data_9IHW
# 
_entry.id   9IHW 
# 
_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   9IHW         pdb_00009ihw 10.2210/pdb9ihw/pdb 
WWPDB D_1300048777 ?            ?                   
# 
_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                        9IHW 
_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 0009-0004-3840-9685 
'Wang, W.W.' 2 0000-0002-0699-3598 
'Yu, F.'     3 0000-0002-9502-3277 
# 
_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' 57252.250 2   ? D352N ? ? 
2 branched    syn 
;alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose
;
990.860   2   ? ?     ? ? 
3 non-polymer syn GLYCEROL 92.094    6   ? ?     ? ? 
4 water       nat water 18.015    617 ? ?     ? ? 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MKKLFLVFWWHMHQPLYREPYTGEYLLPWTFFHAVKDYYDMPAYLKDFEIKLNFNLTPVLIDQIQEYAQGKAKDVFLEAI
RKDPDDLEKEEVEKLIEFTKLNYEKPIYRFERIRELMNKEKLNREELLDLQTLNLLAWCGRTLRKDLKDLLNKGRNYTQE
EKEYVLNKYFEIIKKTLSIYREIKEEGKGSVSTSPYYHPLIPILLNPNCVYETTPNVKIPDFAVSFREDASKHVELAKEK
YFEIFGEHPVYMWPPEASVSNEALELYYEKGINMLATDEVILKNSVERASPYLRYYFRELISVFFRDKTLSDLIGFSYHA
WNAEDAVRDFIGRLKKIHESVDFQPVVFVVLNGENCWEYYEENGIPFLEKLYSTLEKEEWIETLTLEEAMRKEDVKTEVI
ESVKAGTWFDGNFLKWIGNKEKNEYWKILIEAKKKAKNDYILVAEGSDWFWWQGEEKAPFVEVFDKLFRSFVRRAQE
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MKKLFLVFWWHMHQPLYREPYTGEYLLPWTFFHAVKDYYDMPAYLKDFEIKLNFNLTPVLIDQIQEYAQGKAKDVFLEAI
RKDPDDLEKEEVEKLIEFTKLNYEKPIYRFERIRELMNKEKLNREELLDLQTLNLLAWCGRTLRKDLKDLLNKGRNYTQE
EKEYVLNKYFEIIKKTLSIYREIKEEGKGSVSTSPYYHPLIPILLNPNCVYETTPNVKIPDFAVSFREDASKHVELAKEK
YFEIFGEHPVYMWPPEASVSNEALELYYEKGINMLATDEVILKNSVERASPYLRYYFRELISVFFRDKTLSDLIGFSYHA
WNAEDAVRDFIGRLKKIHESVDFQPVVFVVLNGENCWEYYEENGIPFLEKLYSTLEKEEWIETLTLEEAMRKEDVKTEVI
ESVKAGTWFDGNFLKWIGNKEKNEYWKILIEAKKKAKNDYILVAEGSDWFWWQGEEKAPFVEVFDKLFRSFVRRAQE
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 GLYCEROL GOL 
4 water    HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   LYS n 
1 3   LYS n 
1 4   LEU n 
1 5   PHE n 
1 6   LEU n 
1 7   VAL n 
1 8   PHE n 
1 9   TRP n 
1 10  TRP n 
1 11  HIS n 
1 12  MET n 
1 13  HIS n 
1 14  GLN n 
1 15  PRO n 
1 16  LEU n 
1 17  TYR n 
1 18  ARG n 
1 19  GLU n 
1 20  PRO n 
1 21  TYR n 
1 22  THR n 
1 23  GLY n 
1 24  GLU n 
1 25  TYR n 
1 26  LEU n 
1 27  LEU n 
1 28  PRO n 
1 29  TRP n 
1 30  THR n 
1 31  PHE n 
1 32  PHE n 
1 33  HIS n 
1 34  ALA n 
1 35  VAL n 
1 36  LYS n 
1 37  ASP n 
1 38  TYR n 
1 39  TYR n 
1 40  ASP n 
1 41  MET n 
1 42  PRO n 
1 43  ALA n 
1 44  TYR n 
1 45  LEU n 
1 46  LYS n 
1 47  ASP n 
1 48  PHE n 
1 49  GLU n 
1 50  ILE n 
1 51  LYS n 
1 52  LEU n 
1 53  ASN n 
1 54  PHE n 
1 55  ASN n 
1 56  LEU n 
1 57  THR n 
1 58  PRO n 
1 59  VAL n 
1 60  LEU n 
1 61  ILE n 
1 62  ASP n 
1 63  GLN n 
1 64  ILE n 
1 65  GLN n 
1 66  GLU n 
1 67  TYR n 
1 68  ALA n 
1 69  GLN n 
1 70  GLY n 
1 71  LYS n 
1 72  ALA n 
1 73  LYS n 
1 74  ASP n 
1 75  VAL n 
1 76  PHE n 
1 77  LEU n 
1 78  GLU n 
1 79  ALA n 
1 80  ILE n 
1 81  ARG n 
1 82  LYS n 
1 83  ASP n 
1 84  PRO n 
1 85  ASP n 
1 86  ASP n 
1 87  LEU n 
1 88  GLU n 
1 89  LYS n 
1 90  GLU n 
1 91  GLU n 
1 92  VAL n 
1 93  GLU n 
1 94  LYS n 
1 95  LEU n 
1 96  ILE n 
1 97  GLU n 
1 98  PHE n 
1 99  THR n 
1 100 LYS n 
1 101 LEU n 
1 102 ASN n 
1 103 TYR n 
1 104 GLU n 
1 105 LYS n 
1 106 PRO n 
1 107 ILE n 
1 108 TYR n 
1 109 ARG n 
1 110 PHE n 
1 111 GLU n 
1 112 ARG n 
1 113 ILE n 
1 114 ARG n 
1 115 GLU n 
1 116 LEU n 
1 117 MET n 
1 118 ASN n 
1 119 LYS n 
1 120 GLU n 
1 121 LYS n 
1 122 LEU n 
1 123 ASN n 
1 124 ARG n 
1 125 GLU n 
1 126 GLU n 
1 127 LEU n 
1 128 LEU n 
1 129 ASP n 
1 130 LEU n 
1 131 GLN n 
1 132 THR n 
1 133 LEU n 
1 134 ASN n 
1 135 LEU n 
1 136 LEU n 
1 137 ALA n 
1 138 TRP n 
1 139 CYS n 
1 140 GLY n 
1 141 ARG n 
1 142 THR n 
1 143 LEU n 
1 144 ARG n 
1 145 LYS n 
1 146 ASP n 
1 147 LEU n 
1 148 LYS n 
1 149 ASP n 
1 150 LEU n 
1 151 LEU n 
1 152 ASN n 
1 153 LYS n 
1 154 GLY n 
1 155 ARG n 
1 156 ASN n 
1 157 TYR n 
1 158 THR n 
1 159 GLN n 
1 160 GLU n 
1 161 GLU n 
1 162 LYS n 
1 163 GLU n 
1 164 TYR n 
1 165 VAL n 
1 166 LEU n 
1 167 ASN n 
1 168 LYS n 
1 169 TYR n 
1 170 PHE n 
1 171 GLU n 
1 172 ILE n 
1 173 ILE n 
1 174 LYS n 
1 175 LYS n 
1 176 THR n 
1 177 LEU n 
1 178 SER n 
1 179 ILE n 
1 180 TYR n 
1 181 ARG n 
1 182 GLU n 
1 183 ILE n 
1 184 LYS n 
1 185 GLU n 
1 186 GLU n 
1 187 GLY n 
1 188 LYS n 
1 189 GLY n 
1 190 SER n 
1 191 VAL n 
1 192 SER n 
1 193 THR n 
1 194 SER n 
1 195 PRO n 
1 196 TYR n 
1 197 TYR n 
1 198 HIS n 
1 199 PRO n 
1 200 LEU n 
1 201 ILE n 
1 202 PRO n 
1 203 ILE n 
1 204 LEU n 
1 205 LEU n 
1 206 ASN n 
1 207 PRO n 
1 208 ASN n 
1 209 CYS n 
1 210 VAL n 
1 211 TYR n 
1 212 GLU n 
1 213 THR n 
1 214 THR n 
1 215 PRO n 
1 216 ASN n 
1 217 VAL n 
1 218 LYS n 
1 219 ILE n 
1 220 PRO n 
1 221 ASP n 
1 222 PHE n 
1 223 ALA n 
1 224 VAL n 
1 225 SER n 
1 226 PHE n 
1 227 ARG n 
1 228 GLU n 
1 229 ASP n 
1 230 ALA n 
1 231 SER n 
1 232 LYS n 
1 233 HIS n 
1 234 VAL n 
1 235 GLU n 
1 236 LEU n 
1 237 ALA n 
1 238 LYS n 
1 239 GLU n 
1 240 LYS n 
1 241 TYR n 
1 242 PHE n 
1 243 GLU n 
1 244 ILE n 
1 245 PHE n 
1 246 GLY n 
1 247 GLU n 
1 248 HIS n 
1 249 PRO n 
1 250 VAL n 
1 251 TYR n 
1 252 MET n 
1 253 TRP n 
1 254 PRO n 
1 255 PRO n 
1 256 GLU n 
1 257 ALA n 
1 258 SER n 
1 259 VAL n 
1 260 SER n 
1 261 ASN n 
1 262 GLU n 
1 263 ALA n 
1 264 LEU n 
1 265 GLU n 
1 266 LEU n 
1 267 TYR n 
1 268 TYR n 
1 269 GLU n 
1 270 LYS n 
1 271 GLY n 
1 272 ILE n 
1 273 ASN n 
1 274 MET n 
1 275 LEU n 
1 276 ALA n 
1 277 THR n 
1 278 ASP n 
1 279 GLU n 
1 280 VAL n 
1 281 ILE n 
1 282 LEU n 
1 283 LYS n 
1 284 ASN n 
1 285 SER n 
1 286 VAL n 
1 287 GLU n 
1 288 ARG n 
1 289 ALA n 
1 290 SER n 
1 291 PRO n 
1 292 TYR n 
1 293 LEU n 
1 294 ARG n 
1 295 TYR n 
1 296 TYR n 
1 297 PHE n 
1 298 ARG n 
1 299 GLU n 
1 300 LEU n 
1 301 ILE n 
1 302 SER n 
1 303 VAL n 
1 304 PHE n 
1 305 PHE n 
1 306 ARG n 
1 307 ASP n 
1 308 LYS n 
1 309 THR n 
1 310 LEU n 
1 311 SER n 
1 312 ASP n 
1 313 LEU n 
1 314 ILE n 
1 315 GLY n 
1 316 PHE n 
1 317 SER n 
1 318 TYR n 
1 319 HIS n 
1 320 ALA n 
1 321 TRP n 
1 322 ASN n 
1 323 ALA n 
1 324 GLU n 
1 325 ASP n 
1 326 ALA n 
1 327 VAL n 
1 328 ARG n 
1 329 ASP n 
1 330 PHE n 
1 331 ILE n 
1 332 GLY n 
1 333 ARG n 
1 334 LEU n 
1 335 LYS n 
1 336 LYS n 
1 337 ILE n 
1 338 HIS n 
1 339 GLU n 
1 340 SER n 
1 341 VAL n 
1 342 ASP n 
1 343 PHE n 
1 344 GLN n 
1 345 PRO n 
1 346 VAL n 
1 347 VAL n 
1 348 PHE n 
1 349 VAL n 
1 350 VAL n 
1 351 LEU n 
1 352 ASN n 
1 353 GLY n 
1 354 GLU n 
1 355 ASN n 
1 356 CYS n 
1 357 TRP n 
1 358 GLU n 
1 359 TYR n 
1 360 TYR n 
1 361 GLU n 
1 362 GLU n 
1 363 ASN n 
1 364 GLY n 
1 365 ILE n 
1 366 PRO n 
1 367 PHE n 
1 368 LEU n 
1 369 GLU n 
1 370 LYS n 
1 371 LEU n 
1 372 TYR n 
1 373 SER n 
1 374 THR n 
1 375 LEU n 
1 376 GLU n 
1 377 LYS n 
1 378 GLU n 
1 379 GLU n 
1 380 TRP n 
1 381 ILE n 
1 382 GLU n 
1 383 THR n 
1 384 LEU n 
1 385 THR n 
1 386 LEU n 
1 387 GLU n 
1 388 GLU n 
1 389 ALA n 
1 390 MET n 
1 391 ARG n 
1 392 LYS n 
1 393 GLU n 
1 394 ASP n 
1 395 VAL n 
1 396 LYS n 
1 397 THR n 
1 398 GLU n 
1 399 VAL n 
1 400 ILE n 
1 401 GLU n 
1 402 SER n 
1 403 VAL n 
1 404 LYS n 
1 405 ALA n 
1 406 GLY n 
1 407 THR n 
1 408 TRP n 
1 409 PHE n 
1 410 ASP n 
1 411 GLY n 
1 412 ASN n 
1 413 PHE n 
1 414 LEU n 
1 415 LYS n 
1 416 TRP n 
1 417 ILE n 
1 418 GLY n 
1 419 ASN n 
1 420 LYS n 
1 421 GLU n 
1 422 LYS n 
1 423 ASN n 
1 424 GLU n 
1 425 TYR n 
1 426 TRP n 
1 427 LYS n 
1 428 ILE n 
1 429 LEU n 
1 430 ILE n 
1 431 GLU n 
1 432 ALA n 
1 433 LYS n 
1 434 LYS n 
1 435 LYS n 
1 436 ALA n 
1 437 LYS n 
1 438 ASN n 
1 439 ASP n 
1 440 TYR n 
1 441 ILE n 
1 442 LEU n 
1 443 VAL n 
1 444 ALA n 
1 445 GLU n 
1 446 GLY n 
1 447 SER n 
1 448 ASP n 
1 449 TRP n 
1 450 PHE n 
1 451 TRP n 
1 452 TRP n 
1 453 GLN n 
1 454 GLY n 
1 455 GLU n 
1 456 GLU n 
1 457 LYS n 
1 458 ALA n 
1 459 PRO n 
1 460 PHE n 
1 461 VAL n 
1 462 GLU n 
1 463 VAL n 
1 464 PHE n 
1 465 ASP n 
1 466 LYS n 
1 467 LEU n 
1 468 PHE n 
1 469 ARG n 
1 470 SER n 
1 471 PHE n 
1 472 VAL n 
1 473 ARG n 
1 474 ARG n 
1 475 ALA n 
1 476 GLN n 
1 477 GLU n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   477 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 aq_720 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Aquifex aeolicus VF5' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     224324 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
_pdbx_entity_branch.entity_id   2 
_pdbx_entity_branch.type        oligosaccharide 
# 
loop_
_pdbx_entity_branch_descriptor.ordinal 
_pdbx_entity_branch_descriptor.entity_id 
_pdbx_entity_branch_descriptor.descriptor 
_pdbx_entity_branch_descriptor.type 
_pdbx_entity_branch_descriptor.program 
_pdbx_entity_branch_descriptor.program_version 
1 2 DGlcpa1-4DGlcpa1-4DGlcpa1-4DGlcpa1-4DGlcpa1-4DGlcpa1-ROH                                                        
'Glycam Condensed Sequence' GMML       1.0   
2 2 'WURCS=2.0/1,6,5/[a2122h-1a_1-5]/1-1-1-1-1-1/a4-b1_b4-c1_c4-d1_d4-e1_e4-f1'                                     WURCS 
PDB2Glycan 1.1.0 
3 2 '[][a-D-Glcp]{[(4+1)][a-D-Glcp]{[(4+1)][a-D-Glcp]{[(4+1)][a-D-Glcp]{[(4+1)][a-D-Glcp]{[(4+1)][a-D-Glcp]{}}}}}}' LINUCS 
PDB-CARE   ?     
# 
loop_
_pdbx_entity_branch_link.link_id 
_pdbx_entity_branch_link.entity_id 
_pdbx_entity_branch_link.entity_branch_list_num_1 
_pdbx_entity_branch_link.comp_id_1 
_pdbx_entity_branch_link.atom_id_1 
_pdbx_entity_branch_link.leaving_atom_id_1 
_pdbx_entity_branch_link.entity_branch_list_num_2 
_pdbx_entity_branch_link.comp_id_2 
_pdbx_entity_branch_link.atom_id_2 
_pdbx_entity_branch_link.leaving_atom_id_2 
_pdbx_entity_branch_link.value_order 
_pdbx_entity_branch_link.details 
1 2 2 GLC C1 O1 1 GLC O4 HO4 sing ? 
2 2 3 GLC C1 O1 2 GLC O4 HO4 sing ? 
3 2 4 GLC C1 O1 3 GLC O4 HO4 sing ? 
4 2 5 GLC C1 O1 4 GLC O4 HO4 sing ? 
5 2 6 GLC C1 O1 5 GLC O4 HO4 sing ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking'           y ALANINE               ?                                     'C3 H7 N O2'     89.093  
ARG 'L-peptide linking'           y ARGININE              ?                                     'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking'           y ASPARAGINE            ?                                     'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking'           y 'ASPARTIC ACID'       ?                                     'C4 H7 N O4'     133.103 
CYS 'L-peptide linking'           y CYSTEINE              ?                                     'C3 H7 N O2 S'   121.158 
GLC 'D-saccharide, alpha linking' . alpha-D-glucopyranose 'alpha-D-glucose; D-glucose; glucose' 'C6 H12 O6'      180.156 
GLN 'L-peptide linking'           y GLUTAMINE             ?                                     'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking'           y 'GLUTAMIC ACID'       ?                                     'C5 H9 N O4'     147.129 
GLY 'peptide linking'             y GLYCINE               ?                                     'C2 H5 N O2'     75.067  
GOL non-polymer                   . GLYCEROL              'GLYCERIN; PROPANE-1,2,3-TRIOL'       'C3 H8 O3'       92.094  
HIS 'L-peptide linking'           y HISTIDINE             ?                                     'C6 H10 N3 O2 1' 156.162 
HOH non-polymer                   . WATER                 ?                                     'H2 O'           18.015  
ILE 'L-peptide linking'           y ISOLEUCINE            ?                                     'C6 H13 N O2'    131.173 
LEU 'L-peptide linking'           y LEUCINE               ?                                     'C6 H13 N O2'    131.173 
LYS 'L-peptide linking'           y LYSINE                ?                                     'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking'           y METHIONINE            ?                                     'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking'           y PHENYLALANINE         ?                                     'C9 H11 N O2'    165.189 
PRO 'L-peptide linking'           y PROLINE               ?                                     'C5 H9 N O2'     115.130 
SER 'L-peptide linking'           y SERINE                ?                                     'C3 H7 N O3'     105.093 
THR 'L-peptide linking'           y THREONINE             ?                                     'C4 H9 N O3'     119.119 
TRP 'L-peptide linking'           y TRYPTOPHAN            ?                                     'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking'           y TYROSINE              ?                                     'C9 H11 N O3'    181.189 
VAL 'L-peptide linking'           y VALINE                ?                                     'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_chem_comp_identifier.comp_id 
_pdbx_chem_comp_identifier.type 
_pdbx_chem_comp_identifier.program 
_pdbx_chem_comp_identifier.program_version 
_pdbx_chem_comp_identifier.identifier 
GLC 'CONDENSED IUPAC CARBOHYDRATE SYMBOL' GMML     1.0 DGlcpa            
GLC 'COMMON NAME'                         GMML     1.0 a-D-glucopyranose 
GLC 'IUPAC CARBOHYDRATE SYMBOL'           PDB-CARE 1.0 a-D-Glcp          
GLC 'SNFG CARBOHYDRATE SYMBOL'            GMML     1.0 Glc               
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   ?   ?   ?   A . n 
A 1 2   LYS 2   2   2   LYS LYS A . n 
A 1 3   LYS 3   3   3   LYS LYS A . n 
A 1 4   LEU 4   4   4   LEU LEU A . n 
A 1 5   PHE 5   5   5   PHE PHE A . n 
A 1 6   LEU 6   6   6   LEU LEU A . n 
A 1 7   VAL 7   7   7   VAL VAL A . n 
A 1 8   PHE 8   8   8   PHE PHE A . n 
A 1 9   TRP 9   9   9   TRP TRP A . n 
A 1 10  TRP 10  10  10  TRP TRP A . n 
A 1 11  HIS 11  11  11  HIS HIS A . n 
A 1 12  MET 12  12  12  MET MET A . n 
A 1 13  HIS 13  13  13  HIS HIS A . n 
A 1 14  GLN 14  14  14  GLN GLN A . n 
A 1 15  PRO 15  15  15  PRO PRO A . n 
A 1 16  LEU 16  16  16  LEU LEU A . n 
A 1 17  TYR 17  17  17  TYR TYR A . n 
A 1 18  ARG 18  18  18  ARG ARG A . n 
A 1 19  GLU 19  19  19  GLU GLU A . n 
A 1 20  PRO 20  20  20  PRO PRO A . n 
A 1 21  TYR 21  21  21  TYR TYR A . n 
A 1 22  THR 22  22  22  THR THR A . n 
A 1 23  GLY 23  23  23  GLY GLY A . n 
A 1 24  GLU 24  24  24  GLU GLU A . n 
A 1 25  TYR 25  25  25  TYR TYR A . n 
A 1 26  LEU 26  26  26  LEU LEU A . n 
A 1 27  LEU 27  27  27  LEU LEU A . n 
A 1 28  PRO 28  28  28  PRO PRO A . n 
A 1 29  TRP 29  29  29  TRP TRP A . n 
A 1 30  THR 30  30  30  THR THR A . n 
A 1 31  PHE 31  31  31  PHE PHE A . n 
A 1 32  PHE 32  32  32  PHE PHE A . n 
A 1 33  HIS 33  33  33  HIS HIS A . n 
A 1 34  ALA 34  34  34  ALA ALA A . n 
A 1 35  VAL 35  35  35  VAL VAL A . n 
A 1 36  LYS 36  36  36  LYS LYS A . n 
A 1 37  ASP 37  37  37  ASP ASP A . n 
A 1 38  TYR 38  38  38  TYR TYR A . n 
A 1 39  TYR 39  39  39  TYR TYR A . n 
A 1 40  ASP 40  40  40  ASP ASP A . n 
A 1 41  MET 41  41  41  MET MET A . n 
A 1 42  PRO 42  42  42  PRO PRO A . n 
A 1 43  ALA 43  43  43  ALA ALA A . n 
A 1 44  TYR 44  44  44  TYR TYR A . n 
A 1 45  LEU 45  45  45  LEU LEU A . n 
A 1 46  LYS 46  46  46  LYS LYS A . n 
A 1 47  ASP 47  47  47  ASP ASP A . n 
A 1 48  PHE 48  48  48  PHE PHE A . n 
A 1 49  GLU 49  49  49  GLU GLU A . n 
A 1 50  ILE 50  50  50  ILE ILE A . n 
A 1 51  LYS 51  51  51  LYS LYS A . n 
A 1 52  LEU 52  52  52  LEU LEU A . n 
A 1 53  ASN 53  53  53  ASN ASN A . n 
A 1 54  PHE 54  54  54  PHE PHE A . n 
A 1 55  ASN 55  55  55  ASN ASN A . n 
A 1 56  LEU 56  56  56  LEU LEU A . n 
A 1 57  THR 57  57  57  THR THR A . n 
A 1 58  PRO 58  58  58  PRO PRO A . n 
A 1 59  VAL 59  59  59  VAL VAL A . n 
A 1 60  LEU 60  60  60  LEU LEU A . n 
A 1 61  ILE 61  61  61  ILE ILE A . n 
A 1 62  ASP 62  62  62  ASP ASP A . n 
A 1 63  GLN 63  63  63  GLN GLN A . n 
A 1 64  ILE 64  64  64  ILE ILE A . n 
A 1 65  GLN 65  65  65  GLN GLN A . n 
A 1 66  GLU 66  66  66  GLU GLU A . n 
A 1 67  TYR 67  67  67  TYR TYR A . n 
A 1 68  ALA 68  68  68  ALA ALA A . n 
A 1 69  GLN 69  69  69  GLN GLN A . n 
A 1 70  GLY 70  70  70  GLY GLY A . n 
A 1 71  LYS 71  71  71  LYS LYS A . n 
A 1 72  ALA 72  72  72  ALA ALA A . n 
A 1 73  LYS 73  73  73  LYS LYS A . n 
A 1 74  ASP 74  74  74  ASP ASP A . n 
A 1 75  VAL 75  75  75  VAL VAL A . n 
A 1 76  PHE 76  76  76  PHE PHE A . n 
A 1 77  LEU 77  77  77  LEU LEU A . n 
A 1 78  GLU 78  78  78  GLU GLU A . n 
A 1 79  ALA 79  79  79  ALA ALA A . n 
A 1 80  ILE 80  80  80  ILE ILE A . n 
A 1 81  ARG 81  81  81  ARG ARG A . n 
A 1 82  LYS 82  82  82  LYS LYS A . n 
A 1 83  ASP 83  83  83  ASP ASP A . n 
A 1 84  PRO 84  84  84  PRO PRO A . n 
A 1 85  ASP 85  85  85  ASP ASP A . n 
A 1 86  ASP 86  86  86  ASP ASP A . n 
A 1 87  LEU 87  87  87  LEU LEU A . n 
A 1 88  GLU 88  88  88  GLU GLU A . n 
A 1 89  LYS 89  89  89  LYS LYS A . n 
A 1 90  GLU 90  90  90  GLU GLU A . n 
A 1 91  GLU 91  91  91  GLU GLU A . n 
A 1 92  VAL 92  92  92  VAL VAL A . n 
A 1 93  GLU 93  93  93  GLU GLU A . n 
A 1 94  LYS 94  94  94  LYS LYS A . n 
A 1 95  LEU 95  95  95  LEU LEU A . n 
A 1 96  ILE 96  96  96  ILE ILE A . n 
A 1 97  GLU 97  97  97  GLU GLU A . n 
A 1 98  PHE 98  98  98  PHE PHE A . n 
A 1 99  THR 99  99  99  THR THR A . n 
A 1 100 LYS 100 100 100 LYS LYS A . n 
A 1 101 LEU 101 101 101 LEU LEU A . n 
A 1 102 ASN 102 102 102 ASN ASN A . n 
A 1 103 TYR 103 103 103 TYR TYR A . n 
A 1 104 GLU 104 104 104 GLU GLU A . n 
A 1 105 LYS 105 105 105 LYS LYS A . n 
A 1 106 PRO 106 106 106 PRO PRO A . n 
A 1 107 ILE 107 107 107 ILE ILE A . n 
A 1 108 TYR 108 108 108 TYR TYR A . n 
A 1 109 ARG 109 109 109 ARG ARG A . n 
A 1 110 PHE 110 110 110 PHE PHE A . n 
A 1 111 GLU 111 111 111 GLU GLU A . n 
A 1 112 ARG 112 112 112 ARG ARG A . n 
A 1 113 ILE 113 113 113 ILE ILE A . n 
A 1 114 ARG 114 114 114 ARG ARG A . n 
A 1 115 GLU 115 115 115 GLU GLU A . n 
A 1 116 LEU 116 116 116 LEU LEU A . n 
A 1 117 MET 117 117 117 MET MET A . n 
A 1 118 ASN 118 118 118 ASN ASN A . n 
A 1 119 LYS 119 119 119 LYS LYS A . n 
A 1 120 GLU 120 120 120 GLU GLU A . n 
A 1 121 LYS 121 121 121 LYS LYS A . n 
A 1 122 LEU 122 122 122 LEU LEU A . n 
A 1 123 ASN 123 123 123 ASN ASN A . n 
A 1 124 ARG 124 124 124 ARG ARG A . n 
A 1 125 GLU 125 125 125 GLU GLU A . n 
A 1 126 GLU 126 126 126 GLU GLU A . n 
A 1 127 LEU 127 127 127 LEU LEU A . n 
A 1 128 LEU 128 128 128 LEU LEU A . n 
A 1 129 ASP 129 129 129 ASP ASP A . n 
A 1 130 LEU 130 130 130 LEU LEU A . n 
A 1 131 GLN 131 131 131 GLN GLN A . n 
A 1 132 THR 132 132 132 THR THR A . n 
A 1 133 LEU 133 133 133 LEU LEU A . n 
A 1 134 ASN 134 134 134 ASN ASN A . n 
A 1 135 LEU 135 135 135 LEU LEU A . n 
A 1 136 LEU 136 136 136 LEU LEU A . n 
A 1 137 ALA 137 137 137 ALA ALA A . n 
A 1 138 TRP 138 138 138 TRP TRP A . n 
A 1 139 CYS 139 139 139 CYS CYS A . n 
A 1 140 GLY 140 140 140 GLY GLY A . n 
A 1 141 ARG 141 141 141 ARG ARG A . n 
A 1 142 THR 142 142 142 THR THR A . n 
A 1 143 LEU 143 143 143 LEU LEU A . n 
A 1 144 ARG 144 144 144 ARG ARG A . n 
A 1 145 LYS 145 145 145 LYS LYS A . n 
A 1 146 ASP 146 146 146 ASP ASP A . n 
A 1 147 LEU 147 147 147 LEU LEU A . n 
A 1 148 LYS 148 148 148 LYS LYS A . n 
A 1 149 ASP 149 149 149 ASP ASP A . n 
A 1 150 LEU 150 150 150 LEU LEU A . n 
A 1 151 LEU 151 151 151 LEU LEU A . n 
A 1 152 ASN 152 152 152 ASN ASN A . n 
A 1 153 LYS 153 153 153 LYS LYS A . n 
A 1 154 GLY 154 154 154 GLY GLY A . n 
A 1 155 ARG 155 155 155 ARG ARG A . n 
A 1 156 ASN 156 156 156 ASN ASN A . n 
A 1 157 TYR 157 157 157 TYR TYR A . n 
A 1 158 THR 158 158 158 THR THR A . n 
A 1 159 GLN 159 159 159 GLN GLN A . n 
A 1 160 GLU 160 160 160 GLU GLU A . n 
A 1 161 GLU 161 161 161 GLU GLU A . n 
A 1 162 LYS 162 162 162 LYS LYS A . n 
A 1 163 GLU 163 163 163 GLU GLU A . n 
A 1 164 TYR 164 164 164 TYR TYR A . n 
A 1 165 VAL 165 165 165 VAL VAL A . n 
A 1 166 LEU 166 166 166 LEU LEU A . n 
A 1 167 ASN 167 167 167 ASN ASN A . n 
A 1 168 LYS 168 168 168 LYS LYS A . n 
A 1 169 TYR 169 169 169 TYR TYR A . n 
A 1 170 PHE 170 170 170 PHE PHE A . n 
A 1 171 GLU 171 171 171 GLU GLU A . n 
A 1 172 ILE 172 172 172 ILE ILE A . n 
A 1 173 ILE 173 173 173 ILE ILE A . n 
A 1 174 LYS 174 174 174 LYS LYS A . n 
A 1 175 LYS 175 175 175 LYS LYS A . n 
A 1 176 THR 176 176 176 THR THR A . n 
A 1 177 LEU 177 177 177 LEU LEU A . n 
A 1 178 SER 178 178 178 SER SER A . n 
A 1 179 ILE 179 179 179 ILE ILE A . n 
A 1 180 TYR 180 180 180 TYR TYR A . n 
A 1 181 ARG 181 181 181 ARG ARG A . n 
A 1 182 GLU 182 182 182 GLU GLU A . n 
A 1 183 ILE 183 183 183 ILE ILE A . n 
A 1 184 LYS 184 184 184 LYS LYS A . n 
A 1 185 GLU 185 185 185 GLU GLU A . n 
A 1 186 GLU 186 186 186 GLU GLU A . n 
A 1 187 GLY 187 187 187 GLY GLY A . n 
A 1 188 LYS 188 188 188 LYS LYS A . n 
A 1 189 GLY 189 189 189 GLY GLY A . n 
A 1 190 SER 190 190 190 SER SER A . n 
A 1 191 VAL 191 191 191 VAL VAL A . n 
A 1 192 SER 192 192 192 SER SER A . n 
A 1 193 THR 193 193 193 THR THR A . n 
A 1 194 SER 194 194 194 SER SER A . n 
A 1 195 PRO 195 195 195 PRO PRO A . n 
A 1 196 TYR 196 196 196 TYR TYR A . n 
A 1 197 TYR 197 197 197 TYR TYR A . n 
A 1 198 HIS 198 198 198 HIS HIS A . n 
A 1 199 PRO 199 199 199 PRO PRO A . n 
A 1 200 LEU 200 200 200 LEU LEU A . n 
A 1 201 ILE 201 201 201 ILE ILE A . n 
A 1 202 PRO 202 202 202 PRO PRO A . n 
A 1 203 ILE 203 203 203 ILE ILE A . n 
A 1 204 LEU 204 204 204 LEU LEU A . n 
A 1 205 LEU 205 205 205 LEU LEU A . n 
A 1 206 ASN 206 206 206 ASN ASN A . n 
A 1 207 PRO 207 207 207 PRO PRO A . n 
A 1 208 ASN 208 208 208 ASN ASN A . n 
A 1 209 CYS 209 209 209 CYS CYS A . n 
A 1 210 VAL 210 210 210 VAL VAL A . n 
A 1 211 TYR 211 211 211 TYR TYR A . n 
A 1 212 GLU 212 212 212 GLU GLU A . n 
A 1 213 THR 213 213 213 THR THR A . n 
A 1 214 THR 214 214 214 THR THR A . n 
A 1 215 PRO 215 215 215 PRO PRO A . n 
A 1 216 ASN 216 216 216 ASN ASN A . n 
A 1 217 VAL 217 217 217 VAL VAL A . n 
A 1 218 LYS 218 218 218 LYS LYS A . n 
A 1 219 ILE 219 219 219 ILE ILE A . n 
A 1 220 PRO 220 220 220 PRO PRO A . n 
A 1 221 ASP 221 221 221 ASP ASP A . n 
A 1 222 PHE 222 222 222 PHE PHE A . n 
A 1 223 ALA 223 223 223 ALA ALA A . n 
A 1 224 VAL 224 224 224 VAL VAL A . n 
A 1 225 SER 225 225 225 SER SER A . n 
A 1 226 PHE 226 226 226 PHE PHE A . n 
A 1 227 ARG 227 227 227 ARG ARG A . n 
A 1 228 GLU 228 228 228 GLU GLU A . n 
A 1 229 ASP 229 229 229 ASP ASP A . n 
A 1 230 ALA 230 230 230 ALA ALA A . n 
A 1 231 SER 231 231 231 SER SER A . n 
A 1 232 LYS 232 232 232 LYS LYS A . n 
A 1 233 HIS 233 233 233 HIS HIS A . n 
A 1 234 VAL 234 234 234 VAL VAL A . n 
A 1 235 GLU 235 235 235 GLU GLU A . n 
A 1 236 LEU 236 236 236 LEU LEU A . n 
A 1 237 ALA 237 237 237 ALA ALA A . n 
A 1 238 LYS 238 238 238 LYS LYS A . n 
A 1 239 GLU 239 239 239 GLU GLU A . n 
A 1 240 LYS 240 240 240 LYS LYS A . n 
A 1 241 TYR 241 241 241 TYR TYR A . n 
A 1 242 PHE 242 242 242 PHE PHE A . n 
A 1 243 GLU 243 243 243 GLU GLU A . n 
A 1 244 ILE 244 244 244 ILE ILE A . n 
A 1 245 PHE 245 245 245 PHE PHE A . n 
A 1 246 GLY 246 246 246 GLY GLY A . n 
A 1 247 GLU 247 247 247 GLU GLU A . n 
A 1 248 HIS 248 248 248 HIS HIS A . n 
A 1 249 PRO 249 249 249 PRO PRO A . n 
A 1 250 VAL 250 250 250 VAL VAL A . n 
A 1 251 TYR 251 251 251 TYR TYR A . n 
A 1 252 MET 252 252 252 MET MET A . n 
A 1 253 TRP 253 253 253 TRP TRP A . n 
A 1 254 PRO 254 254 254 PRO PRO A . n 
A 1 255 PRO 255 255 255 PRO PRO A . n 
A 1 256 GLU 256 256 256 GLU GLU A . n 
A 1 257 ALA 257 257 257 ALA ALA A . n 
A 1 258 SER 258 258 258 SER SER A . n 
A 1 259 VAL 259 259 259 VAL VAL A . n 
A 1 260 SER 260 260 260 SER SER A . n 
A 1 261 ASN 261 261 261 ASN ASN A . n 
A 1 262 GLU 262 262 262 GLU GLU A . n 
A 1 263 ALA 263 263 263 ALA ALA A . n 
A 1 264 LEU 264 264 264 LEU LEU A . n 
A 1 265 GLU 265 265 265 GLU GLU A . n 
A 1 266 LEU 266 266 266 LEU LEU A . n 
A 1 267 TYR 267 267 267 TYR TYR A . n 
A 1 268 TYR 268 268 268 TYR TYR A . n 
A 1 269 GLU 269 269 269 GLU GLU A . n 
A 1 270 LYS 270 270 270 LYS LYS A . n 
A 1 271 GLY 271 271 271 GLY GLY A . n 
A 1 272 ILE 272 272 272 ILE ILE A . n 
A 1 273 ASN 273 273 273 ASN ASN A . n 
A 1 274 MET 274 274 274 MET MET A . n 
A 1 275 LEU 275 275 275 LEU LEU A . n 
A 1 276 ALA 276 276 276 ALA ALA A . n 
A 1 277 THR 277 277 277 THR THR A . n 
A 1 278 ASP 278 278 278 ASP ASP A . n 
A 1 279 GLU 279 279 279 GLU GLU A . n 
A 1 280 VAL 280 280 280 VAL VAL A . n 
A 1 281 ILE 281 281 281 ILE ILE A . n 
A 1 282 LEU 282 282 282 LEU LEU A . n 
A 1 283 LYS 283 283 283 LYS LYS A . n 
A 1 284 ASN 284 284 284 ASN ASN A . n 
A 1 285 SER 285 285 285 SER SER A . n 
A 1 286 VAL 286 286 286 VAL VAL A . n 
A 1 287 GLU 287 287 287 GLU GLU A . n 
A 1 288 ARG 288 288 288 ARG ARG A . n 
A 1 289 ALA 289 289 289 ALA ALA A . n 
A 1 290 SER 290 290 290 SER SER A . n 
A 1 291 PRO 291 291 291 PRO PRO A . n 
A 1 292 TYR 292 292 292 TYR TYR A . n 
A 1 293 LEU 293 293 293 LEU LEU A . n 
A 1 294 ARG 294 294 294 ARG ARG A . n 
A 1 295 TYR 295 295 295 TYR TYR A . n 
A 1 296 TYR 296 296 296 TYR TYR A . n 
A 1 297 PHE 297 297 297 PHE PHE A . n 
A 1 298 ARG 298 298 298 ARG ARG A . n 
A 1 299 GLU 299 299 299 GLU GLU A . n 
A 1 300 LEU 300 300 300 LEU LEU A . n 
A 1 301 ILE 301 301 301 ILE ILE A . n 
A 1 302 SER 302 302 302 SER SER A . n 
A 1 303 VAL 303 303 303 VAL VAL A . n 
A 1 304 PHE 304 304 304 PHE PHE A . n 
A 1 305 PHE 305 305 305 PHE PHE A . n 
A 1 306 ARG 306 306 306 ARG ARG A . n 
A 1 307 ASP 307 307 307 ASP ASP A . n 
A 1 308 LYS 308 308 308 LYS LYS A . n 
A 1 309 THR 309 309 309 THR THR A . n 
A 1 310 LEU 310 310 310 LEU LEU A . n 
A 1 311 SER 311 311 311 SER SER A . n 
A 1 312 ASP 312 312 312 ASP ASP A . n 
A 1 313 LEU 313 313 313 LEU LEU A . n 
A 1 314 ILE 314 314 314 ILE ILE A . n 
A 1 315 GLY 315 315 315 GLY GLY A . n 
A 1 316 PHE 316 316 316 PHE PHE A . n 
A 1 317 SER 317 317 317 SER SER A . n 
A 1 318 TYR 318 318 318 TYR TYR A . n 
A 1 319 HIS 319 319 319 HIS HIS A . n 
A 1 320 ALA 320 320 320 ALA ALA A . n 
A 1 321 TRP 321 321 321 TRP TRP A . n 
A 1 322 ASN 322 322 322 ASN ASN A . n 
A 1 323 ALA 323 323 323 ALA ALA A . n 
A 1 324 GLU 324 324 324 GLU GLU A . n 
A 1 325 ASP 325 325 325 ASP ASP A . n 
A 1 326 ALA 326 326 326 ALA ALA A . n 
A 1 327 VAL 327 327 327 VAL VAL A . n 
A 1 328 ARG 328 328 328 ARG ARG A . n 
A 1 329 ASP 329 329 329 ASP ASP A . n 
A 1 330 PHE 330 330 330 PHE PHE A . n 
A 1 331 ILE 331 331 331 ILE ILE A . n 
A 1 332 GLY 332 332 332 GLY GLY A . n 
A 1 333 ARG 333 333 333 ARG ARG A . n 
A 1 334 LEU 334 334 334 LEU LEU A . n 
A 1 335 LYS 335 335 335 LYS LYS A . n 
A 1 336 LYS 336 336 336 LYS LYS A . n 
A 1 337 ILE 337 337 337 ILE ILE A . n 
A 1 338 HIS 338 338 338 HIS HIS A . n 
A 1 339 GLU 339 339 339 GLU GLU A . n 
A 1 340 SER 340 340 340 SER SER A . n 
A 1 341 VAL 341 341 341 VAL VAL A . n 
A 1 342 ASP 342 342 342 ASP ASP A . n 
A 1 343 PHE 343 343 343 PHE PHE A . n 
A 1 344 GLN 344 344 344 GLN GLN A . n 
A 1 345 PRO 345 345 345 PRO PRO A . n 
A 1 346 VAL 346 346 346 VAL VAL A . n 
A 1 347 VAL 347 347 347 VAL VAL A . n 
A 1 348 PHE 348 348 348 PHE PHE A . n 
A 1 349 VAL 349 349 349 VAL VAL A . n 
A 1 350 VAL 350 350 350 VAL VAL A . n 
A 1 351 LEU 351 351 351 LEU LEU A . n 
A 1 352 ASN 352 352 352 ASN ASN A . n 
A 1 353 GLY 353 353 353 GLY GLY A . n 
A 1 354 GLU 354 354 354 GLU GLU A . n 
A 1 355 ASN 355 355 355 ASN ASN A . n 
A 1 356 CYS 356 356 356 CYS CYS A . n 
A 1 357 TRP 357 357 357 TRP TRP A . n 
A 1 358 GLU 358 358 358 GLU GLU A . n 
A 1 359 TYR 359 359 359 TYR TYR A . n 
A 1 360 TYR 360 360 360 TYR TYR A . n 
A 1 361 GLU 361 361 361 GLU GLU A . n 
A 1 362 GLU 362 362 362 GLU GLU A . n 
A 1 363 ASN 363 363 363 ASN ASN A . n 
A 1 364 GLY 364 364 364 GLY GLY A . n 
A 1 365 ILE 365 365 365 ILE ILE A . n 
A 1 366 PRO 366 366 366 PRO PRO A . n 
A 1 367 PHE 367 367 367 PHE PHE A . n 
A 1 368 LEU 368 368 368 LEU LEU A . n 
A 1 369 GLU 369 369 369 GLU GLU A . n 
A 1 370 LYS 370 370 370 LYS LYS A . n 
A 1 371 LEU 371 371 371 LEU LEU A . n 
A 1 372 TYR 372 372 372 TYR TYR A . n 
A 1 373 SER 373 373 373 SER SER A . n 
A 1 374 THR 374 374 374 THR THR A . n 
A 1 375 LEU 375 375 375 LEU LEU A . n 
A 1 376 GLU 376 376 376 GLU GLU A . n 
A 1 377 LYS 377 377 377 LYS LYS A . n 
A 1 378 GLU 378 378 378 GLU GLU A . n 
A 1 379 GLU 379 379 379 GLU GLU A . n 
A 1 380 TRP 380 380 380 TRP TRP A . n 
A 1 381 ILE 381 381 381 ILE ILE A . n 
A 1 382 GLU 382 382 382 GLU GLU A . n 
A 1 383 THR 383 383 383 THR THR A . n 
A 1 384 LEU 384 384 384 LEU LEU A . n 
A 1 385 THR 385 385 385 THR THR A . n 
A 1 386 LEU 386 386 386 LEU LEU A . n 
A 1 387 GLU 387 387 387 GLU GLU A . n 
A 1 388 GLU 388 388 388 GLU GLU A . n 
A 1 389 ALA 389 389 389 ALA ALA A . n 
A 1 390 MET 390 390 390 MET MET A . n 
A 1 391 ARG 391 391 391 ARG ARG A . n 
A 1 392 LYS 392 392 392 LYS LYS A . n 
A 1 393 GLU 393 393 393 GLU GLU A . n 
A 1 394 ASP 394 394 394 ASP ASP A . n 
A 1 395 VAL 395 395 395 VAL VAL A . n 
A 1 396 LYS 396 396 396 LYS LYS A . n 
A 1 397 THR 397 397 397 THR THR A . n 
A 1 398 GLU 398 398 398 GLU GLU A . n 
A 1 399 VAL 399 399 399 VAL VAL A . n 
A 1 400 ILE 400 400 400 ILE ILE A . n 
A 1 401 GLU 401 401 401 GLU GLU A . n 
A 1 402 SER 402 402 402 SER SER A . n 
A 1 403 VAL 403 403 403 VAL VAL A . n 
A 1 404 LYS 404 404 404 LYS LYS A . n 
A 1 405 ALA 405 405 405 ALA ALA A . n 
A 1 406 GLY 406 406 406 GLY GLY A . n 
A 1 407 THR 407 407 407 THR THR A . n 
A 1 408 TRP 408 408 408 TRP TRP A . n 
A 1 409 PHE 409 409 409 PHE PHE A . n 
A 1 410 ASP 410 410 410 ASP ASP A . n 
A 1 411 GLY 411 411 411 GLY GLY A . n 
A 1 412 ASN 412 412 412 ASN ASN A . n 
A 1 413 PHE 413 413 413 PHE PHE A . n 
A 1 414 LEU 414 414 414 LEU LEU A . n 
A 1 415 LYS 415 415 415 LYS LYS A . n 
A 1 416 TRP 416 416 416 TRP TRP A . n 
A 1 417 ILE 417 417 417 ILE ILE A . n 
A 1 418 GLY 418 418 418 GLY GLY A . n 
A 1 419 ASN 419 419 419 ASN ASN A . n 
A 1 420 LYS 420 420 420 LYS LYS A . n 
A 1 421 GLU 421 421 421 GLU GLU A . n 
A 1 422 LYS 422 422 422 LYS LYS A . n 
A 1 423 ASN 423 423 423 ASN ASN A . n 
A 1 424 GLU 424 424 424 GLU GLU A . n 
A 1 425 TYR 425 425 425 TYR TYR A . n 
A 1 426 TRP 426 426 426 TRP TRP A . n 
A 1 427 LYS 427 427 427 LYS LYS A . n 
A 1 428 ILE 428 428 428 ILE ILE A . n 
A 1 429 LEU 429 429 429 LEU LEU A . n 
A 1 430 ILE 430 430 430 ILE ILE A . n 
A 1 431 GLU 431 431 431 GLU GLU A . n 
A 1 432 ALA 432 432 432 ALA ALA A . n 
A 1 433 LYS 433 433 433 LYS LYS A . n 
A 1 434 LYS 434 434 434 LYS LYS A . n 
A 1 435 LYS 435 435 435 LYS LYS A . n 
A 1 436 ALA 436 436 436 ALA ALA A . n 
A 1 437 LYS 437 437 437 LYS LYS A . n 
A 1 438 ASN 438 438 438 ASN ASN A . n 
A 1 439 ASP 439 439 439 ASP ASP A . n 
A 1 440 TYR 440 440 440 TYR TYR A . n 
A 1 441 ILE 441 441 441 ILE ILE A . n 
A 1 442 LEU 442 442 442 LEU LEU A . n 
A 1 443 VAL 443 443 443 VAL VAL A . n 
A 1 444 ALA 444 444 444 ALA ALA A . n 
A 1 445 GLU 445 445 445 GLU GLU A . n 
A 1 446 GLY 446 446 446 GLY GLY A . n 
A 1 447 SER 447 447 447 SER SER A . n 
A 1 448 ASP 448 448 448 ASP ASP A . n 
A 1 449 TRP 449 449 449 TRP TRP A . n 
A 1 450 PHE 450 450 450 PHE PHE A . n 
A 1 451 TRP 451 451 451 TRP TRP A . n 
A 1 452 TRP 452 452 452 TRP TRP A . n 
A 1 453 GLN 453 453 453 GLN GLN A . n 
A 1 454 GLY 454 454 454 GLY GLY A . n 
A 1 455 GLU 455 455 455 GLU GLU A . n 
A 1 456 GLU 456 456 456 GLU GLU A . n 
A 1 457 LYS 457 457 457 LYS LYS A . n 
A 1 458 ALA 458 458 458 ALA ALA A . n 
A 1 459 PRO 459 459 459 PRO PRO A . n 
A 1 460 PHE 460 460 460 PHE PHE A . n 
A 1 461 VAL 461 461 461 VAL VAL A . n 
A 1 462 GLU 462 462 462 GLU GLU A . n 
A 1 463 VAL 463 463 463 VAL VAL A . n 
A 1 464 PHE 464 464 464 PHE PHE A . n 
A 1 465 ASP 465 465 465 ASP ASP A . n 
A 1 466 LYS 466 466 466 LYS LYS A . n 
A 1 467 LEU 467 467 467 LEU LEU A . n 
A 1 468 PHE 468 468 468 PHE PHE A . n 
A 1 469 ARG 469 469 469 ARG ARG A . n 
A 1 470 SER 470 470 470 SER SER A . n 
A 1 471 PHE 471 471 471 PHE PHE A . n 
A 1 472 VAL 472 472 472 VAL VAL A . n 
A 1 473 ARG 473 473 473 ARG ARG A . n 
A 1 474 ARG 474 474 474 ARG ARG A . n 
A 1 475 ALA 475 475 475 ALA ALA A . n 
A 1 476 GLN 476 476 476 GLN GLN A . n 
A 1 477 GLU 477 477 477 GLU GLU A . n 
B 1 1   MET 1   1   ?   ?   ?   B . n 
B 1 2   LYS 2   2   2   LYS LYS B . n 
B 1 3   LYS 3   3   3   LYS LYS B . n 
B 1 4   LEU 4   4   4   LEU LEU B . n 
B 1 5   PHE 5   5   5   PHE PHE B . n 
B 1 6   LEU 6   6   6   LEU LEU B . n 
B 1 7   VAL 7   7   7   VAL VAL B . n 
B 1 8   PHE 8   8   8   PHE PHE B . n 
B 1 9   TRP 9   9   9   TRP TRP B . n 
B 1 10  TRP 10  10  10  TRP TRP B . n 
B 1 11  HIS 11  11  11  HIS HIS B . n 
B 1 12  MET 12  12  12  MET MET B . n 
B 1 13  HIS 13  13  13  HIS HIS B . n 
B 1 14  GLN 14  14  14  GLN GLN B . n 
B 1 15  PRO 15  15  15  PRO PRO B . n 
B 1 16  LEU 16  16  16  LEU LEU B . n 
B 1 17  TYR 17  17  17  TYR TYR B . n 
B 1 18  ARG 18  18  18  ARG ARG B . n 
B 1 19  GLU 19  19  19  GLU GLU B . n 
B 1 20  PRO 20  20  20  PRO PRO B . n 
B 1 21  TYR 21  21  21  TYR TYR B . n 
B 1 22  THR 22  22  22  THR THR B . n 
B 1 23  GLY 23  23  23  GLY GLY B . n 
B 1 24  GLU 24  24  24  GLU GLU B . n 
B 1 25  TYR 25  25  25  TYR TYR B . n 
B 1 26  LEU 26  26  26  LEU LEU B . n 
B 1 27  LEU 27  27  27  LEU LEU B . n 
B 1 28  PRO 28  28  28  PRO PRO B . n 
B 1 29  TRP 29  29  29  TRP TRP B . n 
B 1 30  THR 30  30  30  THR THR B . n 
B 1 31  PHE 31  31  31  PHE PHE B . n 
B 1 32  PHE 32  32  32  PHE PHE B . n 
B 1 33  HIS 33  33  33  HIS HIS B . n 
B 1 34  ALA 34  34  34  ALA ALA B . n 
B 1 35  VAL 35  35  35  VAL VAL B . n 
B 1 36  LYS 36  36  36  LYS LYS B . n 
B 1 37  ASP 37  37  37  ASP ASP B . n 
B 1 38  TYR 38  38  38  TYR TYR B . n 
B 1 39  TYR 39  39  39  TYR TYR B . n 
B 1 40  ASP 40  40  40  ASP ASP B . n 
B 1 41  MET 41  41  41  MET MET B . n 
B 1 42  PRO 42  42  42  PRO PRO B . n 
B 1 43  ALA 43  43  43  ALA ALA B . n 
B 1 44  TYR 44  44  44  TYR TYR B . n 
B 1 45  LEU 45  45  45  LEU LEU B . n 
B 1 46  LYS 46  46  46  LYS LYS B . n 
B 1 47  ASP 47  47  47  ASP ASP B . n 
B 1 48  PHE 48  48  48  PHE PHE B . n 
B 1 49  GLU 49  49  49  GLU GLU B . n 
B 1 50  ILE 50  50  50  ILE ILE B . n 
B 1 51  LYS 51  51  51  LYS LYS B . n 
B 1 52  LEU 52  52  52  LEU LEU B . n 
B 1 53  ASN 53  53  53  ASN ASN B . n 
B 1 54  PHE 54  54  54  PHE PHE B . n 
B 1 55  ASN 55  55  55  ASN ASN B . n 
B 1 56  LEU 56  56  56  LEU LEU B . n 
B 1 57  THR 57  57  57  THR THR B . n 
B 1 58  PRO 58  58  58  PRO PRO B . n 
B 1 59  VAL 59  59  59  VAL VAL B . n 
B 1 60  LEU 60  60  60  LEU LEU B . n 
B 1 61  ILE 61  61  61  ILE ILE B . n 
B 1 62  ASP 62  62  62  ASP ASP B . n 
B 1 63  GLN 63  63  63  GLN GLN B . n 
B 1 64  ILE 64  64  64  ILE ILE B . n 
B 1 65  GLN 65  65  65  GLN GLN B . n 
B 1 66  GLU 66  66  66  GLU GLU B . n 
B 1 67  TYR 67  67  67  TYR TYR B . n 
B 1 68  ALA 68  68  68  ALA ALA B . n 
B 1 69  GLN 69  69  69  GLN GLN B . n 
B 1 70  GLY 70  70  70  GLY GLY B . n 
B 1 71  LYS 71  71  71  LYS LYS B . n 
B 1 72  ALA 72  72  72  ALA ALA B . n 
B 1 73  LYS 73  73  73  LYS LYS B . n 
B 1 74  ASP 74  74  74  ASP ASP B . n 
B 1 75  VAL 75  75  75  VAL VAL B . n 
B 1 76  PHE 76  76  76  PHE PHE B . n 
B 1 77  LEU 77  77  77  LEU LEU B . n 
B 1 78  GLU 78  78  78  GLU GLU B . n 
B 1 79  ALA 79  79  79  ALA ALA B . n 
B 1 80  ILE 80  80  80  ILE ILE B . n 
B 1 81  ARG 81  81  81  ARG ARG B . n 
B 1 82  LYS 82  82  82  LYS LYS B . n 
B 1 83  ASP 83  83  83  ASP ASP B . n 
B 1 84  PRO 84  84  84  PRO PRO B . n 
B 1 85  ASP 85  85  85  ASP ASP B . n 
B 1 86  ASP 86  86  86  ASP ASP B . n 
B 1 87  LEU 87  87  87  LEU LEU B . n 
B 1 88  GLU 88  88  88  GLU GLU B . n 
B 1 89  LYS 89  89  89  LYS LYS B . n 
B 1 90  GLU 90  90  90  GLU GLU B . n 
B 1 91  GLU 91  91  91  GLU GLU B . n 
B 1 92  VAL 92  92  92  VAL VAL B . n 
B 1 93  GLU 93  93  93  GLU GLU B . n 
B 1 94  LYS 94  94  94  LYS LYS B . n 
B 1 95  LEU 95  95  95  LEU LEU B . n 
B 1 96  ILE 96  96  96  ILE ILE B . n 
B 1 97  GLU 97  97  97  GLU GLU B . n 
B 1 98  PHE 98  98  98  PHE PHE B . n 
B 1 99  THR 99  99  99  THR THR B . n 
B 1 100 LYS 100 100 100 LYS LYS B . n 
B 1 101 LEU 101 101 101 LEU LEU B . n 
B 1 102 ASN 102 102 102 ASN ASN B . n 
B 1 103 TYR 103 103 103 TYR TYR B . n 
B 1 104 GLU 104 104 104 GLU GLU B . n 
B 1 105 LYS 105 105 105 LYS LYS B . n 
B 1 106 PRO 106 106 106 PRO PRO B . n 
B 1 107 ILE 107 107 107 ILE ILE B . n 
B 1 108 TYR 108 108 108 TYR TYR B . n 
B 1 109 ARG 109 109 109 ARG ARG B . n 
B 1 110 PHE 110 110 110 PHE PHE B . n 
B 1 111 GLU 111 111 111 GLU GLU B . n 
B 1 112 ARG 112 112 112 ARG ARG B . n 
B 1 113 ILE 113 113 113 ILE ILE B . n 
B 1 114 ARG 114 114 114 ARG ARG B . n 
B 1 115 GLU 115 115 115 GLU GLU B . n 
B 1 116 LEU 116 116 116 LEU LEU B . n 
B 1 117 MET 117 117 117 MET MET B . n 
B 1 118 ASN 118 118 118 ASN ASN B . n 
B 1 119 LYS 119 119 119 LYS LYS B . n 
B 1 120 GLU 120 120 120 GLU GLU B . n 
B 1 121 LYS 121 121 121 LYS LYS B . n 
B 1 122 LEU 122 122 122 LEU LEU B . n 
B 1 123 ASN 123 123 123 ASN ASN B . n 
B 1 124 ARG 124 124 124 ARG ARG B . n 
B 1 125 GLU 125 125 125 GLU GLU B . n 
B 1 126 GLU 126 126 126 GLU GLU B . n 
B 1 127 LEU 127 127 127 LEU LEU B . n 
B 1 128 LEU 128 128 128 LEU LEU B . n 
B 1 129 ASP 129 129 129 ASP ASP B . n 
B 1 130 LEU 130 130 130 LEU LEU B . n 
B 1 131 GLN 131 131 131 GLN GLN B . n 
B 1 132 THR 132 132 132 THR THR B . n 
B 1 133 LEU 133 133 133 LEU LEU B . n 
B 1 134 ASN 134 134 134 ASN ASN B . n 
B 1 135 LEU 135 135 135 LEU LEU B . n 
B 1 136 LEU 136 136 136 LEU LEU B . n 
B 1 137 ALA 137 137 137 ALA ALA B . n 
B 1 138 TRP 138 138 138 TRP TRP B . n 
B 1 139 CYS 139 139 139 CYS CYS B . n 
B 1 140 GLY 140 140 140 GLY GLY B . n 
B 1 141 ARG 141 141 141 ARG ARG B . n 
B 1 142 THR 142 142 142 THR THR B . n 
B 1 143 LEU 143 143 143 LEU LEU B . n 
B 1 144 ARG 144 144 144 ARG ARG B . n 
B 1 145 LYS 145 145 145 LYS LYS B . n 
B 1 146 ASP 146 146 146 ASP ASP B . n 
B 1 147 LEU 147 147 147 LEU LEU B . n 
B 1 148 LYS 148 148 148 LYS LYS B . n 
B 1 149 ASP 149 149 149 ASP ASP B . n 
B 1 150 LEU 150 150 150 LEU LEU B . n 
B 1 151 LEU 151 151 151 LEU LEU B . n 
B 1 152 ASN 152 152 152 ASN ASN B . n 
B 1 153 LYS 153 153 153 LYS LYS B . n 
B 1 154 GLY 154 154 154 GLY GLY B . n 
B 1 155 ARG 155 155 155 ARG ARG B . n 
B 1 156 ASN 156 156 156 ASN ASN B . n 
B 1 157 TYR 157 157 157 TYR TYR B . n 
B 1 158 THR 158 158 158 THR THR B . n 
B 1 159 GLN 159 159 159 GLN GLN B . n 
B 1 160 GLU 160 160 160 GLU GLU B . n 
B 1 161 GLU 161 161 161 GLU GLU B . n 
B 1 162 LYS 162 162 162 LYS LYS B . n 
B 1 163 GLU 163 163 163 GLU GLU B . n 
B 1 164 TYR 164 164 164 TYR TYR B . n 
B 1 165 VAL 165 165 165 VAL VAL B . n 
B 1 166 LEU 166 166 166 LEU LEU B . n 
B 1 167 ASN 167 167 167 ASN ASN B . n 
B 1 168 LYS 168 168 168 LYS LYS B . n 
B 1 169 TYR 169 169 169 TYR TYR B . n 
B 1 170 PHE 170 170 170 PHE PHE B . n 
B 1 171 GLU 171 171 171 GLU GLU B . n 
B 1 172 ILE 172 172 172 ILE ILE B . n 
B 1 173 ILE 173 173 173 ILE ILE B . n 
B 1 174 LYS 174 174 174 LYS LYS B . n 
B 1 175 LYS 175 175 175 LYS LYS B . n 
B 1 176 THR 176 176 176 THR THR B . n 
B 1 177 LEU 177 177 177 LEU LEU B . n 
B 1 178 SER 178 178 178 SER SER B . n 
B 1 179 ILE 179 179 179 ILE ILE B . n 
B 1 180 TYR 180 180 180 TYR TYR B . n 
B 1 181 ARG 181 181 181 ARG ARG B . n 
B 1 182 GLU 182 182 182 GLU GLU B . n 
B 1 183 ILE 183 183 183 ILE ILE B . n 
B 1 184 LYS 184 184 184 LYS LYS B . n 
B 1 185 GLU 185 185 185 GLU GLU B . n 
B 1 186 GLU 186 186 186 GLU GLU B . n 
B 1 187 GLY 187 187 187 GLY GLY B . n 
B 1 188 LYS 188 188 188 LYS LYS B . n 
B 1 189 GLY 189 189 189 GLY GLY B . n 
B 1 190 SER 190 190 190 SER SER B . n 
B 1 191 VAL 191 191 191 VAL VAL B . n 
B 1 192 SER 192 192 192 SER SER B . n 
B 1 193 THR 193 193 193 THR THR B . n 
B 1 194 SER 194 194 194 SER SER B . n 
B 1 195 PRO 195 195 195 PRO PRO B . n 
B 1 196 TYR 196 196 196 TYR TYR B . n 
B 1 197 TYR 197 197 197 TYR TYR B . n 
B 1 198 HIS 198 198 198 HIS HIS B . n 
B 1 199 PRO 199 199 199 PRO PRO B . n 
B 1 200 LEU 200 200 200 LEU LEU B . n 
B 1 201 ILE 201 201 201 ILE ILE B . n 
B 1 202 PRO 202 202 202 PRO PRO B . n 
B 1 203 ILE 203 203 203 ILE ILE B . n 
B 1 204 LEU 204 204 204 LEU LEU B . n 
B 1 205 LEU 205 205 205 LEU LEU B . n 
B 1 206 ASN 206 206 206 ASN ASN B . n 
B 1 207 PRO 207 207 207 PRO PRO B . n 
B 1 208 ASN 208 208 208 ASN ASN B . n 
B 1 209 CYS 209 209 209 CYS CYS B . n 
B 1 210 VAL 210 210 210 VAL VAL B . n 
B 1 211 TYR 211 211 211 TYR TYR B . n 
B 1 212 GLU 212 212 212 GLU GLU B . n 
B 1 213 THR 213 213 213 THR THR B . n 
B 1 214 THR 214 214 214 THR THR B . n 
B 1 215 PRO 215 215 215 PRO PRO B . n 
B 1 216 ASN 216 216 216 ASN ASN B . n 
B 1 217 VAL 217 217 217 VAL VAL B . n 
B 1 218 LYS 218 218 218 LYS LYS B . n 
B 1 219 ILE 219 219 219 ILE ILE B . n 
B 1 220 PRO 220 220 220 PRO PRO B . n 
B 1 221 ASP 221 221 221 ASP ASP B . n 
B 1 222 PHE 222 222 222 PHE PHE B . n 
B 1 223 ALA 223 223 223 ALA ALA B . n 
B 1 224 VAL 224 224 224 VAL VAL B . n 
B 1 225 SER 225 225 225 SER SER B . n 
B 1 226 PHE 226 226 226 PHE PHE B . n 
B 1 227 ARG 227 227 227 ARG ARG B . n 
B 1 228 GLU 228 228 228 GLU GLU B . n 
B 1 229 ASP 229 229 229 ASP ASP B . n 
B 1 230 ALA 230 230 230 ALA ALA B . n 
B 1 231 SER 231 231 231 SER SER B . n 
B 1 232 LYS 232 232 232 LYS LYS B . n 
B 1 233 HIS 233 233 233 HIS HIS B . n 
B 1 234 VAL 234 234 234 VAL VAL B . n 
B 1 235 GLU 235 235 235 GLU GLU B . n 
B 1 236 LEU 236 236 236 LEU LEU B . n 
B 1 237 ALA 237 237 237 ALA ALA B . n 
B 1 238 LYS 238 238 238 LYS LYS B . n 
B 1 239 GLU 239 239 239 GLU GLU B . n 
B 1 240 LYS 240 240 240 LYS LYS B . n 
B 1 241 TYR 241 241 241 TYR TYR B . n 
B 1 242 PHE 242 242 242 PHE PHE B . n 
B 1 243 GLU 243 243 243 GLU GLU B . n 
B 1 244 ILE 244 244 244 ILE ILE B . n 
B 1 245 PHE 245 245 245 PHE PHE B . n 
B 1 246 GLY 246 246 246 GLY GLY B . n 
B 1 247 GLU 247 247 247 GLU GLU B . n 
B 1 248 HIS 248 248 248 HIS HIS B . n 
B 1 249 PRO 249 249 249 PRO PRO B . n 
B 1 250 VAL 250 250 250 VAL VAL B . n 
B 1 251 TYR 251 251 251 TYR TYR B . n 
B 1 252 MET 252 252 252 MET MET B . n 
B 1 253 TRP 253 253 253 TRP TRP B . n 
B 1 254 PRO 254 254 254 PRO PRO B . n 
B 1 255 PRO 255 255 255 PRO PRO B . n 
B 1 256 GLU 256 256 256 GLU GLU B . n 
B 1 257 ALA 257 257 257 ALA ALA B . n 
B 1 258 SER 258 258 258 SER SER B . n 
B 1 259 VAL 259 259 259 VAL VAL B . n 
B 1 260 SER 260 260 260 SER SER B . n 
B 1 261 ASN 261 261 261 ASN ASN B . n 
B 1 262 GLU 262 262 262 GLU GLU B . n 
B 1 263 ALA 263 263 263 ALA ALA B . n 
B 1 264 LEU 264 264 264 LEU LEU B . n 
B 1 265 GLU 265 265 265 GLU GLU B . n 
B 1 266 LEU 266 266 266 LEU LEU B . n 
B 1 267 TYR 267 267 267 TYR TYR B . n 
B 1 268 TYR 268 268 268 TYR TYR B . n 
B 1 269 GLU 269 269 269 GLU GLU B . n 
B 1 270 LYS 270 270 270 LYS LYS B . n 
B 1 271 GLY 271 271 271 GLY GLY B . n 
B 1 272 ILE 272 272 272 ILE ILE B . n 
B 1 273 ASN 273 273 273 ASN ASN B . n 
B 1 274 MET 274 274 274 MET MET B . n 
B 1 275 LEU 275 275 275 LEU LEU B . n 
B 1 276 ALA 276 276 276 ALA ALA B . n 
B 1 277 THR 277 277 277 THR THR B . n 
B 1 278 ASP 278 278 278 ASP ASP B . n 
B 1 279 GLU 279 279 279 GLU GLU B . n 
B 1 280 VAL 280 280 280 VAL VAL B . n 
B 1 281 ILE 281 281 281 ILE ILE B . n 
B 1 282 LEU 282 282 282 LEU LEU B . n 
B 1 283 LYS 283 283 283 LYS LYS B . n 
B 1 284 ASN 284 284 284 ASN ASN B . n 
B 1 285 SER 285 285 285 SER SER B . n 
B 1 286 VAL 286 286 286 VAL VAL B . n 
B 1 287 GLU 287 287 287 GLU GLU B . n 
B 1 288 ARG 288 288 288 ARG ARG B . n 
B 1 289 ALA 289 289 289 ALA ALA B . n 
B 1 290 SER 290 290 290 SER SER B . n 
B 1 291 PRO 291 291 291 PRO PRO B . n 
B 1 292 TYR 292 292 292 TYR TYR B . n 
B 1 293 LEU 293 293 293 LEU LEU B . n 
B 1 294 ARG 294 294 294 ARG ARG B . n 
B 1 295 TYR 295 295 295 TYR TYR B . n 
B 1 296 TYR 296 296 296 TYR TYR B . n 
B 1 297 PHE 297 297 297 PHE PHE B . n 
B 1 298 ARG 298 298 298 ARG ARG B . n 
B 1 299 GLU 299 299 299 GLU GLU B . n 
B 1 300 LEU 300 300 300 LEU LEU B . n 
B 1 301 ILE 301 301 301 ILE ILE B . n 
B 1 302 SER 302 302 302 SER SER B . n 
B 1 303 VAL 303 303 303 VAL VAL B . n 
B 1 304 PHE 304 304 304 PHE PHE B . n 
B 1 305 PHE 305 305 305 PHE PHE B . n 
B 1 306 ARG 306 306 306 ARG ARG B . n 
B 1 307 ASP 307 307 307 ASP ASP B . n 
B 1 308 LYS 308 308 308 LYS LYS B . n 
B 1 309 THR 309 309 309 THR THR B . n 
B 1 310 LEU 310 310 310 LEU LEU B . n 
B 1 311 SER 311 311 311 SER SER B . n 
B 1 312 ASP 312 312 312 ASP ASP B . n 
B 1 313 LEU 313 313 313 LEU LEU B . n 
B 1 314 ILE 314 314 314 ILE ILE B . n 
B 1 315 GLY 315 315 315 GLY GLY B . n 
B 1 316 PHE 316 316 316 PHE PHE B . n 
B 1 317 SER 317 317 317 SER SER B . n 
B 1 318 TYR 318 318 318 TYR TYR B . n 
B 1 319 HIS 319 319 319 HIS HIS B . n 
B 1 320 ALA 320 320 320 ALA ALA B . n 
B 1 321 TRP 321 321 321 TRP TRP B . n 
B 1 322 ASN 322 322 322 ASN ASN B . n 
B 1 323 ALA 323 323 323 ALA ALA B . n 
B 1 324 GLU 324 324 324 GLU GLU B . n 
B 1 325 ASP 325 325 325 ASP ASP B . n 
B 1 326 ALA 326 326 326 ALA ALA B . n 
B 1 327 VAL 327 327 327 VAL VAL B . n 
B 1 328 ARG 328 328 328 ARG ARG B . n 
B 1 329 ASP 329 329 329 ASP ASP B . n 
B 1 330 PHE 330 330 330 PHE PHE B . n 
B 1 331 ILE 331 331 331 ILE ILE B . n 
B 1 332 GLY 332 332 332 GLY GLY B . n 
B 1 333 ARG 333 333 333 ARG ARG B . n 
B 1 334 LEU 334 334 334 LEU LEU B . n 
B 1 335 LYS 335 335 335 LYS LYS B . n 
B 1 336 LYS 336 336 336 LYS LYS B . n 
B 1 337 ILE 337 337 337 ILE ILE B . n 
B 1 338 HIS 338 338 338 HIS HIS B . n 
B 1 339 GLU 339 339 339 GLU GLU B . n 
B 1 340 SER 340 340 340 SER SER B . n 
B 1 341 VAL 341 341 341 VAL VAL B . n 
B 1 342 ASP 342 342 342 ASP ASP B . n 
B 1 343 PHE 343 343 343 PHE PHE B . n 
B 1 344 GLN 344 344 344 GLN GLN B . n 
B 1 345 PRO 345 345 345 PRO PRO B . n 
B 1 346 VAL 346 346 346 VAL VAL B . n 
B 1 347 VAL 347 347 347 VAL VAL B . n 
B 1 348 PHE 348 348 348 PHE PHE B . n 
B 1 349 VAL 349 349 349 VAL VAL B . n 
B 1 350 VAL 350 350 350 VAL VAL B . n 
B 1 351 LEU 351 351 351 LEU LEU B . n 
B 1 352 ASN 352 352 352 ASN ASN B . n 
B 1 353 GLY 353 353 353 GLY GLY B . n 
B 1 354 GLU 354 354 354 GLU GLU B . n 
B 1 355 ASN 355 355 355 ASN ASN B . n 
B 1 356 CYS 356 356 356 CYS CYS B . n 
B 1 357 TRP 357 357 357 TRP TRP B . n 
B 1 358 GLU 358 358 358 GLU GLU B . n 
B 1 359 TYR 359 359 359 TYR TYR B . n 
B 1 360 TYR 360 360 360 TYR TYR B . n 
B 1 361 GLU 361 361 361 GLU GLU B . n 
B 1 362 GLU 362 362 362 GLU GLU B . n 
B 1 363 ASN 363 363 363 ASN ASN B . n 
B 1 364 GLY 364 364 364 GLY GLY B . n 
B 1 365 ILE 365 365 365 ILE ILE B . n 
B 1 366 PRO 366 366 366 PRO PRO B . n 
B 1 367 PHE 367 367 367 PHE PHE B . n 
B 1 368 LEU 368 368 368 LEU LEU B . n 
B 1 369 GLU 369 369 369 GLU GLU B . n 
B 1 370 LYS 370 370 370 LYS LYS B . n 
B 1 371 LEU 371 371 371 LEU LEU B . n 
B 1 372 TYR 372 372 372 TYR TYR B . n 
B 1 373 SER 373 373 373 SER SER B . n 
B 1 374 THR 374 374 374 THR THR B . n 
B 1 375 LEU 375 375 375 LEU LEU B . n 
B 1 376 GLU 376 376 376 GLU GLU B . n 
B 1 377 LYS 377 377 377 LYS LYS B . n 
B 1 378 GLU 378 378 378 GLU GLU B . n 
B 1 379 GLU 379 379 379 GLU GLU B . n 
B 1 380 TRP 380 380 380 TRP TRP B . n 
B 1 381 ILE 381 381 381 ILE ILE B . n 
B 1 382 GLU 382 382 382 GLU GLU B . n 
B 1 383 THR 383 383 383 THR THR B . n 
B 1 384 LEU 384 384 384 LEU LEU B . n 
B 1 385 THR 385 385 385 THR THR B . n 
B 1 386 LEU 386 386 386 LEU LEU B . n 
B 1 387 GLU 387 387 387 GLU GLU B . n 
B 1 388 GLU 388 388 388 GLU GLU B . n 
B 1 389 ALA 389 389 389 ALA ALA B . n 
B 1 390 MET 390 390 390 MET MET B . n 
B 1 391 ARG 391 391 391 ARG ARG B . n 
B 1 392 LYS 392 392 392 LYS LYS B . n 
B 1 393 GLU 393 393 393 GLU GLU B . n 
B 1 394 ASP 394 394 394 ASP ASP B . n 
B 1 395 VAL 395 395 395 VAL VAL B . n 
B 1 396 LYS 396 396 396 LYS LYS B . n 
B 1 397 THR 397 397 397 THR THR B . n 
B 1 398 GLU 398 398 398 GLU GLU B . n 
B 1 399 VAL 399 399 399 VAL VAL B . n 
B 1 400 ILE 400 400 400 ILE ILE B . n 
B 1 401 GLU 401 401 401 GLU GLU B . n 
B 1 402 SER 402 402 402 SER SER B . n 
B 1 403 VAL 403 403 403 VAL VAL B . n 
B 1 404 LYS 404 404 404 LYS LYS B . n 
B 1 405 ALA 405 405 405 ALA ALA B . n 
B 1 406 GLY 406 406 406 GLY GLY B . n 
B 1 407 THR 407 407 407 THR THR B . n 
B 1 408 TRP 408 408 408 TRP TRP B . n 
B 1 409 PHE 409 409 409 PHE PHE B . n 
B 1 410 ASP 410 410 410 ASP ASP B . n 
B 1 411 GLY 411 411 411 GLY GLY B . n 
B 1 412 ASN 412 412 412 ASN ASN B . n 
B 1 413 PHE 413 413 413 PHE PHE B . n 
B 1 414 LEU 414 414 414 LEU LEU B . n 
B 1 415 LYS 415 415 415 LYS LYS B . n 
B 1 416 TRP 416 416 416 TRP TRP B . n 
B 1 417 ILE 417 417 417 ILE ILE B . n 
B 1 418 GLY 418 418 418 GLY GLY B . n 
B 1 419 ASN 419 419 419 ASN ASN B . n 
B 1 420 LYS 420 420 420 LYS LYS B . n 
B 1 421 GLU 421 421 421 GLU GLU B . n 
B 1 422 LYS 422 422 422 LYS LYS B . n 
B 1 423 ASN 423 423 423 ASN ASN B . n 
B 1 424 GLU 424 424 424 GLU GLU B . n 
B 1 425 TYR 425 425 425 TYR TYR B . n 
B 1 426 TRP 426 426 426 TRP TRP B . n 
B 1 427 LYS 427 427 427 LYS LYS B . n 
B 1 428 ILE 428 428 428 ILE ILE B . n 
B 1 429 LEU 429 429 429 LEU LEU B . n 
B 1 430 ILE 430 430 430 ILE ILE B . n 
B 1 431 GLU 431 431 431 GLU GLU B . n 
B 1 432 ALA 432 432 432 ALA ALA B . n 
B 1 433 LYS 433 433 433 LYS LYS B . n 
B 1 434 LYS 434 434 434 LYS LYS B . n 
B 1 435 LYS 435 435 435 LYS LYS B . n 
B 1 436 ALA 436 436 436 ALA ALA B . n 
B 1 437 LYS 437 437 437 LYS LYS B . n 
B 1 438 ASN 438 438 438 ASN ASN B . n 
B 1 439 ASP 439 439 439 ASP ASP B . n 
B 1 440 TYR 440 440 440 TYR TYR B . n 
B 1 441 ILE 441 441 441 ILE ILE B . n 
B 1 442 LEU 442 442 442 LEU LEU B . n 
B 1 443 VAL 443 443 443 VAL VAL B . n 
B 1 444 ALA 444 444 444 ALA ALA B . n 
B 1 445 GLU 445 445 445 GLU GLU B . n 
B 1 446 GLY 446 446 446 GLY GLY B . n 
B 1 447 SER 447 447 447 SER SER B . n 
B 1 448 ASP 448 448 448 ASP ASP B . n 
B 1 449 TRP 449 449 449 TRP TRP B . n 
B 1 450 PHE 450 450 450 PHE PHE B . n 
B 1 451 TRP 451 451 451 TRP TRP B . n 
B 1 452 TRP 452 452 452 TRP TRP B . n 
B 1 453 GLN 453 453 453 GLN GLN B . n 
B 1 454 GLY 454 454 454 GLY GLY B . n 
B 1 455 GLU 455 455 455 GLU GLU B . n 
B 1 456 GLU 456 456 456 GLU GLU B . n 
B 1 457 LYS 457 457 457 LYS LYS B . n 
B 1 458 ALA 458 458 458 ALA ALA B . n 
B 1 459 PRO 459 459 459 PRO PRO B . n 
B 1 460 PHE 460 460 460 PHE PHE B . n 
B 1 461 VAL 461 461 461 VAL VAL B . n 
B 1 462 GLU 462 462 462 GLU GLU B . n 
B 1 463 VAL 463 463 463 VAL VAL B . n 
B 1 464 PHE 464 464 464 PHE PHE B . n 
B 1 465 ASP 465 465 465 ASP ASP B . n 
B 1 466 LYS 466 466 466 LYS LYS B . n 
B 1 467 LEU 467 467 467 LEU LEU B . n 
B 1 468 PHE 468 468 468 PHE PHE B . n 
B 1 469 ARG 469 469 469 ARG ARG B . n 
B 1 470 SER 470 470 470 SER SER B . n 
B 1 471 PHE 471 471 471 PHE PHE B . n 
B 1 472 VAL 472 472 472 VAL VAL B . n 
B 1 473 ARG 473 473 473 ARG ARG B . n 
B 1 474 ARG 474 474 474 ARG ARG B . n 
B 1 475 ALA 475 475 475 ALA ALA B . n 
B 1 476 GLN 476 476 476 GLN GLN B . n 
B 1 477 GLU 477 477 477 GLU GLU B . n 
# 
loop_
_pdbx_branch_scheme.asym_id 
_pdbx_branch_scheme.entity_id 
_pdbx_branch_scheme.mon_id 
_pdbx_branch_scheme.num 
_pdbx_branch_scheme.pdb_asym_id 
_pdbx_branch_scheme.pdb_mon_id 
_pdbx_branch_scheme.pdb_seq_num 
_pdbx_branch_scheme.auth_asym_id 
_pdbx_branch_scheme.auth_mon_id 
_pdbx_branch_scheme.auth_seq_num 
_pdbx_branch_scheme.hetero 
C 2 GLC 1 C GLC 1 A GLC 491 n 
C 2 GLC 2 C GLC 2 A GLC 492 n 
C 2 GLC 3 C GLC 3 A GLC 493 n 
C 2 GLC 4 C GLC 4 A GLC 494 n 
C 2 GLC 5 C GLC 5 A GLC 495 n 
C 2 GLC 6 C GLC 6 A GLC 496 n 
D 2 GLC 1 D GLC 1 B GLC 491 n 
D 2 GLC 2 D GLC 2 B GLC 492 n 
D 2 GLC 3 D GLC 3 B GLC 493 n 
D 2 GLC 4 D GLC 4 B GLC 494 n 
D 2 GLC 5 D GLC 5 B GLC 495 n 
D 2 GLC 6 D GLC 6 B GLC 496 n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        GLC 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   GLC 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
E 3 GOL 1   501 510 GOL GOL A . 
F 3 GOL 1   502 520 GOL GOL A . 
G 3 GOL 1   503 530 GOL GOL A . 
H 3 GOL 1   504 1   GOL GOL A . 
I 3 GOL 1   501 510 GOL GOL B . 
J 3 GOL 1   502 520 GOL GOL B . 
K 4 HOH 1   601 156 HOH HOH A . 
K 4 HOH 2   602 352 HOH HOH A . 
K 4 HOH 3   603 578 HOH HOH A . 
K 4 HOH 4   604 190 HOH HOH A . 
K 4 HOH 5   605 329 HOH HOH A . 
K 4 HOH 6   606 570 HOH HOH A . 
K 4 HOH 7   607 300 HOH HOH A . 
K 4 HOH 8   608 370 HOH HOH A . 
K 4 HOH 9   609 175 HOH HOH A . 
K 4 HOH 10  610 303 HOH HOH A . 
K 4 HOH 11  611 119 HOH HOH A . 
K 4 HOH 12  612 293 HOH HOH A . 
K 4 HOH 13  613 501 HOH HOH A . 
K 4 HOH 14  614 433 HOH HOH A . 
K 4 HOH 15  615 105 HOH HOH A . 
K 4 HOH 16  616 395 HOH HOH A . 
K 4 HOH 17  617 526 HOH HOH A . 
K 4 HOH 18  618 551 HOH HOH A . 
K 4 HOH 19  619 564 HOH HOH A . 
K 4 HOH 20  620 277 HOH HOH A . 
K 4 HOH 21  621 349 HOH HOH A . 
K 4 HOH 22  622 359 HOH HOH A . 
K 4 HOH 23  623 178 HOH HOH A . 
K 4 HOH 24  624 482 HOH HOH A . 
K 4 HOH 25  625 586 HOH HOH A . 
K 4 HOH 26  626 106 HOH HOH A . 
K 4 HOH 27  627 389 HOH HOH A . 
K 4 HOH 28  628 266 HOH HOH A . 
K 4 HOH 29  629 253 HOH HOH A . 
K 4 HOH 30  630 129 HOH HOH A . 
K 4 HOH 31  631 294 HOH HOH A . 
K 4 HOH 32  632 188 HOH HOH A . 
K 4 HOH 33  633 166 HOH HOH A . 
K 4 HOH 34  634 378 HOH HOH A . 
K 4 HOH 35  635 142 HOH HOH A . 
K 4 HOH 36  636 488 HOH HOH A . 
K 4 HOH 37  637 553 HOH HOH A . 
K 4 HOH 38  638 360 HOH HOH A . 
K 4 HOH 39  639 113 HOH HOH A . 
K 4 HOH 40  640 316 HOH HOH A . 
K 4 HOH 41  641 30  HOH HOH A . 
K 4 HOH 42  642 140 HOH HOH A . 
K 4 HOH 43  643 5   HOH HOH A . 
K 4 HOH 44  644 356 HOH HOH A . 
K 4 HOH 45  645 198 HOH HOH A . 
K 4 HOH 46  646 353 HOH HOH A . 
K 4 HOH 47  647 434 HOH HOH A . 
K 4 HOH 48  648 589 HOH HOH A . 
K 4 HOH 49  649 560 HOH HOH A . 
K 4 HOH 50  650 256 HOH HOH A . 
K 4 HOH 51  651 311 HOH HOH A . 
K 4 HOH 52  652 599 HOH HOH A . 
K 4 HOH 53  653 301 HOH HOH A . 
K 4 HOH 54  654 19  HOH HOH A . 
K 4 HOH 55  655 347 HOH HOH A . 
K 4 HOH 56  656 174 HOH HOH A . 
K 4 HOH 57  657 79  HOH HOH A . 
K 4 HOH 58  658 33  HOH HOH A . 
K 4 HOH 59  659 377 HOH HOH A . 
K 4 HOH 60  660 127 HOH HOH A . 
K 4 HOH 61  661 87  HOH HOH A . 
K 4 HOH 62  662 14  HOH HOH A . 
K 4 HOH 63  663 78  HOH HOH A . 
K 4 HOH 64  664 449 HOH HOH A . 
K 4 HOH 65  665 261 HOH HOH A . 
K 4 HOH 66  666 37  HOH HOH A . 
K 4 HOH 67  667 11  HOH HOH A . 
K 4 HOH 68  668 259 HOH HOH A . 
K 4 HOH 69  669 12  HOH HOH A . 
K 4 HOH 70  670 283 HOH HOH A . 
K 4 HOH 71  671 584 HOH HOH A . 
K 4 HOH 72  672 155 HOH HOH A . 
K 4 HOH 73  673 84  HOH HOH A . 
K 4 HOH 74  674 88  HOH HOH A . 
K 4 HOH 75  675 236 HOH HOH A . 
K 4 HOH 76  676 44  HOH HOH A . 
K 4 HOH 77  677 6   HOH HOH A . 
K 4 HOH 78  678 435 HOH HOH A . 
K 4 HOH 79  679 545 HOH HOH A . 
K 4 HOH 80  680 148 HOH HOH A . 
K 4 HOH 81  681 132 HOH HOH A . 
K 4 HOH 82  682 437 HOH HOH A . 
K 4 HOH 83  683 234 HOH HOH A . 
K 4 HOH 84  684 139 HOH HOH A . 
K 4 HOH 85  685 60  HOH HOH A . 
K 4 HOH 86  686 128 HOH HOH A . 
K 4 HOH 87  687 3   HOH HOH A . 
K 4 HOH 88  688 160 HOH HOH A . 
K 4 HOH 89  689 110 HOH HOH A . 
K 4 HOH 90  690 61  HOH HOH A . 
K 4 HOH 91  691 197 HOH HOH A . 
K 4 HOH 92  692 419 HOH HOH A . 
K 4 HOH 93  693 333 HOH HOH A . 
K 4 HOH 94  694 35  HOH HOH A . 
K 4 HOH 95  695 102 HOH HOH A . 
K 4 HOH 96  696 372 HOH HOH A . 
K 4 HOH 97  697 420 HOH HOH A . 
K 4 HOH 98  698 270 HOH HOH A . 
K 4 HOH 99  699 22  HOH HOH A . 
K 4 HOH 100 700 296 HOH HOH A . 
K 4 HOH 101 701 75  HOH HOH A . 
K 4 HOH 102 702 355 HOH HOH A . 
K 4 HOH 103 703 144 HOH HOH A . 
K 4 HOH 104 704 222 HOH HOH A . 
K 4 HOH 105 705 204 HOH HOH A . 
K 4 HOH 106 706 292 HOH HOH A . 
K 4 HOH 107 707 25  HOH HOH A . 
K 4 HOH 108 708 131 HOH HOH A . 
K 4 HOH 109 709 424 HOH HOH A . 
K 4 HOH 110 710 39  HOH HOH A . 
K 4 HOH 111 711 354 HOH HOH A . 
K 4 HOH 112 712 16  HOH HOH A . 
K 4 HOH 113 713 365 HOH HOH A . 
K 4 HOH 114 714 18  HOH HOH A . 
K 4 HOH 115 715 200 HOH HOH A . 
K 4 HOH 116 716 123 HOH HOH A . 
K 4 HOH 117 717 191 HOH HOH A . 
K 4 HOH 118 718 417 HOH HOH A . 
K 4 HOH 119 719 351 HOH HOH A . 
K 4 HOH 120 720 318 HOH HOH A . 
K 4 HOH 121 721 15  HOH HOH A . 
K 4 HOH 122 722 248 HOH HOH A . 
K 4 HOH 123 723 77  HOH HOH A . 
K 4 HOH 124 724 36  HOH HOH A . 
K 4 HOH 125 725 51  HOH HOH A . 
K 4 HOH 126 726 159 HOH HOH A . 
K 4 HOH 127 727 97  HOH HOH A . 
K 4 HOH 128 728 7   HOH HOH A . 
K 4 HOH 129 729 432 HOH HOH A . 
K 4 HOH 130 730 566 HOH HOH A . 
K 4 HOH 131 731 43  HOH HOH A . 
K 4 HOH 132 732 217 HOH HOH A . 
K 4 HOH 133 733 1   HOH HOH A . 
K 4 HOH 134 734 28  HOH HOH A . 
K 4 HOH 135 735 158 HOH HOH A . 
K 4 HOH 136 736 46  HOH HOH A . 
K 4 HOH 137 737 27  HOH HOH A . 
K 4 HOH 138 738 196 HOH HOH A . 
K 4 HOH 139 739 52  HOH HOH A . 
K 4 HOH 140 740 344 HOH HOH A . 
K 4 HOH 141 741 364 HOH HOH A . 
K 4 HOH 142 742 9   HOH HOH A . 
K 4 HOH 143 743 134 HOH HOH A . 
K 4 HOH 144 744 89  HOH HOH A . 
K 4 HOH 145 745 212 HOH HOH A . 
K 4 HOH 146 746 263 HOH HOH A . 
K 4 HOH 147 747 45  HOH HOH A . 
K 4 HOH 148 748 146 HOH HOH A . 
K 4 HOH 149 749 567 HOH HOH A . 
K 4 HOH 150 750 251 HOH HOH A . 
K 4 HOH 151 751 465 HOH HOH A . 
K 4 HOH 152 752 308 HOH HOH A . 
K 4 HOH 153 753 31  HOH HOH A . 
K 4 HOH 154 754 10  HOH HOH A . 
K 4 HOH 155 755 409 HOH HOH A . 
K 4 HOH 156 756 124 HOH HOH A . 
K 4 HOH 157 757 116 HOH HOH A . 
K 4 HOH 158 758 103 HOH HOH A . 
K 4 HOH 159 759 593 HOH HOH A . 
K 4 HOH 160 760 258 HOH HOH A . 
K 4 HOH 161 761 157 HOH HOH A . 
K 4 HOH 162 762 115 HOH HOH A . 
K 4 HOH 163 763 141 HOH HOH A . 
K 4 HOH 164 764 59  HOH HOH A . 
K 4 HOH 165 765 181 HOH HOH A . 
K 4 HOH 166 766 273 HOH HOH A . 
K 4 HOH 167 767 493 HOH HOH A . 
K 4 HOH 168 768 182 HOH HOH A . 
K 4 HOH 169 769 416 HOH HOH A . 
K 4 HOH 170 770 507 HOH HOH A . 
K 4 HOH 171 771 304 HOH HOH A . 
K 4 HOH 172 772 458 HOH HOH A . 
K 4 HOH 173 773 162 HOH HOH A . 
K 4 HOH 174 774 108 HOH HOH A . 
K 4 HOH 175 775 285 HOH HOH A . 
K 4 HOH 176 776 539 HOH HOH A . 
K 4 HOH 177 777 169 HOH HOH A . 
K 4 HOH 178 778 490 HOH HOH A . 
K 4 HOH 179 779 29  HOH HOH A . 
K 4 HOH 180 780 177 HOH HOH A . 
K 4 HOH 181 781 418 HOH HOH A . 
K 4 HOH 182 782 246 HOH HOH A . 
K 4 HOH 183 783 555 HOH HOH A . 
K 4 HOH 184 784 241 HOH HOH A . 
K 4 HOH 185 785 4   HOH HOH A . 
K 4 HOH 186 786 227 HOH HOH A . 
K 4 HOH 187 787 161 HOH HOH A . 
K 4 HOH 188 788 287 HOH HOH A . 
K 4 HOH 189 789 516 HOH HOH A . 
K 4 HOH 190 790 149 HOH HOH A . 
K 4 HOH 191 791 92  HOH HOH A . 
K 4 HOH 192 792 125 HOH HOH A . 
K 4 HOH 193 793 252 HOH HOH A . 
K 4 HOH 194 794 32  HOH HOH A . 
K 4 HOH 195 795 267 HOH HOH A . 
K 4 HOH 196 796 67  HOH HOH A . 
K 4 HOH 197 797 147 HOH HOH A . 
K 4 HOH 198 798 167 HOH HOH A . 
K 4 HOH 199 799 48  HOH HOH A . 
K 4 HOH 200 800 223 HOH HOH A . 
K 4 HOH 201 801 64  HOH HOH A . 
K 4 HOH 202 802 607 HOH HOH A . 
K 4 HOH 203 803 606 HOH HOH A . 
K 4 HOH 204 804 130 HOH HOH A . 
K 4 HOH 205 805 242 HOH HOH A . 
K 4 HOH 206 806 264 HOH HOH A . 
K 4 HOH 207 807 615 HOH HOH A . 
K 4 HOH 208 808 195 HOH HOH A . 
K 4 HOH 209 809 219 HOH HOH A . 
K 4 HOH 210 810 221 HOH HOH A . 
K 4 HOH 211 811 70  HOH HOH A . 
K 4 HOH 212 812 91  HOH HOH A . 
K 4 HOH 213 813 173 HOH HOH A . 
K 4 HOH 214 814 23  HOH HOH A . 
K 4 HOH 215 815 81  HOH HOH A . 
K 4 HOH 216 816 425 HOH HOH A . 
K 4 HOH 217 817 2   HOH HOH A . 
K 4 HOH 218 818 17  HOH HOH A . 
K 4 HOH 219 819 271 HOH HOH A . 
K 4 HOH 220 820 396 HOH HOH A . 
K 4 HOH 221 821 565 HOH HOH A . 
K 4 HOH 222 822 406 HOH HOH A . 
K 4 HOH 223 823 602 HOH HOH A . 
K 4 HOH 224 824 441 HOH HOH A . 
K 4 HOH 225 825 326 HOH HOH A . 
K 4 HOH 226 826 275 HOH HOH A . 
K 4 HOH 227 827 427 HOH HOH A . 
K 4 HOH 228 828 421 HOH HOH A . 
K 4 HOH 229 829 390 HOH HOH A . 
K 4 HOH 230 830 523 HOH HOH A . 
K 4 HOH 231 831 585 HOH HOH A . 
K 4 HOH 232 832 93  HOH HOH A . 
K 4 HOH 233 833 80  HOH HOH A . 
K 4 HOH 234 834 403 HOH HOH A . 
K 4 HOH 235 835 407 HOH HOH A . 
K 4 HOH 236 836 476 HOH HOH A . 
K 4 HOH 237 837 494 HOH HOH A . 
K 4 HOH 238 838 508 HOH HOH A . 
K 4 HOH 239 839 281 HOH HOH A . 
K 4 HOH 240 840 506 HOH HOH A . 
K 4 HOH 241 841 492 HOH HOH A . 
K 4 HOH 242 842 597 HOH HOH A . 
K 4 HOH 243 843 96  HOH HOH A . 
K 4 HOH 244 844 408 HOH HOH A . 
K 4 HOH 245 845 497 HOH HOH A . 
K 4 HOH 246 846 401 HOH HOH A . 
K 4 HOH 247 847 288 HOH HOH A . 
K 4 HOH 248 848 532 HOH HOH A . 
K 4 HOH 249 849 20  HOH HOH A . 
K 4 HOH 250 850 145 HOH HOH A . 
K 4 HOH 251 851 179 HOH HOH A . 
K 4 HOH 252 852 298 HOH HOH A . 
K 4 HOH 253 853 580 HOH HOH A . 
K 4 HOH 254 854 381 HOH HOH A . 
K 4 HOH 255 855 209 HOH HOH A . 
K 4 HOH 256 856 207 HOH HOH A . 
K 4 HOH 257 857 438 HOH HOH A . 
K 4 HOH 258 858 604 HOH HOH A . 
K 4 HOH 259 859 272 HOH HOH A . 
K 4 HOH 260 860 450 HOH HOH A . 
K 4 HOH 261 861 176 HOH HOH A . 
K 4 HOH 262 862 549 HOH HOH A . 
K 4 HOH 263 863 620 HOH HOH A . 
K 4 HOH 264 864 335 HOH HOH A . 
K 4 HOH 265 865 170 HOH HOH A . 
K 4 HOH 266 866 573 HOH HOH A . 
K 4 HOH 267 867 387 HOH HOH A . 
K 4 HOH 268 868 563 HOH HOH A . 
K 4 HOH 269 869 47  HOH HOH A . 
K 4 HOH 270 870 400 HOH HOH A . 
K 4 HOH 271 871 363 HOH HOH A . 
K 4 HOH 272 872 192 HOH HOH A . 
K 4 HOH 273 873 546 HOH HOH A . 
K 4 HOH 274 874 208 HOH HOH A . 
K 4 HOH 275 875 350 HOH HOH A . 
K 4 HOH 276 876 495 HOH HOH A . 
K 4 HOH 277 877 436 HOH HOH A . 
K 4 HOH 278 878 522 HOH HOH A . 
K 4 HOH 279 879 447 HOH HOH A . 
K 4 HOH 280 880 240 HOH HOH A . 
K 4 HOH 281 881 231 HOH HOH A . 
K 4 HOH 282 882 423 HOH HOH A . 
K 4 HOH 283 883 600 HOH HOH A . 
K 4 HOH 284 884 348 HOH HOH A . 
K 4 HOH 285 885 603 HOH HOH A . 
K 4 HOH 286 886 290 HOH HOH A . 
K 4 HOH 287 887 202 HOH HOH A . 
K 4 HOH 288 888 577 HOH HOH A . 
K 4 HOH 289 889 574 HOH HOH A . 
K 4 HOH 290 890 598 HOH HOH A . 
K 4 HOH 291 891 415 HOH HOH A . 
K 4 HOH 292 892 595 HOH HOH A . 
K 4 HOH 293 893 529 HOH HOH A . 
K 4 HOH 294 894 581 HOH HOH A . 
K 4 HOH 295 895 284 HOH HOH A . 
K 4 HOH 296 896 211 HOH HOH A . 
K 4 HOH 297 897 238 HOH HOH A . 
K 4 HOH 298 898 376 HOH HOH A . 
K 4 HOH 299 899 164 HOH HOH A . 
K 4 HOH 300 900 375 HOH HOH A . 
K 4 HOH 301 901 530 HOH HOH A . 
K 4 HOH 302 902 554 HOH HOH A . 
K 4 HOH 303 903 104 HOH HOH A . 
K 4 HOH 304 904 461 HOH HOH A . 
K 4 HOH 305 905 440 HOH HOH A . 
K 4 HOH 306 906 534 HOH HOH A . 
K 4 HOH 307 907 525 HOH HOH A . 
K 4 HOH 308 908 561 HOH HOH A . 
K 4 HOH 309 909 557 HOH HOH A . 
K 4 HOH 310 910 76  HOH HOH A . 
K 4 HOH 311 911 500 HOH HOH A . 
K 4 HOH 312 912 331 HOH HOH A . 
K 4 HOH 313 913 384 HOH HOH A . 
K 4 HOH 314 914 618 HOH HOH A . 
K 4 HOH 315 915 591 HOH HOH A . 
K 4 HOH 316 916 330 HOH HOH A . 
K 4 HOH 317 917 601 HOH HOH A . 
K 4 HOH 318 918 512 HOH HOH A . 
K 4 HOH 319 919 481 HOH HOH A . 
K 4 HOH 320 920 430 HOH HOH A . 
K 4 HOH 321 921 611 HOH HOH A . 
K 4 HOH 322 922 314 HOH HOH A . 
K 4 HOH 323 923 276 HOH HOH A . 
K 4 HOH 324 924 524 HOH HOH A . 
K 4 HOH 325 925 535 HOH HOH A . 
K 4 HOH 326 926 515 HOH HOH A . 
K 4 HOH 327 927 379 HOH HOH A . 
K 4 HOH 328 928 619 HOH HOH A . 
K 4 HOH 329 929 610 HOH HOH A . 
K 4 HOH 330 930 533 HOH HOH A . 
K 4 HOH 331 931 463 HOH HOH A . 
K 4 HOH 332 932 451 HOH HOH A . 
K 4 HOH 333 933 312 HOH HOH A . 
K 4 HOH 334 934 587 HOH HOH A . 
K 4 HOH 335 935 442 HOH HOH A . 
K 4 HOH 336 936 459 HOH HOH A . 
K 4 HOH 337 937 374 HOH HOH A . 
K 4 HOH 338 938 528 HOH HOH A . 
K 4 HOH 339 939 499 HOH HOH A . 
K 4 HOH 340 940 215 HOH HOH A . 
K 4 HOH 341 941 518 HOH HOH A . 
K 4 HOH 342 942 616 HOH HOH A . 
K 4 HOH 343 943 340 HOH HOH A . 
L 4 HOH 1   601 391 HOH HOH B . 
L 4 HOH 2   602 517 HOH HOH B . 
L 4 HOH 3   603 265 HOH HOH B . 
L 4 HOH 4   604 392 HOH HOH B . 
L 4 HOH 5   605 297 HOH HOH B . 
L 4 HOH 6   606 504 HOH HOH B . 
L 4 HOH 7   607 572 HOH HOH B . 
L 4 HOH 8   608 548 HOH HOH B . 
L 4 HOH 9   609 514 HOH HOH B . 
L 4 HOH 10  610 274 HOH HOH B . 
L 4 HOH 11  611 54  HOH HOH B . 
L 4 HOH 12  612 321 HOH HOH B . 
L 4 HOH 13  613 171 HOH HOH B . 
L 4 HOH 14  614 380 HOH HOH B . 
L 4 HOH 15  615 109 HOH HOH B . 
L 4 HOH 16  616 477 HOH HOH B . 
L 4 HOH 17  617 319 HOH HOH B . 
L 4 HOH 18  618 225 HOH HOH B . 
L 4 HOH 19  619 163 HOH HOH B . 
L 4 HOH 20  620 187 HOH HOH B . 
L 4 HOH 21  621 558 HOH HOH B . 
L 4 HOH 22  622 571 HOH HOH B . 
L 4 HOH 23  623 122 HOH HOH B . 
L 4 HOH 24  624 260 HOH HOH B . 
L 4 HOH 25  625 339 HOH HOH B . 
L 4 HOH 26  626 68  HOH HOH B . 
L 4 HOH 27  627 143 HOH HOH B . 
L 4 HOH 28  628 216 HOH HOH B . 
L 4 HOH 29  629 98  HOH HOH B . 
L 4 HOH 30  630 367 HOH HOH B . 
L 4 HOH 31  631 510 HOH HOH B . 
L 4 HOH 32  632 101 HOH HOH B . 
L 4 HOH 33  633 268 HOH HOH B . 
L 4 HOH 34  634 220 HOH HOH B . 
L 4 HOH 35  635 422 HOH HOH B . 
L 4 HOH 36  636 21  HOH HOH B . 
L 4 HOH 37  637 455 HOH HOH B . 
L 4 HOH 38  638 82  HOH HOH B . 
L 4 HOH 39  639 57  HOH HOH B . 
L 4 HOH 40  640 117 HOH HOH B . 
L 4 HOH 41  641 457 HOH HOH B . 
L 4 HOH 42  642 398 HOH HOH B . 
L 4 HOH 43  643 468 HOH HOH B . 
L 4 HOH 44  644 111 HOH HOH B . 
L 4 HOH 45  645 336 HOH HOH B . 
L 4 HOH 46  646 107 HOH HOH B . 
L 4 HOH 47  647 445 HOH HOH B . 
L 4 HOH 48  648 90  HOH HOH B . 
L 4 HOH 49  649 537 HOH HOH B . 
L 4 HOH 50  650 135 HOH HOH B . 
L 4 HOH 51  651 467 HOH HOH B . 
L 4 HOH 52  652 210 HOH HOH B . 
L 4 HOH 53  653 118 HOH HOH B . 
L 4 HOH 54  654 410 HOH HOH B . 
L 4 HOH 55  655 257 HOH HOH B . 
L 4 HOH 56  656 583 HOH HOH B . 
L 4 HOH 57  657 69  HOH HOH B . 
L 4 HOH 58  658 41  HOH HOH B . 
L 4 HOH 59  659 73  HOH HOH B . 
L 4 HOH 60  660 250 HOH HOH B . 
L 4 HOH 61  661 53  HOH HOH B . 
L 4 HOH 62  662 153 HOH HOH B . 
L 4 HOH 63  663 151 HOH HOH B . 
L 4 HOH 64  664 150 HOH HOH B . 
L 4 HOH 65  665 49  HOH HOH B . 
L 4 HOH 66  666 201 HOH HOH B . 
L 4 HOH 67  667 575 HOH HOH B . 
L 4 HOH 68  668 213 HOH HOH B . 
L 4 HOH 69  669 71  HOH HOH B . 
L 4 HOH 70  670 85  HOH HOH B . 
L 4 HOH 71  671 237 HOH HOH B . 
L 4 HOH 72  672 489 HOH HOH B . 
L 4 HOH 73  673 473 HOH HOH B . 
L 4 HOH 74  674 373 HOH HOH B . 
L 4 HOH 75  675 244 HOH HOH B . 
L 4 HOH 76  676 245 HOH HOH B . 
L 4 HOH 77  677 121 HOH HOH B . 
L 4 HOH 78  678 454 HOH HOH B . 
L 4 HOH 79  679 249 HOH HOH B . 
L 4 HOH 80  680 199 HOH HOH B . 
L 4 HOH 81  681 26  HOH HOH B . 
L 4 HOH 82  682 72  HOH HOH B . 
L 4 HOH 83  683 486 HOH HOH B . 
L 4 HOH 84  684 328 HOH HOH B . 
L 4 HOH 85  685 346 HOH HOH B . 
L 4 HOH 86  686 34  HOH HOH B . 
L 4 HOH 87  687 180 HOH HOH B . 
L 4 HOH 88  688 24  HOH HOH B . 
L 4 HOH 89  689 361 HOH HOH B . 
L 4 HOH 90  690 38  HOH HOH B . 
L 4 HOH 91  691 94  HOH HOH B . 
L 4 HOH 92  692 183 HOH HOH B . 
L 4 HOH 93  693 126 HOH HOH B . 
L 4 HOH 94  694 239 HOH HOH B . 
L 4 HOH 95  695 509 HOH HOH B . 
L 4 HOH 96  696 444 HOH HOH B . 
L 4 HOH 97  697 13  HOH HOH B . 
L 4 HOH 98  698 513 HOH HOH B . 
L 4 HOH 99  699 95  HOH HOH B . 
L 4 HOH 100 700 50  HOH HOH B . 
L 4 HOH 101 701 305 HOH HOH B . 
L 4 HOH 102 702 83  HOH HOH B . 
L 4 HOH 103 703 302 HOH HOH B . 
L 4 HOH 104 704 186 HOH HOH B . 
L 4 HOH 105 705 100 HOH HOH B . 
L 4 HOH 106 706 394 HOH HOH B . 
L 4 HOH 107 707 483 HOH HOH B . 
L 4 HOH 108 708 120 HOH HOH B . 
L 4 HOH 109 709 307 HOH HOH B . 
L 4 HOH 110 710 299 HOH HOH B . 
L 4 HOH 111 711 86  HOH HOH B . 
L 4 HOH 112 712 8   HOH HOH B . 
L 4 HOH 113 713 74  HOH HOH B . 
L 4 HOH 114 714 562 HOH HOH B . 
L 4 HOH 115 715 168 HOH HOH B . 
L 4 HOH 116 716 193 HOH HOH B . 
L 4 HOH 117 717 206 HOH HOH B . 
L 4 HOH 118 718 413 HOH HOH B . 
L 4 HOH 119 719 99  HOH HOH B . 
L 4 HOH 120 720 368 HOH HOH B . 
L 4 HOH 121 721 475 HOH HOH B . 
L 4 HOH 122 722 315 HOH HOH B . 
L 4 HOH 123 723 324 HOH HOH B . 
L 4 HOH 124 724 332 HOH HOH B . 
L 4 HOH 125 725 133 HOH HOH B . 
L 4 HOH 126 726 608 HOH HOH B . 
L 4 HOH 127 727 40  HOH HOH B . 
L 4 HOH 128 728 397 HOH HOH B . 
L 4 HOH 129 729 243 HOH HOH B . 
L 4 HOH 130 730 138 HOH HOH B . 
L 4 HOH 131 731 184 HOH HOH B . 
L 4 HOH 132 732 203 HOH HOH B . 
L 4 HOH 133 733 341 HOH HOH B . 
L 4 HOH 134 734 254 HOH HOH B . 
L 4 HOH 135 735 498 HOH HOH B . 
L 4 HOH 136 736 228 HOH HOH B . 
L 4 HOH 137 737 342 HOH HOH B . 
L 4 HOH 138 738 291 HOH HOH B . 
L 4 HOH 139 739 279 HOH HOH B . 
L 4 HOH 140 740 137 HOH HOH B . 
L 4 HOH 141 741 205 HOH HOH B . 
L 4 HOH 142 742 402 HOH HOH B . 
L 4 HOH 143 743 278 HOH HOH B . 
L 4 HOH 144 744 313 HOH HOH B . 
L 4 HOH 145 745 543 HOH HOH B . 
L 4 HOH 146 746 393 HOH HOH B . 
L 4 HOH 147 747 358 HOH HOH B . 
L 4 HOH 148 748 232 HOH HOH B . 
L 4 HOH 149 749 269 HOH HOH B . 
L 4 HOH 150 750 214 HOH HOH B . 
L 4 HOH 151 751 386 HOH HOH B . 
L 4 HOH 152 752 317 HOH HOH B . 
L 4 HOH 153 753 613 HOH HOH B . 
L 4 HOH 154 754 594 HOH HOH B . 
L 4 HOH 155 755 66  HOH HOH B . 
L 4 HOH 156 756 446 HOH HOH B . 
L 4 HOH 157 757 247 HOH HOH B . 
L 4 HOH 158 758 136 HOH HOH B . 
L 4 HOH 159 759 58  HOH HOH B . 
L 4 HOH 160 760 426 HOH HOH B . 
L 4 HOH 161 761 456 HOH HOH B . 
L 4 HOH 162 762 521 HOH HOH B . 
L 4 HOH 163 763 588 HOH HOH B . 
L 4 HOH 164 764 472 HOH HOH B . 
L 4 HOH 165 765 568 HOH HOH B . 
L 4 HOH 166 766 582 HOH HOH B . 
L 4 HOH 167 767 362 HOH HOH B . 
L 4 HOH 168 768 154 HOH HOH B . 
L 4 HOH 169 769 218 HOH HOH B . 
L 4 HOH 170 770 612 HOH HOH B . 
L 4 HOH 171 771 65  HOH HOH B . 
L 4 HOH 172 772 235 HOH HOH B . 
L 4 HOH 173 773 286 HOH HOH B . 
L 4 HOH 174 774 226 HOH HOH B . 
L 4 HOH 175 775 527 HOH HOH B . 
L 4 HOH 176 776 194 HOH HOH B . 
L 4 HOH 177 777 165 HOH HOH B . 
L 4 HOH 178 778 431 HOH HOH B . 
L 4 HOH 179 779 338 HOH HOH B . 
L 4 HOH 180 780 412 HOH HOH B . 
L 4 HOH 181 781 320 HOH HOH B . 
L 4 HOH 182 782 617 HOH HOH B . 
L 4 HOH 183 783 224 HOH HOH B . 
L 4 HOH 184 784 42  HOH HOH B . 
L 4 HOH 185 785 114 HOH HOH B . 
L 4 HOH 186 786 519 HOH HOH B . 
L 4 HOH 187 787 289 HOH HOH B . 
L 4 HOH 188 788 411 HOH HOH B . 
L 4 HOH 189 789 172 HOH HOH B . 
L 4 HOH 190 790 63  HOH HOH B . 
L 4 HOH 191 791 576 HOH HOH B . 
L 4 HOH 192 792 480 HOH HOH B . 
L 4 HOH 193 793 452 HOH HOH B . 
L 4 HOH 194 794 337 HOH HOH B . 
L 4 HOH 195 795 556 HOH HOH B . 
L 4 HOH 196 796 322 HOH HOH B . 
L 4 HOH 197 797 414 HOH HOH B . 
L 4 HOH 198 798 471 HOH HOH B . 
L 4 HOH 199 799 152 HOH HOH B . 
L 4 HOH 200 800 62  HOH HOH B . 
L 4 HOH 201 801 485 HOH HOH B . 
L 4 HOH 202 802 605 HOH HOH B . 
L 4 HOH 203 803 56  HOH HOH B . 
L 4 HOH 204 804 233 HOH HOH B . 
L 4 HOH 205 805 255 HOH HOH B . 
L 4 HOH 206 806 112 HOH HOH B . 
L 4 HOH 207 807 282 HOH HOH B . 
L 4 HOH 208 808 511 HOH HOH B . 
L 4 HOH 209 809 428 HOH HOH B . 
L 4 HOH 210 810 399 HOH HOH B . 
L 4 HOH 211 811 536 HOH HOH B . 
L 4 HOH 212 812 262 HOH HOH B . 
L 4 HOH 213 813 323 HOH HOH B . 
L 4 HOH 214 814 474 HOH HOH B . 
L 4 HOH 215 815 460 HOH HOH B . 
L 4 HOH 216 816 345 HOH HOH B . 
L 4 HOH 217 817 484 HOH HOH B . 
L 4 HOH 218 818 542 HOH HOH B . 
L 4 HOH 219 819 366 HOH HOH B . 
L 4 HOH 220 820 295 HOH HOH B . 
L 4 HOH 221 821 189 HOH HOH B . 
L 4 HOH 222 822 464 HOH HOH B . 
L 4 HOH 223 823 538 HOH HOH B . 
L 4 HOH 224 824 478 HOH HOH B . 
L 4 HOH 225 825 383 HOH HOH B . 
L 4 HOH 226 826 280 HOH HOH B . 
L 4 HOH 227 827 469 HOH HOH B . 
L 4 HOH 228 828 309 HOH HOH B . 
L 4 HOH 229 829 439 HOH HOH B . 
L 4 HOH 230 830 404 HOH HOH B . 
L 4 HOH 231 831 479 HOH HOH B . 
L 4 HOH 232 832 230 HOH HOH B . 
L 4 HOH 233 833 334 HOH HOH B . 
L 4 HOH 234 834 306 HOH HOH B . 
L 4 HOH 235 835 371 HOH HOH B . 
L 4 HOH 236 836 448 HOH HOH B . 
L 4 HOH 237 837 503 HOH HOH B . 
L 4 HOH 238 838 343 HOH HOH B . 
L 4 HOH 239 839 388 HOH HOH B . 
L 4 HOH 240 840 547 HOH HOH B . 
L 4 HOH 241 841 579 HOH HOH B . 
L 4 HOH 242 842 590 HOH HOH B . 
L 4 HOH 243 843 496 HOH HOH B . 
L 4 HOH 244 844 405 HOH HOH B . 
L 4 HOH 245 845 491 HOH HOH B . 
L 4 HOH 246 846 592 HOH HOH B . 
L 4 HOH 247 847 505 HOH HOH B . 
L 4 HOH 248 848 229 HOH HOH B . 
L 4 HOH 249 849 559 HOH HOH B . 
L 4 HOH 250 850 429 HOH HOH B . 
L 4 HOH 251 851 569 HOH HOH B . 
L 4 HOH 252 852 185 HOH HOH B . 
L 4 HOH 253 853 541 HOH HOH B . 
L 4 HOH 254 854 327 HOH HOH B . 
L 4 HOH 255 855 382 HOH HOH B . 
L 4 HOH 256 856 552 HOH HOH B . 
L 4 HOH 257 857 596 HOH HOH B . 
L 4 HOH 258 858 369 HOH HOH B . 
L 4 HOH 259 859 357 HOH HOH B . 
L 4 HOH 260 860 443 HOH HOH B . 
L 4 HOH 261 861 550 HOH HOH B . 
L 4 HOH 262 862 310 HOH HOH B . 
L 4 HOH 263 863 609 HOH HOH B . 
L 4 HOH 264 864 325 HOH HOH B . 
L 4 HOH 265 865 453 HOH HOH B . 
L 4 HOH 266 866 466 HOH HOH B . 
L 4 HOH 267 867 502 HOH HOH B . 
L 4 HOH 268 868 531 HOH HOH B . 
L 4 HOH 269 869 614 HOH HOH B . 
L 4 HOH 270 870 544 HOH HOH B . 
L 4 HOH 271 871 540 HOH HOH B . 
L 4 HOH 272 872 462 HOH HOH B . 
L 4 HOH 273 873 520 HOH HOH B . 
L 4 HOH 274 874 470 HOH HOH B . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A GLU 456 ? CG  ? A GLU 456 CG  
2  1 Y 1 A GLU 456 ? CD  ? A GLU 456 CD  
3  1 Y 1 A GLU 456 ? OE1 ? A GLU 456 OE1 
4  1 Y 1 A GLU 456 ? OE2 ? A GLU 456 OE2 
5  1 Y 1 A LYS 457 ? CG  ? A LYS 457 CG  
6  1 Y 1 A LYS 457 ? CD  ? A LYS 457 CD  
7  1 Y 1 A LYS 457 ? CE  ? A LYS 457 CE  
8  1 Y 1 A LYS 457 ? NZ  ? A LYS 457 NZ  
9  1 Y 1 B GLU 120 ? CG  ? B GLU 120 CG  
10 1 Y 1 B GLU 120 ? CD  ? B GLU 120 CD  
11 1 Y 1 B GLU 120 ? OE1 ? B GLU 120 OE1 
12 1 Y 1 B GLU 120 ? OE2 ? B GLU 120 OE2 
13 1 Y 1 B LYS 121 ? CG  ? B LYS 121 CG  
14 1 Y 1 B LYS 121 ? CD  ? B LYS 121 CD  
15 1 Y 1 B LYS 121 ? CE  ? B LYS 121 CE  
16 1 Y 1 B LYS 121 ? NZ  ? B LYS 121 NZ  
17 1 Y 1 B GLU 455 ? CG  ? B GLU 455 CG  
18 1 Y 1 B GLU 455 ? CD  ? B GLU 455 CD  
19 1 Y 1 B GLU 455 ? OE1 ? B GLU 455 OE1 
20 1 Y 1 B GLU 455 ? OE2 ? B GLU 455 OE2 
21 1 Y 1 B GLU 456 ? CG  ? B GLU 456 CG  
22 1 Y 1 B GLU 456 ? CD  ? B GLU 456 CD  
23 1 Y 1 B GLU 456 ? OE1 ? B GLU 456 OE1 
24 1 Y 1 B GLU 456 ? OE2 ? B GLU 456 OE2 
25 1 Y 1 B LYS 457 ? CG  ? B LYS 457 CG  
26 1 Y 1 B LYS 457 ? CD  ? B LYS 457 CD  
27 1 Y 1 B LYS 457 ? CE  ? B LYS 457 CE  
28 1 Y 1 B LYS 457 ? NZ  ? B LYS 457 NZ  
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? '(1.13_2998: ???)' 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .                  2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .                  3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? .                  4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   96.15 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9IHW 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     61.330 
_cell.length_a_esd                 ? 
_cell.length_b                     41.150 
_cell.length_b_esd                 ? 
_cell.length_c                     194.150 
_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                         9IHW 
_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                   9IHW 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.13 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          42.18 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.1 M Sodium citrate, pH 4.2, 20% PEG 3350' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            338 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-10-05 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.97918 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'SSRF BEAMLINE BL10U2' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97918 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL10U2 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9IHW 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.64 
_reflns.d_resolution_low                               64.34 
_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                                     118846 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.9 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.0 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          9.9 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               0.90 
_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                                0.220 
_reflns.pdbx_Rpim_I_all                                0.091 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       712495 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.990 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.199 
_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                                    1.64 
_reflns_shell.d_res_low                                     1.68 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           45146 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             8687 
_reflns_shell.percent_possible_obs                          99.9 
_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                               5.2 
_reflns_shell.pdbx_chi_squared                              0.83 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     1.5 
_reflns_shell.pdbx_Rrim_I_all                               1.584 
_reflns_shell.pdbx_Rpim_I_all                               0.695 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.513 
_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                                  1.417 
_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                                 9IHW 
_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                            1.640 
_refine.ls_d_res_low                             60.977 
_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                     118828 
_refine.ls_number_reflns_R_free                  5863 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.80 
_refine.ls_percent_reflns_R_free                 4.93 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1700 
_refine.ls_R_factor_R_free                       0.1998 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1685 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          0.71 
_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                 19.40 
_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                            0.17 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.640 
_refine_hist.d_res_low                        60.977 
_refine_hist.number_atoms_solvent             617 
_refine_hist.number_atoms_total               8847 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        8224 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         6 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.006 ? 8473  ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.883 ? 11479 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 5.037 ? 7080  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.051 ? 1230  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.006 ? 1424  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.6400 1.6586 . . 203 3701 100.00 . . . . 0.2744 . . . . . . . . . . . 0.2924 
'X-RAY DIFFRACTION' 1.6586 1.6782 . . 169 3728 100.00 . . . . 0.2675 . . . . . . . . . . . 0.3070 
'X-RAY DIFFRACTION' 1.6782 1.6986 . . 199 3741 100.00 . . . . 0.2553 . . . . . . . . . . . 0.2667 
'X-RAY DIFFRACTION' 1.6986 1.7201 . . 179 3793 100.00 . . . . 0.2416 . . . . . . . . . . . 0.2436 
'X-RAY DIFFRACTION' 1.7201 1.7428 . . 197 3681 100.00 . . . . 0.2242 . . . . . . . . . . . 0.2692 
'X-RAY DIFFRACTION' 1.7428 1.7666 . . 188 3774 100.00 . . . . 0.2199 . . . . . . . . . . . 0.2441 
'X-RAY DIFFRACTION' 1.7666 1.7919 . . 191 3783 100.00 . . . . 0.2096 . . . . . . . . . . . 0.2340 
'X-RAY DIFFRACTION' 1.7919 1.8186 . . 192 3671 100.00 . . . . 0.1991 . . . . . . . . . . . 0.2528 
'X-RAY DIFFRACTION' 1.8186 1.8470 . . 179 3806 100.00 . . . . 0.1963 . . . . . . . . . . . 0.2737 
'X-RAY DIFFRACTION' 1.8470 1.8773 . . 209 3719 100.00 . . . . 0.1882 . . . . . . . . . . . 0.2192 
'X-RAY DIFFRACTION' 1.8773 1.9097 . . 170 3749 100.00 . . . . 0.1869 . . . . . . . . . . . 0.2504 
'X-RAY DIFFRACTION' 1.9097 1.9444 . . 205 3781 100.00 . . . . 0.1732 . . . . . . . . . . . 0.2097 
'X-RAY DIFFRACTION' 1.9444 1.9818 . . 214 3715 100.00 . . . . 0.1738 . . . . . . . . . . . 0.2148 
'X-RAY DIFFRACTION' 1.9818 2.0223 . . 205 3710 100.00 . . . . 0.1689 . . . . . . . . . . . 0.1998 
'X-RAY DIFFRACTION' 2.0223 2.0663 . . 185 3806 100.00 . . . . 0.1684 . . . . . . . . . . . 0.2278 
'X-RAY DIFFRACTION' 2.0663 2.1143 . . 175 3764 100.00 . . . . 0.1667 . . . . . . . . . . . 0.1877 
'X-RAY DIFFRACTION' 2.1143 2.1672 . . 192 3781 100.00 . . . . 0.1685 . . . . . . . . . . . 0.2198 
'X-RAY DIFFRACTION' 2.1672 2.2258 . . 210 3704 100.00 . . . . 0.1705 . . . . . . . . . . . 0.1992 
'X-RAY DIFFRACTION' 2.2258 2.2913 . . 215 3776 100.00 . . . . 0.1691 . . . . . . . . . . . 0.1983 
'X-RAY DIFFRACTION' 2.2913 2.3653 . . 208 3711 100.00 . . . . 0.1748 . . . . . . . . . . . 0.2247 
'X-RAY DIFFRACTION' 2.3653 2.4498 . . 169 3837 100.00 . . . . 0.1747 . . . . . . . . . . . 0.2285 
'X-RAY DIFFRACTION' 2.4498 2.5479 . . 196 3775 100.00 . . . . 0.1674 . . . . . . . . . . . 0.2005 
'X-RAY DIFFRACTION' 2.5479 2.6639 . . 154 3754 100.00 . . . . 0.1618 . . . . . . . . . . . 0.1925 
'X-RAY DIFFRACTION' 2.6639 2.8043 . . 191 3803 100.00 . . . . 0.1585 . . . . . . . . . . . 0.1837 
'X-RAY DIFFRACTION' 2.8043 2.9800 . . 200 3778 100.00 . . . . 0.1574 . . . . . . . . . . . 0.1864 
'X-RAY DIFFRACTION' 2.9800 3.2101 . . 235 3793 100.00 . . . . 0.1511 . . . . . . . . . . . 0.1731 
'X-RAY DIFFRACTION' 3.2101 3.5331 . . 176 3803 100.00 . . . . 0.1440 . . . . . . . . . . . 0.1980 
'X-RAY DIFFRACTION' 3.5331 4.0442 . . 203 3830 100.00 . . . . 0.1303 . . . . . . . . . . . 0.1534 
'X-RAY DIFFRACTION' 4.0442 5.0949 . . 221 3850 100.00 . . . . 0.1404 . . . . . . . . . . . 0.1576 
'X-RAY DIFFRACTION' 5.0949 60.977 . . 233 3848 97.00  . . . . 0.1823 . . . . . . . . . . . 0.2043 
# 
_struct.entry_id                     9IHW 
_struct.title                        
'Crystal structure of GH57 family amylopullulanase mutant D352N from Aquifex aeolicusin 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        9IHW 
_struct_keywords.text            'GH57 family, amylopullulanase, Aquifex aeolicus, complex, mutant, HYDROLASE' 
_struct_keywords.pdbx_keywords   HYDROLASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 2 ? 
E N N 3 ? 
F N N 3 ? 
G N N 3 ? 
H N N 3 ? 
I N N 3 ? 
J N N 3 ? 
K N N 4 ? 
