26.134  77.741  1.00 24.51 ? 152 ASN A C   1 
ATOM   1308 O O   . ASN A 1 152 ? -8.175  27.268  77.978  1.00 27.39 ? 152 ASN A O   1 
ATOM   1309 C CB  . ASN A 1 152 ? -8.168  25.726  75.304  1.00 28.05 ? 152 ASN A CB  1 
ATOM   1310 C CG  . ASN A 1 152 ? -7.586  25.885  73.908  1.00 41.13 ? 152 ASN A CG  1 
ATOM   1311 O OD1 . ASN A 1 152 ? -6.460  25.467  73.638  1.00 41.41 ? 152 ASN A OD1 1 
ATOM   1312 N ND2 . ASN A 1 152 ? -8.358  26.482  73.014  1.00 48.64 ? 152 ASN A ND2 1 
ATOM   1313 N N   . LYS A 1 153 ? -7.835  25.139  78.631  1.00 25.36 ? 153 LYS A N   1 
ATOM   1314 C CA  . LYS A 1 153 ? -8.432  25.375  79.946  1.00 26.00 ? 153 LYS A CA  1 
ATOM   1315 C C   . LYS A 1 153 ? -7.680  26.476  80.676  1.00 27.91 ? 153 LYS A C   1 
ATOM   1316 O O   . LYS A 1 153 ? -8.288  27.379  81.257  1.00 33.52 ? 153 LYS A O   1 
ATOM   1317 C CB  . LYS A 1 153 ? -8.421  24.078  80.763  1.00 24.67 ? 153 LYS A CB  1 
ATOM   1318 C CG  . LYS A 1 153 ? -9.013  24.192  82.160  1.00 27.30 ? 153 LYS A CG  1 
ATOM   1319 C CD  . LYS A 1 153 ? -9.095  22.821  82.844  1.00 28.90 ? 153 LYS A CD  1 
ATOM   1320 C CE  . LYS A 1 153 ? -9.734  22.935  84.214  1.00 30.21 ? 153 LYS A CE  1 
ATOM   1321 N NZ  . LYS A 1 153 ? -10.035 21.622  84.827  1.00 30.12 ? 153 LYS A NZ  1 
ATOM   1322 N N   . GLY A 1 154 ? -6.347  26.418  80.640  1.00 22.27 ? 154 GLY A N   1 
ATOM   1323 C CA  . GLY A 1 154 ? -5.509  27.496  81.111  1.00 31.09 ? 154 GLY A CA  1 
ATOM   1324 C C   . GLY A 1 154 ? -5.315  27.595  82.609  1.00 30.73 ? 154 GLY A C   1 
ATOM   1325 O O   . GLY A 1 154 ? -4.341  28.216  83.040  1.00 29.11 ? 154 GLY A O   1 
ATOM   1326 N N   . ARG A 1 155 ? -6.205  27.024  83.421  1.00 31.60 ? 155 ARG A N   1 
ATOM   1327 C CA  . ARG A 1 155 ? -6.127  27.212  84.867  1.00 29.49 ? 155 ARG A CA  1 
ATOM   1328 C C   . ARG A 1 155 ? -7.056  26.215  85.550  1.00 29.84 ? 155 ARG A C   1 
ATOM   1329 O O   . ARG A 1 155 ? -7.854  25.535  84.900  1.00 30.14 ? 155 ARG A O   1 
ATOM   1330 C CB  . ARG A 1 155 ? -6.496  28.643  85.263  1.00 29.81 ? 155 ARG A CB  1 
ATOM   1331 C CG  . ARG A 1 155 ? -7.969  28.973  85.036  1.00 36.33 ? 155 ARG A CG  1 
ATOM   1332 C CD  . ARG A 1 155 ? -8.289  30.411  85.421  1.00 43.86 ? 155 ARG A CD  1 
ATOM   1333 N NE  . ARG A 1 155 ? -7.568  31.366  84.579  1.00 47.92 ? 155 ARG A NE  1 
ATOM   1334 C CZ  . ARG A 1 155 ? -6.731  32.291  85.045  1.00 47.02 ? 155 ARG A CZ  1 
ATOM   1335 N NH1 . ARG A 1 155 ? -6.104  33.110  84.207  1.00 42.19 ? 155 ARG A NH1 1 
ATOM   1336 N NH2 . ARG A 1 155 ? -6.526  32.399  86.352  1.00 48.08 ? 155 ARG A NH2 1 
ATOM   1337 N N   . ASN A 1 156 ? -6.939  26.149  86.882  1.00 25.19 ? 156 ASN A N   1 
ATOM   1338 C CA  . ASN A 1 156 ? -7.781  25.302  87.730  1.00 24.11 ? 156 ASN A CA  1 
ATOM   1339 C C   . ASN A 1 156 ? -7.627  23.819  87.393  1.00 23.44 ? 156 ASN A C   1 
ATOM   1340 O O   . ASN A 1 156 ? -8.612  23.073  87.328  1.00 25.90 ? 156 ASN A O   1 
ATOM   1341 C CB  . ASN A 1 156 ? -9.252  25.733  87.650  1.00 27.96 ? 156 ASN A CB  1 
ATOM   1342 C CG  . ASN A 1 156 ? -9.450  27.182  88.060  1.00 39.61 ? 156 ASN A CG  1 
ATOM   1343 O OD1 . ASN A 1 156 ? -8.741  27.687  88.931  1.00 42.35 ? 156 ASN A OD1 1 
ATOM   1344 N ND2 . ASN A 1 156 ? -10.408 27.858  87.436  1.00 41.82 ? 156 ASN A ND2 1 
ATOM   1345 N N   . TYR A 1 157 ? -6.384  23.389  87.197  1.00 18.45 ? 157 TYR A N   1 
ATOM   1346 C CA  . TYR A 1 157 ? -6.088  21.993  86.927  1.00 20.02 ? 157 TYR A CA  1 
ATOM   1347 C C   . TYR A 1 157 ? -6.175  21.170  88.205  1.00 19.84 ? 157 TYR A C   1 
ATOM   1348 O O   . TYR A 1 157 ? -5.841  21.644  89.296  1.00 26.28 ? 157 TYR A O   1 
ATOM   1349 C CB  . TYR A 1 157 ? -4.703  21.863  86.304  1.00 16.48 ? 157 TYR A CB  1 
ATOM   1350 C CG  . TYR A 1 157 ? -4.612  22.521  84.965  1.00 16.48 ? 157 TYR A CG  1 
ATOM   1351 C CD1 . TYR A 1 157 ? -5.118  21.897  83.834  1.00 20.65 ? 157 TYR A CD1 1 
ATOM   1352 C CD2 . TYR A 1 157 ? -4.046  23.792  84.826  1.00 21.14 ? 157 TYR A CD2 1 
ATOM   1353 C CE1 . TYR A 1 157 ? -5.032  22.510  82.584  1.00 21.14 ? 157 TYR A CE1 1 
ATOM   1354 C CE2 . TYR A 1 157 ? -3.959  24.413  83.586  1.00 22.13 ? 157 TYR A CE2 1 
ATOM   1355 C CZ  . TYR A 1 157 ? -4.448  23.761  82.469  1.00 21.81 ? 157 TYR A CZ  1 
ATOM   1356 O OH  . TYR A 1 157 ? -4.358  24.379  81.225  1.00 20.90 ? 157 TYR A OH  1 
ATOM   1357 N N   . THR A 1 158 ? -6.638  19.931  88.064  1.00 21.30 ? 158 THR A N   1 
ATOM   1358 C CA  . THR A 1 158 ? -6.737  19.005  89.188  1.00 21.58 ? 158 THR A CA  1 
ATOM   1359 C C   . THR A 1 158 ? -5.577  18.014  89.168  1.00 17.04 ? 158 THR A C   1 
ATOM   1360 O O   . THR A 1 158 ? -4.905  17.829  88.154  1.00 15.99 ? 158 THR A O   1 
ATOM   1361 C CB  . THR A 1 158 ? -8.047  18.235  89.153  1.00 23.06 ? 158 THR A CB  1 
ATOM   1362 O OG1 . THR A 1 158 ? -8.067  17.412  87.978  1.00 22.78 ? 158 THR A OG1 1 
ATOM   1363 C CG2 . THR A 1 158 ? -9.223  19.193  89.148  1.00 21.70 ? 158 THR A CG2 1 
ATOM   1364 N N   . GLN A 1 159 ? -5.351  17.365  90.317  1.00 19.38 ? 159 GLN A N   1 
ATOM   1365 C CA  . GLN A 1 159 ? -4.333  16.321  90.376  1.00 19.50 ? 159 GLN A CA  1 
ATOM   1366 C C   . GLN A 1 159 ? -4.645  15.209  89.378  1.00 18.27 ? 159 GLN A C   1 
ATOM   1367 O O   . GLN A 1 159 ? -3.743  14.680  88.718  1.00 19.58 ? 159 GLN A O   1 
ATOM   1368 C CB  . GLN A 1 159 ? -4.238  15.789  91.815  1.00 23.56 ? 159 GLN A CB  1 
ATOM   1369 C CG  . GLN A 1 159 ? -3.314  14.600  92.036  1.00 21.74 ? 159 GLN A CG  1 
ATOM   1370 C CD  . GLN A 1 159 ? -1.836  14.983  92.000  1.00 23.07 ? 159 GLN A CD  1 
ATOM   1371 O OE1 . GLN A 1 159 ? -1.472  16.139  92.246  1.00 21.97 ? 159 GLN A OE1 1 
ATOM   1372 N NE2 . GLN A 1 159 ? -0.982  14.020  91.648  1.00 20.49 ? 159 GLN A NE2 1 
ATOM   1373 N N   . GLU A 1 160 ? -5.935  14.879  89.219  1.00 19.36 ? 160 GLU A N   1 
ATOM   1374 C CA  . GLU A 1 160 ? -6.344  13.856  88.262  1.00 21.07 ? 160 GLU A CA  1 
ATOM   1375 C C   . GLU A 1 160 ? -5.972  14.232  86.827  1.00 22.11 ? 160 GLU A C   1 
ATOM   1376 O O   . GLU A 1 160 ? -5.534  13.374  86.052  1.00 22.53 ? 160 GLU A O   1 
ATOM   1377 C CB  . GLU A 1 160 ? -7.853  13.633  88.378  1.00 27.95 ? 160 GLU A CB  1 
ATOM   1378 C CG  . GLU A 1 160 ? -8.397  12.439  87.630  1.00 35.44 ? 160 GLU A CG  1 
ATOM   1379 C CD  . GLU A 1 160 ? -9.893  12.258  87.869  1.00 47.62 ? 160 GLU A CD  1 
ATOM   1380 O OE1 . GLU A 1 160 ? -10.343 12.371  89.030  1.00 50.58 ? 160 GLU A OE1 1 
ATOM   1381 O OE2 . GLU A 1 160 ? -10.620 12.005  86.892  1.00 51.39 ? 160 GLU A OE2 1 
ATOM   1382 N N   . GLU A 1 161 ? -6.149  15.504  86.451  1.00 17.63 ? 161 GLU A N   1 
ATOM   1383 C CA  . GLU A 1 161 ? -5.798  15.939  85.103  1.00 17.09 ? 161 GLU A CA  1 
ATOM   1384 C C   . GLU A 1 161 ? -4.296  15.883  84.892  1.00 17.45 ? 161 GLU A C   1 
ATOM   1385 O O   . GLU A 1 161 ? -3.825  15.464  83.827  1.00 18.07 ? 161 GLU A O   1 
ATOM   1386 C CB  . GLU A 1 161 ? -6.327  17.360  84.848  1.00 16.84 ? 161 GLU A CB  1 
ATOM   1387 C CG  . GLU A 1 161 ? -7.858  17.398  84.709  1.00 18.31 ? 161 GLU A CG  1 
ATOM   1388 C CD  . GLU A 1 161 ? -8.441  18.817  84.644  1.00 27.34 ? 161 GLU A CD  1 
ATOM   1389 O OE1 . GLU A 1 161 ? -7.887  19.745  85.272  1.00 24.00 ? 161 GLU A OE1 1 
ATOM   1390 O OE2 . GLU A 1 161 ? -9.488  19.002  83.987  1.00 31.65 ? 161 GLU A OE2 1 
ATOM   1391 N N   . LYS A 1 162 ? -3.531  16.326  85.890  1.00 15.36 ? 162 LYS A N   1 
ATOM   1392 C CA  . LYS A 1 162 ? -2.076  16.243  85.805  1.00 14.95 ? 162 LYS A CA  1 
ATOM   1393 C C   . LYS A 1 162 ? -1.617  14.803  85.573  1.00 15.05 ? 162 LYS A C   1 
ATOM   1394 O O   . LYS A 1 162 ? -0.737  14.541  84.737  1.00 15.08 ? 162 LYS A O   1 
ATOM   1395 C CB  . LYS A 1 162 ? -1.478  16.816  87.091  1.00 14.46 ? 162 LYS A CB  1 
ATOM   1396 C CG  . LYS A 1 162 ? 0.021   16.953  87.077  1.00 14.54 ? 162 LYS A CG  1 
ATOM   1397 C CD  . LYS A 1 162 ? 0.472   17.650  88.375  1.00 17.22 ? 162 LYS A CD  1 
ATOM   1398 C CE  . LYS A 1 162 ? -0.007  16.918  89.593  1.00 17.59 ? 162 LYS A CE  1 
ATOM   1399 N NZ  . LYS A 1 162 ? 0.788   17.324  90.815  1.00 16.47 ? 162 LYS A NZ  1 
ATOM   1400 N N   . GLU A 1 163 ? -2.181  13.861  86.337  1.00 16.50 ? 163 GLU A N   1 
ATOM   1401 C CA  . GLU A 1 163 ? -1.807  12.457  86.172  1.00 17.97 ? 163 GLU A CA  1 
ATOM   1402 C C   . GLU A 1 163 ? -2.199  11.932  84.797  1.00 17.41 ? 163 GLU A C   1 
ATOM   1403 O O   . GLU A 1 163 ? -1.484  11.106  84.216  1.00 18.01 ? 163 GLU A O   1 
ATOM   1404 C CB  . GLU A 1 163 ? -2.455  11.614  87.276  1.00 22.00 ? 163 GLU A CB  1 
ATOM   1405 C CG  . GLU A 1 163 ? -1.774  11.843  88.626  1.00 23.87 ? 163 GLU A CG  1 
ATOM   1406 C CD  . GLU A 1 163 ? -2.608  11.411  89.823  1.00 33.71 ? 163 GLU A CD  1 
ATOM   1407 O OE1 . GLU A 1 163 ? -2.097  11.496  90.960  1.00 33.98 ? 163 GLU A OE1 1 
ATOM   1408 O OE2 . GLU A 1 163 ? -3.771  10.996  89.632  1.00 34.49 ? 163 GLU A OE2 1 
ATOM   1409 N N   . TYR A 1 164 ? -3.327  12.400  84.272  1.00 15.33 ? 164 TYR A N   1 
ATOM   1410 C CA  . TYR A 1 164 ? -3.748  12.015  82.924  1.00 17.65 ? 164 TYR A CA  1 
ATOM   1411 C C   . TYR A 1 164 ? -2.732  12.481  81.887  1.00 17.93 ? 164 TYR A C   1 
ATOM   1412 O O   . TYR A 1 164 ? -2.367  11.724  80.978  1.00 17.59 ? 164 TYR A O   1 
ATOM   1413 C CB  . TYR A 1 164 ? -5.143  12.591  82.648  1.00 19.30 ? 164 TYR A CB  1 
ATOM   1414 C CG  . TYR A 1 164 ? -5.691  12.400  81.241  1.00 23.20 ? 164 TYR A CG  1 
ATOM   1415 C CD1 . TYR A 1 164 ? -6.278  11.202  80.859  1.00 27.64 ? 164 TYR A CD1 1 
ATOM   1416 C CD2 . TYR A 1 164 ? -5.646  13.432  80.310  1.00 21.61 ? 164 TYR A CD2 1 
ATOM   1417 C CE1 . TYR A 1 164 ? -6.800  11.040  79.583  1.00 32.82 ? 164 TYR A CE1 1 
ATOM   1418 C CE2 . TYR A 1 164 ? -6.173  13.275  79.027  1.00 25.16 ? 164 TYR A CE2 1 
ATOM   1419 C CZ  . TYR A 1 164 ? -6.729  12.078  78.672  1.00 32.59 ? 164 TYR A CZ  1 
ATOM   1420 O OH  . TYR A 1 164 ? -7.254  11.917  77.401  1.00 40.46 ? 164 TYR A OH  1 
ATOM   1421 N N   . VAL A 1 165 ? -2.249  13.719  82.022  1.00 14.22 ? 165 VAL A N   1 
ATOM   1422 C CA  . VAL A 1 165 ? -1.240  14.238  81.105  1.00 14.53 ? 165 VAL A CA  1 
ATOM   1423 C C   . VAL A 1 165 ? 0.037   13.411  81.209  1.00 15.55 ? 165 VAL A C   1 
ATOM   1424 O O   . VAL A 1 165 ? 0.626   13.007  80.194  1.00 14.83 ? 165 VAL A O   1 
ATOM   1425 C CB  . VAL A 1 165 ? -0.970  15.737  81.380  1.00 14.28 ? 165 VAL A CB  1 
ATOM   1426 C CG1 . VAL A 1 165 ? 0.220   16.230  80.525  1.00 13.64 ? 165 VAL A CG1 1 
ATOM   1427 C CG2 . VAL A 1 165 ? -2.203  16.622  81.097  1.00 13.51 ? 165 VAL A CG2 1 
ATOM   1428 N N   . LEU A 1 166 ? 0.497   13.149  82.442  1.00 13.13 ? 166 LEU A N   1 
ATOM   1429 C CA  . LEU A 1 166 ? 1.694   12.328  82.618  1.00 14.54 ? 166 LEU A CA  1 
ATOM   1430 C C   . LEU A 1 166 ? 1.532   10.954  81.967  1.00 16.94 ? 166 LEU A C   1 
ATOM   1431 O O   . LEU A 1 166 ? 2.477   10.426  81.364  1.00 16.25 ? 166 LEU A O   1 
ATOM   1432 C CB  . LEU A 1 166 ? 2.007   12.172  84.105  1.00 19.00 ? 166 LEU A CB  1 
ATOM   1433 C CG  . LEU A 1 166 ? 2.491   13.438  84.787  1.00 18.09 ? 166 LEU A CG  1 
ATOM   1434 C CD1 . LEU A 1 166 ? 2.343   13.307  86.311  1.00 22.12 ? 166 LEU A CD1 1 
ATOM   1435 C CD2 . LEU A 1 166 ? 3.954   13.694  84.393  1.00 20.76 ? 166 LEU A CD2 1 
ATOM   1436 N N   . ASN A 1 167 ? 0.348   10.353  82.088  1.00 15.41 ? 167 ASN A N   1 
ATOM   1437 C CA  . ASN A 1 167 ? 0.131   9.050   81.455  1.00 18.02 ? 167 ASN A CA  1 
ATOM   1438 C C   . ASN A 1 167 ? 0.253   9.147   79.935  1.00 19.27 ? 167 ASN A C   1 
ATOM   1439 O O   . ASN A 1 167 ? 0.848   8.269   79.291  1.00 17.13 ? 167 ASN A O   1 
ATOM   1440 C CB  . ASN A 1 167 ? -1.240  8.493   81.843  1.00 20.43 ? 167 ASN A CB  1 
ATOM   1441 C CG  . ASN A 1 167 ? -1.519  7.144   81.202  1.00 37.85 ? 167 ASN A CG  1 
ATOM   1442 O OD1 . ASN A 1 167 ? -2.413  7.004   80.362  1.00 42.69 ? 167 ASN A OD1 1 
ATOM   1443 N ND2 . ASN A 1 167 ? -0.741  6.145   81.587  1.00 44.69 ? 167 ASN A ND2 1 
ATOM   1444 N N   . LYS A 1 168 ? -0.305  10.206  79.341  1.00 18.13 ? 168 LYS A N   1 
ATOM   1445 C CA  . LYS A 1 168 ? -0.226  10.347  77.888  1.00 17.18 ? 168 LYS A CA  1 
ATOM   1446 C C   . LYS A 1 168 ? 1.210   10.593  77.462  1.00 14.84 ? 168 LYS A C   1 
ATOM   1447 O O   . LYS A 1 168 ? 1.654   10.088  76.426  1.00 12.85 ? 168 LYS A O   1 
ATOM   1448 C CB  . LYS A 1 168 ? -1.107  11.497  77.398  1.00 17.25 ? 168 LYS A CB  1 
ATOM   1449 C CG  . LYS A 1 168 ? -2.598  11.283  77.573  1.00 19.71 ? 168 LYS A CG  1 
ATOM   1450 C CD  . LYS A 1 168 ? -3.114  10.249  76.613  1.00 27.17 ? 168 LYS A CD  1 
ATOM   1451 C CE  . LYS A 1 168 ? -4.523  10.590  76.185  1.00 41.61 ? 168 LYS A CE  1 
ATOM   1452 N NZ  . LYS A 1 168 ? -5.435  9.439   76.392  1.00 52.67 ? 168 LYS A NZ  1 
ATOM   1453 N N   . TYR A 1 169 ? 1.950   11.355  78.265  1.00 13.52 ? 169 TYR A N   1 
ATOM   1454 C CA  . TYR A 1 169 ? 3.345   11.644  77.937  1.00 12.30 ? 169 TYR A CA  1 
ATOM   1455 C C   . TYR A 1 169 ? 4.191   10.379  77.957  1.00 14.26 ? 169 TYR A C   1 
ATOM   1456 O O   . TYR A 1 169 ? 5.093   10.215  77.121  1.00 13.51 ? 169 TYR A O   1 
ATOM   1457 C CB  . TYR A 1 169 ? 3.918   12.677  78.919  1.00 11.92 ? 169 TYR A CB  1 
ATOM   1458 C CG  . TYR A 1 169 ? 3.575   14.129  78.596  1.00 11.03 ? 169 TYR A CG  1 
ATOM   1459 C CD1 . TYR A 1 169 ? 2.555   14.455  77.696  1.00 10.04 ? 169 TYR A CD1 1 
ATOM   1460 C CD2 . TYR A 1 169 ? 4.242   15.163  79.236  1.00 13.38 ? 169 TYR A CD2 1 
ATOM   1461 C CE1 . TYR A 1 169 ? 2.234   15.793  77.408  1.00 14.58 ? 169 TYR A CE1 1 
ATOM   1462 C CE2 . TYR A 1 169 ? 3.935   16.501  78.955  1.00 11.04 ? 169 TYR A CE2 1 
ATOM   1463 C CZ  . TYR A 1 169 ? 2.938   16.807  78.058  1.00 14.13 ? 169 TYR A CZ  1 
ATOM   1464 O OH  . TYR A 1 169 ? 2.635   18.143  77.780  1.00 13.51 ? 169 TYR A OH  1 
ATOM   1465 N N   . PHE A 1 170 ? 3.964   9.496   78.937  1.00 15.28 ? 170 PHE A N   1 
ATOM   1466 C CA  . PHE A 1 170 ? 4.735   8.268   78.951  1.00 14.94 ? 170 PHE A CA  1 
ATOM   1467 C C   . PHE A 1 170 ? 4.349   7.334   77.808  1.00 15.16 ? 170 PHE A C   1 
ATOM   1468 O O   . PHE A 1 170 ? 5.211   6.585   77.320  1.00 13.51 ? 170 PHE A O   1 
ATOM   1469 C CB  . PHE A 1 170 ? 4.622   7.576   80.310  1.00 19.57 ? 170 PHE A CB  1 
ATOM   1470 C CG  . PHE A 1 170 ? 5.637   8.076   81.288  1.00 18.45 ? 170 PHE A CG  1 
ATOM   1471 C CD1 . PHE A 1 170 ? 6.977   7.695   81.173  1.00 20.48 ? 170 PHE A CD1 1 
ATOM   1472 C CD2 . PHE A 1 170 ? 5.283   8.983   82.273  1.00 21.87 ? 170 PHE A CD2 1 
ATOM   1473 C CE1 . PHE A 1 170 ? 7.932   8.175   82.059  1.00 22.41 ? 170 PHE A CE1 1 
ATOM   1474 C CE2 . PHE A 1 170 ? 6.229   9.454   83.170  1.00 24.20 ? 170 PHE A CE2 1 
ATOM   1475 C CZ  . PHE A 1 170 ? 7.553   9.058   83.061  1.00 23.31 ? 170 PHE A CZ  1 
ATOM   1476 N N   . GLU A 1 171 ? 3.094   7.372   77.347  1.00 13.49 ? 171 GLU A N   1 
ATOM   1477 C CA  . GLU A 1 171 ? 2.758   6.650   76.117  1.00 12.99 ? 171 GLU A CA  1 
ATOM   1478 C C   . GLU A 1 171 ? 3.608   7.126   74.939  1.00 12.47 ? 171 GLU A C   1 
ATOM   1479 O O   . GLU A 1 171 ? 4.092   6.312   74.149  1.00 16.40 ? 171 GLU A O   1 
ATOM   1480 C CB  . GLU A 1 171 ? 1.267   6.805   75.790  1.00 15.55 ? 171 GLU A CB  1 
ATOM   1481 C CG  . GLU A 1 171 ? 0.323   6.093   76.742  1.00 31.63 ? 171 GLU A CG  1 
ATOM   1482 C CD  . GLU A 1 171 ? -1.140  6.464   76.513  1.00 42.95 ? 171 GLU A CD  1 
ATOM   1483 O OE1 . GLU A 1 171 ? -1.448  7.109   75.487  1.00 44.86 ? 171 GLU A OE1 1 
ATOM   1484 O OE2 . GLU A 1 171 ? -1.986  6.105   77.360  1.00 50.08 ? 171 GLU A OE2 1 
ATOM   1485 N N   . ILE A 1 172 ? 3.794   8.438   74.798  1.00 12.39 ? 172 ILE A N   1 
ATOM   1486 C CA  . ILE A 1 172 ? 4.629   8.964   73.716  1.00 11.59 ? 172 ILE A CA  1 
ATOM   1487 C C   . ILE A 1 172 ? 6.053   8.462   73.875  1.00 14.24 ? 172 ILE A C   1 
ATOM   1488 O O   . ILE A 1 172 ? 6.676   8.004   72.907  1.00 13.68 ? 172 ILE A O   1 
ATOM   1489 C CB  . ILE A 1 172 ? 4.579   10.514  73.692  1.00 9.46  ? 172 ILE A CB  1 
ATOM   1490 C CG1 . ILE A 1 172 ? 3.194   11.012  73.260  1.00 13.19 ? 172 ILE A CG1 1 
ATOM   1491 C CG2 . ILE A 1 172 ? 5.666   11.140  72.782  1.00 11.76 ? 172 ILE A CG2 1 
ATOM   1492 C CD1 . ILE A 1 172 ? 2.784   10.677  71.801  1.00 17.22 ? 172 ILE A CD1 1 
ATOM   1493 N N   . ILE A 1 173 ? 6.577   8.504   75.104  1.00 10.27 ? 173 ILE A N   1 
ATOM   1494 C CA  . ILE A 1 173 ? 7.949   8.057   75.315  1.00 9.92  ? 173 ILE A CA  1 
ATOM   1495 C C   . ILE A 1 173 ? 8.078   6.593   74.911  1.00 12.51 ? 173 ILE A C   1 
ATOM   1496 O O   . ILE A 1 173 ? 9.048   6.200   74.254  1.00 12.02 ? 173 ILE A O   1 
ATOM   1497 C CB  . ILE A 1 173 ? 8.387   8.297   76.768  1.00 13.90 ? 173 ILE A CB  1 
ATOM   1498 C CG1 . ILE A 1 173 ? 8.459   9.815   77.016  1.00 17.19 ? 173 ILE A CG1 1 
ATOM   1499 C CG2 . ILE A 1 173 ? 9.723   7.572   77.044  1.00 18.01 ? 173 ILE A CG2 1 
ATOM   1500 C CD1 . ILE A 1 173 ? 8.799   10.203  78.449  1.00 15.97 ? 173 ILE A CD1 1 
ATOM   1501 N N   . LYS A 1 174 ? 7.088   5.777   75.264  1.00 12.93 ? 174 LYS A N   1 
ATOM   1502 C CA  . LYS A 1 174 ? 7.143   4.352   74.956  1.00 13.22 ? 174 LYS A CA  1 
ATOM   1503 C C   . LYS A 1 174 ? 7.095   4.065   73.451  1.00 17.63 ? 174 LYS A C   1 
ATOM   1504 O O   . LYS A 1 174 ? 7.468   2.963   73.028  1.00 17.99 ? 174 LYS A O   1 
ATOM   1505 C CB  . LYS A 1 174 ? 5.990   3.635   75.669  1.00 17.86 ? 174 LYS A CB  1 
ATOM   1506 C CG  . LYS A 1 174 ? 6.256   3.387   77.146  1.00 19.84 ? 174 LYS A CG  1 
ATOM   1507 C CD  . LYS A 1 174 ? 5.008   2.865   77.845  1.00 22.51 ? 174 LYS A CD  1 
ATOM   1508 C CE  . LYS A 1 174 ? 5.296   1.569   78.575  1.00 38.43 ? 174 LYS A CE  1 
ATOM   1509 N NZ  . LYS A 1 174 ? 4.132   1.125   79.391  1.00 50.29 ? 174 LYS A NZ  1 
ATOM   1510 N N   . LYS A 1 175 ? 6.642   5.014   72.640  1.00 14.91 ? 175 LYS A N   1 
ATOM   1511 C CA  . LYS A 1 175 ? 6.556   4.855   71.190  1.00 15.12 ? 175 LYS A CA  1 
ATOM   1512 C C   . LYS A 1 175 ? 7.717   5.502   70.452  1.00 15.04 ? 175 LYS A C   1 
ATOM   1513 O O   . LYS A 1 175 ? 7.731   5.462   69.212  1.00 13.40 ? 175 LYS A O   1 
ATOM   1514 C CB  . LYS A 1 175 ? 5.249   5.472   70.649  1.00 18.24 ? 175 LYS A CB  1 
ATOM   1515 C CG  . LYS A 1 175 ? 3.983   4.805   71.131  1.00 33.21 ? 175 LYS A CG  1 
ATOM   1516 C CD  . LYS A 1 175 ? 2.757   5.401   70.452  1.00 41.20 ? 175 LYS A CD  1 
ATOM   1517 C CE  . LYS A 1 175 ? 2.731   6.920   70.558  1.00 49.61 ? 175 LYS A CE  1 
ATOM   1518 N NZ  . LYS A 1 175 ? 1.513   7.511   69.900  1.00 57.05 ? 175 LYS A NZ  1 
ATOM   1519 N N   . THR A 1 176 ? 8.662   6.118   71.181  1.00 12.95 ? 176 THR A N   1 
ATOM   1520 C CA  . THR A 1 176 ? 9.621   7.029   70.553  1.00 11.68 ? 176 THR A CA  1 
ATOM   1521 C C   . THR A 1 176 ? 10.667  6.265   69.744  1.00 11.72 ? 176 THR A C   1 
ATOM   1522 O O   . THR A 1 176 ? 10.893  6.588   68.578  1.00 14.40 ? 176 THR A O   1 
ATOM   1523 C CB  . THR A 1 176 ? 10.279  7.936   71.605  1.00 11.99 ? 176 THR A CB  1 
ATOM   1524 O OG1 . THR A 1 176 ? 9.305   8.846   72.116  1.00 12.24 ? 176 THR A OG1 1 
ATOM   1525 C CG2 . THR A 1 176 ? 11.442  8.790   71.017  1.00 11.91 ? 176 THR A CG2 1 
ATOM   1526 N N   . LEU A 1 177 ? 11.295  5.219   70.310  1.00 14.52 ? 177 LEU A N   1 
ATOM   1527 C CA  . LEU A 1 177 ? 12.263  4.489   69.488  1.00 15.49 ? 177 LEU A CA  1 
ATOM   1528 C C   . LEU A 1 177 ? 11.583  3.788   68.315  1.00 16.43 ? 177 LEU A C   1 
ATOM   1529 O O   . LEU A 1 177 ? 12.175  3.673   67.235  1.00 14.24 ? 177 LEU A O   1 
ATOM   1530 C CB  . LEU A 1 177 ? 13.046  3.489   70.329  1.00 15.17 ? 177 LEU A CB  1 
ATOM   1531 C CG  . LEU A 1 177 ? 14.043  4.142   71.295  1.00 23.57 ? 177 LEU A CG  1 
ATOM   1532 C CD1 . LEU A 1 177 ? 14.882  3.066   71.938  1.00 29.00 ? 177 LEU A CD1 1 
ATOM   1533 C CD2 . LEU A 1 177 ? 14.940  5.174   70.591  1.00 26.98 ? 177 LEU A CD2 1 
ATOM   1534 N N   . SER A 1 178 ? 10.326  3.373   68.493  1.00 11.86 ? 178 SER A N   1 
ATOM   1535 C CA  . SER A 1 178 ? 9.594   2.706   67.422  1.00 12.73 ? 178 SER A CA  1 
ATOM   1536 C C   . SER A 1 178 ? 9.388   3.609   66.212  1.00 12.74 ? 178 SER A C   1 
ATOM   1537 O O   . SER A 1 178 ? 9.387   3.116   65.079  1.00 13.75 ? 178 SER A O   1 
ATOM   1538 C CB  . SER A 1 178 ? 8.246   2.229   67.944  1.00 13.69 ? 178 SER A CB  1 
ATOM   1539 O OG  . SER A 1 178 ? 8.464   1.140   68.835  1.00 20.28 ? 178 SER A OG  1 
ATOM   1540 N N   . ILE A 1 179 ? 9.186   4.917   66.416  1.00 13.11 ? 179 ILE A N   1 
ATOM   1541 C CA  . ILE A 1 179 ? 8.900   5.745   65.246  1.00 12.91 ? 179 ILE A CA  1 
ATOM   1542 C C   . ILE A 1 179 ? 10.163  5.940   64.409  1.00 10.37 ? 179 ILE A C   1 
ATOM   1543 O O   . ILE A 1 179 ? 10.075  6.049   63.184  1.00 10.68 ? 179 ILE A O   1 
ATOM   1544 C CB  . ILE A 1 179 ? 8.250   7.094   65.646  1.00 14.71 ? 179 ILE A CB  1 
ATOM   1545 C CG1 . ILE A 1 179 ? 7.826   7.941   64.409  1.00 14.52 ? 179 ILE A CG1 1 
ATOM   1546 C CG2 . ILE A 1 179 ? 9.179   7.960   66.477  1.00 15.01 ? 179 ILE A CG2 1 
ATOM   1547 C CD1 . ILE A 1 179 ? 6.672   7.347   63.623  1.00 23.68 ? 179 ILE A CD1 1 
ATOM   1548 N N   . TYR A 1 180 ? 11.342  5.939   65.041  1.00 10.15 ? 180 TYR A N   1 
ATOM   1549 C CA  . TYR A 1 180 ? 12.589  6.004   64.279  1.00 10.31 ? 180 TYR A CA  1 
ATOM   1550 C C   . TYR A 1 180 ? 12.797  4.739   63.480  1.00 13.60 ? 180 TYR A C   1 
ATOM   1551 O O   . TYR A 1 180 ? 13.211  4.798   62.312  1.00 12.85 ? 180 TYR A O   1 
ATOM   1552 C CB  . TYR A 1 180 ? 13.792  6.260   65.199  1.00 10.37 ? 180 TYR A CB  1 
ATOM   1553 C CG  . TYR A 1 180 ? 13.822  7.690   65.736  1.00 9.97  ? 180 TYR A CG  1 
ATOM   1554 C CD1 . TYR A 1 180 ? 14.318  8.731   64.958  1.00 11.11 ? 180 TYR A CD1 1 
ATOM   1555 C CD2 . TYR A 1 180 ? 13.296  8.011   66.995  1.00 9.79  ? 180 TYR A CD2 1 
ATOM   1556 C CE1 . TYR A 1 180 ? 14.319  10.008  65.415  1.00 10.11 ? 180 TYR A CE1 1 
ATOM   1557 C CE2 . TYR A 1 180 ? 13.294  9.314   67.463  1.00 9.41  ? 180 TYR A CE2 1 
ATOM   1558 C CZ  . TYR A 1 180 ? 13.823  10.287  66.673  1.00 9.70  ? 180 TYR A CZ  1 
ATOM   1559 O OH  . TYR A 1 180 ? 13.808  11.598  67.070  1.00 9.81  ? 180 TYR A OH  1 
ATOM   1560 N N   . ARG A 1 181 ? 12.545  3.596   64.098  1.00 14.80 ? 181 ARG A N   1 
ATOM   1561 C CA  . ARG A 1 181 ? 12.632  2.364   63.338  1.00 12.33 ? 181 ARG A CA  1 
ATOM   1562 C C   . ARG A 1 181 ? 11.621  2.348   62.211  1.00 19.78 ? 181 ARG A C   1 
ATOM   1563 O O   . ARG A 1 181 ? 11.937  1.898   61.113  1.00 13.00 ? 181 ARG A O   1 
ATOM   1564 C CB  . ARG A 1 181 ? 12.415  1.147   64.230  1.00 13.31 ? 181 ARG A CB  1 
ATOM   1565 C CG  . ARG A 1 181 ? 13.388  1.062   65.367  1.00 13.57 ? 181 ARG A CG  1 
ATOM   1566 C CD  . ARG A 1 181 ? 13.166  -0.312  65.977  1.00 21.77 ? 181 ARG A CD  1 
ATOM   1567 N NE  . ARG A 1 181 ? 13.930  -0.627  67.168  1.00 31.36 ? 181 ARG A NE  1 
ATOM   1568 C CZ  . ARG A 1 181 ? 13.446  -0.537  68.407  1.00 35.21 ? 181 ARG A CZ  1 
ATOM   1569 N NH1 . ARG A 1 181 ? 12.207  -0.102  68.615  1.00 29.01 ? 181 ARG A NH1 1 
ATOM   1570 N NH2 . ARG A 1 181 ? 14.214  -0.861  69.438  1.00 30.75 ? 181 ARG A NH2 1 
ATOM   1571 N N   . GLU A 1 182 ? 10.390  2.796   62.473  1.00 12.43 ? 182 GLU A N   1 
ATOM   1572 C CA  . GLU A 1 182 ? 9.366   2.762   61.429  1.00 13.08 ? 182 GLU A CA  1 
ATOM   1573 C C   . GLU A 1 182 ? 9.765   3.593   60.214  1.00 14.48 ? 182 GLU A C   1 
ATOM   1574 O O   . GLU A 1 182 ? 9.630   3.143   59.070  1.00 15.74 ? 182 GLU A O   1 
ATOM   1575 C CB  . GLU A 1 182 ? 8.018   3.248   61.964  1.00 13.60 ? 182 GLU A CB  1 
ATOM   1576 C CG  . GLU A 1 182 ? 6.996   3.413   60.850  1.00 18.81 ? 182 GLU A CG  1 
ATOM   1577 C CD  . GLU A 1 182 ? 5.599   3.819   61.341  1.00 27.59 ? 182 GLU A CD  1 
ATOM   1578 O OE1 . GLU A 1 182 ? 4.717   4.049   60.479  1.00 29.52 ? 182 GLU A OE1 1 
ATOM   1579 O OE2 . GLU A 1 182 ? 5.375   3.899   62.568  1.00 24.30 ? 182 GLU A OE2 1 
ATOM   1580 N N   . ILE A 1 183 ? 10.221  4.830   60.427  1.00 12.19 ? 183 ILE A N   1 
ATOM   1581 C CA  . ILE A 1 183 ? 10.472  5.666   59.254  1.00 12.45 ? 183 ILE A CA  1 
ATOM   1582 C C   . ILE A 1 183 ? 11.697  5.170   58.482  1.00 13.58 ? 183 ILE A C   1 
ATOM   1583 O O   . ILE A 1 183 ? 11.765  5.335   57.260  1.00 13.21 ? 183 ILE A O   1 
ATOM   1584 C CB  . ILE A 1 183 ? 10.571  7.165   59.637  1.00 13.25 ? 183 ILE A CB  1 
ATOM   1585 C CG1 . ILE A 1 183 ? 11.780  7.494   60.552  1.00 13.00 ? 183 ILE A CG1 1 
ATOM   1586 C CG2 . ILE A 1 183 ? 9.258   7.633   60.294  1.00 16.58 ? 183 ILE A CG2 1 
ATOM   1587 C CD1 . ILE A 1 183 ? 13.042  7.979   59.771  1.00 14.84 ? 183 ILE A CD1 1 
ATOM   1588 N N   . LYS A 1 184 ? 12.696  4.611   59.180  1.00 13.45 ? 184 LYS A N   1 
ATOM   1589 C CA  . LYS A 1 184 ? 13.813  3.949   58.515  1.00 13.95 ? 184 LYS A CA  1 
ATOM   1590 C C   . LYS A 1 184 ? 13.319  2.791   57.664  1.00 18.84 ? 184 LYS A C   1 
ATOM   1591 O O   . LYS A 1 184 ? 13.689  2.660   56.484  1.00 16.40 ? 184 LYS A O   1 
ATOM   1592 C CB  . LYS A 1 184 ? 14.804  3.418   59.557  1.00 13.00 ? 184 LYS A CB  1 
ATOM   1593 C CG  . LYS A 1 184 ? 16.177  3.035   59.013  1.00 17.40 ? 184 LYS A CG  1 
ATOM   1594 C CD  . LYS A 1 184 ? 16.992  2.405   60.155  1.00 23.43 ? 184 LYS A CD  1 
ATOM   1595 C CE  . LYS A 1 184 ? 18.334  1.795   59.721  1.00 22.07 ? 184 LYS A CE  1 
ATOM   1596 N NZ  . LYS A 1 184 ? 18.290  1.036   58.452  1.00 34.57 ? 184 LYS A NZ  1 
ATOM   1597 N N   . GLU A 1 185 ? 12.484  1.935   58.258  1.00 13.79 ? 185 GLU A N   1 
ATOM   1598 C CA  . GLU A 1 185 ? 12.016  0.747   57.541  1.00 14.80 ? 185 GLU A CA  1 
ATOM   1599 C C   . GLU A 1 185 ? 11.139  1.133   56.355  1.00 20.64 ? 185 GLU A C   1 
ATOM   1600 O O   . GLU A 1 185 ? 11.118  0.432   55.341  1.00 19.30 ? 185 GLU A O   1 
ATOM   1601 C CB  . GLU A 1 185 ? 11.245  -0.185  58.488  1.00 15.41 ? 185 GLU A CB  1 
ATOM   1602 C CG  . GLU A 1 185 ? 12.100  -0.728  59.633  1.00 15.35 ? 185 GLU A CG  1 
ATOM   1603 C CD  . GLU A 1 185 ? 11.296  -1.114  60.866  1.00 15.76 ? 185 GLU A CD  1 
ATOM   1604 O OE1 . GLU A 1 185 ? 11.943  -1.445  61.890  1.00 15.90 ? 185 GLU A OE1 1 
ATOM   1605 O OE2 . GLU A 1 185 ? 10.037  -1.133  60.800  1.00 16.26 ? 185 GLU A OE2 1 
ATOM   1606 N N   . GLU A 1 186 ? 10.422  2.244   56.455  1.00 15.41 ? 186 GLU A N   1 
ATOM   1607 C CA  . GLU A 1 186 ? 9.563   2.722   55.373  1.00 16.09 ? 186 GLU A CA  1 
ATOM   1608 C C   . GLU A 1 186 ? 10.319  3.525   54.312  1.00 15.65 ? 186 GLU A C   1 
ATOM   1609 O O   . GLU A 1 186 ? 9.693   3.976   53.345  1.00 17.78 ? 186 GLU A O   1 
ATOM   1610 C CB  . GLU A 1 186 ? 8.432   3.593   55.941  1.00 19.24 ? 186 GLU A CB  1 
ATOM   1611 C CG  . GLU A 1 186 ? 7.350   2.785   56.650  1.00 25.60 ? 186 GLU A CG  1 
ATOM   1612 C CD  . GLU A 1 186 ? 6.451   3.634   57.545  1.00 30.75 ? 186 GLU A CD  1 
ATOM   1613 O OE1 . GLU A 1 186 ? 6.774   4.812   57.791  1.00 31.69 ? 186 GLU A OE1 1 
ATOM   1614 O OE2 . GLU A 1 186 ? 5.425   3.111   58.024  1.00 31.57 ? 186 GLU A OE2 1 
ATOM   1615 N N   . GLY A 1 187 ? 11.627  3.701   54.467  1.00 15.90 ? 187 GLY A N   1 
ATOM   1616 C CA  . GLY A 1 187 ? 12.387  4.421   53.462  1.00 16.58 ? 187 GLY A CA  1 
ATOM   1617 C C   . GLY A 1 187 ? 12.168  5.912   53.486  1.00 19.38 ? 187 GLY A C   1 
ATOM   1618 O O   . GLY A 1 187 ? 12.501  6.594   52.507  1.00 15.97 ? 187 GLY A O   1 
ATOM   1619 N N   . LYS A 1 188 ? 11.570  6.435   54.563  1.00 14.05 ? 188 LYS A N   1 
ATOM   1620 C CA  . LYS A 1 188 ? 11.251  7.854   54.632  1.00 14.58 ? 188 LYS A CA  1 
ATOM   1621 C C   . LYS A 1 188 ? 12.401  8.669   55.202  1.00 12.93 ? 188 LYS A C   1 
ATOM   1622 O O   . LYS A 1 188 ? 12.413  9.901   55.064  1.00 12.89 ? 188 LYS A O   1 
ATOM   1623 C CB  . LYS A 1 188 ? 9.972   8.059   55.467  1.00 15.95 ? 188 LYS A CB  1 
ATOM   1624 C CG  . LYS A 1 188 ? 8.744   7.473   54.820  1.00 15.26 ? 188 LYS A CG  1 
ATOM   1625 C CD  . LYS A 1 188 ? 7.507   7.661   55.690  1.00 21.19 ? 188 LYS A CD  1 
ATOM   1626 C CE  . LYS A 1 188 ? 6.265   7.142   54.970  1.00 30.96 ? 188 LYS A CE  1 
ATOM   1627 N NZ  . LYS A 1 188 ? 5.025   7.809   55.471  1.00 36.35 ? 188 LYS A NZ  1 
ATOM   1628 N N   . GLY A 1 189 ? 13.374  8.019   55.819  1.00 13.33 ? 189 GLY A N   1 
ATOM   1629 C CA  . GLY A 1 189 ? 14.527  8.701   56.348  1.00 12.67 ? 189 GLY A CA  1 
ATOM   1630 C C   . GLY A 1 189 ? 15.593  7.707   56.726  1.00 15.08 ? 189 GLY A C   1 
ATOM   1631 O O   . GLY A 1 189 ? 15.316  6.518   56.938  1.00 15.01 ? 189 GLY A O   1 
ATOM   1632 N N   . SER A 1 190 ? 16.826  8.192   56.750  1.00 11.46 ? 190 SER A N   1 
ATOM   1633 C CA  . SER A 1 190 ? 17.930  7.447   57.325  1.00 15.06 ? 190 SER A CA  1 
ATOM   1634 C C   . SER A 1 190 ? 18.078  7.821   58.792  1.00 13.38 ? 190 SER A C   1 
ATOM   1635 O O   . SER A 1 190 ? 17.775  8.939   59.198  1.00 10.72 ? 190 SER A O   1 
ATOM   1636 C CB  . SER A 1 190 ? 19.230  7.751   56.574  1.00 12.55 ? 190 SER A CB  1 
ATOM   1637 O OG  . SER A 1 190 ? 19.168  7.277   55.236  1.00 17.19 ? 190 SER A OG  1 
ATOM   1638 N N   . VAL A 1 191 ? 18.538  6.878   59.599  1.00 12.54 ? 191 VAL A N   1 
ATOM   1639 C CA  . VAL A 1 191 ? 18.878  7.149   60.989  1.00 10.45 ? 191 VAL A CA  1 
ATOM   1640 C C   . VAL A 1 191 ? 20.357  6.818   61.172  1.00 14.48 ? 191 VAL A C   1 
ATOM   1641 O O   . VAL A 1 191 ? 20.800  5.706   60.846  1.00 16.50 ? 191 VAL A O   1 
ATOM   1642 C CB  . VAL A 1 191 ? 18.013  6.349   61.975  1.00 14.74 ? 191 VAL A CB  1 
ATOM   1643 C CG1 . VAL A 1 191 ? 18.391  6.731   63.430  1.00 15.94 ? 191 VAL A CG1 1 
ATOM   1644 C CG2 . VAL A 1 191 ? 16.524  6.576   61.708  1.00 12.21 ? 191 VAL A CG2 1 
ATOM   1645 N N   . SER A 1 192 ? 21.108  7.782   61.675  1.00 10.48 ? 192 SER A N   1 
ATOM   1646 C CA  . SER A 1 192 ? 22.529  7.663   61.960  1.00 9.27  ? 192 SER A CA  1 
ATOM   1647 C C   . SER A 1 192 ? 22.751  7.660   63.461  1.00 11.53 ? 192 SER A C   1 
ATOM   1648 O O   . SER A 1 192 ? 21.829  7.875   64.254  1.00 10.61 ? 192 SER A O   1 
ATOM   1649 C CB  . SER A 1 192 ? 23.314  8.803   61.313  1.00 10.64 ? 192 SER A CB  1 
ATOM   1650 O OG  . SER A 1 192 ? 22.979  10.014  61.983  1.00 10.66 ? 192 SER A OG  1 
ATOM   1651 N N   . THR A 1 193 ? 23.994  7.388   63.852  1.00 12.48 ? 193 THR A N   1 
ATOM   1652 C CA  . THR A 1 193 ? 24.367  7.609   65.251  1.00 13.65 ? 193 THR A CA  1 
ATOM   1653 C C   . THR A 1 193 ? 25.703  8.354   65.316  1.00 10.96 ? 193 THR A C   1 
ATOM   1654 O O   . THR A 1 193 ? 26.311  8.689   64.289  1.00 11.50 ? 193 THR A O   1 
ATOM   1655 C CB  . THR A 1 193 ? 24.401  6.281   66.033  1.00 13.15 ? 193 THR A CB  1 
ATOM   1656 O OG1 . THR A 1 193 ? 24.423  6.573   67.446  1.00 14.33 ? 193 THR A OG1 1 
ATOM   1657 C CG2 . THR A 1 193 ? 25.629  5.369   65.666  1.00 16.07 ? 193 THR A CG2 1 
ATOM   1658 N N   . SER A 1 194 ? 26.144  8.636   66.550  1.00 11.33 ? 194 SER A N   1 
ATOM   1659 C CA  . SER A 1 194 ? 27.420  9.280   66.839  1.00 13.27 ? 194 SER A CA  1 
ATOM   1660 C C   . SER A 1 194 ? 28.234  8.412   67.776  1.00 13.11 ? 194 SER A C   1 
ATOM   1661 O O   . SER A 1 194 ? 27.678  7.570   68.485  1.00 12.64 ? 194 SER A O   1 
ATOM   1662 C CB  . SER A 1 194 ? 27.217  10.646  67.520  1.00 13.13 ? 194 SER A CB  1 
ATOM   1663 O OG  . SER A 1 194 ? 26.592  11.590  66.669  1.00 12.56 ? 194 SER A OG  1 
ATOM   1664 N N   . PRO A 1 195 ? 29.551  8.617   67.838  1.00 11.28 ? 195 PRO A N   1 
ATOM   1665 C CA  . PRO A 1 195 ? 30.342  8.000   68.910  1.00 11.47 ? 195 PRO A CA  1 
ATOM   1666 C C   . PRO A 1 195 ? 29.641  8.194   70.248  1.00 11.92 ? 195 PRO A C   1 
ATOM   1667 O O   . PRO A 1 195 ? 29.071  9.259   70.519  1.00 13.01 ? 195 PRO A O   1 
ATOM   1668 C CB  . PRO A 1 195 ? 31.676  8.751   68.852  1.00 19.24 ? 195 PRO A CB  1 
ATOM   1669 C CG  . PRO A 1 195 ? 31.735  9.343   67.479  1.00 25.03 ? 195 PRO A CG  1 
ATOM   1670 C CD  . PRO A 1 195 ? 30.347  9.447   66.917  1.00 14.73 ? 195 PRO A CD  1 
ATOM   1671 N N   . TYR A 1 196 ? 29.721  7.158   71.096  1.00 12.75 ? 196 TYR A N   1 
ATOM   1672 C CA  . TYR A 1 196 ? 28.677  6.842   72.069  1.00 9.45  ? 196 TYR A CA  1 
ATOM   1673 C C   . TYR A 1 196 ? 28.275  8.012   72.958  1.00 9.32  ? 196 TYR A C   1 
ATOM   1674 O O   . TYR A 1 196 ? 27.079  8.275   73.124  1.00 11.20 ? 196 TYR A O   1 
ATOM   1675 C CB  . TYR A 1 196 ? 29.126  5.658   72.934  1.00 14.25 ? 196 TYR A CB  1 
ATOM   1676 C CG  . TYR A 1 196 ? 28.003  4.875   73.581  1.00 10.32 ? 196 TYR A CG  1 
ATOM   1677 C CD1 . TYR A 1 196 ? 27.322  5.373   74.696  1.00 11.05 ? 196 TYR A CD1 1 
ATOM   1678 C CD2 . TYR A 1 196 ? 27.650  3.617   73.102  1.00 13.19 ? 196 TYR A CD2 1 
ATOM   1679 C CE1 . TYR A 1 196 ? 26.294  4.650   75.295  1.00 13.11 ? 196 TYR A CE1 1 
ATOM   1680 C CE2 . TYR A 1 196 ? 26.619  2.894   73.679  1.00 13.06 ? 196 TYR A CE2 1 
ATOM   1681 C CZ  . TYR A 1 196 ? 25.959  3.404   74.784  1.00 13.93 ? 196 TYR A CZ  1 
ATOM   1682 O OH  . TYR A 1 196 ? 24.961  2.658   75.368  1.00 16.66 ? 196 TYR A OH  1 
ATOM   1683 N N   . TYR A 1 197 ? 29.226  8.630   73.660  1.00 11.73 ? 197 TYR A N   1 
ATOM   1684 C CA  . TYR A 1 197 ? 28.841  9.677   74.605  1.00 9.68  ? 197 TYR A CA  1 
ATOM   1685 C C   . TYR A 1 197 ? 29.046  11.071  74.039  1.00 11.37 ? 197 TYR A C   1 
ATOM   1686 O O   . TYR A 1 197 ? 29.164  12.032  74.811  1.00 13.82 ? 197 TYR A O   1 
ATOM   1687 C CB  . TYR A 1 197 ? 29.583  9.517   75.939  1.00 12.79 ? 197 TYR A CB  1 
ATOM   1688 C CG  . TYR A 1 197 ? 29.134  8.266   76.657  1.00 11.26 ? 197 TYR A CG  1 
ATOM   1689 C CD1 . TYR A 1 197 ? 27.914  8.240   77.353  1.00 10.80 ? 197 TYR A CD1 1 
ATOM   1690 C CD2 . TYR A 1 197 ? 29.866  7.080   76.565  1.00 16.62 ? 197 TYR A CD2 1 
ATOM   1691 C CE1 . TYR A 1 197 ? 27.471  7.078   77.976  1.00 13.71 ? 197 TYR A CE1 1 
ATOM   1692 C CE2 . TYR A 1 197 ? 29.427  5.923   77.203  1.00 16.60 ? 197 TYR A CE2 1 
ATOM   1693 C CZ  . TYR A 1 197 ? 28.234  5.937   77.878  1.00 15.26 ? 197 TYR A CZ  1 
ATOM   1694 O OH  . TYR A 1 197 ? 27.788  4.798   78.502  1.00 20.06 ? 197 TYR A OH  1 
ATOM   1695 N N   . HIS A 1 198 ? 29.050  11.201  72.718  1.00 11.48 ? 198 HIS A N   1 
ATOM   1696 C CA  . HIS A 1 198 ? 29.182  12.508  72.064  1.00 11.70 ? 198 HIS A CA  1 
ATOM   1697 C C   . HIS A 1 198 ? 30.470  13.235  72.465  1.00 12.54 ? 198 HIS A C   1 
ATOM   1698 O O   . HIS A 1 198 ? 30.423  14.398  72.882  1.00 11.34 ? 198 HIS A O   1 
ATOM   1699 C CB  . HIS A 1 198 ? 27.940  13.350  72.411  1.00 11.02 ? 198 HIS A CB  1 
ATOM   1700 C CG  . HIS A 1 198 ? 27.670  14.509  71.489  1.00 9.70  ? 198 HIS A CG  1 
ATOM   1701 N ND1 . HIS A 1 198 ? 28.073  15.792  71.787  1.00 10.71 ? 198 HIS A ND1 1 
ATOM   1702 C CD2 . HIS A 1 198 ? 26.944  14.599  70.339  1.00 11.38 ? 198 HIS A CD2 1 
ATOM   1703 C CE1 . HIS A 1 198 ? 27.657  16.618  70.841  1.00 13.44 ? 198 HIS A CE1 1 
ATOM   1704 N NE2 . HIS A 1 198 ? 26.941  15.930  69.968  1.00 12.05 ? 198 HIS A NE2 1 
ATOM   1705 N N   . PRO A 1 199 ? 31.632  12.610  72.365  1.00 10.74 ? 199 PRO A N   1 
ATOM   1706 C CA  . PRO A 1 199 ? 32.890  13.304  72.681  1.00 16.90 ? 199 PRO A CA  1 
ATOM   1707 C C   . PRO A 1 199 ? 33.428  14.130  71.508  1.00 16.86 ? 199 PRO A C   1 
ATOM   1708 O O   . PRO A 1 199 ? 32.940  14.045  70.376  1.00 17.62 ? 199 PRO A O   1 
ATOM   1709 C CB  . PRO A 1 199 ? 33.844  12.146  72.962  1.00 15.34 ? 199 PRO A CB  1 
ATOM   1710 C CG  . PRO A 1 199 ? 33.421  11.126  71.965  1.00 13.55 ? 199 PRO A CG  1 
ATOM   1711 C CD  . PRO A 1 199 ? 31.878  11.216  71.936  1.00 11.57 ? 199 PRO A CD  1 
ATOM   1712 N N   . LEU A 1 200 ? 34.526  14.848  71.774  1.00 17.87 ? 200 LEU A N   1 
ATOM   1713 C CA  . LEU A 1 200 ? 35.319  15.517  70.731  1.00 15.92 ? 200 LEU A CA  1 
ATOM   1714 C C   . LEU A 1 200 ? 36.412  14.562  70.264  1.00 16.69 ? 200 LEU A C   1 
ATOM   1715 O O   . LEU A 1 200 ? 37.521  14.538  70.802  1.00 14.40 ? 200 LEU A O   1 
ATOM   1716 C CB  . LEU A 1 200 ? 35.900  16.820  71.266  1.00 14.30 ? 200 LEU A CB  1 
ATOM   1717 C CG  . LEU A 1 200 ? 34.891  17.966  71.339  1.00 21.77 ? 200 LEU A CG  1 
ATOM   1718 C CD1 . LEU A 1 200 ? 35.403  19.043  72.231  1.00 27.23 ? 200 LEU A CD1 1 
ATOM   1719 C CD2 . LEU A 1 200 ? 34.659  18.503  69.916  1.00 20.81 ? 200 LEU A CD2 1 
ATOM   1720 N N   . ILE A 1 201 ? 36.078  13.745  69.260  1.00 12.00 ? 201 ILE A N   1 
ATOM   1721 C CA  . ILE A 1 201 ? 37.006  12.709  68.798  1.00 12.98 ? 201 ILE A CA  1 
ATOM   1722 C C   . ILE A 1 201 ? 38.355  13.285  68.394  1.00 15.70 ? 201 ILE A C   1 
ATOM   1723 O O   . ILE A 1 201 ? 39.389  12.666  68.712  1.00 16.22 ? 201 ILE A O   1 
ATOM   1724 C CB  . ILE A 1 201 ? 36.359  11.879  67.678  1.00 14.56 ? 201 ILE A CB  1 
ATOM   1725 C CG1 . ILE A 1 201 ? 35.127  11.107  68.203  1.00 15.96 ? 201 ILE A CG1 1 
ATOM   1726 C CG2 . ILE A 1 201 ? 37.373  10.933  67.058  1.00 14.85 ? 201 ILE A CG2 1 
ATOM   1727 C CD1 . ILE A 1 201 ? 35.449  9.863   69.043  1.00 15.25 ? 201 ILE A CD1 1 
ATOM   1728 N N   . PRO A 1 202 ? 38.443  14.421  67.691  1.00 12.69 ? 202 PRO A N   1 
ATOM   1729 C CA  . PRO A 1 202 ? 39.783  14.882  67.283  1.00 13.03 ? 202 PRO A CA  1 
ATOM   1730 C C   . PRO A 1 202 ? 40.704  15.156  68.458  1.00 13.55 ? 202 PRO A C   1 
ATOM   1731 O O   . PRO A 1 202 ? 41.918  14.890  68.373  1.00 16.66 ? 202 PRO A O   1 
ATOM   1732 C CB  . PRO A 1 202 ? 39.484  16.156  66.485  1.00 13.24 ? 202 PRO A CB  1 
ATOM   1733 C CG  . PRO A 1 202 ? 38.117  15.871  65.862  1.00 15.81 ? 202 PRO A CG  1 
ATOM   1734 C CD  . PRO A 1 202 ? 37.365  15.113  66.945  1.00 13.94 ? 202 PRO A CD  1 
ATOM   1735 N N   . ILE A 1 203 ? 40.163  15.695  69.549  1.00 14.08 ? 203 ILE A N   1 
ATOM   1736 C CA  . ILE A 1 203 ? 40.991  15.946  70.726  1.00 12.87 ? 203 ILE A CA  1 
ATOM   1737 C C   . ILE A 1 203 ? 41.429  14.640  71.371  1.00 16.82 ? 203 ILE A C   1 
ATOM   1738 O O   . ILE A 1 203 ? 42.599  14.491  71.750  1.00 16.68 ? 203 ILE A O   1 
ATOM   1739 C CB  . ILE A 1 203 ? 40.258  16.855  71.722  1.00 16.17 ? 203 ILE A CB  1 
ATOM   1740 C CG1 . ILE A 1 203 ? 40.164  18.266  71.142  1.00 20.17 ? 203 ILE A CG1 1 
ATOM   1741 C CG2 . ILE A 1 203 ? 41.056  16.904  73.042  1.00 17.60 ? 203 ILE A CG2 1 
ATOM   1742 C CD1 . ILE A 1 203 ? 39.308  19.196  71.990  1.00 20.82 ? 203 ILE A CD1 1 
ATOM   1743 N N   . LEU A 1 204 ? 40.514  13.664  71.485  1.00 14.01 ? 204 LEU A N   1 
ATOM   1744 C CA  . LEU A 1 204 ? 40.891  12.372  72.058  1.00 15.33 ? 204 LEU A CA  1 
ATOM   1745 C C   . LEU A 1 204 ? 41.998  11.707  71.244  1.00 15.30 ? 204 LEU A C   1 
ATOM   1746 O O   . LEU A 1 204 ? 42.904  11.082  71.807  1.00 15.52 ? 204 LEU A O   1 
ATOM   1747 C CB  . LEU A 1 204 ? 39.680  11.443  72.154  1.00 12.17 ? 204 LEU A CB  1 
ATOM   1748 C CG  . LEU A 1 204 ? 38.504  11.873  73.031  1.00 13.87 ? 204 LEU A CG  1 
ATOM   1749 C CD1 . LEU A 1 204 ? 37.470  10.724  73.039  1.00 15.15 ? 204 LEU A CD1 1 
ATOM   1750 C CD2 . LEU A 1 204 ? 38.950  12.224  74.446  1.00 15.00 ? 204 LEU A CD2 1 
ATOM   1751 N N   . LEU A 1 205 ? 41.961  11.853  69.920  1.00 15.58 ? 205 LEU A N   1 
ATOM   1752 C CA  . LEU A 1 205 ? 42.978  11.220  69.089  1.00 15.23 ? 205 LEU A CA  1 
ATOM   1753 C C   . LEU A 1 205 ? 44.302  11.969  69.128  1.00 16.45 ? 205 LEU A C   1 
ATOM   1754 O O   . LEU A 1 205 ? 45.374  11.355  69.046  1.00 22.01 ? 205 LEU A O   1 
ATOM   1755 C CB  . LEU A 1 205 ? 42.479  11.131  67.647  1.00 16.29 ? 205 LEU A CB  1 
ATOM   1756 C CG  . LEU A 1 205 ? 41.374  10.102  67.419  1.00 17.21 ? 205 LEU A CG  1 
ATOM   1757 C CD1 . LEU A 1 205 ? 40.837  10.276  66.012  1.00 16.02 ? 205 LEU A CD1 1 
ATOM   1758 C CD2 . LEU A 1 205 ? 41.910  8.676   67.611  1.00 17.52 ? 205 LEU A CD2 1 
ATOM   1759 N N   . ASN A 1 206 ? 44.249  13.293  69.177  1.00 16.53 ? 206 ASN A N   1 
ATOM   1760 C CA  . ASN A 1 206 ? 45.470  14.073  69.033  1.00 17.77 ? 206 ASN A CA  1 
ATOM   1761 C C   . ASN A 1 206 ? 45.201  15.464  69.578  1.00 19.43 ? 206 ASN A C   1 
ATOM   1762 O O   . ASN A 1 206 ? 44.794  16.353  68.818  1.00 18.44 ? 206 ASN A O   1 
ATOM   1763 C CB  . ASN A 1 206 ? 45.908  14.145  67.568  1.00 20.90 ? 206 ASN A CB  1 
ATOM   1764 C CG  . ASN A 1 206 ? 47.172  14.943  67.390  1.00 28.57 ? 206 ASN A CG  1 
ATOM   1765 O OD1 . ASN A 1 206 ? 47.855  15.253  68.366  1.00 25.53 ? 206 ASN A OD1 1 
ATOM   1766 N ND2 . ASN A 1 206 ? 47.487  15.299  66.146  1.00 34.28 ? 206 ASN A ND2 1 
ATOM   1767 N N   . PRO A 1 207 ? 45.395  15.693  70.880  1.00 17.96 ? 207 PRO A N   1 
ATOM   1768 C CA  . PRO A 1 207 ? 45.072  17.026  71.432  1.00 17.94 ? 207 PRO A CA  1 
ATOM   1769 C C   . PRO A 1 207 ? 45.799  18.159  70.741  1.00 18.46 ? 207 PRO A C   1 
ATOM   1770 O O   . PRO A 1 207 ? 45.317  19.301  70.767  1.00 20.75 ? 207 PRO A O   1 
ATOM   1771 C CB  . PRO A 1 207 ? 45.510  16.910  72.899  1.00 22.95 ? 207 PRO A CB  1 
ATOM   1772 C CG  . PRO A 1 207 ? 45.395  15.449  73.206  1.00 22.71 ? 207 PRO A CG  1 
ATOM   1773 C CD  . PRO A 1 207 ? 45.755  14.725  71.935  1.00 19.11 ? 207 PRO A CD  1 
ATOM   1774 N N   . ASN A 1 208 ? 46.967  17.889  70.154  1.00 18.83 ? 208 ASN A N   1 
ATOM   1775 C CA  . ASN A 1 208 ? 47.732  18.928  69.467  1.00 19.16 ? 208 ASN A CA  1 
ATOM   1776 C C   . ASN A 1 208 ? 46.991  19.489  68.259  1.00 19.49 ? 208 ASN A C   1 
ATOM   1777 O O   . ASN A 1 208 ? 47.405  20.519  67.713  1.00 18.83 ? 208 ASN A O   1 
ATOM   1778 C CB  . ASN A 1 208 ? 49.100  18.399  69.008  1.00 23.03 ? 208 ASN A CB  1 
ATOM   1779 C CG  . ASN A 1 208 ? 50.164  18.430  70.107  1.00 31.86 ? 208 ASN A CG  1 
ATOM   1780 O OD1 . ASN A 1 208 ? 49.860  18.638  71.277  1.00 34.42 ? 208 ASN A OD1 1 
ATOM   1781 N ND2 . ASN A 1 208 ? 51.421  18.224  69.717  1.00 36.76 ? 208 ASN A ND2 1 
ATOM   1782 N N   . CYS A 1 209 ? 45.904  18.862  67.838  1.00 19.65 ? 209 CYS A N   1 
ATOM   1783 C CA  . CYS A 1 209 ? 45.193  19.404  66.688  1.00 24.54 ? 209 CYS A CA  1 
ATOM   1784 C C   . CYS A 1 209 ? 44.512  20.736  67.000  1.00 23.69 ? 209 CYS A C   1 
ATOM   1785 O O   . CYS A 1 209 ? 44.160  21.456  66.066  1.00 20.17 ? 209 CYS A O   1 
ATOM   1786 C CB  . CYS A 1 209 ? 44.174  18.386  66.172  1.00 23.33 ? 209 CYS A CB  1 
ATOM   1787 S SG  . CYS A 1 209 ? 42.675  18.195  67.159  1.00 23.82 ? 209 CYS A SG  1 
ATOM   1788 N N   . VAL A 1 210 ? 44.380  21.104  68.279  1.00 16.86 ? 210 VAL A N   1 
ATOM   1789 C CA  . VAL A 1 210 ? 43.795  22.397  68.640  1.00 21.06 ? 210 VAL A CA  1 
ATOM   1790 C C   . VAL A 1 210 ? 44.651  23.556  68.134  1.00 21.37 ? 210 VAL A C   1 
ATOM   1791 O O   . VAL A 1 210 ? 44.135  24.654  67.874  1.00 21.14 ? 210 VAL A O   1 
ATOM   1792 C CB  . VAL A 1 210 ? 43.568  22.452  70.167  1.00 25.09 ? 210 VAL A CB  1 
ATOM   1793 C CG1 . VAL A 1 210 ? 43.052  23.800  70.597  1.00 30.49 ? 210 VAL A CG1 1 
ATOM   1794 C CG2 . VAL A 1 210 ? 42.600  21.369  70.587  1.00 27.59 ? 210 VAL A CG2 1 
ATOM   1795 N N   . TYR A 1 211 ? 45.957  23.331  67.930  1.00 18.68 ? 211 TYR A N   1 
ATOM   1796 C CA  . TYR A 1 211 ? 46.846  24.400  67.492  1.00 21.48 ? 211 TYR A CA  1 
ATOM   1797 C C   . TYR A 1 211 ? 46.704  24.724  66.004  1.00 19.79 ? 211 TYR A C   1 
ATOM   1798 O O   . TYR A 1 211 ? 47.266  25.721  65.538  1.00 25.38 ? 211 TYR A O   1 
ATOM   1799 C CB  . TYR A 1 211 ? 48.297  24.020  67.790  1.00 20.29 ? 211 TYR A CB  1 
ATOM   1800 C CG  . TYR A 1 211 ? 48.619  23.782  69.254  1.00 22.02 ? 211 TYR A CG  1 
ATOM   1801 C CD1 . TYR A 1 211 ? 48.555  24.820  70.188  1.00 23.09 ? 211 TYR A CD1 1 
ATOM   1802 C CD2 . TYR A 1 211 ? 49.048  22.538  69.691  1.00 23.99 ? 211 TYR A CD2 1 
ATOM   1803 C CE1 . TYR A 1 211 ? 48.888  24.606  71.528  1.00 25.46 ? 211 TYR A CE1 1 
ATOM   1804 C CE2 . TYR A 1 211 ? 49.376  22.315  71.030  1.00 23.44 ? 211 TYR A CE2 1 
ATOM   1805 C CZ  . TYR A 1 211 ? 49.282  23.349  71.941  1.00 26.89 ? 211 TYR A CZ  1 
ATOM   1806 O OH  . TYR A 1 211 ? 49.619  23.123  73.267  1.00 26.57 ? 211 TYR A OH  1 
ATOM   1807 N N   . GLU A 1 212 ? 45.967  23.911  65.255  1.00 20.12 ? 212 GLU A N   1 
ATOM   1808 C CA  . GLU A 1 212 ? 45.806  24.154  63.825  1.00 24.01 ? 212 GLU A CA  1 
ATOM   1809 C C   . GLU A 1 212 ? 44.994  25.418  63.558  1.00 23.94 ? 212 GLU A C   1 
ATOM   1810 O O   . GLU A 1 212 ? 45.339  26.196  62.660  1.00 25.64 ? 212 GLU A O   1 
ATOM   1811 C CB  . GLU A 1 212 ? 45.172  22.926  63.166  1.00 26.44 ? 212 GLU A CB  1 
ATOM   1812 C CG  . GLU A 1 212 ? 46.136  21.738  63.078  1.00 28.88 ? 212 GLU A CG  1 
ATOM   1813 C CD  . GLU A 1 212 ? 45.472  20.430  62.662  1.00 32.37 ? 212 GLU A CD  1 
ATOM   1814 O OE1 . GLU A 1 212 ? 45.995  19.362  63.044  1.00 35.59 ? 212 GLU A OE1 1 
ATOM   1815 O OE2 . GLU A 1 212 ? 44.444  20.459  61.947  1.00 28.54 ? 212 GLU A OE2 1 
ATOM   1816 N N   . THR A 1 213 ? 43.931  25.655  64.341  1.00 21.05 ? 213 THR A N   1 
ATOM   1817 C CA  . THR A 1 213 ? 43.125  26.873  64.220  1.00 22.25 ? 213 THR A CA  1 
ATOM   1818 C C   . THR A 1 213 ? 43.430  27.916  65.289  1.00 26.83 ? 213 THR A C   1 
ATOM   1819 O O   . THR A 1 213 ? 43.289  29.116  65.025  1.00 29.46 ? 213 THR A O   1 
ATOM   1820 C CB  . THR A 1 213 ? 41.629  26.537  64.285  1.00 21.74 ? 213 THR A CB  1 
ATOM   1821 O OG1 . THR A 1 213 ? 41.390  25.738  65.447  1.00 31.55 ? 213 THR A OG1 1 
ATOM   1822 C CG2 . THR A 1 213 ? 41.215  25.771  63.048  1.00 23.81 ? 213 THR A CG2 1 
ATOM   1823 N N   . THR A 1 214 ? 43.855  27.507  66.488  1.00 19.90 ? 214 THR A N   1 
ATOM   1824 C CA  . THR A 1 214 ? 44.169  28.447  67.569  1.00 19.93 ? 214 THR A CA  1 
ATOM   1825 C C   . THR A 1 214 ? 45.581  28.160  68.048  1.00 25.91 ? 214 THR A C   1 
ATOM   1826 O O   . THR A 1 214 ? 45.787  27.513  69.082  1.00 24.82 ? 214 THR A O   1 
ATOM   1827 C CB  . THR A 1 214 ? 43.148  28.339  68.704  1.00 21.06 ? 214 THR A CB  1 
ATOM   1828 O OG1 . THR A 1 214 ? 43.029  26.971  69.139  1.00 22.77 ? 214 THR A OG1 1 
ATOM   1829 C CG2 . THR A 1 214 ? 41.775  28.812  68.213  1.00 22.97 ? 214 THR A CG2 1 
ATOM   1830 N N   . PRO A 1 215 ? 46.589  28.631  67.310  1.00 23.59 ? 215 PRO A N   1 
ATOM   1831 C CA  . PRO A 1 215 ? 47.980  28.271  67.644  1.00 23.67 ? 215 PRO A CA  1 
ATOM   1832 C C   . PRO A 1 215 ? 48.453  28.813  68.973  1.00 28.14 ? 215 PRO A C   1 
ATOM   1833 O O   . PRO A 1 215 ? 49.424  28.278  69.525  1.00 30.30 ? 215 PRO A O   1 
ATOM   1834 C CB  . PRO A 1 215 ? 48.785  28.872  66.485  1.00 26.23 ? 215 PRO A CB  1 
ATOM   1835 C CG  . PRO A 1 215 ? 47.907  29.976  65.940  1.00 28.79 ? 215 PRO A CG  1 
ATOM   1836 C CD  . PRO A 1 215 ? 46.496  29.512  66.128  1.00 28.07 ? 215 PRO A CD  1 
ATOM   1837 N N   . ASN A 1 216 ? 47.821  29.862  69.494  1.00 28.12 ? 216 ASN A N   1 
ATOM   1838 C CA  . ASN A 1 216 ? 48.253  30.518  70.719  1.00 34.01 ? 216 ASN A CA  1 
ATOM   1839 C C   . ASN A 1 216 ? 47.489  30.032  71.943  1.00 31.38 ? 216 ASN A C   1 
ATOM   1840 O O   . ASN A 1 216 ? 47.668  30.585  73.033  1.00 40.59 ? 216 ASN A O   1 
ATOM   1841 C CB  . ASN A 1 216 ? 48.099  32.037  70.590  1.00 34.28 ? 216 ASN A CB  1 
ATOM   1842 C CG  . ASN A 1 216 ? 48.984  32.627  69.513  1.00 41.54 ? 216 ASN A CG  1 
ATOM   1843 O OD1 . ASN A 1 216 ? 50.122  32.196  69.316  1.00 45.64 ? 216 ASN A OD1 1 
ATOM   1844 N ND2 . ASN A 1 216 ? 48.467  33.626  68.813  1.00 44.67 ? 216 ASN A ND2 1 
ATOM   1845 N N   . VAL A 1 217 ? 46.646  29.018  71.792  1.00 32.90 ? 217 VAL A N   1 
ATOM   1846 C CA  . VAL A 1 217 ? 45.856  28.546  72.918  1.00 30.50 ? 217 VAL A CA  1 
ATOM   1847 C C   . VAL A 1 217 ? 46.762  27.804  73.891  1.00 29.86 ? 217 VAL A C   1 
ATOM   1848 O O   . VAL A 1 217 ? 47.838  27.310  73.523  1.00 27.88 ? 217 VAL A O   1 
ATOM   1849 C CB  . VAL A 1 217 ? 44.700  27.657  72.420  1.00 29.21 ? 217 VAL A CB  1 
ATOM   1850 C CG1 . VAL A 1 217 ? 45.216  26.311  71.953  1.00 25.48 ? 217 VAL A CG1 1 
ATOM   1851 C CG2 . VAL A 1 217 ? 43.653  27.492  73.498  1.00 34.20 ? 217 VAL A CG2 1 
ATOM   1852 N N   . LYS A 1 218 ? 46.354  27.775  75.159  1.00 25.55 ? 218 LYS A N   1 
ATOM   1853 C CA  . LYS A 1 218 ? 47.038  27.037  76.207  1.00 24.97 ? 218 LYS A CA  1 
ATOM   1854 C C   . LYS A 1 218 ? 46.133  25.892  76.633  1.00 25.77 ? 218 LYS A C   1 
ATOM   1855 O O   . LYS A 1 218 ? 44.962  26.107  76.974  1.00 24.24 ? 218 LYS A O   1 
ATOM   1856 C CB  . LYS A 1 218 ? 47.378  27.933  77.398  1.00 31.79 ? 218 LYS A CB  1 
ATOM   1857 C CG  . LYS A 1 218 ? 48.852  28.332  77.478  1.00 44.60 ? 218 LYS A CG  1 
ATOM   1858 C CD  . LYS A 1 218 ? 49.323  28.956  76.170  1.00 52.99 ? 218 LYS A CD  1 
ATOM   1859 C CE  . LYS A 1 218 ? 50.736  29.507  76.268  1.00 59.07 ? 218 LYS A CE  1 
ATOM   1860 N NZ  . LYS A 1 218 ? 51.205  29.982  74.929  1.00 61.97 ? 218 LYS A NZ  1 
ATOM   1861 N N   . ILE A 1 219 ? 46.663  24.678  76.578  1.00 25.90 ? 219 ILE A N   1 
ATOM   1862 C CA  . ILE A 1 219 ? 45.885  23.496  76.945  1.00 23.60 ? 219 ILE A CA  1 
ATOM   1863 C C   . ILE A 1 219 ? 46.681  22.721  77.984  1.00 22.68 ? 219 ILE A C   1 
ATOM   1864 O O   . ILE A 1 219 ? 47.879  22.975  78.177  1.00 23.62 ? 219 ILE A O   1 
ATOM   1865 C CB  . ILE A 1 219 ? 45.557  22.628  75.710  1.00 23.14 ? 219 ILE A CB  1 
ATOM   1866 C CG1 . ILE A 1 219 ? 46.824  22.068  75.065  1.00 28.12 ? 219 ILE A CG1 1 
ATOM   1867 C CG2 . ILE A 1 219 ? 44.714  23.422  74.693  1.00 23.87 ? 219 ILE A CG2 1 
ATOM   1868 C CD1 . ILE A 1 219 ? 46.493  20.935  74.098  1.00 26.13 ? 219 ILE A CD1 1 
ATOM   1869 N N   . PRO A 1 220 ? 46.041  21.795  78.707  1.00 25.19 ? 220 PRO A N   1 
ATOM   1870 C CA  . PRO A 1 220 ? 46.791  21.056  79.731  1.00 24.36 ? 220 PRO A CA  1 
ATOM   1871 C C   . PRO A 1 220 ? 47.744  20.034  79.138  1.00 23.69 ? 220 PRO A C   1 
ATOM   1872 O O   . PRO A 1 220 ? 47.804  19.824  77.923  1.00 23.21 ? 220 PRO A O   1 
ATOM   1873 C CB  . PRO A 1 220 ? 45.703  20.395  80.592  1.00 25.27 ? 220 PRO A CB  1 
ATOM   1874 C CG  . PRO A 1 220 ? 44.440  20.554  79.864  1.00 25.21 ? 220 PRO A CG  1 
ATOM   1875 C CD  . PRO A 1 220 ? 44.583  21.643  78.858  1.00 26.69 ? 220 PRO A CD  1 
ATOM   1876 N N   . ASP A 1 221 ? 48.512  19.415  80.020  1.00 23.86 ? 221 ASP A N   1 
ATOM   1877 C CA  . ASP A 1 221 ? 49.466  18.389  79.631  1.00 29.12 ? 221 ASP A CA  1 
ATOM   1878 C C   . ASP A 1 221 ? 48.711  17.073  79.494  1.00 31.50 ? 221 ASP A C   1 
ATOM   1879 O O   . ASP A 1 221 ? 48.320  16.457  80.492  1.00 34.27 ? 221 ASP A O   1 
ATOM   1880 C CB  . ASP A 1 221 ? 50.579  18.312  80.670  1.00 29.71 ? 221 ASP A CB  1 
ATOM   1881 C CG  . ASP A 1 221 ? 51.381  17.027  80.578  1.00 48.39 ? 221 ASP A CG  1 
ATOM   1882 O OD1 . ASP A 1 221 ? 51.608  16.543  79.446  1.00 51.29 ? 221 ASP A OD1 1 
ATOM   1883 O OD2 . ASP A 1 221 ? 51.807  16.517  81.640  1.00 50.44 ? 221 ASP A OD2 1 
ATOM   1884 N N   . PHE A 1 222 ? 48.486  16.647  78.255  1.00 24.90 ? 222 PHE A N   1 
ATOM   1885 C CA  . PHE A 1 222 ? 47.837  15.371  77.972  1.00 21.70 ? 222 PHE A CA  1 
ATOM   1886 C C   . PHE A 1 222 ? 48.851  14.234  78.105  1.00 26.48 ? 222 PHE A C   1 
ATOM   1887 O O   . PHE A 1 222 ? 49.308  13.631  77.131  1.00 24.56 ? 222 PHE A O   1 
ATOM   1888 C CB  . PHE A 1 222 ? 47.199  15.407  76.590  1.00 18.20 ? 222 PHE A CB  1 
ATOM   1889 C CG  . PHE A 1 222 ? 45.887  16.155  76.547  1.00 18.64 ? 222 PHE A CG  1 
ATOM   1890 C CD1 . PHE A 1 222 ? 45.854  17.554  76.495  1.00 20.67 ? 222 PHE A CD1 1 
ATOM   1891 C CD2 . PHE A 1 222 ? 44.693  15.465  76.567  1.00 21.87 ? 222 PHE A CD2 1 
ATOM   1892 C CE1 . PHE A 1 222 ? 44.636  18.238  76.463  1.00 19.23 ? 222 PHE A CE1 1 
ATOM   1893 C CE2 . PHE A 1 222 ? 43.481  16.135  76.527  1.00 18.48 ? 222 PHE A CE2 1 
ATOM   1894 C CZ  . PHE A 1 222 ? 43.448  17.524  76.467  1.00 21.51 ? 222 PHE A CZ  1 
ATOM   1895 N N   . ALA A 1 223 ? 49.182  13.926  79.354  1.00 25.31 ? 223 ALA A N   1 
ATOM   1896 C CA  . ALA A 1 223 ? 50.199  12.942  79.696  1.00 27.36 ? 223 ALA A CA  1 
ATOM   1897 C C   . ALA A 1 223 ? 49.682  11.504  79.669  1.00 25.68 ? 223 ALA A C   1 
ATOM   1898 O O   . ALA A 1 223 ? 50.318  10.622  80.248  1.00 30.43 ? 223 ALA A O   1 
ATOM   1899 C CB  . ALA A 1 223 ? 50.785  13.253  81.078  1.00 26.14 ? 223 ALA A CB  1 
ATOM   1900 N N   . VAL A 1 224 ? 48.555  11.245  79.012  1.00 23.36 ? 224 VAL A N   1 
ATOM   1901 C CA  . VAL A 1 224 ? 48.012  9.894   78.868  1.00 20.68 ? 224 VAL A CA  1 
ATOM   1902 C C   . VAL A 1 224 ? 47.353  9.835   77.497  1.00 19.30 ? 224 VAL A C   1 
ATOM   1903 O O   . VAL A 1 224 ? 46.960  10.861  76.947  1.00 23.10 ? 224 VAL A O   1 
ATOM   1904 C CB  . VAL A 1 224 ? 46.990  9.564   79.989  1.00 26.41 ? 224 VAL A CB  1 
ATOM   1905 C CG1 . VAL A 1 224 ? 45.719  10.361  79.793  1.00 29.79 ? 224 VAL A CG1 1 
ATOM   1906 C CG2 . VAL A 1 224 ? 46.702  8.081   80.045  1.00 31.38 ? 224 VAL A CG2 1 
ATOM   1907 N N   . SER A 1 225 ? 47.251  8.638   76.926  1.00 18.20 ? 225 SER A N   1 
ATOM   1908 C CA  . SER A 1 225 ? 46.615  8.505   75.620  1.00 18.73 ? 225 SER A CA  1 
ATOM   1909 C C   . SER A 1 225 ? 45.113  8.303   75.754  1.00 19.16 ? 225 SER A C   1 
ATOM   1910 O O   . SER A 1 225 ? 44.667  7.482   76.557  1.00 19.20 ? 225 SER A O   1 
ATOM   1911 C CB  . SER A 1 225 ? 47.215  7.328   74.857  1.00 18.97 ? 225 SER A CB  1 
ATOM   1912 O OG  . SER A 1 225 ? 46.547  7.177   73.617  1.00 19.47 ? 225 SER A OG  1 
ATOM   1913 N N   . PHE A 1 226 ? 44.347  9.031   74.939  1.00 15.60 ? 226 PHE A N   1 
ATOM   1914 C CA  . PHE A 1 226 ? 42.910  8.830   74.796  1.00 15.86 ? 226 PHE A CA  1 
ATOM   1915 C C   . PHE A 1 226 ? 42.564  8.170   73.468  1.00 18.18 ? 226 PHE A C   1 
ATOM   1916 O O   . PHE A 1 226 ? 41.387  8.099   73.114  1.00 17.42 ? 226 PHE A O   1 
ATOM   1917 C CB  . PHE A 1 226 ? 42.173  10.163  74.912  1.00 15.75 ? 226 PHE A CB  1 
ATOM   1918 C CG  . PHE A 1 226 ? 42.132  10.733  76.301  1.00 17.63 ? 226 PHE A CG  1 
ATOM   1919 C CD1 . PHE A 1 226 ? 41.183  10.300  77.224  1.00 16.32 ? 226 PHE A CD1 1 
ATOM   1920 C CD2 . PHE A 1 226 ? 43.019  11.734  76.671  1.00 22.20 ? 226 PHE A CD2 1 
ATOM   1921 C CE1 . PHE A 1 226 ? 41.123  10.853  78.500  1.00 22.46 ? 226 PHE A CE1 1 
ATOM   1922 C CE2 . PHE A 1 226 ? 42.981  12.279  77.965  1.00 28.36 ? 226 PHE A CE2 1 
ATOM   1923 C CZ  . PHE A 1 226 ? 42.027  11.828  78.875  1.00 21.00 ? 226 PHE A CZ  1 
ATOM   1924 N N   . ARG A 1 227 ? 43.569  7.692   72.717  1.00 16.17 ? 227 ARG A N   1 
ATOM   1925 C CA  . ARG A 1 227 ? 43.285  7.199   71.368  1.00 15.74 ? 227 ARG A CA  1 
ATOM   1926 C C   . ARG A 1 227 ? 42.415  5.940   71.395  1.00 18.07 ? 227 ARG A C   1 
ATOM   1927 O O   . ARG A 1 227 ? 41.514  5.784   70.552  1.00 17.29 ? 227 ARG A O   1 
ATOM   1928 C CB  . ARG A 1 227 ? 44.594  6.947   70.613  1.00 19.40 ? 227 ARG A CB  1 
ATOM   1929 C CG  . ARG A 1 227 ? 45.386  8.220   70.337  1.00 25.77 ? 227 ARG A CG  1 
ATOM   1930 C CD  . ARG A 1 227 ? 46.682  7.914   69.567  1.00 28.83 ? 227 ARG A CD  1 
ATOM   1931 N NE  . ARG A 1 227 ? 46.421  7.236   68.298  1.00 32.68 ? 227 ARG A NE  1 
ATOM   1932 C CZ  . ARG A 1 227 ? 46.130  7.846   67.146  1.00 37.36 ? 227 ARG A CZ  1 
ATOM   1933 N NH1 . ARG A 1 227 ? 46.063  9.168   67.075  1.00 32.42 ? 227 ARG A NH1 1 
ATOM   1934 N NH2 . ARG A 1 227 ? 45.920  7.125   66.047  1.00 43.77 ? 227 ARG A NH2 1 
ATOM   1935 N N   . GLU A 1 228 ? 42.660  5.036   72.349  1.00 18.84 ? 228 GLU A N   1 
ATOM   1936 C CA  . GLU A 1 228 ? 41.830  3.840   72.447  1.00 19.81 ? 228 GLU A CA  1 
ATOM   1937 C C   . GLU A 1 228 ? 40.400  4.192   72.853  1.00 14.99 ? 228 GLU A C   1 
ATOM   1938 O O   . GLU A 1 228 ? 39.443  3.599   72.338  1.00 18.50 ? 228 GLU A O   1 
ATOM   1939 C CB  . GLU A 1 228 ? 42.442  2.850   73.444  1.00 27.12 ? 228 GLU A CB  1 
ATOM   1940 C CG  . GLU A 1 228 ? 41.841  2.867   74.864  1.00 46.52 ? 228 GLU A CG  1 
ATOM   1941 C CD  . GLU A 1 228 ? 42.558  3.808   75.858  1.00 56.41 ? 228 GLU A CD  1 
ATOM   1942 O OE1 . GLU A 1 228 ? 42.910  4.973   75.505  1.00 55.04 ? 228 GLU A OE1 1 
ATOM   1943 O OE2 . GLU A 1 228 ? 42.765  3.356   77.011  1.00 54.88 ? 228 GLU A OE2 1 
ATOM   1944 N N   . ASP A 1 229 ? 40.233  5.192   73.734  1.00 16.52 ? 229 ASP A N   1 
ATOM   1945 C CA  . ASP A 1 229 ? 38.891  5.644   74.100  1.00 14.52 ? 229 ASP A CA  1 
ATOM   1946 C C   . ASP A 1 229 ? 38.144  6.180   72.887  1.00 14.98 ? 229 ASP A C   1 
ATOM   1947 O O   . ASP A 1 229 ? 36.940  5.929   72.729  1.00 14.24 ? 229 ASP A O   1 
ATOM   1948 C CB  . ASP A 1 229 ? 38.986  6.710   75.194  1.00 14.86 ? 229 ASP A CB  1 
ATOM   1949 C CG  . ASP A 1 229 ? 39.187  6.095   76.575  1.00 20.10 ? 229 ASP A CG  1 
ATOM   1950 O OD1 . ASP A 1 229 ? 39.233  4.844   76.684  1.00 21.20 ? 229 ASP A OD1 1 
ATOM   1951 O OD2 . ASP A 1 229 ? 39.273  6.850   77.567  1.00 21.10 ? 229 ASP A OD2 1 
ATOM   1952 N N   . ALA A 1 230 ? 38.832  6.929   72.015  1.00 12.70 ? 230 ALA A N   1 
ATOM   1953 C CA  . ALA A 1 230 ? 38.170  7.412   70.804  1.00 11.78 ? 230 ALA A CA  1 
ATOM   1954 C C   . ALA A 1 230 ? 37.615  6.250   69.989  1.00 16.69 ? 230 ALA A C   1 
ATOM   1955 O O   . ALA A 1 230 ? 36.455  6.297   69.534  1.00 15.48 ? 230 ALA A O   1 
ATOM   1956 C CB  . ALA A 1 230 ? 39.148  8.246   69.967  1.00 16.46 ? 230 ALA A CB  1 
ATOM   1957 N N   . SER A 1 231 ? 38.425  5.191   69.818  1.00 15.67 ? 231 SER A N   1 
ATOM   1958 C CA  . SER A 1 231 ? 37.993  4.007   69.068  1.00 12.91 ? 231 SER A CA  1 
ATOM   1959 C C   . SER A 1 231 ? 36.812  3.341   69.759  1.00 17.33 ? 231 SER A C   1 
ATOM   1960 O O   . SER A 1 231 ? 35.844  2.932   69.106  1.00 16.17 ? 231 SER A O   1 
ATOM   1961 C CB  . SER A 1 231 ? 39.135  2.992   68.948  1.00 20.81 ? 231 SER A CB  1 
ATOM   1962 O OG  . SER A 1 231 ? 39.871  3.190   67.774  1.00 34.65 ? 231 SER A OG  1 
ATOM   1963 N N   . LYS A 1 232 ? 36.877  3.243   71.089  1.00 14.98 ? 232 LYS A N   1 
ATOM   1964 C CA  . LYS A 1 232 ? 35.795  2.633   71.862  1.00 18.15 ? 232 LYS A CA  1 
ATOM   1965 C C   . LYS A 1 232 ? 34.483  3.383   71.700  1.00 13.97 ? 232 LYS A C   1 
ATOM   1966 O O   . LYS A 1 232 ? 33.428  2.752   71.595  1.00 16.27 ? 232 LYS A O   1 
ATOM   1967 C CB  . LYS A 1 232 ? 36.157  2.563   73.345  1.00 18.05 ? 232 LYS A CB  1 
ATOM   1968 C CG  . LYS A 1 232 ? 37.042  1.412   73.753  1.00 35.25 ? 232 LYS A CG  1 
ATOM   1969 C CD  . LYS A 1 232 ? 37.009  1.209   75.277  1.00 40.91 ? 232 LYS A CD  1 
ATOM   1970 C CE  . LYS A 1 232 ? 35.706  0.533   75.720  1.00 46.00 ? 232 LYS A CE  1 
ATOM   1971 N NZ  . LYS A 1 232 ? 35.808  -0.117  77.069  1.00 49.12 ? 232 LYS A NZ  1 
ATOM   1972 N N   . HIS A 1 233 ? 34.500  4.733   71.739  1.00 11.10 ? 233 HIS A N   1 
ATOM   1973 C CA  . HIS A 1 233 ? 33.250  5.465   71.513  1.00 12.82 ? 233 HIS A CA  1 
ATOM   1974 C C   . HIS A 1 233 ? 32.632  5.070   70.177  1.00 11.85 ? 233 HIS A C   1 
ATOM   1975 O O   . HIS A 1 233 ? 31.407  4.917   70.064  1.00 12.45 ? 233 HIS A O   1 
ATOM   1976 C CB  . HIS A 1 233 ? 33.463  6.992   71.503  1.00 11.78 ? 233 HIS A CB  1 
ATOM   1977 C CG  . HIS A 1 233 ? 33.645  7.627   72.860  1.00 12.49 ? 233 HIS A CG  1 
ATOM   1978 N ND1 . HIS A 1 233 ? 32.594  8.032   73.662  1.00 14.77 ? 233 HIS A ND1 1 
ATOM   1979 C CD2 . HIS A 1 233 ? 34.774  7.923   73.553  1.00 15.34 ? 233 HIS A CD2 1 
ATOM   1980 C CE1 . HIS A 1 233 ? 33.067  8.576   74.772  1.00 13.15 ? 233 HIS A CE1 1 
ATOM   1981 N NE2 . HIS A 1 233 ? 34.391  8.519   74.731  1.00 13.68 ? 233 HIS A NE2 1 
ATOM   1982 N N   . VAL A 1 234 ? 33.457  4.937   69.139  1.00 11.25 ? 234 VAL A N   1 
ATOM   1983 C CA  . VAL A 1 234 ? 32.901  4.593   67.830  1.00 12.77 ? 234 VAL A CA  1 
ATOM   1984 C C   . VAL A 1 234 ? 32.406  3.148   67.805  1.00 15.86 ? 234 VAL A C   1 
ATOM   1985 O O   . VAL A 1 234 ? 31.308  2.861   67.298  1.00 12.85 ? 234 VAL A O   1 
ATOM   1986 C CB  . VAL A 1 234 ? 33.922  4.864   66.718  1.00 15.09 ? 234 VAL A CB  1 
ATOM   1987 C CG1 . VAL A 1 234 ? 33.321  4.387   65.388  1.00 14.77 ? 234 VAL A CG1 1 
ATOM   1988 C CG2 . VAL A 1 234 ? 34.248  6.372   66.672  1.00 12.67 ? 234 VAL A CG2 1 
ATOM   1989 N N   . GLU A 1 235 ? 33.186  2.234   68.359  1.00 13.96 ? 235 GLU A N   1 
ATOM   1990 C CA  . GLU A 1 235 ? 32.832  0.819   68.336  1.00 12.68 ? 235 GLU A CA  1 
ATOM   1991 C C   . GLU A 1 235 ? 31.577  0.554   69.164  1.00 15.33 ? 235 GLU A C   1 
ATOM   1992 O O   . GLU A 1 235 ? 30.698  -0.206  68.739  1.00 15.62 ? 235 GLU A O   1 
ATOM   1993 C CB  . GLU A 1 235 ? 34.011  -0.021  68.846  1.00 16.84 ? 235 GLU A CB  1 
ATOM   1994 C CG  . GLU A 1 235 ? 33.865  -1.490  68.553  1.00 30.43 ? 235 GLU A CG  1 
ATOM   1995 C CD  . GLU A 1 235 ? 33.468  -1.751  67.110  1.00 42.18 ? 235 GLU A CD  1 
ATOM   1996 O OE1 . GLU A 1 235 ? 34.160  -1.246  66.186  1.00 37.39 ? 235 GLU A OE1 1 
ATOM   1997 O OE2 . GLU A 1 235 ? 32.451  -2.456  66.909  1.00 46.38 ? 235 GLU A OE2 1 
ATOM   1998 N N   . LEU A 1 236 ? 31.478  1.176   70.344  1.00 12.20 ? 236 LEU A N   1 
ATOM   1999 C CA  . LEU A 1 236 ? 30.298  0.970   71.176  1.00 13.82 ? 236 LEU A CA  1 
ATOM   2000 C C   . LEU A 1 236 ? 29.063  1.541   70.500  1.00 14.44 ? 236 LEU A C   1 
ATOM   2001 O O   . LEU A 1 236 ? 27.955  1.002   70.650  1.00 13.10 ? 236 LEU A O   1 
ATOM   2002 C CB  . LEU A 1 236 ? 30.499  1.599   72.551  1.00 13.24 ? 236 LEU A CB  1 
ATOM   2003 C CG  . LEU A 1 236 ? 31.505  0.902   73.485  1.00 13.75 ? 236 LEU A CG  1 
ATOM   2004 C CD1 . LEU A 1 236 ? 31.687  1.707   74.753  1.00 16.94 ? 236 LEU A CD1 1 
ATOM   2005 C CD2 . LEU A 1 236 ? 31.055  -0.509  73.822  1.00 19.66 ? 236 LEU A CD2 1 
ATOM   2006 N N   . ALA A 1 237 ? 29.216  2.658   69.789  1.00 10.73 ? 237 ALA A N   1 
ATOM   2007 C CA  . ALA A 1 237 ? 28.068  3.200   69.057  1.00 10.05 ? 237 ALA A CA  1 
ATOM   2008 C C   . ALA A 1 237 ? 27.619  2.252   67.953  1.00 11.48 ? 237 ALA A C   1 
ATOM   2009 O O   . ALA A 1 237 ? 26.409  2.106   67.705  1.00 11.39 ? 237 ALA A O   1 
ATOM   2010 C CB  . ALA A 1 237 ? 28.393  4.573   68.466  1.00 10.95 ? 237 ALA A CB  1 
ATOM   2011 N N   . LYS A 1 238 ? 28.575  1.657   67.233  1.00 13.91 ? 238 LYS A N   1 
ATOM   2012 C CA  . LYS A 1 238 ? 28.212  0.675   66.212  1.00 12.95 ? 238 LYS A CA  1 
ATOM   2013 C C   . LYS A 1 238 ? 27.437  -0.480  66.831  1.00 16.45 ? 238 LYS A C   1 
ATOM   2014 O O   . LYS A 1 238 ? 26.439  -0.948  66.256  1.00 16.06 ? 238 LYS A O   1 
ATOM   2015 C CB  . LYS A 1 238 ? 29.459  0.173   65.484  1.00 14.24 ? 238 LYS A CB  1 
ATOM   2016 C CG  . LYS A 1 238 ? 30.110  1.221   64.591  1.00 18.45 ? 238 LYS A CG  1 
ATOM   2017 C CD  . LYS A 1 238 ? 31.410  0.655   63.987  1.00 26.08 ? 238 LYS A CD  1 
ATOM   2018 C CE  . LYS A 1 238 ? 31.201  -0.691  63.307  1.00 31.49 ? 238 LYS A CE  1 
ATOM   2019 N NZ  . LYS A 1 238 ? 32.488  -1.153  62.698  1.00 30.13 ? 238 LYS A NZ  1 
ATOM   2020 N N   . GLU A 1 239 ? 27.853  -0.925  68.016  1.00 14.12 ? 239 GLU A N   1 
ATOM   2021 C CA  . GLU A 1 239 ? 27.140  -2.007  68.684  1.00 14.99 ? 239 GLU A CA  1 
ATOM   2022 C C   . GLU A 1 239 ? 25.740  -1.572  69.123  1.00 15.24 ? 239 GLU A C   1 
ATOM   2023 O O   . GLU A 1 239 ? 24.784  -2.342  69.002  1.00 18.04 ? 239 GLU A O   1 
ATOM   2024 C CB  . GLU A 1 239 ? 27.970  -2.508  69.864  1.00 19.75 ? 239 GLU A CB  1 
ATOM   2025 C CG  . GLU A 1 239 ? 29.264  -3.160  69.421  1.00 35.59 ? 239 GLU A CG  1 
ATOM   2026 C CD  . GLU A 1 239 ? 30.195  -3.478  70.584  1.00 54.39 ? 239 GLU A CD  1 
ATOM   2027 O OE1 . GLU A 1 239 ? 31.355  -3.858  70.321  1.00 60.99 ? 239 GLU A OE1 1 
ATOM   2028 O OE2 . GLU A 1 239 ? 29.768  -3.352  71.753  1.00 57.68 ? 239 GLU A OE2 1 
ATOM   2029 N N   . LYS A 1 240 ? 25.588  -0.336  69.614  1.00 14.64 ? 240 LYS A N   1 
ATOM   2030 C CA  . LYS A 1 240 ? 24.256  0.112   70.018  1.00 16.85 ? 240 LYS A CA  1 
ATOM   2031 C C   . LYS A 1 240 ? 23.338  0.226   68.811  1.00 17.09 ? 240 LYS A C   1 
ATOM   2032 O O   . LYS A 1 240 ? 22.157  -0.149  68.876  1.00 16.21 ? 240 LYS A O   1 
ATOM   2033 C CB  . LYS A 1 240 ? 24.334  1.465   70.740  1.00 16.35 ? 240 LYS A CB  1 
ATOM   2034 C CG  . LYS A 1 240 ? 22.980  1.906   71.346  1.00 20.39 ? 240 LYS A CG  1 
ATOM   2035 C CD  . LYS A 1 240 ? 22.679  1.144   72.629  1.00 22.51 ? 240 LYS A CD  1 
ATOM   2036 C CE  . LYS A 1 240 ? 21.290  1.478   73.157  1.00 29.74 ? 240 LYS A CE  1 
ATOM   2037 N NZ  . LYS A 1 240 ? 20.952  0.688   74.393  1.00 31.56 ? 240 LYS A NZ  1 
ATOM   2038 N N   . TYR A 1 241 ? 23.863  0.780   67.720  1.00 14.08 ? 241 TYR A N   1 
ATOM   2039 C CA  . TYR A 1 241 ? 23.117  0.877   66.464  1.00 14.35 ? 241 TYR A CA  1 
ATOM   2040 C C   . TYR A 1 241 ? 22.676  -0.506  65.987  1.00 15.50 ? 241 TYR A C   1 
ATOM   2041 O O   . TYR A 1 241 ? 21.531  -0.695  65.536  1.00 16.64 ? 241 TYR A O   1 
ATOM   2042 C CB  . TYR A 1 241 ? 23.987  1.574   65.410  1.00 15.95 ? 241 TYR A CB  1 
ATOM   2043 C CG  . TYR A 1 241 ? 23.220  1.995   64.162  1.00 17.02 ? 241 TYR A CG  1 
ATOM   2044 C CD1 . TYR A 1 241 ? 23.038  1.106   63.119  1.00 13.94 ? 241 TYR A CD1 1 
ATOM   2045 C CD2 . TYR A 1 241 ? 22.690  3.278   64.046  1.00 15.24 ? 241 TYR A CD2 1 
ATOM   2046 C CE1 . TYR A 1 241 ? 22.318  1.460   61.985  1.00 18.69 ? 241 TYR A CE1 1 
ATOM   2047 C CE2 . TYR A 1 241 ? 21.975  3.662   62.918  1.00 17.28 ? 241 TYR A CE2 1 
ATOM   2048 C CZ  . TYR A 1 241 ? 21.805  2.758   61.898  1.00 15.01 ? 241 TYR A CZ  1 
ATOM   2049 O OH  . TYR A 1 241 ? 21.095  3.124   60.775  1.00 17.78 ? 241 TYR A OH  1 
ATOM   2050 N N   . PHE A 1 242 ? 23.561  -1.484  66.084  1.00 17.45 ? 242 PHE A N   1 
ATOM   2051 C CA  . PHE A 1 242 ? 23.196  -2.854  65.714  1.00 18.27 ? 242 PHE A CA  1 
ATOM   2052 C C   . PHE A 1 242 ? 22.101  -3.415  66.642  1.00 22.00 ? 242 PHE A C   1 
ATOM   2053 O O   . PHE A 1 242 ? 21.186  -4.110  66.189  1.00 19.79 ? 242 PHE A O   1 
ATOM   2054 C CB  . PHE A 1 242 ? 24.464  -3.728  65.713  1.00 18.09 ? 242 PHE A CB  1 
ATOM   2055 C CG  . PHE A 1 242 ? 24.258  -5.141  65.232  1.00 19.66 ? 242 PHE A CG  1 
ATOM   2056 C CD1 . PHE A 1 242 ? 24.327  -5.456  63.879  1.00 24.20 ? 242 PHE A CD1 1 
ATOM   2057 C CD2 . PHE A 1 242 ? 24.016  -6.148  66.135  1.00 17.46 ? 242 PHE A CD2 1 
ATOM   2058 C CE1 . PHE A 1 242 ? 24.149  -6.744  63.442  1.00 21.32 ? 242 PHE A CE1 1 
ATOM   2059 C CE2 . PHE A 1 242 ? 23.847  -7.469  65.714  1.00 19.52 ? 242 PHE A CE2 1 
ATOM   2060 C CZ  . PHE A 1 242 ? 23.906  -7.772  64.355  1.00 21.33 ? 242 PHE A CZ  1 
ATOM   2061 N N   . GLU A 1 243 ? 22.165  -3.113  67.943  1.00 18.53 ? 243 GLU A N   1 
ATOM   2062 C CA  . GLU A 1 243 ? 21.100  -3.546  68.854  1.00 20.54 ? 243 GLU A CA  1 
ATOM   2063 C C   . GLU A 1 243 ? 19.747  -2.953  68.459  1.00 18.76 ? 243 GLU A C   1 
ATOM   2064 O O   . GLU A 1 243 ? 18.713  -3.627  68.553  1.00 21.37 ? 243 GLU A O   1 
ATOM   2065 C CB  . GLU A 1 243 ? 21.452  -3.163  70.298  1.00 23.03 ? 243 GLU A CB  1 
ATOM   2066 C CG  . GLU A 1 243 ? 20.323  -3.448  71.332  1.00 35.20 ? 243 GLU A CG  1 
ATOM   2067 C CD  . GLU A 1 243 ? 20.321  -2.484  72.534  1.00 43.70 ? 243 GLU A CD  1 
ATOM   2068 O OE1 . GLU A 1 243 ? 19.227  -2.141  73.041  1.00 45.26 ? 243 GLU A OE1 1 
ATOM   2069 O OE2 . GLU A 1 243 ? 21.414  -2.077  72.981  1.00 43.93 ? 243 GLU A OE2 1 
ATOM   2070 N N   . ILE A 1 244 ? 19.723  -1.686  68.044  1.00 19.84 ? 244 ILE A N   1 
ATOM   2071 C CA  . ILE A 1 244 ? 18.445  -1.034  67.780  1.00 15.87 ? 244 ILE A CA  1 
ATOM   2072 C C   . ILE A 1 244 ? 17.902  -1.410  66.408  1.00 20.11 ? 244 ILE A C   1 
ATOM   2073 O O   . ILE A 1 244 ? 16.693  -1.636  66.252  1.00 18.44 ? 244 ILE A O   1 
ATOM   2074 C CB  . ILE A 1 244 ? 18.568  0.492   67.899  1.00 19.38 ? 244 ILE A CB  1 
ATOM   2075 C CG1 . ILE A 1 244 ? 18.991  0.902   69.303  1.00 15.06 ? 244 ILE A CG1 1 
ATOM   2076 C CG2 . ILE A 1 244 ? 17.235  1.127   67.496  1.00 21.26 ? 244 ILE A CG2 1 
ATOM   2077 C CD1 . ILE A 1 244 ? 18.031  0.458   70.407  1.00 19.27 ? 244 ILE A CD1 1 
ATOM   2078 N N   . PHE A 1 245 ? 18.774  -1.447  65.384  1.00 18.63 ? 245 PHE A N   1 
ATOM   2079 C CA  . PHE A 1 245 ? 18.346  -1.559  63.994  1.00 17.51 ? 245 PHE A CA  1 
ATOM   2080 C C   . PHE A 1 245 ? 18.779  -2.852  63.332  1.00 20.91 ? 245 PHE A C   1 
ATOM   2081 O O   . PHE A 1 245 ? 18.315  -3.152  62.223  1.00 22.13 ? 245 PHE A O   1 
ATOM   2082 C CB  . PHE A 1 245 ? 18.871  -0.358  63.167  1.00 13.14 ? 245 PHE A CB  1 
ATOM   2083 C CG  . PHE A 1 245 ? 18.396  0.972   63.646  1.00 16.69 ? 245 PHE A CG  1 
ATOM   2084 C CD1 . PHE A 1 245 ? 17.092  1.382   63.406  1.00 16.26 ? 245 PHE A CD1 1 
ATOM   2085 C CD2 . PHE A 1 245 ? 19.245  1.813   64.334  1.00 17.63 ? 245 PHE A CD2 1 
ATOM   2086 C CE1 . PHE A 1 245 ? 16.649  2.614   63.839  1.00 18.50 ? 245 PHE A CE1 1 
ATOM   2087 C CE2 . PHE A 1 245 ? 18.794  3.053   64.782  1.00 20.26 ? 245 PHE A CE2 1 
ATOM   2088 C CZ  . PHE A 1 245 ? 17.495  3.445   64.533  1.00 20.09 ? 245 PHE A CZ  1 
ATOM   2089 N N   . GLY A 1 246 ? 19.628  -3.640  63.981  1.00 19.41 ? 246 GLY A N   1 
ATOM   2090 C CA  . GLY A 1 246 ? 20.003  -4.944  63.458  1.00 20.75 ? 246 GLY A CA  1 
ATOM   2091 C C   . GLY A 1 246 ? 20.899  -4.893  62.246  1.00 20.42 ? 246 GLY A C   1 
ATOM   2092 O O   . GLY A 1 246 ? 21.001  -5.882  61.519  1.00 21.57 ? 246 GLY A O   1 
ATOM   2093 N N   . GLU A 1 247 ? 21.510  -3.740  61.979  1.00 19.21 ? 247 GLU A N   1 
ATOM   2094 C CA  . GLU A 1 247 ? 22.493  -3.576  60.916  1.00 30.07 ? 247 GLU A CA  1 
ATOM   2095 C C   . GLU A 1 247 ? 23.621  -2.720  61.472  1.00 25.55 ? 247 GLU A C   1 
ATOM   2096 O O   . GLU A 1 247 ? 23.448  -2.035  62.480  1.00 26.75 ? 247 GLU A O   1 
ATOM   2097 C CB  . GLU A 1 247 ? 21.877  -2.909  59.672  1.00 39.33 ? 247 GLU A CB  1 
ATOM   2098 C CG  . GLU A 1 247 ? 20.355  -3.070  59.589  1.00 51.21 ? 247 GLU A CG  1 
ATOM   2099 C CD  . GLU A 1 247 ? 19.757  -2.569  58.287  1.00 58.69 ? 247 GLU A CD  1 
ATOM   2100 O OE1 . GLU A 1 247 ? 20.528  -2.141  57.402  1.00 62.88 ? 247 GLU A OE1 1 
ATOM   2101 O OE2 . GLU A 1 247 ? 18.511  -2.605  58.156  1.00 61.20 ? 247 GLU A OE2 1 
ATOM   2102 N N   . HIS A 1 248 ? 24.817  -2.780  60.798  1.00 23.80 ? 248 HIS A N   1 
ATOM   2103 C CA  . HIS A 1 248 ? 25.825  -1.833  61.257  1.00 24.96 ? 248 HIS A CA  1 
ATOM   2104 C C   . HIS A 1 248 ? 25.706  -0.521  60.486  1.00 22.23 ? 248 HIS A C   1 
ATOM   2105 O O   . HIS A 1 248 ? 25.320  -0.517  59.310  1.00 24.79 ? 248 HIS A O   1 
ATOM   2106 C CB  . HIS A 1 248 ? 27.223  -2.407  61.076  1.00 33.45 ? 248 HIS A CB  1 
ATOM   2107 C CG  . HIS A 1 248 ? 27.668  -3.270  62.218  1.00 51.38 ? 248 HIS A CG  1 
ATOM   2108 N ND1 . HIS A 1 248 ? 27.856  -2.781  63.494  1.00 51.92 ? 248 HIS A ND1 1 
ATOM   2109 C CD2 . HIS A 1 248 ? 27.940  -4.596  62.280  1.00 55.20 ? 248 HIS A CD2 1 
ATOM   2110 C CE1 . HIS A 1 248 ? 28.240  -3.766  64.289  1.00 54.98 ? 248 HIS A CE1 1 
ATOM   2111 N NE2 . HIS A 1 248 ? 28.297  -4.878  63.577  1.00 56.55 ? 248 HIS A NE2 1 
ATOM   2112 N N   . PRO A 1 249 ? 26.004  0.606   61.122  1.00 19.11 ? 249 PRO A N   1 
ATOM   2113 C CA  . PRO A 1 249 ? 25.870  1.899   60.436  1.00 16.97 ? 249 PRO A CA  1 
ATOM   2114 C C   . PRO A 1 249 ? 27.015  2.169   59.472  1.00 24.56 ? 249 PRO A C   1 
ATOM   2115 O O   . PRO A 1 249 ? 28.165  1.802   59.713  1.00 26.02 ? 249 PRO A O   1 
ATOM   2116 C CB  . PRO A 1 249 ? 25.879  2.907   61.586  1.00 20.53 ? 249 PRO A CB  1 
ATOM   2117 C CG  . PRO A 1 249 ? 26.797  2.230   62.627  1.00 23.57 ? 249 PRO A CG  1 
ATOM   2118 C CD  . PRO A 1 249 ? 26.456  0.753   62.524  1.00 22.98 ? 249 PRO A CD  1 
ATOM   2119 N N   . VAL A 1 250 ? 26.687  2.834   58.362  1.00 17.78 ? 250 VAL A N   1 
ATOM   2120 C CA  . VAL A 1 250 ? 27.695  3.256   57.393  1.00 15.69 ? 250 VAL A CA  1 
ATOM   2121 C C   . VAL A 1 250 ? 27.813  4.770   57.329  1.00 15.26 ? 250 VAL A C   1 
ATOM   2122 O O   . VAL A 1 250 ? 28.684  5.291   56.605  1.00 20.24 ? 250 VAL A O   1 
ATOM   2123 C CB  . VAL A 1 250 ? 27.416  2.674   55.995  1.00 22.41 ? 250 VAL A CB  1 
ATOM   2124 C CG1 . VAL A 1 250 ? 27.542  1.135   56.022  1.00 25.68 ? 250 VAL A CG1 1 
ATOM   2125 C CG2 . VAL A 1 250 ? 26.039  3.105   55.532  1.00 24.72 ? 250 VAL A CG2 1 
ATOM   2126 N N   . TYR A 1 251 ? 26.977  5.484   58.060  1.00 15.69 ? 251 TYR A N   1 
ATOM   2127 C CA  . TYR A 1 251 ? 27.173  6.914   58.243  1.00 16.23 ? 251 TYR A CA  1 
ATOM   2128 C C   . TYR A 1 251 ? 27.048  7.272   59.718  1.00 17.87 ? 251 TYR A C   1 
ATOM   2129 O O   . TYR A 1 251 ? 26.387  6.579   60.501  1.00 20.34 ? 251 TYR A O   1 
ATOM   2130 C CB  . TYR A 1 251 ? 26.193  7.748   57.431  1.00 26.16 ? 251 TYR A CB  1 
ATOM   2131 C CG  . TYR A 1 251 ? 24.874  7.074   57.231  1.00 23.40 ? 251 TYR A CG  1 
ATOM   2132 C CD1 . TYR A 1 251 ? 23.973  6.940   58.285  1.00 26.33 ? 251 TYR A CD1 1 
ATOM   2133 C CD2 . TYR A 1 251 ? 24.535  6.552   56.002  1.00 22.60 ? 251 TYR A CD2 1 
ATOM   2134 C CE1 . TYR A 1 251 ? 22.768  6.313   58.107  1.00 25.49 ? 251 TYR A CE1 1 
ATOM   2135 C CE2 . TYR A 1 251 ? 23.336  5.921   55.807  1.00 21.63 ? 251 TYR A CE2 1 
ATOM   2136 C CZ  . TYR A 1 251 ? 22.449  5.801   56.864  1.00 27.07 ? 251 TYR A CZ  1 
ATOM   2137 O OH  . TYR A 1 251 ? 21.238  5.172   56.683  1.00 29.39 ? 251 TYR A OH  1 
ATOM   2138 N N   . MET A 1 252 ? 27.715  8.359   60.094  1.00 13.00 ? 252 MET A N   1 
ATOM   2139 C CA  . MET A 1 252 ? 27.679  8.854   61.455  1.00 9.64  ? 252 MET A CA  1 
ATOM   2140 C C   . MET A 1 252 ? 27.699  10.363  61.400  1.00 9.11  ? 252 MET A C   1 
ATOM   2141 O O   . MET A 1 252 ? 28.243  10.971  60.473  1.00 13.03 ? 252 MET A O   1 
ATOM   2142 C CB  . MET A 1 252 ? 28.875  8.379   62.320  1.00 11.61 ? 252 MET A CB  1 
ATOM   2143 C CG  . MET A 1 252 ? 28.693  7.021   62.885  1.00 13.14 ? 252 MET A CG  1 
ATOM   2144 S SD  . MET A 1 252 ? 29.910  6.648   64.160  1.00 15.97 ? 252 MET A SD  1 
ATOM   2145 C CE  . MET A 1 252 ? 29.513  4.943   64.439  1.00 14.29 ? 252 MET A CE  1 
ATOM   2146 N N   . TRP A 1 253 ? 27.110  10.965  62.422  1.00 8.80  ? 253 TRP A N   1 
ATOM   2147 C CA  . TRP A 1 253 ? 27.252  12.395  62.626  1.00 8.70  ? 253 TRP A CA  1 
ATOM   2148 C C   . TRP A 1 253 ? 28.394  12.627  63.607  1.00 11.13 ? 253 TRP A C   1 
ATOM   2149 O O   . TRP A 1 253 ? 28.322  12.157  64.755  1.00 11.75 ? 253 TRP A O   1 
ATOM   2150 C CB  . TRP A 1 253 ? 25.951  12.993  63.188  1.00 9.04  ? 253 TRP A CB  1 
ATOM   2151 C CG  . TRP A 1 253 ? 26.121  14.425  63.656  1.00 8.34  ? 253 TRP A CG  1 
ATOM   2152 C CD1 . TRP A 1 253 ? 26.061  14.867  64.950  1.00 9.97  ? 253 TRP A CD1 1 
ATOM   2153 C CD2 . TRP A 1 253 ? 26.490  15.565  62.857  1.00 11.60 ? 253 TRP A CD2 1 
ATOM   2154 N NE1 . TRP A 1 253 ? 26.315  16.215  65.007  1.00 11.00 ? 253 TRP A NE1 1 
ATOM   2155 C CE2 . TRP A 1 253 ? 26.576  16.673  63.738  1.00 10.81 ? 253 TRP A CE2 1 
ATOM   2156 C CE3 . TRP A 1 253 ? 26.719  15.776  61.485  1.00 12.52 ? 253 TRP A CE3 1 
ATOM   2157 C CZ2 . TRP A 1 253 ? 26.920  17.963  63.307  1.00 11.57 ? 253 TRP A CZ2 1 
ATOM   2158 C CZ3 . TRP A 1 253 ? 27.056  17.106  61.042  1.00 11.15 ? 253 TRP A CZ3 1 
ATOM   2159 C CH2 . TRP A 1 253 ? 27.158  18.165  61.974  1.00 12.55 ? 253 TRP A CH2 1 
ATOM   2160 N N   . PRO A 1 254 ? 29.462  13.316  63.224  1.00 10.13 ? 254 PRO A N   1 
ATOM   2161 C CA  . PRO A 1 254 ? 30.537  13.583  64.192  1.00 9.24  ? 254 PRO A CA  1 
ATOM   2162 C C   . PRO A 1 254 ? 30.089  14.687  65.131  1.00 10.03 ? 254 PRO A C   1 
ATOM   2163 O O   . PRO A 1 254 ? 29.648  15.752  64.677  1.00 12.12 ? 254 PRO A O   1 
ATOM   2164 C CB  . PRO A 1 254 ? 31.720  14.020  63.309  1.00 12.00 ? 254 PRO A CB  1 
ATOM   2165 C CG  . PRO A 1 254 ? 31.074  14.600  62.078  1.00 18.95 ? 254 PRO A CG  1 
ATOM   2166 C CD  . PRO A 1 254 ? 29.744  13.872  61.883  1.00 16.92 ? 254 PRO A CD  1 
ATOM   2167 N N   . PRO A 1 255 ? 30.166  14.477  66.440  1.00 11.61 ? 255 PRO A N   1 
ATOM   2168 C CA  . PRO A 1 255 ? 29.675  15.494  67.375  1.00 12.83 ? 255 PRO A CA  1 
ATOM   2169 C C   . PRO A 1 255 ? 30.300  16.857  67.125  1.00 12.21 ? 255 PRO A C   1 
ATOM   2170 O O   . PRO A 1 255 ? 31.517  16.981  66.904  1.00 11.67 ? 255 PRO A O   1 
ATOM   2171 C CB  . PRO A 1 255 ? 30.081  14.935  68.744  1.00 13.10 ? 255 PRO A CB  1 
ATOM   2172 C CG  . PRO A 1 255 ? 30.002  13.449  68.540  1.00 11.42 ? 255 PRO A CG  1 
ATOM   2173 C CD  . PRO A 1 255 ? 30.550  13.231  67.122  1.00 12.05 ? 255 PRO A CD  1 
ATOM   2174 N N   . LEU A 1 256 ? 29.443  17.875  67.156  1.00 11.35 ? 256 LEU A N   1 
ATOM   2175 C CA  . LEU A 1 256 ? 29.817  19.275  66.939  1.00 10.52 ? 256 LEU A CA  1 
ATOM   2176 C C   . LEU A 1 256 ? 30.434  19.479  65.554  1.00 10.86 ? 256 LEU A C   1 
ATOM   2177 O O   . LEU A 1 256 ? 31.220  20.414  65.367  1.00 11.75 ? 256 LEU A O   1 
ATOM   2178 C CB  . LEU A 1 256 ? 30.784  19.797  68.024  1.00 10.42 ? 256 LEU A CB  1 
ATOM   2179 C CG  . LEU A 1 256 ? 30.425  19.316  69.438  1.00 14.95 ? 256 LEU A CG  1 
ATOM   2180 C CD1 . LEU A 1 256 ? 31.496  19.616  70.410  1.00 22.03 ? 256 LEU A CD1 1 
ATOM   2181 C CD2 . LEU A 1 256 ? 29.091  19.937  69.864  1.00 13.92 ? 256 LEU A CD2 1 
ATOM   2182 N N   . ALA A 1 257 ? 30.071  18.599  64.601  1.00 11.45 ? 257 ALA A N   1 
ATOM   2183 C CA  . ALA A 1 257 ? 30.647  18.575  63.257  1.00 9.20  ? 257 ALA A CA  1 
ATOM   2184 C C   . ALA A 1 257 ? 32.157  18.381  63.309  1.00 14.20 ? 257 ALA A C   1 
ATOM   2185 O O   . ALA A 1 257 ? 32.877  18.778  62.390  1.00 14.86 ? 257 ALA A O   1 
ATOM   2186 C CB  . ALA A 1 257 ? 30.306  19.863  62.502  1.00 11.54 ? 257 ALA A CB  1 
ATOM   2187 N N   . SER A 1 258 ? 32.692  17.825  64.393  1.00 11.76 ? 258 SER A N   1 
ATOM   2188 C CA  . SER A 1 258 ? 34.132  17.932  64.611  1.00 11.13 ? 258 SER A CA  1 
ATOM   2189 C C   . SER A 1 258 ? 34.898  16.879  63.841  1.00 13.94 ? 258 SER A C   1 
ATOM   2190 O O   . SER A 1 258 ? 34.653  15.673  63.969  1.00 15.09 ? 258 SER A O   1 
ATOM   2191 C CB  . SER A 1 258 ? 34.486  17.857  66.098  1.00 13.13 ? 258 SER A CB  1 
ATOM   2192 O OG  . SER A 1 258 ? 35.887  18.151  66.271  1.00 17.09 ? 258 SER A OG  1 
ATOM   2193 N N   . VAL A 1 259 ? 35.852  17.339  63.031  1.00 13.75 ? 259 VAL A N   1 
ATOM   2194 C CA  . VAL A 1 259 ? 36.670  16.426  62.254  1.00 12.35 ? 259 VAL A CA  1 
ATOM   2195 C C   . VAL A 1 259 ? 38.114  16.893  62.304  1.00 13.40 ? 259 VAL A C   1 
ATOM   2196 O O   . VAL A 1 259 ? 38.431  18.022  62.693  1.00 15.08 ? 259 VAL A O   1 
ATOM   2197 C CB  . VAL A 1 259 ? 36.209  16.307  60.787  1.00 13.78 ? 259 VAL A CB  1 
ATOM   2198 C CG1 . VAL A 1 259 ? 34.802  15.717  60.718  1.00 18.20 ? 259 VAL A CG1 1 
ATOM   2199 C CG2 . VAL A 1 259 ? 36.258  17.683  60.126  1.00 17.62 ? 259 VAL A CG2 1 
ATOM   2200 N N   . SER A 1 260 ? 38.992  15.973  61.923  1.00 13.96 ? 260 SER A N   1 
ATOM   2201 C CA  . SER A 1 260 ? 40.420  16.192  61.783  1.00 15.11 ? 260 SER A CA  1 
ATOM   2202 C C   . SER A 1 260 ? 40.864  15.096  60.839  1.00 15.43 ? 260 SER A C   1 
ATOM   2203 O O   . SER A 1 260 ? 40.102  14.170  60.572  1.00 16.35 ? 260 SER A O   1 
ATOM   2204 C CB  . SER A 1 260 ? 41.167  16.074  63.109  1.00 18.52 ? 260 SER A CB  1 
ATOM   2205 O OG  . SER A 1 260 ? 41.011  14.753  63.606  1.00 16.81 ? 260 SER A OG  1 
ATOM   2206 N N   . ASN A 1 261 ? 42.111  15.178  60.366  1.00 16.54 ? 261 ASN A N   1 
ATOM   2207 C CA  . ASN A 1 261 ? 42.603  14.126  59.486  1.00 17.00 ? 261 ASN A CA  1 
ATOM   2208 C C   . ASN A 1 261 ? 42.571  12.774  60.191  1.00 17.91 ? 261 ASN A C   1 
ATOM   2209 O O   . ASN A 1 261 ? 42.108  11.776  59.623  1.00 16.79 ? 261 ASN A O   1 
ATOM   2210 C CB  . ASN A 1 261 ? 44.025  14.451  59.000  1.00 18.39 ? 261 ASN A CB  1 
ATOM   2211 C CG  . ASN A 1 261 ? 44.073  15.655  58.086  1.00 20.61 ? 261 ASN A CG  1 
ATOM   2212 O OD1 . ASN A 1 261 ? 43.121  15.938  57.357  1.00 19.51 ? 261 ASN A OD1 1 
ATOM   2213 N ND2 . ASN A 1 261 ? 45.196  16.365  58.104  1.00 23.46 ? 261 ASN A ND2 1 
ATOM   2214 N N   . GLU A 1 262 ? 43.057  12.724  61.438  1.00 17.15 ? 262 GLU A N   1 
ATOM   2215 C CA  . GLU A 1 262 ? 43.051  11.472  62.182  1.00 17.16 ? 262 GLU A CA  1 
ATOM   2216 C C   . GLU A 1 262 ? 41.643  10.995  62.510  1.00 17.77 ? 262 GLU A C   1 
ATOM   2217 O O   . GLU A 1 262 ? 41.409  9.780   62.533  1.00 18.35 ? 262 GLU A O   1 
ATOM   2218 C CB  . GLU A 1 262 ? 43.867  11.621  63.462  1.00 17.88 ? 262 GLU A CB  1 
ATOM   2219 C CG  . GLU A 1 262 ? 45.333  11.843  63.175  1.00 22.35 ? 262 GLU A CG  1 
ATOM   2220 C CD  . GLU A 1 262 ? 46.190  11.778  64.423  1.00 47.39 ? 262 GLU A CD  1 
ATOM   2221 O OE1 . GLU A 1 262 ? 45.843  11.017  65.353  1.00 43.33 ? 262 GLU A OE1 1 
ATOM   2222 O OE2 . GLU A 1 262 ? 47.210  12.495  64.471  1.00 52.03 ? 262 GLU A OE2 1 
ATOM   2223 N N   . ALA A 1 263 ? 40.704  11.908  62.766  1.00 15.84 ? 263 ALA A N   1 
ATOM   2224 C CA  . ALA A 1 263 ? 39.332  11.477  63.040  1.00 14.94 ? 263 ALA A CA  1 
ATOM   2225 C C   . ALA A 1 263 ? 38.693  10.883  61.790  1.00 16.69 ? 263 ALA A C   1 
ATOM   2226 O O   . ALA A 1 263 ? 37.997  9.859   61.860  1.00 16.48 ? 263 ALA A O   1 
ATOM   2227 C CB  . ALA A 1 263 ? 38.482  12.642  63.560  1.00 13.55 ? 263 ALA A CB  1 
ATOM   2228 N N   . LEU A 1 264 ? 38.897  11.518  60.641  1.00 14.95 ? 264 LEU A N   1 
ATOM   2229 C CA  . LEU A 1 264 ? 38.338  10.953  59.414  1.00 16.53 ? 264 LEU A CA  1 
ATOM   2230 C C   . LEU A 1 264 ? 38.934  9.580   59.116  1.00 19.41 ? 264 LEU A C   1 
ATOM   2231 O O   . LEU A 1 264 ? 38.227  8.673   58.663  1.00 18.32 ? 264 LEU A O   1 
ATOM   2232 C CB  . LEU A 1 264 ? 38.566  11.917  58.257  1.00 16.26 ? 264 LEU A CB  1 
ATOM   2233 C CG  . LEU A 1 264 ? 37.731  13.188  58.347  1.00 17.91 ? 264 LEU A CG  1 
ATOM   2234 C CD1 . LEU A 1 264 ? 38.262  14.242  57.393  1.00 17.90 ? 264 LEU A CD1 1 
ATOM   2235 C CD2 . LEU A 1 264 ? 36.270  12.888  58.031  1.00 23.13 ? 264 LEU A CD2 1 
ATOM   2236 N N   . GLU A 1 265 ? 40.231  9.399   59.383  1.00 15.79 ? 265 GLU A N   1 
ATOM   2237 C CA  . GLU A 1 265 ? 40.836  8.080   59.230  1.00 18.57 ? 265 GLU A CA  1 
ATOM   2238 C C   . GLU A 1 265 ? 40.207  7.050   60.169  1.00 17.18 ? 265 GLU A C   1 
ATOM   2239 O O   . GLU A 1 265 ? 40.048  5.882   59.789  1.00 20.47 ? 265 GLU A O   1 
ATOM   2240 C CB  . GLU A 1 265 ? 42.351  8.160   59.468  1.00 19.67 ? 265 GLU A CB  1 
ATOM   2241 C CG  . GLU A 1 265 ? 43.095  8.951   58.388  1.00 18.80 ? 265 GLU A CG  1 
ATOM   2242 C CD  . GLU A 1 265 ? 44.578  9.127   58.693  1.00 40.50 ? 265 GLU A CD  1 
ATOM   2243 O OE1 . GLU A 1 265 ? 45.122  8.328   59.472  1.00 48.13 ? 265 GLU A OE1 1 
ATOM   2244 O OE2 . GLU A 1 265 ? 45.203  10.063  58.155  1.00 47.93 ? 265 GLU A OE2 1 
ATOM   2245 N N   . LEU A 1 266 ? 39.896  7.443   61.411  1.00 15.97 ? 266 LEU A N   1 
ATOM   2246 C CA  . LEU A 1 266 ? 39.271  6.514   62.359  1.00 18.57 ? 266 LEU A CA  1 
ATOM   2247 C C   . LEU A 1 266 ? 37.873  6.109   61.895  1.00 17.64 ? 266 LEU A C   1 
ATOM   2248 O O   . LEU A 1 266 ? 37.515  4.921   61.906  1.00 18.08 ? 266 LEU A O   1 
ATOM   2249 C CB  . LEU A 1 266 ? 39.200  7.144   63.754  1.00 18.07 ? 266 LEU A CB  1 
ATOM   2250 C CG  . LEU A 1 266 ? 38.366  6.364   64.779  1.00 15.91 ? 266 LEU A CG  1 
ATOM   2251 C CD1 . LEU A 1 266 ? 38.944  4.994   65.061  1.00 20.33 ? 266 LEU A CD1 1 
ATOM   2252 C CD2 . LEU A 1 266 ? 38.241  7.149   66.099  1.00 17.59 ? 266 LEU A CD2 1 
ATOM   2253 N N   . TYR A 1 267 ? 37.063  7.080   61.496  1.00 16.31 ? 267 TYR A N   1 
ATOM   2254 C CA  . TYR A 1 267 ? 35.730  6.744   61.001  1.00 18.39 ? 267 TYR A CA  1 
ATOM   2255 C C   . TYR A 1 267 ? 35.814  5.760   59.830  1.00 18.20 ? 267 TYR A C   1 
ATOM   2256 O O   . TYR A 1 267 ? 35.093  4.753   59.790  1.00 17.63 ? 267 TYR A O   1 
ATOM   2257 C CB  . TYR A 1 267 ? 34.989  8.022   60.603  1.00 15.28 ? 267 TYR A CB  1 
ATOM   2258 C CG  . TYR A 1 267 ? 34.472  8.850   61.781  1.00 14.41 ? 267 TYR A CG  1 
ATOM   2259 C CD1 . TYR A 1 267 ? 33.474  8.349   62.620  1.00 16.50 ? 267 TYR A CD1 1 
ATOM   2260 C CD2 . TYR A 1 267 ? 34.956  10.131  62.029  1.00 13.78 ? 267 TYR A CD2 1 
ATOM   2261 C CE1 . TYR A 1 267 ? 32.979  9.093   63.674  1.00 15.01 ? 267 TYR A CE1 1 
ATOM   2262 C CE2 . TYR A 1 267 ? 34.487  10.882  63.108  1.00 15.35 ? 267 TYR A CE2 1 
ATOM   2263 C CZ  . TYR A 1 267 ? 33.501  10.345  63.923  1.00 16.95 ? 267 TYR A CZ  1 
ATOM   2264 O OH  . TYR A 1 267 ? 33.007  11.083  64.956  1.00 14.55 ? 267 TYR A OH  1 
ATOM   2265 N N   . TYR A 1 268 ? 36.725  6.004   58.883  1.00 15.30 ? 268 TYR A N   1 
ATOM   2266 C CA  . TYR A 1 268 ? 36.852  5.088   57.753  1.00 15.07 ? 268 TYR A CA  1 
ATOM   2267 C C   . TYR A 1 268 ? 37.266  3.696   58.209  1.00 16.60 ? 268 TYR A C   1 
ATOM   2268 O O   . TYR A 1 268 ? 36.737  2.690   57.717  1.00 17.76 ? 268 TYR A O   1 
ATOM   2269 C CB  . TYR A 1 268 ? 37.867  5.628   56.747  1.00 18.85 ? 268 TYR A CB  1 
ATOM   2270 C CG  . TYR A 1 268 ? 38.150  4.642   55.650  1.00 21.94 ? 268 TYR A CG  1 
ATOM   2271 C CD1 . TYR A 1 268 ? 37.213  4.421   54.654  1.00 21.07 ? 268 TYR A CD1 1 
ATOM   2272 C CD2 . TYR A 1 268 ? 39.332  3.914   55.624  1.00 25.34 ? 268 TYR A CD2 1 
ATOM   2273 C CE1 . TYR A 1 268 ? 37.447  3.510   53.631  1.00 22.46 ? 268 TYR A CE1 1 
ATOM   2274 C CE2 . TYR A 1 268 ? 39.575  2.997   54.603  1.00 28.97 ? 268 TYR A CE2 1 
ATOM   2275 C CZ  . TYR A 1 268 ? 38.612  2.801   53.612  1.00 25.25 ? 268 TYR A CZ  1 
ATOM   2276 O OH  . TYR A 1 268 ? 38.815  1.895   52.572  1.00 29.84 ? 268 TYR A OH  1 
ATOM   2277 N N   . GLU A 1 269 ? 38.240  3.613   59.130  1.00 17.51 ? 269 GLU A N   1 
ATOM   2278 C CA  . GLU A 1 269 ? 38.687  2.322   59.637  1.00 20.18 ? 269 GLU A CA  1 
ATOM   2279 C C   . GLU A 1 269 ? 37.557  1.532   60.288  1.00 20.66 ? 269 GLU A C   1 
ATOM   2280 O O   . GLU A 1 269 ? 37.583  0.293   60.268  1.00 22.59 ? 269 GLU A O   1 
ATOM   2281 C CB  . GLU A 1 269 ? 39.821  2.511   60.653  1.00 28.51 ? 269 GLU A CB  1 
ATOM   2282 C CG  . GLU A 1 269 ? 41.224  2.542   60.061  1.00 50.53 ? 269 GLU A CG  1 
ATOM   2283 C CD  . GLU A 1 269 ? 41.452  1.457   59.026  1.00 65.60 ? 269 GLU A CD  1 
ATOM   2284 O OE1 . GLU A 1 269 ? 41.578  1.795   57.831  1.00 71.87 ? 269 GLU A OE1 1 
ATOM   2285 O OE2 . GLU A 1 269 ? 41.498  0.269   59.405  1.00 70.83 ? 269 GLU A OE2 1 
ATOM   2286 N N   . LYS A 1 270 ? 36.586  2.213   60.883  1.00 19.10 ? 270 LYS A N   1 
ATOM   2287 C CA  . LYS A 1 270 ? 35.479  1.561   61.568  1.00 22.18 ? 270 LYS A CA  1 
ATOM   2288 C C   . LYS A 1 270 ? 34.294  1.311   60.641  1.00 23.75 ? 270 LYS A C   1 
ATOM   2289 O O   . LYS A 1 270 ? 33.208  0.948   61.115  1.00 18.73 ? 270 LYS A O   1 
ATOM   2290 C CB  . LYS A 1 270 ? 35.045  2.406   62.777  1.00 20.94 ? 270 LYS A CB  1 
ATOM   2291 C CG  . LYS A 1 270 ? 36.140  2.515   63.855  1.00 20.45 ? 270 LYS A CG  1 
ATOM   2292 C CD  . LYS A 1 270 ? 36.474  1.159   64.426  1.00 29.77 ? 270 LYS A CD  1 
ATOM   2293 C CE  . LYS A 1 270 ? 37.755  1.236   65.252  1.00 34.21 ? 270 LYS A CE  1 
ATOM   2294 N NZ  . LYS A 1 270 ? 38.313  -0.103  65.560  1.00 38.51 ? 270 LYS A NZ  1 
ATOM   2295 N N   . GLY A 1 271 ? 34.478  1.504   59.335  1.00 18.98 ? 271 GLY A N   1 
ATOM   2296 C CA  . GLY A 1 271 ? 33.455  1.175   58.371  1.00 20.15 ? 271 GLY A CA  1 
ATOM   2297 C C   . GLY A 1 271 ? 32.476  2.278   58.053  1.00 14.73 ? 271 GLY A C   1 
ATOM   2298 O O   . GLY A 1 271 ? 31.443  2.011   57.413  1.00 18.77 ? 271 GLY A O   1 
ATOM   2299 N N   . ILE A 1 272 ? 32.735  3.508   58.486  1.00 16.27 ? 272 ILE A N   1 
ATOM   2300 C CA  . ILE A 1 272 ? 31.862  4.615   58.137  1.00 17.06 ? 272 ILE A CA  1 
ATOM   2301 C C   . ILE A 1 272 ? 32.264  5.130   56.756  1.00 22.12 ? 272 ILE A C   1 
ATOM   2302 O O   . ILE A 1 272 ? 33.422  5.492   56.537  1.00 24.33 ? 272 ILE A O   1 
ATOM   2303 C CB  . ILE A 1 272 ? 31.942  5.724   59.200  1.00 16.21 ? 272 ILE A CB  1 
ATOM   2304 C CG1 . ILE A 1 272 ? 31.675  5.133   60.590  1.00 17.23 ? 272 ILE A CG1 1 
ATOM   2305 C CG2 . ILE A 1 272 ? 30.959  6.838   58.896  1.00 15.91 ? 272 ILE A CG2 1 
ATOM   2306 C CD1 . ILE A 1 272 ? 30.358  4.369   60.676  1.00 18.90 ? 272 ILE A CD1 1 
ATOM   2307 N N   . ASN A 1 273 ? 31.310  5.143   55.822  1.00 18.71 ? 273 ASN A N   1 
ATOM   2308 C CA  . ASN A 1 273 ? 31.544  5.566   54.442  1.00 22.97 ? 273 ASN A CA  1 
ATOM   2309 C C   . ASN A 1 273 ? 31.170  7.009   54.175  1.00 16.92 ? 273 ASN A C   1 
ATOM   2310 O O   . ASN A 1 273 ? 31.562  7.544   53.122  1.00 17.06 ? 273 ASN A O   1 
ATOM   2311 C CB  . ASN A 1 273 ? 30.747  4.700   53.462  1.00 27.91 ? 273 ASN A CB  1 
ATOM   2312 C CG  . ASN A 1 273 ? 31.226  3.276   53.433  1.00 37.97 ? 273 ASN A CG  1 
ATOM   2313 O OD1 . ASN A 1 273 ? 32.428  3.022   53.442  1.00 37.01 ? 273 ASN A OD1 1 
ATOM   2314 N ND2 . ASN A 1 273 ? 30.288  2.332   53.402  1.00 45.25 ? 273 ASN A ND2 1 
ATOM   2315 N N   . MET A 1 274 ? 30.392  7.631   55.064  1.00 16.26 ? 274 MET A N   1 
ATOM   2316 C CA  . MET A 1 274 ? 29.953  8.997   54.845  1.00 12.91 ? 274 MET A CA  1 
ATOM   2317 C C   . MET A 1 274 ? 29.729  9.705   56.175  1.00 12.30 ? 274 MET A C   1 
ATOM   2318 O O   . MET A 1 274 ? 29.224  9.104   57.134  1.00 14.58 ? 274 MET A O   1 
ATOM   2319 C CB  . MET A 1 274 ? 28.666  9.032   54.015  1.00 16.08 ? 274 MET A CB  1 
ATOM   2320 C CG  . MET A 1 274 ? 28.255  10.453  53.653  1.00 16.45 ? 274 MET A CG  1 
ATOM   2321 S SD  . MET A 1 274 ? 27.115  11.242  54.843  1.00 32.75 ? 274 MET A SD  1 
ATOM   2322 C CE  . MET A 1 274 ? 25.565  10.665  54.111  1.00 29.50 ? 274 MET A CE  1 
ATOM   2323 N N   . LEU A 1 275 ? 30.095  10.991  56.235  1.00 12.67 ? 275 LEU A N   1 
ATOM   2324 C CA  . LEU A 1 275 ? 29.670  11.862  57.325  1.00 13.53 ? 275 LEU A CA  1 
ATOM   2325 C C   . LEU A 1 275 ? 29.428  13.256  56.774  1.00 13.26 ? 275 LEU A C   1 
ATOM   2326 O O   . LEU A 1 275 ? 29.635  13.530  55.596  1.00 12.68 ? 275 LEU A O   1 
ATOM   2327 C CB  . LEU A 1 275 ? 30.683  11.887  58.469  1.00 16.41 ? 275 LEU A CB  1 
ATOM   2328 C CG  . LEU A 1 275 ? 32.135  12.081  58.082  1.00 16.72 ? 275 LEU A CG  1 
ATOM   2329 C CD1 . LEU A 1 275 ? 32.363  13.561  57.871  1.00 21.62 ? 275 LEU A CD1 1 
ATOM   2330 C CD2 . LEU A 1 275 ? 33.042  11.578  59.189  1.00 19.39 ? 275 LEU A CD2 1 
ATOM   2331 N N   . ALA A 1 276 ? 28.949  14.152  57.642  1.00 9.58  ? 276 ALA A N   1 
ATOM   2332 C CA  . ALA A 1 276 ? 28.898  15.552  57.282  1.00 10.11 ? 276 ALA A CA  1 
ATOM   2333 C C   . ALA A 1 276 ? 29.637  16.350  58.349  1.00 11.80 ? 276 ALA A C   1 
ATOM   2334 O O   . ALA A 1 276 ? 29.843  15.887  59.471  1.00 12.87 ? 276 ALA A O   1 
ATOM   2335 C CB  . ALA A 1 276 ? 27.443  16.022  57.118  1.00 11.79 ? 276 ALA A CB  1 
ATOM   2336 N N   . THR A 1 277 ? 30.041  17.561  57.981  1.00 12.52 ? 277 THR A N   1 
ATOM   2337 C CA  . THR A 1 277 ? 30.688  18.498  58.889  1.00 10.70 ? 277 THR A CA  1 
ATOM   2338 C C   . THR A 1 277 ? 30.276  19.905  58.451  1.00 12.98 ? 277 THR A C   1 
ATOM   2339 O O   . THR A 1 277 ? 29.242  20.075  57.794  1.00 18.13 ? 277 THR A O   1 
ATOM   2340 C CB  . THR A 1 277 ? 32.213  18.261  58.922  1.00 13.66 ? 277 THR A CB  1 
ATOM   2341 O OG1 . THR A 1 277 ? 32.829  19.223  59.783  1.00 14.04 ? 277 THR A OG1 1 
ATOM   2342 C CG2 . THR A 1 277 ? 32.838  18.356  57.535  1.00 18.76 ? 277 THR A CG2 1 
ATOM   2343 N N   . ASP A 1 278 ? 31.021  20.912  58.871  1.00 13.08 ? 278 ASP A N   1 
ATOM   2344 C CA  . ASP A 1 278 ? 30.586  22.298  58.754  1.00 15.90 ? 278 ASP A CA  1 
ATOM   2345 C C   . ASP A 1 278 ? 31.336  23.073  57.676  1.00 17.97 ? 278 ASP A C   1 
ATOM   2346 O O   . ASP A 1 278 ? 32.528  22.859  57.421  1.00 16.61 ? 278 ASP A O   1 
ATOM   2347 C CB  . ASP A 1 278 ? 30.746  23.040  60.087  1.00 16.39 ? 278 ASP A CB  1 
ATOM   2348 C CG  . ASP A 1 278 ? 30.206  24.462  60.034  1.00 20.34 ? 278 ASP A CG  1 
ATOM   2349 O OD1 . ASP A 1 278 ? 28.991  24.644  59.784  1.00 18.80 ? 278 ASP A OD1 1 
ATOM   2350 O OD2 . ASP A 1 278 ? 30.996  25.399  60.232  1.00 21.95 ? 278 ASP A OD2 1 
ATOM   2351 N N   . GLU A 1 279 ? 30.609  24.040  57.106  1.00 18.63 ? 279 GLU A N   1 
ATOM   2352 C CA  . GLU A 1 279 ? 31.132  24.919  56.068  1.00 19.50 ? 279 GLU A CA  1 
ATOM   2353 C C   . GLU A 1 279 ? 32.374  25.710  56.509  1.00 19.32 ? 279 GLU A C   1 
ATOM   2354 O O   . GLU A 1 279 ? 33.264  25.957  55.688  1.00 22.90 ? 279 GLU A O   1 
ATOM   2355 C CB  . GLU A 1 279 ? 30.017  25.876  55.630  1.00 20.23 ? 279 GLU A CB  1 
ATOM   2356 C CG  . GLU A 1 279 ? 30.358  26.628  54.402  1.00 27.19 ? 279 GLU A CG  1 
ATOM   2357 C CD  . GLU A 1 279 ? 29.175  27.318  53.786  1.00 28.81 ? 279 GLU A CD  1 
ATOM   2358 O OE1 . GLU A 1 279 ? 28.055  27.235  54.347  1.00 20.34 ? 279 GLU A OE1 1 
ATOM   2359 O OE2 . GLU A 1 279 ? 29.382  27.935  52.722  1.00 31.73 ? 279 GLU A OE2 1 
ATOM   2360 N N   . VAL A 1 280 ? 32.468  26.114  57.780  1.00 20.88 ? 280 VAL A N   1 
ATOM   2361 C CA  . VAL A 1 280 ? 33.677  26.818  58.218  1.00 16.46 ? 280 VAL A CA  1 
ATOM   2362 C C   . VAL A 1 280 ? 34.900  25.919  58.112  1.00 20.72 ? 280 VAL A C   1 
ATOM   2363 O O   . VAL A 1 280 ? 35.988  26.372  57.737  1.00 24.10 ? 280 VAL A O   1 
ATOM   2364 C CB  . VAL A 1 280 ? 33.519  27.372  59.645  1.00 25.73 ? 280 VAL A CB  1 
ATOM   2365 C CG1 . VAL A 1 280 ? 34.847  27.994  60.107  1.00 26.13 ? 280 VAL A CG1 1 
ATOM   2366 C CG2 . VAL A 1 280 ? 32.410  28.405  59.697  1.00 28.74 ? 280 VAL A CG2 1 
ATOM   2367 N N   . ILE A 1 281 ? 34.750  24.629  58.428  1.00 19.93 ? 281 ILE A N   1 
ATOM   2368 C CA  . ILE A 1 281 ? 35.904  23.745  58.290  1.00 22.68 ? 281 ILE A CA  1 
ATOM   2369 C C   . ILE A 1 281 ? 36.309  23.626  56.821  1.00 23.68 ? 281 ILE A C   1 
ATOM   2370 O O   . ILE A 1 281 ? 37.504  23.638  56.484  1.00 21.44 ? 281 ILE A O   1 
ATOM   2371 C CB  . ILE A 1 281 ? 35.597  22.384  58.945  1.00 21.81 ? 281 ILE A CB  1 
ATOM   2372 C CG1 . ILE A 1 281 ? 35.482  22.577  60.463  1.00 22.41 ? 281 ILE A CG1 1 
ATOM   2373 C CG2 . ILE A 1 281 ? 36.671  21.343  58.540  1.00 23.58 ? 281 ILE A CG2 1 
ATOM   2374 C CD1 . ILE A 1 281 ? 34.866  21.403  61.211  1.00 23.17 ? 281 ILE A CD1 1 
ATOM   2375 N N   . LEU A 1 282 ? 35.321  23.526  55.924  1.00 23.69 ? 282 LEU A N   1 
ATOM   2376 C CA  . LEU A 1 282 ? 35.603  23.536  54.490  1.00 22.47 ? 282 LEU A CA  1 
ATOM   2377 C C   . LEU A 1 282 ? 36.416  24.758  54.104  1.00 26.97 ? 282 LEU A C   1 
ATOM   2378 O O   . LEU A 1 282 ? 37.465  24.647  53.453  1.00 29.84 ? 282 LEU A O   1 
ATOM   2379 C CB  . LEU A 1 282 ? 34.291  23.503  53.686  1.00 26.93 ? 282 LEU A CB  1 
ATOM   2380 C CG  . LEU A 1 282 ? 34.420  23.424  52.158  1.00 24.52 ? 282 LEU A CG  1 
ATOM   2381 C CD1 . LEU A 1 282 ? 35.171  22.174  51.718  1.00 32.06 ? 282 LEU A CD1 1 
ATOM   2382 C CD2 . LEU A 1 282 ? 33.041  23.520  51.482  1.00 25.03 ? 282 LEU A CD2 1 
ATOM   2383 N N   . LYS A 1 283 ? 35.956  25.940  54.521  1.00 25.07 ? 283 LYS A N   1 
ATOM   2384 C CA  . LYS A 1 283 ? 36.649  27.174  54.160  1.00 25.04 ? 283 LYS A CA  1 
ATOM   2385 C C   . LYS A 1 283 ? 38.064  27.211  54.720  1.00 25.64 ? 283 LYS A C   1 
ATOM   2386 O O   . LYS A 1 283 ? 38.968  27.771  54.086  1.00 26.29 ? 283 LYS A O   1 
ATOM   2387 C CB  . LYS A 1 283 ? 35.851  28.382  54.646  1.00 29.56 ? 283 LYS A CB  1 
ATOM   2388 C CG  . LYS A 1 283 ? 34.465  28.476  54.036  1.00 39.50 ? 283 LYS A CG  1 
ATOM   2389 C CD  . LYS A 1 283 ? 33.803  29.800  54.376  1.00 50.85 ? 283 LYS A CD  1 
ATOM   2390 C CE  . LYS A 1 283 ? 32.631  30.066  53.442  1.00 59.30 ? 283 LYS A CE  1 
ATOM   2391 N NZ  . LYS A 1 283 ? 32.821  29.352  52.142  1.00 64.37 ? 283 LYS A NZ  1 
ATOM   2392 N N   . ASN A 1 284 ? 38.284  26.611  55.891  1.00 27.75 ? 284 ASN A N   1 
ATOM   2393 C CA  . ASN A 1 284 ? 39.621  26.577  56.480  1.00 27.97 ? 284 ASN A CA  1 
ATOM   2394 C C   . ASN A 1 284 ? 40.550  25.571  55.812  1.00 30.97 ? 284 ASN A C   1 
ATOM   2395 O O   . ASN A 1 284 ? 41.772  25.700  55.942  1.00 30.10 ? 284 ASN A O   1 
ATOM   2396 C CB  . ASN A 1 284 ? 39.536  26.234  57.969  1.00 27.15 ? 284 ASN A CB  1 
ATOM   2397 C CG  . ASN A 1 284 ? 39.075  27.393  58.814  1.00 31.39 ? 284 ASN A CG  1 
ATOM   2398 O OD1 . ASN A 1 284 ? 39.026  28.535  58.357  1.00 38.23 ? 284 ASN A OD1 1 
ATOM   2399 N ND2 . ASN A 1 284 ? 38.742  27.107  60.069  1.00 26.97 ? 284 ASN A ND2 1 
ATOM   2400 N N   . SER A 1 285 ? 40.005  24.569  55.124  1.00 29.34 ? 285 SER A N   1 
ATOM   2401 C CA  . SER A 1 285 ? 40.765  23.421  54.640  1.00 30.42 ? 285 SER A CA  1 
ATOM   2402 C C   . SER A 1 285 ? 41.017  23.443  53.144  1.00 40.13 ? 285 SER A C   1 
ATOM   2403 O O   . SER A 1 285 ? 42.087  23.025  52.700  1.00 48.44 ? 285 SER A O   1 
ATOM   2404 C CB  . SER A 1 285 ? 40.030  22.116  54.984  1.00 27.13 ? 285 SER A CB  1 
ATOM   2405 O OG  . SER A 1 285 ? 39.655  22.075  56.349  1.00 26.97 ? 285 SER A OG  1 
ATOM   2406 N N   . VAL A 1 286 ? 40.045  23.900  52.358  1.00 42.09 ? 286 VAL A N   1 
ATOM   2407 C CA  . VAL A 1 286 ? 40.082  23.801  50.905  1.00 47.15 ? 286 VAL A CA  1 
ATOM   2408 C C   . VAL A 1 286 ? 40.025  25.201  50.314  1.00 53.32 ? 286 VAL A C   1 
ATOM   2409 O O   . VAL A 1 286 ? 39.377  26.103  50.855  1.00 54.86 ? 286 VAL A O   1 
ATOM   2410 C CB  . VAL A 1 286 ? 38.919  22.936  50.364  1.00 49.60 ? 286 VAL A CB  1 
ATOM   2411 C CG1 . VAL A 1 286 ? 39.108  22.623  48.883  1.00 54.60 ? 286 VAL A CG1 1 
ATOM   2412 C CG2 . VAL A 1 286 ? 38.811  21.664  51.149  1.00 48.18 ? 286 VAL A CG2 1 
ATOM   2413 N N   . GLU A 1 287 ? 40.721  25.375  49.194  1.00 54.34 ? 287 GLU A N   1 
ATOM   2414 C CA  . GLU A 1 287 ? 40.672  26.617  48.434  1.00 60.26 ? 287 GLU A CA  1 
ATOM   2415 C C   . GLU A 1 287 ? 39.241  26.926  47.978  1.00 59.08 ? 287 GLU A C   1 
ATOM   2416 O O   . GLU A 1 287 ? 38.630  27.894  48.445  1.00 56.36 ? 287 GLU A O   1 
ATOM   2417 C CB  . GLU A 1 287 ? 41.673  26.535  47.261  1.00 64.66 ? 287 GLU A CB  1 
ATOM   2418 C CG  . GLU A 1 287 ? 41.253  25.741  45.994  1.00 70.46 ? 287 GLU A CG  1 
ATOM   2419 C CD  . GLU A 1 287 ? 40.920  24.269  46.269  1.00 75.78 ? 287 GLU A CD  1 
ATOM   2420 O OE1 . GLU A 1 287 ? 41.783  23.525  46.790  1.00 78.25 ? 287 GLU A OE1 1 
ATOM   2421 O OE2 . GLU A 1 287 ? 39.771  23.863  45.982  1.00 76.90 ? 287 GLU A OE2 1 
ATOM   2422 N N   . ARG A 1 288 ? 38.678  26.066  47.128  1.00 55.63 ? 288 ARG A N   1 
ATOM   2423 C CA  . ARG A 1 288 ? 37.401  26.311  46.462  1.00 53.59 ? 288 ARG A CA  1 
ATOM   2424 C C   . ARG A 1 288 ? 36.333  25.656  47.321  1.00 47.62 ? 288 ARG A C   1 
ATOM   2425 O O   . ARG A 1 288 ? 35.978  24.492  47.141  1.00 50.62 ? 288 ARG A O   1 
ATOM   2426 C CB  . ARG A 1 288 ? 37.434  25.779  45.035  1.00 52.14 ? 288 ARG A CB  1 
ATOM   2427 C CG  . ARG A 1 288 ? 38.409  26.544  44.154  1.00 57.94 ? 288 ARG A CG  1 
ATOM   2428 C CD  . ARG A 1 288 ? 38.730  25.830  42.846  1.00 65.87 ? 288 ARG A CD  1 
ATOM   2429 N NE  . ARG A 1 288 ? 39.533  24.619  43.013  1.00 71.58 ? 288 ARG A NE  1 
ATOM   2430 C CZ  . ARG A 1 288 ? 39.104  23.395  42.717  1.00 73.55 ? 288 ARG A CZ  1 
ATOM   2431 N NH1 . ARG A 1 288 ? 39.897  22.345  42.893  1.00 72.43 ? 288 ARG A NH1 1 
ATOM   2432 N NH2 . ARG A 1 288 ? 37.878  23.223  42.238  1.00 74.31 ? 288 ARG A NH2 1 
ATOM   2433 N N   . ALA A 1 289 ? 35.834  26.415  48.289  1.00 41.23 ? 289 ALA A N   1 
ATOM   2434 C CA  . ALA A 1 289 ? 34.965  25.860  49.318  1.00 40.02 ? 289 ALA A CA  1 
ATOM   2435 C C   . ALA A 1 289 ? 33.502  25.992  48.896  1.00 34.88 ? 289 ALA A C   1 
ATOM   2436 O O   . ALA A 1 289 ? 32.744  26.810  49.421  1.00 36.09 ? 289 ALA A O   1 
ATOM   2437 C CB  . ALA A 1 289 ? 35.228  26.551  50.650  1.00 44.66 ? 289 ALA A CB  1 
ATOM   2438 N N   . SER A 1 290 ? 33.101  25.156  47.930  1.00 26.43 ? 290 SER A N   1 
ATOM   2439 C CA  . SER A 1 290 ? 31.676  25.028  47.611  1.00 27.76 ? 290 SER A CA  1 
ATOM   2440 C C   . SER A 1 290 ? 31.040  23.982  48.509  1.00 25.72 ? 290 SER A C   1 
ATOM   2441 O O   . SER A 1 290 ? 31.458  22.818  48.475  1.00 28.06 ? 290 SER A O   1 
ATOM   2442 C CB  . SER A 1 290 ? 31.448  24.624  46.169  1.00 24.95 ? 290 SER A CB  1 
ATOM   2443 O OG  . SER A 1 290 ? 30.052  24.418  45.956  1.00 28.19 ? 290 SER A OG  1 
ATOM   2444 N N   . PRO A 1 291 ? 30.025  24.326  49.300  1.00 21.30 ? 291 PRO A N   1 
ATOM   2445 C CA  . PRO A 1 291 ? 29.364  23.317  50.119  1.00 19.47 ? 291 PRO A CA  1 
ATOM   2446 C C   . PRO A 1 291 ? 28.374  22.441  49.362  1.00 15.30 ? 291 PRO A C   1 
ATOM   2447 O O   . PRO A 1 291 ? 27.673  21.668  50.012  1.00 17.62 ? 291 PRO A O   1 
ATOM   2448 C CB  . PRO A 1 291 ? 28.642  24.167  51.178  1.00 24.14 ? 291 PRO A CB  1 
ATOM   2449 C CG  . PRO A 1 291 ? 28.361  25.463  50.461  1.00 20.34 ? 291 PRO A CG  1 
ATOM   2450 C CD  . PRO A 1 291 ? 29.512  25.687  49.551  1.00 24.17 ? 291 PRO A CD  1 
ATOM   2451 N N   . TYR A 1 292 ? 28.296  22.514  48.026  1.00 17.62 ? 292 TYR A N   1 
ATOM   2452 C CA  . TYR A 1 292 ? 27.210  21.852  47.311  1.00 16.11 ? 292 TYR A CA  1 
ATOM   2453 C C   . TYR A 1 292 ? 27.652  20.589  46.593  1.00 17.18 ? 292 TYR A C   1 
ATOM   2454 O O   . TYR A 1 292 ? 26.875  20.033  45.817  1.00 16.28 ? 292 TYR A O   1 
ATOM   2455 C CB  . TYR A 1 292 ? 26.543  22.844  46.346  1.00 19.24 ? 292 TYR A CB  1 
ATOM   2456 C CG  . TYR A 1 292 ? 26.042  24.062  47.096  1.00 19.65 ? 292 TYR A CG  1 
ATOM   2457 C CD1 . TYR A 1 292 ? 25.272  23.922  48.237  1.00 17.72 ? 292 TYR A CD1 1 
ATOM   2458 C CD2 . TYR A 1 292 ? 26.355  25.346  46.676  1.00 24.80 ? 292 TYR A CD2 1 
ATOM   2459 C CE1 . TYR A 1 292 ? 24.824  25.032  48.951  1.00 20.85 ? 292 TYR A CE1 1 
ATOM   2460 C CE2 . TYR A 1 292 ? 25.898  26.464  47.393  1.00 24.54 ? 292 TYR A CE2 1 
ATOM   2461 C CZ  . TYR A 1 292 ? 25.134  26.285  48.519  1.00 24.29 ? 292 TYR A CZ  1 
ATOM   2462 O OH  . TYR A 1 292 ? 24.676  27.373  49.240  1.00 28.05 ? 292 TYR A OH  1 
ATOM   2463 N N   . LEU A 1 293 ? 28.857  20.108  46.873  1.00 16.61 ? 293 LEU A N   1 
ATOM   2464 C CA  . LEU A 1 293 ? 29.436  18.942  46.222  1.00 15.16 ? 293 LEU A CA  1 
ATOM   2465 C C   . LEU A 1 293 ? 29.495  17.785  47.212  1.00 14.32 ? 293 LEU A C   1 
ATOM   2466 O O   . LEU A 1 293 ? 29.485  17.977  48.428  1.00 16.25 ? 293 LEU A O   1 
ATOM   2467 C CB  . LEU A 1 293 ? 30.860  19.228  45.716  1.00 16.21 ? 293 LEU A CB  1 
ATOM   2468 C CG  . LEU A 1 293 ? 31.190  20.131  44.530  1.00 29.72 ? 293 LEU A CG  1 
ATOM   2469 C CD1 . LEU A 1 293 ? 30.435  21.413  44.535  1.00 32.31 ? 293 LEU A CD1 1 
ATOM   2470 C CD2 . LEU A 1 293 ? 32.708  20.381  44.488  1.00 23.15 ? 293 LEU A CD2 1 
ATOM   2471 N N   . ARG A 1 294 ? 29.570  16.571  46.679  1.00 15.85 ? 294 ARG A N   1 
ATOM   2472 C CA  . ARG A 1 294 ? 29.984  15.428  47.488  1.00 17.37 ? 294 ARG A CA  1 
ATOM   2473 C C   . ARG A 1 294 ? 31.507  15.373  47.453  1.00 14.91 ? 294 ARG A C   1 
ATOM   2474 O O   . ARG A 1 294 ? 32.094  15.182  46.380  1.00 18.41 ? 294 ARG A O   1 
ATOM   2475 C CB  . ARG A 1 294 ? 29.403  14.111  46.961  1.00 16.71 ? 294 ARG A CB  1 
ATOM   2476 C CG  . ARG A 1 294 ? 29.748  12.912  47.870  1.00 17.97 ? 294 ARG A CG  1 
ATOM   2477 C CD  . ARG A 1 294 ? 28.938  11.647  47.522  1.00 19.02 ? 294 ARG A CD  1 
ATOM   2478 N NE  . ARG A 1 294 ? 29.102  11.243  46.134  1.00 23.34 ? 294 ARG A NE  1 
ATOM   2479 C CZ  . ARG A 1 294 ? 28.107  11.002  45.288  1.00 21.88 ? 294 ARG A CZ  1 
ATOM   2480 N NH1 . ARG A 1 294 ? 26.848  11.100  45.694  1.00 19.54 ? 294 ARG A NH1 1 
ATOM   2481 N NH2 . ARG A 1 294 ? 28.376  10.653  44.037  1.00 23.39 ? 294 ARG A NH2 1 
ATOM   2482 N N   . TYR A 1 295 ? 32.147  15.507  48.615  1.00 14.39 ? 295 TYR A N   1 
ATOM   2483 C CA  . TYR A 1 295 ? 33.606  15.430  48.695  1.00 16.99 ? 295 TYR A CA  1 
ATOM   2484 C C   . TYR A 1 295 ? 34.041  14.028  49.086  1.00 16.17 ? 295 TYR A C   1 
ATOM   2485 O O   . TYR A 1 295 ? 33.318  13.319  49.785  1.00 16.91 ? 295 TYR A O   1 
ATOM   2486 C CB  . TYR A 1 295 ? 34.160  16.413  49.725  1.00 14.87 ? 295 TYR A CB  1 
ATOM   2487 C CG  . TYR A 1 295 ? 34.079  17.833  49.262  1.00 16.33 ? 295 TYR A CG  1 
ATOM   2488 C CD1 . TYR A 1 295 ? 32.936  18.576  49.481  1.00 18.64 ? 295 TYR A CD1 1 
ATOM   2489 C CD2 . TYR A 1 295 ? 35.132  18.419  48.585  1.00 17.58 ? 295 TYR A CD2 1 
ATOM   2490 C CE1 . TYR A 1 295 ? 32.843  19.888  49.050  1.00 15.80 ? 295 TYR A CE1 1 
ATOM   2491 C CE2 . TYR A 1 295 ? 35.051  19.728  48.151  1.00 19.95 ? 295 TYR A CE2 1 
ATOM   2492 C CZ  . TYR A 1 295 ? 33.896  20.455  48.404  1.00 18.54 ? 295 TYR A CZ  1 
ATOM   2493 O OH  . TYR A 1 295 ? 33.820  21.755  47.954  1.00 20.00 ? 295 TYR A OH  1 
ATOM   2494 N N   . TYR A 1 296 ? 35.250  13.636  48.649  1.00 18.31 ? 296 TYR A N   1 
ATOM   2495 C CA  . TYR A 1 296 ? 35.850  12.383  49.104  1.00 18.05 ? 296 TYR A CA  1 
ATOM   2496 C C   . TYR A 1 296 ? 37.151  12.716  49.811  1.00 17.95 ? 296 TYR A C   1 
ATOM   2497 O O   . TYR A 1 296 ? 38.118  13.153  49.165  1.00 18.29 ? 296 TYR A O   1 
ATOM   2498 C CB  . TYR A 1 296 ? 36.110  11.418  47.950  1.00 20.65 ? 296 TYR A CB  1 
ATOM   2499 C CG  . TYR A 1 296 ? 34.898  11.131  47.099  1.00 18.52 ? 296 TYR A CG  1 
ATOM   2500 C CD1 . TYR A 1 296 ? 33.763  10.542  47.643  1.00 17.28 ? 296 TYR A CD1 1 
ATOM   2501 C CD2 . TYR A 1 296 ? 34.900  11.442  45.740  1.00 20.41 ? 296 TYR A CD2 1 
ATOM   2502 C CE1 . TYR A 1 296 ? 32.644  10.279  46.834  1.00 17.67 ? 296 TYR A CE1 1 
ATOM   2503 C CE2 . TYR A 1 296 ? 33.797  11.185  44.930  1.00 23.05 ? 296 TYR A CE2 1 
ATOM   2504 C CZ  . TYR A 1 296 ? 32.663  10.602  45.504  1.00 21.89 ? 296 TYR A CZ  1 
ATOM   2505 O OH  . TYR A 1 296 ? 31.566  10.330  44.710  1.00 23.96 ? 296 TYR A OH  1 
ATOM   2506 N N   . PHE A 1 297 ? 37.184  12.496  51.118  1.00 16.06 ? 297 PHE A N   1 
ATOM   2507 C CA  . PHE A 1 297 ? 38.422  12.710  51.859  1.00 16.21 ? 297 PHE A CA  1 
ATOM   2508 C C   . PHE A 1 297 ? 39.396  11.598  51.513  1.00 17.15 ? 297 PHE A C   1 
ATOM   2509 O O   . PHE A 1 297 ? 39.158  10.434  51.846  1.00 19.75 ? 297 PHE A O   1 
ATOM   2510 C CB  . PHE A 1 297 ? 38.165  12.762  53.363  1.00 15.72 ? 297 PHE A CB  1 
ATOM   2511 C CG  . PHE A 1 297 ? 39.413  12.938  54.167  1.00 15.87 ? 297 PHE A CG  1 
ATOM   2512 C CD1 . PHE A 1 297 ? 40.034  14.177  54.229  1.00 16.31 ? 297 PHE A CD1 1 
ATOM   2513 C CD2 . PHE A 1 297 ? 39.984  11.863  54.826  1.00 16.48 ? 297 PHE A CD2 1 
ATOM   2514 C CE1 . PHE A 1 297 ? 41.195  14.353  54.950  1.00 16.97 ? 297 PHE A CE1 1 
ATOM   2515 C CE2 . PHE A 1 297 ? 41.165  12.026  55.552  1.00 18.03 ? 297 PHE A CE2 1 
ATOM   2516 C CZ  . PHE A 1 297 ? 41.753  13.285  55.633  1.00 18.45 ? 297 PHE A CZ  1 
ATOM   2517 N N   . ARG A 1 298 ? 40.482  11.966  50.825  1.00 18.28 ? 298 ARG A N   1 
ATOM   2518 C CA  . ARG A 1 298 ? 41.540  11.037  50.402  1.00 19.41 ? 298 ARG A CA  1 
ATOM   2519 C C   . ARG A 1 298 ? 40.970  9.852   49.626  1.00 22.13 ? 298 ARG A C   1 
ATOM   2520 O O   . ARG A 1 298 ? 41.529  8.754   49.637  1.00 22.11 ? 298 ARG A O   1 
ATOM   2521 C CB  . ARG A 1 298 ? 42.387  10.578  51.602  1.00 19.49 ? 298 ARG A CB  1 
ATOM   2522 C CG  . ARG A 1 298 ? 43.065  11.762  52.270  1.00 24.68 ? 298 ARG A CG  1 
ATOM   2523 C CD  . ARG A 1 298 ? 44.065  11.417  53.362  1.00 24.75 ? 298 ARG A CD  1 
ATOM   2524 N NE  . ARG A 1 298 ? 44.598  12.661  53.909  1.00 22.27 ? 298 ARG A NE  1 
ATOM   2525 C CZ  . ARG A 1 298 ? 45.181  12.796  55.098  1.00 25.52 ? 298 ARG A CZ  1 
ATOM   2526 N NH1 . ARG A 1 298 ? 45.341  11.751  55.912  1.00 21.65 ? 298 ARG A NH1 1 
ATOM   2527 N NH2 . ARG A 1 298 ? 45.594  14.002  55.476  1.00 24.29 ? 298 ARG A NH2 1 
ATOM   2528 N N   . GLU A 1 299 ? 39.847  10.086  48.939  1.00 22.01 ? 299 GLU A N   1 
ATOM   2529 C CA  . GLU A 1 299 ? 39.157  9.078   48.131  1.00 19.37 ? 299 GLU A CA  1 
ATOM   2530 C C   . GLU A 1 299 ? 38.714  7.861   48.947  1.00 18.86 ? 299 GLU A C   1 
ATOM   2531 O O   . GLU A 1 299 ? 38.530  6.775   48.387  1.00 19.49 ? 299 GLU A O   1 
ATOM   2532 C CB  . GLU A 1 299 ? 40.027  8.622   46.949  1.00 23.28 ? 299 GLU A CB  1 
ATOM   2533 C CG  . GLU A 1 299 ? 40.192  9.679   45.877  1.00 22.46 ? 299 GLU A CG  1 
ATOM   2534 C CD  . GLU A 1 299 ? 38.982  9.780   44.939  1.00 35.51 ? 299 GLU A CD  1 
ATOM   2535 O OE1 . GLU A 1 299 ? 39.206  10.110  43.748  1.00 45.96 ? 299 GLU A OE1 1 
ATOM   2536 O OE2 . GLU A 1 299 ? 37.821  9.537   45.378  1.00 29.75 ? 299 GLU A OE2 1 
ATOM   2537 N N   . LEU A 1 300 ? 38.500  8.030   50.257  1.00 18.38 ? 300 LEU A N   1 
ATOM   2538 C CA  . LEU A 1 300 ? 38.188  6.940   51.178  1.00 18.25 ? 300 LEU A CA  1 
ATOM   2539 C C   . LEU A 1 300 ? 36.836  7.101   51.864  1.00 19.75 ? 300 LEU A C   1 
ATOM   2540 O O   . LEU A 1 300 ? 36.143  6.110   52.068  1.00 19.27 ? 300 LEU A O   1 
ATOM   2541 C CB  . LEU A 1 300 ? 39.283  6.840   52.253  1.00 24.45 ? 300 LEU A CB  1 
ATOM   2542 C CG  . LEU A 1 300 ? 40.462  5.857   52.193  1.00 29.61 ? 300 LEU A CG  1 
ATOM   2543 C CD1 . LEU A 1 300 ? 40.366  4.847   51.077  1.00 20.90 ? 300 LEU A CD1 1 
ATOM   2544 C CD2 . LEU A 1 300 ? 41.804  6.551   52.214  1.00 30.23 ? 300 LEU A CD2 1 
ATOM   2545 N N   . ILE A 1 301 ? 36.452  8.311   52.254  1.00 17.11 ? 301 ILE A N   1 
ATOM   2546 C CA  . ILE A 1 301 ? 35.196  8.527   52.980  1.00 16.25 ? 301 ILE A CA  1 
ATOM   2547 C C   . ILE A 1 301 ? 34.495  9.731   52.367  1.00 18.41 ? 301 ILE A C   1 
ATOM   2548 O O   . ILE A 1 301 ? 35.131  10.756  52.106  1.00 21.19 ? 301 ILE A O   1 
ATOM   2549 C CB  . ILE A 1 301 ? 35.427  8.706   54.502  1.00 16.09 ? 301 ILE A CB  1 
ATOM   2550 C CG1 . ILE A 1 301 ? 34.107  8.999   55.240  1.00 13.88 ? 301 ILE A CG1 1 
ATOM   2551 C CG2 . ILE A 1 301 ? 36.477  9.774   54.826  1.00 21.53 ? 301 ILE A CG2 1 
ATOM   2552 C CD1 . ILE A 1 301 ? 34.282  8.953   56.785  1.00 17.45 ? 301 ILE A CD1 1 
ATOM   2553 N N   . SER A 1 302 ? 33.186  9.613   52.129  1.00 15.99 ? 302 SER A N   1 
ATOM   2554 C CA  . SER A 1 302 ? 32.442  10.734  51.570  1.00 15.33 ? 302 SER A CA  1 
ATOM   2555 C C   . SER A 1 302 ? 32.136  11.750  52.651  1.00 17.30 ? 302 SER A C   1 
ATOM   2556 O O   . SER A 1 302 ? 31.814  11.396  53.790  1.00 15.80 ? 302 SER A O   1 
ATOM   2557 C CB  . SER A 1 302 ? 31.140  10.265  50.926  1.00 17.70 ? 302 SER A CB  1 
ATOM   2558 O OG  . SER A 1 302 ? 31.442  9.387   49.850  1.00 19.70 ? 302 SER A OG  1 
ATOM   2559 N N   . VAL A 1 303 ? 32.236  13.021  52.297  1.00 15.86 ? 303 VAL A N   1 
ATOM   2560 C CA  . VAL A 1 303 ? 32.025  14.098  53.258  1.00 12.71 ? 303 VAL A CA  1 
ATOM   2561 C C   . VAL A 1 303 ? 31.152  15.159  52.609  1.00 13.57 ? 303 VAL A C   1 
ATOM   2562 O O   . VAL A 1 303 ? 31.453  15.625  51.508  1.00 16.10 ? 303 VAL A O   1 
ATOM   2563 C CB  . VAL A 1 303 ? 33.360  14.722  53.718  1.00 16.48 ? 303 VAL A CB  1 
ATOM   2564 C CG1 . VAL A 1 303 ? 33.087  15.843  54.718  1.00 18.61 ? 303 VAL A CG1 1 
ATOM   2565 C CG2 . VAL A 1 303 ? 34.275  13.656  54.327  1.00 15.71 ? 303 VAL A CG2 1 
ATOM   2566 N N   . PHE A 1 304 ? 30.054  15.523  53.273  1.00 13.60 ? 304 PHE A N   1 
ATOM   2567 C CA  . PHE A 1 304 ? 29.292  16.687  52.858  1.00 10.85 ? 304 PHE A CA  1 
ATOM   2568 C C   . PHE A 1 304 ? 29.467  17.764  53.906  1.00 12.09 ? 304 PHE A C   1 
ATOM   2569 O O   . PHE A 1 304 ? 29.636  17.475  55.088  1.00 13.25 ? 304 PHE A O   1 
ATOM   2570 C CB  . PHE A 1 304 ? 27.797  16.399  52.732  1.00 12.28 ? 304 PHE A CB  1 
ATOM   2571 C CG  . PHE A 1 304 ? 27.435  15.531  51.561  1.00 12.30 ? 304 PHE A CG  1 
ATOM   2572 C CD1 . PHE A 1 304 ? 27.186  16.079  50.314  1.00 13.48 ? 304 PHE A CD1 1 
ATOM   2573 C CD2 . PHE A 1 304 ? 27.291  14.166  51.738  1.00 12.45 ? 304 PHE A CD2 1 
ATOM   2574 C CE1 . PHE A 1 304 ? 26.819  15.285  49.227  1.00 15.16 ? 304 PHE A CE1 1 
ATOM   2575 C CE2 . PHE A 1 304 ? 26.909  13.336  50.652  1.00 14.70 ? 304 PHE A CE2 1 
ATOM   2576 C CZ  . PHE A 1 304 ? 26.678  13.903  49.403  1.00 14.51 ? 304 PHE A CZ  1 
ATOM   2577 N N   . PHE A 1 305 ? 29.447  19.008  53.453  1.00 11.70 ? 305 PHE A N   1 
ATOM   2578 C CA  . PHE A 1 305 ? 29.552  20.152  54.340  1.00 14.92 ? 305 PHE A CA  1 
ATOM   2579 C C   . PHE A 1 305 ? 28.200  20.835  54.384  1.00 14.63 ? 305 PHE A C   1 
ATOM   2580 O O   . PHE A 1 305 ? 27.637  21.148  53.326  1.00 14.88 ? 305 PHE A O   1 
ATOM   2581 C CB  . PHE A 1 305 ? 30.633  21.088  53.839  1.00 15.45 ? 305 PHE A CB  1 
ATOM   2582 C CG  . PHE A 1 305 ? 32.008  20.465  53.864  1.00 17.14 ? 305 PHE A CG  1 
ATOM   2583 C CD1 . PHE A 1 305 ? 32.458  19.685  52.799  1.00 23.27 ? 305 PHE A CD1 1 
ATOM   2584 C CD2 . PHE A 1 305 ? 32.840  20.637  54.960  1.00 19.57 ? 305 PHE A CD2 1 
ATOM   2585 C CE1 . PHE A 1 305 ? 33.714  19.103  52.815  1.00 22.85 ? 305 PHE A CE1 1 
ATOM   2586 C CE2 . PHE A 1 305 ? 34.107  20.065  54.978  1.00 19.97 ? 305 PHE A CE2 1 
ATOM   2587 C CZ  . PHE A 1 305 ? 34.534  19.286  53.915  1.00 22.17 ? 305 PHE A CZ  1 
ATOM   2588 N N   . ARG A 1 306 ? 27.673  21.043  55.597  1.00 13.56 ? 306 ARG A N   1 
ATOM   2589 C CA  . ARG A 1 306 ? 26.346  21.647  55.706  1.00 10.99 ? 306 ARG A CA  1 
ATOM   2590 C C   . ARG A 1 306 ? 26.374  23.097  55.229  1.00 14.17 ? 306 ARG A C   1 
ATOM   2591 O O   . ARG A 1 306 ? 27.384  23.789  55.335  1.00 15.22 ? 306 ARG A O   1 
ATOM   2592 C CB  . ARG A 1 306 ? 25.842  21.600  57.138  1.00 13.88 ? 306 ARG A CB  1 
ATOM   2593 C CG  . ARG A 1 306 ? 26.502  22.581  58.059  1.00 18.20 ? 306 ARG A CG  1 
ATOM   2594 C CD  . ARG A 1 306 ? 25.837  22.580  59.445  1.00 16.95 ? 306 ARG A CD  1 
ATOM   2595 N NE  . ARG A 1 306 ? 26.488  23.614  60.228  1.00 15.87 ? 306 ARG A NE  1 
ATOM   2596 C CZ  . ARG A 1 306 ? 25.979  24.222  61.291  1.00 12.09 ? 306 ARG A CZ  1 
ATOM   2597 N NH1 . ARG A 1 306 ? 24.784  23.899  61.754  1.00 12.67 ? 306 ARG A NH1 1 
ATOM   2598 N NH2 . ARG A 1 306 ? 26.689  25.187  61.880  1.00 12.61 ? 306 ARG A NH2 1 
ATOM   2599 N N   . ASP A 1 307 ? 25.235  23.548  54.700  1.00 12.52 ? 307 ASP A N   1 
ATOM   2600 C CA  . ASP A 1 307 ? 25.038  24.963  54.411  1.00 12.76 ? 307 ASP A CA  1 
ATOM   2601 C C   . ASP A 1 307 ? 24.790  25.643  55.753  1.00 16.26 ? 307 ASP A C   1 
ATOM   2602 O O   . ASP A 1 307 ? 23.728  25.459  56.367  1.00 11.54 ? 307 ASP A O   1 
ATOM   2603 C CB  . ASP A 1 307 ? 23.866  25.162  53.448  1.00 13.76 ? 307 ASP A CB  1 
ATOM   2604 C CG  . ASP A 1 307 ? 23.712  26.591  53.011  1.00 21.11 ? 307 ASP A CG  1 
ATOM   2605 O OD1 . ASP A 1 307 ? 23.751  27.476  53.880  1.00 19.18 ? 307 ASP A OD1 1 
ATOM   2606 O OD2 . ASP A 1 307 ? 23.548  26.840  51.796  1.00 24.14 ? 307 ASP A OD2 1 
ATOM   2607 N N   . LYS A 1 308 ? 25.790  26.379  56.230  1.00 13.56 ? 308 LYS A N   1 
ATOM   2608 C CA  . LYS A 1 308 ? 25.697  26.967  57.554  1.00 14.98 ? 308 LYS A CA  1 
ATOM   2609 C C   . LYS A 1 308 ? 24.629  28.048  57.602  1.00 15.85 ? 308 LYS A C   1 
ATOM   2610 O O   . LYS A 1 308 ? 23.879  28.144  58.581  1.00 13.90 ? 308 LYS A O   1 
ATOM   2611 C CB  . LYS A 1 308 ? 27.058  27.525  57.942  1.00 18.83 ? 308 LYS A CB  1 
ATOM   2612 C CG  . LYS A 1 308 ? 27.054  28.373  59.178  1.00 23.04 ? 308 LYS A CG  1 
ATOM   2613 C CD  . LYS A 1 308 ? 28.481  28.679  59.555  1.00 23.12 ? 308 LYS A CD  1 
ATOM   2614 C CE  . LYS A 1 308 ? 28.590  30.041  60.194  1.00 41.02 ? 308 LYS A CE  1 
ATOM   2615 N NZ  . LYS A 1 308 ? 28.411  29.920  61.659  1.00 47.58 ? 308 LYS A NZ  1 
ATOM   2616 N N   . THR A 1 309 ? 24.501  28.835  56.534  1.00 12.56 ? 309 THR A N   1 
ATOM   2617 C CA  . THR A 1 309 ? 23.516  29.911  56.546  1.00 14.62 ? 309 THR A CA  1 
ATOM   2618 C C   . THR A 1 309 ? 22.099  29.368  56.702  1.00 13.73 ? 309 THR A C   1 
ATOM   2619 O O   . THR A 1 309 ? 21.347  29.827  57.572  1.00 13.60 ? 309 THR A O   1 
ATOM   2620 C CB  . THR A 1 309 ? 23.633  30.754  55.272  1.00 17.59 ? 309 THR A CB  1 
ATOM   2621 O OG1 . THR A 1 309 ? 24.875  31.471  55.294  1.00 19.14 ? 309 THR A OG1 1 
ATOM   2622 C CG2 . THR A 1 309 ? 22.477  31.730  55.198  1.00 17.28 ? 309 THR A CG2 1 
ATOM   2623 N N   . LEU A 1 310 ? 21.724  28.344  55.903  1.00 11.61 ? 310 LEU A N   1 
ATOM   2624 C CA  . LEU A 1 310 ? 20.377  27.777  56.009  1.00 11.67 ? 310 LEU A CA  1 
ATOM   2625 C C   . LEU A 1 310 ? 20.164  27.059  57.342  1.00 13.43 ? 310 LEU A C   1 
ATOM   2626 O O   . LEU A 1 310 ? 19.086  27.165  57.940  1.00 13.07 ? 310 LEU A O   1 
ATOM   2627 C CB  . LEU A 1 310 ? 20.101  26.819  54.853  1.00 14.15 ? 310 LEU A CB  1 
ATOM   2628 C CG  . LEU A 1 310 ? 20.140  27.500  53.485  1.00 17.12 ? 310 LEU A CG  1 
ATOM   2629 C CD1 . LEU A 1 310 ? 20.055  26.436  52.384  1.00 17.47 ? 310 LEU A CD1 1 
ATOM   2630 C CD2 . LEU A 1 310 ? 19.024  28.513  53.345  1.00 17.98 ? 310 LEU A CD2 1 
ATOM   2631 N N   . SER A 1 311 ? 21.192  26.360  57.839  1.00 8.81  ? 311 SER A N   1 
ATOM   2632 C CA  . SER A 1 311 ? 21.094  25.674  59.123  1.00 11.71 ? 311 SER A CA  1 
ATOM   2633 C C   . SER A 1 311 ? 20.909  26.655  60.271  1.00 11.71 ? 311 SER A C   1 
ATOM   2634 O O   . SER A 1 311 ? 20.110  26.401  61.186  1.00 10.95 ? 311 SER A O   1 
ATOM   2635 C CB  . SER A 1 311 ? 22.359  24.844  59.344  1.00 10.65 ? 311 SER A CB  1 
ATOM   2636 O OG  . SER A 1 311 ? 22.476  23.874  58.300  1.00 13.16 ? 311 SER A OG  1 
ATOM   2637 N N   . ASP A 1 312 ? 21.622  27.773  60.224  1.00 11.80 ? 312 ASP A N   1 
ATOM   2638 C CA  . ASP A 1 312 ? 21.505  28.796  61.263  1.00 14.22 ? 312 ASP A CA  1 
ATOM   2639 C C   . ASP A 1 312 ? 20.213  29.603  61.157  1.00 13.16 ? 312 ASP A C   1 
ATOM   2640 O O   . ASP A 1 312 ? 19.722  30.089  62.181  1.00 11.21 ? 312 ASP A O   1 
ATOM   2641 C CB  . ASP A 1 312 ? 22.696  29.742  61.215  1.00 14.84 ? 312 ASP A CB  1 
ATOM   2642 C CG  . ASP A 1 312 ? 23.937  29.141  61.871  1.00 20.34 ? 312 ASP A CG  1 
ATOM   2643 O OD1 . ASP A 1 312 ? 23.806  28.128  62.582  1.00 18.53 ? 312 ASP A OD1 1 
ATOM   2644 O OD2 . ASP A 1 312 ? 25.035  29.683  61.666  1.00 20.55 ? 312 ASP A OD2 1 
ATOM   2645 N N   . LEU A 1 313 ? 19.637  29.764  59.957  1.00 11.50 ? 313 LEU A N   1 
ATOM   2646 C CA  . LEU A 1 313 ? 18.340  30.448  59.899  1.00 9.86  ? 313 LEU A CA  1 
ATOM   2647 C C   . LEU A 1 313 ? 17.277  29.667  60.637  1.00 9.90  ? 313 LEU A C   1 
ATOM   2648 O O   . LEU A 1 313 ? 16.472  30.248  61.375  1.00 12.65 ? 313 LEU A O   1 
ATOM   2649 C CB  . LEU A 1 313 ? 17.899  30.690  58.448  1.00 10.22 ? 313 LEU A CB  1 
ATOM   2650 C CG  . LEU A 1 313 ? 18.764  31.730  57.732  1.00 11.88 ? 313 LEU A CG  1 
ATOM   2651 C CD1 . LEU A 1 313 ? 18.426  31.743  56.256  1.00 17.16 ? 313 LEU A CD1 1 
ATOM   2652 C CD2 . LEU A 1 313 ? 18.564  33.148  58.293  1.00 14.82 ? 313 LEU A CD2 1 
ATOM   2653 N N   . ILE A 1 314 ? 17.229  28.346  60.422  1.00 8.71  ? 314 ILE A N   1 
ATOM   2654 C CA  . ILE A 1 314 ? 16.267  27.528  61.163  1.00 8.47  ? 314 ILE A CA  1 
ATOM   2655 C C   . ILE A 1 314 ? 16.606  27.542  62.648  1.00 13.06 ? 314 ILE A C   1 
ATOM   2656 O O   . ILE A 1 314 ? 15.723  27.692  63.502  1.00 10.11 ? 314 ILE A O   1 
ATOM   2657 C CB  . ILE A 1 314 ? 16.212  26.095  60.618  1.00 8.25  ? 314 ILE A CB  1 
ATOM   2658 C CG1 . ILE A 1 314 ? 15.691  26.111  59.185  1.00 10.27 ? 314 ILE A CG1 1 
ATOM   2659 C CG2 . ILE A 1 314 ? 15.262  25.269  61.487  1.00 10.17 ? 314 ILE A CG2 1 
ATOM   2660 C CD1 . ILE A 1 314 ? 15.698  24.718  58.527  1.00 11.84 ? 314 ILE A CD1 1 
ATOM   2661 N N   . GLY A 1 315 ? 17.891  27.449  62.982  1.00 9.75  ? 315 GLY A N   1 
ATOM   2662 C CA  . GLY A 1 315 ? 18.234  27.320  64.388  1.00 9.49  ? 315 GLY A CA  1 
ATOM   2663 C C   . GLY A 1 315 ? 18.087  28.603  65.184  1.00 11.58 ? 315 GLY A C   1 
ATOM   2664 O O   . GLY A 1 315 ? 17.857  28.558  66.398  1.00 15.54 ? 315 GLY A O   1 
ATOM   2665 N N   . PHE A 1 316 ? 18.288  29.756  64.546  1.00 11.09 ? 316 PHE A N   1 
ATOM   2666 C CA  . PHE A 1 316 ? 18.391  31.011  65.269  1.00 12.32 ? 316 PHE A CA  1 
ATOM   2667 C C   . PHE A 1 316 ? 17.537  32.152  64.744  1.00 11.58 ? 316 PHE A C   1 
ATOM   2668 O O   . PHE A 1 316 ? 17.262  33.068  65.521  1.00 14.12 ? 316 PHE A O   1 
ATOM   2669 C CB  . PHE A 1 316 ? 19.855  31.487  65.318  1.00 11.17 ? 316 PHE A CB  1 
ATOM   2670 C CG  . PHE A 1 316 ? 20.782  30.527  66.016  1.00 15.32 ? 316 PHE A CG  1 
ATOM   2671 C CD1 . PHE A 1 316 ? 21.420  29.509  65.308  1.00 20.64 ? 316 PHE A CD1 1 
ATOM   2672 C CD2 . PHE A 1 316 ? 21.000  30.638  67.394  1.00 19.73 ? 316 PHE A CD2 1 
ATOM   2673 C CE1 . PHE A 1 316 ? 22.280  28.612  65.967  1.00 22.53 ? 316 PHE A CE1 1 
ATOM   2674 C CE2 . PHE A 1 316 ? 21.855  29.758  68.058  1.00 22.72 ? 316 PHE A CE2 1 
ATOM   2675 C CZ  . PHE A 1 316 ? 22.493  28.745  67.341  1.00 22.96 ? 316 PHE A CZ  1 
ATOM   2676 N N   . SER A 1 317 ? 17.117  32.155  63.473  1.00 11.25 ? 317 SER A N   1 
ATOM   2677 C CA  . SER A 1 317 ? 16.407  33.303  62.911  1.00 11.09 ? 317 SER A CA  1 
ATOM   2678 C C   . SER A 1 317 ? 14.892  33.110  62.924  1.00 10.92 ? 317 SER A C   1 
ATOM   2679 O O   . SER A 1 317 ? 14.150  33.906  63.505  1.00 14.83 ? 317 SER A O   1 
ATOM   2680 C CB  . SER A 1 317 ? 16.868  33.554  61.465  1.00 11.37 ? 317 SER A CB  1 
ATOM   2681 O OG  . SER A 1 317 ? 16.431  34.851  61.060  1.00 12.40 ? 317 SER A OG  1 
ATOM   2682 N N   . TYR A 1 318 ? 14.426  31.999  62.338  1.00 10.31 ? 318 TYR A N   1 
ATOM   2683 C CA  . TYR A 1 318 ? 13.021  31.863  61.951  1.00 10.35 ? 318 TYR A CA  1 
ATOM   2684 C C   . TYR A 1 318 ? 12.067  31.747  63.134  1.00 10.35 ? 318 TYR A C   1 
ATOM   2685 O O   . TYR A 1 318 ? 10.852  31.918  62.950  1.00 10.63 ? 318 TYR A O   1 
ATOM   2686 C CB  . TYR A 1 318 ? 12.872  30.633  61.035  1.00 9.83  ? 318 TYR A CB  1 
ATOM   2687 C CG  . TYR A 1 318 ? 13.440  30.818  59.645  1.00 10.05 ? 318 TYR A CG  1 
ATOM   2688 C CD1 . TYR A 1 318 ? 13.628  32.107  59.085  1.00 10.81 ? 318 TYR A CD1 1 
ATOM   2689 C CD2 . TYR A 1 318 ? 13.803  29.696  58.898  1.00 12.58 ? 318 TYR A CD2 1 
ATOM   2690 C CE1 . TYR A 1 318 ? 14.157  32.253  57.771  1.00 11.82 ? 318 TYR A CE1 1 
ATOM   2691 C CE2 . TYR A 1 318 ? 14.323  29.818  57.608  1.00 13.96 ? 318 TYR A CE2 1 
ATOM   2692 C CZ  . TYR A 1 318 ? 14.474  31.062  57.049  1.00 11.23 ? 318 TYR A CZ  1 
ATOM   2693 O OH  . TYR A 1 318 ? 14.994  31.099  55.757  1.00 13.98 ? 318 TYR A OH  1 
ATOM   2694 N N   . HIS A 1 319 ? 12.557  31.460  64.341  1.00 10.35 ? 319 HIS A N   1 
ATOM   2695 C CA  . HIS A 1 319 ? 11.628  31.428  65.475  1.00 10.35 ? 319 HIS A CA  1 
ATOM   2696 C C   . HIS A 1 319 ? 10.878  32.731  65.622  1.00 11.53 ? 319 HIS A C   1 
ATOM   2697 O O   . HIS A 1 319 ? 9.753   32.741  66.147  1.00 15.06 ? 319 HIS A O   1 
ATOM   2698 C CB  . HIS A 1 319 ? 12.370  31.152  66.789  1.00 10.28 ? 319 HIS A CB  1 
ATOM   2699 C CG  . HIS A 1 319 ? 13.210  32.305  67.273  1.00 10.86 ? 319 HIS A CG  1 
ATOM   2700 N ND1 . HIS A 1 319 ? 12.770  33.229  68.202  1.00 18.45 ? 319 HIS A ND1 1 
ATOM   2701 C CD2 . HIS A 1 319 ? 14.502  32.630  67.005  1.00 13.96 ? 319 HIS A CD2 1 
ATOM   2702 C CE1 . HIS A 1 319 ? 13.735  34.102  68.446  1.00 18.49 ? 319 HIS A CE1 1 
ATOM   2703 N NE2 . HIS A 1 319 ? 14.795  33.767  67.732  1.00 21.40 ? 319 HIS A NE2 1 
ATOM   2704 N N   . ALA A 1 320 ? 11.461  33.839  65.140  1.00 11.67 ? 320 ALA A N   1 
ATOM   2705 C CA  . ALA A 1 320 ? 10.903  35.167  65.316  1.00 16.53 ? 320 ALA A CA  1 
ATOM   2706 C C   . ALA A 1 320 ? 10.126  35.672  64.099  1.00 21.64 ? 320 ALA A C   1 
ATOM   2707 O O   . ALA A 1 320 ? 9.604   36.786  64.138  1.00 33.91 ? 320 ALA A O   1 
ATOM   2708 C CB  . ALA A 1 320 ? 12.013  36.162  65.654  1.00 19.57 ? 320 ALA A CB  1 
ATOM   2709 N N   . TRP A 1 321 ? 10.008  34.881  63.040  1.00 12.53 ? 321 TRP A N   1 
ATOM   2710 C CA  . TRP A 1 321 ? 9.267   35.260  61.847  1.00 12.89 ? 321 TRP A CA  1 
ATOM   2711 C C   . TRP A 1 321 ? 7.851   34.690  61.879  1.00 12.87 ? 321 TRP A C   1 
ATOM   2712 O O   . TRP A 1 321 ? 7.604   33.627  62.457  1.00 15.93 ? 321 TRP A O   1 
ATOM   2713 C CB  . TRP A 1 321 ? 9.922   34.736  60.570  1.00 12.57 ? 321 TRP A CB  1 
ATOM   2714 C CG  . TRP A 1 321 ? 11.321  35.129  60.214  1.00 12.66 ? 321 TRP A CG  1 
ATOM   2715 C CD1 . TRP A 1 321 ? 12.415  35.087  61.000  1.00 12.42 ? 321 TRP A CD1 1 
ATOM   2716 C CD2 . TRP A 1 321 ? 11.765  35.534  58.909  1.00 13.13 ? 321 TRP A CD2 1 
ATOM   2717 N NE1 . TRP A 1 321 ? 13.530  35.452  60.272  1.00 12.72 ? 321 TRP A NE1 1 
ATOM   2718 C CE2 . TRP A 1 321 ? 13.152  35.722  58.981  1.00 13.15 ? 321 TRP A CE2 1 
ATOM   2719 C CE3 . TRP A 1 321 ? 11.110  35.746  57.691  1.00 13.64 ? 321 TRP A CE3 1 
ATOM   2720 C CZ2 . TRP A 1 321 ? 13.911  36.115  57.881  1.00 13.68 ? 321 TRP A CZ2 1 
ATOM   2721 C CZ3 . TRP A 1 321 ? 11.861  36.149  56.596  1.00 15.28 ? 321 TRP A CZ3 1 
ATOM   2722 C CH2 . TRP A 1 321 ? 13.252  36.324  56.705  1.00 14.18 ? 321 TRP A CH2 1 
ATOM   2723 N N   . ASN A 1 322 ? 6.955   35.349  61.156  1.00 14.08 ? 322 ASN A N   1 
ATOM   2724 C CA  . ASN A 1 322 ? 5.707   34.726  60.741  1.00 13.90 ? 322 ASN A CA  1 
ATOM   2725 C C   . ASN A 1 322 ? 6.055   33.484  59.945  1.00 15.23 ? 322 ASN A C   1 
ATOM   2726 O O   . ASN A 1 322 ? 6.933   33.539  59.083  1.00 15.24 ? 322 ASN A O   1 
ATOM   2727 C CB  . ASN A 1 322 ? 4.903   35.701  59.878  1.00 17.77 ? 322 ASN A CB  1 
ATOM   2728 C CG  . ASN A 1 322 ? 3.462   35.285  59.710  1.00 31.12 ? 322 ASN A CG  1 
ATOM   2729 O OD1 . ASN A 1 322 ? 2.906   34.547  60.537  1.00 37.64 ? 322 ASN A OD1 1 
ATOM   2730 N ND2 . ASN A 1 322 ? 2.834   35.768  58.643  1.00 30.55 ? 322 ASN A ND2 1 
ATOM   2731 N N   . ALA A 1 323 ? 5.397   32.360  60.256  1.00 13.98 ? 323 ALA A N   1 
ATOM   2732 C CA  . ALA A 1 323 ? 5.805   31.080  59.680  1.00 12.82 ? 323 ALA A CA  1 
ATOM   2733 C C   . ALA A 1 323 ? 5.791   31.090  58.155  1.00 13.76 ? 323 ALA A C   1 
ATOM   2734 O O   . ALA A 1 323 ? 6.727   30.581  57.523  1.00 11.95 ? 323 ALA A O   1 
ATOM   2735 C CB  . ALA A 1 323 ? 4.909   29.956  60.203  1.00 14.66 ? 323 ALA A CB  1 
ATOM   2736 N N   . GLU A 1 324 ? 4.735   31.631  57.539  1.00 15.33 ? 324 GLU A N   1 
ATOM   2737 C CA  . GLU A 1 324 ? 4.688   31.626  56.076  1.00 16.48 ? 324 GLU A CA  1 
ATOM   2738 C C   . GLU A 1 324 ? 5.838   32.443  55.473  1.00 17.27 ? 324 GLU A C   1 
ATOM   2739 O O   . GLU A 1 324 ? 6.404   32.060  54.448  1.00 15.66 ? 324 GLU A O   1 
ATOM   2740 C CB  . GLU A 1 324 ? 3.333   32.129  55.580  1.00 21.16 ? 324 GLU A CB  1 
ATOM   2741 C CG  . GLU A 1 324 ? 3.097   33.594  55.824  1.00 31.35 ? 324 GLU A CG  1 
ATOM   2742 C CD  . GLU A 1 324 ? 1.731   34.053  55.346  1.00 51.05 ? 324 GLU A CD  1 
ATOM   2743 O OE1 . GLU A 1 324 ? 1.536   35.282  55.212  1.00 59.88 ? 324 GLU A OE1 1 
ATOM   2744 O OE2 . GLU A 1 324 ? 0.859   33.187  55.110  1.00 53.49 ? 324 GLU A OE2 1 
ATOM   2745 N N   . ASP A 1 325 ? 6.225   33.553  56.108  1.00 16.89 ? 325 ASP A N   1 
ATOM   2746 C CA  . ASP A 1 325 ? 7.316   34.347  55.552  1.00 14.21 ? 325 ASP A CA  1 
ATOM   2747 C C   . ASP A 1 325 ? 8.683   33.705  55.738  1.00 13.40 ? 325 ASP A C   1 
ATOM   2748 O O   . ASP A 1 325 ? 9.568   33.887  54.884  1.00 13.63 ? 325 ASP A O   1 
ATOM   2749 C CB  . ASP A 1 325 ? 7.262   35.735  56.164  1.00 14.86 ? 325 ASP A CB  1 
ATOM   2750 C CG  . ASP A 1 325 ? 5.948   36.419  55.845  1.00 28.23 ? 325 ASP A CG  1 
ATOM   2751 O OD1 . ASP A 1 325 ? 5.629   36.550  54.639  1.00 27.34 ? 325 ASP A OD1 1 
ATOM   2752 O OD2 . ASP A 1 325 ? 5.212   36.774  56.782  1.00 32.85 ? 325 ASP A OD2 1 
ATOM   2753 N N   . ALA A 1 326 ? 8.886   32.947  56.827  1.00 12.58 ? 326 ALA A N   1 
ATOM   2754 C CA  . ALA A 1 326 ? 10.129  32.200  56.988  1.00 11.86 ? 326 ALA A CA  1 
ATOM   2755 C C   . ALA A 1 326 ? 10.237  31.111  55.921  1.00 12.01 ? 326 ALA A C   1 
ATOM   2756 O O   . ALA A 1 326 ? 11.306  30.915  55.331  1.00 11.55 ? 326 ALA A O   1 
ATOM   2757 C CB  . ALA A 1 326 ? 10.193  31.570  58.378  1.00 12.94 ? 326 ALA A CB  1 
ATOM   2758 N N   . VAL A 1 327 ? 9.124   30.428  55.634  1.00 11.72 ? 327 VAL A N   1 
ATOM   2759 C CA  . VAL A 1 327 ? 9.146   29.393  54.594  1.00 12.43 ? 327 VAL A CA  1 
ATOM   2760 C C   . VAL A 1 327 ? 9.430   30.007  53.225  1.00 12.70 ? 327 VAL A C   1 
ATOM   2761 O O   . VAL A 1 327 ? 10.255  29.484  52.461  1.00 12.93 ? 327 VAL A O   1 
ATOM   2762 C CB  . VAL A 1 327 ? 7.831   28.596  54.594  1.00 12.42 ? 327 VAL A CB  1 
ATOM   2763 C CG1 . VAL A 1 327 ? 7.807   27.629  53.398  1.00 12.75 ? 327 VAL A CG1 1 
ATOM   2764 C CG2 . VAL A 1 327 ? 7.715   27.764  55.888  1.00 11.20 ? 327 VAL A CG2 1 
ATOM   2765 N N   . ARG A 1 328 ? 8.786   31.130  52.902  1.00 14.31 ? 328 ARG A N   1 
ATOM   2766 C CA  . ARG A 1 328 ? 9.070   31.804  51.633  1.00 15.90 ? 328 ARG A CA  1 
ATOM   2767 C C   . ARG A 1 328 ? 10.540  32.215  51.550  1.00 15.63 ? 328 ARG A C   1 
ATOM   2768 O O   . ARG A 1 328 ? 11.172  32.071  50.494  1.00 16.31 ? 328 ARG A O   1 
ATOM   2769 C CB  . ARG A 1 328 ? 8.148   33.008  51.456  1.00 15.10 ? 328 ARG A CB  1 
ATOM   2770 C CG  . ARG A 1 328 ? 6.689   32.604  51.331  1.00 18.59 ? 328 ARG A CG  1 
ATOM   2771 C CD  . ARG A 1 328 ? 5.751   33.820  51.233  1.00 24.77 ? 328 ARG A CD  1 
ATOM   2772 N NE  . ARG A 1 328 ? 4.360   33.434  51.496  1.00 23.28 ? 328 ARG A NE  1 
ATOM   2773 C CZ  . ARG A 1 328 ? 3.365   34.287  51.711  1.00 22.58 ? 328 ARG A CZ  1 
ATOM   2774 N NH1 . ARG A 1 328 ? 3.582   35.601  51.682  1.00 22.73 ? 328 ARG A NH1 1 
ATOM   2775 N NH2 . ARG A 1 328 ? 2.140   33.819  51.950  1.00 27.42 ? 328 ARG A NH2 1 
ATOM   2776 N N   . ASP A 1 329 ? 11.112  32.708  52.664  1.00 13.66 ? 329 ASP A N   1 
ATOM   2777 C CA  . ASP A 1 329 ? 12.525  33.082  52.651  1.00 13.69 ? 329 ASP A CA  1 
ATOM   2778 C C   . ASP A 1 329 ? 13.399  31.874  52.364  1.00 13.07 ? 329 ASP A C   1 
ATOM   2779 O O   . ASP A 1 329 ? 14.344  31.954  51.558  1.00 13.48 ? 329 ASP A O   1 
ATOM   2780 C CB  . ASP A 1 329 ? 12.928  33.721  53.988  1.00 13.93 ? 329 ASP A CB  1 
ATOM   2781 C CG  . ASP A 1 329 ? 14.359  34.216  53.989  1.00 14.43 ? 329 ASP A CG  1 
ATOM   2782 O OD1 . ASP A 1 329 ? 14.606  35.285  53.376  1.00 17.40 ? 329 ASP A OD1 1 
ATOM   2783 O OD2 . ASP A 1 329 ? 15.212  33.566  54.606  1.00 15.04 ? 329 ASP A OD2 1 
ATOM   2784 N N   . PHE A 1 330 ? 13.097  30.754  53.025  1.00 13.77 ? 330 PHE A N   1 
ATOM   2785 C CA  . PHE A 1 330 ? 13.897  29.543  52.896  1.00 13.48 ? 330 PHE A CA  1 
ATOM   2786 C C   . PHE A 1 330 ? 13.853  29.004  51.473  1.00 12.12 ? 330 PHE A C   1 
ATOM   2787 O O   . PHE A 1 330 ? 14.902  28.721  50.866  1.00 12.26 ? 330 PHE A O   1 
ATOM   2788 C CB  . PHE A 1 330 ? 13.384  28.508  53.889  1.00 11.54 ? 330 PHE A CB  1 
ATOM   2789 C CG  . PHE A 1 330 ? 14.219  27.259  53.999  1.00 12.44 ? 330 PHE A CG  1 
ATOM   2790 C CD1 . PHE A 1 330 ? 15.335  27.223  54.830  1.00 15.96 ? 330 PHE A CD1 1 
ATOM   2791 C CD2 . PHE A 1 330 ? 13.853  26.106  53.320  1.00 14.14 ? 330 PHE A CD2 1 
ATOM   2792 C CE1 . PHE A 1 330 ? 16.092  26.038  54.960  1.00 15.54 ? 330 PHE A CE1 1 
ATOM   2793 C CE2 . PHE A 1 330 ? 14.599  24.923  53.448  1.00 15.72 ? 330 PHE A CE2 1 
ATOM   2794 C CZ  . PHE A 1 330 ? 15.714  24.886  54.276  1.00 13.44 ? 330 PHE A CZ  1 
ATOM   2795 N N   . ILE A 1 331 ? 12.643  28.838  50.932  1.00 12.51 ? 331 ILE A N   1 
ATOM   2796 C CA  . ILE A 1 331 ? 12.493  28.373  49.550  1.00 13.19 ? 331 ILE A CA  1 
ATOM   2797 C C   . ILE A 1 331 ? 13.183  29.333  48.585  1.00 14.10 ? 331 ILE A C   1 
ATOM   2798 O O   . ILE A 1 331 ? 13.836  28.915  47.622  1.00 16.16 ? 331 ILE A O   1 
ATOM   2799 C CB  . ILE A 1 331 ? 10.997  28.219  49.188  1.00 15.31 ? 331 ILE A CB  1 
ATOM   2800 C CG1 . ILE A 1 331 ? 10.294  27.231  50.131  1.00 17.20 ? 331 ILE A CG1 1 
ATOM   2801 C CG2 . ILE A 1 331 ? 10.824  27.865  47.689  1.00 16.66 ? 331 ILE A CG2 1 
ATOM   2802 C CD1 . ILE A 1 331 ? 10.761  25.787  49.995  1.00 19.16 ? 331 ILE A CD1 1 
ATOM   2803 N N   . GLY A 1 332 ? 13.029  30.643  48.819  1.00 14.56 ? 332 GLY A N   1 
ATOM   2804 C CA  . GLY A 1 332 ? 13.683  31.625  47.970  1.00 17.55 ? 332 GLY A CA  1 
ATOM   2805 C C   . GLY A 1 332 ? 15.194  31.505  47.962  1.00 15.46 ? 332 GLY A C   1 
ATOM   2806 O O   . GLY A 1 332 ? 15.835  31.692  46.922  1.00 16.33 ? 332 GLY A O   1 
ATOM   2807 N N   . ARG A 1 333 ? 15.789  31.221  49.123  1.00 17.16 ? 333 ARG A N   1 
ATOM   2808 C CA  . ARG A 1 333 ? 17.236  30.999  49.158  1.00 14.42 ? 333 ARG A CA  1 
ATOM   2809 C C   . ARG A 1 333 ? 17.624  29.724  48.414  1.00 16.95 ? 333 ARG A C   1 
ATOM   2810 O O   . ARG A 1 333 ? 18.666  29.686  47.761  1.00 18.44 ? 333 ARG A O   1 
ATOM   2811 C CB  . ARG A 1 333 ? 17.722  30.960  50.602  1.00 14.91 ? 333 ARG A CB  1 
ATOM   2812 C CG  . ARG A 1 333 ? 17.587  32.315  51.296  1.00 14.18 ? 333 ARG A CG  1 
ATOM   2813 C CD  . ARG A 1 333 ? 17.878  32.166  52.775  1.00 14.85 ? 333 ARG A CD  1 
ATOM   2814 N NE  . ARG A 1 333 ? 17.889  33.440  53.490  1.00 13.73 ? 333 ARG A NE  1 
ATOM   2815 C CZ  . ARG A 1 333 ? 18.979  34.173  53.716  1.00 17.99 ? 333 ARG A CZ  1 
ATOM   2816 N NH1 . ARG A 1 333 ? 20.171  33.805  53.235  1.00 20.80 ? 333 ARG A NH1 1 
ATOM   2817 N NH2 . ARG A 1 333 ? 18.869  35.307  54.392  1.00 18.39 ? 333 ARG A NH2 1 
ATOM   2818 N N   . LEU A 1 334 ? 16.824  28.663  48.518  1.00 14.80 ? 334 LEU A N   1 
ATOM   2819 C CA  . LEU A 1 334 ? 17.114  27.449  47.748  1.00 14.19 ? 334 LEU A CA  1 
ATOM   2820 C C   . LEU A 1 334 ? 17.031  27.716  46.248  1.00 17.36 ? 334 LEU A C   1 
ATOM   2821 O O   . LEU A 1 334 ? 17.864  27.230  45.475  1.00 16.70 ? 334 LEU A O   1 
ATOM   2822 C CB  . LEU A 1 334 ? 16.145  26.339  48.142  1.00 13.74 ? 334 LEU A CB  1 
ATOM   2823 C CG  . LEU A 1 334 ? 16.297  25.777  49.545  1.00 12.91 ? 334 LEU A CG  1 
ATOM   2824 C CD1 . LEU A 1 334 ? 15.255  24.689  49.781  1.00 15.77 ? 334 LEU A CD1 1 
ATOM   2825 C CD2 . LEU A 1 334 ? 17.733  25.265  49.772  1.00 17.35 ? 334 LEU A CD2 1 
ATOM   2826 N N   . LYS A 1 335 ? 16.030  28.475  45.820  1.00 16.22 ? 335 LYS A N   1 
ATOM   2827 C CA  . LYS A 1 335 ? 15.941  28.862  44.415  1.00 18.21 ? 335 LYS A CA  1 
ATOM   2828 C C   . LYS A 1 335 ? 17.192  29.605  43.949  1.00 22.20 ? 335 LYS A C   1 
ATOM   2829 O O   . LYS A 1 335 ? 17.689  29.362  42.846  1.00 22.85 ? 335 LYS A O   1 
ATOM   2830 C CB  . LYS A 1 335 ? 14.690  29.716  44.192  1.00 19.61 ? 335 LYS A CB  1 
ATOM   2831 C CG  . LYS A 1 335 ? 14.512  30.165  42.738  1.00 36.37 ? 335 LYS A CG  1 
ATOM   2832 C CD  . LYS A 1 335 ? 14.589  28.981  41.788  1.00 41.78 ? 335 LYS A CD  1 
ATOM   2833 C CE  . LYS A 1 335 ? 14.194  29.372  40.371  1.00 46.99 ? 335 LYS A CE  1 
ATOM   2834 N NZ  . LYS A 1 335 ? 14.285  28.189  39.468  1.00 52.71 ? 335 LYS A NZ  1 
ATOM   2835 N N   . LYS A 1 336 ? 17.722  30.518  44.775  1.00 18.24 ? 336 LYS A N   1 
ATOM   2836 C CA  . LYS A 1 336 ? 18.946  31.219  44.398  1.00 22.32 ? 336 LYS A CA  1 
ATOM   2837 C C   . LYS A 1 336 ? 20.132  30.263  44.266  1.00 21.38 ? 336 LYS A C   1 
ATOM   2838 O O   . LYS A 1 336 ? 20.940  30.406  43.337  1.00 24.74 ? 336 LYS A O   1 
ATOM   2839 C CB  . LYS A 1 336 ? 19.238  32.340  45.398  1.00 26.11 ? 336 LYS A CB  1 
ATOM   2840 C CG  . LYS A 1 336 ? 18.130  33.380  45.410  1.00 40.65 ? 336 LYS A CG  1 
ATOM   2841 C CD  . LYS A 1 336 ? 18.581  34.726  45.948  1.00 51.34 ? 336 LYS A CD  1 
ATOM   2842 C CE  . LYS A 1 336 ? 17.385  35.513  46.478  1.00 56.38 ? 336 LYS A CE  1 
ATOM   2843 N NZ  . LYS A 1 336 ? 17.584  36.989  46.381  1.00 59.59 ? 336 LYS A NZ  1 
ATOM   2844 N N   . ILE A 1 337 ? 20.261  29.285  45.177  1.00 20.57 ? 337 ILE A N   1 
ATOM   2845 C CA  . ILE A 1 337 ? 21.313  28.273  45.014  1.00 22.40 ? 337 ILE A CA  1 
ATOM   2846 C C   . ILE A 1 337 ? 21.120  27.514  43.705  1.00 24.65 ? 337 ILE A C   1 
ATOM   2847 O O   . ILE A 1 337 ? 22.071  27.292  42.938  1.00 24.56 ? 337 ILE A O   1 
ATOM   2848 C CB  . ILE A 1 337 ? 21.334  27.305  46.215  1.00 19.88 ? 337 ILE A CB  1 
ATOM   2849 C CG1 . ILE A 1 337 ? 21.678  28.046  47.504  1.00 17.41 ? 337 ILE A CG1 1 
ATOM   2850 C CG2 . ILE A 1 337 ? 22.369  26.190  45.969  1.00 20.88 ? 337 ILE A CG2 1 
ATOM   2851 C CD1 . ILE A 1 337 ? 21.386  27.249  48.776  1.00 19.76 ? 337 ILE A CD1 1 
ATOM   2852 N N   . HIS A 1 338 ? 19.888  27.078  43.445  1.00 19.31 ? 338 HIS A N   1 
ATOM   2853 C CA  . HIS A 1 338 ? 19.583  26.332  42.224  1.00 20.15 ? 338 HIS A CA  1 
ATOM   2854 C C   . HIS A 1 338 ? 19.983  27.112  40.976  1.00 25.78 ? 338 HIS A C   1 
ATOM   2855 O O   . HIS A 1 338 ? 20.527  26.543  40.013  1.00 26.27 ? 338 HIS A O   1 
ATOM   2856 C CB  . HIS A 1 338 ? 18.082  26.010  42.222  1.00 22.23 ? 338 HIS A CB  1 
ATOM   2857 C CG  . HIS A 1 338 ? 17.613  25.213  41.045  1.00 28.81 ? 338 HIS A CG  1 
ATOM   2858 N ND1 . HIS A 1 338 ? 16.766  25.736  40.091  1.00 34.56 ? 338 HIS A ND1 1 
ATOM   2859 C CD2 . HIS A 1 338 ? 17.810  23.918  40.706  1.00 30.61 ? 338 HIS A CD2 1 
ATOM   2860 C CE1 . HIS A 1 338 ? 16.493  24.807  39.192  1.00 37.36 ? 338 HIS A CE1 1 
ATOM   2861 N NE2 . HIS A 1 338 ? 17.114  23.695  39.542  1.00 32.03 ? 338 HIS A NE2 1 
ATOM   2862 N N   . GLU A 1 339 ? 19.726  28.417  40.969  1.00 22.72 ? 339 GLU A N   1 
ATOM   2863 C CA  . GLU A 1 339 ? 20.045  29.226  39.792  1.00 33.31 ? 339 GLU A CA  1 
ATOM   2864 C C   . GLU A 1 339 ? 21.508  29.654  39.729  1.00 31.17 ? 339 GLU A C   1 
ATOM   2865 O O   . GLU A 1 339 ? 21.960  30.083  38.667  1.00 35.92 ? 339 GLU A O   1 
ATOM   2866 C CB  . GLU A 1 339 ? 19.140  30.463  39.738  1.00 41.73 ? 339 GLU A CB  1 
ATOM   2867 C CG  . GLU A 1 339 ? 17.688  30.147  39.387  1.00 53.24 ? 339 GLU A CG  1 
ATOM   2868 C CD  . GLU A 1 339 ? 17.573  29.124  38.263  1.00 66.64 ? 339 GLU A CD  1 
ATOM   2869 O OE1 . GLU A 1 339 ? 17.940  29.451  37.110  1.00 72.54 ? 339 GLU A OE1 1 
ATOM   2870 O OE2 . GLU A 1 339 ? 17.127  27.989  38.535  1.00 69.68 ? 339 GLU A OE2 1 
ATOM   2871 N N   . SER A 1 340 ? 22.267  29.513  40.814  1.00 31.80 ? 340 SER A N   1 
ATOM   2872 C CA  . SER A 1 340 ? 23.639  30.007  40.876  1.00 34.05 ? 340 SER A CA  1 
ATOM   2873 C C   . SER A 1 340 ? 24.679  29.023  40.350  1.00 36.65 ? 340 SER A C   1 
ATOM   2874 O O   . SER A 1 340 ? 25.802  29.438  40.051  1.00 36.99 ? 340 SER A O   1 
ATOM   2875 C CB  . SER A 1 340 ? 24.005  30.366  42.321  1.00 36.17 ? 340 SER A CB  1 
ATOM   2876 O OG  . SER A 1 340 ? 24.182  29.189  43.100  1.00 38.05 ? 340 SER A OG  1 
ATOM   2877 N N   . VAL A 1 341 ? 24.356  27.736  40.258  1.00 30.78 ? 341 VAL A N   1 
ATOM   2878 C CA  . VAL A 1 341 ? 25.325  26.724  39.861  1.00 35.79 ? 341 VAL A CA  1 
ATOM   2879 C C   . VAL A 1 341 ? 24.822  26.039  38.598  1.00 37.20 ? 341 VAL A C   1 
ATOM   2880 O O   . VAL A 1 341 ? 23.628  26.040  38.286  1.00 36.94 ? 341 VAL A O   1 
ATOM   2881 C CB  . VAL A 1 341 ? 25.589  25.695  40.982  1.00 32.35 ? 341 VAL A CB  1 
ATOM   2882 C CG1 . VAL A 1 341 ? 26.212  26.380  42.197  1.00 36.66 ? 341 VAL A CG1 1 
ATOM   2883 C CG2 . VAL A 1 341 ? 24.298  24.988  41.385  1.00 31.26 ? 341 VAL A CG2 1 
ATOM   2884 N N   . ASP A 1 342 ? 25.762  25.459  37.851  1.00 41.38 ? 342 ASP A N   1 
ATOM   2885 C CA  . ASP A 1 342 ? 25.412  24.804  36.600  1.00 47.39 ? 342 ASP A CA  1 
ATOM   2886 C C   . ASP A 1 342 ? 25.188  23.302  36.743  1.00 45.16 ? 342 ASP A C   1 
ATOM   2887 O O   . ASP A 1 342 ? 24.795  22.656  35.765  1.00 52.19 ? 342 ASP A O   1 
ATOM   2888 C CB  . ASP A 1 342 ? 26.482  25.087  35.532  1.00 59.80 ? 342 ASP A CB  1 
ATOM   2889 C CG  . ASP A 1 342 ? 27.908  24.817  36.015  1.00 73.52 ? 342 ASP A CG  1 
ATOM   2890 O OD1 . ASP A 1 342 ? 28.182  24.954  37.229  1.00 73.00 ? 342 ASP A OD1 1 
ATOM   2891 O OD2 . ASP A 1 342 ? 28.764  24.493  35.161  1.00 77.98 ? 342 ASP A OD2 1 
ATOM   2892 N N   . PHE A 1 343 ? 25.405  22.732  37.926  1.00 31.90 ? 343 PHE A N   1 
ATOM   2893 C CA  . PHE A 1 343 ? 25.224  21.314  38.212  1.00 25.92 ? 343 PHE A CA  1 
ATOM   2894 C C   . PHE A 1 343 ? 24.048  21.167  39.179  1.00 23.69 ? 343 PHE A C   1 
ATOM   2895 O O   . PHE A 1 343 ? 23.381  22.149  39.513  1.00 24.44 ? 343 PHE A O   1 
ATOM   2896 C CB  . PHE A 1 343 ? 26.509  20.723  38.790  1.00 26.87 ? 343 PHE A CB  1 
ATOM   2897 C CG  . PHE A 1 343 ? 27.032  21.483  39.980  1.00 25.61 ? 343 PHE A CG  1 
ATOM   2898 C CD1 . PHE A 1 343 ? 27.813  22.616  39.809  1.00 29.38 ? 343 PHE A CD1 1 
ATOM   2899 C CD2 . PHE A 1 343 ? 26.708  21.084  41.274  1.00 23.78 ? 343 PHE A CD2 1 
ATOM   2900 C CE1 . PHE A 1 343 ? 28.287  23.324  40.906  1.00 28.47 ? 343 PHE A CE1 1 
ATOM   2901 C CE2 . PHE A 1 343 ? 27.178  21.788  42.382  1.00 24.03 ? 343 PHE A CE2 1 
ATOM   2902 C CZ  . PHE A 1 343 ? 27.971  22.905  42.188  1.00 26.92 ? 343 PHE A CZ  1 
ATOM   2903 N N   . GLN A 1 344 ? 23.798  19.935  39.637  1.00 22.95 ? 344 GLN A N   1 
ATOM   2904 C CA  . GLN A 1 344 ? 22.726  19.696  40.595  1.00 20.49 ? 344 GLN A CA  1 
ATOM   2905 C C   . GLN A 1 344 ? 23.313  19.788  41.995  1.00 19.88 ? 344 GLN A C   1 
ATOM   2906 O O   . GLN A 1 344 ? 24.016  18.851  42.420  1.00 21.47 ? 344 GLN A O   1 
ATOM   2907 C CB  . GLN A 1 344 ? 22.088  18.333  40.363  1.00 20.92 ? 344 GLN A CB  1 
ATOM   2908 C CG  . GLN A 1 344 ? 21.262  18.291  39.067  1.00 24.99 ? 344 GLN A CG  1 
ATOM   2909 C CD  . GLN A 1 344 ? 20.456  17.011  38.860  1.00 26.83 ? 344 GLN A CD  1 
ATOM   2910 O OE1 . GLN A 1 344 ? 19.265  17.068  38.542  1.00 27.13 ? 344 GLN A OE1 1 
ATOM   2911 N NE2 . GLN A 1 344 ? 21.101  15.858  39.011  1.00 27.37 ? 344 GLN A NE2 1 
ATOM   2912 N N   . PRO A 1 345 ? 23.046  20.858  42.755  1.00 19.37 ? 345 PRO A N   1 
ATOM   2913 C CA  . PRO A 1 345 ? 23.691  21.022  44.063  1.00 18.34 ? 345 PRO A CA  1 
ATOM   2914 C C   . PRO A 1 345 ? 23.068  20.115  45.104  1.00 17.37 ? 345 PRO A C   1 
ATOM   2915 O O   . PRO A 1 345 ? 21.879  19.792  45.049  1.00 17.66 ? 345 PRO A O   1 
ATOM   2916 C CB  . PRO A 1 345 ? 23.425  22.494  44.410  1.00 19.04 ? 345 PRO A CB  1 
ATOM   2917 C CG  . PRO A 1 345 ? 22.109  22.803  43.711  1.00 21.01 ? 345 PRO A CG  1 
ATOM   2918 C CD  . PRO A 1 345 ? 22.124  21.968  42.442  1.00 18.72 ? 345 PRO A CD  1 
ATOM   2919 N N   . VAL A 1 346 ? 23.891  19.719  46.072  1.00 13.74 ? 346 VAL A N   1 
ATOM   2920 C CA  . VAL A 1 346 ? 23.413  18.995  47.241  1.00 14.18 ? 346 VAL A CA  1 
ATOM   2921 C C   . VAL A 1 346 ? 23.539  19.934  48.424  1.00 16.24 ? 346 VAL A C   1 
ATOM   2922 O O   . VAL A 1 346 ? 24.634  20.420  48.734  1.00 16.59 ? 346 VAL A O   1 
ATOM   2923 C CB  . VAL A 1 346 ? 24.189  17.684  47.461  1.00 15.12 ? 346 VAL A CB  1 
ATOM   2924 C CG1 . VAL A 1 346 ? 23.623  16.887  48.665  1.00 16.82 ? 346 VAL A CG1 1 
ATOM   2925 C CG2 . VAL A 1 346 ? 24.134  16.840  46.173  1.00 21.44 ? 346 VAL A CG2 1 
ATOM   2926 N N   . VAL A 1 347 ? 22.426  20.166  49.108  1.00 11.40 ? 347 VAL A N   1 
ATOM   2927 C CA  . VAL A 1 347 ? 22.345  21.144  50.177  1.00 12.13 ? 347 VAL A CA  1 
ATOM   2928 C C   . VAL A 1 347 ? 22.009  20.393  51.457  1.00 10.77 ? 347 VAL A C   1 
ATOM   2929 O O   . VAL A 1 347 ? 20.865  19.939  51.649  1.00 12.70 ? 347 VAL A O   1 
ATOM   2930 C CB  . VAL A 1 347 ? 21.305  22.230  49.862  1.00 14.94 ? 347 VAL A CB  1 
ATOM   2931 C CG1 . VAL A 1 347 ? 21.291  23.292  50.925  1.00 12.50 ? 347 VAL A CG1 1 
ATOM   2932 C CG2 . VAL A 1 347 ? 21.617  22.881  48.475  1.00 16.37 ? 347 VAL A CG2 1 
ATOM   2933 N N   . PHE A 1 348 ? 22.983  20.316  52.358  1.00 9.73  ? 348 PHE A N   1 
ATOM   2934 C CA  . PHE A 1 348 ? 22.801  19.686  53.666  1.00 9.70  ? 348 PHE A CA  1 
ATOM   2935 C C   . PHE A 1 348 ? 22.394  20.743  54.683  1.00 10.51 ? 348 PHE A C   1 
ATOM   2936 O O   . PHE A 1 348 ? 23.081  21.748  54.856  1.00 13.29 ? 348 PHE A O   1 
ATOM   2937 C CB  . PHE A 1 348 ? 24.092  18.988  54.129  1.00 12.14 ? 348 PHE A CB  1 
ATOM   2938 C CG  . PHE A 1 348 ? 24.128  17.514  53.815  1.00 11.17 ? 348 PHE A CG  1 
ATOM   2939 C CD1 . PHE A 1 348 ? 24.202  17.096  52.497  1.00 12.21 ? 348 PHE A CD1 1 
ATOM   2940 C CD2 . PHE A 1 348 ? 24.068  16.556  54.828  1.00 11.17 ? 348 PHE A CD2 1 
ATOM   2941 C CE1 . PHE A 1 348 ? 24.219  15.755  52.174  1.00 11.12 ? 348 PHE A CE1 1 
ATOM   2942 C CE2 . PHE A 1 348 ? 24.105  15.197  54.524  1.00 12.19 ? 348 PHE A CE2 1 
ATOM   2943 C CZ  . PHE A 1 348 ? 24.163  14.788  53.198  1.00 12.92 ? 348 PHE A CZ  1 
ATOM   2944 N N   . VAL A 1 349 ? 21.260  20.510  55.355  1.00 11.76 ? 349 VAL A N   1 
ATOM   2945 C CA  . VAL A 1 349 ? 20.782  21.365  56.435  1.00 10.39 ? 349 VAL A CA  1 
ATOM   2946 C C   . VAL A 1 349 ? 20.892  20.524  57.695  1.00 9.16  ? 349 VAL A C   1 
ATOM   2947 O O   . VAL A 1 349 ? 20.178  19.525  57.834  1.00 9.76  ? 349 VAL A O   1 
ATOM   2948 C CB  . VAL A 1 349 ? 19.333  21.809  56.175  1.00 8.56  ? 349 VAL A CB  1 
ATOM   2949 C CG1 . VAL A 1 349 ? 18.778  22.644  57.361  1.00 16.02 ? 349 VAL A CG1 1 
ATOM   2950 C CG2 . VAL A 1 349 ? 19.264  22.629  54.881  1.00 10.74 ? 349 VAL A CG2 1 
ATOM   2951 N N   . VAL A 1 350 ? 21.816  20.870  58.590  1.00 9.16  ? 350 VAL A N   1 
ATOM   2952 C CA  . VAL A 1 350 ? 22.147  19.998  59.721  1.00 11.99 ? 350 VAL A CA  1 
ATOM   2953 C C   . VAL A 1 350 ? 22.203  20.855  60.972  1.00 7.45  ? 350 VAL A C   1 
ATOM   2954 O O   . VAL A 1 350 ? 22.892  21.874  60.995  1.00 10.01 ? 350 VAL A O   1 
ATOM   2955 C CB  . VAL A 1 350 ? 23.497  19.261  59.532  1.00 10.00 ? 350 VAL A CB  1 
ATOM   2956 C CG1 . VAL A 1 350 ? 23.689  18.172  60.650  1.00 10.99 ? 350 VAL A CG1 1 
ATOM   2957 C CG2 . VAL A 1 350 ? 23.587  18.617  58.130  1.00 14.31 ? 350 VAL A CG2 1 
ATOM   2958 N N   . LEU A 1 351 ? 21.448  20.468  62.001  1.00 8.25  ? 351 LEU A N   1 
ATOM   2959 C CA  . LEU A 1 351 ? 21.452  21.231  63.248  1.00 12.37 ? 351 LEU A CA  1 
ATOM   2960 C C   . LEU A 1 351 ? 20.788  20.363  64.300  1.00 8.41  ? 351 LEU A C   1 
ATOM   2961 O O   . LEU A 1 351 ? 20.291  19.271  63.991  1.00 9.89  ? 351 LEU A O   1 
ATOM   2962 C CB  . LEU A 1 351 ? 20.745  22.587  63.126  1.00 11.24 ? 351 LEU A CB  1 
ATOM   2963 C CG  . LEU A 1 351 ? 19.260  22.619  62.741  1.00 11.96 ? 351 LEU A CG  1 
ATOM   2964 C CD1 . LEU A 1 351 ? 18.530  23.734  63.492  1.00 11.30 ? 351 LEU A CD1 1 
ATOM   2965 C CD2 . LEU A 1 351 ? 19.122  22.819  61.234  1.00 13.34 ? 351 LEU A CD2 1 
ATOM   2966 N N   . ASP A 1 352 ? 20.862  20.823  65.558  1.00 8.20  ? 352 ASP A N   1 
ATOM   2967 C CA  . ASP A 1 352 ? 20.172  20.110  66.627  1.00 9.23  ? 352 ASP A CA  1 
ATOM   2968 C C   . ASP A 1 352 ? 18.701  19.993  66.265  1.00 11.09 ? 352 ASP A C   1 
ATOM   2969 O O   . ASP A 1 352 ? 18.121  20.917  65.719  1.00 11.95 ? 352 ASP A O   1 
ATOM   2970 C CB  . ASP A 1 352 ? 20.311  20.850  67.953  1.00 7.92  ? 352 ASP A CB  1 
ATOM   2971 C CG  . ASP A 1 352 ? 21.765  20.929  68.445  1.00 12.46 ? 352 ASP A CG  1 
ATOM   2972 O OD1 . ASP A 1 352 ? 22.681  20.312  67.825  1.00 13.37 ? 352 ASP A OD1 1 
ATOM   2973 O OD2 . ASP A 1 352 ? 21.992  21.626  69.463  1.00 13.38 ? 352 ASP A OD2 1 
ATOM   2974 N N   . GLY A 1 353 ? 18.116  18.826  66.505  1.00 7.64  ? 353 GLY A N   1 
ATOM   2975 C CA  . GLY A 1 353 ? 16.737  18.632  66.118  1.00 7.40  ? 353 GLY A CA  1 
ATOM   2976 C C   . GLY A 1 353 ? 15.728  18.928  67.193  1.00 7.39  ? 353 GLY A C   1 
ATOM   2977 O O   . GLY A 1 353 ? 14.537  18.877  66.888  1.00 7.72  ? 353 GLY A O   1 
ATOM   2978 N N   . GLU A 1 354 ? 16.141  19.260  68.434  1.00 7.73  ? 354 GLU A N   1 
ATOM   2979 C CA  . GLU A 1 354 ? 15.175  19.441  69.523  1.00 8.02  ? 354 GLU A CA  1 
ATOM   2980 C C   . GLU A 1 354 ? 15.290  20.767  70.268  1.00 8.45  ? 354 GLU A C   1 
ATOM   2981 O O   . GLU A 1 354 ? 14.437  21.044  71.128  1.00 10.54 ? 354 GLU A O   1 
ATOM   2982 C CB  . GLU A 1 354 ? 15.274  18.262  70.516  1.00 8.42  ? 354 GLU A CB  1 
ATOM   2983 C CG  . GLU A 1 354 ? 16.456  18.335  71.511  1.00 8.59  ? 354 GLU A CG  1 
ATOM   2984 C CD  . GLU A 1 354 ? 17.782  17.893  70.887  1.00 8.68  ? 354 GLU A CD  1 
ATOM   2985 O OE1 . GLU A 1 354 ? 18.289  16.796  71.261  1.00 8.69  ? 354 GLU A OE1 1 
ATOM   2986 O OE2 . GLU A 1 354 ? 18.305  18.586  70.006  1.00 8.82  ? 354 GLU A OE2 1 
ATOM   2987 N N   . ASN A 1 355 ? 16.274  21.624  69.937  1.00 8.01  ? 355 ASN A N   1 
ATOM   2988 C CA  . ASN A 1 355 ? 16.567  22.789  70.799  1.00 10.66 ? 355 ASN A CA  1 
ATOM   2989 C C   . ASN A 1 355 ? 16.013  24.113  70.301  1.00 12.74 ? 355 ASN A C   1 
ATOM   2990 O O   . ASN A 1 355 ? 15.876  25.053  71.109  1.00 12.33 ? 355 ASN A O   1 
ATOM   2991 C CB  . ASN A 1 355 ? 18.087  22.882  70.987  1.00 11.20 ? 355 ASN A CB  1 
ATOM   2992 C CG  . ASN A 1 355 ? 18.610  21.713  71.798  1.00 12.21 ? 355 ASN A CG  1 
ATOM   2993 O OD1 . ASN A 1 355 ? 17.920  21.241  72.690  1.00 10.64 ? 355 ASN A OD1 1 
ATOM   2994 N ND2 . ASN A 1 355 ? 19.819  21.248  71.496  1.00 11.98 ? 355 ASN A ND2 1 
ATOM   2995 N N   . CYS A 1 356 ? 15.618  24.214  69.037  1.00 10.24 ? 356 CYS A N   1 
ATOM   2996 C CA  . CYS A 1 356 ? 15.195  25.523  68.538  1.00 8.98  ? 356 CYS A CA  1 
ATOM   2997 C C   . CYS A 1 356 ? 13.678  25.743  68.619  1.00 9.94  ? 356 CYS A C   1 
ATOM   2998 O O   . CYS A 1 356 ? 13.240  26.909  68.700  1.00 8.94  ? 356 CYS A O   1 
ATOM   2999 C CB  . CYS A 1 356 ? 15.691  25.703  67.092  1.00 9.41  ? 356 CYS A CB  1 
ATOM   3000 S SG  . CYS A 1 356 ? 15.070  24.424  65.948  1.00 12.18 ? 356 CYS A SG  1 
ATOM   3001 N N   . TRP A 1 357 ? 12.886  24.688  68.706  1.00 9.21  ? 357 TRP A N   1 
ATOM   3002 C CA  . TRP A 1 357 ? 11.435  24.779  68.509  1.00 9.16  ? 357 TRP A CA  1 
ATOM   3003 C C   . TRP A 1 357 ? 10.741  25.456  69.677  1.00 9.94  ? 357 TRP A C   1 
ATOM   3004 O O   . TRP A 1 357 ? 9.690   26.085  69.485  1.00 9.98  ? 357 TRP A O   1 
ATOM   3005 C CB  . TRP A 1 357 ? 10.823  23.369  68.288  1.00 9.36  ? 357 TRP A CB  1 
ATOM   3006 C CG  . TRP A 1 357 ? 11.597  22.627  67.257  1.00 8.24  ? 357 TRP A CG  1 
ATOM   3007 C CD1 . TRP A 1 357 ? 12.236  21.419  67.420  1.00 9.58  ? 357 TRP A CD1 1 
ATOM   3008 C CD2 . TRP A 1 357 ? 11.814  23.024  65.901  1.00 8.00  ? 357 TRP A CD2 1 
ATOM   3009 N NE1 . TRP A 1 357 ? 12.898  21.079  66.250  1.00 11.25 ? 357 TRP A NE1 1 
ATOM   3010 C CE2 . TRP A 1 357 ? 12.645  22.045  65.304  1.00 10.24 ? 357 TRP A CE2 1 
ATOM   3011 C CE3 . TRP A 1 357 ? 11.440  24.162  65.144  1.00 10.56 ? 357 TRP A CE3 1 
ATOM   3012 C CZ2 . TRP A 1 357 ? 13.079  22.132  63.976  1.00 12.55 ? 357 TRP A CZ2 1 
ATOM   3013 C CZ3 . TRP A 1 357 ? 11.871  24.255  63.829  1.00 8.67  ? 357 TRP A CZ3 1 
ATOM   3014 C CH2 . TRP A 1 357 ? 12.689  23.242  63.256  1.00 9.51  ? 357 TRP A CH2 1 
ATOM   3015 N N   . GLU A 1 358 ? 11.307  25.359  70.889  1.00 9.62  ? 358 GLU A N   1 
ATOM   3016 C CA  . GLU A 1 358 ? 10.652  25.982  72.033  1.00 10.33 ? 358 GLU A CA  1 
ATOM   3017 C C   . GLU A 1 358 ? 10.600  27.496  71.925  1.00 10.66 ? 358 GLU A C   1 
ATOM   3018 O O   . GLU A 1 358 ? 9.811   28.117  72.635  1.00 11.33 ? 358 GLU A O   1 
ATOM   3019 C CB  . GLU A 1 358 ? 11.371  25.568  73.317  1.00 10.63 ? 358 GLU A CB  1 
ATOM   3020 C CG  . GLU A 1 358 ? 12.825  26.030  73.371  1.00 12.02 ? 358 GLU A CG  1 
ATOM   3021 C CD  . GLU A 1 358 ? 13.662  25.177  74.305  1.00 19.26 ? 358 GLU A CD  1 
ATOM   3022 O OE1 . GLU A 1 358 ? 14.214  25.737  75.269  1.00 21.22 ? 358 GLU A OE1 1 
ATOM   3023 O OE2 . GLU A 1 358 ? 13.800  23.959  74.047  1.00 17.92 ? 358 GLU A OE2 1 
ATOM   3024 N N   . TYR A 1 359 ? 11.390  28.083  71.027  1.00 10.31 ? 359 TYR A N   1 
ATOM   3025 C CA  . TYR A 1 359 ? 11.398  29.528  70.806  1.00 10.74 ? 359 TYR A CA  1 
ATOM   3026 C C   . TYR A 1 359 ? 10.453  29.940  69.694  1.00 11.77 ? 359 TYR A C   1 
ATOM   3027 O O   . TYR A 1 359 ? 10.279  31.136  69.469  1.00 12.31 ? 359 TYR A O   1 
ATOM   3028 C CB  . TYR A 1 359 ? 12.826  29.989  70.470  1.00 10.87 ? 359 TYR A CB  1 
ATOM   3029 C CG  . TYR A 1 359 ? 13.763  29.778  71.620  1.00 11.39 ? 359 TYR A CG  1 
ATOM   3030 C CD1 . TYR A 1 359 ? 13.809  30.674  72.658  1.00 16.94 ? 359 TYR A CD1 1 
ATOM   3031 C CD2 . TYR A 1 359 ? 14.568  28.657  71.686  1.00 13.96 ? 359 TYR A CD2 1 
ATOM   3032 C CE1 . TYR A 1 359 ? 14.669  30.475  73.742  1.00 17.36 ? 359 TYR A CE1 1 
ATOM   3033 C CE2 . TYR A 1 359 ? 15.436  28.445  72.781  1.00 18.99 ? 359 TYR A CE2 1 
ATOM   3034 C CZ  . TYR A 1 359 ? 15.464  29.366  73.796  1.00 24.48 ? 359 TYR A CZ  1 
ATOM   3035 O OH  . TYR A 1 359 ? 16.311  29.200  74.885  1.00 27.84 ? 359 TYR A OH  1 
ATOM   3036 N N   . TYR A 1 360 ? 9.884   28.993  68.961  1.00 10.37 ? 360 TYR A N   1 
ATOM   3037 C CA  . TYR A 1 360 ? 8.876   29.289  67.945  1.00 10.47 ? 360 TYR A CA  1 
ATOM   3038 C C   . TYR A 1 360 ? 7.468   29.288  68.521  1.00 12.94 ? 360 TYR A C   1 
ATOM   3039 O O   . TYR A 1 360 ? 7.154   28.535  69.435  1.00 12.47 ? 360 TYR A O   1 
ATOM   3040 C CB  . TYR A 1 360 ? 8.858   28.225  66.850  1.00 9.93  ? 360 TYR A CB  1 
ATOM   3041 C CG  . TYR A 1 360 ? 9.994   28.172  65.855  1.00 10.98 ? 360 TYR A CG  1 
ATOM   3042 C CD1 . TYR A 1 360 ? 11.326  27.886  66.259  1.00 9.10  ? 360 TYR A CD1 1 
ATOM   3043 C CD2 . TYR A 1 360 ? 9.729   28.352  64.481  1.00 9.53  ? 360 TYR A CD2 1 
ATOM   3044 C CE1 . TYR A 1 360 ? 12.350  27.808  65.325  1.00 8.77  ? 360 TYR A CE1 1 
ATOM   3045 C CE2 . TYR A 1 360 ? 10.752  28.246  63.536  1.00 9.14  ? 360 TYR A CE2 1 
ATOM   3046 C CZ  . TYR A 1 360 ? 12.046  28.003  63.962  1.00 9.07  ? 360 TYR A CZ  1 
ATOM   3047 O OH  . TYR A 1 360 ? 13.055  27.896  63.011  1.00 11.17 ? 360 TYR A OH  1 
ATOM   3048 N N   . GLU A 1 361 ? 6.595   30.074  67.897  1.00 14.32 ? 361 GLU A N   1 
ATOM   3049 C CA  . GLU A 1 361 ? 5.157   29.966  68.160  1.00 16.31 ? 361 GLU A CA  1 
ATOM   3050 C C   . GLU A 1 361 ? 4.666   28.531  68.017  1.00 15.10 ? 361 GLU A C   1 
ATOM   3051 O O   . GLU A 1 361 ? 4.997   27.847  67.045  1.00 12.96 ? 361 GLU A O   1 
ATOM   3052 C CB  . GLU A 1 361 ? 4.384   30.872  67.179  1.00 18.42 ? 361 GLU A CB  1 
ATOM   3053 C CG  . GLU A 1 361 ? 4.654   32.348  67.303  1.00 35.45 ? 361 GLU A CG  1 
ATOM   3054 C CD  . GLU A 1 361 ? 4.680   32.829  68.736  1.00 52.91 ? 361 GLU A CD  1 
ATOM   3055 O OE1 . GLU A 1 361 ? 5.756   33.246  69.216  1.00 57.81 ? 361 GLU A OE1 1 
ATOM   3056 O OE2 . GLU A 1 361 ? 3.619   32.806  69.398  1.00 59.68 ? 361 GLU A OE2 1 
ATOM   3057 N N   . GLU A 1 362 ? 3.853   28.076  68.989  1.00 13.75 ? 362 GLU A N   1 
ATOM   3058 C CA  . GLU A 1 362 ? 3.293   26.717  68.965  1.00 17.37 ? 362 GLU A CA  1 
ATOM   3059 C C   . GLU A 1 362 ? 4.357   25.654  68.702  1.00 17.30 ? 362 GLU A C   1 
ATOM   3060 O O   . GLU A 1 362 ? 4.120   24.667  67.986  1.00 11.01 ? 362 GLU A O   1 
ATOM   3061 C CB  . GLU A 1 362 ? 2.164   26.609  67.937  1.00 18.08 ? 362 GLU A CB  1 
ATOM   3062 C CG  . GLU A 1 362 ? 0.927   27.396  68.335  1.00 34.05 ? 362 GLU A CG  1 
ATOM   3063 C CD  . GLU A 1 362 ? -0.055  27.565  67.183  1.00 50.07 ? 362 GLU A CD  1 
ATOM   3064 O OE1 . GLU A 1 362 ? -0.313  28.721  66.775  1.00 57.39 ? 362 GLU A OE1 1 
ATOM   3065 O OE2 . GLU A 1 362 ? -0.559  26.543  66.679  1.00 52.84 ? 362 GLU A OE2 1 
ATOM   3066 N N   . ASN A 1 363 ? 5.534   25.822  69.325  1.00 11.61 ? 363 ASN A N   1 
ATOM   3067 C CA  . ASN A 1 363 ? 6.615   24.838  69.271  1.00 10.69 ? 363 ASN A CA  1 
ATOM   3068 C C   . ASN A 1 363 ? 7.060   24.534  67.836  1.00 11.99 ? 363 ASN A C   1 
ATOM   3069 O O   . ASN A 1 363 ? 7.375   23.379  67.498  1.00 11.65 ? 363 ASN A O   1 
ATOM   3070 C CB  . ASN A 1 363 ? 6.201   23.538  69.976  1.00 14.67 ? 363 ASN A CB  1 
ATOM   3071 C CG  . ASN A 1 363 ? 7.392   22.642  70.274  1.00 15.84 ? 363 ASN A CG  1 
ATOM   3072 O OD1 . ASN A 1 363 ? 8.446   23.109  70.677  1.00 12.76 ? 363 ASN A OD1 1 
ATOM   3073 N ND2 . ASN A 1 363 ? 7.209   21.332  70.088  1.00 19.78 ? 363 ASN A ND2 1 
ATOM   3074 N N   . GLY A 1 364 ? 7.003   25.528  66.959  1.00 11.82 ? 364 GLY A N   1 
ATOM   3075 C CA  . GLY A 1 364 ? 7.457   25.316  65.588  1.00 12.02 ? 364 GLY A CA  1 
ATOM   3076 C C   . GLY A 1 364 ? 6.503   24.567  64.685  1.00 13.15 ? 364 GLY A C   1 
ATOM   3077 O O   . GLY A 1 364 ? 6.866   24.267  63.539  1.00 12.47 ? 364 GLY A O   1 
ATOM   3078 N N   . ILE A 1 365 ? 5.291   24.269  65.142  1.00 9.99  ? 365 ILE A N   1 
ATOM   3079 C CA  . ILE A 1 365 ? 4.410   23.393  64.364  1.00 9.35  ? 365 ILE A CA  1 
ATOM   3080 C C   . ILE A 1 365 ? 3.885   24.140  63.137  1.00 13.99 ? 365 ILE A C   1 
ATOM   3081 O O   . ILE A 1 365 ? 3.975   23.603  62.017  1.00 14.03 ? 365 ILE A O   1 
ATOM   3082 C CB  . ILE A 1 365 ? 3.296   22.824  65.265  1.00 12.96 ? 365 ILE A CB  1 
ATOM   3083 C CG1 . ILE A 1 365 ? 3.921   21.818  66.255  1.00 13.15 ? 365 ILE A CG1 1 
ATOM   3084 C CG2 . ILE A 1 365 ? 2.176   22.180  64.425  1.00 14.07 ? 365 ILE A CG2 1 
ATOM   3085 C CD1 . ILE A 1 365 ? 3.056   21.492  67.475  1.00 12.86 ? 365 ILE A CD1 1 
ATOM   3086 N N   . PRO A 1 366 ? 3.419   25.385  63.248  1.00 11.41 ? 366 PRO A N   1 
ATOM   3087 C CA  . PRO A 1 366 ? 3.077   26.122  62.004  1.00 14.78 ? 366 PRO A CA  1 
ATOM   3088 C C   . PRO A 1 366 ? 4.225   26.179  61.009  1.00 16.92 ? 366 PRO A C   1 
ATOM   3089 O O   . PRO A 1 366 ? 4.029   25.918  59.812  1.00 15.31 ? 366 PRO A O   1 
ATOM   3090 C CB  . PRO A 1 366 ? 2.710   27.511  62.525  1.00 14.85 ? 366 PRO A CB  1 
ATOM   3091 C CG  . PRO A 1 366 ? 2.129   27.241  63.877  1.00 17.52 ? 366 PRO A CG  1 
ATOM   3092 C CD  . PRO A 1 366 ? 2.974   26.131  64.448  1.00 15.25 ? 366 PRO A CD  1 
ATOM   3093 N N   . PHE A 1 367 ? 5.424   26.529  61.477  1.00 11.09 ? 367 PHE A N   1 
ATOM   3094 C CA  . PHE A 1 367 ? 6.579   26.613  60.591  1.00 10.11 ? 367 PHE A CA  1 
ATOM   3095 C C   . PHE A 1 367 ? 6.861   25.283  59.886  1.00 9.22  ? 367 PHE A C   1 
ATOM   3096 O O   . PHE A 1 367 ? 7.016   25.255  58.656  1.00 10.76 ? 367 PHE A O   1 
ATOM   3097 C CB  . PHE A 1 367 ? 7.818   27.037  61.367  1.00 9.91  ? 367 PHE A CB  1 
ATOM   3098 C CG  . PHE A 1 367 ? 9.066   26.987  60.532  1.00 9.60  ? 367 PHE A CG  1 
ATOM   3099 C CD1 . PHE A 1 367 ? 9.286   27.951  59.536  1.00 10.48 ? 367 PHE A CD1 1 
ATOM   3100 C CD2 . PHE A 1 367 ? 10.000  25.967  60.711  1.00 11.65 ? 367 PHE A CD2 1 
ATOM   3101 C CE1 . PHE A 1 367 ? 10.436  27.911  58.731  1.00 13.29 ? 367 PHE A CE1 1 
ATOM   3102 C CE2 . PHE A 1 367 ? 11.147  25.905  59.923  1.00 13.04 ? 367 PHE A CE2 1 
ATOM   3103 C CZ  . PHE A 1 367 ? 11.357  26.863  58.912  1.00 14.61 ? 367 PHE A CZ  1 
ATOM   3104 N N   . LEU A 1 368 ? 6.989   24.191  60.651  1.00 9.26  ? 368 LEU A N   1 
ATOM   3105 C CA  . LEU A 1 368 ? 7.367   22.920  60.035  1.00 8.44  ? 368 LEU A CA  1 
ATOM   3106 C C   . LEU A 1 368 ? 6.242   22.378  59.161  1.00 10.17 ? 368 LEU A C   1 
ATOM   3107 O O   . LEU A 1 368 ? 6.497   21.812  58.092  1.00 9.95  ? 368 LEU A O   1 
ATOM   3108 C CB  . LEU A 1 368 ? 7.765   21.884  61.093  1.00 7.27  ? 368 LEU A CB  1 
ATOM   3109 C CG  . LEU A 1 368 ? 9.148   22.117  61.723  1.00 8.24  ? 368 LEU A CG  1 
ATOM   3110 C CD1 . LEU A 1 368 ? 9.394   21.070  62.838  1.00 9.56  ? 368 LEU A CD1 1 
ATOM   3111 C CD2 . LEU A 1 368 ? 10.295  22.082  60.670  1.00 9.93  ? 368 LEU A CD2 1 
ATOM   3112 N N   . GLU A 1 369 ? 4.989   22.519  59.585  1.00 9.12  ? 369 GLU A N   1 
ATOM   3113 C CA  . GLU A 1 369 ? 3.914   22.054  58.704  1.00 11.63 ? 369 GLU A CA  1 
ATOM   3114 C C   . GLU A 1 369 ? 3.903   22.824  57.392  1.00 13.18 ? 369 GLU A C   1 
ATOM   3115 O O   . GLU A 1 369 ? 3.679   22.262  56.308  1.00 13.63 ? 369 GLU A O   1 
ATOM   3116 C CB  . GLU A 1 369 ? 2.570   22.161  59.420  1.00 10.55 ? 369 GLU A CB  1 
ATOM   3117 C CG  . GLU A 1 369 ? 2.393   21.048  60.481  1.00 10.21 ? 369 GLU A CG  1 
ATOM   3118 C CD  . GLU A 1 369 ? 1.048   21.080  61.185  1.00 16.59 ? 369 GLU A CD  1 
ATOM   3119 O OE1 . GLU A 1 369 ? 0.260   22.042  61.006  1.00 21.67 ? 369 GLU A OE1 1 
ATOM   3120 O OE2 . GLU A 1 369 ? 0.765   20.089  61.909  1.00 17.54 ? 369 GLU A OE2 1 
ATOM   3121 N N   . LYS A 1 370 ? 4.145   24.122  57.459  1.00 10.78 ? 370 LYS A N   1 
ATOM   3122 C CA  . LYS A 1 370 ? 4.165   24.885  56.231  1.00 11.71 ? 370 LYS A CA  1 
ATOM   3123 C C   . LYS A 1 370 ? 5.390   24.543  55.395  1.00 11.16 ? 370 LYS A C   1 
ATOM   3124 O O   . LYS A 1 370 ? 5.292   24.450  54.163  1.00 15.90 ? 370 LYS A O   1 
ATOM   3125 C CB  . LYS A 1 370 ? 4.115   26.373  56.562  1.00 12.52 ? 370 LYS A CB  1 
ATOM   3126 C CG  . LYS A 1 370 ? 2.750   26.830  57.080  1.00 16.17 ? 370 LYS A CG  1 
ATOM   3127 C CD  . LYS A 1 370 ? 2.698   28.381  57.234  1.00 20.82 ? 370 LYS A CD  1 
ATOM   3128 C CE  . LYS A 1 370 ? 1.471   28.829  58.008  1.00 29.31 ? 370 LYS A CE  1 
ATOM   3129 N NZ  . LYS A 1 370 ? 0.208   28.382  57.346  1.00 34.60 ? 370 LYS A NZ  1 
ATOM   3130 N N   . LEU A 1 371 ? 6.544   24.419  56.034  1.00 10.12 ? 371 LEU A N   1 
ATOM   3131 C CA  . LEU A 1 371 ? 7.771   24.105  55.301  1.00 9.72  ? 371 LEU A CA  1 
ATOM   3132 C C   . LEU A 1 371 ? 7.658   22.765  54.585  1.00 11.82 ? 371 LEU A C   1 
ATOM   3133 O O   . LEU A 1 371 ? 7.974   22.652  53.393  1.00 12.78 ? 371 LEU A O   1 
ATOM   3134 C CB  . LEU A 1 371 ? 8.946   24.098  56.261  1.00 10.55 ? 371 LEU A CB  1 
ATOM   3135 C CG  . LEU A 1 371 ? 10.291  23.607  55.675  1.00 12.57 ? 371 LEU A CG  1 
ATOM   3136 C CD1 . LEU A 1 371 ? 10.756  24.627  54.697  1.00 13.02 ? 371 LEU A CD1 1 
ATOM   3137 C CD2 . LEU A 1 371 ? 11.363  23.405  56.742  1.00 10.34 ? 371 LEU A CD2 1 
ATOM   3138 N N   . TYR A 1 372 ? 7.228   21.738  55.304  1.00 11.17 ? 372 TYR A N   1 
ATOM   3139 C CA  . TYR A 1 372 ? 7.123   20.413  54.710  1.00 10.85 ? 372 TYR A CA  1 
ATOM   3140 C C   . TYR A 1 372 ? 6.027   20.332  53.656  1.00 13.06 ? 372 TYR A C   1 
ATOM   3141 O O   . TYR A 1 372 ? 6.203   19.662  52.620  1.00 15.52 ? 372 TYR A O   1 
ATOM   3142 C CB  . TYR A 1 372 ? 6.870   19.419  55.837  1.00 9.86  ? 372 TYR A CB  1 
ATOM   3143 C CG  . TYR A 1 372 ? 8.038   19.259  56.804  1.00 9.19  ? 372 TYR A CG  1 
ATOM   3144 C CD1 . TYR A 1 372 ? 9.355   19.654  56.464  1.00 9.58  ? 372 TYR A CD1 1 
ATOM   3145 C CD2 . TYR A 1 372 ? 7.846   18.649  58.062  1.00 8.79  ? 372 TYR A CD2 1 
ATOM   3146 C CE1 . TYR A 1 372 ? 10.437  19.468  57.355  1.00 9.82  ? 372 TYR A CE1 1 
ATOM   3147 C CE2 . TYR A 1 372 ? 8.922   18.485  58.965  1.00 6.90  ? 372 TYR A CE2 1 
ATOM   3148 C CZ  . TYR A 1 372 ? 10.211  18.837  58.581  1.00 6.80  ? 372 TYR A CZ  1 
ATOM   3149 O OH  . TYR A 1 372 ? 11.217  18.633  59.479  1.00 10.67 ? 372 TYR A OH  1 
ATOM   3150 N N   . SER A 1 373 ? 4.866   20.942  53.918  1.00 13.04 ? 373 SER A N   1 
ATOM   3151 C CA  . SER A 1 373 ? 3.818   20.979  52.909  1.00 14.09 ? 373 SER A CA  1 
ATOM   3152 C C   . SER A 1 373 ? 4.292   21.685  51.636  1.00 15.20 ? 373 SER A C   1 
ATOM   3153 O O   . SER A 1 373 ? 3.881   21.319  50.519  1.00 17.02 ? 373 SER A O   1 
ATOM   3154 C CB  . SER A 1 373 ? 2.573   21.667  53.486  1.00 15.62 ? 373 SER A CB  1 
ATOM   3155 O OG  . SER A 1 373 ? 1.543   21.664  52.518  1.00 30.12 ? 373 SER A OG  1 
ATOM   3156 N N   . THR A 1 374 ? 5.124   22.722  51.783  1.00 16.22 ? 374 THR A N   1 
ATOM   3157 C CA  . THR A 1 374 ? 5.620   23.444  50.609  1.00 15.60 ? 374 THR A CA  1 
ATOM   3158 C C   . THR A 1 374 ? 6.640   22.599  49.846  1.00 15.04 ? 374 THR A C   1 
ATOM   3159 O O   . THR A 1 374 ? 6.582   22.493  48.613  1.00 17.97 ? 374 THR A O   1 
ATOM   3160 C CB  . THR A 1 374 ? 6.217   24.789  51.042  1.00 16.20 ? 374 THR A CB  1 
ATOM   3161 O OG1 . THR A 1 374 ? 5.180   25.588  51.627  1.00 16.62 ? 374 THR A OG1 1 
ATOM   3162 C CG2 . THR A 1 374 ? 6.777   25.536  49.833  1.00 19.65 ? 374 THR A CG2 1 
ATOM   3163 N N   . LEU A 1 375 ? 7.571   21.976  50.568  1.00 15.50 ? 375 LEU A N   1 
ATOM   3164 C CA  . LEU A 1 375 ? 8.555   21.128  49.896  1.00 16.35 ? 375 LEU A CA  1 
ATOM   3165 C C   . LEU A 1 375 ? 7.889   19.983  49.147  1.00 19.29 ? 375 LEU A C   1 
ATOM   3166 O O   . LEU A 1 375 ? 8.387   19.550  48.099  1.00 24.93 ? 375 LEU A O   1 
ATOM   3167 C CB  . LEU A 1 375 ? 9.549   20.577  50.921  1.00 12.43 ? 375 LEU A CB  1 
ATOM   3168 C CG  . LEU A 1 375 ? 10.514  21.601  51.494  1.00 15.47 ? 375 LEU A CG  1 
ATOM   3169 C CD1 . LEU A 1 375 ? 11.351  21.023  52.644  1.00 12.60 ? 375 LEU A CD1 1 
ATOM   3170 C CD2 . LEU A 1 375 ? 11.425  22.208  50.413  1.00 21.64 ? 375 LEU A CD2 1 
ATOM   3171 N N   . GLU A 1 376 ? 6.802   19.440  49.708  1.00 19.01 ? 376 GLU A N   1 
ATOM   3172 C CA  . GLU A 1 376 ? 6.022   18.395  49.056  1.00 22.13 ? 376 GLU A CA  1 
ATOM   3173 C C   . GLU A 1 376 ? 5.648   18.771  47.636  1.00 23.86 ? 376 GLU A C   1 
ATOM   3174 O O   . GLU A 1 376 ? 5.454   17.889  46.786  1.00 27.51 ? 376 GLU A O   1 
ATOM   3175 C CB  . GLU A 1 376 ? 4.731   18.150  49.835  1.00 28.78 ? 376 GLU A CB  1 
ATOM   3176 C CG  . GLU A 1 376 ? 4.800   17.172  50.967  1.00 31.32 ? 376 GLU A CG  1 
ATOM   3177 C CD  . GLU A 1 376 ? 3.407   16.838  51.469  1.00 31.02 ? 376 GLU A CD  1 
ATOM   3178 O OE1 . GLU A 1 376 ? 2.529   17.745  51.495  1.00 28.51 ? 376 GLU A OE1 1 
ATOM   3179 O OE2 . GLU A 1 376 ? 3.170   15.657  51.787  1.00 32.73 ? 376 GLU A OE2 1 
ATOM   3180 N N   . LYS A 1 377 ? 5.499   20.067  47.363  1.00 20.69 ? 377 LYS A N   1 
ATOM   3181 C CA  . LYS A 1 377 ? 4.957   20.522  46.090  1.00 21.36 ? 377 LYS A CA  1 
ATOM   3182 C C   . LYS A 1 377 ? 6.009   20.949  45.075  1.00 24.76 ? 377 LYS A C   1 
ATOM   3183 O O   . LYS A 1 377 ? 5.671   21.071  43.893  1.00 26.88 ? 377 LYS A O   1 
ATOM   3184 C CB  . LYS A 1 377 ? 3.996   21.697  46.313  1.00 25.75 ? 377 LYS A CB  1 
ATOM   3185 C CG  . LYS A 1 377 ? 2.744   21.348  47.097  1.00 35.72 ? 377 LYS A CG  1 
ATOM   3186 C CD  . LYS A 1 377 ? 1.841   20.446  46.289  1.00 47.15 ? 377 LYS A CD  1 
ATOM   3187 C CE  . LYS A 1 377 ? 0.425   20.444  46.835  1.00 53.95 ? 377 LYS A CE  1 
ATOM   3188 N NZ  . LYS A 1 377 ? 0.425   20.632  48.311  1.00 54.23 ? 377 LYS A NZ  1 
ATOM   3189 N N   . GLU A 1 378 ? 7.259   21.182  45.481  1.00 23.64 ? 378 GLU A N   1 
ATOM   3190 C CA  . GLU A 1 378 ? 8.260   21.735  44.567  1.00 27.68 ? 378 GLU A CA  1 
ATOM   3191 C C   . GLU A 1 378 ? 8.824   20.648  43.652  1.00 31.35 ? 378 GLU A C   1 
ATOM   3192 O O   . GLU A 1 378 ? 9.406   19.668  44.131  1.00 31.50 ? 378 GLU A O   1 
ATOM   3193 C CB  . GLU A 1 378 ? 9.405   22.386  45.348  1.00 28.85 ? 378 GLU A CB  1 
ATOM   3194 C CG  . GLU A 1 378 ? 8.961   23.402  46.387  1.00 31.41 ? 378 GLU A CG  1 
ATOM   3195 C CD  . GLU A 1 378 ? 8.541   24.735  45.793  1.00 36.56 ? 378 GLU A CD  1 
ATOM   3196 O OE1 . GLU A 1 378 ? 8.789   24.981  44.596  1.00 37.70 ? 378 GLU A OE1 1 
ATOM   3197 O OE2 . GLU A 1 378 ? 7.952   25.550  46.538  1.00 38.26 ? 378 GLU A OE2 1 
ATOM   3198 N N   . GLU A 1 379 ? 8.725   20.866  42.336  1.00 22.33 ? 379 GLU A N   1 
ATOM   3199 C CA  . GLU A 1 379 ? 9.217   19.882  41.373  1.00 29.52 ? 379 GLU A CA  1 
ATOM   3200 C C   . GLU A 1 379 ? 10.735  19.916  41.261  1.00 33.40 ? 379 GLU A C   1 
ATOM   3201 O O   . GLU A 1 379 ? 11.351  18.898  40.926  1.00 31.40 ? 379 GLU A O   1 
ATOM   3202 C CB  . GLU A 1 379 ? 8.579   20.114  39.997  1.00 32.86 ? 379 GLU A CB  1 
ATOM   3203 C CG  . GLU A 1 379 ? 7.048   20.235  40.028  1.00 47.33 ? 379 GLU A CG  1 
ATOM   3204 C CD  . GLU A 1 379 ? 6.333   19.678  38.784  1.00 54.86 ? 379 GLU A CD  1 
ATOM   3205 O OE1 . GLU A 1 379 ? 5.664   18.616  38.873  1.00 52.07 ? 379 GLU A OE1 1 
ATOM   3206 O OE2 . GLU A 1 379 ? 6.434   20.317  37.718  1.00 51.54 ? 379 GLU A OE2 1 
ATOM   3207 N N   . TRP A 1 380 ? 11.357  21.060  41.544  1.00 20.37 ? 380 TRP A N   1 
ATOM   3208 C CA  . TRP A 1 380 ? 12.787  21.207  41.298  1.00 22.38 ? 380 TRP A CA  1 
ATOM   3209 C C   . TRP A 1 380 ? 13.607  20.908  42.543  1.00 21.02 ? 380 TRP A C   1 
ATOM   3210 O O   . TRP A 1 380 ? 14.839  20.925  42.474  1.00 20.86 ? 380 TRP A O   1 
ATOM   3211 C CB  . TRP A 1 380 ? 13.091  22.622  40.760  1.00 21.46 ? 380 TRP A CB  1 
ATOM   3212 C CG  . TRP A 1 380 ? 12.522  23.658  41.673  1.00 22.34 ? 380 TRP A CG  1 
ATOM   3213 C CD1 . TRP A 1 380 ? 11.227  24.080  41.728  1.00 26.17 ? 380 TRP A CD1 1 
ATOM   3214 C CD2 . TRP A 1 380 ? 13.210  24.332  42.744  1.00 23.15 ? 380 TRP A CD2 1 
ATOM   3215 N NE1 . TRP A 1 380 ? 11.065  24.999  42.746  1.00 26.39 ? 380 TRP A NE1 1 
ATOM   3216 C CE2 . TRP A 1 380 ? 12.268  25.176  43.381  1.00 24.43 ? 380 TRP A CE2 1 
ATOM   3217 C CE3 . TRP A 1 380 ? 14.532  24.327  43.202  1.00 21.92 ? 380 TRP A CE3 1 
ATOM   3218 C CZ2 . TRP A 1 380 ? 12.604  26.002  44.465  1.00 26.09 ? 380 TRP A CZ2 1 
ATOM   3219 C CZ3 . TRP A 1 380 ? 14.869  25.149  44.287  1.00 22.92 ? 380 TRP A CZ3 1 
ATOM   3220 C CH2 . TRP A 1 380 ? 13.906  25.975  44.903  1.00 26.39 ? 380 TRP A CH2 1 
ATOM   3221 N N   . ILE A 1 381 ? 12.962  20.626  43.675  1.00 16.82 ? 381 ILE A N   1 
ATOM   3222 C CA  . ILE A 1 381 ? 13.643  20.194  44.897  1.00 16.94 ? 381 ILE A CA  1 
ATOM   3223 C C   . ILE A 1 381 ? 13.305  18.733  45.137  1.00 20.94 ? 381 ILE A C   1 
ATOM   3224 O O   . ILE A 1 381 ? 12.127  18.356  45.115  1.00 22.37 ? 381 ILE A O   1 
ATOM   3225 C CB  . ILE A 1 381 ? 13.230  21.016  46.136  1.00 16.06 ? 381 ILE A CB  1 
ATOM   3226 C CG1 . ILE A 1 381 ? 13.578  22.489  45.977  1.00 24.41 ? 381 ILE A CG1 1 
ATOM   3227 C CG2 . ILE A 1 381 ? 13.854  20.404  47.450  1.00 17.36 ? 381 ILE A CG2 1 
ATOM   3228 C CD1 . ILE A 1 381 ? 12.937  23.339  47.054  1.00 22.14 ? 381 ILE A CD1 1 
ATOM   3229 N N   . GLU A 1 382 ? 14.325  17.918  45.391  1.00 18.67 ? 382 GLU A N   1 
ATOM   3230 C CA  . GLU A 1 382 ? 14.138  16.529  45.790  1.00 14.79 ? 382 GLU A CA  1 
ATOM   3231 C C   . GLU A 1 382 ? 14.805  16.367  47.144  1.00 13.37 ? 382 GLU A C   1 
ATOM   3232 O O   . GLU A 1 382 ? 16.031  16.493  47.252  1.00 15.88 ? 382 GLU A O   1 
ATOM   3233 C CB  . GLU A 1 382 ? 14.743  15.558  44.779  1.00 18.34 ? 382 GLU A CB  1 
ATOM   3234 C CG  . GLU A 1 382 ? 14.459  14.097  45.045  1.00 29.66 ? 382 GLU A CG  1 
ATOM   3235 C CD  . GLU A 1 382 ? 14.974  13.185  43.924  1.00 49.14 ? 382 GLU A CD  1 
ATOM   3236 O OE1 . GLU A 1 382 ? 15.023  13.636  42.754  1.00 51.98 ? 382 GLU A OE1 1 
ATOM   3237 O OE2 . GLU A 1 382 ? 15.335  12.020  44.213  1.00 53.94 ? 382 GLU A OE2 1 
ATOM   3238 N N   . THR A 1 383 ? 14.010  16.093  48.180  1.00 14.17 ? 383 THR A N   1 
ATOM   3239 C CA  . THR A 1 383 ? 14.617  15.753  49.464  1.00 12.46 ? 383 THR A CA  1 
ATOM   3240 C C   . THR A 1 383 ? 15.160  14.323  49.414  1.00 15.00 ? 383 THR A C   1 
ATOM   3241 O O   . THR A 1 383 ? 14.576  13.430  48.773  1.00 14.97 ? 383 THR A O   1 
ATOM   3242 C CB  . THR A 1 383 ? 13.607  15.919  50.620  1.00 11.54 ? 383 THR A CB  1 
ATOM   3243 O OG1 . THR A 1 383 ? 12.458  15.082  50.402  1.00 14.51 ? 383 THR A OG1 1 
ATOM   3244 C CG2 . THR A 1 383 ? 13.220  17.419  50.790  1.00 17.52 ? 383 THR A CG2 1 
ATOM   3245 N N   . LEU A 1 384 ? 16.316  14.105  50.063  1.00 12.04 ? 384 LEU A N   1 
ATOM   3246 C CA  . LEU A 1 384 ? 16.983  12.804  49.989  1.00 11.53 ? 384 LEU A CA  1 
ATOM   3247 C C   . LEU A 1 384 ? 17.183  12.193  51.369  1.00 11.03 ? 384 LEU A C   1 
ATOM   3248 O O   . LEU A 1 384 ? 17.341  12.904  52.360  1.00 12.81 ? 384 LEU A O   1 
ATOM   3249 C CB  . LEU A 1 384 ? 18.364  12.914  49.336  1.00 13.83 ? 384 LEU A CB  1 
ATOM   3250 C CG  . LEU A 1 384 ? 18.402  13.532  47.944  1.00 14.56 ? 384 LEU A CG  1 
ATOM   3251 C CD1 . LEU A 1 384 ? 19.842  13.512  47.459  1.00 13.80 ? 384 LEU A CD1 1 
ATOM   3252 C CD2 . LEU A 1 384 ? 17.507  12.724  46.996  1.00 19.04 ? 384 LEU A CD2 1 
ATOM   3253 N N   . THR A 1 385 ? 17.189  10.865  51.420  1.00 11.89 ? 385 THR A N   1 
ATOM   3254 C CA  . THR A 1 385 ? 17.772  10.205  52.579  1.00 11.90 ? 385 THR A CA  1 
ATOM   3255 C C   . THR A 1 385 ? 19.301  10.279  52.532  1.00 12.25 ? 385 THR A C   1 
ATOM   3256 O O   . THR A 1 385 ? 19.907  10.619  51.508  1.00 12.68 ? 385 THR A O   1 
ATOM   3257 C CB  . THR A 1 385 ? 17.349  8.740   52.653  1.00 13.07 ? 385 THR A CB  1 
ATOM   3258 O OG1 . THR A 1 385 ? 17.946  7.968   51.584  1.00 14.46 ? 385 THR A OG1 1 
ATOM   3259 C CG2 . THR A 1 385 ? 15.812  8.634   52.644  1.00 13.08 ? 385 THR A CG2 1 
ATOM   3260 N N   . LEU A 1 386 ? 19.931  9.972   53.673  1.00 13.05 ? 386 LEU A N   1 
ATOM   3261 C CA  . LEU A 1 386 ? 21.398  9.900   53.690  1.00 13.81 ? 386 LEU A CA  1 
ATOM   3262 C C   . LEU A 1 386 ? 21.914  8.855   52.715  1.00 16.87 ? 386 LEU A C   1 
ATOM   3263 O O   . LEU A 1 386 ? 22.951  9.051   52.060  1.00 16.66 ? 386 LEU A O   1 
ATOM   3264 C CB  . LEU A 1 386 ? 21.886  9.570   55.101  1.00 13.97 ? 386 LEU A CB  1 
ATOM   3265 C CG  . LEU A 1 386 ? 21.491  10.596  56.169  1.00 13.02 ? 386 LEU A CG  1 
ATOM   3266 C CD1 . LEU A 1 386 ? 22.092  10.169  57.513  1.00 14.19 ? 386 LEU A CD1 1 
ATOM   3267 C CD2 . LEU A 1 386 ? 21.942  11.998  55.777  1.00 14.90 ? 386 LEU A CD2 1 
ATOM   3268 N N   . GLU A 1 387 ? 21.256  7.694   52.665  1.00 16.29 ? 387 GLU A N   1 
ATOM   3269 C CA  . GLU A 1 387 ? 21.672  6.669   51.719  1.00 20.08 ? 387 GLU A CA  1 
ATOM   3270 C C   . GLU A 1 387 ? 21.593  7.201   50.289  1.00 22.32 ? 387 GLU A C   1 
ATOM   3271 O O   . GLU A 1 387 ? 22.520  7.019   49.488  1.00 20.55 ? 387 GLU A O   1 
ATOM   3272 C CB  . GLU A 1 387 ? 20.810  5.418   51.889  1.00 28.58 ? 387 GLU A CB  1 
ATOM   3273 C CG  . GLU A 1 387 ? 20.668  4.936   53.333  1.00 52.43 ? 387 GLU A CG  1 
ATOM   3274 C CD  . GLU A 1 387 ? 21.670  3.844   53.698  1.00 71.55 ? 387 GLU A CD  1 
ATOM   3275 O OE1 . GLU A 1 387 ? 21.337  2.979   54.542  1.00 74.60 ? 387 GLU A OE1 1 
ATOM   3276 O OE2 . GLU A 1 387 ? 22.796  3.855   53.152  1.00 76.67 ? 387 GLU A OE2 1 
ATOM   3277 N N   . GLU A 1 388 ? 20.490  7.870   49.954  1.00 16.20 ? 388 GLU A N   1 
ATOM   3278 C CA  . GLU A 1 388 ? 20.340  8.423   48.605  1.00 19.74 ? 388 GLU A CA  1 
ATOM   3279 C C   . GLU A 1 388 ? 21.405  9.480   48.304  1.00 21.10 ? 388 GLU A C   1 
ATOM   3280 O O   . GLU A 1 388 ? 21.957  9.518   47.197  1.00 19.71 ? 388 GLU A O   1 
ATOM   3281 C CB  . GLU A 1 388 ? 18.936  9.006   48.435  1.00 19.82 ? 388 GLU A CB  1 
ATOM   3282 C CG  . GLU A 1 388 ? 17.851  7.950   48.229  1.00 22.34 ? 388 GLU A CG  1 
ATOM   3283 C CD  . GLU A 1 388 ? 16.434  8.523   48.395  1.00 20.34 ? 388 GLU A CD  1 
ATOM   3284 O OE1 . GLU A 1 388 ? 16.257  9.616   48.985  1.00 16.98 ? 388 GLU A OE1 1 
ATOM   3285 O OE2 . GLU A 1 388 ? 15.484  7.902   47.895  1.00 28.24 ? 388 GLU A OE2 1 
ATOM   3286 N N   . ALA A 1 389 ? 21.714  10.348  49.274  1.00 17.38 ? 389 ALA A N   1 
ATOM   3287 C CA  . ALA A 1 389 ? 22.767  11.335  49.058  1.00 14.85 ? 389 ALA A CA  1 
ATOM   3288 C C   . ALA A 1 389 ? 24.127  10.674  48.832  1.00 20.75 ? 389 ALA A C   1 
ATOM   3289 O O   . ALA A 1 389 ? 24.932  11.146  48.013  1.00 18.10 ? 389 ALA A O   1 
ATOM   3290 C CB  . ALA A 1 389 ? 22.834  12.303  50.251  1.00 13.58 ? 389 ALA A CB  1 
ATOM   3291 N N   . MET A 1 390 ? 24.405  9.587   49.561  1.00 17.92 ? 390 MET A N   1 
ATOM   3292 C CA  . MET A 1 390 ? 25.683  8.894   49.437  1.00 21.25 ? 390 MET A CA  1 
ATOM   3293 C C   . MET A 1 390 ? 25.857  8.287   48.053  1.00 23.05 ? 390 MET A C   1 
ATOM   3294 O O   . MET A 1 390 ? 26.979  8.263   47.520  1.00 23.50 ? 390 MET A O   1 
ATOM   3295 C CB  . MET A 1 390 ? 25.782  7.817   50.529  1.00 24.23 ? 390 MET A CB  1 
ATOM   3296 C CG  . MET A 1 390 ? 27.084  6.986   50.528  1.00 34.54 ? 390 MET A CG  1 
ATOM   3297 S SD  . MET A 1 390 ? 27.157  5.865   51.968  1.00 46.49 ? 390 MET A SD  1 
ATOM   3298 C CE  . MET A 1 390 ? 25.724  4.824   51.668  1.00 50.10 ? 390 MET A CE  1 
ATOM   3299 N N   . ARG A 1 391 ? 24.761  7.842   47.433  1.00 22.29 ? 391 ARG A N   1 
ATOM   3300 C CA  . ARG A 1 391 ? 24.809  7.054   46.207  1.00 29.62 ? 391 ARG A CA  1 
ATOM   3301 C C   . ARG A 1 391 ? 24.463  7.841   44.946  1.00 28.44 ? 391 ARG A C   1 
ATOM   3302 O O   . ARG A 1 391 ? 24.672  7.327   43.842  1.00 27.66 ? 391 ARG A O   1 
ATOM   3303 C CB  . ARG A 1 391 ? 23.844  5.865   46.321  1.00 38.16 ? 391 ARG A CB  1 
ATOM   3304 C CG  . ARG A 1 391 ? 24.209  4.852   47.388  1.00 47.43 ? 391 ARG A CG  1 
ATOM   3305 C CD  . ARG A 1 391 ? 23.548  3.518   47.103  1.00 62.88 ? 391 ARG A CD  1 
ATOM   3306 N NE  . ARG A 1 391 ? 23.695  2.585   48.214  1.00 72.74 ? 391 ARG A NE  1 
ATOM   3307 C CZ  . ARG A 1 391 ? 24.710  1.738   48.347  1.00 80.73 ? 391 ARG A CZ  1 
ATOM   3308 N NH1 . ARG A 1 391 ? 25.674  1.703   47.436  1.00 82.69 ? 391 ARG A NH1 1 
ATOM   3309 N NH2 . ARG A 1 391 ? 24.759  0.924   49.391  1.00 83.92 ? 391 ARG A NH2 1 
ATOM   3310 N N   . LYS A 1 392 ? 23.954  9.057   45.086  1.00 22.48 ? 392 LYS A N   1 
ATOM   3311 C CA  . LYS A 1 392 ? 23.423  9.821   43.960  1.00 25.06 ? 392 LYS A CA  1 
ATOM   3312 C C   . LYS A 1 392 ? 24.493  10.024  42.893  1.00 29.23 ? 392 LYS A C   1 
ATOM   3313 O O   . LYS A 1 392 ? 25.569  10.549  43.174  1.00 24.21 ? 392 LYS A O   1 
ATOM   3314 C CB  . LYS A 1 392 ? 22.913  11.172  44.471  1.00 24.43 ? 392 LYS A CB  1 
ATOM   3315 C CG  . LYS A 1 392 ? 22.041  11.917  43.490  1.00 32.67 ? 392 LYS A CG  1 
ATOM   3316 C CD  . LYS A 1 392 ? 20.869  11.065  43.053  1.00 39.79 ? 392 LYS A CD  1 
ATOM   3317 C CE  . LYS A 1 392 ? 19.606  11.469  43.774  1.00 34.40 ? 392 LYS A CE  1 
ATOM   3318 N NZ  . LYS A 1 392 ? 18.444  10.871  43.084  1.00 38.64 ? 392 LYS A NZ  1 
ATOM   3319 N N   . GLU A 1 393 ? 24.198  9.614   41.658  1.00 29.35 ? 393 GLU A N   1 
ATOM   3320 C CA  . GLU A 1 393 ? 25.247  9.658   40.643  1.00 31.39 ? 393 GLU A CA  1 
ATOM   3321 C C   . GLU A 1 393 ? 25.351  11.004  39.938  1.00 36.08 ? 393 GLU A C   1 
ATOM   3322 O O   . GLU A 1 393 ? 26.453  11.410  39.555  1.00 38.51 ? 393 GLU A O   1 
ATOM   3323 C CB  . GLU A 1 393 ? 25.042  8.539   39.619  1.00 38.82 ? 393 GLU A CB  1 
ATOM   3324 C CG  . GLU A 1 393 ? 25.937  7.338   39.902  1.00 54.68 ? 393 GLU A CG  1 
ATOM   3325 C CD  . GLU A 1 393 ? 25.684  6.171   38.973  1.00 65.76 ? 393 GLU A CD  1 
ATOM   3326 O OE1 . GLU A 1 393 ? 26.666  5.514   38.568  1.00 71.37 ? 393 GLU A OE1 1 
ATOM   3327 O OE2 . GLU A 1 393 ? 24.506  5.909   38.650  1.00 68.89 ? 393 GLU A OE2 1 
ATOM   3328 N N   . ASP A 1 394 ? 24.250  11.725  39.771  1.00 31.30 ? 394 ASP A N   1 
ATOM   3329 C CA  . ASP A 1 394 ? 24.263  12.944  38.963  1.00 35.57 ? 394 ASP A CA  1 
ATOM   3330 C C   . ASP A 1 394 ? 24.578  14.182  39.804  1.00 31.73 ? 394 ASP A C   1 
ATOM   3331 O O   . ASP A 1 394 ? 23.899  15.202  39.709  1.00 32.26 ? 394 ASP A O   1 
ATOM   3332 C CB  . ASP A 1 394 ? 22.917  13.083  38.257  1.00 43.49 ? 394 ASP A CB  1 
ATOM   3333 C CG  . ASP A 1 394 ? 21.736  12.758  39.182  1.00 52.33 ? 394 ASP A CG  1 
ATOM   3334 O OD1 . ASP A 1 394 ? 21.965  12.101  40.222  1.00 54.24 ? 394 ASP A OD1 1 
ATOM   3335 O OD2 . ASP A 1 394 ? 20.583  13.153  38.882  1.00 54.71 ? 394 ASP A OD2 1 
ATOM   3336 N N   . VAL A 1 395 ? 25.635  14.115  40.617  1.00 27.41 ? 395 VAL A N   1 
ATOM   3337 C CA  . VAL A 1 395 ? 26.050  15.233  41.458  1.00 25.01 ? 395 VAL A CA  1 
ATOM   3338 C C   . VAL A 1 395 ? 27.520  15.500  41.186  1.00 26.75 ? 395 VAL A C   1 
ATOM   3339 O O   . VAL A 1 395 ? 28.234  14.663  40.635  1.00 31.60 ? 395 VAL A O   1 
ATOM   3340 C CB  . VAL A 1 395 ? 25.817  14.984  42.969  1.00 26.15 ? 395 VAL A CB  1 
ATOM   3341 C CG1 . VAL A 1 395 ? 24.327  14.807  43.276  1.00 25.94 ? 395 VAL A CG1 1 
ATOM   3342 C CG2 . VAL A 1 395 ? 26.613  13.793  43.462  1.00 31.05 ? 395 VAL A CG2 1 
ATOM   3343 N N   . LYS A 1 396 ? 27.972  16.681  41.581  1.00 24.48 ? 396 LYS A N   1 
ATOM   3344 C CA  . LYS A 1 396 ? 29.358  17.065  41.363  1.00 24.61 ? 396 LYS A CA  1 
ATOM   3345 C C   . LYS A 1 396 ? 30.202  16.690  42.579  1.00 24.14 ? 396 LYS A C   1 
ATOM   3346 O O   . LYS A 1 396 ? 29.760  16.813  43.715  1.00 22.57 ? 396 LYS A O   1 
ATOM   3347 C CB  . LYS A 1 396 ? 29.450  18.560  41.086  1.00 26.97 ? 396 LYS A CB  1 
ATOM   3348 C CG  . LYS A 1 396 ? 30.823  19.037  40.694  1.00 32.69 ? 396 LYS A CG  1 
ATOM   3349 C CD  . LYS A 1 396 ? 30.831  20.552  40.727  1.00 39.58 ? 396 LYS A CD  1 
ATOM   3350 C CE  . LYS A 1 396 ? 32.057  21.117  40.084  1.00 41.79 ? 396 LYS A CE  1 
ATOM   3351 N NZ  . LYS A 1 396 ? 32.236  20.588  38.700  1.00 53.32 ? 396 LYS A NZ  1 
ATOM   3352 N N   . THR A 1 397 ? 31.423  16.215  42.328  1.00 24.30 ? 397 THR A N   1 
ATOM   3353 C CA  . THR A 1 397 ? 32.284  15.704  43.385  1.00 23.04 ? 397 THR A CA  1 
ATOM   3354 C C   . THR A 1 397 ? 33.673  16.327  43.285  1.00 23.53 ? 397 THR A C   1 
ATOM   3355 O O   . THR A 1 397 ? 34.069  16.857  42.237  1.00 27.12 ? 397 THR A O   1 
ATOM   3356 C CB  . THR A 1 397 ? 32.392  14.162  43.331  1.00 23.09 ? 397 THR A CB  1 
ATOM   3357 O OG1 . THR A 1 397 ? 33.109  13.779  42.154  1.00 25.50 ? 397 THR A OG1 1 
ATOM   3358 C CG2 . THR A 1 397 ? 31.005  13.524  43.268  1.00 26.53 ? 397 THR A CG2 1 
ATOM   3359 N N   . GLU A 1 398 ? 34.405  16.260  44.395  1.00 22.40 ? 398 GLU A N   1 
ATOM   3360 C CA  . GLU A 1 398 ? 35.795  16.686  44.441  1.00 26.40 ? 398 GLU A CA  1 
ATOM   3361 C C   . GLU A 1 398 ? 36.504  15.909  45.542  1.00 24.17 ? 398 GLU A C   1 
ATOM   3362 O O   . GLU A 1 398 ? 35.879  15.425  46.489  1.00 23.77 ? 398 GLU A O   1 
ATOM   3363 C CB  . GLU A 1 398 ? 35.920  18.198  44.667  1.00 36.76 ? 398 GLU A CB  1 
ATOM   3364 C CG  . GLU A 1 398 ? 37.322  18.745  44.415  1.00 56.98 ? 398 GLU A CG  1 
ATOM   3365 C CD  . GLU A 1 398 ? 37.962  18.167  43.161  1.00 68.32 ? 398 GLU A CD  1 
ATOM   3366 O OE1 . GLU A 1 398 ? 37.671  18.668  42.051  1.00 74.54 ? 398 GLU A OE1 1 
ATOM   3367 O OE2 . GLU A 1 398 ? 38.753  17.204  43.285  1.00 72.44 ? 398 GLU A OE2 1 
ATOM   3368 N N   . VAL A 1 399 ? 37.831  15.796  45.401  1.00 23.23 ? 399 VAL A N   1 
ATOM   3369 C CA  . VAL A 1 399 ? 38.680  15.138  46.386  1.00 22.12 ? 399 VAL A CA  1 
ATOM   3370 C C   . VAL A 1 399 ? 39.263  16.193  47.318  1.00 25.36 ? 399 VAL A C   1 
ATOM   3371 O O   . VAL A 1 399 ? 39.654  17.277  46.869  1.00 27.61 ? 399 VAL A O   1 
ATOM   3372 C CB  . VAL A 1 399 ? 39.799  14.343  45.682  1.00 23.72 ? 399 VAL A CB  1 
ATOM   3373 C CG1 . VAL A 1 399 ? 40.754  13.725  46.699  1.00 27.80 ? 399 VAL A CG1 1 
ATOM   3374 C CG2 . VAL A 1 399 ? 39.187  13.285  44.785  1.00 26.48 ? 399 VAL A CG2 1 
ATOM   3375 N N   . ILE A 1 400 ? 39.341  15.874  48.608  1.00 22.23 ? 400 ILE A N   1 
ATOM   3376 C CA  . ILE A 1 400 ? 39.991  16.725  49.597  1.00 24.80 ? 400 ILE A CA  1 
ATOM   3377 C C   . ILE A 1 400 ? 41.086  15.908  50.278  1.00 26.77 ? 400 ILE A C   1 
ATOM   3378 O O   . ILE A 1 400 ? 40.851  14.772  50.705  1.00 26.84 ? 400 ILE A O   1 
ATOM   3379 C CB  . ILE A 1 400 ? 38.975  17.301  50.608  1.00 27.97 ? 400 ILE A CB  1 
ATOM   3380 C CG1 . ILE A 1 400 ? 39.672  18.017  51.762  1.00 35.96 ? 400 ILE A CG1 1 
ATOM   3381 C CG2 . ILE A 1 400 ? 38.049  16.236  51.160  1.00 28.65 ? 400 ILE A CG2 1 
ATOM   3382 C CD1 . ILE A 1 400 ? 38.674  18.639  52.706  1.00 42.66 ? 400 ILE A CD1 1 
ATOM   3383 N N   . GLU A 1 401 ? 42.291  16.475  50.356  1.00 25.28 ? 401 GLU A N   1 
ATOM   3384 C CA  . GLU A 1 401 ? 43.417  15.718  50.877  1.00 26.36 ? 401 GLU A CA  1 
ATOM   3385 C C   . GLU A 1 401 ? 43.730  16.007  52.336  1.00 25.18 ? 401 GLU A C   1 
ATOM   3386 O O   . GLU A 1 401 ? 44.430  15.206  52.961  1.00 27.75 ? 401 GLU A O   1 
ATOM   3387 C CB  . GLU A 1 401 ? 44.681  15.977  50.041  1.00 28.47 ? 401 GLU A CB  1 
ATOM   3388 C CG  . GLU A 1 401 ? 44.588  15.475  48.612  1.00 35.77 ? 401 GLU A CG  1 
ATOM   3389 C CD  . GLU A 1 401 ? 44.363  13.973  48.515  1.00 49.00 ? 401 GLU A CD  1 
ATOM   3390 O OE1 . GLU A 1 401 ? 43.838  13.518  47.477  1.00 55.86 ? 401 GLU A OE1 1 
ATOM   3391 O OE2 . GLU A 1 401 ? 44.720  13.244  49.464  1.00 52.70 ? 401 GLU A OE2 1 
ATOM   3392 N N   . SER A 1 402 ? 43.234  17.113  52.892  1.00 21.15 ? 402 SER A N   1 
ATOM   3393 C CA  . SER A 1 402 ? 43.594  17.511  54.245  1.00 20.85 ? 402 SER A CA  1 
ATOM   3394 C C   . SER A 1 402 ? 42.535  18.472  54.775  1.00 24.78 ? 402 SER A C   1 
ATOM   3395 O O   . SER A 1 402 ? 42.064  19.344  54.037  1.00 27.58 ? 402 SER A O   1 
ATOM   3396 C CB  . SER A 1 402 ? 44.982  18.170  54.273  1.00 24.47 ? 402 SER A CB  1 
ATOM   3397 O OG  . SER A 1 402 ? 45.336  18.503  55.603  1.00 30.96 ? 402 SER A OG  1 
ATOM   3398 N N   . VAL A 1 403 ? 42.144  18.290  56.038  1.00 20.74 ? 403 VAL A N   1 
ATOM   3399 C CA  . VAL A 1 403 ? 41.287  19.262  56.706  1.00 22.62 ? 403 VAL A CA  1 
ATOM   3400 C C   . VAL A 1 403 ? 42.039  19.903  57.871  1.00 23.46 ? 403 VAL A C   1 
ATOM   3401 O O   . VAL A 1 403 ? 42.989  19.347  58.423  1.00 22.99 ? 403 VAL A O   1 
ATOM   3402 C CB  . VAL A 1 403 ? 39.960  18.650  57.193  1.00 21.20 ? 403 VAL A CB  1 
ATOM   3403 C CG1 . VAL A 1 403 ? 39.188  18.033  56.035  1.00 22.40 ? 403 VAL A CG1 1 
ATOM   3404 C CG2 . VAL A 1 403 ? 40.196  17.623  58.292  1.00 24.58 ? 403 VAL A CG2 1 
ATOM   3405 N N   . LYS A 1 404 ? 41.596  21.101  58.233  1.00 19.30 ? 404 LYS A N   1 
ATOM   3406 C CA  . LYS A 1 404 ? 42.039  21.788  59.441  1.00 18.01 ? 404 LYS A CA  1 
ATOM   3407 C C   . LYS A 1 404 ? 41.074  21.461  60.573  1.00 16.99 ? 404 LYS A C   1 
ATOM   3408 O O   . LYS A 1 404 ? 39.889  21.788  60.485  1.00 18.71 ? 404 LYS A O   1 
ATOM   3409 C CB  . LYS A 1 404 ? 42.064  23.299  59.218  1.00 23.24 ? 404 LYS A CB  1 
ATOM   3410 C CG  . LYS A 1 404 ? 43.158  23.748  58.304  1.00 44.46 ? 404 LYS A CG  1 
ATOM   3411 C CD  . LYS A 1 404 ? 44.325  24.249  59.114  1.00 52.38 ? 404 LYS A CD  1 
ATOM   3412 C CE  . LYS A 1 404 ? 45.236  25.107  58.274  1.00 59.21 ? 404 LYS A CE  1 
ATOM   3413 N NZ  . LYS A 1 404 ? 46.650  24.641  58.429  1.00 62.39 ? 404 LYS A NZ  1 
ATOM   3414 N N   . ALA A 1 405 ? 41.572  20.822  61.637  1.00 16.87 ? 405 ALA A N   1 
ATOM   3415 C CA  . ALA A 1 405 ? 40.706  20.326  62.699  1.00 14.73 ? 405 ALA A CA  1 
ATOM   3416 C C   . ALA A 1 405 ? 39.875  21.442  63.321  1.00 18.16 ? 405 ALA A C   1 
ATOM   3417 O O   . ALA A 1 405 ? 40.366  22.553  63.547  1.00 18.31 ? 405 ALA A O   1 
ATOM   3418 C CB  . ALA A 1 405 ? 41.561  19.637  63.778  1.00 15.51 ? 405 ALA A CB  1 
ATOM   3419 N N   . GLY A 1 406 ? 38.606  21.152  63.597  1.00 16.20 ? 406 GLY A N   1 
ATOM   3420 C CA  . GLY A 1 406 ? 37.780  22.154  64.233  1.00 15.39 ? 406 GLY A CA  1 
ATOM   3421 C C   . GLY A 1 406 ? 36.408  21.601  64.521  1.00 15.46 ? 406 GLY A C   1 
ATOM   3422 O O   . GLY A 1 406 ? 36.178  20.391  64.471  1.00 13.41 ? 406 GLY A O   1 
ATOM   3423 N N   . THR A 1 407 ? 35.497  22.513  64.836  1.00 12.02 ? 407 THR A N   1 
ATOM   3424 C CA  . THR A 1 407 ? 34.095  22.212  65.100  1.00 10.30 ? 407 THR A CA  1 
ATOM   3425 C C   . THR A 1 407 ? 33.235  23.210  64.348  1.00 11.34 ? 407 THR A C   1 
ATOM   3426 O O   . THR A 1 407 ? 33.731  24.153  63.738  1.00 12.81 ? 407 THR A O   1 
ATOM   3427 C CB  . THR A 1 407 ? 33.733  22.329  66.583  1.00 12.22 ? 407 THR A CB  1 
ATOM   3428 O OG1 . THR A 1 407 ? 33.634  23.722  66.955  1.00 13.34 ? 407 THR A OG1 1 
ATOM   3429 C CG2 . THR A 1 407 ? 34.745  21.616  67.472  1.00 14.49 ? 407 THR A CG2 1 
ATOM   3430 N N   . TRP A 1 408 ? 31.922  23.072  64.494  1.00 12.05 ? 408 TRP A N   1 
ATOM   3431 C CA  . TRP A 1 408 ? 31.020  24.037  63.885  1.00 11.44 ? 408 TRP A CA  1 
ATOM   3432 C C   . TRP A 1 408 ? 30.917  25.341  64.669  1.00 13.25 ? 408 TRP A C   1 
ATOM   3433 O O   . TRP A 1 408 ? 30.213  26.265  64.221  1.00 17.47 ? 408 TRP A O   1 
ATOM   3434 C CB  . TRP A 1 408 ? 29.643  23.403  63.663  1.00 15.39 ? 408 TRP A CB  1 
ATOM   3435 C CG  . TRP A 1 408 ? 28.849  22.933  64.874  1.00 13.32 ? 408 TRP A CG  1 
ATOM   3436 C CD1 . TRP A 1 408 ? 29.123  23.118  66.208  1.00 15.07 ? 408 TRP A CD1 1 
ATOM   3437 C CD2 . TRP A 1 408 ? 27.630  22.204  64.805  1.00 12.93 ? 408 TRP A CD2 1 
ATOM   3438 N NE1 . TRP A 1 408 ? 28.133  22.531  66.977  1.00 15.67 ? 408 TRP A NE1 1 
ATOM   3439 C CE2 . TRP A 1 408 ? 27.192  21.983  66.137  1.00 15.35 ? 408 TRP A CE2 1 
ATOM   3440 C CE3 . TRP A 1 408 ? 26.845  21.738  63.736  1.00 11.97 ? 408 TRP A CE3 1 
ATOM   3441 C CZ2 . TRP A 1 408 ? 26.007  21.295  66.429  1.00 13.14 ? 408 TRP A CZ2 1 
ATOM   3442 C CZ3 . TRP A 1 408 ? 25.656  21.061  64.020  1.00 13.95 ? 408 TRP A CZ3 1 
ATOM   3443 C CH2 . TRP A 1 408 ? 25.247  20.856  65.363  1.00 14.23 ? 408 TRP A CH2 1 
ATOM   3444 N N   . PHE A 1 409 ? 31.643  25.483  65.789  1.00 14.12 ? 409 PHE A N   1 
ATOM   3445 C CA  . PHE A 1 409 ? 31.717  26.776  66.486  1.00 19.80 ? 409 PHE A CA  1 
ATOM   3446 C C   . PHE A 1 409 ? 33.001  27.463  66.032  1.00 21.24 ? 409 PHE A C   1 
ATOM   3447 O O   . PHE A 1 409 ? 34.091  27.174  66.534  1.00 17.07 ? 409 PHE A O   1 
ATOM   3448 C CB  . PHE A 1 409 ? 31.660  26.623  68.005  1.00 22.34 ? 409 PHE A CB  1 
ATOM   3449 C CG  . PHE A 1 409 ? 31.233  27.890  68.734  1.00 30.32 ? 409 PHE A CG  1 
ATOM   3450 C CD1 . PHE A 1 409 ? 31.928  29.071  68.576  1.00 37.06 ? 409 PHE A CD1 1 
ATOM   3451 C CD2 . PHE A 1 409 ? 30.138  27.885  69.580  1.00 37.39 ? 409 PHE A CD2 1 
ATOM   3452 C CE1 . PHE A 1 409 ? 31.535  30.226  69.239  1.00 37.07 ? 409 PHE A CE1 1 
ATOM   3453 C CE2 . PHE A 1 409 ? 29.724  29.036  70.234  1.00 44.65 ? 409 PHE A CE2 1 
ATOM   3454 C CZ  . PHE A 1 409 ? 30.432  30.205  70.069  1.00 44.20 ? 409 PHE A CZ  1 
ATOM   3455 N N   . ASP A 1 410 ? 32.867  28.364  65.061  1.00 22.20 ? 410 ASP A N   1 
ATOM   3456 C CA  . ASP A 1 410 ? 33.981  29.163  64.538  1.00 24.90 ? 410 ASP A CA  1 
ATOM   3457 C C   . ASP A 1 410 ? 35.121  28.319  63.979  1.00 21.74 ? 410 ASP A C   1 
ATOM   3458 O O   . ASP A 1 410 ? 36.234  28.826  63.827  1.00 23.97 ? 410 ASP A O   1 
ATOM   3459 C CB  . ASP A 1 410 ? 34.542  30.113  65.607  1.00 35.45 ? 410 ASP A CB  1 
ATOM   3460 C CG  . ASP A 1 410 ? 33.505  31.075  66.143  1.00 46.45 ? 410 ASP A CG  1 
ATOM   3461 O OD1 . ASP A 1 410 ? 32.576  31.436  65.390  1.00 50.39 ? 410 ASP A OD1 1 
ATOM   3462 O OD2 . ASP A 1 410 ? 33.635  31.472  67.322  1.00 53.11 ? 410 ASP A OD2 1 
ATOM   3463 N N   . GLY A 1 411 ? 34.879  27.041  63.683  1.00 19.88 ? 411 GLY A N   1 
ATOM   3464 C CA  . GLY A 1 411 ? 35.920  26.161  63.169  1.00 17.69 ? 411 GLY A CA  1 
ATOM   3465 C C   . GLY A 1 411 ? 37.033  25.834  64.147  1.00 21.38 ? 411 GLY A C   1 
ATOM   3466 O O   . GLY A 1 411 ? 38.137  25.476  63.716  1.00 21.35 ? 411 GLY A O   1 
ATOM   3467 N N   . ASN A 1 412 ? 36.796  25.975  65.454  1.00 18.02 ? 412 ASN A N   1 
ATOM   3468 C CA  . ASN A 1 412 ? 37.861  25.757  66.433  1.00 16.17 ? 412 ASN A CA  1 
ATOM   3469 C C   . ASN A 1 412 ? 37.257  25.128  67.684  1.00 16.08 ? 412 ASN A C   1 
ATOM   3470 O O   . ASN A 1 412 ? 36.059  24.834  67.742  1.00 15.00 ? 412 ASN A O   1 
ATOM   3471 C CB  . ASN A 1 412 ? 38.643  27.052  66.722  1.00 17.72 ? 412 ASN A CB  1 
ATOM   3472 C CG  . ASN A 1 412 ? 37.825  28.119  67.428  1.00 16.56 ? 412 ASN A CG  1 
ATOM   3473 O OD1 . ASN A 1 412 ? 37.088  27.844  68.383  1.00 19.01 ? 412 ASN A OD1 1 
ATOM   3474 N ND2 . ASN A 1 412 ? 37.983  29.370  66.983  1.00 21.51 ? 412 ASN A ND2 1 
ATOM   3475 N N   . PHE A 1 413 ? 38.103  24.920  68.692  1.00 14.95 ? 413 PHE A N   1 
ATOM   3476 C CA  . PHE A 1 413 ? 37.734  24.130  69.850  1.00 15.95 ? 413 PHE A CA  1 
ATOM   3477 C C   . PHE A 1 413 ? 37.541  24.973  71.104  1.00 15.99 ? 413 PHE A C   1 
ATOM   3478 O O   . PHE A 1 413 ? 37.422  24.405  72.194  1.00 15.61 ? 413 PHE A O   1 
ATOM   3479 C CB  . PHE A 1 413 ? 38.796  23.051  70.102  1.00 15.03 ? 413 PHE A CB  1 
ATOM   3480 C CG  . PHE A 1 413 ? 38.852  21.999  69.030  1.00 16.13 ? 413 PHE A CG  1 
ATOM   3481 C CD1 . PHE A 1 413 ? 37.967  20.946  69.037  1.00 16.47 ? 413 PHE A CD1 1 
ATOM   3482 C CD2 . PHE A 1 413 ? 39.824  22.062  68.036  1.00 17.98 ? 413 PHE A CD2 1 
ATOM   3483 C CE1 . PHE A 1 413 ? 38.003  19.982  68.037  1.00 14.19 ? 413 PHE A CE1 1 
ATOM   3484 C CE2 . PHE A 1 413 ? 39.889  21.091  67.031  1.00 20.90 ? 413 PHE A CE2 1 
ATOM   3485 C CZ  . PHE A 1 413 ? 38.982  20.053  67.041  1.00 13.75 ? 413 PHE A CZ  1 
ATOM   3486 N N   . LEU A 1 414 ? 37.478  26.302  70.976  1.00 15.07 ? 414 LEU A N   1 
ATOM   3487 C CA  . LEU A 1 414 ? 37.591  27.147  72.164  1.00 16.22 ? 414 LEU A CA  1 
ATOM   3488 C C   . LEU A 1 414 ? 36.377  27.081  73.085  1.00 16.23 ? 414 LEU A C   1 
ATOM   3489 O O   . LEU A 1 414 ? 36.486  27.534  74.228  1.00 16.99 ? 414 LEU A O   1 
ATOM   3490 C CB  . LEU A 1 414 ? 37.870  28.601  71.763  1.00 18.84 ? 414 LEU A CB  1 
ATOM   3491 C CG  . LEU A 1 414 ? 39.233  28.837  71.096  1.00 18.45 ? 414 LEU A CG  1 
ATOM   3492 C CD1 . LEU A 1 414 ? 39.365  30.280  70.629  1.00 24.89 ? 414 LEU A CD1 1 
ATOM   3493 C CD2 . LEU A 1 414 ? 40.367  28.475  72.042  1.00 23.40 ? 414 LEU A CD2 1 
ATOM   3494 N N   . LYS A 1 415 ? 35.235  26.536  72.641  1.00 14.51 ? 415 LYS A N   1 
ATOM   3495 C CA  . LYS A 1 415 ? 34.131  26.411  73.587  1.00 16.47 ? 415 LYS A CA  1 
ATOM   3496 C C   . LYS A 1 415 ? 34.278  25.196  74.499  1.00 16.99 ? 415 LYS A C   1 
ATOM   3497 O O   . LYS A 1 415 ? 33.433  24.998  75.386  1.00 14.33 ? 415 LYS A O   1 
ATOM   3498 C CB  . LYS A 1 415 ? 32.786  26.345  72.848  1.00 15.43 ? 415 LYS A CB  1 
ATOM   3499 C CG  . LYS A 1 415 ? 32.390  27.655  72.172  1.00 21.00 ? 415 LYS A CG  1 
ATOM   3500 C CD  . LYS A 1 415 ? 32.183  28.774  73.176  1.00 26.88 ? 415 LYS A CD  1 
ATOM   3501 C CE  . LYS A 1 415 ? 30.750  28.815  73.669  1.00 31.86 ? 415 LYS A CE  1 
ATOM   3502 N NZ  . LYS A 1 415 ? 30.438  30.114  74.333  1.00 40.18 ? 415 LYS A NZ  1 
ATOM   3503 N N   . TRP A 1 416 ? 35.316  24.375  74.303  1.00 14.06 ? 416 TRP A N   1 
ATOM   3504 C CA  . TRP A 1 416 ? 35.482  23.175  75.118  1.00 15.03 ? 416 TRP A CA  1 
ATOM   3505 C C   . TRP A 1 416 ? 36.854  23.068  75.754  1.00 12.53 ? 416 TRP A C   1 
ATOM   3506 O O   . TRP A 1 416 ? 37.054  22.176  76.584  1.00 16.13 ? 416 TRP A O   1 
ATOM   3507 C CB  . TRP A 1 416 ? 35.229  21.914  74.276  1.00 12.06 ? 416 TRP A CB  1 
ATOM   3508 C CG  . TRP A 1 416 ? 33.861  21.911  73.672  1.00 10.08 ? 416 TRP A CG  1 
ATOM   3509 C CD1 . TRP A 1 416 ? 32.706  21.399  74.217  1.00 11.33 ? 416 TRP A CD1 1 
ATOM   3510 C CD2 . TRP A 1 416 ? 33.491  22.515  72.439  1.00 12.69 ? 416 TRP A CD2 1 
ATOM   3511 N NE1 . TRP A 1 416 ? 31.634  21.650  73.379  1.00 13.24 ? 416 TRP A NE1 1 
ATOM   3512 C CE2 . TRP A 1 416 ? 32.094  22.343  72.283  1.00 13.29 ? 416 TRP A CE2 1 
ATOM   3513 C CE3 . TRP A 1 416 ? 34.207  23.191  71.442  1.00 14.13 ? 416 TRP A CE3 1 
ATOM   3514 C CZ2 . TRP A 1 416 ? 31.406  22.825  71.165  1.00 15.51 ? 416 TRP A CZ2 1 
ATOM   3515 C CZ3 . TRP A 1 416 ? 33.516  23.659  70.320  1.00 14.97 ? 416 TRP A CZ3 1 
ATOM   3516 C CH2 . TRP A 1 416 ? 32.140  23.468  70.193  1.00 15.90 ? 416 TRP A CH2 1 
ATOM   3517 N N   . ILE A 1 417 ? 37.807  23.919  75.371  1.00 13.09 ? 417 ILE A N   1 
ATOM   3518 C CA  . ILE A 1 417 ? 39.168  23.828  75.891  1.00 12.60 ? 417 ILE A CA  1 
ATOM   3519 C C   . ILE A 1 417 ? 39.833  25.175  75.677  1.00 19.92 ? 417 ILE A C   1 
ATOM   3520 O O   . ILE A 1 417 ? 39.406  25.964  74.832  1.00 21.57 ? 417 ILE A O   1 
ATOM   3521 C CB  . ILE A 1 417 ? 39.931  22.669  75.192  1.00 14.28 ? 417 ILE A CB  1 
ATOM   3522 C CG1 . ILE A 1 417 ? 41.164  22.251  76.009  1.00 16.70 ? 417 ILE A CG1 1 
ATOM   3523 C CG2 . ILE A 1 417 ? 40.330  23.053  73.744  1.00 17.63 ? 417 ILE A CG2 1 
ATOM   3524 C CD1 . ILE A 1 417 ? 41.680  20.883  75.588  1.00 19.04 ? 417 ILE A CD1 1 
ATOM   3525 N N   . GLY A 1 418 ? 40.872  25.459  76.466  1.00 19.69 ? 418 GLY A N   1 
ATOM   3526 C CA  . GLY A 1 418 ? 41.698  26.626  76.242  1.00 24.81 ? 418 GLY A CA  1 
ATOM   3527 C C   . GLY A 1 418 ? 41.477  27.804  77.168  1.00 29.69 ? 418 GLY A C   1 
ATOM   3528 O O   . GLY A 1 418 ? 42.098  28.853  76.954  1.00 33.69 ? 418 GLY A O   1 
ATOM   3529 N N   . ASN A 1 419 ? 40.618  27.691  78.176  1.00 26.53 ? 419 ASN A N   1 
ATOM   3530 C CA  . ASN A 1 419 ? 40.615  28.680  79.246  1.00 21.79 ? 419 ASN A CA  1 
ATOM   3531 C C   . ASN A 1 419 ? 40.801  27.959  80.575  1.00 23.13 ? 419 ASN A C   1 
ATOM   3532 O O   . ASN A 1 419 ? 40.806  26.731  80.635  1.00 26.18 ? 419 ASN A O   1 
ATOM   3533 C CB  . ASN A 1 419 ? 39.355  29.565  79.214  1.00 26.42 ? 419 ASN A CB  1 
ATOM   3534 C CG  . ASN A 1 419 ? 38.062  28.857  79.655  1.00 33.55 ? 419 ASN A CG  1 
ATOM   3535 O OD1 . ASN A 1 419 ? 38.057  27.881  80.410  1.00 28.17 ? 419 ASN A OD1 1 
ATOM   3536 N ND2 . ASN A 1 419 ? 36.941  29.409  79.202  1.00 36.38 ? 419 ASN A ND2 1 
ATOM   3537 N N   . LYS A 1 420 ? 40.990  28.730  81.646  1.00 23.90 ? 420 LYS A N   1 
ATOM   3538 C CA  . LYS A 1 420 ? 41.393  28.121  82.910  1.00 24.84 ? 420 LYS A CA  1 
ATOM   3539 C C   . LYS A 1 420 ? 40.366  27.109  83.387  1.00 24.37 ? 420 LYS A C   1 
ATOM   3540 O O   . LYS A 1 420 ? 40.717  26.002  83.806  1.00 23.51 ? 420 LYS A O   1 
ATOM   3541 C CB  . LYS A 1 420 ? 41.619  29.195  83.982  1.00 32.09 ? 420 LYS A CB  1 
ATOM   3542 C CG  . LYS A 1 420 ? 42.912  29.961  83.837  1.00 43.52 ? 420 LYS A CG  1 
ATOM   3543 C CD  . LYS A 1 420 ? 43.170  30.813  85.083  1.00 50.96 ? 420 LYS A CD  1 
ATOM   3544 C CE  . LYS A 1 420 ? 43.721  32.181  84.715  1.00 57.57 ? 420 LYS A CE  1 
ATOM   3545 N NZ  . LYS A 1 420 ? 44.855  32.069  83.758  1.00 61.78 ? 420 LYS A NZ  1 
ATOM   3546 N N   . GLU A 1 421 ? 39.082  27.464  83.316  1.00 23.74 ? 421 GLU A N   1 
ATOM   3547 C CA  . GLU A 1 421 ? 38.053  26.603  83.889  1.00 25.52 ? 421 GLU A CA  1 
ATOM   3548 C C   . GLU A 1 421 ? 37.840  25.351  83.039  1.00 20.64 ? 421 GLU A C   1 
ATOM   3549 O O   . GLU A 1 421 ? 37.732  24.239  83.570  1.00 20.87 ? 421 GLU A O   1 
ATOM   3550 C CB  . GLU A 1 421 ? 36.751  27.394  84.038  1.00 28.36 ? 421 GLU A CB  1 
ATOM   3551 C CG  . GLU A 1 421 ? 36.839  28.639  84.949  1.00 37.27 ? 421 GLU A CG  1 
ATOM   3552 C CD  . GLU A 1 421 ? 37.669  29.779  84.348  1.00 49.81 ? 421 GLU A CD  1 
ATOM   3553 O OE1 . GLU A 1 421 ? 37.658  29.960  83.109  1.00 51.90 ? 421 GLU A OE1 1 
ATOM   3554 O OE2 . GLU A 1 421 ? 38.349  30.490  85.122  1.00 57.38 ? 421 GLU A OE2 1 
ATOM   3555 N N   . LYS A 1 422 ? 37.749  25.513  81.716  1.00 21.63 ? 422 LYS A N   1 
ATOM   3556 C CA  . LYS A 1 422 ? 37.624  24.347  80.852  1.00 17.70 ? 422 LYS A CA  1 
ATOM   3557 C C   . LYS A 1 422 ? 38.868  23.478  80.926  1.00 21.93 ? 422 LYS A C   1 
ATOM   3558 O O   . LYS A 1 422 ? 38.763  22.242  80.959  1.00 19.99 ? 422 LYS A O   1 
ATOM   3559 C CB  . LYS A 1 422 ? 37.339  24.774  79.406  1.00 21.30 ? 422 LYS A CB  1 
ATOM   3560 C CG  . LYS A 1 422 ? 35.916  25.311  79.239  1.00 18.67 ? 422 LYS A CG  1 
ATOM   3561 C CD  . LYS A 1 422 ? 35.710  26.024  77.897  1.00 18.48 ? 422 LYS A CD  1 
ATOM   3562 C CE  . LYS A 1 422 ? 34.468  26.916  77.916  1.00 16.06 ? 422 LYS A CE  1 
ATOM   3563 N NZ  . LYS A 1 422 ? 33.176  26.133  78.109  1.00 16.83 ? 422 LYS A NZ  1 
ATOM   3564 N N   . ASN A 1 423 ? 40.058  24.101  80.994  1.00 18.57 ? 423 ASN A N   1 
ATOM   3565 C CA  . ASN A 1 423 ? 41.256  23.282  81.101  1.00 21.21 ? 423 ASN A CA  1 
ATOM   3566 C C   . ASN A 1 423 ? 41.234  22.468  82.390  1.00 22.03 ? 423 ASN A C   1 
ATOM   3567 O O   . ASN A 1 423 ? 41.748  21.349  82.422  1.00 19.43 ? 423 ASN A O   1 
ATOM   3568 C CB  . ASN A 1 423 ? 42.520  24.150  81.019  1.00 21.98 ? 423 ASN A CB  1 
ATOM   3569 C CG  . ASN A 1 423 ? 42.850  24.600  79.574  1.00 20.57 ? 423 ASN A CG  1 
ATOM   3570 O OD1 . ASN A 1 423 ? 42.210  24.182  78.594  1.00 19.58 ? 423 ASN A OD1 1 
ATOM   3571 N ND2 . ASN A 1 423 ? 43.866  25.455  79.455  1.00 21.56 ? 423 ASN A ND2 1 
ATOM   3572 N N   . GLU A 1 424 ? 40.615  22.993  83.458  1.00 20.53 ? 424 GLU A N   1 
ATOM   3573 C CA  . GLU A 1 424 ? 40.569  22.234  84.701  1.00 21.73 ? 424 GLU A CA  1 
ATOM   3574 C C   . GLU A 1 424 ? 39.832  20.912  84.510  1.00 20.87 ? 424 GLU A C   1 
ATOM   3575 O O   . GLU A 1 424 ? 40.235  19.886  85.072  1.00 18.32 ? 424 GLU A O   1 
ATOM   3576 C CB  . GLU A 1 424 ? 39.924  23.067  85.813  1.00 29.65 ? 424 GLU A CB  1 
ATOM   3577 C CG  . GLU A 1 424 ? 39.749  22.322  87.135  1.00 43.02 ? 424 GLU A CG  1 
ATOM   3578 C CD  . GLU A 1 424 ? 41.069  21.842  87.746  1.00 60.82 ? 424 GLU A CD  1 
ATOM   3579 O OE1 . GLU A 1 424 ? 42.139  22.387  87.390  1.00 66.08 ? 424 GLU A OE1 1 
ATOM   3580 O OE2 . GLU A 1 424 ? 41.034  20.925  88.600  1.00 65.61 ? 424 GLU A OE2 1 
ATOM   3581 N N   . TYR A 1 425 ? 38.760  20.911  83.708  1.00 16.52 ? 425 TYR A N   1 
ATOM   3582 C CA  . TYR A 1 425 ? 38.056  19.660  83.435  1.00 16.24 ? 425 TYR A CA  1 
ATOM   3583 C C   . TYR A 1 425 ? 38.939  18.675  82.683  1.00 16.34 ? 425 TYR A C   1 
ATOM   3584 O O   . TYR A 1 425 ? 38.944  17.481  82.993  1.00 16.66 ? 425 TYR A O   1 
ATOM   3585 C CB  . TYR A 1 425 ? 36.783  19.915  82.632  1.00 13.82 ? 425 TYR A CB  1 
ATOM   3586 C CG  . TYR A 1 425 ? 35.550  20.137  83.453  1.00 13.22 ? 425 TYR A CG  1 
ATOM   3587 C CD1 . TYR A 1 425 ? 35.614  20.576  84.777  1.00 14.29 ? 425 TYR A CD1 1 
ATOM   3588 C CD2 . TYR A 1 425 ? 34.304  19.925  82.892  1.00 12.75 ? 425 TYR A CD2 1 
ATOM   3589 C CE1 . TYR A 1 425 ? 34.468  20.784  85.516  1.00 15.47 ? 425 TYR A CE1 1 
ATOM   3590 C CE2 . TYR A 1 425 ? 33.162  20.124  83.620  1.00 14.50 ? 425 TYR A CE2 1 
ATOM   3591 C CZ  . TYR A 1 425 ? 33.246  20.559  84.925  1.00 16.03 ? 425 TYR A CZ  1 
ATOM   3592 O OH  . TYR A 1 425 ? 32.067  20.748  85.598  1.00 15.70 ? 425 TYR A OH  1 
ATOM   3593 N N   . TRP A 1 426 ? 39.698  19.151  81.696  1.00 15.64 ? 426 TRP A N   1 
ATOM   3594 C CA  . TRP A 1 426 ? 40.589  18.238  80.985  1.00 15.02 ? 426 TRP A CA  1 
ATOM   3595 C C   . TRP A 1 426 ? 41.670  17.689  81.914  1.00 14.35 ? 426 TRP A C   1 
ATOM   3596 O O   . TRP A 1 426 ? 41.993  16.494  81.857  1.00 16.98 ? 426 TRP A O   1 
ATOM   3597 C CB  . TRP A 1 426 ? 41.208  18.944  79.768  1.00 15.05 ? 426 TRP A CB  1 
ATOM   3598 C CG  . TRP A 1 426 ? 40.202  19.112  78.653  1.00 14.34 ? 426 TRP A CG  1 
ATOM   3599 C CD1 . TRP A 1 426 ? 39.501  20.239  78.359  1.00 18.64 ? 426 TRP A CD1 1 
ATOM   3600 C CD2 . TRP A 1 426 ? 39.750  18.104  77.728  1.00 16.07 ? 426 TRP A CD2 1 
ATOM   3601 N NE1 . TRP A 1 426 ? 38.669  20.016  77.288  1.00 14.14 ? 426 TRP A NE1 1 
ATOM   3602 C CE2 . TRP A 1 426 ? 38.807  18.714  76.876  1.00 15.48 ? 426 TRP A CE2 1 
ATOM   3603 C CE3 . TRP A 1 426 ? 40.073  16.756  77.527  1.00 16.57 ? 426 TRP A CE3 1 
ATOM   3604 C CZ2 . TRP A 1 426 ? 38.146  18.012  75.844  1.00 14.30 ? 426 TRP A CZ2 1 
ATOM   3605 C CZ3 . TRP A 1 426 ? 39.440  16.062  76.501  1.00 18.99 ? 426 TRP A CZ3 1 
ATOM   3606 C CH2 . TRP A 1 426 ? 38.484  16.695  75.669  1.00 17.22 ? 426 TRP A CH2 1 
ATOM   3607 N N   . LYS A 1 427 ? 42.218  18.535  82.799  1.00 15.00 ? 427 LYS A N   1 
ATOM   3608 C CA  . LYS A 1 427 ? 43.220  18.061  83.760  1.00 19.28 ? 427 LYS A CA  1 
ATOM   3609 C C   . LYS A 1 427 ? 42.648  16.956  84.640  1.00 19.43 ? 427 LYS A C   1 
ATOM   3610 O O   . LYS A 1 427 ? 43.294  15.931  84.878  1.00 18.47 ? 427 LYS A O   1 
ATOM   3611 C CB  . LYS A 1 427 ? 43.715  19.216  84.633  1.00 22.82 ? 427 LYS A CB  1 
ATOM   3612 C CG  . LYS A 1 427 ? 44.417  20.350  83.883  1.00 36.17 ? 427 LYS A CG  1 
ATOM   3613 C CD  . LYS A 1 427 ? 44.739  21.514  84.822  1.00 45.30 ? 427 LYS A CD  1 
ATOM   3614 C CE  . LYS A 1 427 ? 45.476  21.018  86.066  1.00 53.66 ? 427 LYS A CE  1 
ATOM   3615 N NZ  . LYS A 1 427 ? 45.767  22.104  87.050  1.00 57.89 ? 427 LYS A NZ  1 
ATOM   3616 N N   . ILE A 1 428 ? 41.423  17.160  85.130  1.00 16.37 ? 428 ILE A N   1 
ATOM   3617 C CA  . ILE A 1 428 ? 40.743  16.152  85.935  1.00 18.13 ? 428 ILE A CA  1 
ATOM   3618 C C   . ILE A 1 428 ? 40.592  14.859  85.149  1.00 16.18 ? 428 ILE A C   1 
ATOM   3619 O O   . ILE A 1 428 ? 40.854  13.765  85.653  1.00 17.21 ? 428 ILE A O   1 
ATOM   3620 C CB  . ILE A 1 428 ? 39.376  16.686  86.397  1.00 17.95 ? 428 ILE A CB  1 
ATOM   3621 C CG1 . ILE A 1 428 ? 39.574  17.757  87.470  1.00 17.88 ? 428 ILE A CG1 1 
ATOM   3622 C CG2 . ILE A 1 428 ? 38.491  15.546  86.904  1.00 20.52 ? 428 ILE A CG2 1 
ATOM   3623 C CD1 . ILE A 1 428 ? 38.328  18.604  87.678  1.00 22.90 ? 428 ILE A CD1 1 
ATOM   3624 N N   . LEU A 1 429 ? 40.156  14.973  83.902  1.00 15.49 ? 429 LEU A N   1 
ATOM   3625 C CA  . LEU A 1 429 ? 39.938  13.787  83.095  1.00 13.83 ? 429 LEU A CA  1 
ATOM   3626 C C   . LEU A 1 429 ? 41.245  13.058  82.828  1.00 18.61 ? 429 LEU A C   1 
ATOM   3627 O O   . LEU A 1 429 ? 41.289  11.823  82.848  1.00 19.74 ? 429 LEU A O   1 
ATOM   3628 C CB  . LEU A 1 429 ? 39.279  14.200  81.789  1.00 17.01 ? 429 LEU A CB  1 
ATOM   3629 C CG  . LEU A 1 429 ? 38.945  13.066  80.835  1.00 19.77 ? 429 LEU A CG  1 
ATOM   3630 C CD1 . LEU A 1 429 ? 37.705  12.331  81.336  1.00 19.48 ? 429 LEU A CD1 1 
ATOM   3631 C CD2 . LEU A 1 429 ? 38.704  13.671  79.458  1.00 24.18 ? 429 LEU A CD2 1 
ATOM   3632 N N   . ILE A 1 430 ? 42.318  13.813  82.561  1.00 14.58 ? 430 ILE A N   1 
ATOM   3633 C CA  . ILE A 1 430 ? 43.627  13.220  82.308  1.00 16.71 ? 430 ILE A CA  1 
ATOM   3634 C C   . ILE A 1 430 ? 44.092  12.419  83.525  1.00 20.39 ? 430 ILE A C   1 
ATOM   3635 O O   . ILE A 1 430 ? 44.541  11.272  83.403  1.00 19.83 ? 430 ILE A O   1 
ATOM   3636 C CB  . ILE A 1 430 ? 44.637  14.316  81.919  1.00 18.74 ? 430 ILE A CB  1 
ATOM   3637 C CG1 . ILE A 1 430 ? 44.351  14.854  80.505  1.00 17.94 ? 430 ILE A CG1 1 
ATOM   3638 C CG2 . ILE A 1 430 ? 46.061  13.781  81.987  1.00 19.27 ? 430 ILE A CG2 1 
ATOM   3639 C CD1 . ILE A 1 430 ? 44.876  16.277  80.249  1.00 21.24 ? 430 ILE A CD1 1 
ATOM   3640 N N   . GLU A 1 431 ? 43.996  13.014  84.722  1.00 17.26 ? 431 GLU A N   1 
ATOM   3641 C CA  . GLU A 1 431 ? 44.394  12.305  85.934  1.00 18.58 ? 431 GLU A CA  1 
ATOM   3642 C C   . GLU A 1 431 ? 43.534  11.070  86.175  1.00 21.00 ? 431 GLU A C   1 
ATOM   3643 O O   . GLU A 1 431 ? 44.040  10.027  86.601  1.00 23.04 ? 431 GLU A O   1 
ATOM   3644 C CB  . GLU A 1 431 ? 44.305  13.245  87.141  1.00 27.89 ? 431 GLU A CB  1 
ATOM   3645 C CG  . GLU A 1 431 ? 45.400  14.287  87.185  1.00 36.34 ? 431 GLU A CG  1 
ATOM   3646 C CD  . GLU A 1 431 ? 46.777  13.687  86.986  1.00 42.91 ? 431 GLU A CD  1 
ATOM   3647 O OE1 . GLU A 1 431 ? 47.412  13.954  85.939  1.00 40.87 ? 431 GLU A OE1 1 
ATOM   3648 O OE2 . GLU A 1 431 ? 47.216  12.932  87.877  1.00 39.72 ? 431 GLU A OE2 1 
ATOM   3649 N N   . ALA A 1 432 ? 42.224  11.174  85.932  1.00 20.90 ? 432 ALA A N   1 
ATOM   3650 C CA  . ALA A 1 432 ? 41.345  10.042  86.211  1.00 20.74 ? 432 ALA A CA  1 
ATOM   3651 C C   . ALA A 1 432 ? 41.582  8.918   85.217  1.00 21.02 ? 432 ALA A C   1 
ATOM   3652 O O   . ALA A 1 432 ? 41.499  7.733   85.570  1.00 22.95 ? 432 ALA A O   1 
ATOM   3653 C CB  . ALA A 1 432 ? 39.881  10.488  86.164  1.00 17.93 ? 432 ALA A CB  1 
ATOM   3654 N N   . LYS A 1 433 ? 41.872  9.277   83.964  1.00 18.66 ? 433 LYS A N   1 
ATOM   3655 C CA  . LYS A 1 433 ? 42.116  8.270   82.937  1.00 20.75 ? 433 LYS A CA  1 
ATOM   3656 C C   . LYS A 1 433 ? 43.289  7.381   83.321  1.00 25.06 ? 433 LYS A C   1 
ATOM   3657 O O   . LYS A 1 433 ? 43.269  6.169   83.072  1.00 24.04 ? 433 LYS A O   1 
ATOM   3658 C CB  . LYS A 1 433 ? 42.363  8.954   81.587  1.00 20.28 ? 433 LYS A CB  1 
ATOM   3659 C CG  . LYS A 1 433 ? 42.853  8.005   80.484  1.00 22.86 ? 433 LYS A CG  1 
ATOM   3660 C CD  . LYS A 1 433 ? 41.753  7.039   80.035  1.00 22.13 ? 433 LYS A CD  1 
ATOM   3661 C CE  . LYS A 1 433 ? 42.288  5.912   79.152  1.00 23.30 ? 433 LYS A CE  1 
ATOM   3662 N NZ  . LYS A 1 433 ? 41.182  4.989   78.753  1.00 25.08 ? 433 LYS A NZ  1 
ATOM   3663 N N   . LYS A 1 434 ? 44.304  7.956   83.978  1.00 25.89 ? 434 LYS A N   1 
ATOM   3664 C CA  . LYS A 1 434 ? 45.439  7.156   84.415  1.00 28.30 ? 434 LYS A CA  1 
ATOM   3665 C C   . LYS A 1 434 ? 45.022  6.067   85.393  1.00 29.74 ? 434 LYS A C   1 
ATOM   3666 O O   . LYS A 1 434 ? 45.695  5.040   85.498  1.00 31.64 ? 434 LYS A O   1 
ATOM   3667 C CB  . LYS A 1 434 ? 46.501  8.042   85.072  1.00 35.66 ? 434 LYS A CB  1 
ATOM   3668 C CG  . LYS A 1 434 ? 47.028  9.151   84.190  1.00 35.21 ? 434 LYS A CG  1 
ATOM   3669 C CD  . LYS A 1 434 ? 48.139  9.902   84.905  1.00 45.28 ? 434 LYS A CD  1 
ATOM   3670 C CE  . LYS A 1 434 ? 48.561  11.104  84.101  1.00 47.13 ? 434 LYS A CE  1 
ATOM   3671 N NZ  . LYS A 1 434 ? 49.296  12.076  84.937  1.00 48.24 ? 434 LYS A NZ  1 
ATOM   3672 N N   . LYS A 1 435 ? 43.931  6.278   86.134  1.00 28.17 ? 435 LYS A N   1 
ATOM   3673 C CA  . LYS A 1 435 ? 43.481  5.324   87.137  1.00 29.74 ? 435 LYS A CA  1 
ATOM   3674 C C   . LYS A 1 435 ? 42.114  4.723   86.815  1.00 29.03 ? 435 LYS A C   1 
ATOM   3675 O O   . LYS A 1 435 ? 41.502  4.114   87.690  1.00 29.48 ? 435 LYS A O   1 
ATOM   3676 C CB  . LYS A 1 435 ? 43.437  5.986   88.517  1.00 36.73 ? 435 LYS A CB  1 
ATOM   3677 C CG  . LYS A 1 435 ? 44.658  6.814   88.867  1.00 42.06 ? 435 LYS A CG  1 
ATOM   3678 C CD  . LYS A 1 435 ? 44.436  7.541   90.182  1.00 49.79 ? 435 LYS A CD  1 
ATOM   3679 C CE  . LYS A 1 435 ? 45.610  8.429   90.547  1.00 54.56 ? 435 LYS A CE  1 
ATOM   3680 N NZ  . LYS A 1 435 ? 45.361  9.141   91.832  1.00 57.15 ? 435 LYS A NZ  1 
ATOM   3681 N N   . ALA A 1 436 ? 41.629  4.860   85.586  1.00 25.56 ? 436 ALA A N   1 
ATOM   3682 C CA  . ALA A 1 436 ? 40.264  4.451   85.267  1.00 25.12 ? 436 ALA A CA  1 
ATOM   3683 C C   . ALA A 1 436 ? 40.103  2.930   85.311  1.00 30.88 ? 436 ALA A C   1 
ATOM   3684 O O   . ALA A 1 436 ? 41.020  2.173   84.977  1.00 28.98 ? 436 ALA A O   1 
ATOM   3685 C CB  . ALA A 1 436 ? 39.872  4.974   83.889  1.00 24.41 ? 436 ALA A CB  1 
ATOM   3686 N N   . LYS A 1 437 ? 38.908  2.485   85.715  1.00 25.37 ? 437 LYS A N   1 
ATOM   3687 C CA  . LYS A 1 437 ? 38.603  1.064   85.861  1.00 30.10 ? 437 LYS A CA  1 
ATOM   3688 C C   . LYS A 1 437 ? 37.398  0.604   85.051  1.00 28.11 ? 437 LYS A C   1 
ATOM   3689 O O   . LYS A 1 437 ? 37.186  -0.609  84.936  1.00 36.15 ? 437 LYS A O   1 
ATOM   3690 C CB  . LYS A 1 437 ? 38.339  0.707   87.336  1.00 33.83 ? 437 LYS A CB  1 
ATOM   3691 C CG  . LYS A 1 437 ? 39.578  0.403   88.164  1.00 45.81 ? 437 LYS A CG  1 
ATOM   3692 C CD  . LYS A 1 437 ? 40.160  1.684   88.674  1.00 51.30 ? 437 LYS A CD  1 
ATOM   3693 C CE  . LYS A 1 437 ? 41.033  1.497   89.888  1.00 54.96 ? 437 LYS A CE  1 
ATOM   3694 N NZ  . LYS A 1 437 ? 41.345  2.856   90.430  1.00 55.45 ? 437 LYS A NZ  1 
ATOM   3695 N N   . ASN A 1 438 ? 36.609  1.515   84.497  1.00 25.23 ? 438 ASN A N   1 
ATOM   3696 C CA  . ASN A 1 438 ? 35.367  1.143   83.846  1.00 23.20 ? 438 ASN A CA  1 
ATOM   3697 C C   . ASN A 1 438 ? 35.004  2.223   82.839  1.00 24.29 ? 438 ASN A C   1 
ATOM   3698 O O   . ASN A 1 438 ? 35.672  3.260   82.735  1.00 23.17 ? 438 ASN A O   1 
ATOM   3699 C CB  . ASN A 1 438 ? 34.261  0.929   84.882  1.00 23.81 ? 438 ASN A CB  1 
ATOM   3700 C CG  . ASN A 1 438 ? 34.012  2.165   85.734  1.00 21.28 ? 438 ASN A CG  1 
ATOM   3701 O OD1 . ASN A 1 438 ? 33.644  3.202   85.211  1.00 20.66 ? 438 ASN A OD1 1 
ATOM   3702 N ND2 . ASN A 1 438 ? 34.228  2.055   87.049  1.00 23.73 ? 438 ASN A ND2 1 
ATOM   3703 N N   . ASP A 1 439 ? 33.901  1.994   82.125  1.00 25.49 ? 439 ASP A N   1 
ATOM   3704 C CA  . ASP A 1 439 ? 33.492  2.874   81.034  1.00 22.03 ? 439 ASP A CA  1 
ATOM   3705 C C   . ASP A 1 439 ? 32.864  4.183   81.493  1.00 18.80 ? 439 ASP A C   1 
ATOM   3706 O O   . ASP A 1 439 ? 32.485  4.992   80.644  1.00 16.80 ? 439 ASP A O   1 
ATOM   3707 C CB  . ASP A 1 439 ? 32.523  2.142   80.107  1.00 25.43 ? 439 ASP A CB  1 
ATOM   3708 C CG  . ASP A 1 439 ? 33.236  1.207   79.150  1.00 32.81 ? 439 ASP A CG  1 
ATOM   3709 O OD1 . ASP A 1 439 ? 34.485  1.163   79.151  1.00 33.59 ? 439 ASP A OD1 1 
ATOM   3710 O OD2 . ASP A 1 439 ? 32.547  0.502   78.394  1.00 37.05 ? 439 ASP A OD2 1 
ATOM   3711 N N   . TYR A 1 440 ? 32.745  4.445   82.800  1.00 18.22 ? 440 TYR A N   1 
ATOM   3712 C CA  . TYR A 1 440 ? 32.347  5.792   83.175  1.00 13.59 ? 440 TYR A CA  1 
ATOM   3713 C C   . TYR A 1 440 ? 33.374  6.826   82.742  1.00 14.48 ? 440 TYR A C   1 
ATOM   3714 O O   . TYR A 1 440 ? 33.037  8.016   82.663  1.00 14.77 ? 440 TYR A O   1 
ATOM   3715 C CB  . TYR A 1 440 ? 32.065  5.875   84.686  1.00 16.18 ? 440 TYR A CB  1 
ATOM   3716 C CG  . TYR A 1 440 ? 30.631  5.521   85.014  1.00 17.29 ? 440 TYR A CG  1 
ATOM   3717 C CD1 . TYR A 1 440 ? 29.593  6.352   84.645  1.00 18.76 ? 440 TYR A CD1 1 
ATOM   3718 C CD2 . TYR A 1 440 ? 30.310  4.322   85.639  1.00 23.27 ? 440 TYR A CD2 1 
ATOM   3719 C CE1 . TYR A 1 440 ? 28.274  6.026   84.931  1.00 19.82 ? 440 TYR A CE1 1 
ATOM   3720 C CE2 . TYR A 1 440 ? 28.975  3.991   85.929  1.00 20.72 ? 440 TYR A CE2 1 
ATOM   3721 C CZ  . TYR A 1 440 ? 27.981  4.843   85.567  1.00 26.28 ? 440 TYR A CZ  1 
ATOM   3722 O OH  . TYR A 1 440 ? 26.677  4.511   85.854  1.00 30.91 ? 440 TYR A OH  1 
ATOM   3723 N N   . ILE A 1 441 ? 34.628  6.417   82.476  1.00 15.04 ? 441 ILE A N   1 
ATOM   3724 C CA  . ILE A 1 441 ? 35.584  7.375   81.925  1.00 14.26 ? 441 ILE A CA  1 
ATOM   3725 C C   . ILE A 1 441 ? 35.103  7.854   80.560  1.00 17.71 ? 441 ILE A C   1 
ATOM   3726 O O   . ILE A 1 441 ? 35.341  9.009   80.170  1.00 14.89 ? 441 ILE A O   1 
ATOM   3727 C CB  . ILE A 1 441 ? 37.002  6.764   81.867  1.00 18.89 ? 441 ILE A CB  1 
ATOM   3728 C CG1 . ILE A 1 441 ? 38.060  7.855   81.715  1.00 17.64 ? 441 ILE A CG1 1 
ATOM   3729 C CG2 . ILE A 1 441 ? 37.136  5.731   80.749  1.00 17.35 ? 441 ILE A CG2 1 
ATOM   3730 C CD1 . ILE A 1 441 ? 38.239  8.709   82.963  1.00 23.92 ? 441 ILE A CD1 1 
ATOM   3731 N N   . LEU A 1 442 ? 34.428  6.984   79.812  1.00 15.28 ? 442 LEU A N   1 
ATOM   3732 C CA  . LEU A 1 442 ? 33.870  7.392   78.520  1.00 15.18 ? 442 LEU A CA  1 
ATOM   3733 C C   . LEU A 1 442 ? 32.730  8.387   78.684  1.00 13.56 ? 442 LEU A C   1 
ATOM   3734 O O   . LEU A 1 442 ? 32.590  9.322   77.875  1.00 12.52 ? 442 LEU A O   1 
ATOM   3735 C CB  . LEU A 1 442 ? 33.377  6.167   77.752  1.00 14.28 ? 442 LEU A CB  1 
ATOM   3736 C CG  . LEU A 1 442 ? 34.379  5.060   77.469  1.00 16.50 ? 442 LEU A CG  1 
ATOM   3737 C CD1 . LEU A 1 442 ? 33.757  3.924   76.652  1.00 18.67 ? 442 LEU A CD1 1 
ATOM   3738 C CD2 . LEU A 1 442 ? 35.624  5.660   76.789  1.00 16.74 ? 442 LEU A CD2 1 
ATOM   3739 N N   . VAL A 1 443 ? 31.868  8.172   79.681  1.00 13.35 ? 443 VAL A N   1 
ATOM   3740 C CA  . VAL A 1 443 ? 30.782  9.120   79.938  1.00 12.65 ? 443 VAL A CA  1 
ATOM   3741 C C   . VAL A 1 443 ? 31.341  10.515  80.181  1.00 13.79 ? 443 VAL A C   1 
ATOM   3742 O O   . VAL A 1 443 ? 30.800  11.509  79.677  1.00 13.85 ? 443 VAL A O   1 
ATOM   3743 C CB  . VAL A 1 443 ? 29.928  8.664   81.135  1.00 13.60 ? 443 VAL A CB  1 
ATOM   3744 C CG1 . VAL A 1 443 ? 28.752  9.644   81.368  1.00 12.56 ? 443 VAL A CG1 1 
ATOM   3745 C CG2 . VAL A 1 443 ? 29.441  7.219   80.968  1.00 11.61 ? 443 VAL A CG2 1 
ATOM   3746 N N   . ALA A 1 444 ? 32.428  10.605  80.962  1.00 10.95 ? 444 ALA A N   1 
ATOM   3747 C CA  . ALA A 1 444 ? 33.055  11.867  81.333  1.00 12.34 ? 444 ALA A CA  1 
ATOM   3748 C C   . ALA A 1 444 ? 33.729  12.545  80.154  1.00 14.68 ? 444 ALA A C   1 
ATOM   3749 O O   . ALA A 1 444 ? 34.080  13.727  80.249  1.00 14.82 ? 444 ALA A O   1 
ATOM   3750 C CB  . ALA A 1 444 ? 34.091  11.624  82.440  1.00 14.98 ? 444 ALA A CB  1 
ATOM   3751 N N   . GLU A 1 445 ? 33.956  11.820  79.070  1.00 11.52 ? 445 GLU A N   1 
ATOM   3752 C CA  . GLU A 1 445 ? 34.517  12.407  77.853  1.00 11.11 ? 445 GLU A CA  1 
ATOM   3753 C C   . GLU A 1 445 ? 33.477  13.122  76.991  1.00 13.39 ? 445 GLU A C   1 
ATOM   3754 O O   . GLU A 1 445 ? 33.844  13.723  75.975  1.00 14.90 ? 445 GLU A O   1 
ATOM   3755 C CB  . GLU A 1 445 ? 35.234  11.312  77.033  1.00 13.59 ? 445 GLU A CB  1 
ATOM   3756 C CG  . GLU A 1 445 ? 36.571  10.926  77.684  1.00 15.58 ? 445 GLU A CG  1 
ATOM   3757 C CD  . GLU A 1 445 ? 37.094  9.547   77.326  1.00 17.61 ? 445 GLU A CD  1 
ATOM   3758 O OE1 . GLU A 1 445 ? 36.556  8.908   76.407  1.00 20.25 ? 445 GLU A OE1 1 
ATOM   3759 O OE2 . GLU A 1 445 ? 38.115  9.110   77.949  1.00 18.07 ? 445 GLU A OE2 1 
ATOM   3760 N N   . GLY A 1 446 ? 32.204  13.120  77.372  1.00 14.77 ? 446 GLY A N   1 
ATOM   3761 C CA  . GLY A 1 446 ? 31.199  13.744  76.527  1.00 12.08 ? 446 GLY A CA  1 
ATOM   3762 C C   . GLY A 1 446 ? 31.384  15.250  76.476  1.00 14.80 ? 446 GLY A C   1 
ATOM   3763 O O   . GLY A 1 446 ? 31.813  15.865  77.451  1.00 13.97 ? 446 GLY A O   1 
ATOM   3764 N N   . SER A 1 447 ? 31.052  15.839  75.312  1.00 12.49 ? 447 SER A N   1 
ATOM   3765 C CA  . SER A 1 447 ? 31.374  17.245  75.072  1.00 13.01 ? 447 SER A CA  1 
ATOM   3766 C C   . SER A 1 447 ? 30.602  18.166  76.007  1.00 12.62 ? 447 SER A C   1 
ATOM   3767 O O   . SER A 1 447 ? 31.073  19.269  76.310  1.00 13.50 ? 447 SER A O   1 
ATOM   3768 C CB  . SER A 1 447 ? 31.102  17.635  73.626  1.00 13.68 ? 447 SER A CB  1 
ATOM   3769 O OG  . SER A 1 447 ? 29.712  17.517  73.345  1.00 14.45 ? 447 SER A OG  1 
ATOM   3770 N N   . ASP A 1 448 ? 29.419  17.741  76.452  1.00 10.96 ? 448 ASP A N   1 
ATOM   3771 C CA  . ASP A 1 448 ? 28.535  18.647  77.177  1.00 10.39 ? 448 ASP A CA  1 
ATOM   3772 C C   . ASP A 1 448 ? 29.188  19.204  78.430  1.00 8.92  ? 448 ASP A C   1 
ATOM   3773 O O   . ASP A 1 448 ? 28.973  20.373  78.779  1.00 11.64 ? 448 ASP A O   1 
ATOM   3774 C CB  . ASP A 1 448 ? 27.244  17.916  77.539  1.00 11.16 ? 448 ASP A CB  1 
ATOM   3775 C CG  . ASP A 1 448 ? 26.613  17.246  76.333  1.00 12.63 ? 448 ASP A CG  1 
ATOM   3776 O OD1 . ASP A 1 448 ? 27.059  16.126  75.923  1.00 15.54 ? 448 ASP A OD1 1 
ATOM   3777 O OD2 . ASP A 1 448 ? 25.673  17.848  75.749  1.00 16.47 ? 448 ASP A OD2 1 
ATOM   3778 N N   . TRP A 1 449 ? 29.939  18.374  79.163  1.00 9.75  ? 449 TRP A N   1 
ATOM   3779 C CA  . TRP A 1 449 ? 30.487  18.849  80.434  1.00 12.06 ? 449 TRP A CA  1 
ATOM   3780 C C   . TRP A 1 449 ? 31.421  20.034  80.212  1.00 11.77 ? 449 TRP A C   1 
ATOM   3781 O O   . TRP A 1 449 ? 31.388  21.039  80.955  1.00 13.14 ? 449 TRP A O   1 
ATOM   3782 C CB  . TRP A 1 449 ? 31.214  17.702  81.155  1.00 13.30 ? 449 TRP A CB  1 
ATOM   3783 C CG  . TRP A 1 449 ? 30.506  16.383  81.028  1.00 10.91 ? 449 TRP A CG  1 
ATOM   3784 C CD1 . TRP A 1 449 ? 30.991  15.230  80.456  1.00 12.18 ? 449 TRP A CD1 1 
ATOM   3785 C CD2 . TRP A 1 449 ? 29.196  16.083  81.486  1.00 10.74 ? 449 TRP A CD2 1 
ATOM   3786 N NE1 . TRP A 1 449 ? 30.042  14.238  80.528  1.00 12.78 ? 449 TRP A NE1 1 
ATOM   3787 C CE2 . TRP A 1 449 ? 28.926  14.729  81.150  1.00 9.27  ? 449 TRP A CE2 1 
ATOM   3788 C CE3 . TRP A 1 449 ? 28.204  16.823  82.141  1.00 12.49 ? 449 TRP A CE3 1 
ATOM   3789 C CZ2 . TRP A 1 449 ? 27.698  14.104  81.438  1.00 11.27 ? 449 TRP A CZ2 1 
ATOM   3790 C CZ3 . TRP A 1 449 ? 26.985  16.186  82.444  1.00 12.31 ? 449 TRP A CZ3 1 
ATOM   3791 C CH2 . TRP A 1 449 ? 26.744  14.845  82.081  1.00 12.80 ? 449 TRP A CH2 1 
ATOM   3792 N N   . PHE A 1 450 ? 32.249  19.941  79.172  1.00 11.57 ? 450 PHE A N   1 
ATOM   3793 C CA  . PHE A 1 450 ? 33.206  20.990  78.872  1.00 12.52 ? 450 PHE A CA  1 
ATOM   3794 C C   . PHE A 1 450 ? 32.522  22.237  78.344  1.00 11.49 ? 450 PHE A C   1 
ATOM   3795 O O   . PHE A 1 450 ? 32.997  23.357  78.584  1.00 16.26 ? 450 PHE A O   1 
ATOM   3796 C CB  . PHE A 1 450 ? 34.240  20.452  77.881  1.00 13.95 ? 450 PHE A CB  1 
ATOM   3797 C CG  . PHE A 1 450 ? 34.923  19.206  78.366  1.00 15.87 ? 450 PHE A CG  1 
ATOM   3798 C CD1 . PHE A 1 450 ? 36.087  19.300  79.107  1.00 13.81 ? 450 PHE A CD1 1 
ATOM   3799 C CD2 . PHE A 1 450 ? 34.410  17.946  78.069  1.00 14.68 ? 450 PHE A CD2 1 
ATOM   3800 C CE1 . PHE A 1 450 ? 36.724  18.149  79.577  1.00 18.53 ? 450 PHE A CE1 1 
ATOM   3801 C CE2 . PHE A 1 450 ? 35.025  16.782  78.547  1.00 18.86 ? 450 PHE A CE2 1 
ATOM   3802 C CZ  . PHE A 1 450 ? 36.196  16.895  79.318  1.00 14.46 ? 450 PHE A CZ  1 
ATOM   3803 N N   . TRP A 1 451 ? 31.399  22.050  77.638  1.00 12.98 ? 451 TRP A N   1 
ATOM   3804 C CA  . TRP A 1 451 ? 30.627  23.164  77.101  1.00 12.60 ? 451 TRP A CA  1 
ATOM   3805 C C   . TRP A 1 451 ? 30.110  24.065  78.219  1.00 13.12 ? 451 TRP A C   1 
ATOM   3806 O O   . TRP A 1 451 ? 30.208  25.293  78.131  1.00 14.99 ? 451 TRP A O   1 
ATOM   3807 C CB  . TRP A 1 451 ? 29.458  22.597  76.275  1.00 12.32 ? 451 TRP A CB  1 
ATOM   3808 C CG  . TRP A 1 451 ? 28.417  23.580  75.763  1.00 13.91 ? 451 TRP A CG  1 
ATOM   3809 C CD1 . TRP A 1 451 ? 27.161  23.799  76.280  1.00 16.94 ? 451 TRP A CD1 1 
ATOM   3810 C CD2 . TRP A 1 451 ? 28.519  24.423  74.603  1.00 17.48 ? 451 TRP A CD2 1 
ATOM   3811 N NE1 . TRP A 1 451 ? 26.489  24.735  75.520  1.00 18.56 ? 451 TRP A NE1 1 
ATOM   3812 C CE2 . TRP A 1 451 ? 27.295  25.126  74.481  1.00 20.44 ? 451 TRP A CE2 1 
ATOM   3813 C CE3 . TRP A 1 451 ? 29.518  24.640  73.642  1.00 17.33 ? 451 TRP A CE3 1 
ATOM   3814 C CZ2 . TRP A 1 451 ? 27.061  26.051  73.471  1.00 19.88 ? 451 TRP A CZ2 1 
ATOM   3815 C CZ3 . TRP A 1 451 ? 29.281  25.564  72.642  1.00 19.87 ? 451 TRP A CZ3 1 
ATOM   3816 C CH2 . TRP A 1 451 ? 28.058  26.253  72.560  1.00 21.56 ? 451 TRP A CH2 1 
ATOM   3817 N N   . TRP A 1 452 ? 29.530  23.464  79.271  1.00 12.39 ? 452 TRP A N   1 
ATOM   3818 C CA  . TRP A 1 452 ? 28.922  24.261  80.335  1.00 13.61 ? 452 TRP A CA  1 
ATOM   3819 C C   . TRP A 1 452 ? 29.947  24.809  81.319  1.00 14.11 ? 452 TRP A C   1 
ATOM   3820 O O   . TRP A 1 452 ? 29.644  25.772  82.022  1.00 15.08 ? 452 TRP A O   1 
ATOM   3821 C CB  . TRP A 1 452 ? 27.870  23.443  81.110  1.00 12.80 ? 452 TRP A CB  1 
ATOM   3822 C CG  . TRP A 1 452 ? 26.725  23.072  80.224  1.00 12.17 ? 452 TRP A CG  1 
ATOM   3823 C CD1 . TRP A 1 452 ? 26.438  21.829  79.748  1.00 12.13 ? 452 TRP A CD1 1 
ATOM   3824 C CD2 . TRP A 1 452 ? 25.771  23.958  79.634  1.00 13.21 ? 452 TRP A CD2 1 
ATOM   3825 N NE1 . TRP A 1 452 ? 25.358  21.891  78.904  1.00 11.26 ? 452 TRP A NE1 1 
ATOM   3826 C CE2 . TRP A 1 452 ? 24.937  23.188  78.815  1.00 14.16 ? 452 TRP A CE2 1 
ATOM   3827 C CE3 . TRP A 1 452 ? 25.548  25.340  79.714  1.00 15.58 ? 452 TRP A CE3 1 
ATOM   3828 C CZ2 . TRP A 1 452 ? 23.876  23.735  78.103  1.00 18.20 ? 452 TRP A CZ2 1 
ATOM   3829 C CZ3 . TRP A 1 452 ? 24.500  25.886  79.013  1.00 21.95 ? 452 TRP A CZ3 1 
ATOM   3830 C CH2 . TRP A 1 452 ? 23.676  25.086  78.208  1.00 20.08 ? 452 TRP A CH2 1 
ATOM   3831 N N   . GLN A 1 453 ? 31.113  24.242  81.396  1.00 14.83 ? 453 GLN A N   1 
ATOM   3832 C CA  . GLN A 1 453 ? 32.089  24.681  82.350  1.00 16.14 ? 453 GLN A CA  1 
ATOM   3833 C C   . GLN A 1 453 ? 32.707  26.007  81.997  1.00 18.88 ? 453 GLN A C   1 
ATOM   3834 O O   . GLN A 1 453 ? 32.956  26.294  80.896  1.00 22.26 ? 453 GLN A O   1 
ATOM   3835 C CB  . GLN A 1 453 ? 33.138  23.587  82.503  1.00 19.29 ? 453 GLN A CB  1 
ATOM   3836 C CG  . GLN A 1 453 ? 34.405  23.905  83.285  1.00 19.75 ? 453 GLN A CG  1 
ATOM   3837 C CD  . GLN A 1 453 ? 34.229  24.098  84.773  1.00 25.40 ? 453 GLN A CD  1 
ATOM   3838 O OE1 . GLN A 1 453 ? 33.164  24.139  85.282  1.00 21.94 ? 453 GLN A OE1 1 
ATOM   3839 N NE2 . GLN A 1 453 ? 35.343  24.239  85.453  1.00 25.07 ? 453 GLN A NE2 1 
ATOM   3840 N N   . GLY A 1 454 ? 32.936  26.803  83.012  1.00 28.20 ? 454 GLY A N   1 
ATOM   3841 C CA  . GLY A 1 454 ? 33.607  28.070  82.828  1.00 38.41 ? 454 GLY A CA  1 
ATOM   3842 C C   . GLY A 1 454 ? 32.946  29.042  81.917  1.00 46.80 ? 454 GLY A C   1 
ATOM   3843 O O   . GLY A 1 454 ? 33.542  29.601  80.979  1.00 51.49 ? 454 GLY A O   1 
ATOM   3844 N N   . GLU A 1 455 ? 31.682  29.210  82.214  1.00 47.13 ? 455 GLU A N   1 
ATOM   3845 C CA  . GLU A 1 455 ? 30.834  30.112  81.535  1.00 48.93 ? 455 GLU A CA  1 
ATOM   3846 C C   . GLU A 1 455 ? 30.195  30.907  82.656  1.00 48.32 ? 455 GLU A C   1 
ATOM   3847 O O   . GLU A 1 455 ? 30.371  30.598  83.800  1.00 39.60 ? 455 GLU A O   1 
ATOM   3848 C CB  . GLU A 1 455 ? 29.797  29.363  80.720  1.00 44.17 ? 455 GLU A CB  1 
ATOM   3849 C CG  . GLU A 1 455 ? 30.397  28.449  79.664  1.00 43.51 ? 455 GLU A CG  1 
ATOM   3850 C CD  . GLU A 1 455 ? 30.814  29.202  78.423  1.00 47.49 ? 455 GLU A CD  1 
ATOM   3851 O OE1 . GLU A 1 455 ? 31.586  28.673  77.617  1.00 41.80 ? 455 GLU A OE1 1 
ATOM   3852 O OE2 . GLU A 1 455 ? 30.346  30.335  78.259  1.00 40.87 ? 455 GLU A OE2 1 
ATOM   3853 N N   . GLU A 1 456 ? 29.457  31.937  82.282  1.00 55.09 ? 456 GLU A N   1 
ATOM   3854 C CA  . GLU A 1 456 ? 28.713  32.791  83.191  1.00 60.54 ? 456 GLU A CA  1 
ATOM   3855 C C   . GLU A 1 456 ? 27.787  31.896  83.975  1.00 59.43 ? 456 GLU A C   1 
ATOM   3856 O O   . GLU A 1 456 ? 27.112  31.074  83.388  1.00 54.09 ? 456 GLU A O   1 
ATOM   3857 C CB  . GLU A 1 456 ? 27.831  33.706  82.335  1.00 68.64 ? 456 GLU A CB  1 
ATOM   3858 C CG  . GLU A 1 456 ? 27.961  35.220  82.567  1.00 72.66 ? 456 GLU A CG  1 
ATOM   3859 C CD  . GLU A 1 456 ? 27.407  36.063  81.414  1.00 75.77 ? 456 GLU A CD  1 
ATOM   3860 O OE1 . GLU A 1 456 ? 28.161  36.899  80.863  1.00 78.92 ? 456 GLU A OE1 1 
ATOM   3861 O OE2 . GLU A 1 456 ? 26.222  35.917  81.061  1.00 74.26 ? 456 GLU A OE2 1 
ATOM   3862 N N   . LYS A 1 457 ? 27.731  32.067  85.285  1.00 59.88 ? 457 LYS A N   1 
ATOM   3863 C CA  . LYS A 1 457 ? 26.834  31.315  86.144  1.00 55.66 ? 457 LYS A CA  1 
ATOM   3864 C C   . LYS A 1 457 ? 25.394  31.333  85.633  1.00 56.74 ? 457 LYS A C   1 
ATOM   3865 O O   . LYS A 1 457 ? 24.932  32.347  85.165  1.00 60.77 ? 457 LYS A O   1 
ATOM   3866 C CB  . LYS A 1 457 ? 26.853  31.843  87.561  1.00 56.53 ? 457 LYS A CB  1 
ATOM   3867 C CG  . LYS A 1 457 ? 26.290  30.837  88.513  1.00 59.20 ? 457 LYS A CG  1 
ATOM   3868 C CD  . LYS A 1 457 ? 26.311  31.307  89.954  1.00 68.65 ? 457 LYS A CD  1 
ATOM   3869 C CE  . LYS A 1 457 ? 25.163  30.664  90.720  1.00 71.46 ? 457 LYS A CE  1 
ATOM   3870 N NZ  . LYS A 1 457 ? 24.831  29.290  90.211  1.00 69.51 ? 457 LYS A NZ  1 
ATOM   3871 N N   . ALA A 1 458 ? 24.686  30.210  85.735  1.00 49.26 ? 458 ALA A N   1 
ATOM   3872 C CA  . ALA A 1 458 ? 23.330  30.117  85.200  1.00 45.37 ? 458 ALA A CA  1 
ATOM   3873 C C   . ALA A 1 458 ? 22.508  29.103  85.944  1.00 34.52 ? 458 ALA A C   1 
ATOM   3874 O O   . ALA A 1 458 ? 23.050  28.220  86.525  1.00 31.45 ? 458 ALA A O   1 
ATOM   3875 C CB  . ALA A 1 458 ? 23.411  29.762  83.737  1.00 44.13 ? 458 ALA A CB  1 
ATOM   3876 N N   . PRO A 1 459 ? 21.194  29.234  85.947  1.00 34.83 ? 459 PRO A N   1 
ATOM   3877 C CA  . PRO A 1 459 ? 20.415  28.259  86.725  1.00 34.80 ? 459 PRO A CA  1 
ATOM   3878 C C   . PRO A 1 459 ? 20.673  26.829  86.259  1.00 33.54 ? 459 PRO A C   1 
ATOM   3879 O O   . PRO A 1 459 ? 20.821  26.555  85.063  1.00 29.81 ? 459 PRO A O   1 
ATOM   3880 C CB  . PRO A 1 459 ? 18.960  28.683  86.491  1.00 39.93 ? 459 PRO A CB  1 
ATOM   3881 C CG  . PRO A 1 459 ? 18.994  29.770  85.455  1.00 48.95 ? 459 PRO A CG  1 
ATOM   3882 C CD  . PRO A 1 459 ? 20.367  30.346  85.453  1.00 44.65 ? 459 PRO A CD  1 
ATOM   3883 N N   . PHE A 1 460 ? 20.799  25.930  87.237  1.00 27.88 ? 460 PHE A N   1 
ATOM   3884 C CA  . PHE A 1 460 ? 20.938  24.485  87.030  1.00 26.70 ? 460 PHE A CA  1 
ATOM   3885 C C   . PHE A 1 460 ? 22.256  24.046  86.401  1.00 27.42 ? 460 PHE A C   1 
ATOM   3886 O O   . PHE A 1 460 ? 22.551  22.846  86.337  1.00 30.85 ? 460 PHE A O   1 
ATOM   3887 C CB  . PHE A 1 460 ? 19.777  23.958  86.181  1.00 27.69 ? 460 PHE A CB  1 
ATOM   3888 C CG  . PHE A 1 460 ? 18.435  24.227  86.771  1.00 32.11 ? 460 PHE A CG  1 
ATOM   3889 C CD1 . PHE A 1 460 ? 18.169  23.893  88.084  1.00 36.94 ? 460 PHE A CD1 1 
ATOM   3890 C CD2 . PHE A 1 460 ? 17.444  24.831  86.025  1.00 30.57 ? 460 PHE A CD2 1 
ATOM   3891 C CE1 . PHE A 1 460 ? 16.932  24.148  88.641  1.00 39.08 ? 460 PHE A CE1 1 
ATOM   3892 C CE2 . PHE A 1 460 ? 16.205  25.093  86.575  1.00 36.80 ? 460 PHE A CE2 1 
ATOM   3893 C CZ  . PHE A 1 460 ? 15.944  24.751  87.884  1.00 39.26 ? 460 PHE A CZ  1 
ATOM   3894 N N   . VAL A 1 461 ? 23.109  24.980  85.988  1.00 27.77 ? 461 VAL A N   1 
ATOM   3895 C CA  . VAL A 1 461 ? 24.305  24.517  85.303  1.00 33.04 ? 461 VAL A CA  1 
ATOM   3896 C C   . VAL A 1 461 ? 25.288  23.877  86.271  1.00 26.23 ? 461 VAL A C   1 
ATOM   3897 O O   . VAL A 1 461 ? 26.112  23.060  85.850  1.00 29.65 ? 461 VAL A O   1 
ATOM   3898 C CB  . VAL A 1 461 ? 24.954  25.650  84.489  1.00 44.46 ? 461 VAL A CB  1 
ATOM   3899 C CG1 . VAL A 1 461 ? 23.943  26.229  83.510  1.00 49.40 ? 461 VAL A CG1 1 
ATOM   3900 C CG2 . VAL A 1 461 ? 25.519  26.717  85.409  1.00 49.60 ? 461 VAL A CG2 1 
ATOM   3901 N N   . GLU A 1 462 ? 25.181  24.158  87.574  1.00 21.87 ? 462 GLU A N   1 
ATOM   3902 C CA  . GLU A 1 462 ? 25.995  23.450  88.552  1.00 24.51 ? 462 GLU A CA  1 
ATOM   3903 C C   . GLU A 1 462 ? 25.662  21.965  88.618  1.00 27.11 ? 462 GLU A C   1 
ATOM   3904 O O   . GLU A 1 462 ? 26.461  21.183  89.140  1.00 25.49 ? 462 GLU A O   1 
ATOM   3905 C CB  . GLU A 1 462 ? 25.818  24.058  89.940  1.00 37.24 ? 462 GLU A CB  1 
ATOM   3906 C CG  . GLU A 1 462 ? 26.860  25.073  90.317  1.00 52.90 ? 462 GLU A CG  1 
ATOM   3907 C CD  . GLU A 1 462 ? 26.352  26.038  91.362  1.00 66.53 ? 462 GLU A CD  1 
ATOM   3908 O OE1 . GLU A 1 462 ? 25.914  25.565  92.430  1.00 70.79 ? 462 GLU A OE1 1 
ATOM   3909 O OE2 . GLU A 1 462 ? 26.391  27.263  91.119  1.00 72.60 ? 462 GLU A OE2 1 
ATOM   3910 N N   . VAL A 1 463 ? 24.491  21.553  88.135  1.00 16.78 ? 463 VAL A N   1 
ATOM   3911 C CA  . VAL A 1 463 ? 24.201  20.120  88.093  1.00 13.88 ? 463 VAL A CA  1 
ATOM   3912 C C   . VAL A 1 463 ? 25.117  19.412  87.105  1.00 14.10 ? 463 VAL A C   1 
ATOM   3913 O O   . VAL A 1 463 ? 25.499  18.248  87.309  1.00 15.65 ? 463 VAL A O   1 
ATOM   3914 C CB  . VAL A 1 463 ? 22.716  19.897  87.743  1.00 14.37 ? 463 VAL A CB  1 
ATOM   3915 C CG1 . VAL A 1 463 ? 22.413  18.407  87.648  1.00 23.51 ? 463 VAL A CG1 1 
ATOM   3916 C CG2 . VAL A 1 463 ? 21.822  20.573  88.777  1.00 20.43 ? 463 VAL A CG2 1 
ATOM   3917 N N   . PHE A 1 464 ? 25.437  20.071  85.983  1.00 13.50 ? 464 PHE A N   1 
ATOM   3918 C CA  . PHE A 1 464 ? 26.343  19.454  85.007  1.00 12.98 ? 464 PHE A CA  1 
ATOM   3919 C C   . PHE A 1 464 ? 27.701  19.181  85.635  1.00 13.37 ? 464 PHE A C   1 
ATOM   3920 O O   . PHE A 1 464 ? 28.327  18.150  85.348  1.00 13.12 ? 464 PHE A O   1 
ATOM   3921 C CB  . PHE A 1 464 ? 26.488  20.358  83.784  1.00 12.28 ? 464 PHE A CB  1 
ATOM   3922 C CG  . PHE A 1 464 ? 25.270  20.360  82.908  1.00 12.05 ? 464 PHE A CG  1 
ATOM   3923 C CD1 . PHE A 1 464 ? 25.096  19.390  81.916  1.00 11.05 ? 464 PHE A CD1 1 
ATOM   3924 C CD2 . PHE A 1 464 ? 24.292  21.324  83.079  1.00 12.64 ? 464 PHE A CD2 1 
ATOM   3925 C CE1 . PHE A 1 464 ? 23.931  19.391  81.105  1.00 12.65 ? 464 PHE A CE1 1 
ATOM   3926 C CE2 . PHE A 1 464 ? 23.130  21.331  82.275  1.00 14.94 ? 464 PHE A CE2 1 
ATOM   3927 C CZ  . PHE A 1 464 ? 22.966  20.362  81.282  1.00 13.43 ? 464 PHE A CZ  1 
ATOM   3928 N N   . ASP A 1 465 ? 28.166  20.097  86.482  1.00 14.17 ? 465 ASP A N   1 
ATOM   3929 C CA  . ASP A 1 465 ? 29.445  19.922  87.176  1.00 12.95 ? 465 ASP A CA  1 
ATOM   3930 C C   . ASP A 1 465 ? 29.374  18.747  88.156  1.00 13.93 ? 465 ASP A C   1 
ATOM   3931 O O   . ASP A 1 465 ? 30.308  17.936  88.227  1.00 15.02 ? 465 ASP A O   1 
ATOM   3932 C CB  . ASP A 1 465 ? 29.822  21.231  87.898  1.00 14.35 ? 465 ASP A CB  1 
ATOM   3933 C CG  . ASP A 1 465 ? 31.074  21.083  88.751  1.00 14.88 ? 465 ASP A CG  1 
ATOM   3934 O OD1 . ASP A 1 465 ? 32.218  21.074  88.193  1.00 16.37 ? 465 ASP A OD1 1 
ATOM   3935 O OD2 . ASP A 1 465 ? 30.911  20.974  89.976  1.00 16.41 ? 465 ASP A OD2 1 
ATOM   3936 N N   . LYS A 1 466 ? 28.252  18.611  88.877  1.00 12.51 ? 466 LYS A N   1 
ATOM   3937 C CA  . LYS A 1 466 ? 28.086  17.475  89.782  1.00 13.86 ? 466 LYS A CA  1 
ATOM   3938 C C   . LYS A 1 466 ? 28.101  16.153  89.015  1.00 12.31 ? 466 LYS A C   1 
ATOM   3939 O O   . LYS A 1 466 ? 28.730  15.180  89.450  1.00 16.36 ? 466 LYS A O   1 
ATOM   3940 C CB  . LYS A 1 466 ? 26.785  17.609  90.591  1.00 16.60 ? 466 LYS A CB  1 
ATOM   3941 C CG  . LYS A 1 466 ? 26.461  16.363  91.424  1.00 16.30 ? 466 LYS A CG  1 
ATOM   3942 C CD  . LYS A 1 466 ? 25.224  16.558  92.289  1.00 25.61 ? 466 LYS A CD  1 
ATOM   3943 C CE  . LYS A 1 466 ? 25.129  15.453  93.338  1.00 41.17 ? 466 LYS A CE  1 
ATOM   3944 N NZ  . LYS A 1 466 ? 24.502  15.922  94.607  1.00 52.71 ? 466 LYS A NZ  1 
ATOM   3945 N N   . LEU A 1 467 ? 27.360  16.083  87.901  1.00 12.27 ? 467 LEU A N   1 
ATOM   3946 C CA  . LEU A 1 467 ? 27.361  14.876  87.081  1.00 11.52 ? 467 LEU A CA  1 
ATOM   3947 C C   . LEU A 1 467 ? 28.763  14.538  86.579  1.00 15.20 ? 467 LEU A C   1 
ATOM   3948 O O   . LEU A 1 467 ? 29.229  13.405  86.756  1.00 13.76 ? 467 LEU A O   1 
ATOM   3949 C CB  . LEU A 1 467 ? 26.391  15.027  85.903  1.00 11.94 ? 467 LEU A CB  1 
ATOM   3950 C CG  . LEU A 1 467 ? 24.911  14.983  86.311  1.00 12.09 ? 467 LEU A CG  1 
ATOM   3951 C CD1 . LEU A 1 467 ? 24.001  15.532  85.201  1.00 13.62 ? 467 LEU A CD1 1 
ATOM   3952 C CD2 . LEU A 1 467 ? 24.467  13.547  86.709  1.00 15.62 ? 467 LEU A CD2 1 
ATOM   3953 N N   . PHE A 1 468 ? 29.436  15.491  85.913  1.00 12.80 ? 468 PHE A N   1 
ATOM   3954 C CA  . PHE A 1 468 ? 30.778  15.232  85.382  1.00 11.22 ? 468 PHE A CA  1 
ATOM   3955 C C   . PHE A 1 468 ? 31.685  14.658  86.468  1.00 13.05 ? 468 PHE A C   1 
ATOM   3956 O O   . PHE A 1 468 ? 32.298  13.599  86.300  1.00 14.18 ? 468 PHE A O   1 
ATOM   3957 C CB  . PHE A 1 468 ? 31.383  16.524  84.820  1.00 11.24 ? 468 PHE A CB  1 
ATOM   3958 C CG  . PHE A 1 468 ? 32.851  16.413  84.457  1.00 10.97 ? 468 PHE A CG  1 
ATOM   3959 C CD1 . PHE A 1 468 ? 33.264  15.701  83.331  1.00 12.14 ? 468 PHE A CD1 1 
ATOM   3960 C CD2 . PHE A 1 468 ? 33.802  17.006  85.261  1.00 12.23 ? 468 PHE A CD2 1 
ATOM   3961 C CE1 . PHE A 1 468 ? 34.636  15.622  82.984  1.00 11.99 ? 468 PHE A CE1 1 
ATOM   3962 C CE2 . PHE A 1 468 ? 35.167  16.918  84.953  1.00 15.11 ? 468 PHE A CE2 1 
ATOM   3963 C CZ  . PHE A 1 468 ? 35.571  16.214  83.802  1.00 15.30 ? 468 PHE A CZ  1 
ATOM   3964 N N   . ARG A 1 469 ? 31.738  15.325  87.620  1.00 12.17 ? 469 ARG A N   1 
ATOM   3965 C CA  . ARG A 1 469 ? 32.652  14.888  88.658  1.00 13.86 ? 469 ARG A CA  1 
ATOM   3966 C C   . ARG A 1 469 ? 32.211  13.553  89.266  1.00 13.87 ? 469 ARG A C   1 
ATOM   3967 O O   . ARG A 1 469 ? 33.059  12.775  89.721  1.00 18.08 ? 469 ARG A O   1 
ATOM   3968 C CB  . ARG A 1 469 ? 32.759  15.998  89.696  1.00 15.46 ? 469 ARG A CB  1 
ATOM   3969 C CG  . ARG A 1 469 ? 33.461  17.226  89.098  1.00 17.25 ? 469 ARG A CG  1 
ATOM   3970 C CD  . ARG A 1 469 ? 33.565  18.322  90.115  1.00 18.19 ? 469 ARG A CD  1 
ATOM   3971 N NE  . ARG A 1 469 ? 34.211  19.551  89.658  1.00 18.20 ? 469 ARG A NE  1 
ATOM   3972 C CZ  . ARG A 1 469 ? 35.512  19.788  89.789  1.00 20.16 ? 469 ARG A CZ  1 
ATOM   3973 N NH1 . ARG A 1 469 ? 36.286  18.852  90.317  1.00 17.70 ? 469 ARG A NH1 1 
ATOM   3974 N NH2 . ARG A 1 469 ? 36.049  20.960  89.436  1.00 20.34 ? 469 ARG A NH2 1 
ATOM   3975 N N   . SER A 1 470 ? 30.902  13.276  89.300  1.00 14.51 ? 470 SER A N   1 
ATOM   3976 C CA  . SER A 1 470 ? 30.469  11.973  89.798  1.00 15.52 ? 470 SER A CA  1 
ATOM   3977 C C   . SER A 1 470 ? 30.891  10.861  88.840  1.00 16.05 ? 470 SER A C   1 
ATOM   3978 O O   . SER A 1 470 ? 31.301  9.773   89.278  1.00 16.93 ? 470 SER A O   1 
ATOM   3979 C CB  . SER A 1 470 ? 28.944  11.936  89.998  1.00 20.33 ? 470 SER A CB  1 
ATOM   3980 O OG  . SER A 1 470 ? 28.518  12.884  90.958  1.00 23.34 ? 470 SER A OG  1 
ATOM   3981 N N   . PHE A 1 471 ? 30.783  11.102  87.539  1.00 13.88 ? 471 PHE A N   1 
ATOM   3982 C CA  . PHE A 1 471 ? 31.228  10.087  86.581  1.00 12.68 ? 471 PHE A CA  1 
ATOM   3983 C C   . PHE A 1 471 ? 32.737  9.870   86.684  1.00 16.48 ? 471 PHE A C   1 
ATOM   3984 O O   . PHE A 1 471 ? 33.213  8.726   86.636  1.00 16.56 ? 471 PHE A O   1 
ATOM   3985 C CB  . PHE A 1 471 ? 30.826  10.499  85.160  1.00 13.87 ? 471 PHE A CB  1 
ATOM   3986 C CG  . PHE A 1 471 ? 29.336  10.549  84.945  1.00 14.70 ? 471 PHE A CG  1 
ATOM   3987 C CD1 . PHE A 1 471 ? 28.518  9.507   85.373  1.00 14.82 ? 471 PHE A CD1 1 
ATOM   3988 C CD2 . PHE A 1 471 ? 28.741  11.643  84.316  1.00 14.29 ? 471 PHE A CD2 1 
ATOM   3989 C CE1 . PHE A 1 471 ? 27.123  9.548   85.170  1.00 15.56 ? 471 PHE A CE1 1 
ATOM   3990 C CE2 . PHE A 1 471 ? 27.337  11.691  84.125  1.00 12.06 ? 471 PHE A CE2 1 
ATOM   3991 C CZ  . PHE A 1 471 ? 26.553  10.663  84.552  1.00 13.63 ? 471 PHE A CZ  1 
ATOM   3992 N N   . VAL A 1 472 ? 33.498  10.954  86.852  1.00 14.63 ? 472 VAL A N   1 
ATOM   3993 C CA  . VAL A 1 472 ? 34.953  10.852  87.004  1.00 14.94 ? 472 VAL A CA  1 
ATOM   3994 C C   . VAL A 1 472 ? 35.300  10.017  88.232  1.00 16.16 ? 472 VAL A C   1 
ATOM   3995 O O   . VAL A 1 472 ? 36.221  9.186   88.200  1.00 19.00 ? 472 VAL A O   1 
ATOM   3996 C CB  . VAL A 1 472 ? 35.572  12.264  87.081  1.00 14.82 ? 472 VAL A CB  1 
ATOM   3997 C CG1 . VAL A 1 472 ? 36.982  12.222  87.692  1.00 20.18 ? 472 VAL A CG1 1 
ATOM   3998 C CG2 . VAL A 1 472 ? 35.561  12.937  85.692  1.00 19.24 ? 472 VAL A CG2 1 
ATOM   3999 N N   . ARG A 1 473 ? 34.569  10.233  89.337  1.00 13.87 ? 473 ARG A N   1 
ATOM   4000 C CA  . ARG A 1 473 ? 34.813  9.479   90.566  1.00 17.09 ? 473 ARG A CA  1 
ATOM   4001 C C   . ARG A 1 473 ? 34.457  8.018   90.370  1.00 20.09 ? 473 ARG A C   1 
ATOM   4002 O O   . ARG A 1 473 ? 35.220  7.117   90.754  1.00 21.54 ? 473 ARG A O   1 
ATOM   4003 C CB  . ARG A 1 473 ? 34.000  10.079  91.713  1.00 20.00 ? 473 ARG A CB  1 
ATOM   4004 C CG  . ARG A 1 473 ? 34.255  9.480   93.095  1.00 27.36 ? 473 ARG A CG  1 
ATOM   4005 C CD  . ARG A 1 473 ? 33.391  10.191  94.131  1.00 37.83 ? 473 ARG A CD  1 
ATOM   4006 N NE  . ARG A 1 473 ? 32.728  9.250   95.029  1.00 58.35 ? 473 ARG A NE  1 
ATOM   4007 C CZ  . ARG A 1 473 ? 33.260  8.789   96.159  1.00 70.91 ? 473 ARG A CZ  1 
ATOM   4008 N NH1 . ARG A 1 473 ? 34.471  9.183   96.533  1.00 75.56 ? 473 ARG A NH1 1 
ATOM   4009 N NH2 . ARG A 1 473 ? 32.581  7.935   96.917  1.00 74.26 ? 473 ARG A NH2 1 
ATOM   4010 N N   . ARG A 1 474 ? 33.290  7.764   89.773  1.00 17.79 ? 474 ARG A N   1 
ATOM   4011 C CA  . ARG A 1 474 ? 32.849  6.391   89.573  1.00 20.53 ? 474 ARG A CA  1 
ATOM   4012 C C   . ARG A 1 474 ? 33.790  5.646   88.637  1.00 17.48 ? 474 ARG A C   1 
ATOM   4013 O O   . ARG A 1 474 ? 33.994  4.436   88.794  1.00 19.56 ? 474 ARG A O   1 
ATOM   4014 C CB  . ARG A 1 474 ? 31.413  6.385   89.026  1.00 21.58 ? 474 ARG A CB  1 
ATOM   4015 C CG  . ARG A 1 474 ? 30.820  4.995   88.861  1.00 30.67 ? 474 ARG A CG  1 
ATOM   4016 C CD  . ARG A 1 474 ? 30.503  4.332   90.201  1.00 29.92 ? 474 ARG A CD  1 
ATOM   4017 N NE  . ARG A 1 474 ? 29.902  3.009   90.018  1.00 33.63 ? 474 ARG A NE  1 
ATOM   4018 C CZ  . ARG A 1 474 ? 30.581  1.919   89.659  1.00 47.99 ? 474 ARG A CZ  1 
ATOM   4019 N NH1 . ARG A 1 474 ? 31.894  1.982   89.450  1.00 45.64 ? 474 ARG A NH1 1 
ATOM   4020 N NH2 . ARG A 1 474 ? 29.950  0.759   89.515  1.00 56.08 ? 474 ARG A NH2 1 
ATOM   4021 N N   . ALA A 1 475 ? 34.401  6.358   87.690  1.00 17.63 ? 475 ALA A N   1 
ATOM   4022 C CA  . ALA A 1 475 ? 35.303  5.739   86.716  1.00 19.04 ? 475 ALA A CA  1 
ATOM   4023 C C   . ALA A 1 475 ? 36.540  5.133   87.366  1.00 23.63 ? 475 ALA A C   1 
ATOM   4024 O O   . ALA A 1 475 ? 37.160  4.219   86.794  1.00 24.94 ? 475 ALA A O   1 
ATOM   4025 C CB  . ALA A 1 475 ? 35.739  6.771   85.680  1.00 15.34 ? 475 ALA A CB  1 
ATOM   4026 N N   . GLN A 1 476 ? 36.902  5.595   88.558  1.00 20.50 ? 476 GLN A N   1 
ATOM   4027 C CA  . GLN A 1 476 ? 38.111  5.133   89.218  1.00 21.67 ? 476 GLN A CA  1 
ATOM   4028 C C   . GLN A 1 476 ? 37.829  4.077   90.287  1.00 24.25 ? 476 GLN A C   1 
ATOM   4029 O O   . GLN A 1 476 ? 38.757  3.645   90.984  1.00 28.77 ? 476 GLN A O   1 
ATOM   4030 C CB  . GLN A 1 476 ? 38.857  6.324   89.819  1.00 22.76 ? 476 GLN A CB  1 
ATOM   4031 C CG  . GLN A 1 476 ? 39.190  7.404   88.783  1.00 24.81 ? 476 GLN A CG  1 
ATOM   4032 C CD  . GLN A 1 476 ? 39.747  8.666   89.418  1.00 23.46 ? 476 GLN A CD  1 
ATOM   4033 O OE1 . GLN A 1 476 ? 40.896  8.701   89.864  1.00 25.03 ? 476 GLN A OE1 1 
ATOM   4034 N NE2 . GLN A 1 476 ? 38.940  9.710   89.449  1.00 24.41 ? 476 GLN A NE2 1 
ATOM   4035 N N   . GLU A 1 477 ? 36.577  3.645   90.418  1.00 28.73 ? 477 GLU A N   1 
ATOM   4036 C CA  . GLU A 1 477 ? 36.195  2.643   91.419  1.00 34.60 ? 477 GLU A CA  1 
ATOM   4037 C C   . GLU A 1 477 ? 35.854  1.320   90.750  1.00 38.87 ? 477 GLU A C   1 
ATOM   4038 O O   . GLU A 1 477 ? 35.110  1.300   89.765  1.00 32.29 ? 477 GLU A O   1 
ATOM   4039 C CB  . GLU A 1 477 ? 34.998  3.132   92.235  1.00 35.96 ? 477 GLU A CB  1 
ATOM   4040 C CG  . GLU A 1 477 ? 35.199  4.497   92.866  1.00 42.38 ? 477 GLU A CG  1 
ATOM   4041 C CD  . GLU A 1 477 ? 34.037  4.907   93.759  1.00 51.67 ? 477 GLU A CD  1 
ATOM   4042 O OE1 . GLU A 1 477 ? 34.255  5.734   94.670  1.00 54.84 ? 477 GLU A OE1 1 
ATOM   4043 O OE2 . GLU A 1 477 ? 32.908  4.415   93.543  1.00 52.79 ? 477 GLU A OE2 1 
ATOM   4044 N N   . LYS B 1 2   ? -6.846  -0.382  60.302  1.00 40.96 ? 2   LYS B N   1 
ATOM   4045 C CA  . LYS B 1 2   ? -7.695  0.037   59.186  1.00 37.26 ? 2   LYS B CA  1 
ATOM   4046 C C   . LYS B 1 2   ? -6.856  0.239   57.936  1.00 25.73 ? 2   LYS B C   1 
ATOM   4047 O O   . LYS B 1 2   ? -6.122  1.217   57.846  1.00 31.07 ? 2   LYS B O   1 
ATOM   4048 C CB  . LYS B 1 2   ? -8.435  1.335   59.532  1.00 43.50 ? 2   LYS B CB  1 
ATOM   4049 C CG  . LYS B 1 2   ? -9.674  1.611   58.700  1.00 47.46 ? 2   LYS B CG  1 
ATOM   4050 C CD  . LYS B 1 2   ? -9.738  3.067   58.223  1.00 51.01 ? 2   LYS B CD  1 
ATOM   4051 C CE  . LYS B 1 2   ? -9.698  4.048   59.383  1.00 51.11 ? 2   LYS B CE  1 
ATOM   4052 N NZ  . LYS B 1 2   ? -9.912  5.472   58.959  1.00 49.35 ? 2   LYS B NZ  1 
ATOM   4053 N N   . LYS B 1 3   ? -6.964  -0.662  56.966  1.00 22.77 ? 3   LYS B N   1 
ATOM   4054 C CA  . LYS B 1 3   ? -6.195  -0.553  55.732  1.00 18.49 ? 3   LYS B CA  1 
ATOM   4055 C C   . LYS B 1 3   ? -7.028  0.093   54.624  1.00 20.48 ? 3   LYS B C   1 
ATOM   4056 O O   . LYS B 1 3   ? -8.260  0.049   54.637  1.00 22.97 ? 3   LYS B O   1 
ATOM   4057 C CB  . LYS B 1 3   ? -5.719  -1.935  55.262  1.00 21.99 ? 3   LYS B CB  1 
ATOM   4058 C CG  . LYS B 1 3   ? -4.892  -2.700  56.293  1.00 28.62 ? 3   LYS B CG  1 
ATOM   4059 C CD  . LYS B 1 3   ? -3.436  -2.306  56.178  1.00 35.04 ? 3   LYS B CD  1 
ATOM   4060 C CE  . LYS B 1 3   ? -2.557  -3.144  57.083  1.00 38.07 ? 3   LYS B CE  1 
ATOM   4061 N NZ  . LYS B 1 3   ? -2.032  -2.298  58.182  1.00 48.64 ? 3   LYS B NZ  1 
ATOM   4062 N N   . LEU B 1 4   ? -6.334  0.692   53.655  1.00 17.72 ? 4   LEU B N   1 
ATOM   4063 C CA  . LEU B 1 4   ? -6.908  0.983   52.343  1.00 18.89 ? 4   LEU B CA  1 
ATOM   4064 C C   . LEU B 1 4   ? -6.485  -0.132  51.402  1.00 20.72 ? 4   LEU B C   1 
ATOM   4065 O O   . LEU B 1 4   ? -5.292  -0.441  51.307  1.00 17.65 ? 4   LEU B O   1 
ATOM   4066 C CB  . LEU B 1 4   ? -6.420  2.323   51.791  1.00 15.26 ? 4   LEU B CB  1 
ATOM   4067 C CG  . LEU B 1 4   ? -6.979  2.765   50.436  1.00 17.39 ? 4   LEU B CG  1 
ATOM   4068 C CD1 . LEU B 1 4   ? -7.248  4.277   50.476  1.00 20.16 ? 4   LEU B CD1 1 
ATOM   4069 C CD2 . LEU B 1 4   ? -5.989  2.417   49.314  1.00 18.75 ? 4   LEU B CD2 1 
ATOM   4070 N N   . PHE B 1 5   ? -7.441  -0.722  50.689  1.00 17.52 ? 5   PHE B N   1 
ATOM   4071 C CA  . PHE B 1 5   ? -7.119  -1.746  49.708  1.00 18.53 ? 5   PHE B CA  1 
ATOM   4072 C C   . PHE B 1 5   ? -7.046  -1.103  48.329  1.00 20.11 ? 5   PHE B C   1 
ATOM   4073 O O   . PHE B 1 5   ? -7.971  -0.396  47.921  1.00 19.29 ? 5   PHE B O   1 
ATOM   4074 C CB  . PHE B 1 5   ? -8.155  -2.868  49.742  1.00 14.26 ? 5   PHE B CB  1 
ATOM   4075 C CG  . PHE B 1 5   ? -8.196  -3.597  51.047  1.00 15.37 ? 5   PHE B CG  1 
ATOM   4076 C CD1 . PHE B 1 5   ? -7.039  -4.187  51.569  1.00 19.56 ? 5   PHE B CD1 1 
ATOM   4077 C CD2 . PHE B 1 5   ? -9.359  -3.640  51.798  1.00 16.65 ? 5   PHE B CD2 1 
ATOM   4078 C CE1 . PHE B 1 5   ? -7.076  -4.838  52.793  1.00 20.67 ? 5   PHE B CE1 1 
ATOM   4079 C CE2 . PHE B 1 5   ? -9.397  -4.298  53.010  1.00 21.91 ? 5   PHE B CE2 1 
ATOM   4080 C CZ  . PHE B 1 5   ? -8.255  -4.892  53.511  1.00 22.44 ? 5   PHE B CZ  1 
ATOM   4081 N N   . LEU B 1 6   ? -5.933  -1.318  47.631  1.00 14.60 ? 6   LEU B N   1 
ATOM   4082 C CA  . LEU B 1 6   ? -5.652  -0.694  46.345  1.00 14.14 ? 6   LEU B CA  1 
ATOM   4083 C C   . LEU B 1 6   ? -5.519  -1.804  45.312  1.00 16.99 ? 6   LEU B C   1 
ATOM   4084 O O   . LEU B 1 6   ? -4.824  -2.789  45.561  1.00 15.37 ? 6   LEU B O   1 
ATOM   4085 C CB  . LEU B 1 6   ? -4.364  0.131   46.426  1.00 15.06 ? 6   LEU B CB  1 
ATOM   4086 C CG  . LEU B 1 6   ? -3.910  0.929   45.203  1.00 16.05 ? 6   LEU B CG  1 
ATOM   4087 C CD1 . LEU B 1 6   ? -4.959  1.926   44.704  1.00 20.16 ? 6   LEU B CD1 1 
ATOM   4088 C CD2 . LEU B 1 6   ? -2.607  1.627   45.530  1.00 15.10 ? 6   LEU B CD2 1 
ATOM   4089 N N   . VAL B 1 7   ? -6.203  -1.665  44.179  1.00 11.01 ? 7   VAL B N   1 
ATOM   4090 C CA  . VAL B 1 7   ? -6.241  -2.724  43.162  1.00 12.19 ? 7   VAL B CA  1 
ATOM   4091 C C   . VAL B 1 7   ? -5.938  -2.083  41.821  1.00 13.41 ? 7   VAL B C   1 
ATOM   4092 O O   . VAL B 1 7   ? -6.768  -1.337  41.281  1.00 17.84 ? 7   VAL B O   1 
ATOM   4093 C CB  . VAL B 1 7   ? -7.600  -3.438  43.126  1.00 14.71 ? 7   VAL B CB  1 
ATOM   4094 C CG1 . VAL B 1 7   ? -7.511  -4.676  42.217  1.00 17.38 ? 7   VAL B CG1 1 
ATOM   4095 C CG2 . VAL B 1 7   ? -8.067  -3.827  44.551  1.00 16.35 ? 7   VAL B CG2 1 
ATOM   4096 N N   . PHE B 1 8   ? -4.751  -2.356  41.282  1.00 12.05 ? 8   PHE B N   1 
ATOM   4097 C CA  . PHE B 1 8   ? -4.397  -1.942  39.925  1.00 12.91 ? 8   PHE B CA  1 
ATOM   4098 C C   . PHE B 1 8   ? -4.849  -2.999  38.932  1.00 12.67 ? 8   PHE B C   1 
ATOM   4099 O O   . PHE B 1 8   ? -4.586  -4.184  39.124  1.00 12.93 ? 8   PHE B O   1 
ATOM   4100 C CB  . PHE B 1 8   ? -2.877  -1.750  39.782  1.00 13.27 ? 8   PHE B CB  1 
ATOM   4101 C CG  . PHE B 1 8   ? -2.356  -0.547  40.493  1.00 12.13 ? 8   PHE B CG  1 
ATOM   4102 C CD1 . PHE B 1 8   ? -2.319  0.682   39.847  1.00 12.89 ? 8   PHE B CD1 1 
ATOM   4103 C CD2 . PHE B 1 8   ? -1.873  -0.653  41.784  1.00 14.74 ? 8   PHE B CD2 1 
ATOM   4104 C CE1 . PHE B 1 8   ? -1.841  1.820   40.521  1.00 13.96 ? 8   PHE B CE1 1 
ATOM   4105 C CE2 . PHE B 1 8   ? -1.382  0.470   42.454  1.00 18.83 ? 8   PHE B CE2 1 
ATOM   4106 C CZ  . PHE B 1 8   ? -1.365  1.694   41.822  1.00 15.21 ? 8   PHE B CZ  1 
ATOM   4107 N N   . TRP B 1 9   ? -5.499  -2.577  37.851  1.00 8.80  ? 9   TRP B N   1 
ATOM   4108 C CA  . TRP B 1 9   ? -5.872  -3.526  36.800  1.00 10.97 ? 9   TRP B CA  1 
ATOM   4109 C C   . TRP B 1 9   ? -5.529  -2.886  35.460  1.00 11.84 ? 9   TRP B C   1 
ATOM   4110 O O   . TRP B 1 9   ? -6.210  -1.957  35.019  1.00 12.09 ? 9   TRP B O   1 
ATOM   4111 C CB  . TRP B 1 9   ? -7.355  -3.860  36.928  1.00 11.99 ? 9   TRP B CB  1 
ATOM   4112 C CG  . TRP B 1 9   ? -7.852  -5.085  36.156  1.00 11.63 ? 9   TRP B CG  1 
ATOM   4113 C CD1 . TRP B 1 9   ? -7.173  -5.856  35.247  1.00 14.35 ? 9   TRP B CD1 1 
ATOM   4114 C CD2 . TRP B 1 9   ? -9.172  -5.615  36.230  1.00 11.25 ? 9   TRP B CD2 1 
ATOM   4115 N NE1 . TRP B 1 9   ? -8.009  -6.862  34.765  1.00 14.66 ? 9   TRP B NE1 1 
ATOM   4116 C CE2 . TRP B 1 9   ? -9.243  -6.720  35.351  1.00 12.62 ? 9   TRP B CE2 1 
ATOM   4117 C CE3 . TRP B 1 9   ? -10.311 -5.264  36.973  1.00 14.02 ? 9   TRP B CE3 1 
ATOM   4118 C CZ2 . TRP B 1 9   ? -10.410 -7.470  35.182  1.00 13.29 ? 9   TRP B CZ2 1 
ATOM   4119 C CZ3 . TRP B 1 9   ? -11.464 -6.009  36.814  1.00 17.39 ? 9   TRP B CZ3 1 
ATOM   4120 C CH2 . TRP B 1 9   ? -11.504 -7.110  35.919  1.00 14.50 ? 9   TRP B CH2 1 
ATOM   4121 N N   . TRP B 1 10  ? -4.418  -3.328  34.872  1.00 12.11 ? 10  TRP B N   1 
ATOM   4122 C CA  . TRP B 1 10  ? -3.861  -2.749  33.662  1.00 9.61  ? 10  TRP B CA  1 
ATOM   4123 C C   . TRP B 1 10  ? -4.366  -3.533  32.460  1.00 10.01 ? 10  TRP B C   1 
ATOM   4124 O O   . TRP B 1 10  ? -4.066  -4.732  32.333  1.00 13.43 ? 10  TRP B O   1 
ATOM   4125 C CB  . TRP B 1 10  ? -2.333  -2.838  33.696  1.00 11.92 ? 10  TRP B CB  1 
ATOM   4126 C CG  . TRP B 1 10  ? -1.645  -2.105  34.832  1.00 8.94  ? 10  TRP B CG  1 
ATOM   4127 C CD1 . TRP B 1 10  ? -0.917  -2.675  35.866  1.00 10.09 ? 10  TRP B CD1 1 
ATOM   4128 C CD2 . TRP B 1 10  ? -1.548  -0.680  35.026  1.00 10.79 ? 10  TRP B CD2 1 
ATOM   4129 N NE1 . TRP B 1 10  ? -0.404  -1.690  36.695  1.00 13.92 ? 10  TRP B NE1 1 
ATOM   4130 C CE2 . TRP B 1 10  ? -0.755  -0.473  36.182  1.00 10.53 ? 10  TRP B CE2 1 
ATOM   4131 C CE3 . TRP B 1 10  ? -2.010  0.433   34.317  1.00 10.86 ? 10  TRP B CE3 1 
ATOM   4132 C CZ2 . TRP B 1 10  ? -0.465  0.799   36.665  1.00 9.67  ? 10  TRP B CZ2 1 
ATOM   4133 C CZ3 . TRP B 1 10  ? -1.709  1.707   34.805  1.00 10.36 ? 10  TRP B CZ3 1 
ATOM   4134 C CH2 . TRP B 1 10  ? -0.943  1.871   35.969  1.00 11.94 ? 10  TRP B CH2 1 
ATOM   4135 N N   . HIS B 1 11  ? -5.058  -2.866  31.544  1.00 11.01 ? 11  HIS B N   1 
ATOM   4136 C CA  . HIS B 1 11  ? -5.724  -3.521  30.419  1.00 11.21 ? 11  HIS B CA  1 
ATOM   4137 C C   . HIS B 1 11  ? -4.877  -3.416  29.151  1.00 10.34 ? 11  HIS B C   1 
ATOM   4138 O O   . HIS B 1 11  ? -4.569  -2.312  28.693  1.00 11.36 ? 11  HIS B O   1 
ATOM   4139 C CB  . HIS B 1 11  ? -7.094  -2.875  30.214  1.00 11.56 ? 11  HIS B CB  1 
ATOM   4140 C CG  . HIS B 1 11  ? -7.648  -3.072  28.840  1.00 12.54 ? 11  HIS B CG  1 
ATOM   4141 N ND1 . HIS B 1 11  ? -7.958  -4.319  28.342  1.00 11.53 ? 11  HIS B ND1 1 
ATOM   4142 C CD2 . HIS B 1 11  ? -7.892  -2.195  27.841  1.00 11.28 ? 11  HIS B CD2 1 
ATOM   4143 C CE1 . HIS B 1 11  ? -8.442  -4.192  27.119  1.00 14.28 ? 11  HIS B CE1 1 
ATOM   4144 N NE2 . HIS B 1 11  ? -8.376  -2.920  26.776  1.00 14.45 ? 11  HIS B NE2 1 
ATOM   4145 N N   . MET B 1 12  ? -4.547  -4.561  28.564  1.00 10.05 ? 12  MET B N   1 
ATOM   4146 C CA  . MET B 1 12  ? -3.674  -4.644  27.401  1.00 11.40 ? 12  MET B CA  1 
ATOM   4147 C C   . MET B 1 12  ? -4.454  -5.153  26.197  1.00 13.15 ? 12  MET B C   1 
ATOM   4148 O O   . MET B 1 12  ? -5.091  -6.216  26.272  1.00 13.08 ? 12  MET B O   1 
ATOM   4149 C CB  . MET B 1 12  ? -2.506  -5.590  27.669  1.00 11.54 ? 12  MET B CB  1 
ATOM   4150 C CG  . MET B 1 12  ? -1.728  -5.382  28.974  1.00 11.82 ? 12  MET B CG  1 
ATOM   4151 S SD  . MET B 1 12  ? -1.065  -3.701  29.015  1.00 12.45 ? 12  MET B SD  1 
ATOM   4152 C CE  . MET B 1 12  ? 0.097   -3.924  30.402  1.00 13.47 ? 12  MET B CE  1 
ATOM   4153 N N   . HIS B 1 13  ? -4.372  -4.430  25.079  1.00 9.16  ? 13  HIS B N   1 
ATOM   4154 C CA  . HIS B 1 13  ? -5.138  -4.853  23.906  1.00 9.82  ? 13  HIS B CA  1 
ATOM   4155 C C   . HIS B 1 13  ? -4.535  -4.269  22.636  1.00 12.91 ? 13  HIS B C   1 
ATOM   4156 O O   . HIS B 1 13  ? -4.008  -3.156  22.647  1.00 13.09 ? 13  HIS B O   1 
ATOM   4157 C CB  . HIS B 1 13  ? -6.602  -4.415  24.038  1.00 9.28  ? 13  HIS B CB  1 
ATOM   4158 C CG  . HIS B 1 13  ? -7.385  -4.507  22.767  1.00 12.63 ? 13  HIS B CG  1 
ATOM   4159 N ND1 . HIS B 1 13  ? -7.621  -5.705  22.123  1.00 13.33 ? 13  HIS B ND1 1 
ATOM   4160 C CD2 . HIS B 1 13  ? -8.014  -3.553  22.030  1.00 12.63 ? 13  HIS B CD2 1 
ATOM   4161 C CE1 . HIS B 1 13  ? -8.352  -5.485  21.045  1.00 14.78 ? 13  HIS B CE1 1 
ATOM   4162 N NE2 . HIS B 1 13  ? -8.593  -4.187  20.957  1.00 13.72 ? 13  HIS B NE2 1 
ATOM   4163 N N   . GLN B 1 14  ? -4.610  -5.040  21.546  1.00 13.23 ? 14  GLN B N   1 
ATOM   4164 C CA  . GLN B 1 14  ? -4.434  -4.499  20.190  1.00 12.49 ? 14  GLN B CA  1 
ATOM   4165 C C   . GLN B 1 14  ? -5.433  -5.196  19.283  1.00 12.76 ? 14  GLN B C   1 
ATOM   4166 O O   . GLN B 1 14  ? -5.599  -6.425  19.375  1.00 16.57 ? 14  GLN B O   1 
ATOM   4167 C CB  . GLN B 1 14  ? -3.027  -4.703  19.598  1.00 11.26 ? 14  GLN B CB  1 
ATOM   4168 C CG  . GLN B 1 14  ? -1.920  -4.028  20.373  1.00 13.94 ? 14  GLN B CG  1 
ATOM   4169 C CD  . GLN B 1 14  ? -1.937  -2.519  20.262  1.00 13.54 ? 14  GLN B CD  1 
ATOM   4170 O OE1 . GLN B 1 14  ? -2.478  -1.939  19.308  1.00 14.73 ? 14  GLN B OE1 1 
ATOM   4171 N NE2 . GLN B 1 14  ? -1.280  -1.864  21.220  1.00 14.15 ? 14  GLN B NE2 1 
ATOM   4172 N N   . PRO B 1 15  ? -6.078  -4.461  18.375  1.00 14.03 ? 15  PRO B N   1 
ATOM   4173 C CA  . PRO B 1 15  ? -6.883  -5.112  17.338  1.00 13.84 ? 15  PRO B CA  1 
ATOM   4174 C C   . PRO B 1 15  ? -5.976  -5.840  16.356  1.00 13.00 ? 15  PRO B C   1 
ATOM   4175 O O   . PRO B 1 15  ? -4.757  -5.631  16.321  1.00 15.92 ? 15  PRO B O   1 
ATOM   4176 C CB  . PRO B 1 15  ? -7.600  -3.943  16.662  1.00 15.85 ? 15  PRO B CB  1 
ATOM   4177 C CG  . PRO B 1 15  ? -6.589  -2.827  16.765  1.00 15.53 ? 15  PRO B CG  1 
ATOM   4178 C CD  . PRO B 1 15  ? -5.953  -3.009  18.142  1.00 15.19 ? 15  PRO B CD  1 
ATOM   4179 N N   . LEU B 1 16  ? -6.586  -6.684  15.529  1.00 15.57 ? 16  LEU B N   1 
ATOM   4180 C CA  . LEU B 1 16  ? -5.795  -7.535  14.640  1.00 17.69 ? 16  LEU B CA  1 
ATOM   4181 C C   . LEU B 1 16  ? -5.256  -6.720  13.469  1.00 18.62 ? 16  LEU B C   1 
ATOM   4182 O O   . LEU B 1 16  ? -6.019  -6.242  12.627  1.00 17.27 ? 16  LEU B O   1 
ATOM   4183 C CB  . LEU B 1 16  ? -6.634  -8.707  14.150  1.00 16.66 ? 16  LEU B CB  1 
ATOM   4184 C CG  . LEU B 1 16  ? -5.917  -9.777  13.320  1.00 17.89 ? 16  LEU B CG  1 
ATOM   4185 C CD1 . LEU B 1 16  ? -4.755  -10.382 14.125  1.00 21.05 ? 16  LEU B CD1 1 
ATOM   4186 C CD2 . LEU B 1 16  ? -6.905  -10.861 12.909  1.00 21.90 ? 16  LEU B CD2 1 
ATOM   4187 N N   . TYR B 1 17  ? -3.936  -6.596  13.381  1.00 16.66 ? 17  TYR B N   1 
ATOM   4188 C CA  . TYR B 1 17  ? -3.314  -5.849  12.298  1.00 15.98 ? 17  TYR B CA  1 
ATOM   4189 C C   . TYR B 1 17  ? -2.939  -6.725  11.113  1.00 17.72 ? 17  TYR B C   1 
ATOM   4190 O O   . TYR B 1 17  ? -2.455  -6.202  10.099  1.00 18.93 ? 17  TYR B O   1 
ATOM   4191 C CB  . TYR B 1 17  ? -2.044  -5.122  12.797  1.00 14.40 ? 17  TYR B CB  1 
ATOM   4192 C CG  . TYR B 1 17  ? -2.319  -4.083  13.884  1.00 13.46 ? 17  TYR B CG  1 
ATOM   4193 C CD1 . TYR B 1 17  ? -3.116  -2.973  13.617  1.00 14.80 ? 17  TYR B CD1 1 
ATOM   4194 C CD2 . TYR B 1 17  ? -1.763  -4.206  15.159  1.00 12.55 ? 17  TYR B CD2 1 
ATOM   4195 C CE1 . TYR B 1 17  ? -3.380  -2.027  14.587  1.00 13.68 ? 17  TYR B CE1 1 
ATOM   4196 C CE2 . TYR B 1 17  ? -2.017  -3.256  16.167  1.00 14.02 ? 17  TYR B CE2 1 
ATOM   4197 C CZ  . TYR B 1 17  ? -2.814  -2.166  15.858  1.00 13.98 ? 17  TYR B CZ  1 
ATOM   4198 O OH  . TYR B 1 17  ? -3.100  -1.187  16.799  1.00 18.07 ? 17  TYR B OH  1 
ATOM   4199 N N   . ARG B 1 18  ? -3.172  -8.038  11.211  1.00 17.93 ? 18  ARG B N   1 
ATOM   4200 C CA  . ARG B 1 18  ? -2.812  -9.000  10.179  1.00 19.47 ? 18  ARG B CA  1 
ATOM   4201 C C   . ARG B 1 18  ? -3.867  -8.987  9.069   1.00 20.74 ? 18  ARG B C   1 
ATOM   4202 O O   . ARG B 1 18  ? -4.983  -9.483  9.252   1.00 20.58 ? 18  ARG B O   1 
ATOM   4203 C CB  . ARG B 1 18  ? -2.685  -10.393 10.794  1.00 19.89 ? 18  ARG B CB  1 
ATOM   4204 C CG  . ARG B 1 18  ? -2.009  -11.423 9.900   1.00 22.19 ? 18  ARG B CG  1 
ATOM   4205 C CD  . ARG B 1 18  ? -2.011  -12.790 10.589  1.00 26.02 ? 18  ARG B CD  1 
ATOM   4206 N NE  . ARG B 1 18  ? -1.422  -13.823 9.740   1.00 28.83 ? 18  ARG B NE  1 
ATOM   4207 C CZ  . ARG B 1 18  ? -2.030  -14.392 8.702   1.00 35.85 ? 18  ARG B CZ  1 
ATOM   4208 N NH1 . ARG B 1 18  ? -3.272  -14.050 8.375   1.00 33.72 ? 18  ARG B NH1 1 
ATOM   4209 N NH2 . ARG B 1 18  ? -1.397  -15.315 7.986   1.00 42.38 ? 18  ARG B NH2 1 
ATOM   4210 N N   . GLU B 1 19  ? -3.502  -8.428  7.920   1.00 20.27 ? 19  GLU B N   1 
ATOM   4211 C CA  . GLU B 1 19  ? -4.374  -8.441  6.747   1.00 19.30 ? 19  GLU B CA  1 
ATOM   4212 C C   . GLU B 1 19  ? -4.648  -9.885  6.329   1.00 20.41 ? 19  GLU B C   1 
ATOM   4213 O O   . GLU B 1 19  ? -3.703  -10.667 6.160   1.00 23.27 ? 19  GLU B O   1 
ATOM   4214 C CB  . GLU B 1 19  ? -3.701  -7.667  5.617   1.00 25.47 ? 19  GLU B CB  1 
ATOM   4215 C CG  . GLU B 1 19  ? -4.667  -6.932  4.711   1.00 31.48 ? 19  GLU B CG  1 
ATOM   4216 C CD  . GLU B 1 19  ? -5.187  -7.801  3.594   1.00 36.95 ? 19  GLU B CD  1 
ATOM   4217 O OE1 . GLU B 1 19  ? -4.537  -8.823  3.259   1.00 31.92 ? 19  GLU B OE1 1 
ATOM   4218 O OE2 . GLU B 1 19  ? -6.257  -7.458  3.060   1.00 40.49 ? 19  GLU B OE2 1 
ATOM   4219 N N   . PRO B 1 20  ? -5.910  -10.272 6.124   1.00 24.57 ? 20  PRO B N   1 
ATOM   4220 C CA  . PRO B 1 20  ? -6.219  -11.704 6.001   1.00 29.73 ? 20  PRO B CA  1 
ATOM   4221 C C   . PRO B 1 20  ? -5.805  -12.313 4.679   1.00 32.99 ? 20  PRO B C   1 
ATOM   4222 O O   . PRO B 1 20  ? -5.618  -13.535 4.614   1.00 38.67 ? 20  PRO B O   1 
ATOM   4223 C CB  . PRO B 1 20  ? -7.746  -11.755 6.177   1.00 30.61 ? 20  PRO B CB  1 
ATOM   4224 C CG  . PRO B 1 20  ? -8.221  -10.383 5.829   1.00 28.37 ? 20  PRO B CG  1 
ATOM   4225 C CD  . PRO B 1 20  ? -7.126  -9.451  6.271   1.00 26.39 ? 20  PRO B CD  1 
ATOM   4226 N N   . TYR B 1 21  ? -5.642  -11.517 3.627   1.00 25.50 ? 21  TYR B N   1 
ATOM   4227 C CA  . TYR B 1 21  ? -5.300  -12.101 2.340   1.00 28.46 ? 21  TYR B CA  1 
ATOM   4228 C C   . TYR B 1 21  ? -3.796  -12.222 2.169   1.00 34.04 ? 21  TYR B C   1 
ATOM   4229 O O   . TYR B 1 21  ? -3.312  -13.251 1.685   1.00 37.93 ? 21  TYR B O   1 
ATOM   4230 C CB  . TYR B 1 21  ? -5.910  -11.280 1.200   1.00 28.38 ? 21  TYR B CB  1 
ATOM   4231 C CG  . TYR B 1 21  ? -7.422  -11.327 1.207   1.00 31.89 ? 21  TYR B CG  1 
ATOM   4232 C CD1 . TYR B 1 21  ? -8.104  -12.313 0.505   1.00 33.34 ? 21  TYR B CD1 1 
ATOM   4233 C CD2 . TYR B 1 21  ? -8.169  -10.408 1.947   1.00 34.82 ? 21  TYR B CD2 1 
ATOM   4234 C CE1 . TYR B 1 21  ? -9.478  -12.374 0.508   1.00 34.06 ? 21  TYR B CE1 1 
ATOM   4235 C CE2 . TYR B 1 21  ? -9.571  -10.469 1.966   1.00 31.50 ? 21  TYR B CE2 1 
ATOM   4236 C CZ  . TYR B 1 21  ? -10.208 -11.455 1.239   1.00 37.52 ? 21  TYR B CZ  1 
ATOM   4237 O OH  . TYR B 1 21  ? -11.582 -11.528 1.233   1.00 39.99 ? 21  TYR B OH  1 
ATOM   4238 N N   . THR B 1 22  ? -3.048  -11.208 2.606   1.00 25.58 ? 22  THR B N   1 
ATOM   4239 C CA  . THR B 1 22  ? -1.599  -11.217 2.446   1.00 29.77 ? 22  THR B CA  1 
ATOM   4240 C C   . THR B 1 22  ? -0.859  -11.734 3.668   1.00 31.12 ? 22  THR B C   1 
ATOM   4241 O O   . THR B 1 22  ? 0.317   -12.090 3.547   1.00 30.82 ? 22  THR B O   1 
ATOM   4242 C CB  . THR B 1 22  ? -1.091  -9.809  2.130   1.00 28.00 ? 22  THR B CB  1 
ATOM   4243 O OG1 . THR B 1 22  ? -1.374  -8.945  3.241   1.00 25.65 ? 22  THR B OG1 1 
ATOM   4244 C CG2 . THR B 1 22  ? -1.746  -9.271  0.840   1.00 29.67 ? 22  THR B CG2 1 
ATOM   4245 N N   . GLY B 1 23  ? -1.515  -11.781 4.829   1.00 27.35 ? 23  GLY B N   1 
ATOM   4246 C CA  . GLY B 1 23  ? -0.864  -12.125 6.074   1.00 26.97 ? 23  GLY B CA  1 
ATOM   4247 C C   . GLY B 1 23  ? 0.061   -11.063 6.601   1.00 28.47 ? 23  GLY B C   1 
ATOM   4248 O O   . GLY B 1 23  ? 0.781   -11.317 7.574   1.00 30.80 ? 23  GLY B O   1 
ATOM   4249 N N   . GLU B 1 24  ? 0.056   -9.870  6.010   1.00 23.34 ? 24  GLU B N   1 
ATOM   4250 C CA  . GLU B 1 24  ? 0.943   -8.797  6.450   1.00 22.90 ? 24  GLU B CA  1 
ATOM   4251 C C   . GLU B 1 24  ? 0.364   -8.015  7.624   1.00 21.80 ? 24  GLU B C   1 
ATOM   4252 O O   . GLU B 1 24  ? -0.816  -7.652  7.623   1.00 21.68 ? 24  GLU B O   1 
ATOM   4253 C CB  . GLU B 1 24  ? 1.226   -7.865  5.279   1.00 22.52 ? 24  GLU B CB  1 
ATOM   4254 C CG  . GLU B 1 24  ? 2.107   -8.582  4.226   1.00 24.49 ? 24  GLU B CG  1 
ATOM   4255 C CD  . GLU B 1 24  ? 2.431   -7.750  3.008   1.00 39.45 ? 24  GLU B CD  1 
ATOM   4256 O OE1 . GLU B 1 24  ? 1.898   -6.630  2.872   1.00 42.90 ? 24  GLU B OE1 1 
ATOM   4257 O OE2 . GLU B 1 24  ? 3.228   -8.231  2.174   1.00 47.26 ? 24  GLU B OE2 1 
ATOM   4258 N N   . TYR B 1 25  ? 1.204   -7.754  8.633   1.00 19.71 ? 25  TYR B N   1 
ATOM   4259 C CA  . TYR B 1 25  ? 0.850   -6.836  9.713   1.00 17.42 ? 25  TYR B CA  1 
ATOM   4260 C C   . TYR B 1 25  ? 1.033   -5.409  9.202   1.00 21.05 ? 25  TYR B C   1 
ATOM   4261 O O   . TYR B 1 25  ? 2.166   -4.968  8.937   1.00 19.80 ? 25  TYR B O   1 
ATOM   4262 C CB  . TYR B 1 25  ? 1.702   -7.091  10.957  1.00 21.41 ? 25  TYR B CB  1 
ATOM   4263 C CG  . TYR B 1 25  ? 1.195   -8.233  11.796  1.00 19.70 ? 25  TYR B CG  1 
ATOM   4264 C CD1 . TYR B 1 25  ? 1.302   -9.551  11.352  1.00 22.81 ? 25  TYR B CD1 1 
ATOM   4265 C CD2 . TYR B 1 25  ? 0.571   -7.999  13.008  1.00 17.98 ? 25  TYR B CD2 1 
ATOM   4266 C CE1 . TYR B 1 25  ? 0.817   -10.604 12.110  1.00 22.74 ? 25  TYR B CE1 1 
ATOM   4267 C CE2 . TYR B 1 25  ? 0.094   -9.047  13.773  1.00 16.69 ? 25  TYR B CE2 1 
ATOM   4268 C CZ  . TYR B 1 25  ? 0.221   -10.340 13.321  1.00 20.99 ? 25  TYR B CZ  1 
ATOM   4269 O OH  . TYR B 1 25  ? -0.284  -11.371 14.097  1.00 24.23 ? 25  TYR B OH  1 
ATOM   4270 N N   . LEU B 1 26  ? -0.081  -4.695  9.047   1.00 19.50 ? 26  LEU B N   1 
ATOM   4271 C CA  . LEU B 1 26  ? -0.060  -3.431  8.332   1.00 19.01 ? 26  LEU B CA  1 
ATOM   4272 C C   . LEU B 1 26  ? 0.317   -2.251  9.211   1.00 22.38 ? 26  LEU B C   1 
ATOM   4273 O O   . LEU B 1 26  ? 0.695   -1.208  8.670   1.00 21.39 ? 26  LEU B O   1 
ATOM   4274 C CB  . LEU B 1 26  ? -1.418  -3.185  7.670   1.00 18.14 ? 26  LEU B CB  1 
ATOM   4275 C CG  . LEU B 1 26  ? -1.805  -4.201  6.600   1.00 21.35 ? 26  LEU B CG  1 
ATOM   4276 C CD1 . LEU B 1 26  ? -3.145  -3.820  5.959   1.00 22.11 ? 26  LEU B CD1 1 
ATOM   4277 C CD2 . LEU B 1 26  ? -0.721  -4.269  5.532   1.00 22.22 ? 26  LEU B CD2 1 
ATOM   4278 N N   . LEU B 1 27  ? 0.223   -2.386  10.534  1.00 18.61 ? 27  LEU B N   1 
ATOM   4279 C CA  . LEU B 1 27  ? 0.794   -1.419  11.453  1.00 17.75 ? 27  LEU B CA  1 
ATOM   4280 C C   . LEU B 1 27  ? 1.644   -2.154  12.474  1.00 17.56 ? 27  LEU B C   1 
ATOM   4281 O O   . LEU B 1 27  ? 1.419   -3.347  12.720  1.00 18.16 ? 27  LEU B O   1 
ATOM   4282 C CB  . LEU B 1 27  ? -0.298  -0.600  12.159  1.00 19.40 ? 27  LEU B CB  1 
ATOM   4283 C CG  . LEU B 1 27  ? -1.060  0.351   11.224  1.00 19.64 ? 27  LEU B CG  1 
ATOM   4284 C CD1 . LEU B 1 27  ? -2.384  0.705   11.873  1.00 18.95 ? 27  LEU B CD1 1 
ATOM   4285 C CD2 . LEU B 1 27  ? -0.244  1.598   10.927  1.00 27.97 ? 27  LEU B CD2 1 
ATOM   4286 N N   . PRO B 1 28  ? 2.673   -1.470  13.062  1.00 19.55 ? 28  PRO B N   1 
ATOM   4287 C CA  . PRO B 1 28  ? 3.625   -2.147  13.950  1.00 18.79 ? 28  PRO B CA  1 
ATOM   4288 C C   . PRO B 1 28  ? 3.288   -1.991  15.426  1.00 17.80 ? 28  PRO B C   1 
ATOM   4289 O O   . PRO B 1 28  ? 4.158   -2.204  16.273  1.00 16.27 ? 28  PRO B O   1 
ATOM   4290 C CB  . PRO B 1 28  ? 4.944   -1.443  13.630  1.00 19.69 ? 28  PRO B CB  1 
ATOM   4291 C CG  . PRO B 1 28  ? 4.493   -0.004  13.503  1.00 19.43 ? 28  PRO B CG  1 
ATOM   4292 C CD  . PRO B 1 28  ? 3.147   -0.111  12.737  1.00 20.03 ? 28  PRO B CD  1 
ATOM   4293 N N   . TRP B 1 29  ? 2.072   -1.541  15.746  1.00 14.93 ? 29  TRP B N   1 
ATOM   4294 C CA  . TRP B 1 29  ? 1.780   -1.146  17.129  1.00 18.24 ? 29  TRP B CA  1 
ATOM   4295 C C   . TRP B 1 29  ? 1.832   -2.320  18.103  1.00 17.55 ? 29  TRP B C   1 
ATOM   4296 O O   . TRP B 1 29  ? 2.211   -2.130  19.267  1.00 14.68 ? 29  TRP B O   1 
ATOM   4297 C CB  . TRP B 1 29  ? 0.413   -0.468  17.207  1.00 17.11 ? 29  TRP B CB  1 
ATOM   4298 C CG  . TRP B 1 29  ? 0.262   0.800   16.402  1.00 18.26 ? 29  TRP B CG  1 
ATOM   4299 C CD1 . TRP B 1 29  ? -0.713  1.069   15.482  1.00 16.80 ? 29  TRP B CD1 1 
ATOM   4300 C CD2 . TRP B 1 29  ? 1.056   1.990   16.499  1.00 16.46 ? 29  TRP B CD2 1 
ATOM   4301 N NE1 . TRP B 1 29  ? -0.562  2.351   14.984  1.00 19.83 ? 29  TRP B NE1 1 
ATOM   4302 C CE2 . TRP B 1 29  ? 0.506   2.939   15.606  1.00 18.32 ? 29  TRP B CE2 1 
ATOM   4303 C CE3 . TRP B 1 29  ? 2.151   2.361   17.283  1.00 20.43 ? 29  TRP B CE3 1 
ATOM   4304 C CZ2 . TRP B 1 29  ? 1.035   4.220   15.452  1.00 21.11 ? 29  TRP B CZ2 1 
ATOM   4305 C CZ3 . TRP B 1 29  ? 2.679   3.639   17.129  1.00 18.75 ? 29  TRP B CZ3 1 
ATOM   4306 C CH2 . TRP B 1 29  ? 2.121   4.551   16.227  1.00 22.68 ? 29  TRP B CH2 1 
ATOM   4307 N N   . THR B 1 30  ? 1.488   -3.538  17.667  1.00 13.96 ? 30  THR B N   1 
ATOM   4308 C CA  . THR B 1 30  ? 1.643   -4.669  18.583  1.00 12.42 ? 30  THR B CA  1 
ATOM   4309 C C   . THR B 1 30  ? 3.111   -4.915  18.885  1.00 12.96 ? 30  THR B C   1 
ATOM   4310 O O   . THR B 1 30  ? 3.480   -5.181  20.039  1.00 13.26 ? 30  THR B O   1 
ATOM   4311 C CB  . THR B 1 30  ? 1.025   -5.940  17.998  1.00 16.10 ? 30  THR B CB  1 
ATOM   4312 O OG1 . THR B 1 30  ? -0.376  -5.732  17.775  1.00 16.39 ? 30  THR B OG1 1 
ATOM   4313 C CG2 . THR B 1 30  ? 1.244   -7.147  18.960  1.00 15.03 ? 30  THR B CG2 1 
ATOM   4314 N N   . PHE B 1 31  ? 3.957   -4.887  17.847  1.00 14.18 ? 31  PHE B N   1 
ATOM   4315 C CA  . PHE B 1 31  ? 5.388   -5.048  18.064  1.00 14.93 ? 31  PHE B CA  1 
ATOM   4316 C C   . PHE B 1 31  ? 5.922   -3.986  19.025  1.00 13.50 ? 31  PHE B C   1 
ATOM   4317 O O   . PHE B 1 31  ? 6.604   -4.304  20.009  1.00 14.61 ? 31  PHE B O   1 
ATOM   4318 C CB  . PHE B 1 31  ? 6.128   -4.981  16.732  1.00 14.23 ? 31  PHE B CB  1 
ATOM   4319 C CG  . PHE B 1 31  ? 7.621   -5.013  16.886  1.00 16.47 ? 31  PHE B CG  1 
ATOM   4320 C CD1 . PHE B 1 31  ? 8.272   -6.219  17.061  1.00 17.23 ? 31  PHE B CD1 1 
ATOM   4321 C CD2 . PHE B 1 31  ? 8.367   -3.836  16.908  1.00 16.94 ? 31  PHE B CD2 1 
ATOM   4322 C CE1 . PHE B 1 31  ? 9.668   -6.264  17.196  1.00 18.31 ? 31  PHE B CE1 1 
ATOM   4323 C CE2 . PHE B 1 31  ? 9.750   -3.874  17.059  1.00 20.20 ? 31  PHE B CE2 1 
ATOM   4324 C CZ  . PHE B 1 31  ? 10.385  -5.087  17.212  1.00 18.78 ? 31  PHE B CZ  1 
ATOM   4325 N N   . PHE B 1 32  ? 5.614   -2.716  18.758  1.00 12.79 ? 32  PHE B N   1 
ATOM   4326 C CA  . PHE B 1 32  ? 6.201   -1.655  19.578  1.00 14.02 ? 32  PHE B CA  1 
ATOM   4327 C C   . PHE B 1 32  ? 5.671   -1.674  21.013  1.00 13.10 ? 32  PHE B C   1 
ATOM   4328 O O   . PHE B 1 32  ? 6.435   -1.436  21.958  1.00 13.44 ? 32  PHE B O   1 
ATOM   4329 C CB  . PHE B 1 32  ? 5.975   -0.287  18.941  1.00 13.79 ? 32  PHE B CB  1 
ATOM   4330 C CG  . PHE B 1 32  ? 6.922   0.011   17.782  1.00 13.89 ? 32  PHE B CG  1 
ATOM   4331 C CD1 . PHE B 1 32  ? 8.295   -0.177  17.902  1.00 15.47 ? 32  PHE B CD1 1 
ATOM   4332 C CD2 . PHE B 1 32  ? 6.432   0.475   16.579  1.00 19.13 ? 32  PHE B CD2 1 
ATOM   4333 C CE1 . PHE B 1 32  ? 9.161   0.091   16.819  1.00 20.50 ? 32  PHE B CE1 1 
ATOM   4334 C CE2 . PHE B 1 32  ? 7.287   0.744   15.498  1.00 19.97 ? 32  PHE B CE2 1 
ATOM   4335 C CZ  . PHE B 1 32  ? 8.637   0.562   15.619  1.00 19.49 ? 32  PHE B CZ  1 
ATOM   4336 N N   . HIS B 1 33  ? 4.379   -1.955  21.214  1.00 12.62 ? 33  HIS B N   1 
ATOM   4337 C CA  . HIS B 1 33  ? 3.930   -2.035  22.602  1.00 10.23 ? 33  HIS B CA  1 
ATOM   4338 C C   . HIS B 1 33  ? 4.336   -3.333  23.289  1.00 14.47 ? 33  HIS B C   1 
ATOM   4339 O O   . HIS B 1 33  ? 4.476   -3.349  24.520  1.00 13.95 ? 33  HIS B O   1 
ATOM   4340 C CB  . HIS B 1 33  ? 2.421   -1.819  22.696  1.00 11.20 ? 33  HIS B CB  1 
ATOM   4341 C CG  . HIS B 1 33  ? 2.025   -0.387  22.498  1.00 13.02 ? 33  HIS B CG  1 
ATOM   4342 N ND1 . HIS B 1 33  ? 2.323   0.599   23.413  1.00 14.14 ? 33  HIS B ND1 1 
ATOM   4343 C CD2 . HIS B 1 33  ? 1.364   0.222   21.483  1.00 14.85 ? 33  HIS B CD2 1 
ATOM   4344 C CE1 . HIS B 1 33  ? 1.868   1.758   22.970  1.00 12.53 ? 33  HIS B CE1 1 
ATOM   4345 N NE2 . HIS B 1 33  ? 1.271   1.556   21.806  1.00 11.53 ? 33  HIS B NE2 1 
ATOM   4346 N N   . ALA B 1 34  ? 4.605   -4.397  22.534  1.00 13.66 ? 34  ALA B N   1 
ATOM   4347 C CA  . ALA B 1 34  ? 5.188   -5.579  23.165  1.00 14.35 ? 34  ALA B CA  1 
ATOM   4348 C C   . ALA B 1 34  ? 6.584   -5.280  23.701  1.00 16.31 ? 34  ALA B C   1 
ATOM   4349 O O   . ALA B 1 34  ? 6.904   -5.626  24.847  1.00 16.68 ? 34  ALA B O   1 
ATOM   4350 C CB  . ALA B 1 34  ? 5.227   -6.748  22.177  1.00 16.90 ? 34  ALA B CB  1 
ATOM   4351 N N   . VAL B 1 35  ? 7.434   -4.630  22.895  1.00 14.30 ? 35  VAL B N   1 
ATOM   4352 C CA  . VAL B 1 35  ? 8.810   -4.438  23.347  1.00 11.31 ? 35  VAL B CA  1 
ATOM   4353 C C   . VAL B 1 35  ? 8.875   -3.373  24.427  1.00 15.23 ? 35  VAL B C   1 
ATOM   4354 O O   . VAL B 1 35  ? 9.794   -3.390  25.260  1.00 16.32 ? 35  VAL B O   1 
ATOM   4355 C CB  . VAL B 1 35  ? 9.764   -4.098  22.176  1.00 17.33 ? 35  VAL B CB  1 
ATOM   4356 C CG1 . VAL B 1 35  ? 9.692   -5.151  21.075  1.00 15.24 ? 35  VAL B CG1 1 
ATOM   4357 C CG2 . VAL B 1 35  ? 9.461   -2.718  21.598  1.00 17.78 ? 35  VAL B CG2 1 
ATOM   4358 N N   . LYS B 1 36  ? 7.920   -2.433  24.430  1.00 16.52 ? 36  LYS B N   1 
ATOM   4359 C CA  . LYS B 1 36  ? 7.968   -1.316  25.366  1.00 14.33 ? 36  LYS B CA  1 
ATOM   4360 C C   . LYS B 1 36  ? 7.193   -1.585  26.649  1.00 15.36 ? 36  LYS B C   1 
ATOM   4361 O O   . LYS B 1 36  ? 7.654   -1.195  27.733  1.00 16.29 ? 36  LYS B O   1 
ATOM   4362 C CB  . LYS B 1 36  ? 7.428   -0.035  24.700  1.00 15.27 ? 36  LYS B CB  1 
ATOM   4363 C CG  . LYS B 1 36  ? 7.681   1.231   25.530  1.00 14.95 ? 36  LYS B CG  1 
ATOM   4364 C CD  . LYS B 1 36  ? 7.363   2.525   24.763  1.00 13.06 ? 36  LYS B CD  1 
ATOM   4365 C CE  . LYS B 1 36  ? 5.849   2.815   24.718  1.00 14.77 ? 36  LYS B CE  1 
ATOM   4366 N NZ  . LYS B 1 36  ? 5.225   3.046   26.082  1.00 14.09 ? 36  LYS B NZ  1 
ATOM   4367 N N   . ASP B 1 37  ? 6.008   -2.198  26.547  1.00 11.39 ? 37  ASP B N   1 
ATOM   4368 C CA  . ASP B 1 37  ? 5.039   -2.268  27.640  1.00 12.45 ? 37  ASP B CA  1 
ATOM   4369 C C   . ASP B 1 37  ? 4.615   -3.672  28.049  1.00 12.86 ? 37  ASP B C   1 
ATOM   4370 O O   . ASP B 1 37  ? 4.465   -3.934  29.244  1.00 12.75 ? 37  ASP B O   1 
ATOM   4371 C CB  . ASP B 1 37  ? 3.779   -1.467  27.262  1.00 15.37 ? 37  ASP B CB  1 
ATOM   4372 C CG  . ASP B 1 37  ? 4.124   -0.068  26.789  1.00 11.82 ? 37  ASP B CG  1 
ATOM   4373 O OD1 . ASP B 1 37  ? 4.704   0.689   27.586  1.00 15.78 ? 37  ASP B OD1 1 
ATOM   4374 O OD2 . ASP B 1 37  ? 3.885   0.249   25.599  1.00 13.48 ? 37  ASP B OD2 1 
ATOM   4375 N N   . TYR B 1 38  ? 4.369   -4.584  27.111  1.00 11.70 ? 38  TYR B N   1 
ATOM   4376 C CA  . TYR B 1 38  ? 3.640   -5.796  27.486  1.00 14.73 ? 38  TYR B CA  1 
ATOM   4377 C C   . TYR B 1 38  ? 4.485   -6.762  28.312  1.00 14.29 ? 38  TYR B C   1 
ATOM   4378 O O   . TYR B 1 38  ? 3.929   -7.483  29.159  1.00 12.75 ? 38  TYR B O   1 
ATOM   4379 C CB  . TYR B 1 38  ? 3.064   -6.492  26.263  1.00 14.02 ? 38  TYR B CB  1 
ATOM   4380 C CG  . TYR B 1 38  ? 2.010   -5.697  25.528  1.00 11.05 ? 38  TYR B CG  1 
ATOM   4381 C CD1 . TYR B 1 38  ? 1.120   -4.885  26.228  1.00 10.34 ? 38  TYR B CD1 1 
ATOM   4382 C CD2 . TYR B 1 38  ? 1.918   -5.749  24.146  1.00 13.25 ? 38  TYR B CD2 1 
ATOM   4383 C CE1 . TYR B 1 38  ? 0.130   -4.147  25.563  1.00 11.52 ? 38  TYR B CE1 1 
ATOM   4384 C CE2 . TYR B 1 38  ? 0.916   -5.019  23.454  1.00 13.11 ? 38  TYR B CE2 1 
ATOM   4385 C CZ  . TYR B 1 38  ? 0.040   -4.219  24.175  1.00 14.58 ? 38  TYR B CZ  1 
ATOM   4386 O OH  . TYR B 1 38  ? -0.935  -3.509  23.503  1.00 12.95 ? 38  TYR B OH  1 
ATOM   4387 N N   . TYR B 1 39  ? 5.805   -6.815  28.077  1.00 13.16 ? 39  TYR B N   1 
ATOM   4388 C CA  . TYR B 1 39  ? 6.668   -7.548  28.988  1.00 15.06 ? 39  TYR B CA  1 
ATOM   4389 C C   . TYR B 1 39  ? 6.968   -6.714  30.227  1.00 14.53 ? 39  TYR B C   1 
ATOM   4390 O O   . TYR B 1 39  ? 6.911   -7.211  31.362  1.00 12.49 ? 39  TYR B O   1 
ATOM   4391 C CB  . TYR B 1 39  ? 7.978   -7.934  28.294  1.00 12.95 ? 39  TYR B CB  1 
ATOM   4392 C CG  . TYR B 1 39  ? 8.978   -8.546  29.263  1.00 11.88 ? 39  TYR B CG  1 
ATOM   4393 C CD1 . TYR B 1 39  ? 8.869   -9.883  29.633  1.00 13.83 ? 39  TYR B CD1 1 
ATOM   4394 C CD2 . TYR B 1 39  ? 10.006  -7.793  29.803  1.00 12.40 ? 39  TYR B CD2 1 
ATOM   4395 C CE1 . TYR B 1 39  ? 9.756   -10.447 30.524  1.00 19.70 ? 39  TYR B CE1 1 
ATOM   4396 C CE2 . TYR B 1 39  ? 10.890  -8.342  30.717  1.00 17.76 ? 39  TYR B CE2 1 
ATOM   4397 C CZ  . TYR B 1 39  ? 10.758  -9.679  31.057  1.00 16.64 ? 39  TYR B CZ  1 
ATOM   4398 O OH  . TYR B 1 39  ? 11.639  -10.262 31.950  1.00 23.06 ? 39  TYR B OH  1 
ATOM   4399 N N   . ASP B 1 40  ? 7.265   -5.429  30.031  1.00 11.48 ? 40  ASP B N   1 
ATOM   4400 C CA  . ASP B 1 40  ? 7.842   -4.670  31.131  1.00 13.32 ? 40  ASP B CA  1 
ATOM   4401 C C   . ASP B 1 40  ? 6.833   -4.317  32.226  1.00 13.62 ? 40  ASP B C   1 
ATOM   4402 O O   . ASP B 1 40  ? 7.223   -4.237  33.395  1.00 13.35 ? 40  ASP B O   1 
ATOM   4403 C CB  . ASP B 1 40  ? 8.509   -3.419  30.578  1.00 14.81 ? 40  ASP B CB  1 
ATOM   4404 C CG  . ASP B 1 40  ? 9.895   -3.715  30.057  1.00 19.01 ? 40  ASP B CG  1 
ATOM   4405 O OD1 . ASP B 1 40  ? 10.781  -3.930  30.903  1.00 16.62 ? 40  ASP B OD1 1 
ATOM   4406 O OD2 . ASP B 1 40  ? 10.099  -3.774  28.826  1.00 20.35 ? 40  ASP B OD2 1 
ATOM   4407 N N   . MET B 1 41  ? 5.561   -4.108  31.886  1.00 11.20 ? 41  MET B N   1 
ATOM   4408 C CA  . MET B 1 41  ? 4.593   -3.777  32.929  1.00 11.45 ? 41  MET B CA  1 
ATOM   4409 C C   . MET B 1 41  ? 4.474   -4.884  33.963  1.00 13.01 ? 41  MET B C   1 
ATOM   4410 O O   . MET B 1 41  ? 4.615   -4.593  35.164  1.00 13.48 ? 41  MET B O   1 
ATOM   4411 C CB  . MET B 1 41  ? 3.258   -3.426  32.271  1.00 12.67 ? 41  MET B CB  1 
ATOM   4412 C CG  . MET B 1 41  ? 3.263   -1.978  31.674  1.00 11.46 ? 41  MET B CG  1 
ATOM   4413 S SD  . MET B 1 41  ? 3.318   -0.650  32.912  1.00 12.82 ? 41  MET B SD  1 
ATOM   4414 C CE  . MET B 1 41  ? 1.626   -0.680  33.482  1.00 10.42 ? 41  MET B CE  1 
ATOM   4415 N N   . PRO B 1 42  ? 4.272   -6.154  33.596  1.00 11.02 ? 42  PRO B N   1 
ATOM   4416 C CA  . PRO B 1 42  ? 4.289   -7.186  34.642  1.00 12.67 ? 42  PRO B CA  1 
ATOM   4417 C C   . PRO B 1 42  ? 5.663   -7.425  35.212  1.00 14.59 ? 42  PRO B C   1 
ATOM   4418 O O   . PRO B 1 42  ? 5.780   -7.883  36.356  1.00 15.13 ? 42  PRO B O   1 
ATOM   4419 C CB  . PRO B 1 42  ? 3.763   -8.436  33.916  1.00 12.98 ? 42  PRO B CB  1 
ATOM   4420 C CG  . PRO B 1 42  ? 4.054   -8.177  32.454  1.00 13.50 ? 42  PRO B CG  1 
ATOM   4421 C CD  . PRO B 1 42  ? 3.761   -6.710  32.320  1.00 10.83 ? 42  PRO B CD  1 
ATOM   4422 N N   . ALA B 1 43  ? 6.722   -7.151  34.446  1.00 12.31 ? 43  ALA B N   1 
ATOM   4423 C CA  . ALA B 1 43  ? 8.061   -7.396  34.958  1.00 13.19 ? 43  ALA B CA  1 
ATOM   4424 C C   . ALA B 1 43  ? 8.438   -6.465  36.117  1.00 11.96 ? 43  ALA B C   1 
ATOM   4425 O O   . ALA B 1 43  ? 9.378   -6.780  36.849  1.00 15.66 ? 43  ALA B O   1 
ATOM   4426 C CB  . ALA B 1 43  ? 9.073   -7.279  33.820  1.00 13.64 ? 43  ALA B CB  1 
ATOM   4427 N N   . TYR B 1 44  ? 7.734   -5.333  36.307  1.00 13.60 ? 44  TYR B N   1 
ATOM   4428 C CA  . TYR B 1 44  ? 7.928   -4.566  37.541  1.00 15.34 ? 44  TYR B CA  1 
ATOM   4429 C C   . TYR B 1 44  ? 7.727   -5.432  38.780  1.00 15.42 ? 44  TYR B C   1 
ATOM   4430 O O   . TYR B 1 44  ? 8.344   -5.170  39.821  1.00 17.07 ? 44  TYR B O   1 
ATOM   4431 C CB  . TYR B 1 44  ? 6.972   -3.365  37.627  1.00 14.33 ? 44  TYR B CB  1 
ATOM   4432 C CG  . TYR B 1 44  ? 7.347   -2.133  36.811  1.00 13.67 ? 44  TYR B CG  1 
ATOM   4433 C CD1 . TYR B 1 44  ? 8.196   -1.141  37.331  1.00 15.89 ? 44  TYR B CD1 1 
ATOM   4434 C CD2 . TYR B 1 44  ? 6.825   -1.950  35.528  1.00 12.23 ? 44  TYR B CD2 1 
ATOM   4435 C CE1 . TYR B 1 44  ? 8.519   0.007   36.585  1.00 14.34 ? 44  TYR B CE1 1 
ATOM   4436 C CE2 . TYR B 1 44  ? 7.166   -0.833  34.764  1.00 12.56 ? 44  TYR B CE2 1 
ATOM   4437 C CZ  . TYR B 1 44  ? 8.002   0.134   35.296  1.00 14.22 ? 44  TYR B CZ  1 
ATOM   4438 O OH  . TYR B 1 44  ? 8.311   1.261   34.556  1.00 18.75 ? 44  TYR B OH  1 
ATOM   4439 N N   . LEU B 1 45  ? 6.890   -6.478  38.686  1.00 16.20 ? 45  LEU B N   1 
ATOM   4440 C CA  . LEU B 1 45  ? 6.612   -7.306  39.860  1.00 15.72 ? 45  LEU B CA  1 
ATOM   4441 C C   . LEU B 1 45  ? 7.811   -8.131  40.269  1.00 20.59 ? 45  LEU B C   1 
ATOM   4442 O O   . LEU B 1 45  ? 7.846   -8.641  41.396  1.00 19.83 ? 45  LEU B O   1 
ATOM   4443 C CB  . LEU B 1 45  ? 5.410   -8.212  39.606  1.00 16.60 ? 45  LEU B CB  1 
ATOM   4444 C CG  . LEU B 1 45  ? 4.045   -7.509  39.553  1.00 19.66 ? 45  LEU B CG  1 
ATOM   4445 C CD1 . LEU B 1 45  ? 2.957   -8.451  39.036  1.00 19.40 ? 45  LEU B CD1 1 
ATOM   4446 C CD2 . LEU B 1 45  ? 3.669   -6.991  40.930  1.00 16.73 ? 45  LEU B CD2 1 
ATOM   4447 N N   . LYS B 1 46  ? 8.804   -8.277  39.385  1.00 18.32 ? 46  LYS B N   1 
ATOM   4448 C CA  . LYS B 1 46  ? 10.031  -8.936  39.810  1.00 21.78 ? 46  LYS B CA  1 
ATOM   4449 C C   . LYS B 1 46  ? 10.798  -8.085  40.807  1.00 20.58 ? 46  LYS B C   1 
ATOM   4450 O O   . LYS B 1 46  ? 11.515  -8.625  41.655  1.00 25.01 ? 46  LYS B O   1 
ATOM   4451 C CB  . LYS B 1 46  ? 10.907  -9.254  38.600  1.00 25.43 ? 46  LYS B CB  1 
ATOM   4452 C CG  . LYS B 1 46  ? 10.390  -10.426 37.774  1.00 28.50 ? 46  LYS B CG  1 
ATOM   4453 C CD  . LYS B 1 46  ? 10.898  -10.396 36.337  1.00 41.18 ? 46  LYS B CD  1 
ATOM   4454 C CE  . LYS B 1 46  ? 12.405  -10.358 36.277  1.00 51.64 ? 46  LYS B CE  1 
ATOM   4455 N NZ  . LYS B 1 46  ? 12.892  -10.985 35.013  1.00 56.11 ? 46  LYS B NZ  1 
ATOM   4456 N N   . ASP B 1 47  ? 10.639  -6.762  40.746  1.00 19.46 ? 47  ASP B N   1 
ATOM   4457 C CA  . ASP B 1 47  ? 11.474  -5.833  41.496  1.00 18.74 ? 47  ASP B CA  1 
ATOM   4458 C C   . ASP B 1 47  ? 10.757  -5.144  42.650  1.00 17.67 ? 47  ASP B C   1 
ATOM   4459 O O   . ASP B 1 47  ? 11.428  -4.504  43.469  1.00 21.35 ? 47  ASP B O   1 
ATOM   4460 C CB  . ASP B 1 47  ? 12.021  -4.748  40.558  1.00 18.97 ? 47  ASP B CB  1 
ATOM   4461 C CG  . ASP B 1 47  ? 13.050  -5.280  39.590  1.00 32.91 ? 47  ASP B CG  1 
ATOM   4462 O OD1 . ASP B 1 47  ? 13.784  -6.201  39.985  1.00 33.06 ? 47  ASP B OD1 1 
ATOM   4463 O OD2 . ASP B 1 47  ? 13.114  -4.779  38.442  1.00 34.78 ? 47  ASP B OD2 1 
ATOM   4464 N N   . PHE B 1 48  ? 9.425   -5.229  42.722  1.00 18.13 ? 48  PHE B N   1 
ATOM   4465 C CA  . PHE B 1 48  ? 8.661   -4.568  43.772  1.00 19.15 ? 48  PHE B CA  1 
ATOM   4466 C C   . PHE B 1 48  ? 7.669   -5.563  44.351  1.00 18.20 ? 48  PHE B C   1 
ATOM   4467 O O   . PHE B 1 48  ? 6.959   -6.245  43.605  1.00 17.49 ? 48  PHE B O   1 
ATOM   4468 C CB  . PHE B 1 48  ? 7.947   -3.320  43.231  1.00 18.96 ? 48  PHE B CB  1 
ATOM   4469 C CG  . PHE B 1 48  ? 8.889   -2.310  42.654  1.00 20.30 ? 48  PHE B CG  1 
ATOM   4470 C CD1 . PHE B 1 48  ? 9.557   -1.420  43.487  1.00 23.11 ? 48  PHE B CD1 1 
ATOM   4471 C CD2 . PHE B 1 48  ? 9.160   -2.289  41.292  1.00 18.02 ? 48  PHE B CD2 1 
ATOM   4472 C CE1 . PHE B 1 48  ? 10.455  -0.499  42.972  1.00 21.23 ? 48  PHE B CE1 1 
ATOM   4473 C CE2 . PHE B 1 48  ? 10.078  -1.374  40.770  1.00 21.15 ? 48  PHE B CE2 1 
ATOM   4474 C CZ  . PHE B 1 48  ? 10.724  -0.479  41.623  1.00 24.59 ? 48  PHE B CZ  1 
ATOM   4475 N N   . GLU B 1 49  ? 7.609   -5.632  45.680  1.00 16.54 ? 49  GLU B N   1 
ATOM   4476 C CA  . GLU B 1 49  ? 6.785   -6.623  46.380  1.00 16.33 ? 49  GLU B CA  1 
ATOM   4477 C C   . GLU B 1 49  ? 5.377   -6.077  46.619  1.00 14.98 ? 49  GLU B C   1 
ATOM   4478 O O   . GLU B 1 49  ? 4.934   -5.862  47.751  1.00 17.36 ? 49  GLU B O   1 
ATOM   4479 C CB  . GLU B 1 49  ? 7.462   -7.038  47.682  1.00 17.43 ? 49  GLU B CB  1 
ATOM   4480 C CG  . GLU B 1 49  ? 8.705   -7.875  47.396  1.00 23.13 ? 49  GLU B CG  1 
ATOM   4481 C CD  . GLU B 1 49  ? 8.372   -9.201  46.696  1.00 29.19 ? 49  GLU B CD  1 
ATOM   4482 O OE1 . GLU B 1 49  ? 7.560   -9.996  47.235  1.00 32.98 ? 49  GLU B OE1 1 
ATOM   4483 O OE2 . GLU B 1 49  ? 8.926   -9.455  45.608  1.00 33.94 ? 49  GLU B OE2 1 
ATOM   4484 N N   . ILE B 1 50  ? 4.655   -5.877  45.510  1.00 16.21 ? 50  ILE B N   1 
ATOM   4485 C CA  . ILE B 1 50  ? 3.259   -5.431  45.503  1.00 13.47 ? 50  ILE B CA  1 
ATOM   4486 C C   . ILE B 1 50  ? 2.463   -6.386  44.620  1.00 15.34 ? 50  ILE B C   1 
ATOM   4487 O O   . ILE B 1 50  ? 3.019   -7.295  44.011  1.00 16.14 ? 50  ILE B O   1 
ATOM   4488 C CB  . ILE B 1 50  ? 3.108   -3.983  44.986  1.00 12.14 ? 50  ILE B CB  1 
ATOM   4489 C CG1 . ILE B 1 50  ? 3.719   -3.890  43.586  1.00 16.19 ? 50  ILE B CG1 1 
ATOM   4490 C CG2 . ILE B 1 50  ? 3.737   -2.944  45.977  1.00 17.42 ? 50  ILE B CG2 1 
ATOM   4491 C CD1 . ILE B 1 50  ? 3.439   -2.635  42.879  1.00 21.96 ? 50  ILE B CD1 1 
ATOM   4492 N N   . LYS B 1 51  ? 1.150   -6.188  44.564  1.00 14.86 ? 51  LYS B N   1 
ATOM   4493 C CA  . LYS B 1 51  ? 0.294   -6.936  43.640  1.00 14.18 ? 51  LYS B CA  1 
ATOM   4494 C C   . LYS B 1 51  ? -0.148  -6.019  42.510  1.00 11.39 ? 51  LYS B C   1 
ATOM   4495 O O   . LYS B 1 51  ? -0.467  -4.849  42.747  1.00 12.49 ? 51  LYS B O   1 
ATOM   4496 C CB  . LYS B 1 51  ? -0.948  -7.498  44.342  1.00 12.16 ? 51  LYS B CB  1 
ATOM   4497 C CG  . LYS B 1 51  ? -0.676  -8.153  45.675  1.00 18.72 ? 51  LYS B CG  1 
ATOM   4498 C CD  . LYS B 1 51  ? 0.125   -9.413  45.519  1.00 19.78 ? 51  LYS B CD  1 
ATOM   4499 C CE  . LYS B 1 51  ? 0.260   -10.142 46.874  1.00 23.19 ? 51  LYS B CE  1 
ATOM   4500 N NZ  . LYS B 1 51  ? 1.092   -11.353 46.709  1.00 35.39 ? 51  LYS B NZ  1 
ATOM   4501 N N   . LEU B 1 52  ? -0.165  -6.546  41.284  1.00 9.75  ? 52  LEU B N   1 
ATOM   4502 C CA  . LEU B 1 52  ? -0.645  -5.803  40.125  1.00 11.17 ? 52  LEU B CA  1 
ATOM   4503 C C   . LEU B 1 52  ? -1.377  -6.779  39.232  1.00 13.07 ? 52  LEU B C   1 
ATOM   4504 O O   . LEU B 1 52  ? -0.887  -7.885  39.007  1.00 15.07 ? 52  LEU B O   1 
ATOM   4505 C CB  . LEU B 1 52  ? 0.504   -5.170  39.323  1.00 13.91 ? 52  LEU B CB  1 
ATOM   4506 C CG  . LEU B 1 52  ? 1.401   -4.125  39.987  1.00 14.02 ? 52  LEU B CG  1 
ATOM   4507 C CD1 . LEU B 1 52  ? 2.649   -3.940  39.079  1.00 14.87 ? 52  LEU B CD1 1 
ATOM   4508 C CD2 . LEU B 1 52  ? 0.637   -2.799  40.237  1.00 13.61 ? 52  LEU B CD2 1 
ATOM   4509 N N   . ASN B 1 53  ? -2.530  -6.383  38.713  1.00 11.50 ? 53  ASN B N   1 
ATOM   4510 C CA  . ASN B 1 53  ? -3.329  -7.274  37.885  1.00 10.51 ? 53  ASN B CA  1 
ATOM   4511 C C   . ASN B 1 53  ? -3.371  -6.789  36.447  1.00 10.50 ? 53  ASN B C   1 
ATOM   4512 O O   . ASN B 1 53  ? -3.173  -5.602  36.157  1.00 10.50 ? 53  ASN B O   1 
ATOM   4513 C CB  . ASN B 1 53  ? -4.760  -7.378  38.435  1.00 10.26 ? 53  ASN B CB  1 
ATOM   4514 C CG  . ASN B 1 53  ? -4.753  -7.676  39.914  1.00 10.23 ? 53  ASN B CG  1 
ATOM   4515 O OD1 . ASN B 1 53  ? -4.561  -8.827  40.323  1.00 11.43 ? 53  ASN B OD1 1 
ATOM   4516 N ND2 . ASN B 1 53  ? -4.931  -6.638  40.739  1.00 11.24 ? 53  ASN B ND2 1 
ATOM   4517 N N   . PHE B 1 54  ? -3.652  -7.727  35.553  1.00 10.41 ? 54  PHE B N   1 
ATOM   4518 C CA  . PHE B 1 54  ? -3.570  -7.455  34.123  1.00 12.54 ? 54  PHE B CA  1 
ATOM   4519 C C   . PHE B 1 54  ? -4.741  -8.083  33.397  1.00 13.90 ? 54  PHE B C   1 
ATOM   4520 O O   . PHE B 1 54  ? -5.188  -9.183  33.731  1.00 13.75 ? 54  PHE B O   1 
ATOM   4521 C CB  . PHE B 1 54  ? -2.250  -7.995  33.530  1.00 9.15  ? 54  PHE B CB  1 
ATOM   4522 C CG  . PHE B 1 54  ? -1.056  -7.366  34.152  1.00 11.66 ? 54  PHE B CG  1 
ATOM   4523 C CD1 . PHE B 1 54  ? -0.471  -7.912  35.302  1.00 14.93 ? 54  PHE B CD1 1 
ATOM   4524 C CD2 . PHE B 1 54  ? -0.578  -6.152  33.657  1.00 12.64 ? 54  PHE B CD2 1 
ATOM   4525 C CE1 . PHE B 1 54  ? 0.605   -7.254  35.919  1.00 12.90 ? 54  PHE B CE1 1 
ATOM   4526 C CE2 . PHE B 1 54  ? 0.513   -5.510  34.262  1.00 12.67 ? 54  PHE B CE2 1 
ATOM   4527 C CZ  . PHE B 1 54  ? 1.087   -6.059  35.385  1.00 12.41 ? 54  PHE B CZ  1 
ATOM   4528 N N   . ASN B 1 55  ? -5.179  -7.398  32.363  1.00 11.72 ? 55  ASN B N   1 
ATOM   4529 C CA  . ASN B 1 55  ? -6.106  -7.940  31.383  1.00 12.83 ? 55  ASN B CA  1 
ATOM   4530 C C   . ASN B 1 55  ? -5.370  -8.107  30.065  1.00 11.34 ? 55  ASN B C   1 
ATOM   4531 O O   . ASN B 1 55  ? -4.689  -7.184  29.623  1.00 12.95 ? 55  ASN B O   1 
ATOM   4532 C CB  . ASN B 1 55  ? -7.300  -7.011  31.156  1.00 13.86 ? 55  ASN B CB  1 
ATOM   4533 C CG  . ASN B 1 55  ? -8.353  -7.664  30.264  1.00 14.80 ? 55  ASN B CG  1 
ATOM   4534 O OD1 . ASN B 1 55  ? -8.923  -8.688  30.621  1.00 15.33 ? 55  ASN B OD1 1 
ATOM   4535 N ND2 . ASN B 1 55  ? -8.595  -7.089  29.097  1.00 11.77 ? 55  ASN B ND2 1 
ATOM   4536 N N   . LEU B 1 56  ? -5.508  -9.273  29.437  1.00 12.36 ? 56  LEU B N   1 
ATOM   4537 C CA  . LEU B 1 56  ? -4.964  -9.506  28.098  1.00 16.23 ? 56  LEU B CA  1 
ATOM   4538 C C   . LEU B 1 56  ? -6.101  -9.911  27.174  1.00 14.95 ? 56  LEU B C   1 
ATOM   4539 O O   . LEU B 1 56  ? -6.725  -10.949 27.404  1.00 14.63 ? 56  LEU B O   1 
ATOM   4540 C CB  . LEU B 1 56  ? -3.918  -10.621 28.105  1.00 15.55 ? 56  LEU B CB  1 
ATOM   4541 C CG  . LEU B 1 56  ? -2.619  -10.359 28.845  1.00 18.46 ? 56  LEU B CG  1 
ATOM   4542 C CD1 . LEU B 1 56  ? -1.809  -11.646 28.921  1.00 22.71 ? 56  LEU B CD1 1 
ATOM   4543 C CD2 . LEU B 1 56  ? -1.821  -9.296  28.134  1.00 20.67 ? 56  LEU B CD2 1 
ATOM   4544 N N   . THR B 1 57  ? -6.326  -9.154  26.094  1.00 13.69 ? 57  THR B N   1 
ATOM   4545 C CA  . THR B 1 57  ? -7.353  -9.612  25.165  1.00 13.62 ? 57  THR B CA  1 
ATOM   4546 C C   . THR B 1 57  ? -6.848  -10.806 24.341  1.00 14.85 ? 57  THR B C   1 
ATOM   4547 O O   . THR B 1 57  ? -5.650  -10.927 24.058  1.00 14.21 ? 57  THR B O   1 
ATOM   4548 C CB  . THR B 1 57  ? -7.824  -8.494  24.212  1.00 15.28 ? 57  THR B CB  1 
ATOM   4549 O OG1 . THR B 1 57  ? -6.746  -8.105  23.357  1.00 15.17 ? 57  THR B OG1 1 
ATOM   4550 C CG2 . THR B 1 57  ? -8.368  -7.274  24.986  1.00 14.59 ? 57  THR B CG2 1 
ATOM   4551 N N   . PRO B 1 58  ? -7.742  -11.713 23.953  1.00 14.55 ? 58  PRO B N   1 
ATOM   4552 C CA  . PRO B 1 58  ? -7.281  -12.874 23.177  1.00 15.30 ? 58  PRO B CA  1 
ATOM   4553 C C   . PRO B 1 58  ? -6.651  -12.496 21.862  1.00 19.36 ? 58  PRO B C   1 
ATOM   4554 O O   . PRO B 1 58  ? -5.656  -13.119 21.466  1.00 18.49 ? 58  PRO B O   1 
ATOM   4555 C CB  . PRO B 1 58  ? -8.567  -13.687 22.977  1.00 16.43 ? 58  PRO B CB  1 
ATOM   4556 C CG  . PRO B 1 58  ? -9.378  -13.375 24.202  1.00 19.58 ? 58  PRO B CG  1 
ATOM   4557 C CD  . PRO B 1 58  ? -9.108  -11.908 24.471  1.00 15.84 ? 58  PRO B CD  1 
ATOM   4558 N N   . VAL B 1 59  ? -7.191  -11.489 21.166  1.00 17.33 ? 59  VAL B N   1 
ATOM   4559 C CA  . VAL B 1 59  ? -6.589  -11.088 19.893  1.00 15.36 ? 59  VAL B CA  1 
ATOM   4560 C C   . VAL B 1 59  ? -5.176  -10.530 20.097  1.00 14.78 ? 59  VAL B C   1 
ATOM   4561 O O   . VAL B 1 59  ? -4.304  -10.745 19.245  1.00 15.39 ? 59  VAL B O   1 
ATOM   4562 C CB  . VAL B 1 59  ? -7.538  -10.119 19.130  1.00 19.44 ? 59  VAL B CB  1 
ATOM   4563 C CG1 . VAL B 1 59  ? -7.877  -8.859  19.953  1.00 16.19 ? 59  VAL B CG1 1 
ATOM   4564 C CG2 . VAL B 1 59  ? -6.968  -9.774  17.729  1.00 18.54 ? 59  VAL B CG2 1 
ATOM   4565 N N   . LEU B 1 60  ? -4.898  -9.861  21.230  1.00 13.44 ? 60  LEU B N   1 
ATOM   4566 C CA  . LEU B 1 60  ? -3.517  -9.464  21.498  1.00 13.30 ? 60  LEU B CA  1 
ATOM   4567 C C   . LEU B 1 60  ? -2.633  -10.690 21.718  1.00 16.95 ? 60  LEU B C   1 
ATOM   4568 O O   . LEU B 1 60  ? -1.537  -10.786 21.146  1.00 14.42 ? 60  LEU B O   1 
ATOM   4569 C CB  . LEU B 1 60  ? -3.454  -8.507  22.700  1.00 11.92 ? 60  LEU B CB  1 
ATOM   4570 C CG  . LEU B 1 60  ? -2.042  -8.143  23.179  1.00 11.82 ? 60  LEU B CG  1 
ATOM   4571 C CD1 . LEU B 1 60  ? -1.245  -7.463  22.066  1.00 14.86 ? 60  LEU B CD1 1 
ATOM   4572 C CD2 . LEU B 1 60  ? -2.109  -7.252  24.421  1.00 10.80 ? 60  LEU B CD2 1 
ATOM   4573 N N   . ILE B 1 61  ? -3.113  -11.658 22.496  1.00 16.13 ? 61  ILE B N   1 
ATOM   4574 C CA  . ILE B 1 61  ? -2.317  -12.854 22.762  1.00 18.76 ? 61  ILE B CA  1 
ATOM   4575 C C   . ILE B 1 61  ? -1.948  -13.544 21.466  1.00 16.87 ? 61  ILE B C   1 
ATOM   4576 O O   . ILE B 1 61  ? -0.794  -13.933 21.278  1.00 16.59 ? 61  ILE B O   1 
ATOM   4577 C CB  . ILE B 1 61  ? -3.055  -13.817 23.708  1.00 17.01 ? 61  ILE B CB  1 
ATOM   4578 C CG1 . ILE B 1 61  ? -3.208  -13.199 25.100  1.00 15.68 ? 61  ILE B CG1 1 
ATOM   4579 C CG2 . ILE B 1 61  ? -2.335  -15.179 23.761  1.00 19.23 ? 61  ILE B CG2 1 
ATOM   4580 C CD1 . ILE B 1 61  ? -4.075  -14.074 26.043  1.00 15.83 ? 61  ILE B CD1 1 
ATOM   4581 N N   . ASP B 1 62  ? -2.916  -13.686 20.539  1.00 15.61 ? 62  ASP B N   1 
ATOM   4582 C CA  . ASP B 1 62  ? -2.637  -14.303 19.237  1.00 16.23 ? 62  ASP B CA  1 
ATOM   4583 C C   . ASP B 1 62  ? -1.481  -13.619 18.517  1.00 16.72 ? 62  ASP B C   1 
ATOM   4584 O O   . ASP B 1 62  ? -0.630  -14.283 17.913  1.00 17.60 ? 62  ASP B O   1 
ATOM   4585 C CB  . ASP B 1 62  ? -3.886  -14.237 18.348  1.00 17.36 ? 62  ASP B CB  1 
ATOM   4586 C CG  . ASP B 1 62  ? -4.941  -15.254 18.732  1.00 29.08 ? 62  ASP B CG  1 
ATOM   4587 O OD1 . ASP B 1 62  ? -4.587  -16.259 19.388  1.00 28.69 ? 62  ASP B OD1 1 
ATOM   4588 O OD2 . ASP B 1 62  ? -6.130  -15.056 18.367  1.00 27.08 ? 62  ASP B OD2 1 
ATOM   4589 N N   . GLN B 1 63  ? -1.461  -12.281 18.533  1.00 14.47 ? 63  GLN B N   1 
ATOM   4590 C CA  . GLN B 1 63  ? -0.441  -11.532 17.810  1.00 15.45 ? 63  GLN B CA  1 
ATOM   4591 C C   . GLN B 1 63  ? 0.921   -11.634 18.488  1.00 14.05 ? 63  GLN B C   1 
ATOM   4592 O O   . GLN B 1 63  ? 1.949   -11.742 17.804  1.00 15.74 ? 63  GLN B O   1 
ATOM   4593 C CB  . GLN B 1 63  ? -0.856  -10.065 17.703  1.00 15.79 ? 63  GLN B CB  1 
ATOM   4594 C CG  . GLN B 1 63  ? -2.062  -9.830  16.797  1.00 15.87 ? 63  GLN B CG  1 
ATOM   4595 C CD  . GLN B 1 63  ? -2.501  -8.375  16.837  1.00 19.07 ? 63  GLN B CD  1 
ATOM   4596 O OE1 . GLN B 1 63  ? -1.873  -7.514  16.219  1.00 22.77 ? 63  GLN B OE1 1 
ATOM   4597 N NE2 . GLN B 1 63  ? -3.567  -8.094  17.576  1.00 15.29 ? 63  GLN B NE2 1 
ATOM   4598 N N   . ILE B 1 64  ? 0.953   -11.556 19.822  1.00 13.43 ? 64  ILE B N   1 
ATOM   4599 C CA  . ILE B 1 64  ? 2.221   -11.737 20.527  1.00 14.61 ? 64  ILE B CA  1 
ATOM   4600 C C   . ILE B 1 64  ? 2.811   -13.096 20.178  1.00 18.88 ? 64  ILE B C   1 
ATOM   4601 O O   . ILE B 1 64  ? 4.011   -13.216 19.892  1.00 17.48 ? 64  ILE B O   1 
ATOM   4602 C CB  . ILE B 1 64  ? 2.034   -11.556 22.044  1.00 15.99 ? 64  ILE B CB  1 
ATOM   4603 C CG1 . ILE B 1 64  ? 1.667   -10.093 22.357  1.00 14.69 ? 64  ILE B CG1 1 
ATOM   4604 C CG2 . ILE B 1 64  ? 3.327   -11.979 22.782  1.00 15.39 ? 64  ILE B CG2 1 
ATOM   4605 C CD1 . ILE B 1 64  ? 1.293   -9.843  23.809  1.00 16.00 ? 64  ILE B CD1 1 
ATOM   4606 N N   . GLN B 1 65  ? 1.969   -14.131 20.155  1.00 17.33 ? 65  GLN B N   1 
ATOM   4607 C CA  . GLN B 1 65  ? 2.465   -15.456 19.805  1.00 19.10 ? 65  GLN B CA  1 
ATOM   4608 C C   . GLN B 1 65  ? 3.077   -15.453 18.410  1.00 21.08 ? 65  GLN B C   1 
ATOM   4609 O O   . GLN B 1 65  ? 4.173   -15.997 18.203  1.00 20.64 ? 65  GLN B O   1 
ATOM   4610 C CB  . GLN B 1 65  ? 1.341   -16.487 19.913  1.00 23.40 ? 65  GLN B CB  1 
ATOM   4611 C CG  . GLN B 1 65  ? 0.861   -16.693 21.341  1.00 25.19 ? 65  GLN B CG  1 
ATOM   4612 C CD  . GLN B 1 65  ? -0.238  -17.737 21.462  1.00 33.06 ? 65  GLN B CD  1 
ATOM   4613 O OE1 . GLN B 1 65  ? -1.269  -17.667 20.782  1.00 35.36 ? 65  GLN B OE1 1 
ATOM   4614 N NE2 . GLN B 1 65  ? -0.024  -18.715 22.330  1.00 41.98 ? 65  GLN B NE2 1 
ATOM   4615 N N   . GLU B 1 66  ? 2.404   -14.817 17.442  1.00 19.65 ? 66  GLU B N   1 
ATOM   4616 C CA  . GLU B 1 66  ? 2.931   -14.827 16.078  1.00 23.14 ? 66  GLU B CA  1 
ATOM   4617 C C   . GLU B 1 66  ? 4.283   -14.120 16.001  1.00 21.93 ? 66  GLU B C   1 
ATOM   4618 O O   . GLU B 1 66  ? 5.215   -14.622 15.360  1.00 22.13 ? 66  GLU B O   1 
ATOM   4619 C CB  . GLU B 1 66  ? 1.918   -14.210 15.101  1.00 22.61 ? 66  GLU B CB  1 
ATOM   4620 C CG  . GLU B 1 66  ? 2.190   -14.550 13.627  1.00 35.32 ? 66  GLU B CG  1 
ATOM   4621 C CD  . GLU B 1 66  ? 1.036   -14.183 12.691  1.00 38.92 ? 66  GLU B CD  1 
ATOM   4622 O OE1 . GLU B 1 66  ? -0.021  -13.742 13.192  1.00 30.39 ? 66  GLU B OE1 1 
ATOM   4623 O OE2 . GLU B 1 66  ? 1.197   -14.331 11.453  1.00 43.62 ? 66  GLU B OE2 1 
ATOM   4624 N N   . TYR B 1 67  ? 4.428   -12.963 16.654  1.00 17.31 ? 67  TYR B N   1 
ATOM   4625 C CA  . TYR B 1 67  ? 5.739   -12.314 16.671  1.00 19.60 ? 67  TYR B CA  1 
ATOM   4626 C C   . TYR B 1 67  ? 6.770   -13.181 17.374  1.00 23.90 ? 67  TYR B C   1 
ATOM   4627 O O   . TYR B 1 67  ? 7.930   -13.260 16.943  1.00 23.27 ? 67  TYR B O   1 
ATOM   4628 C CB  . TYR B 1 67  ? 5.670   -10.958 17.358  1.00 17.81 ? 67  TYR B CB  1 
ATOM   4629 C CG  . TYR B 1 67  ? 5.153   -9.844  16.479  1.00 19.48 ? 67  TYR B CG  1 
ATOM   4630 C CD1 . TYR B 1 67  ? 6.017   -9.139  15.639  1.00 16.28 ? 67  TYR B CD1 1 
ATOM   4631 C CD2 . TYR B 1 67  ? 3.810   -9.484  16.498  1.00 21.31 ? 67  TYR B CD2 1 
ATOM   4632 C CE1 . TYR B 1 67  ? 5.561   -8.125  14.857  1.00 16.96 ? 67  TYR B CE1 1 
ATOM   4633 C CE2 . TYR B 1 67  ? 3.339   -8.462  15.705  1.00 19.23 ? 67  TYR B CE2 1 
ATOM   4634 C CZ  . TYR B 1 67  ? 4.214   -7.777  14.893  1.00 20.49 ? 67  TYR B CZ  1 
ATOM   4635 O OH  . TYR B 1 67  ? 3.750   -6.738  14.113  1.00 20.82 ? 67  TYR B OH  1 
ATOM   4636 N N   . ALA B 1 68  ? 6.365   -13.843 18.457  1.00 19.90 ? 68  ALA B N   1 
ATOM   4637 C CA  . ALA B 1 68  ? 7.310   -14.640 19.238  1.00 22.00 ? 68  ALA B CA  1 
ATOM   4638 C C   . ALA B 1 68  ? 7.809   -15.843 18.453  1.00 23.88 ? 68  ALA B C   1 
ATOM   4639 O O   . ALA B 1 68  ? 8.962   -16.268 18.629  1.00 25.42 ? 68  ALA B O   1 
ATOM   4640 C CB  . ALA B 1 68  ? 6.659   -15.094 20.539  1.00 18.95 ? 68  ALA B CB  1 
ATOM   4641 N N   . GLN B 1 69  ? 6.962   -16.402 17.596  1.00 23.07 ? 69  GLN B N   1 
ATOM   4642 C CA  . GLN B 1 69  ? 7.311   -17.565 16.795  1.00 26.51 ? 69  GLN B CA  1 
ATOM   4643 C C   . GLN B 1 69  ? 8.036   -17.190 15.512  1.00 30.26 ? 69  GLN B C   1 
ATOM   4644 O O   . GLN B 1 69  ? 8.359   -18.082 14.721  1.00 36.11 ? 69  GLN B O   1 
ATOM   4645 C CB  . GLN B 1 69  ? 6.050   -18.368 16.470  1.00 32.69 ? 69  GLN B CB  1 
ATOM   4646 C CG  . GLN B 1 69  ? 5.313   -18.889 17.704  1.00 37.95 ? 69  GLN B CG  1 
ATOM   4647 C CD  . GLN B 1 69  ? 3.882   -19.314 17.408  1.00 51.52 ? 69  GLN B CD  1 
ATOM   4648 O OE1 . GLN B 1 69  ? 3.424   -19.232 16.270  1.00 57.07 ? 69  GLN B OE1 1 
ATOM   4649 N NE2 . GLN B 1 69  ? 3.167   -19.761 18.438  1.00 50.48 ? 69  GLN B NE2 1 
ATOM   4650 N N   . GLY B 1 70  ? 8.297   -15.904 15.287  1.00 30.95 ? 70  GLY B N   1 
ATOM   4651 C CA  . GLY B 1 70  ? 8.970   -15.486 14.071  1.00 30.93 ? 70  GLY B CA  1 
ATOM   4652 C C   . GLY B 1 70  ? 8.116   -15.594 12.831  1.00 37.36 ? 70  GLY B C   1 
ATOM   4653 O O   . GLY B 1 70  ? 8.651   -15.781 11.737  1.00 43.05 ? 70  GLY B O   1 
ATOM   4654 N N   . LYS B 1 71  ? 6.794   -15.476 12.968  1.00 33.37 ? 71  LYS B N   1 
ATOM   4655 C CA  . LYS B 1 71  ? 5.884   -15.630 11.843  1.00 38.93 ? 71  LYS B CA  1 
ATOM   4656 C C   . LYS B 1 71  ? 5.205   -14.340 11.398  1.00 36.12 ? 71  LYS B C   1 
ATOM   4657 O O   . LYS B 1 71  ? 4.523   -14.350 10.365  1.00 39.08 ? 71  LYS B O   1 
ATOM   4658 C CB  . LYS B 1 71  ? 4.802   -16.667 12.175  1.00 42.71 ? 71  LYS B CB  1 
ATOM   4659 C CG  . LYS B 1 71  ? 5.314   -18.093 12.199  1.00 48.54 ? 71  LYS B CG  1 
ATOM   4660 C CD  . LYS B 1 71  ? 4.188   -19.085 12.429  1.00 50.00 ? 71  LYS B CD  1 
ATOM   4661 C CE  . LYS B 1 71  ? 3.086   -18.489 13.288  1.00 51.62 ? 71  LYS B CE  1 
ATOM   4662 N NZ  . LYS B 1 71  ? 2.240   -19.557 13.908  1.00 52.60 ? 71  LYS B NZ  1 
ATOM   4663 N N   . ALA B 1 72  ? 5.363   -13.238 12.132  1.00 26.89 ? 72  ALA B N   1 
ATOM   4664 C CA  . ALA B 1 72  ? 4.674   -11.998 11.794  1.00 25.27 ? 72  ALA B CA  1 
ATOM   4665 C C   . ALA B 1 72  ? 5.440   -11.248 10.711  1.00 26.94 ? 72  ALA B C   1 
ATOM   4666 O O   . ALA B 1 72  ? 6.599   -10.879 10.908  1.00 30.32 ? 72  ALA B O   1 
ATOM   4667 C CB  . ALA B 1 72  ? 4.511   -11.116 13.030  1.00 27.32 ? 72  ALA B CB  1 
ATOM   4668 N N   . LYS B 1 73  ? 4.795   -11.020 9.570   1.00 22.12 ? 73  LYS B N   1 
ATOM   4669 C CA  . LYS B 1 73  ? 5.378   -10.226 8.487   1.00 21.51 ? 73  LYS B CA  1 
ATOM   4670 C C   . LYS B 1 73  ? 4.908   -8.785  8.669   1.00 24.94 ? 73  LYS B C   1 
ATOM   4671 O O   . LYS B 1 73  ? 3.859   -8.377  8.169   1.00 26.95 ? 73  LYS B O   1 
ATOM   4672 C CB  . LYS B 1 73  ? 4.986   -10.791 7.123   1.00 28.67 ? 73  LYS B CB  1 
ATOM   4673 C CG  . LYS B 1 73  ? 6.071   -10.618 6.070   1.00 38.86 ? 73  LYS B CG  1 
ATOM   4674 C CD  . LYS B 1 73  ? 5.505   -10.449 4.667   1.00 44.47 ? 73  LYS B CD  1 
ATOM   4675 C CE  . LYS B 1 73  ? 6.628   -10.387 3.633   1.00 51.81 ? 73  LYS B CE  1 
ATOM   4676 N NZ  . LYS B 1 73  ? 6.232   -9.689  2.375   1.00 54.82 ? 73  LYS B NZ  1 
ATOM   4677 N N   . ASP B 1 74  ? 5.706   -8.002  9.381   1.00 21.04 ? 74  ASP B N   1 
ATOM   4678 C CA  . ASP B 1 74  ? 5.351   -6.649  9.801   1.00 20.31 ? 74  ASP B CA  1 
ATOM   4679 C C   . ASP B 1 74  ? 5.976   -5.680  8.799   1.00 27.34 ? 74  ASP B C   1 
ATOM   4680 O O   . ASP B 1 74  ? 7.207   -5.590  8.702   1.00 22.37 ? 74  ASP B O   1 
ATOM   4681 C CB  . ASP B 1 74  ? 5.860   -6.425  11.228  1.00 18.97 ? 74  ASP B CB  1 
ATOM   4682 C CG  . ASP B 1 74  ? 5.491   -5.090  11.798  1.00 24.15 ? 74  ASP B CG  1 
ATOM   4683 O OD1 . ASP B 1 74  ? 5.656   -4.073  11.098  1.00 22.75 ? 74  ASP B OD1 1 
ATOM   4684 O OD2 . ASP B 1 74  ? 5.088   -5.042  12.990  1.00 23.89 ? 74  ASP B OD2 1 
ATOM   4685 N N   . VAL B 1 75  ? 5.136   -4.958  8.046   1.00 23.47 ? 75  VAL B N   1 
ATOM   4686 C CA  . VAL B 1 75  ? 5.654   -4.162  6.932   1.00 21.88 ? 75  VAL B CA  1 
ATOM   4687 C C   . VAL B 1 75  ? 6.473   -2.971  7.422   1.00 24.96 ? 75  VAL B C   1 
ATOM   4688 O O   . VAL B 1 75  ? 7.522   -2.649  6.834   1.00 23.22 ? 75  VAL B O   1 
ATOM   4689 C CB  . VAL B 1 75  ? 4.514   -3.724  5.987   1.00 27.87 ? 75  VAL B CB  1 
ATOM   4690 C CG1 . VAL B 1 75  ? 3.737   -4.938  5.502   1.00 31.22 ? 75  VAL B CG1 1 
ATOM   4691 C CG2 . VAL B 1 75  ? 3.587   -2.729  6.663   1.00 32.11 ? 75  VAL B CG2 1 
ATOM   4692 N N   . PHE B 1 76  ? 6.041   -2.302  8.500   1.00 24.92 ? 76  PHE B N   1 
ATOM   4693 C CA  . PHE B 1 76  ? 6.840   -1.185  9.008   1.00 24.74 ? 76  PHE B CA  1 
ATOM   4694 C C   . PHE B 1 76  ? 8.157   -1.668  9.573   1.00 23.83 ? 76  PHE B C   1 
ATOM   4695 O O   . PHE B 1 76  ? 9.197   -1.019  9.386   1.00 24.39 ? 76  PHE B O   1 
ATOM   4696 C CB  . PHE B 1 76  ? 6.075   -0.399  10.075  1.00 23.48 ? 76  PHE B CB  1 
ATOM   4697 C CG  . PHE B 1 76  ? 5.138   0.607   9.504   1.00 32.50 ? 76  PHE B CG  1 
ATOM   4698 C CD1 . PHE B 1 76  ? 3.930   0.200   8.951   1.00 36.22 ? 76  PHE B CD1 1 
ATOM   4699 C CD2 . PHE B 1 76  ? 5.475   1.951   9.477   1.00 33.90 ? 76  PHE B CD2 1 
ATOM   4700 C CE1 . PHE B 1 76  ? 3.060   1.115   8.401   1.00 39.11 ? 76  PHE B CE1 1 
ATOM   4701 C CE2 . PHE B 1 76  ? 4.602   2.880   8.931   1.00 37.25 ? 76  PHE B CE2 1 
ATOM   4702 C CZ  . PHE B 1 76  ? 3.393   2.457   8.385   1.00 42.42 ? 76  PHE B CZ  1 
ATOM   4703 N N   . LEU B 1 77  ? 8.143   -2.818  10.250  1.00 20.69 ? 77  LEU B N   1 
ATOM   4704 C CA  . LEU B 1 77  ? 9.375   -3.349  10.817  1.00 21.97 ? 77  LEU B CA  1 
ATOM   4705 C C   . LEU B 1 77  ? 10.351  -3.770  9.723   1.00 24.49 ? 77  LEU B C   1 
ATOM   4706 O O   . LEU B 1 77  ? 11.568  -3.584  9.860   1.00 24.92 ? 77  LEU B O   1 
ATOM   4707 C CB  . LEU B 1 77  ? 9.040   -4.522  11.743  1.00 23.50 ? 77  LEU B CB  1 
ATOM   4708 C CG  . LEU B 1 77  ? 10.129  -4.978  12.708  1.00 31.58 ? 77  LEU B CG  1 
ATOM   4709 C CD1 . LEU B 1 77  ? 10.654  -3.800  13.562  1.00 28.32 ? 77  LEU B CD1 1 
ATOM   4710 C CD2 . LEU B 1 77  ? 9.582   -6.108  13.565  1.00 29.73 ? 77  LEU B CD2 1 
ATOM   4711 N N   . GLU B 1 78  ? 9.844   -4.348  8.631   1.00 21.67 ? 78  GLU B N   1 
ATOM   4712 C CA  . GLU B 1 78  ? 10.699  -4.645  7.480   1.00 23.98 ? 78  GLU B CA  1 
ATOM   4713 C C   . GLU B 1 78  ? 11.418  -3.400  6.978   1.00 23.00 ? 78  GLU B C   1 
ATOM   4714 O O   . GLU B 1 78  ? 12.590  -3.469  6.587   1.00 25.15 ? 78  GLU B O   1 
ATOM   4715 C CB  . GLU B 1 78  ? 9.865   -5.254  6.344   1.00 27.63 ? 78  GLU B CB  1 
ATOM   4716 C CG  . GLU B 1 78  ? 9.619   -6.743  6.468   1.00 37.55 ? 78  GLU B CG  1 
ATOM   4717 C CD  . GLU B 1 78  ? 8.639   -7.259  5.416   1.00 57.02 ? 78  GLU B CD  1 
ATOM   4718 O OE1 . GLU B 1 78  ? 8.142   -6.451  4.598   1.00 63.20 ? 78  GLU B OE1 1 
ATOM   4719 O OE2 . GLU B 1 78  ? 8.368   -8.475  5.409   1.00 63.24 ? 78  GLU B OE2 1 
ATOM   4720 N N   . ALA B 1 79  ? 10.731  -2.254  6.960   1.00 21.68 ? 79  ALA B N   1 
ATOM   4721 C CA  . ALA B 1 79  ? 11.366  -1.021  6.502   1.00 21.70 ? 79  ALA B CA  1 
ATOM   4722 C C   . ALA B 1 79  ? 12.444  -0.565  7.473   1.00 22.81 ? 79  ALA B C   1 
ATOM   4723 O O   . ALA B 1 79  ? 13.476  -0.029  7.053   1.00 27.98 ? 79  ALA B O   1 
ATOM   4724 C CB  . ALA B 1 79  ? 10.330  0.084   6.325   1.00 22.95 ? 79  ALA B CB  1 
ATOM   4725 N N   . ILE B 1 80  ? 12.218  -0.776  8.771   1.00 19.05 ? 80  ILE B N   1 
ATOM   4726 C CA  . ILE B 1 80  ? 13.242  -0.477  9.780   1.00 19.36 ? 80  ILE B CA  1 
ATOM   4727 C C   . ILE B 1 80  ? 14.455  -1.369  9.596   1.00 22.45 ? 80  ILE B C   1 
ATOM   4728 O O   . ILE B 1 80  ? 15.597  -0.907  9.654   1.00 24.91 ? 80  ILE B O   1 
ATOM   4729 C CB  . ILE B 1 80  ? 12.660  -0.640  11.197  1.00 17.47 ? 80  ILE B CB  1 
ATOM   4730 C CG1 . ILE B 1 80  ? 11.565  0.378   11.448  1.00 25.12 ? 80  ILE B CG1 1 
ATOM   4731 C CG2 . ILE B 1 80  ? 13.767  -0.563  12.270  1.00 20.55 ? 80  ILE B CG2 1 
ATOM   4732 C CD1 . ILE B 1 80  ? 12.025  1.786   11.413  1.00 25.08 ? 80  ILE B CD1 1 
ATOM   4733 N N   . ARG B 1 81  ? 14.225  -2.672  9.408   1.00 21.73 ? 81  ARG B N   1 
ATOM   4734 C CA  . ARG B 1 81  ? 15.326  -3.629  9.432   1.00 22.43 ? 81  ARG B CA  1 
ATOM   4735 C C   . ARG B 1 81  ? 16.253  -3.494  8.225   1.00 24.97 ? 81  ARG B C   1 
ATOM   4736 O O   . ARG B 1 81  ? 17.466  -3.740  8.345   1.00 25.01 ? 81  ARG B O   1 
ATOM   4737 C CB  . ARG B 1 81  ? 14.779  -5.056  9.517   1.00 29.26 ? 81  ARG B CB  1 
ATOM   4738 C CG  . ARG B 1 81  ? 15.869  -6.095  9.700   1.00 36.28 ? 81  ARG B CG  1 
ATOM   4739 C CD  . ARG B 1 81  ? 15.402  -7.493  9.365   1.00 41.34 ? 81  ARG B CD  1 
ATOM   4740 N NE  . ARG B 1 81  ? 14.208  -7.867  10.112  1.00 50.45 ? 81  ARG B NE  1 
ATOM   4741 C CZ  . ARG B 1 81  ? 14.218  -8.400  11.330  1.00 62.63 ? 81  ARG B CZ  1 
ATOM   4742 N NH1 . ARG B 1 81  ? 15.370  -8.623  11.953  1.00 61.92 ? 81  ARG B NH1 1 
ATOM   4743 N NH2 . ARG B 1 81  ? 13.071  -8.709  11.927  1.00 69.72 ? 81  ARG B NH2 1 
ATOM   4744 N N   . LYS B 1 82  ? 15.719  -3.103  7.064   1.00 22.75 ? 82  LYS B N   1 
ATOM   4745 C CA  . LYS B 1 82  ? 16.510  -3.089  5.836   1.00 25.66 ? 82  LYS B CA  1 
ATOM   4746 C C   . LYS B 1 82  ? 17.701  -2.137  5.922   1.00 22.37 ? 82  LYS B C   1 
ATOM   4747 O O   . LYS B 1 82  ? 17.642  -1.082  6.554   1.00 22.86 ? 82  LYS B O   1 
ATOM   4748 C CB  . LYS B 1 82  ? 15.646  -2.654  4.647   1.00 27.90 ? 82  LYS B CB  1 
ATOM   4749 C CG  . LYS B 1 82  ? 14.636  -3.636  4.167   1.00 33.55 ? 82  LYS B CG  1 
ATOM   4750 C CD  . LYS B 1 82  ? 13.784  -2.941  3.104   1.00 27.16 ? 82  LYS B CD  1 
ATOM   4751 C CE  . LYS B 1 82  ? 12.724  -3.842  2.547   1.00 38.11 ? 82  LYS B CE  1 
ATOM   4752 N NZ  . LYS B 1 82  ? 12.219  -3.225  1.301   1.00 40.33 ? 82  LYS B NZ  1 
ATOM   4753 N N   . ASP B 1 83  ? 18.766  -2.483  5.206   1.00 22.23 ? 83  ASP B N   1 
ATOM   4754 C CA  . ASP B 1 83  ? 19.786  -1.490  4.929   1.00 24.81 ? 83  ASP B CA  1 
ATOM   4755 C C   . ASP B 1 83  ? 19.136  -0.337  4.173   1.00 23.26 ? 83  ASP B C   1 
ATOM   4756 O O   . ASP B 1 83  ? 18.302  -0.576  3.289   1.00 23.06 ? 83  ASP B O   1 
ATOM   4757 C CB  . ASP B 1 83  ? 20.926  -2.102  4.109   1.00 27.25 ? 83  ASP B CB  1 
ATOM   4758 C CG  . ASP B 1 83  ? 22.102  -1.156  3.938   1.00 36.39 ? 83  ASP B CG  1 
ATOM   4759 O OD1 . ASP B 1 83  ? 21.937  -0.100  3.284   1.00 27.87 ? 83  ASP B OD1 1 
ATOM   4760 O OD2 . ASP B 1 83  ? 23.204  -1.469  4.458   1.00 38.63 ? 83  ASP B OD2 1 
ATOM   4761 N N   . PRO B 1 84  ? 19.457  0.916   4.507   1.00 22.06 ? 84  PRO B N   1 
ATOM   4762 C CA  . PRO B 1 84  ? 18.771  2.042   3.848   1.00 26.47 ? 84  PRO B CA  1 
ATOM   4763 C C   . PRO B 1 84  ? 18.947  2.077   2.343   1.00 28.76 ? 84  PRO B C   1 
ATOM   4764 O O   . PRO B 1 84  ? 18.058  2.587   1.638   1.00 30.92 ? 84  PRO B O   1 
ATOM   4765 C CB  . PRO B 1 84  ? 19.394  3.272   4.521   1.00 31.23 ? 84  PRO B CB  1 
ATOM   4766 C CG  . PRO B 1 84  ? 19.834  2.776   5.835   1.00 31.74 ? 84  PRO B CG  1 
ATOM   4767 C CD  . PRO B 1 84  ? 20.343  1.379   5.592   1.00 26.03 ? 84  PRO B CD  1 
ATOM   4768 N N   . ASP B 1 85  ? 20.055  1.544   1.813   1.00 24.19 ? 85  ASP B N   1 
ATOM   4769 C CA  . ASP B 1 85  ? 20.178  1.464   0.359   1.00 24.87 ? 85  ASP B CA  1 
ATOM   4770 C C   . ASP B 1 85  ? 19.102  0.585   -0.269  1.00 27.23 ? 85  ASP B C   1 
ATOM   4771 O O   . ASP B 1 85  ? 18.930  0.633   -1.488  1.00 25.73 ? 85  ASP B O   1 
ATOM   4772 C CB  . ASP B 1 85  ? 21.552  0.937   -0.059  1.00 28.70 ? 85  ASP B CB  1 
ATOM   4773 C CG  . ASP B 1 85  ? 22.665  1.930   0.222   1.00 38.48 ? 85  ASP B CG  1 
ATOM   4774 O OD1 . ASP B 1 85  ? 22.369  3.121   0.453   1.00 42.45 ? 85  ASP B OD1 1 
ATOM   4775 O OD2 . ASP B 1 85  ? 23.838  1.516   0.203   1.00 42.82 ? 85  ASP B OD2 1 
ATOM   4776 N N   . ASP B 1 86  ? 18.389  -0.208  0.529   1.00 25.80 ? 86  ASP B N   1 
ATOM   4777 C CA  . ASP B 1 86  ? 17.359  -1.108  0.038   1.00 26.19 ? 86  ASP B CA  1 
ATOM   4778 C C   . ASP B 1 86  ? 15.954  -0.587  0.293   1.00 24.80 ? 86  ASP B C   1 
ATOM   4779 O O   . ASP B 1 86  ? 14.978  -1.231  -0.117  1.00 25.47 ? 86  ASP B O   1 
ATOM   4780 C CB  . ASP B 1 86  ? 17.544  -2.485  0.679   1.00 28.15 ? 86  ASP B CB  1 
ATOM   4781 C CG  . ASP B 1 86  ? 18.799  -3.165  0.183   1.00 32.67 ? 86  ASP B CG  1 
ATOM   4782 O OD1 . ASP B 1 86  ? 19.132  -2.969  -1.005  1.00 45.59 ? 86  ASP B OD1 1 
ATOM   4783 O OD2 . ASP B 1 86  ? 19.458  -3.866  0.968   1.00 37.02 ? 86  ASP B OD2 1 
ATOM   4784 N N   . LEU B 1 87  ? 15.825  0.572   0.924   1.00 22.69 ? 87  LEU B N   1 
ATOM   4785 C CA  . LEU B 1 87  ? 14.508  1.133   1.189   1.00 22.25 ? 87  LEU B CA  1 
ATOM   4786 C C   . LEU B 1 87  ? 13.823  1.551   -0.101  1.00 23.72 ? 87  LEU B C   1 
ATOM   4787 O O   . LEU B 1 87  ? 14.415  2.238   -0.938  1.00 24.27 ? 87  LEU B O   1 
ATOM   4788 C CB  . LEU B 1 87  ? 14.620  2.345   2.095   1.00 21.80 ? 87  LEU B CB  1 
ATOM   4789 C CG  . LEU B 1 87  ? 14.771  1.985   3.565   1.00 20.66 ? 87  LEU B CG  1 
ATOM   4790 C CD1 . LEU B 1 87  ? 15.244  3.221   4.315   1.00 24.10 ? 87  LEU B CD1 1 
ATOM   4791 C CD2 . LEU B 1 87  ? 13.436  1.504   4.098   1.00 24.50 ? 87  LEU B CD2 1 
ATOM   4792 N N   . GLU B 1 88  ? 12.556  1.166   -0.222  1.00 25.51 ? 88  GLU B N   1 
ATOM   4793 C CA  . GLU B 1 88  ? 11.709  1.656   -1.295  1.00 24.26 ? 88  GLU B CA  1 
ATOM   4794 C C   . GLU B 1 88  ? 11.305  3.095   -1.014  1.00 24.34 ? 88  GLU B C   1 
ATOM   4795 O O   . GLU B 1 88  ? 11.241  3.520   0.144   1.00 23.41 ? 88  GLU B O   1 
ATOM   4796 C CB  . GLU B 1 88  ? 10.465  0.781   -1.411  1.00 27.14 ? 88  GLU B CB  1 
ATOM   4797 C CG  . GLU B 1 88  ? 10.779  -0.697  -1.569  1.00 28.57 ? 88  GLU B CG  1 
ATOM   4798 C CD  . GLU B 1 88  ? 9.603   -1.608  -1.246  1.00 36.19 ? 88  GLU B CD  1 
ATOM   4799 O OE1 . GLU B 1 88  ? 9.745   -2.827  -1.477  1.00 44.03 ? 88  GLU B OE1 1 
ATOM   4800 O OE2 . GLU B 1 88  ? 8.548   -1.120  -0.773  1.00 34.35 ? 88  GLU B OE2 1 
ATOM   4801 N N   . LYS B 1 89  ? 11.022  3.844   -2.089  1.00 25.63 ? 89  LYS B N   1 
ATOM   4802 C CA  . LYS B 1 89  ? 10.500  5.197   -1.930  1.00 26.03 ? 89  LYS B CA  1 
ATOM   4803 C C   . LYS B 1 89  ? 9.288   5.208   -1.010  1.00 29.94 ? 89  LYS B C   1 
ATOM   4804 O O   . LYS B 1 89  ? 9.167   6.073   -0.134  1.00 26.28 ? 89  LYS B O   1 
ATOM   4805 C CB  . LYS B 1 89  ? 10.139  5.788   -3.294  1.00 27.70 ? 89  LYS B CB  1 
ATOM   4806 C CG  . LYS B 1 89  ? 11.329  5.867   -4.240  1.00 28.61 ? 89  LYS B CG  1 
ATOM   4807 C CD  . LYS B 1 89  ? 10.935  6.246   -5.681  1.00 30.39 ? 89  LYS B CD  1 
ATOM   4808 C CE  . LYS B 1 89  ? 12.187  6.456   -6.558  1.00 32.99 ? 89  LYS B CE  1 
ATOM   4809 N NZ  . LYS B 1 89  ? 11.871  7.019   -7.912  1.00 38.22 ? 89  LYS B NZ  1 
ATOM   4810 N N   . GLU B 1 90  ? 8.402   4.224   -1.177  1.00 25.15 ? 90  GLU B N   1 
ATOM   4811 C CA  . GLU B 1 90  ? 7.205   4.119   -0.344  1.00 24.52 ? 90  GLU B CA  1 
ATOM   4812 C C   . GLU B 1 90  ? 7.559   3.887   1.125   1.00 24.87 ? 90  GLU B C   1 
ATOM   4813 O O   . GLU B 1 90  ? 6.838   4.343   2.026   1.00 27.73 ? 90  GLU B O   1 
ATOM   4814 C CB  . GLU B 1 90  ? 6.339   2.978   -0.873  1.00 37.60 ? 90  GLU B CB  1 
ATOM   4815 C CG  . GLU B 1 90  ? 4.880   3.025   -0.502  1.00 54.50 ? 90  GLU B CG  1 
ATOM   4816 C CD  . GLU B 1 90  ? 4.074   2.009   -1.297  1.00 63.85 ? 90  GLU B CD  1 
ATOM   4817 O OE1 . GLU B 1 90  ? 3.400   2.410   -2.273  1.00 70.95 ? 90  GLU B OE1 1 
ATOM   4818 O OE2 . GLU B 1 90  ? 4.132   0.807   -0.956  1.00 61.60 ? 90  GLU B OE2 1 
ATOM   4819 N N   . GLU B 1 91  ? 8.642   3.143   1.387   1.00 22.32 ? 91  GLU B N   1 
ATOM   4820 C CA  . GLU B 1 91  ? 9.035   2.853   2.762   1.00 24.10 ? 91  GLU B CA  1 
ATOM   4821 C C   . GLU B 1 91  ? 9.667   4.068   3.428   1.00 21.43 ? 91  GLU B C   1 
ATOM   4822 O O   . GLU B 1 91  ? 9.447   4.310   4.620   1.00 21.34 ? 91  GLU B O   1 
ATOM   4823 C CB  . GLU B 1 91  ? 9.995   1.667   2.790   1.00 24.46 ? 91  GLU B CB  1 
ATOM   4824 C CG  . GLU B 1 91  ? 9.339   0.329   2.527   1.00 25.19 ? 91  GLU B CG  1 
ATOM   4825 C CD  . GLU B 1 91  ? 10.337  -0.789  2.347   1.00 28.12 ? 91  GLU B CD  1 
ATOM   4826 O OE1 . GLU B 1 91  ? 11.344  -0.599  1.607   1.00 24.27 ? 91  GLU B OE1 1 
ATOM   4827 O OE2 . GLU B 1 91  ? 10.107  -1.862  2.940   1.00 27.82 ? 91  GLU B OE2 1 
ATOM   4828 N N   . VAL B 1 92  ? 10.445  4.853   2.675   1.00 21.79 ? 92  VAL B N   1 
ATOM   4829 C CA  . VAL B 1 92  ? 10.981  6.097   3.216   1.00 27.27 ? 92  VAL B CA  1 
ATOM   4830 C C   . VAL B 1 92  ? 9.847   7.044   3.575   1.00 23.29 ? 92  VAL B C   1 
ATOM   4831 O O   . VAL B 1 92  ? 9.857   7.677   4.641   1.00 23.42 ? 92  VAL B O   1 
ATOM   4832 C CB  . VAL B 1 92  ? 11.973  6.743   2.230   1.00 27.67 ? 92  VAL B CB  1 
ATOM   4833 C CG1 . VAL B 1 92  ? 12.467  8.077   2.777   1.00 28.32 ? 92  VAL B CG1 1 
ATOM   4834 C CG2 . VAL B 1 92  ? 13.162  5.825   1.973   1.00 22.95 ? 92  VAL B CG2 1 
ATOM   4835 N N   . GLU B 1 93  ? 8.830   7.132   2.712   1.00 23.27 ? 93  GLU B N   1 
ATOM   4836 C CA  . GLU B 1 93  ? 7.685   7.991   3.002   1.00 24.78 ? 93  GLU B CA  1 
ATOM   4837 C C   . GLU B 1 93  ? 6.979   7.563   4.280   1.00 26.80 ? 93  GLU B C   1 
ATOM   4838 O O   . GLU B 1 93  ? 6.609   8.409   5.105   1.00 27.02 ? 93  GLU B O   1 
ATOM   4839 C CB  . GLU B 1 93  ? 6.703   7.980   1.823   1.00 30.81 ? 93  GLU B CB  1 
ATOM   4840 C CG  . GLU B 1 93  ? 7.247   8.661   0.574   1.00 36.85 ? 93  GLU B CG  1 
ATOM   4841 C CD  . GLU B 1 93  ? 6.506   8.254   -0.707  1.00 39.77 ? 93  GLU B CD  1 
ATOM   4842 O OE1 . GLU B 1 93  ? 5.498   7.523   -0.616  1.00 40.74 ? 93  GLU B OE1 1 
ATOM   4843 O OE2 . GLU B 1 93  ? 6.941   8.656   -1.805  1.00 41.00 ? 93  GLU B OE2 1 
ATOM   4844 N N   . LYS B 1 94  ? 6.760   6.252   4.453   1.00 22.67 ? 94  LYS B N   1 
ATOM   4845 C CA  . LYS B 1 94  ? 6.051   5.763   5.625   1.00 24.63 ? 94  LYS B CA  1 
ATOM   4846 C C   . LYS B 1 94  ? 6.855   6.004   6.894   1.00 22.56 ? 94  LYS B C   1 
ATOM   4847 O O   . LYS B 1 94  ? 6.285   6.301   7.951   1.00 26.12 ? 94  LYS B O   1 
ATOM   4848 C CB  . LYS B 1 94  ? 5.740   4.271   5.480   1.00 33.18 ? 94  LYS B CB  1 
ATOM   4849 C CG  . LYS B 1 94  ? 4.266   4.000   5.208   1.00 49.34 ? 94  LYS B CG  1 
ATOM   4850 C CD  . LYS B 1 94  ? 4.047   2.890   4.188   1.00 56.23 ? 94  LYS B CD  1 
ATOM   4851 C CE  . LYS B 1 94  ? 2.557   2.732   3.873   1.00 62.41 ? 94  LYS B CE  1 
ATOM   4852 N NZ  . LYS B 1 94  ? 1.773   2.275   5.066   1.00 64.86 ? 94  LYS B NZ  1 
ATOM   4853 N N   . LEU B 1 95  ? 8.175   5.859   6.807   1.00 19.36 ? 95  LEU B N   1 
ATOM   4854 C CA  . LEU B 1 95  ? 9.031   6.073   7.972   1.00 21.68 ? 95  LEU B CA  1 
ATOM   4855 C C   . LEU B 1 95  ? 9.003   7.534   8.405   1.00 25.62 ? 95  LEU B C   1 
ATOM   4856 O O   . LEU B 1 95  ? 8.957   7.834   9.607   1.00 22.68 ? 95  LEU B O   1 
ATOM   4857 C CB  . LEU B 1 95  ? 10.451  5.626   7.637   1.00 21.72 ? 95  LEU B CB  1 
ATOM   4858 C CG  . LEU B 1 95  ? 11.536  5.757   8.701   1.00 37.55 ? 95  LEU B CG  1 
ATOM   4859 C CD1 . LEU B 1 95  ? 11.185  4.898   9.900   1.00 38.67 ? 95  LEU B CD1 1 
ATOM   4860 C CD2 . LEU B 1 95  ? 12.887  5.366   8.116   1.00 43.58 ? 95  LEU B CD2 1 
ATOM   4861 N N   . ILE B 1 96  ? 9.003   8.455   7.437   1.00 21.77 ? 96  ILE B N   1 
ATOM   4862 C CA  . ILE B 1 96  ? 8.884   9.869   7.772   1.00 22.39 ? 96  ILE B CA  1 
ATOM   4863 C C   . ILE B 1 96  ? 7.513   10.159  8.374   1.00 24.59 ? 96  ILE B C   1 
ATOM   4864 O O   . ILE B 1 96  ? 7.398   10.867  9.380   1.00 23.73 ? 96  ILE B O   1 
ATOM   4865 C CB  . ILE B 1 96  ? 9.169   10.735  6.531   1.00 25.28 ? 96  ILE B CB  1 
ATOM   4866 C CG1 . ILE B 1 96  ? 10.658  10.673  6.167   1.00 27.13 ? 96  ILE B CG1 1 
ATOM   4867 C CG2 . ILE B 1 96  ? 8.712   12.180  6.759   1.00 26.40 ? 96  ILE B CG2 1 
ATOM   4868 C CD1 . ILE B 1 96  ? 11.018  11.320  4.833   1.00 27.34 ? 96  ILE B CD1 1 
ATOM   4869 N N   . GLU B 1 97  ? 6.451   9.617   7.773   1.00 22.15 ? 97  GLU B N   1 
ATOM   4870 C CA  . GLU B 1 97  ? 5.116   9.834   8.323   1.00 26.99 ? 97  GLU B CA  1 
ATOM   4871 C C   . GLU B 1 97  ? 5.006   9.282   9.746   1.00 23.26 ? 97  GLU B C   1 
ATOM   4872 O O   . GLU B 1 97  ? 4.398   9.914   10.619  1.00 25.33 ? 97  GLU B O   1 
ATOM   4873 C CB  . GLU B 1 97  ? 4.067   9.190   7.413   1.00 31.83 ? 97  GLU B CB  1 
ATOM   4874 C CG  . GLU B 1 97  ? 2.647   9.272   7.955   1.00 46.89 ? 97  GLU B CG  1 
ATOM   4875 C CD  . GLU B 1 97  ? 1.603   8.735   6.980   1.00 63.16 ? 97  GLU B CD  1 
ATOM   4876 O OE1 . GLU B 1 97  ? 1.973   7.968   6.062   1.00 67.47 ? 97  GLU B OE1 1 
ATOM   4877 O OE2 . GLU B 1 97  ? 0.409   9.080   7.136   1.00 67.31 ? 97  GLU B OE2 1 
ATOM   4878 N N   . PHE B 1 98  ? 5.586   8.100   9.996   1.00 20.99 ? 98  PHE B N   1 
ATOM   4879 C CA  . PHE B 1 98  ? 5.556   7.511   11.330  1.00 20.48 ? 98  PHE B CA  1 
ATOM   4880 C C   . PHE B 1 98  ? 6.338   8.368   12.326  1.00 23.94 ? 98  PHE B C   1 
ATOM   4881 O O   . PHE B 1 98  ? 5.903   8.565   13.470  1.00 20.98 ? 98  PHE B O   1 
ATOM   4882 C CB  . PHE B 1 98  ? 6.113   6.086   11.268  1.00 19.77 ? 98  PHE B CB  1 
ATOM   4883 C CG  . PHE B 1 98  ? 5.884   5.275   12.518  1.00 21.49 ? 98  PHE B CG  1 
ATOM   4884 C CD1 . PHE B 1 98  ? 4.647   4.680   12.757  1.00 24.17 ? 98  PHE B CD1 1 
ATOM   4885 C CD2 . PHE B 1 98  ? 6.888   5.124   13.460  1.00 19.26 ? 98  PHE B CD2 1 
ATOM   4886 C CE1 . PHE B 1 98  ? 4.422   3.940   13.899  1.00 19.22 ? 98  PHE B CE1 1 
ATOM   4887 C CE2 . PHE B 1 98  ? 6.665   4.385   14.634  1.00 22.36 ? 98  PHE B CE2 1 
ATOM   4888 C CZ  . PHE B 1 98  ? 5.440   3.794   14.851  1.00 21.66 ? 98  PHE B CZ  1 
ATOM   4889 N N   . THR B 1 99  ? 7.490   8.894   11.903  1.00 24.13 ? 99  THR B N   1 
ATOM   4890 C CA  . THR B 1 99  ? 8.251   9.804   12.756  1.00 22.97 ? 99  THR B CA  1 
ATOM   4891 C C   . THR B 1 99  ? 7.438   11.049  13.090  1.00 24.80 ? 99  THR B C   1 
ATOM   4892 O O   . THR B 1 99  ? 7.367   11.466  14.254  1.00 25.77 ? 99  THR B O   1 
ATOM   4893 C CB  . THR B 1 99  ? 9.563   10.180  12.068  1.00 23.46 ? 99  THR B CB  1 
ATOM   4894 O OG1 . THR B 1 99  ? 10.263  8.980   11.720  1.00 20.00 ? 99  THR B OG1 1 
ATOM   4895 C CG2 . THR B 1 99  ? 10.442  11.026  12.985  1.00 26.80 ? 99  THR B CG2 1 
ATOM   4896 N N   . LYS B 1 100 ? 6.808   11.655  12.076  1.00 23.30 ? 100 LYS B N   1 
ATOM   4897 C CA  . LYS B 1 100 ? 6.044   12.878  12.309  1.00 25.65 ? 100 LYS B CA  1 
ATOM   4898 C C   . LYS B 1 100 ? 4.870   12.656  13.263  1.00 25.98 ? 100 LYS B C   1 
ATOM   4899 O O   . LYS B 1 100 ? 4.504   13.562  14.026  1.00 30.48 ? 100 LYS B O   1 
ATOM   4900 C CB  . LYS B 1 100 ? 5.537   13.431  10.978  1.00 25.55 ? 100 LYS B CB  1 
ATOM   4901 C CG  . LYS B 1 100 ? 6.508   14.362  10.290  1.00 38.30 ? 100 LYS B CG  1 
ATOM   4902 C CD  . LYS B 1 100 ? 6.143   14.540  8.822   1.00 46.10 ? 100 LYS B CD  1 
ATOM   4903 C CE  . LYS B 1 100 ? 7.149   15.407  8.095   1.00 49.81 ? 100 LYS B CE  1 
ATOM   4904 N NZ  . LYS B 1 100 ? 6.708   15.659  6.692   1.00 54.77 ? 100 LYS B NZ  1 
ATOM   4905 N N   . LEU B 1 101 ? 4.250   11.477  13.219  1.00 23.69 ? 101 LEU B N   1 
ATOM   4906 C CA  . LEU B 1 101 ? 3.133   11.202  14.113  1.00 22.45 ? 101 LEU B CA  1 
ATOM   4907 C C   . LEU B 1 101 ? 3.580   11.146  15.573  1.00 23.07 ? 101 LEU B C   1 
ATOM   4908 O O   . LEU B 1 101 ? 2.820   11.537  16.466  1.00 25.39 ? 101 LEU B O   1 
ATOM   4909 C CB  . LEU B 1 101 ? 2.475   9.877   13.722  1.00 26.66 ? 101 LEU B CB  1 
ATOM   4910 C CG  . LEU B 1 101 ? 1.371   9.334   14.618  1.00 27.39 ? 101 LEU B CG  1 
ATOM   4911 C CD1 . LEU B 1 101 ? 0.132   10.216  14.525  1.00 29.70 ? 101 LEU B CD1 1 
ATOM   4912 C CD2 . LEU B 1 101 ? 1.033   7.882   14.278  1.00 28.02 ? 101 LEU B CD2 1 
ATOM   4913 N N   . ASN B 1 102 ? 4.801   10.676  15.822  1.00 22.18 ? 102 ASN B N   1 
ATOM   4914 C CA  . ASN B 1 102 ? 5.317   10.411  17.163  1.00 23.32 ? 102 ASN B CA  1 
ATOM   4915 C C   . ASN B 1 102 ? 6.247   11.495  17.680  1.00 25.31 ? 102 ASN B C   1 
ATOM   4916 O O   . ASN B 1 102 ? 6.591   11.498  18.871  1.00 22.33 ? 102 ASN B O   1 
ATOM   4917 C CB  . ASN B 1 102 ? 6.047   9.078   17.144  1.00 21.08 ? 102 ASN B CB  1 
ATOM   4918 C CG  . ASN B 1 102 ? 5.091   7.913   16.998  1.00 24.88 ? 102 ASN B CG  1 
ATOM   4919 O OD1 . ASN B 1 102 ? 4.270   7.667   17.879  1.00 24.12 ? 102 ASN B OD1 1 
ATOM   4920 N ND2 . ASN B 1 102 ? 5.179   7.203   15.885  1.00 23.57 ? 102 ASN B ND2 1 
ATOM   4921 N N   . TYR B 1 103 ? 6.572   12.444  16.815  1.00 26.43 ? 103 TYR B N   1 
ATOM   4922 C CA  . TYR B 1 103 ? 7.675   13.377  16.980  1.00 34.31 ? 103 TYR B CA  1 
ATOM   4923 C C   . TYR B 1 103 ? 7.646   14.133  18.315  1.00 28.23 ? 103 TYR B C   1 
ATOM   4924 O O   . TYR B 1 103 ? 8.696   14.443  18.898  1.00 26.74 ? 103 TYR B O   1 
ATOM   4925 C CB  . TYR B 1 103 ? 7.569   14.313  15.786  1.00 41.81 ? 103 TYR B CB  1 
ATOM   4926 C CG  . TYR B 1 103 ? 8.489   15.421  15.772  1.00 48.66 ? 103 TYR B CG  1 
ATOM   4927 C CD1 . TYR B 1 103 ? 9.731   15.277  15.200  1.00 56.35 ? 103 TYR B CD1 1 
ATOM   4928 C CD2 . TYR B 1 103 ? 8.114   16.637  16.291  1.00 55.65 ? 103 TYR B CD2 1 
ATOM   4929 C CE1 . TYR B 1 103 ? 10.593  16.318  15.169  1.00 63.72 ? 103 TYR B CE1 1 
ATOM   4930 C CE2 . TYR B 1 103 ? 8.957   17.678  16.269  1.00 62.00 ? 103 TYR B CE2 1 
ATOM   4931 C CZ  . TYR B 1 103 ? 10.190  17.516  15.708  1.00 68.31 ? 103 TYR B CZ  1 
ATOM   4932 O OH  . TYR B 1 103 ? 11.008  18.594  15.704  1.00 74.49 ? 103 TYR B OH  1 
ATOM   4933 N N   . GLU B 1 104 ? 6.460   14.444  18.808  1.00 29.91 ? 104 GLU B N   1 
ATOM   4934 C CA  . GLU B 1 104 ? 6.309   15.324  19.956  1.00 33.84 ? 104 GLU B CA  1 
ATOM   4935 C C   . GLU B 1 104 ? 6.262   14.575  21.280  1.00 30.71 ? 104 GLU B C   1 
ATOM   4936 O O   . GLU B 1 104 ? 6.207   15.213  22.332  1.00 32.32 ? 104 GLU B O   1 
ATOM   4937 C CB  . GLU B 1 104 ? 5.047   16.189  19.787  1.00 46.06 ? 104 GLU B CB  1 
ATOM   4938 C CG  . GLU B 1 104 ? 3.742   15.405  19.713  1.00 62.24 ? 104 GLU B CG  1 
ATOM   4939 C CD  . GLU B 1 104 ? 3.634   14.509  18.479  1.00 69.06 ? 104 GLU B CD  1 
ATOM   4940 O OE1 . GLU B 1 104 ? 3.566   13.273  18.644  1.00 68.11 ? 104 GLU B OE1 1 
ATOM   4941 O OE2 . GLU B 1 104 ? 3.621   15.039  17.347  1.00 73.08 ? 104 GLU B OE2 1 
ATOM   4942 N N   . LYS B 1 105 ? 6.302   13.265  21.258  1.00 25.80 ? 105 LYS B N   1 
ATOM   4943 C CA  . LYS B 1 105 ? 6.251   12.460  22.472  1.00 19.64 ? 105 LYS B CA  1 
ATOM   4944 C C   . LYS B 1 105 ? 7.607   12.472  23.175  1.00 20.04 ? 105 LYS B C   1 
ATOM   4945 O O   . LYS B 1 105 ? 8.654   12.489  22.511  1.00 20.13 ? 105 LYS B O   1 
ATOM   4946 C CB  . LYS B 1 105 ? 5.850   11.019  22.142  1.00 18.07 ? 105 LYS B CB  1 
ATOM   4947 C CG  . LYS B 1 105 ? 4.467   10.937  21.497  1.00 18.03 ? 105 LYS B CG  1 
ATOM   4948 C CD  . LYS B 1 105 ? 4.165   9.548   20.955  1.00 20.87 ? 105 LYS B CD  1 
ATOM   4949 C CE  . LYS B 1 105 ? 2.781   9.514   20.279  1.00 21.11 ? 105 LYS B CE  1 
ATOM   4950 N NZ  . LYS B 1 105 ? 2.477   8.109   19.898  1.00 16.10 ? 105 LYS B NZ  1 
ATOM   4951 N N   . PRO B 1 106 ? 7.617   12.478  24.510  1.00 19.89 ? 106 PRO B N   1 
ATOM   4952 C CA  . PRO B 1 106 ? 8.903   12.484  25.231  1.00 24.27 ? 106 PRO B CA  1 
ATOM   4953 C C   . PRO B 1 106 ? 9.807   11.301  24.920  1.00 21.01 ? 106 PRO B C   1 
ATOM   4954 O O   . PRO B 1 106 ? 11.037  11.453  24.971  1.00 25.83 ? 106 PRO B O   1 
ATOM   4955 C CB  . PRO B 1 106 ? 8.473   12.492  26.706  1.00 25.74 ? 106 PRO B CB  1 
ATOM   4956 C CG  . PRO B 1 106 ? 7.109   13.117  26.690  1.00 25.82 ? 106 PRO B CG  1 
ATOM   4957 C CD  . PRO B 1 106 ? 6.473   12.576  25.432  1.00 19.93 ? 106 PRO B CD  1 
ATOM   4958 N N   . ILE B 1 107 ? 9.263   10.123  24.593  1.00 18.95 ? 107 ILE B N   1 
ATOM   4959 C CA  . ILE B 1 107 ? 10.133  9.013   24.225  1.00 20.51 ? 107 ILE B CA  1 
ATOM   4960 C C   . ILE B 1 107 ? 10.810  9.225   22.878  1.00 21.66 ? 107 ILE B C   1 
ATOM   4961 O O   . ILE B 1 107 ? 11.735  8.479   22.541  1.00 25.28 ? 107 ILE B O   1 
ATOM   4962 C CB  . ILE B 1 107 ? 9.366   7.674   24.236  1.00 23.44 ? 107 ILE B CB  1 
ATOM   4963 C CG1 . ILE B 1 107 ? 8.239   7.659   23.198  1.00 20.60 ? 107 ILE B CG1 1 
ATOM   4964 C CG2 . ILE B 1 107 ? 8.804   7.400   25.620  1.00 24.85 ? 107 ILE B CG2 1 
ATOM   4965 C CD1 . ILE B 1 107 ? 7.700   6.261   22.926  1.00 18.80 ? 107 ILE B CD1 1 
ATOM   4966 N N   . TYR B 1 108 ? 10.380  10.223  22.100  1.00 21.14 ? 108 TYR B N   1 
ATOM   4967 C CA  . TYR B 1 108 ? 11.038  10.598  20.848  1.00 21.26 ? 108 TYR B CA  1 
ATOM   4968 C C   . TYR B 1 108 ? 11.940  11.811  21.004  1.00 25.05 ? 108 TYR B C   1 
ATOM   4969 O O   . TYR B 1 108 ? 12.409  12.356  20.000  1.00 28.48 ? 108 TYR B O   1 
ATOM   4970 C CB  . TYR B 1 108 ? 9.998   10.865  19.744  1.00 21.11 ? 108 TYR B CB  1 
ATOM   4971 C CG  . TYR B 1 108 ? 9.634   9.628   18.935  1.00 21.32 ? 108 TYR B CG  1 
ATOM   4972 C CD1 . TYR B 1 108 ? 8.828   8.625   19.473  1.00 18.04 ? 108 TYR B CD1 1 
ATOM   4973 C CD2 . TYR B 1 108 ? 10.104  9.461   17.635  1.00 20.33 ? 108 TYR B CD2 1 
ATOM   4974 C CE1 . TYR B 1 108 ? 8.504   7.487   18.745  1.00 22.82 ? 108 TYR B CE1 1 
ATOM   4975 C CE2 . TYR B 1 108 ? 9.789   8.344   16.916  1.00 20.24 ? 108 TYR B CE2 1 
ATOM   4976 C CZ  . TYR B 1 108 ? 8.987   7.354   17.468  1.00 21.11 ? 108 TYR B CZ  1 
ATOM   4977 O OH  . TYR B 1 108 ? 8.662   6.239   16.723  1.00 20.70 ? 108 TYR B OH  1 
ATOM   4978 N N   . ARG B 1 109 ? 12.220  12.232  22.237  1.00 26.75 ? 109 ARG B N   1 
ATOM   4979 C CA  . ARG B 1 109 ? 12.994  13.448  22.468  1.00 31.70 ? 109 ARG B CA  1 
ATOM   4980 C C   . ARG B 1 109 ? 14.471  13.190  22.167  1.00 35.04 ? 109 ARG B C   1 
ATOM   4981 O O   . ARG B 1 109 ? 15.313  13.054  23.058  1.00 37.55 ? 109 ARG B O   1 
ATOM   4982 C CB  . ARG B 1 109 ? 12.810  13.951  23.894  1.00 32.67 ? 109 ARG B CB  1 
ATOM   4983 C CG  . ARG B 1 109 ? 13.115  15.428  24.036  1.00 45.76 ? 109 ARG B CG  1 
ATOM   4984 C CD  . ARG B 1 109 ? 11.896  16.155  24.565  1.00 57.73 ? 109 ARG B CD  1 
ATOM   4985 N NE  . ARG B 1 109 ? 11.671  15.832  25.967  1.00 59.20 ? 109 ARG B NE  1 
ATOM   4986 C CZ  . ARG B 1 109 ? 10.497  15.931  26.579  1.00 64.89 ? 109 ARG B CZ  1 
ATOM   4987 N NH1 . ARG B 1 109 ? 9.427   16.335  25.906  1.00 64.92 ? 109 ARG B NH1 1 
ATOM   4988 N NH2 . ARG B 1 109 ? 10.391  15.623  27.858  1.00 68.86 ? 109 ARG B NH2 1 
ATOM   4989 N N   . PHE B 1 110 ? 14.784  13.146  20.876  1.00 26.76 ? 110 PHE B N   1 
ATOM   4990 C CA  . PHE B 1 110 ? 16.155  13.096  20.383  1.00 31.74 ? 110 PHE B CA  1 
ATOM   4991 C C   . PHE B 1 110 ? 16.385  14.304  19.493  1.00 30.23 ? 110 PHE B C   1 
ATOM   4992 O O   . PHE B 1 110 ? 15.667  14.493  18.503  1.00 32.95 ? 110 PHE B O   1 
ATOM   4993 C CB  . PHE B 1 110 ? 16.411  11.818  19.582  1.00 36.78 ? 110 PHE B CB  1 
ATOM   4994 C CG  . PHE B 1 110 ? 16.258  10.564  20.369  1.00 32.09 ? 110 PHE B CG  1 
ATOM   4995 C CD1 . PHE B 1 110 ? 17.305  10.082  21.127  1.00 32.35 ? 110 PHE B CD1 1 
ATOM   4996 C CD2 . PHE B 1 110 ? 15.073  9.846   20.331  1.00 34.20 ? 110 PHE B CD2 1 
ATOM   4997 C CE1 . PHE B 1 110 ? 17.166  8.914   21.849  1.00 33.67 ? 110 PHE B CE1 1 
ATOM   4998 C CE2 . PHE B 1 110 ? 14.927  8.674   21.050  1.00 30.92 ? 110 PHE B CE2 1 
ATOM   4999 C CZ  . PHE B 1 110 ? 15.973  8.206   21.810  1.00 32.59 ? 110 PHE B CZ  1 
ATOM   5000 N N   . GLU B 1 111 ? 17.403  15.103  19.819  1.00 33.49 ? 111 GLU B N   1 
ATOM   5001 C CA  . GLU B 1 111 ? 17.734  16.247  18.981  1.00 36.40 ? 111 GLU B CA  1 
ATOM   5002 C C   . GLU B 1 111 ? 17.993  15.829  17.540  1.00 35.26 ? 111 GLU B C   1 
ATOM   5003 O O   . GLU B 1 111 ? 17.672  16.576  16.611  1.00 35.85 ? 111 GLU B O   1 
ATOM   5004 C CB  . GLU B 1 111 ? 18.952  16.982  19.552  1.00 43.76 ? 111 GLU B CB  1 
ATOM   5005 C CG  . GLU B 1 111 ? 19.982  16.069  20.217  1.00 56.19 ? 111 GLU B CG  1 
ATOM   5006 C CD  . GLU B 1 111 ? 19.666  15.758  21.675  1.00 64.20 ? 111 GLU B CD  1 
ATOM   5007 O OE1 . GLU B 1 111 ? 18.638  15.095  21.942  1.00 61.61 ? 111 GLU B OE1 1 
ATOM   5008 O OE2 . GLU B 1 111 ? 20.452  16.182  22.554  1.00 70.48 ? 111 GLU B OE2 1 
ATOM   5009 N N   . ARG B 1 112 ? 18.560  14.637  17.332  1.00 33.09 ? 112 ARG B N   1 
ATOM   5010 C CA  . ARG B 1 112 ? 18.795  14.162  15.973  1.00 33.76 ? 112 ARG B CA  1 
ATOM   5011 C C   . ARG B 1 112 ? 17.493  13.995  15.196  1.00 29.24 ? 112 ARG B C   1 
ATOM   5012 O O   . ARG B 1 112 ? 17.470  14.203  13.977  1.00 36.05 ? 112 ARG B O   1 
ATOM   5013 C CB  . ARG B 1 112 ? 19.574  12.841  16.004  1.00 33.78 ? 112 ARG B CB  1 
ATOM   5014 C CG  . ARG B 1 112 ? 19.816  12.225  14.632  1.00 35.11 ? 112 ARG B CG  1 
ATOM   5015 C CD  . ARG B 1 112 ? 20.769  13.069  13.804  1.00 37.49 ? 112 ARG B CD  1 
ATOM   5016 N NE  . ARG B 1 112 ? 21.384  12.278  12.744  1.00 38.72 ? 112 ARG B NE  1 
ATOM   5017 C CZ  . ARG B 1 112 ? 22.005  12.788  11.687  1.00 40.61 ? 112 ARG B CZ  1 
ATOM   5018 N NH1 . ARG B 1 112 ? 22.084  14.107  11.535  1.00 40.55 ? 112 ARG B NH1 1 
ATOM   5019 N NH2 . ARG B 1 112 ? 22.538  11.978  10.775  1.00 36.95 ? 112 ARG B NH2 1 
ATOM   5020 N N   . ILE B 1 113 ? 16.397  13.628  15.874  1.00 29.64 ? 113 ILE B N   1 
ATOM   5021 C CA  . ILE B 1 113 ? 15.127  13.472  15.160  1.00 31.54 ? 113 ILE B CA  1 
ATOM   5022 C C   . ILE B 1 113 ? 14.661  14.811  14.596  1.00 35.27 ? 113 ILE B C   1 
ATOM   5023 O O   . ILE B 1 113 ? 14.186  14.886  13.456  1.00 35.59 ? 113 ILE B O   1 
ATOM   5024 C CB  . ILE B 1 113 ? 14.058  12.831  16.067  1.00 31.46 ? 113 ILE B CB  1 
ATOM   5025 C CG1 . ILE B 1 113 ? 14.405  11.371  16.332  1.00 31.10 ? 113 ILE B CG1 1 
ATOM   5026 C CG2 . ILE B 1 113 ? 12.685  12.893  15.399  1.00 33.33 ? 113 ILE B CG2 1 
ATOM   5027 C CD1 . ILE B 1 113 ? 13.430  10.662  17.205  1.00 34.60 ? 113 ILE B CD1 1 
ATOM   5028 N N   . ARG B 1 114 ? 14.809  15.895  15.368  1.00 34.29 ? 114 ARG B N   1 
ATOM   5029 C CA  . ARG B 1 114 ? 14.400  17.205  14.863  1.00 40.42 ? 114 ARG B CA  1 
ATOM   5030 C C   . ARG B 1 114 ? 15.283  17.654  13.708  1.00 42.14 ? 114 ARG B C   1 
ATOM   5031 O O   . ARG B 1 114 ? 14.810  18.336  12.792  1.00 45.42 ? 114 ARG B O   1 
ATOM   5032 C CB  . ARG B 1 114 ? 14.420  18.242  15.997  1.00 49.93 ? 114 ARG B CB  1 
ATOM   5033 C CG  . ARG B 1 114 ? 14.473  19.740  15.566  1.00 63.78 ? 114 ARG B CG  1 
ATOM   5034 C CD  . ARG B 1 114 ? 13.082  20.341  15.605  1.00 71.65 ? 114 ARG B CD  1 
ATOM   5035 N NE  . ARG B 1 114 ? 12.936  21.802  15.454  1.00 77.27 ? 114 ARG B NE  1 
ATOM   5036 C CZ  . ARG B 1 114 ? 12.101  22.532  16.200  1.00 80.80 ? 114 ARG B CZ  1 
ATOM   5037 N NH1 . ARG B 1 114 ? 11.353  21.935  17.130  1.00 78.77 ? 114 ARG B NH1 1 
ATOM   5038 N NH2 . ARG B 1 114 ? 11.992  23.836  16.020  1.00 85.07 ? 114 ARG B NH2 1 
ATOM   5039 N N   . GLU B 1 115 ? 16.558  17.272  13.719  1.00 43.49 ? 115 GLU B N   1 
ATOM   5040 C CA  . GLU B 1 115 ? 17.421  17.572  12.582  1.00 49.50 ? 115 GLU B CA  1 
ATOM   5041 C C   . GLU B 1 115 ? 16.953  16.837  11.334  1.00 44.04 ? 115 GLU B C   1 
ATOM   5042 O O   . GLU B 1 115 ? 16.816  17.439  10.264  1.00 45.24 ? 115 GLU B O   1 
ATOM   5043 C CB  . GLU B 1 115 ? 18.866  17.192  12.896  1.00 54.43 ? 115 GLU B CB  1 
ATOM   5044 C CG  . GLU B 1 115 ? 19.429  17.774  14.168  1.00 60.44 ? 115 GLU B CG  1 
ATOM   5045 C CD  . GLU B 1 115 ? 20.846  17.302  14.423  1.00 66.45 ? 115 GLU B CD  1 
ATOM   5046 O OE1 . GLU B 1 115 ? 21.387  16.559  13.572  1.00 67.98 ? 115 GLU B OE1 1 
ATOM   5047 O OE2 . GLU B 1 115 ? 21.424  17.677  15.465  1.00 69.71 ? 115 GLU B OE2 1 
ATOM   5048 N N   . LEU B 1 116 ? 16.727  15.525  11.452  1.00 39.88 ? 116 LEU B N   1 
ATOM   5049 C CA  . LEU B 1 116 ? 16.359  14.715  10.294  1.00 39.11 ? 116 LEU B CA  1 
ATOM   5050 C C   . LEU B 1 116 ? 15.043  15.179  9.683   1.00 41.33 ? 116 LEU B C   1 
ATOM   5051 O O   . LEU B 1 116 ? 14.868  15.130  8.461   1.00 44.37 ? 116 LEU B O   1 
ATOM   5052 C CB  . LEU B 1 116 ? 16.268  13.240  10.698  1.00 39.08 ? 116 LEU B CB  1 
ATOM   5053 C CG  . LEU B 1 116 ? 17.530  12.558  11.237  1.00 36.92 ? 116 LEU B CG  1 
ATOM   5054 C CD1 . LEU B 1 116 ? 17.229  11.110  11.640  1.00 34.67 ? 116 LEU B CD1 1 
ATOM   5055 C CD2 . LEU B 1 116 ? 18.642  12.604  10.207  1.00 38.56 ? 116 LEU B CD2 1 
ATOM   5056 N N   . MET B 1 117 ? 14.098  15.620  10.519  1.00 41.43 ? 117 MET B N   1 
ATOM   5057 C CA  . MET B 1 117 ? 12.829  16.132  10.009  1.00 45.51 ? 117 MET B CA  1 
ATOM   5058 C C   . MET B 1 117 ? 12.975  17.495  9.344   1.00 49.31 ? 117 MET B C   1 
ATOM   5059 O O   . MET B 1 117 ? 12.065  17.910  8.620   1.00 54.89 ? 117 MET B O   1 
ATOM   5060 C CB  . MET B 1 117 ? 11.793  16.221  11.133  1.00 43.76 ? 117 MET B CB  1 
ATOM   5061 C CG  . MET B 1 117 ? 11.377  14.864  11.679  1.00 49.19 ? 117 MET B CG  1 
ATOM   5062 S SD  . MET B 1 117 ? 11.433  13.581  10.400  1.00 57.18 ? 117 MET B SD  1 
ATOM   5063 C CE  . MET B 1 117 ? 9.704   13.286  10.118  1.00 47.57 ? 117 MET B CE  1 
ATOM   5064 N N   . ASN B 1 118 ? 14.085  18.199  9.582   1.00 51.74 ? 118 ASN B N   1 
ATOM   5065 C CA  . ASN B 1 118 ? 14.360  19.462  8.905   1.00 60.86 ? 118 ASN B CA  1 
ATOM   5066 C C   . ASN B 1 118 ? 15.009  19.270  7.543   1.00 61.90 ? 118 ASN B C   1 
ATOM   5067 O O   . ASN B 1 118 ? 14.917  20.164  6.695   1.00 63.35 ? 118 ASN B O   1 
ATOM   5068 C CB  . ASN B 1 118 ? 15.282  20.340  9.756   1.00 68.89 ? 118 ASN B CB  1 
ATOM   5069 C CG  . ASN B 1 118 ? 14.548  21.072  10.855  1.00 74.03 ? 118 ASN B CG  1 
ATOM   5070 O OD1 . ASN B 1 118 ? 13.324  21.201  10.823  1.00 76.10 ? 118 ASN B OD1 1 
ATOM   5071 N ND2 . ASN B 1 118 ? 15.297  21.564  11.838  1.00 76.28 ? 118 ASN B ND2 1 
ATOM   5072 N N   . LYS B 1 119 ? 15.672  18.141  7.320   1.00 60.46 ? 119 LYS B N   1 
ATOM   5073 C CA  . LYS B 1 119 ? 16.426  17.940  6.094   1.00 59.49 ? 119 LYS B CA  1 
ATOM   5074 C C   . LYS B 1 119 ? 15.486  17.634  4.936   1.00 60.55 ? 119 LYS B C   1 
ATOM   5075 O O   . LYS B 1 119 ? 14.468  16.956  5.102   1.00 57.21 ? 119 LYS B O   1 
ATOM   5076 C CB  . LYS B 1 119 ? 17.442  16.813  6.277   1.00 58.07 ? 119 LYS B CB  1 
ATOM   5077 C CG  . LYS B 1 119 ? 18.339  17.020  7.478   1.00 57.88 ? 119 LYS B CG  1 
ATOM   5078 C CD  . LYS B 1 119 ? 19.614  16.218  7.375   1.00 59.00 ? 119 LYS B CD  1 
ATOM   5079 C CE  . LYS B 1 119 ? 20.809  17.036  7.838   1.00 62.43 ? 119 LYS B CE  1 
ATOM   5080 N NZ  . LYS B 1 119 ? 21.941  16.164  8.271   1.00 66.00 ? 119 LYS B NZ  1 
ATOM   5081 N N   . GLU B 1 120 ? 15.842  18.111  3.747   1.00 65.72 ? 120 GLU B N   1 
ATOM   5082 C CA  . GLU B 1 120 ? 15.064  17.964  2.539   1.00 67.12 ? 120 GLU B CA  1 
ATOM   5083 C C   . GLU B 1 120 ? 15.066  16.545  1.990   1.00 64.53 ? 120 GLU B C   1 
ATOM   5084 O O   . GLU B 1 120 ? 14.039  16.056  1.549   1.00 63.43 ? 120 GLU B O   1 
ATOM   5085 C CB  . GLU B 1 120 ? 15.588  18.943  1.453   1.00 72.01 ? 120 GLU B CB  1 
ATOM   5086 C CG  . GLU B 1 120 ? 15.347  20.430  1.640   1.00 75.81 ? 120 GLU B CG  1 
ATOM   5087 C CD  . GLU B 1 120 ? 16.468  21.292  1.108   1.00 77.38 ? 120 GLU B CD  1 
ATOM   5088 O OE1 . GLU B 1 120 ? 17.349  20.793  0.411   1.00 76.80 ? 120 GLU B OE1 1 
ATOM   5089 O OE2 . GLU B 1 120 ? 16.463  22.477  1.414   1.00 79.96 ? 120 GLU B OE2 1 
ATOM   5090 N N   . LYS B 1 121 ? 16.240  15.918  1.984   1.00 61.80 ? 121 LYS B N   1 
ATOM   5091 C CA  . LYS B 1 121 ? 16.420  14.558  1.505   1.00 60.44 ? 121 LYS B CA  1 
ATOM   5092 C C   . LYS B 1 121 ? 17.428  13.897  2.407   1.00 52.97 ? 121 LYS B C   1 
ATOM   5093 O O   . LYS B 1 121 ? 18.320  14.529  2.889   1.00 54.00 ? 121 LYS B O   1 
ATOM   5094 C CB  . LYS B 1 121 ? 16.887  14.458  0.067   1.00 64.97 ? 121 LYS B CB  1 
ATOM   5095 C CG  . LYS B 1 121 ? 16.099  13.458  -0.764  1.00 70.47 ? 121 LYS B CG  1 
ATOM   5096 C CD  . LYS B 1 121 ? 16.364  11.971  -0.460  1.00 75.28 ? 121 LYS B CD  1 
ATOM   5097 C CE  . LYS B 1 121 ? 15.648  11.429  0.785   1.00 76.57 ? 121 LYS B CE  1 
ATOM   5098 N NZ  . LYS B 1 121 ? 14.197  11.196  0.628   1.00 77.39 ? 121 LYS B NZ  1 
ATOM   5099 N N   . LEU B 1 122 ? 17.265  12.613  2.635   1.00 47.83 ? 122 LEU B N   1 
ATOM   5100 C CA  . LEU B 1 122 ? 18.145  11.926  3.530   1.00 41.14 ? 122 LEU B CA  1 
ATOM   5101 C C   . LEU B 1 122 ? 19.110  11.018  2.840   1.00 37.68 ? 122 LEU B C   1 
ATOM   5102 O O   . LEU B 1 122 ? 18.732  10.294  1.962   1.00 36.98 ? 122 LEU B O   1 
ATOM   5103 C CB  . LEU B 1 122 ? 17.293  11.114  4.497   1.00 36.90 ? 122 LEU B CB  1 
ATOM   5104 C CG  . LEU B 1 122 ? 16.348  11.931  5.367   1.00 44.81 ? 122 LEU B CG  1 
ATOM   5105 C CD1 . LEU B 1 122 ? 15.572  11.079  6.347   1.00 44.83 ? 122 LEU B CD1 1 
ATOM   5106 C CD2 . LEU B 1 122 ? 17.085  12.972  6.131   1.00 45.39 ? 122 LEU B CD2 1 
ATOM   5107 N N   . ASN B 1 123 ? 20.362  11.062  3.270   1.00 34.35 ? 123 ASN B N   1 
ATOM   5108 C CA  . ASN B 1 123 ? 21.345  10.118  2.763   1.00 31.97 ? 123 ASN B CA  1 
ATOM   5109 C C   . ASN B 1 123 ? 21.313  8.854   3.619   1.00 28.40 ? 123 ASN B C   1 
ATOM   5110 O O   . ASN B 1 123 ? 20.525  8.733   4.563   1.00 30.30 ? 123 ASN B O   1 
ATOM   5111 C CB  . ASN B 1 123 ? 22.742  10.740  2.719   1.00 35.04 ? 123 ASN B CB  1 
ATOM   5112 C CG  . ASN B 1 123 ? 23.216  11.250  4.074   1.00 35.42 ? 123 ASN B CG  1 
ATOM   5113 O OD1 . ASN B 1 123 ? 22.911  10.678  5.128   1.00 35.43 ? 123 ASN B OD1 1 
ATOM   5114 N ND2 . ASN B 1 123 ? 23.973  12.335  4.045   1.00 39.88 ? 123 ASN B ND2 1 
ATOM   5115 N N   . ARG B 1 124 ? 22.182  7.897   3.288   1.00 29.90 ? 124 ARG B N   1 
ATOM   5116 C CA  . ARG B 1 124 ? 22.133  6.601   3.963   1.00 27.43 ? 124 ARG B CA  1 
ATOM   5117 C C   . ARG B 1 124 ? 22.303  6.748   5.473   1.00 26.98 ? 124 ARG B C   1 
ATOM   5118 O O   . ARG B 1 124 ? 21.573  6.122   6.254   1.00 27.58 ? 124 ARG B O   1 
ATOM   5119 C CB  . ARG B 1 124 ? 23.206  5.666   3.396   1.00 29.07 ? 124 ARG B CB  1 
ATOM   5120 C CG  . ARG B 1 124 ? 23.119  4.258   3.961   1.00 30.46 ? 124 ARG B CG  1 
ATOM   5121 C CD  . ARG B 1 124 ? 24.198  3.349   3.417   1.00 31.86 ? 124 ARG B CD  1 
ATOM   5122 N NE  . ARG B 1 124 ? 24.161  2.033   4.053   1.00 35.15 ? 124 ARG B NE  1 
ATOM   5123 C CZ  . ARG B 1 124 ? 24.791  1.747   5.191   1.00 39.05 ? 124 ARG B CZ  1 
ATOM   5124 N NH1 . ARG B 1 124 ? 25.492  2.687   5.811   1.00 41.06 ? 124 ARG B NH1 1 
ATOM   5125 N NH2 . ARG B 1 124 ? 24.720  0.529   5.714   1.00 34.09 ? 124 ARG B NH2 1 
ATOM   5126 N N   . GLU B 1 125 ? 23.269  7.560   5.902   1.00 28.96 ? 125 GLU B N   1 
ATOM   5127 C CA  . GLU B 1 125 ? 23.532  7.691   7.329   1.00 30.16 ? 125 GLU B CA  1 
ATOM   5128 C C   . GLU B 1 125 ? 22.349  8.330   8.040   1.00 26.80 ? 125 GLU B C   1 
ATOM   5129 O O   . GLU B 1 125 ? 22.011  7.954   9.167   1.00 24.70 ? 125 GLU B O   1 
ATOM   5130 C CB  . GLU B 1 125 ? 24.812  8.503   7.548   1.00 33.99 ? 125 GLU B CB  1 
ATOM   5131 C CG  . GLU B 1 125 ? 26.083  7.859   6.970   1.00 47.37 ? 125 GLU B CG  1 
ATOM   5132 C CD  . GLU B 1 125 ? 26.113  7.792   5.434   1.00 58.54 ? 125 GLU B CD  1 
ATOM   5133 O OE1 . GLU B 1 125 ? 25.777  8.797   4.761   1.00 58.68 ? 125 GLU B OE1 1 
ATOM   5134 O OE2 . GLU B 1 125 ? 26.459  6.714   4.903   1.00 61.00 ? 125 GLU B OE2 1 
ATOM   5135 N N   . GLU B 1 126 ? 21.684  9.280   7.387   1.00 28.93 ? 126 GLU B N   1 
ATOM   5136 C CA  . GLU B 1 126 ? 20.519  9.900   8.010   1.00 25.19 ? 126 GLU B CA  1 
ATOM   5137 C C   . GLU B 1 126 ? 19.339  8.934   8.067   1.00 23.24 ? 126 GLU B C   1 
ATOM   5138 O O   . GLU B 1 126 ? 18.591  8.913   9.052   1.00 24.56 ? 126 GLU B O   1 
ATOM   5139 C CB  . GLU B 1 126 ? 20.162  11.181  7.260   1.00 26.95 ? 126 GLU B CB  1 
ATOM   5140 C CG  . GLU B 1 126 ? 21.200  12.282  7.521   1.00 29.62 ? 126 GLU B CG  1 
ATOM   5141 C CD  . GLU B 1 126 ? 21.324  13.300  6.411   1.00 37.73 ? 126 GLU B CD  1 
ATOM   5142 O OE1 . GLU B 1 126 ? 20.651  13.171  5.363   1.00 38.77 ? 126 GLU B OE1 1 
ATOM   5143 O OE2 . GLU B 1 126 ? 22.115  14.244  6.597   1.00 43.17 ? 126 GLU B OE2 1 
ATOM   5144 N N   . LEU B 1 127 ? 19.171  8.101   7.039   1.00 26.57 ? 127 LEU B N   1 
ATOM   5145 C CA  . LEU B 1 127 ? 18.086  7.123   7.073   1.00 25.61 ? 127 LEU B CA  1 
ATOM   5146 C C   . LEU B 1 127 ? 18.337  6.062   8.141   1.00 22.77 ? 127 LEU B C   1 
ATOM   5147 O O   . LEU B 1 127 ? 17.406  5.631   8.821   1.00 25.21 ? 127 LEU B O   1 