L N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    O66934_AQUAE 
_struct_ref.pdbx_db_accession          O66934 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MKKLFLVFWWHMHQPLYREPYTGEYLLPWTFFHAVKDYYDMPAYLKDFEIKLNFNLTPVLIDQIQEYAQGKAKDVFLEAI
RKDPDDLEKEEVEKLIEFTKLNYEKPIYRFERIRELMNKEKLNREELLDLQTLNLLAWCGRTLRKDLKDLLNKGRNYTQE
EKEYVLNKYFEIIKKTLSIYREIKEEGKGSVSTSPYYHPLIPILLNPNCVYETTPNVKIPDFAVSFREDASKHVELAKEK
YFEIFGEHPVYMWPPEASVSNEALELYYEKGINMLATDEVILKNSVERASPYLRYYFRELISVFFRDKTLSDLIGFSYHA
WNAEDAVRDFIGRLKKIHESVDFQPVVFVVLDGENCWEYYEENGIPFLEKLYSTLEKEEWIETLTLEEAMRKEDVKTEVI
ESVKAGTWFDGNFLKWIGNKEKNEYWKILIEAKKKAKNDYILVAEGSDWFWWQGEEKAPFVEVFDKLFRSFVRRAQE
;
_struct_ref.pdbx_align_begin           1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9IHW A 1 ? 477 ? O66934 1 ? 477 ? 1 477 
2 1 9IHW 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 9IHW ASN A 352 ? UNP O66934 ASP 352 'engineered mutation' 352 1 
2 9IHW ASN B 352 ? UNP O66934 ASP 352 'engineered mutation' 352 2 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,E,F,G,H,K 
2 1 B,D,I,J,L     
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 PRO A 28  ? ASP A 37  ? PRO A 28  ASP A 37  1 ? 10 
HELX_P HELX_P2  AA2 TYR A 39  ? TYR A 44  ? TYR A 39  TYR A 44  1 ? 6  
HELX_P HELX_P3  AA3 LEU A 45  ? ASP A 47  ? LEU A 45  ASP A 47  5 ? 3  
HELX_P HELX_P4  AA4 THR A 57  ? GLN A 69  ? THR A 57  GLN A 69  1 ? 13 
HELX_P HELX_P5  AA5 VAL A 75  ? LYS A 82  ? VAL A 75  LYS A 82  1 ? 8  
HELX_P HELX_P6  AA6 ASP A 83  ? LEU A 87  ? ASP A 83  LEU A 87  5 ? 5  
HELX_P HELX_P7  AA7 GLU A 88  ? TYR A 103 ? GLU A 88  TYR A 103 1 ? 16 
HELX_P HELX_P8  AA8 LYS A 105 ? ARG A 109 ? LYS A 105 ARG A 109 5 ? 5  
HELX_P HELX_P9  AA9 PHE A 110 ? ASN A 118 ? PHE A 110 ASN A 118 1 ? 9  
HELX_P HELX_P10 AB1 ASN A 123 ? TRP A 138 ? ASN A 123 TRP A 138 1 ? 16 
HELX_P HELX_P11 AB2 GLY A 140 ? LEU A 147 ? GLY A 140 LEU A 147 1 ? 8  
HELX_P HELX_P12 AB3 LEU A 147 ? GLY A 154 ? LEU A 147 GLY A 154 1 ? 8  
HELX_P HELX_P13 AB4 THR A 158 ? LYS A 175 ? THR A 158 LYS A 175 1 ? 18 
HELX_P HELX_P14 AB5 LYS A 175 ? GLU A 186 ? LYS A 175 GLU A 186 1 ? 12 
HELX_P HELX_P15 AB6 LEU A 200 ? ASN A 206 ? LEU A 200 ASN A 206 1 ? 7  
HELX_P HELX_P16 AB7 PRO A 207 ? THR A 213 ? PRO A 207 THR A 213 5 ? 7  
HELX_P HELX_P17 AB8 PHE A 226 ? GLY A 246 ? PHE A 226 GLY A 246 1 ? 21 
HELX_P HELX_P18 AB9 PRO A 254 ? SER A 258 ? PRO A 254 SER A 258 5 ? 5  
HELX_P HELX_P19 AC1 SER A 260 ? LYS A 270 ? SER A 260 LYS A 270 1 ? 11 
HELX_P HELX_P20 AC2 ASP A 278 ? VAL A 286 ? ASP A 278 VAL A 286 1 ? 9  
HELX_P HELX_P21 AC3 ASP A 307 ? SER A 317 ? ASP A 307 SER A 317 1 ? 11 
HELX_P HELX_P22 AC4 TYR A 318 ? TRP A 321 ? TYR A 318 TRP A 321 5 ? 4  
HELX_P HELX_P23 AC5 ASN A 322 ? VAL A 341 ? ASN A 322 VAL A 341 1 ? 20 
HELX_P HELX_P24 AC6 CYS A 356 ? ASN A 363 ? CYS A 356 ASN A 363 5 ? 8  
HELX_P HELX_P25 AC7 GLY A 364 ? GLU A 378 ? GLY A 364 GLU A 378 1 ? 15 
HELX_P HELX_P26 AC8 THR A 385 ? LYS A 392 ? THR A 385 LYS A 392 1 ? 8  
HELX_P HELX_P27 AC9 ASN A 419 ? LYS A 435 ? ASN A 419 LYS A 435 1 ? 17 
HELX_P HELX_P28 AD1 ASP A 439 ? GLU A 445 ? ASP A 439 GLU A 445 1 ? 7  
HELX_P HELX_P29 AD2 GLY A 446 ? GLN A 453 ? GLY A 446 GLN A 453 1 ? 8  
HELX_P HELX_P30 AD3 PHE A 460 ? GLN A 476 ? PHE A 460 GLN A 476 1 ? 17 
HELX_P HELX_P31 AD4 PRO B 28  ? ASP B 37  ? PRO B 28  ASP B 37  1 ? 10 
HELX_P HELX_P32 AD5 TYR B 39  ? TYR B 44  ? TYR B 39  TYR B 44  1 ? 6  
HELX_P HELX_P33 AD6 LEU B 45  ? ASP B 47  ? LEU B 45  ASP B 47  5 ? 3  
HELX_P HELX_P34 AD7 THR B 57  ? GLN B 69  ? THR B 57  GLN B 69  1 ? 13 
HELX_P HELX_P35 AD8 VAL B 75  ? LYS B 82  ? VAL B 75  LYS B 82  1 ? 8  
HELX_P HELX_P36 AD9 ASP B 83  ? LEU B 87  ? ASP B 83  LEU B 87  5 ? 5  
HELX_P HELX_P37 AE1 GLU B 88  ? TYR B 103 ? GLU B 88  TYR B 103 1 ? 16 
HELX_P HELX_P38 AE2 LYS B 105 ? ARG B 109 ? LYS B 105 ARG B 109 5 ? 5  
HELX_P HELX_P39 AE3 PHE B 110 ? ASN B 118 ? PHE B 110 ASN B 118 1 ? 9  
HELX_P HELX_P40 AE4 ASN B 123 ? TRP B 138 ? ASN B 123 TRP B 138 1 ? 16 
HELX_P HELX_P41 AE5 ARG B 141 ? LYS B 145 ? ARG B 141 LYS B 145 5 ? 5  
HELX_P HELX_P42 AE6 LEU B 147 ? GLY B 154 ? LEU B 147 GLY B 154 1 ? 8  
HELX_P HELX_P43 AE7 THR B 158 ? LYS B 175 ? THR B 158 LYS B 175 1 ? 18 
HELX_P HELX_P44 AE8 LYS B 175 ? GLU B 186 ? LYS B 175 GLU B 186 1 ? 12 
HELX_P HELX_P45 AE9 LEU B 200 ? ASN B 206 ? LEU B 200 ASN B 206 1 ? 7  
HELX_P HELX_P46 AF1 PRO B 207 ? THR B 213 ? PRO B 207 THR B 213 5 ? 7  
HELX_P HELX_P47 AF2 PHE B 226 ? GLY B 246 ? PHE B 226 GLY B 246 1 ? 21 
HELX_P HELX_P48 AF3 PRO B 254 ? SER B 258 ? PRO B 254 SER B 258 5 ? 5  
HELX_P HELX_P49 AF4 SER B 260 ? LYS B 270 ? SER B 260 LYS B 270 1 ? 11 
HELX_P HELX_P50 AF5 ASP B 278 ? VAL B 286 ? ASP B 278 VAL B 286 1 ? 9  
HELX_P HELX_P51 AF6 ASP B 307 ? SER B 317 ? ASP B 307 SER B 317 1 ? 11 
HELX_P HELX_P52 AF7 TYR B 318 ? TRP B 321 ? TYR B 318 TRP B 321 5 ? 4  
HELX_P HELX_P53 AF8 ASN B 322 ? VAL B 341 ? ASN B 322 VAL B 341 1 ? 20 
HELX_P HELX_P54 AF9 CYS B 356 ? ASN B 363 ? CYS B 356 ASN B 363 5 ? 8  
HELX_P HELX_P55 AG1 GLY B 364 ? GLU B 376 ? GLY B 364 GLU B 376 1 ? 13 
HELX_P HELX_P56 AG2 THR B 385 ? LYS B 392 ? THR B 385 LYS B 392 1 ? 8  
HELX_P HELX_P57 AG3 ASN B 419 ? LYS B 435 ? ASN B 419 LYS B 435 1 ? 17 
HELX_P HELX_P58 AG4 ASP B 439 ? GLU B 445 ? ASP B 439 GLU B 445 1 ? 7  
HELX_P HELX_P59 AG5 GLY B 446 ? GLN B 453 ? GLY B 446 GLN B 453 1 ? 8  
HELX_P HELX_P60 AG6 PHE B 460 ? 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 ? ? ? ? ? ? ? 1.304 ? ? 
covale2  covale both ? C GLC . O4 ? ? ? 1_555 C GLC . C1 ? ? C GLC 2 C GLC 3 1_555 ? ? ? ? ? ? ? 1.366 ? ? 
covale3  covale both ? C GLC . O4 ? ? ? 1_555 C GLC . C1 ? ? C GLC 3 C GLC 4 1_555 ? ? ? ? ? ? ? 1.387 ? ? 
covale4  covale both ? C GLC . O4 ? ? ? 1_555 C GLC . C1 ? ? C GLC 4 C GLC 5 1_555 ? ? ? ? ? ? ? 1.398 ? ? 
covale5  covale both ? C GLC . O4 ? ? ? 1_555 C GLC . C1 ? ? C GLC 5 C GLC 6 1_555 ? ? ? ? ? ? ? 1.393 ? ? 
covale6  covale both ? D GLC . O4 ? ? ? 1_555 D GLC . C1 ? ? D GLC 1 D GLC 2 1_555 ? ? ? ? ? ? ? 1.394 ? ? 
covale7  covale both ? D GLC . O4 ? ? ? 1_555 D GLC . C1 ? ? D GLC 2 D GLC 3 1_555 ? ? ? ? ? ? ? 1.439 ? ? 
covale8  covale both ? D GLC . O4 ? ? ? 1_555 D GLC . C1 ? ? D GLC 3 D GLC 4 1_555 ? ? ? ? ? ? ? 1.444 ? ? 
covale9  covale both ? D GLC . O4 ? ? ? 1_555 D GLC . C1 ? ? D GLC 4 D GLC 5 1_555 ? ? ? ? ? ? ? 1.438 ? ? 
covale10 covale both ? D GLC . O4 ? ? ? 1_555 D GLC . C1 ? ? D GLC 5 D GLC 6 1_555 ? ? ? ? ? ? ? 1.433 ? ? 
# 
_struct_conn_type.id          covale 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 GLU 455 A . ? GLU 455 A GLU 456 A ? GLU 456 A 1 -5.15 
2 GLU 456 A . ? GLU 456 A LYS 457 A ? LYS 457 A 1 -0.93 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 4 ? 
AA3 ? 2 ? 
AA4 ? 5 ? 
AA5 ? 4 ? 
AA6 ? 4 ? 
AA7 ? 2 ? 
AA8 ? 5 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? parallel      
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA2 1 2 ? parallel      
AA2 2 3 ? parallel      
AA2 3 4 ? parallel      
AA3 1 2 ? parallel      
AA4 1 2 ? parallel      
AA4 2 3 ? parallel      
AA4 3 4 ? anti-parallel 
AA4 4 5 ? parallel      
AA5 1 2 ? parallel      
AA5 2 3 ? parallel      
AA5 3 4 ? parallel      
AA6 1 2 ? parallel      
AA6 2 3 ? parallel      
AA6 3 4 ? parallel      
AA7 1 2 ? parallel      
AA8 1 2 ? parallel      
AA8 2 3 ? parallel      
AA8 3 4 ? anti-parallel 
AA8 4 5 ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 VAL A 191 ? SER A 192 ? VAL A 191 SER A 192 
AA1 2 ASN A 53  ? LEU A 56  ? ASN A 53  LEU A 56  
AA1 3 LEU A 4   ? MET A 12  ? LEU A 4   MET A 12  
AA1 4 VAL A 346 ? ASN A 352 ? VAL A 346 ASN A 352 
AA2 1 VAL A 191 ? SER A 192 ? VAL A 191 SER A 192 
AA2 2 ASN A 53  ? LEU A 56  ? ASN A 53  LEU A 56  
AA2 3 LEU A 4   ? MET A 12  ? LEU A 4   MET A 12  
AA2 4 ILE A 381 ? THR A 383 ? ILE A 381 THR A 383 
AA3 1 GLU A 24  ? TYR A 25  ? GLU A 24  TYR A 25  
AA3 2 LYS A 73  ? ASP A 74  ? LYS A 73  ASP A 74  
AA4 1 TYR A 251 ? MET A 252 ? TYR A 251 MET A 252 
AA4 2 MET A 274 ? THR A 277 ? MET A 274 THR A 277 
AA4 3 ILE A 301 ? PHE A 305 ? ILE A 301 PHE A 305 
AA4 4 ARG A 294 ? PHE A 297 ? ARG A 294 PHE A 297 
AA4 5 THR A 397 ? ILE A 400 ? THR A 397 ILE A 400 
AA5 1 VAL B 191 ? SER B 192 ? VAL B 191 SER B 192 
AA5 2 ASN B 53  ? LEU B 56  ? ASN B 53  LEU B 56  
AA5 3 LEU B 4   ? MET B 12  ? LEU B 4   MET B 12  
AA5 4 VAL B 346 ? ASN B 352 ? VAL B 346 ASN B 352 
AA6 1 VAL B 191 ? SER B 192 ? VAL B 191 SER B 192 
AA6 2 ASN B 53  ? LEU B 56  ? ASN B 53  LEU B 56  
AA6 3 LEU B 4   ? MET B 12  ? LEU B 4   MET B 12  
AA6 4 ILE B 381 ? THR B 383 ? ILE B 381 THR B 383 
AA7 1 GLU B 24  ? TYR B 25  ? GLU B 24  TYR B 25  
AA7 2 LYS B 73  ? ASP B 74  ? LYS B 73  ASP B 74  
AA8 1 TYR B 251 ? MET B 252 ? TYR B 251 MET B 252 
AA8 2 MET B 274 ? THR B 277 ? MET B 274 THR B 277 
AA8 3 ILE B 301 ? PHE B 305 ? ILE B 301 PHE B 305 
AA8 4 ARG B 294 ? PHE B 297 ? ARG B 294 PHE B 297 
AA8 5 THR B 397 ? ILE B 400 ? THR B 397 ILE B 400 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O SER A 192 ? O SER A 192 N PHE A 54  ? N PHE A 54  
AA1 2 3 O ASN A 55  ? O ASN A 55  N TRP A 10  ? N TRP A 10  
AA1 3 4 N PHE A 5   ? N PHE A 5   O VAL A 347 ? O VAL A 347 
AA2 1 2 O SER A 192 ? O SER A 192 N PHE A 54  ? N PHE A 54  
AA2 2 3 O ASN A 55  ? O ASN A 55  N TRP A 10  ? N TRP A 10  
AA2 3 4 N LEU A 4   ? N LEU A 4   O GLU A 382 ? O GLU A 382 
AA3 1 2 N TYR A 25  ? N TYR A 25  O LYS A 73  ? O LYS A 73  
AA4 1 2 N MET A 252 ? N MET A 252 O MET A 274 ? O MET A 274 
AA4 2 3 N THR A 277 ? N THR A 277 O PHE A 304 ? O PHE A 304 
AA4 3 4 O ILE A 301 ? O ILE A 301 N PHE A 297 ? N PHE A 297 
AA4 4 5 N TYR A 296 ? N TYR A 296 O ILE A 400 ? O ILE A 400 
AA5 1 2 O SER B 192 ? O SER B 192 N PHE B 54  ? N PHE B 54  
AA5 2 3 O ASN B 53  ? O ASN B 53  N TRP B 10  ? N TRP B 10  
AA5 3 4 N 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 PHE B 304 ? O PHE B 304 
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 GLU B 398 ? O GLU B 398 
# 
_pdbx_entry_details.entry_id                   9IHW 
_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 751 ? ? O  B HOH 843 ? ? 1.82 
2  1 O   A HOH 652 ? ? O  A HOH 698 ? ? 1.82 
3  1 O   A PRO 459 ? ? O  A HOH 601 ? ? 1.83 
4  1 O   B HOH 831 ? ? O  B HOH 844 ? ? 1.87 
5  1 O   B HOH 794 ? ? O  B HOH 808 ? ? 1.90 
6  1 O   B HOH 825 ? ? O  B HOH 847 ? ? 1.91 
7  1 O   A HOH 682 ? ? O  A HOH 889 ? ? 1.91 
8  1 O   B HOH 849 ? ? O  B HOH 868 ? ? 1.91 
9  1 O   B HOH 608 ? ? O  B HOH 803 ? ? 1.94 
10 1 O   A HOH 883 ? ? O  A HOH 931 ? ? 1.94 
11 1 O   A HOH 767 ? ? O  A HOH 894 ? ? 1.94 
12 1 OE2 A GLU 104 ? ? O  A HOH 602 ? ? 1.94 
13 1 O   B HOH 820 ? ? O  B HOH 850 ? ? 1.96 
14 1 O   A HOH 840 ? ? O  A HOH 893 ? ? 1.97 
15 1 NZ  A LYS 73  ? ? O  A HOH 603 ? ? 2.03 
16 1 OE1 B GLU 287 ? ? O  B HOH 601 ? ? 2.03 
17 1 O   B HOH 840 ? ? O  B HOH 841 ? ? 2.04 
18 1 OE1 A GLU 379 ? ? O  A HOH 604 ? ? 2.05 
19 1 O   A HOH 845 ? ? O  A HOH 902 ? ? 2.07 
20 1 O   B HOH 763 ? ? O  B HOH 856 ? ? 2.07 
21 1 OE2 B GLU 185 ? ? O  A HOH 604 ? ? 2.07 
22 1 O   A HOH 835 ? ? O  B HOH 679 ? ? 2.09 
23 1 O   A HOH 816 ? ? O  A HOH 905 ? ? 2.09 
24 1 O   B HOH 823 ? ? O  B HOH 870 ? ? 2.11 
25 1 O   A HOH 905 ? ? O  A HOH 940 ? ? 2.11 
26 1 OE2 B GLU 382 ? ? O  B HOH 602 ? ? 2.11 
27 1 OD1 A ASN 152 ? ? O  A HOH 605 ? ? 2.12 
28 1 OD1 A ASN 118 ? ? O  A HOH 606 ? ? 2.12 
29 1 O   A HOH 789 ? ? O  A HOH 889 ? ? 2.12 
30 1 O   B HOH 631 ? ? O  B HOH 857 ? ? 2.12 
31 1 O   B HOH 716 ? ? O  B HOH 830 ? ? 2.14 
32 1 ND2 B ASN 352 ? ? O6 D GLC 2   ? ? 2.14 
33 1 O   A HOH 937 ? ? O  A HOH 943 ? ? 2.15 
34 1 O   B PRO 459 ? ? O  B HOH 603 ? ? 2.16 
35 1 O4  C GLC 1   ? ? C2 C GLC 2   ? ? 2.16 
36 1 O   A HOH 622 ? ? O  A HOH 919 ? ? 2.17 
37 1 O6  C GLC 6   ? ? O  A HOH 618 ? ? 2.17 
38 1 NH2 A ARG 109 ? ? O  A HOH 607 ? ? 2.17 
39 1 O   A HOH 614 ? ? O  A HOH 755 ? ? 2.18 
40 1 O   A HOH 819 ? ? O  A HOH 869 ? ? 2.18 
41 1 O   A HOH 900 ? ? O  A HOH 912 ? ? 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 892 ? ? 1_555 O B HOH 766 ? ? 1_645 2.14 
2 1 O A HOH 855 ? ? 1_555 O B HOH 614 ? ? 1_655 2.16 
# 
loop_
_pdbx_validate_rmsd_bond.id 
_pdbx_validate_rmsd_bond.PDB_model_num 
_pdbx_validate_rmsd_bond.auth_atom_id_1 
_pdbx_validate_rmsd_bond.auth_asym_id_1 
_pdbx_validate_rmsd_bond.auth_comp_id_1 
_pdbx_validate_rmsd_bond.auth_seq_id_1 
_pdbx_validate_rmsd_bond.PDB_ins_code_1 
_pdbx_validate_rmsd_bond.label_alt_id_1 
_pdbx_validate_rmsd_bond.auth_atom_id_2 
_pdbx_validate_rmsd_bond.auth_asym_id_2 
_pdbx_validate_rmsd_bond.auth_comp_id_2 
_pdbx_validate_rmsd_bond.auth_seq_id_2 
_pdbx_validate_rmsd_bond.PDB_ins_code_2 
_pdbx_validate_rmsd_bond.label_alt_id_2 
_pdbx_validate_rmsd_bond.bond_value 
_pdbx_validate_rmsd_bond.bond_target_value 
_pdbx_validate_rmsd_bond.bond_deviation 
_pdbx_validate_rmsd_bond.bond_standard_deviation 
_pdbx_validate_rmsd_bond.linker_flag 
1 1 CB A PHE 76  ? B CG  A PHE 76  ? B 1.382 1.509 -0.127 0.017 N 
2 1 CD A GLU 247 ? ? OE2 A GLU 247 ? ? 1.164 1.252 -0.088 0.011 N 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 OE1 A GLU 247 ? ? CD A GLU 247 ? ? OE2 A GLU 247 ? ? 113.89 123.30 -9.41  1.20 N 
2 1 N   A LYS 457 ? ? CA A LYS 457 ? ? C   A LYS 457 ? ? 94.01  111.00 -16.99 2.70 N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 ASN A 206 ? ? -161.96 93.85   
2  1 ALA A 257 ? ? 57.97   18.45   
3  1 ASP A 394 ? ? -90.47  49.69   
4  1 GLU A 456 ? ? -91.06  -80.23  
5  1 LYS A 457 ? ? 161.35  100.72  
6  1 ALA A 458 ? ? 153.11  165.36  
7  1 PHE A 460 ? ? 87.13   -9.27   
8  1 ASN B 206 ? ? -163.98 92.83   
9  1 THR B 277 ? ? -147.52 -158.94 
10 1 GLU B 455 ? ? -110.04 -127.73 
11 1 LYS B 457 ? ? 27.64   18.15   
12 1 ALA B 458 ? ? -45.09  155.41  
13 1 PHE B 460 ? ? 73.20   -12.64  
# 
loop_
_pdbx_validate_peptide_omega.id 
_pdbx_validate_peptide_omega.PDB_model_num 
_pdbx_validate_peptide_omega.auth_comp_id_1 
_pdbx_validate_peptide_omega.auth_asym_id_1 
_pdbx_validate_peptide_omega.auth_seq_id_1 
_pdbx_validate_peptide_omega.PDB_ins_code_1 
_pdbx_validate_peptide_omega.label_alt_id_1 
_pdbx_validate_peptide_omega.auth_comp_id_2 
_pdbx_validate_peptide_omega.auth_asym_id_2 
_pdbx_validate_peptide_omega.auth_seq_id_2 
_pdbx_validate_peptide_omega.PDB_ins_code_2 
_pdbx_validate_peptide_omega.label_alt_id_2 
_pdbx_validate_peptide_omega.omega 
1 1 PRO A 195 ? ? TYR A 196 ? ? -148.15 
2 1 PRO B 195 ? ? TYR B 196 ? ? -149.21 
# 
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 -13.5847 16.7035 76.1473 0.0807 ? -0.0164 ? 0.0066  ? 0.0907 ? 0.0065  ? 0.1203 ? 0.8656 ? 
-0.0832 ? -0.3621 ? 0.3033 ? 0.1247  ? 1.0912 ? -0.0304 ? -0.0760 ? -0.0510 ? 0.0081  ? 0.0311  ? 0.0248  ? 0.0567  ? -0.0316 ? 
0.0074  ? 
2  'X-RAY DIFFRACTION' ? refined -25.8762 22.6867 76.7464 0.0711 ? -0.0052 ? -0.0060 ? 0.1222 ? 0.0138  ? 0.1427 ? 1.9446 ? 
-0.5027 ? -1.3427 ? 0.8840 ? 0.4019  ? 1.9593 ? 0.0540  ? 0.0264  ? 0.1521  ? 0.0173  ? -0.0057 ? 0.1043  ? -0.1230 ? -0.1918 ? 
0.0098  ? 
3  'X-RAY DIFFRACTION' ? refined 8.0987   11.6954 72.8503 0.0870 ? 0.0109  ? 0.0244  ? 0.0654 ? -0.0027 ? 0.1262 ? 2.9673 ? 1.2022 
? 1.2631  ? 0.8450 ? 0.8550  ? 1.6069 ? -0.0061 ? -0.0325 ? -0.0521 ? -0.0096 ? -0.0038 ? -0.0506 ? 0.0739  ? 0.1043  ? -0.0093 ? 
4  'X-RAY DIFFRACTION' ? refined 6.1348   17.9250 59.5497 0.1021 ? -0.0265 ? 0.0178  ? 0.1006 ? -0.0203 ? 0.1164 ? 1.3161 ? 
-0.4094 ? -0.0993 ? 0.3571 ? -0.0951 ? 0.7308 ? -0.0013 ? 0.1157  ? -0.0221 ? -0.0628 ? -0.0153 ? -0.0655 ? 0.0445  ? 0.1146  ? 
0.0164  ? 
5  'X-RAY DIFFRACTION' ? refined -7.9969  23.4941 52.6235 0.1048 ? -0.0307 ? -0.0083 ? 0.1014 ? 0.0053  ? 0.0970 ? 1.9736 ? 
-0.1669 ? -0.9591 ? 1.1761 ? 0.2627  ? 2.6325 ? 0.0362  ? 0.2842  ? 0.0187  ? -0.1822 ? 0.0233  ? 0.0261  ? -0.0919 ? -0.0362 ? 
-0.0553 ? 
6  'X-RAY DIFFRACTION' ? refined 11.9324  21.0524 75.8344 0.0470 ? -0.0204 ? 0.0099  ? 0.1189 ? -0.0153 ? 0.1637 ? 0.8387 ? 
-0.0146 ? 0.2057  ? 0.6840 ? 0.0727  ? 4.0067 ? -0.0362 ? -0.0973 ? 0.1012  ? 0.0113  ? 0.0163  ? -0.0248 ? -0.2526 ? 0.1353  ? 
0.0187  ? 
7  'X-RAY DIFFRACTION' ? refined 1.7025   16.9758 86.4325 0.0359 ? -0.0178 ? 0.0005  ? 0.1441 ? -0.0134 ? 0.0858 ? 5.4367 ? 
-0.9285 ? -0.0608 ? 3.6718 ? 0.0251  ? 4.8839 ? -0.0577 ? -0.3721 ? 0.0489  ? 0.0833  ? 0.0156  ? 0.0921  ? -0.1199 ? -0.0955 ? 
0.0132  ? 
8  'X-RAY DIFFRACTION' ? refined -24.0718 36.5431 19.7359 0.1533 ? 0.0366  ? -0.0133 ? 0.1512 ? -0.0206 ? 0.1145 ? 1.0552 ? 0.2254 
? -0.5964 ? 0.4908 ? -0.1833 ? 1.5798 ? -0.0409 ? 0.1791  ? -0.0549 ? -0.0984 ? 0.0121  ? -0.0095 ? 0.1707  ? 0.1596  ? 0.0127  ? 
9  'X-RAY DIFFRACTION' ? refined -13.8124 54.2646 12.3946 0.2552 ? -0.0230 ? 0.0257  ? 0.2795 ? 0.0549  ? 0.2589 ? 3.5319 ? 0.6152 
? -2.3438 ? 1.9575 ? -1.0796 ? 4.8710 ? 0.3646  ? 0.2273  ? 0.6392  ? 0.0605  ? -0.1935 ? -0.0659 ? -0.6220 ? 0.2939  ? -0.2526 ? 
10 'X-RAY DIFFRACTION' ? refined -11.1507 37.8814 18.7452 0.1592 ? 0.0685  ? -0.0140 ? 0.2839 ? -0.0280 ? 0.1510 ? 1.8448 ? 0.5651 
? -1.3204 ? 1.0982 ? -0.9125 ? 3.1985 ? -0.0200 ? 0.0252  ? -0.0284 ? -0.0666 ? -0.0231 ? -0.0807 ? 0.2245  ? 0.5691  ? 0.1497  ? 
11 'X-RAY DIFFRACTION' ? refined -44.9712 31.5936 26.6390 0.2035 ? -0.0281 ? -0.0229 ? 0.1421 ? -0.0048 ? 0.1635 ? 2.4615 ? 
-0.4770 ? 0.1233  ? 1.3628 ? -0.3743 ? 2.1211 ? 0.0512  ? 0.1247  ? -0.1914 ? -0.1323 ? 0.0627  ? 0.2330  ? 0.2945  ? -0.3164 ? 
-0.0804 ? 
12 'X-RAY DIFFRACTION' ? refined -42.7351 30.2734 35.7476 0.1601 ? -0.0188 ? -0.0106 ? 0.1003 ? 0.0046  ? 0.1310 ? 2.7120 ? 
-0.2808 ? -0.5102 ? 2.5861 ? 0.0306  ? 2.6828 ? -0.0184 ? -0.1112 ? -0.2507 ? 0.1095  ? 0.0558  ? 0.0542  ? 0.4020  ? -0.1105 ? 
-0.0557 ? 
13 'X-RAY DIFFRACTION' ? refined -39.5078 44.1375 41.6890 0.1554 ? 0.0364  ? 0.0048  ? 0.1140 ? -0.0204 ? 0.1577 ? 2.0412 ? 0.8527 
? -0.6792 ? 1.1386 ? -0.5290 ? 2.1241 ? 0.0948  ? -0.1411 ? 0.2064  ? 0.0343  ? -0.0452 ? 0.1668  ? -0.1960 ? -0.1315 ? -0.0975 ? 
14 'X-RAY DIFFRACTION' ? refined -27.9846 47.8610 42.4534 0.1780 ? -0.0059 ? -0.0020 ? 0.0976 ? -0.0325 ? 0.1255 ? 1.7357 ? 0.1974 
? -0.7029 ? 0.9444 ? -0.4209 ? 2.7283 ? 0.0741  ? -0.2147 ? 0.1691  ? 0.1644  ? -0.0813 ? 0.0391  ? -0.3570 ? 0.1669  ? -0.0401 ? 
15 'X-RAY DIFFRACTION' ? refined -23.9708 40.0003 44.9779 0.1612 ? 0.0070  ? -0.0244 ? 0.1369 ? -0.0230 ? 0.1346 ? 2.1531 ? 0.1902 
? -0.6376 ? 0.7443 ? -0.2875 ? 3.1343 ? 0.1084  ? -0.2350 ? -0.0122 ? 0.1869  ? -0.0716 ? -0.0258 ? -0.1138 ? 0.3078  ? 0.0168  ? 
16 'X-RAY DIFFRACTION' ? refined -49.2788 40.9991 24.0299 0.0980 ? 0.0062  ? -0.0171 ? 0.1947 ? 0.0365  ? 0.1971 ? 1.2927 ? 0.0550 
? 0.5651  ? 1.0210 ? -0.5277 ? 6.3291 ? -0.0128 ? 0.3008  ? 0.1466  ? -0.1118 ? 0.1085  ? 0.1440  ? -0.0770 ? -0.4444 ? -0.0261 ? 
17 'X-RAY DIFFRACTION' ? refined -40.8080 36.5146 11.9712 0.1626 ? 0.0083  ? -0.0398 ? 0.2444 ? 0.0060  ? 0.0932 ? 6.0406 ? 0.9329 
? 0.6285  ? 4.0208 ? 0.1193  ? 5.3661 ? -0.0664 ? 0.6052  ? 0.0728  ? -0.3352 ? 0.1127  ? 0.0131  ? 0.1510  ? -0.0422 ? -0.0227 ? 
# 
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 102 )
;
2  'X-RAY DIFFRACTION' 2  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 103 through 185 )
;
3  'X-RAY DIFFRACTION' 3  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 186 through 245 )
;
4  'X-RAY DIFFRACTION' 4  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 246 through 322 )
;
5  'X-RAY DIFFRACTION' 5  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 323 through 396 )
;
6  'X-RAY DIFFRACTION' 6  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 397 through 435 )
;
7  'X-RAY DIFFRACTION' 7  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 436 through 477 )
;
8  'X-RAY DIFFRACTION' 8  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 2 through 102 )
;
9  'X-RAY DIFFRACTION' 9  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 103 through 123 )
;
10 'X-RAY DIFFRACTION' 10 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 124 through 185 )
;
11 'X-RAY DIFFRACTION' 11 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 186 through 245 )
;
12 'X-RAY DIFFRACTION' 12 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 246 through 278 )
;
13 'X-RAY DIFFRACTION' 13 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 279 through 322 )
;
14 'X-RAY DIFFRACTION' 14 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 323 through 360 )
;
15 'X-RAY DIFFRACTION' 15 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 361 through 396 )
;
16 'X-RAY DIFFRACTION' 16 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 397 through 435 )
;
17 'X-RAY DIFFRACTION' 17 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 436 through 477 )
;
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A MET 1 ? A MET 1 
2 1 Y 1 B MET 1 ? B MET 1 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
CYS N    N N N 74  
CYS CA   C N R 75  
CYS C    C N N 76  
CYS O    O N N 77  
CYS CB   C N N 78  
CYS SG   S N N 79  
CYS OXT  O N N 80  
CYS H    H N N 81  
CYS H2   H N N 82  
CYS HA   H N N 83  
CYS HB2  H N N 84  
CYS HB3  H N N 85  
CYS HG   H N N 86  
CYS HXT  H N N 87  
GLC C1   C N S 88  
GLC C2   C N R 89  
GLC C3   C N S 90  
GLC C4   C N S 91  
GLC C5   C N R 92  
GLC C6   C N N 93  
GLC O1   O N N 94  
GLC O2   O N N 95  
GLC O3   O N N 96  
GLC O4   O N N 97  
GLC O5   O N N 98  
GLC O6   O N N 99  
GLC H1   H N N 100 
GLC H2   H N N 101 
GLC H3   H N N 102 
GLC H4   H N N 103 
GLC H5   H N N 104 
GLC H61  H N N 105 
GLC H62  H N N 106 
GLC HO1  H N N 107 
GLC HO2  H N N 108 
GLC HO3  H N N 109 
GLC HO4  H N N 110 
GLC HO6  H N N 111 
GLN N    N N N 112 
GLN CA   C N S 113 
GLN C    C N N 114 
GLN O    O N N 115 
GLN CB   C N N 116 
GLN CG   C N N 117 
GLN CD   C N N 118 
GLN OE1  O N N 119 
GLN NE2  N N N 120 
GLN OXT  O N N 121 
GLN H    H N N 122 
GLN H2   H N N 123 
GLN HA   H N N 124 
GLN HB2  H N N 125 
GLN HB3  H N N 126 
GLN HG2  H N N 127 
GLN HG3  H N N 128 
GLN HE21 H N N 129 
GLN HE22 H N N 130 
GLN HXT  H N N 131 
GLU N    N N N 132 
GLU CA   C N S 133 
GLU C    C N N 134 
GLU O    O N N 135 
GLU CB   C N N 136 
GLU CG   C N N 137 
GLU CD   C N N 138 
GLU OE1  O N N 139 
GLU OE2  O N N 140 
GLU OXT  O N N 141 
GLU H    H N N 142 
GLU H2   H N N 143 
GLU HA   H N N 144 
GLU HB2  H N N 145 
GLU HB3  H N N 146 
GLU HG2  H N N 147 
GLU HG3  H N N 148 
GLU HE2  H N N 149 
GLU HXT  H N N 150 
GLY N    N N N 151 
GLY CA   C N N 152 
GLY C    C N N 153 
GLY O    O N N 154 
GLY OXT  O N N 155 
GLY H    H N N 156 
GLY H2   H N N 157 
GLY HA2  H N N 158 
GLY HA3  H N N 159 
GLY HXT  H N N 160 
GOL C1   C N N 161 
GOL O1   O N N 162 
GOL C2   C N N 163 
GOL O2   O N N 164 
GOL C3   C N N 165 
GOL O3   O N N 166 
GOL H11  H N N 167 
GOL H12  H N N 168 
GOL HO1  H N N 169 
GOL H2   H N N 170 
GOL HO2  H N N 171 
GOL H31  H N N 172 
GOL H32  H N N 173 
GOL HO3  H N N 174 
HIS N    N N N 175 
HIS CA   C N S 176 
HIS C    C N N 177 
HIS O    O N N 178 
HIS CB   C N N 179 
HIS CG   C Y N 180 
HIS ND1  N Y N 181 
HIS CD2  C Y N 182 
HIS CE1  C Y N 183 
HIS NE2  N Y N 184 
HIS OXT  O N N 185 
HIS H    H N N 186 
HIS H2   H N N 187 
HIS HA   H N N 188 
HIS HB2  H N N 189 
HIS HB3  H N N 190 
HIS HD1  H N N 191 
HIS HD2  H N N 192 
HIS HE1  H N N 193 
HIS HE2  H N N 194 
HIS HXT  H N N 195 
HOH O    O N N 196 
HOH H1   H N N 197 
HOH H2   H N N 198 
ILE N    N N N 199 
ILE CA   C N S 200 
ILE C    C N N 201 
ILE O    O N N 202 
ILE CB   C N S 203 
ILE CG1  C N N 204 
ILE CG2  C N N 205 
ILE CD1  C N N 206 
ILE OXT  O N N 207 
ILE H    H N N 208 
ILE H2   H N N 209 
ILE HA   H N N 210 
ILE HB   H N N 211 
ILE HG12 H N N 212 
ILE HG13 H N N 213 
ILE HG21 H N N 214 
ILE HG22 H N N 215 
ILE HG23 H N N 216 
ILE HD11 H N N 217 
ILE HD12 H N N 218 
ILE HD13 H N N 219 
ILE HXT  H N N 220 
LEU N    N N N 221 
LEU CA   C N S 222 
LEU C    C N N 223 
LEU O    O N N 224 
LEU CB   C N N 225 
LEU CG   C N N 226 
LEU CD1  C N N 227 
LEU CD2  C N N 228 
LEU OXT  O N N 229 
LEU H    H N N 230 
LEU H2   H N N 231 
LEU HA   H N N 232 
LEU HB2  H N N 233 
LEU HB3  H N N 234 
LEU HG   H N N 235 
LEU HD11 H N N 236 
LEU HD12 H N N 237 
LEU HD13 H N N 238 
LEU HD21 H N N 239 
LEU HD22 H N N 240 
LEU HD23 H N N 241 
LEU HXT  H N N 242 
LYS N    N N N 243 
LYS CA   C N S 244 
LYS C    C N N 245 
LYS O    O N N 246 
LYS CB   C N N 247 
LYS CG   C N N 248 
LYS CD   C N N 249 
LYS CE   C N N 250 
LYS NZ   N N N 251 
LYS OXT  O N N 252 
LYS H    H N N 253 
LYS H2   H N N 254 
LYS HA   H N N 255 
LYS HB2  H N N 256 
LYS HB3  H N N 257 
LYS HG2  H N N 258 
LYS HG3  H N N 259 
LYS HD2  H N N 260 
LYS HD3  H N N 261 
LYS HE2  H N N 262 
LYS HE3  H N N 263 
LYS HZ1  H N N 264 
LYS HZ2  H N N 265 
LYS HZ3  H N N 266 
LYS HXT  H N N 267 
MET N    N N N 268 
MET CA   C N S 269 
MET C    C N N 270 
MET O    O N N 271 
MET CB   C N N 272 
MET CG   C N N 273 
MET SD   S N N 274 
MET CE   C N N 275 
MET OXT  O N N 276 
MET H    H N N 277 
MET H2   H N N 278 
MET HA   H N N 279 
MET HB2  H N N 280 
MET HB3  H N N 281 
MET HG2  H N N 282 
MET HG3  H N N 283 
MET HE1  H N N 284 
MET HE2  H N N 285 
MET HE3  H N N 286 
MET HXT  H N N 287 
PHE N    N N N 288 
PHE CA   C N S 289 
PHE C    C N N 290 
PHE O    O N N 291 
PHE CB   C N N 292 
PHE CG   C Y N 293 
PHE CD1  C Y N 294 
PHE CD2  C Y N 295 
PHE CE1  C Y N 296 
PHE CE2  C Y N 297 
PHE CZ   C Y N 298 
PHE OXT  O N N 299 
PHE H    H N N 300 
PHE H2   H N N 301 
PHE HA   H N N 302 
PHE HB2  H N N 303 
PHE HB3  H N N 304 
PHE HD1  H N N 305 
PHE HD2  H N N 306 
PHE HE1  H N N 307 
PHE HE2  H N N 308 
PHE HZ   H N N 309 
PHE HXT  H N N 310 
PRO N    N N N 311 
PRO CA   C N S 312 
PRO C    C N N 313 
PRO O    O N N 314 
PRO CB   C N N 315 
PRO CG   C N N 316 
PRO CD   C N N 317 
PRO OXT  O N N 318 
PRO H    H N N 319 
PRO HA   H N N 320 
PRO HB2  H N N 321 
PRO HB3  H N N 322 
PRO HG2  H N N 323 
PRO HG3  H N N 324 
PRO HD2  H N N 325 
PRO HD3  H N N 326 
PRO HXT  H N N 327 
SER N    N N N 328 
SER CA   C N S 329 
SER C    C N N 330 
SER O    O N N 331 
SER CB   C N N 332 
SER OG   O N N 333 
SER OXT  O N N 334 
SER H    H N N 335 
SER H2   H N N 336 
SER HA   H N N 337 
SER HB2  H N N 338 
SER HB3  H N N 339 
SER HG   H N N 340 
SER HXT  H N N 341 
THR N    N N N 342 
THR CA   C N S 343 
THR C    C N N 344 
THR O    O N N 345 
THR CB   C N R 346 
THR OG1  O N N 347 
THR CG2  C N N 348 
THR OXT  O N N 349 
THR H    H N N 350 
THR H2   H N N 351 
THR HA   H N N 352 
THR HB   H N N 353 
THR HG1  H N N 354 
THR HG21 H N N 355 
THR HG22 H N N 356 
THR HG23 H N N 357 
THR HXT  H N N 358 
TRP N    N N N 359 
TRP CA   C N S 360 
TRP C    C N N 361 
TRP O    O N N 362 
TRP CB   C N N 363 
TRP CG   C Y N 364 
TRP CD1  C Y N 365 
TRP CD2  C Y N 366 
TRP NE1  N Y N 367 
TRP CE2  C Y N 368 
TRP CE3  C Y N 369 
TRP CZ2  C Y N 370 
TRP CZ3  C Y N 371 
TRP CH2  C Y N 372 
TRP OXT  O N N 373 
TRP H    H N N 374 
TRP H2   H N N 375 
TRP HA   H N N 376 
TRP HB2  H N N 377 
TRP HB3  H N N 378 
TRP HD1  H N N 379 
TRP HE1  H N N 380 
TRP HE3  H N N 381 
TRP HZ2  H N N 382 
TRP HZ3  H N N 383 
TRP HH2  H N N 384 
TRP HXT  H N N 385 
TYR N    N N N 386 
TYR CA   C N S 387 
TYR C    C N N 388 
TYR O    O N N 389 
TYR CB   C N N 390 
TYR CG   C Y N 391 
TYR CD1  C Y N 392 
TYR CD2  C Y N 393 
TYR CE1  C Y N 394 
TYR CE2  C Y N 395 
TYR CZ   C Y N 396 
TYR OH   O N N 397 
TYR OXT  O N N 398 
TYR H    H N N 399 
TYR H2   H N N 400 
TYR HA   H N N 401 
TYR HB2  H N N 402 
TYR HB3  H N N 403 
TYR HD1  H N N 404 
TYR HD2  H N N 405 
TYR HE1  H N N 406 
TYR HE2  H N N 407 
TYR HH   H N N 408 
TYR HXT  H N N 409 
VAL N    N N N 410 
VAL CA   C N S 411 
VAL C    C N N 412 
VAL O    O N N 413 
VAL CB   C N N 414 
VAL CG1  C N N 415 
VAL CG2  C N N 416 
VAL OXT  O N N 417 
VAL H    H N N 418 
VAL H2   H N N 419 
VAL HA   H N N 420 
VAL HB   H N N 421 
VAL HG11 H N N 422 
VAL HG12 H N N 423 
VAL HG13 H N N 424 
VAL HG21 H N N 425 
VAL HG22 H N N 426 
VAL HG23 H N N 427 
VAL HXT  H N N 428 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLC C1  C2   sing N N 83  
GLC C1  O1   sing N N 84  
GLC C1  O5   sing N N 85  
GLC C1  H1   sing N N 86  
GLC C2  C3   sing N N 87  
GLC C2  O2   sing N N 88  
GLC C2  H2   sing N N 89  
GLC C3  C4   sing N N 90  
GLC C3  O3   sing N N 91  
GLC C3  H3   sing N N 92  
GLC C4  C5   sing N N 93  
GLC C4  O4   sing N N 94  
GLC C4  H4   sing N N 95  
GLC C5  C6   sing N N 96  
GLC C5  O5   sing N N 97  
GLC C5  H5   sing N N 98  
GLC C6  O6   sing N N 99  
GLC C6  H61  sing N N 100 
GLC C6  H62  sing N N 101 
GLC O1  HO1  sing N N 102 
GLC O2  HO2  sing N N 103 
GLC O3  HO3  sing N N 104 
GLC O4  HO4  sing N N 105 
GLC O6  HO6  sing N N 106 
GLN N   CA   sing N N 107 
GLN N   H    sing N N 108 
GLN N   H2   sing N N 109 
GLN CA  C    sing N N 110 
GLN CA  CB   sing N N 111 
GLN CA  HA   sing N N 112 
GLN C   O    doub N N 113 
GLN C   OXT  sing N N 114 
GLN CB  CG   sing N N 115 
GLN CB  HB2  sing N N 116 
GLN CB  HB3  sing N N 117 
GLN CG  CD   sing N N 118 
GLN CG  HG2  sing N N 119 
GLN CG  HG3  sing N N 120 
GLN CD  OE1  doub N N 121 
GLN CD  NE2  sing N N 122 
GLN NE2 HE21 sing N N 123 
GLN NE2 HE22 sing N N 124 
GLN OXT HXT  sing N N 125 
GLU N   CA   sing N N 126 
GLU N   H    sing N N 127 
GLU N   H2   sing N N 128 
GLU CA  C    sing N N 129 
GLU CA  CB   sing N N 130 
GLU CA  HA   sing N N 131 
GLU C   O    doub N N 132 
GLU C   OXT  sing N N 133 
GLU CB  CG   sing N N 134 
GLU CB  HB2  sing N N 135 
GLU CB  HB3  sing N N 136 
GLU CG  CD   sing N N 137 
GLU CG  HG2  sing N N 138 
GLU CG  HG3  sing N N 139 
GLU CD  OE1  doub N N 140 
GLU CD  OE2  sing N N 141 
GLU OE2 HE2  sing N N 142 
GLU OXT HXT  sing N N 143 
GLY N   CA   sing N N 144 
GLY N   H    sing N N 145 
GLY N   H2   sing N N 146 
GLY CA  C    sing N N 147 
GLY CA  HA2  sing N N 148 
GLY CA  HA3  sing N N 149 
GLY C   O    doub N N 150 
GLY C   OXT  sing N N 151 
GLY OXT HXT  sing N N 152 
GOL C1  O1   sing N N 153 
GOL C1  C2   sing N N 154 
GOL C1  H11  sing N N 155 
GOL C1  H12  sing N N 156 
GOL O1  HO1  sing N N 157 
GOL C2  O2   sing N N 158 
GOL C2  C3   sing N N 159 
GOL C2  H2   sing N N 160 
GOL O2  HO2  sing N N 161 
GOL C3  O3   sing N N 162 
GOL C3  H31  sing N N 163 
GOL C3  H32  sing N N 164 
GOL O3  HO3  sing N N 165 
HIS N   CA   sing N N 166 
HIS N   H    sing N N 167 
HIS N   H2   sing N N 168 
HIS CA  C    sing N N 169 
HIS CA  CB   sing N N 170 
HIS CA  HA   sing N N 171 
HIS C   O    doub N N 172 
HIS C   OXT  sing N N 173 
HIS CB  CG   sing N N 174 
HIS CB  HB2  sing N N 175 
HIS CB  HB3  sing N N 176 
HIS CG  ND1  sing Y N 177 
HIS CG  CD2  doub Y N 178 
HIS ND1 CE1  doub Y N 179 
HIS ND1 HD1  sing N N 180 
HIS CD2 NE2  sing Y N 181 
HIS CD2 HD2  sing N N 182 
HIS CE1 NE2  sing Y N 183 
HIS CE1 HE1  sing N N 184 
HIS NE2 HE2  sing N N 185 
HIS OXT HXT  sing N N 186 
HOH O   H1   sing N N 187 
HOH O   H2   sing N N 188 
ILE N   CA   sing N N 189 
ILE N   H    sing N N 190 
ILE N   H2   sing N N 191 
ILE CA  C    sing N N 192 
ILE CA  CB   sing N N 193 
ILE CA  HA   sing N N 194 
ILE C   O    doub N N 195 
ILE C   OXT  sing N N 196 
ILE CB  CG1  sing N N 197 
ILE CB  CG2  sing N N 198 
ILE CB  HB   sing N N 199 
ILE CG1 CD1  sing N N 200 
ILE CG1 HG12 sing N N 201 
ILE CG1 HG13 sing N N 202 
ILE CG2 HG21 sing N N 203 
ILE CG2 HG22 sing N N 204 
ILE CG2 HG23 sing N N 205 
ILE CD1 HD11 sing N N 206 
ILE CD1 HD12 sing N N 207 
ILE CD1 HD13 sing N N 208 
ILE OXT HXT  sing N N 209 
LEU N   CA   sing N N 210 
LEU N   H    sing N N 211 
LEU N   H2   sing N N 212 
LEU CA  C    sing N N 213 
LEU CA  CB   sing N N 214 
LEU CA  HA   sing N N 215 
LEU C   O    doub N N 216 
LEU C   OXT  sing N N 217 
LEU CB  CG   sing N N 218 
LEU CB  HB2  sing N N 219 
LEU CB  HB3  sing N N 220 
LEU CG  CD1  sing N N 221 
LEU CG  CD2  sing N N 222 
LEU CG  HG   sing N N 223 
LEU CD1 HD11 sing N N 224 
LEU CD1 HD12 sing N N 225 
LEU CD1 HD13 sing N N 226 
LEU CD2 HD21 sing N N 227 
LEU CD2 HD22 sing N N 228 
LEU CD2 HD23 sing N N 229 
LEU OXT HXT  sing N N 230 
LYS N   CA   sing N N 231 
LYS N   H    sing N N 232 
LYS N   H2   sing N N 233 
LYS CA  C    sing N N 234 
LYS CA  CB   sing N N 235 
LYS CA  HA   sing N N 236 
LYS C   O    doub N N 237 
LYS C   OXT  sing N N 238 
LYS CB  CG   sing N N 239 
LYS CB  HB2  sing N N 240 
LYS CB  HB3  sing N N 241 
LYS CG  CD   sing N N 242 
LYS CG  HG2  sing N N 243 
LYS CG  HG3  sing N N 244 
LYS CD  CE   sing N N 245 
LYS CD  HD2  sing N N 246 
LYS CD  HD3  sing N N 247 
LYS CE  NZ   sing N N 248 
LYS CE  HE2  sing N N 249 
LYS CE  HE3  sing N N 250 
LYS NZ  HZ1  sing N N 251 
LYS NZ  HZ2  sing N N 252 
LYS NZ  HZ3  sing N N 253 
LYS OXT HXT  sing N N 254 
MET N   CA   sing N N 255 
MET N   H    sing N N 256 
MET N   H2   sing N N 257 
MET CA  C    sing N N 258 
MET CA  CB   sing N N 259 
MET CA  HA   sing N N 260 
MET C   O    doub N N 261 
MET C   OXT  sing N N 262 
MET CB  CG   sing N N 263 
MET CB  HB2  sing N N 264 
MET CB  HB3  sing N N 265 
MET CG  SD   sing N N 266 
MET CG  HG2  sing N N 267 
MET CG  HG3  sing N N 268 
MET SD  CE   sing N N 269 
MET CE  HE1  sing N N 270 
MET CE  HE2  sing N N 271 
MET CE  HE3  sing N N 272 
MET OXT HXT  sing N N 273 
PHE N   CA   sing N N 274 
PHE N   H    sing N N 275 
PHE N   H2   sing N N 276 
PHE CA  C    sing N N 277 
PHE CA  CB   sing N N 278 
PHE CA  HA   sing N N 279 
PHE C   O    doub N N 280 
PHE C   OXT  sing N N 281 
PHE CB  CG   sing N N 282 
PHE CB  HB2  sing N N 283 
PHE CB  HB3  sing N N 284 
PHE CG  CD1  doub Y N 285 
PHE CG  CD2  sing Y N 286 
PHE CD1 CE1  sing Y N 287 
PHE CD1 HD1  sing N N 288 
PHE CD2 CE2  doub Y N 289 
PHE CD2 HD2  sing N N 290 
PHE CE1 CZ   doub Y N 291 
PHE CE1 HE1  sing N N 292 
PHE CE2 CZ   sing Y N 293 
PHE CE2 HE2  sing N N 294 
PHE CZ  HZ   sing N N 295 
PHE OXT HXT  sing N N 296 
PRO N   CA   sing N N 297 
PRO N   CD   sing N N 298 
PRO N   H    sing N N 299 
PRO CA  C    sing N N 300 
PRO CA  CB   sing N N 301 
PRO CA  HA   sing N N 302 
PRO C   O    doub N N 303 
PRO C   OXT  sing N N 304 
PRO CB  CG   sing N N 305 
PRO CB  HB2  sing N N 306 
PRO CB  HB3  sing N N 307 
PRO CG  CD   sing N N 308 
PRO CG  HG2  sing N N 309 
PRO CG  HG3  sing N N 310 
PRO CD  HD2  sing N N 311 
PRO CD  HD3  sing N N 312 
PRO OXT HXT  sing N N 313 
SER N   CA   sing N N 314 
SER N   H    sing N N 315 
SER N   H2   sing N N 316 
SER CA  C    sing N N 317 
SER CA  CB   sing N N 318 
SER CA  HA   sing N N 319 
SER C   O    doub N N 320 
SER C   OXT  sing N N 321 
SER CB  OG   sing N N 322 
SER CB  HB2  sing N N 323 
SER CB  HB3  sing N N 324 
SER OG  HG   sing N N 325 
SER OXT HXT  sing N N 326 
THR N   CA   sing N N 327 
THR N   H    sing N N 328 
THR N   H2   sing N N 329 
THR CA  C    sing N N 330 
THR CA  CB   sing N N 331 
THR CA  HA   sing N N 332 
THR C   O    doub N N 333 
THR C   OXT  sing N N 334 
THR CB  OG1  sing N N 335 
THR CB  CG2  sing N N 336 
THR CB  HB   sing N N 337 
THR OG1 HG1  sing N N 338 
THR CG2 HG21 sing N N 339 
THR CG2 HG22 sing N N 340 
THR CG2 HG23 sing N N 341 
THR OXT HXT  sing N N 342 
TRP N   CA   sing N N 343 
TRP N   H    sing N N 344 
TRP N   H2   sing N N 345 
TRP CA  C    sing N N 346 
TRP CA  CB   sing N N 347 
TRP CA  HA   sing N N 348 
TRP C   O    doub N N 349 
TRP C   OXT  sing N N 350 
TRP CB  CG   sing N N 351 
TRP CB  HB2  sing N N 352 
TRP CB  HB3  sing N N 353 
TRP CG  CD1  doub Y N 354 
TRP CG  CD2  sing Y N 355 
TRP CD1 NE1  sing Y N 356 
TRP CD1 HD1  sing N N 357 
TRP CD2 CE2  doub Y N 358 
TRP CD2 CE3  sing Y N 359 
TRP NE1 CE2  sing Y N 360 
TRP NE1 HE1  sing N N 361 
TRP CE2 CZ2  sing Y N 362 
TRP CE3 CZ3  doub Y N 363 
TRP CE3 HE3  sing N N 364 
TRP CZ2 CH2  doub Y N 365 
TRP CZ2 HZ2  sing N N 366 
TRP CZ3 CH2  sing Y N 367 
TRP CZ3 HZ3  sing N N 368 
TRP CH2 HH2  sing N N 369 
TRP OXT HXT  sing N N 370 
TYR N   CA   sing N N 371 
TYR N   H    sing N N 372 
TYR N   H2   sing N N 373 
TYR CA  C    sing N N 374 
TYR CA  CB   sing N N 375 
TYR CA  HA   sing N N 376 
TYR C   O    doub N N 377 
TYR C   OXT  sing N N 378 
TYR CB  CG   sing N N 379 
TYR CB  HB2  sing N N 380 
TYR CB  HB3  sing N N 381 
TYR CG  CD1  doub Y N 382 
TYR CG  CD2  sing Y N 383 
TYR CD1 CE1  sing Y N 384 
TYR CD1 HD1  sing N N 385 
TYR CD2 CE2  doub Y N 386 
TYR CD2 HD2  sing N N 387 
TYR CE1 CZ   doub Y N 388 
TYR CE1 HE1  sing N N 389 
TYR CE2 CZ   sing Y N 390 
TYR CE2 HE2  sing N N 391 
TYR CZ  OH   sing N N 392 
TYR OH  HH   sing N N 393 
TYR OXT HXT  sing N N 394 
VAL N   CA   sing N N 395 
VAL N   H    sing N N 396 
VAL N   H2   sing N N 397 
VAL CA  C    sing N N 398 
VAL CA  CB   sing N N 399 
VAL CA  HA   sing N N 400 
VAL C   O    doub N N 401 
VAL C   OXT  sing N N 402 
VAL CB  CG1  sing N N 403 
VAL CB  CG2  sing N N 404 
VAL CB  HB   sing N N 405 
VAL CG1 HG11 sing N N 406 
VAL CG1 HG12 sing N N 407 
VAL CG1 HG13 sing N N 408 
VAL CG2 HG21 sing N N 409 
VAL CG2 HG22 sing N N 410 
VAL CG2 HG23 sing N N 411 
VAL OXT HXT  sing N N 412 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'Other government' China 2021YFC2301405 1 
'Other government' China 21ZR1471800    2 
# 
loop_
_pdbx_entity_branch_list.entity_id 
_pdbx_entity_branch_list.comp_id 
_pdbx_entity_branch_list.num 
_pdbx_entity_branch_list.hetero 
2 GLC 1 n 
2 GLC 2 n 
2 GLC 3 n 
2 GLC 4 n 
2 GLC 5 n 
2 GLC 6 n 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'in silico model' 
_pdbx_initial_refinement_model.source_name      AlphaFold 
_pdbx_initial_refinement_model.accession_code   ? 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9IHW 
_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]   0.016305 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.001757 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.024301 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   0.000000 
_atom_sites.fract_transf_matrix[3][3]   0.005180 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . LYS A 1 2   ? -3.490  20.191 36.246  1.00 27.59 ? 2   LYS A N   1 
ATOM   2    C CA  . LYS A 1 2   ? -2.604  20.394 37.387  1.00 28.51 ? 2   LYS A CA  1 
ATOM   3    C C   . LYS A 1 2   ? -3.401  20.697 38.652  1.00 25.41 ? 2   LYS A C   1 
ATOM   4    O O   . LYS A 1 2   ? -4.132  21.679 38.714  1.00 28.25 ? 2   LYS A O   1 
ATOM   5    C CB  . LYS A 1 2   ? -1.623  21.518 37.090  1.00 30.96 ? 2   LYS A CB  1 
ATOM   6    C CG  . LYS A 1 2   ? -0.639  21.769 38.189  1.00 34.34 ? 2   LYS A CG  1 
ATOM   7    C CD  . LYS A 1 2   ? -0.610  23.238 38.508  1.00 44.53 ? 2   LYS A CD  1 
ATOM   8    C CE  . LYS A 1 2   ? 0.051   24.037 37.413  1.00 43.59 ? 2   LYS A CE  1 
ATOM   9    N NZ  . LYS A 1 2   ? 0.095   25.493 37.741  1.00 32.94 ? 2   LYS A NZ  1 
ATOM   10   N N   . LYS A 1 3   ? -3.271  19.847 39.662  1.00 16.16 ? 3   LYS A N   1 
ATOM   11   C CA  . LYS A 1 3   ? -4.028  20.006 40.892  1.00 18.07 ? 3   LYS A CA  1 
ATOM   12   C C   . LYS A 1 3   ? -3.160  20.582 41.998  1.00 14.74 ? 3   LYS A C   1 
ATOM   13   O O   . LYS A 1 3   ? -1.926  20.512 41.972  1.00 17.65 ? 3   LYS A O   1 
ATOM   14   C CB  . LYS A 1 3   ? -4.614  18.670 41.361  1.00 18.70 ? 3   LYS A CB  1 
ATOM   15   C CG  . LYS A 1 3   ? -5.416  17.930 40.291  1.00 23.45 ? 3   LYS A CG  1 
ATOM   16   C CD  . LYS A 1 3   ? -6.832  18.435 40.215  1.00 34.64 ? 3   LYS A CD  1 
ATOM   17   C CE  . LYS A 1 3   ? -7.744  17.367 39.630  1.00 42.63 ? 3   LYS A CE  1 
ATOM   18   N NZ  . LYS A 1 3   ? -7.706  16.119 40.451  1.00 51.55 ? 3   LYS A NZ  1 
ATOM   19   N N   . LEU A 1 4   ? -3.837  21.164 42.978  1.00 15.30 ? 4   LEU A N   1 
ATOM   20   C CA  . LEU A 1 4   ? -3.251  21.455 44.273  1.00 14.01 ? 4   LEU A CA  1 
ATOM   21   C C   . LEU A 1 4   ? -3.734  20.392 45.243  1.00 13.17 ? 4   LEU A C   1 
ATOM   22   O O   . LEU A 1 4   ? -4.940  20.147 45.345  1.00 16.19 ? 4   LEU A O   1 
ATOM   23   C CB  . LEU A 1 4   ? -3.657  22.839 44.766  1.00 13.71 ? 4   LEU A CB  1 
ATOM   24   C CG  . LEU A 1 4   ? -3.124  23.205 46.154  1.00 13.15 ? 4   LEU A CG  1 
ATOM   25   C CD1 . LEU A 1 4   ? -2.828  24.689 46.186  1.00 14.99 ? 4   LEU A CD1 1 
ATOM   26   C CD2 . LEU A 1 4   ? -4.112  22.848 47.252  1.00 15.04 ? 4   LEU A CD2 1 
ATOM   27   N N   . PHE A 1 5   ? -2.803  19.764 45.947  1.00 14.66 ? 5   PHE A N   1 
ATOM   28   C CA  . PHE A 1 5   ? -3.140  18.720 46.901  1.00 15.31 ? 5   PHE A CA  1 
ATOM   29   C C   . PHE A 1 5   ? -3.198  19.347 48.284  1.00 14.29 ? 5   PHE A C   1 
ATOM   30   O O   . PHE A 1 5   ? -2.223  19.958 48.730  1.00 18.96 ? 5   PHE A O   1 
ATOM   31   C CB  . PHE A 1 5   ? -2.121  17.588 46.863  1.00 15.38 ? 5   PHE A CB  1 
ATOM   32   C CG  . PHE A 1 5   ? -2.090  16.858 45.554  1.00 15.07 ? 5   PHE A CG  1 
ATOM   33   C CD1 . PHE A 1 5   ? -3.249  16.338 45.003  1.00 17.06 ? 5   PHE A CD1 1 
ATOM   34   C CD2 . PHE A 1 5   ? -0.891  16.687 44.881  1.00 16.90 ? 5   PHE A CD2 1 
ATOM   35   C CE1 . PHE A 1 5   ? -3.207  15.675 43.787  1.00 16.53 ? 5   PHE A CE1 1 
ATOM   36   C CE2 . PHE A 1 5   ? -0.842  16.016 43.675  1.00 20.12 ? 5   PHE A CE2 1 
ATOM   37   C CZ  . PHE A 1 5   ? -2.001  15.509 43.127  1.00 17.68 ? 5   PHE A CZ  1 
ATOM   38   N N   . LEU A 1 6   ? -4.333  19.194 48.952  1.00 11.54 ? 6   LEU A N   1 
ATOM   39   C CA  . LEU A 1 6   ? -4.590  19.845 50.230  1.00 11.63 ? 6   LEU A CA  1 
ATOM   40   C C   . LEU A 1 6   ? -4.785  18.762 51.278  1.00 13.62 ? 6   LEU A C   1 
ATOM   41   O O   . LEU A 1 6   ? -5.572  17.830 51.070  1.00 13.47 ? 6   LEU A O   1 
ATOM   42   C CB  . LEU A 1 6   ? -5.839  20.734 50.133  1.00 12.14 ? 6   LEU A CB  1 
ATOM   43   C CG  . LEU A 1 6   ? -6.233  21.507 51.390  1.00 11.94 ? 6   LEU A CG  1 
ATOM   44   C CD1 . LEU A 1 6   ? -5.088  22.437 51.821  1.00 13.81 ? 6   LEU A CD1 1 
ATOM   45   C CD2 . LEU A 1 6   ? -7.506  22.295 51.121  1.00 11.59 ? 6   LEU A CD2 1 
ATOM   46   N N   . VAL A 1 7   ? -4.084  18.873 52.402  1.00 10.32 ? 7   VAL A N   1 
ATOM   47   C CA  . VAL A 1 7   ? -4.104  17.815 53.412  1.00 10.00 ? 7   VAL A CA  1 
ATOM   48   C C   . VAL A 1 7   ? -4.394  18.457 54.762  1.00 10.86 ? 7   VAL A C   1 
ATOM   49   O O   . VAL A 1 7   ? -3.536  19.151 55.317  1.00 13.30 ? 7   VAL A O   1 
ATOM   50   C CB  . VAL A 1 7   ? -2.785  17.028 53.451  1.00 12.81 ? 7   VAL A CB  1 
ATOM   51   C CG1 . VAL A 1 7   ? -2.912  15.833 54.358  1.00 13.17 ? 7   VAL A CG1 1 
ATOM   52   C CG2 . VAL A 1 7   ? -2.384  16.558 52.049  1.00 12.50 ? 7   VAL A CG2 1 
ATOM   53   N N   . PHE A 1 8   ? -5.605  18.245 55.281  1.00 10.07 ? 8   PHE A N   1 
ATOM   54   C CA  . PHE A 1 8   ? -5.946  18.660 56.639  1.00 11.98 ? 8   PHE A CA  1 
ATOM   55   C C   . PHE A 1 8   ? -5.517  17.580 57.611  1.00 10.27 ? 8   PHE A C   1 
ATOM   56   O O   . PHE A 1 8   ? -5.796  16.397 57.394  1.00 13.37 ? 8   PHE A O   1 
ATOM   57   C CB  . PHE A 1 8   ? -7.451  18.905 56.797  1.00 10.08 ? 8   PHE A CB  1 
ATOM   58   C CG  . PHE A 1 8   ? -7.934  20.138 56.100  1.00 12.13 ? 8   PHE A CG  1 
ATOM   59   C CD1 . PHE A 1 8   ? -7.942  21.359 56.749  1.00 12.86 ? 8   PHE A CD1 1 
ATOM   60   C CD2 . PHE A 1 8   ? -8.389  20.070 54.794  1.00 13.68 ? 8   PHE A CD2 1 
ATOM   61   C CE1 . PHE A 1 8   ? -8.375  22.500 56.095  1.00 14.29 ? 8   PHE A CE1 1 
ATOM   62   C CE2 . PHE A 1 8   ? -8.838  21.210 54.142  1.00 13.05 ? 8   PHE A CE2 1 
ATOM   63   C CZ  . PHE A 1 8   ? -8.821  22.415 54.786  1.00 13.06 ? 8   PHE A CZ  1 
ATOM   64   N N   . TRP A 1 9   ? -4.899  17.989 58.713  1.00 8.65  ? 9   TRP A N   1 
ATOM   65   C CA  . TRP A 1 9   ? -4.531  17.037 59.757  1.00 9.56  ? 9   TRP A CA  1 
ATOM   66   C C   . TRP A 1 9   ? -4.881  17.714 61.076  1.00 10.32 ? 9   TRP A C   1 
ATOM   67   O O   . TRP A 1 9   ? -4.203  18.651 61.503  1.00 9.33  ? 9   TRP A O   1 
ATOM   68   C CB  . TRP A 1 9   ? -3.057  16.671 59.657  1.00 8.93  ? 9   TRP A CB  1 
ATOM   69   C CG  . TRP A 1 9   ? -2.610  15.454 60.412  1.00 11.85 ? 9   TRP A CG  1 
ATOM   70   C CD1 . TRP A 1 9   ? -3.330  14.693 61.296  1.00 14.53 ? 9   TRP A CD1 1 
ATOM   71   C CD2 . TRP A 1 9   ? -1.314  14.872 60.338  1.00 11.70 ? 9   TRP A CD2 1 
ATOM   72   N NE1 . TRP A 1 9   ? -2.542  13.670 61.777  1.00 11.71 ? 9   TRP A NE1 1 
ATOM   73   C CE2 . TRP A 1 9   ? -1.302  13.755 61.196  1.00 13.68 ? 9   TRP A CE2 1 
ATOM   74   C CE3 . TRP A 1 9   ? -0.160  15.182 59.610  1.00 14.32 ? 9   TRP A CE3 1 
ATOM   75   C CZ2 . TRP A 1 9   ? -0.173  12.948 61.354  1.00 10.71 ? 9   TRP A CZ2 1 
ATOM   76   C CZ3 . TRP A 1 9   ? 0.958   14.378 59.752  1.00 10.03 ? 9   TRP A CZ3 1 
ATOM   77   C CH2 . TRP A 1 9   ? 0.949   13.277 60.625  1.00 10.88 ? 9   TRP A CH2 1 
ATOM   78   N N   . TRP A 1 10  ? -5.985  17.265 61.674  1.00 9.43  ? 10  TRP A N   1 
ATOM   79   C CA  . TRP A 1 10  ? -6.533  17.844 62.889  1.00 7.90  ? 10  TRP A CA  1 
ATOM   80   C C   . TRP A 1 10  ? -6.028  17.059 64.092  1.00 7.96  ? 10  TRP A C   1 
ATOM   81   O O   . TRP A 1 10  ? -6.291  15.852 64.200  1.00 11.97 ? 10  TRP A O   1 
ATOM   82   C CB  . TRP A 1 10  ? -8.060  17.800 62.844  1.00 7.88  ? 10  TRP A CB  1 
ATOM   83   C CG  . TRP A 1 10  ? -8.713  18.549 61.709  1.00 9.98  ? 10  TRP A CG  1 
ATOM   84   C CD1 . TRP A 1 10  ? -9.418  18.002 60.668  1.00 11.08 ? 10  TRP A CD1 1 
ATOM   85   C CD2 . TRP A 1 10  ? -8.801  19.975 61.544  1.00 10.89 ? 10  TRP A CD2 1 
ATOM   86   N NE1 . TRP A 1 10  ? -9.921  19.002 59.860  1.00 12.82 ? 10  TRP A NE1 1 
ATOM   87   C CE2 . TRP A 1 10  ? -9.556  20.215 60.376  1.00 10.99 ? 10  TRP A CE2 1 
ATOM   88   C CE3 . TRP A 1 10  ? -8.299  21.069 62.260  1.00 12.28 ? 10  TRP A CE3 1 
ATOM   89   C CZ2 . TRP A 1 10  ? -9.813  21.489 59.908  1.00 9.35  ? 10  TRP A CZ2 1 
ATOM   90   C CZ3 . TRP A 1 10  ? -8.555  22.343 61.790  1.00 12.37 ? 10  TRP A CZ3 1 
ATOM   91   C CH2 . TRP A 1 10  ? -9.308  22.545 60.629  1.00 12.88 ? 10  TRP A CH2 1 
ATOM   92   N N   . HIS A 1 11  ? -5.373  17.751 65.021  1.00 8.44  ? 11  HIS A N   1 
ATOM   93   C CA  . HIS A 1 11  ? -4.689  17.101 66.135  1.00 9.82  ? 11  HIS A CA  1 
ATOM   94   C C   . HIS A 1 11  ? -5.543  17.230 67.388  1.00 9.24  ? 11  HIS A C   1 
ATOM   95   O O   . HIS A 1 11  ? -5.889  18.343 67.795  1.00 10.06 ? 11  HIS A O   1 
ATOM   96   C CB  . HIS A 1 11  ? -3.299  17.708 66.343  1.00 10.19 ? 11  HIS A CB  1 
ATOM   97   C CG  . HIS A 1 11  ? -2.724  17.448 67.699  1.00 10.15 ? 11  HIS A CG  1 
ATOM   98   N ND1 . HIS A 1 11  ? -2.430  16.182 68.152  1.00 8.22  ? 11  HIS A ND1 1 
ATOM   99   C CD2 . HIS A 1 11  ? -2.396  18.296 68.706  1.00 11.44 ? 11  HIS A CD2 1 
ATOM   100  C CE1 . HIS A 1 11  ? -1.945  16.257 69.380  1.00 12.31 ? 11  HIS A CE1 1 
ATOM   101  N NE2 . HIS A 1 11  ? -1.917  17.529 69.741  1.00 11.58 ? 11  HIS A NE2 1 
ATOM   102  N N   . MET A 1 12  ? -5.894  16.087 67.983  1.00 10.13 ? 12  MET A N   1 
ATOM   103  C CA  . MET A 1 12  ? -6.772  16.020 69.144  1.00 8.93  ? 12  MET A CA  1 
ATOM   104  C C   . MET A 1 12  ? -5.999  15.475 70.331  1.00 9.72  ? 12  MET A C   1 
ATOM   105  O O   . MET A 1 12  ? -5.387  14.407 70.235  1.00 10.13 ? 12  MET A O   1 
ATOM   106  C CB  . MET A 1 12  ? -7.973  15.109 68.868  1.00 7.60  ? 12  MET A CB  1 
ATOM   107  C CG  . MET A 1 12  ? -8.656  15.377 67.547  1.00 9.44  ? 12  MET A CG  1 
ATOM   108  S SD  . MET A 1 12  ? -9.318  17.038 67.464  1.00 10.80 ? 12  MET A SD  1 
ATOM   109  C CE  . MET A 1 12  ? -10.472 16.856 66.084  1.00 13.80 ? 12  MET A CE  1 
ATOM   110  N N   . HIS A 1 13  ? -6.050  16.184 71.460  1.00 8.14  ? 13  HIS A N   1 
ATOM   111  C CA  . HIS A 1 13  ? -5.256  15.758 72.599  1.00 7.85  ? 13  HIS A CA  1 
ATOM   112  C C   . HIS A 1 13  ? -5.809  16.385 73.868  1.00 7.77  ? 13  HIS A C   1 
ATOM   113  O O   . HIS A 1 13  ? -6.274  17.517 73.846  1.00 8.87  ? 13  HIS A O   1 
ATOM   114  C CB  . HIS A 1 13  ? -3.778  16.161 72.418  1.00 7.92  ? 13  HIS A CB  1 
ATOM   115  C CG  . HIS A 1 13  ? -2.985  16.048 73.675  1.00 9.61  ? 13  HIS A CG  1 
ATOM   116  N ND1 . HIS A 1 13  ? -2.826  14.850 74.338  1.00 8.39  ? 13  HIS A ND1 1 
ATOM   117  C CD2 . HIS A 1 13  ? -2.329  16.979 74.415  1.00 11.27 ? 13  HIS A CD2 1 
ATOM   118  C CE1 . HIS A 1 13  ? -2.099  15.044 75.425  1.00 8.64  ? 13  HIS A CE1 1 
ATOM   119  N NE2 . HIS A 1 13  ? -1.788  16.328 75.496  1.00 9.93  ? 13  HIS A NE2 1 
ATOM   120  N N   . GLN A 1 14  ? -5.761  15.630 74.970  1.00 7.93  ? 14  GLN A N   1 
ATOM   121  C CA  . GLN A 1 14  ? -5.942  16.184 76.317  1.00 8.00  ? 14  GLN A CA  1 
ATOM   122  C C   . GLN A 1 14  ? -4.957  15.452 77.224  1.00 12.47 ? 14  GLN A C   1 
ATOM   123  O O   . GLN A 1 14  ? -4.809  14.220 77.115  1.00 9.29  ? 14  GLN A O   1 
ATOM   124  C CB  . GLN A 1 14  ? -7.377  16.009 76.859  1.00 8.88  ? 14  GLN A CB  1 
ATOM   125  C CG  . GLN A 1 14  ? -8.478  16.735 76.104  1.00 7.70  ? 14  GLN A CG  1 
ATOM   126  C CD  . GLN A 1 14  ? -8.408  18.233 76.258  1.00 11.08 ? 14  GLN A CD  1 
ATOM   127  O OE1 . GLN A 1 14  ? -7.824  18.758 77.216  1.00 10.38 ? 14  GLN A OE1 1 
ATOM   128  N NE2 . GLN A 1 14  ? -8.985  18.940 75.289  1.00 9.88  ? 14  GLN A NE2 1 
ATOM   129  N N   . PRO A 1 15  ? -4.278  16.163 78.125  1.00 12.20 ? 15  PRO A N   1 
ATOM   130  C CA  . PRO A 1 15  ? -3.489  15.483 79.160  1.00 10.37 ? 15  PRO A CA  1 
ATOM   131  C C   . PRO A 1 15  ? -4.424  14.749 80.110  1.00 10.84 ? 15  PRO A C   1 
ATOM   132  O O   . PRO A 1 15  ? -5.643  14.947 80.101  1.00 10.95 ? 15  PRO A O   1 
ATOM   133  C CB  . PRO A 1 15  ? -2.765  16.636 79.872  1.00 9.08  ? 15  PRO A CB  1 
ATOM   134  C CG  . PRO A 1 15  ? -3.802  17.792 79.773  1.00 9.14  ? 15  PRO A CG  1 
ATOM   135  C CD  . PRO A 1 15  ? -4.374  17.626 78.363  1.00 9.99  ? 15  PRO A CD  1 
ATOM   136  N N   . LEU A 1 16  ? -3.841  13.908 80.964  1.00 9.50  ? 16  LEU A N   1 
ATOM   137  C CA  . LEU A 1 16  ? -4.652  13.080 81.858  1.00 10.97 ? 16  LEU A CA  1 
ATOM   138  C C   . LEU A 1 16  ? -5.165  13.913 83.031  1.00 12.97 ? 16  LEU A C   1 
ATOM   139  O O   . LEU A 1 16  ? -4.391  14.307 83.904  1.00 12.53 ? 16  LEU A O   1 
ATOM   140  C CB  . LEU A 1 16  ? -3.833  11.885 82.338  1.00 10.26 ? 16  LEU A CB  1 
ATOM   141  C CG  . LEU A 1 16  ? -4.634  10.832 83.122  1.00 10.60 ? 16  LEU A CG  1 
ATOM   142  C CD1 . LEU A 1 16  ? -5.845  10.335 82.302  1.00 11.36 ? 16  LEU A CD1 1 
ATOM   143  C CD2 . LEU A 1 16  ? -3.750  9.649  83.551  1.00 12.32 ? 16  LEU A CD2 1 
ATOM   144  N N   . TYR A 1 17  ? -6.482  14.157 83.071  1.00 10.31 ? 17  TYR A N   1 
ATOM   145  C CA  . TYR A 1 17  ? -7.076  14.919 84.164  1.00 11.45 ? 17  TYR A CA  1 
ATOM   146  C C   . TYR A 1 17  ? -7.461  14.049 85.340  1.00 14.78 ? 17  TYR A C   1 
ATOM   147  O O   . TYR A 1 17  ? -7.926  14.577 86.356  1.00 13.23 ? 17  TYR A O   1 
ATOM   148  C CB  . TYR A 1 17  ? -8.317  15.663 83.692  1.00 9.51  ? 17  TYR A CB  1 
ATOM   149  C CG  . TYR A 1 17  ? -8.033  16.674 82.611  1.00 10.01 ? 17  TYR A CG  1 
ATOM   150  C CD1 . TYR A 1 17  ? -7.240  17.785 82.875  1.00 9.19  ? 17  TYR A CD1 1 
ATOM   151  C CD2 . TYR A 1 17  ? -8.548  16.516 81.330  1.00 11.84 ? 17  TYR A CD2 1 
ATOM   152  C CE1 . TYR A 1 17  ? -6.980  18.736 81.895  1.00 10.19 ? 17  TYR A CE1 1 
ATOM   153  C CE2 . TYR A 1 17  ? -8.288  17.457 80.331  1.00 8.74  ? 17  TYR A CE2 1 
ATOM   154  C CZ  . TYR A 1 17  ? -7.493  18.563 80.629  1.00 8.34  ? 17  TYR A CZ  1 
ATOM   155  O OH  . TYR A 1 17  ? -7.220  19.505 79.666  1.00 12.01 ? 17  TYR A OH  1 
ATOM   156  N N   . ARG A 1 18  ? -7.271  12.739 85.218  1.00 12.43 ? 18  ARG A N   1 
ATOM   157  C CA  . ARG A 1 18  ? -7.680  11.781 86.237  1.00 14.11 ? 18  ARG A CA  1 
ATOM   158  C C   . ARG A 1 18  ? -6.640  11.713 87.352  1.00 13.35 ? 18  ARG A C   1 
ATOM   159  O O   . ARG A 1 18  ? -5.556  11.152 87.163  1.00 12.00 ? 18  ARG A O   1 
ATOM   160  C CB  . ARG A 1 18  ? -7.866  10.421 85.580  1.00 13.49 ? 18  ARG A CB  1 
ATOM   161  C CG  . ARG A 1 18  ? -8.464  9.362  86.491  1.00 15.98 ? 18  ARG A CG  1 
ATOM   162  C CD  . ARG A 1 18  ? -8.446  8.033  85.752  1.00 23.36 ? 18  ARG A CD  1 
ATOM   163  N NE  . ARG A 1 18  ? -9.209  7.014  86.461  1.00 21.97 ? 18  ARG A NE  1 
ATOM   164  C CZ  . ARG A 1 18  ? -8.763  6.335  87.510  1.00 21.35 ? 18  ARG A CZ  1 
ATOM   165  N NH1 . ARG A 1 18  ? -7.542  6.538  87.989  1.00 26.37 ? 18  ARG A NH1 1 
ATOM   166  N NH2 . ARG A 1 18  ? -9.553  5.439  88.085  1.00 32.14 ? 18  ARG A NH2 1 
ATOM   167  N N   . GLU A 1 19  ? -6.990  12.234 88.529  1.00 12.64 ? 19  GLU A N   1 
ATOM   168  C CA  . GLU A 1 19  ? -6.094  12.195 89.679  1.00 14.98 ? 19  GLU A CA  1 
ATOM   169  C C   . GLU A 1 19  ? -5.846  10.745 90.096  1.00 15.82 ? 19  GLU A C   1 
ATOM   170  O O   . GLU A 1 19  ? -6.801  9.974  90.237  1.00 14.52 ? 19  GLU A O   1 
ATOM   171  C CB  . GLU A 1 19  ? -6.722  12.991 90.824  1.00 15.44 ? 19  GLU A CB  1 
ATOM   172  C CG  . GLU A 1 19  ? -5.718  13.653 91.756  1.00 23.92 ? 19  GLU A CG  1 
ATOM   173  C CD  . GLU A 1 19  ? -5.247  12.717 92.848  1.00 33.98 ? 19  GLU A CD  1 
ATOM   174  O OE1 . GLU A 1 19  ? -5.976  11.755 93.150  1.00 25.26 ? 19  GLU A OE1 1 
ATOM   175  O OE2 . GLU A 1 19  ? -4.149  12.937 93.396  1.00 35.27 ? 19  GLU A OE2 1 
ATOM   176  N N   . PRO A 1 20  ? -4.590  10.329 90.282  1.00 17.38 ? 20  PRO A N   1 
ATOM   177  C CA  . PRO A 1 20  ? -4.305  8.889  90.375  1.00 21.17 ? 20  PRO A CA  1 
ATOM   178  C C   . PRO A 1 20  ? -4.704  8.257  91.692  1.00 23.06 ? 20  PRO A C   1 
ATOM   179  O O   . PRO A 1 20  ? -4.875  7.032  91.740  1.00 32.87 ? 20  PRO A O   1 
ATOM   180  C CB  . PRO A 1 20  ? -2.783  8.824  90.173  1.00 22.99 ? 20  PRO A CB  1 
ATOM   181  C CG  . PRO A 1 20  ? -2.295  10.177 90.648  1.00 15.38 ? 20  PRO A CG  1 
ATOM   182  C CD  . PRO A 1 20  ? -3.359  11.145 90.237  1.00 15.05 ? 20  PRO A CD  1 
ATOM   183  N N   . TYR A 1 21  ? -4.850  9.038  92.757  1.00 18.85 ? 21  TYR A N   1 
ATOM   184  C CA  . TYR A 1 21  ? -5.202  8.458  94.043  1.00 21.26 ? 21  TYR A CA  1 
ATOM   185  C C   . TYR A 1 21  ? -6.712  8.345  94.226  1.00 23.37 ? 21  TYR A C   1 
ATOM   186  O O   . TYR A 1 21  ? -7.203  7.317  94.712  1.00 27.42 ? 21  TYR A O   1 
ATOM   187  C CB  . TYR A 1 21  ? -4.573  9.288  95.162  1.00 19.92 ? 21  TYR A CB  1 
ATOM   188  C CG  . TYR A 1 21  ? -3.064  9.191  95.176  1.00 25.76 ? 21  TYR A CG  1 
ATOM   189  C CD1 . TYR A 1 21  ? -2.425  8.186  95.890  1.00 30.07 ? 21  TYR A CD1 1 
ATOM   190  C CD2 . TYR A 1 21  ? -2.276  10.089 94.455  1.00 23.64 ? 21  TYR A CD2 1 
ATOM   191  C CE1 . TYR A 1 21  ? -1.045  8.079  95.911  1.00 30.33 ? 21  TYR A CE1 1 
ATOM   192  C CE2 . TYR A 1 21  ? -0.883  9.988  94.474  1.00 22.52 ? 21  TYR A CE2 1 
ATOM   193  C CZ  . TYR A 1 21  ? -0.282  8.978  95.201  1.00 29.76 ? 21  TYR A CZ  1 
ATOM   194  O OH  . TYR A 1 21  ? 1.093   8.862  95.231  1.00 30.08 ? 21  TYR A OH  1 
ATOM   195  N N   . THR A 1 22  ? -7.455  9.379  93.824  1.00 17.35 ? 22  THR A N   1 
ATOM   196  C CA  . THR A 1 22  ? -8.910  9.400  93.948  1.00 17.88 ? 22  THR A CA  1 
ATOM   197  C C   . THR A 1 22  ? -9.630  8.884  92.710  1.00 19.71 ? 22  THR A C   1 
ATOM   198  O O   . THR A 1 22  ? -10.815 8.532  92.800  1.00 21.72 ? 22  THR A O   1 
ATOM   199  C CB  . THR A 1 22  ? -9.411  10.825 94.222  1.00 23.63 ? 22  THR A CB  1 
ATOM   200  O OG1 . THR A 1 22  ? -9.057  11.682 93.120  1.00 19.45 ? 22  THR A OG1 1 
ATOM   201  C CG2 . THR A 1 22  ? -8.831  11.376 95.526  1.00 22.99 ? 22  THR A CG2 1 
ATOM   202  N N   . GLY A 1 23  ? -8.967  8.859  91.558  1.00 16.15 ? 23  GLY A N   1 
ATOM   203  C CA  . GLY A 1 23  ? -9.644  8.557  90.310  1.00 18.75 ? 23  GLY A CA  1 
ATOM   204  C C   . GLY A 1 23  ? -10.508 9.678  89.762  1.00 22.30 ? 23  GLY A C   1 
ATOM   205  O O   . GLY A 1 23  ? -11.170 9.486  88.735  1.00 24.10 ? 23  GLY A O   1 
ATOM   206  N N   . GLU A 1 24  ? -10.508 10.849 90.390  1.00 16.93 ? 24  GLU A N   1 
ATOM   207  C CA  . GLU A 1 24  ? -11.394 11.936 89.979  1.00 11.96 ? 24  GLU A CA  1 
ATOM   208  C C   . GLU A 1 24  ? -10.800 12.712 88.804  1.00 13.27 ? 24  GLU A C   1 
ATOM   209  O O   . GLU A 1 24  ? -9.607  13.053 88.814  1.00 13.65 ? 24  GLU A O   1 
ATOM   210  C CB  . GLU A 1 24  ? -11.635 12.887 91.145  1.00 17.38 ? 24  GLU A CB  1 
ATOM   211  C CG  . GLU A 1 24  ? -12.377 12.249 92.299  1.00 23.08 ? 24  GLU A CG  1 
ATOM   212  C CD  . GLU A 1 24  ? -12.525 13.182 93.487  1.00 32.31 ? 24  GLU A CD  1 
ATOM   213  O OE1 . GLU A 1 24  ? -13.232 12.809 94.444  1.00 43.91 ? 24  GLU A OE1 1 
ATOM   214  O OE2 . GLU A 1 24  ? -11.933 14.282 93.470  1.00 38.73 ? 24  GLU A OE2 1 
ATOM   215  N N   . TYR A 1 25  ? -11.630 12.990 87.798  1.00 10.58 ? 25  TYR A N   1 
ATOM   216  C CA  . TYR A 1 25  ? -11.247 13.902 86.723  1.00 11.66 ? 25  TYR A CA  1 
ATOM   217  C C   . TYR A 1 25  ? -11.398 15.322 87.259  1.00 10.03 ? 25  TYR A C   1 
ATOM   218  O O   . TYR A 1 25  ? -12.513 15.787 87.496  1.00 13.10 ? 25  TYR A O   1 
ATOM   219  C CB  . TYR A 1 25  ? -12.092 13.687 85.475  1.00 13.52 ? 25  TYR A CB  1 
ATOM   220  C CG  . TYR A 1 25  ? -11.615 12.547 84.606  1.00 9.78  ? 25  TYR A CG  1 
ATOM   221  C CD1 . TYR A 1 25  ? -11.795 11.218 84.999  1.00 13.88 ? 25  TYR A CD1 1 
ATOM   222  C CD2 . TYR A 1 25  ? -10.978 12.794 83.400  1.00 12.82 ? 25  TYR A CD2 1 
ATOM   223  C CE1 . TYR A 1 25  ? -11.355 10.181 84.213  1.00 14.85 ? 25  TYR A CE1 1 
ATOM   224  C CE2 . TYR A 1 25  ? -10.508 11.745 82.608  1.00 9.73  ? 25  TYR A CE2 1 
ATOM   225  C CZ  . TYR A 1 25  ? -10.720 10.457 83.011  1.00 15.87 ? 25  TYR A CZ  1 
ATOM   226  O OH  . TYR A 1 25  ? -10.280 9.416  82.225  1.00 16.89 ? 25  TYR A OH  1 
ATOM   227  N N   . LEU A 1 26  ? -10.275 16.007 87.467  1.00 11.45 ? 26  LEU A N   1 
ATOM   228  C CA  . LEU A 1 26  ? -10.304 17.278 88.184  1.00 12.32 ? 26  LEU A CA  1 
ATOM   229  C C   . LEU A 1 26  ? -10.694 18.471 87.321  1.00 10.87 ? 26  LEU A C   1 
ATOM   230  O O   . LEU A 1 26  ? -10.987 19.534 87.875  1.00 12.85 ? 26  LEU A O   1 
ATOM   231  C CB  . LEU A 1 26  ? -8.938  17.549 88.826  1.00 12.36 ? 26  LEU A CB  1 
ATOM   232  C CG  . LEU A 1 26  ? -8.481  16.501 89.835  1.00 16.61 ? 26  LEU A CG  1 
ATOM   233  C CD1 . LEU A 1 26  ? -7.163  16.937 90.483  1.00 18.53 ? 26  LEU A CD1 1 
ATOM   234  C CD2 . LEU A 1 26  ? -9.555  16.236 90.883  1.00 16.20 ? 26  LEU A CD2 1 
ATOM   235  N N   . LEU A 1 27  ? -10.665 18.341 85.997  1.00 9.31  ? 27  LEU A N   1 
ATOM   236  C CA  . LEU A 1 27  ? -11.132 19.339 85.048  1.00 9.59  ? 27  LEU A CA  1 
ATOM   237  C C   . LEU A 1 27  ? -12.011 18.635 84.030  1.00 15.30 ? 27  LEU A C   1 
ATOM   238  O O   . LEU A 1 27  ? -11.769 17.467 83.718  1.00 12.12 ? 27  LEU A O   1 
ATOM   239  C CB  . LEU A 1 27  ? -9.965  20.033 84.324  1.00 11.32 ? 27  LEU A CB  1 
ATOM   240  C CG  . LEU A 1 27  ? -9.130  20.922 85.258  1.00 12.58 ? 27  LEU A CG  1 
ATOM   241  C CD1 . LEU A 1 27  ? -7.865  21.414 84.581  1.00 15.87 ? 27  LEU A CD1 1 
ATOM   242  C CD2 . LEU A 1 27  ? -9.978  22.080 85.762  1.00 17.00 ? 27  LEU A CD2 1 
ATOM   243  N N   . PRO A 1 28  ? -13.040 19.309 83.516  1.00 12.47 ? 28  PRO A N   1 
ATOM   244  C CA  . PRO A 1 28  ? -13.989 18.683 82.582  1.00 9.07  ? 28  PRO A CA  1 
ATOM   245  C C   . PRO A 1 28  ? -13.602 18.809 81.114  1.00 8.32  ? 28  PRO A C   1 
ATOM   246  O O   . PRO A 1 28  ? -14.444 18.534 80.256  1.00 11.03 ? 28  PRO A O   1 
ATOM   247  C CB  . PRO A 1 28  ? -15.269 19.488 82.851  1.00 10.04 ? 28  PRO A CB  1 
ATOM   248  C CG  . PRO A 1 28  ? -14.728 20.905 83.107  1.00 10.65 ? 28  PRO A CG  1 
ATOM   249  C CD  . PRO A 1 28  ? -13.467 20.673 83.907  1.00 15.51 ? 28  PRO A CD  1 
ATOM   250  N N   . TRP A 1 29  ? -12.369 19.210 80.799  1.00 10.61 ? 29  TRP A N   1 
ATOM   251  C CA  . TRP A 1 29  ? -12.064 19.596 79.422  1.00 9.57  ? 29  TRP A CA  1 
ATOM   252  C C   . TRP A 1 29  ? -12.148 18.431 78.446  1.00 10.57 ? 29  TRP A C   1 
ATOM   253  O O   . TRP A 1 29  ? -12.498 18.634 77.278  1.00 10.08 ? 29  TRP A O   1 
ATOM   254  C CB  . TRP A 1 29  ? -10.674 20.229 79.355  1.00 9.29  ? 29  TRP A CB  1 
ATOM   255  C CG  . TRP A 1 29  ? -10.524 21.552 80.126  1.00 13.00 ? 29  TRP A CG  1 
ATOM   256  C CD1 . TRP A 1 29  ? -9.538  21.849 81.010  1.00 11.87 ? 29  TRP A CD1 1 
ATOM   257  C CD2 . TRP A 1 29  ? -11.356 22.735 80.041  1.00 13.08 ? 29  TRP A CD2 1 
ATOM   258  N NE1 . TRP A 1 29  ? -9.684  23.130 81.484  1.00 11.39 ? 29  TRP A NE1 1 
ATOM   259  C CE2 . TRP A 1 29  ? -10.783 23.705 80.901  1.00 12.56 ? 29  TRP A CE2 1 
ATOM   260  C CE3 . TRP A 1 29  ? -12.489 23.080 79.297  1.00 13.85 ? 29  TRP A CE3 1 
ATOM   261  C CZ2 . TRP A 1 29  ? -11.317 24.987 81.051  1.00 18.91 ? 29  TRP A CZ2 1 
ATOM   262  C CZ3 . TRP A 1 29  ? -13.031 24.374 79.448  1.00 10.23 ? 29  TRP A CZ3 1 
ATOM   263  C CH2 . TRP A 1 29  ? -12.446 25.300 80.327  1.00 14.90 ? 29  TRP A CH2 1 
ATOM   264  N N   . THR A 1 30  ? -11.800 17.208 78.866  1.00 10.40 ? 30  THR A N   1 
ATOM   265  C CA  . THR A 1 30  ? -11.987 16.083 77.951  1.00 10.00 ? 30  THR A CA  1 
ATOM   266  C C   . THR A 1 30  ? -13.465 15.861 77.665  1.00 8.91  ? 30  THR A C   1 
ATOM   267  O O   . THR A 1 30  ? -13.847 15.594 76.520  1.00 10.96 ? 30  THR A O   1 
ATOM   268  C CB  . THR A 1 30  ? -11.338 14.825 78.519  1.00 9.78  ? 30  THR A CB  1 
ATOM   269  O OG1 . THR A 1 30  ? -9.941  15.075 78.674  1.00 11.63 ? 30  THR A OG1 1 
ATOM   270  C CG2 . THR A 1 30  ? -11.532 13.620 77.570  1.00 11.97 ? 30  THR A CG2 1 
ATOM   271  N N   . PHE A 1 31  ? -14.315 15.961 78.687  1.00 9.13  ? 31  PHE A N   1 
ATOM   272  C CA  . PHE A 1 31  ? -15.747 15.784 78.455  1.00 8.96  ? 31  PHE A CA  1 
ATOM   273  C C   . PHE A 1 31  ? -16.259 16.833 77.481  1.00 12.42 ? 31  PHE A C   1 
ATOM   274  O O   . PHE A 1 31  ? -16.964 16.523 76.516  1.00 10.77 ? 31  PHE A O   1 
ATOM   275  C CB  . PHE A 1 31  ? -16.524 15.884 79.773  1.00 10.00 ? 31  PHE A CB  1 
ATOM   276  C CG  . PHE A 1 31  ? -18.030 15.853 79.592  1.00 10.97 ? 31  PHE A CG  1 
ATOM   277  C CD1 . PHE A 1 31  ? -18.686 14.652 79.374  1.00 14.95 ? 31  PHE A CD1 1 
ATOM   278  C CD2 . PHE A 1 31  ? -18.778 17.024 79.606  1.00 11.05 ? 31  PHE A CD2 1 
ATOM   279  C CE1 . PHE A 1 31  ? -20.073 14.612 79.195  1.00 11.73 ? 31  PHE A CE1 1 
ATOM   280  C CE2 . PHE A 1 31  ? -20.179 16.995 79.420  1.00 12.49 ? 31  PHE A CE2 1 
ATOM   281  C CZ  . PHE A 1 31  ? -20.816 15.784 79.212  1.00 14.12 ? 31  PHE A CZ  1 
ATOM   282  N N   . PHE A 1 32  ? -15.887 18.087 77.705  1.00 8.76  ? 32  PHE A N   1 
ATOM   283  C CA  . PHE A 1 32  ? -16.478 19.147 76.896  1.00 8.05  ? 32  PHE A CA  1 
ATOM   284  C C   . PHE A 1 32  ? -15.950 19.126 75.469  1.00 10.18 ? 32  PHE A C   1 
ATOM   285  O O   . PHE A 1 32  ? -16.717 19.337 74.531  1.00 10.04 ? 32  PHE A O   1 
ATOM   286  C CB  . PHE A 1 32  ? -16.249 20.492 77.573  1.00 11.30 ? 32  PHE A CB  1 
ATOM   287  C CG  . PHE A 1 32  ? -17.216 20.766 78.692  1.00 12.15 ? 32  PHE A CG  1 
ATOM   288  C CD1 . PHE A 1 32  ? -18.584 20.572 78.509  1.00 11.59 ? 32  PHE A CD1 1 
ATOM   289  C CD2 . PHE A 1 32  ? -16.760 21.203 79.922  1.00 13.30 ? 32  PHE A CD2 1 
ATOM   290  C CE1 . PHE A 1 32  ? -19.479 20.834 79.540  1.00 13.73 ? 32  PHE A CE1 1 
ATOM   291  C CE2 . PHE A 1 32  ? -17.641 21.460 80.945  1.00 14.19 ? 32  PHE A CE2 1 
ATOM   292  C CZ  . PHE A 1 32  ? -19.001 21.278 80.756  1.00 10.00 ? 32  PHE A CZ  1 
ATOM   293  N N   . HIS A 1 33  ? -14.647 18.864 75.270  1.00 7.81  ? 33  HIS A N   1 
ATOM   294  C CA  . HIS A 1 33  ? -14.194 18.753 73.889  1.00 8.69  ? 33  HIS A CA  1 
ATOM   295  C C   . HIS A 1 33  ? -14.639 17.456 73.220  1.00 9.24  ? 33  HIS A C   1 
ATOM   296  O O   . HIS A 1 33  ? -14.726 17.415 71.990  1.00 9.84  ? 33  HIS A O   1 
ATOM   297  C CB  . HIS A 1 33  ? -12.672 18.919 73.821  1.00 7.37  ? 33  HIS A CB  1 
ATOM   298  C CG  . HIS A 1 33  ? -12.244 20.338 74.006  1.00 8.74  ? 33  HIS A CG  1 
ATOM   299  N ND1 . HIS A 1 33  ? -12.498 21.317 73.066  1.00 9.03  ? 33  HIS A ND1 1 
ATOM   300  C CD2 . HIS A 1 33  ? -11.669 20.964 75.061  1.00 9.10  ? 33  HIS A CD2 1 
ATOM   301  C CE1 . HIS A 1 33  ? -12.060 22.480 73.522  1.00 10.93 ? 33  HIS A CE1 1 
ATOM   302  N NE2 . HIS A 1 33  ? -11.543 22.289 74.725  1.00 11.70 ? 33  HIS A NE2 1 
ATOM   303  N N   . ALA A 1 34  ? -14.924 16.396 73.987  1.00 8.62  ? 34  ALA A N   1 
ATOM   304  C CA  . ALA A 1 34  ? -15.528 15.206 73.381  1.00 9.12  ? 34  ALA A CA  1 
ATOM   305  C C   . ALA A 1 34  ? -16.941 15.494 72.871  1.00 10.43 ? 34  ALA A C   1 
ATOM   306  O O   . ALA A 1 34  ? -17.292 15.118 71.747  1.00 10.14 ? 34  ALA A O   1 
ATOM   307  C CB  . ALA A 1 34  ? -15.541 14.057 74.385  1.00 12.82 ? 34  ALA A CB  1 
ATOM   308  N N   . VAL A 1 35  ? -17.771 16.157 73.680  1.00 9.23  ? 35  VAL A N   1 
ATOM   309  C CA  . VAL A 1 35  ? -19.144 16.388 73.239  1.00 11.80 ? 35  VAL A CA  1 
ATOM   310  C C   . VAL A 1 35  ? -19.214 17.478 72.185  1.00 11.66 ? 35  VAL A C   1 
ATOM   311  O O   . VAL A 1 35  ? -20.157 17.489 71.379  1.00 10.98 ? 35  VAL A O   1 
ATOM   312  C CB  . VAL A 1 35  ? -20.068 16.717 74.420  1.00 11.93 ? 35  VAL A CB  1 
ATOM   313  C CG1 . VAL A 1 35  ? -19.955 15.613 75.475  1.00 11.16 ? 35  VAL A CG1 1 
ATOM   314  C CG2 . VAL A 1 35  ? -19.755 18.103 75.021  1.00 12.64 ? 35  VAL A CG2 1 
ATOM   315  N N   . LYS A 1 36  ? -18.223 18.367 72.144  1.00 12.16 ? 36  LYS A N   1 
ATOM   316  C CA  . LYS A 1 36  ? -18.253 19.477 71.201  1.00 8.91  ? 36  LYS A CA  1 
ATOM   317  C C   . LYS A 1 36  ? -17.494 19.184 69.920  1.00 14.30 ? 36  LYS A C   1 
ATOM   318  O O   . LYS A 1 36  ? -17.975 19.542 68.841  1.00 13.41 ? 36  LYS A O   1 
ATOM   319  C CB  . LYS A 1 36  ? -17.694 20.759 71.840  1.00 10.58 ? 36  LYS A CB  1 
ATOM   320  C CG  . LYS A 1 36  ? -17.994 22.019 71.005  1.00 11.22 ? 36  LYS A CG  1 
ATOM   321  C CD  . LYS A 1 36  ? -17.615 23.302 71.742  1.00 11.13 ? 36  LYS A CD  1 
ATOM   322  C CE  . LYS A 1 36  ? -16.111 23.541 71.732  1.00 10.17 ? 36  LYS A CE  1 
ATOM   323  N NZ  . LYS A 1 36  ? -15.603 23.822 70.338  1.00 11.09 ? 36  LYS A NZ  1 
ATOM   324  N N   . ASP A 1 37  ? -16.301 18.566 70.011  1.00 7.76  ? 37  ASP A N   1 
ATOM   325  C CA  . ASP A 1 37  ? -15.379 18.519 68.874  1.00 8.92  ? 37  ASP A CA  1 
ATOM   326  C C   . ASP A 1 37  ? -14.948 17.117 68.458  1.00 10.23 ? 37  ASP A C   1 
ATOM   327  O O   . ASP A 1 37  ? -14.825 16.844 67.261  1.00 10.49 ? 37  ASP A O   1 
ATOM   328  C CB  . ASP A 1 37  ? -14.119 19.343 69.190  1.00 10.52 ? 37  ASP A CB  1 
ATOM   329  C CG  . ASP A 1 37  ? -14.454 20.709 69.715  1.00 11.35 ? 37  ASP A CG  1 
ATOM   330  O OD1 . ASP A 1 37  ? -15.013 21.517 68.932  1.00 11.60 ? 37  ASP A OD1 1 
ATOM   331  O OD2 . ASP A 1 37  ? -14.216 20.958 70.919  1.00 10.47 ? 37  ASP A OD2 1 
ATOM   332  N N   . TYR A 1 38  ? -14.701 16.206 69.403  1.00 10.39 ? 38  TYR A N   1 
ATOM   333  C CA  . TYR A 1 38  ? -13.992 14.983 69.021  1.00 11.97 ? 38  TYR A CA  1 
ATOM   334  C C   . TYR A 1 38  ? -14.853 14.040 68.183  1.00 12.10 ? 38  TYR A C   1 
ATOM   335  O O   . TYR A 1 38  ? -14.317 13.271 67.380  1.00 10.50 ? 38  TYR A O   1 
ATOM   336  C CB  . TYR A 1 38  ? -13.465 14.278 70.269  1.00 8.94  ? 38  TYR A CB  1 
ATOM   337  C CG  . TYR A 1 38  ? -12.365 15.064 70.973  1.00 10.74 ? 38  TYR A CG  1 
ATOM   338  C CD1 . TYR A 1 38  ? -11.498 15.880 70.257  1.00 9.14  ? 38  TYR A CD1 1 
ATOM   339  C CD2 . TYR A 1 38  ? -12.216 15.008 72.359  1.00 11.89 ? 38  TYR A CD2 1 
ATOM   340  C CE1 . TYR A 1 38  ? -10.493 16.602 70.900  1.00 9.86  ? 38  TYR A CE1 1 
ATOM   341  C CE2 . TYR A 1 38  ? -11.221 15.720 73.006  1.00 10.42 ? 38  TYR A CE2 1 
ATOM   342  C CZ  . TYR A 1 38  ? -10.361 16.507 72.287  1.00 11.86 ? 38  TYR A CZ  1 
ATOM   343  O OH  . TYR A 1 38  ? -9.358  17.227 72.923  1.00 11.46 ? 38  TYR A OH  1 
ATOM   344  N N   . TYR A 1 39  ? -16.171 14.073 68.349  1.00 10.43 ? 39  TYR A N   1 
ATOM   345  C CA  . TYR A 1 39  ? -17.051 13.382 67.417  1.00 12.93 ? 39  TYR A CA  1 
ATOM   346  C C   . TYR A 1 39  ? -17.367 14.253 66.208  1.00 11.95 ? 39  TYR A C   1 
ATOM   347  O O   . TYR A 1 39  ? -17.401 13.767 65.073  1.00 9.08  ? 39  TYR A O   1 
ATOM   348  C CB  . TYR A 1 39  ? -18.359 12.979 68.115  1.00 9.36  ? 39  TYR A CB  1 
ATOM   349  C CG  . TYR A 1 39  ? -19.392 12.363 67.185  1.00 11.03 ? 39  TYR A CG  1 
ATOM   350  C CD1 . TYR A 1 39  ? -19.364 11.008 66.886  1.00 11.42 ? 39  TYR A CD1 1 
ATOM   351  C CD2 . TYR A 1 39  ? -20.400 13.139 66.618  1.00 12.11 ? 39  TYR A CD2 1 
ATOM   352  C CE1 . TYR A 1 39  ? -20.299 10.446 66.040  1.00 13.47 ? 39  TYR A CE1 1 
ATOM   353  C CE2 . TYR A 1 39  ? -21.347 12.583 65.763  1.00 14.02 ? 39  TYR A CE2 1 
ATOM   354  C CZ  . TYR A 1 39  ? -21.289 11.234 65.478  1.00 16.82 ? 39  TYR A CZ  1 
ATOM   355  O OH  . TYR A 1 39  ? -22.220 10.672 64.631  1.00 19.62 ? 39  TYR A OH  1 
ATOM   356  N N   . ASP A 1 40  ? -17.616 15.539 66.435  1.00 11.73 ? 40  ASP A N   1 
ATOM   357  C CA  . ASP A 1 40  ? -18.195 16.344 65.374  1.00 11.23 ? 40  ASP A CA  1 
ATOM   358  C C   . ASP A 1 40  ? -17.193 16.691 64.288  1.00 9.98  ? 40  ASP A C   1 
ATOM   359  O O   . ASP A 1 40  ? -17.600 16.883 63.136  1.00 10.72 ? 40  ASP A O   1 
ATOM   360  C CB  . ASP A 1 40  ? -18.837 17.589 65.980  1.00 8.69  ? 40  ASP A CB  1 
ATOM   361  C CG  . ASP A 1 40  ? -20.252 17.292 66.468  1.00 12.34 ? 40  ASP A CG  1 
ATOM   362  O OD1 . ASP A 1 40  ? -21.121 17.057 65.601  1.00 12.86 ? 40  ASP A OD1 1 
ATOM   363  O OD2 . ASP A 1 40  ? -20.478 17.227 67.701  1.00 14.72 ? 40  ASP A OD2 1 
ATOM   364  N N   . MET A 1 41  ? -15.894 16.799 64.616  1.00 9.83  ? 41  MET A N   1 
ATOM   365  C CA  . MET A 1 41  ? -14.941 17.143 63.561  1.00 8.84  ? 41  MET A CA  1 
ATOM   366  C C   . MET A 1 41  ? -14.864 16.043 62.505  1.00 10.64 ? 41  MET A C   1 
ATOM   367  O O   . MET A 1 41  ? -15.053 16.348 61.313  1.00 11.36 ? 41  MET A O   1 
ATOM   368  C CB  . MET A 1 41  ? -13.577 17.494 64.175  1.00 9.00  ? 41  MET A CB  1 
ATOM   369  C CG  . MET A 1 41  ? -13.563 18.905 64.816  1.00 9.24  ? 41  MET A CG  1 
ATOM   370  S SD  . MET A 1 41  ? -13.556 20.196 63.562  1.00 10.14 ? 41  MET A SD  1 
ATOM   371  C CE  . MET A 1 41  ? -11.846 20.078 63.006  1.00 10.99 ? 41  MET A CE  1 
ATOM   372  N N   . PRO A 1 42  ? -14.623 14.771 62.842  1.00 11.57 ? 42  PRO A N   1 
ATOM   373  C CA  . PRO A 1 42  ? -14.767 13.727 61.806  1.00 9.02  ? 42  PRO A CA  1 
ATOM   374  C C   . PRO A 1 42  ? -16.183 13.603 61.256  1.00 9.41  ? 42  PRO A C   1 
ATOM   375  O O   . PRO A 1 42  ? -16.362 13.197 60.097  1.00 12.07 ? 42  PRO A O   1 
ATOM   376  C CB  . PRO A 1 42  ? -14.337 12.442 62.537  1.00 12.07 ? 42  PRO A CB  1 
ATOM   377  C CG  . PRO A 1 42  ? -14.546 12.758 64.033  1.00 10.17 ? 42  PRO A CG  1 
ATOM   378  C CD  . PRO A 1 42  ? -14.144 14.218 64.126  1.00 10.84 ? 42  PRO A CD  1 
ATOM   379  N N   . ALA A 1 43  ? -17.203 13.943 62.034  1.00 11.29 ? 43  ALA A N   1 
ATOM   380  C CA  . ALA A 1 43  ? -18.563 13.755 61.526  1.00 13.50 ? 43  ALA A CA  1 
ATOM   381  C C   . ALA A 1 43  ? -18.888 14.682 60.358  1.00 14.37 ? 43  ALA A C   1 
ATOM   382  O O   . ALA A 1 43  ? -19.836 14.407 59.622  1.00 13.45 ? 43  ALA A O   1 
ATOM   383  C CB  . ALA A 1 43  ? -19.585 13.938 62.643  1.00 12.98 ? 43  ALA A CB  1 
ATOM   384  N N   . TYR A 1 44  ? -18.119 15.757 60.157  1.00 10.07 ? 44  TYR A N   1 
ATOM   385  C CA  . TYR A 1 44  ? -18.301 16.557 58.946  1.00 10.86 ? 44  TYR A CA  1 
ATOM   386  C C   . TYR A 1 44  ? -18.152 15.704 57.697  1.00 12.40 ? 44  TYR A C   1 
ATOM   387  O O   . TYR A 1 44  ? -18.764 15.996 56.662  1.00 14.21 ? 44  TYR A O   1 
ATOM   388  C CB  . TYR A 1 44  ? -17.276 17.688 58.893  1.00 9.79  ? 44  TYR A CB  1 
ATOM   389  C CG  . TYR A 1 44  ? -17.645 18.945 59.658  1.00 9.65  ? 44  TYR A CG  1 
ATOM   390  C CD1 . TYR A 1 44  ? -18.386 19.958 59.051  1.00 11.12 ? 44  TYR A CD1 1 
ATOM   391  C CD2 . TYR A 1 44  ? -17.223 19.131 60.972  1.00 10.41 ? 44  TYR A CD2 1 
ATOM   392  C CE1 . TYR A 1 44  ? -18.685 21.121 59.738  1.00 10.96 ? 44  TYR A CE1 1 
ATOM   393  C CE2 . TYR A 1 44  ? -17.529 20.285 61.667  1.00 13.61 ? 44  TYR A CE2 1 
ATOM   394  C CZ  . TYR A 1 44  ? -18.251 21.274 61.046  1.00 13.62 ? 44  TYR A CZ  1 
ATOM   395  O OH  . TYR A 1 44  ? -18.562 22.421 61.740  1.00 13.77 ? 44  TYR A OH  1 
ATOM   396  N N   . LEU A 1 45  ? -17.345 14.639 57.779  1.00 10.38 ? 45  LEU A N   1 
ATOM   397  C CA  . LEU A 1 45  ? -17.136 13.771 56.624  1.00 11.80 ? 45  LEU A CA  1 
ATOM   398  C C   . LEU A 1 45  ? -18.389 13.002 56.222  1.00 15.37 ? 45  LEU A C   1 
ATOM   399  O O   . LEU A 1 45  ? -18.439 12.459 55.109  1.00 16.93 ? 45  LEU A O   1 
ATOM   400  C CB  . LEU A 1 45  ? -16.003 12.799 56.931  1.00 10.60 ? 45  LEU A CB  1 
ATOM   401  C CG  . LEU A 1 45  ? -14.627 13.443 57.064  1.00 10.17 ? 45  LEU A CG  1 
ATOM   402  C CD1 . LEU A 1 45  ? -13.666 12.423 57.666  1.00 11.40 ? 45  LEU A CD1 1 
ATOM   403  C CD2 . LEU A 1 45  ? -14.171 13.918 55.676  1.00 14.18 ? 45  LEU A CD2 1 
ATOM   404  N N   . LYS A 1 46  ? -19.399 12.933 57.093  1.00 16.57 ? 46  LYS A N   1 
ATOM   405  C CA  . LYS A 1 46  ? -20.680 12.350 56.710  1.00 18.33 ? 46  LYS A CA  1 
ATOM   406  C C   . LYS A 1 46  ? -21.434 13.237 55.730  1.00 21.94 ? 46  LYS A C   1 
ATOM   407  O O   . LYS A 1 46  ? -22.302 12.747 54.999  1.00 22.39 ? 46  LYS A O   1 
ATOM   408  C CB  . LYS A 1 46  ? -21.550 12.114 57.953  1.00 17.81 ? 46  LYS A CB  1 
ATOM   409  C CG  . LYS A 1 46  ? -21.097 10.961 58.833  1.00 28.47 ? 46  LYS A CG  1 
ATOM   410  C CD  . LYS A 1 46  ? -21.817 10.964 60.178  1.00 36.49 ? 46  LYS A CD  1 
ATOM   411  C CE  . LYS A 1 46  ? -22.565 9.655  60.424  1.00 49.57 ? 46  LYS A CE  1 
ATOM   412  N NZ  . LYS A 1 46  ? -21.795 8.454  59.980  1.00 56.26 ? 46  LYS A NZ  1 
ATOM   413  N N   . ASP A 1 47  ? -21.120 14.534 55.700  1.00 16.74 ? 47  ASP A N   1 
ATOM   414  C CA  . ASP A 1 47  ? -21.894 15.499 54.937  1.00 18.16 ? 47  ASP A CA  1 
ATOM   415  C C   . ASP A 1 47  ? -21.138 16.113 53.773  1.00 18.29 ? 47  ASP A C   1 
ATOM   416  O O   . ASP A 1 47  ? -21.774 16.659 52.869  1.00 19.07 ? 47  ASP A O   1 
ATOM   417  C CB  . ASP A 1 47  ? -22.375 16.627 55.860  1.00 18.16 ? 47  ASP A CB  1 
ATOM   418  C CG  . ASP A 1 47  ? -23.356 16.135 56.907  1.00 25.62 ? 47  ASP A CG  1 
ATOM   419  O OD1 . ASP A 1 47  ? -24.148 15.211 56.595  1.00 24.66 ? 47  ASP A OD1 1 
ATOM   420  O OD2 . ASP A 1 47  ? -23.332 16.675 58.033  1.00 30.73 ? 47  ASP A OD2 1 
ATOM   421  N N   . PHE A 1 48  ? -19.811 16.032 53.767  1.00 15.89 ? 48  PHE A N   1 
ATOM   422  C CA  . PHE A 1 48  ? -18.984 16.671 52.753  1.00 16.39 ? 48  PHE A CA  1 
ATOM   423  C C   . PHE A 1 48  ? -18.025 15.644 52.175  1.00 16.25 ? 48  PHE A C   1 
ATOM   424  O O   . PHE A 1 48  ? -17.379 14.913 52.926  1.00 15.47 ? 48  PHE A O   1 
ATOM   425  C CB  . PHE A 1 48  ? -18.225 17.862 53.358  1.00 13.99 ? 48  PHE A CB  1 
ATOM   426  C CG  . PHE A 1 48  ? -19.138 18.934 53.888  1.00 16.74 ? 48  PHE A CG  1 
ATOM   427  C CD1 . PHE A 1 48  ? -19.732 19.839 53.026  1.00 19.88 ? 48  PHE A CD1 1 
ATOM   428  C CD2 . PHE A 1 48  ? -19.460 18.993 55.238  1.00 14.74 ? 48  PHE A CD2 1 
ATOM   429  C CE1 . PHE A 1 48  ? -20.608 20.811 53.508  1.00 16.94 ? 48  PHE A CE1 1 
ATOM   430  C CE2 . PHE A 1 48  ? -20.319 19.967 55.726  1.00 18.43 ? 48  PHE A CE2 1 
ATOM   431  C CZ  . PHE A 1 48  ? -20.893 20.880 54.862  1.00 14.70 ? 48  PHE A CZ  1 
ATOM   432  N N   . GLU A 1 49  ? -17.954 15.578 50.847  1.00 16.63 ? 49  GLU A N   1 
ATOM   433  C CA  . GLU A 1 49  ? -17.178 14.545 50.165  1.00 21.73 ? 49  GLU A CA  1 
ATOM   434  C C   . GLU A 1 49  ? -15.764 15.068 49.927  1.00 18.60 ? 49  GLU A C   1 
ATOM   435  O O   . GLU A 1 49  ? -15.333 15.336 48.807  1.00 22.81 ? 49  GLU A O   1 
ATOM   436  C CB  . GLU A 1 49  ? -17.857 14.131 48.867  1.00 24.95 ? 49  GLU A CB  1 
ATOM   437  C CG  . GLU A 1 49  ? -18.985 13.127 49.059  1.00 43.24 ? 49  GLU A CG  1 
ATOM   438  C CD  . GLU A 1 49  ? -18.484 11.760 49.493  1.00 59.04 ? 49  GLU A CD  1 
ATOM   439  O OE1 . GLU A 1 49  ? -17.467 11.294 48.935  1.00 63.29 ? 49  GLU A OE1 1 
ATOM   440  O OE2 . GLU A 1 49  ? -19.107 11.153 50.392  1.00 64.57 ? 49  GLU A OE2 1 
ATOM   441  N N   . ILE A 1 50  ? -15.051 15.242 51.035  1.00 14.46 ? 50  ILE A N   1 
ATOM   442  C CA  . ILE A 1 50  ? -13.645 15.612 51.043  1.00 12.57 ? 50  ILE A CA  1 
ATOM   443  C C   . ILE A 1 50  ? -12.909 14.614 51.927  1.00 15.27 ? 50  ILE A C   1 
ATOM   444  O O   . ILE A 1 50  ? -13.520 13.733 52.532  1.00 17.60 ? 50  ILE A O   1 
ATOM   445  C CB  . ILE A 1 50  ? -13.437 17.044 51.550  1.00 13.10 ? 50  ILE A CB  1 
ATOM   446  C CG1 . ILE A 1 50  ? -13.921 17.118 53.003  1.00 17.28 ? 50  ILE A CG1 1 
ATOM   447  C CG2 . ILE A 1 50  ? -14.205 18.009 50.658  1.00 14.87 ? 50  ILE A CG2 1 
ATOM   448  C CD1 . ILE A 1 50  ? -13.881 18.484 53.601  1.00 24.21 ? 50  ILE A CD1 1 
ATOM   449  N N   . LYS A 1 51  ? -11.588 14.740 51.980  1.00 11.88 ? 51  LYS A N   1 
ATOM   450  C CA  . LYS A 1 51  ? -10.772 13.952 52.898  1.00 11.59 ? 51  LYS A CA  1 
ATOM   451  C C   . LYS A 1 51  ? -10.304 14.838 54.044  1.00 11.99 ? 51  LYS A C   1 
ATOM   452  O O   . LYS A 1 51  ? -9.837  15.960 53.818  1.00 12.31 ? 51  LYS A O   1 
ATOM   453  C CB  . LYS A 1 51  ? -9.544  13.353 52.195  1.00 14.10 ? 51  LYS A CB  1 
ATOM   454  C CG  . LYS A 1 51  ? -9.839  12.652 50.866  1.00 13.41 ? 51  LYS A CG  1 
ATOM   455  C CD  . LYS A 1 51  ? -10.766 11.468 51.063  1.00 14.42 ? 51  LYS A CD  1 
ATOM   456  C CE  . LYS A 1 51  ? -10.764 10.604 49.801  1.00 21.26 ? 51  LYS A CE  1 
ATOM   457  N NZ  . LYS A 1 51  ? -11.689 9.460  49.993  1.00 30.74 ? 51  LYS A NZ  1 
ATOM   458  N N   . LEU A 1 52  ? -10.377 14.305 55.267  1.00 10.96 ? 52  LEU A N   1 
ATOM   459  C CA  . LEU A 1 52  ? -9.888  14.976 56.463  1.00 10.89 ? 52  LEU A CA  1 
ATOM   460  C C   . LEU A 1 52  ? -9.171  13.956 57.336  1.00 10.27 ? 52  LEU A C   1 
ATOM   461  O O   . LEU A 1 52  ? -9.708  12.875 57.573  1.00 12.83 ? 52  LEU A O   1 
ATOM   462  C CB  . LEU A 1 52  ? -11.035 15.599 57.252  1.00 12.66 ? 52  LEU A CB  1 
ATOM   463  C CG  . LEU A 1 52  ? -11.856 16.703 56.588  1.00 13.68 ? 52  LEU A CG  1 
ATOM   464  C CD1 . LEU A 1 52  ? -12.992 17.073 57.520  1.00 12.86 ? 52  LEU A CD1 1 
ATOM   465  C CD2 . LEU A 1 52  ? -10.983 17.922 56.294  1.00 9.89  ? 52  LEU A CD2 1 
ATOM   466  N N   . ASN A 1 53  ? -7.977  14.301 57.827  1.00 9.09  ? 53  ASN A N   1 
ATOM   467  C CA  . ASN A 1 53  ? -7.189  13.399 58.659  1.00 10.41 ? 53  ASN A CA  1 
ATOM   468  C C   . ASN A 1 53  ? -7.177  13.862 60.110  1.00 10.99 ? 53  ASN A C   1 
ATOM   469  O O   . ASN A 1 53  ? -7.387  15.041 60.404  1.00 10.03 ? 53  ASN A O   1 
ATOM   470  C CB  . ASN A 1 53  ? -5.768  13.295 58.114  1.00 10.88 ? 53  ASN A CB  1 
ATOM   471  C CG  . ASN A 1 53  ? -5.779  12.966 56.655  1.00 9.53  ? 53  ASN A CG  1 
ATOM   472  O OD1 . ASN A 1 53  ? -6.105  11.846 56.280  1.00 10.49 ? 53  ASN A OD1 1 
ATOM   473  N ND2 . ASN A 1 53  ? -5.538  13.956 55.820  1.00 10.35 ? 53  ASN A ND2 1 
ATOM   474  N N   . PHE A 1 54  ? -6.918  12.909 61.019  1.00 8.67  ? 54  PHE A N   1 
ATOM   475  C CA  . PHE A 1 54  ? -7.000  13.162 62.456  1.00 8.41  ? 54  PHE A CA  1 
ATOM   476  C C   . PHE A 1 54  ? -5.845  12.508 63.189  1.00 10.54 ? 54  PHE A C   1 
ATOM   477  O O   . PHE A 1 54  ? -5.407  11.415 62.832  1.00 10.63 ? 54  PHE A O   1 
ATOM   478  C CB  . PHE A 1 54  ? -8.353  12.658 63.005  1.00 8.45  ? 54  PHE A CB  1 
ATOM   479  C CG  . PHE A 1 54  ? -9.506  13.387 62.399  1.00 8.58  ? 54  PHE A CG  1 
ATOM   480  C CD1 . PHE A 1 54  ? -9.961  14.557 62.966  1.00 14.19 ? 54  PHE A CD1 1 
ATOM   481  C CD2 . PHE A 1 54  ? -10.060 12.946 61.198  1.00 12.23 ? 54  PHE A CD2 1 
ATOM   482  C CE1 . PHE A 1 54  ? -10.991 15.271 62.385  1.00 13.26 ? 54  PHE A CE1 1 
ATOM   483  C CE2 . PHE A 1 54  ? -11.090 13.639 60.607  1.00 13.62 ? 54  PHE A CE2 1 
ATOM   484  C CZ  . PHE A 1 54  ? -11.564 14.809 61.206  1.00 12.01 ? 54  PHE A CZ  1 
ATOM   485  N N   . ASN A 1 55  ? -5.349  13.190 64.209  1.00 11.10 ? 55  ASN A N   1 
ATOM   486  C CA  . ASN A 1 55  ? -4.438  12.591 65.169  1.00 9.00  ? 55  ASN A CA  1 
ATOM   487  C C   . ASN A 1 55  ? -5.162  12.479 66.493  1.00 10.08 ? 55  ASN A C   1 
ATOM   488  O O   . ASN A 1 55  ? -5.769  13.449 66.936  1.00 11.94 ? 55  ASN A O   1 
ATOM   489  C CB  . ASN A 1 55  ? -3.190  13.442 65.363  1.00 9.59  ? 55  ASN A CB  1 
ATOM   490  C CG  . ASN A 1 55  ? -2.169  12.757 66.234  1.00 10.30 ? 55  ASN A CG  1 
ATOM   491  O OD1 . ASN A 1 55  ? -1.664  11.711 65.865  1.00 10.06 ? 55  ASN A OD1 1 
ATOM   492  N ND2 . ASN A 1 55  ? -1.862  13.339 67.394  1.00 10.82 ? 55  ASN A ND2 1 
ATOM   493  N N   . LEU A 1 56  ? -5.064  11.311 67.125  1.00 10.15 ? 56  LEU A N   1 
ATOM   494  C CA  . LEU A 1 56  ? -5.638  11.063 68.445  1.00 11.49 ? 56  LEU A CA  1 
ATOM   495  C C   . LEU A 1 56  ? -4.505  10.646 69.368  1.00 10.83 ? 56  LEU A C   1 
ATOM   496  O O   . LEU A 1 56  ? -3.849  9.629  69.119  1.00 13.64 ? 56  LEU A O   1 
ATOM   497  C CB  . LEU A 1 56  ? -6.696  9.950  68.402  1.00 10.99 ? 56  LEU A CB  1 
ATOM   498  C CG  . LEU A 1 56  ? -7.949  10.219 67.570  1.00 13.17 ? 56  LEU A CG  1 
ATOM   499  C CD1 . LEU A 1 56  ? -8.837  8.961  67.510  1.00 13.82 ? 56  LEU A CD1 1 
ATOM   500  C CD2 . LEU A 1 56  ? -8.731  11.436 68.091  1.00 15.10 ? 56  LEU A CD2 1 
ATOM   501  N N   . THR A 1 57  ? -4.280  11.409 70.439  1.00 9.43  ? 57  THR A N   1 
ATOM   502  C CA  . THR A 1 57  ? -3.242  10.896 71.321  1.00 8.86  ? 57  THR A CA  1 
ATOM   503  C C   . THR A 1 57  ? -3.771  9.739  72.167  1.00 11.42 ? 57  THR A C   1 