ATOM   5148 C CB  . LEU B 1 127 ? 17.917  6.477   5.701   1.00 25.11 ? 127 LEU B CB  1 
ATOM   5149 C CG  . LEU B 1 127 ? 17.335  7.352   4.584   1.00 29.29 ? 127 LEU B CG  1 
ATOM   5150 C CD1 . LEU B 1 127 ? 17.560  6.716   3.202   1.00 32.20 ? 127 LEU B CD1 1 
ATOM   5151 C CD2 . LEU B 1 127 ? 15.860  7.613   4.836   1.00 29.33 ? 127 LEU B CD2 1 
ATOM   5152 N N   . LEU B 1 128 ? 19.590  5.622   8.303   1.00 21.88 ? 128 LEU B N   1 
ATOM   5153 C CA  . LEU B 1 128 ? 19.900  4.675   9.375   1.00 22.05 ? 128 LEU B CA  1 
ATOM   5154 C C   . LEU B 1 128 ? 19.543  5.247   10.743  1.00 21.33 ? 128 LEU B C   1 
ATOM   5155 O O   . LEU B 1 128 ? 19.007  4.538   11.606  1.00 20.89 ? 128 LEU B O   1 
ATOM   5156 C CB  . LEU B 1 128 ? 21.386  4.298   9.335   1.00 22.27 ? 128 LEU B CB  1 
ATOM   5157 C CG  . LEU B 1 128 ? 21.713  2.911   8.773   1.00 24.88 ? 128 LEU B CG  1 
ATOM   5158 C CD1 . LEU B 1 128 ? 23.205  2.737   8.519   1.00 27.99 ? 128 LEU B CD1 1 
ATOM   5159 C CD2 . LEU B 1 128 ? 21.195  1.834   9.688   1.00 27.20 ? 128 LEU B CD2 1 
ATOM   5160 N N   . ASP B 1 129 ? 19.834  6.530   10.960  1.00 21.46 ? 129 ASP B N   1 
ATOM   5161 C CA  . ASP B 1 129 ? 19.471  7.168   12.220  1.00 24.42 ? 129 ASP B CA  1 
ATOM   5162 C C   . ASP B 1 129 ? 17.963  7.282   12.353  1.00 23.63 ? 129 ASP B C   1 
ATOM   5163 O O   . ASP B 1 129 ? 17.426  7.172   13.461  1.00 24.77 ? 129 ASP B O   1 
ATOM   5164 C CB  . ASP B 1 129 ? 20.110  8.559   12.331  1.00 23.86 ? 129 ASP B CB  1 
ATOM   5165 C CG  . ASP B 1 129 ? 21.586  8.506   12.698  1.00 29.53 ? 129 ASP B CG  1 
ATOM   5166 O OD1 . ASP B 1 129 ? 22.088  7.387   12.907  1.00 33.89 ? 129 ASP B OD1 1 
ATOM   5167 O OD2 . ASP B 1 129 ? 22.242  9.573   12.766  1.00 32.53 ? 129 ASP B OD2 1 
ATOM   5168 N N   . LEU B 1 130 ? 17.259  7.513   11.238  1.00 22.24 ? 130 LEU B N   1 
ATOM   5169 C CA  . LEU B 1 130 ? 15.804  7.562   11.307  1.00 26.68 ? 130 LEU B CA  1 
ATOM   5170 C C   . LEU B 1 130 ? 15.235  6.201   11.694  1.00 24.69 ? 130 LEU B C   1 
ATOM   5171 O O   . LEU B 1 130 ? 14.380  6.105   12.584  1.00 23.23 ? 130 LEU B O   1 
ATOM   5172 C CB  . LEU B 1 130 ? 15.220  8.058   9.982   1.00 28.28 ? 130 LEU B CB  1 
ATOM   5173 C CG  . LEU B 1 130 ? 13.765  8.536   10.147  1.00 32.86 ? 130 LEU B CG  1 
ATOM   5174 C CD1 . LEU B 1 130 ? 13.684  9.645   11.193  1.00 32.86 ? 130 LEU B CD1 1 
ATOM   5175 C CD2 . LEU B 1 130 ? 13.156  8.998   8.827   1.00 35.39 ? 130 LEU B CD2 1 
ATOM   5176 N N   . GLN B 1 131 ? 15.713  5.134   11.048  1.00 20.85 ? 131 GLN B N   1 
ATOM   5177 C CA  . GLN B 1 131 ? 15.268  3.789   11.404  1.00 20.23 ? 131 GLN B CA  1 
ATOM   5178 C C   . GLN B 1 131 ? 15.580  3.473   12.854  1.00 19.87 ? 131 GLN B C   1 
ATOM   5179 O O   . GLN B 1 131 ? 14.718  2.999   13.607  1.00 20.35 ? 131 GLN B O   1 
ATOM   5180 C CB  . GLN B 1 131 ? 15.947  2.751   10.517  1.00 17.37 ? 131 GLN B CB  1 
ATOM   5181 C CG  . GLN B 1 131 ? 15.626  2.873   9.075   1.00 17.92 ? 131 GLN B CG  1 
ATOM   5182 C CD  . GLN B 1 131 ? 16.527  1.996   8.245   1.00 19.23 ? 131 GLN B CD  1 
ATOM   5183 O OE1 . GLN B 1 131 ? 17.755  1.987   8.428   1.00 20.09 ? 131 GLN B OE1 1 
ATOM   5184 N NE2 . GLN B 1 131 ? 15.937  1.252   7.320   1.00 20.61 ? 131 GLN B NE2 1 
ATOM   5185 N N   . THR B 1 132 ? 16.827  3.687   13.254  1.00 20.89 ? 132 THR B N   1 
ATOM   5186 C CA  . THR B 1 132 ? 17.255  3.184   14.551  1.00 16.88 ? 132 THR B CA  1 
ATOM   5187 C C   . THR B 1 132 ? 16.662  3.989   15.693  1.00 19.46 ? 132 THR B C   1 
ATOM   5188 O O   . THR B 1 132 ? 16.352  3.427   16.751  1.00 20.79 ? 132 THR B O   1 
ATOM   5189 C CB  . THR B 1 132 ? 18.777  3.184   14.621  1.00 17.80 ? 132 THR B CB  1 
ATOM   5190 O OG1 . THR B 1 132 ? 19.283  2.517   13.463  1.00 19.34 ? 132 THR B OG1 1 
ATOM   5191 C CG2 . THR B 1 132 ? 19.230  2.441   15.859  1.00 17.98 ? 132 THR B CG2 1 
ATOM   5192 N N   . LEU B 1 133 ? 16.520  5.310   15.514  1.00 17.71 ? 133 LEU B N   1 
ATOM   5193 C CA  . LEU B 1 133 ? 15.906  6.119   16.562  1.00 23.99 ? 133 LEU B CA  1 
ATOM   5194 C C   . LEU B 1 133 ? 14.430  5.781   16.724  1.00 21.44 ? 133 LEU B C   1 
ATOM   5195 O O   . LEU B 1 133 ? 13.909  5.790   17.846  1.00 18.79 ? 133 LEU B O   1 
ATOM   5196 C CB  . LEU B 1 133 ? 16.084  7.608   16.269  1.00 18.38 ? 133 LEU B CB  1 
ATOM   5197 C CG  . LEU B 1 133 ? 17.506  8.107   16.543  1.00 20.51 ? 133 LEU B CG  1 
ATOM   5198 C CD1 . LEU B 1 133 ? 17.721  9.506   15.949  1.00 23.01 ? 133 LEU B CD1 1 
ATOM   5199 C CD2 . LEU B 1 133 ? 17.744  8.072   18.030  1.00 22.63 ? 133 LEU B CD2 1 
ATOM   5200 N N   . ASN B 1 134 ? 13.732  5.490   15.617  1.00 19.07 ? 134 ASN B N   1 
ATOM   5201 C CA  . ASN B 1 134 ? 12.353  5.032   15.755  1.00 20.78 ? 134 ASN B CA  1 
ATOM   5202 C C   . ASN B 1 134 ? 12.298  3.745   16.559  1.00 26.56 ? 134 ASN B C   1 
ATOM   5203 O O   . ASN B 1 134 ? 11.405  3.564   17.390  1.00 21.43 ? 134 ASN B O   1 
ATOM   5204 C CB  . ASN B 1 134 ? 11.698  4.826   14.392  1.00 19.75 ? 134 ASN B CB  1 
ATOM   5205 C CG  . ASN B 1 134 ? 10.992  6.071   13.906  1.00 22.33 ? 134 ASN B CG  1 
ATOM   5206 O OD1 . ASN B 1 134 ? 9.883   6.376   14.359  1.00 23.69 ? 134 ASN B OD1 1 
ATOM   5207 N ND2 . ASN B 1 134 ? 11.627  6.807   13.008  1.00 24.55 ? 134 ASN B ND2 1 
ATOM   5208 N N   . LEU B 1 135 ? 13.249  2.840   16.320  1.00 20.13 ? 135 LEU B N   1 
ATOM   5209 C CA  . LEU B 1 135 ? 13.324  1.603   17.094  1.00 22.04 ? 135 LEU B CA  1 
ATOM   5210 C C   . LEU B 1 135 ? 13.595  1.879   18.569  1.00 21.48 ? 135 LEU B C   1 
ATOM   5211 O O   . LEU B 1 135 ? 12.894  1.368   19.452  1.00 24.55 ? 135 LEU B O   1 
ATOM   5212 C CB  . LEU B 1 135 ? 14.429  0.715   16.530  1.00 24.54 ? 135 LEU B CB  1 
ATOM   5213 C CG  . LEU B 1 135 ? 14.161  -0.602  15.820  1.00 30.12 ? 135 LEU B CG  1 
ATOM   5214 C CD1 . LEU B 1 135 ? 15.478  -1.396  15.791  1.00 24.28 ? 135 LEU B CD1 1 
ATOM   5215 C CD2 . LEU B 1 135 ? 13.025  -1.430  16.418  1.00 19.05 ? 135 LEU B CD2 1 
ATOM   5216 N N   . LEU B 1 136 ? 14.650  2.656   18.862  1.00 19.79 ? 136 LEU B N   1 
ATOM   5217 C CA  . LEU B 1 136 ? 15.070  2.883   20.242  1.00 18.10 ? 136 LEU B CA  1 
ATOM   5218 C C   . LEU B 1 136 ? 14.076  3.723   21.040  1.00 21.26 ? 136 LEU B C   1 
ATOM   5219 O O   . LEU B 1 136 ? 14.059  3.629   22.272  1.00 21.19 ? 136 LEU B O   1 
ATOM   5220 C CB  . LEU B 1 136 ? 16.447  3.553   20.266  1.00 22.81 ? 136 LEU B CB  1 
ATOM   5221 C CG  . LEU B 1 136 ? 17.623  2.629   19.931  1.00 24.51 ? 136 LEU B CG  1 
ATOM   5222 C CD1 . LEU B 1 136 ? 18.901  3.440   19.689  1.00 25.11 ? 136 LEU B CD1 1 
ATOM   5223 C CD2 . LEU B 1 136 ? 17.831  1.584   21.019  1.00 27.90 ? 136 LEU B CD2 1 
ATOM   5224 N N   . ALA B 1 137 ? 13.252  4.542   20.375  1.00 22.07 ? 137 ALA B N   1 
ATOM   5225 C CA  . ALA B 1 137 ? 12.244  5.308   21.109  1.00 22.58 ? 137 ALA B CA  1 
ATOM   5226 C C   . ALA B 1 137 ? 11.301  4.398   21.895  1.00 19.62 ? 137 ALA B C   1 
ATOM   5227 O O   . ALA B 1 137 ? 10.760  4.811   22.927  1.00 20.34 ? 137 ALA B O   1 
ATOM   5228 C CB  . ALA B 1 137 ? 11.434  6.191   20.148  1.00 19.44 ? 137 ALA B CB  1 
ATOM   5229 N N   . TRP B 1 138 ? 11.081  3.175   21.432  1.00 19.05 ? 138 TRP B N   1 
ATOM   5230 C CA  . TRP B 1 138 ? 10.120  2.278   22.065  1.00 17.85 ? 138 TRP B CA  1 
ATOM   5231 C C   . TRP B 1 138 ? 10.802  1.290   23.015  1.00 17.79 ? 138 TRP B C   1 
ATOM   5232 O O   . TRP B 1 138 ? 10.210  0.269   23.379  1.00 21.53 ? 138 TRP B O   1 
ATOM   5233 C CB  . TRP B 1 138 ? 9.293   1.557   20.991  1.00 20.28 ? 138 TRP B CB  1 
ATOM   5234 C CG  . TRP B 1 138 ? 8.532   2.523   20.162  1.00 19.36 ? 138 TRP B CG  1 
ATOM   5235 C CD1 . TRP B 1 138 ? 8.987   3.197   19.054  1.00 22.38 ? 138 TRP B CD1 1 
ATOM   5236 C CD2 . TRP B 1 138 ? 7.195   2.986   20.386  1.00 16.52 ? 138 TRP B CD2 1 
ATOM   5237 N NE1 . TRP B 1 138 ? 8.015   4.025   18.572  1.00 20.85 ? 138 TRP B NE1 1 
ATOM   5238 C CE2 . TRP B 1 138 ? 6.900   3.919   19.361  1.00 17.60 ? 138 TRP B CE2 1 
ATOM   5239 C CE3 . TRP B 1 138 ? 6.211   2.681   21.327  1.00 16.57 ? 138 TRP B CE3 1 
ATOM   5240 C CZ2 . TRP B 1 138 ? 5.668   4.573   19.268  1.00 19.65 ? 138 TRP B CZ2 1 
ATOM   5241 C CZ3 . TRP B 1 138 ? 4.976   3.338   21.240  1.00 20.04 ? 138 TRP B CZ3 1 
ATOM   5242 C CH2 . TRP B 1 138 ? 4.721   4.278   20.215  1.00 19.63 ? 138 TRP B CH2 1 
ATOM   5243 N N   . CYS B 1 139 ? 12.036  1.578   23.417  1.00 17.35 ? 139 CYS B N   1 
ATOM   5244 C CA  . CYS B 1 139 ? 12.748  0.688   24.321  1.00 17.92 ? 139 CYS B CA  1 
ATOM   5245 C C   . CYS B 1 139 ? 12.040  0.620   25.670  1.00 21.18 ? 139 CYS B C   1 
ATOM   5246 O O   . CYS B 1 139 ? 11.723  1.654   26.266  1.00 18.89 ? 139 CYS B O   1 
ATOM   5247 C CB  . CYS B 1 139 ? 14.182  1.176   24.510  1.00 22.30 ? 139 CYS B CB  1 
ATOM   5248 S SG  . CYS B 1 139 ? 15.253  -0.047  25.249  1.00 24.01 ? 139 CYS B SG  1 
ATOM   5249 N N   . GLY B 1 140 ? 11.814  -0.608  26.166  1.00 15.72 ? 140 GLY B N   1 
ATOM   5250 C CA  . GLY B 1 140 ? 11.215  -0.781  27.484  1.00 13.85 ? 140 GLY B CA  1 
ATOM   5251 C C   . GLY B 1 140 ? 12.226  -0.704  28.632  1.00 14.78 ? 140 GLY B C   1 
ATOM   5252 O O   . GLY B 1 140 ? 13.445  -0.599  28.455  1.00 17.93 ? 140 GLY B O   1 
ATOM   5253 N N   . ARG B 1 141 ? 11.684  -0.751  29.857  1.00 16.40 ? 141 ARG B N   1 
ATOM   5254 C CA  . ARG B 1 141 ? 12.501  -0.575  31.063  1.00 17.45 ? 141 ARG B CA  1 
ATOM   5255 C C   . ARG B 1 141 ? 13.638  -1.590  31.144  1.00 17.12 ? 141 ARG B C   1 
ATOM   5256 O O   . ARG B 1 141 ? 14.778  -1.230  31.457  1.00 19.10 ? 141 ARG B O   1 
ATOM   5257 C CB  . ARG B 1 141 ? 11.599  -0.679  32.298  1.00 16.37 ? 141 ARG B CB  1 
ATOM   5258 C CG  . ARG B 1 141 ? 12.328  -0.770  33.618  1.00 20.02 ? 141 ARG B CG  1 
ATOM   5259 C CD  . ARG B 1 141 ? 11.306  -0.790  34.762  1.00 17.10 ? 141 ARG B CD  1 
ATOM   5260 N NE  . ARG B 1 141 ? 11.943  -0.927  36.047  1.00 21.09 ? 141 ARG B NE  1 
ATOM   5261 C CZ  . ARG B 1 141 ? 12.037  -2.070  36.709  1.00 24.63 ? 141 ARG B CZ  1 
ATOM   5262 N NH1 . ARG B 1 141 ? 12.675  -2.092  37.872  1.00 23.96 ? 141 ARG B NH1 1 
ATOM   5263 N NH2 . ARG B 1 141 ? 11.502  -3.180  36.208  1.00 20.55 ? 141 ARG B NH2 1 
ATOM   5264 N N   . THR B 1 142 ? 13.348  -2.866  30.865  1.00 17.54 ? 142 THR B N   1 
ATOM   5265 C CA  . THR B 1 142 ? 14.363  -3.903  31.014  1.00 18.10 ? 142 THR B CA  1 
ATOM   5266 C C   . THR B 1 142 ? 15.571  -3.614  30.133  1.00 18.01 ? 142 THR B C   1 
ATOM   5267 O O   . THR B 1 142 ? 16.723  -3.680  30.584  1.00 22.06 ? 142 THR B O   1 
ATOM   5268 C CB  . THR B 1 142 ? 13.769  -5.277  30.674  1.00 21.69 ? 142 THR B CB  1 
ATOM   5269 O OG1 . THR B 1 142 ? 12.728  -5.615  31.605  1.00 19.61 ? 142 THR B OG1 1 
ATOM   5270 C CG2 . THR B 1 142 ? 14.836  -6.353  30.726  1.00 21.06 ? 142 THR B CG2 1 
ATOM   5271 N N   . LEU B 1 143 ? 15.324  -3.298  28.873  1.00 18.44 ? 143 LEU B N   1 
ATOM   5272 C CA  . LEU B 1 143 ? 16.427  -3.114  27.943  1.00 20.46 ? 143 LEU B CA  1 
ATOM   5273 C C   . LEU B 1 143 ? 17.002  -1.709  27.986  1.00 25.65 ? 143 LEU B C   1 
ATOM   5274 O O   . LEU B 1 143 ? 18.112  -1.505  27.491  1.00 27.71 ? 143 LEU B O   1 
ATOM   5275 C CB  . LEU B 1 143 ? 15.981  -3.447  26.517  1.00 21.38 ? 143 LEU B CB  1 
ATOM   5276 C CG  . LEU B 1 143 ? 15.804  -4.938  26.216  1.00 20.38 ? 143 LEU B CG  1 
ATOM   5277 C CD1 . LEU B 1 143 ? 15.421  -5.148  24.756  1.00 16.68 ? 143 LEU B CD1 1 
ATOM   5278 C CD2 . LEU B 1 143 ? 17.070  -5.699  26.530  1.00 22.78 ? 143 LEU B CD2 1 
ATOM   5279 N N   . ARG B 1 144 ? 16.270  -0.739  28.555  1.00 24.45 ? 144 ARG B N   1 
ATOM   5280 C CA  . ARG B 1 144 ? 16.853  0.589   28.748  1.00 26.67 ? 144 ARG B CA  1 
ATOM   5281 C C   . ARG B 1 144 ? 18.083  0.518   29.638  1.00 34.22 ? 144 ARG B C   1 
ATOM   5282 O O   . ARG B 1 144 ? 18.981  1.365   29.538  1.00 35.36 ? 144 ARG B O   1 
ATOM   5283 C CB  . ARG B 1 144 ? 15.811  1.548   29.328  1.00 26.61 ? 144 ARG B CB  1 
ATOM   5284 C CG  . ARG B 1 144 ? 14.963  2.251   28.253  1.00 28.20 ? 144 ARG B CG  1 
ATOM   5285 C CD  . ARG B 1 144 ? 13.888  3.112   28.882  1.00 30.57 ? 144 ARG B CD  1 
ATOM   5286 N NE  . ARG B 1 144 ? 13.044  3.780   27.899  1.00 31.55 ? 144 ARG B NE  1 
ATOM   5287 C CZ  . ARG B 1 144 ? 13.226  5.040   27.516  1.00 28.69 ? 144 ARG B CZ  1 
ATOM   5288 N NH1 . ARG B 1 144 ? 14.229  5.745   28.028  1.00 30.79 ? 144 ARG B NH1 1 
ATOM   5289 N NH2 . ARG B 1 144 ? 12.424  5.583   26.617  1.00 28.77 ? 144 ARG B NH2 1 
ATOM   5290 N N   . LYS B 1 145 ? 18.159  -0.501  30.493  1.00 39.76 ? 145 LYS B N   1 
ATOM   5291 C CA  . LYS B 1 145 ? 19.369  -0.687  31.282  1.00 39.32 ? 145 LYS B CA  1 
ATOM   5292 C C   . LYS B 1 145 ? 20.481  -1.310  30.451  1.00 44.08 ? 145 LYS B C   1 
ATOM   5293 O O   . LYS B 1 145 ? 21.630  -0.873  30.527  1.00 49.77 ? 145 LYS B O   1 
ATOM   5294 C CB  . LYS B 1 145 ? 19.070  -1.534  32.515  1.00 47.38 ? 145 LYS B CB  1 
ATOM   5295 C CG  . LYS B 1 145 ? 17.984  -0.942  33.396  1.00 49.72 ? 145 LYS B CG  1 
ATOM   5296 C CD  . LYS B 1 145 ? 17.822  -1.745  34.679  1.00 57.69 ? 145 LYS B CD  1 
ATOM   5297 C CE  . LYS B 1 145 ? 16.346  -1.950  35.026  1.00 59.82 ? 145 LYS B CE  1 
ATOM   5298 N NZ  . LYS B 1 145 ? 15.693  -0.665  35.410  1.00 55.67 ? 145 LYS B NZ  1 
ATOM   5299 N N   . ASP B 1 146 ? 20.168  -2.314  29.631  1.00 43.97 ? 146 ASP B N   1 
ATOM   5300 C CA  . ASP B 1 146 ? 21.196  -2.968  28.823  1.00 44.31 ? 146 ASP B CA  1 
ATOM   5301 C C   . ASP B 1 146 ? 21.642  -2.090  27.660  1.00 46.79 ? 146 ASP B C   1 
ATOM   5302 O O   . ASP B 1 146 ? 22.835  -2.029  27.346  1.00 56.17 ? 146 ASP B O   1 
ATOM   5303 C CB  . ASP B 1 146 ? 20.686  -4.316  28.304  1.00 52.05 ? 146 ASP B CB  1 
ATOM   5304 C CG  . ASP B 1 146 ? 20.354  -5.282  29.426  1.00 61.97 ? 146 ASP B CG  1 
ATOM   5305 O OD1 . ASP B 1 146 ? 19.241  -5.200  29.980  1.00 62.00 ? 146 ASP B OD1 1 
ATOM   5306 O OD2 . ASP B 1 146 ? 21.212  -6.127  29.754  1.00 68.65 ? 146 ASP B OD2 1 
ATOM   5307 N N   . LEU B 1 147 ? 20.704  -1.413  27.003  1.00 37.82 ? 147 LEU B N   1 
ATOM   5308 C CA  . LEU B 1 147 ? 20.978  -0.595  25.830  1.00 31.44 ? 147 LEU B CA  1 
ATOM   5309 C C   . LEU B 1 147 ? 21.266  0.864   26.180  1.00 30.18 ? 147 LEU B C   1 
ATOM   5310 O O   . LEU B 1 147 ? 21.208  1.728   25.298  1.00 28.22 ? 147 LEU B O   1 
ATOM   5311 C CB  . LEU B 1 147 ? 19.800  -0.679  24.859  1.00 27.17 ? 147 LEU B CB  1 
ATOM   5312 C CG  . LEU B 1 147 ? 19.370  -2.050  24.319  1.00 31.26 ? 147 LEU B CG  1 
ATOM   5313 C CD1 . LEU B 1 147 ? 18.078  -1.926  23.518  1.00 27.95 ? 147 LEU B CD1 1 
ATOM   5314 C CD2 . LEU B 1 147 ? 20.459  -2.689  23.465  1.00 34.61 ? 147 LEU B CD2 1 
ATOM   5315 N N   . LYS B 1 148 ? 21.577  1.155   27.445  1.00 28.84 ? 148 LYS B N   1 
ATOM   5316 C CA  . LYS B 1 148 ? 21.756  2.541   27.875  1.00 32.11 ? 148 LYS B CA  1 
ATOM   5317 C C   . LYS B 1 148 ? 22.824  3.254   27.053  1.00 35.87 ? 148 LYS B C   1 
ATOM   5318 O O   . LYS B 1 148 ? 22.690  4.447   26.753  1.00 39.16 ? 148 LYS B O   1 
ATOM   5319 C CB  . LYS B 1 148 ? 22.122  2.580   29.364  1.00 36.60 ? 148 LYS B CB  1 
ATOM   5320 C CG  . LYS B 1 148 ? 22.271  3.977   29.939  1.00 42.90 ? 148 LYS B CG  1 
ATOM   5321 C CD  . LYS B 1 148 ? 23.124  3.975   31.208  1.00 50.54 ? 148 LYS B CD  1 
ATOM   5322 C CE  . LYS B 1 148 ? 22.665  2.900   32.174  1.00 51.86 ? 148 LYS B CE  1 
ATOM   5323 N NZ  . LYS B 1 148 ? 23.770  2.469   33.069  1.00 58.69 ? 148 LYS B NZ  1 
ATOM   5324 N N   . ASP B 1 149 ? 23.892  2.535   26.678  1.00 40.82 ? 149 ASP B N   1 
ATOM   5325 C CA  . ASP B 1 149 ? 24.966  3.131   25.882  1.00 44.29 ? 149 ASP B CA  1 
ATOM   5326 C C   . ASP B 1 149 ? 24.469  3.585   24.514  1.00 36.09 ? 149 ASP B C   1 
ATOM   5327 O O   . ASP B 1 149 ? 24.762  4.704   24.074  1.00 36.85 ? 149 ASP B O   1 
ATOM   5328 C CB  . ASP B 1 149 ? 26.113  2.133   25.709  1.00 53.07 ? 149 ASP B CB  1 
ATOM   5329 C CG  . ASP B 1 149 ? 26.783  1.770   27.020  1.00 62.32 ? 149 ASP B CG  1 
ATOM   5330 O OD1 . ASP B 1 149 ? 26.628  2.524   28.011  1.00 60.44 ? 149 ASP B OD1 1 
ATOM   5331 O OD2 . ASP B 1 149 ? 27.468  0.721   27.049  1.00 65.50 ? 149 ASP B OD2 1 
ATOM   5332 N N   . LEU B 1 150 ? 23.751  2.711   23.805  1.00 34.50 ? 150 LEU B N   1 
ATOM   5333 C CA  . LEU B 1 150 ? 23.244  3.078   22.484  1.00 31.92 ? 150 LEU B CA  1 
ATOM   5334 C C   . LEU B 1 150 ? 22.228  4.206   22.566  1.00 33.42 ? 150 LEU B C   1 
ATOM   5335 O O   . LEU B 1 150 ? 22.162  5.048   21.661  1.00 31.65 ? 150 LEU B O   1 
ATOM   5336 C CB  . LEU B 1 150 ? 22.616  1.867   21.789  1.00 29.32 ? 150 LEU B CB  1 
ATOM   5337 C CG  . LEU B 1 150 ? 23.591  0.789   21.302  1.00 36.33 ? 150 LEU B CG  1 
ATOM   5338 C CD1 . LEU B 1 150 ? 22.825  -0.369  20.703  1.00 37.02 ? 150 LEU B CD1 1 
ATOM   5339 C CD2 . LEU B 1 150 ? 24.588  1.358   20.295  1.00 34.57 ? 150 LEU B CD2 1 
ATOM   5340 N N   . LEU B 1 151 ? 21.423  4.235   23.633  1.00 32.65 ? 151 LEU B N   1 
ATOM   5341 C CA  . LEU B 1 151 ? 20.413  5.280   23.778  1.00 33.12 ? 151 LEU B CA  1 
ATOM   5342 C C   . LEU B 1 151 ? 21.052  6.655   23.903  1.00 34.65 ? 151 LEU B C   1 
ATOM   5343 O O   . LEU B 1 151 ? 20.614  7.617   23.259  1.00 39.76 ? 151 LEU B O   1 
ATOM   5344 C CB  . LEU B 1 151 ? 19.538  4.989   24.998  1.00 37.09 ? 151 LEU B CB  1 
ATOM   5345 C CG  . LEU B 1 151 ? 18.425  3.970   24.797  1.00 36.27 ? 151 LEU B CG  1 
ATOM   5346 C CD1 . LEU B 1 151 ? 17.840  3.549   26.144  1.00 36.24 ? 151 LEU B CD1 1 
ATOM   5347 C CD2 . LEU B 1 151 ? 17.347  4.552   23.890  1.00 31.25 ? 151 LEU B CD2 1 
ATOM   5348 N N   . ASN B 1 152 ? 22.093  6.767   24.739  1.00 38.15 ? 152 ASN B N   1 
ATOM   5349 C CA  . ASN B 1 152 ? 22.761  8.044   24.973  1.00 42.30 ? 152 ASN B CA  1 
ATOM   5350 C C   . ASN B 1 152 ? 23.528  8.528   23.756  1.00 38.72 ? 152 ASN B C   1 
ATOM   5351 O O   . ASN B 1 152 ? 23.900  9.702   23.691  1.00 39.83 ? 152 ASN B O   1 
ATOM   5352 C CB  . ASN B 1 152 ? 23.715  7.920   26.160  1.00 53.85 ? 152 ASN B CB  1 
ATOM   5353 C CG  . ASN B 1 152 ? 23.399  8.901   27.263  1.00 67.82 ? 152 ASN B CG  1 
ATOM   5354 O OD1 . ASN B 1 152 ? 22.744  9.919   27.037  1.00 73.95 ? 152 ASN B OD1 1 
ATOM   5355 N ND2 . ASN B 1 152 ? 23.870  8.605   28.470  1.00 73.11 ? 152 ASN B ND2 1 
ATOM   5356 N N   . LYS B 1 153 ? 23.790  7.642   22.804  1.00 35.91 ? 153 LYS B N   1 
ATOM   5357 C CA  . LYS B 1 153 ? 24.508  8.015   21.594  1.00 40.07 ? 153 LYS B CA  1 
ATOM   5358 C C   . LYS B 1 153 ? 23.680  8.983   20.746  1.00 37.70 ? 153 LYS B C   1 
ATOM   5359 O O   . LYS B 1 153 ? 24.182  10.017  20.296  1.00 37.81 ? 153 LYS B O   1 
ATOM   5360 C CB  . LYS B 1 153 ? 24.857  6.729   20.844  1.00 41.07 ? 153 LYS B CB  1 
ATOM   5361 C CG  . LYS B 1 153 ? 25.415  6.851   19.479  1.00 43.64 ? 153 LYS B CG  1 
ATOM   5362 C CD  . LYS B 1 153 ? 25.683  5.435   18.982  1.00 44.41 ? 153 LYS B CD  1 
ATOM   5363 C CE  . LYS B 1 153 ? 26.062  5.396   17.524  1.00 47.21 ? 153 LYS B CE  1 
ATOM   5364 N NZ  . LYS B 1 153 ? 27.315  6.127   17.255  1.00 50.24 ? 153 LYS B NZ  1 
ATOM   5365 N N   . GLY B 1 154 ? 22.397  8.680   20.550  1.00 36.88 ? 154 GLY B N   1 
ATOM   5366 C CA  . GLY B 1 154 ? 21.457  9.603   19.941  1.00 34.27 ? 154 GLY B CA  1 
ATOM   5367 C C   . GLY B 1 154 ? 21.592  9.840   18.452  1.00 35.58 ? 154 GLY B C   1 
ATOM   5368 O O   . GLY B 1 154 ? 20.702  10.469  17.871  1.00 34.84 ? 154 GLY B O   1 
ATOM   5369 N N   . ARG B 1 155 ? 22.658  9.368   17.808  1.00 34.51 ? 155 ARG B N   1 
ATOM   5370 C CA  . ARG B 1 155 ? 22.907  9.643   16.396  1.00 32.97 ? 155 ARG B CA  1 
ATOM   5371 C C   . ARG B 1 155 ? 23.989  8.692   15.900  1.00 31.28 ? 155 ARG B C   1 
ATOM   5372 O O   . ARG B 1 155 ? 24.595  7.960   16.681  1.00 35.69 ? 155 ARG B O   1 
ATOM   5373 C CB  . ARG B 1 155 ? 23.350  11.089  16.183  1.00 38.45 ? 155 ARG B CB  1 
ATOM   5374 C CG  . ARG B 1 155 ? 24.755  11.336  16.699  1.00 40.91 ? 155 ARG B CG  1 
ATOM   5375 C CD  . ARG B 1 155 ? 24.948  12.747  17.171  1.00 45.89 ? 155 ARG B CD  1 
ATOM   5376 N NE  . ARG B 1 155 ? 24.356  13.704  16.247  1.00 51.29 ? 155 ARG B NE  1 
ATOM   5377 C CZ  . ARG B 1 155 ? 23.451  14.610  16.598  1.00 57.30 ? 155 ARG B CZ  1 
ATOM   5378 N NH1 . ARG B 1 155 ? 23.031  14.682  17.858  1.00 58.46 ? 155 ARG B NH1 1 
ATOM   5379 N NH2 . ARG B 1 155 ? 22.967  15.442  15.686  1.00 59.50 ? 155 ARG B NH2 1 
ATOM   5380 N N   . ASN B 1 156 ? 24.228  8.720   14.587  1.00 27.62 ? 156 ASN B N   1 
ATOM   5381 C CA  . ASN B 1 156 ? 25.343  7.993   13.964  1.00 29.57 ? 156 ASN B CA  1 
ATOM   5382 C C   . ASN B 1 156 ? 25.258  6.480   14.194  1.00 33.15 ? 156 ASN B C   1 
ATOM   5383 O O   . ASN B 1 156 ? 26.268  5.824   14.470  1.00 36.39 ? 156 ASN B O   1 
ATOM   5384 C CB  . ASN B 1 156 ? 26.691  8.521   14.467  1.00 35.54 ? 156 ASN B CB  1 
ATOM   5385 C CG  . ASN B 1 156 ? 26.895  9.991   14.170  1.00 38.61 ? 156 ASN B CG  1 
ATOM   5386 O OD1 . ASN B 1 156 ? 27.503  10.720  14.961  1.00 48.97 ? 156 ASN B OD1 1 
ATOM   5387 N ND2 . ASN B 1 156 ? 26.404  10.433  13.026  1.00 34.18 ? 156 ASN B ND2 1 
ATOM   5388 N N   . TYR B 1 157 ? 24.057  5.922   14.084  1.00 23.51 ? 157 TYR B N   1 
ATOM   5389 C CA  . TYR B 1 157 ? 23.857  4.493   14.303  1.00 22.32 ? 157 TYR B CA  1 
ATOM   5390 C C   . TYR B 1 157 ? 24.295  3.696   13.076  1.00 27.59 ? 157 TYR B C   1 
ATOM   5391 O O   . TYR B 1 157 ? 24.208  4.167   11.940  1.00 28.16 ? 157 TYR B O   1 
ATOM   5392 C CB  . TYR B 1 157 ? 22.387  4.187   14.621  1.00 20.75 ? 157 TYR B CB  1 
ATOM   5393 C CG  . TYR B 1 157 ? 21.982  4.743   15.960  1.00 22.85 ? 157 TYR B CG  1 
ATOM   5394 C CD1 . TYR B 1 157 ? 22.312  4.077   17.133  1.00 22.06 ? 157 TYR B CD1 1 
ATOM   5395 C CD2 . TYR B 1 157 ? 21.299  5.955   16.055  1.00 28.47 ? 157 TYR B CD2 1 
ATOM   5396 C CE1 . TYR B 1 157 ? 21.952  4.593   18.375  1.00 25.88 ? 157 TYR B CE1 1 
ATOM   5397 C CE2 . TYR B 1 157 ? 20.945  6.488   17.287  1.00 26.72 ? 157 TYR B CE2 1 
ATOM   5398 C CZ  . TYR B 1 157 ? 21.271  5.806   18.442  1.00 28.24 ? 157 TYR B CZ  1 
ATOM   5399 O OH  . TYR B 1 157 ? 20.922  6.337   19.676  1.00 27.48 ? 157 TYR B OH  1 
ATOM   5400 N N   . THR B 1 158 ? 24.735  2.464   13.314  1.00 22.33 ? 158 THR B N   1 
ATOM   5401 C CA  . THR B 1 158 ? 25.142  1.569   12.237  1.00 22.67 ? 158 THR B CA  1 
ATOM   5402 C C   . THR B 1 158 ? 24.101  0.471   12.062  1.00 21.56 ? 158 THR B C   1 
ATOM   5403 O O   . THR B 1 158 ? 23.265  0.222   12.937  1.00 20.61 ? 158 THR B O   1 
ATOM   5404 C CB  . THR B 1 158 ? 26.509  0.936   12.523  1.00 23.80 ? 158 THR B CB  1 
ATOM   5405 O OG1 . THR B 1 158 ? 26.373  0.032   13.633  1.00 23.36 ? 158 THR B OG1 1 
ATOM   5406 C CG2 . THR B 1 158 ? 27.518  2.001   12.853  1.00 25.02 ? 158 THR B CG2 1 
ATOM   5407 N N   . GLN B 1 159 ? 24.161  -0.183  10.897  1.00 22.79 ? 159 GLN B N   1 
ATOM   5408 C CA  . GLN B 1 159 ? 23.257  -1.298  10.622  1.00 23.79 ? 159 GLN B CA  1 
ATOM   5409 C C   . GLN B 1 159 ? 23.407  -2.394  11.677  1.00 22.77 ? 159 GLN B C   1 
ATOM   5410 O O   . GLN B 1 159 ? 22.413  -2.977  12.131  1.00 21.00 ? 159 GLN B O   1 
ATOM   5411 C CB  . GLN B 1 159 ? 23.537  -1.836  9.212   1.00 22.92 ? 159 GLN B CB  1 
ATOM   5412 C CG  . GLN B 1 159 ? 22.713  -3.063  8.828   1.00 24.56 ? 159 GLN B CG  1 
ATOM   5413 C CD  . GLN B 1 159 ? 21.243  -2.752  8.577   1.00 27.01 ? 159 GLN B CD  1 
ATOM   5414 O OE1 . GLN B 1 159 ? 20.874  -1.614  8.296   1.00 23.75 ? 159 GLN B OE1 1 
ATOM   5415 N NE2 . GLN B 1 159 ? 20.404  -3.767  8.680   1.00 26.12 ? 159 GLN B NE2 1 
ATOM   5416 N N   . GLU B 1 160 ? 24.635  -2.638  12.127  1.00 21.88 ? 160 GLU B N   1 
ATOM   5417 C CA  . GLU B 1 160 ? 24.851  -3.675  13.131  1.00 22.00 ? 160 GLU B CA  1 
ATOM   5418 C C   . GLU B 1 160 ? 24.215  -3.311  14.468  1.00 21.44 ? 160 GLU B C   1 
ATOM   5419 O O   . GLU B 1 160 ? 23.659  -4.179  15.144  1.00 21.12 ? 160 GLU B O   1 
ATOM   5420 C CB  . GLU B 1 160 ? 26.343  -3.941  13.330  1.00 23.42 ? 160 GLU B CB  1 
ATOM   5421 C CG  . GLU B 1 160 ? 26.568  -5.162  14.216  1.00 29.00 ? 160 GLU B CG  1 
ATOM   5422 C CD  . GLU B 1 160 ? 26.127  -6.442  13.529  1.00 49.30 ? 160 GLU B CD  1 
ATOM   5423 O OE1 . GLU B 1 160 ? 26.090  -6.470  12.279  1.00 56.47 ? 160 GLU B OE1 1 
ATOM   5424 O OE2 . GLU B 1 160 ? 25.816  -7.419  14.238  1.00 59.51 ? 160 GLU B OE2 1 
ATOM   5425 N N   . GLU B 1 161 ? 24.321  -2.045  14.877  1.00 21.05 ? 161 GLU B N   1 
ATOM   5426 C CA  . GLU B 1 161 ? 23.689  -1.604  16.113  1.00 21.32 ? 161 GLU B CA  1 
ATOM   5427 C C   . GLU B 1 161 ? 22.179  -1.755  16.023  1.00 22.30 ? 161 GLU B C   1 
ATOM   5428 O O   . GLU B 1 161 ? 21.526  -2.220  16.967  1.00 19.27 ? 161 GLU B O   1 
ATOM   5429 C CB  . GLU B 1 161 ? 24.079  -0.156  16.401  1.00 20.80 ? 161 GLU B CB  1 
ATOM   5430 C CG  . GLU B 1 161 ? 25.562  -0.056  16.801  1.00 22.26 ? 161 GLU B CG  1 
ATOM   5431 C CD  . GLU B 1 161 ? 26.093  1.363   16.860  1.00 31.63 ? 161 GLU B CD  1 
ATOM   5432 O OE1 . GLU B 1 161 ? 25.447  2.287   16.339  1.00 27.08 ? 161 GLU B OE1 1 
ATOM   5433 O OE2 . GLU B 1 161 ? 27.185  1.560   17.428  1.00 32.30 ? 161 GLU B OE2 1 
ATOM   5434 N N   . LYS B 1 162 ? 21.618  -1.406  14.875  1.00 18.72 ? 162 LYS B N   1 
ATOM   5435 C CA  . LYS B 1 162 ? 20.177  -1.554  14.684  1.00 17.65 ? 162 LYS B CA  1 
ATOM   5436 C C   . LYS B 1 162 ? 19.756  -3.023  14.761  1.00 18.31 ? 162 LYS B C   1 
ATOM   5437 O O   . LYS B 1 162 ? 18.748  -3.362  15.406  1.00 19.49 ? 162 LYS B O   1 
ATOM   5438 C CB  . LYS B 1 162 ? 19.792  -0.930  13.342  1.00 17.74 ? 162 LYS B CB  1 
ATOM   5439 C CG  . LYS B 1 162 ? 18.322  -1.048  13.004  1.00 16.89 ? 162 LYS B CG  1 
ATOM   5440 C CD  . LYS B 1 162 ? 18.025  -0.367  11.667  1.00 20.82 ? 162 LYS B CD  1 
ATOM   5441 C CE  . LYS B 1 162 ? 18.834  -0.990  10.578  1.00 20.26 ? 162 LYS B CE  1 
ATOM   5442 N NZ  . LYS B 1 162 ? 18.414  -0.596  9.188   1.00 19.46 ? 162 LYS B NZ  1 
ATOM   5443 N N   . GLU B 1 163 ? 20.540  -3.912  14.147  1.00 22.70 ? 163 GLU B N   1 
ATOM   5444 C CA  . GLU B 1 163 ? 20.211  -5.336  14.164  1.00 21.28 ? 163 GLU B CA  1 
ATOM   5445 C C   . GLU B 1 163 ? 20.334  -5.921  15.562  1.00 22.93 ? 163 GLU B C   1 
ATOM   5446 O O   . GLU B 1 163 ? 19.547  -6.792  15.944  1.00 24.65 ? 163 GLU B O   1 
ATOM   5447 C CB  . GLU B 1 163 ? 21.108  -6.097  13.187  1.00 22.69 ? 163 GLU B CB  1 
ATOM   5448 C CG  . GLU B 1 163 ? 20.737  -5.841  11.739  1.00 24.21 ? 163 GLU B CG  1 
ATOM   5449 C CD  . GLU B 1 163 ? 21.722  -6.402  10.739  1.00 36.49 ? 163 GLU B CD  1 
ATOM   5450 O OE1 . GLU B 1 163 ? 21.504  -6.192  9.524   1.00 35.99 ? 163 GLU B OE1 1 
ATOM   5451 O OE2 . GLU B 1 163 ? 22.715  -7.048  11.153  1.00 45.06 ? 163 GLU B OE2 1 
ATOM   5452 N N   . TYR B 1 164 ? 21.338  -5.477  16.318  1.00 20.14 ? 164 TYR B N   1 
ATOM   5453 C CA  . TYR B 1 164 ? 21.484  -5.891  17.711  1.00 23.47 ? 164 TYR B CA  1 
ATOM   5454 C C   . TYR B 1 164 ? 20.248  -5.522  18.531  1.00 23.41 ? 164 TYR B C   1 
ATOM   5455 O O   . TYR B 1 164 ? 19.711  -6.348  19.278  1.00 21.87 ? 164 TYR B O   1 
ATOM   5456 C CB  . TYR B 1 164 ? 22.738  -5.238  18.291  1.00 23.04 ? 164 TYR B CB  1 
ATOM   5457 C CG  . TYR B 1 164 ? 22.978  -5.554  19.743  1.00 27.27 ? 164 TYR B CG  1 
ATOM   5458 C CD1 . TYR B 1 164 ? 23.281  -6.845  20.146  1.00 31.95 ? 164 TYR B CD1 1 
ATOM   5459 C CD2 . TYR B 1 164 ? 22.891  -4.568  20.713  1.00 27.41 ? 164 TYR B CD2 1 
ATOM   5460 C CE1 . TYR B 1 164 ? 23.504  -7.146  21.479  1.00 37.99 ? 164 TYR B CE1 1 
ATOM   5461 C CE2 . TYR B 1 164 ? 23.110  -4.863  22.057  1.00 32.75 ? 164 TYR B CE2 1 
ATOM   5462 C CZ  . TYR B 1 164 ? 23.418  -6.152  22.428  1.00 38.62 ? 164 TYR B CZ  1 
ATOM   5463 O OH  . TYR B 1 164 ? 23.643  -6.456  23.755  1.00 38.86 ? 164 TYR B OH  1 
ATOM   5464 N N   . VAL B 1 165 ? 19.783  -4.276  18.404  1.00 20.37 ? 165 VAL B N   1 
ATOM   5465 C CA  . VAL B 1 165 ? 18.581  -3.862  19.121  1.00 18.71 ? 165 VAL B CA  1 
ATOM   5466 C C   . VAL B 1 165 ? 17.400  -4.749  18.741  1.00 21.11 ? 165 VAL B C   1 
ATOM   5467 O O   . VAL B 1 165 ? 16.602  -5.157  19.600  1.00 20.67 ? 165 VAL B O   1 
ATOM   5468 C CB  . VAL B 1 165 ? 18.278  -2.374  18.851  1.00 18.44 ? 165 VAL B CB  1 
ATOM   5469 C CG1 . VAL B 1 165 ? 16.917  -1.978  19.496  1.00 18.69 ? 165 VAL B CG1 1 
ATOM   5470 C CG2 . VAL B 1 165 ? 19.401  -1.506  19.378  1.00 21.71 ? 165 VAL B CG2 1 
ATOM   5471 N N   . LEU B 1 166 ? 17.262  -5.054  17.443  1.00 18.74 ? 166 LEU B N   1 
ATOM   5472 C CA  . LEU B 1 166 ? 16.125  -5.849  16.985  1.00 19.27 ? 166 LEU B CA  1 
ATOM   5473 C C   . LEU B 1 166 ? 16.150  -7.233  17.611  1.00 21.19 ? 166 LEU B C   1 
ATOM   5474 O O   . LEU B 1 166 ? 15.113  -7.737  18.063  1.00 20.52 ? 166 LEU B O   1 
ATOM   5475 C CB  . LEU B 1 166 ? 16.141  -5.965  15.468  1.00 20.85 ? 166 LEU B CB  1 
ATOM   5476 C CG  . LEU B 1 166 ? 15.541  -4.803  14.715  1.00 29.90 ? 166 LEU B CG  1 
ATOM   5477 C CD1 . LEU B 1 166 ? 15.869  -4.952  13.225  1.00 32.48 ? 166 LEU B CD1 1 
ATOM   5478 C CD2 . LEU B 1 166 ? 14.028  -4.749  14.961  1.00 31.83 ? 166 LEU B CD2 1 
ATOM   5479 N N   . ASN B 1 167 ? 17.338  -7.836  17.691  1.00 18.94 ? 167 ASN B N   1 
ATOM   5480 C CA  . ASN B 1 167 ? 17.468  -9.157  18.300  1.00 20.05 ? 167 ASN B CA  1 
ATOM   5481 C C   . ASN B 1 167 ? 17.091  -9.130  19.770  1.00 21.60 ? 167 ASN B C   1 
ATOM   5482 O O   . ASN B 1 167 ? 16.449  -10.065 20.264  1.00 22.45 ? 167 ASN B O   1 
ATOM   5483 C CB  . ASN B 1 167 ? 18.894  -9.679  18.153  1.00 25.46 ? 167 ASN B CB  1 
ATOM   5484 C CG  . ASN B 1 167 ? 19.234  -10.037 16.721  1.00 43.22 ? 167 ASN B CG  1 
ATOM   5485 O OD1 . ASN B 1 167 ? 18.376  -10.494 15.962  1.00 46.95 ? 167 ASN B OD1 1 
ATOM   5486 N ND2 . ASN B 1 167 ? 20.492  -9.836  16.343  1.00 46.22 ? 167 ASN B ND2 1 
ATOM   5487 N N   . LYS B 1 168 ? 17.515  -8.093  20.497  1.00 18.75 ? 168 LYS B N   1 
ATOM   5488 C CA  . LYS B 1 168 ? 17.148  -8.003  21.909  1.00 17.13 ? 168 LYS B CA  1 
ATOM   5489 C C   . LYS B 1 168 ? 15.649  -7.770  22.067  1.00 17.00 ? 168 LYS B C   1 
ATOM   5490 O O   . LYS B 1 168 ? 15.020  -8.337  22.962  1.00 19.96 ? 168 LYS B O   1 
ATOM   5491 C CB  . LYS B 1 168 ? 17.932  -6.887  22.604  1.00 19.58 ? 168 LYS B CB  1 
ATOM   5492 C CG  . LYS B 1 168 ? 19.432  -7.140  22.716  1.00 23.30 ? 168 LYS B CG  1 
ATOM   5493 C CD  . LYS B 1 168 ? 19.712  -8.277  23.677  1.00 32.00 ? 168 LYS B CD  1 
ATOM   5494 C CE  . LYS B 1 168 ? 21.140  -8.230  24.194  1.00 44.33 ? 168 LYS B CE  1 
ATOM   5495 N NZ  . LYS B 1 168 ? 21.671  -9.592  24.508  1.00 51.82 ? 168 LYS B NZ  1 
ATOM   5496 N N   . TYR B 1 169 ? 15.063  -6.937  21.202  1.00 14.39 ? 169 TYR B N   1 
ATOM   5497 C CA  . TYR B 1 169 ? 13.618  -6.738  21.223  1.00 14.61 ? 169 TYR B CA  1 
ATOM   5498 C C   . TYR B 1 169 ? 12.876  -8.053  21.032  1.00 19.87 ? 169 TYR B C   1 
ATOM   5499 O O   . TYR B 1 169 ? 11.864  -8.308  21.709  1.00 19.47 ? 169 TYR B O   1 
ATOM   5500 C CB  . TYR B 1 169 ? 13.217  -5.731  20.139  1.00 15.08 ? 169 TYR B CB  1 
ATOM   5501 C CG  . TYR B 1 169 ? 13.423  -4.272  20.506  1.00 14.57 ? 169 TYR B CG  1 
ATOM   5502 C CD1 . TYR B 1 169 ? 14.201  -3.896  21.596  1.00 17.08 ? 169 TYR B CD1 1 
ATOM   5503 C CD2 . TYR B 1 169 ? 12.839  -3.261  19.749  1.00 16.21 ? 169 TYR B CD2 1 
ATOM   5504 C CE1 . TYR B 1 169 ? 14.379  -2.537  21.920  1.00 17.46 ? 169 TYR B CE1 1 
ATOM   5505 C CE2 . TYR B 1 169 ? 13.014  -1.915  20.074  1.00 17.21 ? 169 TYR B CE2 1 
ATOM   5506 C CZ  . TYR B 1 169 ? 13.788  -1.565  21.145  1.00 16.41 ? 169 TYR B CZ  1 
ATOM   5507 O OH  . TYR B 1 169 ? 13.957  -0.222  21.442  1.00 19.15 ? 169 TYR B OH  1 
ATOM   5508 N N   . PHE B 1 170 ? 13.344  -8.900  20.112  1.00 18.71 ? 170 PHE B N   1 
ATOM   5509 C CA  . PHE B 1 170 ? 12.621  -10.147 19.900  1.00 20.81 ? 170 PHE B CA  1 
ATOM   5510 C C   . PHE B 1 170 ? 12.801  -11.094 21.072  1.00 20.37 ? 170 PHE B C   1 
ATOM   5511 O O   . PHE B 1 170 ? 11.896  -11.879 21.369  1.00 18.62 ? 170 PHE B O   1 
ATOM   5512 C CB  . PHE B 1 170 ? 13.015  -10.797 18.573  1.00 20.07 ? 170 PHE B CB  1 
ATOM   5513 C CG  . PHE B 1 170 ? 12.138  -10.340 17.434  1.00 24.72 ? 170 PHE B CG  1 
ATOM   5514 C CD1 . PHE B 1 170 ? 10.844  -10.838 17.290  1.00 29.73 ? 170 PHE B CD1 1 
ATOM   5515 C CD2 . PHE B 1 170 ? 12.564  -9.348  16.558  1.00 27.05 ? 170 PHE B CD2 1 
ATOM   5516 C CE1 . PHE B 1 170 ? 10.008  -10.394 16.260  1.00 27.89 ? 170 PHE B CE1 1 
ATOM   5517 C CE2 . PHE B 1 170 ? 11.735  -8.902  15.524  1.00 29.86 ? 170 PHE B CE2 1 
ATOM   5518 C CZ  . PHE B 1 170 ? 10.454  -9.430  15.381  1.00 30.56 ? 170 PHE B CZ  1 
ATOM   5519 N N   . GLU B 1 171 ? 13.934  -11.012 21.770  1.00 17.87 ? 171 GLU B N   1 
ATOM   5520 C CA  . GLU B 1 171 ? 14.089  -11.793 22.992  1.00 20.09 ? 171 GLU B CA  1 
ATOM   5521 C C   . GLU B 1 171 ? 13.045  -11.407 24.025  1.00 20.54 ? 171 GLU B C   1 
ATOM   5522 O O   . GLU B 1 171 ? 12.493  -12.270 24.709  1.00 20.15 ? 171 GLU B O   1 
ATOM   5523 C CB  . GLU B 1 171 ? 15.494  -11.617 23.570  1.00 19.48 ? 171 GLU B CB  1 
ATOM   5524 C CG  . GLU B 1 171 ? 16.586  -12.172 22.683  1.00 28.16 ? 171 GLU B CG  1 
ATOM   5525 C CD  . GLU B 1 171 ? 17.992  -11.961 23.237  1.00 38.39 ? 171 GLU B CD  1 
ATOM   5526 O OE1 . GLU B 1 171 ? 18.138  -11.445 24.370  1.00 41.16 ? 171 GLU B OE1 1 
ATOM   5527 O OE2 . GLU B 1 171 ? 18.953  -12.321 22.525  1.00 42.64 ? 171 GLU B OE2 1 
ATOM   5528 N N   . ILE B 1 172 ? 12.759  -10.109 24.156  1.00 15.76 ? 172 ILE B N   1 
ATOM   5529 C CA  . ILE B 1 172 ? 11.713  -9.668  25.078  1.00 16.12 ? 172 ILE B CA  1 
ATOM   5530 C C   . ILE B 1 172 ? 10.345  -10.211 24.659  1.00 14.96 ? 172 ILE B C   1 
ATOM   5531 O O   . ILE B 1 172 ? 9.552   -10.647 25.496  1.00 17.61 ? 172 ILE B O   1 
ATOM   5532 C CB  . ILE B 1 172 ? 11.696  -8.130  25.152  1.00 17.54 ? 172 ILE B CB  1 
ATOM   5533 C CG1 . ILE B 1 172 ? 12.932  -7.589  25.885  1.00 18.86 ? 172 ILE B CG1 1 
ATOM   5534 C CG2 . ILE B 1 172 ? 10.375  -7.630  25.749  1.00 19.90 ? 172 ILE B CG2 1 
ATOM   5535 C CD1 . ILE B 1 172 ? 13.094  -8.064  27.302  1.00 19.23 ? 172 ILE B CD1 1 
ATOM   5536 N N   . ILE B 1 173 ? 10.031  -10.191 23.364  1.00 15.14 ? 173 ILE B N   1 
ATOM   5537 C CA  . ILE B 1 173 ? 8.708   -10.670 22.953  1.00 16.53 ? 173 ILE B CA  1 
ATOM   5538 C C   . ILE B 1 173 ? 8.543   -12.150 23.284  1.00 21.24 ? 173 ILE B C   1 
ATOM   5539 O O   . ILE B 1 173 ? 7.486   -12.584 23.758  1.00 17.90 ? 173 ILE B O   1 
ATOM   5540 C CB  . ILE B 1 173 ? 8.480   -10.388 21.462  1.00 17.87 ? 173 ILE B CB  1 
ATOM   5541 C CG1 . ILE B 1 173 ? 8.494   -8.876  21.249  1.00 20.09 ? 173 ILE B CG1 1 
ATOM   5542 C CG2 . ILE B 1 173 ? 7.152   -10.984 21.003  1.00 24.26 ? 173 ILE B CG2 1 
ATOM   5543 C CD1 . ILE B 1 173 ? 8.192   -8.451  19.800  1.00 23.48 ? 173 ILE B CD1 1 
ATOM   5544 N N   . LYS B 1 174 ? 9.597   -12.932 23.065  1.00 14.94 ? 174 LYS B N   1 
ATOM   5545 C CA  . LYS B 1 174 ? 9.567   -14.370 23.353  1.00 15.70 ? 174 LYS B CA  1 
ATOM   5546 C C   . LYS B 1 174 ? 9.371   -14.678 24.839  1.00 20.46 ? 174 LYS B C   1 
ATOM   5547 O O   . LYS B 1 174 ? 8.968   -15.798 25.172  1.00 22.40 ? 174 LYS B O   1 
ATOM   5548 C CB  . LYS B 1 174 ? 10.858  -15.028 22.867  1.00 22.67 ? 174 LYS B CB  1 
ATOM   5549 C CG  . LYS B 1 174 ? 10.903  -15.174 21.373  1.00 27.71 ? 174 LYS B CG  1 
ATOM   5550 C CD  . LYS B 1 174 ? 12.114  -15.959 20.925  1.00 30.07 ? 174 LYS B CD  1 
ATOM   5551 C CE  . LYS B 1 174 ? 12.288  -15.785 19.434  1.00 39.63 ? 174 LYS B CE  1 
ATOM   5552 N NZ  . LYS B 1 174 ? 13.674  -15.382 19.062  1.00 48.20 ? 174 LYS B NZ  1 
ATOM   5553 N N   . LYS B 1 175 ? 9.669   -13.747 25.742  1.00 17.61 ? 175 LYS B N   1 
ATOM   5554 C CA  . LYS B 1 175 ? 9.461   -13.962 27.175  1.00 18.23 ? 175 LYS B CA  1 
ATOM   5555 C C   . LYS B 1 175 ? 8.144   -13.383 27.673  1.00 19.23 ? 175 LYS B C   1 
ATOM   5556 O O   . LYS B 1 175 ? 7.855   -13.477 28.874  1.00 20.12 ? 175 LYS B O   1 
ATOM   5557 C CB  . LYS B 1 175 ? 10.605  -13.342 27.996  1.00 23.38 ? 175 LYS B CB  1 
ATOM   5558 C CG  . LYS B 1 175 ? 11.958  -13.382 27.339  1.00 39.52 ? 175 LYS B CG  1 
ATOM   5559 C CD  . LYS B 1 175 ? 13.081  -13.632 28.316  1.00 48.04 ? 175 LYS B CD  1 
ATOM   5560 C CE  . LYS B 1 175 ? 13.160  -12.525 29.362  1.00 54.95 ? 175 LYS B CE  1 
ATOM   5561 N NZ  . LYS B 1 175 ? 14.061  -11.410 28.941  1.00 60.71 ? 175 LYS B NZ  1 
ATOM   5562 N N   . THR B 1 176 ? 7.343   -12.772 26.791  1.00 14.56 ? 176 THR B N   1 
ATOM   5563 C CA  . THR B 1 176 ? 6.218   -11.962 27.262  1.00 16.33 ? 176 THR B CA  1 
ATOM   5564 C C   . THR B 1 176 ? 5.112   -12.820 27.862  1.00 21.70 ? 176 THR B C   1 
ATOM   5565 O O   . THR B 1 176 ? 4.667   -12.558 28.986  1.00 20.42 ? 176 THR B O   1 
ATOM   5566 C CB  . THR B 1 176 ? 5.690   -11.075 26.131  1.00 17.92 ? 176 THR B CB  1 
ATOM   5567 O OG1 . THR B 1 176 ? 6.719   -10.146 25.787  1.00 19.67 ? 176 THR B OG1 1 
ATOM   5568 C CG2 . THR B 1 176 ? 4.437   -10.292 26.558  1.00 17.75 ? 176 THR B CG2 1 
ATOM   5569 N N   . LEU B 1 177 ? 4.643   -13.848 27.149  1.00 17.44 ? 177 LEU B N   1 
ATOM   5570 C CA  . LEU B 1 177 ? 3.584   -14.653 27.763  1.00 22.73 ? 177 LEU B CA  1 
ATOM   5571 C C   . LEU B 1 177 ? 4.085   -15.335 29.030  1.00 19.99 ? 177 LEU B C   1 
ATOM   5572 O O   . LEU B 1 177 ? 3.325   -15.505 29.995  1.00 21.34 ? 177 LEU B O   1 
ATOM   5573 C CB  . LEU B 1 177 ? 3.021   -15.680 26.769  1.00 21.84 ? 177 LEU B CB  1 
ATOM   5574 C CG  . LEU B 1 177 ? 2.318   -15.050 25.562  1.00 29.56 ? 177 LEU B CG  1 
ATOM   5575 C CD1 . LEU B 1 177 ? 1.729   -16.117 24.683  1.00 29.51 ? 177 LEU B CD1 1 
ATOM   5576 C CD2 . LEU B 1 177 ? 1.236   -14.055 25.982  1.00 34.00 ? 177 LEU B CD2 1 
ATOM   5577 N N   . SER B 1 178 ? 5.370   -15.678 29.068  1.00 19.48 ? 178 SER B N   1 
ATOM   5578 C CA  . SER B 1 178 ? 5.932   -16.352 30.230  1.00 18.25 ? 178 SER B CA  1 
ATOM   5579 C C   . SER B 1 178 ? 5.842   -15.490 31.487  1.00 17.09 ? 178 SER B C   1 
ATOM   5580 O O   . SER B 1 178 ? 5.610   -16.010 32.579  1.00 18.69 ? 178 SER B O   1 
ATOM   5581 C CB  . SER B 1 178 ? 7.384   -16.739 29.967  1.00 22.27 ? 178 SER B CB  1 
ATOM   5582 O OG  . SER B 1 178 ? 7.445   -17.759 28.992  1.00 31.29 ? 178 SER B OG  1 
ATOM   5583 N N   . ILE B 1 179 ? 6.047   -14.174 31.370  1.00 19.20 ? 179 ILE B N   1 
ATOM   5584 C CA  . ILE B 1 179 ? 6.038   -13.392 32.604  1.00 15.65 ? 179 ILE B CA  1 
ATOM   5585 C C   . ILE B 1 179 ? 4.617   -13.330 33.177  1.00 14.89 ? 179 ILE B C   1 
ATOM   5586 O O   . ILE B 1 179 ? 4.439   -13.333 34.409  1.00 16.05 ? 179 ILE B O   1 
ATOM   5587 C CB  . ILE B 1 179 ? 6.658   -11.988 32.384  1.00 20.03 ? 179 ILE B CB  1 
ATOM   5588 C CG1 . ILE B 1 179 ? 6.803   -11.239 33.715  1.00 23.02 ? 179 ILE B CG1 1 
ATOM   5589 C CG2 . ILE B 1 179 ? 5.816   -11.131 31.460  1.00 16.52 ? 179 ILE B CG2 1 
ATOM   5590 C CD1 . ILE B 1 179 ? 7.896   -11.783 34.601  1.00 28.07 ? 179 ILE B CD1 1 
ATOM   5591 N N   . TYR B 1 180 ? 3.586   -13.279 32.317  1.00 12.87 ? 180 TYR B N   1 
ATOM   5592 C CA  . TYR B 1 180 ? 2.216   -13.272 32.833  1.00 12.41 ? 180 TYR B CA  1 
ATOM   5593 C C   . TYR B 1 180 ? 1.899   -14.573 33.554  1.00 18.35 ? 180 TYR B C   1 
ATOM   5594 O O   . TYR B 1 180 ? 1.254   -14.562 34.609  1.00 18.05 ? 180 TYR B O   1 
ATOM   5595 C CB  . TYR B 1 180 ? 1.205   -13.030 31.716  1.00 13.97 ? 180 TYR B CB  1 
ATOM   5596 C CG  . TYR B 1 180 ? 1.218   -11.602 31.237  1.00 11.32 ? 180 TYR B CG  1 
ATOM   5597 C CD1 . TYR B 1 180 ? 0.537   -10.612 31.938  1.00 13.94 ? 180 TYR B CD1 1 
ATOM   5598 C CD2 . TYR B 1 180 ? 1.948   -11.240 30.092  1.00 12.07 ? 180 TYR B CD2 1 
ATOM   5599 C CE1 . TYR B 1 180 ? 0.573   -9.289  31.516  1.00 13.85 ? 180 TYR B CE1 1 
ATOM   5600 C CE2 . TYR B 1 180 ? 1.989   -9.904  29.657  1.00 10.61 ? 180 TYR B CE2 1 
ATOM   5601 C CZ  . TYR B 1 180 ? 1.312   -8.961  30.384  1.00 14.10 ? 180 TYR B CZ  1 
ATOM   5602 O OH  . TYR B 1 180 ? 1.353   -7.662  29.964  1.00 12.36 ? 180 TYR B OH  1 
ATOM   5603 N N   . ARG B 1 181 ? 2.331   -15.702 32.986  1.00 15.67 ? 181 ARG B N   1 
ATOM   5604 C CA  . ARG B 1 181 ? 2.161   -16.976 33.671  1.00 15.78 ? 181 ARG B CA  1 
ATOM   5605 C C   . ARG B 1 181 ? 2.860   -16.963 35.025  1.00 15.37 ? 181 ARG B C   1 
ATOM   5606 O O   . ARG B 1 181 ? 2.312   -17.453 36.019  1.00 17.72 ? 181 ARG B O   1 
ATOM   5607 C CB  . ARG B 1 181 ? 2.692   -18.115 32.805  1.00 16.23 ? 181 ARG B CB  1 
ATOM   5608 C CG  . ARG B 1 181 ? 1.819   -18.481 31.621  1.00 17.35 ? 181 ARG B CG  1 
ATOM   5609 C CD  . ARG B 1 181 ? 2.535   -19.549 30.788  1.00 20.81 ? 181 ARG B CD  1 
ATOM   5610 N NE  . ARG B 1 181 ? 1.939   -19.748 29.485  1.00 35.08 ? 181 ARG B NE  1 
ATOM   5611 C CZ  . ARG B 1 181 ? 2.601   -19.564 28.350  1.00 39.89 ? 181 ARG B CZ  1 
ATOM   5612 N NH1 . ARG B 1 181 ? 3.874   -19.180 28.376  1.00 30.28 ? 181 ARG B NH1 1 
ATOM   5613 N NH2 . ARG B 1 181 ? 1.988   -19.768 27.193  1.00 48.35 ? 181 ARG B NH2 1 
ATOM   5614 N N   . GLU B 1 182 ? 4.064   -16.388 35.087  1.00 17.36 ? 182 GLU B N   1 
ATOM   5615 C CA  . GLU B 1 182 ? 4.847   -16.442 36.318  1.00 16.83 ? 182 GLU B CA  1 
ATOM   5616 C C   . GLU B 1 182 ? 4.200   -15.625 37.431  1.00 17.68 ? 182 GLU B C   1 
ATOM   5617 O O   . GLU B 1 182 ? 4.095   -16.090 38.572  1.00 17.02 ? 182 GLU B O   1 
ATOM   5618 C CB  . GLU B 1 182 ? 6.265   -15.944 36.058  1.00 20.65 ? 182 GLU B CB  1 
ATOM   5619 C CG  . GLU B 1 182 ? 7.050   -15.639 37.335  1.00 27.89 ? 182 GLU B CG  1 
ATOM   5620 C CD  . GLU B 1 182 ? 8.528   -15.356 37.091  1.00 46.84 ? 182 GLU B CD  1 
ATOM   5621 O OE1 . GLU B 1 182 ? 9.305   -15.394 38.074  1.00 52.93 ? 182 GLU B OE1 1 
ATOM   5622 O OE2 . GLU B 1 182 ? 8.918   -15.105 35.927  1.00 47.75 ? 182 GLU B OE2 1 
ATOM   5623 N N   . ILE B 1 183 ? 3.795   -14.382 37.130  1.00 14.43 ? 183 ILE B N   1 
ATOM   5624 C CA  . ILE B 1 183 ? 3.242   -13.553 38.198  1.00 14.32 ? 183 ILE B CA  1 
ATOM   5625 C C   . ILE B 1 183 ? 1.896   -14.104 38.652  1.00 17.32 ? 183 ILE B C   1 
ATOM   5626 O O   . ILE B 1 183 ? 1.535   -13.994 39.833  1.00 17.65 ? 183 ILE B O   1 
ATOM   5627 C CB  . ILE B 1 183 ? 3.163   -12.071 37.759  1.00 19.64 ? 183 ILE B CB  1 
ATOM   5628 C CG1 . ILE B 1 183 ? 2.185   -11.871 36.616  1.00 18.29 ? 183 ILE B CG1 1 
ATOM   5629 C CG2 . ILE B 1 183 ? 4.541   -11.562 37.373  1.00 19.07 ? 183 ILE B CG2 1 
ATOM   5630 C CD1 . ILE B 1 183 ? 0.902   -11.263 37.057  1.00 23.05 ? 183 ILE B CD1 1 
ATOM   5631 N N   . LYS B 1 184 ? 1.158   -14.764 37.749  1.00 15.78 ? 184 LYS B N   1 
ATOM   5632 C CA  . LYS B 1 184 ? -0.081  -15.417 38.166  1.00 15.44 ? 184 LYS B CA  1 
ATOM   5633 C C   . LYS B 1 184 ? 0.202   -16.582 39.108  1.00 15.78 ? 184 LYS B C   1 
ATOM   5634 O O   . LYS B 1 184 ? -0.418  -16.707 40.177  1.00 19.74 ? 184 LYS B O   1 
ATOM   5635 C CB  . LYS B 1 184 ? -0.847  -15.884 36.930  1.00 16.83 ? 184 LYS B CB  1 
ATOM   5636 C CG  . LYS B 1 184 ? -2.208  -16.516 37.228  1.00 21.72 ? 184 LYS B CG  1 
ATOM   5637 C CD  . LYS B 1 184 ? -2.787  -17.081 35.931  1.00 25.96 ? 184 LYS B CD  1 
ATOM   5638 C CE  . LYS B 1 184 ? -4.079  -17.810 36.173  1.00 32.51 ? 184 LYS B CE  1 
ATOM   5639 N NZ  . LYS B 1 184 ? -3.870  -18.972 37.081  1.00 45.04 ? 184 LYS B NZ  1 
ATOM   5640 N N   . GLU B 1 185 ? 1.149   -17.446 38.730  1.00 16.45 ? 185 GLU B N   1 
ATOM   5641 C CA  . GLU B 1 185 ? 1.446   -18.609 39.562  1.00 17.76 ? 185 GLU B CA  1 
ATOM   5642 C C   . GLU B 1 185 ? 2.019   -18.220 40.915  1.00 19.07 ? 185 GLU B C   1 
ATOM   5643 O O   . GLU B 1 185 ? 1.830   -18.953 41.901  1.00 19.18 ? 185 GLU B O   1 
ATOM   5644 C CB  . GLU B 1 185 ? 2.427   -19.537 38.851  1.00 21.82 ? 185 GLU B CB  1 
ATOM   5645 C CG  . GLU B 1 185 ? 1.836   -20.172 37.631  1.00 37.54 ? 185 GLU B CG  1 
ATOM   5646 C CD  . GLU B 1 185 ? 2.833   -20.316 36.499  1.00 44.19 ? 185 GLU B CD  1 
ATOM   5647 O OE1 . GLU B 1 185 ? 4.055   -20.342 36.759  1.00 44.00 ? 185 GLU B OE1 1 
ATOM   5648 O OE2 . GLU B 1 185 ? 2.381   -20.404 35.343  1.00 48.06 ? 185 GLU B OE2 1 
ATOM   5649 N N   . GLU B 1 186 ? 2.718   -17.090 40.991  1.00 18.39 ? 186 GLU B N   1 
ATOM   5650 C CA  . GLU B 1 186 ? 3.317   -16.660 42.247  1.00 16.72 ? 186 GLU B CA  1 
ATOM   5651 C C   . GLU B 1 186 ? 2.355   -15.872 43.111  1.00 16.14 ? 186 GLU B C   1 
ATOM   5652 O O   . GLU B 1 186 ? 2.760   -15.412 44.180  1.00 19.32 ? 186 GLU B O   1 
ATOM   5653 C CB  . GLU B 1 186 ? 4.572   -15.810 42.012  1.00 21.09 ? 186 GLU B CB  1 
ATOM   5654 C CG  . GLU B 1 186 ? 5.644   -16.546 41.248  1.00 21.33 ? 186 GLU B CG  1 
ATOM   5655 C CD  . GLU B 1 186 ? 6.919   -15.744 41.076  1.00 26.90 ? 186 GLU B CD  1 
ATOM   5656 O OE1 . GLU B 1 186 ? 6.836   -14.540 40.754  1.00 27.80 ? 186 GLU B OE1 1 
ATOM   5657 O OE2 . GLU B 1 186 ? 8.008   -16.333 41.235  1.00 29.31 ? 186 GLU B OE2 1 
ATOM   5658 N N   . GLY B 1 187 ? 1.107   -15.711 42.683  1.00 17.30 ? 187 GLY B N   1 
ATOM   5659 C CA  . GLY B 1 187 ? 0.176   -14.926 43.467  1.00 16.28 ? 187 GLY B CA  1 
ATOM   5660 C C   . GLY B 1 187 ? 0.481   -13.446 43.486  1.00 17.48 ? 187 GLY B C   1 
ATOM   5661 O O   . GLY B 1 187 ? -0.016  -12.723 44.358  1.00 18.24 ? 187 GLY B O   1 
ATOM   5662 N N   . LYS B 1 188 ? 1.315   -12.969 42.565  1.00 14.94 ? 188 LYS B N   1 
ATOM   5663 C CA  . LYS B 1 188 ? 1.628   -11.543 42.515  1.00 13.50 ? 188 LYS B CA  1 
ATOM   5664 C C   . LYS B 1 188 ? 0.604   -10.741 41.726  1.00 12.67 ? 188 LYS B C   1 
ATOM   5665 O O   . LYS B 1 188 ? 0.587   -9.501  41.829  1.00 15.30 ? 188 LYS B O   1 
ATOM   5666 C CB  . LYS B 1 188 ? 3.017   -11.334 41.896  1.00 18.29 ? 188 LYS B CB  1 
ATOM   5667 C CG  . LYS B 1 188 ? 4.187   -11.749 42.754  1.00 18.04 ? 188 LYS B CG  1 
ATOM   5668 C CD  . LYS B 1 188 ? 5.490   -11.653 41.935  1.00 25.23 ? 188 LYS B CD  1 
ATOM   5669 C CE  . LYS B 1 188 ? 6.737   -11.688 42.845  1.00 33.54 ? 188 LYS B CE  1 
ATOM   5670 N NZ  . LYS B 1 188 ? 7.019   -10.346 43.472  1.00 38.13 ? 188 LYS B NZ  1 
ATOM   5671 N N   . GLY B 1 189 ? -0.254  -11.394 40.962  1.00 13.94 ? 189 GLY B N   1 
ATOM   5672 C CA  . GLY B 1 189 ? -1.311  -10.703 40.259  1.00 17.52 ? 189 GLY B CA  1 
ATOM   5673 C C   . GLY B 1 189 ? -2.263  -11.707 39.662  1.00 15.11 ? 189 GLY B C   1 
ATOM   5674 O O   . GLY B 1 189 ? -1.930  -12.890 39.493  1.00 14.49 ? 189 GLY B O   1 
ATOM   5675 N N   . SER B 1 190 ? -3.472  -11.238 39.406  1.00 15.07 ? 190 SER B N   1 
ATOM   5676 C CA  . SER B 1 190 ? -4.447  -12.019 38.667  1.00 19.51 ? 190 SER B CA  1 
ATOM   5677 C C   . SER B 1 190 ? -4.362  -11.593 37.213  1.00 16.34 ? 190 SER B C   1 
ATOM   5678 O O   . SER B 1 190 ? -4.016  -10.453 36.921  1.00 14.44 ? 190 SER B O   1 
ATOM   5679 C CB  . SER B 1 190 ? -5.865  -11.784 39.207  1.00 18.07 ? 190 SER B CB  1 
ATOM   5680 O OG  . SER B 1 190 ? -5.963  -12.231 40.558  1.00 16.31 ? 190 SER B OG  1 
ATOM   5681 N N   . VAL B 1 191 ? -4.678  -12.510 36.300  1.00 16.14 ? 191 VAL B N   1 
ATOM   5682 C CA  . VAL B 1 191 ? -4.778  -12.169 34.886  1.00 16.24 ? 191 VAL B CA  1 
ATOM   5683 C C   . VAL B 1 191 ? -6.194  -12.464 34.423  1.00 18.12 ? 191 VAL B C   1 
ATOM   5684 O O   . VAL B 1 191 ? -6.687  -13.582 34.609  1.00 19.30 ? 191 VAL B O   1 
ATOM   5685 C CB  . VAL B 1 191 ? -3.762  -12.947 34.031  1.00 13.64 ? 191 VAL B CB  1 
ATOM   5686 C CG1 . VAL B 1 191 ? -3.836  -12.480 32.576  1.00 16.54 ? 191 VAL B CG1 1 
ATOM   5687 C CG2 . VAL B 1 191 ? -2.370  -12.750 34.549  1.00 15.34 ? 191 VAL B CG2 1 
ATOM   5688 N N   . SER B 1 192 ? -6.830  -11.461 33.822  1.00 13.58 ? 192 SER B N   1 
ATOM   5689 C CA  . SER B 1 192 ? -8.157  -11.563 33.235  1.00 13.30 ? 192 SER B CA  1 
ATOM   5690 C C   . SER B 1 192 ? -8.045  -11.571 31.718  1.00 14.82 ? 192 SER B C   1 
ATOM   5691 O O   . SER B 1 192 ? -6.965  -11.429 31.135  1.00 13.44 ? 192 SER B O   1 
ATOM   5692 C CB  . SER B 1 192 ? -9.031  -10.409 33.700  1.00 15.38 ? 192 SER B CB  1 
ATOM   5693 O OG  . SER B 1 192 ? -8.545  -9.189  33.164  1.00 14.34 ? 192 SER B OG  1 
ATOM   5694 N N   . THR B 1 193 ? -9.188  -11.752 31.073  1.00 15.42 ? 193 THR B N   1 
ATOM   5695 C CA  . THR B 1 193 ? -9.284  -11.605 29.634  1.00 15.46 ? 193 THR B CA  1 
ATOM   5696 C C   . THR B 1 193 ? -10.586 -10.873 29.340  1.00 16.54 ? 193 THR B C   1 
ATOM   5697 O O   . THR B 1 193 ? -11.344 -10.524 30.252  1.00 14.61 ? 193 THR B O   1 
ATOM   5698 C CB  . THR B 1 193 ? -9.155  -12.967 28.918  1.00 16.80 ? 193 THR B CB  1 
ATOM   5699 O OG1 . THR B 1 193 ? -8.885  -12.754 27.521  1.00 18.62 ? 193 THR B OG1 1 
ATOM   5700 C CG2 . THR B 1 193 ? -10.421 -13.869 29.049  1.00 16.97 ? 193 THR B CG2 1 
ATOM   5701 N N   . SER B 1 194 ? -10.802 -10.573 28.065  1.00 16.19 ? 194 SER B N   1 
ATOM   5702 C CA  . SER B 1 194 ? -12.006 -9.926  27.561  1.00 16.34 ? 194 SER B CA  1 
ATOM   5703 C C   . SER B 1 194 ? -12.607 -10.795 26.470  1.00 14.97 ? 194 SER B C   1 
ATOM   5704 O O   . SER B 1 194 ? -11.905 -11.604 25.855  1.00 16.63 ? 194 SER B O   1 
ATOM   5705 C CB  . SER B 1 194 ? -11.697 -8.541  26.973  1.00 16.94 ? 194 SER B CB  1 
ATOM   5706 O OG  . SER B 1 194 ? -11.220 -7.673  27.975  1.00 15.88 ? 194 SER B OG  1 
ATOM   5707 N N   . PRO B 1 195 ? -13.910 -10.610 26.155  1.00 15.85 ? 195 PRO B N   1 
ATOM   5708 C CA  . PRO B 1 195 ? -14.453 -11.196 24.917  1.00 14.20 ? 195 PRO B CA  1 
ATOM   5709 C C   . PRO B 1 195 ? -13.483 -11.006 23.752  1.00 16.51 ? 195 PRO B C   1 
ATOM   5710 O O   . PRO B 1 195 ? -12.898 -9.924  23.600  1.00 15.85 ? 195 PRO B O   1 
ATOM   5711 C CB  . PRO B 1 195 ? -15.752 -10.421 24.686  1.00 19.86 ? 195 PRO B CB  1 
ATOM   5712 C CG  . PRO B 1 195 ? -16.084 -9.787  26.010  1.00 27.43 ? 195 PRO B CG  1 
ATOM   5713 C CD  . PRO B 1 195 ? -14.893 -9.816  26.905  1.00 17.84 ? 195 PRO B CD  1 
ATOM   5714 N N   . TYR B 1 196 ? -13.377 -12.032 22.901  1.00 17.20 ? 196 TYR B N   1 
ATOM   5715 C CA  . TYR B 1 196 ? -12.172 -12.297 22.104  1.00 19.89 ? 196 TYR B CA  1 
ATOM   5716 C C   . TYR B 1 196 ? -11.626 -11.074 21.362  1.00 15.07 ? 196 TYR B C   1 
ATOM   5717 O O   . TYR B 1 196 ? -10.427 -10.775 21.450  1.00 16.04 ? 196 TYR B O   1 
ATOM   5718 C CB  . TYR B 1 196 ? -12.464 -13.430 21.112  1.00 16.51 ? 196 TYR B CB  1 
ATOM   5719 C CG  . TYR B 1 196 ? -11.225 -14.210 20.711  1.00 17.66 ? 196 TYR B CG  1 
ATOM   5720 C CD1 . TYR B 1 196 ? -10.298 -13.659 19.830  1.00 17.39 ? 196 TYR B CD1 1 
ATOM   5721 C CD2 . TYR B 1 196 ? -10.975 -15.489 21.222  1.00 20.14 ? 196 TYR B CD2 1 
ATOM   5722 C CE1 . TYR B 1 196 ? -9.145  -14.343 19.469  1.00 19.12 ? 196 TYR B CE1 1 
ATOM   5723 C CE2 . TYR B 1 196 ? -9.820  -16.198 20.857  1.00 18.15 ? 196 TYR B CE2 1 
ATOM   5724 C CZ  . TYR B 1 196 ? -8.922  -15.628 19.967  1.00 24.70 ? 196 TYR B CZ  1 
ATOM   5725 O OH  . TYR B 1 196 ? -7.776  -16.312 19.605  1.00 23.16 ? 196 TYR B OH  1 
ATOM   5726 N N   . TYR B 1 197 ? -12.450 -10.418 20.536  1.00 16.99 ? 197 TYR B N   1 
ATOM   5727 C CA  . TYR B 1 197 ? -11.944 -9.328  19.706  1.00 13.45 ? 197 TYR B CA  1 
ATOM   5728 C C   . TYR B 1 197 ? -12.283 -7.960  20.266  1.00 15.54 ? 197 TYR B C   1 
ATOM   5729 O O   . TYR B 1 197 ? -12.297 -6.976  19.514  1.00 15.69 ? 197 TYR B O   1 
ATOM   5730 C CB  . TYR B 1 197 ? -12.440 -9.477  18.263  1.00 15.77 ? 197 TYR B CB  1 
ATOM   5731 C CG  . TYR B 1 197 ? -11.811 -10.676 17.610  1.00 15.87 ? 197 TYR B CG  1 
ATOM   5732 C CD1 . TYR B 1 197 ? -10.477 -10.645 17.175  1.00 16.98 ? 197 TYR B CD1 1 
ATOM   5733 C CD2 . TYR B 1 197 ? -12.515 -11.863 17.486  1.00 20.61 ? 197 TYR B CD2 1 
ATOM   5734 C CE1 . TYR B 1 197 ? -9.888  -11.762 16.608  1.00 19.10 ? 197 TYR B CE1 1 
ATOM   5735 C CE2 . TYR B 1 197 ? -11.948 -12.975 16.911  1.00 17.58 ? 197 TYR B CE2 1 
ATOM   5736 C CZ  . TYR B 1 197 ? -10.617 -12.932 16.490  1.00 21.99 ? 197 TYR B CZ  1 
ATOM   5737 O OH  . TYR B 1 197 ? -10.032 -14.054 15.919  1.00 26.44 ? 197 TYR B OH  1 
ATOM   5738 N N   . HIS B 1 198 ? -12.543 -7.881  21.567  1.00 14.04 ? 198 HIS B N   1 
ATOM   5739 C CA  . HIS B 1 198 ? -12.785 -6.602  22.244  1.00 17.21 ? 198 HIS B CA  1 
ATOM   5740 C C   . HIS B 1 198 ? -13.976 -5.876  21.618  1.00 18.05 ? 198 HIS B C   1 
ATOM   5741 O O   . HIS B 1 198 ? -13.863 -4.694  21.270  1.00 13.59 ? 198 HIS B O   1 
ATOM   5742 C CB  . HIS B 1 198 ? -11.495 -5.763  22.185  1.00 16.90 ? 198 HIS B CB  1 
ATOM   5743 C CG  . HIS B 1 198 ? -11.429 -4.608  23.143  1.00 12.52 ? 198 HIS B CG  1 
ATOM   5744 N ND1 . HIS B 1 198 ? -11.811 -3.331  22.789  1.00 14.50 ? 198 HIS B ND1 1 
ATOM   5745 C CD2 . HIS B 1 198 ? -10.937 -4.517  24.406  1.00 12.47 ? 198 HIS B CD2 1 
ATOM   5746 C CE1 . HIS B 1 198 ? -11.611 -2.513  23.807  1.00 15.06 ? 198 HIS B CE1 1 
ATOM   5747 N NE2 . HIS B 1 198 ? -11.078 -3.201  24.801  1.00 13.95 ? 198 HIS B NE2 1 
ATOM   5748 N N   . PRO B 1 199 ? -15.134 -6.520  21.475  1.00 18.63 ? 199 PRO B N   1 
ATOM   5749 C CA  . PRO B 1 199 ? -16.319 -5.816  20.972  1.00 19.71 ? 199 PRO B CA  1 
ATOM   5750 C C   . PRO B 1 199 ? -17.048 -5.052  22.070  1.00 19.67 ? 199 PRO B C   1 
ATOM   5751 O O   . PRO B 1 199 ? -16.756 -5.174  23.264  1.00 18.02 ? 199 PRO B O   1 
ATOM   5752 C CB  . PRO B 1 199 ? -17.200 -6.956  20.468  1.00 19.89 ? 199 PRO B CB  1 
ATOM   5753 C CG  . PRO B 1 199 ? -16.939 -8.042  21.485  1.00 16.19 ? 199 PRO B CG  1 
ATOM   5754 C CD  . PRO B 1 199 ? -15.446 -7.928  21.794  1.00 17.99 ? 199 PRO B CD  1 
ATOM   5755 N N   . LEU B 1 200 ? -18.057 -4.290  21.634  1.00 19.17 ? 200 LEU B N   1 
ATOM   5756 C CA  . LEU B 1 200 ? -19.039 -3.666  22.528  1.00 22.24 ? 200 LEU B CA  1 
ATOM   5757 C C   . LEU B 1 200 ? -20.178 -4.662  22.746  1.00 19.54 ? 200 LEU B C   1 
ATOM   5758 O O   . LEU B 1 200 ? -21.197 -4.638  22.053  1.00 18.08 ? 200 LEU B O   1 
ATOM   5759 C CB  . LEU B 1 200 ? -19.536 -2.347  21.946  1.00 22.04 ? 200 LEU B CB  1 
ATOM   5760 C CG  . LEU B 1 200 ? -18.600 -1.145  22.099  1.00 23.77 ? 200 LEU B CG  1 
ATOM   5761 C CD1 . LEU B 1 200 ? -18.937 -0.049  21.135  1.00 26.24 ? 200 LEU B CD1 1 
ATOM   5762 C CD2 . LEU B 1 200 ? -18.654 -0.620  23.534  1.00 26.26 ? 200 LEU B CD2 1 
ATOM   5763 N N   . ILE B 1 201 ? -20.003 -5.540  23.736  1.00 16.69 ? 201 ILE B N   1 
ATOM   5764 C CA  . ILE B 1 201 ? -20.989 -6.577  24.048  1.00 15.82 ? 201 ILE B CA  1 
ATOM   5765 C C   . ILE B 1 201 ? -22.402 -6.016  24.227  1.00 15.92 ? 201 ILE B C   1 
ATOM   5766 O O   . ILE B 1 201 ? -23.357 -6.624  23.719  1.00 17.98 ? 201 ILE B O   1 
ATOM   5767 C CB  . ILE B 1 201 ? -20.550 -7.374  25.288  1.00 17.27 ? 201 ILE B CB  1 
ATOM   5768 C CG1 . ILE B 1 201 ? -19.258 -8.134  25.009  1.00 18.20 ? 201 ILE B CG1 1 
ATOM   5769 C CG2 . ILE B 1 201 ? -21.680 -8.303  25.777  1.00 19.56 ? 201 ILE B CG2 1 
ATOM   5770 C CD1 . ILE B 1 201 ? -19.419 -9.228  24.006  1.00 17.61 ? 201 ILE B CD1 1 
ATOM   5771 N N   . PRO B 1 202 ? -22.623 -4.897  24.932  1.00 16.06 ? 202 PRO B N   1 
ATOM   5772 C CA  . PRO B 1 202 ? -24.017 -4.432  25.087  1.00 16.62 ? 202 PRO B CA  1 
ATOM   5773 C C   . PRO B 1 202 ? -24.716 -4.130  23.778  1.00 18.97 ? 202 PRO B C   1 
ATOM   5774 O O   . PRO B 1 202 ? -25.931 -4.359  23.687  1.00 19.36 ? 202 PRO B O   1 
ATOM   5775 C CB  . PRO B 1 202 ? -23.867 -3.168  25.929  1.00 16.74 ? 202 PRO B CB  1 
ATOM   5776 C CG  . PRO B 1 202 ? -22.671 -3.462  26.777  1.00 16.59 ? 202 PRO B CG  1 
ATOM   5777 C CD  . PRO B 1 202 ? -21.711 -4.146  25.821  1.00 16.77 ? 202 PRO B CD  1 
ATOM   5778 N N   . ILE B 1 203 ? -23.995 -3.603  22.781  1.00 16.51 ? 203 ILE B N   1 
ATOM   5779 C CA  . ILE B 1 203 ? -24.603 -3.316  21.480  1.00 15.37 ? 203 ILE B CA  1 
ATOM   5780 C C   . ILE B 1 203 ? -24.879 -4.606  20.719  1.00 21.61 ? 203 ILE B C   1 
ATOM   5781 O O   . ILE B 1 203 ? -25.951 -4.764  20.114  1.00 20.95 ? 203 ILE B O   1 
ATOM   5782 C CB  . ILE B 1 203 ? -23.703 -2.346  20.682  1.00 16.77 ? 203 ILE B CB  1 
ATOM   5783 C CG1 . ILE B 1 203 ? -23.748 -0.948  21.327  1.00 20.36 ? 203 ILE B CG1 1 
ATOM   5784 C CG2 . ILE B 1 203 ? -24.158 -2.240  19.219  1.00 19.84 ? 203 ILE B CG2 1 
ATOM   5785 C CD1 . ILE B 1 203 ? -22.816 0.085   20.673  1.00 20.73 ? 203 ILE B CD1 1 
ATOM   5786 N N   . LEU B 1 204 ? -23.934 -5.559  20.735  1.00 15.69 ? 204 LEU B N   1 
ATOM   5787 C CA  . LEU B 1 204 ? -24.196 -6.825  20.044  1.00 18.31 ? 204 LEU B CA  1 
ATOM   5788 C C   . LEU B 1 204 ? -25.426 -7.527  20.627  1.00 21.50 ? 204 LEU B C   1 
ATOM   5789 O O   . LEU B 1 204 ? -26.222 -8.123  19.891  1.00 19.33 ? 204 LEU B O   1 
ATOM   5790 C CB  . LEU B 1 204 ? -22.965 -7.735  20.122  1.00 17.45 ? 204 LEU B CB  1 
ATOM   5791 C CG  . LEU B 1 204 ? -21.654 -7.227  19.490  1.00 18.25 ? 204 LEU B CG  1 
ATOM   5792 C CD1 . LEU B 1 204 ? -20.590 -8.304  19.522  1.00 20.39 ? 204 LEU B CD1 1 
ATOM   5793 C CD2 . LEU B 1 204 ? -21.896 -6.779  18.047  1.00 18.56 ? 204 LEU B CD2 1 
ATOM   5794 N N   . LEU B 1 205 ? -25.618 -7.442  21.947  1.00 18.44 ? 205 LEU B N   1 
ATOM   5795 C CA  . LEU B 1 205 ? -26.796 -8.067  22.559  1.00 18.09 ? 205 LEU B CA  1 
ATOM   5796 C C   . LEU B 1 205 ? -28.070 -7.286  22.281  1.00 20.59 ? 205 LEU B C   1 
ATOM   5797 O O   . LEU B 1 205 ? -29.141 -7.878  22.125  1.00 23.59 ? 205 LEU B O   1 
ATOM   5798 C CB  . LEU B 1 205 ? -26.611 -8.189  24.071  1.00 18.12 ? 205 LEU B CB  1 
ATOM   5799 C CG  . LEU B 1 205 ? -25.579 -9.238  24.488  1.00 19.34 ? 205 LEU B CG  1 
ATOM   5800 C CD1 . LEU B 1 205 ? -25.300 -9.115  25.982  1.00 16.28 ? 205 LEU B CD1 1 
ATOM   5801 C CD2 . LEU B 1 205 ? -26.058 -10.639 24.142  1.00 22.39 ? 205 LEU B CD2 1 
ATOM   5802 N N   . ASN B 1 206 ? -28.001 -5.964  22.307  1.00 19.31 ? 206 ASN B N   1 
ATOM   5803 C CA  . ASN B 1 206 ? -29.217 -5.179  22.184  1.00 23.82 ? 206 ASN B CA  1 
ATOM   5804 C C   . ASN B 1 206 ? -28.856 -3.760  21.768  1.00 21.53 ? 206 ASN B C   1 
ATOM   5805 O O   . ASN B 1 206 ? -28.595 -2.917  22.633  1.00 20.89 ? 206 ASN B O   1 
ATOM   5806 C CB  . ASN B 1 206 ? -30.002 -5.163  23.499  1.00 24.10 ? 206 ASN B CB  1 
ATOM   5807 C CG  . ASN B 1 206 ? -31.137 -4.161  23.472  1.00 32.73 ? 206 ASN B CG  1 
ATOM   5808 O OD1 . ASN B 1 206 ? -31.643 -3.821  22.396  1.00 28.10 ? 206 ASN B OD1 1 
ATOM   5809 N ND2 . ASN B 1 206 ? -31.526 -3.653  24.649  1.00 32.65 ? 206 ASN B ND2 1 
ATOM   5810 N N   . PRO B 1 207 ? -28.817 -3.460  20.470  1.00 23.24 ? 207 PRO B N   1 
ATOM   5811 C CA  . PRO B 1 207 ? -28.447 -2.102  20.045  1.00 23.09 ? 207 PRO B CA  1 
ATOM   5812 C C   . PRO B 1 207 ? -29.282 -0.990  20.660  1.00 23.08 ? 207 PRO B C   1 
ATOM   5813 O O   . PRO B 1 207 ? -28.812 0.150   20.736  1.00 24.26 ? 207 PRO B O   1 
ATOM   5814 C CB  . PRO B 1 207 ? -28.637 -2.164  18.520  1.00 23.48 ? 207 PRO B CB  1 
ATOM   5815 C CG  . PRO B 1 207 ? -28.316 -3.579  18.186  1.00 24.02 ? 207 PRO B CG  1 
ATOM   5816 C CD  . PRO B 1 207 ? -28.953 -4.370  19.317  1.00 23.40 ? 207 PRO B CD  1 
ATOM   5817 N N   . ASN B 1 208 ? -30.517 -1.275  21.073  1.00 20.49 ? 208 ASN B N   1 
ATOM   5818 C CA  . ASN B 1 208 ? -31.366 -0.239  21.651  1.00 23.90 ? 208 ASN B CA  1 
ATOM   5819 C C   . ASN B 1 208 ? -30.874 0.256   23.008  1.00 21.91 ? 208 ASN B C   1 
ATOM   5820 O O   . ASN B 1 208 ? -31.401 1.261   23.508  1.00 23.62 ? 208 ASN B O   1 
ATOM   5821 C CB  . ASN B 1 208 ? -32.794 -0.761  21.774  1.00 26.43 ? 208 ASN B CB  1 
ATOM   5822 C CG  . ASN B 1 208 ? -33.365 -1.198  20.428  1.00 29.42 ? 208 ASN B CG  1 
ATOM   5823 O OD1 . ASN B 1 208 ? -33.024 -0.634  19.382  1.00 32.84 ? 208 ASN B OD1 1 
ATOM   5824 N ND2 . ASN B 1 208 ? -34.223 -2.209  20.451  1.00 31.67 ? 208 ASN B ND2 1 
ATOM   5825 N N   . CYS B 1 209 ? -29.897 -0.417  23.613  1.00 21.55 ? 209 CYS B N   1 
ATOM   5826 C CA  . CYS B 1 209 ? -29.393 0.048   24.901  1.00 24.48 ? 209 CYS B CA  1 
ATOM   5827 C C   . CYS B 1 209 ? -28.705 1.409   24.794  1.00 26.40 ? 209 CYS B C   1 
ATOM   5828 O O   . CYS B 1 209 ? -28.532 2.081   25.819  1.00 21.69 ? 209 CYS B O   1 
ATOM   5829 C CB  . CYS B 1 209 ? -28.448 -0.995  25.513  1.00 25.27 ? 209 CYS B CB  1 
ATOM   5830 S SG  . CYS B 1 209 ? -26.807 -1.115  24.746  1.00 27.11 ? 209 CYS B SG  1 
ATOM   5831 N N   . VAL B 1 210 ? -28.359 1.856   23.579  1.00 22.30 ? 210 VAL B N   1 
ATOM   5832 C CA  . VAL B 1 210 ? -27.751 3.174   23.429  1.00 21.15 ? 210 VAL B CA  1 
ATOM   5833 C C   . VAL B 1 210 ? -28.730 4.270   23.826  1.00 22.92 ? 210 VAL B C   1 
ATOM   5834 O O   . VAL B 1 210 ? -28.327 5.372   24.227  1.00 26.54 ? 210 VAL B O   1 
ATOM   5835 C CB  . VAL B 1 210 ? -27.232 3.364   21.990  1.00 24.87 ? 210 VAL B CB  1 
ATOM   5836 C CG1 . VAL B 1 210 ? -26.378 2.158   21.566  1.00 24.87 ? 210 VAL B CG1 1 
ATOM   5837 C CG2 . VAL B 1 210 ? -28.384 3.585   21.039  1.00 27.17 ? 210 VAL B CG2 1 
ATOM   5838 N N   . TYR B 1 211 ? -30.028 4.000   23.732  1.00 21.72 ? 211 TYR B N   1 
ATOM   5839 C CA  . TYR B 1 211 ? -31.023 5.005   24.084  1.00 24.81 ? 211 TYR B CA  1 
ATOM   5840 C C   . TYR B 1 211 ? -31.175 5.200   25.585  1.00 26.56 ? 211 TYR B C   1 
ATOM   5841 O O   . TYR B 1 211 ? -31.883 6.124   25.996  1.00 25.92 ? 211 TYR B O   1 
ATOM   5842 C CB  . TYR B 1 211 ? -32.359 4.633   23.445  1.00 25.95 ? 211 TYR B CB  1 
ATOM   5843 C CG  . TYR B 1 211 ? -32.212 4.486   21.949  1.00 29.99 ? 211 TYR B CG  1 
ATOM   5844 C CD1 . TYR B 1 211 ? -31.808 5.557   21.170  1.00 26.81 ? 211 TYR B CD1 1 
ATOM   5845 C CD2 . TYR B 1 211 ? -32.442 3.269   21.322  1.00 31.33 ? 211 TYR B CD2 1 
ATOM   5846 C CE1 . TYR B 1 211 ? -31.653 5.426   19.804  1.00 26.39 ? 211 TYR B CE1 1 
ATOM   5847 C CE2 . TYR B 1 211 ? -32.292 3.129   19.965  1.00 32.80 ? 211 TYR B CE2 1 
ATOM   5848 C CZ  . TYR B 1 211 ? -31.895 4.211   19.213  1.00 34.47 ? 211 TYR B CZ  1 
ATOM   5849 O OH  . TYR B 1 211 ? -31.770 4.089   17.853  1.00 42.83 ? 211 TYR B OH  1 
ATOM   5850 N N   . GLU B 1 212 ? -30.516 4.379   26.411  1.00 21.59 ? 212 GLU B N   1 
ATOM   5851 C CA  . GLU B 1 212 ? -30.606 4.579   27.856  1.00 28.83 ? 212 GLU B CA  1 
ATOM   5852 C C   . GLU B 1 212 ? -29.876 5.839   28.299  1.00 30.97 ? 212 GLU B C   1 
ATOM   5853 O O   . GLU B 1 212 ? -30.261 6.452   29.302  1.00 32.73 ? 212 GLU B O   1 
ATOM   5854 C CB  . GLU B 1 212 ? -30.066 3.349   28.587  1.00 26.55 ? 212 GLU B CB  1 
ATOM   5855 C CG  . GLU B 1 212 ? -30.935 2.131   28.352  1.00 29.36 ? 212 GLU B CG  1 
ATOM   5856 C CD  . GLU B 1 212 ? -30.467 0.876   29.069  1.00 33.09 ? 212 GLU B CD  1 
ATOM   5857 O OE1 . GLU B 1 212 ? -30.949 -0.213  28.697  1.00 38.63 ? 212 GLU B OE1 1 
ATOM   5858 O OE2 . GLU B 1 212 ? -29.637 0.963   29.994  1.00 31.29 ? 212 GLU B OE2 1 
ATOM   5859 N N   . THR B 1 213 ? -28.837 6.253   27.566  1.00 28.45 ? 213 THR B N   1 
ATOM   5860 C CA  . THR B 1 213 ? -28.097 7.472   27.877  1.00 29.63 ? 213 THR B CA  1 
ATOM   5861 C C   . THR B 1 213 ? -28.201 8.556   26.818  1.00 29.23 ? 213 THR B C   1 
ATOM   5862 O O   . THR B 1 213 ? -28.053 9.732   27.153  1.00 35.08 ? 213 THR B O   1 
ATOM   5863 C CB  . THR B 1 213 ? -26.612 7.158   28.074  1.00 29.70 ? 213 THR B CB  1 
ATOM   5864 O OG1 . THR B 1 213 ? -26.119 6.478   26.906  1.00 32.79 ? 213 THR B OG1 1 
ATOM   5865 C CG2 . THR B 1 213 ? -26.434 6.302   29.299  1.00 28.19 ? 213 THR B CG2 1 
ATOM   5866 N N   . THR B 1 214 ? -28.406 8.200   25.548  1.00 27.66 ? 214 THR B N   1 
ATOM   5867 C CA  . THR B 1 214 ? -28.464 9.166   24.448  1.00 27.26 ? 214 THR B CA  1 
ATOM   5868 C C   . THR B 1 214 ? -29.680 8.855   23.591  1.00 26.42 ? 214 THR B C   1 
ATOM   5869 O O   . THR B 1 214 ? -29.564 8.240   22.521  1.00 28.73 ? 214 THR B O   1 
ATOM   5870 C CB  . THR B 1 214 ? -27.194 9.147   23.593  1.00 26.85 ? 214 THR B CB  1 
ATOM   5871 O OG1 . THR B 1 214 ? -26.993 7.835   23.029  1.00 26.91 ? 214 THR B OG1 1 
ATOM   5872 C CG2 . THR B 1 214 ? -25.985 9.516   24.440  1.00 26.01 ? 214 THR B CG2 1 
ATOM   5873 N N   . PRO B 1 215 ? -30.866 9.279   24.028  1.00 30.37 ? 215 PRO B N   1 
ATOM   5874 C CA  . PRO B 1 215 ? -32.094 8.904   23.307  1.00 31.40 ? 215 PRO B CA  1 
ATOM   5875 C C   . PRO B 1 215 ? -32.223 9.532   21.923  1.00 33.71 ? 215 PRO B C   1 
ATOM   5876 O O   . PRO B 1 215 ? -33.025 9.042   21.115  1.00 35.16 ? 215 PRO B O   1 
ATOM   5877 C CB  . PRO B 1 215 ? -33.209 9.387   24.243  1.00 34.64 ? 215 PRO B CB  1 
ATOM   5878 C CG  . PRO B 1 215 ? -32.580 10.475  25.053  1.00 34.81 ? 215 PRO B CG  1 
ATOM   5879 C CD  . PRO B 1 215 ? -31.135 10.097  25.224  1.00 32.72 ? 215 PRO B CD  1 
ATOM   5880 N N   . ASN B 1 216 ? -31.467 10.586  21.615  1.00 33.61 ? 216 ASN B N   1 
ATOM   5881 C CA  . ASN B 1 216 ? -31.588 11.261  20.328  1.00 36.57 ? 216 ASN B CA  1 
ATOM   5882 C C   . ASN B 1 216 ? -30.619 10.739  19.277  1.00 36.82 ? 216 ASN B C   1 
ATOM   5883 O O   . ASN B 1 216 ? -30.574 11.285  18.171  1.00 42.04 ? 216 ASN B O   1 
ATOM   5884 C CB  . ASN B 1 216 ? -31.387 12.761  20.501  1.00 40.63 ? 216 ASN B CB  1 
ATOM   5885 C CG  . ASN B 1 216 ? -32.467 13.385  21.347  1.00 46.59 ? 216 ASN B CG  1 
ATOM   5886 O OD1 . ASN B 1 216 ? -32.199 13.892  22.432  1.00 52.10 ? 216 ASN B OD1 1 
ATOM   5887 N ND2 . ASN B 1 216 ? -33.702 13.332  20.864  1.00 48.68 ? 216 ASN B ND2 1 
ATOM   5888 N N   . VAL B 1 217 ? -29.856 9.697   19.583  1.00 37.53 ? 217 VAL B N   1 
ATOM   5889 C CA  . VAL B 1 217 ? -28.890 9.186   18.620  1.00 38.43 ? 217 VAL B CA  1 
ATOM   5890 C C   . VAL B 1 217 ? -29.623 8.441   17.503  1.00 34.35 ? 217 VAL B C   1 
ATOM   5891 O O   . VAL B 1 217 ? -30.679 7.829   17.715  1.00 32.70 ? 217 VAL B O   1 
ATOM   5892 C CB  . VAL B 1 217 ? -27.849 8.302   19.339  1.00 34.57 ? 217 VAL B CB  1 
ATOM   5893 C CG1 . VAL B 1 217 ? -28.430 6.960   19.778  1.00 30.16 ? 217 VAL B CG1 1 
ATOM   5894 C CG2 . VAL B 1 217 ? -26.630 8.085   18.482  1.00 36.69 ? 217 VAL B CG2 1 
ATOM   5895 N N   . LYS B 1 218 ? -29.083 8.527   16.289  1.00 30.41 ? 218 LYS B N   1 
ATOM   5896 C CA  . LYS B 1 218 ? -29.558 7.734   15.161  1.00 30.33 ? 218 LYS B CA  1 
ATOM   5897 C C   . LYS B 1 218 ? -28.650 6.524   15.002  1.00 26.35 ? 218 LYS B C   1 
ATOM   5898 O O   . LYS B 1 218 ? -27.423 6.662   15.050  1.00 27.24 ? 218 LYS B O   1 
ATOM   5899 C CB  . LYS B 1 218 ? -29.564 8.545   13.867  1.00 36.67 ? 218 LYS B CB  1 
ATOM   5900 C CG  . LYS B 1 218 ? -30.355 9.835   13.935  1.00 47.32 ? 218 LYS B CG  1 
ATOM   5901 C CD  . LYS B 1 218 ? -29.975 10.769  12.800  1.00 55.33 ? 218 LYS B CD  1 
ATOM   5902 C CE  . LYS B 1 218 ? -31.116 10.938  11.812  1.00 59.77 ? 218 LYS B CE  1 
ATOM   5903 N NZ  . LYS B 1 218 ? -31.495 12.370  11.637  1.00 64.48 ? 218 LYS B NZ  1 
ATOM   5904 N N   . ILE B 1 219 ? -29.246 5.344   14.831  1.00 25.00 ? 219 ILE B N   1 
ATOM   5905 C CA  . ILE B 1 219 ? -28.468 4.124   14.607  1.00 23.22 ? 219 ILE B CA  1 
ATOM   5906 C C   . ILE B 1 219 ? -29.022 3.416   13.380  1.00 22.97 ? 219 ILE B C   1 
ATOM   5907 O O   . ILE B 1 219 ? -30.173 3.637   12.980  1.00 23.88 ? 219 ILE B O   1 
ATOM   5908 C CB  . ILE B 1 219 ? -28.494 3.180   15.837  1.00 27.20 ? 219 ILE B CB  1 
ATOM   5909 C CG1 . ILE B 1 219 ? -29.890 2.555   16.002  1.00 26.14 ? 219 ILE B CG1 1 
ATOM   5910 C CG2 . ILE B 1 219 ? -28.021 3.896   17.111  1.00 25.35 ? 219 ILE B CG2 1 
ATOM   5911 C CD1 . ILE B 1 219 ? -29.960 1.489   17.110  1.00 26.57 ? 219 ILE B CD1 1 
ATOM   5912 N N   . PRO B 1 220 ? -28.223 2.567   12.743  1.00 25.93 ? 220 PRO B N   1 
ATOM   5913 C CA  . PRO B 1 220 ? -28.717 1.858   11.558  1.00 28.32 ? 220 PRO B CA  1 
ATOM   5914 C C   . PRO B 1 220 ? -29.725 0.770   11.917  1.00 23.49 ? 220 PRO B C   1 
ATOM   5915 O O   . PRO B 1 220 ? -29.995 0.469   13.087  1.00 22.64 ? 220 PRO B O   1 
ATOM   5916 C CB  . PRO B 1 220 ? -27.450 1.267   10.932  1.00 31.18 ? 220 PRO B CB  1 
ATOM   5917 C CG  . PRO B 1 220 ? -26.447 1.264   11.984  1.00 28.92 ? 220 PRO B CG  1 
ATOM   5918 C CD  . PRO B 1 220 ? -26.776 2.362   12.944  1.00 28.16 ? 220 PRO B CD  1 
ATOM   5919 N N   . ASP B 1 221 ? -30.290 0.186   10.855  1.00 22.58 ? 221 ASP B N   1 
ATOM   5920 C CA  . ASP B 1 221 ? -31.246 -0.915  10.952  1.00 23.13 ? 221 ASP B CA  1 
ATOM   5921 C C   . ASP B 1 221 ? -30.504 -2.222  11.230  1.00 22.45 ? 221 ASP B C   1 
ATOM   5922 O O   . ASP B 1 221 ? -29.910 -2.820  10.333  1.00 23.26 ? 221 ASP B O   1 
ATOM   5923 C CB  . ASP B 1 221 ? -32.039 -0.995  9.656   1.00 24.11 ? 221 ASP B CB  1 
ATOM   5924 C CG  . ASP B 1 221 ? -33.132 -2.031  9.702   1.00 26.95 ? 221 ASP B CG  1 
ATOM   5925 O OD1 . ASP B 1 221 ? -33.631 -2.339  10.797  1.00 25.20 ? 221 ASP B OD1 1 
ATOM   5926 O OD2 . ASP B 1 221 ? -33.502 -2.527  8.617   1.00 32.98 ? 221 ASP B OD2 1 
ATOM   5927 N N   . PHE B 1 222 ? -30.536 -2.684  12.476  1.00 21.65 ? 222 PHE B N   1 
ATOM   5928 C CA  . PHE B 1 222 ? -29.891 -3.942  12.846  1.00 23.28 ? 222 PHE B CA  1 
ATOM   5929 C C   . PHE B 1 222 ? -30.775 -5.116  12.417  1.00 27.56 ? 222 PHE B C   1 
ATOM   5930 O O   . PHE B 1 222 ? -31.403 -5.799  13.226  1.00 26.70 ? 222 PHE B O   1 
ATOM   5931 C CB  . PHE B 1 222 ? -29.599 -3.960  14.340  1.00 22.61 ? 222 PHE B CB  1 
ATOM   5932 C CG  . PHE B 1 222 ? -28.349 -3.225  14.704  1.00 23.59 ? 222 PHE B CG  1 
ATOM   5933 C CD1 . PHE B 1 222 ? -28.347 -1.838  14.805  1.00 23.24 ? 222 PHE B CD1 1 
ATOM   5934 C CD2 . PHE B 1 222 ? -27.166 -3.918  14.897  1.00 24.50 ? 222 PHE B CD2 1 
ATOM   5935 C CE1 . PHE B 1 222 ? -27.196 -1.155  15.124  1.00 22.89 ? 222 PHE B CE1 1 
ATOM   5936 C CE2 . PHE B 1 222 ? -26.003 -3.244  15.213  1.00 22.18 ? 222 PHE B CE2 1 
ATOM   5937 C CZ  . PHE B 1 222 ? -26.024 -1.857  15.328  1.00 22.05 ? 222 PHE B CZ  1 
ATOM   5938 N N   . ALA B 1 223 ? -30.799 -5.354  11.101  1.00 26.61 ? 223 ALA B N   1 
ATOM   5939 C CA  . ALA B 1 223 ? -31.671 -6.363  10.507  1.00 30.18 ? 223 ALA B CA  1 
ATOM   5940 C C   . ALA B 1 223 ? -31.218 -7.803  10.756  1.00 31.91 ? 223 ALA B C   1 
ATOM   5941 O O   . ALA B 1 223 ? -31.857 -8.719  10.219  1.00 34.80 ? 223 ALA B O   1 
ATOM   5942 C CB  . ALA B 1 223 ? -31.797 -6.122  9.000   1.00 34.45 ? 223 ALA B CB  1 
ATOM   5943 N N   . VAL B 1 224 ? -30.145 -8.031  11.520  1.00 24.02 ? 224 VAL B N   1 
ATOM   5944 C CA  . VAL B 1 224 ? -29.716 -9.367  11.921  1.00 24.97 ? 224 VAL B CA  1 
ATOM   5945 C C   . VAL B 1 224 ? -29.346 -9.339  13.396  1.00 24.93 ? 224 VAL B C   1 
ATOM   5946 O O   . VAL B 1 224 ? -29.038 -8.291  13.965  1.00 25.94 ? 224 VAL B O   1 
ATOM   5947 C CB  . VAL B 1 224 ? -28.517 -9.889  11.107  1.00 30.10 ? 224 VAL B CB  1 
ATOM   5948 C CG1 . VAL B 1 224 ? -28.852 -9.880  9.676   1.00 47.53 ? 224 VAL B CG1 1 
ATOM   5949 C CG2 . VAL B 1 224 ? -27.295 -9.034  11.364  1.00 34.75 ? 224 VAL B CG2 1 
ATOM   5950 N N   . SER B 1 225 ? -29.375 -10.514 14.017  1.00 24.32 ? 225 SER B N   1 
ATOM   5951 C CA  . SER B 1 225 ? -29.029 -10.643 15.420  1.00 21.69 ? 225 SER B CA  1 
ATOM   5952 C C   . SER B 1 225 ? -27.533 -10.887 15.588  1.00 24.40 ? 225 SER B C   1 
ATOM   5953 O O   . SER B 1 225 ? -26.956 -11.748 14.912  1.00 23.73 ? 225 SER B O   1 
ATOM   5954 C CB  . SER B 1 225 ? -29.805 -11.790 16.059  1.00 27.61 ? 225 SER B CB  1 
ATOM   5955 O OG  . SER B 1 225 ? -29.401 -11.951 17.407  1.00 27.64 ? 225 SER B OG  1 
ATOM   5956 N N   . PHE B 1 226 ? -26.917 -10.139 16.507  1.00 20.68 ? 226 PHE B N   1 
ATOM   5957 C CA  . PHE B 1 226 ? -25.534 -10.347 16.926  1.00 21.27 ? 226 PHE B CA  1 
ATOM   5958 C C   . PHE B 1 226 ? -25.436 -11.011 18.300  1.00 21.76 ? 226 PHE B C   1 
ATOM   5959 O O   . PHE B 1 226 ? -24.351 -11.024 18.901  1.00 20.27 ? 226 PHE B O   1 
ATOM   5960 C CB  . PHE B 1 226 ? -24.774 -9.010  16.952  1.00 19.17 ? 226 PHE B CB  1 
ATOM   5961 C CG  . PHE B 1 226 ? -24.450 -8.462  15.588  1.00 21.99 ? 226 PHE B CG  1 
ATOM   5962 C CD1 . PHE B 1 226 ? -23.385 -8.963  14.860  1.00 22.61 ? 226 PHE B CD1 1 
ATOM   5963 C CD2 . PHE B 1 226 ? -25.202 -7.429  15.044  1.00 25.42 ? 226 PHE B CD2 1 
ATOM   5964 C CE1 . PHE B 1 226 ? -23.068 -8.451  13.609  1.00 21.19 ? 226 PHE B CE1 1 
ATOM   5965 C CE2 . PHE B 1 226 ? -24.903 -6.912  13.777  1.00 27.75 ? 226 PHE B CE2 1 
ATOM   5966 C CZ  . PHE B 1 226 ? -23.840 -7.435  13.057  1.00 20.55 ? 226 PHE B CZ  1 
ATOM   5967 N N   . ARG B 1 227 ? -26.552 -11.528 18.825  1.00 23.22 ? 227 ARG B N   1 
ATOM   5968 C CA  . ARG B 1 227 ? -26.570 -12.077 20.182  1.00 20.07 ? 227 ARG B CA  1 
ATOM   5969 C C   . ARG B 1 227 ? -25.726 -13.344 20.304  1.00 20.08 ? 227 ARG B C   1 
ATOM   5970 O O   . ARG B 1 227 ? -24.979 -13.508 21.283  1.00 19.46 ? 227 ARG B O   1 
ATOM   5971 C CB  . ARG B 1 227 ? -28.016 -12.356 20.604  1.00 22.59 ? 227 ARG B CB  1 
ATOM   5972 C CG  . ARG B 1 227 ? -28.830 -11.086 20.822  1.00 30.09 ? 227 ARG B CG  1 
ATOM   5973 C CD  . ARG B 1 227 ? -30.244 -11.377 21.338  1.00 31.19 ? 227 ARG B CD  1 
ATOM   5974 N NE  . ARG B 1 227 ? -30.245 -11.995 22.663  1.00 36.15 ? 227 ARG B NE  1 
ATOM   5975 C CZ  . ARG B 1 227 ? -30.193 -11.315 23.808  1.00 38.63 ? 227 ARG B CZ  1 
ATOM   5976 N NH1 . ARG B 1 227 ? -30.122 -9.992  23.791  1.00 31.85 ? 227 ARG B NH1 1 
ATOM   5977 N NH2 . ARG B 1 227 ? -30.215 -11.957 24.971  1.00 42.83 ? 227 ARG B NH2 1 
ATOM   5978 N N   . GLU B 1 228 ? -25.823 -14.255 19.331  1.00 23.23 ? 228 GLU B N   1 
ATOM   5979 C CA  . GLU B 1 228 ? -24.965 -15.434 19.395  1.00 24.96 ? 228 GLU B CA  1 
ATOM   5980 C C   . GLU B 1 228 ? -23.491 -15.071 19.217  1.00 23.66 ? 228 GLU B C   1 
ATOM   5981 O O   . GLU B 1 228 ? -22.626 -15.713 19.827  1.00 25.71 ? 228 GLU B O   1 
ATOM   5982 C CB  . GLU B 1 228 ? -25.400 -16.474 18.366  1.00 28.88 ? 228 GLU B CB  1 
ATOM   5983 C CG  . GLU B 1 228 ? -26.626 -17.269 18.821  1.00 47.13 ? 228 GLU B CG  1 
ATOM   5984 C CD  . GLU B 1 228 ? -26.267 -18.569 19.522  1.00 66.13 ? 228 GLU B CD  1 
ATOM   5985 O OE1 . GLU B 1 228 ? -25.945 -18.532 20.732  1.00 71.20 ? 228 GLU B OE1 1 
ATOM   5986 O OE2 . GLU B 1 228 ? -26.321 -19.632 18.861  1.00 74.34 ? 228 GLU B OE2 1 
ATOM   5987 N N   . ASP B 1 229 ? -23.176 -14.043 18.423  1.00 22.41 ? 229 ASP B N   1 
ATOM   5988 C CA  . ASP B 1 229 ? -21.770 -13.627 18.315  1.00 20.79 ? 229 ASP B CA  1 
ATOM   5989 C C   . ASP B 1 229 ? -21.258 -13.074 19.644  1.00 18.54 ? 229 ASP B C   1 
ATOM   5990 O O   . ASP B 1 229 ? -20.096 -13.279 20.005  1.00 19.53 ? 229 ASP B O   1 
ATOM   5991 C CB  . ASP B 1 229 ? -21.597 -12.575 17.214  1.00 21.02 ? 229 ASP B CB  1 
ATOM   5992 C CG  . ASP B 1 229 ? -21.536 -13.183 15.800  1.00 26.52 ? 229 ASP B CG  1 
ATOM   5993 O OD1 . ASP B 1 229 ? -21.543 -14.432 15.653  1.00 26.36 ? 229 ASP B OD1 1 
ATOM   5994 O OD2 . ASP B 1 229 ? -21.461 -12.399 14.831  1.00 25.26 ? 229 ASP B OD2 1 
ATOM   5995 N N   . ALA B 1 230 ? -22.103 -12.347 20.380  1.00 19.05 ? 230 ALA B N   1 
ATOM   5996 C CA  . ALA B 1 230 ? -21.684 -11.882 21.700  1.00 18.27 ? 230 ALA B CA  1 
ATOM   5997 C C   . ALA B 1 230 ? -21.276 -13.062 22.581  1.00 21.47 ? 230 ALA B C   1 
ATOM   5998 O O   . ALA B 1 230 ? -20.228 -13.022 23.242  1.00 20.38 ? 230 ALA B O   1 
ATOM   5999 C CB  . ALA B 1 230 ? -22.803 -11.075 22.361  1.00 19.78 ? 230 ALA B CB  1 
ATOM   6000 N N   . SER B 1 231 ? -22.076 -14.134 22.572  1.00 22.08 ? 231 SER B N   1 
ATOM   6001 C CA  . SER B 1 231 ? -21.716 -15.332 23.328  1.00 21.21 ? 231 SER B CA  1 
ATOM   6002 C C   . SER B 1 231 ? -20.421 -15.938 22.811  1.00 24.80 ? 231 SER B C   1 
ATOM   6003 O O   . SER B 1 231 ? -19.555 -16.332 23.603  1.00 24.37 ? 231 SER B O   1 
ATOM   6004 C CB  . SER B 1 231 ? -22.839 -16.369 23.265  1.00 23.94 ? 231 SER B CB  1 
ATOM   6005 O OG  . SER B 1 231 ? -23.761 -16.188 24.314  1.00 38.31 ? 231 SER B OG  1 
ATOM   6006 N N   . LYS B 1 232 ? -20.266 -16.012 21.485  1.00 20.47 ? 232 LYS B N   1 
ATOM   6007 C CA  . LYS B 1 232 ? -19.056 -16.591 20.908  1.00 22.72 ? 232 LYS B CA  1 
ATOM   6008 C C   . LYS B 1 232 ? -17.810 -15.826 21.344  1.00 22.11 ? 232 LYS B C   1 
ATOM   6009 O O   . LYS B 1 232 ? -16.788 -16.439 21.672  1.00 20.19 ? 232 LYS B O   1 
ATOM   6010 C CB  . LYS B 1 232 ? -19.154 -16.623 19.382  1.00 22.67 ? 232 LYS B CB  1 
ATOM   6011 C CG  . LYS B 1 232 ? -19.773 -17.888 18.817  1.00 37.63 ? 232 LYS B CG  1 
ATOM   6012 C CD  . LYS B 1 232 ? -19.617 -17.970 17.296  1.00 43.45 ? 232 LYS B CD  1 
ATOM   6013 C CE  . LYS B 1 232 ? -18.192 -18.340 16.889  1.00 49.23 ? 232 LYS B CE  1 
ATOM   6014 N NZ  . LYS B 1 232 ? -17.665 -19.523 17.628  1.00 53.65 ? 232 LYS B NZ  1 
ATOM   6015 N N   . HIS B 1 233 ? -17.864 -14.483 21.364  1.00 17.67 ? 233 HIS B N   1 
ATOM   6016 C CA  . HIS B 1 233 ? -16.696 -13.724 21.831  1.00 15.26 ? 233 HIS B CA  1 
ATOM   6017 C C   . HIS B 1 233 ? -16.313 -14.139 23.246  1.00 14.77 ? 233 HIS B C   1 
ATOM   6018 O O   . HIS B 1 233 ? -15.130 -14.310 23.550  1.00 16.01 ? 233 HIS B O   1 
ATOM   6019 C CB  . HIS B 1 233 ? -16.950 -12.212 21.839  1.00 15.83 ? 233 HIS B CB  1 
ATOM   6020 C CG  . HIS B 1 233 ? -16.874 -11.537 20.500  1.00 15.20 ? 233 HIS B CG  1 
ATOM   6021 N ND1 . HIS B 1 233 ? -15.681 -11.134 19.933  1.00 15.75 ? 233 HIS B ND1 1 
ATOM   6022 C CD2 . HIS B 1 233 ? -17.852 -11.128 19.655  1.00 17.20 ? 233 HIS B CD2 1 
ATOM   6023 C CE1 . HIS B 1 233 ? -15.925 -10.538 18.779  1.00 15.48 ? 233 HIS B CE1 1 
ATOM   6024 N NE2 . HIS B 1 233 ? -17.237 -10.523 18.586  1.00 17.01 ? 233 HIS B NE2 1 
ATOM   6025 N N   . VAL B 1 234 ? -17.308 -14.290 24.132  1.00 18.28 ? 234 VAL B N   1 
ATOM   6026 C CA  . VAL B 1 234 ? -17.002 -14.649 25.512  1.00 16.01 ? 234 VAL B CA  1 
ATOM   6027 C C   . VAL B 1 234 ? -16.537 -16.095 25.587  1.00 19.47 ? 234 VAL B C   1 
ATOM   6028 O O   . VAL B 1 234 ? -15.555 -16.413 26.279  1.00 18.10 ? 234 VAL B O   1 
ATOM   6029 C CB  . VAL B 1 234 ? -18.220 -14.386 26.422  1.00 16.58 ? 234 VAL B CB  1 
ATOM   6030 C CG1 . VAL B 1 234 ? -17.895 -14.810 27.863  1.00 17.98 ? 234 VAL B CG1 1 
ATOM   6031 C CG2 . VAL B 1 234 ? -18.556 -12.889 26.408  1.00 17.76 ? 234 VAL B CG2 1 
ATOM   6032 N N   . GLU B 1 235 ? -17.210 -16.984 24.859  1.00 19.82 ? 235 GLU B N   1 
ATOM   6033 C CA  . GLU B 1 235 ? -16.863 -18.402 24.908  1.00 21.19 ? 235 GLU B CA  1 
ATOM   6034 C C   . GLU B 1 235 ? -15.465 -18.650 24.353  1.00 24.44 ? 235 GLU B C   1 
ATOM   6035 O O   . GLU B 1 235 ? -14.660 -19.378 24.958  1.00 20.73 ? 235 GLU B O   1 
ATOM   6036 C CB  . GLU B 1 235 ? -17.905 -19.227 24.153  1.00 23.45 ? 235 GLU B CB  1 
ATOM   6037 C CG  . GLU B 1 235 ? -17.808 -20.711 24.447  1.00 38.17 ? 235 GLU B CG  1 
ATOM   6038 C CD  . GLU B 1 235 ? -17.759 -21.012 25.942  1.00 48.42 ? 235 GLU B CD  1 
ATOM   6039 O OE1 . GLU B 1 235 ? -18.572 -20.448 26.708  1.00 48.56 ? 235 GLU B OE1 1 
ATOM   6040 O OE2 . GLU B 1 235 ? -16.891 -21.812 26.350  1.00 52.05 ? 235 GLU B OE2 1 
ATOM   6041 N N   . LEU B 1 236 ? -15.151 -18.049 23.203  1.00 17.72 ? 236 LEU B N   1 
ATOM   6042 C CA  . LEU B 1 236 ? -13.819 -18.226 22.627  1.00 17.42 ? 236 LEU B CA  1 
ATOM   6043 C C   . LEU B 1 236 ? -12.725 -17.614 23.492  1.00 18.95 ? 236 LEU B C   1 
ATOM   6044 O O   . LEU B 1 236 ? -11.599 -18.125 23.514  1.00 20.26 ? 236 LEU B O   1 
ATOM   6045 C CB  . LEU B 1 236 ? -13.768 -17.621 21.230  1.00 16.99 ? 236 LEU B CB  1 
ATOM   6046 C CG  . LEU B 1 236 ? -14.624 -18.374 20.205  1.00 21.95 ? 236 LEU B CG  1 
ATOM   6047 C CD1 . LEU B 1 236 ? -14.611 -17.642 18.888  1.00 24.71 ? 236 LEU B CD1 1 
ATOM   6048 C CD2 . LEU B 1 236 ? -14.149 -19.811 20.013  1.00 27.67 ? 236 LEU B CD2 1 
ATOM   6049 N N   . ALA B 1 237 ? -13.020 -16.513 24.184  1.00 17.95 ? 237 ALA B N   1 
ATOM   6050 C CA  . ALA B 1 237 ? -12.044 -15.962 25.113  1.00 17.08 ? 237 ALA B CA  1 
ATOM   6051 C C   . ALA B 1 237 ? -11.777 -16.916 26.263  1.00 21.27 ? 237 ALA B C   1 
ATOM   6052 O O   . ALA B 1 237 ? -10.623 -17.079 26.684  1.00 21.25 ? 237 ALA B O   1 
ATOM   6053 C CB  . ALA B 1 237 ? -12.532 -14.617 25.646  1.00 17.00 ? 237 ALA B CB  1 
ATOM   6054 N N   . LYS B 1 238 ? -12.832 -17.515 26.825  1.00 17.09 ? 238 LYS B N   1 
ATOM   6055 C CA  . LYS B 1 238 ? -12.618 -18.527 27.854  1.00 23.75 ? 238 LYS B CA  1 
ATOM   6056 C C   . LYS B 1 238 ? -11.683 -19.621 27.355  1.00 25.45 ? 238 LYS B C   1 
ATOM   6057 O O   . LYS B 1 238 ? -10.766 -20.038 28.073  1.00 25.06 ? 238 LYS B O   1 
ATOM   6058 C CB  . LYS B 1 238 ? -13.947 -19.117 28.305  1.00 19.87 ? 238 LYS B CB  1 
ATOM   6059 C CG  . LYS B 1 238 ? -14.820 -18.145 29.084  1.00 24.20 ? 238 LYS B CG  1 
ATOM   6060 C CD  . LYS B 1 238 ? -16.216 -18.731 29.311  1.00 24.87 ? 238 LYS B CD  1 
ATOM   6061 C CE  . LYS B 1 238 ? -16.182 -19.913 30.283  1.00 38.78 ? 238 LYS B CE  1 
ATOM   6062 N NZ  . LYS B 1 238 ? -15.892 -19.476 31.687  1.00 46.94 ? 238 LYS B NZ  1 
ATOM   6063 N N   . GLU B 1 239 ? -11.873 -20.069 26.109  1.00 24.77 ? 239 GLU B N   1 
ATOM   6064 C CA  . GLU B 1 239 ? -11.052 -21.151 25.572  1.00 24.09 ? 239 GLU B CA  1 
ATOM   6065 C C   . GLU B 1 239 ? -9.601  -20.720 25.386  1.00 25.11 ? 239 GLU B C   1 
ATOM   6066 O O   . GLU B 1 239 ? -8.680  -21.494 25.668  1.00 25.79 ? 239 GLU B O   1 
ATOM   6067 C CB  . GLU B 1 239 ? -11.640 -21.634 24.249  1.00 26.77 ? 239 GLU B CB  1 
ATOM   6068 C CG  . GLU B 1 239 ? -13.015 -22.242 24.384  1.00 39.43 ? 239 GLU B CG  1 
ATOM   6069 C CD  . GLU B 1 239 ? -13.658 -22.470 23.029  1.00 53.90 ? 239 GLU B CD  1 
ATOM   6070 O OE1 . GLU B 1 239 ? -14.906 -22.445 22.944  1.00 57.61 ? 239 GLU B OE1 1 
ATOM   6071 O OE2 . GLU B 1 239 ? -12.906 -22.656 22.046  1.00 56.95 ? 239 GLU B OE2 1 
ATOM   6072 N N   . LYS B 1 240 ? -9.376  -19.503 24.887  1.00 25.90 ? 240 LYS B N   1 
ATOM   6073 C CA  . LYS B 1 240 ? -8.012  -19.020 24.682  1.00 22.11 ? 240 LYS B CA  1 
ATOM   6074 C C   . LYS B 1 240 ? -7.281  -18.894 26.010  1.00 29.15 ? 240 LYS B C   1 
ATOM   6075 O O   . LYS B 1 240 ? -6.110  -19.276 26.128  1.00 29.54 ? 240 LYS B O   1 
ATOM   6076 C CB  . LYS B 1 240 ? -8.033  -17.663 23.960  1.00 29.09 ? 240 LYS B CB  1 
ATOM   6077 C CG  . LYS B 1 240 ? -6.647  -17.091 23.641  1.00 29.86 ? 240 LYS B CG  1 
ATOM   6078 C CD  . LYS B 1 240 ? -5.973  -17.897 22.541  1.00 31.08 ? 240 LYS B CD  1 
ATOM   6079 C CE  . LYS B 1 240 ? -4.526  -17.477 22.336  1.00 34.55 ? 240 LYS B CE  1 
ATOM   6080 N NZ  . LYS B 1 240 ? -3.921  -18.115 21.126  1.00 41.38 ? 240 LYS B NZ  1 
ATOM   6081 N N   . TYR B 1 241 ? -7.965  -18.343 27.017  1.00 23.77 ? 241 TYR B N   1 
ATOM   6082 C CA  . TYR B 1 241 ? -7.389  -18.208 28.349  1.00 25.34 ? 241 TYR B CA  1 
ATOM   6083 C C   . TYR B 1 241 ? -7.043  -19.570 28.936  1.00 30.06 ? 241 TYR B C   1 
ATOM   6084 O O   . TYR B 1 241 ? -5.970  -19.744 29.538  1.00 28.24 ? 241 TYR B O   1 
ATOM   6085 C CB  . TYR B 1 241 ? -8.379  -17.460 29.243  1.00 22.98 ? 241 TYR B CB  1 
ATOM   6086 C CG  . TYR B 1 241 ? -7.867  -17.104 30.621  1.00 24.79 ? 241 TYR B CG  1 
ATOM   6087 C CD1 . TYR B 1 241 ? -7.898  -18.038 31.656  1.00 23.78 ? 241 TYR B CD1 1 
ATOM   6088 C CD2 . TYR B 1 241 ? -7.392  -15.833 30.898  1.00 25.81 ? 241 TYR B CD2 1 
ATOM   6089 C CE1 . TYR B 1 241 ? -7.442  -17.723 32.931  1.00 21.04 ? 241 TYR B CE1 1 
ATOM   6090 C CE2 . TYR B 1 241 ? -6.935  -15.500 32.175  1.00 26.28 ? 241 TYR B CE2 1 
ATOM   6091 C CZ  . TYR B 1 241 ? -6.969  -16.447 33.180  1.00 24.16 ? 241 TYR B CZ  1 
ATOM   6092 O OH  . TYR B 1 241 ? -6.519  -16.131 34.444  1.00 24.78 ? 241 TYR B OH  1 
ATOM   6093 N N   . PHE B 1 242 ? -7.953  -20.541 28.780  1.00 26.71 ? 242 PHE B N   1 
ATOM   6094 C CA  . PHE B 1 242 ? -7.684  -21.921 29.177  1.00 31.67 ? 242 PHE B CA  1 
ATOM   6095 C C   . PHE B 1 242 ? -6.422  -22.445 28.502  1.00 31.46 ? 242 PHE B C   1 
ATOM   6096 O O   . PHE B 1 242 ? -5.591  -23.095 29.149  1.00 27.84 ? 242 PHE B O   1 
ATOM   6097 C CB  . PHE B 1 242 ? -8.893  -22.794 28.836  1.00 32.15 ? 242 PHE B CB  1 
ATOM   6098 C CG  . PHE B 1 242 ? -8.938  -24.115 29.555  1.00 35.02 ? 242 PHE B CG  1 
ATOM   6099 C CD1 . PHE B 1 242 ? -9.317  -24.182 30.881  1.00 37.89 ? 242 PHE B CD1 1 
ATOM   6100 C CD2 . PHE B 1 242 ? -8.660  -25.293 28.884  1.00 29.60 ? 242 PHE B CD2 1 
ATOM   6101 C CE1 . PHE B 1 242 ? -9.385  -25.391 31.541  1.00 33.86 ? 242 PHE B CE1 1 
ATOM   6102 C CE2 . PHE B 1 242 ? -8.723  -26.507 29.530  1.00 26.34 ? 242 PHE B CE2 1 
ATOM   6103 C CZ  . PHE B 1 242 ? -9.086  -26.565 30.864  1.00 31.72 ? 242 PHE B CZ  1 
ATOM   6104 N N   . GLU B 1 243 ? -6.241  -22.152 27.207  1.00 27.23 ? 243 GLU B N   1 
ATOM   6105 C CA  . GLU B 1 243 ? -5.045  -22.641 26.516  1.00 35.66 ? 243 GLU B CA  1 
ATOM   6106 C C   . GLU B 1 243 ? -3.776  -22.065 27.136  1.00 33.21 ? 243 GLU B C   1 
ATOM   6107 O O   . GLU B 1 243 ? -2.771  -22.768 27.283  1.00 34.52 ? 243 GLU B O   1 
ATOM   6108 C CB  . GLU B 1 243 ? -5.114  -22.298 25.025  1.00 45.43 ? 243 GLU B CB  1 
ATOM   6109 C CG  . GLU B 1 243 ? -3.779  -22.421 24.275  1.00 54.61 ? 243 GLU B CG  1 
ATOM   6110 C CD  . GLU B 1 243 ? -3.736  -21.593 22.992  1.00 57.57 ? 243 GLU B CD  1 
ATOM   6111 O OE1 . GLU B 1 243 ? -4.814  -21.257 22.463  1.00 59.28 ? 243 GLU B OE1 1 
ATOM   6112 O OE2 . GLU B 1 243 ? -2.624  -21.278 22.514  1.00 58.79 ? 243 GLU B OE2 1 
ATOM   6113 N N   . ILE B 1 244 ? -3.812  -20.791 27.516  1.00 30.40 ? 244 ILE B N   1 
ATOM   6114 C CA  . ILE B 1 244 ? -2.609  -20.088 27.955  1.00 34.26 ? 244 ILE B CA  1 
ATOM   6115 C C   . ILE B 1 244 ? -2.307  -20.389 29.417  1.00 33.85 ? 244 ILE B C   1 
ATOM   6116 O O   . ILE B 1 244 ? -1.149  -20.636 29.782  1.00 26.93 ? 244 ILE B O   1 
ATOM   6117 C CB  . ILE B 1 244 ? -2.754  -18.569 27.725  1.00 35.20 ? 244 ILE B CB  1 
ATOM   6118 C CG1 . ILE B 1 244 ? -2.985  -18.240 26.245  1.00 33.87 ? 244 ILE B CG1 1 
ATOM   6119 C CG2 . ILE B 1 244 ? -1.523  -17.827 28.251  1.00 38.10 ? 244 ILE B CG2 1 
ATOM   6120 C CD1 . ILE B 1 244 ? -1.815  -18.587 25.327  1.00 35.73 ? 244 ILE B CD1 1 
ATOM   6121 N N   . PHE B 1 245 ? -3.336  -20.342 30.278  1.00 32.85 ? 245 PHE B N   1 
ATOM   6122 C CA  . PHE B 1 245 ? -3.169  -20.466 31.724  1.00 31.35 ? 245 PHE B CA  1 
ATOM   6123 C C   . PHE B 1 245 ? -3.738  -21.752 32.299  1.00 30.89 ? 245 PHE B C   1 
ATOM   6124 O O   . PHE B 1 245 ? -3.504  -22.045 33.476  1.00 37.47 ? 245 PHE B O   1 
ATOM   6125 C CB  . PHE B 1 245 ? -3.812  -19.270 32.446  1.00 29.98 ? 245 PHE B CB  1 
ATOM   6126 C CG  . PHE B 1 245 ? -3.286  -17.943 31.984  1.00 33.30 ? 245 PHE B CG  1 
ATOM   6127 C CD1 . PHE B 1 245 ? -2.006  -17.528 32.333  1.00 25.74 ? 245 PHE B CD1 1 
ATOM   6128 C CD2 . PHE B 1 245 ? -4.051  -17.121 31.180  1.00 33.14 ? 245 PHE B CD2 1 
ATOM   6129 C CE1 . PHE B 1 245 ? -1.508  -16.319 31.891  1.00 28.53 ? 245 PHE B CE1 1 
ATOM   6130 C CE2 . PHE B 1 245 ? -3.559  -15.901 30.736  1.00 32.82 ? 245 PHE B CE2 1 
ATOM   6131 C CZ  . PHE B 1 245 ? -2.283  -15.502 31.095  1.00 32.26 ? 245 PHE B CZ  1 
ATOM   6132 N N   . GLY B 1 246 ? -4.500  -22.508 31.528  1.00 26.38 ? 246 GLY B N   1 
ATOM   6133 C CA  . GLY B 1 246 ? -4.907  -23.820 31.994  1.00 29.44 ? 246 GLY B CA  1 
ATOM   6134 C C   . GLY B 1 246 ? -6.067  -23.830 32.957  1.00 33.22 ? 246 GLY B C   1 
ATOM   6135 O O   . GLY B 1 246 ? -6.318  -24.859 33.589  1.00 32.05 ? 246 GLY B O   1 
ATOM   6136 N N   . GLU B 1 247 ? -6.780  -22.719 33.103  1.00 29.84 ? 247 GLU B N   1 
ATOM   6137 C CA  . GLU B 1 247 ? -7.992  -22.679 33.907  1.00 33.14 ? 247 GLU B CA  1 
ATOM   6138 C C   . GLU B 1 247 ? -8.987  -21.785 33.188  1.00 31.63 ? 247 GLU B C   1 
ATOM   6139 O O   . GLU B 1 247 ? -8.615  -21.003 32.313  1.00 32.27 ? 247 GLU B O   1 
ATOM   6140 C CB  . GLU B 1 247 ? -7.727  -22.154 35.327  1.00 39.24 ? 247 GLU B CB  1 
ATOM   6141 C CG  . GLU B 1 247 ? -7.104  -20.765 35.344  1.00 49.61 ? 247 GLU B CG  1 
ATOM   6142 C CD  . GLU B 1 247 ? -6.691  -20.302 36.734  1.00 58.55 ? 247 GLU B CD  1 
ATOM   6143 O OE1 . GLU B 1 247 ? -5.954  -21.050 37.416  1.00 63.36 ? 247 GLU B OE1 1 
ATOM   6144 O OE2 . GLU B 1 247 ? -7.090  -19.184 37.135  1.00 59.07 ? 247 GLU B OE2 1 
ATOM   6145 N N   . HIS B 1 248 ? -10.243 -21.922 33.540  1.00 29.28 ? 248 HIS B N   1 
ATOM   6146 C CA  . HIS B 1 248 ? -11.203 -20.996 32.952  1.00 33.03 ? 248 HIS B CA  1 
ATOM   6147 C C   . HIS B 1 248 ? -11.173 -19.677 33.714  1.00 28.04 ? 248 HIS B C   1 
ATOM   6148 O O   . HIS B 1 248 ? -11.022 -19.673 34.937  1.00 35.72 ? 248 HIS B O   1 
ATOM   6149 C CB  . HIS B 1 248 ? -12.611 -21.586 32.970  1.00 41.59 ? 248 HIS B CB  1 
ATOM   6150 C CG  . HIS B 1 248 ? -12.836 -22.626 31.914  1.00 52.39 ? 248 HIS B CG  1 
ATOM   6151 N ND1 . HIS B 1 248 ? -12.915 -22.320 30.572  1.00 53.67 ? 248 HIS B ND1 1 
ATOM   6152 C CD2 . HIS B 1 248 ? -12.980 -23.970 32.002  1.00 55.65 ? 248 HIS B CD2 1 
ATOM   6153 C CE1 . HIS B 1 248 ? -13.107 -23.429 29.880  1.00 55.75 ? 248 HIS B CE1 1 
ATOM   6154 N NE2 . HIS B 1 248 ? -13.149 -24.445 30.724  1.00 57.53 ? 248 HIS B NE2 1 
ATOM   6155 N N   . PRO B 1 249 ? -11.291 -18.545 33.023  1.00 26.75 ? 249 PRO B N   1 
ATOM   6156 C CA  . PRO B 1 249 ? -11.218 -17.257 33.723  1.00 23.49 ? 249 PRO B CA  1 
ATOM   6157 C C   . PRO B 1 249 ? -12.499 -16.987 34.496  1.00 30.30 ? 249 PRO B C   1 
ATOM   6158 O O   . PRO B 1 249 ? -13.607 -17.218 34.003  1.00 37.45 ? 249 PRO B O   1 
ATOM   6159 C CB  . PRO B 1 249 ? -11.017 -16.245 32.587  1.00 25.38 ? 249 PRO B CB  1 
ATOM   6160 C CG  . PRO B 1 249 ? -11.707 -16.877 31.396  1.00 26.84 ? 249 PRO B CG  1 
ATOM   6161 C CD  . PRO B 1 249 ? -11.542 -18.390 31.576  1.00 26.23 ? 249 PRO B CD  1 
ATOM   6162 N N   . VAL B 1 250 ? -12.345 -16.524 35.738  1.00 28.02 ? 250 VAL B N   1 
ATOM   6163 C CA  . VAL B 1 250 ? -13.491 -16.080 36.531  1.00 24.29 ? 250 VAL B CA  1 
ATOM   6164 C C   . VAL B 1 250 ? -13.563 -14.563 36.627  1.00 19.17 ? 250 VAL B C   1 
ATOM   6165 O O   . VAL B 1 250 ? -14.516 -14.041 37.219  1.00 27.17 ? 250 VAL B O   1 
ATOM   6166 C CB  . VAL B 1 250 ? -13.502 -16.702 37.951  1.00 27.66 ? 250 VAL B CB  1 
ATOM   6167 C CG1 . VAL B 1 250 ? -13.677 -18.212 37.895  1.00 27.24 ? 250 VAL B CG1 1 
ATOM   6168 C CG2 . VAL B 1 250 ? -12.245 -16.354 38.720  1.00 26.54 ? 250 VAL B CG2 1 
ATOM   6169 N N   . TYR B 1 251 ? -12.565 -13.852 36.107  1.00 19.32 ? 251 TYR B N   1 
ATOM   6170 C CA  . TYR B 1 251 ? -12.547 -12.399 36.014  1.00 21.62 ? 251 TYR B CA  1 
ATOM   6171 C C   . TYR B 1 251 ? -12.471 -12.010 34.553  1.00 21.50 ? 251 TYR B C   1 
ATOM   6172 O O   . TYR B 1 251 ? -11.692 -12.596 33.784  1.00 21.74 ? 251 TYR B O   1 
ATOM   6173 C CB  . TYR B 1 251 ? -11.325 -11.803 36.737  1.00 27.80 ? 251 TYR B CB  1 
ATOM   6174 C CG  . TYR B 1 251 ? -11.067 -12.479 38.035  1.00 27.52 ? 251 TYR B CG  1 
ATOM   6175 C CD1 . TYR B 1 251 ? -12.025 -12.446 39.036  1.00 34.43 ? 251 TYR B CD1 1 
ATOM   6176 C CD2 . TYR B 1 251 ? -9.888  -13.177 38.263  1.00 35.55 ? 251 TYR B CD2 1 
ATOM   6177 C CE1 . TYR B 1 251 ? -11.821 -13.072 40.230  1.00 38.67 ? 251 TYR B CE1 1 
ATOM   6178 C CE2 . TYR B 1 251 ? -9.671  -13.809 39.467  1.00 35.06 ? 251 TYR B CE2 1 
ATOM   6179 C CZ  . TYR B 1 251 ? -10.649 -13.750 40.446  1.00 39.61 ? 251 TYR B CZ  1 
ATOM   6180 O OH  . TYR B 1 251 ? -10.491 -14.378 41.652  1.00 47.28 ? 251 TYR B OH  1 
ATOM   6181 N N   . MET B 1 252 ? -13.261 -11.015 34.172  1.00 19.20 ? 252 MET B N   1 
ATOM   6182 C CA  . MET B 1 252 ? -13.162 -10.479 32.822  1.00 15.74 ? 252 MET B CA  1 
ATOM   6183 C C   . MET B 1 252 ? -13.209 -8.970  32.909  1.00 13.70 ? 252 MET B C   1 
ATOM   6184 O O   . MET B 1 252 ? -13.877 -8.402  33.777  1.00 16.49 ? 252 MET B O   1 
ATOM   6185 C CB  . MET B 1 252 ? -14.282 -10.977 31.892  1.00 18.66 ? 252 MET B CB  1 
ATOM   6186 C CG  . MET B 1 252 ? -13.993 -12.336 31.281  1.00 21.66 ? 252 MET B CG  1 
ATOM   6187 S SD  . MET B 1 252 ? -14.886 -12.606 29.714  1.00 22.60 ? 252 MET B SD  1 
ATOM   6188 C CE  . MET B 1 252 ? -14.360 -14.281 29.406  1.00 20.55 ? 252 MET B CE  1 
ATOM   6189 N N   . TRP B 1 253 ? -12.486 -8.332  32.000  1.00 13.05 ? 253 TRP B N   1 
ATOM   6190 C CA  . TRP B 1 253 ? -12.595 -6.896  31.818  1.00 11.67 ? 253 TRP B CA  1 
ATOM   6191 C C   . TRP B 1 253 ? -13.558 -6.653  30.677  1.00 14.57 ? 253 TRP B C   1 
ATOM   6192 O O   . TRP B 1 253 ? -13.306 -7.118  29.555  1.00 16.44 ? 253 TRP B O   1 
ATOM   6193 C CB  . TRP B 1 253 ? -11.237 -6.275  31.506  1.00 14.61 ? 253 TRP B CB  1 
ATOM   6194 C CG  . TRP B 1 253 ? -11.338 -4.848  31.043  1.00 12.84 ? 253 TRP B CG  1 
ATOM   6195 C CD1 . TRP B 1 253 ? -11.008 -4.359  29.786  1.00 14.92 ? 253 TRP B CD1 1 
ATOM   6196 C CD2 . TRP B 1 253 ? -11.820 -3.728  31.794  1.00 14.33 ? 253 TRP B CD2 1 
ATOM   6197 N NE1 . TRP B 1 253 ? -11.247 -3.017  29.732  1.00 12.68 ? 253 TRP B NE1 1 
ATOM   6198 C CE2 . TRP B 1 253 ? -11.749 -2.596  30.940  1.00 13.02 ? 253 TRP B CE2 1 
ATOM   6199 C CE3 . TRP B 1 253 ? -12.320 -3.566  33.097  1.00 17.39 ? 253 TRP B CE3 1 
ATOM   6200 C CZ2 . TRP B 1 253 ? -12.155 -1.329  31.344  1.00 15.87 ? 253 TRP B CZ2 1 
ATOM   6201 C CZ3 . TRP B 1 253 ? -12.706 -2.284  33.512  1.00 15.36 ? 253 TRP B CZ3 1 
ATOM   6202 C CH2 . TRP B 1 253 ? -12.640 -1.188  32.621  1.00 15.28 ? 253 TRP B CH2 1 
ATOM   6203 N N   . PRO B 1 254 ? -14.690 -6.001  30.910  1.00 12.21 ? 254 PRO B N   1 
ATOM   6204 C CA  . PRO B 1 254 ? -15.584 -5.692  29.798  1.00 13.36 ? 254 PRO B CA  1 
ATOM   6205 C C   . PRO B 1 254 ? -14.980 -4.588  28.957  1.00 14.54 ? 254 PRO B C   1 
ATOM   6206 O O   . PRO B 1 254 ? -14.650 -3.520  29.476  1.00 14.48 ? 254 PRO B O   1 
ATOM   6207 C CB  . PRO B 1 254 ? -16.881 -5.244  30.483  1.00 14.56 ? 254 PRO B CB  1 
ATOM   6208 C CG  . PRO B 1 254 ? -16.439 -4.733  31.835  1.00 18.22 ? 254 PRO B CG  1 
ATOM   6209 C CD  . PRO B 1 254 ? -15.162 -5.475  32.208  1.00 14.95 ? 254 PRO B CD  1 
ATOM   6210 N N   . PRO B 1 255 ? -14.819 -4.799  27.654  1.00 13.39 ? 255 PRO B N   1 
ATOM   6211 C CA  . PRO B 1 255 ? -14.170 -3.762  26.832  1.00 13.85 ? 255 PRO B CA  1 
ATOM   6212 C C   . PRO B 1 255 ? -14.864 -2.411  26.978  1.00 14.44 ? 255 PRO B C   1 
ATOM   6213 O O   . PRO B 1 255 ? -16.099 -2.314  26.986  1.00 15.21 ? 255 PRO B O   1 
ATOM   6214 C CB  . PRO B 1 255 ? -14.271 -4.318  25.409  1.00 12.80 ? 255 PRO B CB  1 
ATOM   6215 C CG  . PRO B 1 255 ? -14.250 -5.826  25.604  1.00 17.02 ? 255 PRO B CG  1 
ATOM   6216 C CD  . PRO B 1 255 ? -15.055 -6.050  26.908  1.00 12.37 ? 255 PRO B CD  1 
ATOM   6217 N N   . LEU B 1 256 ? -14.046 -1.360  27.102  1.00 15.10 ? 256 LEU B N   1 
ATOM   6218 C CA  . LEU B 1 256 ? -14.497 0.026   27.292  1.00 12.47 ? 256 LEU B CA  1 
ATOM   6219 C C   . LEU B 1 256 ? -15.334 0.183   28.560  1.00 13.05 ? 256 LEU B C   1 
ATOM   6220 O O   . LEU B 1 256 ? -16.112 1.130   28.682  1.00 15.18 ? 256 LEU B O   1 
ATOM   6221 C CB  . LEU B 1 256 ? -15.280 0.537   26.070  1.00 12.79 ? 256 LEU B CB  1 
ATOM   6222 C CG  . LEU B 1 256 ? -14.514 0.169   24.780  1.00 20.27 ? 256 LEU B CG  1 
ATOM   6223 C CD1 . LEU B 1 256 ? -15.352 0.349   23.580  1.00 29.05 ? 256 LEU B CD1 1 
ATOM   6224 C CD2 . LEU B 1 256 ? -13.183 0.942   24.662  1.00 18.54 ? 256 LEU B CD2 1 
ATOM   6225 N N   . ALA B 1 257 ? -15.113 -0.701  29.538  1.00 13.54 ? 257 ALA B N   1 
ATOM   6226 C CA  . ALA B 1 257 ? -15.912 -0.756  30.754  1.00 12.40 ? 257 ALA B CA  1 
ATOM   6227 C C   . ALA B 1 257 ? -17.393 -0.974  30.456  1.00 13.96 ? 257 ALA B C   1 
ATOM   6228 O O   . ALA B 1 257 ? -18.254 -0.610  31.279  1.00 16.25 ? 257 ALA B O   1 
ATOM   6229 C CB  . ALA B 1 257 ? -15.728 0.521   31.594  1.00 12.72 ? 257 ALA B CB  1 
ATOM   6230 N N   . SER B 1 258 ? -17.723 -1.513  29.277  1.00 14.72 ? 258 SER B N   1 
ATOM   6231 C CA  . SER B 1 258 ? -19.098 -1.429  28.793  1.00 13.62 ? 258 SER B CA  1 
ATOM   6232 C C   . SER B 1 258 ? -19.957 -2.512  29.411  1.00 14.88 ? 258 SER B C   1 
ATOM   6233 O O   . SER B 1 258 ? -19.672 -3.708  29.271  1.00 16.60 ? 258 SER B O   1 
ATOM   6234 C CB  . SER B 1 258 ? -19.172 -1.511  27.274  1.00 15.93 ? 258 SER B CB  1 
ATOM   6235 O OG  . SER B 1 258 ? -20.445 -1.001  26.865  1.00 19.37 ? 258 SER B OG  1 
ATOM   6236 N N   . VAL B 1 259 ? -21.050 -2.098  30.047  1.00 14.69 ? 259 VAL B N   1 
ATOM   6237 C CA  . VAL B 1 259 ? -21.969 -3.041  30.657  1.00 14.43 ? 259 VAL B CA  1 
ATOM   6238 C C   . VAL B 1 259 ? -23.384 -2.567  30.367  1.00 14.10 ? 259 VAL B C   1 
ATOM   6239 O O   . VAL B 1 259 ? -23.627 -1.411  30.000  1.00 18.52 ? 259 VAL B O   1 
ATOM   6240 C CB  . VAL B 1 259 ? -21.759 -3.199  32.184  1.00 15.56 ? 259 VAL B CB  1 
ATOM   6241 C CG1 . VAL B 1 259 ? -20.342 -3.778  32.462  1.00 16.99 ? 259 VAL B CG1 1 
ATOM   6242 C CG2 . VAL B 1 259 ? -21.936 -1.856  32.897  1.00 17.97 ? 259 VAL B CG2 1 
ATOM   6243 N N   . SER B 1 260 ? -24.310 -3.492  30.557  1.00 15.74 ? 260 SER B N   1 
ATOM   6244 C CA  . SER B 1 260 ? -25.744 -3.286  30.495  1.00 15.47 ? 260 SER B CA  1 
ATOM   6245 C C   . SER B 1 260 ? -26.340 -4.420  31.300  1.00 17.41 ? 260 SER B C   1 
ATOM   6246 O O   . SER B 1 260 ? -25.644 -5.378  31.630  1.00 19.18 ? 260 SER B O   1 
ATOM   6247 C CB  . SER B 1 260 ? -26.262 -3.327  29.058  1.00 20.20 ? 260 SER B CB  1 
ATOM   6248 O OG  . SER B 1 260 ? -26.001 -4.619  28.517  1.00 20.23 ? 260 SER B OG  1 
ATOM   6249 N N   . ASN B 1 261 ? -27.649 -4.336  31.580  1.00 17.87 ? 261 ASN B N   1 
ATOM   6250 C CA  . ASN B 1 261 ? -28.281 -5.454  32.272  1.00 21.14 ? 261 ASN B CA  1 
ATOM   6251 C C   . ASN B 1 261 ? -28.083 -6.759  31.501  1.00 21.52 ? 261 ASN B C   1 
ATOM   6252 O O   . ASN B 1 261 ? -27.726 -7.788  32.093  1.00 22.19 ? 261 ASN B O   1 
ATOM   6253 C CB  . ASN B 1 261 ? -29.767 -5.172  32.493  1.00 19.96 ? 261 ASN B CB  1 
ATOM   6254 C CG  . ASN B 1 261 ? -29.996 -4.024  33.450  1.00 22.32 ? 261 ASN B CG  1 
ATOM   6255 O OD1 . ASN B 1 261 ? -29.158 -3.746  34.310  1.00 21.63 ? 261 ASN B OD1 1 
ATOM   6256 N ND2 . ASN B 1 261 ? -31.127 -3.348  33.309  1.00 24.65 ? 261 ASN B ND2 1 
ATOM   6257 N N   . GLU B 1 262 ? -28.288 -6.728  30.179  1.00 19.14 ? 262 GLU B N   1 
ATOM   6258 C CA  . GLU B 1 262 ? -28.147 -7.950  29.393  1.00 19.55 ? 262 GLU B CA  1 
ATOM   6259 C C   . GLU B 1 262 ? -26.699 -8.418  29.346  1.00 21.47 ? 262 GLU B C   1 
ATOM   6260 O O   . GLU B 1 262 ? -26.432 -9.627  29.369  1.00 19.48 ? 262 GLU B O   1 
ATOM   6261 C CB  . GLU B 1 262 ? -28.700 -7.740  27.984  1.00 18.51 ? 262 GLU B CB  1 
ATOM   6262 C CG  . GLU B 1 262 ? -30.221 -7.614  28.001  1.00 23.26 ? 262 GLU B CG  1 
ATOM   6263 C CD  . GLU B 1 262 ? -30.798 -7.565  26.610  1.00 34.93 ? 262 GLU B CD  1 
ATOM   6264 O OE1 . GLU B 1 262 ? -30.132 -8.075  25.689  1.00 36.58 ? 262 GLU B OE1 1 
ATOM   6265 O OE2 . GLU B 1 262 ? -31.910 -7.015  26.437  1.00 42.20 ? 262 GLU B OE2 1 
ATOM   6266 N N   . ALA B 1 263 ? -25.746 -7.489  29.287  1.00 18.65 ? 263 ALA B N   1 
ATOM   6267 C CA  . ALA B 1 263 ? -24.349 -7.916  29.221  1.00 16.21 ? 263 ALA B CA  1 
ATOM   6268 C C   . ALA B 1 263 ? -23.898 -8.543  30.533  1.00 17.89 ? 263 ALA B C   1 
ATOM   6269 O O   . ALA B 1 263 ? -23.178 -9.550  30.529  1.00 19.63 ? 263 ALA B O   1 
ATOM   6270 C CB  . ALA B 1 263 ? -23.437 -6.749  28.840  1.00 17.42 ? 263 ALA B CB  1 
ATOM   6271 N N   . LEU B 1 264 ? -24.325 -7.982  31.668  1.00 16.87 ? 264 LEU B N   1 
ATOM   6272 C CA  . LEU B 1 264 ? -23.980 -8.586  32.957  1.00 17.86 ? 264 LEU B CA  1 
ATOM   6273 C C   . LEU B 1 264 ? -24.584 -9.977  33.097  1.00 18.72 ? 264 LEU B C   1 
ATOM   6274 O O   . LEU B 1 264 ? -23.949 -10.875 33.660  1.00 18.82 ? 264 LEU B O   1 
ATOM   6275 C CB  . LEU B 1 264 ? -24.449 -7.698  34.116  1.00 19.83 ? 264 LEU B CB  1 
ATOM   6276 C CG  . LEU B 1 264 ? -23.718 -6.355  34.205  1.00 22.35 ? 264 LEU B CG  1 
ATOM   6277 C CD1 . LEU B 1 264 ? -24.387 -5.456  35.233  1.00 27.33 ? 264 LEU B CD1 1 
ATOM   6278 C CD2 . LEU B 1 264 ? -22.268 -6.583  34.567  1.00 22.43 ? 264 LEU B CD2 1 
ATOM   6279 N N   . GLU B 1 265 ? -25.820 -10.169 32.601  1.00 18.76 ? 265 GLU B N   1 
ATOM   6280 C CA  . GLU B 1 265 ? -26.416 -11.499 32.593  1.00 20.72 ? 265 GLU B CA  1 
ATOM   6281 C C   . GLU B 1 265 ? -25.589 -12.472 31.760  1.00 21.08 ? 265 GLU B C   1 
ATOM   6282 O O   . GLU B 1 265 ? -25.379 -13.621 32.167  1.00 22.55 ? 265 GLU B O   1 
ATOM   6283 C CB  . GLU B 1 265 ? -27.851 -11.435 32.053  1.00 26.05 ? 265 GLU B CB  1 
ATOM   6284 C CG  . GLU B 1 265 ? -28.818 -10.688 32.951  1.00 43.12 ? 265 GLU B CG  1 
ATOM   6285 C CD  . GLU B 1 265 ? -29.342 -11.547 34.088  1.00 59.91 ? 265 GLU B CD  1 
ATOM   6286 O OE1 . GLU B 1 265 ? -30.105 -11.019 34.929  1.00 62.05 ? 265 GLU B OE1 1 
ATOM   6287 O OE2 . GLU B 1 265 ? -28.990 -12.748 34.138  1.00 66.00 ? 265 GLU B OE2 1 
ATOM   6288 N N   . LEU B 1 266 ? -25.130 -12.036 30.583  1.00 21.38 ? 266 LEU B N   1 
ATOM   6289 C CA  . LEU B 1 266 ? -24.309 -12.900 29.734  1.00 17.29 ? 266 LEU B CA  1 
ATOM   6290 C C   . LEU B 1 266 ? -23.013 -13.302 30.439  1.00 21.33 ? 266 LEU B C   1 
ATOM   6291 O O   . LEU B 1 266 ? -22.653 -14.486 30.457  1.00 19.62 ? 266 LEU B O   1 
ATOM   6292 C CB  . LEU B 1 266 ? -24.010 -12.200 28.402  1.00 17.91 ? 266 LEU B CB  1 
ATOM   6293 C CG  . LEU B 1 266 ? -22.994 -12.918 27.504  1.00 19.49 ? 266 LEU B CG  1 
ATOM   6294 C CD1 . LEU B 1 266 ? -23.549 -14.238 27.053  1.00 20.10 ? 266 LEU B CD1 1 
ATOM   6295 C CD2 . LEU B 1 266 ? -22.591 -12.054 26.308  1.00 18.72 ? 266 LEU B CD2 1 
ATOM   6296 N N   . TYR B 1 267 ? -22.297 -12.335 31.030  1.00 16.71 ? 267 TYR B N   1 
ATOM   6297 C CA  . TYR B 1 267 ? -21.070 -12.674 31.747  1.00 19.82 ? 267 TYR B CA  1 
ATOM   6298 C C   . TYR B 1 267 ? -21.358 -13.669 32.864  1.00 27.30 ? 267 TYR B C   1 
ATOM   6299 O O   . TYR B 1 267 ? -20.613 -14.639 33.051  1.00 22.10 ? 267 TYR B O   1 
ATOM   6300 C CB  . TYR B 1 267 ? -20.412 -11.415 32.311  1.00 18.32 ? 267 TYR B CB  1 
ATOM   6301 C CG  . TYR B 1 267 ? -19.731 -10.564 31.273  1.00 19.36 ? 267 TYR B CG  1 
ATOM   6302 C CD1 . TYR B 1 267 ? -18.635 -11.046 30.558  1.00 21.27 ? 267 TYR B CD1 1 
ATOM   6303 C CD2 . TYR B 1 267 ? -20.163 -9.260  31.023  1.00 18.22 ? 267 TYR B CD2 1 
ATOM   6304 C CE1 . TYR B 1 267 ? -18.004 -10.262 29.616  1.00 23.22 ? 267 TYR B CE1 1 
ATOM   6305 C CE2 . TYR B 1 267 ? -19.542 -8.467  30.068  1.00 15.86 ? 267 TYR B CE2 1 
ATOM   6306 C CZ  . TYR B 1 267 ? -18.463 -8.972  29.377  1.00 17.17 ? 267 TYR B CZ  1 
ATOM   6307 O OH  . TYR B 1 267 ? -17.844 -8.189  28.432  1.00 18.26 ? 267 TYR B OH  1 
ATOM   6308 N N   . TYR B 1 268 ? -22.458 -13.462 33.595  1.00 18.97 ? 268 TYR B N   1 
ATOM   6309 C CA  . TYR B 1 268 ? -22.845 -14.400 34.642  1.00 19.05 ? 268 TYR B CA  1 
ATOM   6310 C C   . TYR B 1 268 ? -23.115 -15.789 34.072  1.00 21.64 ? 268 TYR B C   1 
ATOM   6311 O O   . TYR B 1 268 ? -22.679 -16.800 34.634  1.00 21.68 ? 268 TYR B O   1 
ATOM   6312 C CB  . TYR B 1 268 ? -24.089 -13.878 35.358  1.00 20.36 ? 268 TYR B CB  1 
ATOM   6313 C CG  . TYR B 1 268 ? -24.800 -14.975 36.074  1.00 23.03 ? 268 TYR B CG  1 
ATOM   6314 C CD1 . TYR B 1 268 ? -24.260 -15.526 37.223  1.00 25.40 ? 268 TYR B CD1 1 
ATOM   6315 C CD2 . TYR B 1 268 ? -25.995 -15.478 35.592  1.00 24.49 ? 268 TYR B CD2 1 
ATOM   6316 C CE1 . TYR B 1 268 ? -24.897 -16.538 37.882  1.00 30.04 ? 268 TYR B CE1 1 
ATOM   6317 C CE2 . TYR B 1 268 ? -26.638 -16.493 36.241  1.00 30.07 ? 268 TYR B CE2 1 
ATOM   6318 C CZ  . TYR B 1 268 ? -26.088 -17.016 37.382  1.00 35.21 ? 268 TYR B CZ  1 
ATOM   6319 O OH  . TYR B 1 268 ? -26.736 -18.036 38.028  1.00 44.83 ? 268 TYR B OH  1 
ATOM   6320 N N   . GLU B 1 269 ? -23.893 -15.860 32.993  1.00 21.57 ? 269 GLU B N   1 
ATOM   6321 C CA  . GLU B 1 269 ? -24.217 -17.148 32.382  1.00 22.86 ? 269 GLU B CA  1 
ATOM   6322 C C   . GLU B 1 269 ? -22.973 -17.912 31.936  1.00 26.31 ? 269 GLU B C   1 
ATOM   6323 O O   . GLU B 1 269 ? -22.983 -19.152 31.908  1.00 28.83 ? 269 GLU B O   1 
ATOM   6324 C CB  . GLU B 1 269 ? -25.156 -16.933 31.194  1.00 25.05 ? 269 GLU B CB  1 
ATOM   6325 C CG  . GLU B 1 269 ? -26.619 -16.873 31.584  1.00 37.16 ? 269 GLU B CG  1 
ATOM   6326 C CD  . GLU B 1 269 ? -27.453 -16.032 30.627  1.00 51.57 ? 269 GLU B CD  1 
ATOM   6327 O OE1 . GLU B 1 269 ? -28.391 -15.343 31.094  1.00 51.96 ? 269 GLU B OE1 1 
ATOM   6328 O OE2 . GLU B 1 269 ? -27.167 -16.058 29.408  1.00 54.03 ? 269 GLU B OE2 1 
ATOM   6329 N N   . LYS B 1 270 ? -21.914 -17.202 31.565  1.00 21.78 ? 270 LYS B N   1 
ATOM   6330 C CA  . LYS B 1 270 ? -20.677 -17.797 31.087  1.00 23.01 ? 270 LYS B CA  1 
ATOM   6331 C C   . LYS B 1 270 ? -19.688 -18.082 32.211  1.00 25.76 ? 270 LYS B C   1 
ATOM   6332 O O   . LYS B 1 270 ? -18.530 -18.417 31.932  1.00 26.42 ? 270 LYS B O   1 
ATOM   6333 C CB  . LYS B 1 270 ? -20.034 -16.882 30.036  1.00 22.43 ? 270 LYS B CB  1 
ATOM   6334 C CG  . LYS B 1 270 ? -20.834 -16.778 28.720  1.00 25.05 ? 270 LYS B CG  1 
ATOM   6335 C CD  . LYS B 1 270 ? -20.992 -18.140 28.069  1.00 34.07 ? 270 LYS B CD  1 
ATOM   6336 C CE  . LYS B 1 270 ? -21.794 -18.052 26.773  1.00 40.32 ? 270 LYS B CE  1 
ATOM   6337 N NZ  . LYS B 1 270 ? -23.022 -18.895 26.814  1.00 47.85 ? 270 LYS B NZ  1 
ATOM   6338 N N   . GLY B 1 271 ? -20.098 -17.928 33.466  1.00 25.78 ? 271 GLY B N   1 
ATOM   6339 C CA  . GLY B 1 271 ? -19.245 -18.291 34.586  1.00 25.04 ? 271 GLY B CA  1 
ATOM   6340 C C   . GLY B 1 271 ? -18.303 -17.228 35.103  1.00 26.30 ? 271 GLY B C   1 
ATOM   6341 O O   . GLY B 1 271 ? -17.402 -17.553 35.886  1.00 27.12 ? 271 GLY B O   1 
ATOM   6342 N N   . ILE B 1 272 ? -18.452 -15.976 34.682  1.00 21.06 ? 272 ILE B N   1 
ATOM   6343 C CA  . ILE B 1 272 ? -17.633 -14.901 35.224  1.00 23.10 ? 272 ILE B CA  1 
ATOM   6344 C C   . ILE B 1 272 ? -18.170 -14.513 36.597  1.00 26.57 ? 272 ILE B C   1 
ATOM   6345 O O   . ILE B 1 272 ? -19.366 -14.260 36.753  1.00 22.39 ? 272 ILE B O   1 
ATOM   6346 C CB  . ILE B 1 272 ? -17.617 -13.698 34.268  1.00 20.00 ? 272 ILE B CB  1 
ATOM   6347 C CG1 . ILE B 1 272 ? -17.200 -14.147 32.860  1.00 24.71 ? 272 ILE B CG1 1 
ATOM   6348 C CG2 . ILE B 1 272 ? -16.701 -12.604 34.807  1.00 21.87 ? 272 ILE B CG2 1 
ATOM   6349 C CD1 . ILE B 1 272 ? -15.915 -14.933 32.819  1.00 28.68 ? 272 ILE B CD1 1 
ATOM   6350 N N   . ASN B 1 273 ? -17.286 -14.463 37.600  1.00 23.07 ? 273 ASN B N   1 
ATOM   6351 C CA  . ASN B 1 273 ? -17.714 -14.099 38.949  1.00 26.83 ? 273 ASN B CA  1 
ATOM   6352 C C   . ASN B 1 273 ? -17.491 -12.630 39.294  1.00 19.53 ? 273 ASN B C   1 
ATOM   6353 O O   . ASN B 1 273 ? -18.147 -12.122 40.215  1.00 21.16 ? 273 ASN B O   1 
ATOM   6354 C CB  . ASN B 1 273 ? -16.994 -14.957 39.992  1.00 29.21 ? 273 ASN B CB  1 
ATOM   6355 C CG  . ASN B 1 273 ? -17.406 -16.399 39.924  1.00 35.45 ? 273 ASN B CG  1 
ATOM   6356 O OD1 . ASN B 1 273 ? -18.575 -16.711 39.681  1.00 33.69 ? 273 ASN B OD1 1 
ATOM   6357 N ND2 . ASN B 1 273 ? -16.451 -17.292 40.131  1.00 39.19 ? 273 ASN B ND2 1 
ATOM   6358 N N   . MET B 1 274 ? -16.582 -11.947 38.605  1.00 20.38 ? 274 MET B N   1 
ATOM   6359 C CA  . MET B 1 274 ? -16.362 -10.542 38.893  1.00 22.02 ? 274 MET B CA  1 
ATOM   6360 C C   . MET B 1 274 ? -15.900 -9.813  37.639  1.00 21.44 ? 274 MET B C   1 
ATOM   6361 O O   . MET B 1 274 ? -15.182 -10.364 36.795  1.00 20.60 ? 274 MET B O   1 
ATOM   6362 C CB  . MET B 1 274 ? -15.339 -10.374 40.022  1.00 27.41 ? 274 MET B CB  1 
ATOM   6363 C CG  . MET B 1 274 ? -15.202 -8.943  40.491  1.00 33.45 ? 274 MET B CG  1 
ATOM   6364 S SD  . MET B 1 274 ? -13.875 -8.084  39.615  1.00 43.89 ? 274 MET B SD  1 
ATOM   6365 C CE  . MET B 1 274 ? -12.480 -8.594  40.640  1.00 37.73 ? 274 MET B CE  1 
ATOM   6366 N N   . LEU B 1 275 ? -16.312 -8.555  37.535  1.00 19.71 ? 275 LEU B N   1 
ATOM   6367 C CA  . LEU B 1 275 ? -15.767 -7.655  36.546  1.00 16.55 ? 275 LEU B CA  1 
ATOM   6368 C C   . LEU B 1 275 ? -15.692 -6.277  37.177  1.00 15.61 ? 275 LEU B C   1 
ATOM   6369 O O   . LEU B 1 275 ? -16.168 -6.061  38.296  1.00 18.37 ? 275 LEU B O   1 
ATOM   6370 C CB  . LEU B 1 275 ? -16.613 -7.645  35.265  1.00 22.34 ? 275 LEU B CB  1 
ATOM   6371 C CG  . LEU B 1 275 ? -18.117 -7.532  35.387  1.00 22.99 ? 275 LEU B CG  1 
ATOM   6372 C CD1 . LEU B 1 275 ? -18.487 -6.071  35.528  1.00 30.20 ? 275 LEU B CD1 1 
ATOM   6373 C CD2 . LEU B 1 275 ? -18.831 -8.134  34.176  1.00 25.07 ? 275 LEU B CD2 1 
ATOM   6374 N N   . ALA B 1 276 ? -15.110 -5.333  36.450  1.00 16.25 ? 276 ALA B N   1 
ATOM   6375 C CA  . ALA B 1 276 ? -15.172 -3.951  36.886  1.00 18.53 ? 276 ALA B CA  1 
ATOM   6376 C C   . ALA B 1 276 ? -15.725 -3.093  35.761  1.00 16.73 ? 276 ALA B C   1 
ATOM   6377 O O   . ALA B 1 276 ? -15.762 -3.495  34.597  1.00 16.32 ? 276 ALA B O   1 
ATOM   6378 C CB  . ALA B 1 276 ? -13.808 -3.418  37.330  1.00 20.27 ? 276 ALA B CB  1 
ATOM   6379 N N   . THR B 1 277 ? -16.199 -1.915  36.138  1.00 17.34 ? 277 THR B N   1 
ATOM   6380 C CA  . THR B 1 277 ? -16.678 -0.967  35.154  1.00 16.05 ? 277 THR B CA  1 
ATOM   6381 C C   . THR B 1 277 ? -16.407 0.425   35.708  1.00 17.76 ? 277 THR B C   1 
ATOM   6382 O O   . THR B 1 277 ? -15.541 0.598   36.576  1.00 20.57 ? 277 THR B O   1 
ATOM   6383 C CB  . THR B 1 277 ? -18.152 -1.257  34.790  1.00 14.21 ? 277 THR B CB  1 
ATOM   6384 O OG1 . THR B 1 277 ? -18.615 -0.277  33.854  1.00 18.70 ? 277 THR B OG1 1 
ATOM   6385 C CG2 . THR B 1 277 ? -19.025 -1.244  36.016  1.00 18.94 ? 277 THR B CG2 1 
ATOM   6386 N N   . ASP B 1 278 ? -17.073 1.431   35.156  1.00 17.05 ? 278 ASP B N   1 
ATOM   6387 C CA  . ASP B 1 278 ? -16.715 2.814   35.419  1.00 15.65 ? 278 ASP B CA  1 
ATOM   6388 C C   . ASP B 1 278 ? -17.643 3.498   36.420  1.00 17.35 ? 278 ASP B C   1 
ATOM   6389 O O   . ASP B 1 278 ? -18.849 3.241   36.487  1.00 18.12 ? 278 ASP B O   1 
ATOM   6390 C CB  . ASP B 1 278 ? -16.685 3.615   34.113  1.00 18.99 ? 278 ASP B CB  1 
ATOM   6391 C CG  . ASP B 1 278 ? -16.163 5.027   34.309  1.00 21.71 ? 278 ASP B CG  1 
ATOM   6392 O OD1 . ASP B 1 278 ? -15.044 5.193   34.841  1.00 22.79 ? 278 ASP B OD1 1 
ATOM   6393 O OD2 . ASP B 1 278 ? -16.860 5.981   33.930  1.00 23.64 ? 278 ASP B OD2 1 
ATOM   6394 N N   . GLU B 1 279 ? -17.051 4.433   37.173  1.00 18.37 ? 279 GLU B N   1 
ATOM   6395 C CA  . GLU B 1 279 ? -17.781 5.223   38.162  1.00 23.31 ? 279 GLU B CA  1 
ATOM   6396 C C   . GLU B 1 279 ? -18.932 6.038   37.562  1.00 19.08 ? 279 GLU B C   1 
ATOM   6397 O O   . GLU B 1 279 ? -19.947 6.254   38.243  1.00 22.47 ? 279 GLU B O   1 
ATOM   6398 C CB  . GLU B 1 279 ? -16.785 6.131   38.892  1.00 24.96 ? 279 GLU B CB  1 
ATOM   6399 C CG  . GLU B 1 279 ? -17.303 6.798   40.121  1.00 28.08 ? 279 GLU B CG  1 
ATOM   6400 C CD  . GLU B 1 279 ? -16.228 7.596   40.862  1.00 29.53 ? 279 GLU B CD  1 
ATOM   6401 O OE1 . GLU B 1 279 ? -15.046 7.605   40.439  1.00 24.88 ? 279 GLU B OE1 1 
ATOM   6402 O OE2 . GLU B 1 279 ? -16.582 8.233   41.876  1.00 29.36 ? 279 GLU B OE2 1 
ATOM   6403 N N   . VAL B 1 280 ? -18.817 6.501   36.308  1.00 19.76 ? 280 VAL B N   1 
ATOM   6404 C CA  . VAL B 1 280 ? -19.928 7.256   35.712  1.00 20.18 ? 280 VAL B CA  1 
ATOM   6405 C C   . VAL B 1 280 ? -21.154 6.368   35.570  1.00 21.63 ? 280 VAL B C   1 
ATOM   6406 O O   . VAL B 1 280 ? -22.289 6.801   35.823  1.00 20.42 ? 280 VAL B O   1 
ATOM   6407 C CB  . VAL B 1 280 ? -19.523 7.879   34.364  1.00 22.15 ? 280 VAL B CB  1 
ATOM   6408 C CG1 . VAL B 1 280 ? -20.755 8.448   33.638  1.00 22.28 ? 280 VAL B CG1 1 
ATOM   6409 C CG2 . VAL B 1 280 ? -18.519 8.985   34.576  1.00 29.19 ? 280 VAL B CG2 1 
ATOM   6410 N N   . ILE B 1 281 ? -20.943 5.098   35.203  1.00 21.15 ? 281 ILE B N   1 
ATOM   6411 C CA  . ILE B 1 281 ? -22.056 4.157   35.084  1.00 21.00 ? 281 ILE B CA  1 
ATOM   6412 C C   . ILE B 1 281 ? -22.722 3.934   36.441  1.00 21.07 ? 281 ILE B C   1 
ATOM   6413 O O   . ILE B 1 281 ? -23.953 3.874   36.537  1.00 20.97 ? 281 ILE B O   1 
ATOM   6414 C CB  . ILE B 1 281 ? -21.562 2.847   34.438  1.00 21.15 ? 281 ILE B CB  1 
ATOM   6415 C CG1 . ILE B 1 281 ? -21.154 3.133   32.974  1.00 19.73 ? 281 ILE B CG1 1 
ATOM   6416 C CG2 . ILE B 1 281 ? -22.615 1.753   34.577  1.00 20.24 ? 281 ILE B CG2 1 
ATOM   6417 C CD1 . ILE B 1 281 ? -20.581 1.923   32.220  1.00 22.53 ? 281 ILE B CD1 1 
ATOM   6418 N N   . LEU B 1 282 ? -21.923 3.852   37.512  1.00 20.13 ? 282 LEU B N   1 
ATOM   6419 C CA  . LEU B 1 282 ? -22.470 3.755   38.865  1.00 18.39 ? 282 LEU B CA  1 
ATOM   6420 C C   . LEU B 1 282 ? -23.306 4.981   39.215  1.00 18.28 ? 282 LEU B C   1 
ATOM   6421 O O   . LEU B 1 282 ? -24.438 4.855   39.704  1.00 20.92 ? 282 LEU B O   1 
ATOM   6422 C CB  . LEU B 1 282 ? -21.327 3.572   39.880  1.00 19.27 ? 282 LEU B CB  1 
ATOM   6423 C CG  . LEU B 1 282 ? -21.732 3.339   41.345  1.00 24.06 ? 282 LEU B CG  1 
ATOM   6424 C CD1 . LEU B 1 282 ? -22.536 2.058   41.498  1.00 23.08 ? 282 LEU B CD1 1 
ATOM   6425 C CD2 . LEU B 1 282 ? -20.483 3.287   42.249  1.00 23.87 ? 282 LEU B CD2 1 
ATOM   6426 N N   . LYS B 1 283 ? -22.766 6.179   38.972  1.00 20.09 ? 283 LYS B N   1 
ATOM   6427 C CA  . LYS B 1 283 ? -23.515 7.397   39.298  1.00 21.17 ? 283 LYS B CA  1 
ATOM   6428 C C   . LYS B 1 283 ? -24.833 7.452   38.533  1.00 21.18 ? 283 LYS B C   1 
ATOM   6429 O O   . LYS B 1 283 ? -25.836 7.957   39.045  1.00 22.25 ? 283 LYS B O   1 
ATOM   6430 C CB  . LYS B 1 283 ? -22.682 8.640   38.986  1.00 26.21 ? 283 LYS B CB  1 
ATOM   6431 C CG  . LYS B 1 283 ? -21.497 8.864   39.932  1.00 35.14 ? 283 LYS B CG  1 
ATOM   6432 C CD  . LYS B 1 283 ? -20.750 10.149  39.560  1.00 42.05 ? 283 LYS B CD  1 
ATOM   6433 C CE  . LYS B 1 283 ? -20.153 10.836  40.785  1.00 54.37 ? 283 LYS B CE  1 
ATOM   6434 N NZ  . LYS B 1 283 ? -18.841 11.493  40.478  1.00 58.34 ? 283 LYS B NZ  1 
ATOM   6435 N N   . ASN B 1 284 ? -24.839 6.933   37.305  1.00 25.10 ? 284 ASN B N   1 
ATOM   6436 C CA  . ASN B 1 284 ? -26.043 6.889   36.481  1.00 21.44 ? 284 ASN B CA  1 
ATOM   6437 C C   . ASN B 1 284 ? -27.040 5.841   36.950  1.00 25.03 ? 284 ASN B C   1 
ATOM   6438 O O   . ASN B 1 284 ? -28.197 5.896   36.535  1.00 25.06 ? 284 ASN B O   1 
ATOM   6439 C CB  . ASN B 1 284 ? -25.687 6.565   35.024  1.00 24.16 ? 284 ASN B CB  1 
ATOM   6440 C CG  . ASN B 1 284 ? -25.030 7.717   34.305  1.00 30.89 ? 284 ASN B CG  1 
ATOM   6441 O OD1 . ASN B 1 284 ? -25.005 8.841   34.804  1.00 30.45 ? 284 ASN B OD1 1 
ATOM   6442 N ND2 . ASN B 1 284 ? -24.488 7.440   33.111  1.00 27.00 ? 284 ASN B ND2 1 
ATOM   6443 N N   . SER B 1 285 ? -26.605 4.855   37.745  1.00 23.22 ? 285 SER B N   1 
ATOM   6444 C CA  . SER B 1 285 ? -27.403 3.663   38.026  1.00 24.99 ? 285 SER B CA  1 
ATOM   6445 C C   . SER B 1 285 ? -27.940 3.574   39.445  1.00 26.41 ? 285 SER B C   1 
ATOM   6446 O O   . SER B 1 285 ? -28.997 2.977   39.644  1.00 27.03 ? 285 SER B O   1 
ATOM   6447 C CB  . SER B 1 285 ? -26.586 2.397   37.748  1.00 27.24 ? 285 SER B CB  1 
ATOM   6448 O OG  . SER B 1 285 ? -26.077 2.422   36.416  1.00 24.97 ? 285 SER B OG  1 
ATOM   6449 N N   . VAL B 1 286 ? -27.232 4.125   40.435  1.00 22.54 ? 286 VAL B N   1 
ATOM   6450 C CA  . VAL B 1 286 ? -27.656 4.078   41.829  1.00 26.10 ? 286 VAL B CA  1 
ATOM   6451 C C   . VAL B 1 286 ? -27.627 5.487   42.403  1.00 29.11 ? 286 VAL B C   1 
ATOM   6452 O O   . VAL B 1 286 ? -26.992 6.394   41.860  1.00 28.28 ? 286 VAL B O   1 
ATOM   6453 C CB  . VAL B 1 286 ? -26.770 3.159   42.694  1.00 32.18 ? 286 VAL B CB  1 
ATOM   6454 C CG1 . VAL B 1 286 ? -26.640 1.786   42.065  1.00 35.19 ? 286 VAL B CG1 1 
ATOM   6455 C CG2 . VAL B 1 286 ? -25.393 3.780   42.886  1.00 29.54 ? 286 VAL B CG2 1 
ATOM   6456 N N   . GLU B 1 287 ? -28.304 5.648   43.539  1.00 24.57 ? 287 GLU B N   1 
ATOM   6457 C CA  . GLU B 1 287 ? -28.290 6.935   44.227  1.00 24.00 ? 287 GLU B CA  1 
ATOM   6458 C C   . GLU B 1 287 ? -26.956 7.165   44.931  1.00 23.39 ? 287 GLU B C   1 
ATOM   6459 O O   . GLU B 1 287 ? -26.185 8.055   44.556  1.00 27.05 ? 287 GLU B O   1 
ATOM   6460 C CB  . GLU B 1 287 ? -29.458 6.999   45.208  1.00 25.54 ? 287 GLU B CB  1 
ATOM   6461 C CG  . GLU B 1 287 ? -30.773 6.927   44.474  1.00 33.65 ? 287 GLU B CG  1 
ATOM   6462 C CD  . GLU B 1 287 ? -31.906 7.376   45.335  1.00 46.68 ? 287 GLU B CD  1 
ATOM   6463 O OE1 . GLU B 1 287 ? -31.647 8.144   46.287  1.00 49.34 ? 287 GLU B OE1 1 
ATOM   6464 O OE2 . GLU B 1 287 ? -33.046 6.957   45.065  1.00 54.29 ? 287 GLU B OE2 1 
ATOM   6465 N N   . ARG B 1 288 ? -26.636 6.337   45.919  1.00 24.30 ? 288 ARG B N   1 
ATOM   6466 C CA  . ARG B 1 288 ? -25.454 6.562   46.750  1.00 24.11 ? 288 ARG B CA  1 
ATOM   6467 C C   . ARG B 1 288 ? -24.322 5.790   46.091  1.00 24.76 ? 288 ARG B C   1 
ATOM   6468 O O   . ARG B 1 288 ? -24.134 4.590   46.310  1.00 31.31 ? 288 ARG B O   1 
ATOM   6469 C CB  . ARG B 1 288 ? -25.727 6.154   48.194  1.00 23.75 ? 288 ARG B CB  1 
ATOM   6470 C CG  . ARG B 1 288 ? -26.909 6.920   48.809  1.00 25.45 ? 288 ARG B CG  1 
ATOM   6471 C CD  . ARG B 1 288 ? -27.402 6.313   50.149  1.00 26.43 ? 288 ARG B CD  1 
ATOM   6472 N NE  . ARG B 1 288 ? -27.870 4.942   49.954  1.00 30.95 ? 288 ARG B NE  1 
ATOM   6473 C CZ  . ARG B 1 288 ? -27.137 3.868   50.220  1.00 33.80 ? 288 ARG B CZ  1 
ATOM   6474 N NH1 . ARG B 1 288 ? -27.619 2.656   49.991  1.00 36.58 ? 288 ARG B NH1 1 
ATOM   6475 N NH2 . ARG B 1 288 ? -25.912 4.009   50.712  1.00 32.25 ? 288 ARG B NH2 1 
ATOM   6476 N N   . ALA B 1 289 ? -23.573 6.495   45.250  1.00 20.72 ? 289 ALA B N   1 
ATOM   6477 C CA  . ALA B 1 289 ? -22.693 5.869   44.258  1.00 19.36 ? 289 ALA B CA  1 
ATOM   6478 C C   . ALA B 1 289 ? -21.227 5.832   44.700  1.00 20.05 ? 289 ALA B C   1 
ATOM   6479 O O   . ALA B 1 289 ? -20.345 6.310   43.980  1.00 23.09 ? 289 ALA B O   1 
ATOM   6480 C CB  . ALA B 1 289 ? -22.827 6.611   42.931  1.00 22.56 ? 289 ALA B CB  1 
ATOM   6481 N N   . SER B 1 290 ? -20.933 5.203   45.847  1.00 18.74 ? 290 SER B N   1 
ATOM   6482 C CA  . SER B 1 290 ? -19.532 5.179   46.281  1.00 23.21 ? 290 SER B CA  1 
ATOM   6483 C C   . SER B 1 290 ? -18.758 4.096   45.544  1.00 21.14 ? 290 SER B C   1 
ATOM   6484 O O   . SER B 1 290 ? -19.169 2.926   45.552  1.00 19.31 ? 290 SER B O   1 
ATOM   6485 C CB  . SER B 1 290 ? -19.419 4.920   47.775  1.00 20.86 ? 290 SER B CB  1 
ATOM   6486 O OG  . SER B 1 290 ? -18.046 4.740   48.112  1.00 19.17 ? 290 SER B OG  1 
ATOM   6487 N N   . PRO B 1 291 ? -17.597 4.411   44.969  1.00 18.80 ? 291 PRO B N   1 
ATOM   6488 C CA  . PRO B 1 291 ? -16.807 3.375   44.296  1.00 16.55 ? 291 PRO B CA  1 
ATOM   6489 C C   . PRO B 1 291 ? -15.936 2.534   45.219  1.00 17.77 ? 291 PRO B C   1 
ATOM   6490 O O   . PRO B 1 291 ? -15.177 1.707   44.711  1.00 18.11 ? 291 PRO B O   1 
ATOM   6491 C CB  . PRO B 1 291 ? -15.942 4.196   43.321  1.00 17.75 ? 291 PRO B CB  1 
ATOM   6492 C CG  . PRO B 1 291 ? -15.679 5.457   44.044  1.00 16.99 ? 291 PRO B CG  1 
ATOM   6493 C CD  . PRO B 1 291 ? -16.972 5.742   44.865  1.00 19.34 ? 291 PRO B CD  1 
ATOM   6494 N N   . TYR B 1 292 ? -16.030 2.693   46.544  1.00 17.23 ? 292 TYR B N   1 
ATOM   6495 C CA  . TYR B 1 292 ? -15.133 1.998   47.462  1.00 17.56 ? 292 TYR B CA  1 
ATOM   6496 C C   . TYR B 1 292 ? -15.742 0.726   48.045  1.00 19.92 ? 292 TYR B C   1 
ATOM   6497 O O   . TYR B 1 292 ? -15.142 0.105   48.937  1.00 19.20 ? 292 TYR B O   1 
ATOM   6498 C CB  . TYR B 1 292 ? -14.670 2.973   48.561  1.00 19.48 ? 292 TYR B CB  1 
ATOM   6499 C CG  . TYR B 1 292 ? -14.077 4.222   47.930  1.00 17.58 ? 292 TYR B CG  1 
ATOM   6500 C CD1 . TYR B 1 292 ? -13.155 4.117   46.896  1.00 21.65 ? 292 TYR B CD1 1 
ATOM   6501 C CD2 . TYR B 1 292 ? -14.443 5.498   48.352  1.00 23.97 ? 292 TYR B CD2 1 
ATOM   6502 C CE1 . TYR B 1 292 ? -12.628 5.245   46.283  1.00 21.66 ? 292 TYR B CE1 1 
ATOM   6503 C CE2 . TYR B 1 292 ? -13.903 6.639   47.731  1.00 22.85 ? 292 TYR B CE2 1 
ATOM   6504 C CZ  . TYR B 1 292 ? -12.986 6.495   46.709  1.00 26.12 ? 292 TYR B CZ  1 
ATOM   6505 O OH  . TYR B 1 292 ? -12.446 7.608   46.066  1.00 25.62 ? 292 TYR B OH  1 
ATOM   6506 N N   . LEU B 1 293 ? -16.892 0.312   47.536  1.00 19.96 ? 293 LEU B N   1 
ATOM   6507 C CA  . LEU B 1 293 ? -17.619 -0.868  47.971  1.00 19.37 ? 293 LEU B CA  1 
ATOM   6508 C C   . LEU B 1 293 ? -17.525 -1.960  46.909  1.00 16.74 ? 293 LEU B C   1 
ATOM   6509 O O   . LEU B 1 293 ? -17.328 -1.685  45.727  1.00 17.64 ? 293 LEU B O   1 
ATOM   6510 C CB  . LEU B 1 293 ? -19.092 -0.532  48.187  1.00 18.64 ? 293 LEU B CB  1 
ATOM   6511 C CG  . LEU B 1 293 ? -19.580 0.154   49.464  1.00 30.85 ? 293 LEU B CG  1 
ATOM   6512 C CD1 . LEU B 1 293 ? -18.864 1.462   49.747  1.00 33.25 ? 293 LEU B CD1 1 
ATOM   6513 C CD2 . LEU B 1 293 ? -21.079 0.383   49.362  1.00 34.19 ? 293 LEU B CD2 1 
ATOM   6514 N N   . ARG B 1 294 ? -17.712 -3.208  47.336  1.00 18.67 ? 294 ARG B N   1 
ATOM   6515 C CA  . ARG B 1 294 ? -17.923 -4.299  46.386  1.00 20.68 ? 294 ARG B CA  1 
ATOM   6516 C C   . ARG B 1 294 ? -19.422 -4.385  46.129  1.00 18.59 ? 294 ARG B C   1 
ATOM   6517 O O   . ARG B 1 294 ? -20.205 -4.502  47.079  1.00 22.75 ? 294 ARG B O   1 
ATOM   6518 C CB  . ARG B 1 294 ? -17.390 -5.628  46.929  1.00 22.55 ? 294 ARG B CB  1 
ATOM   6519 C CG  . ARG B 1 294 ? -17.476 -6.798  45.910  1.00 21.63 ? 294 ARG B CG  1 
ATOM   6520 C CD  . ARG B 1 294 ? -16.679 -8.034  46.373  1.00 28.47 ? 294 ARG B CD  1 
ATOM   6521 N NE  . ARG B 1 294 ? -17.072 -8.483  47.700  1.00 30.86 ? 294 ARG B NE  1 
ATOM   6522 C CZ  . ARG B 1 294 ? -16.229 -8.736  48.701  1.00 28.95 ? 294 ARG B CZ  1 
ATOM   6523 N NH1 . ARG B 1 294 ? -14.915 -8.598  48.535  1.00 25.96 ? 294 ARG B NH1 1 
ATOM   6524 N NH2 . ARG B 1 294 ? -16.702 -9.130  49.878  1.00 30.57 ? 294 ARG B NH2 1 
ATOM   6525 N N   . TYR B 1 295 ? -19.834 -4.294  44.869  1.00 16.48 ? 295 TYR B N   1 
ATOM   6526 C CA  . TYR B 1 295 ? -21.250 -4.360  44.525  1.00 17.85 ? 295 TYR B CA  1 
ATOM   6527 C C   . TYR B 1 295 ? -21.614 -5.749  44.011  1.00 21.86 ? 295 TYR B C   1 
ATOM   6528 O O   . TYR B 1 295 ? -20.777 -6.464  43.456  1.00 22.07 ? 295 TYR B O   1 
ATOM   6529 C CB  . TYR B 1 295 ? -21.605 -3.314  43.465  1.00 17.36 ? 295 TYR B CB  1 
ATOM   6530 C CG  . TYR B 1 295 ? -21.610 -1.931  44.042  1.00 19.95 ? 295 TYR B CG  1 
ATOM   6531 C CD1 . TYR B 1 295 ? -20.432 -1.205  44.155  1.00 18.74 ? 295 TYR B CD1 1 
ATOM   6532 C CD2 . TYR B 1 295 ? -22.788 -1.356  44.505  1.00 19.34 ? 295 TYR B CD2 1 
ATOM   6533 C CE1 . TYR B 1 295 ? -20.426 0.078   44.707  1.00 19.33 ? 295 TYR B CE1 1 
ATOM   6534 C CE2 . TYR B 1 295 ? -22.795 -0.066  45.048  1.00 20.74 ? 295 TYR B CE2 1 
ATOM   6535 C CZ  . TYR B 1 295 ? -21.596 0.642   45.143  1.00 21.97 ? 295 TYR B CZ  1 
ATOM   6536 O OH  . TYR B 1 295 ? -21.560 1.914   45.696  1.00 23.27 ? 295 TYR B OH  1 
ATOM   6537 N N   . TYR B 1 296 ? -22.872 -6.131  44.221  1.00 23.88 ? 296 TYR B N   1 
ATOM   6538 C CA  . TYR B 1 296 ? -23.408 -7.397  43.726  1.00 24.46 ? 296 TYR B CA  1 
ATOM   6539 C C   . TYR B 1 296 ? -24.582 -7.089  42.806  1.00 18.80 ? 296 TYR B C   1 
ATOM   6540 O O   . TYR B 1 296 ? -25.618 -6.608  43.267  1.00 23.15 ? 296 TYR B O   1 
ATOM   6541 C CB  . TYR B 1 296 ? -23.850 -8.303  44.872  1.00 25.74 ? 296 TYR B CB  1 
ATOM   6542 C CG  . TYR B 1 296 ? -22.720 -8.656  45.820  1.00 28.66 ? 296 TYR B CG  1 
ATOM   6543 C CD1 . TYR B 1 296 ? -21.616 -9.377  45.377  1.00 33.33 ? 296 TYR B CD1 1 
ATOM   6544 C CD2 . TYR B 1 296 ? -22.754 -8.259  47.149  1.00 36.93 ? 296 TYR B CD2 1 
ATOM   6545 C CE1 . TYR B 1 296 ? -20.578 -9.699  46.237  1.00 34.13 ? 296 TYR B CE1 1 
ATOM   6546 C CE2 . TYR B 1 296 ? -21.725 -8.577  48.016  1.00 39.69 ? 296 TYR B CE2 1 
ATOM   6547 C CZ  . TYR B 1 296 ? -20.637 -9.293  47.550  1.00 31.42 ? 296 TYR B CZ  1 
ATOM   6548 O OH  . TYR B 1 296 ? -19.617 -9.608  48.419  1.00 33.51 ? 296 TYR B OH  1 
ATOM   6549 N N   . PHE B 1 297 ? -24.427 -7.374  41.520  1.00 20.39 ? 297 PHE B N   1 
ATOM   6550 C CA  . PHE B 1 297 ? -25.516 -7.147  40.573  1.00 23.46 ? 297 PHE B CA  1 
ATOM   6551 C C   . PHE B 1 297 ? -26.505 -8.304  40.656  1.00 23.83 ? 297 PHE B C   1 
ATOM   6552 O O   . PHE B 1 297 ? -26.193 -9.426  40.249  1.00 23.84 ? 297 PHE B O   1 
ATOM   6553 C CB  . PHE B 1 297 ? -24.982 -6.992  39.158  1.00 20.18 ? 297 PHE B CB  1 
ATOM   6554 C CG  . PHE B 1 297 ? -26.063 -6.827  38.126  1.00 19.73 ? 297 PHE B CG  1 
ATOM   6555 C CD1 . PHE B 1 297 ? -26.696 -5.607  37.967  1.00 18.75 ? 297 PHE B CD1 1 
ATOM   6556 C CD2 . PHE B 1 297 ? -26.437 -7.884  37.312  1.00 21.52 ? 297 PHE B CD2 1 
ATOM   6557 C CE1 . PHE B 1 297 ? -27.696 -5.448  37.030  1.00 22.37 ? 297 PHE B CE1 1 
ATOM   6558 C CE2 . PHE B 1 297 ? -27.426 -7.727  36.343  1.00 21.30 ? 297 PHE B CE2 1 
ATOM   6559 C CZ  . PHE B 1 297 ? -28.050 -6.506  36.200  1.00 22.49 ? 297 PHE B CZ  1 
ATOM   6560 N N   . ARG B 1 298 ? -27.697 -8.018  41.179  1.00 22.30 ? 298 ARG B N   1 
ATOM   6561 C CA  . ARG B 1 298 ? -28.782 -8.994  41.344  1.00 27.99 ? 298 ARG B CA  1 
ATOM   6562 C C   . ARG B 1 298 ? -28.313 -10.270 42.047  1.00 27.36 ? 298 ARG B C   1 
ATOM   6563 O O   . ARG B 1 298 ? -28.838 -11.360 41.792  1.00 25.29 ? 298 ARG B O   1 
ATOM   6564 C CB  . ARG B 1 298 ? -29.416 -9.330  39.997  1.00 24.96 ? 298 ARG B CB  1 
ATOM   6565 C CG  . ARG B 1 298 ? -29.844 -8.098  39.205  1.00 24.54 ? 298 ARG B CG  1 
ATOM   6566 C CD  . ARG B 1 298 ? -30.679 -8.457  37.979  1.00 29.77 ? 298 ARG B CD  1 
ATOM   6567 N NE  . ARG B 1 298 ? -31.206 -7.255  37.342  1.00 30.93 ? 298 ARG B NE  1 
ATOM   6568 C CZ  . ARG B 1 298 ? -31.524 -7.168  36.051  1.00 38.84 ? 298 ARG B CZ  1 
ATOM   6569 N NH1 . ARG B 1 298 ? -31.348 -8.210  35.246  1.00 39.05 ? 298 ARG B NH1 1 
ATOM   6570 N NH2 . ARG B 1 298 ? -31.995 -6.030  35.557  1.00 36.42 ? 298 ARG B NH2 1 
ATOM   6571 N N   . GLU B 1 299 ? -27.310 -10.143 42.923  1.00 25.17 ? 299 GLU B N   1 
ATOM   6572 C CA  . GLU B 1 299 ? -26.676 -11.281 43.592  1.00 27.40 ? 299 GLU B CA  1 
ATOM   6573 C C   . GLU B 1 299 ? -26.122 -12.315 42.609  1.00 28.03 ? 299 GLU B C   1 
ATOM   6574 O O   . GLU B 1 299 ? -25.871 -13.461 42.989  1.00 33.36 ? 299 GLU B O   1 
ATOM   6575 C CB  . GLU B 1 299 ? -27.634 -11.960 44.578  1.00 34.31 ? 299 GLU B CB  1 
ATOM   6576 C CG  . GLU B 1 299 ? -28.184 -11.035 45.653  1.00 34.15 ? 299 GLU B CG  1 
ATOM   6577 C CD  . GLU B 1 299 ? -27.130 -10.638 46.670  1.00 47.02 ? 299 GLU B CD  1 
ATOM   6578 O OE1 . GLU B 1 299 ? -26.004 -11.187 46.624  1.00 49.03 ? 299 GLU B OE1 1 
ATOM   6579 O OE2 . GLU B 1 299 ? -27.430 -9.775  47.522  1.00 53.96 ? 299 GLU B OE2 1 
ATOM   6580 N N   . LEU B 1 300 ? -25.895 -11.928 41.358  1.00 27.14 ? 300 LEU B N   1 
ATOM   6581 C CA  . LEU B 1 300 ? -25.405 -12.827 40.320  1.00 25.76 ? 300 LEU B CA  1 
ATOM   6582 C C   . LEU B 1 300 ? -23.900 -12.753 40.142  1.00 28.25 ? 300 LEU B C   1 
ATOM   6583 O O   . LEU B 1 300 ? -23.239 -13.784 39.981  1.00 27.66 ? 300 LEU B O   1 
ATOM   6584 C CB  . LEU B 1 300 ? -26.078 -12.505 38.975  1.00 25.75 ? 300 LEU B CB  1 
ATOM   6585 C CG  . LEU B 1 300 ? -27.581 -12.790 38.899  1.00 28.90 ? 300 LEU B CG  1 
ATOM   6586 C CD1 . LEU B 1 300 ? -28.128 -12.337 37.553  1.00 31.72 ? 300 LEU B CD1 1 
ATOM   6587 C CD2 . LEU B 1 300 ? -27.871 -14.273 39.133  1.00 34.47 ? 300 LEU B CD2 1 
ATOM   6588 N N   . ILE B 1 301 ? -23.354 -11.545 40.151  1.00 25.42 ? 301 ILE B N   1 
ATOM   6589 C CA  . ILE B 1 301 ? -21.969 -11.304 39.782  1.00 22.98 ? 301 ILE B CA  1 
ATOM   6590 C C   . ILE B 1 301 ? -21.489 -10.116 40.603  1.00 21.36 ? 301 ILE B C   1 
ATOM   6591 O O   . ILE B 1 301 ? -22.277 -9.225  40.927  1.00 26.01 ? 301 ILE B O   1 
ATOM   6592 C CB  . ILE B 1 301 ? -21.866 -11.087 38.252  1.00 23.37 ? 301 ILE B CB  1 
ATOM   6593 C CG1 . ILE B 1 301 ? -20.425 -10.876 37.784  1.00 23.28 ? 301 ILE B CG1 1 
ATOM   6594 C CG2 . ILE B 1 301 ? -22.777 -9.947  37.788  1.00 23.42 ? 301 ILE B CG2 1 
ATOM   6595 C CD1 . ILE B 1 301 ? -20.323 -10.946 36.276  1.00 24.61 ? 301 ILE B CD1 1 
ATOM   6596 N N   . SER B 1 302 ? -20.210 -10.136 40.999  1.00 22.23 ? 302 SER B N   1 
ATOM   6597 C CA  . SER B 1 302 ? -19.609 -9.024  41.726  1.00 20.21 ? 302 SER B CA  1 
ATOM   6598 C C   . SER B 1 302 ? -19.105 -7.977  40.746  1.00 21.00 ? 302 SER B C   1 
ATOM   6599 O O   . SER B 1 302 ? -18.567 -8.301  39.689  1.00 19.38 ? 302 SER B O   1 
ATOM   6600 C CB  . SER B 1 302 ? -18.452 -9.494  42.607  1.00 23.95 ? 302 SER B CB  1 
ATOM   6601 O OG  . SER B 1 302 ? -18.919 -10.384 43.602  1.00 30.41 ? 302 SER B OG  1 
ATOM   6602 N N   . VAL B 1 303 ? -19.310 -6.712  41.091  1.00 19.34 ? 303 VAL B N   1 
ATOM   6603 C CA  . VAL B 1 303 ? -18.924 -5.605  40.236  1.00 18.64 ? 303 VAL B CA  1 
ATOM   6604 C C   . VAL B 1 303 ? -18.177 -4.597  41.089  1.00 18.05 ? 303 VAL B C   1 
ATOM   6605 O O   . VAL B 1 303 ? -18.682 -4.166  42.130  1.00 18.50 ? 303 VAL B O   1 
ATOM   6606 C CB  . VAL B 1 303 ? -20.142 -4.949  39.559  1.00 16.94 ? 303 VAL B CB  1 
ATOM   6607 C CG1 . VAL B 1 303 ? -19.682 -3.795  38.673  1.00 18.37 ? 303 VAL B CG1 1 
ATOM   6608 C CG2 . VAL B 1 303 ? -20.936 -5.972  38.726  1.00 21.99 ? 303 VAL B CG2 1 
ATOM   6609 N N   . PHE B 1 304 ? -16.972 -4.244  40.667  1.00 18.14 ? 304 PHE B N   1 
ATOM   6610 C CA  . PHE B 1 304 ? -16.261 -3.112  41.229  1.00 14.56 ? 304 PHE B CA  1 
ATOM   6611 C C   . PHE B 1 304 ? -16.304 -1.969  40.225  1.00 15.00 ? 304 PHE B C   1 
ATOM   6612 O O   . PHE B 1 304 ? -16.329 -2.179  39.006  1.00 18.32 ? 304 PHE B O   1 
ATOM   6613 C CB  . PHE B 1 304 ? -14.797 -3.468  41.541  1.00 15.65 ? 304 PHE B CB  1 
ATOM   6614 C CG  . PHE B 1 304 ? -14.617 -4.248  42.812  1.00 20.05 ? 304 PHE B CG  1 
ATOM   6615 C CD1 . PHE B 1 304 ? -14.655 -3.605  44.036  1.00 18.42 ? 304 PHE B CD1 1 
ATOM   6616 C CD2 . PHE B 1 304 ? -14.383 -5.615  42.784  1.00 20.92 ? 304 PHE B CD2 1 
ATOM   6617 C CE1 . PHE B 1 304 ? -14.451 -4.307  45.219  1.00 23.88 ? 304 PHE B CE1 1 
ATOM   6618 C CE2 . PHE B 1 304 ? -14.193 -6.325  43.964  1.00 23.32 ? 304 PHE B CE2 1 
ATOM   6619 C CZ  . PHE B 1 304 ? -14.235 -5.667  45.180  1.00 23.40 ? 304 PHE B CZ  1 
ATOM   6620 N N   . PHE B 1 305 ? -16.359 -0.753  40.738  1.00 15.95 ? 305 PHE B N   1 
ATOM   6621 C CA  . PHE B 1 305 ? -16.353 0.439   39.903  1.00 18.25 ? 305 PHE B CA  1 
ATOM   6622 C C   . PHE B 1 305 ? -15.045 1.174   40.157  1.00 19.25 ? 305 PHE B C   1 
ATOM   6623 O O   . PHE B 1 305 ? -14.710 1.474   41.307  1.00 16.84 ? 305 PHE B O   1 
ATOM   6624 C CB  . PHE B 1 305 ? -17.574 1.311   40.215  1.00 18.48 ? 305 PHE B CB  1 
ATOM   6625 C CG  . PHE B 1 305 ? -18.900 0.623   39.926  1.00 16.90 ? 305 PHE B CG  1 
ATOM   6626 C CD1 . PHE B 1 305 ? -19.453 -0.257  40.858  1.00 18.15 ? 305 PHE B CD1 1 
ATOM   6627 C CD2 . PHE B 1 305 ? -19.577 0.845   38.724  1.00 19.04 ? 305 PHE B CD2 1 
ATOM   6628 C CE1 . PHE B 1 305 ? -20.645 -0.909  40.603  1.00 22.07 ? 305 PHE B CE1 1 
ATOM   6629 C CE2 . PHE B 1 305 ? -20.778 0.217   38.475  1.00 22.04 ? 305 PHE B CE2 1 
ATOM   6630 C CZ  . PHE B 1 305 ? -21.312 -0.664  39.404  1.00 21.59 ? 305 PHE B CZ  1 
ATOM   6631 N N   . ARG B 1 306 ? -14.302 1.442   39.093  1.00 18.21 ? 306 ARG B N   1 
ATOM   6632 C CA  . ARG B 1 306 ? -12.996 2.062   39.262  1.00 16.05 ? 306 ARG B CA  1 
ATOM   6633 C C   . ARG B 1 306 ? -13.149 3.491   39.755  1.00 18.49 ? 306 ARG B C   1 
ATOM   6634 O O   . ARG B 1 306 ? -14.143 4.172   39.476  1.00 19.12 ? 306 ARG B O   1 
ATOM   6635 C CB  . ARG B 1 306 ? -12.212 2.071   37.951  1.00 15.88 ? 306 ARG B CB  1 
ATOM   6636 C CG  . ARG B 1 306 ? -12.773 3.068   36.927  1.00 15.97 ? 306 ARG B CG  1 
ATOM   6637 C CD  . ARG B 1 306 ? -11.935 3.132   35.653  1.00 16.28 ? 306 ARG B CD  1 
ATOM   6638 N NE  . ARG B 1 306 ? -12.452 4.207   34.803  1.00 14.90 ? 306 ARG B NE  1 
ATOM   6639 C CZ  . ARG B 1 306 ? -11.756 4.870   33.903  1.00 19.84 ? 306 ARG B CZ  1 
ATOM   6640 N NH1 . ARG B 1 306 ? -10.481 4.568   33.669  1.00 15.70 ? 306 ARG B NH1 1 
ATOM   6641 N NH2 . ARG B 1 306 ? -12.356 5.831   33.214  1.00 19.10 ? 306 ARG B NH2 1 
ATOM   6642 N N   . ASP B 1 307 ? -12.164 3.930   40.519  1.00 13.70 ? 307 ASP B N   1 
ATOM   6643 C CA  . ASP B 1 307 ? -12.049 5.332   40.904  1.00 12.96 ? 307 ASP B CA  1 
ATOM   6644 C C   . ASP B 1 307 ? -11.593 6.091   39.666  1.00 17.13 ? 307 ASP B C   1 
ATOM   6645 O O   . ASP B 1 307 ? -10.423 6.036   39.266  1.00 16.72 ? 307 ASP B O   1 
ATOM   6646 C CB  . ASP B 1 307 ? -11.061 5.485   42.061  1.00 14.89 ? 307 ASP B CB  1 
ATOM   6647 C CG  . ASP B 1 307 ? -10.977 6.906   42.585  1.00 23.65 ? 307 ASP B CG  1 
ATOM   6648 O OD1 . ASP B 1 307 ? -10.925 7.850   41.774  1.00 23.80 ? 307 ASP B OD1 1 
ATOM   6649 O OD2 . ASP B 1 307 ? -10.932 7.088   43.821  1.00 25.28 ? 307 ASP B OD2 1 
ATOM   6650 N N   . LYS B 1 308 ? -12.527 6.809   39.044  1.00 18.79 ? 308 LYS B N   1 
ATOM   6651 C CA  . LYS B 1 308 ? -12.228 7.447   37.773  1.00 16.76 ? 308 LYS B CA  1 
ATOM   6652 C C   . LYS B 1 308 ? -11.193 8.553   37.942  1.00 18.53 ? 308 LYS B C   1 
ATOM   6653 O O   . LYS B 1 308 ? -10.301 8.706   37.100  1.00 20.18 ? 308 LYS B O   1 
ATOM   6654 C CB  . LYS B 1 308 ? -13.526 7.976   37.157  1.00 20.26 ? 308 LYS B CB  1 
ATOM   6655 C CG  . LYS B 1 308 ? -13.349 8.846   35.939  1.00 23.27 ? 308 LYS B CG  1 
ATOM   6656 C CD  . LYS B 1 308 ? -14.609 9.690   35.759  1.00 28.45 ? 308 LYS B CD  1 
ATOM   6657 C CE  . LYS B 1 308 ? -14.789 10.229  34.350  1.00 29.45 ? 308 LYS B CE  1 
ATOM   6658 N NZ  . LYS B 1 308 ? -13.611 10.044  33.464  1.00 25.52 ? 308 LYS B NZ  1 
ATOM   6659 N N   . THR B 1 309 ? -11.256 9.311   39.039  1.00 17.25 ? 309 THR B N   1 
ATOM   6660 C CA  . THR B 1 309 ? -10.284 10.379  39.213  1.00 20.86 ? 309 THR B CA  1 
ATOM   6661 C C   . THR B 1 309 ? -8.862  9.826   39.261  1.00 20.05 ? 309 THR B C   1 
ATOM   6662 O O   . THR B 1 309 ? -7.969  10.333  38.570  1.00 18.02 ? 309 THR B O   1 
ATOM   6663 C CB  . THR B 1 309 ? -10.610 11.175  40.476  1.00 26.34 ? 309 THR B CB  1 
ATOM   6664 O OG1 . THR B 1 309 ? -11.913 11.738  40.316  1.00 26.92 ? 309 THR B OG1 1 
ATOM   6665 C CG2 . THR B 1 309 ? -9.607  12.290  40.678  1.00 26.26 ? 309 THR B CG2 1 
ATOM   6666 N N   . LEU B 1 310 ? -8.627  8.803   40.092  1.00 18.03 ? 310 LEU B N   1 
ATOM   6667 C CA  . LEU B 1 310 ? -7.278  8.241   40.201  1.00 17.42 ? 310 LEU B CA  1 
ATOM   6668 C C   . LEU B 1 310 ? -6.846  7.597   38.896  1.00 16.07 ? 310 LEU B C   1 
ATOM   6669 O O   . LEU B 1 310 ? -5.676  7.708   38.493  1.00 18.73 ? 310 LEU B O   1 
ATOM   6670 C CB  . LEU B 1 310 ? -7.218  7.201   41.316  1.00 17.79 ? 310 LEU B CB  1 
ATOM   6671 C CG  . LEU B 1 310 ? -7.443  7.730   42.728  1.00 15.90 ? 310 LEU B CG  1 
ATOM   6672 C CD1 . LEU B 1 310 ? -7.337  6.594   43.726  1.00 17.77 ? 310 LEU B CD1 1 
ATOM   6673 C CD2 . LEU B 1 310 ? -6.474  8.869   43.119  1.00 23.67 ? 310 LEU B CD2 1 
ATOM   6674 N N   . SER B 1 311 ? -7.773  6.890   38.240  1.00 16.53 ? 311 SER B N   1 
ATOM   6675 C CA  . SER B 1 311 ? -7.459  6.227   36.979  1.00 20.02 ? 311 SER B CA  1 
ATOM   6676 C C   . SER B 1 311 ? -7.072  7.227   35.902  1.00 15.53 ? 311 SER B C   1 
ATOM   6677 O O   . SER B 1 311 ? -6.103  7.012   35.155  1.00 17.14 ? 311 SER B O   1 
ATOM   6678 C CB  . SER B 1 311 ? -8.648  5.380   36.529  1.00 17.10 ? 311 SER B CB  1 
ATOM   6679 O OG  . SER B 1 311 ? -8.941  4.415   37.514  1.00 16.60 ? 311 SER B OG  1 
ATOM   6680 N N   . ASP B 1 312 ? -7.786  8.356   35.836  1.00 16.21 ? 312 ASP B N   1 
ATOM   6681 C CA  . ASP B 1 312 ? -7.494  9.375   34.837  1.00 15.70 ? 312 ASP B CA  1 
ATOM   6682 C C   . ASP B 1 312 ? -6.279  10.208  35.206  1.00 21.53 ? 312 ASP B C   1 
ATOM   6683 O O   . ASP B 1 312 ? -5.637  10.774  34.313  1.00 19.43 ? 312 ASP B O   1 
ATOM   6684 C CB  . ASP B 1 312 ? -8.688  10.316  34.654  1.00 25.33 ? 312 ASP B CB  1 
ATOM   6685 C CG  . ASP B 1 312 ? -9.809  9.704   33.831  1.00 27.77 ? 312 ASP B CG  1 
ATOM   6686 O OD1 . ASP B 1 312 ? -9.587  8.700   33.126  1.00 26.26 ? 312 ASP B OD1 1 
ATOM   6687 O OD2 . ASP B 1 312 ? -10.931 10.237  33.915  1.00 29.50 ? 312 ASP B OD2 1 
ATOM   6688 N N   . LEU B 1 313 ? -5.954  10.323  36.506  1.00 15.45 ? 313 LEU B N   1 
ATOM   6689 C CA  . LEU B 1 313 ? -4.707  10.995  36.855  1.00 21.69 ? 313 LEU B CA  1 
ATOM   6690 C C   . LEU B 1 313 ? -3.514  10.279  36.231  1.00 13.78 ? 313 LEU B C   1 
ATOM   6691 O O   . LEU B 1 313 ? -2.673  10.910  35.592  1.00 18.59 ? 313 LEU B O   1 
ATOM   6692 C CB  . LEU B 1 313 ? -4.563  11.091  38.378  1.00 20.42 ? 313 LEU B CB  1 
ATOM   6693 C CG  . LEU B 1 313 ? -5.464  12.140  39.038  1.00 24.20 ? 313 LEU B CG  1 
ATOM   6694 C CD1 . LEU B 1 313 ? -5.365  12.000  40.522  1.00 25.83 ? 313 LEU B CD1 1 
ATOM   6695 C CD2 . LEU B 1 313 ? -5.066  13.541  38.611  1.00 21.46 ? 313 LEU B CD2 1 
ATOM   6696 N N   . ILE B 1 314 ? -3.445  8.942   36.376  1.00 14.79 ? 314 ILE B N   1 
ATOM   6697 C CA  . ILE B 1 314 ? -2.346  8.193   35.775  1.00 14.20 ? 314 ILE B CA  1 
ATOM   6698 C C   . ILE B 1 314 ? -2.450  8.220   34.263  1.00 14.41 ? 314 ILE B C   1 
ATOM   6699 O O   . ILE B 1 314 ? -1.452  8.389   33.555  1.00 16.34 ? 314 ILE B O   1 
ATOM   6700 C CB  . ILE B 1 314 ? -2.335  6.751   36.320  1.00 12.78 ? 314 ILE B CB  1 
ATOM   6701 C CG1 . ILE B 1 314 ? -2.150  6.772   37.846  1.00 13.57 ? 314 ILE B CG1 1 
ATOM   6702 C CG2 . ILE B 1 314 ? -1.253  5.886   35.611  1.00 15.26 ? 314 ILE B CG2 1 
ATOM   6703 C CD1 . ILE B 1 314 ? -2.069  5.371   38.485  1.00 19.28 ? 314 ILE B CD1 1 
ATOM   6704 N N   . GLY B 1 315 ? -3.659  8.064   33.741  1.00 16.01 ? 315 GLY B N   1 
ATOM   6705 C CA  . GLY B 1 315 ? -3.807  7.889   32.311  1.00 16.72 ? 315 GLY B CA  1 
ATOM   6706 C C   . GLY B 1 315 ? -3.585  9.161   31.526  1.00 22.35 ? 315 GLY B C   1 
ATOM   6707 O O   . GLY B 1 315 ? -3.123  9.108   30.380  1.00 23.95 ? 315 GLY B O   1 
ATOM   6708 N N   . PHE B 1 316 ? -3.912  10.322  32.115  1.00 19.56 ? 316 PHE B N   1 
ATOM   6709 C CA  . PHE B 1 316 ? -3.905  11.577  31.375  1.00 19.50 ? 316 PHE B CA  1 
ATOM   6710 C C   . PHE B 1 316 ? -3.195  12.745  32.041  1.00 22.42 ? 316 PHE B C   1 
ATOM   6711 O O   . PHE B 1 316 ? -2.733  13.636  31.322  1.00 23.19 ? 316 PHE B O   1 
ATOM   6712 C CB  . PHE B 1 316 ? -5.341  12.007  31.065  1.00 19.95 ? 316 PHE B CB  1 
ATOM   6713 C CG  . PHE B 1 316 ? -6.072  11.026  30.214  1.00 19.51 ? 316 PHE B CG  1 
ATOM   6714 C CD1 . PHE B 1 316 ? -5.894  11.023  28.844  1.00 25.03 ? 316 PHE B CD1 1 
ATOM   6715 C CD2 . PHE B 1 316 ? -6.916  10.097  30.781  1.00 24.34 ? 316 PHE B CD2 1 
ATOM   6716 C CE1 . PHE B 1 316 ? -6.569  10.113  28.051  1.00 30.35 ? 316 PHE B CE1 1 
ATOM   6717 C CE2 . PHE B 1 316 ? -7.595  9.184   29.995  1.00 29.59 ? 316 PHE B CE2 1 
ATOM   6718 C CZ  . PHE B 1 316 ? -7.412  9.190   28.630  1.00 29.10 ? 316 PHE B CZ  1 
ATOM   6719 N N   . SER B 1 317 ? -3.060  12.775  33.363  1.00 18.87 ? 317 SER B N   1 
ATOM   6720 C CA  . SER B 1 317 ? -2.494  13.949  34.010  1.00 18.80 ? 317 SER B CA  1 
ATOM   6721 C C   . SER B 1 317 ? -0.999  13.846  34.294  1.00 20.06 ? 317 SER B C   1 
ATOM   6722 O O   . SER B 1 317 ? -0.232  14.745  33.954  1.00 22.65 ? 317 SER B O   1 
ATOM   6723 C CB  . SER B 1 317 ? -3.237  14.221  35.316  1.00 25.74 ? 317 SER B CB  1 
ATOM   6724 O OG  . SER B 1 317 ? -2.761  15.434  35.857  1.00 30.04 ? 317 SER B OG  1 
ATOM   6725 N N   . TYR B 1 318 ? -0.559  12.761  34.936  1.00 15.27 ? 318 TYR B N   1 
ATOM   6726 C CA  . TYR B 1 318 ? 0.774   12.723  35.523  1.00 15.44 ? 318 TYR B CA  1 
ATOM   6727 C C   . TYR B 1 318 ? 1.900   12.698  34.492  1.00 16.41 ? 318 TYR B C   1 
ATOM   6728 O O   . TYR B 1 318 ? 3.055   12.902  34.874  1.00 20.62 ? 318 TYR B O   1 
ATOM   6729 C CB  . TYR B 1 318 ? 0.890   11.509  36.445  1.00 14.66 ? 318 TYR B CB  1 
ATOM   6730 C CG  . TYR B 1 318 ? 0.133   11.633  37.747  1.00 14.74 ? 318 TYR B CG  1 
ATOM   6731 C CD1 . TYR B 1 318 ? -0.207  12.885  38.289  1.00 15.64 ? 318 TYR B CD1 1 
ATOM   6732 C CD2 . TYR B 1 318 ? -0.234  10.497  38.456  1.00 19.01 ? 318 TYR B CD2 1 
ATOM   6733 C CE1 . TYR B 1 318 ? -0.899  12.967  39.518  1.00 19.69 ? 318 TYR B CE1 1 
ATOM   6734 C CE2 . TYR B 1 318 ? -0.927  10.582  39.660  1.00 18.76 ? 318 TYR B CE2 1 
ATOM   6735 C CZ  . TYR B 1 318 ? -1.248  11.792  40.182  1.00 21.65 ? 318 TYR B CZ  1 
ATOM   6736 O OH  . TYR B 1 318 ? -1.924  11.802  41.382  1.00 21.41 ? 318 TYR B OH  1 
ATOM   6737 N N   . HIS B 1 319 ? 1.618   12.443  33.208  1.00 18.27 ? 319 HIS B N   1 
ATOM   6738 C CA  . HIS B 1 319 ? 2.688   12.616  32.229  1.00 21.78 ? 319 HIS B CA  1 
ATOM   6739 C C   . HIS B 1 319 ? 3.228   14.041  32.279  1.00 27.64 ? 319 HIS B C   1 
ATOM   6740 O O   . HIS B 1 319 ? 4.403   14.272  31.997  1.00 32.50 ? 319 HIS B O   1 
ATOM   6741 C CB  . HIS B 1 319 ? 2.209   12.299  30.815  1.00 22.37 ? 319 HIS B CB  1 
ATOM   6742 C CG  . HIS B 1 319 ? 1.341   13.361  30.232  1.00 25.05 ? 319 HIS B CG  1 
ATOM   6743 N ND1 . HIS B 1 319 ? 1.850   14.434  29.528  1.00 30.53 ? 319 HIS B ND1 1 
ATOM   6744 C CD2 . HIS B 1 319 ? 0.001   13.537  30.271  1.00 28.86 ? 319 HIS B CD2 1 
ATOM   6745 C CE1 . HIS B 1 319 ? 0.858   15.216  29.147  1.00 30.40 ? 319 HIS B CE1 1 
ATOM   6746 N NE2 . HIS B 1 319 ? -0.274  14.694  29.580  1.00 35.69 ? 319 HIS B NE2 1 
ATOM   6747 N N   . ALA B 1 320 ? 2.390   14.993  32.665  1.00 32.99 ? 320 ALA B N   1 
ATOM   6748 C CA  . ALA B 1 320 ? 2.780   16.394  32.707  1.00 36.76 ? 320 ALA B CA  1 
ATOM   6749 C C   . ALA B 1 320 ? 3.571   16.760  33.961  1.00 41.50 ? 320 ALA B C   1 
ATOM   6750 O O   . ALA B 1 320 ? 4.054   17.894  34.049  1.00 44.87 ? 320 ALA B O   1 
ATOM   6751 C CB  . ALA B 1 320 ? 1.529   17.268  32.594  1.00 40.84 ? 320 ALA B CB  1 
ATOM   6752 N N   . TRP B 1 321 ? 3.754   15.832  34.902  1.00 29.95 ? 321 TRP B N   1 
ATOM   6753 C CA  . TRP B 1 321 ? 4.362   16.117  36.196  1.00 27.34 ? 321 TRP B CA  1 
ATOM   6754 C C   . TRP B 1 321 ? 5.771   15.559  36.280  1.00 29.72 ? 321 TRP B C   1 
ATOM   6755 O O   . TRP B 1 321 ? 6.143   14.634  35.556  1.00 36.80 ? 321 TRP B O   1 
ATOM   6756 C CB  . TRP B 1 321 ? 3.569   15.498  37.352  1.00 23.05 ? 321 TRP B CB  1 
ATOM   6757 C CG  . TRP B 1 321 ? 2.162   15.943  37.552  1.00 22.36 ? 321 TRP B CG  1 
ATOM   6758 C CD1 . TRP B 1 321 ? 1.181   16.064  36.608  1.00 20.74 ? 321 TRP B CD1 1 
ATOM   6759 C CD2 . TRP B 1 321 ? 1.560   16.286  38.805  1.00 19.27 ? 321 TRP B CD2 1 
ATOM   6760 N NE1 . TRP B 1 321 ? 0.004   16.475  37.194  1.00 21.89 ? 321 TRP B NE1 1 
ATOM   6761 C CE2 . TRP B 1 321 ? 0.213   16.625  38.542  1.00 20.68 ? 321 TRP B CE2 1 
ATOM   6762 C CE3 . TRP B 1 321 ? 2.036   16.364  40.121  1.00 19.11 ? 321 TRP B CE3 1 
ATOM   6763 C CZ2 . TRP B 1 321 ? -0.663  17.012  39.543  1.00 26.20 ? 321 TRP B CZ2 1 
ATOM   6764 C CZ3 . TRP B 1 321 ? 1.164   16.769  41.117  1.00 19.75 ? 321 TRP B CZ3 1 
ATOM   6765 C CH2 . TRP B 1 321 ? -0.173  17.081  40.820  1.00 24.82 ? 321 TRP B CH2 1 
ATOM   6766 N N   . ASN B 1 322 ? 6.531   16.096  37.225  1.00 25.38 ? 322 ASN B N   1 
ATOM   6767 C CA  . ASN B 1 322 ? 7.730   15.439  37.711  1.00 28.77 ? 322 ASN B CA  1 
ATOM   6768 C C   . ASN B 1 322 ? 7.315   14.180  38.463  1.00 31.26 ? 322 ASN B C   1 
ATOM   6769 O O   . ASN B 1 322 ? 6.251   14.141  39.089  1.00 33.22 ? 322 ASN B O   1 
ATOM   6770 C CB  . ASN B 1 322 ? 8.519   16.381  38.619  1.00 32.78 ? 322 ASN B CB  1 
ATOM   6771 C CG  . ASN B 1 322 ? 9.657   15.692  39.349  1.00 44.64 ? 322 ASN B CG  1 
ATOM   6772 O OD1 . ASN B 1 322 ? 10.570  15.147  38.725  1.00 54.45 ? 322 ASN B OD1 1 
ATOM   6773 N ND2 . ASN B 1 322 ? 9.618   15.727  40.678  1.00 41.68 ? 322 ASN B ND2 1 
ATOM   6774 N N   . ALA B 1 323 ? 8.154   13.139  38.379  1.00 28.02 ? 323 ALA B N   1 
ATOM   6775 C CA  . ALA B 1 323 ? 7.750   11.811  38.848  1.00 26.66 ? 323 ALA B CA  1 
ATOM   6776 C C   . ALA B 1 323 ? 7.459   11.803  40.344  1.00 24.63 ? 323 ALA B C   1 
ATOM   6777 O O   . ALA B 1 323 ? 6.418   11.297  40.776  1.00 22.54 ? 323 ALA B O   1 
ATOM   6778 C CB  . ALA B 1 323 ? 8.822   10.780  38.512  1.00 22.74 ? 323 ALA B CB  1 
ATOM   6779 N N   . GLU B 1 324 ? 8.371   12.355  41.159  1.00 23.91 ? 324 GLU B N   1 
ATOM   6780 C CA  . GLU B 1 324 ? 8.184   12.241  42.600  1.00 27.13 ? 324 GLU B CA  1 
ATOM   6781 C C   . GLU B 1 324 ? 7.040   13.120  43.068  1.00 27.20 ? 324 GLU B C   1 
ATOM   6782 O O   . GLU B 1 324 ? 6.282   12.733  43.962  1.00 30.63 ? 324 GLU B O   1 
ATOM   6783 C CB  . GLU B 1 324 ? 9.473   12.582  43.348  1.00 41.64 ? 324 GLU B CB  1 
ATOM   6784 C CG  . GLU B 1 324 ? 10.677  11.836  42.821  1.00 56.08 ? 324 GLU B CG  1 
ATOM   6785 C CD  . GLU B 1 324 ? 11.714  11.511  43.887  1.00 73.22 ? 324 GLU B CD  1 
ATOM   6786 O OE1 . GLU B 1 324 ? 11.444  11.716  45.093  1.00 79.44 ? 324 GLU B OE1 1 
ATOM   6787 O OE2 . GLU B 1 324 ? 12.804  11.029  43.513  1.00 78.96 ? 324 GLU B OE2 1 
ATOM   6788 N N   . ASP B 1 325 ? 6.869   14.282  42.442  1.00 24.60 ? 325 ASP B N   1 
ATOM   6789 C CA  . ASP B 1 325 ? 5.711   15.123  42.712  1.00 25.41 ? 325 ASP B CA  1 
ATOM   6790 C C   . ASP B 1 325 ? 4.406   14.403  42.399  1.00 23.54 ? 325 ASP B C   1 
ATOM   6791 O O   . ASP B 1 325 ? 3.416   14.553  43.124  1.00 22.27 ? 325 ASP B O   1 
ATOM   6792 C CB  . ASP B 1 325 ? 5.815   16.402  41.887  1.00 30.96 ? 325 ASP B CB  1 
ATOM   6793 C CG  . ASP B 1 325 ? 5.585   17.620  42.703  1.00 41.95 ? 325 ASP B CG  1 
ATOM   6794 O OD1 . ASP B 1 325 ? 5.519   17.483  43.943  1.00 42.74 ? 325 ASP B OD1 1 
ATOM   6795 O OD2 . ASP B 1 325 ? 5.450   18.712  42.116  1.00 46.36 ? 325 ASP B OD2 1 
ATOM   6796 N N   . ALA B 1 326 ? 4.371   13.636  41.303  1.00 21.03 ? 326 ALA B N   1 
ATOM   6797 C CA  . ALA B 1 326 ? 3.139   12.943  40.957  1.00 19.05 ? 326 ALA B CA  1 
ATOM   6798 C C   . ALA B 1 326 ? 2.837   11.848  41.970  1.00 22.18 ? 326 ALA B C   1 
ATOM   6799 O O   . ALA B 1 326 ? 1.678   11.644  42.360  1.00 18.24 ? 326 ALA B O   1 
ATOM   6800 C CB  . ALA B 1 326 ? 3.243   12.345  39.551  1.00 17.33 ? 326 ALA B CB  1 
ATOM   6801 N N   . VAL B 1 327 ? 3.879   11.149  42.417  1.00 20.23 ? 327 VAL B N   1 
ATOM   6802 C CA  . VAL B 1 327 ? 3.700   10.089  43.408  1.00 19.53 ? 327 VAL B CA  1 
ATOM   6803 C C   . VAL B 1 327 ? 3.167   10.667  44.716  1.00 25.44 ? 327 VAL B C   1 
ATOM   6804 O O   . VAL B 1 327 ? 2.240   10.115  45.319  1.00 23.37 ? 327 VAL B O   1 
ATOM   6805 C CB  . VAL B 1 327 ? 5.023   9.321   43.606  1.00 16.72 ? 327 VAL B CB  1 
ATOM   6806 C CG1 . VAL B 1 327 ? 4.910   8.323   44.776  1.00 20.78 ? 327 VAL B CG1 1 
ATOM   6807 C CG2 . VAL B 1 327 ? 5.408   8.568   42.312  1.00 16.11 ? 327 VAL B CG2 1 
ATOM   6808 N N   . ARG B 1 328 ? 3.718   11.804  45.161  1.00 19.67 ? 328 ARG B N   1 
ATOM   6809 C CA  . ARG B 1 328 ? 3.202   12.455  46.367  1.00 19.95 ? 328 ARG B CA  1 
ATOM   6810 C C   . ARG B 1 328 ? 1.723   12.784  46.232  1.00 22.16 ? 328 ARG B C   1 
ATOM   6811 O O   . ARG B 1 328 ? 0.943   12.557  47.162  1.00 27.24 ? 328 ARG B O   1 
ATOM   6812 C CB  . ARG B 1 328 ? 3.981   13.732  46.667  1.00 22.35 ? 328 ARG B CB  1 
ATOM   6813 C CG  . ARG B 1 328 ? 5.430   13.527  47.024  1.00 26.97 ? 328 ARG B CG  1 
ATOM   6814 C CD  . ARG B 1 328 ? 6.067   14.842  47.534  1.00 30.81 ? 328 ARG B CD  1 
ATOM   6815 N NE  . ARG B 1 328 ? 7.510   14.785  47.380  1.00 36.02 ? 328 ARG B NE  1 
ATOM   6816 C CZ  . ARG B 1 328 ? 8.212   15.462  46.473  1.00 40.46 ? 328 ARG B CZ  1 
ATOM   6817 N NH1 . ARG B 1 328 ? 7.623   16.320  45.651  1.00 32.66 ? 328 ARG B NH1 1 
ATOM   6818 N NH2 . ARG B 1 328 ? 9.526   15.298  46.411  1.00 52.28 ? 328 ARG B NH2 1 
ATOM   6819 N N   . ASP B 1 329 ? 1.326   13.364  45.086  1.00 17.64 ? 329 ASP B N   1 
ATOM   6820 C CA  . ASP B 1 329 ? -0.071  13.684  44.851  1.00 17.79 ? 329 ASP B CA  1 
ATOM   6821 C C   . ASP B 1 329 ? -0.958  12.457  44.978  1.00 20.98 ? 329 ASP B C   1 
ATOM   6822 O O   . ASP B 1 329 ? -2.005  12.503  45.626  1.00 22.22 ? 329 ASP B O   1 
ATOM   6823 C CB  . ASP B 1 329 ? -0.247  14.307  43.462  1.00 19.39 ? 329 ASP B CB  1 
ATOM   6824 C CG  . ASP B 1 329 ? -1.643  14.847  43.241  1.00 29.93 ? 329 ASP B CG  1 
ATOM   6825 O OD1 . ASP B 1 329 ? -1.937  15.952  43.754  1.00 29.43 ? 329 ASP B OD1 1 
ATOM   6826 O OD2 . ASP B 1 329 ? -2.447  14.180  42.553  1.00 25.58 ? 329 ASP B OD2 1 
ATOM   6827 N N   . PHE B 1 330 ? -0.573  11.362  44.316  1.00 21.13 ? 330 PHE B N   1 
ATOM   6828 C CA  . PHE B 1 330 ? -1.374  10.143  44.326  1.00 22.41 ? 330 PHE B CA  1 
ATOM   6829 C C   . PHE B 1 330 ? -1.480  9.562   45.734  1.00 21.47 ? 330 PHE B C   1 
ATOM   6830 O O   . PHE B 1 330 ? -2.568  9.170   46.177  1.00 19.76 ? 330 PHE B O   1 
ATOM   6831 C CB  . PHE B 1 330 ? -0.732  9.143   43.378  1.00 16.09 ? 330 PHE B CB  1 
ATOM   6832 C CG  . PHE B 1 330 ? -1.529  7.909   43.130  1.00 17.08 ? 330 PHE B CG  1 
ATOM   6833 C CD1 . PHE B 1 330 ? -2.537  7.907   42.180  1.00 17.25 ? 330 PHE B CD1 1 
ATOM   6834 C CD2 . PHE B 1 330 ? -1.212  6.716   43.775  1.00 20.76 ? 330 PHE B CD2 1 
ATOM   6835 C CE1 . PHE B 1 330 ? -3.248  6.730   41.900  1.00 17.68 ? 330 PHE B CE1 1 
ATOM   6836 C CE2 . PHE B 1 330 ? -1.923  5.535   43.501  1.00 19.70 ? 330 PHE B CE2 1 
ATOM   6837 C CZ  . PHE B 1 330 ? -2.938  5.541   42.580  1.00 16.71 ? 330 PHE B CZ  1 
ATOM   6838 N N   . ILE B 1 331 ? -0.354  9.485   46.447  1.00 16.11 ? 331 ILE B N   1 
ATOM   6839 C CA  . ILE B 1 331 ? -0.380  8.966   47.815  1.00 20.29 ? 331 ILE B CA  1 
ATOM   6840 C C   . ILE B 1 331 ? -1.247  9.846   48.703  1.00 19.77 ? 331 ILE B C   1 
ATOM   6841 O O   . ILE B 1 331 ? -2.018  9.353   49.536  1.00 21.94 ? 331 ILE B O   1 
ATOM   6842 C CB  . ILE B 1 331 ? 1.048   8.851   48.383  1.00 23.99 ? 331 ILE B CB  1 
ATOM   6843 C CG1 . ILE B 1 331 ? 1.854   7.825   47.586  1.00 24.37 ? 331 ILE B CG1 1 
ATOM   6844 C CG2 . ILE B 1 331 ? 1.023   8.526   49.902  1.00 24.95 ? 331 ILE B CG2 1 
ATOM   6845 C CD1 . ILE B 1 331 ? 1.263   6.424   47.584  1.00 24.09 ? 331 ILE B CD1 1 
ATOM   6846 N N   . GLY B 1 332 ? -1.127  11.165  48.551  1.00 18.18 ? 332 GLY B N   1 
ATOM   6847 C CA  . GLY B 1 332 ? -1.943  12.064  49.347  1.00 19.85 ? 332 GLY B CA  1 
ATOM   6848 C C   . GLY B 1 332 ? -3.426  11.916  49.070  1.00 21.04 ? 332 GLY B C   1 
ATOM   6849 O O   . GLY B 1 332 ? -4.258  12.087  49.969  1.00 22.88 ? 332 GLY B O   1 
ATOM   6850 N N   . ARG B 1 333 ? -3.786  11.600  47.831  1.00 20.55 ? 333 ARG B N   1 
ATOM   6851 C CA  . ARG B 1 333 ? -5.194  11.364  47.531  1.00 19.76 ? 333 ARG B CA  1 
ATOM   6852 C C   . ARG B 1 333 ? -5.675  10.065  48.162  1.00 22.60 ? 333 ARG B C   1 
ATOM   6853 O O   . ARG B 1 333 ? -6.798  9.987   48.667  1.00 21.58 ? 333 ARG B O   1 
ATOM   6854 C CB  . ARG B 1 333 ? -5.397  11.364  46.016  1.00 23.23 ? 333 ARG B CB  1 
ATOM   6855 C CG  . ARG B 1 333 ? -5.128  12.744  45.386  1.00 20.50 ? 333 ARG B CG  1 
ATOM   6856 C CD  . ARG B 1 333 ? -5.257  12.680  43.885  1.00 23.00 ? 333 ARG B CD  1 
ATOM   6857 N NE  . ARG B 1 333 ? -5.260  13.992  43.226  1.00 20.55 ? 333 ARG B NE  1 
ATOM   6858 C CZ  . ARG B 1 333 ? -6.364  14.658  42.890  1.00 24.31 ? 333 ARG B CZ  1 
ATOM   6859 N NH1 . ARG B 1 333 ? -7.563  14.172  43.189  1.00 27.38 ? 333 ARG B NH1 1 
ATOM   6860 N NH2 . ARG B 1 333 ? -6.270  15.814  42.271  1.00 29.73 ? 333 ARG B NH2 1 
ATOM   6861 N N   . LEU B 1 334 ? -4.833  9.034   48.152  1.00 22.48 ? 334 LEU B N   1 
ATOM   6862 C CA  . LEU B 1 334 ? -5.180  7.801   48.850  1.00 19.21 ? 334 LEU B CA  1 
ATOM   6863 C C   . LEU B 1 334 ? -5.325  8.028   50.351  1.00 21.62 ? 334 LEU B C   1 
ATOM   6864 O O   . LEU B 1 334 ? -6.215  7.450   50.986  1.00 19.00 ? 334 LEU B O   1 
ATOM   6865 C CB  . LEU B 1 334 ? -4.131  6.727   48.575  1.00 19.33 ? 334 LEU B CB  1 
ATOM   6866 C CG  . LEU B 1 334 ? -4.014  6.184   47.153  1.00 20.47 ? 334 LEU B CG  1 
ATOM   6867 C CD1 . LEU B 1 334 ? -2.862  5.204   47.059  1.00 20.73 ? 334 LEU B CD1 1 
ATOM   6868 C CD2 . LEU B 1 334 ? -5.319  5.548   46.697  1.00 20.80 ? 334 LEU B CD2 1 
ATOM   6869 N N   . LYS B 1 335 ? -4.474  8.891   50.935  1.00 20.83 ? 335 LYS B N   1 
ATOM   6870 C CA  . LYS B 1 335 ? -4.581  9.184   52.361  1.00 23.08 ? 335 LYS B CA  1 
ATOM   6871 C C   . LYS B 1 335 ? -5.930  9.822   52.677  1.00 23.98 ? 335 LYS B C   1 
ATOM   6872 O O   . LYS B 1 335 ? -6.574  9.465   53.675  1.00 23.96 ? 335 LYS B O   1 
ATOM   6873 C CB  . LYS B 1 335 ? -3.416  10.083  52.793  1.00 25.03 ? 335 LYS B CB  1 
ATOM   6874 C CG  . LYS B 1 335 ? -3.338  10.315  54.300  1.00 41.99 ? 335 LYS B CG  1 
ATOM   6875 C CD  . LYS B 1 335 ? -2.010  9.834   54.871  1.00 49.66 ? 335 LYS B CD  1 
ATOM   6876 C CE  . LYS B 1 335 ? -0.831  10.499  54.160  1.00 53.91 ? 335 LYS B CE  1 
ATOM   6877 N NZ  . LYS B 1 335 ? 0.451   10.396  54.922  1.00 55.08 ? 335 LYS B NZ  1 
ATOM   6878 N N   . LYS B 1 336 ? -6.388  10.751  51.822  1.00 22.85 ? 336 LYS B N   1 
ATOM   6879 C CA  . LYS B 1 336 ? -7.702  11.362  52.024  1.00 25.41 ? 336 LYS B CA  1 
ATOM   6880 C C   . LYS B 1 336 ? -8.796  10.308  52.005  1.00 24.33 ? 336 LYS B C   1 
ATOM   6881 O O   . LYS B 1 336 ? -9.719  10.337  52.831  1.00 26.61 ? 336 LYS B O   1 
ATOM   6882 C CB  . LYS B 1 336 ? -7.974  12.424  50.951  1.00 29.95 ? 336 LYS B CB  1 
ATOM   6883 C CG  . LYS B 1 336 ? -9.360  13.164  51.014  1.00 42.25 ? 336 LYS B CG  1 
ATOM   6884 C CD  . LYS B 1 336 ? -10.612 12.304  50.644  1.00 50.64 ? 336 LYS B CD  1 
ATOM   6885 C CE  . LYS B 1 336 ? -10.891 12.209  49.150  1.00 49.55 ? 336 LYS B CE  1 
ATOM   6886 N NZ  . LYS B 1 336 ? -12.181 11.509  48.937  1.00 54.17 ? 336 LYS B NZ  1 
ATOM   6887 N N   . ILE B 1 337 ? -8.746  9.403   51.027  1.00 24.02 ? 337 ILE B N   1 
ATOM   6888 C CA  . ILE B 1 337 ? -9.756  8.355   50.956  1.00 20.03 ? 337 ILE B CA  1 
ATOM   6889 C C   . ILE B 1 337 ? -9.726  7.522   52.227  1.00 24.16 ? 337 ILE B C   1 
ATOM   6890 O O   . ILE B 1 337 ? -10.762 7.247   52.843  1.00 24.54 ? 337 ILE B O   1 
ATOM   6891 C CB  . ILE B 1 337 ? -9.526  7.477   49.714  1.00 18.54 ? 337 ILE B CB  1 
ATOM   6892 C CG1 . ILE B 1 337 ? -9.716  8.290   48.415  1.00 21.41 ? 337 ILE B CG1 1 
ATOM   6893 C CG2 . ILE B 1 337 ? -10.449 6.270   49.728  1.00 21.54 ? 337 ILE B CG2 1 
ATOM   6894 C CD1 . ILE B 1 337 ? -9.215  7.524   47.181  1.00 19.70 ? 337 ILE B CD1 1 
ATOM   6895 N N   . HIS B 1 338 ? -8.524  7.101   52.625  1.00 19.73 ? 338 HIS B N   1 
ATOM   6896 C CA  . HIS B 1 338 ? -8.330  6.394   53.889  1.00 19.87 ? 338 HIS B CA  1 
ATOM   6897 C C   . HIS B 1 338 ? -8.999  7.116   55.055  1.00 24.40 ? 338 HIS B C   1 
ATOM   6898 O O   . HIS B 1 338 ? -9.663  6.492   55.893  1.00 27.35 ? 338 HIS B O   1 
ATOM   6899 C CB  . HIS B 1 338 ? -6.827  6.251   54.133  1.00 22.68 ? 338 HIS B CB  1 
ATOM   6900 C CG  . HIS B 1 338 ? -6.468  5.438   55.337  1.00 25.17 ? 338 HIS B CG  1 
ATOM   6901 N ND1 . HIS B 1 338 ? -5.655  5.917   56.340  1.00 31.29 ? 338 HIS B ND1 1 
ATOM   6902 C CD2 . HIS B 1 338 ? -6.783  4.168   55.679  1.00 26.07 ? 338 HIS B CD2 1 
ATOM   6903 C CE1 . HIS B 1 338 ? -5.502  4.982   57.262  1.00 31.50 ? 338 HIS B CE1 1 
ATOM   6904 N NE2 . HIS B 1 338 ? -6.167  3.907   56.875  1.00 30.83 ? 338 HIS B NE2 1 
ATOM   6905 N N   . GLU B 1 339 ? -8.828  8.432   55.129  1.00 22.27 ? 339 GLU B N   1 
ATOM   6906 C CA  . GLU B 1 339 ? -9.321  9.201   56.261  1.00 22.32 ? 339 GLU B CA  1 
ATOM   6907 C C   . GLU B 1 339 ? -10.795 9.556   56.142  1.00 28.12 ? 339 GLU B C   1 
ATOM   6908 O O   . GLU B 1 339 ? -11.379 10.024  57.121  1.00 29.41 ? 339 GLU B O   1 
ATOM   6909 C CB  . GLU B 1 339 ? -8.470  10.457  56.409  1.00 29.36 ? 339 GLU B CB  1 
ATOM   6910 C CG  . GLU B 1 339 ? -7.046  10.136  56.866  1.00 34.96 ? 339 GLU B CG  1 
ATOM   6911 C CD  . GLU B 1 339 ? -6.099  11.310  56.737  1.00 43.90 ? 339 GLU B CD  1 
ATOM   6912 O OE1 . GLU B 1 339 ? -5.115  11.363  57.503  1.00 50.88 ? 339 GLU B OE1 1 
ATOM   6913 O OE2 . GLU B 1 339 ? -6.327  12.180  55.872  1.00 46.65 ? 339 GLU B OE2 1 
ATOM   6914 N N   . SER B 1 340 ? -11.415 9.333   54.983  1.00 29.53 ? 340 SER B N   1 
ATOM   6915 C CA  . SER B 1 340 ? -12.785 9.772   54.740  1.00 27.69 ? 340 SER B CA  1 
ATOM   6916 C C   . SER B 1 340 ? -13.828 8.753   55.177  1.00 31.34 ? 340 SER B C   1 
ATOM   6917 O O   . SER B 1 340 ? -15.015 9.088   55.234  1.00 30.96 ? 340 SER B O   1 
ATOM   6918 C CB  . SER B 1 340 ? -12.988 10.085  53.256  1.00 24.83 ? 340 SER B CB  1 
ATOM   6919 O OG  . SER B 1 340 ? -13.188 8.879   52.512  1.00 30.34 ? 340 SER B OG  1 
ATOM   6920 N N   . VAL B 1 341 ? -13.426 7.523   55.489  1.00 31.94 ? 341 VAL B N   1 
ATOM   6921 C CA  . VAL B 1 341 ? -14.376 6.483   55.859  1.00 29.04 ? 341 VAL B CA  1 
ATOM   6922 C C   . VAL B 1 341 ? -13.847 5.719   57.060  1.00 29.89 ? 341 VAL B C   1 
ATOM   6923 O O   . VAL B 1 341 ? -12.633 5.602   57.260  1.00 32.81 ? 341 VAL B O   1 
ATOM   6924 C CB  . VAL B 1 341 ? -14.657 5.516   54.688  1.00 32.85 ? 341 VAL B CB  1 
ATOM   6925 C CG1 . VAL B 1 341 ? -15.460 6.215   53.609  1.00 32.07 ? 341 VAL B CG1 1 
ATOM   6926 C CG2 . VAL B 1 341 ? -13.345 4.960   54.121  1.00 31.20 ? 341 VAL B CG2 1 
ATOM   6927 N N   . ASP B 1 342 ? -14.785 5.170   57.833  1.00 32.53 ? 342 ASP B N   1 
ATOM   6928 C CA  . ASP B 1 342 ? -14.495 4.347   58.998  1.00 40.65 ? 342 ASP B CA  1 
ATOM   6929 C C   . ASP B 1 342 ? -14.153 2.917   58.629  1.00 39.49 ? 342 ASP B C   1 
ATOM   6930 O O   . ASP B 1 342 ? -13.513 2.223   59.426  1.00 43.72 ? 342 ASP B O   1 
ATOM   6931 C CB  . ASP B 1 342 ? -15.703 4.322   59.944  1.00 48.53 ? 342 ASP B CB  1 
ATOM   6932 C CG  . ASP B 1 342 ? -15.758 5.521   60.860  1.00 58.72 ? 342 ASP B CG  1 
ATOM   6933 O OD1 . ASP B 1 342 ? -14.696 6.148   61.076  1.00 64.68 ? 342 ASP B OD1 1 
ATOM   6934 O OD2 . ASP B 1 342 ? -16.858 5.823   61.382  1.00 58.90 ? 342 ASP B OD2 1 
ATOM   6935 N N   . PHE B 1 343 ? -14.581 2.462   57.454  1.00 33.66 ? 343 PHE B N   1 
ATOM   6936 C CA  . PHE B 1 343 ? -14.389 1.093   57.016  1.00 31.21 ? 343 PHE B CA  1 
ATOM   6937 C C   . PHE B 1 343 ? -13.166 1.025   56.106  1.00 22.78 ? 343 PHE B C   1 
ATOM   6938 O O   . PHE B 1 343 ? -12.472 2.018   55.890  1.00 29.23 ? 343 PHE B O   1 
ATOM   6939 C CB  . PHE B 1 343 ? -15.656 0.578   56.327  1.00 26.75 ? 343 PHE B CB  1 
ATOM   6940 C CG  . PHE B 1 343 ? -16.081 1.383   55.119  1.00 25.36 ? 343 PHE B CG  1 
ATOM   6941 C CD1 . PHE B 1 343 ? -16.915 2.490   55.260  1.00 28.06 ? 343 PHE B CD1 1 
ATOM   6942 C CD2 . PHE B 1 343 ? -15.674 1.011   53.848  1.00 26.67 ? 343 PHE B CD2 1 
ATOM   6943 C CE1 . PHE B 1 343 ? -17.319 3.229   54.140  1.00 29.89 ? 343 PHE B CE1 1 
ATOM   6944 C CE2 . PHE B 1 343 ? -16.060 1.741   52.719  1.00 30.69 ? 343 PHE B CE2 1 
ATOM   6945 C CZ  . PHE B 1 343 ? -16.891 2.856   52.868  1.00 30.24 ? 343 PHE B CZ  1 
ATOM   6946 N N   . GLN B 1 344 ? -12.889 -0.165  55.563  1.00 20.87 ? 344 GLN B N   1 
ATOM   6947 C CA  . GLN B 1 344 ? -11.735 -0.338  54.700  1.00 21.02 ? 344 GLN B CA  1 
ATOM   6948 C C   . GLN B 1 344 ? -12.178 -0.196  53.253  1.00 19.30 ? 344 GLN B C   1 
ATOM   6949 O O   . GLN B 1 344 ? -12.857 -1.098  52.728  1.00 20.32 ? 344 GLN B O   1 
ATOM   6950 C CB  . GLN B 1 344 ? -11.076 -1.686  54.948  1.00 21.03 ? 344 GLN B CB  1 
ATOM   6951 C CG  . GLN B 1 344 ? -10.553 -1.783  56.380  1.00 19.88 ? 344 GLN B CG  1 
ATOM   6952 C CD  . GLN B 1 344 ? -9.670  -3.002  56.636  1.00 26.72 ? 344 GLN B CD  1 
ATOM   6953 O OE1 . GLN B 1 344 ? -8.526  -2.878  57.080  1.00 25.73 ? 344 GLN B OE1 1 
ATOM   6954 N NE2 . GLN B 1 344 ? -10.199 -4.174  56.363  1.00 22.75 ? 344 GLN B NE2 1 
ATOM   6955 N N   . PRO B 1 345 ? -11.825 0.893   52.574  1.00 20.50 ? 345 PRO B N   1 
ATOM   6956 C CA  . PRO B 1 345 ? -12.278 1.098   51.198  1.00 20.72 ? 345 PRO B CA  1 
ATOM   6957 C C   . PRO B 1 345 ? -11.478 0.251   50.229  1.00 21.12 ? 345 PRO B C   1 
ATOM   6958 O O   . PRO B 1 345 ? -10.305 -0.056  50.456  1.00 18.37 ? 345 PRO B O   1 
ATOM   6959 C CB  . PRO B 1 345 ? -12.014 2.591   50.964  1.00 20.27 ? 345 PRO B CB  1 
ATOM   6960 C CG  . PRO B 1 345 ? -10.778 2.881   51.855  1.00 20.11 ? 345 PRO B CG  1 
ATOM   6961 C CD  . PRO B 1 345 ? -10.967 1.991   53.067  1.00 24.07 ? 345 PRO B CD  1 
ATOM   6962 N N   . VAL B 1 346 ? -12.136 -0.129  49.142  1.00 15.66 ? 346 VAL B N   1 
ATOM   6963 C CA  . VAL B 1 346 ? -11.472 -0.811  48.037  1.00 16.24 ? 346 VAL B CA  1 
ATOM   6964 C C   . VAL B 1 346 ? -11.390 0.172   46.878  1.00 16.66 ? 346 VAL B C   1 
ATOM   6965 O O   . VAL B 1 346 ? -12.423 0.633   46.370  1.00 17.40 ? 346 VAL B O   1 
ATOM   6966 C CB  . VAL B 1 346 ? -12.208 -2.099  47.641  1.00 18.52 ? 346 VAL B CB  1 
ATOM   6967 C CG1 . VAL B 1 346 ? -11.431 -2.845  46.549  1.00 19.45 ? 346 VAL B CG1 1 
ATOM   6968 C CG2 . VAL B 1 346 ? -12.422 -2.978  48.867  1.00 21.33 ? 346 VAL B CG2 1 
ATOM   6969 N N   . VAL B 1 347 ? -10.163 0.459   46.432  1.00 15.91 ? 347 VAL B N   1 
ATOM   6970 C CA  . VAL B 1 347 ? -9.891  1.494   45.439  1.00 14.18 ? 347 VAL B CA  1 
ATOM   6971 C C   . VAL B 1 347 ? -9.376  0.801   44.183  1.00 15.01 ? 347 VAL B C   1 
ATOM   6972 O O   . VAL B 1 347 ? -8.235  0.323   44.156  1.00 16.39 ? 347 VAL B O   1 
ATOM   6973 C CB  . VAL B 1 347 ? -8.876  2.520   45.970  1.00 18.24 ? 347 VAL B CB  1 
ATOM   6974 C CG1 . VAL B 1 347 ? -8.635  3.610   44.928  1.00 15.37 ? 347 VAL B CG1 1 
ATOM   6975 C CG2 . VAL B 1 347 ? -9.377  3.150   47.299  1.00 18.42 ? 347 VAL B CG2 1 
ATOM   6976 N N   . PHE B 1 348 ? -10.203 0.747   43.134  1.00 14.54 ? 348 PHE B N   1 
ATOM   6977 C CA  . PHE B 1 348 ? -9.791  0.151   41.861  1.00 14.84 ? 348 PHE B CA  1 
ATOM   6978 C C   . PHE B 1 348 ? -9.238  1.228   40.932  1.00 16.46 ? 348 PHE B C   1 
ATOM   6979 O O   . PHE B 1 348 ? -9.910  2.226   40.664  1.00 17.26 ? 348 PHE B O   1 
ATOM   6980 C CB  . PHE B 1 348 ? -10.975 -0.546  41.177  1.00 16.06 ? 348 PHE B CB  1 
ATOM   6981 C CG  . PHE B 1 348 ? -11.054 -2.029  41.440  1.00 14.55 ? 348 PHE B CG  1 
ATOM   6982 C CD1 . PHE B 1 348 ? -11.364 -2.512  42.710  1.00 15.29 ? 348 PHE B CD1 1 
ATOM   6983 C CD2 . PHE B 1 348 ? -10.799 -2.937  40.429  1.00 16.47 ? 348 PHE B CD2 1 
ATOM   6984 C CE1 . PHE B 1 348 ? -11.437 -3.910  42.961  1.00 16.57 ? 348 PHE B CE1 1 
ATOM   6985 C CE2 . PHE B 1 348 ? -10.869 -4.318  40.667  1.00 15.85 ? 348 PHE B CE2 1 
ATOM   6986 C CZ  . PHE B 1 348 ? -11.188 -4.788  41.933  1.00 16.66 ? 348 PHE B CZ  1 
ATOM   6987 N N   . VAL B 1 349 ? -8.016  1.014   40.437  1.00 13.20 ? 349 VAL B N   1 
ATOM   6988 C CA  . VAL B 1 349 ? -7.362  1.882   39.465  1.00 14.62 ? 349 VAL B CA  1 
ATOM   6989 C C   . VAL B 1 349 ? -7.261  1.060   38.182  1.00 12.87 ? 349 VAL B C   1 
ATOM   6990 O O   . VAL B 1 349 ? -6.505  0.081   38.127  1.00 13.63 ? 349 VAL B O   1 
ATOM   6991 C CB  . VAL B 1 349 ? -5.982  2.331   39.965  1.00 14.23 ? 349 VAL B CB  1 
ATOM   6992 C CG1 . VAL B 1 349 ? -5.316  3.249   38.955  1.00 15.50 ? 349 VAL B CG1 1 
ATOM   6993 C CG2 . VAL B 1 349 ? -6.143  3.034   41.300  1.00 16.57 ? 349 VAL B CG2 1 
ATOM   6994 N N   . VAL B 1 350 ? -8.080  1.395   37.185  1.00 11.21 ? 350 VAL B N   1 
ATOM   6995 C CA  . VAL B 1 350 ? -8.245  0.584   35.986  1.00 12.09 ? 350 VAL B CA  1 
ATOM   6996 C C   . VAL B 1 350 ? -8.114  1.485   34.770  1.00 14.52 ? 350 VAL B C   1 
ATOM   6997 O O   . VAL B 1 350 ? -8.834  2.486   34.661  1.00 13.65 ? 350 VAL B O   1 
ATOM   6998 C CB  . VAL B 1 350 ? -9.613  -0.121  35.954  1.00 15.36 ? 350 VAL B CB  1 
ATOM   6999 C CG1 . VAL B 1 350 ? -9.658  -1.131  34.738  1.00 13.72 ? 350 VAL B CG1 1 
ATOM   7000 C CG2 . VAL B 1 350 ? -9.902  -0.820  37.279  1.00 17.63 ? 350 VAL B CG2 1 
ATOM   7001 N N   . LEU B 1 351 ? -7.202  1.132   33.855  1.00 13.28 ? 351 LEU B N   1 
ATOM   7002 C CA  . LEU B 1 351 ? -6.996  1.915   32.639  1.00 11.05 ? 351 LEU B CA  1 
ATOM   7003 C C   . LEU B 1 351 ? -6.162  1.090   31.677  1.00 11.01 ? 351 LEU B C   1 
ATOM   7004 O O   . LEU B 1 351 ? -5.647  0.033   32.040  1.00 13.42 ? 351 LEU B O   1 
ATOM   7005 C CB  . LEU B 1 351 ? -6.331  3.277   32.930  1.00 15.75 ? 351 LEU B CB  1 
ATOM   7006 C CG  . LEU B 1 351 ? -4.940  3.201   33.597  1.00 16.41 ? 351 LEU B CG  1 
ATOM   7007 C CD1 . LEU B 1 351 ? -4.085  4.365   33.130  1.00 17.82 ? 351 LEU B CD1 1 
ATOM   7008 C CD2 . LEU B 1 351 ? -5.042  3.185   35.142  1.00 19.03 ? 351 LEU B CD2 1 
ATOM   7009 N N   . ASP B 1 352 ? -6.048  1.575   30.438  1.00 11.24 ? 352 ASP B N   1 
ATOM   7010 C CA  . ASP B 1 352 ? -5.138  0.936   29.477  1.00 14.78 ? 352 ASP B CA  1 
ATOM   7011 C C   . ASP B 1 352 ? -3.744  0.848   30.085  1.00 15.15 ? 352 ASP B C   1 
ATOM   7012 O O   . ASP B 1 352 ? -3.290  1.779   30.752  1.00 15.13 ? 352 ASP B O   1 
ATOM   7013 C CB  . ASP B 1 352 ? -5.064  1.728   28.169  1.00 14.09 ? 352 ASP B CB  1 
ATOM   7014 C CG  . ASP B 1 352 ? -6.390  1.785   27.420  1.00 17.49 ? 352 ASP B CG  1 
ATOM   7015 O OD1 . ASP B 1 352 ? -7.366  1.137   27.845  1.00 16.04 ? 352 ASP B OD1 1 
ATOM   7016 O OD2 . ASP B 1 352 ? -6.445  2.519   26.404  1.00 16.79 ? 352 ASP B OD2 1 
ATOM   7017 N N   . GLY B 1 353 ? -3.076  -0.282  29.877  1.00 10.23 ? 353 GLY B N   1 
ATOM   7018 C CA  . GLY B 1 353 ? -1.798  -0.483  30.508  1.00 12.03 ? 353 GLY B CA  1 
ATOM   7019 C C   . GLY B 1 353 ? -0.622  -0.141  29.642  1.00 13.63 ? 353 GLY B C   1 
ATOM   7020 O O   . GLY B 1 353 ? 0.515   -0.224  30.124  1.00 13.06 ? 353 GLY B O   1 
ATOM   7021 N N   . GLU B 1 354 ? -0.839  0.261   28.385  1.00 13.11 ? 354 GLU B N   1 
ATOM   7022 C CA  . GLU B 1 354 ? 0.297   0.486   27.492  1.00 12.77 ? 354 GLU B CA  1 
ATOM   7023 C C   . GLU B 1 354 ? 0.266   1.811   26.741  1.00 15.82 ? 354 GLU B C   1 
ATOM   7024 O O   . GLU B 1 354 ? 1.199   2.082   25.978  1.00 16.28 ? 354 GLU B O   1 
ATOM   7025 C CB  . GLU B 1 354 ? 0.414   -0.656  26.458  1.00 11.37 ? 354 GLU B CB  1 
ATOM   7026 C CG  . GLU B 1 354 ? -0.567  -0.555  25.293  1.00 13.09 ? 354 GLU B CG  1 
ATOM   7027 C CD  . GLU B 1 354 ? -1.989  -1.038  25.658  1.00 11.31 ? 354 GLU B CD  1 
ATOM   7028 O OE1 . GLU B 1 354 ? -2.396  -2.122  25.140  1.00 13.78 ? 354 GLU B OE1 1 
ATOM   7029 O OE2 . GLU B 1 354 ? -2.672  -0.356  26.439  1.00 13.65 ? 354 GLU B OE2 1 
ATOM   7030 N N   . ASN B 1 355 ? -0.758  2.643   26.924  1.00 12.27 ? 355 ASN B N   1 
ATOM   7031 C CA  . ASN B 1 355 ? -0.899  3.816   26.070  1.00 11.61 ? 355 ASN B CA  1 
ATOM   7032 C C   . ASN B 1 355 ? -0.485  5.135   26.701  1.00 17.10 ? 355 ASN B C   1 
ATOM   7033 O O   . ASN B 1 355 ? -0.216  6.090   25.962  1.00 16.25 ? 355 ASN B O   1 
ATOM   7034 C CB  . ASN B 1 355 ? -2.348  3.907   25.571  1.00 13.42 ? 355 ASN B CB  1 
ATOM   7035 C CG  . ASN B 1 355 ? -2.684  2.768   24.645  1.00 13.88 ? 355 ASN B CG  1 
ATOM   7036 O OD1 . ASN B 1 355 ? -1.835  2.357   23.857  1.00 14.22 ? 355 ASN B OD1 1 
ATOM   7037 N ND2 . ASN B 1 355 ? -3.897  2.208   24.767  1.00 15.15 ? 355 ASN B ND2 1 
ATOM   7038 N N   . CYS B 1 356 ? -0.393  5.219   28.012  1.00 15.73 ? 356 CYS B N   1 
ATOM   7039 C CA  . CYS B 1 356 ? -0.087  6.516   28.610  1.00 14.09 ? 356 CYS B CA  1 
ATOM   7040 C C   . CYS B 1 356 ? 1.412   6.769   28.762  1.00 16.18 ? 356 CYS B C   1 
ATOM   7041 O O   . CYS B 1 356 ? 1.830   7.931   28.774  1.00 15.20 ? 356 CYS B O   1 
ATOM   7042 C CB  . CYS B 1 356 ? -0.787  6.640   29.964  1.00 14.21 ? 356 CYS B CB  1 
ATOM   7043 S SG  . CYS B 1 356 ? -0.352  5.346   31.165  1.00 15.91 ? 356 CYS B SG  1 
ATOM   7044 N N   . TRP B 1 357 ? 2.236   5.720   28.830  1.00 14.21 ? 357 TRP B N   1 
ATOM   7045 C CA  . TRP B 1 357 ? 3.625   5.875   29.273  1.00 16.44 ? 357 TRP B CA  1 
ATOM   7046 C C   . TRP B 1 357 ? 4.476   6.631   28.264  1.00 16.83 ? 357 TRP B C   1 
ATOM   7047 O O   . TRP B 1 357 ? 5.449   7.293   28.654  1.00 17.72 ? 357 TRP B O   1 
ATOM   7048 C CB  . TRP B 1 357 ? 4.252   4.503   29.541  1.00 13.11 ? 357 TRP B CB  1 
ATOM   7049 C CG  . TRP B 1 357 ? 3.326   3.677   30.388  1.00 13.31 ? 357 TRP B CG  1 
ATOM   7050 C CD1 . TRP B 1 357 ? 2.702   2.491   30.065  1.00 15.28 ? 357 TRP B CD1 1 
ATOM   7051 C CD2 . TRP B 1 357 ? 2.860   4.037   31.679  1.00 15.88 ? 357 TRP B CD2 1 
ATOM   7052 N NE1 . TRP B 1 357 ? 1.893   2.094   31.109  1.00 11.77 ? 357 TRP B NE1 1 
ATOM   7053 C CE2 . TRP B 1 357 ? 1.969   3.031   32.107  1.00 12.11 ? 357 TRP B CE2 1 
ATOM   7054 C CE3 . TRP B 1 357 ? 3.116   5.127   32.526  1.00 14.35 ? 357 TRP B CE3 1 
ATOM   7055 C CZ2 . TRP B 1 357 ? 1.321   3.082   33.351  1.00 11.59 ? 357 TRP B CZ2 1 
ATOM   7056 C CZ3 . TRP B 1 357 ? 2.475   5.187   33.749  1.00 13.51 ? 357 TRP B CZ3 1 
ATOM   7057 C CH2 . TRP B 1 357 ? 1.588   4.170   34.158  1.00 11.21 ? 357 TRP B CH2 1 
ATOM   7058 N N   . GLU B 1 358 ? 4.137   6.531   26.974  1.00 16.16 ? 358 GLU B N   1 
ATOM   7059 C CA  . GLU B 1 358 ? 4.921   7.200   25.935  1.00 17.07 ? 358 GLU B CA  1 
ATOM   7060 C C   . GLU B 1 358 ? 4.885   8.717   26.063  1.00 19.62 ? 358 GLU B C   1 
ATOM   7061 O O   . GLU B 1 358 ? 5.739   9.400   25.474  1.00 19.05 ? 358 GLU B O   1 
ATOM   7062 C CB  . GLU B 1 358 ? 4.427   6.809   24.545  1.00 16.99 ? 358 GLU B CB  1 
ATOM   7063 C CG  . GLU B 1 358 ? 2.997   7.231   24.238  1.00 21.42 ? 358 GLU B CG  1 
ATOM   7064 C CD  . GLU B 1 358 ? 2.374   6.349   23.169  1.00 21.53 ? 358 GLU B CD  1 
ATOM   7065 O OE1 . GLU B 1 358 ? 2.075   6.855   22.064  1.00 24.53 ? 358 GLU B OE1 1 
ATOM   7066 O OE2 . GLU B 1 358 ? 2.177   5.137   23.435  1.00 22.11 ? 358 GLU B OE2 1 
ATOM   7067 N N   . TYR B 1 359 ? 3.930   9.257   26.819  1.00 19.05 ? 359 TYR B N   1 
ATOM   7068 C CA  . TYR B 1 359 ? 3.885   10.695  27.057  1.00 18.98 ? 359 TYR B CA  1 
ATOM   7069 C C   . TYR B 1 359 ? 4.588   11.097  28.352  1.00 22.23 ? 359 TYR B C   1 
ATOM   7070 O O   . TYR B 1 359 ? 4.693   12.291  28.634  1.00 22.95 ? 359 TYR B O   1 
ATOM   7071 C CB  . TYR B 1 359 ? 2.427   11.188  27.049  1.00 21.21 ? 359 TYR B CB  1 
ATOM   7072 C CG  . TYR B 1 359 ? 1.678   10.840  25.765  1.00 23.38 ? 359 TYR B CG  1 
ATOM   7073 C CD1 . TYR B 1 359 ? 1.822   11.612  24.610  1.00 30.70 ? 359 TYR B CD1 1 
ATOM   7074 C CD2 . TYR B 1 359 ? 0.860   9.719   25.696  1.00 24.71 ? 359 TYR B CD2 1 
ATOM   7075 C CE1 . TYR B 1 359 ? 1.148   11.278  23.433  1.00 26.74 ? 359 TYR B CE1 1 
ATOM   7076 C CE2 . TYR B 1 359 ? 0.182   9.379   24.515  1.00 28.73 ? 359 TYR B CE2 1 
ATOM   7077 C CZ  . TYR B 1 359 ? 0.329   10.161  23.397  1.00 29.46 ? 359 TYR B CZ  1 
ATOM   7078 O OH  . TYR B 1 359 ? -0.347  9.805   22.238  1.00 37.19 ? 359 TYR B OH  1 
ATOM   7079 N N   . TYR B 1 360 ? 5.080   10.138  29.138  1.00 18.33 ? 360 TYR B N   1 
ATOM   7080 C CA  . TYR B 1 360 ? 5.844   10.418  30.339  1.00 19.94 ? 360 TYR B CA  1 
ATOM   7081 C C   . TYR B 1 360 ? 7.330   10.538  30.016  1.00 24.13 ? 360 TYR B C   1 
ATOM   7082 O O   . TYR B 1 360 ? 7.835   9.881   29.104  1.00 22.61 ? 360 TYR B O   1 
ATOM   7083 C CB  . TYR B 1 360 ? 5.691   9.297   31.373  1.00 18.08 ? 360 TYR B CB  1 
ATOM   7084 C CG  . TYR B 1 360 ? 4.412   9.212   32.194  1.00 15.53 ? 360 TYR B CG  1 
ATOM   7085 C CD1 . TYR B 1 360 ? 3.201   8.877   31.614  1.00 16.29 ? 360 TYR B CD1 1 
ATOM   7086 C CD2 . TYR B 1 360 ? 4.449   9.369   33.584  1.00 17.75 ? 360 TYR B CD2 1 
ATOM   7087 C CE1 . TYR B 1 360 ? 2.057   8.735   32.376  1.00 14.88 ? 360 TYR B CE1 1 
ATOM   7088 C CE2 . TYR B 1 360 ? 3.304   9.214   34.361  1.00 14.79 ? 360 TYR B CE2 1 
ATOM   7089 C CZ  . TYR B 1 360 ? 2.114   8.917   33.754  1.00 13.46 ? 360 TYR B CZ  1 
ATOM   7090 O OH  . TYR B 1 360 ? 0.972   8.771   34.505  1.00 15.05 ? 360 TYR B OH  1 
ATOM   7091 N N   . GLU B 1 361 ? 8.038   11.363  30.789  1.00 24.78 ? 361 GLU B N   1 
ATOM   7092 C CA  . GLU B 1 361 ? 9.494   11.350  30.725  1.00 28.61 ? 361 GLU B CA  1 
ATOM   7093 C C   . GLU B 1 361 ? 10.010  9.936   30.938  1.00 26.69 ? 361 GLU B C   1 
ATOM   7094 O O   . GLU B 1 361 ? 9.506   9.200   31.793  1.00 25.06 ? 361 GLU B O   1 
ATOM   7095 C CB  . GLU B 1 361 ? 10.095  12.282  31.782  1.00 35.99 ? 361 GLU B CB  1 
ATOM   7096 C CG  . GLU B 1 361 ? 9.638   13.704  31.651  1.00 49.79 ? 361 GLU B CG  1 
ATOM   7097 C CD  . GLU B 1 361 ? 9.865   14.246  30.260  1.00 60.14 ? 361 GLU B CD  1 
ATOM   7098 O OE1 . GLU B 1 361 ? 8.963   14.931  29.733  1.00 65.53 ? 361 GLU B OE1 1 
ATOM   7099 O OE2 . GLU B 1 361 ? 10.952  13.997  29.692  1.00 62.89 ? 361 GLU B OE2 1 
ATOM   7100 N N   . GLU B 1 362 ? 11.010  9.555   30.138  1.00 24.28 ? 362 GLU B N   1 
ATOM   7101 C CA  . GLU B 1 362 ? 11.632  8.226   30.225  1.00 23.59 ? 362 GLU B CA  1 
ATOM   7102 C C   . GLU B 1 362 ? 10.592  7.105   30.282  1.00 24.13 ? 362 GLU B C   1 
ATOM   7103 O O   . GLU B 1 362 ? 10.746  6.120   31.006  1.00 20.56 ? 362 GLU B O   1 
ATOM   7104 C CB  . GLU B 1 362 ? 12.587  8.153   31.422  1.00 26.35 ? 362 GLU B CB  1 
ATOM   7105 C CG  . GLU B 1 362 ? 13.962  8.716   31.113  1.00 34.05 ? 362 GLU B CG  1 
ATOM   7106 C CD  . GLU B 1 362 ? 14.827  8.864   32.348  1.00 50.99 ? 362 GLU B CD  1 
ATOM   7107 O OE1 . GLU B 1 362 ? 15.304  9.990   32.612  1.00 58.08 ? 362 GLU B OE1 1 
ATOM   7108 O OE2 . GLU B 1 362 ? 15.029  7.852   33.052  1.00 55.27 ? 362 GLU B OE2 1 
ATOM   7109 N N   . ASN B 1 363 ? 9.521   7.242   29.494  1.00 17.86 ? 363 ASN B N   1 
ATOM   7110 C CA  . ASN B 1 363 ? 8.515   6.197   29.345  1.00 20.19 ? 363 ASN B CA  1 
ATOM   7111 C C   . ASN B 1 363 ? 7.860   5.818   30.685  1.00 19.37 ? 363 ASN B C   1 
ATOM   7112 O O   . ASN B 1 363 ? 7.465   4.667   30.899  1.00 17.81 ? 363 ASN B O   1 
ATOM   7113 C CB  . ASN B 1 363 ? 9.109   4.955   28.658  1.00 20.35 ? 363 ASN B CB  1 
ATOM   7114 C CG  . ASN B 1 363 ? 8.042   3.991   28.197  1.00 22.62 ? 363 ASN B CG  1 
ATOM   7115 O OD1 . ASN B 1 363 ? 7.028   4.394   27.649  1.00 17.52 ? 363 ASN B OD1 1 
ATOM   7116 N ND2 . ASN B 1 363 ? 8.248   2.713   28.449  1.00 20.84 ? 363 ASN B ND2 1 
ATOM   7117 N N   . GLY B 1 364 ? 7.727   6.777   31.607  1.00 18.46 ? 364 GLY B N   1 
ATOM   7118 C CA  . GLY B 1 364 ? 7.041   6.480   32.853  1.00 17.29 ? 364 GLY B CA  1 
ATOM   7119 C C   . GLY B 1 364 ? 7.835   5.669   33.855  1.00 16.66 ? 364 GLY B C   1 
ATOM   7120 O O   . GLY B 1 364 ? 7.300   5.336   34.919  1.00 17.58 ? 364 GLY B O   1 
ATOM   7121 N N   . ILE B 1 365 ? 9.093   5.359   33.578  1.00 14.81 ? 365 ILE B N   1 
ATOM   7122 C CA  . ILE B 1 365 ? 9.854   4.466   34.442  1.00 15.99 ? 365 ILE B CA  1 
ATOM   7123 C C   . ILE B 1 365 ? 10.164  5.146   35.776  1.00 21.44 ? 365 ILE B C   1 
ATOM   7124 O O   . ILE B 1 365 ? 9.933   4.531   36.831  1.00 20.12 ? 365 ILE B O   1 
ATOM   7125 C CB  . ILE B 1 365 ? 11.109  3.958   33.718  1.00 20.14 ? 365 ILE B CB  1 
ATOM   7126 C CG1 . ILE B 1 365 ? 10.657  3.093   32.537  1.00 20.14 ? 365 ILE B CG1 1 
ATOM   7127 C CG2 . ILE B 1 365 ? 11.965  3.125   34.664  1.00 23.39 ? 365 ILE B CG2 1 
ATOM   7128 C CD1 . ILE B 1 365 ? 11.737  2.816   31.540  1.00 23.85 ? 365 ILE B CD1 1 
ATOM   7129 N N   . PRO B 1 366 ? 10.643  6.397   35.803  1.00 22.95 ? 366 PRO B N   1 
ATOM   7130 C CA  . PRO B 1 366 ? 10.786  7.073   37.107  1.00 21.21 ? 366 PRO B CA  1 
ATOM   7131 C C   . PRO B 1 366 ? 9.488   7.119   37.900  1.00 15.56 ? 366 PRO B C   1 
ATOM   7132 O O   . PRO B 1 366 ? 9.510   6.906   39.122  1.00 21.09 ? 366 PRO B O   1 
ATOM   7133 C CB  . PRO B 1 366 ? 11.275  8.477   36.722  1.00 24.88 ? 366 PRO B CB  1 
ATOM   7134 C CG  . PRO B 1 366 ? 11.948  8.291   35.408  1.00 24.94 ? 366 PRO B CG  1 
ATOM   7135 C CD  . PRO B 1 366 ? 11.169  7.230   34.702  1.00 22.11 ? 366 PRO B CD  1 
ATOM   7136 N N   . PHE B 1 367 ? 8.354   7.350   37.234  1.00 15.07 ? 367 PHE B N   1 
ATOM   7137 C CA  . PHE B 1 367 ? 7.076   7.405   37.943  1.00 14.59 ? 367 PHE B CA  1 
ATOM   7138 C C   . PHE B 1 367 ? 6.696   6.051   38.536  1.00 16.28 ? 367 PHE B C   1 
ATOM   7139 O O   . PHE B 1 367 ? 6.401   5.956   39.736  1.00 15.90 ? 367 PHE B O   1 
ATOM   7140 C CB  . PHE B 1 367 ? 5.970   7.919   37.017  1.00 14.37 ? 367 PHE B CB  1 
ATOM   7141 C CG  . PHE B 1 367 ? 4.600   7.822   37.626  1.00 19.56 ? 367 PHE B CG  1 
ATOM   7142 C CD1 . PHE B 1 367 ? 4.191   8.741   38.606  1.00 22.84 ? 367 PHE B CD1 1 
ATOM   7143 C CD2 . PHE B 1 367 ? 3.738   6.811   37.245  1.00 15.05 ? 367 PHE B CD2 1 
ATOM   7144 C CE1 . PHE B 1 367 ? 2.927   8.661   39.183  1.00 15.99 ? 367 PHE B CE1 1 
ATOM   7145 C CE2 . PHE B 1 367 ? 2.456   6.695   37.812  1.00 14.64 ? 367 PHE B CE2 1 
ATOM   7146 C CZ  . PHE B 1 367 ? 2.049   7.630   38.785  1.00 17.32 ? 367 PHE B CZ  1 
ATOM   7147 N N   . LEU B 1 368 ? 6.688   4.984   37.719  1.00 14.62 ? 368 LEU B N   1 
ATOM   7148 C CA  . LEU B 1 368 ? 6.268   3.692   38.269  1.00 14.61 ? 368 LEU B CA  1 
ATOM   7149 C C   . LEU B 1 368 ? 7.263   3.163   39.303  1.00 14.33 ? 368 LEU B C   1 
ATOM   7150 O O   . LEU B 1 368 ? 6.856   2.549   40.291  1.00 14.69 ? 368 LEU B O   1 
ATOM   7151 C CB  . LEU B 1 368 ? 6.058   2.670   37.149  1.00 12.04 ? 368 LEU B CB  1 
ATOM   7152 C CG  . LEU B 1 368 ? 4.823   3.023   36.326  1.00 11.61 ? 368 LEU B CG  1 
ATOM   7153 C CD1 . LEU B 1 368 ? 4.691   2.098   35.113  1.00 14.16 ? 368 LEU B CD1 1 
ATOM   7154 C CD2 . LEU B 1 368 ? 3.558   2.996   37.195  1.00 13.70 ? 368 LEU B CD2 1 
ATOM   7155 N N   . GLU B 1 369 ? 8.564   3.299   39.060  1.00 13.89 ? 369 GLU B N   1 
ATOM   7156 C CA  . GLU B 1 369 ? 9.526   2.843   40.062  1.00 17.11 ? 369 GLU B CA  1 
ATOM   7157 C C   . GLU B 1 369 ? 9.329   3.562   41.390  1.00 17.34 ? 369 GLU B C   1 
ATOM   7158 O O   . GLU B 1 369 ? 9.351   2.930   42.458  1.00 17.59 ? 369 GLU B O   1 
ATOM   7159 C CB  . GLU B 1 369 ? 10.961  3.026   39.558  1.00 15.33 ? 369 GLU B CB  1 
ATOM   7160 C CG  . GLU B 1 369 ? 11.327  1.979   38.492  1.00 15.82 ? 369 GLU B CG  1 
ATOM   7161 C CD  . GLU B 1 369 ? 12.784  2.049   38.047  1.00 25.60 ? 369 GLU B CD  1 
ATOM   7162 O OE1 . GLU B 1 369 ? 13.486  3.019   38.427  1.00 30.70 ? 369 GLU B OE1 1 
ATOM   7163 O OE2 . GLU B 1 369 ? 13.226  1.113   37.340  1.00 24.65 ? 369 GLU B OE2 1 
ATOM   7164 N N   . LYS B 1 370 ? 9.107   4.872   41.351  1.00 16.56 ? 370 LYS B N   1 
ATOM   7165 C CA  . LYS B 1 370 ? 8.872   5.592   42.588  1.00 19.40 ? 370 LYS B CA  1 
ATOM   7166 C C   . LYS B 1 370 ? 7.513   5.244   43.191  1.00 15.85 ? 370 LYS B C   1 
ATOM   7167 O O   . LYS B 1 370 ? 7.399   5.123   44.422  1.00 17.73 ? 370 LYS B O   1 
ATOM   7168 C CB  . LYS B 1 370 ? 9.005   7.094   42.336  1.00 18.18 ? 370 LYS B CB  1 
ATOM   7169 C CG  . LYS B 1 370 ? 10.469  7.520   42.201  1.00 32.07 ? 370 LYS B CG  1 
ATOM   7170 C CD  . LYS B 1 370 ? 10.633  8.774   41.338  1.00 43.72 ? 370 LYS B CD  1 
ATOM   7171 C CE  . LYS B 1 370 ? 12.082  8.968   40.872  1.00 47.63 ? 370 LYS B CE  1 
ATOM   7172 N NZ  . LYS B 1 370 ? 13.073  8.807   41.981  1.00 45.11 ? 370 LYS B NZ  1 
ATOM   7173 N N   . LEU B 1 371 ? 6.488   5.056   42.353  1.00 14.77 ? 371 LEU B N   1 
ATOM   7174 C CA  . LEU B 1 371 ? 5.166   4.715   42.871  1.00 13.63 ? 371 LEU B CA  1 
ATOM   7175 C C   . LEU B 1 371 ? 5.192   3.357   43.557  1.00 15.60 ? 371 LEU B C   1 
ATOM   7176 O O   . LEU B 1 371 ? 4.719   3.202   44.693  1.00 14.82 ? 371 LEU B O   1 
ATOM   7177 C CB  . LEU B 1 371 ? 4.137   4.720   41.740  1.00 13.01 ? 371 LEU B CB  1 
ATOM   7178 C CG  . LEU B 1 371 ? 2.720   4.282   42.123  1.00 17.47 ? 371 LEU B CG  1 
ATOM   7179 C CD1 . LEU B 1 371 ? 2.105   5.256   43.116  1.00 18.85 ? 371 LEU B CD1 1 
ATOM   7180 C CD2 . LEU B 1 371 ? 1.811   4.126   40.890  1.00 19.06 ? 371 LEU B CD2 1 
ATOM   7181 N N   . TYR B 1 372 ? 5.749   2.365   42.876  1.00 14.03 ? 372 TYR B N   1 
ATOM   7182 C CA  . TYR B 1 372 ? 5.713   1.011   43.421  1.00 12.83 ? 372 TYR B CA  1 
ATOM   7183 C C   . TYR B 1 372 ? 6.622   0.878   44.641  1.00 17.15 ? 372 TYR B C   1 
ATOM   7184 O O   . TYR B 1 372 ? 6.297   0.147   45.594  1.00 14.77 ? 372 TYR B O   1 
ATOM   7185 C CB  . TYR B 1 372 ? 6.128   0.039   42.323  1.00 14.03 ? 372 TYR B CB  1 
ATOM   7186 C CG  . TYR B 1 372 ? 5.120   -0.077  41.183  1.00 12.61 ? 372 TYR B CG  1 
ATOM   7187 C CD1 . TYR B 1 372 ? 3.793   0.326   41.336  1.00 13.60 ? 372 TYR B CD1 1 
ATOM   7188 C CD2 . TYR B 1 372 ? 5.508   -0.620  39.953  1.00 13.39 ? 372 TYR B CD2 1 
ATOM   7189 C CE1 . TYR B 1 372 ? 2.883   0.193   40.275  1.00 14.60 ? 372 TYR B CE1 1 
ATOM   7190 C CE2 . TYR B 1 372 ? 4.617   -0.768  38.896  1.00 13.18 ? 372 TYR B CE2 1 
ATOM   7191 C CZ  . TYR B 1 372 ? 3.307   -0.389  39.057  1.00 11.41 ? 372 TYR B CZ  1 
ATOM   7192 O OH  . TYR B 1 372 ? 2.430   -0.549  37.994  1.00 12.26 ? 372 TYR B OH  1 
ATOM   7193 N N   . SER B 1 373 ? 7.777   1.553   44.613  1.00 15.75 ? 373 SER B N   1 
ATOM   7194 C CA  . SER B 1 373 ? 8.654   1.578   45.782  1.00 17.80 ? 373 SER B CA  1 
ATOM   7195 C C   . SER B 1 373 ? 7.934   2.189   46.976  1.00 17.82 ? 373 SER B C   1 
ATOM   7196 O O   . SER B 1 373 ? 8.075   1.716   48.114  1.00 20.79 ? 373 SER B O   1 
ATOM   7197 C CB  . SER B 1 373 ? 9.928   2.373   45.469  1.00 19.46 ? 373 SER B CB  1 
ATOM   7198 O OG  . SER B 1 373 ? 10.795  2.377   46.596  1.00 29.25 ? 373 SER B OG  1 
ATOM   7199 N N   . THR B 1 374 ? 7.175   3.259   46.743  1.00 15.13 ? 374 THR B N   1 
ATOM   7200 C CA  . THR B 1 374 ? 6.480   3.904   47.848  1.00 19.52 ? 374 THR B CA  1 
ATOM   7201 C C   . THR B 1 374 ? 5.352   3.014   48.357  1.00 20.40 ? 374 THR B C   1 
ATOM   7202 O O   . THR B 1 374 ? 5.200   2.823   49.574  1.00 19.55 ? 374 THR B O   1 
ATOM   7203 C CB  . THR B 1 374 ? 5.971   5.280   47.393  1.00 21.06 ? 374 THR B CB  1 
ATOM   7204 O OG1 . THR B 1 374 ? 7.081   6.076   46.939  1.00 22.81 ? 374 THR B OG1 1 
ATOM   7205 C CG2 . THR B 1 374 ? 5.268   6.029   48.534  1.00 21.51 ? 374 THR B CG2 1 
ATOM   7206 N N   . LEU B 1 375 ? 4.587   2.419   47.434  1.00 18.80 ? 375 LEU B N   1 
ATOM   7207 C CA  . LEU B 1 375 ? 3.452   1.590   47.830  1.00 16.74 ? 375 LEU B CA  1 
ATOM   7208 C C   . LEU B 1 375 ? 3.896   0.370   48.632  1.00 19.70 ? 375 LEU B C   1 
ATOM   7209 O O   . LEU B 1 375 ? 3.230   -0.005  49.610  1.00 21.05 ? 375 LEU B O   1 
ATOM   7210 C CB  . LEU B 1 375 ? 2.654   1.153   46.599  1.00 18.31 ? 375 LEU B CB  1 
ATOM   7211 C CG  . LEU B 1 375 ? 1.836   2.267   45.934  1.00 19.75 ? 375 LEU B CG  1 
ATOM   7212 C CD1 . LEU B 1 375 ? 1.190   1.756   44.646  1.00 17.46 ? 375 LEU B CD1 1 
ATOM   7213 C CD2 . LEU B 1 375 ? 0.772   2.795   46.861  1.00 22.83 ? 375 LEU B CD2 1 
ATOM   7214 N N   . GLU B 1 376 ? 5.029   -0.250  48.251  1.00 17.65 ? 376 GLU B N   1 
ATOM   7215 C CA  . GLU B 1 376 ? 5.447   -1.490  48.903  1.00 19.78 ? 376 GLU B CA  1 
ATOM   7216 C C   . GLU B 1 376 ? 5.825   -1.254  50.351  1.00 19.67 ? 376 GLU B C   1 
ATOM   7217 O O   . GLU B 1 376 ? 5.873   -2.213  51.119  1.00 21.93 ? 376 GLU B O   1 
ATOM   7218 C CB  . GLU B 1 376 ? 6.599   -2.174  48.147  1.00 20.92 ? 376 GLU B CB  1 
ATOM   7219 C CG  . GLU B 1 376 ? 7.965   -1.562  48.269  1.00 26.33 ? 376 GLU B CG  1 
ATOM   7220 C CD  . GLU B 1 376 ? 9.033   -2.238  47.396  1.00 33.36 ? 376 GLU B CD  1 
ATOM   7221 O OE1 . GLU B 1 376 ? 8.801   -3.351  46.866  1.00 32.65 ? 376 GLU B OE1 1 
ATOM   7222 O OE2 . GLU B 1 376 ? 10.129  -1.647  47.245  1.00 34.96 ? 376 GLU B OE2 1 
ATOM   7223 N N   . LYS B 1 377 ? 6.060   -0.003  50.746  1.00 16.94 ? 377 LYS B N   1 
ATOM   7224 C CA  . LYS B 1 377 ? 6.498   0.297   52.101  1.00 17.73 ? 377 LYS B CA  1 
ATOM   7225 C C   . LYS B 1 377 ? 5.457   1.043   52.934  1.00 21.14 ? 377 LYS B C   1 
ATOM   7226 O O   . LYS B 1 377 ? 5.679   1.254   54.135  1.00 23.82 ? 377 LYS B O   1 
ATOM   7227 C CB  . LYS B 1 377 ? 7.816   1.087   52.058  1.00 20.17 ? 377 LYS B CB  1 
ATOM   7228 C CG  . LYS B 1 377 ? 8.935   0.389   51.295  1.00 23.64 ? 377 LYS B CG  1 
ATOM   7229 C CD  . LYS B 1 377 ? 10.256  1.129   51.420  1.00 29.39 ? 377 LYS B CD  1 
ATOM   7230 C CE  . LYS B 1 377 ? 11.272  0.614   50.426  1.00 31.70 ? 377 LYS B CE  1 
ATOM   7231 N NZ  . LYS B 1 377 ? 10.740  0.770   49.029  1.00 29.32 ? 377 LYS B NZ  1 
ATOM   7232 N N   . GLU B 1 378 ? 4.313   1.409   52.354  1.00 23.37 ? 378 GLU B N   1 
ATOM   7233 C CA  . GLU B 1 378 ? 3.267   2.120   53.084  1.00 27.04 ? 378 GLU B CA  1 
ATOM   7234 C C   . GLU B 1 378 ? 2.458   1.126   53.916  1.00 26.23 ? 378 GLU B C   1 
ATOM   7235 O O   . GLU B 1 378 ? 1.855   0.196   53.369  1.00 31.32 ? 378 GLU B O   1 
ATOM   7236 C CB  . GLU B 1 378 ? 2.375   2.875   52.100  1.00 35.02 ? 378 GLU B CB  1 
ATOM   7237 C CG  . GLU B 1 378 ? 1.750   4.118   52.671  1.00 44.44 ? 378 GLU B CG  1 
ATOM   7238 C CD  . GLU B 1 378 ? 2.775   5.141   53.092  1.00 51.47 ? 378 GLU B CD  1 
ATOM   7239 O OE1 . GLU B 1 378 ? 2.999   5.303   54.310  1.00 55.33 ? 378 GLU B OE1 1 
ATOM   7240 O OE2 . GLU B 1 378 ? 3.352   5.794   52.202  1.00 53.75 ? 378 GLU B OE2 1 
ATOM   7241 N N   . GLU B 1 379 ? 2.433   1.316   55.238  1.00 22.29 ? 379 GLU B N   1 
ATOM   7242 C CA  . GLU B 1 379 ? 1.898   0.253   56.081  1.00 27.72 ? 379 GLU B CA  1 
ATOM   7243 C C   . GLU B 1 379 ? 0.381   0.285   56.205  1.00 27.79 ? 379 GLU B C   1 
ATOM   7244 O O   . GLU B 1 379 ? -0.201  -0.674  56.719  1.00 35.96 ? 379 GLU B O   1 
ATOM   7245 C CB  . GLU B 1 379 ? 2.580   0.301   57.455  1.00 28.91 ? 379 GLU B CB  1 
ATOM   7246 C CG  . GLU B 1 379 ? 4.102   0.333   57.269  1.00 34.23 ? 379 GLU B CG  1 
ATOM   7247 C CD  . GLU B 1 379 ? 4.921   0.058   58.526  1.00 36.59 ? 379 GLU B CD  1 
ATOM   7248 O OE1 . GLU B 1 379 ? 6.143   -0.180  58.362  1.00 32.88 ? 379 GLU B OE1 1 
ATOM   7249 O OE2 . GLU B 1 379 ? 4.371   0.097   59.656  1.00 33.92 ? 379 GLU B OE2 1 
ATOM   7250 N N   . TRP B 1 380 ? -0.279  1.326   55.718  1.00 21.78 ? 380 TRP B N   1 
ATOM   7251 C CA  . TRP B 1 380 ? -1.732  1.399   55.781  1.00 22.55 ? 380 TRP B CA  1 
ATOM   7252 C C   . TRP B 1 380 ? -2.366  1.087   54.432  1.00 25.00 ? 380 TRP B C   1 
ATOM   7253 O O   . TRP B 1 380 ? -3.600  1.098   54.318  1.00 22.62 ? 380 TRP B O   1 
ATOM   7254 C CB  . TRP B 1 380 ? -2.163  2.788   56.282  1.00 22.26 ? 380 TRP B CB  1 
ATOM   7255 C CG  . TRP B 1 380 ? -1.512  3.907   55.520  1.00 20.99 ? 380 TRP B CG  1 
ATOM   7256 C CD1 . TRP B 1 380 ? -0.288  4.464   55.762  1.00 27.57 ? 380 TRP B CD1 1 
ATOM   7257 C CD2 . TRP B 1 380 ? -2.055  4.611   54.390  1.00 20.51 ? 380 TRP B CD2 1 
ATOM   7258 N NE1 . TRP B 1 380 ? -0.037  5.475   54.860  1.00 28.77 ? 380 TRP B NE1 1 
ATOM   7259 C CE2 . TRP B 1 380 ? -1.101  5.578   53.999  1.00 24.16 ? 380 TRP B CE2 1 
ATOM   7260 C CE3 . TRP B 1 380 ? -3.258  4.521   53.675  1.00 22.03 ? 380 TRP B CE3 1 
ATOM   7261 C CZ2 . TRP B 1 380 ? -1.310  6.449   52.917  1.00 25.81 ? 380 TRP B CZ2 1 
ATOM   7262 C CZ3 . TRP B 1 380 ? -3.457  5.379   52.588  1.00 25.66 ? 380 TRP B CZ3 1 
ATOM   7263 C CH2 . TRP B 1 380 ? -2.490  6.330   52.227  1.00 25.83 ? 380 TRP B CH2 1 
ATOM   7264 N N   . ILE B 1 381 ? -1.551  0.805   53.415  1.00 18.40 ? 381 ILE B N   1 
ATOM   7265 C CA  . ILE B 1 381 ? -2.033  0.428   52.090  1.00 21.63 ? 381 ILE B CA  1 
ATOM   7266 C C   . ILE B 1 381 ? -1.710  -1.039  51.879  1.00 22.99 ? 381 ILE B C   1 
ATOM   7267 O O   . ILE B 1 381 ? -0.574  -1.470  52.123  1.00 20.85 ? 381 ILE B O   1 
ATOM   7268 C CB  . ILE B 1 381 ? -1.398  1.271   50.966  1.00 19.50 ? 381 ILE B CB  1 
ATOM   7269 C CG1 . ILE B 1 381 ? -1.756  2.749   51.129  1.00 20.79 ? 381 ILE B CG1 1 
ATOM   7270 C CG2 . ILE B 1 381 ? -1.826  0.760   49.577  1.00 21.95 ? 381 ILE B CG2 1 
ATOM   7271 C CD1 . ILE B 1 381 ? -1.009  3.657   50.157  1.00 22.93 ? 381 ILE B CD1 1 
ATOM   7272 N N   . GLU B 1 382 ? -2.686  -1.796  51.396  1.00 19.16 ? 382 GLU B N   1 
ATOM   7273 C CA  . GLU B 1 382 ? -2.443  -3.151  50.922  1.00 16.95 ? 382 GLU B CA  1 
ATOM   7274 C C   . GLU B 1 382 ? -2.891  -3.250  49.472  1.00 15.40 ? 382 GLU B C   1 
ATOM   7275 O O   . GLU B 1 382 ? -4.085  -3.112  49.183  1.00 15.98 ? 382 GLU B O   1 
ATOM   7276 C CB  . GLU B 1 382 ? -3.187  -4.178  51.776  1.00 20.19 ? 382 GLU B CB  1 
ATOM   7277 C CG  . GLU B 1 382 ? -2.933  -5.630  51.361  1.00 35.87 ? 382 GLU B CG  1 
ATOM   7278 C CD  . GLU B 1 382 ? -3.561  -6.643  52.309  1.00 56.74 ? 382 GLU B CD  1 
ATOM   7279 O OE1 . GLU B 1 382 ? -4.001  -6.246  53.410  1.00 65.36 ? 382 GLU B OE1 1 
ATOM   7280 O OE2 . GLU B 1 382 ? -3.608  -7.842  51.952  1.00 63.67 ? 382 GLU B OE2 1 
ATOM   7281 N N   . THR B 1 383 ? -1.954  -3.527  48.564  1.00 14.44 ? 383 THR B N   1 
ATOM   7282 C CA  . THR B 1 383 ? -2.364  -3.855  47.194  1.00 15.85 ? 383 THR B CA  1 
ATOM   7283 C C   . THR B 1 383 ? -2.866  -5.294  47.120  1.00 13.28 ? 383 THR B C   1 
ATOM   7284 O O   . THR B 1 383 ? -2.384  -6.184  47.844  1.00 15.00 ? 383 THR B O   1 
ATOM   7285 C CB  . THR B 1 383 ? -1.222  -3.638  46.173  1.00 18.67 ? 383 THR B CB  1 
ATOM   7286 O OG1 . THR B 1 383 ? -0.071  -4.420  46.526  1.00 14.90 ? 383 THR B OG1 1 
ATOM   7287 C CG2 . THR B 1 383 ? -0.825  -2.193  46.171  1.00 20.19 ? 383 THR B CG2 1 
ATOM   7288 N N   . LEU B 1 384 ? -3.872  -5.521  46.255  1.00 13.31 ? 384 LEU B N   1 
ATOM   7289 C CA  . LEU B 1 384 ? -4.551  -6.818  46.175  1.00 14.15 ? 384 LEU B CA  1 
ATOM   7290 C C   . LEU B 1 384 ? -4.535  -7.364  44.752  1.00 12.65 ? 384 LEU B C   1 
ATOM   7291 O O   . LEU B 1 384 ? -4.555  -6.609  43.777  1.00 12.23 ? 384 LEU B O   1 
ATOM   7292 C CB  . LEU B 1 384 ? -6.036  -6.737  46.615  1.00 15.08 ? 384 LEU B CB  1 
ATOM   7293 C CG  . LEU B 1 384 ? -6.309  -6.186  48.016  1.00 17.59 ? 384 LEU B CG  1 
ATOM   7294 C CD1 . LEU B 1 384 ? -7.816  -6.233  48.279  1.00 18.29 ? 384 LEU B CD1 1 
ATOM   7295 C CD2 . LEU B 1 384 ? -5.575  -6.995  49.065  1.00 15.16 ? 384 LEU B CD2 1 
ATOM   7296 N N   . THR B 1 385 ? -4.531  -8.693  44.648  1.00 13.01 ? 385 THR B N   1 
ATOM   7297 C CA  . THR B 1 385 ? -4.903  -9.331  43.398  1.00 12.71 ? 385 THR B CA  1 
ATOM   7298 C C   . THR B 1 385 ? -6.413  -9.260  43.221  1.00 14.85 ? 385 THR B C   1 
ATOM   7299 O O   . THR B 1 385 ? -7.162  -9.002  44.169  1.00 15.80 ? 385 THR B O   1 
ATOM   7300 C CB  . THR B 1 385 ? -4.477  -10.809 43.365  1.00 13.30 ? 385 THR B CB  1 
ATOM   7301 O OG1 . THR B 1 385 ? -5.238  -11.534 44.338  1.00 16.14 ? 385 THR B OG1 1 
ATOM   7302 C CG2 . THR B 1 385 ? -2.947  -10.990 43.681  1.00 16.31 ? 385 THR B CG2 1 
ATOM   7303 N N   . LEU B 1 386 ? -6.868  -9.520  41.994  1.00 13.66 ? 386 LEU B N   1 
ATOM   7304 C CA  . LEU B 1 386 ? -8.315  -9.550  41.765  1.00 16.68 ? 386 LEU B CA  1 
ATOM   7305 C C   . LEU B 1 386 ? -8.969  -10.610 42.624  1.00 20.57 ? 386 LEU B C   1 
ATOM   7306 O O   . LEU B 1 386 ? -10.048 -10.386 43.190  1.00 20.90 ? 386 LEU B O   1 
ATOM   7307 C CB  . LEU B 1 386 ? -8.634  -9.802  40.285  1.00 14.70 ? 386 LEU B CB  1 
ATOM   7308 C CG  . LEU B 1 386 ? -8.083  -8.773  39.283  1.00 14.47 ? 386 LEU B CG  1 
ATOM   7309 C CD1 . LEU B 1 386 ? -8.477  -9.131  37.855  1.00 14.92 ? 386 LEU B CD1 1 
ATOM   7310 C CD2 . LEU B 1 386 ? -8.511  -7.321  39.586  1.00 16.83 ? 386 LEU B CD2 1 
ATOM   7311 N N   . GLU B 1 387 ? -8.322  -11.776 42.741  1.00 15.67 ? 387 GLU B N   1 
ATOM   7312 C CA  . GLU B 1 387 ? -8.847  -12.831 43.595  1.00 19.08 ? 387 GLU B CA  1 
ATOM   7313 C C   . GLU B 1 387 ? -8.958  -12.371 45.040  1.00 17.59 ? 387 GLU B C   1 
ATOM   7314 O O   . GLU B 1 387 ? -9.956  -12.651 45.711  1.00 21.30 ? 387 GLU B O   1 
ATOM   7315 C CB  . GLU B 1 387 ? -7.966  -14.073 43.500  1.00 23.63 ? 387 GLU B CB  1 
ATOM   7316 C CG  . GLU B 1 387 ? -8.536  -15.277 44.248  1.00 35.06 ? 387 GLU B CG  1 
ATOM   7317 C CD  . GLU B 1 387 ? -7.941  -16.592 43.783  1.00 58.67 ? 387 GLU B CD  1 
ATOM   7318 O OE1 . GLU B 1 387 ? -8.614  -17.636 43.921  1.00 69.21 ? 387 GLU B OE1 1 
ATOM   7319 O OE2 . GLU B 1 387 ? -6.799  -16.585 43.278  1.00 67.11 ? 387 GLU B OE2 1 
ATOM   7320 N N   . GLU B 1 388 ? -7.940  -11.675 45.539  1.00 21.17 ? 388 GLU B N   1 
ATOM   7321 C CA  . GLU B 1 388 ? -7.999  -11.166 46.906  1.00 18.01 ? 388 GLU B CA  1 
ATOM   7322 C C   . GLU B 1 388 ? -9.096  -10.122 47.062  1.00 21.49 ? 388 GLU B C   1 
ATOM   7323 O O   . GLU B 1 388 ? -9.785  -10.095 48.089  1.00 24.31 ? 388 GLU B O   1 
ATOM   7324 C CB  . GLU B 1 388 ? -6.639  -10.601 47.315  1.00 20.20 ? 388 GLU B CB  1 
ATOM   7325 C CG  . GLU B 1 388 ? -5.634  -11.688 47.631  1.00 24.14 ? 388 GLU B CG  1 
ATOM   7326 C CD  . GLU B 1 388 ? -4.206  -11.171 47.724  1.00 29.97 ? 388 GLU B CD  1 
ATOM   7327 O OE1 . GLU B 1 388 ? -3.930  -10.042 47.264  1.00 19.54 ? 388 GLU B OE1 1 
ATOM   7328 O OE2 . GLU B 1 388 ? -3.345  -11.903 48.267  1.00 30.10 ? 388 GLU B OE2 1 
ATOM   7329 N N   . ALA B 1 389 ? -9.282  -9.259  46.060  1.00 19.75 ? 389 ALA B N   1 
ATOM   7330 C CA  . ALA B 1 389 ? -10.347 -8.261  46.166  1.00 22.13 ? 389 ALA B CA  1 
ATOM   7331 C C   . ALA B 1 389 ? -11.722 -8.912  46.110  1.00 25.71 ? 389 ALA B C   1 
ATOM   7332 O O   . ALA B 1 389 ? -12.653 -8.466  46.803  1.00 25.21 ? 389 ALA B O   1 
ATOM   7333 C CB  . ALA B 1 389 ? -10.217 -7.209  45.071  1.00 19.66 ? 389 ALA B CB  1 
ATOM   7334 N N   . MET B 1 390 ? -11.853 -9.979  45.318  1.00 25.58 ? 390 MET B N   1 
ATOM   7335 C CA  . MET B 1 390 ? -13.127 -10.681 45.189  1.00 32.88 ? 390 MET B CA  1 
ATOM   7336 C C   . MET B 1 390 ? -13.538 -11.363 46.485  1.00 36.57 ? 390 MET B C   1 
ATOM   7337 O O   . MET B 1 390 ? -14.737 -11.426 46.794  1.00 36.69 ? 390 MET B O   1 
ATOM   7338 C CB  . MET B 1 390 ? -13.048 -11.711 44.058  1.00 29.80 ? 390 MET B CB  1 
ATOM   7339 C CG  . MET B 1 390 ? -14.383 -12.322 43.674  1.00 43.32 ? 390 MET B CG  1 
ATOM   7340 S SD  . MET B 1 390 ? -14.221 -13.649 42.459  1.00 55.20 ? 390 MET B SD  1 
ATOM   7341 C CE  . MET B 1 390 ? -13.151 -14.808 43.311  1.00 56.43 ? 390 MET B CE  1 
ATOM   7342 N N   . ARG B 1 391 ? -12.570 -11.862 47.260  1.00 33.00 ? 391 ARG B N   1 
ATOM   7343 C CA  . ARG B 1 391 ? -12.844 -12.670 48.439  1.00 33.08 ? 391 ARG B CA  1 
ATOM   7344 C C   . ARG B 1 391 ? -12.654 -11.918 49.751  1.00 30.67 ? 391 ARG B C   1 
ATOM   7345 O O   . ARG B 1 391 ? -12.849 -12.509 50.816  1.00 32.33 ? 391 ARG B O   1 
ATOM   7346 C CB  . ARG B 1 391 ? -11.943 -13.918 48.435  1.00 42.42 ? 391 ARG B CB  1 
ATOM   7347 C CG  . ARG B 1 391 ? -12.346 -15.005 47.441  1.00 54.44 ? 391 ARG B CG  1 
ATOM   7348 C CD  . ARG B 1 391 ? -12.042 -16.403 47.983  1.00 69.16 ? 391 ARG B CD  1 
ATOM   7349 N NE  . ARG B 1 391 ? -11.110 -17.155 47.147  1.00 73.16 ? 391 ARG B NE  1 
ATOM   7350 C CZ  . ARG B 1 391 ? -9.870  -17.480 47.505  1.00 75.61 ? 391 ARG B CZ  1 
ATOM   7351 N NH1 . ARG B 1 391 ? -9.393  -17.112 48.689  1.00 76.34 ? 391 ARG B NH1 1 
ATOM   7352 N NH2 . ARG B 1 391 ? -9.105  -18.177 46.677  1.00 75.14 ? 391 ARG B NH2 1 
ATOM   7353 N N   . LYS B 1 392 ? -12.278 -10.641 49.703  1.00 29.21 ? 392 LYS B N   1 
ATOM   7354 C CA  . LYS B 1 392 ? -11.937 -9.899  50.912  1.00 32.31 ? 392 LYS B CA  1 
ATOM   7355 C C   . LYS B 1 392 ? -13.162 -9.744  51.805  1.00 29.78 ? 392 LYS B C   1 
ATOM   7356 O O   . LYS B 1 392 ? -14.210 -9.262  51.362  1.00 27.25 ? 392 LYS B O   1 
ATOM   7357 C CB  . LYS B 1 392 ? -11.381 -8.528  50.529  1.00 33.64 ? 392 LYS B CB  1 
ATOM   7358 C CG  . LYS B 1 392 ? -10.593 -7.833  51.619  1.00 37.81 ? 392 LYS B CG  1 
ATOM   7359 C CD  . LYS B 1 392 ? -9.518  -8.733  52.201  1.00 45.30 ? 392 LYS B CD  1 
ATOM   7360 C CE  . LYS B 1 392 ? -8.131  -8.166  51.963  1.00 45.26 ? 392 LYS B CE  1 
ATOM   7361 N NZ  . LYS B 1 392 ? -7.087  -8.952  52.682  1.00 47.52 ? 392 LYS B NZ  1 
ATOM   7362 N N   . GLU B 1 393 ? -13.035 -10.145 53.068  1.00 29.81 ? 393 GLU B N   1 
ATOM   7363 C CA  . GLU B 1 393 ? -14.216 -10.156 53.923  1.00 35.04 ? 393 GLU B CA  1 
ATOM   7364 C C   . GLU B 1 393 ? -14.464 -8.817  54.606  1.00 35.64 ? 393 GLU B C   1 
ATOM   7365 O O   . GLU B 1 393 ? -15.617 -8.396  54.738  1.00 41.71 ? 393 GLU B O   1 
ATOM   7366 C CB  . GLU B 1 393 ? -14.082 -11.256 54.980  1.00 46.44 ? 393 GLU B CB  1 
ATOM   7367 C CG  . GLU B 1 393 ? -14.022 -12.653 54.394  1.00 60.29 ? 393 GLU B CG  1 
ATOM   7368 C CD  . GLU B 1 393 ? -13.601 -13.702 55.402  1.00 71.84 ? 393 GLU B CD  1 
ATOM   7369 O OE1 . GLU B 1 393 ? -13.061 -13.334 56.468  1.00 75.07 ? 393 GLU B OE1 1 
ATOM   7370 O OE2 . GLU B 1 393 ? -13.809 -14.902 55.119  1.00 77.02 ? 393 GLU B OE2 1 
ATOM   7371 N N   . ASP B 1 394 ? -13.407 -8.140  55.041  1.00 32.76 ? 394 ASP B N   1 
ATOM   7372 C CA  . ASP B 1 394 ? -13.539 -6.951  55.874  1.00 36.87 ? 394 ASP B CA  1 
ATOM   7373 C C   . ASP B 1 394 ? -13.733 -5.688  55.035  1.00 31.77 ? 394 ASP B C   1 
ATOM   7374 O O   . ASP B 1 394 ? -13.016 -4.701  55.210  1.00 31.61 ? 394 ASP B O   1 
ATOM   7375 C CB  . ASP B 1 394 ? -12.298 -6.819  56.771  1.00 43.87 ? 394 ASP B CB  1 
ATOM   7376 C CG  . ASP B 1 394 ? -11.003 -7.247  56.059  1.00 52.70 ? 394 ASP B CG  1 
ATOM   7377 O OD1 . ASP B 1 394 ? -11.088 -7.720  54.901  1.00 54.45 ? 394 ASP B OD1 1 
ATOM   7378 O OD2 . ASP B 1 394 ? -9.899  -7.112  56.651  1.00 51.32 ? 394 ASP B OD2 1 
ATOM   7379 N N   . VAL B 1 395 ? -14.702 -5.703  54.122  1.00 29.22 ? 395 VAL B N   1 
ATOM   7380 C CA  . VAL B 1 395 ? -15.023 -4.547  53.289  1.00 31.80 ? 395 VAL B CA  1 
ATOM   7381 C C   . VAL B 1 395 ? -16.535 -4.339  53.312  1.00 30.76 ? 395 VAL B C   1 
ATOM   7382 O O   . VAL B 1 395 ? -17.287 -5.153  53.847  1.00 33.37 ? 395 VAL B O   1 
ATOM   7383 C CB  . VAL B 1 395 ? -14.521 -4.692  51.832  1.00 30.99 ? 395 VAL B CB  1 
ATOM   7384 C CG1 . VAL B 1 395 ? -13.024 -4.958  51.803  1.00 28.54 ? 395 VAL B CG1 1 
ATOM   7385 C CG2 . VAL B 1 395 ? -15.283 -5.775  51.086  1.00 28.82 ? 395 VAL B CG2 1 
ATOM   7386 N N   . LYS B 1 396 ? -16.977 -3.228  52.728  1.00 26.62 ? 396 LYS B N   1 
ATOM   7387 C CA  . LYS B 1 396 ? -18.404 -2.934  52.650  1.00 27.74 ? 396 LYS B CA  1 
ATOM   7388 C C   . LYS B 1 396 ? -18.950 -3.307  51.280  1.00 24.76 ? 396 LYS B C   1 
ATOM   7389 O O   . LYS B 1 396 ? -18.246 -3.235  50.266  1.00 23.63 ? 396 LYS B O   1 
ATOM   7390 C CB  . LYS B 1 396 ? -18.692 -1.461  52.927  1.00 31.96 ? 396 LYS B CB  1 
ATOM   7391 C CG  . LYS B 1 396 ? -18.447 -1.072  54.362  1.00 41.98 ? 396 LYS B CG  1 
ATOM   7392 C CD  . LYS B 1 396 ? -19.748 -0.831  55.094  1.00 51.24 ? 396 LYS B CD  1 
ATOM   7393 C CE  . LYS B 1 396 ? -19.575 -1.118  56.578  1.00 59.90 ? 396 LYS B CE  1 
ATOM   7394 N NZ  . LYS B 1 396 ? -20.864 -1.452  57.249  1.00 65.50 ? 396 LYS B NZ  1 
ATOM   7395 N N   . THR B 1 397 ? -20.221 -3.709  51.262  1.00 27.43 ? 397 THR B N   1 
ATOM   7396 C CA  . THR B 1 397 ? -20.853 -4.210  50.050  1.00 27.26 ? 397 THR B CA  1 
ATOM   7397 C C   . THR B 1 397 ? -22.263 -3.651  49.926  1.00 29.26 ? 397 THR B C   1 
ATOM   7398 O O   . THR B 1 397 ? -22.870 -3.204  50.903  1.00 31.30 ? 397 THR B O   1 
ATOM   7399 C CB  . THR B 1 397 ? -20.912 -5.747  50.018  1.00 34.19 ? 397 THR B CB  1 
ATOM   7400 O OG1 . THR B 1 397 ? -21.777 -6.205  51.063  1.00 35.31 ? 397 THR B OG1 1 
ATOM   7401 C CG2 . THR B 1 397 ? -19.520 -6.362  50.213  1.00 31.58 ? 397 THR B CG2 1 
ATOM   7402 N N   . GLU B 1 398 ? -22.779 -3.694  48.699  1.00 27.55 ? 398 GLU B N   1 
ATOM   7403 C CA  . GLU B 1 398 ? -24.079 -3.134  48.361  1.00 27.56 ? 398 GLU B CA  1 
ATOM   7404 C C   . GLU B 1 398 ? -24.627 -3.936  47.193  1.00 27.89 ? 398 GLU B C   1 
ATOM   7405 O O   . GLU B 1 398 ? -23.863 -4.481  46.394  1.00 28.81 ? 398 GLU B O   1 
ATOM   7406 C CB  . GLU B 1 398 ? -23.952 -1.645  47.999  1.00 32.80 ? 398 GLU B CB  1 
ATOM   7407 C CG  . GLU B 1 398 ? -25.263 -0.885  47.804  1.00 38.54 ? 398 GLU B CG  1 
ATOM   7408 C CD  . GLU B 1 398 ? -26.125 -0.901  49.047  1.00 43.08 ? 398 GLU B CD  1 
ATOM   7409 O OE1 . GLU B 1 398 ? -25.863 -0.110  49.989  1.00 42.62 ? 398 GLU B OE1 1 
ATOM   7410 O OE2 . GLU B 1 398 ? -27.059 -1.728  49.086  1.00 46.14 ? 398 GLU B OE2 1 
ATOM   7411 N N   . VAL B 1 399 ? -25.948 -4.025  47.100  1.00 30.60 ? 399 VAL B N   1 
ATOM   7412 C CA  . VAL B 1 399 ? -26.584 -4.720  45.986  1.00 32.25 ? 399 VAL B CA  1 
ATOM   7413 C C   . VAL B 1 399 ? -27.060 -3.681  44.978  1.00 34.32 ? 399 VAL B C   1 
ATOM   7414 O O   . VAL B 1 399 ? -27.460 -2.571  45.350  1.00 38.74 ? 399 VAL B O   1 
ATOM   7415 C CB  . VAL B 1 399 ? -27.745 -5.609  46.479  1.00 33.39 ? 399 VAL B CB  1 
ATOM   7416 C CG1 . VAL B 1 399 ? -28.338 -6.403  45.328  1.00 41.99 ? 399 VAL B CG1 1 
ATOM   7417 C CG2 . VAL B 1 399 ? -27.248 -6.556  47.563  1.00 34.54 ? 399 VAL B CG2 1 
ATOM   7418 N N   . ILE B 1 400 ? -26.997 -4.026  43.697  1.00 24.84 ? 400 ILE B N   1 
ATOM   7419 C CA  . ILE B 1 400 ? -27.532 -3.187  42.634  1.00 27.60 ? 400 ILE B CA  1 
ATOM   7420 C C   . ILE B 1 400 ? -28.453 -4.044  41.768  1.00 27.42 ? 400 ILE B C   1 
ATOM   7421 O O   . ILE B 1 400 ? -28.119 -5.185  41.430  1.00 30.21 ? 400 ILE B O   1 
ATOM   7422 C CB  . ILE B 1 400 ? -26.389 -2.534  41.821  1.00 30.67 ? 400 ILE B CB  1 
ATOM   7423 C CG1 . ILE B 1 400 ? -26.887 -1.941  40.508  1.00 32.82 ? 400 ILE B CG1 1 
ATOM   7424 C CG2 . ILE B 1 400 ? -25.228 -3.498  41.595  1.00 32.76 ? 400 ILE B CG2 1 
ATOM   7425 C CD1 . ILE B 1 400 ? -25.983 -0.840  39.975  1.00 36.93 ? 400 ILE B CD1 1 
ATOM   7426 N N   . GLU B 1 401 ? -29.620 -3.499  41.416  1.00 25.64 ? 401 GLU B N   1 
ATOM   7427 C CA  . GLU B 1 401 ? -30.602 -4.250  40.639  1.00 29.69 ? 401 GLU B CA  1 
ATOM   7428 C C   . GLU B 1 401 ? -30.609 -3.914  39.151  1.00 31.43 ? 401 GLU B C   1 
ATOM   7429 O O   . GLU B 1 401 ? -31.180 -4.680  38.360  1.00 28.63 ? 401 GLU B O   1 
ATOM   7430 C CB  . GLU B 1 401 ? -32.019 -4.023  41.190  1.00 32.61 ? 401 GLU B CB  1 
ATOM   7431 C CG  . GLU B 1 401 ? -32.185 -4.283  42.684  1.00 45.05 ? 401 GLU B CG  1 
ATOM   7432 C CD  . GLU B 1 401 ? -31.767 -5.687  43.098  1.00 52.87 ? 401 GLU B CD  1 
ATOM   7433 O OE1 . GLU B 1 401 ? -31.969 -6.645  42.316  1.00 54.13 ? 401 GLU B OE1 1 
ATOM   7434 O OE2 . GLU B 1 401 ? -31.227 -5.829  44.215  1.00 55.75 ? 401 GLU B OE2 1 
ATOM   7435 N N   . SER B 1 402 ? -30.004 -2.803  38.745  1.00 25.69 ? 402 SER B N   1 
ATOM   7436 C CA  . SER B 1 402 ? -30.098 -2.375  37.355  1.00 25.02 ? 402 SER B CA  1 
ATOM   7437 C C   . SER B 1 402 ? -28.996 -1.364  37.079  1.00 25.99 ? 402 SER B C   1 
ATOM   7438 O O   . SER B 1 402 ? -28.661 -0.559  37.949  1.00 30.25 ? 402 SER B O   1 
ATOM   7439 C CB  . SER B 1 402 ? -31.481 -1.766  37.079  1.00 31.11 ? 402 SER B CB  1 
ATOM   7440 O OG  . SER B 1 402 ? -31.618 -1.369  35.727  1.00 33.92 ? 402 SER B OG  1 
ATOM   7441 N N   . VAL B 1 403 ? -28.415 -1.423  35.882  1.00 23.33 ? 403 VAL B N   1 
ATOM   7442 C CA  . VAL B 1 403 ? -27.427 -0.437  35.469  1.00 22.65 ? 403 VAL B CA  1 
ATOM   7443 C C   . VAL B 1 403 ? -27.961 0.270   34.229  1.00 26.62 ? 403 VAL B C   1 
ATOM   7444 O O   . VAL B 1 403 ? -28.779 -0.274  33.476  1.00 25.68 ? 403 VAL B O   1 
ATOM   7445 C CB  . VAL B 1 403 ? -26.024 -1.042  35.208  1.00 22.92 ? 403 VAL B CB  1 
ATOM   7446 C CG1 . VAL B 1 403 ? -25.494 -1.735  36.481  1.00 24.96 ? 403 VAL B CG1 1 
ATOM   7447 C CG2 . VAL B 1 403 ? -26.041 -2.015  34.036  1.00 19.69 ? 403 VAL B CG2 1 
ATOM   7448 N N   . LYS B 1 404 ? -27.539 1.516   34.048  1.00 22.51 ? 404 LYS B N   1 
ATOM   7449 C CA  . LYS B 1 404 ? -27.807 2.231   32.806  1.00 21.68 ? 404 LYS B CA  1 
ATOM   7450 C C   . LYS B 1 404 ? -26.640 1.955   31.870  1.00 19.84 ? 404 LYS B C   1 
ATOM   7451 O O   . LYS B 1 404 ? -25.485 2.266   32.197  1.00 21.33 ? 404 LYS B O   1 
ATOM   7452 C CB  . LYS B 1 404 ? -27.975 3.731   33.036  1.00 28.39 ? 404 LYS B CB  1 
ATOM   7453 C CG  . LYS B 1 404 ? -29.092 4.095   34.020  1.00 48.66 ? 404 LYS B CG  1 
ATOM   7454 C CD  . LYS B 1 404 ? -30.321 3.192   33.884  1.00 60.89 ? 404 LYS B CD  1 
ATOM   7455 C CE  . LYS B 1 404 ? -30.837 2.739   35.255  1.00 66.05 ? 404 LYS B CE  1 
ATOM   7456 N NZ  . LYS B 1 404 ? -31.587 1.453   35.162  1.00 67.81 ? 404 LYS B NZ  1 
ATOM   7457 N N   . ALA B 1 405 ? -26.942 1.379   30.706  1.00 18.63 ? 405 ALA B N   1 
ATOM   7458 C CA  . ALA B 1 405 ? -25.891 0.905   29.815  1.00 17.75 ? 405 ALA B CA  1 
ATOM   7459 C C   . ALA B 1 405 ? -24.991 2.050   29.391  1.00 17.90 ? 405 ALA B C   1 
ATOM   7460 O O   . ALA B 1 405 ? -25.454 3.169   29.162  1.00 21.99 ? 405 ALA B O   1 
ATOM   7461 C CB  . ALA B 1 405 ? -26.527 0.255   28.575  1.00 19.71 ? 405 ALA B CB  1 
ATOM   7462 N N   . GLY B 1 406 ? -23.703 1.762   29.255  1.00 16.41 ? 406 GLY B N   1 
ATOM   7463 C CA  . GLY B 1 406 ? -22.783 2.795   28.833  1.00 21.26 ? 406 GLY B CA  1 
ATOM   7464 C C   . GLY B 1 406 ? -21.373 2.259   28.752  1.00 17.44 ? 406 GLY B C   1 
ATOM   7465 O O   . GLY B 1 406 ? -21.142 1.045   28.789  1.00 16.33 ? 406 GLY B O   1 
ATOM   7466 N N   . THR B 1 407 ? -20.426 3.187   28.596  1.00 15.86 ? 407 THR B N   1 
ATOM   7467 C CA  . THR B 1 407 ? -18.995 2.906   28.546  1.00 13.99 ? 407 THR B CA  1 
ATOM   7468 C C   . THR B 1 407 ? -18.280 3.887   29.459  1.00 13.19 ? 407 THR B C   1 
ATOM   7469 O O   . THR B 1 407 ? -18.891 4.801   30.013  1.00 16.99 ? 407 THR B O   1 
ATOM   7470 C CB  . THR B 1 407 ? -18.379 3.052   27.140  1.00 14.53 ? 407 THR B CB  1 
ATOM   7471 O OG1 . THR B 1 407 ? -18.265 4.454   26.817  1.00 16.04 ? 407 THR B OG1 1 
ATOM   7472 C CG2 . THR B 1 407 ? -19.214 2.310   26.059  1.00 16.22 ? 407 THR B CG2 1 
ATOM   7473 N N   . TRP B 1 408 ? -16.957 3.747   29.545  1.00 15.35 ? 408 TRP B N   1 
ATOM   7474 C CA  . TRP B 1 408 ? -16.209 4.696   30.351  1.00 15.01 ? 408 TRP B CA  1 
ATOM   7475 C C   . TRP B 1 408 ? -15.956 6.002   29.611  1.00 17.21 ? 408 TRP B C   1 
ATOM   7476 O O   . TRP B 1 408 ? -15.343 6.916   30.184  1.00 20.30 ? 408 TRP B O   1 
ATOM   7477 C CB  . TRP B 1 408 ? -14.892 4.051   30.842  1.00 14.11 ? 408 TRP B CB  1 
ATOM   7478 C CG  . TRP B 1 408 ? -13.906 3.602   29.784  1.00 13.61 ? 408 TRP B CG  1 
ATOM   7479 C CD1 . TRP B 1 408 ? -13.964 3.823   28.438  1.00 13.72 ? 408 TRP B CD1 1 
ATOM   7480 C CD2 . TRP B 1 408 ? -12.679 2.917   30.031  1.00 16.60 ? 408 TRP B CD2 1 
ATOM   7481 N NE1 . TRP B 1 408 ? -12.838 3.289   27.819  1.00 14.64 ? 408 TRP B NE1 1 
ATOM   7482 C CE2 . TRP B 1 408 ? -12.039 2.721   28.786  1.00 18.14 ? 408 TRP B CE2 1 
ATOM   7483 C CE3 . TRP B 1 408 ? -12.055 2.445   31.196  1.00 15.30 ? 408 TRP B CE3 1 
ATOM   7484 C CZ2 . TRP B 1 408 ? -10.802 2.062   28.677  1.00 15.12 ? 408 TRP B CZ2 1 
ATOM   7485 C CZ3 . TRP B 1 408 ? -10.844 1.798   31.088  1.00 15.51 ? 408 TRP B CZ3 1 
ATOM   7486 C CH2 . TRP B 1 408 ? -10.229 1.601   29.838  1.00 16.13 ? 408 TRP B CH2 1 
ATOM   7487 N N   . PHE B 1 409 ? -16.428 6.136   28.367  1.00 14.46 ? 409 PHE B N   1 
ATOM   7488 C CA  . PHE B 1 409 ? -16.390 7.438   27.697  1.00 19.08 ? 409 PHE B CA  1 
ATOM   7489 C C   . PHE B 1 409 ? -17.737 8.114   27.936  1.00 24.60 ? 409 PHE B C   1 
ATOM   7490 O O   . PHE B 1 409 ? -18.724 7.823   27.261  1.00 23.04 ? 409 PHE B O   1 
ATOM   7491 C CB  . PHE B 1 409 ? -16.055 7.281   26.209  1.00 23.56 ? 409 PHE B CB  1 
ATOM   7492 C CG  . PHE B 1 409 ? -15.555 8.554   25.557  1.00 30.00 ? 409 PHE B CG  1 
ATOM   7493 C CD1 . PHE B 1 409 ? -16.298 9.703   25.604  1.00 26.59 ? 409 PHE B CD1 1 
ATOM   7494 C CD2 . PHE B 1 409 ? -14.345 8.592   24.886  1.00 39.83 ? 409 PHE B CD2 1 
ATOM   7495 C CE1 . PHE B 1 409 ? -15.856 10.866  25.014  1.00 33.85 ? 409 PHE B CE1 1 
ATOM   7496 C CE2 . PHE B 1 409 ? -13.879 9.769   24.306  1.00 39.17 ? 409 PHE B CE2 1 
ATOM   7497 C CZ  . PHE B 1 409 ? -14.645 10.902  24.368  1.00 38.03 ? 409 PHE B CZ  1 
ATOM   7498 N N   . ASP B 1 410 ? -17.776 9.015   28.918  1.00 22.03 ? 410 ASP B N   1 
ATOM   7499 C CA  . ASP B 1 410 ? -18.956 9.806   29.267  1.00 28.02 ? 410 ASP B CA  1 
ATOM   7500 C C   . ASP B 1 410 ? -20.174 8.952   29.618  1.00 25.55 ? 410 ASP B C   1 
ATOM   7501 O O   . ASP B 1 410 ? -21.298 9.463   29.652  1.00 30.31 ? 410 ASP B O   1 
ATOM   7502 C CB  . ASP B 1 410 ? -19.312 10.785  28.143  1.00 41.98 ? 410 ASP B CB  1 
ATOM   7503 C CG  . ASP B 1 410 ? -18.261 11.863  27.951  1.00 51.01 ? 410 ASP B CG  1 
ATOM   7504 O OD1 . ASP B 1 410 ? -17.393 12.019  28.836  1.00 54.50 ? 410 ASP B OD1 1 
ATOM   7505 O OD2 . ASP B 1 410 ? -18.305 12.552  26.908  1.00 55.21 ? 410 ASP B OD2 1 
ATOM   7506 N N   . GLY B 1 411 ? -19.991 7.662   29.897  1.00 17.30 ? 411 GLY B N   1 
ATOM   7507 C CA  . GLY B 1 411 ? -21.136 6.823   30.201  1.00 21.39 ? 411 GLY B CA  1 
ATOM   7508 C C   . GLY B 1 411 ? -22.029 6.476   29.020  1.00 21.60 ? 411 GLY B C   1 
ATOM   7509 O O   . GLY B 1 411 ? -23.161 6.039   29.235  1.00 22.11 ? 411 GLY B O   1 
ATOM   7510 N N   . ASN B 1 412 ? -21.560 6.642   27.777  1.00 19.74 ? 412 ASN B N   1 
ATOM   7511 C CA  . ASN B 1 412 ? -22.434 6.418   26.617  1.00 18.28 ? 412 ASN B CA  1 
ATOM   7512 C C   . ASN B 1 412 ? -21.624 5.844   25.457  1.00 18.57 ? 412 ASN B C   1 
ATOM   7513 O O   . ASN B 1 412 ? -20.420 5.592   25.571  1.00 16.85 ? 412 ASN B O   1 
ATOM   7514 C CB  . ASN B 1 412 ? -23.194 7.700   26.207  1.00 21.98 ? 412 ASN B CB  1 
ATOM   7515 C CG  . ASN B 1 412 ? -22.291 8.822   25.689  1.00 25.30 ? 412 ASN B CG  1 
ATOM   7516 O OD1 . ASN B 1 412 ? -21.438 8.636   24.813  1.00 23.04 ? 412 ASN B OD1 1 
ATOM   7517 N ND2 . ASN B 1 412 ? -22.545 10.027  26.186  1.00 27.58 ? 412 ASN B ND2 1 
ATOM   7518 N N   . PHE B 1 413 ? -22.297 5.646   24.320  1.00 19.54 ? 413 PHE B N   1 
ATOM   7519 C CA  . PHE B 1 413 ? -21.724 4.887   23.211  1.00 20.76 ? 413 PHE B CA  1 
ATOM   7520 C C   . PHE B 1 413 ? -21.333 5.745   22.007  1.00 18.95 ? 413 PHE B C   1 
ATOM   7521 O O   . PHE B 1 413 ? -21.015 5.189   20.944  1.00 16.72 ? 413 PHE B O   1 
ATOM   7522 C CB  . PHE B 1 413 ? -22.726 3.806   22.773  1.00 21.14 ? 413 PHE B CB  1 
ATOM   7523 C CG  . PHE B 1 413 ? -22.936 2.718   23.813  1.00 16.79 ? 413 PHE B CG  1 
ATOM   7524 C CD1 . PHE B 1 413 ? -22.083 1.623   23.867  1.00 15.28 ? 413 PHE B CD1 1 
ATOM   7525 C CD2 . PHE B 1 413 ? -23.998 2.786   24.711  1.00 17.59 ? 413 PHE B CD2 1 
ATOM   7526 C CE1 . PHE B 1 413 ? -22.262 0.609   24.828  1.00 16.22 ? 413 PHE B CE1 1 
ATOM   7527 C CE2 . PHE B 1 413 ? -24.191 1.776   25.671  1.00 18.73 ? 413 PHE B CE2 1 
ATOM   7528 C CZ  . PHE B 1 413 ? -23.332 0.697   25.727  1.00 16.27 ? 413 PHE B CZ  1 
ATOM   7529 N N   . LEU B 1 414 ? -21.325 7.074   22.147  1.00 19.74 ? 414 LEU B N   1 
ATOM   7530 C CA  . LEU B 1 414 ? -21.246 7.964   20.988  1.00 20.74 ? 414 LEU B CA  1 
ATOM   7531 C C   . LEU B 1 414 ? -19.901 7.884   20.268  1.00 22.41 ? 414 LEU B C   1 
ATOM   7532 O O   . LEU B 1 414 ? -19.837 8.230   19.080  1.00 24.03 ? 414 LEU B O   1 
ATOM   7533 C CB  . LEU B 1 414 ? -21.543 9.397   21.422  1.00 23.29 ? 414 LEU B CB  1 
ATOM   7534 C CG  . LEU B 1 414 ? -22.977 9.645   21.913  1.00 20.97 ? 414 LEU B CG  1 
ATOM   7535 C CD1 . LEU B 1 414 ? -23.159 11.108  22.294  1.00 24.97 ? 414 LEU B CD1 1 
ATOM   7536 C CD2 . LEU B 1 414 ? -23.977 9.242   20.838  1.00 24.95 ? 414 LEU B CD2 1 
ATOM   7537 N N   . LYS B 1 415 ? -18.839 7.413   20.934  1.00 17.33 ? 415 LYS B N   1 
ATOM   7538 C CA  . LYS B 1 415 ? -17.561 7.279   20.233  1.00 15.91 ? 415 LYS B CA  1 
ATOM   7539 C C   . LYS B 1 415 ? -17.540 6.103   19.265  1.00 16.68 ? 415 LYS B C   1 
ATOM   7540 O O   . LYS B 1 415 ? -16.573 5.966   18.511  1.00 18.39 ? 415 LYS B O   1 
ATOM   7541 C CB  . LYS B 1 415 ? -16.399 7.143   21.221  1.00 17.68 ? 415 LYS B CB  1 
ATOM   7542 C CG  . LYS B 1 415 ? -16.163 8.401   22.021  1.00 26.17 ? 415 LYS B CG  1 
ATOM   7543 C CD  . LYS B 1 415 ? -15.789 9.572   21.130  1.00 27.86 ? 415 LYS B CD  1 
ATOM   7544 C CE  . LYS B 1 415 ? -14.309 9.528   20.790  1.00 33.51 ? 415 LYS B CE  1 
ATOM   7545 N NZ  . LYS B 1 415 ? -13.940 10.546  19.770  1.00 41.48 ? 415 LYS B NZ  1 
ATOM   7546 N N   . TRP B 1 416 ? -18.582 5.269   19.240  1.00 17.44 ? 416 TRP B N   1 
ATOM   7547 C CA  . TRP B 1 416 ? -18.572 4.097   18.369  1.00 14.84 ? 416 TRP B CA  1 
ATOM   7548 C C   . TRP B 1 416 ? -19.780 4.005   17.463  1.00 15.79 ? 416 TRP B C   1 
ATOM   7549 O O   . TRP B 1 416 ? -19.793 3.130   16.592  1.00 18.72 ? 416 TRP B O   1 
ATOM   7550 C CB  . TRP B 1 416 ? -18.473 2.793   19.186  1.00 14.74 ? 416 TRP B CB  1 
ATOM   7551 C CG  . TRP B 1 416 ? -17.224 2.780   20.045  1.00 16.05 ? 416 TRP B CG  1 
ATOM   7552 C CD1 . TRP B 1 416 ? -15.971 2.334   19.688  1.00 15.36 ? 416 TRP B CD1 1 
ATOM   7553 C CD2 . TRP B 1 416 ? -17.099 3.345   21.354  1.00 14.68 ? 416 TRP B CD2 1 
ATOM   7554 N NE1 . TRP B 1 416 ? -15.081 2.562   20.731  1.00 15.65 ? 416 TRP B NE1 1 
ATOM   7555 C CE2 . TRP B 1 416 ? -15.754 3.189   21.756  1.00 15.99 ? 416 TRP B CE2 1 
ATOM   7556 C CE3 . TRP B 1 416 ? -18.009 3.963   22.237  1.00 15.73 ? 416 TRP B CE3 1 
ATOM   7557 C CZ2 . TRP B 1 416 ? -15.293 3.616   23.018  1.00 17.68 ? 416 TRP B CZ2 1 
ATOM   7558 C CZ3 . TRP B 1 416 ? -17.554 4.379   23.489  1.00 15.38 ? 416 TRP B CZ3 1 
ATOM   7559 C CH2 . TRP B 1 416 ? -16.209 4.204   23.863  1.00 17.62 ? 416 TRP B CH2 1 
ATOM   7560 N N   . ILE B 1 417 ? -20.786 4.858   17.650  1.00 18.03 ? 417 ILE B N   1 
ATOM   7561 C CA  . ILE B 1 417 ? -22.022 4.777   16.887  1.00 20.08 ? 417 ILE B CA  1 
ATOM   7562 C C   . ILE B 1 417 ? -22.687 6.141   16.966  1.00 22.43 ? 417 ILE B C   1 
ATOM   7563 O O   . ILE B 1 417 ? -22.495 6.881   17.929  1.00 21.98 ? 417 ILE B O   1 
ATOM   7564 C CB  . ILE B 1 417 ? -22.925 3.643   17.441  1.00 20.97 ? 417 ILE B CB  1 
ATOM   7565 C CG1 . ILE B 1 417 ? -24.069 3.304   16.466  1.00 21.70 ? 417 ILE B CG1 1 
ATOM   7566 C CG2 . ILE B 1 417 ? -23.504 4.019   18.824  1.00 21.16 ? 417 ILE B CG2 1 
ATOM   7567 C CD1 . ILE B 1 417 ? -24.586 1.893   16.666  1.00 25.28 ? 417 ILE B CD1 1 
ATOM   7568 N N   . GLY B 1 418 ? -23.481 6.479   15.949  1.00 26.88 ? 418 GLY B N   1 
ATOM   7569 C CA  . GLY B 1 418 ? -24.364 7.630   16.011  1.00 28.49 ? 418 GLY B CA  1 
ATOM   7570 C C   . GLY B 1 418 ? -24.109 8.725   14.995  1.00 34.81 ? 418 GLY B C   1 
ATOM   7571 O O   . GLY B 1 418 ? -25.021 9.520   14.737  1.00 45.87 ? 418 GLY B O   1 
ATOM   7572 N N   . ASN B 1 419 ? -22.915 8.837   14.429  1.00 32.32 ? 419 ASN B N   1 
ATOM   7573 C CA  . ASN B 1 419 ? -22.728 9.770   13.328  1.00 34.05 ? 419 ASN B CA  1 
ATOM   7574 C C   . ASN B 1 419 ? -22.729 9.001   12.008  1.00 30.80 ? 419 ASN B C   1 
ATOM   7575 O O   . ASN B 1 419 ? -22.727 7.770   11.984  1.00 27.83 ? 419 ASN B O   1 
ATOM   7576 C CB  . ASN B 1 419 ? -21.464 10.637  13.525  1.00 34.85 ? 419 ASN B CB  1 
ATOM   7577 C CG  . ASN B 1 419 ? -20.136 9.887   13.341  1.00 36.41 ? 419 ASN B CG  1 
ATOM   7578 O OD1 . ASN B 1 419 ? -20.064 8.808   12.762  1.00 34.00 ? 419 ASN B OD1 1 
ATOM   7579 N ND2 . ASN B 1 419 ? -19.058 10.515  13.808  1.00 36.07 ? 419 ASN B ND2 1 
ATOM   7580 N N   . LYS B 1 420 ? -22.762 9.739   10.894  1.00 31.70 ? 420 LYS B N   1 
ATOM   7581 C CA  . LYS B 1 420 ? -22.963 9.074   9.608   1.00 30.56 ? 420 LYS B CA  1 
ATOM   7582 C C   . LYS B 1 420 ? -21.846 8.075   9.320   1.00 31.52 ? 420 LYS B C   1 
ATOM   7583 O O   . LYS B 1 420 ? -22.115 6.944   8.898   1.00 29.62 ? 420 LYS B O   1 
ATOM   7584 C CB  . LYS B 1 420 ? -23.093 10.115  8.487   1.00 37.43 ? 420 LYS B CB  1 
ATOM   7585 C CG  . LYS B 1 420 ? -22.813 9.624   7.054   1.00 50.22 ? 420 LYS B CG  1 
ATOM   7586 C CD  . LYS B 1 420 ? -23.505 8.314   6.696   1.00 55.05 ? 420 LYS B CD  1 
ATOM   7587 C CE  . LYS B 1 420 ? -23.671 8.069   5.218   1.00 56.93 ? 420 LYS B CE  1 
ATOM   7588 N NZ  . LYS B 1 420 ? -24.985 8.581   4.792   1.00 60.99 ? 420 LYS B NZ  1 
ATOM   7589 N N   . GLU B 1 421 ? -20.589 8.454   9.570   1.00 28.60 ? 421 GLU B N   1 
ATOM   7590 C CA  . GLU B 1 421 ? -19.488 7.572   9.186   1.00 29.97 ? 421 GLU B CA  1 
ATOM   7591 C C   . GLU B 1 421 ? -19.409 6.336   10.080  1.00 25.15 ? 421 GLU B C   1 
ATOM   7592 O O   . GLU B 1 421 ? -19.198 5.228   9.580   1.00 23.87 ? 421 GLU B O   1 
ATOM   7593 C CB  . GLU B 1 421 ? -18.163 8.335   9.196   1.00 36.99 ? 421 GLU B CB  1 
ATOM   7594 C CG  . GLU B 1 421 ? -18.017 9.356   8.078   1.00 44.53 ? 421 GLU B CG  1 
ATOM   7595 C CD  . GLU B 1 421 ? -18.762 10.646  8.372   1.00 57.49 ? 421 GLU B CD  1 
ATOM   7596 O OE1 . GLU B 1 421 ? -19.028 10.930  9.562   1.00 59.29 ? 421 GLU B OE1 1 
ATOM   7597 O OE2 . GLU B 1 421 ? -19.086 11.377  7.412   1.00 65.20 ? 421 GLU B OE2 1 
ATOM   7598 N N   . LYS B 1 422 ? -19.570 6.492   11.400  1.00 22.03 ? 422 LYS B N   1 
ATOM   7599 C CA  . LYS B 1 422 ? -19.573 5.304   12.252  1.00 18.80 ? 422 LYS B CA  1 
ATOM   7600 C C   . LYS B 1 422 ? -20.776 4.423   11.941  1.00 18.81 ? 422 LYS B C   1 
ATOM   7601 O O   . LYS B 1 422 ? -20.647 3.187   11.883  1.00 21.14 ? 422 LYS B O   1 
ATOM   7602 C CB  . LYS B 1 422 ? -19.561 5.692   13.734  1.00 22.03 ? 422 LYS B CB  1 
ATOM   7603 C CG  . LYS B 1 422 ? -18.236 6.289   14.191  1.00 22.46 ? 422 LYS B CG  1 
ATOM   7604 C CD  . LYS B 1 422 ? -18.335 6.863   15.606  1.00 21.43 ? 422 LYS B CD  1 
ATOM   7605 C CE  . LYS B 1 422 ? -17.181 7.817   15.870  1.00 20.96 ? 422 LYS B CE  1 
ATOM   7606 N NZ  . LYS B 1 422 ? -15.876 7.066   15.953  1.00 17.77 ? 422 LYS B NZ  1 
ATOM   7607 N N   . ASN B 1 423 ? -21.948 5.045   11.699  1.00 19.84 ? 423 ASN B N   1 
ATOM   7608 C CA  . ASN B 1 423 ? -23.121 4.258   11.334  1.00 19.25 ? 423 ASN B CA  1 
ATOM   7609 C C   . ASN B 1 423 ? -22.900 3.491   10.035  1.00 22.98 ? 423 ASN B C   1 
ATOM   7610 O O   . ASN B 1 423 ? -23.421 2.382   9.873   1.00 22.83 ? 423 ASN B O   1 
ATOM   7611 C CB  . ASN B 1 423 ? -24.358 5.151   11.235  1.00 20.38 ? 423 ASN B CB  1 
ATOM   7612 C CG  . ASN B 1 423 ? -24.911 5.508   12.599  1.00 22.53 ? 423 ASN B CG  1 
ATOM   7613 O OD1 . ASN B 1 423 ? -24.355 5.095   13.634  1.00 24.26 ? 423 ASN B OD1 1 
ATOM   7614 N ND2 . ASN B 1 423 ? -26.011 6.273   12.620  1.00 23.98 ? 423 ASN B ND2 1 
ATOM   7615 N N   . GLU B 1 424 ? -22.116 4.048   9.105   1.00 23.74 ? 424 GLU B N   1 
ATOM   7616 C CA  . GLU B 1 424 ? -21.815 3.324   7.871   1.00 25.90 ? 424 GLU B CA  1 
ATOM   7617 C C   . GLU B 1 424 ? -21.087 2.008   8.153   1.00 19.89 ? 424 GLU B C   1 
ATOM   7618 O O   . GLU B 1 424 ? -21.362 0.988   7.507   1.00 22.02 ? 424 GLU B O   1 
ATOM   7619 C CB  . GLU B 1 424 ? -20.991 4.218   6.939   1.00 30.26 ? 424 GLU B CB  1 
ATOM   7620 C CG  . GLU B 1 424 ? -20.645 3.584   5.604   1.00 41.30 ? 424 GLU B CG  1 
ATOM   7621 C CD  . GLU B 1 424 ? -21.873 3.346   4.736   1.00 59.23 ? 424 GLU B CD  1 
ATOM   7622 O OE1 . GLU B 1 424 ? -22.346 2.190   4.658   1.00 61.70 ? 424 GLU B OE1 1 
ATOM   7623 O OE2 . GLU B 1 424 ? -22.370 4.324   4.139   1.00 67.70 ? 424 GLU B OE2 1 
ATOM   7624 N N   . TYR B 1 425 ? -20.135 2.014   9.096   1.00 22.47 ? 425 TYR B N   1 
ATOM   7625 C CA  . TYR B 1 425 ? -19.449 0.780   9.465   1.00 19.46 ? 425 TYR B CA  1 
ATOM   7626 C C   . TYR B 1 425 ? -20.415 -0.252  10.009  1.00 17.65 ? 425 TYR B C   1 
ATOM   7627 O O   . TYR B 1 425 ? -20.344 -1.429  9.637   1.00 19.60 ? 425 TYR B O   1 
ATOM   7628 C CB  . TYR B 1 425 ? -18.359 1.041   10.508  1.00 18.39 ? 425 TYR B CB  1 
ATOM   7629 C CG  . TYR B 1 425 ? -16.987 1.296   9.944   1.00 17.73 ? 425 TYR B CG  1 
ATOM   7630 C CD1 . TYR B 1 425 ? -16.808 1.766   8.640   1.00 21.73 ? 425 TYR B CD1 1 
ATOM   7631 C CD2 . TYR B 1 425 ? -15.870 1.071   10.725  1.00 17.12 ? 425 TYR B CD2 1 
ATOM   7632 C CE1 . TYR B 1 425 ? -15.515 2.000   8.136   1.00 19.46 ? 425 TYR B CE1 1 
ATOM   7633 C CE2 . TYR B 1 425 ? -14.614 1.305   10.255  1.00 17.35 ? 425 TYR B CE2 1 
ATOM   7634 C CZ  . TYR B 1 425 ? -14.432 1.771   8.970   1.00 17.21 ? 425 TYR B CZ  1 
ATOM   7635 O OH  . TYR B 1 425 ? -13.140 1.985   8.528   1.00 21.06 ? 425 TYR B OH  1 
ATOM   7636 N N   . TRP B 1 426 ? -21.321 0.164   10.907  1.00 17.29 ? 426 TRP B N   1 
ATOM   7637 C CA  . TRP B 1 426 ? -22.306 -0.774  11.424  1.00 18.76 ? 426 TRP B CA  1 
ATOM   7638 C C   . TRP B 1 426 ? -23.177 -1.320  10.295  1.00 18.23 ? 426 TRP B C   1 
ATOM   7639 O O   . TRP B 1 426 ? -23.446 -2.528  10.238  1.00 19.38 ? 426 TRP B O   1 
ATOM   7640 C CB  . TRP B 1 426 ? -23.161 -0.103  12.507  1.00 17.82 ? 426 TRP B CB  1 
ATOM   7641 C CG  . TRP B 1 426 ? -22.407 0.078   13.804  1.00 18.94 ? 426 TRP B CG  1 
ATOM   7642 C CD1 . TRP B 1 426 ? -21.885 1.236   14.291  1.00 16.28 ? 426 TRP B CD1 1 
ATOM   7643 C CD2 . TRP B 1 426 ? -22.101 -0.934  14.765  1.00 17.31 ? 426 TRP B CD2 1 
ATOM   7644 N NE1 . TRP B 1 426 ? -21.273 1.019   15.502  1.00 17.25 ? 426 TRP B NE1 1 
ATOM   7645 C CE2 . TRP B 1 426 ? -21.380 -0.309  15.817  1.00 18.33 ? 426 TRP B CE2 1 
ATOM   7646 C CE3 . TRP B 1 426 ? -22.351 -2.311  14.839  1.00 19.26 ? 426 TRP B CE3 1 
ATOM   7647 C CZ2 . TRP B 1 426 ? -20.907 -1.014  16.936  1.00 21.61 ? 426 TRP B CZ2 1 
ATOM   7648 C CZ3 . TRP B 1 426 ? -21.893 -3.010  15.959  1.00 19.51 ? 426 TRP B CZ3 1 
ATOM   7649 C CH2 . TRP B 1 426 ? -21.173 -2.360  16.988  1.00 17.68 ? 426 TRP B CH2 1 
ATOM   7650 N N   . LYS B 1 427 ? -23.612 -0.456  9.370   1.00 19.05 ? 427 LYS B N   1 
ATOM   7651 C CA  . LYS B 1 427 ? -24.407 -0.946  8.242   1.00 22.12 ? 427 LYS B CA  1 
ATOM   7652 C C   . LYS B 1 427 ? -23.632 -1.966  7.417   1.00 20.00 ? 427 LYS B C   1 
ATOM   7653 O O   . LYS B 1 427 ? -24.207 -2.967  6.964   1.00 22.64 ? 427 LYS B O   1 
ATOM   7654 C CB  . LYS B 1 427 ? -24.849 0.197   7.335   1.00 27.67 ? 427 LYS B CB  1 
ATOM   7655 C CG  . LYS B 1 427 ? -25.852 1.144   7.934   1.00 41.70 ? 427 LYS B CG  1 
ATOM   7656 C CD  . LYS B 1 427 ? -26.538 1.985   6.899   1.00 51.78 ? 427 LYS B CD  1 
ATOM   7657 C CE  . LYS B 1 427 ? -27.894 2.502   7.422   1.00 55.64 ? 427 LYS B CE  1 
ATOM   7658 N NZ  . LYS B 1 427 ? -28.881 1.593   8.160   1.00 55.65 ? 427 LYS B NZ  1 
ATOM   7659 N N   . ILE B 1 428 ? -22.330 -1.715  7.194   1.00 20.08 ? 428 ILE B N   1 
ATOM   7660 C CA  . ILE B 1 428 ? -21.497 -2.666  6.462   1.00 20.26 ? 428 ILE B CA  1 
ATOM   7661 C C   . ILE B 1 428 ? -21.415 -3.984  7.215   1.00 19.12 ? 428 ILE B C   1 
ATOM   7662 O O   . ILE B 1 428 ? -21.536 -5.067  6.621   1.00 20.06 ? 428 ILE B O   1 
ATOM   7663 C CB  . ILE B 1 428 ? -20.097 -2.067  6.222   1.00 24.00 ? 428 ILE B CB  1 
ATOM   7664 C CG1 . ILE B 1 428 ? -20.153 -0.990  5.135   1.00 23.32 ? 428 ILE B CG1 1 
ATOM   7665 C CG2 . ILE B 1 428 ? -19.084 -3.156  5.900   1.00 22.15 ? 428 ILE B CG2 1 
ATOM   7666 C CD1 . ILE B 1 428 ? -18.979 -0.022  5.235   1.00 29.03 ? 428 ILE B CD1 1 
ATOM   7667 N N   . LEU B 1 429 ? -21.233 -3.909  8.537   1.00 19.82 ? 429 LEU B N   1 
ATOM   7668 C CA  . LEU B 1 429 ? -21.154 -5.108  9.362   1.00 21.14 ? 429 LEU B CA  1 
ATOM   7669 C C   . LEU B 1 429 ? -22.473 -5.868  9.359   1.00 20.77 ? 429 LEU B C   1 
ATOM   7670 O O   . LEU B 1 429 ? -22.483 -7.102  9.266   1.00 22.17 ? 429 LEU B O   1 
ATOM   7671 C CB  . LEU B 1 429 ? -20.753 -4.719  10.794  1.00 17.78 ? 429 LEU B CB  1 
ATOM   7672 C CG  . LEU B 1 429 ? -20.645 -5.889  11.774  1.00 20.19 ? 429 LEU B CG  1 
ATOM   7673 C CD1 . LEU B 1 429 ? -19.364 -6.677  11.508  1.00 22.33 ? 429 LEU B CD1 1 
ATOM   7674 C CD2 . LEU B 1 429 ? -20.720 -5.402  13.247  1.00 19.58 ? 429 LEU B CD2 1 
ATOM   7675 N N   . ILE B 1 430 ? -23.601 -5.150  9.453   1.00 19.23 ? 430 ILE B N   1 
ATOM   7676 C CA  . ILE B 1 430 ? -24.909 -5.797  9.441   1.00 22.97 ? 430 ILE B CA  1 
ATOM   7677 C C   . ILE B 1 430 ? -25.114 -6.547  8.130   1.00 21.92 ? 430 ILE B C   1 
ATOM   7678 O O   . ILE B 1 430 ? -25.548 -7.706  8.113   1.00 21.19 ? 430 ILE B O   1 
ATOM   7679 C CB  . ILE B 1 430 ? -26.015 -4.749  9.687   1.00 23.24 ? 430 ILE B CB  1 
ATOM   7680 C CG1 . ILE B 1 430 ? -26.001 -4.266  11.145  1.00 20.48 ? 430 ILE B CG1 1 
ATOM   7681 C CG2 . ILE B 1 430 ? -27.408 -5.300  9.304   1.00 23.31 ? 430 ILE B CG2 1 
ATOM   7682 C CD1 . ILE B 1 430 ? -26.468 -2.818  11.334  1.00 21.98 ? 430 ILE B CD1 1 
ATOM   7683 N N   . GLU B 1 431 ? -24.774 -5.908  7.011   1.00 22.62 ? 431 GLU B N   1 
ATOM   7684 C CA  . GLU B 1 431 ? -24.981 -6.536  5.712   1.00 24.71 ? 431 GLU B CA  1 
ATOM   7685 C C   . GLU B 1 431 ? -24.047 -7.729  5.525   1.00 24.36 ? 431 GLU B C   1 
ATOM   7686 O O   . GLU B 1 431 ? -24.457 -8.767  4.989   1.00 29.33 ? 431 GLU B O   1 
ATOM   7687 C CB  . GLU B 1 431 ? -24.786 -5.496  4.607   1.00 31.62 ? 431 GLU B CB  1 
ATOM   7688 C CG  . GLU B 1 431 ? -25.328 -5.910  3.253   1.00 46.03 ? 431 GLU B CG  1 
ATOM   7689 C CD  . GLU B 1 431 ? -26.706 -6.546  3.354   1.00 52.48 ? 431 GLU B CD  1 
ATOM   7690 O OE1 . GLU B 1 431 ? -27.641 -5.874  3.841   1.00 53.77 ? 431 GLU B OE1 1 
ATOM   7691 O OE2 . GLU B 1 431 ? -26.845 -7.723  2.959   1.00 54.27 ? 431 GLU B OE2 1 
ATOM   7692 N N   . ALA B 1 432 ? -22.801 -7.625  6.010   1.00 21.34 ? 432 ALA B N   1 
ATOM   7693 C CA  . ALA B 1 432 ? -21.880 -8.749  5.875   1.00 25.60 ? 432 ALA B CA  1 
ATOM   7694 C C   . ALA B 1 432 ? -22.293 -9.917  6.764   1.00 26.67 ? 432 ALA B C   1 
ATOM   7695 O O   . ALA B 1 432 ? -22.150 -11.083 6.377   1.00 26.71 ? 432 ALA B O   1 
ATOM   7696 C CB  . ALA B 1 432 ? -20.457 -8.310  6.207   1.00 25.19 ? 432 ALA B CB  1 
ATOM   7697 N N   . LYS B 1 433 ? -22.807 -9.621  7.957   1.00 25.31 ? 433 LYS B N   1 
ATOM   7698 C CA  . LYS B 1 433 ? -23.249 -10.670 8.866   1.00 23.92 ? 433 LYS B CA  1 
ATOM   7699 C C   . LYS B 1 433 ? -24.362 -11.524 8.260   1.00 26.60 ? 433 LYS B C   1 
ATOM   7700 O O   . LYS B 1 433 ? -24.422 -12.730 8.523   1.00 25.25 ? 433 LYS B O   1 
ATOM   7701 C CB  . LYS B 1 433 ? -23.702 -10.042 10.186  1.00 25.65 ? 433 LYS B CB  1 
ATOM   7702 C CG  . LYS B 1 433 ? -24.351 -10.999 11.171  1.00 25.42 ? 433 LYS B CG  1 
ATOM   7703 C CD  . LYS B 1 433 ? -23.359 -11.953 11.792  1.00 24.48 ? 433 LYS B CD  1 
ATOM   7704 C CE  . LYS B 1 433 ? -24.068 -13.028 12.603  1.00 28.01 ? 433 LYS B CE  1 
ATOM   7705 N NZ  . LYS B 1 433 ? -23.101 -14.061 13.095  1.00 28.92 ? 433 LYS B NZ  1 
ATOM   7706 N N   . LYS B 1 434 ? -25.236 -10.930 7.434   1.00 28.30 ? 434 LYS B N   1 
ATOM   7707 C CA  . LYS B 1 434 ? -26.281 -11.710 6.769   1.00 30.69 ? 434 LYS B CA  1 
ATOM   7708 C C   . LYS B 1 434 ? -25.703 -12.858 5.950   1.00 34.03 ? 434 LYS B C   1 
ATOM   7709 O O   . LYS B 1 434 ? -26.351 -13.902 5.799   1.00 34.52 ? 434 LYS B O   1 
ATOM   7710 C CB  . LYS B 1 434 ? -27.124 -10.817 5.851   1.00 33.58 ? 434 LYS B CB  1 
ATOM   7711 C CG  . LYS B 1 434 ? -27.934 -9.756  6.558   1.00 41.62 ? 434 LYS B CG  1 
ATOM   7712 C CD  . LYS B 1 434 ? -28.796 -8.927  5.614   1.00 49.31 ? 434 LYS B CD  1 
ATOM   7713 C CE  . LYS B 1 434 ? -29.590 -7.882  6.386   1.00 52.54 ? 434 LYS B CE  1 
ATOM   7714 N NZ  . LYS B 1 434 ? -30.172 -6.841  5.495   1.00 54.13 ? 434 LYS B NZ  1 
ATOM   7715 N N   . LYS B 1 435 ? -24.502 -12.682 5.393   1.00 28.49 ? 435 LYS B N   1 
ATOM   7716 C CA  . LYS B 1 435 ? -23.894 -13.696 4.538   1.00 32.40 ? 435 LYS B CA  1 
ATOM   7717 C C   . LYS B 1 435 ? -22.547 -14.166 5.077   1.00 34.82 ? 435 LYS B C   1 
ATOM   7718 O O   . LYS B 1 435 ? -21.724 -14.684 4.311   1.00 34.09 ? 435 LYS B O   1 
ATOM   7719 C CB  . LYS B 1 435 ? -23.744 -13.175 3.107   1.00 42.56 ? 435 LYS B CB  1 
ATOM   7720 C CG  . LYS B 1 435 ? -23.831 -11.658 2.955   1.00 47.01 ? 435 LYS B CG  1 
ATOM   7721 C CD  . LYS B 1 435 ? -24.186 -11.282 1.518   1.00 52.09 ? 435 LYS B CD  1 
ATOM   7722 C CE  . LYS B 1 435 ? -23.760 -9.860  1.177   1.00 57.62 ? 435 LYS B CE  1 
ATOM   7723 N NZ  . LYS B 1 435 ? -24.164 -9.472  -0.209  1.00 62.46 ? 435 LYS B NZ  1 
ATOM   7724 N N   . ALA B 1 436 ? -22.313 -14.012 6.379   1.00 29.82 ? 436 ALA B N   1 
ATOM   7725 C CA  . ALA B 1 436 ? -21.027 -14.385 6.954   1.00 30.01 ? 436 ALA B CA  1 
ATOM   7726 C C   . ALA B 1 436 ? -20.869 -15.898 6.944   1.00 33.96 ? 436 ALA B C   1 
ATOM   7727 O O   . ALA B 1 436 ? -21.841 -16.637 7.107   1.00 34.37 ? 436 ALA B O   1 
ATOM   7728 C CB  . ALA B 1 436 ? -20.901 -13.843 8.380   1.00 27.12 ? 436 ALA B CB  1 
ATOM   7729 N N   . LYS B 1 437 ? -19.632 -16.362 6.731   1.00 32.42 ? 437 LYS B N   1 
ATOM   7730 C CA  . LYS B 1 437 ? -19.354 -17.792 6.638   1.00 31.34 ? 437 LYS B CA  1 
ATOM   7731 C C   . LYS B 1 437 ? -18.226 -18.260 7.552   1.00 34.48 ? 437 LYS B C   1 
ATOM   7732 O O   . LYS B 1 437 ? -17.973 -19.468 7.620   1.00 38.41 ? 437 LYS B O   1 
ATOM   7733 C CB  . LYS B 1 437 ? -19.021 -18.181 5.192   1.00 34.13 ? 437 LYS B CB  1 
ATOM   7734 C CG  . LYS B 1 437 ? -20.040 -17.670 4.173   1.00 42.06 ? 437 LYS B CG  1 
ATOM   7735 C CD  . LYS B 1 437 ? -19.862 -18.325 2.824   1.00 53.15 ? 437 LYS B CD  1 
ATOM   7736 C CE  . LYS B 1 437 ? -20.806 -19.506 2.664   1.00 60.96 ? 437 LYS B CE  1 
ATOM   7737 N NZ  . LYS B 1 437 ? -22.239 -19.086 2.675   1.00 62.58 ? 437 LYS B NZ  1 
ATOM   7738 N N   . ASN B 1 438 ? -17.568 -17.360 8.273   1.00 29.24 ? 438 ASN B N   1 
ATOM   7739 C CA  . ASN B 1 438 ? -16.459 -17.742 9.133   1.00 27.93 ? 438 ASN B CA  1 
ATOM   7740 C C   . ASN B 1 438 ? -16.300 -16.686 10.218  1.00 31.00 ? 438 ASN B C   1 
ATOM   7741 O O   . ASN B 1 438 ? -16.989 -15.660 10.218  1.00 34.25 ? 438 ASN B O   1 
ATOM   7742 C CB  . ASN B 1 438 ? -15.181 -17.933 8.310   1.00 30.53 ? 438 ASN B CB  1 
ATOM   7743 C CG  . ASN B 1 438 ? -14.795 -16.689 7.531   1.00 28.92 ? 438 ASN B CG  1 
ATOM   7744 O OD1 . ASN B 1 438 ? -14.519 -15.646 8.111   1.00 28.93 ? 438 ASN B OD1 1 
ATOM   7745 N ND2 . ASN B 1 438 ? -14.751 -16.803 6.211   1.00 28.48 ? 438 ASN B ND2 1 
ATOM   7746 N N   . ASP B 1 439 ? -15.364 -16.936 11.137  1.00 27.43 ? 439 ASP B N   1 
ATOM   7747 C CA  . ASP B 1 439 ? -15.181 -16.102 12.321  1.00 27.63 ? 439 ASP B CA  1 
ATOM   7748 C C   . ASP B 1 439 ? -14.476 -14.780 12.046  1.00 23.44 ? 439 ASP B C   1 
ATOM   7749 O O   . ASP B 1 439 ? -14.253 -14.016 12.993  1.00 22.32 ? 439 ASP B O   1 
ATOM   7750 C CB  . ASP B 1 439 ? -14.412 -16.873 13.399  1.00 32.13 ? 439 ASP B CB  1 
ATOM   7751 C CG  . ASP B 1 439 ? -15.299 -17.862 14.146  1.00 40.10 ? 439 ASP B CG  1 
ATOM   7752 O OD1 . ASP B 1 439 ? -16.516 -17.907 13.865  1.00 41.24 ? 439 ASP B OD1 1 
ATOM   7753 O OD2 . ASP B 1 439 ? -14.782 -18.590 15.017  1.00 46.81 ? 439 ASP B OD2 1 
ATOM   7754 N N   . TYR B 1 440 ? -14.124 -14.474 10.790  1.00 24.81 ? 440 TYR B N   1 
ATOM   7755 C CA  . TYR B 1 440 ? -13.646 -13.123 10.526  1.00 21.65 ? 440 TYR B CA  1 
ATOM   7756 C C   . TYR B 1 440 ? -14.734 -12.079 10.771  1.00 23.62 ? 440 TYR B C   1 
ATOM   7757 O O   . TYR B 1 440 ? -14.412 -10.906 11.012  1.00 19.35 ? 440 TYR B O   1 
ATOM   7758 C CB  . TYR B 1 440 ? -13.080 -13.027 9.104   1.00 18.93 ? 440 TYR B CB  1 
ATOM   7759 C CG  . TYR B 1 440 ? -11.609 -13.371 9.061   1.00 23.73 ? 440 TYR B CG  1 
ATOM   7760 C CD1 . TYR B 1 440 ? -10.676 -12.523 9.631   1.00 28.64 ? 440 TYR B CD1 1 
ATOM   7761 C CD2 . TYR B 1 440 ? -11.159 -14.561 8.499   1.00 27.42 ? 440 TYR B CD2 1 
ATOM   7762 C CE1 . TYR B 1 440 ? -9.328  -12.829 9.625   1.00 31.24 ? 440 TYR B CE1 1 
ATOM   7763 C CE2 . TYR B 1 440 ? -9.782  -14.879 8.487   1.00 28.72 ? 440 TYR B CE2 1 
ATOM   7764 C CZ  . TYR B 1 440 ? -8.888  -13.998 9.054   1.00 29.97 ? 440 TYR B CZ  1 
ATOM   7765 O OH  . TYR B 1 440 ? -7.527  -14.266 9.074   1.00 32.92 ? 440 TYR B OH  1 
ATOM   7766 N N   . ILE B 1 441 ? -16.012 -12.480 10.774  1.00 21.67 ? 441 ILE B N   1 
ATOM   7767 C CA  . ILE B 1 441 ? -17.052 -11.533 11.174  1.00 19.71 ? 441 ILE B CA  1 
ATOM   7768 C C   . ILE B 1 441 ? -16.854 -11.100 12.622  1.00 21.38 ? 441 ILE B C   1 
ATOM   7769 O O   . ILE B 1 441 ? -17.175 -9.959  12.988  1.00 20.39 ? 441 ILE B O   1 
ATOM   7770 C CB  . ILE B 1 441 ? -18.467 -12.125 10.933  1.00 24.28 ? 441 ILE B CB  1 
ATOM   7771 C CG1 . ILE B 1 441 ? -19.535 -11.026 10.968  1.00 25.43 ? 441 ILE B CG1 1 
ATOM   7772 C CG2 . ILE B 1 441 ? -18.822 -13.199 11.966  1.00 20.98 ? 441 ILE B CG2 1 
ATOM   7773 C CD1 . ILE B 1 441 ? -19.460 -10.061 9.806   1.00 22.07 ? 441 ILE B CD1 1 
ATOM   7774 N N   . LEU B 1 442 ? -16.312 -11.985 13.465  1.00 18.65 ? 442 LEU B N   1 
ATOM   7775 C CA  . LEU B 1 442 ? -16.028 -11.611 14.848  1.00 15.82 ? 442 LEU B CA  1 
ATOM   7776 C C   . LEU B 1 442 ? -14.909 -10.590 14.925  1.00 15.24 ? 442 LEU B C   1 
ATOM   7777 O O   . LEU B 1 442 ? -14.973 -9.656  15.738  1.00 16.21 ? 442 LEU B O   1 
ATOM   7778 C CB  . LEU B 1 442 ? -15.657 -12.839 15.681  1.00 19.93 ? 442 LEU B CB  1 
ATOM   7779 C CG  . LEU B 1 442 ? -16.643 -14.008 15.703  1.00 24.43 ? 442 LEU B CG  1 
ATOM   7780 C CD1 . LEU B 1 442 ? -16.106 -15.088 16.636  1.00 21.86 ? 442 LEU B CD1 1 
ATOM   7781 C CD2 . LEU B 1 442 ? -18.021 -13.538 16.163  1.00 21.79 ? 442 LEU B CD2 1 
ATOM   7782 N N   . VAL B 1 443 ? -13.864 -10.755 14.098  1.00 16.45 ? 443 VAL B N   1 
ATOM   7783 C CA  . VAL B 1 443 ? -12.777 -9.773  14.067  1.00 18.44 ? 443 VAL B CA  1 
ATOM   7784 C C   . VAL B 1 443 ? -13.314 -8.382  13.758  1.00 16.00 ? 443 VAL B C   1 
ATOM   7785 O O   . VAL B 1 443 ? -12.905 -7.393  14.391  1.00 15.70 ? 443 VAL B O   1 
ATOM   7786 C CB  . VAL B 1 443 ? -11.698 -10.169 13.036  1.00 19.55 ? 443 VAL B CB  1 
ATOM   7787 C CG1 . VAL B 1 443 ? -10.542 -9.166  13.061  1.00 17.76 ? 443 VAL B CG1 1 
ATOM   7788 C CG2 . VAL B 1 443 ? -11.202 -11.599 13.254  1.00 20.04 ? 443 VAL B CG2 1 
ATOM   7789 N N   . ALA B 1 444 ? -14.230 -8.283  12.783  1.00 16.48 ? 444 ALA B N   1 
ATOM   7790 C CA  . ALA B 1 444 ? -14.794 -6.999  12.369  1.00 19.08 ? 444 ALA B CA  1 
ATOM   7791 C C   . ALA B 1 444 ? -15.708 -6.390  13.422  1.00 20.02 ? 444 ALA B C   1 
ATOM   7792 O O   . ALA B 1 444 ? -16.058 -5.208  13.302  1.00 17.50 ? 444 ALA B O   1 
ATOM   7793 C CB  . ALA B 1 444 ? -15.565 -7.137  11.049  1.00 19.39 ? 444 ALA B CB  1 
ATOM   7794 N N   . GLU B 1 445 ? -16.117 -7.163  14.434  1.00 15.72 ? 445 GLU B N   1 
ATOM   7795 C CA  . GLU B 1 445 ? -16.918 -6.622  15.528  1.00 15.14 ? 445 GLU B CA  1 
ATOM   7796 C C   . GLU B 1 445 ? -16.072 -5.946  16.604  1.00 16.97 ? 445 GLU B C   1 
ATOM   7797 O O   . GLU B 1 445 ? -16.628 -5.410  17.568  1.00 17.85 ? 445 GLU B O   1 
ATOM   7798 C CB  . GLU B 1 445 ? -17.788 -7.736  16.124  1.00 16.88 ? 445 GLU B CB  1 
ATOM   7799 C CG  . GLU B 1 445 ? -18.903 -8.168  15.134  1.00 20.16 ? 445 GLU B CG  1 
ATOM   7800 C CD  . GLU B 1 445 ? -19.518 -9.548  15.418  1.00 19.06 ? 445 GLU B CD  1 
ATOM   7801 O OE1 . GLU B 1 445 ? -19.192 -10.154 16.454  1.00 20.18 ? 445 GLU B OE1 1 
ATOM   7802 O OE2 . GLU B 1 445 ? -20.334 -10.014 14.590  1.00 20.53 ? 445 GLU B OE2 1 
ATOM   7803 N N   . GLY B 1 446 ? -14.755 -5.901  16.445  1.00 15.55 ? 446 GLY B N   1 
ATOM   7804 C CA  . GLY B 1 446 ? -13.931 -5.265  17.447  1.00 15.78 ? 446 GLY B CA  1 
ATOM   7805 C C   . GLY B 1 446 ? -14.209 -3.777  17.528  1.00 17.80 ? 446 GLY B C   1 
ATOM   7806 O O   . GLY B 1 446 ? -14.533 -3.128  16.536  1.00 17.28 ? 446 GLY B O   1 
ATOM   7807 N N   . SER B 1 447 ? -14.080 -3.225  18.739  1.00 14.97 ? 447 SER B N   1 
ATOM   7808 C CA  . SER B 1 447 ? -14.491 -1.838  18.930  1.00 13.74 ? 447 SER B CA  1 
ATOM   7809 C C   . SER B 1 447 ? -13.578 -0.870  18.193  1.00 14.83 ? 447 SER B C   1 
ATOM   7810 O O   . SER B 1 447 ? -14.012 0.232   17.841  1.00 15.72 ? 447 SER B O   1 
ATOM   7811 C CB  . SER B 1 447 ? -14.529 -1.500  20.432  1.00 15.17 ? 447 SER B CB  1 
ATOM   7812 O OG  . SER B 1 447 ? -13.207 -1.525  20.958  1.00 16.14 ? 447 SER B OG  1 
ATOM   7813 N N   . ASP B 1 448 ? -12.317 -1.261  17.956  1.00 12.93 ? 448 ASP B N   1 
ATOM   7814 C CA  . ASP B 1 448 ? -11.311 -0.333  17.447  1.00 12.13 ? 448 ASP B CA  1 
ATOM   7815 C C   . ASP B 1 448 ? -11.700 0.261   16.096  1.00 12.65 ? 448 ASP B C   1 
ATOM   7816 O O   . ASP B 1 448 ? -11.474 1.451   15.851  1.00 16.63 ? 448 ASP B O   1 
ATOM   7817 C CB  . ASP B 1 448 ? -9.970  -1.046  17.354  1.00 15.01 ? 448 ASP B CB  1 
ATOM   7818 C CG  . ASP B 1 448 ? -9.610  -1.750  18.651  1.00 17.76 ? 448 ASP B CG  1 
ATOM   7819 O OD1 . ASP B 1 448 ? -10.129 -2.865  18.921  1.00 15.25 ? 448 ASP B OD1 1 
ATOM   7820 O OD2 . ASP B 1 448 ? -8.818  -1.161  19.422  1.00 18.66 ? 448 ASP B OD2 1 
ATOM   7821 N N   . TRP B 1 449 ? -12.268 -0.552  15.202  1.00 14.61 ? 449 TRP B N   1 
ATOM   7822 C CA  . TRP B 1 449 ? -12.625 -0.045  13.876  1.00 15.57 ? 449 TRP B CA  1 
ATOM   7823 C C   . TRP B 1 449 ? -13.598 1.124   13.963  1.00 16.27 ? 449 TRP B C   1 
ATOM   7824 O O   . TRP B 1 449 ? -13.462 2.118   13.231  1.00 15.90 ? 449 TRP B O   1 
ATOM   7825 C CB  . TRP B 1 449 ? -13.221 -1.180  13.034  1.00 16.88 ? 449 TRP B CB  1 
ATOM   7826 C CG  . TRP B 1 449 ? -12.505 -2.492  13.265  1.00 13.56 ? 449 TRP B CG  1 
ATOM   7827 C CD1 . TRP B 1 449 ? -13.059 -3.650  13.718  1.00 13.96 ? 449 TRP B CD1 1 
ATOM   7828 C CD2 . TRP B 1 449 ? -11.113 -2.773  13.031  1.00 13.82 ? 449 TRP B CD2 1 
ATOM   7829 N NE1 . TRP B 1 449 ? -12.095 -4.634  13.803  1.00 15.88 ? 449 TRP B NE1 1 
ATOM   7830 C CE2 . TRP B 1 449 ? -10.896 -4.121  13.388  1.00 14.63 ? 449 TRP B CE2 1 
ATOM   7831 C CE3 . TRP B 1 449 ? -10.027 -2.014  12.556  1.00 14.26 ? 449 TRP B CE3 1 
ATOM   7832 C CZ2 . TRP B 1 449 ? -9.647  -4.730  13.289  1.00 15.02 ? 449 TRP B CZ2 1 
ATOM   7833 C CZ3 . TRP B 1 449 ? -8.781  -2.612  12.470  1.00 14.71 ? 449 TRP B CZ3 1 
ATOM   7834 C CH2 . TRP B 1 449 ? -8.601  -3.968  12.832  1.00 17.60 ? 449 TRP B CH2 1 
ATOM   7835 N N   . PHE B 1 450 ? -14.603 1.016   14.838  1.00 15.61 ? 450 PHE B N   1 
ATOM   7836 C CA  . PHE B 1 450 ? -15.617 2.063   14.955  1.00 16.47 ? 450 PHE B CA  1 
ATOM   7837 C C   . PHE B 1 450 ? -15.074 3.298   15.660  1.00 16.19 ? 450 PHE B C   1 
ATOM   7838 O O   . PHE B 1 450 ? -15.527 4.417   15.392  1.00 17.86 ? 450 PHE B O   1 
ATOM   7839 C CB  . PHE B 1 450 ? -16.856 1.503   15.673  1.00 16.42 ? 450 PHE B CB  1 
ATOM   7840 C CG  . PHE B 1 450 ? -17.360 0.234   15.067  1.00 18.83 ? 450 PHE B CG  1 
ATOM   7841 C CD1 . PHE B 1 450 ? -16.850 -0.999  15.454  1.00 18.16 ? 450 PHE B CD1 1 
ATOM   7842 C CD2 . PHE B 1 450 ? -18.352 0.276   14.083  1.00 16.58 ? 450 PHE B CD2 1 
ATOM   7843 C CE1 . PHE B 1 450 ? -17.309 -2.173  14.854  1.00 16.16 ? 450 PHE B CE1 1 
ATOM   7844 C CE2 . PHE B 1 450 ? -18.799 -0.877  13.485  1.00 17.83 ? 450 PHE B CE2 1 
ATOM   7845 C CZ  . PHE B 1 450 ? -18.295 -2.103  13.872  1.00 14.42 ? 450 PHE B CZ  1 
ATOM   7846 N N   . TRP B 1 451 ? -14.095 3.122   16.551  1.00 18.42 ? 451 TRP B N   1 
ATOM   7847 C CA  . TRP B 1 451 ? -13.474 4.247   17.245  1.00 14.87 ? 451 TRP B CA  1 
ATOM   7848 C C   . TRP B 1 451 ? -12.771 5.197   16.278  1.00 17.16 ? 451 TRP B C   1 
ATOM   7849 O O   . TRP B 1 451 ? -12.923 6.422   16.369  1.00 17.15 ? 451 TRP B O   1 
ATOM   7850 C CB  . TRP B 1 451 ? -12.480 3.672   18.266  1.00 17.94 ? 451 TRP B CB  1 
ATOM   7851 C CG  . TRP B 1 451 ? -11.573 4.643   18.984  1.00 18.57 ? 451 TRP B CG  1 
ATOM   7852 C CD1 . TRP B 1 451 ? -10.250 4.919   18.697  1.00 18.09 ? 451 TRP B CD1 1 
ATOM   7853 C CD2 . TRP B 1 451 ? -11.899 5.419   20.146  1.00 18.18 ? 451 TRP B CD2 1 
ATOM   7854 N NE1 . TRP B 1 451 ? -9.752  5.824   19.614  1.00 19.71 ? 451 TRP B NE1 1 
ATOM   7855 C CE2 . TRP B 1 451 ? -10.748 6.150   20.502  1.00 23.10 ? 451 TRP B CE2 1 
ATOM   7856 C CE3 . TRP B 1 451 ? -13.063 5.567   20.917  1.00 18.29 ? 451 TRP B CE3 1 
ATOM   7857 C CZ2 . TRP B 1 451 ? -10.727 7.026   21.598  1.00 20.80 ? 451 TRP B CZ2 1 
ATOM   7858 C CZ3 . TRP B 1 451 ? -13.039 6.440   22.003  1.00 21.37 ? 451 TRP B CZ3 1 
ATOM   7859 C CH2 . TRP B 1 451 ? -11.877 7.152   22.331  1.00 19.73 ? 451 TRP B CH2 1 
ATOM   7860 N N   . TRP B 1 452 ? -11.987 4.643   15.336  1.00 15.70 ? 452 TRP B N   1 
ATOM   7861 C CA  . TRP B 1 452 ? -11.183 5.452   14.423  1.00 16.75 ? 452 TRP B CA  1 
ATOM   7862 C C   . TRP B 1 452 ? -11.984 6.011   13.261  1.00 21.38 ? 452 TRP B C   1 
ATOM   7863 O O   . TRP B 1 452 ? -11.556 6.997   12.651  1.00 21.12 ? 452 TRP B O   1 
ATOM   7864 C CB  . TRP B 1 452 ? -10.009 4.631   13.863  1.00 17.83 ? 452 TRP B CB  1 
ATOM   7865 C CG  . TRP B 1 452 ? -9.079  4.178   14.942  1.00 15.66 ? 452 TRP B CG  1 
ATOM   7866 C CD1 . TRP B 1 452 ? -8.862  2.883   15.337  1.00 15.38 ? 452 TRP B CD1 1 
ATOM   7867 C CD2 . TRP B 1 452 ? -8.291  5.002   15.813  1.00 19.38 ? 452 TRP B CD2 1 
ATOM   7868 N NE1 . TRP B 1 452 ? -7.976  2.853   16.385  1.00 16.46 ? 452 TRP B NE1 1 
ATOM   7869 C CE2 . TRP B 1 452 ? -7.611  4.137   16.698  1.00 17.33 ? 452 TRP B CE2 1 
ATOM   7870 C CE3 . TRP B 1 452 ? -8.090  6.382   15.924  1.00 21.49 ? 452 TRP B CE3 1 
ATOM   7871 C CZ2 . TRP B 1 452 ? -6.746  4.606   17.694  1.00 18.20 ? 452 TRP B CZ2 1 
ATOM   7872 C CZ3 . TRP B 1 452 ? -7.220  6.851   16.922  1.00 22.19 ? 452 TRP B CZ3 1 
ATOM   7873 C CH2 . TRP B 1 452 ? -6.558  5.962   17.778  1.00 21.48 ? 452 TRP B CH2 1 
ATOM   7874 N N   . GLN B 1 453 ? -13.132 5.416   12.966  1.00 17.63 ? 453 GLN B N   1 
ATOM   7875 C CA  . GLN B 1 453 ? -13.942 5.796   11.818  1.00 20.11 ? 453 GLN B CA  1 
ATOM   7876 C C   . GLN B 1 453 ? -14.718 7.062   12.132  1.00 21.24 ? 453 GLN B C   1 
ATOM   7877 O O   . GLN B 1 453 ? -15.155 7.269   13.265  1.00 23.44 ? 453 GLN B O   1 
ATOM   7878 C CB  . GLN B 1 453 ? -14.898 4.655   11.467  1.00 19.32 ? 453 GLN B CB  1 
ATOM   7879 C CG  . GLN B 1 453 ? -16.035 5.026   10.525  1.00 22.93 ? 453 GLN B CG  1 
ATOM   7880 C CD  . GLN B 1 453 ? -15.592 5.212   9.085   1.00 23.95 ? 453 GLN B CD  1 
ATOM   7881 O OE1 . GLN B 1 453 ? -14.391 5.325   8.793   1.00 24.25 ? 453 GLN B OE1 1 
ATOM   7882 N NE2 . GLN B 1 453 ? -16.566 5.240   8.167   1.00 25.84 ? 453 GLN B NE2 1 
ATOM   7883 N N   . GLY B 1 454 ? -14.866 7.921   11.130  1.00 27.89 ? 454 GLY B N   1 
ATOM   7884 C CA  . GLY B 1 454 ? -15.676 9.107   11.334  1.00 33.38 ? 454 GLY B CA  1 
ATOM   7885 C C   . GLY B 1 454 ? -15.094 10.096  12.314  1.00 37.20 ? 454 GLY B C   1 
ATOM   7886 O O   . GLY B 1 454 ? -15.844 10.715  13.087  1.00 32.28 ? 454 GLY B O   1 
ATOM   7887 N N   . GLU B 1 455 ? -13.771 10.233  12.321  1.00 37.82 ? 455 GLU B N   1 
ATOM   7888 C CA  . GLU B 1 455 ? -13.040 11.215  13.105  1.00 42.00 ? 455 GLU B CA  1 
ATOM   7889 C C   . GLU B 1 455 ? -12.255 12.116  12.158  1.00 46.42 ? 455 GLU B C   1 
ATOM   7890 O O   . GLU B 1 455 ? -12.159 11.856  10.954  1.00 43.51 ? 455 GLU B O   1 
ATOM   7891 C CB  . GLU B 1 455 ? -12.096 10.532  14.104  1.00 41.89 ? 455 GLU B CB  1 
ATOM   7892 C CG  . GLU B 1 455 ? -12.777 9.494   14.990  1.00 42.17 ? 455 GLU B CG  1 
ATOM   7893 C CD  . GLU B 1 455 ? -13.671 10.127  16.044  1.00 44.60 ? 455 GLU B CD  1 
ATOM   7894 O OE1 . GLU B 1 455 ? -13.476 11.321  16.346  1.00 45.79 ? 455 GLU B OE1 1 
ATOM   7895 O OE2 . GLU B 1 455 ? -14.562 9.436   16.577  1.00 39.64 ? 455 GLU B OE2 1 
ATOM   7896 N N   . GLU B 1 456 ? -11.692 13.189  12.710  1.00 50.31 ? 456 GLU B N   1 
ATOM   7897 C CA  . GLU B 1 456 ? -10.845 14.061  11.908  1.00 55.00 ? 456 GLU B CA  1 
ATOM   7898 C C   . GLU B 1 456 ? -9.672  13.266  11.351  1.00 50.25 ? 456 GLU B C   1 
ATOM   7899 O O   . GLU B 1 456 ? -9.108  12.404  12.032  1.00 48.59 ? 456 GLU B O   1 
ATOM   7900 C CB  . GLU B 1 456 ? -10.345 15.247  12.736  1.00 57.80 ? 456 GLU B CB  1 
ATOM   7901 C CG  . GLU B 1 456 ? -11.216 16.495  12.617  1.00 66.06 ? 456 GLU B CG  1 
ATOM   7902 C CD  . GLU B 1 456 ? -11.553 16.841  11.177  1.00 75.75 ? 456 GLU B CD  1 
ATOM   7903 O OE1 . GLU B 1 456 ? -12.724 16.661  10.774  1.00 79.01 ? 456 GLU B OE1 1 
ATOM   7904 O OE2 . GLU B 1 456 ? -10.646 17.293  10.446  1.00 80.26 ? 456 GLU B OE2 1 
ATOM   7905 N N   . LYS B 1 457 ? -9.322  13.547  10.095  1.00 39.63 ? 457 LYS B N   1 
ATOM   7906 C CA  . LYS B 1 457 ? -8.314  12.755  9.401   1.00 39.70 ? 457 LYS B CA  1 
ATOM   7907 C C   . LYS B 1 457 ? -6.995  12.777  10.158  1.00 41.96 ? 457 LYS B C   1 
ATOM   7908 O O   . LYS B 1 457 ? -6.456  13.843  10.467  1.00 47.46 ? 457 LYS B O   1 
ATOM   7909 C CB  . LYS B 1 457 ? -8.107  13.273  7.977   1.00 44.66 ? 457 LYS B CB  1 
ATOM   7910 C CG  . LYS B 1 457 ? -7.438  12.263  7.066   1.00 50.84 ? 457 LYS B CG  1 
ATOM   7911 C CD  . LYS B 1 457 ? -7.578  12.667  5.601   1.00 59.49 ? 457 LYS B CD  1 
ATOM   7912 C CE  . LYS B 1 457 ? -7.148  11.542  4.667   1.00 62.16 ? 457 LYS B CE  1 
ATOM   7913 N NZ  . LYS B 1 457 ? -5.692  11.244  4.795   1.00 63.59 ? 457 LYS B NZ  1 
ATOM   7914 N N   . ALA B 1 458 ? -6.489  11.591  10.466  1.00 37.75 ? 458 ALA B N   1 
ATOM   7915 C CA  . ALA B 1 458 ? -5.222  11.393  11.151  1.00 39.52 ? 458 ALA B CA  1 
ATOM   7916 C C   . ALA B 1 458 ? -4.365  10.436  10.338  1.00 38.30 ? 458 ALA B C   1 
ATOM   7917 O O   . ALA B 1 458 ? -4.889  9.635   9.555   1.00 37.56 ? 458 ALA B O   1 
ATOM   7918 C CB  . ALA B 1 458 ? -5.450  10.832  12.563  1.00 38.36 ? 458 ALA B CB  1 
ATOM   7919 N N   . PRO B 1 459 ? -3.043  10.505  10.477  1.00 32.94 ? 459 PRO B N   1 
ATOM   7920 C CA  . PRO B 1 459 ? -2.191  9.586   9.712   1.00 34.86 ? 459 PRO B CA  1 
ATOM   7921 C C   . PRO B 1 459 ? -2.470  8.132   10.084  1.00 33.84 ? 459 PRO B C   1 
ATOM   7922 O O   . PRO B 1 459 ? -2.728  7.799   11.246  1.00 32.30 ? 459 PRO B O   1 
ATOM   7923 C CB  . PRO B 1 459 ? -0.761  10.012  10.081  1.00 39.84 ? 459 PRO B CB  1 
ATOM   7924 C CG  . PRO B 1 459 ? -0.882  11.016  11.176  1.00 38.27 ? 459 PRO B CG  1 
ATOM   7925 C CD  . PRO B 1 459 ? -2.275  11.567  11.148  1.00 37.03 ? 459 PRO B CD  1 
ATOM   7926 N N   . PHE B 1 460 ? -2.475  7.277   9.061   1.00 32.71 ? 460 PHE B N   1 
ATOM   7927 C CA  . PHE B 1 460 ? -2.641  5.827   9.140   1.00 33.81 ? 460 PHE B CA  1 
ATOM   7928 C C   . PHE B 1 460 ? -4.067  5.370   9.438   1.00 31.00 ? 460 PHE B C   1 
ATOM   7929 O O   . PHE B 1 460 ? -4.304  4.158   9.521   1.00 28.82 ? 460 PHE B O   1 
ATOM   7930 C CB  . PHE B 1 460 ? -1.687  5.192   10.162  1.00 33.09 ? 460 PHE B CB  1 
ATOM   7931 C CG  . PHE B 1 460 ? -0.243  5.499   9.894   1.00 37.86 ? 460 PHE B CG  1 
ATOM   7932 C CD1 . PHE B 1 460 ? 0.384   4.992   8.771   1.00 41.60 ? 460 PHE B CD1 1 
ATOM   7933 C CD2 . PHE B 1 460 ? 0.486   6.299   10.755  1.00 39.79 ? 460 PHE B CD2 1 
ATOM   7934 C CE1 . PHE B 1 460 ? 1.719   5.277   8.502   1.00 44.74 ? 460 PHE B CE1 1 
ATOM   7935 C CE2 . PHE B 1 460 ? 1.825   6.587   10.496  1.00 43.01 ? 460 PHE B CE2 1 
ATOM   7936 C CZ  . PHE B 1 460 ? 2.441   6.073   9.368   1.00 43.29 ? 460 PHE B CZ  1 
ATOM   7937 N N   . VAL B 1 461 ? -5.037  6.277   9.572   1.00 36.52 ? 461 VAL B N   1 
ATOM   7938 C CA  . VAL B 1 461 ? -6.419  5.830   9.763   1.00 37.13 ? 461 VAL B CA  1 
ATOM   7939 C C   . VAL B 1 461 ? -6.913  5.043   8.552   1.00 35.81 ? 461 VAL B C   1 
ATOM   7940 O O   . VAL B 1 461 ? -7.769  4.151   8.680   1.00 35.18 ? 461 VAL B O   1 
ATOM   7941 C CB  . VAL B 1 461 ? -7.318  7.041   10.085  1.00 42.10 ? 461 VAL B CB  1 
ATOM   7942 C CG1 . VAL B 1 461 ? -8.788  6.625   10.210  1.00 38.42 ? 461 VAL B CG1 1 
ATOM   7943 C CG2 . VAL B 1 461 ? -6.836  7.688   11.378  1.00 43.72 ? 461 VAL B CG2 1 
ATOM   7944 N N   . GLU B 1 462 ? -6.387  5.344   7.366   1.00 25.54 ? 462 GLU B N   1 
ATOM   7945 C CA  . GLU B 1 462 ? -6.703  4.530   6.195   1.00 29.22 ? 462 GLU B CA  1 
ATOM   7946 C C   . GLU B 1 462 ? -6.351  3.066   6.419   1.00 28.10 ? 462 GLU B C   1 
ATOM   7947 O O   . GLU B 1 462 ? -6.934  2.179   5.782   1.00 27.81 ? 462 GLU B O   1 
ATOM   7948 C CB  . GLU B 1 462 ? -5.962  5.047   4.960   1.00 38.80 ? 462 GLU B CB  1 
ATOM   7949 C CG  . GLU B 1 462 ? -6.416  6.408   4.505   1.00 49.16 ? 462 GLU B CG  1 
ATOM   7950 C CD  . GLU B 1 462 ? -5.500  7.504   4.998   1.00 54.04 ? 462 GLU B CD  1 
ATOM   7951 O OE1 . GLU B 1 462 ? -4.780  7.280   6.011   1.00 43.60 ? 462 GLU B OE1 1 
ATOM   7952 O OE2 . GLU B 1 462 ? -5.501  8.580   4.355   1.00 59.07 ? 462 GLU B OE2 1 
ATOM   7953 N N   . VAL B 1 463 ? -5.382  2.789   7.299   1.00 23.35 ? 463 VAL B N   1 
ATOM   7954 C CA  . VAL B 1 463 ? -4.995  1.405   7.513   1.00 21.37 ? 463 VAL B CA  1 
ATOM   7955 C C   . VAL B 1 463 ? -6.042  0.675   8.336   1.00 19.86 ? 463 VAL B C   1 
ATOM   7956 O O   . VAL B 1 463 ? -6.387  -0.471  8.029   1.00 20.46 ? 463 VAL B O   1 
ATOM   7957 C CB  . VAL B 1 463 ? -3.600  1.331   8.161   1.00 21.68 ? 463 VAL B CB  1 
ATOM   7958 C CG1 . VAL B 1 463 ? -3.165  -0.115  8.262   1.00 27.30 ? 463 VAL B CG1 1 
ATOM   7959 C CG2 . VAL B 1 463 ? -2.607  2.111   7.332   1.00 21.66 ? 463 VAL B CG2 1 
ATOM   7960 N N   . PHE B 1 464 ? -6.554  1.305   9.407   1.00 18.72 ? 464 PHE B N   1 
ATOM   7961 C CA  . PHE B 1 464 ? -7.648  0.695   10.158  1.00 17.54 ? 464 PHE B CA  1 
ATOM   7962 C C   . PHE B 1 464 ? -8.861  0.459   9.255   1.00 18.00 ? 464 PHE B C   1 
ATOM   7963 O O   . PHE B 1 464 ? -9.541  -0.568  9.363   1.00 17.90 ? 464 PHE B O   1 
ATOM   7964 C CB  . PHE B 1 464 ? -8.030  1.581   11.353  1.00 17.01 ? 464 PHE B CB  1 
ATOM   7965 C CG  . PHE B 1 464 ? -6.984  1.607   12.446  1.00 14.68 ? 464 PHE B CG  1 
ATOM   7966 C CD1 . PHE B 1 464 ? -6.992  0.645   13.446  1.00 16.57 ? 464 PHE B CD1 1 
ATOM   7967 C CD2 . PHE B 1 464 ? -5.986  2.564   12.449  1.00 16.63 ? 464 PHE B CD2 1 
ATOM   7968 C CE1 . PHE B 1 464 ? -6.040  0.644   14.461  1.00 15.85 ? 464 PHE B CE1 1 
ATOM   7969 C CE2 . PHE B 1 464 ? -5.006  2.580   13.482  1.00 17.19 ? 464 PHE B CE2 1 
ATOM   7970 C CZ  . PHE B 1 464 ? -5.034  1.610   14.473  1.00 17.85 ? 464 PHE B CZ  1 
ATOM   7971 N N   . ASP B 1 465 ? -9.149  1.405   8.362   1.00 18.49 ? 465 ASP B N   1 
ATOM   7972 C CA  . ASP B 1 465 ? -10.270 1.237   7.435   1.00 17.70 ? 465 ASP B CA  1 
ATOM   7973 C C   . ASP B 1 465 ? -10.033 0.075   6.474   1.00 18.63 ? 465 ASP B C   1 
ATOM   7974 O O   . ASP B 1 465 ? -10.944 -0.721  6.209   1.00 21.71 ? 465 ASP B O   1 
ATOM   7975 C CB  . ASP B 1 465 ? -10.476 2.531   6.651   1.00 18.99 ? 465 ASP B CB  1 
ATOM   7976 C CG  . ASP B 1 465 ? -11.552 2.408   5.609   1.00 24.13 ? 465 ASP B CG  1 
ATOM   7977 O OD1 . ASP B 1 465 ? -12.744 2.500   5.980   1.00 20.63 ? 465 ASP B OD1 1 
ATOM   7978 O OD2 . ASP B 1 465 ? -11.202 2.215   4.427   1.00 26.37 ? 465 ASP B OD2 1 
ATOM   7979 N N   . LYS B 1 466 ? -8.814  -0.029  5.932   1.00 18.78 ? 466 LYS B N   1 
ATOM   7980 C CA  . LYS B 1 466 ? -8.461  -1.156  5.070   1.00 19.41 ? 466 LYS B CA  1 
ATOM   7981 C C   . LYS B 1 466 ? -8.606  -2.481  5.811   1.00 19.94 ? 466 LYS B C   1 
ATOM   7982 O O   . LYS B 1 466 ? -9.145  -3.454  5.266   1.00 21.85 ? 466 LYS B O   1 
ATOM   7983 C CB  . LYS B 1 466 ? -7.023  -0.981  4.545   1.00 21.09 ? 466 LYS B CB  1 
ATOM   7984 C CG  . LYS B 1 466 ? -6.537  -2.143  3.738   1.00 23.03 ? 466 LYS B CG  1 
ATOM   7985 C CD  . LYS B 1 466 ? -5.227  -1.813  3.028   1.00 34.64 ? 466 LYS B CD  1 
ATOM   7986 C CE  . LYS B 1 466 ? -4.589  -3.056  2.417   1.00 45.47 ? 466 LYS B CE  1 
ATOM   7987 N NZ  . LYS B 1 466 ? -5.239  -3.441  1.130   1.00 51.38 ? 466 LYS B NZ  1 
ATOM   7988 N N   . LEU B 1 467 ? -8.120  -2.543  7.057   1.00 17.74 ? 467 LEU B N   1 
ATOM   7989 C CA  . LEU B 1 467 ? -8.231  -3.772  7.836   1.00 19.39 ? 467 LEU B CA  1 
ATOM   7990 C C   . LEU B 1 467 ? -9.692  -4.146  8.091   1.00 16.79 ? 467 LEU B C   1 
ATOM   7991 O O   . LEU B 1 467 ? -10.107 -5.277  7.820   1.00 18.81 ? 467 LEU B O   1 
ATOM   7992 C CB  . LEU B 1 467 ? -7.476  -3.627  9.160   1.00 19.53 ? 467 LEU B CB  1 
ATOM   7993 C CG  . LEU B 1 467 ? -5.959  -3.709  9.046   1.00 19.48 ? 467 LEU B CG  1 
ATOM   7994 C CD1 . LEU B 1 467 ? -5.299  -3.197  10.331  1.00 17.80 ? 467 LEU B CD1 1 
ATOM   7995 C CD2 . LEU B 1 467 ? -5.542  -5.137  8.722   1.00 19.58 ? 467 LEU B CD2 1 
ATOM   7996 N N   . PHE B 1 468 ? -10.487 -3.207  8.609   1.00 17.51 ? 468 PHE B N   1 
ATOM   7997 C CA  . PHE B 1 468 ? -11.901 -3.498  8.870   1.00 16.12 ? 468 PHE B CA  1 
ATOM   7998 C C   . PHE B 1 468 ? -12.588 -4.056  7.622   1.00 18.74 ? 468 PHE B C   1 
ATOM   7999 O O   . PHE B 1 468 ? -13.250 -5.100  7.657   1.00 20.11 ? 468 PHE B O   1 
ATOM   8000 C CB  . PHE B 1 468 ? -12.614 -2.232  9.337   1.00 15.86 ? 468 PHE B CB  1 
ATOM   8001 C CG  . PHE B 1 468 ? -14.118 -2.371  9.417   1.00 18.24 ? 468 PHE B CG  1 
ATOM   8002 C CD1 . PHE B 1 468 ? -14.692 -3.112  10.427  1.00 15.70 ? 468 PHE B CD1 1 
ATOM   8003 C CD2 . PHE B 1 468 ? -14.953 -1.771  8.465   1.00 18.53 ? 468 PHE B CD2 1 
ATOM   8004 C CE1 . PHE B 1 468 ? -16.079 -3.232  10.533  1.00 15.59 ? 468 PHE B CE1 1 
ATOM   8005 C CE2 . PHE B 1 468 ? -16.335 -1.882  8.549   1.00 19.76 ? 468 PHE B CE2 1 
ATOM   8006 C CZ  . PHE B 1 468 ? -16.912 -2.628  9.576   1.00 17.68 ? 468 PHE B CZ  1 
ATOM   8007 N N   . ARG B 1 469 ? -12.407 -3.383  6.490   1.00 18.87 ? 469 ARG B N   1 
ATOM   8008 C CA  . ARG B 1 469 ? -13.130 -3.786  5.295   1.00 18.81 ? 469 ARG B CA  1 
ATOM   8009 C C   . ARG B 1 469 ? -12.589 -5.094  4.733   1.00 19.37 ? 469 ARG B C   1 
ATOM   8010 O O   . ARG B 1 469 ? -13.338 -5.851  4.099   1.00 22.56 ? 469 ARG B O   1 
ATOM   8011 C CB  . ARG B 1 469 ? -13.065 -2.659  4.262   1.00 19.64 ? 469 ARG B CB  1 
ATOM   8012 C CG  . ARG B 1 469 ? -13.888 -1.436  4.709   1.00 21.22 ? 469 ARG B CG  1 
ATOM   8013 C CD  . ARG B 1 469 ? -13.687 -0.267  3.762   1.00 22.05 ? 469 ARG B CD  1 
ATOM   8014 N NE  . ARG B 1 469 ? -14.411 0.945   4.151   1.00 22.43 ? 469 ARG B NE  1 
ATOM   8015 C CZ  . ARG B 1 469 ? -15.654 1.242   3.755   1.00 24.36 ? 469 ARG B CZ  1 
ATOM   8016 N NH1 . ARG B 1 469 ? -16.368 0.405   2.991   1.00 22.18 ? 469 ARG B NH1 1 
ATOM   8017 N NH2 . ARG B 1 469 ? -16.197 2.393   4.117   1.00 26.44 ? 469 ARG B NH2 1 
ATOM   8018 N N   . SER B 1 470 ? -11.291 -5.365  4.936   1.00 19.31 ? 470 SER B N   1 
ATOM   8019 C CA  . SER B 1 470 ? -10.746 -6.650  4.509   1.00 21.37 ? 470 SER B CA  1 
ATOM   8020 C C   . SER B 1 470 ? -11.295 -7.804  5.346   1.00 20.98 ? 470 SER B C   1 
ATOM   8021 O O   . SER B 1 470 ? -11.562 -8.890  4.810   1.00 22.45 ? 470 SER B O   1 
ATOM   8022 C CB  . SER B 1 470 ? -9.213  -6.622  4.578   1.00 23.34 ? 470 SER B CB  1 
ATOM   8023 O OG  . SER B 1 470 ? -8.712  -5.595  3.755   1.00 31.81 ? 470 SER B OG  1 
ATOM   8024 N N   . PHE B 1 471 ? -11.432 -7.612  6.664   1.00 19.19 ? 471 PHE B N   1 
ATOM   8025 C CA  . PHE B 1 471 ? -12.028 -8.670  7.484   1.00 19.91 ? 471 PHE B CA  1 
ATOM   8026 C C   . PHE B 1 471 ? -13.496 -8.888  7.118   1.00 20.87 ? 471 PHE B C   1 
ATOM   8027 O O   . PHE B 1 471 ? -13.974 -10.032 7.070   1.00 21.72 ? 471 PHE B O   1 
ATOM   8028 C CB  . PHE B 1 471 ? -11.895 -8.330  8.971   1.00 18.90 ? 471 PHE B CB  1 
ATOM   8029 C CG  . PHE B 1 471 ? -10.476 -8.266  9.458   1.00 18.52 ? 471 PHE B CG  1 
ATOM   8030 C CD1 . PHE B 1 471 ? -9.585  -9.283  9.168   1.00 18.64 ? 471 PHE B CD1 1 
ATOM   8031 C CD2 . PHE B 1 471 ? -10.049 -7.191  10.225  1.00 18.53 ? 471 PHE B CD2 1 
ATOM   8032 C CE1 . PHE B 1 471 ? -8.285  -9.236  9.635   1.00 20.28 ? 471 PHE B CE1 1 
ATOM   8033 C CE2 . PHE B 1 471 ? -8.750  -7.140  10.689  1.00 19.08 ? 471 PHE B CE2 1 
ATOM   8034 C CZ  . PHE B 1 471 ? -7.870  -8.159  10.380  1.00 19.28 ? 471 PHE B CZ  1 
ATOM   8035 N N   . VAL B 1 472 ? -14.210 -7.802  6.817   1.00 21.69 ? 472 VAL B N   1 
ATOM   8036 C CA  . VAL B 1 472 ? -15.605 -7.909  6.389   1.00 19.77 ? 472 VAL B CA  1 
ATOM   8037 C C   . VAL B 1 472 ? -15.706 -8.707  5.100   1.00 20.06 ? 472 VAL B C   1 
ATOM   8038 O O   . VAL B 1 472 ? -16.598 -9.554  4.942   1.00 21.61 ? 472 VAL B O   1 
ATOM   8039 C CB  . VAL B 1 472 ? -16.227 -6.507  6.242   1.00 23.11 ? 472 VAL B CB  1 
ATOM   8040 C CG1 . VAL B 1 472 ? -17.489 -6.565  5.366   1.00 28.94 ? 472 VAL B CG1 1 
ATOM   8041 C CG2 . VAL B 1 472 ? -16.552 -5.937  7.628   1.00 22.51 ? 472 VAL B CG2 1 
ATOM   8042 N N   . ARG B 1 473 ? -14.799 -8.447  4.151   1.00 20.65 ? 473 ARG B N   1 
ATOM   8043 C CA  . ARG B 1 473 ? -14.804 -9.180  2.888   1.00 23.77 ? 473 ARG B CA  1 
ATOM   8044 C C   . ARG B 1 473 ? -14.481 -10.656 3.110   1.00 25.46 ? 473 ARG B C   1 
ATOM   8045 O O   . ARG B 1 473 ? -15.176 -11.548 2.604   1.00 24.49 ? 473 ARG B O   1 
ATOM   8046 C CB  . ARG B 1 473 ? -13.789 -8.541  1.937   1.00 23.53 ? 473 ARG B CB  1 
ATOM   8047 C CG  . ARG B 1 473 ? -13.872 -9.058  0.509   1.00 46.21 ? 473 ARG B CG  1 
ATOM   8048 C CD  . ARG B 1 473 ? -13.108 -8.165  -0.453  1.00 65.62 ? 473 ARG B CD  1 
ATOM   8049 N NE  . ARG B 1 473 ? -11.733 -8.614  -0.642  1.00 76.08 ? 473 ARG B NE  1 
ATOM   8050 C CZ  . ARG B 1 473 ? -11.212 -8.959  -1.817  1.00 83.68 ? 473 ARG B CZ  1 
ATOM   8051 N NH1 . ARG B 1 473 ? -11.956 -8.906  -2.916  1.00 87.11 ? 473 ARG B NH1 1 
ATOM   8052 N NH2 . ARG B 1 473 ? -9.949  -9.353  -1.897  1.00 85.13 ? 473 ARG B NH2 1 
ATOM   8053 N N   . ARG B 1 474 ? -13.434 -10.928 3.897   1.00 25.27 ? 474 ARG B N   1 
ATOM   8054 C CA  . ARG B 1 474 ? -13.005 -12.304 4.121   1.00 25.62 ? 474 ARG B CA  1 
ATOM   8055 C C   . ARG B 1 474 ? -14.055 -13.113 4.879   1.00 25.90 ? 474 ARG B C   1 
ATOM   8056 O O   . ARG B 1 474 ? -14.170 -14.332 4.678   1.00 25.28 ? 474 ARG B O   1 
ATOM   8057 C CB  . ARG B 1 474 ? -11.665 -12.291 4.869   1.00 28.12 ? 474 ARG B CB  1 
ATOM   8058 C CG  . ARG B 1 474 ? -11.095 -13.655 5.217   1.00 33.43 ? 474 ARG B CG  1 
ATOM   8059 C CD  . ARG B 1 474 ? -10.506 -14.373 4.008   1.00 43.91 ? 474 ARG B CD  1 
ATOM   8060 N NE  . ARG B 1 474 ? -9.913  -15.648 4.402   1.00 54.11 ? 474 ARG B NE  1 
ATOM   8061 C CZ  . ARG B 1 474 ? -10.615 -16.751 4.653   1.00 63.54 ? 474 ARG B CZ  1 
ATOM   8062 N NH1 . ARG B 1 474 ? -11.938 -16.741 4.537   1.00 60.16 ? 474 ARG B NH1 1 
ATOM   8063 N NH2 . ARG B 1 474 ? -9.993  -17.867 5.012   1.00 68.79 ? 474 ARG B NH2 1 
ATOM   8064 N N   . ALA B 1 475 ? -14.845 -12.456 5.732   1.00 25.05 ? 475 ALA B N   1 
ATOM   8065 C CA  . ALA B 1 475 ? -15.910 -13.136 6.465   1.00 24.91 ? 475 ALA B CA  1 
ATOM   8066 C C   . ALA B 1 475 ? -16.964 -13.729 5.542   1.00 30.41 ? 475 ALA B C   1 
ATOM   8067 O O   . ALA B 1 475 ? -17.677 -14.661 5.935   1.00 29.81 ? 475 ALA B O   1 
ATOM   8068 C CB  . ALA B 1 475 ? -16.581 -12.158 7.436   1.00 23.08 ? 475 ALA B CB  1 
ATOM   8069 N N   . GLN B 1 476 ? -17.090 -13.202 4.335   1.00 26.70 ? 476 GLN B N   1 
ATOM   8070 C CA  . GLN B 1 476 ? -18.133 -13.623 3.418   1.00 32.13 ? 476 GLN B CA  1 
ATOM   8071 C C   . GLN B 1 476 ? -17.632 -14.619 2.390   1.00 36.74 ? 476 GLN B C   1 
ATOM   8072 O O   . GLN B 1 476 ? -18.414 -15.058 1.543   1.00 36.08 ? 476 GLN B O   1 
ATOM   8073 C CB  . GLN B 1 476 ? -18.738 -12.398 2.723   1.00 28.74 ? 476 GLN B CB  1 
ATOM   8074 C CG  . GLN B 1 476 ? -19.338 -11.404 3.703   1.00 28.93 ? 476 GLN B CG  1 
ATOM   8075 C CD  . GLN B 1 476 ? -19.766 -10.122 3.041   1.00 34.16 ? 476 GLN B CD  1 
ATOM   8076 O OE1 . GLN B 1 476 ? -20.825 -10.061 2.403   1.00 34.23 ? 476 GLN B OE1 1 
ATOM   8077 N NE2 . GLN B 1 476 ? -18.951 -9.080  3.186   1.00 30.24 ? 476 GLN B NE2 1 
ATOM   8078 N N   . GLU B 1 477 ? -16.363 -15.004 2.462   1.00 40.34 ? 477 GLU B N   1 
ATOM   8079 C CA  . GLU B 1 477 ? -15.778 -15.931 1.500   1.00 51.79 ? 477 GLU B CA  1 
ATOM   8080 C C   . GLU B 1 477 ? -15.635 -17.330 2.094   1.00 57.90 ? 477 GLU B C   1 
ATOM   8081 O O   . GLU B 1 477 ? -15.567 -17.495 3.313   1.00 57.14 ? 477 GLU B O   1 
ATOM   8082 C CB  . GLU B 1 477 ? -14.415 -15.418 1.035   1.00 55.86 ? 477 GLU B CB  1 
ATOM   8083 C CG  . GLU B 1 477 ? -14.456 -14.040 0.394   1.00 61.41 ? 477 GLU B CG  1 
ATOM   8084 C CD  . GLU B 1 477 ? -13.103 -13.617 -0.150  1.00 63.86 ? 477 GLU B CD  1 
ATOM   8085 O OE1 . GLU B 1 477 ? -12.076 -14.060 0.411   1.00 65.02 ? 477 GLU B OE1 1 
ATOM   8086 O OE2 . GLU B 1 477 ? -13.069 -12.840 -1.132  1.00 65.74 ? 477 GLU B OE2 1 
HETATM 8087 C C1  . GLC C 2 .   ? 25.503  20.923  70.634  1.00 16.48 ? 1   GLC C C1  1 
HETATM 8088 C C2  . GLC C 2 .   ? 24.988  19.505  70.432  1.00 11.42 ? 1   GLC C C2  1 
HETATM 8089 C C3  . GLC C 2 .   ? 23.719  19.311  71.277  1.00 8.72  ? 1   GLC C C3  1 
HETATM 8090 C C4  . GLC C 2 .   ? 23.967  19.733  72.739  1.00 10.65 ? 1   GLC C C4  1 
HETATM 8091 C C5  . GLC C 2 .   ? 24.713  21.061  72.851  1.00 9.28  ? 1   GLC C C5  1 
HETATM 8092 C C6  . GLC C 2 .   ? 25.266  21.281  74.265  1.00 11.62 ? 1   GLC C C6  1 
HETATM 8093 O O1  . GLC C 2 .   ? 24.678  21.922  70.101  1.00 15.52 ? 1   GLC C O1  1 
HETATM 8094 O O2  . GLC C 2 .   ? 24.787  19.318  69.055  1.00 11.95 ? 1   GLC C O2  1 
HETATM 8095 O O3  . GLC C 2 .   ? 23.291  17.967  71.162  1.00 10.02 ? 1   GLC C O3  1 
HETATM 8096 O O4  . GLC C 2 .   ? 22.697  19.847  73.376  1.00 8.01  ? 1   GLC C O4  1 
HETATM 8097 O O5  . GLC C 2 .   ? 25.824  21.177  71.966  1.00 10.83 ? 1   GLC C O5  1 
HETATM 8098 O O6  . GLC C 2 .   ? 26.223  20.290  74.603  1.00 14.46 ? 1   GLC C O6  1 
HETATM 8099 C C1  . GLC C 2 .   ? 22.299  18.716  74.100  1.00 7.96  ? 2   GLC C C1  1 
HETATM 8100 C C2  . GLC C 2 .   ? 20.766  18.668  74.074  1.00 7.26  ? 2   GLC C C2  1 
HETATM 8101 C C3  . GLC C 2 .   ? 20.224  19.911  74.803  1.00 7.33  ? 2   GLC C C3  1 
HETATM 8102 C C4  . GLC C 2 .   ? 20.739  19.942  76.243  1.00 7.43  ? 2   GLC C C4  1 
HETATM 8103 C C5  . GLC C 2 .   ? 22.285  19.861  76.216  1.00 7.01  ? 2   GLC C C5  1 
HETATM 8104 C C6  . GLC C 2 .   ? 22.829  19.710  77.633  1.00 9.66  ? 2   GLC C C6  1 
HETATM 8105 O O2  . GLC C 2 .   ? 20.269  18.620  72.732  1.00 9.02  ? 2   GLC C O2  1 
HETATM 8106 O O3  . GLC C 2 .   ? 18.791  19.912  74.815  1.00 8.32  ? 2   GLC C O3  1 
HETATM 8107 O O4  . GLC C 2 .   ? 20.289  21.190  76.816  1.00 8.69  ? 2   GLC C O4  1 
HETATM 8108 O O5  . GLC C 2 .   ? 22.718  18.735  75.453  1.00 9.85  ? 2   GLC C O5  1 
HETATM 8109 O O6  . GLC C 2 .   ? 24.251  19.652  77.508  1.00 10.06 ? 2   GLC C O6  1 
HETATM 8110 C C1  . GLC C 2 .   ? 19.618  21.003  78.071  1.00 13.09 ? 3   GLC C C1  1 
HETATM 8111 C C2  . GLC C 2 .   ? 18.224  21.625  77.927  1.00 9.26  ? 3   GLC C C2  1 
HETATM 8112 C C3  . GLC C 2 .   ? 18.339  23.126  77.670  1.00 11.60 ? 3   GLC C C3  1 
HETATM 8113 C C4  . GLC C 2 .   ? 19.032  23.720  78.887  1.00 9.74  ? 3   GLC C C4  1 
HETATM 8114 C C5  . GLC C 2 .   ? 20.413  23.070  79.044  1.00 9.90  ? 3   GLC C C5  1 
HETATM 8115 C C6  . GLC C 2 .   ? 21.150  23.586  80.298  1.00 11.00 ? 3   GLC C C6  1 
HETATM 8116 O O2  . GLC C 2 .   ? 17.489  20.979  76.907  1.00 9.85  ? 3   GLC C O2  1 
HETATM 8117 O O3  . GLC C 2 .   ? 17.052  23.711  77.533  1.00 16.45 ? 3   GLC C O3  1 
HETATM 8118 O O4  . GLC C 2 .   ? 19.180  25.102  78.611  1.00 13.38 ? 3   GLC C O4  1 
HETATM 8119 O O5  . GLC C 2 .   ? 20.277  21.635  79.155  1.00 10.38 ? 3   GLC C O5  1 
HETATM 8120 O O6  . GLC C 2 .   ? 20.363  23.211  81.430  1.00 14.36 ? 3   GLC C O6  1 
HETATM 8121 C C1  . GLC C 2 .   ? 18.565  25.882  79.653  1.00 17.35 ? 4   GLC C C1  1 
HETATM 8122 C C2  . GLC C 2 .   ? 17.641  26.914  79.027  1.00 21.92 ? 4   GLC C C2  1 
HETATM 8123 C C3  . GLC C 2 .   ? 18.386  27.881  78.150  1.00 32.21 ? 4   GLC C C3  1 
HETATM 8124 C C4  . GLC C 2 .   ? 19.585  28.468  78.903  1.00 37.25 ? 4   GLC C C4  1 
HETATM 8125 C C5  . GLC C 2 .   ? 20.391  27.373  79.605  1.00 26.05 ? 4   GLC C C5  1 
HETATM 8126 C C6  . GLC C 2 .   ? 21.488  27.973  80.482  1.00 33.92 ? 4   GLC C C6  1 
HETATM 8127 O O2  . GLC C 2 .   ? 16.766  26.266  78.153  1.00 21.41 ? 4   GLC C O2  1 
HETATM 8128 O O3  . GLC C 2 .   ? 17.380  28.797  77.743  1.00 36.58 ? 4   GLC C O3  1 
HETATM 8129 O O4  . GLC C 2 .   ? 20.452  29.088  77.988  1.00 53.13 ? 4   GLC C O4  1 
HETATM 8130 O O5  . GLC C 2 .   ? 19.557  26.560  80.405  1.00 20.55 ? 4   GLC C O5  1 
HETATM 8131 O O6  . GLC C 2 .   ? 21.011  28.059  81.810  1.00 41.74 ? 4   GLC C O6  1 
HETATM 8132 C C1  . GLC C 2 .   ? 19.749  30.212  77.404  1.00 65.51 ? 5   GLC C C1  1 
HETATM 8133 C C2  . GLC C 2 .   ? 20.153  30.339  75.930  1.00 71.84 ? 5   GLC C C2  1 
HETATM 8134 C C3  . GLC C 2 .   ? 21.635  30.656  75.816  1.00 74.23 ? 5   GLC C C3  1 
HETATM 8135 C C4  . GLC C 2 .   ? 21.925  31.872  76.686  1.00 75.13 ? 5   GLC C C4  1 
HETATM 8136 C C5  . GLC C 2 .   ? 21.452  31.628  78.118  1.00 74.21 ? 5   GLC C C5  1 
HETATM 8137 C C6  . GLC C 2 .   ? 21.729  32.820  79.021  1.00 79.47 ? 5   GLC C C6  1 
HETATM 8138 O O2  . GLC C 2 .   ? 19.793  29.200  75.164  1.00 72.41 ? 5   GLC C O2  1 
HETATM 8139 O O3  . GLC C 2 .   ? 21.979  30.920  74.475  1.00 74.55 ? 5   GLC C O3  1 
HETATM 8140 O O4  . GLC C 2 .   ? 23.304  32.151  76.663  1.00 77.06 ? 5   GLC C O4  1 
HETATM 8141 O O5  . GLC C 2 .   ? 20.065  31.399  78.107  1.00 68.86 ? 5   GLC C O5  1 
HETATM 8142 O O6  . GLC C 2 .   ? 21.132  33.967  78.457  1.00 81.93 ? 5   GLC C O6  1 
HETATM 8143 C C1  . GLC D 3 .   ? 28.230  29.132  65.341  1.00 49.47 ? 1   GLC D C1  1 
HETATM 8144 C C2  . GLC D 3 .   ? 27.537  28.367  64.250  1.00 45.92 ? 1   GLC D C2  1 
HETATM 8145 C C3  . GLC D 3 .   ? 26.313  27.625  64.741  1.00 37.90 ? 1   GLC D C3  1 
HETATM 8146 C C4  . GLC D 3 .   ? 26.639  26.822  65.978  1.00 37.19 ? 1   GLC D C4  1 
HETATM 8147 C C5  . GLC D 3 .   ? 27.289  27.718  67.015  1.00 48.79 ? 1   GLC D C5  1 
HETATM 8148 C C6  . GLC D 3 .   ? 27.715  27.021  68.316  1.00 57.95 ? 1   GLC D C6  1 
HETATM 8149 O O1  . GLC D 3 .   ? 27.533  30.294  65.696  1.00 56.42 ? 1   GLC D O1  1 
HETATM 8150 O O2  . GLC D 3 .   ? 27.185  29.363  63.319  1.00 43.77 ? 1   GLC D O2  1 
HETATM 8151 O O3  . GLC D 3 .   ? 25.861  26.770  63.732  1.00 26.40 ? 1   GLC D O3  1 
HETATM 8152 O O4  . GLC D 3 .   ? 25.391  26.345  66.464  1.00 39.74 ? 1   GLC D O4  1 
HETATM 8153 O O5  . GLC D 3 .   ? 28.425  28.350  66.497  1.00 47.83 ? 1   GLC D O5  1 
HETATM 8154 O O6  . GLC D 3 .   ? 28.552  25.866  68.182  1.00 60.06 ? 1   GLC D O6  1 
HETATM 8155 C C1  . GLC D 3 .   ? 25.391  24.968  66.789  1.00 38.01 ? 2   GLC D C1  1 
HETATM 8156 C C2  . GLC D 3 .   ? 24.186  24.344  66.118  1.00 33.18 ? 2   GLC D C2  1 
HETATM 8157 C C3  . GLC D 3 .   ? 22.922  24.903  66.727  1.00 35.59 ? 2   GLC D C3  1 
HETATM 8158 C C4  . GLC D 3 .   ? 22.939  24.941  68.241  1.00 34.82 ? 2   GLC D C4  1 
HETATM 8159 C C5  . GLC D 3 .   ? 24.251  25.489  68.757  1.00 40.42 ? 2   GLC D C5  1 
HETATM 8160 C C6  . GLC D 3 .   ? 24.307  25.617  70.273  1.00 43.87 ? 2   GLC D C6  1 
HETATM 8161 O O2  . GLC D 3 .   ? 24.139  24.709  64.774  1.00 30.73 ? 2   GLC D O2  1 
HETATM 8162 O O3  . GLC D 3 .   ? 21.809  24.104  66.317  1.00 29.48 ? 2   GLC D O3  1 
HETATM 8163 O O4  . GLC D 3 .   ? 21.824  25.763  68.548  1.00 36.70 ? 2   GLC D O4  1 
HETATM 8164 O O5  . GLC D 3 .   ? 25.333  24.785  68.203  1.00 39.40 ? 2   GLC D O5  1 
HETATM 8165 O O6  . GLC D 3 .   ? 24.088  24.360  70.895  1.00 47.99 ? 2   GLC D O6  1 
HETATM 8166 C C1  . GLC D 3 .   ? 20.888  25.137  69.379  1.00 37.05 ? 3   GLC D C1  1 
HETATM 8167 C C2  . GLC D 3 .   ? 19.499  25.492  68.840  1.00 27.37 ? 3   GLC D C2  1 
HETATM 8168 C C3  . GLC D 3 .   ? 19.278  26.989  68.925  1.00 30.43 ? 3   GLC D C3  1 
HETATM 8169 C C4  . GLC D 3 .   ? 19.520  27.447  70.336  1.00 41.01 ? 3   GLC D C4  1 
HETATM 8170 C C5  . GLC D 3 .   ? 20.927  27.085  70.721  1.00 46.86 ? 3   GLC D C5  1 
HETATM 8171 C C6  . GLC D 3 .   ? 21.202  27.482  72.143  1.00 57.72 ? 3   GLC D C6  1 
HETATM 8172 O O2  . GLC D 3 .   ? 19.358  25.128  67.526  1.00 25.23 ? 3   GLC D O2  1 
HETATM 8173 O O3  . GLC D 3 .   ? 17.943  27.274  68.597  1.00 23.06 ? 3   GLC D O3  1 
HETATM 8174 O O4  . GLC D 3 .   ? 19.381  28.839  70.373  1.00 51.38 ? 3   GLC D O4  1 
HETATM 8175 O O5  . GLC D 3 .   ? 20.968  25.675  70.690  1.00 45.10 ? 3   GLC D O5  1 
HETATM 8176 O O6  . GLC D 3 .   ? 20.692  26.328  72.802  1.00 61.81 ? 3   GLC D O6  1 
HETATM 8177 C C1  . GLC D 3 .   ? 18.174  29.209  70.977  1.00 55.97 ? 4   GLC D C1  1 
HETATM 8178 C C2  . GLC D 3 .   ? 17.349  30.148  70.037  1.00 54.16 ? 4   GLC D C2  1 
HETATM 8179 C C3  . GLC D 3 .   ? 17.984  31.529  70.059  1.00 60.74 ? 4   GLC D C3  1 
HETATM 8180 C C4  . GLC D 3 .   ? 17.723  31.952  71.455  1.00 62.87 ? 4   GLC D C4  1 
HETATM 8181 C C5  . GLC D 3 .   ? 18.870  31.214  72.147  1.00 62.30 ? 4   GLC D C5  1 
HETATM 8182 C C6  . GLC D 3 .   ? 19.367  31.963  73.351  1.00 62.88 ? 4   GLC D C6  1 
HETATM 8183 O O2  . GLC D 3 .   ? 17.253  29.706  68.739  1.00 46.73 ? 4   GLC D O2  1 
HETATM 8184 O O3  . GLC D 3 .   ? 17.519  32.480  69.095  1.00 65.05 ? 4   GLC D O3  1 
HETATM 8185 O O4  . GLC D 3 .   ? 17.684  33.352  71.548  1.00 67.01 ? 4   GLC D O4  1 
HETATM 8186 O O5  . GLC D 3 .   ? 18.505  29.804  72.265  1.00 61.29 ? 4   GLC D O5  1 
HETATM 8187 O O6  . GLC D 3 .   ? 20.172  32.943  72.731  1.00 63.30 ? 4   GLC D O6  1 
HETATM 8188 C C1  . GLC E 2 .   ? -9.631  1.867   24.508  1.00 18.21 ? 1   GLC E C1  1 
HETATM 8189 C C2  . GLC E 2 .   ? -9.101  0.471   24.760  1.00 11.59 ? 1   GLC E C2  1 
HETATM 8190 C C3  . GLC E 2 .   ? -7.705  0.329   24.156  1.00 12.14 ? 1   GLC E C3  1 
HETATM 8191 C C4  . GLC E 2 .   ? -7.749  0.655   22.676  1.00 11.73 ? 1   GLC E C4  1 
HETATM 8192 C C5  . GLC E 2 .   ? -8.486  1.955   22.402  1.00 15.88 ? 1   GLC E C5  1 
HETATM 8193 C C6  . GLC E 2 .   ? -8.789  2.150   20.911  1.00 14.91 ? 1   GLC E C6  1 
HETATM 8194 O O1  . GLC E 2 .   ? -8.945  2.870   25.197  1.00 20.35 ? 1   GLC E O1  1 
HETATM 8195 O O2  . GLC E 2 .   ? -9.177  0.118   26.130  1.00 14.20 ? 1   GLC E O2  1 
HETATM 8196 O O3  . GLC E 2 .   ? -7.278  -0.999  24.384  1.00 14.18 ? 1   GLC E O3  1 
HETATM 8197 O O4  . GLC E 2 .   ? -6.426  0.888   22.239  1.00 12.33 ? 1   GLC E O4  1 
HETATM 8198 O O5  . GLC E 2 .   ? -9.693  2.050   23.120  1.00 15.85 ? 1   GLC E O5  1 
HETATM 8199 O O6  . GLC E 2 .   ? -9.676  1.182   20.436  1.00 17.37 ? 1   GLC E O6  1 
HETATM 8200 C C1  . GLC E 2 .   ? -5.831  -0.251  21.672  1.00 11.30 ? 2   GLC E C1  1 
HETATM 8201 C C2  . GLC E 2 .   ? -4.336  -0.232  21.990  1.00 15.94 ? 2   GLC E C2  1 
HETATM 8202 C C3  . GLC E 2 .   ? -3.704  1.001   21.357  1.00 13.61 ? 2   GLC E C3  1 
HETATM 8203 C C4  . GLC E 2 .   ? -3.889  0.984   19.848  1.00 10.24 ? 2   GLC E C4  1 
HETATM 8204 C C5  . GLC E 2 .   ? -5.402  0.891   19.624  1.00 11.88 ? 2   GLC E C5  1 
HETATM 8205 C C6  . GLC E 2 .   ? -5.703  0.756   18.134  1.00 16.31 ? 2   GLC E C6  1 
HETATM 8206 O O2  . GLC E 2 .   ? -4.116  -0.284  23.410  1.00 12.71 ? 2   GLC E O2  1 
HETATM 8207 O O3  . GLC E 2 .   ? -2.296  1.103   21.629  1.00 12.83 ? 2   GLC E O3  1 
HETATM 8208 O O4  . GLC E 2 .   ? -3.489  2.248   19.389  1.00 11.84 ? 2   GLC E O4  1 
HETATM 8209 O O5  . GLC E 2 .   ? -5.974  -0.235  20.259  1.00 12.03 ? 2   GLC E O5  1 
HETATM 8210 O O6  . GLC E 2 .   ? -7.111  0.796   17.985  1.00 15.24 ? 2   GLC E O6  1 
HETATM 8211 C C1  . GLC E 2 .   ? -2.531  2.218   18.307  1.00 14.82 ? 3   GLC E C1  1 
HETATM 8212 C C2  . GLC E 2 .   ? -1.223  2.896   18.721  1.00 14.68 ? 3   GLC E C2  1 
HETATM 8213 C C3  . GLC E 2 .   ? -1.416  4.400   18.998  1.00 17.30 ? 3   GLC E C3  1 
HETATM 8214 C C4  . GLC E 2 .   ? -1.962  5.029   17.725  1.00 13.18 ? 3   GLC E C4  1 
HETATM 8215 C C5  . GLC E 2 .   ? -3.228  4.298   17.282  1.00 11.48 ? 3   GLC E C5  1 
HETATM 8216 C C6  . GLC E 2 .   ? -3.764  4.836   15.939  1.00 15.57 ? 3   GLC E C6  1 
HETATM 8217 O O2  . GLC E 2 .   ? -0.651  2.221   19.833  1.00 12.75 ? 3   GLC E O2  1 
HETATM 8218 O O3  . GLC E 2 .   ? -0.246  5.121   19.383  1.00 19.04 ? 3   GLC E O3  1 
HETATM 8219 O O4  . GLC E 2 .   ? -2.239  6.401   17.982  1.00 17.06 ? 3   GLC E O4  1 
HETATM 8220 O O5  . GLC E 2 .   ? -3.042  2.884   17.149  1.00 13.55 ? 3   GLC E O5  1 
HETATM 8221 O O6  . GLC E 2 .   ? -2.811  4.629   14.901  1.00 16.03 ? 3   GLC E O6  1 
HETATM 8222 C C1  . GLC E 2 .   ? -1.564  7.281   17.064  1.00 20.30 ? 4   GLC E C1  1 
HETATM 8223 C C2  . GLC E 2 .   ? -0.749  8.288   17.869  1.00 24.17 ? 4   GLC E C2  1 
HETATM 8224 C C3  . GLC E 2 .   ? -1.659  9.117   18.753  1.00 33.97 ? 4   GLC E C3  1 
HETATM 8225 C C4  . GLC E 2 .   ? -2.717  9.816   17.914  1.00 36.07 ? 4   GLC E C4  1 
HETATM 8226 C C5  . GLC E 2 .   ? -3.395  8.832   16.961  1.00 34.34 ? 4   GLC E C5  1 
HETATM 8227 C C6  . GLC E 2 .   ? -4.226  9.623   15.954  1.00 45.14 ? 4   GLC E C6  1 
HETATM 8228 O O2  . GLC E 2 .   ? 0.127   7.583   18.719  1.00 22.61 ? 4   GLC E O2  1 
HETATM 8229 O O3  . GLC E 2 .   ? -0.870  10.054  19.443  1.00 37.54 ? 4   GLC E O3  1 
HETATM 8230 O O4  . GLC E 2 .   ? -3.689  10.374  18.777  1.00 47.72 ? 4   GLC E O4  1 
HETATM 8231 O O5  . GLC E 2 .   ? -2.488  7.993   16.249  1.00 22.40 ? 4   GLC E O5  1 
HETATM 8232 O O6  . GLC E 2 .   ? -4.519  8.781   14.866  1.00 47.77 ? 4   GLC E O6  1 
HETATM 8233 C C1  . GLC E 2 .   ? -3.408  11.771  19.028  1.00 57.99 ? 5   GLC E C1  1 
HETATM 8234 C C2  . GLC E 2 .   ? -3.725  12.109  20.499  1.00 65.08 ? 5   GLC E C2  1 
HETATM 8235 C C3  . GLC E 2 .   ? -5.218  12.195  20.795  1.00 71.83 ? 5   GLC E C3  1 
HETATM 8236 C C4  . GLC E 2 .   ? -5.981  12.939  19.702  1.00 69.73 ? 5   GLC E C4  1 
HETATM 8237 C C5  . GLC E 2 .   ? -5.572  12.440  18.323  1.00 62.84 ? 5   GLC E C5  1 
HETATM 8238 C C6  . GLC E 2 .   ? -6.287  13.229  17.234  1.00 65.11 ? 5   GLC E C6  1 
HETATM 8239 O O2  . GLC E 2 .   ? -3.163  11.148  21.377  1.00 63.73 ? 5   GLC E O2  1 
HETATM 8240 O O3  . GLC E 2 .   ? -5.396  12.849  22.035  1.00 77.30 ? 5   GLC E O3  1 
HETATM 8241 O O4  . GLC E 2 .   ? -7.372  12.758  19.875  1.00 71.03 ? 5   GLC E O4  1 
HETATM 8242 O O5  . GLC E 2 .   ? -4.180  12.593  18.166  1.00 60.31 ? 5   GLC E O5  1 
HETATM 8243 O O6  . GLC E 2 .   ? -7.621  13.463  17.632  1.00 66.14 ? 5   GLC E O6  1 
HETATM 8244 C C2  . BGC F 4 .   ? -12.775 9.839   30.294  1.00 75.94 ? 1   BGC G C2  1 
HETATM 8245 C C3  . BGC F 4 .   ? -11.754 8.735   30.542  1.00 74.74 ? 1   BGC G C3  1 
HETATM 8246 C C4  . BGC F 4 .   ? -11.620 7.794   29.340  1.00 77.12 ? 1   BGC G C4  1 
HETATM 8247 C C5  . BGC F 4 .   ? -11.640 8.559   28.011  1.00 79.79 ? 1   BGC G C5  1 
HETATM 8248 C C6  . BGC F 4 .   ? -12.178 7.761   26.828  1.00 83.87 ? 1   BGC G C6  1 
HETATM 8249 C C1  . BGC F 4 .   ? -12.309 10.609  29.077  1.00 76.62 ? 1   BGC G C1  1 
HETATM 8250 O O1  . BGC F 4 .   ? -13.119 11.746  28.868  1.00 75.12 ? 1   BGC G O1  1 
HETATM 8251 O O2  . BGC F 4 .   ? -12.862 10.706  31.398  1.00 76.24 ? 1   BGC G O2  1 
HETATM 8252 O O3  . BGC F 4 .   ? -12.078 8.015   31.709  1.00 71.34 ? 1   BGC G O3  1 
HETATM 8253 O O4  . BGC F 4 .   ? -10.348 7.182   29.461  1.00 76.13 ? 1   BGC G O4  1 
HETATM 8254 O O5  . BGC F 4 .   ? -12.448 9.726   27.997  1.00 78.74 ? 1   BGC G O5  1 
HETATM 8255 O O6  . BGC F 4 .   ? -12.212 6.355   26.906  1.00 85.62 ? 1   BGC G O6  1 
HETATM 8256 C C1  . GLC F 4 .   ? -10.298 5.807   28.998  1.00 70.93 ? 2   GLC G C1  1 
HETATM 8257 C C2  . GLC F 4 .   ? -9.183  5.096   29.753  1.00 66.81 ? 2   GLC G C2  1 
HETATM 8258 C C3  . GLC F 4 .   ? -7.790  5.550   29.328  1.00 61.41 ? 2   GLC G C3  1 
HETATM 8259 C C4  . GLC F 4 .   ? -7.619  5.633   27.812  1.00 64.02 ? 2   GLC G C4  1 
HETATM 8260 C C5  . GLC F 4 .   ? -8.827  6.278   27.140  1.00 67.01 ? 2   GLC G C5  1 
HETATM 8261 C C6  . GLC F 4 .   ? -8.724  6.141   25.619  1.00 65.22 ? 2   GLC G C6  1 
HETATM 8262 O O2  . GLC F 4 .   ? -9.362  5.393   31.115  1.00 68.02 ? 2   GLC G O2  1 
HETATM 8263 O O3  . GLC F 4 .   ? -6.846  4.646   29.858  1.00 45.21 ? 2   GLC G O3  1 
HETATM 8264 O O4  . GLC F 4 .   ? -6.493  6.437   27.539  1.00 64.24 ? 2   GLC G O4  1 
HETATM 8265 O O5  . GLC F 4 .   ? -10.036 5.703   27.596  1.00 68.48 ? 2   GLC G O5  1 
HETATM 8266 O O6  . GLC F 4 .   ? -9.869  6.690   25.011  1.00 61.22 ? 2   GLC G O6  1 
HETATM 8267 C C1  . GLC F 4 .   ? -5.411  5.688   26.950  1.00 61.19 ? 3   GLC G C1  1 
HETATM 8268 C C2  . GLC F 4 .   ? -4.133  6.105   27.675  1.00 51.21 ? 3   GLC G C2  1 
HETATM 8269 C C3  . GLC F 4 .   ? -3.879  7.583   27.395  1.00 57.28 ? 3   GLC G C3  1 
HETATM 8270 C C4  . GLC F 4 .   ? -3.746  7.782   25.893  1.00 60.82 ? 3   GLC G C4  1 
HETATM 8271 C C5  . GLC F 4 .   ? -5.043  7.307   25.234  1.00 64.92 ? 3   GLC G C5  1 
HETATM 8272 C C6  . GLC F 4 .   ? -5.022  7.489   23.716  1.00 67.20 ? 3   GLC G C6  1 
HETATM 8273 O O2  . GLC F 4 .   ? -4.300  5.875   29.051  1.00 37.07 ? 3   GLC G O2  1 
HETATM 8274 O O3  . GLC F 4 .   ? -2.744  8.091   28.064  1.00 50.61 ? 3   GLC G O3  1 
HETATM 8275 O O4  . GLC F 4 .   ? -3.481  9.137   25.608  1.00 60.55 ? 3   GLC G O4  1 
HETATM 8276 O O5  . GLC F 4 .   ? -5.288  5.946   25.559  1.00 64.66 ? 3   GLC G O5  1 
HETATM 8277 O O6  . GLC F 4 .   ? -4.021  6.688   23.124  1.00 66.52 ? 3   GLC G O6  1 
HETATM 8278 C C1  . GOL G 5 .   ? 7.006   19.681  66.538  1.00 31.76 ? 501 GOL A C1  1 
HETATM 8279 O O1  . GOL G 5 .   ? 7.566   20.907  66.236  1.00 21.05 ? 501 GOL A O1  1 
HETATM 8280 C C2  . GOL G 5 .   ? 7.317   19.369  67.914  1.00 33.29 ? 501 GOL A C2  1 
HETATM 8281 O O2  . GOL G 5 .   ? 6.228   18.833  68.601  1.00 12.21 ? 501 GOL A O2  1 
HETATM 8282 C C3  . GOL G 5 .   ? 8.586   18.494  67.834  1.00 35.67 ? 501 GOL A C3  1 
HETATM 8283 O O3  . GOL G 5 .   ? 9.661   19.343  67.648  1.00 16.61 ? 501 GOL A O3  1 
HETATM 8284 C C1  . GOL H 5 .   ? 7.608   0.301   64.358  1.00 52.15 ? 502 GOL A C1  1 
HETATM 8285 O O1  . GOL H 5 .   ? 6.472   0.181   65.156  1.00 52.09 ? 502 GOL A O1  1 
HETATM 8286 C C2  . GOL H 5 .   ? 7.472   -0.714  63.179  1.00 48.99 ? 502 GOL A C2  1 
HETATM 8287 O O2  . GOL H 5 .   ? 8.700   -1.067  62.685  1.00 49.33 ? 502 GOL A O2  1 
HETATM 8288 C C3  . GOL H 5 .   ? 6.613   -0.006  62.098  1.00 49.45 ? 502 GOL A C3  1 
HETATM 8289 O O3  . GOL H 5 .   ? 5.345   -0.536  62.179  1.00 47.86 ? 502 GOL A O3  1 
HETATM 8290 C C1  . GOL I 5 .   ? 1.819   27.536  74.641  1.00 34.03 ? 503 GOL A C1  1 
HETATM 8291 O O1  . GOL I 5 .   ? 2.181   26.163  74.755  1.00 25.83 ? 503 GOL A O1  1 
HETATM 8292 C C2  . GOL I 5 .   ? 0.391   27.691  74.024  1.00 45.56 ? 503 GOL A C2  1 
HETATM 8293 O O2  . GOL I 5 .   ? -0.611  27.203  74.844  1.00 57.36 ? 503 GOL A O2  1 
HETATM 8294 C C3  . GOL I 5 .   ? 0.405   27.003  72.642  1.00 43.98 ? 503 GOL A C3  1 
HETATM 8295 O O3  . GOL I 5 .   ? 1.728   26.841  72.256  1.00 50.59 ? 503 GOL A O3  1 
HETATM 8296 C C1  . GOL J 5 .   ? 14.830  -2.934  62.743  1.00 35.94 ? 504 GOL A C1  1 
HETATM 8297 O O1  . GOL J 5 .   ? 15.147  -3.129  64.115  1.00 17.21 ? 504 GOL A O1  1 
HETATM 8298 C C2  . GOL J 5 .   ? 15.179  -1.516  62.194  1.00 35.77 ? 504 GOL A C2  1 
HETATM 8299 O O2  . GOL J 5 .   ? 14.124  -0.715  62.305  1.00 37.93 ? 504 GOL A O2  1 
HETATM 8300 C C3  . GOL J 5 .   ? 15.505  -1.723  60.682  1.00 44.34 ? 504 GOL A C3  1 
HETATM 8301 O O3  . GOL J 5 .   ? 16.797  -1.290  60.437  1.00 37.56 ? 504 GOL A O3  1 
HETATM 8302 C C1  . GOL K 5 .   ? 6.583   0.666   29.805  1.00 30.58 ? 501 GOL B C1  1 
HETATM 8303 O O1  . GOL K 5 .   ? 5.387   0.323   30.358  1.00 17.83 ? 501 GOL B O1  1 
HETATM 8304 C C2  . GOL K 5 .   ? 7.767   0.118   30.632  1.00 31.44 ? 501 GOL B C2  1 
HETATM 8305 O O2  . GOL K 5 .   ? 8.914   0.006   29.845  1.00 15.50 ? 501 GOL B O2  1 
HETATM 8306 C C3  . GOL K 5 .   ? 7.979   1.179   31.679  1.00 28.77 ? 501 GOL B C3  1 
HETATM 8307 O O3  . GOL K 5 .   ? 6.797   1.813   31.932  1.00 28.29 ? 501 GOL B O3  1 
HETATM 8308 O O   . HOH L 6 .   ? 42.362  23.238  48.710  1.00 53.12 ? 601 HOH A O   1 
HETATM 8309 O O   . HOH L 6 .   ? -0.023  24.537  66.079  1.00 43.06 ? 602 HOH A O   1 
HETATM 8310 O O   . HOH L 6 .   ? 1.299   19.977  50.202  1.00 34.05 ? 603 HOH A O   1 
HETATM 8311 O O   . HOH L 6 .   ? 25.033  5.802   62.172  1.00 75.43 ? 604 HOH A O   1 
HETATM 8312 O O   . HOH L 6 .   ? 1.308   9.528   65.677  1.00 30.19 ? 605 HOH A O   1 
HETATM 8313 O O   . HOH L 6 .   ? 2.826   7.983   53.195  1.00 57.77 ? 606 HOH A O   1 
HETATM 8314 O O   . HOH L 6 .   ? 19.484  4.463   58.010  1.00 20.13 ? 607 HOH A O   1 
HETATM 8315 O O   . HOH L 6 .   ? 17.194  27.064  75.202  1.00 40.62 ? 608 HOH A O   1 
HETATM 8316 O O   . HOH L 6 .   ? 13.221  14.416  41.489  1.00 70.71 ? 609 HOH A O   1 
HETATM 8317 O O   . HOH L 6 .   ? -10.826 17.130  83.359  1.00 42.20 ? 610 HOH A O   1 
HETATM 8318 O O   . HOH L 6 .   ? 43.752  11.098  47.715  1.00 49.42 ? 611 HOH A O   1 
HETATM 8319 O O   . HOH L 6 .   ? 6.372   9.465   86.882  1.00 58.36 ? 612 HOH A O   1 
HETATM 8320 O O   . HOH L 6 .   ? 16.919  6.139   87.492  1.00 21.37 ? 613 HOH A O   1 
HETATM 8321 O O   . HOH L 6 .   ? 35.148  15.346  74.632  1.00 34.64 ? 614 HOH A O   1 
HETATM 8322 O O   . HOH L 6 .   ? 3.431   37.614  54.198  1.00 31.77 ? 615 HOH A O   1 
HETATM 8323 O O   . HOH L 6 .   ? 29.714  7.912   48.786  1.00 33.28 ? 616 HOH A O   1 
HETATM 8324 O O   . HOH L 6 .   ? 35.154  22.755  45.528  1.00 38.04 ? 617 HOH A O   1 
HETATM 8325 O O   . HOH L 6 .   ? 17.783  15.378  37.414  1.00 44.07 ? 618 HOH A O   1 
HETATM 8326 O O   . HOH L 6 .   ? 17.570  1.322   56.051  1.00 45.18 ? 619 HOH A O   1 
HETATM 8327 O O   . HOH L 6 .   ? 27.551  28.725  84.203  1.00 43.89 ? 620 HOH A O   1 
HETATM 8328 O O   . HOH L 6 .   ? 44.313  29.560  75.960  1.00 35.98 ? 621 HOH A O   1 
HETATM 8329 O O   . HOH L 6 .   ? 37.007  10.732  42.618  1.00 30.96 ? 622 HOH A O   1 
HETATM 8330 O O   . HOH L 6 .   ? 50.007  24.205  77.402  1.00 28.18 ? 623 HOH A O   1 
HETATM 8331 O O   . HOH L 6 .   ? 12.163  16.191  93.821  1.00 23.41 ? 624 HOH A O   1 
HETATM 8332 O O   . HOH L 6 .   ? 26.219  29.045  54.051  1.00 28.62 ? 625 HOH A O   1 
HETATM 8333 O O   . HOH L 6 .   ? 8.962   5.325   51.251  1.00 32.99 ? 626 HOH A O   1 
HETATM 8334 O O   . HOH L 6 .   ? 11.015  33.361  70.595  1.00 45.25 ? 627 HOH A O   1 
HETATM 8335 O O   . HOH L 6 .   ? 42.195  23.264  65.503  1.00 20.81 ? 628 HOH A O   1 
HETATM 8336 O O   . HOH L 6 .   ? -5.456  9.561   88.257  1.00 46.25 ? 629 HOH A O   1 
HETATM 8337 O O   . HOH L 6 .   ? 24.736  5.089   78.937  1.00 24.40 ? 630 HOH A O   1 
HETATM 8338 O O   . HOH L 6 .   ? 2.228   12.580  62.538  1.00 22.93 ? 631 HOH A O   1 
HETATM 8339 O O   . HOH L 6 .   ? 12.978  23.138  71.667  1.00 13.42 ? 632 HOH A O   1 
HETATM 8340 O O   . HOH L 6 .   ? 21.228  32.659  42.045  1.00 38.08 ? 633 HOH A O   1 
HETATM 8341 O O   . HOH L 6 .   ? 30.260  27.699  83.804  1.00 57.17 ? 634 HOH A O   1 
HETATM 8342 O O   . HOH L 6 .   ? 49.274  24.896  75.160  1.00 30.98 ? 635 HOH A O   1 
HETATM 8343 O O   . HOH L 6 .   ? 20.791  0.102   58.740  1.00 44.14 ? 636 HOH A O   1 
HETATM 8344 O O   . HOH L 6 .   ? 32.180  12.161  40.307  1.00 45.68 ? 637 HOH A O   1 
HETATM 8345 O O   . HOH L 6 .   ? 7.344   31.780  65.737  1.00 17.54 ? 638 HOH A O   1 
HETATM 8346 O O   . HOH L 6 .   ? -5.467  19.935  100.958 1.00 44.30 ? 639 HOH A O   1 
HETATM 8347 O O   . HOH L 6 .   ? -5.807  23.927  90.602  1.00 23.79 ? 640 HOH A O   1 
HETATM 8348 O O   . HOH L 6 .   ? -0.991  20.206  63.869  1.00 34.09 ? 641 HOH A O   1 
HETATM 8349 O O   . HOH L 6 .   ? 10.574  18.325  47.246  1.00 24.27 ? 642 HOH A O   1 
HETATM 8350 O O   . HOH L 6 .   ? 40.997  1.268   66.352  1.00 48.54 ? 643 HOH A O   1 
HETATM 8351 O O   . HOH L 6 .   ? 15.275  15.704  87.102  1.00 15.53 ? 644 HOH A O   1 
HETATM 8352 O O   . HOH L 6 .   ? -6.160  10.817  85.792  1.00 25.43 ? 645 HOH A O   1 
HETATM 8353 O O   . HOH L 6 .   ? 45.271  16.878  62.485  1.00 36.24 ? 646 HOH A O   1 
HETATM 8354 O O   . HOH L 6 .   ? 43.607  7.282   48.908  1.00 25.82 ? 647 HOH A O   1 
HETATM 8355 O O   . HOH L 6 .   ? 16.572  36.381  51.968  1.00 45.36 ? 648 HOH A O   1 
HETATM 8356 O O   . HOH L 6 .   ? 16.871  5.578   51.090  1.00 21.60 ? 649 HOH A O   1 
HETATM 8357 O O   . HOH L 6 .   ? 10.228  8.305   85.208  1.00 43.90 ? 650 HOH A O   1 
HETATM 8358 O O   . HOH L 6 .   ? 9.169   -0.991  85.205  1.00 51.28 ? 651 HOH A O   1 
HETATM 8359 O O   . HOH L 6 .   ? 3.710   15.306  73.996  1.00 18.60 ? 652 HOH A O   1 
HETATM 8360 O O   . HOH L 6 .   ? 1.381   12.057  65.106  1.00 24.57 ? 653 HOH A O   1 
HETATM 8361 O O   . HOH L 6 .   ? 3.538   5.876   66.474  1.00 26.14 ? 654 HOH A O   1 
HETATM 8362 O O   . HOH L 6 .   ? 16.624  35.911  55.720  1.00 28.97 ? 655 HOH A O   1 
HETATM 8363 O O   . HOH L 6 .   ? 13.185  -0.290  53.793  1.00 28.83 ? 656 HOH A O   1 
HETATM 8364 O O   . HOH L 6 .   ? 3.904   21.860  100.189 1.00 30.08 ? 657 HOH A O   1 
HETATM 8365 O O   . HOH L 6 .   ? 5.015   6.787   58.256  1.00 47.15 ? 658 HOH A O   1 
HETATM 8366 O O   . HOH L 6 .   ? -11.237 22.551  87.571  1.00 48.16 ? 659 HOH A O   1 
HETATM 8367 O O   . HOH L 6 .   ? 14.116  5.892   50.474  1.00 26.35 ? 660 HOH A O   1 
HETATM 8368 O O   . HOH L 6 .   ? 38.089  29.172  61.907  1.00 45.33 ? 661 HOH A O   1 
HETATM 8369 O O   . HOH L 6 .   ? 38.520  28.677  75.577  1.00 33.36 ? 662 HOH A O   1 
HETATM 8370 O O   . HOH L 6 .   ? 24.904  -1.564  56.858  1.00 52.08 ? 663 HOH A O   1 
HETATM 8371 O O   . HOH L 6 .   ? 29.337  19.639  50.646  1.00 16.97 ? 664 HOH A O   1 
HETATM 8372 O O   . HOH L 6 .   ? 16.190  23.130  74.993  1.00 21.58 ? 665 HOH A O   1 
HETATM 8373 O O   . HOH L 6 .   ? 8.531   27.229  107.077 1.00 56.20 ? 666 HOH A O   1 
HETATM 8374 O O   . HOH L 6 .   ? 38.512  3.143   78.655  1.00 42.77 ? 667 HOH A O   1 
HETATM 8375 O O   . HOH L 6 .   ? 45.223  4.823   73.766  1.00 26.86 ? 668 HOH A O   1 
HETATM 8376 O O   . HOH L 6 .   ? 5.994   3.054   65.062  1.00 25.39 ? 669 HOH A O   1 
HETATM 8377 O O   . HOH L 6 .   ? 10.486  16.568  43.912  1.00 52.43 ? 670 HOH A O   1 
HETATM 8378 O O   . HOH L 6 .   ? 3.215   4.946   63.825  1.00 34.80 ? 671 HOH A O   1 
HETATM 8379 O O   . HOH L 6 .   ? -3.840  22.432  70.616  1.00 31.89 ? 672 HOH A O   1 
HETATM 8380 O O   . HOH L 6 .   ? 32.165  10.300  42.066  1.00 33.07 ? 673 HOH A O   1 
HETATM 8381 O O   . HOH L 6 .   ? 46.582  12.555  74.863  1.00 27.17 ? 674 HOH A O   1 
HETATM 8382 O O   . HOH L 6 .   ? 16.248  30.708  79.218  1.00 34.24 ? 675 HOH A O   1 
HETATM 8383 O O   . HOH L 6 .   ? -1.602  14.275  62.244  1.00 34.34 ? 676 HOH A O   1 
HETATM 8384 O O   . HOH L 6 .   ? 16.101  15.159  53.778  1.00 11.02 ? 677 HOH A O   1 
HETATM 8385 O O   . HOH L 6 .   ? 26.501  18.442  43.467  1.00 17.24 ? 678 HOH A O   1 
HETATM 8386 O O   . HOH L 6 .   ? 45.300  10.842  73.133  1.00 19.32 ? 679 HOH A O   1 
HETATM 8387 O O   . HOH L 6 .   ? 3.019   14.602  71.186  1.00 16.65 ? 680 HOH A O   1 
HETATM 8388 O O   . HOH L 6 .   ? 34.169  13.469  65.595  1.00 14.50 ? 681 HOH A O   1 
HETATM 8389 O O   . HOH L 6 .   ? 0.802   16.376  53.416  1.00 34.09 ? 682 HOH A O   1 
HETATM 8390 O O   . HOH L 6 .   ? 10.661  17.032  61.622  1.00 12.31 ? 683 HOH A O   1 
HETATM 8391 O O   . HOH L 6 .   ? 15.731  5.440   46.734  1.00 49.50 ? 684 HOH A O   1 
HETATM 8392 O O   . HOH L 6 .   ? 43.272  25.339  84.518  1.00 29.19 ? 685 HOH A O   1 
HETATM 8393 O O   . HOH L 6 .   ? 27.599  13.517  76.537  1.00 13.52 ? 686 HOH A O   1 
HETATM 8394 O O   . HOH L 6 .   ? 25.053  17.450  38.662  1.00 27.26 ? 687 HOH A O   1 
HETATM 8395 O O   . HOH L 6 .   ? 43.204  17.901  60.736  1.00 20.22 ? 688 HOH A O   1 
HETATM 8396 O O   . HOH L 6 .   ? 17.704  22.918  67.543  1.00 14.12 ? 689 HOH A O   1 
HETATM 8397 O O   . HOH L 6 .   ? 21.884  12.242  93.387  1.00 48.04 ? 690 HOH A O   1 
HETATM 8398 O O   . HOH L 6 .   ? 5.331   22.622  73.278  1.00 16.61 ? 691 HOH A O   1 
HETATM 8399 O O   . HOH L 6 .   ? 12.498  36.834  52.521  1.00 20.60 ? 692 HOH A O   1 
HETATM 8400 O O   . HOH L 6 .   ? 41.049  25.312  68.189  1.00 19.88 ? 693 HOH A O   1 
HETATM 8401 O O   . HOH L 6 .   ? 20.966  17.923  69.752  1.00 9.70  ? 694 HOH A O   1 
HETATM 8402 O O   . HOH L 6 .   ? 12.135  12.887  47.616  1.00 42.25 ? 695 HOH A O   1 
HETATM 8403 O O   . HOH L 6 .   ? 40.846  3.416   80.994  1.00 58.16 ? 696 HOH A O   1 
HETATM 8404 O O   . HOH L 6 .   ? 9.522   27.629  44.341  1.00 39.78 ? 697 HOH A O   1 
HETATM 8405 O O   . HOH L 6 .   ? 46.041  16.221  84.868  1.00 39.19 ? 698 HOH A O   1 
HETATM 8406 O O   . HOH L 6 .   ? -3.774  13.902  95.630  1.00 41.47 ? 699 HOH A O   1 
HETATM 8407 O O   . HOH L 6 .   ? 9.417   2.482   71.125  1.00 19.19 ? 700 HOH A O   1 
HETATM 8408 O O   . HOH L 6 .   ? 27.968  23.699  69.479  1.00 20.12 ? 701 HOH A O   1 
HETATM 8409 O O   . HOH L 6 .   ? -0.264  15.288  102.722 1.00 36.89 ? 702 HOH A O   1 
HETATM 8410 O O   . HOH L 6 .   ? 35.365  13.694  90.946  1.00 20.90 ? 703 HOH A O   1 
HETATM 8411 O O   . HOH L 6 .   ? 33.453  14.800  67.758  1.00 17.22 ? 704 HOH A O   1 
HETATM 8412 O O   . HOH L 6 .   ? 15.596  4.319   55.267  1.00 23.89 ? 705 HOH A O   1 
HETATM 8413 O O   . HOH L 6 .   ? 8.448   31.041  61.867  1.00 14.99 ? 706 HOH A O   1 
HETATM 8414 O O   . HOH L 6 .   ? 31.250  -0.354  55.962  1.00 39.28 ? 707 HOH A O   1 
HETATM 8415 O O   . HOH L 6 .   ? 16.203  13.721  81.843  1.00 14.25 ? 708 HOH A O   1 
HETATM 8416 O O   . HOH L 6 .   ? 5.966   33.102  77.246  1.00 26.64 ? 709 HOH A O   1 
HETATM 8417 O O   . HOH L 6 .   ? 12.517  32.238  79.164  1.00 24.73 ? 710 HOH A O   1 
HETATM 8418 O O   . HOH L 6 .   ? 38.666  28.865  51.536  1.00 37.14 ? 711 HOH A O   1 
HETATM 8419 O O   . HOH L 6 .   ? 7.754   14.237  70.836  1.00 10.41 ? 712 HOH A O   1 
HETATM 8420 O O   . HOH L 6 .   ? 13.286  11.908  95.709  1.00 46.13 ? 713 HOH A O   1 
HETATM 8421 O O   . HOH L 6 .   ? 48.739  6.442   77.799  1.00 37.43 ? 714 HOH A O   1 
HETATM 8422 O O   . HOH L 6 .   ? -4.018  9.280   80.139  1.00 44.38 ? 715 HOH A O   1 
HETATM 8423 O O   . HOH L 6 .   ? 2.259   32.283  59.029  1.00 23.13 ? 716 HOH A O   1 
HETATM 8424 O O   . HOH L 6 .   ? 8.914   39.826  77.229  1.00 53.47 ? 717 HOH A O   1 
HETATM 8425 O O   . HOH L 6 .   ? 42.817  14.486  65.726  1.00 16.98 ? 718 HOH A O   1 
HETATM 8426 O O   . HOH L 6 .   ? 19.571  25.397  82.837  1.00 45.20 ? 719 HOH A O   1 
HETATM 8427 O O   . HOH L 6 .   ? 3.523   27.612  50.613  1.00 39.06 ? 720 HOH A O   1 
HETATM 8428 O O   . HOH L 6 .   ? -0.249  9.364   74.311  1.00 46.74 ? 721 HOH A O   1 
HETATM 8429 O O   . HOH L 6 .   ? 37.076  7.301   92.859  1.00 39.03 ? 722 HOH A O   1 
HETATM 8430 O O   . HOH L 6 .   ? 11.146  34.145  48.593  1.00 37.26 ? 723 HOH A O   1 
HETATM 8431 O O   . HOH L 6 .   ? 16.020  -3.390  69.337  1.00 35.05 ? 724 HOH A O   1 
HETATM 8432 O O   . HOH L 6 .   ? 24.280  6.390   85.939  1.00 19.08 ? 725 HOH A O   1 
HETATM 8433 O O   . HOH L 6 .   ? 25.408  21.750  51.704  1.00 19.35 ? 726 HOH A O   1 
HETATM 8434 O O   . HOH L 6 .   ? 19.026  1.951   79.109  1.00 41.32 ? 727 HOH A O   1 
HETATM 8435 O O   . HOH L 6 .   ? 9.225   -1.546  54.655  1.00 22.37 ? 728 HOH A O   1 
HETATM 8436 O O   . HOH L 6 .   ? 23.155  29.634  51.680  1.00 33.96 ? 729 HOH A O   1 
HETATM 8437 O O   . HOH L 6 .   ? 28.442  21.239  91.321  1.00 19.75 ? 730 HOH A O   1 
HETATM 8438 O O   . HOH L 6 .   ? 38.642  21.811  90.163  1.00 36.21 ? 731 HOH A O   1 
HETATM 8439 O O   . HOH L 6 .   ? 18.952  18.189  90.610  1.00 28.02 ? 732 HOH A O   1 
HETATM 8440 O O   . HOH L 6 .   ? 4.955   32.840  80.449  1.00 34.33 ? 733 HOH A O   1 
HETATM 8441 O O   . HOH L 6 .   ? 0.104   9.492   85.922  1.00 29.89 ? 734 HOH A O   1 
HETATM 8442 O O   . HOH L 6 .   ? 9.828   36.171  53.224  1.00 24.46 ? 735 HOH A O   1 
HETATM 8443 O O   . HOH L 6 .   ? 10.867  4.348   73.110  1.00 14.46 ? 736 HOH A O   1 
HETATM 8444 O O   . HOH L 6 .   ? 1.842   13.248  96.638  1.00 35.77 ? 737 HOH A O   1 
HETATM 8445 O O   . HOH L 6 .   ? -1.316  23.694  69.962  1.00 28.66 ? 738 HOH A O   1 
HETATM 8446 O O   . HOH L 6 .   ? 26.655  17.587  67.656  1.00 9.59  ? 739 HOH A O   1 
HETATM 8447 O O   . HOH L 6 .   ? 2.216   7.674   55.923  1.00 43.24 ? 740 HOH A O   1 
HETATM 8448 O O   . HOH L 6 .   ? 41.065  13.399  88.471  1.00 23.17 ? 741 HOH A O   1 
HETATM 8449 O O   . HOH L 6 .   ? 14.027  10.785  47.650  1.00 28.58 ? 742 HOH A O   1 
HETATM 8450 O O   . HOH L 6 .   ? 42.963  19.088  49.409  1.00 34.19 ? 743 HOH A O   1 
HETATM 8451 O O   . HOH L 6 .   ? 23.843  3.012   58.125  1.00 41.89 ? 744 HOH A O   1 
HETATM 8452 O O   . HOH L 6 .   ? 25.070  31.957  59.931  1.00 25.50 ? 745 HOH A O   1 
HETATM 8453 O O   . HOH L 6 .   ? 49.200  20.793  65.501  1.00 33.76 ? 746 HOH A O   1 
HETATM 8454 O O   . HOH L 6 .   ? -3.483  30.414  81.290  1.00 24.76 ? 747 HOH A O   1 
HETATM 8455 O O   . HOH L 6 .   ? 22.008  26.054  63.409  1.00 30.50 ? 748 HOH A O   1 
HETATM 8456 O O   . HOH L 6 .   ? 42.112  5.021   67.849  1.00 31.79 ? 749 HOH A O   1 
HETATM 8457 O O   . HOH L 6 .   ? 2.917   29.341  71.480  1.00 24.31 ? 750 HOH A O   1 
HETATM 8458 O O   . HOH L 6 .   ? 20.711  31.510  48.648  1.00 21.27 ? 751 HOH A O   1 
HETATM 8459 O O   . HOH L 6 .   ? 17.426  0.255   80.429  1.00 47.56 ? 752 HOH A O   1 
HETATM 8460 O O   . HOH L 6 .   ? 4.534   15.113  64.931  1.00 12.49 ? 753 HOH A O   1 
HETATM 8461 O O   . HOH L 6 .   ? 47.994  8.427   59.243  1.00 50.75 ? 754 HOH A O   1 
HETATM 8462 O O   . HOH L 6 .   ? -6.196  31.916  81.582  1.00 50.48 ? 755 HOH A O   1 
HETATM 8463 O O   . HOH L 6 .   ? 34.723  2.358   55.675  1.00 31.92 ? 756 HOH A O   1 
HETATM 8464 O O   . HOH L 6 .   ? 7.060   14.499  99.792  1.00 48.75 ? 757 HOH A O   1 
HETATM 8465 O O   . HOH L 6 .   ? 32.137  15.474  39.624  1.00 33.69 ? 758 HOH A O   1 
HETATM 8466 O O   . HOH L 6 .   ? 3.251   30.764  51.630  1.00 33.20 ? 759 HOH A O   1 
HETATM 8467 O O   . HOH L 6 .   ? 17.213  25.100  73.680  1.00 32.86 ? 760 HOH A O   1 
HETATM 8468 O O   . HOH L 6 .   ? -0.699  25.654  57.760  1.00 51.33 ? 761 HOH A O   1 
HETATM 8469 O O   . HOH L 6 .   ? 22.385  -7.088  59.267  1.00 32.94 ? 762 HOH A O   1 
HETATM 8470 O O   . HOH L 6 .   ? 28.906  27.386  76.592  1.00 34.27 ? 763 HOH A O   1 
HETATM 8471 O O   . HOH L 6 .   ? -9.007  17.989  73.429  1.00 24.79 ? 764 HOH A O   1 
HETATM 8472 O O   . HOH L 6 .   ? 6.762   34.783  64.988  1.00 51.82 ? 765 HOH A O   1 
HETATM 8473 O O   . HOH L 6 .   ? 28.863  20.290  73.600  1.00 15.09 ? 766 HOH A O   1 
HETATM 8474 O O   . HOH L 6 .   ? 11.482  0.323   71.406  1.00 32.75 ? 767 HOH A O   1 
HETATM 8475 O O   . HOH L 6 .   ? 5.952   27.819  64.288  1.00 15.46 ? 768 HOH A O   1 
HETATM 8476 O O   . HOH L 6 .   ? 14.362  33.418  45.087  1.00 36.01 ? 769 HOH A O   1 
HETATM 8477 O O   . HOH L 6 .   ? -5.451  31.780  92.350  1.00 41.90 ? 770 HOH A O   1 
HETATM 8478 O O   . HOH L 6 .   ? 35.988  13.426  42.510  1.00 28.73 ? 771 HOH A O   1 
HETATM 8479 O O   . HOH L 6 .   ? 7.475   10.579  54.187  1.00 30.84 ? 772 HOH A O   1 
HETATM 8480 O O   . HOH L 6 .   ? 47.332  13.428  57.758  1.00 37.34 ? 773 HOH A O   1 
HETATM 8481 O O   . HOH L 6 .   ? 36.184  29.393  49.046  1.00 39.10 ? 774 HOH A O   1 
HETATM 8482 O O   . HOH L 6 .   ? 2.329   8.483   84.297  1.00 39.76 ? 775 HOH A O   1 
HETATM 8483 O O   . HOH L 6 .   ? 34.676  26.835  69.713  1.00 25.56 ? 776 HOH A O   1 
HETATM 8484 O O   . HOH L 6 .   ? 2.661   3.765   73.868  1.00 31.15 ? 777 HOH A O   1 
HETATM 8485 O O   . HOH L 6 .   ? 38.269  24.220  60.759  1.00 53.80 ? 778 HOH A O   1 
HETATM 8486 O O   . HOH L 6 .   ? 15.039  30.123  65.165  1.00 11.59 ? 779 HOH A O   1 
HETATM 8487 O O   . HOH L 6 .   ? -7.884  17.864  76.720  1.00 34.20 ? 780 HOH A O   1 
HETATM 8488 O O   . HOH L 6 .   ? 13.400  29.551  93.671  1.00 53.47 ? 781 HOH A O   1 
HETATM 8489 O O   . HOH L 6 .   ? 29.978  21.308  83.591  1.00 19.56 ? 782 HOH A O   1 
HETATM 8490 O O   . HOH L 6 .   ? -6.419  30.042  94.671  1.00 42.35 ? 783 HOH A O   1 
HETATM 8491 O O   . HOH L 6 .   ? -10.279 15.876  75.136  1.00 42.38 ? 784 HOH A O   1 
HETATM 8492 O O   . HOH L 6 .   ? 27.165  -0.577  73.019  1.00 27.07 ? 785 HOH A O   1 
HETATM 8493 O O   . HOH L 6 .   ? 14.918  29.134  67.715  1.00 14.43 ? 786 HOH A O   1 
HETATM 8494 O O   . HOH L 6 .   ? -3.366  32.393  77.999  1.00 27.25 ? 787 HOH A O   1 
HETATM 8495 O O   . HOH L 6 .   ? -9.524  26.591  67.958  1.00 31.20 ? 788 HOH A O   1 
HETATM 8496 O O   . HOH L 6 .   ? 39.742  30.085  64.705  1.00 41.83 ? 789 HOH A O   1 
HETATM 8497 O O   . HOH L 6 .   ? 4.169   31.992  62.934  1.00 21.52 ? 790 HOH A O   1 
HETATM 8498 O O   . HOH L 6 .   ? 5.690   4.348   67.363  1.00 31.00 ? 791 HOH A O   1 
HETATM 8499 O O   . HOH L 6 .   ? -0.081  23.083  99.136  1.00 45.09 ? 792 HOH A O   1 
HETATM 8500 O O   . HOH L 6 .   ? 42.096  4.729   57.963  1.00 41.83 ? 793 HOH A O   1 
HETATM 8501 O O   . HOH L 6 .   ? 14.780  34.440  49.977  1.00 29.62 ? 794 HOH A O   1 
HETATM 8502 O O   . HOH L 6 .   ? -3.387  25.603  100.090 1.00 47.44 ? 795 HOH A O   1 
HETATM 8503 O O   . HOH L 6 .   ? 36.660  15.896  90.117  1.00 19.73 ? 796 HOH A O   1 
HETATM 8504 O O   . HOH L 6 .   ? 36.795  31.759  68.329  1.00 38.52 ? 797 HOH A O   1 
HETATM 8505 O O   . HOH L 6 .   ? 15.772  30.603  86.829  1.00 38.72 ? 798 HOH A O   1 
HETATM 8506 O O   . HOH L 6 .   ? -0.642  19.971  66.793  1.00 27.88 ? 799 HOH A O   1 
HETATM 8507 O O   . HOH L 6 .   ? 8.830   0.921   74.756  1.00 36.58 ? 800 HOH A O   1 
HETATM 8508 O O   . HOH L 6 .   ? 5.502   32.743  92.526  1.00 49.54 ? 801 HOH A O   1 
HETATM 8509 O O   . HOH L 6 .   ? 26.560  31.872  57.769  1.00 34.23 ? 802 HOH A O   1 
HETATM 8510 O O   . HOH L 6 .   ? 9.881   34.180  68.817  1.00 43.89 ? 803 HOH A O   1 
HETATM 8511 O O   . HOH L 6 .   ? 47.246  17.354  83.199  1.00 35.21 ? 804 HOH A O   1 
HETATM 8512 O O   . HOH L 6 .   ? -8.084  20.036  93.444  1.00 44.99 ? 805 HOH A O   1 
HETATM 8513 O O   . HOH L 6 .   ? -7.030  18.065  92.767  1.00 17.48 ? 806 HOH A O   1 
HETATM 8514 O O   . HOH L 6 .   ? 45.278  31.390  68.762  1.00 28.31 ? 807 HOH A O   1 
HETATM 8515 O O   . HOH L 6 .   ? 34.080  23.395  88.900  1.00 36.56 ? 808 HOH A O   1 
HETATM 8516 O O   . HOH L 6 .   ? -8.062  15.317  91.376  1.00 24.42 ? 809 HOH A O   1 
HETATM 8517 O O   . HOH L 6 .   ? 34.854  29.546  69.618  1.00 39.22 ? 810 HOH A O   1 
HETATM 8518 O O   . HOH L 6 .   ? 21.120  31.471  51.481  1.00 26.55 ? 811 HOH A O   1 
HETATM 8519 O O   . HOH L 6 .   ? 10.594  6.138   84.102  1.00 30.28 ? 812 HOH A O   1 
HETATM 8520 O O   . HOH L 6 .   ? 12.155  33.380  74.150  1.00 41.16 ? 813 HOH A O   1 
HETATM 8521 O O   . HOH L 6 .   ? 36.007  -1.410  58.242  1.00 45.25 ? 814 HOH A O   1 
HETATM 8522 O O   . HOH L 6 .   ? 24.025  26.554  75.135  1.00 36.62 ? 815 HOH A O   1 
HETATM 8523 O O   . HOH L 6 .   ? 6.332   11.810  93.023  1.00 38.70 ? 816 HOH A O   1 
HETATM 8524 O O   . HOH L 6 .   ? 20.572  7.681   45.128  1.00 38.88 ? 817 HOH A O   1 
HETATM 8525 O O   . HOH L 6 .   ? 27.236  11.772  78.684  1.00 13.22 ? 818 HOH A O   1 
HETATM 8526 O O   . HOH L 6 .   ? 45.138  26.487  82.103  1.00 32.21 ? 819 HOH A O   1 
HETATM 8527 O O   . HOH L 6 .   ? 43.861  21.713  54.981  1.00 47.86 ? 820 HOH A O   1 
HETATM 8528 O O   . HOH L 6 .   ? 21.461  8.146   41.208  1.00 38.53 ? 821 HOH A O   1 
HETATM 8529 O O   . HOH L 6 .   ? 2.192   24.713  51.205  1.00 47.78 ? 822 HOH A O   1 
HETATM 8530 O O   . HOH L 6 .   ? 34.543  -2.198  60.558  1.00 45.31 ? 823 HOH A O   1 
HETATM 8531 O O   . HOH L 6 .   ? 7.518   10.512  88.701  1.00 48.71 ? 824 HOH A O   1 
HETATM 8532 O O   . HOH L 6 .   ? 13.586  0.044   72.395  1.00 36.33 ? 825 HOH A O   1 
HETATM 8533 O O   . HOH L 6 .   ? 15.672  18.873  88.426  1.00 40.86 ? 826 HOH A O   1 
HETATM 8534 O O   . HOH L 6 .   ? 10.267  10.074  88.385  1.00 41.75 ? 827 HOH A O   1 
HETATM 8535 O O   . HOH L 6 .   ? 42.233  11.579  89.786  1.00 37.99 ? 828 HOH A O   1 
HETATM 8536 O O   . HOH L 6 .   ? 9.600   -0.810  66.599  1.00 39.58 ? 829 HOH A O   1 
HETATM 8537 O O   . HOH L 6 .   ? 6.064   32.370  95.038  1.00 50.10 ? 830 HOH A O   1 
HETATM 8538 O O   . HOH L 6 .   ? 6.938   23.753  100.752 1.00 32.21 ? 831 HOH A O   1 
HETATM 8539 O O   . HOH L 6 .   ? 48.337  20.577  83.019  1.00 16.47 ? 832 HOH A O   1 
HETATM 8540 O O   . HOH L 6 .   ? 18.851  21.229  90.919  1.00 39.86 ? 833 HOH A O   1 
HETATM 8541 O O   . HOH L 6 .   ? 2.463   25.997  53.337  1.00 38.45 ? 834 HOH A O   1 
HETATM 8542 O O   . HOH L 6 .   ? 34.946  22.265  41.192  1.00 39.42 ? 835 HOH A O   1 
HETATM 8543 O O   . HOH L 6 .   ? 48.457  13.267  73.946  1.00 39.92 ? 836 HOH A O   1 
HETATM 8544 O O   . HOH L 6 .   ? 42.948  5.825   65.334  1.00 48.22 ? 837 HOH A O   1 
HETATM 8545 O O   . HOH L 6 .   ? 52.383  10.924  84.203  1.00 39.06 ? 838 HOH A O   1 
HETATM 8546 O O   . HOH L 6 .   ? 16.012  31.843  76.964  1.00 49.91 ? 839 HOH A O   1 
HETATM 8547 O O   . HOH L 6 .   ? 37.413  11.950  91.492  1.00 31.67 ? 840 HOH A O   1 
HETATM 8548 O O   . HOH L 6 .   ? 47.525  10.890  71.632  1.00 47.19 ? 841 HOH A O   1 
HETATM 8549 O O   . HOH L 6 .   ? -8.376  13.399  84.060  1.00 48.51 ? 842 HOH A O   1 
HETATM 8550 O O   . HOH L 6 .   ? 17.224  6.468   95.075  1.00 47.45 ? 843 HOH A O   1 
HETATM 8551 O O   . HOH L 6 .   ? -5.109  8.018   82.394  1.00 40.24 ? 844 HOH A O   1 
HETATM 8552 O O   . HOH L 6 .   ? 27.403  3.466   81.751  1.00 39.18 ? 845 HOH A O   1 
HETATM 8553 O O   . HOH L 6 .   ? 23.303  24.472  73.996  1.00 35.79 ? 846 HOH A O   1 
HETATM 8554 O O   . HOH L 6 .   ? 5.049   29.121  51.191  1.00 35.82 ? 847 HOH A O   1 
HETATM 8555 O O   . HOH L 6 .   ? 44.851  15.216  63.672  1.00 24.45 ? 848 HOH A O   1 
HETATM 8556 O O   . HOH L 6 .   ? 1.111   35.021  78.583  1.00 54.30 ? 849 HOH A O   1 
HETATM 8557 O O   . HOH L 6 .   ? 6.473   30.348  63.513  1.00 19.68 ? 850 HOH A O   1 
HETATM 8558 O O   . HOH L 6 .   ? 20.050  24.223  73.560  1.00 36.85 ? 851 HOH A O   1 
HETATM 8559 O O   . HOH L 6 .   ? -0.995  23.577  46.725  1.00 49.75 ? 852 HOH A O   1 
HETATM 8560 O O   . HOH L 6 .   ? 27.762  -2.419  57.399  1.00 44.19 ? 853 HOH A O   1 
HETATM 8561 O O   . HOH L 6 .   ? 3.601   28.697  52.861  1.00 38.68 ? 854 HOH A O   1 
HETATM 8562 O O   . HOH L 6 .   ? 4.387   12.333  97.847  1.00 44.82 ? 855 HOH A O   1 
HETATM 8563 O O   . HOH L 6 .   ? 16.095  32.437  84.925  1.00 37.29 ? 856 HOH A O   1 
HETATM 8564 O O   . HOH L 6 .   ? 1.125   4.791   67.370  1.00 46.04 ? 857 HOH A O   1 
HETATM 8565 O O   . HOH L 6 .   ? 43.555  3.146   68.816  1.00 58.91 ? 858 HOH A O   1 
HETATM 8566 O O   . HOH L 6 .   ? 0.364   24.148  56.490  1.00 49.78 ? 859 HOH A O   1 
HETATM 8567 O O   . HOH L 6 .   ? 39.732  31.075  74.939  1.00 44.35 ? 860 HOH A O   1 
HETATM 8568 O O   . HOH L 6 .   ? 49.554  10.503  74.139  1.00 48.77 ? 861 HOH A O   1 
HETATM 8569 O O   . HOH L 6 .   ? 28.122  22.446  72.039  1.00 22.14 ? 862 HOH A O   1 
HETATM 8570 O O   . HOH L 6 .   ? 14.059  31.182  91.313  1.00 43.13 ? 863 HOH A O   1 
HETATM 8571 O O   . HOH L 6 .   ? 44.011  8.876   46.696  1.00 28.37 ? 864 HOH A O   1 
HETATM 8572 O O   . HOH L 6 .   ? 25.892  28.415  76.501  1.00 50.53 ? 865 HOH A O   1 
HETATM 8573 O O   . HOH L 6 .   ? 16.895  33.044  75.269  1.00 51.36 ? 866 HOH A O   1 
HETATM 8574 O O   . HOH L 6 .   ? 38.903  2.003   80.822  1.00 48.63 ? 867 HOH A O   1 
HETATM 8575 O O   . HOH L 6 .   ? 19.764  18.074  101.072 1.00 50.73 ? 868 HOH A O   1 
HETATM 8576 O O   . HOH L 6 .   ? 28.852  9.502   96.000  1.00 56.51 ? 869 HOH A O   1 
HETATM 8577 O O   . HOH L 6 .   ? -0.709  22.577  67.256  1.00 39.03 ? 870 HOH A O   1 
HETATM 8578 O O   . HOH L 6 .   ? -1.926  17.441  104.029 1.00 38.24 ? 871 HOH A O   1 
HETATM 8579 O O   . HOH L 6 .   ? 7.081   9.682   91.563  1.00 50.82 ? 872 HOH A O   1 
HETATM 8580 O O   . HOH L 6 .   ? 51.221  21.616  66.893  1.00 40.17 ? 873 HOH A O   1 
HETATM 8581 O O   . HOH L 6 .   ? 3.740   1.314   73.115  1.00 50.89 ? 874 HOH A O   1 
HETATM 8582 O O   . HOH L 6 .   ? 14.285  1.560   52.223  1.00 38.78 ? 875 HOH A O   1 
HETATM 8583 O O   . HOH L 6 .   ? 3.847   11.100  93.670  1.00 44.74 ? 876 HOH A O   1 
HETATM 8584 O O   . HOH L 6 .   ? 13.832  32.504  76.876  1.00 42.46 ? 877 HOH A O   1 
HETATM 8585 O O   . HOH L 6 .   ? 1.545   28.190  53.429  1.00 38.76 ? 878 HOH A O   1 
HETATM 8586 O O   . HOH L 6 .   ? 26.427  5.279   97.239  1.00 54.36 ? 879 HOH A O   1 
HETATM 8587 O O   . HOH L 6 .   ? 46.893  23.089  83.123  1.00 38.91 ? 880 HOH A O   1 
HETATM 8588 O O   . HOH L 6 .   ? 31.328  23.898  41.984  1.00 42.64 ? 881 HOH A O   1 
HETATM 8589 O O   . HOH L 6 .   ? 4.402   2.163   68.330  1.00 46.49 ? 882 HOH A O   1 
HETATM 8590 O O   . HOH L 6 .   ? -6.926  33.615  93.036  1.00 50.14 ? 883 HOH A O   1 
HETATM 8591 O O   . HOH L 6 .   ? -4.588  29.820  78.725  1.00 45.46 ? 884 HOH A O   1 
HETATM 8592 O O   . HOH L 6 .   ? 3.800   24.452  100.061 1.00 50.84 ? 885 HOH A O   1 
HETATM 8593 O O   . HOH L 6 .   ? 26.728  41.000  81.557  1.00 52.59 ? 886 HOH A O   1 
HETATM 8594 O O   . HOH L 6 .   ? 7.667   26.086  100.228 1.00 35.50 ? 887 HOH A O   1 
HETATM 8595 O O   . HOH L 6 .   ? 18.231  4.227   48.840  1.00 44.51 ? 888 HOH A O   1 
HETATM 8596 O O   . HOH L 6 .   ? 23.155  31.867  47.668  1.00 44.28 ? 889 HOH A O   1 
HETATM 8597 O O   . HOH L 6 .   ? 21.550  23.633  75.055  1.00 35.56 ? 890 HOH A O   1 
HETATM 8598 O O   . HOH L 6 .   ? 15.545  31.710  89.731  1.00 49.75 ? 891 HOH A O   1 
HETATM 8599 O O   . HOH L 6 .   ? 11.982  1.574   74.322  1.00 29.69 ? 892 HOH A O   1 
HETATM 8600 O O   . HOH L 6 .   ? 18.865  16.594  93.168  1.00 57.97 ? 893 HOH A O   1 
HETATM 8601 O O   . HOH L 6 .   ? 20.646  25.690  75.623  1.00 40.43 ? 894 HOH A O   1 
HETATM 8602 O O   . HOH M 6 .   ? 15.270  1.441   35.661  1.00 38.56 ? 601 HOH B O   1 
HETATM 8603 O O   . HOH M 6 .   ? 0.291   -19.872 34.997  1.00 32.78 ? 602 HOH B O   1 
HETATM 8604 O O   . HOH M 6 .   ? 5.565   -20.052 35.066  1.00 38.28 ? 603 HOH B O   1 
HETATM 8605 O O   . HOH M 6 .   ? -5.149  -0.840  61.808  1.00 46.25 ? 604 HOH B O   1 
HETATM 8606 O O   . HOH M 6 .   ? 5.259   -8.864  43.841  1.00 40.78 ? 605 HOH B O   1 
HETATM 8607 O O   . HOH M 6 .   ? 13.441  -9.328  33.435  1.00 38.99 ? 606 HOH B O   1 
HETATM 8608 O O   . HOH M 6 .   ? 3.404   3.983   56.233  1.00 30.15 ? 607 HOH B O   1 
HETATM 8609 O O   . HOH M 6 .   ? -2.331  -0.222  59.419  1.00 45.18 ? 608 HOH B O   1 
HETATM 8610 O O   . HOH M 6 .   ? -3.892  6.676   13.070  1.00 37.71 ? 609 HOH B O   1 
HETATM 8611 O O   . HOH M 6 .   ? 11.174  15.750  48.169  1.00 23.15 ? 610 HOH B O   1 
HETATM 8612 O O   . HOH M 6 .   ? 3.255   -20.466 43.204  1.00 28.74 ? 611 HOH B O   1 
HETATM 8613 O O   . HOH M 6 .   ? -27.057 10.538  15.657  1.00 32.88 ? 612 HOH B O   1 
HETATM 8614 O O   . HOH M 6 .   ? 6.933   -10.278 49.594  1.00 25.09 ? 613 HOH B O   1 
HETATM 8615 O O   . HOH M 6 .   ? -7.490  -3.869  0.223   1.00 41.61 ? 614 HOH B O   1 
HETATM 8616 O O   . HOH M 6 .   ? -7.958  -26.010 35.039  1.00 50.08 ? 615 HOH B O   1 
HETATM 8617 O O   . HOH M 6 .   ? 18.451  -8.862  14.092  1.00 40.61 ? 616 HOH B O   1 
HETATM 8618 O O   . HOH M 6 .   ? 2.245   -12.561 9.149   1.00 23.16 ? 617 HOH B O   1 
HETATM 8619 O O   . HOH M 6 .   ? -31.606 -4.792  5.577   1.00 46.75 ? 618 HOH B O   1 
HETATM 8620 O O   . HOH M 6 .   ? 12.034  -2.512  45.859  1.00 39.21 ? 619 HOH B O   1 
HETATM 8621 O O   . HOH M 6 .   ? -16.940 -2.039  3.146   1.00 51.47 ? 620 HOH B O   1 
HETATM 8622 O O   . HOH M 6 .   ? -24.133 1.722   50.356  1.00 27.44 ? 621 HOH B O   1 
HETATM 8623 O O   . HOH M 6 .   ? -21.290 9.351   17.292  1.00 34.58 ? 622 HOH B O   1 
HETATM 8624 O O   . HOH M 6 .   ? -26.724 3.988   26.827  1.00 22.68 ? 623 HOH B O   1 
HETATM 8625 O O   . HOH M 6 .   ? 7.856   -2.386  4.083   1.00 26.07 ? 624 HOH B O   1 
HETATM 8626 O O   . HOH M 6 .   ? -2.134  -8.532  48.887  1.00 32.08 ? 625 HOH B O   1 
HETATM 8627 O O   . HOH M 6 .   ? 11.766  16.122  42.075  1.00 48.48 ? 626 HOH B O   1 
HETATM 8628 O O   . HOH M 6 .   ? 9.833   14.674  21.763  1.00 35.40 ? 627 HOH B O   1 
HETATM 8629 O O   . HOH M 6 .   ? 6.231   -0.582  0.262   1.00 40.86 ? 628 HOH B O   1 
HETATM 8630 O O   . HOH M 6 .   ? 8.367   -10.222 12.694  1.00 47.04 ? 629 HOH B O   1 
HETATM 8631 O O   . HOH M 6 .   ? -3.916  13.664  52.005  1.00 46.07 ? 630 HOH B O   1 
HETATM 8632 O O   . HOH M 6 .   ? 2.748   4.206   25.804  1.00 17.13 ? 631 HOH B O   1 
HETATM 8633 O O   . HOH M 6 .   ? -18.673 -4.357  18.803  1.00 34.34 ? 632 HOH B O   1 
HETATM 8634 O O   . HOH M 6 .   ? -22.995 2.869   47.910  1.00 27.62 ? 633 HOH B O   1 
HETATM 8635 O O   . HOH M 6 .   ? -2.418  -14.960 41.010  1.00 31.28 ? 634 HOH B O   1 
HETATM 8636 O O   . HOH M 6 .   ? -25.081 -18.258 25.221  1.00 46.16 ? 635 HOH B O   1 
HETATM 8637 O O   . HOH M 6 .   ? 3.624   -2.753  10.105  1.00 18.82 ? 636 HOH B O   1 
HETATM 8638 O O   . HOH M 6 .   ? 24.713  -0.233  27.672  1.00 36.48 ? 637 HOH B O   1 
HETATM 8639 O O   . HOH M 6 .   ? 15.915  -10.083 15.122  1.00 39.33 ? 638 HOH B O   1 
HETATM 8640 O O   . HOH M 6 .   ? -19.189 8.207   42.243  1.00 29.07 ? 639 HOH B O   1 
HETATM 8641 O O   . HOH M 6 .   ? 18.668  3.970   29.807  1.00 52.06 ? 640 HOH B O   1 
HETATM 8642 O O   . HOH M 6 .   ? -28.267 -8.414  18.246  1.00 23.86 ? 641 HOH B O   1 
HETATM 8643 O O   . HOH M 6 .   ? -26.711 -15.915 43.488  1.00 49.89 ? 642 HOH B O   1 
HETATM 8644 O O   . HOH M 6 .   ? 0.051   4.337   22.086  1.00 23.80 ? 643 HOH B O   1 
HETATM 8645 O O   . HOH M 6 .   ? 13.066  -6.822  33.931  1.00 30.28 ? 644 HOH B O   1 
HETATM 8646 O O   . HOH M 6 .   ? -22.496 -15.419 10.903  1.00 41.50 ? 645 HOH B O   1 
HETATM 8647 O O   . HOH M 6 .   ? -14.932 7.651   32.697  1.00 44.52 ? 646 HOH B O   1 
HETATM 8648 O O   . HOH M 6 .   ? -21.494 -15.061 1.696   1.00 40.63 ? 647 HOH B O   1 
HETATM 8649 O O   . HOH M 6 .   ? 16.242  -12.440 19.100  1.00 40.31 ? 648 HOH B O   1 
HETATM 8650 O O   . HOH M 6 .   ? 20.915  15.065  3.519   1.00 52.09 ? 649 HOH B O   1 
HETATM 8651 O O   . HOH M 6 .   ? 8.821   -15.984 33.419  1.00 40.39 ? 650 HOH B O   1 
HETATM 8652 O O   . HOH M 6 .   ? 15.172  -6.317  42.251  1.00 48.04 ? 651 HOH B O   1 
HETATM 8653 O O   . HOH M 6 .   ? -13.368 9.409   41.442  1.00 31.68 ? 652 HOH B O   1 
HETATM 8654 O O   . HOH M 6 .   ? 15.469  -4.569  37.221  1.00 48.52 ? 653 HOH B O   1 
HETATM 8655 O O   . HOH M 6 .   ? 28.857  5.308   14.108  1.00 39.22 ? 654 HOH B O   1 
HETATM 8656 O O   . HOH M 6 .   ? 6.768   -16.576 26.699  1.00 21.20 ? 655 HOH B O   1 
HETATM 8657 O O   . HOH M 6 .   ? 1.777   -1.902  50.799  1.00 25.84 ? 656 HOH B O   1 
HETATM 8658 O O   . HOH M 6 .   ? -18.795 -5.770  27.809  1.00 17.93 ? 657 HOH B O   1 
HETATM 8659 O O   . HOH M 6 .   ? -14.309 -2.586  56.214  1.00 29.75 ? 658 HOH B O   1 
HETATM 8660 O O   . HOH M 6 .   ? 12.428  -3.147  24.843  1.00 19.91 ? 659 HOH B O   1 
HETATM 8661 O O   . HOH M 6 .   ? 13.908  -3.688  -0.725  1.00 36.70 ? 660 HOH B O   1 
HETATM 8662 O O   . HOH M 6 .   ? 28.728  -0.988  14.415  1.00 21.96 ? 661 HOH B O   1 
HETATM 8663 O O   . HOH M 6 .   ? 0.546   11.811  17.879  1.00 41.22 ? 662 HOH B O   1 
HETATM 8664 O O   . HOH M 6 .   ? 23.881  -3.936  5.295   1.00 48.32 ? 663 HOH B O   1 
HETATM 8665 O O   . HOH M 6 .   ? -2.545  3.805   29.136  1.00 17.82 ? 664 HOH B O   1 
HETATM 8666 O O   . HOH M 6 .   ? -23.427 9.711   31.291  1.00 34.36 ? 665 HOH B O   1 
HETATM 8667 O O   . HOH M 6 .   ? 11.989  -6.303  36.355  1.00 33.91 ? 666 HOH B O   1 
HETATM 8668 O O   . HOH M 6 .   ? 4.994   11.899  36.466  1.00 26.25 ? 667 HOH B O   1 
HETATM 8669 O O   . HOH M 6 .   ? 13.336  7.709   24.583  1.00 31.74 ? 668 HOH B O   1 
HETATM 8670 O O   . HOH M 6 .   ? 10.356  4.015   25.484  1.00 21.64 ? 669 HOH B O   1 
HETATM 8671 O O   . HOH M 6 .   ? 1.833   13.232  20.729  1.00 37.74 ? 670 HOH B O   1 
HETATM 8672 O O   . HOH M 6 .   ? -4.335  -14.029 44.898  1.00 30.83 ? 671 HOH B O   1 
HETATM 8673 O O   . HOH M 6 .   ? 27.310  -1.394  25.356  1.00 43.38 ? 672 HOH B O   1 
HETATM 8674 O O   . HOH M 6 .   ? -8.536  2.412   3.598   1.00 19.35 ? 673 HOH B O   1 
HETATM 8675 O O   . HOH M 6 .   ? -11.995 8.647   10.531  1.00 33.93 ? 674 HOH B O   1 
HETATM 8676 O O   . HOH M 6 .   ? 0.843   -3.893  49.036  1.00 19.50 ? 675 HOH B O   1 
HETATM 8677 O O   . HOH M 6 .   ? 7.092   -0.421  55.751  1.00 28.68 ? 676 HOH B O   1 
HETATM 8678 O O   . HOH M 6 .   ? 12.582  -3.931  27.718  1.00 16.46 ? 677 HOH B O   1 
HETATM 8679 O O   . HOH M 6 .   ? -3.855  16.371  41.132  1.00 33.56 ? 678 HOH B O   1 
HETATM 8680 O O   . HOH M 6 .   ? -24.291 -6.482  50.031  1.00 45.85 ? 679 HOH B O   1 
HETATM 8681 O O   . HOH M 6 .   ? 16.126  5.452   29.972  1.00 43.66 ? 680 HOH B O   1 
HETATM 8682 O O   . HOH M 6 .   ? -29.007 -6.863  16.298  1.00 26.74 ? 681 HOH B O   1 
HETATM 8683 O O   . HOH M 6 .   ? -27.289 -4.853  26.114  1.00 17.46 ? 682 HOH B O   1 
HETATM 8684 O O   . HOH M 6 .   ? -1.855  -13.647 46.164  1.00 29.93 ? 683 HOH B O   1 
HETATM 8685 O O   . HOH M 6 .   ? -15.157 -1.410  51.271  1.00 21.75 ? 684 HOH B O   1 
HETATM 8686 O O   . HOH M 6 .   ? 9.017   -12.978 40.154  1.00 31.13 ? 685 HOH B O   1 
HETATM 8687 O O   . HOH M 6 .   ? -4.421  -15.790 6.582   1.00 48.72 ? 686 HOH B O   1 
HETATM 8688 O O   . HOH M 6 .   ? 24.143  6.604   10.662  1.00 28.71 ? 687 HOH B O   1 
HETATM 8689 O O   . HOH M 6 .   ? -25.666 -14.238 23.849  1.00 38.50 ? 688 HOH B O   1 
HETATM 8690 O O   . HOH M 6 .   ? -16.690 -0.228  43.457  1.00 18.08 ? 689 HOH B O   1 
HETATM 8691 O O   . HOH M 6 .   ? 7.875   -2.103  59.317  1.00 15.89 ? 690 HOH B O   1 
HETATM 8692 O O   . HOH M 6 .   ? -10.374 -5.586  18.105  1.00 18.44 ? 691 HOH B O   1 
HETATM 8693 O O   . HOH M 6 .   ? -11.210 12.536  35.418  1.00 45.05 ? 692 HOH B O   1 
HETATM 8694 O O   . HOH M 6 .   ? -9.301  9.815   11.089  1.00 33.44 ? 693 HOH B O   1 
HETATM 8695 O O   . HOH M 6 .   ? -35.065 -4.805  8.536   1.00 37.46 ? 694 HOH B O   1 
HETATM 8696 O O   . HOH M 6 .   ? -15.146 8.861   50.558  1.00 34.97 ? 695 HOH B O   1 
HETATM 8697 O O   . HOH M 6 .   ? -3.202  -4.392  42.666  1.00 14.24 ? 696 HOH B O   1 
HETATM 8698 O O   . HOH M 6 .   ? 21.524  -3.137  -2.401  1.00 44.58 ? 697 HOH B O   1 
HETATM 8699 O O   . HOH M 6 .   ? -20.326 -16.103 13.795  1.00 38.49 ? 698 HOH B O   1 
HETATM 8700 O O   . HOH M 6 .   ? 3.408   -2.125  35.922  1.00 13.67 ? 699 HOH B O   1 
HETATM 8701 O O   . HOH M 6 .   ? -5.331  -12.242 9.430   1.00 23.82 ? 700 HOH B O   1 
HETATM 8702 O O   . HOH M 6 .   ? 11.486  -14.401 35.102  1.00 46.31 ? 701 HOH B O   1 
HETATM 8703 O O   . HOH M 6 .   ? -14.275 8.442   8.456   1.00 35.82 ? 702 HOH B O   1 
HETATM 8704 O O   . HOH M 6 .   ? 7.907   -4.626  27.329  1.00 14.58 ? 703 HOH B O   1 
HETATM 8705 O O   . HOH M 6 .   ? 16.990  3.672   -0.701  1.00 32.69 ? 704 HOH B O   1 
HETATM 8706 O O   . HOH M 6 .   ? -17.657 7.722   63.266  1.00 30.28 ? 705 HOH B O   1 
HETATM 8707 O O   . HOH M 6 .   ? 7.274   8.659   47.989  1.00 44.29 ? 706 HOH B O   1 
HETATM 8708 O O   . HOH M 6 .   ? -20.099 -9.480  51.170  1.00 38.33 ? 707 HOH B O   1 
HETATM 8709 O O   . HOH M 6 .   ? -17.773 -4.328  25.730  1.00 17.20 ? 708 HOH B O   1 
HETATM 8710 O O   . HOH M 6 .   ? 11.450  -12.958 32.677  1.00 42.71 ? 709 HOH B O   1 
HETATM 8711 O O   . HOH M 6 .   ? -27.737 -13.940 13.356  1.00 38.28 ? 710 HOH B O   1 
HETATM 8712 O O   . HOH M 6 .   ? -30.599 -13.495 41.361  1.00 35.82 ? 711 HOH B O   1 
HETATM 8713 O O   . HOH M 6 .   ? -12.772 1.914   43.284  1.00 16.95 ? 712 HOH B O   1 
HETATM 8714 O O   . HOH M 6 .   ? 17.395  -4.718  33.103  1.00 49.23 ? 713 HOH B O   1 
HETATM 8715 O O   . HOH M 6 .   ? 9.947   -3.639  33.711  1.00 16.16 ? 714 HOH B O   1 
HETATM 8716 O O   . HOH M 6 .   ? -11.204 -1.558  27.077  1.00 13.68 ? 715 HOH B O   1 
HETATM 8717 O O   . HOH M 6 .   ? -21.379 -4.145  53.787  1.00 42.59 ? 716 HOH B O   1 
HETATM 8718 O O   . HOH M 6 .   ? 1.766   -4.892  15.046  1.00 18.21 ? 717 HOH B O   1 
HETATM 8719 O O   . HOH M 6 .   ? 21.120  -6.000  0.192   1.00 51.31 ? 718 HOH B O   1 
HETATM 8720 O O   . HOH M 6 .   ? -10.730 9.873   44.181  1.00 37.12 ? 719 HOH B O   1 
HETATM 8721 O O   . HOH M 6 .   ? -25.908 8.994   41.833  1.00 22.90 ? 720 HOH B O   1 
HETATM 8722 O O   . HOH M 6 .   ? 15.249  1.107   32.958  1.00 40.08 ? 721 HOH B O   1 
HETATM 8723 O O   . HOH M 6 .   ? -0.032  -6.647  49.328  1.00 31.19 ? 722 HOH B O   1 
HETATM 8724 O O   . HOH M 6 .   ? -22.860 12.543  11.176  1.00 46.68 ? 723 HOH B O   1 
HETATM 8725 O O   . HOH M 6 .   ? -12.318 13.873  15.377  1.00 44.93 ? 724 HOH B O   1 
HETATM 8726 O O   . HOH M 6 .   ? -28.752 -1.729  31.055  1.00 20.16 ? 725 HOH B O   1 
HETATM 8727 O O   . HOH M 6 .   ? 19.887  12.824  19.208  1.00 31.51 ? 726 HOH B O   1 
HETATM 8728 O O   . HOH M 6 .   ? 18.719  -4.867  3.508   1.00 33.82 ? 727 HOH B O   1 
HETATM 8729 O O   . HOH M 6 .   ? -24.719 -15.797 14.634  1.00 38.59 ? 728 HOH B O   1 
HETATM 8730 O O   . HOH M 6 .   ? -12.463 4.432   25.259  1.00 24.45 ? 729 HOH B O   1 
HETATM 8731 O O   . HOH M 6 .   ? 13.893  -14.691 25.136  1.00 31.60 ? 730 HOH B O   1 
HETATM 8732 O O   . HOH M 6 .   ? -4.063  -15.864 43.237  1.00 48.81 ? 731 HOH B O   1 
HETATM 8733 O O   . HOH M 6 .   ? -28.008 -14.655 17.576  1.00 35.87 ? 732 HOH B O   1 
HETATM 8734 O O   . HOH M 6 .   ? 6.051   4.373   51.785  1.00 27.64 ? 733 HOH B O   1 
HETATM 8735 O O   . HOH M 6 .   ? -5.812  -15.060 40.625  1.00 38.68 ? 734 HOH B O   1 
HETATM 8736 O O   . HOH M 6 .   ? -14.751 4.669   4.997   1.00 33.39 ? 735 HOH B O   1 
HETATM 8737 O O   . HOH M 6 .   ? -25.220 5.951   24.196  1.00 23.06 ? 736 HOH B O   1 
HETATM 8738 O O   . HOH M 6 .   ? -21.252 -5.427  3.816   1.00 27.81 ? 737 HOH B O   1 
HETATM 8739 O O   . HOH M 6 .   ? 5.624   -14.613 24.462  1.00 17.80 ? 738 HOH B O   1 
HETATM 8740 O O   . HOH M 6 .   ? 6.535   -18.614 33.254  1.00 36.76 ? 739 HOH B O   1 
HETATM 8741 O O   . HOH M 6 .   ? -5.397  -1.129  26.172  1.00 14.17 ? 740 HOH B O   1 
HETATM 8742 O O   . HOH M 6 .   ? -6.991  -13.678 16.031  1.00 28.68 ? 741 HOH B O   1 
HETATM 8743 O O   . HOH M 6 .   ? -3.734  16.822  38.150  1.00 47.56 ? 742 HOH B O   1 
HETATM 8744 O O   . HOH M 6 .   ? -29.813 -4.072  26.891  1.00 28.94 ? 743 HOH B O   1 
HETATM 8745 O O   . HOH M 6 .   ? -1.948  7.743   6.237   1.00 43.03 ? 744 HOH B O   1 
HETATM 8746 O O   . HOH M 6 .   ? 5.380   -7.720  0.368   1.00 53.98 ? 745 HOH B O   1 
HETATM 8747 O O   . HOH M 6 .   ? -1.053  -16.964 17.014  1.00 39.50 ? 746 HOH B O   1 
HETATM 8748 O O   . HOH M 6 .   ? -31.938 -7.517  21.649  1.00 49.13 ? 747 HOH B O   1 
HETATM 8749 O O   . HOH M 6 .   ? -21.091 -17.024 37.003  1.00 30.89 ? 748 HOH B O   1 
HETATM 8750 O O   . HOH M 6 .   ? -7.235  -7.679  55.762  1.00 53.34 ? 749 HOH B O   1 
HETATM 8751 O O   . HOH M 6 .   ? 11.562  4.516   -9.274  1.00 31.23 ? 750 HOH B O   1 
HETATM 8752 O O   . HOH M 6 .   ? -24.310 4.863   31.853  1.00 23.70 ? 751 HOH B O   1 
HETATM 8753 O O   . HOH M 6 .   ? -18.915 9.852   24.180  1.00 47.01 ? 752 HOH B O   1 
HETATM 8754 O O   . HOH M 6 .   ? -11.931 8.468   18.129  1.00 32.49 ? 753 HOH B O   1 
HETATM 8755 O O   . HOH M 6 .   ? -30.614 -1.022  42.493  1.00 40.64 ? 754 HOH B O   1 
HETATM 8756 O O   . HOH M 6 .   ? 0.576   -0.182  5.976   1.00 29.55 ? 755 HOH B O   1 
HETATM 8757 O O   . HOH M 6 .   ? -18.660 7.539   23.809  1.00 26.68 ? 756 HOH B O   1 
HETATM 8758 O O   . HOH M 6 .   ? 6.055   14.678  29.666  1.00 43.52 ? 757 HOH B O   1 
HETATM 8759 O O   . HOH M 6 .   ? -18.936 -13.192 42.779  1.00 45.71 ? 758 HOH B O   1 
HETATM 8760 O O   . HOH M 6 .   ? -2.310  10.258  27.858  1.00 48.73 ? 759 HOH B O   1 
HETATM 8761 O O   . HOH M 6 .   ? -28.002 3.850   46.483  1.00 29.49 ? 760 HOH B O   1 
HETATM 8762 O O   . HOH M 6 .   ? -7.615  6.657   32.554  1.00 39.45 ? 761 HOH B O   1 
HETATM 8763 O O   . HOH M 6 .   ? -12.343 1.240   21.039  1.00 18.27 ? 762 HOH B O   1 
HETATM 8764 O O   . HOH M 6 .   ? -2.595  14.907  47.134  1.00 35.57 ? 763 HOH B O   1 
HETATM 8765 O O   . HOH M 6 .   ? -5.605  -14.958 37.546  1.00 21.47 ? 764 HOH B O   1 
HETATM 8766 O O   . HOH M 6 .   ? -8.565  11.883  44.668  1.00 31.62 ? 765 HOH B O   1 
HETATM 8767 O O   . HOH M 6 .   ? -16.476 -11.388 0.008   1.00 49.52 ? 766 HOH B O   1 
HETATM 8768 O O   . HOH M 6 .   ? 3.225   -13.530 46.354  1.00 52.44 ? 767 HOH B O   1 
HETATM 8769 O O   . HOH M 6 .   ? 14.247  5.001   -1.845  1.00 36.27 ? 768 HOH B O   1 
HETATM 8770 O O   . HOH M 6 .   ? -18.488 3.622   2.796   1.00 32.21 ? 769 HOH B O   1 
HETATM 8771 O O   . HOH M 6 .   ? -14.403 -19.687 11.281  1.00 40.56 ? 770 HOH B O   1 
HETATM 8772 O O   . HOH M 6 .   ? -17.412 5.839   56.754  1.00 42.34 ? 771 HOH B O   1 
HETATM 8773 O O   . HOH M 6 .   ? 23.389  8.298   0.661   1.00 42.81 ? 772 HOH B O   1 
HETATM 8774 O O   . HOH M 6 .   ? -30.635 5.240   49.066  1.00 47.07 ? 773 HOH B O   1 
HETATM 8775 O O   . HOH M 6 .   ? -22.127 -7.446  2.383   1.00 40.56 ? 774 HOH B O   1 
HETATM 8776 O O   . HOH M 6 .   ? 2.539   -7.396  48.432  1.00 38.40 ? 775 HOH B O   1 
HETATM 8777 O O   . HOH M 6 .   ? 12.181  11.023  27.888  1.00 30.19 ? 776 HOH B O   1 
HETATM 8778 O O   . HOH M 6 .   ? -28.105 -11.742 28.218  1.00 32.90 ? 777 HOH B O   1 
HETATM 8779 O O   . HOH M 6 .   ? -24.749 6.108   7.913   1.00 41.37 ? 778 HOH B O   1 
HETATM 8780 O O   . HOH M 6 .   ? -34.941 -3.756  18.063  1.00 33.27 ? 779 HOH B O   1 
HETATM 8781 O O   . HOH M 6 .   ? 8.288   9.122   34.468  1.00 24.21 ? 780 HOH B O   1 
HETATM 8782 O O   . HOH M 6 .   ? -32.111 -1.963  16.922  1.00 34.44 ? 781 HOH B O   1 
HETATM 8783 O O   . HOH M 6 .   ? -30.142 -0.234  40.473  1.00 43.87 ? 782 HOH B O   1 
HETATM 8784 O O   . HOH M 6 .   ? -25.016 -13.617 16.129  1.00 22.11 ? 783 HOH B O   1 
HETATM 8785 O O   . HOH M 6 .   ? -30.590 -12.843 12.661  1.00 37.87 ? 784 HOH B O   1 
HETATM 8786 O O   . HOH M 6 .   ? -0.060  10.072  29.555  1.00 16.97 ? 785 HOH B O   1 
HETATM 8787 O O   . HOH M 6 .   ? -0.714  -19.551 43.296  1.00 42.24 ? 786 HOH B O   1 
HETATM 8788 O O   . HOH M 6 .   ? -0.688  11.004  32.022  1.00 17.20 ? 787 HOH B O   1 
HETATM 8789 O O   . HOH M 6 .   ? 9.515   13.019  35.746  1.00 35.52 ? 788 HOH B O   1 
HETATM 8790 O O   . HOH M 6 .   ? 0.094   17.783  44.911  1.00 37.13 ? 789 HOH B O   1 
HETATM 8791 O O   . HOH M 6 .   ? 11.812  -5.849  46.090  1.00 39.20 ? 790 HOH B O   1 
HETATM 8792 O O   . HOH M 6 .   ? -9.670  15.954  42.057  1.00 50.12 ? 791 HOH B O   1 
HETATM 8793 O O   . HOH M 6 .   ? 24.097  14.087  8.831   1.00 47.28 ? 792 HOH B O   1 
HETATM 8794 O O   . HOH M 6 .   ? -11.506 2.511   10.981  1.00 20.42 ? 793 HOH B O   1 
HETATM 8795 O O   . HOH M 6 .   ? 25.653  12.797  6.490   1.00 49.82 ? 794 HOH B O   1 
HETATM 8796 O O   . HOH M 6 .   ? -3.542  -5.900  0.718   1.00 47.26 ? 795 HOH B O   1 
HETATM 8797 O O   . HOH M 6 .   ? 2.306   12.076  10.361  1.00 50.00 ? 796 HOH B O   1 
HETATM 8798 O O   . HOH M 6 .   ? -31.629 -0.118  32.429  1.00 57.91 ? 797 HOH B O   1 
HETATM 8799 O O   . HOH M 6 .   ? -7.113  -5.536  57.531  1.00 45.43 ? 798 HOH B O   1 
HETATM 8800 O O   . HOH M 6 .   ? 7.937   -17.762 23.076  1.00 41.38 ? 799 HOH B O   1 
HETATM 8801 O O   . HOH M 6 .   ? 4.991   -18.588 25.598  1.00 42.68 ? 800 HOH B O   1 
HETATM 8802 O O   . HOH M 6 .   ? -25.131 -19.745 23.414  1.00 59.01 ? 801 HOH B O   1 
HETATM 8803 O O   . HOH M 6 .   ? -26.204 2.342   46.485  1.00 31.98 ? 802 HOH B O   1 
HETATM 8804 O O   . HOH M 6 .   ? -34.628 -8.855  8.904   1.00 43.90 ? 803 HOH B O   1 
HETATM 8805 O O   . HOH M 6 .   ? -32.889 -4.619  31.121  1.00 47.26 ? 804 HOH B O   1 
HETATM 8806 O O   . HOH M 6 .   ? -31.492 -3.033  30.261  1.00 41.48 ? 805 HOH B O   1 
HETATM 8807 O O   . HOH M 6 .   ? -8.809  12.956  37.174  1.00 40.81 ? 806 HOH B O   1 
HETATM 8808 O O   . HOH M 6 .   ? -29.844 3.092   44.359  1.00 34.47 ? 807 HOH B O   1 
HETATM 8809 O O   . HOH M 6 .   ? 10.673  -11.603 41.730  1.00 45.24 ? 808 HOH B O   1 
HETATM 8810 O O   . HOH M 6 .   ? -10.423 -19.879 21.248  1.00 33.32 ? 809 HOH B O   1 
HETATM 8811 O O   . HOH M 6 .   ? -32.678 -5.667  20.128  1.00 37.52 ? 810 HOH B O   1 
HETATM 8812 O O   . HOH M 6 .   ? -9.610  -7.159  16.038  1.00 17.72 ? 811 HOH B O   1 
HETATM 8813 O O   . HOH M 6 .   ? 2.607   16.885  45.010  1.00 37.32 ? 812 HOH B O   1 
HETATM 8814 O O   . HOH M 6 .   ? 25.075  11.983  8.958   1.00 55.57 ? 813 HOH B O   1 
HETATM 8815 O O   . HOH M 6 .   ? -21.112 12.636  25.227  1.00 47.40 ? 814 HOH B O   1 
HETATM 8816 O O   . HOH M 6 .   ? 9.681   -14.419 31.234  1.00 31.65 ? 815 HOH B O   1 
HETATM 8817 O O   . HOH M 6 .   ? -29.837 -4.242  29.076  1.00 28.15 ? 816 HOH B O   1 
HETATM 8818 O O   . HOH M 6 .   ? 7.913   -12.483 13.799  1.00 34.91 ? 817 HOH B O   1 
HETATM 8819 O O   . HOH M 6 .   ? -24.663 10.305  28.503  1.00 38.83 ? 818 HOH B O   1 
HETATM 8820 O O   . HOH M 6 .   ? -28.938 7.704   39.544  1.00 45.49 ? 819 HOH B O   1 
HETATM 8821 O O   . HOH M 6 .   ? 13.406  -6.461  5.900   1.00 35.19 ? 820 HOH B O   1 
HETATM 8822 O O   . HOH M 6 .   ? -26.807 7.724   9.908   1.00 33.68 ? 821 HOH B O   1 
HETATM 8823 O O   . HOH M 6 .   ? -19.172 -6.023  2.237   1.00 42.75 ? 822 HOH B O   1 
HETATM 8824 O O   . HOH M 6 .   ? -9.577  -14.797 35.374  1.00 30.10 ? 823 HOH B O   1 
HETATM 8825 O O   . HOH M 6 .   ? 4.948   -9.839  49.129  1.00 37.18 ? 824 HOH B O   1 
HETATM 8826 O O   . HOH M 6 .   ? -31.479 -6.603  16.376  1.00 40.14 ? 825 HOH B O   1 
HETATM 8827 O O   . HOH M 6 .   ? -32.856 -5.351  29.182  1.00 44.86 ? 826 HOH B O   1 
HETATM 8828 O O   . HOH M 6 .   ? -30.756 -8.833  19.340  1.00 36.03 ? 827 HOH B O   1 
HETATM 8829 O O   . HOH M 6 .   ? -27.606 -13.676 26.295  1.00 54.88 ? 828 HOH B O   1 
HETATM 8830 O O   . HOH M 6 .   ? -8.514  -16.133 37.607  1.00 54.57 ? 829 HOH B O   1 
HETATM 8831 O O   . HOH M 6 .   ? 9.996   4.776   48.870  1.00 45.12 ? 830 HOH B O   1 
HETATM 8832 O O   . HOH M 6 .   ? -25.469 -8.383  49.953  1.00 56.24 ? 831 HOH B O   1 
HETATM 8833 O O   . HOH M 6 .   ? -8.829  -17.008 40.043  1.00 48.00 ? 832 HOH B O   1 
HETATM 8834 O O   . HOH M 6 .   ? -24.793 4.395   6.870   1.00 48.00 ? 833 HOH B O   1 
HETATM 8835 O O   . HOH M 6 .   ? -0.264  -8.485  50.992  1.00 50.25 ? 834 HOH B O   1 
HETATM 8836 O O   . HOH M 6 .   ? 1.402   13.815  12.203  1.00 39.88 ? 835 HOH B O   1 
HETATM 8837 O O   . HOH M 6 .   ? -23.382 -1.041  3.380   1.00 39.79 ? 836 HOH B O   1 
HETATM 8838 O O   . HOH M 6 .   ? 2.544   5.964   57.849  1.00 45.09 ? 837 HOH B O   1 
HETATM 8839 O O   . HOH M 6 .   ? 7.524   11.281  34.968  1.00 36.33 ? 838 HOH B O   1 
HETATM 8840 O O   . HOH M 6 .   ? 1.121   -1.067  3.638   1.00 46.41 ? 839 HOH B O   1 
HETATM 8841 O O   . HOH M 6 .   ? -34.880 13.889  10.759  1.00 50.75 ? 840 HOH B O   1 
HETATM 8842 O O   . HOH M 6 .   ? -11.882 3.384   22.718  1.00 27.13 ? 841 HOH B O   1 
HETATM 8843 O O   . HOH M 6 .   ? -30.526 -11.639 28.806  1.00 45.71 ? 842 HOH B O   1 
HETATM 8844 O O   . HOH M 6 .   ? 2.000   -10.180 50.290  1.00 30.24 ? 843 HOH B O   1 
HETATM 8845 O O   . HOH M 6 .   ? 1.608   -0.509  -4.401  1.00 41.55 ? 844 HOH B O   1 
HETATM 8846 O O   . HOH M 6 .   ? -27.920 -15.701 14.985  1.00 48.13 ? 845 HOH B O   1 
HETATM 8847 O O   . HOH M 6 .   ? 13.202  7.808   -1.412  1.00 49.98 ? 846 HOH B O   1 
HETATM 8848 O O   . HOH M 6 .   ? -5.756  -15.346 47.080  1.00 42.81 ? 847 HOH B O   1 
HETATM 8849 O O   . HOH M 6 .   ? -1.920  -17.623 44.747  1.00 43.79 ? 848 HOH B O   1 
HETATM 8850 O O   . HOH M 6 .   ? 16.123  -7.001  5.583   1.00 45.48 ? 849 HOH B O   1 
HETATM 8851 O O   . HOH M 6 .   ? -13.406 -2.277  59.145  1.00 48.74 ? 850 HOH B O   1 
HETATM 8852 O O   . HOH M 6 .   ? -18.329 3.203   64.402  1.00 59.04 ? 851 HOH B O   1 
HETATM 8853 O O   . HOH M 6 .   ? -4.772  -14.667 14.269  1.00 50.47 ? 852 HOH B O   1 
HETATM 8854 O O   . HOH M 6 .   ? 5.801   -0.638  2.822   1.00 42.22 ? 853 HOH B O   1 
HETATM 8855 O O   . HOH M 6 .   ? -4.998  4.775   21.205  1.00 40.49 ? 854 HOH B O   1 
HETATM 8856 O O   . HOH M 6 .   ? 4.922   -16.995 23.109  1.00 35.91 ? 855 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   ? 0.4784 0.4646 0.2255 0.0615  0.0123  0.0085  2   LYS A N   
2    C CA  . LYS A 2   ? 0.4360 0.4225 0.1983 0.0571  0.0203  0.0111  2   LYS A CA  
3    C C   . LYS A 2   ? 0.4040 0.3791 0.1856 0.0532  0.0158  0.0109  2   LYS A C   
4    O O   . LYS A 2   ? 0.4131 0.3809 0.1974 0.0511  0.0118  0.0183  2   LYS A O   
5    C CB  . LYS A 2   ? 0.5230 0.5145 0.2812 0.0527  0.0288  0.0248  2   LYS A CB  
6    C CG  . LYS A 2   ? 0.5798 0.5766 0.3511 0.0478  0.0377  0.0265  2   LYS A CG  
7    C CD  . LYS A 2   ? 0.6465 0.6379 0.4230 0.0395  0.0419  0.0403  2   LYS A CD  
8    C CE  . LYS A 2   ? 0.7441 0.7380 0.5030 0.0382  0.0447  0.0521  2   LYS A CE  
9    N NZ  . LYS A 2   ? 0.7596 0.7425 0.5225 0.0298  0.0473  0.0654  2   LYS A NZ  
10   N N   . LYS A 3   ? 0.3495 0.3231 0.1438 0.0528  0.0167  0.0027  3   LYS A N   
11   C CA  . LYS A 3   ? 0.3256 0.2896 0.1376 0.0492  0.0128  0.0020  3   LYS A CA  
12   C C   . LYS A 3   ? 0.3175 0.2822 0.1427 0.0442  0.0203  0.0071  3   LYS A C   
13   O O   . LYS A 3   ? 0.3469 0.3209 0.1699 0.0437  0.0282  0.0085  3   LYS A O   
14   C CB  . LYS A 3   ? 0.3858 0.3456 0.2031 0.0515  0.0071  -0.0106 3   LYS A CB  
15   C CG  . LYS A 3   ? 0.5035 0.4622 0.3081 0.0551  -0.0012 -0.0175 3   LYS A CG  
16   C CD  . LYS A 3   ? 0.5913 0.5451 0.4020 0.0525  -0.0100 -0.0149 3   LYS A CD  
17   C CE  . LYS A 3   ? 0.6495 0.6048 0.4469 0.0550  -0.0188 -0.0208 3   LYS A CE  
18   N NZ  . LYS A 3   ? 0.6918 0.6520 0.4792 0.0565  -0.0215 -0.0119 3   LYS A NZ  
19   N N   . LEU A 4   ? 0.2689 0.2248 0.1078 0.0404  0.0178  0.0096  4   LEU A N   
20   C CA  . LEU A 4   ? 0.2553 0.2104 0.1084 0.0356  0.0228  0.0113  4   LEU A CA  
21   C C   . LEU A 4   ? 0.2869 0.2386 0.1518 0.0368  0.0188  0.0020  4   LEU A C   
22   O O   . LEU A 4   ? 0.2771 0.2224 0.1448 0.0378  0.0115  -0.0011 4   LEU A O   
23   C CB  . LEU A 4   ? 0.2530 0.1991 0.1113 0.0306  0.0232  0.0209  4   LEU A CB  
24   C CG  . LEU A 4   ? 0.2700 0.2135 0.1431 0.0250  0.0269  0.0216  4   LEU A CG  
25   C CD1 . LEU A 4   ? 0.2881 0.2251 0.1591 0.0189  0.0309  0.0326  4   LEU A CD1 
26   C CD2 . LEU A 4   ? 0.2286 0.1651 0.1150 0.0254  0.0216  0.0164  4   LEU A CD2 
27   N N   . PHE A 5   ? 0.2350 0.1921 0.1068 0.0368  0.0234  -0.0021 5   PHE A N   
28   C CA  . PHE A 5   ? 0.2439 0.1968 0.1258 0.0381  0.0200  -0.0101 5   PHE A CA  
29   C C   . PHE A 5   ? 0.2208 0.1704 0.1177 0.0327  0.0215  -0.0063 5   PHE A C   
30   O O   . PHE A 5   ? 0.2759 0.2311 0.1765 0.0290  0.0277  -0.0013 5   PHE A O   
31   C CB  . PHE A 5   ? 0.2537 0.2135 0.1326 0.0433  0.0234  -0.0174 5   PHE A CB  
32   C CG  . PHE A 5   ? 0.2930 0.2542 0.1558 0.0495  0.0213  -0.0231 5   PHE A CG  
33   C CD1 . PHE A 5   ? 0.2788 0.2303 0.1362 0.0508  0.0128  -0.0286 5   PHE A CD1 
34   C CD2 . PHE A 5   ? 0.2848 0.2580 0.1372 0.0535  0.0278  -0.0229 5   PHE A CD2 
35   C CE1 . PHE A 5   ? 0.2909 0.2429 0.1320 0.0560  0.0102  -0.0346 5   PHE A CE1 
36   C CE2 . PHE A 5   ? 0.3375 0.3120 0.1732 0.0599  0.0259  -0.0290 5   PHE A CE2 
37   C CZ  . PHE A 5   ? 0.3629 0.3258 0.1924 0.0611  0.0169  -0.0351 5   PHE A CZ  
38   N N   . LEU A 6   ? 0.2010 0.1424 0.1059 0.0316  0.0158  -0.0084 6   LEU A N   
39   C CA  . LEU A 6   ? 0.2109 0.1484 0.1286 0.0270  0.0164  -0.0052 6   LEU A CA  
40   C C   . LEU A 6   ? 0.2087 0.1447 0.1357 0.0277  0.0145  -0.0116 6   LEU A C   
41   O O   . LEU A 6   ? 0.2149 0.1468 0.1403 0.0300  0.0090  -0.0171 6   LEU A O   
42   C CB  . LEU A 6   ? 0.2486 0.1790 0.1674 0.0259  0.0118  -0.0012 6   LEU A CB  
43   C CG  . LEU A 6   ? 0.2211 0.1465 0.1513 0.0223  0.0123  0.0018  6   LEU A CG  
44   C CD1 . LEU A 6   ? 0.2071 0.1328 0.1378 0.0180  0.0188  0.0071  6   LEU A CD1 
45   C CD2 . LEU A 6   ? 0.2140 0.1341 0.1436 0.0237  0.0077  0.0052  6   LEU A CD2 
46   N N   . VAL A 7   ? 0.1796 0.1186 0.1157 0.0252  0.0185  -0.0107 7   VAL A N   
47   C CA  . VAL A 7   ? 0.1624 0.1004 0.1065 0.0264  0.0170  -0.0159 7   VAL A CA  
48   C C   . VAL A 7   ? 0.1787 0.1148 0.1342 0.0216  0.0175  -0.0128 7   VAL A C   
49   O O   . VAL A 7   ? 0.2059 0.1472 0.1651 0.0184  0.0222  -0.0093 7   VAL A O   
50   C CB  . VAL A 7   ? 0.1794 0.1261 0.1221 0.0304  0.0216  -0.0190 7   VAL A CB  
51   C CG1 . VAL A 7   ? 0.2740 0.2164 0.2222 0.0334  0.0188  -0.0246 7   VAL A CG1 
52   C CG2 . VAL A 7   ? 0.2030 0.1536 0.1325 0.0357  0.0226  -0.0218 7   VAL A CG2 
53   N N   . PHE A 8   ? 0.1555 0.0852 0.1164 0.0207  0.0128  -0.0141 8   PHE A N   
54   C CA  . PHE A 8   ? 0.1496 0.0780 0.1205 0.0171  0.0133  -0.0121 8   PHE A CA  
55   C C   . PHE A 8   ? 0.1347 0.0648 0.1116 0.0181  0.0133  -0.0157 8   PHE A C   
56   O O   . PHE A 8   ? 0.1666 0.0931 0.1414 0.0209  0.0100  -0.0199 8   PHE A O   
57   C CB  . PHE A 8   ? 0.1474 0.0709 0.1219 0.0160  0.0087  -0.0113 8   PHE A CB  
58   C CG  . PHE A 8   ? 0.1579 0.0791 0.1281 0.0160  0.0085  -0.0068 8   PHE A CG  
59   C CD1 . PHE A 8   ? 0.1873 0.1057 0.1600 0.0137  0.0111  -0.0028 8   PHE A CD1 
60   C CD2 . PHE A 8   ? 0.1889 0.1098 0.1518 0.0185  0.0050  -0.0069 8   PHE A CD2 
61   C CE1 . PHE A 8   ? 0.2194 0.1331 0.1871 0.0149  0.0107  0.0015  8   PHE A CE1 
62   C CE2 . PHE A 8   ? 0.2079 0.1266 0.1663 0.0197  0.0044  -0.0021 8   PHE A CE2 
63   C CZ  . PHE A 8   ? 0.2393 0.1536 0.2000 0.0183  0.0073  0.0023  8   PHE A CZ  
64   N N   . TRP A 9   ? 0.1246 0.0591 0.1081 0.0155  0.0165  -0.0139 9   TRP A N   
65   C CA  . TRP A 9   ? 0.1230 0.0597 0.1121 0.0171  0.0162  -0.0164 9   TRP A CA  
66   C C   . TRP A 9   ? 0.1318 0.0688 0.1289 0.0126  0.0166  -0.0141 9   TRP A C   
67   O O   . TRP A 9   ? 0.1664 0.1084 0.1657 0.0092  0.0199  -0.0117 9   TRP A O   
68   C CB  . TRP A 9   ? 0.1389 0.0854 0.1269 0.0202  0.0203  -0.0174 9   TRP A CB  
69   C CG  . TRP A 9   ? 0.1295 0.0775 0.1204 0.0252  0.0194  -0.0207 9   TRP A CG  
70   C CD1 . TRP A 9   ? 0.1714 0.1117 0.1656 0.0258  0.0155  -0.0220 9   TRP A CD1 
71   C CD2 . TRP A 9   ? 0.1255 0.0836 0.1155 0.0308  0.0225  -0.0225 9   TRP A CD2 
72   N NE1 . TRP A 9   ? 0.1561 0.0990 0.1509 0.0319  0.0158  -0.0243 9   TRP A NE1 
73   C CE2 . TRP A 9   ? 0.1544 0.1090 0.1470 0.0356  0.0201  -0.0249 9   TRP A CE2 
74   C CE3 . TRP A 9   ? 0.1472 0.1183 0.1346 0.0324  0.0274  -0.0217 9   TRP A CE3 
75   C CZ2 . TRP A 9   ? 0.1566 0.1196 0.1490 0.0435  0.0222  -0.0271 9   TRP A CZ2 
76   C CZ3 . TRP A 9   ? 0.2033 0.1853 0.1913 0.0396  0.0299  -0.0240 9   TRP A CZ3 
77   C CH2 . TRP A 9   ? 0.2045 0.1824 0.1953 0.0457  0.0271  -0.0268 9   TRP A CH2 
78   N N   . TRP A 10  ? 0.1390 0.0706 0.1395 0.0120  0.0130  -0.0147 10  TRP A N   
79   C CA  . TRP A 10  ? 0.1076 0.0406 0.1139 0.0084  0.0125  -0.0125 10  TRP A CA  
80   C C   . TRP A 10  ? 0.1633 0.1005 0.1741 0.0088  0.0124  -0.0131 10  TRP A C   
81   O O   . TRP A 10  ? 0.1407 0.0762 0.1502 0.0108  0.0088  -0.0140 10  TRP A O   
82   C CB  . TRP A 10  ? 0.0986 0.0307 0.1046 0.0076  0.0075  -0.0115 10  TRP A CB  
83   C CG  . TRP A 10  ? 0.1287 0.0568 0.1319 0.0082  0.0071  -0.0108 10  TRP A CG  
84   C CD1 . TRP A 10  ? 0.1643 0.0879 0.1649 0.0098  0.0043  -0.0122 10  TRP A CD1 
85   C CD2 . TRP A 10  ? 0.1153 0.0418 0.1171 0.0076  0.0094  -0.0083 10  TRP A CD2 
86   N NE1 . TRP A 10  ? 0.1492 0.0715 0.1467 0.0108  0.0044  -0.0101 10  TRP A NE1 
87   C CE2 . TRP A 10  ? 0.1117 0.0331 0.1097 0.0099  0.0080  -0.0076 10  TRP A CE2 
88   C CE3 . TRP A 10  ? 0.1469 0.0741 0.1492 0.0052  0.0121  -0.0066 10  TRP A CE3 
89   C CZ2 . TRP A 10  ? 0.1304 0.0482 0.1246 0.0109  0.0090  -0.0046 10  TRP A CZ2 
90   C CZ3 . TRP A 10  ? 0.1774 0.0992 0.1757 0.0053  0.0130  -0.0041 10  TRP A CZ3 
91   C CH2 . TRP A 10  ? 0.1514 0.0684 0.1459 0.0087  0.0115  -0.0029 10  TRP A CH2 
92   N N   . HIS A 11  ? 0.1254 0.0668 0.1402 0.0066  0.0158  -0.0124 11  HIS A N   
93   C CA  . HIS A 11  ? 0.1392 0.0863 0.1582 0.0078  0.0157  -0.0128 11  HIS A CA  
94   C C   . HIS A 11  ? 0.1044 0.0509 0.1271 0.0051  0.0142  -0.0116 11  HIS A C   
95   O O   . HIS A 11  ? 0.1044 0.0520 0.1276 0.0014  0.0152  -0.0107 11  HIS A O   
96   C CB  . HIS A 11  ? 0.1387 0.0968 0.1591 0.0066  0.0191  -0.0124 11  HIS A CB  
97   C CG  . HIS A 11  ? 0.1251 0.0917 0.1509 0.0058  0.0191  -0.0119 11  HIS A CG  
98   N ND1 . HIS A 11  ? 0.1060 0.0756 0.1336 0.0112  0.0175  -0.0124 11  HIS A ND1 
99   C CD2 . HIS A 11  ? 0.1363 0.1080 0.1650 0.0004  0.0199  -0.0111 11  HIS A CD2 
100  C CE1 . HIS A 11  ? 0.0894 0.0677 0.1214 0.0093  0.0174  -0.0114 11  HIS A CE1 
101  N NE2 . HIS A 11  ? 0.1383 0.1181 0.1710 0.0023  0.0187  -0.0110 11  HIS A NE2 
102  N N   . MET A 12  ? 0.1051 0.0513 0.1284 0.0071  0.0114  -0.0111 12  MET A N   
103  C CA  . MET A 12  ? 0.1283 0.0756 0.1531 0.0048  0.0097  -0.0092 12  MET A CA  
104  C C   . MET A 12  ? 0.1201 0.0701 0.1498 0.0065  0.0106  -0.0090 12  MET A C   
105  O O   . MET A 12  ? 0.1093 0.0582 0.1380 0.0110  0.0093  -0.0091 12  MET A O   
106  C CB  . MET A 12  ? 0.1075 0.0503 0.1281 0.0048  0.0059  -0.0079 12  MET A CB  
107  C CG  . MET A 12  ? 0.0909 0.0312 0.1073 0.0041  0.0045  -0.0084 12  MET A CG  
108  S SD  . MET A 12  ? 0.1325 0.0766 0.1506 0.0020  0.0062  -0.0077 12  MET A SD  
109  C CE  . MET A 12  ? 0.1322 0.0723 0.1474 0.0023  0.0038  -0.0079 12  MET A CE  
110  N N   . HIS A 13  ? 0.1086 0.0646 0.1404 0.0033  0.0115  -0.0082 13  HIS A N   
111  C CA  . HIS A 13  ? 0.1178 0.0817 0.1516 0.0047  0.0109  -0.0071 13  HIS A CA  
112  C C   . HIS A 13  ? 0.1322 0.0995 0.1666 0.0011  0.0109  -0.0062 13  HIS A C   
113  O O   . HIS A 13  ? 0.1401 0.1061 0.1736 -0.0026 0.0123  -0.0076 13  HIS A O   
114  C CB  . HIS A 13  ? 0.0775 0.0518 0.1129 0.0051  0.0126  -0.0084 13  HIS A CB  
115  C CG  . HIS A 13  ? 0.0790 0.0652 0.1172 0.0052  0.0119  -0.0074 13  HIS A CG  
116  N ND1 . HIS A 13  ? 0.1038 0.0921 0.1425 0.0107  0.0097  -0.0053 13  HIS A ND1 
117  C CD2 . HIS A 13  ? 0.0901 0.0868 0.1302 0.0003  0.0127  -0.0082 13  HIS A CD2 
118  C CE1 . HIS A 13  ? 0.1026 0.1040 0.1439 0.0098  0.0091  -0.0046 13  HIS A CE1 
119  N NE2 . HIS A 13  ? 0.1040 0.1111 0.1463 0.0029  0.0108  -0.0067 13  HIS A NE2 
120  N N   . GLN A 14  ? 0.1013 0.0722 0.1362 0.0027  0.0092  -0.0038 14  GLN A N   
121  C CA  . GLN A 14  ? 0.1113 0.0892 0.1458 -0.0003 0.0093  -0.0034 14  GLN A CA  
122  C C   . GLN A 14  ? 0.0906 0.0777 0.1262 0.0027  0.0075  -0.0016 14  GLN A C   
123  O O   . GLN A 14  ? 0.1221 0.1057 0.1574 0.0077  0.0057  0.0012  14  GLN A O   
124  C CB  . GLN A 14  ? 0.1277 0.1021 0.1607 -0.0017 0.0090  -0.0011 14  GLN A CB  
125  C CG  . GLN A 14  ? 0.1255 0.0936 0.1583 -0.0037 0.0106  -0.0025 14  GLN A CG  
126  C CD  . GLN A 14  ? 0.1072 0.0766 0.1384 -0.0061 0.0127  -0.0063 14  GLN A CD  
127  O OE1 . GLN A 14  ? 0.1388 0.1138 0.1684 -0.0079 0.0129  -0.0078 14  GLN A OE1 
128  N NE2 . GLN A 14  ? 0.1148 0.0782 0.1455 -0.0062 0.0139  -0.0078 14  GLN A NE2 
129  N N   . PRO A 15  ? 0.1076 0.1057 0.1437 -0.0001 0.0075  -0.0029 15  PRO A N   
130  C CA  . PRO A 15  ? 0.1334 0.1428 0.1706 0.0030  0.0051  -0.0005 15  PRO A CA  
131  C C   . PRO A 15  ? 0.1098 0.1158 0.1436 0.0046  0.0035  0.0036  15  PRO A C   
132  O O   . PRO A 15  ? 0.1261 0.1246 0.1575 0.0019  0.0046  0.0041  15  PRO A O   
133  C CB  . PRO A 15  ? 0.1380 0.1598 0.1760 -0.0027 0.0052  -0.0037 15  PRO A CB  
134  C CG  . PRO A 15  ? 0.1148 0.1274 0.1491 -0.0084 0.0072  -0.0069 15  PRO A CG  
135  C CD  . PRO A 15  ? 0.0770 0.0764 0.1117 -0.0064 0.0091  -0.0066 15  PRO A CD  