ATOM   504  O O   . THR A 1 57  ? -4.972  9.658  72.458  1.00 9.06  ? 57  THR A O   1 
ATOM   505  C CB  . THR A 1 57  ? -2.705  11.995 72.243  1.00 10.65 ? 57  THR A CB  1 
ATOM   506  O OG1 . THR A 1 57  ? -3.748  12.418 73.131  1.00 10.89 ? 57  THR A OG1 1 
ATOM   507  C CG2 . THR A 1 57  ? -2.181  13.189 71.402  1.00 8.52  ? 57  THR A CG2 1 
ATOM   508  N N   . PRO A 1 58  ? -2.895  8.805  72.541  1.00 9.61  ? 58  PRO A N   1 
ATOM   509  C CA  . PRO A 1 58  ? -3.372  7.652  73.307  1.00 10.01 ? 58  PRO A CA  1 
ATOM   510  C C   . PRO A 1 58  ? -3.963  8.056  74.640  1.00 9.92  ? 58  PRO A C   1 
ATOM   511  O O   . PRO A 1 58  ? -4.978  7.488  75.070  1.00 12.28 ? 58  PRO A O   1 
ATOM   512  C CB  . PRO A 1 58  ? -2.111  6.783  73.450  1.00 10.55 ? 58  PRO A CB  1 
ATOM   513  C CG  . PRO A 1 58  ? -1.267  7.152  72.250  1.00 10.59 ? 58  PRO A CG  1 
ATOM   514  C CD  . PRO A 1 58  ? -1.489  8.655  72.117  1.00 9.86  ? 58  PRO A CD  1 
ATOM   515  N N   . VAL A 1 59  ? -3.382  9.066  75.293  1.00 9.75  ? 59  VAL A N   1 
ATOM   516  C CA  . VAL A 1 59  ? -3.931  9.463  76.584  1.00 12.54 ? 59  VAL A CA  1 
ATOM   517  C C   . VAL A 1 59  ? -5.325  10.073 76.404  1.00 10.08 ? 59  VAL A C   1 
ATOM   518  O O   . VAL A 1 59  ? -6.207  9.873  77.250  1.00 10.45 ? 59  VAL A O   1 
ATOM   519  C CB  . VAL A 1 59  ? -2.943  10.395 77.322  1.00 9.74  ? 59  VAL A CB  1 
ATOM   520  C CG1 . VAL A 1 59  ? -2.573  11.640 76.478  1.00 9.34  ? 59  VAL A CG1 1 
ATOM   521  C CG2 . VAL A 1 59  ? -3.484  10.798 78.703  1.00 13.70 ? 59  VAL A CG2 1 
ATOM   522  N N   . LEU A 1 60  ? -5.572  10.785 75.294  1.00 9.15  ? 60  LEU A N   1 
ATOM   523  C CA  . LEU A 1 60  ? -6.943  11.217 75.015  1.00 8.81  ? 60  LEU A CA  1 
ATOM   524  C C   . LEU A 1 60  ? -7.859  10.022 74.780  1.00 11.24 ? 60  LEU A C   1 
ATOM   525  O O   . LEU A 1 60  ? -8.981  9.976  75.302  1.00 11.05 ? 60  LEU A O   1 
ATOM   526  C CB  . LEU A 1 60  ? -6.986  12.148 73.798  1.00 9.31  ? 60  LEU A CB  1 
ATOM   527  C CG  . LEU A 1 60  ? -8.414  12.489 73.350  1.00 9.35  ? 60  LEU A CG  1 
ATOM   528  C CD1 . LEU A 1 60  ? -9.188  13.205 74.475  1.00 11.65 ? 60  LEU A CD1 1 
ATOM   529  C CD2 . LEU A 1 60  ? -8.374  13.350 72.083  1.00 10.02 ? 60  LEU A CD2 1 
ATOM   530  N N   . ILE A 1 61  ? -7.401  9.038  74.000  1.00 10.45 ? 61  ILE A N   1 
ATOM   531  C CA  . ILE A 1 61  ? -8.230  7.856  73.754  1.00 13.10 ? 61  ILE A CA  1 
ATOM   532  C C   . ILE A 1 61  ? -8.613  7.173  75.060  1.00 11.05 ? 61  ILE A C   1 
ATOM   533  O O   . ILE A 1 61  ? -9.769  6.777  75.247  1.00 10.89 ? 61  ILE A O   1 
ATOM   534  C CB  . ILE A 1 61  ? -7.521  6.875  72.814  1.00 10.78 ? 61  ILE A CB  1 
ATOM   535  C CG1 . ILE A 1 61  ? -7.348  7.506  71.434  1.00 10.38 ? 61  ILE A CG1 1 
ATOM   536  C CG2 . ILE A 1 61  ? -8.332  5.574  72.696  1.00 13.10 ? 61  ILE A CG2 1 
ATOM   537  C CD1 . ILE A 1 61  ? -6.505  6.591  70.522  1.00 9.90  ? 61  ILE A CD1 1 
ATOM   538  N N   . ASP A 1 62  ? -7.652  7.014  75.977  1.00 10.09 ? 62  ASP A N   1 
ATOM   539  C CA  . ASP A 1 62  ? -7.955  6.404  77.277  1.00 12.54 ? 62  ASP A CA  1 
ATOM   540  C C   . ASP A 1 62  ? -9.126  7.107  77.953  1.00 14.40 ? 62  ASP A C   1 
ATOM   541  O O   . ASP A 1 62  ? -10.019 6.467  78.520  1.00 12.90 ? 62  ASP A O   1 
ATOM   542  C CB  . ASP A 1 62  ? -6.736  6.475  78.198  1.00 12.81 ? 62  ASP A CB  1 
ATOM   543  C CG  . ASP A 1 62  ? -5.708  5.429  77.894  1.00 19.21 ? 62  ASP A CG  1 
ATOM   544  O OD1 . ASP A 1 62  ? -6.075  4.400  77.302  1.00 18.39 ? 62  ASP A OD1 1 
ATOM   545  O OD2 . ASP A 1 62  ? -4.519  5.629  78.268  1.00 15.14 ? 62  ASP A OD2 1 
ATOM   546  N N   . GLN A 1 63  ? -9.110  8.440  77.941  1.00 9.75  ? 63  GLN A N   1 
ATOM   547  C CA  . GLN A 1 63  ? -10.135 9.188  78.658  1.00 10.15 ? 63  GLN A CA  1 
ATOM   548  C C   . GLN A 1 63  ? -11.477 9.104  77.950  1.00 9.59  ? 63  GLN A C   1 
ATOM   549  O O   . GLN A 1 63  ? -12.518 9.002  78.599  1.00 13.26 ? 63  GLN A O   1 
ATOM   550  C CB  . GLN A 1 63  ? -9.708  10.643 78.820  1.00 12.71 ? 63  GLN A CB  1 
ATOM   551  C CG  . GLN A 1 63  ? -8.362  10.806 79.519  1.00 11.74 ? 63  GLN A CG  1 
ATOM   552  C CD  . GLN A 1 63  ? -7.930  12.258 79.556  1.00 12.24 ? 63  GLN A CD  1 
ATOM   553  O OE1 . GLN A 1 63  ? -8.585  13.087 80.194  1.00 14.04 ? 63  GLN A OE1 1 
ATOM   554  N NE2 . GLN A 1 63  ? -6.836  12.586 78.854  1.00 10.52 ? 63  GLN A NE2 1 
ATOM   555  N N   . ILE A 1 64  ? -11.477 9.168  76.618  1.00 10.85 ? 64  ILE A N   1 
ATOM   556  C CA  . ILE A 1 64  ? -12.729 9.038  75.882  1.00 11.21 ? 64  ILE A CA  1 
ATOM   557  C C   . ILE A 1 64  ? -13.373 7.706  76.214  1.00 14.08 ? 64  ILE A C   1 
ATOM   558  O O   . ILE A 1 64  ? -14.589 7.623  76.446  1.00 12.28 ? 64  ILE A O   1 
ATOM   559  C CB  . ILE A 1 64  ? -12.476 9.189  74.367  1.00 11.17 ? 64  ILE A CB  1 
ATOM   560  C CG1 . ILE A 1 64  ? -12.091 10.627 74.024  1.00 9.79  ? 64  ILE A CG1 1 
ATOM   561  C CG2 . ILE A 1 64  ? -13.713 8.797  73.580  1.00 12.22 ? 64  ILE A CG2 1 
ATOM   562  C CD1 . ILE A 1 64  ? -11.764 10.848 72.546  1.00 13.66 ? 64  ILE A CD1 1 
ATOM   563  N N   . GLN A 1 65  ? -12.554 6.658  76.317  1.00 13.55 ? 65  GLN A N   1 
ATOM   564  C CA  . GLN A 1 65  ? -13.068 5.339  76.663  1.00 10.85 ? 65  GLN A CA  1 
ATOM   565  C C   . GLN A 1 65  ? -13.654 5.329  78.070  1.00 11.08 ? 65  GLN A C   1 
ATOM   566  O O   . GLN A 1 65  ? -14.716 4.740  78.303  1.00 14.27 ? 65  GLN A O   1 
ATOM   567  C CB  . GLN A 1 65  ? -11.951 4.298  76.563  1.00 11.28 ? 65  GLN A CB  1 
ATOM   568  C CG  . GLN A 1 65  ? -11.538 3.992  75.149  1.00 11.57 ? 65  GLN A CG  1 
ATOM   569  C CD  . GLN A 1 65  ? -10.456 2.960  75.123  1.00 18.21 ? 65  GLN A CD  1 
ATOM   570  O OE1 . GLN A 1 65  ? -9.358  3.207  75.598  1.00 22.08 ? 65  GLN A OE1 1 
ATOM   571  N NE2 . GLN A 1 65  ? -10.767 1.775  74.602  1.00 23.85 ? 65  GLN A NE2 1 
ATOM   572  N N   . GLU A 1 66  ? -12.976 5.985  79.022  1.00 10.93 ? 66  GLU A N   1 
ATOM   573  C CA  . GLU A 1 66  ? -13.465 5.961  80.400  1.00 12.35 ? 66  GLU A CA  1 
ATOM   574  C C   . GLU A 1 66  ? -14.800 6.690  80.516  1.00 14.52 ? 66  GLU A C   1 
ATOM   575  O O   . GLU A 1 66  ? -15.698 6.243  81.236  1.00 13.41 ? 66  GLU A O   1 
ATOM   576  C CB  . GLU A 1 66  ? -12.420 6.563  81.348  1.00 12.32 ? 66  GLU A CB  1 
ATOM   577  C CG  . GLU A 1 66  ? -12.715 6.270  82.827  1.00 22.97 ? 66  GLU A CG  1 
ATOM   578  C CD  . GLU A 1 66  ? -11.576 6.657  83.768  1.00 24.50 ? 66  GLU A CD  1 
ATOM   579  O OE1 . GLU A 1 66  ? -11.771 6.569  85.007  1.00 26.30 ? 66  GLU A OE1 1 
ATOM   580  O OE2 . GLU A 1 66  ? -10.489 7.035  83.274  1.00 18.32 ? 66  GLU A OE2 1 
ATOM   581  N N   . TYR A 1 67  ? -14.962 7.799  79.799  1.00 11.53 ? 67  TYR A N   1 
ATOM   582  C CA  . TYR A 1 67  ? -16.256 8.472  79.788  1.00 12.67 ? 67  TYR A CA  1 
ATOM   583  C C   . TYR A 1 67  ? -17.320 7.630  79.101  1.00 13.48 ? 67  TYR A C   1 
ATOM   584  O O   . TYR A 1 67  ? -18.461 7.555  79.571  1.00 14.79 ? 67  TYR A O   1 
ATOM   585  C CB  . TYR A 1 67  ? -16.146 9.826  79.075  1.00 10.95 ? 67  TYR A CB  1 
ATOM   586  C CG  . TYR A 1 67  ? -15.635 10.957 79.949  1.00 11.87 ? 67  TYR A CG  1 
ATOM   587  C CD1 . TYR A 1 67  ? -16.503 11.699 80.763  1.00 10.95 ? 67  TYR A CD1 1 
ATOM   588  C CD2 . TYR A 1 67  ? -14.281 11.285 79.963  1.00 9.18  ? 67  TYR A CD2 1 
ATOM   589  C CE1 . TYR A 1 67  ? -16.023 12.733 81.579  1.00 10.62 ? 67  TYR A CE1 1 
ATOM   590  C CE2 . TYR A 1 67  ? -13.800 12.311 80.757  1.00 14.40 ? 67  TYR A CE2 1 
ATOM   591  C CZ  . TYR A 1 67  ? -14.668 13.041 81.552  1.00 12.43 ? 67  TYR A CZ  1 
ATOM   592  O OH  . TYR A 1 67  ? -14.149 14.059 82.329  1.00 14.07 ? 67  TYR A OH  1 
ATOM   593  N N   . ALA A 1 68  ? -16.978 7.042  77.948  1.00 10.87 ? 68  ALA A N   1 
ATOM   594  C CA  . ALA A 1 68  ? -17.932 6.227  77.201  1.00 13.74 ? 68  ALA A CA  1 
ATOM   595  C C   . ALA A 1 68  ? -18.416 5.043  78.019  1.00 16.35 ? 68  ALA A C   1 
ATOM   596  O O   . ALA A 1 68  ? -19.575 4.615  77.890  1.00 17.84 ? 68  ALA A O   1 
ATOM   597  C CB  . ALA A 1 68  ? -17.277 5.739  75.910  1.00 14.68 ? 68  ALA A CB  1 
ATOM   598  N N   . GLN A 1 69  ? -17.551 4.504  78.874  1.00 14.60 ? 69  GLN A N   1 
ATOM   599  C CA  . GLN A 1 69  ? -17.917 3.367  79.700  1.00 16.80 ? 69  GLN A CA  1 
ATOM   600  C C   . GLN A 1 69  ? -18.640 3.766  80.981  1.00 19.01 ? 69  GLN A C   1 
ATOM   601  O O   . GLN A 1 69  ? -18.988 2.882  81.774  1.00 22.85 ? 69  GLN A O   1 
ATOM   602  C CB  . GLN A 1 69  ? -16.671 2.544  80.042  1.00 21.27 ? 69  GLN A CB  1 
ATOM   603  C CG  . GLN A 1 69  ? -16.063 1.861  78.837  1.00 23.53 ? 69  GLN A CG  1 
ATOM   604  C CD  . GLN A 1 69  ? -14.658 1.352  79.091  1.00 37.43 ? 69  GLN A CD  1 
ATOM   605  O OE1 . GLN A 1 69  ? -14.170 1.379  80.220  1.00 41.25 ? 69  GLN A OE1 1 
ATOM   606  N NE2 . GLN A 1 69  ? -13.996 0.889  78.035  1.00 31.94 ? 69  GLN A NE2 1 
ATOM   607  N N   . GLY A 1 70  ? -18.870 5.056  81.202  1.00 17.77 ? 70  GLY A N   1 
ATOM   608  C CA  . GLY A 1 70  ? -19.513 5.518  82.413  1.00 21.10 ? 70  GLY A CA  1 
ATOM   609  C C   . GLY A 1 70  ? -18.655 5.460  83.648  1.00 24.00 ? 70  GLY A C   1 
ATOM   610  O O   . GLY A 1 70  ? -19.191 5.488  84.758  1.00 28.51 ? 70  GLY A O   1 
ATOM   611  N N   . LYS A 1 71  ? -17.330 5.372  83.494  1.00 24.31 ? 71  LYS A N   1 
ATOM   612  C CA  . LYS A 1 71  ? -16.430 5.210  84.628  1.00 23.09 ? 71  LYS A CA  1 
ATOM   613  C C   . LYS A 1 71  ? -15.731 6.499  85.044  1.00 24.35 ? 71  LYS A C   1 
ATOM   614  O O   . LYS A 1 71  ? -15.067 6.512  86.082  1.00 26.72 ? 71  LYS A O   1 
ATOM   615  C CB  . LYS A 1 71  ? -15.360 4.160  84.316  1.00 20.07 ? 71  LYS A CB  1 
ATOM   616  C CG  . LYS A 1 71  ? -15.881 2.744  84.083  1.00 28.81 ? 71  LYS A CG  1 
ATOM   617  C CD  . LYS A 1 71  ? -14.752 1.858  83.564  1.00 35.56 ? 71  LYS A CD  1 
ATOM   618  C CE  . LYS A 1 71  ? -15.209 0.424  83.330  1.00 43.69 ? 71  LYS A CE  1 
ATOM   619  N NZ  . LYS A 1 71  ? -14.125 -0.395 82.709  1.00 44.23 ? 71  LYS A NZ  1 
ATOM   620  N N   . ALA A 1 72  ? -15.845 7.569  84.265  1.00 16.79 ? 72  ALA A N   1 
ATOM   621  C CA  . ALA A 1 72  ? -15.142 8.811  84.568  1.00 16.52 ? 72  ALA A CA  1 
ATOM   622  C C   . ALA A 1 72  ? -15.868 9.571  85.672  1.00 22.86 ? 72  ALA A C   1 
ATOM   623  O O   . ALA A 1 72  ? -17.026 9.967  85.499  1.00 23.02 ? 72  ALA A O   1 
ATOM   624  C CB  . ALA A 1 72  ? -15.038 9.681  83.318  1.00 16.33 ? 72  ALA A CB  1 
ATOM   625  N N   . LYS A 1 73  ? -15.188 9.778  86.803  1.00 14.95 ? 73  LYS A N   1 
ATOM   626  C CA  . LYS A 1 73  ? -15.739 10.556 87.914  1.00 12.42 ? 73  LYS A CA  1 
ATOM   627  C C   . LYS A 1 73  ? -15.282 12.003 87.730  1.00 16.45 ? 73  LYS A C   1 
ATOM   628  O O   . LYS A 1 73  ? -14.205 12.407 88.181  1.00 17.95 ? 73  LYS A O   1 
ATOM   629  C CB  . LYS A 1 73  ? -15.286 9.978  89.252  1.00 18.19 ? 73  LYS A CB  1 
ATOM   630  C CG  . LYS A 1 73  ? -16.073 10.497 90.438  1.00 37.59 ? 73  LYS A CG  1 
ATOM   631  C CD  . LYS A 1 73  ? -17.569 10.388 90.175  1.00 53.78 ? 73  LYS A CD  1 
ATOM   632  C CE  . LYS A 1 73  ? -18.329 11.473 90.907  1.00 57.86 ? 73  LYS A CE  1 
ATOM   633  N NZ  . LYS A 1 73  ? -17.682 12.788 90.652  1.00 61.37 ? 73  LYS A NZ  1 
ATOM   634  N N   . ASP A 1 74  ? -16.116 12.796 87.063  1.00 15.83 ? 74  ASP A N   1 
ATOM   635  C CA  . ASP A 1 74  ? -15.771 14.160 86.663  1.00 12.73 ? 74  ASP A CA  1 
ATOM   636  C C   . ASP A 1 74  ? -16.414 15.119 87.666  1.00 12.42 ? 74  ASP A C   1 
ATOM   637  O O   . ASP A 1 74  ? -17.648 15.227 87.730  1.00 14.33 ? 74  ASP A O   1 
ATOM   638  C CB  . ASP A 1 74  ? -16.233 14.400 85.223  1.00 10.26 ? 74  ASP A CB  1 
ATOM   639  C CG  . ASP A 1 74  ? -15.888 15.774 84.689  1.00 11.03 ? 74  ASP A CG  1 
ATOM   640  O OD1 . ASP A 1 74  ? -16.030 16.768 85.424  1.00 15.06 ? 74  ASP A OD1 1 
ATOM   641  O OD2 . ASP A 1 74  ? -15.545 15.859 83.481  1.00 14.04 ? 74  ASP A OD2 1 
ATOM   642  N N   . VAL A 1 75  ? -15.577 15.833 88.431  1.00 16.60 ? 75  VAL A N   1 
ATOM   643  C CA  . VAL A 1 75  ? -16.101 16.611 89.554  1.00 18.31 ? 75  VAL A CA  1 
ATOM   644  C C   . VAL A 1 75  ? -16.911 17.807 89.060  1.00 18.82 ? 75  VAL A C   1 
ATOM   645  O O   . VAL A 1 75  ? -17.992 18.097 89.595  1.00 19.57 ? 75  VAL A O   1 
ATOM   646  C CB  . VAL A 1 75  ? -14.967 17.027 90.516  1.00 21.14 ? 75  VAL A CB  1 
ATOM   647  C CG1 . VAL A 1 75  ? -14.280 15.786 91.079  1.00 24.47 ? 75  VAL A CG1 1 
ATOM   648  C CG2 . VAL A 1 75  ? -13.961 17.937 89.841  1.00 29.57 ? 75  VAL A CG2 1 
ATOM   649  N N   A PHE A 1 76  ? -16.431 18.494 88.022  0.50 15.02 ? 76  PHE A N   1 
ATOM   650  N N   B PHE A 1 76  ? -16.414 18.471 88.042  0.50 15.02 ? 76  PHE A N   1 
ATOM   651  C CA  A PHE A 1 76  ? -17.198 19.603 87.481  0.50 13.40 ? 76  PHE A CA  1 
ATOM   652  C CA  B PHE A 1 76  ? -17.171 19.538 87.500  0.50 13.40 ? 76  PHE A CA  1 
ATOM   653  C C   A PHE A 1 76  ? -18.532 19.102 86.873  0.50 17.57 ? 76  PHE A C   1 
ATOM   654  C C   B PHE A 1 76  ? -18.529 19.086 86.883  0.50 17.57 ? 76  PHE A C   1 
ATOM   655  O O   A PHE A 1 76  ? -19.534 19.704 87.006  0.50 15.98 ? 76  PHE A O   1 
ATOM   656  O O   B PHE A 1 76  ? -19.520 19.714 87.000  0.50 15.98 ? 76  PHE A O   1 
ATOM   657  C CB  A PHE A 1 76  ? -16.457 20.468 86.443  0.50 16.54 ? 76  PHE A CB  1 
ATOM   658  C CB  B PHE A 1 76  ? -16.360 20.326 86.515  0.50 16.54 ? 76  PHE A CB  1 
ATOM   659  C CG  A PHE A 1 76  ? -15.509 21.453 87.032  0.50 23.54 ? 76  PHE A CG  1 
ATOM   660  C CG  B PHE A 1 76  ? -16.997 21.504 86.173  0.50 23.54 ? 76  PHE A CG  1 
ATOM   661  C CD1 A PHE A 1 76  ? -14.236 21.068 87.413  0.50 24.54 ? 76  PHE A CD1 1 
ATOM   662  C CD1 B PHE A 1 76  ? -17.900 21.509 85.129  0.50 24.54 ? 76  PHE A CD1 1 
ATOM   663  C CD2 A PHE A 1 76  ? -15.854 22.788 87.154  0.50 29.05 ? 76  PHE A CD2 1 
ATOM   664  C CD2 B PHE A 1 76  ? -16.836 22.629 86.961  0.50 29.05 ? 76  PHE A CD2 1 
ATOM   665  C CE1 A PHE A 1 76  ? -13.358 21.941 87.940  0.50 24.31 ? 76  PHE A CE1 1 
ATOM   666  C CE1 B PHE A 1 76  ? -18.579 22.650 84.811  0.50 24.31 ? 76  PHE A CE1 1 
ATOM   667  C CE2 A PHE A 1 76  ? -14.942 23.690 87.681  0.50 31.54 ? 76  PHE A CE2 1 
ATOM   668  C CE2 B PHE A 1 76  ? -17.563 23.747 86.693  0.50 31.54 ? 76  PHE A CE2 1 
ATOM   669  C CZ  A PHE A 1 76  ? -13.690 23.266 88.078  0.50 28.91 ? 76  PHE A CZ  1 
ATOM   670  C CZ  B PHE A 1 76  ? -18.426 23.765 85.615  0.50 28.91 ? 76  PHE A CZ  1 
ATOM   671  N N   . LEU A 1 77  ? -18.495 17.988 86.187  1.00 15.92 ? 77  LEU A N   1 
ATOM   672  C CA  . LEU A 1 77  ? -19.736 17.476 85.603  1.00 18.94 ? 77  LEU A CA  1 
ATOM   673  C C   . LEU A 1 77  ? -20.746 17.079 86.675  1.00 18.97 ? 77  LEU A C   1 
ATOM   674  O O   . LEU A 1 77  ? -21.962 17.236 86.484  1.00 17.11 ? 77  LEU A O   1 
ATOM   675  C CB  . LEU A 1 77  ? -19.432 16.290 84.687  1.00 17.10 ? 77  LEU A CB  1 
ATOM   676  C CG  . LEU A 1 77  ? -20.551 15.824 83.755  1.00 24.93 ? 77  LEU A CG  1 
ATOM   677  C CD1 . LEU A 1 77  ? -21.156 16.991 82.957  1.00 19.48 ? 77  LEU A CD1 1 
ATOM   678  C CD2 . LEU A 1 77  ? -19.997 14.766 82.823  1.00 21.72 ? 77  LEU A CD2 1 
ATOM   679  N N   . GLU A 1 78  ? -20.272 16.562 87.810  1.00 19.49 ? 78  GLU A N   1 
ATOM   680  C CA  . GLU A 1 78  ? -21.184 16.257 88.906  1.00 18.96 ? 78  GLU A CA  1 
ATOM   681  C C   . GLU A 1 78  ? -21.877 17.515 89.412  1.00 18.58 ? 78  GLU A C   1 
ATOM   682  O O   . GLU A 1 78  ? -23.058 17.475 89.770  1.00 21.70 ? 78  GLU A O   1 
ATOM   683  C CB  . GLU A 1 78  ? -20.425 15.567 90.039  1.00 23.58 ? 78  GLU A CB  1 
ATOM   684  C CG  . GLU A 1 78  ? -20.612 14.066 90.055  1.00 42.04 ? 78  GLU A CG  1 
ATOM   685  C CD  . GLU A 1 78  ? -22.075 13.661 90.136  1.00 53.24 ? 78  GLU A CD  1 
ATOM   686  O OE1 . GLU A 1 78  ? -22.645 13.269 89.096  1.00 59.09 ? 78  GLU A OE1 1 
ATOM   687  O OE2 . GLU A 1 78  ? -22.659 13.739 91.238  1.00 56.76 ? 78  GLU A OE2 1 
ATOM   688  N N   . ALA A 1 79  ? -21.165 18.640 89.450  1.00 18.86 ? 79  ALA A N   1 
ATOM   689  C CA  . ALA A 1 79  ? -21.816 19.887 89.840  1.00 14.47 ? 79  ALA A CA  1 
ATOM   690  C C   . ALA A 1 79  ? -22.841 20.337 88.810  1.00 17.90 ? 79  ALA A C   1 
ATOM   691  O O   . ALA A 1 79  ? -23.766 21.077 89.155  1.00 20.53 ? 79  ALA A O   1 
ATOM   692  C CB  . ALA A 1 79  ? -20.787 21.001 90.049  1.00 17.32 ? 79  ALA A CB  1 
ATOM   693  N N   . ILE A 1 80  ? -22.701 19.914 87.553  1.00 14.99 ? 80  ILE A N   1 
ATOM   694  C CA  . ILE A 1 80  ? -23.730 20.232 86.565  1.00 15.54 ? 80  ILE A CA  1 
ATOM   695  C C   . ILE A 1 80  ? -24.919 19.280 86.694  1.00 15.65 ? 80  ILE A C   1 
ATOM   696  O O   . ILE A 1 80  ? -26.077 19.700 86.601  1.00 15.17 ? 80  ILE A O   1 
ATOM   697  C CB  . ILE A 1 80  ? -23.114 20.205 85.149  1.00 13.78 ? 80  ILE A CB  1 
ATOM   698  C CG1 . ILE A 1 80  ? -22.121 21.361 84.991  1.00 18.22 ? 80  ILE A CG1 1 
ATOM   699  C CG2 . ILE A 1 80  ? -24.218 20.210 84.055  1.00 13.20 ? 80  ILE A CG2 1 
ATOM   700  C CD1 . ILE A 1 80  ? -21.679 21.618 83.574  1.00 23.27 ? 80  ILE A CD1 1 
ATOM   701  N N   . ARG A 1 81  ? -24.660 17.993 86.935  1.00 15.61 ? 81  ARG A N   1 
ATOM   702  C CA  . ARG A 1 81  ? -25.731 16.997 86.890  1.00 18.93 ? 81  ARG A CA  1 
ATOM   703  C C   . ARG A 1 81  ? -26.695 17.128 88.070  1.00 15.18 ? 81  ARG A C   1 
ATOM   704  O O   . ARG A 1 81  ? -27.902 16.905 87.918  1.00 18.60 ? 81  ARG A O   1 
ATOM   705  C CB  . ARG A 1 81  ? -25.128 15.590 86.847  1.00 18.27 ? 81  ARG A CB  1 
ATOM   706  C CG  . ARG A 1 81  ? -26.158 14.473 86.866  1.00 26.94 ? 81  ARG A CG  1 
ATOM   707  C CD  . ARG A 1 81  ? -25.513 13.101 86.992  1.00 36.92 ? 81  ARG A CD  1 
ATOM   708  N NE  . ARG A 1 81  ? -25.000 12.621 85.714  1.00 43.19 ? 81  ARG A NE  1 
ATOM   709  C CZ  . ARG A 1 81  ? -25.764 12.203 84.706  1.00 47.39 ? 81  ARG A CZ  1 
ATOM   710  N NH1 . ARG A 1 81  ? -27.089 12.209 84.817  1.00 43.40 ? 81  ARG A NH1 1 
ATOM   711  N NH2 . ARG A 1 81  ? -25.198 11.782 83.581  1.00 45.90 ? 81  ARG A NH2 1 
ATOM   712  N N   . LYS A 1 82  ? -26.186 17.469 89.255  1.00 16.30 ? 82  LYS A N   1 
ATOM   713  C CA  . LYS A 1 82  ? -27.012 17.458 90.459  1.00 13.71 ? 82  LYS A CA  1 
ATOM   714  C C   . LYS A 1 82  ? -28.174 18.435 90.362  1.00 15.73 ? 82  LYS A C   1 
ATOM   715  O O   . LYS A 1 82  ? -28.060 19.511 89.768  1.00 15.79 ? 82  LYS A O   1 
ATOM   716  C CB  . LYS A 1 82  ? -26.190 17.853 91.687  1.00 18.68 ? 82  LYS A CB  1 
ATOM   717  C CG  . LYS A 1 82  ? -25.199 16.845 92.198  1.00 30.50 ? 82  LYS A CG  1 
ATOM   718  C CD  . LYS A 1 82  ? -24.429 17.511 93.332  1.00 26.40 ? 82  LYS A CD  1 
ATOM   719  C CE  . LYS A 1 82  ? -23.426 16.599 93.986  1.00 31.22 ? 82  LYS A CE  1 
ATOM   720  N NZ  . LYS A 1 82  ? -23.029 17.200 95.288  1.00 28.86 ? 82  LYS A NZ  1 
ATOM   721  N N   . ASP A 1 83  ? -29.277 18.074 91.015  1.00 15.61 ? 83  ASP A N   1 
ATOM   722  C CA  . ASP A 1 83  ? -30.293 19.063 91.352  1.00 14.63 ? 83  ASP A CA  1 
ATOM   723  C C   . ASP A 1 83  ? -29.626 20.191 92.139  1.00 16.22 ? 83  ASP A C   1 
ATOM   724  O O   . ASP A 1 83  ? -28.802 19.914 93.024  1.00 13.45 ? 83  ASP A O   1 
ATOM   725  C CB  . ASP A 1 83  ? -31.407 18.421 92.178  1.00 18.38 ? 83  ASP A CB  1 
ATOM   726  C CG  . ASP A 1 83  ? -32.612 19.334 92.361  1.00 24.61 ? 83  ASP A CG  1 
ATOM   727  O OD1 . ASP A 1 83  ? -32.484 20.390 93.013  1.00 21.46 ? 83  ASP A OD1 1 
ATOM   728  O OD2 . ASP A 1 83  ? -33.705 18.970 91.865  1.00 26.92 ? 83  ASP A OD2 1 
ATOM   729  N N   . PRO A 1 84  ? -29.892 21.455 91.814  1.00 19.57 ? 84  PRO A N   1 
ATOM   730  C CA  . PRO A 1 84  ? -29.222 22.537 92.551  1.00 14.79 ? 84  PRO A CA  1 
ATOM   731  C C   . PRO A 1 84  ? -29.427 22.468 94.052  1.00 14.98 ? 84  PRO A C   1 
ATOM   732  O O   . PRO A 1 84  ? -28.562 22.952 94.794  1.00 18.64 ? 84  PRO A O   1 
ATOM   733  C CB  . PRO A 1 84  ? -29.843 23.809 91.958  1.00 18.78 ? 84  PRO A CB  1 
ATOM   734  C CG  . PRO A 1 84  ? -30.234 23.404 90.561  1.00 16.34 ? 84  PRO A CG  1 
ATOM   735  C CD  . PRO A 1 84  ? -30.708 21.971 90.698  1.00 21.96 ? 84  PRO A CD  1 
ATOM   736  N N   . ASP A 1 85  ? -30.534 21.880 94.525  1.00 14.14 ? 85  ASP A N   1 
ATOM   737  C CA  . ASP A 1 85  ? -30.718 21.742 95.969  1.00 16.59 ? 85  ASP A CA  1 
ATOM   738  C C   . ASP A 1 85  ? -29.653 20.849 96.598  1.00 16.92 ? 85  ASP A C   1 
ATOM   739  O O   . ASP A 1 85  ? -29.432 20.919 97.817  1.00 15.99 ? 85  ASP A O   1 
ATOM   740  C CB  . ASP A 1 85  ? -32.097 21.174 96.282  1.00 18.09 ? 85  ASP A CB  1 
ATOM   741  C CG  . ASP A 1 85  ? -33.215 22.178 96.059  1.00 26.11 ? 85  ASP A CG  1 
ATOM   742  O OD1 . ASP A 1 85  ? -32.940 23.394 95.975  1.00 24.48 ? 85  ASP A OD1 1 
ATOM   743  O OD2 . ASP A 1 85  ? -34.384 21.740 95.991  1.00 32.97 ? 85  ASP A OD2 1 
ATOM   744  N N   . ASP A 1 86  ? -29.009 20.004 95.804  1.00 15.69 ? 86  ASP A N   1 
ATOM   745  C CA  . ASP A 1 86  ? -27.993 19.080 96.283  1.00 15.01 ? 86  ASP A CA  1 
ATOM   746  C C   . ASP A 1 86  ? -26.580 19.632 96.144  1.00 19.34 ? 86  ASP A C   1 
ATOM   747  O O   . ASP A 1 86  ? -25.620 18.967 96.556  1.00 18.63 ? 86  ASP A O   1 
ATOM   748  C CB  . ASP A 1 86  ? -28.108 17.753 95.532  1.00 18.86 ? 86  ASP A CB  1 
ATOM   749  C CG  . ASP A 1 86  ? -29.346 16.965 95.921  1.00 23.74 ? 86  ASP A CG  1 
ATOM   750  O OD1 . ASP A 1 86  ? -29.883 17.182 97.024  1.00 30.59 ? 86  ASP A OD1 1 
ATOM   751  O OD2 . ASP A 1 86  ? -29.771 16.118 95.119  1.00 29.53 ? 86  ASP A OD2 1 
ATOM   752  N N   . LEU A 1 87  ? -26.430 20.823 95.576  1.00 14.50 ? 87  LEU A N   1 
ATOM   753  C CA  . LEU A 1 87  ? -25.113 21.399 95.344  1.00 13.04 ? 87  LEU A CA  1 
ATOM   754  C C   . LEU A 1 87  ? -24.413 21.803 96.643  1.00 13.40 ? 87  LEU A C   1 
ATOM   755  O O   . LEU A 1 87  ? -24.998 22.462 97.505  1.00 15.95 ? 87  LEU A O   1 
ATOM   756  C CB  . LEU A 1 87  ? -25.233 22.617 94.436  1.00 13.31 ? 87  LEU A CB  1 
ATOM   757  C CG  . LEU A 1 87  ? -25.459 22.292 92.965  1.00 13.41 ? 87  LEU A CG  1 
ATOM   758  C CD1 . LEU A 1 87  ? -25.811 23.574 92.204  1.00 14.50 ? 87  LEU A CD1 1 
ATOM   759  C CD2 . LEU A 1 87  ? -24.211 21.645 92.360  1.00 18.33 ? 87  LEU A CD2 1 
ATOM   760  N N   . GLU A 1 88  ? -23.138 21.436 96.752  1.00 13.25 ? 88  GLU A N   1 
ATOM   761  C CA  . GLU A 1 88  ? -22.291 21.982 97.799  1.00 14.39 ? 88  GLU A CA  1 
ATOM   762  C C   . GLU A 1 88  ? -21.973 23.437 97.496  1.00 15.45 ? 88  GLU A C   1 
ATOM   763  O O   . GLU A 1 88  ? -21.934 23.860 96.337  1.00 14.52 ? 88  GLU A O   1 
ATOM   764  C CB  . GLU A 1 88  ? -20.989 21.181 97.909  1.00 19.49 ? 88  GLU A CB  1 
ATOM   765  C CG  . GLU A 1 88  ? -21.254 19.700 98.117  1.00 18.20 ? 88  GLU A CG  1 
ATOM   766  C CD  . GLU A 1 88  ? -20.061 18.804 97.820  1.00 28.37 ? 88  GLU A CD  1 
ATOM   767  O OE1 . GLU A 1 88  ? -19.030 19.293 97.309  1.00 26.45 ? 88  GLU A OE1 1 
ATOM   768  O OE2 . GLU A 1 88  ? -20.167 17.589 98.101  1.00 31.69 ? 88  GLU A OE2 1 
ATOM   769  N N   . LYS A 1 89  ? -21.735 24.209 98.558  1.00 14.74 ? 89  LYS A N   1 
ATOM   770  C CA  . LYS A 1 89  ? -21.248 25.570 98.366  1.00 18.58 ? 89  LYS A CA  1 
ATOM   771  C C   . LYS A 1 89  ? -20.031 25.586 97.452  1.00 15.89 ? 89  LYS A C   1 
ATOM   772  O O   . LYS A 1 89  ? -19.927 26.435 96.557  1.00 18.90 ? 89  LYS A O   1 
ATOM   773  C CB  . LYS A 1 89  ? -20.907 26.213 99.712  1.00 21.49 ? 89  LYS A CB  1 
ATOM   774  C CG  . LYS A 1 89  ? -22.042 26.255 100.701 1.00 26.09 ? 89  LYS A CG  1 
ATOM   775  C CD  . LYS A 1 89  ? -21.548 26.772 102.052 1.00 31.80 ? 89  LYS A CD  1 
ATOM   776  C CE  . LYS A 1 89  ? -22.522 26.450 103.172 1.00 36.01 ? 89  LYS A CE  1 
ATOM   777  N NZ  . LYS A 1 89  ? -23.846 27.095 102.979 1.00 36.38 ? 89  LYS A NZ  1 
ATOM   778  N N   . GLU A 1 90  ? -19.120 24.626 97.629  1.00 14.30 ? 90  GLU A N   1 
ATOM   779  C CA  . GLU A 1 90  ? -17.930 24.578 96.777  1.00 15.27 ? 90  GLU A CA  1 
ATOM   780  C C   . GLU A 1 90  ? -18.285 24.331 95.318  1.00 19.62 ? 90  GLU A C   1 
ATOM   781  O O   . GLU A 1 90  ? -17.595 24.833 94.425  1.00 17.02 ? 90  GLU A O   1 
ATOM   782  C CB  . GLU A 1 90  ? -16.961 23.495 97.246  1.00 17.19 ? 90  GLU A CB  1 
ATOM   783  C CG  . GLU A 1 90  ? -16.147 23.857 98.472  1.00 35.35 ? 90  GLU A CG  1 
ATOM   784  C CD  . GLU A 1 90  ? -15.268 22.704 98.929  1.00 48.60 ? 90  GLU A CD  1 
ATOM   785  O OE1 . GLU A 1 90  ? -15.074 21.753 98.138  1.00 44.47 ? 90  GLU A OE1 1 
ATOM   786  O OE2 . GLU A 1 90  ? -14.786 22.744 100.083 1.00 49.13 ? 90  GLU A OE2 1 
ATOM   787  N N   . GLU A 1 91  ? -19.337 23.545 95.056  1.00 14.88 ? 91  GLU A N   1 
ATOM   788  C CA  . GLU A 1 91  ? -19.724 23.253 93.678  1.00 13.01 ? 91  GLU A CA  1 
ATOM   789  C C   . GLU A 1 91  ? -20.374 24.462 93.020  1.00 14.75 ? 91  GLU A C   1 
ATOM   790  O O   . GLU A 1 91  ? -20.183 24.701 91.823  1.00 14.41 ? 91  GLU A O   1 
ATOM   791  C CB  . GLU A 1 91  ? -20.660 22.048 93.642  1.00 12.24 ? 91  GLU A CB  1 
ATOM   792  C CG  . GLU A 1 91  ? -19.969 20.737 94.001  1.00 19.93 ? 91  GLU A CG  1 
ATOM   793  C CD  . GLU A 1 91  ? -20.943 19.579 94.125  1.00 21.14 ? 91  GLU A CD  1 
ATOM   794  O OE1 . GLU A 1 91  ? -21.968 19.719 94.828  1.00 17.54 ? 91  GLU A OE1 1 
ATOM   795  O OE2 . GLU A 1 91  ? -20.689 18.528 93.504  1.00 21.77 ? 91  GLU A OE2 1 
ATOM   796  N N   . VAL A 1 92  ? -21.149 25.230 93.781  1.00 15.03 ? 92  VAL A N   1 
ATOM   797  C CA  . VAL A 1 92  ? -21.700 26.471 93.245  1.00 17.04 ? 92  VAL A CA  1 
ATOM   798  C C   . VAL A 1 92  ? -20.566 27.409 92.867  1.00 17.32 ? 92  VAL A C   1 
ATOM   799  O O   . VAL A 1 92  ? -20.568 28.014 91.789  1.00 16.80 ? 92  VAL A O   1 
ATOM   800  C CB  . VAL A 1 92  ? -22.658 27.121 94.258  1.00 15.19 ? 92  VAL A CB  1 
ATOM   801  C CG1 . VAL A 1 92  ? -23.107 28.490 93.747  1.00 19.61 ? 92  VAL A CG1 1 
ATOM   802  C CG2 . VAL A 1 92  ? -23.871 26.209 94.547  1.00 14.02 ? 92  VAL A CG2 1 
ATOM   803  N N   . GLU A 1 93  ? -19.570 27.527 93.741  1.00 16.28 ? 93  GLU A N   1 
ATOM   804  C CA  . GLU A 1 93  ? -18.411 28.358 93.431  1.00 16.14 ? 93  GLU A CA  1 
ATOM   805  C C   . GLU A 1 93  ? -17.721 27.887 92.161  1.00 17.22 ? 93  GLU A C   1 
ATOM   806  O O   . GLU A 1 93  ? -17.358 28.705 91.305  1.00 20.72 ? 93  GLU A O   1 
ATOM   807  C CB  . GLU A 1 93  ? -17.441 28.355 94.607  1.00 20.01 ? 93  GLU A CB  1 
ATOM   808  C CG  . GLU A 1 93  ? -17.918 29.234 95.740  1.00 25.68 ? 93  GLU A CG  1 
ATOM   809  C CD  . GLU A 1 93  ? -17.231 28.921 97.051  1.00 38.96 ? 93  GLU A CD  1 
ATOM   810  O OE1 . GLU A 1 93  ? -17.650 29.484 98.083  1.00 40.91 ? 93  GLU A OE1 1 
ATOM   811  O OE2 . GLU A 1 93  ? -16.275 28.116 97.047  1.00 40.45 ? 93  GLU A OE2 1 
ATOM   812  N N   . LYS A 1 94  ? -17.537 26.572 92.018  1.00 15.68 ? 94  LYS A N   1 
ATOM   813  C CA  . LYS A 1 94  ? -16.894 26.039 90.822  1.00 19.81 ? 94  LYS A CA  1 
ATOM   814  C C   . LYS A 1 94  ? -17.698 26.373 89.572  1.00 15.54 ? 94  LYS A C   1 
ATOM   815  O O   . LYS A 1 94  ? -17.126 26.738 88.538  1.00 18.61 ? 94  LYS A O   1 
ATOM   816  C CB  . LYS A 1 94  ? -16.736 24.526 90.935  1.00 21.03 ? 94  LYS A CB  1 
ATOM   817  C CG  . LYS A 1 94  ? -15.527 24.035 91.691  1.00 25.92 ? 94  LYS A CG  1 
ATOM   818  C CD  . LYS A 1 94  ? -15.522 22.508 91.684  1.00 36.86 ? 94  LYS A CD  1 
ATOM   819  C CE  . LYS A 1 94  ? -14.165 21.934 92.064  1.00 41.02 ? 94  LYS A CE  1 
ATOM   820  N NZ  . LYS A 1 94  ? -13.645 22.525 93.327  1.00 47.25 ? 94  LYS A NZ  1 
ATOM   821  N N   . LEU A 1 95  ? -19.027 26.230 89.646  1.00 12.53 ? 95  LEU A N   1 
ATOM   822  C CA  . LEU A 1 95  ? -19.888 26.538 88.504  1.00 16.01 ? 95  LEU A CA  1 
ATOM   823  C C   . LEU A 1 95  ? -19.749 27.995 88.085  1.00 18.01 ? 95  LEU A C   1 
ATOM   824  O O   . LEU A 1 95  ? -19.630 28.304 86.893  1.00 14.07 ? 95  LEU A O   1 
ATOM   825  C CB  . LEU A 1 95  ? -21.350 26.244 88.851  1.00 20.22 ? 95  LEU A CB  1 
ATOM   826  C CG  . LEU A 1 95  ? -21.879 24.817 88.932  1.00 32.29 ? 95  LEU A CG  1 
ATOM   827  C CD1 . LEU A 1 95  ? -23.361 24.851 89.270  1.00 36.16 ? 95  LEU A CD1 1 
ATOM   828  C CD2 . LEU A 1 95  ? -21.647 24.079 87.618  1.00 35.74 ? 95  LEU A CD2 1 
ATOM   829  N N   . ILE A 1 96  ? -19.799 28.909 89.056  1.00 17.12 ? 96  ILE A N   1 
ATOM   830  C CA  . ILE A 1 96  ? -19.692 30.335 88.753  1.00 16.55 ? 96  ILE A CA  1 
ATOM   831  C C   . ILE A 1 96  ? -18.316 30.654 88.179  1.00 16.29 ? 96  ILE A C   1 
ATOM   832  O O   . ILE A 1 96  ? -18.194 31.371 87.177  1.00 17.66 ? 96  ILE A O   1 
ATOM   833  C CB  . ILE A 1 96  ? -19.994 31.167 90.015  1.00 18.64 ? 96  ILE A CB  1 
ATOM   834  C CG1 . ILE A 1 96  ? -21.478 31.049 90.381  1.00 17.37 ? 96  ILE A CG1 1 
ATOM   835  C CG2 . ILE A 1 96  ? -19.644 32.645 89.800  1.00 17.43 ? 96  ILE A CG2 1 
ATOM   836  C CD1 . ILE A 1 96  ? -21.772 31.504 91.781  1.00 24.65 ? 96  ILE A CD1 1 
ATOM   837  N N   . GLU A 1 97  ? -17.263 30.097 88.779  1.00 14.48 ? 97  GLU A N   1 
ATOM   838  C CA  . GLU A 1 97  ? -15.908 30.346 88.292  1.00 17.05 ? 97  GLU A CA  1 
ATOM   839  C C   . GLU A 1 97  ? -15.721 29.820 86.869  1.00 16.81 ? 97  GLU A C   1 
ATOM   840  O O   . GLU A 1 97  ? -15.131 30.504 86.018  1.00 17.07 ? 97  GLU A O   1 
ATOM   841  C CB  . GLU A 1 97  ? -14.906 29.714 89.256  1.00 19.01 ? 97  GLU A CB  1 
ATOM   842  C CG  . GLU A 1 97  ? -13.459 29.826 88.844  1.00 31.77 ? 97  GLU A CG  1 
ATOM   843  C CD  . GLU A 1 97  ? -12.537 29.146 89.835  1.00 51.45 ? 97  GLU A CD  1 
ATOM   844  O OE1 . GLU A 1 97  ? -11.386 29.608 89.996  1.00 57.53 ? 97  GLU A OE1 1 
ATOM   845  O OE2 . GLU A 1 97  ? -12.971 28.152 90.456  1.00 51.94 ? 97  GLU A OE2 1 
ATOM   846  N N   . PHE A 1 98  ? -16.231 28.614 86.585  1.00 12.97 ? 98  PHE A N   1 
ATOM   847  C CA  . PHE A 1 98  ? -16.176 28.074 85.225  1.00 14.04 ? 98  PHE A CA  1 
ATOM   848  C C   . PHE A 1 98  ? -16.922 28.967 84.241  1.00 14.18 ? 98  PHE A C   1 
ATOM   849  O O   . PHE A 1 98  ? -16.458 29.187 83.111  1.00 13.51 ? 98  PHE A O   1 
ATOM   850  C CB  . PHE A 1 98  ? -16.754 26.655 85.188  1.00 15.48 ? 98  PHE A CB  1 
ATOM   851  C CG  . PHE A 1 98  ? -16.405 25.884 83.937  1.00 16.62 ? 98  PHE A CG  1 
ATOM   852  C CD1 . PHE A 1 98  ? -15.132 25.330 83.766  1.00 13.43 ? 98  PHE A CD1 1 
ATOM   853  C CD2 . PHE A 1 98  ? -17.341 25.713 82.941  1.00 15.32 ? 98  PHE A CD2 1 
ATOM   854  C CE1 . PHE A 1 98  ? -14.816 24.608 82.614  1.00 12.16 ? 98  PHE A CE1 1 
ATOM   855  C CE2 . PHE A 1 98  ? -17.036 25.007 81.782  1.00 12.30 ? 98  PHE A CE2 1 
ATOM   856  C CZ  . PHE A 1 98  ? -15.754 24.443 81.621  1.00 13.26 ? 98  PHE A CZ  1 
ATOM   857  N N   . THR A 1 99  ? -18.094 29.472 84.639  1.00 13.82 ? 99  THR A N   1 
ATOM   858  C CA  . THR A 1 99  ? -18.840 30.361 83.755  1.00 14.07 ? 99  THR A CA  1 
ATOM   859  C C   . THR A 1 99  ? -18.049 31.630 83.473  1.00 14.98 ? 99  THR A C   1 
ATOM   860  O O   . THR A 1 99  ? -17.960 32.073 82.321  1.00 14.14 ? 99  THR A O   1 
ATOM   861  C CB  . THR A 1 99  ? -20.194 30.705 84.377  1.00 14.08 ? 99  THR A CB  1 
ATOM   862  O OG1 . THR A 1 99  ? -20.892 29.489 84.704  1.00 15.95 ? 99  THR A OG1 1 
ATOM   863  C CG2 . THR A 1 99  ? -21.032 31.512 83.415  1.00 13.49 ? 99  THR A CG2 1 
ATOM   864  N N   . LYS A 1 100 ? -17.447 32.212 84.516  1.00 17.16 ? 100 LYS A N   1 
ATOM   865  C CA  . LYS A 1 100 ? -16.669 33.438 84.353  1.00 14.01 ? 100 LYS A CA  1 
ATOM   866  C C   . LYS A 1 100 ? -15.488 33.248 83.410  1.00 14.19 ? 100 LYS A C   1 
ATOM   867  O O   . LYS A 1 100 ? -15.172 34.142 82.615  1.00 18.05 ? 100 LYS A O   1 
ATOM   868  C CB  . LYS A 1 100 ? -16.163 33.921 85.710  1.00 19.19 ? 100 LYS A CB  1 
ATOM   869  C CG  . LYS A 1 100 ? -17.196 34.633 86.555  1.00 27.09 ? 100 LYS A CG  1 
ATOM   870  C CD  . LYS A 1 100 ? -16.527 35.368 87.713  1.00 37.97 ? 100 LYS A CD  1 
ATOM   871  C CE  . LYS A 1 100 ? -17.417 35.427 88.942  1.00 46.52 ? 100 LYS A CE  1 
ATOM   872  N NZ  . LYS A 1 100 ? -18.710 36.114 88.683  1.00 52.41 ? 100 LYS A NZ  1 
ATOM   873  N N   . LEU A 1 101 ? -14.796 32.115 83.518  1.00 15.60 ? 101 LEU A N   1 
ATOM   874  C CA  . LEU A 1 101 ? -13.670 31.845 82.628  1.00 13.95 ? 101 LEU A CA  1 
ATOM   875  C C   . LEU A 1 101 ? -14.102 31.859 81.170  1.00 16.62 ? 101 LEU A C   1 
ATOM   876  O O   . LEU A 1 101 ? -13.369 32.338 80.298  1.00 16.27 ? 101 LEU A O   1 
ATOM   877  C CB  . LEU A 1 101 ? -13.055 30.493 82.983  1.00 15.30 ? 101 LEU A CB  1 
ATOM   878  C CG  . LEU A 1 101 ? -11.997 29.963 82.026  1.00 18.73 ? 101 LEU A CG  1 
ATOM   879  C CD1 . LEU A 1 101 ? -10.738 30.847 82.101  1.00 25.73 ? 101 LEU A CD1 1 
ATOM   880  C CD2 . LEU A 1 101 ? -11.656 28.516 82.378  1.00 19.04 ? 101 LEU A CD2 1 
ATOM   881  N N   . ASN A 1 102 ? -15.294 31.337 80.887  1.00 12.83 ? 102 ASN A N   1 
ATOM   882  C CA  . ASN A 1 102 ? -15.767 31.115 79.534  1.00 11.62 ? 102 ASN A CA  1 
ATOM   883  C C   . ASN A 1 102 ? -16.691 32.213 79.029  1.00 10.28 ? 102 ASN A C   1 
ATOM   884  O O   . ASN A 1 102 ? -17.087 32.175 77.851  1.00 12.00 ? 102 ASN A O   1 
ATOM   885  C CB  . ASN A 1 102 ? -16.508 29.777 79.470  1.00 11.56 ? 102 ASN A CB  1 
ATOM   886  C CG  . ASN A 1 102 ? -15.579 28.585 79.599  1.00 20.02 ? 102 ASN A CG  1 
ATOM   887  O OD1 . ASN A 1 102 ? -14.725 28.364 78.749  1.00 18.60 ? 102 ASN A OD1 1 
ATOM   888  N ND2 . ASN A 1 102 ? -15.769 27.791 80.643  1.00 17.97 ? 102 ASN A ND2 1 
ATOM   889  N N   . TYR A 1 103 ? -16.978 33.204 79.878  1.00 16.08 ? 103 TYR A N   1 
ATOM   890  C CA  . TYR A 1 103 ? -18.091 34.134 79.693  1.00 21.73 ? 103 TYR A CA  1 
ATOM   891  C C   . TYR A 1 103 ? -18.011 34.889 78.370  1.00 17.53 ? 103 TYR A C   1 
ATOM   892  O O   . TYR A 1 103 ? -19.042 35.166 77.748  1.00 19.20 ? 103 TYR A O   1 
ATOM   893  C CB  . TYR A 1 103 ? -18.112 35.119 80.869  1.00 18.42 ? 103 TYR A CB  1 
ATOM   894  C CG  . TYR A 1 103 ? -19.239 36.123 80.857  1.00 22.17 ? 103 TYR A CG  1 
ATOM   895  C CD1 . TYR A 1 103 ? -20.502 35.791 81.329  1.00 24.56 ? 103 TYR A CD1 1 
ATOM   896  C CD2 . TYR A 1 103 ? -19.029 37.416 80.401  1.00 28.84 ? 103 TYR A CD2 1 
ATOM   897  C CE1 . TYR A 1 103 ? -21.529 36.721 81.331  1.00 24.59 ? 103 TYR A CE1 1 
ATOM   898  C CE2 . TYR A 1 103 ? -20.043 38.349 80.401  1.00 31.46 ? 103 TYR A CE2 1 
ATOM   899  C CZ  . TYR A 1 103 ? -21.286 37.999 80.865  1.00 33.03 ? 103 TYR A CZ  1 
ATOM   900  O OH  . TYR A 1 103 ? -22.289 38.934 80.855  1.00 35.31 ? 103 TYR A OH  1 
ATOM   901  N N   . GLU A 1 104 ? -16.811 35.249 77.939  1.00 17.44 ? 104 GLU A N   1 
ATOM   902  C CA  . GLU A 1 104 ? -16.669 36.099 76.762  1.00 20.85 ? 104 GLU A CA  1 
ATOM   903  C C   . GLU A 1 104 ? -16.585 35.313 75.464  1.00 18.40 ? 104 GLU A C   1 
ATOM   904  O O   . GLU A 1 104 ? -16.535 35.925 74.394  1.00 21.20 ? 104 GLU A O   1 
ATOM   905  C CB  . GLU A 1 104 ? -15.439 36.996 76.896  1.00 21.87 ? 104 GLU A CB  1 
ATOM   906  C CG  . GLU A 1 104 ? -15.547 38.013 78.020  1.00 24.16 ? 104 GLU A CG  1 
ATOM   907  C CD  . GLU A 1 104 ? -16.570 39.102 77.735  1.00 46.13 ? 104 GLU A CD  1 
ATOM   908  O OE1 . GLU A 1 104 ? -16.992 39.246 76.567  1.00 47.49 ? 104 GLU A OE1 1 
ATOM   909  O OE2 . GLU A 1 104 ? -16.951 39.817 78.684  1.00 55.85 ? 104 GLU A OE2 1 
ATOM   910  N N   . LYS A 1 105 ? -16.556 33.987 75.529  1.00 15.88 ? 105 LYS A N   1 
ATOM   911  C CA  . LYS A 1 105 ? -16.451 33.194 74.316  1.00 15.49 ? 105 LYS A CA  1 
ATOM   912  C C   . LYS A 1 105 ? -17.767 33.212 73.549  1.00 16.45 ? 105 LYS A C   1 
ATOM   913  O O   . LYS A 1 105 ? -18.840 33.219 74.153  1.00 15.10 ? 105 LYS A O   1 
ATOM   914  C CB  . LYS A 1 105 ? -16.072 31.755 74.651  1.00 13.75 ? 105 LYS A CB  1 
ATOM   915  C CG  . LYS A 1 105 ? -14.676 31.647 75.228  1.00 17.56 ? 105 LYS A CG  1 
ATOM   916  C CD  . LYS A 1 105 ? -14.424 30.251 75.774  1.00 13.38 ? 105 LYS A CD  1 
ATOM   917  C CE  . LYS A 1 105 ? -13.020 30.164 76.381  1.00 16.46 ? 105 LYS A CE  1 
ATOM   918  N NZ  . LYS A 1 105 ? -12.811 28.753 76.828  1.00 16.41 ? 105 LYS A NZ  1 
ATOM   919  N N   . PRO A 1 106 ? -17.712 33.250 72.220  1.00 16.48 ? 106 PRO A N   1 
ATOM   920  C CA  . PRO A 1 106 ? -18.955 33.273 71.440  1.00 15.08 ? 106 PRO A CA  1 
ATOM   921  C C   . PRO A 1 106 ? -19.879 32.107 71.733  1.00 15.34 ? 106 PRO A C   1 
ATOM   922  O O   . PRO A 1 106 ? -21.100 32.276 71.652  1.00 18.68 ? 106 PRO A O   1 
ATOM   923  C CB  . PRO A 1 106 ? -18.448 33.257 69.989  1.00 16.14 ? 106 PRO A CB  1 
ATOM   924  C CG  . PRO A 1 106 ? -17.128 33.938 70.061  1.00 21.93 ? 106 PRO A CG  1 
ATOM   925  C CD  . PRO A 1 106 ? -16.531 33.557 71.398  1.00 20.42 ? 106 PRO A CD  1 
ATOM   926  N N   . ILE A 1 107 ? -19.357 30.927 72.087  1.00 14.37 ? 107 ILE A N   1 
ATOM   927  C CA  . ILE A 1 107 ? -20.264 29.826 72.372  1.00 11.90 ? 107 ILE A CA  1 
ATOM   928  C C   . ILE A 1 107 ? -21.018 30.010 73.677  1.00 14.98 ? 107 ILE A C   1 
ATOM   929  O O   . ILE A 1 107 ? -21.995 29.292 73.904  1.00 15.55 ? 107 ILE A O   1 
ATOM   930  C CB  . ILE A 1 107 ? -19.543 28.465 72.375  1.00 10.87 ? 107 ILE A CB  1 
ATOM   931  C CG1 . ILE A 1 107 ? -18.333 28.453 73.311  1.00 12.41 ? 107 ILE A CG1 1 
ATOM   932  C CG2 . ILE A 1 107 ? -19.082 28.137 70.962  1.00 12.20 ? 107 ILE A CG2 1 
ATOM   933  C CD1 . ILE A 1 107 ? -17.844 27.018 73.641  1.00 13.35 ? 107 ILE A CD1 1 
ATOM   934  N N   . TYR A 1 108 ? -20.618 30.975 74.510  1.00 15.57 ? 108 TYR A N   1 
ATOM   935  C CA  . TYR A 1 108 ? -21.335 31.312 75.736  1.00 18.20 ? 108 TYR A CA  1 
ATOM   936  C C   . TYR A 1 108 ? -22.263 32.506 75.556  1.00 15.09 ? 108 TYR A C   1 
ATOM   937  O O   . TYR A 1 108 ? -22.744 33.071 76.546  1.00 15.52 ? 108 TYR A O   1 
ATOM   938  C CB  . TYR A 1 108 ? -20.349 31.579 76.883  1.00 14.01 ? 108 TYR A CB  1 
ATOM   939  C CG  . TYR A 1 108 ? -20.023 30.327 77.679  1.00 12.24 ? 108 TYR A CG  1 
ATOM   940  C CD1 . TYR A 1 108 ? -19.224 29.323 77.138  1.00 13.07 ? 108 TYR A CD1 1 
ATOM   941  C CD2 . TYR A 1 108 ? -20.501 30.158 78.969  1.00 13.72 ? 108 TYR A CD2 1 
ATOM   942  C CE1 . TYR A 1 108 ? -18.943 28.167 77.855  1.00 13.24 ? 108 TYR A CE1 1 
ATOM   943  C CE2 . TYR A 1 108 ? -20.233 29.002 79.698  1.00 13.56 ? 108 TYR A CE2 1 
ATOM   944  C CZ  . TYR A 1 108 ? -19.440 28.016 79.134  1.00 13.83 ? 108 TYR A CZ  1 
ATOM   945  O OH  . TYR A 1 108 ? -19.138 26.873 79.835  1.00 14.27 ? 108 TYR A OH  1 
ATOM   946  N N   . ARG A 1 109 ? -22.526 32.913 74.316  1.00 14.47 ? 109 ARG A N   1 
ATOM   947  C CA  . ARG A 1 109 ? -23.346 34.091 74.057  1.00 17.23 ? 109 ARG A CA  1 
ATOM   948  C C   . ARG A 1 109 ? -24.819 33.704 74.184  1.00 20.63 ? 109 ARG A C   1 
ATOM   949  O O   . ARG A 1 109 ? -25.526 33.441 73.205  1.00 21.85 ? 109 ARG A O   1 
ATOM   950  C CB  . ARG A 1 109 ? -23.019 34.687 72.691  1.00 20.34 ? 109 ARG A CB  1 
ATOM   951  C CG  . ARG A 1 109 ? -23.299 36.179 72.593  1.00 31.41 ? 109 ARG A CG  1 
ATOM   952  C CD  . ARG A 1 109 ? -22.735 36.737 71.295  1.00 41.59 ? 109 ARG A CD  1 
ATOM   953  N NE  . ARG A 1 109 ? -21.299 36.994 71.382  1.00 48.32 ? 109 ARG A NE  1 
ATOM   954  C CZ  . ARG A 1 109 ? -20.460 36.900 70.357  1.00 48.43 ? 109 ARG A CZ  1 
ATOM   955  N NH1 . ARG A 1 109 ? -20.911 36.545 69.162  1.00 49.76 ? 109 ARG A NH1 1 
ATOM   956  N NH2 . ARG A 1 109 ? -19.170 37.161 70.530  1.00 45.60 ? 109 ARG A NH2 1 
ATOM   957  N N   . PHE A 1 110 ? -25.270 33.634 75.435  1.00 18.01 ? 110 PHE A N   1 
ATOM   958  C CA  . PHE A 1 110 ? -26.672 33.451 75.788  1.00 17.34 ? 110 PHE A CA  1 
ATOM   959  C C   . PHE A 1 110 ? -27.078 34.614 76.676  1.00 17.70 ? 110 PHE A C   1 
ATOM   960  O O   . PHE A 1 110 ? -26.419 34.871 77.684  1.00 17.42 ? 110 PHE A O   1 
ATOM   961  C CB  . PHE A 1 110 ? -26.909 32.160 76.585  1.00 17.19 ? 110 PHE A CB  1 
ATOM   962  C CG  . PHE A 1 110 ? -26.631 30.880 75.845  1.00 14.94 ? 110 PHE A CG  1 
ATOM   963  C CD1 . PHE A 1 110 ? -27.633 30.248 75.121  1.00 16.88 ? 110 PHE A CD1 1 
ATOM   964  C CD2 . PHE A 1 110 ? -25.390 30.266 75.937  1.00 21.78 ? 110 PHE A CD2 1 
ATOM   965  C CE1 . PHE A 1 110 ? -27.390 29.036 74.478  1.00 16.26 ? 110 PHE A CE1 1 
ATOM   966  C CE2 . PHE A 1 110 ? -25.142 29.062 75.293  1.00 20.81 ? 110 PHE A CE2 1 
ATOM   967  C CZ  . PHE A 1 110 ? -26.149 28.450 74.564  1.00 18.13 ? 110 PHE A CZ  1 
ATOM   968  N N   . GLU A 1 111 ? -28.177 35.295 76.332  1.00 20.50 ? 111 GLU A N   1 
ATOM   969  C CA  . GLU A 1 111 ? -28.629 36.406 77.163  1.00 19.62 ? 111 GLU A CA  1 
ATOM   970  C C   . GLU A 1 111 ? -28.834 35.964 78.608  1.00 20.05 ? 111 GLU A C   1 
ATOM   971  O O   . GLU A 1 111 ? -28.550 36.717 79.547  1.00 18.96 ? 111 GLU A O   1 
ATOM   972  C CB  . GLU A 1 111 ? -29.920 36.987 76.595  1.00 25.56 ? 111 GLU A CB  1 
ATOM   973  C CG  . GLU A 1 111 ? -30.573 38.022 77.487  1.00 44.15 ? 111 GLU A CG  1 
ATOM   974  C CD  . GLU A 1 111 ? -29.984 39.401 77.282  1.00 64.91 ? 111 GLU A CD  1 
ATOM   975  O OE1 . GLU A 1 111 ? -29.873 39.832 76.113  1.00 73.36 ? 111 GLU A OE1 1 
ATOM   976  O OE2 . GLU A 1 111 ? -29.627 40.052 78.288  1.00 71.58 ? 111 GLU A OE2 1 
ATOM   977  N N   . ARG A 1 112 ? -29.315 34.737 78.805  1.00 17.07 ? 112 ARG A N   1 
ATOM   978  C CA  . ARG A 1 112 ? -29.586 34.270 80.160  1.00 16.66 ? 112 ARG A CA  1 
ATOM   979  C C   . ARG A 1 112 ? -28.312 34.177 80.990  1.00 18.65 ? 112 ARG A C   1 
ATOM   980  O O   . ARG A 1 112 ? -28.341 34.432 82.198  1.00 21.12 ? 112 ARG A O   1 
ATOM   981  C CB  . ARG A 1 112 ? -30.305 32.923 80.115  1.00 17.08 ? 112 ARG A CB  1 
ATOM   982  C CG  . ARG A 1 112 ? -30.666 32.356 81.483  1.00 18.15 ? 112 ARG A CG  1 
ATOM   983  C CD  . ARG A 1 112 ? -31.581 33.277 82.268  1.00 19.40 ? 112 ARG A CD  1 
ATOM   984  N NE  . ARG A 1 112 ? -32.244 32.527 83.333  1.00 20.47 ? 112 ARG A NE  1 
ATOM   985  C CZ  . ARG A 1 112 ? -32.877 33.064 84.373  1.00 26.63 ? 112 ARG A CZ  1 
ATOM   986  N NH1 . ARG A 1 112 ? -32.966 34.380 84.510  1.00 27.21 ? 112 ARG A NH1 1 
ATOM   987  N NH2 . ARG A 1 112 ? -33.434 32.269 85.276  1.00 27.57 ? 112 ARG A NH2 1 
ATOM   988  N N   . ILE A 1 113 ? -27.187 33.825 80.370  1.00 17.79 ? 113 ILE A N   1 
ATOM   989  C CA  . ILE A 1 113 ? -25.938 33.777 81.124  1.00 17.11 ? 113 ILE A CA  1 
ATOM   990  C C   . ILE A 1 113 ? -25.545 35.175 81.596  1.00 19.50 ? 113 ILE A C   1 
ATOM   991  O O   . ILE A 1 113 ? -25.087 35.352 82.730  1.00 19.17 ? 113 ILE A O   1 
ATOM   992  C CB  . ILE A 1 113 ? -24.828 33.116 80.289  1.00 17.05 ? 113 ILE A CB  1 
ATOM   993  C CG1 . ILE A 1 113 ? -25.074 31.615 80.223  1.00 17.76 ? 113 ILE A CG1 1 
ATOM   994  C CG2 . ILE A 1 113 ? -23.469 33.397 80.900  1.00 17.76 ? 113 ILE A CG2 1 
ATOM   995  C CD1 . ILE A 1 113 ? -24.017 30.872 79.497  1.00 24.11 ? 113 ILE A CD1 1 
ATOM   996  N N   . ARG A 1 114 ? -25.747 36.193 80.754  1.00 18.20 ? 114 ARG A N   1 
ATOM   997  C CA  . ARG A 1 114 ? -25.472 37.556 81.186  1.00 24.77 ? 114 ARG A CA  1 
ATOM   998  C C   . ARG A 1 114 ? -26.370 37.944 82.351  1.00 25.81 ? 114 ARG A C   1 
ATOM   999  O O   . ARG A 1 114 ? -25.915 38.580 83.308  1.00 22.76 ? 114 ARG A O   1 
ATOM   1000 C CB  . ARG A 1 114 ? -25.642 38.525 80.014  1.00 29.29 ? 114 ARG A CB  1 
ATOM   1001 C CG  . ARG A 1 114 ? -25.180 39.939 80.306  1.00 45.84 ? 114 ARG A CG  1 
ATOM   1002 C CD  . ARG A 1 114 ? -25.178 40.775 79.041  1.00 54.03 ? 114 ARG A CD  1 
ATOM   1003 N NE  . ARG A 1 114 ? -26.535 41.085 78.610  1.00 58.18 ? 114 ARG A NE  1 
ATOM   1004 C CZ  . ARG A 1 114 ? -27.136 42.245 78.838  1.00 66.99 ? 114 ARG A CZ  1 
ATOM   1005 N NH1 . ARG A 1 114 ? -26.494 43.205 79.493  1.00 70.81 ? 114 ARG A NH1 1 
ATOM   1006 N NH2 . ARG A 1 114 ? -28.376 42.448 78.414  1.00 69.51 ? 114 ARG A NH2 1 
ATOM   1007 N N   . GLU A 1 115 ? -27.648 37.546 82.299  1.00 22.90 ? 115 GLU A N   1 
ATOM   1008 C CA  . GLU A 1 115 ? -28.556 37.827 83.407  1.00 27.06 ? 115 GLU A CA  1 
ATOM   1009 C C   . GLU A 1 115 ? -28.090 37.143 84.683  1.00 21.24 ? 115 GLU A C   1 
ATOM   1010 O O   . GLU A 1 115 ? -28.067 37.756 85.761  1.00 26.81 ? 115 GLU A O   1 
ATOM   1011 C CB  . GLU A 1 115 ? -29.974 37.369 83.064  1.00 27.31 ? 115 GLU A CB  1 
ATOM   1012 C CG  . GLU A 1 115 ? -30.529 37.903 81.774  1.00 29.61 ? 115 GLU A CG  1 
ATOM   1013 C CD  . GLU A 1 115 ? -31.946 37.422 81.540  1.00 37.83 ? 115 GLU A CD  1 
ATOM   1014 O OE1 . GLU A 1 115 ? -32.548 37.821 80.523  1.00 41.04 ? 115 GLU A OE1 1 
ATOM   1015 O OE2 . GLU A 1 115 ? -32.452 36.644 82.381  1.00 34.66 ? 115 GLU A OE2 1 
ATOM   1016 N N   . LEU A 1 116 ? -27.709 35.869 84.579  1.00 23.17 ? 116 LEU A N   1 
ATOM   1017 C CA  . LEU A 1 116 ? -27.341 35.111 85.770  1.00 22.13 ? 116 LEU A CA  1 
ATOM   1018 C C   . LEU A 1 116 ? -26.075 35.661 86.416  1.00 28.55 ? 116 LEU A C   1 
ATOM   1019 O O   . LEU A 1 116 ? -25.987 35.742 87.645  1.00 24.53 ? 116 LEU A O   1 
ATOM   1020 C CB  . LEU A 1 116 ? -27.171 33.637 85.412  1.00 20.17 ? 116 LEU A CB  1 
ATOM   1021 C CG  . LEU A 1 116 ? -28.460 32.950 84.959  1.00 19.62 ? 116 LEU A CG  1 
ATOM   1022 C CD1 . LEU A 1 116 ? -28.133 31.625 84.263  1.00 18.91 ? 116 LEU A CD1 1 
ATOM   1023 C CD2 . LEU A 1 116 ? -29.405 32.748 86.142  1.00 23.97 ? 116 LEU A CD2 1 
ATOM   1024 N N   . MET A 1 117 ? -25.079 36.044 85.611  1.00 24.56 ? 117 MET A N   1 
ATOM   1025 C CA  . MET A 1 117 ? -23.833 36.536 86.187  1.00 25.20 ? 117 MET A CA  1 
ATOM   1026 C C   . MET A 1 117 ? -23.961 37.944 86.758  1.00 32.59 ? 117 MET A C   1 
ATOM   1027 O O   . MET A 1 117 ? -23.037 38.401 87.436  1.00 36.11 ? 117 MET A O   1 
ATOM   1028 C CB  . MET A 1 117 ? -22.709 36.493 85.144  1.00 23.07 ? 117 MET A CB  1 
ATOM   1029 C CG  . MET A 1 117 ? -22.374 35.082 84.647  1.00 27.64 ? 117 MET A CG  1 
ATOM   1030 S SD  . MET A 1 117 ? -22.115 33.878 85.984  1.00 33.91 ? 117 MET A SD  1 
ATOM   1031 C CE  . MET A 1 117 ? -20.553 34.406 86.616  1.00 40.88 ? 117 MET A CE  1 
ATOM   1032 N N   . ASN A 1 118 ? -25.074 38.631 86.511  1.00 26.32 ? 118 ASN A N   1 
ATOM   1033 C CA  . ASN A 1 118 ? -25.328 39.950 87.077  1.00 35.42 ? 118 ASN A CA  1 
ATOM   1034 C C   . ASN A 1 118 ? -26.162 39.885 88.343  1.00 37.24 ? 118 ASN A C   1 
ATOM   1035 O O   . ASN A 1 118 ? -26.502 40.930 88.903  1.00 39.05 ? 118 ASN A O   1 
ATOM   1036 C CB  . ASN A 1 118 ? -26.033 40.844 86.050  1.00 31.69 ? 118 ASN A CB  1 
ATOM   1037 C CG  . ASN A 1 118 ? -25.077 41.775 85.338  1.00 47.20 ? 118 ASN A CG  1 
ATOM   1038 O OD1 . ASN A 1 118 ? -24.339 41.361 84.445  1.00 53.59 ? 118 ASN A OD1 1 
ATOM   1039 N ND2 . ASN A 1 118 ? -25.085 43.046 85.734  1.00 51.56 ? 118 ASN A ND2 1 
ATOM   1040 N N   . LYS A 1 119 ? -26.503 38.692 88.803  1.00 34.86 ? 119 LYS A N   1 
ATOM   1041 C CA  . LYS A 1 119 ? -27.396 38.526 89.933  1.00 32.55 ? 119 LYS A CA  1 
ATOM   1042 C C   . LYS A 1 119 ? -26.582 38.299 91.199  1.00 28.17 ? 119 LYS A C   1 
ATOM   1043 O O   . LYS A 1 119 ? -25.571 37.592 91.183  1.00 37.97 ? 119 LYS A O   1 
ATOM   1044 C CB  . LYS A 1 119 ? -28.342 37.356 89.678  1.00 34.52 ? 119 LYS A CB  1 
ATOM   1045 C CG  . LYS A 1 119 ? -29.499 37.733 88.768  1.00 43.01 ? 119 LYS A CG  1 
ATOM   1046 C CD  . LYS A 1 119 ? -30.735 36.969 89.166  1.00 49.00 ? 119 LYS A CD  1 
ATOM   1047 C CE  . LYS A 1 119 ? -30.839 36.916 90.692  1.00 56.48 ? 119 LYS A CE  1 
ATOM   1048 N NZ  . LYS A 1 119 ? -32.238 36.770 91.129  1.00 58.19 ? 119 LYS A NZ  1 
ATOM   1049 N N   . GLU A 1 120 ? -27.022 38.915 92.295  1.00 36.09 ? 120 GLU A N   1 
ATOM   1050 C CA  . GLU A 1 120 ? -26.280 38.806 93.545  1.00 42.00 ? 120 GLU A CA  1 
ATOM   1051 C C   . GLU A 1 120 ? -26.326 37.383 94.086  1.00 42.42 ? 120 GLU A C   1 
ATOM   1052 O O   . GLU A 1 120 ? -25.312 36.858 94.559  1.00 41.69 ? 120 GLU A O   1 
ATOM   1053 C CB  . GLU A 1 120 ? -26.833 39.805 94.565  1.00 41.98 ? 120 GLU A CB  1 
ATOM   1054 C CG  . GLU A 1 120 ? -26.297 41.229 94.389  1.00 46.81 ? 120 GLU A CG  1 
ATOM   1055 C CD  . GLU A 1 120 ? -27.001 42.246 95.282  1.00 59.47 ? 120 GLU A CD  1 
ATOM   1056 O OE1 . GLU A 1 120 ? -27.888 41.844 96.064  1.00 62.01 ? 120 GLU A OE1 1 
ATOM   1057 O OE2 . GLU A 1 120 ? -26.664 43.448 95.206  1.00 63.48 ? 120 GLU A OE2 1 
ATOM   1058 N N   . LYS A 1 121 ? -27.483 36.735 93.995  1.00 41.04 ? 121 LYS A N   1 
ATOM   1059 C CA  . LYS A 1 121 ? -27.667 35.382 94.490  1.00 35.10 ? 121 LYS A CA  1 
ATOM   1060 C C   . LYS A 1 121 ? -28.557 34.627 93.515  1.00 34.41 ? 121 LYS A C   1 
ATOM   1061 O O   . LYS A 1 121 ? -29.448 35.209 92.896  1.00 36.97 ? 121 LYS A O   1 
ATOM   1062 C CB  . LYS A 1 121 ? -28.284 35.377 95.893  1.00 41.77 ? 121 LYS A CB  1 
ATOM   1063 C CG  . LYS A 1 121 ? -27.998 34.115 96.687  1.00 50.29 ? 121 LYS A CG  1 
ATOM   1064 C CD  . LYS A 1 121 ? -27.811 34.434 98.163  1.00 58.30 ? 121 LYS A CD  1 
ATOM   1065 C CE  . LYS A 1 121 ? -26.439 35.046 98.432  1.00 59.96 ? 121 LYS A CE  1 
ATOM   1066 N NZ  . LYS A 1 121 ? -25.460 34.047 98.943  1.00 58.87 ? 121 LYS A NZ  1 
ATOM   1067 N N   . LEU A 1 122 ? -28.301 33.330 93.369  1.00 30.77 ? 122 LEU A N   1 
ATOM   1068 C CA  . LEU A 1 122 ? -29.036 32.490 92.432  1.00 24.73 ? 122 LEU A CA  1 
ATOM   1069 C C   . LEU A 1 122 ? -29.927 31.522 93.198  1.00 27.97 ? 122 LEU A C   1 
ATOM   1070 O O   . LEU A 1 122 ? -29.461 30.842 94.117  1.00 25.71 ? 122 LEU A O   1 
ATOM   1071 C CB  . LEU A 1 122 ? -28.074 31.718 91.524  1.00 24.57 ? 122 LEU A CB  1 
ATOM   1072 C CG  . LEU A 1 122 ? -27.112 32.600 90.726  1.00 27.45 ? 122 LEU A CG  1 
ATOM   1073 C CD1 . LEU A 1 122 ? -26.061 31.755 90.028  1.00 31.19 ? 122 LEU A CD1 1 
ATOM   1074 C CD2 . LEU A 1 122 ? -27.880 33.451 89.727  1.00 28.98 ? 122 LEU A CD2 1 
ATOM   1075 N N   . ASN A 1 123 ? -31.204 31.458 92.820  1.00 23.15 ? 123 ASN A N   1 
ATOM   1076 C CA  . ASN A 1 123 ? -32.100 30.468 93.396  1.00 17.97 ? 123 ASN A CA  1 
ATOM   1077 C C   . ASN A 1 123 ? -32.001 29.172 92.586  1.00 18.31 ? 123 ASN A C   1 
ATOM   1078 O O   . ASN A 1 123 ? -31.188 29.049 91.666  1.00 18.35 ? 123 ASN A O   1 
ATOM   1079 C CB  . ASN A 1 123 ? -33.529 31.005 93.466  1.00 26.84 ? 123 ASN A CB  1 
ATOM   1080 C CG  . ASN A 1 123 ? -34.090 31.398 92.106  1.00 27.83 ? 123 ASN A CG  1 
ATOM   1081 O OD1 . ASN A 1 123 ? -33.755 30.813 91.081  1.00 24.00 ? 123 ASN A OD1 1 
ATOM   1082 N ND2 . ASN A 1 123 ? -34.980 32.381 92.104  1.00 32.99 ? 123 ASN A ND2 1 
ATOM   1083 N N   . ARG A 1 124 ? -32.860 28.201 92.906  1.00 22.82 ? 124 ARG A N   1 
ATOM   1084 C CA  . ARG A 1 124 ? -32.746 26.886 92.282  1.00 18.39 ? 124 ARG A CA  1 
ATOM   1085 C C   . ARG A 1 124 ? -32.979 26.944 90.776  1.00 16.38 ? 124 ARG A C   1 
ATOM   1086 O O   . ARG A 1 124 ? -32.254 26.299 90.016  1.00 17.83 ? 124 ARG A O   1 
ATOM   1087 C CB  . ARG A 1 124 ? -33.729 25.909 92.924  1.00 16.29 ? 124 ARG A CB  1 
ATOM   1088 C CG  . ARG A 1 124 ? -33.676 24.522 92.300  1.00 22.34 ? 124 ARG A CG  1 
ATOM   1089 C CD  . ARG A 1 124 ? -34.691 23.578 92.955  1.00 20.13 ? 124 ARG A CD  1 
ATOM   1090 N NE  . ARG A 1 124 ? -34.702 22.300 92.252  1.00 22.17 ? 124 ARG A NE  1 
ATOM   1091 C CZ  . ARG A 1 124 ? -35.395 22.072 91.145  1.00 31.50 ? 124 ARG A CZ  1 
ATOM   1092 N NH1 . ARG A 1 124 ? -36.157 23.032 90.632  1.00 29.00 ? 124 ARG A NH1 1 
ATOM   1093 N NH2 . ARG A 1 124 ? -35.335 20.880 90.562  1.00 24.78 ? 124 ARG A NH2 1 
ATOM   1094 N N   . GLU A 1 125 ? -34.018 27.666 90.325  1.00 19.12 ? 125 GLU A N   1 
ATOM   1095 C CA  . GLU A 1 125 ? -34.261 27.761 88.879  1.00 18.68 ? 125 GLU A CA  1 
ATOM   1096 C C   . GLU A 1 125 ? -33.103 28.438 88.170  1.00 17.58 ? 125 GLU A C   1 
ATOM   1097 O O   . GLU A 1 125 ? -32.733 28.059 87.047  1.00 18.73 ? 125 GLU A O   1 
ATOM   1098 C CB  . GLU A 1 125 ? -35.532 28.557 88.565  1.00 23.93 ? 125 GLU A CB  1 
ATOM   1099 C CG  . GLU A 1 125 ? -36.832 28.030 89.094  1.00 40.53 ? 125 GLU A CG  1 
ATOM   1100 C CD  . GLU A 1 125 ? -37.995 28.832 88.542  1.00 59.59 ? 125 GLU A CD  1 
ATOM   1101 O OE1 . GLU A 1 125 ? -37.754 29.963 88.071  1.00 66.08 ? 125 GLU A OE1 1 
ATOM   1102 O OE2 . GLU A 1 125 ? -39.140 28.341 88.564  1.00 65.11 ? 125 GLU A OE2 1 
ATOM   1103 N N   . GLU A 1 126 ? -32.549 29.475 88.792  1.00 15.88 ? 126 GLU A N   1 
ATOM   1104 C CA  . GLU A 1 126 ? -31.438 30.191 88.185  1.00 15.81 ? 126 GLU A CA  1 
ATOM   1105 C C   . GLU A 1 126 ? -30.195 29.306 88.109  1.00 16.19 ? 126 GLU A C   1 
ATOM   1106 O O   . GLU A 1 126 ? -29.488 29.311 87.098  1.00 16.90 ? 126 GLU A O   1 
ATOM   1107 C CB  . GLU A 1 126 ? -31.180 31.488 88.968  1.00 16.40 ? 126 GLU A CB  1 
ATOM   1108 C CG  . GLU A 1 126 ? -32.192 32.579 88.618  1.00 17.71 ? 126 GLU A CG  1 
ATOM   1109 C CD  . GLU A 1 126 ? -32.405 33.611 89.714  1.00 27.39 ? 126 GLU A CD  1 
ATOM   1110 O OE1 . GLU A 1 126 ? -31.748 33.528 90.773  1.00 26.25 ? 126 GLU A OE1 1 
ATOM   1111 O OE2 . GLU A 1 126 ? -33.257 34.504 89.507  1.00 29.53 ? 126 GLU A OE2 1 
ATOM   1112 N N   . LEU A 1 127 ? -29.938 28.501 89.146  1.00 14.50 ? 127 LEU A N   1 
ATOM   1113 C CA  . LEU A 1 127 ? -28.819 27.558 89.088  1.00 14.25 ? 127 LEU A CA  1 
ATOM   1114 C C   . LEU A 1 127 ? -29.054 26.466 88.049  1.00 14.72 ? 127 LEU A C   1 
ATOM   1115 O O   . LEU A 1 127 ? -28.115 26.036 87.377  1.00 15.26 ? 127 LEU A O   1 
ATOM   1116 C CB  . LEU A 1 127 ? -28.586 26.935 90.464  1.00 18.81 ? 127 LEU A CB  1 
ATOM   1117 C CG  . LEU A 1 127 ? -27.972 27.878 91.496  1.00 21.60 ? 127 LEU A CG  1 
ATOM   1118 C CD1 . LEU A 1 127 ? -28.223 27.382 92.915  1.00 20.13 ? 127 LEU A CD1 1 
ATOM   1119 C CD2 . LEU A 1 127 ? -26.482 28.048 91.208  1.00 20.59 ? 127 LEU A CD2 1 
ATOM   1120 N N   . LEU A 1 128 ? -30.289 25.974 87.922  1.00 13.11 ? 128 LEU A N   1 
ATOM   1121 C CA  . LEU A 1 128 ? -30.559 24.997 86.870  1.00 13.61 ? 128 LEU A CA  1 
ATOM   1122 C C   . LEU A 1 128 ? -30.228 25.576 85.501  1.00 13.03 ? 128 LEU A C   1 
ATOM   1123 O O   . LEU A 1 128 ? -29.634 24.892 84.654  1.00 15.36 ? 128 LEU A O   1 
ATOM   1124 C CB  . LEU A 1 128 ? -32.022 24.547 86.906  1.00 13.64 ? 128 LEU A CB  1 
ATOM   1125 C CG  . LEU A 1 128 ? -32.365 23.264 87.650  1.00 18.55 ? 128 LEU A CG  1 
ATOM   1126 C CD1 . LEU A 1 128 ? -33.900 23.145 87.727  1.00 20.61 ? 128 LEU A CD1 1 
ATOM   1127 C CD2 . LEU A 1 128 ? -31.741 22.061 86.961  1.00 23.79 ? 128 LEU A CD2 1 
ATOM   1128 N N   . ASP A 1 129 ? -30.566 26.851 85.277  1.00 12.55 ? 129 ASP A N   1 
ATOM   1129 C CA  . ASP A 1 129 ? -30.215 27.485 84.008  1.00 12.45 ? 129 ASP A CA  1 
ATOM   1130 C C   . ASP A 1 129 ? -28.706 27.605 83.854  1.00 16.14 ? 129 ASP A C   1 
ATOM   1131 O O   . ASP A 1 129 ? -28.173 27.361 82.770  1.00 14.84 ? 129 ASP A O   1 
ATOM   1132 C CB  . ASP A 1 129 ? -30.877 28.858 83.885  1.00 13.32 ? 129 ASP A CB  1 
ATOM   1133 C CG  . ASP A 1 129 ? -32.323 28.764 83.479  1.00 17.65 ? 129 ASP A CG  1 
ATOM   1134 O OD1 . ASP A 1 129 ? -32.812 27.626 83.335  1.00 17.78 ? 129 ASP A OD1 1 
ATOM   1135 O OD2 . ASP A 1 129 ? -32.980 29.817 83.288  1.00 18.38 ? 129 ASP A OD2 1 
ATOM   1136 N N   . LEU A 1 130 ? -27.997 27.960 84.929  1.00 12.43 ? 130 LEU A N   1 
ATOM   1137 C CA  . LEU A 1 130 ? -26.543 28.073 84.837  1.00 12.30 ? 130 LEU A CA  1 
ATOM   1138 C C   . LEU A 1 130 ? -25.913 26.727 84.497  1.00 15.63 ? 130 LEU A C   1 
ATOM   1139 O O   . LEU A 1 130 ? -25.019 26.648 83.640  1.00 15.07 ? 130 LEU A O   1 
ATOM   1140 C CB  . LEU A 1 130 ? -25.987 28.634 86.148  1.00 13.02 ? 130 LEU A CB  1 
ATOM   1141 C CG  . LEU A 1 130 ? -24.516 29.062 86.180  1.00 17.44 ? 130 LEU A CG  1 
ATOM   1142 C CD1 . LEU A 1 130 ? -24.289 30.194 85.194  1.00 17.80 ? 130 LEU A CD1 1 
ATOM   1143 C CD2 . LEU A 1 130 ? -24.168 29.499 87.602  1.00 19.43 ? 130 LEU A CD2 1 
ATOM   1144 N N   . GLN A 1 131 ? -26.388 25.657 85.140  1.00 15.35 ? 131 GLN A N   1 
ATOM   1145 C CA  . GLN A 1 131 ? -25.881 24.320 84.850  1.00 12.50 ? 131 GLN A CA  1 
ATOM   1146 C C   . GLN A 1 131 ? -26.155 23.938 83.407  1.00 11.76 ? 131 GLN A C   1 
ATOM   1147 O O   . GLN A 1 131 ? -25.261 23.476 82.688  1.00 11.61 ? 131 GLN A O   1 
ATOM   1148 C CB  . GLN A 1 131 ? -26.535 23.293 85.772  1.00 10.80 ? 131 GLN A CB  1 
ATOM   1149 C CG  . GLN A 1 131 ? -26.194 23.415 87.218  1.00 12.57 ? 131 GLN A CG  1 
ATOM   1150 C CD  . GLN A 1 131 ? -27.080 22.524 88.057  1.00 14.58 ? 131 GLN A CD  1 
ATOM   1151 O OE1 . GLN A 1 131 ? -28.304 22.471 87.848  1.00 13.27 ? 131 GLN A OE1 1 
ATOM   1152 N NE2 . GLN A 1 131 ? -26.479 21.816 89.009  1.00 15.54 ? 131 GLN A NE2 1 
ATOM   1153 N N   . THR A 1 132 ? -27.408 24.077 82.983  1.00 12.56 ? 132 THR A N   1 
ATOM   1154 C CA  . THR A 1 132 ? -27.798 23.589 81.667  1.00 11.52 ? 132 THR A CA  1 
ATOM   1155 C C   . THR A 1 132 ? -27.193 24.438 80.562  1.00 13.24 ? 132 THR A C   1 
ATOM   1156 O O   . THR A 1 132 ? -26.818 23.915 79.508  1.00 10.63 ? 132 THR A O   1 
ATOM   1157 C CB  . THR A 1 132 ? -29.318 23.565 81.572  1.00 12.91 ? 132 THR A CB  1 
ATOM   1158 O OG1 . THR A 1 132 ? -29.827 22.840 82.701  1.00 12.45 ? 132 THR A OG1 1 
ATOM   1159 C CG2 . THR A 1 132 ? -29.780 22.862 80.305  1.00 13.55 ? 132 THR A CG2 1 
ATOM   1160 N N   . LEU A 1 133 ? -27.077 25.750 80.784  1.00 10.43 ? 133 LEU A N   1 
ATOM   1161 C CA  . LEU A 1 133 ? -26.455 26.598 79.769  1.00 12.55 ? 133 LEU A CA  1 
ATOM   1162 C C   . LEU A 1 133 ? -24.953 26.350 79.668  1.00 14.96 ? 133 LEU A C   1 
ATOM   1163 O O   . LEU A 1 133 ? -24.380 26.487 78.582  1.00 13.37 ? 133 LEU A O   1 
ATOM   1164 C CB  . LEU A 1 133 ? -26.726 28.072 80.053  1.00 12.32 ? 133 LEU A CB  1 
ATOM   1165 C CG  . LEU A 1 133 ? -28.159 28.459 79.683  1.00 16.65 ? 133 LEU A CG  1 
ATOM   1166 C CD1 . LEU A 1 133 ? -28.526 29.804 80.293  1.00 18.01 ? 133 LEU A CD1 1 
ATOM   1167 C CD2 . LEU A 1 133 ? -28.360 28.452 78.157  1.00 14.08 ? 133 LEU A CD2 1 
ATOM   1168 N N   . ASN A 1 134 ? -24.289 25.982 80.768  1.00 12.81 ? 134 ASN A N   1 
ATOM   1169 C CA  . ASN A 1 134 ? -22.893 25.579 80.633  1.00 11.86 ? 134 ASN A CA  1 
ATOM   1170 C C   . ASN A 1 134 ? -22.791 24.317 79.793  1.00 13.91 ? 134 ASN A C   1 
ATOM   1171 O O   . ASN A 1 134 ? -21.923 24.214 78.928  1.00 17.17 ? 134 ASN A O   1 
ATOM   1172 C CB  . ASN A 1 134 ? -22.253 25.384 82.005  1.00 11.98 ? 134 ASN A CB  1 
ATOM   1173 C CG  . ASN A 1 134 ? -21.591 26.636 82.500  1.00 14.80 ? 134 ASN A CG  1 
ATOM   1174 O OD1 . ASN A 1 134 ? -20.446 26.911 82.157  1.00 13.86 ? 134 ASN A OD1 1 
ATOM   1175 N ND2 . ASN A 1 134 ? -22.317 27.426 83.291  1.00 14.90 ? 134 ASN A ND2 1 
ATOM   1176 N N   . LEU A 1 135 ? -23.712 23.367 79.992  1.00 11.40 ? 135 LEU A N   1 
ATOM   1177 C CA  . LEU A 1 135 ? -23.736 22.182 79.136  1.00 10.60 ? 135 LEU A CA  1 
ATOM   1178 C C   . LEU A 1 135 ? -23.957 22.553 77.674  1.00 14.48 ? 135 LEU A C   1 
ATOM   1179 O O   . LEU A 1 135 ? -23.231 22.099 76.783  1.00 14.03 ? 135 LEU A O   1 
ATOM   1180 C CB  . LEU A 1 135 ? -24.847 21.225 79.573  1.00 16.48 ? 135 LEU A CB  1 
ATOM   1181 C CG  . LEU A 1 135 ? -24.597 20.047 80.497  1.00 23.18 ? 135 LEU A CG  1 
ATOM   1182 C CD1 . LEU A 1 135 ? -25.865 19.162 80.526  1.00 21.57 ? 135 LEU A CD1 1 
ATOM   1183 C CD2 . LEU A 1 135 ? -23.342 19.244 80.085  1.00 15.69 ? 135 LEU A CD2 1 
ATOM   1184 N N   . LEU A 1 136 ? -24.990 23.347 77.401  1.00 13.04 ? 136 LEU A N   1 
ATOM   1185 C CA  . LEU A 1 136 ? -25.371 23.625 76.020  1.00 10.40 ? 136 LEU A CA  1 
ATOM   1186 C C   . LEU A 1 136 ? -24.362 24.507 75.306  1.00 12.24 ? 136 LEU A C   1 
ATOM   1187 O O   . LEU A 1 136 ? -24.292 24.478 74.072  1.00 13.21 ? 136 LEU A O   1 
ATOM   1188 C CB  . LEU A 1 136 ? -26.747 24.275 75.982  1.00 13.59 ? 136 LEU A CB  1 
ATOM   1189 C CG  . LEU A 1 136 ? -27.901 23.327 76.291  1.00 16.03 ? 136 LEU A CG  1 
ATOM   1190 C CD1 . LEU A 1 136 ? -29.178 24.119 76.590  1.00 18.52 ? 136 LEU A CD1 1 
ATOM   1191 C CD2 . LEU A 1 136 ? -28.139 22.314 75.134  1.00 12.99 ? 136 LEU A CD2 1 
ATOM   1192 N N   . ALA A 1 137 ? -23.598 25.310 76.046  1.00 12.75 ? 137 ALA A N   1 
ATOM   1193 C CA  . ALA A 1 137 ? -22.566 26.134 75.412  1.00 11.86 ? 137 ALA A CA  1 
ATOM   1194 C C   . ALA A 1 137 ? -21.549 25.276 74.663  1.00 13.24 ? 137 ALA A C   1 
ATOM   1195 O O   . ALA A 1 137 ? -20.976 25.716 73.656  1.00 13.48 ? 137 ALA A O   1 
ATOM   1196 C CB  . ALA A 1 137 ? -21.869 27.007 76.468  1.00 12.72 ? 137 ALA A CB  1 
ATOM   1197 N N   . TRP A 1 138 ? -21.346 24.035 75.107  1.00 11.90 ? 138 TRP A N   1 
ATOM   1198 C CA  . TRP A 1 138 ? -20.390 23.130 74.483  1.00 12.97 ? 138 TRP A CA  1 
ATOM   1199 C C   . TRP A 1 138 ? -21.061 22.157 73.517  1.00 13.24 ? 138 TRP A C   1 
ATOM   1200 O O   . TRP A 1 138 ? -20.466 21.143 73.146  1.00 13.65 ? 138 TRP A O   1 
ATOM   1201 C CB  . TRP A 1 138 ? -19.598 22.381 75.563  1.00 11.62 ? 138 TRP A CB  1 
ATOM   1202 C CG  . TRP A 1 138 ? -18.796 23.333 76.391  1.00 11.07 ? 138 TRP A CG  1 
ATOM   1203 C CD1 . TRP A 1 138 ? -19.193 23.964 77.534  1.00 12.44 ? 138 TRP A CD1 1 
ATOM   1204 C CD2 . TRP A 1 138 ? -17.462 23.786 76.124  1.00 13.29 ? 138 TRP A CD2 1 
ATOM   1205 N NE1 . TRP A 1 138 ? -18.188 24.777 77.996  1.00 14.07 ? 138 TRP A NE1 1 
ATOM   1206 C CE2 . TRP A 1 138 ? -17.118 24.699 77.146  1.00 10.82 ? 138 TRP A CE2 1 
ATOM   1207 C CE3 . TRP A 1 138 ? -16.533 23.516 75.121  1.00 12.71 ? 138 TRP A CE3 1 
ATOM   1208 C CZ2 . TRP A 1 138 ? -15.869 25.338 77.202  1.00 12.08 ? 138 TRP A CZ2 1 
ATOM   1209 C CZ3 . TRP A 1 138 ? -15.291 24.161 75.168  1.00 12.18 ? 138 TRP A CZ3 1 
ATOM   1210 C CH2 . TRP A 1 138 ? -14.970 25.056 76.207  1.00 14.52 ? 138 TRP A CH2 1 
ATOM   1211 N N   . CYS A 1 139 ? -22.278 22.457 73.083  1.00 9.96  ? 139 CYS A N   1 
ATOM   1212 C CA  . CYS A 1 139 ? -22.979 21.553 72.184  1.00 10.08 ? 139 CYS A CA  1 
ATOM   1213 C C   . CYS A 1 139 ? -22.271 21.483 70.839  1.00 11.60 ? 139 CYS A C   1 
ATOM   1214 O O   . CYS A 1 139 ? -21.965 22.513 70.236  1.00 11.99 ? 139 CYS A O   1 
ATOM   1215 C CB  . CYS A 1 139 ? -24.415 22.024 71.973  1.00 10.84 ? 139 CYS A CB  1 
ATOM   1216 S SG  . CYS A 1 139 ? -25.520 20.796 71.216  1.00 15.37 ? 139 CYS A SG  1 
ATOM   1217 N N   . GLY A 1 140 ? -22.057 20.267 70.351  1.00 12.50 ? 140 GLY A N   1 
ATOM   1218 C CA  . GLY A 1 140 ? -21.474 20.074 69.041  1.00 12.76 ? 140 GLY A CA  1 
ATOM   1219 C C   . GLY A 1 140 ? -22.467 20.227 67.905  1.00 12.34 ? 140 GLY A C   1 
ATOM   1220 O O   . GLY A 1 140 ? -23.682 20.389 68.079  1.00 11.98 ? 140 GLY A O   1 
ATOM   1221 N N   . ARG A 1 141 ? -21.916 20.154 66.689  1.00 10.84 ? 141 ARG A N   1 
ATOM   1222 C CA  . ARG A 1 141 ? -22.697 20.434 65.485  1.00 12.15 ? 141 ARG A CA  1 
ATOM   1223 C C   . ARG A 1 141 ? -23.887 19.485 65.351  1.00 10.35 ? 141 ARG A C   1 
ATOM   1224 O O   . ARG A 1 141 ? -24.997 19.914 65.037  1.00 13.05 ? 141 ARG A O   1 
ATOM   1225 C CB  . ARG A 1 141 ? -21.787 20.332 64.260  1.00 11.69 ? 141 ARG A CB  1 
ATOM   1226 C CG  . ARG A 1 141 ? -22.499 20.413 62.910  1.00 13.15 ? 141 ARG A CG  1 
ATOM   1227 C CD  . ARG A 1 141 ? -21.462 20.489 61.796  1.00 15.31 ? 141 ARG A CD  1 
ATOM   1228 N NE  . ARG A 1 141 ? -22.028 20.411 60.462  1.00 18.57 ? 141 ARG A NE  1 
ATOM   1229 C CZ  . ARG A 1 141 ? -22.171 19.281 59.782  1.00 16.22 ? 141 ARG A CZ  1 
ATOM   1230 N NH1 . ARG A 1 141 ? -21.788 18.123 60.313  1.00 14.24 ? 141 ARG A NH1 1 
ATOM   1231 N NH2 . ARG A 1 141 ? -22.704 19.323 58.576  1.00 20.12 ? 141 ARG A NH2 1 
ATOM   1232 N N   . THR A 1 142 ? -23.668 18.196 65.604  1.00 12.48 ? 142 THR A N   1 
ATOM   1233 C CA  . THR A 1 142 ? -24.721 17.204 65.409  1.00 10.93 ? 142 THR A CA  1 
ATOM   1234 C C   . THR A 1 142 ? -25.914 17.501 66.304  1.00 12.28 ? 142 THR A C   1 
ATOM   1235 O O   . THR A 1 142 ? -27.063 17.560 65.846  1.00 16.67 ? 142 THR A O   1 
ATOM   1236 C CB  . THR A 1 142 ? -24.157 15.806 65.707  1.00 14.35 ? 142 THR A CB  1 
ATOM   1237 O OG1 . THR A 1 142 ? -23.102 15.495 64.783  1.00 15.21 ? 142 THR A OG1 1 
ATOM   1238 C CG2 . THR A 1 142 ? -25.261 14.752 65.586  1.00 15.16 ? 142 THR A CG2 1 
ATOM   1239 N N   . LEU A 1 143 ? -25.650 17.707 67.594  1.00 13.91 ? 143 LEU A N   1 
ATOM   1240 C CA  . LEU A 1 143 ? -26.728 17.946 68.528  1.00 14.65 ? 143 LEU A CA  1 
ATOM   1241 C C   . LEU A 1 143 ? -27.245 19.378 68.491  1.00 19.33 ? 143 LEU A C   1 
ATOM   1242 O O   . LEU A 1 143 ? -28.348 19.626 68.984  1.00 18.02 ? 143 LEU A O   1 
ATOM   1243 C CB  . LEU A 1 143 ? -26.278 17.579 69.939  1.00 13.37 ? 143 LEU A CB  1 
ATOM   1244 C CG  . LEU A 1 143 ? -26.110 16.066 70.135  1.00 10.89 ? 143 LEU A CG  1 
ATOM   1245 C CD1 . LEU A 1 143 ? -25.705 15.761 71.566  1.00 11.67 ? 143 LEU A CD1 1 
ATOM   1246 C CD2 . LEU A 1 143 ? -27.397 15.320 69.774  1.00 15.09 ? 143 LEU A CD2 1 
ATOM   1247 N N   . ARG A 1 144 ? -26.500 20.329 67.914  1.00 15.24 ? 144 ARG A N   1 
ATOM   1248 C CA  . ARG A 1 144 ? -27.095 21.650 67.726  1.00 19.12 ? 144 ARG A CA  1 
ATOM   1249 C C   . ARG A 1 144 ? -28.295 21.564 66.797  1.00 23.26 ? 144 ARG A C   1 
ATOM   1250 O O   . ARG A 1 144 ? -29.230 22.365 66.902  1.00 21.33 ? 144 ARG A O   1 
ATOM   1251 C CB  . ARG A 1 144 ? -26.056 22.644 67.197  1.00 17.97 ? 144 ARG A CB  1 
ATOM   1252 C CG  . ARG A 1 144 ? -25.190 23.278 68.306  1.00 23.96 ? 144 ARG A CG  1 
ATOM   1253 C CD  . ARG A 1 144 ? -24.013 24.052 67.721  1.00 20.11 ? 144 ARG A CD  1 
ATOM   1254 N NE  . ARG A 1 144 ? -23.224 24.764 68.723  1.00 18.89 ? 144 ARG A NE  1 
ATOM   1255 C CZ  . ARG A 1 144 ? -23.372 26.049 69.030  1.00 24.54 ? 144 ARG A CZ  1 
ATOM   1256 N NH1 . ARG A 1 144 ? -24.300 26.778 68.420  1.00 24.56 ? 144 ARG A NH1 1 
ATOM   1257 N NH2 . ARG A 1 144 ? -22.587 26.609 69.948  1.00 24.90 ? 144 ARG A NH2 1 
ATOM   1258 N N   . LYS A 1 145 ? -28.298 20.583 65.897  1.00 19.41 ? 145 LYS A N   1 
ATOM   1259 C CA  . LYS A 1 145 ? -29.474 20.332 65.073  1.00 26.83 ? 145 LYS A CA  1 
ATOM   1260 C C   . LYS A 1 145 ? -30.529 19.573 65.867  1.00 27.06 ? 145 LYS A C   1 
ATOM   1261 O O   . LYS A 1 145 ? -31.695 19.975 65.916  1.00 25.95 ? 145 LYS A O   1 
ATOM   1262 C CB  . LYS A 1 145 ? -29.100 19.548 63.809  1.00 32.83 ? 145 LYS A CB  1 
ATOM   1263 C CG  . LYS A 1 145 ? -27.872 20.016 62.984  1.00 49.03 ? 145 LYS A CG  1 
ATOM   1264 C CD  . LYS A 1 145 ? -27.423 21.456 63.245  1.00 58.40 ? 145 LYS A CD  1 
ATOM   1265 C CE  . LYS A 1 145 ? -25.971 21.675 62.824  1.00 57.58 ? 145 LYS A CE  1 
ATOM   1266 N NZ  . LYS A 1 145 ? -25.318 22.746 63.636  1.00 50.43 ? 145 LYS A NZ  1 
ATOM   1267 N N   . ASP A 1 146 ? -30.126 18.477 66.508  1.00 25.38 ? 146 ASP A N   1 
ATOM   1268 C CA  . ASP A 1 146 ? -31.088 17.595 67.160  1.00 22.09 ? 146 ASP A CA  1 
ATOM   1269 C C   . ASP A 1 146 ? -31.751 18.273 68.356  1.00 28.09 ? 146 ASP A C   1 
ATOM   1270 O O   . ASP A 1 146 ? -32.944 18.066 68.608  1.00 26.57 ? 146 ASP A O   1 
ATOM   1271 C CB  . ASP A 1 146 ? -30.390 16.303 67.584  1.00 22.74 ? 146 ASP A CB  1 
ATOM   1272 C CG  . ASP A 1 146 ? -29.792 15.544 66.404  1.00 29.19 ? 146 ASP A CG  1 
ATOM   1273 O OD1 . ASP A 1 146 ? -30.125 15.865 65.245  1.00 33.46 ? 146 ASP A OD1 1 
ATOM   1274 O OD2 . ASP A 1 146 ? -28.985 14.621 66.634  1.00 36.04 ? 146 ASP A OD2 1 
ATOM   1275 N N   . LEU A 1 147 ? -31.002 19.103 69.087  1.00 21.19 ? 147 LEU A N   1 
ATOM   1276 C CA  . LEU A 1 147 ? -31.473 19.782 70.290  1.00 19.98 ? 147 LEU A CA  1 
ATOM   1277 C C   . LEU A 1 147 ? -31.817 21.247 70.042  1.00 21.70 ? 147 LEU A C   1 
ATOM   1278 O O   . LEU A 1 147 ? -31.816 22.042 70.987  1.00 21.01 ? 147 LEU A O   1 
ATOM   1279 C CB  . LEU A 1 147 ? -30.426 19.691 71.404  1.00 23.09 ? 147 LEU A CB  1 
ATOM   1280 C CG  . LEU A 1 147 ? -29.845 18.323 71.756  1.00 23.07 ? 147 LEU A CG  1 
ATOM   1281 C CD1 . LEU A 1 147 ? -28.771 18.452 72.807  1.00 25.35 ? 147 LEU A CD1 1 
ATOM   1282 C CD2 . LEU A 1 147 ? -30.948 17.390 72.225  1.00 37.73 ? 147 LEU A CD2 1 
ATOM   1283 N N   . LYS A 1 148 ? -32.123 21.618 68.800  1.00 19.47 ? 148 LYS A N   1 
ATOM   1284 C CA  . LYS A 1 148 ? -32.255 23.036 68.471  1.00 21.13 ? 148 LYS A CA  1 
ATOM   1285 C C   . LYS A 1 148 ? -33.335 23.721 69.306  1.00 25.92 ? 148 LYS A C   1 
ATOM   1286 O O   . LYS A 1 148 ? -33.176 24.887 69.689  1.00 24.87 ? 148 LYS A O   1 
ATOM   1287 C CB  . LYS A 1 148 ? -32.541 23.211 66.976  1.00 24.33 ? 148 LYS A CB  1 
ATOM   1288 C CG  . LYS A 1 148 ? -33.917 22.733 66.533  1.00 29.83 ? 148 LYS A CG  1 
ATOM   1289 C CD  . LYS A 1 148 ? -34.630 23.796 65.702  1.00 45.43 ? 148 LYS A CD  1 
ATOM   1290 C CE  . LYS A 1 148 ? -33.777 24.265 64.534  1.00 46.35 ? 148 LYS A CE  1 
ATOM   1291 N NZ  . LYS A 1 148 ? -34.538 25.151 63.612  1.00 53.77 ? 148 LYS A NZ  1 
ATOM   1292 N N   . ASP A 1 149 ? -34.429 23.017 69.614  1.00 21.91 ? 149 ASP A N   1 
ATOM   1293 C CA  . ASP A 1 149 ? -35.515 23.655 70.356  1.00 29.25 ? 149 ASP A CA  1 
ATOM   1294 C C   . ASP A 1 149 ? -35.094 23.979 71.783  1.00 26.02 ? 149 ASP A C   1 
ATOM   1295 O O   . ASP A 1 149 ? -35.433 25.047 72.305  1.00 23.44 ? 149 ASP A O   1 
ATOM   1296 C CB  . ASP A 1 149 ? -36.756 22.764 70.372  1.00 29.43 ? 149 ASP A CB  1 
ATOM   1297 C CG  . ASP A 1 149 ? -37.256 22.434 68.984  1.00 36.00 ? 149 ASP A CG  1 
ATOM   1298 O OD1 . ASP A 1 149 ? -37.220 23.322 68.103  1.00 33.23 ? 149 ASP A OD1 1 
ATOM   1299 O OD2 . ASP A 1 149 ? -37.684 21.278 68.787  1.00 43.54 ? 149 ASP A OD2 1 
ATOM   1300 N N   . LEU A 1 150 ? -34.369 23.066 72.435  1.00 24.70 ? 150 LEU A N   1 
ATOM   1301 C CA  . LEU A 1 150 ? -33.891 23.349 73.782  1.00 22.31 ? 150 LEU A CA  1 
ATOM   1302 C C   . LEU A 1 150 ? -32.848 24.456 73.764  1.00 18.07 ? 150 LEU A C   1 
ATOM   1303 O O   . LEU A 1 150 ? -32.786 25.274 74.683  1.00 19.98 ? 150 LEU A O   1 
ATOM   1304 C CB  . LEU A 1 150 ? -33.309 22.089 74.429  1.00 22.97 ? 150 LEU A CB  1 
ATOM   1305 C CG  . LEU A 1 150 ? -34.312 21.006 74.822  1.00 26.70 ? 150 LEU A CG  1 
ATOM   1306 C CD1 . LEU A 1 150 ? -33.594 19.820 75.445  1.00 24.03 ? 150 LEU A CD1 1 
ATOM   1307 C CD2 . LEU A 1 150 ? -35.367 21.553 75.769  1.00 29.01 ? 150 LEU A CD2 1 
ATOM   1308 N N   . LEU A 1 151 ? -32.009 24.486 72.729  1.00 20.94 ? 151 LEU A N   1 
ATOM   1309 C CA  . LEU A 1 151 ? -31.012 25.548 72.615  1.00 22.05 ? 151 LEU A CA  1 
ATOM   1310 C C   . LEU A 1 151 ? -31.672 26.911 72.478  1.00 27.91 ? 151 LEU A C   1 
ATOM   1311 O O   . LEU A 1 151 ? -31.217 27.893 73.077  1.00 22.53 ? 151 LEU A O   1 
ATOM   1312 C CB  . LEU A 1 151 ? -30.107 25.279 71.413  1.00 26.88 ? 151 LEU A CB  1 
ATOM   1313 C CG  . LEU A 1 151 ? -28.889 24.408 71.670  1.00 31.07 ? 151 LEU A CG  1 
ATOM   1314 C CD1 . LEU A 1 151 ? -28.300 23.928 70.348  1.00 33.80 ? 151 LEU A CD1 1 
ATOM   1315 C CD2 . LEU A 1 151 ? -27.855 25.193 72.469  1.00 29.20 ? 151 LEU A CD2 1 
ATOM   1316 N N   . ASN A 1 152 ? -32.753 26.987 71.695  1.00 27.18 ? 152 ASN A N   1 
ATOM   1317 C CA  . ASN A 1 152 ? -33.441 28.251 71.457  1.00 23.32 ? 152 ASN A CA  1 
ATOM   1318 C C   . ASN A 1 152 ? -34.261 28.716 72.651  1.00 23.63 ? 152 ASN A C   1 
ATOM   1319 O O   . ASN A 1 152 ? -34.613 29.900 72.713  1.00 25.76 ? 152 ASN A O   1 
ATOM   1320 C CB  . ASN A 1 152 ? -34.364 28.132 70.241  1.00 33.76 ? 152 ASN A CB  1 
ATOM   1321 C CG  . ASN A 1 152 ? -33.612 28.194 68.935  1.00 42.43 ? 152 ASN A CG  1 
ATOM   1322 O OD1 . ASN A 1 152 ? -32.389 28.313 68.916  1.00 46.83 ? 152 ASN A OD1 1 
ATOM   1323 N ND2 . ASN A 1 152 ? -34.341 28.113 67.829  1.00 47.66 ? 152 ASN A ND2 1 
ATOM   1324 N N   . LYS A 1 153 ? -34.622 27.808 73.563  1.00 21.51 ? 153 LYS A N   1 
ATOM   1325 C CA  . LYS A 1 153 ? -35.198 28.235 74.833  1.00 26.45 ? 153 LYS A CA  1 
ATOM   1326 C C   . LYS A 1 153 ? -34.312 29.281 75.484  1.00 28.80 ? 153 LYS A C   1 
ATOM   1327 O O   . LYS A 1 153 ? -34.768 30.373 75.846  1.00 28.04 ? 153 LYS A O   1 
ATOM   1328 C CB  . LYS A 1 153 ? -35.339 27.048 75.780  1.00 26.84 ? 153 LYS A CB  1 
ATOM   1329 C CG  . LYS A 1 153 ? -36.481 26.122 75.519  1.00 27.31 ? 153 LYS A CG  1 
ATOM   1330 C CD  . LYS A 1 153 ? -36.408 24.946 76.490  1.00 32.79 ? 153 LYS A CD  1 
ATOM   1331 C CE  . LYS A 1 153 ? -36.125 25.399 77.915  1.00 26.79 ? 153 LYS A CE  1 
ATOM   1332 N NZ  . LYS A 1 153 ? -37.297 25.934 78.651  1.00 28.54 ? 153 LYS A NZ  1 
ATOM   1333 N N   . GLY A 1 154 ? -33.037 28.938 75.658  1.00 23.09 ? 154 GLY A N   1 
ATOM   1334 C CA  . GLY A 1 154 ? -32.035 29.802 76.240  1.00 24.14 ? 154 GLY A CA  1 
ATOM   1335 C C   . GLY A 1 154 ? -32.205 30.082 77.711  1.00 22.31 ? 154 GLY A C   1 
ATOM   1336 O O   . GLY A 1 154 ? -31.381 30.800 78.277  1.00 19.92 ? 154 GLY A O   1 
ATOM   1337 N N   . ARG A 1 155 ? -33.226 29.526 78.352  1.00 16.80 ? 155 ARG A N   1 
ATOM   1338 C CA  . ARG A 1 155 ? -33.550 29.817 79.744  1.00 17.72 ? 155 ARG A CA  1 
ATOM   1339 C C   . ARG A 1 155 ? -34.619 28.837 80.205  1.00 18.43 ? 155 ARG A C   1 
ATOM   1340 O O   . ARG A 1 155 ? -35.173 28.075 79.409  1.00 21.03 ? 155 ARG A O   1 
ATOM   1341 C CB  . ARG A 1 155 ? -34.061 31.250 79.912  1.00 22.23 ? 155 ARG A CB  1 
ATOM   1342 C CG  . ARG A 1 155 ? -35.371 31.500 79.207  1.00 27.28 ? 155 ARG A CG  1 
ATOM   1343 C CD  . ARG A 1 155 ? -35.813 32.937 79.363  1.00 32.17 ? 155 ARG A CD  1 
ATOM   1344 N NE  . ARG A 1 155 ? -34.844 33.848 78.761  1.00 32.90 ? 155 ARG A NE  1 
ATOM   1345 C CZ  . ARG A 1 155 ? -34.160 34.764 79.439  1.00 32.81 ? 155 ARG A CZ  1 
ATOM   1346 N NH1 . ARG A 1 155 ? -33.293 35.546 78.809  1.00 38.75 ? 155 ARG A NH1 1 
ATOM   1347 N NH2 . ARG A 1 155 ? -34.350 34.907 80.743  1.00 30.67 ? 155 ARG A NH2 1 
ATOM   1348 N N   . ASN A 1 156 ? -34.906 28.879 81.507  1.00 19.16 ? 156 ASN A N   1 
ATOM   1349 C CA  . ASN A 1 156 ? -36.041 28.169 82.110  1.00 19.26 ? 156 ASN A CA  1 
ATOM   1350 C C   . ASN A 1 156 ? -35.941 26.651 81.935  1.00 17.55 ? 156 ASN A C   1 
ATOM   1351 O O   . ASN A 1 156 ? -36.931 25.976 81.624  1.00 21.61 ? 156 ASN A O   1 
ATOM   1352 C CB  . ASN A 1 156 ? -37.374 28.670 81.538  1.00 25.86 ? 156 ASN A CB  1 
ATOM   1353 C CG  . ASN A 1 156 ? -37.570 30.159 81.710  1.00 29.92 ? 156 ASN A CG  1 
ATOM   1354 O OD1 . ASN A 1 156 ? -37.138 30.741 82.701  1.00 31.13 ? 156 ASN A OD1 1 
ATOM   1355 N ND2 . ASN A 1 156 ? -38.259 30.779 80.754  1.00 26.39 ? 156 ASN A ND2 1 
ATOM   1356 N N   . TYR A 1 157 ? -34.752 26.108 82.162  1.00 13.51 ? 157 TYR A N   1 
ATOM   1357 C CA  . TYR A 1 157 ? -34.527 24.681 81.975  1.00 15.76 ? 157 TYR A CA  1 
ATOM   1358 C C   . TYR A 1 157 ? -34.958 23.898 83.206  1.00 15.37 ? 157 TYR A C   1 
ATOM   1359 O O   . TYR A 1 157 ? -34.875 24.378 84.338  1.00 17.60 ? 157 TYR A O   1 
ATOM   1360 C CB  . TYR A 1 157 ? -33.047 24.399 81.682  1.00 13.65 ? 157 TYR A CB  1 
ATOM   1361 C CG  . TYR A 1 157 ? -32.633 24.947 80.342  1.00 12.02 ? 157 TYR A CG  1 
ATOM   1362 C CD1 . TYR A 1 157 ? -33.040 24.324 79.171  1.00 13.53 ? 157 TYR A CD1 1 
ATOM   1363 C CD2 . TYR A 1 157 ? -31.881 26.104 80.245  1.00 12.08 ? 157 TYR A CD2 1 
ATOM   1364 C CE1 . TYR A 1 157 ? -32.693 24.835 77.929  1.00 14.81 ? 157 TYR A CE1 1 
ATOM   1365 C CE2 . TYR A 1 157 ? -31.520 26.619 79.006  1.00 12.52 ? 157 TYR A CE2 1 
ATOM   1366 C CZ  . TYR A 1 157 ? -31.927 25.978 77.865  1.00 14.74 ? 157 TYR A CZ  1 
ATOM   1367 O OH  . TYR A 1 157 ? -31.592 26.478 76.634  1.00 15.28 ? 157 TYR A OH  1 
ATOM   1368 N N   . THR A 1 158 ? -35.411 22.674 82.977  1.00 13.06 ? 158 THR A N   1 
ATOM   1369 C CA  . THR A 1 158 ? -35.766 21.771 84.063  1.00 13.27 ? 158 THR A CA  1 
ATOM   1370 C C   . THR A 1 158 ? -34.692 20.704 84.219  1.00 12.69 ? 158 THR A C   1 
ATOM   1371 O O   . THR A 1 158 ? -33.883 20.470 83.323  1.00 14.21 ? 158 THR A O   1 
ATOM   1372 C CB  . THR A 1 158 ? -37.120 21.094 83.810  1.00 14.07 ? 158 THR A CB  1 
ATOM   1373 O OG1 . THR A 1 158 ? -36.997 20.188 82.703  1.00 15.90 ? 158 THR A OG1 1 
ATOM   1374 C CG2 . THR A 1 158 ? -38.198 22.122 83.509  1.00 16.14 ? 158 THR A CG2 1 
ATOM   1375 N N   . GLN A 1 159 ? -34.709 20.036 85.376  1.00 12.89 ? 159 GLN A N   1 
ATOM   1376 C CA  . GLN A 1 159 ? -33.782 18.933 85.610  1.00 12.56 ? 159 GLN A CA  1 
ATOM   1377 C C   . GLN A 1 159 ? -33.934 17.850 84.543  1.00 12.54 ? 159 GLN A C   1 
ATOM   1378 O O   . GLN A 1 159 ? -32.938 17.295 84.060  1.00 13.79 ? 159 GLN A O   1 
ATOM   1379 C CB  . GLN A 1 159 ? -34.006 18.362 87.011  1.00 13.77 ? 159 GLN A CB  1 
ATOM   1380 C CG  . GLN A 1 159 ? -33.122 17.175 87.360  1.00 16.48 ? 159 GLN A CG  1 
ATOM   1381 C CD  . GLN A 1 159 ? -31.694 17.577 87.642  1.00 19.62 ? 159 GLN A CD  1 
ATOM   1382 O OE1 . GLN A 1 159 ? -31.415 18.739 87.928  1.00 17.83 ? 159 GLN A OE1 1 
ATOM   1383 N NE2 . GLN A 1 159 ? -30.784 16.615 87.585  1.00 20.14 ? 159 GLN A NE2 1 
ATOM   1384 N N   . GLU A 1 160 ? -35.172 17.557 84.150  1.00 13.20 ? 160 GLU A N   1 
ATOM   1385 C CA  . GLU A 1 160 ? -35.411 16.555 83.119  1.00 13.42 ? 160 GLU A CA  1 
ATOM   1386 C C   . GLU A 1 160 ? -34.759 16.958 81.800  1.00 13.67 ? 160 GLU A C   1 
ATOM   1387 O O   . GLU A 1 160 ? -34.130 16.128 81.125  1.00 18.56 ? 160 GLU A O   1 
ATOM   1388 C CB  . GLU A 1 160 ? -36.919 16.364 82.962  1.00 17.55 ? 160 GLU A CB  1 
ATOM   1389 C CG  . GLU A 1 160 ? -37.297 15.291 81.978  1.00 25.74 ? 160 GLU A CG  1 
ATOM   1390 C CD  . GLU A 1 160 ? -37.291 15.802 80.544  1.00 49.70 ? 160 GLU A CD  1 
ATOM   1391 O OE1 . GLU A 1 160 ? -37.020 14.995 79.633  1.00 52.75 ? 160 GLU A OE1 1 
ATOM   1392 O OE2 . GLU A 1 160 ? -37.541 17.010 80.362  1.00 56.61 ? 160 GLU A OE2 1 
ATOM   1393 N N   . GLU A 1 161 ? -34.881 18.230 81.421  1.00 12.64 ? 161 GLU A N   1 
ATOM   1394 C CA  . GLU A 1 161 ? -34.250 18.684 80.187  1.00 13.03 ? 161 GLU A CA  1 
ATOM   1395 C C   . GLU A 1 161 ? -32.736 18.610 80.284  1.00 12.24 ? 161 GLU A C   1 
ATOM   1396 O O   . GLU A 1 161 ? -32.066 18.200 79.329  1.00 13.54 ? 161 GLU A O   1 
ATOM   1397 C CB  . GLU A 1 161 ? -34.705 20.108 79.848  1.00 12.42 ? 161 GLU A CB  1 
ATOM   1398 C CG  . GLU A 1 161 ? -36.153 20.138 79.450  1.00 13.53 ? 161 GLU A CG  1 
ATOM   1399 C CD  . GLU A 1 161 ? -36.725 21.512 79.427  1.00 21.51 ? 161 GLU A CD  1 
ATOM   1400 O OE1 . GLU A 1 161 ? -36.080 22.462 79.913  1.00 17.52 ? 161 GLU A OE1 1 
ATOM   1401 O OE2 . GLU A 1 161 ? -37.854 21.634 78.915  1.00 22.82 ? 161 GLU A OE2 1 
ATOM   1402 N N   . LYS A 1 162 ? -32.179 19.013 81.431  1.00 11.08 ? 162 LYS A N   1 
ATOM   1403 C CA  . LYS A 1 162 ? -30.736 18.911 81.632  1.00 10.45 ? 162 LYS A CA  1 
ATOM   1404 C C   . LYS A 1 162 ? -30.273 17.471 81.494  1.00 13.48 ? 162 LYS A C   1 
ATOM   1405 O O   . LYS A 1 162 ? -29.265 17.191 80.832  1.00 12.83 ? 162 LYS A O   1 
ATOM   1406 C CB  . LYS A 1 162 ? -30.372 19.465 83.012  1.00 10.52 ? 162 LYS A CB  1 
ATOM   1407 C CG  . LYS A 1 162 ? -28.864 19.481 83.299  1.00 10.08 ? 162 LYS A CG  1 
ATOM   1408 C CD  . LYS A 1 162 ? -28.550 20.071 84.672  1.00 18.39 ? 162 LYS A CD  1 
ATOM   1409 C CE  . LYS A 1 162 ? -29.297 19.341 85.744  1.00 20.27 ? 162 LYS A CE  1 
ATOM   1410 N NZ  . LYS A 1 162 ? -28.868 19.735 87.131  1.00 15.40 ? 162 LYS A NZ  1 
ATOM   1411 N N   . GLU A 1 163 ? -31.001 16.541 82.127  1.00 12.58 ? 163 GLU A N   1 
ATOM   1412 C CA  . GLU A 1 163 ? -30.618 15.138 82.063  1.00 17.37 ? 163 GLU A CA  1 
ATOM   1413 C C   . GLU A 1 163 ? -30.748 14.602 80.645  1.00 18.15 ? 163 GLU A C   1 
ATOM   1414 O O   . GLU A 1 163 ? -29.953 13.755 80.225  1.00 14.61 ? 163 GLU A O   1 
ATOM   1415 C CB  . GLU A 1 163 ? -31.459 14.311 83.033  1.00 18.55 ? 163 GLU A CB  1 
ATOM   1416 C CG  . GLU A 1 163 ? -31.134 14.612 84.487  1.00 16.66 ? 163 GLU A CG  1 
ATOM   1417 C CD  . GLU A 1 163 ? -31.964 13.813 85.462  1.00 23.17 ? 163 GLU A CD  1 
ATOM   1418 O OE1 . GLU A 1 163 ? -31.808 14.028 86.687  1.00 28.72 ? 163 GLU A OE1 1 
ATOM   1419 O OE2 . GLU A 1 163 ? -32.779 12.980 85.009  1.00 29.55 ? 163 GLU A OE2 1 
ATOM   1420 N N   . TYR A 1 164 ? -31.751 15.072 79.901  1.00 17.57 ? 164 TYR A N   1 
ATOM   1421 C CA  . TYR A 1 164 ? -31.881 14.670 78.502  1.00 19.94 ? 164 TYR A CA  1 
ATOM   1422 C C   . TYR A 1 164 ? -30.651 15.078 77.700  1.00 20.32 ? 164 TYR A C   1 
ATOM   1423 O O   . TYR A 1 164 ? -30.080 14.270 76.955  1.00 14.12 ? 164 TYR A O   1 
ATOM   1424 C CB  . TYR A 1 164 ? -33.141 15.286 77.899  1.00 16.30 ? 164 TYR A CB  1 
ATOM   1425 C CG  . TYR A 1 164 ? -33.388 14.882 76.467  1.00 20.43 ? 164 TYR A CG  1 
ATOM   1426 C CD1 . TYR A 1 164 ? -33.978 13.665 76.163  1.00 25.23 ? 164 TYR A CD1 1 
ATOM   1427 C CD2 . TYR A 1 164 ? -33.046 15.725 75.422  1.00 22.25 ? 164 TYR A CD2 1 
ATOM   1428 C CE1 . TYR A 1 164 ? -34.201 13.292 74.851  1.00 27.17 ? 164 TYR A CE1 1 
ATOM   1429 C CE2 . TYR A 1 164 ? -33.266 15.360 74.107  1.00 18.98 ? 164 TYR A CE2 1 
ATOM   1430 C CZ  . TYR A 1 164 ? -33.841 14.146 73.829  1.00 24.66 ? 164 TYR A CZ  1 
ATOM   1431 O OH  . TYR A 1 164 ? -34.070 13.781 72.520  1.00 29.72 ? 164 TYR A OH  1 
ATOM   1432 N N   . VAL A 1 165 ? -30.226 16.335 77.842  1.00 14.36 ? 165 VAL A N   1 
ATOM   1433 C CA  . VAL A 1 165 ? -29.018 16.803 77.160  1.00 14.11 ? 165 VAL A CA  1 
ATOM   1434 C C   . VAL A 1 165 ? -27.806 15.961 77.561  1.00 13.62 ? 165 VAL A C   1 
ATOM   1435 O O   . VAL A 1 165 ? -27.012 15.547 76.714  1.00 13.28 ? 165 VAL A O   1 
ATOM   1436 C CB  . VAL A 1 165 ? -28.796 18.297 77.452  1.00 12.45 ? 165 VAL A CB  1 
ATOM   1437 C CG1 . VAL A 1 165 ? -27.433 18.775 76.930  1.00 13.04 ? 165 VAL A CG1 1 
ATOM   1438 C CG2 . VAL A 1 165 ? -29.933 19.126 76.867  1.00 12.83 ? 165 VAL A CG2 1 