136  N N   . LEU A 16  ? 0.1269 0.1399 0.1604 0.0092  0.0009  0.0071  16  LEU A N   
137  C CA  . LEU A 16  ? 0.1470 0.1556 0.1763 0.0109  -0.0008 0.0125  16  LEU A CA  
138  C C   . LEU A 16  ? 0.1027 0.1190 0.1289 0.0058  -0.0004 0.0119  16  LEU A C   
139  O O   . LEU A 16  ? 0.1280 0.1576 0.1539 0.0051  -0.0019 0.0107  16  LEU A O   
140  C CB  . LEU A 16  ? 0.1486 0.1611 0.1774 0.0185  -0.0040 0.0170  16  LEU A CB  
141  C CG  . LEU A 16  ? 0.1417 0.1459 0.1649 0.0206  -0.0060 0.0240  16  LEU A CG  
142  C CD1 . LEU A 16  ? 0.1790 0.1648 0.2001 0.0180  -0.0049 0.0258  16  LEU A CD1 
143  C CD2 . LEU A 16  ? 0.1862 0.1910 0.2084 0.0299  -0.0092 0.0281  16  LEU A CD2 
144  N N   . TYR A 17  ? 0.1143 0.1235 0.1377 0.0026  0.0015  0.0128  17  TYR A N   
145  C CA  . TYR A 17  ? 0.1357 0.1516 0.1548 -0.0011 0.0025  0.0117  17  TYR A CA  
146  C C   . TYR A 17  ? 0.1379 0.1580 0.1522 0.0006  0.0008  0.0183  17  TYR A C   
147  O O   . TYR A 17  ? 0.1518 0.1789 0.1611 -0.0018 0.0017  0.0178  17  TYR A O   
148  C CB  . TYR A 17  ? 0.1559 0.1651 0.1745 -0.0043 0.0059  0.0094  17  TYR A CB  
149  C CG  . TYR A 17  ? 0.1217 0.1269 0.1431 -0.0062 0.0075  0.0030  17  TYR A CG  
150  C CD1 . TYR A 17  ? 0.1476 0.1581 0.1678 -0.0088 0.0074  -0.0023 17  TYR A CD1 
151  C CD2 . TYR A 17  ? 0.1339 0.1294 0.1584 -0.0059 0.0089  0.0028  17  TYR A CD2 
152  C CE1 . TYR A 17  ? 0.1336 0.1383 0.1553 -0.0111 0.0089  -0.0072 17  TYR A CE1 
153  C CE2 . TYR A 17  ? 0.1282 0.1194 0.1541 -0.0072 0.0103  -0.0020 17  TYR A CE2 
154  C CZ  . TYR A 17  ? 0.1349 0.1299 0.1593 -0.0098 0.0105  -0.0066 17  TYR A CZ  
155  O OH  . TYR A 17  ? 0.1293 0.1181 0.1540 -0.0117 0.0119  -0.0104 17  TYR A OH  
156  N N   . ARG A 18  ? 0.1289 0.1435 0.1431 0.0049  -0.0015 0.0245  18  ARG A N   
157  C CA  . ARG A 18  ? 0.1675 0.1821 0.1762 0.0064  -0.0031 0.0324  18  ARG A CA  
158  C C   . ARG A 18  ? 0.1569 0.1850 0.1631 0.0101  -0.0064 0.0337  18  ARG A C   
159  O O   . ARG A 18  ? 0.1949 0.2247 0.2037 0.0157  -0.0092 0.0345  18  ARG A O   
160  C CB  . ARG A 18  ? 0.1925 0.1915 0.2011 0.0095  -0.0047 0.0383  18  ARG A CB  
161  C CG  . ARG A 18  ? 0.2126 0.2075 0.2146 0.0100  -0.0063 0.0475  18  ARG A CG  
162  C CD  . ARG A 18  ? 0.2867 0.2627 0.2874 0.0136  -0.0088 0.0525  18  ARG A CD  
163  N NE  . ARG A 18  ? 0.3464 0.3142 0.3402 0.0118  -0.0100 0.0624  18  ARG A NE  
164  C CZ  . ARG A 18  ? 0.3472 0.3179 0.3346 0.0161  -0.0127 0.0692  18  ARG A CZ  
165  N NH1 . ARG A 18  ? 0.3523 0.3360 0.3402 0.0228  -0.0148 0.0670  18  ARG A NH1 
166  N NH2 . ARG A 18  ? 0.4564 0.4178 0.4368 0.0133  -0.0134 0.0790  18  ARG A NH2 
167  N N   . GLU A 19  ? 0.1533 0.1919 0.1542 0.0074  -0.0062 0.0339  19  GLU A N   
168  C CA  . GLU A 19  ? 0.1560 0.2093 0.1536 0.0101  -0.0098 0.0351  19  GLU A CA  
169  C C   . GLU A 19  ? 0.1993 0.2486 0.1935 0.0166  -0.0131 0.0450  19  GLU A C   
170  O O   . GLU A 19  ? 0.2263 0.2656 0.2157 0.0158  -0.0121 0.0519  19  GLU A O   
171  C CB  . GLU A 19  ? 0.2685 0.3319 0.2590 0.0056  -0.0086 0.0329  19  GLU A CB  
172  C CG  . GLU A 19  ? 0.3425 0.4231 0.3308 0.0053  -0.0122 0.0290  19  GLU A CG  
173  C CD  . GLU A 19  ? 0.3878 0.4775 0.3702 0.0102  -0.0162 0.0371  19  GLU A CD  
174  O OE1 . GLU A 19  ? 0.3620 0.4437 0.3400 0.0126  -0.0156 0.0458  19  GLU A OE1 
175  O OE2 . GLU A 19  ? 0.4674 0.5726 0.4496 0.0112  -0.0203 0.0351  19  GLU A OE2 
176  N N   . PRO A 20  ? 0.2319 0.2893 0.2281 0.0232  -0.0171 0.0463  20  PRO A N   
177  C CA  . PRO A 20  ? 0.2392 0.2876 0.2323 0.0315  -0.0202 0.0554  20  PRO A CA  
178  C C   . PRO A 20  ? 0.3163 0.3681 0.2997 0.0330  -0.0225 0.0642  20  PRO A C   
179  O O   . PRO A 20  ? 0.4103 0.4486 0.3888 0.0381  -0.0244 0.0732  20  PRO A O   
180  C CB  . PRO A 20  ? 0.2213 0.2807 0.2208 0.0391  -0.0233 0.0528  20  PRO A CB  
181  C CG  . PRO A 20  ? 0.2618 0.3417 0.2653 0.0333  -0.0232 0.0449  20  PRO A CG  
182  C CD  . PRO A 20  ? 0.2239 0.2967 0.2266 0.0236  -0.0186 0.0393  20  PRO A CD  
183  N N   . TYR A 21  ? 0.2538 0.3216 0.2331 0.0285  -0.0224 0.0622  21  TYR A N   
184  C CA  . TYR A 21  ? 0.2831 0.3559 0.2521 0.0304  -0.0247 0.0711  21  TYR A CA  
185  C C   . TYR A 21  ? 0.3280 0.3918 0.2904 0.0239  -0.0206 0.0755  21  TYR A C   
186  O O   . TYR A 21  ? 0.4141 0.4704 0.3688 0.0256  -0.0215 0.0863  21  TYR A O   
187  C CB  . TYR A 21  ? 0.2919 0.3887 0.2583 0.0300  -0.0277 0.0671  21  TYR A CB  
188  C CG  . TYR A 21  ? 0.3253 0.4350 0.2982 0.0370  -0.0327 0.0655  21  TYR A CG  
189  C CD1 . TYR A 21  ? 0.3119 0.4263 0.2810 0.0466  -0.0377 0.0744  21  TYR A CD1 
190  C CD2 . TYR A 21  ? 0.3644 0.4821 0.3475 0.0344  -0.0321 0.0556  21  TYR A CD2 
191  C CE1 . TYR A 21  ? 0.2926 0.4218 0.2686 0.0542  -0.0421 0.0731  21  TYR A CE1 
192  C CE2 . TYR A 21  ? 0.3419 0.4747 0.3321 0.0405  -0.0362 0.0545  21  TYR A CE2 
193  C CZ  . TYR A 21  ? 0.3666 0.5063 0.3537 0.0508  -0.0412 0.0631  21  TYR A CZ  
194  O OH  . TYR A 21  ? 0.3327 0.4907 0.3275 0.0582  -0.0452 0.0625  21  TYR A OH  
195  N N   . THR A 22  ? 0.2407 0.3050 0.2062 0.0166  -0.0158 0.0680  22  THR A N   
196  C CA  . THR A 22  ? 0.2466 0.3060 0.2077 0.0107  -0.0112 0.0714  22  THR A CA  
197  C C   . THR A 22  ? 0.3294 0.3704 0.2962 0.0080  -0.0086 0.0730  22  THR A C   
198  O O   . THR A 22  ? 0.3146 0.3509 0.2784 0.0031  -0.0056 0.0788  22  THR A O   
199  C CB  . THR A 22  ? 0.2491 0.3207 0.2090 0.0055  -0.0075 0.0620  22  THR A CB  
200  O OG1 . THR A 22  ? 0.2776 0.3456 0.2465 0.0040  -0.0061 0.0517  22  THR A OG1 
201  C CG2 . THR A 22  ? 0.2629 0.3523 0.2153 0.0068  -0.0103 0.0595  22  THR A CG2 
202  N N   . GLY A 23  ? 0.2489 0.2812 0.2239 0.0104  -0.0097 0.0678  23  GLY A N   
203  C CA  . GLY A 23  ? 0.2170 0.2330 0.1970 0.0074  -0.0076 0.0679  23  GLY A CA  
204  C C   . GLY A 23  ? 0.2571 0.2765 0.2416 0.0012  -0.0028 0.0608  23  GLY A C   
205  O O   . GLY A 23  ? 0.3197 0.3280 0.3085 -0.0020 -0.0012 0.0609  23  GLY A O   
206  N N   . GLU A 24  ? 0.2636 0.2977 0.2467 -0.0002 -0.0009 0.0544  24  GLU A N   
207  C CA  . GLU A 24  ? 0.2455 0.2824 0.2313 -0.0045 0.0037  0.0480  24  GLU A CA  
208  C C   . GLU A 24  ? 0.1740 0.2063 0.1672 -0.0040 0.0039  0.0388  24  GLU A C   
209  O O   . GLU A 24  ? 0.1802 0.2154 0.1750 -0.0014 0.0012  0.0347  24  GLU A O   
210  C CB  . GLU A 24  ? 0.2486 0.3007 0.2274 -0.0055 0.0056  0.0445  24  GLU A CB  
211  C CG  . GLU A 24  ? 0.3118 0.3698 0.2829 -0.0069 0.0070  0.0538  24  GLU A CG  
212  C CD  . GLU A 24  ? 0.4057 0.4792 0.3676 -0.0066 0.0081  0.0506  24  GLU A CD  
213  O OE1 . GLU A 24  ? 0.5303 0.6109 0.4848 -0.0077 0.0098  0.0580  24  GLU A OE1 
214  O OE2 . GLU A 24  ? 0.4671 0.5453 0.4283 -0.0056 0.0071  0.0408  24  GLU A OE2 
215  N N   . TYR A 25  ? 0.1847 0.2108 0.1827 -0.0067 0.0069  0.0362  25  TYR A N   
216  C CA  . TYR A 25  ? 0.1428 0.1646 0.1465 -0.0065 0.0076  0.0279  25  TYR A CA  
217  C C   . TYR A 25  ? 0.1474 0.1776 0.1479 -0.0075 0.0100  0.0202  25  TYR A C   
218  O O   . TYR A 25  ? 0.1677 0.2018 0.1659 -0.0087 0.0135  0.0196  25  TYR A O   
219  C CB  . TYR A 25  ? 0.1869 0.1993 0.1962 -0.0084 0.0094  0.0286  25  TYR A CB  
220  C CG  . TYR A 25  ? 0.1744 0.1742 0.1866 -0.0071 0.0063  0.0323  25  TYR A CG  
221  C CD1 . TYR A 25  ? 0.2178 0.2118 0.2270 -0.0071 0.0042  0.0409  25  TYR A CD1 
222  C CD2 . TYR A 25  ? 0.1957 0.1886 0.2127 -0.0054 0.0056  0.0272  25  TYR A CD2 
223  C CE1 . TYR A 25  ? 0.2694 0.2491 0.2797 -0.0050 0.0012  0.0433  25  TYR A CE1 
224  C CE2 . TYR A 25  ? 0.2047 0.1861 0.2230 -0.0032 0.0031  0.0294  25  TYR A CE2 
225  C CZ  . TYR A 25  ? 0.2238 0.1978 0.2385 -0.0027 0.0007  0.0369  25  TYR A CZ  
226  O OH  . TYR A 25  ? 0.2509 0.2107 0.2655 0.0004  -0.0021 0.0381  25  TYR A OH  
227  N N   . LEU A 26  ? 0.1453 0.1784 0.1452 -0.0071 0.0080  0.0143  26  LEU A N   
228  C CA  . LEU A 26  ? 0.1568 0.1962 0.1509 -0.0086 0.0092  0.0070  26  LEU A CA  
229  C C   . LEU A 26  ? 0.1368 0.1687 0.1324 -0.0096 0.0120  -0.0003 26  LEU A C   
230  O O   . LEU A 26  ? 0.1809 0.2145 0.1701 -0.0101 0.0136  -0.0064 26  LEU A O   
231  C CB  . LEU A 26  ? 0.1488 0.1952 0.1411 -0.0093 0.0052  0.0039  26  LEU A CB  
232  C CG  . LEU A 26  ? 0.2085 0.2641 0.1977 -0.0071 0.0020  0.0111  26  LEU A CG  
233  C CD1 . LEU A 26  ? 0.2210 0.2875 0.2090 -0.0080 -0.0023 0.0073  26  LEU A CD1 
234  C CD2 . LEU A 26  ? 0.2050 0.2660 0.1861 -0.0069 0.0040  0.0149  26  LEU A CD2 
235  N N   . LEU A 27  ? 0.1534 0.1763 0.1561 -0.0094 0.0125  0.0001  27  LEU A N   
236  C CA  . LEU A 27  ? 0.1353 0.1504 0.1393 -0.0094 0.0151  -0.0052 27  LEU A CA  
237  C C   . LEU A 27  ? 0.1325 0.1428 0.1426 -0.0084 0.0164  -0.0006 27  LEU A C   
238  O O   . LEU A 27  ? 0.1580 0.1668 0.1717 -0.0084 0.0144  0.0052  27  LEU A O   
239  C CB  . LEU A 27  ? 0.1829 0.1918 0.1886 -0.0113 0.0137  -0.0106 27  LEU A CB  
240  C CG  . LEU A 27  ? 0.1874 0.1996 0.1870 -0.0144 0.0122  -0.0166 27  LEU A CG  
241  C CD1 . LEU A 27  ? 0.1886 0.1978 0.1917 -0.0178 0.0103  -0.0193 27  LEU A CD1 
242  C CD2 . LEU A 27  ? 0.2364 0.2440 0.2281 -0.0140 0.0147  -0.0229 27  LEU A CD2 
243  N N   . PRO A 28  ? 0.1556 0.1636 0.1664 -0.0072 0.0193  -0.0029 28  PRO A N   
244  C CA  . PRO A 28  ? 0.1368 0.1435 0.1536 -0.0070 0.0203  0.0016  28  PRO A CA  
245  C C   . PRO A 28  ? 0.1332 0.1301 0.1549 -0.0067 0.0193  -0.0001 28  PRO A C   
246  O O   . PRO A 28  ? 0.1449 0.1411 0.1710 -0.0067 0.0198  0.0022  28  PRO A O   
247  C CB  . PRO A 28  ? 0.1286 0.1420 0.1433 -0.0048 0.0241  -0.0003 28  PRO A CB  
248  C CG  . PRO A 28  ? 0.1802 0.1885 0.1888 -0.0027 0.0249  -0.0086 28  PRO A CG  
249  C CD  . PRO A 28  ? 0.1755 0.1831 0.1805 -0.0055 0.0218  -0.0097 28  PRO A CD  
250  N N   . TRP A 29  ? 0.1127 0.1037 0.1336 -0.0070 0.0178  -0.0039 29  TRP A N   
251  C CA  . TRP A 29  ? 0.1250 0.1075 0.1488 -0.0065 0.0177  -0.0061 29  TRP A CA  
252  C C   . TRP A 29  ? 0.1264 0.1055 0.1552 -0.0067 0.0159  -0.0019 29  TRP A C   
253  O O   . TRP A 29  ? 0.1411 0.1153 0.1721 -0.0059 0.0160  -0.0026 29  TRP A O   
254  C CB  . TRP A 29  ? 0.1225 0.1013 0.1443 -0.0080 0.0167  -0.0100 29  TRP A CB  
255  C CG  . TRP A 29  ? 0.1527 0.1313 0.1681 -0.0091 0.0178  -0.0154 29  TRP A CG  
256  C CD1 . TRP A 29  ? 0.1270 0.1097 0.1391 -0.0120 0.0163  -0.0175 29  TRP A CD1 
257  C CD2 . TRP A 29  ? 0.1995 0.1724 0.2102 -0.0072 0.0201  -0.0196 29  TRP A CD2 
258  N NE1 . TRP A 29  ? 0.1417 0.1203 0.1468 -0.0131 0.0173  -0.0233 29  TRP A NE1 
259  C CE2 . TRP A 29  ? 0.1669 0.1384 0.1706 -0.0095 0.0198  -0.0247 29  TRP A CE2 
260  C CE3 . TRP A 29  ? 0.1775 0.1466 0.1892 -0.0033 0.0220  -0.0196 29  TRP A CE3 
261  C CZ2 . TRP A 29  ? 0.1913 0.1546 0.1875 -0.0077 0.0215  -0.0302 29  TRP A CZ2 
262  C CZ3 . TRP A 29  ? 0.2088 0.1717 0.2139 -0.0003 0.0240  -0.0247 29  TRP A CZ3 
263  C CH2 . TRP A 29  ? 0.2222 0.1809 0.2191 -0.0023 0.0237  -0.0301 29  TRP A CH2 
264  N N   . THR A 30  ? 0.1148 0.0952 0.1443 -0.0073 0.0139  0.0025  30  THR A N   
265  C CA  . THR A 30  ? 0.1442 0.1184 0.1767 -0.0075 0.0118  0.0058  30  THR A CA  
266  C C   . THR A 30  ? 0.1243 0.1004 0.1594 -0.0095 0.0125  0.0085  30  THR A C   
267  O O   . THR A 30  ? 0.1479 0.1191 0.1857 -0.0101 0.0114  0.0084  30  THR A O   
268  C CB  . THR A 30  ? 0.1592 0.1316 0.1905 -0.0070 0.0093  0.0101  30  THR A CB  
269  O OG1 . THR A 30  ? 0.1734 0.1475 0.2037 -0.0046 0.0086  0.0075  30  THR A OG1 
270  C CG2 . THR A 30  ? 0.1617 0.1237 0.1942 -0.0072 0.0067  0.0126  30  THR A CG2 
271  N N   . PHE A 31  ? 0.1170 0.1019 0.1514 -0.0107 0.0144  0.0110  31  PHE A N   
272  C CA  . PHE A 31  ? 0.1137 0.1047 0.1517 -0.0129 0.0155  0.0140  31  PHE A CA  
273  C C   . PHE A 31  ? 0.1306 0.1228 0.1711 -0.0104 0.0170  0.0096  31  PHE A C   
274  O O   . PHE A 31  ? 0.1432 0.1353 0.1880 -0.0118 0.0157  0.0109  31  PHE A O   
275  C CB  . PHE A 31  ? 0.1155 0.1184 0.1515 -0.0137 0.0182  0.0170  31  PHE A CB  
276  C CG  . PHE A 31  ? 0.1165 0.1304 0.1570 -0.0157 0.0203  0.0200  31  PHE A CG  
277  C CD1 . PHE A 31  ? 0.1339 0.1496 0.1777 -0.0217 0.0188  0.0269  31  PHE A CD1 
278  C CD2 . PHE A 31  ? 0.1287 0.1514 0.1700 -0.0116 0.0237  0.0160  31  PHE A CD2 
279  C CE1 . PHE A 31  ? 0.1476 0.1770 0.1969 -0.0245 0.0208  0.0301  31  PHE A CE1 
280  C CE2 . PHE A 31  ? 0.1344 0.1713 0.1810 -0.0124 0.0259  0.0189  31  PHE A CE2 
281  C CZ  . PHE A 31  ? 0.1292 0.1709 0.1806 -0.0193 0.0245  0.0260  31  PHE A CZ  
282  N N   . PHE A 32  ? 0.1000 0.0925 0.1370 -0.0066 0.0192  0.0045  32  PHE A N   
283  C CA  . PHE A 32  ? 0.1464 0.1387 0.1843 -0.0030 0.0207  0.0009  32  PHE A CA  
284  C C   . PHE A 32  ? 0.1229 0.1055 0.1624 -0.0028 0.0183  -0.0004 32  PHE A C   
285  O O   . PHE A 32  ? 0.1194 0.1038 0.1621 -0.0012 0.0180  -0.0001 32  PHE A O   
286  C CB  . PHE A 32  ? 0.1354 0.1261 0.1671 0.0007  0.0232  -0.0044 32  PHE A CB  
287  C CG  . PHE A 32  ? 0.1586 0.1608 0.1883 0.0027  0.0263  -0.0043 32  PHE A CG  
288  C CD1 . PHE A 32  ? 0.1867 0.2004 0.2212 0.0047  0.0282  -0.0019 32  PHE A CD1 
289  C CD2 . PHE A 32  ? 0.1796 0.1833 0.2030 0.0025  0.0273  -0.0065 32  PHE A CD2 
290  C CE1 . PHE A 32  ? 0.2404 0.2672 0.2730 0.0072  0.0318  -0.0016 32  PHE A CE1 
291  C CE2 . PHE A 32  ? 0.1835 0.1986 0.2037 0.0049  0.0305  -0.0066 32  PHE A CE2 
292  C CZ  . PHE A 32  ? 0.2048 0.2316 0.2297 0.0074  0.0330  -0.0041 32  PHE A CZ  
293  N N   . HIS A 33  ? 0.1129 0.0871 0.1503 -0.0040 0.0166  -0.0013 33  HIS A N   
294  C CA  . HIS A 33  ? 0.0969 0.0634 0.1350 -0.0036 0.0148  -0.0023 33  HIS A CA  
295  C C   . HIS A 33  ? 0.0991 0.0649 0.1406 -0.0060 0.0119  0.0009  33  HIS A C   
296  O O   . HIS A 33  ? 0.1092 0.0715 0.1515 -0.0053 0.0104  0.0000  33  HIS A O   
297  C CB  . HIS A 33  ? 0.0826 0.0426 0.1174 -0.0037 0.0145  -0.0047 33  HIS A CB  
298  C CG  . HIS A 33  ? 0.0839 0.0411 0.1147 -0.0026 0.0166  -0.0084 33  HIS A CG  
299  N ND1 . HIS A 33  ? 0.1580 0.1095 0.1870 -0.0005 0.0173  -0.0101 33  HIS A ND1 
300  C CD2 . HIS A 33  ? 0.1233 0.0814 0.1507 -0.0038 0.0177  -0.0107 33  HIS A CD2 
301  C CE1 . HIS A 33  ? 0.1316 0.0785 0.1557 -0.0006 0.0188  -0.0131 33  HIS A CE1 
302  N NE2 . HIS A 33  ? 0.1233 0.0744 0.1465 -0.0031 0.0190  -0.0140 33  HIS A NE2 
303  N N   . ALA A 34  ? 0.0915 0.0598 0.1343 -0.0090 0.0109  0.0046  34  ALA A N   
304  C CA  . ALA A 34  ? 0.1346 0.1001 0.1797 -0.0126 0.0077  0.0076  34  ALA A CA  
305  C C   . ALA A 34  ? 0.1790 0.1536 0.2290 -0.0140 0.0078  0.0087  34  ALA A C   
306  O O   . ALA A 34  ? 0.1376 0.1096 0.1892 -0.0154 0.0050  0.0083  34  ALA A O   
307  C CB  . ALA A 34  ? 0.1653 0.1295 0.2095 -0.0161 0.0066  0.0122  34  ALA A CB  
308  N N   . VAL A 35  ? 0.1205 0.1070 0.1726 -0.0132 0.0109  0.0099  35  VAL A N   
309  C CA  . VAL A 35  ? 0.0882 0.0873 0.1463 -0.0138 0.0112  0.0115  35  VAL A CA  
310  C C   . VAL A 35  ? 0.1123 0.1104 0.1704 -0.0083 0.0113  0.0077  35  VAL A C   
311  O O   . VAL A 35  ? 0.1103 0.1159 0.1732 -0.0087 0.0095  0.0087  35  VAL A O   
312  C CB  . VAL A 35  ? 0.1290 0.1434 0.1893 -0.0133 0.0151  0.0139  35  VAL A CB  
313  C CG1 . VAL A 35  ? 0.1101 0.1247 0.1689 -0.0189 0.0151  0.0187  35  VAL A CG1 
314  C CG2 . VAL A 35  ? 0.1763 0.1915 0.2322 -0.0060 0.0189  0.0094  35  VAL A CG2 
315  N N   . LYS A 36  ? 0.1263 0.1154 0.1789 -0.0035 0.0129  0.0037  36  LYS A N   
316  C CA  . LYS A 36  ? 0.1151 0.1013 0.1660 0.0020  0.0132  0.0008  36  LYS A CA  
317  C C   . LYS A 36  ? 0.1160 0.0917 0.1646 0.0013  0.0102  -0.0003 36  LYS A C   
318  O O   . LYS A 36  ? 0.1478 0.1249 0.1973 0.0038  0.0086  -0.0004 36  LYS A O   
319  C CB  . LYS A 36  ? 0.1567 0.1375 0.2018 0.0066  0.0166  -0.0027 36  LYS A CB  
320  C CG  . LYS A 36  ? 0.1182 0.0945 0.1606 0.0128  0.0171  -0.0049 36  LYS A CG  
321  C CD  . LYS A 36  ? 0.1358 0.1047 0.1712 0.0174  0.0203  -0.0087 36  LYS A CD  
322  C CE  . LYS A 36  ? 0.1473 0.1023 0.1765 0.0139  0.0201  -0.0109 36  LYS A CE  
323  N NZ  . LYS A 36  ? 0.1303 0.0754 0.1570 0.0142  0.0185  -0.0106 36  LYS A NZ  
324  N N   . ASP A 37  ? 0.1131 0.0797 0.1585 -0.0013 0.0093  -0.0010 37  ASP A N   
325  C CA  . ASP A 37  ? 0.1995 0.1565 0.2409 -0.0006 0.0076  -0.0028 37  ASP A CA  
326  C C   . ASP A 37  ? 0.1288 0.0808 0.1698 -0.0041 0.0044  -0.0023 37  ASP A C   
327  O O   . ASP A 37  ? 0.1308 0.0793 0.1689 -0.0036 0.0020  -0.0034 37  ASP A O   
328  C CB  . ASP A 37  ? 0.1215 0.0731 0.1567 0.0011  0.0099  -0.0050 37  ASP A CB  
329  C CG  . ASP A 37  ? 0.1202 0.0710 0.1545 0.0042  0.0130  -0.0064 37  ASP A CG  
330  O OD1 . ASP A 37  ? 0.1507 0.1002 0.1842 0.0078  0.0131  -0.0065 37  ASP A OD1 
331  O OD2 . ASP A 37  ? 0.1064 0.0579 0.1398 0.0034  0.0150  -0.0074 37  ASP A OD2 
332  N N   . TYR A 38  ? 0.0795 0.0311 0.1204 -0.0066 0.0041  -0.0008 38  TYR A N   
333  C CA  . TYR A 38  ? 0.1120 0.0583 0.1461 -0.0073 0.0012  -0.0011 38  TYR A CA  
334  C C   . TYR A 38  ? 0.1684 0.1116 0.2037 -0.0109 -0.0025 -0.0004 38  TYR A C   
335  O O   . TYR A 38  ? 0.1482 0.0851 0.1766 -0.0100 -0.0044 -0.0025 38  TYR A O   
336  C CB  . TYR A 38  ? 0.1074 0.0523 0.1401 -0.0079 0.0016  0.0006  38  TYR A CB  
337  C CG  . TYR A 38  ? 0.1147 0.0620 0.1463 -0.0051 0.0043  -0.0007 38  TYR A CG  
338  C CD1 . TYR A 38  ? 0.1189 0.0666 0.1469 -0.0025 0.0052  -0.0034 38  TYR A CD1 
339  C CD2 . TYR A 38  ? 0.1162 0.0653 0.1511 -0.0059 0.0058  0.0012  38  TYR A CD2 
340  C CE1 . TYR A 38  ? 0.1257 0.0757 0.1540 -0.0017 0.0075  -0.0045 38  TYR A CE1 
341  C CE2 . TYR A 38  ? 0.1030 0.0539 0.1379 -0.0044 0.0081  -0.0005 38  TYR A CE2 
342  C CZ  . TYR A 38  ? 0.1583 0.1098 0.1902 -0.0026 0.0088  -0.0035 38  TYR A CZ  
343  O OH  . TYR A 38  ? 0.1286 0.0818 0.1615 -0.0027 0.0111  -0.0052 38  TYR A OH  
344  N N   . TYR A 39  ? 0.1169 0.0651 0.1612 -0.0157 -0.0037 0.0025  39  TYR A N   
345  C CA  . TYR A 39  ? 0.1337 0.0818 0.1797 -0.0205 -0.0082 0.0030  39  TYR A CA  
346  C C   . TYR A 39  ? 0.1164 0.0689 0.1625 -0.0174 -0.0091 0.0005  39  TYR A C   
347  O O   . TYR A 39  ? 0.1305 0.0772 0.1732 -0.0186 -0.0130 -0.0017 39  TYR A O   
348  C CB  . TYR A 39  ? 0.0963 0.0557 0.1491 -0.0267 -0.0085 0.0077  39  TYR A CB  
349  C CG  . TYR A 39  ? 0.1081 0.0710 0.1638 -0.0331 -0.0134 0.0084  39  TYR A CG  
350  C CD1 . TYR A 39  ? 0.1398 0.0909 0.1904 -0.0391 -0.0176 0.0085  39  TYR A CD1 
351  C CD2 . TYR A 39  ? 0.1293 0.1075 0.1907 -0.0323 -0.0139 0.0086  39  TYR A CD2 
352  C CE1 . TYR A 39  ? 0.1819 0.1355 0.2340 -0.0460 -0.0225 0.0085  39  TYR A CE1 
353  C CE2 . TYR A 39  ? 0.1540 0.1375 0.2186 -0.0388 -0.0191 0.0091  39  TYR A CE2 
354  C CZ  . TYR A 39  ? 0.1888 0.1594 0.2496 -0.0471 -0.0240 0.0091  39  TYR A CZ  
355  O OH  . TYR A 39  ? 0.2282 0.2039 0.2917 -0.0552 -0.0298 0.0094  39  TYR A OH  
356  N N   . ASP A 40  ? 0.0950 0.0564 0.1436 -0.0128 -0.0057 0.0008  40  ASP A N   
357  C CA  . ASP A 40  ? 0.1168 0.0841 0.1662 -0.0098 -0.0070 0.0000  40  ASP A CA  
358  C C   . ASP A 40  ? 0.1080 0.0654 0.1499 -0.0057 -0.0075 -0.0030 40  ASP A C   
359  O O   . ASP A 40  ? 0.1268 0.0861 0.1674 -0.0050 -0.0107 -0.0036 40  ASP A O   
360  C CB  . ASP A 40  ? 0.1095 0.0878 0.1629 -0.0050 -0.0034 0.0014  40  ASP A CB  
361  C CG  . ASP A 40  ? 0.1434 0.1379 0.2053 -0.0086 -0.0039 0.0047  40  ASP A CG  
362  O OD1 . ASP A 40  ? 0.1440 0.1472 0.2099 -0.0109 -0.0077 0.0057  40  ASP A OD1 
363  O OD2 . ASP A 40  ? 0.1785 0.1782 0.2430 -0.0097 -0.0007 0.0065  40  ASP A OD2 
364  N N   . MET A 41  ? 0.1100 0.0583 0.1470 -0.0036 -0.0047 -0.0046 41  MET A N   
365  C CA  . MET A 41  ? 0.1091 0.0501 0.1392 -0.0003 -0.0046 -0.0069 41  MET A CA  
366  C C   . MET A 41  ? 0.0999 0.0353 0.1256 -0.0022 -0.0090 -0.0091 41  MET A C   
367  O O   . MET A 41  ? 0.1453 0.0814 0.1673 -0.0004 -0.0110 -0.0099 41  MET A O   
368  C CB  . MET A 41  ? 0.1140 0.0529 0.1376 0.0014  -0.0004 -0.0072 41  MET A CB  
369  C CG  . MET A 41  ? 0.0971 0.0384 0.1213 0.0035  0.0029  -0.0062 41  MET A CG  
370  S SD  . MET A 41  ? 0.1322 0.0694 0.1525 0.0077  0.0034  -0.0059 41  MET A SD  
371  C CE  . MET A 41  ? 0.1169 0.0500 0.1283 0.0071  0.0044  -0.0067 41  MET A CE  
372  N N   . PRO A 42  ? 0.1268 0.0577 0.1509 -0.0055 -0.0106 -0.0098 42  PRO A N   
373  C CA  . PRO A 42  ? 0.1560 0.0802 0.1745 -0.0072 -0.0152 -0.0127 42  PRO A CA  
374  C C   . PRO A 42  ? 0.1546 0.0835 0.1776 -0.0123 -0.0210 -0.0122 42  PRO A C   
375  O O   . PRO A 42  ? 0.1542 0.0798 0.1718 -0.0133 -0.0253 -0.0151 42  PRO A O   
376  C CB  . PRO A 42  ? 0.1908 0.1105 0.2048 -0.0085 -0.0137 -0.0125 42  PRO A CB  
377  C CG  . PRO A 42  ? 0.1610 0.0864 0.1805 -0.0097 -0.0108 -0.0088 42  PRO A CG  
378  C CD  . PRO A 42  ? 0.1170 0.0486 0.1396 -0.0062 -0.0076 -0.0082 42  PRO A CD  
379  N N   . ALA A 43  ? 0.1118 0.0518 0.1438 -0.0156 -0.0205 -0.0084 43  ALA A N   
380  C CA  . ALA A 43  ? 0.1145 0.0653 0.1517 -0.0208 -0.0250 -0.0069 43  ALA A CA  
381  C C   . ALA A 43  ? 0.1541 0.1135 0.1905 -0.0164 -0.0265 -0.0074 43  ALA A C   
382  O O   . ALA A 43  ? 0.1605 0.1288 0.1997 -0.0204 -0.0317 -0.0072 43  ALA A O   
383  C CB  . ALA A 43  ? 0.1357 0.1000 0.1832 -0.0242 -0.0231 -0.0023 43  ALA A CB  
384  N N   . TYR A 44  ? 0.1276 0.0853 0.1604 -0.0087 -0.0224 -0.0075 44  TYR A N   
385  C CA  . TYR A 44  ? 0.1734 0.1355 0.2026 -0.0042 -0.0243 -0.0076 44  TYR A CA  
386  C C   . TYR A 44  ? 0.1679 0.1245 0.1894 -0.0067 -0.0298 -0.0112 44  TYR A C   
387  O O   . TYR A 44  ? 0.1590 0.1235 0.1793 -0.0055 -0.0338 -0.0110 44  TYR A O   
388  C CB  . TYR A 44  ? 0.1623 0.1183 0.1858 0.0030  -0.0192 -0.0072 44  TYR A CB  
389  C CG  . TYR A 44  ? 0.1352 0.0966 0.1636 0.0074  -0.0150 -0.0041 44  TYR A CG  
390  C CD1 . TYR A 44  ? 0.1513 0.1211 0.1811 0.0128  -0.0158 -0.0017 44  TYR A CD1 
391  C CD2 . TYR A 44  ? 0.1177 0.0751 0.1482 0.0071  -0.0102 -0.0040 44  TYR A CD2 
392  C CE1 . TYR A 44  ? 0.1414 0.1134 0.1739 0.0182  -0.0118 0.0003  44  TYR A CE1 
393  C CE2 . TYR A 44  ? 0.1284 0.0890 0.1616 0.0113  -0.0065 -0.0023 44  TYR A CE2 
394  C CZ  . TYR A 44  ? 0.1488 0.1154 0.1825 0.0170  -0.0071 -0.0004 44  TYR A CZ  
395  O OH  . TYR A 44  ? 0.1475 0.1145 0.1822 0.0222  -0.0034 0.0005  44  TYR A OH  
396  N N   . LEU A 45  ? 0.1386 0.0817 0.1540 -0.0093 -0.0304 -0.0148 45  LEU A N   
397  C CA  . LEU A 45  ? 0.1658 0.1013 0.1717 -0.0108 -0.0355 -0.0195 45  LEU A CA  
398  C C   . LEU A 45  ? 0.2224 0.1633 0.2313 -0.0189 -0.0429 -0.0203 45  LEU A C   
399  O O   . LEU A 45  ? 0.2352 0.1726 0.2360 -0.0202 -0.0482 -0.0243 45  LEU A O   
400  C CB  . LEU A 45  ? 0.1892 0.1084 0.1876 -0.0100 -0.0338 -0.0234 45  LEU A CB  
401  C CG  . LEU A 45  ? 0.1990 0.1150 0.1928 -0.0025 -0.0273 -0.0233 45  LEU A CG  
402  C CD1 . LEU A 45  ? 0.2061 0.1105 0.1961 -0.0010 -0.0250 -0.0260 45  LEU A CD1 
403  C CD2 . LEU A 45  ? 0.1984 0.1154 0.1827 0.0021  -0.0278 -0.0250 45  LEU A CD2 
404  N N   . LYS A 46  ? 0.1537 0.1042 0.1737 -0.0248 -0.0436 -0.0167 46  LYS A N   
405  C CA  . LYS A 46  ? 0.2704 0.2304 0.2949 -0.0335 -0.0507 -0.0165 46  LYS A CA  
406  C C   . LYS A 46  ? 0.2696 0.2475 0.2970 -0.0303 -0.0536 -0.0150 46  LYS A C   
407  O O   . LYS A 46  ? 0.2535 0.2388 0.2812 -0.0366 -0.0608 -0.0165 46  LYS A O   
408  C CB  . LYS A 46  ? 0.2606 0.2296 0.2970 -0.0408 -0.0498 -0.0119 46  LYS A CB  
409  C CG  . LYS A 46  ? 0.3038 0.2555 0.3373 -0.0446 -0.0479 -0.0123 46  LYS A CG  
410  C CD  . LYS A 46  ? 0.4422 0.4049 0.4869 -0.0476 -0.0438 -0.0064 46  LYS A CD  
411  C CE  . LYS A 46  ? 0.6275 0.5906 0.6762 -0.0606 -0.0485 -0.0041 46  LYS A CE  
412  N NZ  . LYS A 46  ? 0.7215 0.7046 0.7830 -0.0639 -0.0450 0.0025  46  LYS A NZ  
413  N N   . ASP A 47  ? 0.1875 0.1724 0.2167 -0.0208 -0.0485 -0.0120 47  ASP A N   
414  C CA  . ASP A 47  ? 0.2256 0.2276 0.2579 -0.0158 -0.0507 -0.0093 47  ASP A CA  
415  C C   . ASP A 47  ? 0.2027 0.1980 0.2232 -0.0077 -0.0505 -0.0106 47  ASP A C   
416  O O   . ASP A 47  ? 0.2298 0.2375 0.2503 -0.0039 -0.0541 -0.0088 47  ASP A O   
417  C CB  . ASP A 47  ? 0.2135 0.2288 0.2564 -0.0102 -0.0455 -0.0042 47  ASP A CB  
418  C CG  . ASP A 47  ? 0.3030 0.3314 0.3585 -0.0179 -0.0458 -0.0018 47  ASP A CG  
419  O OD1 . ASP A 47  ? 0.2783 0.3135 0.3371 -0.0276 -0.0520 -0.0025 47  ASP A OD1 
420  O OD2 . ASP A 47  ? 0.3175 0.3494 0.3789 -0.0146 -0.0399 0.0010  47  ASP A OD2 
421  N N   . PHE A 48  ? 0.1808 0.1585 0.1913 -0.0048 -0.0466 -0.0133 48  PHE A N   
422  C CA  . PHE A 48  ? 0.2333 0.2054 0.2323 0.0022  -0.0455 -0.0136 48  PHE A CA  
423  C C   . PHE A 48  ? 0.1802 0.1379 0.1672 0.0001  -0.0467 -0.0195 48  PHE A C   
424  O O   . PHE A 48  ? 0.2599 0.2064 0.2464 -0.0021 -0.0438 -0.0220 48  PHE A O   
425  C CB  . PHE A 48  ? 0.2726 0.2401 0.2713 0.0094  -0.0377 -0.0099 48  PHE A CB  
426  C CG  . PHE A 48  ? 0.2123 0.1915 0.2206 0.0132  -0.0363 -0.0049 48  PHE A CG  
427  C CD1 . PHE A 48  ? 0.2056 0.1940 0.2125 0.0195  -0.0388 -0.0015 48  PHE A CD1 
428  C CD2 . PHE A 48  ? 0.1760 0.1578 0.1942 0.0114  -0.0327 -0.0038 48  PHE A CD2 
429  C CE1 . PHE A 48  ? 0.2328 0.2323 0.2484 0.0247  -0.0376 0.0026  48  PHE A CE1 
430  C CE2 . PHE A 48  ? 0.2357 0.2290 0.2621 0.0161  -0.0311 0.0000  48  PHE A CE2 
431  C CZ  . PHE A 48  ? 0.2126 0.2145 0.2378 0.0231  -0.0335 0.0030  48  PHE A CZ  
432  N N   . GLU A 49  ? 0.2219 0.1802 0.1985 0.0019  -0.0510 -0.0217 49  GLU A N   
433  C CA  . GLU A 49  ? 0.2998 0.2458 0.2636 0.0004  -0.0533 -0.0285 49  GLU A CA  
434  C C   . GLU A 49  ? 0.2729 0.2102 0.2263 0.0075  -0.0467 -0.0287 49  GLU A C   
435  O O   . GLU A 49  ? 0.3340 0.2704 0.2751 0.0110  -0.0479 -0.0306 49  GLU A O   
436  C CB  . GLU A 49  ? 0.3588 0.3110 0.3157 -0.0022 -0.0620 -0.0316 49  GLU A CB  
437  C CG  . GLU A 49  ? 0.6431 0.6032 0.6092 -0.0118 -0.0694 -0.0327 49  GLU A CG  
438  C CD  . GLU A 49  ? 0.8896 0.8352 0.8567 -0.0192 -0.0698 -0.0370 49  GLU A CD  
439  O OE1 . GLU A 49  ? 0.9618 0.9115 0.9418 -0.0237 -0.0681 -0.0334 49  GLU A OE1 
440  O OE2 . GLU A 49  ? 0.9751 0.9048 0.9295 -0.0198 -0.0717 -0.0439 49  GLU A OE2 
441  N N   . ILE A 50  ? 0.2410 0.1735 0.1995 0.0092  -0.0396 -0.0265 50  ILE A N   
442  C CA  . ILE A 50  ? 0.2154 0.1416 0.1662 0.0144  -0.0329 -0.0264 50  ILE A CA  
443  C C   . ILE A 50  ? 0.2580 0.1749 0.2105 0.0132  -0.0299 -0.0301 50  ILE A C   
444  O O   . ILE A 50  ? 0.2667 0.1801 0.2250 0.0084  -0.0331 -0.0322 50  ILE A O   
445  C CB  . ILE A 50  ? 0.2518 0.1821 0.2068 0.0178  -0.0272 -0.0194 50  ILE A CB  
446  C CG1 . ILE A 50  ? 0.2890 0.2208 0.2575 0.0154  -0.0249 -0.0169 50  ILE A CG1 
447  C CG2 . ILE A 50  ? 0.3212 0.2589 0.2724 0.0209  -0.0302 -0.0153 50  ILE A CG2 
448  C CD1 . ILE A 50  ? 0.3047 0.2364 0.2754 0.0184  -0.0190 -0.0116 50  ILE A CD1 
449  N N   . LYS A 51  ? 0.1766 0.0901 0.1235 0.0175  -0.0240 -0.0307 51  LYS A N   
450  C CA  . LYS A 51  ? 0.1946 0.1015 0.1435 0.0182  -0.0206 -0.0334 51  LYS A CA  
451  C C   . LYS A 51  ? 0.1778 0.0888 0.1361 0.0182  -0.0143 -0.0282 51  LYS A C   
452  O O   . LYS A 51  ? 0.1719 0.0879 0.1293 0.0198  -0.0104 -0.0239 51  LYS A O   
453  C CB  . LYS A 51  ? 0.1979 0.1008 0.1345 0.0236  -0.0182 -0.0383 51  LYS A CB  
454  C CG  . LYS A 51  ? 0.2480 0.1465 0.1721 0.0245  -0.0239 -0.0442 51  LYS A CG  
455  C CD  . LYS A 51  ? 0.2641 0.1522 0.1887 0.0199  -0.0309 -0.0493 51  LYS A CD  
456  C CE  . LYS A 51  ? 0.3807 0.2616 0.2899 0.0214  -0.0363 -0.0571 51  LYS A CE  
457  N NZ  . LYS A 51  ? 0.5145 0.3865 0.4259 0.0144  -0.0432 -0.0603 51  LYS A NZ  
458  N N   . LEU A 52  ? 0.1606 0.0687 0.1270 0.0160  -0.0138 -0.0283 52  LEU A N   
459  C CA  . LEU A 52  ? 0.1421 0.0538 0.1165 0.0158  -0.0084 -0.0244 52  LEU A CA  
460  C C   . LEU A 52  ? 0.1849 0.0920 0.1610 0.0169  -0.0071 -0.0270 52  LEU A C   
461  O O   . LEU A 52  ? 0.2064 0.1103 0.1835 0.0146  -0.0102 -0.0288 52  LEU A O   
462  C CB  . LEU A 52  ? 0.1748 0.0903 0.1591 0.0121  -0.0092 -0.0204 52  LEU A CB  
463  C CG  . LEU A 52  ? 0.1732 0.0939 0.1576 0.0123  -0.0109 -0.0172 52  LEU A CG  
464  C CD1 . LEU A 52  ? 0.1576 0.0832 0.1523 0.0095  -0.0123 -0.0146 52  LEU A CD1 
465  C CD2 . LEU A 52  ? 0.2163 0.1380 0.1964 0.0152  -0.0062 -0.0137 52  LEU A CD2 
466  N N   . ASN A 53  ? 0.1600 0.0713 0.1379 0.0191  -0.0016 -0.0256 53  ASN A N   
467  C CA  . ASN A 53  ? 0.1365 0.0489 0.1175 0.0208  0.0001  -0.0269 53  ASN A CA  
468  C C   . ASN A 53  ? 0.1244 0.0423 0.1157 0.0179  0.0026  -0.0231 53  ASN A C   
469  O O   . ASN A 53  ? 0.1352 0.0557 0.1295 0.0157  0.0041  -0.0202 53  ASN A O   
470  C CB  . ASN A 53  ? 0.1438 0.0574 0.1170 0.0275  0.0037  -0.0298 53  ASN A CB  
471  C CG  . ASN A 53  ? 0.1562 0.0665 0.1181 0.0306  0.0020  -0.0336 53  ASN A CG  
472  O OD1 . ASN A 53  ? 0.1771 0.0819 0.1351 0.0316  -0.0016 -0.0374 53  ASN A OD1 
473  N ND2 . ASN A 53  ? 0.1569 0.0741 0.1150 0.0302  0.0046  -0.0311 53  ASN A ND2 
474  N N   . PHE A 54  ? 0.1427 0.0611 0.1375 0.0181  0.0030  -0.0229 54  PHE A N   
475  C CA  . PHE A 54  ? 0.1165 0.0377 0.1144 0.0159  0.0047  -0.0189 54  PHE A CA  
476  C C   . PHE A 54  ? 0.1591 0.0823 0.1590 0.0202  0.0063  -0.0199 54  PHE A C   
477  O O   . PHE A 54  ? 0.1477 0.0679 0.1465 0.0239  0.0052  -0.0228 54  PHE A O   
478  C CB  . PHE A 54  ? 0.1523 0.0705 0.1507 0.0113  0.0021  -0.0166 54  PHE A CB  
479  C CG  . PHE A 54  ? 0.1143 0.0333 0.1140 0.0080  0.0000  -0.0161 54  PHE A CG  
480  C CD1 . PHE A 54  ? 0.1481 0.0631 0.1459 0.0075  -0.0035 -0.0190 54  PHE A CD1 
481  C CD2 . PHE A 54  ? 0.1398 0.0638 0.1425 0.0063  0.0002  -0.0134 54  PHE A CD2 
482  C CE1 . PHE A 54  ? 0.1660 0.0816 0.1650 0.0053  -0.0068 -0.0187 54  PHE A CE1 
483  C CE2 . PHE A 54  ? 0.1781 0.1031 0.1837 0.0047  -0.0015 -0.0130 54  PHE A CE2 
484  C CZ  . PHE A 54  ? 0.1661 0.0871 0.1702 0.0045  -0.0052 -0.0154 54  PHE A CZ  
485  N N   . ASN A 55  ? 0.1303 0.0589 0.1339 0.0205  0.0059  -0.0185 55  ASN A N   
486  C CA  . ASN A 55  ? 0.1616 0.0934 0.1686 0.0246  0.0074  -0.0187 55  ASN A CA  
487  C C   . ASN A 55  ? 0.1333 0.0645 0.1430 0.0208  0.0054  -0.0152 55  ASN A C   
488  O O   . ASN A 55  ? 0.1327 0.0676 0.1460 0.0154  0.0058  -0.0131 55  ASN A O   
489  C CB  . ASN A 55  ? 0.1713 0.1160 0.1838 0.0253  0.0129  -0.0184 55  ASN A CB  
490  C CG  . ASN A 55  ? 0.1604 0.1129 0.1758 0.0308  0.0135  -0.0183 55  ASN A CG  
491  O OD1 . ASN A 55  ? 0.1650 0.1145 0.1763 0.0385  0.0128  -0.0207 55  ASN A OD1 
492  N ND2 . ASN A 55  ? 0.1306 0.0932 0.1524 0.0274  0.0145  -0.0157 55  ASN A ND2 
493  N N   . LEU A 56  ? 0.1330 0.0590 0.1401 0.0241  0.0041  -0.0144 56  LEU A N   
494  C CA  . LEU A 56  ? 0.1730 0.0990 0.1834 0.0215  0.0026  -0.0111 56  LEU A CA  
495  C C   . LEU A 56  ? 0.1468 0.0771 0.1622 0.0279  0.0035  -0.0110 56  LEU A C   
496  O O   . LEU A 56  ? 0.1801 0.1064 0.1924 0.0342  0.0038  -0.0118 56  LEU A O   
497  C CB  . LEU A 56  ? 0.2184 0.1339 0.2232 0.0188  0.0012  -0.0093 56  LEU A CB  
498  C CG  . LEU A 56  ? 0.2083 0.1219 0.2111 0.0128  0.0005  -0.0094 56  LEU A CG  
499  C CD1 . LEU A 56  ? 0.2235 0.1283 0.2253 0.0104  -0.0009 -0.0087 56  LEU A CD1 
500  C CD2 . LEU A 56  ? 0.2145 0.1358 0.2221 0.0080  -0.0003 -0.0074 56  LEU A CD2 
501  N N   . THR A 57  ? 0.1261 0.0664 0.1497 0.0258  0.0052  -0.0092 57  THR A N   
502  C CA  . THR A 57  ? 0.1250 0.0739 0.1505 0.0312  0.0051  -0.0078 57  THR A CA  
503  C C   . THR A 57  ? 0.1487 0.0863 0.1713 0.0338  0.0015  -0.0046 57  THR A C   
504  O O   . THR A 57  ? 0.1406 0.0698 0.1624 0.0281  -0.0001 -0.0023 57  THR A O   
505  C CB  . THR A 57  ? 0.0982 0.0639 0.1295 0.0269  0.0072  -0.0065 57  THR A CB  
506  O OG1 . THR A 57  ? 0.1139 0.0772 0.1461 0.0208  0.0062  -0.0042 57  THR A OG1 
507  C CG2 . THR A 57  ? 0.1287 0.1031 0.1618 0.0229  0.0106  -0.0089 57  THR A CG2 
508  N N   . PRO A 58  ? 0.1258 0.0636 0.1466 0.0425  0.0003  -0.0039 58  PRO A N   
509  C CA  . PRO A 58  ? 0.1446 0.0690 0.1612 0.0450  -0.0034 0.0001  58  PRO A CA  
510  C C   . PRO A 58  ? 0.1825 0.1132 0.2022 0.0389  -0.0038 0.0050  58  PRO A C   
511  O O   . PRO A 58  ? 0.1646 0.0827 0.1809 0.0356  -0.0062 0.0088  58  PRO A O   
512  C CB  . PRO A 58  ? 0.1989 0.1282 0.2144 0.0556  -0.0037 -0.0001 58  PRO A CB  
513  C CG  . PRO A 58  ? 0.1644 0.1017 0.1808 0.0586  -0.0006 -0.0055 58  PRO A CG  
514  C CD  . PRO A 58  ? 0.1268 0.0756 0.1484 0.0513  0.0021  -0.0064 58  PRO A CD  
515  N N   . VAL A 59  ? 0.1590 0.1088 0.1844 0.0368  -0.0017 0.0049  59  VAL A N   
516  C CA  . VAL A 59  ? 0.1538 0.1103 0.1807 0.0315  -0.0021 0.0088  59  VAL A CA  
517  C C   . VAL A 59  ? 0.1761 0.1265 0.2030 0.0225  -0.0012 0.0089  59  VAL A C   
518  O O   . VAL A 59  ? 0.1477 0.0955 0.1731 0.0190  -0.0021 0.0131  59  VAL A O   
519  C CB  . VAL A 59  ? 0.1149 0.0927 0.1470 0.0308  -0.0006 0.0077  59  VAL A CB  
520  C CG1 . VAL A 59  ? 0.1189 0.1043 0.1547 0.0257  0.0026  0.0030  59  VAL A CG1 
521  C CG2 . VAL A 59  ? 0.1322 0.1164 0.1640 0.0260  -0.0015 0.0110  59  VAL A CG2 
522  N N   . LEU A 60  ? 0.1185 0.0671 0.1467 0.0193  0.0007  0.0049  60  LEU A N   
523  C CA  . LEU A 60  ? 0.1326 0.0758 0.1609 0.0126  0.0012  0.0053  60  LEU A CA  
524  C C   . LEU A 60  ? 0.1781 0.1066 0.2029 0.0116  -0.0017 0.0083  60  LEU A C   
525  O O   . LEU A 60  ? 0.1544 0.0821 0.1796 0.0063  -0.0019 0.0118  60  LEU A O   
526  C CB  . LEU A 60  ? 0.0944 0.0379 0.1240 0.0107  0.0032  0.0009  60  LEU A CB  
527  C CG  . LEU A 60  ? 0.1153 0.0539 0.1453 0.0053  0.0031  0.0012  60  LEU A CG  
528  C CD1 . LEU A 60  ? 0.1351 0.0815 0.1672 0.0011  0.0047  0.0031  60  LEU A CD1 
529  C CD2 . LEU A 60  ? 0.1117 0.0529 0.1395 0.0046  0.0043  -0.0025 60  LEU A CD2 
530  N N   . ILE A 61  ? 0.1469 0.0648 0.1662 0.0161  -0.0035 0.0067  61  ILE A N   
531  C CA  . ILE A 61  ? 0.1642 0.0699 0.1754 0.0137  -0.0052 0.0086  61  ILE A CA  
532  C C   . ILE A 61  ? 0.1484 0.0500 0.1592 0.0127  -0.0070 0.0150  61  ILE A C   
533  O O   . ILE A 61  ? 0.1612 0.0594 0.1706 0.0060  -0.0075 0.0182  61  ILE A O   
534  C CB  . ILE A 61  ? 0.1444 0.0422 0.1505 0.0194  -0.0046 0.0057  61  ILE A CB  
535  C CG1 . ILE A 61  ? 0.1746 0.0761 0.1803 0.0189  -0.0027 0.0005  61  ILE A CG1 
536  C CG2 . ILE A 61  ? 0.1840 0.0696 0.1863 0.0168  -0.0060 0.0079  61  ILE A CG2 
537  C CD1 . ILE A 61  ? 0.1845 0.0821 0.1895 0.0251  -0.0022 -0.0027 61  ILE A CD1 
538  N N   . ASP A 62  ? 0.1646 0.0683 0.1772 0.0194  -0.0083 0.0176  62  ASP A N   
539  C CA  . ASP A 62  ? 0.1772 0.0776 0.1879 0.0193  -0.0104 0.0250  62  ASP A CA  
540  C C   . ASP A 62  ? 0.1663 0.0763 0.1800 0.0104  -0.0085 0.0283  62  ASP A C   
541  O O   . ASP A 62  ? 0.2073 0.1108 0.2180 0.0058  -0.0098 0.0346  62  ASP A O   
542  C CB  . ASP A 62  ? 0.1919 0.1043 0.2031 0.0273  -0.0103 0.0259  62  ASP A CB  
543  C CG  . ASP A 62  ? 0.2741 0.1766 0.2809 0.0383  -0.0127 0.0250  62  ASP A CG  
544  O OD1 . ASP A 62  ? 0.3234 0.2121 0.3258 0.0378  -0.0125 0.0244  62  ASP A OD1 
545  O OD2 . ASP A 62  ? 0.2535 0.1700 0.2629 0.0457  -0.0122 0.0240  62  ASP A OD2 
546  N N   . GLN A 63  ? 0.1304 0.0559 0.1494 0.0080  -0.0053 0.0244  63  GLN A N   
547  C CA  . GLN A 63  ? 0.1411 0.0769 0.1622 0.0015  -0.0030 0.0265  63  GLN A CA  
548  C C   . GLN A 63  ? 0.1383 0.0690 0.1610 -0.0054 -0.0028 0.0273  63  GLN A C   
549  O O   . GLN A 63  ? 0.1607 0.0949 0.1834 -0.0108 -0.0021 0.0323  63  GLN A O   
550  C CB  . GLN A 63  ? 0.1085 0.0589 0.1334 0.0018  0.0000  0.0212  63  GLN A CB  
551  C CG  . GLN A 63  ? 0.1116 0.0716 0.1359 0.0065  -0.0004 0.0206  63  GLN A CG  
552  C CD  . GLN A 63  ? 0.1998 0.1718 0.2271 0.0048  0.0021  0.0150  63  GLN A CD  
553  O OE1 . GLN A 63  ? 0.2490 0.2283 0.2756 0.0011  0.0039  0.0144  63  GLN A OE1 
554  N NE2 . GLN A 63  ? 0.1386 0.1120 0.1682 0.0072  0.0025  0.0109  63  GLN A NE2 
555  N N   . ILE A 64  ? 0.1554 0.0800 0.1797 -0.0055 -0.0032 0.0227  64  ILE A N   
556  C CA  . ILE A 64  ? 0.1360 0.0584 0.1607 -0.0119 -0.0037 0.0231  64  ILE A CA  
557  C C   . ILE A 64  ? 0.1649 0.0778 0.1837 -0.0155 -0.0059 0.0280  64  ILE A C   
558  O O   . ILE A 64  ? 0.1748 0.0918 0.1956 -0.0225 -0.0055 0.0319  64  ILE A O   
559  C CB  . ILE A 64  ? 0.1267 0.0468 0.1490 -0.0102 -0.0040 0.0163  64  ILE A CB  
560  C CG1 . ILE A 64  ? 0.1420 0.0718 0.1695 -0.0080 -0.0013 0.0122  64  ILE A CG1 
561  C CG2 . ILE A 64  ? 0.1632 0.0822 0.1853 -0.0165 -0.0050 0.0167  64  ILE A CG2 
562  C CD1 . ILE A 64  ? 0.1589 0.0865 0.1823 -0.0055 -0.0018 0.0068  64  ILE A CD1 
563  N N   . GLN A 65  ? 0.1784 0.0791 0.1902 -0.0105 -0.0077 0.0280  65  GLN A N   
564  C CA  . GLN A 65  ? 0.2096 0.0993 0.2157 -0.0134 -0.0092 0.0327  65  GLN A CA  
565  C C   . GLN A 65  ? 0.2227 0.1174 0.2295 -0.0176 -0.0090 0.0410  65  GLN A C   
566  O O   . GLN A 65  ? 0.2335 0.1263 0.2389 -0.0247 -0.0091 0.0454  65  GLN A O   
567  C CB  . GLN A 65  ? 0.2159 0.0924 0.2156 -0.0052 -0.0104 0.0315  65  GLN A CB  
568  C CG  . GLN A 65  ? 0.2559 0.1276 0.2546 -0.0023 -0.0101 0.0244  65  GLN A CG  
569  C CD  . GLN A 65  ? 0.3179 0.1792 0.3126 0.0064  -0.0109 0.0234  65  GLN A CD  
570  O OE1 . GLN A 65  ? 0.3387 0.2032 0.3337 0.0141  -0.0110 0.0244  65  GLN A OE1 
571  N NE2 . GLN A 65  ? 0.4020 0.2516 0.3936 0.0055  -0.0122 0.0214  65  GLN A NE2 
572  N N   . GLU A 66  ? 0.2172 0.1198 0.2266 -0.0137 -0.0086 0.0438  66  GLU A N   
573  C CA  . GLU A 66  ? 0.2475 0.1569 0.2564 -0.0174 -0.0079 0.0526  66  GLU A CA  
574  C C   . GLU A 66  ? 0.1928 0.1166 0.2074 -0.0259 -0.0047 0.0542  66  GLU A C   
575  O O   . GLU A 66  ? 0.2275 0.1541 0.2399 -0.0319 -0.0040 0.0607  66  GLU A O   
576  C CB  . GLU A 66  ? 0.2538 0.1751 0.2622 -0.0100 -0.0068 0.0518  66  GLU A CB  
577  C CG  . GLU A 66  ? 0.3620 0.2899 0.3657 -0.0118 -0.0063 0.0600  66  GLU A CG  
578  C CD  . GLU A 66  ? 0.3522 0.2899 0.3534 -0.0039 -0.0068 0.0595  66  GLU A CD  
579  O OE1 . GLU A 66  ? 0.3558 0.2961 0.3598 0.0023  -0.0073 0.0530  66  GLU A OE1 
580  O OE2 . GLU A 66  ? 0.3864 0.3310 0.3829 -0.0046 -0.0066 0.0659  66  GLU A OE2 
581  N N   . TYR A 67  ? 0.1727 0.1077 0.1935 -0.0253 -0.0021 0.0472  67  TYR A N   
582  C CA  . TYR A 67  ? 0.1695 0.1189 0.1957 -0.0315 0.0010  0.0480  67  TYR A CA  
583  C C   . TYR A 67  ? 0.2530 0.1964 0.2799 -0.0392 -0.0009 0.0507  67  TYR A C   
584  O O   . TYR A 67  ? 0.2051 0.1589 0.2337 -0.0457 0.0009  0.0557  67  TYR A O   
585  C CB  . TYR A 67  ? 0.1392 0.0985 0.1706 -0.0280 0.0036  0.0397  67  TYR A CB  
586  C CG  . TYR A 67  ? 0.1770 0.1483 0.2073 -0.0229 0.0068  0.0362  67  TYR A CG  
587  C CD1 . TYR A 67  ? 0.1737 0.1604 0.2047 -0.0243 0.0106  0.0374  67  TYR A CD1 
588  C CD2 . TYR A 67  ? 0.1518 0.1196 0.1800 -0.0170 0.0060  0.0316  67  TYR A CD2 
589  C CE1 . TYR A 67  ? 0.1242 0.1197 0.1526 -0.0201 0.0130  0.0332  67  TYR A CE1 
590  C CE2 . TYR A 67  ? 0.1639 0.1423 0.1907 -0.0139 0.0083  0.0279  67  TYR A CE2 
591  C CZ  . TYR A 67  ? 0.1570 0.1477 0.1831 -0.0156 0.0115  0.0286  67  TYR A CZ  
592  O OH  . TYR A 67  ? 0.1918 0.1908 0.2149 -0.0130 0.0134  0.0242  67  TYR A OH  
593  N N   . ALA A 68  ? 0.2576 0.1874 0.2813 -0.0375 -0.0038 0.0453  68  ALA A N   
594  C CA  . ALA A 68  ? 0.2132 0.1390 0.2364 -0.0439 -0.0054 0.0452  68  ALA A CA  
595  C C   . ALA A 68  ? 0.2178 0.1366 0.2357 -0.0486 -0.0062 0.0522  68  ALA A C   
596  O O   . ALA A 68  ? 0.2710 0.1930 0.2908 -0.0566 -0.0065 0.0550  68  ALA A O   
597  C CB  . ALA A 68  ? 0.2116 0.1244 0.2313 -0.0402 -0.0078 0.0381  68  ALA A CB  
598  N N   . GLN A 69  ? 0.3225 0.1752 0.2190 -0.0083 0.0120  0.0293  69  GLN A N   
599  C CA  . GLN A 69  ? 0.3635 0.1783 0.2321 -0.0098 0.0246  0.0349  69  GLN A CA  
600  C C   . GLN A 69  ? 0.3902 0.2115 0.2591 -0.0140 0.0285  0.0386  69  GLN A C   
601  O O   . GLN A 69  ? 0.4795 0.2677 0.3227 -0.0147 0.0402  0.0442  69  GLN A O   
602  C CB  . GLN A 69  ? 0.4359 0.2259 0.2794 0.0121  0.0265  0.0444  69  GLN A CB  
603  C CG  . GLN A 69  ? 0.5190 0.2893 0.3528 0.0154  0.0272  0.0413  69  GLN A CG  
604  C CD  . GLN A 69  ? 0.6380 0.4002 0.4561 0.0412  0.0251  0.0497  69  GLN A CD  
605  O OE1 . GLN A 69  ? 0.6960 0.4636 0.5064 0.0569  0.0242  0.0578  69  GLN A OE1 
606  N NE2 . GLN A 69  ? 0.6546 0.4077 0.4686 0.0465  0.0237  0.0469  69  GLN A NE2 
607  N N   . GLY A 70  ? 0.3271 0.1868 0.2214 -0.0161 0.0201  0.0360  70  GLY A N   
608  C CA  . GLY A 70  ? 0.3457 0.2122 0.2395 -0.0181 0.0234  0.0399  70  GLY A CA  
609  C C   . GLY A 70  ? 0.4545 0.3138 0.3312 0.0017  0.0230  0.0506  70  GLY A C   
610  O O   . GLY A 70  ? 0.5360 0.3876 0.4012 0.0018  0.0290  0.0555  70  GLY A O   
611  N N   . LYS A 71  ? 0.3622 0.2266 0.2373 0.0190  0.0159  0.0536  71  LYS A N   
612  C CA  . LYS A 71  ? 0.3982 0.2613 0.2573 0.0400  0.0144  0.0623  71  LYS A CA  
613  C C   . LYS A 71  ? 0.3948 0.3002 0.2757 0.0473  0.0029  0.0607  71  LYS A C   
614  O O   . LYS A 71  ? 0.4184 0.3303 0.2889 0.0627  0.0009  0.0660  71  LYS A O   
615  C CB  . LYS A 71  ? 0.4593 0.3014 0.2991 0.0568  0.0153  0.0664  71  LYS A CB  
616  C CG  . LYS A 71  ? 0.5510 0.3414 0.3580 0.0546  0.0291  0.0702  71  LYS A CG  
617  C CD  . LYS A 71  ? 0.5996 0.3704 0.3882 0.0725  0.0294  0.0735  71  LYS A CD  
618  C CE  . LYS A 71  ? 0.7620 0.4753 0.5145 0.0692  0.0447  0.0766  71  LYS A CE  
619  N NZ  . LYS A 71  ? 0.8386 0.5304 0.5722 0.0864  0.0456  0.0790  71  LYS A NZ  
620  N N   . ALA A 72  ? 0.2966 0.2295 0.2048 0.0374  -0.0041 0.0531  72  ALA A N   
621  C CA  . ALA A 72  ? 0.2801 0.2482 0.2063 0.0430  -0.0132 0.0505  72  ALA A CA  
622  C C   . ALA A 72  ? 0.3087 0.2902 0.2391 0.0384  -0.0133 0.0507  72  ALA A C   
623  O O   . ALA A 72  ? 0.3504 0.3321 0.2887 0.0245  -0.0104 0.0476  72  ALA A O   
624  C CB  . ALA A 72  ? 0.2399 0.2253 0.1881 0.0352  -0.0186 0.0431  72  ALA A CB  
625  N N   . LYS A 73  ? 0.2732 0.2682 0.1981 0.0508  -0.0166 0.0536  73  LYS A N   
626  C CA  . LYS A 73  ? 0.2765 0.2867 0.2049 0.0482  -0.0176 0.0531  73  LYS A CA  
627  C C   . LYS A 73  ? 0.2684 0.3106 0.2198 0.0440  -0.0253 0.0453  73  LYS A C   
628  O O   . LYS A 73  ? 0.2982 0.3610 0.2530 0.0528  -0.0308 0.0431  73  LYS A O   
629  C CB  . LYS A 73  ? 0.3551 0.3625 0.2624 0.0645  -0.0171 0.0595  73  LYS A CB  
630  C CG  . LYS A 73  ? 0.4926 0.4612 0.3703 0.0700  -0.0071 0.0684  73  LYS A CG  
631  C CD  . LYS A 73  ? 0.6337 0.5995 0.4888 0.0852  -0.0057 0.0749  73  LYS A CD  
632  C CE  . LYS A 73  ? 0.7051 0.6932 0.5566 0.1067  -0.0144 0.0751  73  LYS A CE  
633  N NZ  . LYS A 73  ? 0.7639 0.7315 0.6009 0.1188  -0.0121 0.0790  73  LYS A NZ  
634  N N   . ASP A 74  ? 0.2389 0.2853 0.2048 0.0307  -0.0249 0.0405  74  ASP A N   
635  C CA  . ASP A 74  ? 0.1609 0.2285 0.1444 0.0259  -0.0297 0.0333  74  ASP A CA  
636  C C   . ASP A 74  ? 0.1831 0.2634 0.1694 0.0222  -0.0301 0.0311  74  ASP A C   
637  O O   . ASP A 74  ? 0.1911 0.2660 0.1780 0.0152  -0.0266 0.0314  74  ASP A O   
638  C CB  . ASP A 74  ? 0.1536 0.2150 0.1467 0.0172  -0.0288 0.0299  74  ASP A CB  
639  C CG  . ASP A 74  ? 0.2161 0.2917 0.2219 0.0136  -0.0317 0.0235  74  ASP A CG  
640  O OD1 . ASP A 74  ? 0.2024 0.2897 0.2114 0.0116  -0.0323 0.0206  74  ASP A OD1 
641  O OD2 . ASP A 74  ? 0.2117 0.2839 0.2220 0.0129  -0.0323 0.0212  74  ASP A OD2 
642  N N   . VAL A 75  ? 0.2052 0.3042 0.1932 0.0267  -0.0340 0.0280  75  VAL A N   
643  C CA  . VAL A 75  ? 0.2218 0.3308 0.2084 0.0247  -0.0342 0.0260  75  VAL A CA  
644  C C   . VAL A 75  ? 0.2420 0.3523 0.2385 0.0144  -0.0326 0.0210  75  VAL A C   
645  O O   . VAL A 75  ? 0.2038 0.3128 0.1977 0.0114  -0.0301 0.0216  75  VAL A O   
646  C CB  . VAL A 75  ? 0.2720 0.4037 0.2582 0.0310  -0.0392 0.0217  75  VAL A CB  
647  C CG1 . VAL A 75  ? 0.2454 0.3768 0.2185 0.0455  -0.0409 0.0274  75  VAL A CG1 
648  C CG2 . VAL A 75  ? 0.2846 0.4309 0.2844 0.0256  -0.0414 0.0132  75  VAL A CG2 
649  N N   . PHE A 76  ? 0.1953 0.3068 0.2011 0.0103  -0.0333 0.0163  76  PHE A N   
650  C CA  . PHE A 76  ? 0.2085 0.3177 0.2189 0.0040  -0.0311 0.0123  76  PHE A CA  
651  C C   . PHE A 76  ? 0.2004 0.3003 0.2115 0.0020  -0.0286 0.0154  76  PHE A C   
652  O O   . PHE A 76  ? 0.1778 0.2797 0.1896 -0.0003 -0.0266 0.0139  76  PHE A O   
653  C CB  . PHE A 76  ? 0.2192 0.3274 0.2349 0.0015  -0.0310 0.0073  76  PHE A CB  
654  C CG  . PHE A 76  ? 0.2986 0.4014 0.3136 -0.0018 -0.0280 0.0035  76  PHE A CG  
655  C CD1 . PHE A 76  ? 0.3304 0.4366 0.3420 -0.0051 -0.0261 -0.0018 76  PHE A CD1 
656  C CD2 . PHE A 76  ? 0.3389 0.4330 0.3548 -0.0006 -0.0270 0.0045  76  PHE A CD2 
657  C CE1 . PHE A 76  ? 0.3619 0.4583 0.3684 -0.0060 -0.0222 -0.0047 76  PHE A CE1 
658  C CE2 . PHE A 76  ? 0.3123 0.4009 0.3242 0.0002  -0.0242 0.0014  76  PHE A CE2 
659  C CZ  . PHE A 76  ? 0.3785 0.4659 0.3845 -0.0020 -0.0212 -0.0026 76  PHE A CZ  
660  N N   . LEU A 77  ? 0.1817 0.2727 0.1924 0.0026  -0.0283 0.0188  77  LEU A N   
661  C CA  . LEU A 77  ? 0.1993 0.2852 0.2120 -0.0019 -0.0255 0.0193  77  LEU A CA  
662  C C   . LEU A 77  ? 0.2296 0.3148 0.2366 -0.0043 -0.0214 0.0225  77  LEU A C   
663  O O   . LEU A 77  ? 0.2454 0.3349 0.2568 -0.0094 -0.0184 0.0205  77  LEU A O   
664  C CB  . LEU A 77  ? 0.2181 0.2927 0.2298 -0.0023 -0.0253 0.0209  77  LEU A CB  
665  C CG  . LEU A 77  ? 0.3640 0.4367 0.3805 -0.0085 -0.0236 0.0180  77  LEU A CG  
666  C CD1 . LEU A 77  ? 0.2889 0.3736 0.3139 -0.0078 -0.0261 0.0124  77  LEU A CD1 
667  C CD2 . LEU A 77  ? 0.3936 0.4529 0.4066 -0.0082 -0.0238 0.0189  77  LEU A CD2 
668  N N   . GLU A 78  ? 0.2025 0.2842 0.1993 0.0003  -0.0208 0.0270  78  GLU A N   
669  C CA  . GLU A 78  ? 0.2230 0.3017 0.2110 -0.0009 -0.0158 0.0306  78  GLU A CA  
670  C C   . GLU A 78  ? 0.2370 0.3292 0.2302 -0.0032 -0.0156 0.0268  78  GLU A C   
671  O O   . GLU A 78  ? 0.2892 0.3821 0.2817 -0.0077 -0.0103 0.0273  78  GLU A O   
672  C CB  . GLU A 78  ? 0.2973 0.3705 0.2700 0.0081  -0.0162 0.0361  78  GLU A CB  
673  C CG  . GLU A 78  ? 0.4644 0.5176 0.4246 0.0123  -0.0132 0.0419  78  GLU A CG  
674  C CD  . GLU A 78  ? 0.6655 0.7169 0.6094 0.0263  -0.0153 0.0470  78  GLU A CD  
675  O OE1 . GLU A 78  ? 0.6755 0.7441 0.6194 0.0313  -0.0196 0.0450  78  GLU A OE1 
676  O OE2 . GLU A 78  ? 0.7356 0.7687 0.6654 0.0333  -0.0127 0.0523  78  GLU A OE2 
677  N N   . ALA A 79  ? 0.2016 0.3034 0.1992 -0.0006 -0.0202 0.0222  79  ALA A N   
678  C CA  . ALA A 79  ? 0.2278 0.3382 0.2274 -0.0016 -0.0195 0.0180  79  ALA A CA  
679  C C   . ALA A 79  ? 0.2142 0.3276 0.2221 -0.0043 -0.0176 0.0148  79  ALA A C   
680  O O   . ALA A 79  ? 0.2670 0.3869 0.2750 -0.0044 -0.0149 0.0130  79  ALA A O   
681  C CB  . ALA A 79  ? 0.2049 0.3202 0.2042 0.0002  -0.0231 0.0130  79  ALA A CB  
682  N N   . ILE A 80  ? 0.1419 0.2525 0.1562 -0.0051 -0.0194 0.0136  80  ILE A N   
683  C CA  . ILE A 80  ? 0.1201 0.2375 0.1418 -0.0058 -0.0185 0.0099  80  ILE A CA  
684  C C   . ILE A 80  ? 0.1824 0.3057 0.2078 -0.0120 -0.0141 0.0106  80  ILE A C   
685  O O   . ILE A 80  ? 0.1826 0.3198 0.2138 -0.0126 -0.0120 0.0069  80  ILE A O   
686  C CB  . ILE A 80  ? 0.1612 0.2741 0.1867 -0.0044 -0.0218 0.0081  80  ILE A CB  
687  C CG1 . ILE A 80  ? 0.2673 0.3735 0.2884 0.0001  -0.0239 0.0066  80  ILE A CG1 
688  C CG2 . ILE A 80  ? 0.1537 0.2777 0.1866 -0.0040 -0.0220 0.0037  80  ILE A CG2 
689  C CD1 . ILE A 80  ? 0.3130 0.4203 0.3301 0.0048  -0.0224 0.0031  80  ILE A CD1 
690  N N   . ARG A 81  ? 0.1648 0.2775 0.1859 -0.0168 -0.0116 0.0147  81  ARG A N   
691  C CA  . ARG A 81  ? 0.1726 0.2867 0.1958 -0.0258 -0.0051 0.0143  81  ARG A CA  
692  C C   . ARG A 81  ? 0.1935 0.3135 0.2131 -0.0281 0.0011  0.0157  81  ARG A C   
693  O O   . ARG A 81  ? 0.2319 0.3646 0.2589 -0.0354 0.0063  0.0118  81  ARG A O   
694  C CB  . ARG A 81  ? 0.2726 0.3663 0.2867 -0.0297 -0.0021 0.0188  81  ARG A CB  
695  C CG  . ARG A 81  ? 0.3120 0.4007 0.3244 -0.0421 0.0075  0.0179  81  ARG A CG  
696  C CD  . ARG A 81  ? 0.4394 0.4998 0.4362 -0.0444 0.0124  0.0234  81  ARG A CD  
697  N NE  . ARG A 81  ? 0.5345 0.5891 0.5350 -0.0447 0.0081  0.0205  81  ARG A NE  
698  C CZ  . ARG A 81  ? 0.5333 0.5934 0.5430 -0.0554 0.0099  0.0131  81  ARG A CZ  
699  N NH1 . ARG A 81  ? 0.4532 0.5281 0.4714 -0.0675 0.0162  0.0069  81  ARG A NH1 
700  N NH2 . ARG A 81  ? 0.5309 0.5843 0.5416 -0.0542 0.0056  0.0107  81  ARG A NH2 
701  N N   . LYS A 82  ? 0.1735 0.2869 0.1820 -0.0223 0.0007  0.0204  82  LYS A N   
702  C CA  . LYS A 82  ? 0.2177 0.3334 0.2192 -0.0237 0.0071  0.0227  82  LYS A CA  
703  C C   . LYS A 82  ? 0.1573 0.2938 0.1693 -0.0243 0.0086  0.0169  82  LYS A C   
704  O O   . LYS A 82  ? 0.1650 0.3114 0.1842 -0.0187 0.0031  0.0123  82  LYS A O   
705  C CB  . LYS A 82  ? 0.2517 0.3620 0.2403 -0.0151 0.0040  0.0265  82  LYS A CB  
706  C CG  . LYS A 82  ? 0.3872 0.4815 0.3625 -0.0106 0.0028  0.0326  82  LYS A CG  
707  C CD  . LYS A 82  ? 0.2899 0.3892 0.2568 -0.0017 -0.0023 0.0328  82  LYS A CD  
708  C CE  . LYS A 82  ? 0.4435 0.5330 0.3968 0.0063  -0.0048 0.0380  82  LYS A CE  
709  N NZ  . LYS A 82  ? 0.4547 0.5543 0.3996 0.0139  -0.0091 0.0368  82  LYS A NZ  
710  N N   . ASP A 83  ? 0.1874 0.3289 0.1974 -0.0298 0.0171  0.0175  83  ASP A N   
711  C CA  . ASP A 83  ? 0.1769 0.3383 0.1931 -0.0270 0.0188  0.0131  83  ASP A CA  
712  C C   . ASP A 83  ? 0.1780 0.3355 0.1850 -0.0163 0.0136  0.0141  83  ASP A C   
713  O O   . ASP A 83  ? 0.1818 0.3251 0.1758 -0.0137 0.0123  0.0190  83  ASP A O   
714  C CB  . ASP A 83  ? 0.2547 0.4200 0.2677 -0.0350 0.0302  0.0144  83  ASP A CB  
715  C CG  . ASP A 83  ? 0.3411 0.5324 0.3638 -0.0329 0.0330  0.0085  83  ASP A CG  
716  O OD1 . ASP A 83  ? 0.2520 0.4457 0.2692 -0.0223 0.0296  0.0084  83  ASP A OD1 
717  O OD2 . ASP A 83  ? 0.3413 0.5517 0.3767 -0.0420 0.0394  0.0032  83  ASP A OD2 
718  N N   . PRO A 84  ? 0.1523 0.3214 0.1639 -0.0093 0.0106  0.0090  84  PRO A N   
719  C CA  . PRO A 84  ? 0.1768 0.3382 0.1775 -0.0014 0.0071  0.0086  84  PRO A CA  
720  C C   . PRO A 84  ? 0.1652 0.3237 0.1536 -0.0007 0.0111  0.0114  84  PRO A C   
721  O O   . PRO A 84  ? 0.2106 0.3605 0.1884 0.0029  0.0076  0.0113  84  PRO A O   
722  C CB  . PRO A 84  ? 0.1846 0.3558 0.1891 0.0064  0.0063  0.0028  84  PRO A CB  
723  C CG  . PRO A 84  ? 0.1733 0.3559 0.1918 0.0044  0.0048  0.0003  84  PRO A CG  
724  C CD  . PRO A 84  ? 0.1883 0.3760 0.2132 -0.0073 0.0099  0.0028  84  PRO A CD  
725  N N   . ASP A 85  ? 0.1729 0.3395 0.1621 -0.0048 0.0190  0.0130  85  ASP A N   
726  C CA  . ASP A 85  ? 0.2483 0.4098 0.2230 -0.0036 0.0236  0.0167  85  ASP A CA  
727  C C   . ASP A 85  ? 0.2533 0.3982 0.2147 -0.0031 0.0209  0.0225  85  ASP A C   
728  O O   . ASP A 85  ? 0.2699 0.4102 0.2163 0.0013  0.0215  0.0246  85  ASP A O   
729  C CB  . ASP A 85  ? 0.2424 0.4126 0.2191 -0.0101 0.0345  0.0182  85  ASP A CB  
730  C CG  . ASP A 85  ? 0.3042 0.4969 0.2918 -0.0075 0.0378  0.0119  85  ASP A CG  
731  O OD1 . ASP A 85  ? 0.3632 0.5583 0.3490 0.0021  0.0327  0.0080  85  ASP A OD1 
732  O OD2 . ASP A 85  ? 0.3635 0.5711 0.3600 -0.0148 0.0464  0.0105  85  ASP A OD2 
733  N N   . ASP A 86  ? 0.1919 0.3286 0.1572 -0.0062 0.0180  0.0248  86  ASP A N   
734  C CA  . ASP A 86  ? 0.2375 0.3599 0.1894 -0.0030 0.0154  0.0304  86  ASP A CA  
735  C C   . ASP A 86  ? 0.2373 0.3605 0.1912 0.0020  0.0051  0.0273  86  ASP A C   
736  O O   . ASP A 86  ? 0.2240 0.3406 0.1686 0.0066  0.0017  0.0307  86  ASP A O   
737  C CB  . ASP A 86  ? 0.2431 0.3529 0.1942 -0.0091 0.0209  0.0354  86  ASP A CB  
738  C CG  . ASP A 86  ? 0.3509 0.4573 0.2969 -0.0166 0.0336  0.0382  86  ASP A CG  
739  O OD1 . ASP A 86  ? 0.4978 0.6053 0.4326 -0.0131 0.0378  0.0400  86  ASP A OD1 
740  O OD2 . ASP A 86  ? 0.4045 0.5079 0.3576 -0.0268 0.0400  0.0376  86  ASP A OD2 
741  N N   . LEU A 87  ? 0.1774 0.3083 0.1413 0.0020  0.0011  0.0206  87  LEU A N   
742  C CA  . LEU A 87  ? 0.1697 0.3003 0.1354 0.0039  -0.0065 0.0167  87  LEU A CA  
743  C C   . LEU A 87  ? 0.1780 0.3121 0.1319 0.0079  -0.0098 0.0141  87  LEU A C   
744  O O   . LEU A 87  ? 0.1926 0.3296 0.1398 0.0091  -0.0074 0.0116  87  LEU A O   
745  C CB  . LEU A 87  ? 0.1611 0.2935 0.1356 0.0030  -0.0075 0.0104  87  LEU A CB  
746  C CG  . LEU A 87  ? 0.1797 0.3115 0.1662 0.0007  -0.0075 0.0110  87  LEU A CG  
747  C CD1 . LEU A 87  ? 0.1992 0.3322 0.1894 0.0036  -0.0074 0.0055  87  LEU A CD1 
748  C CD2 . LEU A 87  ? 0.2167 0.3426 0.2054 -0.0002 -0.0122 0.0126  87  LEU A CD2 
749  N N   . GLU A 88  ? 0.1783 0.3145 0.1301 0.0104  -0.0155 0.0139  88  GLU A N   
750  C CA  . GLU A 88  ? 0.1847 0.3308 0.1284 0.0135  -0.0204 0.0085  88  GLU A CA  
751  C C   . GLU A 88  ? 0.1986 0.3474 0.1475 0.0076  -0.0215 -0.0018 88  GLU A C   
752  O O   . GLU A 88  ? 0.1765 0.3188 0.1347 0.0036  -0.0202 -0.0034 88  GLU A O   
753  C CB  . GLU A 88  ? 0.2425 0.3952 0.1845 0.0187  -0.0264 0.0098  88  GLU A CB  
754  C CG  . GLU A 88  ? 0.2752 0.4176 0.2072 0.0258  -0.0236 0.0206  88  GLU A CG  
755  C CD  . GLU A 88  ? 0.3760 0.5200 0.3081 0.0320  -0.0283 0.0231  88  GLU A CD  
756  O OE1 . GLU A 88  ? 0.4622 0.5920 0.3830 0.0384  -0.0248 0.0323  88  GLU A OE1 
757  O OE2 . GLU A 88  ? 0.3248 0.4829 0.2669 0.0305  -0.0342 0.0157  88  GLU A OE2 
758  N N   . LYS A 89  ? 0.2064 0.3631 0.1469 0.0073  -0.0233 -0.0090 89  LYS A N   
759  C CA  . LYS A 89  ? 0.2178 0.3733 0.1595 -0.0001 -0.0228 -0.0201 89  LYS A CA  
760  C C   . LYS A 89  ? 0.2314 0.3892 0.1837 -0.0053 -0.0254 -0.0240 89  LYS A C   
761  O O   . LYS A 89  ? 0.2431 0.3887 0.1984 -0.0110 -0.0216 -0.0279 89  LYS A O   
762  C CB  . LYS A 89  ? 0.2218 0.3885 0.1528 -0.0013 -0.0252 -0.0290 89  LYS A CB  
763  C CG  . LYS A 89  ? 0.2865 0.4492 0.2050 0.0036  -0.0216 -0.0262 89  LYS A CG  
764  C CD  . LYS A 89  ? 0.3322 0.5083 0.2387 0.0038  -0.0253 -0.0350 89  LYS A CD  
765  C CE  . LYS A 89  ? 0.3472 0.5184 0.2395 0.0098  -0.0213 -0.0314 89  LYS A CE  
766  N NZ  . LYS A 89  ? 0.4056 0.5893 0.2844 0.0102  -0.0249 -0.0412 89  LYS A NZ  
767  N N   . GLU A 90  ? 0.1942 0.3667 0.1503 -0.0020 -0.0313 -0.0227 90  GLU A N   
768  C CA  . GLU A 90  ? 0.2412 0.4191 0.2081 -0.0060 -0.0336 -0.0261 90  GLU A CA  
769  C C   . GLU A 90  ? 0.2347 0.3955 0.2091 -0.0065 -0.0302 -0.0194 90  GLU A C   
770  O O   . GLU A 90  ? 0.2060 0.3625 0.1868 -0.0123 -0.0287 -0.0238 90  GLU A O   
771  C CB  . GLU A 90  ? 0.2741 0.4716 0.2419 0.0021  -0.0404 -0.0240 90  GLU A CB  
772  C CG  . GLU A 90  ? 0.5834 0.8055 0.5457 0.0035  -0.0457 -0.0333 90  GLU A CG  
773  C CD  . GLU A 90  ? 0.8145 1.0543 0.7759 0.0162  -0.0519 -0.0297 90  GLU A CD  
774  O OE1 . GLU A 90  ? 0.8489 1.1033 0.8065 0.0210  -0.0541 -0.0349 90  GLU A OE1 
775  O OE2 . GLU A 90  ? 0.8708 1.1041 0.8352 0.0222  -0.0523 -0.0213 90  GLU A OE2 
776  N N   . GLU A 91  ? 0.1649 0.3164 0.1379 -0.0009 -0.0284 -0.0095 91  GLU A N   
777  C CA  . GLU A 91  ? 0.1673 0.3066 0.1477 -0.0014 -0.0260 -0.0046 91  GLU A CA  
778  C C   . GLU A 91  ? 0.1996 0.3275 0.1797 -0.0046 -0.0213 -0.0083 91  GLU A C   
779  O O   . GLU A 91  ? 0.1886 0.3081 0.1735 -0.0057 -0.0201 -0.0084 91  GLU A O   
780  C CB  . GLU A 91  ? 0.2133 0.3482 0.1922 0.0030  -0.0245 0.0049  91  GLU A CB  
781  C CG  . GLU A 91  ? 0.2286 0.3665 0.2035 0.0087  -0.0275 0.0105  91  GLU A CG  
782  C CD  . GLU A 91  ? 0.2680 0.3950 0.2370 0.0111  -0.0230 0.0195  91  GLU A CD  
783  O OE1 . GLU A 91  ? 0.2008 0.3261 0.1637 0.0105  -0.0186 0.0213  91  GLU A OE1 
784  O OE2 . GLU A 91  ? 0.2775 0.3963 0.2467 0.0128  -0.0228 0.0242  91  GLU A OE2 
785  N N   . VAL A 92  ? 0.1628 0.2889 0.1349 -0.0042 -0.0182 -0.0107 92  VAL A N   
786  C CA  . VAL A 92  ? 0.2095 0.3228 0.1769 -0.0043 -0.0132 -0.0145 92  VAL A CA  
787  C C   . VAL A 92  ? 0.2152 0.3193 0.1791 -0.0106 -0.0114 -0.0224 92  VAL A C   
788  O O   . VAL A 92  ? 0.2069 0.2962 0.1686 -0.0098 -0.0077 -0.0231 92  VAL A O   
789  C CB  . VAL A 92  ? 0.1893 0.3019 0.1464 -0.0018 -0.0098 -0.0162 92  VAL A CB  
790  C CG1 . VAL A 92  ? 0.2469 0.3436 0.1954 0.0010  -0.0040 -0.0199 92  VAL A CG1 
791  C CG2 . VAL A 92  ? 0.2150 0.3363 0.1756 0.0027  -0.0095 -0.0086 92  VAL A CG2 
792  N N   . GLU A 93  ? 0.2244 0.3378 0.1867 -0.0169 -0.0134 -0.0292 93  GLU A N   
793  C CA  . GLU A 93  ? 0.2080 0.3152 0.1681 -0.0264 -0.0101 -0.0386 93  GLU A CA  
794  C C   . GLU A 93  ? 0.2227 0.3267 0.1918 -0.0272 -0.0104 -0.0359 93  GLU A C   
795  O O   . GLU A 93  ? 0.2274 0.3132 0.1908 -0.0315 -0.0041 -0.0397 93  GLU A O   
796  C CB  . GLU A 93  ? 0.2192 0.3467 0.1804 -0.0334 -0.0137 -0.0475 93  GLU A CB  
797  C CG  . GLU A 93  ? 0.3164 0.4436 0.2653 -0.0351 -0.0120 -0.0535 93  GLU A CG  
798  C CD  . GLU A 93  ? 0.4974 0.6524 0.4483 -0.0376 -0.0185 -0.0605 93  GLU A CD  
799  O OE1 . GLU A 93  ? 0.6181 0.7762 0.5592 -0.0357 -0.0191 -0.0630 93  GLU A OE1 
800  O OE2 . GLU A 93  ? 0.5348 0.7101 0.4963 -0.0402 -0.0234 -0.0639 93  GLU A OE2 
801  N N   . LYS A 94  ? 0.1883 0.3069 0.1685 -0.0226 -0.0168 -0.0294 94  LYS A N   
802  C CA  . LYS A 94  ? 0.2117 0.3277 0.1999 -0.0228 -0.0172 -0.0270 94  LYS A CA  
803  C C   . LYS A 94  ? 0.2055 0.3025 0.1913 -0.0176 -0.0140 -0.0215 94  LYS A C   
804  O O   . LYS A 94  ? 0.2213 0.3069 0.2065 -0.0193 -0.0109 -0.0227 94  LYS A O   
805  C CB  . LYS A 94  ? 0.2808 0.4139 0.2779 -0.0176 -0.0241 -0.0215 94  LYS A CB  
806  C CG  . LYS A 94  ? 0.4343 0.5903 0.4340 -0.0204 -0.0280 -0.0283 94  LYS A CG  
807  C CD  . LYS A 94  ? 0.5537 0.7244 0.5586 -0.0119 -0.0342 -0.0226 94  LYS A CD  
808  C CE  . LYS A 94  ? 0.6292 0.8283 0.6359 -0.0116 -0.0391 -0.0305 94  LYS A CE  
809  N NZ  . LYS A 94  ? 0.6751 0.8828 0.6857 -0.0251 -0.0356 -0.0443 94  LYS A NZ  
810  N N   . LEU A 95  ? 0.1551 0.2504 0.1391 -0.0111 -0.0144 -0.0163 95  LEU A N   
811  C CA  . LEU A 95  ? 0.1649 0.2483 0.1468 -0.0050 -0.0120 -0.0131 95  LEU A CA  
812  C C   . LEU A 95  ? 0.1945 0.2573 0.1621 -0.0047 -0.0050 -0.0182 95  LEU A C   
813  O O   . LEU A 95  ? 0.1964 0.2460 0.1599 -0.0007 -0.0026 -0.0172 95  LEU A O   
814  C CB  . LEU A 95  ? 0.2047 0.2959 0.1884 0.0006  -0.0129 -0.0088 95  LEU A CB  
815  C CG  . LEU A 95  ? 0.3003 0.3887 0.2844 0.0082  -0.0118 -0.0069 95  LEU A CG  
816  C CD1 . LEU A 95  ? 0.3210 0.4101 0.3134 0.0087  -0.0149 -0.0044 95  LEU A CD1 
817  C CD2 . LEU A 95  ? 0.3593 0.4612 0.3474 0.0111  -0.0117 -0.0046 95  LEU A CD2 
818  N N   . ILE A 96  ? 0.2206 0.2779 0.1778 -0.0083 -0.0010 -0.0236 96  ILE A N   
819  C CA  . ILE A 96  ? 0.2264 0.2574 0.1650 -0.0085 0.0079  -0.0287 96  ILE A CA  
820  C C   . ILE A 96  ? 0.2100 0.2294 0.1461 -0.0179 0.0124  -0.0335 96  ILE A C   
821  O O   . ILE A 96  ? 0.2474 0.2419 0.1698 -0.0148 0.0195  -0.0335 96  ILE A O   
822  C CB  . ILE A 96  ? 0.2837 0.3102 0.2104 -0.0117 0.0117  -0.0345 96  ILE A CB  
823  C CG1 . ILE A 96  ? 0.2964 0.3289 0.2215 -0.0002 0.0101  -0.0296 96  ILE A CG1 
824  C CG2 . ILE A 96  ? 0.2865 0.2813 0.1911 -0.0163 0.0228  -0.0417 96  ILE A CG2 
825  C CD1 . ILE A 96  ? 0.3504 0.3847 0.2670 -0.0029 0.0120  -0.0342 96  ILE A CD1 
826  N N   . GLU A 97  ? 0.2112 0.2491 0.1592 -0.0285 0.0089  -0.0377 97  GLU A N   
827  C CA  . GLU A 97  ? 0.2348 0.2671 0.1832 -0.0389 0.0138  -0.0435 97  GLU A CA  
828  C C   . GLU A 97  ? 0.2382 0.2643 0.1909 -0.0324 0.0129  -0.0368 97  GLU A C   
829  O O   . GLU A 97  ? 0.2672 0.2718 0.2095 -0.0356 0.0212  -0.0391 97  GLU A O   
830  C CB  . GLU A 97  ? 0.2962 0.3585 0.2595 -0.0487 0.0084  -0.0496 97  GLU A CB  
831  C CG  . GLU A 97  ? 0.3871 0.4530 0.3551 -0.0609 0.0132  -0.0574 97  GLU A CG  
832  C CD  . GLU A 97  ? 0.5915 0.6954 0.5762 -0.0665 0.0057  -0.0634 97  GLU A CD  
833  O OE1 . GLU A 97  ? 0.6635 0.7803 0.6572 -0.0744 0.0075  -0.0692 97  GLU A OE1 
834  O OE2 . GLU A 97  ? 0.6475 0.7695 0.6352 -0.0618 -0.0017 -0.0625 97  GLU A OE2 
835  N N   . PHE A 98  ? 0.1948 0.2371 0.1605 -0.0237 0.0040  -0.0288 98  PHE A N   
836  C CA  . PHE A 98  ? 0.2185 0.2555 0.1875 -0.0172 0.0025  -0.0232 98  PHE A CA  
837  C C   . PHE A 98  ? 0.2140 0.2259 0.1663 -0.0078 0.0081  -0.0210 98  PHE A C   
838  O O   . PHE A 98  ? 0.2274 0.2239 0.1728 -0.0051 0.0119  -0.0200 98  PHE A O   
839  C CB  . PHE A 98  ? 0.1757 0.2325 0.1592 -0.0111 -0.0069 -0.0164 98  PHE A CB  
840  C CG  . PHE A 98  ? 0.1775 0.2327 0.1663 -0.0066 -0.0095 -0.0120 98  PHE A CG  
841  C CD1 . PHE A 98  ? 0.1962 0.2575 0.1922 -0.0109 -0.0104 -0.0129 98  PHE A CD1 
842  C CD2 . PHE A 98  ? 0.2027 0.2531 0.1895 0.0025  -0.0112 -0.0081 98  PHE A CD2 
843  C CE1 . PHE A 98  ? 0.2207 0.2789 0.2200 -0.0063 -0.0125 -0.0091 98  PHE A CE1 
844  C CE2 . PHE A 98  ? 0.1723 0.2220 0.1633 0.0063  -0.0139 -0.0052 98  PHE A CE2 
845  C CZ  . PHE A 98  ? 0.1978 0.2491 0.1940 0.0018  -0.0143 -0.0054 98  PHE A CZ  
846  N N   . THR A 99  ? 0.1953 0.2033 0.1395 -0.0007 0.0087  -0.0202 99  THR A N   
847  C CA  . THR A 99  ? 0.2297 0.2156 0.1555 0.0117  0.0138  -0.0184 99  THR A CA  
848  C C   . THR A 99  ? 0.2446 0.1968 0.1473 0.0077  0.0261  -0.0229 99  THR A C   
849  O O   . THR A 99  ? 0.2695 0.1997 0.1571 0.0158  0.0312  -0.0208 99  THR A O   
850  C CB  . THR A 99  ? 0.2865 0.2784 0.2086 0.0205  0.0125  -0.0175 99  THR A CB  
851  O OG1 . THR A 99  ? 0.2126 0.2343 0.1556 0.0207  0.0033  -0.0140 99  THR A OG1 
852  C CG2 . THR A 99  ? 0.2480 0.2239 0.1527 0.0376  0.0158  -0.0153 99  THR A CG2 
853  N N   . LYS A 100 ? 0.2705 0.2172 0.1684 -0.0055 0.0318  -0.0299 100 LYS A N   
854  C CA  . LYS A 100 ? 0.3596 0.2715 0.2342 -0.0133 0.0459  -0.0359 100 LYS A CA  
855  C C   . LYS A 100 ? 0.3046 0.2103 0.1816 -0.0206 0.0500  -0.0366 100 LYS A C   
856  O O   . LYS A 100 ? 0.3668 0.2370 0.2199 -0.0201 0.0624  -0.0375 100 LYS A O   
857  C CB  . LYS A 100 ? 0.3306 0.2441 0.2035 -0.0297 0.0505  -0.0456 100 LYS A CB  
858  C CG  . LYS A 100 ? 0.5125 0.4048 0.3637 -0.0238 0.0564  -0.0475 100 LYS A CG  
859  C CD  . LYS A 100 ? 0.5619 0.4704 0.4196 -0.0374 0.0550  -0.0560 100 LYS A CD  
860  C CE  . LYS A 100 ? 0.6789 0.5663 0.5143 -0.0297 0.0605  -0.0574 100 LYS A CE  
861  N NZ  . LYS A 100 ? 0.7207 0.6219 0.5597 -0.0432 0.0596  -0.0668 100 LYS A NZ  
862  N N   . LEU A 101 ? 0.2777 0.2152 0.1807 -0.0265 0.0408  -0.0359 101 LEU A N   
863  C CA  . LEU A 101 ? 0.2904 0.2263 0.1978 -0.0327 0.0441  -0.0366 101 LEU A CA  
864  C C   . LEU A 101 ? 0.2685 0.1844 0.1636 -0.0176 0.0454  -0.0290 101 LEU A C   
865  O O   . LEU A 101 ? 0.3172 0.2133 0.2015 -0.0209 0.0542  -0.0299 101 LEU A O   
866  C CB  . LEU A 101 ? 0.2634 0.2385 0.1996 -0.0375 0.0327  -0.0364 101 LEU A CB  
867  C CG  . LEU A 101 ? 0.3268 0.3083 0.2719 -0.0432 0.0344  -0.0374 101 LEU A CG  
868  C CD1 . LEU A 101 ? 0.3201 0.2926 0.2588 -0.0610 0.0472  -0.0480 101 LEU A CD1 
869  C CD2 . LEU A 101 ? 0.3440 0.3625 0.3141 -0.0420 0.0220  -0.0354 101 LEU A CD2 
870  N N   . ASN A 102 ? 0.2592 0.1809 0.1548 -0.0012 0.0372  -0.0224 102 ASN A N   
871  C CA  . ASN A 102 ? 0.2604 0.1755 0.1500 0.0145  0.0342  -0.0161 102 ASN A CA  
872  C C   . ASN A 102 ? 0.2879 0.1768 0.1504 0.0319  0.0394  -0.0135 102 ASN A C   
873  O O   . ASN A 102 ? 0.2984 0.1792 0.1508 0.0469  0.0382  -0.0093 102 ASN A O   
874  C CB  . ASN A 102 ? 0.2450 0.1946 0.1596 0.0194  0.0197  -0.0121 102 ASN A CB  
875  C CG  . ASN A 102 ? 0.2562 0.2260 0.1918 0.0084  0.0149  -0.0127 102 ASN A CG  
876  O OD1 . ASN A 102 ? 0.3031 0.2643 0.2362 0.0056  0.0188  -0.0130 102 ASN A OD1 
877  N ND2 . ASN A 102 ? 0.2651 0.2609 0.2194 0.0035  0.0070  -0.0127 102 ASN A ND2 
878  N N   . TYR A 103 ? 0.2683 0.1505 0.2820 -0.0620 0.0361  -0.0446 103 TYR A N   
879  C CA  . TYR A 103 ? 0.3990 0.2513 0.3986 -0.0476 0.0436  -0.0469 103 TYR A CA  
880  C C   . TYR A 103 ? 0.3321 0.1519 0.3260 -0.0401 0.0524  -0.0379 103 TYR A C   
881  O O   . TYR A 103 ? 0.3282 0.1352 0.3149 -0.0206 0.0569  -0.0326 103 TYR A O   
882  C CB  . TYR A 103 ? 0.4388 0.2725 0.4245 -0.0574 0.0466  -0.0640 103 TYR A CB  
883  C CG  . TYR A 103 ? 0.5228 0.3192 0.4904 -0.0439 0.0563  -0.0694 103 TYR A CG  
884  C CD1 . TYR A 103 ? 0.5830 0.3900 0.5455 -0.0280 0.0560  -0.0723 103 TYR A CD1 
885  C CD2 . TYR A 103 ? 0.6115 0.3713 0.5682 -0.0448 0.0640  -0.0684 103 TYR A CD2 
886  C CE1 . TYR A 103 ? 0.6454 0.4200 0.5909 -0.0130 0.0658  -0.0771 103 TYR A CE1 
887  C CE2 . TYR A 103 ? 0.6719 0.4027 0.6124 -0.0294 0.0716  -0.0707 103 TYR A CE2 
888  C CZ  . TYR A 103 ? 0.7276 0.4638 0.6620 -0.0131 0.0731  -0.0758 103 TYR A CZ  
889  O OH  . TYR A 103 ? 0.7537 0.4660 0.6731 0.0042  0.0805  -0.0773 103 TYR A OH  
890  N N   . GLU A 104 ? 0.2982 0.1079 0.2948 -0.0537 0.0549  -0.0347 104 GLU A N   
891  C CA  . GLU A 104 ? 0.3518 0.1377 0.3412 -0.0450 0.0616  -0.0238 104 GLU A CA  
892  C C   . GLU A 104 ? 0.3112 0.1116 0.3095 -0.0358 0.0604  -0.0089 104 GLU A C   
893  O O   . GLU A 104 ? 0.3666 0.1520 0.3582 -0.0268 0.0654  0.0012  104 GLU A O   
894  C CB  . GLU A 104 ? 0.4304 0.2044 0.4173 -0.0620 0.0637  -0.0264 104 GLU A CB  
895  C CG  . GLU A 104 ? 0.5570 0.3093 0.5318 -0.0697 0.0665  -0.0408 104 GLU A CG  
896  C CD  . GLU A 104 ? 0.6794 0.3969 0.6369 -0.0513 0.0752  -0.0401 104 GLU A CD  
897  O OE1 . GLU A 104 ? 0.6830 0.3897 0.6372 -0.0356 0.0801  -0.0269 104 GLU A OE1 
898  O OE2 . GLU A 104 ? 0.6926 0.3960 0.6393 -0.0515 0.0769  -0.0526 104 GLU A OE2 
899  N N   . LYS A 105 ? 0.2585 0.0924 0.2704 -0.0371 0.0526  -0.0072 105 LYS A N   
900  C CA  . LYS A 105 ? 0.2365 0.0881 0.2553 -0.0277 0.0498  0.0054  105 LYS A CA  
901  C C   . LYS A 105 ? 0.2345 0.0871 0.2479 -0.0056 0.0496  0.0110  105 LYS A C   
902  O O   . LYS A 105 ? 0.2325 0.0903 0.2442 0.0013  0.0476  0.0048  105 LYS A O   
903  C CB  . LYS A 105 ? 0.2008 0.0902 0.2340 -0.0346 0.0403  0.0047  105 LYS A CB  
904  C CG  . LYS A 105 ? 0.2008 0.0987 0.2417 -0.0547 0.0398  0.0010  105 LYS A CG  
905  C CD  . LYS A 105 ? 0.2117 0.1466 0.2649 -0.0578 0.0309  0.0005  105 LYS A CD  
906  C CE  . LYS A 105 ? 0.1864 0.1372 0.2484 -0.0762 0.0297  -0.0034 105 LYS A CE  
907  N NZ  . LYS A 105 ? 0.2002 0.1857 0.2718 -0.0747 0.0217  -0.0026 105 LYS A NZ  
908  N N   . PRO A 106 ? 0.2365 0.0876 0.2472 0.0063  0.0517  0.0226  106 PRO A N   
909  C CA  . PRO A 106 ? 0.2523 0.1098 0.2585 0.0276  0.0508  0.0275  106 PRO A CA  
910  C C   . PRO A 106 ? 0.2131 0.1071 0.2303 0.0306  0.0411  0.0236  106 PRO A C   
911  O O   . PRO A 106 ? 0.2355 0.1385 0.2513 0.0448  0.0403  0.0237  106 PRO A O   
912  C CB  . PRO A 106 ? 0.2874 0.1420 0.2886 0.0372  0.0536  0.0407  106 PRO A CB  
913  C CG  . PRO A 106 ? 0.2875 0.1172 0.2846 0.0232  0.0610  0.0429  106 PRO A CG  
914  C CD  . PRO A 106 ? 0.2469 0.0871 0.2557 0.0020  0.0569  0.0320  106 PRO A CD  
915  N N   . ILE A 107 ? 0.1784 0.0940 0.2065 0.0182  0.0344  0.0208  107 ILE A N   
916  C CA  . ILE A 107 ? 0.1854 0.1296 0.2224 0.0194  0.0270  0.0173  107 ILE A CA  
917  C C   . ILE A 107 ? 0.1945 0.1397 0.2313 0.0182  0.0274  0.0090  107 ILE A C   
918  O O   . ILE A 107 ? 0.1833 0.1503 0.2260 0.0216  0.0235  0.0073  107 ILE A O   
919  C CB  . ILE A 107 ? 0.1705 0.1328 0.2167 0.0084  0.0214  0.0172  107 ILE A CB  
920  C CG1 . ILE A 107 ? 0.1605 0.1178 0.2093 -0.0060 0.0222  0.0130  107 ILE A CG1 
921  C CG2 . ILE A 107 ? 0.1874 0.1520 0.2324 0.0118  0.0210  0.0246  107 ILE A CG2 
922  C CD1 . ILE A 107 ? 0.1404 0.1183 0.1980 -0.0131 0.0170  0.0132  107 ILE A CD1 
923  N N   . TYR A 108 ? 0.2100 0.1317 0.2391 0.0129  0.0327  0.0034  108 TYR A N   
924  C CA  . TYR A 108 ? 0.2119 0.1318 0.2370 0.0133  0.0341  -0.0057 108 TYR A CA  
925  C C   . TYR A 108 ? 0.2713 0.1718 0.2851 0.0297  0.0413  -0.0058 108 TYR A C   
926  O O   . TYR A 108 ? 0.2774 0.1688 0.2840 0.0313  0.0448  -0.0143 108 TYR A O   
927  C CB  . TYR A 108 ? 0.1957 0.1037 0.2174 -0.0033 0.0349  -0.0149 108 TYR A CB  
928  C CG  . TYR A 108 ? 0.2054 0.1423 0.2372 -0.0140 0.0273  -0.0170 108 TYR A CG  
929  C CD1 . TYR A 108 ? 0.1801 0.1320 0.2216 -0.0196 0.0230  -0.0104 108 TYR A CD1 
930  C CD2 . TYR A 108 ? 0.2258 0.1745 0.2557 -0.0161 0.0254  -0.0246 108 TYR A CD2 
931  C CE1 . TYR A 108 ? 0.1324 0.1085 0.1815 -0.0261 0.0172  -0.0106 108 TYR A CE1 
932  C CE2 . TYR A 108 ? 0.2076 0.1821 0.2449 -0.0232 0.0194  -0.0240 108 TYR A CE2 
933  C CZ  . TYR A 108 ? 0.1656 0.1524 0.2124 -0.0278 0.0155  -0.0167 108 TYR A CZ  
934  O OH  . TYR A 108 ? 0.1730 0.1823 0.2252 -0.0320 0.0109  -0.0150 108 TYR A OH  
935  N N   . ARG A 109 ? 0.2692 0.1641 0.2801 0.0439  0.0440  0.0037  109 ARG A N   
936  C CA  . ARG A 109 ? 0.2820 0.1558 0.2804 0.0629  0.0523  0.0059  109 ARG A CA  
937  C C   . ARG A 109 ? 0.3697 0.2722 0.3732 0.0767  0.0501  0.0047  109 ARG A C   
938  O O   . ARG A 109 ? 0.3529 0.2782 0.3615 0.0911  0.0478  0.0125  109 ARG A O   
939  C CB  . ARG A 109 ? 0.2795 0.1414 0.2721 0.0756  0.0560  0.0186  109 ARG A CB  
940  C CG  . ARG A 109 ? 0.5190 0.3473 0.4942 0.0903  0.0662  0.0210  109 ARG A CG  
941  C CD  . ARG A 109 ? 0.6942 0.5239 0.6631 0.1024  0.0671  0.0342  109 ARG A CD  
942  N NE  . ARG A 109 ? 0.7773 0.6007 0.7469 0.0917  0.0666  0.0407  109 ARG A NE  
943  C CZ  . ARG A 109 ? 0.7993 0.5959 0.7652 0.0742  0.0711  0.0378  109 ARG A CZ  
944  N NH1 . ARG A 109 ? 0.8863 0.6581 0.8468 0.0636  0.0756  0.0273  109 ARG A NH1 
945  N NH2 . ARG A 109 ? 0.7412 0.5392 0.7089 0.0666  0.0707  0.0449  109 ARG A NH2 
946  N N   . PHE A 110 ? 0.2852 0.1895 0.2874 0.0718  0.0510  -0.0055 110 PHE A N   
947  C CA  . PHE A 110 ? 0.2377 0.1672 0.2436 0.0845  0.0513  -0.0073 110 PHE A CA  
948  C C   . PHE A 110 ? 0.3138 0.2138 0.3031 0.0927  0.0609  -0.0159 110 PHE A C   
949  O O   . PHE A 110 ? 0.3729 0.2513 0.3540 0.0782  0.0623  -0.0262 110 PHE A O   
950  C CB  . PHE A 110 ? 0.2578 0.2212 0.2768 0.0711  0.0440  -0.0113 110 PHE A CB  
951  C CG  . PHE A 110 ? 0.2862 0.2759 0.3198 0.0626  0.0356  -0.0048 110 PHE A CG  
952  C CD1 . PHE A 110 ? 0.2796 0.3015 0.3241 0.0712  0.0324  0.0009  110 PHE A CD1 
953  C CD2 . PHE A 110 ? 0.2561 0.2403 0.2927 0.0456  0.0311  -0.0053 110 PHE A CD2 
954  C CE1 . PHE A 110 ? 0.2306 0.2733 0.2865 0.0614  0.0250  0.0046  110 PHE A CE1 
955  C CE2 . PHE A 110 ? 0.2186 0.2231 0.2663 0.0388  0.0246  -0.0003 110 PHE A CE2 
956  C CZ  . PHE A 110 ? 0.2295 0.2607 0.2859 0.0461  0.0216  0.0039  110 PHE A CZ  
957  N N   . GLU A 111 ? 0.3193 0.2193 0.3028 0.1164  0.0675  -0.0124 111 GLU A N   
958  C CA  . GLU A 111 ? 0.3761 0.2476 0.3423 0.1246  0.0765  -0.0209 111 GLU A CA  
959  C C   . GLU A 111 ? 0.3711 0.2526 0.3360 0.1157  0.0765  -0.0339 111 GLU A C   
960  O O   . GLU A 111 ? 0.3691 0.2176 0.3170 0.1111  0.0826  -0.0461 111 GLU A O   
961  C CB  . GLU A 111 ? 0.4960 0.3826 0.4613 0.1455  0.0784  -0.0130 111 GLU A CB  
962  C CG  . GLU A 111 ? 0.6994 0.5640 0.6490 0.1543  0.0865  -0.0211 111 GLU A CG  
963  C CD  . GLU A 111 ? 0.9472 0.8243 0.8947 0.1761  0.0895  -0.0115 111 GLU A CD  
964  O OE1 . GLU A 111 ? 1.0719 0.9139 1.0022 0.1852  0.0974  -0.0117 111 GLU A OE1 
965  O OE2 . GLU A 111 ? 0.9896 0.9121 0.9523 0.1833  0.0841  -0.0037 111 GLU A OE2 
966  N N   . ARG A 112 ? 0.3432 0.2710 0.3255 0.1096  0.0686  -0.0315 112 ARG A N   
967  C CA  . ARG A 112 ? 0.3365 0.2796 0.3177 0.1008  0.0678  -0.0411 112 ARG A CA  
968  C C   . ARG A 112 ? 0.3584 0.2820 0.3331 0.0779  0.0640  -0.0505 112 ARG A C   
969  O O   . ARG A 112 ? 0.3765 0.2909 0.3384 0.0735  0.0668  -0.0626 112 ARG A O   
970  C CB  . ARG A 112 ? 0.2587 0.2525 0.2602 0.0976  0.0612  -0.0343 112 ARG A CB  
971  C CG  . ARG A 112 ? 0.2497 0.2631 0.2504 0.0895  0.0609  -0.0409 112 ARG A CG  
972  C CD  . ARG A 112 ? 0.2717 0.2785 0.2575 0.1055  0.0707  -0.0491 112 ARG A CD  
973  N NE  . ARG A 112 ? 0.3218 0.3605 0.3110 0.1009  0.0706  -0.0511 112 ARG A NE  
974  C CZ  . ARG A 112 ? 0.3973 0.4349 0.3719 0.1096  0.0781  -0.0600 112 ARG A CZ  
975  N NH1 . ARG A 112 ? 0.3812 0.3844 0.3360 0.1237  0.0866  -0.0693 112 ARG A NH1 
976  N NH2 . ARG A 112 ? 0.3715 0.4409 0.3499 0.1047  0.0780  -0.0594 112 ARG A NH2 
977  N N   . ILE A 113 ? 0.2913 0.2105 0.2737 0.0637  0.0578  -0.0456 113 ILE A N   
978  C CA  . ILE A 113 ? 0.2693 0.1737 0.2470 0.0427  0.0544  -0.0538 113 ILE A CA  
979  C C   . ILE A 113 ? 0.3829 0.2432 0.3398 0.0417  0.0626  -0.0660 113 ILE A C   
980  O O   . ILE A 113 ? 0.4143 0.2683 0.3620 0.0284  0.0617  -0.0790 113 ILE A O   
981  C CB  . ILE A 113 ? 0.2674 0.1741 0.2570 0.0309  0.0482  -0.0452 113 ILE A CB  
982  C CG1 . ILE A 113 ? 0.2986 0.2452 0.3054 0.0260  0.0398  -0.0376 113 ILE A CG1 
983  C CG2 . ILE A 113 ? 0.3659 0.2511 0.3491 0.0115  0.0474  -0.0535 113 ILE A CG2 
984  C CD1 . ILE A 113 ? 0.3927 0.3431 0.4101 0.0204  0.0351  -0.0284 113 ILE A CD1 
985  N N   . ARG A 114 ? 0.3685 0.1966 0.3163 0.0558  0.0711  -0.0622 114 ARG A N   
986  C CA  . ARG A 114 ? 0.4745 0.2526 0.4001 0.0556  0.0813  -0.0737 114 ARG A CA  
987  C C   . ARG A 114 ? 0.4803 0.2561 0.3911 0.0625  0.0860  -0.0878 114 ARG A C   
988  O O   . ARG A 114 ? 0.5148 0.2728 0.4132 0.0477  0.0858  -0.1023 114 ARG A O   
989  C CB  . ARG A 114 ? 0.5375 0.2933 0.4589 0.0723  0.0869  -0.0617 114 ARG A CB  
990  C CG  . ARG A 114 ? 0.6958 0.4113 0.5994 0.0715  0.0935  -0.0680 114 ARG A CG  
991  C CD  . ARG A 114 ? 0.8795 0.5740 0.7779 0.0441  0.0916  -0.0797 114 ARG A CD  
992  N NE  . ARG A 114 ? 0.9903 0.6510 0.8823 0.0386  0.0965  -0.0744 114 ARG A NE  
993  C CZ  . ARG A 114 ? 1.0515 0.6785 0.9276 0.0461  0.1047  -0.0774 114 ARG A CZ  
994  N NH1 . ARG A 114 ? 1.0695 0.6931 0.9350 0.0599  0.1084  -0.0859 114 ARG A NH1 
995  N NH2 . ARG A 114 ? 1.0854 0.6819 0.9557 0.0401  0.1103  -0.0717 114 ARG A NH2 
996  N N   . GLU A 115 ? 0.4491 0.2515 0.3639 0.0834  0.0880  -0.0825 115 GLU A N   
997  C CA  . GLU A 115 ? 0.4674 0.2758 0.3704 0.0908  0.0918  -0.0939 115 GLU A CA  
998  C C   . GLU A 115 ? 0.4382 0.2659 0.3399 0.0708  0.0851  -0.1055 115 GLU A C   
999  O O   . GLU A 115 ? 0.5269 0.3360 0.4090 0.0662  0.0891  -0.1223 115 GLU A O   
1000 C CB  . GLU A 115 ? 0.4893 0.3356 0.4034 0.1133  0.0933  -0.0835 115 GLU A CB  
1001 C CG  . GLU A 115 ? 0.5880 0.4333 0.5100 0.1299  0.0946  -0.0684 115 GLU A CG  
1002 C CD  . GLU A 115 ? 0.6817 0.5725 0.6180 0.1473  0.0942  -0.0584 115 GLU A CD  
1003 O OE1 . GLU A 115 ? 0.6341 0.5582 0.5765 0.1455  0.0931  -0.0617 115 GLU A OE1 
1004 O OE2 . GLU A 115 ? 0.7219 0.6169 0.6629 0.1614  0.0948  -0.0466 115 GLU A OE2 
1005 N N   . LEU A 116 ? 0.3742 0.2415 0.2966 0.0587  0.0741  -0.0961 116 LEU A N   
1006 C CA  . LEU A 116 ? 0.3714 0.2645 0.2942 0.0425  0.0667  -0.1031 116 LEU A CA  
1007 C C   . LEU A 116 ? 0.4339 0.3024 0.3453 0.0213  0.0640  -0.1170 116 LEU A C   
1008 O O   . LEU A 116 ? 0.5170 0.3903 0.4152 0.0132  0.0626  -0.1309 116 LEU A O   
1009 C CB  . LEU A 116 ? 0.3752 0.3097 0.3213 0.0356  0.0571  -0.0885 116 LEU A CB  
1010 C CG  . LEU A 116 ? 0.3732 0.3399 0.3332 0.0508  0.0584  -0.0759 116 LEU A CG  
1011 C CD1 . LEU A 116 ? 0.3270 0.3243 0.3081 0.0410  0.0497  -0.0627 116 LEU A CD1 
1012 C CD2 . LEU A 116 ? 0.3684 0.3535 0.3195 0.0595  0.0633  -0.0816 116 LEU A CD2 
1013 N N   . MET A 117 ? 0.4320 0.2761 0.3476 0.0116  0.0634  -0.1139 117 MET A N   
1014 C CA  . MET A 117 ? 0.4543 0.2785 0.3616 -0.0113 0.0611  -0.1273 117 MET A CA  
1015 C C   . MET A 117 ? 0.5723 0.3545 0.4548 -0.0108 0.0696  -0.1443 117 MET A C   
1016 O O   . MET A 117 ? 0.5974 0.3730 0.4745 -0.0301 0.0646  -0.1545 117 MET A O   
1017 C CB  . MET A 117 ? 0.5369 0.3492 0.4569 -0.0224 0.0592  -0.1177 117 MET A CB  
1018 C CG  . MET A 117 ? 0.5409 0.3947 0.4845 -0.0255 0.0493  -0.1019 117 MET A CG  
1019 S SD  . MET A 117 ? 0.5767 0.4787 0.5262 -0.0369 0.0380  -0.1057 117 MET A SD  
1020 C CE  . MET A 117 ? 0.5165 0.4166 0.4692 -0.0635 0.0324  -0.1132 117 MET A CE  
1021 N N   . ASN A 118 ? 0.5903 0.3558 0.4632 0.0122  0.0781  -0.1423 118 ASN A N   
1022 C CA  . ASN A 118 ? 0.6353 0.3707 0.4894 0.0165  0.0827  -0.1538 118 ASN A CA  
1023 C C   . ASN A 118 ? 0.6791 0.4327 0.5198 0.0228  0.0828  -0.1668 118 ASN A C   
1024 O O   . ASN A 118 ? 0.7441 0.4750 0.5681 0.0274  0.0868  -0.1786 118 ASN A O   
1025 C CB  . ASN A 118 ? 0.7201 0.4288 0.5720 0.0390  0.0920  -0.1437 118 ASN A CB  
1026 C CG  . ASN A 118 ? 0.8561 0.5359 0.7128 0.0313  0.0935  -0.1341 118 ASN A CG  
1027 O OD1 . ASN A 118 ? 0.8761 0.5507 0.7361 0.0077  0.0886  -0.1376 118 ASN A OD1 
1028 N ND2 . ASN A 118 ? 0.8835 0.5487 0.7409 0.0514  0.1004  -0.1207 118 ASN A ND2 
1029 N N   . LYS A 119 ? 0.6369 0.4311 0.4839 0.0233  0.0794  -0.1649 119 LYS A N   
1030 C CA  . LYS A 119 ? 0.6461 0.4621 0.4799 0.0306  0.0802  -0.1746 119 LYS A CA  
1031 C C   . LYS A 119 ? 0.6963 0.5275 0.5224 0.0079  0.0704  -0.1874 119 LYS A C   
1032 O O   . LYS A 119 ? 0.6717 0.5179 0.5106 -0.0119 0.0618  -0.1848 119 LYS A O   
1033 C CB  . LYS A 119 ? 0.6127 0.4709 0.4596 0.0451  0.0823  -0.1618 119 LYS A CB  
1034 C CG  . LYS A 119 ? 0.6585 0.5099 0.5091 0.0720  0.0923  -0.1512 119 LYS A CG  
1035 C CD  . LYS A 119 ? 0.6823 0.5848 0.5544 0.0824  0.0896  -0.1336 119 LYS A CD  
1036 C CE  . LYS A 119 ? 0.7135 0.6161 0.5933 0.1074  0.0979  -0.1221 119 LYS A CE  
1037 N NZ  . LYS A 119 ? 0.7531 0.6369 0.6209 0.1195  0.1057  -0.1302 119 LYS A NZ  
1038 N N   . GLU A 120 ? 0.7691 0.5996 0.5746 0.0122  0.0710  -0.2005 120 GLU A N   
1039 C CA  . GLU A 120 ? 0.8403 0.6864 0.6363 -0.0072 0.0612  -0.2122 120 GLU A CA  
1040 C C   . GLU A 120 ? 0.7736 0.6737 0.5784 -0.0104 0.0548  -0.2051 120 GLU A C   
1041 O O   . GLU A 120 ? 0.7292 0.6535 0.5411 -0.0290 0.0439  -0.2058 120 GLU A O   
1042 C CB  . GLU A 120 ? 0.9108 0.7359 0.6798 -0.0004 0.0643  -0.2289 120 GLU A CB  
1043 C CG  . GLU A 120 ? 0.9442 0.7184 0.7066 0.0011  0.0700  -0.2371 120 GLU A CG  
1044 C CD  . GLU A 120 ? 0.9794 0.7338 0.7163 0.0010  0.0707  -0.2573 120 GLU A CD  
1045 O OE1 . GLU A 120 ? 1.0197 0.7459 0.7519 -0.0166 0.0682  -0.2680 120 GLU A OE1 
1046 O OE2 . GLU A 120 ? 0.9690 0.7365 0.6903 0.0184  0.0742  -0.2625 120 GLU A OE2 
1047 N N   . LYS A 121 ? 0.7744 0.6973 0.5807 0.0085  0.0613  -0.1968 121 LYS A N   
1048 C CA  . LYS A 121 ? 0.7164 0.6920 0.5341 0.0080  0.0559  -0.1862 121 LYS A CA  
1049 C C   . LYS A 121 ? 0.6084 0.6005 0.4465 0.0248  0.0614  -0.1666 121 LYS A C   
1050 O O   . LYS A 121 ? 0.6245 0.5997 0.4594 0.0427  0.0719  -0.1661 121 LYS A O   
1051 C CB  . LYS A 121 ? 0.7721 0.7678 0.5702 0.0126  0.0554  -0.1914 121 LYS A CB  
1052 C CG  . LYS A 121 ? 0.8335 0.8787 0.6396 0.0050  0.0455  -0.1816 121 LYS A CG  
1053 C CD  . LYS A 121 ? 0.8805 0.9333 0.6679 -0.0055 0.0379  -0.1934 121 LYS A CD  
1054 C CE  . LYS A 121 ? 0.8684 0.9686 0.6659 -0.0128 0.0272  -0.1817 121 LYS A CE  
1055 N NZ  . LYS A 121 ? 0.8696 1.0022 0.6723 0.0021  0.0320  -0.1636 121 LYS A NZ  
1056 N N   . LEU A 122 ? 0.4588 0.4834 0.3187 0.0193  0.0536  -0.1484 122 LEU A N   
1057 C CA  . LEU A 122 ? 0.3959 0.4372 0.2783 0.0304  0.0564  -0.1276 122 LEU A CA  
1058 C C   . LEU A 122 ? 0.4089 0.4894 0.2914 0.0381  0.0588  -0.1183 122 LEU A C   
1059 O O   . LEU A 122 ? 0.4007 0.5040 0.2766 0.0302  0.0532  -0.1182 122 LEU A O   
1060 C CB  . LEU A 122 ? 0.3799 0.4257 0.2852 0.0188  0.0478  -0.1138 122 LEU A CB  
1061 C CG  . LEU A 122 ? 0.4390 0.4491 0.3454 0.0092  0.0457  -0.1208 122 LEU A CG  
1062 C CD1 . LEU A 122 ? 0.4617 0.4806 0.3909 0.0005  0.0384  -0.1057 122 LEU A CD1 
1063 C CD2 . LEU A 122 ? 0.4571 0.4335 0.3576 0.0235  0.0558  -0.1249 122 LEU A CD2 
1064 N N   . ASN A 123 ? 0.3449 0.4349 0.2344 0.0540  0.0677  -0.1101 123 ASN A N   
1065 C CA  . ASN A 123 ? 0.3138 0.4420 0.2078 0.0602  0.0718  -0.0981 123 ASN A CA  
1066 C C   . ASN A 123 ? 0.2745 0.4217 0.1955 0.0532  0.0673  -0.0775 123 ASN A C   
1067 O O   . ASN A 123 ? 0.2578 0.3904 0.1915 0.0443  0.0604  -0.0738 123 ASN A O   
1068 C CB  . ASN A 123 ? 0.3321 0.4643 0.2209 0.0792  0.0839  -0.1000 123 ASN A CB  
1069 C CG  . ASN A 123 ? 0.4139 0.5373 0.3203 0.0896  0.0881  -0.0934 123 ASN A CG  
1070 O OD1 . ASN A 123 ? 0.3504 0.4775 0.2782 0.0825  0.0825  -0.0818 123 ASN A OD1 
1071 N ND2 . ASN A 123 ? 0.4910 0.5996 0.3906 0.1041  0.0961  -0.0977 123 ASN A ND2 
1072 N N   . ARG A 124 ? 0.2959 0.4747 0.2249 0.0565  0.0721  -0.0640 124 ARG A N   
1073 C CA  . ARG A 124 ? 0.2316 0.4246 0.1830 0.0476  0.0687  -0.0459 124 ARG A CA  
1074 C C   . ARG A 124 ? 0.2187 0.4032 0.1909 0.0494  0.0684  -0.0413 124 ARG A C   
1075 O O   . ARG A 124 ? 0.2370 0.4135 0.2226 0.0397  0.0616  -0.0347 124 ARG A O   
1076 C CB  . ARG A 124 ? 0.2279 0.4536 0.1828 0.0491  0.0759  -0.0324 124 ARG A CB  
1077 C CG  . ARG A 124 ? 0.2791 0.5143 0.2562 0.0386  0.0741  -0.0144 124 ARG A CG  
1078 C CD  . ARG A 124 ? 0.2720 0.5245 0.2541 0.0364  0.0793  0.0002  124 ARG A CD  
1079 N NE  . ARG A 124 ? 0.2280 0.4804 0.2285 0.0248  0.0778  0.0145  124 ARG A NE  
1080 C CZ  . ARG A 124 ? 0.2626 0.5171 0.2830 0.0211  0.0786  0.0185  124 ARG A CZ  
1081 N NH1 . ARG A 124 ? 0.2306 0.4910 0.2560 0.0298  0.0809  0.0115  124 ARG A NH1 
1082 N NH2 . ARG A 124 ? 0.2357 0.4852 0.2694 0.0092  0.0771  0.0287  124 ARG A NH2 
1083 N N   . GLU A 125 ? 0.2446 0.4322 0.2185 0.0631  0.0759  -0.0447 125 GLU A N   
1084 C CA  . GLU A 125 ? 0.2620 0.4461 0.2542 0.0671  0.0753  -0.0401 125 GLU A CA  
1085 C C   . GLU A 125 ? 0.2228 0.3720 0.2125 0.0625  0.0679  -0.0463 125 GLU A C   
1086 O O   . GLU A 125 ? 0.2145 0.3609 0.2201 0.0562  0.0624  -0.0389 125 GLU A O   
1087 C CB  . GLU A 125 ? 0.2955 0.4866 0.2865 0.0853  0.0840  -0.0430 125 GLU A CB  
1088 C CG  . GLU A 125 ? 0.5610 0.7575 0.5720 0.0904  0.0825  -0.0353 125 GLU A CG  
1089 C CD  . GLU A 125 ? 0.7881 0.9535 0.7929 0.0995  0.0815  -0.0427 125 GLU A CD  
1090 O OE1 . GLU A 125 ? 0.8004 0.9688 0.8211 0.0990  0.0772  -0.0357 125 GLU A OE1 
1091 O OE2 . GLU A 125 ? 0.8723 1.0071 0.8552 0.1056  0.0846  -0.0554 125 GLU A OE2 
1092 N N   . GLU A 126 ? 0.2715 0.3938 0.2405 0.0641  0.0680  -0.0605 126 GLU A N   
1093 C CA  . GLU A 126 ? 0.2725 0.3606 0.2383 0.0580  0.0627  -0.0666 126 GLU A CA  
1094 C C   . GLU A 126 ? 0.2952 0.3854 0.2700 0.0405  0.0528  -0.0604 126 GLU A C   
1095 O O   . GLU A 126 ? 0.2501 0.3271 0.2354 0.0357  0.0484  -0.0562 126 GLU A O   
1096 C CB  . GLU A 126 ? 0.3103 0.3690 0.2509 0.0606  0.0661  -0.0846 126 GLU A CB  
1097 C CG  . GLU A 126 ? 0.3137 0.3595 0.2450 0.0814  0.0770  -0.0902 126 GLU A CG  
1098 C CD  . GLU A 126 ? 0.4318 0.4569 0.3349 0.0868  0.0835  -0.1086 126 GLU A CD  
1099 O OE1 . GLU A 126 ? 0.4029 0.4317 0.2933 0.0743  0.0791  -0.1176 126 GLU A OE1 
1100 O OE2 . GLU A 126 ? 0.5177 0.5234 0.4102 0.1050  0.0933  -0.1143 126 GLU A OE2 
1101 N N   . LEU A 127 ? 0.2149 0.3231 0.1850 0.0326  0.0500  -0.0589 127 LEU A N   
1102 C CA  . LEU A 127 ? 0.1962 0.3083 0.1740 0.0191  0.0416  -0.0519 127 LEU A CA  
1103 C C   . LEU A 127 ? 0.2094 0.3323 0.2081 0.0169  0.0403  -0.0367 127 LEU A C   
1104 O O   . LEU A 127 ? 0.1887 0.3035 0.1959 0.0089  0.0344  -0.0322 127 LEU A O   
1105 C CB  . LEU A 127 ? 0.2012 0.3328 0.1679 0.0146  0.0396  -0.0515 127 LEU A CB  
1106 C CG  . LEU A 127 ? 0.2786 0.4019 0.2242 0.0113  0.0372  -0.0683 127 LEU A CG  
1107 C CD1 . LEU A 127 ? 0.2695 0.4195 0.2024 0.0114  0.0367  -0.0665 127 LEU A CD1 
1108 C CD2 . LEU A 127 ? 0.3151 0.4229 0.2639 -0.0012 0.0288  -0.0729 127 LEU A CD2 
1109 N N   . LEU A 128 ? 0.1637 0.3061 0.1707 0.0230  0.0462  -0.0293 128 LEU A N   
1110 C CA  . LEU A 128 ? 0.1426 0.2941 0.1692 0.0189  0.0452  -0.0176 128 LEU A CA  
1111 C C   . LEU A 128 ? 0.1496 0.2842 0.1840 0.0211  0.0420  -0.0197 128 LEU A C   
1112 O O   . LEU A 128 ? 0.1702 0.3010 0.2152 0.0140  0.0372  -0.0137 128 LEU A O   
1113 C CB  . LEU A 128 ? 0.1886 0.3668 0.2238 0.0237  0.0527  -0.0112 128 LEU A CB  
1114 C CG  . LEU A 128 ? 0.1803 0.3778 0.2191 0.0159  0.0559  -0.0001 128 LEU A CG  
1115 C CD1 . LEU A 128 ? 0.2010 0.4267 0.2484 0.0208  0.0648  0.0041  128 LEU A CD1 
1116 C CD2 . LEU A 128 ? 0.1871 0.3787 0.2377 0.0040  0.0515  0.0090  128 LEU A CD2 
1117 N N   . ASP A 129 ? 0.1701 0.2926 0.1972 0.0323  0.0454  -0.0279 129 ASP A N   
1118 C CA  . ASP A 129 ? 0.1933 0.2975 0.2246 0.0363  0.0433  -0.0286 129 ASP A CA  
1119 C C   . ASP A 129 ? 0.2000 0.2802 0.2270 0.0260  0.0373  -0.0313 129 ASP A C   
1120 O O   . ASP A 129 ? 0.1734 0.2466 0.2090 0.0230  0.0335  -0.0264 129 ASP A O   
1121 C CB  . ASP A 129 ? 0.1987 0.2903 0.2200 0.0526  0.0500  -0.0357 129 ASP A CB  
1122 C CG  . ASP A 129 ? 0.2433 0.3633 0.2748 0.0656  0.0553  -0.0303 129 ASP A CG  
1123 O OD1 . ASP A 129 ? 0.2194 0.3686 0.2663 0.0586  0.0537  -0.0221 129 ASP A OD1 
1124 O OD2 . ASP A 129 ? 0.3024 0.4158 0.3265 0.0826  0.0618  -0.0344 129 ASP A OD2 
1125 N N   . LEU A 130 ? 0.1754 0.2463 0.1892 0.0200  0.0363  -0.0392 130 LEU A N   
1126 C CA  . LEU A 130 ? 0.1633 0.2174 0.1753 0.0090  0.0306  -0.0417 130 LEU A CA  
1127 C C   . LEU A 130 ? 0.1572 0.2249 0.1820 0.0004  0.0249  -0.0310 130 LEU A C   
1128 O O   . LEU A 130 ? 0.1715 0.2285 0.2026 -0.0041 0.0215  -0.0280 130 LEU A O   
1129 C CB  . LEU A 130 ? 0.2089 0.2568 0.2051 0.0028  0.0299  -0.0536 130 LEU A CB  
1130 C CG  . LEU A 130 ? 0.2584 0.2899 0.2524 -0.0097 0.0250  -0.0590 130 LEU A CG  
1131 C CD1 . LEU A 130 ? 0.3280 0.3288 0.3214 -0.0067 0.0287  -0.0613 130 LEU A CD1 
1132 C CD2 . LEU A 130 ? 0.3443 0.3758 0.3224 -0.0173 0.0236  -0.0728 130 LEU A CD2 
1133 N N   . GLN A 131 ? 0.1314 0.2206 0.1588 -0.0013 0.0250  -0.0248 131 GLN A N   
1134 C CA  . GLN A 131 ? 0.1189 0.2162 0.1562 -0.0077 0.0215  -0.0141 131 GLN A CA  
1135 C C   . GLN A 131 ? 0.1367 0.2310 0.1870 -0.0069 0.0212  -0.0083 131 GLN A C   
1136 O O   . GLN A 131 ? 0.1408 0.2278 0.1964 -0.0114 0.0176  -0.0044 131 GLN A O   
1137 C CB  . GLN A 131 ? 0.1308 0.2475 0.1670 -0.0081 0.0242  -0.0069 131 GLN A CB  
1138 C CG  . GLN A 131 ? 0.1239 0.2502 0.1460 -0.0084 0.0236  -0.0104 131 GLN A CG  
1139 C CD  . GLN A 131 ? 0.1658 0.3107 0.1854 -0.0061 0.0289  -0.0020 131 GLN A CD  
1140 O OE1 . GLN A 131 ? 0.1513 0.3037 0.1760 -0.0026 0.0349  0.0002  131 GLN A OE1 
1141 N NE2 . GLN A 131 ? 0.1736 0.3286 0.1857 -0.0075 0.0274  0.0041  131 GLN A NE2 
1142 N N   . THR A 132 ? 0.1319 0.2356 0.1872 -0.0008 0.0251  -0.0076 132 THR A N   
1143 C CA  . THR A 132 ? 0.1121 0.2199 0.1797 -0.0010 0.0240  -0.0028 132 THR A CA  
1144 C C   . THR A 132 ? 0.1287 0.2195 0.1959 0.0029  0.0213  -0.0055 132 THR A C   
1145 O O   . THR A 132 ? 0.1127 0.2015 0.1866 -0.0002 0.0181  -0.0018 132 THR A O   
1146 C CB  . THR A 132 ? 0.1028 0.2323 0.1775 0.0042  0.0285  -0.0014 132 THR A CB  
1147 O OG1 . THR A 132 ? 0.1402 0.2844 0.2136 0.0004  0.0326  0.0019  132 THR A OG1 
1148 C CG2 . THR A 132 ? 0.1006 0.2409 0.1891 0.0005  0.0262  0.0029  132 THR A CG2 
1149 N N   . LEU A 133 ? 0.1331 0.2096 0.1908 0.0100  0.0235  -0.0120 133 LEU A N   
1150 C CA  . LEU A 133 ? 0.1448 0.2018 0.2006 0.0137  0.0225  -0.0126 133 LEU A CA  
1151 C C   . LEU A 133 ? 0.1822 0.2258 0.2369 0.0036  0.0187  -0.0120 133 LEU A C   
1152 O O   . LEU A 133 ? 0.1639 0.1981 0.2210 0.0040  0.0171  -0.0088 133 LEU A O   
1153 C CB  . LEU A 133 ? 0.1615 0.2003 0.2054 0.0236  0.0278  -0.0193 133 LEU A CB  
1154 C CG  . LEU A 133 ? 0.1746 0.2287 0.2215 0.0381  0.0321  -0.0177 133 LEU A CG  
1155 C CD1 . LEU A 133 ? 0.2299 0.2650 0.2621 0.0504  0.0394  -0.0252 133 LEU A CD1 
1156 C CD2 . LEU A 133 ? 0.2409 0.3022 0.2967 0.0443  0.0297  -0.0106 133 LEU A CD2 
1157 N N   . ASN A 134 ? 0.1665 0.2120 0.2174 -0.0044 0.0172  -0.0145 134 ASN A N   
1158 C CA  . ASN A 134 ? 0.1389 0.1795 0.1917 -0.0130 0.0134  -0.0124 134 ASN A CA  
1159 C C   . ASN A 134 ? 0.2292 0.2779 0.2913 -0.0145 0.0109  -0.0041 134 ASN A C   
1160 O O   . ASN A 134 ? 0.2163 0.2575 0.2810 -0.0166 0.0092  -0.0014 134 ASN A O   
1161 C CB  . ASN A 134 ? 0.1156 0.1641 0.1633 -0.0198 0.0115  -0.0158 134 ASN A CB  
1162 C CG  . ASN A 134 ? 0.1375 0.1717 0.1760 -0.0247 0.0120  -0.0260 134 ASN A CG  
1163 O OD1 . ASN A 134 ? 0.1768 0.2028 0.2173 -0.0316 0.0104  -0.0265 134 ASN A OD1 
1164 N ND2 . ASN A 134 ? 0.1586 0.1894 0.1868 -0.0219 0.0150  -0.0345 134 ASN A ND2 
1165 N N   . LEU A 135 ? 0.1569 0.2197 0.2234 -0.0141 0.0116  -0.0003 135 LEU A N   
1166 C CA  . LEU A 135 ? 0.1438 0.2097 0.2174 -0.0167 0.0103  0.0056  135 LEU A CA  
1167 C C   . LEU A 135 ? 0.1610 0.2232 0.2381 -0.0128 0.0093  0.0052  135 LEU A C   
1168 O O   . LEU A 135 ? 0.1471 0.2028 0.2253 -0.0144 0.0072  0.0074  135 LEU A O   
1169 C CB  . LEU A 135 ? 0.1750 0.2545 0.2524 -0.0190 0.0128  0.0090  135 LEU A CB  
1170 C CG  . LEU A 135 ? 0.2301 0.3122 0.3048 -0.0231 0.0143  0.0145  135 LEU A CG  
1171 C CD1 . LEU A 135 ? 0.1874 0.2800 0.2665 -0.0265 0.0184  0.0184  135 LEU A CD1 
1172 C CD2 . LEU A 135 ? 0.1935 0.2649 0.2680 -0.0252 0.0124  0.0189  135 LEU A CD2 
1173 N N   . LEU A 136 ? 0.1033 0.1724 0.1814 -0.0062 0.0109  0.0030  136 LEU A N   
1174 C CA  . LEU A 136 ? 0.1174 0.1893 0.1986 -0.0004 0.0094  0.0038  136 LEU A CA  
1175 C C   . LEU A 136 ? 0.1254 0.1787 0.2006 0.0033  0.0089  0.0044  136 LEU A C   
1176 O O   . LEU A 136 ? 0.1223 0.1770 0.1985 0.0064  0.0068  0.0067  136 LEU A O   
1177 C CB  . LEU A 136 ? 0.1205 0.2067 0.2039 0.0091  0.0119  0.0025  136 LEU A CB  
1178 C CG  . LEU A 136 ? 0.1309 0.2421 0.2237 0.0044  0.0126  0.0032  136 LEU A CG  
1179 C CD1 . LEU A 136 ? 0.1141 0.2429 0.2092 0.0159  0.0161  0.0021  136 LEU A CD1 
1180 C CD2 . LEU A 136 ? 0.1626 0.2852 0.2636 -0.0027 0.0086  0.0047  136 LEU A CD2 
1181 N N   . ALA A 137 ? 0.1184 0.1555 0.1869 0.0022  0.0111  0.0021  137 ALA A N   
1182 C CA  . ALA A 137 ? 0.1391 0.1574 0.2022 0.0035  0.0122  0.0034  137 ALA A CA  
1183 C C   . ALA A 137 ? 0.1158 0.1348 0.1821 -0.0015 0.0094  0.0074  137 ALA A C   
1184 O O   . ALA A 137 ? 0.1532 0.1625 0.2163 0.0015  0.0103  0.0106  137 ALA A O   
1185 C CB  . ALA A 137 ? 0.1562 0.1587 0.2128 -0.0018 0.0148  -0.0014 137 ALA A CB  
1186 N N   . TRP A 138 ? 0.1276 0.1563 0.1985 -0.0081 0.0070  0.0080  138 TRP A N   
1187 C CA  . TRP A 138 ? 0.1443 0.1719 0.2165 -0.0115 0.0056  0.0113  138 TRP A CA  
1188 C C   . TRP A 138 ? 0.1222 0.1569 0.1966 -0.0104 0.0035  0.0120  138 TRP A C   
1189 O O   . TRP A 138 ? 0.1474 0.1799 0.2213 -0.0129 0.0029  0.0134  138 TRP A O   
1190 C CB  . TRP A 138 ? 0.1293 0.1605 0.2032 -0.0174 0.0053  0.0122  138 TRP A CB  
1191 C CG  . TRP A 138 ? 0.1315 0.1592 0.2035 -0.0210 0.0062  0.0101  138 TRP A CG  
1192 C CD1 . TRP A 138 ? 0.1794 0.2073 0.2483 -0.0226 0.0068  0.0050  138 TRP A CD1 
1193 C CD2 . TRP A 138 ? 0.1352 0.1598 0.2079 -0.0247 0.0068  0.0116  138 TRP A CD2 
1194 N NE1 . TRP A 138 ? 0.1286 0.1524 0.1959 -0.0287 0.0072  0.0021  138 TRP A NE1 
1195 C CE2 . TRP A 138 ? 0.1513 0.1747 0.2222 -0.0307 0.0073  0.0066  138 TRP A CE2 
1196 C CE3 . TRP A 138 ? 0.1320 0.1562 0.2066 -0.0239 0.0075  0.0163  138 TRP A CE3 
1197 C CZ2 . TRP A 138 ? 0.1903 0.2139 0.2632 -0.0381 0.0081  0.0061  138 TRP A CZ2 
1198 C CZ3 . TRP A 138 ? 0.1842 0.2099 0.2611 -0.0293 0.0090  0.0173  138 TRP A CZ3 
1199 C CH2 . TRP A 138 ? 0.2320 0.2583 0.3091 -0.0374 0.0091  0.0123  138 TRP A CH2 
1200 N N   . CYS A 139 ? 0.0959 0.1400 0.1720 -0.0064 0.0025  0.0104  139 CYS A N   
1201 C CA  . CYS A 139 ? 0.0853 0.1404 0.1641 -0.0080 -0.0003 0.0090  139 CYS A CA  
1202 C C   . CYS A 139 ? 0.1091 0.1587 0.1824 -0.0048 -0.0019 0.0101  139 CYS A C   
1203 O O   . CYS A 139 ? 0.1316 0.1758 0.2002 0.0027  -0.0009 0.0129  139 CYS A O   
1204 C CB  . CYS A 139 ? 0.1411 0.2143 0.2245 -0.0035 -0.0014 0.0074  139 CYS A CB  
1205 S SG  . CYS A 139 ? 0.1534 0.2481 0.2437 -0.0110 -0.0053 0.0035  139 CYS A SG  
1206 N N   . GLY A 140 ? 0.1075 0.1562 0.1796 -0.0103 -0.0033 0.0079  140 GLY A N   
1207 C CA  . GLY A 140 ? 0.1134 0.1588 0.1784 -0.0070 -0.0046 0.0076  140 GLY A CA  
1208 C C   . GLY A 140 ? 0.0916 0.1543 0.1556 -0.0039 -0.0092 0.0043  140 GLY A C   
1209 O O   . GLY A 140 ? 0.1202 0.2002 0.1911 -0.0053 -0.0115 0.0020  140 GLY A O   
1210 N N   . ARG A 141 ? 0.0904 0.1520 0.1455 0.0010  -0.0105 0.0044  141 ARG A N   
1211 C CA  . ARG A 141 ? 0.1091 0.1905 0.1608 0.0056  -0.0157 0.0018  141 ARG A CA  
1212 C C   . ARG A 141 ? 0.1160 0.2152 0.1741 -0.0052 -0.0204 -0.0072 141 ARG A C   
1213 O O   . ARG A 141 ? 0.1288 0.2540 0.1925 -0.0029 -0.0247 -0.0086 141 ARG A O   
1214 C CB  . ARG A 141 ? 0.1055 0.1812 0.1442 0.0107  -0.0159 0.0022  141 ARG A CB  
1215 C CG  . ARG A 141 ? 0.1193 0.2181 0.1514 0.0164  -0.0221 -0.0008 141 ARG A CG  
1216 C CD  . ARG A 141 ? 0.1275 0.2194 0.1443 0.0248  -0.0205 0.0025  141 ARG A CD  
1217 N NE  . ARG A 141 ? 0.1510 0.2666 0.1585 0.0291  -0.0273 -0.0024 141 ARG A NE  
1218 C CZ  . ARG A 141 ? 0.1755 0.2967 0.1764 0.0202  -0.0316 -0.0146 141 ARG A CZ  
1219 N NH1 . ARG A 141 ? 0.1853 0.2862 0.1872 0.0079  -0.0286 -0.0221 141 ARG A NH1 
1220 N NH2 . ARG A 141 ? 0.1747 0.3215 0.1671 0.0239  -0.0387 -0.0194 141 ARG A NH2 
1221 N N   . THR A 142 ? 0.1292 0.2153 0.1863 -0.0171 -0.0190 -0.0131 142 THR A N   
1222 C CA  . THR A 142 ? 0.1352 0.2340 0.1969 -0.0307 -0.0223 -0.0226 142 THR A CA  
1223 C C   . THR A 142 ? 0.0980 0.2154 0.1742 -0.0350 -0.0224 -0.0212 142 THR A C   
1224 O O   . THR A 142 ? 0.1319 0.2787 0.2155 -0.0395 -0.0273 -0.0261 142 THR A O   
1225 C CB  . THR A 142 ? 0.1494 0.2216 0.2057 -0.0416 -0.0179 -0.0275 142 THR A CB  
1226 O OG1 . THR A 142 ? 0.1859 0.2441 0.2278 -0.0366 -0.0176 -0.0301 142 THR A OG1 
1227 C CG2 . THR A 142 ? 0.1861 0.2661 0.2472 -0.0591 -0.0195 -0.0374 142 THR A CG2 
1228 N N   . LEU A 143 ? 0.1288 0.2331 0.2094 -0.0336 -0.0171 -0.0149 143 LEU A N   
1229 C CA  . LEU A 143 ? 0.1088 0.2297 0.2016 -0.0374 -0.0158 -0.0135 143 LEU A CA  
1230 C C   . LEU A 143 ? 0.1482 0.2896 0.2453 -0.0236 -0.0174 -0.0091 143 LEU A C   
1231 O O   . LEU A 143 ? 0.1125 0.2753 0.2199 -0.0248 -0.0168 -0.0089 143 LEU A O   
1232 C CB  . LEU A 143 ? 0.1079 0.2086 0.2015 -0.0406 -0.0094 -0.0088 143 LEU A CB  
1233 C CG  . LEU A 143 ? 0.1509 0.2353 0.2430 -0.0547 -0.0058 -0.0115 143 LEU A CG  
1234 C CD1 . LEU A 143 ? 0.1017 0.1703 0.1932 -0.0534 0.0002  -0.0043 143 LEU A CD1 
1235 C CD2 . LEU A 143 ? 0.1799 0.2833 0.2808 -0.0693 -0.0068 -0.0178 143 LEU A CD2 
1236 N N   . ARG A 144 ? 0.1675 0.3017 0.2561 -0.0099 -0.0180 -0.0048 144 ARG A N   
1237 C CA  . ARG A 144 ? 0.1745 0.3236 0.2645 0.0053  -0.0182 0.0001  144 ARG A CA  
1238 C C   . ARG A 144 ? 0.2374 0.4255 0.3348 0.0070  -0.0240 -0.0030 144 ARG A C   
1239 O O   . ARG A 144 ? 0.1907 0.3990 0.2939 0.0180  -0.0234 0.0005  144 ARG A O   
1240 C CB  . ARG A 144 ? 0.1971 0.3275 0.2749 0.0185  -0.0165 0.0062  144 ARG A CB  
1241 C CG  . ARG A 144 ? 0.1949 0.2976 0.2695 0.0213  -0.0099 0.0107  144 ARG A CG  
1242 C CD  . ARG A 144 ? 0.1568 0.2380 0.2201 0.0289  -0.0071 0.0164  144 ARG A CD  
1243 N NE  . ARG A 144 ? 0.1799 0.2368 0.2412 0.0273  -0.0013 0.0186  144 ARG A NE  
1244 C CZ  . ARG A 144 ? 0.3045 0.3500 0.3618 0.0362  0.0033  0.0219  144 ARG A CZ  
1245 N NH1 . ARG A 144 ? 0.2732 0.3296 0.3282 0.0501  0.0034  0.0251  144 ARG A NH1 
1246 N NH2 . ARG A 144 ? 0.2446 0.2685 0.2996 0.0315  0.0081  0.0215  144 ARG A NH2 
1247 N N   . LYS A 145 ? 0.2279 0.4288 0.3254 -0.0040 -0.0296 -0.0104 145 LYS A N   
1248 C CA  . LYS A 145 ? 0.2234 0.4564 0.3257 -0.0068 -0.0344 -0.0147 145 LYS A CA  
1249 C C   . LYS A 145 ? 0.2640 0.5016 0.3764 -0.0196 -0.0309 -0.0171 145 LYS A C   
1250 O O   . LYS A 145 ? 0.3188 0.5778 0.4363 -0.0141 -0.0305 -0.0150 145 LYS A O   
1251 C CB  . LYS A 145 ? 0.3463 0.5854 0.4416 -0.0161 -0.0406 -0.0234 145 LYS A CB  
1252 C CG  . LYS A 145 ? 0.4505 0.7208 0.5461 -0.0158 -0.0454 -0.0269 145 LYS A CG  
1253 C CD  . LYS A 145 ? 0.5495 0.8270 0.6335 -0.0182 -0.0519 -0.0342 145 LYS A CD  
1254 C CE  . LYS A 145 ? 0.6209 0.8800 0.6929 -0.0071 -0.0523 -0.0303 145 LYS A CE  
1255 N NZ  . LYS A 145 ? 0.7191 0.9913 0.7766 -0.0003 -0.0581 -0.0332 145 LYS A NZ  
1256 N N   . ASP A 146 ? 0.2759 0.4928 0.3902 -0.0352 -0.0275 -0.0203 146 ASP A N   
1257 C CA  . ASP A 146 ? 0.2724 0.4908 0.3944 -0.0471 -0.0234 -0.0212 146 ASP A CA  
1258 C C   . ASP A 146 ? 0.2798 0.5007 0.4070 -0.0377 -0.0181 -0.0141 146 ASP A C   
1259 O O   . ASP A 146 ? 0.3281 0.5652 0.4623 -0.0404 -0.0159 -0.0135 146 ASP A O   
1260 C CB  . ASP A 146 ? 0.4518 0.6418 0.5708 -0.0633 -0.0198 -0.0243 146 ASP A CB  
1261 C CG  . ASP A 146 ? 0.6390 0.8245 0.7514 -0.0744 -0.0240 -0.0336 146 ASP A CG  
1262 O OD1 . ASP A 146 ? 0.6298 0.8078 0.7338 -0.0698 -0.0272 -0.0361 146 ASP A OD1 
1263 O OD2 . ASP A 146 ? 0.7380 0.9277 0.8530 -0.0880 -0.0239 -0.0389 146 ASP A OD2 
1264 N N   . LEU A 147 ? 0.1472 0.3529 0.2708 -0.0272 -0.0155 -0.0093 147 LEU A N   
1265 C CA  . LEU A 147 ? 0.1301 0.3346 0.2560 -0.0186 -0.0099 -0.0044 147 LEU A CA  
1266 C C   . LEU A 147 ? 0.1369 0.3542 0.2610 0.0013  -0.0103 -0.0007 147 LEU A C   
1267 O O   . LEU A 147 ? 0.1207 0.3313 0.2435 0.0112  -0.0053 0.0025  147 LEU A O   
1268 C CB  . LEU A 147 ? 0.1461 0.3249 0.2682 -0.0206 -0.0059 -0.0020 147 LEU A CB  
1269 C CG  . LEU A 147 ? 0.2315 0.3924 0.3526 -0.0368 -0.0033 -0.0031 147 LEU A CG  
1270 C CD1 . LEU A 147 ? 0.2720 0.4078 0.3863 -0.0356 0.0002  0.0005  147 LEU A CD1 
1271 C CD2 . LEU A 147 ? 0.2689 0.4385 0.3953 -0.0440 0.0006  -0.0026 147 LEU A CD2 
1272 N N   . LYS A 148 ? 0.1225 0.3556 0.2441 0.0085  -0.0154 -0.0010 148 LYS A N   
1273 C CA  . LYS A 148 ? 0.1344 0.3741 0.2508 0.0297  -0.0145 0.0043  148 LYS A CA  
1274 C C   . LYS A 148 ? 0.1134 0.3637 0.2334 0.0371  -0.0092 0.0064  148 LYS A C   
1275 O O   . LYS A 148 ? 0.1502 0.3887 0.2642 0.0532  -0.0044 0.0104  148 LYS A O   
1276 C CB  . LYS A 148 ? 0.1585 0.4190 0.2710 0.0348  -0.0206 0.0041  148 LYS A CB  
1277 C CG  . LYS A 148 ? 0.1619 0.4268 0.2656 0.0579  -0.0190 0.0113  148 LYS A CG  
1278 C CD  . LYS A 148 ? 0.2280 0.5142 0.3262 0.0615  -0.0253 0.0111  148 LYS A CD  
1279 C CE  . LYS A 148 ? 0.3755 0.6583 0.4602 0.0851  -0.0230 0.0201  148 LYS A CE  
1280 N NZ  . LYS A 148 ? 0.4518 0.7314 0.5347 0.1005  -0.0162 0.0258  148 LYS A NZ  
1281 N N   . ASP A 149 ? 0.1307 0.4012 0.2594 0.0257  -0.0093 0.0035  149 ASP A N   
1282 C CA  . ASP A 149 ? 0.1437 0.4278 0.2757 0.0333  -0.0041 0.0057  149 ASP A CA  
1283 C C   . ASP A 149 ? 0.1219 0.3843 0.2514 0.0358  0.0028  0.0066  149 ASP A C   
1284 O O   . ASP A 149 ? 0.1576 0.4196 0.2830 0.0511  0.0079  0.0088  149 ASP A O   
1285 C CB  . ASP A 149 ? 0.2268 0.5364 0.3694 0.0188  -0.0047 0.0029  149 ASP A CB  
1286 C CG  . ASP A 149 ? 0.3118 0.6463 0.4572 0.0146  -0.0115 0.0003  149 ASP A CG  
1287 O OD1 . ASP A 149 ? 0.2776 0.6185 0.4162 0.0294  -0.0146 0.0028  149 ASP A OD1 
1288 O OD2 . ASP A 149 ? 0.4377 0.7842 0.5909 -0.0034 -0.0131 -0.0041 149 ASP A OD2 
1289 N N   . LEU A 150 ? 0.1086 0.3529 0.2391 0.0214  0.0035  0.0046  150 LEU A N   
1290 C CA  . LEU A 150 ? 0.1428 0.3695 0.2698 0.0231  0.0095  0.0050  150 LEU A CA  
1291 C C   . LEU A 150 ? 0.2101 0.4172 0.3284 0.0386  0.0113  0.0062  150 LEU A C   
1292 O O   . LEU A 150 ? 0.2398 0.4385 0.3526 0.0496  0.0175  0.0059  150 LEU A O   
1293 C CB  . LEU A 150 ? 0.1642 0.3761 0.2922 0.0050  0.0098  0.0040  150 LEU A CB  
1294 C CG  . LEU A 150 ? 0.2647 0.4864 0.3981 -0.0074 0.0130  0.0044  150 LEU A CG  
1295 C CD1 . LEU A 150 ? 0.2237 0.4261 0.3557 -0.0237 0.0134  0.0047  150 LEU A CD1 
1296 C CD2 . LEU A 150 ? 0.1666 0.3953 0.2982 0.0008  0.0198  0.0059  150 LEU A CD2 
1297 N N   . LEU A 151 ? 0.1732 0.3706 0.2887 0.0399  0.0068  0.0072  151 LEU A N   
1298 C CA  . LEU A 151 ? 0.1456 0.3120 0.2473 0.0523  0.0091  0.0092  151 LEU A CA  
1299 C C   . LEU A 151 ? 0.1869 0.3588 0.2844 0.0746  0.0138  0.0121  151 LEU A C   
1300 O O   . LEU A 151 ? 0.2727 0.4144 0.3575 0.0836  0.0198  0.0117  151 LEU A O   
1301 C CB  . LEU A 151 ? 0.1646 0.3209 0.2619 0.0503  0.0038  0.0111  151 LEU A CB  
1302 C CG  . LEU A 151 ? 0.1761 0.3161 0.2727 0.0324  0.0013  0.0086  151 LEU A CG  
1303 C CD1 . LEU A 151 ? 0.1695 0.3117 0.2640 0.0307  -0.0043 0.0094  151 LEU A CD1 
1304 C CD2 . LEU A 151 ? 0.1739 0.2794 0.2604 0.0309  0.0055  0.0085  151 LEU A CD2 
1305 N N   . ASN A 152 ? 0.1617 0.3587 0.2622 0.0787  0.0106  0.0139  152 ASN A N   
1306 C CA  . ASN A 152 ? 0.2165 0.4134 0.3085 0.0982  0.0146  0.0174  152 ASN A CA  
1307 C C   . ASN A 152 ? 0.2116 0.4149 0.3047 0.1021  0.0209  0.0150  152 ASN A C   
1308 O O   . ASN A 152 ? 0.2550 0.4477 0.3379 0.1194  0.0266  0.0170  152 ASN A O   
1309 C CB  . ASN A 152 ? 0.2489 0.4741 0.3428 0.1020  0.0089  0.0208  152 ASN A CB  
1310 C CG  . ASN A 152 ? 0.4205 0.6355 0.5067 0.1055  0.0047  0.0244  152 ASN A CG  
1311 O OD1 . ASN A 152 ? 0.4300 0.6274 0.5159 0.0966  0.0030  0.0230  152 ASN A OD1 
1312 N ND2 . ASN A 152 ? 0.5136 0.7415 0.5928 0.1190  0.0036  0.0296  152 ASN A ND2 
1313 N N   . LYS A 153 ? 0.2142 0.4318 0.3175 0.0867  0.0207  0.0113  153 LYS A N   
1314 C CA  . LYS A 153 ? 0.2201 0.4447 0.3231 0.0905  0.0272  0.0094  153 LYS A CA  
1315 C C   . LYS A 153 ? 0.2599 0.4517 0.3488 0.1028  0.0350  0.0064  153 LYS A C   
1316 O O   . LYS A 153 ? 0.3351 0.5229 0.4156 0.1172  0.0411  0.0059  153 LYS A O   
1317 C CB  . LYS A 153 ? 0.1951 0.4338 0.3085 0.0704  0.0266  0.0071  153 LYS A CB  
1318 C CG  . LYS A 153 ? 0.2256 0.4737 0.3381 0.0730  0.0335  0.0059  153 LYS A CG  
1319 C CD  . LYS A 153 ? 0.2386 0.4994 0.3600 0.0527  0.0332  0.0060  153 LYS A CD  
1320 C CE  . LYS A 153 ? 0.2520 0.5242 0.3715 0.0561  0.0405  0.0060  153 LYS A CE  
1321 N NZ  . LYS A 153 ? 0.2439 0.5291 0.3715 0.0379  0.0412  0.0082  153 LYS A NZ  
1322 N N   . GLY A 154 ? 0.1982 0.3649 0.2829 0.0971  0.0352  0.0039  154 GLY A N   
1323 C CA  . GLY A 154 ? 0.3291 0.4558 0.3965 0.1054  0.0418  -0.0005 154 GLY A CA  
1324 C C   . GLY A 154 ? 0.3298 0.4482 0.3894 0.1014  0.0472  -0.0079 154 GLY A C   
1325 O O   . GLY A 154 ? 0.3266 0.4085 0.3710 0.0977  0.0496  -0.0141 154 GLY A O   
1326 N N   . ARG A 155 ? 0.3263 0.4789 0.3953 0.1013  0.0495  -0.0078 155 ARG A N   
1327 C CA  . ARG A 155 ? 0.3047 0.4519 0.3637 0.1009  0.0556  -0.0145 155 ARG A CA  
1328 C C   . ARG A 155 ? 0.2920 0.4778 0.3640 0.0932  0.0556  -0.0108 155 ARG A C   
1329 O O   . ARG A 155 ? 0.2830 0.4931 0.3692 0.0874  0.0505  -0.0044 155 ARG A O   
1330 C CB  . ARG A 155 ? 0.3222 0.4465 0.3638 0.1209  0.0640  -0.0195 155 ARG A CB  
1331 C CG  . ARG A 155 ? 0.3956 0.5420 0.4427 0.1329  0.0645  -0.0132 155 ARG A CG  
1332 C CD  . ARG A 155 ? 0.5064 0.6251 0.5348 0.1514  0.0726  -0.0174 155 ARG A CD  
1333 N NE  . ARG A 155 ? 0.5760 0.6533 0.5916 0.1577  0.0736  -0.0179 155 ARG A NE  
1334 C CZ  . ARG A 155 ? 0.5862 0.6186 0.5819 0.1592  0.0797  -0.0272 155 ARG A CZ  
1335 N NH1 . ARG A 155 ? 0.5412 0.5354 0.5263 0.1619  0.0808  -0.0260 155 ARG A NH1 
1336 N NH2 . ARG A 155 ? 0.6055 0.6307 0.5905 0.1563  0.0848  -0.0380 155 ARG A NH2 
1337 N N   . ASN A 156 ? 0.2354 0.4224 0.2993 0.0913  0.0610  -0.0154 156 ASN A N   
1338 C CA  . ASN A 156 ? 0.2096 0.4253 0.2812 0.0836  0.0624  -0.0113 156 ASN A CA  
1339 C C   . ASN A 156 ? 0.1910 0.4220 0.2776 0.0630  0.0565  -0.0047 156 ASN A C   
1340 O O   . ASN A 156 ? 0.2108 0.4642 0.3090 0.0561  0.0553  0.0008  156 ASN A O   
1341 C CB  . ASN A 156 ? 0.2503 0.4855 0.3265 0.0954  0.0645  -0.0078 156 ASN A CB  
1342 C CG  . ASN A 156 ? 0.4101 0.6255 0.4693 0.1161  0.0713  -0.0138 156 ASN A CG  
1343 O OD1 . ASN A 156 ? 0.4577 0.6509 0.5004 0.1189  0.0764  -0.0221 156 ASN A OD1 
1344 N ND2 . ASN A 156 ? 0.4352 0.6573 0.4965 0.1302  0.0715  -0.0101 156 ASN A ND2 
1345 N N   . TYR A 157 ? 0.1332 0.3496 0.2183 0.0530  0.0535  -0.0057 157 TYR A N   
1346 C CA  . TYR A 157 ? 0.1481 0.3695 0.2433 0.0339  0.0487  0.0003  157 TYR A CA  
1347 C C   . TYR A 157 ? 0.1443 0.3736 0.2361 0.0252  0.0530  0.0038  157 TYR A C   
1348 O O   . TYR A 157 ? 0.2309 0.4580 0.3097 0.0313  0.0580  0.0002  157 TYR A O   
1349 C CB  . TYR A 157 ? 0.1143 0.3076 0.2043 0.0264  0.0425  -0.0010 157 TYR A CB  
1350 C CG  . TYR A 157 ? 0.1176 0.2991 0.2094 0.0329  0.0378  -0.0024 157 TYR A CG  
1351 C CD1 . TYR A 157 ? 0.1603 0.3579 0.2663 0.0282  0.0334  0.0015  157 TYR A CD1 
1352 C CD2 . TYR A 157 ? 0.1903 0.3445 0.2684 0.0437  0.0384  -0.0078 157 TYR A CD2 
1353 C CE1 . TYR A 157 ? 0.1696 0.3584 0.2752 0.0358  0.0292  0.0012  157 TYR A CE1 
1354 C CE2 . TYR A 157 ? 0.2070 0.3489 0.2851 0.0507  0.0355  -0.0070 157 TYR A CE2 
1355 C CZ  . TYR A 157 ? 0.1921 0.3527 0.2837 0.0477  0.0307  -0.0019 157 TYR A CZ  
1356 O OH  . TYR A 157 ? 0.1847 0.3350 0.2744 0.0562  0.0278  -0.0001 157 TYR A OH  
1357 N N   . THR A 158 ? 0.1570 0.3938 0.2583 0.0114  0.0515  0.0102  158 THR A N   
1358 C CA  . THR A 158 ? 0.1602 0.4015 0.2583 0.0029  0.0564  0.0157  158 THR A CA  
1359 C C   . THR A 158 ? 0.1098 0.3331 0.2045 -0.0090 0.0543  0.0201  158 THR A C   
1360 O O   . THR A 158 ? 0.0999 0.3095 0.1981 -0.0135 0.0486  0.0191  158 THR A O   
1361 C CB  . THR A 158 ? 0.1691 0.4281 0.2790 -0.0044 0.0585  0.0200  158 THR A CB  
1362 O OG1 . THR A 158 ? 0.1642 0.4170 0.2845 -0.0162 0.0531  0.0208  158 THR A OG1 
1363 C CG2 . THR A 158 ? 0.1436 0.4236 0.2574 0.0086  0.0603  0.0170  158 THR A CG2 
1364 N N   . GLN A 159 ? 0.1386 0.3942 0.2036 -0.0261 0.0106  0.0000  159 GLN A N   
1365 C CA  . GLN A 159 ? 0.1526 0.3838 0.2047 -0.0302 0.0172  0.0148  159 GLN A CA  
1366 C C   . GLN A 159 ? 0.1407 0.3575 0.1960 -0.0447 0.0243  0.0131  159 GLN A C   
1367 O O   . GLN A 159 ? 0.1695 0.3583 0.2160 -0.0419 0.0217  0.0210  159 GLN A O   
1368 C CB  . GLN A 159 ? 0.2144 0.4359 0.2448 -0.0315 0.0296  0.0250  159 GLN A CB  
1369 C CG  . GLN A 159 ? 0.2150 0.3950 0.2161 -0.0290 0.0378  0.0412  159 GLN A CG  
1370 C CD  . GLN A 159 ? 0.2366 0.4095 0.2304 -0.0089 0.0234  0.0467  159 GLN A CD  
1371 O OE1 . GLN A 159 ? 0.2108 0.4075 0.2163 0.0011  0.0119  0.0395  159 GLN A OE1 
1372 N NE2 . GLN A 159 ? 0.2206 0.3618 0.1961 -0.0039 0.0254  0.0567  159 GLN A NE2 
1373 N N   . GLU A 160 ? 0.1424 0.3811 0.2119 -0.0605 0.0332  -0.0010 160 GLU A N   
1374 C CA  . GLU A 160 ? 0.1659 0.3937 0.2409 -0.0760 0.0405  -0.0087 160 GLU A CA  
1375 C C   . GLU A 160 ? 0.1751 0.4049 0.2600 -0.0651 0.0240  -0.0133 160 GLU A C   
1376 O O   . GLU A 160 ? 0.1869 0.3987 0.2704 -0.0737 0.0280  -0.0104 160 GLU A O   
1377 C CB  . GLU A 160 ? 0.2432 0.4897 0.3293 -0.0884 0.0481  -0.0288 160 GLU A CB  
1378 C CG  . GLU A 160 ? 0.3402 0.5759 0.4306 -0.1075 0.0599  -0.0403 160 GLU A CG  
1379 C CD  . GLU A 160 ? 0.4825 0.7434 0.5835 -0.1204 0.0681  -0.0633 160 GLU A CD  
1380 O OE1 . GLU A 160 ? 0.5204 0.7848 0.6165 -0.1256 0.0779  -0.0626 160 GLU A OE1 
1381 O OE2 . GLU A 160 ? 0.5199 0.7996 0.6332 -0.1249 0.0651  -0.0836 160 GLU A OE2 
1382 N N   . GLU A 161 ? 0.1132 0.3554 0.2011 -0.0453 0.0079  -0.0197 161 GLU A N   
1383 C CA  . GLU A 161 ? 0.1094 0.3432 0.1968 -0.0322 -0.0043 -0.0221 161 GLU A CA  
1384 C C   . GLU A 161 ? 0.1241 0.3344 0.2044 -0.0278 -0.0078 -0.0065 161 GLU A C   
1385 O O   . GLU A 161 ? 0.1358 0.3343 0.2166 -0.0283 -0.0112 -0.0054 161 GLU A O   
1386 C CB  . GLU A 161 ? 0.1061 0.3461 0.1876 -0.0117 -0.0139 -0.0295 161 GLU A CB  
1387 C CG  . GLU A 161 ? 0.1126 0.3823 0.2008 -0.0121 -0.0130 -0.0482 161 GLU A CG  
1388 C CD  . GLU A 161 ? 0.2276 0.5051 0.3060 0.0095  -0.0200 -0.0549 161 GLU A CD  
1389 O OE1 . GLU A 161 ? 0.1933 0.4563 0.2622 0.0185  -0.0213 -0.0461 161 GLU A OE1 
1390 O OE2 . GLU A 161 ? 0.2744 0.5746 0.3535 0.0180  -0.0231 -0.0711 161 GLU A OE2 
1391 N N   . LYS A 162 ? 0.1023 0.3064 0.1749 -0.0223 -0.0076 0.0038  162 LYS A N   
1392 C CA  . LYS A 162 ? 0.1112 0.2855 0.1715 -0.0161 -0.0099 0.0151  162 LYS A CA  
1393 C C   . LYS A 162 ? 0.1239 0.2728 0.1753 -0.0254 -0.0026 0.0234  162 LYS A C   
1394 O O   . LYS A 162 ? 0.1321 0.2611 0.1797 -0.0219 -0.0064 0.0269  162 LYS A O   
1395 C CB  . LYS A 162 ? 0.1061 0.2838 0.1594 -0.0089 -0.0097 0.0197  162 LYS A CB  
1396 C CG  . LYS A 162 ? 0.1150 0.2766 0.1610 -0.0008 -0.0133 0.0240  162 LYS A CG  
1397 C CD  . LYS A 162 ? 0.1448 0.3217 0.1879 0.0066  -0.0141 0.0221  162 LYS A CD  
1398 C CE  . LYS A 162 ? 0.1513 0.3339 0.1831 0.0052  -0.0076 0.0293  162 LYS A CE  
1399 N NZ  . LYS A 162 ? 0.1352 0.3314 0.1591 0.0169  -0.0101 0.0283  162 LYS A NZ  
1400 N N   . GLU A 163 ? 0.1459 0.2906 0.1904 -0.0373 0.0103  0.0267  163 GLU A N   
1401 C CA  . GLU A 163 ? 0.1812 0.2916 0.2098 -0.0454 0.0215  0.0352  163 GLU A CA  
1402 C C   . GLU A 163 ? 0.1706 0.2791 0.2117 -0.0564 0.0217  0.0258  163 GLU A C   
1403 O O   . GLU A 163 ? 0.1917 0.2704 0.2222 -0.0568 0.0240  0.0321  163 GLU A O   
1404 C CB  . GLU A 163 ? 0.2419 0.3398 0.2541 -0.0575 0.0411  0.0398  163 GLU A CB  
1405 C CG  . GLU A 163 ? 0.2758 0.3659 0.2653 -0.0414 0.0411  0.0526  163 GLU A CG  
1406 C CD  . GLU A 163 ? 0.4079 0.4924 0.3807 -0.0511 0.0601  0.0557  163 GLU A CD  
1407 O OE1 . GLU A 163 ? 0.4219 0.4983 0.3706 -0.0359 0.0612  0.0665  163 GLU A OE1 
1408 O OE2 . GLU A 163 ? 0.4120 0.5028 0.3955 -0.0739 0.0748  0.0452  163 GLU A OE2 
1409 N N   . TYR A 164 ? 0.1255 0.2688 0.1882 -0.0630 0.0184  0.0091  164 TYR A N   
1410 C CA  . TYR A 164 ? 0.1477 0.2993 0.2235 -0.0700 0.0157  -0.0040 164 TYR A CA  
1411 C C   . TYR A 164 ? 0.1577 0.2945 0.2291 -0.0537 0.0015  0.0016  164 TYR A C   
1412 O O   . TYR A 164 ? 0.1601 0.2788 0.2294 -0.0582 0.0027  0.0013  164 TYR A O   
1413 C CB  . TYR A 164 ? 0.1452 0.3454 0.2428 -0.0719 0.0114  -0.0258 164 TYR A CB  
1414 C CG  . TYR A 164 ? 0.1883 0.3994 0.2938 -0.0691 0.0046  -0.0422 164 TYR A CG  
1415 C CD1 . TYR A 164 ? 0.2437 0.4521 0.3543 -0.0884 0.0169  -0.0546 164 TYR A CD1 
1416 C CD2 . TYR A 164 ? 0.1662 0.3862 0.2687 -0.0458 -0.0120 -0.0453 164 TYR A CD2 
1417 C CE1 . TYR A 164 ? 0.3014 0.5265 0.4190 -0.0846 0.0104  -0.0715 164 TYR A CE1 
1418 C CE2 . TYR A 164 ? 0.2063 0.4385 0.3113 -0.0402 -0.0176 -0.0598 164 TYR A CE2 
1419 C CZ  . TYR A 164 ? 0.2948 0.5339 0.4097 -0.0596 -0.0076 -0.0735 164 TYR A CZ  
1420 O OH  . TYR A 164 ? 0.3876 0.6444 0.5055 -0.0529 -0.0132 -0.0900 164 TYR A OH  
1421 N N   . VAL A 165 ? 0.1101 0.2516 0.1786 -0.0362 -0.0093 0.0056  165 VAL A N   
1422 C CA  . VAL A 165 ? 0.1226 0.2456 0.1840 -0.0235 -0.0178 0.0097  165 VAL A CA  
1423 C C   . VAL A 165 ? 0.1494 0.2412 0.2001 -0.0254 -0.0138 0.0216  165 VAL A C   
1424 O O   . VAL A 165 ? 0.1470 0.2218 0.1948 -0.0246 -0.0157 0.0222  165 VAL A O   
1425 C CB  . VAL A 165 ? 0.1192 0.2468 0.1766 -0.0084 -0.0239 0.0098  165 VAL A CB  
1426 C CG1 . VAL A 165 ? 0.1233 0.2246 0.1704 0.0001  -0.0263 0.0132  165 VAL A CG1 
1427 C CG2 . VAL A 165 ? 0.0990 0.2536 0.1607 0.0010  -0.0294 -0.0020 165 VAL A CG2 
1428 N N   . LEU A 166 ? 0.1238 0.2091 0.1660 -0.0247 -0.0087 0.0303  166 LEU A N   
1429 C CA  . LEU A 166 ? 0.1549 0.2145 0.1830 -0.0202 -0.0062 0.0402  166 LEU A CA  
1430 C C   . LEU A 166 ? 0.1957 0.2308 0.2170 -0.0303 0.0019  0.0424  166 LEU A C   
1431 O O   . LEU A 166 ? 0.1962 0.2108 0.2103 -0.0251 0.0003  0.0462  166 LEU A O   
1432 C CB  . LEU A 166 ? 0.2163 0.2752 0.2305 -0.0135 -0.0019 0.0483  166 LEU A CB  
1433 C CG  . LEU A 166 ? 0.1949 0.2771 0.2152 -0.0029 -0.0096 0.0441  166 LEU A CG  
1434 C CD1 . LEU A 166 ? 0.2481 0.3371 0.2553 0.0025  -0.0051 0.0498  166 LEU A CD1 
1435 C CD2 . LEU A 166 ? 0.2293 0.3094 0.2503 0.0074  -0.0160 0.0411  166 LEU A CD2 
1436 N N   . ASN A 167 ? 0.1746 0.2121 0.1988 -0.0461 0.0125  0.0376  167 ASN A N   
1437 C CA  . ASN A 167 ? 0.2180 0.2303 0.2364 -0.0599 0.0240  0.0358  167 ASN A CA  
1438 C C   . ASN A 167 ? 0.2272 0.2460 0.2590 -0.0599 0.0145  0.0265  167 ASN A C   
1439 O O   . ASN A 167 ? 0.2123 0.2035 0.2352 -0.0613 0.0180  0.0295  167 ASN A O   
1440 C CB  . ASN A 167 ? 0.2441 0.2643 0.2678 -0.0820 0.0404  0.0258  167 ASN A CB  
1441 C CG  . ASN A 167 ? 0.4759 0.4681 0.4942 -0.1010 0.0568  0.0199  167 ASN A CG  
1442 O OD1 . ASN A 167 ? 0.5214 0.5388 0.5617 -0.1169 0.0583  0.0000  167 ASN A OD1 
1443 N ND2 . ASN A 167 ? 0.5902 0.5307 0.5773 -0.0975 0.0693  0.0352  167 ASN A ND2 
1444 N N   . LYS A 168 ? 0.1959 0.2481 0.2447 -0.0556 0.0029  0.0154  168 LYS A N   
1445 C CA  . LYS A 168 ? 0.1804 0.2369 0.2353 -0.0516 -0.0059 0.0071  168 LYS A CA  
1446 C C   . LYS A 168 ? 0.1626 0.1949 0.2065 -0.0385 -0.0118 0.0175  168 LYS A C   
1447 O O   . LYS A 168 ? 0.1428 0.1609 0.1844 -0.0387 -0.0129 0.0159  168 LYS A O   
1448 C CB  . LYS A 168 ? 0.1659 0.2583 0.2314 -0.0425 -0.0167 -0.0055 168 LYS A CB  
1449 C CG  . LYS A 168 ? 0.1788 0.3090 0.2612 -0.0542 -0.0131 -0.0233 168 LYS A CG  
1450 C CD  . LYS A 168 ? 0.2673 0.4055 0.3597 -0.0685 -0.0087 -0.0393 168 LYS A CD  
1451 C CE  . LYS A 168 ? 0.4291 0.6153 0.5366 -0.0657 -0.0138 -0.0629 168 LYS A CE  
1452 N NZ  . LYS A 168 ? 0.5647 0.7558 0.6806 -0.0880 0.0027  -0.0776 168 LYS A NZ  
1453 N N   . TYR A 169 ? 0.1479 0.1790 0.1867 -0.0283 -0.0144 0.0255  169 TYR A N   
1454 C CA  . TYR A 169 ? 0.1395 0.1558 0.1722 -0.0184 -0.0178 0.0299  169 TYR A CA  
1455 C C   . TYR A 169 ? 0.1753 0.1679 0.1986 -0.0187 -0.0133 0.0366  169 TYR A C   
1456 O O   . TYR A 169 ? 0.1704 0.1513 0.1917 -0.0144 -0.0156 0.0357  169 TYR A O   
1457 C CB  . TYR A 169 ? 0.1310 0.1580 0.1638 -0.0104 -0.0196 0.0314  169 TYR A CB  
1458 C CG  . TYR A 169 ? 0.1156 0.1526 0.1509 -0.0058 -0.0225 0.0249  169 TYR A CG  
1459 C CD1 . TYR A 169 ? 0.1017 0.1433 0.1364 -0.0042 -0.0255 0.0196  169 TYR A CD1 
1460 C CD2 . TYR A 169 ? 0.1438 0.1855 0.1791 -0.0012 -0.0213 0.0225  169 TYR A CD2 
1461 C CE1 . TYR A 169 ? 0.1614 0.2038 0.1887 0.0060  -0.0269 0.0153  169 TYR A CE1 
1462 C CE2 . TYR A 169 ? 0.1162 0.1561 0.1470 0.0035  -0.0199 0.0171  169 TYR A CE2 
1463 C CZ  . TYR A 169 ? 0.1590 0.1954 0.1825 0.0089  -0.0225 0.0154  169 TYR A CZ  
1464 O OH  . TYR A 169 ? 0.1591 0.1854 0.1687 0.0191  -0.0198 0.0117  169 TYR A OH  
1465 N N   . PHE A 170 ? 0.1954 0.1769 0.2083 -0.0214 -0.0055 0.0436  170 PHE A N   
1466 C CA  . PHE A 170 ? 0.2071 0.1580 0.2025 -0.0168 0.0003  0.0511  170 PHE A CA  
1467 C C   . PHE A 170 ? 0.2161 0.1480 0.2120 -0.0289 0.0058  0.0466  170 PHE A C   
1468 O O   . PHE A 170 ? 0.2065 0.1151 0.1917 -0.0226 0.0069  0.0498  170 PHE A O   
1469 C CB  . PHE A 170 ? 0.2790 0.2124 0.2522 -0.0126 0.0103  0.0616  170 PHE A CB  
1470 C CG  . PHE A 170 ? 0.2633 0.2093 0.2285 0.0080  0.0030  0.0660  170 PHE A CG  
1471 C CD1 . PHE A 170 ? 0.2947 0.2340 0.2494 0.0266  -0.0023 0.0674  170 PHE A CD1 
1472 C CD2 . PHE A 170 ? 0.2960 0.2677 0.2671 0.0098  0.0002  0.0649  170 PHE A CD2 
1473 C CE1 . PHE A 170 ? 0.3125 0.2752 0.2639 0.0466  -0.0103 0.0654  170 PHE A CE1 
1474 C CE2 . PHE A 170 ? 0.3211 0.3111 0.2871 0.0284  -0.0069 0.0647  170 PHE A CE2 
1475 C CZ  . PHE A 170 ? 0.3133 0.3018 0.2706 0.0468  -0.0125 0.0635  170 PHE A CZ  
1476 N N   . GLU A 171 ? 0.1858 0.1317 0.1950 -0.0450 0.0088  0.0363  171 GLU A N   
1477 C CA  . GLU A 171 ? 0.1803 0.1186 0.1948 -0.0561 0.0117  0.0266  171 GLU A CA  
1478 C C   . GLU A 171 ? 0.1714 0.1126 0.1897 -0.0451 -0.0002 0.0245  171 GLU A C   
1479 O O   . GLU A 171 ? 0.2299 0.1505 0.2428 -0.0463 0.0022  0.0235  171 GLU A O   
1480 C CB  . GLU A 171 ? 0.1963 0.1652 0.2292 -0.0721 0.0136  0.0097  171 GLU A CB  
1481 C CG  . GLU A 171 ? 0.4024 0.3661 0.4332 -0.0907 0.0314  0.0064  171 GLU A CG  
1482 C CD  . GLU A 171 ? 0.5221 0.5322 0.5776 -0.1048 0.0312  -0.0155 171 GLU A CD  
1483 O OE1 . GLU A 171 ? 0.5304 0.5734 0.6008 -0.0975 0.0166  -0.0282 171 GLU A OE1 
1484 O OE2 . GLU A 171 ? 0.6104 0.6247 0.6676 -0.1205 0.0460  -0.0209 171 GLU A OE2 
1485 N N   . ILE A 172 ? 0.1612 0.1236 0.1861 -0.0350 -0.0105 0.0233  172 ILE A N   
1486 C CA  . ILE A 172 ? 0.1527 0.1114 0.1762 -0.0259 -0.0170 0.0214  172 ILE A CA  
1487 C C   . ILE A 172 ? 0.1954 0.1347 0.2110 -0.0188 -0.0152 0.0282  172 ILE A C   
1488 O O   . ILE A 172 ? 0.1936 0.1198 0.2063 -0.0174 -0.0154 0.0259  172 ILE A O   
1489 C CB  . ILE A 172 ? 0.1202 0.0945 0.1447 -0.0171 -0.0225 0.0195  172 ILE A CB  
1490 C CG1 . ILE A 172 ? 0.1592 0.1545 0.1873 -0.0168 -0.0269 0.0106  172 ILE A CG1 
1491 C CG2 . ILE A 172 ? 0.1562 0.1173 0.1733 -0.0095 -0.0230 0.0186  172 ILE A CG2 
1492 C CD1 . ILE A 172 ? 0.2104 0.2077 0.2362 -0.0153 -0.0308 0.0010  172 ILE A CD1 
1493 N N   . ILE A 173 ? 0.1460 0.0867 0.1575 -0.0123 -0.0140 0.0348  173 ILE A N   
1494 C CA  . ILE A 173 ? 0.1469 0.0790 0.1512 -0.0003 -0.0145 0.0375  173 ILE A CA  
1495 C C   . ILE A 173 ? 0.1941 0.0962 0.1851 -0.0004 -0.0090 0.0414  173 ILE A C   
1496 O O   . ILE A 173 ? 0.1915 0.0854 0.1798 0.0070  -0.0106 0.0391  173 ILE A O   
1497 C CB  . ILE A 173 ? 0.1947 0.1391 0.1943 0.0108  -0.0155 0.0416  173 ILE A CB  
1498 C CG1 . ILE A 173 ? 0.2222 0.1946 0.2363 0.0095  -0.0194 0.0342  173 ILE A CG1 
1499 C CG2 . ILE A 173 ? 0.2522 0.1914 0.2405 0.0288  -0.0172 0.0425  173 ILE A CG2 
1500 C CD1 . ILE A 173 ? 0.2005 0.1928 0.2134 0.0191  -0.0213 0.0344  173 ILE A CD1 
1501 N N   . LYS A 174 ? 0.2083 0.0924 0.1905 -0.0103 -0.0001 0.0455  174 LYS A N   
1502 C CA  . LYS A 174 ? 0.2302 0.0769 0.1951 -0.0127 0.0101  0.0485  174 LYS A CA  
1503 C C   . LYS A 174 ? 0.2820 0.1292 0.2585 -0.0212 0.0082  0.0383  174 LYS A C   
1504 O O   . LYS A 174 ? 0.2944 0.1251 0.2639 -0.0190 0.0124  0.0375  174 LYS A O   
1505 C CB  . LYS A 174 ? 0.2957 0.1300 0.2529 -0.0264 0.0234  0.0499  174 LYS A CB  
1506 C CG  . LYS A 174 ? 0.3320 0.1547 0.2671 -0.0132 0.0284  0.0614  174 LYS A CG  
1507 C CD  . LYS A 174 ? 0.3722 0.1832 0.3000 -0.0298 0.0440  0.0610  174 LYS A CD  
1508 C CE  . LYS A 174 ? 0.5967 0.3712 0.4923 -0.0203 0.0569  0.0679  174 LYS A CE  
1509 N NZ  . LYS A 174 ? 0.7553 0.5154 0.6402 -0.0358 0.0750  0.0669  174 LYS A NZ  
1510 N N   . LYS A 175 ? 0.2338 0.1056 0.2271 -0.0278 0.0004  0.0295  175 LYS A N   
1511 C CA  . LYS A 175 ? 0.2341 0.1067 0.2337 -0.0330 -0.0023 0.0196  175 LYS A CA  
1512 C C   . LYS A 175 ? 0.2311 0.1086 0.2316 -0.0209 -0.0097 0.0191  175 LYS A C   
1513 O O   . LYS A 175 ? 0.2102 0.0870 0.2121 -0.0227 -0.0119 0.0118  175 LYS A O   
1514 C CB  . LYS A 175 ? 0.2598 0.1604 0.2729 -0.0428 -0.0063 0.0078  175 LYS A CB  
1515 C CG  . LYS A 175 ? 0.4462 0.3509 0.4647 -0.0602 0.0031  0.0004  175 LYS A CG  
1516 C CD  . LYS A 175 ? 0.5289 0.4729 0.5635 -0.0655 -0.0037 -0.0168 175 LYS A CD  
1517 C CE  . LYS A 175 ? 0.6273 0.5949 0.6629 -0.0496 -0.0158 -0.0131 175 LYS A CE  
1518 N NZ  . LYS A 175 ? 0.7053 0.7118 0.7504 -0.0471 -0.0239 -0.0301 175 LYS A NZ  
1519 N N   . THR A 176 ? 0.2024 0.0873 0.2024 -0.0098 -0.0122 0.0239  176 THR A N   
1520 C CA  . THR A 176 ? 0.1813 0.0766 0.1858 -0.0039 -0.0153 0.0188  176 THR A CA  
1521 C C   . THR A 176 ? 0.1873 0.0698 0.1881 0.0012  -0.0140 0.0155  176 THR A C   
1522 O O   . THR A 176 ? 0.2209 0.1043 0.2218 -0.0010 -0.0127 0.0093  176 THR A O   
1523 C CB  . THR A 176 ? 0.1772 0.0913 0.1869 0.0025  -0.0162 0.0189  176 THR A CB  
1524 O OG1 . THR A 176 ? 0.1755 0.1010 0.1884 -0.0023 -0.0171 0.0205  176 THR A OG1 
1525 C CG2 . THR A 176 ? 0.1713 0.0946 0.1866 0.0042  -0.0137 0.0091  176 THR A CG2 
1526 N N   . LEU A 177 ? 0.2295 0.0999 0.2225 0.0105  -0.0128 0.0194  177 LEU A N   
1527 C CA  . LEU A 177 ? 0.2458 0.1072 0.2354 0.0172  -0.0115 0.0148  177 LEU A CA  
1528 C C   . LEU A 177 ? 0.2600 0.1139 0.2505 0.0064  -0.0059 0.0119  177 LEU A C   
1529 O O   . LEU A 177 ? 0.2319 0.0855 0.2238 0.0071  -0.0055 0.0057  177 LEU A O   
1530 C CB  . LEU A 177 ? 0.2497 0.1005 0.2262 0.0351  -0.0113 0.0193  177 LEU A CB  
1531 C CG  . LEU A 177 ? 0.3446 0.2248 0.3261 0.0511  -0.0169 0.0150  177 LEU A CG  
1532 C CD1 . LEU A 177 ? 0.4233 0.2934 0.3852 0.0769  -0.0185 0.0178  177 LEU A CD1 
1533 C CD2 . LEU A 177 ? 0.3707 0.2818 0.3728 0.0463  -0.0178 -0.0006 177 LEU A CD2 
1534 N N   . SER A 178 ? 0.2034 0.0525 0.1947 -0.0040 -0.0025 0.0136  178 SER A N   
1535 C CA  . SER A 178 ? 0.2150 0.0586 0.2101 -0.0143 -0.0005 0.0064  178 SER A CA  
1536 C C   . SER A 178 ? 0.2112 0.0661 0.2066 -0.0169 -0.0050 -0.0017 178 SER A C   
1537 O O   . SER A 178 ? 0.2256 0.0760 0.2207 -0.0192 -0.0048 -0.0089 178 SER A O   
1538 C CB  . SER A 178 ? 0.2289 0.0669 0.2244 -0.0276 0.0021  0.0054  178 SER A CB  
1539 O OG  . SER A 178 ? 0.3235 0.1409 0.3062 -0.0248 0.0087  0.0129  178 SER A OG  
1540 N N   . ILE A 179 ? 0.2117 0.0791 0.2072 -0.0150 -0.0107 -0.0003 179 ILE A N   
1541 C CA  . ILE A 179 ? 0.2100 0.0798 0.2006 -0.0134 -0.0162 -0.0064 179 ILE A CA  
1542 C C   . ILE A 179 ? 0.1799 0.0475 0.1666 -0.0070 -0.0114 -0.0074 179 ILE A C   
1543 O O   . ILE A 179 ? 0.1889 0.0504 0.1664 -0.0050 -0.0128 -0.0129 179 ILE A O   
1544 C CB  . ILE A 179 ? 0.2294 0.1116 0.2179 -0.0100 -0.0202 -0.0044 179 ILE A CB  
1545 C CG1 . ILE A 179 ? 0.2315 0.1155 0.2046 -0.0013 -0.0230 -0.0097 179 ILE A CG1 
1546 C CG2 . ILE A 179 ? 0.2329 0.1150 0.2223 -0.0063 -0.0163 0.0017  179 ILE A CG2 
1547 C CD1 . ILE A 179 ? 0.3420 0.2413 0.3163 -0.0020 -0.0296 -0.0212 179 ILE A CD1 
1548 N N   . TYR A 180 ? 0.1744 0.0449 0.1664 -0.0035 -0.0070 -0.0048 180 TYR A N   
1549 C CA  . TYR A 180 ? 0.1770 0.0453 0.1695 -0.0005 -0.0031 -0.0099 180 TYR A CA  
1550 C C   . TYR A 180 ? 0.2213 0.0820 0.2135 0.0002  -0.0027 -0.0129 180 TYR A C   
1551 O O   . TYR A 180 ? 0.2136 0.0719 0.2029 0.0007  -0.0015 -0.0182 180 TYR A O   
1552 C CB  . TYR A 180 ? 0.1757 0.0457 0.1724 0.0039  -0.0020 -0.0126 180 TYR A CB  
1553 C CG  . TYR A 180 ? 0.1681 0.0444 0.1662 0.0005  0.0009  -0.0144 180 TYR A CG  
1554 C CD1 . TYR A 180 ? 0.1846 0.0610 0.1767 -0.0040 0.0099  -0.0205 180 TYR A CD1 
1555 C CD2 . TYR A 180 ? 0.1600 0.0480 0.1638 0.0011  -0.0030 -0.0089 180 TYR A CD2 
1556 C CE1 . TYR A 180 ? 0.1712 0.0514 0.1616 -0.0085 0.0174  -0.0222 180 TYR A CE1 
1557 C CE2 . TYR A 180 ? 0.1518 0.0485 0.1573 -0.0028 0.0022  -0.0114 180 TYR A CE2 
1558 C CZ  . TYR A 180 ? 0.1609 0.0486 0.1591 -0.0083 0.0140  -0.0191 180 TYR A CZ  
1559 O OH  . TYR A 180 ? 0.1628 0.0519 0.1579 -0.0133 0.0227  -0.0219 180 TYR A OH  
1560 N N   . ARG A 181 ? 0.2383 0.0922 0.2319 0.0004  -0.0029 -0.0096 181 ARG A N   
1561 C CA  . ARG A 181 ? 0.2105 0.0539 0.2042 -0.0001 -0.0015 -0.0133 181 ARG A CA  
1562 C C   . ARG A 181 ? 0.3060 0.1487 0.2970 -0.0076 -0.0030 -0.0202 181 ARG A C   
1563 O O   . ARG A 181 ? 0.2221 0.0606 0.2111 -0.0070 -0.0027 -0.0265 181 ARG A O   
1564 C CB  . ARG A 181 ? 0.2278 0.0574 0.2206 0.0010  -0.0005 -0.0083 181 ARG A CB  
1565 C CG  . ARG A 181 ? 0.2345 0.0601 0.2210 0.0141  -0.0011 -0.0022 181 ARG A CG  
1566 C CD  . ARG A 181 ? 0.3499 0.1529 0.3244 0.0171  0.0022  0.0033  181 ARG A CD  
1567 N NE  . ARG A 181 ? 0.4790 0.2738 0.4386 0.0344  0.0024  0.0102  181 ARG A NE  
1568 C CZ  . ARG A 181 ? 0.5318 0.3229 0.4831 0.0362  0.0037  0.0183  181 ARG A CZ  
1569 N NH1 . ARG A 181 ? 0.4491 0.2447 0.4083 0.0200  0.0053  0.0197  181 ARG A NH1 
1570 N NH2 . ARG A 181 ? 0.4830 0.2687 0.4166 0.0564  0.0031  0.0236  181 ARG A NH2 
1571 N N   . GLU A 182 ? 0.2126 0.0584 0.2015 -0.0139 -0.0061 -0.0215 182 GLU A N   
1572 C CA  . GLU A 182 ? 0.2233 0.0678 0.2058 -0.0193 -0.0117 -0.0335 182 GLU A CA  
1573 C C   . GLU A 182 ? 0.2462 0.0896 0.2144 -0.0099 -0.0156 -0.0367 182 GLU A C   
1574 O O   . GLU A 182 ? 0.2658 0.1055 0.2269 -0.0092 -0.0178 -0.0471 182 GLU A O   
1575 C CB  . GLU A 182 ? 0.2254 0.0809 0.2104 -0.0255 -0.0183 -0.0381 182 GLU A CB  
1576 C CG  . GLU A 182 ? 0.2839 0.1632 0.2675 -0.0241 -0.0252 -0.0540 182 GLU A CG  
1577 C CD  . GLU A 182 ? 0.3811 0.2924 0.3747 -0.0278 -0.0300 -0.0625 182 GLU A CD  
1578 O OE1 . GLU A 182 ? 0.3963 0.3367 0.3888 -0.0217 -0.0380 -0.0785 182 GLU A OE1 
1579 O OE2 . GLU A 182 ? 0.3367 0.2477 0.3389 -0.0348 -0.0262 -0.0549 182 GLU A OE2 
1580 N N   . ILE A 183 ? 0.2189 0.0640 0.1801 -0.0026 -0.0143 -0.0291 183 ILE A N   
1581 C CA  . ILE A 183 ? 0.2324 0.0688 0.1720 0.0068  -0.0131 -0.0313 183 ILE A CA  
1582 C C   . ILE A 183 ? 0.2461 0.0807 0.1893 0.0062  -0.0059 -0.0325 183 ILE A C   
1583 O O   . ILE A 183 ? 0.2509 0.0759 0.1752 0.0121  -0.0047 -0.0370 183 ILE A O   
1584 C CB  . ILE A 183 ? 0.2474 0.0812 0.1750 0.0126  -0.0083 -0.0235 183 ILE A CB  
1585 C CG1 . ILE A 183 ? 0.2343 0.0788 0.1811 0.0061  0.0003  -0.0181 183 ILE A CG1 
1586 C CG2 . ILE A 183 ? 0.2868 0.1305 0.2127 0.0162  -0.0168 -0.0231 183 ILE A CG2 
1587 C CD1 . ILE A 183 ? 0.2618 0.1007 0.2014 0.0057  0.0109  -0.0204 183 ILE A CD1 
1588 N N   . LYS A 184 ? 0.2350 0.0774 0.1984 0.0023  -0.0021 -0.0298 184 LYS A N   
1589 C CA  . LYS A 184 ? 0.2406 0.0813 0.2082 0.0035  0.0011  -0.0343 184 LYS A CA  
1590 C C   . LYS A 184 ? 0.3054 0.1396 0.2708 0.0022  -0.0014 -0.0409 184 LYS A C   
1591 O O   . LYS A 184 ? 0.2794 0.1084 0.2355 0.0048  0.0002  -0.0467 184 LYS A O   
1592 C CB  . LYS A 184 ? 0.2218 0.0674 0.2047 0.0049  0.0017  -0.0333 184 LYS A CB  
1593 C CG  . LYS A 184 ? 0.2781 0.1217 0.2613 0.0092  0.0041  -0.0410 184 LYS A CG  
1594 C CD  . LYS A 184 ? 0.3515 0.1959 0.3429 0.0165  0.0043  -0.0424 184 LYS A CD  
1595 C CE  . LYS A 184 ? 0.3340 0.1788 0.3257 0.0250  0.0076  -0.0532 184 LYS A CE  
1596 N NZ  . LYS A 184 ? 0.4959 0.3335 0.4843 0.0235  0.0072  -0.0560 184 LYS A NZ  
1597 N N   . GLU A 185 ? 0.2393 0.0723 0.2123 -0.0031 -0.0037 -0.0417 185 GLU A N   
1598 C CA  . GLU A 185 ? 0.2539 0.0803 0.2281 -0.0078 -0.0041 -0.0516 185 GLU A CA  
1599 C C   . GLU A 185 ? 0.3334 0.1602 0.2907 -0.0074 -0.0094 -0.0636 185 GLU A C   
1600 O O   . GLU A 185 ? 0.3183 0.1429 0.2722 -0.0085 -0.0092 -0.0746 185 GLU A O   
1601 C CB  . GLU A 185 ? 0.2592 0.0816 0.2447 -0.0158 -0.0045 -0.0518 185 GLU A CB  
1602 C CG  . GLU A 185 ? 0.2592 0.0743 0.2496 -0.0106 -0.0021 -0.0401 185 GLU A CG  
1603 C CD  . GLU A 185 ? 0.2669 0.0748 0.2572 -0.0164 -0.0015 -0.0344 185 GLU A CD  
1604 O OE1 . GLU A 185 ? 0.2723 0.0720 0.2597 -0.0094 0.0014  -0.0249 185 GLU A OE1 
1605 O OE2 . GLU A 185 ? 0.2730 0.0824 0.2624 -0.0279 -0.0028 -0.0412 185 GLU A OE2 
1606 N N   . GLU A 186 ? 0.2187 0.1295 0.2375 -0.0385 -0.0786 -0.0252 186 GLU A N   
1607 C CA  . GLU A 186 ? 0.2250 0.1405 0.2458 -0.0395 -0.0879 -0.0269 186 GLU A CA  
1608 C C   . GLU A 186 ? 0.2272 0.1373 0.2302 -0.0315 -0.0884 -0.0301 186 GLU A C   
1609 O O   . GLU A 186 ? 0.2536 0.1665 0.2553 -0.0323 -0.0972 -0.0304 186 GLU A O   
1610 C CB  . GLU A 186 ? 0.2488 0.1882 0.2939 -0.0417 -0.0873 -0.0224 186 GLU A CB  
1611 C CG  . GLU A 186 ? 0.3199 0.2692 0.3836 -0.0526 -0.0895 -0.0191 186 GLU A CG  
1612 C CD  . GLU A 186 ? 0.3672 0.3449 0.4564 -0.0533 -0.0843 -0.0160 186 GLU A CD  
1613 O OE1 . GLU A 186 ? 0.3749 0.3618 0.4672 -0.0445 -0.0783 -0.0168 186 GLU A OE1 
1614 O OE2 . GLU A 186 ? 0.3670 0.3587 0.4738 -0.0629 -0.0861 -0.0132 186 GLU A OE2 
1615 N N   . GLY A 187 ? 0.2369 0.1407 0.2266 -0.0249 -0.0799 -0.0317 187 GLY A N   
1616 C CA  . GLY A 187 ? 0.2524 0.1531 0.2246 -0.0192 -0.0796 -0.0338 187 GLY A CA  
1617 C C   . GLY A 187 ? 0.2809 0.1944 0.2611 -0.0163 -0.0785 -0.0282 187 GLY A C   
1618 O O   . GLY A 187 ? 0.2428 0.1545 0.2097 -0.0141 -0.0814 -0.0276 187 GLY A O   
1619 N N   . LYS A 188 ? 0.2018 0.1284 0.2037 -0.0165 -0.0750 -0.0244 188 LYS A N   
1620 C CA  . LYS A 188 ? 0.2012 0.1387 0.2141 -0.0128 -0.0756 -0.0206 188 LYS A CA  
1621 C C   . LYS A 188 ? 0.1815 0.1193 0.1903 -0.0071 -0.0657 -0.0193 188 LYS A C   
1622 O O   . LYS A 188 ? 0.1783 0.1199 0.1915 -0.0036 -0.0672 -0.0163 188 LYS A O   
1623 C CB  . LYS A 188 ? 0.2039 0.1580 0.2441 -0.0149 -0.0769 -0.0194 188 LYS A CB  
1624 C CG  . LYS A 188 ? 0.1917 0.1486 0.2394 -0.0210 -0.0883 -0.0198 188 LYS A CG  
1625 C CD  . LYS A 188 ? 0.2502 0.2281 0.3271 -0.0234 -0.0882 -0.0191 188 LYS A CD  
1626 C CE  . LYS A 188 ? 0.3691 0.3516 0.4555 -0.0299 -0.1008 -0.0191 188 LYS A CE  
1627 N NZ  . LYS A 188 ? 0.4190 0.4259 0.5362 -0.0292 -0.1030 -0.0188 188 LYS A NZ  
1628 N N   . GLY A 189 ? 0.1908 0.1238 0.1919 -0.0062 -0.0570 -0.0213 189 GLY A N   
1629 C CA  . GLY A 189 ? 0.1836 0.1173 0.1805 -0.0015 -0.0482 -0.0204 189 GLY A CA  
1630 C C   . GLY A 189 ? 0.2201 0.1466 0.2062 -0.0007 -0.0415 -0.0233 189 GLY A C   
1631 O O   . GLY A 189 ? 0.2210 0.1422 0.2073 -0.0037 -0.0431 -0.0253 189 GLY A O   
1632 N N   . SER A 190 ? 0.1776 0.1032 0.1547 0.0033  -0.0352 -0.0232 190 SER A N   
1633 C CA  . SER A 190 ? 0.2263 0.1482 0.1976 0.0058  -0.0284 -0.0257 190 SER A CA  
1634 C C   . SER A 190 ? 0.1981 0.1281 0.1820 0.0066  -0.0220 -0.0232 190 SER A C   
1635 O O   . SER A 190 ? 0.1585 0.0969 0.1518 0.0072  -0.0208 -0.0211 190 SER A O   
1636 C CB  . SER A 190 ? 0.2001 0.1202 0.1564 0.0094  -0.0246 -0.0274 190 SER A CB  
1637 O OG  . SER A 190 ? 0.2658 0.1798 0.2076 0.0086  -0.0296 -0.0311 190 SER A OG  
1638 N N   . VAL A 191 ? 0.1887 0.1155 0.1723 0.0067  -0.0188 -0.0238 191 VAL A N   
1639 C CA  . VAL A 191 ? 0.1569 0.0916 0.1483 0.0071  -0.0126 -0.0215 191 VAL A CA  
1640 C C   . VAL A 191 ? 0.2124 0.1428 0.1952 0.0116  -0.0083 -0.0229 191 VAL A C   
1641 O O   . VAL A 191 ? 0.2435 0.1639 0.2194 0.0131  -0.0104 -0.0253 191 VAL A O   
1642 C CB  . VAL A 191 ? 0.2075 0.1450 0.2076 0.0016  -0.0133 -0.0189 191 VAL A CB  
1643 C CG1 . VAL A 191 ? 0.2175 0.1653 0.2229 0.0017  -0.0066 -0.0167 191 VAL A CG1 
1644 C CG2 . VAL A 191 ? 0.1695 0.1140 0.1803 -0.0030 -0.0178 -0.0183 191 VAL A CG2 
1645 N N   . SER A 192 ? 0.1585 0.0965 0.1431 0.0142  -0.0031 -0.0221 192 SER A N   
1646 C CA  . SER A 192 ? 0.1447 0.0830 0.1245 0.0183  0.0012  -0.0230 192 SER A CA  
1647 C C   . SER A 192 ? 0.1692 0.1134 0.1553 0.0176  0.0044  -0.0205 192 SER A C   
1648 O O   . SER A 192 ? 0.1533 0.1034 0.1466 0.0138  0.0046  -0.0186 192 SER A O   
1649 C CB  . SER A 192 ? 0.1615 0.1048 0.1378 0.0202  0.0039  -0.0234 192 SER A CB  
1650 O OG  . SER A 192 ? 0.1565 0.1070 0.1414 0.0186  0.0051  -0.0212 192 SER A OG  
1651 N N   . THR A 193 ? 0.1822 0.1266 0.1654 0.0212  0.0068  -0.0209 193 THR A N   
1652 C CA  . THR A 193 ? 0.1932 0.1449 0.1805 0.0204  0.0096  -0.0183 193 THR A CA  
1653 C C   . THR A 193 ? 0.1572 0.1152 0.1441 0.0241  0.0130  -0.0197 193 THR A C   
1654 O O   . THR A 193 ? 0.1650 0.1231 0.1487 0.0265  0.0140  -0.0219 193 THR A O   
1655 C CB  . THR A 193 ? 0.1895 0.1348 0.1755 0.0193  0.0067  -0.0151 193 THR A CB  
1656 O OG1 . THR A 193 ? 0.2006 0.1549 0.1891 0.0163  0.0090  -0.0116 193 THR A OG1 
1657 C CG2 . THR A 193 ? 0.2304 0.1675 0.2125 0.0256  0.0046  -0.0170 193 THR A CG2 
1658 N N   . SER A 194 ? 0.1585 0.1235 0.1483 0.0235  0.0148  -0.0181 194 SER A N   
1659 C CA  . SER A 194 ? 0.1804 0.1525 0.1714 0.0258  0.0172  -0.0190 194 SER A CA  
1660 C C   . SER A 194 ? 0.1784 0.1511 0.1688 0.0279  0.0157  -0.0168 194 SER A C   
1661 O O   . SER A 194 ? 0.1743 0.1427 0.1631 0.0257  0.0131  -0.0135 194 SER A O   
1662 C CB  . SER A 194 ? 0.1743 0.1546 0.1699 0.0230  0.0191  -0.0199 194 SER A CB  
1663 O OG  . SER A 194 ? 0.1669 0.1456 0.1646 0.0218  0.0188  -0.0212 194 SER A OG  
1664 N N   . PRO A 195 ? 0.1524 0.1312 0.1449 0.0314  0.0166  -0.0179 195 PRO A N   
1665 C CA  . PRO A 195 ? 0.1538 0.1349 0.1472 0.0332  0.0139  -0.0153 195 PRO A CA  
1666 C C   . PRO A 195 ? 0.1592 0.1433 0.1503 0.0276  0.0133  -0.0118 195 PRO A C   
1667 O O   . PRO A 195 ? 0.1707 0.1608 0.1628 0.0239  0.0163  -0.0139 195 PRO A O   
1668 C CB  . PRO A 195 ? 0.2468 0.2392 0.2451 0.0356  0.0160  -0.0175 195 PRO A CB  
1669 C CG  . PRO A 195 ? 0.3196 0.3134 0.3182 0.0359  0.0196  -0.0208 195 PRO A CG  
1670 C CD  . PRO A 195 ? 0.1934 0.1785 0.1877 0.0327  0.0197  -0.0207 195 PRO A CD  
1671 N N   . TYR A 196 ? 0.1721 0.1523 0.1602 0.0271  0.0090  -0.0067 196 TYR A N   
1672 C CA  . TYR A 196 ? 0.1319 0.1122 0.1151 0.0203  0.0082  -0.0019 196 TYR A CA  
1673 C C   . TYR A 196 ? 0.1260 0.1197 0.1084 0.0156  0.0125  -0.0043 196 TYR A C   
1674 O O   . TYR A 196 ? 0.1487 0.1460 0.1308 0.0111  0.0155  -0.0052 196 TYR A O   
1675 C CB  . TYR A 196 ? 0.1959 0.1706 0.1751 0.0197  0.0016  0.0058  196 TYR A CB  
1676 C CG  . TYR A 196 ? 0.1494 0.1198 0.1228 0.0117  -0.0005 0.0132  196 TYR A CG  
1677 C CD1 . TYR A 196 ? 0.1561 0.1394 0.1243 0.0038  0.0030  0.0155  196 TYR A CD1 
1678 C CD2 . TYR A 196 ? 0.1913 0.1455 0.1644 0.0115  -0.0063 0.0176  196 TYR A CD2 
1679 C CE1 . TYR A 196 ? 0.1840 0.1670 0.1471 -0.0052 0.0019  0.0231  196 TYR A CE1 
1680 C CE2 . TYR A 196 ? 0.1924 0.1429 0.1608 0.0021  -0.0087 0.0258  196 TYR A CE2 
1681 C CZ  . TYR A 196 ? 0.1999 0.1661 0.1632 -0.0066 -0.0042 0.0292  196 TYR A CZ  
1682 O OH  . TYR A 196 ? 0.2362 0.2019 0.1950 -0.0173 -0.0060 0.0383  196 TYR A OH  
1683 N N   . TYR A 197 ? 0.1537 0.1559 0.1360 0.0166  0.0123  -0.0058 197 TYR A N   
1684 C CA  . TYR A 197 ? 0.1244 0.1385 0.1049 0.0124  0.0156  -0.0097 197 TYR A CA  
1685 C C   . TYR A 197 ? 0.1424 0.1596 0.1298 0.0146  0.0184  -0.0175 197 TYR A C   
1686 O O   . TYR A 197 ? 0.1707 0.1964 0.1581 0.0128  0.0194  -0.0224 197 TYR A O   
1687 C CB  . TYR A 197 ? 0.1634 0.1851 0.1375 0.0101  0.0125  -0.0065 197 TYR A CB  
1688 C CG  . TYR A 197 ? 0.1477 0.1666 0.1134 0.0055  0.0092  0.0028  197 TYR A CG  
1689 C CD1 . TYR A 197 ? 0.1413 0.1678 0.1011 -0.0018 0.0128  0.0040  197 TYR A CD1 
1690 C CD2 . TYR A 197 ? 0.2194 0.2278 0.1843 0.0082  0.0021  0.0105  197 TYR A CD2 
1691 C CE1 . TYR A 197 ? 0.1819 0.2058 0.1334 -0.0082 0.0096  0.0145  197 TYR A CE1 
1692 C CE2 . TYR A 197 ? 0.2236 0.2263 0.1807 0.0029  -0.0026 0.0206  197 TYR A CE2 
1693 C CZ  . TYR A 197 ? 0.2065 0.2168 0.1565 -0.0061 0.0013  0.0233  197 TYR A CZ  
1694 O OH  . TYR A 197 ? 0.2717 0.2769 0.2135 -0.0135 -0.0036 0.0351  197 TYR A OH  
1695 N N   . HIS A 198 ? 0.1446 0.1546 0.1371 0.0176  0.0191  -0.0186 198 HIS A N   
1696 C CA  . HIS A 198 ? 0.1452 0.1558 0.1436 0.0183  0.0205  -0.0238 198 HIS A CA  
1697 C C   . HIS A 198 ? 0.1529 0.1697 0.1539 0.0183  0.0192  -0.0255 198 HIS A C   
1698 O O   . HIS A 198 ? 0.1357 0.1557 0.1395 0.0164  0.0191  -0.0305 198 HIS A O   
1699 C CB  . HIS A 198 ? 0.1348 0.1483 0.1357 0.0162  0.0224  -0.0289 198 HIS A CB  
1700 C CG  . HIS A 198 ? 0.1172 0.1261 0.1251 0.0172  0.0220  -0.0326 198 HIS A CG  
1701 N ND1 . HIS A 198 ? 0.1279 0.1384 0.1404 0.0166  0.0206  -0.0376 198 HIS A ND1 
1702 C CD2 . HIS A 198 ? 0.1399 0.1417 0.1507 0.0180  0.0214  -0.0317 198 HIS A CD2 
1703 C CE1 . HIS A 198 ? 0.1630 0.1664 0.1813 0.0171  0.0189  -0.0386 198 HIS A CE1 
1704 N NE2 . HIS A 198 ? 0.1473 0.1462 0.1642 0.0180  0.0194  -0.0351 198 HIS A NE2 
1705 N N   . PRO A 199 ? 0.1293 0.1479 0.1307 0.0206  0.0174  -0.0222 199 PRO A N   
1706 C CA  . PRO A 199 ? 0.2031 0.2297 0.2091 0.0200  0.0158  -0.0236 199 PRO A CA  
1707 C C   . PRO A 199 ? 0.2004 0.2272 0.2130 0.0193  0.0174  -0.0245 199 PRO A C   
1708 O O   . PRO A 199 ? 0.2123 0.2329 0.2244 0.0201  0.0195  -0.0236 199 PRO A O   
1709 C CB  . PRO A 199 ? 0.1824 0.2122 0.1883 0.0236  0.0129  -0.0194 199 PRO A CB  
1710 C CG  . PRO A 199 ? 0.1630 0.1841 0.1678 0.0275  0.0141  -0.0173 199 PRO A CG  
1711 C CD  . PRO A 199 ? 0.1422 0.1559 0.1417 0.0245  0.0161  -0.0178 199 PRO A CD  
1712 N N   . LEU A 200 ? 0.2087 0.2435 0.2268 0.0170  0.0158  -0.0254 200 LEU A N   
1713 C CA  . LEU A 200 ? 0.1805 0.2191 0.2052 0.0147  0.0171  -0.0242 200 LEU A CA  
1714 C C   . LEU A 200 ? 0.1858 0.2340 0.2143 0.0189  0.0184  -0.0220 200 LEU A C   
1715 O O   . LEU A 200 ? 0.1508 0.2105 0.1857 0.0190  0.0163  -0.0219 200 LEU A O   
1716 C CB  . LEU A 200 ? 0.1568 0.1994 0.1871 0.0088  0.0140  -0.0263 200 LEU A CB  
1717 C CG  . LEU A 200 ? 0.2553 0.2869 0.2848 0.0054  0.0123  -0.0298 200 LEU A CG  
1718 C CD1 . LEU A 200 ? 0.3223 0.3561 0.3563 0.0009  0.0078  -0.0341 200 LEU A CD1 
1719 C CD2 . LEU A 200 ? 0.2447 0.2697 0.2760 0.0028  0.0136  -0.0260 200 LEU A CD2 
1720 N N   . ILE A 201 ? 0.1287 0.1729 0.1542 0.0230  0.0214  -0.0212 201 ILE A N   
1721 C CA  . ILE A 201 ? 0.1369 0.1896 0.1666 0.0292  0.0226  -0.0215 201 ILE A CA  
1722 C C   . ILE A 201 ? 0.1623 0.2324 0.2019 0.0269  0.0247  -0.0216 201 ILE A C   
1723 O O   . ILE A 201 ? 0.1622 0.2443 0.2100 0.0317  0.0234  -0.0226 201 ILE A O   
1724 C CB  . ILE A 201 ? 0.1616 0.2061 0.1854 0.0334  0.0254  -0.0226 201 ILE A CB  
1725 C CG1 . ILE A 201 ? 0.1870 0.2162 0.2033 0.0353  0.0224  -0.0219 201 ILE A CG1 
1726 C CG2 . ILE A 201 ? 0.1601 0.2146 0.1895 0.0407  0.0272  -0.0255 201 ILE A CG2 
1727 C CD1 . ILE A 201 ? 0.1783 0.2054 0.1956 0.0410  0.0179  -0.0209 201 ILE A CD1 
1728 N N   . PRO A 202 ? 0.1228 0.1959 0.1633 0.0193  0.0273  -0.0199 202 PRO A N   
1729 C CA  . PRO A 202 ? 0.1171 0.2098 0.1680 0.0157  0.0297  -0.0189 202 PRO A CA  
1730 C C   . PRO A 202 ? 0.1171 0.2202 0.1777 0.0143  0.0251  -0.0192 202 PRO A C   
1731 O O   . PRO A 202 ? 0.1462 0.2687 0.2182 0.0160  0.0262  -0.0199 202 PRO A O   
1732 C CB  . PRO A 202 ? 0.1220 0.2110 0.1699 0.0055  0.0312  -0.0149 202 PRO A CB  
1733 C CG  . PRO A 202 ? 0.1644 0.2359 0.2003 0.0078  0.0319  -0.0149 202 PRO A CG  
1734 C CD  . PRO A 202 ? 0.1455 0.2058 0.1782 0.0145  0.0284  -0.0181 202 PRO A CD  
1735 N N   . ILE A 203 ? 0.1286 0.2209 0.1855 0.0112  0.0198  -0.0196 203 ILE A N   
1736 C CA  . ILE A 203 ? 0.1078 0.2094 0.1718 0.0095  0.0143  -0.0204 203 ILE A CA  
1737 C C   . ILE A 203 ? 0.1552 0.2626 0.2214 0.0187  0.0115  -0.0211 203 ILE A C   
1738 O O   . ILE A 203 ? 0.1443 0.2679 0.2216 0.0199  0.0086  -0.0212 203 ILE A O   
1739 C CB  . ILE A 203 ? 0.1557 0.2450 0.2136 0.0044  0.0095  -0.0225 203 ILE A CB  
1740 C CG1 . ILE A 203 ? 0.2071 0.2917 0.2677 -0.0049 0.0096  -0.0216 203 ILE A CG1 
1741 C CG2 . ILE A 203 ? 0.1693 0.2679 0.2313 0.0035  0.0030  -0.0241 203 ILE A CG2 
1742 C CD1 . ILE A 203 ? 0.2217 0.2920 0.2772 -0.0083 0.0049  -0.0260 203 ILE A CD1 
1743 N N   . LEU A 204 ? 0.1272 0.2213 0.1838 0.0250  0.0114  -0.0211 204 LEU A N   
1744 C CA  . LEU A 204 ? 0.1428 0.2386 0.2012 0.0334  0.0070  -0.0203 204 LEU A CA  
1745 C C   . LEU A 204 ? 0.1330 0.2439 0.2044 0.0404  0.0090  -0.0221 204 LEU A C   
1746 O O   . LEU A 204 ? 0.1292 0.2501 0.2101 0.0461  0.0037  -0.0220 204 LEU A O   
1747 C CB  . LEU A 204 ? 0.1128 0.1905 0.1591 0.0372  0.0064  -0.0190 204 LEU A CB  
1748 C CG  . LEU A 204 ? 0.1423 0.2084 0.1764 0.0316  0.0051  -0.0180 204 LEU A CG  
1749 C CD1 . LEU A 204 ? 0.1663 0.2180 0.1912 0.0353  0.0044  -0.0156 204 LEU A CD1 
1750 C CD2 . LEU A 204 ? 0.1549 0.2274 0.1877 0.0282  -0.0010 -0.0173 204 LEU A CD2 
1751 N N   . LEU A 205 ? 0.1350 0.2494 0.2076 0.0402  0.0165  -0.0241 205 LEU A N   
1752 C CA  . LEU A 205 ? 0.1207 0.2526 0.2055 0.0474  0.0200  -0.0278 205 LEU A CA  
1753 C C   . LEU A 205 ? 0.1225 0.2797 0.2228 0.0428  0.0210  -0.0278 205 LEU A C   
1754 O O   . LEU A 205 ? 0.1816 0.3577 0.2969 0.0501  0.0205  -0.0310 205 LEU A O   
1755 C CB  . LEU A 205 ? 0.1372 0.2664 0.2155 0.0477  0.0281  -0.0304 205 LEU A CB  
1756 C CG  . LEU A 205 ? 0.1598 0.2675 0.2265 0.0543  0.0268  -0.0320 205 LEU A CG  
1757 C CD1 . LEU A 205 ? 0.1482 0.2539 0.2066 0.0522  0.0341  -0.0342 205 LEU A CD1 
1758 C CD2 . LEU A 205 ? 0.1609 0.2694 0.2355 0.0673  0.0224  -0.0362 205 LEU A CD2 
1759 N N   . ASN A 206 ? 0.1235 0.2822 0.2221 0.0306  0.0221  -0.0246 206 ASN A N   
1760 C CA  . ASN A 206 ? 0.1261 0.3092 0.2397 0.0238  0.0235  -0.0237 206 ASN A CA  
1761 C C   . ASN A 206 ? 0.1512 0.3263 0.2609 0.0108  0.0199  -0.0199 206 ASN A C   
1762 O O   . ASN A 206 ? 0.1421 0.3119 0.2465 0.0020  0.0238  -0.0171 206 ASN A O   
1763 C CB  . ASN A 206 ? 0.1585 0.3588 0.2766 0.0222  0.0335  -0.0248 206 ASN A CB  
1764 C CG  . ASN A 206 ? 0.2409 0.4694 0.3753 0.0133  0.0356  -0.0228 206 ASN A CG  
1765 O OD1 . ASN A 206 ? 0.1960 0.4327 0.3413 0.0108  0.0289  -0.0219 206 ASN A OD1 
1766 N ND2 . ASN A 206 ? 0.3108 0.5483 0.4434 0.0072  0.0437  -0.0209 206 ASN A ND2 
1767 N N   . PRO A 207 ? 0.1327 0.3056 0.2442 0.0094  0.0116  -0.0200 207 PRO A N   
1768 C CA  . PRO A 207 ? 0.1372 0.3000 0.2444 -0.0021 0.0074  -0.0188 207 PRO A CA  
1769 C C   . PRO A 207 ? 0.1362 0.3118 0.2535 -0.0141 0.0096  -0.0157 207 PRO A C   
1770 O O   . PRO A 207 ? 0.1714 0.3334 0.2838 -0.0238 0.0072  -0.0142 207 PRO A O   
1771 C CB  . PRO A 207 ? 0.1987 0.3647 0.3084 -0.0008 -0.0019 -0.0206 207 PRO A CB  
1772 C CG  . PRO A 207 ? 0.1971 0.3618 0.3040 0.0118  -0.0031 -0.0211 207 PRO A CG  
1773 C CD  . PRO A 207 ? 0.1453 0.3208 0.2600 0.0183  0.0045  -0.0214 207 PRO A CD  
1774 N N   . ASN A 208 ? 0.1270 0.3291 0.2594 -0.0142 0.0136  -0.0147 208 ASN A N   
1775 C CA  . ASN A 208 ? 0.1224 0.3403 0.2652 -0.0276 0.0163  -0.0102 208 ASN A CA  
1776 C C   . ASN A 208 ? 0.1341 0.3405 0.2660 -0.0344 0.0226  -0.0056 208 ASN A C   
1777 O O   . ASN A 208 ? 0.1219 0.3349 0.2586 -0.0481 0.0233  0.0003  208 ASN A O   
1778 C CB  . ASN A 208 ? 0.1531 0.4066 0.3152 -0.0253 0.0212  -0.0108 208 ASN A CB  
1779 C CG  . ASN A 208 ? 0.2536 0.5243 0.4325 -0.0257 0.0129  -0.0125 208 ASN A CG  
1780 O OD1 . ASN A 208 ? 0.2930 0.5483 0.4664 -0.0257 0.0034  -0.0139 208 ASN A OD1 
1781 N ND2 . ASN A 208 ? 0.3036 0.5962 0.4968 -0.0251 0.0159  -0.0120 208 ASN A ND2 
1782 N N   . CYS A 209 ? 0.1468 0.3357 0.2641 -0.0262 0.0260  -0.0073 209 CYS A N   
1783 C CA  . CYS A 209 ? 0.2159 0.3940 0.3224 -0.0328 0.0305  -0.0024 209 CYS A CA  
1784 C C   . CYS A 209 ? 0.2146 0.3698 0.3157 -0.0434 0.0233  0.0014  209 CYS A C   
1785 O O   . CYS A 209 ? 0.1743 0.3223 0.2698 -0.0522 0.0247  0.0078  209 CYS A O   
1786 C CB  . CYS A 209 ? 0.2095 0.3746 0.3024 -0.0215 0.0347  -0.0057 209 CYS A CB  
1787 S SG  . CYS A 209 ? 0.2307 0.3637 0.3105 -0.0146 0.0281  -0.0093 209 CYS A SG  
1788 N N   . VAL A 210 ? 0.1311 0.2755 0.2341 -0.0430 0.0150  -0.0026 210 VAL A N   
1789 C CA  . VAL A 210 ? 0.1924 0.3152 0.2924 -0.0518 0.0073  -0.0015 210 VAL A CA  
1790 C C   . VAL A 210 ? 0.1904 0.3213 0.3004 -0.0678 0.0049  0.0060  210 VAL A C   
1791 O O   . VAL A 210 ? 0.1948 0.3064 0.3018 -0.0767 -0.0005 0.0099  210 VAL A O   
1792 C CB  . VAL A 210 ? 0.2468 0.3605 0.3462 -0.0474 -0.0003 -0.0095 210 VAL A CB  
1793 C CG1 . VAL A 210 ? 0.3225 0.4153 0.4208 -0.0552 -0.0087 -0.0112 210 VAL A CG1 
1794 C CG2 . VAL A 210 ? 0.2852 0.3899 0.3733 -0.0341 0.0021  -0.0146 210 VAL A CG2 
1795 N N   . TYR A 211 ? 0.1424 0.3022 0.2653 -0.0721 0.0085  0.0086  211 TYR A N   
1796 C CA  . TYR A 211 ? 0.1705 0.3414 0.3043 -0.0892 0.0064  0.0168  211 TYR A CA  
1797 C C   . TYR A 211 ? 0.1503 0.3235 0.2781 -0.0982 0.0128  0.0269  211 TYR A C   
1798 O O   . TYR A 211 ? 0.2173 0.3954 0.3514 -0.1148 0.0103  0.0362  211 TYR A O   
1799 C CB  . TYR A 211 ? 0.1380 0.3433 0.2897 -0.0910 0.0085  0.0159  211 TYR A CB  
1800 C CG  . TYR A 211 ? 0.1576 0.3635 0.3157 -0.0846 0.0005  0.0076  211 TYR A CG  
1801 C CD1 . TYR A 211 ? 0.1761 0.3654 0.3358 -0.0926 -0.0110 0.0056  211 TYR A CD1 
1802 C CD2 . TYR A 211 ? 0.1749 0.3986 0.3379 -0.0710 0.0035  0.0019  211 TYR A CD2 
1803 C CE1 . TYR A 211 ? 0.2039 0.3958 0.3676 -0.0877 -0.0186 -0.0021 211 TYR A CE1 
1804 C CE2 . TYR A 211 ? 0.1659 0.3910 0.3335 -0.0661 -0.0049 -0.0041 211 TYR A CE2 
1805 C CZ  . TYR A 211 ? 0.2151 0.4250 0.3818 -0.0748 -0.0155 -0.0061 211 TYR A CZ  
1806 O OH  . TYR A 211 ? 0.2092 0.4220 0.3783 -0.0706 -0.0241 -0.0122 211 TYR A OH  
1807 N N   . GLU A 212 ? 0.1598 0.3296 0.2750 -0.0886 0.0202  0.0259  212 GLU A N   
1808 C CA  . GLU A 212 ? 0.2109 0.3840 0.3175 -0.0969 0.0262  0.0354  212 GLU A CA  
1809 C C   . GLU A 212 ? 0.2226 0.3656 0.3216 -0.1080 0.0171  0.0436  212 GLU A C   
1810 O O   . GLU A 212 ? 0.2428 0.3903 0.3412 -0.1236 0.0171  0.0556  212 GLU A O   
1811 C CB  . GLU A 212 ? 0.2451 0.4201 0.3393 -0.0830 0.0349  0.0305  212 GLU A CB  
1812 C CG  . GLU A 212 ? 0.2621 0.4699 0.3654 -0.0738 0.0444  0.0237  212 GLU A CG  
1813 C CD  . GLU A 212 ? 0.3109 0.5158 0.4032 -0.0579 0.0506  0.0162  212 GLU A CD  
1814 O OE1 . GLU A 212 ? 0.3438 0.5643 0.4443 -0.0456 0.0539  0.0077  212 GLU A OE1 
1815 O OE2 . GLU A 212 ? 0.2737 0.4604 0.3501 -0.0576 0.0511  0.0187  212 GLU A OE2 
1816 N N   . THR A 213 ? 0.1976 0.3105 0.2916 -0.1005 0.0088  0.0375  213 THR A N   
1817 C CA  . THR A 213 ? 0.2244 0.3068 0.3144 -0.1086 -0.0018 0.0430  213 THR A CA  
1818 C C   . THR A 213 ? 0.2828 0.3523 0.3842 -0.1153 -0.0135 0.0401  213 THR A C   
1819 O O   . THR A 213 ? 0.3218 0.3725 0.4251 -0.1274 -0.0230 0.0477  213 THR A O   
1820 C CB  . THR A 213 ? 0.2300 0.2878 0.3082 -0.0955 -0.0036 0.0371  213 THR A CB  
1821 O OG1 . THR A 213 ? 0.3534 0.4122 0.4331 -0.0814 -0.0024 0.0241  213 THR A OG1 
1822 C CG2 . THR A 213 ? 0.2582 0.3228 0.3237 -0.0922 0.0050  0.0418  213 THR A CG2 
1823 N N   . THR A 214 ? 0.1897 0.2680 0.2983 -0.1081 -0.0142 0.0295  214 THR A N   
1824 C CA  . THR A 214 ? 0.1905 0.2578 0.3088 -0.1140 -0.0257 0.0246  214 THR A CA  
1825 C C   . THR A 214 ? 0.2521 0.3491 0.3834 -0.1187 -0.0235 0.0240  214 THR A C   
1826 O O   . THR A 214 ? 0.2347 0.3402 0.3682 -0.1090 -0.0235 0.0140  214 THR A O   
1827 C CB  . THR A 214 ? 0.2137 0.2604 0.3263 -0.1006 -0.0306 0.0108  214 THR A CB  
1828 O OG1 . THR A 214 ? 0.2322 0.2937 0.3394 -0.0863 -0.0221 0.0038  214 THR A OG1 
1829 C CG2 . THR A 214 ? 0.2503 0.2684 0.3542 -0.0972 -0.0344 0.0115  214 THR A CG2 
1830 N N   . PRO A 215 ? 0.2136 0.3285 0.3542 -0.1343 -0.0221 0.0351  215 PRO A N   
1831 C CA  . PRO A 215 ? 0.1998 0.3460 0.3535 -0.1359 -0.0183 0.0338  215 PRO A CA  
1832 C C   . PRO A 215 ? 0.2549 0.3962 0.4181 -0.1380 -0.0292 0.0259  215 PRO A C   
1833 O O   . PRO A 215 ? 0.2705 0.4367 0.4442 -0.1352 -0.0275 0.0221  215 PRO A O   
1834 C CB  . PRO A 215 ? 0.2288 0.3845 0.3832 -0.1471 -0.0138 0.0454  215 PRO A CB  
1835 C CG  . PRO A 215 ? 0.2758 0.3983 0.4198 -0.1546 -0.0211 0.0525  215 PRO A CG  
1836 C CD  . PRO A 215 ? 0.2766 0.3792 0.4108 -0.1446 -0.0225 0.0472  215 PRO A CD  
1837 N N   . ASN A 216 ? 0.2664 0.3762 0.4260 -0.1417 -0.0407 0.0225  216 ASN A N   
1838 C CA  . ASN A 216 ? 0.3411 0.4437 0.5074 -0.1441 -0.0515 0.0137  216 ASN A CA  
1839 C C   . ASN A 216 ? 0.3124 0.4059 0.4738 -0.1332 -0.0569 0.0002  216 ASN A C   
1840 O O   . ASN A 216 ? 0.4316 0.5162 0.5946 -0.1337 -0.0662 -0.0095 216 ASN A O   
1841 C CB  . ASN A 216 ? 0.3547 0.4283 0.5193 -0.1535 -0.0609 0.0160  216 ASN A CB  
1842 C CG  . ASN A 216 ? 0.4419 0.5252 0.6113 -0.1663 -0.0576 0.0300  216 ASN A CG  
1843 O OD1 . ASN A 216 ? 0.4805 0.5941 0.6594 -0.1701 -0.0513 0.0340  216 ASN A OD1 
1844 N ND2 . ASN A 216 ? 0.4922 0.5503 0.6549 -0.1724 -0.0623 0.0375  216 ASN A ND2 
1845 N N   . VAL A 217 ? 0.3361 0.4287 0.4853 -0.1181 -0.0481 -0.0029 217 VAL A N   
1846 C CA  . VAL A 217 ? 0.3128 0.3946 0.4515 -0.1040 -0.0498 -0.0162 217 VAL A CA  
1847 C C   . VAL A 217 ? 0.2950 0.4008 0.4386 -0.1000 -0.0503 -0.0211 217 VAL A C   
1848 O O   . VAL A 217 ? 0.2572 0.3902 0.4119 -0.1033 -0.0461 -0.0147 217 VAL A O   
1849 C CB  . VAL A 217 ? 0.3035 0.3780 0.4285 -0.0905 -0.0405 -0.0165 217 VAL A CB  
1850 C CG1 . VAL A 217 ? 0.2473 0.3479 0.3729 -0.0835 -0.0296 -0.0119 217 VAL A CG1 
1851 C CG2 . VAL A 217 ? 0.3756 0.4343 0.4895 -0.0791 -0.0433 -0.0293 217 VAL A CG2 
1852 N N   . LYS A 218 ? 0.2459 0.3429 0.3818 -0.0933 -0.0562 -0.0329 218 LYS A N   
1853 C CA  . LYS A 218 ? 0.2320 0.3482 0.3688 -0.0885 -0.0584 -0.0377 218 LYS A CA  
1854 C C   . LYS A 218 ? 0.2481 0.3618 0.3694 -0.0731 -0.0522 -0.0421 218 LYS A C   
1855 O O   . LYS A 218 ? 0.2396 0.3332 0.3483 -0.0679 -0.0524 -0.0492 218 LYS A O   
1856 C CB  . LYS A 218 ? 0.3198 0.4298 0.4583 -0.0953 -0.0713 -0.0473 218 LYS A CB  
1857 C CG  . LYS A 218 ? 0.4692 0.5996 0.6258 -0.1079 -0.0779 -0.0429 218 LYS A CG  
1858 C CD  . LYS A 218 ? 0.5699 0.7033 0.7401 -0.1205 -0.0751 -0.0309 218 LYS A CD  
1859 C CE  . LYS A 218 ? 0.6360 0.7859 0.8224 -0.1309 -0.0793 -0.0278 218 LYS A CE  
1860 N NZ  . LYS A 218 ? 0.6686 0.8225 0.8636 -0.1400 -0.0724 -0.0155 218 LYS A NZ  
1861 N N   . ILE A 219 ? 0.2421 0.3764 0.3656 -0.0661 -0.0470 -0.0378 219 ILE A N   
1862 C CA  . ILE A 219 ? 0.2184 0.3503 0.3281 -0.0528 -0.0421 -0.0398 219 ILE A CA  
1863 C C   . ILE A 219 ? 0.2004 0.3500 0.3116 -0.0488 -0.0474 -0.0410 219 ILE A C   
1864 O O   . ILE A 219 ? 0.2017 0.3686 0.3270 -0.0551 -0.0530 -0.0394 219 ILE A O   
1865 C CB  . ILE A 219 ? 0.2117 0.3462 0.3213 -0.0462 -0.0312 -0.0327 219 ILE A CB  
1866 C CG1 . ILE A 219 ? 0.2607 0.4213 0.3862 -0.0468 -0.0280 -0.0261 219 ILE A CG1 
1867 C CG2 . ILE A 219 ? 0.2280 0.3442 0.3345 -0.0506 -0.0275 -0.0306 219 ILE A CG2 
1868 C CD1 . ILE A 219 ? 0.2353 0.3995 0.3580 -0.0370 -0.0180 -0.0223 219 ILE A CD1 
1869 N N   . PRO A 220 ? 0.2381 0.3840 0.3349 -0.0394 -0.0467 -0.0432 220 PRO A N   
1870 C CA  . PRO A 220 ? 0.2225 0.3837 0.3194 -0.0361 -0.0537 -0.0428 220 PRO A CA  
1871 C C   . PRO A 220 ? 0.2025 0.3835 0.3141 -0.0304 -0.0514 -0.0353 220 PRO A C   
1872 O O   . PRO A 220 ? 0.1924 0.3769 0.3127 -0.0286 -0.0431 -0.0311 220 PRO A O   
1873 C CB  . PRO A 220 ? 0.2450 0.3947 0.3206 -0.0292 -0.0532 -0.0458 220 PRO A CB  
1874 C CG  . PRO A 220 ? 0.2527 0.3847 0.3204 -0.0268 -0.0444 -0.0471 220 PRO A CG  
1875 C CD  . PRO A 220 ? 0.2694 0.3961 0.3487 -0.0339 -0.0423 -0.0472 220 PRO A CD  
1876 N N   . ASP A 221 ? 0.1989 0.3940 0.3137 -0.0273 -0.0595 -0.0342 221 ASP A N   
1877 C CA  . ASP A 221 ? 0.2536 0.4686 0.3844 -0.0199 -0.0595 -0.0286 221 ASP A CA  
1878 C C   . ASP A 221 ? 0.2907 0.4956 0.4104 -0.0077 -0.0552 -0.0253 221 ASP A C   
1879 O O   . ASP A 221 ? 0.3329 0.5308 0.4384 -0.0039 -0.0613 -0.0243 221 ASP A O   
1880 C CB  . ASP A 221 ? 0.2520 0.4850 0.3918 -0.0216 -0.0721 -0.0284 221 ASP A CB  
1881 C CG  . ASP A 221 ? 0.4782 0.7286 0.6318 -0.0104 -0.0749 -0.0234 221 ASP A CG  
1882 O OD1 . ASP A 221 ? 0.5077 0.7664 0.6748 -0.0044 -0.0663 -0.0215 221 ASP A OD1 
1883 O OD2 . ASP A 221 ? 0.5029 0.7591 0.6544 -0.0074 -0.0864 -0.0217 221 ASP A OD2 
1884 N N   . PHE A 222 ? 0.2056 0.4095 0.3309 -0.0026 -0.0453 -0.0234 222 PHE A N   
1885 C CA  . PHE A 222 ? 0.1710 0.3651 0.2885 0.0087  -0.0416 -0.0207 222 PHE A CA  
1886 C C   . PHE A 222 ? 0.2212 0.4316 0.3535 0.0188  -0.0475 -0.0179 222 PHE A C   
1887 O O   . PHE A 222 ? 0.1886 0.4094 0.3350 0.0261  -0.0422 -0.0180 222 PHE A O   
1888 C CB  . PHE A 222 ? 0.1295 0.3158 0.2463 0.0100  -0.0297 -0.0211 222 PHE A CB  
1889 C CG  . PHE A 222 ? 0.1480 0.3128 0.2475 0.0042  -0.0255 -0.0232 222 PHE A CG  
1890 C CD1 . PHE A 222 ? 0.1741 0.3364 0.2746 -0.0067 -0.0254 -0.0259 222 PHE A CD1 
1891 C CD2 . PHE A 222 ? 0.1999 0.3470 0.2839 0.0096  -0.0225 -0.0225 222 PHE A CD2 
1892 C CE1 . PHE A 222 ? 0.1671 0.3094 0.2540 -0.0103 -0.0227 -0.0288 222 PHE A CE1 
1893 C CE2 . PHE A 222 ? 0.1670 0.2971 0.2379 0.0052  -0.0187 -0.0251 222 PHE A CE2 
1894 C CZ  . PHE A 222 ? 0.2056 0.3332 0.2784 -0.0039 -0.0189 -0.0287 222 PHE A CZ  
1895 N N   . ALA A 223 ? 0.2069 0.4195 0.3352 0.0195  -0.0592 -0.0157 223 ALA A N   
1896 C CA  . ALA A 223 ? 0.2229 0.4504 0.3662 0.0286  -0.0684 -0.0125 223 ALA A CA  
1897 C C   . ALA A 223 ? 0.2087 0.4220 0.3451 0.0407  -0.0703 -0.0083 223 ALA A C   
1898 O O   . ALA A 223 ? 0.2645 0.4834 0.4083 0.0484  -0.0813 -0.0043 223 ALA A O   
1899 C CB  . ALA A 223 ? 0.2057 0.4411 0.3466 0.0233  -0.0823 -0.0110 223 ALA A CB  
1900 N N   . VAL A 224 ? 0.1899 0.3843 0.3133 0.0423  -0.0610 -0.0087 224 VAL A N   
1901 C CA  . VAL A 224 ? 0.1632 0.3419 0.2807 0.0526  -0.0626 -0.0049 224 VAL A CA  
1902 C C   . VAL A 224 ? 0.1483 0.3192 0.2657 0.0552  -0.0494 -0.0090 224 VAL A C   
1903 O O   . VAL A 224 ? 0.1977 0.3687 0.3113 0.0471  -0.0403 -0.0125 224 VAL A O   
1904 C CB  . VAL A 224 ? 0.2508 0.4096 0.3430 0.0484  -0.0686 0.0013  224 VAL A CB  
1905 C CG1 . VAL A 224 ? 0.3041 0.4495 0.3783 0.0397  -0.0582 -0.0017 224 VAL A CG1 
1906 C CG2 . VAL A 224 ? 0.3196 0.4637 0.4089 0.0581  -0.0747 0.0077  224 VAL A CG2 
1907 N N   . SER A 225 ? 0.1356 0.2988 0.2572 0.0665  -0.0496 -0.0087 225 SER A N   
1908 C CA  . SER A 225 ? 0.1454 0.3011 0.2652 0.0692  -0.0380 -0.0132 225 SER A CA  
1909 C C   . SER A 225 ? 0.1671 0.2968 0.2642 0.0653  -0.0356 -0.0100 225 SER A C   
1910 O O   . SER A 225 ? 0.1758 0.2910 0.2629 0.0672  -0.0438 -0.0040 225 SER A O   
1911 C CB  . SER A 225 ? 0.1415 0.3017 0.2775 0.0838  -0.0390 -0.0170 225 SER A CB  
1912 O OG  . SER A 225 ? 0.1520 0.3043 0.2834 0.0858  -0.0283 -0.0219 225 SER A OG  
1913 N N   . PHE A 226 ? 0.1261 0.2508 0.2158 0.0594  -0.0249 -0.0132 226 PHE A N   
1914 C CA  . PHE A 226 ? 0.1424 0.2456 0.2145 0.0567  -0.0212 -0.0116 226 PHE A CA  
1915 C C   . PHE A 226 ? 0.1734 0.2697 0.2477 0.0635  -0.0149 -0.0154 226 PHE A C   
1916 O O   . PHE A 226 ? 0.1732 0.2537 0.2351 0.0607  -0.0109 -0.0149 226 PHE A O   
1917 C CB  . PHE A 226 ? 0.1452 0.2461 0.2071 0.0454  -0.0155 -0.0129 226 PHE A CB  
1918 C CG  . PHE A 226 ? 0.1711 0.2736 0.2250 0.0384  -0.0216 -0.0108 226 PHE A CG  
1919 C CD1 . PHE A 226 ? 0.1642 0.2541 0.2018 0.0361  -0.0250 -0.0067 226 PHE A CD1 
1920 C CD2 . PHE A 226 ? 0.2213 0.3388 0.2832 0.0332  -0.0236 -0.0131 226 PHE A CD2 
1921 C CE1 . PHE A 226 ? 0.2439 0.3375 0.2720 0.0293  -0.0297 -0.0061 226 PHE A CE1 
1922 C CE2 . PHE A 226 ? 0.3019 0.4208 0.3550 0.0268  -0.0297 -0.0128 226 PHE A CE2 
1923 C CZ  . PHE A 226 ? 0.2184 0.3258 0.2538 0.0252  -0.0324 -0.0097 226 PHE A CZ  
1924 N N   . ARG A 227 ? 0.1381 0.2478 0.2286 0.0724  -0.0139 -0.0201 227 ARG A N   
1925 C CA  . ARG A 227 ? 0.1336 0.2395 0.2250 0.0783  -0.0068 -0.0259 227 ARG A CA  
1926 C C   . ARG A 227 ? 0.1740 0.2559 0.2566 0.0844  -0.0118 -0.0243 227 ARG A C   
1927 O O   . ARG A 227 ? 0.1712 0.2410 0.2448 0.0836  -0.0064 -0.0268 227 ARG A O   
1928 C CB  . ARG A 227 ? 0.1655 0.2947 0.2769 0.0871  -0.0040 -0.0329 227 ARG A CB  
1929 C CG  . ARG A 227 ? 0.2352 0.3888 0.3552 0.0786  0.0026  -0.0338 227 ARG A CG  
1930 C CD  . ARG A 227 ? 0.2636 0.4340 0.3977 0.0819  0.0066  -0.0382 227 ARG A CD  
1931 N NE  . ARG A 227 ? 0.3171 0.4792 0.4453 0.0858  0.0133  -0.0433 227 ARG A NE  
1932 C CZ  . ARG A 227 ? 0.3778 0.5434 0.4984 0.0793  0.0233  -0.0451 227 ARG A CZ  
1933 N NH1 . ARG A 227 ? 0.3124 0.4884 0.4311 0.0681  0.0280  -0.0415 227 ARG A NH1 
1934 N NH2 . ARG A 227 ? 0.4632 0.6219 0.5779 0.0834  0.0278  -0.0503 227 ARG A NH2 
1935 N N   . GLU A 228 ? 0.1856 0.2597 0.2705 0.0896  -0.0232 -0.0195 228 GLU A N   
1936 C CA  . GLU A 228 ? 0.2090 0.2582 0.2855 0.0935  -0.0296 -0.0163 228 GLU A CA  
1937 C C   . GLU A 228 ? 0.1597 0.1933 0.2166 0.0819  -0.0273 -0.0100 228 GLU A C   
1938 O O   . GLU A 228 ? 0.2124 0.2288 0.2615 0.0819  -0.0263 -0.0102 228 GLU A O   
1939 C CB  . GLU A 228 ? 0.3012 0.3448 0.3843 0.1002  -0.0441 -0.0103 228 GLU A CB  
1940 C CG  . GLU A 228 ? 0.5555 0.5885 0.6234 0.0905  -0.0519 0.0020  228 GLU A CG  
1941 C CD  . GLU A 228 ? 0.6741 0.7259 0.7435 0.0845  -0.0540 0.0051  228 GLU A CD  
1942 O OE1 . GLU A 228 ? 0.6492 0.7189 0.7230 0.0803  -0.0451 -0.0008 228 GLU A OE1 
1943 O OE2 . GLU A 228 ? 0.6573 0.7051 0.7227 0.0833  -0.0657 0.0139  228 GLU A OE2 
1944 N N   . ASP A 229 ? 0.1790 0.2200 0.2288 0.0719  -0.0261 -0.0058 229 ASP A N   
1945 C CA  . ASP A 229 ? 0.1625 0.1932 0.1959 0.0617  -0.0225 -0.0021 229 ASP A CA  
1946 C C   . ASP A 229 ? 0.1701 0.1983 0.2009 0.0596  -0.0123 -0.0079 229 ASP A C   
1947 O O   . ASP A 229 ? 0.1685 0.1830 0.1894 0.0559  -0.0107 -0.0061 229 ASP A O   
1948 C CB  . ASP A 229 ? 0.1650 0.2067 0.1930 0.0530  -0.0226 0.0002  229 ASP A CB  
1949 C CG  . ASP A 229 ? 0.2341 0.2734 0.2562 0.0515  -0.0333 0.0086  229 ASP A CG  
1950 O OD1 . ASP A 229 ? 0.2518 0.2792 0.2746 0.0569  -0.0413 0.0140  229 ASP A OD1 
1951 O OD2 . ASP A 229 ? 0.2460 0.2942 0.2616 0.0446  -0.0346 0.0100  229 ASP A OD2 
1952 N N   . ALA A 230 ? 0.1336 0.1757 0.1732 0.0611  -0.0059 -0.0142 230 ALA A N   
1953 C CA  . ALA A 230 ? 0.1241 0.1635 0.1601 0.0588  0.0025  -0.0185 230 ALA A CA  
1954 C C   . ALA A 230 ? 0.1920 0.2169 0.2251 0.0650  0.0017  -0.0207 230 ALA A C   
1955 O O   . ALA A 230 ? 0.1836 0.1971 0.2076 0.0609  0.0044  -0.0204 230 ALA A O   
1956 C CB  . ALA A 230 ? 0.1739 0.2319 0.2196 0.0589  0.0087  -0.0233 230 ALA A CB  
1957 N N   . SER A 231 ? 0.1761 0.2011 0.2181 0.0751  -0.0030 -0.0234 231 SER A N   
1958 C CA  . SER A 231 ? 0.1469 0.1562 0.1873 0.0821  -0.0055 -0.0272 231 SER A CA  
1959 C C   . SER A 231 ? 0.2136 0.2013 0.2434 0.0772  -0.0119 -0.0197 231 SER A C   
1960 O O   . SER A 231 ? 0.2059 0.1798 0.2287 0.0758  -0.0110 -0.0211 231 SER A O   
1961 C CB  . SER A 231 ? 0.2415 0.2540 0.2954 0.0943  -0.0111 -0.0319 231 SER A CB  
1962 O OG  . SER A 231 ? 0.4100 0.4370 0.4694 0.0950  -0.0028 -0.0395 231 SER A OG  
1963 N N   . LYS A 232 ? 0.1850 0.1712 0.2129 0.0736  -0.0185 -0.0112 232 LYS A N   
1964 C CA  . LYS A 232 ? 0.2345 0.2036 0.2516 0.0669  -0.0242 -0.0023 232 LYS A CA  
1965 C C   . LYS A 232 ? 0.1853 0.1534 0.1922 0.0569  -0.0168 -0.0016 232 LYS A C   
1966 O O   . LYS A 232 ? 0.2213 0.1749 0.2218 0.0531  -0.0188 0.0015  232 LYS A O   
1967 C CB  . LYS A 232 ? 0.2330 0.2052 0.2477 0.0632  -0.0316 0.0070  232 LYS A CB  
1968 C CG  . LYS A 232 ? 0.4509 0.4153 0.4733 0.0718  -0.0439 0.0107  232 LYS A CG  
1969 C CD  . LYS A 232 ? 0.5259 0.4885 0.5400 0.0648  -0.0526 0.0232  232 LYS A CD  
1970 C CE  . LYS A 232 ? 0.6009 0.5458 0.6012 0.0552  -0.0560 0.0330  232 LYS A CE  
1971 N NZ  . LYS A 232 ? 0.6450 0.5838 0.6376 0.0499  -0.0679 0.0470  232 LYS A NZ  
1972 N N   . HIS A 233 ? 0.1442 0.1271 0.1505 0.0522  -0.0092 -0.0042 233 HIS A N   
1973 C CA  . HIS A 233 ? 0.1688 0.1504 0.1680 0.0445  -0.0031 -0.0048 233 HIS A CA  
1974 C C   . HIS A 233 ? 0.1599 0.1317 0.1586 0.0469  -0.0009 -0.0092 233 HIS A C   
1975 O O   . HIS A 233 ? 0.1722 0.1357 0.1653 0.0417  -0.0004 -0.0074 233 HIS A O   
1976 C CB  . HIS A 233 ? 0.1502 0.1463 0.1512 0.0409  0.0034  -0.0086 233 HIS A CB  
1977 C CG  . HIS A 233 ? 0.1570 0.1622 0.1554 0.0358  0.0020  -0.0058 233 HIS A CG  
1978 N ND1 . HIS A 233 ? 0.1881 0.1939 0.1790 0.0286  0.0036  -0.0040 233 HIS A ND1 
1979 C CD2 . HIS A 233 ? 0.1882 0.2039 0.1908 0.0370  -0.0009 -0.0054 233 HIS A CD2 
1980 C CE1 . HIS A 233 ? 0.1651 0.1807 0.1539 0.0257  0.0020  -0.0034 233 HIS A CE1 
1981 N NE2 . HIS A 233 ? 0.1677 0.1887 0.1633 0.0304  -0.0013 -0.0037 233 HIS A NE2 
1982 N N   . VAL A 234 ? 0.1494 0.1242 0.1537 0.0543  0.0008  -0.0157 234 VAL A N   
1983 C CA  . VAL A 234 ? 0.1722 0.1390 0.1739 0.0564  0.0029  -0.0210 234 VAL A CA  
1984 C C   . VAL A 234 ? 0.2184 0.1662 0.2181 0.0591  -0.0046 -0.0198 234 VAL A C   
1985 O O   . VAL A 234 ? 0.1858 0.1226 0.1800 0.0553  -0.0051 -0.0200 234 VAL A O   
1986 C CB  . VAL A 234 ? 0.1961 0.1743 0.2028 0.0628  0.0078  -0.0290 234 VAL A CB  
1987 C CG1 . VAL A 234 ? 0.1969 0.1662 0.1980 0.0649  0.0091  -0.0350 234 VAL A CG1 
1988 C CG2 . VAL A 234 ? 0.1597 0.1542 0.1676 0.0573  0.0144  -0.0283 234 VAL A CG2 
1989 N N   . GLU A 235 ? 0.1943 0.1370 0.1992 0.0653  -0.0117 -0.0183 235 GLU A N   
1990 C CA  . GLU A 235 ? 0.1853 0.1070 0.1897 0.0683  -0.0210 -0.0169 235 GLU A CA  
1991 C C   . GLU A 235 ? 0.2251 0.1357 0.2217 0.0571  -0.0247 -0.0065 235 GLU A C   
1992 O O   . GLU A 235 ? 0.2352 0.1298 0.2286 0.0545  -0.0287 -0.0060 235 GLU A O   
1993 C CB  . GLU A 235 ? 0.2359 0.1546 0.2494 0.0779  -0.0294 -0.0166 235 GLU A CB  
1994 C CG  . GLU A 235 ? 0.4138 0.3132 0.4292 0.0806  -0.0379 -0.0172 235 GLU A CG  
1995 C CD  . GLU A 235 ? 0.5638 0.4616 0.5772 0.0808  -0.0327 -0.0271 235 GLU A CD  
1996 O OE1 . GLU A 235 ? 0.4966 0.4108 0.5132 0.0849  -0.0245 -0.0360 235 GLU A OE1 
1997 O OE2 . GLU A 235 ? 0.6244 0.5053 0.6325 0.0758  -0.0372 -0.0249 235 GLU A OE2 
1998 N N   . LEU A 236 ? 0.1831 0.1037 0.1766 0.0499  -0.0233 0.0015  236 LEU A N   
1999 C CA  . LEU A 236 ? 0.2079 0.1232 0.1939 0.0385  -0.0253 0.0111  236 LEU A CA  
2000 C C   . LEU A 236 ? 0.2160 0.1337 0.1991 0.0324  -0.0185 0.0079  236 LEU A C   
2001 O O   . LEU A 236 ? 0.2030 0.1122 0.1827 0.0247  -0.0211 0.0131  236 LEU A O   
2002 C CB  . LEU A 236 ? 0.1972 0.1262 0.1794 0.0326  -0.0241 0.0180  236 LEU A CB  
2003 C CG  . LEU A 236 ? 0.2046 0.1300 0.1877 0.0359  -0.0335 0.0250  236 LEU A CG  
2004 C CD1 . LEU A 236 ? 0.2415 0.1834 0.2189 0.0295  -0.0313 0.0300  236 LEU A CD1 
2005 C CD2 . LEU A 236 ? 0.2875 0.1919 0.2675 0.0326  -0.0446 0.0347  236 LEU A CD2 
2006 N N   . ALA A 237 ? 0.1642 0.0941 0.1493 0.0349  -0.0105 0.0002  237 ALA A N   
2007 C CA  . ALA A 237 ? 0.1558 0.0868 0.1392 0.0302  -0.0058 -0.0028 237 ALA A CA  
2008 C C   . ALA A 237 ? 0.1794 0.0946 0.1620 0.0325  -0.0101 -0.0063 237 ALA A C   
2009 O O   . ALA A 237 ? 0.1804 0.0910 0.1614 0.0260  -0.0108 -0.0047 237 ALA A O   
2010 C CB  . ALA A 237 ? 0.1620 0.1066 0.1474 0.0323  0.0017  -0.0090 237 ALA A CB  
2011 N N   . LYS A 238 ? 0.2118 0.1204 0.1964 0.0418  -0.0128 -0.0125 238 LYS A N   
2012 C CA  . LYS A 238 ? 0.2055 0.0979 0.1886 0.0448  -0.0178 -0.0178 238 LYS A CA  
2013 C C   . LYS A 238 ? 0.2560 0.1307 0.2383 0.0388  -0.0269 -0.0100 238 LYS A C   
2014 O O   . LYS A 238 ? 0.2554 0.1193 0.2354 0.0341  -0.0302 -0.0108 238 LYS A O   
2015 C CB  . LYS A 238 ? 0.2215 0.1118 0.2080 0.0571  -0.0192 -0.0272 238 LYS A CB  
2016 C CG  . LYS A 238 ? 0.2683 0.1778 0.2549 0.0602  -0.0096 -0.0343 238 LYS A CG  
2017 C CD  . LYS A 238 ? 0.3604 0.2775 0.3532 0.0677  -0.0086 -0.0412 238 LYS A CD  
2018 C CE  . LYS A 238 ? 0.4335 0.3367 0.4261 0.0700  -0.0145 -0.0459 238 LYS A CE  
2019 N NZ  . LYS A 238 ? 0.4113 0.3235 0.4099 0.0784  -0.0126 -0.0540 238 LYS A NZ  
2020 N N   . GLU A 239 ? 0.2270 0.0990 0.2106 0.0375  -0.0318 -0.0015 239 GLU A N   
2021 C CA  . GLU A 239 ? 0.2442 0.0994 0.2260 0.0296  -0.0411 0.0085  239 GLU A CA  
2022 C C   . GLU A 239 ? 0.2457 0.1091 0.2242 0.0158  -0.0370 0.0156  239 GLU A C   
2023 O O   . GLU A 239 ? 0.2856 0.1364 0.2634 0.0082  -0.0426 0.0199  239 GLU A O   
2024 C CB  . GLU A 239 ? 0.3053 0.1570 0.2880 0.0309  -0.0478 0.0173  239 GLU A CB  
2025 C CG  . GLU A 239 ? 0.5070 0.3489 0.4964 0.0453  -0.0541 0.0100  239 GLU A CG  
2026 C CD  . GLU A 239 ? 0.7441 0.5864 0.7359 0.0476  -0.0608 0.0185  239 GLU A CD  
2027 O OE1 . GLU A 239 ? 0.8237 0.6696 0.8239 0.0582  -0.0624 0.0117  239 GLU A OE1 
2028 O OE2 . GLU A 239 ? 0.7867 0.6328 0.7722 0.0369  -0.0621 0.0314  239 GLU A OE2 
2029 N N   . LYS A 240 ? 0.2312 0.1162 0.2089 0.0125  -0.0275 0.0161  240 LYS A N   
2030 C CA  . LYS A 240 ? 0.2558 0.1517 0.2327 0.0011  -0.0231 0.0206  240 LYS A CA  
2031 C C   . LYS A 240 ? 0.2590 0.1519 0.2385 0.0002  -0.0220 0.0141  240 LYS A C   
2032 O O   . LYS A 240 ? 0.2478 0.1394 0.2287 -0.0093 -0.0240 0.0187  240 LYS A O   
2033 C CB  . LYS A 240 ? 0.2419 0.1608 0.2185 -0.0001 -0.0137 0.0196  240 LYS A CB  
2034 C CG  . LYS A 240 ? 0.2878 0.2215 0.2653 -0.0111 -0.0087 0.0233  240 LYS A CG  
2035 C CD  . LYS A 240 ? 0.3161 0.2509 0.2884 -0.0215 -0.0120 0.0355  240 LYS A CD  
2036 C CE  . LYS A 240 ? 0.4010 0.3536 0.3753 -0.0328 -0.0062 0.0383  240 LYS A CE  
2037 N NZ  . LYS A 240 ? 0.4253 0.3811 0.3928 -0.0453 -0.0089 0.0517  240 LYS A NZ  
2038 N N   . TYR A 241 ? 0.2203 0.1141 0.2004 0.0092  -0.0190 0.0041  241 TYR A N   
2039 C CA  . TYR A 241 ? 0.2249 0.1151 0.2054 0.0092  -0.0193 -0.0023 241 TYR A CA  
2040 C C   . TYR A 241 ? 0.2469 0.1159 0.2264 0.0069  -0.0290 -0.0018 241 TYR A C   
2041 O O   . TYR A 241 ? 0.2616 0.1281 0.2426 0.0000  -0.0315 -0.0014 241 TYR A O   
2042 C CB  . TYR A 241 ? 0.2445 0.1386 0.2230 0.0189  -0.0151 -0.0118 241 TYR A CB  
2043 C CG  . TYR A 241 ? 0.2583 0.1530 0.2352 0.0180  -0.0146 -0.0174 241 TYR A CG  
2044 C CD1 . TYR A 241 ? 0.2256 0.1054 0.1986 0.0199  -0.0206 -0.0230 241 TYR A CD1 
2045 C CD2 . TYR A 241 ? 0.2302 0.1392 0.2094 0.0155  -0.0092 -0.0174 241 TYR A CD2 
2046 C CE1 . TYR A 241 ? 0.2866 0.1671 0.2565 0.0184  -0.0213 -0.0275 241 TYR A CE1 
2047 C CE2 . TYR A 241 ? 0.2567 0.1656 0.2344 0.0144  -0.0104 -0.0211 241 TYR A CE2 
2048 C CZ  . TYR A 241 ? 0.2342 0.1297 0.2065 0.0156  -0.0162 -0.0258 241 TYR A CZ  
2049 O OH  . TYR A 241 ? 0.2701 0.1660 0.2394 0.0140  -0.0184 -0.0291 241 TYR A OH  
2050 N N   . PHE A 242 ? 0.2770 0.1304 0.2554 0.0126  -0.0355 -0.0022 242 PHE A N   
2051 C CA  . PHE A 242 ? 0.2955 0.1251 0.2737 0.0107  -0.0466 -0.0020 242 PHE A CA  
2052 C C   . PHE A 242 ? 0.3434 0.1693 0.3233 -0.0039 -0.0514 0.0111  242 PHE A C   
2053 O O   . PHE A 242 ? 0.3183 0.1339 0.2996 -0.0108 -0.0575 0.0118  242 PHE A O   
2054 C CB  . PHE A 242 ? 0.2952 0.1172 0.2751 0.0207  -0.0509 -0.0054 242 PHE A CB  
2055 C CG  . PHE A 242 ? 0.3194 0.1267 0.3010 0.0201  -0.0595 -0.0075 242 PHE A CG  
2056 C CD1 . PHE A 242 ? 0.3777 0.1834 0.3583 0.0260  -0.0594 -0.0196 242 PHE A CD1 
2057 C CD2 . PHE A 242 ? 0.2949 0.0901 0.2784 0.0133  -0.0682 0.0031  242 PHE A CD2 
2058 C CE1 . PHE A 242 ? 0.3458 0.1367 0.3277 0.0260  -0.0680 -0.0224 242 PHE A CE1 
2059 C CE2 . PHE A 242 ? 0.3254 0.1053 0.3109 0.0130  -0.0774 0.0010  242 PHE A CE2 
2060 C CZ  . PHE A 242 ? 0.3494 0.1265 0.3344 0.0198  -0.0775 -0.0124 242 PHE A CZ  
2061 N N   . GLU A 243 ? 0.2955 0.1335 0.2752 -0.0097 -0.0480 0.0216  243 GLU A N   
2062 C CA  . GLU A 243 ? 0.3200 0.1601 0.3003 -0.0252 -0.0505 0.0345  243 GLU A CA  
2063 C C   . GLU A 243 ? 0.2909 0.1462 0.2756 -0.0335 -0.0450 0.0328  243 GLU A C   
2064 O O   . GLU A 243 ? 0.3246 0.1753 0.3122 -0.0455 -0.0501 0.0396  243 GLU A O   
2065 C CB  . GLU A 243 ? 0.3476 0.2027 0.3246 -0.0296 -0.0461 0.0444  243 GLU A CB  
2066 C CG  . GLU A 243 ? 0.4988 0.3636 0.4749 -0.0472 -0.0458 0.0581  243 GLU A CG  
2067 C CD  . GLU A 243 ? 0.5984 0.4909 0.5710 -0.0514 -0.0355 0.0622  243 GLU A CD  
2068 O OE1 . GLU A 243 ? 0.6109 0.5234 0.5855 -0.0627 -0.0293 0.0662  243 GLU A OE1 
2069 O OE2 . GLU A 243 ? 0.6017 0.4972 0.5702 -0.0433 -0.0339 0.0606  243 GLU A OE2 
2070 N N   . ILE A 244 ? 0.2978 0.1717 0.2843 -0.0277 -0.0355 0.0245  244 ILE A N   
2071 C CA  . ILE A 244 ? 0.2399 0.1302 0.2328 -0.0345 -0.0309 0.0232  244 ILE A CA  
2072 C C   . ILE A 244 ? 0.2973 0.1749 0.2919 -0.0334 -0.0370 0.0163  244 ILE A C   
2073 O O   . ILE A 244 ? 0.2727 0.1543 0.2736 -0.0431 -0.0396 0.0190  244 ILE A O   
2074 C CB  . ILE A 244 ? 0.2761 0.1891 0.2713 -0.0289 -0.0202 0.0174  244 ILE A CB  
2075 C CG1 . ILE A 244 ? 0.2173 0.1446 0.2103 -0.0310 -0.0143 0.0230  244 ILE A CG1 
2076 C CG2 . ILE A 244 ? 0.2918 0.2200 0.2961 -0.0339 -0.0174 0.0148  244 ILE A CG2 
2077 C CD1 . ILE A 244 ? 0.2663 0.2049 0.2611 -0.0450 -0.0135 0.0333  244 ILE A CD1 
2078 N N   . PHE A 245 ? 0.2846 0.1493 0.2738 -0.0220 -0.0392 0.0068  245 PHE A N   
2079 C CA  . PHE A 245 ? 0.2736 0.1301 0.2617 -0.0197 -0.0436 -0.0018 245 PHE A CA  
2080 C C   . PHE A 245 ? 0.3272 0.1570 0.3103 -0.0163 -0.0540 -0.0065 245 PHE A C   
2081 O O   . PHE A 245 ? 0.3449 0.1696 0.3263 -0.0158 -0.0581 -0.0134 245 PHE A O   
2082 C CB  . PHE A 245 ? 0.2157 0.0833 0.2004 -0.0099 -0.0367 -0.0106 245 PHE A CB  
2083 C CG  . PHE A 245 ? 0.2510 0.1415 0.2417 -0.0120 -0.0285 -0.0081 245 PHE A CG  
2084 C CD1 . PHE A 245 ? 0.2394 0.1405 0.2378 -0.0185 -0.0292 -0.0072 245 PHE A CD1 
2085 C CD2 . PHE A 245 ? 0.2593 0.1610 0.2494 -0.0070 -0.0209 -0.0075 245 PHE A CD2 
2086 C CE1 . PHE A 245 ? 0.2584 0.1802 0.2645 -0.0188 -0.0224 -0.0066 245 PHE A CE1 
2087 C CE2 . PHE A 245 ? 0.2841 0.2052 0.2805 -0.0082 -0.0143 -0.0068 245 PHE A CE2 
2088 C CZ  . PHE A 245 ? 0.2760 0.2067 0.2807 -0.0135 -0.0151 -0.0068 245 PHE A CZ  
2089 N N   . GLY A 246 ? 0.3060 0.0865 0.3450 -0.0007 0.0036  0.0055  246 GLY A N   
2090 C CA  . GLY A 246 ? 0.3306 0.0916 0.3662 0.0026  0.0018  0.0014  246 GLY A CA  
2091 C C   . GLY A 246 ? 0.3296 0.0899 0.3563 0.0094  -0.0008 -0.0097 246 GLY A C   
2092 O O   . GLY A 246 ? 0.3492 0.0954 0.3749 0.0110  -0.0022 -0.0160 246 GLY A O   
2093 N N   . GLU A 247 ? 0.3108 0.0868 0.3324 0.0132  -0.0009 -0.0124 247 GLU A N   
2094 C CA  . GLU A 247 ? 0.4492 0.2288 0.4644 0.0205  -0.0014 -0.0214 247 GLU A CA  
2095 C C   . GLU A 247 ? 0.3902 0.1810 0.3994 0.0283  0.0008  -0.0174 247 GLU A C   
2096 O O   . GLU A 247 ? 0.4025 0.2007 0.4130 0.0264  0.0009  -0.0099 247 GLU A O   
2097 C CB  . GLU A 247 ? 0.5613 0.3525 0.5805 0.0151  -0.0049 -0.0311 247 GLU A CB  
2098 C CG  . GLU A 247 ? 0.7088 0.4989 0.7381 0.0042  -0.0075 -0.0317 247 GLU A CG  
2099 C CD  . GLU A 247 ? 0.7992 0.5993 0.8316 0.0008  -0.0125 -0.0419 247 GLU A CD  
2100 O OE1 . GLU A 247 ? 0.8523 0.6592 0.8779 0.0069  -0.0139 -0.0485 247 GLU A OE1 
2101 O OE2 . GLU A 247 ? 0.8271 0.6291 0.8693 -0.0074 -0.0151 -0.0432 247 GLU A OE2 
2102 N N   . HIS A 248 ? 0.3676 0.1624 0.3744 0.0372  0.0026  -0.0229 248 HIS A N   
2103 C CA  . HIS A 248 ? 0.3769 0.1874 0.3838 0.0431  0.0047  -0.0200 248 HIS A CA  
2104 C C   . HIS A 248 ? 0.3365 0.1637 0.3444 0.0391  0.0022  -0.0260 248 HIS A C   
2105 O O   . HIS A 248 ? 0.3686 0.1971 0.3760 0.0363  -0.0007 -0.0341 248 HIS A O   
2106 C CB  . HIS A 248 ? 0.4816 0.2959 0.4936 0.0539  0.0056  -0.0223 248 HIS A CB  
2107 C CG  . HIS A 248 ? 0.7074 0.5176 0.7273 0.0589  0.0066  -0.0137 248 HIS A CG  
2108 N ND1 . HIS A 248 ? 0.7106 0.5285 0.7335 0.0605  0.0013  -0.0061 248 HIS A ND1 
2109 C CD2 . HIS A 248 ? 0.7587 0.5561 0.7825 0.0635  0.0072  -0.0126 248 HIS A CD2 
2110 C CE1 . HIS A 248 ? 0.7532 0.5607 0.7751 0.0671  -0.0003 0.0002  248 HIS A CE1 
2111 N NE2 . HIS A 248 ? 0.7740 0.5718 0.8027 0.0680  0.0006  -0.0043 248 HIS A NE2 
2112 N N   . PRO A 249 ? 0.2927 0.1322 0.3010 0.0393  0.0028  -0.0222 249 PRO A N   
2113 C CA  . PRO A 249 ? 0.2611 0.1145 0.2691 0.0355  0.0009  -0.0270 249 PRO A CA  
2114 C C   . PRO A 249 ? 0.3553 0.2185 0.3595 0.0429  -0.0003 -0.0341 249 PRO A C   
2115 O O   . PRO A 249 ? 0.3734 0.2393 0.3759 0.0518  0.0004  -0.0337 249 PRO A O   
2116 C CB  . PRO A 249 ? 0.3030 0.1641 0.3128 0.0339  0.0019  -0.0204 249 PRO A CB  
2117 C CG  . PRO A 249 ? 0.3425 0.2003 0.3529 0.0427  0.0037  -0.0145 249 PRO A CG  
2118 C CD  . PRO A 249 ? 0.3410 0.1826 0.3496 0.0433  0.0047  -0.0131 249 PRO A CD  
2119 N N   . VAL A 250 ? 0.2682 0.1376 0.2695 0.0400  -0.0021 -0.0402 250 VAL A N   
2120 C CA  . VAL A 250 ? 0.2404 0.1203 0.2355 0.0472  -0.0021 -0.0461 250 VAL A CA  
2121 C C   . VAL A 250 ? 0.2311 0.1237 0.2249 0.0452  -0.0011 -0.0457 250 VAL A C   
2122 O O   . VAL A 250 ? 0.2916 0.1969 0.2807 0.0499  0.0013  -0.0480 250 VAL A O   
2123 C CB  . VAL A 250 ? 0.3283 0.2047 0.3187 0.0486  -0.0046 -0.0539 250 VAL A CB  