ATOM   1439 N N   . LEU A 1 166 ? -27.643 15.704 78.864  1.00 12.21 ? 166 LEU A N   1 
ATOM   1440 C CA  . LEU A 1 166 ? -26.528 14.887 79.333  1.00 10.93 ? 166 LEU A CA  1 
ATOM   1441 C C   . LEU A 1 166 ? -26.551 13.511 78.685  1.00 13.55 ? 166 LEU A C   1 
ATOM   1442 O O   . LEU A 1 166 ? -25.512 12.991 78.266  1.00 11.71 ? 166 LEU A O   1 
ATOM   1443 C CB  . LEU A 1 166 ? -26.588 14.738 80.848  1.00 10.87 ? 166 LEU A CB  1 
ATOM   1444 C CG  . LEU A 1 166 ? -25.966 15.846 81.669  1.00 16.97 ? 166 LEU A CG  1 
ATOM   1445 C CD1 . LEU A 1 166 ? -26.334 15.674 83.150  1.00 23.94 ? 166 LEU A CD1 1 
ATOM   1446 C CD2 . LEU A 1 166 ? -24.442 15.857 81.478  1.00 24.41 ? 166 LEU A CD2 1 
ATOM   1447 N N   . ASN A 1 167 ? -27.731 12.917 78.575  1.00 11.52 ? 167 ASN A N   1 
ATOM   1448 C CA  . ASN A 1 167 ? -27.818 11.585 77.983  1.00 11.52 ? 167 ASN A CA  1 
ATOM   1449 C C   . ASN A 1 167 ? -27.439 11.618 76.512  1.00 12.09 ? 167 ASN A C   1 
ATOM   1450 O O   . ASN A 1 167 ? -26.733 10.721 76.023  1.00 15.50 ? 167 ASN A O   1 
ATOM   1451 C CB  . ASN A 1 167 ? -29.234 11.029 78.158  1.00 13.79 ? 167 ASN A CB  1 
ATOM   1452 C CG  . ASN A 1 167 ? -29.500 10.556 79.574  1.00 29.89 ? 167 ASN A CG  1 
ATOM   1453 O OD1 . ASN A 1 167 ? -28.570 10.243 80.319  1.00 38.87 ? 167 ASN A OD1 1 
ATOM   1454 N ND2 . ASN A 1 167 ? -30.775 10.489 79.951  1.00 34.91 ? 167 ASN A ND2 1 
ATOM   1455 N N   . LYS A 1 168 ? -27.865 12.664 75.795  1.00 13.01 ? 168 LYS A N   1 
ATOM   1456 C CA  . LYS A 1 168 ? -27.489 12.771 74.389  1.00 10.12 ? 168 LYS A CA  1 
ATOM   1457 C C   . LYS A 1 168 ? -25.993 13.008 74.252  1.00 12.62 ? 168 LYS A C   1 
ATOM   1458 O O   . LYS A 1 168 ? -25.362 12.494 73.324  1.00 13.52 ? 168 LYS A O   1 
ATOM   1459 C CB  . LYS A 1 168 ? -28.250 13.906 73.696  1.00 11.12 ? 168 LYS A CB  1 
ATOM   1460 C CG  . LYS A 1 168 ? -29.768 13.721 73.607  1.00 15.97 ? 168 LYS A CG  1 
ATOM   1461 C CD  . LYS A 1 168 ? -30.157 12.415 72.938  1.00 21.67 ? 168 LYS A CD  1 
ATOM   1462 C CE  . LYS A 1 168 ? -29.938 12.465 71.445  1.00 32.41 ? 168 LYS A CE  1 
ATOM   1463 N NZ  . LYS A 1 168 ? -30.583 11.284 70.790  1.00 40.20 ? 168 LYS A NZ  1 
ATOM   1464 N N   . TYR A 1 169 ? -25.417 13.780 75.171  1.00 10.66 ? 169 TYR A N   1 
ATOM   1465 C CA  . TYR A 1 169 ? -23.983 14.046 75.125  1.00 11.22 ? 169 TYR A CA  1 
ATOM   1466 C C   . TYR A 1 169 ? -23.186 12.760 75.303  1.00 10.08 ? 169 TYR A C   1 
ATOM   1467 O O   . TYR A 1 169 ? -22.197 12.537 74.594  1.00 11.86 ? 169 TYR A O   1 
ATOM   1468 C CB  . TYR A 1 169 ? -23.597 15.066 76.198  1.00 9.39  ? 169 TYR A CB  1 
ATOM   1469 C CG  . TYR A 1 169 ? -23.814 16.520 75.825  1.00 10.50 ? 169 TYR A CG  1 
ATOM   1470 C CD1 . TYR A 1 169 ? -24.611 16.875 74.753  1.00 12.79 ? 169 TYR A CD1 1 
ATOM   1471 C CD2 . TYR A 1 169 ? -23.190 17.538 76.555  1.00 10.28 ? 169 TYR A CD2 1 
ATOM   1472 C CE1 . TYR A 1 169 ? -24.801 18.211 74.419  1.00 13.28 ? 169 TYR A CE1 1 
ATOM   1473 C CE2 . TYR A 1 169 ? -23.372 18.867 76.235  1.00 13.00 ? 169 TYR A CE2 1 
ATOM   1474 C CZ  . TYR A 1 169 ? -24.182 19.198 75.180  1.00 13.01 ? 169 TYR A CZ  1 
ATOM   1475 O OH  . TYR A 1 169 ? -24.366 20.523 74.860  1.00 12.71 ? 169 TYR A OH  1 
ATOM   1476 N N   . PHE A 1 170 ? -23.602 11.901 76.242  1.00 14.11 ? 170 PHE A N   1 
ATOM   1477 C CA  . PHE A 1 170 ? -22.888 10.643 76.436  1.00 14.41 ? 170 PHE A CA  1 
ATOM   1478 C C   . PHE A 1 170 ? -23.081 9.692  75.259  1.00 15.47 ? 170 PHE A C   1 
ATOM   1479 O O   . PHE A 1 170 ? -22.165 8.923  74.936  1.00 11.68 ? 170 PHE A O   1 
ATOM   1480 C CB  . PHE A 1 170 ? -23.309 10.005 77.764  1.00 14.44 ? 170 PHE A CB  1 
ATOM   1481 C CG  . PHE A 1 170 ? -22.496 10.506 78.923  1.00 16.38 ? 170 PHE A CG  1 
ATOM   1482 C CD1 . PHE A 1 170 ? -21.212 10.028 79.135  1.00 19.34 ? 170 PHE A CD1 1 
ATOM   1483 C CD2 . PHE A 1 170 ? -22.986 11.492 79.760  1.00 19.71 ? 170 PHE A CD2 1 
ATOM   1484 C CE1 . PHE A 1 170 ? -20.436 10.509 80.180  1.00 20.78 ? 170 PHE A CE1 1 
ATOM   1485 C CE2 . PHE A 1 170 ? -22.216 11.980 80.809  1.00 16.93 ? 170 PHE A CE2 1 
ATOM   1486 C CZ  . PHE A 1 170 ? -20.943 11.479 81.027  1.00 19.53 ? 170 PHE A CZ  1 
ATOM   1487 N N   . GLU A 1 171 ? -24.244 9.739  74.599  1.00 13.16 ? 171 GLU A N   1 
ATOM   1488 C CA  . GLU A 1 171 ? -24.406 9.016  73.338  1.00 15.55 ? 171 GLU A CA  1 
ATOM   1489 C C   . GLU A 1 171 ? -23.342 9.423  72.325  1.00 15.85 ? 171 GLU A C   1 
ATOM   1490 O O   . GLU A 1 171 ? -22.763 8.558  71.652  1.00 14.23 ? 171 GLU A O   1 
ATOM   1491 C CB  . GLU A 1 171 ? -25.806 9.250  72.757  1.00 20.73 ? 171 GLU A CB  1 
ATOM   1492 C CG  . GLU A 1 171 ? -26.926 8.590  73.546  1.00 27.82 ? 171 GLU A CG  1 
ATOM   1493 C CD  . GLU A 1 171 ? -28.293 8.750  72.888  1.00 39.81 ? 171 GLU A CD  1 
ATOM   1494 O OE1 . GLU A 1 171 ? -28.382 9.391  71.817  1.00 40.70 ? 171 GLU A OE1 1 
ATOM   1495 O OE2 . GLU A 1 171 ? -29.280 8.224  73.444  1.00 44.45 ? 171 GLU A OE2 1 
ATOM   1496 N N   . ILE A 1 172 ? -23.081 10.732 72.198  1.00 12.50 ? 172 ILE A N   1 
ATOM   1497 C CA  . ILE A 1 172 ? -22.046 11.216 71.285  1.00 13.70 ? 172 ILE A CA  1 
ATOM   1498 C C   . ILE A 1 172 ? -20.688 10.639 71.675  1.00 14.06 ? 172 ILE A C   1 
ATOM   1499 O O   . ILE A 1 172 ? -19.936 10.135 70.829  1.00 10.49 ? 172 ILE A O   1 
ATOM   1500 C CB  . ILE A 1 172 ? -22.027 12.760 71.268  1.00 9.40  ? 172 ILE A CB  1 
ATOM   1501 C CG1 . ILE A 1 172 ? -23.247 13.316 70.526  1.00 13.74 ? 172 ILE A CG1 1 
ATOM   1502 C CG2 . ILE A 1 172 ? -20.728 13.299 70.662  1.00 14.91 ? 172 ILE A CG2 1 
ATOM   1503 C CD1 . ILE A 1 172 ? -23.289 13.005 69.019  1.00 17.78 ? 172 ILE A CD1 1 
ATOM   1504 N N   . ILE A 1 173 ? -20.360 10.684 72.968  1.00 10.36 ? 173 ILE A N   1 
ATOM   1505 C CA  . ILE A 1 173 ? -19.072 10.151 73.408  1.00 12.20 ? 173 ILE A CA  1 
ATOM   1506 C C   . ILE A 1 173 ? -18.966 8.672  73.061  1.00 13.37 ? 173 ILE A C   1 
ATOM   1507 O O   . ILE A 1 173 ? -17.923 8.198  72.587  1.00 10.95 ? 173 ILE A O   1 
ATOM   1508 C CB  . ILE A 1 173 ? -18.889 10.378 74.918  1.00 10.40 ? 173 ILE A CB  1 
ATOM   1509 C CG1 . ILE A 1 173 ? -18.868 11.882 75.221  1.00 13.08 ? 173 ILE A CG1 1 
ATOM   1510 C CG2 . ILE A 1 173 ? -17.612 9.668  75.394  1.00 14.43 ? 173 ILE A CG2 1 
ATOM   1511 C CD1 . ILE A 1 173 ? -18.624 12.219 76.684  1.00 14.87 ? 173 ILE A CD1 1 
ATOM   1512 N N   . LYS A 1 174 ? -20.056 7.925  73.268  1.00 10.73 ? 174 LYS A N   1 
ATOM   1513 C CA  . LYS A 1 174 ? -20.022 6.481  73.047  1.00 11.26 ? 174 LYS A CA  1 
ATOM   1514 C C   . LYS A 1 174 ? -19.824 6.127  71.577  1.00 14.97 ? 174 LYS A C   1 
ATOM   1515 O O   . LYS A 1 174 ? -19.356 5.020  71.276  1.00 16.56 ? 174 LYS A O   1 
ATOM   1516 C CB  . LYS A 1 174 ? -21.310 5.823  73.564  1.00 13.25 ? 174 LYS A CB  1 
ATOM   1517 C CG  . LYS A 1 174 ? -21.463 5.888  75.087  1.00 13.09 ? 174 LYS A CG  1 
ATOM   1518 C CD  . LYS A 1 174 ? -22.760 5.262  75.554  1.00 25.91 ? 174 LYS A CD  1 
ATOM   1519 C CE  . LYS A 1 174 ? -22.876 5.353  77.061  1.00 37.31 ? 174 LYS A CE  1 
ATOM   1520 N NZ  . LYS A 1 174 ? -24.083 4.642  77.558  1.00 50.74 ? 174 LYS A NZ  1 
ATOM   1521 N N   . LYS A 1 175 ? -20.190 7.024  70.662  1.00 13.64 ? 175 LYS A N   1 
ATOM   1522 C CA  . LYS A 1 175 ? -20.044 6.791  69.232  1.00 13.56 ? 175 LYS A CA  1 
ATOM   1523 C C   . LYS A 1 175 ? -18.736 7.340  68.680  1.00 16.25 ? 175 LYS A C   1 
ATOM   1524 O O   . LYS A 1 175 ? -18.492 7.239  67.472  1.00 13.54 ? 175 LYS A O   1 
ATOM   1525 C CB  . LYS A 1 175 ? -21.212 7.434  68.471  1.00 19.76 ? 175 LYS A CB  1 
ATOM   1526 C CG  . LYS A 1 175 ? -22.578 6.876  68.834  1.00 25.21 ? 175 LYS A CG  1 
ATOM   1527 C CD  . LYS A 1 175 ? -23.687 7.550  68.024  1.00 32.47 ? 175 LYS A CD  1 
ATOM   1528 C CE  . LYS A 1 175 ? -23.414 9.032  67.813  1.00 45.10 ? 175 LYS A CE  1 
ATOM   1529 N NZ  . LYS A 1 175 ? -24.582 9.749  67.215  1.00 56.52 ? 175 LYS A NZ  1 
ATOM   1530 N N   . THR A 1 176 ? -17.890 7.925  69.528  1.00 12.46 ? 176 THR A N   1 
ATOM   1531 C CA  . THR A 1 176 ? -16.756 8.690  69.010  1.00 13.51 ? 176 THR A CA  1 
ATOM   1532 C C   . THR A 1 176 ? -15.673 7.789  68.412  1.00 12.35 ? 176 THR A C   1 
ATOM   1533 O O   . THR A 1 176 ? -15.254 7.991  67.266  1.00 13.87 ? 176 THR A O   1 
ATOM   1534 C CB  . THR A 1 176 ? -16.198 9.603  70.099  1.00 11.01 ? 176 THR A CB  1 
ATOM   1535 O OG1 . THR A 1 176 ? -17.167 10.615 70.374  1.00 13.00 ? 176 THR A OG1 1 
ATOM   1536 C CG2 . THR A 1 176 ? -14.898 10.294 69.613  1.00 12.59 ? 176 THR A CG2 1 
ATOM   1537 N N   . LEU A 1 177 ? -15.190 6.793  69.150  1.00 15.25 ? 177 LEU A N   1 
ATOM   1538 C CA  . LEU A 1 177 ? -14.172 5.942  68.539  1.00 12.49 ? 177 LEU A CA  1 
ATOM   1539 C C   . LEU A 1 177 ? -14.718 5.231  67.307  1.00 14.00 ? 177 LEU A C   1 
ATOM   1540 O O   . LEU A 1 177 ? -13.969 4.987  66.351  1.00 14.75 ? 177 LEU A O   1 
ATOM   1541 C CB  . LEU A 1 177 ? -13.625 4.932  69.551  1.00 12.11 ? 177 LEU A CB  1 
ATOM   1542 C CG  . LEU A 1 177 ? -12.927 5.615  70.731  1.00 16.03 ? 177 LEU A CG  1 
ATOM   1543 C CD1 . LEU A 1 177 ? -12.333 4.614  71.691  1.00 16.71 ? 177 LEU A CD1 1 
ATOM   1544 C CD2 . LEU A 1 177 ? -11.832 6.551  70.227  1.00 20.47 ? 177 LEU A CD2 1 
ATOM   1545 N N   . SER A 1 178 ? -16.020 4.926  67.291  1.00 11.94 ? 178 SER A N   1 
ATOM   1546 C CA  . SER A 1 178 ? -16.605 4.281  66.122  1.00 13.86 ? 178 SER A CA  1 
ATOM   1547 C C   . SER A 1 178 ? -16.538 5.180  64.895  1.00 15.97 ? 178 SER A C   1 
ATOM   1548 O O   . SER A 1 178 ? -16.305 4.694  63.783  1.00 15.07 ? 178 SER A O   1 
ATOM   1549 C CB  . SER A 1 178 ? -18.057 3.879  66.399  1.00 15.80 ? 178 SER A CB  1 
ATOM   1550 O OG  . SER A 1 178 ? -18.089 2.718  67.194  1.00 24.72 ? 178 SER A OG  1 
ATOM   1551 N N   . ILE A 1 179 ? -16.738 6.493  65.061  1.00 12.35 ? 179 ILE A N   1 
ATOM   1552 C CA  . ILE A 1 179 ? -16.715 7.308  63.846  1.00 11.57 ? 179 ILE A CA  1 
ATOM   1553 C C   . ILE A 1 179 ? -15.303 7.388  63.276  1.00 15.45 ? 179 ILE A C   1 
ATOM   1554 O O   . ILE A 1 179 ? -15.134 7.438  62.053  1.00 14.21 ? 179 ILE A O   1 
ATOM   1555 C CB  . ILE A 1 179 ? -17.326 8.708  64.063  1.00 15.40 ? 179 ILE A CB  1 
ATOM   1556 C CG1 . ILE A 1 179 ? -17.614 9.358  62.703  1.00 20.71 ? 179 ILE A CG1 1 
ATOM   1557 C CG2 . ILE A 1 179 ? -16.404 9.609  64.825  1.00 14.73 ? 179 ILE A CG2 1 
ATOM   1558 C CD1 . ILE A 1 179 ? -18.699 10.390 62.755  1.00 29.44 ? 179 ILE A CD1 1 
ATOM   1559 N N   . TYR A 1 180 ? -14.268 7.389  64.130  1.00 12.73 ? 180 TYR A N   1 
ATOM   1560 C CA  . TYR A 1 180 ? -12.903 7.338  63.613  1.00 11.25 ? 180 TYR A CA  1 
ATOM   1561 C C   . TYR A 1 180 ? -12.631 6.036  62.873  1.00 14.69 ? 180 TYR A C   1 
ATOM   1562 O O   . TYR A 1 180 ? -11.994 6.045  61.815  1.00 14.48 ? 180 TYR A O   1 
ATOM   1563 C CB  . TYR A 1 180 ? -11.897 7.540  64.740  1.00 12.82 ? 180 TYR A CB  1 
ATOM   1564 C CG  . TYR A 1 180 ? -11.864 8.975  65.193  1.00 9.20  ? 180 TYR A CG  1 
ATOM   1565 C CD1 . TYR A 1 180 ? -11.200 9.948  64.437  1.00 13.92 ? 180 TYR A CD1 1 
ATOM   1566 C CD2 . TYR A 1 180 ? -12.501 9.370  66.357  1.00 10.52 ? 180 TYR A CD2 1 
ATOM   1567 C CE1 . TYR A 1 180 ? -11.174 11.277 64.836  1.00 12.34 ? 180 TYR A CE1 1 
ATOM   1568 C CE2 . TYR A 1 180 ? -12.487 10.711 66.765  1.00 8.15  ? 180 TYR A CE2 1 
ATOM   1569 C CZ  . TYR A 1 180 ? -11.823 11.650 65.998  1.00 12.18 ? 180 TYR A CZ  1 
ATOM   1570 O OH  . TYR A 1 180 ? -11.790 12.972 66.381  1.00 14.18 ? 180 TYR A OH  1 
ATOM   1571 N N   . ARG A 1 181 ? -13.087 4.903  63.411  1.00 14.12 ? 181 ARG A N   1 
ATOM   1572 C CA  . ARG A 1 181 ? -12.927 3.663  62.662  1.00 14.15 ? 181 ARG A CA  1 
ATOM   1573 C C   . ARG A 1 181 ? -13.642 3.752  61.322  1.00 14.63 ? 181 ARG A C   1 
ATOM   1574 O O   . ARG A 1 181 ? -13.120 3.299  60.300  1.00 17.19 ? 181 ARG A O   1 
ATOM   1575 C CB  . ARG A 1 181 ? -13.453 2.464  63.451  1.00 18.41 ? 181 ARG A CB  1 
ATOM   1576 C CG  . ARG A 1 181 ? -12.681 2.142  64.712  1.00 18.28 ? 181 ARG A CG  1 
ATOM   1577 C CD  . ARG A 1 181 ? -13.155 0.835  65.357  1.00 21.66 ? 181 ARG A CD  1 
ATOM   1578 N NE  . ARG A 1 181 ? -12.689 0.796  66.736  1.00 31.35 ? 181 ARG A NE  1 
ATOM   1579 C CZ  . ARG A 1 181 ? -13.432 1.094  67.792  1.00 26.48 ? 181 ARG A CZ  1 
ATOM   1580 N NH1 . ARG A 1 181 ? -14.712 1.422  67.650  1.00 29.03 ? 181 ARG A NH1 1 
ATOM   1581 N NH2 . ARG A 1 181 ? -12.893 1.043  69.002  1.00 32.46 ? 181 ARG A NH2 1 
ATOM   1582 N N   . GLU A 1 182 ? -14.841 4.338  61.315  1.00 14.41 ? 182 GLU A N   1 
ATOM   1583 C CA  . GLU A 1 182 ? -15.645 4.354  60.102  1.00 15.32 ? 182 GLU A CA  1 
ATOM   1584 C C   . GLU A 1 182 ? -14.992 5.218  59.032  1.00 13.70 ? 182 GLU A C   1 
ATOM   1585 O O   . GLU A 1 182 ? -14.861 4.795  57.877  1.00 15.15 ? 182 GLU A O   1 
ATOM   1586 C CB  . GLU A 1 182 ? -17.061 4.857  60.400  1.00 16.46 ? 182 GLU A CB  1 
ATOM   1587 C CG  . GLU A 1 182 ? -17.916 4.953  59.153  1.00 23.66 ? 182 GLU A CG  1 
ATOM   1588 C CD  . GLU A 1 182 ? -19.386 5.232  59.447  1.00 36.80 ? 182 GLU A CD  1 
ATOM   1589 O OE1 . GLU A 1 182 ? -20.212 5.048  58.529  1.00 40.70 ? 182 GLU A OE1 1 
ATOM   1590 O OE2 . GLU A 1 182 ? -19.717 5.623  60.586  1.00 38.38 ? 182 GLU A OE2 1 
ATOM   1591 N N   . ILE A 1 183 ? -14.552 6.426  59.398  1.00 16.03 ? 183 ILE A N   1 
ATOM   1592 C CA  . ILE A 1 183 ? -13.997 7.285  58.357  1.00 13.36 ? 183 ILE A CA  1 
ATOM   1593 C C   . ILE A 1 183 ? -12.661 6.739  57.880  1.00 15.95 ? 183 ILE A C   1 
ATOM   1594 O O   . ILE A 1 183 ? -12.306 6.882  56.703  1.00 17.65 ? 183 ILE A O   1 
ATOM   1595 C CB  . ILE A 1 183 ? -13.909 8.750  58.832  1.00 13.87 ? 183 ILE A CB  1 
ATOM   1596 C CG1 . ILE A 1 183 ? -12.906 8.924  59.983  1.00 16.64 ? 183 ILE A CG1 1 
ATOM   1597 C CG2 . ILE A 1 183 ? -15.290 9.253  59.196  1.00 16.02 ? 183 ILE A CG2 1 
ATOM   1598 C CD1 . ILE A 1 183 ? -11.558 9.445  59.530  1.00 18.23 ? 183 ILE A CD1 1 
ATOM   1599 N N   . LYS A 1 184 ? -11.934 6.050  58.755  1.00 13.44 ? 184 LYS A N   1 
ATOM   1600 C CA  . LYS A 1 184 ? -10.709 5.378  58.331  1.00 12.62 ? 184 LYS A CA  1 
ATOM   1601 C C   . LYS A 1 184 ? -11.017 4.225  57.384  1.00 14.64 ? 184 LYS A C   1 
ATOM   1602 O O   . LYS A 1 184 ? -10.445 4.135  56.290  1.00 16.28 ? 184 LYS A O   1 
ATOM   1603 C CB  . LYS A 1 184 ? -9.950  4.892  59.561  1.00 14.66 ? 184 LYS A CB  1 
ATOM   1604 C CG  . LYS A 1 184 ? -8.609  4.259  59.275  1.00 16.59 ? 184 LYS A CG  1 
ATOM   1605 C CD  . LYS A 1 184 ? -7.994  3.751  60.584  1.00 15.01 ? 184 LYS A CD  1 
ATOM   1606 C CE  . LYS A 1 184 ? -6.717  2.957  60.349  1.00 17.33 ? 184 LYS A CE  1 
ATOM   1607 N NZ  . LYS A 1 184 ? -6.933  1.786  59.426  1.00 24.06 ? 184 LYS A NZ  1 
ATOM   1608 N N   . GLU A 1 185 ? -11.949 3.350  57.771  1.00 14.91 ? 185 GLU A N   1 
ATOM   1609 C CA  . GLU A 1 185 ? -12.257 2.194  56.934  1.00 15.72 ? 185 GLU A CA  1 
ATOM   1610 C C   . GLU A 1 185 ? -12.828 2.617  55.585  1.00 17.14 ? 185 GLU A C   1 
ATOM   1611 O O   . GLU A 1 185 ? -12.571 1.967  54.560  1.00 19.47 ? 185 GLU A O   1 
ATOM   1612 C CB  . GLU A 1 185 ? -13.226 1.275  57.679  1.00 16.43 ? 185 GLU A CB  1 
ATOM   1613 C CG  . GLU A 1 185 ? -13.526 -0.005 56.933  1.00 19.13 ? 185 GLU A CG  1 
ATOM   1614 C CD  . GLU A 1 185 ? -14.085 -1.079 57.846  1.00 22.66 ? 185 GLU A CD  1 
ATOM   1615 O OE1 . GLU A 1 185 ? -14.557 -2.096 57.322  1.00 31.75 ? 185 GLU A OE1 1 
ATOM   1616 O OE2 . GLU A 1 185 ? -14.056 -0.902 59.075  1.00 26.41 ? 185 GLU A OE2 1 
ATOM   1617 N N   . GLU A 1 186 ? -13.587 3.713  55.559  1.00 15.67 ? 186 GLU A N   1 
ATOM   1618 C CA  . GLU A 1 186 ? -14.199 4.156  54.313  1.00 17.96 ? 186 GLU A CA  1 
ATOM   1619 C C   . GLU A 1 186 ? -13.250 4.985  53.466  1.00 16.59 ? 186 GLU A C   1 
ATOM   1620 O O   . GLU A 1 186 ? -13.641 5.425  52.375  1.00 17.30 ? 186 GLU A O   1 
ATOM   1621 C CB  . GLU A 1 186 ? -15.482 4.941  54.608  1.00 19.10 ? 186 GLU A CB  1 
ATOM   1622 C CG  . GLU A 1 186 ? -16.556 4.083  55.296  1.00 19.59 ? 186 GLU A CG  1 
ATOM   1623 C CD  . GLU A 1 186 ? -17.828 4.837  55.618  1.00 25.49 ? 186 GLU A CD  1 
ATOM   1624 O OE1 . GLU A 1 186 ? -17.784 6.072  55.779  1.00 21.84 ? 186 GLU A OE1 1 
ATOM   1625 O OE2 . GLU A 1 186 ? -18.880 4.179  55.733  1.00 26.66 ? 186 GLU A OE2 1 
ATOM   1626 N N   . GLY A 1 187 ? -12.014 5.175  53.919  1.00 16.48 ? 187 GLY A N   1 
ATOM   1627 C CA  . GLY A 1 187 ? -11.063 5.947  53.149  1.00 18.22 ? 187 GLY A CA  1 
ATOM   1628 C C   . GLY A 1 187 ? -11.358 7.428  53.109  1.00 18.71 ? 187 GLY A C   1 
ATOM   1629 O O   . GLY A 1 187 ? -10.869 8.128  52.214  1.00 16.32 ? 187 GLY A O   1 
ATOM   1630 N N   . LYS A 1 188 ? -12.146 7.932  54.055  1.00 13.72 ? 188 LYS A N   1 
ATOM   1631 C CA  . LYS A 1 188 ? -12.426 9.363  54.090  1.00 14.20 ? 188 LYS A CA  1 
ATOM   1632 C C   . LYS A 1 188 ? -11.351 10.146 54.832  1.00 16.10 ? 188 LYS A C   1 
ATOM   1633 O O   . LYS A 1 188 ? -11.306 11.373 54.713  1.00 14.36 ? 188 LYS A O   1 
ATOM   1634 C CB  . LYS A 1 188 ? -13.792 9.609  54.720  1.00 14.27 ? 188 LYS A CB  1 
ATOM   1635 C CG  . LYS A 1 188 ? -14.922 8.878  53.975  1.00 15.38 ? 188 LYS A CG  1 
ATOM   1636 C CD  . LYS A 1 188 ? -16.267 9.136  54.602  1.00 19.68 ? 188 LYS A CD  1 
ATOM   1637 C CE  . LYS A 1 188 ? -17.376 8.487  53.764  1.00 31.71 ? 188 LYS A CE  1 
ATOM   1638 N NZ  . LYS A 1 188 ? -18.710 8.954  54.189  1.00 42.76 ? 188 LYS A NZ  1 
ATOM   1639 N N   . GLY A 1 189 ? -10.502 9.464  55.583  1.00 13.08 ? 189 GLY A N   1 
ATOM   1640 C CA  . GLY A 1 189 ? -9.417  10.101 56.293  1.00 12.48 ? 189 GLY A CA  1 
ATOM   1641 C C   . GLY A 1 189 ? -8.479  9.060  56.849  1.00 12.45 ? 189 GLY A C   1 
ATOM   1642 O O   . GLY A 1 189 ? -8.847  7.893  57.023  1.00 15.21 ? 189 GLY A O   1 
ATOM   1643 N N   . SER A 1 190 ? -7.255  9.491  57.109  1.00 11.43 ? 190 SER A N   1 
ATOM   1644 C CA  . SER A 1 190 ? -6.318  8.675  57.861  1.00 10.77 ? 190 SER A CA  1 
ATOM   1645 C C   . SER A 1 190 ? -6.353  9.113  59.316  1.00 12.90 ? 190 SER A C   1 
ATOM   1646 O O   . SER A 1 190 ? -6.693  10.260 59.626  1.00 12.96 ? 190 SER A O   1 
ATOM   1647 C CB  . SER A 1 190 ? -4.895  8.810  57.307  1.00 13.48 ? 190 SER A CB  1 
ATOM   1648 O OG  . SER A 1 190 ? -4.813  8.344  55.961  1.00 14.48 ? 190 SER A OG  1 
ATOM   1649 N N   . VAL A 1 191 ? -6.009  8.189  60.209  1.00 11.75 ? 191 VAL A N   1 
ATOM   1650 C CA  . VAL A 1 191 ? -5.911  8.472  61.634  1.00 9.99  ? 191 VAL A CA  1 
ATOM   1651 C C   . VAL A 1 191 ? -4.499  8.136  62.084  1.00 12.19 ? 191 VAL A C   1 
ATOM   1652 O O   . VAL A 1 191 ? -4.016  7.018  61.854  1.00 14.07 ? 191 VAL A O   1 
ATOM   1653 C CB  . VAL A 1 191 ? -6.940  7.684  62.462  1.00 10.81 ? 191 VAL A CB  1 
ATOM   1654 C CG1 . VAL A 1 191 ? -6.826  8.070  63.950  1.00 9.97  ? 191 VAL A CG1 1 
ATOM   1655 C CG2 . VAL A 1 191 ? -8.364  7.925  61.927  1.00 14.87 ? 191 VAL A CG2 1 
ATOM   1656 N N   . SER A 1 192 ? -3.857  9.089  62.741  1.00 12.78 ? 192 SER A N   1 
ATOM   1657 C CA  . SER A 1 192 ? -2.519  8.922  63.270  1.00 10.46 ? 192 SER A CA  1 
ATOM   1658 C C   . SER A 1 192 ? -2.609  8.925  64.787  1.00 10.41 ? 192 SER A C   1 
ATOM   1659 O O   . SER A 1 192 ? -3.672  9.162  65.346  1.00 9.94  ? 192 SER A O   1 
ATOM   1660 C CB  . SER A 1 192 ? -1.616  10.048 62.784  1.00 8.47  ? 192 SER A CB  1 
ATOM   1661 O OG  . SER A 1 192 ? -2.084  11.288 63.312  1.00 11.21 ? 192 SER A OG  1 
ATOM   1662 N N   . THR A 1 193 ? -1.470  8.694  65.444  1.00 10.60 ? 193 THR A N   1 
ATOM   1663 C CA  . THR A 1 193 ? -1.373  8.911  66.885  1.00 8.42  ? 193 THR A CA  1 
ATOM   1664 C C   . THR A 1 193 ? -0.034  9.579  67.199  1.00 13.75 ? 193 THR A C   1 
ATOM   1665 O O   . THR A 1 193 ? 0.770   9.848  66.311  1.00 11.50 ? 193 THR A O   1 
ATOM   1666 C CB  . THR A 1 193 ? -1.574  7.608  67.667  1.00 10.98 ? 193 THR A CB  1 
ATOM   1667 O OG1 . THR A 1 193 ? -1.819  7.937  69.048  1.00 11.01 ? 193 THR A OG1 1 
ATOM   1668 C CG2 . THR A 1 193 ? -0.351  6.679  67.585  1.00 11.80 ? 193 THR A CG2 1 
ATOM   1669 N N   . SER A 1 194 ? 0.176   9.891  68.469  1.00 12.84 ? 194 SER A N   1 
ATOM   1670 C CA  . SER A 1 194 ? 1.383   10.525 68.977  1.00 11.11 ? 194 SER A CA  1 
ATOM   1671 C C   . SER A 1 194 ? 1.980   9.633  70.051  1.00 12.61 ? 194 SER A C   1 
ATOM   1672 O O   . SER A 1 194 ? 1.273   8.805  70.637  1.00 12.84 ? 194 SER A O   1 
ATOM   1673 C CB  . SER A 1 194 ? 1.065   11.895 69.591  1.00 9.70  ? 194 SER A CB  1 
ATOM   1674 O OG  . SER A 1 194 ? 0.622   12.835 68.621  1.00 9.35  ? 194 SER A OG  1 
ATOM   1675 N N   . PRO A 1 195 ? 3.269   9.782  70.354  1.00 9.67  ? 195 PRO A N   1 
ATOM   1676 C CA  . PRO A 1 195 ? 3.818   9.124  71.549  1.00 8.75  ? 195 PRO A CA  1 
ATOM   1677 C C   . PRO A 1 195 ? 2.926   9.396  72.757  1.00 14.20 ? 195 PRO A C   1 
ATOM   1678 O O   . PRO A 1 195 ? 2.345   10.482 72.899  1.00 11.96 ? 195 PRO A O   1 
ATOM   1679 C CB  . PRO A 1 195 ? 5.210   9.750  71.696  1.00 18.43 ? 195 PRO A CB  1 
ATOM   1680 C CG  . PRO A 1 195 ? 5.580   10.149 70.266  1.00 24.18 ? 195 PRO A CG  1 
ATOM   1681 C CD  . PRO A 1 195 ? 4.282   10.534 69.593  1.00 13.68 ? 195 PRO A CD  1 
ATOM   1682 N N   . TYR A 1 196 ? 2.828   8.386  73.629  1.00 11.27 ? 196 TYR A N   1 
ATOM   1683 C CA  . TYR A 1 196 ? 1.613   8.133  74.416  1.00 11.53 ? 196 TYR A CA  1 
ATOM   1684 C C   . TYR A 1 196 ? 1.074   9.360  75.160  1.00 13.22 ? 196 TYR A C   1 
ATOM   1685 O O   . TYR A 1 196 ? -0.117  9.691  75.061  1.00 10.65 ? 196 TYR A O   1 
ATOM   1686 C CB  . TYR A 1 196 ? 1.872   6.997  75.405  1.00 11.28 ? 196 TYR A CB  1 
ATOM   1687 C CG  . TYR A 1 196 ? 0.600   6.287  75.827  1.00 9.30  ? 196 TYR A CG  1 
ATOM   1688 C CD1 . TYR A 1 196 ? -0.296  6.885  76.706  1.00 9.78  ? 196 TYR A CD1 1 
ATOM   1689 C CD2 . TYR A 1 196 ? 0.310   5.002  75.357  1.00 9.70  ? 196 TYR A CD2 1 
ATOM   1690 C CE1 . TYR A 1 196 ? -1.467  6.227  77.090  1.00 10.27 ? 196 TYR A CE1 1 
ATOM   1691 C CE2 . TYR A 1 196 ? -0.839  4.341  75.733  1.00 11.51 ? 196 TYR A CE2 1 
ATOM   1692 C CZ  . TYR A 1 196 ? -1.721  4.950  76.600  1.00 13.80 ? 196 TYR A CZ  1 
ATOM   1693 O OH  . TYR A 1 196 ? -2.859  4.279  76.965  1.00 15.21 ? 196 TYR A OH  1 
ATOM   1694 N N   . TYR A 1 197 ? 1.902   9.995  75.985  1.00 12.60 ? 197 TYR A N   1 
ATOM   1695 C CA  . TYR A 1 197 ? 1.432   11.101 76.808  1.00 11.96 ? 197 TYR A CA  1 
ATOM   1696 C C   . TYR A 1 197 ? 1.836   12.456 76.245  1.00 11.23 ? 197 TYR A C   1 
ATOM   1697 O O   . TYR A 1 197 ? 1.913   13.434 76.992  1.00 11.36 ? 197 TYR A O   1 
ATOM   1698 C CB  . TYR A 1 197 ? 1.908   10.946 78.254  1.00 9.99  ? 197 TYR A CB  1 
ATOM   1699 C CG  . TYR A 1 197 ? 1.261   9.762  78.884  1.00 12.27 ? 197 TYR A CG  1 
ATOM   1700 C CD1 . TYR A 1 197 ? -0.066  9.818  79.282  1.00 11.71 ? 197 TYR A CD1 1 
ATOM   1701 C CD2 . TYR A 1 197 ? 1.957   8.570  79.048  1.00 14.04 ? 197 TYR A CD2 1 
ATOM   1702 C CE1 . TYR A 1 197 ? -0.685  8.723  79.828  1.00 14.17 ? 197 TYR A CE1 1 
ATOM   1703 C CE2 . TYR A 1 197 ? 1.346   7.479  79.609  1.00 11.46 ? 197 TYR A CE2 1 
ATOM   1704 C CZ  . TYR A 1 197 ? 0.026   7.561  79.997  1.00 14.54 ? 197 TYR A CZ  1 
ATOM   1705 O OH  . TYR A 1 197 ? -0.620  6.496  80.555  1.00 16.90 ? 197 TYR A OH  1 
ATOM   1706 N N   . HIS A 1 198 ? 2.045   12.537 74.925  1.00 10.30 ? 198 HIS A N   1 
ATOM   1707 C CA  . HIS A 1 198 ? 2.340   13.800 74.255  1.00 11.28 ? 198 HIS A CA  1 
ATOM   1708 C C   . HIS A 1 198 ? 3.572   14.480 74.868  1.00 8.73  ? 198 HIS A C   1 
ATOM   1709 O O   . HIS A 1 198 ? 3.517   15.670 75.197  1.00 9.50  ? 198 HIS A O   1 
ATOM   1710 C CB  . HIS A 1 198 ? 1.101   14.698 74.320  1.00 12.02 ? 198 HIS A CB  1 
ATOM   1711 C CG  . HIS A 1 198 ? 1.082   15.829 73.328  1.00 8.13  ? 198 HIS A CG  1 
ATOM   1712 N ND1 . HIS A 1 198 ? 1.499   17.100 73.652  1.00 9.38  ? 198 HIS A ND1 1 
ATOM   1713 C CD2 . HIS A 1 198 ? 0.611   15.901 72.058  1.00 10.37 ? 198 HIS A CD2 1 
ATOM   1714 C CE1 . HIS A 1 198 ? 1.328   17.900 72.611  1.00 12.11 ? 198 HIS A CE1 1 
ATOM   1715 N NE2 . HIS A 1 198 ? 0.774   17.204 71.635  1.00 10.72 ? 198 HIS A NE2 1 
ATOM   1716 N N   . PRO A 1 199 ? 4.691   13.765 75.045  1.00 7.95  ? 199 PRO A N   1 
ATOM   1717 C CA  . PRO A 1 199 ? 5.919   14.394 75.549  1.00 8.20  ? 199 PRO A CA  1 
ATOM   1718 C C   . PRO A 1 199 ? 6.700   15.099 74.444  1.00 15.14 ? 199 PRO A C   1 
ATOM   1719 O O   . PRO A 1 199 ? 6.452   14.911 73.255  1.00 14.07 ? 199 PRO A O   1 
ATOM   1720 C CB  . PRO A 1 199 ? 6.722   13.193 76.045  1.00 12.64 ? 199 PRO A CB  1 
ATOM   1721 C CG  . PRO A 1 199 ? 6.400   12.130 74.990  1.00 14.18 ? 199 PRO A CG  1 
ATOM   1722 C CD  . PRO A 1 199 ? 4.911   12.335 74.743  1.00 11.81 ? 199 PRO A CD  1 
ATOM   1723 N N   . LEU A 1 200 ? 7.714   15.868 74.867  1.00 12.43 ? 200 LEU A N   1 
ATOM   1724 C CA  . LEU A 1 200 ? 8.699   16.448 73.944  1.00 10.95 ? 200 LEU A CA  1 
ATOM   1725 C C   . LEU A 1 200 ? 9.803   15.422 73.702  1.00 11.91 ? 200 LEU A C   1 
ATOM   1726 O O   . LEU A 1 200 ? 10.814  15.386 74.407  1.00 13.98 ? 200 LEU A O   1 
ATOM   1727 C CB  . LEU A 1 200 ? 9.264   17.741 74.508  1.00 14.35 ? 200 LEU A CB  1 
ATOM   1728 C CG  . LEU A 1 200 ? 8.249   18.870 74.591  1.00 15.42 ? 200 LEU A CG  1 
ATOM   1729 C CD1 . LEU A 1 200 ? 8.832   19.973 75.435  1.00 14.85 ? 200 LEU A CD1 1 
ATOM   1730 C CD2 . LEU A 1 200 ? 7.919   19.374 73.193  1.00 18.23 ? 200 LEU A CD2 1 
ATOM   1731 N N   . ILE A 1 201 ? 9.608   14.576 72.679  1.00 13.72 ? 201 ILE A N   1 
ATOM   1732 C CA  . ILE A 1 201 ? 10.575  13.504 72.404  1.00 11.67 ? 201 ILE A CA  1 
ATOM   1733 C C   . ILE A 1 201 ? 11.995  14.026 72.241  1.00 10.87 ? 201 ILE A C   1 
ATOM   1734 O O   . ILE A 1 201 ? 12.920  13.392 72.773  1.00 12.74 ? 201 ILE A O   1 
ATOM   1735 C CB  . ILE A 1 201 ? 10.112  12.669 71.202  1.00 9.39  ? 201 ILE A CB  1 
ATOM   1736 C CG1 . ILE A 1 201 ? 8.806   11.914 71.534  1.00 11.59 ? 201 ILE A CG1 1 
ATOM   1737 C CG2 . ILE A 1 201 ? 11.235  11.715 70.712  1.00 12.08 ? 201 ILE A CG2 1 
ATOM   1738 C CD1 . ILE A 1 201 ? 8.964   10.761 72.544  1.00 13.13 ? 201 ILE A CD1 1 
ATOM   1739 N N   . PRO A 1 202 ? 12.261  15.121 71.508  1.00 10.72 ? 202 PRO A N   1 
ATOM   1740 C CA  . PRO A 1 202 ? 13.666  15.543 71.348  1.00 8.71  ? 202 PRO A CA  1 
ATOM   1741 C C   . PRO A 1 202 ? 14.379  15.811 72.663  1.00 10.10 ? 202 PRO A C   1 
ATOM   1742 O O   . PRO A 1 202 ? 15.586  15.508 72.788  1.00 10.88 ? 202 PRO A O   1 
ATOM   1743 C CB  . PRO A 1 202 ? 13.540  16.804 70.480  1.00 10.85 ? 202 PRO A CB  1 
ATOM   1744 C CG  . PRO A 1 202 ? 12.326  16.505 69.615  1.00 12.00 ? 202 PRO A CG  1 
ATOM   1745 C CD  . PRO A 1 202 ? 11.372  15.873 70.596  1.00 10.64 ? 202 PRO A CD  1 
ATOM   1746 N N   . ILE A 1 203 ? 13.667  16.383 73.638  1.00 13.33 ? 203 ILE A N   1 
ATOM   1747 C CA  . ILE A 1 203 ? 14.264  16.681 74.937  1.00 10.72 ? 203 ILE A CA  1 
ATOM   1748 C C   . ILE A 1 203 ? 14.521  15.396 75.697  1.00 8.80  ? 203 ILE A C   1 
ATOM   1749 O O   . ILE A 1 203 ? 15.597  15.205 76.276  1.00 10.73 ? 203 ILE A O   1 
ATOM   1750 C CB  . ILE A 1 203 ? 13.355  17.643 75.721  1.00 10.69 ? 203 ILE A CB  1 
ATOM   1751 C CG1 . ILE A 1 203 ? 13.374  19.034 75.073  1.00 12.96 ? 203 ILE A CG1 1 
ATOM   1752 C CG2 . ILE A 1 203 ? 13.769  17.736 77.191  1.00 14.01 ? 203 ILE A CG2 1 
ATOM   1753 C CD1 . ILE A 1 203 ? 12.536  20.062 75.831  1.00 14.35 ? 203 ILE A CD1 1 
ATOM   1754 N N   . LEU A 1 204 ? 13.545  14.476 75.687  1.00 8.46  ? 204 LEU A N   1 
ATOM   1755 C CA  . LEU A 1 204 ? 13.759  13.190 76.342  1.00 14.74 ? 204 LEU A CA  1 
ATOM   1756 C C   . LEU A 1 204 ? 14.984  12.470 75.778  1.00 12.95 ? 204 LEU A C   1 
ATOM   1757 O O   . LEU A 1 204 ? 15.722  11.817 76.521  1.00 14.36 ? 204 LEU A O   1 
ATOM   1758 C CB  . LEU A 1 204 ? 12.517  12.313 76.208  1.00 14.67 ? 204 LEU A CB  1 
ATOM   1759 C CG  . LEU A 1 204 ? 11.224  12.840 76.842  1.00 10.39 ? 204 LEU A CG  1 
ATOM   1760 C CD1 . LEU A 1 204 ? 10.202  11.702 76.853  1.00 13.60 ? 204 LEU A CD1 1 
ATOM   1761 C CD2 . LEU A 1 204 ? 11.442  13.371 78.255  1.00 13.55 ? 204 LEU A CD2 1 
ATOM   1762 N N   . LEU A 1 205 ? 15.199  12.541 74.463  1.00 10.22 ? 205 LEU A N   1 
ATOM   1763 C CA  . LEU A 1 205 ? 16.353  11.859 73.882  1.00 10.42 ? 205 LEU A CA  1 
ATOM   1764 C C   . LEU A 1 205 ? 17.643  12.607 74.161  1.00 14.10 ? 205 LEU A C   1 
ATOM   1765 O O   . LEU A 1 205 ? 18.695  11.987 74.340  1.00 13.14 ? 205 LEU A O   1 
ATOM   1766 C CB  . LEU A 1 205 ? 16.183  11.695 72.368  1.00 9.85  ? 205 LEU A CB  1 
ATOM   1767 C CG  . LEU A 1 205 ? 15.089  10.704 71.965  1.00 13.37 ? 205 LEU A CG  1 
ATOM   1768 C CD1 . LEU A 1 205 ? 14.872  10.703 70.442  1.00 13.03 ? 205 LEU A CD1 1 
ATOM   1769 C CD2 . LEU A 1 205 ? 15.512  9.319  72.446  1.00 16.54 ? 205 LEU A CD2 1 
ATOM   1770 N N   . ASN A 1 206 ? 17.588  13.932 74.163  1.00 11.18 ? 206 ASN A N   1 
ATOM   1771 C CA  . ASN A 1 206 ? 18.816  14.700 74.298  1.00 11.30 ? 206 ASN A CA  1 
ATOM   1772 C C   . ASN A 1 206 ? 18.455  16.116 74.717  1.00 12.37 ? 206 ASN A C   1 
ATOM   1773 O O   . ASN A 1 206 ? 18.165  16.964 73.867  1.00 13.89 ? 206 ASN A O   1 
ATOM   1774 C CB  . ASN A 1 206 ? 19.611  14.708 72.988  1.00 14.25 ? 206 ASN A CB  1 
ATOM   1775 C CG  . ASN A 1 206 ? 20.797  15.653 73.040  1.00 23.49 ? 206 ASN A CG  1 
ATOM   1776 O OD1 . ASN A 1 206 ? 21.258  16.020 74.123  1.00 18.85 ? 206 ASN A OD1 1 
ATOM   1777 N ND2 . ASN A 1 206 ? 21.263  16.091 71.875  1.00 26.37 ? 206 ASN A ND2 1 
ATOM   1778 N N   . PRO A 1 207 ? 18.456  16.403 76.017  1.00 12.69 ? 207 PRO A N   1 
ATOM   1779 C CA  . PRO A 1 207 ? 18.066  17.742 76.479  1.00 13.30 ? 207 PRO A CA  1 
ATOM   1780 C C   . PRO A 1 207 ? 18.904  18.858 75.888  1.00 17.94 ? 207 PRO A C   1 
ATOM   1781 O O   . PRO A 1 207 ? 18.422  19.995 75.821  1.00 20.52 ? 207 PRO A O   1 
ATOM   1782 C CB  . PRO A 1 207 ? 18.258  17.651 77.998  1.00 14.05 ? 207 PRO A CB  1 
ATOM   1783 C CG  . PRO A 1 207 ? 18.063  16.193 78.292  1.00 14.00 ? 207 PRO A CG  1 
ATOM   1784 C CD  . PRO A 1 207 ? 18.686  15.468 77.128  1.00 16.35 ? 207 PRO A CD  1 
ATOM   1785 N N   . ASN A 1 208 ? 20.135  18.573 75.452  1.00 11.19 ? 208 ASN A N   1 
ATOM   1786 C CA  . ASN A 1 208 ? 20.983  19.619 74.895  1.00 14.34 ? 208 ASN A CA  1 
ATOM   1787 C C   . ASN A 1 208 ? 20.531  20.065 73.516  1.00 13.87 ? 208 ASN A C   1 
ATOM   1788 O O   . ASN A 1 208 ? 21.092  21.033 72.993  1.00 13.51 ? 208 ASN A O   1 
ATOM   1789 C CB  . ASN A 1 208 ? 22.436  19.157 74.848  1.00 15.75 ? 208 ASN A CB  1 
ATOM   1790 C CG  . ASN A 1 208 ? 22.986  18.884 76.228  1.00 17.09 ? 208 ASN A CG  1 
ATOM   1791 O OD1 . ASN A 1 208 ? 22.649  19.583 77.188  1.00 21.13 ? 208 ASN A OD1 1 
ATOM   1792 N ND2 . ASN A 1 208 ? 23.821  17.861 76.340  1.00 24.28 ? 208 ASN A ND2 1 
ATOM   1793 N N   . CYS A 1 209 ? 19.527  19.411 72.928  1.00 15.98 ? 209 CYS A N   1 
ATOM   1794 C CA  . CYS A 1 209 ? 19.054  19.867 71.628  1.00 17.81 ? 209 CYS A CA  1 
ATOM   1795 C C   . CYS A 1 209 ? 18.392  21.241 71.700  1.00 13.13 ? 209 CYS A C   1 
ATOM   1796 O O   . CYS A 1 209 ? 18.269  21.899 70.656  1.00 12.48 ? 209 CYS A O   1 
ATOM   1797 C CB  . CYS A 1 209 ? 18.092  18.835 71.020  1.00 19.07 ? 209 CYS A CB  1 
ATOM   1798 S SG  . CYS A 1 209 ? 16.460  18.818 71.721  1.00 18.94 ? 209 CYS A SG  1 
ATOM   1799 N N   . VAL A 1 210 ? 18.040  21.720 72.901  1.00 13.81 ? 210 VAL A N   1 
ATOM   1800 C CA  . VAL A 1 210 ? 17.474  23.067 73.006  1.00 15.02 ? 210 VAL A CA  1 
ATOM   1801 C C   . VAL A 1 210 ? 18.487  24.107 72.572  1.00 13.59 ? 210 VAL A C   1 
ATOM   1802 O O   . VAL A 1 210 ? 18.114  25.177 72.084  1.00 13.53 ? 210 VAL A O   1 
ATOM   1803 C CB  . VAL A 1 210 ? 16.957  23.365 74.433  1.00 15.60 ? 210 VAL A CB  1 
ATOM   1804 C CG1 . VAL A 1 210 ? 15.940  22.315 74.881  1.00 15.60 ? 210 VAL A CG1 1 
ATOM   1805 C CG2 . VAL A 1 210 ? 18.104  23.477 75.424  1.00 20.09 ? 210 VAL A CG2 1 
ATOM   1806 N N   . TYR A 1 211 ? 19.783  23.811 72.710  1.00 13.88 ? 211 TYR A N   1 
ATOM   1807 C CA  . TYR A 1 211 ? 20.788  24.789 72.326  1.00 14.10 ? 211 TYR A CA  1 
ATOM   1808 C C   . TYR A 1 211 ? 20.975  24.905 70.840  1.00 18.49 ? 211 TYR A C   1 
ATOM   1809 O O   . TYR A 1 211 ? 21.758  25.752 70.421  1.00 22.18 ? 211 TYR A O   1 
ATOM   1810 C CB  . TYR A 1 211 ? 22.117  24.435 72.978  1.00 14.17 ? 211 TYR A CB  1 
ATOM   1811 C CG  . TYR A 1 211 ? 21.939  24.567 74.445  1.00 16.37 ? 211 TYR A CG  1 
ATOM   1812 C CD1 . TYR A 1 211 ? 21.598  25.789 74.946  1.00 22.54 ? 211 TYR A CD1 1 
ATOM   1813 C CD2 . TYR A 1 211 ? 21.975  23.462 75.313  1.00 21.61 ? 211 TYR A CD2 1 
ATOM   1814 C CE1 . TYR A 1 211 ? 21.373  25.953 76.262  1.00 21.38 ? 211 TYR A CE1 1 
ATOM   1815 C CE2 . TYR A 1 211 ? 21.747  23.613 76.659  1.00 19.89 ? 211 TYR A CE2 1 
ATOM   1816 C CZ  . TYR A 1 211 ? 21.437  24.849 77.117  1.00 24.39 ? 211 TYR A CZ  1 
ATOM   1817 O OH  . TYR A 1 211 ? 21.201  25.034 78.455  1.00 35.19 ? 211 TYR A OH  1 
ATOM   1818 N N   . GLU A 1 212 ? 20.305  24.078 70.045  1.00 15.66 ? 212 GLU A N   1 
ATOM   1819 C CA  . GLU A 1 212 ? 20.367  24.288 68.609  1.00 15.66 ? 212 GLU A CA  1 
ATOM   1820 C C   . GLU A 1 212 ? 19.650  25.566 68.191  1.00 23.27 ? 212 GLU A C   1 
ATOM   1821 O O   . GLU A 1 212 ? 19.974  26.119 67.138  1.00 24.38 ? 212 GLU A O   1 
ATOM   1822 C CB  . GLU A 1 212 ? 19.786  23.071 67.892  1.00 20.76 ? 212 GLU A CB  1 
ATOM   1823 C CG  . GLU A 1 212 ? 20.628  21.819 68.129  1.00 22.11 ? 212 GLU A CG  1 
ATOM   1824 C CD  . GLU A 1 212 ? 20.027  20.554 67.560  1.00 30.69 ? 212 GLU A CD  1 
ATOM   1825 O OE1 . GLU A 1 212 ? 20.221  19.483 68.176  1.00 34.91 ? 212 GLU A OE1 1 
ATOM   1826 O OE2 . GLU A 1 212 ? 19.368  20.622 66.502  1.00 31.50 ? 212 GLU A OE2 1 
ATOM   1827 N N   . THR A 1 213 ? 18.709  26.067 68.997  1.00 22.61 ? 213 THR A N   1 
ATOM   1828 C CA  . THR A 1 213 ? 17.979  27.284 68.650  1.00 18.33 ? 213 THR A CA  1 
ATOM   1829 C C   . THR A 1 213 ? 18.092  28.401 69.673  1.00 23.58 ? 213 THR A C   1 
ATOM   1830 O O   . THR A 1 213 ? 18.035  29.570 69.291  1.00 31.19 ? 213 THR A O   1 
ATOM   1831 C CB  . THR A 1 213 ? 16.490  26.982 68.453  1.00 19.22 ? 213 THR A CB  1 
ATOM   1832 O OG1 . THR A 1 213 ? 16.002  26.304 69.616  1.00 22.78 ? 213 THR A OG1 1 
ATOM   1833 C CG2 . THR A 1 213 ? 16.297  26.120 67.231  1.00 16.52 ? 213 THR A CG2 1 
ATOM   1834 N N   . THR A 1 214 ? 18.230  28.085 70.958  1.00 17.32 ? 214 THR A N   1 
ATOM   1835 C CA  . THR A 1 214 ? 18.291  29.103 72.004  1.00 17.92 ? 214 THR A CA  1 
ATOM   1836 C C   . THR A 1 214 ? 19.548  28.843 72.823  1.00 16.57 ? 214 THR A C   1 
ATOM   1837 O O   . THR A 1 214 ? 19.496  28.174 73.866  1.00 20.87 ? 214 THR A O   1 
ATOM   1838 C CB  . THR A 1 214 ? 17.031  29.082 72.872  1.00 19.45 ? 214 THR A CB  1 
ATOM   1839 O OG1 . THR A 1 214 ? 16.859  27.782 73.452  1.00 16.89 ? 214 THR A OG1 1 
ATOM   1840 C CG2 . THR A 1 214 ? 15.790  29.405 72.037  1.00 21.61 ? 214 THR A CG2 1 
ATOM   1841 N N   . PRO A 1 215 ? 20.701  29.348 72.377  1.00 23.39 ? 215 PRO A N   1 
ATOM   1842 C CA  . PRO A 1 215 ? 21.957  29.048 73.085  1.00 22.15 ? 215 PRO A CA  1 
ATOM   1843 C C   . PRO A 1 215 ? 22.025  29.615 74.487  1.00 26.94 ? 215 PRO A C   1 
ATOM   1844 O O   . PRO A 1 215 ? 22.805  29.109 75.301  1.00 26.34 ? 215 PRO A O   1 
ATOM   1845 C CB  . PRO A 1 215 ? 23.034  29.679 72.188  1.00 24.10 ? 215 PRO A CB  1 
ATOM   1846 C CG  . PRO A 1 215 ? 22.312  30.691 71.358  1.00 29.25 ? 215 PRO A CG  1 
ATOM   1847 C CD  . PRO A 1 215 ? 20.915  30.174 71.177  1.00 22.77 ? 215 PRO A CD  1 
ATOM   1848 N N   . ASN A 1 216 ? 21.238  30.640 74.799  1.00 20.02 ? 216 ASN A N   1 
ATOM   1849 C CA  . ASN A 1 216 ? 21.348  31.332 76.077  1.00 29.95 ? 216 ASN A CA  1 
ATOM   1850 C C   . ASN A 1 216 ? 20.439  30.756 77.150  1.00 30.42 ? 216 ASN A C   1 
ATOM   1851 O O   . ASN A 1 216 ? 20.477  31.226 78.291  1.00 34.11 ? 216 ASN A O   1 
ATOM   1852 C CB  . ASN A 1 216 ? 21.039  32.817 75.895  1.00 36.88 ? 216 ASN A CB  1 
ATOM   1853 C CG  . ASN A 1 216 ? 22.165  33.564 75.220  1.00 47.63 ? 216 ASN A CG  1 
ATOM   1854 O OD1 . ASN A 1 216 ? 23.311  33.111 75.212  1.00 52.51 ? 216 ASN A OD1 1 
ATOM   1855 N ND2 . ASN A 1 216 ? 21.846  34.714 74.643  1.00 53.46 ? 216 ASN A ND2 1 
ATOM   1856 N N   . VAL A 1 217 ? 19.633  29.750 76.820  1.00 22.53 ? 217 VAL A N   1 
ATOM   1857 C CA  . VAL A 1 217 ? 18.662  29.238 77.774  1.00 23.88 ? 217 VAL A CA  1 
ATOM   1858 C C   . VAL A 1 217 ? 19.384  28.486 78.887  1.00 24.40 ? 217 VAL A C   1 
ATOM   1859 O O   . VAL A 1 217 ? 20.431  27.856 78.667  1.00 21.91 ? 217 VAL A O   1 
ATOM   1860 C CB  . VAL A 1 217 ? 17.619  28.370 77.042  1.00 20.62 ? 217 VAL A CB  1 
ATOM   1861 C CG1 . VAL A 1 217 ? 18.180  27.028 76.599  1.00 25.87 ? 217 VAL A CG1 1 
ATOM   1862 C CG2 . VAL A 1 217 ? 16.401  28.153 77.891  1.00 27.69 ? 217 VAL A CG2 1 
ATOM   1863 N N   . LYS A 1 218 ? 18.863  28.609 80.110  1.00 20.29 ? 218 LYS A N   1 
ATOM   1864 C CA  . LYS A 1 218 ? 19.322  27.810 81.240  1.00 18.13 ? 218 LYS A CA  1 
ATOM   1865 C C   . LYS A 1 218 ? 18.434  26.583 81.371  1.00 15.51 ? 218 LYS A C   1 
ATOM   1866 O O   . LYS A 1 218 ? 17.207  26.694 81.317  1.00 16.98 ? 218 LYS A O   1 
ATOM   1867 C CB  . LYS A 1 218 ? 19.289  28.618 82.537  1.00 19.58 ? 218 LYS A CB  1 
ATOM   1868 C CG  . LYS A 1 218 ? 20.241  29.786 82.541  1.00 20.14 ? 218 LYS A CG  1 
ATOM   1869 C CD  . LYS A 1 218 ? 20.216  30.510 83.875  1.00 26.18 ? 218 LYS A CD  1 
ATOM   1870 C CE  . LYS A 1 218 ? 21.034  31.793 83.829  1.00 35.91 ? 218 LYS A CE  1 
ATOM   1871 N NZ  . LYS A 1 218 ? 21.172  32.390 85.190  1.00 45.83 ? 218 LYS A NZ  1 
ATOM   1872 N N   . ILE A 1 219 ? 19.044  25.411 81.514  1.00 13.32 ? 219 ILE A N   1 
ATOM   1873 C CA  . ILE A 1 219 ? 18.251  24.220 81.812  1.00 12.83 ? 219 ILE A CA  1 
ATOM   1874 C C   . ILE A 1 219 ? 18.847  23.526 83.029  1.00 17.31 ? 219 ILE A C   1 
ATOM   1875 O O   . ILE A 1 219 ? 20.022  23.722 83.370  1.00 16.72 ? 219 ILE A O   1 
ATOM   1876 C CB  . ILE A 1 219 ? 18.169  23.253 80.605  1.00 14.79 ? 219 ILE A CB  1 
ATOM   1877 C CG1 . ILE A 1 219 ? 19.503  22.555 80.387  1.00 18.33 ? 219 ILE A CG1 1 
ATOM   1878 C CG2 . ILE A 1 219 ? 17.689  23.968 79.340  1.00 17.01 ? 219 ILE A CG2 1 
ATOM   1879 C CD1 . ILE A 1 219 ? 19.464  21.432 79.342  1.00 20.54 ? 219 ILE A CD1 1 
ATOM   1880 N N   . PRO A 1 220 ? 18.060  22.712 83.706  1.00 12.96 ? 220 PRO A N   1 
ATOM   1881 C CA  . PRO A 1 220 ? 18.590  21.970 84.856  1.00 14.73 ? 220 PRO A CA  1 
ATOM   1882 C C   . PRO A 1 220 ? 19.551  20.849 84.497  1.00 12.64 ? 220 PRO A C   1 
ATOM   1883 O O   . PRO A 1 220 ? 19.797  20.539 83.325  1.00 13.85 ? 220 PRO A O   1 
ATOM   1884 C CB  . PRO A 1 220 ? 17.325  21.407 85.523  1.00 21.57 ? 220 PRO A CB  1 
ATOM   1885 C CG  . PRO A 1 220 ? 16.299  21.447 84.500  1.00 22.53 ? 220 PRO A CG  1 
ATOM   1886 C CD  . PRO A 1 220 ? 16.592  22.579 83.599  1.00 16.97 ? 220 PRO A CD  1 
ATOM   1887 N N   . ASP A 1 221 ? 20.094  20.244 85.545  1.00 13.31 ? 221 ASP A N   1 
ATOM   1888 C CA  . ASP A 1 221 ? 21.081  19.177 85.427  1.00 13.19 ? 221 ASP A CA  1 
ATOM   1889 C C   . ASP A 1 221 ? 20.352  17.875 85.119  1.00 14.27 ? 221 ASP A C   1 
ATOM   1890 O O   . ASP A 1 221 ? 19.732  17.294 86.008  1.00 15.83 ? 221 ASP A O   1 
ATOM   1891 C CB  . ASP A 1 221 ? 21.859  19.072 86.734  1.00 15.77 ? 221 ASP A CB  1 
ATOM   1892 C CG  . ASP A 1 221 ? 23.016  18.101 86.652  1.00 21.40 ? 221 ASP A CG  1 
ATOM   1893 O OD1 . ASP A 1 221 ? 23.555  17.912 85.557  1.00 18.71 ? 221 ASP A OD1 1 
ATOM   1894 O OD2 . ASP A 1 221 ? 23.385  17.528 87.691  1.00 31.24 ? 221 ASP A OD2 1 
ATOM   1895 N N   . PHE A 1 222 ? 20.423  17.403 83.872  1.00 12.83 ? 222 PHE A N   1 
ATOM   1896 C CA  . PHE A 1 222 ? 19.723  16.165 83.505  1.00 11.63 ? 222 PHE A CA  1 
ATOM   1897 C C   . PHE A 1 222 ? 20.554  14.957 83.930  1.00 15.73 ? 222 PHE A C   1 
ATOM   1898 O O   . PHE A 1 222 ? 21.202  14.288 83.124  1.00 15.70 ? 222 PHE A O   1 
ATOM   1899 C CB  . PHE A 1 222 ? 19.401  16.160 82.013  1.00 11.02 ? 222 PHE A CB  1 
ATOM   1900 C CG  . PHE A 1 222 ? 18.130  16.908 81.689  1.00 10.66 ? 222 PHE A CG  1 
ATOM   1901 C CD1 . PHE A 1 222 ? 18.119  18.297 81.636  1.00 12.52 ? 222 PHE A CD1 1 
ATOM   1902 C CD2 . PHE A 1 222 ? 16.936  16.220 81.483  1.00 13.74 ? 222 PHE A CD2 1 
ATOM   1903 C CE1 . PHE A 1 222 ? 16.946  18.992 81.354  1.00 13.05 ? 222 PHE A CE1 1 
ATOM   1904 C CE2 . PHE A 1 222 ? 15.769  16.905 81.195  1.00 15.36 ? 222 PHE A CE2 1 
ATOM   1905 C CZ  . PHE A 1 222 ? 15.769  18.293 81.133  1.00 14.91 ? 222 PHE A CZ  1 
ATOM   1906 N N   . ALA A 1 223 ? 20.500  14.662 85.235  1.00 14.95 ? 223 ALA A N   1 
ATOM   1907 C CA  . ALA A 1 223 ? 21.330  13.631 85.848  1.00 16.84 ? 223 ALA A CA  1 
ATOM   1908 C C   . ALA A 1 223 ? 20.794  12.215 85.649  1.00 18.92 ? 223 ALA A C   1 
ATOM   1909 O O   . ALA A 1 223 ? 21.363  11.271 86.210  1.00 22.51 ? 223 ALA A O   1 
ATOM   1910 C CB  . ALA A 1 223 ? 21.486  13.913 87.345  1.00 21.99 ? 223 ALA A CB  1 
ATOM   1911 N N   . VAL A 1 224 ? 19.719  12.058 84.880  1.00 17.86 ? 224 VAL A N   1 
ATOM   1912 C CA  . VAL A 1 224 ? 19.111  10.770 84.570  1.00 14.39 ? 224 VAL A CA  1 
ATOM   1913 C C   . VAL A 1 224 ? 18.805  10.752 83.075  1.00 15.21 ? 224 VAL A C   1 
ATOM   1914 O O   . VAL A 1 224 ? 18.630  11.797 82.444  1.00 16.31 ? 224 VAL A O   1 
ATOM   1915 C CB  . VAL A 1 224 ? 17.837  10.550 85.422  1.00 22.59 ? 224 VAL A CB  1 
ATOM   1916 C CG1 . VAL A 1 224 ? 16.667  11.351 84.860  1.00 19.24 ? 224 VAL A CG1 1 
ATOM   1917 C CG2 . VAL A 1 224 ? 17.509  9.075  85.551  1.00 34.62 ? 224 VAL A CG2 1 
ATOM   1918 N N   . SER A 1 225 ? 18.731  9.552  82.504  1.00 15.58 ? 225 SER A N   1 
ATOM   1919 C CA  . SER A 1 225 ? 18.436  9.382  81.082  1.00 12.92 ? 225 SER A CA  1 
ATOM   1920 C C   . SER A 1 225 ? 16.944  9.127  80.878  1.00 13.21 ? 225 SER A C   1 
ATOM   1921 O O   . SER A 1 225 ? 16.364  8.260  81.537  1.00 16.71 ? 225 SER A O   1 
ATOM   1922 C CB  . SER A 1 225 ? 19.233  8.224  80.479  1.00 18.49 ? 225 SER A CB  1 
ATOM   1923 O OG  . SER A 1 225 ? 18.786  7.951  79.147  1.00 17.04 ? 225 SER A OG  1 
ATOM   1924 N N   . PHE A 1 226 ? 16.340  9.877  79.953  1.00 11.96 ? 226 PHE A N   1 
ATOM   1925 C CA  . PHE A 1 226 ? 14.958  9.684  79.519  1.00 11.52 ? 226 PHE A CA  1 
ATOM   1926 C C   . PHE A 1 226 ? 14.871  8.998  78.158  1.00 10.57 ? 226 PHE A C   1 
ATOM   1927 O O   . PHE A 1 226 ? 13.786  8.943  77.567  1.00 14.12 ? 226 PHE A O   1 
ATOM   1928 C CB  . PHE A 1 226 ? 14.224  11.029 79.460  1.00 10.90 ? 226 PHE A CB  1 
ATOM   1929 C CG  . PHE A 1 226 ? 13.974  11.644 80.806  1.00 14.69 ? 226 PHE A CG  1 
ATOM   1930 C CD1 . PHE A 1 226 ? 12.927  11.201 81.612  1.00 16.01 ? 226 PHE A CD1 1 
ATOM   1931 C CD2 . PHE A 1 226 ? 14.785  12.671 81.263  1.00 17.04 ? 226 PHE A CD2 1 
ATOM   1932 C CE1 . PHE A 1 226 ? 12.699  11.784 82.855  1.00 13.93 ? 226 PHE A CE1 1 
ATOM   1933 C CE2 . PHE A 1 226 ? 14.562  13.261 82.503  1.00 20.20 ? 226 PHE A CE2 1 
ATOM   1934 C CZ  . PHE A 1 226 ? 13.530  12.819 83.297  1.00 15.42 ? 226 PHE A CZ  1 
ATOM   1935 N N   . ARG A 1 227 ? 15.983  8.467  77.655  1.00 12.36 ? 227 ARG A N   1 
ATOM   1936 C CA  . ARG A 1 227 ? 15.970  7.903  76.306  1.00 14.02 ? 227 ARG A CA  1 
ATOM   1937 C C   . ARG A 1 227 ? 15.084  6.661  76.207  1.00 15.79 ? 227 ARG A C   1 
ATOM   1938 O O   . ARG A 1 227 ? 14.377  6.481  75.207  1.00 16.67 ? 227 ARG A O   1 
ATOM   1939 C CB  . ARG A 1 227 ? 17.393  7.589  75.858  1.00 18.57 ? 227 ARG A CB  1 
ATOM   1940 C CG  . ARG A 1 227 ? 18.249  8.849  75.690  1.00 20.07 ? 227 ARG A CG  1 
ATOM   1941 C CD  . ARG A 1 227 ? 19.654  8.497  75.229  1.00 24.03 ? 227 ARG A CD  1 
ATOM   1942 N NE  . ARG A 1 227 ? 19.652  7.797  73.948  1.00 25.97 ? 227 ARG A NE  1 
ATOM   1943 C CZ  . ARG A 1 227 ? 19.634  8.416  72.772  1.00 31.85 ? 227 ARG A CZ  1 
ATOM   1944 N NH1 . ARG A 1 227 ? 19.604  9.744  72.722  1.00 23.03 ? 227 ARG A NH1 1 
ATOM   1945 N NH2 . ARG A 1 227 ? 19.648  7.714  71.648  1.00 37.16 ? 227 ARG A NH2 1 
ATOM   1946 N N   . GLU A 1 228 ? 15.117  5.779  77.209  1.00 13.34 ? 228 GLU A N   1 
ATOM   1947 C CA  . GLU A 1 228 ? 14.248  4.609  77.145  1.00 16.39 ? 228 GLU A CA  1 
ATOM   1948 C C   . GLU A 1 228 ? 12.785  5.018  77.251  1.00 14.75 ? 228 GLU A C   1 
ATOM   1949 O O   . GLU A 1 228 ? 11.921  4.449  76.573  1.00 15.51 ? 228 GLU A O   1 
ATOM   1950 C CB  . GLU A 1 228 ? 14.615  3.606  78.242  1.00 18.58 ? 228 GLU A CB  1 
ATOM   1951 C CG  . GLU A 1 228 ? 13.627  2.453  78.411  1.00 36.65 ? 228 GLU A CG  1 
ATOM   1952 C CD  . GLU A 1 228 ? 13.870  1.300  77.451  1.00 61.11 ? 228 GLU A CD  1 
ATOM   1953 O OE1 . GLU A 1 228 ? 13.981  1.539  76.231  1.00 66.72 ? 228 GLU A OE1 1 
ATOM   1954 O OE2 . GLU A 1 228 ? 13.945  0.144  77.924  1.00 70.08 ? 228 GLU A OE2 1 
ATOM   1955 N N   . ASP A 1 229 ? 12.488  6.010  78.087  1.00 14.57 ? 229 ASP A N   1 
ATOM   1956 C CA  . ASP A 1 229 ? 11.115  6.482  78.186  1.00 12.26 ? 229 ASP A CA  1 
ATOM   1957 C C   . ASP A 1 229 ? 10.609  7.016  76.853  1.00 14.06 ? 229 ASP A C   1 
ATOM   1958 O O   . ASP A 1 229 ? 9.448   6.791  76.493  1.00 13.86 ? 229 ASP A O   1 
ATOM   1959 C CB  . ASP A 1 229 ? 11.007  7.552  79.267  1.00 10.64 ? 229 ASP A CB  1 
ATOM   1960 C CG  . ASP A 1 229 ? 10.961  6.953  80.660  1.00 14.52 ? 229 ASP A CG  1 
ATOM   1961 O OD1 . ASP A 1 229 ? 10.987  5.709  80.795  1.00 20.29 ? 229 ASP A OD1 1 
ATOM   1962 O OD2 . ASP A 1 229 ? 10.893  7.728  81.635  1.00 17.07 ? 229 ASP A OD2 1 
ATOM   1963 N N   . ALA A 1 230 ? 11.453  7.747  76.121  1.00 12.13 ? 230 ALA A N   1 
ATOM   1964 C CA  . ALA A 1 230 ? 11.063  8.216  74.797  1.00 13.71 ? 230 ALA A CA  1 
ATOM   1965 C C   . ALA A 1 230 ? 10.608  7.043  73.938  1.00 10.84 ? 230 ALA A C   1 
ATOM   1966 O O   . ALA A 1 230 ? 9.562   7.101  73.284  1.00 13.92 ? 230 ALA A O   1 
ATOM   1967 C CB  . ALA A 1 230 ? 12.221  8.960  74.127  1.00 15.90 ? 230 ALA A CB  1 
ATOM   1968 N N   . SER A 1 231 ? 11.388  5.963  73.947  1.00 12.68 ? 231 SER A N   1 
ATOM   1969 C CA  . SER A 1 231 ? 11.014  4.760  73.210  1.00 13.52 ? 231 SER A CA  1 
ATOM   1970 C C   . SER A 1 231 ? 9.685   4.201  73.689  1.00 16.99 ? 231 SER A C   1 
ATOM   1971 O O   . SER A 1 231 ? 8.846   3.788  72.876  1.00 17.53 ? 231 SER A O   1 
ATOM   1972 C CB  . SER A 1 231 ? 12.092  3.683  73.367  1.00 19.78 ? 231 SER A CB  1 
ATOM   1973 O OG  . SER A 1 231 ? 13.037  3.742  72.329  1.00 31.52 ? 231 SER A OG  1 
ATOM   1974 N N   . LYS A 1 232 ? 9.494   4.148  75.011  1.00 13.78 ? 232 LYS A N   1 
ATOM   1975 C CA  . LYS A 1 232 ? 8.261   3.601  75.566  1.00 14.45 ? 232 LYS A CA  1 
ATOM   1976 C C   . LYS A 1 232 ? 7.039   4.401  75.130  1.00 14.85 ? 232 LYS A C   1 
ATOM   1977 O O   . LYS A 1 232 ? 6.000   3.813  74.792  1.00 13.23 ? 232 LYS A O   1 
ATOM   1978 C CB  . LYS A 1 232 ? 8.350   3.547  77.092  1.00 16.23 ? 232 LYS A CB  1 
ATOM   1979 C CG  . LYS A 1 232 ? 9.283   2.455  77.612  1.00 26.17 ? 232 LYS A CG  1 
ATOM   1980 C CD  . LYS A 1 232 ? 9.080   2.202  79.104  1.00 33.33 ? 232 LYS A CD  1 
ATOM   1981 C CE  . LYS A 1 232 ? 7.600   2.008  79.433  1.00 47.33 ? 232 LYS A CE  1 
ATOM   1982 N NZ  . LYS A 1 232 ? 7.356   0.921  80.434  1.00 56.85 ? 232 LYS A NZ  1 
ATOM   1983 N N   . HIS A 1 233 ? 7.129   5.737  75.146  1.00 12.94 ? 233 HIS A N   1 
ATOM   1984 C CA  . HIS A 1 233 ? 5.996   6.545  74.684  1.00 12.31 ? 233 HIS A CA  1 
ATOM   1985 C C   . HIS A 1 233 ? 5.598   6.146  73.272  1.00 10.50 ? 233 HIS A C   1 
ATOM   1986 O O   . HIS A 1 233 ? 4.404   6.003  72.971  1.00 11.91 ? 233 HIS A O   1 
ATOM   1987 C CB  . HIS A 1 233 ? 6.318   8.039  74.693  1.00 12.18 ? 233 HIS A CB  1 
ATOM   1988 C CG  . HIS A 1 233 ? 6.261   8.699  76.040  1.00 12.19 ? 233 HIS A CG  1 
ATOM   1989 N ND1 . HIS A 1 233 ? 5.093   9.190  76.590  1.00 12.68 ? 233 HIS A ND1 1 
ATOM   1990 C CD2 . HIS A 1 233 ? 7.250   9.020  76.909  1.00 12.16 ? 233 HIS A CD2 1 
ATOM   1991 C CE1 . HIS A 1 233 ? 5.360   9.745  77.760  1.00 10.89 ? 233 HIS A CE1 1 
ATOM   1992 N NE2 . HIS A 1 233 ? 6.664   9.669  77.970  1.00 10.92 ? 233 HIS A NE2 1 
ATOM   1993 N N   . VAL A 1 234 ? 6.589   5.940  72.400  1.00 14.52 ? 234 VAL A N   1 
ATOM   1994 C CA  . VAL A 1 234 ? 6.277   5.581  71.022  1.00 14.60 ? 234 VAL A CA  1 
ATOM   1995 C C   . VAL A 1 234 ? 5.706   4.172  70.958  1.00 14.27 ? 234 VAL A C   1 
ATOM   1996 O O   . VAL A 1 234 ? 4.685   3.931  70.296  1.00 12.22 ? 234 VAL A O   1 
ATOM   1997 C CB  . VAL A 1 234 ? 7.508   5.737  70.120  1.00 14.57 ? 234 VAL A CB  1 
ATOM   1998 C CG1 . VAL A 1 234 ? 7.148   5.321  68.689  1.00 15.07 ? 234 VAL A CG1 1 
ATOM   1999 C CG2 . VAL A 1 234 ? 7.988   7.200  70.151  1.00 12.89 ? 234 VAL A CG2 1 
ATOM   2000 N N   . GLU A 1 235 ? 6.347   3.224  71.656  1.00 10.31 ? 235 GLU A N   1 
ATOM   2001 C CA  . GLU A 1 235 ? 5.921   1.829  71.583  1.00 11.21 ? 235 GLU A CA  1 
ATOM   2002 C C   . GLU A 1 235 ? 4.522   1.658  72.156  1.00 15.96 ? 235 GLU A C   1 
ATOM   2003 O O   . GLU A 1 235 ? 3.674   0.977  71.570  1.00 16.08 ? 235 GLU A O   1 
ATOM   2004 C CB  . GLU A 1 235 ? 6.912   0.945  72.333  1.00 15.12 ? 235 GLU A CB  1 
ATOM   2005 C CG  . GLU A 1 235 ? 7.924   0.259  71.439  1.00 36.62 ? 235 GLU A CG  1 
ATOM   2006 C CD  . GLU A 1 235 ? 7.273   -0.531 70.315  1.00 45.98 ? 235 GLU A CD  1 
ATOM   2007 O OE1 . GLU A 1 235 ? 7.746   -0.425 69.165  1.00 48.95 ? 235 GLU A OE1 1 
ATOM   2008 O OE2 . GLU A 1 235 ? 6.289   -1.257 70.583  1.00 52.79 ? 235 GLU A OE2 1 
ATOM   2009 N N   . LEU A 1 236 ? 4.262   2.269  73.313  1.00 11.27 ? 236 LEU A N   1 
ATOM   2010 C CA  . LEU A 1 236 ? 2.944   2.125  73.917  1.00 12.95 ? 236 LEU A CA  1 
ATOM   2011 C C   . LEU A 1 236 ? 1.858   2.767  73.065  1.00 12.39 ? 236 LEU A C   1 
ATOM   2012 O O   . LEU A 1 236 ? 0.718   2.278  73.054  1.00 12.00 ? 236 LEU A O   1 
ATOM   2013 C CB  . LEU A 1 236 ? 2.935   2.727  75.325  1.00 13.19 ? 236 LEU A CB  1 
ATOM   2014 C CG  . LEU A 1 236 ? 3.793   2.011  76.367  1.00 16.74 ? 236 LEU A CG  1 
ATOM   2015 C CD1 . LEU A 1 236 ? 3.865   2.861  77.629  1.00 17.56 ? 236 LEU A CD1 1 
ATOM   2016 C CD2 . LEU A 1 236 ? 3.246   0.621  76.670  1.00 19.25 ? 236 LEU A CD2 1 
ATOM   2017 N N   . ALA A 1 237 ? 2.183   3.868  72.377  1.00 11.09 ? 237 ALA A N   1 
ATOM   2018 C CA  . ALA A 1 237 ? 1.226   4.497  71.470  1.00 13.12 ? 237 ALA A CA  1 
ATOM   2019 C C   . ALA A 1 237 ? 0.888   3.573  70.311  1.00 11.95 ? 237 ALA A C   1 
ATOM   2020 O O   . ALA A 1 237 ? -0.273  3.477  69.906  1.00 13.39 ? 237 ALA A O   1 
ATOM   2021 C CB  . ALA A 1 237 ? 1.781   5.815  70.929  1.00 12.40 ? 237 ALA A CB  1 
ATOM   2022 N N   . LYS A 1 238 ? 1.894   2.889  69.763  1.00 13.87 ? 238 LYS A N   1 
ATOM   2023 C CA  . LYS A 1 238 ? 1.614   1.895  68.727  1.00 14.55 ? 238 LYS A CA  1 
ATOM   2024 C C   . LYS A 1 238 ? 0.641   0.832  69.224  1.00 15.41 ? 238 LYS A C   1 
ATOM   2025 O O   . LYS A 1 238 ? -0.272  0.427  68.491  1.00 15.79 ? 238 LYS A O   1 
ATOM   2026 C CB  . LYS A 1 238 ? 2.915   1.246  68.248  1.00 11.99 ? 238 LYS A CB  1 
ATOM   2027 C CG  . LYS A 1 238 ? 3.789   2.202  67.403  1.00 13.38 ? 238 LYS A CG  1 
ATOM   2028 C CD  . LYS A 1 238 ? 5.161   1.589  67.117  1.00 17.63 ? 238 LYS A CD  1 
ATOM   2029 C CE  . LYS A 1 238 ? 5.040   0.290  66.354  1.00 23.98 ? 238 LYS A CE  1 
ATOM   2030 N NZ  . LYS A 1 238 ? 6.368   -0.194 65.893  1.00 24.47 ? 238 LYS A NZ  1 
ATOM   2031 N N   . GLU A 1 239 ? 0.824   0.356  70.466  1.00 13.26 ? 239 GLU A N   1 
ATOM   2032 C CA  . GLU A 1 239 ? -0.063  -0.668 71.013  1.00 14.44 ? 239 GLU A CA  1 
ATOM   2033 C C   . GLU A 1 239 ? -1.471  -0.137 71.231  1.00 18.73 ? 239 GLU A C   1 
ATOM   2034 O O   . GLU A 1 239 ? -2.446  -0.845 70.958  1.00 15.65 ? 239 GLU A O   1 
ATOM   2035 C CB  . GLU A 1 239 ? 0.498   -1.218 72.324  1.00 16.45 ? 239 GLU A CB  1 
ATOM   2036 C CG  . GLU A 1 239 ? 1.915   -1.754 72.225  1.00 30.09 ? 239 GLU A CG  1 
ATOM   2037 C CD  . GLU A 1 239 ? 2.448   -2.247 73.562  1.00 52.82 ? 239 GLU A CD  1 
ATOM   2038 O OE1 . GLU A 1 239 ? 1.629   -2.592 74.443  1.00 58.53 ? 239 GLU A OE1 1 
ATOM   2039 O OE2 . GLU A 1 239 ? 3.687   -2.284 73.733  1.00 58.28 ? 239 GLU A OE2 1 
ATOM   2040 N N   . LYS A 1 240 ? -1.605  1.094  71.744  1.00 15.49 ? 240 LYS A N   1 
ATOM   2041 C CA  . LYS A 1 240 ? -2.949  1.611  71.981  1.00 12.97 ? 240 LYS A CA  1 
ATOM   2042 C C   . LYS A 1 240 ? -3.693  1.809  70.666  1.00 14.93 ? 240 LYS A C   1 
ATOM   2043 O O   . LYS A 1 240 ? -4.870  1.431  70.545  1.00 16.45 ? 240 LYS A O   1 
ATOM   2044 C CB  . LYS A 1 240 ? -2.900  2.923  72.775  1.00 11.58 ? 240 LYS A CB  1 
ATOM   2045 C CG  . LYS A 1 240 ? -4.293  3.459  73.143  1.00 14.90 ? 240 LYS A CG  1 
ATOM   2046 C CD  . LYS A 1 240 ? -4.902  2.664  74.275  1.00 15.34 ? 240 LYS A CD  1 
ATOM   2047 C CE  . LYS A 1 240 ? -6.359  3.026  74.487  1.00 18.97 ? 240 LYS A CE  1 
ATOM   2048 N NZ  . LYS A 1 240 ? -6.905  2.247  75.621  1.00 18.48 ? 240 LYS A NZ  1 
ATOM   2049 N N   . TYR A 1 241 ? -3.015  2.397  69.686  1.00 13.32 ? 241 TYR A N   1 
ATOM   2050 C CA  . TYR A 1 241 ? -3.614  2.644  68.380  1.00 13.92 ? 241 TYR A CA  1 
ATOM   2051 C C   . TYR A 1 241 ? -3.957  1.337  67.673  1.00 16.02 ? 241 TYR A C   1 
ATOM   2052 O O   . TYR A 1 241 ? -4.808  1.306  66.784  1.00 14.93 ? 241 TYR A O   1 
ATOM   2053 C CB  . TYR A 1 241 ? -2.675  3.482  67.510  1.00 10.56 ? 241 TYR A CB  1 
ATOM   2054 C CG  . TYR A 1 241 ? -3.182  3.707  66.103  1.00 10.30 ? 241 TYR A CG  1 
ATOM   2055 C CD1 . TYR A 1 241 ? -3.145  2.689  65.159  1.00 11.19 ? 241 TYR A CD1 1 
ATOM   2056 C CD2 . TYR A 1 241 ? -3.698  4.938  65.718  1.00 11.86 ? 241 TYR A CD2 1 
ATOM   2057 C CE1 . TYR A 1 241 ? -3.607  2.890  63.873  1.00 17.61 ? 241 TYR A CE1 1 
ATOM   2058 C CE2 . TYR A 1 241 ? -4.162  5.148  64.434  1.00 12.50 ? 241 TYR A CE2 1 
ATOM   2059 C CZ  . TYR A 1 241 ? -4.114  4.121  63.515  1.00 11.67 ? 241 TYR A CZ  1 
ATOM   2060 O OH  . TYR A 1 241 ? -4.576  4.326  62.235  1.00 15.39 ? 241 TYR A OH  1 
ATOM   2061 N N   . PHE A 1 242 ? -3.281  0.246  68.058  1.00 13.59 ? 242 PHE A N   1 
ATOM   2062 C CA  . PHE A 1 242 ? -3.533  -1.107 67.520  1.00 19.14 ? 242 PHE A CA  1 
ATOM   2063 C C   . PHE A 1 242 ? -4.782  -1.694 68.181  1.00 16.84 ? 242 PHE A C   1 
ATOM   2064 O O   . PHE A 1 242 ? -5.558  -2.311 67.543  1.00 18.95 ? 242 PHE A O   1 
ATOM   2065 C CB  . PHE A 1 242 ? -2.313  -2.022 67.744  1.00 17.99 ? 242 PHE A CB  1 
ATOM   2066 C CG  . PHE A 1 242 ? -2.473  -3.449 67.285  1.00 23.15 ? 242 PHE A CG  1 
ATOM   2067 C CD1 . PHE A 1 242 ? -2.581  -3.740 65.984  1.00 27.21 ? 242 PHE A CD1 1 
ATOM   2068 C CD2 . PHE A 1 242 ? -2.323  -4.450 68.167  1.00 36.19 ? 242 PHE A CD2 1 
ATOM   2069 C CE1 . PHE A 1 242 ? -2.646  -5.031 65.550  1.00 34.94 ? 242 PHE A CE1 1 
ATOM   2070 C CE2 . PHE A 1 242 ? -2.405  -5.767 67.761  1.00 39.88 ? 242 PHE A CE2 1 
ATOM   2071 C CZ  . PHE A 1 242 ? -2.575  -6.034 66.450  1.00 37.25 ? 242 PHE A CZ  1 
ATOM   2072 N N   . GLU A 1 243 ? -4.943  -1.482 69.466  1.00 15.26 ? 243 GLU A N   1 
ATOM   2073 C CA  . GLU A 1 243 ? -6.116  -1.954 70.177  1.00 17.27 ? 243 GLU A CA  1 
ATOM   2074 C C   . GLU A 1 243 ? -7.410  -1.390 69.538  1.00 22.36 ? 243 GLU A C   1 
ATOM   2075 O O   . GLU A 1 243 ? -8.416  -2.029 69.452  1.00 19.99 ? 243 GLU A O   1 
ATOM   2076 C CB  . GLU A 1 243 ? -6.069  -1.480 71.668  1.00 23.04 ? 243 GLU A CB  1 
ATOM   2077 C CG  . GLU A 1 243 ? -7.407  -1.510 72.455  1.00 29.72 ? 243 GLU A CG  1 
ATOM   2078 C CD  . GLU A 1 243 ? -7.512  -0.744 73.831  1.00 36.54 ? 243 GLU A CD  1 
ATOM   2079 O OE1 . GLU A 1 243 ? -6.532  -0.439 74.451  1.00 28.31 ? 243 GLU A OE1 1 
ATOM   2080 O OE2 . GLU A 1 243 ? -8.628  -0.523 74.292  1.00 33.41 ? 243 GLU A OE2 1 
ATOM   2081 N N   . ILE A 1 244 ? -7.336  -0.175 69.042  1.00 14.43 ? 244 ILE A N   1 
ATOM   2082 C CA  . ILE A 1 244 ? -8.518  0.594  68.673  1.00 16.00 ? 244 ILE A CA  1 
ATOM   2083 C C   . ILE A 1 244 ? -8.834  0.443  67.188  1.00 16.61 ? 244 ILE A C   1 
ATOM   2084 O O   . ILE A 1 244 ? -9.997  0.448  66.787  1.00 17.41 ? 244 ILE A O   1 
ATOM   2085 C CB  . ILE A 1 244 ? -8.345  2.088  69.002  1.00 15.94 ? 244 ILE A CB  1 
ATOM   2086 C CG1 . ILE A 1 244 ? -8.089  2.279  70.498  1.00 18.66 ? 244 ILE A CG1 1 
ATOM   2087 C CG2 . ILE A 1 244 ? -9.569  2.876  68.561  1.00 16.33 ? 244 ILE A CG2 1 
ATOM   2088 C CD1 . ILE A 1 244 ? -9.270  1.918  71.371  1.00 24.00 ? 244 ILE A CD1 1 
ATOM   2089 N N   . PHE A 1 245 ? -7.789  0.309  66.377  1.00 13.47 ? 245 PHE A N   1 
ATOM   2090 C CA  . PHE A 1 245 ? -7.950  0.160  64.964  1.00 15.31 ? 245 PHE A CA  1 
ATOM   2091 C C   . PHE A 1 245 ? -7.532  -1.145 64.296  1.00 15.55 ? 245 PHE A C   1 
ATOM   2092 O O   . PHE A 1 245 ? -7.763  -1.283 63.185  1.00 16.92 ? 245 PHE A O   1 
ATOM   2093 C CB  . PHE A 1 245 ? -7.221  1.322  64.239  1.00 11.54 ? 245 PHE A CB  1 
ATOM   2094 C CG  . PHE A 1 245 ? -7.692  2.691  64.643  1.00 14.95 ? 245 PHE A CG  1 
ATOM   2095 C CD1 . PHE A 1 245 ? -8.901  3.147  64.228  1.00 18.36 ? 245 PHE A CD1 1 
ATOM   2096 C CD2 . PHE A 1 245 ? -6.977  3.474  65.477  1.00 12.31 ? 245 PHE A CD2 1 
ATOM   2097 C CE1 . PHE A 1 245 ? -9.362  4.389  64.592  1.00 15.30 ? 245 PHE A CE1 1 
ATOM   2098 C CE2 . PHE A 1 245 ? -7.441  4.692  65.873  1.00 13.42 ? 245 PHE A CE2 1 
ATOM   2099 C CZ  . PHE A 1 245 ? -8.621  5.147  65.429  1.00 15.53 ? 245 PHE A CZ  1 
ATOM   2100 N N   . GLY A 1 246 ? -6.941  -2.040 65.043  1.00 16.41 ? 246 GLY A N   1 
ATOM   2101 C CA  . GLY A 1 246 ? -6.515  -3.309 64.529  1.00 17.44 ? 246 GLY A CA  1 
ATOM   2102 C C   . GLY A 1 246 ? -5.221  -3.393 63.763  1.00 23.89 ? 246 GLY A C   1 
ATOM   2103 O O   . GLY A 1 246 ? -4.869  -4.464 63.285  1.00 22.60 ? 246 GLY A O   1 
ATOM   2104 N N   . GLU A 1 247 ? -4.531  -2.276 63.641  1.00 22.30 ? 247 GLU A N   1 
ATOM   2105 C CA  . GLU A 1 247 ? -3.263  -2.216 62.958  1.00 20.83 ? 247 GLU A CA  1 
ATOM   2106 C C   . GLU A 1 247 ? -2.351  -1.240 63.675  1.00 22.03 ? 247 GLU A C   1 
ATOM   2107 O O   . GLU A 1 247 ? -2.802  -0.450 64.384  1.00 18.63 ? 247 GLU A O   1 
ATOM   2108 C CB  . GLU A 1 247 ? -3.417  -1.725 61.539  1.00 27.14 ? 247 GLU A CB  1 
ATOM   2109 C CG  . GLU A 1 247 ? -4.141  -0.434 61.394  1.00 31.73 ? 247 GLU A CG  1 
ATOM   2110 C CD  . GLU A 1 247 ? -3.984  0.240  60.030  1.00 45.16 ? 247 GLU A CD  1 
ATOM   2111 O OE1 . GLU A 1 247 ? -4.492  1.298  59.782  1.00 46.01 ? 247 GLU A OE1 1 
ATOM   2112 O OE2 . GLU A 1 247 ? -3.268  -0.146 59.197  1.00 50.30 ? 247 GLU A OE2 1 
ATOM   2113 N N   . HIS A 1 248 ? -1.077  -1.371 63.422  1.00 16.79 ? 248 HIS A N   1 
ATOM   2114 C CA  . HIS A 1 248 ? -0.125  -0.474 64.000  1.00 18.33 ? 248 HIS A CA  1 
ATOM   2115 C C   . HIS A 1 248 ? -0.128  0.782  63.155  1.00 20.32 ? 248 HIS A C   1 
ATOM   2116 O O   . HIS A 1 248 ? -0.294  0.708  61.996  1.00 20.07 ? 248 HIS A O   1 
ATOM   2117 C CB  . HIS A 1 248 ? 1.259   -1.097 63.996  1.00 18.38 ? 248 HIS A CB  1 
ATOM   2118 C CG  . HIS A 1 248 ? 1.413   -2.155 65.042  1.00 25.07 ? 248 HIS A CG  1 
ATOM   2119 N ND1 . HIS A 1 248 ? 1.575   -3.483 64.734  1.00 31.83 ? 248 HIS A ND1 1 
ATOM   2120 C CD2 . HIS A 1 248 ? 1.363   -2.089 66.386  1.00 26.02 ? 248 HIS A CD2 1 
ATOM   2121 C CE1 . HIS A 1 248 ? 1.634   -4.182 65.842  1.00 34.82 ? 248 HIS A CE1 1 
ATOM   2122 N NE2 . HIS A 1 248 ? 1.509   -3.365 66.862  1.00 31.23 ? 248 HIS A NE2 1 
ATOM   2123 N N   . PRO A 1 249 ? 0.068   1.929  63.782  1.00 15.59 ? 249 PRO A N   1 
ATOM   2124 C CA  . PRO A 1 249 ? 0.076   3.189  63.029  1.00 12.54 ? 249 PRO A CA  1 
ATOM   2125 C C   . PRO A 1 249 ? 1.343   3.322  62.206  1.00 21.30 ? 249 PRO A C   1 
ATOM   2126 O O   . PRO A 1 249 ? 2.432   2.949  62.643  1.00 20.22 ? 249 PRO A O   1 
ATOM   2127 C CB  . PRO A 1 249 ? 0.012   4.253  64.128  1.00 15.84 ? 249 PRO A CB  1 
ATOM   2128 C CG  . PRO A 1 249 ? 0.717   3.580  65.306  1.00 12.43 ? 249 PRO A CG  1 
ATOM   2129 C CD  . PRO A 1 249 ? 0.330   2.125  65.219  1.00 14.48 ? 249 PRO A CD  1 
ATOM   2130 N N   . VAL A 1 250 ? 1.196   3.846  60.994  1.00 17.74 ? 250 VAL A N   1 
ATOM   2131 C CA  . VAL A 1 250 ? 2.355   4.196  60.184  1.00 16.52 ? 250 VAL A CA  1 
ATOM   2132 C C   . VAL A 1 250 ? 2.536   5.696  60.060  1.00 11.82 ? 250 VAL A C   1 
ATOM   2133 O O   . VAL A 1 250 ? 3.563   6.132  59.523  1.00 17.63 ? 250 VAL A O   1 
ATOM   2134 C CB  . VAL A 1 250 ? 2.294   3.554  58.783  1.00 21.30 ? 250 VAL A CB  1 
ATOM   2135 C CG1 . VAL A 1 250 ? 2.296   2.034  58.908  1.00 23.68 ? 250 VAL A CG1 1 
ATOM   2136 C CG2 . VAL A 1 250 ? 1.072   4.051  58.048  1.00 22.15 ? 250 VAL A CG2 1 
ATOM   2137 N N   . TYR A 1 251 ? 1.581   6.497  60.536  1.00 15.28 ? 251 TYR A N   1 
ATOM   2138 C CA  . TYR A 1 251 ? 1.720   7.944  60.622  1.00 14.92 ? 251 TYR A CA  1 
ATOM   2139 C C   . TYR A 1 251 ? 1.669   8.365  62.080  1.00 16.10 ? 251 TYR A C   1 
ATOM   2140 O O   . TYR A 1 251 ? 0.849   7.857  62.850  1.00 14.47 ? 251 TYR A O   1 
ATOM   2141 C CB  . TYR A 1 251 ? 0.608   8.679  59.850  1.00 17.11 ? 251 TYR A CB  1 
ATOM   2142 C CG  . TYR A 1 251 ? 0.297   7.996  58.556  1.00 15.74 ? 251 TYR A CG  1 
ATOM   2143 C CD1 . TYR A 1 251 ? 1.270   7.890  57.577  1.00 29.94 ? 251 TYR A CD1 1 
ATOM   2144 C CD2 . TYR A 1 251 ? -0.937  7.398  58.327  1.00 23.59 ? 251 TYR A CD2 1 
ATOM   2145 C CE1 . TYR A 1 251 ? 1.024   7.247  56.396  1.00 33.03 ? 251 TYR A CE1 1 
ATOM   2146 C CE2 . TYR A 1 251 ? -1.192  6.746  57.127  1.00 24.02 ? 251 TYR A CE2 1 
ATOM   2147 C CZ  . TYR A 1 251 ? -0.198  6.680  56.170  1.00 35.35 ? 251 TYR A CZ  1 
ATOM   2148 O OH  . TYR A 1 251 ? -0.400  6.034  54.973  1.00 44.76 ? 251 TYR A OH  1 
ATOM   2149 N N   . MET A 1 252 ? 2.544   9.295  62.457  1.00 11.32 ? 252 MET A N   1 
ATOM   2150 C CA  . MET A 1 252 ? 2.463   9.898  63.775  1.00 10.76 ? 252 MET A CA  1 
ATOM   2151 C C   . MET A 1 252 ? 2.578   11.409 63.671  1.00 12.63 ? 252 MET A C   1 
ATOM   2152 O O   . MET A 1 252 ? 3.294   11.947 62.815  1.00 11.61 ? 252 MET A O   1 
ATOM   2153 C CB  . MET A 1 252 ? 3.544   9.383  64.721  1.00 15.96 ? 252 MET A CB  1 
ATOM   2154 C CG  . MET A 1 252 ? 3.281   7.981  65.231  1.00 18.70 ? 252 MET A CG  1 
ATOM   2155 S SD  . MET A 1 252 ? 4.189   7.688  66.763  1.00 16.52 ? 252 MET A SD  1 
ATOM   2156 C CE  . MET A 1 252 ? 3.414   6.147  67.292  1.00 17.81 ? 252 MET A CE  1 
ATOM   2157 N N   . TRP A 1 253 ? 1.880   12.087 64.572  1.00 12.06 ? 253 TRP A N   1 
ATOM   2158 C CA  . TRP A 1 253 ? 2.079   13.504 64.764  1.00 10.66 ? 253 TRP A CA  1 
ATOM   2159 C C   . TRP A 1 253 ? 3.048   13.702 65.916  1.00 8.82  ? 253 TRP A C   1 
ATOM   2160 O O   . TRP A 1 253 ? 2.738   13.301 67.053  1.00 11.30 ? 253 TRP A O   1 
ATOM   2161 C CB  . TRP A 1 253 ? 0.745   14.205 65.049  1.00 9.66  ? 253 TRP A CB  1 
ATOM   2162 C CG  . TRP A 1 253 ? 0.938   15.619 65.465  1.00 10.19 ? 253 TRP A CG  1 
ATOM   2163 C CD1 . TRP A 1 253 ? 0.661   16.165 66.706  1.00 9.01  ? 253 TRP A CD1 1 
ATOM   2164 C CD2 . TRP A 1 253 ? 1.472   16.691 64.665  1.00 10.19 ? 253 TRP A CD2 1 
ATOM   2165 N NE1 . TRP A 1 253 ? 1.008   17.498 66.710  1.00 11.68 ? 253 TRP A NE1 1 
ATOM   2166 C CE2 . TRP A 1 253 ? 1.507   17.843 65.481  1.00 10.23 ? 253 TRP A CE2 1 
ATOM   2167 C CE3 . TRP A 1 253 ? 1.942   16.781 63.348  1.00 15.56 ? 253 TRP A CE3 1 
ATOM   2168 C CZ2 . TRP A 1 253 ? 1.978   19.084 65.019  1.00 11.67 ? 253 TRP A CZ2 1 
ATOM   2169 C CZ3 . TRP A 1 253 ? 2.416   18.007 62.886  1.00 10.43 ? 253 TRP A CZ3 1 
ATOM   2170 C CH2 . TRP A 1 253 ? 2.430   19.148 63.723  1.00 10.13 ? 253 TRP A CH2 1 
ATOM   2171 N N   . PRO A 1 254 ? 4.224   14.284 65.695  1.00 10.68 ? 254 PRO A N   1 
ATOM   2172 C CA  . PRO A 1 254 ? 5.125   14.552 66.817  1.00 12.03 ? 254 PRO A CA  1 
ATOM   2173 C C   . PRO A 1 254 ? 4.557   15.667 67.674  1.00 9.02  ? 254 PRO A C   1 
ATOM   2174 O O   . PRO A 1 254 ? 4.154   16.714 67.149  1.00 11.61 ? 254 PRO A O   1 
ATOM   2175 C CB  . PRO A 1 254 ? 6.444   14.960 66.137  1.00 11.94 ? 254 PRO A CB  1 
ATOM   2176 C CG  . PRO A 1 254 ? 6.035   15.486 64.786  1.00 14.20 ? 254 PRO A CG  1 
ATOM   2177 C CD  . PRO A 1 254 ? 4.770   14.723 64.395  1.00 11.36 ? 254 PRO A CD  1 
ATOM   2178 N N   . PRO A 1 255 ? 4.441   15.462 68.986  1.00 8.17  ? 255 PRO A N   1 
ATOM   2179 C CA  . PRO A 1 255 ? 3.847   16.497 69.835  1.00 9.27  ? 255 PRO A CA  1 
ATOM   2180 C C   . PRO A 1 255 ? 4.569   17.817 69.656  1.00 9.68  ? 255 PRO A C   1 
ATOM   2181 O O   . PRO A 1 255 ? 5.799   17.867 69.614  1.00 10.22 ? 255 PRO A O   1 
ATOM   2182 C CB  . PRO A 1 255 ? 4.025   15.944 71.251  1.00 11.33 ? 255 PRO A CB  1 
ATOM   2183 C CG  . PRO A 1 255 ? 3.973   14.449 71.042  1.00 14.91 ? 255 PRO A CG  1 
ATOM   2184 C CD  . PRO A 1 255 ? 4.693   14.212 69.718  1.00 11.11 ? 255 PRO A CD  1 
ATOM   2185 N N   . GLU A 1 256 ? 3.782   18.881 69.516  1.00 10.37 ? 256 GLU A N   1 
ATOM   2186 C CA  . GLU A 1 256 ? 4.279   20.237 69.299  1.00 9.37  ? 256 GLU A CA  1 
ATOM   2187 C C   . GLU A 1 256 ? 5.091   20.342 68.021  1.00 9.63  ? 256 GLU A C   1 
ATOM   2188 O O   . GLU A 1 256 ? 5.977   21.202 67.912  1.00 11.22 ? 256 GLU A O   1 
ATOM   2189 C CB  . GLU A 1 256 ? 5.117   20.756 70.476  1.00 11.83 ? 256 GLU A CB  1 
ATOM   2190 C CG  . GLU A 1 256 ? 4.496   20.546 71.863  1.00 13.35 ? 256 GLU A CG  1 
ATOM   2191 C CD  . GLU A 1 256 ? 3.191   21.305 72.043  1.00 14.88 ? 256 GLU A CD  1 
ATOM   2192 O OE1 . GLU A 1 256 ? 2.965   22.314 71.338  1.00 15.10 ? 256 GLU A OE1 1 
ATOM   2193 O OE2 . GLU A 1 256 ? 2.396   20.897 72.913  1.00 15.98 ? 256 GLU A OE2 1 
ATOM   2194 N N   . ALA A 1 257 ? 4.807   19.468 67.050  1.00 8.90  ? 257 ALA A N   1 
ATOM   2195 C CA  . ALA A 1 257 ? 5.556   19.394 65.802  1.00 14.35 ? 257 ALA A CA  1 
ATOM   2196 C C   . ALA A 1 257 ? 7.041   19.130 66.054  1.00 11.35 ? 257 ALA A C   1 
ATOM   2197 O O   . ALA A 1 257 ? 7.871   19.374 65.178  1.00 15.18 ? 257 ALA A O   1 
ATOM   2198 C CB  . ALA A 1 257 ? 5.389   20.684 64.968  1.00 10.78 ? 257 ALA A CB  1 
ATOM   2199 N N   . SER A 1 258 ? 7.403   18.638 67.245  1.00 9.72  ? 258 SER A N   1 
ATOM   2200 C CA  . SER A 1 258 ? 8.791   18.694 67.689  1.00 10.60 ? 258 SER A CA  1 
ATOM   2201 C C   . SER A 1 258 ? 9.599   17.569 67.064  1.00 11.56 ? 258 SER A C   1 
ATOM   2202 O O   . SER A 1 258 ? 9.256   16.391 67.211  1.00 13.16 ? 258 SER A O   1 
ATOM   2203 C CB  . SER A 1 258 ? 8.895   18.622 69.211  1.00 12.64 ? 258 SER A CB  1 
ATOM   2204 O OG  . SER A 1 258 ? 10.233  18.927 69.583  1.00 14.95 ? 258 SER A OG  1 
ATOM   2205 N N   . VAL A 1 259 ? 10.672  17.931 66.362  1.00 11.61 ? 259 VAL A N   1 
ATOM   2206 C CA  . VAL A 1 259 ? 11.570  16.950 65.776  1.00 9.14  ? 259 VAL A CA  1 
ATOM   2207 C C   . VAL A 1 259 ? 13.002  17.373 66.068  1.00 13.38 ? 259 VAL A C   1 
ATOM   2208 O O   . VAL A 1 259 ? 13.282  18.491 66.508  1.00 13.45 ? 259 VAL A O   1 
ATOM   2209 C CB  . VAL A 1 259 ? 11.368  16.754 64.249  1.00 10.22 ? 259 VAL A CB  1 
ATOM   2210 C CG1 . VAL A 1 259 ? 9.930   16.297 63.921  1.00 11.71 ? 259 VAL A CG1 1 
ATOM   2211 C CG2 . VAL A 1 259 ? 11.703  18.017 63.503  1.00 13.25 ? 259 VAL A CG2 1 
ATOM   2212 N N   . SER A 1 260 ? 13.892  16.408 65.880  1.00 11.16 ? 260 SER A N   1 
ATOM   2213 C CA  . SER A 1 260 ? 15.340  16.527 65.951  1.00 12.30 ? 260 SER A CA  1 
ATOM   2214 C C   . SER A 1 260 ? 15.867  15.343 65.156  1.00 11.36 ? 260 SER A C   1 
ATOM   2215 O O   . SER A 1 260 ? 15.114  14.428 64.817  1.00 14.42 ? 260 SER A O   1 
ATOM   2216 C CB  . SER A 1 260 ? 15.845  16.484 67.392  1.00 14.04 ? 260 SER A CB  1 
ATOM   2217 O OG  . SER A 1 260 ? 15.579  15.203 67.967  1.00 12.57 ? 260 SER A OG  1 
ATOM   2218 N N   . ASN A 1 261 ? 17.176  15.346 64.877  1.00 10.95 ? 261 ASN A N   1 
ATOM   2219 C CA  . ASN A 1 261 ? 17.744  14.214 64.153  1.00 13.48 ? 261 ASN A CA  1 
ATOM   2220 C C   . ASN A 1 261 ? 17.548  12.927 64.936  1.00 13.84 ? 261 ASN A C   1 
ATOM   2221 O O   . ASN A 1 261 ? 17.195  11.888 64.363  1.00 14.52 ? 261 ASN A O   1 
ATOM   2222 C CB  . ASN A 1 261 ? 19.226  14.438 63.887  1.00 12.31 ? 261 ASN A CB  1 
ATOM   2223 C CG  . ASN A 1 261 ? 19.469  15.563 62.933  1.00 14.37 ? 261 ASN A CG  1 
ATOM   2224 O OD1 . ASN A 1 261 ? 18.618  15.866 62.089  1.00 15.32 ? 261 ASN A OD1 1 
ATOM   2225 N ND2 . ASN A 1 261 ? 20.628  16.202 63.056  1.00 19.53 ? 261 ASN A ND2 1 
ATOM   2226 N N   . GLU A 1 262 ? 17.733  12.993 66.257  1.00 11.39 ? 262 GLU A N   1 
ATOM   2227 C CA  . GLU A 1 262 ? 17.575  11.801 67.086  1.00 11.68 ? 262 GLU A CA  1 
ATOM   2228 C C   . GLU A 1 262 ? 16.122  11.353 67.129  1.00 14.25 ? 262 GLU A C   1 
ATOM   2229 O O   . GLU A 1 262 ? 15.836  10.151 67.063  1.00 13.95 ? 262 GLU A O   1 
ATOM   2230 C CB  . GLU A 1 262 ? 18.107  12.071 68.496  1.00 11.79 ? 262 GLU A CB  1 
ATOM   2231 C CG  . GLU A 1 262 ? 19.650  12.216 68.496  1.00 14.81 ? 262 GLU A CG  1 
ATOM   2232 C CD  . GLU A 1 262 ? 20.244  12.353 69.889  1.00 29.24 ? 262 GLU A CD  1 
ATOM   2233 O OE1 . GLU A 1 262 ? 19.733  11.720 70.830  1.00 27.80 ? 262 GLU A OE1 1 
ATOM   2234 O OE2 . GLU A 1 262 ? 21.239  13.090 70.037  1.00 33.94 ? 262 GLU A OE2 1 
ATOM   2235 N N   . ALA A 1 263 ? 15.188  12.305 67.215  1.00 11.58 ? 263 ALA A N   1 
ATOM   2236 C CA  . ALA A 1 263 ? 13.779  11.931 67.245  1.00 10.55 ? 263 ALA A CA  1 
ATOM   2237 C C   . ALA A 1 263 ? 13.350  11.297 65.932  1.00 11.95 ? 263 ALA A C   1 
ATOM   2238 O O   . ALA A 1 263 ? 12.610  10.310 65.937  1.00 12.68 ? 263 ALA A O   1 
ATOM   2239 C CB  . ALA A 1 263 ? 12.893  13.146 67.575  1.00 10.31 ? 263 ALA A CB  1 
ATOM   2240 N N   . LEU A 1 264 ? 13.797  11.847 64.800  1.00 14.84 ? 264 LEU A N   1 
ATOM   2241 C CA  . LEU A 1 264 ? 13.444  11.242 63.518  1.00 14.81 ? 264 LEU A CA  1 
ATOM   2242 C C   . LEU A 1 264 ? 14.001  9.830  63.407  1.00 13.59 ? 264 LEU A C   1 
ATOM   2243 O O   . LEU A 1 264 ? 13.335  8.930  62.878  1.00 14.32 ? 264 LEU A O   1 
ATOM   2244 C CB  . LEU A 1 264 ? 13.942  12.116 62.368  1.00 13.52 ? 264 LEU A CB  1 
ATOM   2245 C CG  . LEU A 1 264 ? 13.216  13.458 62.239  1.00 14.11 ? 264 LEU A CG  1 
ATOM   2246 C CD1 . LEU A 1 264 ? 13.919  14.341 61.250  1.00 16.74 ? 264 LEU A CD1 1 
ATOM   2247 C CD2 . LEU A 1 264 ? 11.764  13.260 61.810  1.00 14.78 ? 264 LEU A CD2 1 
ATOM   2248 N N   . GLU A 1 265 ? 15.218  9.608  63.913  1.00 13.15 ? 265 GLU A N   1 
ATOM   2249 C CA  . GLU A 1 265 ? 15.737  8.246  63.931  1.00 16.66 ? 265 GLU A CA  1 
ATOM   2250 C C   . GLU A 1 265 ? 14.851  7.330  64.770  1.00 16.92 ? 265 GLU A C   1 
ATOM   2251 O O   . GLU A 1 265 ? 14.538  6.213  64.353  1.00 13.96 ? 265 GLU A O   1 
ATOM   2252 C CB  . GLU A 1 265 ? 17.178  8.237  64.434  1.00 19.00 ? 265 GLU A CB  1 
ATOM   2253 C CG  . GLU A 1 265 ? 18.120  8.905  63.468  1.00 24.52 ? 265 GLU A CG  1 
ATOM   2254 C CD  . GLU A 1 265 ? 18.598  7.970  62.369  1.00 37.71 ? 265 GLU A CD  1 
ATOM   2255 O OE1 . GLU A 1 265 ? 18.261  6.754  62.412  1.00 27.36 ? 265 GLU A OE1 1 
ATOM   2256 O OE2 . GLU A 1 265 ? 19.320  8.457  61.466  1.00 34.49 ? 265 GLU A OE2 1 
ATOM   2257 N N   . LEU A 1 266 ? 14.406  7.792  65.941  1.00 13.04 ? 266 LEU A N   1 
ATOM   2258 C CA  . LEU A 1 266 ? 13.591  6.937  66.793  1.00 12.77 ? 266 LEU A CA  1 
ATOM   2259 C C   . LEU A 1 266 ? 12.267  6.583  66.120  1.00 14.22 ? 266 LEU A C   1 
ATOM   2260 O O   . LEU A 1 266 ? 11.846  5.424  66.138  1.00 13.65 ? 266 LEU A O   1 
ATOM   2261 C CB  . LEU A 1 266 ? 13.342  7.615  68.143  1.00 12.58 ? 266 LEU A CB  1 
ATOM   2262 C CG  . LEU A 1 266 ? 12.335  6.895  69.047  1.00 16.21 ? 266 LEU A CG  1 
ATOM   2263 C CD1 . LEU A 1 266 ? 12.836  5.519  69.442  1.00 17.56 ? 266 LEU A CD1 1 
ATOM   2264 C CD2 . LEU A 1 266 ? 12.000  7.735  70.294  1.00 15.66 ? 266 LEU A CD2 1 
ATOM   2265 N N   . TYR A 1 267 ? 11.603  7.563  65.505  1.00 13.99 ? 267 TYR A N   1 
ATOM   2266 C CA  . TYR A 1 267 ? 10.367  7.260  64.787  1.00 12.44 ? 267 TYR A CA  1 
ATOM   2267 C C   . TYR A 1 267 ? 10.619  6.262  63.664  1.00 13.70 ? 267 TYR A C   1 
ATOM   2268 O O   . TYR A 1 267 ? 9.818   5.349  63.448  1.00 14.18 ? 267 TYR A O   1 
ATOM   2269 C CB  . TYR A 1 267 ? 9.752   8.531  64.217  1.00 13.46 ? 267 TYR A CB  1 
ATOM   2270 C CG  . TYR A 1 267 ? 9.102   9.438  65.246  1.00 11.62 ? 267 TYR A CG  1 
ATOM   2271 C CD1 . TYR A 1 267 ? 7.955   9.034  65.934  1.00 13.16 ? 267 TYR A CD1 1 
ATOM   2272 C CD2 . TYR A 1 267 ? 9.607   10.713 65.494  1.00 12.96 ? 267 TYR A CD2 1 
ATOM   2273 C CE1 . TYR A 1 267 ? 7.347   9.870  66.870  1.00 12.55 ? 267 TYR A CE1 1 
ATOM   2274 C CE2 . TYR A 1 267 ? 9.014   11.552 66.427  1.00 12.29 ? 267 TYR A CE2 1 
ATOM   2275 C CZ  . TYR A 1 267 ? 7.869   11.136 67.102  1.00 13.44 ? 267 TYR A CZ  1 
ATOM   2276 O OH  . TYR A 1 267 ? 7.260   11.955 68.037  1.00 12.42 ? 267 TYR A OH  1 
ATOM   2277 N N   . TYR A 1 268 ? 11.720  6.434  62.927  1.00 12.72 ? 268 TYR A N   1 
ATOM   2278 C CA  . TYR A 1 268 ? 12.081  5.468  61.888  1.00 14.37 ? 268 TYR A CA  1 
ATOM   2279 C C   . TYR A 1 268 ? 12.288  4.085  62.481  1.00 15.52 ? 268 TYR A C   1 
ATOM   2280 O O   . TYR A 1 268 ? 11.760  3.092  61.968  1.00 13.94 ? 268 TYR A O   1 
ATOM   2281 C CB  . TYR A 1 268 ? 13.346  5.920  61.153  1.00 14.77 ? 268 TYR A CB  1 
ATOM   2282 C CG  . TYR A 1 268 ? 14.022  4.787  60.426  1.00 17.49 ? 268 TYR A CG  1 
ATOM   2283 C CD1 . TYR A 1 268 ? 13.428  4.211  59.313  1.00 20.44 ? 268 TYR A CD1 1 
ATOM   2284 C CD2 . TYR A 1 268 ? 15.237  4.268  60.869  1.00 18.43 ? 268 TYR A CD2 1 
ATOM   2285 C CE1 . TYR A 1 268 ? 14.034  3.159  58.641  1.00 23.38 ? 268 TYR A CE1 1 
ATOM   2286 C CE2 . TYR A 1 268 ? 15.850  3.209  60.205  1.00 24.23 ? 268 TYR A CE2 1 
ATOM   2287 C CZ  . TYR A 1 268 ? 15.237  2.661  59.094  1.00 28.23 ? 268 TYR A CZ  1 
ATOM   2288 O OH  . TYR A 1 268 ? 15.826  1.611  58.421  1.00 35.52 ? 268 TYR A OH  1 
ATOM   2289 N N   . GLU A 1 269 ? 13.044  4.001  63.581  1.00 16.54 ? 269 GLU A N   1 
ATOM   2290 C CA  . GLU A 1 269 ? 13.309  2.708  64.198  1.00 17.19 ? 269 GLU A CA  1 
ATOM   2291 C C   . GLU A 1 269 ? 12.035  2.031  64.689  1.00 13.62 ? 269 GLU A C   1 
ATOM   2292 O O   . GLU A 1 269 ? 11.969  0.794  64.706  1.00 20.52 ? 269 GLU A O   1 
ATOM   2293 C CB  . GLU A 1 269 ? 14.306  2.871  65.345  1.00 18.22 ? 269 GLU A CB  1 
ATOM   2294 C CG  . GLU A 1 269 ? 15.716  3.131  64.844  1.00 23.33 ? 269 GLU A CG  1 
ATOM   2295 C CD  . GLU A 1 269 ? 16.598  3.799  65.871  1.00 38.75 ? 269 GLU A CD  1 
ATOM   2296 O OE1 . GLU A 1 269 ? 16.156  3.954  67.031  1.00 38.13 ? 269 GLU A OE1 1 
ATOM   2297 O OE2 . GLU A 1 269 ? 17.737  4.172  65.510  1.00 41.06 ? 269 GLU A OE2 1 
ATOM   2298 N N   . LYS A 1 270 ? 11.013  2.803  65.077  1.00 13.79 ? 270 LYS A N   1 
ATOM   2299 C CA  . LYS A 1 270 ? 9.761   2.212  65.541  1.00 15.76 ? 270 LYS A CA  1 
ATOM   2300 C C   . LYS A 1 270 ? 8.763   1.996  64.406  1.00 17.51 ? 270 LYS A C   1 
ATOM   2301 O O   . LYS A 1 270 ? 7.588   1.699  64.668  1.00 18.57 ? 270 LYS A O   1 
ATOM   2302 C CB  . LYS A 1 270 ? 9.145   3.064  66.651  1.00 16.32 ? 270 LYS A CB  1 
ATOM   2303 C CG  . LYS A 1 270 ? 9.997   3.120  67.926  1.00 20.50 ? 270 LYS A CG  1 
ATOM   2304 C CD  . LYS A 1 270 ? 10.280  1.738  68.491  1.00 27.28 ? 270 LYS A CD  1 
ATOM   2305 C CE  . LYS A 1 270 ? 11.105  1.826  69.771  1.00 37.94 ? 270 LYS A CE  1 
ATOM   2306 N NZ  . LYS A 1 270 ? 12.280  0.904  69.768  1.00 47.94 ? 270 LYS A NZ  1 
ATOM   2307 N N   . GLY A 1 271 ? 9.210   2.099  63.155  1.00 15.97 ? 271 GLY A N   1 
ATOM   2308 C CA  . GLY A 1 271 ? 8.370   1.710  62.041  1.00 22.36 ? 271 GLY A CA  1 
ATOM   2309 C C   . GLY A 1 271 ? 7.409   2.767  61.551  1.00 20.98 ? 271 GLY A C   1 
ATOM   2310 O O   . GLY A 1 271 ? 6.459   2.435  60.833  1.00 18.22 ? 271 GLY A O   1 
ATOM   2311 N N   . ILE A 1 272 ? 7.621   4.028  61.918  1.00 14.72 ? 272 ILE A N   1 
ATOM   2312 C CA  . ILE A 1 272 ? 6.766   5.119  61.463  1.00 15.67 ? 272 ILE A CA  1 
ATOM   2313 C C   . ILE A 1 272 ? 7.238   5.541  60.079  1.00 14.53 ? 272 ILE A C   1 
ATOM   2314 O O   . ILE A 1 272 ? 8.436   5.773  59.866  1.00 19.24 ? 272 ILE A O   1 
ATOM   2315 C CB  . ILE A 1 272 ? 6.801   6.301  62.446  1.00 15.04 ? 272 ILE A CB  1 
ATOM   2316 C CG1 . ILE A 1 272 ? 6.436   5.858  63.877  1.00 15.56 ? 272 ILE A CG1 1 
ATOM   2317 C CG2 . ILE A 1 272 ? 5.900   7.425  61.952  1.00 12.88 ? 272 ILE A CG2 1 
ATOM   2318 C CD1 . ILE A 1 272 ? 5.143   5.054  63.997  1.00 20.96 ? 272 ILE A CD1 1 
ATOM   2319 N N   . ASN A 1 273 ? 6.303   5.615  59.131  1.00 11.98 ? 273 ASN A N   1 
ATOM   2320 C CA  . ASN A 1 273 ? 6.638   5.877  57.737  1.00 15.80 ? 273 ASN A CA  1 
ATOM   2321 C C   . ASN A 1 273 ? 6.568   7.354  57.375  1.00 16.92 ? 273 ASN A C   1 
ATOM   2322 O O   . ASN A 1 273 ? 7.260   7.787  56.442  1.00 15.22 ? 273 ASN A O   1 
ATOM   2323 C CB  . ASN A 1 273 ? 5.691   5.106  56.817  1.00 18.65 ? 273 ASN A CB  1 
ATOM   2324 C CG  . ASN A 1 273 ? 6.037   3.639  56.720  1.00 31.80 ? 273 ASN A CG  1 
ATOM   2325 O OD1 . ASN A 1 273 ? 7.107   3.211  57.147  1.00 40.23 ? 273 ASN A OD1 1 
ATOM   2326 N ND2 . ASN A 1 273 ? 5.132   2.858  56.149  1.00 38.60 ? 273 ASN A ND2 1 
ATOM   2327 N N   A MET A 1 274 ? 5.750   8.132  58.080  0.52 17.28 ? 274 MET A N   1 
ATOM   2328 N N   B MET A 1 274 ? 5.725   8.128  58.057  0.48 16.88 ? 274 MET A N   1 
ATOM   2329 C CA  A MET A 1 274 ? 5.583   9.540  57.751  0.52 14.66 ? 274 MET A CA  1 
ATOM   2330 C CA  B MET A 1 274 ? 5.577   9.544  57.749  0.48 14.78 ? 274 MET A CA  1 
ATOM   2331 C C   A MET A 1 274 ? 5.161   10.325 58.983  0.52 16.10 ? 274 MET A C   1 
ATOM   2332 C C   B MET A 1 274 ? 5.187   10.311 59.003  0.48 16.09 ? 274 MET A C   1 
ATOM   2333 O O   A MET A 1 274 ? 4.364   9.846  59.797  0.52 14.13 ? 274 MET A O   1 
ATOM   2334 O O   B MET A 1 274 ? 4.437   9.811  59.847  0.48 13.96 ? 274 MET A O   1 
ATOM   2335 C CB  A MET A 1 274 ? 4.542   9.730  56.645  0.52 15.96 ? 274 MET A CB  1 
ATOM   2336 C CB  B MET A 1 274 ? 4.519   9.781  56.663  0.48 15.64 ? 274 MET A CB  1 
ATOM   2337 C CG  A MET A 1 274 ? 4.447   11.160 56.145  0.52 15.29 ? 274 MET A CG  1 
ATOM   2338 C CG  B MET A 1 274 ? 4.428   11.235 56.197  0.48 15.32 ? 274 MET A CG  1 
ATOM   2339 S SD  A MET A 1 274 ? 3.222   11.331 54.841  0.52 19.35 ? 274 MET A SD  1 
ATOM   2340 S SD  B MET A 1 274 ? 3.276   12.242 57.164  0.48 14.85 ? 274 MET A SD  1 
ATOM   2341 C CE  A MET A 1 274 ? 1.683   11.149 55.738  0.52 12.79 ? 274 MET A CE  1 
ATOM   2342 C CE  B MET A 1 274 ? 1.703   11.642 56.551  0.48 20.03 ? 274 MET A CE  1 
ATOM   2343 N N   . LEU A 1 275 ? 5.697   11.535 59.113  1.00 11.80 ? 275 LEU A N   1 
ATOM   2344 C CA  . LEU A 1 275 ? 5.226   12.474 60.105  1.00 9.39  ? 275 LEU A CA  1 
ATOM   2345 C C   . LEU A 1 275 ? 5.193   13.838 59.443  1.00 13.88 ? 275 LEU A C   1 
ATOM   2346 O O   . LEU A 1 275 ? 5.582   13.993 58.286  1.00 13.07 ? 275 LEU A O   1 
ATOM   2347 C CB  . LEU A 1 275 ? 6.090   12.461 61.365  1.00 15.63 ? 275 LEU A CB  1 
ATOM   2348 C CG  . LEU A 1 275 ? 7.602   12.614 61.241  1.00 23.66 ? 275 LEU A CG  1 
ATOM   2349 C CD1 . LEU A 1 275 ? 8.008   14.076 61.094  1.00 28.40 ? 275 LEU A CD1 1 
ATOM   2350 C CD2 . LEU A 1 275 ? 8.289   12.005 62.457  1.00 21.73 ? 275 LEU A CD2 1 
ATOM   2351 N N   . ALA A 1 276 ? 4.697   14.820 60.174  1.00 15.73 ? 276 ALA A N   1 
ATOM   2352 C CA  . ALA A 1 276 ? 4.756   16.196 59.725  1.00 10.34 ? 276 ALA A CA  1 
ATOM   2353 C C   . ALA A 1 276 ? 5.352   17.026 60.838  1.00 11.49 ? 276 ALA A C   1 
ATOM   2354 O O   . ALA A 1 276 ? 5.338   16.633 62.006  1.00 12.56 ? 276 ALA A O   1 
ATOM   2355 C CB  . ALA A 1 276 ? 3.375   16.760 59.340  1.00 11.24 ? 276 ALA A CB  1 
ATOM   2356 N N   . THR A 1 277 ? 5.873   18.183 60.463  1.00 11.33 ? 277 THR A N   1 
ATOM   2357 C CA  . THR A 1 277 ? 6.393   19.123 61.444  1.00 10.06 ? 277 THR A CA  1 
ATOM   2358 C C   . THR A 1 277 ? 6.120   20.525 60.905  1.00 11.85 ? 277 THR A C   1 
ATOM   2359 O O   . THR A 1 277 ? 5.284   20.696 60.012  1.00 15.39 ? 277 THR A O   1 
ATOM   2360 C CB  . THR A 1 277 ? 7.879   18.815 61.722  1.00 10.41 ? 277 THR A CB  1 
ATOM   2361 O OG1 . THR A 1 277 ? 8.382   19.744 62.687  1.00 13.43 ? 277 THR A OG1 1 
ATOM   2362 C CG2 . THR A 1 277 ? 8.703   18.920 60.453  1.00 14.57 ? 277 THR A CG2 1 
ATOM   2363 N N   . ASP A 1 278 ? 6.826   21.529 61.424  1.00 13.14 ? 278 ASP A N   1 
ATOM   2364 C CA  . ASP A 1 278 ? 6.479   22.922 61.160  1.00 11.89 ? 278 ASP A CA  1 
ATOM   2365 C C   . ASP A 1 278 ? 7.401   23.566 60.130  1.00 15.04 ? 278 ASP A C   1 
ATOM   2366 O O   . ASP A 1 278 ? 8.578   23.216 60.009  1.00 14.60 ? 278 ASP A O   1 
ATOM   2367 C CB  . ASP A 1 278 ? 6.526   23.742 62.454  1.00 11.74 ? 278 ASP A CB  1 
ATOM   2368 C CG  . ASP A 1 278 ? 6.044   25.160 62.258  1.00 16.15 ? 278 ASP A CG  1 
ATOM   2369 O OD1 . ASP A 1 278 ? 4.930   25.336 61.727  1.00 15.93 ? 278 ASP A OD1 1 
ATOM   2370 O OD2 . ASP A 1 278 ? 6.776   26.086 62.642  1.00 21.35 ? 278 ASP A OD2 1 
ATOM   2371 N N   . GLU A 1 279 ? 6.846   24.545 59.409  1.00 15.35 ? 279 GLU A N   1 
ATOM   2372 C CA  . GLU A 1 279 ? 7.601   25.292 58.406  1.00 15.89 ? 279 GLU A CA  1 
ATOM   2373 C C   . GLU A 1 279 ? 8.812   26.019 59.000  1.00 15.99 ? 279 GLU A C   1 
ATOM   2374 O O   . GLU A 1 279 ? 9.828   26.193 58.313  1.00 16.02 ? 279 GLU A O   1 
ATOM   2375 C CB  . GLU A 1 279 ? 6.661   26.290 57.711  1.00 13.28 ? 279 GLU A CB  1 
ATOM   2376 C CG  . GLU A 1 279 ? 7.200   26.792 56.407  1.00 18.66 ? 279 GLU A CG  1 
ATOM   2377 C CD  . GLU A 1 279 ? 6.249   27.711 55.661  1.00 25.23 ? 279 GLU A CD  1 
ATOM   2378 O OE1 . GLU A 1 279 ? 5.062   27.834 56.052  1.00 19.03 ? 279 GLU A OE1 1 
ATOM   2379 O OE2 . GLU A 1 279 ? 6.707   28.321 54.674  1.00 26.35 ? 279 GLU A OE2 1 
ATOM   2380 N N   . VAL A 1 280 ? 8.728   26.465 60.257  1.00 14.06 ? 280 VAL A N   1 
ATOM   2381 C CA  . VAL A 1 280 ? 9.858   27.182 60.835  1.00 16.27 ? 280 VAL A CA  1 
ATOM   2382 C C   . VAL A 1 280 ? 11.046  26.246 60.974  1.00 13.81 ? 280 VAL A C   1 
ATOM   2383 O O   . VAL A 1 280 ? 12.206  26.664 60.814  1.00 15.43 ? 280 VAL A O   1 
ATOM   2384 C CB  . VAL A 1 280 ? 9.477   27.805 62.189  1.00 19.12 ? 280 VAL A CB  1 
ATOM   2385 C CG1 . VAL A 1 280 ? 10.716  28.351 62.878  1.00 16.98 ? 280 VAL A CG1 1 
ATOM   2386 C CG2 . VAL A 1 280 ? 8.438   28.918 61.999  1.00 20.90 ? 280 VAL A CG2 1 
ATOM   2387 N N   . ILE A 1 281 ? 10.782  24.972 61.265  1.00 16.47 ? 281 ILE A N   1 
ATOM   2388 C CA  . ILE A 1 281 ? 11.865  24.005 61.378  1.00 15.09 ? 281 ILE A CA  1 
ATOM   2389 C C   . ILE A 1 281 ? 12.518  23.787 60.015  1.00 14.15 ? 281 ILE A C   1 
ATOM   2390 O O   . ILE A 1 281 ? 13.750  23.727 59.912  1.00 16.23 ? 281 ILE A O   1 
ATOM   2391 C CB  . ILE A 1 281 ? 11.346  22.701 62.018  1.00 13.60 ? 281 ILE A CB  1 
ATOM   2392 C CG1 . ILE A 1 281 ? 11.026  22.983 63.498  1.00 17.53 ? 281 ILE A CG1 1 
ATOM   2393 C CG2 . ILE A 1 281 ? 12.396  21.589 61.889  1.00 18.22 ? 281 ILE A CG2 1 
ATOM   2394 C CD1 . ILE A 1 281 ? 10.318  21.860 64.223  1.00 22.79 ? 281 ILE A CD1 1 
ATOM   2395 N N   . LEU A 1 282 ? 11.712  23.718 58.947  1.00 11.63 ? 282 LEU A N   1 
ATOM   2396 C CA  . LEU A 1 282 ? 12.260  23.677 57.594  1.00 13.81 ? 282 LEU A CA  1 
ATOM   2397 C C   . LEU A 1 282 ? 13.164  24.875 57.343  1.00 14.59 ? 282 LEU A C   1 
ATOM   2398 O O   . LEU A 1 282 ? 14.307  24.726 56.903  1.00 14.68 ? 282 LEU A O   1 
ATOM   2399 C CB  . LEU A 1 282 ? 11.137  23.653 56.553  1.00 15.40 ? 282 LEU A CB  1 
ATOM   2400 C CG  . LEU A 1 282 ? 11.582  23.532 55.091  1.00 14.12 ? 282 LEU A CG  1 
ATOM   2401 C CD1 . LEU A 1 282 ? 12.366  22.258 54.865  1.00 16.76 ? 282 LEU A CD1 1 
ATOM   2402 C CD2 . LEU A 1 282 ? 10.364  23.564 54.167  1.00 17.05 ? 282 LEU A CD2 1 
ATOM   2403 N N   . LYS A 1 283 ? 12.658  26.081 57.596  1.00 13.12 ? 283 LYS A N   1 
ATOM   2404 C CA  . LYS A 1 283 ? 13.471  27.267 57.322  1.00 14.66 ? 283 LYS A CA  1 
ATOM   2405 C C   . LYS A 1 283 ? 14.760  27.281 58.139  1.00 16.15 ? 283 LYS A C   1 
ATOM   2406 O O   . LYS A 1 283 ? 15.785  27.803 57.676  1.00 18.10 ? 283 LYS A O   1 
ATOM   2407 C CB  . LYS A 1 283 ? 12.646  28.525 57.587  1.00 22.73 ? 283 LYS A CB  1 
ATOM   2408 C CG  . LYS A 1 283 ? 11.552  28.726 56.540  1.00 37.66 ? 283 LYS A CG  1 
ATOM   2409 C CD  . LYS A 1 283 ? 10.842  30.063 56.658  1.00 47.63 ? 283 LYS A CD  1 
ATOM   2410 C CE  . LYS A 1 283 ? 9.333   29.884 56.538  1.00 55.21 ? 283 LYS A CE  1 
ATOM   2411 N NZ  . LYS A 1 283 ? 8.597   30.425 57.717  1.00 57.97 ? 283 LYS A NZ  1 
ATOM   2412 N N   . ASN A 1 284 ? 14.725  26.741 59.361  1.00 16.00 ? 284 ASN A N   1 
ATOM   2413 C CA  . ASN A 1 284 ? 15.912  26.681 60.210  1.00 17.24 ? 284 ASN A CA  1 
ATOM   2414 C C   . ASN A 1 284 ? 16.908  25.615 59.780  1.00 16.08 ? 284 ASN A C   1 
ATOM   2415 O O   . ASN A 1 284 ? 18.088  25.709 60.144  1.00 16.70 ? 284 ASN A O   1 
ATOM   2416 C CB  . ASN A 1 284 ? 15.522  26.393 61.666  1.00 12.96 ? 284 ASN A CB  1 
ATOM   2417 C CG  . ASN A 1 284 ? 14.918  27.592 62.365  1.00 22.90 ? 284 ASN A CG  1 
ATOM   2418 O OD1 . ASN A 1 284 ? 14.972  28.717 61.868  1.00 23.33 ? 284 ASN A OD1 1 
ATOM   2419 N ND2 . ASN A 1 284 ? 14.366  27.360 63.551  1.00 17.16 ? 284 ASN A ND2 1 
ATOM   2420 N N   . SER A 1 285 ? 16.472  24.620 59.008  1.00 15.59 ? 285 SER A N   1 
ATOM   2421 C CA  . SER A 1 285 ? 17.283  23.446 58.687  1.00 15.67 ? 285 SER A CA  1 
ATOM   2422 C C   . SER A 1 285 ? 17.873  23.457 57.286  1.00 19.22 ? 285 SER A C   1 
ATOM   2423 O O   . SER A 1 285 ? 18.898  22.802 57.053  1.00 21.93 ? 285 SER A O   1 
ATOM   2424 C CB  . SER A 1 285 ? 16.440  22.172 58.824  1.00 19.25 ? 285 SER A CB  1 
ATOM   2425 O OG  . SER A 1 285 ? 15.853  22.104 60.106  1.00 19.20 ? 285 SER A OG  1 
ATOM   2426 N N   . VAL A 1 286 ? 17.233  24.136 56.341  1.00 15.14 ? 286 VAL A N   1 
ATOM   2427 C CA  . VAL A 1 286 ? 17.629  24.111 54.937  1.00 15.32 ? 286 VAL A CA  1 
ATOM   2428 C C   . VAL A 1 286 ? 17.635  25.550 54.450  1.00 18.75 ? 286 VAL A C   1 
ATOM   2429 O O   . VAL A 1 286 ? 16.685  26.298 54.717  1.00 22.47 ? 286 VAL A O   1 
ATOM   2430 C CB  . VAL A 1 286 ? 16.670  23.264 54.073  1.00 21.11 ? 286 VAL A CB  1 
ATOM   2431 C CG1 . VAL A 1 286 ? 17.201  23.126 52.656  1.00 26.54 ? 286 VAL A CG1 1 
ATOM   2432 C CG2 . VAL A 1 286 ? 16.424  21.887 54.693  1.00 22.04 ? 286 VAL A CG2 1 
ATOM   2433 N N   . GLU A 1 287 ? 18.705  25.938 53.747  1.00 23.83 ? 287 GLU A N   1 
ATOM   2434 C CA  . GLU A 1 287 ? 18.825  27.317 53.282  1.00 28.09 ? 287 GLU A CA  1 
ATOM   2435 C C   . GLU A 1 287 ? 17.634  27.713 52.422  1.00 29.42 ? 287 GLU A C   1 
ATOM   2436 O O   . GLU A 1 287 ? 16.982  28.733 52.673  1.00 29.32 ? 287 GLU A O   1 
ATOM   2437 C CB  . GLU A 1 287 ? 20.135  27.501 52.518  1.00 28.96 ? 287 GLU A CB  1 
ATOM   2438 C CG  . GLU A 1 287 ? 21.329  27.556 53.440  1.00 31.53 ? 287 GLU A CG  1 
ATOM   2439 C CD  . GLU A 1 287 ? 22.644  27.725 52.713  1.00 32.60 ? 287 GLU A CD  1 
ATOM   2440 O OE1 . GLU A 1 287 ? 22.696  27.505 51.483  1.00 34.32 ? 287 GLU A OE1 1 
ATOM   2441 O OE2 . GLU A 1 287 ? 23.633  28.075 53.389  1.00 28.89 ? 287 GLU A OE2 1 
ATOM   2442 N N   . ARG A 1 288 ? 17.322  26.910 51.409  1.00 24.59 ? 288 ARG A N   1 
ATOM   2443 C CA  . ARG A 1 288 ? 16.236  27.210 50.489  1.00 15.32 ? 288 ARG A CA  1 
ATOM   2444 C C   . ARG A 1 288 ? 15.394  25.958 50.325  1.00 20.72 ? 288 ARG A C   1 
ATOM   2445 O O   . ARG A 1 288 ? 15.872  24.958 49.781  1.00 28.79 ? 288 ARG A O   1 
ATOM   2446 C CB  . ARG A 1 288 ? 16.772  27.677 49.132  1.00 21.89 ? 288 ARG A CB  1 
ATOM   2447 C CG  . ARG A 1 288 ? 15.690  28.169 48.195  1.00 20.52 ? 288 ARG A CG  1 
ATOM   2448 C CD  . ARG A 1 288 ? 16.182  28.147 46.766  1.00 23.38 ? 288 ARG A CD  1 
ATOM   2449 N NE  . ARG A 1 288 ? 16.373  26.777 46.301  1.00 26.72 ? 288 ARG A NE  1 
ATOM   2450 C CZ  . ARG A 1 288 ? 17.386  26.377 45.543  1.00 30.91 ? 288 ARG A CZ  1 
ATOM   2451 N NH1 . ARG A 1 288 ? 18.316  27.244 45.153  1.00 28.38 ? 288 ARG A NH1 1 
ATOM   2452 N NH2 . ARG A 1 288 ? 17.470  25.109 45.165  1.00 30.69 ? 288 ARG A NH2 1 
ATOM   2453 N N   . ALA A 1 289 ? 14.145  26.014 50.781  1.00 17.79 ? 289 ALA A N   1 
ATOM   2454 C CA  . ALA A 1 289 ? 13.297  24.837 50.699  1.00 20.34 ? 289 ALA A CA  1 
ATOM   2455 C C   . ALA A 1 289 ? 11.839  25.259 50.669  1.00 20.08 ? 289 ALA A C   1 
ATOM   2456 O O   . ALA A 1 289 ? 11.413  26.124 51.439  1.00 20.35 ? 289 ALA A O   1 
ATOM   2457 C CB  . ALA A 1 289 ? 13.538  23.886 51.879  1.00 24.47 ? 289 ALA A CB  1 
ATOM   2458 N N   . SER A 1 290 ? 11.077  24.613 49.804  1.00 16.89 ? 290 SER A N   1 
ATOM   2459 C CA  . SER A 1 290 ? 9.649   24.868 49.732  1.00 17.63 ? 290 SER A CA  1 
ATOM   2460 C C   . SER A 1 290 ? 8.880   23.858 50.584  1.00 15.46 ? 290 SER A C   1 
ATOM   2461 O O   . SER A 1 290 ? 9.211   22.669 50.574  1.00 16.60 ? 290 SER A O   1 
ATOM   2462 C CB  . SER A 1 290 ? 9.185   24.777 48.287  1.00 19.67 ? 290 SER A CB  1 
ATOM   2463 O OG  . SER A 1 290 ? 7.784   24.671 48.216  1.00 19.26 ? 290 SER A OG  1 
ATOM   2464 N N   . PRO A 1 291 ? 7.841   24.290 51.303  1.00 16.25 ? 291 PRO A N   1 
ATOM   2465 C CA  . PRO A 1 291 ? 7.022   23.354 52.080  1.00 15.71 ? 291 PRO A CA  1 
ATOM   2466 C C   . PRO A 1 291 ? 6.028   22.548 51.256  1.00 15.05 ? 291 PRO A C   1 
ATOM   2467 O O   . PRO A 1 291 ? 5.238   21.800 51.835  1.00 15.25 ? 291 PRO A O   1 
ATOM   2468 C CB  . PRO A 1 291 ? 6.284   24.288 53.055  1.00 21.38 ? 291 PRO A CB  1 
ATOM   2469 C CG  . PRO A 1 291 ? 6.078   25.547 52.244  1.00 23.03 ? 291 PRO A CG  1 
ATOM   2470 C CD  . PRO A 1 291 ? 7.299   25.663 51.352  1.00 19.64 ? 291 PRO A CD  1 
ATOM   2471 N N   . TYR A 1 292 ? 6.038   22.654 49.927  1.00 14.22 ? 292 TYR A N   1 
ATOM   2472 C CA  . TYR A 1 292 ? 5.043   21.966 49.107  1.00 13.59 ? 292 TYR A CA  1 
ATOM   2473 C C   . TYR A 1 292 ? 5.570   20.659 48.525  1.00 16.60 ? 292 TYR A C   1 
ATOM   2474 O O   . TYR A 1 292 ? 4.922   20.059 47.659  1.00 15.01 ? 292 TYR A O   1 
ATOM   2475 C CB  . TYR A 1 292 ? 4.551   22.908 48.000  1.00 16.29 ? 292 TYR A CB  1 
ATOM   2476 C CG  . TYR A 1 292 ? 4.031   24.202 48.588  1.00 18.73 ? 292 TYR A CG  1 
ATOM   2477 C CD1 . TYR A 1 292 ? 3.194   24.179 49.694  1.00 15.77 ? 292 TYR A CD1 1 
ATOM   2478 C CD2 . TYR A 1 292 ? 4.396   25.437 48.068  1.00 23.62 ? 292 TYR A CD2 1 
ATOM   2479 C CE1 . TYR A 1 292 ? 2.720   25.344 50.262  1.00 21.18 ? 292 TYR A CE1 1 
ATOM   2480 C CE2 . TYR A 1 292 ? 3.911   26.615 48.626  1.00 23.53 ? 292 TYR A CE2 1 
ATOM   2481 C CZ  . TYR A 1 292 ? 3.086   26.556 49.731  1.00 23.89 ? 292 TYR A CZ  1 
ATOM   2482 O OH  . TYR A 1 292 ? 2.603   27.709 50.319  1.00 26.97 ? 292 TYR A OH  1 
ATOM   2483 N N   . LEU A 1 293 ? 6.728   20.208 48.983  1.00 14.96 ? 293 LEU A N   1 
ATOM   2484 C CA  . LEU A 1 293 ? 7.334   18.955 48.567  1.00 14.71 ? 293 LEU A CA  1 
ATOM   2485 C C   . LEU A 1 293 ? 7.149   17.891 49.645  1.00 15.26 ? 293 LEU A C   1 
ATOM   2486 O O   . LEU A 1 293 ? 6.974   18.193 50.829  1.00 13.01 ? 293 LEU A O   1 
ATOM   2487 C CB  . LEU A 1 293 ? 8.833   19.152 48.300  1.00 14.26 ? 293 LEU A CB  1 
ATOM   2488 C CG  . LEU A 1 293 ? 9.324   19.799 46.996  1.00 20.01 ? 293 LEU A CG  1 
ATOM   2489 C CD1 . LEU A 1 293 ? 8.813   21.222 46.843  1.00 23.58 ? 293 LEU A CD1 1 
ATOM   2490 C CD2 . LEU A 1 293 ? 10.843  19.791 46.947  1.00 26.30 ? 293 LEU A CD2 1 
ATOM   2491 N N   . ARG A 1 294 ? 7.248   16.624 49.229  1.00 14.19 ? 294 ARG A N   1 
ATOM   2492 C CA  . ARG A 1 294 ? 7.417   15.531 50.184  1.00 14.04 ? 294 ARG A CA  1 
ATOM   2493 C C   . ARG A 1 294 ? 8.907   15.372 50.464  1.00 15.75 ? 294 ARG A C   1 
ATOM   2494 O O   . ARG A 1 294 ? 9.695   15.198 49.536  1.00 15.32 ? 294 ARG A O   1 
ATOM   2495 C CB  . ARG A 1 294 ? 6.822   14.223 49.655  1.00 14.68 ? 294 ARG A CB  1 
ATOM   2496 C CG  . ARG A 1 294 ? 6.940   13.045 50.651  1.00 14.81 ? 294 ARG A CG  1 
ATOM   2497 C CD  . ARG A 1 294 ? 6.065   11.843 50.242  1.00 15.27 ? 294 ARG A CD  1 
ATOM   2498 N NE  . ARG A 1 294 ? 6.430   11.349 48.929  1.00 22.95 ? 294 ARG A NE  1 
ATOM   2499 C CZ  . ARG A 1 294 ? 5.591   11.170 47.915  1.00 20.15 ? 294 ARG A CZ  1 
ATOM   2500 N NH1 . ARG A 1 294 ? 4.292   11.419 48.045  1.00 18.30 ? 294 ARG A NH1 1 
ATOM   2501 N NH2 . ARG A 1 294 ? 6.063   10.718 46.758  1.00 21.12 ? 294 ARG A NH2 1 
ATOM   2502 N N   . TYR A 1 295 ? 9.300   15.452 51.733  1.00 13.49 ? 295 TYR A N   1 
ATOM   2503 C CA  . TYR A 1 295 ? 10.709  15.321 52.082  1.00 15.94 ? 295 TYR A CA  1 
ATOM   2504 C C   . TYR A 1 295 ? 11.004  13.918 52.591  1.00 16.49 ? 295 TYR A C   1 
ATOM   2505 O O   . TYR A 1 295 ? 10.151  13.263 53.188  1.00 15.93 ? 295 TYR A O   1 
ATOM   2506 C CB  . TYR A 1 295 ? 11.112  16.356 53.137  1.00 15.44 ? 295 TYR A CB  1 
ATOM   2507 C CG  . TYR A 1 295 ? 11.211  17.732 52.545  1.00 13.94 ? 295 TYR A CG  1 
ATOM   2508 C CD1 . TYR A 1 295 ? 10.069  18.499 52.329  1.00 13.39 ? 295 TYR A CD1 1 
ATOM   2509 C CD2 . TYR A 1 295 ? 12.445  18.261 52.173  1.00 16.99 ? 295 TYR A CD2 1 
ATOM   2510 C CE1 . TYR A 1 295 ? 10.156  19.761 51.755  1.00 15.97 ? 295 TYR A CE1 1 
ATOM   2511 C CE2 . TYR A 1 295 ? 12.541  19.523 51.605  1.00 18.43 ? 295 TYR A CE2 1 
ATOM   2512 C CZ  . TYR A 1 295 ? 11.398  20.269 51.409  1.00 20.04 ? 295 TYR A CZ  1 
ATOM   2513 O OH  . TYR A 1 295 ? 11.486  21.522 50.841  1.00 20.52 ? 295 TYR A OH  1 
ATOM   2514 N N   . TYR A 1 296 ? 12.223  13.451 52.325  1.00 13.69 ? 296 TYR A N   1 
ATOM   2515 C CA  . TYR A 1 296 ? 12.704  12.176 52.849  1.00 13.84 ? 296 TYR A CA  1 
ATOM   2516 C C   . TYR A 1 296 ? 13.887  12.486 53.749  1.00 16.95 ? 296 TYR A C   1 
ATOM   2517 O O   . TYR A 1 296 ? 14.920  12.965 53.273  1.00 17.38 ? 296 TYR A O   1 
ATOM   2518 C CB  . TYR A 1 296 ? 13.110  11.220 51.729  1.00 14.84 ? 296 TYR A CB  1 
ATOM   2519 C CG  . TYR A 1 296 ? 12.012  10.933 50.736  1.00 16.97 ? 296 TYR A CG  1 
ATOM   2520 C CD1 . TYR A 1 296 ? 10.780  10.435 51.150  1.00 17.65 ? 296 TYR A CD1 1 
ATOM   2521 C CD2 . TYR A 1 296 ? 12.205  11.166 49.375  1.00 23.96 ? 296 TYR A CD2 1 
ATOM   2522 C CE1 . TYR A 1 296 ? 9.768   10.169 50.230  1.00 18.56 ? 296 TYR A CE1 1 
ATOM   2523 C CE2 . TYR A 1 296 ? 11.197  10.908 48.452  1.00 20.80 ? 296 TYR A CE2 1 
ATOM   2524 C CZ  . TYR A 1 296 ? 9.984   10.408 48.884  1.00 23.24 ? 296 TYR A CZ  1 
ATOM   2525 O OH  . TYR A 1 296 ? 8.998   10.148 47.954  1.00 20.60 ? 296 TYR A OH  1 
ATOM   2526 N N   . PHE A 1 297 ? 13.733  12.235 55.044  1.00 16.62 ? 297 PHE A N   1 
ATOM   2527 C CA  . PHE A 1 297 ? 14.832  12.451 55.979  1.00 12.86 ? 297 PHE A CA  1 
ATOM   2528 C C   . PHE A 1 297 ? 15.762  11.243 55.901  1.00 14.55 ? 297 PHE A C   1 
ATOM   2529 O O   . PHE A 1 297 ? 15.392  10.144 56.333  1.00 17.51 ? 297 PHE A O   1 
ATOM   2530 C CB  . PHE A 1 297 ? 14.301  12.655 57.397  1.00 14.62 ? 297 PHE A CB  1 
ATOM   2531 C CG  . PHE A 1 297 ? 15.388  12.801 58.426  1.00 12.60 ? 297 PHE A CG  1 
ATOM   2532 C CD1 . PHE A 1 297 ? 16.070  14.003 58.570  1.00 14.18 ? 297 PHE A CD1 1 
ATOM   2533 C CD2 . PHE A 1 297 ? 15.738  11.740 59.233  1.00 16.43 ? 297 PHE A CD2 1 
ATOM   2534 C CE1 . PHE A 1 297 ? 17.084  14.136 59.521  1.00 13.81 ? 297 PHE A CE1 1 
ATOM   2535 C CE2 . PHE A 1 297 ? 16.743  11.868 60.178  1.00 17.34 ? 297 PHE A CE2 1 
ATOM   2536 C CZ  . PHE A 1 297 ? 17.417  13.068 60.314  1.00 13.02 ? 297 PHE A CZ  1 
ATOM   2537 N N   . ARG A 1 298 ? 16.960  11.445 55.334  1.00 14.14 ? 298 ARG A N   1 
ATOM   2538 C CA  . ARG A 1 298 ? 17.993  10.416 55.191  1.00 16.69 ? 298 ARG A CA  1 
ATOM   2539 C C   . ARG A 1 298 ? 17.486  9.163  54.479  1.00 19.33 ? 298 ARG A C   1 
ATOM   2540 O O   . ARG A 1 298 ? 18.049  8.075  54.655  1.00 18.43 ? 298 ARG A O   1 
ATOM   2541 C CB  . ARG A 1 298 ? 18.590  10.044 56.556  1.00 17.63 ? 298 ARG A CB  1 
ATOM   2542 C CG  . ARG A 1 298 ? 19.240  11.229 57.231  1.00 15.29 ? 298 ARG A CG  1 
ATOM   2543 C CD  . ARG A 1 298 ? 19.921  10.875 58.557  1.00 22.30 ? 298 ARG A CD  1 
ATOM   2544 N NE  . ARG A 1 298 ? 20.431  12.091 59.191  1.00 20.93 ? 298 ARG A NE  1 
ATOM   2545 C CZ  . ARG A 1 298 ? 20.819  12.183 60.462  1.00 22.47 ? 298 ARG A CZ  1 
ATOM   2546 N NH1 . ARG A 1 298 ? 20.771  11.121 61.256  1.00 22.87 ? 298 ARG A NH1 1 
ATOM   2547 N NH2 . ARG A 1 298 ? 21.261  13.341 60.936  1.00 24.79 ? 298 ARG A NH2 1 
ATOM   2548 N N   . GLU A 1 299 ? 16.439  9.301  53.662  1.00 18.86 ? 299 GLU A N   1 
ATOM   2549 C CA  . GLU A 1 299 ? 15.781  8.175  53.000  1.00 17.41 ? 299 GLU A CA  1 
ATOM   2550 C C   . GLU A 1 299 ? 15.231  7.161  54.000  1.00 21.33 ? 299 GLU A C   1 
ATOM   2551 O O   . GLU A 1 299 ? 15.008  5.994  53.656  1.00 22.96 ? 299 GLU A O   1 
ATOM   2552 C CB  . GLU A 1 299 ? 16.716  7.477  51.995  1.00 19.08 ? 299 GLU A CB  1 
ATOM   2553 C CG  . GLU A 1 299 ? 17.329  8.406  50.948  1.00 26.12 ? 299 GLU A CG  1 
ATOM   2554 C CD  . GLU A 1 299 ? 16.377  8.740  49.817  1.00 32.27 ? 299 GLU A CD  1 
ATOM   2555 O OE1 . GLU A 1 299 ? 16.865  8.997  48.691  1.00 34.01 ? 299 GLU A OE1 1 
ATOM   2556 O OE2 . GLU A 1 299 ? 15.151  8.754  50.040  1.00 25.89 ? 299 GLU A OE2 1 
ATOM   2557 N N   . LEU A 1 300 ? 14.995  7.585  55.239  1.00 14.83 ? 300 LEU A N   1 
ATOM   2558 C CA  . LEU A 1 300 ? 14.485  6.704  56.279  1.00 17.61 ? 300 LEU A CA  1 
ATOM   2559 C C   . LEU A 1 300 ? 13.002  6.893  56.541  1.00 17.83 ? 300 LEU A C   1 
ATOM   2560 O O   . LEU A 1 300 ? 12.282  5.915  56.746  1.00 19.12 ? 300 LEU A O   1 
ATOM   2561 C CB  . LEU A 1 300 ? 15.230  6.942  57.587  1.00 14.13 ? 300 LEU A CB  1 
ATOM   2562 C CG  . LEU A 1 300 ? 16.746  6.771  57.527  1.00 21.70 ? 300 LEU A CG  1 
ATOM   2563 C CD1 . LEU A 1 300 ? 17.320  7.039  58.904  1.00 20.54 ? 300 LEU A CD1 1 
ATOM   2564 C CD2 . LEU A 1 300 ? 17.098  5.377  57.051  1.00 27.95 ? 300 LEU A CD2 1 
ATOM   2565 N N   . ILE A 1 301 ? 12.535  8.133  56.546  1.00 14.60 ? 301 ILE A N   1 
ATOM   2566 C CA  . ILE A 1 301 ? 11.167  8.453  56.938  1.00 12.79 ? 301 ILE A CA  1 
ATOM   2567 C C   . ILE A 1 301 ? 10.723  9.675  56.140  1.00 14.57 ? 301 ILE A C   1 
ATOM   2568 O O   . ILE A 1 301 ? 11.523  10.574 55.861  1.00 14.63 ? 301 ILE A O   1 
ATOM   2569 C CB  . ILE A 1 301 ? 11.081  8.682  58.467  1.00 14.44 ? 301 ILE A CB  1 
ATOM   2570 C CG1 . ILE A 1 301 ? 9.668   9.054  58.906  1.00 12.83 ? 301 ILE A CG1 1 
ATOM   2571 C CG2 . ILE A 1 301 ? 12.060  9.758  58.914  1.00 15.44 ? 301 ILE A CG2 1 
ATOM   2572 C CD1 . ILE A 1 301 ? 9.492   8.953  60.448  1.00 17.08 ? 301 ILE A CD1 1 
ATOM   2573 N N   . SER A 1 302 ? 9.451   9.685  55.742  1.00 13.93 ? 302 SER A N   1 
ATOM   2574 C CA  . SER A 1 302 ? 8.887   10.817 55.010  1.00 14.32 ? 302 SER A CA  1 
ATOM   2575 C C   . SER A 1 302 ? 8.434   11.903 55.974  1.00 14.55 ? 302 SER A C   1 
ATOM   2576 O O   . SER A 1 302 ? 7.907   11.614 57.052  1.00 13.75 ? 302 SER A O   1 
ATOM   2577 C CB  . SER A 1 302 ? 7.709   10.371 54.149  1.00 16.08 ? 302 SER A CB  1 
ATOM   2578 O OG  . SER A 1 302 ? 8.126   9.481  53.126  1.00 18.21 ? 302 SER A OG  1 
ATOM   2579 N N   . VAL A 1 303 ? 8.666   13.159 55.584  1.00 14.44 ? 303 VAL A N   1 
ATOM   2580 C CA  . VAL A 1 303 ? 8.351   14.330 56.400  1.00 14.70 ? 303 VAL A CA  1 
ATOM   2581 C C   . VAL A 1 303 ? 7.644   15.340 55.511  1.00 16.34 ? 303 VAL A C   1 
ATOM   2582 O O   . VAL A 1 303 ? 8.132   15.659 54.421  1.00 16.23 ? 303 VAL A O   1 
ATOM   2583 C CB  . VAL A 1 303 ? 9.617   14.973 57.002  1.00 13.68 ? 303 VAL A CB  1 
ATOM   2584 C CG1 . VAL A 1 303 ? 9.248   16.189 57.858  1.00 17.62 ? 303 VAL A CG1 1 
ATOM   2585 C CG2 . VAL A 1 303 ? 10.418  13.940 57.820  1.00 15.61 ? 303 VAL A CG2 1 
ATOM   2586 N N   . PHE A 1 304 ? 6.505   15.845 55.966  1.00 9.93  ? 304 PHE A N   1 
ATOM   2587 C CA  . PHE A 1 304 ? 5.912   17.023 55.360  1.00 9.36  ? 304 PHE A CA  1 
ATOM   2588 C C   . PHE A 1 304 ? 6.010   18.164 56.355  1.00 12.38 ? 304 PHE A C   1 
ATOM   2589 O O   . PHE A 1 304 ? 5.928   17.950 57.570  1.00 14.76 ? 304 PHE A O   1 
ATOM   2590 C CB  . PHE A 1 304 ? 4.443   16.802 54.982  1.00 10.83 ? 304 PHE A CB  1 
ATOM   2591 C CG  . PHE A 1 304 ? 4.240   16.009 53.727  1.00 10.41 ? 304 PHE A CG  1 
ATOM   2592 C CD1 . PHE A 1 304 ? 4.373   16.609 52.486  1.00 12.44 ? 304 PHE A CD1 1 
ATOM   2593 C CD2 . PHE A 1 304 ? 3.863   14.674 53.794  1.00 14.52 ? 304 PHE A CD2 1 
ATOM   2594 C CE1 . PHE A 1 304 ? 4.153   15.872 51.314  1.00 17.02 ? 304 PHE A CE1 1 
ATOM   2595 C CE2 . PHE A 1 304 ? 3.645   13.934 52.639  1.00 15.81 ? 304 PHE A CE2 1 
ATOM   2596 C CZ  . PHE A 1 304 ? 3.790   14.533 51.396  1.00 15.89 ? 304 PHE A CZ  1 
ATOM   2597 N N   . PHE A 1 305 ? 6.209   19.365 55.841  1.00 11.94 ? 305 PHE A N   1 
ATOM   2598 C CA  . PHE A 1 305 ? 6.256   20.571 56.661  1.00 10.51 ? 305 PHE A CA  1 
ATOM   2599 C C   . PHE A 1 305 ? 4.983   21.347 56.394  1.00 10.31 ? 305 PHE A C   1 
ATOM   2600 O O   . PHE A 1 305 ? 4.682   21.659 55.236  1.00 13.95 ? 305 PHE A O   1 
ATOM   2601 C CB  . PHE A 1 305 ? 7.484   21.421 56.331  1.00 11.43 ? 305 PHE A CB  1 
ATOM   2602 C CG  . PHE A 1 305 ? 8.775   20.708 56.556  1.00 16.64 ? 305 PHE A CG  1 
ATOM   2603 C CD1 . PHE A 1 305 ? 9.301   19.875 55.580  1.00 16.25 ? 305 PHE A CD1 1 
ATOM   2604 C CD2 . PHE A 1 305 ? 9.444   20.835 57.754  1.00 14.40 ? 305 PHE A CD2 1 
ATOM   2605 C CE1 . PHE A 1 305 ? 10.484  19.200 55.797  1.00 12.88 ? 305 PHE A CE1 1 
ATOM   2606 C CE2 . PHE A 1 305 ? 10.638  20.172 57.967  1.00 11.13 ? 305 PHE A CE2 1 
ATOM   2607 C CZ  . PHE A 1 305 ? 11.146  19.343 56.990  1.00 14.08 ? 305 PHE A CZ  1 
ATOM   2608 N N   . ARG A 1 306 ? 4.229   21.632 57.452  1.00 11.57 ? 306 ARG A N   1 
ATOM   2609 C CA  . ARG A 1 306 ? 2.936   22.276 57.270  1.00 11.46 ? 306 ARG A CA  1 
ATOM   2610 C C   . ARG A 1 306 ? 3.109   23.695 56.751  1.00 14.83 ? 306 ARG A C   1 
ATOM   2611 O O   . ARG A 1 306 ? 4.134   24.351 56.974  1.00 13.58 ? 306 ARG A O   1 
ATOM   2612 C CB  . ARG A 1 306 ? 2.151   22.299 58.581  1.00 12.32 ? 306 ARG A CB  1 
ATOM   2613 C CG  . ARG A 1 306 ? 2.696   23.264 59.585  1.00 15.72 ? 306 ARG A CG  1 
ATOM   2614 C CD  . ARG A 1 306 ? 1.862   23.328 60.857  1.00 20.10 ? 306 ARG A CD  1 
ATOM   2615 N NE  . ARG A 1 306 ? 2.398   24.409 61.654  1.00 19.86 ? 306 ARG A NE  1 
ATOM   2616 C CZ  . ARG A 1 306 ? 1.717   25.151 62.508  1.00 12.73 ? 306 ARG A CZ  1 
ATOM   2617 N NH1 . ARG A 1 306 ? 0.415   24.933 62.744  1.00 12.45 ? 306 ARG A NH1 1 
ATOM   2618 N NH2 . ARG A 1 306 ? 2.356   26.111 63.136  1.00 15.31 ? 306 ARG A NH2 1 
ATOM   2619 N N   . ASP A 1 307 ? 2.098   24.152 56.021  1.00 14.25 ? 307 ASP A N   1 
ATOM   2620 C CA  . ASP A 1 307 ? 1.971   25.565 55.684  1.00 15.03 ? 307 ASP A CA  1 
ATOM   2621 C C   . ASP A 1 307 ? 1.567   26.293 56.958  1.00 11.29 ? 307 ASP A C   1 
ATOM   2622 O O   . ASP A 1 307 ? 0.408   26.245 57.373  1.00 12.44 ? 307 ASP A O   1 
ATOM   2623 C CB  . ASP A 1 307 ? 0.941   25.760 54.577  1.00 16.13 ? 307 ASP A CB  1 
ATOM   2624 C CG  . ASP A 1 307 ? 0.949   27.170 54.023  1.00 17.82 ? 307 ASP A CG  1 
ATOM   2625 O OD1 . ASP A 1 307 ? 0.886   28.127 54.815  1.00 16.99 ? 307 ASP A OD1 1 
ATOM   2626 O OD2 . ASP A 1 307 ? 1.045   27.327 52.790  1.00 22.99 ? 307 ASP A OD2 1 
ATOM   2627 N N   . LYS A 1 308 ? 2.540   26.947 57.592  1.00 14.30 ? 308 LYS A N   1 
ATOM   2628 C CA  . LYS A 1 308 ? 2.285   27.621 58.860  1.00 12.09 ? 308 LYS A CA  1 
ATOM   2629 C C   . LYS A 1 308 ? 1.244   28.731 58.714  1.00 12.64 ? 308 LYS A C   1 
ATOM   2630 O O   . LYS A 1 308 ? 0.360   28.875 59.569  1.00 14.35 ? 308 LYS A O   1 
ATOM   2631 C CB  . LYS A 1 308 ? 3.597   28.176 59.410  1.00 10.86 ? 308 LYS A CB  1 
ATOM   2632 C CG  . LYS A 1 308 ? 3.462   29.038 60.664  1.00 13.89 ? 308 LYS A CG  1 
ATOM   2633 C CD  . LYS A 1 308 ? 4.843   29.566 61.102  1.00 17.06 ? 308 LYS A CD  1 
ATOM   2634 C CE  . LYS A 1 308 ? 4.683   30.683 62.124  1.00 21.16 ? 308 LYS A CE  1 
ATOM   2635 N NZ  . LYS A 1 308 ? 3.826   30.214 63.243  1.00 20.40 ? 308 LYS A NZ  1 
ATOM   2636 N N   . THR A 1 309 ? 1.333   29.531 57.646  1.00 13.26 ? 309 THR A N   1 
ATOM   2637 C CA  . THR A 1 309 ? 0.394   30.637 57.468  1.00 12.37 ? 309 THR A CA  1 
ATOM   2638 C C   . THR A 1 309 ? -1.039  30.136 57.394  1.00 12.42 ? 309 THR A C   1 
ATOM   2639 O O   . THR A 1 309 ? -1.919  30.639 58.093  1.00 13.47 ? 309 THR A O   1 
ATOM   2640 C CB  . THR A 1 309 ? 0.727   31.419 56.201  1.00 13.96 ? 309 THR A CB  1 
ATOM   2641 O OG1 . THR A 1 309 ? 2.028   32.000 56.342  1.00 17.53 ? 309 THR A OG1 1 
ATOM   2642 C CG2 . THR A 1 309 ? -0.295  32.521 55.963  1.00 18.24 ? 309 THR A CG2 1 
ATOM   2643 N N   . LEU A 1 310 ? -1.294  29.154 56.525  1.00 10.13 ? 310 LEU A N   1 
ATOM   2644 C CA  . LEU A 1 310 ? -2.655  28.644 56.395  1.00 8.88  ? 310 LEU A CA  1 
ATOM   2645 C C   . LEU A 1 310 ? -3.130  28.022 57.694  1.00 9.90  ? 310 LEU A C   1 
ATOM   2646 O O   . LEU A 1 310 ? -4.308  28.157 58.060  1.00 9.65  ? 310 LEU A O   1 
ATOM   2647 C CB  . LEU A 1 310 ? -2.733  27.618 55.270  1.00 9.50  ? 310 LEU A CB  1 
ATOM   2648 C CG  . LEU A 1 310 ? -2.494  28.211 53.884  1.00 12.62 ? 310 LEU A CG  1 
ATOM   2649 C CD1 . LEU A 1 310 ? -2.536  27.103 52.844  1.00 18.64 ? 310 LEU A CD1 1 
ATOM   2650 C CD2 . LEU A 1 310 ? -3.545  29.278 53.577  1.00 15.71 ? 310 LEU A CD2 1 
ATOM   2651 N N   . SER A 1 311 ? -2.247  27.283 58.370  1.00 11.12 ? 311 SER A N   1 
ATOM   2652 C CA  . SER A 1 311 ? -2.641  26.612 59.602  1.00 10.48 ? 311 SER A CA  1 
ATOM   2653 C C   . SER A 1 311 ? -2.970  27.631 60.672  1.00 11.52 ? 311 SER A C   1 
ATOM   2654 O O   . SER A 1 311 ? -3.949  27.477 61.408  1.00 11.69 ? 311 SER A O   1 
ATOM   2655 C CB  . SER A 1 311 ? -1.521  25.678 60.077  1.00 11.19 ? 311 SER A CB  1 
ATOM   2656 O OG  . SER A 1 311 ? -1.213  24.723 59.077  1.00 10.80 ? 311 SER A OG  1 
ATOM   2657 N N   . ASP A 1 312 ? -2.168  28.692 60.755  1.00 13.30 ? 312 ASP A N   1 
ATOM   2658 C CA  . ASP A 1 312 ? -2.416  29.728 61.752  1.00 13.54 ? 312 ASP A CA  1 
ATOM   2659 C C   . ASP A 1 312 ? -3.638  30.571 61.408  1.00 14.19 ? 312 ASP A C   1 
ATOM   2660 O O   . ASP A 1 312 ? -4.265  31.116 62.311  1.00 11.79 ? 312 ASP A O   1 
ATOM   2661 C CB  . ASP A 1 312 ? -1.216  30.654 61.889  1.00 13.42 ? 312 ASP A CB  1 
ATOM   2662 C CG  . ASP A 1 312 ? -0.050  30.036 62.650  1.00 20.03 ? 312 ASP A CG  1 
ATOM   2663 O OD1 . ASP A 1 312 ? -0.207  29.005 63.327  1.00 18.81 ? 312 ASP A OD1 1 
ATOM   2664 O OD2 . ASP A 1 312 ? 1.048   30.627 62.557  1.00 19.21 ? 312 ASP A OD2 1 
ATOM   2665 N N   . LEU A 1 313 ? -3.951  30.762 60.119  1.00 10.92 ? 313 LEU A N   1 
ATOM   2666 C CA  . LEU A 1 313 ? -5.161  31.511 59.783  1.00 11.77 ? 313 LEU A CA  1 
ATOM   2667 C C   . LEU A 1 313 ? -6.386  30.847 60.395  1.00 13.03 ? 313 LEU A C   1 
ATOM   2668 O O   . LEU A 1 313 ? -7.233  31.515 61.002  1.00 13.01 ? 313 LEU A O   1 
ATOM   2669 C CB  . LEU A 1 313 ? -5.319  31.635 58.267  1.00 10.26 ? 313 LEU A CB  1 
ATOM   2670 C CG  . LEU A 1 313 ? -4.381  32.665 57.640  1.00 15.66 ? 313 LEU A CG  1 
ATOM   2671 C CD1 . LEU A 1 313 ? -4.293  32.454 56.135  1.00 14.39 ? 313 LEU A CD1 1 
ATOM   2672 C CD2 . LEU A 1 313 ? -4.847  34.098 57.973  1.00 14.57 ? 313 LEU A CD2 1 
ATOM   2673 N N   . ILE A 1 314 ? -6.491  29.522 60.257  1.00 9.90  ? 314 ILE A N   1 
ATOM   2674 C CA  . ILE A 1 314 ? -7.635  28.824 60.827  1.00 10.25 ? 314 ILE A CA  1 
ATOM   2675 C C   . ILE A 1 314 ? -7.538  28.819 62.347  1.00 13.50 ? 314 ILE A C   1 
ATOM   2676 O O   . ILE A 1 314 ? -8.503  29.130 63.053  1.00 14.03 ? 314 ILE A O   1 
ATOM   2677 C CB  . ILE A 1 314 ? -7.732  27.395 60.270  1.00 11.03 ? 314 ILE A CB  1 
ATOM   2678 C CG1 . ILE A 1 314 ? -7.990  27.436 58.761  1.00 8.98  ? 314 ILE A CG1 1 
ATOM   2679 C CG2 . ILE A 1 314 ? -8.805  26.612 61.020  1.00 12.26 ? 314 ILE A CG2 1 
ATOM   2680 C CD1 . ILE A 1 314 ? -8.020  26.049 58.089  1.00 12.08 ? 314 ILE A CD1 1 
ATOM   2681 N N   . GLY A 1 315 ? -6.358  28.488 62.872  1.00 11.45 ? 315 GLY A N   1 
ATOM   2682 C CA  . GLY A 1 315 ? -6.236  28.281 64.303  1.00 11.93 ? 315 GLY A CA  1 
ATOM   2683 C C   . GLY A 1 315 ? -6.294  29.549 65.124  1.00 14.27 ? 315 GLY A C   1 
ATOM   2684 O O   . GLY A 1 315 ? -6.699  29.496 66.289  1.00 14.14 ? 315 GLY A O   1 
ATOM   2685 N N   . PHE A 1 316 ? -5.923  30.690 64.545  1.00 12.03 ? 316 PHE A N   1 
ATOM   2686 C CA  . PHE A 1 316 ? -5.806  31.919 65.322  1.00 13.51 ? 316 PHE A CA  1 
ATOM   2687 C C   . PHE A 1 316 ? -6.473  33.138 64.712  1.00 13.73 ? 316 PHE A C   1 
ATOM   2688 O O   . PHE A 1 316 ? -6.802  34.064 65.462  1.00 19.34 ? 316 PHE A O   1 
ATOM   2689 C CB  . PHE A 1 316 ? -4.324  32.240 65.571  1.00 13.61 ? 316 PHE A CB  1 
ATOM   2690 C CG  . PHE A 1 316 ? -3.642  31.223 66.416  1.00 21.89 ? 316 PHE A CG  1 
ATOM   2691 C CD1 . PHE A 1 316 ? -3.851  31.191 67.788  1.00 25.81 ? 316 PHE A CD1 1 
ATOM   2692 C CD2 . PHE A 1 316 ? -2.837  30.255 65.843  1.00 24.94 ? 316 PHE A CD2 1 
ATOM   2693 C CE1 . PHE A 1 316 ? -3.238  30.234 68.574  1.00 28.73 ? 316 PHE A CE1 1 
ATOM   2694 C CE2 . PHE A 1 316 ? -2.220  29.294 66.629  1.00 33.40 ? 316 PHE A CE2 1 
ATOM   2695 C CZ  . PHE A 1 316 ? -2.424  29.284 67.994  1.00 32.66 ? 316 PHE A CZ  1 
ATOM   2696 N N   . SER A 1 317 ? -6.671  33.195 63.396  1.00 11.96 ? 317 SER A N   1 
ATOM   2697 C CA  . SER A 1 317 ? -7.139  34.422 62.758  1.00 9.39  ? 317 SER A CA  1 
ATOM   2698 C C   . SER A 1 317 ? -8.632  34.443 62.453  1.00 12.02 ? 317 SER A C   1 
ATOM   2699 O O   . SER A 1 317 ? -9.305  35.427 62.774  1.00 13.49 ? 317 SER A O   1 
ATOM   2700 C CB  . SER A 1 317 ? -6.366  34.658 61.460  1.00 14.73 ? 317 SER A CB  1 
ATOM   2701 O OG  . SER A 1 317 ? -4.989  34.818 61.755  1.00 20.76 ? 317 SER A OG  1 
ATOM   2702 N N   . TYR A 1 318 ? -9.151  33.411 61.781  1.00 11.14 ? 318 TYR A N   1 
ATOM   2703 C CA  . TYR A 1 318 ? -10.463 33.518 61.146  1.00 11.24 ? 318 TYR A CA  1 
ATOM   2704 C C   . TYR A 1 318 ? -11.628 33.593 62.139  1.00 14.35 ? 318 TYR A C   1 
ATOM   2705 O O   . TYR A 1 318 ? -12.729 33.987 61.739  1.00 13.83 ? 318 TYR A O   1 
ATOM   2706 C CB  . TYR A 1 318 ? -10.672 32.340 60.196  1.00 13.18 ? 318 TYR A CB  1 
ATOM   2707 C CG  . TYR A 1 318 ? -9.874  32.402 58.906  1.00 13.72 ? 318 TYR A CG  1 
ATOM   2708 C CD1 . TYR A 1 318 ? -9.471  33.614 58.346  1.00 15.60 ? 318 TYR A CD1 1 
ATOM   2709 C CD2 . TYR A 1 318 ? -9.555  31.235 58.237  1.00 11.80 ? 318 TYR A CD2 1 
ATOM   2710 C CE1 . TYR A 1 318 ? -8.776  33.643 57.143  1.00 13.48 ? 318 TYR A CE1 1 
ATOM   2711 C CE2 . TYR A 1 318 ? -8.870  31.244 57.056  1.00 10.65 ? 318 TYR A CE2 1 
ATOM   2712 C CZ  . TYR A 1 318 ? -8.471  32.438 56.513  1.00 15.20 ? 318 TYR A CZ  1 
ATOM   2713 O OH  . TYR A 1 318 ? -7.791  32.406 55.322  1.00 15.76 ? 318 TYR A OH  1 
ATOM   2714 N N   . HIS A 1 319 ? -11.425 33.259 63.418  1.00 14.84 ? 319 HIS A N   1 
ATOM   2715 C CA  . HIS A 1 319 ? -12.473 33.538 64.398  1.00 14.37 ? 319 HIS A CA  1 
ATOM   2716 C C   . HIS A 1 319 ? -12.878 35.011 64.378  1.00 14.13 ? 319 HIS A C   1 
ATOM   2717 O O   . HIS A 1 319 ? -14.033 35.338 64.662  1.00 16.07 ? 319 HIS A O   1 
ATOM   2718 C CB  . HIS A 1 319 ? -12.018 33.179 65.807  1.00 12.04 ? 319 HIS A CB  1 
ATOM   2719 C CG  . HIS A 1 319 ? -11.025 34.146 66.374  1.00 12.62 ? 319 HIS A CG  1 
ATOM   2720 N ND1 . HIS A 1 319 ? -11.385 35.213 67.168  1.00 18.35 ? 319 HIS A ND1 1 
ATOM   2721 C CD2 . HIS A 1 319 ? -9.681  34.214 66.238  1.00 13.03 ? 319 HIS A CD2 1 
ATOM   2722 C CE1 . HIS A 1 319 ? -10.302 35.885 67.516  1.00 16.28 ? 319 HIS A CE1 1 
ATOM   2723 N NE2 . HIS A 1 319 ? -9.254  35.303 66.963  1.00 19.26 ? 319 HIS A NE2 1 
ATOM   2724 N N   . ALA A 1 320 ? -11.946 35.905 64.046  1.00 13.45 ? 320 ALA A N   1 
ATOM   2725 C CA  . ALA A 1 320 ? -12.202 37.340 64.026  1.00 12.95 ? 320 ALA A CA  1 
ATOM   2726 C C   . ALA A 1 320 ? -12.763 37.824 62.694  1.00 18.33 ? 320 ALA A C   1 
ATOM   2727 O O   . ALA A 1 320 ? -12.946 39.037 62.518  1.00 17.08 ? 320 ALA A O   1 
ATOM   2728 C CB  . ALA A 1 320 ? -10.907 38.108 64.355  1.00 13.56 ? 320 ALA A CB  1 
ATOM   2729 N N   . TRP A 1 321 ? -13.027 36.914 61.762  1.00 17.08 ? 321 TRP A N   1 
ATOM   2730 C CA  . TRP A 1 321 ? -13.560 37.227 60.445  1.00 17.31 ? 321 TRP A CA  1 
ATOM   2731 C C   . TRP A 1 321 ? -14.990 36.732 60.291  1.00 15.36 ? 321 TRP A C   1 
ATOM   2732 O O   . TRP A 1 321 ? -15.403 35.748 60.909  1.00 19.31 ? 321 TRP A O   1 
ATOM   2733 C CB  . TRP A 1 321 ? -12.765 36.559 59.330  1.00 16.12 ? 321 TRP A CB  1 
ATOM   2734 C CG  . TRP A 1 321 ? -11.330 36.908 59.193  1.00 15.50 ? 321 TRP A CG  1 
ATOM   2735 C CD1 . TRP A 1 321 ? -10.381 36.970 60.175  1.00 15.05 ? 321 TRP A CD1 1 
ATOM   2736 C CD2 . TRP A 1 321 ? -10.655 37.163 57.961  1.00 18.19 ? 321 TRP A CD2 1 
ATOM   2737 N NE1 . TRP A 1 321 ? -9.159  37.280 59.625  1.00 17.84 ? 321 TRP A NE1 1 
ATOM   2738 C CE2 . TRP A 1 321 ? -9.301  37.392 58.265  1.00 16.56 ? 321 TRP A CE2 1 
ATOM   2739 C CE3 . TRP A 1 321 ? -11.071 37.220 56.625  1.00 19.25 ? 321 TRP A CE3 1 
ATOM   2740 C CZ2 . TRP A 1 321 ? -8.354  37.689 57.278  1.00 20.79 ? 321 TRP A CZ2 1 
ATOM   2741 C CZ3 . TRP A 1 321 ? -10.139 37.518 55.652  1.00 17.82 ? 321 TRP A CZ3 1 
ATOM   2742 C CH2 . TRP A 1 321 ? -8.793  37.747 55.983  1.00 22.09 ? 321 TRP A CH2 1 
ATOM   2743 N N   . ASN A 1 322 ? -15.718 37.407 59.412  1.00 17.31 ? 322 ASN A N   1 
ATOM   2744 C CA  . ASN A 1 322 ? -16.938 36.871 58.836  1.00 18.28 ? 322 ASN A CA  1 
ATOM   2745 C C   . ASN A 1 322 ? -16.623 35.569 58.094  1.00 24.05 ? 322 ASN A C   1 
ATOM   2746 O O   . ASN A 1 322 ? -15.563 35.427 57.479  1.00 20.43 ? 322 ASN A O   1 
ATOM   2747 C CB  . ASN A 1 322 ? -17.520 37.971 57.929  1.00 28.66 ? 322 ASN A CB  1 
ATOM   2748 C CG  . ASN A 1 322 ? -18.444 37.464 56.874  1.00 36.70 ? 322 ASN A CG  1 
ATOM   2749 O OD1 . ASN A 1 322 ? -18.011 36.863 55.896  1.00 33.52 ? 322 ASN A OD1 1 
ATOM   2750 N ND2 . ASN A 1 322 ? -19.725 37.794 57.006  1.00 36.06 ? 322 ASN A ND2 1 
ATOM   2751 N N   . ALA A 1 323 ? -17.540 34.602 58.166  1.00 19.08 ? 323 ALA A N   1 
ATOM   2752 C CA  . ALA A 1 323 ? -17.214 33.257 57.690  1.00 16.95 ? 323 ALA A CA  1 
ATOM   2753 C C   . ALA A 1 323 ? -17.009 33.219 56.179  1.00 15.05 ? 323 ALA A C   1 
ATOM   2754 O O   . ALA A 1 323 ? -16.078 32.557 55.694  1.00 16.38 ? 323 ALA A O   1 
ATOM   2755 C CB  . ALA A 1 323 ? -18.299 32.264 58.107  1.00 19.38 ? 323 ALA A CB  1 
ATOM   2756 N N   . GLU A 1 324 ? -17.875 33.907 55.418  1.00 18.40 ? 324 GLU A N   1 
ATOM   2757 C CA  . GLU A 1 324 ? -17.723 33.940 53.961  1.00 20.66 ? 324 GLU A CA  1 
ATOM   2758 C C   . GLU A 1 324 ? -16.386 34.559 53.562  1.00 22.21 ? 324 GLU A C   1 
ATOM   2759 O O   . GLU A 1 324 ? -15.705 34.054 52.669  1.00 20.54 ? 324 GLU A O   1 
ATOM   2760 C CB  . GLU A 1 324 ? -18.860 34.722 53.298  1.00 32.81 ? 324 GLU A CB  1 
ATOM   2761 C CG  . GLU A 1 324 ? -20.213 34.048 53.296  1.00 57.50 ? 324 GLU A CG  1 
ATOM   2762 C CD  . GLU A 1 324 ? -21.023 34.379 54.523  1.00 77.30 ? 324 GLU A CD  1 
ATOM   2763 O OE1 . GLU A 1 324 ? -22.042 35.073 54.377  1.00 85.39 ? 324 GLU A OE1 1 
ATOM   2764 O OE2 . GLU A 1 324 ? -20.637 33.956 55.630  1.00 81.18 ? 324 GLU A OE2 1 
ATOM   2765 N N   . ASP A 1 325 ? -16.016 35.679 54.196  1.00 20.81 ? 325 ASP A N   1 
ATOM   2766 C CA  . ASP A 1 325 ? -14.764 36.358 53.875  1.00 20.53 ? 325 ASP A CA  1 
ATOM   2767 C C   . ASP A 1 325 ? -13.556 35.489 54.182  1.00 17.76 ? 325 ASP A C   1 
ATOM   2768 O O   . ASP A 1 325 ? -12.569 35.495 53.432  1.00 17.19 ? 325 ASP A O   1 
ATOM   2769 C CB  . ASP A 1 325 ? -14.650 37.663 54.665  1.00 17.92 ? 325 ASP A CB  1 
ATOM   2770 C CG  . ASP A 1 325 ? -15.672 38.697 54.252  1.00 37.87 ? 325 ASP A CG  1 
ATOM   2771 O OD1 . ASP A 1 325 ? -16.301 38.534 53.186  1.00 45.19 ? 325 ASP A OD1 1 
ATOM   2772 O OD2 . ASP A 1 325 ? -15.842 39.684 54.998  1.00 45.30 ? 325 ASP A OD2 1 
ATOM   2773 N N   . ALA A 1 326 ? -13.597 34.768 55.304  1.00 15.02 ? 326 ALA A N   1 
ATOM   2774 C CA  . ALA A 1 326 ? -12.498 33.887 55.673  1.00 17.29 ? 326 ALA A CA  1 
ATOM   2775 C C   . ALA A 1 326 ? -12.307 32.781 54.646  1.00 17.97 ? 326 ALA A C   1 
ATOM   2776 O O   . ALA A 1 326 ? -11.174 32.455 54.275  1.00 14.80 ? 326 ALA A O   1 
ATOM   2777 C CB  . ALA A 1 326 ? -12.758 33.282 57.058  1.00 16.54 ? 326 ALA A CB  1 
ATOM   2778 N N   . VAL A 1 327 ? -13.402 32.183 54.179  1.00 11.94 ? 327 VAL A N   1 
ATOM   2779 C CA  . VAL A 1 327 ? -13.283 31.124 53.181  1.00 14.77 ? 327 VAL A CA  1 
ATOM   2780 C C   . VAL A 1 327 ? -12.761 31.685 51.863  1.00 14.62 ? 327 VAL A C   1 
ATOM   2781 O O   . VAL A 1 327 ? -11.916 31.064 51.210  1.00 17.21 ? 327 VAL A O   1 
ATOM   2782 C CB  . VAL A 1 327 ? -14.630 30.399 53.006  1.00 14.76 ? 327 VAL A CB  1 
ATOM   2783 C CG1 . VAL A 1 327 ? -14.583 29.457 51.796  1.00 16.15 ? 327 VAL A CG1 1 
ATOM   2784 C CG2 . VAL A 1 327 ? -14.945 29.596 54.275  1.00 16.94 ? 327 VAL A CG2 1 
ATOM   2785 N N   . ARG A 1 328 ? -13.238 32.867 51.466  1.00 14.18 ? 328 ARG A N   1 
ATOM   2786 C CA  . ARG A 1 328 ? -12.716 33.520 50.267  1.00 18.01 ? 328 ARG A CA  1 
ATOM   2787 C C   . ARG A 1 328 ? -11.215 33.765 50.384  1.00 16.49 ? 328 ARG A C   1 
ATOM   2788 O O   . ARG A 1 328 ? -10.464 33.519 49.437  1.00 18.84 ? 328 ARG A O   1 
ATOM   2789 C CB  . ARG A 1 328 ? -13.450 34.833 50.022  1.00 17.36 ? 328 ARG A CB  1 
ATOM   2790 C CG  . ARG A 1 328 ? -13.001 35.563 48.768  1.00 23.57 ? 328 ARG A CG  1 
ATOM   2791 C CD  . ARG A 1 328 ? -13.791 36.854 48.548  1.00 33.84 ? 328 ARG A CD  1 
ATOM   2792 N NE  . ARG A 1 328 ? -13.394 37.905 49.481  1.00 39.12 ? 328 ARG A NE  1 
ATOM   2793 C CZ  . ARG A 1 328 ? -14.197 38.434 50.398  1.00 45.17 ? 328 ARG A CZ  1 
ATOM   2794 N NH1 . ARG A 1 328 ? -15.450 38.006 50.515  1.00 40.73 ? 328 ARG A NH1 1 
ATOM   2795 N NH2 . ARG A 1 328 ? -13.746 39.390 51.200  1.00 47.59 ? 328 ARG A NH2 1 
ATOM   2796 N N   . ASP A 1 329 ? -10.765 34.225 51.554  1.00 16.16 ? 329 ASP A N   1 
ATOM   2797 C CA  . ASP A 1 329 ? -9.344  34.463 51.776  1.00 14.77 ? 329 ASP A CA  1 
ATOM   2798 C C   . ASP A 1 329 ? -8.543  33.173 51.647  1.00 16.26 ? 329 ASP A C   1 
ATOM   2799 O O   . ASP A 1 329 ? -7.511  33.135 50.965  1.00 15.93 ? 329 ASP A O   1 
ATOM   2800 C CB  . ASP A 1 329 ? -9.139  35.080 53.160  1.00 13.93 ? 329 ASP A CB  1 
ATOM   2801 C CG  . ASP A 1 329 ? -7.700  35.460 53.414  1.00 19.47 ? 329 ASP A CG  1 
ATOM   2802 O OD1 . ASP A 1 329 ? -7.255  36.471 52.825  1.00 19.80 ? 329 ASP A OD1 1 
ATOM   2803 O OD2 . ASP A 1 329 ? -7.013  34.742 54.177  1.00 20.22 ? 329 ASP A OD2 1 
ATOM   2804 N N   . PHE A 1 330 ? -9.005  32.114 52.312  1.00 13.62 ? 330 PHE A N   1 
ATOM   2805 C CA  . PHE A 1 330 ? -8.309  30.830 52.316  1.00 16.80 ? 330 PHE A CA  1 
ATOM   2806 C C   . PHE A 1 330 ? -8.233  30.246 50.910  1.00 21.48 ? 330 PHE A C   1 
ATOM   2807 O O   . PHE A 1 330 ? -7.155  29.859 50.439  1.00 15.58 ? 330 PHE A O   1 
ATOM   2808 C CB  . PHE A 1 330 ? -9.033  29.882 53.276  1.00 14.28 ? 330 PHE A CB  1 
ATOM   2809 C CG  . PHE A 1 330 ? -8.276  28.636 53.612  1.00 14.43 ? 330 PHE A CG  1 
ATOM   2810 C CD1 . PHE A 1 330 ? -7.322  28.639 54.618  1.00 19.49 ? 330 PHE A CD1 1 
ATOM   2811 C CD2 . PHE A 1 330 ? -8.555  27.443 52.952  1.00 15.04 ? 330 PHE A CD2 1 
ATOM   2812 C CE1 . PHE A 1 330 ? -6.639  27.471 54.956  1.00 16.71 ? 330 PHE A CE1 1 
ATOM   2813 C CE2 . PHE A 1 330 ? -7.872  26.265 53.283  1.00 17.65 ? 330 PHE A CE2 1 
ATOM   2814 C CZ  . PHE A 1 330 ? -6.919  26.286 54.286  1.00 16.81 ? 330 PHE A CZ  1 
ATOM   2815 N N   . ILE A 1 331 ? -9.371  30.188 50.216  1.00 16.13 ? 331 ILE A N   1 
ATOM   2816 C CA  . ILE A 1 331 ? -9.370  29.700 48.838  1.00 17.64 ? 331 ILE A CA  1 
ATOM   2817 C C   . ILE A 1 331 ? -8.470  30.563 47.963  1.00 19.96 ? 331 ILE A C   1 
ATOM   2818 O O   . ILE A 1 331 ? -7.734  30.050 47.111  1.00 15.83 ? 331 ILE A O   1 
ATOM   2819 C CB  . ILE A 1 331 ? -10.808 29.641 48.289  1.00 23.95 ? 331 ILE A CB  1 
ATOM   2820 C CG1 . ILE A 1 331 ? -11.649 28.668 49.108  1.00 30.00 ? 331 ILE A CG1 1 
ATOM   2821 C CG2 . ILE A 1 331 ? -10.803 29.241 46.816  1.00 25.56 ? 331 ILE A CG2 1 
ATOM   2822 C CD1 . ILE A 1 331 ? -11.120 27.256 49.100  1.00 28.00 ? 331 ILE A CD1 1 
ATOM   2823 N N   . GLY A 1 332 ? -8.519  31.888 48.148  1.00 15.84 ? 332 GLY A N   1 
ATOM   2824 C CA  . GLY A 1 332 ? -7.682  32.760 47.347  1.00 19.50 ? 332 GLY A CA  1 
ATOM   2825 C C   . GLY A 1 332 ? -6.205  32.522 47.582  1.00 21.45 ? 332 GLY A C   1 
ATOM   2826 O O   . GLY A 1 332 ? -5.400  32.633 46.658  1.00 18.64 ? 332 GLY A O   1 
ATOM   2827 N N   . ARG A 1 333 ? -5.834  32.165 48.815  1.00 18.56 ? 333 ARG A N   1 
ATOM   2828 C CA  . ARG A 1 333 ? -4.441  31.840 49.082  1.00 14.59 ? 333 ARG A CA  1 
ATOM   2829 C C   . ARG A 1 333 ? -4.052  30.532 48.410  1.00 13.28 ? 333 ARG A C   1 
ATOM   2830 O O   . ARG A 1 333 ? -2.963  30.426 47.838  1.00 15.93 ? 333 ARG A O   1 
ATOM   2831 C CB  . ARG A 1 333 ? -4.202  31.787 50.583  1.00 13.54 ? 333 ARG A CB  1 
ATOM   2832 C CG  . ARG A 1 333 ? -4.160  33.161 51.223  1.00 13.45 ? 333 ARG A CG  1 
ATOM   2833 C CD  . ARG A 1 333 ? -4.215  33.025 52.736  1.00 14.98 ? 333 ARG A CD  1 
ATOM   2834 N NE  . ARG A 1 333 ? -4.230  34.322 53.393  1.00 17.01 ? 333 ARG A NE  1 
ATOM   2835 C CZ  . ARG A 1 333 ? -3.135  35.001 53.727  1.00 21.52 ? 333 ARG A CZ  1 
ATOM   2836 N NH1 . ARG A 1 333 ? -1.931  34.498 53.484  1.00 20.02 ? 333 ARG A NH1 1 
ATOM   2837 N NH2 . ARG A 1 333 ? -3.246  36.174 54.323  1.00 21.74 ? 333 ARG A NH2 1 
ATOM   2838 N N   . LEU A 1 334 ? -4.950  29.544 48.430  1.00 14.57 ? 334 LEU A N   1 
ATOM   2839 C CA  . LEU A 1 334 ? -4.700  28.299 47.712  1.00 15.17 ? 334 LEU A CA  1 
ATOM   2840 C C   . LEU A 1 334 ? -4.556  28.538 46.218  1.00 14.38 ? 334 LEU A C   1 
ATOM   2841 O O   . LEU A 1 334 ? -3.710  27.919 45.563  1.00 17.53 ? 334 LEU A O   1 
ATOM   2842 C CB  . LEU A 1 334 ? -5.833  27.304 47.970  1.00 11.41 ? 334 LEU A CB  1 
ATOM   2843 C CG  . LEU A 1 334 ? -5.980  26.842 49.419  1.00 14.35 ? 334 LEU A CG  1 
ATOM   2844 C CD1 . LEU A 1 334 ? -7.168  25.883 49.540  1.00 14.93 ? 334 LEU A CD1 1 
ATOM   2845 C CD2 . LEU A 1 334 ? -4.695  26.177 49.913  1.00 14.98 ? 334 LEU A CD2 1 
ATOM   2846 N N   . LYS A 1 335 ? -5.386  29.423 45.658  1.00 15.16 ? 335 LYS A N   1 
ATOM   2847 C CA  . LYS A 1 335 ? -5.270  29.746 44.240  1.00 18.10 ? 335 LYS A CA  1 
ATOM   2848 C C   . LYS A 1 335 ? -3.891  30.306 43.914  1.00 20.03 ? 335 LYS A C   1 
ATOM   2849 O O   . LYS A 1 335 ? -3.310  29.970 42.877  1.00 18.91 ? 335 LYS A O   1 
ATOM   2850 C CB  . LYS A 1 335 ? -6.367  30.740 43.845  1.00 19.16 ? 335 LYS A CB  1 
ATOM   2851 C CG  . LYS A 1 335 ? -6.487  31.042 42.364  1.00 33.64 ? 335 LYS A CG  1 
ATOM   2852 C CD  . LYS A 1 335 ? -7.919  31.482 42.029  1.00 37.13 ? 335 LYS A CD  1 
ATOM   2853 C CE  . LYS A 1 335 ? -8.030  32.055 40.626  1.00 48.73 ? 335 LYS A CE  1 
ATOM   2854 N NZ  . LYS A 1 335 ? -7.497  33.444 40.552  1.00 53.43 ? 335 LYS A NZ  1 
ATOM   2855 N N   . LYS A 1 336 ? -3.343  31.152 44.792  1.00 16.01 ? 336 LYS A N   1 
ATOM   2856 C CA  . LYS A 1 336 ? -2.033  31.736 44.515  1.00 17.61 ? 336 LYS A CA  1 
ATOM   2857 C C   . LYS A 1 336 ? -0.931  30.688 44.583  1.00 16.80 ? 336 LYS A C   1 
ATOM   2858 O O   . LYS A 1 336 ? -0.028  30.682 43.733  1.00 20.50 ? 336 LYS A O   1 
ATOM   2859 C CB  . LYS A 1 336 ? -1.750  32.884 45.476  1.00 23.53 ? 336 LYS A CB  1 
ATOM   2860 C CG  . LYS A 1 336 ? -2.516  34.139 45.123  1.00 32.94 ? 336 LYS A CG  1 
ATOM   2861 C CD  . LYS A 1 336 ? -1.984  35.352 45.859  1.00 46.23 ? 336 LYS A CD  1 
ATOM   2862 C CE  . LYS A 1 336 ? -0.467  35.358 45.882  1.00 55.42 ? 336 LYS A CE  1 
ATOM   2863 N NZ  . LYS A 1 336 ? 0.046   36.176 47.011  1.00 56.54 ? 336 LYS A NZ  1 
ATOM   2864 N N   . ILE A 1 337 ? -0.992  29.789 45.567  1.00 17.72 ? 337 ILE A N   1 
ATOM   2865 C CA  . ILE A 1 337 ? -0.058  28.665 45.606  1.00 19.94 ? 337 ILE A CA  1 
ATOM   2866 C C   . ILE A 1 337 ? -0.165  27.856 44.319  1.00 18.16 ? 337 ILE A C   1 
ATOM   2867 O O   . ILE A 1 337 ? 0.839   27.572 43.651  1.00 23.35 ? 337 ILE A O   1 
ATOM   2868 C CB  . ILE A 1 337 ? -0.320  27.783 46.843  1.00 16.98 ? 337 ILE A CB  1 
ATOM   2869 C CG1 . ILE A 1 337 ? -0.160  28.590 48.146  1.00 14.00 ? 337 ILE A CG1 1 
ATOM   2870 C CG2 . ILE A 1 337 ? 0.601   26.582 46.829  1.00 19.89 ? 337 ILE A CG2 1 
ATOM   2871 C CD1 . ILE A 1 337 ? -0.699  27.882 49.390  1.00 18.05 ? 337 ILE A CD1 1 
ATOM   2872 N N   . HIS A 1 338 ? -1.399  27.489 43.953  1.00 15.65 ? 338 HIS A N   1 
ATOM   2873 C CA  . HIS A 1 338 ? -1.670  26.746 42.726  1.00 16.26 ? 338 HIS A CA  1 
ATOM   2874 C C   . HIS A 1 338 ? -1.034  27.407 41.504  1.00 21.17 ? 338 HIS A C   1 
ATOM   2875 O O   . HIS A 1 338 ? -0.440  26.729 40.659  1.00 23.27 ? 338 HIS A O   1 
ATOM   2876 C CB  . HIS A 1 338 ? -3.193  26.630 42.566  1.00 20.61 ? 338 HIS A CB  1 
ATOM   2877 C CG  . HIS A 1 338 ? -3.639  25.970 41.300  1.00 27.93 ? 338 HIS A CG  1 
ATOM   2878 N ND1 . HIS A 1 338 ? -3.479  24.622 41.064  1.00 26.49 ? 338 HIS A ND1 1 
ATOM   2879 C CD2 . HIS A 1 338 ? -4.267  26.471 40.211  1.00 31.00 ? 338 HIS A CD2 1 
ATOM   2880 C CE1 . HIS A 1 338 ? -3.986  24.322 39.882  1.00 26.38 ? 338 HIS A CE1 1 
ATOM   2881 N NE2 . HIS A 1 338 ? -4.464  25.427 39.340  1.00 32.16 ? 338 HIS A NE2 1 
ATOM   2882 N N   . GLU A 1 339 ? -1.131  28.733 41.400  1.00 18.31 ? 339 GLU A N   1 
ATOM   2883 C CA  . GLU A 1 339 ? -0.614  29.421 40.225  1.00 19.34 ? 339 GLU A CA  1 
ATOM   2884 C C   . GLU A 1 339 ? 0.880   29.701 40.307  1.00 26.35 ? 339 GLU A C   1 
ATOM   2885 O O   . GLU A 1 339 ? 1.489   30.046 39.284  1.00 27.83 ? 339 GLU A O   1 
ATOM   2886 C CB  . GLU A 1 339 ? -1.383  30.731 40.005  1.00 22.61 ? 339 GLU A CB  1 
ATOM   2887 C CG  . GLU A 1 339 ? -2.865  30.507 39.676  1.00 32.21 ? 339 GLU A CG  1 
ATOM   2888 C CD  . GLU A 1 339 ? -3.709  31.761 39.828  1.00 48.16 ? 339 GLU A CD  1 
ATOM   2889 O OE1 . GLU A 1 339 ? -4.860  31.767 39.337  1.00 52.24 ? 339 GLU A OE1 1 
ATOM   2890 O OE2 . GLU A 1 339 ? -3.227  32.739 40.437  1.00 49.70 ? 339 GLU A OE2 1 
ATOM   2891 N N   . SER A 1 340 ? 1.494   29.521 41.475  1.00 28.87 ? 340 SER A N   1 
ATOM   2892 C CA  . SER A 1 340 ? 2.870   29.951 41.682  1.00 26.78 ? 340 SER A CA  1 
ATOM   2893 C C   . SER A 1 340 ? 3.901   28.902 41.294  1.00 26.01 ? 340 SER A C   1 
ATOM   2894 O O   . SER A 1 340 ? 5.093   29.223 41.254  1.00 28.10 ? 340 SER A O   1 
ATOM   2895 C CB  . SER A 1 340 ? 3.093   30.337 43.146  1.00 29.71 ? 340 SER A CB  1 
ATOM   2896 O OG  . SER A 1 340 ? 3.263   29.174 43.939  1.00 27.05 ? 340 SER A OG  1 
ATOM   2897 N N   . VAL A 1 341 ? 3.490   27.661 41.032  1.00 24.26 ? 341 VAL A N   1 
ATOM   2898 C CA  . VAL A 1 341 ? 4.416   26.604 40.642  1.00 26.07 ? 341 VAL A CA  1 
ATOM   2899 C C   . VAL A 1 341 ? 3.785   25.819 39.503  1.00 24.35 ? 341 VAL A C   1 
ATOM   2900 O O   . VAL A 1 341 ? 2.559   25.775 39.362  1.00 26.64 ? 341 VAL A O   1 
ATOM   2901 C CB  . VAL A 1 341 ? 4.769   25.668 41.825  1.00 24.28 ? 341 VAL A CB  1 
ATOM   2902 C CG1 . VAL A 1 341 ? 5.530   26.429 42.904  1.00 26.64 ? 341 VAL A CG1 1 
ATOM   2903 C CG2 . VAL A 1 341 ? 3.502   25.046 42.417  1.00 21.01 ? 341 VAL A CG2 1 
ATOM   2904 N N   . ASP A 1 342 ? 4.626   25.220 38.664  1.00 24.48 ? 342 ASP A N   1 
ATOM   2905 C CA  . ASP A 1 342 ? 4.123   24.404 37.571  1.00 25.48 ? 342 ASP A CA  1 
ATOM   2906 C C   . ASP A 1 342 ? 4.068   22.921 37.920  1.00 33.33 ? 342 ASP A C   1 
ATOM   2907 O O   . ASP A 1 342 ? 3.683   22.112 37.074  1.00 36.58 ? 342 ASP A O   1 
ATOM   2908 C CB  . ASP A 1 342 ? 4.952   24.633 36.299  1.00 35.39 ? 342 ASP A CB  1 
ATOM   2909 C CG  . ASP A 1 342 ? 6.439   24.477 36.528  1.00 45.08 ? 342 ASP A CG  1 
ATOM   2910 O OD1 . ASP A 1 342 ? 6.880   24.566 37.691  1.00 50.38 ? 342 ASP A OD1 1 
ATOM   2911 O OD2 . ASP A 1 342 ? 7.171   24.270 35.536  1.00 53.08 ? 342 ASP A OD2 1 
ATOM   2912 N N   . PHE A 1 343 ? 4.415   22.546 39.148  1.00 22.63 ? 343 PHE A N   1 
ATOM   2913 C CA  . PHE A 1 343 ? 4.184   21.194 39.618  1.00 21.57 ? 343 PHE A CA  1 
ATOM   2914 C C   . PHE A 1 343 ? 2.965   21.208 40.536  1.00 20.92 ? 343 PHE A C   1 
ATOM   2915 O O   . PHE A 1 343 ? 2.338   22.249 40.754  1.00 19.93 ? 343 PHE A O   1 
ATOM   2916 C CB  . PHE A 1 343 ? 5.433   20.631 40.305  1.00 22.58 ? 343 PHE A CB  1 
ATOM   2917 C CG  . PHE A 1 343 ? 5.889   21.419 41.509  1.00 21.09 ? 343 PHE A CG  1 
ATOM   2918 C CD1 . PHE A 1 343 ? 5.410   21.122 42.777  1.00 19.93 ? 343 PHE A CD1 1 
ATOM   2919 C CD2 . PHE A 1 343 ? 6.829   22.432 41.372  1.00 22.10 ? 343 PHE A CD2 1 
ATOM   2920 C CE1 . PHE A 1 343 ? 5.838   21.846 43.892  1.00 22.43 ? 343 PHE A CE1 1 
ATOM   2921 C CE2 . PHE A 1 343 ? 7.268   23.156 42.481  1.00 23.93 ? 343 PHE A CE2 1 
ATOM   2922 C CZ  . PHE A 1 343 ? 6.778   22.858 43.736  1.00 25.57 ? 343 PHE A CZ  1 
ATOM   2923 N N   . GLN A 1 344 ? 2.603   20.031 41.056  1.00 20.08 ? 344 GLN A N   1 
ATOM   2924 C CA  . GLN A 1 344 ? 1.437   19.920 41.919  1.00 16.90 ? 344 GLN A CA  1 
ATOM   2925 C C   . GLN A 1 344 ? 1.903   20.026 43.358  1.00 17.45 ? 344 GLN A C   1 
ATOM   2926 O O   . GLN A 1 344 ? 2.552   19.092 43.862  1.00 16.70 ? 344 GLN A O   1 
ATOM   2927 C CB  . GLN A 1 344 ? 0.691   18.608 41.678  1.00 16.09 ? 344 GLN A CB  1 
ATOM   2928 C CG  . GLN A 1 344 ? 0.226   18.487 40.229  1.00 17.24 ? 344 GLN A CG  1 
ATOM   2929 C CD  . GLN A 1 344 ? -0.663  17.281 39.960  1.00 25.34 ? 344 GLN A CD  1 
ATOM   2930 O OE1 . GLN A 1 344 ? -1.807  17.431 39.536  1.00 24.82 ? 344 GLN A OE1 1 
ATOM   2931 N NE2 . GLN A 1 344 ? -0.133  16.080 40.184  1.00 22.24 ? 344 GLN A NE2 1 
ATOM   2932 N N   . PRO A 1 345 ? 1.635   21.130 44.035  1.00 14.35 ? 345 PRO A N   1 
ATOM   2933 C CA  . PRO A 1 345 ? 2.100   21.303 45.411  1.00 15.35 ? 345 PRO A CA  1 
ATOM   2934 C C   . PRO A 1 345 ? 1.263   20.500 46.395  1.00 12.71 ? 345 PRO A C   1 
ATOM   2935 O O   . PRO A 1 345 ? 0.071   20.256 46.178  1.00 15.33 ? 345 PRO A O   1 
ATOM   2936 C CB  . PRO A 1 345 ? 1.919   22.808 45.640  1.00 18.38 ? 345 PRO A CB  1 
ATOM   2937 C CG  . PRO A 1 345 ? 0.723   23.162 44.793  1.00 15.46 ? 345 PRO A CG  1 
ATOM   2938 C CD  . PRO A 1 345 ? 0.854   22.288 43.551  1.00 17.89 ? 345 PRO A CD  1 
ATOM   2939 N N   . VAL A 1 346 ? 1.906   20.079 47.485  1.00 12.41 ? 346 VAL A N   1 
ATOM   2940 C CA  . VAL A 1 346 ? 1.222   19.411 48.593  1.00 11.65 ? 346 VAL A CA  1 
ATOM   2941 C C   . VAL A 1 346 ? 1.176   20.387 49.756  1.00 10.98 ? 346 VAL A C   1 
ATOM   2942 O O   . VAL A 1 346 ? 2.220   20.812 50.266  1.00 14.53 ? 346 VAL A O   1 
ATOM   2943 C CB  . VAL A 1 346 ? 1.909   18.095 49.000  1.00 14.28 ? 346 VAL A CB  1 
ATOM   2944 C CG1 . VAL A 1 346 ? 1.097   17.361 50.089  1.00 14.89 ? 346 VAL A CG1 1 
ATOM   2945 C CG2 . VAL A 1 346 ? 2.092   17.204 47.792  1.00 17.69 ? 346 VAL A CG2 1 
ATOM   2946 N N   . VAL A 1 347 ? -0.033  20.720 50.197  1.00 11.65 ? 347 VAL A N   1 
ATOM   2947 C CA  . VAL A 1 347 ? -0.244  21.800 51.158  1.00 10.62 ? 347 VAL A CA  1 
ATOM   2948 C C   . VAL A 1 347 ? -0.814  21.178 52.428  1.00 10.03 ? 347 VAL A C   1 
ATOM   2949 O O   . VAL A 1 347 ? -1.997  20.802 52.462  1.00 11.67 ? 347 VAL A O   1 
ATOM   2950 C CB  . VAL A 1 347 ? -1.183  22.874 50.592  1.00 11.10 ? 347 VAL A CB  1 
ATOM   2951 C CG1 . VAL A 1 347 ? -1.309  24.025 51.584  1.00 11.91 ? 347 VAL A CG1 1 
ATOM   2952 C CG2 . VAL A 1 347 ? -0.661  23.389 49.258  1.00 16.43 ? 347 VAL A CG2 1 
ATOM   2953 N N   . PHE A 1 348 ? 0.021   21.060 53.466  1.00 12.23 ? 348 PHE A N   1 
ATOM   2954 C CA  . PHE A 1 348 ? -0.392  20.486 54.745  1.00 12.11 ? 348 PHE A CA  1 
ATOM   2955 C C   . PHE A 1 348 ? -0.900  21.593 55.662  1.00 12.63 ? 348 PHE A C   1 
ATOM   2956 O O   . PHE A 1 348 ? -0.191  22.574 55.926  1.00 15.25 ? 348 PHE A O   1 
ATOM   2957 C CB  . PHE A 1 348 ? 0.757   19.730 55.418  1.00 13.00 ? 348 PHE A CB  1 
ATOM   2958 C CG  . PHE A 1 348 ? 0.738   18.245 55.163  1.00 13.12 ? 348 PHE A CG  1 
ATOM   2959 C CD1 . PHE A 1 348 ? 0.982   17.760 53.891  1.00 12.17 ? 348 PHE A CD1 1 
ATOM   2960 C CD2 . PHE A 1 348 ? 0.480   17.335 56.193  1.00 12.75 ? 348 PHE A CD2 1 
ATOM   2961 C CE1 . PHE A 1 348 ? 0.961   16.392 53.637  1.00 16.42 ? 348 PHE A CE1 1 
ATOM   2962 C CE2 . PHE A 1 348 ? 0.461   15.972 55.948  1.00 15.09 ? 348 PHE A CE2 1 
ATOM   2963 C CZ  . PHE A 1 348 ? 0.691   15.496 54.667  1.00 13.03 ? 348 PHE A CZ  1 
ATOM   2964 N N   . VAL A 1 349 ? -2.134  21.437 56.131  1.00 10.62 ? 349 VAL A N   1 
ATOM   2965 C CA  . VAL A 1 349 ? -2.752  22.346 57.083  1.00 10.53 ? 349 VAL A CA  1 
ATOM   2966 C C   . VAL A 1 349 ? -2.910  21.537 58.359  1.00 11.04 ? 349 VAL A C   1 
ATOM   2967 O O   . VAL A 1 349 ? -3.739  20.624 58.414  1.00 11.03 ? 349 VAL A O   1 
ATOM   2968 C CB  . VAL A 1 349 ? -4.107  22.863 56.571  1.00 11.37 ? 349 VAL A CB  1 
ATOM   2969 C CG1 . VAL A 1 349 ? -4.753  23.779 57.589  1.00 16.60 ? 349 VAL A CG1 1 
ATOM   2970 C CG2 . VAL A 1 349 ? -3.929  23.587 55.233  1.00 15.24 ? 349 VAL A CG2 1 
ATOM   2971 N N   . VAL A 1 350 ? -2.075  21.809 59.351  1.00 10.25 ? 350 VAL A N   1 
ATOM   2972 C CA  . VAL A 1 350 ? -1.989  20.962 60.540  1.00 9.77  ? 350 VAL A CA  1 
ATOM   2973 C C   . VAL A 1 350 ? -2.120  21.856 61.754  1.00 10.01 ? 350 VAL A C   1 
ATOM   2974 O O   . VAL A 1 350 ? -1.329  22.786 61.915  1.00 9.71  ? 350 VAL A O   1 
ATOM   2975 C CB  . VAL A 1 350 ? -0.662  20.191 60.604  1.00 9.46  ? 350 VAL A CB  1 
ATOM   2976 C CG1 . VAL A 1 350 ? -0.674  19.209 61.782  1.00 13.06 ? 350 VAL A CG1 1 
ATOM   2977 C CG2 . VAL A 1 350 ? -0.373  19.461 59.273  1.00 8.96  ? 350 VAL A CG2 1 
ATOM   2978 N N   . LEU A 1 351 ? -3.092  21.567 62.617  1.00 10.29 ? 351 LEU A N   1 
ATOM   2979 C CA  . LEU A 1 351 ? -3.262  22.360 63.824  1.00 11.60 ? 351 LEU A CA  1 
ATOM   2980 C C   . LEU A 1 351 ? -4.132  21.561 64.778  1.00 10.01 ? 351 LEU A C   1 
ATOM   2981 O O   . LEU A 1 351 ? -4.677  20.514 64.416  1.00 10.25 ? 351 LEU A O   1 
ATOM   2982 C CB  . LEU A 1 351 ? -3.888  23.737 63.524  1.00 8.97  ? 351 LEU A CB  1 
ATOM   2983 C CG  . LEU A 1 351 ? -5.288  23.696 62.888  1.00 10.18 ? 351 LEU A CG  1 
ATOM   2984 C CD1 . LEU A 1 351 ? -6.116  24.938 63.271  1.00 11.57 ? 351 LEU A CD1 1 
ATOM   2985 C CD2 . LEU A 1 351 ? -5.223  23.584 61.358  1.00 16.11 ? 351 LEU A CD2 1 
ATOM   2986 N N   . ASN A 1 352 ? -4.319  22.093 65.973  1.00 11.27 ? 352 ASN A N   1 
ATOM   2987 C CA  . ASN A 1 352 ? -5.178  21.452 66.939  1.00 12.93 ? 352 ASN A CA  1 
ATOM   2988 C C   . ASN A 1 352 ? -6.612  21.475 66.374  1.00 11.77 ? 352 ASN A C   1 
ATOM   2989 O O   . ASN A 1 352 ? -7.045  22.447 65.865  1.00 11.18 ? 352 ASN A O   1 
ATOM   2990 C CB  . ASN A 1 352 ? -5.166  22.196 68.291  1.00 14.94 ? 352 ASN A CB  1 
ATOM   2991 C CG  . ASN A 1 352 ? -3.765  22.235 68.978  1.00 20.57 ? 352 ASN A CG  1 
ATOM   2992 O OD1 . ASN A 1 352 ? -3.015  21.424 68.847  1.00 16.25 ? 352 ASN A OD1 1 
ATOM   2993 N ND2 . ASN A 1 352 ? -3.499  23.315 69.729  1.00 28.36 ? 352 ASN A ND2 1 
ATOM   2994 N N   . GLY A 1 353 ? -7.324  20.368 66.560  1.00 10.48 ? 353 GLY A N   1 
ATOM   2995 C CA  . GLY A 1 353 ? -8.653  20.219 66.002  1.00 11.76 ? 353 GLY A CA  1 
ATOM   2996 C C   . GLY A 1 353 ? -9.802  20.612 66.894  1.00 10.63 ? 353 GLY A C   1 
ATOM   2997 O O   . GLY A 1 353 ? -10.960 20.510 66.464  1.00 11.56 ? 353 GLY A O   1 
ATOM   2998 N N   . GLU A 1 354 ? -9.543  21.077 68.132  1.00 9.83  ? 354 GLU A N   1 
ATOM   2999 C CA  . GLU A 1 354 ? -10.642 21.259 69.069  1.00 9.51  ? 354 GLU A CA  1 
ATOM   3000 C C   . GLU A 1 354 ? -10.609 22.569 69.840  1.00 12.15 ? 354 GLU A C   1 
ATOM   3001 O O   . GLU A 1 354 ? -11.557 22.849 70.573  1.00 12.36 ? 354 GLU A O   1 
ATOM   3002 C CB  . GLU A 1 354 ? -10.693 20.071 70.069  1.00 10.50 ? 354 GLU A CB  1 
ATOM   3003 C CG  . GLU A 1 354 ? -9.701  20.117 71.233  1.00 9.59  ? 354 GLU A CG  1 
ATOM   3004 C CD  . GLU A 1 354 ? -8.294  19.630 70.881  1.00 13.15 ? 354 GLU A CD  1 
ATOM   3005 O OE1 . GLU A 1 354 ? -7.842  18.627 71.471  1.00 11.03 ? 354 GLU A OE1 1 
ATOM   3006 O OE2 . GLU A 1 354 ? -7.641  20.231 70.005  1.00 12.80 ? 354 GLU A OE2 1 
ATOM   3007 N N   . ASN A 1 355 ? -9.578  23.396 69.678  1.00 8.86  ? 355 ASN A N   1 
ATOM   3008 C CA  . ASN A 1 355 ? -9.404  24.552 70.549  1.00 10.10 ? 355 ASN A CA  1 
ATOM   3009 C C   . ASN A 1 355 ? -9.828  25.867 69.918  1.00 11.33 ? 355 ASN A C   1 
ATOM   3010 O O   . ASN A 1 355 ? -10.129 26.817 70.654  1.00 11.71 ? 355 ASN A O   1 
ATOM   3011 C CB  . ASN A 1 355 ? -7.936  24.626 70.985  1.00 12.62 ? 355 ASN A CB  1 
ATOM   3012 C CG  . ASN A 1 355 ? -7.578  23.479 71.901  1.00 10.39 ? 355 ASN A CG  1 
ATOM   3013 O OD1 . ASN A 1 355 ? -8.421  23.065 72.704  1.00 11.35 ? 355 ASN A OD1 1 
ATOM   3014 N ND2 . ASN A 1 355 ? -6.356  22.955 71.790  1.00 12.66 ? 355 ASN A ND2 1 
ATOM   3015 N N   . CYS A 1 356 ? -9.851  25.958 68.593  1.00 8.95  ? 356 CYS A N   1 
ATOM   3016 C CA  . CYS A 1 356 ? -10.127 27.264 67.998  1.00 8.73  ? 356 CYS A CA  1 
ATOM   3017 C C   . CYS A 1 356 ? -11.618 27.568 67.864  1.00 8.66  ? 356 CYS A C   1 
ATOM   3018 O O   . CYS A 1 356 ? -12.012 28.745 67.896  1.00 9.50  ? 356 CYS A O   1 
ATOM   3019 C CB  . CYS A 1 356 ? -9.456  27.369 66.622  1.00 11.09 ? 356 CYS A CB  1 
ATOM   3020 S SG  . CYS A 1 356 ? -9.772  26.045 65.452  1.00 11.17 ? 356 CYS A SG  1 
ATOM   3021 N N   . TRP A 1 357 ? -12.462 26.537 67.781  1.00 10.51 ? 357 TRP A N   1 
ATOM   3022 C CA  . TRP A 1 357 ? -13.846 26.755 67.353  1.00 13.43 ? 357 TRP A CA  1 
ATOM   3023 C C   . TRP A 1 357 ? -14.673 27.525 68.373  1.00 12.22 ? 357 TRP A C   1 
ATOM   3024 O O   . TRP A 1 357 ? -15.586 28.253 67.980  1.00 9.95  ? 357 TRP A O   1 
ATOM   3025 C CB  . TRP A 1 357 ? -14.515 25.415 67.030  1.00 12.81 ? 357 TRP A CB  1 
ATOM   3026 C CG  . TRP A 1 357 ? -13.619 24.577 66.205  1.00 8.22  ? 357 TRP A CG  1 
ATOM   3027 C CD1 . TRP A 1 357 ? -13.106 23.342 66.520  1.00 11.68 ? 357 TRP A CD1 1 
ATOM   3028 C CD2 . TRP A 1 357 ? -13.107 24.911 64.916  1.00 11.64 ? 357 TRP A CD2 1 
ATOM   3029 N NE1 . TRP A 1 357 ? -12.278 22.904 65.502  1.00 10.96 ? 357 TRP A NE1 1 
ATOM   3030 C CE2 . TRP A 1 357 ? -12.270 23.846 64.505  1.00 11.40 ? 357 TRP A CE2 1 
ATOM   3031 C CE3 . TRP A 1 357 ? -13.252 26.027 64.073  1.00 15.49 ? 357 TRP A CE3 1 
ATOM   3032 C CZ2 . TRP A 1 357 ? -11.595 23.854 63.280  1.00 11.94 ? 357 TRP A CZ2 1 
ATOM   3033 C CZ3 . TRP A 1 357 ? -12.591 26.031 62.858  1.00 15.59 ? 357 TRP A CZ3 1 
ATOM   3034 C CH2 . TRP A 1 357 ? -11.762 24.953 62.475  1.00 11.58 ? 357 TRP A CH2 1 
ATOM   3035 N N   . GLU A 1 358 ? -14.371 27.390 69.668  1.00 9.75  ? 358 GLU A N   1 
ATOM   3036 C CA  . GLU A 1 358 ? -15.146 28.093 70.684  1.00 10.78 ? 358 GLU A CA  1 
ATOM   3037 C C   . GLU A 1 358 ? -15.053 29.604 70.543  1.00 10.92 ? 358 GLU A C   1 
ATOM   3038 O O   . GLU A 1 358 ? -15.890 30.319 71.114  1.00 11.21 ? 358 GLU A O   1 
ATOM   3039 C CB  . GLU A 1 358 ? -14.699 27.677 72.091  1.00 11.71 ? 358 GLU A CB  1 
ATOM   3040 C CG  . GLU A 1 358 ? -13.224 27.961 72.405  1.00 12.71 ? 358 GLU A CG  1 
ATOM   3041 C CD  . GLU A 1 358 ? -12.678 27.010 73.465  1.00 12.40 ? 358 GLU A CD  1 
ATOM   3042 O OE1 . GLU A 1 358 ? -12.359 27.474 74.581  1.00 18.68 ? 358 GLU A OE1 1 
ATOM   3043 O OE2 . GLU A 1 358 ? -12.588 25.796 73.179  1.00 14.98 ? 358 GLU A OE2 1 
ATOM   3044 N N   . TYR A 1 359 ? -14.061 30.105 69.804  1.00 12.79 ? 359 TYR A N   1 
ATOM   3045 C CA  . TYR A 1 359 ? -13.925 31.539 69.567  1.00 13.04 ? 359 TYR A CA  1 
ATOM   3046 C C   . TYR A 1 359 ? -14.550 31.983 68.249  1.00 14.46 ? 359 TYR A C   1 
ATOM   3047 O O   . TYR A 1 359 ? -14.621 33.192 67.997  1.00 15.13 ? 359 TYR A O   1 
ATOM   3048 C CB  . TYR A 1 359 ? -12.431 31.955 69.596  1.00 10.88 ? 359 TYR A CB  1 
ATOM   3049 C CG  . TYR A 1 359 ? -11.744 31.545 70.897  1.00 12.52 ? 359 TYR A CG  1 
ATOM   3050 C CD1 . TYR A 1 359 ? -11.880 32.313 72.049  1.00 21.53 ? 359 TYR A CD1 1 
ATOM   3051 C CD2 . TYR A 1 359 ? -10.971 30.384 70.969  1.00 19.95 ? 359 TYR A CD2 1 
ATOM   3052 C CE1 . TYR A 1 359 ? -11.272 31.935 73.235  1.00 20.76 ? 359 TYR A CE1 1 
ATOM   3053 C CE2 . TYR A 1 359 ? -10.361 30.002 72.159  1.00 20.77 ? 359 TYR A CE2 1 
ATOM   3054 C CZ  . TYR A 1 359 ? -10.523 30.775 73.284  1.00 27.63 ? 359 TYR A CZ  1 
ATOM   3055 O OH  . TYR A 1 359 ? -9.914  30.394 74.464  1.00 34.76 ? 359 TYR A OH  1 
ATOM   3056 N N   . TYR A 1 360 ? -14.994 31.047 67.404  1.00 12.69 ? 360 TYR A N   1 
ATOM   3057 C CA  . TYR A 1 360 ? -15.728 31.393 66.194  1.00 12.77 ? 360 TYR A CA  1 
ATOM   3058 C C   . TYR A 1 360 ? -17.212 31.544 66.517  1.00 11.51 ? 360 TYR A C   1 
ATOM   3059 O O   . TYR A 1 360 ? -17.738 30.883 67.413  1.00 12.43 ? 360 TYR A O   1 
ATOM   3060 C CB  . TYR A 1 360 ? -15.603 30.314 65.118  1.00 11.16 ? 360 TYR A CB  1 
ATOM   3061 C CG  . TYR A 1 360 ? -14.322 30.181 64.333  1.00 15.33 ? 360 TYR A CG  1 
ATOM   3062 C CD1 . TYR A 1 360 ? -13.142 29.757 64.937  1.00 13.56 ? 360 TYR A CD1 1 
ATOM   3063 C CD2 . TYR A 1 360 ? -14.322 30.360 62.946  1.00 11.37 ? 360 TYR A CD2 1 
ATOM   3064 C CE1 . TYR A 1 360 ? -11.977 29.596 64.191  1.00 10.61 ? 360 TYR A CE1 1 
ATOM   3065 C CE2 . TYR A 1 360 ? -13.182 30.168 62.197  1.00 14.62 ? 360 TYR A CE2 1 
ATOM   3066 C CZ  . TYR A 1 360 ? -12.015 29.794 62.815  1.00 9.77  ? 360 TYR A CZ  1 
ATOM   3067 O OH  . TYR A 1 360 ? -10.880 29.622 62.054  1.00 13.68 ? 360 TYR A OH  1 
ATOM   3068 N N   . GLU A 1 361 ? -17.890 32.384 65.744  1.00 17.86 ? 361 GLU A N   1 
ATOM   3069 C CA  . GLU A 1 361 ? -19.343 32.449 65.837  1.00 19.39 ? 361 GLU A CA  1 
ATOM   3070 C C   . GLU A 1 361 ? -19.944 31.072 65.582  1.00 15.32 ? 361 GLU A C   1 
ATOM   3071 O O   . GLU A 1 361 ? -19.507 30.338 64.687  1.00 15.33 ? 361 GLU A O   1 
ATOM   3072 C CB  . GLU A 1 361 ? -19.891 33.463 64.834  1.00 24.30 ? 361 GLU A CB  1 
ATOM   3073 C CG  . GLU A 1 361 ? -19.415 34.888 65.094  1.00 39.19 ? 361 GLU A CG  1 
ATOM   3074 C CD  . GLU A 1 361 ? -19.824 35.402 66.466  1.00 51.90 ? 361 GLU A CD  1 
ATOM   3075 O OE1 . GLU A 1 361 ? -20.987 35.181 66.870  1.00 54.15 ? 361 GLU A OE1 1 
ATOM   3076 O OE2 . GLU A 1 361 ? -18.982 36.027 67.145  1.00 54.84 ? 361 GLU A OE2 1 
ATOM   3077 N N   . GLU A 1 362 ? -20.931 30.715 66.405  1.00 16.69 ? 362 GLU A N   1 
ATOM   3078 C CA  . GLU A 1 362 ? -21.643 29.438 66.276  1.00 17.15 ? 362 GLU A CA  1 
ATOM   3079 C C   . GLU A 1 362 ? -20.668 28.266 66.197  1.00 16.70 ? 362 GLU A C   1 
ATOM   3080 O O   . GLU A 1 362 ? -20.815 27.360 65.373  1.00 13.48 ? 362 GLU A O   1 
ATOM   3081 C CB  . GLU A 1 362 ? -22.573 29.457 65.067  1.00 17.10 ? 362 GLU A CB  1 
ATOM   3082 C CG  . GLU A 1 362 ? -23.449 30.692 65.029  1.00 25.24 ? 362 GLU A CG  1 
ATOM   3083 C CD  . GLU A 1 362 ? -24.665 30.526 64.134  1.00 42.76 ? 362 GLU A CD  1 
ATOM   3084 O OE1 . GLU A 1 362 ? -25.461 31.483 64.045  1.00 47.86 ? 362 GLU A OE1 1 
ATOM   3085 O OE2 . GLU A 1 362 ? -24.830 29.441 63.532  1.00 44.44 ? 362 GLU A OE2 1 
ATOM   3086 N N   . ASN A 1 363 ? -19.630 28.318 67.032  1.00 11.94 ? 363 ASN A N   1 
ATOM   3087 C CA  . ASN A 1 363 ? -18.717 27.186 67.233  1.00 10.28 ? 363 ASN A CA  1 
ATOM   3088 C C   . ASN A 1 363 ? -17.996 26.777 65.943  1.00 12.96 ? 363 ASN A C   1 
ATOM   3089 O O   . ASN A 1 363 ? -17.699 25.597 65.738  1.00 13.82 ? 363 ASN A O   1 
ATOM   3090 C CB  . ASN A 1 363 ? -19.474 25.998 67.837  1.00 10.71 ? 363 ASN A CB  1 
ATOM   3091 C CG  . ASN A 1 363 ? -18.552 24.950 68.375  1.00 14.95 ? 363 ASN A CG  1 
ATOM   3092 O OD1 . ASN A 1 363 ? -17.470 25.267 68.866  1.00 15.21 ? 363 ASN A OD1 1 
ATOM   3093 N ND2 . ASN A 1 363 ? -18.953 23.684 68.255  1.00 10.47 ? 363 ASN A ND2 1 
ATOM   3094 N N   . GLY A 1 364 ? -17.745 27.746 65.057  1.00 13.36 ? 364 GLY A N   1 
ATOM   3095 C CA  . GLY A 1 364 ? -17.078 27.503 63.789  1.00 11.61 ? 364 GLY A CA  1 
ATOM   3096 C C   . GLY A 1 364 ? -17.878 26.747 62.754  1.00 12.16 ? 364 GLY A C   1 
ATOM   3097 O O   . GLY A 1 364 ? -17.332 26.399 61.705  1.00 12.49 ? 364 GLY A O   1 
ATOM   3098 N N   . ILE A 1 365 ? -19.158 26.488 63.003  1.00 14.03 ? 365 ILE A N   1 
ATOM   3099 C CA  . ILE A 1 365 ? -19.931 25.656 62.089  1.00 10.65 ? 365 ILE A CA  1 
ATOM   3100 C C   . ILE A 1 365 ? -20.163 26.398 60.773  1.00 13.60 ? 365 ILE A C   1 
ATOM   3101 O O   . ILE A 1 365 ? -19.924 25.813 59.701  1.00 13.44 ? 365 ILE A O   1 
ATOM   3102 C CB  . ILE A 1 365 ? -21.234 25.188 62.756  1.00 12.73 ? 365 ILE A CB  1 
ATOM   3103 C CG1 . ILE A 1 365 ? -20.886 24.181 63.857  1.00 14.67 ? 365 ILE A CG1 1 
ATOM   3104 C CG2 . ILE A 1 365 ? -22.165 24.550 61.730  1.00 15.06 ? 365 ILE A CG2 1 
ATOM   3105 C CD1 . ILE A 1 365 ? -21.952 24.043 64.892  1.00 19.71 ? 365 ILE A CD1 1 
ATOM   3106 N N   . PRO A 1 366 ? -20.596 27.668 60.777  1.00 13.76 ? 366 PRO A N   1 
ATOM   3107 C CA  . PRO A 1 366 ? -20.710 28.375 59.488  1.00 13.05 ? 366 PRO A CA  1 
ATOM   3108 C C   . PRO A 1 366 ? -19.400 28.409 58.708  1.00 11.87 ? 366 PRO A C   1 
ATOM   3109 O O   . PRO A 1 366 ? -19.409 28.240 57.479  1.00 14.55 ? 366 PRO A O   1 
ATOM   3110 C CB  . PRO A 1 366 ? -21.190 29.777 59.897  1.00 16.04 ? 366 PRO A CB  1 
ATOM   3111 C CG  . PRO A 1 366 ? -21.892 29.575 61.213  1.00 15.63 ? 366 PRO A CG  1 
ATOM   3112 C CD  . PRO A 1 366 ? -21.086 28.497 61.898  1.00 12.80 ? 366 PRO A CD  1 
ATOM   3113 N N   . PHE A 1 367 ? -18.271 28.608 59.392  1.00 11.33 ? 367 PHE A N   1 
ATOM   3114 C CA  . PHE A 1 367 ? -16.982 28.622 58.710  1.00 14.25 ? 367 PHE A CA  1 
ATOM   3115 C C   . PHE A 1 367 ? -16.676 27.272 58.073  1.00 13.74 ? 367 PHE A C   1 
ATOM   3116 O O   . PHE A 1 367 ? -16.395 27.194 56.873  1.00 13.61 ? 367 PHE A O   1 
ATOM   3117 C CB  . PHE A 1 367 ? -15.852 28.995 59.667  1.00 13.43 ? 367 PHE A CB  1 
ATOM   3118 C CG  . PHE A 1 367 ? -14.498 28.848 59.052  1.00 15.20 ? 367 PHE A CG  1 
ATOM   3119 C CD1 . PHE A 1 367 ? -14.068 29.754 58.095  1.00 17.44 ? 367 PHE A CD1 1 
ATOM   3120 C CD2 . PHE A 1 367 ? -13.673 27.772 59.380  1.00 14.01 ? 367 PHE A CD2 1 
ATOM   3121 C CE1 . PHE A 1 367 ? -12.840 29.637 57.496  1.00 15.14 ? 367 PHE A CE1 1 
ATOM   3122 C CE2 . PHE A 1 367 ? -12.426 27.643 58.783  1.00 11.37 ? 367 PHE A CE2 1 
ATOM   3123 C CZ  . PHE A 1 367 ? -12.006 28.577 57.834  1.00 11.91 ? 367 PHE A CZ  1 
ATOM   3124 N N   . LEU A 1 368 ? -16.735 26.196 58.861  1.00 12.61 ? 368 LEU A N   1 
ATOM   3125 C CA  . LEU A 1 368 ? -16.338 24.898 58.334  1.00 11.95 ? 368 LEU A CA  1 
ATOM   3126 C C   . LEU A 1 368 ? -17.319 24.398 57.282  1.00 13.67 ? 368 LEU A C   1 
ATOM   3127 O O   . LEU A 1 368 ? -16.905 23.823 56.268  1.00 13.69 ? 368 LEU A O   1 
ATOM   3128 C CB  . LEU A 1 368 ? -16.181 23.876 59.462  1.00 13.31 ? 368 LEU A CB  1 
ATOM   3129 C CG  . LEU A 1 368 ? -14.871 24.037 60.248  1.00 11.29 ? 368 LEU A CG  1 
ATOM   3130 C CD1 . LEU A 1 368 ? -14.794 23.018 61.365  1.00 12.54 ? 368 LEU A CD1 1 
ATOM   3131 C CD2 . LEU A 1 368 ? -13.622 23.920 59.366  1.00 9.62  ? 368 LEU A CD2 1 
ATOM   3132 N N   . GLU A 1 369 ? -18.620 24.617 57.482  1.00 13.52 ? 369 GLU A N   1 
ATOM   3133 C CA  . GLU A 1 369 ? -19.578 24.198 56.460  1.00 13.90 ? 369 GLU A CA  1 
ATOM   3134 C C   . GLU A 1 369 ? -19.350 24.941 55.149  1.00 15.01 ? 369 GLU A C   1 
ATOM   3135 O O   . GLU A 1 369 ? -19.471 24.349 54.076  1.00 17.85 ? 369 GLU A O   1 
ATOM   3136 C CB  . GLU A 1 369 ? -21.020 24.392 56.942  1.00 13.96 ? 369 GLU A CB  1 
ATOM   3137 C CG  . GLU A 1 369 ? -21.384 23.404 58.064  1.00 14.46 ? 369 GLU A CG  1 
ATOM   3138 C CD  . GLU A 1 369 ? -22.851 23.406 58.424  1.00 20.19 ? 369 GLU A CD  1 
ATOM   3139 O OE1 . GLU A 1 369 ? -23.581 24.336 58.024  1.00 21.94 ? 369 GLU A OE1 1 
ATOM   3140 O OE2 . GLU A 1 369 ? -23.287 22.461 59.117  1.00 21.00 ? 369 GLU A OE2 1 
ATOM   3141 N N   . LYS A 1 370 ? -19.031 26.241 55.209  1.00 14.29 ? 370 LYS A N   1 
ATOM   3142 C CA  . LYS A 1 370 ? -18.734 26.959 53.974  1.00 15.81 ? 370 LYS A CA  1 
ATOM   3143 C C   . LYS A 1 370 ? -17.421 26.494 53.376  1.00 16.45 ? 370 LYS A C   1 
ATOM   3144 O O   . LYS A 1 370 ? -17.319 26.310 52.154  1.00 16.35 ? 370 LYS A O   1 
ATOM   3145 C CB  . LYS A 1 370 ? -18.676 28.468 54.217  1.00 19.03 ? 370 LYS A CB  1 
ATOM   3146 C CG  . LYS A 1 370 ? -20.010 29.050 54.498  1.00 34.63 ? 370 LYS A CG  1 
ATOM   3147 C CD  . LYS A 1 370 ? -20.053 30.545 54.355  1.00 44.85 ? 370 LYS A CD  1 
ATOM   3148 C CE  . LYS A 1 370 ? -21.318 31.024 55.041  1.00 48.94 ? 370 LYS A CE  1 
ATOM   3149 N NZ  . LYS A 1 370 ? -22.556 30.611 54.329  1.00 46.06 ? 370 LYS A NZ  1 
ATOM   3150 N N   . LEU A 1 371 ? -16.403 26.318 54.223  1.00 12.65 ? 371 LEU A N   1 
ATOM   3151 C CA  . LEU A 1 371 ? -15.094 25.884 53.743  1.00 11.14 ? 371 LEU A CA  1 
ATOM   3152 C C   . LEU A 1 371 ? -15.193 24.539 53.048  1.00 16.24 ? 371 LEU A C   1 
ATOM   3153 O O   . LEU A 1 371 ? -14.756 24.379 51.901  1.00 14.46 ? 371 LEU A O   1 
ATOM   3154 C CB  . LEU A 1 371 ? -14.128 25.809 54.918  1.00 12.08 ? 371 LEU A CB  1 
ATOM   3155 C CG  . LEU A 1 371 ? -12.739 25.308 54.534  1.00 14.56 ? 371 LEU A CG  1 
ATOM   3156 C CD1 . LEU A 1 371 ? -12.109 26.236 53.509  1.00 16.86 ? 371 LEU A CD1 1 
ATOM   3157 C CD2 . LEU A 1 371 ? -11.882 25.207 55.782  1.00 13.73 ? 371 LEU A CD2 1 
ATOM   3158 N N   . TYR A 1 372 ? -15.799 23.562 53.723  1.00 13.19 ? 372 TYR A N   1 
ATOM   3159 C CA  . TYR A 1 372 ? -15.867 22.219 53.164  1.00 17.13 ? 372 TYR A CA  1 
ATOM   3160 C C   . TYR A 1 372 ? -16.775 22.172 51.937  1.00 19.97 ? 372 TYR A C   1 
ATOM   3161 O O   . TYR A 1 372 ? -16.467 21.481 50.956  1.00 18.80 ? 372 TYR A O   1 
ATOM   3162 C CB  . TYR A 1 372 ? -16.349 21.256 54.243  1.00 14.53 ? 372 TYR A CB  1 
ATOM   3163 C CG  . TYR A 1 372 ? -15.366 21.054 55.383  1.00 11.16 ? 372 TYR A CG  1 
ATOM   3164 C CD1 . TYR A 1 372 ? -14.020 21.409 55.262  1.00 10.67 ? 372 TYR A CD1 1 
ATOM   3165 C CD2 . TYR A 1 372 ? -15.785 20.488 56.583  1.00 13.12 ? 372 TYR A CD2 1 
ATOM   3166 C CE1 . TYR A 1 372 ? -13.107 21.186 56.318  1.00 11.03 ? 372 TYR A CE1 1 
ATOM   3167 C CE2 . TYR A 1 372 ? -14.909 20.276 57.614  1.00 11.88 ? 372 TYR A CE2 1 
ATOM   3168 C CZ  . TYR A 1 372 ? -13.565 20.613 57.487  1.00 7.61  ? 372 TYR A CZ  1 
ATOM   3169 O OH  . TYR A 1 372 ? -12.714 20.374 58.539  1.00 10.61 ? 372 TYR A OH  1 
ATOM   3170 N N   . SER A 1 373 ? -17.901 22.894 51.971  1.00 15.99 ? 373 SER A N   1 
ATOM   3171 C CA  . SER A 1 373 ? -18.781 22.945 50.806  1.00 16.68 ? 373 SER A CA  1 
ATOM   3172 C C   . SER A 1 373 ? -18.071 23.556 49.607  1.00 21.74 ? 373 SER A C   1 
ATOM   3173 O O   . SER A 1 373 ? -18.257 23.106 48.471  1.00 20.20 ? 373 SER A O   1 
ATOM   3174 C CB  . SER A 1 373 ? -20.046 23.741 51.134  1.00 21.20 ? 373 SER A CB  1 
ATOM   3175 O OG  . SER A 1 373 ? -20.871 23.858 49.988  1.00 31.21 ? 373 SER A OG  1 
ATOM   3176 N N   . THR A 1 374 ? -17.251 24.584 49.844  1.00 15.11 ? 374 THR A N   1 
ATOM   3177 C CA  . THR A 1 374 ? -16.529 25.229 48.758  1.00 20.22 ? 374 THR A CA  1 
ATOM   3178 C C   . THR A 1 374 ? -15.424 24.324 48.225  1.00 17.84 ? 374 THR A C   1 
ATOM   3179 O O   . THR A 1 374 ? -15.260 24.181 47.007  1.00 19.11 ? 374 THR A O   1 
ATOM   3180 C CB  . THR A 1 374 ? -15.942 26.558 49.244  1.00 18.70 ? 374 THR A CB  1 
ATOM   3181 O OG1 . THR A 1 374 ? -16.992 27.393 49.756  1.00 19.11 ? 374 THR A OG1 1 
ATOM   3182 C CG2 . THR A 1 374 ? -15.267 27.271 48.108  1.00 19.34 ? 374 THR A CG2 1 
ATOM   3183 N N   . LEU A 1 375 ? -14.666 23.700 49.130  1.00 18.55 ? 375 LEU A N   1 
ATOM   3184 C CA  . LEU A 1 375 ? -13.551 22.858 48.714  1.00 17.77 ? 375 LEU A CA  1 
ATOM   3185 C C   . LEU A 1 375 ? -14.023 21.691 47.865  1.00 22.42 ? 375 LEU A C   1 
ATOM   3186 O O   . LEU A 1 375 ? -13.390 21.355 46.859  1.00 21.98 ? 375 LEU A O   1 
ATOM   3187 C CB  . LEU A 1 375 ? -12.796 22.342 49.939  1.00 17.08 ? 375 LEU A CB  1 
ATOM   3188 C CG  . LEU A 1 375 ? -11.881 23.337 50.659  1.00 18.62 ? 375 LEU A CG  1 
ATOM   3189 C CD1 . LEU A 1 375 ? -11.331 22.704 51.914  1.00 17.88 ? 375 LEU A CD1 1 
ATOM   3190 C CD2 . LEU A 1 375 ? -10.738 23.796 49.758  1.00 21.05 ? 375 LEU A CD2 1 
ATOM   3191 N N   . GLU A 1 376 ? -15.139 21.064 48.245  1.00 23.51 ? 376 GLU A N   1 
ATOM   3192 C CA  . GLU A 1 376 ? -15.580 19.880 47.523  1.00 23.38 ? 376 GLU A CA  1 
ATOM   3193 C C   . GLU A 1 376 ? -16.007 20.208 46.106  1.00 24.27 ? 376 GLU A C   1 
ATOM   3194 O O   . GLU A 1 376 ? -16.108 19.300 45.276  1.00 32.17 ? 376 GLU A O   1 
ATOM   3195 C CB  . GLU A 1 376 ? -16.725 19.186 48.265  1.00 28.80 ? 376 GLU A CB  1 
ATOM   3196 C CG  . GLU A 1 376 ? -18.048 19.907 48.208  1.00 31.48 ? 376 GLU A CG  1 
ATOM   3197 C CD  . GLU A 1 376 ? -19.122 19.181 48.997  1.00 33.76 ? 376 GLU A CD  1 
ATOM   3198 O OE1 . GLU A 1 376 ? -20.242 19.719 49.124  1.00 28.67 ? 376 GLU A OE1 1 
ATOM   3199 O OE2 . GLU A 1 376 ? -18.847 18.066 49.487  1.00 34.16 ? 376 GLU A OE2 1 
ATOM   3200 N N   . LYS A 1 377 ? -16.255 21.479 45.812  1.00 20.53 ? 377 LYS A N   1 
ATOM   3201 C CA  . LYS A 1 377 ? -16.663 21.893 44.481  1.00 23.92 ? 377 LYS A CA  1 
ATOM   3202 C C   . LYS A 1 377 ? -15.535 22.498 43.658  1.00 26.17 ? 377 LYS A C   1 
ATOM   3203 O O   . LYS A 1 377 ? -15.749 22.760 42.476  1.00 25.28 ? 377 LYS A O   1 
ATOM   3204 C CB  . LYS A 1 377 ? -17.818 22.897 44.571  1.00 27.10 ? 377 LYS A CB  1 
ATOM   3205 C CG  . LYS A 1 377 ? -19.093 22.275 45.105  1.00 30.23 ? 377 LYS A CG  1 
ATOM   3206 C CD  . LYS A 1 377 ? -20.149 23.317 45.397  1.00 35.48 ? 377 LYS A CD  1 
ATOM   3207 C CE  . LYS A 1 377 ? -21.344 22.688 46.100  1.00 39.91 ? 377 LYS A CE  1 
ATOM   3208 N NZ  . LYS A 1 377 ? -21.008 22.320 47.514  1.00 33.38 ? 377 LYS A NZ  1 
ATOM   3209 N N   . GLU A 1 378 ? -14.355 22.735 44.233  1.00 26.18 ? 378 GLU A N   1 
ATOM   3210 C CA  . GLU A 1 378 ? -13.232 23.283 43.469  1.00 25.97 ? 378 GLU A CA  1 
ATOM   3211 C C   . GLU A 1 378 ? -12.535 22.149 42.720  1.00 25.85 ? 378 GLU A C   1 
ATOM   3212 O O   . GLU A 1 378 ? -11.897 21.292 43.336  1.00 30.16 ? 378 GLU A O   1 
ATOM   3213 C CB  . GLU A 1 378 ? -12.244 23.998 44.385  1.00 33.30 ? 378 GLU A CB  1 
ATOM   3214 C CG  . GLU A 1 378 ? -12.797 25.207 45.122  1.00 42.69 ? 378 GLU A CG  1 
ATOM   3215 C CD  . GLU A 1 378 ? -12.829 26.462 44.265  1.00 47.17 ? 378 GLU A CD  1 
ATOM   3216 O OE1 . GLU A 1 378 ? -12.453 26.393 43.075  1.00 44.75 ? 378 GLU A OE1 1 
ATOM   3217 O OE2 . GLU A 1 378 ? -13.230 27.525 44.786  1.00 46.77 ? 378 GLU A OE2 1 
ATOM   3218 N N   . GLU A 1 379 ? -12.619 22.159 41.389  1.00 26.21 ? 379 GLU A N   1 
ATOM   3219 C CA  . GLU A 1 379 ? -12.091 21.040 40.606  1.00 32.33 ? 379 GLU A CA  1 
ATOM   3220 C C   . GLU A 1 379 ? -10.576 20.921 40.729  1.00 26.86 ? 379 GLU A C   1 
ATOM   3221 O O   . GLU A 1 379 ? -10.014 19.837 40.535  1.00 33.65 ? 379 GLU A O   1 
ATOM   3222 C CB  . GLU A 1 379 ? -12.447 21.200 39.128  1.00 39.99 ? 379 GLU A CB  1 
ATOM   3223 C CG  . GLU A 1 379 ? -13.703 22.002 38.865  1.00 60.35 ? 379 GLU A CG  1 
ATOM   3224 C CD  . GLU A 1 379 ? -14.871 21.251 39.467  1.00 69.90 ? 379 GLU A CD  1 
ATOM   3225 O OE1 . GLU A 1 379 ? -15.618 21.866 40.240  1.00 68.07 ? 379 GLU A OE1 1 
ATOM   3226 O OE2 . GLU A 1 379 ? -15.016 20.032 39.169  1.00 73.84 ? 379 GLU A OE2 1 
ATOM   3227 N N   . TRP A 1 380 ? -9.900  22.033 40.951  1.00 21.46 ? 380 TRP A N   1 
ATOM   3228 C CA  . TRP A 1 380 ? -8.449  22.044 40.908  1.00 21.81 ? 380 TRP A CA  1 
ATOM   3229 C C   . TRP A 1 380 ? -7.825  21.765 42.267  1.00 19.56 ? 380 TRP A C   1 
ATOM   3230 O O   . TRP A 1 380 ? -6.600  21.689 42.357  1.00 22.13 ? 380 TRP A O   1 
ATOM   3231 C CB  . TRP A 1 380 ? -7.952  23.390 40.366  1.00 22.67 ? 380 TRP A CB  1 
ATOM   3232 C CG  . TRP A 1 380 ? -8.555  24.538 41.097  1.00 22.82 ? 380 TRP A CG  1 
ATOM   3233 C CD1 . TRP A 1 380 ? -9.769  25.116 40.866  1.00 28.39 ? 380 TRP A CD1 1 
ATOM   3234 C CD2 . TRP A 1 380 ? -7.977  25.247 42.200  1.00 22.39 ? 380 TRP A CD2 1 
ATOM   3235 N NE1 . TRP A 1 380 ? -9.980  26.143 41.754  1.00 27.20 ? 380 TRP A NE1 1 
ATOM   3236 C CE2 . TRP A 1 380 ? -8.890  26.250 42.577  1.00 20.97 ? 380 TRP A CE2 1 
ATOM   3237 C CE3 . TRP A 1 380 ? -6.767  25.140 42.895  1.00 20.59 ? 380 TRP A CE3 1 
ATOM   3238 C CZ2 . TRP A 1 380 ? -8.643  27.129 43.636  1.00 20.30 ? 380 TRP A CZ2 1 
ATOM   3239 C CZ3 . TRP A 1 380 ? -6.524  26.014 43.940  1.00 22.51 ? 380 TRP A CZ3 1 
ATOM   3240 C CH2 . TRP A 1 380 ? -7.458  26.991 44.302  1.00 24.92 ? 380 TRP A CH2 1 
ATOM   3241 N N   . ILE A 1 381 ? -8.641  21.615 43.318  1.00 14.97 ? 381 ILE A N   1 
ATOM   3242 C CA  . ILE A 1 381 ? -8.168  21.197 44.639  1.00 14.69 ? 381 ILE A CA  1 
ATOM   3243 C C   . ILE A 1 381 ? -8.565  19.741 44.835  1.00 16.04 ? 381 ILE A C   1 
ATOM   3244 O O   . ILE A 1 381 ? -9.723  19.371 44.607  1.00 18.86 ? 381 ILE A O   1 
ATOM   3245 C CB  . ILE A 1 381 ? -8.758  22.067 45.761  1.00 20.50 ? 381 ILE A CB  1 
ATOM   3246 C CG1 . ILE A 1 381 ? -8.326  23.528 45.600  1.00 19.75 ? 381 ILE A CG1 1 
ATOM   3247 C CG2 . ILE A 1 381 ? -8.348  21.512 47.139  1.00 18.40 ? 381 ILE A CG2 1 
ATOM   3248 C CD1 . ILE A 1 381 ? -8.967  24.466 46.606  1.00 22.55 ? 381 ILE A CD1 1 
ATOM   3249 N N   . GLU A 1 382 ? -7.615  18.914 45.254  1.00 15.24 ? 382 GLU A N   1 
ATOM   3250 C CA  . GLU A 1 382 ? -7.899  17.536 45.631  1.00 15.40 ? 382 GLU A CA  1 
ATOM   3251 C C   . GLU A 1 382 ? -7.425  17.360 47.067  1.00 16.07 ? 382 GLU A C   1 
ATOM   3252 O O   . GLU A 1 382 ? -6.218  17.411 47.333  1.00 15.19 ? 382 GLU A O   1 
ATOM   3253 C CB  . GLU A 1 382 ? -7.205  16.555 44.690  1.00 21.26 ? 382 GLU A CB  1 
ATOM   3254 C CG  . GLU A 1 382 ? -7.460  15.108 45.028  1.00 22.36 ? 382 GLU A CG  1 
ATOM   3255 C CD  . GLU A 1 382 ? -6.807  14.161 44.037  1.00 32.63 ? 382 GLU A CD  1 
ATOM   3256 O OE1 . GLU A 1 382 ? -6.612  14.568 42.869  1.00 37.09 ? 382 GLU A OE1 1 
ATOM   3257 O OE2 . GLU A 1 382 ? -6.496  13.016 44.427  1.00 38.99 ? 382 GLU A OE2 1 
ATOM   3258 N N   . THR A 1 383 ? -8.360  17.201 47.999  1.00 13.92 ? 383 THR A N   1 
ATOM   3259 C CA  . THR A 1 383 ? -7.956  16.893 49.363  1.00 10.49 ? 383 THR A CA  1 
ATOM   3260 C C   . THR A 1 383 ? -7.519  15.434 49.443  1.00 11.42 ? 383 THR A C   1 
ATOM   3261 O O   . THR A 1 383 ? -8.056  14.564 48.748  1.00 14.72 ? 383 THR A O   1 
ATOM   3262 C CB  . THR A 1 383 ? -9.078  17.152 50.369  1.00 14.08 ? 383 THR A CB  1 
ATOM   3263 O OG1 . THR A 1 383 ? -10.264 16.428 49.995  1.00 14.54 ? 383 THR A OG1 1 
ATOM   3264 C CG2 . THR A 1 383 ? -9.376  18.648 50.474  1.00 15.14 ? 383 THR A CG2 1 
ATOM   3265 N N   . LEU A 1 384 ? -6.528  15.173 50.300  1.00 12.87 ? 384 LEU A N   1 
ATOM   3266 C CA  . LEU A 1 384 ? -5.931  13.846 50.385  1.00 13.50 ? 384 LEU A CA  1 
ATOM   3267 C C   . LEU A 1 384 ? -5.966  13.318 51.810  1.00 13.90 ? 384 LEU A C   1 
ATOM   3268 O O   . LEU A 1 384 ? -5.863  14.079 52.776  1.00 12.31 ? 384 LEU A O   1 
ATOM   3269 C CB  . LEU A 1 384 ? -4.471  13.851 49.933  1.00 15.56 ? 384 LEU A CB  1 
ATOM   3270 C CG  . LEU A 1 384 ? -4.171  14.378 48.533  1.00 15.60 ? 384 LEU A CG  1 
ATOM   3271 C CD1 . LEU A 1 384 ? -2.667  14.353 48.350  1.00 16.10 ? 384 LEU A CD1 1 
ATOM   3272 C CD2 . LEU A 1 384 ? -4.887  13.546 47.473  1.00 13.98 ? 384 LEU A CD2 1 
ATOM   3273 N N   . THR A 1 385 ? -6.068  11.998 51.926  1.00 12.65 ? 385 THR A N   1 
ATOM   3274 C CA  . THR A 1 385 ? -5.736  11.348 53.188  1.00 13.78 ? 385 THR A CA  1 
ATOM   3275 C C   . THR A 1 385 ? -4.220  11.352 53.380  1.00 15.57 ? 385 THR A C   1 
ATOM   3276 O O   . THR A 1 385 ? -3.455  11.569 52.436  1.00 14.41 ? 385 THR A O   1 
ATOM   3277 C CB  . THR A 1 385 ? -6.228  9.898  53.216  1.00 13.16 ? 385 THR A CB  1 
ATOM   3278 O OG1 . THR A 1 385 ? -5.489  9.124  52.263  1.00 14.22 ? 385 THR A OG1 1 
ATOM   3279 C CG2 . THR A 1 385 ? -7.739  9.807  52.883  1.00 20.57 ? 385 THR A CG2 1 
ATOM   3280 N N   . LEU A 1 386 ? -3.781  11.091 54.617  1.00 12.04 ? 386 LEU A N   1 
ATOM   3281 C CA  . LEU A 1 386 ? -2.342  10.972 54.847  1.00 17.31 ? 386 LEU A CA  1 
ATOM   3282 C C   . LEU A 1 386 ? -1.749  9.863  53.989  1.00 16.42 ? 386 LEU A C   1 
ATOM   3283 O O   . LEU A 1 386 ? -0.631  9.991  53.469  1.00 15.42 ? 386 LEU A O   1 
ATOM   3284 C CB  . LEU A 1 386 ? -2.049  10.714 56.320  1.00 15.15 ? 386 LEU A CB  1 
ATOM   3285 C CG  . LEU A 1 386 ? -2.565  11.765 57.303  1.00 14.88 ? 386 LEU A CG  1 
ATOM   3286 C CD1 . LEU A 1 386 ? -2.176  11.351 58.724  1.00 14.95 ? 386 LEU A CD1 1 
ATOM   3287 C CD2 . LEU A 1 386 ? -2.060  13.178 56.967  1.00 14.83 ? 386 LEU A CD2 1 
ATOM   3288 N N   . GLU A 1 387 ? -2.486  8.761  53.821  1.00 14.59 ? 387 GLU A N   1 
ATOM   3289 C CA  . GLU A 1 387 ? -1.989  7.676  52.988  1.00 20.12 ? 387 GLU A CA  1 
ATOM   3290 C C   . GLU A 1 387 ? -1.792  8.127  51.548  1.00 16.02 ? 387 GLU A C   1 
ATOM   3291 O O   . GLU A 1 387 ? -0.786  7.785  50.915  1.00 17.89 ? 387 GLU A O   1 
ATOM   3292 C CB  . GLU A 1 387 ? -2.950  6.496  53.044  1.00 17.15 ? 387 GLU A CB  1 
ATOM   3293 C CG  . GLU A 1 387 ? -2.349  5.230  52.488  1.00 24.15 ? 387 GLU A CG  1 
ATOM   3294 C CD  . GLU A 1 387 ? -3.385  4.223  52.068  1.00 50.13 ? 387 GLU A CD  1 
ATOM   3295 O OE1 . GLU A 1 387 ? -3.283  3.710  50.933  1.00 57.33 ? 387 GLU A OE1 1 
ATOM   3296 O OE2 . GLU A 1 387 ? -4.298  3.942  52.873  1.00 56.93 ? 387 GLU A OE2 1 
ATOM   3297 N N   . GLU A 1 388 ? -2.756  8.875  51.006  1.00 15.25 ? 388 GLU A N   1 
ATOM   3298 C CA  . GLU A 1 388 ? -2.633  9.347  49.630  1.00 15.39 ? 388 GLU A CA  1 
ATOM   3299 C C   . GLU A 1 388 ? -1.483  10.333 49.491  1.00 17.22 ? 388 GLU A C   1 
ATOM   3300 O O   . GLU A 1 388 ? -0.763  10.319 48.487  1.00 20.23 ? 388 GLU A O   1 
ATOM   3301 C CB  . GLU A 1 388 ? -3.948  9.975  49.163  1.00 19.82 ? 388 GLU A CB  1 
ATOM   3302 C CG  . GLU A 1 388 ? -5.047  8.946  48.952  1.00 23.58 ? 388 GLU A CG  1 
ATOM   3303 C CD  . GLU A 1 388 ? -6.433  9.537  48.835  1.00 25.77 ? 388 GLU A CD  1 
ATOM   3304 O OE1 . GLU A 1 388 ? -6.665  10.663 49.315  1.00 17.33 ? 388 GLU A OE1 1 
ATOM   3305 O OE2 . GLU A 1 388 ? -7.308  8.849  48.259  1.00 31.04 ? 388 GLU A OE2 1 
ATOM   3306 N N   . ALA A 1 389 ? -1.299  11.188 50.490  1.00 15.75 ? 389 ALA A N   1 
ATOM   3307 C CA  . ALA A 1 389 ? -0.206  12.149 50.458  1.00 13.77 ? 389 ALA A CA  1 
ATOM   3308 C C   . ALA A 1 389 ? 1.139   11.444 50.528  1.00 21.07 ? 389 ALA A C   1 
ATOM   3309 O O   . ALA A 1 389 ? 2.098   11.858 49.867  1.00 22.64 ? 389 ALA A O   1 