2124 C CG1 . VAL A 250 ? 0.3736 0.2370 0.3653 0.0521  -0.0054 -0.0554 250 VAL A CG1 
2125 C CG2 . VAL A 250 ? 0.3576 0.2323 0.3493 0.0398  -0.0073 -0.0555 250 VAL A CG2 
2126 N N   . TYR A 251 ? 0.2346 0.1281 0.2333 0.0367  -0.0009 -0.0407 251 TYR A N   
2127 C CA  . TYR A 251 ? 0.2360 0.1454 0.2353 0.0321  0.0020  -0.0369 251 TYR A CA  
2128 C C   . TYR A 251 ? 0.2540 0.1662 0.2586 0.0281  0.0034  -0.0298 251 TYR A C   
2129 O O   . TYR A 251 ? 0.2880 0.1894 0.2955 0.0266  0.0025  -0.0266 251 TYR A O   
2130 C CB  . TYR A 251 ? 0.3621 0.2723 0.3597 0.0264  0.0007  -0.0391 251 TYR A CB  
2131 C CG  . TYR A 251 ? 0.3309 0.2272 0.3311 0.0229  -0.0037 -0.0424 251 TYR A CG  
2132 C CD1 . TYR A 251 ? 0.3671 0.2595 0.3738 0.0163  -0.0034 -0.0365 251 TYR A CD1 
2133 C CD2 . TYR A 251 ? 0.3233 0.2169 0.3185 0.0248  -0.0064 -0.0484 251 TYR A CD2 
2134 C CE1 . TYR A 251 ? 0.3577 0.2443 0.3666 0.0113  -0.0054 -0.0366 251 TYR A CE1 
2135 C CE2 . TYR A 251 ? 0.3119 0.1993 0.3104 0.0195  -0.0094 -0.0495 251 TYR A CE2 
2136 C CZ  . TYR A 251 ? 0.3796 0.2636 0.3855 0.0126  -0.0087 -0.0435 251 TYR A CZ  
2137 O OH  . TYR A 251 ? 0.4090 0.2883 0.4195 0.0075  -0.0116 -0.0447 251 TYR A OH  
2138 N N   . MET A 252 ? 0.1870 0.1141 0.1928 0.0266  0.0058  -0.0272 252 MET A N   
2139 C CA  . MET A 252 ? 0.1417 0.0738 0.1509 0.0237  0.0064  -0.0220 252 MET A CA  
2140 C C   . MET A 252 ? 0.1305 0.0740 0.1416 0.0179  0.0077  -0.0218 252 MET A C   
2141 O O   . MET A 252 ? 0.1779 0.1287 0.1886 0.0177  0.0093  -0.0240 252 MET A O   
2142 C CB  . MET A 252 ? 0.1641 0.1031 0.1739 0.0306  0.0067  -0.0200 252 MET A CB  
2143 C CG  . MET A 252 ? 0.1884 0.1144 0.1965 0.0359  0.0059  -0.0173 252 MET A CG  
2144 S SD  . MET A 252 ? 0.2213 0.1567 0.2289 0.0447  0.0057  -0.0132 252 MET A SD  
2145 C CE  . MET A 252 ? 0.2082 0.1221 0.2128 0.0510  0.0056  -0.0094 252 MET A CE  
2146 N N   . TRP A 253 ? 0.1257 0.0700 0.1387 0.0137  0.0075  -0.0187 253 TRP A N   
2147 C CA  . TRP A 253 ? 0.1204 0.0744 0.1359 0.0089  0.0083  -0.0188 253 TRP A CA  
2148 C C   . TRP A 253 ? 0.1461 0.1120 0.1647 0.0115  0.0079  -0.0186 253 TRP A C   
2149 O O   . TRP A 253 ? 0.1547 0.1199 0.1719 0.0145  0.0066  -0.0163 253 TRP A O   
2150 C CB  . TRP A 253 ? 0.1263 0.0753 0.1419 0.0038  0.0078  -0.0168 253 TRP A CB  
2151 C CG  . TRP A 253 ? 0.1140 0.0709 0.1320 -0.0001 0.0081  -0.0174 253 TRP A CG  
2152 C CD1 . TRP A 253 ? 0.1331 0.0941 0.1516 -0.0002 0.0072  -0.0167 253 TRP A CD1 
2153 C CD2 . TRP A 253 ? 0.1530 0.1145 0.1733 -0.0038 0.0095  -0.0191 253 TRP A CD2 
2154 N NE1 . TRP A 253 ? 0.1433 0.1098 0.1648 -0.0042 0.0070  -0.0191 253 TRP A NE1 
2155 C CE2 . TRP A 253 ? 0.1403 0.1065 0.1637 -0.0070 0.0088  -0.0199 253 TRP A CE2 
2156 C CE3 . TRP A 253 ? 0.1651 0.1264 0.1844 -0.0044 0.0115  -0.0196 253 TRP A CE3 
2157 C CZ2 . TRP A 253 ? 0.1476 0.1169 0.1752 -0.0116 0.0101  -0.0210 253 TRP A CZ2 
2158 C CZ3 . TRP A 253 ? 0.1452 0.1107 0.1676 -0.0086 0.0138  -0.0192 253 TRP A CZ3 
2159 C CH2 . TRP A 253 ? 0.1602 0.1289 0.1877 -0.0127 0.0131  -0.0198 253 TRP A CH2 
2160 N N   . PRO A 254 ? 0.1278 0.1057 0.1512 0.0107  0.0089  -0.0208 254 PRO A N   
2161 C CA  . PRO A 254 ? 0.1103 0.1018 0.1389 0.0127  0.0073  -0.0219 254 PRO A CA  
2162 C C   . PRO A 254 ? 0.1191 0.1126 0.1494 0.0076  0.0055  -0.0226 254 PRO A C   
2163 O O   . PRO A 254 ? 0.1456 0.1370 0.1780 0.0012  0.0068  -0.0234 254 PRO A O   
2164 C CB  . PRO A 254 ? 0.1387 0.1428 0.1745 0.0120  0.0097  -0.0240 254 PRO A CB  
2165 C CG  . PRO A 254 ? 0.2298 0.2268 0.2634 0.0071  0.0130  -0.0232 254 PRO A CG  
2166 C CD  . PRO A 254 ? 0.2125 0.1932 0.2372 0.0082  0.0119  -0.0220 254 PRO A CD  
2167 N N   . PRO A 255 ? 0.1386 0.1356 0.1668 0.0114  0.0026  -0.0225 255 PRO A N   
2168 C CA  . PRO A 255 ? 0.1537 0.1521 0.1816 0.0080  0.0005  -0.0242 255 PRO A CA  
2169 C C   . PRO A 255 ? 0.1399 0.1468 0.1771 0.0014  -0.0002 -0.0291 255 PRO A C   
2170 O O   . PRO A 255 ? 0.1261 0.1454 0.1720 0.0013  -0.0008 -0.0317 255 PRO A O   
2171 C CB  . PRO A 255 ? 0.1563 0.1615 0.1800 0.0156  -0.0028 -0.0239 255 PRO A CB  
2172 C CG  . PRO A 255 ? 0.1393 0.1370 0.1577 0.0220  -0.0010 -0.0187 255 PRO A CG  
2173 C CD  . PRO A 255 ? 0.1455 0.1431 0.1693 0.0201  0.0012  -0.0200 255 PRO A CD  
2174 N N   . LEU A 256 ? 0.1314 0.1316 0.1681 -0.0040 0.0002  -0.0299 256 LEU A N   
2175 C CA  . LEU A 256 ? 0.1169 0.1205 0.1624 -0.0110 -0.0001 -0.0339 256 LEU A CA  
2176 C C   . LEU A 256 ? 0.1182 0.1236 0.1708 -0.0151 0.0042  -0.0321 256 LEU A C   
2177 O O   . LEU A 256 ? 0.1236 0.1358 0.1871 -0.0207 0.0047  -0.0347 256 LEU A O   
2178 C CB  . LEU A 256 ? 0.1089 0.1257 0.1614 -0.0108 -0.0053 -0.0405 256 LEU A CB  
2179 C CG  . LEU A 256 ? 0.1688 0.1874 0.2118 -0.0034 -0.0095 -0.0418 256 LEU A CG  
2180 C CD1 . LEU A 256 ? 0.2515 0.2854 0.3002 -0.0012 -0.0156 -0.0488 256 LEU A CD1 
2181 C CD2 . LEU A 256 ? 0.1621 0.1694 0.1974 -0.0045 -0.0090 -0.0415 256 LEU A CD2 
2182 N N   . ALA A 257 ? 0.1298 0.1291 0.1762 -0.0123 0.0075  -0.0278 257 ALA A N   
2183 C CA  . ALA A 257 ? 0.0993 0.1012 0.1490 -0.0135 0.0120  -0.0257 257 ALA A CA  
2184 C C   . ALA A 257 ? 0.1538 0.1722 0.2137 -0.0122 0.0123  -0.0276 257 ALA A C   
2185 O O   . ALA A 257 ? 0.1575 0.1825 0.2245 -0.0149 0.0167  -0.0262 257 ALA A O   
2186 C CB  . ALA A 257 ? 0.1298 0.1263 0.1824 -0.0203 0.0153  -0.0240 257 ALA A CB  
2187 N N   . SER A 258 ? 0.1196 0.1463 0.1810 -0.0076 0.0078  -0.0305 258 SER A N   
2188 C CA  . SER A 258 ? 0.1010 0.1464 0.1753 -0.0074 0.0068  -0.0337 258 SER A CA  
2189 C C   . SER A 258 ? 0.1343 0.1868 0.2087 -0.0009 0.0099  -0.0317 258 SER A C   
2190 O O   . SER A 258 ? 0.1539 0.2009 0.2186 0.0072  0.0088  -0.0304 258 SER A O   
2191 C CB  . SER A 258 ? 0.1230 0.1771 0.1989 -0.0040 -0.0001 -0.0384 258 SER A CB  
2192 O OG  . SER A 258 ? 0.1611 0.2356 0.2526 -0.0051 -0.0019 -0.0427 258 SER A OG  
2193 N N   . VAL A 259 ? 0.1238 0.1887 0.2099 -0.0042 0.0143  -0.0314 259 VAL A N   
2194 C CA  . VAL A 259 ? 0.1027 0.1768 0.1896 0.0028  0.0180  -0.0300 259 VAL A CA  
2195 C C   . VAL A 259 ? 0.1018 0.1995 0.2080 0.0004  0.0192  -0.0321 259 VAL A C   
2196 O O   . VAL A 259 ? 0.1161 0.2210 0.2358 -0.0085 0.0181  -0.0343 259 VAL A O   
2197 C CB  . VAL A 259 ? 0.1267 0.1914 0.2054 0.0033  0.0247  -0.0257 259 VAL A CB  
2198 C CG1 . VAL A 259 ? 0.1954 0.2388 0.2573 0.0060  0.0225  -0.0247 259 VAL A CG1 
2199 C CG2 . VAL A 259 ? 0.1719 0.2384 0.2590 -0.0065 0.0300  -0.0229 259 VAL A CG2 
2200 N N   . SER A 260 ? 0.1041 0.2141 0.2123 0.0088  0.0211  -0.0320 260 SER A N   
2201 C CA  . SER A 260 ? 0.1039 0.2393 0.2311 0.0084  0.0234  -0.0335 260 SER A CA  
2202 C C   . SER A 260 ? 0.1086 0.2480 0.2296 0.0190  0.0284  -0.0313 260 SER A C   
2203 O O   . SER A 260 ? 0.1319 0.2541 0.2352 0.0263  0.0278  -0.0303 260 SER A O   
2204 C CB  . SER A 260 ? 0.1382 0.2897 0.2757 0.0110  0.0151  -0.0393 260 SER A CB  
2205 O OG  . SER A 260 ? 0.1231 0.2690 0.2466 0.0237  0.0109  -0.0396 260 SER A OG  
2206 N N   . ASN A 261 ? 0.1095 0.2724 0.2463 0.0202  0.0332  -0.0311 261 ASN A N   
2207 C CA  . ASN A 261 ? 0.1156 0.2839 0.2463 0.0320  0.0381  -0.0298 261 ASN A CA  
2208 C C   . ASN A 261 ? 0.1328 0.2954 0.2524 0.0449  0.0312  -0.0330 261 ASN A C   
2209 O O   . ASN A 261 ? 0.1289 0.2766 0.2322 0.0540  0.0324  -0.0325 261 ASN A O   
2210 C CB  . ASN A 261 ? 0.1162 0.3144 0.2681 0.0316  0.0445  -0.0291 261 ASN A CB  
2211 C CG  . ASN A 261 ? 0.1399 0.3420 0.3014 0.0201  0.0538  -0.0236 261 ASN A CG  
2212 O OD1 . ASN A 261 ? 0.1373 0.3199 0.2842 0.0174  0.0577  -0.0196 261 ASN A OD1 
2213 N ND2 . ASN A 261 ? 0.1588 0.3867 0.3458 0.0136  0.0577  -0.0231 261 ASN A ND2 
2214 N N   . GLU A 262 ? 0.1166 0.2903 0.2448 0.0464  0.0238  -0.0365 262 GLU A N   
2215 C CA  . GLU A 262 ? 0.1223 0.2901 0.2396 0.0594  0.0176  -0.0380 262 GLU A CA  
2216 C C   . GLU A 262 ? 0.1468 0.2844 0.2438 0.0599  0.0145  -0.0362 262 GLU A C   
2217 O O   . GLU A 262 ? 0.1627 0.2875 0.2470 0.0707  0.0131  -0.0354 262 GLU A O   
2218 C CB  . GLU A 262 ? 0.1204 0.3083 0.2505 0.0613  0.0100  -0.0419 262 GLU A CB  
2219 C CG  . GLU A 262 ? 0.1589 0.3792 0.3109 0.0628  0.0124  -0.0443 262 GLU A CG  
2220 C CD  . GLU A 262 ? 0.4649 0.7069 0.6288 0.0677  0.0034  -0.0492 262 GLU A CD  
2221 O OE1 . GLU A 262 ? 0.4216 0.6532 0.5714 0.0771  -0.0035 -0.0494 262 GLU A OE1 
2222 O OE2 . GLU A 262 ? 0.5097 0.7736 0.6935 0.0609  0.0033  -0.0513 262 GLU A OE2 
2223 N N   . ALA A 263 ? 0.1272 0.2529 0.2219 0.0487  0.0135  -0.0354 263 ALA A N   
2224 C CA  . ALA A 263 ? 0.1303 0.2295 0.2078 0.0487  0.0112  -0.0332 263 ALA A CA  
2225 C C   . ALA A 263 ? 0.1619 0.2445 0.2278 0.0512  0.0161  -0.0315 263 ALA A C   
2226 O O   . ALA A 263 ? 0.1696 0.2338 0.2229 0.0573  0.0143  -0.0307 263 ALA A O   
2227 C CB  . ALA A 263 ? 0.1148 0.2070 0.1931 0.0370  0.0094  -0.0332 263 ALA A CB  
2228 N N   . LEU A 264 ? 0.1364 0.2249 0.2066 0.0466  0.0223  -0.0309 264 LEU A N   
2229 C CA  . LEU A 264 ? 0.1652 0.2399 0.2229 0.0504  0.0262  -0.0304 264 LEU A CA  
2230 C C   . LEU A 264 ? 0.2033 0.2784 0.2558 0.0643  0.0261  -0.0326 264 LEU A C   
2231 O O   . LEU A 264 ? 0.2002 0.2563 0.2396 0.0697  0.0251  -0.0339 264 LEU A O   
2232 C CB  . LEU A 264 ? 0.1573 0.2408 0.2196 0.0446  0.0335  -0.0284 264 LEU A CB  
2233 C CG  . LEU A 264 ? 0.1803 0.2564 0.2440 0.0320  0.0338  -0.0259 264 LEU A CG  
2234 C CD1 . LEU A 264 ? 0.1732 0.2616 0.2453 0.0262  0.0418  -0.0223 264 LEU A CD1 
2235 C CD2 . LEU A 264 ? 0.2597 0.3118 0.3075 0.0316  0.0315  -0.0257 264 LEU A CD2 
2236 N N   . GLU A 265 ? 0.1466 0.2432 0.2101 0.0704  0.0268  -0.0337 265 GLU A N   
2237 C CA  . GLU A 265 ? 0.1833 0.2802 0.2419 0.0850  0.0262  -0.0359 265 GLU A CA  
2238 C C   . GLU A 265 ? 0.1758 0.2525 0.2243 0.0909  0.0197  -0.0356 265 GLU A C   
2239 O O   . GLU A 265 ? 0.2258 0.2878 0.2642 0.1008  0.0192  -0.0372 265 GLU A O   
2240 C CB  . GLU A 265 ? 0.1821 0.3089 0.2566 0.0906  0.0275  -0.0368 265 GLU A CB  
2241 C CG  . GLU A 265 ? 0.1604 0.3082 0.2459 0.0869  0.0360  -0.0360 265 GLU A CG  
2242 C CD  . GLU A 265 ? 0.4176 0.5980 0.5231 0.0904  0.0373  -0.0370 265 GLU A CD  
2243 O OE1 . GLU A 265 ? 0.5129 0.6970 0.6190 0.0994  0.0317  -0.0387 265 GLU A OE1 
2244 O OE2 . GLU A 265 ? 0.5000 0.7007 0.6205 0.0832  0.0439  -0.0351 265 GLU A OE2 
2245 N N   . LEU A 266 ? 0.1599 0.2358 0.2112 0.0856  0.0149  -0.0336 266 LEU A N   
2246 C CA  . LEU A 266 ? 0.2022 0.2595 0.2437 0.0910  0.0100  -0.0314 266 LEU A CA  
2247 C C   . LEU A 266 ? 0.2038 0.2330 0.2333 0.0871  0.0104  -0.0305 266 LEU A C   
2248 O O   . LEU A 266 ? 0.2184 0.2290 0.2394 0.0946  0.0090  -0.0300 266 LEU A O   
2249 C CB  . LEU A 266 ? 0.1921 0.2565 0.2378 0.0864  0.0054  -0.0294 266 LEU A CB  
2250 C CG  . LEU A 266 ? 0.1753 0.2198 0.2097 0.0904  0.0018  -0.0251 266 LEU A CG  
2251 C CD1 . LEU A 266 ? 0.2345 0.2744 0.2637 0.1055  0.0003  -0.0235 266 LEU A CD1 
2252 C CD2 . LEU A 266 ? 0.1927 0.2460 0.2294 0.0859  -0.0024 -0.0238 266 LEU A CD2 
2253 N N   . TYR A 267 ? 0.1882 0.2138 0.2179 0.0753  0.0120  -0.0303 267 TYR A N   
2254 C CA  . TYR A 267 ? 0.2255 0.2274 0.2457 0.0715  0.0118  -0.0302 267 TYR A CA  
2255 C C   . TYR A 267 ? 0.2286 0.2208 0.2420 0.0796  0.0132  -0.0343 267 TYR A C   
2256 O O   . TYR A 267 ? 0.2308 0.2019 0.2372 0.0828  0.0109  -0.0351 267 TYR A O   
2257 C CB  . TYR A 267 ? 0.1853 0.1882 0.2072 0.0592  0.0135  -0.0298 267 TYR A CB  
2258 C CG  . TYR A 267 ? 0.1727 0.1769 0.1980 0.0512  0.0111  -0.0268 267 TYR A CG  
2259 C CD1 . TYR A 267 ? 0.2063 0.1945 0.2261 0.0505  0.0084  -0.0239 267 TYR A CD1 
2260 C CD2 . TYR A 267 ? 0.1561 0.1769 0.1905 0.0444  0.0120  -0.0270 267 TYR A CD2 
2261 C CE1 . TYR A 267 ? 0.1864 0.1764 0.2077 0.0447  0.0067  -0.0215 267 TYR A CE1 
2262 C CE2 . TYR A 267 ? 0.1752 0.1964 0.2117 0.0382  0.0092  -0.0257 267 TYR A CE2 
2263 C CZ  . TYR A 267 ? 0.2029 0.2092 0.2318 0.0391  0.0067  -0.0230 267 TYR A CZ  
2264 O OH  . TYR A 267 ? 0.1721 0.1794 0.2014 0.0344  0.0045  -0.0220 267 TYR A OH  
2265 N N   . TYR A 268 ? 0.1859 0.1938 0.2018 0.0835  0.0171  -0.0371 268 TYR A N   
2266 C CA  . TYR A 268 ? 0.1882 0.1883 0.1960 0.0929  0.0184  -0.0421 268 TYR A CA  
2267 C C   . TYR A 268 ? 0.2119 0.2022 0.2167 0.1053  0.0156  -0.0434 268 TYR A C   
2268 O O   . TYR A 268 ? 0.2359 0.2062 0.2328 0.1077  0.0134  -0.0462 268 TYR A O   
2269 C CB  . TYR A 268 ? 0.2277 0.2497 0.2389 0.0962  0.0244  -0.0437 268 TYR A CB  
2270 C CG  . TYR A 268 ? 0.2717 0.2881 0.2736 0.1081  0.0257  -0.0493 268 TYR A CG  
2271 C CD1 . TYR A 268 ? 0.2700 0.2699 0.2606 0.1062  0.0246  -0.0530 268 TYR A CD1 
2272 C CD2 . TYR A 268 ? 0.3105 0.3372 0.3151 0.1167  0.0265  -0.0496 268 TYR A CD2 
2273 C CE1 . TYR A 268 ? 0.2924 0.2867 0.2744 0.1127  0.0242  -0.0573 268 TYR A CE1 
2274 C CE2 . TYR A 268 ? 0.3617 0.3817 0.3574 0.1235  0.0268  -0.0536 268 TYR A CE2 
2275 C CZ  . TYR A 268 ? 0.3237 0.3275 0.3081 0.1215  0.0255  -0.0577 268 TYR A CZ  
2276 O OH  . TYR A 268 ? 0.3870 0.3847 0.3621 0.1287  0.0249  -0.0627 268 TYR A OH  
2277 N N   . GLU A 269 ? 0.2161 0.2211 0.2281 0.1106  0.0150  -0.0406 269 GLU A N   
2278 C CA  . GLU A 269 ? 0.2539 0.2499 0.2628 0.1197  0.0122  -0.0393 269 GLU A CA  
2279 C C   . GLU A 269 ? 0.2713 0.2396 0.2740 0.1172  0.0085  -0.0363 269 GLU A C   
2280 O O   . GLU A 269 ? 0.3023 0.2553 0.3007 0.1221  0.0070  -0.0360 269 GLU A O   
2281 C CB  . GLU A 269 ? 0.3492 0.3672 0.3669 0.1249  0.0111  -0.0363 269 GLU A CB  
2282 C CG  . GLU A 269 ? 0.6179 0.6597 0.6422 0.1307  0.0140  -0.0386 269 GLU A CG  
2283 C CD  . GLU A 269 ? 0.8153 0.8458 0.8315 0.1375  0.0153  -0.0419 269 GLU A CD  
2284 O OE1 . GLU A 269 ? 0.8930 0.9298 0.9081 0.1363  0.0195  -0.0453 269 GLU A OE1 
2285 O OE2 . GLU A 269 ? 0.8885 0.9037 0.8990 0.1442  0.0123  -0.0410 269 GLU A OE2 
2286 N N   . LYS A 270 ? 0.2536 0.2154 0.2566 0.1095  0.0076  -0.0335 270 LYS A N   
2287 C CA  . LYS A 270 ? 0.3020 0.2398 0.3011 0.1056  0.0053  -0.0291 270 LYS A CA  
2288 C C   . LYS A 270 ? 0.3293 0.2480 0.3251 0.0978  0.0049  -0.0328 270 LYS A C   
2289 O O   . LYS A 270 ? 0.2716 0.1727 0.2674 0.0916  0.0037  -0.0293 270 LYS A O   
2290 C CB  . LYS A 270 ? 0.2833 0.2271 0.2851 0.0984  0.0046  -0.0229 270 LYS A CB  
2291 C CG  . LYS A 270 ? 0.2699 0.2323 0.2747 0.1060  0.0034  -0.0195 270 LYS A CG  
2292 C CD  . LYS A 270 ? 0.3937 0.3438 0.3937 0.1177  0.0021  -0.0155 270 LYS A CD  
2293 C CE  . LYS A 270 ? 0.4415 0.4140 0.4445 0.1266  0.0001  -0.0138 270 LYS A CE  
2294 N NZ  . LYS A 270 ? 0.5002 0.4640 0.4988 0.1358  -0.0008 -0.0106 270 LYS A NZ  
2295 N N   . GLY A 271 ? 0.2678 0.1918 0.2617 0.0978  0.0061  -0.0394 271 GLY A N   
2296 C CA  . GLY A 271 ? 0.2888 0.1977 0.2793 0.0917  0.0047  -0.0440 271 GLY A CA  
2297 C C   . GLY A 271 ? 0.2199 0.1294 0.2102 0.0822  0.0046  -0.0450 271 GLY A C   
2298 O O   . GLY A 271 ? 0.2758 0.1731 0.2645 0.0760  0.0025  -0.0481 271 GLY A O   
2299 N N   . ILE A 272 ? 0.2329 0.1586 0.2265 0.0784  0.0067  -0.0417 272 ILE A N   
2300 C CA  . ILE A 272 ? 0.2418 0.1705 0.2360 0.0674  0.0071  -0.0413 272 ILE A CA  
2301 C C   . ILE A 272 ? 0.3038 0.2432 0.2936 0.0697  0.0097  -0.0461 272 ILE A C   
2302 O O   . ILE A 272 ? 0.3251 0.2824 0.3171 0.0743  0.0135  -0.0456 272 ILE A O   
2303 C CB  . ILE A 272 ? 0.2244 0.1664 0.2251 0.0601  0.0085  -0.0349 272 ILE A CB  
2304 C CG1 . ILE A 272 ? 0.2397 0.1729 0.2422 0.0607  0.0066  -0.0296 272 ILE A CG1 
2305 C CG2 . ILE A 272 ? 0.2203 0.1627 0.2214 0.0495  0.0088  -0.0342 272 ILE A CG2 
2306 C CD1 . ILE A 272 ? 0.2689 0.1796 0.2697 0.0572  0.0044  -0.0290 272 ILE A CD1 
2307 N N   . ASN A 273 ? 0.2658 0.1953 0.2499 0.0669  0.0077  -0.0506 273 ASN A N   
2308 C CA  . ASN A 273 ? 0.3193 0.2571 0.2962 0.0704  0.0100  -0.0549 273 ASN A CA  
2309 C C   . ASN A 273 ? 0.2389 0.1872 0.2166 0.0618  0.0128  -0.0506 273 ASN A C   
2310 O O   . ASN A 273 ? 0.2391 0.1977 0.2112 0.0649  0.0167  -0.0515 273 ASN A O   
2311 C CB  . ASN A 273 ? 0.3894 0.3125 0.3587 0.0725  0.0054  -0.0622 273 ASN A CB  
2312 C CG  . ASN A 273 ? 0.5193 0.4349 0.4885 0.0785  0.0036  -0.0647 273 ASN A CG  
2313 O OD1 . ASN A 273 ? 0.5040 0.4293 0.4730 0.0866  0.0068  -0.0643 273 ASN A OD1 
2314 N ND2 . ASN A 273 ? 0.6166 0.5157 0.5871 0.0744  -0.0011 -0.0672 273 ASN A ND2 
2315 N N   . MET A 274 ? 0.2297 0.1747 0.2134 0.0520  0.0113  -0.0460 274 MET A N   
2316 C CA  . MET A 274 ? 0.1846 0.1368 0.1691 0.0442  0.0136  -0.0422 274 MET A CA  
2317 C C   . MET A 274 ? 0.1732 0.1276 0.1667 0.0359  0.0135  -0.0365 274 MET A C   
2318 O O   . MET A 274 ? 0.2041 0.1491 0.2006 0.0343  0.0102  -0.0357 274 MET A O   
2319 C CB  . MET A 274 ? 0.2307 0.1722 0.2082 0.0422  0.0098  -0.0458 274 MET A CB  
2320 C CG  . MET A 274 ? 0.2334 0.1818 0.2099 0.0363  0.0124  -0.0415 274 MET A CG  
2321 S SD  . MET A 274 ? 0.4387 0.3821 0.4235 0.0253  0.0100  -0.0368 274 MET A SD  
2322 C CE  . MET A 274 ? 0.4037 0.3339 0.3833 0.0252  0.0033  -0.0428 274 MET A CE  
2323 N N   . LEU A 275 ? 0.1725 0.1388 0.1700 0.0308  0.0173  -0.0323 275 LEU A N   
2324 C CA  . LEU A 275 ? 0.1809 0.1480 0.1851 0.0226  0.0165  -0.0285 275 LEU A CA  
2325 C C   . LEU A 275 ? 0.1760 0.1476 0.1804 0.0169  0.0196  -0.0257 275 LEU A C   
2326 O O   . LEU A 275 ? 0.1692 0.1441 0.1684 0.0194  0.0228  -0.0256 275 LEU A O   
2327 C CB  . LEU A 275 ? 0.2112 0.1887 0.2237 0.0230  0.0170  -0.0268 275 LEU A CB  
2328 C CG  . LEU A 275 ? 0.2079 0.2020 0.2255 0.0265  0.0210  -0.0268 275 LEU A CG  
2329 C CD1 . LEU A 275 ? 0.2648 0.2682 0.2886 0.0190  0.0248  -0.0239 275 LEU A CD1 
2330 C CD2 . LEU A 275 ? 0.2367 0.2391 0.2609 0.0303  0.0192  -0.0271 275 LEU A CD2 
2331 N N   . ALA A 276 ? 0.1279 0.0987 0.1373 0.0099  0.0187  -0.0231 276 ALA A N   
2332 C CA  . ALA A 276 ? 0.1327 0.1072 0.1442 0.0045  0.0220  -0.0200 276 ALA A CA  
2333 C C   . ALA A 276 ? 0.1476 0.1308 0.1699 -0.0005 0.0227  -0.0188 276 ALA A C   
2334 O O   . ALA A 276 ? 0.1593 0.1444 0.1853 0.0003  0.0196  -0.0204 276 ALA A O   
2335 C CB  . ALA A 276 ? 0.1592 0.1229 0.1658 0.0014  0.0195  -0.0194 276 ALA A CB  
2336 N N   . THR A 277 ? 0.1533 0.1418 0.1807 -0.0053 0.0268  -0.0159 277 THR A N   
2337 C CA  . THR A 277 ? 0.1238 0.1197 0.1631 -0.0114 0.0269  -0.0160 277 THR A CA  
2338 C C   . THR A 277 ? 0.1539 0.1445 0.1948 -0.0177 0.0300  -0.0125 277 THR A C   
2339 O O   . THR A 277 ? 0.2257 0.2059 0.2572 -0.0166 0.0302  -0.0104 277 THR A O   
2340 C CB  . THR A 277 ? 0.1523 0.1648 0.2018 -0.0100 0.0294  -0.0168 277 THR A CB  
2341 O OG1 . THR A 277 ? 0.1501 0.1705 0.2131 -0.0168 0.0284  -0.0181 277 THR A OG1 
2342 C CG2 . THR A 277 ? 0.2150 0.2339 0.2639 -0.0081 0.0365  -0.0131 277 THR A CG2 
2343 N N   . ASP A 278 ? 0.1488 0.1459 0.2022 -0.0240 0.0316  -0.0122 278 ASP A N   
2344 C CA  . ASP A 278 ? 0.1862 0.1752 0.2426 -0.0304 0.0336  -0.0095 278 ASP A CA  
2345 C C   . ASP A 278 ? 0.2091 0.2024 0.2715 -0.0338 0.0417  -0.0033 278 ASP A C   
2346 O O   . ASP A 278 ? 0.1841 0.1914 0.2558 -0.0343 0.0456  -0.0024 278 ASP A O   
2347 C CB  . ASP A 278 ? 0.1888 0.1785 0.2555 -0.0361 0.0291  -0.0144 278 ASP A CB  
2348 C CG  . ASP A 278 ? 0.2418 0.2200 0.3111 -0.0421 0.0304  -0.0125 278 ASP A CG  
2349 O OD1 . ASP A 278 ? 0.2301 0.1958 0.2885 -0.0398 0.0297  -0.0106 278 ASP A OD1 
2350 O OD2 . ASP A 278 ? 0.2563 0.2380 0.3396 -0.0491 0.0321  -0.0131 278 ASP A OD2 
2351 N N   . GLU A 279 ? 0.2229 0.2042 0.2807 -0.0361 0.0445  0.0016  279 GLU A N   
2352 C CA  . GLU A 279 ? 0.2324 0.2143 0.2943 -0.0392 0.0532  0.0097  279 GLU A CA  
2353 C C   . GLU A 279 ? 0.2199 0.2112 0.3031 -0.0483 0.0565  0.0099  279 GLU A C   
2354 O O   . GLU A 279 ? 0.2599 0.2600 0.3502 -0.0501 0.0648  0.0163  279 GLU A O   
2355 C CB  . GLU A 279 ? 0.2502 0.2152 0.3032 -0.0395 0.0541  0.0146  279 GLU A CB  
2356 C CG  . GLU A 279 ? 0.3393 0.3026 0.3913 -0.0400 0.0637  0.0249  279 GLU A CG  
2357 C CD  . GLU A 279 ? 0.3695 0.3169 0.4082 -0.0366 0.0643  0.0304  279 GLU A CD  
2358 O OE1 . GLU A 279 ? 0.2676 0.2060 0.2994 -0.0344 0.0569  0.0253  279 GLU A OE1 
2359 O OE2 . GLU A 279 ? 0.4085 0.3535 0.4437 -0.0356 0.0726  0.0403  279 GLU A OE2 
2360 N N   . VAL A 280 ? 0.2361 0.2270 0.3302 -0.0539 0.0501  0.0027  280 VAL A N   
2361 C CA  . VAL A 280 ? 0.1692 0.1705 0.2857 -0.0629 0.0518  0.0010  280 VAL A CA  
2362 C C   . VAL A 280 ? 0.2130 0.2361 0.3383 -0.0608 0.0537  -0.0002 280 VAL A C   
2363 O O   . VAL A 280 ? 0.2462 0.2814 0.3882 -0.0664 0.0598  0.0032  280 VAL A O   
2364 C CB  . VAL A 280 ? 0.2866 0.2841 0.4070 -0.0657 0.0414  -0.0081 280 VAL A CB  
2365 C CG1 . VAL A 280 ? 0.2811 0.2914 0.4202 -0.0723 0.0398  -0.0111 280 VAL A CG1 
2366 C CG2 . VAL A 280 ? 0.3349 0.3128 0.4442 -0.0653 0.0387  -0.0063 280 VAL A CG2 
2367 N N   . ILE A 281 ? 0.2047 0.2333 0.3194 -0.0521 0.0487  -0.0047 281 ILE A N   
2368 C CA  . ILE A 281 ? 0.2303 0.2791 0.3524 -0.0484 0.0506  -0.0058 281 ILE A CA  
2369 C C   . ILE A 281 ? 0.2422 0.2963 0.3611 -0.0454 0.0612  0.0030  281 ILE A C   
2370 O O   . ILE A 281 ? 0.2029 0.2750 0.3365 -0.0472 0.0670  0.0053  281 ILE A O   
2371 C CB  . ILE A 281 ? 0.2228 0.2728 0.3331 -0.0390 0.0432  -0.0117 281 ILE A CB  
2372 C CG1 . ILE A 281 ? 0.2287 0.2784 0.3444 -0.0417 0.0339  -0.0197 281 ILE A CG1 
2373 C CG2 . ILE A 281 ? 0.2380 0.3062 0.3518 -0.0323 0.0460  -0.0117 281 ILE A CG2 
2374 C CD1 . ILE A 281 ? 0.2443 0.2899 0.3460 -0.0330 0.0271  -0.0237 281 ILE A CD1 
2375 N N   . LEU A 282 ? 0.2534 0.2934 0.3532 -0.0402 0.0638  0.0080  282 LEU A N   
2376 C CA  . LEU A 282 ? 0.2388 0.2826 0.3324 -0.0363 0.0740  0.0168  282 LEU A CA  
2377 C C   . LEU A 282 ? 0.2878 0.3377 0.3994 -0.0457 0.0833  0.0246  282 LEU A C   
2378 O O   . LEU A 282 ? 0.3155 0.3822 0.4361 -0.0451 0.0918  0.0294  282 LEU A O   
2379 C CB  . LEU A 282 ? 0.3087 0.3350 0.3796 -0.0302 0.0738  0.0203  282 LEU A CB  
2380 C CG  . LEU A 282 ? 0.2811 0.3104 0.3400 -0.0233 0.0833  0.0287  282 LEU A CG  
2381 C CD1 . LEU A 282 ? 0.3728 0.4175 0.4278 -0.0141 0.0850  0.0258  282 LEU A CD1 
2382 C CD2 . LEU A 282 ? 0.3005 0.3127 0.3379 -0.0175 0.0811  0.0310  282 LEU A CD2 
2383 N N   . LYS A 283 ? 0.2661 0.3023 0.3841 -0.0546 0.0821  0.0259  283 LYS A N   
2384 C CA  . LYS A 283 ? 0.2612 0.2985 0.3918 -0.0626 0.0873  0.0328  283 LYS A CA  
2385 C C   . LYS A 283 ? 0.2546 0.3123 0.4074 -0.0686 0.0860  0.0288  283 LYS A C   
2386 O O   . LYS A 283 ? 0.2567 0.3236 0.4186 -0.0724 0.0926  0.0355  283 LYS A O   
2387 C CB  . LYS A 283 ? 0.3261 0.3427 0.4542 -0.0680 0.0813  0.0320  283 LYS A CB  
2388 C CG  . LYS A 283 ? 0.4654 0.4630 0.5725 -0.0619 0.0824  0.0366  283 LYS A CG  
2389 C CD  . LYS A 283 ? 0.6157 0.5951 0.7214 -0.0662 0.0777  0.0370  283 LYS A CD  
2390 C CE  . LYS A 283 ? 0.7344 0.6980 0.8208 -0.0595 0.0809  0.0446  283 LYS A CE  
2391 N NZ  . LYS A 283 ? 0.7996 0.7710 0.8752 -0.0523 0.0905  0.0531  283 LYS A NZ  
2392 N N   . ASN A 284 ? 0.2756 0.3417 0.4370 -0.0690 0.0776  0.0180  284 ASN A N   
2393 C CA  . ASN A 284 ? 0.2645 0.3518 0.4467 -0.0734 0.0751  0.0133  284 ASN A CA  
2394 C C   . ASN A 284 ? 0.2933 0.4036 0.4799 -0.0669 0.0822  0.0160  284 ASN A C   
2395 O O   . ASN A 284 ? 0.2699 0.3997 0.4740 -0.0706 0.0829  0.0154  284 ASN A O   
2396 C CB  . ASN A 284 ? 0.2515 0.3410 0.4391 -0.0738 0.0629  0.0007  284 ASN A CB  
2397 C CG  . ASN A 284 ? 0.3103 0.3835 0.4987 -0.0807 0.0551  -0.0035 284 ASN A CG  
2398 O OD1 . ASN A 284 ? 0.4003 0.4626 0.5898 -0.0865 0.0583  0.0024  284 ASN A OD1 
2399 N ND2 . ASN A 284 ? 0.2552 0.3270 0.4424 -0.0791 0.0447  -0.0139 284 ASN A ND2 
2400 N N   . SER A 285 ? 0.2784 0.3873 0.4492 -0.0566 0.0872  0.0182  285 SER A N   
2401 C CA  . SER A 285 ? 0.2858 0.4144 0.4557 -0.0468 0.0915  0.0180  285 SER A CA  
2402 C C   . SER A 285 ? 0.4102 0.5433 0.5714 -0.0418 0.1041  0.0289  285 SER A C   
2403 O O   . SER A 285 ? 0.5062 0.6601 0.6743 -0.0379 0.1090  0.0304  285 SER A O   
2404 C CB  . SER A 285 ? 0.2544 0.3744 0.4019 -0.0348 0.0823  0.0107  285 SER A CB  
2405 O OG  . SER A 285 ? 0.2536 0.3673 0.4038 -0.0377 0.0705  0.0019  285 SER A OG  
2406 N N   . VAL A 286 ? 0.4474 0.5612 0.5905 -0.0404 0.1080  0.0359  286 VAL A N   
2407 C CA  . VAL A 286 ? 0.5164 0.6317 0.6434 -0.0324 0.1178  0.0451  286 VAL A CA  
2408 C C   . VAL A 286 ? 0.5978 0.7027 0.7255 -0.0405 0.1225  0.0547  286 VAL A C   
2409 O O   . VAL A 286 ? 0.6222 0.7099 0.7524 -0.0485 0.1175  0.0545  286 VAL A O   
2410 C CB  . VAL A 286 ? 0.5617 0.6629 0.6600 -0.0197 0.1154  0.0434  286 VAL A CB  
2411 C CG1 . VAL A 286 ? 0.6283 0.7361 0.7102 -0.0087 0.1259  0.0512  286 VAL A CG1 
2412 C CG2 . VAL A 286 ? 0.5449 0.6476 0.6381 -0.0130 0.1041  0.0312  286 VAL A CG2 
2413 N N   . GLU A 287 ? 0.6082 0.7231 0.7333 -0.0376 0.1320  0.0629  287 GLU A N   
2414 C CA  . GLU A 287 ? 0.6871 0.7920 0.8103 -0.0429 0.1382  0.0736  287 GLU A CA  
2415 C C   . GLU A 287 ? 0.6878 0.7688 0.7881 -0.0378 0.1368  0.0777  287 GLU A C   
2416 O O   . GLU A 287 ? 0.6581 0.7218 0.7616 -0.0455 0.1327  0.0786  287 GLU A O   
2417 C CB  . GLU A 287 ? 0.7376 0.8593 0.8600 -0.0384 0.1494  0.0813  287 GLU A CB  
2418 C CG  . GLU A 287 ? 0.8202 0.9418 0.9152 -0.0223 0.1546  0.0851  287 GLU A CG  
2419 C CD  . GLU A 287 ? 0.8899 1.0162 0.9733 -0.0108 0.1487  0.0749  287 GLU A CD  
2420 O OE1 . GLU A 287 ? 0.9109 1.0549 1.0075 -0.0101 0.1473  0.0679  287 GLU A OE1 
2421 O OE2 . GLU A 287 ? 0.9164 1.0281 0.9774 -0.0022 0.1451  0.0735  287 GLU A OE2 
2422 N N   . ARG A 288 ? 0.6523 0.7324 0.7291 -0.0241 0.1390  0.0788  288 ARG A N   
2423 C CA  . ARG A 288 ? 0.6407 0.7018 0.6939 -0.0172 0.1384  0.0834  288 ARG A CA  
2424 C C   . ARG A 288 ? 0.5710 0.6211 0.6173 -0.0151 0.1294  0.0742  288 ARG A C   
2425 O O   . ARG A 288 ? 0.6127 0.6662 0.6444 -0.0044 0.1274  0.0686  288 ARG A O   
2426 C CB  . ARG A 288 ? 0.6276 0.6950 0.6587 -0.0031 0.1448  0.0885  288 ARG A CB  
2427 C CG  . ARG A 288 ? 0.6958 0.7722 0.7333 -0.0055 0.1549  0.0991  288 ARG A CG  
2428 C CD  . ARG A 288 ? 0.7987 0.8864 0.8175 0.0089  0.1610  0.1021  288 ARG A CD  
2429 N NE  . ARG A 288 ? 0.8635 0.9698 0.8863 0.0142  0.1605  0.0937  288 ARG A NE  
2430 C CZ  . ARG A 288 ? 0.8944 1.0021 0.8981 0.0276  0.1557  0.0856  288 ARG A CZ  
2431 N NH1 . ARG A 288 ? 0.8732 0.9967 0.8819 0.0325  0.1550  0.0778  288 ARG A NH1 
2432 N NH2 . ARG A 288 ? 0.9169 1.0098 0.8966 0.0364  0.1509  0.0845  288 ARG A NH2 
2433 N N   . ALA A 289 ? 0.4911 0.5275 0.5480 -0.0252 0.1234  0.0717  289 ALA A N   
2434 C CA  . ALA A 289 ? 0.4795 0.5066 0.5344 -0.0256 0.1135  0.0616  289 ALA A CA  
2435 C C   . ALA A 289 ? 0.4285 0.4364 0.4604 -0.0190 0.1085  0.0623  289 ALA A C   
2436 O O   . ALA A 289 ? 0.4484 0.4406 0.4823 -0.0247 0.1043  0.0624  289 ALA A O   
2437 C CB  . ALA A 289 ? 0.5316 0.5558 0.6094 -0.0388 0.1080  0.0563  289 ALA A CB  
2438 N N   . SER A 290 ? 0.3281 0.3382 0.3380 -0.0062 0.1084  0.0619  290 SER A N   
2439 C CA  . SER A 290 ? 0.3570 0.3520 0.3459 0.0010  0.1008  0.0593  290 SER A CA  
2440 C C   . SER A 290 ? 0.3326 0.3246 0.3201 0.0021  0.0878  0.0455  290 SER A C   
2441 O O   . SER A 290 ? 0.3598 0.3616 0.3449 0.0076  0.0854  0.0386  290 SER A O   
2442 C CB  . SER A 290 ? 0.3281 0.3264 0.2936 0.0146  0.1051  0.0638  290 SER A CB  
2443 O OG  . SER A 290 ? 0.3791 0.3650 0.3269 0.0212  0.0957  0.0590  290 SER A OG  
2444 N N   . PRO A 291 ? 0.2807 0.2594 0.2693 -0.0022 0.0796  0.0414  291 PRO A N   
2445 C CA  . PRO A 291 ? 0.2589 0.2349 0.2460 -0.0009 0.0684  0.0298  291 PRO A CA  
2446 C C   . PRO A 291 ? 0.2138 0.1860 0.1816 0.0095  0.0626  0.0252  291 PRO A C   
2447 O O   . PRO A 291 ? 0.2447 0.2127 0.2121 0.0097  0.0536  0.0166  291 PRO A O   
2448 C CB  . PRO A 291 ? 0.3191 0.2834 0.3147 -0.0089 0.0635  0.0286  291 PRO A CB  
2449 C CG  . PRO A 291 ? 0.2752 0.2309 0.2667 -0.0095 0.0699  0.0390  291 PRO A CG  
2450 C CD  . PRO A 291 ? 0.3198 0.2855 0.3130 -0.0086 0.0811  0.0476  291 PRO A CD  
2451 N N   . TYR A 292 ? 0.2478 0.2218 0.1999 0.0182  0.0672  0.0304  292 TYR A N   
2452 C CA  . TYR A 292 ? 0.2361 0.2057 0.1702 0.0278  0.0599  0.0250  292 TYR A CA  
2453 C C   . TYR A 292 ? 0.2502 0.2284 0.1741 0.0373  0.0591  0.0186  292 TYR A C   
2454 O O   . TYR A 292 ? 0.2449 0.2208 0.1531 0.0462  0.0534  0.0135  292 TYR A O   
2455 C CB  . TYR A 292 ? 0.2822 0.2460 0.2026 0.0329  0.0631  0.0338  292 TYR A CB  
2456 C CG  . TYR A 292 ? 0.2878 0.2407 0.2181 0.0243  0.0632  0.0390  292 TYR A CG  
2457 C CD1 . TYR A 292 ? 0.2625 0.2089 0.2020 0.0184  0.0544  0.0315  292 TYR A CD1 
2458 C CD2 . TYR A 292 ? 0.3543 0.3031 0.2850 0.0225  0.0725  0.0516  292 TYR A CD2 
2459 C CE1 . TYR A 292 ? 0.3025 0.2392 0.2505 0.0117  0.0543  0.0352  292 TYR A CE1 
2460 C CE2 . TYR A 292 ? 0.3518 0.2886 0.2920 0.0150  0.0720  0.0553  292 TYR A CE2 
2461 C CZ  . TYR A 292 ? 0.3479 0.2791 0.2960 0.0102  0.0626  0.0464  292 TYR A CZ  
2462 O OH  . TYR A 292 ? 0.3967 0.3162 0.3530 0.0042  0.0619  0.0489  292 TYR A OH  
2463 N N   . LEU A 293 ? 0.2366 0.2248 0.1698 0.0359  0.0638  0.0178  293 LEU A N   
2464 C CA  . LEU A 293 ? 0.2182 0.2150 0.1428 0.0456  0.0641  0.0118  293 LEU A CA  
2465 C C   . LEU A 293 ? 0.2050 0.2001 0.1388 0.0434  0.0562  0.0012  293 LEU A C   
2466 O O   . LEU A 293 ? 0.2255 0.2175 0.1744 0.0340  0.0535  0.0006  293 LEU A O   
2467 C CB  . LEU A 293 ? 0.2252 0.2370 0.1537 0.0475  0.0767  0.0198  293 LEU A CB  
2468 C CG  . LEU A 293 ? 0.3979 0.4154 0.3161 0.0524  0.0881  0.0320  293 LEU A CG  
2469 C CD1 . LEU A 293 ? 0.4344 0.4410 0.3521 0.0468  0.0894  0.0408  293 LEU A CD1 
2470 C CD2 . LEU A 293 ? 0.3046 0.3386 0.2365 0.0498  0.1006  0.0395  293 LEU A CD2 
2471 N N   . ARG A 294 ? 0.2273 0.2239 0.1511 0.0529  0.0525  -0.0072 294 ARG A N   
2472 C CA  . ARG A 294 ? 0.2437 0.2401 0.1762 0.0526  0.0479  -0.0153 294 ARG A CA  
2473 C C   . ARG A 294 ? 0.2049 0.2169 0.1449 0.0547  0.0569  -0.0116 294 ARG A C   
2474 O O   . ARG A 294 ? 0.2497 0.2708 0.1792 0.0643  0.0629  -0.0105 294 ARG A O   
2475 C CB  . ARG A 294 ? 0.2419 0.2311 0.1620 0.0619  0.0395  -0.0268 294 ARG A CB  
2476 C CG  . ARG A 294 ? 0.2559 0.2414 0.1853 0.0615  0.0347  -0.0342 294 ARG A CG  
2477 C CD  . ARG A 294 ? 0.2762 0.2496 0.1968 0.0678  0.0249  -0.0461 294 ARG A CD  
2478 N NE  . ARG A 294 ? 0.3356 0.3126 0.2387 0.0804  0.0256  -0.0512 294 ARG A NE  
2479 C CZ  . ARG A 294 ? 0.3236 0.2939 0.2137 0.0855  0.0186  -0.0582 294 ARG A CZ  
2480 N NH1 . ARG A 294 ? 0.2960 0.2560 0.1905 0.0783  0.0105  -0.0606 294 ARG A NH1 
2481 N NH2 . ARG A 294 ? 0.3460 0.3217 0.2211 0.0966  0.0189  -0.0619 294 ARG A NH2 
2482 N N   . TYR A 295 ? 0.1908 0.2072 0.1488 0.0467  0.0577  -0.0101 295 TYR A N   
2483 C CA  . TYR A 295 ? 0.2145 0.2479 0.1831 0.0481  0.0653  -0.0074 295 TYR A CA  
2484 C C   . TYR A 295 ? 0.2036 0.2379 0.1730 0.0551  0.0604  -0.0162 295 TYR A C   
2485 O O   . TYR A 295 ? 0.2174 0.2386 0.1862 0.0540  0.0514  -0.0226 295 TYR A O   
2486 C CB  . TYR A 295 ? 0.1787 0.2186 0.1678 0.0359  0.0683  -0.0016 295 TYR A CB  
2487 C CG  . TYR A 295 ? 0.1961 0.2369 0.1874 0.0295  0.0756  0.0083  295 TYR A CG  
2488 C CD1 . TYR A 295 ? 0.2315 0.2575 0.2191 0.0236  0.0715  0.0101  295 TYR A CD1 
2489 C CD2 . TYR A 295 ? 0.2049 0.2611 0.2021 0.0298  0.0871  0.0165  295 TYR A CD2 
2490 C CE1 . TYR A 295 ? 0.1956 0.2201 0.1846 0.0185  0.0782  0.0197  295 TYR A CE1 
2491 C CE2 . TYR A 295 ? 0.2345 0.2894 0.2340 0.0237  0.0946  0.0269  295 TYR A CE2 
2492 C CZ  . TYR A 295 ? 0.2239 0.2617 0.2189 0.0182  0.0897  0.0283  295 TYR A CZ  
2493 O OH  . TYR A 295 ? 0.2429 0.2773 0.2396 0.0131  0.0974  0.0392  295 TYR A OH  
2494 N N   . TYR A 296 ? 0.2246 0.2748 0.1961 0.0625  0.0670  -0.0159 296 TYR A N   
2495 C CA  . TYR A 296 ? 0.2196 0.2721 0.1941 0.0697  0.0633  -0.0232 296 TYR A CA  
2496 C C   . TYR A 296 ? 0.2053 0.2771 0.1996 0.0659  0.0686  -0.0191 296 TYR A C   
2497 O O   . TYR A 296 ? 0.2019 0.2922 0.2010 0.0683  0.0784  -0.0138 296 TYR A O   
2498 C CB  . TYR A 296 ? 0.2572 0.3116 0.2157 0.0848  0.0648  -0.0291 296 TYR A CB  
2499 C CG  . TYR A 296 ? 0.2423 0.2805 0.1811 0.0895  0.0592  -0.0344 296 TYR A CG  
2500 C CD1 . TYR A 296 ? 0.2339 0.2523 0.1703 0.0862  0.0482  -0.0412 296 TYR A CD1 
2501 C CD2 . TYR A 296 ? 0.2694 0.3137 0.1925 0.0977  0.0650  -0.0325 296 TYR A CD2 
2502 C CE1 . TYR A 296 ? 0.2484 0.2540 0.1690 0.0902  0.0422  -0.0472 296 TYR A CE1 
2503 C CE2 . TYR A 296 ? 0.3130 0.3438 0.2188 0.1016  0.0579  -0.0379 296 TYR A CE2 
2504 C CZ  . TYR A 296 ? 0.3050 0.3171 0.2097 0.0987  0.0467  -0.0464 296 TYR A CZ  
2505 O OH  . TYR A 296 ? 0.3393 0.3403 0.2306 0.1013  0.0385  -0.0523 296 TYR A OH  
2506 N N   . PHE A 297 ? 0.1785 0.2474 0.1845 0.0605  0.0623  -0.0214 297 PHE A N   
2507 C CA  . PHE A 297 ? 0.1674 0.2558 0.1926 0.0579  0.0653  -0.0193 297 PHE A CA  
2508 C C   . PHE A 297 ? 0.1759 0.2759 0.1997 0.0714  0.0673  -0.0235 297 PHE A C   
2509 O O   . PHE A 297 ? 0.2150 0.3036 0.2316 0.0791  0.0605  -0.0300 297 PHE A O   
2510 C CB  . PHE A 297 ? 0.1597 0.2423 0.1952 0.0503  0.0573  -0.0210 297 PHE A CB  
2511 C CG  . PHE A 297 ? 0.1480 0.2517 0.2032 0.0485  0.0585  -0.0205 297 PHE A CG  
2512 C CD1 . PHE A 297 ? 0.1428 0.2621 0.2148 0.0386  0.0640  -0.0154 297 PHE A CD1 
2513 C CD2 . PHE A 297 ? 0.1535 0.2616 0.2110 0.0571  0.0539  -0.0251 297 PHE A CD2 
2514 C CE1 . PHE A 297 ? 0.1373 0.2780 0.2295 0.0365  0.0642  -0.0161 297 PHE A CE1 
2515 C CE2 . PHE A 297 ? 0.1597 0.2898 0.2356 0.0565  0.0542  -0.0252 297 PHE A CE2 
2516 C CZ  . PHE A 297 ? 0.1532 0.3004 0.2473 0.0457  0.0588  -0.0212 297 PHE A CZ  
2517 N N   . ARG A 298 ? 0.1803 0.3026 0.2116 0.0744  0.0772  -0.0193 298 ARG A N   
2518 C CA  . ARG A 298 ? 0.1895 0.3270 0.2209 0.0880  0.0808  -0.0226 298 ARG A CA  
2519 C C   . ARG A 298 ? 0.2381 0.3560 0.2468 0.0989  0.0755  -0.0295 298 ARG A C   
2520 O O   . ARG A 298 ? 0.2389 0.3558 0.2454 0.1075  0.0719  -0.0344 298 ARG A O   
2521 C CB  . ARG A 298 ? 0.1812 0.3300 0.2294 0.0887  0.0762  -0.0253 298 ARG A CB  
2522 C CG  . ARG A 298 ? 0.2322 0.4009 0.3046 0.0760  0.0796  -0.0197 298 ARG A CG  
2523 C CD  . ARG A 298 ? 0.2211 0.4074 0.3118 0.0777  0.0755  -0.0226 298 ARG A CD  
2524 N NE  . ARG A 298 ? 0.1762 0.3797 0.2903 0.0638  0.0778  -0.0184 298 ARG A NE  
2525 C CZ  . ARG A 298 ? 0.2072 0.4233 0.3391 0.0597  0.0718  -0.0211 298 ARG A CZ  
2526 N NH1 . ARG A 298 ? 0.1600 0.3741 0.2884 0.0694  0.0635  -0.0266 298 ARG A NH1 
2527 N NH2 . ARG A 298 ? 0.1799 0.4099 0.3331 0.0460  0.0737  -0.0183 298 ARG A NH2 
2528 N N   . GLU A 299 ? 0.2471 0.3494 0.2397 0.0983  0.0746  -0.0300 299 GLU A N   
2529 C CA  . GLU A 299 ? 0.2267 0.3102 0.1990 0.1066  0.0683  -0.0373 299 GLU A CA  
2530 C C   . GLU A 299 ? 0.2270 0.2920 0.1975 0.1096  0.0577  -0.0453 299 GLU A C   
2531 O O   . GLU A 299 ? 0.2429 0.2956 0.2019 0.1169  0.0524  -0.0517 299 GLU A O   
2532 C CB  . GLU A 299 ? 0.2753 0.3690 0.2403 0.1158  0.0726  -0.0375 299 GLU A CB  
2533 C CG  . GLU A 299 ? 0.2623 0.3680 0.2231 0.1142  0.0821  -0.0295 299 GLU A CG  
2534 C CD  . GLU A 299 ? 0.4396 0.5297 0.3798 0.1164  0.0787  -0.0315 299 GLU A CD  
2535 O OE1 . GLU A 299 ? 0.5729 0.6702 0.5030 0.1210  0.0843  -0.0275 299 GLU A OE1 
2536 O OE2 . GLU A 299 ? 0.3749 0.4461 0.3094 0.1137  0.0702  -0.0370 299 GLU A OE2 
2537 N N   . LEU A 300 ? 0.2181 0.2804 0.1999 0.1039  0.0545  -0.0446 300 LEU A N   
2538 C CA  . LEU A 300 ? 0.2218 0.2675 0.2040 0.1060  0.0456  -0.0496 300 LEU A CA  
2539 C C   . LEU A 300 ? 0.2481 0.2736 0.2285 0.0970  0.0389  -0.0500 300 LEU A C   
2540 O O   . LEU A 300 ? 0.2509 0.2563 0.2249 0.1001  0.0321  -0.0554 300 LEU A O   
2541 C CB  . LEU A 300 ? 0.2898 0.3510 0.2880 0.1070  0.0464  -0.0470 300 LEU A CB  
2542 C CG  . LEU A 300 ? 0.3517 0.4210 0.3523 0.1163  0.0463  -0.0486 300 LEU A CG  
2543 C CD1 . LEU A 300 ? 0.2505 0.3078 0.2360 0.1245  0.0446  -0.0538 300 LEU A CD1 
2544 C CD2 . LEU A 300 ? 0.3446 0.4436 0.3605 0.1158  0.0536  -0.0439 300 LEU A CD2 
2545 N N   . ILE A 301 ? 0.2111 0.2405 0.1985 0.0844  0.0402  -0.0437 301 ILE A N   
2546 C CA  . ILE A 301 ? 0.2060 0.2180 0.1933 0.0746  0.0339  -0.0430 301 ILE A CA  
2547 C C   . ILE A 301 ? 0.2345 0.2467 0.2185 0.0665  0.0366  -0.0391 301 ILE A C   
2548 O O   . ILE A 301 ? 0.2624 0.2903 0.2525 0.0629  0.0434  -0.0335 301 ILE A O   
2549 C CB  . ILE A 301 ? 0.1987 0.2136 0.1990 0.0684  0.0313  -0.0395 301 ILE A CB  
2550 C CG1 . ILE A 301 ? 0.1763 0.1750 0.1760 0.0588  0.0260  -0.0381 301 ILE A CG1 
2551 C CG2 . ILE A 301 ? 0.2554 0.2932 0.2695 0.0634  0.0367  -0.0344 301 ILE A CG2 
2552 C CD1 . ILE A 301 ? 0.2180 0.2179 0.2269 0.0555  0.0228  -0.0354 301 ILE A CD1 
2553 N N   . SER A 302 ? 0.2123 0.2075 0.1877 0.0639  0.0313  -0.0418 302 SER A N   
2554 C CA  . SER A 302 ? 0.2056 0.2001 0.1769 0.0575  0.0330  -0.0380 302 SER A CA  
2555 C C   . SER A 302 ? 0.2264 0.2216 0.2092 0.0456  0.0327  -0.0322 302 SER A C   
2556 O O   . SER A 302 ? 0.2077 0.1960 0.1967 0.0419  0.0280  -0.0330 302 SER A O   
2557 C CB  . SER A 302 ? 0.2450 0.2234 0.2043 0.0594  0.0266  -0.0439 302 SER A CB  
2558 O OG  . SER A 302 ? 0.2744 0.2523 0.2219 0.0712  0.0265  -0.0507 302 SER A OG  
2559 N N   . VAL A 303 ? 0.2049 0.2077 0.1899 0.0403  0.0381  -0.0261 303 VAL A N   
2560 C CA  . VAL A 303 ? 0.1613 0.1646 0.1571 0.0295  0.0380  -0.0214 303 VAL A CA  
2561 C C   . VAL A 303 ? 0.1760 0.1736 0.1659 0.0252  0.0396  -0.0174 303 VAL A C   
2562 O O   . VAL A 303 ? 0.2083 0.2116 0.1920 0.0284  0.0457  -0.0137 303 VAL A O   
2563 C CB  . VAL A 303 ? 0.1983 0.2189 0.2088 0.0260  0.0436  -0.0176 303 VAL A CB  
2564 C CG1 . VAL A 303 ? 0.2222 0.2415 0.2434 0.0150  0.0423  -0.0146 303 VAL A CG1 
2565 C CG2 . VAL A 303 ? 0.1843 0.2125 0.2003 0.0320  0.0417  -0.0215 303 VAL A CG2 
2566 N N   . PHE A 304 ? 0.1798 0.1665 0.1706 0.0192  0.0346  -0.0175 304 PHE A N   
2567 C CA  . PHE A 304 ? 0.1476 0.1295 0.1350 0.0149  0.0361  -0.0130 304 PHE A CA  
2568 C C   . PHE A 304 ? 0.1586 0.1421 0.1588 0.0056  0.0372  -0.0093 304 PHE A C   
2569 O O   . PHE A 304 ? 0.1702 0.1546 0.1788 0.0027  0.0337  -0.0120 304 PHE A O   
2570 C CB  . PHE A 304 ? 0.1727 0.1419 0.1519 0.0157  0.0293  -0.0164 304 PHE A CB  
2571 C CG  . PHE A 304 ? 0.1783 0.1447 0.1443 0.0244  0.0269  -0.0212 304 PHE A CG  
2572 C CD1 . PHE A 304 ? 0.1967 0.1644 0.1510 0.0290  0.0295  -0.0186 304 PHE A CD1 
2573 C CD2 . PHE A 304 ? 0.1823 0.1436 0.1471 0.0284  0.0214  -0.0286 304 PHE A CD2 
2574 C CE1 . PHE A 304 ? 0.2232 0.1889 0.1638 0.0381  0.0261  -0.0245 304 PHE A CE1 
2575 C CE2 . PHE A 304 ? 0.2160 0.1736 0.1689 0.0365  0.0178  -0.0351 304 PHE A CE2 
2576 C CZ  . PHE A 304 ? 0.2168 0.1773 0.1573 0.0416  0.0197  -0.0337 304 PHE A CZ  
2577 N N   . PHE A 305 ? 0.1533 0.1369 0.1544 0.0018  0.0421  -0.0033 305 PHE A N   
2578 C CA  . PHE A 305 ? 0.1903 0.1731 0.2033 -0.0071 0.0429  -0.0006 305 PHE A CA  
2579 C C   . PHE A 305 ? 0.1930 0.1628 0.2000 -0.0090 0.0397  0.0005  305 PHE A C   
2580 O O   . PHE A 305 ? 0.2012 0.1664 0.1977 -0.0053 0.0416  0.0041  305 PHE A O   
2581 C CB  . PHE A 305 ? 0.1913 0.1830 0.2126 -0.0107 0.0515  0.0058  305 PHE A CB  
2582 C CG  . PHE A 305 ? 0.2046 0.2122 0.2345 -0.0089 0.0549  0.0046  305 PHE A CG  
2583 C CD1 . PHE A 305 ? 0.2827 0.2975 0.3039 -0.0003 0.0589  0.0053  305 PHE A CD1 
2584 C CD2 . PHE A 305 ? 0.2268 0.2434 0.2733 -0.0147 0.0534  0.0019  305 PHE A CD2 
2585 C CE1 . PHE A 305 ? 0.2694 0.2999 0.2988 0.0026  0.0622  0.0041  305 PHE A CE1 
2586 C CE2 . PHE A 305 ? 0.2232 0.2566 0.2788 -0.0122 0.0561  0.0007  305 PHE A CE2 
2587 C CZ  . PHE A 305 ? 0.2516 0.2919 0.2989 -0.0035 0.0608  0.0020  305 PHE A CZ  
2588 N N   . ARG A 306 ? 0.1791 0.1439 0.1920 -0.0135 0.0347  -0.0026 306 ARG A N   
2589 C CA  . ARG A 306 ? 0.1519 0.1057 0.1599 -0.0144 0.0316  -0.0020 306 ARG A CA  
2590 C C   . ARG A 306 ? 0.1932 0.1425 0.2025 -0.0177 0.0365  0.0043  306 ARG A C   
2591 O O   . ARG A 306 ? 0.2019 0.1554 0.2209 -0.0226 0.0413  0.0072  306 ARG A O   
2592 C CB  . ARG A 306 ? 0.1875 0.1385 0.2013 -0.0176 0.0264  -0.0063 306 ARG A CB  
2593 C CG  . ARG A 306 ? 0.2379 0.1909 0.2627 -0.0239 0.0274  -0.0066 306 ARG A CG  
2594 C CD  . ARG A 306 ? 0.2224 0.1723 0.2494 -0.0251 0.0221  -0.0110 306 ARG A CD  
2595 N NE  . ARG A 306 ? 0.2049 0.1563 0.2417 -0.0305 0.0223  -0.0127 306 ARG A NE  
2596 C CZ  . ARG A 306 ? 0.1579 0.1050 0.1966 -0.0322 0.0189  -0.0162 306 ARG A CZ  
2597 N NH1 . ARG A 306 ? 0.1690 0.1113 0.2009 -0.0287 0.0159  -0.0173 306 ARG A NH1 
2598 N NH2 . ARG A 306 ? 0.1608 0.1090 0.2092 -0.0373 0.0187  -0.0190 306 ARG A NH2 
2599 N N   . ASP A 307 ? 0.1782 0.1187 0.1786 -0.0149 0.0352  0.0066  307 ASP A N   
2600 C CA  . ASP A 307 ? 0.1838 0.1163 0.1847 -0.0173 0.0390  0.0128  307 ASP A CA  
2601 C C   . ASP A 307 ? 0.2266 0.1538 0.2373 -0.0232 0.0358  0.0093  307 ASP A C   
2602 O O   . ASP A 307 ? 0.1690 0.0922 0.1771 -0.0215 0.0302  0.0052  307 ASP A O   
2603 C CB  . ASP A 307 ? 0.2033 0.1291 0.1905 -0.0105 0.0376  0.0159  307 ASP A CB  
2604 C CG  . ASP A 307 ? 0.3000 0.2164 0.2859 -0.0113 0.0424  0.0240  307 ASP A CG  
2605 O OD1 . ASP A 307 ? 0.2745 0.1843 0.2700 -0.0172 0.0425  0.0237  307 ASP A OD1 
2606 O OD2 . ASP A 307 ? 0.3426 0.2574 0.3171 -0.0053 0.0460  0.0305  307 ASP A OD2 
2607 N N   . LYS A 308 ? 0.1880 0.1165 0.2108 -0.0299 0.0391  0.0100  308 LYS A N   
2608 C CA  . LYS A 308 ? 0.2042 0.1290 0.2360 -0.0349 0.0352  0.0047  308 LYS A CA  
2609 C C   . LYS A 308 ? 0.2208 0.1330 0.2483 -0.0336 0.0336  0.0064  308 LYS A C   
2610 O O   . LYS A 308 ? 0.1968 0.1084 0.2232 -0.0319 0.0272  0.0012  308 LYS A O   
2611 C CB  . LYS A 308 ? 0.2461 0.1765 0.2930 -0.0423 0.0381  0.0041  308 LYS A CB  
2612 C CG  . LYS A 308 ? 0.2977 0.2275 0.3503 -0.0448 0.0314  -0.0016 308 LYS A CG  
2613 C CD  . LYS A 308 ? 0.2906 0.2299 0.3578 -0.0511 0.0323  -0.0037 308 LYS A CD  
2614 C CE  . LYS A 308 ? 0.5177 0.4510 0.5900 -0.0549 0.0288  -0.0059 308 LYS A CE  
2615 N NZ  . LYS A 308 ? 0.5998 0.5358 0.6723 -0.0538 0.0211  -0.0152 308 LYS A NZ  
2616 N N   . THR A 309 ? 0.1833 0.0876 0.2065 -0.0324 0.0387  0.0144  309 THR A N   
2617 C CA  . THR A 309 ? 0.2143 0.1083 0.2330 -0.0297 0.0362  0.0161  309 THR A CA  
2618 C C   . THR A 309 ? 0.2070 0.0979 0.2166 -0.0234 0.0316  0.0131  309 THR A C   
2619 O O   . THR A 309 ? 0.2056 0.0948 0.2162 -0.0222 0.0263  0.0087  309 THR A O   
2620 C CB  . THR A 309 ? 0.2561 0.1422 0.2701 -0.0281 0.0430  0.0266  309 THR A CB  
2621 O OG1 . THR A 309 ? 0.2710 0.1600 0.2962 -0.0349 0.0466  0.0290  309 THR A OG1 
2622 C CG2 . THR A 309 ? 0.2581 0.1326 0.2658 -0.0235 0.0403  0.0286  309 THR A CG2 
2623 N N   . LEU A 310 ? 0.1817 0.0773 0.1823 -0.0184 0.0315  0.0143  310 LEU A N   
2624 C CA  . LEU A 310 ? 0.1840 0.0811 0.1783 -0.0127 0.0255  0.0107  310 LEU A CA  
2625 C C   . LEU A 310 ? 0.2023 0.1050 0.2030 -0.0152 0.0210  0.0030  310 LEU A C   
2626 O O   . LEU A 310 ? 0.1983 0.0995 0.1989 -0.0128 0.0174  0.0002  310 LEU A O   
2627 C CB  . LEU A 310 ? 0.2165 0.1200 0.2010 -0.0069 0.0245  0.0119  310 LEU A CB  
2628 C CG  . LEU A 310 ? 0.2591 0.1580 0.2335 -0.0019 0.0288  0.0201  310 LEU A CG  
2629 C CD1 . LEU A 310 ? 0.2642 0.1713 0.2281 0.0044  0.0272  0.0193  310 LEU A CD1 
2630 C CD2 . LEU A 310 ? 0.2746 0.1642 0.2445 0.0027  0.0272  0.0233  310 LEU A CD2 
2631 N N   . SER A 311 ? 0.1395 0.0494 0.1459 -0.0191 0.0215  0.0001  311 SER A N   
2632 C CA  . SER A 311 ? 0.1729 0.0879 0.1840 -0.0205 0.0179  -0.0060 311 SER A CA  
2633 C C   . SER A 311 ? 0.1719 0.0864 0.1865 -0.0214 0.0151  -0.0084 311 SER A C   
2634 O O   . SER A 311 ? 0.1618 0.0786 0.1757 -0.0193 0.0118  -0.0115 311 SER A O   
2635 C CB  . SER A 311 ? 0.1552 0.0787 0.1707 -0.0231 0.0189  -0.0077 311 SER A CB  
2636 O OG  . SER A 311 ? 0.1875 0.1150 0.1975 -0.0199 0.0196  -0.0060 311 SER A OG  
2637 N N   . ASP A 312 ? 0.1731 0.0840 0.1914 -0.0245 0.0166  -0.0070 312 ASP A N   
2638 C CA  . ASP A 312 ? 0.2040 0.1119 0.2246 -0.0252 0.0136  -0.0104 312 ASP A CA  
2639 C C   . ASP A 312 ? 0.1951 0.0943 0.2107 -0.0209 0.0124  -0.0093 312 ASP A C   
2640 O O   . ASP A 312 ? 0.1711 0.0684 0.1863 -0.0193 0.0096  -0.0136 312 ASP A O   
2641 C CB  . ASP A 312 ? 0.2101 0.1161 0.2377 -0.0305 0.0152  -0.0098 312 ASP A CB  
2642 C CG  . ASP A 312 ? 0.2740 0.1900 0.3090 -0.0345 0.0146  -0.0139 312 ASP A CG  
2643 O OD1 . ASP A 312 ? 0.2492 0.1721 0.2828 -0.0325 0.0123  -0.0177 312 ASP A OD1 
2644 O OD2 . ASP A 312 ? 0.2735 0.1907 0.3166 -0.0396 0.0167  -0.0131 312 ASP A OD2 
2645 N N   . LEU A 313 ? 0.1775 0.0707 0.1888 -0.0181 0.0150  -0.0038 313 LEU A N   
2646 C CA  . LEU A 313 ? 0.1606 0.0462 0.1678 -0.0128 0.0137  -0.0031 313 LEU A CA  
2647 C C   . LEU A 313 ? 0.1595 0.0508 0.1658 -0.0092 0.0109  -0.0074 313 LEU A C   
2648 O O   . LEU A 313 ? 0.1953 0.0838 0.2014 -0.0059 0.0092  -0.0103 313 LEU A O   
2649 C CB  . LEU A 313 ? 0.1699 0.0477 0.1708 -0.0088 0.0171  0.0041  313 LEU A CB  
2650 C CG  . LEU A 313 ? 0.1932 0.0635 0.1948 -0.0115 0.0211  0.0102  313 LEU A CG  
2651 C CD1 . LEU A 313 ? 0.2655 0.1292 0.2574 -0.0062 0.0254  0.0187  313 LEU A CD1 
2652 C CD2 . LEU A 313 ? 0.2325 0.0937 0.2368 -0.0115 0.0192  0.0092  313 LEU A CD2 
2653 N N   . ILE A 314 ? 0.1421 0.0408 0.1482 -0.0096 0.0110  -0.0078 314 ILE A N   
2654 C CA  . ILE A 314 ? 0.1364 0.0412 0.1443 -0.0074 0.0092  -0.0112 314 ILE A CA  
2655 C C   . ILE A 314 ? 0.1922 0.1015 0.2026 -0.0089 0.0081  -0.0156 314 ILE A C   
2656 O O   . ILE A 314 ? 0.1543 0.0641 0.1657 -0.0057 0.0079  -0.0184 314 ILE A O   
2657 C CB  . ILE A 314 ? 0.1310 0.0439 0.1388 -0.0080 0.0082  -0.0106 314 ILE A CB  
2658 C CG1 . ILE A 314 ? 0.1586 0.0703 0.1612 -0.0044 0.0073  -0.0073 314 ILE A CG1 
2659 C CG2 . ILE A 314 ? 0.1512 0.0722 0.1629 -0.0068 0.0065  -0.0129 314 ILE A CG2 
2660 C CD1 . ILE A 314 ? 0.1763 0.0952 0.1783 -0.0046 0.0052  -0.0083 314 ILE A CD1 
2661 N N   . GLY A 315 ? 0.1488 0.0610 0.1606 -0.0129 0.0080  -0.0167 315 GLY A N   
2662 C CA  . GLY A 315 ? 0.1436 0.0598 0.1571 -0.0132 0.0069  -0.0216 315 GLY A CA  
2663 C C   . GLY A 315 ? 0.1723 0.0824 0.1851 -0.0117 0.0056  -0.0256 315 GLY A C   
2664 O O   . GLY A 315 ? 0.2219 0.1341 0.2345 -0.0093 0.0048  -0.0309 315 GLY A O   
2665 N N   . PHE A 316 ? 0.1691 0.0708 0.1813 -0.0127 0.0055  -0.0237 316 PHE A N   
2666 C CA  . PHE A 316 ? 0.1874 0.0815 0.1991 -0.0122 0.0038  -0.0280 316 PHE A CA  
2667 C C   . PHE A 316 ? 0.1830 0.0655 0.1916 -0.0086 0.0040  -0.0259 316 PHE A C   
2668 O O   . PHE A 316 ? 0.2181 0.0937 0.2246 -0.0061 0.0027  -0.0306 316 PHE A O   
2669 C CB  . PHE A 316 ? 0.1715 0.0650 0.1878 -0.0185 0.0031  -0.0293 316 PHE A CB  
2670 C CG  . PHE A 316 ? 0.2192 0.1238 0.2393 -0.0210 0.0021  -0.0329 316 PHE A CG  
2671 C CD1 . PHE A 316 ? 0.2831 0.1951 0.3061 -0.0236 0.0040  -0.0289 316 PHE A CD1 
2672 C CD2 . PHE A 316 ? 0.2739 0.1813 0.2942 -0.0197 -0.0008 -0.0409 316 PHE A CD2 
2673 C CE1 . PHE A 316 ? 0.3026 0.2241 0.3292 -0.0251 0.0030  -0.0325 316 PHE A CE1 
2674 C CE2 . PHE A 316 ? 0.3073 0.2251 0.3311 -0.0210 -0.0022 -0.0447 316 PHE A CE2 
2675 C CZ  . PHE A 316 ? 0.3069 0.2315 0.3342 -0.0238 -0.0003 -0.0403 316 PHE A CZ  
2676 N N   . SER A 317 ? 0.1800 0.0595 0.1879 -0.0075 0.0057  -0.0195 317 SER A N   
2677 C CA  . SER A 317 ? 0.1828 0.0505 0.1882 -0.0034 0.0058  -0.0168 317 SER A CA  
2678 C C   . SER A 317 ? 0.1811 0.0497 0.1842 0.0045  0.0058  -0.0171 317 SER A C   
2679 O O   . SER A 317 ? 0.2331 0.0959 0.2345 0.0099  0.0046  -0.0204 317 SER A O   
2680 C CB  . SER A 317 ? 0.1877 0.0508 0.1936 -0.0056 0.0084  -0.0090 317 SER A CB  
2681 O OG  . SER A 317 ? 0.2056 0.0556 0.2098 -0.0022 0.0085  -0.0062 317 SER A OG  
2682 N N   . TYR A 318 ? 0.1706 0.0470 0.1741 0.0054  0.0072  -0.0144 318 TYR A N   
2683 C CA  . TYR A 318 ? 0.1713 0.0479 0.1739 0.0129  0.0077  -0.0129 318 TYR A CA  
2684 C C   . TYR A 318 ? 0.1679 0.0526 0.1727 0.0176  0.0067  -0.0180 318 TYR A C   
2685 O O   . TYR A 318 ? 0.1700 0.0591 0.1747 0.0245  0.0058  -0.0169 318 TYR A O   
2686 C CB  . TYR A 318 ? 0.1613 0.0488 0.1634 0.0117  0.0070  -0.0094 318 TYR A CB  
2687 C CG  . TYR A 318 ? 0.1680 0.0490 0.1650 0.0110  0.0083  -0.0034 318 TYR A CG  
2688 C CD1 . TYR A 318 ? 0.1840 0.0498 0.1770 0.0134  0.0106  0.0011  318 TYR A CD1 
2689 C CD2 . TYR A 318 ? 0.1975 0.0869 0.1934 0.0084  0.0079  -0.0019 318 TYR A CD2 
2690 C CE1 . TYR A 318 ? 0.2004 0.0611 0.1875 0.0136  0.0131  0.0083  318 TYR A CE1 
2691 C CE2 . TYR A 318 ? 0.2187 0.1038 0.2081 0.0091  0.0096  0.0037  318 TYR A CE2 
2692 C CZ  . TYR A 318 ? 0.1900 0.0620 0.1748 0.0119  0.0125  0.0093  318 TYR A CZ  
2693 O OH  . TYR A 318 ? 0.2282 0.0975 0.2055 0.0133  0.0152  0.0160  318 TYR A OH  
2694 N N   . HIS A 319 ? 0.1660 0.0546 0.1726 0.0149  0.0069  -0.0233 319 HIS A N   
2695 C CA  . HIS A 319 ? 0.1630 0.0601 0.1702 0.0207  0.0070  -0.0272 319 HIS A CA  
2696 C C   . HIS A 319 ? 0.1819 0.0696 0.1866 0.0286  0.0066  -0.0294 319 HIS A C   
2697 O O   . HIS A 319 ? 0.2234 0.1200 0.2287 0.0357  0.0070  -0.0307 319 HIS A O   
2698 C CB  . HIS A 319 ? 0.1611 0.0617 0.1676 0.0184  0.0071  -0.0328 319 HIS A CB  
2699 C CG  . HIS A 319 ? 0.1738 0.0615 0.1774 0.0174  0.0055  -0.0384 319 HIS A CG  
2700 N ND1 . HIS A 319 ? 0.2725 0.1563 0.2724 0.0236  0.0050  -0.0443 319 HIS A ND1 
2701 C CD2 . HIS A 319 ? 0.2153 0.0975 0.2175 0.0101  0.0041  -0.0376 319 HIS A CD2 
2702 C CE1 . HIS A 319 ? 0.2769 0.1517 0.2739 0.0193  0.0038  -0.0470 319 HIS A CE1 
2703 N NE2 . HIS A 319 ? 0.3135 0.1874 0.3124 0.0112  0.0029  -0.0429 319 HIS A NE2 
2704 N N   . ALA A 320 ? 0.1904 0.0614 0.1916 0.0275  0.0060  -0.0289 320 ALA A N   
2705 C CA  . ALA A 320 ? 0.2546 0.1174 0.2560 0.0334  0.0073  -0.0305 320 ALA A CA  
2706 C C   . ALA A 320 ? 0.3206 0.1791 0.3224 0.0389  0.0060  -0.0243 320 ALA A C   
2707 O O   . ALA A 320 ? 0.4784 0.3299 0.4802 0.0446  0.0061  -0.0248 320 ALA A O   
2708 C CB  . ALA A 320 ? 0.2996 0.1493 0.2946 0.0279  0.0077  -0.0325 320 ALA A CB  
2709 N N   . TRP A 321 ? 0.2050 0.0668 0.2044 0.0383  0.0056  -0.0183 321 TRP A N   
2710 C CA  . TRP A 321 ? 0.2119 0.0704 0.2076 0.0449  0.0049  -0.0119 321 TRP A CA  
2711 C C   . TRP A 321 ? 0.2053 0.0805 0.2032 0.0527  0.0029  -0.0123 321 TRP A C   
2712 O O   . TRP A 321 ? 0.2365 0.1286 0.2401 0.0495  0.0028  -0.0149 321 TRP A O   
2713 C CB  . TRP A 321 ? 0.2097 0.0661 0.2018 0.0404  0.0055  -0.0052 321 TRP A CB  
2714 C CG  . TRP A 321 ? 0.2131 0.0618 0.2063 0.0314  0.0071  -0.0025 321 TRP A CG  
2715 C CD1 . TRP A 321 ? 0.2084 0.0576 0.2060 0.0229  0.0067  -0.0068 321 TRP A CD1 
2716 C CD2 . TRP A 321 ? 0.2231 0.0643 0.2114 0.0311  0.0087  0.0057  321 TRP A CD2 
2717 N NE1 . TRP A 321 ? 0.2143 0.0573 0.2115 0.0168  0.0081  -0.0020 321 TRP A NE1 
2718 C CE2 . TRP A 321 ? 0.2234 0.0612 0.2152 0.0215  0.0102  0.0061  321 TRP A CE2 
2719 C CE3 . TRP A 321 ? 0.2333 0.0713 0.2135 0.0392  0.0090  0.0130  321 TRP A CE3 
2720 C CZ2 . TRP A 321 ? 0.2334 0.0644 0.2220 0.0191  0.0134  0.0141  321 TRP A CZ2 
2721 C CZ3 . TRP A 321 ? 0.2582 0.0888 0.2335 0.0373  0.0120  0.0211  321 TRP A CZ3 
2722 C CH2 . TRP A 321 ? 0.2440 0.0710 0.2240 0.0270  0.0148  0.0218  321 TRP A CH2 
2723 N N   . ASN A 322 ? 0.2224 0.0951 0.2174 0.0622  0.0014  -0.0088 322 ASN A N   
2724 C CA  . ASN A 322 ? 0.2121 0.1044 0.2116 0.0680  -0.0016 -0.0079 322 ASN A CA  
2725 C C   . ASN A 322 ? 0.2249 0.1279 0.2260 0.0607  -0.0033 -0.0056 322 ASN A C   
2726 O O   . ASN A 322 ? 0.2306 0.1232 0.2251 0.0571  -0.0028 -0.0015 322 ASN A O   
2727 C CB  . ASN A 322 ? 0.2650 0.1509 0.2592 0.0799  -0.0037 -0.0037 322 ASN A CB  
2728 C CG  . ASN A 322 ? 0.4243 0.3323 0.4257 0.0878  -0.0074 -0.0046 322 ASN A CG  
2729 O OD1 . ASN A 322 ? 0.4975 0.4236 0.5091 0.0856  -0.0070 -0.0089 322 ASN A OD1 
2730 N ND2 . ASN A 322 ? 0.4190 0.3264 0.4156 0.0973  -0.0108 -0.0002 322 ASN A ND2 
2731 N N   . ALA A 323 ? 0.1990 0.1225 0.2097 0.0583  -0.0049 -0.0083 323 ALA A N   
2732 C CA  . ALA A 323 ? 0.1806 0.1127 0.1939 0.0504  -0.0066 -0.0079 323 ALA A CA  
2733 C C   . ALA A 323 ? 0.1953 0.1256 0.2017 0.0538  -0.0104 -0.0041 323 ALA A C   
2734 O O   . ALA A 323 ? 0.1757 0.1014 0.1770 0.0482  -0.0101 -0.0026 323 ALA A O   
2735 C CB  . ALA A 323 ? 0.1924 0.1456 0.2190 0.0480  -0.0078 -0.0109 323 ALA A CB  
2736 N N   . GLU A 324 ? 0.2139 0.1491 0.2194 0.0639  -0.0140 -0.0028 324 GLU A N   
2737 C CA  . GLU A 324 ? 0.2315 0.1663 0.2284 0.0688  -0.0182 0.0007  324 GLU A CA  
2738 C C   . GLU A 324 ? 0.2535 0.1668 0.2361 0.0689  -0.0141 0.0071  324 GLU A C   
2739 O O   . GLU A 324 ? 0.2362 0.1481 0.2108 0.0680  -0.0149 0.0100  324 GLU A O   
2740 C CB  . GLU A 324 ? 0.2870 0.2319 0.2852 0.0811  -0.0233 0.0010  324 GLU A CB  
2741 C CG  . GLU A 324 ? 0.4229 0.3534 0.4147 0.0906  -0.0206 0.0048  324 GLU A CG  
2742 C CD  . GLU A 324 ? 0.6679 0.6102 0.6615 0.1041  -0.0260 0.0050  324 GLU A CD  
2743 O OE1 . GLU A 324 ? 0.7872 0.7156 0.7725 0.1143  -0.0248 0.0094  324 GLU A OE1 
2744 O OE2 . GLU A 324 ? 0.6877 0.6528 0.6919 0.1045  -0.0318 0.0007  324 GLU A OE2 
2745 N N   . ASP A 325 ? 0.2552 0.1515 0.2351 0.0698  -0.0094 0.0092  325 ASP A N   
2746 C CA  . ASP A 325 ? 0.2316 0.1073 0.2010 0.0686  -0.0049 0.0159  325 ASP A CA  
2747 C C   . ASP A 325 ? 0.2220 0.0945 0.1927 0.0565  -0.0012 0.0152  325 ASP A C   
2748 O O   . ASP A 325 ? 0.2306 0.0939 0.1934 0.0548  0.0019  0.0213  325 ASP A O   
2749 C CB  . ASP A 325 ? 0.2463 0.1038 0.2145 0.0730  -0.0018 0.0173  325 ASP A CB  
2750 C CG  . ASP A 325 ? 0.4152 0.2760 0.3813 0.0865  -0.0053 0.0188  325 ASP A CG  
2751 O OD1 . ASP A 325 ? 0.4063 0.2687 0.3639 0.0937  -0.0075 0.0248  325 ASP A OD1 
2752 O OD2 . ASP A 325 ? 0.4700 0.3351 0.4432 0.0896  -0.0059 0.0138  325 ASP A OD2 
2753 N N   . ALA A 326 ? 0.2056 0.0865 0.1858 0.0486  -0.0010 0.0086  326 ALA A N   
2754 C CA  . ALA A 326 ? 0.1960 0.0767 0.1778 0.0383  0.0015  0.0075  326 ALA A CA  
2755 C C   . ALA A 326 ? 0.1956 0.0868 0.1739 0.0376  -0.0009 0.0086  326 ALA A C   
2756 O O   . ALA A 326 ? 0.1930 0.0795 0.1664 0.0336  0.0020  0.0118  326 ALA A O   
2757 C CB  . ALA A 326 ? 0.2039 0.0924 0.1952 0.0322  0.0017  0.0007  326 ALA A CB  
2758 N N   . VAL A 327 ? 0.1860 0.0919 0.1674 0.0418  -0.0064 0.0056  327 VAL A N   
2759 C CA  . VAL A 327 ? 0.1929 0.1083 0.1710 0.0420  -0.0102 0.0047  327 VAL A CA  
2760 C C   . VAL A 327 ? 0.2036 0.1117 0.1672 0.0491  -0.0096 0.0114  327 VAL A C   
2761 O O   . VAL A 327 ? 0.2089 0.1166 0.1656 0.0472  -0.0084 0.0129  327 VAL A O   
2762 C CB  . VAL A 327 ? 0.1840 0.1169 0.1711 0.0445  -0.0170 -0.0010 327 VAL A CB  
2763 C CG1 . VAL A 327 ? 0.1867 0.1281 0.1695 0.0459  -0.0223 -0.0033 327 VAL A CG1 
2764 C CG2 . VAL A 327 ? 0.1613 0.1020 0.1624 0.0364  -0.0159 -0.0060 327 VAL A CG2 
2765 N N   . ARG A 328 ? 0.2280 0.1297 0.1859 0.0582  -0.0099 0.0161  328 ARG A N   
2766 C CA  . ARG A 328 ? 0.2562 0.1492 0.1987 0.0660  -0.0082 0.0245  328 ARG A CA  
2767 C C   . ARG A 328 ? 0.2593 0.1374 0.1972 0.0595  0.0003  0.0309  328 ARG A C   
2768 O O   . ARG A 328 ? 0.2719 0.1489 0.1990 0.0617  0.0027  0.0363  328 ARG A O   
2769 C CB  . ARG A 328 ? 0.2498 0.1362 0.1878 0.0772  -0.0093 0.0292  328 ARG A CB  
2770 C CG  . ARG A 328 ? 0.2863 0.1907 0.2291 0.0849  -0.0181 0.0234  328 ARG A CG  
2771 C CD  . ARG A 328 ? 0.3679 0.2665 0.3068 0.0973  -0.0193 0.0279  328 ARG A CD  
2772 N NE  . ARG A 328 ? 0.3388 0.2572 0.2884 0.1025  -0.0270 0.0208  328 ARG A NE  
2773 C CZ  . ARG A 328 ? 0.3292 0.2483 0.2806 0.1127  -0.0289 0.0218  328 ARG A CZ  
2774 N NH1 . ARG A 328 ? 0.3411 0.2394 0.2832 0.1194  -0.0241 0.0295  328 ARG A NH1 
2775 N NH2 . ARG A 328 ? 0.3792 0.3197 0.3430 0.1163  -0.0356 0.0150  328 ARG A NH2 
2776 N N   . ASP A 329 ? 0.2346 0.1028 0.1814 0.0517  0.0048  0.0299  329 ASP A N   
2777 C CA  . ASP A 329 ? 0.2393 0.0954 0.1856 0.0442  0.0124  0.0349  329 ASP A CA  
2778 C C   . ASP A 329 ? 0.2278 0.0944 0.1745 0.0379  0.0130  0.0324  329 ASP A C   
2779 O O   . ASP A 329 ? 0.2364 0.0993 0.1765 0.0371  0.0183  0.0389  329 ASP A O   
2780 C CB  . ASP A 329 ? 0.2420 0.0880 0.1993 0.0368  0.0150  0.0315  329 ASP A CB  
2781 C CG  . ASP A 329 ? 0.2505 0.0867 0.2111 0.0282  0.0218  0.0357  329 ASP A CG  
2782 O OD1 . ASP A 329 ? 0.2919 0.1197 0.2498 0.0296  0.0250  0.0431  329 ASP A OD1 
2783 O OD2 . ASP A 329 ? 0.2538 0.0955 0.2220 0.0193  0.0227  0.0309  329 ASP A OD2 
2784 N N   . PHE A 330 ? 0.2297 0.1093 0.1844 0.0339  0.0082  0.0234  330 PHE A N   
2785 C CA  . PHE A 330 ? 0.2226 0.1109 0.1787 0.0283  0.0084  0.0200  330 PHE A CA  
2786 C C   . PHE A 330 ? 0.2074 0.1019 0.1514 0.0350  0.0066  0.0222  330 PHE A C   
2787 O O   . PHE A 330 ? 0.2110 0.1053 0.1496 0.0334  0.0110  0.0253  330 PHE A O   
2788 C CB  . PHE A 330 ? 0.1908 0.0898 0.1577 0.0239  0.0036  0.0110  330 PHE A CB  
2789 C CG  . PHE A 330 ? 0.1990 0.1048 0.1690 0.0179  0.0038  0.0071  330 PHE A CG  
2790 C CD1 . PHE A 330 ? 0.2426 0.1453 0.2186 0.0103  0.0081  0.0066  330 PHE A CD1 
2791 C CD2 . PHE A 330 ? 0.2180 0.1334 0.1858 0.0202  -0.0011 0.0029  330 PHE A CD2 
2792 C CE1 . PHE A 330 ? 0.2341 0.1433 0.2130 0.0060  0.0080  0.0030  330 PHE A CE1 
2793 C CE2 . PHE A 330 ? 0.2355 0.1554 0.2062 0.0154  -0.0011 -0.0010 330 PHE A CE2 
2794 C CZ  . PHE A 330 ? 0.2059 0.1227 0.1818 0.0087  0.0037  -0.0005 330 PHE A CZ  
2795 N N   . ILE A 331 ? 0.2113 0.1129 0.1510 0.0431  -0.0002 0.0199  331 ILE A N   
2796 C CA  . ILE A 331 ? 0.2221 0.1304 0.1486 0.0514  -0.0035 0.0206  331 ILE A CA  
2797 C C   . ILE A 331 ? 0.2418 0.1401 0.1538 0.0570  0.0037  0.0321  331 ILE A C   
2798 O O   . ILE A 331 ? 0.2705 0.1720 0.1714 0.0603  0.0058  0.0345  331 ILE A O   
2799 C CB  . ILE A 331 ? 0.2458 0.1640 0.1717 0.0597  -0.0129 0.0159  331 ILE A CB  
2800 C CG1 . ILE A 331 ? 0.2607 0.1897 0.2032 0.0532  -0.0188 0.0056  331 ILE A CG1 
2801 C CG2 . ILE A 331 ? 0.2661 0.1912 0.1759 0.0701  -0.0173 0.0161  331 ILE A CG2 
2802 C CD1 . ILE A 331 ? 0.2821 0.2183 0.2277 0.0478  -0.0215 -0.0017 331 ILE A CD1 
2803 N N   . GLY A 332 ? 0.2520 0.1376 0.1635 0.0590  0.0078  0.0397  332 GLY A N   
2804 C CA  . GLY A 332 ? 0.2979 0.1717 0.1973 0.0635  0.0159  0.0524  332 GLY A CA  
2805 C C   . GLY A 332 ? 0.2717 0.1421 0.1736 0.0549  0.0249  0.0565  332 GLY A C   
2806 O O   . GLY A 332 ? 0.2872 0.1561 0.1771 0.0595  0.0310  0.0654  332 GLY A O   
2807 N N   . ARG A 333 ? 0.2881 0.1582 0.2056 0.0431  0.0260  0.0506  333 ARG A N   
2808 C CA  . ARG A 333 ? 0.2517 0.1220 0.1740 0.0350  0.0336  0.0531  333 ARG A CA  
2809 C C   . ARG A 333 ? 0.2816 0.1658 0.1965 0.0376  0.0320  0.0493  333 ARG A C   
2810 O O   . ARG A 333 ? 0.3015 0.1873 0.2119 0.0373  0.0394  0.0554  333 ARG A O   
2811 C CB  . ARG A 333 ? 0.2527 0.1211 0.1926 0.0232  0.0336  0.0465  333 ARG A CB  
2812 C CG  . ARG A 333 ? 0.2464 0.0992 0.1933 0.0203  0.0362  0.0500  333 ARG A CG  
2813 C CD  . ARG A 333 ? 0.2496 0.1030 0.2118 0.0108  0.0339  0.0409  333 ARG A CD  
2814 N NE  . ARG A 333 ? 0.2358 0.0792 0.2065 0.0071  0.0343  0.0409  333 ARG A NE  
2815 C CZ  . ARG A 333 ? 0.2872 0.1290 0.2675 -0.0008 0.0375  0.0424  333 ARG A CZ  
2816 N NH1 . ARG A 333 ? 0.3202 0.1673 0.3030 -0.0057 0.0430  0.0461  333 ARG A NH1 
2817 N NH2 . ARG A 333 ? 0.2925 0.1269 0.2795 -0.0033 0.0351  0.0402  333 ARG A NH2 
2818 N N   . LEU A 334 ? 0.2510 0.1456 0.1658 0.0401  0.0228  0.0391  334 LEU A N   
2819 C CA  . LEU A 334 ? 0.2421 0.1480 0.1492 0.0438  0.0203  0.0342  334 LEU A CA  
2820 C C   . LEU A 334 ? 0.2883 0.1957 0.1755 0.0559  0.0220  0.0412  334 LEU A C   
2821 O O   . LEU A 334 ? 0.2811 0.1939 0.1595 0.0589  0.0262  0.0429  334 LEU A O   
2822 C CB  . LEU A 334 ? 0.2317 0.1462 0.1443 0.0437  0.0096  0.0219  334 LEU A CB  
2823 C CG  . LEU A 334 ? 0.2152 0.1305 0.1450 0.0331  0.0083  0.0151  334 LEU A CG  
2824 C CD1 . LEU A 334 ? 0.2468 0.1704 0.1821 0.0335  -0.0013 0.0048  334 LEU A CD1 
2825 C CD2 . LEU A 334 ? 0.2697 0.1863 0.2034 0.0269  0.0142  0.0153  334 LEU A CD2 
2826 N N   . LYS A 335 ? 0.2780 0.1816 0.1569 0.0642  0.0189  0.0452  335 LYS A N   
2827 C CA  . LYS A 335 ? 0.3098 0.2142 0.1678 0.0773  0.0210  0.0535  335 LYS A CA  
2828 C C   . LYS A 335 ? 0.3646 0.2615 0.2172 0.0762  0.0347  0.0674  335 LYS A C   
2829 O O   . LYS A 335 ? 0.3763 0.2789 0.2131 0.0842  0.0388  0.0722  335 LYS A O   
2830 C CB  . LYS A 335 ? 0.3311 0.2312 0.1830 0.0863  0.0160  0.0569  335 LYS A CB  
2831 C CG  . LYS A 335 ? 0.5511 0.4520 0.3790 0.1019  0.0176  0.0662  335 LYS A CG  
2832 C CD  . LYS A 335 ? 0.6189 0.5347 0.4337 0.1093  0.0120  0.0583  335 LYS A CD  
2833 C CE  . LYS A 335 ? 0.6923 0.6114 0.4815 0.1272  0.0111  0.0656  335 LYS A CE  
2834 N NZ  . LYS A 335 ? 0.7644 0.6982 0.5402 0.1350  0.0048  0.0557  335 LYS A NZ  
2835 N N   . LYS A 336 ? 0.3141 0.1989 0.1802 0.0664  0.0420  0.0738  336 LYS A N   
2836 C CA  . LYS A 336 ? 0.3681 0.2464 0.2337 0.0631  0.0554  0.0869  336 LYS A CA  
2837 C C   . LYS A 336 ? 0.3513 0.2413 0.2199 0.0585  0.0598  0.0837  336 LYS A C   
2838 O O   . LYS A 336 ? 0.3961 0.2890 0.2549 0.0627  0.0693  0.0936  336 LYS A O   
2839 C CB  . LYS A 336 ? 0.4156 0.2784 0.2982 0.0523  0.0606  0.0917  336 LYS A CB  
2840 C CG  . LYS A 336 ? 0.6039 0.4567 0.4841 0.0578  0.0566  0.0942  336 LYS A CG  
2841 C CD  . LYS A 336 ? 0.7376 0.5791 0.6338 0.0482  0.0617  0.0984  336 LYS A CD  
2842 C CE  . LYS A 336 ? 0.8039 0.6361 0.7022 0.0515  0.0551  0.0956  336 LYS A CE  
2843 N NZ  . LYS A 336 ? 0.8466 0.6669 0.7506 0.0488  0.0598  0.1030  336 LYS A NZ  
2844 N N   . ILE A 337 ? 0.3341 0.2313 0.2160 0.0505  0.0537  0.0707  337 ILE A N   
2845 C CA  . ILE A 337 ? 0.3528 0.2617 0.2364 0.0481  0.0567  0.0667  337 ILE A CA  
2846 C C   . ILE A 337 ? 0.3851 0.3040 0.2475 0.0616  0.0544  0.0652  337 ILE A C   
2847 O O   . ILE A 337 ? 0.3842 0.3100 0.2389 0.0654  0.0625  0.0704  337 ILE A O   
2848 C CB  . ILE A 337 ? 0.3140 0.2277 0.2136 0.0392  0.0494  0.0531  337 ILE A CB  
2849 C CG1 . ILE A 337 ? 0.2790 0.1845 0.1980 0.0269  0.0519  0.0540  337 ILE A CG1 
2850 C CG2 . ILE A 337 ? 0.3228 0.2482 0.2224 0.0390  0.0518  0.0486  337 ILE A CG2 
2851 C CD1 . ILE A 337 ? 0.3034 0.2120 0.2355 0.0201  0.0438  0.0416  337 ILE A CD1 
2852 N N   . HIS A 338 ? 0.3197 0.2408 0.1733 0.0693  0.0431  0.0571  338 HIS A N   
2853 C CA  . HIS A 338 ? 0.3339 0.2646 0.1670 0.0828  0.0384  0.0529  338 HIS A CA  
2854 C C   . HIS A 338 ? 0.4120 0.3423 0.2252 0.0938  0.0481  0.0675  338 HIS A C   
2855 O O   . HIS A 338 ? 0.4202 0.3598 0.2183 0.1027  0.0512  0.0677  338 HIS A O   
2856 C CB  . HIS A 338 ? 0.3607 0.2931 0.1910 0.0881  0.0243  0.0429  338 HIS A CB  
2857 C CG  . HIS A 338 ? 0.4470 0.3897 0.2580 0.1018  0.0164  0.0355  338 HIS A CG  
2858 N ND1 . HIS A 338 ? 0.5253 0.4695 0.3182 0.1153  0.0124  0.0393  338 HIS A ND1 
2859 C CD2 . HIS A 338 ? 0.4680 0.4196 0.2754 0.1045  0.0106  0.0231  338 HIS A CD2 
2860 C CE1 . HIS A 338 ? 0.5621 0.5169 0.3406 0.1257  0.0042  0.0291  338 HIS A CE1 
2861 N NE2 . HIS A 338 ? 0.4903 0.4490 0.2775 0.1192  0.0030  0.0190  338 HIS A NE2 
2862 N N   . GLU A 339 ? 0.3774 0.2964 0.1897 0.0942  0.0537  0.0804  339 GLU A N   
2863 C CA  . GLU A 339 ? 0.5156 0.4349 0.3152 0.1029  0.0624  0.0932  339 GLU A CA  
2864 C C   . GLU A 339 ? 0.4844 0.4045 0.2953 0.0945  0.0766  0.1028  339 GLU A C   
2865 O O   . GLU A 339 ? 0.5456 0.4702 0.3492 0.1009  0.0836  0.1110  339 GLU A O   
2866 C CB  . GLU A 339 ? 0.6257 0.5343 0.4255 0.1055  0.0610  0.1001  339 GLU A CB  
2867 C CG  . GLU A 339 ? 0.7743 0.6870 0.5614 0.1173  0.0473  0.0917  339 GLU A CG  
2868 C CD  . GLU A 339 ? 0.9446 0.8729 0.7145 0.1295  0.0413  0.0834  339 GLU A CD  
2869 O OE1 . GLU A 339 ? 1.0213 0.9544 0.7804 0.1379  0.0474  0.0901  339 GLU A OE1 
2870 O OE2 . GLU A 339 ? 0.9813 0.9167 0.7495 0.1306  0.0303  0.0696  339 GLU A OE2 
2871 N N   . SER A 340 ? 0.4873 0.4046 0.3164 0.0809  0.0806  0.1016  340 SER A N   
2872 C CA  . SER A 340 ? 0.5099 0.4292 0.3547 0.0713  0.0928  0.1096  340 SER A CA  
2873 C C   . SER A 340 ? 0.5387 0.4738 0.3801 0.0740  0.0974  0.1070  340 SER A C   
2874 O O   . SER A 340 ? 0.5381 0.4782 0.3891 0.0695  0.1076  0.1147  340 SER A O   
2875 C CB  . SER A 340 ? 0.5316 0.4423 0.4006 0.0551  0.0938  0.1077  340 SER A CB  
2876 O OG  . SER A 340 ? 0.5516 0.4686 0.4256 0.0509  0.0892  0.0966  340 SER A OG  
2877 N N   . VAL A 341 ? 0.4657 0.4089 0.2949 0.0811  0.0898  0.0955  341 VAL A N   
2878 C CA  . VAL A 341 ? 0.5249 0.4828 0.3522 0.0840  0.0931  0.0907  341 VAL A CA  
2879 C C   . VAL A 341 ? 0.5476 0.5139 0.3519 0.1004  0.0867  0.0848  341 VAL A C   
2880 O O   . VAL A 341 ? 0.5500 0.5123 0.3413 0.1083  0.0770  0.0804  341 VAL A O   
2881 C CB  . VAL A 341 ? 0.4763 0.4370 0.3161 0.0758  0.0882  0.0783  341 VAL A CB  
2882 C CG1 . VAL A 341 ? 0.5237 0.4787 0.3904 0.0591  0.0932  0.0822  341 VAL A CG1 
2883 C CG2 . VAL A 341 ? 0.4646 0.4213 0.3020 0.0776  0.0717  0.0633  341 VAL A CG2 
2884 N N   . ASP A 342 ? 0.5975 0.5765 0.3982 0.1056  0.0916  0.0842  342 ASP A N   
2885 C CA  . ASP A 342 ? 0.6775 0.6649 0.4580 0.1213  0.0858  0.0780  342 ASP A CA  
2886 C C   . ASP A 342 ? 0.6491 0.6422 0.4245 0.1254  0.0747  0.0600  342 ASP A C   
2887 O O   . ASP A 342 ? 0.7411 0.7402 0.5017 0.1378  0.0673  0.0520  342 ASP A O   
2888 C CB  . ASP A 342 ? 0.8325 0.8299 0.6098 0.1269  0.0971  0.0881  342 ASP A CB  
2889 C CG  . ASP A 342 ? 0.9980 1.0032 0.7921 0.1178  0.1067  0.0904  342 ASP A CG  
2890 O OD1 . ASP A 342 ? 0.9870 0.9875 0.7993 0.1042  0.1084  0.0901  342 ASP A OD1 
2891 O OD2 . ASP A 342 ? 1.0522 1.0691 0.8416 0.1246  0.1126  0.0926  342 ASP A OD2 
2892 N N   . PHE A 343 ? 0.4777 0.4684 0.2660 0.1155  0.0728  0.0527  343 PHE A N   
2893 C CA  . PHE A 343 ? 0.4015 0.3949 0.1883 0.1176  0.0624  0.0351  343 PHE A CA  
2894 C C   . PHE A 343 ? 0.3749 0.3580 0.1674 0.1113  0.0508  0.0262  343 PHE A C   
2895 O O   . PHE A 343 ? 0.3854 0.3606 0.1825 0.1066  0.0504  0.0335  343 PHE A O   
2896 C CB  . PHE A 343 ? 0.4069 0.4068 0.2074 0.1114  0.0695  0.0336  343 PHE A CB  
2897 C CG  . PHE A 343 ? 0.3855 0.3812 0.2065 0.0966  0.0780  0.0425  343 PHE A CG  
2898 C CD1 . PHE A 343 ? 0.4300 0.4278 0.2585 0.0918  0.0913  0.0587  343 PHE A CD1 
2899 C CD2 . PHE A 343 ? 0.3580 0.3469 0.1987 0.0847  0.0692  0.0332  343 PHE A CD2 
2900 C CE1 . PHE A 343 ? 0.4125 0.4061 0.2633 0.0771  0.0973  0.0652  343 PHE A CE1 
2901 C CE2 . PHE A 343 ? 0.3548 0.3401 0.2181 0.0703  0.0741  0.0393  343 PHE A CE2 
2902 C CZ  . PHE A 343 ? 0.3889 0.3766 0.2574 0.0665  0.0875  0.0545  343 PHE A CZ  
2903 N N   . GLN A 344 ? 0.3632 0.3461 0.1627 0.1092  0.0400  0.0100  344 GLN A N   
2904 C CA  . GLN A 344 ? 0.3299 0.3045 0.1440 0.1002  0.0281  0.0011  344 GLN A CA  
2905 C C   . GLN A 344 ? 0.3155 0.2859 0.1541 0.0849  0.0322  0.0035  344 GLN A C   
2906 O O   . GLN A 344 ? 0.3320 0.3051 0.1786 0.0822  0.0322  -0.0033 344 GLN A O   
2907 C CB  . GLN A 344 ? 0.3366 0.3119 0.1465 0.1053  0.0145  -0.0168 344 GLN A CB  
2908 C CG  . GLN A 344 ? 0.3945 0.3740 0.1811 0.1203  0.0070  -0.0216 344 GLN A CG  
2909 C CD  . GLN A 344 ? 0.4166 0.3963 0.2064 0.1225  -0.0087 -0.0401 344 GLN A CD  
2910 O OE1 . GLN A 344 ? 0.4208 0.4009 0.2093 0.1251  -0.0193 -0.0456 344 GLN A OE1 
2911 N NE2 . GLN A 344 ? 0.4210 0.4006 0.2182 0.1206  -0.0101 -0.0489 344 GLN A NE2 
2912 N N   . PRO A 345 ? 0.3072 0.2712 0.1577 0.0755  0.0352  0.0121  345 PRO A N   
2913 C CA  . PRO A 345 ? 0.2878 0.2491 0.1601 0.0621  0.0392  0.0141  345 PRO A CA  
2914 C C   . PRO A 345 ? 0.2725 0.2299 0.1578 0.0555  0.0288  0.0022  345 PRO A C   
2915 O O   . PRO A 345 ? 0.2781 0.2323 0.1607 0.0576  0.0189  -0.0049 345 PRO A O   
2916 C CB  . PRO A 345 ? 0.2972 0.2512 0.1750 0.0563  0.0443  0.0257  345 PRO A CB  
2917 C CG  . PRO A 345 ? 0.3281 0.2785 0.1915 0.0648  0.0372  0.0251  345 PRO A CG  
2918 C CD  . PRO A 345 ? 0.3030 0.2616 0.1466 0.0782  0.0344  0.0197  345 PRO A CD  
2919 N N   . VAL A 346 ? 0.2211 0.1796 0.1213 0.0476  0.0314  0.0006  346 VAL A N   
2920 C CA  . VAL A 346 ? 0.2237 0.1777 0.1374 0.0404  0.0238  -0.0076 346 VAL A CA  
2921 C C   . VAL A 346 ? 0.2460 0.1965 0.1747 0.0299  0.0273  -0.0015 346 VAL A C   
2922 O O   . VAL A 346 ? 0.2468 0.2009 0.1828 0.0257  0.0351  0.0043  346 VAL A O   
2923 C CB  . VAL A 346 ? 0.2332 0.1907 0.1504 0.0416  0.0227  -0.0152 346 VAL A CB  
2924 C CG1 . VAL A 346 ? 0.2524 0.2038 0.1827 0.0348  0.0153  -0.0223 346 VAL A CG1 
2925 C CG2 . VAL A 346 ? 0.3179 0.2783 0.2184 0.0534  0.0195  -0.0219 346 VAL A CG2 
2926 N N   . VAL A 347 ? 0.1848 0.1291 0.1192 0.0258  0.0212  -0.0038 347 VAL A N   
2927 C CA  . VAL A 347 ? 0.1917 0.1316 0.1377 0.0176  0.0234  0.0009  347 VAL A CA  
2928 C C   . VAL A 347 ? 0.1710 0.1095 0.1288 0.0118  0.0180  -0.0058 347 VAL A C   
2929 O O   . VAL A 347 ? 0.1959 0.1320 0.1545 0.0123  0.0111  -0.0107 347 VAL A O   
2930 C CB  . VAL A 347 ? 0.2308 0.1651 0.1718 0.0195  0.0223  0.0055  347 VAL A CB  
2931 C CG1 . VAL A 347 ? 0.1981 0.1265 0.1502 0.0119  0.0248  0.0096  347 VAL A CG1 
2932 C CG2 . VAL A 347 ? 0.2535 0.1887 0.1797 0.0272  0.0280  0.0134  347 VAL A CG2 
2933 N N   . PHE A 348 ? 0.1536 0.0945 0.1214 0.0064  0.0214  -0.0053 348 PHE A N   
2934 C CA  . PHE A 348 ? 0.1502 0.0902 0.1281 0.0017  0.0175  -0.0098 348 PHE A CA  
2935 C C   . PHE A 348 ? 0.1592 0.0956 0.1446 -0.0039 0.0179  -0.0073 348 PHE A C   
2936 O O   . PHE A 348 ? 0.1931 0.1295 0.1823 -0.0073 0.0226  -0.0030 348 PHE A O   
2937 C CB  . PHE A 348 ? 0.1773 0.1231 0.1608 0.0007  0.0201  -0.0113 348 PHE A CB  
2938 C CG  . PHE A 348 ? 0.1662 0.1123 0.1460 0.0055  0.0165  -0.0171 348 PHE A CG  
2939 C CD1 . PHE A 348 ? 0.1825 0.1300 0.1515 0.0125  0.0166  -0.0189 348 PHE A CD1 
2940 C CD2 . PHE A 348 ? 0.1646 0.1088 0.1510 0.0038  0.0131  -0.0208 348 PHE A CD2 
2941 C CE1 . PHE A 348 ? 0.1703 0.1164 0.1359 0.0173  0.0127  -0.0256 348 PHE A CE1 
2942 C CE2 . PHE A 348 ? 0.1792 0.1211 0.1629 0.0082  0.0100  -0.0260 348 PHE A CE2 
2943 C CZ  . PHE A 348 ? 0.1916 0.1338 0.1653 0.0148  0.0093  -0.0293 348 PHE A CZ  
2944 N N   . VAL A 349 ? 0.1751 0.1084 0.1633 -0.0050 0.0129  -0.0102 349 VAL A N   
2945 C CA  . VAL A 349 ? 0.1566 0.0870 0.1511 -0.0089 0.0127  -0.0092 349 VAL A CA  
2946 C C   . VAL A 349 ? 0.1379 0.0706 0.1393 -0.0114 0.0108  -0.0125 349 VAL A C   
2947 O O   . VAL A 349 ? 0.1453 0.0780 0.1475 -0.0104 0.0074  -0.0152 349 VAL A O   
2948 C CB  . VAL A 349 ? 0.1354 0.0625 0.1272 -0.0066 0.0094  -0.0090 349 VAL A CB  
2949 C CG1 . VAL A 349 ? 0.2288 0.1532 0.2267 -0.0093 0.0093  -0.0087 349 VAL A CG1 
2950 C CG2 . VAL A 349 ? 0.1669 0.0914 0.1496 -0.0023 0.0113  -0.0047 349 VAL A CG2 
2951 N N   . VAL A 350 ? 0.1355 0.0705 0.1422 -0.0146 0.0130  -0.0123 350 VAL A N   
2952 C CA  . VAL A 350 ? 0.1688 0.1072 0.1798 -0.0153 0.0116  -0.0147 350 VAL A CA  
2953 C C   . VAL A 350 ? 0.1096 0.0485 0.1250 -0.0179 0.0116  -0.0153 350 VAL A C   
2954 O O   . VAL A 350 ? 0.1409 0.0802 0.1592 -0.0205 0.0134  -0.0150 350 VAL A O   
2955 C CB  . VAL A 350 ? 0.1413 0.0852 0.1533 -0.0142 0.0132  -0.0154 350 VAL A CB  
2956 C CG1 . VAL A 350 ? 0.1523 0.0984 0.1670 -0.0130 0.0112  -0.0171 350 VAL A CG1 
2957 C CG2 . VAL A 350 ? 0.1981 0.1416 0.2041 -0.0104 0.0137  -0.0155 350 VAL A CG2 
2958 N N   . LEU A 351 ? 0.1194 0.0584 0.1357 -0.0171 0.0097  -0.0162 351 LEU A N   
2959 C CA  . LEU A 351 ? 0.1705 0.1107 0.1889 -0.0180 0.0093  -0.0179 351 LEU A CA  
2960 C C   . LEU A 351 ? 0.1198 0.0622 0.1377 -0.0156 0.0084  -0.0175 351 LEU A C   
2961 O O   . LEU A 351 ? 0.1388 0.0803 0.1566 -0.0147 0.0082  -0.0158 351 LEU A O   
2962 C CB  . LEU A 351 ? 0.1580 0.0935 0.1756 -0.0185 0.0093  -0.0176 351 LEU A CB  
2963 C CG  . LEU A 351 ? 0.1689 0.1016 0.1842 -0.0163 0.0085  -0.0159 351 LEU A CG  
2964 C CD1 . LEU A 351 ? 0.1613 0.0914 0.1765 -0.0150 0.0082  -0.0172 351 LEU A CD1 
2965 C CD2 . LEU A 351 ? 0.1886 0.1171 0.2013 -0.0160 0.0092  -0.0139 351 LEU A CD2 
2966 N N   . ASP A 352 ? 0.1162 0.0614 0.1339 -0.0146 0.0079  -0.0193 352 ASP A N   
2967 C CA  . ASP A 352 ? 0.1289 0.0768 0.1449 -0.0115 0.0083  -0.0176 352 ASP A CA  
2968 C C   . ASP A 352 ? 0.1528 0.0982 0.1702 -0.0115 0.0093  -0.0150 352 ASP A C   
2969 O O   . ASP A 352 ? 0.1646 0.1071 0.1824 -0.0122 0.0090  -0.0160 352 ASP A O   
2970 C CB  . ASP A 352 ? 0.1119 0.0636 0.1253 -0.0090 0.0075  -0.0206 352 ASP A CB  
2971 C CG  . ASP A 352 ? 0.1677 0.1245 0.1813 -0.0087 0.0052  -0.0243 352 ASP A CG  
2972 O OD1 . ASP A 352 ? 0.1777 0.1362 0.1939 -0.0100 0.0051  -0.0236 352 ASP A OD1 
2973 O OD2 . ASP A 352 ? 0.1788 0.1391 0.1904 -0.0066 0.0032  -0.0288 352 ASP A OD2 
2974 N N   . GLY A 353 ? 0.1082 0.0545 0.1275 -0.0108 0.0105  -0.0115 353 GLY A N   
2975 C CA  . GLY A 353 ? 0.1038 0.0498 0.1276 -0.0118 0.0111  -0.0096 353 GLY A CA  
2976 C C   . GLY A 353 ? 0.1017 0.0525 0.1266 -0.0095 0.0136  -0.0075 353 GLY A C   
2977 O O   . GLY A 353 ? 0.1032 0.0560 0.1339 -0.0103 0.0142  -0.0061 353 GLY A O   
2978 N N   . GLU A 354 ? 0.1066 0.0609 0.1261 -0.0059 0.0150  -0.0078 354 GLU A N   
2979 C CA  . GLU A 354 ? 0.1084 0.0687 0.1275 -0.0022 0.0184  -0.0053 354 GLU A CA  
2980 C C   . GLU A 354 ? 0.1154 0.0775 0.1280 0.0020  0.0175  -0.0103 354 GLU A C   
2981 O O   . GLU A 354 ? 0.1407 0.1083 0.1517 0.0064  0.0205  -0.0090 354 GLU A O   
2982 C CB  . GLU A 354 ? 0.1128 0.0765 0.1305 0.0001  0.0220  0.0007  354 GLU A CB  
2983 C CG  . GLU A 354 ? 0.1176 0.0834 0.1255 0.0048  0.0210  -0.0010 354 GLU A CG  
2984 C CD  . GLU A 354 ? 0.1202 0.0818 0.1278 0.0026  0.0175  -0.0032 354 GLU A CD  
2985 O OE1 . GLU A 354 ? 0.1210 0.0824 0.1268 0.0046  0.0187  0.0011  354 GLU A OE1 
2986 O OE2 . GLU A 354 ? 0.1224 0.0809 0.1317 -0.0007 0.0142  -0.0084 354 GLU A OE2 
2987 N N   . ASN A 355 ? 0.1124 0.0698 0.1221 0.0008  0.0138  -0.0160 355 ASN A N   
2988 C CA  . ASN A 355 ? 0.1477 0.1056 0.1519 0.0046  0.0121  -0.0221 355 ASN A CA  
2989 C C   . ASN A 355 ? 0.1756 0.1276 0.1810 0.0045  0.0110  -0.0259 355 ASN A C   
2990 O O   . ASN A 355 ? 0.1720 0.1237 0.1730 0.0089  0.0101  -0.0311 355 ASN A O   
2991 C CB  . ASN A 355 ? 0.1553 0.1127 0.1574 0.0032  0.0086  -0.0266 355 ASN A CB  
2992 C CG  . ASN A 355 ? 0.1671 0.1313 0.1655 0.0063  0.0094  -0.0233 355 ASN A CG  
2993 O OD1 . ASN A 355 ? 0.1470 0.1162 0.1411 0.0112  0.0126  -0.0194 355 ASN A OD1 
2994 N ND2 . ASN A 355 ? 0.1635 0.1282 0.1634 0.0040  0.0072  -0.0241 355 ASN A ND2 
2995 N N   . CYS A 356 ? 0.1440 0.0910 0.1542 0.0010  0.0108  -0.0237 356 CYS A N   
2996 C CA  . CYS A 356 ? 0.1303 0.0701 0.1406 0.0019  0.0097  -0.0266 356 CYS A CA  
2997 C C   . CYS A 356 ? 0.1407 0.0843 0.1525 0.0065  0.0116  -0.0247 356 CYS A C   
2998 O O   . CYS A 356 ? 0.1303 0.0690 0.1403 0.0103  0.0109  -0.0280 356 CYS A O   
2999 C CB  . CYS A 356 ? 0.1374 0.0698 0.1503 -0.0029 0.0085  -0.0250 356 CYS A CB  
3000 S SG  . CYS A 356 ? 0.1699 0.1063 0.1867 -0.0050 0.0091  -0.0192 356 CYS A SG  
3001 N N   . TRP A 357 ? 0.1272 0.0795 0.1432 0.0067  0.0140  -0.0198 357 TRP A N   
3002 C CA  . TRP A 357 ? 0.1229 0.0810 0.1442 0.0097  0.0156  -0.0175 357 TRP A CA  
3003 C C   . TRP A 357 ? 0.1320 0.0955 0.1501 0.0169  0.0181  -0.0195 357 TRP A C   
3004 O O   . TRP A 357 ? 0.1307 0.0968 0.1517 0.0211  0.0186  -0.0198 357 TRP A O   
3005 C CB  . TRP A 357 ? 0.1197 0.0863 0.1496 0.0062  0.0175  -0.0120 357 TRP A CB  
3006 C CG  . TRP A 357 ? 0.1070 0.0680 0.1382 0.0004  0.0148  -0.0113 357 TRP A CG  
3007 C CD1 . TRP A 357 ? 0.1236 0.0847 0.1558 -0.0031 0.0156  -0.0088 357 TRP A CD1 
3008 C CD2 . TRP A 357 ? 0.1064 0.0606 0.1370 -0.0015 0.0111  -0.0129 357 TRP A CD2 
3009 N NE1 . TRP A 357 ? 0.1467 0.1018 0.1789 -0.0069 0.0125  -0.0099 357 TRP A NE1 
3010 C CE2 . TRP A 357 ? 0.1356 0.0870 0.1664 -0.0059 0.0099  -0.0121 357 TRP A CE2 
3011 C CE3 . TRP A 357 ? 0.1410 0.0907 0.1695 0.0013  0.0091  -0.0145 357 TRP A CE3 
3012 C CZ2 . TRP A 357 ? 0.1674 0.1133 0.1961 -0.0075 0.0070  -0.0131 357 TRP A CZ2 
3013 C CZ3 . TRP A 357 ? 0.1198 0.0634 0.1460 -0.0005 0.0064  -0.0143 357 TRP A CZ3 
3014 C CH2 . TRP A 357 ? 0.1310 0.0734 0.1570 -0.0048 0.0055  -0.0138 357 TRP A CH2 
3015 N N   . GLU A 358 ? 0.1293 0.0954 0.1408 0.0197  0.0196  -0.0213 358 GLU A N   
3016 C CA  . GLU A 358 ? 0.1381 0.1101 0.1445 0.0281  0.0222  -0.0238 358 GLU A CA  
3017 C C   . GLU A 358 ? 0.1467 0.1093 0.1490 0.0324  0.0190  -0.0312 358 GLU A C   
3018 O O   . GLU A 358 ? 0.1548 0.1218 0.1540 0.0404  0.0210  -0.0337 358 GLU A O   
3019 C CB  . GLU A 358 ? 0.1432 0.1198 0.1409 0.0313  0.0235  -0.0248 358 GLU A CB  
3020 C CG  . GLU A 358 ? 0.1658 0.1332 0.1577 0.0289  0.0180  -0.0318 358 GLU A CG  
3021 C CD  . GLU A 358 ? 0.2576 0.2310 0.2432 0.0302  0.0184  -0.0306 358 GLU A CD  
3022 O OE1 . GLU A 358 ? 0.2850 0.2594 0.2617 0.0356  0.0158  -0.0376 358 GLU A OE1 
3023 O OE2 . GLU A 358 ? 0.2383 0.2149 0.2277 0.0263  0.0207  -0.0233 358 GLU A OE2 
3024 N N   . TYR A 359 ? 0.1465 0.0962 0.1492 0.0275  0.0148  -0.0340 359 TYR A N   
3025 C CA  . TYR A 359 ? 0.1569 0.0941 0.1569 0.0306  0.0121  -0.0399 359 TYR A CA  
3026 C C   . TYR A 359 ? 0.1693 0.1035 0.1742 0.0318  0.0121  -0.0363 359 TYR A C   
3027 O O   . TYR A 359 ? 0.1806 0.1038 0.1834 0.0356  0.0105  -0.0398 359 TYR A O   
3028 C CB  . TYR A 359 ? 0.1631 0.0878 0.1622 0.0242  0.0083  -0.0440 359 TYR A CB  
3029 C CG  . TYR A 359 ? 0.1701 0.0985 0.1643 0.0245  0.0067  -0.0495 359 TYR A CG  
3030 C CD1 . TYR A 359 ? 0.2433 0.1690 0.2315 0.0307  0.0046  -0.0584 359 TYR A CD1 
3031 C CD2 . TYR A 359 ? 0.2000 0.1352 0.1952 0.0197  0.0068  -0.0464 359 TYR A CD2 
3032 C CE1 . TYR A 359 ? 0.2486 0.1794 0.2314 0.0321  0.0020  -0.0645 359 TYR A CE1 
3033 C CE2 . TYR A 359 ? 0.2638 0.2041 0.2538 0.0214  0.0047  -0.0515 359 TYR A CE2 
3034 C CZ  . TYR A 359 ? 0.3359 0.2745 0.3196 0.0276  0.0021  -0.0606 359 TYR A CZ  
3035 O OH  . TYR A 359 ? 0.3785 0.3233 0.3561 0.0304  -0.0012 -0.0668 359 TYR A OH  
3036 N N   . TYR A 360 ? 0.1466 0.0893 0.1580 0.0288  0.0133  -0.0298 360 TYR A N   
3037 C CA  . TYR A 360 ? 0.1460 0.0894 0.1622 0.0312  0.0126  -0.0268 360 TYR A CA  
3038 C C   . TYR A 360 ? 0.1713 0.1285 0.1920 0.0385  0.0154  -0.0260 360 TYR A C   
3039 O O   . TYR A 360 ? 0.1603 0.1301 0.1834 0.0391  0.0191  -0.0245 360 TYR A O   
3040 C CB  . TYR A 360 ? 0.1356 0.0837 0.1580 0.0248  0.0114  -0.0217 360 TYR A CB  
3041 C CG  . TYR A 360 ? 0.1537 0.0907 0.1730 0.0187  0.0091  -0.0209 360 TYR A CG  
3042 C CD1 . TYR A 360 ? 0.1325 0.0647 0.1485 0.0135  0.0093  -0.0226 360 TYR A CD1 
3043 C CD2 . TYR A 360 ? 0.1364 0.0697 0.1561 0.0188  0.0067  -0.0182 360 TYR A CD2 
3044 C CE1 . TYR A 360 ? 0.1313 0.0559 0.1459 0.0082  0.0080  -0.0213 360 TYR A CE1 
3045 C CE2 . TYR A 360 ? 0.1353 0.0603 0.1516 0.0140  0.0056  -0.0166 360 TYR A CE2 
3046 C CZ  . TYR A 360 ? 0.1366 0.0573 0.1509 0.0086  0.0067  -0.0180 360 TYR A CZ  
3047 O OH  . TYR A 360 ? 0.1660 0.0806 0.1780 0.0043  0.0064  -0.0160 360 TYR A OH  
3048 N N   . GLU A 361 ? 0.2286 0.0910 0.2244 -0.0015 0.0657  -0.0432 361 GLU A N   
3049 C CA  . GLU A 361 ? 0.2485 0.1158 0.2556 0.0135  0.0698  -0.0405 361 GLU A CA  
3050 C C   . GLU A 361 ? 0.2181 0.1150 0.2406 0.0156  0.0596  -0.0298 361 GLU A C   
3051 O O   . GLU A 361 ? 0.1887 0.0884 0.2151 0.0140  0.0496  -0.0211 361 GLU A O   
3052 C CB  . GLU A 361 ? 0.2790 0.1331 0.2877 0.0276  0.0683  -0.0318 361 GLU A CB  
3053 C CG  . GLU A 361 ? 0.5064 0.3376 0.5027 0.0265  0.0760  -0.0378 361 GLU A CG  
3054 C CD  . GLU A 361 ? 0.7300 0.5598 0.7205 0.0209  0.0866  -0.0530 361 GLU A CD  
3055 O OE1 . GLU A 361 ? 0.7975 0.6214 0.7775 0.0059  0.0894  -0.0630 361 GLU A OE1 
3056 O OE2 . GLU A 361 ? 0.8107 0.6490 0.8078 0.0316  0.0921  -0.0556 361 GLU A OE2 
3057 N N   . GLU A 362 ? 0.1903 0.1107 0.2212 0.0183  0.0625  -0.0302 362 GLU A N   
3058 C CA  . GLU A 362 ? 0.2213 0.1703 0.2684 0.0181  0.0545  -0.0196 362 GLU A CA  
3059 C C   . GLU A 362 ? 0.2193 0.1747 0.2632 0.0067  0.0449  -0.0146 362 GLU A C   
3060 O O   . GLU A 362 ? 0.1327 0.0970 0.1885 0.0069  0.0363  -0.0057 362 GLU A O   
3061 C CB  . GLU A 362 ? 0.2228 0.1764 0.2877 0.0305  0.0496  -0.0113 362 GLU A CB  
3062 C CG  . GLU A 362 ? 0.4207 0.3786 0.4945 0.0445  0.0590  -0.0139 362 GLU A CG  
3063 C CD  . GLU A 362 ? 0.6169 0.5793 0.7062 0.0593  0.0532  -0.0063 362 GLU A CD  
3064 O OE1 . GLU A 362 ? 0.7182 0.6601 0.8021 0.0732  0.0585  -0.0072 362 GLU A OE1 
3065 O OE2 . GLU A 362 ? 0.6383 0.6247 0.7447 0.0573  0.0434  0.0004  362 GLU A OE2 
3066 N N   . ASN A 363 ? 0.1532 0.1062 0.1816 -0.0032 0.0466  -0.0215 363 ASN A N   
3067 C CA  . ASN A 363 ? 0.1393 0.1024 0.1645 -0.0120 0.0387  -0.0169 363 ASN A CA  
3068 C C   . ASN A 363 ? 0.1586 0.1096 0.1872 -0.0116 0.0303  -0.0112 363 ASN A C   
3069 O O   . ASN A 363 ? 0.1494 0.1097 0.1836 -0.0136 0.0231  -0.0036 363 ASN A O   
3070 C CB  . ASN A 363 ? 0.1790 0.1658 0.2125 -0.0122 0.0371  -0.0074 363 ASN A CB  
3071 C CG  . ASN A 363 ? 0.1925 0.1903 0.2191 -0.0186 0.0317  -0.0029 363 ASN A CG  
3072 O OD1 . ASN A 363 ? 0.1570 0.1574 0.1703 -0.0242 0.0319  -0.0105 363 ASN A OD1 
3073 N ND2 . ASN A 363 ? 0.2366 0.2417 0.2733 -0.0176 0.0275  0.0091  363 ASN A ND2 
3074 N N   . GLY A 364 ? 0.1650 0.0941 0.1900 -0.0077 0.0322  -0.0141 364 GLY A N   
3075 C CA  . GLY A 364 ? 0.1712 0.0898 0.1958 -0.0069 0.0253  -0.0088 364 GLY A CA  
3076 C C   . GLY A 364 ? 0.1788 0.1043 0.2166 0.0012  0.0175  -0.0004 364 GLY A C   
3077 O O   . GLY A 364 ? 0.1726 0.0926 0.2086 0.0020  0.0111  0.0032  364 GLY A O   
3078 N N   . ILE A 365 ? 0.1295 0.0693 0.1807 0.0065  0.0182  0.0017  365 ILE A N   
3079 C CA  . ILE A 365 ? 0.1119 0.0646 0.1789 0.0105  0.0100  0.0074  365 ILE A CA  
3080 C C   . ILE A 365 ? 0.1739 0.1177 0.2401 0.0216  0.0063  0.0093  365 ILE A C   
3081 O O   . ILE A 365 ? 0.1736 0.1189 0.2406 0.0222  -0.0027 0.0119  365 ILE A O   
3082 C CB  . ILE A 365 ? 0.1447 0.1190 0.2288 0.0107  0.0130  0.0090  365 ILE A CB  
3083 C CG1 . ILE A 365 ? 0.1449 0.1273 0.2274 0.0005  0.0151  0.0112  365 ILE A CG1 
3084 C CG2 . ILE A 365 ? 0.1468 0.1370 0.2507 0.0142  0.0054  0.0120  365 ILE A CG2 
3085 C CD1 . ILE A 365 ? 0.1318 0.1324 0.2244 -0.0004 0.0229  0.0134  365 ILE A CD1 
3086 N N   . PRO A 366 ? 0.1464 0.0789 0.2084 0.0316  0.0134  0.0083  366 PRO A N   
3087 C CA  . PRO A 366 ? 0.1943 0.1156 0.2514 0.0445  0.0103  0.0132  366 PRO A CA  
3088 C C   . PRO A 366 ? 0.2332 0.1401 0.2695 0.0385  0.0059  0.0143  366 PRO A C   
3089 O O   . PRO A 366 ? 0.2122 0.1229 0.2465 0.0443  -0.0022 0.0189  366 PRO A O   
3090 C CB  . PRO A 366 ? 0.2030 0.1101 0.2511 0.0524  0.0206  0.0106  366 PRO A CB  
3091 C CG  . PRO A 366 ? 0.2271 0.1479 0.2905 0.0516  0.0282  0.0060  366 PRO A CG  
3092 C CD  . PRO A 366 ? 0.1952 0.1266 0.2578 0.0345  0.0247  0.0034  366 PRO A CD  
3093 N N   . PHE A 367 ? 0.1682 0.0623 0.1909 0.0273  0.0111  0.0096  367 PHE A N   
3094 C CA  . PHE A 367 ? 0.1631 0.0492 0.1719 0.0210  0.0077  0.0104  367 PHE A CA  
3095 C C   . PHE A 367 ? 0.1481 0.0444 0.1579 0.0185  0.0001  0.0125  367 PHE A C   
3096 O O   . PHE A 367 ? 0.1718 0.0640 0.1730 0.0229  -0.0034 0.0162  367 PHE A O   
3097 C CB  . PHE A 367 ? 0.1641 0.0458 0.1665 0.0087  0.0142  0.0043  367 PHE A CB  
3098 C CG  . PHE A 367 ? 0.1627 0.0435 0.1584 0.0022  0.0121  0.0054  367 PHE A CG  
3099 C CD1 . PHE A 367 ? 0.1807 0.0488 0.1687 0.0054  0.0153  0.0093  367 PHE A CD1 
3100 C CD2 . PHE A 367 ? 0.1841 0.0768 0.1818 -0.0058 0.0085  0.0036  367 PHE A CD2 
3101 C CE1 . PHE A 367 ? 0.2185 0.0857 0.2007 -0.0002 0.0163  0.0108  367 PHE A CE1 
3102 C CE2 . PHE A 367 ? 0.2026 0.0962 0.1966 -0.0102 0.0086  0.0046  367 PHE A CE2 
3103 C CZ  . PHE A 367 ? 0.2295 0.1103 0.2153 -0.0078 0.0128  0.0079  367 PHE A CZ  
3104 N N   . LEU A 368 ? 0.1395 0.0505 0.1617 0.0112  -0.0013 0.0102  368 LEU A N   
3105 C CA  . LEU A 368 ? 0.1243 0.0459 0.1505 0.0074  -0.0083 0.0107  368 LEU A CA  
3106 C C   . LEU A 368 ? 0.1391 0.0691 0.1783 0.0144  -0.0182 0.0128  368 LEU A C   
3107 O O   . LEU A 368 ? 0.1372 0.0678 0.1730 0.0148  -0.0252 0.0125  368 LEU A O   
3108 C CB  . LEU A 368 ? 0.1029 0.0359 0.1376 -0.0006 -0.0082 0.0092  368 LEU A CB  
3109 C CG  . LEU A 368 ? 0.1199 0.0498 0.1434 -0.0075 -0.0031 0.0068  368 LEU A CG  
3110 C CD1 . LEU A 368 ? 0.1293 0.0713 0.1626 -0.0121 -0.0035 0.0084  368 LEU A CD1 
3111 C CD2 . LEU A 368 ? 0.1466 0.0720 0.1586 -0.0088 -0.0032 0.0063  368 LEU A CD2 
3112 N N   . GLU A 369 ? 0.1172 0.0572 0.1722 0.0200  -0.0195 0.0138  369 GLU A N   
3113 C CA  . GLU A 369 ? 0.1393 0.0968 0.2056 0.0257  -0.0293 0.0137  369 GLU A CA  
3114 C C   . GLU A 369 ? 0.1661 0.1169 0.2176 0.0371  -0.0337 0.0175  369 GLU A C   
3115 O O   . GLU A 369 ? 0.1684 0.1304 0.2192 0.0390  -0.0437 0.0158  369 GLU A O   
3116 C CB  . GLU A 369 ? 0.1126 0.0893 0.1988 0.0297  -0.0280 0.0138  369 GLU A CB  
3117 C CG  . GLU A 369 ? 0.0990 0.0873 0.2015 0.0175  -0.0252 0.0114  369 GLU A CG  
3118 C CD  . GLU A 369 ? 0.1651 0.1760 0.2891 0.0200  -0.0224 0.0116  369 GLU A CD  
3119 O OE1 . GLU A 369 ? 0.2259 0.2442 0.3532 0.0328  -0.0218 0.0131  369 GLU A OE1 
3120 O OE2 . GLU A 369 ? 0.1687 0.1905 0.3073 0.0097  -0.0198 0.0110  369 GLU A OE2 
3121 N N   . LYS A 370 ? 0.1466 0.0787 0.1845 0.0446  -0.0252 0.0224  370 LYS A N   
3122 C CA  . LYS A 370 ? 0.1663 0.0913 0.1874 0.0555  -0.0257 0.0290  370 LYS A CA  
3123 C C   . LYS A 370 ? 0.1680 0.0829 0.1730 0.0484  -0.0265 0.0286  370 LYS A C   
3124 O O   . LYS A 370 ? 0.2298 0.1494 0.2249 0.0555  -0.0341 0.0316  370 LYS A O   
3125 C CB  . LYS A 370 ? 0.1832 0.0916 0.2010 0.0596  -0.0159 0.0330  370 LYS A CB  
3126 C CG  . LYS A 370 ? 0.2220 0.1407 0.2517 0.0716  -0.0169 0.0331  370 LYS A CG  
3127 C CD  . LYS A 370 ? 0.2909 0.1898 0.3102 0.0769  -0.0069 0.0355  370 LYS A CD  
3128 C CE  . LYS A 370 ? 0.3911 0.2992 0.4233 0.0877  -0.0039 0.0344  370 LYS A CE  
3129 N NZ  . LYS A 370 ? 0.4426 0.3812 0.4909 0.1006  -0.0146 0.0387  370 LYS A NZ  
3130 N N   . LEU A 371 ? 0.1595 0.0642 0.1607 0.0358  -0.0183 0.0248  371 LEU A N   
3131 C CA  . LEU A 371 ? 0.1606 0.0592 0.1496 0.0297  -0.0179 0.0241  371 LEU A CA  
3132 C C   . LEU A 371 ? 0.1833 0.0916 0.1742 0.0298  -0.0318 0.0199  371 LEU A C   
3133 O O   . LEU A 371 ? 0.2004 0.1082 0.1771 0.0338  -0.0356 0.0210  371 LEU A O   
3134 C CB  . LEU A 371 ? 0.1711 0.0674 0.1626 0.0171  -0.0084 0.0196  371 LEU A CB  
3135 C CG  . LEU A 371 ? 0.1998 0.0947 0.1831 0.0107  -0.0083 0.0179  371 LEU A CG  
3136 C CD1 . LEU A 371 ? 0.2149 0.0967 0.1831 0.0135  -0.0039 0.0235  371 LEU A CD1 
3137 C CD2 . LEU A 371 ? 0.1670 0.0683 0.1576 0.0002  -0.0026 0.0131  371 LEU A CD2 
3138 N N   . TYR A 372 ? 0.1644 0.0864 0.1738 0.0235  -0.0361 0.0139  372 TYR A N   
3139 C CA  . TYR A 372 ? 0.1543 0.0883 0.1695 0.0197  -0.0449 0.0070  372 TYR A CA  
3140 C C   . TYR A 372 ? 0.1767 0.1270 0.1927 0.0274  -0.0558 0.0049  372 TYR A C   
3141 O O   . TYR A 372 ? 0.2086 0.1642 0.2170 0.0271  -0.0626 -0.0010 372 TYR A O   
3142 C CB  . TYR A 372 ? 0.1329 0.0736 0.1681 0.0107  -0.0440 0.0031  372 TYR A CB  
3143 C CG  . TYR A 372 ? 0.1279 0.0607 0.1605 0.0040  -0.0349 0.0046  372 TYR A CG  
3144 C CD1 . TYR A 372 ? 0.1405 0.0667 0.1569 0.0034  -0.0288 0.0055  372 TYR A CD1 
3145 C CD2 . TYR A 372 ? 0.1160 0.0576 0.1604 -0.0015 -0.0303 0.0049  372 TYR A CD2 
3146 C CE1 . TYR A 372 ? 0.1427 0.0727 0.1579 -0.0017 -0.0208 0.0057  372 TYR A CE1 
3147 C CE2 . TYR A 372 ? 0.0935 0.0372 0.1314 -0.0047 -0.0222 0.0064  372 TYR A CE2 
3148 C CZ  . TYR A 372 ? 0.0982 0.0369 0.1233 -0.0048 -0.0188 0.0061  372 TYR A CZ  
3149 O OH  . TYR A 372 ? 0.1466 0.0884 0.1704 -0.0077 -0.0144 0.0072  372 TYR A OH  
3150 N N   . SER A 373 ? 0.1691 0.1310 0.1953 0.0347  -0.0580 0.0085  373 SER A N   
3151 C CA  . SER A 373 ? 0.1748 0.1586 0.2021 0.0441  -0.0695 0.0074  373 SER A CA  
3152 C C   . SER A 373 ? 0.2005 0.1766 0.2004 0.0554  -0.0711 0.0138  373 SER A C   
3153 O O   . SER A 373 ? 0.2195 0.2141 0.2129 0.0602  -0.0822 0.0097  373 SER A O   
3154 C CB  . SER A 373 ? 0.1837 0.1825 0.2272 0.0530  -0.0697 0.0121  373 SER A CB  
3155 O OG  . SER A 373 ? 0.3569 0.3840 0.4037 0.0630  -0.0823 0.0109  373 SER A OG  
3156 N N   . THR A 374 ? 0.2276 0.1778 0.2108 0.0592  -0.0596 0.0236  374 THR A N   
3157 C CA  . THR A 374 ? 0.2324 0.1719 0.1883 0.0693  -0.0580 0.0323  374 THR A CA  
3158 C C   . THR A 374 ? 0.2302 0.1683 0.1730 0.0613  -0.0595 0.0254  374 THR A C   
3159 O O   . THR A 374 ? 0.2697 0.2177 0.1952 0.0687  -0.0662 0.0257  374 THR A O   
3160 C CB  . THR A 374 ? 0.2508 0.1652 0.1994 0.0686  -0.0405 0.0422  374 THR A CB  
3161 O OG1 . THR A 374 ? 0.2500 0.1691 0.2124 0.0751  -0.0376 0.0466  374 THR A OG1 
3162 C CG2 . THR A 374 ? 0.3058 0.2104 0.2305 0.0743  -0.0353 0.0512  374 THR A CG2 
3163 N N   . LEU A 375 ? 0.2367 0.1651 0.1870 0.0477  -0.0532 0.0189  375 LEU A N   
3164 C CA  . LEU A 375 ? 0.2512 0.1789 0.1913 0.0419  -0.0534 0.0119  375 LEU A CA  
3165 C C   . LEU A 375 ? 0.2802 0.2284 0.2242 0.0416  -0.0665 -0.0004 375 LEU A C   
3166 O O   . LEU A 375 ? 0.3563 0.3072 0.2837 0.0430  -0.0688 -0.0056 375 LEU A O   
3167 C CB  . LEU A 375 ? 0.2008 0.1192 0.1524 0.0298  -0.0455 0.0076  375 LEU A CB  
3168 C CG  . LEU A 375 ? 0.2470 0.1484 0.1923 0.0266  -0.0324 0.0156  375 LEU A CG  
3169 C CD1 . LEU A 375 ? 0.2062 0.1071 0.1655 0.0158  -0.0272 0.0110  375 LEU A CD1 
3170 C CD2 . LEU A 375 ? 0.3361 0.2283 0.2578 0.0297  -0.0256 0.0214  375 LEU A CD2 
3171 N N   . GLU A 376 ? 0.2642 0.2273 0.2310 0.0381  -0.0741 -0.0067 376 GLU A N   
3172 C CA  . GLU A 376 ? 0.2941 0.2784 0.2684 0.0350  -0.0866 -0.0206 376 GLU A CA  
3173 C C   . GLU A 376 ? 0.3175 0.3184 0.2705 0.0465  -0.0961 -0.0205 376 GLU A C   
3174 O O   . GLU A 376 ? 0.3602 0.3757 0.3093 0.0432  -0.1052 -0.0347 376 GLU A O   
3175 C CB  . GLU A 376 ? 0.3631 0.3650 0.3656 0.0310  -0.0922 -0.0237 376 GLU A CB  
3176 C CG  . GLU A 376 ? 0.3901 0.3844 0.4154 0.0169  -0.0870 -0.0297 376 GLU A CG  
3177 C CD  . GLU A 376 ? 0.3696 0.3867 0.4222 0.0120  -0.0930 -0.0343 376 GLU A CD  
3178 O OE1 . GLU A 376 ? 0.3305 0.3649 0.3877 0.0218  -0.0966 -0.0274 376 GLU A OE1 
3179 O OE2 . GLU A 376 ? 0.3850 0.4033 0.4552 -0.0012 -0.0934 -0.0448 376 GLU A OE2 
3180 N N   . LYS A 377 ? 0.2830 0.2817 0.2213 0.0605  -0.0937 -0.0048 377 LYS A N   
3181 C CA  . LYS A 377 ? 0.2915 0.3096 0.2103 0.0741  -0.1022 -0.0008 377 LYS A CA  
3182 C C   . LYS A 377 ? 0.3502 0.3542 0.2362 0.0799  -0.0949 0.0064  377 LYS A C   
3183 O O   . LYS A 377 ? 0.3761 0.3976 0.2478 0.0864  -0.0989 0.0073  377 LYS A O   
3184 C CB  . LYS A 377 ? 0.3424 0.3674 0.2685 0.0853  -0.0993 0.0141  377 LYS A CB  
3185 C CG  . LYS A 377 ? 0.4505 0.4983 0.4084 0.0816  -0.1062 0.0078  377 LYS A CG  
3186 C CD  . LYS A 377 ? 0.5807 0.6638 0.5469 0.0766  -0.1194 -0.0062 377 LYS A CD  
3187 C CE  . LYS A 377 ? 0.6481 0.7585 0.6432 0.0760  -0.1244 -0.0075 377 LYS A CE  
3188 N NZ  . LYS A 377 ? 0.6495 0.7459 0.6651 0.0727  -0.1166 -0.0039 377 LYS A NZ  
3189 N N   . GLU A 378 ? 0.3485 0.3240 0.2257 0.0753  -0.0819 0.0117  378 GLU A N   
3190 C CA  . GLU A 378 ? 0.4145 0.3768 0.2606 0.0811  -0.0729 0.0211  378 GLU A CA  
3191 C C   . GLU A 378 ? 0.4616 0.4344 0.2950 0.0766  -0.0769 0.0060  378 GLU A C   
3192 O O   . GLU A 378 ? 0.4606 0.4281 0.3082 0.0643  -0.0743 -0.0073 378 GLU A O   
3193 C CB  . GLU A 378 ? 0.4387 0.3713 0.2861 0.0737  -0.0550 0.0303  378 GLU A CB  
3194 C CG  . GLU A 378 ? 0.4716 0.3895 0.3323 0.0756  -0.0489 0.0414  378 GLU A CG  
3195 C CD  . GLU A 378 ? 0.5411 0.4555 0.3925 0.0857  -0.0419 0.0564  378 GLU A CD  
3196 O OE1 . GLU A 378 ? 0.5613 0.4796 0.3916 0.0918  -0.0404 0.0619  378 GLU A OE1 
3197 O OE2 . GLU A 378 ? 0.5599 0.4676 0.4261 0.0871  -0.0374 0.0619  378 GLU A OE2 
3198 N N   . GLU A 379 ? 0.3499 0.3364 0.1621 0.0844  -0.0783 0.0087  379 GLU A N   
3199 C CA  . GLU A 379 ? 0.4418 0.4391 0.2408 0.0808  -0.0808 -0.0066 379 GLU A CA  
3200 C C   . GLU A 379 ? 0.5036 0.4806 0.2849 0.0785  -0.0663 -0.0036 379 GLU A C   
3201 O O   . GLU A 379 ? 0.4786 0.4580 0.2564 0.0731  -0.0657 -0.0195 379 GLU A O   
3202 C CB  . GLU A 379 ? 0.4815 0.5021 0.2650 0.0889  -0.0866 -0.0045 379 GLU A CB  
3203 C CG  . GLU A 379 ? 0.6512 0.6958 0.4514 0.0925  -0.0999 -0.0051 379 GLU A CG  
3204 C CD  . GLU A 379 ? 0.7392 0.8141 0.5312 0.0937  -0.1114 -0.0165 379 GLU A CD  
3205 O OE1 . GLU A 379 ? 0.6923 0.7843 0.5019 0.0836  -0.1219 -0.0360 379 GLU A OE1 
3206 O OE2 . GLU A 379 ? 0.7032 0.7839 0.4713 0.1041  -0.1093 -0.0059 379 GLU A OE2 
3207 N N   . TRP A 380 ? 0.3479 0.3050 0.1211 0.0812  -0.0526 0.0157  380 TRP A N   
3208 C CA  . TRP A 380 ? 0.3832 0.3262 0.1410 0.0777  -0.0366 0.0200  380 TRP A CA  
3209 C C   . TRP A 380 ? 0.3620 0.2911 0.1458 0.0643  -0.0277 0.0156  380 TRP A C   
3210 O O   . TRP A 380 ? 0.3633 0.2863 0.1430 0.0592  -0.0143 0.0168  380 TRP A O   
3211 C CB  . TRP A 380 ? 0.3795 0.3119 0.1240 0.0823  -0.0231 0.0417  380 TRP A CB  
3212 C CG  . TRP A 380 ? 0.3909 0.3076 0.1504 0.0829  -0.0204 0.0546  380 TRP A CG  
3213 C CD1 . TRP A 380 ? 0.4336 0.3587 0.2020 0.0909  -0.0302 0.0588  380 TRP A CD1 
3214 C CD2 . TRP A 380 ? 0.4054 0.2976 0.1765 0.0736  -0.0068 0.0617  380 TRP A CD2 
3215 N NE1 . TRP A 380 ? 0.4377 0.3434 0.2217 0.0884  -0.0227 0.0680  380 TRP A NE1 
3216 C CE2 . TRP A 380 ? 0.4189 0.3040 0.2052 0.0768  -0.0086 0.0691  380 TRP A CE2 
3217 C CE3 . TRP A 380 ? 0.3938 0.2728 0.1661 0.0618  0.0075  0.0613  380 TRP A CE3 
3218 C CZ2 . TRP A 380 ? 0.4417 0.3057 0.2439 0.0679  0.0029  0.0737  380 TRP A CZ2 
3219 C CZ3 . TRP A 380 ? 0.4071 0.2672 0.1966 0.0518  0.0181  0.0666  380 TRP A CZ3 
3220 C CH2 . TRP A 380 ? 0.4488 0.3011 0.2527 0.0547  0.0155  0.0715  380 TRP A CH2 
3221 N N   . ILE A 381 ? 0.2998 0.2276 0.1116 0.0586  -0.0345 0.0106  381 ILE A N   
3222 C CA  . ILE A 381 ? 0.2954 0.2153 0.1329 0.0469  -0.0283 0.0054  381 ILE A CA  
3223 C C   . ILE A 381 ? 0.3374 0.2665 0.1916 0.0429  -0.0381 -0.0127 381 ILE A C   
3224 O O   . ILE A 381 ? 0.3501 0.2884 0.2115 0.0444  -0.0508 -0.0191 381 ILE A O   
3225 C CB  . ILE A 381 ? 0.2819 0.1908 0.1374 0.0430  -0.0259 0.0146  381 ILE A CB  
3226 C CG1 . ILE A 381 ? 0.3982 0.2910 0.2385 0.0454  -0.0138 0.0315  381 ILE A CG1 
3227 C CG2 . ILE A 381 ? 0.2906 0.1972 0.1718 0.0316  -0.0220 0.0078  381 ILE A CG2 
3228 C CD1 . ILE A 381 ? 0.3687 0.2494 0.2233 0.0441  -0.0123 0.0385  381 ILE A CD1 
3229 N N   . GLU A 382 ? 0.3069 0.2336 0.1688 0.0379  -0.0316 -0.0206 382 GLU A N   
3230 C CA  . GLU A 382 ? 0.2516 0.1792 0.1312 0.0339  -0.0372 -0.0357 382 GLU A CA  
3231 C C   . GLU A 382 ? 0.2284 0.1491 0.1304 0.0278  -0.0300 -0.0316 382 GLU A C   
3232 O O   . GLU A 382 ? 0.2607 0.1814 0.1613 0.0274  -0.0196 -0.0282 382 GLU A O   
3233 C CB  . GLU A 382 ? 0.3001 0.2306 0.1663 0.0373  -0.0356 -0.0497 382 GLU A CB  
3234 C CG  . GLU A 382 ? 0.4397 0.3654 0.3219 0.0337  -0.0403 -0.0666 382 GLU A CG  
3235 C CD  . GLU A 382 ? 0.6916 0.6179 0.5574 0.0380  -0.0382 -0.0831 382 GLU A CD  
3236 O OE1 . GLU A 382 ? 0.7330 0.6695 0.5724 0.0436  -0.0391 -0.0841 382 GLU A OE1 
3237 O OE2 . GLU A 382 ? 0.7520 0.6674 0.6301 0.0369  -0.0348 -0.0946 382 GLU A OE2 
3238 N N   . THR A 383 ? 0.2325 0.1508 0.1551 0.0233  -0.0355 -0.0318 383 THR A N   
3239 C CA  . THR A 383 ? 0.2057 0.1202 0.1475 0.0188  -0.0297 -0.0286 383 THR A CA  
3240 C C   . THR A 383 ? 0.2369 0.1475 0.1855 0.0204  -0.0279 -0.0389 383 THR A C   
3241 O O   . THR A 383 ? 0.2384 0.1452 0.1853 0.0209  -0.0335 -0.0511 383 THR A O   
3242 C CB  . THR A 383 ? 0.1884 0.1019 0.1481 0.0142  -0.0343 -0.0243 383 THR A CB  
3243 O OG1 . THR A 383 ? 0.2232 0.1375 0.1907 0.0126  -0.0434 -0.0335 383 THR A OG1 
3244 C CG2 . THR A 383 ? 0.2661 0.1801 0.2196 0.0145  -0.0332 -0.0137 383 THR A CG2 
3245 N N   . LEU A 384 ? 0.1964 0.1085 0.1527 0.0216  -0.0196 -0.0348 384 LEU A N   
3246 C CA  . LEU A 384 ? 0.1899 0.0968 0.1515 0.0269  -0.0157 -0.0424 384 LEU A CA  
3247 C C   . LEU A 384 ? 0.1778 0.0819 0.1595 0.0270  -0.0134 -0.0362 384 LEU A C   
3248 O O   . LEU A 384 ? 0.1950 0.1078 0.1839 0.0236  -0.0124 -0.0260 384 LEU A O   
3249 C CB  . LEU A 384 ? 0.2192 0.1355 0.1708 0.0330  -0.0066 -0.0429 384 LEU A CB  
3250 C CG  . LEU A 384 ? 0.2348 0.1555 0.1630 0.0344  -0.0058 -0.0466 384 LEU A CG  
3251 C CD1 . LEU A 384 ? 0.2233 0.1552 0.1458 0.0400  0.0056  -0.0467 384 LEU A CD1 
3252 C CD2 . LEU A 384 ? 0.2978 0.2097 0.2159 0.0363  -0.0133 -0.0612 384 LEU A CD2 
3253 N N   . THR A 385 ? 0.1908 0.0814 0.1798 0.0313  -0.0119 -0.0427 385 THR A N   
3254 C CA  . THR A 385 ? 0.1864 0.0754 0.1903 0.0364  -0.0068 -0.0342 385 THR A CA  
3255 C C   . THR A 385 ? 0.1859 0.0909 0.1886 0.0458  0.0007  -0.0305 385 THR A C   
3256 O O   . THR A 385 ? 0.1926 0.1056 0.1835 0.0482  0.0038  -0.0363 385 THR A O   
3257 C CB  . THR A 385 ? 0.2053 0.0761 0.2153 0.0370  -0.0029 -0.0377 385 THR A CB  
3258 O OG1 . THR A 385 ? 0.2284 0.0903 0.2308 0.0441  0.0022  -0.0493 385 THR A OG1 
3259 C CG2 . THR A 385 ? 0.2065 0.0729 0.2174 0.0241  -0.0079 -0.0404 385 THR A CG2 
3260 N N   . LEU A 386 ? 0.1890 0.1025 0.2044 0.0516  0.0040  -0.0200 386 LEU A N   
3261 C CA  . LEU A 386 ? 0.1906 0.1249 0.2091 0.0621  0.0107  -0.0168 386 LEU A CA  
3262 C C   . LEU A 386 ? 0.2347 0.1570 0.2492 0.0742  0.0170  -0.0265 386 LEU A C   
3263 O O   . LEU A 386 ? 0.2275 0.1673 0.2381 0.0803  0.0228  -0.0296 386 LEU A O   
3264 C CB  . LEU A 386 ? 0.1837 0.1309 0.2162 0.0688  0.0115  -0.0037 386 LEU A CB  
3265 C CG  . LEU A 386 ? 0.1656 0.1278 0.2012 0.0574  0.0063  0.0043  386 LEU A CG  
3266 C CD1 . LEU A 386 ? 0.1709 0.1507 0.2175 0.0664  0.0069  0.0167  386 LEU A CD1 
3267 C CD2 . LEU A 386 ? 0.1844 0.1675 0.2141 0.0470  0.0063  0.0011  386 LEU A CD2 
3268 N N   . GLU A 387 ? 0.2368 0.1290 0.2533 0.0780  0.0175  -0.0316 387 GLU A N   
3269 C CA  . GLU A 387 ? 0.2891 0.1700 0.3037 0.0854  0.0237  -0.0429 387 GLU A CA  
3270 C C   . GLU A 387 ? 0.3240 0.2055 0.3184 0.0824  0.0234  -0.0576 387 GLU A C   
3271 O O   . GLU A 387 ? 0.3009 0.1912 0.2888 0.0917  0.0306  -0.0640 387 GLU A O   
3272 C CB  . GLU A 387 ? 0.4014 0.2581 0.4263 0.0801  0.0206  -0.0473 387 GLU A CB  
3273 C CG  . GLU A 387 ? 0.7029 0.5554 0.7339 0.0829  0.0163  -0.0321 387 GLU A CG  
3274 C CD  . GLU A 387 ? 0.9427 0.7938 0.9819 0.0976  0.0229  -0.0264 387 GLU A CD  
3275 O OE1 . GLU A 387 ? 0.9855 0.8216 1.0273 0.0986  0.0223  -0.0182 387 GLU A OE1 
3276 O OE2 . GLU A 387 ? 1.0022 0.8675 1.0432 0.1087  0.0297  -0.0292 387 GLU A OE2 
3277 N N   . GLU A 388 ? 0.2513 0.1278 0.2362 0.0696  0.0147  -0.0622 388 GLU A N   
3278 C CA  . GLU A 388 ? 0.3010 0.1833 0.2656 0.0658  0.0129  -0.0733 388 GLU A CA  
3279 C C   . GLU A 388 ? 0.3113 0.2214 0.2690 0.0677  0.0182  -0.0659 388 GLU A C   
3280 O O   . GLU A 388 ? 0.2966 0.2132 0.2392 0.0726  0.0237  -0.0740 388 GLU A O   
3281 C CB  . GLU A 388 ? 0.3054 0.1835 0.2643 0.0526  0.0017  -0.0757 388 GLU A CB  
3282 C CG  . GLU A 388 ? 0.3411 0.2025 0.3052 0.0443  -0.0010 -0.0848 388 GLU A CG  
3283 C CD  . GLU A 388 ? 0.3139 0.1788 0.2800 0.0320  -0.0118 -0.0834 388 GLU A CD  
3284 O OE1 . GLU A 388 ? 0.2677 0.1419 0.2355 0.0304  -0.0168 -0.0733 388 GLU A OE1 
3285 O OE2 . GLU A 388 ? 0.4161 0.2755 0.3813 0.0241  -0.0152 -0.0931 388 GLU A OE2 
3286 N N   . ALA A 389 ? 0.2550 0.1820 0.2232 0.0630  0.0177  -0.0515 389 ALA A N   
3287 C CA  . ALA A 389 ? 0.2153 0.1684 0.1803 0.0618  0.0243  -0.0454 389 ALA A CA  
3288 C C   . ALA A 389 ? 0.2831 0.2513 0.2541 0.0751  0.0347  -0.0479 389 ALA A C   
3289 O O   . ALA A 389 ? 0.2467 0.2322 0.2089 0.0761  0.0426  -0.0498 389 ALA A O   
3290 C CB  . ALA A 389 ? 0.1905 0.1580 0.1677 0.0526  0.0218  -0.0327 389 ALA A CB  
3291 N N   . MET A 390 ? 0.2439 0.2066 0.2302 0.0864  0.0360  -0.0466 390 MET A N   
3292 C CA  . MET A 390 ? 0.2781 0.2564 0.2727 0.1026  0.0460  -0.0476 390 MET A CA  
3293 C C   . MET A 390 ? 0.3102 0.2768 0.2889 0.1109  0.0531  -0.0629 390 MET A C   
3294 O O   . MET A 390 ? 0.3084 0.2970 0.2873 0.1203  0.0632  -0.0651 390 MET A O   
3295 C CB  . MET A 390 ? 0.3132 0.2822 0.3251 0.1154  0.0458  -0.0408 390 MET A CB  
3296 C CG  . MET A 390 ? 0.4341 0.4198 0.4583 0.1321  0.0543  -0.0390 390 MET A CG  
3297 S SD  . MET A 390 ? 0.5818 0.5594 0.6253 0.1401  0.0504  -0.0253 390 MET A SD  
3298 C CE  . MET A 390 ? 0.6469 0.5725 0.6841 0.1327  0.0468  -0.0347 390 MET A CE  
3299 N N   . ARG A 391 ? 0.3156 0.2513 0.2801 0.1066  0.0480  -0.0747 391 ARG A N   
3300 C CA  . ARG A 391 ? 0.4163 0.3401 0.3692 0.1093  0.0527  -0.0898 391 ARG A CA  
3301 C C   . ARG A 391 ? 0.4082 0.3376 0.3346 0.1022  0.0514  -0.0983 391 ARG A C   
3302 O O   . ARG A 391 ? 0.4033 0.3300 0.3178 0.1044  0.0565  -0.1101 391 ARG A O   
3303 C CB  . ARG A 391 ? 0.5330 0.4241 0.4926 0.1046  0.0488  -0.0975 391 ARG A CB  
3304 C CG  . ARG A 391 ? 0.6451 0.5276 0.6294 0.1126  0.0519  -0.0894 391 ARG A CG  
3305 C CD  . ARG A 391 ? 0.8485 0.7009 0.8397 0.1093  0.0533  -0.1018 391 ARG A CD  
3306 N NE  . ARG A 391 ? 0.9692 0.8120 0.9826 0.1168  0.0513  -0.0929 391 ARG A NE  
3307 C CZ  . ARG A 391 ? 1.0671 0.9108 1.0893 0.1326  0.0575  -0.0910 391 ARG A CZ  
3308 N NH1 . ARG A 391 ? 1.0897 0.9461 1.1060 0.1417  0.0672  -0.0989 391 ARG A NH1 
3309 N NH2 . ARG A 391 ? 1.1076 0.9394 1.1417 0.1397  0.0549  -0.0799 391 ARG A NH2 
3310 N N   . LYS A 392 ? 0.3329 0.2706 0.2507 0.0925  0.0450  -0.0907 392 LYS A N   
3311 C CA  . LYS A 392 ? 0.3732 0.3139 0.2650 0.0855  0.0419  -0.0951 392 LYS A CA  
3312 C C   . LYS A 392 ? 0.4247 0.3845 0.3013 0.0922  0.0545  -0.0982 392 LYS A C   
3313 O O   . LYS A 392 ? 0.3505 0.3331 0.2363 0.0942  0.0642  -0.0882 392 LYS A O   
3314 C CB  . LYS A 392 ? 0.3623 0.3108 0.2550 0.0726  0.0354  -0.0794 392 LYS A CB  
3315 C CG  . LYS A 392 ? 0.4760 0.4224 0.3430 0.0670  0.0292  -0.0809 392 LYS A CG  
3316 C CD  . LYS A 392 ? 0.5745 0.5036 0.4340 0.0669  0.0183  -0.0968 392 LYS A CD  
3317 C CE  . LYS A 392 ? 0.5055 0.4270 0.3746 0.0573  0.0054  -0.0906 392 LYS A CE  
3318 N NZ  . LYS A 392 ? 0.5654 0.4787 0.4240 0.0552  -0.0056 -0.1068 392 LYS A NZ  
3319 N N   . GLU A 393 ? 0.4342 0.3886 0.2924 0.0914  0.0541  -0.1101 393 GLU A N   
3320 C CA  . GLU A 393 ? 0.4579 0.4298 0.3051 0.0963  0.0668  -0.1123 393 GLU A CA  
3321 C C   . GLU A 393 ? 0.5188 0.5077 0.3443 0.0905  0.0702  -0.1019 393 GLU A C   
3322 O O   . GLU A 393 ? 0.5432 0.5521 0.3679 0.0921  0.0832  -0.0960 393 GLU A O   
3323 C CB  . GLU A 393 ? 0.5599 0.5187 0.3964 0.0990  0.0677  -0.1302 393 GLU A CB  
3324 C CG  . GLU A 393 ? 0.7560 0.7094 0.6121 0.1094  0.0777  -0.1368 393 GLU A CG  
3325 C CD  . GLU A 393 ? 0.9060 0.8407 0.7517 0.1109  0.0805  -0.1560 393 GLU A CD  
3326 O OE1 . GLU A 393 ? 0.9747 0.9130 0.8241 0.1205  0.0930  -0.1621 393 GLU A OE1 
3327 O OE2 . GLU A 393 ? 0.9551 0.8726 0.7897 0.1021  0.0706  -0.1655 393 GLU A OE2 
3328 N N   . ASP A 394 ? 0.4661 0.4476 0.2756 0.0835  0.0595  -0.0978 394 ASP A N   
3329 C CA  . ASP A 394 ? 0.5241 0.5170 0.3104 0.0789  0.0632  -0.0861 394 ASP A CA  
3330 C C   . ASP A 394 ? 0.4711 0.4703 0.2643 0.0730  0.0686  -0.0674 394 ASP A C   
3331 O O   . ASP A 394 ? 0.4843 0.4780 0.2633 0.0676  0.0644  -0.0558 394 ASP A O   
3332 C CB  . ASP A 394 ? 0.6343 0.6183 0.3997 0.0762  0.0492  -0.0898 394 ASP A CB  
3333 C CG  . ASP A 394 ? 0.7471 0.7154 0.5259 0.0730  0.0337  -0.0941 394 ASP A CG  
3334 O OD1 . ASP A 394 ? 0.7661 0.7258 0.5688 0.0741  0.0341  -0.0980 394 ASP A OD1 
3335 O OD2 . ASP A 394 ? 0.7818 0.7478 0.5491 0.0697  0.0214  -0.0927 394 ASP A OD2 
3336 N N   . VAL A 395 ? 0.4044 0.4163 0.2207 0.0736  0.0785  -0.0638 395 VAL A N   
3337 C CA  . VAL A 395 ? 0.3656 0.3861 0.1986 0.0616  0.0830  -0.0470 395 VAL A CA  
3338 C C   . VAL A 395 ? 0.3764 0.4242 0.2158 0.0613  0.1014  -0.0434 395 VAL A C   
3339 O O   . VAL A 395 ? 0.4333 0.4918 0.2756 0.0696  0.1072  -0.0530 395 VAL A O   
3340 C CB  . VAL A 395 ? 0.3711 0.3871 0.2354 0.0572  0.0735  -0.0450 395 VAL A CB  
3341 C CG1 . VAL A 395 ? 0.3779 0.3694 0.2381 0.0556  0.0568  -0.0474 395 VAL A CG1 
3342 C CG2 . VAL A 395 ? 0.4222 0.4492 0.3082 0.0678  0.0764  -0.0536 395 VAL A CG2 
3343 N N   . LYS A 396 ? 0.3418 0.3988 0.1894 0.0476  0.1090  -0.0296 396 LYS A N   
3344 C CA  . LYS A 396 ? 0.3304 0.4153 0.1893 0.0419  0.1259  -0.0258 396 LYS A CA  
3345 C C   . LYS A 396 ? 0.3037 0.4140 0.1994 0.0415  0.1268  -0.0279 396 LYS A C   
3346 O O   . LYS A 396 ? 0.2805 0.3841 0.1931 0.0357  0.1159  -0.0254 396 LYS A O   
3347 C CB  . LYS A 396 ? 0.3649 0.4459 0.2140 0.0250  0.1352  -0.0111 396 LYS A CB  
3348 C CG  . LYS A 396 ? 0.4261 0.5300 0.2861 0.0146  0.1523  -0.0083 396 LYS A CG  
3349 C CD  . LYS A 396 ? 0.5145 0.6170 0.3723 -0.0044 0.1581  0.0062  396 LYS A CD  
3350 C CE  . LYS A 396 ? 0.5310 0.6597 0.3970 -0.0124 0.1708  0.0115  396 LYS A CE  
3351 N NZ  . LYS A 396 ? 0.6905 0.8073 0.5281 -0.0058 0.1814  0.0044  396 LYS A NZ  
3352 N N   . THR A 397 ? 0.4273 0.3429 0.1533 0.0654  0.0049  0.0005  397 THR A N   
3353 C CA  . THR A 397 ? 0.3956 0.3285 0.1515 0.0622  0.0173  -0.0030 397 THR A CA  
3354 C C   . THR A 397 ? 0.4003 0.3417 0.1521 0.0579  0.0374  0.0058  397 THR A C   
3355 O O   . THR A 397 ? 0.4588 0.3921 0.1796 0.0575  0.0440  0.0127  397 THR A O   
3356 C CB  . THR A 397 ? 0.3963 0.3302 0.1507 0.0676  0.0167  -0.0167 397 THR A CB  
3357 O OG1 . THR A 397 ? 0.4404 0.3681 0.1605 0.0738  0.0259  -0.0192 397 THR A OG1 
3358 C CG2 . THR A 397 ? 0.4431 0.3677 0.1971 0.0682  -0.0038 -0.0251 397 THR A CG2 
3359 N N   . GLU A 398 ? 0.3695 0.3289 0.1527 0.0536  0.0469  0.0058  398 GLU A N   
3360 C CA  . GLU A 398 ? 0.4138 0.3893 0.2002 0.0481  0.0660  0.0123  398 GLU A CA  
3361 C C   . GLU A 398 ? 0.3673 0.3649 0.1862 0.0495  0.0728  0.0055  398 GLU A C   
3362 O O   . GLU A 398 ? 0.3551 0.3520 0.1962 0.0509  0.0629  -0.0004 398 GLU A O   
3363 C CB  . GLU A 398 ? 0.5462 0.5164 0.3340 0.0365  0.0684  0.0262  398 GLU A CB  
3364 C CG  . GLU A 398 ? 0.7985 0.7843 0.5822 0.0269  0.0880  0.0347  398 GLU A CG  
3365 C CD  . GLU A 398 ? 0.9497 0.9418 0.7043 0.0327  0.0997  0.0326  398 GLU A CD  
3366 O OE1 . GLU A 398 ? 1.0469 1.0199 0.7654 0.0319  0.0985  0.0392  398 GLU A OE1 
3367 O OE2 . GLU A 398 ? 0.9903 1.0057 0.7562 0.0394  0.1098  0.0241  398 GLU A OE2 
3368 N N   . VAL A 399 ? 0.3476 0.3666 0.1684 0.0493  0.0901  0.0066  399 VAL A N   
3369 C CA  . VAL A 399 ? 0.3157 0.3588 0.1659 0.0522  0.0974  0.0012  399 VAL A CA  
3370 C C   . VAL A 399 ? 0.3427 0.4021 0.2189 0.0385  0.1031  0.0106  399 VAL A C   
3371 O O   . VAL A 399 ? 0.3743 0.4345 0.2402 0.0272  0.1104  0.0212  399 VAL A O   
3372 C CB  . VAL A 399 ? 0.3332 0.3949 0.1730 0.0620  0.1116  -0.0046 399 VAL A CB  
3373 C CG1 . VAL A 399 ? 0.3651 0.4506 0.2404 0.0635  0.1146  -0.0101 399 VAL A CG1 
3374 C CG2 . VAL A 399 ? 0.3848 0.4247 0.1965 0.0751  0.1038  -0.0152 399 VAL A CG2 
3375 N N   . ILE A 400 ? 0.2892 0.3592 0.1961 0.0384  0.0996  0.0068  400 ILE A N   
3376 C CA  . ILE A 400 ? 0.3077 0.3947 0.2400 0.0262  0.1044  0.0134  400 ILE A CA  
3377 C C   . ILE A 400 ? 0.3147 0.4318 0.2708 0.0319  0.1119  0.0072  400 ILE A C   
3378 O O   . ILE A 400 ? 0.3146 0.4282 0.2772 0.0437  0.1054  -0.0021 400 ILE A O   
3379 C CB  . ILE A 400 ? 0.3491 0.4188 0.2950 0.0204  0.0907  0.0151  400 ILE A CB  
3380 C CG1 . ILE A 400 ? 0.4362 0.5221 0.4080 0.0091  0.0944  0.0195  400 ILE A CG1 
3381 C CG2 . ILE A 400 ? 0.3581 0.4186 0.3118 0.0306  0.0790  0.0055  400 ILE A CG2 
3382 C CD1 . ILE A 400 ? 0.5239 0.5917 0.5052 0.0052  0.0820  0.0204  400 ILE A CD1 
3383 N N   . GLU A 401 ? 0.2849 0.4214 0.2542 0.0202  0.1196  0.0107  401 GLU A N   
3384 C CA  . GLU A 401 ? 0.2847 0.4407 0.2760 0.0246  0.1212  0.0035  401 GLU A CA  
3385 C C   . GLU A 401 ? 0.2576 0.4215 0.2775 0.0178  0.1159  0.0040  401 GLU A C   
3386 O O   . GLU A 401 ? 0.2812 0.4560 0.3172 0.0250  0.1136  -0.0018 401 GLU A O   
3387 C CB  . GLU A 401 ? 0.3062 0.4805 0.2949 0.0196  0.1336  0.0057  401 GLU A CB  
3388 C CG  . GLU A 401 ? 0.4100 0.5786 0.3705 0.0284  0.1393  0.0029  401 GLU A CG  
3389 C CD  . GLU A 401 ? 0.5814 0.7435 0.5371 0.0484  0.1334  -0.0086 401 GLU A CD  
3390 O OE1 . GLU A 401 ? 0.6823 0.8294 0.6107 0.0570  0.1333  -0.0120 401 GLU A OE1 
3391 O OE2 . GLU A 401 ? 0.6190 0.7878 0.5954 0.0553  0.1281  -0.0139 401 GLU A OE2 
3392 N N   . SER A 402 ? 0.2076 0.3644 0.2315 0.0050  0.1131  0.0111  402 SER A N   
3393 C CA  . SER A 402 ? 0.1939 0.3562 0.2419 -0.0024 0.1081  0.0115  402 SER A CA  
3394 C C   . SER A 402 ? 0.2497 0.3963 0.2955 -0.0112 0.1024  0.0173  402 SER A C   
3395 O O   . SER A 402 ? 0.2948 0.4306 0.3224 -0.0188 0.1058  0.0260  402 SER A O   
3396 C CB  . SER A 402 ? 0.2299 0.4103 0.2894 -0.0131 0.1153  0.0158  402 SER A CB  
3397 O OG  . SER A 402 ? 0.3036 0.4886 0.3842 -0.0185 0.1090  0.0157  402 SER A OG  
3398 N N   . VAL A 403 ? 0.1943 0.3377 0.2560 -0.0094 0.0936  0.0134  403 VAL A N   
3399 C CA  . VAL A 403 ? 0.2215 0.3528 0.2850 -0.0177 0.0884  0.0188  403 VAL A CA  
3400 C C   . VAL A 403 ? 0.2251 0.3606 0.3058 -0.0279 0.0856  0.0187  403 VAL A C   
3401 O O   . VAL A 403 ? 0.2104 0.3581 0.3050 -0.0241 0.0850  0.0146  403 VAL A O   
3402 C CB  . VAL A 403 ? 0.2096 0.3230 0.2728 -0.0066 0.0779  0.0136  403 VAL A CB  
3403 C CG1 . VAL A 403 ? 0.2367 0.3350 0.2795 0.0033  0.0761  0.0116  403 VAL A CG1 
3404 C CG2 . VAL A 403 ? 0.2432 0.3677 0.3231 0.0002  0.0732  0.0056  403 VAL A CG2 
3405 N N   . LYS A 404 ? 0.1774 0.3009 0.2549 -0.0402 0.0830  0.0250  404 LYS A N   
3406 C CA  . LYS A 404 ? 0.1569 0.2801 0.2474 -0.0486 0.0773  0.0255  404 LYS A CA  
3407 C C   . LYS A 404 ? 0.1439 0.2609 0.2409 -0.0417 0.0679  0.0195  404 LYS A C   
3408 O O   . LYS A 404 ? 0.1775 0.2691 0.2641 -0.0381 0.0636  0.0185  404 LYS A O   
3409 C CB  . LYS A 404 ? 0.2339 0.3385 0.3105 -0.0677 0.0781  0.0330  404 LYS A CB  
3410 C CG  . LYS A 404 ? 0.5022 0.6141 0.5729 -0.0768 0.0857  0.0395  404 LYS A CG  
3411 C CD  . LYS A 404 ? 0.5932 0.7175 0.6796 -0.0862 0.0837  0.0392  404 LYS A CD  
3412 C CE  . LYS A 404 ? 0.6821 0.8077 0.7597 -0.1013 0.0904  0.0468  404 LYS A CE  
3413 N NZ  . LYS A 404 ? 0.7044 0.8638 0.8024 -0.1006 0.0947  0.0439  404 LYS A NZ  
3414 N N   . ALA A 405 ? 0.1345 0.2626 0.2440 -0.0345 0.0615  0.0171  405 ALA A N   
3415 C CA  . ALA A 405 ? 0.1088 0.2324 0.2186 -0.0276 0.0528  0.0105  405 ALA A CA  
3416 C C   . ALA A 405 ? 0.1588 0.2618 0.2694 -0.0350 0.0508  0.0089  405 ALA A C   
3417 O O   . ALA A 405 ? 0.1625 0.2601 0.2731 -0.0484 0.0517  0.0117  405 ALA A O   
3418 C CB  . ALA A 405 ? 0.1130 0.2456 0.2308 -0.0214 0.0476  0.0116  405 ALA A CB  
3419 N N   . GLY A 406 ? 0.1379 0.2284 0.2492 -0.0261 0.0477  0.0050  406 GLY A N   
3420 C CA  . GLY A 406 ? 0.1371 0.2059 0.2417 -0.0273 0.0417  0.0036  406 GLY A CA  
3421 C C   . GLY A 406 ? 0.1397 0.2032 0.2443 -0.0152 0.0371  -0.0008 406 GLY A C   
3422 O O   . GLY A 406 ? 0.1075 0.1833 0.2186 -0.0087 0.0379  -0.0029 406 GLY A O   
3423 N N   . THR A 407 ? 0.1050 0.1500 0.2016 -0.0123 0.0320  -0.0025 407 THR A N   
3424 C CA  . THR A 407 ? 0.0833 0.1270 0.1810 -0.0012 0.0277  -0.0067 407 THR A CA  
3425 C C   . THR A 407 ? 0.1086 0.1309 0.1914 0.0045  0.0232  -0.0053 407 THR A C   
3426 O O   . THR A 407 ? 0.1382 0.1416 0.2070 -0.0008 0.0232  -0.0006 407 THR A O   
3427 C CB  . THR A 407 ? 0.1040 0.1517 0.2086 0.0007  0.0256  -0.0121 407 THR A CB  
3428 O OG1 . THR A 407 ? 0.1290 0.1557 0.2224 0.0002  0.0221  -0.0134 407 THR A OG1 
3429 C CG2 . THR A 407 ? 0.1236 0.1878 0.2390 -0.0054 0.0283  -0.0128 407 THR A CG2 
3430 N N   . TRP A 408 ? 0.1158 0.1410 0.2011 0.0154  0.0189  -0.0092 408 TRP A N   
3431 C CA  . TRP A 408 ? 0.1188 0.1254 0.1906 0.0246  0.0129  -0.0088 408 TRP A CA  
3432 C C   . TRP A 408 ? 0.1519 0.1375 0.2140 0.0276  0.0095  -0.0114 408 TRP A C   
3433 O O   . TRP A 408 ? 0.2171 0.1821 0.2646 0.0375  0.0036  -0.0112 408 TRP A O   
3434 C CB  . TRP A 408 ? 0.1606 0.1835 0.2406 0.0356  0.0088  -0.0125 408 TRP A CB  
3435 C CG  . TRP A 408 ? 0.1218 0.1661 0.2181 0.0398  0.0091  -0.0190 408 TRP A CG  
3436 C CD1 . TRP A 408 ? 0.1412 0.1887 0.2426 0.0377  0.0120  -0.0226 408 TRP A CD1 
3437 C CD2 . TRP A 408 ? 0.1054 0.1722 0.2135 0.0457  0.0066  -0.0223 408 TRP A CD2 
3438 N NE1 . TRP A 408 ? 0.1374 0.2073 0.2506 0.0419  0.0125  -0.0270 408 TRP A NE1 
3439 C CE2 . TRP A 408 ? 0.1301 0.2098 0.2434 0.0444  0.0093  -0.0249 408 TRP A CE2 
3440 C CE3 . TRP A 408 ? 0.0904 0.1652 0.1991 0.0494  0.0017  -0.0216 408 TRP A CE3 
3441 C CZ2 . TRP A 408 ? 0.0957 0.1919 0.2115 0.0433  0.0087  -0.0236 408 TRP A CZ2 
3442 C CZ3 . TRP A 408 ? 0.1056 0.2016 0.2226 0.0492  0.0001  -0.0231 408 TRP A CZ3 
3443 C CH2 . TRP A 408 ? 0.1056 0.2101 0.2249 0.0449  0.0043  -0.0229 408 TRP A CH2 
3444 N N   . PHE A 409 ? 0.1609 0.1479 0.2276 0.0200  0.0121  -0.0140 409 PHE A N   
3445 C CA  . PHE A 409 ? 0.2463 0.2072 0.2989 0.0208  0.0083  -0.0169 409 PHE A CA  
3446 C C   . PHE A 409 ? 0.2759 0.2158 0.3155 0.0047  0.0095  -0.0105 409 PHE A C   
3447 O O   . PHE A 409 ? 0.2162 0.1679 0.2645 -0.0087 0.0133  -0.0097 409 PHE A O   
3448 C CB  . PHE A 409 ? 0.2713 0.2442 0.3332 0.0219  0.0093  -0.0243 409 PHE A CB  
3449 C CG  . PHE A 409 ? 0.3868 0.3329 0.4322 0.0300  0.0041  -0.0305 409 PHE A CG  
3450 C CD1 . PHE A 409 ? 0.4913 0.4012 0.5157 0.0222  0.0002  -0.0284 409 PHE A CD1 
3451 C CD2 . PHE A 409 ? 0.4713 0.4283 0.5209 0.0452  0.0033  -0.0386 409 PHE A CD2 
3452 C CE1 . PHE A 409 ? 0.5080 0.3873 0.5132 0.0307  -0.0056 -0.0350 409 PHE A CE1 
3453 C CE2 . PHE A 409 ? 0.5775 0.5091 0.6099 0.0558  -0.0013 -0.0456 409 PHE A CE2 
3454 C CZ  . PHE A 409 ? 0.5935 0.4836 0.6024 0.0491  -0.0063 -0.0441 409 PHE A CZ  
3455 N N   . ASP A 410 ? 0.3050 0.2151 0.3235 0.0058  0.0059  -0.0053 410 ASP A N   
3456 C CA  . ASP A 410 ? 0.3527 0.2388 0.3547 -0.0115 0.0071  0.0022  410 ASP A CA  
3457 C C   . ASP A 410 ? 0.2993 0.2122 0.3145 -0.0265 0.0156  0.0081  410 ASP A C   
3458 O O   . ASP A 410 ? 0.3320 0.2376 0.3411 -0.0444 0.0185  0.0133  410 ASP A O   
3459 C CB  . ASP A 410 ? 0.4965 0.3610 0.4895 -0.0210 0.0038  -0.0015 410 ASP A CB  
3460 C CG  . ASP A 410 ? 0.6524 0.4850 0.6274 -0.0048 -0.0045 -0.0082 410 ASP A CG  
3461 O OD1 . ASP A 410 ? 0.7127 0.5278 0.6741 0.0103  -0.0089 -0.0066 410 ASP A OD1 
3462 O OD2 . ASP A 410 ? 0.7397 0.5651 0.7131 -0.0059 -0.0070 -0.0155 410 ASP A OD2 
3463 N N   . GLY A 411 ? 0.2595 0.2037 0.2922 -0.0197 0.0196  0.0070  411 GLY A N   
3464 C CA  . GLY A 411 ? 0.2193 0.1894 0.2636 -0.0295 0.0276  0.0110  411 GLY A CA  
3465 C C   . GLY A 411 ? 0.2530 0.2452 0.3144 -0.0406 0.0310  0.0088  411 GLY A C   
3466 O O   . GLY A 411 ? 0.2438 0.2549 0.3123 -0.0510 0.0375  0.0128  411 GLY A O   
3467 N N   . ASN A 412 ? 0.2083 0.2004 0.2759 -0.0382 0.0268  0.0022  412 ASN A N   
3468 C CA  . ASN A 412 ? 0.1738 0.1853 0.2553 -0.0486 0.0280  0.0000  412 ASN A CA  
3469 C C   . ASN A 412 ? 0.1654 0.1882 0.2573 -0.0383 0.0251  -0.0075 412 ASN A C   
3470 O O   . ASN A 412 ? 0.1534 0.1727 0.2438 -0.0249 0.0234  -0.0106 412 ASN A O   
3471 C CB  . ASN A 412 ? 0.2041 0.1953 0.2740 -0.0655 0.0252  0.0017  412 ASN A CB  
3472 C CG  . ASN A 412 ? 0.2071 0.1630 0.2591 -0.0605 0.0174  -0.0034 412 ASN A CG  
3473 O OD1 . ASN A 412 ? 0.2356 0.1949 0.2919 -0.0483 0.0144  -0.0108 412 ASN A OD1 
3474 N ND2 . ASN A 412 ? 0.2892 0.2094 0.3187 -0.0701 0.0142  0.0005  412 ASN A ND2 
3475 N N   . PHE A 413 ? 0.1423 0.1810 0.2446 -0.0454 0.0244  -0.0101 413 PHE A N   
3476 C CA  . PHE A 413 ? 0.1472 0.2001 0.2585 -0.0372 0.0228  -0.0157 413 PHE A CA  
3477 C C   . PHE A 413 ? 0.1557 0.1936 0.2583 -0.0385 0.0172  -0.0219 413 PHE A C   
3478 O O   . PHE A 413 ? 0.1450 0.1952 0.2530 -0.0342 0.0160  -0.0261 413 PHE A O   
3479 C CB  . PHE A 413 ? 0.1199 0.2033 0.2477 -0.0402 0.0253  -0.0143 413 PHE A CB  
3480 C CG  . PHE A 413 ? 0.1327 0.2240 0.2562 -0.0319 0.0278  -0.0084 413 PHE A CG  
3481 C CD1 . PHE A 413 ? 0.1392 0.2292 0.2572 -0.0200 0.0268  -0.0088 413 PHE A CD1 
3482 C CD2 . PHE A 413 ? 0.1533 0.2530 0.2767 -0.0377 0.0309  -0.0029 413 PHE A CD2 
3483 C CE1 . PHE A 413 ? 0.1111 0.2046 0.2236 -0.0145 0.0281  -0.0054 413 PHE A CE1 
3484 C CE2 . PHE A 413 ? 0.1891 0.2962 0.3088 -0.0299 0.0335  0.0005  413 PHE A CE2 
3485 C CZ  . PHE A 413 ? 0.1020 0.2045 0.2160 -0.0184 0.0317  -0.0016 413 PHE A CZ  
3486 N N   . LEU A 414 ? 0.1594 0.1679 0.2454 -0.0439 0.0135  -0.0226 414 LEU A N   
3487 C CA  . LEU A 414 ? 0.1830 0.1752 0.2582 -0.0477 0.0075  -0.0293 414 LEU A CA  
3488 C C   . LEU A 414 ? 0.1866 0.1738 0.2561 -0.0315 0.0061  -0.0370 414 LEU A C   
3489 O O   . LEU A 414 ? 0.2017 0.1809 0.2629 -0.0328 0.0019  -0.0436 414 LEU A O   
3490 C CB  . LEU A 414 ? 0.2353 0.1908 0.2898 -0.0585 0.0031  -0.0282 414 LEU A CB  
3491 C CG  . LEU A 414 ? 0.2265 0.1890 0.2857 -0.0800 0.0047  -0.0209 414 LEU A CG  
3492 C CD1 . LEU A 414 ? 0.3307 0.2503 0.3648 -0.0920 0.0003  -0.0184 414 LEU A CD1 
3493 C CD2 . LEU A 414 ? 0.2750 0.2650 0.3493 -0.0920 0.0026  -0.0234 414 LEU A CD2 
3494 N N   . LYS A 415 ? 0.1613 0.1552 0.2348 -0.0171 0.0095  -0.0366 415 LYS A N   
3495 C CA  . LYS A 415 ? 0.1857 0.1832 0.2569 -0.0034 0.0096  -0.0437 415 LYS A CA  
3496 C C   . LYS A 415 ? 0.1784 0.2046 0.2626 -0.0038 0.0127  -0.0443 415 LYS A C   
3497 O O   . LYS A 415 ? 0.1432 0.1761 0.2253 0.0053  0.0142  -0.0495 415 LYS A O   
3498 C CB  . LYS A 415 ? 0.1722 0.1699 0.2440 0.0113  0.0114  -0.0436 415 LYS A CB  
3499 C CG  . LYS A 415 ? 0.2601 0.2244 0.3135 0.0172  0.0066  -0.0445 415 LYS A CG  
3500 C CD  . LYS A 415 ? 0.3494 0.2881 0.3839 0.0229  0.0020  -0.0533 415 LYS A CD  
3501 C CE  . LYS A 415 ? 0.4097 0.3569 0.4438 0.0438  0.0031  -0.0609 415 LYS A CE  
3502 N NZ  . LYS A 415 ? 0.5343 0.4482 0.5442 0.0542  -0.0022 -0.0700 415 LYS A NZ  
3503 N N   . TRP A 416 ? 0.1315 0.1749 0.2277 -0.0132 0.0138  -0.0390 416 TRP A N   
3504 C CA  . TRP A 416 ? 0.1334 0.1992 0.2384 -0.0123 0.0155  -0.0385 416 TRP A CA  
3505 C C   . TRP A 416 ? 0.0978 0.1723 0.2060 -0.0222 0.0118  -0.0381 416 TRP A C   
3506 O O   . TRP A 416 ? 0.1373 0.2265 0.2489 -0.0205 0.0114  -0.0379 416 TRP A O   
3507 C CB  . TRP A 416 ? 0.0867 0.1681 0.2035 -0.0091 0.0200  -0.0328 416 TRP A CB  
3508 C CG  . TRP A 416 ? 0.0629 0.1412 0.1789 -0.0004 0.0225  -0.0334 416 TRP A CG  
3509 C CD1 . TRP A 416 ? 0.0776 0.1623 0.1907 0.0062  0.0241  -0.0345 416 TRP A CD1 
3510 C CD2 . TRP A 416 ? 0.1007 0.1674 0.2141 0.0020  0.0221  -0.0316 416 TRP A CD2 
3511 N NE1 . TRP A 416 ? 0.1033 0.1848 0.2149 0.0126  0.0242  -0.0340 416 TRP A NE1 
3512 C CE2 . TRP A 416 ? 0.1062 0.1776 0.2210 0.0117  0.0233  -0.0337 416 TRP A CE2 
3513 C CE3 . TRP A 416 ? 0.1246 0.1782 0.2339 -0.0038 0.0210  -0.0280 416 TRP A CE3 
3514 C CZ2 . TRP A 416 ? 0.1381 0.2010 0.2501 0.0177  0.0218  -0.0327 416 TRP A CZ2 
3515 C CZ3 . TRP A 416 ? 0.1413 0.1828 0.2448 0.0015  0.0204  -0.0262 416 TRP A CZ3 
3516 C CH2 . TRP A 416 ? 0.1511 0.1970 0.2559 0.0130  0.0201  -0.0287 416 TRP A CH2 
3517 N N   . ILE A 417 ? 0.1077 0.1746 0.2149 -0.0332 0.0085  -0.0373 417 ILE A N   
3518 C CA  . ILE A 417 ? 0.0943 0.1761 0.2083 -0.0440 0.0042  -0.0369 417 ILE A CA  
3519 C C   . ILE A 417 ? 0.1953 0.2599 0.3016 -0.0582 -0.0001 -0.0382 417 ILE A C   
3520 O O   . ILE A 417 ? 0.2266 0.2690 0.3238 -0.0596 0.0014  -0.0367 417 ILE A O   
3521 C CB  . ILE A 417 ? 0.1009 0.2093 0.2323 -0.0435 0.0077  -0.0303 417 ILE A CB  
3522 C CG1 . ILE A 417 ? 0.1252 0.2502 0.2592 -0.0461 0.0020  -0.0282 417 ILE A CG1 
3523 C CG2 . ILE A 417 ? 0.1446 0.2490 0.2765 -0.0486 0.0112  -0.0238 417 ILE A CG2 
3524 C CD1 . ILE A 417 ? 0.1501 0.2866 0.2869 -0.0358 0.0038  -0.0195 417 ILE A CD1 
3525 N N   . GLY A 418 ? 0.1891 0.2622 0.2970 -0.0696 -0.0066 -0.0407 418 GLY A N   
3526 C CA  . GLY A 418 ? 0.2598 0.3203 0.3624 -0.0880 -0.0112 -0.0410 418 GLY A CA  
3527 C C   . GLY A 418 ? 0.3402 0.3681 0.4199 -0.0932 -0.0192 -0.0493 418 GLY A C   
3528 O O   . GLY A 418 ? 0.3996 0.4097 0.4708 -0.1105 -0.0240 -0.0494 418 GLY A O   
3529 N N   . ASN A 419 ? 0.3075 0.3256 0.3750 -0.0796 -0.0208 -0.0563 419 ASN A N   
3530 C CA  . ASN A 419 ? 0.2636 0.2555 0.3090 -0.0839 -0.0293 -0.0658 419 ASN A CA  
3531 C C   . ASN A 419 ? 0.2732 0.2858 0.3200 -0.0789 -0.0329 -0.0703 419 ASN A C   
3532 O O   . ASN A 419 ? 0.2965 0.3389 0.3592 -0.0709 -0.0285 -0.0656 419 ASN A O   
3533 C CB  . ASN A 419 ? 0.3436 0.2956 0.3648 -0.0713 -0.0283 -0.0717 419 ASN A CB  
3534 C CG  . ASN A 419 ? 0.4310 0.3921 0.4517 -0.0488 -0.0217 -0.0746 419 ASN A CG  
3535 O OD1 . ASN A 419 ? 0.3513 0.3385 0.3804 -0.0438 -0.0198 -0.0747 419 ASN A OD1 
3536 N ND2 . ASN A 419 ? 0.4783 0.4166 0.4873 -0.0355 -0.0186 -0.0770 419 ASN A ND2 
3537 N N   . LYS A 420 ? 0.2959 0.2895 0.3227 -0.0841 -0.0417 -0.0795 420 LYS A N   
3538 C CA  . LYS A 420 ? 0.3014 0.3149 0.3275 -0.0825 -0.0472 -0.0833 420 LYS A CA  
3539 C C   . LYS A 420 ? 0.2919 0.3169 0.3170 -0.0626 -0.0393 -0.0826 420 LYS A C   
3540 O O   . LYS A 420 ? 0.2681 0.3210 0.3043 -0.0593 -0.0391 -0.0783 420 LYS A O   
3541 C CB  . LYS A 420 ? 0.4114 0.3973 0.4108 -0.0902 -0.0582 -0.0947 420 LYS A CB  
3542 C CG  . LYS A 420 ? 0.5559 0.5395 0.5582 -0.1150 -0.0689 -0.0953 420 LYS A CG  
3543 C CD  . LYS A 420 ? 0.6676 0.6265 0.6422 -0.1225 -0.0817 -0.1076 420 LYS A CD  
3544 C CE  . LYS A 420 ? 0.7638 0.6929 0.7306 -0.1361 -0.0871 -0.1078 420 LYS A CE  
3545 N NZ  . LYS A 420 ? 0.7977 0.7550 0.7947 -0.1504 -0.0854 -0.0957 420 LYS A NZ  
3546 N N   . GLU A 421 ? 0.2954 0.2997 0.3069 -0.0491 -0.0327 -0.0864 421 GLU A N   
3547 C CA  . GLU A 421 ? 0.3148 0.3313 0.3238 -0.0330 -0.0249 -0.0864 421 GLU A CA  
3548 C C   . GLU A 421 ? 0.2365 0.2787 0.2689 -0.0287 -0.0167 -0.0756 421 GLU A C   
3549 O O   . GLU A 421 ? 0.2317 0.2933 0.2679 -0.0239 -0.0140 -0.0718 421 GLU A O   
3550 C CB  . GLU A 421 ? 0.3649 0.3575 0.3551 -0.0193 -0.0203 -0.0945 421 GLU A CB  
3551 C CG  . GLU A 421 ? 0.4981 0.4590 0.4591 -0.0202 -0.0284 -0.1072 421 GLU A CG  
3552 C CD  . GLU A 421 ? 0.6683 0.6007 0.6233 -0.0354 -0.0377 -0.1088 421 GLU A CD  
3553 O OE1 . GLU A 421 ? 0.6926 0.6199 0.6593 -0.0387 -0.0350 -0.1021 421 GLU A OE1 
3554 O OE2 . GLU A 421 ? 0.7764 0.6906 0.7131 -0.0455 -0.0480 -0.1165 421 GLU A OE2 
3555 N N   . LYS A 422 ? 0.2460 0.2851 0.2908 -0.0305 -0.0132 -0.0706 422 LYS A N   
3556 C CA  . LYS A 422 ? 0.1824 0.2430 0.2470 -0.0272 -0.0066 -0.0613 422 LYS A CA  
3557 C C   . LYS A 422 ? 0.2235 0.3074 0.3022 -0.0343 -0.0104 -0.0558 422 LYS A C   
3558 O O   . LYS A 422 ? 0.1908 0.2915 0.2773 -0.0283 -0.0070 -0.0504 422 LYS A O   
3559 C CB  . LYS A 422 ? 0.2288 0.2799 0.3006 -0.0277 -0.0029 -0.0577 422 LYS A CB  
3560 C CG  . LYS A 422 ? 0.2044 0.2391 0.2658 -0.0153 0.0015  -0.0619 422 LYS A CG  
3561 C CD  . LYS A 422 ? 0.2074 0.2253 0.2695 -0.0158 0.0021  -0.0592 422 LYS A CD  
3562 C CE  . LYS A 422 ? 0.1890 0.1853 0.2360 -0.0023 0.0028  -0.0658 422 LYS A CE  
3563 N NZ  . LYS A 422 ? 0.1896 0.2061 0.2436 0.0120  0.0098  -0.0666 422 LYS A NZ  
3564 N N   . ASN A 423 ? 0.1797 0.2651 0.2609 -0.0470 -0.0181 -0.0572 423 ASN A N   
3565 C CA  . ASN A 423 ? 0.1985 0.3120 0.2953 -0.0513 -0.0224 -0.0527 423 ASN A CA  
3566 C C   . ASN A 423 ? 0.2088 0.3312 0.2971 -0.0439 -0.0261 -0.0538 423 ASN A C   
3567 O O   . ASN A 423 ? 0.1655 0.3085 0.2641 -0.0392 -0.0270 -0.0483 423 ASN A O   
3568 C CB  . ASN A 423 ? 0.2046 0.3234 0.3072 -0.0683 -0.0305 -0.0546 423 ASN A CB  
3569 C CG  . ASN A 423 ? 0.1825 0.3016 0.2976 -0.0773 -0.0257 -0.0496 423 ASN A CG  
3570 O OD1 . ASN A 423 ? 0.1690 0.2859 0.2891 -0.0694 -0.0170 -0.0448 423 ASN A OD1 
3571 N ND2 . ASN A 423 ? 0.1945 0.3135 0.3111 -0.0933 -0.0313 -0.0491 423 ASN A ND2 
3572 N N   . GLU A 424 ? 0.2025 0.3080 0.2694 -0.0415 -0.0282 -0.0609 424 GLU A N   
3573 C CA  . GLU A 424 ? 0.2194 0.3318 0.2743 -0.0351 -0.0312 -0.0612 424 GLU A CA  
3574 C C   . GLU A 424 ? 0.2049 0.3248 0.2632 -0.0245 -0.0227 -0.0535 424 GLU A C   
3575 O O   . GLU A 424 ? 0.1695 0.3007 0.2260 -0.0205 -0.0259 -0.0488 424 GLU A O   
3576 C CB  . GLU A 424 ? 0.3352 0.4274 0.3640 -0.0333 -0.0329 -0.0707 424 GLU A CB  
3577 C CG  . GLU A 424 ? 0.5086 0.6060 0.5201 -0.0268 -0.0345 -0.0707 424 GLU A CG  
3578 C CD  . GLU A 424 ? 0.7275 0.8417 0.7418 -0.0313 -0.0468 -0.0685 424 GLU A CD  
3579 O OE1 . GLU A 424 ? 0.7871 0.9092 0.8143 -0.0416 -0.0554 -0.0704 424 GLU A OE1 
3580 O OE2 . GLU A 424 ? 0.7900 0.9102 0.7928 -0.0247 -0.0483 -0.0647 424 GLU A OE2 
3581 N N   . TYR A 425 ? 0.1512 0.2636 0.2130 -0.0202 -0.0129 -0.0520 425 TYR A N   
3582 C CA  . TYR A 425 ? 0.1445 0.2629 0.2097 -0.0133 -0.0055 -0.0448 425 TYR A CA  
3583 C C   . TYR A 425 ? 0.1360 0.2676 0.2173 -0.0129 -0.0076 -0.0373 425 TYR A C   
3584 O O   . TYR A 425 ? 0.1402 0.2754 0.2176 -0.0080 -0.0076 -0.0315 425 TYR A O   
3585 C CB  . TYR A 425 ? 0.1151 0.2266 0.1836 -0.0099 0.0039  -0.0453 425 TYR A CB  
3586 C CG  . TYR A 425 ? 0.1139 0.2209 0.1675 -0.0047 0.0097  -0.0497 425 TYR A CG  
3587 C CD1 . TYR A 425 ? 0.1354 0.2378 0.1698 -0.0040 0.0066  -0.0558 425 TYR A CD1 
3588 C CD2 . TYR A 425 ? 0.1053 0.2152 0.1638 -0.0004 0.0184  -0.0485 425 TYR A CD2 
3589 C CE1 . TYR A 425 ? 0.1553 0.2569 0.1757 0.0020  0.0136  -0.0603 425 TYR A CE1 
3590 C CE2 . TYR A 425 ? 0.1302 0.2428 0.1779 0.0049  0.0249  -0.0528 425 TYR A CE2 
3591 C CZ  . TYR A 425 ? 0.1573 0.2660 0.1858 0.0065  0.0233  -0.0587 425 TYR A CZ  
3592 O OH  . TYR A 425 ? 0.1545 0.2693 0.1726 0.0129  0.0315  -0.0634 425 TYR A OH  
3593 N N   . TRP A 426 ? 0.1200 0.2575 0.2170 -0.0178 -0.0093 -0.0373 426 TRP A N   
3594 C CA  . TRP A 426 ? 0.1018 0.2552 0.2139 -0.0152 -0.0106 -0.0314 426 TRP A CA  
3595 C C   . TRP A 426 ? 0.0889 0.2566 0.1998 -0.0129 -0.0200 -0.0304 426 TRP A C   
3596 O O   . TRP A 426 ? 0.1194 0.2937 0.2321 -0.0043 -0.0212 -0.0251 426 TRP A O   
3597 C CB  . TRP A 426 ? 0.0947 0.2544 0.2227 -0.0219 -0.0092 -0.0314 426 TRP A CB  
3598 C CG  . TRP A 426 ? 0.0916 0.2352 0.2180 -0.0201 -0.0007 -0.0291 426 TRP A CG  
3599 C CD1 . TRP A 426 ? 0.1510 0.2823 0.2748 -0.0247 0.0018  -0.0339 426 TRP A CD1 
3600 C CD2 . TRP A 426 ? 0.1170 0.2525 0.2409 -0.0125 0.0046  -0.0216 426 TRP A CD2 
3601 N NE1 . TRP A 426 ? 0.0974 0.2192 0.2207 -0.0200 0.0081  -0.0301 426 TRP A NE1 
3602 C CE2 . TRP A 426 ? 0.1150 0.2374 0.2356 -0.0133 0.0094  -0.0219 426 TRP A CE2 
3603 C CE3 . TRP A 426 ? 0.1223 0.2607 0.2467 -0.0053 0.0046  -0.0161 426 TRP A CE3 
3604 C CZ2 . TRP A 426 ? 0.1049 0.2180 0.2204 -0.0082 0.0133  -0.0161 426 TRP A CZ2 
3605 C CZ3 . TRP A 426 ? 0.1578 0.2853 0.2785 -0.0011 0.0094  -0.0114 426 TRP A CZ3 
3606 C CH2 . TRP A 426 ? 0.1412 0.2569 0.2562 -0.0032 0.0132  -0.0110 426 TRP A CH2 
3607 N N   . LYS A 427 ? 0.0980 0.2685 0.2035 -0.0197 -0.0279 -0.0359 427 LYS A N   
3608 C CA  . LYS A 427 ? 0.1479 0.3336 0.2512 -0.0170 -0.0388 -0.0355 427 LYS A CA  
3609 C C   . LYS A 427 ? 0.1596 0.3351 0.2437 -0.0067 -0.0387 -0.0312 427 LYS A C   
3610 O O   . LYS A 427 ? 0.1442 0.3290 0.2284 0.0020  -0.0445 -0.0262 427 LYS A O   
3611 C CB  . LYS A 427 ? 0.1949 0.3810 0.2912 -0.0276 -0.0478 -0.0432 427 LYS A CB  
3612 C CG  . LYS A 427 ? 0.3559 0.5500 0.4683 -0.0417 -0.0497 -0.0469 427 LYS A CG  
3613 C CD  . LYS A 427 ? 0.4787 0.6646 0.5781 -0.0536 -0.0594 -0.0555 427 LYS A CD  
3614 C CE  . LYS A 427 ? 0.5817 0.7829 0.6741 -0.0503 -0.0718 -0.0567 427 LYS A CE  
3615 N NZ  . LYS A 427 ? 0.6440 0.8353 0.7202 -0.0620 -0.0826 -0.0661 427 LYS A NZ  
3616 N N   . ILE A 428 ? 0.1332 0.2894 0.1993 -0.0072 -0.0322 -0.0327 428 ILE A N   
3617 C CA  . ILE A 428 ? 0.1660 0.3114 0.2117 -0.0008 -0.0299 -0.0275 428 ILE A CA  
3618 C C   . ILE A 428 ? 0.1402 0.2832 0.1915 0.0059  -0.0258 -0.0190 428 ILE A C   
3619 O O   . ILE A 428 ? 0.1586 0.2973 0.1980 0.0128  -0.0302 -0.0128 428 ILE A O   
3620 C CB  . ILE A 428 ? 0.1735 0.3049 0.2036 -0.0034 -0.0209 -0.0312 428 ILE A CB  
3621 C CG1 . ILE A 428 ? 0.1785 0.3070 0.1938 -0.0070 -0.0268 -0.0400 428 ILE A CG1 
3622 C CG2 . ILE A 428 ? 0.2148 0.3372 0.2276 0.0001  -0.0147 -0.0239 428 ILE A CG2 
3623 C CD1 . ILE A 428 ? 0.2496 0.3666 0.2540 -0.0076 -0.0176 -0.0467 428 ILE A CD1 
3624 N N   . LEU A 429 ? 0.1264 0.2690 0.1931 0.0043  -0.0180 -0.0189 429 LEU A N   
3625 C CA  . LEU A 429 ? 0.1064 0.2432 0.1760 0.0099  -0.0143 -0.0122 429 LEU A CA  
3626 C C   . LEU A 429 ? 0.1606 0.3083 0.2383 0.0187  -0.0223 -0.0093 429 LEU A C   
3627 O O   . LEU A 429 ? 0.1817 0.3189 0.2495 0.0271  -0.0242 -0.0033 429 LEU A O   
3628 C CB  . LEU A 429 ? 0.1424 0.2780 0.2262 0.0063  -0.0057 -0.0138 429 LEU A CB  
3629 C CG  . LEU A 429 ? 0.1795 0.3069 0.2650 0.0107  -0.0019 -0.0084 429 LEU A CG  
3630 C CD1 . LEU A 429 ? 0.1869 0.2983 0.2551 0.0080  0.0030  -0.0042 429 LEU A CD1 
3631 C CD2 . LEU A 429 ? 0.2285 0.3599 0.3304 0.0080  0.0037  -0.0111 429 LEU A CD2 
3632 N N   . ILE A 430 ? 0.0964 0.2656 0.1920 0.0170  -0.0273 -0.0137 430 ILE A N   
3633 C CA  . ILE A 430 ? 0.1128 0.3015 0.2205 0.0264  -0.0347 -0.0121 430 ILE A CA  
3634 C C   . ILE A 430 ? 0.1660 0.3521 0.2566 0.0358  -0.0452 -0.0088 430 ILE A C   
3635 O O   . ILE A 430 ? 0.1611 0.3447 0.2476 0.0495  -0.0493 -0.0041 430 ILE A O   
3636 C CB  . ILE A 430 ? 0.1232 0.3367 0.2523 0.0183  -0.0371 -0.0170 430 ILE A CB  
3637 C CG1 . ILE A 430 ? 0.1139 0.3164 0.2514 0.0113  -0.0259 -0.0164 430 ILE A CG1 
3638 C CG2 . ILE A 430 ? 0.1228 0.3508 0.2585 0.0263  -0.0441 -0.0150 430 ILE A CG2 
3639 C CD1 . ILE A 430 ? 0.1519 0.3580 0.2972 -0.0025 -0.0256 -0.0193 430 ILE A CD1 
3640 N N   . GLU A 431 ? 0.1314 0.3156 0.2088 0.0296  -0.0504 -0.0114 431 GLU A N   
3641 C CA  . GLU A 431 ? 0.1564 0.3362 0.2135 0.0381  -0.0610 -0.0078 431 GLU A CA  
3642 C C   . GLU A 431 ? 0.2055 0.3549 0.2374 0.0446  -0.0571 0.0006  431 GLU A C   
3643 O O   . GLU A 431 ? 0.2385 0.3805 0.2565 0.0571  -0.0655 0.0064  431 GLU A O   
3644 C CB  . GLU A 431 ? 0.2785 0.4588 0.3224 0.0291  -0.0660 -0.0129 431 GLU A CB  
3645 C CG  . GLU A 431 ? 0.3696 0.5781 0.4330 0.0224  -0.0749 -0.0204 431 GLU A CG  
3646 C CD  . GLU A 431 ? 0.4375 0.6744 0.5183 0.0332  -0.0858 -0.0186 431 GLU A CD  
3647 O OE1 . GLU A 431 ? 0.3982 0.6504 0.5043 0.0303  -0.0812 -0.0196 431 GLU A OE1 
3648 O OE2 . GLU A 431 ? 0.4024 0.6390 0.4679 0.0445  -0.0967 -0.0151 431 GLU A OE2 
3649 N N   . ALA A 432 ? 0.2129 0.3440 0.2372 0.0358  -0.0450 0.0016  432 ALA A N   
3650 C CA  . ALA A 432 ? 0.2285 0.3315 0.2281 0.0373  -0.0409 0.0099  432 ALA A CA  
3651 C C   . ALA A 432 ? 0.2344 0.3268 0.2376 0.0469  -0.0412 0.0148  432 ALA A C   
3652 O O   . ALA A 432 ? 0.2747 0.3426 0.2545 0.0536  -0.0449 0.0225  432 ALA A O   
3653 C CB  . ALA A 432 ? 0.1975 0.2914 0.1924 0.0245  -0.0278 0.0089  432 ALA A CB  
3654 N N   . LYS A 433 ? 0.1908 0.2981 0.2200 0.0478  -0.0374 0.0102  433 LYS A N   
3655 C CA  . LYS A 433 ? 0.2197 0.3172 0.2516 0.0582  -0.0371 0.0130  433 LYS A CA  
3656 C C   . LYS A 433 ? 0.2767 0.3746 0.3008 0.0764  -0.0494 0.0160  433 LYS A C   
3657 O O   . LYS A 433 ? 0.2779 0.3503 0.2852 0.0871  -0.0519 0.0211  433 LYS A O   
3658 C CB  . LYS A 433 ? 0.1972 0.3155 0.2578 0.0563  -0.0310 0.0070  433 LYS A CB  
3659 C CG  . LYS A 433 ? 0.2300 0.3438 0.2947 0.0698  -0.0313 0.0079  433 LYS A CG  
3660 C CD  . LYS A 433 ? 0.2391 0.3173 0.2844 0.0675  -0.0263 0.0123  433 LYS A CD  
3661 C CE  . LYS A 433 ? 0.2602 0.3250 0.3003 0.0838  -0.0291 0.0128  433 LYS A CE  
3662 N NZ  . LYS A 433 ? 0.3026 0.3290 0.3212 0.0783  -0.0256 0.0168  433 LYS A NZ  
3663 N N   . LYS A 434 ? 0.2749 0.4000 0.3089 0.0804  -0.0584 0.0127  434 LYS A N   
3664 C CA  . LYS A 434 ? 0.3057 0.4361 0.3336 0.0997  -0.0716 0.0152  434 LYS A CA  
3665 C C   . LYS A 434 ? 0.3496 0.4415 0.3388 0.1058  -0.0776 0.0241  434 LYS A C   
3666 O O   . LYS A 434 ? 0.3819 0.4624 0.3581 0.1250  -0.0875 0.0281  434 LYS A O   
3667 C CB  . LYS A 434 ? 0.3803 0.5491 0.4254 0.0996  -0.0813 0.0099  434 LYS A CB  
3668 C CG  . LYS A 434 ? 0.3511 0.5551 0.4316 0.0898  -0.0754 0.0021  434 LYS A CG  
3669 C CD  . LYS A 434 ? 0.4666 0.6956 0.5582 0.0838  -0.0832 -0.0020 434 LYS A CD  
3670 C CE  . LYS A 434 ? 0.4743 0.7238 0.5926 0.0676  -0.0752 -0.0077 434 LYS A CE  
3671 N NZ  . LYS A 434 ? 0.4800 0.7483 0.6046 0.0569  -0.0832 -0.0117 434 LYS A NZ  
3672 N N   . LYS A 435 ? 0.3434 0.4149 0.3122 0.0903  -0.0719 0.0275  435 LYS A N   
3673 C CA  . LYS A 435 ? 0.3885 0.4236 0.3178 0.0921  -0.0763 0.0372  435 LYS A CA  
3674 C C   . LYS A 435 ? 0.3972 0.3976 0.3081 0.0794  -0.0648 0.0432  435 LYS A C   
3675 O O   . LYS A 435 ? 0.4237 0.3950 0.3014 0.0738  -0.0649 0.0518  435 LYS A O   
3676 C CB  . LYS A 435 ? 0.4792 0.5220 0.3945 0.0848  -0.0804 0.0372  435 LYS A CB  
3677 C CG  . LYS A 435 ? 0.5271 0.6081 0.4630 0.0914  -0.0916 0.0296  435 LYS A CG  
3678 C CD  . LYS A 435 ? 0.6296 0.7137 0.5485 0.0816  -0.0945 0.0282  435 LYS A CD  
3679 C CE  . LYS A 435 ? 0.6710 0.7925 0.6096 0.0846  -0.1067 0.0198  435 LYS A CE  
3680 N NZ  . LYS A 435 ? 0.7109 0.8315 0.6289 0.0752  -0.1101 0.0172  435 LYS A NZ  
3681 N N   . ALA A 436 ? 0.2366 0.3821 0.3523 0.1345  -0.0483 0.0469  436 ALA A N   
3682 C CA  . ALA A 436 ? 0.2508 0.3546 0.3492 0.1322  -0.0434 0.0485  436 ALA A CA  
3683 C C   . ALA A 436 ? 0.3411 0.3963 0.4358 0.1520  -0.0440 0.0579  436 ALA A C   
3684 O O   . ALA A 436 ? 0.3130 0.3658 0.4224 0.1706  -0.0433 0.0548  436 ALA A O   
3685 C CB  . ALA A 436 ? 0.2400 0.3457 0.3417 0.1251  -0.0322 0.0304  436 ALA A CB  
3686 N N   . LYS A 437 ? 0.2916 0.3046 0.3678 0.1460  -0.0440 0.0701  437 LYS A N   
3687 C CA  . LYS A 437 ? 0.3729 0.3270 0.4435 0.1572  -0.0444 0.0814  437 LYS A CA  
3688 C C   . LYS A 437 ? 0.3680 0.2677 0.4323 0.1471  -0.0363 0.0735  437 LYS A C   
3689 O O   . LYS A 437 ? 0.4890 0.3324 0.5523 0.1532  -0.0366 0.0764  437 LYS A O   
3690 C CB  . LYS A 437 ? 0.4300 0.3732 0.4822 0.1533  -0.0514 0.1086  437 LYS A CB  
3691 C CG  . LYS A 437 ? 0.5722 0.5398 0.6285 0.1702  -0.0626 0.1179  437 LYS A CG  
3692 C CD  . LYS A 437 ? 0.6205 0.6505 0.6781 0.1616  -0.0679 0.1120  437 LYS A CD  
3693 C CE  . LYS A 437 ? 0.6618 0.7129 0.7138 0.1717  -0.0809 0.1260  437 LYS A CE  
3694 N NZ  . LYS A 437 ? 0.6517 0.7541 0.7008 0.1567  -0.0861 0.1168  437 LYS A NZ  
3695 N N   . ASN A 438 ? 0.3269 0.2433 0.3884 0.1214  -0.0320 0.0576  438 ASN A N   
3696 C CA  . ASN A 438 ? 0.3163 0.1912 0.3739 0.1004  -0.0285 0.0466  438 ASN A CA  
3697 C C   . ASN A 438 ? 0.3200 0.2258 0.3772 0.0853  -0.0255 0.0232  438 ASN A C   
3698 O O   . ASN A 438 ? 0.2889 0.2427 0.3487 0.0887  -0.0244 0.0188  438 ASN A O   
3699 C CB  . ASN A 438 ? 0.3325 0.1882 0.3840 0.0793  -0.0275 0.0699  438 ASN A CB  
3700 C CG  . ASN A 438 ? 0.2860 0.1924 0.3302 0.0668  -0.0265 0.0794  438 ASN A CG  
3701 O OD1 . ASN A 438 ? 0.2678 0.2033 0.3138 0.0536  -0.0248 0.0631  438 ASN A OD1 
3702 N ND2 . ASN A 438 ? 0.3179 0.2326 0.3510 0.0728  -0.0281 0.1056  438 ASN A ND2 
3703 N N   . ASP A 439 ? 0.3451 0.2234 0.4002 0.0669  -0.0254 0.0099  439 ASP A N   
3704 C CA  . ASP A 439 ? 0.2947 0.1964 0.3460 0.0558  -0.0246 -0.0116 439 ASP A CA  
3705 C C   . ASP A 439 ? 0.2407 0.1816 0.2921 0.0375  -0.0236 -0.0040 439 ASP A C   
3706 O O   . ASP A 439 ? 0.2104 0.1698 0.2582 0.0295  -0.0235 -0.0176 439 ASP A O   
3707 C CB  . ASP A 439 ? 0.3518 0.2136 0.4008 0.0436  -0.0289 -0.0302 439 ASP A CB  
3708 C CG  . ASP A 439 ? 0.4585 0.2878 0.5003 0.0648  -0.0294 -0.0515 439 ASP A CG  
3709 O OD1 . ASP A 439 ? 0.4636 0.3071 0.5053 0.0907  -0.0241 -0.0506 439 ASP A OD1 
3710 O OD2 . ASP A 439 ? 0.5264 0.3177 0.5638 0.0563  -0.0353 -0.0710 439 ASP A OD2 
3711 N N   . TYR A 440 ? 0.2288 0.1822 0.2812 0.0330  -0.0228 0.0170  440 TYR A N   
3712 C CA  . TYR A 440 ? 0.1584 0.1491 0.2088 0.0212  -0.0212 0.0189  440 TYR A CA  
3713 C C   . TYR A 440 ? 0.1585 0.1832 0.2086 0.0296  -0.0210 0.0101  440 TYR A C   
3714 O O   . TYR A 440 ? 0.1551 0.2023 0.2037 0.0197  -0.0200 0.0063  440 TYR A O   
3715 C CB  . TYR A 440 ? 0.1901 0.1889 0.2356 0.0171  -0.0195 0.0402  440 TYR A CB  
3716 C CG  . TYR A 440 ? 0.2076 0.1919 0.2572 -0.0011 -0.0150 0.0483  440 TYR A CG  
3717 C CD1 . TYR A 440 ? 0.2182 0.2207 0.2740 -0.0155 -0.0129 0.0391  440 TYR A CD1 
3718 C CD2 . TYR A 440 ? 0.2935 0.2462 0.3446 -0.0040 -0.0125 0.0667  440 TYR A CD2 
3719 C CE1 . TYR A 440 ? 0.2289 0.2278 0.2962 -0.0325 -0.0081 0.0468  440 TYR A CE1 
3720 C CE2 . TYR A 440 ? 0.2604 0.2051 0.3218 -0.0246 -0.0063 0.0761  440 TYR A CE2 
3721 C CZ  . TYR A 440 ? 0.3185 0.2902 0.3900 -0.0387 -0.0042 0.0651  440 TYR A CZ  
3722 O OH  . TYR A 440 ? 0.3708 0.3439 0.4597 -0.0589 0.0026  0.0748  440 TYR A OH  
3723 N N   . ILE A 441 ? 0.1625 0.1921 0.2169 0.0479  -0.0211 0.0078  441 ILE A N   
3724 C CA  . ILE A 441 ? 0.1386 0.2045 0.1987 0.0521  -0.0185 0.0003  441 ILE A CA  
3725 C C   . ILE A 441 ? 0.1850 0.2494 0.2385 0.0451  -0.0140 -0.0146 441 ILE A C   
3726 O O   . ILE A 441 ? 0.1406 0.2305 0.1948 0.0386  -0.0108 -0.0165 441 ILE A O   
3727 C CB  . ILE A 441 ? 0.1888 0.2680 0.2608 0.0747  -0.0179 0.0012  441 ILE A CB  
3728 C CG1 . ILE A 441 ? 0.1519 0.2800 0.2383 0.0742  -0.0155 -0.0004 441 ILE A CG1 
3729 C CG2 . ILE A 441 ? 0.1793 0.2316 0.2483 0.0898  -0.0129 -0.0123 441 ILE A CG2 
3730 C CD1 . ILE A 441 ? 0.2237 0.3728 0.3125 0.0620  -0.0234 0.0091  441 ILE A CD1 
3731 N N   . LEU A 442 ? 0.1675 0.2002 0.2129 0.0458  -0.0148 -0.0248 442 LEU A N   
3732 C CA  . LEU A 442 ? 0.1703 0.2030 0.2037 0.0401  -0.0138 -0.0391 442 LEU A CA  
3733 C C   . LEU A 442 ? 0.1471 0.1886 0.1794 0.0219  -0.0173 -0.0349 442 LEU A C   
3734 O O   . LEU A 442 ? 0.1316 0.1884 0.1557 0.0187  -0.0157 -0.0386 442 LEU A O   
3735 C CB  . LEU A 442 ? 0.1741 0.1700 0.1986 0.0440  -0.0178 -0.0549 442 LEU A CB  
3736 C CG  . LEU A 442 ? 0.2086 0.1860 0.2322 0.0663  -0.0141 -0.0635 442 LEU A CG  
3737 C CD1 . LEU A 442 ? 0.2550 0.1879 0.2666 0.0675  -0.0200 -0.0845 442 LEU A CD1 
3738 C CD2 . LEU A 442 ? 0.1999 0.2148 0.2213 0.0822  -0.0031 -0.0672 442 LEU A CD2 
3739 N N   . VAL A 443 ? 0.1453 0.1769 0.1850 0.0115  -0.0209 -0.0259 443 VAL A N   
3740 C CA  . VAL A 443 ? 0.1313 0.1758 0.1736 -0.0018 -0.0225 -0.0222 443 VAL A CA  
3741 C C   . VAL A 443 ? 0.1381 0.2071 0.1787 -0.0010 -0.0189 -0.0177 443 VAL A C   
3742 O O   . VAL A 443 ? 0.1370 0.2146 0.1746 -0.0056 -0.0195 -0.0196 443 VAL A O   
3743 C CB  . VAL A 443 ? 0.1427 0.1799 0.1943 -0.0110 -0.0223 -0.0109 443 VAL A CB  
3744 C CG1 . VAL A 443 ? 0.1213 0.1771 0.1787 -0.0211 -0.0219 -0.0089 443 VAL A CG1 
3745 C CG2 . VAL A 443 ? 0.1257 0.1321 0.1834 -0.0156 -0.0255 -0.0127 443 VAL A CG2 
3746 N N   . ALA A 444 ? 0.0976 0.1770 0.1416 0.0046  -0.0169 -0.0115 444 ALA A N   
3747 C CA  . ALA A 444 ? 0.1074 0.2077 0.1537 0.0017  -0.0157 -0.0091 444 ALA A CA  
3748 C C   . ALA A 444 ? 0.1336 0.2447 0.1795 0.0026  -0.0112 -0.0129 444 ALA A C   
3749 O O   . ALA A 444 ? 0.1330 0.2502 0.1801 -0.0039 -0.0093 -0.0101 444 ALA A O   
3750 C CB  . ALA A 444 ? 0.1346 0.2478 0.1868 0.0070  -0.0183 -0.0030 444 ALA A CB  
3751 N N   . GLU A 445 ? 0.0969 0.2034 0.1373 0.0106  -0.0080 -0.0186 445 GLU A N   
3752 C CA  . GLU A 445 ? 0.0896 0.2087 0.1239 0.0125  -0.0007 -0.0201 445 GLU A CA  
3753 C C   . GLU A 445 ? 0.1264 0.2372 0.1451 0.0070  -0.0024 -0.0205 445 GLU A C   
3754 O O   . GLU A 445 ? 0.1461 0.2658 0.1544 0.0082  0.0042  -0.0176 445 GLU A O   
3755 C CB  . GLU A 445 ? 0.1223 0.2423 0.1517 0.0277  0.0049  -0.0284 445 GLU A CB  
3756 C CG  . GLU A 445 ? 0.1339 0.2743 0.1837 0.0370  0.0086  -0.0247 445 GLU A CG  
3757 C CD  . GLU A 445 ? 0.1629 0.2946 0.2117 0.0570  0.0115  -0.0338 445 GLU A CD  
3758 O OE1 . GLU A 445 ? 0.2102 0.3195 0.2396 0.0630  0.0120  -0.0463 445 GLU A OE1 
3759 O OE2 . GLU A 445 ? 0.1568 0.3052 0.2248 0.0687  0.0123  -0.0295 445 GLU A OE2 
3760 N N   . GLY A 446 ? 0.1484 0.2463 0.1663 0.0017  -0.0106 -0.0218 446 GLY A N   
3761 C CA  . GLY A 446 ? 0.1193 0.2143 0.1254 0.0000  -0.0149 -0.0218 446 GLY A CA  
3762 C C   . GLY A 446 ? 0.1523 0.2518 0.1581 -0.0038 -0.0109 -0.0109 446 GLY A C   
3763 O O   . GLY A 446 ? 0.1372 0.2379 0.1557 -0.0092 -0.0086 -0.0068 446 GLY A O   
3764 N N   . SER A 447 ? 0.1289 0.2281 0.1176 -0.0006 -0.0112 -0.0063 447 SER A N   
3765 C CA  . SER A 447 ? 0.1372 0.2337 0.1235 -0.0039 -0.0056 0.0076  447 SER A CA  
3766 C C   . SER A 447 ? 0.1321 0.2164 0.1310 -0.0071 -0.0107 0.0102  447 SER A C   
3767 O O   . SER A 447 ? 0.1445 0.2192 0.1491 -0.0129 -0.0062 0.0179  447 SER A O   
3768 C CB  . SER A 447 ? 0.1543 0.2511 0.1145 0.0027  -0.0052 0.0159  447 SER A CB  
3769 O OG  . SER A 447 ? 0.1671 0.2612 0.1206 0.0087  -0.0191 0.0117  447 SER A OG  
3770 N N   . ASP A 448 ? 0.1089 0.1938 0.1136 -0.0037 -0.0192 0.0031  448 ASP A N   
3771 C CA  . ASP A 448 ? 0.1009 0.1783 0.1155 -0.0016 -0.0222 0.0047  448 ASP A CA  
3772 C C   . ASP A 448 ? 0.0816 0.1513 0.1061 -0.0079 -0.0171 0.0020  448 ASP A C   
3773 O O   . ASP A 448 ? 0.1207 0.1747 0.1471 -0.0065 -0.0166 0.0038  448 ASP A O   
3774 C CB  . ASP A 448 ? 0.1029 0.1927 0.1286 0.0015  -0.0291 -0.0025 448 ASP A CB  
3775 C CG  . ASP A 448 ? 0.1207 0.2205 0.1385 0.0048  -0.0384 -0.0045 448 ASP A CG  
3776 O OD1 . ASP A 448 ? 0.1605 0.2591 0.1710 0.0010  -0.0384 -0.0113 448 ASP A OD1 
3777 O OD2 . ASP A 448 ? 0.1676 0.2732 0.1848 0.0128  -0.0464 0.0000  448 ASP A OD2 
3778 N N   . TRP A 449 ? 0.0874 0.1661 0.1170 -0.0133 -0.0150 -0.0036 449 TRP A N   
3779 C CA  . TRP A 449 ? 0.1155 0.1914 0.1513 -0.0186 -0.0140 -0.0085 449 TRP A CA  
3780 C C   . TRP A 449 ? 0.1148 0.1793 0.1529 -0.0267 -0.0118 -0.0048 449 TRP A C   
3781 O O   . TRP A 449 ? 0.1366 0.1856 0.1769 -0.0300 -0.0135 -0.0102 449 TRP A O   
3782 C CB  . TRP A 449 ? 0.1257 0.2152 0.1646 -0.0204 -0.0142 -0.0115 449 TRP A CB  
3783 C CG  . TRP A 449 ? 0.0974 0.1845 0.1326 -0.0146 -0.0140 -0.0107 449 TRP A CG  
3784 C CD1 . TRP A 449 ? 0.1131 0.2025 0.1473 -0.0125 -0.0136 -0.0105 449 TRP A CD1 
3785 C CD2 . TRP A 449 ? 0.0949 0.1813 0.1319 -0.0125 -0.0145 -0.0114 449 TRP A CD2 
3786 N NE1 . TRP A 449 ? 0.1212 0.2072 0.1572 -0.0118 -0.0159 -0.0117 449 TRP A NE1 
3787 C CE2 . TRP A 449 ? 0.0762 0.1612 0.1150 -0.0128 -0.0156 -0.0106 449 TRP A CE2 
3788 C CE3 . TRP A 449 ? 0.1133 0.2061 0.1550 -0.0107 -0.0140 -0.0138 449 TRP A CE3 
3789 C CZ2 . TRP A 449 ? 0.0976 0.1858 0.1450 -0.0149 -0.0164 -0.0098 449 TRP A CZ2 
3790 C CZ3 . TRP A 449 ? 0.1063 0.2062 0.1552 -0.0096 -0.0122 -0.0122 449 TRP A CZ3 
3791 C CH2 . TRP A 449 ? 0.1124 0.2090 0.1651 -0.0136 -0.0136 -0.0092 449 TRP A CH2 
3792 N N   . PHE A 450 ? 0.1103 0.1814 0.1481 -0.0306 -0.0070 0.0039  450 PHE A N   
3793 C CA  . PHE A 450 ? 0.1224 0.1861 0.1672 -0.0424 -0.0024 0.0113  450 PHE A CA  
3794 C C   . PHE A 450 ? 0.1219 0.1557 0.1590 -0.0409 -0.0018 0.0203  450 PHE A C   
3795 O O   . PHE A 450 ? 0.1864 0.1995 0.2318 -0.0521 -0.0008 0.0229  450 PHE A O   
3796 C CB  . PHE A 450 ? 0.1323 0.2184 0.1791 -0.0450 0.0065  0.0201  450 PHE A CB  
3797 C CG  . PHE A 450 ? 0.1447 0.2576 0.2008 -0.0416 0.0057  0.0118  450 PHE A CG  
3798 C CD1 . PHE A 450 ? 0.1079 0.2342 0.1827 -0.0491 0.0045  0.0086  450 PHE A CD1 
3799 C CD2 . PHE A 450 ? 0.1317 0.2495 0.1765 -0.0287 0.0043  0.0069  450 PHE A CD2 
3800 C CE1 . PHE A 450 ? 0.1630 0.3008 0.2402 -0.0387 0.0022  0.0032  450 PHE A CE1 
3801 C CE2 . PHE A 450 ? 0.1766 0.3105 0.2294 -0.0229 0.0032  0.0009  450 PHE A CE2 
3802 C CZ  . PHE A 450 ? 0.1149 0.2538 0.1805 -0.0259 0.0022  0.0005  450 PHE A CZ  
3803 N N   . TRP A 451 ? 0.1466 0.1768 0.1697 -0.0270 -0.0042 0.0250  451 TRP A N   
3804 C CA  . TRP A 451 ? 0.1534 0.1568 0.1684 -0.0197 -0.0058 0.0359  451 TRP A CA  
3805 C C   . TRP A 451 ? 0.1655 0.1438 0.1892 -0.0173 -0.0097 0.0255  451 TRP A C   
3806 O O   . TRP A 451 ? 0.2004 0.1447 0.2246 -0.0197 -0.0086 0.0323  451 TRP A O   
3807 C CB  . TRP A 451 ? 0.1502 0.1657 0.1521 -0.0035 -0.0119 0.0392  451 TRP A CB  
3808 C CG  . TRP A 451 ? 0.1794 0.1750 0.1743 0.0108  -0.0173 0.0505  451 TRP A CG  
3809 C CD1 . TRP A 451 ? 0.2148 0.2098 0.2189 0.0251  -0.0246 0.0434  451 TRP A CD1 
3810 C CD2 . TRP A 451 ? 0.2363 0.2137 0.2140 0.0150  -0.0154 0.0730  451 TRP A CD2 
3811 N NE1 . TRP A 451 ? 0.2440 0.2213 0.2400 0.0399  -0.0292 0.0591  451 TRP A NE1 
3812 C CE2 . TRP A 451 ? 0.2787 0.2423 0.2558 0.0339  -0.0243 0.0787  451 TRP A CE2 
3813 C CE3 . TRP A 451 ? 0.2405 0.2148 0.2030 0.0059  -0.0057 0.0912  451 TRP A CE3 
3814 C CZ2 . TRP A 451 ? 0.2848 0.2262 0.2445 0.0446  -0.0260 0.1030  451 TRP A CZ2 
3815 C CZ3 . TRP A 451 ? 0.2863 0.2390 0.2296 0.0140  -0.0050 0.1163  451 TRP A CZ3 
3816 C CH2 . TRP A 451 ? 0.3148 0.2490 0.2554 0.0338  -0.0163 0.1227  451 TRP A CH2 
3817 N N   . TRP A 452 ? 0.1500 0.1423 0.1786 -0.0117 -0.0133 0.0091  452 TRP A N   
3818 C CA  . TRP A 452 ? 0.1710 0.1435 0.2027 -0.0049 -0.0152 -0.0037 452 TRP A CA  
3819 C C   . TRP A 452 ? 0.1810 0.1388 0.2165 -0.0197 -0.0157 -0.0162 452 TRP A C   
3820 O O   . TRP A 452 ? 0.2032 0.1327 0.2372 -0.0155 -0.0174 -0.0280 452 TRP A O   
3821 C CB  . TRP A 452 ? 0.1514 0.1493 0.1856 0.0067  -0.0159 -0.0144 452 TRP A CB  
3822 C CG  . TRP A 452 ? 0.1373 0.1508 0.1743 0.0198  -0.0185 -0.0052 452 TRP A CG  
3823 C CD1 . TRP A 452 ? 0.1264 0.1688 0.1656 0.0180  -0.0209 -0.0025 452 TRP A CD1 
3824 C CD2 . TRP A 452 ? 0.1543 0.1548 0.1930 0.0364  -0.0217 0.0022  452 TRP A CD2 
3825 N NE1 . TRP A 452 ? 0.1110 0.1632 0.1537 0.0302  -0.0269 0.0043  452 TRP A NE1 
3826 C CE2 . TRP A 452 ? 0.1553 0.1848 0.1980 0.0431  -0.0276 0.0088  452 TRP A CE2 
3827 C CE3 . TRP A 452 ? 0.1967 0.1611 0.2344 0.0473  -0.0214 0.0036  452 TRP A CE3 
3828 C CZ2 . TRP A 452 ? 0.2041 0.2363 0.2510 0.0613  -0.0345 0.0177  452 TRP A CZ2 
3829 C CZ3 . TRP A 452 ? 0.2772 0.2386 0.3183 0.0678  -0.0263 0.0141  452 TRP A CZ3 
3830 C CH2 . TRP A 452 ? 0.2393 0.2382 0.2854 0.0751  -0.0335 0.0218  452 TRP A CH2 
3831 N N   . GLN A 453 ? 0.1817 0.1587 0.2229 -0.0355 -0.0155 -0.0156 453 GLN A N   
3832 C CA  . GLN A 453 ? 0.1975 0.1705 0.2453 -0.0505 -0.0201 -0.0296 453 GLN A CA  
3833 C C   . GLN A 453 ? 0.2415 0.1778 0.2979 -0.0651 -0.0201 -0.0260 453 GLN A C   
3834 O O   . GLN A 453 ? 0.2860 0.2135 0.3463 -0.0703 -0.0138 -0.0056 453 GLN A O   
3835 C CB  . GLN A 453 ? 0.2216 0.2332 0.2781 -0.0601 -0.0210 -0.0281 453 GLN A CB  
3836 C CG  . GLN A 453 ? 0.2203 0.2395 0.2907 -0.0787 -0.0282 -0.0385 453 GLN A CG  
3837 C CD  . GLN A 453 ? 0.2966 0.3131 0.3554 -0.0758 -0.0381 -0.0610 453 GLN A CD  
3838 O OE1 . GLN A 453 ? 0.2625 0.2675 0.3034 -0.0600 -0.0364 -0.0684 453 GLN A OE1 
3839 N NE2 . GLN A 453 ? 0.2883 0.3142 0.3502 -0.0839 -0.0474 -0.0637 453 GLN A NE2 
3840 N N   . GLY A 454 ? 0.3677 0.2792 0.4245 -0.0716 -0.0271 -0.0457 454 GLY A N   
3841 C CA  . GLY A 454 ? 0.5048 0.3794 0.5751 -0.0921 -0.0288 -0.0440 454 GLY A CA  
3842 C C   . GLY A 454 ? 0.6290 0.4551 0.6942 -0.0831 -0.0231 -0.0287 454 GLY A C   
3843 O O   . GLY A 454 ? 0.6917 0.4965 0.7681 -0.0992 -0.0181 -0.0091 454 GLY A O   
3844 N N   . GLU A 455 ? 0.6429 0.4551 0.6928 -0.0564 -0.0229 -0.0343 455 GLU A N   
3845 C CA  . GLU A 455 ? 0.6833 0.4481 0.7279 -0.0406 -0.0204 -0.0229 455 GLU A CA  
3846 C C   . GLU A 455 ? 0.6906 0.4170 0.7285 -0.0275 -0.0252 -0.0510 455 GLU A C   
3847 O O   . GLU A 455 ? 0.5759 0.3207 0.6081 -0.0286 -0.0295 -0.0777 455 GLU A O   
3848 C CB  . GLU A 455 ? 0.6171 0.4079 0.6532 -0.0162 -0.0168 -0.0050 455 GLU A CB  
3849 C CG  . GLU A 455 ? 0.5953 0.4267 0.6313 -0.0259 -0.0126 0.0161  455 GLU A CG  
3850 C CD  . GLU A 455 ? 0.6551 0.4603 0.6891 -0.0345 -0.0070 0.0452  455 GLU A CD  
3851 O OE1 . GLU A 455 ? 0.6006 0.3563 0.6311 -0.0253 -0.0078 0.0545  455 GLU A OE1 
3852 O OE2 . GLU A 455 ? 0.5614 0.3948 0.5965 -0.0488 -0.0006 0.0598  455 GLU A OE2 
3853 N N   . GLU A 456 ? 0.7951 0.4677 0.8304 -0.0125 -0.0241 -0.0445 456 GLU A N   
3854 C CA  . GLU A 456 ? 0.8773 0.5238 0.8993 0.0076  -0.0226 -0.0692 456 GLU A CA  
3855 C C   . GLU A 456 ? 0.8501 0.5403 0.8678 0.0322  -0.0223 -0.0862 456 GLU A C   
3856 O O   . GLU A 456 ? 0.7667 0.4996 0.7890 0.0436  -0.0198 -0.0694 456 GLU A O   
3857 C CB  . GLU A 456 ? 0.9975 0.5945 1.0159 0.0270  -0.0170 -0.0528 456 GLU A CB  
3858 C CG  . GLU A 456 ? 1.0409 0.6561 1.0639 0.0517  -0.0168 -0.0248 456 GLU A CG  
3859 C CD  . GLU A 456 ? 1.0684 0.7174 1.0932 0.0857  -0.0157 -0.0383 456 GLU A CD  
3860 O OE1 . GLU A 456 ? 1.1138 0.7508 1.1340 0.0977  -0.0103 -0.0628 456 GLU A OE1 
3861 O OE2 . GLU A 456 ? 1.0330 0.7247 1.0637 0.0990  -0.0193 -0.0242 456 GLU A OE2 
3862 N N   . LYS A 457 ? 0.8598 0.5524 0.8628 0.0366  -0.0204 -0.1148 457 LYS A N   
3863 C CA  . LYS A 457 ? 0.7931 0.5329 0.7887 0.0564  -0.0157 -0.1289 457 LYS A CA  
3864 C C   . LYS A 457 ? 0.8007 0.5504 0.8049 0.0896  -0.0080 -0.1184 457 LYS A C   
3865 O O   . LYS A 457 ? 0.8637 0.5751 0.8703 0.1041  -0.0046 -0.1134 457 LYS A O   
3866 C CB  . LYS A 457 ? 0.8132 0.5486 0.7862 0.0555  -0.0134 -0.1572 457 LYS A CB  
3867 C CG  . LYS A 457 ? 0.8337 0.6202 0.7956 0.0724  -0.0054 -0.1671 457 LYS A CG  
3868 C CD  . LYS A 457 ? 0.9665 0.7383 0.9036 0.0799  -0.0003 -0.1923 457 LYS A CD  
3869 C CE  . LYS A 457 ? 0.9893 0.8147 0.9113 0.0897  0.0082  -0.1980 457 LYS A CE  
3870 N NZ  . LYS A 457 ? 0.9418 0.8180 0.8813 0.0915  0.0113  -0.1769 457 LYS A NZ  
3871 N N   . ALA A 458 ? 0.6849 0.4906 0.6963 0.1007  -0.0047 -0.1137 458 ALA A N   
3872 C CA  . ALA A 458 ? 0.6217 0.4536 0.6488 0.1272  0.0007  -0.0993 458 ALA A CA  
3873 C C   . ALA A 458 ? 0.4623 0.3571 0.4924 0.1344  0.0105  -0.1058 458 ALA A C   
3874 O O   . ALA A 458 ? 0.4182 0.3382 0.4386 0.1188  0.0109  -0.1134 458 ALA A O   
3875 C CB  . ALA A 458 ? 0.5985 0.4399 0.6384 0.1224  -0.0067 -0.0690 458 ALA A CB  
3876 N N   . PRO A 459 ? 0.4516 0.3745 0.4974 0.1555  0.0190  -0.1004 459 PRO A N   
3877 C CA  . PRO A 459 ? 0.4292 0.4116 0.4815 0.1569  0.0303  -0.1019 459 PRO A CA  
3878 C C   . PRO A 459 ? 0.3960 0.4207 0.4577 0.1398  0.0261  -0.0881 459 PRO A C   
3879 O O   . PRO A 459 ? 0.3439 0.3703 0.4184 0.1362  0.0156  -0.0728 459 PRO A O   
3880 C CB  . PRO A 459 ? 0.4785 0.4821 0.5565 0.1793  0.0368  -0.0941 459 PRO A CB  
3881 C CG  . PRO A 459 ? 0.6055 0.5645 0.6899 0.1910  0.0271  -0.0853 459 PRO A CG  
3882 C CD  . PRO A 459 ? 0.5796 0.4784 0.6385 0.1773  0.0201  -0.0938 459 PRO A CD  
3883 N N   . PHE A 460 ? 0.3175 0.3727 0.3691 0.1285  0.0342  -0.0930 460 PHE A N   
3884 C CA  . PHE A 460 ? 0.2862 0.3812 0.3468 0.1108  0.0336  -0.0796 460 PHE A CA  
3885 C C   . PHE A 460 ? 0.3048 0.3810 0.3560 0.0897  0.0215  -0.0743 460 PHE A C   
3886 O O   . PHE A 460 ? 0.3397 0.4396 0.3931 0.0729  0.0207  -0.0638 460 PHE A O   
3887 C CB  . PHE A 460 ? 0.2765 0.4063 0.3695 0.1125  0.0325  -0.0614 460 PHE A CB  
3888 C CG  . PHE A 460 ? 0.3197 0.4727 0.4278 0.1259  0.0444  -0.0618 460 PHE A CG  
3889 C CD1 . PHE A 460 ? 0.3787 0.5489 0.4758 0.1245  0.0593  -0.0677 460 PHE A CD1 
3890 C CD2 . PHE A 460 ? 0.2897 0.4490 0.4229 0.1410  0.0407  -0.0556 460 PHE A CD2 
3891 C CE1 . PHE A 460 ? 0.3923 0.5871 0.5056 0.1378  0.0723  -0.0688 460 PHE A CE1 
3892 C CE2 . PHE A 460 ? 0.3536 0.5388 0.5060 0.1547  0.0523  -0.0575 460 PHE A CE2 
3893 C CZ  . PHE A 460 ? 0.3815 0.5852 0.5250 0.1530  0.0691  -0.0647 460 PHE A CZ  
3894 N N   . VAL A 461 ? 0.3285 0.3583 0.3684 0.0861  0.0127  -0.0784 461 VAL A N   
3895 C CA  . VAL A 461 ? 0.4004 0.4193 0.4356 0.0630  0.0034  -0.0678 461 VAL A CA  
3896 C C   . VAL A 461 ? 0.3170 0.3440 0.3357 0.0472  0.0034  -0.0757 461 VAL A C   
3897 O O   . VAL A 461 ? 0.3570 0.3928 0.3769 0.0309  -0.0016 -0.0655 461 VAL A O   
3898 C CB  . VAL A 461 ? 0.5615 0.5335 0.5942 0.0602  -0.0041 -0.0646 461 VAL A CB  
3899 C CG1 . VAL A 461 ? 0.6218 0.5874 0.6678 0.0795  -0.0057 -0.0524 461 VAL A CG1 
3900 C CG2 . VAL A 461 ? 0.6445 0.5774 0.6626 0.0596  -0.0048 -0.0857 461 VAL A CG2 
3901 N N   . GLU A 462 ? 0.2670 0.2951 0.2687 0.0544  0.0088  -0.0937 462 GLU A N   
3902 C CA  . GLU A 462 ? 0.3018 0.3449 0.2846 0.0427  0.0073  -0.0986 462 GLU A CA  
3903 C C   . GLU A 462 ? 0.3196 0.4018 0.3088 0.0382  0.0132  -0.0811 462 GLU A C   
3904 O O   . GLU A 462 ? 0.2994 0.3924 0.2765 0.0278  0.0097  -0.0774 462 GLU A O   
3905 C CB  . GLU A 462 ? 0.4732 0.5122 0.4295 0.0544  0.0120  -0.1223 462 GLU A CB  
3906 C CG  . GLU A 462 ? 0.6891 0.6901 0.6306 0.0448  -0.0002 -0.1395 462 GLU A CG  
3907 C CD  . GLU A 462 ? 0.8748 0.8572 0.7959 0.0579  0.0053  -0.1565 462 GLU A CD  
3908 O OE1 . GLU A 462 ? 0.9262 0.9342 0.8291 0.0650  0.0139  -0.1568 462 GLU A OE1 
3909 O OE2 . GLU A 462 ? 0.9654 0.9053 0.8879 0.0608  0.0018  -0.1687 462 GLU A OE2 
3910 N N   . VAL A 463 ? 0.1746 0.2783 0.1844 0.0456  0.0210  -0.0700 463 VAL A N   
3911 C CA  . VAL A 463 ? 0.1245 0.2582 0.1447 0.0366  0.0252  -0.0531 463 VAL A CA  
3912 C C   . VAL A 463 ? 0.1285 0.2522 0.1550 0.0214  0.0140  -0.0424 463 VAL A C   
3913 O O   . VAL A 463 ? 0.1454 0.2792 0.1700 0.0121  0.0139  -0.0325 463 VAL A O   
3914 C CB  . VAL A 463 ? 0.1120 0.2743 0.1599 0.0448  0.0340  -0.0457 463 VAL A CB  
3915 C CG1 . VAL A 463 ? 0.2176 0.3978 0.2779 0.0295  0.0355  -0.0278 463 VAL A CG1 
3916 C CG2 . VAL A 463 ? 0.1890 0.3577 0.2297 0.0598  0.0462  -0.0536 463 VAL A CG2 
3917 N N   . PHE A 464 ? 0.1253 0.2286 0.1589 0.0205  0.0057  -0.0427 464 PHE A N   
3918 C CA  . PHE A 464 ? 0.1198 0.2168 0.1565 0.0087  -0.0022 -0.0339 464 PHE A CA  
3919 C C   . PHE A 464 ? 0.1305 0.2235 0.1540 -0.0002 -0.0058 -0.0366 464 PHE A C   
3920 O O   . PHE A 464 ? 0.1242 0.2241 0.1501 -0.0068 -0.0083 -0.0287 464 PHE A O   
3921 C CB  . PHE A 464 ? 0.1162 0.1934 0.1571 0.0104  -0.0077 -0.0317 464 PHE A CB  
3922 C CG  . PHE A 464 ? 0.1052 0.1927 0.1598 0.0193  -0.0089 -0.0255 464 PHE A CG  
3923 C CD1 . PHE A 464 ? 0.0859 0.1866 0.1473 0.0140  -0.0140 -0.0177 464 PHE A CD1 
3924 C CD2 . PHE A 464 ? 0.1112 0.1965 0.1724 0.0347  -0.0065 -0.0293 464 PHE A CD2 
3925 C CE1 . PHE A 464 ? 0.0964 0.2124 0.1717 0.0216  -0.0192 -0.0137 464 PHE A CE1 
3926 C CE2 . PHE A 464 ? 0.1289 0.2317 0.2072 0.0451  -0.0103 -0.0228 464 PHE A CE2 
3927 C CZ  . PHE A 464 ? 0.1016 0.2216 0.1870 0.0371  -0.0179 -0.0149 464 PHE A CZ  
3928 N N   . ASP A 465 ? 0.1485 0.2306 0.1592 0.0007  -0.0075 -0.0493 465 ASP A N   
3929 C CA  . ASP A 465 ? 0.1354 0.2206 0.1359 -0.0076 -0.0145 -0.0537 465 ASP A CA  
3930 C C   . ASP A 465 ? 0.1444 0.2517 0.1331 -0.0049 -0.0119 -0.0473 465 ASP A C   
3931 O O   . ASP A 465 ? 0.1552 0.2716 0.1441 -0.0096 -0.0176 -0.0400 465 ASP A O   
3932 C CB  . ASP A 465 ? 0.1632 0.2303 0.1519 -0.0084 -0.0196 -0.0730 465 ASP A CB  
3933 C CG  . ASP A 465 ? 0.1698 0.2468 0.1488 -0.0171 -0.0303 -0.0797 465 ASP A CG  
3934 O OD1 . ASP A 465 ? 0.1839 0.2597 0.1784 -0.0282 -0.0363 -0.0723 465 ASP A OD1 
3935 O OD2 . ASP A 465 ? 0.1939 0.2777 0.1521 -0.0103 -0.0296 -0.0851 465 ASP A OD2 
3936 N N   . LYS A 466 ? 0.1260 0.2433 0.1061 0.0038  -0.0017 -0.0472 466 LYS A N   
3937 C CA  . LYS A 466 ? 0.1407 0.2771 0.1086 0.0053  0.0038  -0.0354 466 LYS A CA  
3938 C C   . LYS A 466 ? 0.1145 0.2529 0.1002 -0.0010 0.0040  -0.0171 466 LYS A C   
3939 O O   . LYS A 466 ? 0.1672 0.3093 0.1452 -0.0024 0.0012  -0.0060 466 LYS A O   
3940 C CB  . LYS A 466 ? 0.1733 0.3248 0.1328 0.0149  0.0190  -0.0363 466 LYS A CB  
3941 C CG  . LYS A 466 ? 0.1664 0.3368 0.1161 0.0140  0.0285  -0.0172 466 LYS A CG  
3942 C CD  . LYS A 466 ? 0.2818 0.4631 0.2281 0.0217  0.0433  -0.0159 466 LYS A CD  
3943 C CE  . LYS A 466 ? 0.4810 0.6710 0.4121 0.0197  0.0507  0.0037  466 LYS A CE  
3944 N NZ  . LYS A 466 ? 0.6318 0.8304 0.5405 0.0296  0.0619  -0.0013 466 LYS A NZ  
3945 N N   . LEU A 467 ? 0.1077 0.2426 0.1158 -0.0034 0.0063  -0.0144 467 LEU A N   
3946 C CA  . LEU A 467 ? 0.0943 0.2260 0.1173 -0.0099 0.0044  -0.0028 467 LEU A CA  
3947 C C   . LEU A 467 ? 0.1450 0.2664 0.1660 -0.0117 -0.0050 -0.0027 467 LEU A C   
3948 O O   . LEU A 467 ? 0.1281 0.2468 0.1480 -0.0121 -0.0063 0.0071  467 LEU A O   
3949 C CB  . LEU A 467 ? 0.0924 0.2247 0.1364 -0.0117 0.0042  -0.0046 467 LEU A CB  
3950 C CG  . LEU A 467 ? 0.0832 0.2354 0.1408 -0.0107 0.0139  -0.0012 467 LEU A CG  
3951 C CD1 . LEU A 467 ? 0.0984 0.2472 0.1717 -0.0075 0.0091  -0.0055 467 LEU A CD1 
3952 C CD2 . LEU A 467 ? 0.1242 0.2797 0.1897 -0.0202 0.0194  0.0131  467 LEU A CD2 
3953 N N   . PHE A 468 ? 0.1160 0.2315 0.1389 -0.0123 -0.0104 -0.0118 468 PHE A N   
3954 C CA  . PHE A 468 ? 0.0976 0.2067 0.1222 -0.0133 -0.0152 -0.0106 468 PHE A CA  
3955 C C   . PHE A 468 ? 0.1195 0.2399 0.1366 -0.0107 -0.0197 -0.0067 468 PHE A C   
3956 O O   . PHE A 468 ? 0.1317 0.2539 0.1533 -0.0072 -0.0220 0.0009  468 PHE A O   
3957 C CB  . PHE A 468 ? 0.1001 0.2001 0.1268 -0.0163 -0.0168 -0.0172 468 PHE A CB  
3958 C CG  . PHE A 468 ? 0.0948 0.1953 0.1268 -0.0179 -0.0190 -0.0150 468 PHE A CG  
3959 C CD1 . PHE A 468 ? 0.1078 0.2079 0.1456 -0.0156 -0.0164 -0.0105 468 PHE A CD1 
3960 C CD2 . PHE A 468 ? 0.1084 0.2151 0.1412 -0.0216 -0.0243 -0.0193 468 PHE A CD2 
3961 C CE1 . PHE A 468 ? 0.0994 0.2100 0.1462 -0.0159 -0.0166 -0.0092 468 PHE A CE1 
3962 C CE2 . PHE A 468 ? 0.1381 0.2534 0.1825 -0.0236 -0.0265 -0.0170 468 PHE A CE2 
3963 C CZ  . PHE A 468 ? 0.1366 0.2557 0.1890 -0.0201 -0.0214 -0.0113 468 PHE A CZ  
3964 N N   . ARG A 469 ? 0.1102 0.2386 0.1136 -0.0102 -0.0223 -0.0125 469 ARG A N   
3965 C CA  . ARG A 469 ? 0.1323 0.2693 0.1252 -0.0062 -0.0282 -0.0088 469 ARG A CA  
3966 C C   . ARG A 469 ? 0.1333 0.2788 0.1150 0.0000  -0.0266 0.0081  469 ARG A C   
3967 O O   . ARG A 469 ? 0.1867 0.3349 0.1655 0.0064  -0.0320 0.0175  469 ARG A O   
3968 C CB  . ARG A 469 ? 0.1572 0.2954 0.1347 -0.0071 -0.0319 -0.0217 469 ARG A CB  
3969 C CG  . ARG A 469 ? 0.1792 0.3061 0.1701 -0.0152 -0.0365 -0.0335 469 ARG A CG  
3970 C CD  . ARG A 469 ? 0.1974 0.3204 0.1733 -0.0172 -0.0428 -0.0488 469 ARG A CD  
3971 N NE  . ARG A 469 ? 0.1980 0.3073 0.1863 -0.0278 -0.0489 -0.0593 469 ARG A NE  
3972 C CZ  . ARG A 469 ? 0.2174 0.3321 0.2166 -0.0354 -0.0591 -0.0602 469 ARG A CZ  
3973 N NH1 . ARG A 469 ? 0.1799 0.3137 0.1790 -0.0305 -0.0644 -0.0524 469 ARG A NH1 
3974 N NH2 . ARG A 469 ? 0.2197 0.3216 0.2313 -0.0481 -0.0648 -0.0687 469 ARG A NH2 
3975 N N   . SER A 470 ? 0.1444 0.2826 0.1245 -0.0016 -0.0149 0.0140  470 SER A N   
3976 C CA  . SER A 470 ? 0.1604 0.2939 0.1353 0.0005  -0.0088 0.0340  470 SER A CA  
3977 C C   . SER A 470 ? 0.1669 0.2828 0.1601 0.0006  -0.0118 0.0416  470 SER A C   
3978 O O   . SER A 470 ? 0.1828 0.2899 0.1707 0.0066  -0.0134 0.0575  470 SER A O   
3979 C CB  . SER A 470 ? 0.2197 0.3554 0.1971 -0.0048 0.0058  0.0390  470 SER A CB  
3980 O OG  . SER A 470 ? 0.2589 0.4112 0.2165 -0.0006 0.0113  0.0310  470 SER A OG  
3981 N N   . PHE A 471 ? 0.1360 0.2441 0.1473 -0.0038 -0.0125 0.0304  471 PHE A N   
3982 C CA  . PHE A 471 ? 0.1224 0.2130 0.1462 -0.0012 -0.0151 0.0323  471 PHE A CA  
3983 C C   . PHE A 471 ? 0.1682 0.2663 0.1917 0.0104  -0.0229 0.0333  471 PHE A C   
3984 O O   . PHE A 471 ? 0.1730 0.2568 0.1994 0.0195  -0.0246 0.0422  471 PHE A O   
3985 C CB  . PHE A 471 ? 0.1351 0.2209 0.1711 -0.0065 -0.0148 0.0188  471 PHE A CB  
3986 C CG  . PHE A 471 ? 0.1439 0.2275 0.1871 -0.0163 -0.0102 0.0182  471 PHE A CG  
3987 C CD1 . PHE A 471 ? 0.1470 0.2202 0.1961 -0.0228 -0.0059 0.0295  471 PHE A CD1 
3988 C CD2 . PHE A 471 ? 0.1340 0.2276 0.1814 -0.0191 -0.0103 0.0082  471 PHE A CD2 
3989 C CE1 . PHE A 471 ? 0.1489 0.2292 0.2130 -0.0338 -0.0019 0.0291  471 PHE A CE1 
3990 C CE2 . PHE A 471 ? 0.0997 0.1994 0.1592 -0.0257 -0.0076 0.0080  471 PHE A CE2 
3991 C CZ  . PHE A 471 ? 0.1169 0.2141 0.1870 -0.0338 -0.0035 0.0174  471 PHE A CZ  
3992 N N   . VAL A 472 ? 0.1374 0.2580 0.1605 0.0102  -0.0281 0.0243  472 VAL A N   
3993 C CA  . VAL A 472 ? 0.1333 0.2709 0.1633 0.0192  -0.0361 0.0246  472 VAL A CA  
3994 C C   . VAL A 472 ? 0.1524 0.2922 0.1693 0.0300  -0.0419 0.0397  472 VAL A C   
3995 O O   . VAL A 472 ? 0.1858 0.3254 0.2106 0.0428  -0.0462 0.0462  472 VAL A O   
3996 C CB  . VAL A 472 ? 0.1297 0.2729 0.1606 0.0097  -0.0366 0.0106  472 VAL A CB  
3997 C CG1 . VAL A 472 ? 0.1904 0.3492 0.2270 0.0147  -0.0449 0.0111  472 VAL A CG1 
3998 C CG2 . VAL A 472 ? 0.1845 0.3197 0.2268 0.0029  -0.0301 0.0024  472 VAL A CG2 
3999 N N   . ARG A 473 ? 0.1304 0.2714 0.1252 0.0266  -0.0407 0.0457  473 ARG A N   
4000 C CA  . ARG A 473 ? 0.1780 0.3175 0.1537 0.0362  -0.0439 0.0619  473 ARG A CA  
4001 C C   . ARG A 473 ? 0.2237 0.3388 0.2008 0.0447  -0.0401 0.0851  473 ARG A C   
4002 O O   . ARG A 473 ? 0.2455 0.3518 0.2213 0.0580  -0.0453 0.0966  473 ARG A O   
4003 C CB  . ARG A 473 ? 0.2217 0.3672 0.1710 0.0308  -0.0391 0.0616  473 ARG A CB  
4004 C CG  . ARG A 473 ? 0.3231 0.4692 0.2475 0.0398  -0.0418 0.0762  473 ARG A CG  
4005 C CD  . ARG A 473 ? 0.4618 0.6157 0.3600 0.0354  -0.0344 0.0717  473 ARG A CD  
4006 N NE  . ARG A 473 ? 0.7319 0.8767 0.6086 0.0392  -0.0248 0.0954  473 ARG A NE  
4007 C CZ  . ARG A 473 ? 0.8981 1.0449 0.7513 0.0485  -0.0309 0.1066  473 ARG A CZ  
4008 N NH1 . ARG A 473 ? 0.9533 1.1139 0.8036 0.0547  -0.0481 0.0953  473 ARG A NH1 
4009 N NH2 . ARG A 473 ? 0.9506 1.0863 0.7847 0.0501  -0.0198 0.1300  473 ARG A NH2 
4010 N N   . ARG A 474 ? 0.2003 0.2912 0.1845 0.0326  -0.0279 0.0846  474 ARG A N   
4011 C CA  . ARG A 474 ? 0.2453 0.2998 0.2350 0.0336  -0.0223 0.1011  474 ARG A CA  
4012 C C   . ARG A 474 ? 0.2068 0.2437 0.2137 0.0467  -0.0284 0.0958  474 ARG A C   
4013 O O   . ARG A 474 ? 0.2434 0.2498 0.2503 0.0572  -0.0291 0.1119  474 ARG A O   
4014 C CB  . ARG A 474 ? 0.2599 0.2996 0.2603 0.0145  -0.0110 0.0967  474 ARG A CB  
4015 C CG  . ARG A 474 ? 0.3854 0.3848 0.3951 0.0088  -0.0057 0.1124  474 ARG A CG  
4016 C CD  . ARG A 474 ? 0.3845 0.3764 0.3761 0.0092  0.0013  0.1438  474 ARG A CD  
4017 N NE  . ARG A 474 ? 0.4421 0.3890 0.4468 -0.0005 0.0071  0.1606  474 ARG A NE  
4018 C CZ  . ARG A 474 ? 0.6361 0.5413 0.6460 0.0111  0.0005  0.1664  474 ARG A CZ  
4019 N NH1 . ARG A 474 ? 0.6060 0.5167 0.6112 0.0348  -0.0108 0.1582  474 ARG A NH1 
4020 N NH2 . ARG A 474 ? 0.7502 0.6092 0.7713 -0.0010 0.0055  0.1772  474 ARG A NH2 
4021 N N   . ALA A 475 ? 0.1980 0.2532 0.2188 0.0480  -0.0316 0.0745  475 ALA A N   
4022 C CA  . ALA A 475 ? 0.2137 0.2594 0.2503 0.0626  -0.0340 0.0665  475 ALA A CA  
4023 C C   . ALA A 475 ? 0.2678 0.3238 0.3063 0.0859  -0.0426 0.0798  475 ALA A C   
4024 O O   . ALA A 475 ? 0.2867 0.3244 0.3366 0.1038  -0.0430 0.0791  475 ALA A O   
4025 C CB  . ALA A 475 ? 0.1541 0.2263 0.2026 0.0582  -0.0328 0.0452  475 ALA A CB  
4026 N N   . GLN A 476 ? 0.2233 0.3064 0.2491 0.0866  -0.0501 0.0889  476 GLN A N   
4027 C CA  . GLN A 476 ? 0.2346 0.3275 0.2614 0.1010  -0.0593 0.0935  476 GLN A CA  
4028 C C   . GLN A 476 ? 0.2837 0.3483 0.2895 0.1092  -0.0613 0.1179  476 GLN A C   
4029 O O   . GLN A 476 ? 0.3389 0.4116 0.3426 0.1224  -0.0710 0.1252  476 GLN A O   
4030 C CB  . GLN A 476 ? 0.2345 0.3688 0.2613 0.0921  -0.0668 0.0811  476 GLN A CB  
4031 C CG  . GLN A 476 ? 0.2466 0.4021 0.2940 0.0802  -0.0629 0.0596  476 GLN A CG  
4032 C CD  . GLN A 476 ? 0.2207 0.4035 0.2671 0.0671  -0.0694 0.0484  476 GLN A CD  
4033 O OE1 . GLN A 476 ? 0.2298 0.4344 0.2867 0.0724  -0.0789 0.0480  476 GLN A OE1 
4034 N NE2 . GLN A 476 ? 0.2371 0.4173 0.2729 0.0506  -0.0650 0.0390  476 GLN A NE2 
4035 N N   . GLU A 477 ? 0.3558 0.3877 0.3482 0.1000  -0.0517 0.1322  477 GLU A N   
4036 C CA  . GLU A 477 ? 0.4473 0.4484 0.4188 0.1027  -0.0498 0.1573  477 GLU A CA  
4037 C C   . GLU A 477 ? 0.5170 0.4611 0.4990 0.1072  -0.0445 0.1667  477 GLU A C   
4038 O O   . GLU A 477 ? 0.4357 0.3584 0.4328 0.0963  -0.0365 0.1584  477 GLU A O   
4039 C CB  . GLU A 477 ? 0.4700 0.4771 0.4193 0.0840  -0.0397 0.1667  477 GLU A CB  
4040 C CG  . GLU A 477 ? 0.5398 0.5942 0.4763 0.0786  -0.0442 0.1515  477 GLU A CG  
4041 C CD  . GLU A 477 ? 0.6635 0.7237 0.5760 0.0649  -0.0324 0.1587  477 GLU A CD  
4042 O OE1 . GLU A 477 ? 0.7008 0.7893 0.5936 0.0651  -0.0368 0.1500  477 GLU A OE1 
4043 O OE2 . GLU A 477 ? 0.6843 0.7212 0.6004 0.0531  -0.0184 0.1711  477 GLU A OE2 
4044 N N   . LYS B 2   ? 0.6154 0.5736 0.3672 0.0570  0.0096  -0.0089 2   LYS B N   
4045 C CA  . LYS B 2   ? 0.5656 0.5194 0.3306 0.0612  0.0149  -0.0120 2   LYS B CA  
4046 C C   . LYS B 2   ? 0.4187 0.3609 0.1980 0.0570  0.0084  -0.0143 2   LYS B C   
4047 O O   . LYS B 2   ? 0.4938 0.4224 0.2645 0.0553  0.0038  -0.0234 2   LYS B O   
4048 C CB  . LYS B 2   ? 0.6521 0.5989 0.4020 0.0692  0.0210  -0.0231 2   LYS B CB  
4049 C CG  . LYS B 2   ? 0.6969 0.6475 0.4587 0.0768  0.0289  -0.0234 2   LYS B CG  
4050 C CD  . LYS B 2   ? 0.7484 0.6813 0.5087 0.0814  0.0292  -0.0342 2   LYS B CD  
4051 C CE  . LYS B 2   ? 0.7574 0.6831 0.5015 0.0824  0.0300  -0.0427 2   LYS B CE  
4052 N NZ  . LYS B 2   ? 0.7420 0.6490 0.4840 0.0875  0.0317  -0.0516 2   LYS B NZ  
4053 N N   . LYS B 3   ? 0.3727 0.3198 0.1727 0.0545  0.0083  -0.0065 3   LYS B N   
4054 C CA  . LYS B 3   ? 0.3167 0.2552 0.1308 0.0509  0.0028  -0.0080 3   LYS B CA  
4055 C C   . LYS B 3   ? 0.3401 0.2744 0.1635 0.0554  0.0075  -0.0121 3   LYS B C   
4056 O O   . LYS B 3   ? 0.3681 0.3112 0.1935 0.0607  0.0150  -0.0106 3   LYS B O   
4057 C CB  . LYS B 3   ? 0.3535 0.2983 0.1837 0.0460  -0.0004 0.0022  3   LYS B CB  
4058 C CG  . LYS B 3   ? 0.4384 0.3884 0.2607 0.0434  -0.0050 0.0086  3   LYS B CG  
4059 C CD  . LYS B 3   ? 0.5217 0.4674 0.3424 0.0398  -0.0143 0.0048  3   LYS B CD  
4060 C CE  . LYS B 3   ? 0.5591 0.5133 0.3743 0.0385  -0.0196 0.0126  3   LYS B CE  
4061 N NZ  . LYS B 3   ? 0.6988 0.6551 0.4941 0.0371  -0.0238 0.0059  3   LYS B NZ  
4062 N N   . LEU B 4   ? 0.3071 0.2299 0.1361 0.0532  0.0030  -0.0167 4   LEU B N   
4063 C CA  . LEU B 4   ? 0.3180 0.2392 0.1605 0.0563  0.0057  -0.0174 4   LEU B CA  
4064 C C   . LEU B 4   ? 0.3326 0.2604 0.1945 0.0505  0.0024  -0.0106 4   LEU B C   
4065 O O   . LEU B 4   ? 0.2939 0.2184 0.1583 0.0450  -0.0042 -0.0096 4   LEU B O   
4066 C CB  . LEU B 4   ? 0.2803 0.1832 0.1161 0.0572  0.0034  -0.0257 4   LEU B CB  
4067 C CG  . LEU B 4   ? 0.3046 0.2047 0.1516 0.0616  0.0061  -0.0260 4   LEU B CG  
4068 C CD1 . LEU B 4   ? 0.3511 0.2324 0.1824 0.0686  0.0091  -0.0341 4   LEU B CD1 
4069 C CD2 . LEU B 4   ? 0.3175 0.2160 0.1789 0.0542  0.0000  -0.0238 4   LEU B CD2 
4070 N N   . PHE B 5   ? 0.2841 0.2221 0.1594 0.0519  0.0070  -0.0064 5   PHE B N   
4071 C CA  . PHE B 5   ? 0.2899 0.2319 0.1823 0.0466  0.0046  -0.0014 5   PHE B CA  
4072 C C   . PHE B 5   ? 0.3084 0.2460 0.2099 0.0477  0.0034  -0.0052 5   PHE B C   
4073 O O   . PHE B 5   ? 0.2970 0.2373 0.1987 0.0534  0.0077  -0.0077 5   PHE B O   
4074 C CB  . PHE B 5   ? 0.2286 0.1840 0.1294 0.0447  0.0100  0.0051  5   PHE B CB  
4075 C CG  . PHE B 5   ? 0.2445 0.2034 0.1362 0.0430  0.0115  0.0106  5   PHE B CG  
4076 C CD1 . PHE B 5   ? 0.3010 0.2535 0.1888 0.0398  0.0060  0.0141  5   PHE B CD1 
4077 C CD2 . PHE B 5   ? 0.2587 0.2291 0.1450 0.0453  0.0184  0.0127  5   PHE B CD2 
4078 C CE1 . PHE B 5   ? 0.3172 0.2730 0.1951 0.0390  0.0074  0.0203  5   PHE B CE1 
4079 C CE2 . PHE B 5   ? 0.3272 0.3012 0.2040 0.0434  0.0201  0.0185  5   PHE B CE2 
4080 C CZ  . PHE B 5   ? 0.3382 0.3041 0.2103 0.0403  0.0145  0.0226  5   PHE B CZ  
4081 N N   . LEU B 6   ? 0.2380 0.1703 0.1465 0.0430  -0.0023 -0.0053 6   LEU B N   
4082 C CA  . LEU B 6   ? 0.2313 0.1590 0.1470 0.0431  -0.0040 -0.0083 6   LEU B CA  
4083 C C   . LEU B 6   ? 0.2596 0.1945 0.1915 0.0391  -0.0050 -0.0046 6   LEU B C   
4084 O O   . LEU B 6   ? 0.2377 0.1733 0.1730 0.0354  -0.0076 -0.0012 6   LEU B O   
4085 C CB  . LEU B 6   ? 0.2494 0.1652 0.1577 0.0401  -0.0097 -0.0124 6   LEU B CB  
4086 C CG  . LEU B 6   ? 0.2628 0.1716 0.1755 0.0390  -0.0115 -0.0153 6   LEU B CG  
4087 C CD1 . LEU B 6   ? 0.3178 0.2215 0.2267 0.0460  -0.0066 -0.0176 6   LEU B CD1 
4088 C CD2 . LEU B 6   ? 0.2567 0.1558 0.1611 0.0334  -0.0170 -0.0189 6   LEU B CD2 
4089 N N   . VAL B 7   ? 0.1790 0.1193 0.1200 0.0406  -0.0026 -0.0053 7   VAL B N   
4090 C CA  . VAL B 7   ? 0.1869 0.1343 0.1419 0.0365  -0.0028 -0.0032 7   VAL B CA  
4091 C C   . VAL B 7   ? 0.2007 0.1472 0.1616 0.0371  -0.0046 -0.0059 7   VAL B C   
4092 O O   . VAL B 7   ? 0.2553 0.2061 0.2164 0.0415  -0.0020 -0.0071 7   VAL B O   
4093 C CB  . VAL B 7   ? 0.2127 0.1730 0.1733 0.0356  0.0024  -0.0007 7   VAL B CB  
4094 C CG1 . VAL B 7   ? 0.2414 0.2052 0.2139 0.0292  0.0019  0.0006  7   VAL B CG1 
4095 C CG2 . VAL B 7   ? 0.2355 0.1977 0.1879 0.0356  0.0055  0.0025  7   VAL B CG2 
4096 N N   . PHE B 8   ? 0.1833 0.1257 0.1487 0.0336  -0.0089 -0.0063 8   PHE B N   
4097 C CA  . PHE B 8   ? 0.1917 0.1352 0.1637 0.0331  -0.0103 -0.0080 8   PHE B CA  
4098 C C   . PHE B 8   ? 0.1815 0.1348 0.1652 0.0306  -0.0088 -0.0075 8   PHE B C   
4099 O O   . PHE B 8   ? 0.1835 0.1366 0.1711 0.0274  -0.0090 -0.0062 8   PHE B O   
4100 C CB  . PHE B 8   ? 0.1982 0.1359 0.1700 0.0300  -0.0151 -0.0088 8   PHE B CB  
4101 C CG  . PHE B 8   ? 0.1910 0.1188 0.1512 0.0300  -0.0171 -0.0107 8   PHE B CG  
4102 C CD1 . PHE B 8   ? 0.2043 0.1251 0.1602 0.0306  -0.0169 -0.0126 8   PHE B CD1 
4103 C CD2 . PHE B 8   ? 0.2279 0.1522 0.1801 0.0287  -0.0192 -0.0105 8   PHE B CD2 
4104 C CE1 . PHE B 8   ? 0.2266 0.1341 0.1695 0.0291  -0.0184 -0.0152 8   PHE B CE1 
4105 C CE2 . PHE B 8   ? 0.2871 0.2016 0.2269 0.0271  -0.0213 -0.0136 8   PHE B CE2 
4106 C CZ  . PHE B 8   ? 0.2461 0.1509 0.1810 0.0268  -0.0207 -0.0163 8   PHE B CZ  
4107 N N   . TRP B 9   ? 0.1285 0.0893 0.1165 0.0322  -0.0074 -0.0086 9   TRP B N   
4108 C CA  . TRP B 9   ? 0.1493 0.1202 0.1474 0.0285  -0.0066 -0.0095 9   TRP B CA  
4109 C C   . TRP B 9   ? 0.1580 0.1323 0.1594 0.0296  -0.0081 -0.0110 9   TRP B C   
4110 O O   . TRP B 9   ? 0.1602 0.1396 0.1597 0.0341  -0.0069 -0.0103 9   TRP B O   