ATOM   3310 C CB  . ALA A 1 389 ? -0.336  13.128 51.614  1.00 12.65 ? 389 ALA A CB  1 
ATOM   3311 N N   . MET A 1 390 ? 1.222   10.378 51.333  1.00 19.29 ? 390 MET A N   1 
ATOM   3312 C CA  . MET A 1 390 ? 2.468   9.632  51.464  1.00 19.04 ? 390 MET A CA  1 
ATOM   3313 C C   . MET A 1 390 ? 2.842   8.935  50.168  1.00 22.77 ? 390 MET A C   1 
ATOM   3314 O O   . MET A 1 390 ? 4.032   8.845  49.844  1.00 25.27 ? 390 MET A O   1 
ATOM   3315 C CB  . MET A 1 390 ? 2.358   8.615  52.607  1.00 20.02 ? 390 MET A CB  1 
ATOM   3316 C CG  . MET A 1 390 ? 3.662   7.901  52.929  1.00 39.16 ? 390 MET A CG  1 
ATOM   3317 S SD  . MET A 1 390 ? 3.498   6.693  54.269  1.00 42.05 ? 390 MET A SD  1 
ATOM   3318 C CE  . MET A 1 390 ? 2.511   5.410  53.494  1.00 37.60 ? 390 MET A CE  1 
ATOM   3319 N N   . ARG A 1 391 ? 1.852   8.472  49.400  1.00 19.34 ? 391 ARG A N   1 
ATOM   3320 C CA  . ARG A 1 391 ? 2.098   7.633  48.241  1.00 24.77 ? 391 ARG A CA  1 
ATOM   3321 C C   . ARG A 1 391 ? 1.944   8.343  46.902  1.00 27.04 ? 391 ARG A C   1 
ATOM   3322 O O   . ARG A 1 391 ? 2.282   7.752  45.874  1.00 25.62 ? 391 ARG A O   1 
ATOM   3323 C CB  . ARG A 1 391 ? 1.158   6.421  48.272  1.00 28.75 ? 391 ARG A CB  1 
ATOM   3324 C CG  . ARG A 1 391 ? 1.289   5.589  49.539  1.00 38.05 ? 391 ARG A CG  1 
ATOM   3325 C CD  . ARG A 1 391 ? 0.474   4.306  49.468  1.00 45.32 ? 391 ARG A CD  1 
ATOM   3326 N NE  . ARG A 1 391 ? 0.638   3.497  50.675  1.00 53.97 ? 391 ARG A NE  1 
ATOM   3327 C CZ  . ARG A 1 391 ? 1.708   2.752  50.939  1.00 60.15 ? 391 ARG A CZ  1 
ATOM   3328 N NH1 . ARG A 1 391 ? 2.719   2.704  50.080  1.00 62.68 ? 391 ARG A NH1 1 
ATOM   3329 N NH2 . ARG A 1 391 ? 1.769   2.051  52.064  1.00 60.57 ? 391 ARG A NH2 1 
ATOM   3330 N N   . LYS A 1 392 ? 1.449   9.577  46.882  1.00 24.18 ? 392 LYS A N   1 
ATOM   3331 C CA  . LYS A 1 392 ? 1.216   10.288 45.628  1.00 25.71 ? 392 LYS A CA  1 
ATOM   3332 C C   . LYS A 1 392 ? 2.479   10.331 44.779  1.00 23.75 ? 392 LYS A C   1 
ATOM   3333 O O   . LYS A 1 392 ? 3.546   10.728 45.252  1.00 24.70 ? 392 LYS A O   1 
ATOM   3334 C CB  . LYS A 1 392 ? 0.741   11.713 45.923  1.00 28.99 ? 392 LYS A CB  1 
ATOM   3335 C CG  . LYS A 1 392 ? -0.253  12.253 44.921  1.00 34.03 ? 392 LYS A CG  1 
ATOM   3336 C CD  . LYS A 1 392 ? -1.657  11.795 45.247  1.00 31.48 ? 392 LYS A CD  1 
ATOM   3337 C CE  . LYS A 1 392 ? -2.606  12.117 44.115  1.00 39.40 ? 392 LYS A CE  1 
ATOM   3338 N NZ  . LYS A 1 392 ? -3.601  11.033 43.894  1.00 49.77 ? 392 LYS A NZ  1 
ATOM   3339 N N   . GLU A 1 393 ? 2.355   9.921  43.519  1.00 22.07 ? 393 GLU A N   1 
ATOM   3340 C CA  . GLU A 1 393 ? 3.531   9.866  42.658  1.00 23.82 ? 393 GLU A CA  1 
ATOM   3341 C C   . GLU A 1 393 ? 3.809   11.186 41.951  1.00 26.42 ? 393 GLU A C   1 
ATOM   3342 O O   . GLU A 1 393 ? 4.977   11.535 41.748  1.00 32.59 ? 393 GLU A O   1 
ATOM   3343 C CB  . GLU A 1 393 ? 3.380   8.739  41.635  1.00 32.78 ? 393 GLU A CB  1 
ATOM   3344 C CG  . GLU A 1 393 ? 3.494   7.365  42.267  1.00 37.91 ? 393 GLU A CG  1 
ATOM   3345 C CD  . GLU A 1 393 ? 3.353   6.233  41.270  1.00 53.76 ? 393 GLU A CD  1 
ATOM   3346 O OE1 . GLU A 1 393 ? 3.549   6.468  40.057  1.00 56.64 ? 393 GLU A OE1 1 
ATOM   3347 O OE2 . GLU A 1 393 ? 3.046   5.105  41.707  1.00 56.69 ? 393 GLU A OE2 1 
ATOM   3348 N N   . ASP A 1 394 ? 2.775   11.945 41.607  1.00 24.52 ? 394 ASP A N   1 
ATOM   3349 C CA  . ASP A 1 394 ? 2.935   13.132 40.767  1.00 28.34 ? 394 ASP A CA  1 
ATOM   3350 C C   . ASP A 1 394 ? 3.183   14.392 41.597  1.00 28.10 ? 394 ASP A C   1 
ATOM   3351 O O   . ASP A 1 394 ? 2.540   15.423 41.401  1.00 22.91 ? 394 ASP A O   1 
ATOM   3352 C CB  . ASP A 1 394 ? 1.712   13.290 39.868  1.00 29.00 ? 394 ASP A CB  1 
ATOM   3353 C CG  . ASP A 1 394 ? 0.405   13.021 40.602  1.00 45.08 ? 394 ASP A CG  1 
ATOM   3354 O OD1 . ASP A 1 394 ? 0.453   12.519 41.747  1.00 50.45 ? 394 ASP A OD1 1 
ATOM   3355 O OD2 . ASP A 1 394 ? -0.673  13.318 40.032  1.00 39.72 ? 394 ASP A OD2 1 
ATOM   3356 N N   . VAL A 1 395 ? 4.137   14.314 42.528  1.00 22.30 ? 395 VAL A N   1 
ATOM   3357 C CA  . VAL A 1 395 ? 4.526   15.434 43.378  1.00 21.87 ? 395 VAL A CA  1 
ATOM   3358 C C   . VAL A 1 395 ? 6.044   15.576 43.330  1.00 24.79 ? 395 VAL A C   1 
ATOM   3359 O O   . VAL A 1 395 ? 6.756   14.699 42.849  1.00 25.52 ? 395 VAL A O   1 
ATOM   3360 C CB  . VAL A 1 395 ? 4.046   15.260 44.837  1.00 21.14 ? 395 VAL A CB  1 
ATOM   3361 C CG1 . VAL A 1 395 ? 2.521   15.176 44.896  1.00 20.80 ? 395 VAL A CG1 1 
ATOM   3362 C CG2 . VAL A 1 395 ? 4.690   14.025 45.471  1.00 22.10 ? 395 VAL A CG2 1 
ATOM   3363 N N   . LYS A 1 396 ? 6.536   16.707 43.824  1.00 20.89 ? 396 LYS A N   1 
ATOM   3364 C CA  . LYS A 1 396 ? 7.973   16.935 43.922  1.00 18.76 ? 396 LYS A CA  1 
ATOM   3365 C C   . LYS A 1 396 ? 8.490   16.437 45.270  1.00 18.58 ? 396 LYS A C   1 
ATOM   3366 O O   . LYS A 1 396 ? 7.801   16.531 46.284  1.00 17.49 ? 396 LYS A O   1 
ATOM   3367 C CB  . LYS A 1 396 ? 8.302   18.421 43.775  1.00 27.71 ? 396 LYS A CB  1 
ATOM   3368 C CG  . LYS A 1 396 ? 8.060   18.993 42.399  1.00 33.44 ? 396 LYS A CG  1 
ATOM   3369 C CD  . LYS A 1 396 ? 9.100   18.530 41.399  1.00 39.86 ? 396 LYS A CD  1 
ATOM   3370 C CE  . LYS A 1 396 ? 9.214   19.522 40.253  1.00 40.55 ? 396 LYS A CE  1 
ATOM   3371 N NZ  . LYS A 1 396 ? 10.051  18.994 39.158  1.00 38.59 ? 396 LYS A NZ  1 
ATOM   3372 N N   . THR A 1 397 ? 9.724   15.927 45.279  1.00 15.84 ? 397 THR A N   1 
ATOM   3373 C CA  . THR A 1 397 ? 10.314  15.391 46.502  1.00 16.38 ? 397 THR A CA  1 
ATOM   3374 C C   . THR A 1 397 ? 11.747  15.875 46.652  1.00 17.32 ? 397 THR A C   1 
ATOM   3375 O O   . THR A 1 397 ? 12.384  16.323 45.696  1.00 21.03 ? 397 THR A O   1 
ATOM   3376 C CB  . THR A 1 397 ? 10.305  13.852 46.545  1.00 21.25 ? 397 THR A CB  1 
ATOM   3377 O OG1 . THR A 1 397 ? 11.251  13.334 45.594  1.00 22.31 ? 397 THR A OG1 1 
ATOM   3378 C CG2 . THR A 1 397 ? 8.929   13.309 46.231  1.00 18.03 ? 397 THR A CG2 1 
ATOM   3379 N N   . GLU A 1 398 ? 12.250  15.764 47.879  1.00 14.88 ? 398 GLU A N   1 
ATOM   3380 C CA  . GLU A 1 398 ? 13.605  16.187 48.192  1.00 19.24 ? 398 GLU A CA  1 
ATOM   3381 C C   . GLU A 1 398 ? 14.126  15.389 49.378  1.00 16.81 ? 398 GLU A C   1 
ATOM   3382 O O   . GLU A 1 398 ? 13.377  15.082 50.307  1.00 17.60 ? 398 GLU A O   1 
ATOM   3383 C CB  . GLU A 1 398 ? 13.645  17.688 48.501  1.00 21.57 ? 398 GLU A CB  1 
ATOM   3384 C CG  . GLU A 1 398 ? 15.016  18.222 48.834  1.00 20.92 ? 398 GLU A CG  1 
ATOM   3385 C CD  . GLU A 1 398 ? 15.019  19.731 48.976  1.00 29.73 ? 398 GLU A CD  1 
ATOM   3386 O OE1 . GLU A 1 398 ? 14.065  20.371 48.487  1.00 29.75 ? 398 GLU A OE1 1 
ATOM   3387 O OE2 . GLU A 1 398 ? 15.970  20.272 49.578  1.00 28.41 ? 398 GLU A OE2 1 
ATOM   3388 N N   . VAL A 1 399 ? 15.418  15.069 49.353  1.00 16.39 ? 399 VAL A N   1 
ATOM   3389 C CA  . VAL A 1 399 ? 16.069  14.404 50.476  1.00 18.00 ? 399 VAL A CA  1 
ATOM   3390 C C   . VAL A 1 399 ? 16.717  15.459 51.357  1.00 21.79 ? 399 VAL A C   1 
ATOM   3391 O O   . VAL A 1 399 ? 17.403  16.360 50.857  1.00 24.49 ? 399 VAL A O   1 
ATOM   3392 C CB  . VAL A 1 399 ? 17.122  13.390 49.995  1.00 17.32 ? 399 VAL A CB  1 
ATOM   3393 C CG1 . VAL A 1 399 ? 17.880  12.828 51.194  1.00 23.04 ? 399 VAL A CG1 1 
ATOM   3394 C CG2 . VAL A 1 399 ? 16.449  12.288 49.194  1.00 21.14 ? 399 VAL A CG2 1 
ATOM   3395 N N   . ILE A 1 400 ? 16.525  15.336 52.667  1.00 18.95 ? 400 ILE A N   1 
ATOM   3396 C CA  . ILE A 1 400 ? 17.235  16.177 53.622  1.00 21.42 ? 400 ILE A CA  1 
ATOM   3397 C C   . ILE A 1 400 ? 17.989  15.293 54.609  1.00 18.65 ? 400 ILE A C   1 
ATOM   3398 O O   . ILE A 1 400 ? 17.582  14.166 54.910  1.00 19.36 ? 400 ILE A O   1 
ATOM   3399 C CB  . ILE A 1 400 ? 16.289  17.156 54.347  1.00 23.17 ? 400 ILE A CB  1 
ATOM   3400 C CG1 . ILE A 1 400 ? 15.086  16.424 54.940  1.00 29.11 ? 400 ILE A CG1 1 
ATOM   3401 C CG2 . ILE A 1 400 ? 15.836  18.246 53.383  1.00 24.04 ? 400 ILE A CG2 1 
ATOM   3402 C CD1 . ILE A 1 400 ? 14.144  17.337 55.700  1.00 36.71 ? 400 ILE A CD1 1 
ATOM   3403 N N   . GLU A 1 401 ? 19.130  15.804 55.087  1.00 18.32 ? 401 GLU A N   1 
ATOM   3404 C CA  . GLU A 1 401 ? 20.041  15.028 55.918  1.00 15.03 ? 401 GLU A CA  1 
ATOM   3405 C C   . GLU A 1 401 ? 20.030  15.429 57.384  1.00 15.52 ? 401 GLU A C   1 
ATOM   3406 O O   . GLU A 1 401 ? 20.492  14.647 58.220  1.00 18.23 ? 401 GLU A O   1 
ATOM   3407 C CB  . GLU A 1 401 ? 21.482  15.152 55.388  1.00 18.77 ? 401 GLU A CB  1 
ATOM   3408 C CG  . GLU A 1 401 ? 21.616  14.756 53.931  1.00 29.69 ? 401 GLU A CG  1 
ATOM   3409 C CD  . GLU A 1 401 ? 21.379  13.274 53.707  1.00 37.86 ? 401 GLU A CD  1 
ATOM   3410 O OE1 . GLU A 1 401 ? 20.981  12.899 52.583  1.00 38.92 ? 401 GLU A OE1 1 
ATOM   3411 O OE2 . GLU A 1 401 ? 21.603  12.484 54.650  1.00 37.79 ? 401 GLU A OE2 1 
ATOM   3412 N N   . SER A 1 402 ? 19.514  16.610 57.716  1.00 14.39 ? 402 SER A N   1 
ATOM   3413 C CA  . SER A 1 402 ? 19.650  17.140 59.067  1.00 13.82 ? 402 SER A CA  1 
ATOM   3414 C C   . SER A 1 402 ? 18.546  18.156 59.314  1.00 18.86 ? 402 SER A C   1 
ATOM   3415 O O   . SER A 1 402 ? 18.184  18.922 58.415  1.00 20.42 ? 402 SER A O   1 
ATOM   3416 C CB  . SER A 1 402 ? 21.039  17.790 59.248  1.00 16.57 ? 402 SER A CB  1 
ATOM   3417 O OG  . SER A 1 402 ? 21.291  18.131 60.603  1.00 22.29 ? 402 SER A OG  1 
ATOM   3418 N N   . VAL A 1 403 ? 18.019  18.169 60.534  1.00 17.07 ? 403 VAL A N   1 
ATOM   3419 C CA  . VAL A 1 403 ? 17.087  19.208 60.941  1.00 16.42 ? 403 VAL A CA  1 
ATOM   3420 C C   . VAL A 1 403 ? 17.634  19.870 62.188  1.00 16.98 ? 403 VAL A C   1 
ATOM   3421 O O   . VAL A 1 403 ? 18.392  19.269 62.953  1.00 18.55 ? 403 VAL A O   1 
ATOM   3422 C CB  . VAL A 1 403 ? 15.660  18.678 61.192  1.00 17.03 ? 403 VAL A CB  1 
ATOM   3423 C CG1 . VAL A 1 403 ? 15.111  18.067 59.927  1.00 15.63 ? 403 VAL A CG1 1 
ATOM   3424 C CG2 . VAL A 1 403 ? 15.637  17.657 62.360  1.00 17.06 ? 403 VAL A CG2 1 
ATOM   3425 N N   . LYS A 1 404 ? 17.260  21.130 62.369  1.00 15.87 ? 404 LYS A N   1 
ATOM   3426 C CA  . LYS A 1 404 ? 17.561  21.862 63.591  1.00 14.10 ? 404 LYS A CA  1 
ATOM   3427 C C   . LYS A 1 404 ? 16.397  21.640 64.548  1.00 15.70 ? 404 LYS A C   1 
ATOM   3428 O O   . LYS A 1 404 ? 15.249  21.945 64.210  1.00 14.48 ? 404 LYS A O   1 
ATOM   3429 C CB  . LYS A 1 404 ? 17.776  23.346 63.285  1.00 14.78 ? 404 LYS A CB  1 
ATOM   3430 C CG  . LYS A 1 404 ? 18.220  24.163 64.478  1.00 19.88 ? 404 LYS A CG  1 
ATOM   3431 C CD  . LYS A 1 404 ? 18.842  25.490 64.040  1.00 32.58 ? 404 LYS A CD  1 
ATOM   3432 C CE  . LYS A 1 404 ? 20.273  25.323 63.523  1.00 38.28 ? 404 LYS A CE  1 
ATOM   3433 N NZ  . LYS A 1 404 ? 21.248  26.035 64.398  1.00 48.04 ? 404 LYS A NZ  1 
ATOM   3434 N N   . ALA A 1 405 ? 16.679  21.057 65.715  1.00 14.73 ? 405 ALA A N   1 
ATOM   3435 C CA  . ALA A 1 405 ? 15.618  20.675 66.643  1.00 12.87 ? 405 ALA A CA  1 
ATOM   3436 C C   . ALA A 1 405 ? 14.735  21.864 67.026  1.00 10.16 ? 405 ALA A C   1 
ATOM   3437 O O   . ALA A 1 405 ? 15.216  22.974 67.241  1.00 15.97 ? 405 ALA A O   1 
ATOM   3438 C CB  . ALA A 1 405 ? 16.222  20.063 67.907  1.00 15.88 ? 405 ALA A CB  1 
ATOM   3439 N N   . GLY A 1 406 ? 13.436  21.626 67.130  1.00 11.71 ? 406 GLY A N   1 
ATOM   3440 C CA  . GLY A 1 406 ? 12.549  22.707 67.497  1.00 13.06 ? 406 GLY A CA  1 
ATOM   3441 C C   . GLY A 1 406 ? 11.127  22.215 67.647  1.00 10.80 ? 406 GLY A C   1 
ATOM   3442 O O   . GLY A 1 406 ? 10.863  21.015 67.679  1.00 10.52 ? 406 GLY A O   1 
ATOM   3443 N N   . THR A 1 407 ? 10.213  23.178 67.766  1.00 9.70  ? 407 THR A N   1 
ATOM   3444 C CA  . THR A 1 407 ? 8.779   22.921 67.850  1.00 11.03 ? 407 THR A CA  1 
ATOM   3445 C C   . THR A 1 407 ? 8.072   23.942 66.979  1.00 12.88 ? 407 THR A C   1 
ATOM   3446 O O   . THR A 1 407 ? 8.684   24.886 66.472  1.00 14.19 ? 407 THR A O   1 
ATOM   3447 C CB  . THR A 1 407 ? 8.229   23.050 69.278  1.00 11.55 ? 407 THR A CB  1 
ATOM   3448 O OG1 . THR A 1 407 ? 8.162   24.441 69.610  1.00 12.32 ? 407 THR A OG1 1 
ATOM   3449 C CG2 . THR A 1 407 ? 9.105   22.326 70.301  1.00 11.33 ? 407 THR A CG2 1 
ATOM   3450 N N   . TRP A 1 408 ? 6.755   23.812 66.871  1.00 10.61 ? 408 TRP A N   1 
ATOM   3451 C CA  . TRP A 1 408 ? 6.017   24.827 66.133  1.00 12.49 ? 408 TRP A CA  1 
ATOM   3452 C C   . TRP A 1 408 ? 5.822   26.126 66.913  1.00 14.51 ? 408 TRP A C   1 
ATOM   3453 O O   . TRP A 1 408 ? 5.233   27.068 66.370  1.00 14.83 ? 408 TRP A O   1 
ATOM   3454 C CB  . TRP A 1 408 ? 4.663   24.276 65.665  1.00 11.49 ? 408 TRP A CB  1 
ATOM   3455 C CG  . TRP A 1 408 ? 3.711   23.761 66.709  1.00 15.75 ? 408 TRP A CG  1 
ATOM   3456 C CD1 . TRP A 1 408 ? 3.833   23.823 68.075  1.00 15.37 ? 408 TRP A CD1 1 
ATOM   3457 C CD2 . TRP A 1 408 ? 2.463   23.112 66.443  1.00 14.87 ? 408 TRP A CD2 1 
ATOM   3458 N NE1 . TRP A 1 408 ? 2.725   23.240 68.667  1.00 11.63 ? 408 TRP A NE1 1 
ATOM   3459 C CE2 . TRP A 1 408 ? 1.875   22.797 67.689  1.00 11.42 ? 408 TRP A CE2 1 
ATOM   3460 C CE3 . TRP A 1 408 ? 1.798   22.745 65.266  1.00 11.68 ? 408 TRP A CE3 1 
ATOM   3461 C CZ2 . TRP A 1 408 ? 0.630   22.151 67.790  1.00 12.94 ? 408 TRP A CZ2 1 
ATOM   3462 C CZ3 . TRP A 1 408 ? 0.566   22.110 65.363  1.00 16.79 ? 408 TRP A CZ3 1 
ATOM   3463 C CH2 . TRP A 1 408 ? 0.001   21.812 66.621  1.00 15.46 ? 408 TRP A CH2 1 
ATOM   3464 N N   . PHE A 1 409 ? 6.295   26.222 68.158  1.00 12.24 ? 409 PHE A N   1 
ATOM   3465 C CA  . PHE A 1 409 ? 6.283   27.504 68.866  1.00 17.15 ? 409 PHE A CA  1 
ATOM   3466 C C   . PHE A 1 409 ? 7.638   28.165 68.629  1.00 17.57 ? 409 PHE A C   1 
ATOM   3467 O O   . PHE A 1 409 ? 8.623   27.838 69.292  1.00 15.27 ? 409 PHE A O   1 
ATOM   3468 C CB  . PHE A 1 409 ? 6.000   27.328 70.354  1.00 17.24 ? 409 PHE A CB  1 
ATOM   3469 C CG  . PHE A 1 409 ? 5.530   28.595 71.024  1.00 35.90 ? 409 PHE A CG  1 
ATOM   3470 C CD1 . PHE A 1 409 ? 6.433   29.566 71.409  1.00 42.14 ? 409 PHE A CD1 1 
ATOM   3471 C CD2 . PHE A 1 409 ? 4.183   28.822 71.241  1.00 43.26 ? 409 PHE A CD2 1 
ATOM   3472 C CE1 . PHE A 1 409 ? 6.003   30.730 72.016  1.00 40.78 ? 409 PHE A CE1 1 
ATOM   3473 C CE2 . PHE A 1 409 ? 3.746   29.986 71.848  1.00 47.50 ? 409 PHE A CE2 1 
ATOM   3474 C CZ  . PHE A 1 409 ? 4.658   30.939 72.234  1.00 43.73 ? 409 PHE A CZ  1 
ATOM   3475 N N   . ASP A 1 410 ? 7.692   29.064 67.643  1.00 19.10 ? 410 ASP A N   1 
ATOM   3476 C CA  . ASP A 1 410 ? 8.886   29.844 67.312  1.00 20.60 ? 410 ASP A CA  1 
ATOM   3477 C C   . ASP A 1 410 ? 10.092  28.976 66.959  1.00 20.95 ? 410 ASP A C   1 
ATOM   3478 O O   . ASP A 1 410 ? 11.240  29.447 67.026  1.00 23.12 ? 410 ASP A O   1 
ATOM   3479 C CB  . ASP A 1 410 ? 9.262   30.798 68.449  1.00 20.83 ? 410 ASP A CB  1 
ATOM   3480 C CG  . ASP A 1 410 ? 8.142   31.762 68.797  1.00 34.27 ? 410 ASP A CG  1 
ATOM   3481 O OD1 . ASP A 1 410 ? 7.383   32.152 67.884  1.00 35.13 ? 410 ASP A OD1 1 
ATOM   3482 O OD2 . ASP A 1 410 ? 8.038   32.147 69.980  1.00 38.50 ? 410 ASP A OD2 1 
ATOM   3483 N N   . GLY A 1 411 ? 9.861   27.727 66.567  1.00 16.19 ? 411 GLY A N   1 
ATOM   3484 C CA  . GLY A 1 411 ? 10.950  26.814 66.290  1.00 18.12 ? 411 GLY A CA  1 
ATOM   3485 C C   . GLY A 1 411 ? 11.810  26.429 67.477  1.00 18.95 ? 411 GLY A C   1 
ATOM   3486 O O   . GLY A 1 411 ? 12.916  25.922 67.270  1.00 16.94 ? 411 GLY A O   1 
ATOM   3487 N N   . ASN A 1 412 ? 11.360  26.660 68.713  1.00 12.18 ? 412 ASN A N   1 
ATOM   3488 C CA  . ASN A 1 412 ? 12.227  26.413 69.860  1.00 13.76 ? 412 ASN A CA  1 
ATOM   3489 C C   . ASN A 1 412 ? 11.417  25.798 71.002  1.00 15.08 ? 412 ASN A C   1 
ATOM   3490 O O   . ASN A 1 412 ? 10.222  25.511 70.866  1.00 14.37 ? 412 ASN A O   1 
ATOM   3491 C CB  . ASN A 1 412 ? 12.981  27.695 70.280  1.00 15.42 ? 412 ASN A CB  1 
ATOM   3492 C CG  . ASN A 1 412 ? 12.063  28.802 70.809  1.00 16.36 ? 412 ASN A CG  1 
ATOM   3493 O OD1 . ASN A 1 412 ? 11.163  28.558 71.624  1.00 16.56 ? 412 ASN A OD1 1 
ATOM   3494 N ND2 . ASN A 1 412 ? 12.311  30.038 70.362  1.00 20.59 ? 412 ASN A ND2 1 
ATOM   3495 N N   . PHE A 1 413 ? 12.089  25.571 72.136  1.00 13.13 ? 413 PHE A N   1 
ATOM   3496 C CA  . PHE A 1 413 ? 11.512  24.841 73.259  1.00 11.21 ? 413 PHE A CA  1 
ATOM   3497 C C   . PHE A 1 413 ? 11.139  25.725 74.446  1.00 13.91 ? 413 PHE A C   1 
ATOM   3498 O O   . PHE A 1 413 ? 10.803  25.189 75.517  1.00 13.11 ? 413 PHE A O   1 
ATOM   3499 C CB  . PHE A 1 413 ? 12.478  23.749 73.712  1.00 10.00 ? 413 PHE A CB  1 
ATOM   3500 C CG  . PHE A 1 413 ? 12.633  22.653 72.698  1.00 10.79 ? 413 PHE A CG  1 
ATOM   3501 C CD1 . PHE A 1 413 ? 11.716  21.611 72.637  1.00 12.52 ? 413 PHE A CD1 1 
ATOM   3502 C CD2 . PHE A 1 413 ? 13.675  22.698 71.771  1.00 12.84 ? 413 PHE A CD2 1 
ATOM   3503 C CE1 . PHE A 1 413 ? 11.848  20.609 71.687  1.00 11.59 ? 413 PHE A CE1 1 
ATOM   3504 C CE2 . PHE A 1 413 ? 13.809  21.701 70.812  1.00 14.73 ? 413 PHE A CE2 1 
ATOM   3505 C CZ  . PHE A 1 413 ? 12.900  20.657 70.774  1.00 10.89 ? 413 PHE A CZ  1 
ATOM   3506 N N   . LEU A 1 414 ? 11.137  27.054 74.274  1.00 12.43 ? 414 LEU A N   1 
ATOM   3507 C CA  . LEU A 1 414 ? 10.994  27.964 75.414  1.00 13.77 ? 414 LEU A CA  1 
ATOM   3508 C C   . LEU A 1 414 ? 9.616   27.923 76.077  1.00 13.78 ? 414 LEU A C   1 
ATOM   3509 O O   . LEU A 1 414 ? 9.469   28.430 77.201  1.00 15.64 ? 414 LEU A O   1 
ATOM   3510 C CB  . LEU A 1 414 ? 11.297  29.392 74.974  1.00 15.40 ? 414 LEU A CB  1 
ATOM   3511 C CG  . LEU A 1 414 ? 12.741  29.614 74.530  1.00 18.80 ? 414 LEU A CG  1 
ATOM   3512 C CD1 . LEU A 1 414 ? 12.947  31.060 74.107  1.00 20.72 ? 414 LEU A CD1 1 
ATOM   3513 C CD2 . LEU A 1 414 ? 13.680  29.238 75.656  1.00 22.47 ? 414 LEU A CD2 1 
ATOM   3514 N N   . LYS A 1 415 ? 8.603   27.359 75.426  1.00 12.66 ? 415 LYS A N   1 
ATOM   3515 C CA  . LYS A 1 415 ? 7.318   27.246 76.110  1.00 14.38 ? 415 LYS A CA  1 
ATOM   3516 C C   . LYS A 1 415 ? 7.308   26.145 77.155  1.00 15.87 ? 415 LYS A C   1 
ATOM   3517 O O   . LYS A 1 415 ? 6.352   26.072 77.937  1.00 16.86 ? 415 LYS A O   1 
ATOM   3518 C CB  . LYS A 1 415 ? 6.186   27.004 75.099  1.00 16.67 ? 415 LYS A CB  1 
ATOM   3519 C CG  . LYS A 1 415 ? 5.290   28.228 74.865  1.00 38.47 ? 415 LYS A CG  1 
ATOM   3520 C CD  . LYS A 1 415 ? 4.270   28.442 75.995  1.00 46.95 ? 415 LYS A CD  1 
ATOM   3521 C CE  . LYS A 1 415 ? 3.512   29.762 75.832  1.00 56.93 ? 415 LYS A CE  1 
ATOM   3522 N NZ  . LYS A 1 415 ? 3.127   30.361 77.140  1.00 60.44 ? 415 LYS A NZ  1 
ATOM   3523 N N   . TRP A 1 416 ? 8.339   25.292 77.193  1.00 11.71 ? 416 TRP A N   1 
ATOM   3524 C CA  . TRP A 1 416 ? 8.350   24.157 78.109  1.00 10.32 ? 416 TRP A CA  1 
ATOM   3525 C C   . TRP A 1 416 ? 9.584   24.074 78.982  1.00 13.87 ? 416 TRP A C   1 
ATOM   3526 O O   . TRP A 1 416 ? 9.614   23.233 79.891  1.00 13.14 ? 416 TRP A O   1 
ATOM   3527 C CB  . TRP A 1 416 ? 8.223   22.834 77.332  1.00 13.78 ? 416 TRP A CB  1 
ATOM   3528 C CG  . TRP A 1 416 ? 7.026   22.840 76.456  1.00 10.43 ? 416 TRP A CG  1 
ATOM   3529 C CD1 . TRP A 1 416 ? 5.773   22.413 76.779  1.00 10.56 ? 416 TRP A CD1 1 
ATOM   3530 C CD2 . TRP A 1 416 ? 6.951   23.312 75.104  1.00 14.30 ? 416 TRP A CD2 1 
ATOM   3531 N NE1 . TRP A 1 416 ? 4.915   22.598 75.724  1.00 12.20 ? 416 TRP A NE1 1 
ATOM   3532 C CE2 . TRP A 1 416 ? 5.608   23.152 74.681  1.00 13.28 ? 416 TRP A CE2 1 
ATOM   3533 C CE3 . TRP A 1 416 ? 7.874   23.874 74.219  1.00 13.55 ? 416 TRP A CE3 1 
ATOM   3534 C CZ2 . TRP A 1 416 ? 5.174   23.515 73.408  1.00 12.99 ? 416 TRP A CZ2 1 
ATOM   3535 C CZ3 . TRP A 1 416 ? 7.434   24.230 72.940  1.00 12.44 ? 416 TRP A CZ3 1 
ATOM   3536 C CH2 . TRP A 1 416 ? 6.098   24.054 72.556  1.00 15.07 ? 416 TRP A CH2 1 
ATOM   3537 N N   . ILE A 1 417 ? 10.594  24.906 78.747  1.00 13.33 ? 417 ILE A N   1 
ATOM   3538 C CA  . ILE A 1 417 ? 11.838  24.839 79.503  1.00 14.00 ? 417 ILE A CA  1 
ATOM   3539 C C   . ILE A 1 417 ? 12.520  26.193 79.376  1.00 14.47 ? 417 ILE A C   1 
ATOM   3540 O O   . ILE A 1 417 ? 12.319  26.921 78.396  1.00 15.04 ? 417 ILE A O   1 
ATOM   3541 C CB  . ILE A 1 417 ? 12.738  23.686 78.988  1.00 13.96 ? 417 ILE A CB  1 
ATOM   3542 C CG1 . ILE A 1 417 ? 13.849  23.362 79.990  1.00 12.99 ? 417 ILE A CG1 1 
ATOM   3543 C CG2 . ILE A 1 417 ? 13.348  24.059 77.660  1.00 12.17 ? 417 ILE A CG2 1 
ATOM   3544 C CD1 . ILE A 1 417 ? 14.419  21.967 79.784  1.00 13.75 ? 417 ILE A CD1 1 
ATOM   3545 N N   . GLY A 1 418 ? 13.302  26.557 80.383  1.00 15.87 ? 418 GLY A N   1 
ATOM   3546 C CA  . GLY A 1 418 ? 14.166  27.721 80.293  1.00 16.86 ? 418 GLY A CA  1 
ATOM   3547 C C   . GLY A 1 418 ? 13.863  28.854 81.243  1.00 24.50 ? 418 GLY A C   1 
ATOM   3548 O O   . GLY A 1 418 ? 14.685  29.773 81.356  1.00 37.18 ? 418 GLY A O   1 
ATOM   3549 N N   . ASN A 1 419 ? 12.725  28.865 81.917  1.00 18.72 ? 419 ASN A N   1 
ATOM   3550 C CA  . ASN A 1 419 ? 12.571  29.838 82.983  1.00 19.86 ? 419 ASN A CA  1 
ATOM   3551 C C   . ASN A 1 419 ? 12.542  29.110 84.322  1.00 20.37 ? 419 ASN A C   1 
ATOM   3552 O O   . ASN A 1 419 ? 12.526  27.878 84.385  1.00 21.85 ? 419 ASN A O   1 
ATOM   3553 C CB  . ASN A 1 419 ? 11.350  30.751 82.757  1.00 22.15 ? 419 ASN A CB  1 
ATOM   3554 C CG  . ASN A 1 419 ? 10.015  30.054 82.918  1.00 28.58 ? 419 ASN A CG  1 
ATOM   3555 O OD1 . ASN A 1 419 ? 9.915   28.971 83.479  1.00 28.62 ? 419 ASN A OD1 1 
ATOM   3556 N ND2 . ASN A 1 419 ? 8.955   30.724 82.455  1.00 25.16 ? 419 ASN A ND2 1 
ATOM   3557 N N   . LYS A 1 420 ? 12.599  29.898 85.397  1.00 18.81 ? 420 LYS A N   1 
ATOM   3558 C CA  . LYS A 1 420 ? 12.775  29.330 86.728  1.00 22.04 ? 420 LYS A CA  1 
ATOM   3559 C C   . LYS A 1 420 ? 11.700  28.294 87.031  1.00 24.41 ? 420 LYS A C   1 
ATOM   3560 O O   . LYS A 1 420 ? 11.998  27.198 87.518  1.00 22.92 ? 420 LYS A O   1 
ATOM   3561 C CB  . LYS A 1 420 ? 12.759  30.448 87.771  1.00 27.20 ? 420 LYS A CB  1 
ATOM   3562 C CG  . LYS A 1 420 ? 13.055  29.982 89.191  1.00 38.27 ? 420 LYS A CG  1 
ATOM   3563 C CD  . LYS A 1 420 ? 13.304  31.167 90.130  1.00 45.35 ? 420 LYS A CD  1 
ATOM   3564 C CE  . LYS A 1 420 ? 13.947  30.716 91.437  1.00 48.21 ? 420 LYS A CE  1 
ATOM   3565 N NZ  . LYS A 1 420 ? 13.672  31.651 92.569  1.00 50.64 ? 420 LYS A NZ  1 
ATOM   3566 N N   . GLU A 1 421 ? 10.442  28.621 86.724  1.00 21.41 ? 421 GLU A N   1 
ATOM   3567 C CA  . GLU A 1 421 ? 9.330   27.764 87.119  1.00 19.49 ? 421 GLU A CA  1 
ATOM   3568 C C   . GLU A 1 421 ? 9.255   26.506 86.259  1.00 15.98 ? 421 GLU A C   1 
ATOM   3569 O O   . GLU A 1 421 ? 9.027   25.405 86.776  1.00 17.94 ? 421 GLU A O   1 
ATOM   3570 C CB  . GLU A 1 421 ? 8.018   28.545 87.040  1.00 22.42 ? 421 GLU A CB  1 
ATOM   3571 C CG  . GLU A 1 421 ? 7.901   29.695 88.039  1.00 32.25 ? 421 GLU A CG  1 
ATOM   3572 C CD  . GLU A 1 421 ? 8.532   30.993 87.541  1.00 44.96 ? 421 GLU A CD  1 
ATOM   3573 O OE1 . GLU A 1 421 ? 8.614   31.953 88.338  1.00 51.17 ? 421 GLU A OE1 1 
ATOM   3574 O OE2 . GLU A 1 421 ? 8.944   31.063 86.362  1.00 43.12 ? 421 GLU A OE2 1 
ATOM   3575 N N   . LYS A 1 422 ? 9.395   26.641 84.941  1.00 16.83 ? 422 LYS A N   1 
ATOM   3576 C CA  . LYS A 1 422 ? 9.378   25.440 84.108  1.00 12.95 ? 422 LYS A CA  1 
ATOM   3577 C C   . LYS A 1 422 ? 10.567  24.540 84.421  1.00 15.34 ? 422 LYS A C   1 
ATOM   3578 O O   . LYS A 1 422 ? 10.428  23.312 84.449  1.00 15.20 ? 422 LYS A O   1 
ATOM   3579 C CB  . LYS A 1 422 ? 9.366   25.806 82.624  1.00 14.93 ? 422 LYS A CB  1 
ATOM   3580 C CG  . LYS A 1 422 ? 8.083   26.499 82.188  1.00 13.31 ? 422 LYS A CG  1 
ATOM   3581 C CD  . LYS A 1 422 ? 8.188   26.924 80.748  1.00 13.65 ? 422 LYS A CD  1 
ATOM   3582 C CE  . LYS A 1 422 ? 7.164   27.985 80.399  1.00 16.97 ? 422 LYS A CE  1 
ATOM   3583 N NZ  . LYS A 1 422 ? 5.787   27.416 80.355  1.00 17.05 ? 422 LYS A NZ  1 
ATOM   3584 N N   . ASN A 1 423 ? 11.744  25.133 84.653  1.00 12.41 ? 423 ASN A N   1 
ATOM   3585 C CA  . ASN A 1 423 ? 12.902  24.330 85.026  1.00 13.69 ? 423 ASN A CA  1 
ATOM   3586 C C   . ASN A 1 423 ? 12.682  23.611 86.346  1.00 17.62 ? 423 ASN A C   1 
ATOM   3587 O O   . ASN A 1 423 ? 13.180  22.496 86.537  1.00 16.45 ? 423 ASN A O   1 
ATOM   3588 C CB  . ASN A 1 423 ? 14.149  25.202 85.118  1.00 13.07 ? 423 ASN A CB  1 
ATOM   3589 C CG  . ASN A 1 423 ? 14.684  25.600 83.760  1.00 16.42 ? 423 ASN A CG  1 
ATOM   3590 O OD1 . ASN A 1 423 ? 14.167  25.181 82.717  1.00 14.54 ? 423 ASN A OD1 1 
ATOM   3591 N ND2 . ASN A 1 423 ? 15.723  26.418 83.769  1.00 17.27 ? 423 ASN A ND2 1 
ATOM   3592 N N   . GLU A 1 424 ? 11.933  24.222 87.263  1.00 18.37 ? 424 GLU A N   1 
ATOM   3593 C CA  . GLU A 1 424 ? 11.627  23.532 88.508  1.00 17.62 ? 424 GLU A CA  1 
ATOM   3594 C C   . GLU A 1 424 ? 10.882  22.228 88.239  1.00 15.47 ? 424 GLU A C   1 
ATOM   3595 O O   . GLU A 1 424 ? 11.182  21.200 88.858  1.00 15.26 ? 424 GLU A O   1 
ATOM   3596 C CB  . GLU A 1 424 ? 10.823  24.443 89.435  1.00 16.29 ? 424 GLU A CB  1 
ATOM   3597 C CG  . GLU A 1 424 ? 10.402  23.783 90.762  1.00 26.35 ? 424 GLU A CG  1 
ATOM   3598 C CD  . GLU A 1 424 ? 11.584  23.310 91.620  1.00 36.22 ? 424 GLU A CD  1 
ATOM   3599 O OE1 . GLU A 1 424 ? 11.357  22.477 92.530  1.00 36.89 ? 424 GLU A OE1 1 
ATOM   3600 O OE2 . GLU A 1 424 ? 12.733  23.761 91.398  1.00 34.87 ? 424 GLU A OE2 1 
ATOM   3601 N N   . TYR A 1 425 ? 9.926   22.242 87.303  1.00 15.06 ? 425 TYR A N   1 
ATOM   3602 C CA  . TYR A 1 425 ? 9.228   21.006 86.954  1.00 12.80 ? 425 TYR A CA  1 
ATOM   3603 C C   . TYR A 1 425 ? 10.183  19.956 86.407  1.00 15.25 ? 425 TYR A C   1 
ATOM   3604 O O   . TYR A 1 425 ? 10.051  18.775 86.733  1.00 12.63 ? 425 TYR A O   1 
ATOM   3605 C CB  . TYR A 1 425 ? 8.131   21.267 85.924  1.00 15.30 ? 425 TYR A CB  1 
ATOM   3606 C CG  . TYR A 1 425 ? 6.763   21.519 86.497  1.00 11.71 ? 425 TYR A CG  1 
ATOM   3607 C CD1 . TYR A 1 425 ? 6.589   22.050 87.786  1.00 13.47 ? 425 TYR A CD1 1 
ATOM   3608 C CD2 . TYR A 1 425 ? 5.623   21.245 85.747  1.00 13.36 ? 425 TYR A CD2 1 
ATOM   3609 C CE1 . TYR A 1 425 ? 5.320   22.276 88.299  1.00 14.84 ? 425 TYR A CE1 1 
ATOM   3610 C CE2 . TYR A 1 425 ? 4.373   21.489 86.236  1.00 15.15 ? 425 TYR A CE2 1 
ATOM   3611 C CZ  . TYR A 1 425 ? 4.215   22.000 87.519  1.00 14.24 ? 425 TYR A CZ  1 
ATOM   3612 O OH  . TYR A 1 425 ? 2.953   22.226 87.995  1.00 14.87 ? 425 TYR A OH  1 
ATOM   3613 N N   . TRP A 1 426 ? 11.107  20.350 85.519  1.00 13.60 ? 426 TRP A N   1 
ATOM   3614 C CA  . TRP A 1 426 ? 12.075  19.382 85.014  1.00 11.68 ? 426 TRP A CA  1 
ATOM   3615 C C   . TRP A 1 426 ? 12.936  18.838 86.146  1.00 15.13 ? 426 TRP A C   1 
ATOM   3616 O O   . TRP A 1 426 ? 13.188  17.629 86.208  1.00 12.17 ? 426 TRP A O   1 
ATOM   3617 C CB  . TRP A 1 426 ? 12.939  20.005 83.909  1.00 11.65 ? 426 TRP A CB  1 
ATOM   3618 C CG  . TRP A 1 426 ? 12.196  20.150 82.603  1.00 13.21 ? 426 TRP A CG  1 
ATOM   3619 C CD1 . TRP A 1 426 ? 11.664  21.300 82.070  1.00 15.20 ? 426 TRP A CD1 1 
ATOM   3620 C CD2 . TRP A 1 426 ? 11.888  19.102 81.685  1.00 13.70 ? 426 TRP A CD2 1 
ATOM   3621 N NE1 . TRP A 1 426 ? 11.060  21.022 80.864  1.00 12.33 ? 426 TRP A NE1 1 
ATOM   3622 C CE2 . TRP A 1 426 ? 11.184  19.679 80.607  1.00 14.55 ? 426 TRP A CE2 1 
ATOM   3623 C CE3 . TRP A 1 426 ? 12.142  17.729 81.670  1.00 13.19 ? 426 TRP A CE3 1 
ATOM   3624 C CZ2 . TRP A 1 426 ? 10.736  18.926 79.516  1.00 15.40 ? 426 TRP A CZ2 1 
ATOM   3625 C CZ3 . TRP A 1 426 ? 11.700  16.984 80.587  1.00 16.27 ? 426 TRP A CZ3 1 
ATOM   3626 C CH2 . TRP A 1 426 ? 11.007  17.587 79.525  1.00 17.91 ? 426 TRP A CH2 1 
ATOM   3627 N N   . LYS A 1 427 ? 13.365  19.711 87.075  1.00 13.85 ? 427 LYS A N   1 
ATOM   3628 C CA  . LYS A 1 427 ? 14.116  19.241 88.240  1.00 17.42 ? 427 LYS A CA  1 
ATOM   3629 C C   . LYS A 1 427 ? 13.319  18.213 89.039  1.00 14.38 ? 427 LYS A C   1 
ATOM   3630 O O   . LYS A 1 427 ? 13.867  17.190 89.473  1.00 16.09 ? 427 LYS A O   1 
ATOM   3631 C CB  . LYS A 1 427 ? 14.486  20.419 89.136  1.00 19.69 ? 427 LYS A CB  1 
ATOM   3632 C CG  . LYS A 1 427 ? 15.770  21.090 88.742  1.00 27.68 ? 427 LYS A CG  1 
ATOM   3633 C CD  . LYS A 1 427 ? 16.030  22.315 89.586  1.00 36.43 ? 427 LYS A CD  1 
ATOM   3634 C CE  . LYS A 1 427 ? 15.409  23.530 88.934  1.00 49.61 ? 427 LYS A CE  1 
ATOM   3635 N NZ  . LYS A 1 427 ? 14.796  24.452 89.932  1.00 56.18 ? 427 LYS A NZ  1 
ATOM   3636 N N   . ILE A 1 428 ? 12.030  18.483 89.259  1.00 14.49 ? 428 ILE A N   1 
ATOM   3637 C CA  . ILE A 1 428 ? 11.165  17.537 89.964  1.00 14.78 ? 428 ILE A CA  1 
ATOM   3638 C C   . ILE A 1 428 ? 11.087  16.219 89.203  1.00 15.47 ? 428 ILE A C   1 
ATOM   3639 O O   . ILE A 1 428 ? 11.185  15.133 89.789  1.00 14.69 ? 428 ILE A O   1 
ATOM   3640 C CB  . ILE A 1 428 ? 9.767   18.148 90.163  1.00 12.09 ? 428 ILE A CB  1 
ATOM   3641 C CG1 . ILE A 1 428 ? 9.810   19.247 91.231  1.00 15.75 ? 428 ILE A CG1 1 
ATOM   3642 C CG2 . ILE A 1 428 ? 8.734   17.073 90.507  1.00 15.72 ? 428 ILE A CG2 1 
ATOM   3643 C CD1 . ILE A 1 428 ? 8.614   20.168 91.177  1.00 18.77 ? 428 ILE A CD1 1 
ATOM   3644 N N   . LEU A 1 429 ? 10.899  16.301 87.883  1.00 11.47 ? 429 LEU A N   1 
ATOM   3645 C CA  . LEU A 1 429 ? 10.796  15.093 87.071  1.00 11.40 ? 429 LEU A CA  1 
ATOM   3646 C C   . LEU A 1 429 ? 12.107  14.309 87.072  1.00 12.18 ? 429 LEU A C   1 
ATOM   3647 O O   . LEU A 1 429 ? 12.101  13.076 87.165  1.00 14.41 ? 429 LEU A O   1 
ATOM   3648 C CB  . LEU A 1 429 ? 10.386  15.468 85.644  1.00 12.34 ? 429 LEU A CB  1 
ATOM   3649 C CG  . LEU A 1 429 ? 10.215  14.302 84.667  1.00 13.54 ? 429 LEU A CG  1 
ATOM   3650 C CD1 . LEU A 1 429 ? 8.973   13.526 84.981  1.00 15.76 ? 429 LEU A CD1 1 
ATOM   3651 C CD2 . LEU A 1 429 ? 10.180  14.799 83.221  1.00 14.99 ? 429 LEU A CD2 1 
ATOM   3652 N N   . ILE A 1 430 ? 13.244  15.007 86.973  1.00 12.37 ? 430 ILE A N   1 
ATOM   3653 C CA  . ILE A 1 430 ? 14.538  14.328 86.976  1.00 12.53 ? 430 ILE A CA  1 
ATOM   3654 C C   . ILE A 1 430 ? 14.739  13.559 88.277  1.00 13.55 ? 430 ILE A C   1 
ATOM   3655 O O   . ILE A 1 430 ? 15.171  12.397 88.277  1.00 18.54 ? 430 ILE A O   1 
ATOM   3656 C CB  . ILE A 1 430 ? 15.671  15.342 86.743  1.00 12.67 ? 430 ILE A CB  1 
ATOM   3657 C CG1 . ILE A 1 430 ? 15.655  15.812 85.274  1.00 12.92 ? 430 ILE A CG1 1 
ATOM   3658 C CG2 . ILE A 1 430 ? 17.005  14.747 87.148  1.00 13.62 ? 430 ILE A CG2 1 
ATOM   3659 C CD1 . ILE A 1 430 ? 16.257  17.217 85.088  1.00 17.34 ? 430 ILE A CD1 1 
ATOM   3660 N N   . GLU A 1 431 ? 14.464  14.210 89.408  1.00 12.63 ? 431 GLU A N   1 
ATOM   3661 C CA  . GLU A 1 431 ? 14.627  13.543 90.695  1.00 14.06 ? 431 GLU A CA  1 
ATOM   3662 C C   . GLU A 1 431 ? 13.649  12.384 90.834  1.00 21.95 ? 431 GLU A C   1 
ATOM   3663 O O   . GLU A 1 431 ? 14.022  11.304 91.309  1.00 19.12 ? 431 GLU A O   1 
ATOM   3664 C CB  . GLU A 1 431 ? 14.440  14.554 91.828  1.00 15.45 ? 431 GLU A CB  1 
ATOM   3665 C CG  . GLU A 1 431 ? 14.688  14.003 93.210  1.00 26.84 ? 431 GLU A CG  1 
ATOM   3666 C CD  . GLU A 1 431 ? 16.110  13.506 93.403  1.00 40.77 ? 431 GLU A CD  1 
ATOM   3667 O OE1 . GLU A 1 431 ? 16.313  12.631 94.271  1.00 46.26 ? 431 GLU A OE1 1 
ATOM   3668 O OE2 . GLU A 1 431 ? 17.023  13.999 92.704  1.00 36.14 ? 431 GLU A OE2 1 
ATOM   3669 N N   . ALA A 1 432 ? 12.395  12.581 90.414  1.00 17.32 ? 432 ALA A N   1 
ATOM   3670 C CA  . ALA A 1 432 ? 11.427  11.488 90.491  1.00 16.78 ? 432 ALA A CA  1 
ATOM   3671 C C   . ALA A 1 432 ? 11.818  10.327 89.589  1.00 21.27 ? 432 ALA A C   1 
ATOM   3672 O O   . ALA A 1 432 ? 11.574  9.162  89.930  1.00 19.48 ? 432 ALA A O   1 
ATOM   3673 C CB  . ALA A 1 432 ? 10.025  11.985 90.137  1.00 15.18 ? 432 ALA A CB  1 
ATOM   3674 N N   . LYS A 1 433 ? 12.434  10.619 88.440  1.00 15.47 ? 433 LYS A N   1 
ATOM   3675 C CA  . LYS A 1 433 ? 12.790  9.554  87.515  1.00 16.73 ? 433 LYS A CA  1 
ATOM   3676 C C   . LYS A 1 433 ? 13.845  8.631  88.116  1.00 18.39 ? 433 LYS A C   1 
ATOM   3677 O O   . LYS A 1 433 ? 13.862  7.431  87.820  1.00 18.68 ? 433 LYS A O   1 
ATOM   3678 C CB  . LYS A 1 433 ? 13.259  10.164 86.193  1.00 15.13 ? 433 LYS A CB  1 
ATOM   3679 C CG  . LYS A 1 433 ? 13.865  9.168  85.208  1.00 18.36 ? 433 LYS A CG  1 
ATOM   3680 C CD  . LYS A 1 433 ? 12.838  8.158  84.731  1.00 17.18 ? 433 LYS A CD  1 
ATOM   3681 C CE  . LYS A 1 433 ? 13.449  7.233  83.682  1.00 17.71 ? 433 LYS A CE  1 
ATOM   3682 N NZ  . LYS A 1 433 ? 12.531  6.113  83.305  1.00 20.02 ? 433 LYS A NZ  1 
ATOM   3683 N N   . LYS A 1 434 ? 14.715  9.162  88.982  1.00 21.36 ? 434 LYS A N   1 
ATOM   3684 C CA  . LYS A 1 434 ? 15.709  8.319  89.643  1.00 24.55 ? 434 LYS A CA  1 
ATOM   3685 C C   . LYS A 1 434 ? 15.061  7.222  90.478  1.00 24.04 ? 434 LYS A C   1 
ATOM   3686 O O   . LYS A 1 434 ? 15.634  6.137  90.629  1.00 30.24 ? 434 LYS A O   1 
ATOM   3687 C CB  . LYS A 1 434 ? 16.615  9.170  90.537  1.00 23.52 ? 434 LYS A CB  1 
ATOM   3688 C CG  . LYS A 1 434 ? 17.470  10.196 89.815  1.00 31.07 ? 434 LYS A CG  1 
ATOM   3689 C CD  . LYS A 1 434 ? 18.236  11.029 90.845  1.00 36.35 ? 434 LYS A CD  1 
ATOM   3690 C CE  . LYS A 1 434 ? 19.112  12.089 90.204  1.00 38.82 ? 434 LYS A CE  1 
ATOM   3691 N NZ  . LYS A 1 434 ? 19.619  13.040 91.232  1.00 42.51 ? 434 LYS A NZ  1 
ATOM   3692 N N   . LYS A 1 435 ? 13.873  7.478  91.025  1.00 18.85 ? 435 LYS A N   1 
ATOM   3693 C CA  . LYS A 1 435 ? 13.189  6.543  91.909  1.00 22.30 ? 435 LYS A CA  1 
ATOM   3694 C C   . LYS A 1 435 ? 11.897  5.986  91.313  1.00 22.67 ? 435 LYS A C   1 
ATOM   3695 O O   . LYS A 1 435 ? 11.123  5.346  92.036  1.00 24.91 ? 435 LYS A O   1 
ATOM   3696 C CB  . LYS A 1 435 ? 12.886  7.221  93.247  1.00 28.40 ? 435 LYS A CB  1 
ATOM   3697 C CG  . LYS A 1 435 ? 14.126  7.605  94.044  1.00 38.84 ? 435 LYS A CG  1 
ATOM   3698 C CD  . LYS A 1 435 ? 13.793  8.637  95.111  1.00 48.25 ? 435 LYS A CD  1 
ATOM   3699 C CE  . LYS A 1 435 ? 14.373  9.990  94.755  1.00 54.31 ? 435 LYS A CE  1 
ATOM   3700 N NZ  . LYS A 1 435 ? 13.983  10.402 93.379  1.00 60.13 ? 435 LYS A NZ  1 
ATOM   3701 N N   . ALA A 1 436 ? 11.637  6.212  90.056  1.00 21.33 ? 436 ALA A N   1 
ATOM   3702 C CA  . ALA A 1 436 ? 10.430  5.722  89.467  1.00 22.00 ? 436 ALA A CA  1 
ATOM   3703 C C   . ALA A 1 436 ? 10.226  4.226  89.468  1.00 22.88 ? 436 ALA A C   1 
ATOM   3704 O O   . ALA A 1 436 ? 11.121  3.503  89.237  1.00 26.24 ? 436 ALA A O   1 
ATOM   3705 C CB  . ALA A 1 436 ? 10.331  6.220  88.044  1.00 20.74 ? 436 ALA A CB  1 
ATOM   3706 N N   . LYS A 1 437 ? 8.999   3.810  89.669  1.00 23.44 ? 437 LYS A N   1 
ATOM   3707 C CA  . LYS A 1 437 ? 8.623   2.400  89.671  1.00 28.91 ? 437 LYS A CA  1 
ATOM   3708 C C   . LYS A 1 437 ? 7.537   2.009  88.731  1.00 24.64 ? 437 LYS A C   1 
ATOM   3709 O O   . LYS A 1 437 ? 7.318   0.879  88.561  1.00 29.69 ? 437 LYS A O   1 
ATOM   3710 C CB  . LYS A 1 437 ? 8.126   1.961  91.023  1.00 28.75 ? 437 LYS A CB  1 
ATOM   3711 C CG  . LYS A 1 437 ? 8.656   2.698  92.172  1.00 40.87 ? 437 LYS A CG  1 
ATOM   3712 C CD  . LYS A 1 437 ? 9.343   1.758  93.056  1.00 53.49 ? 437 LYS A CD  1 
ATOM   3713 C CE  . LYS A 1 437 ? 10.638  1.473  92.379  1.00 57.11 ? 437 LYS A CE  1 
ATOM   3714 N NZ  . LYS A 1 437 ? 11.747  1.583  93.345  1.00 58.20 ? 437 LYS A NZ  1 
ATOM   3715 N N   . ASN A 1 438 ? 6.847   2.965  88.135  1.00 22.86 ? 438 ASN A N   1 
ATOM   3716 C CA  . ASN A 1 438 ? 5.762   2.640  87.266  1.00 25.98 ? 438 ASN A CA  1 
ATOM   3717 C C   . ASN A 1 438 ? 5.589   3.678  86.203  1.00 19.08 ? 438 ASN A C   1 
ATOM   3718 O O   . ASN A 1 438 ? 6.271   4.641  86.225  1.00 21.47 ? 438 ASN A O   1 
ATOM   3719 C CB  . ASN A 1 438 ? 4.502   2.463  88.029  1.00 28.13 ? 438 ASN A CB  1 
ATOM   3720 C CG  . ASN A 1 438 ? 4.127   3.691  88.775  1.00 20.50 ? 438 ASN A CG  1 
ATOM   3721 O OD1 . ASN A 1 438 ? 3.833   4.650  88.195  1.00 18.11 ? 438 ASN A OD1 1 
ATOM   3722 N ND2 . ASN A 1 438 ? 4.110   3.619  90.068  1.00 22.68 ? 438 ASN A ND2 1 
ATOM   3723 N N   . ASP A 1 439 ? 4.679   3.434  85.291  1.00 23.22 ? 439 ASP A N   1 
ATOM   3724 C CA  . ASP A 1 439 ? 4.505   4.273  84.114  1.00 21.93 ? 439 ASP A CA  1 
ATOM   3725 C C   . ASP A 1 439 ? 3.852   5.611  84.417  1.00 18.92 ? 439 ASP A C   1 
ATOM   3726 O O   . ASP A 1 439 ? 3.646   6.403  83.491  1.00 15.10 ? 439 ASP A O   1 
ATOM   3727 C CB  . ASP A 1 439 ? 3.681   3.527  83.061  1.00 19.43 ? 439 ASP A CB  1 
ATOM   3728 C CG  . ASP A 1 439 ? 4.493   2.502  82.308  1.00 28.58 ? 439 ASP A CG  1 
ATOM   3729 O OD1 . ASP A 1 439 ? 5.732   2.466  82.479  1.00 31.71 ? 439 ASP A OD1 1 
ATOM   3730 O OD2 . ASP A 1 439 ? 3.889   1.736  81.533  1.00 32.75 ? 439 ASP A OD2 1 
ATOM   3731 N N   . TYR A 1 440 ? 3.495   5.900  85.672  1.00 15.12 ? 440 TYR A N   1 
ATOM   3732 C CA  . TYR A 1 440 ? 3.067   7.263  85.941  1.00 16.21 ? 440 TYR A CA  1 
ATOM   3733 C C   . TYR A 1 440 ? 4.194   8.252  85.681  1.00 11.34 ? 440 TYR A C   1 
ATOM   3734 O O   . TYR A 1 440 ? 3.918   9.426  85.438  1.00 14.35 ? 440 TYR A O   1 
ATOM   3735 C CB  . TYR A 1 440 ? 2.506   7.402  87.367  1.00 13.35 ? 440 TYR A CB  1 
ATOM   3736 C CG  . TYR A 1 440 ? 1.014   7.112  87.427  1.00 18.07 ? 440 TYR A CG  1 
ATOM   3737 C CD1 . TYR A 1 440 ? 0.091   8.027  86.921  1.00 21.49 ? 440 TYR A CD1 1 
ATOM   3738 C CD2 . TYR A 1 440 ? 0.536   5.922  87.960  1.00 26.21 ? 440 TYR A CD2 1 
ATOM   3739 C CE1 . TYR A 1 440 ? -1.269  7.769  86.957  1.00 23.30 ? 440 TYR A CE1 1 
ATOM   3740 C CE2 . TYR A 1 440 ? -0.831  5.655  88.011  1.00 25.36 ? 440 TYR A CE2 1 
ATOM   3741 C CZ  . TYR A 1 440 ? -1.725  6.586  87.508  1.00 25.83 ? 440 TYR A CZ  1 
ATOM   3742 O OH  . TYR A 1 440 ? -3.081  6.317  87.553  1.00 28.17 ? 440 TYR A OH  1 
ATOM   3743 N N   . ILE A 1 441 ? 5.458   7.803  85.655  1.00 13.69 ? 441 ILE A N   1 
ATOM   3744 C CA  . ILE A 1 441 ? 6.513   8.738  85.274  1.00 11.11 ? 441 ILE A CA  1 
ATOM   3745 C C   . ILE A 1 441 ? 6.335   9.176  83.815  1.00 12.80 ? 441 ILE A C   1 
ATOM   3746 O O   . ILE A 1 441 ? 6.688   10.307 83.451  1.00 11.97 ? 441 ILE A O   1 
ATOM   3747 C CB  . ILE A 1 441 ? 7.915   8.136  85.540  1.00 12.53 ? 441 ILE A CB  1 
ATOM   3748 C CG1 . ILE A 1 441 ? 8.982   9.238  85.567  1.00 15.18 ? 441 ILE A CG1 1 
ATOM   3749 C CG2 . ILE A 1 441 ? 8.299   7.078  84.492  1.00 19.66 ? 441 ILE A CG2 1 
ATOM   3750 C CD1 . ILE A 1 441 ? 8.908   10.128 86.803  1.00 16.98 ? 441 ILE A CD1 1 
ATOM   3751 N N   . LEU A 1 442 ? 5.794   8.301  82.960  1.00 11.57 ? 442 LEU A N   1 
ATOM   3752 C CA  . LEU A 1 442 ? 5.519   8.696  81.579  1.00 10.91 ? 442 LEU A CA  1 
ATOM   3753 C C   . LEU A 1 442 ? 4.414   9.742  81.515  1.00 10.45 ? 442 LEU A C   1 
ATOM   3754 O O   . LEU A 1 442 ? 4.464   10.661 80.685  1.00 11.93 ? 442 LEU A O   1 
ATOM   3755 C CB  . LEU A 1 442 ? 5.124   7.478  80.747  1.00 12.66 ? 442 LEU A CB  1 
ATOM   3756 C CG  . LEU A 1 442 ? 6.109   6.310  80.778  1.00 15.29 ? 442 LEU A CG  1 
ATOM   3757 C CD1 . LEU A 1 442 ? 5.557   5.153  79.948  1.00 17.39 ? 442 LEU A CD1 1 
ATOM   3758 C CD2 . LEU A 1 442 ? 7.477   6.757  80.245  1.00 14.61 ? 442 LEU A CD2 1 
ATOM   3759 N N   . VAL A 1 443 ? 3.386   9.593  82.361  1.00 11.30 ? 443 VAL A N   1 
ATOM   3760 C CA  . VAL A 1 443 ? 2.311   10.577 82.395  1.00 11.03 ? 443 VAL A CA  1 
ATOM   3761 C C   . VAL A 1 443 ? 2.882   11.951 82.691  1.00 12.45 ? 443 VAL A C   1 
ATOM   3762 O O   . VAL A 1 443 ? 2.501   12.945 82.056  1.00 10.20 ? 443 VAL A O   1 
ATOM   3763 C CB  . VAL A 1 443 ? 1.243   10.196 83.437  1.00 11.31 ? 443 VAL A CB  1 
ATOM   3764 C CG1 . VAL A 1 443 ? 0.134   11.279 83.467  1.00 11.65 ? 443 VAL A CG1 1 
ATOM   3765 C CG2 . VAL A 1 443 ? 0.633   8.793  83.161  1.00 13.28 ? 443 VAL A CG2 1 
ATOM   3766 N N   . ALA A 1 444 ? 3.790   12.020 83.670  1.00 11.63 ? 444 ALA A N   1 
ATOM   3767 C CA  . ALA A 1 444 ? 4.408   13.264 84.112  1.00 10.33 ? 444 ALA A CA  1 
ATOM   3768 C C   . ALA A 1 444 ? 5.314   13.861 83.053  1.00 13.52 ? 444 ALA A C   1 
ATOM   3769 O O   . ALA A 1 444 ? 5.667   15.046 83.140  1.00 13.63 ? 444 ALA A O   1 
ATOM   3770 C CB  . ALA A 1 444 ? 5.197   13.033 85.405  1.00 13.47 ? 444 ALA A CB  1 
ATOM   3771 N N   . GLU A 1 445 ? 5.717   13.067 82.066  1.00 11.99 ? 445 GLU A N   1 
ATOM   3772 C CA  . GLU A 1 445 ? 6.531   13.580 80.974  1.00 12.63 ? 445 GLU A CA  1 
ATOM   3773 C C   . GLU A 1 445 ? 5.706   14.294 79.904  1.00 9.90  ? 445 GLU A C   1 
ATOM   3774 O O   . GLU A 1 445 ? 6.288   14.826 78.959  1.00 11.51 ? 445 GLU A O   1 
ATOM   3775 C CB  . GLU A 1 445 ? 7.357   12.430 80.359  1.00 11.81 ? 445 GLU A CB  1 
ATOM   3776 C CG  . GLU A 1 445 ? 8.501   11.988 81.272  1.00 14.01 ? 445 GLU A CG  1 
ATOM   3777 C CD  . GLU A 1 445 ? 8.995   10.576 81.029  1.00 15.27 ? 445 GLU A CD  1 
ATOM   3778 O OE1 . GLU A 1 445 ? 8.619   9.950  80.016  1.00 12.46 ? 445 GLU A OE1 1 
ATOM   3779 O OE2 . GLU A 1 445 ? 9.803   10.093 81.857  1.00 15.66 ? 445 GLU A OE2 1 
ATOM   3780 N N   . GLY A 1 446 ? 4.384   14.347 80.044  1.00 9.71  ? 446 GLY A N   1 
ATOM   3781 C CA  . GLY A 1 446 ? 3.565   15.056 79.065  1.00 10.32 ? 446 GLY A CA  1 
ATOM   3782 C C   . GLY A 1 446 ? 3.925   16.532 78.970  1.00 10.35 ? 446 GLY A C   1 
ATOM   3783 O O   . GLY A 1 446 ? 4.248   17.187 79.968  1.00 10.39 ? 446 GLY A O   1 
ATOM   3784 N N   . SER A 1 447 ? 3.831   17.069 77.745  1.00 9.19  ? 447 SER A N   1 
ATOM   3785 C CA  . SER A 1 447 ? 4.225   18.459 77.522  1.00 11.07 ? 447 SER A CA  1 
ATOM   3786 C C   . SER A 1 447 ? 3.313   19.428 78.267  1.00 13.23 ? 447 SER A C   1 
ATOM   3787 O O   . SER A 1 447 ? 3.755   20.514 78.673  1.00 12.03 ? 447 SER A O   1 
ATOM   3788 C CB  . SER A 1 447 ? 4.209   18.777 76.030  1.00 11.14 ? 447 SER A CB  1 
ATOM   3789 O OG  . SER A 1 447 ? 2.885   18.729 75.514  1.00 14.19 ? 447 SER A OG  1 
ATOM   3790 N N   . ASP A 1 448 ? 2.044   19.053 78.458  1.00 10.69 ? 448 ASP A N   1 
ATOM   3791 C CA  . ASP A 1 448 ? 1.065   19.988 79.005  1.00 10.75 ? 448 ASP A CA  1 
ATOM   3792 C C   . ASP A 1 448 ? 1.488   20.548 80.355  1.00 12.27 ? 448 ASP A C   1 
ATOM   3793 O O   . ASP A 1 448 ? 1.278   21.735 80.620  1.00 10.03 ? 448 ASP A O   1 
ATOM   3794 C CB  . ASP A 1 448 ? -0.287  19.303 79.136  1.00 13.24 ? 448 ASP A CB  1 
ATOM   3795 C CG  . ASP A 1 448 ? -0.739  18.721 77.838  1.00 10.11 ? 448 ASP A CG  1 
ATOM   3796 O OD1 . ASP A 1 448 ? -0.222  17.633 77.500  1.00 11.97 ? 448 ASP A OD1 1 
ATOM   3797 O OD2 . ASP A 1 448 ? -1.572  19.358 77.159  1.00 11.46 ? 448 ASP A OD2 1 
ATOM   3798 N N   . TRP A 1 449 ? 2.040   19.709 81.239  1.00 9.77  ? 449 TRP A N   1 
ATOM   3799 C CA  . TRP A 1 449 ? 2.374   20.190 82.581  1.00 9.31  ? 449 TRP A CA  1 
ATOM   3800 C C   . TRP A 1 449 ? 3.383   21.334 82.521  1.00 11.73 ? 449 TRP A C   1 
ATOM   3801 O O   . TRP A 1 449 ? 3.284   22.313 83.278  1.00 11.79 ? 449 TRP A O   1 
ATOM   3802 C CB  . TRP A 1 449 ? 2.921   19.036 83.428  1.00 14.03 ? 449 TRP A CB  1 
ATOM   3803 C CG  . TRP A 1 449 ? 2.155   17.762 83.229  1.00 12.44 ? 449 TRP A CG  1 
ATOM   3804 C CD1 . TRP A 1 449 ? 2.642   16.580 82.755  1.00 12.87 ? 449 TRP A CD1 1 
ATOM   3805 C CD2 . TRP A 1 449 ? 0.760   17.555 83.462  1.00 7.98  ? 449 TRP A CD2 1 
ATOM   3806 N NE1 . TRP A 1 449 ? 1.642   15.639 82.690  1.00 10.94 ? 449 TRP A NE1 1 
ATOM   3807 C CE2 . TRP A 1 449 ? 0.470   16.219 83.097  1.00 7.86  ? 449 TRP A CE2 1 
ATOM   3808 C CE3 . TRP A 1 449 ? -0.288  18.377 83.918  1.00 8.85  ? 449 TRP A CE3 1 
ATOM   3809 C CZ2 . TRP A 1 449 ? -0.801  15.673 83.214  1.00 10.58 ? 449 TRP A CZ2 1 
ATOM   3810 C CZ3 . TRP A 1 449 ? -1.549  17.833 84.018  1.00 9.70  ? 449 TRP A CZ3 1 
ATOM   3811 C CH2 . TRP A 1 449 ? -1.798  16.493 83.665  1.00 13.38 ? 449 TRP A CH2 1 
ATOM   3812 N N   . PHE A 1 450 ? 4.359   21.228 81.624  1.00 10.10 ? 450 PHE A N   1 
ATOM   3813 C CA  . PHE A 1 450 ? 5.385   22.253 81.491  1.00 14.06 ? 450 PHE A CA  1 
ATOM   3814 C C   . PHE A 1 450 ? 4.854   23.484 80.772  1.00 12.92 ? 450 PHE A C   1 
ATOM   3815 O O   . PHE A 1 450 ? 5.338   24.601 81.011  1.00 13.56 ? 450 PHE A O   1 
ATOM   3816 C CB  . PHE A 1 450 ? 6.588   21.666 80.745  1.00 12.97 ? 450 PHE A CB  1 
ATOM   3817 C CG  . PHE A 1 450 ? 7.123   20.419 81.379  1.00 13.61 ? 450 PHE A CG  1 
ATOM   3818 C CD1 . PHE A 1 450 ? 6.561   19.173 81.084  1.00 15.27 ? 450 PHE A CD1 1 
ATOM   3819 C CD2 . PHE A 1 450 ? 8.161   20.489 82.295  1.00 12.59 ? 450 PHE A CD2 1 
ATOM   3820 C CE1 . PHE A 1 450 ? 7.047   18.021 81.669  1.00 12.59 ? 450 PHE A CE1 1 
ATOM   3821 C CE2 . PHE A 1 450 ? 8.653   19.335 82.900  1.00 14.63 ? 450 PHE A CE2 1 
ATOM   3822 C CZ  . PHE A 1 450 ? 8.100   18.104 82.595  1.00 13.52 ? 450 PHE A CZ  1 
ATOM   3823 N N   . TRP A 1 451 ? 3.863   23.282 79.896  1.00 12.89 ? 451 TRP A N   1 
ATOM   3824 C CA  . TRP A 1 451 ? 3.246   24.385 79.171  1.00 13.58 ? 451 TRP A CA  1 
ATOM   3825 C C   . TRP A 1 451 ? 2.636   25.403 80.129  1.00 16.74 ? 451 TRP A C   1 
ATOM   3826 O O   . TRP A 1 451 ? 2.856   26.611 79.995  1.00 16.58 ? 451 TRP A O   1 
ATOM   3827 C CB  . TRP A 1 451 ? 2.181   23.800 78.241  1.00 13.38 ? 451 TRP A CB  1 
ATOM   3828 C CG  . TRP A 1 451 ? 1.884   24.602 77.060  1.00 32.50 ? 451 TRP A CG  1 
ATOM   3829 C CD1 . TRP A 1 451 ? 2.438   24.469 75.828  1.00 37.16 ? 451 TRP A CD1 1 
ATOM   3830 C CD2 . TRP A 1 451 ? 0.941   25.668 76.969  1.00 40.07 ? 451 TRP A CD2 1 
ATOM   3831 N NE1 . TRP A 1 451 ? 1.908   25.393 74.971  1.00 37.56 ? 451 TRP A NE1 1 
ATOM   3832 C CE2 . TRP A 1 451 ? 0.983   26.144 75.646  1.00 37.08 ? 451 TRP A CE2 1 
ATOM   3833 C CE3 . TRP A 1 451 ? 0.063   26.267 77.875  1.00 36.98 ? 451 TRP A CE3 1 
ATOM   3834 C CZ2 . TRP A 1 451 ? 0.190   27.197 75.203  1.00 39.08 ? 451 TRP A CZ2 1 
ATOM   3835 C CZ3 . TRP A 1 451 ? -0.722  27.317 77.435  1.00 43.75 ? 451 TRP A CZ3 1 
ATOM   3836 C CH2 . TRP A 1 451 ? -0.656  27.770 76.111  1.00 49.17 ? 451 TRP A CH2 1 
ATOM   3837 N N   . TRP A 1 452 ? 1.874   24.921 81.117  1.00 13.39 ? 452 TRP A N   1 
ATOM   3838 C CA  . TRP A 1 452 ? 1.126   25.817 81.986  1.00 17.09 ? 452 TRP A CA  1 
ATOM   3839 C C   . TRP A 1 452 ? 1.981   26.361 83.117  1.00 15.16 ? 452 TRP A C   1 
ATOM   3840 O O   . TRP A 1 452 ? 1.650   27.402 83.690  1.00 17.02 ? 452 TRP A O   1 
ATOM   3841 C CB  . TRP A 1 452 ? -0.094  25.078 82.554  1.00 15.03 ? 452 TRP A CB  1 
ATOM   3842 C CG  . TRP A 1 452 ? -1.042  24.682 81.479  1.00 15.15 ? 452 TRP A CG  1 
ATOM   3843 C CD1 . TRP A 1 452 ? -1.282  23.417 81.018  1.00 15.87 ? 452 TRP A CD1 1 
ATOM   3844 C CD2 . TRP A 1 452 ? -1.872  25.556 80.709  1.00 15.49 ? 452 TRP A CD2 1 
ATOM   3845 N NE1 . TRP A 1 452 ? -2.195  23.451 80.002  1.00 14.95 ? 452 TRP A NE1 1 
ATOM   3846 C CE2 . TRP A 1 452 ? -2.586  24.749 79.795  1.00 15.85 ? 452 TRP A CE2 1 
ATOM   3847 C CE3 . TRP A 1 452 ? -2.082  26.941 80.699  1.00 19.40 ? 452 TRP A CE3 1 
ATOM   3848 C CZ2 . TRP A 1 452 ? -3.492  25.273 78.887  1.00 17.24 ? 452 TRP A CZ2 1 
ATOM   3849 C CZ3 . TRP A 1 452 ? -2.991  27.465 79.795  1.00 25.85 ? 452 TRP A CZ3 1 
ATOM   3850 C CH2 . TRP A 1 452 ? -3.689  26.635 78.901  1.00 19.42 ? 452 TRP A CH2 1 
ATOM   3851 N N   . GLN A 1 453 ? 3.073   25.684 83.442  1.00 15.49 ? 453 GLN A N   1 
ATOM   3852 C CA  . GLN A 1 453 ? 3.856   26.073 84.605  1.00 19.48 ? 453 GLN A CA  1 
ATOM   3853 C C   . GLN A 1 453 ? 4.561   27.391 84.332  1.00 20.49 ? 453 GLN A C   1 
ATOM   3854 O O   . GLN A 1 453 ? 5.021   27.659 83.218  1.00 23.09 ? 453 GLN A O   1 
ATOM   3855 C CB  . GLN A 1 453 ? 4.849   24.958 84.967  1.00 19.54 ? 453 GLN A CB  1 
ATOM   3856 C CG  . GLN A 1 453 ? 5.976   25.361 85.919  1.00 30.98 ? 453 GLN A CG  1 
ATOM   3857 C CD  . GLN A 1 453 ? 5.505   25.535 87.361  1.00 25.91 ? 453 GLN A CD  1 
ATOM   3858 O OE1 . GLN A 1 453 ? 4.303   25.533 87.636  1.00 25.13 ? 453 GLN A OE1 1 
ATOM   3859 N NE2 . GLN A 1 453 ? 6.454   25.678 88.283  1.00 24.70 ? 453 GLN A NE2 1 
ATOM   3860 N N   . GLY A 1 454 ? 4.625   28.236 85.352  1.00 28.40 ? 454 GLY A N   1 
ATOM   3861 C CA  . GLY A 1 454 ? 5.358   29.480 85.200  1.00 33.75 ? 454 GLY A CA  1 
ATOM   3862 C C   . GLY A 1 454 ? 4.793   30.389 84.135  1.00 46.19 ? 454 GLY A C   1 
ATOM   3863 O O   . GLY A 1 454 ? 5.551   31.000 83.370  1.00 44.80 ? 454 GLY A O   1 
ATOM   3864 N N   . GLU A 1 455 ? 3.471   30.459 84.088  1.00 49.83 ? 455 GLU A N   1 
ATOM   3865 C CA  . GLU A 1 455 ? 2.825   31.355 83.142  1.00 52.58 ? 455 GLU A CA  1 
ATOM   3866 C C   . GLU A 1 455 ? 2.063   32.508 83.845  1.00 57.37 ? 455 GLU A C   1 
ATOM   3867 O O   . GLU A 1 455 ? 2.139   33.592 83.356  1.00 63.90 ? 455 GLU A O   1 
ATOM   3868 C CB  . GLU A 1 455 ? 1.913   30.647 82.133  1.00 47.64 ? 455 GLU A CB  1 
ATOM   3869 C CG  . GLU A 1 455 ? 2.591   29.739 81.126  1.00 42.99 ? 455 GLU A CG  1 
ATOM   3870 C CD  . GLU A 1 455 ? 3.529   30.478 80.208  1.00 50.50 ? 455 GLU A CD  1 
ATOM   3871 O OE1 . GLU A 1 455 ? 4.434   29.853 79.606  1.00 42.62 ? 455 GLU A OE1 1 
ATOM   3872 O OE2 . GLU A 1 455 ? 3.296   31.699 80.061  1.00 52.30 ? 455 GLU A OE2 1 
ATOM   3873 N N   . GLU A 1 456 ? 1.345   32.329 84.938  1.00 60.45 ? 456 GLU A N   1 
ATOM   3874 C CA  . GLU A 1 456 ? 1.030   31.107 85.628  1.00 65.19 ? 456 GLU A CA  1 
ATOM   3875 C C   . GLU A 1 456 ? -0.273  30.660 85.003  1.00 66.91 ? 456 GLU A C   1 
ATOM   3876 O O   . GLU A 1 456 ? -0.264  29.821 84.131  1.00 67.66 ? 456 GLU A O   1 
ATOM   3877 C CB  . GLU A 1 456 ? 0.850   31.318 87.147  1.00 67.50 ? 456 GLU A CB  1 
ATOM   3878 N N   . LYS A 1 457 ? -1.438  31.198 85.378  1.00 69.09 ? 457 LYS A N   1 
ATOM   3879 C CA  . LYS A 1 457 ? -1.744  32.216 86.375  1.00 65.94 ? 457 LYS A CA  1 
ATOM   3880 C C   . LYS A 1 457 ? -3.102  32.527 85.795  1.00 69.27 ? 457 LYS A C   1 
ATOM   3881 O O   . LYS A 1 457 ? -3.182  33.202 84.795  1.00 77.51 ? 457 LYS A O   1 
ATOM   3882 C CB  . LYS A 1 457 ? -0.872  33.432 86.262  1.00 61.99 ? 457 LYS A CB  1 
ATOM   3883 N N   . ALA A 1 458 ? -4.138  31.987 86.409  1.00 60.14 ? 458 ALA A N   1 
ATOM   3884 C CA  . ALA A 1 458 ? -5.491  32.119 85.986  1.00 61.28 ? 458 ALA A CA  1 
ATOM   3885 C C   . ALA A 1 458 ? -6.175  30.879 86.508  1.00 58.25 ? 458 ALA A C   1 
ATOM   3886 O O   . ALA A 1 458 ? -5.496  29.931 86.881  1.00 52.13 ? 458 ALA A O   1 
ATOM   3887 C CB  . ALA A 1 458 ? -5.625  32.171 84.487  1.00 58.24 ? 458 ALA A CB  1 
ATOM   3888 N N   . PRO A 1 459 ? -7.557  30.895 86.511  1.00 55.47 ? 459 PRO A N   1 
ATOM   3889 C CA  . PRO A 1 459 ? -8.133  29.673 87.071  1.00 55.75 ? 459 PRO A CA  1 
ATOM   3890 C C   . PRO A 1 459 ? -7.649  28.336 86.447  1.00 57.90 ? 459 PRO A C   1 
ATOM   3891 O O   . PRO A 1 459 ? -7.375  28.138 85.295  1.00 59.97 ? 459 PRO A O   1 
ATOM   3892 C CB  . PRO A 1 459 ? -9.645  29.900 87.035  1.00 54.59 ? 459 PRO A CB  1 
ATOM   3893 C CG  . PRO A 1 459 ? -9.889  30.916 86.031  1.00 54.01 ? 459 PRO A CG  1 
ATOM   3894 C CD  . PRO A 1 459 ? -8.698  31.800 86.035  1.00 56.03 ? 459 PRO A CD  1 
ATOM   3895 N N   . PHE A 1 460 ? -7.413  27.425 87.351  1.00 58.41 ? 460 PHE A N   1 
ATOM   3896 C CA  . PHE A 1 460 ? -7.168  26.000 87.103  1.00 45.01 ? 460 PHE A CA  1 
ATOM   3897 C C   . PHE A 1 460 ? -5.712  25.644 86.826  1.00 39.35 ? 460 PHE A C   1 
ATOM   3898 O O   . PHE A 1 460 ? -5.393  24.459 86.792  1.00 42.28 ? 460 PHE A O   1 
ATOM   3899 C CB  . PHE A 1 460 ? -8.050  25.419 85.985  1.00 38.24 ? 460 PHE A CB  1 
ATOM   3900 C CG  . PHE A 1 460 ? -9.493  25.796 86.107  1.00 33.07 ? 460 PHE A CG  1 
ATOM   3901 C CD1 . PHE A 1 460 ? -10.092 25.917 87.354  1.00 34.17 ? 460 PHE A CD1 1 
ATOM   3902 C CD2 . PHE A 1 460 ? -10.249 26.071 84.982  1.00 33.90 ? 460 PHE A CD2 1 
ATOM   3903 C CE1 . PHE A 1 460 ? -11.416 26.282 87.473  1.00 39.98 ? 460 PHE A CE1 1 
ATOM   3904 C CE2 . PHE A 1 460 ? -11.580 26.440 85.103  1.00 34.97 ? 460 PHE A CE2 1 
ATOM   3905 C CZ  . PHE A 1 460 ? -12.160 26.550 86.346  1.00 36.37 ? 460 PHE A CZ  1 
ATOM   3906 N N   . VAL A 1 461 ? -4.809  26.617 86.639  1.00 35.14 ? 461 VAL A N   1 
ATOM   3907 C CA  . VAL A 1 461 ? -3.399  26.231 86.557  1.00 37.20 ? 461 VAL A CA  1 
ATOM   3908 C C   . VAL A 1 461 ? -2.996  25.508 87.829  1.00 33.88 ? 461 VAL A C   1 
ATOM   3909 O O   . VAL A 1 461 ? -2.144  24.612 87.807  1.00 31.87 ? 461 VAL A O   1 
ATOM   3910 C CB  . VAL A 1 461 ? -2.479  27.441 86.288  1.00 43.05 ? 461 VAL A CB  1 
ATOM   3911 C CG1 . VAL A 1 461 ? -2.517  28.427 87.442  1.00 43.86 ? 461 VAL A CG1 1 
ATOM   3912 C CG2 . VAL A 1 461 ? -1.042  26.964 86.052  1.00 44.13 ? 461 VAL A CG2 1 
ATOM   3913 N N   . GLU A 1 462 ? -3.617  25.858 88.956  1.00 20.57 ? 462 GLU A N   1 
ATOM   3914 C CA  . GLU A 1 462 ? -3.323  25.110 90.161  1.00 20.59 ? 462 GLU A CA  1 
ATOM   3915 C C   . GLU A 1 462 ? -3.756  23.652 90.016  1.00 23.65 ? 462 GLU A C   1 
ATOM   3916 O O   . GLU A 1 462 ? -3.130  22.767 90.603  1.00 21.40 ? 462 GLU A O   1 
ATOM   3917 C CB  . GLU A 1 462 ? -3.966  25.784 91.384  1.00 26.65 ? 462 GLU A CB  1 
ATOM   3918 C CG  . GLU A 1 462 ? -5.496  25.898 91.414  1.00 49.19 ? 462 GLU A CG  1 
ATOM   3919 C CD  . GLU A 1 462 ? -6.096  26.841 90.369  1.00 55.36 ? 462 GLU A CD  1 
ATOM   3920 O OE1 . GLU A 1 462 ? -7.320  26.737 90.130  1.00 55.40 ? 462 GLU A OE1 1 
ATOM   3921 O OE2 . GLU A 1 462 ? -5.365  27.678 89.793  1.00 53.57 ? 462 GLU A OE2 1 
ATOM   3922 N N   . VAL A 1 463 ? -4.781  23.372 89.195  1.00 16.45 ? 463 VAL A N   1 
ATOM   3923 C CA  . VAL A 1 463 ? -5.192  21.987 88.992  1.00 15.43 ? 463 VAL A CA  1 
ATOM   3924 C C   . VAL A 1 463 ? -4.150  21.219 88.182  1.00 15.91 ? 463 VAL A C   1 
ATOM   3925 O O   . VAL A 1 463 ? -3.829  20.058 88.489  1.00 15.12 ? 463 VAL A O   1 
ATOM   3926 C CB  . VAL A 1 463 ? -6.580  21.921 88.329  1.00 18.45 ? 463 VAL A CB  1 
ATOM   3927 C CG1 . VAL A 1 463 ? -7.016  20.469 88.185  1.00 23.48 ? 463 VAL A CG1 1 
ATOM   3928 C CG2 . VAL A 1 463 ? -7.598  22.711 89.139  1.00 18.99 ? 463 VAL A CG2 1 
ATOM   3929 N N   . PHE A 1 464 ? -3.606  21.835 87.127  1.00 14.44 ? 464 PHE A N   1 
ATOM   3930 C CA  . PHE A 1 464 ? -2.546  21.176 86.377  1.00 13.93 ? 464 PHE A CA  1 
ATOM   3931 C C   . PHE A 1 464 ? -1.346  20.881 87.268  1.00 14.75 ? 464 PHE A C   1 
ATOM   3932 O O   . PHE A 1 464 ? -0.694  19.834 87.127  1.00 13.75 ? 464 PHE A O   1 
ATOM   3933 C CB  . PHE A 1 464 ? -2.133  22.032 85.177  1.00 17.01 ? 464 PHE A CB  1 
ATOM   3934 C CG  . PHE A 1 464 ? -3.182  22.099 84.106  1.00 12.41 ? 464 PHE A CG  1 
ATOM   3935 C CD1 . PHE A 1 464 ? -4.160  23.078 84.143  1.00 15.44 ? 464 PHE A CD1 1 
ATOM   3936 C CD2 . PHE A 1 464 ? -3.198  21.176 83.075  1.00 14.55 ? 464 PHE A CD2 1 
ATOM   3937 C CE1 . PHE A 1 464 ? -5.138  23.140 83.168  1.00 17.39 ? 464 PHE A CE1 1 
ATOM   3938 C CE2 . PHE A 1 464 ? -4.168  21.234 82.094  1.00 13.19 ? 464 PHE A CE2 1 
ATOM   3939 C CZ  . PHE A 1 464 ? -5.142  22.209 82.137  1.00 13.52 ? 464 PHE A CZ  1 
ATOM   3940 N N   . ASP A 1 465 ? -1.041  21.789 88.198  1.00 13.67 ? 465 ASP A N   1 
ATOM   3941 C CA  . ASP A 1 465 ? 0.090   21.575 89.095  1.00 13.02 ? 465 ASP A CA  1 
ATOM   3942 C C   . ASP A 1 465 ? -0.194  20.441 90.080  1.00 13.19 ? 465 ASP A C   1 
ATOM   3943 O O   . ASP A 1 465 ? 0.690   19.617 90.356  1.00 15.00 ? 465 ASP A O   1 
ATOM   3944 C CB  . ASP A 1 465 ? 0.404   22.881 89.819  1.00 13.27 ? 465 ASP A CB  1 
ATOM   3945 C CG  . ASP A 1 465 ? 1.428   22.711 90.897  1.00 16.10 ? 465 ASP A CG  1 
ATOM   3946 O OD1 . ASP A 1 465 ? 2.642   22.681 90.553  1.00 17.00 ? 465 ASP A OD1 1 
ATOM   3947 O OD2 . ASP A 1 465 ? 1.018   22.612 92.077  1.00 18.68 ? 465 ASP A OD2 1 
ATOM   3948 N N   . LYS A 1 466 ? -1.427  20.368 90.596  1.00 13.38 ? 466 LYS A N   1 
ATOM   3949 C CA  . LYS A 1 466 ? -1.833  19.239 91.441  1.00 13.03 ? 466 LYS A CA  1 
ATOM   3950 C C   . LYS A 1 466 ? -1.730  17.913 90.692  1.00 12.37 ? 466 LYS A C   1 
ATOM   3951 O O   . LYS A 1 466 ? -1.236  16.918 91.236  1.00 15.88 ? 466 LYS A O   1 
ATOM   3952 C CB  . LYS A 1 466 ? -3.268  19.445 91.949  1.00 16.25 ? 466 LYS A CB  1 
ATOM   3953 C CG  . LYS A 1 466 ? -3.814  18.237 92.727  1.00 15.75 ? 466 LYS A CG  1 
ATOM   3954 C CD  . LYS A 1 466 ? -5.193  18.512 93.333  1.00 25.10 ? 466 LYS A CD  1 
ATOM   3955 C CE  . LYS A 1 466 ? -5.337  17.802 94.672  1.00 44.00 ? 466 LYS A CE  1 
ATOM   3956 N NZ  . LYS A 1 466 ? -6.222  16.606 94.593  1.00 50.67 ? 466 LYS A NZ  1 
ATOM   3957 N N   . LEU A 1 467 ? -2.177  17.885 89.434  1.00 11.89 ? 467 LEU A N   1 
ATOM   3958 C CA  . LEU A 1 467 ? -2.080  16.668 88.632  1.00 11.01 ? 467 LEU A CA  1 
ATOM   3959 C C   . LEU A 1 467 ? -0.628  16.273 88.402  1.00 12.42 ? 467 LEU A C   1 
ATOM   3960 O O   . LEU A 1 467 ? -0.236  15.135 88.679  1.00 14.90 ? 467 LEU A O   1 
ATOM   3961 C CB  . LEU A 1 467 ? -2.805  16.855 87.298  1.00 9.57  ? 467 LEU A CB  1 
ATOM   3962 C CG  . LEU A 1 467 ? -4.332  16.849 87.466  1.00 11.50 ? 467 LEU A CG  1 
ATOM   3963 C CD1 . LEU A 1 467 ? -4.977  17.364 86.175  1.00 13.06 ? 467 LEU A CD1 1 
ATOM   3964 C CD2 . LEU A 1 467 ? -4.827  15.444 87.782  1.00 14.10 ? 467 LEU A CD2 1 
ATOM   3965 N N   . PHE A 1 468 ? 0.188   17.198 87.880  1.00 10.59 ? 468 PHE A N   1 
ATOM   3966 C CA  . PHE A 1 468 ? 1.589   16.876 87.627  1.00 11.55 ? 468 PHE A CA  1 
ATOM   3967 C C   . PHE A 1 468 ? 2.252   16.305 88.873  1.00 11.95 ? 468 PHE A C   1 
ATOM   3968 O O   . PHE A 1 468 ? 2.856   15.224 88.832  1.00 13.67 ? 468 PHE A O   1 
ATOM   3969 C CB  . PHE A 1 468 ? 2.338   18.115 87.150  1.00 10.43 ? 468 PHE A CB  1 
ATOM   3970 C CG  . PHE A 1 468 ? 3.829   17.935 87.072  1.00 7.49  ? 468 PHE A CG  1 
ATOM   3971 C CD1 . PHE A 1 468 ? 4.404   17.198 86.033  1.00 11.27 ? 468 PHE A CD1 1 
ATOM   3972 C CD2 . PHE A 1 468 ? 4.652   18.492 88.028  1.00 9.74  ? 468 PHE A CD2 1 
ATOM   3973 C CE1 . PHE A 1 468 ? 5.791   17.034 85.950  1.00 12.04 ? 468 PHE A CE1 1 
ATOM   3974 C CE2 . PHE A 1 468 ? 6.064   18.334 87.944  1.00 14.56 ? 468 PHE A CE2 1 
ATOM   3975 C CZ  . PHE A 1 468 ? 6.620   17.614 86.896  1.00 14.19 ? 468 PHE A CZ  1 
ATOM   3976 N N   . ARG A 1 469 ? 2.131   17.011 89.994  1.00 12.15 ? 469 ARG A N   1 
ATOM   3977 C CA  . ARG A 1 469 ? 2.801   16.570 91.208  1.00 11.94 ? 469 ARG A CA  1 
ATOM   3978 C C   . ARG A 1 469 ? 2.217   15.271 91.754  1.00 14.85 ? 469 ARG A C   1 
ATOM   3979 O O   . ARG A 1 469 ? 2.950   14.480 92.364  1.00 15.48 ? 469 ARG A O   1 
ATOM   3980 C CB  . ARG A 1 469 ? 2.750   17.684 92.243  1.00 15.00 ? 469 ARG A CB  1 
ATOM   3981 C CG  . ARG A 1 469 ? 3.627   18.873 91.831  1.00 15.88 ? 469 ARG A CG  1 
ATOM   3982 C CD  . ARG A 1 469 ? 3.517   19.977 92.835  1.00 19.85 ? 469 ARG A CD  1 
ATOM   3983 N NE  . ARG A 1 469 ? 4.256   21.180 92.452  1.00 16.11 ? 469 ARG A NE  1 
ATOM   3984 C CZ  . ARG A 1 469 ? 5.496   21.459 92.837  1.00 17.75 ? 469 ARG A CZ  1 
ATOM   3985 N NH1 . ARG A 1 469 ? 6.175   20.608 93.613  1.00 16.96 ? 469 ARG A NH1 1 
ATOM   3986 N NH2 . ARG A 1 469 ? 6.056   22.603 92.469  1.00 17.50 ? 469 ARG A NH2 1 
ATOM   3987 N N   . SER A 1 470 ? 0.918   15.025 91.543  1.00 16.03 ? 470 SER A N   1 
ATOM   3988 C CA  . SER A 1 470 ? 0.334   13.755 91.968  1.00 14.44 ? 470 SER A CA  1 
ATOM   3989 C C   . SER A 1 470 ? 0.866   12.596 91.134  1.00 13.05 ? 470 SER A C   1 
ATOM   3990 O O   . SER A 1 470 ? 1.158   11.515 91.667  1.00 15.65 ? 470 SER A O   1 
ATOM   3991 C CB  . SER A 1 470 ? -1.196  13.817 91.882  1.00 18.03 ? 470 SER A CB  1 
ATOM   3992 O OG  . SER A 1 470 ? -1.693  14.797 92.765  1.00 21.14 ? 470 SER A OG  1 
ATOM   3993 N N   . PHE A 1 471 ? 0.970   12.794 89.820  1.00 13.32 ? 471 PHE A N   1 
ATOM   3994 C CA  . PHE A 1 471 ? 1.556   11.778 88.956  1.00 12.64 ? 471 PHE A CA  1 
ATOM   3995 C C   . PHE A 1 471 ? 3.012   11.512 89.331  1.00 14.13 ? 471 PHE A C   1 
ATOM   3996 O O   . PHE A 1 471 ? 3.455   10.361 89.361  1.00 15.45 ? 471 PHE A O   1 
ATOM   3997 C CB  . PHE A 1 471 ? 1.433   12.223 87.493  1.00 9.78  ? 471 PHE A CB  1 
ATOM   3998 C CG  . PHE A 1 471 ? 0.010   12.276 86.991  1.00 12.62 ? 471 PHE A CG  1 
ATOM   3999 C CD1 . PHE A 1 471 ? -0.870  11.234 87.247  1.00 15.91 ? 471 PHE A CD1 1 
ATOM   4000 C CD2 . PHE A 1 471 ? -0.449  13.370 86.272  1.00 13.83 ? 471 PHE A CD2 1 
ATOM   4001 C CE1 . PHE A 1 471 ? -2.192  11.269 86.796  1.00 18.88 ? 471 PHE A CE1 1 
ATOM   4002 C CE2 . PHE A 1 471 ? -1.767  13.414 85.823  1.00 12.63 ? 471 PHE A CE2 1 
ATOM   4003 C CZ  . PHE A 1 471 ? -2.633  12.357 86.073  1.00 17.74 ? 471 PHE A CZ  1 
ATOM   4004 N N   . VAL A 1 472 ? 3.771   12.568 89.628  1.00 10.56 ? 472 VAL A N   1 
ATOM   4005 C CA  . VAL A 1 472 ? 5.159   12.403 90.049  1.00 11.99 ? 472 VAL A CA  1 
ATOM   4006 C C   . VAL A 1 472 ? 5.228   11.596 91.344  1.00 13.11 ? 472 VAL A C   1 
ATOM   4007 O O   . VAL A 1 472 ? 6.065   10.693 91.496  1.00 16.96 ? 472 VAL A O   1 
ATOM   4008 C CB  . VAL A 1 472 ? 5.814   13.789 90.203  1.00 17.14 ? 472 VAL A CB  1 
ATOM   4009 C CG1 . VAL A 1 472 ? 7.069   13.697 91.024  1.00 22.15 ? 472 VAL A CG1 1 
ATOM   4010 C CG2 . VAL A 1 472 ? 6.100   14.413 88.813  1.00 15.69 ? 472 VAL A CG2 1 
ATOM   4011 N N   . ARG A 1 473 ? 4.334   11.896 92.290  1.00 15.30 ? 473 ARG A N   1 
ATOM   4012 C CA  . ARG A 1 473 ? 4.309   11.161 93.547  1.00 17.94 ? 473 ARG A CA  1 
ATOM   4013 C C   . ARG A 1 473 ? 3.966   9.696  93.305  1.00 18.72 ? 473 ARG A C   1 
ATOM   4014 O O   . ARG A 1 473 ? 4.651   8.789  93.798  1.00 19.98 ? 473 ARG A O   1 
ATOM   4015 C CB  . ARG A 1 473 ? 3.295   11.816 94.492  1.00 24.01 ? 473 ARG A CB  1 
ATOM   4016 C CG  . ARG A 1 473 ? 3.300   11.327 95.933  1.00 33.63 ? 473 ARG A CG  1 
ATOM   4017 C CD  . ARG A 1 473 ? 2.579   12.335 96.852  1.00 42.98 ? 473 ARG A CD  1 
ATOM   4018 N NE  . ARG A 1 473 ? 1.209   12.648 96.432  1.00 53.93 ? 473 ARG A NE  1 
ATOM   4019 C CZ  . ARG A 1 473 ? 0.816   13.822 95.936  1.00 56.17 ? 473 ARG A CZ  1 
ATOM   4020 N NH1 . ARG A 1 473 ? -0.453  14.007 95.591  1.00 49.82 ? 473 ARG A NH1 1 
ATOM   4021 N NH2 . ARG A 1 473 ? 1.688   14.813 95.784  1.00 58.10 ? 473 ARG A NH2 1 
ATOM   4022 N N   . ARG A 1 474 ? 2.911   9.450  92.525  1.00 17.06 ? 474 ARG A N   1 
ATOM   4023 C CA  . ARG A 1 474 ? 2.454   8.085  92.293  1.00 19.02 ? 474 ARG A CA  1 
ATOM   4024 C C   . ARG A 1 474 ? 3.500   7.266  91.545  1.00 20.37 ? 474 ARG A C   1 
ATOM   4025 O O   . ARG A 1 474 ? 3.604   6.053  91.763  1.00 19.72 ? 474 ARG A O   1 
ATOM   4026 C CB  . ARG A 1 474 ? 1.131   8.116  91.526  1.00 19.91 ? 474 ARG A CB  1 
ATOM   4027 C CG  . ARG A 1 474 ? 0.526   6.744  91.269  1.00 25.89 ? 474 ARG A CG  1 
ATOM   4028 C CD  . ARG A 1 474 ? 0.001   6.095  92.527  1.00 38.60 ? 474 ARG A CD  1 
ATOM   4029 N NE  . ARG A 1 474 ? -0.618  4.811  92.216  1.00 46.44 ? 474 ARG A NE  1 
ATOM   4030 C CZ  . ARG A 1 474 ? 0.059   3.678  92.053  1.00 59.02 ? 474 ARG A CZ  1 
ATOM   4031 N NH1 . ARG A 1 474 ? 1.381   3.665  92.181  1.00 58.09 ? 474 ARG A NH1 1 
ATOM   4032 N NH2 . ARG A 1 474 ? -0.585  2.555  91.764  1.00 66.02 ? 474 ARG A NH2 1 
ATOM   4033 N N   . ALA A 1 475 ? 4.293   7.915  90.683  1.00 16.30 ? 475 ALA A N   1 
ATOM   4034 C CA  . ALA A 1 475 ? 5.310   7.205  89.908  1.00 16.46 ? 475 ALA A CA  1 
ATOM   4035 C C   . ALA A 1 475 ? 6.355   6.551  90.791  1.00 19.17 ? 475 ALA A C   1 
ATOM   4036 O O   . ALA A 1 475 ? 7.049   5.641  90.333  1.00 23.37 ? 475 ALA A O   1 
ATOM   4037 C CB  . ALA A 1 475 ? 6.005   8.154  88.930  1.00 17.08 ? 475 ALA A CB  1 
ATOM   4038 N N   . GLN A 1 476 ? 6.489   6.985  92.042  1.00 18.43 ? 476 GLN A N   1 
ATOM   4039 C CA  . GLN A 1 476 ? 7.547   6.486  92.906  1.00 20.73 ? 476 GLN A CA  1 
ATOM   4040 C C   . GLN A 1 476 ? 7.050   5.424  93.872  1.00 29.52 ? 476 GLN A C   1 
ATOM   4041 O O   . GLN A 1 476 ? 7.804   4.991  94.751  1.00 31.98 ? 476 GLN A O   1 
ATOM   4042 C CB  . GLN A 1 476 ? 8.192   7.654  93.654  1.00 24.95 ? 476 GLN A CB  1 
ATOM   4043 C CG  . GLN A 1 476 ? 8.803   8.686  92.695  1.00 25.49 ? 476 GLN A CG  1 
ATOM   4044 C CD  . GLN A 1 476 ? 9.207   9.974  93.386  1.00 27.55 ? 476 GLN A CD  1 
ATOM   4045 O OE1 . GLN A 1 476 ? 10.263  10.048 94.022  1.00 26.84 ? 476 GLN A OE1 1 
ATOM   4046 N NE2 . GLN A 1 476 ? 8.365   10.998 93.270  1.00 20.03 ? 476 GLN A NE2 1 
ATOM   4047 N N   . GLU A 1 477 ? 5.808   4.980  93.710  1.00 26.79 ? 477 GLU A N   1 
ATOM   4048 C CA  . GLU A 1 477 ? 5.212   3.963  94.566  1.00 34.04 ? 477 GLU A CA  1 
ATOM   4049 C C   . GLU A 1 477 ? 4.893   2.697  93.776  1.00 33.90 ? 477 GLU A C   1 
ATOM   4050 O O   . GLU A 1 477 ? 4.803   1.602  94.352  1.00 35.18 ? 477 GLU A O   1 
ATOM   4051 C CB  . GLU A 1 477 ? 3.939   4.502  95.224  1.00 37.39 ? 477 GLU A CB  1 
ATOM   4052 C CG  . GLU A 1 477 ? 4.106   5.870  95.867  1.00 43.08 ? 477 GLU A CG  1 
ATOM   4053 C CD  . GLU A 1 477 ? 2.792   6.447  96.364  1.00 54.43 ? 477 GLU A CD  1 
ATOM   4054 O OE1 . GLU A 1 477 ? 2.817   7.283  97.293  1.00 57.73 ? 477 GLU A OE1 1 
ATOM   4055 O OE2 . GLU A 1 477 ? 1.731   6.063  95.825  1.00 58.54 ? 477 GLU A OE2 1 
ATOM   4056 N N   . LYS B 1 2   ? -27.928 41.190 60.539  1.00 35.94 ? 2   LYS B N   1 
ATOM   4057 C CA  . LYS B 1 2   ? -29.017 41.357 59.579  1.00 30.98 ? 2   LYS B CA  1 
ATOM   4058 C C   . LYS B 1 2   ? -28.454 41.633 58.186  1.00 26.00 ? 2   LYS B C   1 
ATOM   4059 O O   . LYS B 1 2   ? -27.750 42.613 57.981  1.00 31.23 ? 2   LYS B O   1 
ATOM   4060 C CB  . LYS B 1 2   ? -29.945 42.495 60.015  1.00 35.82 ? 2   LYS B CB  1 
ATOM   4061 C CG  . LYS B 1 2   ? -31.203 42.635 59.184  1.00 39.64 ? 2   LYS B CG  1 
ATOM   4062 C CD  . LYS B 1 2   ? -31.327 44.025 58.575  1.00 49.33 ? 2   LYS B CD  1 
ATOM   4063 C CE  . LYS B 1 2   ? -31.509 45.088 59.639  1.00 51.28 ? 2   LYS B CE  1 
ATOM   4064 N NZ  . LYS B 1 2   ? -31.835 46.414 59.046  1.00 54.07 ? 2   LYS B NZ  1 
ATOM   4065 N N   . LYS B 1 3   ? -28.765 40.765 57.233  1.00 18.11 ? 3   LYS B N   1 
ATOM   4066 C CA  . LYS B 1 3   ? -28.217 40.862 55.891  1.00 17.37 ? 3   LYS B CA  1 
ATOM   4067 C C   . LYS B 1 3   ? -29.239 41.435 54.920  1.00 19.52 ? 3   LYS B C   1 
ATOM   4068 O O   . LYS B 1 3   ? -30.453 41.348 55.134  1.00 22.17 ? 3   LYS B O   1 
ATOM   4069 C CB  . LYS B 1 3   ? -27.767 39.484 55.394  1.00 23.53 ? 3   LYS B CB  1 
ATOM   4070 C CG  . LYS B 1 3   ? -26.825 38.742 56.339  1.00 29.71 ? 3   LYS B CG  1 
ATOM   4071 C CD  . LYS B 1 3   ? -25.376 39.087 56.061  1.00 36.06 ? 3   LYS B CD  1 
ATOM   4072 C CE  . LYS B 1 3   ? -24.442 38.275 56.944  1.00 38.73 ? 3   LYS B CE  1 
ATOM   4073 N NZ  . LYS B 1 3   ? -23.406 39.139 57.571  1.00 46.07 ? 3   LYS B NZ  1 
ATOM   4074 N N   . LEU B 1 4   ? -28.728 42.039 53.855  1.00 15.29 ? 4   LEU B N   1 
ATOM   4075 C CA  . LEU B 1 4   ? -29.481 42.237 52.624  1.00 15.89 ? 4   LEU B CA  1 
ATOM   4076 C C   . LEU B 1 4   ? -29.095 41.117 51.670  1.00 17.98 ? 4   LEU B C   1 
ATOM   4077 O O   . LEU B 1 4   ? -27.905 40.861 51.459  1.00 17.10 ? 4   LEU B O   1 
ATOM   4078 C CB  . LEU B 1 4   ? -29.187 43.601 51.993  1.00 15.04 ? 4   LEU B CB  1 
ATOM   4079 C CG  . LEU B 1 4   ? -29.870 43.945 50.665  1.00 16.40 ? 4   LEU B CG  1 
ATOM   4080 C CD1 . LEU B 1 4   ? -30.164 45.444 50.592  1.00 20.00 ? 4   LEU B CD1 1 
ATOM   4081 C CD2 . LEU B 1 4   ? -29.033 43.492 49.467  1.00 12.94 ? 4   LEU B CD2 1 
ATOM   4082 N N   . PHE B 1 5   ? -30.093 40.443 51.112  1.00 14.83 ? 5   PHE B N   1 
ATOM   4083 C CA  . PHE B 1 5   ? -29.865 39.379 50.146  1.00 14.94 ? 5   PHE B CA  1 
ATOM   4084 C C   . PHE B 1 5   ? -30.012 39.954 48.746  1.00 16.40 ? 5   PHE B C   1 
ATOM   4085 O O   . PHE B 1 5   ? -31.065 40.502 48.406  1.00 17.89 ? 5   PHE B O   1 
ATOM   4086 C CB  . PHE B 1 5   ? -30.840 38.227 50.371  1.00 13.55 ? 5   PHE B CB  1 
ATOM   4087 C CG  . PHE B 1 5   ? -30.646 37.540 51.682  1.00 15.77 ? 5   PHE B CG  1 
ATOM   4088 C CD1 . PHE B 1 5   ? -29.401 37.016 52.020  1.00 15.84 ? 5   PHE B CD1 1 
ATOM   4089 C CD2 . PHE B 1 5   ? -31.682 37.437 52.584  1.00 17.64 ? 5   PHE B CD2 1 
ATOM   4090 C CE1 . PHE B 1 5   ? -29.207 36.381 53.242  1.00 17.06 ? 5   PHE B CE1 1 
ATOM   4091 C CE2 . PHE B 1 5   ? -31.496 36.805 53.808  1.00 17.01 ? 5   PHE B CE2 1 
ATOM   4092 C CZ  . PHE B 1 5   ? -30.252 36.284 54.140  1.00 18.83 ? 5   PHE B CZ  1 
ATOM   4093 N N   . LEU B 1 6   ? -28.965 39.807 47.940  1.00 13.76 ? 6   LEU B N   1 
ATOM   4094 C CA  . LEU B 1 6   ? -28.884 40.401 46.614  1.00 13.82 ? 6   LEU B CA  1 
ATOM   4095 C C   . LEU B 1 6   ? -28.852 39.283 45.588  1.00 13.00 ? 6   LEU B C   1 
ATOM   4096 O O   . LEU B 1 6   ? -28.038 38.363 45.709  1.00 14.29 ? 6   LEU B O   1 
ATOM   4097 C CB  . LEU B 1 6   ? -27.630 41.273 46.503  1.00 14.14 ? 6   LEU B CB  1 
ATOM   4098 C CG  . LEU B 1 6   ? -27.431 42.034 45.180  1.00 13.31 ? 6   LEU B CG  1 
ATOM   4099 C CD1 . LEU B 1 6   ? -28.621 42.978 44.923  1.00 16.62 ? 6   LEU B CD1 1 
ATOM   4100 C CD2 . LEU B 1 6   ? -26.123 42.816 45.249  1.00 14.57 ? 6   LEU B CD2 1 
ATOM   4101 N N   . VAL B 1 7   ? -29.747 39.336 44.607  1.00 10.73 ? 7   VAL B N   1 
ATOM   4102 C CA  . VAL B 1 7   ? -29.868 38.260 43.616  1.00 10.21 ? 7   VAL B CA  1 
ATOM   4103 C C   . VAL B 1 7   ? -29.753 38.872 42.225  1.00 14.46 ? 7   VAL B C   1 
ATOM   4104 O O   . VAL B 1 7   ? -30.667 39.577 41.778  1.00 16.50 ? 7   VAL B O   1 
ATOM   4105 C CB  . VAL B 1 7   ? -31.187 37.489 43.755  1.00 10.56 ? 7   VAL B CB  1 
ATOM   4106 C CG1 . VAL B 1 7   ? -31.167 36.258 42.837  1.00 14.18 ? 7   VAL B CG1 1 
ATOM   4107 C CG2 . VAL B 1 7   ? -31.410 37.067 45.216  1.00 13.72 ? 7   VAL B CG2 1 
ATOM   4108 N N   . PHE B 1 8   ? -28.643 38.603 41.539  1.00 13.47 ? 8   PHE B N   1 
ATOM   4109 C CA  . PHE B 1 8   ? -28.489 38.997 40.140  1.00 14.14 ? 8   PHE B CA  1 
ATOM   4110 C C   . PHE B 1 8   ? -29.043 37.886 39.265  1.00 13.04 ? 8   PHE B C   1 
ATOM   4111 O O   . PHE B 1 8   ? -28.687 36.723 39.448  1.00 15.18 ? 8   PHE B O   1 
ATOM   4112 C CB  . PHE B 1 8   ? -27.022 39.218 39.764  1.00 10.26 ? 8   PHE B CB  1 
ATOM   4113 C CG  . PHE B 1 8   ? -26.433 40.469 40.326  1.00 14.89 ? 8   PHE B CG  1 
ATOM   4114 C CD1 . PHE B 1 8   ? -26.561 41.675 39.649  1.00 15.21 ? 8   PHE B CD1 1 
ATOM   4115 C CD2 . PHE B 1 8   ? -25.751 40.438 41.534  1.00 15.48 ? 8   PHE B CD2 1 
ATOM   4116 C CE1 . PHE B 1 8   ? -26.014 42.834 40.178  1.00 16.04 ? 8   PHE B CE1 1 
ATOM   4117 C CE2 . PHE B 1 8   ? -25.193 41.580 42.054  1.00 15.82 ? 8   PHE B CE2 1 
ATOM   4118 C CZ  . PHE B 1 8   ? -25.326 42.779 41.382  1.00 16.72 ? 8   PHE B CZ  1 
ATOM   4119 N N   . TRP B 1 9   ? -29.859 38.249 38.277  1.00 11.19 ? 9   TRP B N   1 
ATOM   4120 C CA  . TRP B 1 9   ? -30.389 37.272 37.325  1.00 12.21 ? 9   TRP B CA  1 
ATOM   4121 C C   . TRP B 1 9   ? -30.218 37.888 35.943  1.00 15.77 ? 9   TRP B C   1 
ATOM   4122 O O   . TRP B 1 9   ? -30.984 38.766 35.544  1.00 13.36 ? 9   TRP B O   1 
ATOM   4123 C CB  . TRP B 1 9   ? -31.835 36.944 37.633  1.00 11.73 ? 9   TRP B CB  1 
ATOM   4124 C CG  . TRP B 1 9   ? -32.376 35.715 37.020  1.00 10.74 ? 9   TRP B CG  1 
ATOM   4125 C CD1 . TRP B 1 9   ? -31.794 34.913 36.075  1.00 12.67 ? 9   TRP B CD1 1 
ATOM   4126 C CD2 . TRP B 1 9   ? -33.654 35.150 37.300  1.00 13.64 ? 9   TRP B CD2 1 
ATOM   4127 N NE1 . TRP B 1 9   ? -32.638 33.861 35.767  1.00 13.31 ? 9   TRP B NE1 1 
ATOM   4128 C CE2 . TRP B 1 9   ? -33.788 33.994 36.505  1.00 14.45 ? 9   TRP B CE2 1 
ATOM   4129 C CE3 . TRP B 1 9   ? -34.693 35.500 38.169  1.00 14.57 ? 9   TRP B CE3 1 
ATOM   4130 C CZ2 . TRP B 1 9   ? -34.932 33.192 36.548  1.00 14.99 ? 9   TRP B CZ2 1 
ATOM   4131 C CZ3 . TRP B 1 9   ? -35.817 34.711 38.211  1.00 17.34 ? 9   TRP B CZ3 1 
ATOM   4132 C CH2 . TRP B 1 9   ? -35.932 33.569 37.405  1.00 13.00 ? 9   TRP B CH2 1 
ATOM   4133 N N   . TRP B 1 10  ? -29.196 37.446 35.229  1.00 11.79 ? 10  TRP B N   1 
ATOM   4134 C CA  . TRP B 1 10  ? -28.836 38.020 33.941  1.00 11.47 ? 10  TRP B CA  1 
ATOM   4135 C C   . TRP B 1 10  ? -29.511 37.222 32.833  1.00 12.33 ? 10  TRP B C   1 
ATOM   4136 O O   . TRP B 1 10  ? -29.215 36.033 32.658  1.00 13.33 ? 10  TRP B O   1 
ATOM   4137 C CB  . TRP B 1 10  ? -27.326 37.978 33.745  1.00 9.97  ? 10  TRP B CB  1 
ATOM   4138 C CG  . TRP B 1 10  ? -26.500 38.754 34.746  1.00 10.62 ? 10  TRP B CG  1 
ATOM   4139 C CD1 . TRP B 1 10  ? -25.646 38.243 35.686  1.00 11.82 ? 10  TRP B CD1 1 
ATOM   4140 C CD2 . TRP B 1 10  ? -26.374 40.179 34.825  1.00 13.90 ? 10  TRP B CD2 1 
ATOM   4141 N NE1 . TRP B 1 10  ? -25.038 39.262 36.378  1.00 13.46 ? 10  TRP B NE1 1 
ATOM   4142 C CE2 . TRP B 1 10  ? -25.463 40.460 35.864  1.00 13.77 ? 10  TRP B CE2 1 
ATOM   4143 C CE3 . TRP B 1 10  ? -26.969 41.244 34.130  1.00 12.26 ? 10  TRP B CE3 1 
ATOM   4144 C CZ2 . TRP B 1 10  ? -25.110 41.770 36.220  1.00 16.15 ? 10  TRP B CZ2 1 
ATOM   4145 C CZ3 . TRP B 1 10  ? -26.620 42.540 34.477  1.00 13.46 ? 10  TRP B CZ3 1 
ATOM   4146 C CH2 . TRP B 1 10  ? -25.704 42.791 35.524  1.00 15.64 ? 10  TRP B CH2 1 
ATOM   4147 N N   . HIS B 1 11  ? -30.360 37.882 32.050  1.00 10.01 ? 11  HIS B N   1 
ATOM   4148 C CA  . HIS B 1 11  ? -31.173 37.201 31.047  1.00 10.27 ? 11  HIS B CA  1 
ATOM   4149 C C   . HIS B 1 11  ? -30.506 37.310 29.677  1.00 12.13 ? 11  HIS B C   1 
ATOM   4150 O O   . HIS B 1 11  ? -30.206 38.412 29.213  1.00 14.27 ? 11  HIS B O   1 
ATOM   4151 C CB  . HIS B 1 11  ? -32.598 37.783 31.043  1.00 15.37 ? 11  HIS B CB  1 
ATOM   4152 C CG  . HIS B 1 11  ? -33.380 37.513 29.789  1.00 15.06 ? 11  HIS B CG  1 
ATOM   4153 N ND1 . HIS B 1 11  ? -33.775 36.248 29.401  1.00 14.43 ? 11  HIS B ND1 1 
ATOM   4154 C CD2 . HIS B 1 11  ? -33.834 38.358 28.829  1.00 14.00 ? 11  HIS B CD2 1 
ATOM   4155 C CE1 . HIS B 1 11  ? -34.431 36.326 28.254  1.00 13.22 ? 11  HIS B CE1 1 
ATOM   4156 N NE2 . HIS B 1 11  ? -34.479 37.595 27.886  1.00 14.09 ? 11  HIS B NE2 1 
ATOM   4157 N N   . MET B 1 12  ? -30.285 36.162 29.038  1.00 12.24 ? 12  MET B N   1 
ATOM   4158 C CA  . MET B 1 12  ? -29.587 36.037 27.761  1.00 13.61 ? 12  MET B CA  1 
ATOM   4159 C C   . MET B 1 12  ? -30.552 35.474 26.728  1.00 14.02 ? 12  MET B C   1 
ATOM   4160 O O   . MET B 1 12  ? -31.146 34.414 26.948  1.00 13.09 ? 12  MET B O   1 
ATOM   4161 C CB  . MET B 1 12  ? -28.374 35.098 27.873  1.00 13.35 ? 12  MET B CB  1 
ATOM   4162 C CG  . MET B 1 12  ? -27.432 35.417 29.043  1.00 11.86 ? 12  MET B CG  1 
ATOM   4163 S SD  . MET B 1 12  ? -26.777 37.089 28.973  1.00 14.35 ? 12  MET B SD  1 
ATOM   4164 C CE  . MET B 1 12  ? -25.398 36.919 30.122  1.00 15.55 ? 12  MET B CE  1 
ATOM   4165 N N   . HIS B 1 13  ? -30.695 36.167 25.599  1.00 10.57 ? 13  HIS B N   1 
ATOM   4166 C CA  . HIS B 1 13  ? -31.659 35.739 24.594  1.00 13.50 ? 13  HIS B CA  1 
ATOM   4167 C C   . HIS B 1 13  ? -31.284 36.317 23.235  1.00 14.24 ? 13  HIS B C   1 
ATOM   4168 O O   . HIS B 1 13  ? -30.801 37.446 23.142  1.00 14.01 ? 13  HIS B O   1 
ATOM   4169 C CB  . HIS B 1 13  ? -33.091 36.179 24.972  1.00 12.07 ? 13  HIS B CB  1 
ATOM   4170 C CG  . HIS B 1 13  ? -34.085 36.022 23.860  1.00 10.98 ? 13  HIS B CG  1 
ATOM   4171 N ND1 . HIS B 1 13  ? -34.328 34.807 23.256  1.00 12.47 ? 13  HIS B ND1 1 
ATOM   4172 C CD2 . HIS B 1 13  ? -34.916 36.912 23.259  1.00 13.70 ? 13  HIS B CD2 1 
ATOM   4173 C CE1 . HIS B 1 13  ? -35.235 34.961 22.309  1.00 14.55 ? 13  HIS B CE1 1 
ATOM   4174 N NE2 . HIS B 1 13  ? -35.618 36.224 22.295  1.00 13.23 ? 13  HIS B NE2 1 
ATOM   4175 N N   . GLN B 1 14  ? -31.533 35.537 22.184  1.00 12.30 ? 14  GLN B N   1 
ATOM   4176 C CA  . GLN B 1 14  ? -31.544 36.038 20.798  1.00 11.20 ? 14  GLN B CA  1 
ATOM   4177 C C   . GLN B 1 14  ? -32.668 35.310 20.083  1.00 13.71 ? 14  GLN B C   1 
ATOM   4178 O O   . GLN B 1 14  ? -32.798 34.086 20.233  1.00 14.82 ? 14  GLN B O   1 
ATOM   4179 C CB  . GLN B 1 14  ? -30.234 35.794 20.019  1.00 13.75 ? 14  GLN B CB  1 
ATOM   4180 C CG  . GLN B 1 14  ? -29.016 36.527 20.563  1.00 15.30 ? 14  GLN B CG  1 
ATOM   4181 C CD  . GLN B 1 14  ? -29.130 38.034 20.432  1.00 17.29 ? 14  GLN B CD  1 
ATOM   4182 O OE1 . GLN B 1 14  ? -29.849 38.555 19.570  1.00 15.60 ? 14  GLN B OE1 1 
ATOM   4183 N NE2 . GLN B 1 14  ? -28.428 38.744 21.301  1.00 12.34 ? 14  GLN B NE2 1 
ATOM   4184 N N   . PRO B 1 15  ? -33.467 36.018 19.280  1.00 14.08 ? 15  PRO B N   1 
ATOM   4185 C CA  . PRO B 1 15  ? -34.419 35.337 18.396  1.00 15.52 ? 15  PRO B CA  1 
ATOM   4186 C C   . PRO B 1 15  ? -33.670 34.574 17.311  1.00 17.34 ? 15  PRO B C   1 
ATOM   4187 O O   . PRO B 1 15  ? -32.468 34.751 17.100  1.00 17.28 ? 15  PRO B O   1 
ATOM   4188 C CB  . PRO B 1 15  ? -35.251 36.491 17.815  1.00 15.81 ? 15  PRO B CB  1 
ATOM   4189 C CG  . PRO B 1 15  ? -34.264 37.648 17.762  1.00 15.00 ? 15  PRO B CG  1 
ATOM   4190 C CD  . PRO B 1 15  ? -33.425 37.472 19.043  1.00 16.22 ? 15  PRO B CD  1 
ATOM   4191 N N   . LEU B 1 16  ? -34.394 33.713 16.603  1.00 19.03 ? 16  LEU B N   1 
ATOM   4192 C CA  . LEU B 1 16  ? -33.756 32.845 15.622  1.00 15.61 ? 16  LEU B CA  1 
ATOM   4193 C C   . LEU B 1 16  ? -33.455 33.640 14.352  1.00 16.35 ? 16  LEU B C   1 
ATOM   4194 O O   . LEU B 1 16  ? -34.368 33.994 13.599  1.00 19.23 ? 16  LEU B O   1 
ATOM   4195 C CB  . LEU B 1 16  ? -34.640 31.636 15.326  1.00 14.45 ? 16  LEU B CB  1 
ATOM   4196 C CG  . LEU B 1 16  ? -33.975 30.596 14.410  1.00 15.19 ? 16  LEU B CG  1 
ATOM   4197 C CD1 . LEU B 1 16  ? -32.648 30.102 15.000  1.00 17.35 ? 16  LEU B CD1 1 
ATOM   4198 C CD2 . LEU B 1 16  ? -34.926 29.422 14.142  1.00 16.37 ? 16  LEU B CD2 1 
ATOM   4199 N N   . TYR B 1 17  ? -32.173 33.915 14.112  1.00 19.80 ? 17  TYR B N   1 
ATOM   4200 C CA  . TYR B 1 17  ? -31.730 34.622 12.914  1.00 15.94 ? 17  TYR B CA  1 
ATOM   4201 C C   . TYR B 1 17  ? -31.582 33.701 11.714  1.00 19.47 ? 17  TYR B C   1 
ATOM   4202 O O   . TYR B 1 17  ? -31.330 34.186 10.608  1.00 20.05 ? 17  TYR B O   1 
ATOM   4203 C CB  . TYR B 1 17  ? -30.402 35.333 13.192  1.00 15.85 ? 17  TYR B CB  1 
ATOM   4204 C CG  . TYR B 1 17  ? -30.497 36.390 14.280  1.00 16.27 ? 17  TYR B CG  1 
ATOM   4205 C CD1 . TYR B 1 17  ? -31.299 37.512 14.101  1.00 15.82 ? 17  TYR B CD1 1 
ATOM   4206 C CD2 . TYR B 1 17  ? -29.778 36.277 15.467  1.00 15.67 ? 17  TYR B CD2 1 
ATOM   4207 C CE1 . TYR B 1 17  ? -31.395 38.500 15.089  1.00 16.62 ? 17  TYR B CE1 1 
ATOM   4208 C CE2 . TYR B 1 17  ? -29.862 37.264 16.460  1.00 15.97 ? 17  TYR B CE2 1 
ATOM   4209 C CZ  . TYR B 1 17  ? -30.685 38.370 16.258  1.00 14.15 ? 17  TYR B CZ  1 
ATOM   4210 O OH  . TYR B 1 17  ? -30.792 39.366 17.220  1.00 16.00 ? 17  TYR B OH  1 
ATOM   4211 N N   . ARG B 1 18  ? -31.763 32.400 11.911  1.00 19.04 ? 18  ARG B N   1 
ATOM   4212 C CA  . ARG B 1 18  ? -31.556 31.390 10.880  1.00 16.83 ? 18  ARG B CA  1 
ATOM   4213 C C   . ARG B 1 18  ? -32.761 31.323 9.944   1.00 17.17 ? 18  ARG B C   1 
ATOM   4214 O O   . ARG B 1 18  ? -33.798 30.751 10.288  1.00 22.13 ? 18  ARG B O   1 
ATOM   4215 C CB  . ARG B 1 18  ? -31.299 30.044 11.554  1.00 18.29 ? 18  ARG B CB  1 
ATOM   4216 C CG  . ARG B 1 18  ? -30.703 28.993 10.629  1.00 25.18 ? 18  ARG B CG  1 
ATOM   4217 C CD  . ARG B 1 18  ? -30.631 27.638 11.320  1.00 27.60 ? 18  ARG B CD  1 
ATOM   4218 N NE  . ARG B 1 18  ? -30.052 26.633 10.439  1.00 29.06 ? 18  ARG B NE  1 
ATOM   4219 C CZ  . ARG B 1 18  ? -30.704 26.025 9.451   1.00 30.57 ? 18  ARG B CZ  1 
ATOM   4220 N NH1 . ARG B 1 18  ? -31.983 26.298 9.207   1.00 31.16 ? 18  ARG B NH1 1 
ATOM   4221 N NH2 . ARG B 1 18  ? -30.077 25.127 8.706   1.00 39.09 ? 18  ARG B NH2 1 
ATOM   4222 N N   . GLU B 1 19  ? -32.610 31.861 8.739   1.00 21.17 ? 19  GLU B N   1 
ATOM   4223 C CA  . GLU B 1 19  ? -33.673 31.796 7.745   1.00 21.58 ? 19  GLU B CA  1 
ATOM   4224 C C   . GLU B 1 19  ? -33.946 30.339 7.371   1.00 24.36 ? 19  GLU B C   1 
ATOM   4225 O O   . GLU B 1 19  ? -33.005 29.599 7.058   1.00 27.71 ? 19  GLU B O   1 
ATOM   4226 C CB  . GLU B 1 19  ? -33.270 32.600 6.510   1.00 26.10 ? 19  GLU B CB  1 
ATOM   4227 C CG  . GLU B 1 19  ? -34.439 33.171 5.741   1.00 29.04 ? 19  GLU B CG  1 
ATOM   4228 C CD  . GLU B 1 19  ? -34.835 32.301 4.572   1.00 39.22 ? 19  GLU B CD  1 
ATOM   4229 O OE1 . GLU B 1 19  ? -34.257 31.207 4.430   1.00 33.98 ? 19  GLU B OE1 1 
ATOM   4230 O OE2 . GLU B 1 19  ? -35.726 32.708 3.802   1.00 47.06 ? 19  GLU B OE2 1 
ATOM   4231 N N   . PRO B 1 20  ? -35.204 29.888 7.392   1.00 27.12 ? 20  PRO B N   1 
ATOM   4232 C CA  . PRO B 1 20  ? -35.460 28.439 7.324   1.00 29.85 ? 20  PRO B CA  1 
ATOM   4233 C C   . PRO B 1 20  ? -35.269 27.823 5.948   1.00 31.81 ? 20  PRO B C   1 
ATOM   4234 O O   . PRO B 1 20  ? -35.015 26.613 5.867   1.00 34.98 ? 20  PRO B O   1 
ATOM   4235 C CB  . PRO B 1 20  ? -36.922 28.317 7.783   1.00 30.91 ? 20  PRO B CB  1 
ATOM   4236 C CG  . PRO B 1 20  ? -37.535 29.639 7.443   1.00 30.05 ? 20  PRO B CG  1 
ATOM   4237 C CD  . PRO B 1 20  ? -36.438 30.667 7.603   1.00 29.37 ? 20  PRO B CD  1 
ATOM   4238 N N   . TYR B 1 21  ? -35.380 28.592 4.869   1.00 30.15 ? 21  TYR B N   1 
ATOM   4239 C CA  . TYR B 1 21  ? -35.227 27.993 3.550   1.00 37.22 ? 21  TYR B CA  1 
ATOM   4240 C C   . TYR B 1 21  ? -33.769 27.934 3.106   1.00 33.76 ? 21  TYR B C   1 
ATOM   4241 O O   . TYR B 1 21  ? -33.346 26.936 2.514   1.00 33.90 ? 21  TYR B O   1 
ATOM   4242 C CB  . TYR B 1 21  ? -36.078 28.753 2.531   1.00 35.96 ? 21  TYR B CB  1 
ATOM   4243 C CG  . TYR B 1 21  ? -37.556 28.608 2.801   1.00 37.34 ? 21  TYR B CG  1 
ATOM   4244 C CD1 . TYR B 1 21  ? -38.278 27.560 2.251   1.00 34.32 ? 21  TYR B CD1 1 
ATOM   4245 C CD2 . TYR B 1 21  ? -38.225 29.502 3.634   1.00 37.28 ? 21  TYR B CD2 1 
ATOM   4246 C CE1 . TYR B 1 21  ? -39.627 27.412 2.504   1.00 33.92 ? 21  TYR B CE1 1 
ATOM   4247 C CE2 . TYR B 1 21  ? -39.575 29.364 3.890   1.00 35.64 ? 21  TYR B CE2 1 
ATOM   4248 C CZ  . TYR B 1 21  ? -40.271 28.314 3.321   1.00 37.20 ? 21  TYR B CZ  1 
ATOM   4249 O OH  . TYR B 1 21  ? -41.616 28.164 3.567   1.00 39.76 ? 21  TYR B OH  1 
ATOM   4250 N N   . THR B 1 22  ? -32.985 28.969 3.406   1.00 27.97 ? 22  THR B N   1 
ATOM   4251 C CA  . THR B 1 22  ? -31.569 28.995 3.061   1.00 30.77 ? 22  THR B CA  1 
ATOM   4252 C C   . THR B 1 22  ? -30.659 28.529 4.189   1.00 30.28 ? 22  THR B C   1 
ATOM   4253 O O   . THR B 1 22  ? -29.500 28.195 3.924   1.00 32.91 ? 22  THR B O   1 
ATOM   4254 C CB  . THR B 1 22  ? -31.142 30.412 2.645   1.00 30.37 ? 22  THR B CB  1 
ATOM   4255 O OG1 . THR B 1 22  ? -31.283 31.305 3.759   1.00 30.17 ? 22  THR B OG1 1 
ATOM   4256 C CG2 . THR B 1 22  ? -31.988 30.912 1.487   1.00 26.92 ? 22  THR B CG2 1 
ATOM   4257 N N   . GLY B 1 23  ? -31.141 28.505 5.433   1.00 25.27 ? 23  GLY B N   1 
ATOM   4258 C CA  . GLY B 1 23  ? -30.268 28.200 6.552   1.00 28.40 ? 23  GLY B CA  1 
ATOM   4259 C C   . GLY B 1 23  ? -29.289 29.295 6.903   1.00 29.94 ? 23  GLY B C   1 
ATOM   4260 O O   . GLY B 1 23  ? -28.434 29.090 7.774   1.00 32.10 ? 23  GLY B O   1 
ATOM   4261 N N   . GLU B 1 24  ? -29.396 30.458 6.264   1.00 26.47 ? 24  GLU B N   1 
ATOM   4262 C CA  . GLU B 1 24  ? -28.474 31.557 6.511   1.00 26.94 ? 24  GLU B CA  1 
ATOM   4263 C C   . GLU B 1 24  ? -28.883 32.316 7.763   1.00 23.35 ? 24  GLU B C   1 
ATOM   4264 O O   . GLU B 1 24  ? -30.063 32.634 7.951   1.00 23.15 ? 24  GLU B O   1 
ATOM   4265 C CB  . GLU B 1 24  ? -28.446 32.521 5.326   1.00 27.59 ? 24  GLU B CB  1 
ATOM   4266 C CG  . GLU B 1 24  ? -28.063 31.891 3.997   1.00 38.97 ? 24  GLU B CG  1 
ATOM   4267 C CD  . GLU B 1 24  ? -27.881 32.928 2.903   1.00 48.34 ? 24  GLU B CD  1 
ATOM   4268 O OE1 . GLU B 1 24  ? -26.733 33.119 2.448   1.00 56.30 ? 24  GLU B OE1 1 
ATOM   4269 O OE2 . GLU B 1 24  ? -28.882 33.565 2.508   1.00 50.87 ? 24  GLU B OE2 1 
ATOM   4270 N N   . TYR B 1 25  ? -27.905 32.601 8.618   1.00 19.08 ? 25  TYR B N   1 
ATOM   4271 C CA  . TYR B 1 25  ? -28.112 33.521 9.728   1.00 17.68 ? 25  TYR B CA  1 
ATOM   4272 C C   . TYR B 1 25  ? -28.067 34.930 9.157   1.00 18.07 ? 25  TYR B C   1 
ATOM   4273 O O   . TYR B 1 25  ? -27.006 35.399 8.728   1.00 19.26 ? 25  TYR B O   1 
ATOM   4274 C CB  . TYR B 1 25  ? -27.054 33.325 10.806  1.00 22.31 ? 25  TYR B CB  1 
ATOM   4275 C CG  . TYR B 1 25  ? -27.367 32.205 11.763  1.00 21.96 ? 25  TYR B CG  1 
ATOM   4276 C CD1 . TYR B 1 25  ? -27.261 30.875 11.365  1.00 24.51 ? 25  TYR B CD1 1 
ATOM   4277 C CD2 . TYR B 1 25  ? -27.760 32.475 13.074  1.00 19.34 ? 25  TYR B CD2 1 
ATOM   4278 C CE1 . TYR B 1 25  ? -27.546 29.844 12.239  1.00 24.20 ? 25  TYR B CE1 1 
ATOM   4279 C CE2 . TYR B 1 25  ? -28.045 31.446 13.951  1.00 21.86 ? 25  TYR B CE2 1 
ATOM   4280 C CZ  . TYR B 1 25  ? -27.933 30.142 13.535  1.00 21.39 ? 25  TYR B CZ  1 
ATOM   4281 O OH  . TYR B 1 25  ? -28.219 29.121 14.414  1.00 26.65 ? 25  TYR B OH  1 
ATOM   4282 N N   . LEU B 1 26  ? -29.222 35.594 9.133   1.00 16.79 ? 26  LEU B N   1 
ATOM   4283 C CA  . LEU B 1 26  ? -29.352 36.860 8.423   1.00 20.86 ? 26  LEU B CA  1 
ATOM   4284 C C   . LEU B 1 26  ? -28.791 38.046 9.189   1.00 21.64 ? 26  LEU B C   1 
ATOM   4285 O O   . LEU B 1 26  ? -28.604 39.109 8.590   1.00 19.56 ? 26  LEU B O   1 
ATOM   4286 C CB  . LEU B 1 26  ? -30.819 37.124 8.099   1.00 17.37 ? 26  LEU B CB  1 
ATOM   4287 C CG  . LEU B 1 26  ? -31.447 36.101 7.174   1.00 17.44 ? 26  LEU B CG  1 
ATOM   4288 C CD1 . LEU B 1 26  ? -32.808 36.602 6.706   1.00 22.12 ? 26  LEU B CD1 1 
ATOM   4289 C CD2 . LEU B 1 26  ? -30.526 35.808 5.992   1.00 23.35 ? 26  LEU B CD2 1 
ATOM   4290 N N   . LEU B 1 27  ? -28.576 37.910 10.493  1.00 17.91 ? 27  LEU B N   1 
ATOM   4291 C CA  . LEU B 1 27  ? -27.901 38.906 11.304  1.00 18.14 ? 27  LEU B CA  1 
ATOM   4292 C C   . LEU B 1 27  ? -26.895 38.198 12.197  1.00 16.93 ? 27  LEU B C   1 
ATOM   4293 O O   . LEU B 1 27  ? -27.090 37.032 12.543  1.00 19.24 ? 27  LEU B O   1 
ATOM   4294 C CB  . LEU B 1 27  ? -28.896 39.697 12.165  1.00 18.32 ? 27  LEU B CB  1 
ATOM   4295 C CG  . LEU B 1 27  ? -29.823 40.642 11.391  1.00 20.66 ? 27  LEU B CG  1 
ATOM   4296 C CD1 . LEU B 1 27  ? -30.956 41.126 12.287  1.00 21.50 ? 27  LEU B CD1 1 
ATOM   4297 C CD2 . LEU B 1 27  ? -29.063 41.828 10.781  1.00 25.14 ? 27  LEU B CD2 1 
ATOM   4298 N N   . PRO B 1 28  ? -25.808 38.877 12.573  1.00 15.25 ? 28  PRO B N   1 
ATOM   4299 C CA  . PRO B 1 28  ? -24.722 38.219 13.309  1.00 14.40 ? 28  PRO B CA  1 
ATOM   4300 C C   . PRO B 1 28  ? -24.776 38.441 14.814  1.00 19.73 ? 28  PRO B C   1 
ATOM   4301 O O   . PRO B 1 28  ? -23.784 38.195 15.506  1.00 16.75 ? 28  PRO B O   1 
ATOM   4302 C CB  . PRO B 1 28  ? -23.481 38.898 12.726  1.00 19.31 ? 28  PRO B CB  1 
ATOM   4303 C CG  . PRO B 1 28  ? -23.949 40.334 12.550  1.00 20.70 ? 28  PRO B CG  1 
ATOM   4304 C CD  . PRO B 1 28  ? -25.432 40.246 12.166  1.00 19.53 ? 28  PRO B CD  1 
ATOM   4305 N N   . TRP B 1 29  ? -25.914 38.909 15.328  1.00 15.90 ? 29  TRP B N   1 
ATOM   4306 C CA  . TRP B 1 29  ? -25.962 39.351 16.722  1.00 15.06 ? 29  TRP B CA  1 
ATOM   4307 C C   . TRP B 1 29  ? -25.711 38.210 17.704  1.00 17.93 ? 29  TRP B C   1 
ATOM   4308 O O   . TRP B 1 29  ? -25.155 38.434 18.783  1.00 16.71 ? 29  TRP B O   1 
ATOM   4309 C CB  . TRP B 1 29  ? -27.309 39.999 17.010  1.00 14.50 ? 29  TRP B CB  1 
ATOM   4310 C CG  . TRP B 1 29  ? -27.583 41.271 16.241  1.00 13.95 ? 29  TRP B CG  1 
ATOM   4311 C CD1 . TRP B 1 29  ? -28.687 41.549 15.480  1.00 15.39 ? 29  TRP B CD1 1 
ATOM   4312 C CD2 . TRP B 1 29  ? -26.753 42.445 16.188  1.00 19.22 ? 29  TRP B CD2 1 
ATOM   4313 N NE1 . TRP B 1 29  ? -28.594 42.819 14.960  1.00 15.96 ? 29  TRP B NE1 1 
ATOM   4314 C CE2 . TRP B 1 29  ? -27.421 43.390 15.383  1.00 16.87 ? 29  TRP B CE2 1 
ATOM   4315 C CE3 . TRP B 1 29  ? -25.520 42.790 16.757  1.00 18.95 ? 29  TRP B CE3 1 
ATOM   4316 C CZ2 . TRP B 1 29  ? -26.897 44.663 15.131  1.00 15.95 ? 29  TRP B CZ2 1 
ATOM   4317 C CZ3 . TRP B 1 29  ? -24.999 44.050 16.506  1.00 20.00 ? 29  TRP B CZ3 1 
ATOM   4318 C CH2 . TRP B 1 29  ? -25.686 44.971 15.691  1.00 15.00 ? 29  TRP B CH2 1 
ATOM   4319 N N   . THR B 1 30  ? -26.134 36.985 17.382  1.00 15.42 ? 30  THR B N   1 
ATOM   4320 C CA  . THR B 1 30  ? -25.802 35.880 18.278  1.00 15.52 ? 30  THR B CA  1 
ATOM   4321 C C   . THR B 1 30  ? -24.297 35.645 18.326  1.00 15.20 ? 30  THR B C   1 
ATOM   4322 O O   . THR B 1 30  ? -23.717 35.485 19.406  1.00 14.61 ? 30  THR B O   1 
ATOM   4323 C CB  . THR B 1 30  ? -26.538 34.610 17.856  1.00 19.09 ? 30  THR B CB  1 
ATOM   4324 O OG1 . THR B 1 30  ? -27.952 34.832 17.935  1.00 16.40 ? 30  THR B OG1 1 
ATOM   4325 C CG2 . THR B 1 30  ? -26.153 33.439 18.767  1.00 21.26 ? 30  THR B CG2 1 
ATOM   4326 N N   . PHE B 1 31  ? -23.639 35.644 17.165  1.00 17.48 ? 31  PHE B N   1 
ATOM   4327 C CA  . PHE B 1 31  ? -22.187 35.514 17.154  1.00 15.12 ? 31  PHE B CA  1 
ATOM   4328 C C   . PHE B 1 31  ? -21.538 36.590 18.016  1.00 14.30 ? 31  PHE B C   1 
ATOM   4329 O O   . PHE B 1 31  ? -20.715 36.288 18.891  1.00 14.61 ? 31  PHE B O   1 
ATOM   4330 C CB  . PHE B 1 31  ? -21.662 35.588 15.717  1.00 15.93 ? 31  PHE B CB  1 
ATOM   4331 C CG  . PHE B 1 31  ? -20.167 35.586 15.623  1.00 18.08 ? 31  PHE B CG  1 
ATOM   4332 C CD1 . PHE B 1 31  ? -19.464 34.396 15.700  1.00 18.04 ? 31  PHE B CD1 1 
ATOM   4333 C CD2 . PHE B 1 31  ? -19.464 36.772 15.468  1.00 16.10 ? 31  PHE B CD2 1 
ATOM   4334 C CE1 . PHE B 1 31  ? -18.074 34.382 15.625  1.00 18.88 ? 31  PHE B CE1 1 
ATOM   4335 C CE2 . PHE B 1 31  ? -18.071 36.772 15.403  1.00 14.74 ? 31  PHE B CE2 1 
ATOM   4336 C CZ  . PHE B 1 31  ? -17.380 35.575 15.477  1.00 17.20 ? 31  PHE B CZ  1 
ATOM   4337 N N   . PHE B 1 32  ? -21.925 37.852 17.811  1.00 13.72 ? 32  PHE B N   1 
ATOM   4338 C CA  . PHE B 1 32  ? -21.201 38.933 18.468  1.00 11.93 ? 32  PHE B CA  1 
ATOM   4339 C C   . PHE B 1 32  ? -21.477 38.973 19.965  1.00 14.80 ? 32  PHE B C   1 
ATOM   4340 O O   . PHE B 1 32  ? -20.567 39.256 20.750  1.00 13.76 ? 32  PHE B O   1 
ATOM   4341 C CB  . PHE B 1 32  ? -21.530 40.263 17.803  1.00 14.73 ? 32  PHE B CB  1 
ATOM   4342 C CG  . PHE B 1 32  ? -20.750 40.495 16.538  1.00 14.70 ? 32  PHE B CG  1 
ATOM   4343 C CD1 . PHE B 1 32  ? -19.366 40.406 16.540  1.00 16.69 ? 32  PHE B CD1 1 
ATOM   4344 C CD2 . PHE B 1 32  ? -21.394 40.784 15.354  1.00 17.40 ? 32  PHE B CD2 1 
ATOM   4345 C CE1 . PHE B 1 32  ? -18.640 40.611 15.371  1.00 20.42 ? 32  PHE B CE1 1 
ATOM   4346 C CE2 . PHE B 1 32  ? -20.681 40.988 14.192  1.00 23.31 ? 32  PHE B CE2 1 
ATOM   4347 C CZ  . PHE B 1 32  ? -19.301 40.907 14.201  1.00 20.73 ? 32  PHE B CZ  1 
ATOM   4348 N N   . HIS B 1 33  ? -22.712 38.683 20.385  1.00 13.85 ? 33  HIS B N   1 
ATOM   4349 C CA  . HIS B 1 33  ? -22.962 38.604 21.826  1.00 15.92 ? 33  HIS B CA  1 
ATOM   4350 C C   . HIS B 1 33  ? -22.397 37.324 22.444  1.00 18.73 ? 33  HIS B C   1 
ATOM   4351 O O   . HIS B 1 33  ? -22.061 37.315 23.632  1.00 15.04 ? 33  HIS B O   1 
ATOM   4352 C CB  . HIS B 1 33  ? -24.457 38.758 22.106  1.00 12.68 ? 33  HIS B CB  1 
ATOM   4353 C CG  . HIS B 1 33  ? -24.918 40.171 21.959  1.00 11.70 ? 33  HIS B CG  1 
ATOM   4354 N ND1 . HIS B 1 33  ? -24.508 41.174 22.815  1.00 14.22 ? 33  HIS B ND1 1 
ATOM   4355 C CD2 . HIS B 1 33  ? -25.691 40.766 21.022  1.00 14.52 ? 33  HIS B CD2 1 
ATOM   4356 C CE1 . HIS B 1 33  ? -25.021 42.324 22.415  1.00 15.85 ? 33  HIS B CE1 1 
ATOM   4357 N NE2 . HIS B 1 33  ? -25.739 42.105 21.327  1.00 13.55 ? 33  HIS B NE2 1 
ATOM   4358 N N   . ALA B 1 34  ? -22.262 36.246 21.673  1.00 14.63 ? 34  ALA B N   1 
ATOM   4359 C CA  . ALA B 1 34  ? -21.599 35.059 22.205  1.00 17.19 ? 34  ALA B CA  1 
ATOM   4360 C C   . ALA B 1 34  ? -20.129 35.343 22.500  1.00 17.47 ? 34  ALA B C   1 
ATOM   4361 O O   . ALA B 1 34  ? -19.624 35.005 23.579  1.00 16.88 ? 34  ALA B O   1 
ATOM   4362 C CB  . ALA B 1 34  ? -21.737 33.883 21.233  1.00 16.95 ? 34  ALA B CB  1 
ATOM   4363 N N   . VAL B 1 35  ? -19.427 35.985 21.560  1.00 15.18 ? 35  VAL B N   1 
ATOM   4364 C CA  . VAL B 1 35  ? -17.999 36.215 21.763  1.00 15.32 ? 35  VAL B CA  1 
ATOM   4365 C C   . VAL B 1 35  ? -17.764 37.298 22.802  1.00 19.13 ? 35  VAL B C   1 
ATOM   4366 O O   . VAL B 1 35  ? -16.746 37.273 23.508  1.00 18.44 ? 35  VAL B O   1 
ATOM   4367 C CB  . VAL B 1 35  ? -17.299 36.556 20.436  1.00 18.58 ? 35  VAL B CB  1 
ATOM   4368 C CG1 . VAL B 1 35  ? -17.565 35.465 19.404  1.00 19.81 ? 35  VAL B CG1 1 
ATOM   4369 C CG2 . VAL B 1 35  ? -17.748 37.908 19.910  1.00 21.92 ? 35  VAL B CG2 1 
ATOM   4370 N N   . LYS B 1 36  ? -18.684 38.259 22.923  1.00 13.50 ? 36  LYS B N   1 
ATOM   4371 C CA  . LYS B 1 36  ? -18.474 39.375 23.842  1.00 13.88 ? 36  LYS B CA  1 
ATOM   4372 C C   . LYS B 1 36  ? -19.037 39.108 25.231  1.00 14.54 ? 36  LYS B C   1 
ATOM   4373 O O   . LYS B 1 36  ? -18.377 39.424 26.228  1.00 14.81 ? 36  LYS B O   1 
ATOM   4374 C CB  . LYS B 1 36  ? -19.099 40.664 23.292  1.00 14.92 ? 36  LYS B CB  1 
ATOM   4375 C CG  . LYS B 1 36  ? -18.578 41.931 24.014  1.00 15.04 ? 36  LYS B CG  1 
ATOM   4376 C CD  . LYS B 1 36  ? -19.053 43.250 23.372  1.00 15.31 ? 36  LYS B CD  1 
ATOM   4377 C CE  . LYS B 1 36  ? -20.560 43.487 23.574  1.00 15.71 ? 36  LYS B CE  1 
ATOM   4378 N NZ  . LYS B 1 36  ? -20.899 43.683 25.033  1.00 14.60 ? 36  LYS B NZ  1 
ATOM   4379 N N   . ASP B 1 37  ? -20.228 38.514 25.319  1.00 14.18 ? 37  ASP B N   1 
ATOM   4380 C CA  . ASP B 1 37  ? -20.960 38.495 26.580  1.00 12.70 ? 37  ASP B CA  1 
ATOM   4381 C C   . ASP B 1 37  ? -21.326 37.113 27.098  1.00 16.72 ? 37  ASP B C   1 
ATOM   4382 O O   . ASP B 1 37  ? -21.287 36.899 28.310  1.00 15.25 ? 37  ASP B O   1 
ATOM   4383 C CB  . ASP B 1 37  ? -22.244 39.331 26.433  1.00 11.62 ? 37  ASP B CB  1 
ATOM   4384 C CG  . ASP B 1 37  ? -21.981 40.689 25.818  1.00 14.42 ? 37  ASP B CG  1 
ATOM   4385 O OD1 . ASP B 1 37  ? -21.265 41.498 26.447  1.00 16.88 ? 37  ASP B OD1 1 
ATOM   4386 O OD2 . ASP B 1 37  ? -22.480 40.938 24.698  1.00 12.86 ? 37  ASP B OD2 1 
ATOM   4387 N N   . TYR B 1 38  ? -21.720 36.168 26.237  1.00 13.27 ? 38  TYR B N   1 
ATOM   4388 C CA  . TYR B 1 38  ? -22.383 34.975 26.764  1.00 12.70 ? 38  TYR B CA  1 
ATOM   4389 C C   . TYR B 1 38  ? -21.417 34.047 27.489  1.00 14.12 ? 38  TYR B C   1 
ATOM   4390 O O   . TYR B 1 38  ? -21.833 33.298 28.382  1.00 16.90 ? 38  TYR B O   1 
ATOM   4391 C CB  . TYR B 1 38  ? -23.109 34.230 25.644  1.00 13.43 ? 38  TYR B CB  1 
ATOM   4392 C CG  . TYR B 1 38  ? -24.302 34.998 25.108  1.00 12.85 ? 38  TYR B CG  1 
ATOM   4393 C CD1 . TYR B 1 38  ? -25.051 35.832 25.933  1.00 14.60 ? 38  TYR B CD1 1 
ATOM   4394 C CD2 . TYR B 1 38  ? -24.664 34.903 23.770  1.00 15.32 ? 38  TYR B CD2 1 
ATOM   4395 C CE1 . TYR B 1 38  ? -26.136 36.546 25.433  1.00 12.34 ? 38  TYR B CE1 1 
ATOM   4396 C CE2 . TYR B 1 38  ? -25.732 35.609 23.271  1.00 11.36 ? 38  TYR B CE2 1 
ATOM   4397 C CZ  . TYR B 1 38  ? -26.466 36.428 24.098  1.00 12.50 ? 38  TYR B CZ  1 
ATOM   4398 O OH  . TYR B 1 38  ? -27.532 37.125 23.578  1.00 13.28 ? 38  TYR B OH  1 
ATOM   4399 N N   . TYR B 1 39  ? -20.131 34.089 27.144  1.00 13.56 ? 39  TYR B N   1 
ATOM   4400 C CA  . TYR B 1 39  ? -19.132 33.373 27.925  1.00 18.36 ? 39  TYR B CA  1 
ATOM   4401 C C   . TYR B 1 39  ? -18.599 34.254 29.041  1.00 20.09 ? 39  TYR B C   1 
ATOM   4402 O O   . TYR B 1 39  ? -18.424 33.806 30.180  1.00 16.34 ? 39  TYR B O   1 
ATOM   4403 C CB  . TYR B 1 39  ? -17.982 32.913 27.020  1.00 16.27 ? 39  TYR B CB  1 
ATOM   4404 C CG  . TYR B 1 39  ? -16.796 32.338 27.755  1.00 20.26 ? 39  TYR B CG  1 
ATOM   4405 C CD1 . TYR B 1 39  ? -15.759 33.156 28.197  1.00 19.39 ? 39  TYR B CD1 1 
ATOM   4406 C CD2 . TYR B 1 39  ? -16.709 30.982 28.004  1.00 22.06 ? 39  TYR B CD2 1 
ATOM   4407 C CE1 . TYR B 1 39  ? -14.676 32.638 28.880  1.00 19.54 ? 39  TYR B CE1 1 
ATOM   4408 C CE2 . TYR B 1 39  ? -15.619 30.445 28.687  1.00 22.58 ? 39  TYR B CE2 1 
ATOM   4409 C CZ  . TYR B 1 39  ? -14.607 31.282 29.122  1.00 24.69 ? 39  TYR B CZ  1 
ATOM   4410 O OH  . TYR B 1 39  ? -13.527 30.779 29.800  1.00 27.44 ? 39  TYR B OH  1 
ATOM   4411 N N   . ASP B 1 40  ? -18.363 35.518 28.727  1.00 19.19 ? 40  ASP B N   1 
ATOM   4412 C CA  . ASP B 1 40  ? -17.617 36.362 29.642  1.00 17.12 ? 40  ASP B CA  1 
ATOM   4413 C C   . ASP B 1 40  ? -18.432 36.761 30.859  1.00 11.85 ? 40  ASP B C   1 
ATOM   4414 O O   . ASP B 1 40  ? -17.856 36.960 31.929  1.00 15.41 ? 40  ASP B O   1 
ATOM   4415 C CB  . ASP B 1 40  ? -17.110 37.585 28.896  1.00 17.33 ? 40  ASP B CB  1 
ATOM   4416 C CG  . ASP B 1 40  ? -15.795 37.311 28.221  1.00 22.00 ? 40  ASP B CG  1 
ATOM   4417 O OD1 . ASP B 1 40  ? -14.805 37.148 28.958  1.00 20.87 ? 40  ASP B OD1 1 
ATOM   4418 O OD2 . ASP B 1 40  ? -15.765 37.202 26.975  1.00 20.50 ? 40  ASP B OD2 1 
ATOM   4419 N N   . MET B 1 41  ? -19.763 36.894 30.726  1.00 14.41 ? 41  MET B N   1 
ATOM   4420 C CA  . MET B 1 41  ? -20.551 37.258 31.903  1.00 13.74 ? 41  MET B CA  1 
ATOM   4421 C C   . MET B 1 41  ? -20.494 36.188 32.986  1.00 14.01 ? 41  MET B C   1 
ATOM   4422 O O   . MET B 1 41  ? -20.182 36.531 34.141  1.00 16.26 ? 41  MET B O   1 
ATOM   4423 C CB  . MET B 1 41  ? -21.992 37.588 31.497  1.00 10.92 ? 41  MET B CB  1 
ATOM   4424 C CG  . MET B 1 41  ? -22.144 39.004 30.901  1.00 12.85 ? 41  MET B CG  1 
ATOM   4425 S SD  . MET B 1 41  ? -21.951 40.352 32.101  1.00 13.56 ? 41  MET B SD  1 
ATOM   4426 C CE  . MET B 1 41  ? -23.555 40.272 32.910  1.00 12.94 ? 41  MET B CE  1 
ATOM   4427 N N   . PRO B 1 42  ? -20.753 34.904 32.716  1.00 13.62 ? 42  PRO B N   1 
ATOM   4428 C CA  . PRO B 1 42  ? -20.508 33.921 33.778  1.00 17.74 ? 42  PRO B CA  1 
ATOM   4429 C C   . PRO B 1 42  ? -19.033 33.774 34.118  1.00 15.97 ? 42  PRO B C   1 
ATOM   4430 O O   . PRO B 1 42  ? -18.707 33.403 35.253  1.00 18.01 ? 42  PRO B O   1 
ATOM   4431 C CB  . PRO B 1 42  ? -21.102 32.620 33.214  1.00 14.44 ? 42  PRO B CB  1 
ATOM   4432 C CG  . PRO B 1 42  ? -21.113 32.807 31.719  1.00 13.30 ? 42  PRO B CG  1 
ATOM   4433 C CD  . PRO B 1 42  ? -21.409 34.282 31.542  1.00 13.41 ? 42  PRO B CD  1 
ATOM   4434 N N   . ALA B 1 43  ? -18.123 34.073 33.184  1.00 13.72 ? 43  ALA B N   1 
ATOM   4435 C CA  . ALA B 1 43  ? -16.703 33.888 33.480  1.00 15.08 ? 43  ALA B CA  1 
ATOM   4436 C C   . ALA B 1 43  ? -16.200 34.819 34.578  1.00 17.62 ? 43  ALA B C   1 
ATOM   4437 O O   . ALA B 1 43  ? -15.152 34.535 35.168  1.00 21.34 ? 43  ALA B O   1 
ATOM   4438 C CB  . ALA B 1 43  ? -15.860 34.067 32.212  1.00 19.84 ? 43  ALA B CB  1 
ATOM   4439 N N   . TYR B 1 44  ? -16.921 35.915 34.870  1.00 17.34 ? 44  TYR B N   1 
ATOM   4440 C CA  . TYR B 1 44  ? -16.571 36.745 36.027  1.00 17.21 ? 44  TYR B CA  1 
ATOM   4441 C C   . TYR B 1 44  ? -16.528 35.936 37.310  1.00 18.47 ? 44  TYR B C   1 
ATOM   4442 O O   . TYR B 1 44  ? -15.795 36.294 38.239  1.00 19.39 ? 44  TYR B O   1 
ATOM   4443 C CB  . TYR B 1 44  ? -17.580 37.884 36.213  1.00 14.97 ? 44  TYR B CB  1 
ATOM   4444 C CG  . TYR B 1 44  ? -17.332 39.111 35.378  1.00 13.98 ? 44  TYR B CG  1 
ATOM   4445 C CD1 . TYR B 1 44  ? -16.472 40.117 35.817  1.00 14.56 ? 44  TYR B CD1 1 
ATOM   4446 C CD2 . TYR B 1 44  ? -17.968 39.273 34.152  1.00 15.98 ? 44  TYR B CD2 1 
ATOM   4447 C CE1 . TYR B 1 44  ? -16.252 41.258 35.040  1.00 17.49 ? 44  TYR B CE1 1 
ATOM   4448 C CE2 . TYR B 1 44  ? -17.748 40.393 33.373  1.00 16.45 ? 44  TYR B CE2 1 
ATOM   4449 C CZ  . TYR B 1 44  ? -16.902 41.385 33.825  1.00 16.58 ? 44  TYR B CZ  1 
ATOM   4450 O OH  . TYR B 1 44  ? -16.711 42.493 33.036  1.00 17.31 ? 44  TYR B OH  1 
ATOM   4451 N N   . LEU B 1 45  ? -17.320 34.863 37.395  1.00 16.57 ? 45  LEU B N   1 
ATOM   4452 C CA  . LEU B 1 45  ? -17.343 34.054 38.604  1.00 16.03 ? 45  LEU B CA  1 
ATOM   4453 C C   . LEU B 1 45  ? -16.033 33.316 38.843  1.00 20.40 ? 45  LEU B C   1 
ATOM   4454 O O   . LEU B 1 45  ? -15.802 32.835 39.960  1.00 23.98 ? 45  LEU B O   1 
ATOM   4455 C CB  . LEU B 1 45  ? -18.516 33.075 38.545  1.00 16.36 ? 45  LEU B CB  1 
ATOM   4456 C CG  . LEU B 1 45  ? -19.911 33.705 38.588  1.00 16.90 ? 45  LEU B CG  1 
ATOM   4457 C CD1 . LEU B 1 45  ? -20.980 32.728 38.107  1.00 17.63 ? 45  LEU B CD1 1 
ATOM   4458 C CD2 . LEU B 1 45  ? -20.221 34.229 40.006  1.00 17.06 ? 45  LEU B CD2 1 
ATOM   4459 N N   . LYS B 1 46  ? -15.160 33.232 37.841  1.00 21.41 ? 46  LYS B N   1 
ATOM   4460 C CA  . LYS B 1 46  ? -13.837 32.667 38.076  1.00 22.86 ? 46  LYS B CA  1 
ATOM   4461 C C   . LYS B 1 46  ? -12.968 33.584 38.925  1.00 24.53 ? 46  LYS B C   1 
ATOM   4462 O O   . LYS B 1 46  ? -12.026 33.108 39.574  1.00 24.45 ? 46  LYS B O   1 
ATOM   4463 C CB  . LYS B 1 46  ? -13.138 32.393 36.743  1.00 26.46 ? 46  LYS B CB  1 
ATOM   4464 C CG  . LYS B 1 46  ? -13.737 31.254 35.929  1.00 34.81 ? 46  LYS B CG  1 
ATOM   4465 C CD  . LYS B 1 46  ? -12.953 31.060 34.635  1.00 47.40 ? 46  LYS B CD  1 
ATOM   4466 C CE  . LYS B 1 46  ? -13.396 29.819 33.873  1.00 57.77 ? 46  LYS B CE  1 
ATOM   4467 N NZ  . LYS B 1 46  ? -12.978 28.561 34.554  1.00 64.61 ? 46  LYS B NZ  1 
ATOM   4468 N N   . ASP B 1 47  ? -13.257 34.886 38.930  1.00 21.80 ? 47  ASP B N   1 
ATOM   4469 C CA  . ASP B 1 47  ? -12.402 35.874 39.567  1.00 23.12 ? 47  ASP B CA  1 
ATOM   4470 C C   . ASP B 1 47  ? -13.030 36.540 40.780  1.00 25.84 ? 47  ASP B C   1 
ATOM   4471 O O   . ASP B 1 47  ? -12.307 37.161 41.566  1.00 27.22 ? 47  ASP B O   1 
ATOM   4472 C CB  . ASP B 1 47  ? -12.011 36.959 38.555  1.00 23.39 ? 47  ASP B CB  1 
ATOM   4473 C CG  . ASP B 1 47  ? -11.224 36.398 37.384  1.00 37.15 ? 47  ASP B CG  1 
ATOM   4474 O OD1 . ASP B 1 47  ? -10.432 35.458 37.608  1.00 33.50 ? 47  ASP B OD1 1 
ATOM   4475 O OD2 . ASP B 1 47  ? -11.395 36.895 36.249  1.00 37.97 ? 47  ASP B OD2 1 
ATOM   4476 N N   . PHE B 1 48  ? -14.339 36.414 40.964  1.00 24.24 ? 48  PHE B N   1 
ATOM   4477 C CA  . PHE B 1 48  ? -15.039 37.066 42.061  1.00 24.28 ? 48  PHE B CA  1 
ATOM   4478 C C   . PHE B 1 48  ? -15.885 36.021 42.772  1.00 24.29 ? 48  PHE B C   1 
ATOM   4479 O O   . PHE B 1 48  ? -16.689 35.338 42.134  1.00 25.86 ? 48  PHE B O   1 
ATOM   4480 C CB  . PHE B 1 48  ? -15.896 38.219 41.536  1.00 22.72 ? 48  PHE B CB  1 
ATOM   4481 C CG  . PHE B 1 48  ? -15.099 39.293 40.859  1.00 23.76 ? 48  PHE B CG  1 
ATOM   4482 C CD1 . PHE B 1 48  ? -14.489 40.287 41.602  1.00 24.50 ? 48  PHE B CD1 1 
ATOM   4483 C CD2 . PHE B 1 48  ? -14.943 39.300 39.481  1.00 22.94 ? 48  PHE B CD2 1 
ATOM   4484 C CE1 . PHE B 1 48  ? -13.740 41.278 40.985  1.00 22.73 ? 48  PHE B CE1 1 
ATOM   4485 C CE2 . PHE B 1 48  ? -14.202 40.286 38.860  1.00 23.11 ? 48  PHE B CE2 1 
ATOM   4486 C CZ  . PHE B 1 48  ? -13.592 41.279 39.620  1.00 25.39 ? 48  PHE B CZ  1 
ATOM   4487 N N   . GLU B 1 49  ? -15.672 35.861 44.081  1.00 22.87 ? 49  GLU B N   1 
ATOM   4488 C CA  . GLU B 1 49  ? -16.386 34.837 44.845  1.00 22.19 ? 49  GLU B CA  1 
ATOM   4489 C C   . GLU B 1 49  ? -17.707 35.438 45.311  1.00 20.67 ? 49  GLU B C   1 
ATOM   4490 O O   . GLU B 1 49  ? -17.895 35.810 46.471  1.00 25.81 ? 49  GLU B O   1 
ATOM   4491 C CB  . GLU B 1 49  ? -15.542 34.311 46.006  1.00 36.16 ? 49  GLU B CB  1 
ATOM   4492 C CG  . GLU B 1 49  ? -16.136 33.049 46.661  1.00 46.26 ? 49  GLU B CG  1 
ATOM   4493 C CD  . GLU B 1 49  ? -15.147 32.257 47.516  1.00 60.88 ? 49  GLU B CD  1 
ATOM   4494 O OE1 . GLU B 1 49  ? -13.956 32.167 47.144  1.00 62.87 ? 49  GLU B OE1 1 
ATOM   4495 O OE2 . GLU B 1 49  ? -15.571 31.709 48.560  1.00 61.56 ? 49  GLU B OE2 1 
ATOM   4496 N N   . ILE B 1 50  ? -18.633 35.544 44.359  1.00 17.90 ? 50  ILE B N   1 
ATOM   4497 C CA  . ILE B 1 50  ? -20.007 35.955 44.595  1.00 21.07 ? 50  ILE B CA  1 
ATOM   4498 C C   . ILE B 1 50  ? -20.902 34.974 43.845  1.00 18.37 ? 50  ILE B C   1 
ATOM   4499 O O   . ILE B 1 50  ? -20.425 34.079 43.152  1.00 24.29 ? 50  ILE B O   1 
ATOM   4500 C CB  . ILE B 1 50  ? -20.274 37.401 44.136  1.00 19.64 ? 50  ILE B CB  1 
ATOM   4501 C CG1 . ILE B 1 50  ? -19.949 37.550 42.645  1.00 18.70 ? 50  ILE B CG1 1 
ATOM   4502 C CG2 . ILE B 1 50  ? -19.451 38.379 44.953  1.00 25.03 ? 50  ILE B CG2 1 
ATOM   4503 C CD1 . ILE B 1 50  ? -20.442 38.852 42.067  1.00 24.09 ? 50  ILE B CD1 1 
ATOM   4504 N N   . LYS B 1 51  ? -22.209 35.122 44.024  1.00 14.41 ? 51  LYS B N   1 
ATOM   4505 C CA  . LYS B 1 51  ? -23.182 34.341 43.269  1.00 14.74 ? 51  LYS B CA  1 
ATOM   4506 C C   . LYS B 1 51  ? -23.790 35.212 42.180  1.00 16.54 ? 51  LYS B C   1 
ATOM   4507 O O   . LYS B 1 51  ? -24.150 36.365 42.434  1.00 15.28 ? 51  LYS B O   1 
ATOM   4508 C CB  . LYS B 1 51  ? -24.294 33.796 44.165  1.00 13.08 ? 51  LYS B CB  1 
ATOM   4509 C CG  . LYS B 1 51  ? -23.840 33.123 45.447  1.00 15.24 ? 51  LYS B CG  1 
ATOM   4510 C CD  . LYS B 1 51  ? -22.940 31.940 45.172  1.00 19.02 ? 51  LYS B CD  1 
ATOM   4511 C CE  . LYS B 1 51  ? -22.709 31.140 46.448  1.00 22.43 ? 51  LYS B CE  1 
ATOM   4512 N NZ  . LYS B 1 51  ? -21.860 29.966 46.152  1.00 34.70 ? 51  LYS B NZ  1 
ATOM   4513 N N   . LEU B 1 52  ? -23.899 34.659 40.970  1.00 13.93 ? 52  LEU B N   1 
ATOM   4514 C CA  . LEU B 1 52  ? -24.559 35.323 39.858  1.00 17.17 ? 52  LEU B CA  1 
ATOM   4515 C C   . LEU B 1 52  ? -25.400 34.277 39.149  1.00 14.29 ? 52  LEU B C   1 
ATOM   4516 O O   . LEU B 1 52  ? -24.952 33.146 38.974  1.00 14.96 ? 52  LEU B O   1 
ATOM   4517 C CB  . LEU B 1 52  ? -23.549 35.942 38.869  1.00 15.14 ? 52  LEU B CB  1 
ATOM   4518 C CG  . LEU B 1 52  ? -22.588 37.025 39.374  1.00 15.12 ? 52  LEU B CG  1 
ATOM   4519 C CD1 . LEU B 1 52  ? -21.559 37.370 38.297  1.00 16.03 ? 52  LEU B CD1 1 
ATOM   4520 C CD2 . LEU B 1 52  ? -23.362 38.285 39.805  1.00 15.37 ? 52  LEU B CD2 1 
ATOM   4521 N N   . ASN B 1 53  ? -26.617 34.647 38.760  1.00 12.13 ? 53  ASN B N   1 
ATOM   4522 C CA  . ASN B 1 53  ? -27.535 33.729 38.108  1.00 11.93 ? 53  ASN B CA  1 
ATOM   4523 C C   . ASN B 1 53  ? -27.794 34.148 36.672  1.00 13.11 ? 53  ASN B C   1 
ATOM   4524 O O   . ASN B 1 53  ? -27.646 35.312 36.303  1.00 12.92 ? 53  ASN B O   1 
ATOM   4525 C CB  . ASN B 1 53  ? -28.839 33.650 38.899  1.00 11.70 ? 53  ASN B CB  1 
ATOM   4526 C CG  . ASN B 1 53  ? -28.569 33.346 40.358  1.00 12.02 ? 53  ASN B CG  1 
ATOM   4527 O OD1 . ASN B 1 53  ? -28.253 32.211 40.701  1.00 13.40 ? 53  ASN B OD1 1 
ATOM   4528 N ND2 . ASN B 1 53  ? -28.622 34.365 41.208  1.00 13.77 ? 53  ASN B ND2 1 
ATOM   4529 N N   . PHE B 1 54  ? -28.186 33.172 35.860  1.00 12.39 ? 54  PHE B N   1 
ATOM   4530 C CA  . PHE B 1 54  ? -28.304 33.382 34.428  1.00 12.06 ? 54  PHE B CA  1 
ATOM   4531 C C   . PHE B 1 54  ? -29.559 32.719 33.909  1.00 13.28 ? 54  PHE B C   1 
ATOM   4532 O O   . PHE B 1 54  ? -29.925 31.634 34.367  1.00 16.39 ? 54  PHE B O   1 
ATOM   4533 C CB  . PHE B 1 54  ? -27.072 32.819 33.712  1.00 12.46 ? 54  PHE B CB  1 
ATOM   4534 C CG  . PHE B 1 54  ? -25.834 33.522 34.111  1.00 13.51 ? 54  PHE B CG  1 
ATOM   4535 C CD1 . PHE B 1 54  ? -25.459 34.684 33.458  1.00 15.14 ? 54  PHE B CD1 1 
ATOM   4536 C CD2 . PHE B 1 54  ? -25.100 33.090 35.210  1.00 13.82 ? 54  PHE B CD2 1 
ATOM   4537 C CE1 . PHE B 1 54  ? -24.342 35.372 33.850  1.00 12.99 ? 54  PHE B CE1 1 
ATOM   4538 C CE2 . PHE B 1 54  ? -23.975 33.787 35.616  1.00 16.61 ? 54  PHE B CE2 1 
ATOM   4539 C CZ  . PHE B 1 54  ? -23.611 34.946 34.920  1.00 12.76 ? 54  PHE B CZ  1 
ATOM   4540 N N   . ASN B 1 55  ? -30.189 33.360 32.932  1.00 12.20 ? 55  ASN B N   1 
ATOM   4541 C CA  . ASN B 1 55  ? -31.250 32.750 32.146  1.00 12.43 ? 55  ASN B CA  1 
ATOM   4542 C C   . ASN B 1 55  ? -30.746 32.585 30.722  1.00 13.64 ? 55  ASN B C   1 
ATOM   4543 O O   . ASN B 1 55  ? -30.182 33.524 30.155  1.00 12.89 ? 55  ASN B O   1 
ATOM   4544 C CB  . ASN B 1 55  ? -32.516 33.615 32.139  1.00 11.81 ? 55  ASN B CB  1 
ATOM   4545 C CG  . ASN B 1 55  ? -33.679 32.917 31.462  1.00 14.09 ? 55  ASN B CG  1 
ATOM   4546 O OD1 . ASN B 1 55  ? -34.166 31.909 31.956  1.00 14.13 ? 55  ASN B OD1 1 
ATOM   4547 N ND2 . ASN B 1 55  ? -34.108 33.430 30.307  1.00 15.09 ? 55  ASN B ND2 1 
ATOM   4548 N N   . LEU B 1 56  ? -30.937 31.397 30.160  1.00 11.82 ? 56  LEU B N   1 
ATOM   4549 C CA  . LEU B 1 56  ? -30.622 31.133 28.761  1.00 11.10 ? 56  LEU B CA  1 
ATOM   4550 C C   . LEU B 1 56  ? -31.891 30.669 28.066  1.00 12.67 ? 56  LEU B C   1 
ATOM   4551 O O   . LEU B 1 56  ? -32.465 29.644 28.451  1.00 16.21 ? 56  LEU B O   1 
ATOM   4552 C CB  . LEU B 1 56  ? -29.536 30.057 28.637  1.00 13.44 ? 56  LEU B CB  1 
ATOM   4553 C CG  . LEU B 1 56  ? -28.172 30.337 29.268  1.00 19.94 ? 56  LEU B CG  1 
ATOM   4554 C CD1 . LEU B 1 56  ? -27.325 29.062 29.233  1.00 19.18 ? 56  LEU B CD1 1 
ATOM   4555 C CD2 . LEU B 1 56  ? -27.470 31.474 28.541  1.00 23.50 ? 56  LEU B CD2 1 
ATOM   4556 N N   . THR B 1 57  ? -32.327 31.402 27.035  1.00 12.28 ? 57  THR B N   1 
ATOM   4557 C CA  . THR B 1 57  ? -33.491 30.923 26.300  1.00 13.79 ? 57  THR B CA  1 
ATOM   4558 C C   . THR B 1 57  ? -33.087 29.743 25.418  1.00 15.93 ? 57  THR B C   1 
ATOM   4559 O O   . THR B 1 57  ? -31.956 29.677 24.922  1.00 13.20 ? 57  THR B O   1 
ATOM   4560 C CB  . THR B 1 57  ? -34.130 32.019 25.438  1.00 15.82 ? 57  THR B CB  1 
ATOM   4561 O OG1 . THR B 1 57  ? -33.234 32.422 24.396  1.00 15.49 ? 57  THR B OG1 1 
ATOM   4562 C CG2 . THR B 1 57  ? -34.505 33.234 26.294  1.00 13.65 ? 57  THR B CG2 1 
ATOM   4563 N N   . PRO B 1 58  ? -33.985 28.786 25.222  1.00 16.79 ? 58  PRO B N   1 
ATOM   4564 C CA  . PRO B 1 58  ? -33.611 27.619 24.413  1.00 15.26 ? 58  PRO B CA  1 
ATOM   4565 C C   . PRO B 1 58  ? -33.255 27.985 22.988  1.00 12.97 ? 58  PRO B C   1 
ATOM   4566 O O   . PRO B 1 58  ? -32.364 27.365 22.403  1.00 15.76 ? 58  PRO B O   1 
ATOM   4567 C CB  . PRO B 1 58  ? -34.860 26.734 24.476  1.00 16.21 ? 58  PRO B CB  1 
ATOM   4568 C CG  . PRO B 1 58  ? -35.555 27.160 25.757  1.00 17.22 ? 58  PRO B CG  1 
ATOM   4569 C CD  . PRO B 1 58  ? -35.312 28.642 25.845  1.00 15.44 ? 58  PRO B CD  1 
ATOM   4570 N N   . VAL B 1 59  ? -33.933 28.973 22.406  1.00 15.03 ? 59  VAL B N   1 
ATOM   4571 C CA  . VAL B 1 59  ? -33.606 29.337 21.031  1.00 17.84 ? 59  VAL B CA  1 
ATOM   4572 C C   . VAL B 1 59  ? -32.203 29.947 20.965  1.00 18.41 ? 59  VAL B C   1 
ATOM   4573 O O   . VAL B 1 59  ? -31.472 29.727 19.992  1.00 16.60 ? 59  VAL B O   1 
ATOM   4574 C CB  . VAL B 1 59  ? -34.696 30.264 20.445  1.00 14.15 ? 59  VAL B CB  1 
ATOM   4575 C CG1 . VAL B 1 59  ? -34.857 31.539 21.269  1.00 16.86 ? 59  VAL B CG1 1 
ATOM   4576 C CG2 . VAL B 1 59  ? -34.384 30.603 18.982  1.00 16.39 ? 59  VAL B CG2 1 
ATOM   4577 N N   . LEU B 1 60  ? -31.778 30.669 22.008  1.00 14.68 ? 60  LEU B N   1 
ATOM   4578 C CA  . LEU B 1 60  ? -30.385 31.104 22.062  1.00 13.29 ? 60  LEU B CA  1 
ATOM   4579 C C   . LEU B 1 60  ? -29.440 29.908 22.119  1.00 17.37 ? 60  LEU B C   1 
ATOM   4580 O O   . LEU B 1 60  ? -28.437 29.857 21.397  1.00 16.64 ? 60  LEU B O   1 
ATOM   4581 C CB  . LEU B 1 60  ? -30.145 32.013 23.269  1.00 12.10 ? 60  LEU B CB  1 
ATOM   4582 C CG  . LEU B 1 60  ? -28.664 32.374 23.460  1.00 13.31 ? 60  LEU B CG  1 
ATOM   4583 C CD1 . LEU B 1 60  ? -28.073 33.059 22.208  1.00 14.66 ? 60  LEU B CD1 1 
ATOM   4584 C CD2 . LEU B 1 60  ? -28.459 33.259 24.691  1.00 12.02 ? 60  LEU B CD2 1 
ATOM   4585 N N   . ILE B 1 61  ? -29.747 28.932 22.978  1.00 14.52 ? 61  ILE B N   1 
ATOM   4586 C CA  . ILE B 1 61  ? -28.882 27.762 23.118  1.00 14.90 ? 61  ILE B CA  1 
ATOM   4587 C C   . ILE B 1 61  ? -28.721 27.044 21.779  1.00 15.02 ? 61  ILE B C   1 
ATOM   4588 O O   . ILE B 1 61  ? -27.606 26.662 21.397  1.00 18.39 ? 61  ILE B O   1 
ATOM   4589 C CB  . ILE B 1 61  ? -29.435 26.822 24.202  1.00 14.49 ? 61  ILE B CB  1 
ATOM   4590 C CG1 . ILE B 1 61  ? -29.363 27.478 25.580  1.00 16.76 ? 61  ILE B CG1 1 
ATOM   4591 C CG2 . ILE B 1 61  ? -28.635 25.514 24.240  1.00 17.21 ? 61  ILE B CG2 1 
ATOM   4592 C CD1 . ILE B 1 61  ? -30.104 26.689 26.647  1.00 18.45 ? 61  ILE B CD1 1 
ATOM   4593 N N   . ASP B 1 62  ? -29.828 26.841 21.053  1.00 16.04 ? 62  ASP B N   1 
ATOM   4594 C CA  . ASP B 1 62  ? -29.771 26.241 19.716  1.00 18.86 ? 62  ASP B CA  1 
ATOM   4595 C C   . ASP B 1 62  ? -28.741 26.938 18.830  1.00 20.76 ? 62  ASP B C   1 
ATOM   4596 O O   . ASP B 1 62  ? -27.960 26.293 18.123  1.00 19.85 ? 62  ASP B O   1 
ATOM   4597 C CB  . ASP B 1 62  ? -31.142 26.321 19.040  1.00 19.28 ? 62  ASP B CB  1 
ATOM   4598 C CG  . ASP B 1 62  ? -32.111 25.266 19.528  1.00 22.68 ? 62  ASP B CG  1 
ATOM   4599 O OD1 . ASP B 1 62  ? -31.669 24.287 20.158  1.00 26.22 ? 62  ASP B OD1 1 
ATOM   4600 O OD2 . ASP B 1 62  ? -33.326 25.417 19.260  1.00 22.12 ? 62  ASP B OD2 1 
ATOM   4601 N N   . GLN B 1 63  ? -28.757 28.267 18.828  1.00 17.09 ? 63  GLN B N   1 
ATOM   4602 C CA  . GLN B 1 63  ? -27.850 28.997 17.952  1.00 17.42 ? 63  GLN B CA  1 
ATOM   4603 C C   . GLN B 1 63  ? -26.407 28.901 18.437  1.00 18.49 ? 63  GLN B C   1 
ATOM   4604 O O   . GLN B 1 63  ? -25.488 28.720 17.631  1.00 17.21 ? 63  GLN B O   1 
ATOM   4605 C CB  . GLN B 1 63  ? -28.289 30.454 17.856  1.00 13.25 ? 63  GLN B CB  1 
ATOM   4606 C CG  . GLN B 1 63  ? -29.730 30.643 17.411  1.00 18.61 ? 63  GLN B CG  1 
ATOM   4607 C CD  . GLN B 1 63  ? -30.120 32.111 17.395  1.00 18.34 ? 63  GLN B CD  1 
ATOM   4608 O OE1 . GLN B 1 63  ? -29.588 32.891 16.612  1.00 20.18 ? 63  GLN B OE1 1 
ATOM   4609 N NE2 . GLN B 1 63  ? -31.034 32.498 18.276  1.00 15.70 ? 63  GLN B NE2 1 
ATOM   4610 N N   . ILE B 1 64  ? -26.183 29.038 19.746  1.00 17.75 ? 64  ILE B N   1 
ATOM   4611 C CA  . ILE B 1 64  ? -24.834 28.852 20.277  1.00 15.73 ? 64  ILE B CA  1 
ATOM   4612 C C   . ILE B 1 64  ? -24.290 27.481 19.869  1.00 19.95 ? 64  ILE B C   1 
ATOM   4613 O O   . ILE B 1 64  ? -23.123 27.347 19.477  1.00 18.22 ? 64  ILE B O   1 
ATOM   4614 C CB  . ILE B 1 64  ? -24.830 29.051 21.805  1.00 13.64 ? 64  ILE B CB  1 
ATOM   4615 C CG1 . ILE B 1 64  ? -25.039 30.535 22.169  1.00 14.59 ? 64  ILE B CG1 1 
ATOM   4616 C CG2 . ILE B 1 64  ? -23.531 28.498 22.413  1.00 17.81 ? 64  ILE B CG2 1 
ATOM   4617 C CD1 . ILE B 1 64  ? -25.185 30.795 23.669  1.00 17.80 ? 64  ILE B CD1 1 
ATOM   4618 N N   . GLN B 1 65  ? -25.130 26.446 19.917  1.00 16.49 ? 65  GLN B N   1 
ATOM   4619 C CA  . GLN B 1 65  ? -24.651 25.125 19.518  1.00 20.28 ? 65  GLN B CA  1 
ATOM   4620 C C   . GLN B 1 65  ? -24.309 25.085 18.036  1.00 23.75 ? 65  GLN B C   1 
ATOM   4621 O O   . GLN B 1 65  ? -23.304 24.479 17.636  1.00 23.38 ? 65  GLN B O   1 
ATOM   4622 C CB  . GLN B 1 65  ? -25.692 24.061 19.845  1.00 22.99 ? 65  GLN B CB  1 
ATOM   4623 C CG  . GLN B 1 65  ? -25.785 23.717 21.315  1.00 22.07 ? 65  GLN B CG  1 
ATOM   4624 C CD  . GLN B 1 65  ? -26.957 22.802 21.582  1.00 27.23 ? 65  GLN B CD  1 
ATOM   4625 O OE1 . GLN B 1 65  ? -28.095 23.141 21.274  1.00 27.91 ? 65  GLN B OE1 1 
ATOM   4626 N NE2 . GLN B 1 65  ? -26.683 21.622 22.116  1.00 27.53 ? 65  GLN B NE2 1 
ATOM   4627 N N   . GLU B 1 66  ? -25.137 25.719 17.204  1.00 21.17 ? 66  GLU B N   1 
ATOM   4628 C CA  . GLU B 1 66  ? -24.887 25.701 15.768  1.00 21.63 ? 66  GLU B CA  1 
ATOM   4629 C C   . GLU B 1 66  ? -23.569 26.389 15.441  1.00 19.33 ? 66  GLU B C   1 
ATOM   4630 O O   . GLU B 1 66  ? -22.779 25.871 14.647  1.00 22.14 ? 66  GLU B O   1 
ATOM   4631 C CB  . GLU B 1 66  ? -26.052 26.355 15.015  1.00 19.19 ? 66  GLU B CB  1 
ATOM   4632 C CG  . GLU B 1 66  ? -25.941 26.268 13.504  1.00 22.72 ? 66  GLU B CG  1 
ATOM   4633 C CD  . GLU B 1 66  ? -27.273 26.425 12.778  1.00 26.03 ? 66  GLU B CD  1 
ATOM   4634 O OE1 . GLU B 1 66  ? -28.291 26.757 13.428  1.00 24.42 ? 66  GLU B OE1 1 
ATOM   4635 O OE2 . GLU B 1 66  ? -27.296 26.207 11.546  1.00 31.57 ? 66  GLU B OE2 1 
ATOM   4636 N N   . TYR B 1 67  ? -23.295 27.535 16.074  1.00 19.16 ? 67  TYR B N   1 
ATOM   4637 C CA  . TYR B 1 67  ? -22.013 28.200 15.857  1.00 18.06 ? 67  TYR B CA  1 
ATOM   4638 C C   . TYR B 1 67  ? -20.864 27.346 16.380  1.00 21.12 ? 67  TYR B C   1 
ATOM   4639 O O   . TYR B 1 67  ? -19.847 27.165 15.695  1.00 21.89 ? 67  TYR B O   1 
ATOM   4640 C CB  . TYR B 1 67  ? -22.002 29.576 16.535  1.00 15.14 ? 67  TYR B CB  1 
ATOM   4641 C CG  . TYR B 1 67  ? -22.666 30.693 15.751  1.00 19.56 ? 67  TYR B CG  1 
ATOM   4642 C CD1 . TYR B 1 67  ? -21.968 31.393 14.769  1.00 20.10 ? 67  TYR B CD1 1 
ATOM   4643 C CD2 . TYR B 1 67  ? -23.980 31.069 16.011  1.00 15.82 ? 67  TYR B CD2 1 
ATOM   4644 C CE1 . TYR B 1 67  ? -22.570 32.428 14.052  1.00 19.39 ? 67  TYR B CE1 1 
ATOM   4645 C CE2 . TYR B 1 67  ? -24.591 32.101 15.294  1.00 20.36 ? 67  TYR B CE2 1 
ATOM   4646 C CZ  . TYR B 1 67  ? -23.876 32.775 14.316  1.00 18.41 ? 67  TYR B CZ  1 
ATOM   4647 O OH  . TYR B 1 67  ? -24.463 33.804 13.600  1.00 19.63 ? 67  TYR B OH  1 
ATOM   4648 N N   . ALA B 1 68  ? -21.022 26.799 17.590  1.00 20.99 ? 68  ALA B N   1 
ATOM   4649 C CA  . ALA B 1 68  ? -19.970 26.001 18.210  1.00 22.71 ? 68  ALA B CA  1 
ATOM   4650 C C   . ALA B 1 68  ? -19.570 24.822 17.340  1.00 25.43 ? 68  ALA B C   1 
ATOM   4651 O O   . ALA B 1 68  ? -18.401 24.420 17.333  1.00 25.24 ? 68  ALA B O   1 
ATOM   4652 C CB  . ALA B 1 68  ? -20.427 25.504 19.585  1.00 20.60 ? 68  ALA B CB  1 
ATOM   4653 N N   . GLN B 1 69  ? -20.517 24.256 16.605  1.00 23.17 ? 69  GLN B N   1 
ATOM   4654 C CA  . GLN B 1 69  ? -20.246 23.106 15.760  1.00 26.55 ? 69  GLN B CA  1 
ATOM   4655 C C   . GLN B 1 69  ? -19.800 23.496 14.360  1.00 28.21 ? 69  GLN B C   1 
ATOM   4656 O O   . GLN B 1 69  ? -19.602 22.612 13.521  1.00 33.02 ? 69  GLN B O   1 
ATOM   4657 C CB  . GLN B 1 69  ? -21.483 22.211 15.678  1.00 31.32 ? 69  GLN B CB  1 
ATOM   4658 C CG  . GLN B 1 69  ? -21.941 21.696 17.029  1.00 31.81 ? 69  GLN B CG  1 
ATOM   4659 C CD  . GLN B 1 69  ? -23.265 20.958 16.961  1.00 43.81 ? 69  GLN B CD  1 
ATOM   4660 O OE1 . GLN B 1 69  ? -23.747 20.613 15.880  1.00 44.85 ? 69  GLN B OE1 1 
ATOM   4661 N NE2 . GLN B 1 69  ? -23.862 20.711 18.122  1.00 51.27 ? 69  GLN B NE2 1 
ATOM   4662 N N   . GLY B 1 70  ? -19.635 24.786 14.087  1.00 29.22 ? 70  GLY B N   1 
ATOM   4663 C CA  . GLY B 1 70  ? -19.207 25.190 12.763  1.00 31.35 ? 70  GLY B CA  1 
ATOM   4664 C C   . GLY B 1 70  ? -20.249 25.011 11.687  1.00 33.23 ? 70  GLY B C   1 
ATOM   4665 O O   . GLY B 1 70  ? -19.902 24.956 10.503  1.00 38.31 ? 70  GLY B O   1 
ATOM   4666 N N   . LYS B 1 71  ? -21.527 24.918 12.063  1.00 30.27 ? 71  LYS B N   1 
ATOM   4667 C CA  . LYS B 1 71  ? -22.603 24.738 11.100  1.00 33.85 ? 71  LYS B CA  1 
ATOM   4668 C C   . LYS B 1 71  ? -23.330 26.030 10.763  1.00 33.79 ? 71  LYS B C   1 
ATOM   4669 O O   . LYS B 1 71  ? -24.162 26.033 9.851   1.00 33.78 ? 71  LYS B O   1 
ATOM   4670 C CB  . LYS B 1 71  ? -23.625 23.717 11.620  1.00 31.98 ? 71  LYS B CB  1 
ATOM   4671 C CG  . LYS B 1 71  ? -23.050 22.370 12.019  1.00 37.92 ? 71  LYS B CG  1 
ATOM   4672 C CD  . LYS B 1 71  ? -24.130 21.519 12.666  1.00 44.38 ? 71  LYS B CD  1 
ATOM   4673 C CE  . LYS B 1 71  ? -23.757 20.044 12.664  1.00 48.13 ? 71  LYS B CE  1 
ATOM   4674 N NZ  . LYS B 1 71  ? -22.764 19.735 11.598  1.00 53.19 ? 71  LYS B NZ  1 
ATOM   4675 N N   . ALA B 1 72  ? -23.054 27.121 11.470  1.00 28.88 ? 72  ALA B N   1 
ATOM   4676 C CA  . ALA B 1 72  ? -23.799 28.352 11.253  1.00 26.67 ? 72  ALA B CA  1 
ATOM   4677 C C   . ALA B 1 72  ? -23.266 29.063 10.016  1.00 26.47 ? 72  ALA B C   1 
ATOM   4678 O O   . ALA B 1 72  ? -22.076 29.388 9.940   1.00 32.16 ? 72  ALA B O   1 
ATOM   4679 C CB  . ALA B 1 72  ? -23.715 29.256 12.480  1.00 26.97 ? 72  ALA B CB  1 
ATOM   4680 N N   . LYS B 1 73  ? -24.143 29.295 9.046   1.00 26.59 ? 73  LYS B N   1 
ATOM   4681 C CA  . LYS B 1 73  ? -23.806 30.077 7.859   1.00 28.03 ? 73  LYS B CA  1 
ATOM   4682 C C   . LYS B 1 73  ? -24.238 31.515 8.124   1.00 23.61 ? 73  LYS B C   1 
ATOM   4683 O O   . LYS B 1 73  ? -25.398 31.875 7.916   1.00 27.08 ? 73  LYS B O   1 
ATOM   4684 C CB  . LYS B 1 73  ? -24.485 29.500 6.622   1.00 33.54 ? 73  LYS B CB  1 
ATOM   4685 C CG  . LYS B 1 73  ? -24.093 28.058 6.330   1.00 48.53 ? 73  LYS B CG  1 
ATOM   4686 C CD  . LYS B 1 73  ? -25.233 27.258 5.688   1.00 59.17 ? 73  LYS B CD  1 
ATOM   4687 C CE  . LYS B 1 73  ? -26.075 26.514 6.725   1.00 60.57 ? 73  LYS B CE  1 
ATOM   4688 N NZ  . LYS B 1 73  ? -25.260 25.644 7.624   1.00 60.48 ? 73  LYS B NZ  1 
ATOM   4689 N N   . ASP B 1 74  ? -23.296 32.339 8.573   1.00 23.09 ? 74  ASP B N   1 
ATOM   4690 C CA  . ASP B 1 74  ? -23.570 33.703 9.008   1.00 20.76 ? 74  ASP B CA  1 
ATOM   4691 C C   . ASP B 1 74  ? -23.182 34.674 7.895   1.00 27.31 ? 74  ASP B C   1 
ATOM   4692 O O   . ASP B 1 74  ? -22.002 34.785 7.547   1.00 24.16 ? 74  ASP B O   1 
ATOM   4693 C CB  . ASP B 1 74  ? -22.802 33.988 10.301  1.00 20.06 ? 74  ASP B CB  1 
ATOM   4694 C CG  . ASP B 1 74  ? -23.116 35.351 10.901  1.00 24.73 ? 74  ASP B CG  1 
ATOM   4695 O OD1 . ASP B 1 74  ? -23.102 36.368 10.171  1.00 19.37 ? 74  ASP B OD1 1 
ATOM   4696 O OD2 . ASP B 1 74  ? -23.342 35.405 12.125  1.00 23.19 ? 74  ASP B OD2 1 
ATOM   4697 N N   . VAL B 1 75  ? -24.175 35.399 7.373   1.00 27.41 ? 75  VAL B N   1 
ATOM   4698 C CA  . VAL B 1 75  ? -23.984 36.212 6.172   1.00 28.04 ? 75  VAL B CA  1 
ATOM   4699 C C   . VAL B 1 75  ? -23.033 37.375 6.440   1.00 27.22 ? 75  VAL B C   1 
ATOM   4700 O O   . VAL B 1 75  ? -22.086 37.607 5.676   1.00 25.96 ? 75  VAL B O   1 
ATOM   4701 C CB  . VAL B 1 75  ? -25.350 36.700 5.655   1.00 29.54 ? 75  VAL B CB  1 
ATOM   4702 C CG1 . VAL B 1 75  ? -25.186 37.904 4.734   1.00 37.82 ? 75  VAL B CG1 1 
ATOM   4703 C CG2 . VAL B 1 75  ? -26.071 35.556 4.958   1.00 26.84 ? 75  VAL B CG2 1 
ATOM   4704 N N   . PHE B 1 76  ? -23.286 38.141 7.508   1.00 22.92 ? 76  PHE B N   1 
ATOM   4705 C CA  . PHE B 1 76  ? -22.400 39.252 7.859   1.00 22.37 ? 76  PHE B CA  1 
ATOM   4706 C C   . PHE B 1 76  ? -21.018 38.750 8.240   1.00 22.86 ? 76  PHE B C   1 
ATOM   4707 O O   . PHE B 1 76  ? -20.002 39.377 7.903   1.00 24.27 ? 76  PHE B O   1 
ATOM   4708 C CB  . PHE B 1 76  ? -22.987 40.068 9.018   1.00 22.59 ? 76  PHE B CB  1 
ATOM   4709 C CG  . PHE B 1 76  ? -23.986 41.108 8.582   1.00 29.57 ? 76  PHE B CG  1 
ATOM   4710 C CD1 . PHE B 1 76  ? -25.297 40.751 8.288   1.00 23.09 ? 76  PHE B CD1 1 
ATOM   4711 C CD2 . PHE B 1 76  ? -23.612 42.438 8.455   1.00 33.68 ? 76  PHE B CD2 1 
ATOM   4712 C CE1 . PHE B 1 76  ? -26.221 41.699 7.882   1.00 28.83 ? 76  PHE B CE1 1 
ATOM   4713 C CE2 . PHE B 1 76  ? -24.533 43.395 8.050   1.00 33.58 ? 76  PHE B CE2 1 
ATOM   4714 C CZ  . PHE B 1 76  ? -25.841 43.022 7.760   1.00 31.62 ? 76  PHE B CZ  1 
ATOM   4715 N N   . LEU B 1 77  ? -20.956 37.630 8.960   1.00 21.24 ? 77  LEU B N   1 
ATOM   4716 C CA  . LEU B 1 77  ? -19.654 37.105 9.347   1.00 23.82 ? 77  LEU B CA  1 
ATOM   4717 C C   . LEU B 1 77  ? -18.876 36.639 8.127   1.00 25.83 ? 77  LEU B C   1 
ATOM   4718 O O   . LEU B 1 77  ? -17.642 36.698 8.120   1.00 28.00 ? 77  LEU B O   1 
ATOM   4719 C CB  . LEU B 1 77  ? -19.819 35.975 10.363  1.00 26.45 ? 77  LEU B CB  1 
ATOM   4720 C CG  . LEU B 1 77  ? -18.553 35.574 11.127  1.00 32.16 ? 77  LEU B CG  1 
ATOM   4721 C CD1 . LEU B 1 77  ? -17.870 36.783 11.777  1.00 25.36 ? 77  LEU B CD1 1 
ATOM   4722 C CD2 . LEU B 1 77  ? -18.882 34.529 12.169  1.00 27.06 ? 77  LEU B CD2 1 
ATOM   4723 N N   . GLU B 1 78  ? -19.582 36.203 7.080   1.00 24.40 ? 78  GLU B N   1 
ATOM   4724 C CA  . GLU B 1 78  ? -18.922 35.849 5.831   1.00 31.43 ? 78  GLU B CA  1 
ATOM   4725 C C   . GLU B 1 78  ? -18.257 37.065 5.196   1.00 27.32 ? 78  GLU B C   1 
ATOM   4726 O O   . GLU B 1 78  ? -17.157 36.961 4.641   1.00 28.91 ? 78  GLU B O   1 
ATOM   4727 C CB  . GLU B 1 78  ? -19.936 35.223 4.874   1.00 32.45 ? 78  GLU B CB  1 
ATOM   4728 C CG  . GLU B 1 78  ? -19.776 33.729 4.725   1.00 44.46 ? 78  GLU B CG  1 
ATOM   4729 C CD  . GLU B 1 78  ? -18.352 33.346 4.375   1.00 57.20 ? 78  GLU B CD  1 
ATOM   4730 O OE1 . GLU B 1 78  ? -17.766 33.987 3.476   1.00 62.93 ? 78  GLU B OE1 1 
ATOM   4731 O OE2 . GLU B 1 78  ? -17.813 32.414 5.008   1.00 62.43 ? 78  GLU B OE2 1 
ATOM   4732 N N   . ALA B 1 79  ? -18.908 38.228 5.272   1.00 25.72 ? 79  ALA B N   1 
ATOM   4733 C CA  . ALA B 1 79  ? -18.328 39.464 4.753   1.00 25.06 ? 79  ALA B CA  1 
ATOM   4734 C C   . ALA B 1 79  ? -17.125 39.925 5.566   1.00 28.39 ? 79  ALA B C   1 
ATOM   4735 O O   . ALA B 1 79  ? -16.328 40.737 5.081   1.00 24.02 ? 79  ALA B O   1 
ATOM   4736 C CB  . ALA B 1 79  ? -19.383 40.569 4.734   1.00 24.76 ? 79  ALA B CB  1 
ATOM   4737 N N   . ILE B 1 80  ? -16.999 39.450 6.800   1.00 21.78 ? 80  ILE B N   1 
ATOM   4738 C CA  . ILE B 1 80  ? -15.834 39.771 7.610   1.00 18.15 ? 80  ILE B CA  1 
ATOM   4739 C C   . ILE B 1 80  ? -14.685 38.832 7.290   1.00 24.40 ? 80  ILE B C   1 
ATOM   4740 O O   . ILE B 1 80  ? -13.534 39.262 7.170   1.00 22.00 ? 80  ILE B O   1 
ATOM   4741 C CB  . ILE B 1 80  ? -16.218 39.706 9.099   1.00 19.02 ? 80  ILE B CB  1 
ATOM   4742 C CG1 . ILE B 1 80  ? -17.255 40.779 9.426   1.00 29.53 ? 80  ILE B CG1 1 
ATOM   4743 C CG2 . ILE B 1 80  ? -14.961 39.790 9.986   1.00 19.84 ? 80  ILE B CG2 1 
ATOM   4744 C CD1 . ILE B 1 80  ? -16.675 42.038 9.980   1.00 38.65 ? 80  ILE B CD1 1 
ATOM   4745 N N   . ARG B 1 81  ? -14.982 37.541 7.127   1.00 24.32 ? 81  ARG B N   1 
ATOM   4746 C CA  . ARG B 1 81  ? -13.924 36.547 6.990   1.00 28.05 ? 81  ARG B CA  1 
ATOM   4747 C C   . ARG B 1 81  ? -13.181 36.687 5.666   1.00 26.15 ? 81  ARG B C   1 
ATOM   4748 O O   . ARG B 1 81  ? -11.948 36.604 5.634   1.00 28.35 ? 81  ARG B O   1 
ATOM   4749 C CB  . ARG B 1 81  ? -14.503 35.139 7.127   1.00 23.76 ? 81  ARG B CB  1 
ATOM   4750 C CG  . ARG B 1 81  ? -13.464 34.045 6.963   1.00 34.58 ? 81  ARG B CG  1 
ATOM   4751 C CD  . ARG B 1 81  ? -14.084 32.658 7.029   1.00 36.71 ? 81  ARG B CD  1 
ATOM   4752 N NE  . ARG B 1 81  ? -14.404 32.251 8.396   1.00 41.31 ? 81  ARG B NE  1 
ATOM   4753 C CZ  . ARG B 1 81  ? -13.506 31.845 9.290   1.00 43.32 ? 81  ARG B CZ  1 
ATOM   4754 N NH1 . ARG B 1 81  ? -12.220 31.791 8.968   1.00 48.02 ? 81  ARG B NH1 1 
ATOM   4755 N NH2 . ARG B 1 81  ? -13.894 31.489 10.510  1.00 40.46 ? 81  ARG B NH2 1 
ATOM   4756 N N   . LYS B 1 82  ? -13.910 36.918 4.570   1.00 25.40 ? 82  LYS B N   1 
ATOM   4757 C CA  . LYS B 1 82  ? -13.320 36.921 3.237   1.00 23.52 ? 82  LYS B CA  1 
ATOM   4758 C C   . LYS B 1 82  ? -12.167 37.908 3.125   1.00 24.48 ? 82  LYS B C   1 
ATOM   4759 O O   . LYS B 1 82  ? -12.170 38.979 3.736   1.00 23.21 ? 82  LYS B O   1 
ATOM   4760 C CB  . LYS B 1 82  ? -14.369 37.289 2.187   1.00 23.75 ? 82  LYS B CB  1 
ATOM   4761 C CG  . LYS B 1 82  ? -15.378 36.219 1.864   1.00 34.92 ? 82  LYS B CG  1 
ATOM   4762 C CD  . LYS B 1 82  ? -16.201 36.675 0.670   1.00 33.31 ? 82  LYS B CD  1 
ATOM   4763 C CE  . LYS B 1 82  ? -17.419 35.808 0.458   1.00 43.18 ? 82  LYS B CE  1 
ATOM   4764 N NZ  . LYS B 1 82  ? -18.261 36.382 -0.631  1.00 45.28 ? 82  LYS B NZ  1 
ATOM   4765 N N   . ASP B 1 83  ? -11.186 37.539 2.322   1.00 25.46 ? 83  ASP B N   1 
ATOM   4766 C CA  . ASP B 1 83  ? -10.243 38.517 1.805   1.00 26.75 ? 83  ASP B CA  1 
ATOM   4767 C C   . ASP B 1 83  ? -11.038 39.603 1.088   1.00 24.22 ? 83  ASP B C   1 
ATOM   4768 O O   . ASP B 1 83  ? -11.965 39.282 0.327   1.00 25.22 ? 83  ASP B O   1 
ATOM   4769 C CB  . ASP B 1 83  ? -9.252  37.849 0.853   1.00 30.56 ? 83  ASP B CB  1 
ATOM   4770 C CG  . ASP B 1 83  ? -8.077  38.747 0.494   1.00 38.28 ? 83  ASP B CG  1 
ATOM   4771 O OD1 . ASP B 1 83  ? -8.298  39.817 -0.115  1.00 32.39 ? 83  ASP B OD1 1 
ATOM   4772 O OD2 . ASP B 1 83  ? -6.924  38.372 0.802   1.00 39.99 ? 83  ASP B OD2 1 
ATOM   4773 N N   . PRO B 1 84  ? -10.752 40.884 1.333   1.00 24.99 ? 84  PRO B N   1 
ATOM   4774 C CA  . PRO B 1 84  ? -11.554 41.942 0.696   1.00 23.59 ? 84  PRO B CA  1 
ATOM   4775 C C   . PRO B 1 84  ? -11.578 41.862 -0.822  1.00 28.02 ? 84  PRO B C   1 
ATOM   4776 O O   . PRO B 1 84  ? -12.558 42.316 -1.427  1.00 30.83 ? 84  PRO B O   1 
ATOM   4777 C CB  . PRO B 1 84  ? -10.884 43.230 1.193   1.00 29.58 ? 84  PRO B CB  1 
ATOM   4778 C CG  . PRO B 1 84  ? -10.360 42.842 2.565   1.00 23.09 ? 84  PRO B CG  1 
ATOM   4779 C CD  . PRO B 1 84  ? -9.843  41.427 2.363   1.00 23.69 ? 84  PRO B CD  1 
ATOM   4780 N N   . ASP B 1 85  ? -10.554 41.268 -1.448  1.00 30.04 ? 85  ASP B N   1 
ATOM   4781 C CA  . ASP B 1 85  ? -10.569 41.056 -2.895  1.00 33.47 ? 85  ASP B CA  1 
ATOM   4782 C C   . ASP B 1 85  ? -11.736 40.176 -3.336  1.00 25.36 ? 85  ASP B C   1 
ATOM   4783 O O   . ASP B 1 85  ? -12.156 40.240 -4.499  1.00 25.75 ? 85  ASP B O   1 
ATOM   4784 C CB  . ASP B 1 85  ? -9.253  40.419 -3.353  1.00 39.50 ? 85  ASP B CB  1 
ATOM   4785 C CG  . ASP B 1 85  ? -8.086  41.398 -3.364  1.00 41.37 ? 85  ASP B CG  1 
ATOM   4786 O OD1 . ASP B 1 85  ? -8.321  42.626 -3.330  1.00 34.74 ? 85  ASP B OD1 1 
ATOM   4787 O OD2 . ASP B 1 85  ? -6.929  40.931 -3.423  1.00 38.88 ? 85  ASP B OD2 1 
ATOM   4788 N N   . ASP B 1 86  ? -12.241 39.326 -2.445  1.00 24.76 ? 86  ASP B N   1 
ATOM   4789 C CA  . ASP B 1 86  ? -13.350 38.429 -2.738  1.00 28.60 ? 86  ASP B CA  1 
ATOM   4790 C C   . ASP B 1 86  ? -14.703 39.007 -2.340  1.00 26.94 ? 86  ASP B C   1 
ATOM   4791 O O   . ASP B 1 86  ? -15.724 38.350 -2.559  1.00 28.98 ? 86  ASP B O   1 
ATOM   4792 C CB  . ASP B 1 86  ? -13.161 37.081 -2.024  1.00 30.23 ? 86  ASP B CB  1 
ATOM   4793 C CG  . ASP B 1 86  ? -11.817 36.433 -2.321  1.00 38.22 ? 86  ASP B CG  1 
ATOM   4794 O OD1 . ASP B 1 86  ? -11.222 36.738 -3.374  1.00 41.27 ? 86  ASP B OD1 1 
ATOM   4795 O OD2 . ASP B 1 86  ? -11.359 35.610 -1.494  1.00 39.37 ? 86  ASP B OD2 1 
ATOM   4796 N N   . LEU B 1 87  ? -14.736 40.199 -1.748  1.00 22.59 ? 87  LEU B N   1 
ATOM   4797 C CA  . LEU B 1 87  ? -15.991 40.782 -1.286  1.00 21.69 ? 87  LEU B CA  1 
ATOM   4798 C C   . LEU B 1 87  ? -16.873 41.201 -2.460  1.00 24.90 ? 87  LEU B C   1 
ATOM   4799 O O   . LEU B 1 87  ? -16.408 41.848 -3.405  1.00 24.67 ? 87  LEU B O   1 
ATOM   4800 C CB  . LEU B 1 87  ? -15.719 41.995 -0.403  1.00 21.05 ? 87  LEU B CB  1 
ATOM   4801 C CG  . LEU B 1 87  ? -15.270 41.686 1.017   1.00 20.27 ? 87  LEU B CG  1 
ATOM   4802 C CD1 . LEU B 1 87  ? -14.900 42.973 1.753   1.00 23.70 ? 87  LEU B CD1 1 
ATOM   4803 C CD2 . LEU B 1 87  ? -16.373 40.951 1.770   1.00 23.17 ? 87  LEU B CD2 1 
ATOM   4804 N N   . GLU B 1 88  ? -18.154 40.838 -2.381  1.00 23.29 ? 88  GLU B N   1 
ATOM   4805 C CA  . GLU B 1 88  ? -19.154 41.380 -3.285  1.00 26.80 ? 88  GLU B CA  1 
ATOM   4806 C C   . GLU B 1 88  ? -19.460 42.819 -2.894  1.00 22.22 ? 88  GLU B C   1 
ATOM   4807 O O   . GLU B 1 88  ? -19.323 43.207 -1.730  1.00 21.37 ? 88  GLU B O   1 
ATOM   4808 C CB  . GLU B 1 88  ? -20.432 40.532 -3.231  1.00 27.97 ? 88  GLU B CB  1 
ATOM   4809 C CG  . GLU B 1 88  ? -20.169 39.032 -3.311  1.00 31.54 ? 88  GLU B CG  1 
ATOM   4810 C CD  . GLU B 1 88  ? -21.380 38.186 -2.957  1.00 39.21 ? 88  GLU B CD  1 
ATOM   4811 O OE1 . GLU B 1 88  ? -21.391 36.990 -3.322  1.00 44.53 ? 88  GLU B OE1 1 
ATOM   4812 O OE2 . GLU B 1 88  ? -22.318 38.712 -2.324  1.00 36.53 ? 88  GLU B OE2 1 
ATOM   4813 N N   . LYS B 1 89  ? -19.874 43.616 -3.880  1.00 22.95 ? 89  LYS B N   1 
ATOM   4814 C CA  . LYS B 1 89  ? -20.291 44.985 -3.588  1.00 29.60 ? 89  LYS B CA  1 
ATOM   4815 C C   . LYS B 1 89  ? -21.318 45.018 -2.460  1.00 29.97 ? 89  LYS B C   1 
ATOM   4816 O O   . LYS B 1 89  ? -21.222 45.847 -1.545  1.00 27.49 ? 89  LYS B O   1 
ATOM   4817 C CB  . LYS B 1 89  ? -20.857 45.652 -4.847  1.00 25.86 ? 89  LYS B CB  1 
ATOM   4818 C CG  . LYS B 1 89  ? -20.002 45.507 -6.098  1.00 31.82 ? 89  LYS B CG  1 
ATOM   4819 C CD  . LYS B 1 89  ? -20.708 46.126 -7.321  1.00 36.70 ? 89  LYS B CD  1 
ATOM   4820 C CE  . LYS B 1 89  ? -19.998 45.804 -8.637  1.00 40.10 ? 89  LYS B CE  1 
ATOM   4821 N NZ  . LYS B 1 89  ? -18.547 46.112 -8.614  1.00 39.65 ? 89  LYS B NZ  1 
ATOM   4822 N N   . GLU B 1 90  ? -22.291 44.098 -2.490  1.00 23.99 ? 90  GLU B N   1 
ATOM   4823 C CA  . GLU B 1 90  ? -23.306 44.058 -1.440  1.00 23.69 ? 90  GLU B CA  1 
ATOM   4824 C C   . GLU B 1 90  ? -22.708 43.748 -0.070  1.00 23.07 ? 90  GLU B C   1 
ATOM   4825 O O   . GLU B 1 90  ? -23.247 44.187 0.954   1.00 24.35 ? 90  GLU B O   1 
ATOM   4826 C CB  . GLU B 1 90  ? -24.385 43.029 -1.789  1.00 30.13 ? 90  GLU B CB  1 
ATOM   4827 C CG  . GLU B 1 90  ? -25.115 43.319 -3.093  1.00 43.69 ? 90  GLU B CG  1 
ATOM   4828 C CD  . GLU B 1 90  ? -26.249 42.345 -3.368  1.00 54.32 ? 90  GLU B CD  1 
ATOM   4829 O OE1 . GLU B 1 90  ? -27.120 42.659 -4.209  1.00 58.55 ? 90  GLU B OE1 1 
ATOM   4830 O OE2 . GLU B 1 90  ? -26.276 41.268 -2.736  1.00 58.17 ? 90  GLU B OE2 1 
ATOM   4831 N N   . GLU B 1 91  ? -21.614 42.982 -0.024  1.00 24.93 ? 91  GLU B N   1 
ATOM   4832 C CA  . GLU B 1 91  ? -20.974 42.682 1.252   1.00 22.59 ? 91  GLU B CA  1 
ATOM   4833 C C   . GLU B 1 91  ? -20.187 43.879 1.769   1.00 21.38 ? 91  GLU B C   1 
ATOM   4834 O O   . GLU B 1 91  ? -20.150 44.126 2.979   1.00 21.74 ? 91  GLU B O   1 
ATOM   4835 C CB  . GLU B 1 91  ? -20.064 41.463 1.121   1.00 22.24 ? 91  GLU B CB  1 
ATOM   4836 C CG  . GLU B 1 91  ? -20.828 40.138 0.971   1.00 23.34 ? 91  GLU B CG  1 
ATOM   4837 C CD  . GLU B 1 91  ? -19.918 38.963 0.665   1.00 29.67 ? 91  GLU B CD  1 
ATOM   4838 O OE1 . GLU B 1 91  ? -19.083 39.072 -0.258  1.00 25.52 ? 91  GLU B OE1 1 
ATOM   4839 O OE2 . GLU B 1 91  ? -20.034 37.928 1.359   1.00 30.75 ? 91  GLU B OE2 1 
ATOM   4840 N N   . VAL B 1 92  ? -19.561 44.637 0.871   1.00 22.47 ? 92  VAL B N   1 
ATOM   4841 C CA  . VAL B 1 92  ? -18.920 45.875 1.299   1.00 24.79 ? 92  VAL B CA  1 
ATOM   4842 C C   . VAL B 1 92  ? -19.965 46.821 1.875   1.00 23.72 ? 92  VAL B C   1 
ATOM   4843 O O   . VAL B 1 92  ? -19.756 47.436 2.929   1.00 21.86 ? 92  VAL B O   1 
ATOM   4844 C CB  . VAL B 1 92  ? -18.152 46.513 0.126   1.00 23.88 ? 92  VAL B CB  1 
ATOM   4845 C CG1 . VAL B 1 92  ? -17.523 47.844 0.550   1.00 25.57 ? 92  VAL B CG1 1 
ATOM   4846 C CG2 . VAL B 1 92  ? -17.084 45.556 -0.382  1.00 26.30 ? 92  VAL B CG2 1 
ATOM   4847 N N   . GLU B 1 93  ? -21.118 46.926 1.205   1.00 24.65 ? 93  GLU B N   1 
ATOM   4848 C CA  . GLU B 1 93  ? -22.222 47.744 1.703   1.00 24.31 ? 93  GLU B CA  1 
ATOM   4849 C C   . GLU B 1 93  ? -22.636 47.328 3.110   1.00 23.02 ? 93  GLU B C   1 
ATOM   4850 O O   . GLU B 1 93  ? -22.755 48.172 4.003   1.00 23.97 ? 93  GLU B O   1 
ATOM   4851 C CB  . GLU B 1 93  ? -23.414 47.652 0.748   1.00 26.34 ? 93  GLU B CB  1 
ATOM   4852 C CG  . GLU B 1 93  ? -23.225 48.397 -0.564  1.00 43.07 ? 93  GLU B CG  1 
ATOM   4853 C CD  . GLU B 1 93  ? -24.289 48.050 -1.601  1.00 49.78 ? 93  GLU B CD  1 
ATOM   4854 O OE1 . GLU B 1 93  ? -25.406 47.640 -1.215  1.00 54.72 ? 93  GLU B OE1 1 
ATOM   4855 O OE2 . GLU B 1 93  ? -24.006 48.195 -2.806  1.00 59.08 ? 93  GLU B OE2 1 
ATOM   4856 N N   . LYS B 1 94  ? -22.864 46.026 3.323   1.00 22.60 ? 94  LYS B N   1 
ATOM   4857 C CA  . LYS B 1 94  ? -23.229 45.533 4.649   1.00 25.61 ? 94  LYS B CA  1 
ATOM   4858 C C   . LYS B 1 94  ? -22.168 45.871 5.690   1.00 22.79 ? 94  LYS B C   1 
ATOM   4859 O O   . LYS B 1 94  ? -22.495 46.249 6.823   1.00 20.26 ? 94  LYS B O   1 
ATOM   4860 C CB  . LYS B 1 94  ? -23.446 44.019 4.608   1.00 28.34 ? 94  LYS B CB  1 
ATOM   4861 C CG  . LYS B 1 94  ? -24.744 43.589 3.964   1.00 31.42 ? 94  LYS B CG  1 
ATOM   4862 C CD  . LYS B 1 94  ? -24.980 42.099 4.146   1.00 42.96 ? 94  LYS B CD  1 
ATOM   4863 C CE  . LYS B 1 94  ? -26.345 41.693 3.602   1.00 49.21 ? 94  LYS B CE  1 
ATOM   4864 N NZ  . LYS B 1 94  ? -26.515 42.095 2.177   1.00 49.77 ? 94  LYS B NZ  1 
ATOM   4865 N N   . LEU B 1 95  ? -20.891 45.699 5.341   1.00 20.89 ? 95  LEU B N   1 
ATOM   4866 C CA  . LEU B 1 95  ? -19.818 45.989 6.289   1.00 23.07 ? 95  LEU B CA  1 
ATOM   4867 C C   . LEU B 1 95  ? -19.839 47.452 6.711   1.00 20.93 ? 95  LEU B C   1 
ATOM   4868 O O   . LEU B 1 95  ? -19.723 47.766 7.904   1.00 21.74 ? 95  LEU B O   1 
ATOM   4869 C CB  . LEU B 1 95  ? -18.472 45.626 5.663   1.00 23.28 ? 95  LEU B CB  1 
ATOM   4870 C CG  . LEU B 1 95  ? -17.203 45.639 6.513   1.00 34.73 ? 95  LEU B CG  1 
ATOM   4871 C CD1 . LEU B 1 95  ? -17.278 44.586 7.598   1.00 38.13 ? 95  LEU B CD1 1 
ATOM   4872 C CD2 . LEU B 1 95  ? -15.971 45.414 5.632   1.00 39.58 ? 95  LEU B CD2 1 
ATOM   4873 N N   . ILE B 1 96  ? -19.997 48.361 5.746   1.00 22.35 ? 96  ILE B N   1 
ATOM   4874 C CA  . ILE B 1 96  ? -20.010 49.786 6.057   1.00 20.50 ? 96  ILE B CA  1 
ATOM   4875 C C   . ILE B 1 96  ? -21.262 50.154 6.852   1.00 22.28 ? 96  ILE B C   1 
ATOM   4876 O O   . ILE B 1 96  ? -21.185 50.907 7.832   1.00 23.20 ? 96  ILE B O   1 
ATOM   4877 C CB  . ILE B 1 96  ? -19.875 50.608 4.762   1.00 22.51 ? 96  ILE B CB  1 
ATOM   4878 C CG1 . ILE B 1 96  ? -18.474 50.418 4.167   1.00 27.74 ? 96  ILE B CG1 1 
ATOM   4879 C CG2 . ILE B 1 96  ? -20.125 52.088 5.036   1.00 23.96 ? 96  ILE B CG2 1 
ATOM   4880 C CD1 . ILE B 1 96  ? -18.341 50.836 2.712   1.00 30.51 ? 96  ILE B CD1 1 
ATOM   4881 N N   . GLU B 1 97  ? -22.427 49.616 6.463   1.00 25.75 ? 97  GLU B N   1 
ATOM   4882 C CA  . GLU B 1 97  ? -23.656 49.858 7.221   1.00 25.25 ? 97  GLU B CA  1 
ATOM   4883 C C   . GLU B 1 97  ? -23.541 49.353 8.649   1.00 23.02 ? 97  GLU B C   1 
ATOM   4884 O O   . GLU B 1 97  ? -24.020 50.003 9.588   1.00 24.81 ? 97  GLU B O   1 
ATOM   4885 C CB  . GLU B 1 97  ? -24.850 49.172 6.557   1.00 26.73 ? 97  GLU B CB  1 
ATOM   4886 C CG  . GLU B 1 97  ? -25.219 49.647 5.177   1.00 46.42 ? 97  GLU B CG  1 
ATOM   4887 C CD  . GLU B 1 97  ? -26.319 48.789 4.574   1.00 62.49 ? 97  GLU B CD  1 
ATOM   4888 O OE1 . GLU B 1 97  ? -27.319 48.524 5.279   1.00 65.70 ? 97  GLU B OE1 1 
ATOM   4889 O OE2 . GLU B 1 97  ? -26.177 48.368 3.406   1.00 67.64 ? 97  GLU B OE2 1 
ATOM   4890 N N   . PHE B 1 98  ? -22.970 48.158 8.829   1.00 19.56 ? 98  PHE B N   1 
ATOM   4891 C CA  . PHE B 1 98  ? -22.821 47.618 10.175  1.00 20.20 ? 98  PHE B CA  1 
ATOM   4892 C C   . PHE B 1 98  ? -21.919 48.516 11.011  1.00 21.78 ? 98  PHE B C   1 
ATOM   4893 O O   . PHE B 1 98  ? -22.203 48.782 12.188  1.00 19.24 ? 98  PHE B O   1 
ATOM   4894 C CB  . PHE B 1 98  ? -22.266 46.194 10.115  1.00 21.50 ? 98  PHE B CB  1 
ATOM   4895 C CG  . PHE B 1 98  ? -22.334 45.457 11.425  1.00 20.01 ? 98  PHE B CG  1 
ATOM   4896 C CD1 . PHE B 1 98  ? -23.518 44.878 11.851  1.00 16.57 ? 98  PHE B CD1 1 
ATOM   4897 C CD2 . PHE B 1 98  ? -21.208 45.322 12.217  1.00 19.46 ? 98  PHE B CD2 1 
ATOM   4898 C CE1 . PHE B 1 98  ? -23.579 44.194 13.066  1.00 17.81 ? 98  PHE B CE1 1 
ATOM   4899 C CE2 . PHE B 1 98  ? -21.257 44.636 13.427  1.00 18.40 ? 98  PHE B CE2 1 
ATOM   4900 C CZ  . PHE B 1 98  ? -22.447 44.075 13.852  1.00 21.84 ? 98  PHE B CZ  1 
ATOM   4901 N N   . THR B 1 99  ? -20.830 49.001 10.412  1.00 20.28 ? 99  THR B N   1 
ATOM   4902 C CA  . THR B 1 99  ? -19.943 49.909 11.128  1.00 19.32 ? 99  THR B CA  1 
ATOM   4903 C C   . THR B 1 99  ? -20.675 51.186 11.513  1.00 20.36 ? 99  THR B C   1 
ATOM   4904 O O   . THR B 1 99  ? -20.563 51.665 12.649  1.00 21.67 ? 99  THR B O   1 
ATOM   4905 C CB  . THR B 1 99  ? -18.721 50.243 10.270  1.00 20.97 ? 99  THR B CB  1 
ATOM   4906 O OG1 . THR B 1 99  ? -18.088 49.035 9.836   1.00 20.67 ? 99  THR B OG1 1 
ATOM   4907 C CG2 . THR B 1 99  ? -17.733 51.054 11.075  1.00 20.81 ? 99  THR B CG2 1 
ATOM   4908 N N   . LYS B 1 100 ? -21.427 51.751 10.567  1.00 21.21 ? 100 LYS B N   1 
ATOM   4909 C CA  . LYS B 1 100 ? -22.137 53.000 10.827  1.00 24.98 ? 100 LYS B CA  1 
ATOM   4910 C C   . LYS B 1 100 ? -23.130 52.843 11.967  1.00 22.30 ? 100 LYS B C   1 
ATOM   4911 O O   . LYS B 1 100 ? -23.305 53.762 12.779  1.00 24.06 ? 100 LYS B O   1 
ATOM   4912 C CB  . LYS B 1 100 ? -22.847 53.471 9.557   1.00 28.77 ? 100 LYS B CB  1 
ATOM   4913 C CG  . LYS B 1 100 ? -22.088 54.545 8.807   1.00 38.63 ? 100 LYS B CG  1 
ATOM   4914 C CD  . LYS B 1 100 ? -22.565 54.701 7.380   1.00 45.62 ? 100 LYS B CD  1 
ATOM   4915 C CE  . LYS B 1 100 ? -21.762 55.777 6.659   1.00 51.23 ? 100 LYS B CE  1 
ATOM   4916 N NZ  . LYS B 1 100 ? -21.987 55.757 5.186   1.00 55.39 ? 100 LYS B NZ  1 
ATOM   4917 N N   . LEU B 1 101 ? -23.794 51.685 12.040  1.00 21.15 ? 101 LEU B N   1 
ATOM   4918 C CA  . LEU B 1 101 ? -24.772 51.445 13.097  1.00 22.49 ? 101 LEU B CA  1 
ATOM   4919 C C   . LEU B 1 101 ? -24.115 51.433 14.469  1.00 19.67 ? 101 LEU B C   1 
ATOM   4920 O O   . LEU B 1 101 ? -24.705 51.891 15.455  1.00 20.12 ? 101 LEU B O   1 
ATOM   4921 C CB  . LEU B 1 101 ? -25.495 50.118 12.840  1.00 25.53 ? 101 LEU B CB  1 
ATOM   4922 C CG  . LEU B 1 101 ? -26.445 49.638 13.945  1.00 25.54 ? 101 LEU B CG  1 
ATOM   4923 C CD1 . LEU B 1 101 ? -27.659 50.560 14.073  1.00 27.61 ? 101 LEU B CD1 1 
ATOM   4924 C CD2 . LEU B 1 101 ? -26.882 48.181 13.727  1.00 23.36 ? 101 LEU B CD2 1 
ATOM   4925 N N   . ASN B 1 102 ? -22.895 50.914 14.554  1.00 16.74 ? 102 ASN B N   1 
ATOM   4926 C CA  . ASN B 1 102 ? -22.201 50.725 15.820  1.00 15.16 ? 102 ASN B CA  1 
ATOM   4927 C C   . ASN B 1 102 ? -21.209 51.842 16.130  1.00 21.97 ? 102 ASN B C   1 
ATOM   4928 O O   . ASN B 1 102 ? -20.609 51.839 17.214  1.00 21.91 ? 102 ASN B O   1 
ATOM   4929 C CB  . ASN B 1 102 ? -21.476 49.375 15.797  1.00 19.59 ? 102 ASN B CB  1 
ATOM   4930 C CG  . ASN B 1 102 ? -22.434 48.199 15.878  1.00 22.74 ? 102 ASN B CG  1 
ATOM   4931 O OD1 . ASN B 1 102 ? -23.147 48.035 16.865  1.00 22.07 ? 102 ASN B OD1 1 
ATOM   4932 N ND2 . ASN B 1 102 ? -22.446 47.367 14.842  1.00 21.93 ? 102 ASN B ND2 1 
ATOM   4933 N N   . TYR B 1 103 ? -21.079 52.816 15.225  1.00 21.49 ? 103 TYR B N   1 
ATOM   4934 C CA  . TYR B 1 103 ? -19.937 53.732 15.202  1.00 19.59 ? 103 TYR B CA  1 
ATOM   4935 C C   . TYR B 1 103 ? -19.799 54.526 16.499  1.00 22.46 ? 103 TYR B C   1 
ATOM   4936 O O   . TYR B 1 103 ? -18.679 54.793 16.955  1.00 28.35 ? 103 TYR B O   1 
ATOM   4937 C CB  . TYR B 1 103 ? -20.093 54.673 13.999  1.00 25.33 ? 103 TYR B CB  1 
ATOM   4938 C CG  . TYR B 1 103 ? -18.975 55.659 13.774  1.00 28.67 ? 103 TYR B CG  1 
ATOM   4939 C CD1 . TYR B 1 103 ? -17.788 55.273 13.170  1.00 28.87 ? 103 TYR B CD1 1 
ATOM   4940 C CD2 . TYR B 1 103 ? -19.119 56.989 14.147  1.00 30.91 ? 103 TYR B CD2 1 
ATOM   4941 C CE1 . TYR B 1 103 ? -16.765 56.185 12.959  1.00 32.25 ? 103 TYR B CE1 1 
ATOM   4942 C CE2 . TYR B 1 103 ? -18.110 57.908 13.934  1.00 33.32 ? 103 TYR B CE2 1 
ATOM   4943 C CZ  . TYR B 1 103 ? -16.936 57.501 13.341  1.00 35.36 ? 103 TYR B CZ  1 
ATOM   4944 O OH  . TYR B 1 103 ? -15.928 58.416 13.138  1.00 30.67 ? 103 TYR B OH  1 
ATOM   4945 N N   . GLU B 1 104 ? -20.915 54.918 17.104  1.00 21.18 ? 104 GLU B N   1 
ATOM   4946 C CA  . GLU B 1 104 ? -20.862 55.803 18.265  1.00 22.54 ? 104 GLU B CA  1 
ATOM   4947 C C   . GLU B 1 104 ? -20.730 55.053 19.586  1.00 22.20 ? 104 GLU B C   1 
ATOM   4948 O O   . GLU B 1 104 ? -20.597 55.696 20.635  1.00 22.88 ? 104 GLU B O   1 
ATOM   4949 C CB  . GLU B 1 104 ? -22.107 56.698 18.310  1.00 26.43 ? 104 GLU B CB  1 
ATOM   4950 C CG  . GLU B 1 104 ? -22.308 57.569 17.069  1.00 43.12 ? 104 GLU B CG  1 
ATOM   4951 C CD  . GLU B 1 104 ? -21.300 58.701 16.968  1.00 51.59 ? 104 GLU B CD  1 
ATOM   4952 O OE1 . GLU B 1 104 ? -21.121 59.255 15.858  1.00 57.79 ? 104 GLU B OE1 1 
ATOM   4953 O OE2 . GLU B 1 104 ? -20.686 59.041 17.999  1.00 56.84 ? 104 GLU B OE2 1 
ATOM   4954 N N   . LYS B 1 105 ? -20.763 53.728 19.568  1.00 22.72 ? 105 LYS B N   1 
ATOM   4955 C CA  . LYS B 1 105 ? -20.669 52.978 20.809  1.00 22.53 ? 105 LYS B CA  1 
ATOM   4956 C C   . LYS B 1 105 ? -19.233 53.004 21.327  1.00 25.92 ? 105 LYS B C   1 
ATOM   4957 O O   . LYS B 1 105 ? -18.288 52.944 20.537  1.00 21.41 ? 105 LYS B O   1 
ATOM   4958 C CB  . LYS B 1 105 ? -21.123 51.535 20.600  1.00 17.60 ? 105 LYS B CB  1 
ATOM   4959 C CG  . LYS B 1 105 ? -22.579 51.442 20.164  1.00 19.60 ? 105 LYS B CG  1 
ATOM   4960 C CD  . LYS B 1 105 ? -22.970 50.024 19.764  1.00 18.71 ? 105 LYS B CD  1 
ATOM   4961 C CE  . LYS B 1 105 ? -24.427 49.979 19.322  1.00 19.09 ? 105 LYS B CE  1 
ATOM   4962 N NZ  . LYS B 1 105 ? -24.865 48.600 18.940  1.00 20.16 ? 105 LYS B NZ  1 
ATOM   4963 N N   . PRO B 1 106 ? -19.037 53.106 22.644  1.00 20.18 ? 106 PRO B N   1 
ATOM   4964 C CA  . PRO B 1 106 ? -17.664 53.138 23.173  1.00 20.85 ? 106 PRO B CA  1 
ATOM   4965 C C   . PRO B 1 106 ? -16.809 51.955 22.743  1.00 19.55 ? 106 PRO B C   1 
ATOM   4966 O O   . PRO B 1 106 ? -15.593 52.119 22.575  1.00 25.18 ? 106 PRO B O   1 
ATOM   4967 C CB  . PRO B 1 106 ? -17.879 53.160 24.693  1.00 29.63 ? 106 PRO B CB  1 
ATOM   4968 C CG  . PRO B 1 106 ? -19.225 53.788 24.879  1.00 29.15 ? 106 PRO B CG  1 
ATOM   4969 C CD  . PRO B 1 106 ? -20.049 53.339 23.689  1.00 21.95 ? 106 PRO B CD  1 
ATOM   4970 N N   . ILE B 1 107 ? -17.393 50.771 22.538  1.00 19.40 ? 107 ILE B N   1 
ATOM   4971 C CA  . ILE B 1 107 ? -16.575 49.631 22.133  1.00 18.25 ? 107 ILE B CA  1 
ATOM   4972 C C   . ILE B 1 107 ? -16.069 49.761 20.707  1.00 20.92 ? 107 ILE B C   1 
ATOM   4973 O O   . ILE B 1 107 ? -15.138 49.043 20.322  1.00 21.08 ? 107 ILE B O   1 
ATOM   4974 C CB  . ILE B 1 107 ? -17.307 48.279 22.292  1.00 16.57 ? 107 ILE B CB  1 
ATOM   4975 C CG1 . ILE B 1 107 ? -18.622 48.263 21.519  1.00 17.32 ? 107 ILE B CG1 1 
ATOM   4976 C CG2 . ILE B 1 107 ? -17.532 47.962 23.778  1.00 18.42 ? 107 ILE B CG2 1 
ATOM   4977 C CD1 . ILE B 1 107 ? -19.172 46.858 21.320  1.00 23.08 ? 107 ILE B CD1 1 
ATOM   4978 N N   . TYR B 1 108 ? -16.616 50.698 19.932  1.00 18.06 ? 108 TYR B N   1 
ATOM   4979 C CA  . TYR B 1 108 ? -16.132 50.966 18.584  1.00 20.91 ? 108 TYR B CA  1 
ATOM   4980 C C   . TYR B 1 108 ? -15.164 52.142 18.524  1.00 19.64 ? 108 TYR B C   1 
ATOM   4981 O O   . TYR B 1 108 ? -14.884 52.643 17.431  1.00 23.95 ? 108 TYR B O   1 
ATOM   4982 C CB  . TYR B 1 108 ? -17.309 51.212 17.637  1.00 24.56 ? 108 TYR B CB  1 
ATOM   4983 C CG  . TYR B 1 108 ? -17.742 49.954 16.939  1.00 17.68 ? 108 TYR B CG  1 
ATOM   4984 C CD1 . TYR B 1 108 ? -18.419 48.959 17.630  1.00 18.41 ? 108 TYR B CD1 1 
ATOM   4985 C CD2 . TYR B 1 108 ? -17.447 49.740 15.600  1.00 19.99 ? 108 TYR B CD2 1 
ATOM   4986 C CE1 . TYR B 1 108 ? -18.800 47.794 17.008  1.00 18.28 ? 108 TYR B CE1 1 
ATOM   4987 C CE2 . TYR B 1 108 ? -17.826 48.571 14.968  1.00 17.39 ? 108 TYR B CE2 1 
ATOM   4988 C CZ  . TYR B 1 108 ? -18.504 47.604 15.678  1.00 19.86 ? 108 TYR B CZ  1 
ATOM   4989 O OH  . TYR B 1 108 ? -18.887 46.444 15.053  1.00 21.08 ? 108 TYR B OH  1 
ATOM   4990 N N   . ARG B 1 109 ? -14.641 52.591 19.665  1.00 23.14 ? 109 ARG B N   1 
ATOM   4991 C CA  . ARG B 1 109 ? -13.790 53.782 19.704  1.00 26.35 ? 109 ARG B CA  1 
ATOM   4992 C C   . ARG B 1 109 ? -12.354 53.400 19.340  1.00 28.30 ? 109 ARG B C   1 
ATOM   4993 O O   . ARG B 1 109 ? -11.459 53.300 20.181  1.00 31.72 ? 109 ARG B O   1 
ATOM   4994 C CB  . ARG B 1 109 ? -13.866 54.456 21.069  1.00 28.58 ? 109 ARG B CB  1 
ATOM   4995 C CG  . ARG B 1 109 ? -13.527 55.939 21.049  1.00 43.04 ? 109 ARG B CG  1 
ATOM   4996 C CD  . ARG B 1 109 ? -13.631 56.562 22.438  1.00 54.75 ? 109 ARG B CD  1 
ATOM   4997 N NE  . ARG B 1 109 ? -15.014 56.710 22.887  1.00 59.71 ? 109 ARG B NE  1 
ATOM   4998 C CZ  . ARG B 1 109 ? -15.462 56.305 24.073  1.00 60.89 ? 109 ARG B CZ  1 
ATOM   4999 N NH1 . ARG B 1 109 ? -14.635 55.723 24.932  1.00 59.86 ? 109 ARG B NH1 1 
ATOM   5000 N NH2 . ARG B 1 109 ? -16.735 56.485 24.401  1.00 60.97 ? 109 ARG B NH2 1 
ATOM   5001 N N   . PHE B 1 110 ? -12.152 53.166 18.048  1.00 21.20 ? 110 PHE B N   1 
ATOM   5002 C CA  . PHE B 1 110 ? -10.826 52.990 17.473  1.00 25.77 ? 110 PHE B CA  1 
ATOM   5003 C C   . PHE B 1 110 ? -10.559 54.151 16.532  1.00 24.75 ? 110 PHE B C   1 
ATOM   5004 O O   . PHE B 1 110 ? -11.392 54.461 15.672  1.00 27.49 ? 110 PHE B O   1 
ATOM   5005 C CB  . PHE B 1 110 ? -10.713 51.673 16.702  1.00 28.72 ? 110 PHE B CB  1 
ATOM   5006 C CG  . PHE B 1 110 ? -10.838 50.451 17.555  1.00 24.87 ? 110 PHE B CG  1 
ATOM   5007 C CD1 . PHE B 1 110 ? -9.724  49.894 18.153  1.00 24.19 ? 110 PHE B CD1 1 
ATOM   5008 C CD2 . PHE B 1 110 ? -12.065 49.832 17.726  1.00 28.29 ? 110 PHE B CD2 1 
ATOM   5009 C CE1 . PHE B 1 110 ? -9.831  48.751 18.927  1.00 24.24 ? 110 PHE B CE1 1 
ATOM   5010 C CE2 . PHE B 1 110 ? -12.180 48.694 18.500  1.00 31.57 ? 110 PHE B CE2 1 
ATOM   5011 C CZ  . PHE B 1 110 ? -11.065 48.155 19.103  1.00 29.33 ? 110 PHE B CZ  1 
ATOM   5012 N N   . GLU B 1 111 ? -9.400  54.789 16.696  1.00 24.92 ? 111 GLU B N   1 
ATOM   5013 C CA  . GLU B 1 111 ? -9.033  55.883 15.807  1.00 33.34 ? 111 GLU B CA  1 
ATOM   5014 C C   . GLU B 1 111 ? -9.079  55.444 14.349  1.00 30.64 ? 111 GLU B C   1 
ATOM   5015 O O   . GLU B 1 111 ? -9.511  56.205 13.477  1.00 25.84 ? 111 GLU B O   1 
ATOM   5016 C CB  . GLU B 1 111 ? -7.642  56.400 16.165  1.00 32.90 ? 111 GLU B CB  1 
ATOM   5017 C CG  . GLU B 1 111 ? -7.174  57.567 15.313  1.00 50.22 ? 111 GLU B CG  1 
ATOM   5018 C CD  . GLU B 1 111 ? -8.152  58.726 15.331  1.00 65.28 ? 111 GLU B CD  1 
ATOM   5019 O OE1 . GLU B 1 111 ? -8.487  59.239 14.242  1.00 71.17 ? 111 GLU B OE1 1 
ATOM   5020 O OE2 . GLU B 1 111 ? -8.591  59.118 16.435  1.00 70.25 ? 111 GLU B OE2 1 
ATOM   5021 N N   . ARG B 1 112 ? -8.656  54.209 14.069  1.00 26.36 ? 112 ARG B N   1 
ATOM   5022 C CA  . ARG B 1 112 ? -8.611  53.757 12.683  1.00 28.11 ? 112 ARG B CA  1 
ATOM   5023 C C   . ARG B 1 112 ? -10.004 53.679 12.074  1.00 25.33 ? 112 ARG B C   1 
ATOM   5024 O O   . ARG B 1 112 ? -10.175 53.957 10.881  1.00 26.56 ? 112 ARG B O   1 
ATOM   5025 C CB  . ARG B 1 112 ? -7.893  52.407 12.607  1.00 26.83 ? 112 ARG B CB  1 
ATOM   5026 C CG  . ARG B 1 112 ? -7.785  51.809 11.209  1.00 25.03 ? 112 ARG B CG  1 
ATOM   5027 C CD  . ARG B 1 112 ? -7.108  52.755 10.226  1.00 27.24 ? 112 ARG B CD  1 
ATOM   5028 N NE  . ARG B 1 112 ? -6.614  52.028 9.059   1.00 26.45 ? 112 ARG B NE  1 
ATOM   5029 C CZ  . ARG B 1 112 ? -6.250  52.595 7.912   1.00 31.45 ? 112 ARG B CZ  1 
ATOM   5030 N NH1 . ARG B 1 112 ? -6.323  53.910 7.762   1.00 38.38 ? 112 ARG B NH1 1 
ATOM   5031 N NH2 . ARG B 1 112 ? -5.812  51.844 6.909   1.00 34.40 ? 112 ARG B NH2 1 
ATOM   5032 N N   . ILE B 1 113 ? -11.011 53.328 12.876  1.00 22.78 ? 113 ILE B N   1 
ATOM   5033 C CA  . ILE B 1 113 ? -12.374 53.263 12.358  1.00 20.40 ? 113 ILE B CA  1 
ATOM   5034 C C   . ILE B 1 113 ? -12.853 54.650 11.951  1.00 27.54 ? 113 ILE B C   1 
ATOM   5035 O O   . ILE B 1 113 ? -13.531 54.813 10.929  1.00 27.58 ? 113 ILE B O   1 
ATOM   5036 C CB  . ILE B 1 113 ? -13.302 52.614 13.395  1.00 22.30 ? 113 ILE B CB  1 
ATOM   5037 C CG1 . ILE B 1 113 ? -12.970 51.128 13.516  1.00 22.56 ? 113 ILE B CG1 1 
ATOM   5038 C CG2 . ILE B 1 113 ? -14.767 52.804 13.002  1.00 26.06 ? 113 ILE B CG2 1 
ATOM   5039 C CD1 . ILE B 1 113 ? -13.875 50.369 14.473  1.00 29.57 ? 113 ILE B CD1 1 
ATOM   5040 N N   . ARG B 1 114 ? -12.493 55.675 12.728  1.00 23.14 ? 114 ARG B N   1 
ATOM   5041 C CA  . ARG B 1 114 ? -12.857 57.038 12.361  1.00 27.47 ? 114 ARG B CA  1 
ATOM   5042 C C   . ARG B 1 114 ? -12.195 57.440 11.054  1.00 30.58 ? 114 ARG B C   1 
ATOM   5043 O O   . ARG B 1 114 ? -12.810 58.110 10.215  1.00 31.23 ? 114 ARG B O   1 
ATOM   5044 C CB  . ARG B 1 114 ? -12.467 58.010 13.475  1.00 34.06 ? 114 ARG B CB  1 
ATOM   5045 C CG  . ARG B 1 114 ? -13.017 57.642 14.848  1.00 45.50 ? 114 ARG B CG  1 
ATOM   5046 C CD  . ARG B 1 114 ? -12.825 58.778 15.850  1.00 55.91 ? 114 ARG B CD  1 
ATOM   5047 N NE  . ARG B 1 114 ? -11.562 58.677 16.579  1.00 61.16 ? 114 ARG B NE  1 
ATOM   5048 C CZ  . ARG B 1 114 ? -11.425 58.076 17.758  1.00 64.42 ? 114 ARG B CZ  1 
ATOM   5049 N NH1 . ARG B 1 114 ? -12.474 57.517 18.346  1.00 61.41 ? 114 ARG B NH1 1 
ATOM   5050 N NH2 . ARG B 1 114 ? -10.240 58.034 18.350  1.00 65.48 ? 114 ARG B NH2 1 
ATOM   5051 N N   . GLU B 1 115 ? -10.929 57.058 10.876  1.00 29.26 ? 115 GLU B N   1 
ATOM   5052 C CA  . GLU B 1 115 ? -10.241 57.331 9.620   1.00 30.22 ? 115 GLU B CA  1 
ATOM   5053 C C   . GLU B 1 115 ? -10.948 56.662 8.454   1.00 27.60 ? 115 GLU B C   1 
ATOM   5054 O O   . GLU B 1 115 ? -11.215 57.295 7.426   1.00 34.21 ? 115 GLU B O   1 
ATOM   5055 C CB  . GLU B 1 115 ? -8.792  56.852 9.703   1.00 29.00 ? 115 GLU B CB  1 
ATOM   5056 C CG  . GLU B 1 115 ? -7.964  57.563 10.741  1.00 34.77 ? 115 GLU B CG  1 
ATOM   5057 C CD  . GLU B 1 115 ? -6.535  57.063 10.775  1.00 41.88 ? 115 GLU B CD  1 
ATOM   5058 O OE1 . GLU B 1 115 ? -6.181  56.217 9.922   1.00 33.69 ? 115 GLU B OE1 1 
ATOM   5059 O OE2 . GLU B 1 115 ? -5.771  57.520 11.652  1.00 47.42 ? 115 GLU B OE2 1 
ATOM   5060 N N   . LEU B 1 116 ? -11.264 55.375 8.600   1.00 24.40 ? 116 LEU B N   1 
ATOM   5061 C CA  . LEU B 1 116 ? -11.830 54.616 7.489   1.00 29.66 ? 116 LEU B CA  1 
ATOM   5062 C C   . LEU B 1 116 ? -13.193 55.156 7.071   1.00 29.87 ? 116 LEU B C   1 
ATOM   5063 O O   . LEU B 1 116 ? -13.511 55.193 5.877   1.00 30.70 ? 116 LEU B O   1 
ATOM   5064 C CB  . LEU B 1 116 ? -11.930 53.137 7.868   1.00 25.06 ? 116 LEU B CB  1 
ATOM   5065 C CG  . LEU B 1 116 ? -10.601 52.419 8.114   1.00 28.48 ? 116 LEU B CG  1 
ATOM   5066 C CD1 . LEU B 1 116 ? -10.849 51.023 8.676   1.00 28.87 ? 116 LEU B CD1 1 
ATOM   5067 C CD2 . LEU B 1 116 ? -9.772  52.363 6.849   1.00 31.92 ? 116 LEU B CD2 1 
ATOM   5068 N N   . MET B 1 117 ? -14.005 55.597 8.032   1.00 26.94 ? 117 MET B N   1 
ATOM   5069 C CA  . MET B 1 117 ? -15.359 56.045 7.722   1.00 27.60 ? 117 MET B CA  1 
ATOM   5070 C C   . MET B 1 117 ? -15.395 57.446 7.126   1.00 36.79 ? 117 MET B C   1 
ATOM   5071 O O   . MET B 1 117 ? -16.436 57.847 6.594   1.00 38.70 ? 117 MET B O   1 
ATOM   5072 C CB  . MET B 1 117 ? -16.233 55.980 8.979   1.00 25.63 ? 117 MET B CB  1 
ATOM   5073 C CG  . MET B 1 117 ? -16.415 54.558 9.523   1.00 31.35 ? 117 MET B CG  1 
ATOM   5074 S SD  . MET B 1 117 ? -17.088 53.412 8.288   1.00 36.58 ? 117 MET B SD  1 
ATOM   5075 C CE  . MET B 1 117 ? -18.787 53.930 8.255   1.00 39.86 ? 117 MET B CE  1 
ATOM   5076 N N   . ASN B 1 118 ? -14.291 58.187 7.191   1.00 40.30 ? 118 ASN B N   1 
ATOM   5077 C CA  . ASN B 1 118 ? -14.169 59.485 6.544   1.00 47.79 ? 118 ASN B CA  1 
ATOM   5078 C C   . ASN B 1 118 ? -13.522 59.390 5.170   1.00 47.16 ? 118 ASN B C   1 
ATOM   5079 O O   . ASN B 1 118 ? -13.257 60.423 4.547   1.00 50.74 ? 118 ASN B O   1 
ATOM   5080 C CB  . ASN B 1 118 ? -13.371 60.446 7.427   1.00 55.72 ? 118 ASN B CB  1 
ATOM   5081 C CG  . ASN B 1 118 ? -14.182 60.977 8.588   1.00 64.32 ? 118 ASN B CG  1 
ATOM   5082 O OD1 . ASN B 1 118 ? -15.411 61.001 8.539   1.00 69.37 ? 118 ASN B OD1 1 
ATOM   5083 N ND2 . ASN B 1 118 ? -13.498 61.411 9.640   1.00 67.63 ? 118 ASN B ND2 1 
ATOM   5084 N N   . LYS B 1 119 ? -13.255 58.181 4.690   1.00 40.08 ? 119 LYS B N   1 
ATOM   5085 C CA  . LYS B 1 119 ? -12.708 57.992 3.357   1.00 43.71 ? 119 LYS B CA  1 
ATOM   5086 C C   . LYS B 1 119 ? -13.836 57.768 2.360   1.00 45.62 ? 119 LYS B C   1 
ATOM   5087 O O   . LYS B 1 119 ? -14.889 57.220 2.696   1.00 46.46 ? 119 LYS B O   1 
ATOM   5088 C CB  . LYS B 1 119 ? -11.740 56.807 3.333   1.00 39.96 ? 119 LYS B CB  1 
ATOM   5089 C CG  . LYS B 1 119 ? -10.402 57.094 3.994   1.00 44.87 ? 119 LYS B CG  1 
ATOM   5090 C CD  . LYS B 1 119 ? -9.492  55.880 3.941   1.00 48.63 ? 119 LYS B CD  1 
ATOM   5091 C CE  . LYS B 1 119 ? -8.288  56.052 4.853   1.00 53.32 ? 119 LYS B CE  1 
ATOM   5092 N NZ  . LYS B 1 119 ? -7.197  56.815 4.190   1.00 52.26 ? 119 LYS B NZ  1 
ATOM   5093 N N   . GLU B 1 120 ? -13.607 58.207 1.122   1.00 49.57 ? 120 GLU B N   1 
ATOM   5094 C CA  . GLU B 1 120 ? -14.618 58.040 0.084   1.00 50.93 ? 120 GLU B CA  1 
ATOM   5095 C C   . GLU B 1 120 ? -14.612 56.624 -0.482  1.00 51.59 ? 120 GLU B C   1 
ATOM   5096 O O   . GLU B 1 120 ? -15.674 56.073 -0.794  1.00 53.86 ? 120 GLU B O   1 
ATOM   5097 C CB  . GLU B 1 120 ? -14.399 59.066 -1.028  1.00 52.34 ? 120 GLU B CB  1 
ATOM   5098 N N   . LYS B 1 121 ? -13.433 56.020 -0.617  1.00 41.46 ? 121 LYS B N   1 
ATOM   5099 C CA  . LYS B 1 121 ? -13.301 54.660 -1.118  1.00 44.80 ? 121 LYS B CA  1 
ATOM   5100 C C   . LYS B 1 121 ? -12.272 53.922 -0.275  1.00 42.87 ? 121 LYS B C   1 
ATOM   5101 O O   . LYS B 1 121 ? -11.293 54.515 0.186   1.00 44.25 ? 121 LYS B O   1 
ATOM   5102 C CB  . LYS B 1 121 ? -12.886 54.636 -2.596  1.00 42.36 ? 121 LYS B CB  1 
ATOM   5103 N N   . LEU B 1 122 ? -12.501 52.625 -0.072  1.00 38.23 ? 122 LEU B N   1 
ATOM   5104 C CA  . LEU B 1 122 ? -11.612 51.780 0.721   1.00 31.05 ? 122 LEU B CA  1 
ATOM   5105 C C   . LEU B 1 122 ? -10.886 50.792 -0.181  1.00 35.67 ? 122 LEU B C   1 
ATOM   5106 O O   . LEU B 1 122 ? -11.526 50.072 -0.955  1.00 37.82 ? 122 LEU B O   1 
ATOM   5107 C CB  . LEU B 1 122 ? -12.377 50.997 1.791   1.00 30.90 ? 122 LEU B CB  1 
ATOM   5108 C CG  . LEU B 1 122 ? -13.114 51.691 2.933   1.00 41.39 ? 122 LEU B CG  1 
ATOM   5109 C CD1 . LEU B 1 122 ? -12.386 52.940 3.408   1.00 39.55 ? 122 LEU B CD1 1 
ATOM   5110 C CD2 . LEU B 1 122 ? -14.531 52.005 2.493   1.00 47.76 ? 122 LEU B CD2 1 
ATOM   5111 N N   . ASN B 1 123 ? -9.558  50.735 -0.054  1.00 29.75 ? 123 ASN B N   1 
ATOM   5112 C CA  . ASN B 1 123 ? -8.761  49.742 -0.759  1.00 28.48 ? 123 ASN B CA  1 
ATOM   5113 C C   . ASN B 1 123 ? -8.729  48.443 0.047   1.00 29.42 ? 123 ASN B C   1 
ATOM   5114 O O   . ASN B 1 123 ? -9.370  48.322 1.088   1.00 28.69 ? 123 ASN B O   1 
ATOM   5115 C CB  . ASN B 1 123 ? -7.351  50.267 -1.027  1.00 31.48 ? 123 ASN B CB  1 
ATOM   5116 C CG  . ASN B 1 123 ? -6.587  50.619 0.254   1.00 38.75 ? 123 ASN B CG  1 
ATOM   5117 O OD1 . ASN B 1 123 ? -6.794  50.026 1.324   1.00 34.33 ? 123 ASN B OD1 1 
ATOM   5118 N ND2 . ASN B 1 123 ? -5.689  51.591 0.140   1.00 43.36 ? 123 ASN B ND2 1 
ATOM   5119 N N   . ARG B 1 124 ? -7.954  47.461 -0.425  1.00 29.93 ? 124 ARG B N   1 
ATOM   5120 C CA  . ARG B 1 124 ? -7.966  46.148 0.220   1.00 25.49 ? 124 ARG B CA  1 
ATOM   5121 C C   . ARG B 1 124 ? -7.478  46.226 1.660   1.00 28.64 ? 124 ARG B C   1 
ATOM   5122 O O   . ARG B 1 124 ? -8.079  45.637 2.567   1.00 25.68 ? 124 ARG B O   1 
ATOM   5123 C CB  . ARG B 1 124 ? -7.108  45.155 -0.560  1.00 29.75 ? 124 ARG B CB  1 
ATOM   5124 C CG  . ARG B 1 124 ? -6.904  43.859 0.224   1.00 24.99 ? 124 ARG B CG  1 
ATOM   5125 C CD  . ARG B 1 124 ? -6.112  42.821 -0.553  1.00 27.83 ? 124 ARG B CD  1 
ATOM   5126 N NE  . ARG B 1 124 ? -6.024  41.576 0.201   1.00 28.23 ? 124 ARG B NE  1 
ATOM   5127 C CZ  . ARG B 1 124 ? -5.141  41.355 1.170   1.00 34.88 ? 124 ARG B CZ  1 
ATOM   5128 N NH1 . ARG B 1 124 ? -4.257  42.292 1.488   1.00 37.73 ? 124 ARG B NH1 1 
ATOM   5129 N NH2 . ARG B 1 124 ? -5.136  40.197 1.818   1.00 34.69 ? 124 ARG B NH2 1 
ATOM   5130 N N   . GLU B 1 125 ? -6.368  46.924 1.887   1.00 30.87 ? 125 GLU B N   1 
ATOM   5131 C CA  . GLU B 1 125 ? -5.816  47.007 3.236   1.00 28.14 ? 125 GLU B CA  1 
ATOM   5132 C C   . GLU B 1 125 ? -6.749  47.783 4.158   1.00 26.63 ? 125 GLU B C   1 
ATOM   5133 O O   . GLU B 1 125 ? -6.878  47.463 5.347   1.00 25.15 ? 125 GLU B O   1 
ATOM   5134 C CB  . GLU B 1 125 ? -4.430  47.654 3.188   1.00 34.62 ? 125 GLU B CB  1 
ATOM   5135 C CG  . GLU B 1 125 ? -3.354  46.828 2.468   1.00 45.24 ? 125 GLU B CG  1 
ATOM   5136 C CD  . GLU B 1 125 ? -3.692  46.516 1.011   1.00 53.24 ? 125 GLU B CD  1 
ATOM   5137 O OE1 . GLU B 1 125 ? -3.670  45.322 0.638   1.00 54.21 ? 125 GLU B OE1 1 
ATOM   5138 O OE2 . GLU B 1 125 ? -3.994  47.458 0.243   1.00 50.24 ? 125 GLU B OE2 1 
ATOM   5139 N N   . GLU B 1 126 ? -7.425  48.798 3.624   1.00 26.49 ? 126 GLU B N   1 
ATOM   5140 C CA  . GLU B 1 126 ? -8.378  49.539 4.439   1.00 25.87 ? 126 GLU B CA  1 
ATOM   5141 C C   . GLU B 1 126 ? -9.580  48.675 4.806   1.00 24.06 ? 126 GLU B C   1 
ATOM   5142 O O   . GLU B 1 126 ? -10.061 48.729 5.944   1.00 21.08 ? 126 GLU B O   1 
ATOM   5143 C CB  . GLU B 1 126 ? -8.806  50.815 3.709   1.00 29.09 ? 126 GLU B CB  1 
ATOM   5144 C CG  . GLU B 1 126 ? -7.784  51.939 3.856   1.00 29.58 ? 126 GLU B CG  1 
ATOM   5145 C CD  . GLU B 1 126 ? -7.781  52.930 2.700   1.00 33.41 ? 126 GLU B CD  1 
ATOM   5146 O OE1 . GLU B 1 126 ? -8.584  52.777 1.752   1.00 34.71 ? 126 GLU B OE1 1 
ATOM   5147 O OE2 . GLU B 1 126 ? -6.955  53.866 2.744   1.00 36.84 ? 126 GLU B OE2 1 
ATOM   5148 N N   . LEU B 1 127 ? -10.074 47.864 3.866   1.00 23.59 ? 127 LEU B N   1 
ATOM   5149 C CA  . LEU B 1 127 ? -11.196 46.990 4.193   1.00 21.15 ? 127 LEU B CA  1 
ATOM   5150 C C   . LEU B 1 127 ? -10.787 45.911 5.189   1.00 22.41 ? 127 LEU B C   1 
ATOM   5151 O O   . LEU B 1 127 ? -11.593 45.514 6.038   1.00 21.84 ? 127 LEU B O   1 
ATOM   5152 C CB  . LEU B 1 127 ? -11.765 46.365 2.919   1.00 23.76 ? 127 LEU B CB  1 
ATOM   5153 C CG  . LEU B 1 127 ? -12.569 47.343 2.059   1.00 25.40 ? 127 LEU B CG  1 
ATOM   5154 C CD1 . LEU B 1 127 ? -12.785 46.772 0.667   1.00 28.06 ? 127 LEU B CD1 1 
ATOM   5155 C CD2 . LEU B 1 127 ? -13.904 47.679 2.734   1.00 23.59 ? 127 LEU B CD2 1 
ATOM   5156 N N   . LEU B 1 128 ? -9.540  45.436 5.110   1.00 20.81 ? 128 LEU B N   1 
ATOM   5157 C CA  . LEU B 1 128 ? -9.053  44.466 6.087   1.00 20.20 ? 128 LEU B CA  1 
ATOM   5158 C C   . LEU B 1 128 ? -9.095  45.042 7.493   1.00 19.55 ? 128 LEU B C   1 
ATOM   5159 O O   . LEU B 1 128 ? -9.465  44.348 8.451   1.00 20.25 ? 128 LEU B O   1 
ATOM   5160 C CB  . LEU B 1 128 ? -7.626  44.044 5.737   1.00 24.91 ? 128 LEU B CB  1 
ATOM   5161 C CG  . LEU B 1 128 ? -7.456  42.695 5.041   1.00 30.31 ? 128 LEU B CG  1 
ATOM   5162 C CD1 . LEU B 1 128 ? -6.005  42.502 4.623   1.00 24.58 ? 128 LEU B CD1 1 
ATOM   5163 C CD2 . LEU B 1 128 ? -7.913  41.560 5.940   1.00 32.02 ? 128 LEU B CD2 1 
ATOM   5164 N N   . ASP B 1 129 ? -8.697  46.307 7.640   1.00 23.13 ? 129 ASP B N   1 
ATOM   5165 C CA  . ASP B 1 129 ? -8.797  46.970 8.937   1.00 19.72 ? 129 ASP B CA  1 
ATOM   5166 C C   . ASP B 1 129 ? -10.252 47.107 9.364   1.00 24.82 ? 129 ASP B C   1 
ATOM   5167 O O   . ASP B 1 129 ? -10.595 46.858 10.528  1.00 18.44 ? 129 ASP B O   1 
ATOM   5168 C CB  . ASP B 1 129 ? -8.114  48.341 8.877   1.00 24.29 ? 129 ASP B CB  1 
ATOM   5169 C CG  . ASP B 1 129 ? -6.602  48.238 8.911   1.00 27.56 ? 129 ASP B CG  1 
ATOM   5170 O OD1 . ASP B 1 129 ? -6.093  47.104 8.826   1.00 28.09 ? 129 ASP B OD1 1 
ATOM   5171 O OD2 . ASP B 1 129 ? -5.916  49.280 9.023   1.00 28.45 ? 129 ASP B OD2 1 
ATOM   5172 N N   . LEU B 1 130 ? -11.129 47.483 8.430   1.00 22.13 ? 130 LEU B N   1 
ATOM   5173 C CA  . LEU B 1 130 ? -12.543 47.605 8.771   1.00 21.29 ? 130 LEU B CA  1 
ATOM   5174 C C   . LEU B 1 130 ? -13.100 46.268 9.241   1.00 19.77 ? 130 LEU B C   1 
ATOM   5175 O O   . LEU B 1 130 ? -13.792 46.196 10.267  1.00 21.19 ? 130 LEU B O   1 
ATOM   5176 C CB  . LEU B 1 130 ? -13.336 48.141 7.572   1.00 20.30 ? 130 LEU B CB  1 
ATOM   5177 C CG  . LEU B 1 130 ? -14.790 48.536 7.872   1.00 22.66 ? 130 LEU B CG  1 
ATOM   5178 C CD1 . LEU B 1 130 ? -14.857 49.672 8.883   1.00 28.82 ? 130 LEU B CD1 1 
ATOM   5179 C CD2 . LEU B 1 130 ? -15.540 48.914 6.601   1.00 23.78 ? 130 LEU B CD2 1 
ATOM   5180 N N   . GLN B 1 131 ? -12.760 45.187 8.534   1.00 21.13 ? 131 GLN B N   1 