4111 C CB  . TRP B 9   ? 0.1573 0.1407 0.1578 0.0282  -0.0027 -0.0088 9   TRP B CB  
4112 C CG  . TRP B 9   ? 0.1465 0.1395 0.1558 0.0213  -0.0015 -0.0103 9   TRP B CG  
4113 C CD1 . TRP B 9   ? 0.1803 0.1704 0.1946 0.0170  -0.0032 -0.0130 9   TRP B CD1 
4114 C CD2 . TRP B 9   ? 0.1358 0.1430 0.1487 0.0175  0.0018  -0.0099 9   TRP B CD2 
4115 N NE1 . TRP B 9   ? 0.1795 0.1783 0.1992 0.0100  -0.0011 -0.0150 9   TRP B NE1 
4116 C CE2 . TRP B 9   ? 0.1499 0.1604 0.1693 0.0093  0.0018  -0.0129 9   TRP B CE2 
4117 C CE3 . TRP B 9   ? 0.1677 0.1863 0.1788 0.0199  0.0052  -0.0075 9   TRP B CE3 
4118 C CZ2 . TRP B 9   ? 0.1520 0.1767 0.1761 0.0016  0.0046  -0.0138 9   TRP B CZ2 
4119 C CZ3 . TRP B 9   ? 0.2027 0.2384 0.2198 0.0132  0.0081  -0.0075 9   TRP B CZ3 
4120 C CH2 . TRP B 9   ? 0.1629 0.2014 0.1865 0.0031  0.0075  -0.0107 9   TRP B CH2 
4121 N N   . TRP B 10  ? 0.1611 0.1325 0.1664 0.0267  -0.0105 -0.0123 10  TRP B N   
4122 C CA  . TRP B 10  ? 0.1276 0.1022 0.1353 0.0270  -0.0119 -0.0131 10  TRP B CA  
4123 C C   . TRP B 10  ? 0.1261 0.1127 0.1413 0.0246  -0.0108 -0.0155 10  TRP B C   
4124 O O   . TRP B 10  ? 0.1682 0.1542 0.1877 0.0210  -0.0107 -0.0179 10  TRP B O   
4125 C CB  . TRP B 10  ? 0.1587 0.1273 0.1670 0.0250  -0.0148 -0.0133 10  TRP B CB  
4126 C CG  . TRP B 10  ? 0.1268 0.0853 0.1276 0.0253  -0.0169 -0.0118 10  TRP B CG  
4127 C CD1 . TRP B 10  ? 0.1431 0.0976 0.1426 0.0242  -0.0188 -0.0111 10  TRP B CD1 
4128 C CD2 . TRP B 10  ? 0.1556 0.1064 0.1480 0.0261  -0.0174 -0.0111 10  TRP B CD2 
4129 N NE1 . TRP B 10  ? 0.1968 0.1442 0.1880 0.0234  -0.0209 -0.0107 10  TRP B NE1 
4130 C CE2 . TRP B 10  ? 0.1569 0.1000 0.1432 0.0240  -0.0199 -0.0111 10  TRP B CE2 
4131 C CE3 . TRP B 10  ? 0.1587 0.1071 0.1470 0.0284  -0.0161 -0.0102 10  TRP B CE3 
4132 C CZ2 . TRP B 10  ? 0.1532 0.0852 0.1290 0.0228  -0.0209 -0.0116 10  TRP B CZ2 
4133 C CZ3 . TRP B 10  ? 0.1606 0.0950 0.1379 0.0284  -0.0165 -0.0098 10  TRP B CZ3 
4134 C CH2 . TRP B 10  ? 0.1857 0.1114 0.1567 0.0248  -0.0189 -0.0112 10  TRP B CH2 
4135 N N   . HIS B 11  ? 0.1353 0.1320 0.1511 0.0269  -0.0101 -0.0151 11  HIS B N   
4136 C CA  . HIS B 11  ? 0.1309 0.1425 0.1527 0.0241  -0.0094 -0.0178 11  HIS B CA  
4137 C C   . HIS B 11  ? 0.1180 0.1332 0.1417 0.0233  -0.0108 -0.0194 11  HIS B C   
4138 O O   . HIS B 11  ? 0.1321 0.1470 0.1524 0.0268  -0.0115 -0.0163 11  HIS B O   
4139 C CB  . HIS B 11  ? 0.1308 0.1563 0.1521 0.0280  -0.0080 -0.0157 11  HIS B CB  
4140 C CG  . HIS B 11  ? 0.1356 0.1796 0.1614 0.0264  -0.0083 -0.0175 11  HIS B CG  
4141 N ND1 . HIS B 11  ? 0.1179 0.1709 0.1491 0.0186  -0.0081 -0.0227 11  HIS B ND1 
4142 C CD2 . HIS B 11  ? 0.1165 0.1711 0.1410 0.0313  -0.0089 -0.0149 11  HIS B CD2 
4143 C CE1 . HIS B 11  ? 0.1461 0.2171 0.1795 0.0183  -0.0088 -0.0239 11  HIS B CE1 
4144 N NE2 . HIS B 11  ? 0.1488 0.2217 0.1785 0.0265  -0.0094 -0.0187 11  HIS B NE2 
4145 N N   . MET B 12  ? 0.1120 0.1298 0.1401 0.0188  -0.0106 -0.0241 12  MET B N   
4146 C CA  . MET B 12  ? 0.1270 0.1492 0.1569 0.0182  -0.0113 -0.0264 12  MET B CA  
4147 C C   . MET B 12  ? 0.1433 0.1809 0.1755 0.0151  -0.0107 -0.0308 12  MET B C   
4148 O O   . MET B 12  ? 0.1413 0.1803 0.1755 0.0101  -0.0096 -0.0353 12  MET B O   
4149 C CB  . MET B 12  ? 0.1315 0.1437 0.1634 0.0170  -0.0113 -0.0292 12  MET B CB  
4150 C CG  . MET B 12  ? 0.1399 0.1394 0.1699 0.0191  -0.0125 -0.0256 12  MET B CG  
4151 S SD  . MET B 12  ? 0.1494 0.1484 0.1754 0.0212  -0.0144 -0.0204 12  MET B SD  
4152 C CE  . MET B 12  ? 0.1662 0.1544 0.1914 0.0214  -0.0164 -0.0187 12  MET B CE  
4153 N N   . HIS B 13  ? 0.0893 0.1383 0.1206 0.0171  -0.0113 -0.0295 13  HIS B N   
4154 C CA  . HIS B 13  ? 0.0912 0.1581 0.1238 0.0140  -0.0113 -0.0336 13  HIS B CA  
4155 C C   . HIS B 13  ? 0.1278 0.2042 0.1584 0.0161  -0.0117 -0.0326 13  HIS B C   
4156 O O   . HIS B 13  ? 0.1325 0.2049 0.1602 0.0205  -0.0121 -0.0261 13  HIS B O   
4157 C CB  . HIS B 13  ? 0.0796 0.1603 0.1126 0.0153  -0.0115 -0.0307 13  HIS B CB  
4158 C CG  . HIS B 13  ? 0.1141 0.2182 0.1478 0.0133  -0.0124 -0.0332 13  HIS B CG  
4159 N ND1 . HIS B 13  ? 0.1197 0.2316 0.1552 0.0049  -0.0123 -0.0419 13  HIS B ND1 
4160 C CD2 . HIS B 13  ? 0.1088 0.2305 0.1407 0.0188  -0.0135 -0.0280 13  HIS B CD2 
4161 C CE1 . HIS B 13  ? 0.1302 0.2659 0.1654 0.0043  -0.0138 -0.0425 13  HIS B CE1 
4162 N NE2 . HIS B 13  ? 0.1149 0.2579 0.1483 0.0133  -0.0145 -0.0336 13  HIS B NE2 
4163 N N   . GLN B 14  ? 0.1277 0.2160 0.1589 0.0122  -0.0115 -0.0392 14  GLN B N   
4164 C CA  . GLN B 14  ? 0.1140 0.2180 0.1424 0.0138  -0.0119 -0.0381 14  GLN B CA  
4165 C C   . GLN B 14  ? 0.1110 0.2343 0.1394 0.0089  -0.0126 -0.0447 14  GLN B C   
4166 O O   . GLN B 14  ? 0.1602 0.2794 0.1898 0.0023  -0.0118 -0.0536 14  GLN B O   
4167 C CB  . GLN B 14  ? 0.0999 0.2003 0.1277 0.0140  -0.0106 -0.0405 14  GLN B CB  
4168 C CG  . GLN B 14  ? 0.1385 0.2244 0.1668 0.0170  -0.0103 -0.0344 14  GLN B CG  
4169 C CD  . GLN B 14  ? 0.1345 0.2214 0.1587 0.0205  -0.0110 -0.0245 14  GLN B CD  
4170 O OE1 . GLN B 14  ? 0.1462 0.2466 0.1668 0.0223  -0.0113 -0.0212 14  GLN B OE1 
4171 N NE2 . GLN B 14  ? 0.1473 0.2191 0.1710 0.0215  -0.0112 -0.0196 14  GLN B NE2 
4172 N N   . PRO B 15  ? 0.1211 0.2649 0.1471 0.0115  -0.0141 -0.0407 15  PRO B N   
4173 C CA  . PRO B 15  ? 0.1115 0.2777 0.1366 0.0059  -0.0153 -0.0477 15  PRO B CA  
4174 C C   . PRO B 15  ? 0.1019 0.2683 0.1237 0.0023  -0.0140 -0.0561 15  PRO B C   
4175 O O   . PRO B 15  ? 0.1431 0.2978 0.1638 0.0058  -0.0123 -0.0543 15  PRO B O   
4176 C CB  . PRO B 15  ? 0.1307 0.3184 0.1532 0.0125  -0.0172 -0.0387 15  PRO B CB  
4177 C CG  . PRO B 15  ? 0.1326 0.3058 0.1516 0.0201  -0.0160 -0.0293 15  PRO B CG  
4178 C CD  . PRO B 15  ? 0.1361 0.2826 0.1584 0.0196  -0.0145 -0.0296 15  PRO B CD  
4179 N N   . LEU B 16  ? 0.1300 0.3117 0.1497 -0.0049 -0.0148 -0.0656 16  LEU B N   
4180 C CA  . LEU B 16  ? 0.1590 0.3389 0.1742 -0.0084 -0.0129 -0.0759 16  LEU B CA  
4181 C C   . LEU B 16  ? 0.1669 0.3633 0.1772 -0.0031 -0.0130 -0.0713 16  LEU B C   
4182 O O   . LEU B 16  ? 0.1430 0.3625 0.1506 -0.0029 -0.0149 -0.0681 16  LEU B O   
4183 C CB  . LEU B 16  ? 0.1446 0.3309 0.1576 -0.0189 -0.0128 -0.0873 16  LEU B CB  
4184 C CG  . LEU B 16  ? 0.1648 0.3424 0.1725 -0.0224 -0.0095 -0.0983 16  LEU B CG  
4185 C CD1 . LEU B 16  ? 0.2141 0.3637 0.2218 -0.0195 -0.0068 -0.1031 16  LEU B CD1 
4186 C CD2 . LEU B 16  ? 0.2157 0.3948 0.2216 -0.0332 -0.0086 -0.1061 16  LEU B CD2 
4187 N N   . TYR B 17  ? 0.1461 0.3313 0.1556 0.0011  -0.0103 -0.0700 17  TYR B N   
4188 C CA  . TYR B 17  ? 0.1341 0.3343 0.1388 0.0052  -0.0095 -0.0651 17  TYR B CA  
4189 C C   . TYR B 17  ? 0.1545 0.3656 0.1531 0.0019  -0.0076 -0.0769 17  TYR B C   
4190 O O   . TYR B 17  ? 0.1664 0.3930 0.1599 0.0047  -0.0066 -0.0736 17  TYR B O   
4191 C CB  . TYR B 17  ? 0.1179 0.3040 0.1252 0.0106  -0.0073 -0.0564 17  TYR B CB  
4192 C CG  . TYR B 17  ? 0.1088 0.2830 0.1195 0.0141  -0.0088 -0.0447 17  TYR B CG  
4193 C CD1 . TYR B 17  ? 0.1234 0.3082 0.1309 0.0176  -0.0108 -0.0346 17  TYR B CD1 
4194 C CD2 . TYR B 17  ? 0.1028 0.2551 0.1188 0.0146  -0.0082 -0.0437 17  TYR B CD2 
4195 C CE1 . TYR B 17  ? 0.1131 0.2847 0.1218 0.0217  -0.0116 -0.0249 17  TYR B CE1 
4196 C CE2 . TYR B 17  ? 0.1250 0.2655 0.1423 0.0175  -0.0094 -0.0342 17  TYR B CE2 
4197 C CZ  . TYR B 17  ? 0.1229 0.2721 0.1362 0.0210  -0.0109 -0.0253 17  TYR B CZ  
4198 O OH  . TYR B 17  ? 0.1794 0.3151 0.1919 0.0250  -0.0115 -0.0166 17  TYR B OH  
4199 N N   . ARG B 18  ? 0.1605 0.3620 0.1588 -0.0041 -0.0066 -0.0899 18  ARG B N   
4200 C CA  . ARG B 18  ? 0.1809 0.3834 0.1754 -0.0069 -0.0036 -0.0997 18  ARG B CA  
4201 C C   . ARG B 18  ? 0.1904 0.4149 0.1827 -0.0119 -0.0053 -0.1001 18  ARG B C   
4202 O O   . ARG B 18  ? 0.1877 0.4129 0.1815 -0.0188 -0.0067 -0.1033 18  ARG B O   
4203 C CB  . ARG B 18  ? 0.1948 0.3715 0.1896 -0.0109 -0.0012 -0.1105 18  ARG B CB  
4204 C CG  . ARG B 18  ? 0.2278 0.3981 0.2170 -0.0111 0.0025  -0.1204 18  ARG B CG  
4205 C CD  . ARG B 18  ? 0.2870 0.4273 0.2743 -0.0146 0.0049  -0.1291 18  ARG B CD  
4206 N NE  . ARG B 18  ? 0.3284 0.4592 0.3078 -0.0139 0.0086  -0.1386 18  ARG B NE  
4207 C CZ  . ARG B 18  ? 0.4173 0.5552 0.3898 -0.0209 0.0085  -0.1460 18  ARG B CZ  
4208 N NH1 . ARG B 18  ? 0.3835 0.5402 0.3573 -0.0292 0.0049  -0.1443 18  ARG B NH1 
4209 N NH2 . ARG B 18  ? 0.5068 0.6331 0.4704 -0.0190 0.0122  -0.1550 18  ARG B NH2 
4210 N N   . GLU B 19  ? 0.1794 0.4226 0.1681 -0.0087 -0.0048 -0.0964 19  GLU B N   
4211 C CA  . GLU B 19  ? 0.1606 0.4262 0.1467 -0.0126 -0.0060 -0.0972 19  GLU B CA  
4212 C C   . GLU B 19  ? 0.1783 0.4360 0.1611 -0.0210 -0.0046 -0.1117 19  GLU B C   
4213 O O   . GLU B 19  ? 0.2208 0.4634 0.1998 -0.0202 -0.0015 -0.1201 19  GLU B O   
4214 C CB  . GLU B 19  ? 0.2340 0.5176 0.2162 -0.0073 -0.0052 -0.0910 19  GLU B CB  
4215 C CG  . GLU B 19  ? 0.3016 0.6117 0.2828 -0.0070 -0.0073 -0.0835 19  GLU B CG  
4216 C CD  . GLU B 19  ? 0.3677 0.6911 0.3454 -0.0138 -0.0072 -0.0937 19  GLU B CD  
4217 O OE1 . GLU B 19  ? 0.3088 0.6215 0.2826 -0.0171 -0.0049 -0.1055 19  GLU B OE1 
4218 O OE2 . GLU B 19  ? 0.4054 0.7496 0.3835 -0.0153 -0.0091 -0.0897 19  GLU B OE2 
4219 N N   . PRO B 20  ? 0.2278 0.4950 0.2109 -0.0288 -0.0063 -0.1148 20  PRO B N   
4220 C CA  . PRO B 20  ? 0.2993 0.5523 0.2781 -0.0384 -0.0049 -0.1284 20  PRO B CA  
4221 C C   . PRO B 20  ? 0.3413 0.6001 0.3118 -0.0404 -0.0032 -0.1375 20  PRO B C   
4222 O O   . PRO B 20  ? 0.4222 0.6606 0.3863 -0.0457 -0.0010 -0.1493 20  PRO B O   
4223 C CB  . PRO B 20  ? 0.3050 0.5714 0.2869 -0.0466 -0.0074 -0.1271 20  PRO B CB  
4224 C CG  . PRO B 20  ? 0.2659 0.5605 0.2516 -0.0399 -0.0097 -0.1141 20  PRO B CG  
4225 C CD  . PRO B 20  ? 0.2428 0.5297 0.2302 -0.0289 -0.0092 -0.1054 20  PRO B CD  
4226 N N   . TYR B 21  ? 0.2385 0.5226 0.2077 -0.0360 -0.0039 -0.1321 21  TYR B N   
4227 C CA  . TYR B 21  ? 0.2764 0.5677 0.2371 -0.0381 -0.0024 -0.1411 21  TYR B CA  
4228 C C   . TYR B 21  ? 0.3527 0.6310 0.3096 -0.0302 0.0013  -0.1433 21  TYR B C   
4229 O O   . TYR B 21  ? 0.4091 0.6741 0.3578 -0.0319 0.0042  -0.1551 21  TYR B O   
4230 C CB  . TYR B 21  ? 0.2638 0.5903 0.2242 -0.0376 -0.0047 -0.1346 21  TYR B CB  
4231 C CG  . TYR B 21  ? 0.3020 0.6445 0.2653 -0.0455 -0.0075 -0.1341 21  TYR B CG  
4232 C CD1 . TYR B 21  ? 0.3206 0.6683 0.2779 -0.0562 -0.0078 -0.1458 21  TYR B CD1 
4233 C CD2 . TYR B 21  ? 0.3333 0.6851 0.3045 -0.0423 -0.0096 -0.1220 21  TYR B CD2 
4234 C CE1 . TYR B 21  ? 0.3230 0.6879 0.2832 -0.0640 -0.0102 -0.1453 21  TYR B CE1 
4235 C CE2 . TYR B 21  ? 0.2849 0.6534 0.2587 -0.0489 -0.0116 -0.1213 21  TYR B CE2 
4236 C CZ  . TYR B 21  ? 0.3601 0.7364 0.3289 -0.0601 -0.0119 -0.1329 21  TYR B CZ  
4237 O OH  . TYR B 21  ? 0.3840 0.7797 0.3556 -0.0672 -0.0137 -0.1323 21  TYR B OH  
4238 N N   . THR B 22  ? 0.2430 0.5239 0.2051 -0.0215 0.0015  -0.1322 22  THR B N   
4239 C CA  . THR B 22  ? 0.2993 0.5726 0.2591 -0.0138 0.0052  -0.1328 22  THR B CA  
4240 C C   . THR B 22  ? 0.3252 0.5693 0.2878 -0.0102 0.0078  -0.1354 22  THR B C   
4241 O O   . THR B 22  ? 0.3253 0.5602 0.2854 -0.0041 0.0118  -0.1387 22  THR B O   
4242 C CB  . THR B 22  ? 0.2692 0.5629 0.2319 -0.0071 0.0045  -0.1186 22  THR B CB  
4243 O OG1 . THR B 22  ? 0.2385 0.5280 0.2080 -0.0050 0.0023  -0.1079 22  THR B OG1 
4244 C CG2 . THR B 22  ? 0.2817 0.6046 0.2411 -0.0090 0.0024  -0.1147 22  THR B CG2 
4245 N N   . GLY B 23  ? 0.2801 0.5109 0.2480 -0.0133 0.0058  -0.1336 23  GLY B N   
4246 C CA  . GLY B 23  ? 0.2828 0.4876 0.2543 -0.0093 0.0078  -0.1340 23  GLY B CA  
4247 C C   . GLY B 23  ? 0.2984 0.5079 0.2756 -0.0010 0.0082  -0.1232 23  GLY B C   
4248 O O   . GLY B 23  ? 0.3330 0.5236 0.3137 0.0036  0.0103  -0.1233 23  GLY B O   
4249 N N   . GLU B 24  ? 0.2252 0.4587 0.2031 0.0009  0.0065  -0.1132 24  GLU B N   
4250 C CA  . GLU B 24  ? 0.2171 0.4546 0.1985 0.0073  0.0073  -0.1021 24  GLU B CA  
4251 C C   . GLU B 24  ? 0.2034 0.4354 0.1893 0.0072  0.0044  -0.0937 24  GLU B C   
4252 O O   . GLU B 24  ? 0.1994 0.4393 0.1852 0.0037  0.0007  -0.0903 24  GLU B O   
4253 C CB  . GLU B 24  ? 0.2052 0.4673 0.1832 0.0090  0.0073  -0.0939 24  GLU B CB  
4254 C CG  . GLU B 24  ? 0.2300 0.4968 0.2036 0.0109  0.0111  -0.1017 24  GLU B CG  
4255 C CD  . GLU B 24  ? 0.4126 0.7039 0.3824 0.0121  0.0114  -0.0941 24  GLU B CD  
4256 O OE1 . GLU B 24  ? 0.4520 0.7562 0.4218 0.0115  0.0087  -0.0823 24  GLU B OE1 
4257 O OE2 . GLU B 24  ? 0.5109 0.8077 0.4770 0.0142  0.0147  -0.0995 24  GLU B OE2 
4258 N N   . TYR B 25  ? 0.1798 0.3992 0.1698 0.0117  0.0063  -0.0901 25  TYR B N   
4259 C CA  . TYR B 25  ? 0.1516 0.3643 0.1461 0.0124  0.0038  -0.0796 25  TYR B CA  
4260 C C   . TYR B 25  ? 0.1932 0.4211 0.1857 0.0144  0.0032  -0.0651 25  TYR B C   
4261 O O   . TYR B 25  ? 0.1757 0.4079 0.1689 0.0169  0.0064  -0.0599 25  TYR B O   
4262 C CB  . TYR B 25  ? 0.2067 0.3973 0.2096 0.0155  0.0053  -0.0782 25  TYR B CB  
4263 C CG  . TYR B 25  ? 0.1911 0.3615 0.1959 0.0133  0.0048  -0.0876 25  TYR B CG  
4264 C CD1 . TYR B 25  ? 0.2341 0.3987 0.2339 0.0125  0.0076  -0.1022 25  TYR B CD1 
4265 C CD2 . TYR B 25  ? 0.1724 0.3283 0.1824 0.0118  0.0018  -0.0820 25  TYR B CD2 
4266 C CE1 . TYR B 25  ? 0.2404 0.3828 0.2408 0.0094  0.0075  -0.1094 25  TYR B CE1 
4267 C CE2 . TYR B 25  ? 0.1619 0.2995 0.1729 0.0089  0.0018  -0.0896 25  TYR B CE2 
4268 C CZ  . TYR B 25  ? 0.2204 0.3508 0.2263 0.0074  0.0046  -0.1032 25  TYR B CZ  
4269 O OH  . TYR B 25  ? 0.2687 0.3777 0.2743 0.0035  0.0050  -0.1099 25  TYR B OH  
4270 N N   . LEU B 26  ? 0.1715 0.4080 0.1612 0.0135  -0.0006 -0.0581 26  LEU B N   
4271 C CA  . LEU B 26  ? 0.1622 0.4133 0.1466 0.0160  -0.0009 -0.0449 26  LEU B CA  
4272 C C   . LEU B 26  ? 0.2089 0.4443 0.1970 0.0183  -0.0009 -0.0306 26  LEU B C   
4273 O O   . LEU B 26  ? 0.1959 0.4377 0.1791 0.0197  0.0003  -0.0191 26  LEU B O   
4274 C CB  . LEU B 26  ? 0.1469 0.4155 0.1268 0.0157  -0.0046 -0.0428 26  LEU B CB  
4275 C CG  . LEU B 26  ? 0.1831 0.4645 0.1635 0.0115  -0.0043 -0.0541 26  LEU B CG  
4276 C CD1 . LEU B 26  ? 0.1872 0.4858 0.1672 0.0113  -0.0070 -0.0493 26  LEU B CD1 
4277 C CD2 . LEU B 26  ? 0.1922 0.4830 0.1690 0.0121  -0.0010 -0.0553 26  LEU B CD2 
4278 N N   . LEU B 27  ? 0.1659 0.3801 0.1612 0.0182  -0.0022 -0.0310 27  LEU B N   
4279 C CA  . LEU B 27  ? 0.1598 0.3567 0.1580 0.0191  -0.0018 -0.0204 27  LEU B CA  
4280 C C   . LEU B 27  ? 0.1598 0.3411 0.1662 0.0178  -0.0007 -0.0268 27  LEU B C   
4281 O O   . LEU B 27  ? 0.1674 0.3455 0.1769 0.0173  -0.0008 -0.0380 27  LEU B O   
4282 C CB  . LEU B 27  ? 0.1845 0.3713 0.1815 0.0218  -0.0049 -0.0122 27  LEU B CB  
4283 C CG  . LEU B 27  ? 0.1855 0.3867 0.1739 0.0256  -0.0059 -0.0025 27  LEU B CG  
4284 C CD1 . LEU B 27  ? 0.1781 0.3750 0.1668 0.0299  -0.0089 0.0012  27  LEU B CD1 
4285 C CD2 . LEU B 27  ? 0.2950 0.4902 0.2775 0.0261  -0.0034 0.0106  27  LEU B CD2 
4286 N N   . PRO B 28  ? 0.1873 0.3589 0.1966 0.0169  0.0005  -0.0196 28  PRO B N   
4287 C CA  . PRO B 28  ? 0.1783 0.3401 0.1955 0.0165  0.0014  -0.0247 28  PRO B CA  
4288 C C   . PRO B 28  ? 0.1715 0.3124 0.1924 0.0164  -0.0013 -0.0226 28  PRO B C   
4289 O O   . PRO B 28  ? 0.1529 0.2858 0.1794 0.0160  -0.0011 -0.0232 28  PRO B O   
4290 C CB  . PRO B 28  ? 0.1869 0.3564 0.2049 0.0142  0.0041  -0.0178 28  PRO B CB  
4291 C CG  . PRO B 28  ? 0.1875 0.3521 0.1985 0.0120  0.0030  -0.0054 28  PRO B CG  
4292 C CD  . PRO B 28  ? 0.1947 0.3672 0.1992 0.0154  0.0016  -0.0068 28  PRO B CD  
4293 N N   . TRP B 29  ? 0.1386 0.2725 0.1560 0.0173  -0.0037 -0.0193 29  TRP B N   
4294 C CA  . TRP B 29  ? 0.1864 0.3011 0.2056 0.0175  -0.0057 -0.0158 29  TRP B CA  
4295 C C   . TRP B 29  ? 0.1788 0.2839 0.2041 0.0177  -0.0063 -0.0240 29  TRP B C   
4296 O O   . TRP B 29  ? 0.1463 0.2375 0.1741 0.0173  -0.0073 -0.0217 29  TRP B O   
4297 C CB  . TRP B 29  ? 0.1746 0.2867 0.1887 0.0203  -0.0075 -0.0109 29  TRP B CB  
4298 C CG  . TRP B 29  ? 0.1903 0.3070 0.1965 0.0220  -0.0069 -0.0007 29  TRP B CG  
4299 C CD1 . TRP B 29  ? 0.1689 0.2996 0.1699 0.0255  -0.0074 0.0022  29  TRP B CD1 
4300 C CD2 . TRP B 29  ? 0.1726 0.2786 0.1741 0.0201  -0.0057 0.0087  29  TRP B CD2 
4301 N NE1 . TRP B 29  ? 0.2108 0.3389 0.2038 0.0275  -0.0064 0.0136  29  TRP B NE1 
4302 C CE2 . TRP B 29  ? 0.1975 0.3086 0.1901 0.0234  -0.0050 0.0176  29  TRP B CE2 
4303 C CE3 . TRP B 29  ? 0.2268 0.3194 0.2301 0.0153  -0.0052 0.0107  29  TRP B CE3 
4304 C CZ2 . TRP B 29  ? 0.2393 0.3388 0.2239 0.0218  -0.0033 0.0285  29  TRP B CZ2 
4305 C CZ3 . TRP B 29  ? 0.2111 0.2943 0.2071 0.0121  -0.0038 0.0205  29  TRP B CZ3 
4306 C CH2 . TRP B 29  ? 0.2636 0.3483 0.2499 0.0152  -0.0026 0.0294  29  TRP B CH2 
4307 N N   . THR B 30  ? 0.1310 0.2420 0.1576 0.0180  -0.0055 -0.0335 30  THR B N   
4308 C CA  . THR B 30  ? 0.1141 0.2126 0.1452 0.0184  -0.0054 -0.0402 30  THR B CA  
4309 C C   . THR B 30  ? 0.1201 0.2168 0.1556 0.0203  -0.0039 -0.0403 30  THR B C   
4310 O O   . THR B 30  ? 0.1268 0.2112 0.1658 0.0214  -0.0049 -0.0395 30  THR B O   
4311 C CB  . THR B 30  ? 0.1600 0.2618 0.1898 0.0171  -0.0043 -0.0509 30  THR B CB  
4312 O OG1 . THR B 30  ? 0.1628 0.2705 0.1897 0.0145  -0.0061 -0.0507 30  THR B OG1 
4313 C CG2 . THR B 30  ? 0.1513 0.2357 0.1840 0.0179  -0.0034 -0.0569 30  THR B CG2 
4314 N N   . PHE B 31  ? 0.1306 0.2421 0.1661 0.0210  -0.0015 -0.0413 31  PHE B N   
4315 C CA  . PHE B 31  ? 0.1370 0.2526 0.1778 0.0233  0.0001  -0.0406 31  PHE B CA  
4316 C C   . PHE B 31  ? 0.1198 0.2301 0.1631 0.0204  -0.0022 -0.0314 31  PHE B C   
4317 O O   . PHE B 31  ? 0.1341 0.2387 0.1823 0.0220  -0.0032 -0.0311 31  PHE B O   
4318 C CB  . PHE B 31  ? 0.1216 0.2575 0.1615 0.0240  0.0034  -0.0418 31  PHE B CB  
4319 C CG  . PHE B 31  ? 0.1444 0.2904 0.1909 0.0261  0.0053  -0.0399 31  PHE B CG  
4320 C CD1 . PHE B 31  ? 0.1527 0.2986 0.2033 0.0331  0.0075  -0.0472 31  PHE B CD1 
4321 C CD2 . PHE B 31  ? 0.1467 0.3018 0.1950 0.0211  0.0049  -0.0305 31  PHE B CD2 
4322 C CE1 . PHE B 31  ? 0.1593 0.3191 0.2171 0.0366  0.0093  -0.0450 31  PHE B CE1 
4323 C CE2 . PHE B 31  ? 0.1810 0.3500 0.2366 0.0220  0.0065  -0.0287 31  PHE B CE2 
4324 C CZ  . PHE B 31  ? 0.1598 0.3331 0.2208 0.0304  0.0085  -0.0358 31  PHE B CZ  
4325 N N   . PHE B 32  ? 0.1121 0.2233 0.1507 0.0161  -0.0032 -0.0237 32  PHE B N   
4326 C CA  . PHE B 32  ? 0.1298 0.2342 0.1687 0.0118  -0.0049 -0.0159 32  PHE B CA  
4327 C C   . PHE B 32  ? 0.1246 0.2100 0.1633 0.0122  -0.0079 -0.0158 32  PHE B C   
4328 O O   . PHE B 32  ? 0.1294 0.2105 0.1709 0.0100  -0.0095 -0.0135 32  PHE B O   
4329 C CB  . PHE B 32  ? 0.1292 0.2340 0.1608 0.0074  -0.0044 -0.0076 32  PHE B CB  
4330 C CG  . PHE B 32  ? 0.1240 0.2479 0.1560 0.0045  -0.0014 -0.0047 32  PHE B CG  
4331 C CD1 . PHE B 32  ? 0.1375 0.2737 0.1766 0.0020  -0.0002 -0.0049 32  PHE B CD1 
4332 C CD2 . PHE B 32  ? 0.1898 0.3220 0.2151 0.0046  0.0004  -0.0014 32  PHE B CD2 
4333 C CE1 . PHE B 32  ? 0.1941 0.3510 0.2339 -0.0009 0.0032  -0.0020 32  PHE B CE1 
4334 C CE2 . PHE B 32  ? 0.1944 0.3453 0.2190 0.0016  0.0037  0.0018  32  PHE B CE2 
4335 C CZ  . PHE B 32  ? 0.1818 0.3449 0.2138 -0.0014 0.0054  0.0014  32  PHE B CZ  
4336 N N   . HIS B 33  ? 0.1225 0.1989 0.1581 0.0147  -0.0087 -0.0182 33  HIS B N   
4337 C CA  . HIS B 33  ? 0.0977 0.1580 0.1331 0.0153  -0.0109 -0.0180 33  HIS B CA  
4338 C C   . HIS B 33  ? 0.1504 0.2079 0.1914 0.0182  -0.0110 -0.0236 33  HIS B C   
4339 O O   . HIS B 33  ? 0.1472 0.1944 0.1886 0.0183  -0.0129 -0.0221 33  HIS B O   
4340 C CB  . HIS B 33  ? 0.1138 0.1674 0.1444 0.0168  -0.0114 -0.0177 33  HIS B CB  
4341 C CG  . HIS B 33  ? 0.1406 0.1900 0.1641 0.0161  -0.0116 -0.0103 33  HIS B CG  
4342 N ND1 . HIS B 33  ? 0.1610 0.1961 0.1802 0.0141  -0.0127 -0.0054 33  HIS B ND1 
4343 C CD2 . HIS B 33  ? 0.1631 0.2194 0.1818 0.0176  -0.0107 -0.0068 33  HIS B CD2 
4344 C CE1 . HIS B 33  ? 0.1448 0.1750 0.1562 0.0147  -0.0119 0.0007  33  HIS B CE1 
4345 N NE2 . HIS B 33  ? 0.1276 0.1714 0.1389 0.0176  -0.0108 0.0007  33  HIS B NE2 
4346 N N   . ALA B 34  ? 0.1364 0.2022 0.1805 0.0212  -0.0088 -0.0297 34  ALA B N   
4347 C CA  . ALA B 34  ? 0.1453 0.2064 0.1936 0.0255  -0.0083 -0.0337 34  ALA B CA  
4348 C C   . ALA B 34  ? 0.1662 0.2342 0.2195 0.0263  -0.0094 -0.0297 34  ALA B C   
4349 O O   . ALA B 34  ? 0.1727 0.2333 0.2278 0.0285  -0.0112 -0.0284 34  ALA B O   
4350 C CB  . ALA B 34  ? 0.1759 0.2416 0.2245 0.0291  -0.0049 -0.0418 34  ALA B CB  
4351 N N   . VAL B 35  ? 0.1346 0.2188 0.1899 0.0240  -0.0084 -0.0272 35  VAL B N   
4352 C CA  . VAL B 35  ? 0.0909 0.1867 0.1523 0.0239  -0.0093 -0.0238 35  VAL B CA  
4353 C C   . VAL B 35  ? 0.1438 0.2320 0.2030 0.0172  -0.0132 -0.0179 35  VAL B C   
4354 O O   . VAL B 35  ? 0.1541 0.2481 0.2177 0.0169  -0.0154 -0.0158 35  VAL B O   
4355 C CB  . VAL B 35  ? 0.1584 0.2768 0.2233 0.0224  -0.0066 -0.0228 35  VAL B CB  
4356 C CG1 . VAL B 35  ? 0.1295 0.2549 0.1947 0.0294  -0.0023 -0.0300 35  VAL B CG1 
4357 C CG2 . VAL B 35  ? 0.1656 0.2849 0.2250 0.0135  -0.0067 -0.0171 35  VAL B CG2 
4358 N N   . LYS B 36  ? 0.1668 0.2426 0.2185 0.0123  -0.0140 -0.0153 36  LYS B N   
4359 C CA  . LYS B 36  ? 0.1439 0.2095 0.1910 0.0057  -0.0169 -0.0105 36  LYS B CA  
4360 C C   . LYS B 36  ? 0.1639 0.2122 0.2074 0.0082  -0.0191 -0.0116 36  LYS B C   
4361 O O   . LYS B 36  ? 0.1776 0.2216 0.2198 0.0050  -0.0221 -0.0097 36  LYS B O   
4362 C CB  . LYS B 36  ? 0.1606 0.2199 0.1997 0.0003  -0.0159 -0.0062 36  LYS B CB  
4363 C CG  . LYS B 36  ? 0.1631 0.2097 0.1954 -0.0076 -0.0181 -0.0017 36  LYS B CG  
4364 C CD  . LYS B 36  ? 0.1447 0.1834 0.1680 -0.0126 -0.0162 0.0037  36  LYS B CD  
4365 C CE  . LYS B 36  ? 0.1744 0.1970 0.1896 -0.0065 -0.0154 0.0042  36  LYS B CE  
4366 N NZ  . LYS B 36  ? 0.1741 0.1776 0.1837 -0.0051 -0.0174 0.0029  36  LYS B NZ  
4367 N N   . ASP B 37  ? 0.1172 0.1569 0.1586 0.0129  -0.0178 -0.0147 37  ASP B N   
4368 C CA  . ASP B 37  ? 0.1374 0.1615 0.1742 0.0143  -0.0191 -0.0148 37  ASP B CA  
4369 C C   . ASP B 37  ? 0.1429 0.1632 0.1826 0.0195  -0.0183 -0.0187 37  ASP B C   
4370 O O   . ASP B 37  ? 0.1451 0.1563 0.1830 0.0206  -0.0199 -0.0179 37  ASP B O   
4371 C CB  . ASP B 37  ? 0.1792 0.1957 0.2092 0.0138  -0.0180 -0.0134 37  ASP B CB  
4372 C CG  . ASP B 37  ? 0.1362 0.1518 0.1611 0.0092  -0.0180 -0.0087 37  ASP B CG  
4373 O OD1 . ASP B 37  ? 0.1902 0.1982 0.2112 0.0048  -0.0198 -0.0064 37  ASP B OD1 
4374 O OD2 . ASP B 37  ? 0.1553 0.1778 0.1792 0.0093  -0.0161 -0.0074 37  ASP B OD2 
4375 N N   . TYR B 38  ? 0.1255 0.1508 0.1682 0.0223  -0.0158 -0.0231 38  TYR B N   
4376 C CA  . TYR B 38  ? 0.1671 0.1832 0.2096 0.0251  -0.0145 -0.0268 38  TYR B CA  
4377 C C   . TYR B 38  ? 0.1620 0.1738 0.2072 0.0297  -0.0149 -0.0267 38  TYR B C   
4378 O O   . TYR B 38  ? 0.1473 0.1468 0.1902 0.0310  -0.0147 -0.0268 38  TYR B O   
4379 C CB  . TYR B 38  ? 0.1565 0.1769 0.1994 0.0252  -0.0117 -0.0325 38  TYR B CB  
4380 C CG  . TYR B 38  ? 0.1181 0.1440 0.1578 0.0219  -0.0116 -0.0321 38  TYR B CG  
4381 C CD1 . TYR B 38  ? 0.1122 0.1324 0.1483 0.0205  -0.0129 -0.0280 38  TYR B CD1 
4382 C CD2 . TYR B 38  ? 0.1420 0.1797 0.1817 0.0212  -0.0100 -0.0354 38  TYR B CD2 
4383 C CE1 . TYR B 38  ? 0.1260 0.1525 0.1591 0.0196  -0.0126 -0.0266 38  TYR B CE1 
4384 C CE2 . TYR B 38  ? 0.1388 0.1839 0.1753 0.0193  -0.0102 -0.0339 38  TYR B CE2 
4385 C CZ  . TYR B 38  ? 0.1602 0.1998 0.1938 0.0191  -0.0116 -0.0291 38  TYR B CZ  
4386 O OH  . TYR B 38  ? 0.1378 0.1859 0.1683 0.0193  -0.0116 -0.0268 38  TYR B OH  
4387 N N   . TYR B 39  ? 0.1423 0.1654 0.1924 0.0326  -0.0153 -0.0260 39  TYR B N   
4388 C CA  . TYR B 39  ? 0.1659 0.1878 0.2185 0.0384  -0.0164 -0.0241 39  TYR B CA  
4389 C C   . TYR B 39  ? 0.1597 0.1817 0.2106 0.0352  -0.0206 -0.0187 39  TYR B C   
4390 O O   . TYR B 39  ? 0.1375 0.1509 0.1861 0.0381  -0.0220 -0.0164 39  TYR B O   
4391 C CB  . TYR B 39  ? 0.1315 0.1697 0.1908 0.0440  -0.0151 -0.0251 39  TYR B CB  
4392 C CG  . TYR B 39  ? 0.1157 0.1572 0.1783 0.0514  -0.0169 -0.0216 39  TYR B CG  
4393 C CD1 . TYR B 39  ? 0.1457 0.1735 0.2065 0.0601  -0.0147 -0.0228 39  TYR B CD1 
4394 C CD2 . TYR B 39  ? 0.1154 0.1736 0.1822 0.0493  -0.0206 -0.0168 39  TYR B CD2 
4395 C CE1 . TYR B 39  ? 0.2182 0.2492 0.2813 0.0686  -0.0163 -0.0184 39  TYR B CE1 
4396 C CE2 . TYR B 39  ? 0.1800 0.2449 0.2500 0.0566  -0.0228 -0.0131 39  TYR B CE2 
4397 C CZ  . TYR B 39  ? 0.1709 0.2224 0.2390 0.0673  -0.0206 -0.0135 39  TYR B CZ  
4398 O OH  . TYR B 39  ? 0.2490 0.3074 0.3196 0.0765  -0.0227 -0.0085 39  TYR B OH  
4399 N N   . ASP B 40  ? 0.1186 0.1486 0.1690 0.0286  -0.0224 -0.0166 40  ASP B N   
4400 C CA  . ASP B 40  ? 0.1419 0.1739 0.1904 0.0247  -0.0265 -0.0127 40  ASP B CA  
4401 C C   . ASP B 40  ? 0.1540 0.1692 0.1940 0.0226  -0.0279 -0.0118 40  ASP B C   
4402 O O   . ASP B 40  ? 0.1517 0.1662 0.1892 0.0222  -0.0310 -0.0095 40  ASP B O   
4403 C CB  . ASP B 40  ? 0.1568 0.1998 0.2060 0.0168  -0.0276 -0.0112 40  ASP B CB  
4404 C CG  . ASP B 40  ? 0.1995 0.2650 0.2578 0.0183  -0.0277 -0.0105 40  ASP B CG  
4405 O OD1 . ASP B 40  ? 0.1648 0.2402 0.2265 0.0197  -0.0308 -0.0083 40  ASP B OD1 
4406 O OD2 . ASP B 40  ? 0.2119 0.2871 0.2740 0.0189  -0.0246 -0.0119 40  ASP B OD2 
4407 N N   . MET B 41  ? 0.1285 0.1329 0.1641 0.0215  -0.0255 -0.0134 41  MET B N   
4408 C CA  . MET B 41  ? 0.1387 0.1297 0.1665 0.0206  -0.0260 -0.0124 41  MET B CA  
4409 C C   . MET B 41  ? 0.1606 0.1460 0.1879 0.0250  -0.0263 -0.0114 41  MET B C   
4410 O O   . MET B 41  ? 0.1695 0.1512 0.1915 0.0242  -0.0288 -0.0092 41  MET B O   
4411 C CB  . MET B 41  ? 0.1571 0.1424 0.1818 0.0200  -0.0232 -0.0139 41  MET B CB  
4412 C CG  . MET B 41  ? 0.1431 0.1285 0.1638 0.0160  -0.0233 -0.0126 41  MET B CG  
4413 S SD  . MET B 41  ? 0.1682 0.1409 0.1779 0.0122  -0.0257 -0.0107 41  MET B SD  
4414 C CE  . MET B 41  ? 0.1433 0.1056 0.1469 0.0170  -0.0231 -0.0112 41  MET B CE  
4415 N N   . PRO B 42  ? 0.1348 0.1181 0.1659 0.0294  -0.0238 -0.0129 42  PRO B N   
4416 C CA  . PRO B 42  ? 0.1589 0.1344 0.1879 0.0337  -0.0238 -0.0105 42  PRO B CA  
4417 C C   . PRO B 42  ? 0.1795 0.1637 0.2113 0.0380  -0.0270 -0.0072 42  PRO B C   
4418 O O   . PRO B 42  ? 0.1890 0.1688 0.2171 0.0411  -0.0285 -0.0034 42  PRO B O   
4419 C CB  . PRO B 42  ? 0.1646 0.1329 0.1958 0.0363  -0.0197 -0.0135 42  PRO B CB  
4420 C CG  . PRO B 42  ? 0.1661 0.1443 0.2026 0.0354  -0.0185 -0.0178 42  PRO B CG  
4421 C CD  . PRO B 42  ? 0.1310 0.1150 0.1655 0.0299  -0.0203 -0.0170 42  PRO B CD  
4422 N N   . ALA B 43  ? 0.1434 0.1424 0.1818 0.0385  -0.0281 -0.0081 43  ALA B N   
4423 C CA  . ALA B 43  ? 0.1487 0.1613 0.1912 0.0431  -0.0312 -0.0047 43  ALA B CA  
4424 C C   . ALA B 43  ? 0.1328 0.1508 0.1707 0.0378  -0.0363 -0.0017 43  ALA B C   
4425 O O   . ALA B 43  ? 0.1753 0.2047 0.2151 0.0417  -0.0396 0.0019  43  ALA B O   
4426 C CB  . ALA B 43  ? 0.1454 0.1761 0.1966 0.0442  -0.0306 -0.0064 43  ALA B CB  
4427 N N   . TYR B 44  ? 0.1585 0.1688 0.1896 0.0294  -0.0369 -0.0033 44  TYR B N   
4428 C CA  . TYR B 44  ? 0.1830 0.1935 0.2066 0.0246  -0.0412 -0.0018 44  TYR B CA  
4429 C C   . TYR B 44  ? 0.1873 0.1925 0.2062 0.0305  -0.0422 0.0018  44  TYR B C   
4430 O O   . TYR B 44  ? 0.2070 0.2198 0.2219 0.0292  -0.0467 0.0040  44  TYR B O   
4431 C CB  . TYR B 44  ? 0.1777 0.1745 0.1921 0.0174  -0.0403 -0.0045 44  TYR B CB  
4432 C CG  . TYR B 44  ? 0.1683 0.1684 0.1828 0.0093  -0.0406 -0.0065 44  TYR B CG  
4433 C CD1 . TYR B 44  ? 0.1960 0.2015 0.2063 0.0008  -0.0448 -0.0068 44  TYR B CD1 
4434 C CD2 . TYR B 44  ? 0.1500 0.1471 0.1676 0.0093  -0.0368 -0.0080 44  TYR B CD2 
4435 C CE1 . TYR B 44  ? 0.1771 0.1821 0.1858 -0.0081 -0.0445 -0.0081 44  TYR B CE1 
4436 C CE2 . TYR B 44  ? 0.1540 0.1527 0.1706 0.0022  -0.0367 -0.0084 44  TYR B CE2 
4437 C CZ  . TYR B 44  ? 0.1757 0.1769 0.1877 -0.0067 -0.0403 -0.0083 44  TYR B CZ  
4438 O OH  . TYR B 44  ? 0.2345 0.2339 0.2438 -0.0151 -0.0396 -0.0081 44  TYR B OH  
4439 N N   . LEU B 45  ? 0.2014 0.1941 0.2201 0.0364  -0.0381 0.0026  45  LEU B N   
4440 C CA  . LEU B 45  ? 0.1998 0.1849 0.2125 0.0414  -0.0383 0.0071  45  LEU B CA  
4441 C C   . LEU B 45  ? 0.2563 0.2530 0.2730 0.0496  -0.0411 0.0121  45  LEU B C   
4442 O O   . LEU B 45  ? 0.2495 0.2437 0.2602 0.0538  -0.0426 0.0173  45  LEU B O   
4443 C CB  . LEU B 45  ? 0.2172 0.1852 0.2282 0.0436  -0.0328 0.0068  45  LEU B CB  
4444 C CG  . LEU B 45  ? 0.2607 0.2198 0.2666 0.0372  -0.0302 0.0036  45  LEU B CG  
4445 C CD1 . LEU B 45  ? 0.2608 0.2084 0.2678 0.0376  -0.0249 0.0026  45  LEU B CD1 
4446 C CD2 . LEU B 45  ? 0.2279 0.1840 0.2236 0.0353  -0.0319 0.0059  45  LEU B CD2 
4447 N N   . LYS B 46  ? 0.2197 0.2305 0.2461 0.0528  -0.0415 0.0112  46  LYS B N   
4448 C CA  . LYS B 46  ? 0.2567 0.2833 0.2875 0.0619  -0.0446 0.0164  46  LYS B CA  
4449 C C   . LYS B 46  ? 0.2362 0.2813 0.2645 0.0568  -0.0514 0.0186  46  LYS B C   
4450 O O   . LYS B 46  ? 0.2886 0.3451 0.3164 0.0641  -0.0548 0.0246  46  LYS B O   
4451 C CB  . LYS B 46  ? 0.2946 0.3350 0.3367 0.0671  -0.0429 0.0145  46  LYS B CB  
4452 C CG  . LYS B 46  ? 0.3390 0.3617 0.3822 0.0751  -0.0365 0.0127  46  LYS B CG  
4453 C CD  . LYS B 46  ? 0.4930 0.5266 0.5452 0.0763  -0.0337 0.0078  46  LYS B CD  
4454 C CE  . LYS B 46  ? 0.6128 0.6753 0.6741 0.0826  -0.0367 0.0108  46  LYS B CE  
4455 N NZ  . LYS B 46  ? 0.6661 0.7323 0.7336 0.0878  -0.0310 0.0074  46  LYS B NZ  
4456 N N   . ASP B 47  ? 0.2223 0.2696 0.2476 0.0444  -0.0533 0.0140  47  ASP B N   
4457 C CA  . ASP B 47  ? 0.2079 0.2733 0.2308 0.0366  -0.0598 0.0141  47  ASP B CA  
4458 C C   . ASP B 47  ? 0.2033 0.2562 0.2120 0.0297  -0.0618 0.0128  47  ASP B C   
4459 O O   . ASP B 47  ? 0.2467 0.3133 0.2510 0.0234  -0.0676 0.0126  47  ASP B O   
4460 C CB  . ASP B 47  ? 0.2051 0.2818 0.2338 0.0259  -0.0605 0.0095  47  ASP B CB  
4461 C CG  . ASP B 47  ? 0.3699 0.4680 0.4126 0.0317  -0.0598 0.0111  47  ASP B CG  
4462 O OD1 . ASP B 47  ? 0.3650 0.4782 0.4129 0.0425  -0.0615 0.0161  47  ASP B OD1 
4463 O OD2 . ASP B 47  ? 0.3912 0.4913 0.4392 0.0265  -0.0571 0.0078  47  ASP B OD2 
4464 N N   . PHE B 48  ? 0.2194 0.2487 0.2209 0.0303  -0.0572 0.0113  48  PHE B N   
4465 C CA  . PHE B 48  ? 0.2409 0.2584 0.2284 0.0251  -0.0579 0.0095  48  PHE B CA  
4466 C C   . PHE B 48  ? 0.2354 0.2385 0.2177 0.0327  -0.0540 0.0136  48  PHE B C   
4467 O O   . PHE B 48  ? 0.2285 0.2203 0.2156 0.0368  -0.0488 0.0139  48  PHE B O   
4468 C CB  . PHE B 48  ? 0.2445 0.2487 0.2272 0.0162  -0.0555 0.0028  48  PHE B CB  
4469 C CG  . PHE B 48  ? 0.2567 0.2718 0.2428 0.0069  -0.0587 -0.0006 48  PHE B CG  
4470 C CD1 . PHE B 48  ? 0.2925 0.3148 0.2706 -0.0022 -0.0641 -0.0030 48  PHE B CD1 
4471 C CD2 . PHE B 48  ? 0.2227 0.2422 0.2197 0.0064  -0.0563 -0.0013 48  PHE B CD2 
4472 C CE1 . PHE B 48  ? 0.2645 0.2967 0.2453 -0.0130 -0.0668 -0.0059 48  PHE B CE1 
4473 C CE2 . PHE B 48  ? 0.2575 0.2884 0.2576 -0.0033 -0.0589 -0.0035 48  PHE B CE2 
4474 C CZ  . PHE B 48  ? 0.3018 0.3387 0.2940 -0.0135 -0.0641 -0.0056 48  PHE B CZ  
4475 N N   . GLU B 49  ? 0.2176 0.2216 0.1894 0.0336  -0.0566 0.0167  49  GLU B N   
4476 C CA  . GLU B 49  ? 0.2207 0.2130 0.1866 0.0402  -0.0531 0.0222  49  GLU B CA  
4477 C C   . GLU B 49  ? 0.2120 0.1882 0.1688 0.0358  -0.0485 0.0184  49  GLU B C   
4478 O O   . GLU B 49  ? 0.2471 0.2207 0.1918 0.0349  -0.0488 0.0194  49  GLU B O   
4479 C CB  . GLU B 49  ? 0.2332 0.2371 0.1919 0.0445  -0.0580 0.0288  49  GLU B CB  
4480 C CG  . GLU B 49  ? 0.2967 0.3166 0.2657 0.0530  -0.0611 0.0346  49  GLU B CG  
4481 C CD  . GLU B 49  ? 0.3758 0.3818 0.3514 0.0625  -0.0553 0.0391  49  GLU B CD  
4482 O OE1 . GLU B 49  ? 0.4317 0.4215 0.4001 0.0664  -0.0513 0.0441  49  GLU B OE1 
4483 O OE2 . GLU B 49  ? 0.4305 0.4413 0.4177 0.0657  -0.0543 0.0373  49  GLU B OE2 
4484 N N   . ILE B 50  ? 0.2287 0.1958 0.1916 0.0338  -0.0439 0.0142  50  ILE B N   
4485 C CA  . ILE B 50  ? 0.1999 0.1548 0.1572 0.0313  -0.0389 0.0110  50  ILE B CA  
4486 C C   . ILE B 50  ? 0.2233 0.1708 0.1887 0.0338  -0.0334 0.0124  50  ILE B C   
4487 O O   . ILE B 50  ? 0.2302 0.1791 0.2040 0.0373  -0.0333 0.0148  50  ILE B O   
4488 C CB  . ILE B 50  ? 0.1847 0.1371 0.1396 0.0254  -0.0392 0.0038  50  ILE B CB  
4489 C CG1 . ILE B 50  ? 0.2303 0.1873 0.1974 0.0241  -0.0397 0.0018  50  ILE B CG1 
4490 C CG2 . ILE B 50  ? 0.2544 0.2098 0.1976 0.0207  -0.0441 0.0008  50  ILE B CG2 
4491 C CD1 . ILE B 50  ? 0.3058 0.2576 0.2712 0.0192  -0.0388 -0.0035 50  ILE B CD1 
4492 N N   . LYS B 51  ? 0.2205 0.1610 0.1830 0.0320  -0.0285 0.0106  51  LYS B N   
4493 C CA  . LYS B 51  ? 0.2110 0.1468 0.1811 0.0319  -0.0236 0.0105  51  LYS B CA  
4494 C C   . LYS B 51  ? 0.1735 0.1111 0.1483 0.0293  -0.0224 0.0046  51  LYS B C   
4495 O O   . LYS B 51  ? 0.1895 0.1270 0.1582 0.0282  -0.0226 0.0016  51  LYS B O   
4496 C CB  . LYS B 51  ? 0.1889 0.1197 0.1535 0.0311  -0.0187 0.0137  51  LYS B CB  
4497 C CG  . LYS B 51  ? 0.2755 0.2041 0.2316 0.0334  -0.0195 0.0204  51  LYS B CG  
4498 C CD  . LYS B 51  ? 0.2892 0.2130 0.2495 0.0371  -0.0203 0.0257  51  LYS B CD  
4499 C CE  . LYS B 51  ? 0.3368 0.2573 0.2871 0.0403  -0.0205 0.0343  51  LYS B CE  
4500 N NZ  . LYS B 51  ? 0.4924 0.4063 0.4459 0.0461  -0.0211 0.0401  51  LYS B NZ  
4501 N N   . LEU B 52  ? 0.1493 0.0876 0.1337 0.0289  -0.0208 0.0029  52  LEU B N   
4502 C CA  . LEU B 52  ? 0.1646 0.1061 0.1536 0.0271  -0.0195 -0.0016 52  LEU B CA  
4503 C C   . LEU B 52  ? 0.1865 0.1278 0.1823 0.0258  -0.0158 -0.0025 52  LEU B C   
4504 O O   . LEU B 52  ? 0.2119 0.1495 0.2114 0.0266  -0.0155 -0.0015 52  LEU B O   
4505 C CB  . LEU B 52  ? 0.1964 0.1426 0.1897 0.0266  -0.0230 -0.0038 52  LEU B CB  
4506 C CG  . LEU B 52  ? 0.1993 0.1468 0.1864 0.0251  -0.0272 -0.0041 52  LEU B CG  
4507 C CD1 . LEU B 52  ? 0.2050 0.1606 0.1995 0.0236  -0.0301 -0.0051 52  LEU B CD1 
4508 C CD2 . LEU B 52  ? 0.1991 0.1406 0.1773 0.0236  -0.0261 -0.0066 52  LEU B CD2 
4509 N N   . ASN B 53  ? 0.1648 0.1102 0.1618 0.0239  -0.0129 -0.0047 53  ASN B N   
4510 C CA  . ASN B 53  ? 0.1496 0.0972 0.1525 0.0207  -0.0097 -0.0064 53  ASN B CA  
4511 C C   . ASN B 53  ? 0.1449 0.1004 0.1537 0.0201  -0.0101 -0.0105 53  ASN B C   
4512 O O   . ASN B 53  ? 0.1442 0.1032 0.1516 0.0223  -0.0117 -0.0111 53  ASN B O   
4513 C CB  . ASN B 53  ? 0.1459 0.0974 0.1465 0.0181  -0.0059 -0.0051 53  ASN B CB  
4514 C CG  . ASN B 53  ? 0.1502 0.0954 0.1432 0.0189  -0.0052 -0.0004 53  ASN B CG  
4515 O OD1 . ASN B 53  ? 0.1684 0.1054 0.1605 0.0170  -0.0042 0.0026  53  ASN B OD1 
4516 N ND2 . ASN B 53  ? 0.1645 0.1118 0.1505 0.0222  -0.0057 0.0004  53  ASN B ND2 
4517 N N   . PHE B 54  ? 0.1415 0.0985 0.1556 0.0168  -0.0083 -0.0133 54  PHE B N   
4518 C CA  . PHE B 54  ? 0.1640 0.1293 0.1832 0.0162  -0.0088 -0.0174 54  PHE B CA  
4519 C C   . PHE B 54  ? 0.1777 0.1503 0.2001 0.0107  -0.0062 -0.0207 54  PHE B C   
4520 O O   . PHE B 54  ? 0.1779 0.1445 0.2000 0.0060  -0.0039 -0.0212 54  PHE B O   
4521 C CB  . PHE B 54  ? 0.1215 0.0826 0.1436 0.0180  -0.0103 -0.0193 54  PHE B CB  
4522 C CG  . PHE B 54  ? 0.1547 0.1136 0.1749 0.0221  -0.0134 -0.0162 54  PHE B CG  
4523 C CD1 . PHE B 54  ? 0.1997 0.1505 0.2170 0.0244  -0.0143 -0.0127 54  PHE B CD1 
4524 C CD2 . PHE B 54  ? 0.1647 0.1304 0.1852 0.0229  -0.0154 -0.0163 54  PHE B CD2 
4525 C CE1 . PHE B 54  ? 0.1740 0.1267 0.1894 0.0270  -0.0179 -0.0101 54  PHE B CE1 
4526 C CE2 . PHE B 54  ? 0.1661 0.1309 0.1844 0.0242  -0.0186 -0.0139 54  PHE B CE2 
4527 C CZ  . PHE B 54  ? 0.1651 0.1250 0.1814 0.0260  -0.0200 -0.0113 54  PHE B CZ  
4528 N N   . ASN B 55  ? 0.1448 0.1305 0.1699 0.0109  -0.0066 -0.0228 55  ASN B N   
4529 C CA  . ASN B 55  ? 0.1539 0.1510 0.1828 0.0053  -0.0051 -0.0270 55  ASN B CA  
4530 C C   . ASN B 55  ? 0.1333 0.1330 0.1645 0.0053  -0.0063 -0.0316 55  ASN B C   
4531 O O   . ASN B 55  ? 0.1527 0.1557 0.1838 0.0101  -0.0081 -0.0301 55  ASN B O   
4532 C CB  . ASN B 55  ? 0.1605 0.1757 0.1905 0.0066  -0.0048 -0.0253 55  ASN B CB  
4533 C CG  . ASN B 55  ? 0.1655 0.1968 0.1998 -0.0007 -0.0037 -0.0296 55  ASN B CG  
4534 O OD1 . ASN B 55  ? 0.1726 0.2022 0.2077 -0.0086 -0.0017 -0.0314 55  ASN B OD1 
4535 N ND2 . ASN B 55  ? 0.1213 0.1684 0.1576 0.0010  -0.0052 -0.0310 55  ASN B ND2 
4536 N N   . LEU B 56  ? 0.1466 0.1442 0.1789 -0.0007 -0.0048 -0.0373 56  LEU B N   
4537 C CA  . LEU B 56  ? 0.1937 0.1958 0.2272 -0.0010 -0.0052 -0.0429 56  LEU B CA  
4538 C C   . LEU B 56  ? 0.1723 0.1887 0.2070 -0.0088 -0.0045 -0.0484 56  LEU B C   
4539 O O   . LEU B 56  ? 0.1706 0.1811 0.2043 -0.0169 -0.0025 -0.0519 56  LEU B O   
4540 C CB  . LEU B 56  ? 0.1916 0.1760 0.2234 -0.0001 -0.0038 -0.0464 56  LEU B CB  
4541 C CG  . LEU B 56  ? 0.2317 0.2063 0.2633 0.0079  -0.0050 -0.0416 56  LEU B CG  
4542 C CD1 . LEU B 56  ? 0.2919 0.2495 0.3216 0.0100  -0.0030 -0.0446 56  LEU B CD1 
4543 C CD2 . LEU B 56  ? 0.2550 0.2415 0.2888 0.0125  -0.0071 -0.0404 56  LEU B CD2 
4544 N N   . THR B 57  ? 0.1497 0.1847 0.1857 -0.0073 -0.0061 -0.0493 57  THR B N   
4545 C CA  . THR B 57  ? 0.1430 0.1946 0.1799 -0.0154 -0.0060 -0.0552 57  THR B CA  
4546 C C   . THR B 57  ? 0.1626 0.2050 0.1966 -0.0209 -0.0047 -0.0647 57  THR B C   
4547 O O   . THR B 57  ? 0.1588 0.1902 0.1911 -0.0155 -0.0042 -0.0662 57  THR B O   
4548 C CB  . THR B 57  ? 0.1553 0.2317 0.1936 -0.0115 -0.0083 -0.0527 57  THR B CB  
4549 O OG1 . THR B 57  ? 0.1549 0.2301 0.1913 -0.0063 -0.0090 -0.0533 57  THR B OG1 
4550 C CG2 . THR B 57  ? 0.1439 0.2269 0.1833 -0.0043 -0.0089 -0.0436 57  THR B CG2 
4551 N N   . PRO B 58  ? 0.1489 0.2255 0.1786 -0.0340 -0.0100 -0.0597 58  PRO B N   
4552 C CA  . PRO B 58  ? 0.1670 0.2294 0.1847 -0.0432 -0.0072 -0.0694 58  PRO B CA  
4553 C C   . PRO B 58  ? 0.2160 0.2884 0.2313 -0.0415 -0.0107 -0.0712 58  PRO B C   
4554 O O   . PRO B 58  ? 0.2146 0.2677 0.2202 -0.0406 -0.0075 -0.0769 58  PRO B O   
4555 C CB  . PRO B 58  ? 0.1780 0.2519 0.1943 -0.0604 -0.0056 -0.0749 58  PRO B CB  
4556 C CG  . PRO B 58  ? 0.2132 0.2925 0.2383 -0.0581 -0.0048 -0.0683 58  PRO B CG  
4557 C CD  . PRO B 58  ? 0.1584 0.2497 0.1939 -0.0420 -0.0090 -0.0584 58  PRO B CD  
4558 N N   . VAL B 59  ? 0.1773 0.2801 0.2010 -0.0400 -0.0164 -0.0656 59  VAL B N   
4559 C CA  . VAL B 59  ? 0.1496 0.2636 0.1706 -0.0382 -0.0197 -0.0661 59  VAL B CA  
4560 C C   . VAL B 59  ? 0.1483 0.2446 0.1686 -0.0247 -0.0191 -0.0625 59  VAL B C   
4561 O O   . VAL B 59  ? 0.1598 0.2517 0.1730 -0.0243 -0.0185 -0.0665 59  VAL B O   
4562 C CB  . VAL B 59  ? 0.1853 0.3376 0.2157 -0.0385 -0.0256 -0.0584 59  VAL B CB  
4563 C CG1 . VAL B 59  ? 0.1373 0.2968 0.1809 -0.0254 -0.0267 -0.0461 59  VAL B CG1 
4564 C CG2 . VAL B 59  ? 0.1708 0.3368 0.1968 -0.0381 -0.0288 -0.0585 59  VAL B CG2 
4565 N N   . LEU B 60  ? 0.1325 0.2190 0.1591 -0.0145 -0.0186 -0.0559 60  LEU B N   
4566 C CA  . LEU B 60  ? 0.1365 0.2073 0.1615 -0.0045 -0.0179 -0.0537 60  LEU B CA  
4567 C C   . LEU B 60  ? 0.1940 0.2409 0.2093 -0.0054 -0.0131 -0.0606 60  LEU B C   
4568 O O   . LEU B 60  ? 0.1651 0.2067 0.1761 -0.0014 -0.0123 -0.0622 60  LEU B O   
4569 C CB  . LEU B 60  ? 0.1183 0.1844 0.1503 0.0041  -0.0182 -0.0465 60  LEU B CB  
4570 C CG  . LEU B 60  ? 0.1223 0.1741 0.1525 0.0120  -0.0176 -0.0448 60  LEU B CG  
4571 C CD1 . LEU B 60  ? 0.1578 0.2183 0.1884 0.0149  -0.0198 -0.0428 60  LEU B CD1 
4572 C CD2 . LEU B 60  ? 0.1095 0.1566 0.1442 0.0174  -0.0173 -0.0398 60  LEU B CD2 
4573 N N   . ILE B 61  ? 0.1895 0.2223 0.2010 -0.0103 -0.0091 -0.0641 61  ILE B N   
4574 C CA  . ILE B 61  ? 0.2346 0.2419 0.2365 -0.0094 -0.0029 -0.0690 61  ILE B CA  
4575 C C   . ILE B 61  ? 0.2145 0.2190 0.2074 -0.0145 -0.0002 -0.0772 61  ILE B C   
4576 O O   . ILE B 61  ? 0.2172 0.2081 0.2050 -0.0075 0.0035  -0.0785 61  ILE B O   
4577 C CB  . ILE B 61  ? 0.2187 0.2106 0.2171 -0.0154 0.0020  -0.0709 61  ILE B CB  
4578 C CG1 . ILE B 61  ? 0.1994 0.1917 0.2047 -0.0087 0.0004  -0.0630 61  ILE B CG1 
4579 C CG2 . ILE B 61  ? 0.2603 0.2234 0.2470 -0.0149 0.0103  -0.0760 61  ILE B CG2 
4580 C CD1 . ILE B 61  ? 0.2063 0.1867 0.2086 -0.0155 0.0052  -0.0637 61  ILE B CD1 
4581 N N   . ASP B 62  ? 0.1942 0.2140 0.1849 -0.0268 -0.0018 -0.0828 62  ASP B N   
4582 C CA  . ASP B 62  ? 0.2058 0.2250 0.1859 -0.0337 0.0008  -0.0921 62  ASP B CA  
4583 C C   . ASP B 62  ? 0.2093 0.2355 0.1904 -0.0237 -0.0012 -0.0890 62  ASP B C   
4584 O O   . ASP B 62  ? 0.2281 0.2410 0.1997 -0.0221 0.0042  -0.0952 62  ASP B O   
4585 C CB  . ASP B 62  ? 0.2116 0.2567 0.1911 -0.0486 -0.0031 -0.0964 62  ASP B CB  
4586 C CG  . ASP B 62  ? 0.3646 0.4014 0.3389 -0.0634 0.0009  -0.1035 62  ASP B CG  
4587 O OD1 . ASP B 62  ? 0.3730 0.3777 0.3395 -0.0635 0.0090  -0.1078 62  ASP B OD1 
4588 O OD2 . ASP B 62  ? 0.3290 0.3926 0.3071 -0.0751 -0.0035 -0.1041 62  ASP B OD2 
4589 N N   . GLN B 63  ? 0.1703 0.2171 0.1625 -0.0170 -0.0081 -0.0794 63  GLN B N   
4590 C CA  . GLN B 63  ? 0.1793 0.2349 0.1729 -0.0093 -0.0102 -0.0756 63  GLN B CA  
4591 C C   . GLN B 63  ? 0.1673 0.2051 0.1614 0.0021  -0.0068 -0.0729 63  GLN B C   
4592 O O   . GLN B 63  ? 0.1903 0.2272 0.1806 0.0065  -0.0044 -0.0745 63  GLN B O   
4593 C CB  . GLN B 63  ? 0.1721 0.2509 0.1767 -0.0059 -0.0170 -0.0655 63  GLN B CB  
4594 C CG  . GLN B 63  ? 0.1644 0.2690 0.1697 -0.0148 -0.0210 -0.0654 63  GLN B CG  
4595 C CD  . GLN B 63  ? 0.1945 0.3186 0.2114 -0.0082 -0.0260 -0.0531 63  GLN B CD  
4596 O OE1 . GLN B 63  ? 0.2381 0.3703 0.2568 -0.0024 -0.0277 -0.0470 63  GLN B OE1 
4597 N NE2 . GLN B 63  ? 0.1420 0.2725 0.1665 -0.0087 -0.0273 -0.0489 63  GLN B NE2 
4598 N N   . ILE B 64  ? 0.1613 0.1884 0.1605 0.0071  -0.0066 -0.0682 64  ILE B N   
4599 C CA  . ILE B 64  ? 0.1804 0.1948 0.1799 0.0174  -0.0038 -0.0650 64  ILE B CA  
4600 C C   . ILE B 64  ? 0.2440 0.2399 0.2333 0.0188  0.0043  -0.0717 64  ILE B C   
4601 O O   . ILE B 64  ? 0.2271 0.2214 0.2155 0.0271  0.0072  -0.0706 64  ILE B O   
4602 C CB  . ILE B 64  ? 0.1986 0.2058 0.2030 0.0208  -0.0048 -0.0595 64  ILE B CB  
4603 C CG1 . ILE B 64  ? 0.1740 0.1967 0.1875 0.0212  -0.0110 -0.0531 64  ILE B CG1 
4604 C CG2 . ILE B 64  ? 0.1949 0.1915 0.1984 0.0309  -0.0015 -0.0559 64  ILE B CG2 
4605 C CD1 . ILE B 64  ? 0.1914 0.2082 0.2081 0.0229  -0.0116 -0.0493 64  ILE B CD1 
4606 N N   . GLN B 65  ? 0.2318 0.2134 0.2131 0.0105  0.0091  -0.0790 65  GLN B N   
4607 C CA  . GLN B 65  ? 0.2659 0.2244 0.2354 0.0115  0.0190  -0.0863 65  GLN B CA  
4608 C C   . GLN B 65  ? 0.2904 0.2563 0.2542 0.0113  0.0209  -0.0921 65  GLN B C   
4609 O O   . GLN B 65  ? 0.2902 0.2445 0.2496 0.0208  0.0279  -0.0929 65  GLN B O   
4610 C CB  . GLN B 65  ? 0.3291 0.2705 0.2897 -0.0010 0.0242  -0.0945 65  GLN B CB  
4611 C CG  . GLN B 65  ? 0.3542 0.2845 0.3186 0.0003  0.0246  -0.0885 65  GLN B CG  
4612 C CD  . GLN B 65  ? 0.4625 0.3755 0.4180 -0.0135 0.0306  -0.0962 65  GLN B CD  
4613 O OE1 . GLN B 65  ? 0.4878 0.4141 0.4417 -0.0282 0.0278  -0.1030 65  GLN B OE1 
4614 N NE2 . GLN B 65  ? 0.5869 0.4715 0.5367 -0.0093 0.0392  -0.0945 65  GLN B NE2 
4615 N N   . GLU B 66  ? 0.2650 0.2525 0.2290 0.0017  0.0150  -0.0950 66  GLU B N   
4616 C CA  . GLU B 66  ? 0.3086 0.3049 0.2656 0.0004  0.0170  -0.1007 66  GLU B CA  
4617 C C   . GLU B 66  ? 0.2879 0.2934 0.2520 0.0139  0.0158  -0.0927 66  GLU B C   
4618 O O   . GLU B 66  ? 0.2947 0.2941 0.2522 0.0193  0.0225  -0.0966 66  GLU B O   
4619 C CB  . GLU B 66  ? 0.2934 0.3158 0.2499 -0.0120 0.0100  -0.1031 66  GLU B CB  
4620 C CG  . GLU B 66  ? 0.4563 0.4854 0.4003 -0.0178 0.0134  -0.1124 66  GLU B CG  
4621 C CD  . GLU B 66  ? 0.4938 0.5500 0.4350 -0.0323 0.0070  -0.1155 66  GLU B CD  
4622 O OE1 . GLU B 66  ? 0.3788 0.4476 0.3282 -0.0373 0.0006  -0.1105 66  GLU B OE1 
4623 O OE2 . GLU B 66  ? 0.5533 0.6202 0.4839 -0.0381 0.0085  -0.1224 66  GLU B OE2 
4624 N N   . TYR B 67  ? 0.2203 0.2402 0.1973 0.0189  0.0082  -0.0819 67  TYR B N   
4625 C CA  . TYR B 67  ? 0.2439 0.2729 0.2277 0.0295  0.0074  -0.0746 67  TYR B CA  
4626 C C   . TYR B 67  ? 0.3045 0.3166 0.2872 0.0405  0.0146  -0.0735 67  TYR B C   
4627 O O   . TYR B 67  ? 0.2948 0.3115 0.2778 0.0487  0.0184  -0.0720 67  TYR B O   
4628 C CB  . TYR B 67  ? 0.2125 0.2556 0.2085 0.0309  -0.0007 -0.0645 67  TYR B CB  
4629 C CG  . TYR B 67  ? 0.2259 0.2894 0.2249 0.0253  -0.0066 -0.0615 67  TYR B CG  
4630 C CD1 . TYR B 67  ? 0.1799 0.2579 0.1807 0.0279  -0.0073 -0.0577 67  TYR B CD1 
4631 C CD2 . TYR B 67  ? 0.2464 0.3161 0.2470 0.0181  -0.0108 -0.0611 67  TYR B CD2 
4632 C CE1 . TYR B 67  ? 0.1821 0.2774 0.1851 0.0240  -0.0118 -0.0532 67  TYR B CE1 
4633 C CE2 . TYR B 67  ? 0.2125 0.3019 0.2162 0.0153  -0.0155 -0.0560 67  TYR B CE2 
4634 C CZ  . TYR B 67  ? 0.2243 0.3253 0.2288 0.0184  -0.0159 -0.0518 67  TYR B CZ  
4635 O OH  . TYR B 67  ? 0.2214 0.3410 0.2287 0.0165  -0.0198 -0.0449 67  TYR B OH  
4636 N N   . ALA B 68  ? 0.2599 0.2542 0.2418 0.0416  0.0169  -0.0730 68  ALA B N   
4637 C CA  . ALA B 68  ? 0.2915 0.2713 0.2731 0.0539  0.0236  -0.0692 68  ALA B CA  
4638 C C   . ALA B 68  ? 0.3249 0.2871 0.2953 0.0584  0.0353  -0.0766 68  ALA B C   
4639 O O   . ALA B 68  ? 0.3449 0.3041 0.3167 0.0719  0.0414  -0.0719 68  ALA B O   
4640 C CB  . ALA B 68  ? 0.2580 0.2222 0.2398 0.0535  0.0240  -0.0664 68  ALA B CB  
4641 N N   . GLN B 69  ? 0.3222 0.2734 0.2810 0.0471  0.0391  -0.0881 69  GLN B N   
4642 C CA  . GLN B 69  ? 0.3774 0.3075 0.3222 0.0489  0.0517  -0.0978 69  GLN B CA  
4643 C C   . GLN B 69  ? 0.4200 0.3671 0.3626 0.0506  0.0526  -0.1012 69  GLN B C   
4644 O O   . GLN B 69  ? 0.5038 0.4348 0.4335 0.0519  0.0638  -0.1106 69  GLN B O   
4645 C CB  . GLN B 69  ? 0.4668 0.3774 0.3981 0.0330  0.0559  -0.1104 69  GLN B CB  
4646 C CG  . GLN B 69  ? 0.5396 0.4307 0.4716 0.0305  0.0571  -0.1076 69  GLN B CG  
4647 C CD  . GLN B 69  ? 0.7168 0.6010 0.6399 0.0108  0.0565  -0.1176 69  GLN B CD  
4648 O OE1 . GLN B 69  ? 0.7853 0.6811 0.7018 -0.0011 0.0542  -0.1257 69  GLN B OE1 
4649 N NE2 . GLN B 69  ? 0.7081 0.5778 0.6320 0.0071  0.0571  -0.1145 69  GLN B NE2 
4650 N N   . GLY B 70  ? 0.4150 0.3923 0.3687 0.0504  0.0423  -0.0940 70  GLY B N   
4651 C CA  . GLY B 70  ? 0.4094 0.4047 0.3612 0.0514  0.0430  -0.0959 70  GLY B CA  
4652 C C   . GLY B 70  ? 0.4938 0.4927 0.4330 0.0370  0.0431  -0.1074 70  GLY B C   
4653 O O   . GLY B 70  ? 0.5670 0.5708 0.4979 0.0377  0.0486  -0.1132 70  GLY B O   
4654 N N   . LYS B 71  ? 0.4436 0.4432 0.3811 0.0237  0.0371  -0.1107 71  LYS B N   
4655 C CA  . LYS B 71  ? 0.5156 0.5228 0.4409 0.0083  0.0363  -0.1214 71  LYS B CA  
4656 C C   . LYS B 71  ? 0.4664 0.5066 0.3997 0.0010  0.0238  -0.1146 71  LYS B C   
4657 O O   . LYS B 71  ? 0.5022 0.5564 0.4263 -0.0110 0.0220  -0.1215 71  LYS B O   
4658 C CB  . LYS B 71  ? 0.5745 0.5589 0.4895 -0.0036 0.0406  -0.1318 71  LYS B CB  
4659 C CG  . LYS B 71  ? 0.6645 0.6130 0.5667 0.0009  0.0541  -0.1380 71  LYS B CG  
4660 C CD  . LYS B 71  ? 0.6927 0.6206 0.5866 -0.0125 0.0561  -0.1434 71  LYS B CD  
4661 C CE  . LYS B 71  ? 0.7059 0.6458 0.6098 -0.0206 0.0472  -0.1396 71  LYS B CE  
4662 N NZ  . LYS B 71  ? 0.7282 0.6435 0.6268 -0.0293 0.0515  -0.1423 71  LYS B NZ  
4663 N N   . ALA B 72  ? 0.3399 0.3928 0.2891 0.0078  0.0158  -0.1011 72  ALA B N   
4664 C CA  . ALA B 72  ? 0.3077 0.3877 0.2646 0.0028  0.0057  -0.0932 72  ALA B CA  
4665 C C   . ALA B 72  ? 0.3221 0.4227 0.2788 0.0058  0.0046  -0.0889 72  ALA B C   
4666 O O   . ALA B 72  ? 0.3629 0.4635 0.3258 0.0157  0.0064  -0.0829 72  ALA B O   
4667 C CB  . ALA B 72  ? 0.3284 0.4092 0.3003 0.0084  -0.0004 -0.0817 72  ALA B CB  
4668 N N   . LYS B 73  ? 0.2567 0.3774 0.2063 -0.0034 0.0016  -0.0914 73  LYS B N   
4669 C CA  . LYS B 73  ? 0.2418 0.3849 0.1906 -0.0015 0.0000  -0.0858 73  LYS B CA  
4670 C C   . LYS B 73  ? 0.2746 0.4367 0.2364 0.0001  -0.0088 -0.0708 73  LYS B C   
4671 O O   . LYS B 73  ? 0.2940 0.4751 0.2550 -0.0066 -0.0143 -0.0677 73  LYS B O   
4672 C CB  . LYS B 73  ? 0.3339 0.4893 0.2660 -0.0121 0.0023  -0.0964 73  LYS B CB  
4673 C CG  . LYS B 73  ? 0.4616 0.6277 0.3874 -0.0080 0.0067  -0.0964 73  LYS B CG  
4674 C CD  . LYS B 73  ? 0.5276 0.7206 0.4413 -0.0185 0.0040  -0.0992 73  LYS B CD  
4675 C CE  . LYS B 73  ? 0.6202 0.8223 0.5260 -0.0145 0.0099  -0.1003 73  LYS B CE  
4676 N NZ  . LYS B 73  ? 0.6493 0.8808 0.5529 -0.0208 0.0047  -0.0926 73  LYS B NZ  
4677 N N   . ASP B 74  ? 0.2228 0.3803 0.1962 0.0091  -0.0095 -0.0610 74  ASP B N   
4678 C CA  . ASP B 74  ? 0.2066 0.3730 0.1920 0.0117  -0.0155 -0.0474 74  ASP B CA  
4679 C C   . ASP B 74  ? 0.2894 0.4742 0.2752 0.0134  -0.0160 -0.0384 74  ASP B C   
4680 O O   . ASP B 74  ? 0.2268 0.4096 0.2137 0.0178  -0.0123 -0.0374 74  ASP B O   
4681 C CB  . ASP B 74  ? 0.1923 0.3406 0.1878 0.0179  -0.0151 -0.0440 74  ASP B CB  
4682 C CG  . ASP B 74  ? 0.2534 0.4047 0.2594 0.0200  -0.0194 -0.0322 74  ASP B CG  
4683 O OD1 . ASP B 74  ? 0.2306 0.3951 0.2386 0.0206  -0.0206 -0.0232 74  ASP B OD1 
4684 O OD2 . ASP B 74  ? 0.2525 0.3909 0.2642 0.0213  -0.0206 -0.0318 74  ASP B OD2 
4685 N N   . VAL B 75  ? 0.2340 0.4387 0.2193 0.0104  -0.0203 -0.0308 75  VAL B N   
4686 C CA  . VAL B 75  ? 0.2084 0.4317 0.1914 0.0113  -0.0201 -0.0221 75  VAL B CA  
4687 C C   . VAL B 75  ? 0.2459 0.4630 0.2395 0.0173  -0.0192 -0.0101 75  VAL B C   
4688 O O   . VAL B 75  ? 0.2222 0.4454 0.2145 0.0185  -0.0161 -0.0069 75  VAL B O   
4689 C CB  . VAL B 75  ? 0.2769 0.5258 0.2563 0.0074  -0.0248 -0.0153 75  VAL B CB  
4690 C CG1 . VAL B 75  ? 0.3206 0.5774 0.2882 -0.0018 -0.0256 -0.0291 75  VAL B CG1 
4691 C CG2 . VAL B 75  ? 0.3265 0.5759 0.3174 0.0114  -0.0288 -0.0027 75  VAL B CG2 
4692 N N   . PHE B 76  ? 0.2462 0.4510 0.2497 0.0200  -0.0212 -0.0040 76  PHE B N   
4693 C CA  . PHE B 76  ? 0.2442 0.4402 0.2557 0.0232  -0.0195 0.0053  76  PHE B CA  
4694 C C   . PHE B 76  ? 0.2354 0.4213 0.2485 0.0238  -0.0162 -0.0013 76  PHE B C   
4695 O O   . PHE B 76  ? 0.2407 0.4296 0.2565 0.0238  -0.0138 0.0042  76  PHE B O   
4696 C CB  . PHE B 76  ? 0.2300 0.4126 0.2496 0.0255  -0.0210 0.0115  76  PHE B CB  
4697 C CG  . PHE B 76  ? 0.3401 0.5333 0.3614 0.0280  -0.0222 0.0245  76  PHE B CG  
4698 C CD1 . PHE B 76  ? 0.3826 0.5928 0.4010 0.0276  -0.0257 0.0246  76  PHE B CD1 
4699 C CD2 . PHE B 76  ? 0.3585 0.5458 0.3839 0.0306  -0.0191 0.0371  76  PHE B CD2 
4700 C CE1 . PHE B 76  ? 0.4135 0.6380 0.4344 0.0317  -0.0268 0.0387  76  PHE B CE1 
4701 C CE2 . PHE B 76  ? 0.3975 0.5935 0.4243 0.0352  -0.0189 0.0511  76  PHE B CE2 
4702 C CZ  . PHE B 76  ? 0.4567 0.6732 0.4819 0.0367  -0.0230 0.0527  76  PHE B CZ  
4703 N N   . LEU B 77  ? 0.1998 0.3752 0.2113 0.0245  -0.0158 -0.0123 77  LEU B N   
4704 C CA  . LEU B 77  ? 0.2174 0.3860 0.2311 0.0272  -0.0125 -0.0170 77  LEU B CA  
4705 C C   . LEU B 77  ? 0.2469 0.4287 0.2551 0.0282  -0.0081 -0.0195 77  LEU B C   
4706 O O   . LEU B 77  ? 0.2493 0.4353 0.2622 0.0303  -0.0054 -0.0170 77  LEU B O   
4707 C CB  . LEU B 77  ? 0.2424 0.3958 0.2548 0.0290  -0.0120 -0.0266 77  LEU B CB  
4708 C CG  . LEU B 77  ? 0.3457 0.4913 0.3628 0.0337  -0.0095 -0.0286 77  LEU B CG  
4709 C CD1 . LEU B 77  ? 0.3013 0.4470 0.3277 0.0325  -0.0119 -0.0204 77  LEU B CD1 
4710 C CD2 . LEU B 77  ? 0.3286 0.4578 0.3431 0.0358  -0.0086 -0.0362 77  LEU B CD2 
4711 N N   . GLU B 78  ? 0.2116 0.4020 0.2095 0.0260  -0.0071 -0.0246 78  GLU B N   
4712 C CA  . GLU B 78  ? 0.2387 0.4428 0.2296 0.0266  -0.0023 -0.0269 78  GLU B CA  
4713 C C   . GLU B 78  ? 0.2198 0.4383 0.2159 0.0259  -0.0023 -0.0146 78  GLU B C   
4714 O O   . GLU B 78  ? 0.2439 0.4712 0.2405 0.0281  0.0024  -0.0142 78  GLU B O   
4715 C CB  . GLU B 78  ? 0.2865 0.4997 0.2638 0.0218  -0.0020 -0.0339 78  GLU B CB  
4716 C CG  . GLU B 78  ? 0.4199 0.6190 0.3876 0.0211  0.0021  -0.0492 78  GLU B CG  
4717 C CD  . GLU B 78  ? 0.6680 0.8770 0.6213 0.0127  0.0015  -0.0571 78  GLU B CD  
4718 O OE1 . GLU B 78  ? 0.7398 0.9700 0.6914 0.0086  -0.0031 -0.0493 78  GLU B OE1 
4719 O OE2 . GLU B 78  ? 0.7547 0.9504 0.6977 0.0097  0.0059  -0.0710 78  GLU B OE2 
4720 N N   . ALA B 79  ? 0.2009 0.4218 0.2008 0.0233  -0.0064 -0.0040 79  ALA B N   
4721 C CA  . ALA B 79  ? 0.1968 0.4272 0.2006 0.0219  -0.0052 0.0085  79  ALA B CA  
4722 C C   . ALA B 79  ? 0.2101 0.4325 0.2241 0.0219  -0.0036 0.0110  79  ALA B C   
4723 O O   . ALA B 79  ? 0.2713 0.5041 0.2876 0.0200  -0.0003 0.0167  79  ALA B O   
4724 C CB  . ALA B 79  ? 0.2119 0.4428 0.2171 0.0208  -0.0085 0.0203  79  ALA B CB  
4725 N N   . ILE B 80  ? 0.1660 0.3721 0.1856 0.0229  -0.0058 0.0069  80  ILE B N   
4726 C CA  . ILE B 80  ? 0.1686 0.3702 0.1968 0.0218  -0.0049 0.0078  80  ILE B CA  
4727 C C   . ILE B 80  ? 0.2034 0.4172 0.2323 0.0254  -0.0011 0.0026  80  ILE B C   
4728 O O   . ILE B 80  ? 0.2289 0.4537 0.2638 0.0231  0.0011  0.0070  80  ILE B O   
4729 C CB  . ILE B 80  ? 0.1494 0.3328 0.1814 0.0225  -0.0081 0.0038  80  ILE B CB  
4730 C CG1 . ILE B 80  ? 0.2501 0.4217 0.2827 0.0200  -0.0104 0.0101  80  ILE B CG1 
4731 C CG2 . ILE B 80  ? 0.1860 0.3693 0.2255 0.0210  -0.0077 0.0032  80  ILE B CG2 
4732 C CD1 . ILE B 80  ? 0.2492 0.4188 0.2851 0.0147  -0.0083 0.0197  80  ILE B CD1 
4733 N N   . ARG B 81  ? 0.1971 0.4086 0.2200 0.0310  0.0007  -0.0069 81  ARG B N   
4734 C CA  . ARG B 81  ? 0.2031 0.4219 0.2272 0.0374  0.0057  -0.0118 81  ARG B CA  
4735 C C   . ARG B 81  ? 0.2292 0.4686 0.2511 0.0377  0.0109  -0.0090 81  ARG B C   
4736 O O   . ARG B 81  ? 0.2234 0.4755 0.2513 0.0419  0.0150  -0.0079 81  ARG B O   
4737 C CB  . ARG B 81  ? 0.2968 0.5022 0.3129 0.0433  0.0083  -0.0228 81  ARG B CB  
4738 C CG  . ARG B 81  ? 0.3841 0.5926 0.4017 0.0527  0.0150  -0.0269 81  ARG B CG  
4739 C CD  . ARG B 81  ? 0.4571 0.6506 0.4630 0.0578  0.0208  -0.0383 81  ARG B CD  
4740 N NE  . ARG B 81  ? 0.5805 0.7530 0.5832 0.0551  0.0169  -0.0429 81  ARG B NE  
4741 C CZ  . ARG B 81  ? 0.7379 0.8966 0.7453 0.0600  0.0168  -0.0435 81  ARG B CZ  
4742 N NH1 . ARG B 81  ? 0.7239 0.8892 0.7395 0.0686  0.0198  -0.0391 81  ARG B NH1 
4743 N NH2 . ARG B 81  ? 0.8347 0.9756 0.8386 0.0565  0.0136  -0.0475 81  ARG B NH2 
4744 N N   . LYS B 82  ? 0.2016 0.4475 0.2152 0.0338  0.0109  -0.0070 82  LYS B N   
4745 C CA  . LYS B 82  ? 0.2333 0.4990 0.2425 0.0342  0.0165  -0.0052 82  LYS B CA  
4746 C C   . LYS B 82  ? 0.1830 0.4642 0.2027 0.0311  0.0179  0.0048  82  LYS B C   
4747 O O   . LYS B 82  ? 0.1883 0.4647 0.2154 0.0248  0.0140  0.0125  82  LYS B O   
4748 C CB  . LYS B 82  ? 0.2631 0.5354 0.2616 0.0294  0.0150  -0.0024 82  LYS B CB  
4749 C CG  . LYS B 82  ? 0.3411 0.6072 0.3266 0.0299  0.0148  -0.0132 82  LYS B CG  
4750 C CD  . LYS B 82  ? 0.2587 0.5373 0.2361 0.0242  0.0116  -0.0067 82  LYS B CD  
4751 C CE  . LYS B 82  ? 0.4022 0.6801 0.3658 0.0217  0.0105  -0.0174 82  LYS B CE  
4752 N NZ  . LYS B 82  ? 0.4261 0.7252 0.3810 0.0170  0.0086  -0.0101 82  LYS B NZ  
4753 N N   . ASP B 83  ? 0.1750 0.4751 0.1944 0.0345  0.0245  0.0045  83  ASP B N   
4754 C CA  . ASP B 83  ? 0.1987 0.5181 0.2259 0.0289  0.0264  0.0149  83  ASP B CA  
4755 C C   . ASP B 83  ? 0.1810 0.5000 0.2028 0.0205  0.0242  0.0240  83  ASP B C   
4756 O O   . ASP B 83  ? 0.1827 0.5008 0.1928 0.0216  0.0240  0.0218  83  ASP B O   
4757 C CB  . ASP B 83  ? 0.2223 0.5645 0.2487 0.0348  0.0348  0.0131  83  ASP B CB  
4758 C CG  . ASP B 83  ? 0.3269 0.6924 0.3634 0.0283  0.0372  0.0238  83  ASP B CG  
4759 O OD1 . ASP B 83  ? 0.2187 0.5880 0.2524 0.0194  0.0366  0.0325  83  ASP B OD1 
4760 O OD2 . ASP B 83  ? 0.3472 0.7264 0.3941 0.0320  0.0396  0.0243  83  ASP B OD2 
4761 N N   . PRO B 84  ? 0.1632 0.4823 0.1926 0.0120  0.0228  0.0345  84  PRO B N   
4762 C CA  . PRO B 84  ? 0.2224 0.5369 0.2466 0.0058  0.0218  0.0450  84  PRO B CA  
4763 C C   . PRO B 84  ? 0.2479 0.5819 0.2628 0.0062  0.0263  0.0495  84  PRO B C   
4764 O O   . PRO B 84  ? 0.2787 0.6105 0.2855 0.0051  0.0248  0.0562  84  PRO B O   
4765 C CB  . PRO B 84  ? 0.2809 0.5910 0.3147 -0.0041 0.0223  0.0539  84  PRO B CB  
4766 C CG  . PRO B 84  ? 0.2858 0.5914 0.3287 -0.0033 0.0198  0.0462  84  PRO B CG  
4767 C CD  . PRO B 84  ? 0.2086 0.5295 0.2509 0.0068  0.0221  0.0370  84  PRO B CD  
4768 N N   . ASP B 85  ? 0.1828 0.5380 0.1983 0.0084  0.0321  0.0467  85  ASP B N   
4769 C CA  . ASP B 85  ? 0.1887 0.5631 0.1933 0.0091  0.0368  0.0494  85  ASP B CA  
4770 C C   . ASP B 85  ? 0.2247 0.5954 0.2147 0.0143  0.0350  0.0403  85  ASP B C   
4771 O O   . ASP B 85  ? 0.2046 0.5902 0.1828 0.0133  0.0375  0.0430  85  ASP B O   
4772 C CB  . ASP B 85  ? 0.2283 0.6263 0.2361 0.0120  0.0445  0.0466  85  ASP B CB  
4773 C CG  . ASP B 85  ? 0.3446 0.7524 0.3650 0.0039  0.0461  0.0572  85  ASP B CG  
4774 O OD1 . ASP B 85  ? 0.3967 0.7963 0.4200 -0.0054 0.0443  0.0680  85  ASP B OD1 
4775 O OD2 . ASP B 85  ? 0.3938 0.8132 0.4200 0.0065  0.0487  0.0545  85  ASP B OD2 
4776 N N   . ASP B 86  ? 0.2126 0.5652 0.2024 0.0184  0.0310  0.0296  86  ASP B N   
4777 C CA  . ASP B 86  ? 0.2236 0.5719 0.1996 0.0209  0.0294  0.0193  86  ASP B CA  
4778 C C   . ASP B 86  ? 0.2106 0.5468 0.1849 0.0178  0.0216  0.0239  86  ASP B C   
4779 O O   . ASP B 86  ? 0.2228 0.5587 0.1861 0.0177  0.0192  0.0164  86  ASP B O   
4780 C CB  . ASP B 86  ? 0.2525 0.5888 0.2282 0.0277  0.0321  0.0037  86  ASP B CB  
4781 C CG  . ASP B 86  ? 0.3054 0.6560 0.2798 0.0334  0.0416  -0.0014 86  ASP B CG  
4782 O OD1 . ASP B 86  ? 0.4659 0.8339 0.4322 0.0314  0.0455  0.0014  86  ASP B OD1 
4783 O OD2 . ASP B 86  ? 0.3601 0.7044 0.3420 0.0405  0.0450  -0.0071 86  ASP B OD2 
4784 N N   . LEU B 87  ? 0.1835 0.5109 0.1679 0.0149  0.0183  0.0360  87  LEU B N   
4785 C CA  . LEU B 87  ? 0.1816 0.4980 0.1657 0.0140  0.0122  0.0419  87  LEU B CA  
4786 C C   . LEU B 87  ? 0.1980 0.5321 0.1712 0.0127  0.0114  0.0509  87  LEU B C   
4787 O O   . LEU B 87  ? 0.2010 0.5495 0.1718 0.0107  0.0152  0.0615  87  LEU B O   
4788 C CB  . LEU B 87  ? 0.1773 0.4781 0.1731 0.0115  0.0113  0.0530  87  LEU B CB  
4789 C CG  . LEU B 87  ? 0.1660 0.4476 0.1714 0.0123  0.0093  0.0445  87  LEU B CG  
4790 C CD1 . LEU B 87  ? 0.2105 0.4800 0.2254 0.0070  0.0104  0.0541  87  LEU B CD1 
4791 C CD2 . LEU B 87  ? 0.2197 0.4882 0.2230 0.0154  0.0039  0.0386  87  LEU B CD2 
4792 N N   . GLU B 88  ? 0.2224 0.5573 0.1894 0.0135  0.0062  0.0474  88  GLU B N   
4793 C CA  . GLU B 88  ? 0.2031 0.5573 0.1613 0.0127  0.0037  0.0582  88  GLU B CA  
4794 C C   . GLU B 88  ? 0.2040 0.5503 0.1706 0.0148  0.0027  0.0777  88  GLU B C   
4795 O O   . GLU B 88  ? 0.1963 0.5193 0.1739 0.0161  0.0021  0.0789  88  GLU B O   
4796 C CB  . GLU B 88  ? 0.2403 0.6003 0.1905 0.0117  -0.0019 0.0482  88  GLU B CB  
4797 C CG  . GLU B 88  ? 0.2617 0.6216 0.2021 0.0092  0.0007  0.0272  88  GLU B CG  
4798 C CD  . GLU B 88  ? 0.3614 0.7169 0.2968 0.0063  -0.0042 0.0149  88  GLU B CD  
4799 O OE1 . GLU B 88  ? 0.4649 0.8165 0.3914 0.0031  -0.0009 -0.0025 88  GLU B OE1 
4800 O OE2 . GLU B 88  ? 0.3365 0.6902 0.2784 0.0070  -0.0101 0.0225  88  GLU B OE2 
4801 N N   . LYS B 89  ? 0.2160 0.5813 0.1763 0.0153  0.0033  0.0933  89  LYS B N   
4802 C CA  . LYS B 89  ? 0.2218 0.5785 0.1885 0.0192  0.0037  0.1135  89  LYS B CA  
4803 C C   . LYS B 89  ? 0.2738 0.6167 0.2472 0.0236  -0.0014 0.1127  89  LYS B C   
4804 O O   . LYS B 89  ? 0.2323 0.5511 0.2152 0.0264  0.0007  0.1206  89  LYS B O   
4805 C CB  . LYS B 89  ? 0.2373 0.6160 0.1993 0.0206  0.0043  0.1277  89  LYS B CB  
4806 C CG  . LYS B 89  ? 0.2462 0.6369 0.2039 0.0163  0.0095  0.1287  89  LYS B CG  
4807 C CD  . LYS B 89  ? 0.2623 0.6752 0.2172 0.0173  0.0089  0.1381  89  LYS B CD  
4808 C CE  . LYS B 89  ? 0.2933 0.7158 0.2444 0.0133  0.0144  0.1408  89  LYS B CE  
4809 N NZ  . LYS B 89  ? 0.3536 0.7963 0.3021 0.0146  0.0143  0.1531  89  LYS B NZ  
4810 N N   . GLU B 90  ? 0.2101 0.5673 0.1780 0.0232  -0.0073 0.1021  90  GLU B N   
4811 C CA  . GLU B 90  ? 0.2029 0.5515 0.1772 0.0267  -0.0123 0.1005  90  GLU B CA  
4812 C C   . GLU B 90  ? 0.2147 0.5313 0.1989 0.0263  -0.0113 0.0892  90  GLU B C   
4813 O O   . GLU B 90  ? 0.2535 0.5542 0.2460 0.0305  -0.0124 0.0934  90  GLU B O   
4814 C CB  . GLU B 90  ? 0.3645 0.7302 0.3339 0.0221  -0.0163 0.0864  90  GLU B CB  
4815 C CG  . GLU B 90  ? 0.5760 0.9427 0.5522 0.0246  -0.0199 0.0887  90  GLU B CG  
4816 C CD  . GLU B 90  ? 0.6895 1.0769 0.6597 0.0173  -0.0224 0.0769  90  GLU B CD  
4817 O OE1 . GLU B 90  ? 0.7718 1.1814 0.7426 0.0175  -0.0225 0.0865  90  GLU B OE1 
4818 O OE2 . GLU B 90  ? 0.6648 1.0462 0.6296 0.0110  -0.0239 0.0582  90  GLU B OE2 
4819 N N   . GLU B 91  ? 0.1853 0.4943 0.1684 0.0219  -0.0089 0.0749  91  GLU B N   
4820 C CA  . GLU B 91  ? 0.2136 0.4967 0.2054 0.0215  -0.0083 0.0646  91  GLU B CA  
4821 C C   . GLU B 91  ? 0.1834 0.4468 0.1840 0.0217  -0.0041 0.0751  91  GLU B C   
4822 O O   . GLU B 91  ? 0.1870 0.4286 0.1951 0.0225  -0.0045 0.0729  91  GLU B O   
4823 C CB  . GLU B 91  ? 0.2192 0.5031 0.2072 0.0186  -0.0064 0.0481  91  GLU B CB  
4824 C CG  . GLU B 91  ? 0.2287 0.5203 0.2080 0.0172  -0.0092 0.0335  91  GLU B CG  
4825 C CD  . GLU B 91  ? 0.2677 0.5595 0.2413 0.0161  -0.0048 0.0190  91  GLU B CD  
4826 O OE1 . GLU B 91  ? 0.2161 0.5194 0.1867 0.0158  -0.0002 0.0220  91  GLU B OE1 
4827 O OE2 . GLU B 91  ? 0.2684 0.5484 0.2404 0.0161  -0.0051 0.0052  91  GLU B OE2 
4828 N N   . VAL B 92  ? 0.1862 0.4566 0.1850 0.0197  0.0006  0.0861  92  VAL B N   
4829 C CA  . VAL B 92  ? 0.2601 0.5106 0.2655 0.0176  0.0057  0.0965  92  VAL B CA  
4830 C C   . VAL B 92  ? 0.2136 0.4491 0.2220 0.0233  0.0061  0.1088  92  VAL B C   
4831 O O   . VAL B 92  ? 0.2221 0.4313 0.2365 0.0224  0.0088  0.1093  92  VAL B O   
4832 C CB  . VAL B 92  ? 0.2624 0.5246 0.2644 0.0135  0.0114  0.1070  92  VAL B CB  
4833 C CG1 . VAL B 92  ? 0.2766 0.5154 0.2841 0.0092  0.0177  0.1177  92  VAL B CG1 
4834 C CG2 . VAL B 92  ? 0.1981 0.4753 0.1987 0.0091  0.0123  0.0948  92  VAL B CG2 
4835 N N   . GLU B 93  ? 0.2089 0.4623 0.2128 0.0294  0.0037  0.1187  93  GLU B N   
4836 C CA  . GLU B 93  ? 0.2303 0.4732 0.2380 0.0375  0.0046  0.1321  93  GLU B CA  
4837 C C   . GLU B 93  ? 0.2593 0.4855 0.2733 0.0396  0.0014  0.1211  93  GLU B C   
4838 O O   . GLU B 93  ? 0.2686 0.4700 0.2879 0.0434  0.0055  0.1272  93  GLU B O   
4839 C CB  . GLU B 93  ? 0.2983 0.5718 0.3005 0.0440  0.0012  0.1444  93  GLU B CB  
4840 C CG  . GLU B 93  ? 0.3720 0.6606 0.3675 0.0438  0.0056  0.1601  93  GLU B CG  
4841 C CD  . GLU B 93  ? 0.3986 0.7240 0.3884 0.0462  0.0009  0.1640  93  GLU B CD  
4842 O OE1 . GLU B 93  ? 0.4061 0.7435 0.3982 0.0470  -0.0048 0.1547  93  GLU B OE1 
4843 O OE2 . GLU B 93  ? 0.4108 0.7497 0.3973 0.0448  0.0041  0.1721  93  GLU B OE2 
4844 N N   . LYS B 94  ? 0.2037 0.4417 0.2162 0.0371  -0.0050 0.1049  94  LYS B N   
4845 C CA  . LYS B 94  ? 0.2312 0.4556 0.2491 0.0386  -0.0081 0.0949  94  LYS B CA  
4846 C C   . LYS B 94  ? 0.2130 0.4080 0.2361 0.0347  -0.0047 0.0873  94  LYS B C   
4847 O O   . LYS B 94  ? 0.2628 0.4385 0.2909 0.0374  -0.0039 0.0862  94  LYS B O   
4848 C CB  . LYS B 94  ? 0.3353 0.5765 0.3490 0.0352  -0.0143 0.0791  94  LYS B CB  
4849 C CG  . LYS B 94  ? 0.5339 0.7936 0.5474 0.0391  -0.0193 0.0824  94  LYS B CG  
4850 C CD  . LYS B 94  ? 0.6148 0.9030 0.6186 0.0336  -0.0239 0.0737  94  LYS B CD  
4851 C CE  . LYS B 94  ? 0.6863 0.9942 0.6907 0.0349  -0.0278 0.0773  94  LYS B CE  
4852 N NZ  . LYS B 94  ? 0.7196 1.0144 0.7306 0.0353  -0.0301 0.0693  94  LYS B NZ  
4853 N N   . LEU B 95  ? 0.1733 0.3672 0.1950 0.0280  -0.0026 0.0819  95  LEU B N   
4854 C CA  . LEU B 95  ? 0.2085 0.3805 0.2349 0.0226  0.0000  0.0749  95  LEU B CA  
4855 C C   . LEU B 95  ? 0.2656 0.4138 0.2941 0.0221  0.0065  0.0862  95  LEU B C   
4856 O O   . LEU B 95  ? 0.2348 0.3605 0.2666 0.0201  0.0081  0.0812  95  LEU B O   
4857 C CB  . LEU B 95  ? 0.2057 0.3887 0.2310 0.0161  0.0010  0.0689  95  LEU B CB  
4858 C CG  . LEU B 95  ? 0.4089 0.5788 0.4391 0.0091  0.0028  0.0621  95  LEU B CG  
4859 C CD1 . LEU B 95  ? 0.4252 0.5860 0.4583 0.0108  -0.0014 0.0496  95  LEU B CD1 
4860 C CD2 . LEU B 95  ? 0.4792 0.6675 0.5093 0.0044  0.0043  0.0594  95  LEU B CD2 
4861 N N   . ILE B 96  ? 0.2166 0.3683 0.2424 0.0239  0.0111  0.1016  96  ILE B N   
4862 C CA  . ILE B 96  ? 0.2332 0.3580 0.2595 0.0243  0.0194  0.1135  96  ILE B CA  
4863 C C   . ILE B 96  ? 0.2646 0.3761 0.2936 0.0344  0.0199  0.1174  96  ILE B C   
4864 O O   . ILE B 96  ? 0.2631 0.3451 0.2935 0.0335  0.0255  0.1164  96  ILE B O   
4865 C CB  . ILE B 96  ? 0.2689 0.4007 0.2911 0.0251  0.0250  0.1309  96  ILE B CB  
4866 C CG1 . ILE B 96  ? 0.2901 0.4299 0.3109 0.0133  0.0268  0.1271  96  ILE B CG1 
4867 C CG2 . ILE B 96  ? 0.2931 0.3950 0.3148 0.0293  0.0349  0.1459  96  ILE B CG2 
4868 C CD1 . ILE B 96  ? 0.2902 0.4425 0.3060 0.0132  0.0317  0.1433  96  ILE B CD1 
4869 N N   . GLU B 97  ? 0.2260 0.3602 0.2553 0.0434  0.0146  0.1215  97  GLU B N   
4870 C CA  . GLU B 97  ? 0.2883 0.4154 0.3216 0.0536  0.0149  0.1258  97  GLU B CA  
4871 C C   . GLU B 97  ? 0.2455 0.3559 0.2822 0.0503  0.0127  0.1095  97  GLU B C   
4872 O O   . GLU B 97  ? 0.2786 0.3662 0.3178 0.0552  0.0177  0.1117  97  GLU B O   
4873 C CB  . GLU B 97  ? 0.3380 0.4999 0.3714 0.0611  0.0081  0.1313  97  GLU B CB  
4874 C CG  . GLU B 97  ? 0.5267 0.6889 0.5659 0.0714  0.0075  0.1356  97  GLU B CG  
4875 C CD  . GLU B 97  ? 0.7194 0.9214 0.7590 0.0773  0.0006  0.1427  97  GLU B CD  
4876 O OE1 . GLU B 97  ? 0.7673 0.9950 0.8011 0.0708  -0.0052 0.1379  97  GLU B OE1 
4877 O OE2 . GLU B 97  ? 0.7678 0.9766 0.8131 0.0880  0.0014  0.1530  97  GLU B OE2 
4878 N N   . PHE B 98  ? 0.2134 0.3345 0.2495 0.0428  0.0061  0.0936  98  PHE B N   
4879 C CA  . PHE B 98  ? 0.2108 0.3180 0.2494 0.0397  0.0039  0.0791  98  PHE B CA  
4880 C C   . PHE B 98  ? 0.2647 0.3422 0.3029 0.0332  0.0102  0.0763  98  PHE B C   
4881 O O   . PHE B 98  ? 0.2332 0.2913 0.2727 0.0340  0.0123  0.0713  98  PHE B O   
4882 C CB  . PHE B 98  ? 0.1965 0.3208 0.2337 0.0343  -0.0031 0.0649  98  PHE B CB  
4883 C CG  . PHE B 98  ? 0.2207 0.3357 0.2602 0.0330  -0.0062 0.0517  98  PHE B CG  
4884 C CD1 . PHE B 98  ? 0.2521 0.3732 0.2933 0.0381  -0.0096 0.0494  98  PHE B CD1 
4885 C CD2 . PHE B 98  ? 0.1964 0.2990 0.2363 0.0264  -0.0056 0.0425  98  PHE B CD2 
4886 C CE1 . PHE B 98  ? 0.1918 0.3039 0.2344 0.0367  -0.0118 0.0383  98  PHE B CE1 
4887 C CE2 . PHE B 98  ? 0.2379 0.3328 0.2791 0.0258  -0.0083 0.0319  98  PHE B CE2 
4888 C CZ  . PHE B 98  ? 0.2276 0.3257 0.2699 0.0311  -0.0110 0.0298  98  PHE B CZ  
4889 N N   . THR B 99  ? 0.2687 0.3437 0.3045 0.0255  0.0138  0.0792  99  THR B N   
4890 C CA  . THR B 99  ? 0.2634 0.3116 0.2977 0.0164  0.0204  0.0767  99  THR B CA  
4891 C C   . THR B 99  ? 0.2968 0.3162 0.3294 0.0221  0.0296  0.0864  99  THR B C   
4892 O O   . THR B 99  ? 0.3180 0.3122 0.3491 0.0185  0.0338  0.0796  99  THR B O   
4893 C CB  . THR B 99  ? 0.2682 0.3226 0.3005 0.0065  0.0230  0.0800  99  THR B CB  
4894 O OG1 . THR B 99  ? 0.2145 0.2965 0.2487 0.0039  0.0157  0.0716  99  THR B OG1 
4895 C CG2 . THR B 99  ? 0.3192 0.3494 0.3495 -0.0066 0.0292  0.0753  99  THR B CG2 
4896 N N   . LYS B 100 ? 0.2767 0.2998 0.3089 0.0317  0.0335  0.1027  100 LYS B N   
4897 C CA  . LYS B 100 ? 0.3164 0.3111 0.3472 0.0398  0.0442  0.1144  100 LYS B CA  
4898 C C   . LYS B 100 ? 0.3222 0.3089 0.3562 0.0490  0.0437  0.1098  100 LYS B C   
4899 O O   . LYS B 100 ? 0.3907 0.3453 0.4224 0.0518  0.0535  0.1115  100 LYS B O   
4900 C CB  . LYS B 100 ? 0.3110 0.3179 0.3418 0.0508  0.0475  0.1350  100 LYS B CB  
4901 C CG  . LYS B 100 ? 0.4783 0.4731 0.5038 0.0435  0.0554  0.1448  100 LYS B CG  
4902 C CD  . LYS B 100 ? 0.5691 0.5882 0.5943 0.0534  0.0552  0.1639  100 LYS B CD  
4903 C CE  . LYS B 100 ? 0.6213 0.6301 0.6410 0.0454  0.0632  0.1743  100 LYS B CE  
4904 N NZ  . LYS B 100 ? 0.6768 0.7089 0.6952 0.0564  0.0638  0.1951  100 LYS B NZ  
4905 N N   . LEU B 101 ? 0.2823 0.2967 0.3210 0.0535  0.0335  0.1041  101 LEU B N   
4906 C CA  . LEU B 101 ? 0.2667 0.2769 0.3092 0.0613  0.0329  0.0999  101 LEU B CA  
4907 C C   . LEU B 101 ? 0.2837 0.2694 0.3234 0.0522  0.0347  0.0841  101 LEU B C   
4908 O O   . LEU B 101 ? 0.3194 0.2861 0.3592 0.0579  0.0402  0.0828  101 LEU B O   
4909 C CB  . LEU B 101 ? 0.3067 0.3523 0.3537 0.0647  0.0216  0.0958  101 LEU B CB  
4910 C CG  . LEU B 101 ? 0.3139 0.3615 0.3654 0.0704  0.0193  0.0898  101 LEU B CG  
4911 C CD1 . LEU B 101 ? 0.3428 0.3869 0.3987 0.0854  0.0264  0.1052  101 LEU B CD1 
4912 C CD2 . LEU B 101 ? 0.3104 0.3899 0.3643 0.0679  0.0082  0.0819  101 LEU B CD2 
4913 N N   . ASN B 102 ? 0.2726 0.2606 0.3096 0.0386  0.0304  0.0726  102 ASN B N   
4914 C CA  . ASN B 102 ? 0.2926 0.2666 0.3269 0.0289  0.0295  0.0572  102 ASN B CA  
4915 C C   . ASN B 102 ? 0.3294 0.2753 0.3571 0.0170  0.0380  0.0546  102 ASN B C   
4916 O O   . ASN B 102 ? 0.2975 0.2295 0.3214 0.0083  0.0388  0.0426  102 ASN B O   
4917 C CB  . ASN B 102 ? 0.2551 0.2545 0.2915 0.0225  0.0189  0.0469  102 ASN B CB  
4918 C CG  . ASN B 102 ? 0.2947 0.3150 0.3355 0.0310  0.0115  0.0448  102 ASN B CG  
4919 O OD1 . ASN B 102 ? 0.2870 0.3006 0.3290 0.0349  0.0114  0.0404  102 ASN B OD1 
4920 N ND2 . ASN B 102 ? 0.2692 0.3147 0.3116 0.0328  0.0061  0.0477  102 ASN B ND2 
4921 N N   . TYR B 103 ? 0.3473 0.2842 0.3728 0.0162  0.0450  0.0661  103 TYR B N   
4922 C CA  . TYR B 103 ? 0.4564 0.3721 0.4753 0.0015  0.0524  0.0644  103 TYR B CA  
4923 C C   . TYR B 103 ? 0.3936 0.2738 0.4050 -0.0062 0.0610  0.0548  103 TYR B C   
4924 O O   . TYR B 103 ? 0.3798 0.2506 0.3857 -0.0236 0.0628  0.0453  103 TYR B O   
4925 C CB  . TYR B 103 ? 0.5542 0.4626 0.5719 0.0071  0.0605  0.0819  103 TYR B CB  
4926 C CG  . TYR B 103 ? 0.6519 0.5347 0.6625 -0.0066 0.0706  0.0837  103 TYR B CG  
4927 C CD1 . TYR B 103 ? 0.7434 0.6435 0.7543 -0.0197 0.0672  0.0828  103 TYR B CD1 
4928 C CD2 . TYR B 103 ? 0.7570 0.5974 0.7601 -0.0065 0.0848  0.0866  103 TYR B CD2 
4929 C CE1 . TYR B 103 ? 0.8464 0.7239 0.8508 -0.0344 0.0770  0.0845  103 TYR B CE1 
4930 C CE2 . TYR B 103 ? 0.8490 0.6626 0.8442 -0.0210 0.0954  0.0876  103 TYR B CE2 
4931 C CZ  . TYR B 103 ? 0.9222 0.7552 0.9182 -0.0358 0.0910  0.0866  103 TYR B CZ  
4932 O OH  . TYR B 103 ? 1.0122 0.8180 1.0000 -0.0521 0.1023  0.0876  103 TYR B OH  
4933 N N   . GLU B 104 ? 0.4213 0.2833 0.4319 0.0061  0.0668  0.0571  104 GLU B N   
4934 C CA  . GLU B 104 ? 0.4869 0.3104 0.4884 0.0006  0.0780  0.0494  104 GLU B CA  
4935 C C   . GLU B 104 ? 0.4462 0.2744 0.4462 -0.0048 0.0717  0.0328  104 GLU B C   
4936 O O   . GLU B 104 ? 0.4796 0.2782 0.4703 -0.0114 0.0802  0.0237  104 GLU B O   
4937 C CB  . GLU B 104 ? 0.6503 0.4487 0.6511 0.0186  0.0903  0.0621  104 GLU B CB  
4938 C CG  . GLU B 104 ? 0.8443 0.6659 0.8548 0.0376  0.0841  0.0673  104 GLU B CG  
4939 C CD  . GLU B 104 ? 0.9133 0.7769 0.9336 0.0446  0.0720  0.0767  104 GLU B CD  
4940 O OE1 . GLU B 104 ? 0.8899 0.7825 0.9155 0.0436  0.0596  0.0686  104 GLU B OE1 
4941 O OE2 . GLU B 104 ? 0.9628 0.8295 0.9844 0.0507  0.0756  0.0921  104 GLU B OE2 
4942 N N   . LYS B 105 ? 0.3700 0.2327 0.3775 -0.0027 0.0581  0.0285  105 LYS B N   
4943 C CA  . LYS B 105 ? 0.2901 0.1596 0.2964 -0.0066 0.0519  0.0148  105 LYS B CA  
4944 C C   . LYS B 105 ? 0.2968 0.1674 0.2971 -0.0268 0.0493  0.0027  105 LYS B C   
4945 O O   . LYS B 105 ? 0.2931 0.1769 0.2950 -0.0359 0.0465  0.0048  105 LYS B O   
4946 C CB  . LYS B 105 ? 0.2555 0.1598 0.2714 0.0026  0.0393  0.0154  105 LYS B CB  
4947 C CG  . LYS B 105 ? 0.2511 0.1605 0.2735 0.0206  0.0406  0.0266  105 LYS B CG  
4948 C CD  . LYS B 105 ? 0.2730 0.2167 0.3033 0.0264  0.0289  0.0270  105 LYS B CD  
4949 C CE  . LYS B 105 ? 0.2706 0.2242 0.3073 0.0421  0.0298  0.0383  105 LYS B CE  
4950 N NZ  . LYS B 105 ? 0.1950 0.1793 0.2373 0.0443  0.0189  0.0356  105 LYS B NZ  
4951 N N   . PRO B 106 ? 0.3011 0.1605 0.2941 -0.0344 0.0505  -0.0097 106 PRO B N   
4952 C CA  . PRO B 106 ? 0.3565 0.2222 0.3436 -0.0546 0.0472  -0.0210 106 PRO B CA  
4953 C C   . PRO B 106 ? 0.2989 0.2047 0.2946 -0.0572 0.0340  -0.0214 106 PRO B C   
4954 O O   . PRO B 106 ? 0.3567 0.2739 0.3509 -0.0726 0.0318  -0.0250 106 PRO B O   
4955 C CB  . PRO B 106 ? 0.3827 0.2344 0.3609 -0.0581 0.0495  -0.0330 106 PRO B CB  
4956 C CG  . PRO B 106 ? 0.3940 0.2168 0.3701 -0.0434 0.0603  -0.0280 106 PRO B CG  
4957 C CD  . PRO B 106 ? 0.3090 0.1503 0.2981 -0.0257 0.0556  -0.0137 106 PRO B CD  
4958 N N   . ILE B 107 ? 0.2625 0.1904 0.2671 -0.0429 0.0257  -0.0177 107 ILE B N   
4959 C CA  . ILE B 107 ? 0.2685 0.2306 0.2804 -0.0438 0.0154  -0.0175 107 ILE B CA  
4960 C C   . ILE B 107 ? 0.2774 0.2511 0.2942 -0.0450 0.0155  -0.0091 107 ILE B C   
4961 O O   . ILE B 107 ? 0.3124 0.3135 0.3346 -0.0474 0.0089  -0.0091 107 ILE B O   
4962 C CB  . ILE B 107 ? 0.2981 0.2763 0.3162 -0.0295 0.0082  -0.0169 107 ILE B CB  
4963 C CG1 . ILE B 107 ? 0.2618 0.2365 0.2844 -0.0153 0.0102  -0.0078 107 ILE B CG1 
4964 C CG2 . ILE B 107 ? 0.3205 0.2902 0.3336 -0.0293 0.0078  -0.0249 107 ILE B CG2 
4965 C CD1 . ILE B 107 ? 0.2302 0.2250 0.2589 -0.0047 0.0027  -0.0074 107 ILE B CD1 
4966 N N   . TYR B 108 ? 0.2781 0.2322 0.2931 -0.0424 0.0237  -0.0009 108 TYR B N   
4967 C CA  . TYR B 108 ? 0.2758 0.2384 0.2936 -0.0451 0.0253  0.0079  108 TYR B CA  
4968 C C   . TYR B 108 ? 0.3317 0.2772 0.3428 -0.0627 0.0332  0.0065  108 TYR B C   
4969 O O   . TYR B 108 ? 0.3746 0.3209 0.3866 -0.0660 0.0370  0.0150  108 TYR B O   
4970 C CB  . TYR B 108 ? 0.2753 0.2313 0.2956 -0.0301 0.0290  0.0204  108 TYR B CB  
4971 C CG  . TYR B 108 ? 0.2658 0.2509 0.2935 -0.0179 0.0203  0.0239  108 TYR B CG  
4972 C CD1 . TYR B 108 ? 0.2209 0.2135 0.2511 -0.0092 0.0145  0.0187  108 TYR B CD1 
4973 C CD2 . TYR B 108 ? 0.2457 0.2499 0.2766 -0.0163 0.0186  0.0317  108 TYR B CD2 
4974 C CE1 . TYR B 108 ? 0.2719 0.2882 0.3071 -0.0004 0.0077  0.0203  108 TYR B CE1 
4975 C CE2 . TYR B 108 ? 0.2351 0.2636 0.2704 -0.0070 0.0117  0.0329  108 TYR B CE2 
4976 C CZ  . TYR B 108 ? 0.2438 0.2773 0.2809 0.0005  0.0064  0.0268  108 TYR B CZ  
4977 O OH  . TYR B 108 ? 0.2305 0.2856 0.2703 0.0078  0.0006  0.0268  108 TYR B OH  
4978 N N   . ARG B 109 ? 0.3607 0.2916 0.3643 -0.0757 0.0358  -0.0043 109 ARG B N   
4979 C CA  . ARG B 109 ? 0.4331 0.3434 0.4279 -0.0953 0.0446  -0.0076 109 ARG B CA  
4980 C C   . ARG B 109 ? 0.4633 0.4053 0.4629 -0.1100 0.0388  -0.0087 109 ARG B C   
4981 O O   . ARG B 109 ? 0.4910 0.4471 0.4884 -0.1253 0.0349  -0.0185 109 ARG B O   
4982 C CB  . ARG B 109 ? 0.4573 0.3433 0.4407 -0.1060 0.0494  -0.0205 109 ARG B CB  
4983 C CG  . ARG B 109 ? 0.6397 0.4885 0.6107 -0.1228 0.0633  -0.0232 109 ARG B CG  
4984 C CD  . ARG B 109 ? 0.8088 0.6143 0.7702 -0.1141 0.0751  -0.0248 109 ARG B CD  
4985 N NE  . ARG B 109 ? 0.8304 0.6342 0.7849 -0.1188 0.0725  -0.0389 109 ARG B NE  
4986 C CZ  . ARG B 109 ? 0.9117 0.6924 0.8616 -0.1062 0.0782  -0.0412 109 ARG B CZ  
4987 N NH1 . ARG B 109 ? 0.9183 0.6774 0.8709 -0.0873 0.0864  -0.0296 109 ARG B NH1 
4988 N NH2 . ARG B 109 ? 0.9640 0.7457 0.9067 -0.1121 0.0757  -0.0543 109 ARG B NH2 
4989 N N   . PHE B 110 ? 0.3516 0.3073 0.3577 -0.1054 0.0386  0.0023  110 PHE B N   
4990 C CA  . PHE B 110 ? 0.4038 0.3874 0.4147 -0.1187 0.0358  0.0037  110 PHE B CA  
4991 C C   . PHE B 110 ? 0.3932 0.3557 0.3998 -0.1269 0.0467  0.0125  110 PHE B C   
4992 O O   . PHE B 110 ? 0.4309 0.3827 0.4385 -0.1127 0.0507  0.0241  110 PHE B O   
4993 C CB  . PHE B 110 ? 0.4508 0.4735 0.4734 -0.1051 0.0262  0.0089  110 PHE B CB  
4994 C CG  . PHE B 110 ? 0.3831 0.4260 0.4100 -0.0964 0.0165  0.0018  110 PHE B CG  
4995 C CD1 . PHE B 110 ? 0.3763 0.4464 0.4064 -0.1067 0.0105  -0.0049 110 PHE B CD1 
4996 C CD2 . PHE B 110 ? 0.4115 0.4482 0.4396 -0.0780 0.0137  0.0029  110 PHE B CD2 
4997 C CE1 . PHE B 110 ? 0.3860 0.4735 0.4197 -0.0973 0.0025  -0.0096 110 PHE B CE1 
4998 C CE2 . PHE B 110 ? 0.3636 0.4162 0.3949 -0.0704 0.0059  -0.0030 110 PHE B CE2 
4999 C CZ  . PHE B 110 ? 0.3759 0.4526 0.4098 -0.0794 0.0006  -0.0088 110 PHE B CZ  
5000 N N   . GLU B 111 ? 0.4374 0.3960 0.4389 -0.1503 0.0516  0.0077  111 GLU B N   
5001 C CA  . GLU B 111 ? 0.4828 0.4207 0.4797 -0.1604 0.0629  0.0164  111 GLU B CA  
5002 C C   . GLU B 111 ? 0.4563 0.4207 0.4626 -0.1496 0.0600  0.0301  111 GLU B C   
5003 O O   . GLU B 111 ? 0.4717 0.4156 0.4747 -0.1457 0.0689  0.0421  111 GLU B O   
5004 C CB  . GLU B 111 ? 0.5776 0.5161 0.5689 -0.1904 0.0668  0.0078  111 GLU B CB  
5005 C CG  . GLU B 111 ? 0.7165 0.7027 0.7157 -0.2003 0.0544  -0.0014 111 GLU B CG  
5006 C CD  . GLU B 111 ? 0.8212 0.8034 0.8148 -0.2033 0.0498  -0.0154 111 GLU B CD  
5007 O OE1 . GLU B 111 ? 0.7902 0.7658 0.7849 -0.1829 0.0458  -0.0156 111 GLU B OE1 
5008 O OE2 . GLU B 111 ? 0.9011 0.8883 0.8886 -0.2272 0.0502  -0.0261 111 GLU B OE2 
5009 N N   . ARG B 112 ? 0.4103 0.4194 0.4274 -0.1441 0.0486  0.0288  112 ARG B N   
5010 C CA  . ARG B 112 ? 0.4077 0.4426 0.4323 -0.1335 0.0463  0.0402  112 ARG B CA  
5011 C C   . ARG B 112 ? 0.3555 0.3763 0.3791 -0.1111 0.0474  0.0496  112 ARG B C   
5012 O O   . ARG B 112 ? 0.4399 0.4657 0.4642 -0.1054 0.0507  0.0618  112 ARG B O   
5013 C CB  . ARG B 112 ? 0.3887 0.4708 0.4241 -0.1296 0.0351  0.0357  112 ARG B CB  
5014 C CG  . ARG B 112 ? 0.3942 0.5037 0.4361 -0.1179 0.0332  0.0453  112 ARG B CG  
5015 C CD  . ARG B 112 ? 0.4221 0.5384 0.4641 -0.1325 0.0402  0.0534  112 ARG B CD  
5016 N NE  . ARG B 112 ? 0.4225 0.5766 0.4722 -0.1246 0.0369  0.0591  112 ARG B NE  
5017 C CZ  . ARG B 112 ? 0.4429 0.6071 0.4931 -0.1309 0.0427  0.0689  112 ARG B CZ  
5018 N NH1 . ARG B 112 ? 0.4534 0.5907 0.4968 -0.1454 0.0523  0.0749  112 ARG B NH1 
5019 N NH2 . ARG B 112 ? 0.3826 0.5822 0.4391 -0.1226 0.0399  0.0726  112 ARG B NH2 
5020 N N   . ILE B 113 ? 0.3661 0.3721 0.3880 -0.0988 0.0446  0.0449  113 ILE B N   
5021 C CA  . ILE B 113 ? 0.3931 0.3903 0.4148 -0.0784 0.0452  0.0542  113 ILE B CA  
5022 C C   . ILE B 113 ? 0.4538 0.4176 0.4686 -0.0783 0.0577  0.0665  113 ILE B C   
5023 O O   . ILE B 113 ? 0.4559 0.4247 0.4716 -0.0663 0.0593  0.0799  113 ILE B O   
5024 C CB  . ILE B 113 ? 0.3946 0.3842 0.4165 -0.0667 0.0403  0.0465  113 ILE B CB  
5025 C CG1 . ILE B 113 ? 0.3764 0.4000 0.4053 -0.0624 0.0287  0.0382  113 ILE B CG1 
5026 C CG2 . ILE B 113 ? 0.4218 0.4012 0.4434 -0.0479 0.0424  0.0570  113 ILE B CG2 
5027 C CD1 . ILE B 113 ? 0.4225 0.4406 0.4516 -0.0522 0.0239  0.0311  113 ILE B CD1 
5028 N N   . ARG B 114 ? 0.4557 0.3848 0.4625 -0.0919 0.0673  0.0625  114 ARG B N   
5029 C CA  . ARG B 114 ? 0.5482 0.4403 0.5473 -0.0913 0.0814  0.0749  114 ARG B CA  
5030 C C   . ARG B 114 ? 0.5662 0.4693 0.5657 -0.0996 0.0856  0.0863  114 ARG B C   
5031 O O   . ARG B 114 ? 0.6138 0.5015 0.6103 -0.0908 0.0939  0.1023  114 ARG B O   
5032 C CB  . ARG B 114 ? 0.6867 0.5354 0.6750 -0.1058 0.0925  0.0658  114 ARG B CB  
5033 C CG  . ARG B 114 ? 0.8798 0.6856 0.8579 -0.1133 0.1101  0.0764  114 ARG B CG  
5034 C CD  . ARG B 114 ? 0.9935 0.7621 0.9667 -0.0936 0.1202  0.0855  114 ARG B CD  
5035 N NE  . ARG B 114 ? 1.0856 0.8030 1.0473 -0.0977 0.1397  0.0946  114 ARG B NE  
5036 C CZ  . ARG B 114 ? 1.1459 0.8246 1.0997 -0.0901 0.1489  0.0908  114 ARG B CZ  
5037 N NH1 . ARG B 114 ? 1.1201 0.7978 1.0750 -0.0818 0.1450  0.0809  114 ARG B NH1 
5038 N NH2 . ARG B 114 ? 1.2133 0.8600 1.1588 -0.0889 0.1600  0.0955  114 ARG B NH2 
5039 N N   . GLU B 115 ? 0.5722 0.5042 0.5760 -0.1157 0.0802  0.0795  115 GLU B N   
5040 C CA  . GLU B 115 ? 0.6422 0.5908 0.6477 -0.1231 0.0834  0.0903  115 GLU B CA  
5041 C C   . GLU B 115 ? 0.5620 0.5386 0.5729 -0.1030 0.0776  0.1021  115 GLU B C   
5042 O O   . GLU B 115 ? 0.5800 0.5509 0.5880 -0.0987 0.0845  0.1178  115 GLU B O   
5043 C CB  . GLU B 115 ? 0.6923 0.6728 0.7031 -0.1429 0.0780  0.0804  115 GLU B CB  
5044 C CG  . GLU B 115 ? 0.7762 0.7386 0.7817 -0.1654 0.0815  0.0668  115 GLU B CG  
5045 C CD  . GLU B 115 ? 0.8361 0.8398 0.8490 -0.1834 0.0746  0.0588  115 GLU B CD  
5046 O OE1 . GLU B 115 ? 0.8391 0.8823 0.8614 -0.1768 0.0686  0.0645  115 GLU B OE1 
5047 O OE2 . GLU B 115 ? 0.8805 0.8787 0.8896 -0.2040 0.0757  0.0469  115 GLU B OE2 
5048 N N   . LEU B 116 ? 0.4967 0.5038 0.5146 -0.0915 0.0653  0.0946  116 LEU B N   
5049 C CA  . LEU B 116 ? 0.4760 0.5122 0.4977 -0.0753 0.0594  0.1027  116 LEU B CA  
5050 C C   . LEU B 116 ? 0.5118 0.5294 0.5291 -0.0587 0.0638  0.1164  116 LEU B C   
5051 O O   . LEU B 116 ? 0.5451 0.5792 0.5617 -0.0502 0.0640  0.1290  116 LEU B O   
5052 C CB  . LEU B 116 ? 0.4641 0.5284 0.4922 -0.0670 0.0471  0.0903  116 LEU B CB  
5053 C CG  . LEU B 116 ? 0.4260 0.5166 0.4602 -0.0785 0.0417  0.0787  116 LEU B CG  
5054 C CD1 . LEU B 116 ? 0.3890 0.5003 0.4282 -0.0667 0.0314  0.0685  116 LEU B CD1 
5055 C CD2 . LEU B 116 ? 0.4370 0.5543 0.4739 -0.0856 0.0438  0.0853  116 LEU B CD2 
5056 N N   . MET B 117 ? 0.5246 0.5107 0.5389 -0.0532 0.0674  0.1145  117 MET B N   
5057 C CA  . MET B 117 ? 0.5827 0.5523 0.5941 -0.0362 0.0725  0.1291  117 MET B CA  
5058 C C   . MET B 117 ? 0.6416 0.5854 0.6465 -0.0394 0.0863  0.1460  117 MET B C   
5059 O O   . MET B 117 ? 0.7147 0.6529 0.7178 -0.0238 0.0907  0.1626  117 MET B O   
5060 C CB  . MET B 117 ? 0.5694 0.5133 0.5800 -0.0286 0.0737  0.1224  117 MET B CB  
5061 C CG  . MET B 117 ? 0.6280 0.5964 0.6446 -0.0219 0.0607  0.1092  117 MET B CG  
5062 S SD  . MET B 117 ? 0.7111 0.7288 0.7329 -0.0133 0.0492  0.1123  117 MET B SD  
5063 C CE  . MET B 117 ? 0.5874 0.6095 0.6108 0.0076  0.0462  0.1204  117 MET B CE  
5064 N N   . ASN B 118 ? 0.6788 0.6072 0.6799 -0.0594 0.0936  0.1429  118 ASN B N   
5065 C CA  . ASN B 118 ? 0.8050 0.7081 0.7992 -0.0650 0.1077  0.1589  118 ASN B CA  
5066 C C   . ASN B 118 ? 0.8067 0.7427 0.8026 -0.0658 0.1057  0.1709  118 ASN B C   
5067 O O   . ASN B 118 ? 0.8317 0.7532 0.8223 -0.0631 0.1161  0.1894  118 ASN B O   
5068 C CB  . ASN B 118 ? 0.9194 0.7905 0.9074 -0.0893 0.1174  0.1495  118 ASN B CB  
5069 C CG  . ASN B 118 ? 1.0029 0.8260 0.9838 -0.0884 0.1268  0.1439  118 ASN B CG  
5070 O OD1 . ASN B 118 ? 1.0344 0.8423 1.0147 -0.0679 0.1297  0.1523  118 ASN B OD1 
5071 N ND2 . ASN B 118 ? 1.0409 0.8413 1.0160 -0.1111 0.1322  0.1295  118 ASN B ND2 
5072 N N   . LYS B 119 ? 0.7719 0.7509 0.7745 -0.0691 0.0938  0.1613  119 LYS B N   
5073 C CA  . LYS B 119 ? 0.7486 0.7597 0.7522 -0.0719 0.0928  0.1703  119 LYS B CA  
5074 C C   . LYS B 119 ? 0.7562 0.7860 0.7585 -0.0514 0.0898  0.1853  119 LYS B C   
5075 O O   . LYS B 119 ? 0.7105 0.7482 0.7150 -0.0362 0.0822  0.1820  119 LYS B O   
5076 C CB  . LYS B 119 ? 0.7151 0.7650 0.7261 -0.0805 0.0824  0.1548  119 LYS B CB  
5077 C CG  . LYS B 119 ? 0.7156 0.7548 0.7289 -0.1004 0.0834  0.1400  119 LYS B CG  
5078 C CD  . LYS B 119 ? 0.7135 0.7939 0.7344 -0.1107 0.0769  0.1313  119 LYS B CD  
5079 C CE  . LYS B 119 ? 0.7594 0.8327 0.7802 -0.1360 0.0838  0.1282  119 LYS B CE  
5080 N NZ  . LYS B 119 ? 0.7881 0.9011 0.8186 -0.1454 0.0757  0.1157  119 LYS B NZ  
5081 N N   . GLU B 120 ? 0.8202 0.8586 0.8183 -0.0522 0.0959  0.2021  120 GLU B N   
5082 C CA  . GLU B 120 ? 0.8323 0.8906 0.8275 -0.0342 0.0939  0.2184  120 GLU B CA  
5083 C C   . GLU B 120 ? 0.7824 0.8886 0.7808 -0.0289 0.0809  0.2092  120 GLU B C   
5084 O O   . GLU B 120 ? 0.7630 0.8867 0.7604 -0.0136 0.0743  0.2128  120 GLU B O   
5085 C CB  . GLU B 120 ? 0.8988 0.9501 0.8872 -0.0371 0.1055  0.2404  120 GLU B CB  
5086 C CG  . GLU B 120 ? 0.9661 0.9650 0.9493 -0.0458 0.1195  0.2449  120 GLU B CG  
5087 C CD  . GLU B 120 ? 0.9908 0.9825 0.9669 -0.0569 0.1279  0.2537  120 GLU B CD  
5088 O OE1 . GLU B 120 ? 0.9707 0.9994 0.9479 -0.0603 0.1234  0.2549  120 GLU B OE1 
5089 O OE2 . GLU B 120 ? 1.0405 0.9886 1.0092 -0.0624 0.1394  0.2585  120 GLU B OE2 
5090 N N   . LYS B 121 ? 0.7395 0.8674 0.7413 -0.0416 0.0777  0.1972  121 LYS B N   
5091 C CA  . LYS B 121 ? 0.7079 0.8768 0.7118 -0.0371 0.0676  0.1868  121 LYS B CA  
5092 C C   . LYS B 121 ? 0.6082 0.7850 0.6196 -0.0484 0.0634  0.1674  121 LYS B C   
5093 O O   . LYS B 121 ? 0.6240 0.7896 0.6380 -0.0638 0.0691  0.1659  121 LYS B O   
5094 C CB  . LYS B 121 ? 0.7572 0.9558 0.7558 -0.0371 0.0702  0.1990  121 LYS B CB  
5095 C CG  . LYS B 121 ? 0.8132 1.0521 0.8121 -0.0337 0.0621  0.1869  121 LYS B CG  
5096 C CD  . LYS B 121 ? 0.8720 1.1195 0.8690 -0.0196 0.0528  0.1798  121 LYS B CD  
5097 C CE  . LYS B 121 ? 0.8783 1.1551 0.8760 -0.0184 0.0460  0.1622  121 LYS B CE  
5098 N NZ  . LYS B 121 ? 0.8811 1.1900 0.8692 -0.0131 0.0450  0.1672  121 LYS B NZ  
5099 N N   . LEU B 122 ? 0.5354 0.7318 0.5500 -0.0411 0.0539  0.1530  122 LEU B N   
5100 C CA  . LEU B 122 ? 0.4453 0.6501 0.4675 -0.0482 0.0495  0.1357  122 LEU B CA  
5101 C C   . LEU B 122 ? 0.3885 0.6310 0.4124 -0.0488 0.0478  0.1313  122 LEU B C   
5102 O O   . LEU B 122 ? 0.3746 0.6372 0.3933 -0.0388 0.0451  0.1322  122 LEU B O   
5103 C CB  . LEU B 122 ? 0.3935 0.5905 0.4180 -0.0391 0.0415  0.1229  122 LEU B CB  
5104 C CG  . LEU B 122 ? 0.5061 0.6673 0.5291 -0.0364 0.0434  0.1261  122 LEU B CG  
5105 C CD1 . LEU B 122 ? 0.5065 0.6648 0.5319 -0.0272 0.0353  0.1137  122 LEU B CD1 
5106 C CD2 . LEU B 122 ? 0.5215 0.6570 0.5461 -0.0515 0.0500  0.1254  122 LEU B CD2 
5107 N N   . ASN B 123 ? 0.3403 0.5936 0.3711 -0.0610 0.0500  0.1263  123 ASN B N   
5108 C CA  . ASN B 123 ? 0.2969 0.5864 0.3314 -0.0601 0.0489  0.1205  123 ASN B CA  
5109 C C   . ASN B 123 ? 0.2474 0.5441 0.2874 -0.0525 0.0416  0.1043  123 ASN B C   
5110 O O   . ASN B 123 ? 0.2786 0.5535 0.3190 -0.0491 0.0371  0.0980  123 ASN B O   
5111 C CB  . ASN B 123 ? 0.3290 0.6326 0.3695 -0.0760 0.0551  0.1247  123 ASN B CB  
5112 C CG  . ASN B 123 ? 0.3365 0.6249 0.3842 -0.0898 0.0547  0.1185  123 ASN B CG  
5113 O OD1 . ASN B 123 ? 0.3380 0.6190 0.3894 -0.0860 0.0485  0.1071  123 ASN B OD1 
5114 N ND2 . ASN B 123 ? 0.3942 0.6783 0.4430 -0.1073 0.0618  0.1260  123 ASN B ND2 
5115 N N   . ARG B 124 ? 0.2550 0.5820 0.2989 -0.0491 0.0415  0.0980  124 ARG B N   
5116 C CA  . ARG B 124 ? 0.2205 0.5536 0.2682 -0.0394 0.0361  0.0842  124 ARG B CA  
5117 C C   . ARG B 124 ? 0.2165 0.5363 0.2724 -0.0457 0.0324  0.0779  124 ARG B C   
5118 O O   . ARG B 124 ? 0.2288 0.5345 0.2844 -0.0383 0.0271  0.0695  124 ARG B O   
5119 C CB  . ARG B 124 ? 0.2287 0.5957 0.2801 -0.0346 0.0391  0.0802  124 ARG B CB  
5120 C CG  . ARG B 124 ? 0.2443 0.6150 0.2979 -0.0222 0.0355  0.0671  124 ARG B CG  
5121 C CD  . ARG B 124 ? 0.2504 0.6523 0.3076 -0.0154 0.0404  0.0638  124 ARG B CD  
5122 N NE  . ARG B 124 ? 0.2920 0.6924 0.3512 -0.0028 0.0383  0.0524  124 ARG B NE  
5123 C CZ  . ARG B 124 ? 0.3377 0.7396 0.4066 -0.0023 0.0352  0.0491  124 ARG B CZ  
5124 N NH1 . ARG B 124 ? 0.3585 0.7658 0.4358 -0.0153 0.0336  0.0548  124 ARG B NH1 
5125 N NH2 . ARG B 124 ? 0.2764 0.6735 0.3453 0.0104  0.0341  0.0404  124 ARG B NH2 
5126 N N   . GLU B 125 ? 0.2374 0.5629 0.3001 -0.0604 0.0353  0.0815  125 GLU B N   
5127 C CA  . GLU B 125 ? 0.2529 0.5706 0.3223 -0.0683 0.0317  0.0748  125 GLU B CA  
5128 C C   . GLU B 125 ? 0.2254 0.5042 0.2887 -0.0698 0.0298  0.0739  125 GLU B C   
5129 O O   . GLU B 125 ? 0.2017 0.4699 0.2669 -0.0679 0.0248  0.0654  125 GLU B O   
5130 C CB  . GLU B 125 ? 0.2936 0.6279 0.3702 -0.0869 0.0356  0.0788  125 GLU B CB  
5131 C CG  . GLU B 125 ? 0.4454 0.8235 0.5308 -0.0852 0.0378  0.0800  125 GLU B CG  
5132 C CD  . GLU B 125 ? 0.5859 0.9734 0.6648 -0.0782 0.0428  0.0872  125 GLU B CD  
5133 O OE1 . GLU B 125 ? 0.5943 0.9686 0.6668 -0.0861 0.0479  0.0971  125 GLU B OE1 
5134 O OE2 . GLU B 125 ? 0.6111 1.0169 0.6898 -0.0640 0.0418  0.0828  125 GLU B OE2 
5135 N N   . GLU B 126 ? 0.2620 0.5197 0.3175 -0.0718 0.0343  0.0835  126 GLU B N   
5136 C CA  . GLU B 126 ? 0.2288 0.4497 0.2787 -0.0707 0.0340  0.0838  126 GLU B CA  
5137 C C   . GLU B 126 ? 0.2067 0.4224 0.2539 -0.0538 0.0279  0.0784  126 GLU B C   
5138 O O   . GLU B 126 ? 0.2307 0.4253 0.2773 -0.0515 0.0249  0.0726  126 GLU B O   
5139 C CB  . GLU B 126 ? 0.2602 0.4607 0.3031 -0.0755 0.0418  0.0977  126 GLU B CB  
5140 C CG  . GLU B 126 ? 0.2954 0.4904 0.3398 -0.0960 0.0487  0.1012  126 GLU B CG  
5141 C CD  . GLU B 126 ? 0.4021 0.5905 0.4409 -0.1011 0.0578  0.1168  126 GLU B CD  
5142 O OE1 . GLU B 126 ? 0.4157 0.6077 0.4495 -0.0882 0.0583  0.1261  126 GLU B OE1 
5143 O OE2 . GLU B 126 ? 0.4736 0.6541 0.5125 -0.1193 0.0646  0.1199  126 GLU B OE2 
5144 N N   . LEU B 127 ? 0.2431 0.4786 0.2878 -0.0428 0.0264  0.0792  127 LEU B N   
5145 C CA  . LEU B 127 ? 0.2333 0.4654 0.2746 -0.0293 0.0210  0.0728  127 LEU B CA  
5146 C C   . LEU B 127 ? 0.1940 0.4302 0.2409 -0.0261 0.0160  0.0597  127 LEU B C   
5147 O O   . LEU B 127 ? 0.2304 0.4514 0.2760 -0.0201 0.0119  0.0538  127 LEU B O   
5148 C CB  . LEU B 127 ? 0.2220 0.4747 0.2574 -0.0210 0.0214  0.0753  127 LEU B CB  
5149 C CG  . LEU B 127 ? 0.2781 0.5286 0.3062 -0.0203 0.0249  0.0893  127 LEU B CG  
5150 C CD1 . LEU B 127 ? 0.3079 0.5860 0.3295 -0.0155 0.0260  0.0908  127 LEU B CD1 
5151 C CD2 . LEU B 127 ? 0.2867 0.5167 0.3111 -0.0135 0.0220  0.0923  127 LEU B CD2 
5152 N N   . LEU B 128 ? 0.1732 0.4314 0.2267 -0.0295 0.0167  0.0561  128 LEU B N   
5153 C CA  . LEU B 128 ? 0.1718 0.4350 0.2311 -0.0257 0.0126  0.0461  128 LEU B CA  
5154 C C   . LEU B 128 ? 0.1694 0.4108 0.2304 -0.0328 0.0098  0.0431  128 LEU B C   
5155 O O   . LEU B 128 ? 0.1667 0.3992 0.2278 -0.0264 0.0055  0.0357  128 LEU B O   
5156 C CB  . LEU B 128 ? 0.1615 0.4556 0.2291 -0.0284 0.0146  0.0457  128 LEU B CB  
5157 C CG  . LEU B 128 ? 0.1878 0.5018 0.2557 -0.0145 0.0157  0.0408  128 LEU B CG  
5158 C CD1 . LEU B 128 ? 0.2130 0.5606 0.2898 -0.0164 0.0196  0.0435  128 LEU B CD1 
5159 C CD2 . LEU B 128 ? 0.2206 0.5242 0.2887 -0.0045 0.0116  0.0319  128 LEU B CD2 
5160 N N   . ASP B 129 ? 0.1745 0.4054 0.2354 -0.0465 0.0130  0.0483  129 ASP B N   
5161 C CA  . ASP B 129 ? 0.2202 0.4275 0.2802 -0.0545 0.0119  0.0445  129 ASP B CA  
5162 C C   . ASP B 129 ? 0.2219 0.4006 0.2755 -0.0459 0.0111  0.0445  129 ASP B C   
5163 O O   . ASP B 129 ? 0.2417 0.4047 0.2946 -0.0453 0.0083  0.0380  129 ASP B O   
5164 C CB  . ASP B 129 ? 0.2163 0.4150 0.2754 -0.0727 0.0175  0.0494  129 ASP B CB  
5165 C CG  . ASP B 129 ? 0.2757 0.5035 0.3427 -0.0851 0.0170  0.0471  129 ASP B CG  
5166 O OD1 . ASP B 129 ? 0.3199 0.5742 0.3935 -0.0772 0.0124  0.0427  129 ASP B OD1 
5167 O OD2 . ASP B 129 ? 0.3149 0.5397 0.3814 -0.1028 0.0217  0.0501  129 ASP B OD2 
5168 N N   . LEU B 130 ? 0.2074 0.3815 0.2563 -0.0391 0.0135  0.0524  130 LEU B N   
5169 C CA  . LEU B 130 ? 0.2721 0.4253 0.3163 -0.0298 0.0124  0.0536  130 LEU B CA  
5170 C C   . LEU B 130 ? 0.2444 0.4042 0.2896 -0.0192 0.0061  0.0442  130 LEU B C   
5171 O O   . LEU B 130 ? 0.2317 0.3745 0.2762 -0.0161 0.0039  0.0397  130 LEU B O   
5172 C CB  . LEU B 130 ? 0.2938 0.4474 0.3332 -0.0246 0.0159  0.0655  130 LEU B CB  
5173 C CG  . LEU B 130 ? 0.3606 0.4916 0.3965 -0.0169 0.0165  0.0703  130 LEU B CG  
5174 C CD1 . LEU B 130 ? 0.3710 0.4713 0.4062 -0.0245 0.0216  0.0707  130 LEU B CD1 
5175 C CD2 . LEU B 130 ? 0.3923 0.5285 0.4237 -0.0103 0.0193  0.0841  130 LEU B CD2 
5176 N N   . GLN B 131 ? 0.1876 0.3707 0.2338 -0.0138 0.0042  0.0409  131 GLN B N   
5177 C CA  . GLN B 131 ? 0.1787 0.3652 0.2248 -0.0047 -0.0002 0.0316  131 GLN B CA  
5178 C C   . GLN B 131 ? 0.1746 0.3551 0.2251 -0.0069 -0.0029 0.0243  131 GLN B C   
5179 O O   . GLN B 131 ? 0.1855 0.3529 0.2348 -0.0022 -0.0059 0.0191  131 GLN B O   
5180 C CB  . GLN B 131 ? 0.1349 0.3446 0.1804 0.0006  0.0006  0.0286  131 GLN B CB  
5181 C CG  . GLN B 131 ? 0.1408 0.3599 0.1800 0.0030  0.0028  0.0343  131 GLN B CG  
5182 C CD  . GLN B 131 ? 0.1503 0.3921 0.1884 0.0066  0.0055  0.0309  131 GLN B CD  
5183 O OE1 . GLN B 131 ? 0.1545 0.4100 0.1987 0.0038  0.0079  0.0312  131 GLN B OE1 
5184 N NE2 . GLN B 131 ? 0.1686 0.4160 0.1984 0.0124  0.0057  0.0275  131 GLN B NE2 
5185 N N   . THR B 132 ? 0.1816 0.3748 0.2374 -0.0143 -0.0020 0.0242  132 THR B N   
5186 C CA  . THR B 132 ? 0.1285 0.3243 0.1885 -0.0153 -0.0052 0.0178  132 THR B CA  
5187 C C   . THR B 132 ? 0.1696 0.3423 0.2274 -0.0224 -0.0062 0.0159  132 THR B C   
5188 O O   . THR B 132 ? 0.1883 0.3554 0.2462 -0.0195 -0.0096 0.0100  132 THR B O   
5189 C CB  . THR B 132 ? 0.1290 0.3514 0.1961 -0.0214 -0.0044 0.0192  132 THR B CB  
5190 O OG1 . THR B 132 ? 0.1414 0.3837 0.2097 -0.0139 -0.0018 0.0214  132 THR B OG1 
5191 C CG2 . THR B 132 ? 0.1266 0.3583 0.1984 -0.0193 -0.0082 0.0141  132 THR B CG2 
5192 N N   . LEU B 133 ? 0.1535 0.3112 0.2083 -0.0318 -0.0023 0.0208  133 LEU B N   
5193 C CA  . LEU B 133 ? 0.2429 0.3748 0.2939 -0.0380 -0.0012 0.0182  133 LEU B CA  
5194 C C   . LEU B 133 ? 0.2178 0.3314 0.2654 -0.0268 -0.0025 0.0169  133 LEU B C   
5195 O O   . LEU B 133 ? 0.1898 0.2888 0.2354 -0.0274 -0.0037 0.0115  133 LEU B O   
5196 C CB  . LEU B 133 ? 0.1784 0.2942 0.2258 -0.0499 0.0055  0.0241  133 LEU B CB  
5197 C CG  . LEU B 133 ? 0.1996 0.3300 0.2497 -0.0662 0.0069  0.0230  133 LEU B CG  
5198 C CD1 . LEU B 133 ? 0.2380 0.3523 0.2839 -0.0780 0.0150  0.0302  133 LEU B CD1 
5199 C CD2 . LEU B 133 ? 0.2275 0.3553 0.2768 -0.0745 0.0039  0.0139  133 LEU B CD2 
5200 N N   . ASN B 134 ? 0.1872 0.3036 0.2337 -0.0173 -0.0023 0.0218  134 ASN B N   
5201 C CA  . ASN B 134 ? 0.2132 0.3187 0.2576 -0.0075 -0.0043 0.0204  134 ASN B CA  
5202 C C   . ASN B 134 ? 0.2839 0.3955 0.3299 -0.0028 -0.0091 0.0114  134 ASN B C   
5203 O O   . ASN B 134 ? 0.2238 0.3219 0.2685 0.0003  -0.0104 0.0078  134 ASN B O   
5204 C CB  . ASN B 134 ? 0.1978 0.3120 0.2405 0.0002  -0.0041 0.0266  134 ASN B CB  
5205 C CG  . ASN B 134 ? 0.2360 0.3361 0.2763 0.0008  0.0006  0.0371  134 ASN B CG  
5206 O OD1 . ASN B 134 ? 0.2585 0.3435 0.2981 0.0056  0.0014  0.0385  134 ASN B OD1 
5207 N ND2 . ASN B 134 ? 0.2628 0.3679 0.3021 -0.0034 0.0046  0.0454  134 ASN B ND2 
5208 N N   . LEU B 135 ? 0.1950 0.3263 0.2436 -0.0014 -0.0109 0.0086  135 LEU B N   
5209 C CA  . LEU B 135 ? 0.2173 0.3530 0.2672 0.0040  -0.0142 0.0016  135 LEU B CA  
5210 C C   . LEU B 135 ? 0.2120 0.3412 0.2629 -0.0017 -0.0157 -0.0018 135 LEU B C   
5211 O O   . LEU B 135 ? 0.2549 0.3739 0.3041 0.0020  -0.0177 -0.0061 135 LEU B O   
5212 C CB  . LEU B 135 ? 0.2406 0.3984 0.2934 0.0077  -0.0138 0.0009  135 LEU B CB  
5213 C CG  . LEU B 135 ? 0.3104 0.4734 0.3606 0.0178  -0.0132 -0.0026 135 LEU B CG  
5214 C CD1 . LEU B 135 ? 0.2286 0.4110 0.2830 0.0220  -0.0115 -0.0034 135 LEU B CD1 
5215 C CD2 . LEU B 135 ? 0.1765 0.3241 0.2232 0.0232  -0.0150 -0.0081 135 LEU B CD2 
5216 N N   . LEU B 136 ? 0.1873 0.3242 0.2404 -0.0120 -0.0148 -0.0004 136 LEU B N   
5217 C CA  . LEU B 136 ? 0.1662 0.3024 0.2192 -0.0196 -0.0167 -0.0044 136 LEU B CA  
5218 C C   . LEU B 136 ? 0.2171 0.3264 0.2642 -0.0241 -0.0150 -0.0071 136 LEU B C   
5219 O O   . LEU B 136 ? 0.2182 0.3240 0.2630 -0.0275 -0.0169 -0.0121 136 LEU B O   
5220 C CB  . LEU B 136 ? 0.2187 0.3728 0.2751 -0.0321 -0.0160 -0.0026 136 LEU B CB  
5221 C CG  . LEU B 136 ? 0.2270 0.4134 0.2908 -0.0274 -0.0179 -0.0006 136 LEU B CG  
5222 C CD1 . LEU B 136 ? 0.2264 0.4330 0.2944 -0.0410 -0.0164 0.0026  136 LEU B CD1 
5223 C CD2 . LEU B 136 ? 0.2656 0.4630 0.3315 -0.0209 -0.0220 -0.0035 136 LEU B CD2 
5224 N N   . ALA B 137 ? 0.2345 0.3254 0.2786 -0.0234 -0.0108 -0.0033 137 ALA B N   
5225 C CA  . ALA B 137 ? 0.2515 0.3159 0.2903 -0.0250 -0.0076 -0.0051 137 ALA B CA  
5226 C C   . ALA B 137 ? 0.2158 0.2757 0.2539 -0.0163 -0.0108 -0.0097 137 ALA B C   
5227 O O   . ALA B 137 ? 0.2319 0.2753 0.2656 -0.0189 -0.0091 -0.0137 137 ALA B O   
5228 C CB  . ALA B 137 ? 0.2177 0.2662 0.2548 -0.0214 -0.0022 0.0024  137 ALA B CB  
5229 N N   . TRP B 138 ? 0.2033 0.2760 0.2446 -0.0066 -0.0145 -0.0095 138 TRP B N   
5230 C CA  . TRP B 138 ? 0.1902 0.2576 0.2305 0.0009  -0.0167 -0.0132 138 TRP B CA  
5231 C C   . TRP B 138 ? 0.1855 0.2640 0.2265 0.0013  -0.0204 -0.0175 138 TRP B C   
5232 O O   . TRP B 138 ? 0.2335 0.3105 0.2740 0.0083  -0.0220 -0.0197 138 TRP B O   
5233 C CB  . TRP B 138 ? 0.2192 0.2905 0.2609 0.0099  -0.0174 -0.0108 138 TRP B CB  
5234 C CG  . TRP B 138 ? 0.2101 0.2738 0.2515 0.0110  -0.0142 -0.0047 138 TRP B CG  
5235 C CD1 . TRP B 138 ? 0.2463 0.3156 0.2883 0.0091  -0.0120 0.0015  138 TRP B CD1 
5236 C CD2 . TRP B 138 ? 0.1788 0.2292 0.2196 0.0151  -0.0120 -0.0026 138 TRP B CD2 
5237 N NE1 . TRP B 138 ? 0.2304 0.2902 0.2718 0.0124  -0.0088 0.0082  138 TRP B NE1 
5238 C CE2 . TRP B 138 ? 0.1929 0.2418 0.2341 0.0167  -0.0086 0.0060  138 TRP B CE2 
5239 C CE3 . TRP B 138 ? 0.1828 0.2241 0.2229 0.0182  -0.0121 -0.0061 138 TRP B CE3 
5240 C CZ2 . TRP B 138 ? 0.2218 0.2613 0.2636 0.0226  -0.0052 0.0118  138 TRP B CZ2 
5241 C CZ3 . TRP B 138 ? 0.2293 0.2617 0.2703 0.0233  -0.0087 -0.0013 138 TRP B CZ3 
5242 C CH2 . TRP B 138 ? 0.2239 0.2559 0.2661 0.0261  -0.0053 0.0080  138 TRP B CH2 
5243 N N   . CYS B 139 ? 0.1755 0.2663 0.2175 -0.0063 -0.0214 -0.0179 139 CYS B N   
5244 C CA  . CYS B 139 ? 0.1773 0.2831 0.2206 -0.0048 -0.0250 -0.0198 139 CYS B CA  
5245 C C   . CYS B 139 ? 0.2244 0.3179 0.2626 -0.0057 -0.0258 -0.0239 139 CYS B C   
5246 O O   . CYS B 139 ? 0.2016 0.2814 0.2348 -0.0141 -0.0237 -0.0269 139 CYS B O   
5247 C CB  . CYS B 139 ? 0.2250 0.3511 0.2710 -0.0146 -0.0262 -0.0187 139 CYS B CB  
5248 S SG  . CYS B 139 ? 0.2357 0.3902 0.2863 -0.0089 -0.0304 -0.0169 139 CYS B SG  
5249 N N   . GLY B 140 ? 0.1540 0.2510 0.1923 0.0031  -0.0278 -0.0241 140 GLY B N   
5250 C CA  . GLY B 140 ? 0.1350 0.2233 0.1682 0.0025  -0.0286 -0.0272 140 GLY B CA  
5251 C C   . GLY B 140 ? 0.1418 0.2467 0.1732 -0.0041 -0.0317 -0.0277 140 GLY B C   
5252 O O   . GLY B 140 ? 0.1732 0.2995 0.2085 -0.0081 -0.0337 -0.0253 140 GLY B O   
5253 N N   . ARG B 141 ? 0.1669 0.2643 0.1919 -0.0058 -0.0322 -0.0307 141 ARG B N   
5254 C CA  . ARG B 141 ? 0.1760 0.2900 0.1969 -0.0140 -0.0354 -0.0320 141 ARG B CA  
5255 C C   . ARG B 141 ? 0.1602 0.3033 0.1871 -0.0074 -0.0393 -0.0252 141 ARG B C   
5256 O O   . ARG B 141 ? 0.1765 0.3442 0.2050 -0.0156 -0.0424 -0.0241 141 ARG B O   
5257 C CB  . ARG B 141 ? 0.1694 0.2706 0.1819 -0.0143 -0.0347 -0.0356 141 ARG B CB  
5258 C CG  . ARG B 141 ? 0.2109 0.3319 0.2178 -0.0208 -0.0386 -0.0360 141 ARG B CG  
5259 C CD  . ARG B 141 ? 0.1823 0.2879 0.1795 -0.0212 -0.0368 -0.0401 141 ARG B CD  
5260 N NE  . ARG B 141 ? 0.2282 0.3545 0.2186 -0.0273 -0.0407 -0.0401 141 ARG B NE  
5261 C CZ  . ARG B 141 ? 0.2685 0.4085 0.2590 -0.0178 -0.0435 -0.0332 141 ARG B CZ  
5262 N NH1 . ARG B 141 ? 0.2545 0.4174 0.2383 -0.0242 -0.0476 -0.0323 141 ARG B NH1 
5263 N NH2 . ARG B 141 ? 0.2178 0.3488 0.2142 -0.0028 -0.0418 -0.0270 141 ARG B NH2 
5264 N N   . THR B 142 ? 0.1649 0.3062 0.1952 0.0073  -0.0385 -0.0205 142 THR B N   
5265 C CA  . THR B 142 ? 0.1621 0.3281 0.1977 0.0167  -0.0404 -0.0128 142 THR B CA  
5266 C C   . THR B 142 ? 0.1507 0.3394 0.1944 0.0148  -0.0411 -0.0097 142 THR B C   
5267 O O   . THR B 142 ? 0.1903 0.4097 0.2381 0.0133  -0.0444 -0.0048 142 THR B O   
5268 C CB  . THR B 142 ? 0.2117 0.3640 0.2482 0.0325  -0.0369 -0.0093 142 THR B CB  
5269 O OG1 . THR B 142 ? 0.1935 0.3286 0.2229 0.0336  -0.0362 -0.0109 142 THR B OG1 
5270 C CG2 . THR B 142 ? 0.1946 0.3690 0.2366 0.0448  -0.0366 -0.0002 142 THR B CG2 
5271 N N   . LEU B 143 ? 0.1591 0.3360 0.2056 0.0149  -0.0381 -0.0118 143 LEU B N   
5272 C CA  . LEU B 143 ? 0.1751 0.3732 0.2293 0.0142  -0.0378 -0.0084 143 LEU B CA  
5273 C C   . LEU B 143 ? 0.2377 0.4454 0.2917 -0.0035 -0.0396 -0.0114 143 LEU B C   
5274 O O   . LEU B 143 ? 0.2532 0.4858 0.3140 -0.0067 -0.0402 -0.0078 143 LEU B O   
5275 C CB  . LEU B 143 ? 0.1909 0.3746 0.2470 0.0219  -0.0335 -0.0090 143 LEU B CB  
5276 C CG  . LEU B 143 ? 0.1796 0.3584 0.2365 0.0386  -0.0301 -0.0062 143 LEU B CG  
5277 C CD1 . LEU B 143 ? 0.1366 0.3036 0.1935 0.0429  -0.0259 -0.0085 143 LEU B CD1 
5278 C CD2 . LEU B 143 ? 0.1984 0.4053 0.2617 0.0478  -0.0302 0.0014  143 LEU B CD2 
5279 N N   . ARG B 144 ? 0.2318 0.4194 0.2778 -0.0152 -0.0394 -0.0179 144 ARG B N   
5280 C CA  . ARG B 144 ? 0.2589 0.4521 0.3023 -0.0338 -0.0397 -0.0217 144 ARG B CA  
5281 C C   . ARG B 144 ? 0.3418 0.5711 0.3873 -0.0415 -0.0447 -0.0196 144 ARG B C   
5282 O O   . ARG B 144 ? 0.3502 0.5961 0.3971 -0.0564 -0.0453 -0.0207 144 ARG B O   
5283 C CB  . ARG B 144 ? 0.2720 0.4341 0.3048 -0.0432 -0.0369 -0.0294 144 ARG B CB  
5284 C CG  . ARG B 144 ? 0.3019 0.4356 0.3338 -0.0423 -0.0314 -0.0304 144 ARG B CG  
5285 C CD  . ARG B 144 ? 0.3454 0.4484 0.3676 -0.0481 -0.0272 -0.0368 144 ARG B CD  
5286 N NE  . ARG B 144 ? 0.3662 0.4444 0.3882 -0.0451 -0.0216 -0.0355 144 ARG B NE  
5287 C CZ  . ARG B 144 ? 0.3355 0.4003 0.3543 -0.0560 -0.0165 -0.0366 144 ARG B CZ  
5288 N NH1 . ARG B 144 ? 0.3605 0.4340 0.3754 -0.0727 -0.0164 -0.0406 144 ARG B NH1 
5289 N NH2 . ARG B 144 ? 0.3433 0.3874 0.3624 -0.0507 -0.0112 -0.0332 144 ARG B NH2 
5290 N N   . LYS B 145 ? 0.4072 0.6506 0.4531 -0.0315 -0.0480 -0.0156 145 LYS B N   
5291 C CA  . LYS B 145 ? 0.3932 0.6621 0.4388 -0.0342 -0.0491 -0.0102 145 LYS B CA  
5292 C C   . LYS B 145 ? 0.4433 0.7331 0.4984 -0.0243 -0.0470 -0.0013 145 LYS B C   
5293 O O   . LYS B 145 ? 0.5076 0.8194 0.5641 -0.0330 -0.0470 0.0011  145 LYS B O   
5294 C CB  . LYS B 145 ? 0.4960 0.7675 0.5366 -0.0262 -0.0512 -0.0073 145 LYS B CB  
5295 C CG  . LYS B 145 ? 0.5361 0.7875 0.5657 -0.0359 -0.0526 -0.0165 145 LYS B CG  
5296 C CD  . LYS B 145 ? 0.6366 0.8948 0.6607 -0.0291 -0.0545 -0.0126 145 LYS B CD  
5297 C CE  . LYS B 145 ? 0.6741 0.9074 0.6915 -0.0250 -0.0547 -0.0180 145 LYS B CE  
5298 N NZ  . LYS B 145 ? 0.6329 0.8434 0.6391 -0.0420 -0.0525 -0.0301 145 LYS B NZ  
5299 N N   . ASP B 146 ? 0.4424 0.7251 0.5031 -0.0066 -0.0445 0.0029  146 ASP B N   
5300 C CA  . ASP B 146 ? 0.4387 0.7382 0.5066 0.0037  -0.0410 0.0106  146 ASP B CA  
5301 C C   . ASP B 146 ? 0.4673 0.7711 0.5394 -0.0053 -0.0393 0.0086  146 ASP B C   
5302 O O   . ASP B 146 ? 0.5773 0.9037 0.6533 -0.0069 -0.0378 0.0135  146 ASP B O   
5303 C CB  . ASP B 146 ? 0.5407 0.8265 0.6106 0.0243  -0.0372 0.0142  146 ASP B CB  
5304 C CG  . ASP B 146 ? 0.6688 0.9511 0.7348 0.0343  -0.0378 0.0181  146 ASP B CG  
5305 O OD1 . ASP B 146 ? 0.6767 0.9413 0.7376 0.0324  -0.0401 0.0133  146 ASP B OD1 
5306 O OD2 . ASP B 146 ? 0.7476 1.0456 0.8153 0.0443  -0.0355 0.0265  146 ASP B OD2 
5307 N N   . LEU B 147 ? 0.3606 0.6445 0.4318 -0.0111 -0.0392 0.0023  147 LEU B N   
5308 C CA  . LEU B 147 ? 0.2780 0.5637 0.3530 -0.0191 -0.0370 0.0013  147 LEU B CA  
5309 C C   . LEU B 147 ? 0.2625 0.5502 0.3340 -0.0420 -0.0384 -0.0034 147 LEU B C   
5310 O O   . LEU B 147 ? 0.2388 0.5215 0.3121 -0.0514 -0.0362 -0.0051 147 LEU B O   
5311 C CB  . LEU B 147 ? 0.2314 0.4943 0.3068 -0.0124 -0.0351 -0.0018 147 LEU B CB  
5312 C CG  . LEU B 147 ? 0.2854 0.5403 0.3620 0.0080  -0.0322 0.0006  147 LEU B CG  
5313 C CD1 . LEU B 147 ? 0.2569 0.4780 0.3270 0.0103  -0.0291 -0.0039 147 LEU B CD1 
5314 C CD2 . LEU B 147 ? 0.3204 0.5929 0.4019 0.0171  -0.0280 0.0064  147 LEU B CD2 
5315 N N   . LYS B 148 ? 0.2456 0.5393 0.3110 -0.0516 -0.0410 -0.0056 148 LYS B N   
5316 C CA  . LYS B 148 ? 0.2908 0.5799 0.3494 -0.0746 -0.0408 -0.0122 148 LYS B CA  
5317 C C   . LYS B 148 ? 0.3320 0.6364 0.3944 -0.0852 -0.0381 -0.0095 148 LYS B C   
5318 O O   . LYS B 148 ? 0.3797 0.6701 0.4383 -0.1024 -0.0355 -0.0146 148 LYS B O   
5319 C CB  . LYS B 148 ? 0.3472 0.6457 0.3978 -0.0817 -0.0434 -0.0142 148 LYS B CB  
5320 C CG  . LYS B 148 ? 0.4335 0.7228 0.4737 -0.1058 -0.0419 -0.0228 148 LYS B CG  
5321 C CD  . LYS B 148 ? 0.5247 0.8367 0.5589 -0.1135 -0.0440 -0.0225 148 LYS B CD  
5322 C CE  . LYS B 148 ? 0.5405 0.8564 0.5735 -0.0993 -0.0473 -0.0197 148 LYS B CE  
5323 N NZ  . LYS B 148 ? 0.6156 0.9658 0.6485 -0.0996 -0.0495 -0.0136 148 LYS B NZ  
5324 N N   . ASP B 149 ? 0.3834 0.7150 0.4527 -0.0754 -0.0378 -0.0014 149 ASP B N   
5325 C CA  . ASP B 149 ? 0.4201 0.7695 0.4931 -0.0845 -0.0353 0.0019  149 ASP B CA  
5326 C C   . ASP B 149 ? 0.3199 0.6544 0.3970 -0.0853 -0.0317 0.0017  149 ASP B C   
5327 O O   . ASP B 149 ? 0.3310 0.6624 0.4066 -0.1024 -0.0290 -0.0001 149 ASP B O   
5328 C CB  . ASP B 149 ? 0.5188 0.8994 0.5983 -0.0708 -0.0350 0.0111  149 ASP B CB  
5329 C CG  . ASP B 149 ? 0.6300 1.0318 0.7063 -0.0717 -0.0380 0.0134  149 ASP B CG  
5330 O OD1 . ASP B 149 ? 0.6104 1.0074 0.6785 -0.0876 -0.0402 0.0072  149 ASP B OD1 
5331 O OD2 . ASP B 149 ? 0.6615 1.0845 0.7427 -0.0563 -0.0375 0.0217  149 ASP B OD2 
5332 N N   . LEU B 150 ? 0.3011 0.6268 0.3829 -0.0670 -0.0308 0.0040  150 LEU B N   
5333 C CA  . LEU B 150 ? 0.2708 0.5857 0.3563 -0.0667 -0.0273 0.0047  150 LEU B CA  
5334 C C   . LEU B 150 ? 0.3023 0.5864 0.3812 -0.0807 -0.0257 -0.0012 150 LEU B C   
5335 O O   . LEU B 150 ? 0.2851 0.5556 0.3620 -0.0879 -0.0207 0.0004  150 LEU B O   
5336 C CB  . LEU B 150 ? 0.2385 0.5481 0.3274 -0.0443 -0.0262 0.0072  150 LEU B CB  
5337 C CG  . LEU B 150 ? 0.3193 0.6489 0.4120 -0.0289 -0.0238 0.0133  150 LEU B CG  
5338 C CD1 . LEU B 150 ? 0.3325 0.6490 0.4251 -0.0092 -0.0215 0.0132  150 LEU B CD1 
5339 C CD2 . LEU B 150 ? 0.2898 0.6376 0.3862 -0.0359 -0.0203 0.0176  150 LEU B CD2 
5340 N N   . LEU B 151 ? 0.3022 0.5651 0.3731 -0.0816 -0.0278 -0.0072 151 LEU B N   
5341 C CA  . LEU B 151 ? 0.3255 0.5475 0.3853 -0.0903 -0.0236 -0.0125 151 LEU B CA  
5342 C C   . LEU B 151 ? 0.3471 0.5667 0.4026 -0.1145 -0.0201 -0.0155 151 LEU B C   
5343 O O   . LEU B 151 ? 0.4231 0.6144 0.4733 -0.1204 -0.0134 -0.0150 151 LEU B O   
5344 C CB  . LEU B 151 ? 0.3841 0.5887 0.4365 -0.0868 -0.0261 -0.0186 151 LEU B CB  
5345 C CG  . LEU B 151 ? 0.3788 0.5677 0.4313 -0.0658 -0.0268 -0.0172 151 LEU B CG  
5346 C CD1 . LEU B 151 ? 0.3829 0.5645 0.4296 -0.0635 -0.0299 -0.0222 151 LEU B CD1 
5347 C CD2 . LEU B 151 ? 0.3276 0.4838 0.3760 -0.0619 -0.0212 -0.0164 151 LEU B CD2 
5348 N N   . ASN B 152 ? 0.3808 0.6305 0.4381 -0.1293 -0.0240 -0.0181 152 ASN B N   
5349 C CA  . ASN B 152 ? 0.4382 0.6815 0.4876 -0.1524 -0.0198 -0.0221 152 ASN B CA  
5350 C C   . ASN B 152 ? 0.3874 0.6413 0.4427 -0.1582 -0.0156 -0.0156 152 ASN B C   
5351 O O   . ASN B 152 ? 0.4086 0.6484 0.4565 -0.1771 -0.0101 -0.0182 152 ASN B O   
5352 C CB  . ASN B 152 ? 0.5790 0.8442 0.6228 -0.1580 -0.0238 -0.0245 152 ASN B CB  
5353 C CG  . ASN B 152 ? 0.7696 1.0094 0.7979 -0.1754 -0.0210 -0.0350 152 ASN B CG  
5354 O OD1 . ASN B 152 ? 0.8619 1.0655 0.8823 -0.1866 -0.0141 -0.0403 152 ASN B OD1 
5355 N ND2 . ASN B 152 ? 0.8327 1.0898 0.8554 -0.1773 -0.0250 -0.0375 152 ASN B ND2 
5356 N N   . LYS B 153 ? 0.3402 0.6170 0.4071 -0.1419 -0.0172 -0.0073 153 LYS B N   
5357 C CA  . LYS B 153 ? 0.3871 0.6760 0.4595 -0.1456 -0.0130 -0.0005 153 LYS B CA  
5358 C C   . LYS B 153 ? 0.3706 0.6236 0.4381 -0.1519 -0.0051 0.0008  153 LYS B C   
5359 O O   . LYS B 153 ? 0.3743 0.6227 0.4396 -0.1695 0.0008  0.0026  153 LYS B O   
5360 C CB  . LYS B 153 ? 0.3871 0.7032 0.4700 -0.1232 -0.0155 0.0069  153 LYS B CB  
5361 C CG  . LYS B 153 ? 0.4135 0.7426 0.5021 -0.1214 -0.0110 0.0142  153 LYS B CG  
5362 C CD  . LYS B 153 ? 0.4141 0.7642 0.5093 -0.0974 -0.0129 0.0189  153 LYS B CD  
5363 C CE  . LYS B 153 ? 0.4444 0.8054 0.5440 -0.0922 -0.0080 0.0255  153 LYS B CE  
5364 N NZ  . LYS B 153 ? 0.4765 0.8558 0.5765 -0.1064 -0.0058 0.0289  153 LYS B NZ  
5365 N N   . GLY B 154 ? 0.3726 0.5939 0.4349 -0.1347 -0.0041 0.0009  154 GLY B N   
5366 C CA  . GLY B 154 ? 0.3564 0.5358 0.4100 -0.1349 0.0036  0.0031  154 GLY B CA  
5367 C C   . GLY B 154 ? 0.3712 0.5526 0.4279 -0.1305 0.0085  0.0129  154 GLY B C   
5368 O O   . GLY B 154 ? 0.3749 0.5239 0.4250 -0.1262 0.0144  0.0171  154 GLY B O   
5369 N N   . ARG B 155 ? 0.3419 0.5613 0.4082 -0.1305 0.0067  0.0177  155 ARG B N   
5370 C CA  . ARG B 155 ? 0.3199 0.5445 0.3883 -0.1285 0.0118  0.0270  155 ARG B CA  
5371 C C   . ARG B 155 ? 0.2789 0.5504 0.3591 -0.1224 0.0084  0.0303  155 ARG B C   
5372 O O   . ARG B 155 ? 0.3233 0.6223 0.4103 -0.1211 0.0027  0.0263  155 ARG B O   
5373 C CB  . ARG B 155 ? 0.3963 0.6054 0.4594 -0.1506 0.0199  0.0299  155 ARG B CB  
5374 C CG  . ARG B 155 ? 0.4145 0.6564 0.4836 -0.1717 0.0186  0.0269  155 ARG B CG  
5375 C CD  . ARG B 155 ? 0.4894 0.7051 0.5492 -0.1978 0.0257  0.0233  155 ARG B CD  
5376 N NE  . ARG B 155 ? 0.5730 0.7513 0.6246 -0.1983 0.0358  0.0311  155 ARG B NE  
5377 C CZ  . ARG B 155 ? 0.6695 0.7988 0.7087 -0.2020 0.0428  0.0289  155 ARG B CZ  
5378 N NH1 . ARG B 155 ? 0.6923 0.8037 0.7250 -0.2067 0.0408  0.0177  155 ARG B NH1 
5379 N NH2 . ARG B 155 ? 0.7098 0.8083 0.7426 -0.2001 0.0525  0.0386  155 ARG B NH2 
5380 N N   . ASN B 156 ? 0.2287 0.5097 0.3109 -0.1178 0.0127  0.0383  156 ASN B N   
5381 C CA  . ASN B 156 ? 0.2352 0.5603 0.3281 -0.1132 0.0121  0.0422  156 ASN B CA  
5382 C C   . ASN B 156 ? 0.2727 0.6158 0.3710 -0.0922 0.0067  0.0389  156 ASN B C   
5383 O O   . ASN B 156 ? 0.3030 0.6733 0.4064 -0.0877 0.0041  0.0385  156 ASN B O   
5384 C CB  . ASN B 156 ? 0.3020 0.6498 0.3986 -0.1310 0.0116  0.0415  156 ASN B CB  
5385 C CG  . ASN B 156 ? 0.3489 0.6784 0.4396 -0.1530 0.0184  0.0446  156 ASN B CG  
5386 O OD1 . ASN B 156 ? 0.4827 0.8083 0.5695 -0.1702 0.0178  0.0398  156 ASN B OD1 
5387 N ND2 . ASN B 156 ? 0.2978 0.6147 0.3862 -0.1520 0.0254  0.0528  156 ASN B ND2 
5388 N N   . TYR B 157 ? 0.1615 0.4787 0.2531 -0.0767 0.0053  0.0362  157 TYR B N   
5389 C CA  . TYR B 157 ? 0.1422 0.4690 0.2367 -0.0576 0.0017  0.0325  157 TYR B CA  
5390 C C   . TYR B 157 ? 0.2009 0.5493 0.2983 -0.0446 0.0054  0.0361  157 TYR B C   
5391 O O   . TYR B 157 ? 0.2103 0.5558 0.3039 -0.0465 0.0099  0.0408  157 TYR B O   
5392 C CB  . TYR B 157 ? 0.1370 0.4287 0.2227 -0.0478 -0.0007 0.0276  157 TYR B CB  
5393 C CG  . TYR B 157 ? 0.1709 0.4436 0.2536 -0.0576 -0.0040 0.0228  157 TYR B CG  
5394 C CD1 . TYR B 157 ? 0.1553 0.4409 0.2421 -0.0555 -0.0089 0.0184  157 TYR B CD1 
5395 C CD2 . TYR B 157 ? 0.2549 0.4969 0.3300 -0.0686 -0.0012 0.0231  157 TYR B CD2 
5396 C CE1 . TYR B 157 ? 0.2104 0.4801 0.2929 -0.0654 -0.0116 0.0133  157 TYR B CE1 
5397 C CE2 . TYR B 157 ? 0.2405 0.4636 0.3112 -0.0779 -0.0028 0.0174  157 TYR B CE2 
5398 C CZ  . TYR B 157 ? 0.2537 0.4914 0.3278 -0.0770 -0.0083 0.0120  157 TYR B CZ  
5399 O OH  . TYR B 157 ? 0.2519 0.4720 0.3201 -0.0871 -0.0097 0.0057  157 TYR B OH  
5400 N N   . THR B 158 ? 0.1276 0.4921 0.2289 -0.0302 0.0042  0.0338  158 THR B N   
5401 C CA  . THR B 158 ? 0.1290 0.5041 0.2282 -0.0158 0.0087  0.0351  158 THR B CA  
5402 C C   . THR B 158 ? 0.1220 0.4810 0.2163 0.0005  0.0091  0.0295  158 THR B C   
5403 O O   . THR B 158 ? 0.1161 0.4578 0.2092 0.0029  0.0050  0.0251  158 THR B O   
5404 C CB  . THR B 158 ? 0.1354 0.5316 0.2374 -0.0102 0.0091  0.0370  158 THR B CB  
5405 O OG1 . THR B 158 ? 0.1317 0.5218 0.2339 -0.0005 0.0057  0.0336  158 THR B OG1 
5406 C CG2 . THR B 158 ? 0.1439 0.5567 0.2500 -0.0278 0.0077  0.0413  158 THR B CG2 
5407 N N   . GLN B 159 ? 0.1375 0.5010 0.2272 0.0109  0.0144  0.0290  159 GLN B N   
5408 C CA  . GLN B 159 ? 0.1574 0.5060 0.2406 0.0252  0.0161  0.0223  159 GLN B CA  
5409 C C   . GLN B 159 ? 0.1465 0.4879 0.2306 0.0360  0.0145  0.0185  159 GLN B C   
5410 O O   . GLN B 159 ? 0.1315 0.4542 0.2122 0.0421  0.0129  0.0130  159 GLN B O   
5411 C CB  . GLN B 159 ? 0.1459 0.5027 0.2224 0.0328  0.0231  0.0215  159 GLN B CB  
5412 C CG  . GLN B 159 ? 0.1747 0.5164 0.2421 0.0461  0.0266  0.0128  159 GLN B CG  
5413 C CD  . GLN B 159 ? 0.2185 0.5331 0.2746 0.0408  0.0224  0.0091  159 GLN B CD  
5414 O OE1 . GLN B 159 ? 0.1787 0.4903 0.2335 0.0300  0.0194  0.0146  159 GLN B OE1 
5415 N NE2 . GLN B 159 ? 0.2166 0.5115 0.2644 0.0486  0.0229  0.0006  159 GLN B NE2 
5416 N N   . GLU B 160 ? 0.1286 0.4854 0.2172 0.0380  0.0149  0.0225  160 GLU B N   
5417 C CA  . GLU B 160 ? 0.1316 0.4835 0.2210 0.0490  0.0142  0.0215  160 GLU B CA  
5418 C C   . GLU B 160 ? 0.1277 0.4680 0.2189 0.0423  0.0072  0.0201  160 GLU B C   
5419 O O   . GLU B 160 ? 0.1296 0.4545 0.2182 0.0516  0.0066  0.0170  160 GLU B O   
5420 C CB  . GLU B 160 ? 0.1400 0.5153 0.2344 0.0524  0.0159  0.0279  160 GLU B CB  
5421 C CG  . GLU B 160 ? 0.2123 0.5827 0.3067 0.0666  0.0168  0.0286  160 GLU B CG  
5422 C CD  . GLU B 160 ? 0.4774 0.8301 0.5655 0.0830  0.0242  0.0238  160 GLU B CD  
5423 O OE1 . GLU B 160 ? 0.5693 0.9226 0.6535 0.0847  0.0294  0.0210  160 GLU B OE1 
5424 O OE2 . GLU B 160 ? 0.6126 0.9500 0.6985 0.0936  0.0254  0.0226  160 GLU B OE2 
5425 N N   . GLU B 161 ? 0.1194 0.4660 0.2142 0.0259  0.0027  0.0224  161 GLU B N   
5426 C CA  . GLU B 161 ? 0.1266 0.4615 0.2219 0.0181  -0.0034 0.0201  161 GLU B CA  
5427 C C   . GLU B 161 ? 0.1486 0.4590 0.2397 0.0217  -0.0046 0.0146  161 GLU B C   
5428 O O   . GLU B 161 ? 0.1156 0.4118 0.2048 0.0258  -0.0077 0.0113  161 GLU B O   
5429 C CB  . GLU B 161 ? 0.1159 0.4600 0.2145 -0.0019 -0.0063 0.0224  161 GLU B CB  
5430 C CG  . GLU B 161 ? 0.1248 0.4943 0.2267 -0.0066 -0.0065 0.0271  161 GLU B CG  
5431 C CD  . GLU B 161 ? 0.2395 0.6190 0.3434 -0.0279 -0.0077 0.0288  161 GLU B CD  
5432 O OE1 . GLU B 161 ? 0.1861 0.5537 0.2893 -0.0385 -0.0066 0.0280  161 GLU B OE1 
5433 O OE2 . GLU B 161 ? 0.2408 0.6402 0.3463 -0.0347 -0.0092 0.0315  161 GLU B OE2 
5434 N N   . LYS B 162 ? 0.1077 0.4093 0.1942 0.0201  -0.0019 0.0138  162 LYS B N   
5435 C CA  . LYS B 162 ? 0.1081 0.3783 0.1844 0.0227  -0.0029 0.0088  162 LYS B CA  
5436 C C   . LYS B 162 ? 0.1209 0.3815 0.1933 0.0377  -0.0008 0.0036  162 LYS B C   
5437 O O   . LYS B 162 ? 0.1449 0.3833 0.2124 0.0396  -0.0034 -0.0007 162 LYS B O   
5438 C CB  . LYS B 162 ? 0.1125 0.3785 0.1831 0.0185  -0.0002 0.0107  162 LYS B CB  
5439 C CG  . LYS B 162 ? 0.1134 0.3540 0.1744 0.0209  -0.0014 0.0069  162 LYS B CG  
5440 C CD  . LYS B 162 ? 0.1644 0.4065 0.2201 0.0169  0.0010  0.0111  162 LYS B CD  
5441 C CE  . LYS B 162 ? 0.1509 0.4134 0.2057 0.0226  0.0062  0.0110  162 LYS B CE  
5442 N NZ  . LYS B 162 ? 0.1425 0.4075 0.1893 0.0207  0.0086  0.0140  162 LYS B NZ  
5443 N N   . GLU B 163 ? 0.1707 0.4469 0.2449 0.0484  0.0050  0.0038  163 GLU B N   
5444 C CA  . GLU B 163 ? 0.1588 0.4222 0.2277 0.0627  0.0093  -0.0015 163 GLU B CA  
5445 C C   . GLU B 163 ? 0.1788 0.4399 0.2524 0.0688  0.0070  -0.0003 163 GLU B C   
5446 O O   . GLU B 163 ? 0.2104 0.4488 0.2775 0.0755  0.0081  -0.0050 163 GLU B O   
5447 C CB  . GLU B 163 ? 0.1716 0.4500 0.2404 0.0733  0.0179  -0.0014 163 GLU B CB  
5448 C CG  . GLU B 163 ? 0.1943 0.4711 0.2546 0.0696  0.0213  -0.0048 163 GLU B CG  
5449 C CD  . GLU B 163 ? 0.3450 0.6375 0.4040 0.0777  0.0298  -0.0044 163 GLU B CD  
5450 O OE1 . GLU B 163 ? 0.3395 0.6364 0.3917 0.0750  0.0334  -0.0070 163 GLU B OE1 
5451 O OE2 . GLU B 163 ? 0.4508 0.7480 0.5134 0.0859  0.0325  -0.0008 163 GLU B OE2 
5452 N N   . TYR B 164 ? 0.1360 0.4135 0.2159 0.0640  0.0039  0.0063  164 TYR B N   
5453 C CA  . TYR B 164 ? 0.1787 0.4531 0.2599 0.0667  0.0007  0.0087  164 TYR B CA  
5454 C C   . TYR B 164 ? 0.1845 0.4412 0.2638 0.0609  -0.0050 0.0045  164 TYR B C   
5455 O O   . TYR B 164 ? 0.1711 0.4128 0.2472 0.0685  -0.0049 0.0029  164 TYR B O   
5456 C CB  . TYR B 164 ? 0.1631 0.4621 0.2503 0.0587  -0.0023 0.0155  164 TYR B CB  
5457 C CG  . TYR B 164 ? 0.2156 0.5170 0.3035 0.0599  -0.0059 0.0187  164 TYR B CG  
5458 C CD1 . TYR B 164 ? 0.2764 0.5747 0.3628 0.0751  -0.0021 0.0221  164 TYR B CD1 
5459 C CD2 . TYR B 164 ? 0.2155 0.5215 0.3047 0.0457  -0.0125 0.0185  164 TYR B CD2 
5460 C CE1 . TYR B 164 ? 0.3513 0.6540 0.4380 0.0766  -0.0052 0.0264  164 TYR B CE1 
5461 C CE2 . TYR B 164 ? 0.2818 0.5922 0.3704 0.0464  -0.0157 0.0213  164 TYR B CE2 
5462 C CZ  . TYR B 164 ? 0.3566 0.6666 0.4442 0.0622  -0.0122 0.0258  164 TYR B CZ  
5463 O OH  . TYR B 164 ? 0.3577 0.6744 0.4445 0.0633  -0.0152 0.0299  164 TYR B OH  
5464 N N   . VAL B 165 ? 0.1464 0.4013 0.2261 0.0470  -0.0092 0.0031  165 VAL B N   
5465 C CA  . VAL B 165 ? 0.1360 0.3654 0.2095 0.0403  -0.0135 -0.0009 165 VAL B CA  
5466 C C   . VAL B 165 ? 0.1778 0.3813 0.2430 0.0483  -0.0109 -0.0064 165 VAL B C   
5467 O O   . VAL B 165 ? 0.1791 0.3656 0.2407 0.0502  -0.0127 -0.0089 165 VAL B O   
5468 C CB  . VAL B 165 ? 0.1349 0.3588 0.2070 0.0251  -0.0158 -0.0008 165 VAL B CB  
5469 C CG1 . VAL B 165 ? 0.1496 0.3455 0.2152 0.0207  -0.0185 -0.0048 165 VAL B CG1 
5470 C CG2 . VAL B 165 ? 0.1664 0.4133 0.2453 0.0139  -0.0180 0.0031  165 VAL B CG2 
5471 N N   . LEU B 166 ? 0.1498 0.3513 0.2111 0.0519  -0.0065 -0.0085 166 LEU B N   
5472 C CA  . LEU B 166 ? 0.1670 0.3461 0.2192 0.0562  -0.0042 -0.0149 166 LEU B CA  
5473 C C   . LEU B 166 ? 0.1951 0.3648 0.2453 0.0678  -0.0005 -0.0171 166 LEU B C   
5474 O O   . LEU B 166 ? 0.1955 0.3441 0.2400 0.0681  -0.0010 -0.0213 166 LEU B O   
5475 C CB  . LEU B 166 ? 0.1873 0.3704 0.2345 0.0571  0.0002  -0.0173 166 LEU B CB  
5476 C CG  . LEU B 166 ? 0.3026 0.4857 0.3476 0.0469  -0.0027 -0.0156 166 LEU B CG  
5477 C CD1 . LEU B 166 ? 0.3332 0.5273 0.3736 0.0484  0.0020  -0.0165 166 LEU B CD1 
5478 C CD2 . LEU B 166 ? 0.3358 0.4984 0.3751 0.0434  -0.0060 -0.0192 166 LEU B CD2 
5479 N N   . ASN B 167 ? 0.1595 0.3454 0.2149 0.0776  0.0037  -0.0131 167 ASN B N   
5480 C CA  . ASN B 167 ? 0.1772 0.3536 0.2310 0.0909  0.0088  -0.0129 167 ASN B CA  
5481 C C   . ASN B 167 ? 0.1984 0.3685 0.2539 0.0895  0.0036  -0.0101 167 ASN B C   
5482 O O   . ASN B 167 ? 0.2181 0.3670 0.2679 0.0954  0.0065  -0.0123 167 ASN B O   
5483 C CB  . ASN B 167 ? 0.2372 0.4334 0.2966 0.1016  0.0143  -0.0065 167 ASN B CB  
5484 C CG  . ASN B 167 ? 0.4632 0.6607 0.5183 0.1059  0.0221  -0.0103 167 ASN B CG  
5485 O OD1 . ASN B 167 ? 0.5198 0.6988 0.5654 0.1067  0.0265  -0.0193 167 ASN B OD1 
5486 N ND2 . ASN B 167 ? 0.4921 0.7115 0.5526 0.1073  0.0237  -0.0040 167 ASN B ND2 
5487 N N   . LYS B 168 ? 0.1538 0.3421 0.2164 0.0810  -0.0034 -0.0053 168 LYS B N   
5488 C CA  . LYS B 168 ? 0.1349 0.3185 0.1976 0.0784  -0.0084 -0.0034 168 LYS B CA  
5489 C C   . LYS B 168 ? 0.1451 0.3011 0.1999 0.0709  -0.0107 -0.0100 168 LYS B C   
5490 O O   . LYS B 168 ? 0.1886 0.3301 0.2397 0.0737  -0.0109 -0.0105 168 LYS B O   
5491 C CB  . LYS B 168 ? 0.1550 0.3640 0.2248 0.0683  -0.0149 0.0012  168 LYS B CB  
5492 C CG  . LYS B 168 ? 0.1930 0.4254 0.2671 0.0719  -0.0129 0.0088  168 LYS B CG  
5493 C CD  . LYS B 168 ? 0.3047 0.5345 0.3769 0.0833  -0.0107 0.0143  168 LYS B CD  
5494 C CE  . LYS B 168 ? 0.4502 0.7074 0.5266 0.0831  -0.0114 0.0227  168 LYS B CE  
5495 N NZ  . LYS B 168 ? 0.5461 0.8020 0.6210 0.0993  -0.0055 0.0299  168 LYS B NZ  
5496 N N   . TYR B 169 ? 0.1146 0.2648 0.1672 0.0618  -0.0120 -0.0139 169 TYR B N   
5497 C CA  . TYR B 169 ? 0.1269 0.2549 0.1733 0.0561  -0.0136 -0.0190 169 TYR B CA  
5498 C C   . TYR B 169 ? 0.2020 0.3111 0.2417 0.0632  -0.0089 -0.0236 169 TYR B C   
5499 O O   . TYR B 169 ? 0.2037 0.2966 0.2396 0.0614  -0.0099 -0.0260 169 TYR B O   
5500 C CB  . TYR B 169 ? 0.1328 0.2617 0.1785 0.0481  -0.0147 -0.0203 169 TYR B CB  
5501 C CG  . TYR B 169 ? 0.1230 0.2583 0.1724 0.0380  -0.0186 -0.0171 169 TYR B CG  
5502 C CD1 . TYR B 169 ? 0.1499 0.2957 0.2033 0.0347  -0.0212 -0.0144 169 TYR B CD1 
5503 C CD2 . TYR B 169 ? 0.1457 0.2765 0.1938 0.0314  -0.0190 -0.0166 169 TYR B CD2 
5504 C CE1 . TYR B 169 ? 0.1535 0.3017 0.2081 0.0232  -0.0234 -0.0133 169 TYR B CE1 
5505 C CE2 . TYR B 169 ? 0.1575 0.2887 0.2075 0.0222  -0.0205 -0.0138 169 TYR B CE2 
5506 C CZ  . TYR B 169 ? 0.1441 0.2826 0.1968 0.0172  -0.0224 -0.0131 169 TYR B CZ  
5507 O OH  . TYR B 169 ? 0.1798 0.3155 0.2323 0.0060  -0.0226 -0.0120 169 TYR B OH  
5508 N N   . PHE B 170 ? 0.1880 0.2977 0.2251 0.0705  -0.0028 -0.0254 170 PHE B N   
5509 C CA  . PHE B 170 ? 0.2247 0.3127 0.2533 0.0749  0.0030  -0.0313 170 PHE B CA  
5510 C C   . PHE B 170 ? 0.2224 0.3008 0.2507 0.0837  0.0059  -0.0280 170 PHE B C   
5511 O O   . PHE B 170 ? 0.2098 0.2663 0.2313 0.0836  0.0088  -0.0320 170 PHE B O   
5512 C CB  . PHE B 170 ? 0.2172 0.3048 0.2406 0.0794  0.0102  -0.0359 170 PHE B CB  
5513 C CG  . PHE B 170 ? 0.2785 0.3646 0.2962 0.0695  0.0085  -0.0421 170 PHE B CG  
5514 C CD1 . PHE B 170 ? 0.3507 0.4189 0.3601 0.0636  0.0091  -0.0493 170 PHE B CD1 
5515 C CD2 . PHE B 170 ? 0.3007 0.4055 0.3217 0.0652  0.0059  -0.0396 170 PHE B CD2 
5516 C CE1 . PHE B 170 ? 0.3276 0.4000 0.3323 0.0544  0.0066  -0.0536 170 PHE B CE1 
5517 C CE2 . PHE B 170 ? 0.3375 0.4437 0.3532 0.0570  0.0040  -0.0433 170 PHE B CE2 
5518 C CZ  . PHE B 170 ? 0.3539 0.4455 0.3618 0.0519  0.0040  -0.0501 170 PHE B CZ  
5519 N N   . GLU B 171 ? 0.1824 0.2786 0.2181 0.0907  0.0050  -0.0199 171 GLU B N   
5520 C CA  . GLU B 171 ? 0.2123 0.3030 0.2480 0.0993  0.0067  -0.0143 171 GLU B CA  
5521 C C   . GLU B 171 ? 0.2223 0.3025 0.2557 0.0908  0.0010  -0.0153 171 GLU B C   
5522 O O   . GLU B 171 ? 0.2251 0.2872 0.2534 0.0948  0.0043  -0.0148 171 GLU B O   
5523 C CB  . GLU B 171 ? 0.1918 0.3114 0.2369 0.1069  0.0051  -0.0042 171 GLU B CB  
5524 C CG  . GLU B 171 ? 0.2983 0.4267 0.3451 0.1160  0.0121  -0.0015 171 GLU B CG  
5525 C CD  . GLU B 171 ? 0.4161 0.5723 0.4704 0.1180  0.0097  0.0091  171 GLU B CD  
5526 O OE1 . GLU B 171 ? 0.4457 0.6153 0.5031 0.1131  0.0029  0.0140  171 GLU B OE1 
5527 O OE2 . GLU B 171 ? 0.4663 0.6316 0.5222 0.1241  0.0149  0.0120  171 GLU B OE2 
5528 N N   . ILE B 172 ? 0.1575 0.2473 0.1941 0.0792  -0.0064 -0.0165 172 ILE B N   
5529 C CA  . ILE B 172 ? 0.1664 0.2457 0.2003 0.0715  -0.0106 -0.0182 172 ILE B CA  
5530 C C   . ILE B 172 ? 0.1618 0.2176 0.1890 0.0685  -0.0076 -0.0249 172 ILE B C   
5531 O O   . ILE B 172 ? 0.2010 0.2434 0.2246 0.0678  -0.0071 -0.0252 172 ILE B O   
5532 C CB  . ILE B 172 ? 0.1793 0.2702 0.2169 0.0603  -0.0169 -0.0188 172 ILE B CB  
5533 C CG1 . ILE B 172 ? 0.1865 0.3008 0.2294 0.0595  -0.0205 -0.0131 172 ILE B CG1 
5534 C CG2 . ILE B 172 ? 0.2153 0.2914 0.2494 0.0528  -0.0192 -0.0223 172 ILE B CG2 
5535 C CD1 . ILE B 172 ? 0.1904 0.3082 0.2320 0.0632  -0.0219 -0.0086 172 ILE B CD1 
5536 N N   . ILE B 173 ? 0.1657 0.2187 0.1909 0.0656  -0.0057 -0.0301 173 ILE B N   
5537 C CA  . ILE B 173 ? 0.1912 0.2267 0.2100 0.0604  -0.0037 -0.0368 173 ILE B CA  
5538 C C   . ILE B 173 ? 0.2597 0.2756 0.2718 0.0664  0.0036  -0.0384 173 ILE B C   
5539 O O   . ILE B 173 ? 0.2237 0.2248 0.2316 0.0619  0.0046  -0.0411 173 ILE B O   
5540 C CB  . ILE B 173 ? 0.2073 0.2476 0.2242 0.0558  -0.0033 -0.0417 173 ILE B CB  
5541 C CG1 . ILE B 173 ? 0.2281 0.2841 0.2513 0.0500  -0.0096 -0.0384 173 ILE B CG1 
5542 C CG2 . ILE B 173 ? 0.2950 0.3219 0.3050 0.0492  -0.0013 -0.0489 173 ILE B CG2 
5543 C CD1 . ILE B 173 ? 0.2691 0.3326 0.2905 0.0455  -0.0099 -0.0411 173 ILE B CD1 
5544 N N   . LYS B 174 ? 0.1805 0.1956 0.1916 0.0768  0.0096  -0.0362 174 LYS B N   
5545 C CA  . LYS B 174 ? 0.2001 0.1927 0.2039 0.0844  0.0188  -0.0366 174 LYS B CA  
5546 C C   . LYS B 174 ? 0.2623 0.2484 0.2666 0.0879  0.0181  -0.0297 174 LYS B C   
5547 O O   . LYS B 174 ? 0.2970 0.2599 0.2941 0.0911  0.0256  -0.0302 174 LYS B O   
5548 C CB  . LYS B 174 ? 0.2873 0.2828 0.2913 0.0978  0.0263  -0.0335 174 LYS B CB  
5549 C CG  . LYS B 174 ? 0.3537 0.3468 0.3525 0.0951  0.0308  -0.0422 174 LYS B CG  
5550 C CD  . LYS B 174 ? 0.3841 0.3766 0.3820 0.1099  0.0406  -0.0397 174 LYS B CD  
5551 C CE  . LYS B 174 ? 0.5046 0.5026 0.4984 0.1060  0.0432  -0.0479 174 LYS B CE  
5552 N NZ  . LYS B 174 ? 0.6018 0.6254 0.6041 0.1158  0.0438  -0.0413 174 LYS B NZ  
5553 N N   . LYS B 175 ? 0.2175 0.2227 0.2289 0.0868  0.0102  -0.0234 175 LYS B N   
5554 C CA  . LYS B 175 ? 0.2266 0.2287 0.2373 0.0891  0.0090  -0.0170 175 LYS B CA  
5555 C C   . LYS B 175 ? 0.2418 0.2379 0.2509 0.0772  0.0044  -0.0212 175 LYS B C   
5556 O O   . LYS B 175 ? 0.2542 0.2482 0.2619 0.0775  0.0033  -0.0167 175 LYS B O   
5557 C CB  . LYS B 175 ? 0.2807 0.3091 0.2984 0.0942  0.0035  -0.0078 175 LYS B CB  
5558 C CG  . LYS B 175 ? 0.4773 0.5237 0.5005 0.1030  0.0052  -0.0038 175 LYS B CG  
5559 C CD  . LYS B 175 ? 0.5769 0.6436 0.6047 0.1139  0.0045  0.0082  175 LYS B CD  
5560 C CE  . LYS B 175 ? 0.6563 0.7443 0.6873 0.1046  -0.0053 0.0106  175 LYS B CE  
5561 N NZ  . LYS B 175 ? 0.7174 0.8334 0.7560 0.0986  -0.0111 0.0103  175 LYS B NZ  
5562 N N   . THR B 176 ? 0.1827 0.1784 0.1922 0.0674  0.0019  -0.0288 176 THR B N   
5563 C CA  . THR B 176 ? 0.2044 0.2010 0.2150 0.0579  -0.0029 -0.0311 176 THR B CA  
5564 C C   . THR B 176 ? 0.2803 0.2588 0.2854 0.0550  0.0011  -0.0325 176 THR B C   
5565 O O   . THR B 176 ? 0.2640 0.2429 0.2691 0.0533  -0.0008 -0.0295 176 THR B O   
5566 C CB  . THR B 176 ? 0.2212 0.2252 0.2346 0.0503  -0.0062 -0.0364 176 THR B CB  
5567 O OG1 . THR B 176 ? 0.2361 0.2567 0.2547 0.0519  -0.0098 -0.0337 176 THR B OG1 
5568 C CG2 . THR B 176 ? 0.2182 0.2229 0.2335 0.0426  -0.0095 -0.0377 176 THR B CG2 
5569 N N   . LEU B 177 ? 0.2337 0.1958 0.2331 0.0531  0.0073  -0.0377 177 LEU B N   
5570 C CA  . LEU B 177 ? 0.3082 0.2531 0.3022 0.0484  0.0116  -0.0390 177 LEU B CA  
5571 C C   . LEU B 177 ? 0.2775 0.2135 0.2686 0.0571  0.0152  -0.0305 177 LEU B C   
5572 O O   . LEU B 177 ? 0.2972 0.2273 0.2862 0.0538  0.0158  -0.0282 177 LEU B O   
5573 C CB  . LEU B 177 ? 0.3053 0.2326 0.2919 0.0424  0.0185  -0.0472 177 LEU B CB  
5574 C CG  . LEU B 177 ? 0.3982 0.3380 0.3869 0.0321  0.0144  -0.0550 177 LEU B CG  
5575 C CD1 . LEU B 177 ? 0.4061 0.3298 0.3854 0.0236  0.0212  -0.0643 177 LEU B CD1 
5576 C CD2 . LEU B 177 ? 0.4473 0.4019 0.4425 0.0249  0.0077  -0.0539 177 LEU B CD2 
5577 N N   . SER B 178 ? 0.2701 0.2085 0.2614 0.0690  0.0175  -0.0247 178 SER B N   
5578 C CA  . SER B 178 ? 0.2570 0.1906 0.2459 0.0793  0.0210  -0.0144 178 SER B CA  
5579 C C   . SER B 178 ? 0.2355 0.1864 0.2275 0.0773  0.0136  -0.0089 178 SER B C   
5580 O O   . SER B 178 ? 0.2594 0.2034 0.2471 0.0800  0.0161  -0.0025 178 SER B O   
5581 C CB  . SER B 178 ? 0.3050 0.2452 0.2958 0.0936  0.0242  -0.0079 178 SER B CB  
5582 O OG  . SER B 178 ? 0.4286 0.3466 0.4135 0.0970  0.0340  -0.0126 178 SER B OG  
5583 N N   . ILE B 179 ? 0.2531 0.2251 0.2512 0.0724  0.0053  -0.0114 179 ILE B N   
5584 C CA  . ILE B 179 ? 0.2033 0.1894 0.2021 0.0700  -0.0003 -0.0075 179 ILE B CA  
5585 C C   . ILE B 179 ? 0.1983 0.1736 0.1938 0.0616  0.0005  -0.0109 179 ILE B C   
5586 O O   . ILE B 179 ? 0.2135 0.1911 0.2054 0.0618  0.0000  -0.0062 179 ILE B O   
5587 C CB  . ILE B 179 ? 0.2494 0.2575 0.2541 0.0657  -0.0078 -0.0098 179 ILE B CB  
5588 C CG1 . ILE B 179 ? 0.2834 0.3051 0.2862 0.0625  -0.0126 -0.0068 179 ILE B CG1 
5589 C CG2 . ILE B 179 ? 0.2049 0.2103 0.2126 0.0566  -0.0098 -0.0183 179 ILE B CG2 
5590 C CD1 . ILE B 179 ? 0.3433 0.3787 0.3445 0.0711  -0.0131 0.0033  179 ILE B CD1 
5591 N N   . TYR B 180 ? 0.1754 0.1415 0.1719 0.0540  0.0019  -0.0186 180 TYR B N   
5592 C CA  . TYR B 180 ? 0.1725 0.1318 0.1672 0.0463  0.0032  -0.0211 180 TYR B CA  
5593 C C   . TYR B 180 ? 0.2559 0.1978 0.2437 0.0485  0.0101  -0.0164 180 TYR B C   
5594 O O   . TYR B 180 ? 0.2531 0.1943 0.2382 0.0460  0.0108  -0.0137 180 TYR B O   
5595 C CB  . TYR B 180 ? 0.1916 0.1496 0.1897 0.0379  0.0031  -0.0290 180 TYR B CB  
5596 C CG  . TYR B 180 ? 0.1505 0.1246 0.1551 0.0356  -0.0029 -0.0316 180 TYR B CG  
5597 C CD1 . TYR B 180 ? 0.1805 0.1617 0.1873 0.0324  -0.0051 -0.0317 180 TYR B CD1 
5598 C CD2 . TYR B 180 ? 0.1567 0.1374 0.1644 0.0372  -0.0052 -0.0337 180 TYR B CD2 
5599 C CE1 . TYR B 180 ? 0.1742 0.1659 0.1860 0.0311  -0.0088 -0.0334 180 TYR B CE1 
5600 C CE2 . TYR B 180 ? 0.1322 0.1256 0.1453 0.0351  -0.0097 -0.0349 180 TYR B CE2 
5601 C CZ  . TYR B 180 ? 0.1746 0.1718 0.1895 0.0323  -0.0111 -0.0346 180 TYR B CZ  
5602 O OH  . TYR B 180 ? 0.1485 0.1536 0.1676 0.0311  -0.0137 -0.0352 180 TYR B OH  
5603 N N   . ARG B 181 ? 0.2284 0.1546 0.2124 0.0533  0.0163  -0.0155 181 ARG B N   
5604 C CA  . ARG B 181 ? 0.2392 0.1448 0.2155 0.0567  0.0246  -0.0097 181 ARG B CA  
5605 C C   . ARG B 181 ? 0.2316 0.1462 0.2060 0.0660  0.0232  0.0018  181 ARG B C   
5606 O O   . ARG B 181 ? 0.2659 0.1723 0.2350 0.0651  0.0268  0.0072  181 ARG B O   
5607 C CB  . ARG B 181 ? 0.2533 0.1383 0.2250 0.0623  0.0330  -0.0106 181 ARG B CB  
5608 C CG  . ARG B 181 ? 0.2729 0.1441 0.2422 0.0507  0.0368  -0.0223 181 ARG B CG  
5609 C CD  . ARG B 181 ? 0.3261 0.1757 0.2889 0.0574  0.0461  -0.0240 181 ARG B CD  
5610 N NE  . ARG B 181 ? 0.5105 0.3521 0.4702 0.0459  0.0485  -0.0368 181 ARG B NE  
5611 C CZ  . ARG B 181 ? 0.5694 0.4162 0.5300 0.0486  0.0480  -0.0422 181 ARG B CZ  
5612 N NH1 . ARG B 181 ? 0.4416 0.3016 0.4072 0.0624  0.0454  -0.0355 181 ARG B NH1 
5613 N NH2 . ARG B 181 ? 0.6799 0.5211 0.6361 0.0367  0.0500  -0.0541 181 ARG B NH2 
5614 N N   . GLU B 182 ? 0.2490 0.1831 0.2274 0.0739  0.0178  0.0061  182 GLU B N   
5615 C CA  . GLU B 182 ? 0.2386 0.1859 0.2148 0.0825  0.0161  0.0177  182 GLU B CA  
5616 C C   . GLU B 182 ? 0.2461 0.2055 0.2203 0.0747  0.0110  0.0172  182 GLU B C   
5617 O O   . GLU B 182 ? 0.2399 0.1986 0.2080 0.0778  0.0132  0.0255  182 GLU B O   
5618 C CB  . GLU B 182 ? 0.2774 0.2478 0.2592 0.0903  0.0109  0.0213  182 GLU B CB  
5619 C CG  . GLU B 182 ? 0.3615 0.3562 0.3421 0.0954  0.0059  0.0316  182 GLU B CG  
5620 C CD  . GLU B 182 ? 0.5909 0.6111 0.5776 0.1036  0.0018  0.0371  182 GLU B CD  
5621 O OE1 . GLU B 182 ? 0.6612 0.7033 0.6467 0.1098  -0.0012 0.0478  182 GLU B OE1 
5622 O OE2 . GLU B 182 ? 0.6002 0.6213 0.5928 0.1035  0.0015  0.0313  182 GLU B OE2 
5623 N N   . ILE B 183 ? 0.1997 0.1702 0.1783 0.0654  0.0049  0.0079  183 ILE B N   
5624 C CA  . ILE B 183 ? 0.1960 0.1766 0.1717 0.0589  0.0016  0.0066  183 ILE B CA  
5625 C C   . ILE B 183 ? 0.2405 0.2055 0.2122 0.0539  0.0072  0.0060  183 ILE B C   
5626 O O   . ILE B 183 ? 0.2450 0.2144 0.2110 0.0523  0.0075  0.0095  183 ILE B O   
5627 C CB  . ILE B 183 ? 0.2576 0.2502 0.2383 0.0514  -0.0043 -0.0026 183 ILE B CB  
5628 C CG1 . ILE B 183 ? 0.2423 0.2244 0.2285 0.0458  -0.0027 -0.0107 183 ILE B CG1 
5629 C CG2 . ILE B 183 ? 0.2438 0.2528 0.2281 0.0548  -0.0094 -0.0014 183 ILE B CG2 
5630 C CD1 . ILE B 183 ? 0.3031 0.2837 0.2891 0.0388  -0.0016 -0.0151 183 ILE B CD1 
5631 N N   . LYS B 184 ? 0.2262 0.1738 0.1998 0.0506  0.0121  0.0019  184 LYS B N   
5632 C CA  . LYS B 184 ? 0.2275 0.1614 0.1975 0.0446  0.0180  0.0020  184 LYS B CA  
5633 C C   . LYS B 184 ? 0.2387 0.1608 0.2003 0.0512  0.0241  0.0131  184 LYS B C   
5634 O O   . LYS B 184 ? 0.2904 0.2127 0.2470 0.0486  0.0264  0.0173  184 LYS B O   
5635 C CB  . LYS B 184 ? 0.2485 0.1690 0.2218 0.0376  0.0216  -0.0056 184 LYS B CB  
5636 C CG  . LYS B 184 ? 0.3151 0.2243 0.2858 0.0283  0.0276  -0.0068 184 LYS B CG  
5637 C CD  . LYS B 184 ? 0.3720 0.2699 0.3446 0.0201  0.0310  -0.0148 184 LYS B CD  
5638 C CE  . LYS B 184 ? 0.4591 0.3469 0.4291 0.0087  0.0374  -0.0162 184 LYS B CE  
5639 N NZ  . LYS B 184 ? 0.6282 0.4947 0.5885 0.0123  0.0457  -0.0074 184 LYS B NZ  
5640 N N   . GLU B 185 ? 0.2511 0.1631 0.2108 0.0607  0.0277  0.0190  185 GLU B N   
5641 C CA  . GLU B 185 ? 0.2748 0.1733 0.2265 0.0692  0.0350  0.0316  185 GLU B CA  
5642 C C   . GLU B 185 ? 0.2856 0.2054 0.2336 0.0753  0.0305  0.0418  185 GLU B C   
5643 O O   . GLU B 185 ? 0.2919 0.2046 0.2324 0.0788  0.0357  0.0523  185 GLU B O   
5644 C CB  . GLU B 185 ? 0.3313 0.2153 0.2822 0.0808  0.0407  0.0365  185 GLU B CB  
5645 C CG  . GLU B 185 ? 0.5391 0.3976 0.4895 0.0740  0.0476  0.0267  185 GLU B CG  
5646 C CD  . GLU B 185 ? 0.6231 0.4793 0.5766 0.0820  0.0485  0.0240  185 GLU B CD  
5647 O OE1 . GLU B 185 ? 0.6162 0.4843 0.5713 0.0962  0.0472  0.0335  185 GLU B OE1 
5648 O OE2 . GLU B 185 ? 0.6756 0.5205 0.6300 0.0737  0.0505  0.0124  185 GLU B OE2 
5649 N N   . GLU B 186 ? 0.2719 0.1478 0.2792 0.0747  -0.0820 -0.0246 186 GLU B N   
5650 C CA  . GLU B 186 ? 0.2528 0.1288 0.2539 0.0761  -0.0847 -0.0183 186 GLU B CA  
5651 C C   . GLU B 186 ? 0.2505 0.1216 0.2411 0.0705  -0.0819 -0.0102 186 GLU B C   
5652 O O   . GLU B 186 ? 0.2930 0.1647 0.2764 0.0711  -0.0841 -0.0047 186 GLU B O   
5653 C CB  . GLU B 186 ? 0.3019 0.1940 0.3053 0.0811  -0.0848 -0.0248 186 GLU B CB  
5654 C CG  . GLU B 186 ? 0.2993 0.1988 0.3126 0.0876  -0.0878 -0.0328 186 GLU B CG  
5655 C CD  . GLU B 186 ? 0.3629 0.2803 0.3790 0.0924  -0.0884 -0.0387 186 GLU B CD  
5656 O OE1 . GLU B 186 ? 0.3720 0.2990 0.3855 0.0901  -0.0844 -0.0413 186 GLU B OE1 
5657 O OE2 . GLU B 186 ? 0.3899 0.3123 0.4113 0.0985  -0.0931 -0.0408 186 GLU B OE2 
5658 N N   . GLY B 187 ? 0.2671 0.1341 0.2560 0.0655  -0.0775 -0.0094 187 GLY B N   
5659 C CA  . GLY B 187 ? 0.2590 0.1224 0.2373 0.0611  -0.0747 -0.0023 187 GLY B CA  
5660 C C   . GLY B 187 ? 0.2716 0.1479 0.2446 0.0608  -0.0693 -0.0059 187 GLY B C   
5661 O O   . GLY B 187 ? 0.2837 0.1625 0.2468 0.0563  -0.0656 -0.0008 187 GLY B O   
5662 N N   . LYS B 188 ? 0.2342 0.1204 0.2132 0.0646  -0.0686 -0.0149 188 LYS B N   
5663 C CA  . LYS B 188 ? 0.2134 0.1117 0.1876 0.0626  -0.0636 -0.0180 188 LYS B CA  
5664 C C   . LYS B 188 ? 0.2023 0.1039 0.1752 0.0585  -0.0564 -0.0204 188 LYS B C   
5665 O O   . LYS B 188 ? 0.2357 0.1432 0.2025 0.0559  -0.0521 -0.0214 188 LYS B O   
5666 C CB  . LYS B 188 ? 0.2681 0.1778 0.2490 0.0672  -0.0661 -0.0254 188 LYS B CB  
5667 C CG  . LYS B 188 ? 0.2642 0.1756 0.2455 0.0714  -0.0727 -0.0235 188 LYS B CG  
5668 C CD  . LYS B 188 ? 0.3474 0.2734 0.3378 0.0765  -0.0749 -0.0318 188 LYS B CD  
5669 C CE  . LYS B 188 ? 0.4506 0.3835 0.4403 0.0797  -0.0806 -0.0300 188 LYS B CE  
5670 N NZ  . LYS B 188 ? 0.5092 0.4501 0.4894 0.0733  -0.0775 -0.0285 188 LYS B NZ  
5671 N N   . GLY B 189 ? 0.2181 0.1154 0.1964 0.0579  -0.0555 -0.0214 189 GLY B N   
5672 C CA  . GLY B 189 ? 0.2625 0.1636 0.2397 0.0543  -0.0492 -0.0227 189 GLY B CA  
5673 C C   . GLY B 189 ? 0.2320 0.1271 0.2149 0.0530  -0.0498 -0.0223 189 GLY B C   
5674 O O   . GLY B 189 ? 0.2245 0.1124 0.2136 0.0556  -0.0553 -0.0236 189 GLY B O   
5675 N N   . SER B 190 ? 0.2314 0.1292 0.2121 0.0490  -0.0445 -0.0205 190 SER B N   
5676 C CA  . SER B 190 ? 0.2866 0.1818 0.2729 0.0465  -0.0445 -0.0210 190 SER B CA  
5677 C C   . SER B 190 ? 0.2413 0.1461 0.2333 0.0480  -0.0422 -0.0291 190 SER B C   
5678 O O   . SER B 190 ? 0.2152 0.1288 0.2048 0.0488  -0.0388 -0.0313 190 SER B O   
5679 C CB  . SER B 190 ? 0.2698 0.1658 0.2511 0.0412  -0.0401 -0.0142 190 SER B CB  
5680 O OG  . SER B 190 ? 0.2519 0.1408 0.2272 0.0391  -0.0421 -0.0062 190 SER B OG  
5681 N N   . VAL B 191 ? 0.2369 0.1399 0.2363 0.0477  -0.0445 -0.0333 191 VAL B N   
5682 C CA  . VAL B 191 ? 0.2329 0.1469 0.2371 0.0482  -0.0421 -0.0405 191 VAL B CA  
5683 C C   . VAL B 191 ? 0.2559 0.1706 0.2618 0.0433  -0.0401 -0.0387 191 VAL B C   
5684 O O   . VAL B 191 ? 0.2733 0.1782 0.2819 0.0407  -0.0436 -0.0372 191 VAL B O   
5685 C CB  . VAL B 191 ? 0.1963 0.1139 0.2080 0.0517  -0.0459 -0.0485 191 VAL B CB  
5686 C CG1 . VAL B 191 ? 0.2271 0.1590 0.2425 0.0517  -0.0430 -0.0554 191 VAL B CG1 
5687 C CG2 . VAL B 191 ? 0.2171 0.1381 0.2278 0.0552  -0.0475 -0.0487 191 VAL B CG2 
5688 N N   . SER B 192 ? 0.1951 0.1212 0.1996 0.0417  -0.0349 -0.0387 192 SER B N   
5689 C CA  . SER B 192 ? 0.1892 0.1204 0.1958 0.0375  -0.0326 -0.0375 192 SER B CA  
5690 C C   . SER B 192 ? 0.2031 0.1447 0.2153 0.0382  -0.0327 -0.0455 192 SER B C   
5691 O O   . SER B 192 ? 0.1835 0.1295 0.1975 0.0419  -0.0340 -0.0516 192 SER B O   
5692 C CB  . SER B 192 ? 0.2153 0.1529 0.2162 0.0362  -0.0271 -0.0312 192 SER B CB  
5693 O OG  . SER B 192 ? 0.2002 0.1457 0.1989 0.0392  -0.0243 -0.0335 192 SER B OG  
5694 N N   . THR B 193 ? 0.2078 0.1553 0.2227 0.0343  -0.0314 -0.0453 193 THR B N   
5695 C CA  . THR B 193 ? 0.2028 0.1630 0.2216 0.0342  -0.0308 -0.0518 193 THR B CA  
5696 C C   . THR B 193 ? 0.2133 0.1842 0.2310 0.0311  -0.0267 -0.0468 193 THR B C   
5697 O O   . THR B 193 ? 0.1907 0.1594 0.2051 0.0297  -0.0242 -0.0394 193 THR B O   
5698 C CB  . THR B 193 ? 0.2190 0.1751 0.2441 0.0333  -0.0358 -0.0600 193 THR B CB  
5699 O OG1 . THR B 193 ? 0.2363 0.2068 0.2644 0.0345  -0.0353 -0.0679 193 THR B OG1 
5700 C CG2 . THR B 193 ? 0.2222 0.1729 0.2498 0.0268  -0.0375 -0.0573 193 THR B CG2 
5701 N N   . SER B 194 ? 0.2035 0.1878 0.2238 0.0307  -0.0258 -0.0509 194 SER B N   
5702 C CA  . SER B 194 ? 0.2012 0.1980 0.2216 0.0285  -0.0227 -0.0470 194 SER B CA  
5703 C C   . SER B 194 ? 0.1793 0.1840 0.2054 0.0244  -0.0251 -0.0527 194 SER B C   
5704 O O   . SER B 194 ? 0.2000 0.2027 0.2290 0.0246  -0.0285 -0.0611 194 SER B O   
5705 C CB  . SER B 194 ? 0.2066 0.2136 0.2236 0.0316  -0.0198 -0.0455 194 SER B CB  
5706 O OG  . SER B 194 ? 0.1978 0.1966 0.2089 0.0347  -0.0179 -0.0406 194 SER B OG  
5707 N N   . PRO B 195 ? 0.1863 0.2018 0.2141 0.0209  -0.0234 -0.0489 195 PRO B N   
5708 C CA  . PRO B 195 ? 0.1601 0.1871 0.1926 0.0169  -0.0255 -0.0547 195 PRO B CA  
5709 C C   . PRO B 195 ? 0.1866 0.2217 0.2190 0.0197  -0.0265 -0.0626 195 PRO B C   
5710 O O   . PRO B 195 ? 0.1778 0.2181 0.2065 0.0235  -0.0240 -0.0601 195 PRO B O   
5711 C CB  . PRO B 195 ? 0.2265 0.2687 0.2594 0.0155  -0.0224 -0.0480 195 PRO B CB  
5712 C CG  . PRO B 195 ? 0.3257 0.3615 0.3551 0.0179  -0.0191 -0.0393 195 PRO B CG  
5713 C CD  . PRO B 195 ? 0.2111 0.2303 0.2366 0.0213  -0.0196 -0.0399 195 PRO B CD  
5714 N N   . TYR B 196 ? 0.1933 0.2307 0.2296 0.0172  -0.0301 -0.0721 196 TYR B N   
5715 C CA  . TYR B 196 ? 0.2261 0.2667 0.2629 0.0205  -0.0320 -0.0821 196 TYR B CA  
5716 C C   . TYR B 196 ? 0.1608 0.2176 0.1941 0.0232  -0.0289 -0.0806 196 TYR B C   
5717 O O   . TYR B 196 ? 0.1741 0.2296 0.2057 0.0271  -0.0285 -0.0828 196 TYR B O   
5718 C CB  . TYR B 196 ? 0.1804 0.2254 0.2214 0.0170  -0.0360 -0.0929 196 TYR B CB  
5719 C CG  . TYR B 196 ? 0.1958 0.2364 0.2386 0.0213  -0.0392 -0.1051 196 TYR B CG  
5720 C CD1 . TYR B 196 ? 0.1875 0.2442 0.2289 0.0251  -0.0376 -0.1105 196 TYR B CD1 
5721 C CD2 . TYR B 196 ? 0.2328 0.2537 0.2787 0.0218  -0.0441 -0.1111 196 TYR B CD2 
5722 C CE1 . TYR B 196 ? 0.2090 0.2650 0.2526 0.0301  -0.0401 -0.1220 196 TYR B CE1 
5723 C CE2 . TYR B 196 ? 0.2080 0.2255 0.2562 0.0274  -0.0470 -0.1218 196 TYR B CE2 
5724 C CZ  . TYR B 196 ? 0.2847 0.3214 0.3323 0.0315  -0.0439 -0.1248 196 TYR B CZ  
5725 O OH  . TYR B 196 ? 0.2637 0.3013 0.3148 0.0367  -0.0451 -0.1301 196 TYR B OH  
5726 N N   . TYR B 197 ? 0.1798 0.2532 0.2124 0.0208  -0.0272 -0.0772 197 TYR B N   
5727 C CA  . TYR B 197 ? 0.1311 0.2198 0.1601 0.0223  -0.0252 -0.0753 197 TYR B CA  
5728 C C   . TYR B 197 ? 0.1595 0.2465 0.1842 0.0240  -0.0220 -0.0631 197 TYR B C   
5729 O O   . TYR B 197 ? 0.1582 0.2580 0.1799 0.0240  -0.0208 -0.0588 197 TYR B O   
5730 C CB  . TYR B 197 ? 0.1532 0.2627 0.1834 0.0190  -0.0262 -0.0800 197 TYR B CB  
5731 C CG  . TYR B 197 ? 0.1526 0.2646 0.1859 0.0187  -0.0293 -0.0941 197 TYR B CG  
5732 C CD1 . TYR B 197 ? 0.1649 0.2830 0.1971 0.0219  -0.0292 -0.1009 197 TYR B CD1 
5733 C CD2 . TYR B 197 ? 0.2127 0.3202 0.2502 0.0153  -0.0326 -0.1010 197 TYR B CD2 
5734 C CE1 . TYR B 197 ? 0.1900 0.3105 0.2253 0.0232  -0.0321 -0.1151 197 TYR B CE1 
5735 C CE2 . TYR B 197 ? 0.1736 0.2808 0.2137 0.0159  -0.0360 -0.1149 197 TYR B CE2 
5736 C CZ  . TYR B 197 ? 0.2277 0.3411 0.2668 0.0207  -0.0357 -0.1225 197 TYR B CZ  
5737 O OH  . TYR B 197 ? 0.2832 0.3948 0.3266 0.0228  -0.0372 -0.1321 197 TYR B OH  
5738 N N   . HIS B 198 ? 0.1461 0.2173 0.1700 0.0256  -0.0210 -0.0576 198 HIS B N   
5739 C CA  . HIS B 198 ? 0.1892 0.2560 0.2086 0.0284  -0.0181 -0.0477 198 HIS B CA  
5740 C C   . HIS B 198 ? 0.1954 0.2755 0.2149 0.0281  -0.0171 -0.0415 198 HIS B C   
5741 O O   . HIS B 198 ? 0.1388 0.2232 0.1543 0.0301  -0.0161 -0.0358 198 HIS B O   
5742 C CB  . HIS B 198 ? 0.1875 0.2524 0.2022 0.0304  -0.0176 -0.0470 198 HIS B CB  
5743 C CG  . HIS B 198 ? 0.1376 0.1912 0.1470 0.0334  -0.0156 -0.0389 198 HIS B CG  
5744 N ND1 . HIS B 198 ? 0.1625 0.2203 0.1680 0.0346  -0.0145 -0.0315 198 HIS B ND1 
5745 C CD2 . HIS B 198 ? 0.1431 0.1809 0.1497 0.0355  -0.0150 -0.0375 198 HIS B CD2 
5746 C CE1 . HIS B 198 ? 0.1758 0.2197 0.1766 0.0375  -0.0133 -0.0267 198 HIS B CE1 
5747 N NE2 . HIS B 198 ? 0.1653 0.1980 0.1665 0.0378  -0.0134 -0.0303 198 HIS B NE2 
5748 N N   . PRO B 199 ? 0.1990 0.2858 0.2231 0.0254  -0.0177 -0.0419 199 PRO B N   
5749 C CA  . PRO B 199 ? 0.2076 0.3086 0.2326 0.0259  -0.0168 -0.0356 199 PRO B CA  
5750 C C   . PRO B 199 ? 0.2098 0.3040 0.2335 0.0303  -0.0142 -0.0273 199 PRO B C   
5751 O O   . PRO B 199 ? 0.1945 0.2737 0.2164 0.0318  -0.0128 -0.0267 199 PRO B O   
5752 C CB  . PRO B 199 ? 0.2045 0.3158 0.2354 0.0204  -0.0188 -0.0404 199 PRO B CB  
5753 C CG  . PRO B 199 ? 0.1626 0.2573 0.1953 0.0183  -0.0196 -0.0444 199 PRO B CG  
5754 C CD  . PRO B 199 ? 0.1911 0.2726 0.2199 0.0214  -0.0196 -0.0477 199 PRO B CD  
5755 N N   . LEU B 200 ? 0.1989 0.3059 0.2235 0.0326  -0.0136 -0.0213 200 LEU B N   
5756 C CA  . LEU B 200 ? 0.2380 0.3441 0.2630 0.0375  -0.0111 -0.0147 200 LEU B CA  
5757 C C   . LEU B 200 ? 0.1982 0.3145 0.2299 0.0331  -0.0110 -0.0157 200 LEU B C   
5758 O O   . LEU B 200 ? 0.1722 0.3066 0.2083 0.0321  -0.0118 -0.0137 200 LEU B O   
5759 C CB  . LEU B 200 ? 0.2331 0.3478 0.2564 0.0433  -0.0112 -0.0078 200 LEU B CB  
5760 C CG  . LEU B 200 ? 0.2622 0.3628 0.2781 0.0480  -0.0111 -0.0043 200 LEU B CG  
5761 C CD1 . LEU B 200 ? 0.2911 0.4007 0.3054 0.0514  -0.0128 0.0022  200 LEU B CD1 
5762 C CD2 . LEU B 200 ? 0.3001 0.3848 0.3128 0.0538  -0.0085 -0.0021 200 LEU B CD2 
5763 N N   . ILE B 201 ? 0.1657 0.2705 0.1980 0.0299  -0.0105 -0.0183 201 ILE B N   
5764 C CA  . ILE B 201 ? 0.1503 0.2624 0.1884 0.0238  -0.0108 -0.0186 201 ILE B CA  
5765 C C   . ILE B 201 ? 0.1445 0.2739 0.1864 0.0265  -0.0085 -0.0122 201 ILE B C   
5766 O O   . ILE B 201 ? 0.1632 0.3090 0.2111 0.0209  -0.0098 -0.0125 201 ILE B O   
5767 C CB  . ILE B 201 ? 0.1749 0.2698 0.2115 0.0209  -0.0104 -0.0197 201 ILE B CB  
5768 C CG1 . ILE B 201 ? 0.1921 0.2724 0.2269 0.0182  -0.0135 -0.0269 201 ILE B CG1 
5769 C CG2 . ILE B 201 ? 0.1995 0.3020 0.2414 0.0139  -0.0104 -0.0176 201 ILE B CG2 
5770 C CD1 . ILE B 201 ? 0.1809 0.2676 0.2206 0.0112  -0.0173 -0.0335 201 ILE B CD1 
5771 N N   . PRO B 202 ? 0.1479 0.2755 0.1867 0.0351  -0.0053 -0.0070 202 PRO B N   
5772 C CA  . PRO B 202 ? 0.1471 0.2938 0.1906 0.0387  -0.0033 -0.0018 202 PRO B CA  
5773 C C   . PRO B 202 ? 0.1685 0.3355 0.2166 0.0392  -0.0055 -0.0004 202 PRO B C   
5774 O O   . PRO B 202 ? 0.1644 0.3519 0.2192 0.0375  -0.0051 0.0020  202 PRO B O   
5775 C CB  . PRO B 202 ? 0.1535 0.2909 0.1916 0.0496  -0.0002 0.0016  202 PRO B CB  
5776 C CG  . PRO B 202 ? 0.1614 0.2759 0.1931 0.0479  0.0002  -0.0013 202 PRO B CG  
5777 C CD  . PRO B 202 ? 0.1658 0.2742 0.1972 0.0413  -0.0035 -0.0062 202 PRO B CD  
5778 N N   . ILE B 203 ? 0.1397 0.3035 0.1843 0.0411  -0.0079 -0.0013 203 ILE B N   
5779 C CA  . ILE B 203 ? 0.1174 0.3013 0.1654 0.0411  -0.0105 0.0006  203 ILE B CA  
5780 C C   . ILE B 203 ? 0.1907 0.3868 0.2437 0.0301  -0.0132 -0.0049 203 ILE B C   
5781 O O   . ILE B 203 ? 0.1728 0.3912 0.2318 0.0278  -0.0146 -0.0032 203 ILE B O   
5782 C CB  . ILE B 203 ? 0.1395 0.3164 0.1812 0.0455  -0.0122 0.0023  203 ILE B CB  
5783 C CG1 . ILE B 203 ? 0.1896 0.3566 0.2273 0.0567  -0.0105 0.0086  203 ILE B CG1 
5784 C CG2 . ILE B 203 ? 0.1706 0.3685 0.2148 0.0434  -0.0156 0.0038  203 ILE B CG2 
5785 C CD1 . ILE B 203 ? 0.2001 0.3567 0.2307 0.0600  -0.0126 0.0117  203 ILE B CD1 
5786 N N   . LEU B 204 ? 0.1210 0.3032 0.1719 0.0234  -0.0145 -0.0119 204 LEU B N   
5787 C CA  . LEU B 204 ? 0.1498 0.3407 0.2051 0.0132  -0.0177 -0.0184 204 LEU B CA  
5788 C C   . LEU B 204 ? 0.1844 0.3860 0.2465 0.0076  -0.0172 -0.0164 204 LEU B C   
5789 O O   . LEU B 204 ? 0.1493 0.3687 0.2166 0.0006  -0.0198 -0.0183 204 LEU B O   
5790 C CB  . LEU B 204 ? 0.1465 0.3179 0.1986 0.0087  -0.0193 -0.0267 204 LEU B CB  
5791 C CG  . LEU B 204 ? 0.1612 0.3249 0.2073 0.0125  -0.0199 -0.0299 204 LEU B CG  
5792 C CD1 . LEU B 204 ? 0.1937 0.3423 0.2387 0.0083  -0.0219 -0.0394 204 LEU B CD1 
5793 C CD2 . LEU B 204 ? 0.1582 0.3425 0.2043 0.0122  -0.0219 -0.0299 204 LEU B CD2 
5794 N N   . LEU B 205 ? 0.1486 0.3416 0.2105 0.0099  -0.0139 -0.0124 205 LEU B N   
5795 C CA  . LEU B 205 ? 0.1378 0.3434 0.2059 0.0038  -0.0130 -0.0094 205 LEU B CA  
5796 C C   . LEU B 205 ? 0.1587 0.3913 0.2322 0.0086  -0.0116 -0.0033 205 LEU B C   
5797 O O   . LEU B 205 ? 0.1878 0.4403 0.2683 0.0013  -0.0126 -0.0022 205 LEU B O   
5798 C CB  . LEU B 205 ? 0.1440 0.3347 0.2095 0.0048  -0.0096 -0.0065 205 LEU B CB  
5799 C CG  . LEU B 205 ? 0.1689 0.3350 0.2308 -0.0018 -0.0118 -0.0116 205 LEU B CG  
5800 C CD1 . LEU B 205 ? 0.1362 0.2883 0.1941 0.0011  -0.0084 -0.0076 205 LEU B CD1 
5801 C CD2 . LEU B 205 ? 0.2046 0.3742 0.2717 -0.0150 -0.0159 -0.0150 205 LEU B CD2 
5802 N N   . ASN B 206 ? 0.1431 0.3767 0.2138 0.0208  -0.0095 0.0009  206 ASN B N   
5803 C CA  . ASN B 206 ? 0.1902 0.4483 0.2664 0.0276  -0.0082 0.0069  206 ASN B CA  
5804 C C   . ASN B 206 ? 0.1641 0.4180 0.2358 0.0404  -0.0082 0.0103  206 ASN B C   
5805 O O   . ASN B 206 ? 0.1617 0.4029 0.2292 0.0499  -0.0052 0.0127  206 ASN B O   
5806 C CB  . ASN B 206 ? 0.1906 0.4553 0.2699 0.0297  -0.0038 0.0106  206 ASN B CB  
5807 C CG  . ASN B 206 ? 0.2901 0.5789 0.3748 0.0403  -0.0021 0.0161  206 ASN B CG  
5808 O OD1 . ASN B 206 ? 0.2242 0.5306 0.3128 0.0423  -0.0050 0.0178  206 ASN B OD1 
5809 N ND2 . ASN B 206 ? 0.2886 0.5788 0.3732 0.0480  0.0025  0.0188  206 ASN B ND2 
5810 N N   . PRO B 207 ? 0.1826 0.4461 0.2543 0.0406  -0.0119 0.0107  207 PRO B N   
5811 C CA  . PRO B 207 ? 0.1842 0.4420 0.2510 0.0518  -0.0127 0.0154  207 PRO B CA  
5812 C C   . PRO B 207 ? 0.1811 0.4457 0.2502 0.0649  -0.0105 0.0217  207 PRO B C   
5813 O O   . PRO B 207 ? 0.2027 0.4530 0.2662 0.0749  -0.0107 0.0250  207 PRO B O   
5814 C CB  . PRO B 207 ? 0.1826 0.4584 0.2510 0.0479  -0.0172 0.0158  207 PRO B CB  
5815 C CG  . PRO B 207 ? 0.1890 0.4652 0.2586 0.0342  -0.0187 0.0078  207 PRO B CG  
5816 C CD  . PRO B 207 ? 0.1790 0.4562 0.2538 0.0299  -0.0159 0.0065  207 PRO B CD  
5817 N N   . ASN B 208 ? 0.1384 0.4246 0.2156 0.0652  -0.0087 0.0232  208 ASN B N   
5818 C CA  . ASN B 208 ? 0.1815 0.4687 0.2576 0.0767  -0.0061 0.0274  208 ASN B CA  
5819 C C   . ASN B 208 ? 0.1638 0.4327 0.2359 0.0849  -0.0022 0.0265  208 ASN B C   
5820 O O   . ASN B 208 ? 0.1877 0.4527 0.2572 0.0957  -0.0003 0.0286  208 ASN B O   
5821 C CB  . ASN B 208 ? 0.2033 0.5149 0.2861 0.0725  -0.0047 0.0283  208 ASN B CB  
5822 C CG  . ASN B 208 ? 0.2343 0.5636 0.3200 0.0647  -0.0086 0.0290  208 ASN B CG  
5823 O OD1 . ASN B 208 ? 0.2800 0.6059 0.3620 0.0672  -0.0119 0.0309  208 ASN B OD1 
5824 N ND2 . ASN B 208 ? 0.2546 0.6026 0.3462 0.0545  -0.0084 0.0277  208 ASN B ND2 
5825 N N   . CYS B 209 ? 0.1657 0.4184 0.2346 0.0786  -0.0008 0.0224  209 CYS B N   
5826 C CA  . CYS B 209 ? 0.2116 0.4442 0.2743 0.0850  0.0029  0.0211  209 CYS B CA  
5827 C C   . CYS B 209 ? 0.2452 0.4573 0.3003 0.0966  0.0015  0.0228  209 CYS B C   
5828 O O   . CYS B 209 ? 0.1917 0.3903 0.2422 0.1051  0.0042  0.0219  209 CYS B O   
5829 C CB  . CYS B 209 ? 0.2292 0.4437 0.2873 0.0739  0.0040  0.0165  209 CYS B CB  
5830 S SG  . CYS B 209 ? 0.2637 0.4524 0.3138 0.0683  0.0003  0.0132  209 CYS B SG  
5831 N N   . VAL B 210 ? 0.1944 0.4048 0.2480 0.0969  -0.0029 0.0255  210 VAL B N   
5832 C CA  . VAL B 210 ? 0.1888 0.3795 0.2351 0.1067  -0.0049 0.0285  210 VAL B CA  
5833 C C   . VAL B 210 ? 0.2116 0.4021 0.2572 0.1178  -0.0038 0.0308  210 VAL B C   
5834 O O   . VAL B 210 ? 0.2671 0.4356 0.3057 0.1258  -0.0043 0.0313  210 VAL B O   
5835 C CB  . VAL B 210 ? 0.2366 0.4275 0.2807 0.1024  -0.0100 0.0318  210 VAL B CB  
5836 C CG1 . VAL B 210 ? 0.2379 0.4266 0.2806 0.0878  -0.0103 0.0267  210 VAL B CG1 
5837 C CG2 . VAL B 210 ? 0.2563 0.4699 0.3061 0.1041  -0.0123 0.0363  210 VAL B CG2 
5838 N N   . TYR B 211 ? 0.1863 0.4002 0.2388 0.1178  -0.0026 0.0317  211 TYR B N   
5839 C CA  . TYR B 211 ? 0.2247 0.4406 0.2772 0.1285  -0.0018 0.0331  211 TYR B CA  
5840 C C   . TYR B 211 ? 0.2505 0.4587 0.3002 0.1340  0.0029  0.0287  211 TYR B C   
5841 O O   . TYR B 211 ? 0.2429 0.4500 0.2917 0.1439  0.0036  0.0285  211 TYR B O   
5842 C CB  . TYR B 211 ? 0.2268 0.4721 0.2873 0.1265  -0.0022 0.0355  211 TYR B CB  
5843 C CG  . TYR B 211 ? 0.2749 0.5279 0.3369 0.1209  -0.0070 0.0395  211 TYR B CG  
5844 C CD1 . TYR B 211 ? 0.2406 0.4800 0.2980 0.1267  -0.0111 0.0440  211 TYR B CD1 
5845 C CD2 . TYR B 211 ? 0.2832 0.5565 0.3506 0.1088  -0.0077 0.0386  211 TYR B CD2 
5846 C CE1 . TYR B 211 ? 0.2323 0.4803 0.2902 0.1211  -0.0154 0.0480  211 TYR B CE1 
5847 C CE2 . TYR B 211 ? 0.2993 0.5802 0.3670 0.1033  -0.0119 0.0412  211 TYR B CE2 
5848 C CZ  . TYR B 211 ? 0.3259 0.5951 0.3886 0.1095  -0.0155 0.0461  211 TYR B CZ  
5849 O OH  . TYR B 211 ? 0.4288 0.7075 0.4910 0.1036  -0.0196 0.0491  211 TYR B OH  
5850 N N   . GLU B 212 ? 0.1896 0.3927 0.2380 0.1280  0.0059  0.0251  212 GLU B N   
5851 C CA  . GLU B 212 ? 0.2849 0.4811 0.3295 0.1327  0.0103  0.0210  212 GLU B CA  
5852 C C   . GLU B 212 ? 0.3251 0.4916 0.3600 0.1414  0.0092  0.0192  212 GLU B C   
5853 O O   . GLU B 212 ? 0.3499 0.5121 0.3815 0.1486  0.0117  0.0159  212 GLU B O   
5854 C CB  . GLU B 212 ? 0.2548 0.4536 0.3004 0.1235  0.0135  0.0184  212 GLU B CB  
5855 C CG  . GLU B 212 ? 0.2772 0.5056 0.3328 0.1141  0.0147  0.0199  212 GLU B CG  
5856 C CD  . GLU B 212 ? 0.3225 0.5544 0.3803 0.1042  0.0176  0.0181  212 GLU B CD  
5857 O OE1 . GLU B 212 ? 0.3837 0.6348 0.4491 0.0930  0.0171  0.0194  212 GLU B OE1 
5858 O OE2 . GLU B 212 ? 0.3089 0.5210 0.3591 0.1053  0.0196  0.0153  212 GLU B OE2 
5859 N N   . THR B 213 ? 0.3013 0.4482 0.3315 0.1402  0.0053  0.0211  213 THR B N   
5860 C CA  . THR B 213 ? 0.3290 0.4466 0.3501 0.1464  0.0033  0.0200  213 THR B CA  
5861 C C   . THR B 213 ? 0.3267 0.4368 0.3472 0.1516  -0.0019 0.0251  213 THR B C   
5862 O O   . THR B 213 ? 0.4093 0.4993 0.4244 0.1587  -0.0036 0.0243  213 THR B O   
5863 C CB  . THR B 213 ? 0.3391 0.4359 0.3535 0.1400  0.0028  0.0183  213 THR B CB  
5864 O OG1 . THR B 213 ? 0.3747 0.4789 0.3924 0.1327  -0.0001 0.0220  213 THR B OG1 
5865 C CG2 . THR B 213 ? 0.3195 0.4186 0.3328 0.1365  0.0076  0.0133  213 THR B CG2 
5866 N N   . THR B 214 ? 0.3001 0.4251 0.3258 0.1476  -0.0048 0.0304  214 THR B N   
5867 C CA  . THR B 214 ? 0.2973 0.4164 0.3222 0.1514  -0.0103 0.0366  214 THR B CA  
5868 C C   . THR B 214 ? 0.2741 0.4220 0.3078 0.1517  -0.0111 0.0402  214 THR B C   
5869 O O   . THR B 214 ? 0.2978 0.4593 0.3344 0.1444  -0.0133 0.0439  214 THR B O   
5870 C CB  . THR B 214 ? 0.2981 0.4041 0.3180 0.1445  -0.0142 0.0405  214 THR B CB  
5871 O OG1 . THR B 214 ? 0.2908 0.4163 0.3152 0.1348  -0.0134 0.0403  214 THR B OG1 
5872 C CG2 . THR B 214 ? 0.3000 0.3773 0.3109 0.1437  -0.0137 0.0370  214 THR B CG2 
5873 N N   . PRO B 215 ? 0.3193 0.4778 0.3570 0.1600  -0.0095 0.0390  215 PRO B N   
5874 C CA  . PRO B 215 ? 0.3196 0.5077 0.3658 0.1599  -0.0099 0.0420  215 PRO B CA  
5875 C C   . PRO B 215 ? 0.3480 0.5377 0.3951 0.1613  -0.0158 0.0494  215 PRO B C   
5876 O O   . PRO B 215 ? 0.3559 0.5707 0.4093 0.1581  -0.0167 0.0523  215 PRO B O   
5877 C CB  . PRO B 215 ? 0.3572 0.5529 0.4061 0.1700  -0.0069 0.0386  215 PRO B CB  
5878 C CG  . PRO B 215 ? 0.3720 0.5375 0.4133 0.1779  -0.0074 0.0355  215 PRO B CG  
5879 C CD  . PRO B 215 ? 0.3546 0.4997 0.3890 0.1696  -0.0073 0.0342  215 PRO B CD  
5880 N N   . ASN B 216 ? 0.3573 0.5216 0.3982 0.1652  -0.0202 0.0529  216 ASN B N   
5881 C CA  . ASN B 216 ? 0.3944 0.5593 0.4357 0.1666  -0.0265 0.0611  216 ASN B CA  
5882 C C   . ASN B 216 ? 0.3985 0.5642 0.4364 0.1554  -0.0293 0.0654  216 ASN B C   
5883 O O   . ASN B 216 ? 0.4650 0.6306 0.5017 0.1549  -0.0347 0.0729  216 ASN B O   
5884 C CB  . ASN B 216 ? 0.4566 0.5939 0.4933 0.1764  -0.0308 0.0638  216 ASN B CB  
5885 C CG  . ASN B 216 ? 0.5300 0.6696 0.5708 0.1887  -0.0290 0.0597  216 ASN B CG  
5886 O OD1 . ASN B 216 ? 0.6073 0.7279 0.6443 0.1939  -0.0271 0.0541  216 ASN B OD1 
5887 N ND2 . ASN B 216 ? 0.5456 0.7099 0.5941 0.1932  -0.0295 0.0619  216 ASN B ND2 
5888 N N   . VAL B 217 ? 0.4074 0.5748 0.4439 0.1463  -0.0260 0.0610  217 VAL B N   
5889 C CA  . VAL B 217 ? 0.4192 0.5886 0.4524 0.1359  -0.0286 0.0641  217 VAL B CA  
5890 C C   . VAL B 217 ? 0.3553 0.5551 0.3947 0.1296  -0.0297 0.0662  217 VAL B C   
5891 O O   . VAL B 217 ? 0.3251 0.5457 0.3716 0.1297  -0.0269 0.0631  217 VAL B O   
5892 C CB  . VAL B 217 ? 0.3738 0.5354 0.4043 0.1292  -0.0252 0.0578  217 VAL B CB  
5893 C CG1 . VAL B 217 ? 0.3082 0.4919 0.3459 0.1239  -0.0206 0.0515  217 VAL B CG1 
5894 C CG2 . VAL B 217 ? 0.4040 0.5612 0.4289 0.1205  -0.0284 0.0608  217 VAL B CG2 
5895 N N   . LYS B 218 ? 0.3056 0.5083 0.3415 0.1234  -0.0340 0.0717  218 LYS B N   
5896 C CA  . LYS B 218 ? 0.2940 0.5244 0.3340 0.1150  -0.0351 0.0725  218 LYS B CA  
5897 C C   . LYS B 218 ? 0.2420 0.4784 0.2808 0.1030  -0.0336 0.0667  218 LYS B C   
5898 O O   . LYS B 218 ? 0.2608 0.4811 0.2931 0.1001  -0.0346 0.0670  218 LYS B O   
5899 C CB  . LYS B 218 ? 0.3748 0.6071 0.4112 0.1149  -0.0408 0.0816  218 LYS B CB  
5900 C CG  . LYS B 218 ? 0.5125 0.7358 0.5498 0.1271  -0.0438 0.0878  218 LYS B CG  
5901 C CD  . LYS B 218 ? 0.6182 0.8344 0.6497 0.1263  -0.0503 0.0978  218 LYS B CD  
5902 C CE  . LYS B 218 ? 0.6654 0.9037 0.7017 0.1283  -0.0533 0.1030  218 LYS B CE  
5903 N NZ  . LYS B 218 ? 0.7309 0.9534 0.7657 0.1390  -0.0591 0.1114  218 LYS B NZ  
5904 N N   . ILE B 219 ? 0.2154 0.4742 0.2603 0.0958  -0.0316 0.0612  219 ILE B N   
5905 C CA  . ILE B 219 ? 0.1909 0.4558 0.2354 0.0840  -0.0309 0.0544  219 ILE B CA  
5906 C C   . ILE B 219 ? 0.1788 0.4682 0.2257 0.0750  -0.0325 0.0532  219 ILE B C   
5907 O O   . ILE B 219 ? 0.1841 0.4882 0.2348 0.0777  -0.0331 0.0567  219 ILE B O   
5908 C CB  . ILE B 219 ? 0.2404 0.5034 0.2897 0.0822  -0.0267 0.0465  219 ILE B CB  
5909 C CG1 . ILE B 219 ? 0.2176 0.5010 0.2747 0.0807  -0.0247 0.0444  219 ILE B CG1 
5910 C CG2 . ILE B 219 ? 0.2260 0.4650 0.2723 0.0916  -0.0245 0.0470  219 ILE B CG2 
5911 C CD1 . ILE B 219 ? 0.2210 0.5053 0.2831 0.0762  -0.0210 0.0374  219 ILE B CD1 
5912 N N   . PRO B 220 ? 0.2156 0.5098 0.2599 0.0643  -0.0333 0.0478  220 PRO B N   
5913 C CA  . PRO B 220 ? 0.2383 0.5540 0.2836 0.0553  -0.0346 0.0453  220 PRO B CA  
5914 C C   . PRO B 220 ? 0.1701 0.4998 0.2228 0.0506  -0.0327 0.0390  220 PRO B C   
5915 O O   . PRO B 220 ? 0.1596 0.4837 0.2169 0.0531  -0.0301 0.0364  220 PRO B O   
5916 C CB  . PRO B 220 ? 0.2772 0.5905 0.3169 0.0461  -0.0355 0.0394  220 PRO B CB  
5917 C CG  . PRO B 220 ? 0.2555 0.5494 0.2939 0.0485  -0.0341 0.0365  220 PRO B CG  
5918 C CD  . PRO B 220 ? 0.2503 0.5300 0.2894 0.0606  -0.0334 0.0441  220 PRO B CD  
5919 N N   . ASP B 221 ? 0.1521 0.5005 0.2052 0.0430  -0.0341 0.0368  221 ASP B N   
5920 C CA  . ASP B 221 ? 0.1523 0.5152 0.2113 0.0360  -0.0333 0.0310  221 ASP B CA  
5921 C C   . ASP B 221 ? 0.1458 0.5021 0.2052 0.0259  -0.0327 0.0200  221 ASP B C   
5922 O O   . ASP B 221 ? 0.1566 0.5153 0.2119 0.0181  -0.0342 0.0140  221 ASP B O   
5923 C CB  . ASP B 221 ? 0.1580 0.5417 0.2163 0.0318  -0.0354 0.0328  221 ASP B CB  
5924 C CG  . ASP B 221 ? 0.1868 0.5863 0.2509 0.0246  -0.0350 0.0279  221 ASP B CG  
5925 O OD1 . ASP B 221 ? 0.1634 0.5610 0.2332 0.0257  -0.0331 0.0269  221 ASP B OD1 
5926 O OD2 . ASP B 221 ? 0.2586 0.6731 0.3212 0.0173  -0.0368 0.0254  221 ASP B OD2 
5927 N N   . PHE B 222 ? 0.1367 0.4848 0.2010 0.0262  -0.0307 0.0170  222 PHE B N   
5928 C CA  . PHE B 222 ? 0.1593 0.4999 0.2252 0.0169  -0.0307 0.0069  222 PHE B CA  
5929 C C   . PHE B 222 ? 0.2075 0.5624 0.2774 0.0061  -0.0320 0.0013  222 PHE B C   
5930 O O   . PHE B 222 ? 0.1936 0.5509 0.2698 0.0020  -0.0310 -0.0003 222 PHE B O   
5931 C CB  . PHE B 222 ? 0.1541 0.4811 0.2238 0.0210  -0.0281 0.0070  222 PHE B CB  
5932 C CG  . PHE B 222 ? 0.1741 0.4832 0.2389 0.0280  -0.0276 0.0084  222 PHE B CG  
5933 C CD1 . PHE B 222 ? 0.1727 0.4764 0.2341 0.0393  -0.0270 0.0173  222 PHE B CD1 
5934 C CD2 . PHE B 222 ? 0.1913 0.4862 0.2536 0.0228  -0.0278 0.0005  222 PHE B CD2 
5935 C CE1 . PHE B 222 ? 0.1758 0.4621 0.2320 0.0449  -0.0270 0.0190  222 PHE B CE1 
5936 C CE2 . PHE B 222 ? 0.1716 0.4444 0.2265 0.0280  -0.0262 0.0018  222 PHE B CE2 
5937 C CZ  . PHE B 222 ? 0.1725 0.4412 0.2242 0.0384  -0.0258 0.0111  222 PHE B CZ  
5938 N N   . ALA B 223 ? 0.1936 0.5582 0.2593 0.0009  -0.0341 -0.0016 223 ALA B N   
5939 C CA  . ALA B 223 ? 0.2332 0.6120 0.3016 -0.0090 -0.0358 -0.0066 223 ALA B CA  
5940 C C   . ALA B 223 ? 0.2576 0.6269 0.3280 -0.0198 -0.0372 -0.0182 223 ALA B C   
5941 O O   . ALA B 223 ? 0.2905 0.6691 0.3626 -0.0290 -0.0392 -0.0234 223 ALA B O   
5942 C CB  . ALA B 223 ? 0.2846 0.6769 0.3474 -0.0106 -0.0375 -0.0062 223 ALA B CB  
5943 N N   . VAL B 224 ? 0.1639 0.5148 0.2340 -0.0190 -0.0366 -0.0224 224 VAL B N   
5944 C CA  . VAL B 224 ? 0.1789 0.5181 0.2517 -0.0284 -0.0384 -0.0329 224 VAL B CA  
5945 C C   . VAL B 224 ? 0.1814 0.5073 0.2586 -0.0255 -0.0368 -0.0309 224 VAL B C   
5946 O O   . VAL B 224 ? 0.1957 0.5179 0.2720 -0.0155 -0.0342 -0.0238 224 VAL B O   
5947 C CB  . VAL B 224 ? 0.2494 0.5784 0.3160 -0.0312 -0.0401 -0.0435 224 VAL B CB  
5948 C CG1 . VAL B 224 ? 0.4668 0.8104 0.5288 -0.0336 -0.0411 -0.0452 224 VAL B CG1 
5949 C CG2 . VAL B 224 ? 0.3137 0.6313 0.3756 -0.0226 -0.0383 -0.0415 224 VAL B CG2 
5950 N N   . SER B 225 ? 0.1748 0.4926 0.2565 -0.0348 -0.0385 -0.0372 225 SER B N   
5951 C CA  . SER B 225 ? 0.1455 0.4484 0.2303 -0.0336 -0.0366 -0.0354 225 SER B CA  
5952 C C   . SER B 225 ? 0.1917 0.4661 0.2694 -0.0310 -0.0362 -0.0423 225 SER B C   
5953 O O   . SER B 225 ? 0.1858 0.4541 0.2616 -0.0369 -0.0398 -0.0529 225 SER B O   
5954 C CB  . SER B 225 ? 0.2186 0.5209 0.3094 -0.0453 -0.0381 -0.0368 225 SER B CB  
5955 O OG  . SER B 225 ? 0.2271 0.5064 0.3166 -0.0437 -0.0349 -0.0339 225 SER B OG  
5956 N N   . PHE B 226 ? 0.1512 0.4092 0.2254 -0.0220 -0.0321 -0.0367 226 PHE B N   
5957 C CA  . PHE B 226 ? 0.1696 0.4007 0.2379 -0.0192 -0.0313 -0.0418 226 PHE B CA  
5958 C C   . PHE B 226 ? 0.1824 0.3927 0.2517 -0.0219 -0.0300 -0.0409 226 PHE B C   
5959 O O   . PHE B 226 ? 0.1725 0.3607 0.2372 -0.0180 -0.0288 -0.0428 226 PHE B O   
5960 C CB  . PHE B 226 ? 0.1464 0.3729 0.2089 -0.0080 -0.0282 -0.0364 226 PHE B CB  
5961 C CG  . PHE B 226 ? 0.1784 0.4196 0.2377 -0.0061 -0.0301 -0.0380 226 PHE B CG  
5962 C CD1 . PHE B 226 ? 0.1893 0.4251 0.2447 -0.0085 -0.0321 -0.0476 226 PHE B CD1 
5963 C CD2 . PHE B 226 ? 0.2147 0.4761 0.2748 -0.0015 -0.0299 -0.0297 226 PHE B CD2 
5964 C CE1 . PHE B 226 ? 0.1673 0.4189 0.2189 -0.0075 -0.0335 -0.0487 226 PHE B CE1 
5965 C CE2 . PHE B 226 ? 0.2408 0.5165 0.2972 -0.0004 -0.0320 -0.0298 226 PHE B CE2 
5966 C CZ  . PHE B 226 ? 0.1525 0.4241 0.2044 -0.0041 -0.0336 -0.0392 226 PHE B CZ  
5967 N N   . ARG B 227 ? 0.1962 0.4148 0.2712 -0.0288 -0.0302 -0.0372 227 ARG B N   
5968 C CA  . ARG B 227 ? 0.1618 0.3636 0.2373 -0.0319 -0.0287 -0.0341 227 ARG B CA  
5969 C C   . ARG B 227 ? 0.1706 0.3480 0.2443 -0.0386 -0.0326 -0.0427 227 ARG B C   
5970 O O   . ARG B 227 ? 0.1712 0.3265 0.2415 -0.0361 -0.0314 -0.0416 227 ARG B O   
5971 C CB  . ARG B 227 ? 0.1851 0.4057 0.2675 -0.0391 -0.0282 -0.0278 227 ARG B CB  
5972 C CG  . ARG B 227 ? 0.2721 0.5144 0.3568 -0.0300 -0.0237 -0.0188 227 ARG B CG  
5973 C CD  . ARG B 227 ? 0.2763 0.5401 0.3685 -0.0368 -0.0226 -0.0126 227 ARG B CD  
5974 N NE  . ARG B 227 ? 0.3440 0.5940 0.4357 -0.0421 -0.0208 -0.0094 227 ARG B NE  
5975 C CZ  . ARG B 227 ? 0.3776 0.6235 0.4667 -0.0341 -0.0157 -0.0033 227 ARG B CZ  
5976 N NH1 . ARG B 227 ? 0.2902 0.5424 0.3774 -0.0201 -0.0121 -0.0004 227 ARG B NH1 
5977 N NH2 . ARG B 227 ? 0.4345 0.6699 0.5228 -0.0403 -0.0145 0.0000  227 ARG B NH2 
5978 N N   . GLU B 228 ? 0.2088 0.3893 0.2845 -0.0468 -0.0378 -0.0515 228 GLU B N   
5979 C CA  . GLU B 228 ? 0.2397 0.3952 0.3136 -0.0514 -0.0421 -0.0608 228 GLU B CA  
5980 C C   . GLU B 228 ? 0.2300 0.3707 0.2982 -0.0415 -0.0412 -0.0664 228 GLU B C   
5981 O O   . GLU B 228 ? 0.2647 0.3811 0.3309 -0.0408 -0.0429 -0.0700 228 GLU B O   
5982 C CB  . GLU B 228 ? 0.2863 0.4478 0.3633 -0.0619 -0.0482 -0.0705 228 GLU B CB  
5983 C CG  . GLU B 228 ? 0.5139 0.6801 0.5965 -0.0750 -0.0506 -0.0661 228 GLU B CG  
5984 C CD  . GLU B 228 ? 0.7645 0.9013 0.8467 -0.0830 -0.0553 -0.0694 228 GLU B CD  
5985 O OE1 . GLU B 228 ? 0.8348 0.9554 0.9152 -0.0805 -0.0529 -0.0622 228 GLU B OE1 
5986 O OE2 . GLU B 228 ? 0.8705 1.0001 0.9540 -0.0917 -0.0617 -0.0793 228 GLU B OE2 
5987 N N   . ASP B 229 ? 0.2102 0.3655 0.2758 -0.0340 -0.0389 -0.0665 229 ASP B N   
5988 C CA  . ASP B 229 ? 0.1953 0.3388 0.2556 -0.0254 -0.0377 -0.0706 229 ASP B CA  
5989 C C   . ASP B 229 ? 0.1733 0.3004 0.2308 -0.0190 -0.0339 -0.0628 229 ASP B C   
5990 O O   . ASP B 229 ? 0.1929 0.3019 0.2474 -0.0151 -0.0342 -0.0668 229 ASP B O   
5991 C CB  . ASP B 229 ? 0.1925 0.3561 0.2501 -0.0201 -0.0361 -0.0703 229 ASP B CB  
5992 C CG  . ASP B 229 ? 0.2576 0.4344 0.3156 -0.0247 -0.0401 -0.0816 229 ASP B CG  
5993 O OD1 . ASP B 229 ? 0.2578 0.4257 0.3179 -0.0313 -0.0444 -0.0912 229 ASP B OD1 
5994 O OD2 . ASP B 229 ? 0.2363 0.4318 0.2917 -0.0217 -0.0393 -0.0808 229 ASP B OD2 
5995 N N   . ALA B 230 ? 0.1770 0.3113 0.2355 -0.0175 -0.0302 -0.0521 230 ALA B N   
5996 C CA  . ALA B 230 ? 0.1732 0.2923 0.2285 -0.0121 -0.0268 -0.0455 230 ALA B CA  
5997 C C   . ALA B 230 ? 0.2211 0.3180 0.2765 -0.0170 -0.0294 -0.0480 230 ALA B C   
5998 O O   . ALA B 230 ? 0.2146 0.2937 0.2662 -0.0123 -0.0289 -0.0486 230 ALA B O   
5999 C CB  . ALA B 230 ? 0.1874 0.3197 0.2443 -0.0101 -0.0228 -0.0350 230 ALA B CB  
6000 N N   . SER B 231 ? 0.2271 0.3247 0.2870 -0.0270 -0.0327 -0.0493 231 SER B N   
6001 C CA  . SER B 231 ? 0.2237 0.2984 0.2836 -0.0326 -0.0364 -0.0512 231 SER B CA  
6002 C C   . SER B 231 ? 0.2755 0.3332 0.3335 -0.0295 -0.0404 -0.0623 231 SER B C   
6003 O O   . SER B 231 ? 0.2779 0.3145 0.3336 -0.0268 -0.0417 -0.0626 231 SER B O   
6004 C CB  . SER B 231 ? 0.2553 0.3341 0.3203 -0.0454 -0.0402 -0.0506 231 SER B CB  
6005 O OG  . SER B 231 ? 0.4347 0.5200 0.5009 -0.0493 -0.0371 -0.0394 231 SER B OG  
6006 N N   . LYS B 232 ? 0.2168 0.2852 0.2758 -0.0293 -0.0425 -0.0716 232 LYS B N   
6007 C CA  . LYS B 232 ? 0.2497 0.3059 0.3075 -0.0255 -0.0460 -0.0837 232 LYS B CA  
6008 C C   . LYS B 232 ? 0.2459 0.2949 0.2994 -0.0151 -0.0428 -0.0824 232 LYS B C   
6009 O O   . LYS B 232 ? 0.2280 0.2586 0.2807 -0.0118 -0.0455 -0.0879 232 LYS B O   
6010 C CB  . LYS B 232 ? 0.2428 0.3171 0.3015 -0.0266 -0.0478 -0.0935 232 LYS B CB  
6011 C CG  . LYS B 232 ? 0.4320 0.5035 0.4943 -0.0364 -0.0538 -0.1021 232 LYS B CG  
6012 C CD  . LYS B 232 ? 0.5002 0.5886 0.5623 -0.0362 -0.0558 -0.1143 232 LYS B CD  
6013 C CE  . LYS B 232 ? 0.5777 0.6552 0.6375 -0.0286 -0.0577 -0.1268 232 LYS B CE  
6014 N NZ  . LYS B 232 ? 0.6433 0.6907 0.7045 -0.0290 -0.0627 -0.1320 232 LYS B NZ  
6015 N N   . HIS B 233 ? 0.1860 0.2487 0.2368 -0.0099 -0.0375 -0.0751 233 HIS B N   
6016 C CA  . HIS B 233 ? 0.1593 0.2146 0.2058 -0.0014 -0.0348 -0.0733 233 HIS B CA  
6017 C C   . HIS B 233 ? 0.1608 0.1944 0.2061 -0.0006 -0.0353 -0.0690 233 HIS B C   
6018 O O   . HIS B 233 ? 0.1813 0.2022 0.2248 0.0043  -0.0365 -0.0728 233 HIS B O   
6019 C CB  . HIS B 233 ? 0.1629 0.2321 0.2064 0.0031  -0.0297 -0.0645 233 HIS B CB  
6020 C CG  . HIS B 233 ? 0.1487 0.2374 0.1913 0.0047  -0.0291 -0.0675 233 HIS B CG  
6021 N ND1 . HIS B 233 ? 0.1561 0.2467 0.1956 0.0092  -0.0288 -0.0722 233 HIS B ND1 
6022 C CD2 . HIS B 233 ? 0.1668 0.2756 0.2109 0.0022  -0.0286 -0.0651 233 HIS B CD2 
6023 C CE1 . HIS B 233 ? 0.1463 0.2568 0.1850 0.0088  -0.0283 -0.0724 233 HIS B CE1 
6024 N NE2 . HIS B 233 ? 0.1612 0.2825 0.2026 0.0050  -0.0284 -0.0681 233 HIS B NE2 
6025 N N   . VAL B 234 ? 0.2057 0.2369 0.2519 -0.0055 -0.0344 -0.0605 234 VAL B N   
6026 C CA  . VAL B 234 ? 0.1839 0.1964 0.2280 -0.0055 -0.0348 -0.0551 234 VAL B CA  
6027 C C   . VAL B 234 ? 0.2334 0.2265 0.2798 -0.0091 -0.0412 -0.0616 234 VAL B C   
6028 O O   . VAL B 234 ? 0.2226 0.1984 0.2669 -0.0050 -0.0431 -0.0623 234 VAL B O   
6029 C CB  . VAL B 234 ? 0.1891 0.2078 0.2333 -0.0100 -0.0317 -0.0442 234 VAL B CB  
6030 C CG1 . VAL B 234 ? 0.2138 0.2143 0.2549 -0.0108 -0.0323 -0.0382 234 VAL B CG1 
6031 C CG2 . VAL B 234 ? 0.1994 0.2345 0.2411 -0.0038 -0.0258 -0.0386 234 VAL B CG2 
6032 N N   . GLU B 235 ? 0.2358 0.2309 0.2863 -0.0165 -0.0452 -0.0669 235 GLU B N   
6033 C CA  . GLU B 235 ? 0.2596 0.2335 0.3122 -0.0203 -0.0523 -0.0734 235 GLU B CA  
6034 C C   . GLU B 235 ? 0.3036 0.2691 0.3559 -0.0117 -0.0549 -0.0850 235 GLU B C   
6035 O O   . GLU B 235 ? 0.2638 0.2081 0.3159 -0.0087 -0.0591 -0.0870 235 GLU B O   
6036 C CB  . GLU B 235 ? 0.2851 0.2639 0.3418 -0.0306 -0.0562 -0.0776 235 GLU B CB  
6037 C CG  . GLU B 235 ? 0.4795 0.4327 0.5380 -0.0368 -0.0640 -0.0814 235 GLU B CG  
6038 C CD  . GLU B 235 ? 0.6162 0.5511 0.6724 -0.0390 -0.0648 -0.0699 235 GLU B CD  
6039 O OE1 . GLU B 235 ? 0.6148 0.5604 0.6699 -0.0432 -0.0602 -0.0578 235 GLU B OE1 
6040 O OE2 . GLU B 235 ? 0.6704 0.5811 0.7260 -0.0360 -0.0701 -0.0731 235 GLU B OE2 
6041 N N   . LEU B 236 ? 0.2125 0.1958 0.2649 -0.0073 -0.0528 -0.0925 236 LEU B N   
6042 C CA  . LEU B 236 ? 0.2098 0.1900 0.2622 0.0010  -0.0546 -0.1039 236 LEU B CA  
6043 C C   . LEU B 236 ? 0.2323 0.2058 0.2817 0.0091  -0.0522 -0.0993 236 LEU B C   
6044 O O   . LEU B 236 ? 0.2521 0.2152 0.3024 0.0154  -0.0553 -0.1069 236 LEU B O   
6045 C CB  . LEU B 236 ? 0.1963 0.2007 0.2486 0.0027  -0.0522 -0.1113 236 LEU B CB  
6046 C CG  . LEU B 236 ? 0.2558 0.2673 0.3110 -0.0045 -0.0559 -0.1194 236 LEU B CG  
6047 C CD1 . LEU B 236 ? 0.2822 0.3203 0.3362 -0.0029 -0.0530 -0.1246 236 LEU B CD1 
6048 C CD2 . LEU B 236 ? 0.3339 0.3258 0.3915 -0.0043 -0.0628 -0.1314 236 LEU B CD2 
6049 N N   . ALA B 237 ? 0.2186 0.1989 0.2645 0.0095  -0.0468 -0.0878 237 ALA B N   
6050 C CA  . ALA B 237 ? 0.2112 0.1839 0.2538 0.0159  -0.0449 -0.0832 237 ALA B CA  
6051 C C   . ALA B 237 ? 0.2720 0.2213 0.3148 0.0154  -0.0493 -0.0802 237 ALA B C   
6052 O O   . ALA B 237 ? 0.2752 0.2147 0.3174 0.0218  -0.0512 -0.0828 237 ALA B O   
6053 C CB  . ALA B 237 ? 0.2082 0.1911 0.2466 0.0161  -0.0388 -0.0721 237 ALA B CB  
6054 N N   . LYS B 238 ? 0.2215 0.1628 0.2649 0.0075  -0.0509 -0.0738 238 LYS B N   
6055 C CA  . LYS B 238 ? 0.3136 0.2317 0.3569 0.0058  -0.0561 -0.0703 238 LYS B CA  
6056 C C   . LYS B 238 ? 0.3390 0.2421 0.3858 0.0102  -0.0630 -0.0821 238 LYS B C   
6057 O O   . LYS B 238 ? 0.3395 0.2268 0.3858 0.0155  -0.0665 -0.0817 238 LYS B O   
6058 C CB  . LYS B 238 ? 0.2657 0.1795 0.3097 -0.0053 -0.0574 -0.0625 238 LYS B CB  
6059 C CG  . LYS B 238 ? 0.3173 0.2443 0.3578 -0.0085 -0.0509 -0.0502 238 LYS B CG  
6060 C CD  . LYS B 238 ? 0.3245 0.2535 0.3670 -0.0204 -0.0519 -0.0436 238 LYS B CD  
6061 C CE  . LYS B 238 ? 0.5086 0.4144 0.5504 -0.0264 -0.0579 -0.0381 238 LYS B CE  
6062 N NZ  . LYS B 238 ? 0.6153 0.5168 0.6514 -0.0241 -0.0552 -0.0274 238 LYS B NZ  
6063 N N   . GLU B 239 ? 0.3272 0.2364 0.3777 0.0090  -0.0652 -0.0934 239 GLU B N   
6064 C CA  . GLU B 239 ? 0.3209 0.2210 0.3735 0.0137  -0.0695 -0.1021 239 GLU B CA  
6065 C C   . GLU B 239 ? 0.3307 0.2406 0.3826 0.0247  -0.0665 -0.1049 239 GLU B C   
6066 O O   . GLU B 239 ? 0.3424 0.2425 0.3950 0.0299  -0.0693 -0.1055 239 GLU B O   
6067 C CB  . GLU B 239 ? 0.3509 0.2601 0.4059 0.0095  -0.0706 -0.1116 239 GLU B CB  
6068 C CG  . GLU B 239 ? 0.5139 0.4140 0.5703 -0.0028 -0.0745 -0.1090 239 GLU B CG  
6069 C CD  . GLU B 239 ? 0.6918 0.6062 0.7499 -0.0074 -0.0748 -0.1182 239 GLU B CD  
6070 O OE1 . GLU B 239 ? 0.7365 0.6557 0.7966 -0.0183 -0.0762 -0.1162 239 GLU B OE1 
6071 O OE2 . GLU B 239 ? 0.7277 0.6505 0.7856 -0.0005 -0.0736 -0.1271 239 GLU B OE2 
6072 N N   . LYS B 240 ? 0.3343 0.2645 0.3852 0.0276  -0.0613 -0.1066 240 LYS B N   
6073 C CA  . LYS B 240 ? 0.2825 0.2243 0.3332 0.0360  -0.0586 -0.1084 240 LYS B CA  
6074 C C   . LYS B 240 ? 0.3763 0.3066 0.4247 0.0395  -0.0591 -0.1003 240 LYS B C   
6075 O O   . LYS B 240 ? 0.3809 0.3108 0.4306 0.0455  -0.0607 -0.1018 240 LYS B O   
6076 C CB  . LYS B 240 ? 0.3639 0.3285 0.4129 0.0365  -0.0532 -0.1099 240 LYS B CB  
6077 C CG  . LYS B 240 ? 0.3688 0.3478 0.4180 0.0432  -0.0507 -0.1116 240 LYS B CG  
6078 C CD  . LYS B 240 ? 0.3797 0.3678 0.4334 0.0466  -0.0526 -0.1213 240 LYS B CD  
6079 C CE  . LYS B 240 ? 0.4186 0.4206 0.4737 0.0527  -0.0513 -0.1232 240 LYS B CE  
6080 N NZ  . LYS B 240 ? 0.4990 0.5145 0.5588 0.0562  -0.0527 -0.1336 240 LYS B NZ  
6081 N N   . TYR B 241 ? 0.3121 0.2342 0.3571 0.0358  -0.0580 -0.0918 241 TYR B N   
6082 C CA  . TYR B 241 ? 0.3365 0.2479 0.3783 0.0383  -0.0585 -0.0833 241 TYR B CA  
6083 C C   . TYR B 241 ? 0.4019 0.2952 0.4451 0.0388  -0.0643 -0.0816 241 TYR B C   
6084 O O   . TYR B 241 ? 0.3800 0.2705 0.4226 0.0440  -0.0656 -0.0794 241 TYR B O   
6085 C CB  . TYR B 241 ? 0.3096 0.2161 0.3475 0.0336  -0.0563 -0.0747 241 TYR B CB  
6086 C CG  . TYR B 241 ? 0.3368 0.2352 0.3700 0.0359  -0.0559 -0.0655 241 TYR B CG  
6087 C CD1 . TYR B 241 ? 0.3307 0.2100 0.3630 0.0340  -0.0608 -0.0594 241 TYR B CD1 
6088 C CD2 . TYR B 241 ? 0.3472 0.2574 0.3761 0.0389  -0.0507 -0.0622 241 TYR B CD2 
6089 C CE1 . TYR B 241 ? 0.2996 0.1728 0.3269 0.0357  -0.0607 -0.0509 241 TYR B CE1 
6090 C CE2 . TYR B 241 ? 0.3571 0.2605 0.3811 0.0405  -0.0505 -0.0545 241 TYR B CE2 
6091 C CZ  . TYR B 241 ? 0.3362 0.2222 0.3594 0.0391  -0.0553 -0.0491 241 TYR B CZ  
6092 O OH  . TYR B 241 ? 0.3477 0.2285 0.3653 0.0405  -0.0553 -0.0414 241 TYR B OH  
6093 N N   . PHE B 242 ? 0.3630 0.2438 0.4080 0.0329  -0.0682 -0.0824 242 PHE B N   
6094 C CA  . PHE B 242 ? 0.4315 0.2940 0.4777 0.0330  -0.0742 -0.0814 242 PHE B CA  
6095 C C   . PHE B 242 ? 0.4258 0.2942 0.4753 0.0416  -0.0758 -0.0900 242 PHE B C   
6096 O O   . PHE B 242 ? 0.3832 0.2417 0.4330 0.0461  -0.0795 -0.0879 242 PHE B O   
6097 C CB  . PHE B 242 ? 0.4409 0.2919 0.4886 0.0241  -0.0779 -0.0824 242 PHE B CB  
6098 C CG  . PHE B 242 ? 0.4850 0.3130 0.5324 0.0213  -0.0844 -0.0775 242 PHE B CG  
6099 C CD1 . PHE B 242 ? 0.5271 0.3416 0.5710 0.0162  -0.0862 -0.0650 242 PHE B CD1 
6100 C CD2 . PHE B 242 ? 0.4183 0.2380 0.4685 0.0232  -0.0888 -0.0851 242 PHE B CD2 
6101 C CE1 . PHE B 242 ? 0.4831 0.2770 0.5263 0.0127  -0.0923 -0.0593 242 PHE B CE1 
6102 C CE2 . PHE B 242 ? 0.3846 0.1820 0.4343 0.0205  -0.0952 -0.0804 242 PHE B CE2 
6103 C CZ  . PHE B 242 ? 0.4582 0.2427 0.5043 0.0150  -0.0970 -0.0671 242 PHE B CZ  
6104 N N   . GLU B 243 ? 0.3656 0.2513 0.4179 0.0440  -0.0732 -0.0997 243 GLU B N   
6105 C CA  . GLU B 243 ? 0.4686 0.3618 0.5247 0.0521  -0.0749 -0.1084 243 GLU B CA  
6106 C C   . GLU B 243 ? 0.4352 0.3358 0.4907 0.0587  -0.0737 -0.1054 243 GLU B C   
6107 O O   . GLU B 243 ? 0.4521 0.3491 0.5103 0.0650  -0.0776 -0.1084 243 GLU B O   
6108 C CB  . GLU B 243 ? 0.5848 0.4981 0.6434 0.0528  -0.0720 -0.1184 243 GLU B CB  
6109 C CG  . GLU B 243 ? 0.6947 0.6231 0.7573 0.0613  -0.0724 -0.1272 243 GLU B CG  
6110 C CD  . GLU B 243 ? 0.7231 0.6772 0.7869 0.0614  -0.0677 -0.1338 243 GLU B CD  
6111 O OE1 . GLU B 243 ? 0.7439 0.7022 0.8062 0.0553  -0.0653 -0.1342 243 GLU B OE1 
6112 O OE2 . GLU B 243 ? 0.7321 0.7033 0.7986 0.0672  -0.0666 -0.1386 243 GLU B OE2 
6113 N N   . ILE B 244 ? 0.3974 0.3082 0.4496 0.0572  -0.0688 -0.0998 244 ILE B N   
6114 C CA  . ILE B 244 ? 0.4431 0.3641 0.4946 0.0623  -0.0672 -0.0980 244 ILE B CA  
6115 C C   . ILE B 244 ? 0.4442 0.3492 0.4929 0.0630  -0.0701 -0.0894 244 ILE B C   
6116 O O   . ILE B 244 ? 0.3557 0.2618 0.4058 0.0689  -0.0727 -0.0904 244 ILE B O   
6117 C CB  . ILE B 244 ? 0.4504 0.3880 0.4989 0.0601  -0.0609 -0.0959 244 ILE B CB  
6118 C CG1 . ILE B 244 ? 0.4267 0.3823 0.4778 0.0594  -0.0582 -0.1041 244 ILE B CG1 
6119 C CG2 . ILE B 244 ? 0.4846 0.4312 0.5318 0.0643  -0.0597 -0.0937 244 ILE B CG2 
6120 C CD1 . ILE B 244 ? 0.4437 0.4141 0.4998 0.0654  -0.0596 -0.1134 244 ILE B CD1 
6121 N N   . PHE B 245 ? 0.4375 0.3287 0.4820 0.0571  -0.0700 -0.0808 245 PHE B N   
6122 C CA  . PHE B 245 ? 0.4242 0.3020 0.4648 0.0568  -0.0722 -0.0711 245 PHE B CA  
6123 C C   . PHE B 245 ? 0.4257 0.2817 0.4664 0.0535  -0.0779 -0.0668 245 PHE B C   
6124 O O   . PHE B 245 ? 0.5138 0.3583 0.5516 0.0536  -0.0808 -0.0588 245 PHE B O   
6125 C CB  . PHE B 245 ? 0.4079 0.2882 0.4429 0.0525  -0.0675 -0.0632 245 PHE B CB  
6126 C CG  . PHE B 245 ? 0.4439 0.3434 0.4778 0.0549  -0.0621 -0.0661 245 PHE B CG  
6127 C CD1 . PHE B 245 ? 0.3458 0.2530 0.3793 0.0598  -0.0621 -0.0665 245 PHE B CD1 
6128 C CD2 . PHE B 245 ? 0.4386 0.3484 0.4721 0.0519  -0.0576 -0.0686 245 PHE B CD2 
6129 C CE1 . PHE B 245 ? 0.3758 0.2998 0.4083 0.0610  -0.0578 -0.0689 245 PHE B CE1 
6130 C CE2 . PHE B 245 ? 0.4295 0.3559 0.4616 0.0536  -0.0531 -0.0706 245 PHE B CE2 
6131 C CZ  . PHE B 245 ? 0.4205 0.3534 0.4520 0.0577  -0.0532 -0.0706 245 PHE B CZ  
6132 N N   . GLY B 246 ? 0.3697 0.2195 0.4132 0.0501  -0.0800 -0.0714 246 GLY B N   
6133 C CA  . GLY B 246 ? 0.4155 0.2437 0.4593 0.0469  -0.0863 -0.0678 246 GLY B CA  
6134 C C   . GLY B 246 ? 0.4693 0.2842 0.5088 0.0376  -0.0870 -0.0565 246 GLY B C   
6135 O O   . GLY B 246 ? 0.4609 0.2573 0.4995 0.0341  -0.0925 -0.0507 246 GLY B O   
6136 N N   . GLU B 247 ? 0.4246 0.2482 0.4612 0.0333  -0.0819 -0.0527 247 GLU B N   
6137 C CA  . GLU B 247 ? 0.4709 0.2842 0.5039 0.0236  -0.0826 -0.0423 247 GLU B CA  
6138 C C   . GLU B 247 ? 0.4477 0.2725 0.4816 0.0190  -0.0781 -0.0455 247 GLU B C   
6139 O O   . GLU B 247 ? 0.4497 0.2910 0.4854 0.0242  -0.0738 -0.0538 247 GLU B O   
6140 C CB  . GLU B 247 ? 0.5512 0.3615 0.5782 0.0240  -0.0818 -0.0310 247 GLU B CB  
6141 C CG  . GLU B 247 ? 0.6776 0.5048 0.7025 0.0303  -0.0758 -0.0332 247 GLU B CG  
6142 C CD  . GLU B 247 ? 0.7940 0.6185 0.8124 0.0315  -0.0756 -0.0233 247 GLU B CD  
6143 O OE1 . GLU B 247 ? 0.8579 0.6740 0.8756 0.0339  -0.0799 -0.0198 247 GLU B OE1 
6144 O OE2 . GLU B 247 ? 0.7999 0.6308 0.8136 0.0304  -0.0713 -0.0194 247 GLU B OE2 
6145 N N   . HIS B 248 ? 0.4208 0.2378 0.4538 0.0085  -0.0795 -0.0385 248 HIS B N   
6146 C CA  . HIS B 248 ? 0.4613 0.2996 0.4943 0.0039  -0.0723 -0.0390 248 HIS B CA  
6147 C C   . HIS B 248 ? 0.3948 0.2487 0.4220 0.0064  -0.0646 -0.0313 248 HIS B C   
6148 O O   . HIS B 248 ? 0.4960 0.3430 0.5182 0.0056  -0.0650 -0.0217 248 HIS B O   
6149 C CB  . HIS B 248 ? 0.5699 0.4067 0.6038 -0.0090 -0.0733 -0.0329 248 HIS B CB  
6150 C CG  . HIS B 248 ? 0.7081 0.5348 0.7478 -0.0124 -0.0795 -0.0428 248 HIS B CG  
6151 N ND1 . HIS B 248 ? 0.7183 0.5593 0.7618 -0.0100 -0.0774 -0.0548 248 HIS B ND1 
6152 C CD2 . HIS B 248 ? 0.7566 0.5598 0.7982 -0.0181 -0.0882 -0.0429 248 HIS B CD2 
6153 C CE1 . HIS B 248 ? 0.7477 0.5753 0.7953 -0.0139 -0.0843 -0.0627 248 HIS B CE1 
6154 N NE2 . HIS B 248 ? 0.7774 0.5852 0.8232 -0.0184 -0.0891 -0.0546 248 HIS B NE2 
6155 N N   . PRO B 249 ? 0.3717 0.2458 0.3989 0.0094  -0.0580 -0.0355 249 PRO B N   
6156 C CA  . PRO B 249 ? 0.3283 0.2146 0.3496 0.0123  -0.0513 -0.0294 249 PRO B CA  
6157 C C   . PRO B 249 ? 0.4134 0.3066 0.4312 0.0045  -0.0473 -0.0186 249 PRO B C   
6158 O O   . PRO B 249 ? 0.5004 0.4011 0.5213 -0.0023 -0.0463 -0.0179 249 PRO B O   
6159 C CB  . PRO B 249 ? 0.3460 0.2495 0.3690 0.0172  -0.0467 -0.0373 249 PRO B CB  
6160 C CG  . PRO B 249 ? 0.3612 0.2684 0.3901 0.0128  -0.0486 -0.0438 249 PRO B CG  
6161 C CD  . PRO B 249 ? 0.3595 0.2458 0.3915 0.0098  -0.0567 -0.0456 249 PRO B CD  
6162 N N   . VAL B 250 ? 0.3869 0.2794 0.3982 0.0055  -0.0450 -0.0105 250 VAL B N   
6163 C CA  . VAL B 250 ? 0.3374 0.2408 0.3446 -0.0003 -0.0400 -0.0011 250 VAL B CA  
6164 C C   . VAL B 250 ? 0.2687 0.1880 0.2718 0.0055  -0.0326 -0.0016 250 VAL B C   
6165 O O   . VAL B 250 ? 0.3671 0.2981 0.3671 0.0028  -0.0277 0.0046  250 VAL B O   
6166 C CB  . VAL B 250 ? 0.3853 0.2783 0.3872 -0.0049 -0.0426 0.0093  250 VAL B CB  
6167 C CG1 . VAL B 250 ? 0.3844 0.2604 0.3901 -0.0125 -0.0503 0.0118  250 VAL B CG1 
6168 C CG2 . VAL B 250 ? 0.3756 0.2608 0.3720 0.0025  -0.0438 0.0096  250 VAL B CG2 
6169 N N   . TYR B 251 ? 0.2705 0.1903 0.2733 0.0134  -0.0320 -0.0085 251 TYR B N   
6170 C CA  . TYR B 251 ? 0.2968 0.2286 0.2960 0.0187  -0.0261 -0.0098 251 TYR B CA  
6171 C C   . TYR B 251 ? 0.2909 0.2308 0.2953 0.0212  -0.0254 -0.0175 251 TYR B C   
6172 O O   . TYR B 251 ? 0.2943 0.2288 0.3029 0.0227  -0.0295 -0.0242 251 TYR B O   
6173 C CB  . TYR B 251 ? 0.3793 0.3046 0.3725 0.0246  -0.0264 -0.0103 251 TYR B CB  
6174 C CG  . TYR B 251 ? 0.3807 0.2956 0.3694 0.0223  -0.0293 -0.0039 251 TYR B CG  
6175 C CD1 . TYR B 251 ? 0.4682 0.3878 0.4524 0.0179  -0.0264 0.0042  251 TYR B CD1 
6176 C CD2 . TYR B 251 ? 0.4865 0.3885 0.4759 0.0247  -0.0351 -0.0056 251 TYR B CD2 
6177 C CE1 . TYR B 251 ? 0.5262 0.4376 0.5055 0.0150  -0.0291 0.0112  251 TYR B CE1 
6178 C CE2 . TYR B 251 ? 0.4849 0.3773 0.4698 0.0226  -0.0384 0.0015  251 TYR B CE2 
6179 C CZ  . TYR B 251 ? 0.5428 0.4399 0.5224 0.0172  -0.0353 0.0102  251 TYR B CZ  
6180 O OH  . TYR B 251 ? 0.6443 0.5334 0.6185 0.0141  -0.0386 0.0184  251 TYR B OH  
6181 N N   . MET B 252 ? 0.2573 0.2110 0.2612 0.0223  -0.0205 -0.0167 252 MET B N   
6182 C CA  . MET B 252 ? 0.2093 0.1720 0.2166 0.0248  -0.0197 -0.0226 252 MET B CA  
6183 C C   . MET B 252 ? 0.1827 0.1526 0.1853 0.0299  -0.0151 -0.0209 252 MET B C   
6184 O O   . MET B 252 ? 0.2184 0.1911 0.2169 0.0308  -0.0116 -0.0157 252 MET B O   
6185 C CB  . MET B 252 ? 0.2408 0.2138 0.2544 0.0198  -0.0199 -0.0236 252 MET B CB  
6186 C CG  . MET B 252 ? 0.2794 0.2448 0.2985 0.0158  -0.0255 -0.0291 252 MET B CG  
6187 S SD  . MET B 252 ? 0.2842 0.2643 0.3101 0.0118  -0.0262 -0.0344 252 MET B SD  
6188 C CE  . MET B 252 ? 0.2621 0.2263 0.2924 0.0079  -0.0336 -0.0414 252 MET B CE  
6189 N N   . TRP B 253 ? 0.1734 0.1462 0.1763 0.0332  -0.0153 -0.0254 253 TRP B N   
6190 C CA  . TRP B 253 ? 0.1554 0.1339 0.1543 0.0373  -0.0119 -0.0238 253 TRP B CA  
6191 C C   . TRP B 253 ? 0.1860 0.1784 0.1894 0.0365  -0.0107 -0.0239 253 TRP B C   
6192 O O   . TRP B 253 ? 0.2064 0.2039 0.2142 0.0345  -0.0129 -0.0285 253 TRP B O   
6193 C CB  . TRP B 253 ? 0.1949 0.1693 0.1910 0.0399  -0.0131 -0.0272 253 TRP B CB  
6194 C CG  . TRP B 253 ? 0.1721 0.1512 0.1646 0.0429  -0.0107 -0.0255 253 TRP B CG  
6195 C CD1 . TRP B 253 ? 0.1953 0.1822 0.1895 0.0427  -0.0114 -0.0274 253 TRP B CD1 
6196 C CD2 . TRP B 253 ? 0.1940 0.1700 0.1805 0.0464  -0.0078 -0.0213 253 TRP B CD2 
6197 N NE1 . TRP B 253 ? 0.1685 0.1554 0.1580 0.0455  -0.0095 -0.0237 253 TRP B NE1 
6198 C CE2 . TRP B 253 ? 0.1768 0.1563 0.1617 0.0484  -0.0074 -0.0205 253 TRP B CE2 
6199 C CE3 . TRP B 253 ? 0.2359 0.2069 0.2180 0.0483  -0.0057 -0.0183 253 TRP B CE3 
6200 C CZ2 . TRP B 253 ? 0.2160 0.1915 0.1954 0.0527  -0.0055 -0.0173 253 TRP B CZ2 
6201 C CZ3 . TRP B 253 ? 0.2127 0.1817 0.1891 0.0530  -0.0031 -0.0162 253 TRP B CZ3 
6202 C CH2 . TRP B 253 ? 0.2118 0.1819 0.1871 0.0555  -0.0033 -0.0159 253 TRP B CH2 
6203 N N   . PRO B 254 ? 0.1538 0.1538 0.1564 0.0381  -0.0074 -0.0194 254 PRO B N   
6204 C CA  . PRO B 254 ? 0.1621 0.1767 0.1690 0.0380  -0.0067 -0.0190 254 PRO B CA  
6205 C C   . PRO B 254 ? 0.1774 0.1934 0.1817 0.0417  -0.0068 -0.0198 254 PRO B C   
6206 O O   . PRO B 254 ? 0.1809 0.1900 0.1794 0.0462  -0.0054 -0.0176 254 PRO B O   
6207 C CB  . PRO B 254 ? 0.1747 0.1972 0.1814 0.0402  -0.0031 -0.0138 254 PRO B CB  
6208 C CG  . PRO B 254 ? 0.2272 0.2382 0.2268 0.0438  -0.0013 -0.0120 254 PRO B CG  
6209 C CD  . PRO B 254 ? 0.1911 0.1882 0.1886 0.0409  -0.0042 -0.0149 254 PRO B CD  
6210 N N   . PRO B 255 ? 0.1586 0.1834 0.1666 0.0395  -0.0088 -0.0229 255 PRO B N   
6211 C CA  . PRO B 255 ? 0.1648 0.1918 0.1697 0.0417  -0.0092 -0.0225 255 PRO B CA  
6212 C C   . PRO B 255 ? 0.1730 0.2011 0.1744 0.0469  -0.0071 -0.0164 255 PRO B C   
6213 O O   . PRO B 255 ? 0.1789 0.2159 0.1832 0.0487  -0.0057 -0.0134 255 PRO B O   
6214 C CB  . PRO B 255 ? 0.1452 0.1862 0.1550 0.0380  -0.0112 -0.0263 255 PRO B CB  
6215 C CG  . PRO B 255 ? 0.1978 0.2365 0.2124 0.0338  -0.0130 -0.0318 255 PRO B CG  
6216 C CD  . PRO B 255 ? 0.1413 0.1731 0.1556 0.0341  -0.0112 -0.0275 255 PRO B CD  
6217 N N   . LEU B 256 ? 0.1866 0.2053 0.1819 0.0494  -0.0074 -0.0148 256 LEU B N   
6218 C CA  . LEU B 256 ? 0.1562 0.1706 0.1469 0.0550  -0.0064 -0.0096 256 LEU B CA  
6219 C C   . LEU B 256 ? 0.1656 0.1754 0.1549 0.0599  -0.0036 -0.0082 256 LEU B C   
6220 O O   . LEU B 256 ? 0.1929 0.2032 0.1807 0.0660  -0.0025 -0.0048 256 LEU B O   
6221 C CB  . LEU B 256 ? 0.1548 0.1827 0.1483 0.0562  -0.0073 -0.0058 256 LEU B CB  
6222 C CG  . LEU B 256 ? 0.2460 0.2830 0.2411 0.0504  -0.0097 -0.0079 256 LEU B CG  
6223 C CD1 . LEU B 256 ? 0.3506 0.4041 0.3491 0.0503  -0.0107 -0.0048 256 LEU B CD1 
6224 C CD2 . LEU B 256 ? 0.2294 0.2565 0.2183 0.0487  -0.0111 -0.0071 256 LEU B CD2 
6225 N N   . ALA B 257 ? 0.1734 0.1784 0.1627 0.0576  -0.0027 -0.0108 257 ALA B N   
6226 C CA  . ALA B 257 ? 0.1596 0.1637 0.1477 0.0607  0.0002  -0.0096 257 ALA B CA  
6227 C C   . ALA B 257 ? 0.1717 0.1927 0.1661 0.0621  0.0019  -0.0071 257 ALA B C   
6228 O O   . ALA B 257 ? 0.1998 0.2244 0.1932 0.0669  0.0049  -0.0054 257 ALA B O   
6229 C CB  . ALA B 257 ? 0.1704 0.1624 0.1505 0.0673  0.0014  -0.0088 257 ALA B CB  
6230 N N   . SER B 258 ? 0.1752 0.2084 0.1759 0.0581  0.0003  -0.0073 258 SER B N   
6231 C CA  . SER B 258 ? 0.1534 0.2043 0.1599 0.0601  0.0013  -0.0045 258 SER B CA  
6232 C C   . SER B 258 ? 0.1645 0.2250 0.1759 0.0556  0.0030  -0.0043 258 SER B C   
6233 O O   . SER B 258 ? 0.1855 0.2453 0.1999 0.0478  0.0012  -0.0067 258 SER B O   
6234 C CB  . SER B 258 ? 0.1774 0.2395 0.1882 0.0573  -0.0014 -0.0045 258 SER B CB  
6235 O OG  . SER B 258 ? 0.2142 0.2924 0.2292 0.0617  -0.0006 -0.0006 258 SER B OG  
6236 N N   . VAL B 259 ? 0.1584 0.2290 0.1710 0.0605  0.0061  -0.0013 259 VAL B N   
6237 C CA  . VAL B 259 ? 0.1493 0.2323 0.1666 0.0555  0.0080  0.0001  259 VAL B CA  
6238 C C   . VAL B 259 ? 0.1359 0.2410 0.1590 0.0601  0.0100  0.0032  259 VAL B C   
6239 O O   . VAL B 259 ? 0.1914 0.2988 0.2136 0.0693  0.0103  0.0043  259 VAL B O   
6240 C CB  . VAL B 259 ? 0.1684 0.2427 0.1802 0.0557  0.0107  0.0006  259 VAL B CB  
6241 C CG1 . VAL B 259 ? 0.1951 0.2487 0.2019 0.0509  0.0080  -0.0022 259 VAL B CG1 
6242 C CG2 . VAL B 259 ? 0.2015 0.2734 0.2076 0.0668  0.0138  0.0008  259 VAL B CG2 
6243 N N   . SER B 260 ? 0.1492 0.2705 0.1785 0.0534  0.0109  0.0049  260 SER B N   
6244 C CA  . SER B 260 ? 0.1350 0.2816 0.1711 0.0562  0.0132  0.0081  260 SER B CA  
6245 C C   . SER B 260 ? 0.1553 0.3118 0.1945 0.0465  0.0149  0.0101  260 SER B C   
6246 O O   . SER B 260 ? 0.1832 0.3255 0.2199 0.0378  0.0130  0.0092  260 SER B O   
6247 C CB  . SER B 260 ? 0.1876 0.3492 0.2307 0.0545  0.0102  0.0085  260 SER B CB  
6248 O OG  . SER B 260 ? 0.1874 0.3475 0.2336 0.0419  0.0069  0.0065  260 SER B OG  
6249 N N   . ASN B 261 ? 0.1506 0.3325 0.1957 0.0479  0.0179  0.0133  261 ASN B N   
6250 C CA  . ASN B 261 ? 0.1869 0.3807 0.2354 0.0366  0.0192  0.0164  261 ASN B CA  
6251 C C   . ASN B 261 ? 0.1920 0.3812 0.2445 0.0225  0.0142  0.0158  261 ASN B C   
6252 O O   . ASN B 261 ? 0.2049 0.3830 0.2553 0.0124  0.0129  0.0169  261 ASN B O   
6253 C CB  . ASN B 261 ? 0.1586 0.3852 0.2144 0.0395  0.0230  0.0199  261 ASN B CB  
6254 C CG  . ASN B 261 ? 0.1885 0.4196 0.2399 0.0534  0.0281  0.0194  261 ASN B CG  
6255 O OD1 . ASN B 261 ? 0.1894 0.4008 0.2318 0.0568  0.0294  0.0176  261 ASN B OD1 
6256 N ND2 . ASN B 261 ? 0.2071 0.4645 0.2650 0.0620  0.0307  0.0204  261 ASN B ND2 
6257 N N   . GLU B 262 ? 0.1575 0.3542 0.2153 0.0218  0.0110  0.0139  262 GLU B N   
6258 C CA  . GLU B 262 ? 0.1627 0.3558 0.2242 0.0089  0.0061  0.0118  262 GLU B CA  
6259 C C   . GLU B 262 ? 0.1992 0.3623 0.2543 0.0067  0.0028  0.0073  262 GLU B C   
6260 O O   . GLU B 262 ? 0.1770 0.3301 0.2329 -0.0042 -0.0007 0.0060  262 GLU B O   
6261 C CB  . GLU B 262 ? 0.1418 0.3520 0.2096 0.0093  0.0035  0.0102  262 GLU B CB  
6262 C CG  . GLU B 262 ? 0.1882 0.4312 0.2644 0.0085  0.0057  0.0147  262 GLU B CG  
6263 C CD  . GLU B 262 ? 0.3277 0.5891 0.4105 0.0071  0.0023  0.0135  262 GLU B CD  
6264 O OE1 . GLU B 262 ? 0.3530 0.6026 0.4344 0.0017  -0.0021 0.0087  262 GLU B OE1 
6265 O OE2 . GLU B 262 ? 0.4085 0.6972 0.4977 0.0119  0.0040  0.0169  262 GLU B OE2 
6266 N N   . ALA B 263 ? 0.1704 0.3190 0.2193 0.0167  0.0035  0.0049  263 ALA B N   
6267 C CA  . ALA B 263 ? 0.1497 0.2730 0.1933 0.0150  0.0004  0.0004  263 ALA B CA  
6268 C C   . ALA B 263 ? 0.1775 0.2858 0.2166 0.0111  0.0010  0.0023  263 ALA B C   
6269 O O   . ALA B 263 ? 0.2050 0.2974 0.2433 0.0044  -0.0028 -0.0002 263 ALA B O   
6270 C CB  . ALA B 263 ? 0.1702 0.2834 0.2084 0.0253  0.0008  -0.0019 263 ALA B CB  
6271 N N   . LEU B 264 ? 0.1638 0.2774 0.1999 0.0156  0.0055  0.0067  264 LEU B N   
6272 C CA  . LEU B 264 ? 0.1817 0.2839 0.2130 0.0112  0.0061  0.0096  264 LEU B CA  
6273 C C   . LEU B 264 ? 0.1896 0.2961 0.2256 -0.0024 0.0036  0.0129  264 LEU B C   
6274 O O   . LEU B 264 ? 0.1976 0.2868 0.2306 -0.0088 0.0006  0.0139  264 LEU B O   
6275 C CB  . LEU B 264 ? 0.2050 0.3164 0.2320 0.0185  0.0118  0.0130  264 LEU B CB  
6276 C CG  . LEU B 264 ? 0.2426 0.3437 0.2630 0.0313  0.0136  0.0097  264 LEU B CG  
6277 C CD1 . LEU B 264 ? 0.3028 0.4158 0.3199 0.0393  0.0190  0.0116  264 LEU B CD1 
6278 C CD2 . LEU B 264 ? 0.2543 0.3301 0.2678 0.0307  0.0108  0.0072  264 LEU B CD2 
6279 N N   . GLU B 265 ? 0.1800 0.3094 0.2235 -0.0074 0.0042  0.0150  265 GLU B N   
6280 C CA  . GLU B 265 ? 0.2018 0.3350 0.2503 -0.0220 0.0009  0.0180  265 GLU B CA  
6281 C C   . GLU B 265 ? 0.2131 0.3254 0.2624 -0.0282 -0.0058 0.0124  265 GLU B C   
6282 O O   . GLU B 265 ? 0.2367 0.3348 0.2853 -0.0382 -0.0098 0.0142  265 GLU B O   
6283 C CB  . GLU B 265 ? 0.2565 0.4201 0.3134 -0.0259 0.0024  0.0204  265 GLU B CB  
6284 C CG  . GLU B 265 ? 0.4644 0.6522 0.5219 -0.0210 0.0089  0.0260  265 GLU B CG  
6285 C CD  . GLU B 265 ? 0.6752 0.8689 0.7322 -0.0326 0.0100  0.0333  265 GLU B CD  
6286 O OE1 . GLU B 265 ? 0.6951 0.9103 0.7521 -0.0292 0.0157  0.0377  265 GLU B OE1 
6287 O OE2 . GLU B 265 ? 0.7580 0.9351 0.8145 -0.0450 0.0049  0.0347  265 GLU B OE2 
6288 N N   . LEU B 266 ? 0.2171 0.3277 0.2676 -0.0223 -0.0075 0.0056  266 LEU B N   
6289 C CA  . LEU B 266 ? 0.1709 0.2640 0.2221 -0.0266 -0.0135 -0.0015 266 LEU B CA  
6290 C C   . LEU B 266 ? 0.2331 0.2990 0.2782 -0.0248 -0.0157 -0.0028 266 LEU B C   
6291 O O   . LEU B 266 ? 0.2167 0.2664 0.2625 -0.0324 -0.0210 -0.0047 266 LEU B O   
6292 C CB  . LEU B 266 ? 0.1761 0.2757 0.2287 -0.0196 -0.0140 -0.0080 266 LEU B CB  
6293 C CG  . LEU B 266 ? 0.2017 0.2850 0.2540 -0.0214 -0.0194 -0.0169 266 LEU B CG  
6294 C CD1 . LEU B 266 ? 0.2077 0.2908 0.2651 -0.0338 -0.0245 -0.0196 266 LEU B CD1 
6295 C CD2 . LEU B 266 ? 0.1892 0.2807 0.2412 -0.0139 -0.0189 -0.0221 266 LEU B CD2 
6296 N N   . TYR B 267 ? 0.1787 0.2386 0.2177 -0.0146 -0.0122 -0.0021 267 TYR B N   
6297 C CA  . TYR B 267 ? 0.2278 0.2643 0.2611 -0.0127 -0.0144 -0.0030 267 TYR B CA  
6298 C C   . TYR B 267 ? 0.3254 0.3542 0.3576 -0.0216 -0.0161 0.0037  267 TYR B C   
6299 O O   . TYR B 267 ? 0.2667 0.2752 0.2978 -0.0254 -0.0213 0.0024  267 TYR B O   
6300 C CB  . TYR B 267 ? 0.2117 0.2459 0.2385 -0.0017 -0.0102 -0.0024 267 TYR B CB  
6301 C CG  . TYR B 267 ? 0.2248 0.2593 0.2514 0.0061  -0.0101 -0.0086 267 TYR B CG  
6302 C CD1 . TYR B 267 ? 0.2532 0.2750 0.2802 0.0064  -0.0143 -0.0155 267 TYR B CD1 
6303 C CD2 . TYR B 267 ? 0.2063 0.2540 0.2319 0.0135  -0.0059 -0.0074 267 TYR B CD2 
6304 C CE1 . TYR B 267 ? 0.2771 0.3016 0.3034 0.0124  -0.0140 -0.0203 267 TYR B CE1 
6305 C CE2 . TYR B 267 ? 0.1768 0.2245 0.2015 0.0194  -0.0063 -0.0116 267 TYR B CE2 
6306 C CZ  . TYR B 267 ? 0.1968 0.2338 0.2217 0.0183  -0.0101 -0.0177 267 TYR B CZ  
6307 O OH  . TYR B 267 ? 0.2102 0.2496 0.2339 0.0231  -0.0103 -0.0211 267 TYR B OH  
6308 N N   . TYR B 268 ? 0.2142 0.2598 0.2467 -0.0252 -0.0120 0.0112  268 TYR B N   
6309 C CA  . TYR B 268 ? 0.2170 0.2586 0.2481 -0.0354 -0.0134 0.0191  268 TYR B CA  
6310 C C   . TYR B 268 ? 0.2509 0.2841 0.2873 -0.0479 -0.0201 0.0184  268 TYR B C   
6311 O O   . TYR B 268 ? 0.2586 0.2722 0.2928 -0.0545 -0.0251 0.0215  268 TYR B O   
6312 C CB  . TYR B 268 ? 0.2249 0.2922 0.2564 -0.0371 -0.0073 0.0264  268 TYR B CB  
6313 C CG  . TYR B 268 ? 0.2575 0.3275 0.2901 -0.0513 -0.0092 0.0349  268 TYR B CG  
6314 C CD1 . TYR B 268 ? 0.2949 0.3492 0.3209 -0.0551 -0.0110 0.0410  268 TYR B CD1 
6315 C CD2 . TYR B 268 ? 0.2675 0.3557 0.3075 -0.0618 -0.0098 0.0375  268 TYR B CD2 
6316 C CE1 . TYR B 268 ? 0.3530 0.4090 0.3793 -0.0693 -0.0133 0.0502  268 TYR B CE1 
6317 C CE2 . TYR B 268 ? 0.3370 0.4276 0.3778 -0.0765 -0.0120 0.0462  268 TYR B CE2 
6318 C CZ  . TYR B 268 ? 0.4101 0.4840 0.4439 -0.0803 -0.0137 0.0528  268 TYR B CZ  
6319 O OH  . TYR B 268 ? 0.5312 0.6070 0.5652 -0.0961 -0.0164 0.0628  268 TYR B OH  
6320 N N   . GLU B 269 ? 0.2428 0.2907 0.2861 -0.0516 -0.0207 0.0149  269 GLU B N   
6321 C CA  . GLU B 269 ? 0.2600 0.3003 0.3083 -0.0641 -0.0274 0.0131  269 GLU B CA  
6322 C C   . GLU B 269 ? 0.3138 0.3251 0.3607 -0.0623 -0.0342 0.0052  269 GLU B C   
6323 O O   . GLU B 269 ? 0.3507 0.3456 0.3992 -0.0724 -0.0409 0.0052  269 GLU B O   
6324 C CB  . GLU B 269 ? 0.2778 0.3407 0.3332 -0.0667 -0.0268 0.0090  269 GLU B CB  
6325 C CG  . GLU B 269 ? 0.4207 0.5108 0.4804 -0.0751 -0.0233 0.0173  269 GLU B CG  
6326 C CD  . GLU B 269 ? 0.5918 0.7104 0.6572 -0.0707 -0.0200 0.0144  269 GLU B CD  
6327 O OE1 . GLU B 269 ? 0.5876 0.7317 0.6550 -0.0689 -0.0143 0.0205  269 GLU B OE1 
6328 O OE2 . GLU B 269 ? 0.6229 0.7394 0.6908 -0.0686 -0.0231 0.0060  269 GLU B OE2 
6329 N N   . LYS B 270 ? 0.2595 0.2644 0.3037 -0.0499 -0.0330 -0.0017 270 LYS B N   
6330 C CA  . LYS B 270 ? 0.2831 0.2647 0.3265 -0.0460 -0.0386 -0.0103 270 LYS B CA  
6331 C C   . LYS B 270 ? 0.3269 0.2871 0.3647 -0.0428 -0.0405 -0.0064 270 LYS B C   
6332 O O   . LYS B 270 ? 0.3414 0.2840 0.3785 -0.0370 -0.0446 -0.0134 270 LYS B O   
6333 C CB  . LYS B 270 ? 0.2731 0.2624 0.3168 -0.0351 -0.0363 -0.0194 270 LYS B CB  
6334 C CG  . LYS B 270 ? 0.2981 0.3062 0.3473 -0.0383 -0.0363 -0.0248 270 LYS B CG  
6335 C CD  . LYS B 270 ? 0.4147 0.4119 0.4680 -0.0478 -0.0436 -0.0309 270 LYS B CD  
6336 C CE  . LYS B 270 ? 0.4855 0.5029 0.5438 -0.0516 -0.0439 -0.0365 270 LYS B CE  
6337 N NZ  . LYS B 270 ? 0.5774 0.6007 0.6401 -0.0657 -0.0468 -0.0326 270 LYS B NZ  
6338 N N   . GLY B 271 ? 0.3275 0.2908 0.3613 -0.0459 -0.0376 0.0043  271 GLY B N   
6339 C CA  . GLY B 271 ? 0.3264 0.2703 0.3545 -0.0442 -0.0401 0.0092  271 GLY B CA  
6340 C C   . GLY B 271 ? 0.3443 0.2882 0.3666 -0.0322 -0.0359 0.0083  271 GLY B C   
6341 O O   . GLY B 271 ? 0.3618 0.2889 0.3797 -0.0297 -0.0389 0.0106  271 GLY B O   
6342 N N   . ILE B 272 ? 0.2722 0.2335 0.2943 -0.0247 -0.0298 0.0050  272 ILE B N   
6343 C CA  . ILE B 272 ? 0.3003 0.2613 0.3162 -0.0145 -0.0260 0.0045  272 ILE B CA  
6344 C C   . ILE B 272 ? 0.3437 0.3121 0.3538 -0.0161 -0.0216 0.0140  272 ILE B C   
6345 O O   . ILE B 272 ? 0.2842 0.2708 0.2957 -0.0201 -0.0175 0.0186  272 ILE B O   
6346 C CB  . ILE B 272 ? 0.2560 0.2307 0.2733 -0.0065 -0.0217 -0.0017 272 ILE B CB  
6347 C CG1 . ILE B 272 ? 0.3148 0.2861 0.3378 -0.0062 -0.0258 -0.0110 272 ILE B CG1 
6348 C CG2 . ILE B 272 ? 0.2828 0.2545 0.2936 0.0030  -0.0187 -0.0025 272 ILE B CG2 
6349 C CD1 . ILE B 272 ? 0.3720 0.3229 0.3947 -0.0041 -0.0316 -0.0161 272 ILE B CD1 
6350 N N   . ASN B 273 ? 0.3056 0.2621 0.3090 -0.0127 -0.0225 0.0167  273 ASN B N   
6351 C CA  . ASN B 273 ? 0.3529 0.3171 0.3494 -0.0140 -0.0185 0.0251  273 ASN B CA  
6352 C C   . ASN B 273 ? 0.2593 0.2327 0.2502 -0.0040 -0.0124 0.0224  273 ASN B C   
6353 O O   . ASN B 273 ? 0.2772 0.2635 0.2635 -0.0040 -0.0075 0.0274  273 ASN B O   
6354 C CB  . ASN B 273 ? 0.3905 0.3373 0.3819 -0.0175 -0.0234 0.0311  273 ASN B CB  
6355 C CG  . ASN B 273 ? 0.4715 0.4082 0.4670 -0.0288 -0.0295 0.0362  273 ASN B CG  
6356 O OD1 . ASN B 273 ? 0.4440 0.3928 0.4435 -0.0372 -0.0282 0.0396  273 ASN B OD1 
6357 N ND2 . ASN B 273 ? 0.5267 0.4410 0.5214 -0.0291 -0.0368 0.0367  273 ASN B ND2 
6358 N N   . MET B 274 ? 0.2719 0.2395 0.2630 0.0042  -0.0127 0.0147  274 MET B N   
6359 C CA  . MET B 274 ? 0.2925 0.2661 0.2781 0.0129  -0.0078 0.0122  274 MET B CA  
6360 C C   . MET B 274 ? 0.2839 0.2576 0.2730 0.0190  -0.0078 0.0045  274 MET B C   
6361 O O   . MET B 274 ? 0.2748 0.2399 0.2681 0.0185  -0.0121 0.0000  274 MET B O   
6362 C CB  . MET B 274 ? 0.3672 0.3297 0.3443 0.0158  -0.0089 0.0137  274 MET B CB  
6363 C CG  . MET B 274 ? 0.4444 0.4121 0.4146 0.0236  -0.0041 0.0112  274 MET B CG  
6364 S SD  . MET B 274 ? 0.5799 0.5376 0.5500 0.0310  -0.0060 0.0029  274 MET B SD  
6365 C CE  . MET B 274 ? 0.5089 0.4516 0.4729 0.0305  -0.0107 0.0042  274 MET B CE  
6366 N N   . LEU B 275 ? 0.2593 0.2432 0.2463 0.0251  -0.0031 0.0032  275 LEU B N   
6367 C CA  . LEU B 275 ? 0.2194 0.2022 0.2072 0.0311  -0.0030 -0.0025 275 LEU B CA  
6368 C C   . LEU B 275 ? 0.2097 0.1933 0.1902 0.0384  0.0009  -0.0029 275 LEU B C   
6369 O O   . LEU B 275 ? 0.2450 0.2324 0.2204 0.0392  0.0038  0.0003  275 LEU B O   
6370 C CB  . LEU B 275 ? 0.2861 0.2812 0.2816 0.0300  -0.0025 -0.0041 275 LEU B CB  
6371 C CG  . LEU B 275 ? 0.2874 0.3001 0.2860 0.0286  0.0012  -0.0001 275 LEU B CG  
6372 C CD1 . LEU B 275 ? 0.3775 0.3974 0.3724 0.0375  0.0055  -0.0004 275 LEU B CD1 
6373 C CD2 . LEU B 275 ? 0.3075 0.3305 0.3147 0.0237  -0.0006 -0.0012 275 LEU B CD2 
6374 N N   . ALA B 276 ? 0.2192 0.1995 0.1988 0.0434  0.0006  -0.0068 276 ALA B N   
6375 C CA  . ALA B 276 ? 0.2503 0.2301 0.2235 0.0503  0.0037  -0.0076 276 ALA B CA  
6376 C C   . ALA B 276 ? 0.2239 0.2111 0.2007 0.0544  0.0048  -0.0086 276 ALA B C   
6377 O O   . ALA B 276 ? 0.2150 0.2068 0.1983 0.0517  0.0028  -0.0095 276 ALA B O   
6378 C CB  . ALA B 276 ? 0.2795 0.2449 0.2456 0.0523  0.0017  -0.0103 276 ALA B CB  
6379 N N   . THR B 277 ? 0.2326 0.2211 0.2049 0.0614  0.0077  -0.0087 277 THR B N   
6380 C CA  . THR B 277 ? 0.2140 0.2073 0.1887 0.0664  0.0081  -0.0088 277 THR B CA  
6381 C C   . THR B 277 ? 0.2419 0.2246 0.2084 0.0740  0.0090  -0.0105 277 THR B C   
6382 O O   . THR B 277 ? 0.2839 0.2544 0.2431 0.0736  0.0084  -0.0125 277 THR B O   
6383 C CB  . THR B 277 ? 0.1818 0.1943 0.1639 0.0670  0.0104  -0.0062 277 THR B CB  
6384 O OG1 . THR B 277 ? 0.2364 0.2535 0.2207 0.0729  0.0102  -0.0057 277 THR B OG1 
6385 C CG2 . THR B 277 ? 0.2396 0.2605 0.2194 0.0697  0.0145  -0.0048 277 THR B CG2 
6386 N N   . ASP B 278 ? 0.2314 0.2175 0.1988 0.0807  0.0097  -0.0100 278 ASP B N   
6387 C CA  . ASP B 278 ? 0.2210 0.1931 0.1807 0.0876  0.0091  -0.0118 278 ASP B CA  
6388 C C   . ASP B 278 ? 0.2427 0.2180 0.1987 0.0966  0.0127  -0.0136 278 ASP B C   
6389 O O   . ASP B 278 ? 0.2448 0.2375 0.2061 0.0998  0.0157  -0.0122 278 ASP B O   
6390 C CB  . ASP B 278 ? 0.2633 0.2330 0.2253 0.0898  0.0063  -0.0098 278 ASP B CB  
6391 C CG  . ASP B 278 ? 0.3068 0.2579 0.2604 0.0952  0.0044  -0.0111 278 ASP B CG  
6392 O OD1 . ASP B 278 ? 0.3274 0.2641 0.2743 0.0916  0.0028  -0.0135 278 ASP B OD1 
6393 O OD2 . ASP B 278 ? 0.3313 0.2818 0.2852 0.1024  0.0039  -0.0096 278 ASP B OD2 
6394 N N   . GLU B 279 ? 0.2641 0.2232 0.2107 0.1008  0.0121  -0.0172 279 GLU B N   
6395 C CA  . GLU B 279 ? 0.3276 0.2882 0.2699 0.1079  0.0146  -0.0201 279 GLU B CA  
6396 C C   . GLU B 279 ? 0.2696 0.2384 0.2170 0.1148  0.0148  -0.0188 279 GLU B C   
6397 O O   . GLU B 279 ? 0.3084 0.2888 0.2564 0.1209  0.0181  -0.0205 279 GLU B O   
6398 C CB  . GLU B 279 ? 0.3582 0.2992 0.2909 0.1060  0.0120  -0.0238 279 GLU B CB  
6399 C CG  . GLU B 279 ? 0.3994 0.3410 0.3264 0.1117  0.0143  -0.0282 279 GLU B CG  
6400 C CD  . GLU B 279 ? 0.4271 0.3500 0.3449 0.1090  0.0114  -0.0322 279 GLU B CD  
6401 O OE1 . GLU B 279 ? 0.3729 0.2834 0.2890 0.1022  0.0078  -0.0311 279 GLU B OE1 
6402 O OE2 . GLU B 279 ? 0.4269 0.3490 0.3395 0.1138  0.0128  -0.0368 279 GLU B OE2 
6403 N N   . VAL B 280 ? 0.2786 0.2428 0.2296 0.1144  0.0114  -0.0156 280 VAL B N   
6404 C CA  . VAL B 280 ? 0.2796 0.2517 0.2354 0.1216  0.0111  -0.0137 280 VAL B CA  
6405 C C   . VAL B 280 ? 0.2863 0.2846 0.2509 0.1241  0.0149  -0.0117 280 VAL B C   
6406 O O   . VAL B 280 ? 0.2660 0.2764 0.2336 0.1310  0.0168  -0.0123 280 VAL B O   
6407 C CB  . VAL B 280 ? 0.3072 0.2699 0.2644 0.1205  0.0065  -0.0096 280 VAL B CB  
6408 C CG1 . VAL B 280 ? 0.3030 0.2772 0.2665 0.1279  0.0060  -0.0066 280 VAL B CG1 
6409 C CG2 . VAL B 280 ? 0.4072 0.3457 0.3561 0.1189  0.0029  -0.0113 280 VAL B CG2 
6410 N N   . ILE B 281 ? 0.2752 0.2836 0.2447 0.1185  0.0159  -0.0097 281 ILE B N   
6411 C CA  . ILE B 281 ? 0.2615 0.2961 0.2403 0.1175  0.0191  -0.0073 281 ILE B CA  
6412 C C   . ILE B 281 ? 0.2592 0.3055 0.2360 0.1207  0.0241  -0.0098 281 ILE B C   
6413 O O   . ILE B 281 ? 0.2485 0.3170 0.2315 0.1252  0.0272  -0.0088 281 ILE B O   
6414 C CB  . ILE B 281 ? 0.2606 0.2990 0.2441 0.1042  0.0173  -0.0047 281 ILE B CB  
6415 C CG1 . ILE B 281 ? 0.2431 0.2769 0.2295 0.1024  0.0129  -0.0024 281 ILE B CG1 
6416 C CG2 . ILE B 281 ? 0.2383 0.3007 0.2299 0.0992  0.0201  -0.0025 281 ILE B CG2 
6417 C CD1 . ILE B 281 ? 0.2762 0.3128 0.2669 0.0904  0.0108  -0.0016 281 ILE B CD1 
6418 N N   . LEU B 282 ? 0.2545 0.2878 0.2226 0.1182  0.0250  -0.0130 282 LEU B N   
6419 C CA  . LEU B 282 ? 0.2302 0.2743 0.1944 0.1214  0.0298  -0.0156 282 LEU B CA  
6420 C C   . LEU B 282 ? 0.2283 0.2750 0.1912 0.1308  0.0303  -0.0187 282 LEU B C   
6421 O O   . LEU B 282 ? 0.2531 0.3219 0.2198 0.1343  0.0341  -0.0187 282 LEU B O   
6422 C CB  . LEU B 282 ? 0.2504 0.2775 0.2043 0.1164  0.0293  -0.0182 282 LEU B CB  
6423 C CG  . LEU B 282 ? 0.3091 0.3477 0.2573 0.1175  0.0340  -0.0204 282 LEU B CG  
6424 C CD1 . LEU B 282 ? 0.2863 0.3490 0.2418 0.1091  0.0368  -0.0147 282 LEU B CD1 
6425 C CD2 . LEU B 282 ? 0.3166 0.3365 0.2539 0.1130  0.0323  -0.0230 282 LEU B CD2 
6426 N N   . LYS B 283 ? 0.2603 0.2849 0.2181 0.1337  0.0260  -0.0210 283 LYS B N   
6427 C CA  . LYS B 283 ? 0.2746 0.2987 0.2310 0.1426  0.0258  -0.0244 283 LYS B CA  
6428 C C   . LYS B 283 ? 0.2645 0.3093 0.2308 0.1477  0.0265  -0.0212 283 LYS B C   
6429 O O   . LYS B 283 ? 0.2736 0.3305 0.2412 0.1551  0.0286  -0.0238 283 LYS B O   
6430 C CB  . LYS B 283 ? 0.3496 0.3462 0.3001 0.1438  0.0207  -0.0263 283 LYS B CB  
6431 C CG  . LYS B 283 ? 0.4724 0.4499 0.4127 0.1397  0.0197  -0.0306 283 LYS B CG  
6432 C CD  . LYS B 283 ? 0.5699 0.5222 0.5055 0.1402  0.0145  -0.0319 283 LYS B CD  
6433 C CE  . LYS B 283 ? 0.7339 0.6721 0.6600 0.1408  0.0141  -0.0384 283 LYS B CE  
6434 N NZ  . LYS B 283 ? 0.7941 0.7079 0.7148 0.1349  0.0091  -0.0383 283 LYS B NZ  
6435 N N   . ASN B 284 ? 0.3102 0.3601 0.2835 0.1438  0.0247  -0.0159 284 ASN B N   
6436 C CA  . ASN B 284 ? 0.2535 0.3245 0.2366 0.1474  0.0249  -0.0123 284 ASN B CA  
6437 C C   . ASN B 284 ? 0.2866 0.3881 0.2765 0.1453  0.0299  -0.0110 284 ASN B C   
6438 O O   . ASN B 284 ? 0.2774 0.3996 0.2749 0.1488  0.0305  -0.0089 284 ASN B O   
6439 C CB  . ASN B 284 ? 0.2869 0.3559 0.2752 0.1427  0.0213  -0.0071 284 ASN B CB  
6440 C CG  . ASN B 284 ? 0.3815 0.4267 0.3654 0.1451  0.0162  -0.0065 284 ASN B CG  
6441 O OD1 . ASN B 284 ? 0.3826 0.4133 0.3608 0.1512  0.0150  -0.0098 284 ASN B OD1 
6442 N ND2 . ASN B 284 ? 0.3325 0.3742 0.3190 0.1402  0.0129  -0.0022 284 ASN B ND2 
6443 N N   . SER B 285 ? 0.2630 0.3688 0.2506 0.1390  0.0332  -0.0114 285 SER B N   
6444 C CA  . SER B 285 ? 0.2731 0.4084 0.2681 0.1336  0.0376  -0.0083 285 SER B CA  
6445 C C   . SER B 285 ? 0.2877 0.4369 0.2790 0.1350  0.0425  -0.0108 285 SER B C   
6446 O O   . SER B 285 ? 0.2837 0.4614 0.2819 0.1324  0.0458  -0.0081 285 SER B O   
6447 C CB  . SER B 285 ? 0.3018 0.4348 0.2985 0.1225  0.0376  -0.0051 285 SER B CB  
6448 O OG  . SER B 285 ? 0.2759 0.3968 0.2759 0.1194  0.0325  -0.0030 285 SER B OG  
6449 N N   . VAL B 286 ? 0.2483 0.3796 0.2287 0.1380  0.0429  -0.0158 286 VAL B N   
6450 C CA  . VAL B 286 ? 0.2906 0.4349 0.2661 0.1392  0.0473  -0.0187 286 VAL B CA  
6451 C C   . VAL B 286 ? 0.3363 0.4654 0.3046 0.1493  0.0457  -0.0258 286 VAL B C   
6452 O O   . VAL B 286 ? 0.3352 0.4392 0.3002 0.1530  0.0411  -0.0280 286 VAL B O   
6453 C CB  . VAL B 286 ? 0.3712 0.5119 0.3395 0.1312  0.0499  -0.0179 286 VAL B CB  
6454 C CG1 . VAL B 286 ? 0.4039 0.5542 0.3789 0.1200  0.0505  -0.0108 286 VAL B CG1 
6455 C CG2 . VAL B 286 ? 0.3525 0.4599 0.3101 0.1327  0.0463  -0.0224 286 VAL B CG2 
6456 N N   . GLU B 287 ? 0.2742 0.4195 0.2400 0.1528  0.0494  -0.0292 287 GLU B N   
6457 C CA  . GLU B 287 ? 0.2736 0.4059 0.2323 0.1624  0.0483  -0.0369 287 GLU B CA  
6458 C C   . GLU B 287 ? 0.2784 0.3850 0.2254 0.1597  0.0469  -0.0410 287 GLU B C   
6459 O O   . GLU B 287 ? 0.3352 0.4146 0.2779 0.1621  0.0423  -0.0438 287 GLU B O   
6460 C CB  . GLU B 287 ? 0.2834 0.4435 0.2434 0.1671  0.0528  -0.0398 287 GLU B CB  
6461 C CG  . GLU B 287 ? 0.3742 0.5587 0.3456 0.1705  0.0534  -0.0363 287 GLU B CG  
6462 C CD  . GLU B 287 ? 0.5313 0.7389 0.5036 0.1783  0.0566  -0.0407 287 GLU B CD  
6463 O OE1 . GLU B 287 ? 0.5709 0.7686 0.5350 0.1844  0.0571  -0.0482 287 GLU B OE1 
6464 O OE2 . GLU B 287 ? 0.6151 0.8513 0.5963 0.1779  0.0585  -0.0370 287 GLU B OE2 
6465 N N   . ARG B 288 ? 0.2887 0.4042 0.2304 0.1534  0.0504  -0.0406 288 ARG B N   
6466 C CA  . ARG B 288 ? 0.2972 0.3918 0.2271 0.1511  0.0492  -0.0449 288 ARG B CA  
6467 C C   . ARG B 288 ? 0.3111 0.3897 0.2398 0.1425  0.0468  -0.0401 288 ARG B C   
6468 O O   . ARG B 288 ? 0.3906 0.4803 0.3188 0.1348  0.0496  -0.0353 288 ARG B O   
6469 C CB  . ARG B 288 ? 0.2885 0.4017 0.2122 0.1493  0.0541  -0.0470 288 ARG B CB  
6470 C CG  . ARG B 288 ? 0.3033 0.4346 0.2290 0.1585  0.0566  -0.0524 288 ARG B CG  
6471 C CD  . ARG B 288 ? 0.3082 0.4660 0.2300 0.1552  0.0621  -0.0526 288 ARG B CD  
6472 N NE  . ARG B 288 ? 0.3552 0.5374 0.2832 0.1454  0.0654  -0.0431 288 ARG B NE  
6473 C CZ  . ARG B 288 ? 0.3932 0.5745 0.3165 0.1344  0.0664  -0.0373 288 ARG B CZ  
6474 N NH1 . ARG B 288 ? 0.4192 0.6219 0.3488 0.1247  0.0690  -0.0281 288 ARG B NH1 
6475 N NH2 . ARG B 288 ? 0.3849 0.5434 0.2970 0.1326  0.0644  -0.0403 288 ARG B NH2 
6476 N N   . ALA B 289 ? 0.2687 0.3216 0.1969 0.1435  0.0414  -0.0410 289 ALA B N   
6477 C CA  . ALA B 289 ? 0.2551 0.2950 0.1855 0.1366  0.0385  -0.0361 289 ALA B CA  
6478 C C   . ALA B 289 ? 0.2748 0.2918 0.1952 0.1311  0.0357  -0.0381 289 ALA B C   
6479 O O   . ALA B 289 ? 0.3208 0.3161 0.2404 0.1289  0.0307  -0.0380 289 ALA B O   
6480 C CB  . ALA B 289 ? 0.2969 0.3263 0.2338 0.1396  0.0341  -0.0345 289 ALA B CB  
6481 N N   . SER B 290 ? 0.2587 0.2820 0.1714 0.1279  0.0387  -0.0392 290 SER B N   
6482 C CA  . SER B 290 ? 0.3255 0.3278 0.2285 0.1229  0.0355  -0.0411 290 SER B CA  
6483 C C   . SER B 290 ? 0.3005 0.2968 0.2060 0.1149  0.0336  -0.0353 290 SER B C   
6484 O O   . SER B 290 ? 0.2700 0.2823 0.1815 0.1072  0.0351  -0.0287 290 SER B O   
6485 C CB  . SER B 290 ? 0.2966 0.3069 0.1892 0.1218  0.0387  -0.0439 290 SER B CB  
6486 O OG  . SER B 290 ? 0.2844 0.2762 0.1679 0.1162  0.0352  -0.0448 290 SER B OG  
6487 N N   . PRO B 291 ? 0.2790 0.2528 0.1826 0.1118  0.0284  -0.0360 291 PRO B N   
6488 C CA  . PRO B 291 ? 0.2502 0.2194 0.1594 0.1008  0.0247  -0.0298 291 PRO B CA  
6489 C C   . PRO B 291 ? 0.2683 0.2350 0.1717 0.0924  0.0233  -0.0279 291 PRO B C   
6490 O O   . PRO B 291 ? 0.2730 0.2342 0.1807 0.0845  0.0197  -0.0237 291 PRO B O   
6491 C CB  . PRO B 291 ? 0.2721 0.2210 0.1814 0.1018  0.0200  -0.0318 291 PRO B CB  
6492 C CG  . PRO B 291 ? 0.2688 0.2064 0.1702 0.1054  0.0188  -0.0375 291 PRO B CG  
6493 C CD  . PRO B 291 ? 0.2934 0.2475 0.1940 0.1130  0.0237  -0.0402 291 PRO B CD  
6494 N N   . TYR B 292 ? 0.2632 0.2347 0.1569 0.0943  0.0258  -0.0308 292 TYR B N   
6495 C CA  . TYR B 292 ? 0.2707 0.2390 0.1577 0.0869  0.0238  -0.0287 292 TYR B CA  
6496 C C   . TYR B 292 ? 0.2937 0.2801 0.1830 0.0803  0.0261  -0.0212 292 TYR B C   
6497 O O   . TYR B 292 ? 0.2869 0.2728 0.1699 0.0745  0.0245  -0.0183 292 TYR B O   
6498 C CB  . TYR B 292 ? 0.3021 0.2626 0.1755 0.0917  0.0240  -0.0365 292 TYR B CB  
6499 C CG  . TYR B 292 ? 0.2855 0.2256 0.1567 0.0968  0.0208  -0.0431 292 TYR B CG  
6500 C CD1 . TYR B 292 ? 0.3398 0.2664 0.2165 0.0917  0.0160  -0.0405 292 TYR B CD1 
6501 C CD2 . TYR B 292 ? 0.3690 0.3054 0.2362 0.1037  0.0216  -0.0500 292 TYR B CD2 
6502 C CE1 . TYR B 292 ? 0.3452 0.2558 0.2220 0.0932  0.0125  -0.0440 292 TYR B CE1 
6503 C CE2 . TYR B 292 ? 0.3597 0.2788 0.2298 0.1031  0.0169  -0.0522 292 TYR B CE2 
6504 C CZ  . TYR B 292 ? 0.4036 0.3107 0.2781 0.0973  0.0125  -0.0487 292 TYR B CZ  
6505 O OH  . TYR B 292 ? 0.4015 0.2938 0.2780 0.0957  0.0082  -0.0497 292 TYR B OH  
6506 N N   . LEU B 293 ? 0.2859 0.2882 0.1841 0.0804  0.0293  -0.0174 293 LEU B N   
6507 C CA  . LEU B 293 ? 0.2713 0.2918 0.1728 0.0730  0.0314  -0.0096 293 LEU B CA  
6508 C C   . LEU B 293 ? 0.2353 0.2527 0.1481 0.0649  0.0278  -0.0030 293 LEU B C   
6509 O O   . LEU B 293 ? 0.2473 0.2560 0.1670 0.0670  0.0257  -0.0051 293 LEU B O   
6510 C CB  . LEU B 293 ? 0.2534 0.2976 0.1574 0.0785  0.0378  -0.0105 293 LEU B CB  
6511 C CG  . LEU B 293 ? 0.4069 0.4646 0.3005 0.0852  0.0429  -0.0156 293 LEU B CG  
6512 C CD1 . LEU B 293 ? 0.4464 0.4865 0.3305 0.0946  0.0418  -0.0260 293 LEU B CD1 
6513 C CD2 . LEU B 293 ? 0.4385 0.5220 0.3384 0.0909  0.0489  -0.0161 293 LEU B CD2 
6514 N N   . ARG B 294 ? 0.2568 0.2817 0.1711 0.0554  0.0271  0.0051  294 ARG B N   
6515 C CA  . ARG B 294 ? 0.2786 0.3033 0.2039 0.0478  0.0242  0.0108  294 ARG B CA  
6516 C C   . ARG B 294 ? 0.2422 0.2897 0.1745 0.0475  0.0289  0.0133  294 ARG B C   
6517 O O   . ARG B 294 ? 0.2900 0.3558 0.2185 0.0460  0.0331  0.0164  294 ARG B O   
6518 C CB  . ARG B 294 ? 0.3047 0.3236 0.2285 0.0374  0.0199  0.0186  294 ARG B CB  
6519 C CG  . ARG B 294 ? 0.2910 0.3051 0.2258 0.0296  0.0157  0.0233  294 ARG B CG  
6520 C CD  . ARG B 294 ? 0.3825 0.3838 0.3155 0.0213  0.0097  0.0298  294 ARG B CD  
6521 N NE  . ARG B 294 ? 0.4119 0.4233 0.3374 0.0157  0.0113  0.0374  294 ARG B NE  
6522 C CZ  . ARG B 294 ? 0.3933 0.3966 0.3099 0.0140  0.0084  0.0406  294 ARG B CZ  
6523 N NH1 . ARG B 294 ? 0.3621 0.3473 0.2770 0.0177  0.0036  0.0365  294 ARG B NH1 
6524 N NH2 . ARG B 294 ? 0.4122 0.4277 0.3217 0.0083  0.0101  0.0483  294 ARG B NH2 
6525 N N   . TYR B 295 ? 0.2118 0.2606 0.1539 0.0491  0.0283  0.0119  295 TYR B N   
6526 C CA  . TYR B 295 ? 0.2187 0.2908 0.1686 0.0489  0.0323  0.0141  295 TYR B CA  
6527 C C   . TYR B 295 ? 0.2654 0.3415 0.2238 0.0366  0.0294  0.0213  295 TYR B C   
6528 O O   . TYR B 295 ? 0.2732 0.3315 0.2339 0.0312  0.0239  0.0223  295 TYR B O   
6529 C CB  . TYR B 295 ? 0.2103 0.2837 0.1656 0.0588  0.0333  0.0082  295 TYR B CB  
6530 C CG  . TYR B 295 ? 0.2458 0.3186 0.1935 0.0713  0.0367  0.0013  295 TYR B CG  
6531 C CD1 . TYR B 295 ? 0.2407 0.2909 0.1806 0.0759  0.0340  -0.0040 295 TYR B CD1 
6532 C CD2 . TYR B 295 ? 0.2305 0.3257 0.1786 0.0784  0.0424  -0.0004 295 TYR B CD2 
6533 C CE1 . TYR B 295 ? 0.2518 0.2989 0.1839 0.0869  0.0364  -0.0110 295 TYR B CE1 
6534 C CE2 . TYR B 295 ? 0.2514 0.3443 0.1922 0.0911  0.0450  -0.0081 295 TYR B CE2 
6535 C CZ  . TYR B 295 ? 0.2785 0.3456 0.2109 0.0949  0.0417  -0.0134 295 TYR B CZ  
6536 O OH  . TYR B 295 ? 0.2994 0.3611 0.2237 0.1067  0.0435  -0.0216 295 TYR B OH  
6537 N N   . TYR B 296 ? 0.2813 0.3816 0.2443 0.0321  0.0330  0.0261  296 TYR B N   
6538 C CA  . TYR B 296 ? 0.2839 0.3901 0.2553 0.0195  0.0303  0.0330  296 TYR B CA  
6539 C C   . TYR B 296 ? 0.2019 0.3288 0.1835 0.0219  0.0329  0.0317  296 TYR B C   
6540 O O   . TYR B 296 ? 0.2484 0.4004 0.2309 0.0257  0.0386  0.0322  296 TYR B O   
6541 C CB  . TYR B 296 ? 0.2976 0.4153 0.2651 0.0087  0.0314  0.0420  296 TYR B CB  
6542 C CG  . TYR B 296 ? 0.3444 0.4430 0.3016 0.0061  0.0283  0.0445  296 TYR B CG  
6543 C CD1 . TYR B 296 ? 0.4121 0.4843 0.3699 0.0020  0.0212  0.0450  296 TYR B CD1 
6544 C CD2 . TYR B 296 ? 0.4493 0.5577 0.3962 0.0084  0.0323  0.0458  296 TYR B CD2 
6545 C CE1 . TYR B 296 ? 0.4306 0.4867 0.3797 0.0004  0.0178  0.0475  296 TYR B CE1 
6546 C CE2 . TYR B 296 ? 0.4928 0.5852 0.4301 0.0059  0.0290  0.0484  296 TYR B CE2 
6547 C CZ  . TYR B 296 ? 0.3963 0.4624 0.3350 0.0020  0.0216  0.0496  296 TYR B CZ  
6548 O OH  . TYR B 296 ? 0.4306 0.4823 0.3603 0.0003  0.0179  0.0525  296 TYR B OH  
6549 N N   . PHE B 297 ? 0.2223 0.3407 0.2116 0.0200  0.0288  0.0298  297 PHE B N   
6550 C CA  . PHE B 297 ? 0.2511 0.3897 0.2505 0.0215  0.0304  0.0291  297 PHE B CA  
6551 C C   . PHE B 297 ? 0.2477 0.4044 0.2534 0.0076  0.0302  0.0366  297 PHE B C   
6552 O O   . PHE B 297 ? 0.2510 0.3952 0.2596 -0.0038 0.0249  0.0395  297 PHE B O   
6553 C CB  . PHE B 297 ? 0.2126 0.3371 0.2169 0.0242  0.0261  0.0242  297 PHE B CB  
6554 C CG  . PHE B 297 ? 0.1966 0.3419 0.2110 0.0250  0.0268  0.0240  297 PHE B CG  
6555 C CD1 . PHE B 297 ? 0.1788 0.3390 0.1947 0.0374  0.0308  0.0210  297 PHE B CD1 
6556 C CD2 . PHE B 297 ? 0.2153 0.3646 0.2376 0.0136  0.0231  0.0263  297 PHE B CD2 
6557 C CE1 . PHE B 297 ? 0.2146 0.3952 0.2400 0.0387  0.0311  0.0214  297 PHE B CE1 
6558 C CE2 . PHE B 297 ? 0.2026 0.3725 0.2341 0.0139  0.0234  0.0260  297 PHE B CE2 
6559 C CZ  . PHE B 297 ? 0.2116 0.3979 0.2449 0.0266  0.0274  0.0239  297 PHE B CZ  
6560 N N   . ARG B 298 ? 0.2175 0.4040 0.2258 0.0085  0.0358  0.0394  298 ARG B N   
6561 C CA  . ARG B 298 ? 0.2798 0.4893 0.2944 -0.0052 0.0364  0.0472  298 ARG B CA  
6562 C C   . ARG B 298 ? 0.2781 0.4733 0.2880 -0.0203 0.0325  0.0549  298 ARG B C   
6563 O O   . ARG B 298 ? 0.2484 0.4487 0.2639 -0.0348 0.0294  0.0611  298 ARG B O   
6564 C CB  . ARG B 298 ? 0.2346 0.4529 0.2608 -0.0097 0.0335  0.0465  298 ARG B CB  
6565 C CG  . ARG B 298 ? 0.2235 0.4544 0.2546 0.0051  0.0362  0.0400  298 ARG B CG  
6566 C CD  . ARG B 298 ? 0.2805 0.5274 0.3233 -0.0003 0.0337  0.0405  298 ARG B CD  
6567 N NE  . ARG B 298 ? 0.2885 0.5508 0.3359 0.0144  0.0364  0.0358  298 ARG B NE  
6568 C CZ  . ARG B 298 ? 0.3842 0.6520 0.4394 0.0152  0.0333  0.0338  298 ARG B CZ  
6569 N NH1 . ARG B 298 ? 0.3884 0.6476 0.4476 0.0023  0.0278  0.0348  298 ARG B NH1 
6570 N NH2 . ARG B 298 ? 0.3479 0.6291 0.4068 0.0294  0.0354  0.0306  298 ARG B NH2 
6571 N N   . GLU B 299 ? 0.2603 0.4364 0.2595 -0.0170 0.0321  0.0546  299 GLU B N   
6572 C CA  . GLU B 299 ? 0.2964 0.4545 0.2901 -0.0292 0.0274  0.0619  299 GLU B CA  
6573 C C   . GLU B 299 ? 0.3107 0.4447 0.3098 -0.0376 0.0192  0.0620  299 GLU B C   
6574 O O   . GLU B 299 ? 0.3831 0.5041 0.3803 -0.0499 0.0142  0.0691  299 GLU B O   
6575 C CB  . GLU B 299 ? 0.3764 0.5580 0.3691 -0.0418 0.0301  0.0725  299 GLU B CB  
6576 C CG  . GLU B 299 ? 0.3676 0.5757 0.3544 -0.0338 0.0383  0.0721  299 GLU B CG  
6577 C CD  . GLU B 299 ? 0.5404 0.7320 0.5142 -0.0274 0.0386  0.0705  299 GLU B CD  
6578 O OE1 . GLU B 299 ? 0.5773 0.7386 0.5471 -0.0304 0.0323  0.0715  299 GLU B OE1 
6579 O OE2 . GLU B 299 ? 0.6242 0.8341 0.5919 -0.0189 0.0451  0.0677  299 GLU B OE2 
6580 N N   . LEU B 300 ? 0.2998 0.4267 0.3048 -0.0310 0.0174  0.0540  300 LEU B N   
6581 C CA  . LEU B 300 ? 0.2873 0.3939 0.2976 -0.0375 0.0101  0.0519  300 LEU B CA  
6582 C C   . LEU B 300 ? 0.3305 0.4071 0.3358 -0.0306 0.0059  0.0463  300 LEU B C   
6583 O O   . LEU B 300 ? 0.3301 0.3852 0.3356 -0.0375 -0.0007 0.0474  300 LEU B O   
6584 C CB  . LEU B 300 ? 0.2794 0.3994 0.2994 -0.0352 0.0104  0.0465  300 LEU B CB  
6585 C CG  . LEU B 300 ? 0.3067 0.4572 0.3342 -0.0439 0.0131  0.0518  300 LEU B CG  
6586 C CD1 . LEU B 300 ? 0.3351 0.4986 0.3715 -0.0396 0.0131  0.0459  300 LEU B CD1 
6587 C CD2 . LEU B 300 ? 0.3784 0.5234 0.4078 -0.0623 0.0079  0.0597  300 LEU B CD2 
6588 N N   . ILE B 301 ? 0.2966 0.3715 0.2977 -0.0172 0.0092  0.0401  301 ILE B N   
6589 C CA  . ILE B 301 ? 0.2748 0.3256 0.2726 -0.0101 0.0056  0.0338  301 ILE B CA  
6590 C C   . ILE B 301 ? 0.2573 0.3080 0.2464 0.0007  0.0100  0.0314  301 ILE B C   
6591 O O   . ILE B 301 ? 0.3102 0.3796 0.2983 0.0064  0.0158  0.0311  301 ILE B O   
6592 C CB  . ILE B 301 ? 0.2780 0.3269 0.2830 -0.0067 0.0036  0.0265  301 ILE B CB  
6593 C CG1 . ILE B 301 ? 0.2851 0.3121 0.2874 -0.0003 0.0000  0.0199  301 ILE B CG1 
6594 C CG2 . ILE B 301 ? 0.2703 0.3411 0.2786 0.0009  0.0090  0.0241  301 ILE B CG2 
6595 C CD1 . ILE B 301 ? 0.2998 0.3260 0.3092 0.0004  -0.0028 0.0136  301 ILE B CD1 
6596 N N   . SER B 302 ? 0.2772 0.3073 0.2600 0.0036  0.0069  0.0296  302 SER B N   
6597 C CA  . SER B 302 ? 0.2555 0.2827 0.2295 0.0131  0.0100  0.0264  302 SER B CA  
6598 C C   . SER B 302 ? 0.2669 0.2886 0.2425 0.0227  0.0102  0.0183  302 SER B C   
6599 O O   . SER B 302 ? 0.2479 0.2599 0.2287 0.0218  0.0062  0.0149  302 SER B O   
6600 C CB  . SER B 302 ? 0.3113 0.3207 0.2778 0.0113  0.0061  0.0285  302 SER B CB  
6601 O OG  . SER B 302 ? 0.3924 0.4069 0.3561 0.0023  0.0058  0.0374  302 SER B OG  
6602 N N   . VAL B 303 ? 0.2452 0.2736 0.2161 0.0317  0.0148  0.0151  303 VAL B N   
6603 C CA  . VAL B 303 ? 0.2379 0.2611 0.2093 0.0405  0.0149  0.0088  303 VAL B CA  
6604 C C   . VAL B 303 ? 0.2369 0.2507 0.1982 0.0477  0.0162  0.0054  303 VAL B C   
6605 O O   . VAL B 303 ? 0.2416 0.2642 0.1970 0.0507  0.0202  0.0060  303 VAL B O   
6606 C CB  . VAL B 303 ? 0.2083 0.2496 0.1858 0.0452  0.0185  0.0080  303 VAL B CB  
6607 C CG1 . VAL B 303 ? 0.2290 0.2626 0.2062 0.0537  0.0178  0.0027  303 VAL B CG1 
6608 C CG2 . VAL B 303 ? 0.2652 0.3178 0.2527 0.0369  0.0170  0.0112  303 VAL B CG2 
6609 N N   . PHE B 304 ? 0.2443 0.2415 0.2034 0.0499  0.0128  0.0014  304 PHE B N   
6610 C CA  . PHE B 304 ? 0.2052 0.1926 0.1553 0.0566  0.0135  -0.0028 304 PHE B CA  
6611 C C   . PHE B 304 ? 0.2109 0.1960 0.1630 0.0633  0.0138  -0.0069 304 PHE B C   
6612 O O   . PHE B 304 ? 0.2501 0.2364 0.2096 0.0617  0.0118  -0.0068 304 PHE B O   
6613 C CB  . PHE B 304 ? 0.2258 0.1971 0.1716 0.0535  0.0090  -0.0037 304 PHE B CB  
6614 C CG  . PHE B 304 ? 0.2834 0.2545 0.2238 0.0489  0.0085  0.0003  304 PHE B CG  
6615 C CD1 . PHE B 304 ? 0.2655 0.2385 0.1959 0.0522  0.0112  -0.0006 304 PHE B CD1 
6616 C CD2 . PHE B 304 ? 0.2940 0.2623 0.2386 0.0415  0.0048  0.0050  304 PHE B CD2 
6617 C CE1 . PHE B 304 ? 0.3362 0.3103 0.2607 0.0476  0.0105  0.0039  304 PHE B CE1 
6618 C CE2 . PHE B 304 ? 0.3267 0.2938 0.2657 0.0371  0.0036  0.0100  304 PHE B CE2 
6619 C CZ  . PHE B 304 ? 0.3297 0.3008 0.2585 0.0399  0.0066  0.0099  304 PHE B CZ  
6620 N N   . PHE B 305 ? 0.2263 0.2083 0.1714 0.0710  0.0159  -0.0104 305 PHE B N   
6621 C CA  . PHE B 305 ? 0.2572 0.2335 0.2026 0.0777  0.0154  -0.0135 305 PHE B CA  
6622 C C   . PHE B 305 ? 0.2788 0.2364 0.2162 0.0785  0.0125  -0.0171 305 PHE B C   
6623 O O   . PHE B 305 ? 0.2530 0.2052 0.1816 0.0799  0.0133  -0.0195 305 PHE B O   
6624 C CB  . PHE B 305 ? 0.2568 0.2439 0.2014 0.0867  0.0197  -0.0149 305 PHE B CB  
6625 C CG  . PHE B 305 ? 0.2266 0.2356 0.1801 0.0854  0.0226  -0.0111 305 PHE B CG  
6626 C CD1 . PHE B 305 ? 0.2379 0.2603 0.1913 0.0808  0.0254  -0.0081 305 PHE B CD1 
6627 C CD2 . PHE B 305 ? 0.2481 0.2654 0.2099 0.0879  0.0221  -0.0098 305 PHE B CD2 
6628 C CE1 . PHE B 305 ? 0.2779 0.3213 0.2395 0.0779  0.0277  -0.0042 305 PHE B CE1 
6629 C CE2 . PHE B 305 ? 0.2762 0.3150 0.2464 0.0860  0.0245  -0.0064 305 PHE B CE2 
6630 C CZ  . PHE B 305 ? 0.2661 0.3180 0.2364 0.0806  0.0273  -0.0036 305 PHE B CZ  
6631 N N   . ARG B 306 ? 0.2676 0.2168 0.2076 0.0768  0.0091  -0.0175 306 ARG B N   
6632 C CA  . ARG B 306 ? 0.2479 0.1810 0.1811 0.0756  0.0059  -0.0203 306 ARG B CA  
6633 C C   . ARG B 306 ? 0.2848 0.2081 0.2096 0.0829  0.0067  -0.0239 306 ARG B C   
6634 O O   . ARG B 306 ? 0.2910 0.2182 0.2172 0.0898  0.0087  -0.0241 306 ARG B O   
6635 C CB  . ARG B 306 ? 0.2453 0.1747 0.1834 0.0717  0.0023  -0.0196 306 ARG B CB  
6636 C CG  . ARG B 306 ? 0.2458 0.1750 0.1860 0.0762  0.0023  -0.0186 306 ARG B CG  
6637 C CD  . ARG B 306 ? 0.2492 0.1764 0.1929 0.0714  -0.0012 -0.0174 306 ARG B CD  
6638 N NE  . ARG B 306 ? 0.2323 0.1576 0.1762 0.0757  -0.0018 -0.0154 306 ARG B NE  
6639 C CZ  . ARG B 306 ? 0.2973 0.2165 0.2402 0.0730  -0.0049 -0.0138 306 ARG B CZ  
6640 N NH1 . ARG B 306 ? 0.2459 0.1625 0.1882 0.0659  -0.0074 -0.0146 306 ARG B NH1 
6641 N NH2 . ARG B 306 ? 0.2887 0.2056 0.2313 0.0774  -0.0058 -0.0109 306 ARG B NH2 
6642 N N   . ASP B 307 ? 0.2312 0.1420 0.1475 0.0815  0.0047  -0.0271 307 ASP B N   
6643 C CA  . ASP B 307 ? 0.2269 0.1280 0.1374 0.0836  0.0036  -0.0300 307 ASP B CA  
6644 C C   . ASP B 307 ? 0.2812 0.1748 0.1951 0.0810  0.0001  -0.0280 307 ASP B C   
6645 O O   . ASP B 307 ? 0.2785 0.1652 0.1917 0.0750  -0.0032 -0.0275 307 ASP B O   
6646 C CB  . ASP B 307 ? 0.2574 0.1497 0.1587 0.0805  0.0019  -0.0335 307 ASP B CB  
6647 C CG  . ASP B 307 ? 0.3738 0.2558 0.2690 0.0825  0.0007  -0.0372 307 ASP B CG  
6648 O OD1 . ASP B 307 ? 0.3774 0.2519 0.2748 0.0825  -0.0016 -0.0364 307 ASP B OD1 
6649 O OD2 . ASP B 307 ? 0.3974 0.2781 0.2849 0.0841  0.0016  -0.0413 307 ASP B OD2 
6650 N N   . LYS B 308 ? 0.3004 0.1959 0.2176 0.0861  0.0008  -0.0267 308 LYS B N   
6651 C CA  . LYS B 308 ? 0.2759 0.1651 0.1958 0.0845  -0.0023 -0.0237 308 LYS B CA  
6652 C C   . LYS B 308 ? 0.3064 0.1782 0.2192 0.0810  -0.0062 -0.0253 308 LYS B C   
6653 O O   . LYS B 308 ? 0.3298 0.1948 0.2422 0.0760  -0.0095 -0.0230 308 LYS B O   
6654 C CB  . LYS B 308 ? 0.3168 0.2120 0.2412 0.0917  -0.0010 -0.0216 308 LYS B CB  
6655 C CG  . LYS B 308 ? 0.3573 0.2441 0.2826 0.0917  -0.0046 -0.0180 308 LYS B CG  
6656 C CD  . LYS B 308 ? 0.4214 0.3106 0.3491 0.1001  -0.0039 -0.0171 308 LYS B CD  
6657 C CE  . LYS B 308 ? 0.4337 0.3206 0.3646 0.1014  -0.0070 -0.0115 308 LYS B CE  
6658 N NZ  . LYS B 308 ? 0.3868 0.2667 0.3160 0.0942  -0.0105 -0.0081 308 LYS B NZ  
6659 N N   . THR B 309 ? 0.2949 0.1593 0.2014 0.0834  -0.0060 -0.0294 309 THR B N   
6660 C CA  . THR B 309 ? 0.3486 0.1958 0.2482 0.0796  -0.0101 -0.0311 309 THR B CA  
6661 C C   . THR B 309 ? 0.3403 0.1844 0.2372 0.0711  -0.0125 -0.0311 309 THR B C   
6662 O O   . THR B 309 ? 0.3186 0.1525 0.2134 0.0659  -0.0164 -0.0293 309 THR B O   
6663 C CB  . THR B 309 ? 0.4221 0.2632 0.3155 0.0840  -0.0094 -0.0367 309 THR B CB  
6664 O OG1 . THR B 309 ? 0.4274 0.2716 0.3239 0.0926  -0.0076 -0.0369 309 THR B OG1 
6665 C CG2 . THR B 309 ? 0.4298 0.2521 0.3159 0.0796  -0.0139 -0.0389 309 THR B CG2 
6666 N N   . LEU B 310 ? 0.3120 0.1646 0.2085 0.0697  -0.0106 -0.0330 310 LEU B N   
6667 C CA  . LEU B 310 ? 0.3055 0.1563 0.1999 0.0625  -0.0132 -0.0335 310 LEU B CA  
6668 C C   . LEU B 310 ? 0.2848 0.1402 0.1854 0.0591  -0.0145 -0.0298 310 LEU B C   
6669 O O   . LEU B 310 ? 0.3213 0.1707 0.2196 0.0532  -0.0182 -0.0299 310 LEU B O   
6670 C CB  . LEU B 310 ? 0.3080 0.1669 0.2008 0.0628  -0.0112 -0.0355 310 LEU B CB  
6671 C CG  . LEU B 310 ? 0.2882 0.1432 0.1727 0.0657  -0.0102 -0.0400 310 LEU B CG  
6672 C CD1 . LEU B 310 ? 0.3104 0.1731 0.1919 0.0658  -0.0087 -0.0410 310 LEU B CD1 
6673 C CD2 . LEU B 310 ? 0.3938 0.2346 0.2710 0.0616  -0.0142 -0.0433 310 LEU B CD2 
6674 N N   . SER B 311 ? 0.2845 0.1511 0.1926 0.0628  -0.0118 -0.0273 311 SER B N   
6675 C CA  . SER B 311 ? 0.3243 0.1976 0.2389 0.0600  -0.0129 -0.0245 311 SER B CA  
6676 C C   . SER B 311 ? 0.2700 0.1364 0.1838 0.0569  -0.0159 -0.0214 311 SER B C   
6677 O O   . SER B 311 ? 0.2875 0.1593 0.2045 0.0496  -0.0182 -0.0197 311 SER B O   
6678 C CB  . SER B 311 ? 0.2798 0.1673 0.2026 0.0640  -0.0094 -0.0225 311 SER B CB  
6679 O OG  . SER B 311 ? 0.2712 0.1650 0.1946 0.0652  -0.0071 -0.0241 311 SER B OG  
6680 N N   . ASP B 312 ? 0.2840 0.1385 0.1933 0.0623  -0.0164 -0.0206 312 ASP B N   
6681 C CA  . ASP B 312 ? 0.2811 0.1268 0.1887 0.0592  -0.0200 -0.0163 312 ASP B CA  
6682 C C   . ASP B 312 ? 0.3628 0.1930 0.2623 0.0521  -0.0242 -0.0174 312 ASP B C   
6683 O O   . ASP B 312 ? 0.3374 0.1644 0.2363 0.0451  -0.0277 -0.0128 312 ASP B O   
6684 C CB  . ASP B 312 ? 0.4058 0.2444 0.3124 0.0674  -0.0197 -0.0145 312 ASP B CB  
6685 C CG  . ASP B 312 ? 0.4289 0.2825 0.3437 0.0732  -0.0171 -0.0113 312 ASP B CG  
6686 O OD1 . ASP B 312 ? 0.4017 0.2722 0.3239 0.0680  -0.0161 -0.0094 312 ASP B OD1 
6687 O OD2 . ASP B 312 ? 0.4494 0.3051 0.3664 0.0798  -0.0156 -0.0107 312 ASP B OD2 
6688 N N   . LEU B 313 ? 0.2904 0.1129 0.1835 0.0526  -0.0241 -0.0230 313 LEU B N   
6689 C CA  . LEU B 313 ? 0.3766 0.1855 0.2619 0.0446  -0.0286 -0.0245 313 LEU B CA  
6690 C C   . LEU B 313 ? 0.2694 0.0936 0.1606 0.0345  -0.0299 -0.0220 313 LEU B C   
6691 O O   . LEU B 313 ? 0.3321 0.1525 0.2217 0.0260  -0.0336 -0.0186 313 LEU B O   
6692 C CB  . LEU B 313 ? 0.3621 0.1704 0.2433 0.0453  -0.0274 -0.0303 313 LEU B CB  
6693 C CG  . LEU B 313 ? 0.4134 0.2140 0.2919 0.0514  -0.0264 -0.0324 313 LEU B CG  
6694 C CD1 . LEU B 313 ? 0.4347 0.2375 0.3091 0.0526  -0.0248 -0.0382 313 LEU B CD1 
6695 C CD2 . LEU B 313 ? 0.3871 0.1683 0.2600 0.0476  -0.0313 -0.0308 313 LEU B CD2 
6696 N N   . ILE B 314 ? 0.2739 0.1159 0.1722 0.0354  -0.0270 -0.0234 314 ILE B N   
6697 C CA  . ILE B 314 ? 0.2589 0.1167 0.1637 0.0278  -0.0282 -0.0222 314 ILE B CA  
6698 C C   . ILE B 314 ? 0.2562 0.1240 0.1674 0.0250  -0.0283 -0.0170 314 ILE B C   
6699 O O   . ILE B 314 ? 0.2777 0.1525 0.1904 0.0166  -0.0307 -0.0147 314 ILE B O   
6700 C CB  . ILE B 314 ? 0.2345 0.1060 0.1452 0.0308  -0.0258 -0.0252 314 ILE B CB  
6701 C CG1 . ILE B 314 ? 0.2498 0.1128 0.1530 0.0326  -0.0261 -0.0294 314 ILE B CG1 
6702 C CG2 . ILE B 314 ? 0.2573 0.1464 0.1761 0.0251  -0.0271 -0.0249 314 ILE B CG2 
6703 C CD1 . ILE B 314 ? 0.3167 0.1914 0.2246 0.0349  -0.0247 -0.0311 314 ILE B CD1 
6704 N N   . GLY B 315 ? 0.2744 0.1448 0.1891 0.0315  -0.0257 -0.0150 315 GLY B N   
6705 C CA  . GLY B 315 ? 0.2769 0.1603 0.1981 0.0292  -0.0256 -0.0105 315 GLY B CA  
6706 C C   . GLY B 315 ? 0.3529 0.2271 0.2693 0.0240  -0.0290 -0.0046 315 GLY B C   
6707 O O   . GLY B 315 ? 0.3677 0.2547 0.2878 0.0178  -0.0300 -0.0006 315 GLY B O   
6708 N N   . PHE B 316 ? 0.3278 0.1799 0.2357 0.0265  -0.0310 -0.0039 316 PHE B N   
6709 C CA  . PHE B 316 ? 0.3329 0.1722 0.2359 0.0227  -0.0350 0.0028  316 PHE B CA  
6710 C C   . PHE B 316 ? 0.3809 0.1972 0.2738 0.0174  -0.0395 0.0024  316 PHE B C   
6711 O O   . PHE B 316 ? 0.3944 0.2031 0.2836 0.0095  -0.0438 0.0090  316 PHE B O   
6712 C CB  . PHE B 316 ? 0.3408 0.1732 0.2440 0.0329  -0.0342 0.0056  316 PHE B CB  
6713 C CG  . PHE B 316 ? 0.3247 0.1793 0.2374 0.0364  -0.0307 0.0071  316 PHE B CG  
6714 C CD1 . PHE B 316 ? 0.3890 0.2567 0.3053 0.0307  -0.0320 0.0136  316 PHE B CD1 
6715 C CD2 . PHE B 316 ? 0.3812 0.2446 0.2988 0.0446  -0.0263 0.0022  316 PHE B CD2 
6716 C CE1 . PHE B 316 ? 0.4468 0.3352 0.3714 0.0336  -0.0291 0.0142  316 PHE B CE1 
6717 C CE2 . PHE B 316 ? 0.4384 0.3214 0.3645 0.0468  -0.0237 0.0033  316 PHE B CE2 
6718 C CZ  . PHE B 316 ? 0.4269 0.3222 0.3565 0.0415  -0.0251 0.0087  316 PHE B CZ  
6719 N N   . SER B 317 ? 0.3413 0.1466 0.2289 0.0203  -0.0392 -0.0046 317 SER B N   
6720 C CA  . SER B 317 ? 0.3518 0.1333 0.2291 0.0156  -0.0440 -0.0059 317 SER B CA  
6721 C C   . SER B 317 ? 0.3666 0.1535 0.2422 0.0032  -0.0465 -0.0072 317 SER B C   
6722 O O   . SER B 317 ? 0.4043 0.1811 0.2750 -0.0072 -0.0514 -0.0030 317 SER B O   
6723 C CB  . SER B 317 ? 0.4472 0.2125 0.3181 0.0261  -0.0428 -0.0136 317 SER B CB  
6724 O OG  . SER B 317 ? 0.5113 0.2563 0.3737 0.0215  -0.0472 -0.0151 317 SER B OG  
6725 N N   . TYR B 318 ? 0.2991 0.1021 0.1789 0.0038  -0.0437 -0.0125 318 TYR B N   
6726 C CA  . TYR B 318 ? 0.3010 0.1073 0.1783 -0.0058 -0.0464 -0.0152 318 TYR B CA  
6727 C C   . TYR B 318 ? 0.3063 0.1288 0.1883 -0.0182 -0.0486 -0.0097 318 TYR B C   
6728 O O   . TYR B 318 ? 0.3597 0.1844 0.2392 -0.0277 -0.0517 -0.0109 318 TYR B O   
6729 C CB  . TYR B 318 ? 0.2852 0.1054 0.1663 -0.0007 -0.0431 -0.0214 318 TYR B CB  
6730 C CG  . TYR B 318 ? 0.2934 0.0992 0.1675 0.0083  -0.0417 -0.0276 318 TYR B CG  
6731 C CD1 . TYR B 318 ? 0.3168 0.0973 0.1801 0.0097  -0.0444 -0.0300 318 TYR B CD1 
6732 C CD2 . TYR B 318 ? 0.3423 0.1600 0.2200 0.0153  -0.0379 -0.0313 318 TYR B CD2 
6733 C CE1 . TYR B 318 ? 0.3712 0.1466 0.2305 0.0182  -0.0419 -0.0359 318 TYR B CE1 
6734 C CE2 . TYR B 318 ? 0.3446 0.1525 0.2155 0.0229  -0.0362 -0.0366 318 TYR B CE2 
6735 C CZ  . TYR B 318 ? 0.3894 0.1805 0.2529 0.0242  -0.0375 -0.0386 318 TYR B CZ  
6736 O OH  . TYR B 318 ? 0.3859 0.1796 0.2480 0.0309  -0.0342 -0.0426 318 TYR B OH  
6737 N N   . HIS B 319 ? 0.3231 0.1591 0.2118 -0.0187 -0.0471 -0.0038 319 HIS B N   
6738 C CA  . HIS B 319 ? 0.3617 0.2129 0.2532 -0.0314 -0.0494 0.0018  319 HIS B CA  
6739 C C   . HIS B 319 ? 0.4460 0.2765 0.3279 -0.0424 -0.0553 0.0063  319 HIS B C   
6740 O O   . HIS B 319 ? 0.5040 0.3448 0.3860 -0.0553 -0.0581 0.0091  319 HIS B O   
6741 C CB  . HIS B 319 ? 0.3615 0.2286 0.2597 -0.0306 -0.0472 0.0077  319 HIS B CB  
6742 C CG  . HIS B 319 ? 0.4037 0.2519 0.2963 -0.0295 -0.0494 0.0148  319 HIS B CG  
6743 N ND1 . HIS B 319 ? 0.4772 0.3181 0.3647 -0.0411 -0.0542 0.0233  319 HIS B ND1 
6744 C CD2 . HIS B 319 ? 0.4568 0.2917 0.3482 -0.0182 -0.0480 0.0151  319 HIS B CD2 
6745 C CE1 . HIS B 319 ? 0.4831 0.3054 0.3664 -0.0363 -0.0559 0.0288  319 HIS B CE1 
6746 N NE2 . HIS B 319 ? 0.5502 0.3696 0.4362 -0.0220 -0.0522 0.0236  319 HIS B NE2 
6747 N N   . ALA B 320 ? 0.5261 0.3276 0.3997 -0.0374 -0.0575 0.0068  320 ALA B N   
6748 C CA  . ALA B 320 ? 0.5856 0.3622 0.4492 -0.0470 -0.0639 0.0110  320 ALA B CA  
6749 C C   . ALA B 320 ? 0.6521 0.4162 0.5085 -0.0523 -0.0672 0.0042  320 ALA B C   
6750 O O   . ALA B 320 ? 0.7046 0.4480 0.5524 -0.0625 -0.0732 0.0070  320 ALA B O   
6751 C CB  . ALA B 320 ? 0.6482 0.3975 0.5060 -0.0379 -0.0655 0.0136  320 ALA B CB  
6752 N N   . TRP B 321 ? 0.5008 0.2770 0.3601 -0.0468 -0.0638 -0.0042 321 TRP B N   
6753 C CA  . TRP B 321 ? 0.4739 0.2389 0.3258 -0.0499 -0.0666 -0.0115 321 TRP B CA  
6754 C C   . TRP B 321 ? 0.4944 0.2838 0.3511 -0.0610 -0.0677 -0.0120 321 TRP B C   
6755 O O   . TRP B 321 ? 0.5711 0.3887 0.4382 -0.0618 -0.0646 -0.0094 321 TRP B O   
6756 C CB  . TRP B 321 ? 0.4211 0.1828 0.2717 -0.0357 -0.0627 -0.0204 321 TRP B CB  
6757 C CG  . TRP B 321 ? 0.4208 0.1619 0.2669 -0.0227 -0.0610 -0.0224 321 TRP B CG  
6758 C CD1 . TRP B 321 ? 0.3998 0.1387 0.2497 -0.0162 -0.0592 -0.0168 321 TRP B CD1 
6759 C CD2 . TRP B 321 ? 0.3865 0.1176 0.2280 -0.0134 -0.0592 -0.0297 321 TRP B CD2 
6760 N NE1 . TRP B 321 ? 0.4190 0.1459 0.2667 -0.0033 -0.0568 -0.0207 321 TRP B NE1 
6761 C CE2 . TRP B 321 ? 0.4052 0.1310 0.2494 -0.0015 -0.0561 -0.0284 321 TRP B CE2 
6762 C CE3 . TRP B 321 ? 0.3856 0.1174 0.2231 -0.0141 -0.0594 -0.0366 321 TRP B CE3 
6763 C CZ2 . TRP B 321 ? 0.4765 0.1990 0.3199 0.0091  -0.0530 -0.0341 321 TRP B CZ2 
6764 C CZ3 . TRP B 321 ? 0.3960 0.1225 0.2318 -0.0036 -0.0565 -0.0421 321 TRP B CZ3 
6765 C CH2 . TRP B 321 ? 0.4606 0.1830 0.2995 0.0076  -0.0533 -0.0410 321 TRP B CH2 
6766 N N   . ASN B 322 ? 0.4453 0.2244 0.2945 -0.0685 -0.0721 -0.0164 322 ASN B N   
6767 C CA  . ASN B 322 ? 0.4792 0.2813 0.3325 -0.0751 -0.0728 -0.0195 322 ASN B CA  
6768 C C   . ASN B 322 ? 0.5048 0.3200 0.3630 -0.0616 -0.0678 -0.0259 322 ASN B C   
6769 O O   . ASN B 322 ? 0.5362 0.3361 0.3900 -0.0500 -0.0653 -0.0301 322 ASN B O   
6770 C CB  . ASN B 322 ? 0.5391 0.3247 0.3818 -0.0861 -0.0791 -0.0231 322 ASN B CB  
6771 C CG  . ASN B 322 ? 0.6803 0.4891 0.5266 -0.0909 -0.0801 -0.0274 322 ASN B CG  
6772 O OD1 . ASN B 322 ? 0.7920 0.6291 0.6477 -0.0978 -0.0798 -0.0237 322 ASN B OD1 
6773 N ND2 . ASN B 322 ? 0.6491 0.4470 0.4877 -0.0871 -0.0814 -0.0355 322 ASN B ND2 
6774 N N   . ALA B 323 ? 0.4508 0.2952 0.3185 -0.0632 -0.0665 -0.0263 323 ALA B N   
6775 C CA  . ALA B 323 ? 0.4269 0.2850 0.3011 -0.0507 -0.0620 -0.0303 323 ALA B CA  
6776 C C   . ALA B 323 ? 0.4084 0.2531 0.2741 -0.0448 -0.0626 -0.0371 323 ALA B C   
6777 O O   . ALA B 323 ? 0.3841 0.2232 0.2492 -0.0330 -0.0587 -0.0395 323 ALA B O   
6778 C CB  . ALA B 323 ? 0.3628 0.2528 0.2484 -0.0534 -0.0618 -0.0299 323 ALA B CB  
6779 N N   . GLU B 324 ? 0.4029 0.2438 0.2617 -0.0536 -0.0674 -0.0402 324 GLU B N   
6780 C CA  . GLU B 324 ? 0.4493 0.2818 0.2999 -0.0483 -0.0680 -0.0470 324 GLU B CA  
6781 C C   . GLU B 324 ? 0.4636 0.2668 0.3029 -0.0423 -0.0673 -0.0505 324 GLU B C   
6782 O O   . GLU B 324 ? 0.5080 0.3100 0.3456 -0.0316 -0.0635 -0.0542 324 GLU B O   
6783 C CB  . GLU B 324 ? 0.6327 0.4706 0.4788 -0.0595 -0.0737 -0.0498 324 GLU B CB  
6784 C CG  . GLU B 324 ? 0.8015 0.6700 0.6594 -0.0657 -0.0749 -0.0464 324 GLU B CG  
6785 C CD  . GLU B 324 ? 1.0144 0.8966 0.8709 -0.0696 -0.0789 -0.0502 324 GLU B CD  
6786 O OE1 . GLU B 324 ? 1.1001 0.9704 0.9477 -0.0662 -0.0795 -0.0552 324 GLU B OE1 
6787 O OE2 . GLU B 324 ? 1.0754 0.9832 0.9413 -0.0752 -0.0808 -0.0480 324 GLU B OE2 
6788 N N   . ASP B 325 ? 0.4376 0.2235 0.2736 -0.0474 -0.0691 -0.0476 325 ASP B N   
6789 C CA  . ASP B 325 ? 0.4561 0.2215 0.2877 -0.0385 -0.0666 -0.0489 325 ASP B CA  
6790 C C   . ASP B 325 ? 0.4302 0.1980 0.2663 -0.0248 -0.0608 -0.0482 325 ASP B C   
6791 O O   . ASP B 325 ? 0.4163 0.1790 0.2510 -0.0142 -0.0569 -0.0515 325 ASP B O   
6792 C CB  . ASP B 325 ? 0.5334 0.2811 0.3620 -0.0465 -0.0704 -0.0441 325 ASP B CB  
6793 C CG  . ASP B 325 ? 0.6810 0.4099 0.5028 -0.0452 -0.0719 -0.0480 325 ASP B CG  
6794 O OD1 . ASP B 325 ? 0.6912 0.4226 0.5102 -0.0401 -0.0703 -0.0550 325 ASP B OD1 
6795 O OD2 . ASP B 325 ? 0.7436 0.4551 0.5626 -0.0490 -0.0749 -0.0443 325 ASP B OD2 
6796 N N   . ALA B 326 ? 0.3923 0.1713 0.2354 -0.0251 -0.0596 -0.0435 326 ALA B N   
6797 C CA  . ALA B 326 ? 0.3636 0.1476 0.2127 -0.0126 -0.0539 -0.0422 326 ALA B CA  
6798 C C   . ALA B 326 ? 0.3989 0.1946 0.2492 -0.0043 -0.0503 -0.0466 326 ALA B C   
6799 O O   . ALA B 326 ? 0.3493 0.1436 0.2002 0.0062  -0.0457 -0.0478 326 ALA B O   
6800 C CB  . ALA B 326 ? 0.3318 0.1339 0.1928 -0.0147 -0.0520 -0.0350 326 ALA B CB  
6801 N N   . VAL B 327 ? 0.3680 0.1797 0.2211 -0.0094 -0.0519 -0.0475 327 VAL B N   
6802 C CA  . VAL B 327 ? 0.3552 0.1777 0.2090 -0.0027 -0.0495 -0.0503 327 VAL B CA  
6803 C C   . VAL B 327 ? 0.4371 0.2482 0.2814 0.0017  -0.0485 -0.0554 327 VAL B C   
6804 O O   . VAL B 327 ? 0.4093 0.2244 0.2542 0.0106  -0.0441 -0.0562 327 VAL B O   
6805 C CB  . VAL B 327 ? 0.3114 0.1534 0.1707 -0.0089 -0.0524 -0.0496 327 VAL B CB  
6806 C CG1 . VAL B 327 ? 0.3603 0.2108 0.2183 -0.0027 -0.0513 -0.0518 327 VAL B CG1 
6807 C CG2 . VAL B 327 ? 0.2928 0.1535 0.1658 -0.0104 -0.0514 -0.0445 327 VAL B CG2 
6808 N N   . ARG B 328 ? 0.3697 0.1701 0.2076 -0.0049 -0.0519 -0.0579 328 ARG B N   
6809 C CA  . ARG B 328 ? 0.3780 0.1707 0.2093 -0.0005 -0.0504 -0.0629 328 ARG B CA  
6810 C C   . ARG B 328 ? 0.4077 0.1936 0.2405 0.0099  -0.0455 -0.0628 328 ARG B C   
6811 O O   . ARG B 328 ? 0.4716 0.2612 0.3021 0.0174  -0.0418 -0.0661 328 ARG B O   
6812 C CB  . ARG B 328 ? 0.4147 0.1947 0.2397 -0.0094 -0.0552 -0.0658 328 ARG B CB  
6813 C CG  . ARG B 328 ? 0.4706 0.2599 0.2941 -0.0201 -0.0601 -0.0667 328 ARG B CG  
6814 C CD  . ARG B 328 ? 0.5259 0.3022 0.3425 -0.0285 -0.0644 -0.0705 328 ARG B CD  
6815 N NE  . ARG B 328 ? 0.5882 0.3744 0.4061 -0.0412 -0.0697 -0.0689 328 ARG B NE  
6816 C CZ  . ARG B 328 ? 0.6457 0.4269 0.4648 -0.0522 -0.0737 -0.0650 328 ARG B CZ  
6817 N NH1 . ARG B 328 ? 0.5531 0.3165 0.3712 -0.0520 -0.0737 -0.0619 328 ARG B NH1 
6818 N NH2 . ARG B 328 ? 0.7897 0.5853 0.6113 -0.0636 -0.0780 -0.0635 328 ARG B NH2 
6819 N N   . ASP B 329 ? 0.3524 0.1292 0.1884 0.0101  -0.0457 -0.0590 329 ASP B N   
6820 C CA  . ASP B 329 ? 0.3549 0.1276 0.1935 0.0201  -0.0415 -0.0583 329 ASP B CA  
6821 C C   . ASP B 329 ? 0.3882 0.1766 0.2324 0.0284  -0.0361 -0.0570 329 ASP B C   
6822 O O   . ASP B 329 ? 0.4033 0.1940 0.2470 0.0365  -0.0322 -0.0596 329 ASP B O   
6823 C CB  . ASP B 329 ? 0.3773 0.1403 0.2190 0.0183  -0.0433 -0.0530 329 ASP B CB  
6824 C CG  . ASP B 329 ? 0.5116 0.2697 0.3558 0.0283  -0.0401 -0.0526 329 ASP B CG  
6825 O OD1 . ASP B 329 ? 0.5112 0.2563 0.3507 0.0305  -0.0414 -0.0563 329 ASP B OD1 
6826 O OD2 . ASP B 329 ? 0.4511 0.2187 0.3021 0.0340  -0.0366 -0.0488 329 ASP B OD2 
6827 N N   . PHE B 330 ? 0.3846 0.1839 0.2343 0.0263  -0.0360 -0.0532 330 PHE B N   
6828 C CA  . PHE B 330 ? 0.3942 0.2074 0.2498 0.0331  -0.0314 -0.0513 330 PHE B CA  
6829 C C   . PHE B 330 ? 0.3816 0.2017 0.2323 0.0359  -0.0298 -0.0548 330 PHE B C   
6830 O O   . PHE B 330 ? 0.3578 0.1838 0.2092 0.0431  -0.0254 -0.0550 330 PHE B O   
6831 C CB  . PHE B 330 ? 0.3092 0.1311 0.1711 0.0295  -0.0328 -0.0478 330 PHE B CB  
6832 C CG  . PHE B 330 ? 0.3152 0.1495 0.1842 0.0356  -0.0287 -0.0453 330 PHE B CG  
6833 C CD1 . PHE B 330 ? 0.3146 0.1508 0.1902 0.0401  -0.0257 -0.0420 330 PHE B CD1 
6834 C CD2 . PHE B 330 ? 0.3583 0.2027 0.2279 0.0362  -0.0287 -0.0456 330 PHE B CD2 
6835 C CE1 . PHE B 330 ? 0.3135 0.1618 0.1964 0.0446  -0.0223 -0.0396 330 PHE B CE1 
6836 C CE2 . PHE B 330 ? 0.3380 0.1943 0.2161 0.0404  -0.0253 -0.0421 330 PHE B CE2 
6837 C CZ  . PHE B 330 ? 0.2978 0.1553 0.1818 0.0445  -0.0222 -0.0397 330 PHE B CZ  
6838 N N   . ILE B 331 ? 0.3154 0.1359 0.1606 0.0299  -0.0335 -0.0574 331 ILE B N   
6839 C CA  . ILE B 331 ? 0.3685 0.1953 0.2072 0.0320  -0.0327 -0.0605 331 ILE B CA  
6840 C C   . ILE B 331 ? 0.3657 0.1870 0.1985 0.0370  -0.0300 -0.0653 331 ILE B C   
6841 O O   . ILE B 331 ? 0.3919 0.2204 0.2214 0.0426  -0.0264 -0.0667 331 ILE B O   
6842 C CB  . ILE B 331 ? 0.4161 0.2452 0.2501 0.0240  -0.0380 -0.0624 331 ILE B CB  
6843 C CG1 . ILE B 331 ? 0.4159 0.2538 0.2563 0.0206  -0.0408 -0.0584 331 ILE B CG1 
6844 C CG2 . ILE B 331 ? 0.4294 0.2641 0.2545 0.0257  -0.0377 -0.0658 331 ILE B CG2 
6845 C CD1 . ILE B 331 ? 0.4066 0.2561 0.2525 0.0266  -0.0379 -0.0546 331 ILE B CD1 
6846 N N   . GLY B 332 ? 0.3506 0.1589 0.1812 0.0349  -0.0318 -0.0682 332 GLY B N   
6847 C CA  . GLY B 332 ? 0.3755 0.1778 0.2009 0.0404  -0.0297 -0.0739 332 GLY B CA  
6848 C C   . GLY B 332 ? 0.3874 0.1943 0.2176 0.0501  -0.0244 -0.0725 332 GLY B C   
6849 O O   . GLY B 332 ? 0.4109 0.2213 0.2371 0.0563  -0.0212 -0.0771 332 GLY B O   
6850 N N   . ARG B 333 ? 0.3778 0.1865 0.2166 0.0512  -0.0235 -0.0665 333 ARG B N   
6851 C CA  . ARG B 333 ? 0.3636 0.1793 0.2078 0.0598  -0.0187 -0.0647 333 ARG B CA  
6852 C C   . ARG B 333 ? 0.3945 0.2257 0.2384 0.0630  -0.0149 -0.0637 333 ARG B C   
6853 O O   . ARG B 333 ? 0.3794 0.2179 0.2226 0.0700  -0.0106 -0.0655 333 ARG B O   
6854 C CB  . ARG B 333 ? 0.4052 0.2194 0.2581 0.0594  -0.0191 -0.0586 333 ARG B CB  
6855 C CG  . ARG B 333 ? 0.3765 0.1741 0.2282 0.0572  -0.0228 -0.0590 333 ARG B CG  
6856 C CD  . ARG B 333 ? 0.4059 0.2030 0.2650 0.0562  -0.0235 -0.0526 333 ARG B CD  
6857 N NE  . ARG B 333 ? 0.3807 0.1616 0.2384 0.0555  -0.0269 -0.0518 333 ARG B NE  
6858 C CZ  . ARG B 333 ? 0.4287 0.2060 0.2888 0.0629  -0.0256 -0.0515 333 ARG B CZ  
6859 N NH1 . ARG B 333 ? 0.4620 0.2520 0.3263 0.0714  -0.0208 -0.0524 333 ARG B NH1 
6860 N NH2 . ARG B 333 ? 0.5033 0.2645 0.3617 0.0618  -0.0294 -0.0501 333 ARG B NH2 
6861 N N   . LEU B 334 ? 0.3913 0.2277 0.2352 0.0579  -0.0166 -0.0608 334 LEU B N   
6862 C CA  . LEU B 334 ? 0.3467 0.1953 0.1879 0.0604  -0.0139 -0.0597 334 LEU B CA  
6863 C C   . LEU B 334 ? 0.3799 0.2313 0.2103 0.0622  -0.0127 -0.0652 334 LEU B C   
6864 O O   . LEU B 334 ? 0.3442 0.2062 0.1714 0.0672  -0.0086 -0.0653 334 LEU B O   
6865 C CB  . LEU B 334 ? 0.3468 0.1982 0.1893 0.0548  -0.0173 -0.0560 334 LEU B CB  
6866 C CG  . LEU B 334 ? 0.3572 0.2100 0.2106 0.0534  -0.0179 -0.0509 334 LEU B CG  
6867 C CD1 . LEU B 334 ? 0.3583 0.2156 0.2139 0.0480  -0.0218 -0.0484 334 LEU B CD1 
6868 C CD2 . LEU B 334 ? 0.3568 0.2173 0.2162 0.0594  -0.0131 -0.0477 334 LEU B CD2 
6869 N N   . LYS B 335 ? 0.3747 0.2179 0.1989 0.0580  -0.0163 -0.0701 335 LYS B N   
6870 C CA  . LYS B 335 ? 0.4054 0.2521 0.2193 0.0593  -0.0153 -0.0763 335 LYS B CA  
6871 C C   . LYS B 335 ? 0.4161 0.2652 0.2299 0.0676  -0.0104 -0.0804 335 LYS B C   
6872 O O   . LYS B 335 ? 0.4140 0.2748 0.2217 0.0714  -0.0067 -0.0829 335 LYS B O   
6873 C CB  . LYS B 335 ? 0.4354 0.2719 0.2438 0.0526  -0.0203 -0.0812 335 LYS B CB  
6874 C CG  . LYS B 335 ? 0.6523 0.4936 0.4494 0.0526  -0.0199 -0.0880 335 LYS B CG  
6875 C CD  . LYS B 335 ? 0.7502 0.5950 0.5416 0.0445  -0.0248 -0.0874 335 LYS B CD  
6876 C CE  . LYS B 335 ? 0.8068 0.6397 0.6017 0.0368  -0.0304 -0.0873 335 LYS B CE  
6877 N NZ  . LYS B 335 ? 0.8226 0.6593 0.6111 0.0288  -0.0354 -0.0892 335 LYS B NZ  
6878 N N   . LYS B 336 ? 0.4029 0.2424 0.2231 0.0706  -0.0104 -0.0809 336 LYS B N   
6879 C CA  . LYS B 336 ? 0.4339 0.2764 0.2553 0.0794  -0.0062 -0.0847 336 LYS B CA  
6880 C C   . LYS B 336 ? 0.4132 0.2731 0.2381 0.0848  -0.0008 -0.0807 336 LYS B C   
6881 O O   . LYS B 336 ? 0.4396 0.3105 0.2609 0.0907  0.0035  -0.0846 336 LYS B O   
6882 C CB  . LYS B 336 ? 0.4936 0.3227 0.3216 0.0816  -0.0080 -0.0841 336 LYS B CB  
6883 C CG  . LYS B 336 ? 0.6480 0.4790 0.4784 0.0918  -0.0044 -0.0880 336 LYS B CG  
6884 C CD  . LYS B 336 ? 0.7462 0.5945 0.5835 0.0982  0.0007  -0.0835 336 LYS B CD  
6885 C CE  . LYS B 336 ? 0.7297 0.5756 0.5772 0.0983  -0.0002 -0.0762 336 LYS B CE  
6886 N NZ  . LYS B 336 ? 0.7804 0.6439 0.6340 0.1048  0.0049  -0.0733 336 LYS B NZ  
6887 N N   . ILE B 337 ? 0.4058 0.2690 0.2378 0.0828  -0.0009 -0.0731 337 ILE B N   
6888 C CA  . ILE B 337 ? 0.3489 0.2280 0.1841 0.0870  0.0040  -0.0690 337 ILE B CA  
6889 C C   . ILE B 337 ? 0.4003 0.2919 0.2255 0.0862  0.0062  -0.0699 337 ILE B C   
6890 O O   . ILE B 337 ? 0.4008 0.3076 0.2239 0.0911  0.0113  -0.0707 337 ILE B O   
6891 C CB  . ILE B 337 ? 0.3273 0.2062 0.1710 0.0838  0.0028  -0.0615 337 ILE B CB  
6892 C CG1 . ILE B 337 ? 0.3634 0.2336 0.2166 0.0847  0.0012  -0.0597 337 ILE B CG1 
6893 C CG2 . ILE B 337 ? 0.3593 0.2542 0.2047 0.0870  0.0076  -0.0573 337 ILE B CG2 
6894 C CD1 . ILE B 337 ? 0.3393 0.2087 0.2005 0.0799  -0.0008 -0.0532 337 ILE B CD1 
6895 N N   . HIS B 338 ? 0.3478 0.2349 0.1667 0.0795  0.0022  -0.0692 338 HIS B N   
6896 C CA  . HIS B 338 ? 0.3498 0.2479 0.1574 0.0775  0.0030  -0.0693 338 HIS B CA  
6897 C C   . HIS B 338 ? 0.4065 0.3129 0.2075 0.0816  0.0065  -0.0764 338 HIS B C   
6898 O O   . HIS B 338 ? 0.4401 0.3638 0.2355 0.0831  0.0106  -0.0751 338 HIS B O   
6899 C CB  . HIS B 338 ? 0.3899 0.2795 0.1923 0.0699  -0.0033 -0.0691 338 HIS B CB  
6900 C CG  . HIS B 338 ? 0.4216 0.3223 0.2123 0.0669  -0.0041 -0.0673 338 HIS B CG  
6901 N ND1 . HIS B 338 ? 0.5023 0.4020 0.2845 0.0628  -0.0073 -0.0721 338 HIS B ND1 
6902 C CD2 . HIS B 338 ? 0.4282 0.3435 0.2189 0.0650  -0.0026 -0.0588 338 HIS B CD2 
6903 C CE1 . HIS B 338 ? 0.5038 0.4161 0.2769 0.0604  -0.0078 -0.0677 338 HIS B CE1 
6904 N NE2 . HIS B 338 ? 0.4899 0.4119 0.2697 0.0609  -0.0050 -0.0586 338 HIS B NE2 
6905 N N   . GLU B 339 ? 0.3834 0.2781 0.1847 0.0828  0.0048  -0.0837 339 GLU B N   
6906 C CA  . GLU B 339 ? 0.3846 0.2847 0.1789 0.0865  0.0074  -0.0920 339 GLU B CA  
6907 C C   . GLU B 339 ? 0.4531 0.3627 0.2528 0.0955  0.0130  -0.0941 339 GLU B C   
6908 O O   . GLU B 339 ? 0.4684 0.3867 0.2625 0.0995  0.0162  -0.1008 339 GLU B O   
6909 C CB  . GLU B 339 ? 0.4807 0.3629 0.2720 0.0838  0.0028  -0.0994 339 GLU B CB  
6910 C CG  . GLU B 339 ? 0.5553 0.4334 0.3396 0.0747  -0.0023 -0.0987 339 GLU B CG  
6911 C CD  . GLU B 339 ? 0.6750 0.5346 0.4582 0.0704  -0.0075 -0.1043 339 GLU B CD  
6912 O OE1 . GLU B 339 ? 0.7663 0.6252 0.5416 0.0640  -0.0109 -0.1072 339 GLU B OE1 
6913 O OE2 . GLU B 339 ? 0.7121 0.5584 0.5021 0.0729  -0.0084 -0.1052 339 GLU B OE2 
6914 N N   . SER B 340 ? 0.4674 0.3768 0.2778 0.0987  0.0141  -0.0887 340 SER B N   
6915 C CA  . SER B 340 ? 0.4391 0.3570 0.2560 0.1075  0.0185  -0.0906 340 SER B CA  
6916 C C   . SER B 340 ? 0.4768 0.4202 0.2938 0.1100  0.0247  -0.0867 340 SER B C   
6917 O O   . SER B 340 ? 0.4665 0.4219 0.2879 0.1172  0.0288  -0.0891 340 SER B O   
6918 C CB  . SER B 340 ? 0.4027 0.3097 0.2310 0.1093  0.0165  -0.0863 340 SER B CB  
6919 O OG  . SER B 340 ? 0.4675 0.3836 0.3017 0.1072  0.0179  -0.0777 340 SER B OG  
6920 N N   . VAL B 341 ? 0.4828 0.4357 0.2952 0.1039  0.0252  -0.0804 341 VAL B N   
6921 C CA  . VAL B 341 ? 0.4377 0.4156 0.2501 0.1044  0.0308  -0.0748 341 VAL B CA  
6922 C C   . VAL B 341 ? 0.4489 0.4374 0.2492 0.0979  0.0310  -0.0724 341 VAL B C   
6923 O O   . VAL B 341 ? 0.4924 0.4682 0.2860 0.0923  0.0260  -0.0722 341 VAL B O   
6924 C CB  . VAL B 341 ? 0.4821 0.4627 0.3033 0.1031  0.0315  -0.0657 341 VAL B CB  
6925 C CG1 . VAL B 341 ? 0.4694 0.4462 0.3028 0.1098  0.0322  -0.0672 341 VAL B CG1 
6926 C CG2 . VAL B 341 ? 0.4679 0.4309 0.2868 0.0966  0.0259  -0.0614 341 VAL B CG2 
6927 N N   . ASP B 342 ? 0.4748 0.4885 0.2728 0.0980  0.0365  -0.0696 342 ASP B N   
6928 C CA  . ASP B 342 ? 0.5763 0.6048 0.3634 0.0910  0.0371  -0.0648 342 ASP B CA  
6929 C C   . ASP B 342 ? 0.5607 0.5929 0.3470 0.0837  0.0354  -0.0519 342 ASP B C   
6930 O O   . ASP B 342 ? 0.6158 0.6527 0.3926 0.0767  0.0330  -0.0462 342 ASP B O   
6931 C CB  . ASP B 342 ? 0.6674 0.7230 0.4534 0.0927  0.0436  -0.0656 342 ASP B CB  
6932 C CG  . ASP B 342 ? 0.7989 0.8531 0.5791 0.0976  0.0444  -0.0779 342 ASP B CG  
6933 O OD1 . ASP B 342 ? 0.8830 0.9180 0.6567 0.0964  0.0396  -0.0841 342 ASP B OD1 
6934 O OD2 . ASP B 342 ? 0.7943 0.8673 0.5764 0.1024  0.0497  -0.0814 342 ASP B OD2 
6935 N N   . PHE B 343 ? 0.4840 0.5143 0.2805 0.0850  0.0363  -0.0464 343 PHE B N   
6936 C CA  . PHE B 343 ? 0.4495 0.4812 0.2553 0.0745  0.0334  -0.0322 343 PHE B CA  
6937 C C   . PHE B 343 ? 0.3491 0.3553 0.1609 0.0714  0.0262  -0.0311 343 PHE B C   
6938 O O   . PHE B 343 ? 0.4377 0.4269 0.2459 0.0759  0.0236  -0.0403 343 PHE B O   
6939 C CB  . PHE B 343 ? 0.3838 0.4308 0.2018 0.0746  0.0380  -0.0262 343 PHE B CB  
6940 C CG  . PHE B 343 ? 0.3660 0.4037 0.1939 0.0832  0.0391  -0.0327 343 PHE B CG  
6941 C CD1 . PHE B 343 ? 0.3986 0.4440 0.2237 0.0949  0.0441  -0.0432 343 PHE B CD1 
6942 C CD2 . PHE B 343 ? 0.3838 0.4061 0.2236 0.0800  0.0348  -0.0282 343 PHE B CD2 
6943 C CE1 . PHE B 343 ? 0.4216 0.4577 0.2566 0.1025  0.0442  -0.0477 343 PHE B CE1 
6944 C CE2 . PHE B 343 ? 0.4344 0.4490 0.2826 0.0873  0.0355  -0.0331 343 PHE B CE2 
6945 C CZ  . PHE B 343 ? 0.4275 0.4487 0.2729 0.0988  0.0401  -0.0424 343 PHE B CZ  
6946 N N   . GLN B 344 ? 0.3227 0.3264 0.1439 0.0634  0.0227  -0.0200 344 GLN B N   
6947 C CA  . GLN B 344 ? 0.3294 0.3125 0.1570 0.0606  0.0161  -0.0189 344 GLN B CA  
6948 C C   . GLN B 344 ? 0.3051 0.2820 0.1461 0.0636  0.0169  -0.0196 344 GLN B C   
6949 O O   . GLN B 344 ? 0.3122 0.2971 0.1629 0.0600  0.0181  -0.0120 344 GLN B O   
6950 C CB  . GLN B 344 ? 0.3290 0.3116 0.1586 0.0516  0.0110  -0.0077 344 GLN B CB  
6951 C CG  . GLN B 344 ? 0.3170 0.3058 0.1325 0.0486  0.0094  -0.0064 344 GLN B CG  
6952 C CD  . GLN B 344 ? 0.4046 0.3890 0.2214 0.0408  0.0027  0.0042  344 GLN B CD  
6953 O OE1 . GLN B 344 ? 0.3965 0.3735 0.2074 0.0398  -0.0024 0.0027  344 GLN B OE1 
6954 N NE2 . GLN B 344 ? 0.3502 0.3391 0.1749 0.0355  0.0022  0.0150  344 GLN B NE2 
6955 N N   . PRO B 345 ? 0.3247 0.2876 0.1666 0.0694  0.0160  -0.0280 345 PRO B N   
6956 C CA  . PRO B 345 ? 0.3251 0.2834 0.1788 0.0724  0.0167  -0.0283 345 PRO B CA  
6957 C C   . PRO B 345 ? 0.3300 0.2790 0.1936 0.0661  0.0116  -0.0225 345 PRO B C   
6958 O O   . PRO B 345 ? 0.2988 0.2393 0.1599 0.0618  0.0066  -0.0214 345 PRO B O   
6959 C CB  . PRO B 345 ? 0.3256 0.2702 0.1744 0.0798  0.0163  -0.0387 345 PRO B CB  
6960 C CG  . PRO B 345 ? 0.3307 0.2655 0.1681 0.0766  0.0122  -0.0423 345 PRO B CG  
6961 C CD  . PRO B 345 ? 0.3777 0.3281 0.2088 0.0724  0.0137  -0.0372 345 PRO B CD  
6962 N N   . VAL B 346 ? 0.2559 0.2083 0.1310 0.0661  0.0127  -0.0193 346 VAL B N   
6963 C CA  . VAL B 346 ? 0.2626 0.2068 0.1478 0.0617  0.0083  -0.0158 346 VAL B CA  
6964 C C   . VAL B 346 ? 0.2694 0.2048 0.1590 0.0663  0.0081  -0.0210 346 VAL B C   
6965 O O   . VAL B 346 ? 0.2754 0.2169 0.1689 0.0710  0.0117  -0.0222 346 VAL B O   
6966 C CB  . VAL B 346 ? 0.2850 0.2391 0.1796 0.0567  0.0089  -0.0080 346 VAL B CB  
6967 C CG1 . VAL B 346 ? 0.2966 0.2415 0.2008 0.0528  0.0039  -0.0059 346 VAL B CG1 
6968 C CG2 . VAL B 346 ? 0.3195 0.2825 0.2084 0.0517  0.0093  -0.0016 346 VAL B CG2 
6969 N N   . VAL B 347 ? 0.2641 0.1867 0.1537 0.0645  0.0035  -0.0233 347 VAL B N   
6970 C CA  . VAL B 347 ? 0.2448 0.1577 0.1364 0.0674  0.0024  -0.0276 347 VAL B CA  
6971 C C   . VAL B 347 ? 0.2520 0.1639 0.1543 0.0632  -0.0006 -0.0245 347 VAL B C   
6972 O O   . VAL B 347 ? 0.2705 0.1783 0.1738 0.0589  -0.0047 -0.0238 347 VAL B O   
6973 C CB  . VAL B 347 ? 0.3037 0.2038 0.1854 0.0678  -0.0003 -0.0332 347 VAL B CB  
6974 C CG1 . VAL B 347 ? 0.2705 0.1596 0.1540 0.0697  -0.0019 -0.0363 347 VAL B CG1 
6975 C CG2 . VAL B 347 ? 0.3094 0.2111 0.1794 0.0722  0.0026  -0.0377 347 VAL B CG2 
6976 N N   . PHE B 348 ? 0.2415 0.1588 0.1521 0.0649  0.0012  -0.0230 348 PHE B N   
6977 C CA  . PHE B 348 ? 0.2419 0.1598 0.1623 0.0614  -0.0014 -0.0212 348 PHE B CA  
6978 C C   . PHE B 348 ? 0.2650 0.1750 0.1853 0.0625  -0.0031 -0.0240 348 PHE B C   
6979 O O   . PHE B 348 ? 0.2765 0.1844 0.1950 0.0672  -0.0012 -0.0252 348 PHE B O   
6980 C CB  . PHE B 348 ? 0.2506 0.1799 0.1798 0.0614  0.0011  -0.0179 348 PHE B CB  
6981 C CG  . PHE B 348 ? 0.2281 0.1627 0.1619 0.0563  0.0000  -0.0138 348 PHE B CG  
6982 C CD1 . PHE B 348 ? 0.2382 0.1761 0.1667 0.0550  0.0012  -0.0110 348 PHE B CD1 
6983 C CD2 . PHE B 348 ? 0.2491 0.1849 0.1919 0.0527  -0.0028 -0.0129 348 PHE B CD2 
6984 C CE1 . PHE B 348 ? 0.2522 0.1929 0.1846 0.0495  -0.0007 -0.0059 348 PHE B CE1 
6985 C CE2 . PHE B 348 ? 0.2392 0.1767 0.1861 0.0481  -0.0047 -0.0094 348 PHE B CE2 
6986 C CZ  . PHE B 348 ? 0.2508 0.1898 0.1925 0.0463  -0.0039 -0.0053 348 PHE B CZ  
6987 N N   . VAL B 349 ? 0.2241 0.1305 0.1468 0.0582  -0.0070 -0.0245 349 VAL B N   
6988 C CA  . VAL B 349 ? 0.2436 0.1449 0.1669 0.0569  -0.0091 -0.0259 349 VAL B CA  
6989 C C   . VAL B 349 ? 0.2150 0.1251 0.1488 0.0542  -0.0100 -0.0243 349 VAL B C   
6990 O O   . VAL B 349 ? 0.2221 0.1357 0.1601 0.0511  -0.0123 -0.0246 349 VAL B O   
6991 C CB  . VAL B 349 ? 0.2433 0.1367 0.1606 0.0534  -0.0126 -0.0283 349 VAL B CB  
6992 C CG1 . VAL B 349 ? 0.2607 0.1498 0.1784 0.0505  -0.0149 -0.0286 349 VAL B CG1 
6993 C CG2 . VAL B 349 ? 0.2793 0.1647 0.1857 0.0559  -0.0117 -0.0308 349 VAL B CG2 
6994 N N   . VAL B 350 ? 0.1912 0.1055 0.1291 0.0561  -0.0085 -0.0229 350 VAL B N   
6995 C CA  . VAL B 350 ? 0.1958 0.1205 0.1432 0.0540  -0.0089 -0.0220 350 VAL B CA  
6996 C C   . VAL B 350 ? 0.2260 0.1514 0.1744 0.0534  -0.0097 -0.0212 350 VAL B C   
6997 O O   . VAL B 350 ? 0.2173 0.1389 0.1625 0.0570  -0.0085 -0.0195 350 VAL B O   
6998 C CB  . VAL B 350 ? 0.2328 0.1659 0.1851 0.0560  -0.0061 -0.0201 350 VAL B CB  
6999 C CG1 . VAL B 350 ? 0.2053 0.1485 0.1673 0.0528  -0.0074 -0.0204 350 VAL B CG1 
7000 C CG2 . VAL B 350 ? 0.2628 0.1950 0.2123 0.0562  -0.0049 -0.0193 350 VAL B CG2 
7001 N N   . LEU B 351 ? 0.2068 0.1380 0.1597 0.0491  -0.0120 -0.0222 351 LEU B N   
7002 C CA  . LEU B 351 ? 0.1773 0.1118 0.1309 0.0471  -0.0131 -0.0205 351 LEU B CA  
7003 C C   . LEU B 351 ? 0.1705 0.1170 0.1308 0.0429  -0.0147 -0.0227 351 LEU B C   
7004 O O   . LEU B 351 ? 0.1989 0.1482 0.1627 0.0423  -0.0156 -0.0260 351 LEU B O   
7005 C CB  . LEU B 351 ? 0.2436 0.1659 0.1889 0.0456  -0.0148 -0.0193 351 LEU B CB  
7006 C CG  . LEU B 351 ? 0.2542 0.1728 0.1965 0.0413  -0.0172 -0.0219 351 LEU B CG  
7007 C CD1 . LEU B 351 ? 0.2753 0.1888 0.2129 0.0361  -0.0198 -0.0200 351 LEU B CD1 
7008 C CD2 . LEU B 351 ? 0.2929 0.2012 0.2289 0.0442  -0.0165 -0.0238 351 LEU B CD2 
7009 N N   . ASP B 352 ? 0.1704 0.1245 0.1323 0.0403  -0.0154 -0.0210 352 ASP B N   
7010 C CA  . ASP B 352 ? 0.2087 0.1766 0.1761 0.0363  -0.0168 -0.0239 352 ASP B CA  
7011 C C   . ASP B 352 ? 0.2146 0.1805 0.1805 0.0337  -0.0188 -0.0267 352 ASP B C   
7012 O O   . ASP B 352 ? 0.2201 0.1756 0.1793 0.0320  -0.0197 -0.0247 352 ASP B O   
7013 C CB  . ASP B 352 ? 0.1972 0.1737 0.1643 0.0328  -0.0174 -0.0205 352 ASP B CB  
7014 C CG  . ASP B 352 ? 0.2378 0.2195 0.2071 0.0353  -0.0160 -0.0175 352 ASP B CG  
7015 O OD1 . ASP B 352 ? 0.2189 0.1995 0.1911 0.0394  -0.0144 -0.0188 352 ASP B OD1 
7016 O OD2 . ASP B 352 ? 0.2274 0.2151 0.1954 0.0328  -0.0168 -0.0133 352 ASP B OD2 
7017 N N   . GLY B 353 ? 0.1469 0.1226 0.1192 0.0336  -0.0198 -0.0317 353 GLY B N   
7018 C CA  . GLY B 353 ? 0.1697 0.1455 0.1418 0.0323  -0.0220 -0.0344 353 GLY B CA  
7019 C C   . GLY B 353 ? 0.1847 0.1745 0.1586 0.0275  -0.0233 -0.0357 353 GLY B C   
7020 O O   . GLY B 353 ? 0.1765 0.1690 0.1506 0.0260  -0.0252 -0.0378 353 GLY B O   
7021 N N   . GLU B 354 ? 0.1742 0.1747 0.1492 0.0245  -0.0224 -0.0339 354 GLU B N   
7022 C CA  . GLU B 354 ? 0.1633 0.1814 0.1404 0.0192  -0.0234 -0.0350 354 GLU B CA  
7023 C C   . GLU B 354 ? 0.2033 0.2230 0.1748 0.0126  -0.0234 -0.0280 354 GLU B C   
7024 O O   . GLU B 354 ? 0.2033 0.2392 0.1759 0.0067  -0.0241 -0.0277 354 GLU B O   
7025 C CB  . GLU B 354 ? 0.1364 0.1737 0.1219 0.0215  -0.0229 -0.0417 354 GLU B CB  
7026 C CG  . GLU B 354 ? 0.1555 0.2002 0.1416 0.0208  -0.0213 -0.0398 354 GLU B CG  
7027 C CD  . GLU B 354 ? 0.1369 0.1692 0.1237 0.0259  -0.0202 -0.0393 354 GLU B CD  
7028 O OE1 . GLU B 354 ? 0.1636 0.2036 0.1564 0.0287  -0.0200 -0.0450 354 GLU B OE1 
7029 O OE2 . GLU B 354 ? 0.1737 0.1897 0.1551 0.0268  -0.0197 -0.0339 354 GLU B OE2 
7030 N N   . ASN B 355 ? 0.1654 0.1696 0.1312 0.0135  -0.0229 -0.0221 355 ASN B N   
7031 C CA  . ASN B 355 ? 0.1584 0.1634 0.1194 0.0079  -0.0236 -0.0147 355 ASN B CA  
7032 C C   . ASN B 355 ? 0.2365 0.2245 0.1889 0.0031  -0.0259 -0.0092 355 ASN B C   
7033 O O   . ASN B 355 ? 0.2263 0.2162 0.1748 -0.0039 -0.0275 -0.0027 355 ASN B O   
7034 C CB  . ASN B 355 ? 0.1824 0.1839 0.1434 0.0124  -0.0223 -0.0114 355 ASN B CB  
7035 C CG  . ASN B 355 ? 0.1793 0.2000 0.1479 0.0145  -0.0207 -0.0162 355 ASN B CG  
7036 O OD1 . ASN B 355 ? 0.1761 0.2157 0.1483 0.0107  -0.0209 -0.0195 355 ASN B OD1 
7037 N ND2 . ASN B 355 ? 0.1957 0.2128 0.1671 0.0205  -0.0193 -0.0175 355 ASN B ND2 
7038 N N   . CYS B 356 ? 0.2257 0.1974 0.1746 0.0057  -0.0264 -0.0115 356 CYS B N   
7039 C CA  . CYS B 356 ? 0.2140 0.1675 0.1540 0.0012  -0.0290 -0.0071 356 CYS B CA  
7040 C C   . CYS B 356 ? 0.2384 0.1988 0.1774 -0.0076 -0.0315 -0.0077 356 CYS B C   
7041 O O   . CYS B 356 ? 0.2317 0.1819 0.1638 -0.0151 -0.0343 -0.0027 356 CYS B O   
7042 C CB  . CYS B 356 ? 0.2241 0.1567 0.1594 0.0082  -0.0284 -0.0095 356 CYS B CB  
7043 S SG  . CYS B 356 ? 0.2430 0.1794 0.1822 0.0127  -0.0274 -0.0173 356 CYS B SG  
7044 N N   . TRP B 357 ? 0.2053 0.1834 0.1512 -0.0072 -0.0308 -0.0136 357 TRP B N   
7045 C CA  . TRP B 357 ? 0.2314 0.2162 0.1770 -0.0140 -0.0332 -0.0151 357 TRP B CA  
7046 C C   . TRP B 357 ? 0.2320 0.2308 0.1767 -0.0253 -0.0349 -0.0100 357 TRP B C   
7047 O O   . TRP B 357 ? 0.2448 0.2426 0.1859 -0.0338 -0.0377 -0.0083 357 TRP B O   
7048 C CB  . TRP B 357 ? 0.1808 0.1822 0.1351 -0.0091 -0.0325 -0.0227 357 TRP B CB  
7049 C CG  . TRP B 357 ? 0.1873 0.1761 0.1425 0.0011  -0.0310 -0.0263 357 TRP B CG  
7050 C CD1 . TRP B 357 ? 0.2076 0.2032 0.1698 0.0085  -0.0290 -0.0302 357 TRP B CD1 
7051 C CD2 . TRP B 357 ? 0.2293 0.1966 0.1775 0.0040  -0.0315 -0.0260 357 TRP B CD2 
7052 N NE1 . TRP B 357 ? 0.1691 0.1489 0.1292 0.0149  -0.0283 -0.0312 357 TRP B NE1 
7053 C CE2 . TRP B 357 ? 0.1818 0.1452 0.1332 0.0127  -0.0295 -0.0288 357 TRP B CE2 
7054 C CE3 . TRP B 357 ? 0.2183 0.1694 0.1574 -0.0003 -0.0337 -0.0238 357 TRP B CE3 
7055 C CZ2 . TRP B 357 ? 0.1828 0.1291 0.1286 0.0172  -0.0291 -0.0290 357 TRP B CZ2 
7056 C CZ3 . TRP B 357 ? 0.2156 0.1488 0.1488 0.0050  -0.0333 -0.0252 357 TRP B CZ3 
7057 C CH2 . TRP B 357 ? 0.1857 0.1179 0.1223 0.0136  -0.0308 -0.0276 357 TRP B CH2 
7058 N N   . GLU B 358 ? 0.2177 0.2309 0.1655 -0.0265 -0.0333 -0.0072 358 GLU B N   
7059 C CA  . GLU B 358 ? 0.2239 0.2538 0.1708 -0.0380 -0.0346 -0.0014 358 GLU B CA  
7060 C C   . GLU B 358 ? 0.2666 0.2755 0.2033 -0.0469 -0.0381 0.0079  358 GLU B C   
7061 O O   . GLU B 358 ? 0.2565 0.2761 0.1911 -0.0590 -0.0403 0.0137  358 GLU B O   
7062 C CB  . GLU B 358 ? 0.2152 0.2642 0.1663 -0.0370 -0.0323 0.0000  358 GLU B CB  
7063 C CG  . GLU B 358 ? 0.2783 0.3102 0.2253 -0.0323 -0.0319 0.0052  358 GLU B CG  
7064 C CD  . GLU B 358 ? 0.2712 0.3226 0.2244 -0.0274 -0.0290 0.0024  358 GLU B CD  
7065 O OE1 . GLU B 358 ? 0.3069 0.3670 0.2579 -0.0321 -0.0294 0.0092  358 GLU B OE1 
7066 O OE2 . GLU B 358 ? 0.2742 0.3317 0.2343 -0.0190 -0.0269 -0.0065 358 GLU B OE2 
7067 N N   . TYR B 359 ? 0.2714 0.2509 0.2017 -0.0413 -0.0390 0.0093  359 TYR B N   
7068 C CA  . TYR B 359 ? 0.2819 0.2370 0.2021 -0.0484 -0.0431 0.0167  359 TYR B CA  
7069 C C   . TYR B 359 ? 0.3298 0.2697 0.2450 -0.0516 -0.0459 0.0132  359 TYR B C   
7070 O O   . TYR B 359 ? 0.3491 0.2674 0.2554 -0.0585 -0.0500 0.0181  359 TYR B O   
7071 C CB  . TYR B 359 ? 0.3192 0.2516 0.2350 -0.0399 -0.0430 0.0201  359 TYR B CB  
7072 C CG  . TYR B 359 ? 0.3400 0.2878 0.2603 -0.0370 -0.0409 0.0240  359 TYR B CG  
7073 C CD1 . TYR B 359 ? 0.4318 0.3854 0.3491 -0.0461 -0.0432 0.0339  359 TYR B CD1 
7074 C CD2 . TYR B 359 ? 0.3513 0.3089 0.2786 -0.0262 -0.0368 0.0181  359 TYR B CD2 
7075 C CE1 . TYR B 359 ? 0.3751 0.3449 0.2961 -0.0437 -0.0414 0.0374  359 TYR B CE1 
7076 C CE2 . TYR B 359 ? 0.3958 0.3689 0.3271 -0.0241 -0.0351 0.0209  359 TYR B CE2 
7077 C CZ  . TYR B 359 ? 0.4040 0.3835 0.3320 -0.0325 -0.0374 0.0304  359 TYR B CZ  
7078 O OH  . TYR B 359 ? 0.4951 0.4914 0.4266 -0.0304 -0.0359 0.0330  359 TYR B OH  
7079 N N   . TYR B 360 ? 0.2755 0.2253 0.1958 -0.0471 -0.0443 0.0049  360 TYR B N   
7080 C CA  . TYR B 360 ? 0.3006 0.2406 0.2165 -0.0507 -0.0470 0.0013  360 TYR B CA  
7081 C C   . TYR B 360 ? 0.3455 0.3071 0.2641 -0.0635 -0.0493 0.0027  360 TYR B C   
7082 O O   . TYR B 360 ? 0.3140 0.3043 0.2409 -0.0653 -0.0473 0.0026  360 TYR B O   
7083 C CB  . TYR B 360 ? 0.2750 0.2168 0.1951 -0.0398 -0.0447 -0.0073 360 TYR B CB  
7084 C CG  . TYR B 360 ? 0.2515 0.1712 0.1674 -0.0284 -0.0429 -0.0100 360 TYR B CG  
7085 C CD1 . TYR B 360 ? 0.2606 0.1791 0.1794 -0.0202 -0.0397 -0.0087 360 TYR B CD1 
7086 C CD2 . TYR B 360 ? 0.2869 0.1907 0.1967 -0.0258 -0.0442 -0.0143 360 TYR B CD2 
7087 C CE1 . TYR B 360 ? 0.2489 0.1515 0.1649 -0.0101 -0.0377 -0.0112 360 TYR B CE1 
7088 C CE2 . TYR B 360 ? 0.2558 0.1438 0.1623 -0.0153 -0.0421 -0.0172 360 TYR B CE2 
7089 C CZ  . TYR B 360 ? 0.2381 0.1257 0.1478 -0.0077 -0.0388 -0.0155 360 TYR B CZ  
7090 O OH  . TYR B 360 ? 0.2633 0.1383 0.1703 0.0022  -0.0364 -0.0180 360 TYR B OH  
7091 N N   . GLU B 361 ? 0.3422 0.2873 0.3119 -0.1032 -0.0681 0.0242  361 GLU B N   
7092 C CA  . GLU B 361 ? 0.3799 0.3512 0.3559 -0.1171 -0.0703 0.0277  361 GLU B CA  
7093 C C   . GLU B 361 ? 0.3408 0.3444 0.3288 -0.1079 -0.0639 0.0208  361 GLU B C   
7094 O O   . GLU B 361 ? 0.3229 0.3187 0.3106 -0.0943 -0.0613 0.0124  361 GLU B O   
7095 C CB  . GLU B 361 ? 0.4829 0.4337 0.4509 -0.1276 -0.0793 0.0271  361 GLU B CB  
7096 C CG  . GLU B 361 ? 0.6740 0.5884 0.6294 -0.1363 -0.0873 0.0330  361 GLU B CG  
7097 C CD  . GLU B 361 ? 0.8012 0.7260 0.7578 -0.1489 -0.0881 0.0459  361 GLU B CD  
7098 O OE1 . GLU B 361 ? 0.8803 0.7803 0.8291 -0.1466 -0.0903 0.0506  361 GLU B OE1 
7099 O OE2 . GLU B 361 ? 0.8217 0.7814 0.7866 -0.1588 -0.0858 0.0512  361 GLU B OE2 
7100 N N   . GLU B 362 ? 0.2947 0.3351 0.2928 -0.1153 -0.0617 0.0246  362 GLU B N   
7101 C CA  . GLU B 362 ? 0.2710 0.3440 0.2813 -0.1062 -0.0566 0.0179  362 GLU B CA  
7102 C C   . GLU B 362 ? 0.2792 0.3463 0.2914 -0.0872 -0.0504 0.0102  362 GLU B C   
7103 O O   . GLU B 362 ? 0.2303 0.3036 0.2472 -0.0766 -0.0488 0.0030  362 GLU B O   
7104 C CB  . GLU B 362 ? 0.3038 0.3816 0.3158 -0.1091 -0.0612 0.0140  362 GLU B CB  
7105 C CG  . GLU B 362 ? 0.3906 0.4953 0.4078 -0.1269 -0.0652 0.0204  362 GLU B CG  
7106 C CD  . GLU B 362 ? 0.6051 0.7102 0.6221 -0.1317 -0.0713 0.0173  362 GLU B CD  
7107 O OE1 . GLU B 362 ? 0.7020 0.7933 0.7115 -0.1441 -0.0760 0.0225  362 GLU B OE1 
7108 O OE2 . GLU B 362 ? 0.6539 0.7695 0.6766 -0.1191 -0.0695 0.0097  362 GLU B OE2 
7109 N N   . ASN B 363 ? 0.2048 0.2603 0.2134 -0.0833 -0.0474 0.0125  363 ASN B N   
7110 C CA  . ASN B 363 ? 0.2343 0.2874 0.2454 -0.0676 -0.0416 0.0062  363 ASN B CA  
7111 C C   . ASN B 363 ? 0.2334 0.2628 0.2398 -0.0570 -0.0421 -0.0004 363 ASN B C   
7112 O O   . ASN B 363 ? 0.2108 0.2444 0.2216 -0.0451 -0.0383 -0.0064 363 ASN B O   
7113 C CB  . ASN B 363 ? 0.2207 0.3087 0.2439 -0.0615 -0.0367 0.0019  363 ASN B CB  
7114 C CG  . ASN B 363 ? 0.2496 0.3349 0.2748 -0.0483 -0.0314 -0.0033 363 ASN B CG  
7115 O OD1 . ASN B 363 ? 0.1914 0.2631 0.2113 -0.0478 -0.0302 -0.0003 363 ASN B OD1 
7116 N ND2 . ASN B 363 ? 0.2207 0.3177 0.2532 -0.0375 -0.0291 -0.0110 363 ASN B ND2 
7117 N N   . GLY B 364 ? 0.2335 0.2376 0.2303 -0.0615 -0.0473 0.0005  364 GLY B N   
7118 C CA  . GLY B 364 ? 0.2274 0.2113 0.2184 -0.0517 -0.0473 -0.0057 364 GLY B CA  
7119 C C   . GLY B 364 ? 0.2143 0.2095 0.2093 -0.0484 -0.0483 -0.0105 364 GLY B C   
7120 O O   . GLY B 364 ? 0.2323 0.2134 0.2221 -0.0406 -0.0482 -0.0150 364 GLY B O   
7121 N N   . ILE B 365 ? 0.1793 0.2007 0.1828 -0.0539 -0.0494 -0.0094 365 ILE B N   
7122 C CA  . ILE B 365 ? 0.1881 0.2227 0.1968 -0.0488 -0.0506 -0.0137 365 ILE B CA  
7123 C C   . ILE B 365 ? 0.2653 0.2841 0.2651 -0.0537 -0.0566 -0.0148 365 ILE B C   
7124 O O   . ILE B 365 ? 0.2520 0.2637 0.2488 -0.0455 -0.0569 -0.0189 365 ILE B O   
7125 C CB  . ILE B 365 ? 0.2244 0.2948 0.2458 -0.0520 -0.0502 -0.0129 365 ILE B CB  
7126 C CG1 . ILE B 365 ? 0.2175 0.3015 0.2463 -0.0438 -0.0440 -0.0144 365 ILE B CG1 
7127 C CG2 . ILE B 365 ? 0.2594 0.3431 0.2861 -0.0463 -0.0528 -0.0170 365 ILE B CG2 
7128 C CD1 . ILE B 365 ? 0.2486 0.3691 0.2887 -0.0474 -0.0427 -0.0138 365 ILE B CD1 
7129 N N   . PRO B 366 ? 0.2886 0.3003 0.2829 -0.0673 -0.0619 -0.0112 366 PRO B N   
7130 C CA  . PRO B 366 ? 0.2765 0.2692 0.2604 -0.0711 -0.0680 -0.0140 366 PRO B CA  
7131 C C   . PRO B 366 ? 0.2180 0.1823 0.1909 -0.0609 -0.0665 -0.0187 366 PRO B C   
7132 O O   . PRO B 366 ? 0.2921 0.2500 0.2591 -0.0568 -0.0686 -0.0232 366 PRO B O   
7133 C CB  . PRO B 366 ? 0.3272 0.3118 0.3064 -0.0878 -0.0740 -0.0088 366 PRO B CB  
7134 C CG  . PRO B 366 ? 0.3145 0.3279 0.3052 -0.0947 -0.0714 -0.0027 366 PRO B CG  
7135 C CD  . PRO B 366 ? 0.2737 0.2955 0.2708 -0.0808 -0.0633 -0.0044 366 PRO B CD  
7136 N N   . PHE B 367 ? 0.2175 0.1674 0.1875 -0.0563 -0.0627 -0.0176 367 PHE B N   
7137 C CA  . PHE B 367 ? 0.2222 0.1493 0.1827 -0.0461 -0.0607 -0.0222 367 PHE B CA  
7138 C C   . PHE B 367 ? 0.2395 0.1758 0.2034 -0.0343 -0.0559 -0.0256 367 PHE B C   
7139 O O   . PHE B 367 ? 0.2404 0.1673 0.1963 -0.0297 -0.0570 -0.0297 367 PHE B O   
7140 C CB  . PHE B 367 ? 0.2247 0.1381 0.1830 -0.0434 -0.0580 -0.0199 367 PHE B CB  
7141 C CG  . PHE B 367 ? 0.2985 0.1952 0.2497 -0.0314 -0.0548 -0.0248 367 PHE B CG  
7142 C CD1 . PHE B 367 ? 0.3519 0.2255 0.2905 -0.0300 -0.0589 -0.0298 367 PHE B CD1 
7143 C CD2 . PHE B 367 ? 0.2364 0.1420 0.1934 -0.0219 -0.0480 -0.0250 367 PHE B CD2 
7144 C CE1 . PHE B 367 ? 0.2709 0.1334 0.2031 -0.0184 -0.0555 -0.0348 367 PHE B CE1 
7145 C CE2 . PHE B 367 ? 0.2369 0.1312 0.1881 -0.0118 -0.0447 -0.0289 367 PHE B CE2 
7146 C CZ  . PHE B 367 ? 0.2815 0.1559 0.2205 -0.0097 -0.0481 -0.0338 367 PHE B CZ  
7147 N N   . LEU B 368 ? 0.2088 0.1630 0.1836 -0.0296 -0.0511 -0.0237 368 LEU B N   
7148 C CA  . LEU B 368 ? 0.2063 0.1652 0.1835 -0.0192 -0.0477 -0.0261 368 LEU B CA  
7149 C C   . LEU B 368 ? 0.1994 0.1678 0.1772 -0.0193 -0.0516 -0.0274 368 LEU B C   
7150 O O   . LEU B 368 ? 0.2074 0.1704 0.1804 -0.0130 -0.0512 -0.0291 368 LEU B O   
7151 C CB  . LEU B 368 ? 0.1653 0.1386 0.1535 -0.0142 -0.0428 -0.0249 368 LEU B CB  
7152 C CG  . LEU B 368 ? 0.1638 0.1270 0.1502 -0.0120 -0.0387 -0.0240 368 LEU B CG  
7153 C CD1 . LEU B 368 ? 0.1875 0.1661 0.1842 -0.0084 -0.0346 -0.0234 368 LEU B CD1 
7154 C CD2 . LEU B 368 ? 0.1989 0.1449 0.1766 -0.0052 -0.0366 -0.0263 368 LEU B CD2 
7155 N N   . GLU B 369 ? 0.1861 0.1713 0.1703 -0.0263 -0.0554 -0.0260 369 GLU B N   
7156 C CA  . GLU B 369 ? 0.2232 0.2188 0.2082 -0.0260 -0.0599 -0.0271 369 GLU B CA  
7157 C C   . GLU B 369 ? 0.2365 0.2146 0.2077 -0.0285 -0.0639 -0.0296 369 GLU B C   
7158 O O   . GLU B 369 ? 0.2410 0.2192 0.2082 -0.0232 -0.0654 -0.0309 369 GLU B O   
7159 C CB  . GLU B 369 ? 0.1893 0.2089 0.1840 -0.0341 -0.0635 -0.0253 369 GLU B CB  
7160 C CG  . GLU B 369 ? 0.1832 0.2259 0.1921 -0.0281 -0.0599 -0.0248 369 GLU B CG  
7161 C CD  . GLU B 369 ? 0.2934 0.3661 0.3132 -0.0346 -0.0630 -0.0237 369 GLU B CD  
7162 O OE1 . GLU B 369 ? 0.3583 0.4333 0.3748 -0.0463 -0.0680 -0.0220 369 GLU B OE1 
7163 O OE2 . GLU B 369 ? 0.2701 0.3648 0.3016 -0.0277 -0.0608 -0.0250 369 GLU B OE2 
7164 N N   . LYS B 370 ? 0.2346 0.1969 0.1976 -0.0362 -0.0662 -0.0305 370 LYS B N   
7165 C CA  . LYS B 370 ? 0.2812 0.2258 0.2301 -0.0375 -0.0702 -0.0347 370 LYS B CA  
7166 C C   . LYS B 370 ? 0.2437 0.1742 0.1843 -0.0268 -0.0655 -0.0377 370 LYS B C   
7167 O O   . LYS B 370 ? 0.2720 0.1984 0.2032 -0.0238 -0.0673 -0.0409 370 LYS B O   
7168 C CB  . LYS B 370 ? 0.2733 0.2019 0.2154 -0.0482 -0.0750 -0.0355 370 LYS B CB  
7169 C CG  . LYS B 370 ? 0.4427 0.3859 0.3899 -0.0615 -0.0815 -0.0329 370 LYS B CG  
7170 C CD  . LYS B 370 ? 0.5944 0.5267 0.5402 -0.0739 -0.0850 -0.0296 370 LYS B CD  
7171 C CE  . LYS B 370 ? 0.6329 0.5886 0.5880 -0.0880 -0.0896 -0.0247 370 LYS B CE  
7172 N NZ  . LYS B 370 ? 0.5975 0.5650 0.5516 -0.0917 -0.0954 -0.0277 370 LYS B NZ  
7173 N N   . LEU B 371 ? 0.2306 0.1562 0.1743 -0.0214 -0.0596 -0.0364 371 LEU B N   
7174 C CA  . LEU B 371 ? 0.2215 0.1376 0.1586 -0.0120 -0.0547 -0.0387 371 LEU B CA  
7175 C C   . LEU B 371 ? 0.2419 0.1696 0.1812 -0.0061 -0.0530 -0.0370 371 LEU B C   
7176 O O   . LEU B 371 ? 0.2367 0.1600 0.1662 -0.0024 -0.0528 -0.0391 371 LEU B O   
7177 C CB  . LEU B 371 ? 0.2134 0.1256 0.1553 -0.0081 -0.0492 -0.0370 371 LEU B CB  
7178 C CG  . LEU B 371 ? 0.2730 0.1802 0.2106 0.0011  -0.0436 -0.0386 371 LEU B CG  
7179 C CD1 . LEU B 371 ? 0.3003 0.1923 0.2238 0.0036  -0.0451 -0.0446 371 LEU B CD1 
7180 C CD2 . LEU B 371 ? 0.2906 0.1984 0.2353 0.0044  -0.0386 -0.0363 371 LEU B CD2 
7181 N N   . TYR B 372 ? 0.2130 0.1554 0.1645 -0.0052 -0.0521 -0.0332 372 TYR B N   
7182 C CA  . TYR B 372 ? 0.1947 0.1444 0.1485 0.0009  -0.0513 -0.0308 372 TYR B CA  
7183 C C   . TYR B 372 ? 0.2494 0.2042 0.1979 -0.0006 -0.0572 -0.0309 372 TYR B C   
7184 O O   . TYR B 372 ? 0.2214 0.1755 0.1642 0.0036  -0.0573 -0.0292 372 TYR B O   
7185 C CB  . TYR B 372 ? 0.2009 0.1633 0.1690 0.0034  -0.0500 -0.0282 372 TYR B CB  
7186 C CG  . TYR B 372 ? 0.1825 0.1413 0.1553 0.0059  -0.0441 -0.0280 372 TYR B CG  
7187 C CD1 . TYR B 372 ? 0.2017 0.1480 0.1671 0.0078  -0.0401 -0.0288 372 TYR B CD1 
7188 C CD2 . TYR B 372 ? 0.1845 0.1549 0.1694 0.0069  -0.0429 -0.0274 372 TYR B CD2 
7189 C CE1 . TYR B 372 ? 0.2131 0.1582 0.1835 0.0100  -0.0353 -0.0284 372 TYR B CE1 
7190 C CE2 . TYR B 372 ? 0.1811 0.1497 0.1699 0.0089  -0.0380 -0.0274 372 TYR B CE2 
7191 C CZ  . TYR B 372 ? 0.1652 0.1211 0.1471 0.0102  -0.0344 -0.0275 372 TYR B CZ  
7192 O OH  . TYR B 372 ? 0.1745 0.1305 0.1608 0.0121  -0.0302 -0.0273 372 TYR B OH  
7193 N N   . SER B 373 ? 0.2288 0.1904 0.1793 -0.0075 -0.0624 -0.0321 373 SER B N   
7194 C CA  . SER B 373 ? 0.2548 0.2221 0.1996 -0.0099 -0.0687 -0.0327 373 SER B CA  
7195 C C   . SER B 373 ? 0.2653 0.2185 0.1934 -0.0098 -0.0691 -0.0364 373 SER B C   
7196 O O   . SER B 373 ? 0.3042 0.2607 0.2251 -0.0076 -0.0718 -0.0357 373 SER B O   
7197 C CB  . SER B 373 ? 0.2709 0.2481 0.2205 -0.0194 -0.0743 -0.0336 373 SER B CB  
7198 O OG  . SER B 373 ? 0.3941 0.3787 0.3387 -0.0220 -0.0809 -0.0344 373 SER B OG  
7199 N N   . THR B 374 ? 0.2386 0.1766 0.1599 -0.0116 -0.0670 -0.0406 374 THR B N   
7200 C CA  . THR B 374 ? 0.3036 0.2292 0.2088 -0.0100 -0.0673 -0.0461 374 THR B CA  
7201 C C   . THR B 374 ? 0.3158 0.2423 0.2168 -0.0017 -0.0615 -0.0442 374 THR B C   
7202 O O   . THR B 374 ? 0.3081 0.2366 0.1980 0.0002  -0.0626 -0.0454 374 THR B O   
7203 C CB  . THR B 374 ? 0.3308 0.2387 0.2307 -0.0126 -0.0674 -0.0516 374 THR B CB  
7204 O OG1 . THR B 374 ? 0.3520 0.2592 0.2554 -0.0227 -0.0737 -0.0517 374 THR B OG1 
7205 C CG2 . THR B 374 ? 0.3465 0.2415 0.2293 -0.0093 -0.0683 -0.0596 374 THR B CG2 
7206 N N   . LEU B 375 ? 0.2925 0.2195 0.2023 0.0024  -0.0555 -0.0406 375 LEU B N   
7207 C CA  . LEU B 375 ? 0.2670 0.1955 0.1736 0.0085  -0.0500 -0.0380 375 LEU B CA  
7208 C C   . LEU B 375 ? 0.3013 0.2396 0.2074 0.0096  -0.0523 -0.0320 375 LEU B C   
7209 O O   . LEU B 375 ? 0.3212 0.2611 0.2175 0.0118  -0.0505 -0.0306 375 LEU B O   
7210 C CB  . LEU B 375 ? 0.2836 0.2115 0.2008 0.0114  -0.0442 -0.0352 375 LEU B CB  
7211 C CG  . LEU B 375 ? 0.3057 0.2234 0.2213 0.0124  -0.0411 -0.0400 375 LEU B CG  
7212 C CD1 . LEU B 375 ? 0.2722 0.1921 0.1993 0.0145  -0.0363 -0.0366 375 LEU B CD1 
7213 C CD2 . LEU B 375 ? 0.3507 0.2635 0.2534 0.0169  -0.0384 -0.0449 375 LEU B CD2 
7214 N N   . GLU B 376 ? 0.2695 0.2155 0.1857 0.0082  -0.0567 -0.0284 376 GLU B N   
7215 C CA  . GLU B 376 ? 0.2938 0.2471 0.2107 0.0106  -0.0599 -0.0219 376 GLU B CA  
7216 C C   . GLU B 376 ? 0.2959 0.2522 0.1993 0.0088  -0.0645 -0.0225 376 GLU B C   
7217 O O   . GLU B 376 ? 0.3243 0.2849 0.2241 0.0108  -0.0668 -0.0162 376 GLU B O   
7218 C CB  . GLU B 376 ? 0.3004 0.2625 0.2319 0.0116  -0.0640 -0.0192 376 GLU B CB  
7219 C CG  . GLU B 376 ? 0.3649 0.3364 0.2989 0.0073  -0.0703 -0.0219 376 GLU B CG  
7220 C CD  . GLU B 376 ? 0.4443 0.4288 0.3943 0.0096  -0.0734 -0.0201 376 GLU B CD  
7221 O OE1 . GLU B 376 ? 0.4326 0.4172 0.3906 0.0159  -0.0719 -0.0168 376 GLU B OE1 
7222 O OE2 . GLU B 376 ? 0.4593 0.4550 0.4140 0.0050  -0.0776 -0.0224 376 GLU B OE2 
7223 N N   . LYS B 377 ? 0.2652 0.2184 0.1602 0.0049  -0.0665 -0.0297 377 LYS B N   
7224 C CA  . LYS B 377 ? 0.2784 0.2354 0.1600 0.0028  -0.0716 -0.0316 377 LYS B CA  
7225 C C   . LYS B 377 ? 0.3291 0.2796 0.1943 0.0039  -0.0681 -0.0378 377 LYS B C   
7226 O O   . LYS B 377 ? 0.3662 0.3208 0.2180 0.0027  -0.0717 -0.0401 377 LYS B O   
7227 C CB  . LYS B 377 ? 0.3073 0.2679 0.1913 -0.0034 -0.0789 -0.0358 377 LYS B CB  
7228 C CG  . LYS B 377 ? 0.3418 0.3141 0.2423 -0.0038 -0.0825 -0.0307 377 LYS B CG  
7229 C CD  . LYS B 377 ? 0.4112 0.3919 0.3136 -0.0111 -0.0900 -0.0340 377 LYS B CD  
7230 C CE  . LYS B 377 ? 0.4295 0.4247 0.3501 -0.0112 -0.0921 -0.0304 377 LYS B CE  
7231 N NZ  . LYS B 377 ? 0.3980 0.3874 0.3285 -0.0108 -0.0857 -0.0309 377 LYS B NZ  
7232 N N   . GLU B 378 ? 0.3599 0.3024 0.2255 0.0069  -0.0612 -0.0408 378 GLU B N   
7233 C CA  . GLU B 378 ? 0.4125 0.3512 0.2637 0.0100  -0.0574 -0.0478 378 GLU B CA  
7234 C C   . GLU B 378 ? 0.4010 0.3502 0.2453 0.0129  -0.0533 -0.0415 378 GLU B C   
7235 O O   . GLU B 378 ? 0.4618 0.4137 0.3146 0.0144  -0.0488 -0.0339 378 GLU B O   
7236 C CB  . GLU B 378 ? 0.5157 0.4435 0.3713 0.0129  -0.0523 -0.0529 378 GLU B CB  
7237 C CG  . GLU B 378 ? 0.6424 0.5617 0.4843 0.0162  -0.0518 -0.0643 378 GLU B CG  
7238 C CD  . GLU B 378 ? 0.7369 0.6473 0.5714 0.0112  -0.0601 -0.0718 378 GLU B CD  
7239 O OE1 . GLU B 378 ? 0.7888 0.7038 0.6096 0.0108  -0.0633 -0.0762 378 GLU B OE1 
7240 O OE2 . GLU B 378 ? 0.7669 0.6666 0.6089 0.0068  -0.0637 -0.0730 378 GLU B OE2 
7241 N N   . GLU B 379 ? 0.3543 0.3101 0.1827 0.0128  -0.0551 -0.0443 379 GLU B N   
7242 C CA  . GLU B 379 ? 0.4210 0.3893 0.2428 0.0133  -0.0525 -0.0356 379 GLU B CA  
7243 C C   . GLU B 379 ? 0.4220 0.3954 0.2386 0.0171  -0.0437 -0.0370 379 GLU B C   
7244 O O   . GLU B 379 ? 0.5229 0.5074 0.3360 0.0160  -0.0407 -0.0279 379 GLU B O   
7245 C CB  . GLU B 379 ? 0.4383 0.4152 0.2451 0.0109  -0.0585 -0.0362 379 GLU B CB  
7246 C CG  . GLU B 379 ? 0.5043 0.4786 0.3179 0.0071  -0.0676 -0.0353 379 GLU B CG  
7247 C CD  . GLU B 379 ? 0.5344 0.5195 0.3364 0.0044  -0.0748 -0.0324 379 GLU B CD  
7248 O OE1 . GLU B 379 ? 0.4842 0.4710 0.2939 0.0019  -0.0822 -0.0292 379 GLU B OE1 
7249 O OE2 . GLU B 379 ? 0.5032 0.4970 0.2886 0.0050  -0.0733 -0.0335 379 GLU B OE2 
7250 N N   . TRP B 380 ? 0.3481 0.3146 0.1648 0.0214  -0.0398 -0.0474 380 TRP B N   
7251 C CA  . TRP B 380 ? 0.3563 0.3306 0.1697 0.0262  -0.0314 -0.0495 380 TRP B CA  
7252 C C   . TRP B 380 ? 0.3837 0.3531 0.2132 0.0275  -0.0267 -0.0456 380 TRP B C   
7253 O O   . TRP B 380 ? 0.3508 0.3281 0.1804 0.0313  -0.0197 -0.0466 380 TRP B O   
7254 C CB  . TRP B 380 ? 0.3578 0.3292 0.1587 0.0324  -0.0306 -0.0650 380 TRP B CB  
7255 C CG  . TRP B 380 ? 0.3470 0.2978 0.1525 0.0330  -0.0357 -0.0739 380 TRP B CG  
7256 C CD1 . TRP B 380 ? 0.4351 0.3759 0.2367 0.0285  -0.0441 -0.0781 380 TRP B CD1 
7257 C CD2 . TRP B 380 ? 0.3422 0.2803 0.1566 0.0373  -0.0334 -0.0786 380 TRP B CD2 
7258 N NE1 . TRP B 380 ? 0.4546 0.3767 0.2619 0.0287  -0.0472 -0.0847 380 TRP B NE1 
7259 C CE2 . TRP B 380 ? 0.3946 0.3139 0.2095 0.0344  -0.0408 -0.0848 380 TRP B CE2 
7260 C CE3 . TRP B 380 ? 0.3580 0.2994 0.1798 0.0428  -0.0262 -0.0777 380 TRP B CE3 
7261 C CZ2 . TRP B 380 ? 0.4187 0.3212 0.2406 0.0366  -0.0415 -0.0892 380 TRP B CZ2 
7262 C CZ3 . TRP B 380 ? 0.4067 0.3322 0.2359 0.0462  -0.0269 -0.0826 380 TRP B CZ3 
7263 C CH2 . TRP B 380 ? 0.4158 0.3213 0.2445 0.0431  -0.0345 -0.0879 380 TRP B CH2 
7264 N N   . ILE B 381 ? 0.2990 0.2579 0.1420 0.0244  -0.0304 -0.0414 381 ILE B N   
7265 C CA  . ILE B 381 ? 0.3363 0.2912 0.1944 0.0250  -0.0268 -0.0375 381 ILE B CA  
7266 C C   . ILE B 381 ? 0.3496 0.3081 0.2159 0.0208  -0.0281 -0.0252 381 ILE B C   
7267 O O   . ILE B 381 ? 0.3227 0.2796 0.1900 0.0180  -0.0344 -0.0214 381 ILE B O   
7268 C CB  . ILE B 381 ? 0.3110 0.2519 0.1781 0.0251  -0.0298 -0.0428 381 ILE B CB  
7269 C CG1 . ILE B 381 ? 0.3329 0.2654 0.1914 0.0295  -0.0298 -0.0548 381 ILE B CG1 
7270 C CG2 . ILE B 381 ? 0.3375 0.2765 0.2199 0.0253  -0.0264 -0.0381 381 ILE B CG2 
7271 C CD1 . ILE B 381 ? 0.3631 0.2802 0.2280 0.0274  -0.0345 -0.0587 381 ILE B CD1 
7272 N N   . GLU B 382 ? 0.2974 0.2604 0.1702 0.0207  -0.0230 -0.0194 382 GLU B N   
7273 C CA  . GLU B 382 ? 0.2667 0.2281 0.1491 0.0172  -0.0250 -0.0090 382 GLU B CA  
7274 C C   . GLU B 382 ? 0.2440 0.2004 0.1406 0.0183  -0.0219 -0.0098 382 GLU B C   
7275 O O   . GLU B 382 ? 0.2492 0.2108 0.1469 0.0195  -0.0159 -0.0109 382 GLU B O   
7276 C CB  . GLU B 382 ? 0.3068 0.2778 0.1825 0.0135  -0.0230 0.0007  382 GLU B CB  
7277 C CG  . GLU B 382 ? 0.5045 0.4695 0.3888 0.0097  -0.0267 0.0117  382 GLU B CG  
7278 C CD  . GLU B 382 ? 0.7691 0.7415 0.6451 0.0041  -0.0263 0.0232  382 GLU B CD  
7279 O OE1 . GLU B 382 ? 0.8785 0.8636 0.7412 0.0030  -0.0236 0.0230  382 GLU B OE1 
7280 O OE2 . GLU B 382 ? 0.8571 0.8225 0.7394 0.0005  -0.0293 0.0326  382 GLU B OE2 
7281 N N   . THR B 383 ? 0.2308 0.1795 0.1381 0.0182  -0.0260 -0.0093 383 THR B N   
7282 C CA  . THR B 383 ? 0.2454 0.1911 0.1657 0.0187  -0.0235 -0.0090 383 THR B CA  
7283 C C   . THR B 383 ? 0.2113 0.1575 0.1356 0.0159  -0.0234 -0.0003 383 THR B C   
7284 O O   . THR B 383 ? 0.2348 0.1795 0.1556 0.0139  -0.0279 0.0065  383 THR B O   
7285 C CB  . THR B 383 ? 0.2796 0.2199 0.2099 0.0196  -0.0274 -0.0122 383 THR B CB  
7286 O OG1 . THR B 383 ? 0.2314 0.1712 0.1635 0.0190  -0.0338 -0.0082 383 THR B OG1 
7287 C CG2 . THR B 383 ? 0.3010 0.2390 0.2273 0.0203  -0.0280 -0.0197 383 THR B CG2 
7288 N N   . LEU B 384 ? 0.2090 0.1565 0.1402 0.0154  -0.0189 0.0000  384 LEU B N   
7289 C CA  . LEU B 384 ? 0.2187 0.1660 0.1531 0.0112  -0.0188 0.0080  384 LEU B CA  
7290 C C   . LEU B 384 ? 0.1973 0.1385 0.1447 0.0117  -0.0196 0.0067  384 LEU B C   
7291 O O   . LEU B 384 ? 0.1896 0.1319 0.1432 0.0147  -0.0172 0.0001  384 LEU B O   
7292 C CB  . LEU B 384 ? 0.2281 0.1872 0.1575 0.0083  -0.0123 0.0103  384 LEU B CB  
7293 C CG  . LEU B 384 ? 0.2611 0.2306 0.1766 0.0082  -0.0100 0.0106  384 LEU B CG  
7294 C CD1 . LEU B 384 ? 0.2655 0.2507 0.1786 0.0055  -0.0031 0.0129  384 LEU B CD1 
7295 C CD2 . LEU B 384 ? 0.2340 0.2003 0.1417 0.0045  -0.0156 0.0187  384 LEU B CD2 
7296 N N   . THR B 385 ? 0.2031 0.1374 0.1540 0.0086  -0.0234 0.0132  385 THR B N   
7297 C CA  . THR B 385 ? 0.1972 0.1271 0.1587 0.0079  -0.0234 0.0120  385 THR B CA  
7298 C C   . THR B 385 ? 0.2212 0.1600 0.1829 0.0035  -0.0173 0.0135  385 THR B C   
7299 O O   . THR B 385 ? 0.2328 0.1811 0.1865 0.0004  -0.0137 0.0172  385 THR B O   
7300 C CB  . THR B 385 ? 0.2080 0.1248 0.1724 0.0062  -0.0306 0.0177  385 THR B CB  
7301 O OG1 . THR B 385 ? 0.2468 0.1627 0.2036 -0.0011 -0.0312 0.0277  385 THR B OG1 
7302 C CG2 . THR B 385 ? 0.2483 0.1585 0.2127 0.0117  -0.0375 0.0169  385 THR B CG2 
7303 N N   . LEU B 386 ? 0.2033 0.1413 0.1743 0.0031  -0.0163 0.0104  386 LEU B N   
7304 C CA  . LEU B 386 ? 0.2376 0.1860 0.2103 -0.0015 -0.0112 0.0122  386 LEU B CA  
7305 C C   . LEU B 386 ? 0.2886 0.2367 0.2564 -0.0103 -0.0126 0.0223  386 LEU B C   
7306 O O   . LEU B 386 ? 0.2892 0.2521 0.2531 -0.0146 -0.0075 0.0258  386 LEU B O   
7307 C CB  . LEU B 386 ? 0.2094 0.1565 0.1927 -0.0013 -0.0111 0.0077  386 LEU B CB  
7308 C CG  . LEU B 386 ? 0.2042 0.1533 0.1924 0.0059  -0.0097 -0.0009 386 LEU B CG  
7309 C CD1 . LEU B 386 ? 0.2065 0.1565 0.2040 0.0053  -0.0097 -0.0047 386 LEU B CD1 
7310 C CD2 . LEU B 386 ? 0.2321 0.1916 0.2159 0.0098  -0.0043 -0.0041 386 LEU B CD2 
7311 N N   . GLU B 387 ? 0.2317 0.1639 0.1997 -0.0130 -0.0199 0.0274  387 GLU B N   
7312 C CA  . GLU B 387 ? 0.2780 0.2067 0.2403 -0.0226 -0.0228 0.0388  387 GLU B CA  
7313 C C   . GLU B 387 ? 0.2592 0.1994 0.2096 -0.0245 -0.0200 0.0445  387 GLU B C   
7314 O O   . GLU B 387 ? 0.3041 0.2558 0.2494 -0.0330 -0.0171 0.0524  387 GLU B O   
7315 C CB  . GLU B 387 ? 0.3428 0.2485 0.3064 -0.0230 -0.0327 0.0427  387 GLU B CB  
7316 C CG  . GLU B 387 ? 0.4923 0.3898 0.4501 -0.0344 -0.0374 0.0560  387 GLU B CG  
7317 C CD  . GLU B 387 ? 0.7989 0.6700 0.7604 -0.0347 -0.0479 0.0581  387 GLU B CD  
7318 O OE1 . GLU B 387 ? 0.9363 0.7972 0.8962 -0.0454 -0.0523 0.0672  387 GLU B OE1 
7319 O OE2 . GLU B 387 ? 0.9077 0.7685 0.8738 -0.0241 -0.0521 0.0505  387 GLU B OE2 
7320 N N   . GLU B 388 ? 0.3066 0.2456 0.2522 -0.0171 -0.0210 0.0405  388 GLU B N   
7321 C CA  . GLU B 388 ? 0.2668 0.2174 0.2002 -0.0181 -0.0186 0.0442  388 GLU B CA  
7322 C C   . GLU B 388 ? 0.3045 0.2765 0.2355 -0.0173 -0.0094 0.0395  388 GLU B C   
7323 O O   . GLU B 388 ? 0.3382 0.3252 0.2602 -0.0219 -0.0059 0.0449  388 GLU B O   
7324 C CB  . GLU B 388 ? 0.2979 0.2425 0.2273 -0.0105 -0.0223 0.0396  388 GLU B CB  
7325 C CG  . GLU B 388 ? 0.3535 0.2817 0.2818 -0.0113 -0.0317 0.0467  388 GLU B CG  
7326 C CD  . GLU B 388 ? 0.4288 0.3526 0.3573 -0.0032 -0.0360 0.0408  388 GLU B CD  
7327 O OE1 . GLU B 388 ? 0.2937 0.2234 0.2252 0.0022  -0.0323 0.0308  388 GLU B OE1 
7328 O OE2 . GLU B 388 ? 0.4346 0.3490 0.3602 -0.0025 -0.0436 0.0468  388 GLU B OE2 
7329 N N   . ALA B 389 ? 0.2789 0.2537 0.2177 -0.0109 -0.0056 0.0295  389 ALA B N   
7330 C CA  . ALA B 389 ? 0.3031 0.2973 0.2403 -0.0083 0.0022  0.0245  389 ALA B CA  
7331 C C   . ALA B 389 ? 0.3427 0.3515 0.2829 -0.0165 0.0060  0.0310  389 ALA B C   
7332 O O   . ALA B 389 ? 0.3309 0.3610 0.2660 -0.0171 0.0121  0.0314  389 ALA B O   
7333 C CB  . ALA B 389 ? 0.2702 0.2619 0.2148 0.0003  0.0041  0.0137  389 ALA B CB  
7334 N N   . MET B 390 ? 0.3416 0.3404 0.2900 -0.0231 0.0023  0.0358  390 MET B N   
7335 C CA  . MET B 390 ? 0.4286 0.4402 0.3805 -0.0331 0.0048  0.0425  390 MET B CA  
7336 C C   . MET B 390 ? 0.4755 0.4965 0.4176 -0.0434 0.0048  0.0546  390 MET B C   
7337 O O   . MET B 390 ? 0.4695 0.5134 0.4113 -0.0502 0.0101  0.0590  390 MET B O   
7338 C CB  . MET B 390 ? 0.3920 0.3867 0.3537 -0.0382 -0.0008 0.0441  390 MET B CB  
7339 C CG  . MET B 390 ? 0.5569 0.5646 0.5243 -0.0488 0.0013  0.0492  390 MET B CG  
7340 S SD  . MET B 390 ? 0.7123 0.6962 0.6888 -0.0556 -0.0071 0.0505  390 MET B SD  
7341 C CE  . MET B 390 ? 0.7397 0.6966 0.7079 -0.0602 -0.0168 0.0601  390 MET B CE  
7342 N N   . ARG B 391 ? 0.4379 0.4440 0.3718 -0.0448 -0.0011 0.0605  391 ARG B N   
7343 C CA  . ARG B 391 ? 0.4405 0.4519 0.3643 -0.0559 -0.0029 0.0742  391 ARG B CA  
7344 C C   . ARG B 391 ? 0.4092 0.4364 0.3198 -0.0522 0.0008  0.0740  391 ARG B C   
7345 O O   . ARG B 391 ? 0.4312 0.4657 0.3316 -0.0613 -0.0003 0.0858  391 ARG B O   
7346 C CB  . ARG B 391 ? 0.5688 0.5512 0.4917 -0.0609 -0.0137 0.0830  391 ARG B CB  
7347 C CG  . ARG B 391 ? 0.7230 0.6901 0.6555 -0.0689 -0.0186 0.0867  391 ARG B CG  
7348 C CD  . ARG B 391 ? 0.9184 0.8645 0.8451 -0.0795 -0.0285 0.1013  391 ARG B CD  
7349 N NE  . ARG B 391 ? 0.9774 0.8919 0.9106 -0.0747 -0.0381 0.0981  391 ARG B NE  
7350 C CZ  . ARG B 391 ? 1.0162 0.9111 0.9455 -0.0681 -0.0459 0.0994  391 ARG B CZ  
7351 N NH1 . ARG B 391 ? 1.0265 0.9291 0.9449 -0.0662 -0.0455 0.1043  391 ARG B NH1 
7352 N NH2 . ARG B 391 ? 1.0167 0.8855 0.9529 -0.0626 -0.0544 0.0952  391 ARG B NH2 
7353 N N   . LYS B 392 ? 0.3894 0.4214 0.2992 -0.0396 0.0046  0.0611  392 LYS B N   
7354 C CA  . LYS B 392 ? 0.4293 0.4725 0.3258 -0.0349 0.0068  0.0587  392 LYS B CA  
7355 C C   . LYS B 392 ? 0.3892 0.4641 0.2782 -0.0401 0.0144  0.0626  392 LYS B C   
7356 O O   . LYS B 392 ? 0.3489 0.4425 0.2441 -0.0381 0.0212  0.0573  392 LYS B O   
7357 C CB  . LYS B 392 ? 0.4469 0.4864 0.3449 -0.0211 0.0086  0.0432  392 LYS B CB  
7358 C CG  . LYS B 392 ? 0.5036 0.5445 0.3886 -0.0158 0.0074  0.0391  392 LYS B CG  
7359 C CD  . LYS B 392 ? 0.6055 0.6309 0.4847 -0.0207 -0.0009 0.0488  392 LYS B CD  
7360 C CE  . LYS B 392 ? 0.6105 0.6184 0.4908 -0.0126 -0.0064 0.0407  392 LYS B CE  
7361 N NZ  . LYS B 392 ? 0.6449 0.6419 0.5188 -0.0158 -0.0147 0.0496  392 LYS B NZ  
7362 N N   . GLU B 393 ? 0.3912 0.4746 0.2668 -0.0465 0.0132  0.0721  393 GLU B N   
7363 C CA  . GLU B 393 ? 0.4487 0.5657 0.3171 -0.0534 0.0205  0.0776  393 GLU B CA  
7364 C C   . GLU B 393 ? 0.4513 0.5915 0.3113 -0.0418 0.0278  0.0645  393 GLU B C   
7365 O O   . GLU B 393 ? 0.5180 0.6879 0.3789 -0.0408 0.0360  0.0610  393 GLU B O   
7366 C CB  . GLU B 393 ? 0.5965 0.7150 0.4532 -0.0673 0.0161  0.0954  393 GLU B CB  
7367 C CG  . GLU B 393 ? 0.7771 0.8729 0.6409 -0.0798 0.0084  0.1093  393 GLU B CG  
7368 C CD  . GLU B 393 ? 0.9299 1.0180 0.7815 -0.0916 0.0011  0.1271  393 GLU B CD  
7369 O OE1 . GLU B 393 ? 0.9728 1.0685 0.8108 -0.0883 0.0008  0.1276  393 GLU B OE1 
7370 O OE2 . GLU B 393 ? 0.9993 1.0727 0.8543 -0.1044 -0.0050 0.1406  393 GLU B OE2 
7371 N N   . ASP B 394 ? 0.4218 0.5494 0.2738 -0.0327 0.0245  0.0565  394 ASP B N   
7372 C CA  . ASP B 394 ? 0.4711 0.6177 0.3119 -0.0226 0.0297  0.0443  394 ASP B CA  
7373 C C   . ASP B 394 ? 0.4049 0.5482 0.2539 -0.0082 0.0331  0.0267  394 ASP B C   
7374 O O   . ASP B 394 ? 0.4082 0.5409 0.2517 0.0021  0.0311  0.0147  394 ASP B O   
7375 C CB  . ASP B 394 ? 0.5685 0.7026 0.3960 -0.0208 0.0235  0.0441  394 ASP B CB  
7376 C CG  . ASP B 394 ? 0.6895 0.7884 0.5244 -0.0208 0.0139  0.0465  394 ASP B CG  
7377 O OD1 . ASP B 394 ? 0.7118 0.7961 0.5611 -0.0227 0.0123  0.0488  394 ASP B OD1 
7378 O OD2 . ASP B 394 ? 0.6786 0.7664 0.5050 -0.0187 0.0080  0.0457  394 ASP B OD2 
7379 N N   . VAL B 395 ? 0.3655 0.5175 0.2272 -0.0079 0.0375  0.0255  395 VAL B N   
7380 C CA  . VAL B 395 ? 0.3961 0.5462 0.2658 0.0056  0.0404  0.0106  395 VAL B CA  
7381 C C   . VAL B 395 ? 0.3701 0.5547 0.2437 0.0074  0.0490  0.0085  395 VAL B C   
7382 O O   . VAL B 395 ? 0.3958 0.6047 0.2674 -0.0036 0.0527  0.0195  395 VAL B O   
7383 C CB  . VAL B 395 ? 0.3903 0.5126 0.2746 0.0062  0.0355  0.0099  395 VAL B CB  
7384 C CG1 . VAL B 395 ? 0.3700 0.4626 0.2516 0.0045  0.0272  0.0121  395 VAL B CG1 
7385 C CG2 . VAL B 395 ? 0.3570 0.4849 0.2530 -0.0045 0.0364  0.0206  395 VAL B CG2 
7386 N N   . LYS B 396 ? 0.3150 0.5022 0.1941 0.0212  0.0519  -0.0052 396 LYS B N   
7387 C CA  . LYS B 396 ? 0.3162 0.5372 0.2008 0.0256  0.0597  -0.0088 396 LYS B CA  
7388 C C   . LYS B 396 ? 0.2738 0.4911 0.1758 0.0224  0.0595  -0.0052 396 LYS B C   
7389 O O   . LYS B 396 ? 0.2671 0.4543 0.1764 0.0240  0.0539  -0.0067 396 LYS B O   
7390 C CB  . LYS B 396 ? 0.3695 0.5914 0.2535 0.0431  0.0604  -0.0259 396 LYS B CB  
7391 C CG  . LYS B 396 ? 0.4987 0.7266 0.3697 0.0454  0.0601  -0.0300 396 LYS B CG  
7392 C CD  . LYS B 396 ? 0.6038 0.8641 0.4789 0.0481  0.0647  -0.0325 396 LYS B CD  
7393 C CE  . LYS B 396 ? 0.7131 0.9874 0.5755 0.0425  0.0654  -0.0290 396 LYS B CE  
7394 N NZ  . LYS B 396 ? 0.7699 1.0817 0.6371 0.0384  0.0702  -0.0247 396 LYS B NZ  
7395 N N   . THR B 397 ? 0.2947 0.5440 0.2038 0.0174  0.0650  -0.0004 397 THR B N   
7396 C CA  . THR B 397 ? 0.2864 0.5384 0.2109 0.0120  0.0652  0.0044  397 THR B CA  
7397 C C   . THR B 397 ? 0.2989 0.5786 0.2341 0.0192  0.0689  -0.0017 397 THR B C   
7398 O O   . THR B 397 ? 0.3195 0.6185 0.2514 0.0240  0.0708  -0.0058 397 THR B O   
7399 C CB  . THR B 397 ? 0.3734 0.6246 0.3009 -0.0090 0.0628  0.0218  397 THR B CB  
7400 O OG1 . THR B 397 ? 0.3784 0.6611 0.3022 -0.0178 0.0667  0.0290  397 THR B OG1 
7401 C CG2 . THR B 397 ? 0.3548 0.5699 0.2751 -0.0157 0.0550  0.0281  397 THR B CG2 
7402 N N   . GLU B 398 ? 0.2724 0.5532 0.2211 0.0200  0.0687  -0.0020 398 GLU B N   
7403 C CA  . GLU B 398 ? 0.2615 0.5641 0.2214 0.0277  0.0701  -0.0076 398 GLU B CA  
7404 C C   . GLU B 398 ? 0.2593 0.5676 0.2326 0.0175  0.0696  0.0000  398 GLU B C   
7405 O O   . GLU B 398 ? 0.2770 0.5658 0.2520 0.0109  0.0679  0.0045  398 GLU B O   
7406 C CB  . GLU B 398 ? 0.3325 0.6209 0.2928 0.0483  0.0681  -0.0224 398 GLU B CB  
7407 C CG  . GLU B 398 ? 0.3952 0.7048 0.3644 0.0588  0.0684  -0.0289 398 GLU B CG  
7408 C CD  . GLU B 398 ? 0.4435 0.7841 0.4093 0.0580  0.0715  -0.0289 398 GLU B CD  
7409 O OE1 . GLU B 398 ? 0.4417 0.7798 0.3980 0.0678  0.0714  -0.0370 398 GLU B OE1 
7410 O OE2 . GLU B 398 ? 0.4708 0.8388 0.4434 0.0468  0.0736  -0.0205 398 GLU B OE2 
7411 N N   . VAL B 399 ? 0.2813 0.6174 0.2640 0.0157  0.0708  0.0012  399 VAL B N   
7412 C CA  . VAL B 399 ? 0.2956 0.6386 0.2912 0.0062  0.0696  0.0073  399 VAL B CA  
7413 C C   . VAL B 399 ? 0.3192 0.6611 0.3236 0.0222  0.0681  -0.0030 399 VAL B C   
7414 O O   . VAL B 399 ? 0.3738 0.7219 0.3761 0.0378  0.0683  -0.0126 399 VAL B O   
7415 C CB  . VAL B 399 ? 0.2983 0.6724 0.2980 -0.0084 0.0706  0.0167  399 VAL B CB  
7416 C CG1 . VAL B 399 ? 0.4018 0.7800 0.4137 -0.0201 0.0682  0.0230  399 VAL B CG1 
7417 C CG2 . VAL B 399 ? 0.3169 0.6892 0.3063 -0.0238 0.0708  0.0276  399 VAL B CG2 
7418 N N   . ILE B 400 ? 0.1992 0.5318 0.2129 0.0182  0.0659  -0.0008 400 ILE B N   
7419 C CA  . ILE B 400 ? 0.2313 0.5637 0.2537 0.0309  0.0636  -0.0081 400 ILE B CA  
7420 C C   . ILE B 400 ? 0.2193 0.5691 0.2535 0.0186  0.0624  -0.0014 400 ILE B C   
7421 O O   . ILE B 400 ? 0.2556 0.5999 0.2925 0.0020  0.0616  0.0072  400 ILE B O   
7422 C CB  . ILE B 400 ? 0.2817 0.5811 0.3024 0.0410  0.0608  -0.0141 400 ILE B CB  
7423 C CG1 . ILE B 400 ? 0.3065 0.6037 0.3368 0.0495  0.0573  -0.0182 400 ILE B CG1 
7424 C CG2 . ILE B 400 ? 0.3150 0.5961 0.3335 0.0285  0.0607  -0.0077 400 ILE B CG2 
7425 C CD1 . ILE B 400 ? 0.3700 0.6367 0.3963 0.0639  0.0537  -0.0258 400 ILE B CD1 
7426 N N   . GLU B 401 ? 0.1878 0.5578 0.2285 0.0264  0.0616  -0.0052 401 GLU B N   
7427 C CA  . GLU B 401 ? 0.2294 0.6183 0.2805 0.0151  0.0601  0.0005  401 GLU B CA  
7428 C C   . GLU B 401 ? 0.2525 0.6301 0.3116 0.0209  0.0564  -0.0028 401 GLU B C   
7429 O O   . GLU B 401 ? 0.2110 0.5984 0.2782 0.0095  0.0544  0.0022  401 GLU B O   
7430 C CB  . GLU B 401 ? 0.2538 0.6782 0.3071 0.0177  0.0616  -0.0002 401 GLU B CB  
7431 C CG  . GLU B 401 ? 0.4082 0.8496 0.4538 0.0128  0.0651  0.0028  401 GLU B CG  
7432 C CD  . GLU B 401 ? 0.5093 0.9472 0.5523 -0.0095 0.0654  0.0147  401 GLU B CD  
7433 O OE1 . GLU B 401 ? 0.5236 0.9601 0.5731 -0.0243 0.0628  0.0219  401 GLU B OE1 
7434 O OE2 . GLU B 401 ? 0.5500 0.9849 0.5835 -0.0122 0.0675  0.0170  401 GLU B OE2 
7435 N N   . SER B 402 ? 0.1876 0.5443 0.2441 0.0374  0.0547  -0.0106 402 SER B N   
7436 C CA  . SER B 402 ? 0.1799 0.5276 0.2430 0.0437  0.0507  -0.0132 402 SER B CA  
7437 C C   . SER B 402 ? 0.2046 0.5209 0.2620 0.0575  0.0485  -0.0195 402 SER B C   
7438 O O   . SER B 402 ? 0.2642 0.5719 0.3131 0.0680  0.0495  -0.0246 402 SER B O   
7439 C CB  . SER B 402 ? 0.2474 0.6194 0.3154 0.0522  0.0495  -0.0160 402 SER B CB  
7440 O OG  . SER B 402 ? 0.2835 0.6480 0.3571 0.0577  0.0453  -0.0175 402 SER B OG  
7441 N N   . VAL B 403 ? 0.1754 0.4742 0.2368 0.0567  0.0451  -0.0191 403 VAL B N   
7442 C CA  . VAL B 403 ? 0.1784 0.4476 0.2347 0.0689  0.0420  -0.0241 403 VAL B CA  
7443 C C   . VAL B 403 ? 0.2273 0.4957 0.2886 0.0770  0.0374  -0.0255 403 VAL B C   
7444 O O   . VAL B 403 ? 0.2065 0.4932 0.2761 0.0705  0.0365  -0.0223 403 VAL B O   
7445 C CB  . VAL B 403 ? 0.1899 0.4366 0.2444 0.0616  0.0416  -0.0223 403 VAL B CB  
7446 C CG1 . VAL B 403 ? 0.2174 0.4653 0.2656 0.0536  0.0461  -0.0200 403 VAL B CG1 
7447 C CG2 . VAL B 403 ? 0.1441 0.3956 0.2084 0.0498  0.0397  -0.0178 403 VAL B CG2 
7448 N N   . LYS B 404 ? 0.1842 0.4314 0.2398 0.0909  0.0340  -0.0302 404 LYS B N   
7449 C CA  . LYS B 404 ? 0.1746 0.4158 0.2334 0.0982  0.0290  -0.0304 404 LYS B CA  
7450 C C   . LYS B 404 ? 0.1585 0.3777 0.2176 0.0931  0.0262  -0.0281 404 LYS B C   
7451 O O   . LYS B 404 ? 0.1879 0.3825 0.2399 0.0952  0.0255  -0.0298 404 LYS B O   
7452 C CB  . LYS B 404 ? 0.2658 0.4945 0.3182 0.1146  0.0259  -0.0356 404 LYS B CB  
7453 C CG  . LYS B 404 ? 0.5155 0.7665 0.5670 0.1216  0.0284  -0.0394 404 LYS B CG  
7454 C CD  . LYS B 404 ? 0.6553 0.9423 0.7159 0.1136  0.0312  -0.0358 404 LYS B CD  
7455 C CE  . LYS B 404 ? 0.7138 1.0232 0.7727 0.1101  0.0364  -0.0368 404 LYS B CE  
7456 N NZ  . LYS B 404 ? 0.7238 1.0620 0.7906 0.0950  0.0393  -0.0307 404 LYS B NZ  
7457 N N   . ALA B 405 ? 0.1372 0.3663 0.2043 0.0865  0.0243  -0.0246 405 ALA B N   
7458 C CA  . ALA B 405 ? 0.1308 0.3446 0.1992 0.0800  0.0220  -0.0227 405 ALA B CA  
7459 C C   . ALA B 405 ? 0.1442 0.3303 0.2055 0.0902  0.0177  -0.0240 405 ALA B C   
7460 O O   . ALA B 405 ? 0.1983 0.3803 0.2571 0.1011  0.0146  -0.0249 405 ALA B O   
7461 C CB  . ALA B 405 ? 0.1469 0.3777 0.2241 0.0724  0.0197  -0.0197 405 ALA B CB  
7462 N N   . GLY B 406 ? 0.1326 0.2998 0.1909 0.0861  0.0170  -0.0238 406 GLY B N   
7463 C CA  . GLY B 406 ? 0.2058 0.3455 0.2565 0.0928  0.0123  -0.0239 406 GLY B CA  
7464 C C   . GLY B 406 ? 0.1671 0.2834 0.2120 0.0817  0.0113  -0.0225 406 GLY B C   
7465 O O   . GLY B 406 ? 0.1508 0.2712 0.1983 0.0696  0.0133  -0.0215 406 GLY B O   
7466 N N   . THR B 407 ? 0.1580 0.2495 0.1952 0.0859  0.0076  -0.0223 407 THR B N   
7467 C CA  . THR B 407 ? 0.1433 0.2134 0.1747 0.0773  0.0062  -0.0212 407 THR B CA  
7468 C C   . THR B 407 ? 0.1437 0.1917 0.1657 0.0834  0.0048  -0.0235 407 THR B C   
7469 O O   . THR B 407 ? 0.1929 0.2403 0.2123 0.0949  0.0043  -0.0265 407 THR B O   
7470 C CB  . THR B 407 ? 0.1523 0.2158 0.1838 0.0731  0.0020  -0.0174 407 THR B CB  
7471 O OG1 . THR B 407 ? 0.1779 0.2275 0.2042 0.0819  -0.0027 -0.0154 407 THR B OG1 
7472 C CG2 . THR B 407 ? 0.1634 0.2493 0.2035 0.0690  0.0021  -0.0158 407 THR B CG2 
7473 N N   . TRP B 408 ? 0.1788 0.2087 0.1956 0.0762  0.0034  -0.0228 408 TRP B N   
7474 C CA  . TRP B 408 ? 0.1848 0.1931 0.1923 0.0804  0.0010  -0.0249 408 TRP B CA  
7475 C C   . TRP B 408 ? 0.2197 0.2116 0.2228 0.0857  -0.0051 -0.0224 408 TRP B C   
7476 O O   . TRP B 408 ? 0.2684 0.2394 0.2633 0.0888  -0.0084 -0.0241 408 TRP B O   
7477 C CB  . TRP B 408 ? 0.1782 0.1756 0.1822 0.0706  0.0016  -0.0250 408 TRP B CB  
7478 C CG  . TRP B 408 ? 0.1723 0.1664 0.1785 0.0613  -0.0004 -0.0213 408 TRP B CG  
7479 C CD1 . TRP B 408 ? 0.1713 0.1693 0.1806 0.0600  -0.0029 -0.0176 408 TRP B CD1 
7480 C CD2 . TRP B 408 ? 0.2127 0.2005 0.2177 0.0530  -0.0003 -0.0214 408 TRP B CD2 
7481 N NE1 . TRP B 408 ? 0.1833 0.1795 0.1933 0.0512  -0.0038 -0.0160 408 TRP B NE1 
7482 C CE2 . TRP B 408 ? 0.2304 0.2203 0.2384 0.0473  -0.0023 -0.0186 408 TRP B CE2 
7483 C CE3 . TRP B 408 ? 0.1992 0.1812 0.2008 0.0504  0.0010  -0.0237 408 TRP B CE3 
7484 C CZ2 . TRP B 408 ? 0.1929 0.1803 0.2013 0.0401  -0.0027 -0.0188 408 TRP B CZ2 
7485 C CZ3 . TRP B 408 ? 0.2031 0.1811 0.2052 0.0432  0.0000  -0.0231 408 TRP B CZ3 
7486 C CH2 . TRP B 408 ? 0.2086 0.1898 0.2145 0.0385  -0.0017 -0.0211 408 TRP B CH2 
7487 N N   . PHE B 409 ? 0.1806 0.1806 0.1884 0.0864  -0.0073 -0.0180 409 PHE B N   
7488 C CA  . PHE B 409 ? 0.2456 0.2304 0.2488 0.0924  -0.0139 -0.0143 409 PHE B CA  
7489 C C   . PHE B 409 ? 0.3127 0.3045 0.3176 0.1073  -0.0148 -0.0171 409 PHE B C   
7490 O O   . PHE B 409 ? 0.2835 0.2961 0.2960 0.1105  -0.0139 -0.0154 409 PHE B O   
7491 C CB  . PHE B 409 ? 0.2999 0.2896 0.3056 0.0848  -0.0165 -0.0072 409 PHE B CB  
7492 C CG  . PHE B 409 ? 0.3907 0.3598 0.3893 0.0860  -0.0240 -0.0010 409 PHE B CG  
7493 C CD1 . PHE B 409 ? 0.3522 0.3104 0.3475 0.0984  -0.0291 -0.0003 409 PHE B CD1 
7494 C CD2 . PHE B 409 ? 0.5191 0.4803 0.5141 0.0746  -0.0262 0.0045  409 PHE B CD2 
7495 C CE1 . PHE B 409 ? 0.4541 0.3903 0.4420 0.0987  -0.0372 0.0065  409 PHE B CE1 
7496 C CE2 . PHE B 409 ? 0.5195 0.4617 0.5072 0.0736  -0.0336 0.0117  409 PHE B CE2 
7497 C CZ  . PHE B 409 ? 0.5110 0.4390 0.4949 0.0853  -0.0394 0.0132  409 PHE B CZ  
7498 N N   . ASP B 410 ? 0.2877 0.2637 0.2858 0.1156  -0.0166 -0.0219 410 ASP B N   
7499 C CA  . ASP B 410 ? 0.3616 0.3428 0.3602 0.1254  -0.0172 -0.0250 410 ASP B CA  
7500 C C   . ASP B 410 ? 0.3168 0.3299 0.3241 0.1277  -0.0106 -0.0282 410 ASP B C   
7501 O O   . ASP B 410 ? 0.3727 0.3965 0.3825 0.1361  -0.0111 -0.0299 410 ASP B O   
7502 C CB  . ASP B 410 ? 0.5413 0.5141 0.5397 0.1311  -0.0243 -0.0193 410 ASP B CB  
7503 C CG  . ASP B 410 ? 0.6700 0.6095 0.6587 0.1287  -0.0318 -0.0157 410 ASP B CG  
7504 O OD1 . ASP B 410 ? 0.7218 0.6451 0.7038 0.1242  -0.0316 -0.0193 410 ASP B OD1 
7505 O OD2 . ASP B 410 ? 0.7267 0.6569 0.7141 0.1304  -0.0382 -0.0086 410 ASP B OD2 
7506 N N   . GLY B 411 ? 0.2056 0.2344 0.2175 0.1199  -0.0048 -0.0288 411 GLY B N   
7507 C CA  . GLY B 411 ? 0.2445 0.3037 0.2644 0.1196  0.0009  -0.0305 411 GLY B CA  
7508 C C   . GLY B 411 ? 0.2368 0.3175 0.2663 0.1196  0.0003  -0.0264 411 GLY B C   
7509 O O   . GLY B 411 ? 0.2328 0.3385 0.2686 0.1202  0.0038  -0.0276 411 GLY B O   
7510 N N   . ASN B 412 ? 0.2155 0.2888 0.2459 0.1183  -0.0043 -0.0214 412 ASN B N   
7511 C CA  . ASN B 412 ? 0.1872 0.2815 0.2258 0.1187  -0.0057 -0.0175 412 ASN B CA  
7512 C C   . ASN B 412 ? 0.1911 0.2833 0.2310 0.1086  -0.0078 -0.0125 412 ASN B C   
7513 O O   . ASN B 412 ? 0.1772 0.2516 0.2115 0.0996  -0.0075 -0.0119 412 ASN B O   
7514 C CB  . ASN B 412 ? 0.2365 0.3257 0.2731 0.1299  -0.0111 -0.0160 412 ASN B CB  
7515 C CG  . ASN B 412 ? 0.2915 0.3502 0.3197 0.1334  -0.0184 -0.0119 412 ASN B CG  
7516 O OD1 . ASN B 412 ? 0.2657 0.3173 0.2925 0.1280  -0.0215 -0.0064 412 ASN B OD1 
7517 N ND2 . ASN B 412 ? 0.3280 0.3696 0.3502 0.1425  -0.0219 -0.0141 412 ASN B ND2 
7518 N N   . PHE B 413 ? 0.1952 0.3058 0.2414 0.1079  -0.0098 -0.0089 413 PHE B N   
7519 C CA  . PHE B 413 ? 0.2093 0.3231 0.2563 0.0951  -0.0106 -0.0054 413 PHE B CA  
7520 C C   . PHE B 413 ? 0.1914 0.2951 0.2336 0.0966  -0.0171 0.0013  413 PHE B C   
7521 O O   . PHE B 413 ? 0.1602 0.2718 0.2032 0.0874  -0.0180 0.0041  413 PHE B O   
7522 C CB  . PHE B 413 ? 0.2005 0.3450 0.2578 0.0897  -0.0080 -0.0067 413 PHE B CB  
7523 C CG  . PHE B 413 ? 0.1408 0.2947 0.2022 0.0830  -0.0020 -0.0114 413 PHE B CG  
7524 C CD1 . PHE B 413 ? 0.1246 0.2712 0.1847 0.0699  0.0001  -0.0129 413 PHE B CD1 
7525 C CD2 . PHE B 413 ? 0.1435 0.3147 0.2100 0.0900  0.0012  -0.0140 413 PHE B CD2 
7526 C CE1 . PHE B 413 ? 0.1335 0.2862 0.1965 0.0630  0.0046  -0.0157 413 PHE B CE1 
7527 C CE2 . PHE B 413 ? 0.1538 0.3346 0.2233 0.0821  0.0066  -0.0167 413 PHE B CE2 
7528 C CZ  . PHE B 413 ? 0.1270 0.2970 0.1943 0.0684  0.0079  -0.0169 413 PHE B CZ  
7529 N N   . LEU B 414 ? 0.2094 0.2951 0.2457 0.1075  -0.0222 0.0041  414 LEU B N   
7530 C CA  . LEU B 414 ? 0.2258 0.3044 0.2579 0.1102  -0.0295 0.0123  414 LEU B CA  
7531 C C   . LEU B 414 ? 0.2537 0.3189 0.2788 0.0972  -0.0310 0.0175  414 LEU B C   
7532 O O   . LEU B 414 ? 0.2739 0.3424 0.2967 0.0948  -0.0358 0.0249  414 LEU B O   
7533 C CB  . LEU B 414 ? 0.2667 0.3247 0.2934 0.1252  -0.0355 0.0138  414 LEU B CB  
7534 C CG  . LEU B 414 ? 0.2302 0.3032 0.2633 0.1364  -0.0339 0.0088  414 LEU B CG  
7535 C CD1 . LEU B 414 ? 0.2916 0.3392 0.3179 0.1466  -0.0394 0.0090  414 LEU B CD1 
7536 C CD2 . LEU B 414 ? 0.2684 0.3700 0.3094 0.1359  -0.0348 0.0121  414 LEU B CD2 
7537 N N   . LYS B 415 ? 0.1943 0.2478 0.2165 0.0887  -0.0271 0.0139  415 LYS B N   
7538 C CA  . LYS B 415 ? 0.1805 0.2267 0.1974 0.0767  -0.0281 0.0181  415 LYS B CA  
7539 C C   . LYS B 415 ? 0.1806 0.2506 0.2026 0.0674  -0.0252 0.0170  415 LYS B C   
7540 O O   . LYS B 415 ? 0.2036 0.2735 0.2218 0.0584  -0.0259 0.0201  415 LYS B O   
7541 C CB  . LYS B 415 ? 0.2103 0.2385 0.2230 0.0712  -0.0255 0.0144  415 LYS B CB  
7542 C CG  . LYS B 415 ? 0.3293 0.3305 0.3345 0.0781  -0.0297 0.0158  415 LYS B CG  
7543 C CD  . LYS B 415 ? 0.3581 0.3444 0.3559 0.0773  -0.0376 0.0258  415 LYS B CD  
7544 C CE  . LYS B 415 ? 0.4340 0.4126 0.4267 0.0634  -0.0380 0.0299  415 LYS B CE  
7545 N NZ  . LYS B 415 ? 0.5406 0.5092 0.5261 0.0595  -0.0455 0.0416  415 LYS B NZ  
7546 N N   . TRP B 416 ? 0.1803 0.2717 0.2105 0.0691  -0.0223 0.0124  416 TRP B N   
7547 C CA  . TRP B 416 ? 0.1392 0.2509 0.1737 0.0600  -0.0203 0.0097  416 TRP B CA  
7548 C C   . TRP B 416 ? 0.1418 0.2767 0.1815 0.0630  -0.0227 0.0114  416 TRP B C   
7549 O O   . TRP B 416 ? 0.1725 0.3242 0.2146 0.0555  -0.0222 0.0092  416 TRP B O   
7550 C CB  . TRP B 416 ? 0.1350 0.2504 0.1747 0.0544  -0.0147 0.0013  416 TRP B CB  
7551 C CG  . TRP B 416 ? 0.1601 0.2549 0.1949 0.0511  -0.0126 -0.0006 416 TRP B CG  
7552 C CD1 . TRP B 416 ? 0.1539 0.2441 0.1857 0.0431  -0.0120 -0.0017 416 TRP B CD1 
7553 C CD2 . TRP B 416 ? 0.1493 0.2270 0.1814 0.0566  -0.0116 -0.0014 416 TRP B CD2 
7554 N NE1 . TRP B 416 ? 0.1651 0.2366 0.1931 0.0429  -0.0108 -0.0027 416 TRP B NE1 
7555 C CE2 . TRP B 416 ? 0.1724 0.2353 0.2000 0.0507  -0.0106 -0.0026 416 TRP B CE2 
7556 C CE3 . TRP B 416 ? 0.1631 0.2386 0.1961 0.0665  -0.0113 -0.0021 416 TRP B CE3 
7557 C CZ2 . TRP B 416 ? 0.2011 0.2460 0.2246 0.0535  -0.0097 -0.0041 416 TRP B CZ2 
7558 C CZ3 . TRP B 416 ? 0.1661 0.2238 0.1946 0.0698  -0.0101 -0.0045 416 TRP B CZ3 
7559 C CH2 . TRP B 416 ? 0.2013 0.2434 0.2249 0.0628  -0.0095 -0.0052 416 TRP B CH2 
7560 N N   . ILE B 417 ? 0.1688 0.3059 0.2104 0.0743  -0.0256 0.0146  417 ILE B N   
7561 C CA  . ILE B 417 ? 0.1844 0.3463 0.2323 0.0782  -0.0281 0.0162  417 ILE B CA  
7562 C C   . ILE B 417 ? 0.2169 0.3721 0.2632 0.0926  -0.0335 0.0221  417 ILE B C   
7563 O O   . ILE B 417 ? 0.2192 0.3540 0.2622 0.1003  -0.0337 0.0214  417 ILE B O   
7564 C CB  . ILE B 417 ? 0.1853 0.3680 0.2434 0.0758  -0.0233 0.0086  417 ILE B CB  
7565 C CG1 . ILE B 417 ? 0.1823 0.3947 0.2473 0.0757  -0.0259 0.0095  417 ILE B CG1 
7566 C CG2 . ILE B 417 ? 0.1881 0.3665 0.2495 0.0854  -0.0205 0.0057  417 ILE B CG2 
7567 C CD1 . ILE B 417 ? 0.2186 0.4501 0.2919 0.0662  -0.0219 0.0024  417 ILE B CD1 
7568 N N   . GLY B 418 ? 0.2670 0.4390 0.3153 0.0970  -0.0386 0.0274  418 GLY B N   
7569 C CA  . GLY B 418 ? 0.2881 0.4576 0.3369 0.1123  -0.0441 0.0318  418 GLY B CA  
7570 C C   . GLY B 418 ? 0.3751 0.5322 0.4154 0.1153  -0.0526 0.0430  418 GLY B C   
7571 O O   . GLY B 418 ? 0.5151 0.6714 0.5562 0.1239  -0.0570 0.0460  418 GLY B O   
7572 N N   . ASN B 419 ? 0.3511 0.4945 0.3823 0.1053  -0.0542 0.0487  419 ASN B N   
7573 C CA  . ASN B 419 ? 0.3781 0.5148 0.4009 0.1059  -0.0627 0.0612  419 ASN B CA  
7574 C C   . ASN B 419 ? 0.3277 0.4919 0.3508 0.0950  -0.0624 0.0636  419 ASN B C   
7575 O O   . ASN B 419 ? 0.2817 0.4651 0.3105 0.0867  -0.0560 0.0547  419 ASN B O   
7576 C CB  . ASN B 419 ? 0.4035 0.5061 0.4146 0.1013  -0.0657 0.0679  419 ASN B CB  
7577 C CG  . ASN B 419 ? 0.4246 0.5271 0.4317 0.0844  -0.0601 0.0659  419 ASN B CG  
7578 O OD1 . ASN B 419 ? 0.3848 0.5114 0.3956 0.0757  -0.0555 0.0614  419 ASN B OD1 
7579 N ND2 . ASN B 419 ? 0.4321 0.5070 0.4313 0.0802  -0.0613 0.0693  419 ASN B ND2 
7580 N N   . LYS B 420 ? 0.3411 0.5063 0.3572 0.0951  -0.0699 0.0753  420 LYS B N   
7581 C CA  . LYS B 420 ? 0.3176 0.5099 0.3335 0.0856  -0.0696 0.0760  420 LYS B CA  
7582 C C   . LYS B 420 ? 0.3275 0.5295 0.3407 0.0712  -0.0641 0.0716  420 LYS B C   
7583 O O   . LYS B 420 ? 0.2933 0.5203 0.3117 0.0651  -0.0602 0.0633  420 LYS B O   
7584 C CB  . LYS B 420 ? 0.4095 0.5960 0.4166 0.0861  -0.0779 0.0891  420 LYS B CB  
7585 C CG  . LYS B 420 ? 0.5658 0.7747 0.5675 0.0737  -0.0777 0.0923  420 LYS B CG  
7586 C CD  . LYS B 420 ? 0.6137 0.8537 0.6242 0.0695  -0.0719 0.0806  420 LYS B CD  
7587 C CE  . LYS B 420 ? 0.6321 0.8933 0.6377 0.0617  -0.0733 0.0836  420 LYS B CE  
7588 N NZ  . LYS B 420 ? 0.6800 0.9481 0.6892 0.0704  -0.0784 0.0872  420 LYS B NZ  
7589 N N   . GLU B 421 ? 0.3006 0.4802 0.3059 0.0647  -0.0630 0.0750  421 GLU B N   
7590 C CA  . GLU B 421 ? 0.3159 0.5044 0.3182 0.0509  -0.0574 0.0699  421 GLU B CA  
7591 C C   . GLU B 421 ? 0.2509 0.4426 0.2619 0.0487  -0.0492 0.0547  421 GLU B C   
7592 O O   . GLU B 421 ? 0.2277 0.4385 0.2408 0.0411  -0.0454 0.0466  421 GLU B O   
7593 C CB  . GLU B 421 ? 0.4153 0.5826 0.4075 0.0439  -0.0587 0.0784  421 GLU B CB  
7594 C CG  . GLU B 421 ? 0.5142 0.6819 0.4958 0.0410  -0.0666 0.0947  421 GLU B CG  
7595 C CD  . GLU B 421 ? 0.6865 0.8319 0.6659 0.0530  -0.0753 0.1050  421 GLU B CD  
7596 O OE1 . GLU B 421 ? 0.7150 0.8389 0.6988 0.0622  -0.0746 0.0997  421 GLU B OE1 
7597 O OE2 . GLU B 421 ? 0.7855 0.9336 0.7584 0.0535  -0.0826 0.1172  421 GLU B OE2 
7598 N N   . LYS B 422 ? 0.2162 0.3890 0.2317 0.0554  -0.0469 0.0503  422 LYS B N   
7599 C CA  . LYS B 422 ? 0.1716 0.3479 0.1949 0.0529  -0.0398 0.0374  422 LYS B CA  
7600 C C   . LYS B 422 ? 0.1601 0.3624 0.1922 0.0540  -0.0390 0.0311  422 LYS B C   
7601 O O   . LYS B 422 ? 0.1844 0.3982 0.2205 0.0465  -0.0350 0.0217  422 LYS B O   
7602 C CB  . LYS B 422 ? 0.2194 0.3727 0.2448 0.0597  -0.0377 0.0347  422 LYS B CB  
7603 C CG  . LYS B 422 ? 0.2361 0.3639 0.2535 0.0559  -0.0376 0.0381  422 LYS B CG  
7604 C CD  . LYS B 422 ? 0.2305 0.3353 0.2485 0.0641  -0.0370 0.0359  422 LYS B CD  
7605 C CE  . LYS B 422 ? 0.2365 0.3146 0.2452 0.0612  -0.0399 0.0420  422 LYS B CE  
7606 N NZ  . LYS B 422 ? 0.1966 0.2747 0.2039 0.0494  -0.0351 0.0380  422 LYS B NZ  
7607 N N   . ASN B 423 ? 0.1688 0.3810 0.2042 0.0632  -0.0437 0.0363  423 ASN B N   
7608 C CA  . ASN B 423 ? 0.1489 0.3892 0.1931 0.0632  -0.0437 0.0312  423 ASN B CA  
7609 C C   . ASN B 423 ? 0.1902 0.4512 0.2317 0.0530  -0.0446 0.0291  423 ASN B C   
7610 O O   . ASN B 423 ? 0.1817 0.4572 0.2284 0.0468  -0.0417 0.0201  423 ASN B O   
7611 C CB  . ASN B 423 ? 0.1606 0.4060 0.2077 0.0748  -0.0482 0.0370  423 ASN B CB  
7612 C CG  . ASN B 423 ? 0.1896 0.4240 0.2426 0.0850  -0.0458 0.0339  423 ASN B CG  
7613 O OD1 . ASN B 423 ? 0.2142 0.4385 0.2691 0.0835  -0.0412 0.0283  423 ASN B OD1 
7614 N ND2 . ASN B 423 ? 0.2065 0.4426 0.2619 0.0952  -0.0486 0.0367  423 ASN B ND2 
7615 N N   . GLU B 424 ? 0.2040 0.4625 0.2353 0.0495  -0.0477 0.0368  424 GLU B N   
7616 C CA  . GLU B 424 ? 0.2267 0.5036 0.2537 0.0396  -0.0473 0.0334  424 GLU B CA  
7617 C C   . GLU B 424 ? 0.1490 0.4285 0.1784 0.0312  -0.0420 0.0204  424 GLU B C   
7618 O O   . GLU B 424 ? 0.1712 0.4641 0.2014 0.0248  -0.0401 0.0115  424 GLU B O   
7619 C CB  . GLU B 424 ? 0.2868 0.5609 0.3019 0.0367  -0.0509 0.0448  424 GLU B CB  
7620 C CG  . GLU B 424 ? 0.4222 0.7153 0.4315 0.0271  -0.0493 0.0413  424 GLU B CG  
7621 C CD  . GLU B 424 ? 0.6428 0.9535 0.6543 0.0278  -0.0508 0.0400  424 GLU B CD  
7622 O OE1 . GLU B 424 ? 0.6685 0.9907 0.6851 0.0241  -0.0476 0.0280  424 GLU B OE1 
7623 O OE2 . GLU B 424 ? 0.7509 1.0625 0.7587 0.0318  -0.0558 0.0512  424 GLU B OE2 
7624 N N   . TYR B 425 ? 0.1896 0.4462 0.2180 0.0304  -0.0378 0.0182  425 TYR B N   
7625 C CA  . TYR B 425 ? 0.1516 0.4053 0.1824 0.0238  -0.0327 0.0059  425 TYR B CA  
7626 C C   . TYR B 425 ? 0.1233 0.3834 0.1638 0.0231  -0.0313 -0.0034 425 TYR B C   
7627 O O   . TYR B 425 ? 0.1443 0.4139 0.1865 0.0165  -0.0305 -0.0137 425 TYR B O   
7628 C CB  . TYR B 425 ? 0.1473 0.3755 0.1760 0.0241  -0.0291 0.0062  425 TYR B CB  
7629 C CG  . TYR B 425 ? 0.1423 0.3687 0.1628 0.0189  -0.0284 0.0087  425 TYR B CG  
7630 C CD1 . TYR B 425 ? 0.1898 0.4328 0.2030 0.0158  -0.0316 0.0155  425 TYR B CD1 
7631 C CD2 . TYR B 425 ? 0.1401 0.3503 0.1600 0.0168  -0.0246 0.0049  425 TYR B CD2 
7632 C CE1 . TYR B 425 ? 0.1630 0.4078 0.1686 0.0100  -0.0305 0.0184  425 TYR B CE1 
7633 C CE2 . TYR B 425 ? 0.1447 0.3564 0.1582 0.0118  -0.0237 0.0073  425 TYR B CE2 
7634 C CZ  . TYR B 425 ? 0.1392 0.3689 0.1457 0.0081  -0.0264 0.0140  425 TYR B CZ  
7635 O OH  . TYR B 425 ? 0.1884 0.4229 0.1887 0.0021  -0.0250 0.0166  425 TYR B OH  
7636 N N   . TRP B 426 ? 0.1183 0.3736 0.1650 0.0297  -0.0313 -0.0002 426 TRP B N   
7637 C CA  . TRP B 426 ? 0.1305 0.3954 0.1868 0.0276  -0.0300 -0.0074 426 TRP B CA  
7638 C C   . TRP B 426 ? 0.1169 0.4023 0.1733 0.0229  -0.0324 -0.0101 426 TRP B C   
7639 O O   . TRP B 426 ? 0.1292 0.4186 0.1883 0.0151  -0.0313 -0.0192 426 TRP B O   
7640 C CB  . TRP B 426 ? 0.1180 0.3786 0.1803 0.0364  -0.0292 -0.0029 426 TRP B CB  
7641 C CG  . TRP B 426 ? 0.1413 0.3764 0.2020 0.0386  -0.0249 -0.0036 426 TRP B CG  
7642 C CD1 . TRP B 426 ? 0.1157 0.3317 0.1711 0.0460  -0.0252 0.0029  426 TRP B CD1 
7643 C CD2 . TRP B 426 ? 0.1228 0.3483 0.1867 0.0329  -0.0206 -0.0109 426 TRP B CD2 
7644 N NE1 . TRP B 426 ? 0.1345 0.3314 0.1896 0.0454  -0.0209 -0.0006 426 TRP B NE1 
7645 C CE2 . TRP B 426 ? 0.1446 0.3471 0.2048 0.0376  -0.0180 -0.0085 426 TRP B CE2 
7646 C CE3 . TRP B 426 ? 0.1435 0.3759 0.2123 0.0238  -0.0194 -0.0190 426 TRP B CE3 
7647 C CZ2 . TRP B 426 ? 0.1903 0.3790 0.2517 0.0340  -0.0140 -0.0135 426 TRP B CZ2 
7648 C CZ3 . TRP B 426 ? 0.1517 0.3681 0.2215 0.0201  -0.0158 -0.0232 426 TRP B CZ3 
7649 C CH2 . TRP B 426 ? 0.1366 0.3324 0.2028 0.0254  -0.0130 -0.0202 426 TRP B CH2 
7650 N N   . LYS B 427 ? 0.1258 0.4205 0.1777 0.0269  -0.0358 -0.0022 427 LYS B N   
7651 C CA  . LYS B 427 ? 0.1592 0.4715 0.2097 0.0222  -0.0375 -0.0047 427 LYS B CA  
7652 C C   . LYS B 427 ? 0.1331 0.4487 0.1780 0.0130  -0.0366 -0.0138 427 LYS B C   
7653 O O   . LYS B 427 ? 0.1630 0.4877 0.2093 0.0068  -0.0367 -0.0217 427 LYS B O   
7654 C CB  . LYS B 427 ? 0.2282 0.5491 0.2740 0.0281  -0.0416 0.0060  427 LYS B CB  
7655 C CG  . LYS B 427 ? 0.4044 0.7243 0.4556 0.0384  -0.0435 0.0134  427 LYS B CG  
7656 C CD  . LYS B 427 ? 0.5295 0.8604 0.5774 0.0431  -0.0483 0.0220  427 LYS B CD  
7657 C CE  . LYS B 427 ? 0.5740 0.9102 0.6297 0.0523  -0.0496 0.0248  427 LYS B CE  
7658 N NZ  . LYS B 427 ? 0.5677 0.9139 0.6329 0.0496  -0.0460 0.0166  427 LYS B NZ  
7659 N N   . ILE B 428 ? 0.1386 0.4475 0.1768 0.0124  -0.0358 -0.0130 428 ILE B N   
7660 C CA  . ILE B 428 ? 0.1416 0.4538 0.1745 0.0054  -0.0343 -0.0230 428 ILE B CA  
7661 C C   . ILE B 428 ? 0.1283 0.4313 0.1670 0.0009  -0.0324 -0.0355 428 ILE B C   
7662 O O   . ILE B 428 ? 0.1388 0.4468 0.1765 -0.0047 -0.0327 -0.0458 428 ILE B O   
7663 C CB  . ILE B 428 ? 0.1928 0.5009 0.2182 0.0059  -0.0332 -0.0190 428 ILE B CB  
7664 C CG1 . ILE B 428 ? 0.1830 0.5025 0.2006 0.0072  -0.0357 -0.0072 428 ILE B CG1 
7665 C CG2 . ILE B 428 ? 0.1704 0.4784 0.1927 0.0008  -0.0304 -0.0318 428 ILE B CG2 
7666 C CD1 . ILE B 428 ? 0.2598 0.5720 0.2713 0.0080  -0.0359 0.0021  428 ILE B CD1 
7667 N N   . LEU B 429 ? 0.1397 0.4285 0.1847 0.0033  -0.0309 -0.0346 429 LEU B N   
7668 C CA  . LEU B 429 ? 0.1581 0.4364 0.2088 -0.0014 -0.0297 -0.0447 429 LEU B CA  
7669 C C   . LEU B 429 ? 0.1492 0.4348 0.2054 -0.0063 -0.0312 -0.0480 429 LEU B C   
7670 O O   . LEU B 429 ? 0.1676 0.4497 0.2249 -0.0133 -0.0323 -0.0582 429 LEU B O   
7671 C CB  . LEU B 429 ? 0.1193 0.3813 0.1750 0.0025  -0.0271 -0.0410 429 LEU B CB  
7672 C CG  . LEU B 429 ? 0.1535 0.3998 0.2137 -0.0024 -0.0254 -0.0490 429 LEU B CG  
7673 C CD1 . LEU B 429 ? 0.1860 0.4212 0.2412 -0.0049 -0.0249 -0.0585 429 LEU B CD1 
7674 C CD2 . LEU B 429 ? 0.1501 0.3801 0.2137 0.0017  -0.0218 -0.0427 429 LEU B CD2 
7675 N N   . ILE B 430 ? 0.1252 0.4206 0.1849 -0.0027 -0.0318 -0.0396 430 ILE B N   
7676 C CA  . ILE B 430 ? 0.1673 0.4728 0.2325 -0.0078 -0.0332 -0.0416 430 ILE B CA  
7677 C C   . ILE B 430 ? 0.1521 0.4681 0.2126 -0.0140 -0.0359 -0.0485 430 ILE B C   
7678 O O   . ILE B 430 ? 0.1420 0.4578 0.2055 -0.0222 -0.0375 -0.0564 430 ILE B O   
7679 C CB  . ILE B 430 ? 0.1659 0.4820 0.2349 -0.0007 -0.0333 -0.0314 430 ILE B CB  
7680 C CG1 . ILE B 430 ? 0.1325 0.4383 0.2073 0.0048  -0.0302 -0.0272 430 ILE B CG1 
7681 C CG2 . ILE B 430 ? 0.1598 0.4926 0.2332 -0.0059 -0.0351 -0.0328 430 ILE B CG2 
7682 C CD1 . ILE B 430 ? 0.1503 0.4595 0.2255 0.0168  -0.0305 -0.0171 430 ILE B CD1 
7683 N N   . GLU B 431 ? 0.1606 0.4854 0.2134 -0.0106 -0.0366 -0.0456 431 GLU B N   
7684 C CA  . GLU B 431 ? 0.1847 0.5217 0.2325 -0.0156 -0.0387 -0.0520 431 GLU B CA  
7685 C C   . GLU B 431 ? 0.1846 0.5114 0.2295 -0.0209 -0.0385 -0.0652 431 GLU B C   
7686 O O   . GLU B 431 ? 0.2465 0.5765 0.2915 -0.0273 -0.0409 -0.0742 431 GLU B O   
7687 C CB  . GLU B 431 ? 0.2705 0.6203 0.3106 -0.0108 -0.0393 -0.0444 431 GLU B CB  
7688 C CG  . GLU B 431 ? 0.4485 0.8159 0.4845 -0.0148 -0.0415 -0.0483 431 GLU B CG  
7689 C CD  . GLU B 431 ? 0.5252 0.9008 0.5681 -0.0195 -0.0440 -0.0509 431 GLU B CD  
7690 O OE1 . GLU B 431 ? 0.5378 0.9189 0.5863 -0.0158 -0.0446 -0.0423 431 GLU B OE1 
7691 O OE2 . GLU B 431 ? 0.5475 0.9240 0.5905 -0.0269 -0.0456 -0.0617 431 GLU B OE2 
7692 N N   . ALA B 432 ? 0.1516 0.4650 0.1943 -0.0180 -0.0361 -0.0670 432 ALA B N   
7693 C CA  . ALA B 432 ? 0.2099 0.5127 0.2502 -0.0211 -0.0361 -0.0801 432 ALA B CA  
7694 C C   . ALA B 432 ? 0.2259 0.5141 0.2732 -0.0273 -0.0383 -0.0873 432 ALA B C   
7695 O O   . ALA B 432 ? 0.2291 0.5107 0.2751 -0.0319 -0.0408 -0.0987 432 ALA B O   
7696 C CB  . ALA B 432 ? 0.2088 0.5026 0.2456 -0.0162 -0.0330 -0.0797 432 ALA B CB  
7697 N N   . LYS B 433 ? 0.2082 0.4906 0.2628 -0.0276 -0.0376 -0.0803 433 LYS B N   
7698 C CA  . LYS B 433 ? 0.1927 0.4623 0.2538 -0.0350 -0.0396 -0.0848 433 LYS B CA  
7699 C C   . LYS B 433 ? 0.2234 0.5010 0.2862 -0.0434 -0.0437 -0.0889 433 LYS B C   
7700 O O   . LYS B 433 ? 0.2104 0.4741 0.2748 -0.0511 -0.0471 -0.0966 433 LYS B O   
7701 C CB  . LYS B 433 ? 0.2126 0.4806 0.2813 -0.0334 -0.0371 -0.0751 433 LYS B CB  
7702 C CG  . LYS B 433 ? 0.2102 0.4696 0.2861 -0.0424 -0.0387 -0.0766 433 LYS B CG  
7703 C CD  . LYS B 433 ? 0.2065 0.4420 0.2816 -0.0459 -0.0400 -0.0848 433 LYS B CD  
7704 C CE  . LYS B 433 ? 0.2526 0.4784 0.3333 -0.0573 -0.0430 -0.0857 433 LYS B CE  
7705 N NZ  . LYS B 433 ? 0.2742 0.4723 0.3524 -0.0605 -0.0457 -0.0941 433 LYS B NZ  
7706 N N   . LYS B 434 ? 0.2384 0.5366 0.3003 -0.0422 -0.0440 -0.0836 434 LYS B N   
7707 C CA  . LYS B 434 ? 0.2650 0.5728 0.3282 -0.0503 -0.0482 -0.0876 434 LYS B CA  
7708 C C   . LYS B 434 ? 0.3124 0.6106 0.3699 -0.0546 -0.0518 -0.1012 434 LYS B C   
7709 O O   . LYS B 434 ? 0.3193 0.6138 0.3786 -0.0636 -0.0566 -0.1070 434 LYS B O   
7710 C CB  . LYS B 434 ? 0.2940 0.6261 0.3557 -0.0467 -0.0481 -0.0805 434 LYS B CB  
7711 C CG  . LYS B 434 ? 0.3906 0.7328 0.4581 -0.0417 -0.0457 -0.0680 434 LYS B CG  
7712 C CD  . LYS B 434 ? 0.4811 0.8457 0.5469 -0.0375 -0.0467 -0.0613 434 LYS B CD  
7713 C CE  . LYS B 434 ? 0.5173 0.8898 0.5891 -0.0307 -0.0447 -0.0499 434 LYS B CE  
7714 N NZ  . LYS B 434 ? 0.5324 0.9230 0.6014 -0.0237 -0.0459 -0.0423 434 LYS B NZ  
7715 N N   . LYS B 435 ? 0.2459 0.5406 0.2962 -0.0480 -0.0498 -0.1062 435 LYS B N   
7716 C CA  . LYS B 435 ? 0.2997 0.5874 0.3441 -0.0495 -0.0526 -0.1198 435 LYS B CA  
7717 C C   . LYS B 435 ? 0.3382 0.6040 0.3806 -0.0454 -0.0514 -0.1271 435 LYS B C   
7718 O O   . LYS B 435 ? 0.3319 0.5950 0.3686 -0.0421 -0.0518 -0.1374 435 LYS B O   
7719 C CB  . LYS B 435 ? 0.4235 0.7326 0.4608 -0.0452 -0.0512 -0.1207 435 LYS B CB  
7720 C CG  . LYS B 435 ? 0.4745 0.8012 0.5106 -0.0389 -0.0470 -0.1071 435 LYS B CG  
7721 C CD  . LYS B 435 ? 0.5330 0.8829 0.5631 -0.0382 -0.0474 -0.1062 435 LYS B CD  
7722 C CE  . LYS B 435 ? 0.6003 0.9631 0.6259 -0.0312 -0.0436 -0.0944 435 LYS B CE  
7723 N NZ  . LYS B 435 ? 0.6558 1.0417 0.6756 -0.0312 -0.0444 -0.0921 435 LYS B NZ  
7724 N N   . ALA B 436 ? 0.2781 0.5294 0.3254 -0.0451 -0.0499 -0.1222 436 ALA B N   
7725 C CA  . ALA B 436 ? 0.2879 0.5188 0.3337 -0.0405 -0.0487 -0.1282 436 ALA B CA  
7726 C C   . ALA B 436 ? 0.3458 0.5545 0.3902 -0.0450 -0.0544 -0.1403 436 ALA B C   
7727 O O   . ALA B 436 ? 0.3522 0.5546 0.3991 -0.0545 -0.0595 -0.1408 436 ALA B O   
7728 C CB  . ALA B 436 ? 0.2526 0.4740 0.3040 -0.0397 -0.0461 -0.1195 436 ALA B CB  
7729 N N   . LYS B 437 ? 0.3317 0.5283 0.3718 -0.0381 -0.0539 -0.1495 437 LYS B N   
7730 C CA  . LYS B 437 ? 0.3268 0.5000 0.3641 -0.0399 -0.0599 -0.1613 437 LYS B CA  
7731 C C   . LYS B 437 ? 0.3749 0.5226 0.4124 -0.0343 -0.0597 -0.1646 437 LYS B C   
7732 O O   . LYS B 437 ? 0.4336 0.5575 0.4683 -0.0352 -0.0652 -0.1731 437 LYS B O   
7733 C CB  . LYS B 437 ? 0.3603 0.5449 0.3915 -0.0357 -0.0609 -0.1723 437 LYS B CB  
7734 C CG  . LYS B 437 ? 0.4521 0.6638 0.4821 -0.0402 -0.0608 -0.1691 437 LYS B CG  
7735 C CD  . LYS B 437 ? 0.5921 0.8113 0.6159 -0.0383 -0.0635 -0.1813 437 LYS B CD  
7736 C CE  . LYS B 437 ? 0.6965 0.9010 0.7188 -0.0483 -0.0723 -0.1879 437 LYS B CE  
7737 N NZ  . LYS B 437 ? 0.7108 0.9300 0.7370 -0.0581 -0.0739 -0.1784 437 LYS B NZ  
7738 N N   . ASN B 438 ? 0.3067 0.4572 0.3469 -0.0286 -0.0542 -0.1577 438 ASN B N   
7739 C CA  . ASN B 438 ? 0.2975 0.4257 0.3382 -0.0225 -0.0538 -0.1601 438 ASN B CA  
7740 C C   . ASN B 438 ? 0.3340 0.4647 0.3789 -0.0215 -0.0491 -0.1492 438 ASN B C   
7741 O O   . ASN B 438 ? 0.3681 0.5180 0.4151 -0.0244 -0.0462 -0.1404 438 ASN B O   
7742 C CB  . ASN B 438 ? 0.3298 0.4632 0.3670 -0.0114 -0.0519 -0.1694 438 ASN B CB  
7743 C CG  . ASN B 438 ? 0.2993 0.4641 0.3356 -0.0065 -0.0454 -0.1656 438 ASN B CG  
7744 O OD1 . ASN B 438 ? 0.2965 0.4682 0.3345 -0.0049 -0.0409 -0.1565 438 ASN B OD1 
7745 N ND2 . ASN B 438 ? 0.2887 0.4720 0.3215 -0.0045 -0.0452 -0.1721 438 ASN B ND2 
7746 N N   . ASP B 439 ? 0.2952 0.4061 0.3410 -0.0166 -0.0487 -0.1496 439 ASP B N   
7747 C CA  . ASP B 439 ? 0.2974 0.4055 0.3468 -0.0161 -0.0453 -0.1404 439 ASP B CA  
7748 C C   . ASP B 439 ? 0.2376 0.3668 0.2860 -0.0091 -0.0392 -0.1362 439 ASP B C   
7749 O O   . ASP B 439 ? 0.2236 0.3503 0.2741 -0.0081 -0.0364 -0.1286 439 ASP B O   
7750 C CB  . ASP B 439 ? 0.3639 0.4427 0.4140 -0.0133 -0.0475 -0.1417 439 ASP B CB  
7751 C CG  . ASP B 439 ? 0.4718 0.5283 0.5235 -0.0236 -0.0533 -0.1398 439 ASP B CG  
7752 O OD1 . ASP B 439 ? 0.4826 0.5486 0.5360 -0.0333 -0.0553 -0.1375 439 ASP B OD1 
7753 O OD2 . ASP B 439 ? 0.5656 0.5963 0.6167 -0.0225 -0.0561 -0.1394 439 ASP B OD2 
7754 N N   . TYR B 440 ? 0.2495 0.3991 0.2941 -0.0050 -0.0371 -0.1398 440 TYR B N   
7755 C CA  . TYR B 440 ? 0.2032 0.3737 0.2458 -0.0012 -0.0320 -0.1328 440 TYR B CA  
7756 C C   . TYR B 440 ? 0.2234 0.4063 0.2678 -0.0064 -0.0313 -0.1213 440 TYR B C   
7757 O O   . TYR B 440 ? 0.1674 0.3568 0.2110 -0.0035 -0.0271 -0.1105 440 TYR B O   
7758 C CB  . TYR B 440 ? 0.1630 0.3548 0.2014 0.0029  -0.0299 -0.1378 440 TYR B CB  
7759 C CG  . TYR B 440 ? 0.2248 0.4138 0.2633 0.0109  -0.0282 -0.1442 440 TYR B CG  
7760 C CD1 . TYR B 440 ? 0.2859 0.4779 0.3244 0.0144  -0.0245 -0.1383 440 TYR B CD1 
7761 C CD2 . TYR B 440 ? 0.2731 0.4566 0.3122 0.0150  -0.0310 -0.1560 440 TYR B CD2 
7762 C CE1 . TYR B 440 ? 0.3181 0.5105 0.3583 0.0214  -0.0232 -0.1433 440 TYR B CE1 
7763 C CE2 . TYR B 440 ? 0.2888 0.4726 0.3297 0.0234  -0.0300 -0.1613 440 TYR B CE2 
7764 C CZ  . TYR B 440 ? 0.3023 0.4919 0.3444 0.0262  -0.0260 -0.1545 440 TYR B CZ  
7765 O OH  . TYR B 440 ? 0.3376 0.5305 0.3825 0.0338  -0.0254 -0.1588 440 TYR B OH  
7766 N N   . ILE B 441 ? 0.1978 0.3805 0.2452 -0.0133 -0.0343 -0.1201 441 ILE B N   
7767 C CA  . ILE B 441 ? 0.1682 0.3612 0.2195 -0.0163 -0.0329 -0.1073 441 ILE B CA  
7768 C C   . ILE B 441 ? 0.1943 0.3692 0.2488 -0.0142 -0.0291 -0.0974 441 ILE B C   
7769 O O   . ILE B 441 ? 0.1794 0.3604 0.2349 -0.0117 -0.0256 -0.0857 441 ILE B O   
7770 C CB  . ILE B 441 ? 0.2229 0.4218 0.2778 -0.0245 -0.0368 -0.1082 441 ILE B CB  
7771 C CG1 . ILE B 441 ? 0.2299 0.4479 0.2884 -0.0250 -0.0351 -0.0958 441 ILE B CG1 
7772 C CG2 . ILE B 441 ? 0.1866 0.3641 0.2463 -0.0314 -0.0401 -0.1112 441 ILE B CG2 
7773 C CD1 . ILE B 441 ? 0.1828 0.4204 0.2354 -0.0201 -0.0333 -0.0912 441 ILE B CD1 
7774 N N   . LEU B 442 ? 0.1671 0.3189 0.2226 -0.0148 -0.0302 -0.1021 442 LEU B N   
7775 C CA  . LEU B 442 ? 0.1361 0.2715 0.1935 -0.0128 -0.0268 -0.0933 442 LEU B CA  
7776 C C   . LEU B 442 ? 0.1294 0.2662 0.1834 -0.0051 -0.0224 -0.0887 442 LEU B C   
7777 O O   . LEU B 442 ? 0.1427 0.2762 0.1972 -0.0030 -0.0189 -0.0783 442 LEU B O   
7778 C CB  . LEU B 442 ? 0.1961 0.3065 0.2546 -0.0152 -0.0300 -0.0988 442 LEU B CB  
7779 C CG  . LEU B 442 ? 0.2545 0.3580 0.3157 -0.0249 -0.0356 -0.1034 442 LEU B CG  
7780 C CD1 . LEU B 442 ? 0.2316 0.3065 0.2926 -0.0264 -0.0392 -0.1064 442 LEU B CD1 
7781 C CD2 . LEU B 442 ? 0.2155 0.3309 0.2813 -0.0315 -0.0339 -0.0928 442 LEU B CD2 
7782 N N   . VAL B 443 ? 0.1441 0.2865 0.1944 -0.0011 -0.0228 -0.0967 443 VAL B N   
7783 C CA  . VAL B 443 ? 0.1687 0.3160 0.2159 0.0043  -0.0189 -0.0918 443 VAL B CA  
7784 C C   . VAL B 443 ? 0.1336 0.2951 0.1792 0.0042  -0.0165 -0.0799 443 VAL B C   
7785 O O   . VAL B 443 ? 0.1321 0.2880 0.1766 0.0066  -0.0137 -0.0706 443 VAL B O   
7786 C CB  . VAL B 443 ? 0.1800 0.3390 0.2239 0.0078  -0.0195 -0.1026 443 VAL B CB  
7787 C CG1 . VAL B 443 ? 0.1559 0.3217 0.1971 0.0115  -0.0155 -0.0964 443 VAL B CG1 
7788 C CG2 . VAL B 443 ? 0.1907 0.3344 0.2361 0.0099  -0.0232 -0.1161 443 VAL B CG2 
7789 N N   . ALA B 444 ? 0.1341 0.3131 0.1791 0.0015  -0.0184 -0.0801 444 ALA B N   
7790 C CA  . ALA B 444 ? 0.1631 0.3558 0.2063 0.0023  -0.0175 -0.0688 444 ALA B CA  
7791 C C   . ALA B 444 ? 0.1766 0.3603 0.2238 0.0031  -0.0165 -0.0592 444 ALA B C   
7792 O O   . ALA B 444 ? 0.1432 0.3328 0.1888 0.0059  -0.0160 -0.0492 444 ALA B O   
7793 C CB  . ALA B 444 ? 0.1600 0.3753 0.2016 -0.0004 -0.0205 -0.0718 444 ALA B CB  
7794 N N   . GLU B 445 ? 0.1251 0.2951 0.1770 0.0009  -0.0165 -0.0618 445 GLU B N   
7795 C CA  . GLU B 445 ? 0.1187 0.2826 0.1741 0.0022  -0.0147 -0.0536 445 GLU B CA  
7796 C C   . GLU B 445 ? 0.1483 0.2950 0.2014 0.0065  -0.0116 -0.0483 445 GLU B C   
7797 O O   . GLU B 445 ? 0.1607 0.3021 0.2156 0.0088  -0.0099 -0.0422 445 GLU B O   
7798 C CB  . GLU B 445 ? 0.1401 0.3002 0.2011 -0.0038 -0.0161 -0.0574 445 GLU B CB  
7799 C CG  . GLU B 445 ? 0.1741 0.3539 0.2381 -0.0089 -0.0196 -0.0607 445 GLU B CG  
7800 C CD  . GLU B 445 ? 0.1603 0.3354 0.2285 -0.0178 -0.0227 -0.0670 445 GLU B CD  
7801 O OE1 . GLU B 445 ? 0.1804 0.3367 0.2494 -0.0200 -0.0221 -0.0675 445 GLU B OE1 
7802 O OE2 . GLU B 445 ? 0.1732 0.3632 0.2436 -0.0232 -0.0263 -0.0711 445 GLU B OE2 
7803 N N   . GLY B 446 ? 0.1338 0.2742 0.1830 0.0080  -0.0110 -0.0507 446 GLY B N   
7804 C CA  . GLY B 446 ? 0.1425 0.2677 0.1894 0.0112  -0.0087 -0.0460 446 GLY B CA  
7805 C C   . GLY B 446 ? 0.1686 0.2950 0.2128 0.0150  -0.0080 -0.0359 446 GLY B C   
7806 O O   . GLY B 446 ? 0.1582 0.2977 0.2005 0.0156  -0.0095 -0.0321 446 GLY B O   
7807 N N   . SER B 447 ? 0.1379 0.2495 0.1813 0.0178  -0.0064 -0.0317 447 SER B N   
7808 C CA  . SER B 447 ? 0.1241 0.2333 0.1648 0.0226  -0.0067 -0.0233 447 SER B CA  
7809 C C   . SER B 447 ? 0.1398 0.2489 0.1747 0.0225  -0.0082 -0.0182 447 SER B C   
7810 O O   . SER B 447 ? 0.1517 0.2619 0.1838 0.0256  -0.0102 -0.0109 447 SER B O   
7811 C CB  . SER B 447 ? 0.1475 0.2409 0.1878 0.0259  -0.0048 -0.0215 447 SER B CB  
7812 O OG  . SER B 447 ? 0.1654 0.2455 0.2024 0.0245  -0.0042 -0.0227 447 SER B OG  
7813 N N   . ASP B 448 ? 0.1166 0.2250 0.1497 0.0190  -0.0075 -0.0215 448 ASP B N   
7814 C CA  . ASP B 448 ? 0.1083 0.2169 0.1358 0.0171  -0.0086 -0.0158 448 ASP B CA  
7815 C C   . ASP B 448 ? 0.1106 0.2349 0.1351 0.0159  -0.0109 -0.0102 448 ASP B C   
7816 O O   . ASP B 448 ? 0.1642 0.2843 0.1834 0.0155  -0.0132 -0.0009 448 ASP B O   
7817 C CB  . ASP B 448 ? 0.1435 0.2553 0.1714 0.0139  -0.0071 -0.0217 448 ASP B CB  
7818 C CG  . ASP B 448 ? 0.1823 0.2792 0.2132 0.0154  -0.0056 -0.0270 448 ASP B CG  
7819 O OD1 . ASP B 448 ? 0.1493 0.2456 0.1845 0.0161  -0.0052 -0.0338 448 ASP B OD1 
7820 O OD2 . ASP B 448 ? 0.1984 0.2837 0.2269 0.0152  -0.0055 -0.0237 448 ASP B OD2 
7821 N N   . TRP B 449 ? 0.1288 0.2704 0.1558 0.0148  -0.0111 -0.0155 449 TRP B N   
7822 C CA  . TRP B 449 ? 0.1364 0.2954 0.1598 0.0133  -0.0136 -0.0103 449 TRP B CA  
7823 C C   . TRP B 449 ? 0.1477 0.3011 0.1695 0.0177  -0.0167 -0.0001 449 TRP B C   
7824 O O   . TRP B 449 ? 0.1439 0.3005 0.1598 0.0167  -0.0197 0.0094  449 TRP B O   
7825 C CB  . TRP B 449 ? 0.1457 0.3233 0.1723 0.0118  -0.0138 -0.0192 449 TRP B CB  
7826 C CG  . TRP B 449 ? 0.1030 0.2796 0.1326 0.0100  -0.0116 -0.0315 449 TRP B CG  
7827 C CD1 . TRP B 449 ? 0.1076 0.2800 0.1427 0.0101  -0.0115 -0.0405 449 TRP B CD1 
7828 C CD2 . TRP B 449 ? 0.1059 0.2861 0.1333 0.0083  -0.0100 -0.0359 449 TRP B CD2 
7829 N NE1 . TRP B 449 ? 0.1326 0.3021 0.1685 0.0094  -0.0105 -0.0503 449 TRP B NE1 
7830 C CE2 . TRP B 449 ? 0.1162 0.2919 0.1479 0.0091  -0.0093 -0.0482 449 TRP B CE2 
7831 C CE3 . TRP B 449 ? 0.1106 0.2983 0.1329 0.0058  -0.0094 -0.0302 449 TRP B CE3 
7832 C CZ2 . TRP B 449 ? 0.1201 0.2989 0.1517 0.0096  -0.0081 -0.0560 449 TRP B CZ2 
7833 C CZ3 . TRP B 449 ? 0.1141 0.3081 0.1368 0.0051  -0.0074 -0.0377 449 TRP B CZ3 
7834 C CH2 . TRP B 449 ? 0.1505 0.3402 0.1781 0.0080  -0.0068 -0.0510 449 TRP B CH2 
7835 N N   . PHE B 450 ? 0.1402 0.2860 0.1670 0.0228  -0.0163 -0.0018 450 PHE B N   
7836 C CA  . PHE B 450 ? 0.1524 0.2947 0.1787 0.0293  -0.0193 0.0061  450 PHE B CA  
7837 C C   . PHE B 450 ? 0.1581 0.2780 0.1790 0.0325  -0.0210 0.0134  450 PHE B C   
7838 O O   . PHE B 450 ? 0.1821 0.2970 0.1994 0.0371  -0.0254 0.0220  450 PHE B O   
7839 C CB  . PHE B 450 ? 0.1479 0.2939 0.1820 0.0337  -0.0179 0.0011  450 PHE B CB  
7840 C CG  . PHE B 450 ? 0.1704 0.3353 0.2096 0.0289  -0.0171 -0.0065 450 PHE B CG  
7841 C CD1 . PHE B 450 ? 0.1620 0.3240 0.2039 0.0236  -0.0142 -0.0156 450 PHE B CD1 
7842 C CD2 . PHE B 450 ? 0.1346 0.3195 0.1757 0.0296  -0.0201 -0.0047 450 PHE B CD2 
7843 C CE1 . PHE B 450 ? 0.1306 0.3070 0.1764 0.0187  -0.0147 -0.0232 450 PHE B CE1 
7844 C CE2 . PHE B 450 ? 0.1435 0.3453 0.1887 0.0242  -0.0202 -0.0123 450 PHE B CE2 
7845 C CZ  . PHE B 450 ? 0.1014 0.2979 0.1488 0.0186  -0.0176 -0.0218 450 PHE B CZ  
7846 N N   . TRP B 451 ? 0.1915 0.2970 0.2115 0.0300  -0.0184 0.0101  451 TRP B N   
7847 C CA  . TRP B 451 ? 0.1558 0.2392 0.1700 0.0315  -0.0204 0.0160  451 TRP B CA  
7848 C C   . TRP B 451 ? 0.1875 0.2702 0.1943 0.0265  -0.0246 0.0260  451 TRP B C   
7849 O O   . TRP B 451 ? 0.1944 0.2615 0.1958 0.0296  -0.0294 0.0344  451 TRP B O   
7850 C CB  . TRP B 451 ? 0.1978 0.2708 0.2130 0.0283  -0.0168 0.0098  451 TRP B CB  
7851 C CG  . TRP B 451 ? 0.2148 0.2667 0.2240 0.0272  -0.0187 0.0142  451 TRP B CG  
7852 C CD1 . TRP B 451 ? 0.2107 0.2607 0.2158 0.0194  -0.0196 0.0176  451 TRP B CD1 
7853 C CD2 . TRP B 451 ? 0.2176 0.2487 0.2244 0.0336  -0.0202 0.0147  451 TRP B CD2 
7854 N NE1 . TRP B 451 ? 0.2402 0.2680 0.2406 0.0196  -0.0220 0.0206  451 TRP B NE1 
7855 C CE2 . TRP B 451 ? 0.2873 0.3023 0.2881 0.0287  -0.0225 0.0184  451 TRP B CE2 
7856 C CE3 . TRP B 451 ? 0.2199 0.2463 0.2289 0.0430  -0.0198 0.0119  451 TRP B CE3 
7857 C CZ2 . TRP B 451 ? 0.2675 0.2591 0.2636 0.0331  -0.0250 0.0187  451 TRP B CZ2 
7858 C CZ3 . TRP B 451 ? 0.2674 0.2727 0.2720 0.0485  -0.0217 0.0118  451 TRP B CZ3 
7859 C CH2 . TRP B 451 ? 0.2551 0.2418 0.2528 0.0435  -0.0245 0.0149  451 TRP B CH2 
7860 N N   . TRP B 452 ? 0.1636 0.2635 0.1695 0.0186  -0.0231 0.0252  452 TRP B N   
7861 C CA  . TRP B 452 ? 0.1782 0.2815 0.1768 0.0115  -0.0263 0.0353  452 TRP B CA  
7862 C C   . TRP B 452 ? 0.2343 0.3488 0.2293 0.0125  -0.0308 0.0439  452 TRP B C   
7863 O O   . TRP B 452 ? 0.2347 0.3457 0.2220 0.0076  -0.0353 0.0556  452 TRP B O   
7864 C CB  . TRP B 452 ? 0.1855 0.3074 0.1845 0.0033  -0.0225 0.0304  452 TRP B CB  
7865 C CG  . TRP B 452 ? 0.1606 0.2720 0.1626 0.0022  -0.0192 0.0235  452 TRP B CG  
7866 C CD1 . TRP B 452 ? 0.1527 0.2706 0.1610 0.0037  -0.0149 0.0114  452 TRP B CD1 
7867 C CD2 . TRP B 452 ? 0.2155 0.3066 0.2141 -0.0004 -0.0208 0.0283  452 TRP B CD2 
7868 N NE1 . TRP B 452 ? 0.1705 0.2750 0.1798 0.0028  -0.0135 0.0090  452 TRP B NE1 
7869 C CE2 . TRP B 452 ? 0.1888 0.2777 0.1922 0.0000  -0.0169 0.0188  452 TRP B CE2 
7870 C CE3 . TRP B 452 ? 0.2506 0.3239 0.2421 -0.0032 -0.0260 0.0397  452 TRP B CE3 
7871 C CZ2 . TRP B 452 ? 0.2058 0.2781 0.2075 -0.0025 -0.0176 0.0201  452 TRP B CZ2 
7872 C CZ3 . TRP B 452 ? 0.2663 0.3211 0.2558 -0.0062 -0.0269 0.0404  452 TRP B CZ3 
7873 C CH2 . TRP B 452 ? 0.2551 0.3112 0.2499 -0.0059 -0.0225 0.0306  452 TRP B CH2 
7874 N N   . GLN B 453 ? 0.1806 0.3084 0.1807 0.0180  -0.0302 0.0390  453 GLN B N   
7875 C CA  . GLN B 453 ? 0.2080 0.3506 0.2054 0.0193  -0.0345 0.0462  453 GLN B CA  
7876 C C   . GLN B 453 ? 0.2295 0.3532 0.2242 0.0274  -0.0407 0.0559  453 GLN B C   
7877 O O   . GLN B 453 ? 0.2620 0.3682 0.2602 0.0352  -0.0403 0.0522  453 GLN B O   
7878 C CB  . GLN B 453 ? 0.1884 0.3525 0.1931 0.0219  -0.0321 0.0364  453 GLN B CB  
7879 C CG  . GLN B 453 ? 0.2294 0.4084 0.2334 0.0257  -0.0370 0.0426  453 GLN B CG  
7880 C CD  . GLN B 453 ? 0.2384 0.4367 0.2347 0.0185  -0.0395 0.0496  453 GLN B CD  
7881 O OE1 . GLN B 453 ? 0.2439 0.4429 0.2345 0.0106  -0.0381 0.0522  453 GLN B OE1 
7882 N NE2 . GLN B 453 ? 0.2563 0.4733 0.2524 0.0208  -0.0433 0.0528  453 GLN B NE2 
7883 N N   . GLY B 454 ? 0.3150 0.4422 0.3027 0.0260  -0.0468 0.0682  454 GLY B N   
7884 C CA  . GLY B 454 ? 0.3915 0.5003 0.3765 0.0355  -0.0540 0.0772  454 GLY B CA  
7885 C C   . GLY B 454 ? 0.4527 0.5278 0.4330 0.0369  -0.0569 0.0813  454 GLY B C   
7886 O O   . GLY B 454 ? 0.3961 0.4526 0.3779 0.0486  -0.0602 0.0806  454 GLY B O   
7887 N N   . GLU B 455 ? 0.4647 0.5328 0.4395 0.0256  -0.0559 0.0845  455 GLU B N   
7888 C CA  . GLU B 455 ? 0.5301 0.5668 0.4989 0.0236  -0.0597 0.0896  455 GLU B CA  
7889 C C   . GLU B 455 ? 0.5909 0.6238 0.5492 0.0120  -0.0660 0.1055  455 GLU B C   
7890 O O   . GLU B 455 ? 0.5465 0.6043 0.5025 0.0051  -0.0658 0.1112  455 GLU B O   
7891 C CB  . GLU B 455 ? 0.5287 0.5617 0.5012 0.0188  -0.0529 0.0790  455 GLU B CB  
7892 C CG  . GLU B 455 ? 0.5267 0.5663 0.5091 0.0276  -0.0463 0.0644  455 GLU B CG  
7893 C CD  . GLU B 455 ? 0.5645 0.5821 0.5479 0.0407  -0.0491 0.0618  455 GLU B CD  
7894 O OE1 . GLU B 455 ? 0.5909 0.5820 0.5670 0.0425  -0.0557 0.0688  455 GLU B OE1 
7895 O OE2 . GLU B 455 ? 0.4961 0.5229 0.4871 0.0489  -0.0449 0.0525  455 GLU B OE2 
7896 N N   . GLU B 456 ? 0.6529 0.6547 0.6042 0.0091  -0.0719 0.1127  456 GLU B N   
7897 C CA  . GLU B 456 ? 0.7174 0.7138 0.6583 -0.0046 -0.0783 0.1290  456 GLU B CA  
7898 C C   . GLU B 456 ? 0.6472 0.6730 0.5891 -0.0195 -0.0712 0.1277  456 GLU B C   
7899 O O   . GLU B 456 ? 0.6214 0.6550 0.5699 -0.0205 -0.0635 0.1152  456 GLU B O   
7900 C CB  . GLU B 456 ? 0.7688 0.7248 0.7025 -0.0067 -0.0858 0.1351  456 GLU B CB  
7901 C CG  . GLU B 456 ? 0.8857 0.8121 0.8123 0.0027  -0.0976 0.1456  456 GLU B CG  
7902 C CD  . GLU B 456 ? 1.0049 0.9468 0.9266 -0.0012 -0.1011 0.1579  456 GLU B CD  
7903 O OE1 . GLU B 456 ? 1.0413 0.9942 0.9665 0.0114  -0.1022 0.1565  456 GLU B OE1 
7904 O OE2 . GLU B 456 ? 1.0630 1.0083 0.9783 -0.0169 -0.1020 0.1675  456 GLU B OE2 
7905 N N   . LYS B 457 ? 0.5091 0.5527 0.4440 -0.0304 -0.0740 0.1407  457 LYS B N   
7906 C CA  . LYS B 457 ? 0.4980 0.5764 0.4339 -0.0429 -0.0669 0.1388  457 LYS B CA  
7907 C C   . LYS B 457 ? 0.5288 0.6000 0.4655 -0.0527 -0.0641 0.1363  457 LYS B C   
7908 O O   . LYS B 457 ? 0.6092 0.6552 0.5389 -0.0606 -0.0708 0.1474  457 LYS B O   
7909 C CB  . LYS B 457 ? 0.5578 0.6549 0.4840 -0.0542 -0.0714 0.1555  457 LYS B CB  
7910 C CG  . LYS B 457 ? 0.6205 0.7618 0.5494 -0.0623 -0.0629 0.1495  457 LYS B CG  
7911 C CD  . LYS B 457 ? 0.7250 0.8848 0.6504 -0.0686 -0.0644 0.1580  457 LYS B CD  
7912 C CE  . LYS B 457 ? 0.7425 0.9474 0.6720 -0.0728 -0.0557 0.1485  457 LYS B CE  
7913 N NZ  . LYS B 457 ? 0.7542 0.9759 0.6861 -0.0842 -0.0503 0.1455  457 LYS B NZ  
7914 N N   . ALA B 458 ? 0.4655 0.5581 0.4107 -0.0521 -0.0549 0.1215  458 ALA B N   
7915 C CA  . ALA B 458 ? 0.4869 0.5798 0.4348 -0.0602 -0.0513 0.1170  458 ALA B CA  
7916 C C   . ALA B 458 ? 0.4564 0.5912 0.4075 -0.0676 -0.0440 0.1119  458 ALA B C   
7917 O O   . ALA B 458 ? 0.4379 0.5978 0.3914 -0.0627 -0.0402 0.1058  458 ALA B O   
7918 C CB  . ALA B 458 ? 0.4757 0.5503 0.4316 -0.0491 -0.0477 0.1018  458 ALA B CB  
7919 N N   . PRO B 459 ? 0.3852 0.5300 0.3364 -0.0792 -0.0421 0.1139  459 PRO B N   
7920 C CA  . PRO B 459 ? 0.3940 0.5817 0.3488 -0.0845 -0.0349 0.1077  459 PRO B CA  
7921 C C   . PRO B 459 ? 0.3737 0.5731 0.3388 -0.0715 -0.0277 0.0871  459 PRO B C   
7922 O O   . PRO B 459 ? 0.3599 0.5365 0.3307 -0.0628 -0.0268 0.0776  459 PRO B O   
7923 C CB  . PRO B 459 ? 0.4558 0.6475 0.4104 -0.0980 -0.0350 0.1130  459 PRO B CB  
7924 C CG  . PRO B 459 ? 0.4515 0.5995 0.4030 -0.0989 -0.0419 0.1193  459 PRO B CG  
7925 C CD  . PRO B 459 ? 0.4468 0.5668 0.3934 -0.0894 -0.0477 0.1240  459 PRO B CD  
7926 N N   . PHE B 460 ? 0.3474 0.5815 0.3138 -0.0704 -0.0231 0.0806  460 PHE B N   
7927 C CA  . PHE B 460 ? 0.3535 0.6028 0.3283 -0.0598 -0.0170 0.0613  460 PHE B CA  
7928 C C   . PHE B 460 ? 0.3227 0.5546 0.3005 -0.0475 -0.0179 0.0540  460 PHE B C   
7929 O O   . PHE B 460 ? 0.2899 0.5308 0.2742 -0.0396 -0.0139 0.0386  460 PHE B O   
7930 C CB  . PHE B 460 ? 0.3426 0.5893 0.3256 -0.0576 -0.0131 0.0502  460 PHE B CB  
7931 C CG  . PHE B 460 ? 0.3956 0.6652 0.3778 -0.0692 -0.0116 0.0554  460 PHE B CG  
7932 C CD1 . PHE B 460 ? 0.4291 0.7405 0.4109 -0.0729 -0.0075 0.0520  460 PHE B CD1 
7933 C CD2 . PHE B 460 ? 0.4261 0.6777 0.4079 -0.0767 -0.0144 0.0632  460 PHE B CD2 
7934 C CE1 . PHE B 460 ? 0.4602 0.7978 0.4420 -0.0840 -0.0057 0.0571  460 PHE B CE1 
7935 C CE2 . PHE B 460 ? 0.4588 0.7347 0.4406 -0.0888 -0.0131 0.0686  460 PHE B CE2 
7936 C CZ  . PHE B 460 ? 0.4475 0.7678 0.4297 -0.0924 -0.0085 0.0658  460 PHE B CZ  
7937 N N   . VAL B 461 ? 0.4021 0.6103 0.3754 -0.0456 -0.0235 0.0644  461 VAL B N   
7938 C CA  . VAL B 461 ? 0.4119 0.6100 0.3888 -0.0343 -0.0241 0.0576  461 VAL B CA  
7939 C C   . VAL B 461 ? 0.3852 0.6135 0.3618 -0.0329 -0.0223 0.0519  461 VAL B C   
7940 O O   . VAL B 461 ? 0.3750 0.6043 0.3572 -0.0247 -0.0207 0.0405  461 VAL B O   
7941 C CB  . VAL B 461 ? 0.4859 0.6555 0.4581 -0.0314 -0.0309 0.0701  461 VAL B CB  
7942 C CG1 . VAL B 461 ? 0.4395 0.6043 0.4160 -0.0199 -0.0316 0.0639  461 VAL B CG1 
7943 C CG2 . VAL B 461 ? 0.5167 0.6555 0.4891 -0.0318 -0.0327 0.0722  461 VAL B CG2 
7944 N N   . GLU B 462 ? 0.2487 0.5031 0.2185 -0.0415 -0.0227 0.0597  462 GLU B N   
7945 C CA  . GLU B 462 ? 0.2850 0.5715 0.2536 -0.0405 -0.0206 0.0523  462 GLU B CA  
7946 C C   . GLU B 462 ? 0.2641 0.5630 0.2407 -0.0349 -0.0147 0.0319  462 GLU B C   
7947 O O   . GLU B 462 ? 0.2544 0.5699 0.2322 -0.0306 -0.0137 0.0212  462 GLU B O   
7948 C CB  . GLU B 462 ? 0.3996 0.7154 0.3593 -0.0517 -0.0209 0.0632  462 GLU B CB  
7949 C CG  . GLU B 462 ? 0.5375 0.8401 0.4903 -0.0572 -0.0272 0.0831  462 GLU B CG  
7950 C CD  . GLU B 462 ? 0.6062 0.8923 0.5548 -0.0670 -0.0301 0.0974  462 GLU B CD  
7951 O OE1 . GLU B 462 ? 0.4761 0.7520 0.4284 -0.0670 -0.0278 0.0917  462 GLU B OE1 
7952 O OE2 . GLU B 462 ? 0.6732 0.9543 0.6170 -0.0747 -0.0348 0.1129  462 GLU B OE2 
7953 N N   . VAL B 463 ? 0.2048 0.4958 0.1866 -0.0349 -0.0116 0.0261  463 VAL B N   
7954 C CA  . VAL B 463 ? 0.1741 0.4750 0.1631 -0.0287 -0.0071 0.0071  463 VAL B CA  
7955 C C   . VAL B 463 ? 0.1604 0.4381 0.1560 -0.0196 -0.0077 -0.0025 463 VAL B C   
7956 O O   . VAL B 463 ? 0.1637 0.4510 0.1626 -0.0146 -0.0064 -0.0166 463 VAL B O   
7957 C CB  . VAL B 463 ? 0.1762 0.4785 0.1690 -0.0312 -0.0041 0.0045  463 VAL B CB  
7958 C CG1 . VAL B 463 ? 0.2413 0.5551 0.2410 -0.0235 -0.0004 -0.0151 463 VAL B CG1 
7959 C CG2 . VAL B 463 ? 0.1695 0.4976 0.1559 -0.0422 -0.0035 0.0157  463 VAL B CG2 
7960 N N   . PHE B 464 ? 0.1556 0.4028 0.1528 -0.0176 -0.0100 0.0044  464 PHE B N   
7961 C CA  . PHE B 464 ? 0.1449 0.3737 0.1478 -0.0100 -0.0105 -0.0029 464 PHE B CA  
7962 C C   . PHE B 464 ? 0.1470 0.3882 0.1486 -0.0082 -0.0126 -0.0040 464 PHE B C   
7963 O O   . PHE B 464 ? 0.1441 0.3854 0.1507 -0.0040 -0.0121 -0.0153 464 PHE B O   
7964 C CB  . PHE B 464 ? 0.1482 0.3466 0.1516 -0.0080 -0.0126 0.0057  464 PHE B CB  
7965 C CG  . PHE B 464 ? 0.1226 0.3065 0.1285 -0.0089 -0.0108 0.0040  464 PHE B CG  
7966 C CD1 . PHE B 464 ? 0.1483 0.3206 0.1607 -0.0036 -0.0086 -0.0070 464 PHE B CD1 
7967 C CD2 . PHE B 464 ? 0.1492 0.3321 0.1505 -0.0157 -0.0118 0.0138  464 PHE B CD2 
7968 C CE1 . PHE B 464 ? 0.1426 0.3027 0.1570 -0.0041 -0.0074 -0.0084 464 PHE B CE1 
7969 C CE2 . PHE B 464 ? 0.1595 0.3304 0.1633 -0.0169 -0.0105 0.0119  464 PHE B CE2 
7970 C CZ  . PHE B 464 ? 0.1691 0.3296 0.1795 -0.0105 -0.0083 0.0005  464 PHE B CZ  
7971 N N   . ASP B 465 ? 0.1521 0.4035 0.1467 -0.0120 -0.0156 0.0084  465 ASP B N   
7972 C CA  . ASP B 465 ? 0.1379 0.4040 0.1308 -0.0105 -0.0182 0.0083  465 ASP B CA  
7973 C C   . ASP B 465 ? 0.1405 0.4342 0.1332 -0.0115 -0.0160 -0.0054 465 ASP B C   
7974 O O   . ASP B 465 ? 0.1767 0.4759 0.1724 -0.0084 -0.0171 -0.0145 465 ASP B O   
7975 C CB  . ASP B 465 ? 0.1552 0.4267 0.1395 -0.0147 -0.0227 0.0257  465 ASP B CB  
7976 C CG  . ASP B 465 ? 0.2149 0.5051 0.1967 -0.0135 -0.0259 0.0266  465 ASP B CG  
7977 O OD1 . ASP B 465 ? 0.1730 0.4522 0.1589 -0.0075 -0.0287 0.0274  465 ASP B OD1 
7978 O OD2 . ASP B 465 ? 0.2364 0.5530 0.2127 -0.0183 -0.0251 0.0260  465 ASP B OD2 
7979 N N   . LYS B 466 ? 0.1374 0.4498 0.1264 -0.0158 -0.0132 -0.0075 466 LYS B N   
7980 C CA  . LYS B 466 ? 0.1373 0.4733 0.1269 -0.0149 -0.0100 -0.0225 466 LYS B CA  
7981 C C   . LYS B 466 ? 0.1455 0.4696 0.1427 -0.0085 -0.0093 -0.0403 466 LYS B C   
7982 O O   . LYS B 466 ? 0.1672 0.4964 0.1667 -0.0058 -0.0086 -0.0519 466 LYS B O   
7983 C CB  . LYS B 466 ? 0.1526 0.5082 0.1405 -0.0194 -0.0056 -0.0214 466 LYS B CB  
7984 C CG  . LYS B 466 ? 0.1682 0.5450 0.1617 -0.0163 -0.0017 -0.0375 466 LYS B CG  
7985 C CD  . LYS B 466 ? 0.3059 0.7091 0.3011 -0.0214 0.0008  -0.0341 466 LYS B CD  
7986 C CE  . LYS B 466 ? 0.4336 0.8566 0.4374 -0.0160 0.0019  -0.0520 466 LYS B CE  
7987 N NZ  . LYS B 466 ? 0.5024 0.9438 0.5061 -0.0157 0.0018  -0.0564 466 LYS B NZ  
7988 N N   . LEU B 467 ? 0.1232 0.4249 0.1259 -0.0061 -0.0081 -0.0412 467 LEU B N   
7989 C CA  . LEU B 467 ? 0.1469 0.4331 0.1568 -0.0006 -0.0076 -0.0558 467 LEU B CA  
7990 C C   . LEU B 467 ? 0.1171 0.3905 0.1303 0.0010  -0.0106 -0.0576 467 LEU B C   
7991 O O   . LEU B 467 ? 0.1409 0.4173 0.1565 0.0028  -0.0119 -0.0709 467 LEU B O   
7992 C CB  . LEU B 467 ? 0.1546 0.4185 0.1691 0.0011  -0.0059 -0.0537 467 LEU B CB  
7993 C CG  . LEU B 467 ? 0.1493 0.4271 0.1636 0.0007  -0.0030 -0.0573 467 LEU B CG  
7994 C CD1 . LEU B 467 ? 0.1340 0.3906 0.1515 0.0005  -0.0021 -0.0506 467 LEU B CD1 
7995 C CD2 . LEU B 467 ? 0.1463 0.4341 0.1637 0.0065  -0.0024 -0.0764 467 LEU B CD2 
7996 N N   . PHE B 468 ? 0.1307 0.3904 0.1442 0.0005  -0.0120 -0.0447 468 PHE B N   
7997 C CA  . PHE B 468 ? 0.1142 0.3663 0.1318 0.0020  -0.0145 -0.0456 468 PHE B CA  
7998 C C   . PHE B 468 ? 0.1406 0.4155 0.1559 0.0003  -0.0170 -0.0522 468 PHE B C   
7999 O O   . PHE B 468 ? 0.1571 0.4305 0.1765 0.0004  -0.0186 -0.0630 468 PHE B O   
8000 C CB  . PHE B 468 ? 0.1149 0.3559 0.1319 0.0029  -0.0160 -0.0304 468 PHE B CB  
8001 C CG  . PHE B 468 ? 0.1436 0.3846 0.1648 0.0048  -0.0186 -0.0299 468 PHE B CG  
8002 C CD1 . PHE B 468 ? 0.1137 0.3406 0.1421 0.0063  -0.0179 -0.0361 468 PHE B CD1 
8003 C CD2 . PHE B 468 ? 0.1428 0.4004 0.1609 0.0045  -0.0220 -0.0228 468 PHE B CD2 
8004 C CE1 . PHE B 468 ? 0.1096 0.3400 0.1428 0.0071  -0.0200 -0.0353 468 PHE B CE1 
8005 C CE2 . PHE B 468 ? 0.1556 0.4164 0.1786 0.0065  -0.0245 -0.0223 468 PHE B CE2 
8006 C CZ  . PHE B 468 ? 0.1307 0.3793 0.1618 0.0075  -0.0233 -0.0289 468 PHE B CZ  
8007 N N   . ARG B 469 ? 0.1375 0.4341 0.1455 -0.0023 -0.0178 -0.0457 469 ARG B N   
8008 C CA  . ARG B 469 ? 0.1327 0.4444 0.1377 -0.0036 -0.0179 -0.0493 469 ARG B CA  
8009 C C   . ARG B 469 ? 0.1371 0.4560 0.1429 -0.0029 -0.0152 -0.0662 469 ARG B C   
8010 O O   . ARG B 469 ? 0.1752 0.4997 0.1821 -0.0033 -0.0162 -0.0740 469 ARG B O   
8011 C CB  . ARG B 469 ? 0.1403 0.4685 0.1376 -0.0066 -0.0181 -0.0356 469 ARG B CB  
8012 C CG  . ARG B 469 ? 0.1634 0.4824 0.1606 -0.0055 -0.0225 -0.0194 469 ARG B CG  
8013 C CD  . ARG B 469 ? 0.1727 0.5034 0.1616 -0.0089 -0.0237 -0.0043 469 ARG B CD  
8014 N NE  . ARG B 469 ? 0.1817 0.5009 0.1697 -0.0064 -0.0290 0.0114  469 ARG B NE  
8015 C CZ  . ARG B 469 ? 0.2049 0.5270 0.1938 -0.0036 -0.0325 0.0164  469 ARG B CZ  
8016 N NH1 . ARG B 469 ? 0.1719 0.5083 0.1624 -0.0042 -0.0314 0.0072  469 ARG B NH1 
8017 N NH2 . ARG B 469 ? 0.2354 0.5457 0.2235 0.0003  -0.0375 0.0305  469 ARG B NH2 
8018 N N   . SER B 470 ? 0.1359 0.4556 0.1423 -0.0014 -0.0122 -0.0719 470 SER B N   
8019 C CA  . SER B 470 ? 0.1592 0.4836 0.1691 0.0016  -0.0106 -0.0886 470 SER B CA  
8020 C C   . SER B 470 ? 0.1597 0.4618 0.1756 0.0039  -0.0135 -0.1000 470 SER B C   
8021 O O   . SER B 470 ? 0.1773 0.4801 0.1955 0.0050  -0.0149 -0.1119 470 SER B O   
8022 C CB  . SER B 470 ? 0.1811 0.5133 0.1923 0.0036  -0.0073 -0.0911 470 SER B CB  
8023 O OG  . SER B 470 ? 0.2827 0.6371 0.2890 -0.0005 -0.0050 -0.0798 470 SER B OG  
8024 N N   . PHE B 471 ? 0.1429 0.4246 0.1618 0.0041  -0.0151 -0.0962 471 PHE B N   
8025 C CA  . PHE B 471 ? 0.1571 0.4175 0.1817 0.0045  -0.0181 -0.1050 471 PHE B CA  
8026 C C   . PHE B 471 ? 0.1684 0.4308 0.1940 0.0006  -0.0211 -0.1039 471 PHE B C   
8027 O O   . PHE B 471 ? 0.1810 0.4346 0.2095 -0.0007 -0.0236 -0.1140 471 PHE B O   
8028 C CB  . PHE B 471 ? 0.1498 0.3897 0.1786 0.0051  -0.0183 -0.0991 471 PHE B CB  
8029 C CG  . PHE B 471 ? 0.1470 0.3810 0.1757 0.0090  -0.0153 -0.1004 471 PHE B CG  
8030 C CD1 . PHE B 471 ? 0.1478 0.3835 0.1771 0.0132  -0.0154 -0.1145 471 PHE B CD1 
8031 C CD2 . PHE B 471 ? 0.1498 0.3755 0.1787 0.0090  -0.0124 -0.0872 471 PHE B CD2 
8032 C CE1 . PHE B 471 ? 0.1689 0.4024 0.1992 0.0173  -0.0131 -0.1159 471 PHE B CE1 
8033 C CE2 . PHE B 471 ? 0.1578 0.3799 0.1873 0.0117  -0.0100 -0.0883 471 PHE B CE2 
8034 C CZ  . PHE B 471 ? 0.1582 0.3861 0.1885 0.0159  -0.0103 -0.1027 471 PHE B CZ  
8035 N N   . VAL B 472 ? 0.1757 0.4494 0.1990 -0.0015 -0.0212 -0.0912 472 VAL B N   
8036 C CA  . VAL B 472 ? 0.1491 0.4285 0.1734 -0.0047 -0.0238 -0.0892 472 VAL B CA  
8037 C C   . VAL B 472 ? 0.1496 0.4419 0.1707 -0.0059 -0.0241 -0.0991 472 VAL B C   
8038 O O   . VAL B 472 ? 0.1693 0.4586 0.1931 -0.0090 -0.0271 -0.1056 472 VAL B O   
8039 C CB  . VAL B 472 ? 0.1889 0.4780 0.2112 -0.0045 -0.0241 -0.0730 472 VAL B CB  
8040 C CG1 . VAL B 472 ? 0.2586 0.5609 0.2801 -0.0070 -0.0263 -0.0714 472 VAL B CG1 
8041 C CG2 . VAL B 472 ? 0.1840 0.4586 0.2129 -0.0028 -0.0249 -0.0649 472 VAL B CG2 
8042 N N   . ARG B 473 ? 0.1534 0.4618 0.1693 -0.0040 -0.0212 -0.1001 473 ARG B N   
8043 C CA  . ARG B 473 ? 0.1886 0.5120 0.2025 -0.0043 -0.0213 -0.1099 473 ARG B CA  
8044 C C   . ARG B 473 ? 0.2135 0.5223 0.2317 -0.0024 -0.0233 -0.1264 473 ARG B C   
8045 O O   . ARG B 473 ? 0.2014 0.5092 0.2200 -0.0046 -0.0266 -0.1349 473 ARG B O   
8046 C CB  . ARG B 473 ? 0.1797 0.5255 0.1889 -0.0029 -0.0173 -0.1066 473 ARG B CB  
8047 C CG  . ARG B 473 ? 0.4605 0.8276 0.4677 -0.0033 -0.0173 -0.1144 473 ARG B CG  
8048 C CD  . ARG B 473 ? 0.6990 1.0923 0.7018 -0.0040 -0.0136 -0.1065 473 ARG B CD  
8049 N NE  . ARG B 473 ? 0.8276 1.2294 0.8336 -0.0002 -0.0109 -0.1153 473 ARG B NE  
8050 C CZ  . ARG B 473 ? 0.9157 1.3419 0.9219 0.0008  -0.0098 -0.1223 473 ARG B CZ  
8051 N NH1 . ARG B 473 ? 0.9548 1.3981 0.9570 -0.0021 -0.0107 -0.1216 473 ARG B NH1 
8052 N NH2 . ARG B 473 ? 0.9297 1.3646 0.9404 0.0051  -0.0081 -0.1300 473 ARG B NH2 
8053 N N   . ARG B 474 ? 0.2145 0.5101 0.2356 0.0017  -0.0220 -0.1304 474 ARG B N   
8054 C CA  . ARG B 474 ? 0.2231 0.5022 0.2480 0.0050  -0.0246 -0.1448 474 ARG B CA  
8055 C C   . ARG B 474 ? 0.2336 0.4891 0.2613 0.0005  -0.0296 -0.1477 474 ARG B C   
8056 O O   . ARG B 474 ? 0.2295 0.4730 0.2580 0.0005  -0.0337 -0.1590 474 ARG B O   
8057 C CB  . ARG B 474 ? 0.2567 0.5274 0.2844 0.0107  -0.0224 -0.1461 474 ARG B CB  
8058 C CG  . ARG B 474 ? 0.3291 0.5801 0.3608 0.0157  -0.0257 -0.1592 474 ARG B CG  
8059 C CD  . ARG B 474 ? 0.4570 0.7233 0.4883 0.0205  -0.0264 -0.1709 474 ARG B CD  
8060 N NE  . ARG B 474 ? 0.5921 0.8372 0.6266 0.0265  -0.0305 -0.1825 474 ARG B NE  
8061 C CZ  . ARG B 474 ? 0.7199 0.9407 0.7538 0.0245  -0.0363 -0.1894 474 ARG B CZ  
8062 N NH1 . ARG B 474 ? 0.6791 0.8963 0.7103 0.0161  -0.0384 -0.1865 474 ARG B NH1 
8063 N NH2 . ARG B 474 ? 0.7926 0.9928 0.8283 0.0305  -0.0404 -0.1987 474 ARG B NH2 
8064 N N   . ALA B 475 ? 0.2244 0.4737 0.2538 -0.0038 -0.0299 -0.1371 475 ALA B N   
8065 C CA  . ALA B 475 ? 0.2272 0.4586 0.2605 -0.0098 -0.0344 -0.1379 475 ALA B CA  
8066 C C   . ALA B 475 ? 0.2947 0.5340 0.3266 -0.0152 -0.0382 -0.1424 475 ALA B C   
8067 O O   . ALA B 475 ? 0.2915 0.5151 0.3261 -0.0209 -0.0430 -0.1465 475 ALA B O   
8068 C CB  . ALA B 475 ? 0.2032 0.4340 0.2399 -0.0127 -0.0335 -0.1246 475 ALA B CB  
8069 N N   . GLN B 476 ? 0.2411 0.5046 0.2687 -0.0143 -0.0364 -0.1408 476 GLN B N   
8070 C CA  . GLN B 476 ? 0.3070 0.5809 0.3330 -0.0195 -0.0398 -0.1440 476 GLN B CA  
8071 C C   . GLN B 476 ? 0.3658 0.6419 0.3882 -0.0172 -0.0417 -0.1584 476 GLN B C   
8072 O O   . GLN B 476 ? 0.3554 0.6400 0.3756 -0.0214 -0.0451 -0.1628 476 GLN B O   
8073 C CB  . GLN B 476 ? 0.2565 0.5557 0.2797 -0.0202 -0.0374 -0.1323 476 GLN B CB  
8074 C CG  . GLN B 476 ? 0.2584 0.5553 0.2854 -0.0212 -0.0364 -0.1181 476 GLN B CG  
8075 C CD  . GLN B 476 ? 0.3188 0.6371 0.3422 -0.0199 -0.0346 -0.1055 476 GLN B CD  
8076 O OE1 . GLN B 476 ? 0.3155 0.6466 0.3386 -0.0230 -0.0369 -0.1030 476 GLN B OE1 
8077 N NE2 . GLN B 476 ? 0.2691 0.5905 0.2895 -0.0154 -0.0311 -0.0970 476 GLN B NE2 
8078 N N   . GLU B 477 ? 0.4137 0.6830 0.4360 -0.0103 -0.0401 -0.1659 477 GLU B N   
8079 C CA  . GLU B 477 ? 0.5584 0.8312 0.5780 -0.0062 -0.0418 -0.1801 477 GLU B CA  
8080 C C   . GLU B 477 ? 0.6458 0.8875 0.6668 -0.0058 -0.0477 -0.1912 477 GLU B C   
8081 O O   . GLU B 477 ? 0.6427 0.8614 0.6670 -0.0067 -0.0488 -0.1876 477 GLU B O   
8082 C CB  . GLU B 477 ? 0.6042 0.8949 0.6235 0.0020  -0.0363 -0.1809 477 GLU B CB  
8083 C CG  . GLU B 477 ? 0.6656 0.9856 0.6821 0.0008  -0.0311 -0.1688 477 GLU B CG  
8084 C CD  . GLU B 477 ? 0.6899 1.0301 0.7065 0.0069  -0.0263 -0.1696 477 GLU B CD  
8085 O OE1 . GLU B 477 ? 0.7069 1.0362 0.7273 0.0127  -0.0259 -0.1753 477 GLU B OE1 
8086 O OE2 . GLU B 477 ? 0.7057 1.0734 0.7187 0.0055  -0.0232 -0.1637 477 GLU B OE2 
# 