ATOM   5181 C CA  . GLN B 1 131 ? -13.215 43.862 8.941   1.00 18.20 ? 131 GLN B CA  1 
ATOM   5182 C C   . GLN B 1 131 ? -12.676 43.492 10.319  1.00 22.34 ? 131 GLN B C   1 
ATOM   5183 O O   . GLN B 1 131 ? -13.424 43.041 11.196  1.00 17.39 ? 131 GLN B O   1 
ATOM   5184 C CB  . GLN B 1 131 ? -12.774 42.821 7.919   1.00 17.94 ? 131 GLN B CB  1 
ATOM   5185 C CG  . GLN B 1 131 ? -13.431 42.898 6.559   1.00 18.63 ? 131 GLN B CG  1 
ATOM   5186 C CD  . GLN B 1 131 ? -12.707 42.015 5.564   1.00 22.36 ? 131 GLN B CD  1 
ATOM   5187 O OE1 . GLN B 1 131 ? -11.474 41.948 5.575   1.00 21.46 ? 131 GLN B OE1 1 
ATOM   5188 N NE2 . GLN B 1 131 ? -13.461 41.301 4.729   1.00 21.08 ? 131 GLN B NE2 1 
ATOM   5189 N N   . THR B 1 132 ? -11.369 43.670 10.524  1.00 19.38 ? 132 THR B N   1 
ATOM   5190 C CA  . THR B 1 132 ? -10.749 43.202 11.759  1.00 16.91 ? 132 THR B CA  1 
ATOM   5191 C C   . THR B 1 132 ? -11.169 44.062 12.944  1.00 18.61 ? 132 THR B C   1 
ATOM   5192 O O   . THR B 1 132 ? -11.393 43.546 14.044  1.00 17.29 ? 132 THR B O   1 
ATOM   5193 C CB  . THR B 1 132 ? -9.229  43.187 11.600  1.00 17.68 ? 132 THR B CB  1 
ATOM   5194 O OG1 . THR B 1 132 ? -8.893  42.474 10.403  1.00 19.86 ? 132 THR B OG1 1 
ATOM   5195 C CG2 . THR B 1 132 ? -8.566  42.524 12.782  1.00 17.70 ? 132 THR B CG2 1 
ATOM   5196 N N   . LEU B 1 133 ? -11.270 45.377 12.748  1.00 21.43 ? 133 LEU B N   1 
ATOM   5197 C CA  . LEU B 1 133 ? -11.667 46.240 13.856  1.00 19.33 ? 133 LEU B CA  1 
ATOM   5198 C C   . LEU B 1 133 ? -13.123 46.024 14.243  1.00 20.65 ? 133 LEU B C   1 
ATOM   5199 O O   . LEU B 1 133 ? -13.483 46.199 15.415  1.00 21.94 ? 133 LEU B O   1 
ATOM   5200 C CB  . LEU B 1 133 ? -11.417 47.703 13.501  1.00 17.49 ? 133 LEU B CB  1 
ATOM   5201 C CG  . LEU B 1 133 ? -9.930  48.034 13.584  1.00 23.50 ? 133 LEU B CG  1 
ATOM   5202 C CD1 . LEU B 1 133 ? -9.615  49.319 12.837  1.00 28.40 ? 133 LEU B CD1 1 
ATOM   5203 C CD2 . LEU B 1 133 ? -9.475  48.108 15.030  1.00 20.72 ? 133 LEU B CD2 1 
ATOM   5204 N N   . ASN B 1 134 ? -13.975 45.647 13.287  1.00 16.24 ? 134 ASN B N   1 
ATOM   5205 C CA  . ASN B 1 134 ? -15.329 45.263 13.658  1.00 17.11 ? 134 ASN B CA  1 
ATOM   5206 C C   . ASN B 1 134 ? -15.299 44.050 14.573  1.00 20.53 ? 134 ASN B C   1 
ATOM   5207 O O   . ASN B 1 134 ? -15.991 44.023 15.596  1.00 18.37 ? 134 ASN B O   1 
ATOM   5208 C CB  . ASN B 1 134 ? -16.173 44.996 12.410  1.00 18.56 ? 134 ASN B CB  1 
ATOM   5209 C CG  . ASN B 1 134 ? -16.990 46.203 11.998  1.00 20.42 ? 134 ASN B CG  1 
ATOM   5210 O OD1 . ASN B 1 134 ? -18.080 46.436 12.519  1.00 19.62 ? 134 ASN B OD1 1 
ATOM   5211 N ND2 . ASN B 1 134 ? -16.460 46.986 11.065  1.00 21.85 ? 134 ASN B ND2 1 
ATOM   5212 N N   . LEU B 1 135 ? -14.439 43.074 14.264  1.00 19.48 ? 135 LEU B N   1 
ATOM   5213 C CA  . LEU B 1 135 ? -14.285 41.914 15.137  1.00 21.47 ? 135 LEU B CA  1 
ATOM   5214 C C   . LEU B 1 135 ? -13.775 42.323 16.509  1.00 21.26 ? 135 LEU B C   1 
ATOM   5215 O O   . LEU B 1 135 ? -14.307 41.888 17.539  1.00 20.04 ? 135 LEU B O   1 
ATOM   5216 C CB  . LEU B 1 135 ? -13.323 40.905 14.514  1.00 23.37 ? 135 LEU B CB  1 
ATOM   5217 C CG  . LEU B 1 135 ? -13.841 40.010 13.393  1.00 23.47 ? 135 LEU B CG  1 
ATOM   5218 C CD1 . LEU B 1 135 ? -12.714 39.098 12.911  1.00 23.04 ? 135 LEU B CD1 1 
ATOM   5219 C CD2 . LEU B 1 135 ? -15.069 39.197 13.829  1.00 19.81 ? 135 LEU B CD2 1 
ATOM   5220 N N   . LEU B 1 136 ? -12.727 43.153 16.539  1.00 19.06 ? 136 LEU B N   1 
ATOM   5221 C CA  . LEU B 1 136 ? -12.065 43.470 17.798  1.00 17.37 ? 136 LEU B CA  1 
ATOM   5222 C C   . LEU B 1 136 ? -12.927 44.353 18.686  1.00 20.37 ? 136 LEU B C   1 
ATOM   5223 O O   . LEU B 1 136 ? -12.784 44.322 19.917  1.00 17.08 ? 136 LEU B O   1 
ATOM   5224 C CB  . LEU B 1 136 ? -10.717 44.139 17.524  1.00 17.08 ? 136 LEU B CB  1 
ATOM   5225 C CG  . LEU B 1 136 ? -9.622  43.246 16.941  1.00 17.42 ? 136 LEU B CG  1 
ATOM   5226 C CD1 . LEU B 1 136 ? -8.393  44.045 16.507  1.00 20.31 ? 136 LEU B CD1 1 
ATOM   5227 C CD2 . LEU B 1 136 ? -9.221  42.167 17.944  1.00 17.25 ? 136 LEU B CD2 1 
ATOM   5228 N N   . ALA B 1 137 ? -13.803 45.163 18.085  1.00 14.95 ? 137 ALA B N   1 
ATOM   5229 C CA  . ALA B 1 137 ? -14.743 45.946 18.872  1.00 18.16 ? 137 ALA B CA  1 
ATOM   5230 C C   . ALA B 1 137 ? -15.587 45.066 19.787  1.00 18.38 ? 137 ALA B C   1 
ATOM   5231 O O   . ALA B 1 137 ? -15.994 45.512 20.867  1.00 18.41 ? 137 ALA B O   1 
ATOM   5232 C CB  . ALA B 1 137 ? -15.649 46.760 17.949  1.00 20.02 ? 137 ALA B CB  1 
ATOM   5233 N N   . TRP B 1 138 ? -15.848 43.820 19.392  1.00 17.97 ? 138 TRP B N   1 
ATOM   5234 C CA  . TRP B 1 138 ? -16.688 42.918 20.173  1.00 16.32 ? 138 TRP B CA  1 
ATOM   5235 C C   . TRP B 1 138 ? -15.878 41.958 21.043  1.00 16.12 ? 138 TRP B C   1 
ATOM   5236 O O   . TRP B 1 138 ? -16.441 41.003 21.587  1.00 18.11 ? 138 TRP B O   1 
ATOM   5237 C CB  . TRP B 1 138 ? -17.645 42.145 19.247  1.00 19.41 ? 138 TRP B CB  1 
ATOM   5238 C CG  . TRP B 1 138 ? -18.628 43.069 18.563  1.00 15.57 ? 138 TRP B CG  1 
ATOM   5239 C CD1 . TRP B 1 138 ? -18.444 43.740 17.381  1.00 21.61 ? 138 TRP B CD1 1 
ATOM   5240 C CD2 . TRP B 1 138 ? -19.924 43.460 19.044  1.00 16.55 ? 138 TRP B CD2 1 
ATOM   5241 N NE1 . TRP B 1 138 ? -19.549 44.510 17.101  1.00 20.39 ? 138 TRP B NE1 1 
ATOM   5242 C CE2 . TRP B 1 138 ? -20.465 44.357 18.108  1.00 15.73 ? 138 TRP B CE2 1 
ATOM   5243 C CE3 . TRP B 1 138 ? -20.675 43.133 20.175  1.00 17.61 ? 138 TRP B CE3 1 
ATOM   5244 C CZ2 . TRP B 1 138 ? -21.731 44.932 18.266  1.00 19.62 ? 138 TRP B CZ2 1 
ATOM   5245 C CZ3 . TRP B 1 138 ? -21.929 43.700 20.331  1.00 16.81 ? 138 TRP B CZ3 1 
ATOM   5246 C CH2 . TRP B 1 138 ? -22.440 44.596 19.385  1.00 16.88 ? 138 TRP B CH2 1 
ATOM   5247 N N   . CYS B 1 139 ? -14.578 42.205 21.210  1.00 17.23 ? 139 CYS B N   1 
ATOM   5248 C CA  . CYS B 1 139 ? -13.759 41.350 22.056  1.00 14.98 ? 139 CYS B CA  1 
ATOM   5249 C C   . CYS B 1 139 ? -14.290 41.325 23.486  1.00 15.94 ? 139 CYS B C   1 
ATOM   5250 O O   . CYS B 1 139 ? -14.531 42.374 24.092  1.00 21.07 ? 139 CYS B O   1 
ATOM   5251 C CB  . CYS B 1 139 ? -12.312 41.846 22.049  1.00 16.12 ? 139 CYS B CB  1 
ATOM   5252 S SG  . CYS B 1 139 ? -11.161 40.758 22.898  1.00 22.01 ? 139 CYS B SG  1 
ATOM   5253 N N   . GLY B 1 140 ? -14.442 40.121 24.029  1.00 15.44 ? 140 GLY B N   1 
ATOM   5254 C CA  . GLY B 1 140 ? -14.856 39.968 25.409  1.00 16.59 ? 140 GLY B CA  1 
ATOM   5255 C C   . GLY B 1 140 ? -13.730 40.150 26.409  1.00 16.39 ? 140 GLY B C   1 
ATOM   5256 O O   . GLY B 1 140 ? -12.551 40.237 26.075  1.00 17.76 ? 140 GLY B O   1 
ATOM   5257 N N   . ARG B 1 141 ? -14.118 40.195 27.686  1.00 17.47 ? 141 ARG B N   1 
ATOM   5258 C CA  . ARG B 1 141 ? -13.160 40.454 28.751  1.00 17.51 ? 141 ARG B CA  1 
ATOM   5259 C C   . ARG B 1 141 ? -12.019 39.440 28.737  1.00 18.03 ? 141 ARG B C   1 
ATOM   5260 O O   . ARG B 1 141 ? -10.853 39.812 28.889  1.00 18.24 ? 141 ARG B O   1 
ATOM   5261 C CB  . ARG B 1 141 ? -13.889 40.443 30.095  1.00 15.84 ? 141 ARG B CB  1 
ATOM   5262 C CG  . ARG B 1 141 ? -13.003 40.531 31.311  1.00 17.02 ? 141 ARG B CG  1 
ATOM   5263 C CD  . ARG B 1 141 ? -13.881 40.689 32.532  1.00 20.07 ? 141 ARG B CD  1 
ATOM   5264 N NE  . ARG B 1 141 ? -13.122 40.602 33.766  1.00 20.94 ? 141 ARG B NE  1 
ATOM   5265 C CZ  . ARG B 1 141 ? -12.914 39.480 34.444  1.00 18.72 ? 141 ARG B CZ  1 
ATOM   5266 N NH1 . ARG B 1 141 ? -13.412 38.323 34.023  1.00 19.79 ? 141 ARG B NH1 1 
ATOM   5267 N NH2 . ARG B 1 141 ? -12.204 39.527 35.558  1.00 23.61 ? 141 ARG B NH2 1 
ATOM   5268 N N   . THR B 1 142 ? -12.333 38.158 28.541  1.00 16.15 ? 142 THR B N   1 
ATOM   5269 C CA  . THR B 1 142 ? -11.304 37.119 28.643  1.00 22.21 ? 142 THR B CA  1 
ATOM   5270 C C   . THR B 1 142 ? -10.234 37.275 27.569  1.00 23.03 ? 142 THR B C   1 
ATOM   5271 O O   . THR B 1 142 ? -9.035  37.120 27.842  1.00 27.31 ? 142 THR B O   1 
ATOM   5272 C CB  . THR B 1 142 ? -11.947 35.733 28.542  1.00 25.46 ? 142 THR B CB  1 
ATOM   5273 O OG1 . THR B 1 142 ? -12.796 35.518 29.672  1.00 24.64 ? 142 THR B OG1 1 
ATOM   5274 C CG2 . THR B 1 142 ? -10.874 34.640 28.511  1.00 27.23 ? 142 THR B CG2 1 
ATOM   5275 N N   . LEU B 1 143 ? -10.642 37.572 26.343  1.00 16.79 ? 143 LEU B N   1 
ATOM   5276 C CA  . LEU B 1 143 ? -9.707  37.582 25.224  1.00 22.61 ? 143 LEU B CA  1 
ATOM   5277 C C   . LEU B 1 143 ? -8.902  38.872 25.124  1.00 24.46 ? 143 LEU B C   1 
ATOM   5278 O O   . LEU B 1 143 ? -8.004  38.962 24.277  1.00 25.29 ? 143 LEU B O   1 
ATOM   5279 C CB  . LEU B 1 143 ? -10.461 37.326 23.919  1.00 22.25 ? 143 LEU B CB  1 
ATOM   5280 C CG  . LEU B 1 143 ? -10.736 35.847 23.639  1.00 20.75 ? 143 LEU B CG  1 
ATOM   5281 C CD1 . LEU B 1 143 ? -11.347 35.689 22.254  1.00 16.64 ? 143 LEU B CD1 1 
ATOM   5282 C CD2 . LEU B 1 143 ? -9.465  35.009 23.771  1.00 26.52 ? 143 LEU B CD2 1 
ATOM   5283 N N   . ARG B 1 144 ? -9.185  39.870 25.965  1.00 23.50 ? 144 ARG B N   1 
ATOM   5284 C CA  . ARG B 1 144 ? -8.384  41.086 25.946  1.00 26.65 ? 144 ARG B CA  1 
ATOM   5285 C C   . ARG B 1 144 ? -6.910  40.820 26.216  1.00 31.68 ? 144 ARG B C   1 
ATOM   5286 O O   . ARG B 1 144 ? -6.070  41.626 25.803  1.00 35.64 ? 144 ARG B O   1 
ATOM   5287 C CB  . ARG B 1 144 ? -8.915  42.092 26.961  1.00 33.73 ? 144 ARG B CB  1 
ATOM   5288 C CG  . ARG B 1 144 ? -10.256 42.664 26.583  1.00 37.17 ? 144 ARG B CG  1 
ATOM   5289 C CD  . ARG B 1 144 ? -10.774 43.524 27.702  1.00 42.65 ? 144 ARG B CD  1 
ATOM   5290 N NE  . ARG B 1 144 ? -10.535 42.895 28.997  1.00 48.17 ? 144 ARG B NE  1 
ATOM   5291 C CZ  . ARG B 1 144 ? -10.045 43.530 30.055  1.00 55.66 ? 144 ARG B CZ  1 
ATOM   5292 N NH1 . ARG B 1 144 ? -9.743  44.819 29.973  1.00 57.09 ? 144 ARG B NH1 1 
ATOM   5293 N NH2 . ARG B 1 144 ? -9.860  42.879 31.196  1.00 59.22 ? 144 ARG B NH2 1 
ATOM   5294 N N   . LYS B 1 145 ? -6.571  39.720 26.898  1.00 28.39 ? 145 LYS B N   1 
ATOM   5295 C CA  . LYS B 1 145 ? -5.161  39.454 27.165  1.00 29.14 ? 145 LYS B CA  1 
ATOM   5296 C C   . LYS B 1 145 ? -4.502  38.766 25.973  1.00 30.22 ? 145 LYS B C   1 
ATOM   5297 O O   . LYS B 1 145 ? -3.447  39.209 25.505  1.00 27.57 ? 145 LYS B O   1 
ATOM   5298 C CB  . LYS B 1 145 ? -5.003  38.643 28.465  1.00 42.20 ? 145 LYS B CB  1 
ATOM   5299 C CG  . LYS B 1 145 ? -4.819  37.133 28.324  1.00 51.59 ? 145 LYS B CG  1 
ATOM   5300 C CD  . LYS B 1 145 ? -4.847  36.410 29.664  1.00 57.81 ? 145 LYS B CD  1 
ATOM   5301 C CE  . LYS B 1 145 ? -5.088  34.911 29.477  1.00 61.79 ? 145 LYS B CE  1 
ATOM   5302 N NZ  . LYS B 1 145 ? -6.393  34.612 28.807  1.00 60.88 ? 145 LYS B NZ  1 
ATOM   5303 N N   . ASP B 1 146 ? -5.134  37.719 25.428  1.00 27.88 ? 146 ASP B N   1 
ATOM   5304 C CA  . ASP B 1 146 ? -4.549  37.034 24.282  1.00 28.77 ? 146 ASP B CA  1 
ATOM   5305 C C   . ASP B 1 146 ? -4.477  37.948 23.072  1.00 32.21 ? 146 ASP B C   1 
ATOM   5306 O O   . ASP B 1 146 ? -3.552  37.835 22.263  1.00 31.89 ? 146 ASP B O   1 
ATOM   5307 C CB  . ASP B 1 146 ? -5.357  35.784 23.933  1.00 33.22 ? 146 ASP B CB  1 
ATOM   5308 C CG  . ASP B 1 146 ? -4.974  34.586 24.772  1.00 53.84 ? 146 ASP B CG  1 
ATOM   5309 O OD1 . ASP B 1 146 ? -3.875  34.599 25.368  1.00 60.20 ? 146 ASP B OD1 1 
ATOM   5310 O OD2 . ASP B 1 146 ? -5.778  33.631 24.837  1.00 59.22 ? 146 ASP B OD2 1 
ATOM   5311 N N   . LEU B 1 147 ? -5.435  38.857 22.933  1.00 23.95 ? 147 LEU B N   1 
ATOM   5312 C CA  . LEU B 1 147 ? -5.533  39.707 21.758  1.00 22.70 ? 147 LEU B CA  1 
ATOM   5313 C C   . LEU B 1 147 ? -4.945  41.096 21.980  1.00 21.05 ? 147 LEU B C   1 
ATOM   5314 O O   . LEU B 1 147 ? -5.089  41.955 21.106  1.00 24.19 ? 147 LEU B O   1 
ATOM   5315 C CB  . LEU B 1 147 ? -6.994  39.814 21.311  1.00 20.44 ? 147 LEU B CB  1 
ATOM   5316 C CG  . LEU B 1 147 ? -7.639  38.526 20.796  1.00 22.40 ? 147 LEU B CG  1 
ATOM   5317 C CD1 . LEU B 1 147 ? -9.067  38.773 20.333  1.00 20.86 ? 147 LEU B CD1 1 
ATOM   5318 C CD2 . LEU B 1 147 ? -6.807  37.945 19.661  1.00 26.41 ? 147 LEU B CD2 1 
ATOM   5319 N N   . LYS B 1 148 ? -4.249  41.323 23.103  1.00 25.93 ? 148 LYS B N   1 
ATOM   5320 C CA  . LYS B 1 148 ? -3.763  42.665 23.419  1.00 30.68 ? 148 LYS B CA  1 
ATOM   5321 C C   . LYS B 1 148 ? -2.854  43.217 22.325  1.00 29.71 ? 148 LYS B C   1 
ATOM   5322 O O   . LYS B 1 148 ? -2.954  44.397 21.964  1.00 28.30 ? 148 LYS B O   1 
ATOM   5323 C CB  . LYS B 1 148 ? -3.034  42.675 24.761  1.00 30.28 ? 148 LYS B CB  1 
ATOM   5324 C CG  . LYS B 1 148 ? -2.445  44.040 25.105  1.00 28.42 ? 148 LYS B CG  1 
ATOM   5325 C CD  . LYS B 1 148 ? -2.107  44.144 26.592  1.00 34.81 ? 148 LYS B CD  1 
ATOM   5326 C CE  . LYS B 1 148 ? -1.277  45.384 26.896  1.00 40.15 ? 148 LYS B CE  1 
ATOM   5327 N NZ  . LYS B 1 148 ? -1.873  46.628 26.333  1.00 42.16 ? 148 LYS B NZ  1 
ATOM   5328 N N   . ASP B 1 149 ? -1.970  42.384 21.771  1.00 25.82 ? 149 ASP B N   1 
ATOM   5329 C CA  . ASP B 1 149 ? -1.069  42.893 20.744  1.00 28.63 ? 149 ASP B CA  1 
ATOM   5330 C C   . ASP B 1 149 ? -1.852  43.398 19.538  1.00 25.88 ? 149 ASP B C   1 
ATOM   5331 O O   . ASP B 1 149 ? -1.511  44.437 18.960  1.00 25.96 ? 149 ASP B O   1 
ATOM   5332 C CB  . ASP B 1 149 ? -0.064  41.817 20.335  1.00 44.39 ? 149 ASP B CB  1 
ATOM   5333 C CG  . ASP B 1 149 ? -0.711  40.666 19.611  1.00 58.02 ? 149 ASP B CG  1 
ATOM   5334 O OD1 . ASP B 1 149 ? -1.662  40.070 20.162  1.00 61.44 ? 149 ASP B OD1 1 
ATOM   5335 O OD2 . ASP B 1 149 ? -0.275  40.370 18.480  1.00 63.02 ? 149 ASP B OD2 1 
ATOM   5336 N N   . LEU B 1 150 ? -2.932  42.702 19.171  1.00 22.84 ? 150 LEU B N   1 
ATOM   5337 C CA  . LEU B 1 150 ? -3.739  43.149 18.038  1.00 25.79 ? 150 LEU B CA  1 
ATOM   5338 C C   . LEU B 1 150 ? -4.566  44.378 18.403  1.00 26.50 ? 150 LEU B C   1 
ATOM   5339 O O   . LEU B 1 150 ? -4.758  45.272 17.573  1.00 27.91 ? 150 LEU B O   1 
ATOM   5340 C CB  . LEU B 1 150 ? -4.630  42.007 17.541  1.00 23.45 ? 150 LEU B CB  1 
ATOM   5341 C CG  . LEU B 1 150 ? -3.901  40.824 16.887  1.00 27.60 ? 150 LEU B CG  1 
ATOM   5342 C CD1 . LEU B 1 150 ? -4.889  39.748 16.431  1.00 24.87 ? 150 LEU B CD1 1 
ATOM   5343 C CD2 . LEU B 1 150 ? -3.025  41.280 15.717  1.00 22.46 ? 150 LEU B CD2 1 
ATOM   5344 N N   . LEU B 1 151 ? -5.045  44.460 19.647  1.00 23.59 ? 151 LEU B N   1 
ATOM   5345 C CA  . LEU B 1 151 ? -5.752  45.663 20.072  1.00 24.64 ? 151 LEU B CA  1 
ATOM   5346 C C   . LEU B 1 151 ? -4.807  46.854 20.151  1.00 33.75 ? 151 LEU B C   1 
ATOM   5347 O O   . LEU B 1 151 ? -5.181  47.977 19.792  1.00 39.27 ? 151 LEU B O   1 
ATOM   5348 C CB  . LEU B 1 151 ? -6.428  45.424 21.423  1.00 25.85 ? 151 LEU B CB  1 
ATOM   5349 C CG  . LEU B 1 151 ? -7.540  44.381 21.389  1.00 24.08 ? 151 LEU B CG  1 
ATOM   5350 C CD1 . LEU B 1 151 ? -7.910  43.949 22.805  1.00 27.26 ? 151 LEU B CD1 1 
ATOM   5351 C CD2 . LEU B 1 151 ? -8.766  44.939 20.657  1.00 27.25 ? 151 LEU B CD2 1 
ATOM   5352 N N   . ASN B 1 152 ? -3.576  46.624 20.618  1.00 27.22 ? 152 ASN B N   1 
ATOM   5353 C CA  . ASN B 1 152 ? -2.575  47.684 20.676  1.00 26.84 ? 152 ASN B CA  1 
ATOM   5354 C C   . ASN B 1 152 ? -2.176  48.161 19.283  1.00 34.61 ? 152 ASN B C   1 
ATOM   5355 O O   . ASN B 1 152 ? -1.837  49.337 19.101  1.00 36.79 ? 152 ASN B O   1 
ATOM   5356 C CB  . ASN B 1 152 ? -1.332  47.191 21.418  1.00 36.25 ? 152 ASN B CB  1 
ATOM   5357 C CG  . ASN B 1 152 ? -1.386  47.453 22.912  1.00 42.83 ? 152 ASN B CG  1 
ATOM   5358 O OD1 . ASN B 1 152 ? -2.456  47.607 23.494  1.00 39.48 ? 152 ASN B OD1 1 
ATOM   5359 N ND2 . ASN B 1 152 ? -0.215  47.503 23.540  1.00 46.28 ? 152 ASN B ND2 1 
ATOM   5360 N N   . LYS B 1 153 ? -2.177  47.257 18.301  1.00 33.64 ? 153 LYS B N   1 
ATOM   5361 C CA  . LYS B 1 153 ? -1.744  47.607 16.951  1.00 31.89 ? 153 LYS B CA  1 
ATOM   5362 C C   . LYS B 1 153 ? -2.647  48.678 16.347  1.00 30.32 ? 153 LYS B C   1 
ATOM   5363 O O   . LYS B 1 153 ? -2.168  49.695 15.833  1.00 36.49 ? 153 LYS B O   1 
ATOM   5364 C CB  . LYS B 1 153 ? -1.728  46.348 16.085  1.00 30.94 ? 153 LYS B CB  1 
ATOM   5365 C CG  . LYS B 1 153 ? -1.245  46.540 14.667  1.00 37.06 ? 153 LYS B CG  1 
ATOM   5366 C CD  . LYS B 1 153 ? -1.477  45.272 13.856  1.00 32.29 ? 153 LYS B CD  1 
ATOM   5367 C CE  . LYS B 1 153 ? -0.464  45.144 12.741  1.00 35.06 ? 153 LYS B CE  1 
ATOM   5368 N NZ  . LYS B 1 153 ? -0.611  43.861 12.023  1.00 37.18 ? 153 LYS B NZ  1 
ATOM   5369 N N   . GLY B 1 154 ? -3.962  48.462 16.398  1.00 29.14 ? 154 GLY B N   1 
ATOM   5370 C CA  . GLY B 1 154 ? -4.936  49.462 16.019  1.00 32.36 ? 154 GLY B CA  1 
ATOM   5371 C C   . GLY B 1 154 ? -5.206  49.611 14.535  1.00 25.07 ? 154 GLY B C   1 
ATOM   5372 O O   . GLY B 1 154 ? -6.226  50.202 14.170  1.00 27.98 ? 154 GLY B O   1 
ATOM   5373 N N   . ARG B 1 155 ? -4.339  49.097 13.667  1.00 29.63 ? 155 ARG B N   1 
ATOM   5374 C CA  . ARG B 1 155 ? -4.448  49.342 12.230  1.00 26.59 ? 155 ARG B CA  1 
ATOM   5375 C C   . ARG B 1 155 ? -3.551  48.350 11.505  1.00 27.32 ? 155 ARG B C   1 
ATOM   5376 O O   . ARG B 1 155 ? -2.735  47.658 12.121  1.00 28.65 ? 155 ARG B O   1 
ATOM   5377 C CB  . ARG B 1 155 ? -4.044  50.775 11.866  1.00 31.19 ? 155 ARG B CB  1 
ATOM   5378 C CG  . ARG B 1 155 ? -2.572  51.067 12.160  1.00 30.72 ? 155 ARG B CG  1 
ATOM   5379 C CD  . ARG B 1 155 ? -2.214  52.517 11.910  1.00 37.99 ? 155 ARG B CD  1 
ATOM   5380 N NE  . ARG B 1 155 ? -3.089  53.422 12.645  1.00 42.48 ? 155 ARG B NE  1 
ATOM   5381 C CZ  . ARG B 1 155 ? -3.874  54.325 12.068  1.00 41.04 ? 155 ARG B CZ  1 
ATOM   5382 N NH1 . ARG B 1 155 ? -4.643  55.111 12.811  1.00 42.11 ? 155 ARG B NH1 1 
ATOM   5383 N NH2 . ARG B 1 155 ? -3.880  54.448 10.746  1.00 36.23 ? 155 ARG B NH2 1 
ATOM   5384 N N   . ASN B 1 156 ? -3.701  48.309 10.179  1.00 24.65 ? 156 ASN B N   1 
ATOM   5385 C CA  . ASN B 1 156 ? -2.820  47.538 9.299   1.00 30.40 ? 156 ASN B CA  1 
ATOM   5386 C C   . ASN B 1 156 ? -2.847  46.046 9.636   1.00 28.28 ? 156 ASN B C   1 
ATOM   5387 O O   . ASN B 1 156 ? -1.810  45.405 9.828   1.00 28.44 ? 156 ASN B O   1 
ATOM   5388 C CB  . ASN B 1 156 ? -1.390  48.087 9.343   1.00 33.26 ? 156 ASN B CB  1 
ATOM   5389 C CG  . ASN B 1 156 ? -1.326  49.574 9.038   1.00 42.53 ? 156 ASN B CG  1 
ATOM   5390 O OD1 . ASN B 1 156 ? -2.131  50.095 8.268   1.00 42.89 ? 156 ASN B OD1 1 
ATOM   5391 N ND2 . ASN B 1 156 ? -0.361  50.265 9.642   1.00 45.05 ? 156 ASN B ND2 1 
ATOM   5392 N N   . TYR B 1 157 ? -4.052  45.490 9.694   1.00 23.83 ? 157 TYR B N   1 
ATOM   5393 C CA  . TYR B 1 157 ? -4.230  44.075 9.984   1.00 24.94 ? 157 TYR B CA  1 
ATOM   5394 C C   . TYR B 1 157 ? -4.061  43.239 8.725   1.00 24.92 ? 157 TYR B C   1 
ATOM   5395 O O   . TYR B 1 157 ? -4.370  43.682 7.615   1.00 26.51 ? 157 TYR B O   1 
ATOM   5396 C CB  . TYR B 1 157 ? -5.615  43.833 10.588  1.00 22.03 ? 157 TYR B CB  1 
ATOM   5397 C CG  . TYR B 1 157 ? -5.773  44.526 11.921  1.00 21.52 ? 157 TYR B CG  1 
ATOM   5398 C CD1 . TYR B 1 157 ? -5.241  43.968 13.072  1.00 27.27 ? 157 TYR B CD1 1 
ATOM   5399 C CD2 . TYR B 1 157 ? -6.400  45.760 12.018  1.00 21.59 ? 157 TYR B CD2 1 
ATOM   5400 C CE1 . TYR B 1 157 ? -5.359  44.600 14.300  1.00 23.12 ? 157 TYR B CE1 1 
ATOM   5401 C CE2 . TYR B 1 157 ? -6.523  46.401 13.244  1.00 20.90 ? 157 TYR B CE2 1 
ATOM   5402 C CZ  . TYR B 1 157 ? -5.992  45.810 14.379  1.00 22.52 ? 157 TYR B CZ  1 
ATOM   5403 O OH  . TYR B 1 157 ? -6.100  46.424 15.609  1.00 21.28 ? 157 TYR B OH  1 
ATOM   5404 N N   . THR B 1 158 ? -3.580  42.013 8.906   1.00 26.55 ? 158 THR B N   1 
ATOM   5405 C CA  . THR B 1 158 ? -3.470  41.068 7.803   1.00 25.50 ? 158 THR B CA  1 
ATOM   5406 C C   . THR B 1 158 ? -4.628  40.077 7.832   1.00 23.28 ? 158 THR B C   1 
ATOM   5407 O O   . THR B 1 158 ? -5.306  39.903 8.849   1.00 26.32 ? 158 THR B O   1 
ATOM   5408 C CB  . THR B 1 158 ? -2.150  40.293 7.852   1.00 26.13 ? 158 THR B CB  1 
ATOM   5409 O OG1 . THR B 1 158 ? -2.117  39.492 9.037   1.00 29.02 ? 158 THR B OG1 1 
ATOM   5410 C CG2 . THR B 1 158 ? -0.955  41.236 7.832   1.00 30.43 ? 158 THR B CG2 1 
ATOM   5411 N N   . GLN B 1 159 ? -4.845  39.422 6.688   1.00 25.08 ? 159 GLN B N   1 
ATOM   5412 C CA  . GLN B 1 159 ? -5.847  38.364 6.625   1.00 23.77 ? 159 GLN B CA  1 
ATOM   5413 C C   . GLN B 1 159 ? -5.557  37.278 7.658   1.00 26.82 ? 159 GLN B C   1 
ATOM   5414 O O   . GLN B 1 159 ? -6.477  36.748 8.292   1.00 26.52 ? 159 GLN B O   1 
ATOM   5415 C CB  . GLN B 1 159 ? -5.890  37.778 5.209   1.00 24.52 ? 159 GLN B CB  1 
ATOM   5416 C CG  . GLN B 1 159 ? -6.828  36.591 5.054   1.00 27.50 ? 159 GLN B CG  1 
ATOM   5417 C CD  . GLN B 1 159 ? -8.300  36.974 5.081   1.00 30.26 ? 159 GLN B CD  1 
ATOM   5418 O OE1 . GLN B 1 159 ? -8.671  38.115 4.782   1.00 23.91 ? 159 GLN B OE1 1 
ATOM   5419 N NE2 . GLN B 1 159 ? -9.149  36.014 5.437   1.00 29.87 ? 159 GLN B NE2 1 
ATOM   5420 N N   . GLU B 1 160 ? -4.276  36.956 7.860   1.00 23.95 ? 160 GLU B N   1 
ATOM   5421 C CA  . GLU B 1 160 ? -3.910  35.936 8.836   1.00 27.63 ? 160 GLU B CA  1 
ATOM   5422 C C   . GLU B 1 160 ? -4.247  36.376 10.259  1.00 28.98 ? 160 GLU B C   1 
ATOM   5423 O O   . GLU B 1 160 ? -4.736  35.571 11.063  1.00 27.97 ? 160 GLU B O   1 
ATOM   5424 C CB  . GLU B 1 160 ? -2.419  35.611 8.711   1.00 32.22 ? 160 GLU B CB  1 
ATOM   5425 C CG  . GLU B 1 160 ? -2.045  34.818 7.465   1.00 46.05 ? 160 GLU B CG  1 
ATOM   5426 C CD  . GLU B 1 160 ? -2.180  35.613 6.170   1.00 52.75 ? 160 GLU B CD  1 
ATOM   5427 O OE1 . GLU B 1 160 ? -2.201  36.867 6.218   1.00 43.32 ? 160 GLU B OE1 1 
ATOM   5428 O OE2 . GLU B 1 160 ? -2.263  34.974 5.098   1.00 55.27 ? 160 GLU B OE2 1 
ATOM   5429 N N   . GLU B 1 161 ? -4.000  37.648 10.593  1.00 25.53 ? 161 GLU B N   1 
ATOM   5430 C CA  . GLU B 1 161 ? -4.334  38.126 11.934  1.00 25.53 ? 161 GLU B CA  1 
ATOM   5431 C C   . GLU B 1 161 ? -5.838  38.086 12.168  1.00 26.18 ? 161 GLU B C   1 
ATOM   5432 O O   . GLU B 1 161 ? -6.299  37.656 13.234  1.00 24.72 ? 161 GLU B O   1 
ATOM   5433 C CB  . GLU B 1 161 ? -3.789  39.540 12.141  1.00 26.94 ? 161 GLU B CB  1 
ATOM   5434 C CG  . GLU B 1 161 ? -2.290  39.557 12.441  1.00 30.80 ? 161 GLU B CG  1 
ATOM   5435 C CD  . GLU B 1 161 ? -1.618  40.889 12.153  1.00 36.17 ? 161 GLU B CD  1 
ATOM   5436 O OE1 . GLU B 1 161 ? -2.310  41.864 11.791  1.00 31.19 ? 161 GLU B OE1 1 
ATOM   5437 O OE2 . GLU B 1 161 ? -0.376  40.956 12.289  1.00 39.40 ? 161 GLU B OE2 1 
ATOM   5438 N N   . LYS B 1 162 ? -6.614  38.522 11.175  1.00 23.24 ? 162 LYS B N   1 
ATOM   5439 C CA  . LYS B 1 162 ? -8.068  38.449 11.265  1.00 19.07 ? 162 LYS B CA  1 
ATOM   5440 C C   . LYS B 1 162 ? -8.530  37.018 11.501  1.00 21.67 ? 162 LYS B C   1 
ATOM   5441 O O   . LYS B 1 162 ? -9.422  36.773 12.322  1.00 20.92 ? 162 LYS B O   1 
ATOM   5442 C CB  . LYS B 1 162 ? -8.695  39.007 9.985   1.00 19.02 ? 162 LYS B CB  1 
ATOM   5443 C CG  . LYS B 1 162 ? -10.231 39.091 9.998   1.00 21.11 ? 162 LYS B CG  1 
ATOM   5444 C CD  . LYS B 1 162 ? -10.752 39.683 8.689   1.00 22.35 ? 162 LYS B CD  1 
ATOM   5445 C CE  . LYS B 1 162 ? -10.300 38.869 7.500   1.00 25.24 ? 162 LYS B CE  1 
ATOM   5446 N NZ  . LYS B 1 162 ? -10.905 39.386 6.224   1.00 22.53 ? 162 LYS B NZ  1 
ATOM   5447 N N   . GLU B 1 163 ? -7.942  36.058 10.784  1.00 23.85 ? 163 GLU B N   1 
ATOM   5448 C CA  . GLU B 1 163 ? -8.347  34.669 10.953  1.00 21.66 ? 163 GLU B CA  1 
ATOM   5449 C C   . GLU B 1 163 ? -7.989  34.147 12.334  1.00 26.13 ? 163 GLU B C   1 
ATOM   5450 O O   . GLU B 1 163 ? -8.711  33.308 12.880  1.00 26.77 ? 163 GLU B O   1 
ATOM   5451 C CB  . GLU B 1 163 ? -7.708  33.802 9.871   1.00 30.48 ? 163 GLU B CB  1 
ATOM   5452 C CG  . GLU B 1 163 ? -8.365  33.999 8.528   1.00 33.15 ? 163 GLU B CG  1 
ATOM   5453 C CD  . GLU B 1 163 ? -7.596  33.380 7.383   1.00 36.97 ? 163 GLU B CD  1 
ATOM   5454 O OE1 . GLU B 1 163 ? -8.045  33.556 6.237   1.00 35.81 ? 163 GLU B OE1 1 
ATOM   5455 O OE2 . GLU B 1 163 ? -6.554  32.722 7.615   1.00 38.03 ? 163 GLU B OE2 1 
ATOM   5456 N N   . TYR B 1 164 ? -6.881  34.626 12.906  1.00 25.14 ? 164 TYR B N   1 
ATOM   5457 C CA  . TYR B 1 164 ? -6.536  34.262 14.276  1.00 27.22 ? 164 TYR B CA  1 
ATOM   5458 C C   . TYR B 1 164 ? -7.607  34.741 15.247  1.00 25.52 ? 164 TYR B C   1 
ATOM   5459 O O   . TYR B 1 164 ? -8.032  33.997 16.137  1.00 27.21 ? 164 TYR B O   1 
ATOM   5460 C CB  . TYR B 1 164 ? -5.169  34.846 14.644  1.00 24.56 ? 164 TYR B CB  1 
ATOM   5461 C CG  . TYR B 1 164 ? -4.792  34.637 16.092  1.00 32.86 ? 164 TYR B CG  1 
ATOM   5462 C CD1 . TYR B 1 164 ? -4.406  33.386 16.555  1.00 40.67 ? 164 TYR B CD1 1 
ATOM   5463 C CD2 . TYR B 1 164 ? -4.829  35.689 17.000  1.00 39.40 ? 164 TYR B CD2 1 
ATOM   5464 C CE1 . TYR B 1 164 ? -4.064  33.188 17.882  1.00 39.88 ? 164 TYR B CE1 1 
ATOM   5465 C CE2 . TYR B 1 164 ? -4.485  35.502 18.324  1.00 42.49 ? 164 TYR B CE2 1 
ATOM   5466 C CZ  . TYR B 1 164 ? -4.105  34.251 18.761  1.00 42.55 ? 164 TYR B CZ  1 
ATOM   5467 O OH  . TYR B 1 164 ? -3.764  34.058 20.081  1.00 45.92 ? 164 TYR B OH  1 
ATOM   5468 N N   . VAL B 1 165 ? -8.057  35.987 15.086  1.00 20.01 ? 165 VAL B N   1 
ATOM   5469 C CA  . VAL B 1 165 ? -9.132  36.503 15.929  1.00 21.81 ? 165 VAL B CA  1 
ATOM   5470 C C   . VAL B 1 165 ? -10.370 35.623 15.804  1.00 20.12 ? 165 VAL B C   1 
ATOM   5471 O O   . VAL B 1 165 ? -10.984 35.241 16.809  1.00 21.09 ? 165 VAL B O   1 
ATOM   5472 C CB  . VAL B 1 165 ? -9.442  37.968 15.576  1.00 20.49 ? 165 VAL B CB  1 
ATOM   5473 C CG1 . VAL B 1 165 ? -10.629 38.484 16.399  1.00 18.98 ? 165 VAL B CG1 1 
ATOM   5474 C CG2 . VAL B 1 165 ? -8.222  38.836 15.808  1.00 20.83 ? 165 VAL B CG2 1 
ATOM   5475 N N   . LEU B 1 166 ? -10.753 35.282 14.566  1.00 22.24 ? 166 LEU B N   1 
ATOM   5476 C CA  . LEU B 1 166 ? -11.934 34.443 14.372  1.00 22.51 ? 166 LEU B CA  1 
ATOM   5477 C C   . LEU B 1 166 ? -11.762 33.089 15.049  1.00 22.38 ? 166 LEU B C   1 
ATOM   5478 O O   . LEU B 1 166 ? -12.703 32.560 15.652  1.00 24.68 ? 166 LEU B O   1 
ATOM   5479 C CB  . LEU B 1 166 ? -12.215 34.253 12.880  1.00 21.15 ? 166 LEU B CB  1 
ATOM   5480 C CG  . LEU B 1 166 ? -12.832 35.449 12.157  1.00 20.42 ? 166 LEU B CG  1 
ATOM   5481 C CD1 . LEU B 1 166 ? -12.694 35.279 10.644  1.00 25.83 ? 166 LEU B CD1 1 
ATOM   5482 C CD2 . LEU B 1 166 ? -14.290 35.627 12.559  1.00 26.78 ? 166 LEU B CD2 1 
ATOM   5483 N N   . ASN B 1 167 ? -10.567 32.508 14.952  1.00 23.36 ? 167 ASN B N   1 
ATOM   5484 C CA  . ASN B 1 167 ? -10.321 31.225 15.599  1.00 25.30 ? 167 ASN B CA  1 
ATOM   5485 C C   . ASN B 1 167 ? -10.500 31.337 17.108  1.00 23.87 ? 167 ASN B C   1 
ATOM   5486 O O   . ASN B 1 167 ? -11.169 30.503 17.725  1.00 25.96 ? 167 ASN B O   1 
ATOM   5487 C CB  . ASN B 1 167 ? -8.921  30.716 15.253  1.00 30.40 ? 167 ASN B CB  1 
ATOM   5488 C CG  . ASN B 1 167 ? -8.829  30.205 13.830  1.00 44.55 ? 167 ASN B CG  1 
ATOM   5489 O OD1 . ASN B 1 167 ? -9.847  29.958 13.182  1.00 49.26 ? 167 ASN B OD1 1 
ATOM   5490 N ND2 . ASN B 1 167 ? -7.606  30.041 13.333  1.00 42.52 ? 167 ASN B ND2 1 
ATOM   5491 N N   . LYS B 1 168 ? -9.918  32.373 17.716  1.00 23.91 ? 168 LYS B N   1 
ATOM   5492 C CA  . LYS B 1 168 ? -10.062 32.551 19.158  1.00 25.15 ? 168 LYS B CA  1 
ATOM   5493 C C   . LYS B 1 168 ? -11.513 32.814 19.533  1.00 22.64 ? 168 LYS B C   1 
ATOM   5494 O O   . LYS B 1 168 ? -11.988 32.350 20.576  1.00 22.09 ? 168 LYS B O   1 
ATOM   5495 C CB  . LYS B 1 168 ? -9.170  33.695 19.647  1.00 18.63 ? 168 LYS B CB  1 
ATOM   5496 C CG  . LYS B 1 168 ? -7.682  33.453 19.430  1.00 22.87 ? 168 LYS B CG  1 
ATOM   5497 C CD  . LYS B 1 168 ? -7.202  32.219 20.178  1.00 29.72 ? 168 LYS B CD  1 
ATOM   5498 C CE  . LYS B 1 168 ? -7.208  32.424 21.683  1.00 30.36 ? 168 LYS B CE  1 
ATOM   5499 N NZ  . LYS B 1 168 ? -6.439  31.343 22.369  1.00 42.67 ? 168 LYS B NZ  1 
ATOM   5500 N N   . TYR B 1 169 ? -12.238 33.553 18.692  1.00 16.76 ? 169 TYR B N   1 
ATOM   5501 C CA  . TYR B 1 169 ? -13.640 33.823 18.982  1.00 19.57 ? 169 TYR B CA  1 
ATOM   5502 C C   . TYR B 1 169 ? -14.452 32.534 18.968  1.00 18.55 ? 169 TYR B C   1 
ATOM   5503 O O   . TYR B 1 169 ? -15.257 32.283 19.870  1.00 20.05 ? 169 TYR B O   1 
ATOM   5504 C CB  . TYR B 1 169 ? -14.196 34.832 17.980  1.00 18.71 ? 169 TYR B CB  1 
ATOM   5505 C CG  . TYR B 1 169 ? -13.864 36.283 18.300  1.00 23.59 ? 169 TYR B CG  1 
ATOM   5506 C CD1 . TYR B 1 169 ? -12.925 36.614 19.275  1.00 21.27 ? 169 TYR B CD1 1 
ATOM   5507 C CD2 . TYR B 1 169 ? -14.492 37.319 17.624  1.00 18.12 ? 169 TYR B CD2 1 
ATOM   5508 C CE1 . TYR B 1 169 ? -12.623 37.944 19.558  1.00 22.29 ? 169 TYR B CE1 1 
ATOM   5509 C CE2 . TYR B 1 169 ? -14.198 38.654 17.905  1.00 17.83 ? 169 TYR B CE2 1 
ATOM   5510 C CZ  . TYR B 1 169 ? -13.279 38.962 18.872  1.00 16.30 ? 169 TYR B CZ  1 
ATOM   5511 O OH  . TYR B 1 169 ? -12.989 40.287 19.135  1.00 19.73 ? 169 TYR B OH  1 
ATOM   5512 N N   . PHE B 1 170 ? -14.245 31.695 17.951  1.00 18.30 ? 170 PHE B N   1 
ATOM   5513 C CA  . PHE B 1 170 ? -14.986 30.445 17.911  1.00 21.26 ? 170 PHE B CA  1 
ATOM   5514 C C   . PHE B 1 170 ? -14.592 29.529 19.059  1.00 21.98 ? 170 PHE B C   1 
ATOM   5515 O O   . PHE B 1 170 ? -15.417 28.740 19.526  1.00 19.60 ? 170 PHE B O   1 
ATOM   5516 C CB  . PHE B 1 170 ? -14.799 29.763 16.553  1.00 20.09 ? 170 PHE B CB  1 
ATOM   5517 C CG  . PHE B 1 170 ? -15.804 30.223 15.531  1.00 20.88 ? 170 PHE B CG  1 
ATOM   5518 C CD1 . PHE B 1 170 ? -17.101 29.724 15.549  1.00 24.83 ? 170 PHE B CD1 1 
ATOM   5519 C CD2 . PHE B 1 170 ? -15.476 31.202 14.599  1.00 29.36 ? 170 PHE B CD2 1 
ATOM   5520 C CE1 . PHE B 1 170 ? -18.052 30.160 14.635  1.00 24.86 ? 170 PHE B CE1 1 
ATOM   5521 C CE2 . PHE B 1 170 ? -16.417 31.650 13.679  1.00 29.68 ? 170 PHE B CE2 1 
ATOM   5522 C CZ  . PHE B 1 170 ? -17.710 31.128 13.696  1.00 27.17 ? 170 PHE B CZ  1 
ATOM   5523 N N   . GLU B 1 171 ? -13.347 29.621 19.532  1.00 22.43 ? 171 GLU B N   1 
ATOM   5524 C CA  . GLU B 1 171 ? -12.958 28.875 20.726  1.00 23.75 ? 171 GLU B CA  1 
ATOM   5525 C C   . GLU B 1 171 ? -13.803 29.293 21.927  1.00 25.33 ? 171 GLU B C   1 
ATOM   5526 O O   . GLU B 1 171 ? -14.272 28.440 22.692  1.00 22.61 ? 171 GLU B O   1 
ATOM   5527 C CB  . GLU B 1 171 ? -11.474 29.094 21.004  1.00 26.95 ? 171 GLU B CB  1 
ATOM   5528 C CG  . GLU B 1 171 ? -10.928 28.407 22.238  1.00 41.52 ? 171 GLU B CG  1 
ATOM   5529 C CD  . GLU B 1 171 ? -9.415  28.532 22.319  1.00 55.32 ? 171 GLU B CD  1 
ATOM   5530 O OE1 . GLU B 1 171 ? -8.836  28.229 23.386  1.00 61.10 ? 171 GLU B OE1 1 
ATOM   5531 O OE2 . GLU B 1 171 ? -8.808  28.948 21.309  1.00 54.81 ? 171 GLU B OE2 1 
ATOM   5532 N N   . ILE B 1 172 ? -14.007 30.603 22.102  1.00 20.25 ? 172 ILE B N   1 
ATOM   5533 C CA  . ILE B 1 172 ? -14.869 31.108 23.172  1.00 22.45 ? 172 ILE B CA  1 
ATOM   5534 C C   . ILE B 1 172 ? -16.279 30.536 23.038  1.00 18.45 ? 172 ILE B C   1 
ATOM   5535 O O   . ILE B 1 172 ? -16.873 30.064 24.019  1.00 21.38 ? 172 ILE B O   1 
ATOM   5536 C CB  . ILE B 1 172 ? -14.881 32.649 23.172  1.00 20.08 ? 172 ILE B CB  1 
ATOM   5537 C CG1 . ILE B 1 172 ? -13.551 33.215 23.683  1.00 22.46 ? 172 ILE B CG1 1 
ATOM   5538 C CG2 . ILE B 1 172 ? -16.057 33.188 24.006  1.00 22.34 ? 172 ILE B CG2 1 
ATOM   5539 C CD1 . ILE B 1 172 ? -13.288 32.963 25.165  1.00 24.10 ? 172 ILE B CD1 1 
ATOM   5540 N N   . ILE B 1 173 ? -16.831 30.552 21.820  1.00 16.12 ? 173 ILE B N   1 
ATOM   5541 C CA  . ILE B 1 173 ? -18.190 30.051 21.625  1.00 16.69 ? 173 ILE B CA  1 
ATOM   5542 C C   . ILE B 1 173 ? -18.277 28.575 21.999  1.00 19.15 ? 173 ILE B C   1 
ATOM   5543 O O   . ILE B 1 173 ? -19.226 28.139 22.660  1.00 21.71 ? 173 ILE B O   1 
ATOM   5544 C CB  . ILE B 1 173 ? -18.653 30.291 20.175  1.00 18.56 ? 173 ILE B CB  1 
ATOM   5545 C CG1 . ILE B 1 173 ? -18.804 31.790 19.895  1.00 17.92 ? 173 ILE B CG1 1 
ATOM   5546 C CG2 . ILE B 1 173 ? -19.954 29.530 19.895  1.00 23.82 ? 173 ILE B CG2 1 
ATOM   5547 C CD1 . ILE B 1 173 ? -19.163 32.103 18.448  1.00 19.21 ? 173 ILE B CD1 1 
ATOM   5548 N N   . LYS B 1 174 ? -17.276 27.789 21.594  1.00 21.19 ? 174 LYS B N   1 
ATOM   5549 C CA  . LYS B 1 174 ? -17.265 26.360 21.878  1.00 20.57 ? 174 LYS B CA  1 
ATOM   5550 C C   . LYS B 1 174 ? -17.181 26.061 23.368  1.00 24.65 ? 174 LYS B C   1 
ATOM   5551 O O   . LYS B 1 174 ? -17.614 24.986 23.794  1.00 23.96 ? 174 LYS B O   1 
ATOM   5552 C CB  . LYS B 1 174 ? -16.096 25.703 21.148  1.00 22.06 ? 174 LYS B CB  1 
ATOM   5553 C CG  . LYS B 1 174 ? -16.312 25.590 19.654  1.00 26.67 ? 174 LYS B CG  1 
ATOM   5554 C CD  . LYS B 1 174 ? -15.486 24.464 19.072  1.00 36.40 ? 174 LYS B CD  1 
ATOM   5555 C CE  . LYS B 1 174 ? -14.276 25.000 18.339  1.00 47.58 ? 174 LYS B CE  1 
ATOM   5556 N NZ  . LYS B 1 174 ? -14.437 24.888 16.862  1.00 49.15 ? 174 LYS B NZ  1 
ATOM   5557 N N   . LYS B 1 175 ? -16.644 26.984 24.168  1.00 20.80 ? 175 LYS B N   1 
ATOM   5558 C CA  . LYS B 1 175 ? -16.553 26.811 25.613  1.00 25.11 ? 175 LYS B CA  1 
ATOM   5559 C C   . LYS B 1 175 ? -17.730 27.415 26.366  1.00 17.93 ? 175 LYS B C   1 
ATOM   5560 O O   . LYS B 1 175 ? -17.729 27.394 27.600  1.00 20.16 ? 175 LYS B O   1 
ATOM   5561 C CB  . LYS B 1 175 ? -15.257 27.436 26.142  1.00 25.46 ? 175 LYS B CB  1 
ATOM   5562 C CG  . LYS B 1 175 ? -13.996 26.691 25.705  1.00 34.70 ? 175 LYS B CG  1 
ATOM   5563 C CD  . LYS B 1 175 ? -12.713 27.429 26.090  1.00 47.83 ? 175 LYS B CD  1 
ATOM   5564 C CE  . LYS B 1 175 ? -12.988 28.837 26.610  1.00 54.96 ? 175 LYS B CE  1 
ATOM   5565 N NZ  . LYS B 1 175 ? -11.731 29.583 26.910  1.00 63.25 ? 175 LYS B NZ  1 
ATOM   5566 N N   . THR B 1 176 ? -18.733 27.946 25.669  1.00 19.57 ? 176 THR B N   1 
ATOM   5567 C CA  . THR B 1 176 ? -19.732 28.764 26.354  1.00 18.68 ? 176 THR B CA  1 
ATOM   5568 C C   . THR B 1 176 ? -20.700 27.913 27.175  1.00 20.13 ? 176 THR B C   1 
ATOM   5569 O O   . THR B 1 176 ? -20.923 28.187 28.360  1.00 22.01 ? 176 THR B O   1 
ATOM   5570 C CB  . THR B 1 176 ? -20.467 29.639 25.341  1.00 16.39 ? 176 THR B CB  1 
ATOM   5571 O OG1 . THR B 1 176 ? -19.548 30.616 24.833  1.00 21.07 ? 176 THR B OG1 1 
ATOM   5572 C CG2 . THR B 1 176 ? -21.646 30.369 25.992  1.00 16.26 ? 176 THR B CG2 1 
ATOM   5573 N N   . LEU B 1 177 ? -21.309 26.892 26.573  1.00 18.88 ? 177 LEU B N   1 
ATOM   5574 C CA  . LEU B 1 177 ? -22.216 26.068 27.371  1.00 18.87 ? 177 LEU B CA  1 
ATOM   5575 C C   . LEU B 1 177 ? -21.490 25.408 28.535  1.00 22.52 ? 177 LEU B C   1 
ATOM   5576 O O   . LEU B 1 177 ? -22.066 25.261 29.623  1.00 22.61 ? 177 LEU B O   1 
ATOM   5577 C CB  . LEU B 1 177 ? -22.905 25.020 26.503  1.00 22.43 ? 177 LEU B CB  1 
ATOM   5578 C CG  . LEU B 1 177 ? -23.868 25.627 25.480  1.00 25.66 ? 177 LEU B CG  1 
ATOM   5579 C CD1 . LEU B 1 177 ? -24.599 24.534 24.717  1.00 31.30 ? 177 LEU B CD1 1 
ATOM   5580 C CD2 . LEU B 1 177 ? -24.857 26.550 26.159  1.00 26.24 ? 177 LEU B CD2 1 
ATOM   5581 N N   . SER B 1 178 ? -20.222 25.037 28.335  1.00 22.65 ? 178 SER B N   1 
ATOM   5582 C CA  . SER B 1 178 ? -19.458 24.383 29.390  1.00 25.00 ? 178 SER B CA  1 
ATOM   5583 C C   . SER B 1 178 ? -19.284 25.278 30.606  1.00 22.00 ? 178 SER B C   1 
ATOM   5584 O O   . SER B 1 178 ? -19.278 24.778 31.738  1.00 23.61 ? 178 SER B O   1 
ATOM   5585 C CB  . SER B 1 178 ? -18.094 23.951 28.855  1.00 25.63 ? 178 SER B CB  1 
ATOM   5586 O OG  . SER B 1 178 ? -18.210 22.719 28.179  1.00 36.24 ? 178 SER B OG  1 
ATOM   5587 N N   . ILE B 1 179 ? -19.145 26.595 30.406  1.00 19.06 ? 179 ILE B N   1 
ATOM   5588 C CA  . ILE B 1 179 ? -18.948 27.456 31.565  1.00 20.14 ? 179 ILE B CA  1 
ATOM   5589 C C   . ILE B 1 179 ? -20.245 27.593 32.353  1.00 20.67 ? 179 ILE B C   1 
ATOM   5590 O O   . ILE B 1 179 ? -20.213 27.695 33.584  1.00 22.49 ? 179 ILE B O   1 
ATOM   5591 C CB  . ILE B 1 179 ? -18.349 28.822 31.168  1.00 19.50 ? 179 ILE B CB  1 
ATOM   5592 C CG1 . ILE B 1 179 ? -17.719 29.482 32.404  1.00 31.83 ? 179 ILE B CG1 1 
ATOM   5593 C CG2 . ILE B 1 179 ? -19.378 29.770 30.549  1.00 16.73 ? 179 ILE B CG2 1 
ATOM   5594 C CD1 . ILE B 1 179 ? -16.734 30.580 32.066  1.00 30.48 ? 179 ILE B CD1 1 
ATOM   5595 N N   . TYR B 1 180 ? -21.403 27.546 31.683  1.00 18.31 ? 180 TYR B N   1 
ATOM   5596 C CA  . TYR B 1 180 ? -22.667 27.534 32.418  1.00 19.39 ? 180 TYR B CA  1 
ATOM   5597 C C   . TYR B 1 180 ? -22.814 26.259 33.237  1.00 20.46 ? 180 TYR B C   1 
ATOM   5598 O O   . TYR B 1 180 ? -23.214 26.312 34.404  1.00 19.50 ? 180 TYR B O   1 
ATOM   5599 C CB  . TYR B 1 180 ? -23.849 27.713 31.461  1.00 16.41 ? 180 TYR B CB  1 
ATOM   5600 C CG  . TYR B 1 180 ? -23.962 29.145 30.993  1.00 20.20 ? 180 TYR B CG  1 
ATOM   5601 C CD1 . TYR B 1 180 ? -24.490 30.123 31.828  1.00 14.85 ? 180 TYR B CD1 1 
ATOM   5602 C CD2 . TYR B 1 180 ? -23.495 29.524 29.743  1.00 15.53 ? 180 TYR B CD2 1 
ATOM   5603 C CE1 . TYR B 1 180 ? -24.572 31.449 31.418  1.00 15.95 ? 180 TYR B CE1 1 
ATOM   5604 C CE2 . TYR B 1 180 ? -23.571 30.849 29.321  1.00 14.53 ? 180 TYR B CE2 1 
ATOM   5605 C CZ  . TYR B 1 180 ? -24.108 31.805 30.166  1.00 13.84 ? 180 TYR B CZ  1 
ATOM   5606 O OH  . TYR B 1 180 ? -24.188 33.118 29.774  1.00 14.71 ? 180 TYR B OH  1 
ATOM   5607 N N   . ARG B 1 181 ? -22.483 25.104 32.656  1.00 20.87 ? 181 ARG B N   1 
ATOM   5608 C CA  . ARG B 1 181 ? -22.471 23.880 33.449  1.00 22.67 ? 181 ARG B CA  1 
ATOM   5609 C C   . ARG B 1 181 ? -21.499 23.990 34.618  1.00 20.77 ? 181 ARG B C   1 
ATOM   5610 O O   . ARG B 1 181 ? -21.772 23.482 35.712  1.00 23.87 ? 181 ARG B O   1 
ATOM   5611 C CB  . ARG B 1 181 ? -22.096 22.670 32.589  1.00 27.71 ? 181 ARG B CB  1 
ATOM   5612 C CG  . ARG B 1 181 ? -23.021 22.347 31.431  1.00 25.07 ? 181 ARG B CG  1 
ATOM   5613 C CD  . ARG B 1 181 ? -22.582 21.049 30.753  1.00 26.96 ? 181 ARG B CD  1 
ATOM   5614 N NE  . ARG B 1 181 ? -23.248 20.883 29.471  1.00 31.97 ? 181 ARG B NE  1 
ATOM   5615 C CZ  . ARG B 1 181 ? -22.718 21.225 28.301  1.00 31.95 ? 181 ARG B CZ  1 
ATOM   5616 N NH1 . ARG B 1 181 ? -21.493 21.732 28.241  1.00 29.76 ? 181 ARG B NH1 1 
ATOM   5617 N NH2 . ARG B 1 181 ? -23.406 21.044 27.185  1.00 34.08 ? 181 ARG B NH2 1 
ATOM   5618 N N   . GLU B 1 182 ? -20.359 24.652 34.407  1.00 20.98 ? 182 GLU B N   1 
ATOM   5619 C CA  . GLU B 1 182 ? -19.330 24.704 35.443  1.00 21.22 ? 182 GLU B CA  1 
ATOM   5620 C C   . GLU B 1 182 ? -19.775 25.556 36.625  1.00 21.71 ? 182 GLU B C   1 
ATOM   5621 O O   . GLU B 1 182 ? -19.669 25.136 37.786  1.00 21.56 ? 182 GLU B O   1 
ATOM   5622 C CB  . GLU B 1 182 ? -18.022 25.235 34.851  1.00 26.40 ? 182 GLU B CB  1 
ATOM   5623 C CG  . GLU B 1 182 ? -16.918 25.442 35.864  1.00 40.17 ? 182 GLU B CG  1 
ATOM   5624 C CD  . GLU B 1 182 ? -15.633 25.954 35.236  1.00 51.12 ? 182 GLU B CD  1 
ATOM   5625 O OE1 . GLU B 1 182 ? -15.569 26.051 33.992  1.00 52.85 ? 182 GLU B OE1 1 
ATOM   5626 O OE2 . GLU B 1 182 ? -14.689 26.266 35.992  1.00 56.28 ? 182 GLU B OE2 1 
ATOM   5627 N N   . ILE B 1 183 ? -20.260 26.770 36.359  1.00 20.89 ? 183 ILE B N   1 
ATOM   5628 C CA  . ILE B 1 183 ? -20.632 27.617 37.485  1.00 22.51 ? 183 ILE B CA  1 
ATOM   5629 C C   . ILE B 1 183 ? -21.826 27.030 38.208  1.00 23.97 ? 183 ILE B C   1 
ATOM   5630 O O   . ILE B 1 183 ? -21.973 27.186 39.425  1.00 21.92 ? 183 ILE B O   1 
ATOM   5631 C CB  . ILE B 1 183 ? -20.876 29.063 37.016  1.00 24.68 ? 183 ILE B CB  1 
ATOM   5632 C CG1 . ILE B 1 183 ? -22.072 29.157 36.054  1.00 21.09 ? 183 ILE B CG1 1 
ATOM   5633 C CG2 . ILE B 1 183 ? -19.611 29.619 36.387  1.00 21.46 ? 183 ILE B CG2 1 
ATOM   5634 C CD1 . ILE B 1 183 ? -23.337 29.692 36.711  1.00 19.77 ? 183 ILE B CD1 1 
ATOM   5635 N N   . LYS B 1 184 ? -22.660 26.292 37.498  1.00 19.21 ? 184 LYS B N   1 
ATOM   5636 C CA  . LYS B 1 184 ? -23.817 25.682 38.128  1.00 21.38 ? 184 LYS B CA  1 
ATOM   5637 C C   . LYS B 1 184 ? -23.402 24.522 39.027  1.00 24.65 ? 184 LYS B C   1 
ATOM   5638 O O   . LYS B 1 184 ? -23.793 24.452 40.201  1.00 25.70 ? 184 LYS B O   1 
ATOM   5639 C CB  . LYS B 1 184 ? -24.763 25.242 37.031  1.00 25.73 ? 184 LYS B CB  1 
ATOM   5640 C CG  . LYS B 1 184 ? -25.933 24.513 37.491  1.00 31.93 ? 184 LYS B CG  1 
ATOM   5641 C CD  . LYS B 1 184 ? -26.747 24.181 36.272  1.00 26.89 ? 184 LYS B CD  1 
ATOM   5642 C CE  . LYS B 1 184 ? -27.971 23.431 36.681  1.00 30.55 ? 184 LYS B CE  1 
ATOM   5643 N NZ  . LYS B 1 184 ? -27.496 22.308 37.526  1.00 37.21 ? 184 LYS B NZ  1 
ATOM   5644 N N   . GLU B 1 185 ? -22.577 23.614 38.512  1.00 24.49 ? 185 GLU B N   1 
ATOM   5645 C CA  . GLU B 1 185 ? -22.165 22.505 39.360  1.00 25.40 ? 185 GLU B CA  1 
ATOM   5646 C C   . GLU B 1 185 ? -21.270 22.984 40.504  1.00 24.40 ? 185 GLU B C   1 
ATOM   5647 O O   . GLU B 1 185 ? -21.265 22.378 41.581  1.00 29.28 ? 185 GLU B O   1 
ATOM   5648 C CB  . GLU B 1 185 ? -21.481 21.417 38.521  1.00 32.55 ? 185 GLU B CB  1 
ATOM   5649 C CG  . GLU B 1 185 ? -21.441 20.098 39.271  1.00 52.76 ? 185 GLU B CG  1 
ATOM   5650 C CD  . GLU B 1 185 ? -20.401 20.121 40.356  1.00 68.79 ? 185 GLU B CD  1 
ATOM   5651 O OE1 . GLU B 1 185 ? -20.617 19.522 41.434  1.00 72.90 ? 185 GLU B OE1 1 
ATOM   5652 O OE2 . GLU B 1 185 ? -19.363 20.770 40.123  1.00 71.32 ? 185 GLU B OE2 1 
ATOM   5653 N N   . GLU B 1 186 ? -20.558 24.094 40.320  1.00 26.08 ? 186 GLU B N   1 
ATOM   5654 C CA  . GLU B 1 186 ? -19.727 24.648 41.381  1.00 28.62 ? 186 GLU B CA  1 
ATOM   5655 C C   . GLU B 1 186 ? -20.521 25.417 42.431  1.00 24.92 ? 186 GLU B C   1 
ATOM   5656 O O   . GLU B 1 186 ? -19.924 25.873 43.414  1.00 29.13 ? 186 GLU B O   1 
ATOM   5657 C CB  . GLU B 1 186 ? -18.644 25.547 40.779  1.00 29.59 ? 186 GLU B CB  1 
ATOM   5658 C CG  . GLU B 1 186 ? -17.498 24.764 40.150  1.00 31.51 ? 186 GLU B CG  1 
ATOM   5659 C CD  . GLU B 1 186 ? -16.590 25.617 39.281  1.00 41.72 ? 186 GLU B CD  1 
ATOM   5660 O OE1 . GLU B 1 186 ? -16.836 26.837 39.153  1.00 40.36 ? 186 GLU B OE1 1 
ATOM   5661 O OE2 . GLU B 1 186 ? -15.620 25.061 38.723  1.00 44.70 ? 186 GLU B OE2 1 
ATOM   5662 N N   . GLY B 1 187 ? -21.836 25.565 42.258  1.00 24.33 ? 187 GLY B N   1 
ATOM   5663 C CA  . GLY B 1 187 ? -22.641 26.302 43.215  1.00 26.99 ? 187 GLY B CA  1 
ATOM   5664 C C   . GLY B 1 187 ? -22.472 27.799 43.147  1.00 28.51 ? 187 GLY B C   1 
ATOM   5665 O O   . GLY B 1 187 ? -22.871 28.510 44.080  1.00 23.06 ? 187 GLY B O   1 
ATOM   5666 N N   . LYS B 1 188 ? -21.891 28.307 42.067  1.00 22.70 ? 188 LYS B N   1 
ATOM   5667 C CA  . LYS B 1 188 ? -21.646 29.736 41.971  1.00 20.98 ? 188 LYS B CA  1 
ATOM   5668 C C   . LYS B 1 188 ? -22.823 30.490 41.393  1.00 18.72 ? 188 LYS B C   1 
ATOM   5669 O O   . LYS B 1 188 ? -22.886 31.713 41.545  1.00 18.50 ? 188 LYS B O   1 
ATOM   5670 C CB  . LYS B 1 188 ? -20.398 30.007 41.132  1.00 22.71 ? 188 LYS B CB  1 
ATOM   5671 C CG  . LYS B 1 188 ? -19.137 29.471 41.793  1.00 24.49 ? 188 LYS B CG  1 
ATOM   5672 C CD  . LYS B 1 188 ? -17.910 29.750 40.944  1.00 25.01 ? 188 LYS B CD  1 
ATOM   5673 C CE  . LYS B 1 188 ? -16.647 29.264 41.633  1.00 38.53 ? 188 LYS B CE  1 
ATOM   5674 N NZ  . LYS B 1 188 ? -15.480 30.107 41.248  1.00 41.58 ? 188 LYS B NZ  1 
ATOM   5675 N N   . GLY B 1 189 ? -23.757 29.791 40.762  1.00 17.93 ? 189 GLY B N   1 
ATOM   5676 C CA  . GLY B 1 189 ? -24.957 30.418 40.262  1.00 16.72 ? 189 GLY B CA  1 
ATOM   5677 C C   . GLY B 1 189 ? -25.950 29.369 39.829  1.00 20.90 ? 189 GLY B C   1 
ATOM   5678 O O   . GLY B 1 189 ? -25.589 28.213 39.571  1.00 21.37 ? 189 GLY B O   1 
ATOM   5679 N N   . SER B 1 190 ? -27.215 29.779 39.793  1.00 18.27 ? 190 SER B N   1 
ATOM   5680 C CA  . SER B 1 190 ? -28.266 28.967 39.201  1.00 16.02 ? 190 SER B CA  1 
ATOM   5681 C C   . SER B 1 190 ? -28.441 29.373 37.745  1.00 19.18 ? 190 SER B C   1 
ATOM   5682 O O   . SER B 1 190 ? -28.137 30.504 37.362  1.00 14.11 ? 190 SER B O   1 
ATOM   5683 C CB  . SER B 1 190 ? -29.584 29.140 39.955  1.00 14.97 ? 190 SER B CB  1 
ATOM   5684 O OG  . SER B 1 190 ? -29.492 28.700 41.294  1.00 16.74 ? 190 SER B OG  1 
ATOM   5685 N N   . VAL B 1 191 ? -28.925 28.439 36.931  1.00 16.71 ? 191 VAL B N   1 
ATOM   5686 C CA  . VAL B 1 191 ? -29.251 28.708 35.536  1.00 15.91 ? 191 VAL B CA  1 
ATOM   5687 C C   . VAL B 1 191 ? -30.714 28.358 35.313  1.00 14.40 ? 191 VAL B C   1 
ATOM   5688 O O   . VAL B 1 191 ? -31.149 27.248 35.640  1.00 16.43 ? 191 VAL B O   1 
ATOM   5689 C CB  . VAL B 1 191 ? -28.354 27.922 34.565  1.00 14.01 ? 191 VAL B CB  1 
ATOM   5690 C CG1 . VAL B 1 191 ? -28.671 28.317 33.116  1.00 15.24 ? 191 VAL B CG1 1 
ATOM   5691 C CG2 . VAL B 1 191 ? -26.896 28.154 34.869  1.00 17.27 ? 191 VAL B CG2 1 
ATOM   5692 N N   . SER B 1 192 ? -31.463 29.301 34.757  1.00 12.67 ? 192 SER B N   1 
ATOM   5693 C CA  . SER B 1 192 ? -32.859 29.120 34.411  1.00 13.56 ? 192 SER B CA  1 
ATOM   5694 C C   . SER B 1 192 ? -33.001 29.073 32.894  1.00 18.03 ? 192 SER B C   1 
ATOM   5695 O O   . SER B 1 192 ? -32.035 29.253 32.144  1.00 15.09 ? 192 SER B O   1 
ATOM   5696 C CB  . SER B 1 192 ? -33.705 30.254 34.992  1.00 16.87 ? 192 SER B CB  1 
ATOM   5697 O OG  . SER B 1 192 ? -33.388 31.500 34.371  1.00 16.80 ? 192 SER B OG  1 
ATOM   5698 N N   . THR B 1 193 ? -34.231 28.853 32.441  1.00 11.92 ? 193 THR B N   1 
ATOM   5699 C CA  . THR B 1 193 ? -34.555 29.039 31.034  1.00 12.16 ? 193 THR B CA  1 
ATOM   5700 C C   . THR B 1 193 ? -35.920 29.716 30.941  1.00 13.62 ? 193 THR B C   1 
ATOM   5701 O O   . THR B 1 193 ? -36.583 29.970 31.946  1.00 15.04 ? 193 THR B O   1 
ATOM   5702 C CB  . THR B 1 193 ? -34.514 27.709 30.261  1.00 17.19 ? 193 THR B CB  1 
ATOM   5703 O OG1 . THR B 1 193 ? -34.515 27.965 28.846  1.00 17.17 ? 193 THR B OG1 1 
ATOM   5704 C CG2 . THR B 1 193 ? -35.711 26.814 30.614  1.00 18.40 ? 193 THR B CG2 1 
ATOM   5705 N N   . SER B 1 194 ? -36.336 29.999 29.719  1.00 14.97 ? 194 SER B N   1 
ATOM   5706 C CA  . SER B 1 194 ? -37.612 30.611 29.393  1.00 14.43 ? 194 SER B CA  1 
ATOM   5707 C C   . SER B 1 194 ? -38.365 29.694 28.442  1.00 13.51 ? 194 SER B C   1 
ATOM   5708 O O   . SER B 1 194 ? -37.753 28.859 27.771  1.00 16.99 ? 194 SER B O   1 
ATOM   5709 C CB  . SER B 1 194 ? -37.405 31.963 28.702  1.00 12.15 ? 194 SER B CB  1 
ATOM   5710 O OG  . SER B 1 194 ? -36.856 32.917 29.590  1.00 15.04 ? 194 SER B OG  1 
ATOM   5711 N N   . PRO B 1 195 ? -39.685 29.848 28.329  1.00 14.17 ? 195 PRO B N   1 
ATOM   5712 C CA  . PRO B 1 195 ? -40.417 29.167 27.250  1.00 14.26 ? 195 PRO B CA  1 
ATOM   5713 C C   . PRO B 1 195 ? -39.711 29.394 25.914  1.00 14.36 ? 195 PRO B C   1 
ATOM   5714 O O   . PRO B 1 195 ? -39.179 30.479 25.649  1.00 15.03 ? 195 PRO B O   1 
ATOM   5715 C CB  . PRO B 1 195 ? -41.802 29.822 27.286  1.00 18.78 ? 195 PRO B CB  1 
ATOM   5716 C CG  . PRO B 1 195 ? -41.947 30.314 28.720  1.00 23.40 ? 195 PRO B CG  1 
ATOM   5717 C CD  . PRO B 1 195 ? -40.563 30.605 29.240  1.00 17.26 ? 195 PRO B CD  1 
ATOM   5718 N N   . TYR B 1 196 ? -39.766 28.368 25.058  1.00 17.02 ? 196 TYR B N   1 
ATOM   5719 C CA  . TYR B 1 196 ? -38.706 28.081 24.088  1.00 19.73 ? 196 TYR B CA  1 
ATOM   5720 C C   . TYR B 1 196 ? -38.328 29.285 23.228  1.00 20.44 ? 196 TYR B C   1 
ATOM   5721 O O   . TYR B 1 196 ? -37.158 29.669 23.168  1.00 16.19 ? 196 TYR B O   1 
ATOM   5722 C CB  . TYR B 1 196 ? -39.117 26.903 23.201  1.00 15.72 ? 196 TYR B CB  1 
ATOM   5723 C CG  . TYR B 1 196 ? -37.943 26.173 22.577  1.00 16.09 ? 196 TYR B CG  1 
ATOM   5724 C CD1 . TYR B 1 196 ? -37.231 26.730 21.523  1.00 17.46 ? 196 TYR B CD1 1 
ATOM   5725 C CD2 . TYR B 1 196 ? -37.545 24.930 23.050  1.00 17.09 ? 196 TYR B CD2 1 
ATOM   5726 C CE1 . TYR B 1 196 ? -36.162 26.063 20.953  1.00 20.08 ? 196 TYR B CE1 1 
ATOM   5727 C CE2 . TYR B 1 196 ? -36.501 24.256 22.487  1.00 20.57 ? 196 TYR B CE2 1 
ATOM   5728 C CZ  . TYR B 1 196 ? -35.802 24.819 21.443  1.00 23.59 ? 196 TYR B CZ  1 
ATOM   5729 O OH  . TYR B 1 196 ? -34.739 24.141 20.898  1.00 20.63 ? 196 TYR B OH  1 
ATOM   5730 N N   . TYR B 1 197 ? -39.287 29.876 22.515  1.00 15.37 ? 197 TYR B N   1 
ATOM   5731 C CA  . TYR B 1 197 ? -38.934 30.965 21.610  1.00 18.02 ? 197 TYR B CA  1 
ATOM   5732 C C   . TYR B 1 197 ? -39.236 32.337 22.201  1.00 16.09 ? 197 TYR B C   1 
ATOM   5733 O O   . TYR B 1 197 ? -39.408 33.304 21.460  1.00 13.92 ? 197 TYR B O   1 
ATOM   5734 C CB  . TYR B 1 197 ? -39.611 30.771 20.252  1.00 20.38 ? 197 TYR B CB  1 
ATOM   5735 C CG  . TYR B 1 197 ? -39.039 29.573 19.524  1.00 19.10 ? 197 TYR B CG  1 
ATOM   5736 C CD1 . TYR B 1 197 ? -37.781 29.631 18.931  1.00 16.57 ? 197 TYR B CD1 1 
ATOM   5737 C CD2 . TYR B 1 197 ? -39.731 28.369 19.483  1.00 20.69 ? 197 TYR B CD2 1 
ATOM   5738 C CE1 . TYR B 1 197 ? -37.242 28.535 18.300  1.00 19.08 ? 197 TYR B CE1 1 
ATOM   5739 C CE2 . TYR B 1 197 ? -39.201 27.262 18.845  1.00 21.68 ? 197 TYR B CE2 1 
ATOM   5740 C CZ  . TYR B 1 197 ? -37.955 27.353 18.263  1.00 19.70 ? 197 TYR B CZ  1 
ATOM   5741 O OH  . TYR B 1 197 ? -37.433 26.250 17.643  1.00 25.31 ? 197 TYR B OH  1 
ATOM   5742 N N   . HIS B 1 198 ? -39.270 32.444 23.525  1.00 17.29 ? 198 HIS B N   1 
ATOM   5743 C CA  . HIS B 1 198 ? -39.454 33.723 24.204  1.00 13.13 ? 198 HIS B CA  1 
ATOM   5744 C C   . HIS B 1 198 ? -40.785 34.373 23.802  1.00 15.12 ? 198 HIS B C   1 
ATOM   5745 O O   . HIS B 1 198 ? -40.797 35.556 23.438  1.00 15.45 ? 198 HIS B O   1 
ATOM   5746 C CB  . HIS B 1 198 ? -38.250 34.628 23.884  1.00 11.93 ? 198 HIS B CB  1 
ATOM   5747 C CG  . HIS B 1 198 ? -38.050 35.778 24.829  1.00 11.78 ? 198 HIS B CG  1 
ATOM   5748 N ND1 . HIS B 1 198 ? -38.558 37.039 24.586  1.00 14.74 ? 198 HIS B ND1 1 
ATOM   5749 C CD2 . HIS B 1 198 ? -37.366 35.868 25.995  1.00 15.07 ? 198 HIS B CD2 1 
ATOM   5750 C CE1 . HIS B 1 198 ? -38.203 37.851 25.568  1.00 20.08 ? 198 HIS B CE1 1 
ATOM   5751 N NE2 . HIS B 1 198 ? -37.481 37.167 26.436  1.00 16.89 ? 198 HIS B NE2 1 
ATOM   5752 N N   . PRO B 1 199 ? -41.920 33.658 23.868  1.00 15.84 ? 199 PRO B N   1 
ATOM   5753 C CA  . PRO B 1 199 ? -43.213 34.266 23.524  1.00 17.43 ? 199 PRO B CA  1 
ATOM   5754 C C   . PRO B 1 199 ? -43.827 35.007 24.710  1.00 19.35 ? 199 PRO B C   1 
ATOM   5755 O O   . PRO B 1 199 ? -43.391 34.878 25.853  1.00 18.02 ? 199 PRO B O   1 
ATOM   5756 C CB  . PRO B 1 199 ? -44.068 33.049 23.161  1.00 16.91 ? 199 PRO B CB  1 
ATOM   5757 C CG  . PRO B 1 199 ? -43.596 32.018 24.140  1.00 14.97 ? 199 PRO B CG  1 
ATOM   5758 C CD  . PRO B 1 199 ? -42.101 32.254 24.288  1.00 16.98 ? 199 PRO B CD  1 
ATOM   5759 N N   . LEU B 1 200 ? -44.900 35.753 24.424  1.00 20.58 ? 200 LEU B N   1 
ATOM   5760 C CA  . LEU B 1 200 ? -45.732 36.350 25.475  1.00 17.20 ? 200 LEU B CA  1 
ATOM   5761 C C   . LEU B 1 200 ? -46.778 35.319 25.886  1.00 19.42 ? 200 LEU B C   1 
ATOM   5762 O O   . LEU B 1 200 ? -47.879 35.254 25.331  1.00 17.41 ? 200 LEU B O   1 
ATOM   5763 C CB  . LEU B 1 200 ? -46.369 37.649 24.994  1.00 23.72 ? 200 LEU B CB  1 
ATOM   5764 C CG  . LEU B 1 200 ? -45.393 38.802 24.755  1.00 20.96 ? 200 LEU B CG  1 
ATOM   5765 C CD1 . LEU B 1 200 ? -46.089 39.931 24.037  1.00 22.71 ? 200 LEU B CD1 1 
ATOM   5766 C CD2 . LEU B 1 200 ? -44.790 39.299 26.064  1.00 21.39 ? 200 LEU B CD2 1 
ATOM   5767 N N   . ILE B 1 201 ? -46.425 34.506 26.891  1.00 15.26 ? 201 ILE B N   1 
ATOM   5768 C CA  . ILE B 1 201 ? -47.327 33.437 27.336  1.00 17.68 ? 201 ILE B CA  1 
ATOM   5769 C C   . ILE B 1 201 ? -48.705 33.952 27.726  1.00 18.54 ? 201 ILE B C   1 
ATOM   5770 O O   . ILE B 1 201 ? -49.707 33.299 27.382  1.00 17.20 ? 201 ILE B O   1 
ATOM   5771 C CB  . ILE B 1 201 ? -46.662 32.621 28.455  1.00 17.55 ? 201 ILE B CB  1 
ATOM   5772 C CG1 . ILE B 1 201 ? -45.415 31.891 27.931  1.00 16.31 ? 201 ILE B CG1 1 
ATOM   5773 C CG2 . ILE B 1 201 ? -47.687 31.668 29.114  1.00 15.65 ? 201 ILE B CG2 1 
ATOM   5774 C CD1 . ILE B 1 201 ? -45.706 30.757 26.937  1.00 16.89 ? 201 ILE B CD1 1 
ATOM   5775 N N   . PRO B 1 202 ? -48.855 35.062 28.457  1.00 16.15 ? 202 PRO B N   1 
ATOM   5776 C CA  . PRO B 1 202 ? -50.223 35.456 28.836  1.00 15.19 ? 202 PRO B CA  1 
ATOM   5777 C C   . PRO B 1 202 ? -51.123 35.734 27.644  1.00 16.48 ? 202 PRO B C   1 
ATOM   5778 O O   . PRO B 1 202 ? -52.323 35.434 27.711  1.00 18.12 ? 202 PRO B O   1 
ATOM   5779 C CB  . PRO B 1 202 ? -50.002 36.702 29.704  1.00 15.51 ? 202 PRO B CB  1 
ATOM   5780 C CG  . PRO B 1 202 ? -48.640 36.469 30.317  1.00 17.08 ? 202 PRO B CG  1 
ATOM   5781 C CD  . PRO B 1 202 ? -47.846 35.842 29.199  1.00 15.62 ? 202 PRO B CD  1 
ATOM   5782 N N   . ILE B 1 203 ? -50.576 36.264 26.545  1.00 16.61 ? 203 ILE B N   1 
ATOM   5783 C CA  . ILE B 1 203 ? -51.389 36.500 25.353  1.00 18.94 ? 203 ILE B CA  1 
ATOM   5784 C C   . ILE B 1 203 ? -51.745 35.185 24.671  1.00 21.13 ? 203 ILE B C   1 
ATOM   5785 O O   . ILE B 1 203 ? -52.883 34.997 24.222  1.00 19.25 ? 203 ILE B O   1 
ATOM   5786 C CB  . ILE B 1 203 ? -50.674 37.466 24.395  1.00 20.75 ? 203 ILE B CB  1 
ATOM   5787 C CG1 . ILE B 1 203 ? -50.642 38.873 25.013  1.00 24.05 ? 203 ILE B CG1 1 
ATOM   5788 C CG2 . ILE B 1 203 ? -51.368 37.480 23.030  1.00 20.20 ? 203 ILE B CG2 1 
ATOM   5789 C CD1 . ILE B 1 203 ? -49.806 39.868 24.233  1.00 30.75 ? 203 ILE B CD1 1 
ATOM   5790 N N   . LEU B 1 204 ? -50.788 34.250 24.591  1.00 19.00 ? 204 LEU B N   1 
ATOM   5791 C CA  . LEU B 1 204 ? -51.079 32.956 23.974  1.00 22.18 ? 204 LEU B CA  1 
ATOM   5792 C C   . LEU B 1 204 ? -52.172 32.215 24.732  1.00 20.23 ? 204 LEU B C   1 
ATOM   5793 O O   . LEU B 1 204 ? -52.980 31.501 24.124  1.00 22.74 ? 204 LEU B O   1 
ATOM   5794 C CB  . LEU B 1 204 ? -49.812 32.097 23.901  1.00 18.26 ? 204 LEU B CB  1 
ATOM   5795 C CG  . LEU B 1 204 ? -48.616 32.586 23.071  1.00 16.38 ? 204 LEU B CG  1 
ATOM   5796 C CD1 . LEU B 1 204 ? -47.538 31.494 22.968  1.00 19.05 ? 204 LEU B CD1 1 
ATOM   5797 C CD2 . LEU B 1 204 ? -49.062 33.048 21.683  1.00 20.13 ? 204 LEU B CD2 1 
ATOM   5798 N N   . LEU B 1 205 ? -52.220 32.374 26.057  1.00 18.70 ? 205 LEU B N   1 
ATOM   5799 C CA  . LEU B 1 205 ? -53.231 31.679 26.847  1.00 20.12 ? 205 LEU B CA  1 
ATOM   5800 C C   . LEU B 1 205 ? -54.575 32.385 26.779  1.00 20.41 ? 205 LEU B C   1 
ATOM   5801 O O   . LEU B 1 205 ? -55.621 31.730 26.751  1.00 22.30 ? 205 LEU B O   1 
ATOM   5802 C CB  . LEU B 1 205 ? -52.776 31.562 28.302  1.00 18.77 ? 205 LEU B CB  1 
ATOM   5803 C CG  . LEU B 1 205 ? -51.639 30.577 28.583  1.00 18.22 ? 205 LEU B CG  1 
ATOM   5804 C CD1 . LEU B 1 205 ? -51.147 30.741 30.024  1.00 18.56 ? 205 LEU B CD1 1 
ATOM   5805 C CD2 . LEU B 1 205 ? -52.124 29.154 28.341  1.00 19.85 ? 205 LEU B CD2 1 
ATOM   5806 N N   . ASN B 1 206 ? -54.567 33.710 26.737  1.00 19.86 ? 206 ASN B N   1 
ATOM   5807 C CA  . ASN B 1 206 ? -55.802 34.477 26.797  1.00 20.89 ? 206 ASN B CA  1 
ATOM   5808 C C   . ASN B 1 206 ? -55.528 35.901 26.336  1.00 23.26 ? 206 ASN B C   1 
ATOM   5809 O O   . ASN B 1 206 ? -55.162 36.755 27.153  1.00 21.52 ? 206 ASN B O   1 
ATOM   5810 C CB  . ASN B 1 206 ? -56.374 34.481 28.220  1.00 24.88 ? 206 ASN B CB  1 
ATOM   5811 C CG  . ASN B 1 206 ? -57.742 35.138 28.299  1.00 35.38 ? 206 ASN B CG  1 
ATOM   5812 O OD1 . ASN B 1 206 ? -58.249 35.683 27.314  1.00 33.20 ? 206 ASN B OD1 1 
ATOM   5813 N ND2 . ASN B 1 206 ? -58.342 35.098 29.481  1.00 41.39 ? 206 ASN B ND2 1 
ATOM   5814 N N   . PRO B 1 207 ? -55.715 36.201 25.048  1.00 22.93 ? 207 PRO B N   1 
ATOM   5815 C CA  . PRO B 1 207 ? -55.428 37.561 24.563  1.00 21.88 ? 207 PRO B CA  1 
ATOM   5816 C C   . PRO B 1 207 ? -56.261 38.635 25.240  1.00 23.27 ? 207 PRO B C   1 
ATOM   5817 O O   . PRO B 1 207 ? -55.861 39.804 25.230  1.00 23.22 ? 207 PRO B O   1 
ATOM   5818 C CB  . PRO B 1 207 ? -55.732 37.475 23.059  1.00 24.96 ? 207 PRO B CB  1 
ATOM   5819 C CG  . PRO B 1 207 ? -55.710 36.016 22.735  1.00 25.48 ? 207 PRO B CG  1 
ATOM   5820 C CD  . PRO B 1 207 ? -56.127 35.288 23.969  1.00 22.78 ? 207 PRO B CD  1 
ATOM   5821 N N   . ASN B 1 208 ? -57.402 38.281 25.838  1.00 22.72 ? 208 ASN B N   1 
ATOM   5822 C CA  . ASN B 1 208 ? -58.187 39.270 26.564  1.00 26.22 ? 208 ASN B CA  1 
ATOM   5823 C C   . ASN B 1 208 ? -57.455 39.833 27.781  1.00 27.39 ? 208 ASN B C   1 
ATOM   5824 O O   . ASN B 1 208 ? -57.883 40.862 28.315  1.00 25.91 ? 208 ASN B O   1 
ATOM   5825 C CB  . ASN B 1 208 ? -59.517 38.656 26.993  1.00 29.51 ? 208 ASN B CB  1 
ATOM   5826 C CG  . ASN B 1 208 ? -60.414 38.354 25.816  1.00 34.33 ? 208 ASN B CG  1 
ATOM   5827 O OD1 . ASN B 1 208 ? -60.605 39.197 24.944  1.00 29.61 ? 208 ASN B OD1 1 
ATOM   5828 N ND2 . ASN B 1 208 ? -60.951 37.143 25.771  1.00 41.18 ? 208 ASN B ND2 1 
ATOM   5829 N N   . CYS B 1 209 ? -56.366 39.199 28.229  1.00 21.66 ? 209 CYS B N   1 
ATOM   5830 C CA  . CYS B 1 209 ? -55.645 39.723 29.386  1.00 24.43 ? 209 CYS B CA  1 
ATOM   5831 C C   . CYS B 1 209 ? -55.080 41.118 29.139  1.00 25.22 ? 209 CYS B C   1 
ATOM   5832 O O   . CYS B 1 209 ? -54.752 41.815 30.106  1.00 23.22 ? 209 CYS B O   1 
ATOM   5833 C CB  . CYS B 1 209 ? -54.523 38.763 29.804  1.00 22.54 ? 209 CYS B CB  1 
ATOM   5834 S SG  . CYS B 1 209 ? -53.083 38.684 28.714  1.00 24.98 ? 209 CYS B SG  1 
ATOM   5835 N N   . VAL B 1 210 ? -54.978 41.552 27.877  1.00 26.07 ? 210 VAL B N   1 
ATOM   5836 C CA  . VAL B 1 210 ? -54.467 42.893 27.593  1.00 19.42 ? 210 VAL B CA  1 
ATOM   5837 C C   . VAL B 1 210 ? -55.400 43.957 28.150  1.00 20.67 ? 210 VAL B C   1 
ATOM   5838 O O   . VAL B 1 210 ? -54.967 45.071 28.464  1.00 23.85 ? 210 VAL B O   1 
ATOM   5839 C CB  . VAL B 1 210 ? -54.245 43.092 26.078  1.00 23.15 ? 210 VAL B CB  1 
ATOM   5840 C CG1 . VAL B 1 210 ? -53.302 42.030 25.538  1.00 23.09 ? 210 VAL B CG1 1 
ATOM   5841 C CG2 . VAL B 1 210 ? -55.567 43.059 25.324  1.00 29.30 ? 210 VAL B CG2 1 
ATOM   5842 N N   . TYR B 1 211 ? -56.692 43.647 28.278  1.00 21.88 ? 211 TYR B N   1 
ATOM   5843 C CA  . TYR B 1 211 ? -57.631 44.636 28.780  1.00 25.40 ? 211 TYR B CA  1 
ATOM   5844 C C   . TYR B 1 211 ? -57.460 44.896 30.271  1.00 26.73 ? 211 TYR B C   1 
ATOM   5845 O O   . TYR B 1 211 ? -58.011 45.878 30.774  1.00 26.31 ? 211 TYR B O   1 
ATOM   5846 C CB  . TYR B 1 211 ? -59.067 44.191 28.477  1.00 25.22 ? 211 TYR B CB  1 
ATOM   5847 C CG  . TYR B 1 211 ? -59.330 43.947 26.999  1.00 25.10 ? 211 TYR B CG  1 
ATOM   5848 C CD1 . TYR B 1 211 ? -59.145 44.958 26.067  1.00 30.39 ? 211 TYR B CD1 1 
ATOM   5849 C CD2 . TYR B 1 211 ? -59.781 42.711 26.544  1.00 26.01 ? 211 TYR B CD2 1 
ATOM   5850 C CE1 . TYR B 1 211 ? -59.395 44.745 24.713  1.00 31.98 ? 211 TYR B CE1 1 
ATOM   5851 C CE2 . TYR B 1 211 ? -60.034 42.488 25.191  1.00 25.85 ? 211 TYR B CE2 1 
ATOM   5852 C CZ  . TYR B 1 211 ? -59.833 43.508 24.285  1.00 29.76 ? 211 TYR B CZ  1 
ATOM   5853 O OH  . TYR B 1 211 ? -60.070 43.294 22.944  1.00 35.71 ? 211 TYR B OH  1 
ATOM   5854 N N   . GLU B 1 212 ? -56.699 44.061 30.984  1.00 24.52 ? 212 GLU B N   1 
ATOM   5855 C CA  . GLU B 1 212 ? -56.545 44.282 32.418  1.00 27.34 ? 212 GLU B CA  1 
ATOM   5856 C C   . GLU B 1 212 ? -55.790 45.574 32.716  1.00 27.91 ? 212 GLU B C   1 
ATOM   5857 O O   . GLU B 1 212 ? -56.083 46.239 33.714  1.00 33.98 ? 212 GLU B O   1 
ATOM   5858 C CB  . GLU B 1 212 ? -55.845 43.087 33.063  1.00 23.06 ? 212 GLU B CB  1 
ATOM   5859 C CG  . GLU B 1 212 ? -56.710 41.837 33.117  1.00 25.22 ? 212 GLU B CG  1 
ATOM   5860 C CD  . GLU B 1 212 ? -55.947 40.628 33.621  1.00 35.90 ? 212 GLU B CD  1 
ATOM   5861 O OE1 . GLU B 1 212 ? -56.067 39.544 33.017  1.00 40.29 ? 212 GLU B OE1 1 
ATOM   5862 O OE2 . GLU B 1 212 ? -55.230 40.765 34.627  1.00 34.27 ? 212 GLU B OE2 1 
ATOM   5863 N N   . THR B 1 213 ? -54.835 45.950 31.865  1.00 26.73 ? 213 THR B N   1 
ATOM   5864 C CA  . THR B 1 213 ? -54.109 47.208 32.007  1.00 30.09 ? 213 THR B CA  1 
ATOM   5865 C C   . THR B 1 213 ? -54.459 48.246 30.953  1.00 32.96 ? 213 THR B C   1 
ATOM   5866 O O   . THR B 1 213 ? -54.387 49.441 31.244  1.00 36.99 ? 213 THR B O   1 
ATOM   5867 C CB  . THR B 1 213 ? -52.597 46.965 31.958  1.00 28.15 ? 213 THR B CB  1 
ATOM   5868 O OG1 . THR B 1 213 ? -52.268 46.238 30.766  1.00 31.38 ? 213 THR B OG1 1 
ATOM   5869 C CG2 . THR B 1 213 ? -52.152 46.201 33.179  1.00 23.31 ? 213 THR B CG2 1 
ATOM   5870 N N   . THR B 1 214 ? -54.823 47.831 29.739  1.00 25.75 ? 214 THR B N   1 
ATOM   5871 C CA  . THR B 1 214 ? -55.210 48.749 28.662  1.00 30.23 ? 214 THR B CA  1 
ATOM   5872 C C   . THR B 1 214 ? -56.583 48.350 28.141  1.00 35.09 ? 214 THR B C   1 
ATOM   5873 O O   . THR B 1 214 ? -56.707 47.743 27.066  1.00 32.32 ? 214 THR B O   1 
ATOM   5874 C CB  . THR B 1 214 ? -54.176 48.755 27.536  1.00 29.61 ? 214 THR B CB  1 
ATOM   5875 O OG1 . THR B 1 214 ? -54.005 47.424 27.038  1.00 27.39 ? 214 THR B OG1 1 
ATOM   5876 C CG2 . THR B 1 214 ? -52.834 49.265 28.050  1.00 31.78 ? 214 THR B CG2 1 
ATOM   5877 N N   . PRO B 1 215 ? -57.647 48.698 28.869  1.00 34.00 ? 215 PRO B N   1 
ATOM   5878 C CA  . PRO B 1 215 ? -58.988 48.217 28.492  1.00 31.41 ? 215 PRO B CA  1 
ATOM   5879 C C   . PRO B 1 215 ? -59.506 48.773 27.178  1.00 36.09 ? 215 PRO B C   1 
ATOM   5880 O O   . PRO B 1 215 ? -60.462 48.213 26.624  1.00 34.37 ? 215 PRO B O   1 
ATOM   5881 C CB  . PRO B 1 215 ? -59.864 48.672 29.667  1.00 32.76 ? 215 PRO B CB  1 
ATOM   5882 C CG  . PRO B 1 215 ? -59.139 49.849 30.238  1.00 35.92 ? 215 PRO B CG  1 
ATOM   5883 C CD  . PRO B 1 215 ? -57.675 49.559 30.064  1.00 31.41 ? 215 PRO B CD  1 
ATOM   5884 N N   . ASN B 1 216 ? -58.921 49.848 26.660  1.00 34.39 ? 216 ASN B N   1 
ATOM   5885 C CA  . ASN B 1 216 ? -59.394 50.460 25.427  1.00 37.66 ? 216 ASN B CA  1 
ATOM   5886 C C   . ASN B 1 216 ? -58.519 50.117 24.233  1.00 34.38 ? 216 ASN B C   1 
ATOM   5887 O O   . ASN B 1 216 ? -58.714 50.678 23.151  1.00 35.67 ? 216 ASN B O   1 
ATOM   5888 C CB  . ASN B 1 216 ? -59.481 51.976 25.589  1.00 46.38 ? 216 ASN B CB  1 
ATOM   5889 C CG  . ASN B 1 216 ? -60.496 52.388 26.624  1.00 48.11 ? 216 ASN B CG  1 
ATOM   5890 O OD1 . ASN B 1 216 ? -60.199 53.185 27.511  1.00 52.44 ? 216 ASN B OD1 1 
ATOM   5891 N ND2 . ASN B 1 216 ? -61.702 51.838 26.526  1.00 51.27 ? 216 ASN B ND2 1 
ATOM   5892 N N   . VAL B 1 217 ? -57.559 49.206 24.404  1.00 32.04 ? 217 VAL B N   1 
ATOM   5893 C CA  . VAL B 1 217 ? -56.699 48.832 23.293  1.00 31.22 ? 217 VAL B CA  1 
ATOM   5894 C C   . VAL B 1 217 ? -57.525 48.095 22.245  1.00 31.92 ? 217 VAL B C   1 
ATOM   5895 O O   . VAL B 1 217 ? -58.512 47.414 22.558  1.00 33.21 ? 217 VAL B O   1 
ATOM   5896 C CB  . VAL B 1 217 ? -55.516 47.979 23.795  1.00 28.04 ? 217 VAL B CB  1 
ATOM   5897 C CG1 . VAL B 1 217 ? -55.970 46.584 24.187  1.00 30.03 ? 217 VAL B CG1 1 
ATOM   5898 C CG2 . VAL B 1 217 ? -54.422 47.908 22.751  1.00 31.26 ? 217 VAL B CG2 1 
ATOM   5899 N N   . LYS B 1 218 ? -57.143 48.253 20.984  1.00 27.72 ? 218 LYS B N   1 
ATOM   5900 C CA  . LYS B 1 218 ? -57.737 47.498 19.891  1.00 27.21 ? 218 LYS B CA  1 
ATOM   5901 C C   . LYS B 1 218 ? -56.757 46.417 19.450  1.00 33.47 ? 218 LYS B C   1 
ATOM   5902 O O   . LYS B 1 218 ? -55.612 46.717 19.093  1.00 31.63 ? 218 LYS B O   1 
ATOM   5903 C CB  . LYS B 1 218 ? -58.106 48.420 18.733  1.00 30.43 ? 218 LYS B CB  1 
ATOM   5904 C CG  . LYS B 1 218 ? -59.139 49.463 19.122  1.00 36.24 ? 218 LYS B CG  1 
ATOM   5905 C CD  . LYS B 1 218 ? -59.550 50.294 17.934  1.00 44.77 ? 218 LYS B CD  1 
ATOM   5906 C CE  . LYS B 1 218 ? -60.484 51.400 18.353  1.00 49.00 ? 218 LYS B CE  1 
ATOM   5907 N NZ  . LYS B 1 218 ? -60.978 52.125 17.159  1.00 56.12 ? 218 LYS B NZ  1 
ATOM   5908 N N   . ILE B 1 219 ? -57.192 45.163 19.516  1.00 27.53 ? 219 ILE B N   1 
ATOM   5909 C CA  . ILE B 1 219 ? -56.367 44.045 19.071  1.00 28.91 ? 219 ILE B CA  1 
ATOM   5910 C C   . ILE B 1 219 ? -57.142 43.251 18.029  1.00 33.89 ? 219 ILE B C   1 
ATOM   5911 O O   . ILE B 1 219 ? -58.357 43.454 17.873  1.00 34.53 ? 219 ILE B O   1 
ATOM   5912 C CB  . ILE B 1 219 ? -55.939 43.156 20.251  1.00 30.20 ? 219 ILE B CB  1 
ATOM   5913 C CG1 . ILE B 1 219 ? -57.128 42.350 20.778  1.00 33.66 ? 219 ILE B CG1 1 
ATOM   5914 C CG2 . ILE B 1 219 ? -55.310 43.997 21.355  1.00 32.44 ? 219 ILE B CG2 1 
ATOM   5915 C CD1 . ILE B 1 219 ? -56.753 41.367 21.874  1.00 36.49 ? 219 ILE B CD1 1 
ATOM   5916 N N   . PRO B 1 220 ? -56.492 42.369 17.275  1.00 29.68 ? 220 PRO B N   1 
ATOM   5917 C CA  . PRO B 1 220 ? -57.224 41.580 16.277  1.00 30.95 ? 220 PRO B CA  1 
ATOM   5918 C C   . PRO B 1 220 ? -58.136 40.547 16.924  1.00 29.90 ? 220 PRO B C   1 
ATOM   5919 O O   . PRO B 1 220 ? -58.154 40.339 18.142  1.00 30.94 ? 220 PRO B O   1 
ATOM   5920 C CB  . PRO B 1 220 ? -56.117 40.906 15.455  1.00 34.62 ? 220 PRO B CB  1 
ATOM   5921 C CG  . PRO B 1 220 ? -54.877 41.052 16.227  1.00 33.52 ? 220 PRO B CG  1 
ATOM   5922 C CD  . PRO B 1 220 ? -55.034 42.272 17.088  1.00 31.18 ? 220 PRO B CD  1 
ATOM   5923 N N   . ASP B 1 221 ? -58.898 39.885 16.058  1.00 30.47 ? 221 ASP B N   1 
ATOM   5924 C CA  . ASP B 1 221 ? -59.791 38.801 16.450  1.00 38.20 ? 221 ASP B CA  1 
ATOM   5925 C C   . ASP B 1 221 ? -58.985 37.510 16.528  1.00 31.58 ? 221 ASP B C   1 
ATOM   5926 O O   . ASP B 1 221 ? -58.585 36.955 15.500  1.00 32.68 ? 221 ASP B O   1 
ATOM   5927 C CB  . ASP B 1 221 ? -60.940 38.690 15.447  1.00 41.41 ? 221 ASP B CB  1 
ATOM   5928 C CG  . ASP B 1 221 ? -61.951 37.611 15.810  1.00 50.62 ? 221 ASP B CG  1 
ATOM   5929 O OD1 . ASP B 1 221 ? -61.553 36.509 16.241  1.00 54.73 ? 221 ASP B OD1 1 
ATOM   5930 O OD2 . ASP B 1 221 ? -63.161 37.861 15.641  1.00 52.82 ? 221 ASP B OD2 1 
ATOM   5931 N N   . PHE B 1 222 ? -58.755 37.023 17.746  1.00 27.74 ? 222 PHE B N   1 
ATOM   5932 C CA  . PHE B 1 222 ? -58.045 35.763 17.956  1.00 28.25 ? 222 PHE B CA  1 
ATOM   5933 C C   . PHE B 1 222 ? -59.051 34.624 17.821  1.00 33.77 ? 222 PHE B C   1 
ATOM   5934 O O   . PHE B 1 222 ? -59.589 34.101 18.801  1.00 42.81 ? 222 PHE B O   1 
ATOM   5935 C CB  . PHE B 1 222 ? -57.361 35.745 19.316  1.00 28.92 ? 222 PHE B CB  1 
ATOM   5936 C CG  . PHE B 1 222 ? -56.081 36.521 19.367  1.00 28.08 ? 222 PHE B CG  1 
ATOM   5937 C CD1 . PHE B 1 222 ? -56.094 37.908 19.451  1.00 26.10 ? 222 PHE B CD1 1 
ATOM   5938 C CD2 . PHE B 1 222 ? -54.862 35.863 19.360  1.00 23.68 ? 222 PHE B CD2 1 
ATOM   5939 C CE1 . PHE B 1 222 ? -54.906 38.625 19.509  1.00 23.88 ? 222 PHE B CE1 1 
ATOM   5940 C CE2 . PHE B 1 222 ? -53.676 36.569 19.420  1.00 23.65 ? 222 PHE B CE2 1 
ATOM   5941 C CZ  . PHE B 1 222 ? -53.699 37.952 19.495  1.00 23.69 ? 222 PHE B CZ  1 
ATOM   5942 N N   . ALA B 1 223 ? -59.309 34.239 16.575  1.00 37.04 ? 223 ALA B N   1 
ATOM   5943 C CA  . ALA B 1 223 ? -60.283 33.197 16.273  1.00 43.17 ? 223 ALA B CA  1 
ATOM   5944 C C   . ALA B 1 223 ? -59.667 31.805 16.250  1.00 44.17 ? 223 ALA B C   1 
ATOM   5945 O O   . ALA B 1 223 ? -60.301 30.865 15.759  1.00 43.06 ? 223 ALA B O   1 
ATOM   5946 C CB  . ALA B 1 223 ? -60.972 33.486 14.937  1.00 47.78 ? 223 ALA B CB  1 
ATOM   5947 N N   . VAL B 1 224 ? -58.445 31.657 16.752  1.00 39.73 ? 224 VAL B N   1 
ATOM   5948 C CA  . VAL B 1 224 ? -57.807 30.358 16.909  1.00 36.44 ? 224 VAL B CA  1 
ATOM   5949 C C   . VAL B 1 224 ? -57.171 30.336 18.291  1.00 34.07 ? 224 VAL B C   1 
ATOM   5950 O O   . VAL B 1 224 ? -56.823 31.381 18.847  1.00 31.62 ? 224 VAL B O   1 
ATOM   5951 C CB  . VAL B 1 224 ? -56.769 30.090 15.793  1.00 44.05 ? 224 VAL B CB  1 
ATOM   5952 C CG1 . VAL B 1 224 ? -55.524 30.933 16.000  1.00 46.06 ? 224 VAL B CG1 1 
ATOM   5953 C CG2 . VAL B 1 224 ? -56.423 28.607 15.716  1.00 44.62 ? 224 VAL B CG2 1 
ATOM   5954 N N   . SER B 1 225 ? -57.042 29.141 18.862  1.00 34.62 ? 225 SER B N   1 
ATOM   5955 C CA  . SER B 1 225 ? -56.485 29.002 20.202  1.00 32.75 ? 225 SER B CA  1 
ATOM   5956 C C   . SER B 1 225 ? -54.973 28.831 20.145  1.00 25.77 ? 225 SER B C   1 
ATOM   5957 O O   . SER B 1 225 ? -54.460 28.036 19.351  1.00 29.96 ? 225 SER B O   1 
ATOM   5958 C CB  . SER B 1 225 ? -57.110 27.814 20.933  1.00 32.24 ? 225 SER B CB  1 
ATOM   5959 O OG  . SER B 1 225 ? -56.425 27.591 22.155  1.00 32.13 ? 225 SER B OG  1 
ATOM   5960 N N   . PHE B 1 226 ? -54.262 29.569 21.000  1.00 23.97 ? 226 PHE B N   1 
ATOM   5961 C CA  . PHE B 1 226 ? -52.820 29.424 21.152  1.00 22.56 ? 226 PHE B CA  1 
ATOM   5962 C C   . PHE B 1 226 ? -52.458 28.759 22.474  1.00 21.99 ? 226 PHE B C   1 
ATOM   5963 O O   . PHE B 1 226 ? -51.282 28.721 22.838  1.00 21.68 ? 226 PHE B O   1 
ATOM   5964 C CB  . PHE B 1 226 ? -52.122 30.789 21.038  1.00 21.10 ? 226 PHE B CB  1 
ATOM   5965 C CG  . PHE B 1 226 ? -52.080 31.347 19.627  1.00 21.60 ? 226 PHE B CG  1 
ATOM   5966 C CD1 . PHE B 1 226 ? -51.108 30.930 18.728  1.00 26.36 ? 226 PHE B CD1 1 
ATOM   5967 C CD2 . PHE B 1 226 ? -52.992 32.310 19.218  1.00 30.25 ? 226 PHE B CD2 1 
ATOM   5968 C CE1 . PHE B 1 226 ? -51.053 31.448 17.436  1.00 30.00 ? 226 PHE B CE1 1 
ATOM   5969 C CE2 . PHE B 1 226 ? -52.949 32.829 17.928  1.00 31.75 ? 226 PHE B CE2 1 
ATOM   5970 C CZ  . PHE B 1 226 ? -51.979 32.397 17.036  1.00 30.94 ? 226 PHE B CZ  1 
ATOM   5971 N N   . ARG B 1 227 ? -53.444 28.217 23.195  1.00 26.43 ? 227 ARG B N   1 
ATOM   5972 C CA  . ARG B 1 227 ? -53.176 27.709 24.538  1.00 22.60 ? 227 ARG B CA  1 
ATOM   5973 C C   . ARG B 1 227 ? -52.268 26.490 24.506  1.00 24.92 ? 227 ARG B C   1 
ATOM   5974 O O   . ARG B 1 227 ? -51.366 26.364 25.343  1.00 25.97 ? 227 ARG B O   1 
ATOM   5975 C CB  . ARG B 1 227 ? -54.493 27.382 25.246  1.00 23.97 ? 227 ARG B CB  1 
ATOM   5976 C CG  . ARG B 1 227 ? -55.365 28.615 25.475  1.00 27.96 ? 227 ARG B CG  1 
ATOM   5977 C CD  . ARG B 1 227 ? -56.680 28.252 26.148  1.00 30.38 ? 227 ARG B CD  1 
ATOM   5978 N NE  . ARG B 1 227 ? -56.448 27.625 27.444  1.00 38.47 ? 227 ARG B NE  1 
ATOM   5979 C CZ  . ARG B 1 227 ? -56.261 28.298 28.572  1.00 41.33 ? 227 ARG B CZ  1 
ATOM   5980 N NH1 . ARG B 1 227 ? -56.288 29.623 28.566  1.00 37.64 ? 227 ARG B NH1 1 
ATOM   5981 N NH2 . ARG B 1 227 ? -56.052 27.644 29.707  1.00 46.68 ? 227 ARG B NH2 1 
ATOM   5982 N N   . GLU B 1 228 ? -52.486 25.582 23.552  1.00 24.21 ? 228 GLU B N   1 
ATOM   5983 C CA  . GLU B 1 228 ? -51.611 24.422 23.452  1.00 24.60 ? 228 GLU B CA  1 
ATOM   5984 C C   . GLU B 1 228 ? -50.186 24.844 23.124  1.00 25.63 ? 228 GLU B C   1 
ATOM   5985 O O   . GLU B 1 228 ? -49.227 24.294 23.679  1.00 24.71 ? 228 GLU B O   1 
ATOM   5986 C CB  . GLU B 1 228 ? -52.139 23.443 22.404  1.00 32.27 ? 228 GLU B CB  1 
ATOM   5987 C CG  . GLU B 1 228 ? -51.285 22.191 22.250  1.00 44.88 ? 228 GLU B CG  1 
ATOM   5988 C CD  . GLU B 1 228 ? -50.937 21.543 23.581  1.00 59.62 ? 228 GLU B CD  1 
ATOM   5989 O OE1 . GLU B 1 228 ? -49.732 21.344 23.855  1.00 63.41 ? 228 GLU B OE1 1 
ATOM   5990 O OE2 . GLU B 1 228 ? -51.869 21.234 24.354  1.00 66.66 ? 228 GLU B OE2 1 
ATOM   5991 N N   . ASP B 1 229 ? -50.029 25.829 22.234  1.00 22.43 ? 229 ASP B N   1 
ATOM   5992 C CA  . ASP B 1 229 ? -48.694 26.323 21.903  1.00 21.11 ? 229 ASP B CA  1 
ATOM   5993 C C   . ASP B 1 229 ? -47.981 26.884 23.128  1.00 21.63 ? 229 ASP B C   1 
ATOM   5994 O O   . ASP B 1 229 ? -46.764 26.717 23.277  1.00 20.37 ? 229 ASP B O   1 
ATOM   5995 C CB  . ASP B 1 229 ? -48.791 27.379 20.806  1.00 21.38 ? 229 ASP B CB  1 
ATOM   5996 C CG  . ASP B 1 229 ? -48.988 26.764 19.436  1.00 27.04 ? 229 ASP B CG  1 
ATOM   5997 O OD1 . ASP B 1 229 ? -48.984 25.514 19.336  1.00 26.04 ? 229 ASP B OD1 1 
ATOM   5998 O OD2 . ASP B 1 229 ? -49.139 27.522 18.461  1.00 27.04 ? 229 ASP B OD2 1 
ATOM   5999 N N   . ALA B 1 230 ? -48.713 27.568 24.009  1.00 24.12 ? 230 ALA B N   1 
ATOM   6000 C CA  . ALA B 1 230 ? -48.093 28.084 25.227  1.00 22.00 ? 230 ALA B CA  1 
ATOM   6001 C C   . ALA B 1 230 ? -47.520 26.951 26.071  1.00 22.21 ? 230 ALA B C   1 
ATOM   6002 O O   . ALA B 1 230 ? -46.395 27.049 26.583  1.00 19.86 ? 230 ALA B O   1 
ATOM   6003 C CB  . ALA B 1 230 ? -49.109 28.897 26.032  1.00 20.63 ? 230 ALA B CB  1 
ATOM   6004 N N   . SER B 1 231 ? -48.285 25.868 26.231  1.00 21.41 ? 231 SER B N   1 
ATOM   6005 C CA  . SER B 1 231 ? -47.763 24.698 26.926  1.00 19.92 ? 231 SER B CA  1 
ATOM   6006 C C   . SER B 1 231 ? -46.531 24.143 26.226  1.00 19.83 ? 231 SER B C   1 
ATOM   6007 O O   . SER B 1 231 ? -45.550 23.778 26.884  1.00 25.01 ? 231 SER B O   1 
ATOM   6008 C CB  . SER B 1 231 ? -48.841 23.614 27.021  1.00 25.00 ? 231 SER B CB  1 
ATOM   6009 O OG  . SER B 1 231 ? -49.629 23.785 28.177  1.00 37.56 ? 231 SER B OG  1 
ATOM   6010 N N   . LYS B 1 232 ? -46.577 24.048 24.889  1.00 20.91 ? 232 LYS B N   1 
ATOM   6011 C CA  . LYS B 1 232 ? -45.456 23.496 24.131  1.00 20.61 ? 232 LYS B CA  1 
ATOM   6012 C C   . LYS B 1 232 ? -44.187 24.318 24.342  1.00 21.72 ? 232 LYS B C   1 
ATOM   6013 O O   . LYS B 1 232 ? -43.095 23.753 24.496  1.00 23.40 ? 232 LYS B O   1 
ATOM   6014 C CB  . LYS B 1 232 ? -45.800 23.434 22.635  1.00 23.07 ? 232 LYS B CB  1 
ATOM   6015 C CG  . LYS B 1 232 ? -46.574 22.208 22.181  1.00 36.86 ? 232 LYS B CG  1 
ATOM   6016 C CD  . LYS B 1 232 ? -46.871 22.307 20.682  1.00 32.98 ? 232 LYS B CD  1 
ATOM   6017 C CE  . LYS B 1 232 ? -47.148 20.949 20.048  1.00 50.00 ? 232 LYS B CE  1 
ATOM   6018 N NZ  . LYS B 1 232 ? -48.434 20.353 20.498  1.00 60.51 ? 232 LYS B NZ  1 
ATOM   6019 N N   . HIS B 1 233 ? -44.305 25.652 24.334  1.00 17.79 ? 233 HIS B N   1 
ATOM   6020 C CA  . HIS B 1 233 ? -43.136 26.489 24.593  1.00 16.41 ? 233 HIS B CA  1 
ATOM   6021 C C   . HIS B 1 233 ? -42.493 26.115 25.919  1.00 19.86 ? 233 HIS B C   1 
ATOM   6022 O O   . HIS B 1 233 ? -41.263 26.021 26.023  1.00 17.34 ? 233 HIS B O   1 
ATOM   6023 C CB  . HIS B 1 233 ? -43.512 27.975 24.612  1.00 17.18 ? 233 HIS B CB  1 
ATOM   6024 C CG  . HIS B 1 233 ? -43.653 28.598 23.256  1.00 18.29 ? 233 HIS B CG  1 
ATOM   6025 N ND1 . HIS B 1 233 ? -42.577 29.062 22.529  1.00 19.96 ? 233 HIS B ND1 1 
ATOM   6026 C CD2 . HIS B 1 233 ? -44.752 28.854 22.506  1.00 17.33 ? 233 HIS B CD2 1 
ATOM   6027 C CE1 . HIS B 1 233 ? -43.005 29.579 21.391  1.00 20.20 ? 233 HIS B CE1 1 
ATOM   6028 N NE2 . HIS B 1 233 ? -44.321 29.462 21.351  1.00 19.39 ? 233 HIS B NE2 1 
ATOM   6029 N N   . VAL B 1 234 ? -43.314 25.907 26.949  1.00 19.13 ? 234 VAL B N   1 
ATOM   6030 C CA  . VAL B 1 234 ? -42.767 25.612 28.270  1.00 20.04 ? 234 VAL B CA  1 
ATOM   6031 C C   . VAL B 1 234 ? -42.190 24.206 28.304  1.00 21.88 ? 234 VAL B C   1 
ATOM   6032 O O   . VAL B 1 234 ? -41.079 23.983 28.805  1.00 19.69 ? 234 VAL B O   1 
ATOM   6033 C CB  . VAL B 1 234 ? -43.844 25.814 29.352  1.00 20.74 ? 234 VAL B CB  1 
ATOM   6034 C CG1 . VAL B 1 234 ? -43.292 25.456 30.721  1.00 17.72 ? 234 VAL B CG1 1 
ATOM   6035 C CG2 . VAL B 1 234 ? -44.353 27.254 29.348  1.00 18.40 ? 234 VAL B CG2 1 
ATOM   6036 N N   . GLU B 1 235 ? -42.922 23.237 27.751  1.00 18.36 ? 235 GLU B N   1 
ATOM   6037 C CA  . GLU B 1 235 ? -42.472 21.853 27.805  1.00 19.78 ? 235 GLU B CA  1 
ATOM   6038 C C   . GLU B 1 235 ? -41.192 21.655 26.996  1.00 20.30 ? 235 GLU B C   1 
ATOM   6039 O O   . GLU B 1 235 ? -40.254 20.994 27.463  1.00 20.59 ? 235 GLU B O   1 
ATOM   6040 C CB  . GLU B 1 235 ? -43.592 20.929 27.318  1.00 24.91 ? 235 GLU B CB  1 
ATOM   6041 C CG  . GLU B 1 235 ? -43.304 19.442 27.479  1.00 39.43 ? 235 GLU B CG  1 
ATOM   6042 C CD  . GLU B 1 235 ? -42.968 19.060 28.912  1.00 46.86 ? 235 GLU B CD  1 
ATOM   6043 O OE1 . GLU B 1 235 ? -43.545 19.660 29.847  1.00 45.27 ? 235 GLU B OE1 1 
ATOM   6044 O OE2 . GLU B 1 235 ? -42.123 18.157 29.100  1.00 48.78 ? 235 GLU B OE2 1 
ATOM   6045 N N   . LEU B 1 236 ? -41.121 22.245 25.796  1.00 21.71 ? 236 LEU B N   1 
ATOM   6046 C CA  . LEU B 1 236 ? -39.927 22.080 24.969  1.00 22.59 ? 236 LEU B CA  1 
ATOM   6047 C C   . LEU B 1 236 ? -38.710 22.753 25.589  1.00 19.34 ? 236 LEU B C   1 
ATOM   6048 O O   . LEU B 1 236 ? -37.584 22.259 25.431  1.00 18.53 ? 236 LEU B O   1 
ATOM   6049 C CB  . LEU B 1 236 ? -40.171 22.634 23.565  1.00 19.45 ? 236 LEU B CB  1 
ATOM   6050 C CG  . LEU B 1 236 ? -41.190 21.837 22.739  1.00 21.11 ? 236 LEU B CG  1 
ATOM   6051 C CD1 . LEU B 1 236 ? -41.576 22.641 21.493  1.00 26.27 ? 236 LEU B CD1 1 
ATOM   6052 C CD2 . LEU B 1 236 ? -40.662 20.457 22.361  1.00 28.16 ? 236 LEU B CD2 1 
ATOM   6053 N N   . ALA B 1 237 ? -38.919 23.874 26.282  1.00 16.76 ? 237 ALA B N   1 
ATOM   6054 C CA  . ALA B 1 237 ? -37.838 24.524 27.015  1.00 16.51 ? 237 ALA B CA  1 
ATOM   6055 C C   . ALA B 1 237 ? -37.307 23.624 28.116  1.00 19.41 ? 237 ALA B C   1 
ATOM   6056 O O   . ALA B 1 237 ? -36.089 23.536 28.322  1.00 18.06 ? 237 ALA B O   1 
ATOM   6057 C CB  . ALA B 1 237 ? -38.322 25.844 27.614  1.00 18.14 ? 237 ALA B CB  1 
ATOM   6058 N N   . LYS B 1 238 ? -38.210 22.956 28.844  1.00 17.85 ? 238 LYS B N   1 
ATOM   6059 C CA  . LYS B 1 238 ? -37.781 22.010 29.867  1.00 23.60 ? 238 LYS B CA  1 
ATOM   6060 C C   . LYS B 1 238 ? -36.904 20.923 29.263  1.00 19.49 ? 238 LYS B C   1 
ATOM   6061 O O   . LYS B 1 238 ? -35.859 20.571 29.827  1.00 22.21 ? 238 LYS B O   1 
ATOM   6062 C CB  . LYS B 1 238 ? -38.999 21.399 30.567  1.00 21.54 ? 238 LYS B CB  1 
ATOM   6063 C CG  . LYS B 1 238 ? -39.713 22.373 31.500  1.00 24.01 ? 238 LYS B CG  1 
ATOM   6064 C CD  . LYS B 1 238 ? -41.023 21.802 32.019  1.00 25.48 ? 238 LYS B CD  1 
ATOM   6065 C CE  . LYS B 1 238 ? -40.817 20.527 32.823  1.00 29.18 ? 238 LYS B CE  1 
ATOM   6066 N NZ  . LYS B 1 238 ? -42.126 19.867 33.098  1.00 33.89 ? 238 LYS B NZ  1 
ATOM   6067 N N   . GLU B 1 239 ? -37.290 20.414 28.089  1.00 21.27 ? 239 GLU B N   1 
ATOM   6068 C CA  . GLU B 1 239 ? -36.515 19.366 27.433  1.00 23.58 ? 239 GLU B CA  1 
ATOM   6069 C C   . GLU B 1 239 ? -35.154 19.881 26.972  1.00 23.95 ? 239 GLU B C   1 
ATOM   6070 O O   . GLU B 1 239 ? -34.141 19.187 27.131  1.00 26.25 ? 239 GLU B O   1 
ATOM   6071 C CB  . GLU B 1 239 ? -37.305 18.797 26.255  1.00 26.06 ? 239 GLU B CB  1 
ATOM   6072 C CG  . GLU B 1 239 ? -38.657 18.200 26.652  1.00 41.42 ? 239 GLU B CG  1 
ATOM   6073 C CD  . GLU B 1 239 ? -39.483 17.744 25.458  1.00 57.22 ? 239 GLU B CD  1 
ATOM   6074 O OE1 . GLU B 1 239 ? -40.648 17.339 25.667  1.00 60.83 ? 239 GLU B OE1 1 
ATOM   6075 O OE2 . GLU B 1 239 ? -38.971 17.789 24.315  1.00 59.97 ? 239 GLU B OE2 1 
ATOM   6076 N N   . LYS B 1 240 ? -35.108 21.085 26.391  1.00 22.58 ? 240 LYS B N   1 
ATOM   6077 C CA  . LYS B 1 240 ? -33.833 21.618 25.918  1.00 25.47 ? 240 LYS B CA  1 
ATOM   6078 C C   . LYS B 1 240 ? -32.881 21.894 27.076  1.00 21.60 ? 240 LYS B C   1 
ATOM   6079 O O   . LYS B 1 240 ? -31.686 21.584 26.994  1.00 22.80 ? 240 LYS B O   1 
ATOM   6080 C CB  . LYS B 1 240 ? -34.053 22.891 25.101  1.00 22.95 ? 240 LYS B CB  1 
ATOM   6081 C CG  . LYS B 1 240 ? -32.771 23.450 24.506  1.00 28.73 ? 240 LYS B CG  1 
ATOM   6082 C CD  . LYS B 1 240 ? -32.290 22.575 23.361  1.00 27.50 ? 240 LYS B CD  1 
ATOM   6083 C CE  . LYS B 1 240 ? -30.863 22.894 22.950  1.00 26.22 ? 240 LYS B CE  1 
ATOM   6084 N NZ  . LYS B 1 240 ? -30.518 22.170 21.688  1.00 27.89 ? 240 LYS B NZ  1 
ATOM   6085 N N   . TYR B 1 241 ? -33.389 22.491 28.152  1.00 22.25 ? 241 TYR B N   1 
ATOM   6086 C CA  . TYR B 1 241 ? -32.568 22.699 29.341  1.00 21.04 ? 241 TYR B CA  1 
ATOM   6087 C C   . TYR B 1 241 ? -32.032 21.373 29.874  1.00 25.08 ? 241 TYR B C   1 
ATOM   6088 O O   . TYR B 1 241 ? -30.852 21.266 30.235  1.00 20.74 ? 241 TYR B O   1 
ATOM   6089 C CB  . TYR B 1 241 ? -33.399 23.426 30.395  1.00 22.06 ? 241 TYR B CB  1 
ATOM   6090 C CG  . TYR B 1 241 ? -32.688 23.780 31.680  1.00 20.96 ? 241 TYR B CG  1 
ATOM   6091 C CD1 . TYR B 1 241 ? -32.570 22.846 32.708  1.00 23.83 ? 241 TYR B CD1 1 
ATOM   6092 C CD2 . TYR B 1 241 ? -32.169 25.055 31.881  1.00 17.90 ? 241 TYR B CD2 1 
ATOM   6093 C CE1 . TYR B 1 241 ? -31.941 23.164 33.896  1.00 22.94 ? 241 TYR B CE1 1 
ATOM   6094 C CE2 . TYR B 1 241 ? -31.546 25.392 33.067  1.00 17.41 ? 241 TYR B CE2 1 
ATOM   6095 C CZ  . TYR B 1 241 ? -31.427 24.434 34.073  1.00 18.99 ? 241 TYR B CZ  1 
ATOM   6096 O OH  . TYR B 1 241 ? -30.803 24.731 35.266  1.00 19.98 ? 241 TYR B OH  1 
ATOM   6097 N N   . PHE B 1 242 ? -32.876 20.338 29.895  1.00 24.13 ? 242 PHE B N   1 
ATOM   6098 C CA  . PHE B 1 242 ? -32.437 19.027 30.365  1.00 25.53 ? 242 PHE B CA  1 
ATOM   6099 C C   . PHE B 1 242 ? -31.327 18.455 29.487  1.00 27.37 ? 242 PHE B C   1 
ATOM   6100 O O   . PHE B 1 242 ? -30.434 17.756 29.980  1.00 25.13 ? 242 PHE B O   1 
ATOM   6101 C CB  . PHE B 1 242 ? -33.619 18.059 30.411  1.00 24.26 ? 242 PHE B CB  1 
ATOM   6102 C CG  . PHE B 1 242 ? -33.268 16.704 30.971  1.00 25.78 ? 242 PHE B CG  1 
ATOM   6103 C CD1 . PHE B 1 242 ? -33.166 16.509 32.338  1.00 26.34 ? 242 PHE B CD1 1 
ATOM   6104 C CD2 . PHE B 1 242 ? -33.022 15.634 30.131  1.00 26.17 ? 242 PHE B CD2 1 
ATOM   6105 C CE1 . PHE B 1 242 ? -32.830 15.270 32.855  1.00 29.05 ? 242 PHE B CE1 1 
ATOM   6106 C CE2 . PHE B 1 242 ? -32.695 14.387 30.645  1.00 30.77 ? 242 PHE B CE2 1 
ATOM   6107 C CZ  . PHE B 1 242 ? -32.595 14.209 32.009  1.00 30.96 ? 242 PHE B CZ  1 
ATOM   6108 N N   . GLU B 1 243 ? -31.388 18.709 28.175  1.00 24.92 ? 243 GLU B N   1 
ATOM   6109 C CA  . GLU B 1 243 ? -30.338 18.234 27.281  1.00 25.60 ? 243 GLU B CA  1 
ATOM   6110 C C   . GLU B 1 243 ? -28.986 18.817 27.672  1.00 26.69 ? 243 GLU B C   1 
ATOM   6111 O O   . GLU B 1 243 ? -27.970 18.113 27.674  1.00 27.69 ? 243 GLU B O   1 
ATOM   6112 C CB  . GLU B 1 243 ? -30.678 18.598 25.830  1.00 28.15 ? 243 GLU B CB  1 
ATOM   6113 C CG  . GLU B 1 243 ? -29.558 18.285 24.827  1.00 35.99 ? 243 GLU B CG  1 
ATOM   6114 C CD  . GLU B 1 243 ? -29.682 19.057 23.517  1.00 44.00 ? 243 GLU B CD  1 
ATOM   6115 O OE1 . GLU B 1 243 ? -28.635 19.346 22.893  1.00 44.12 ? 243 GLU B OE1 1 
ATOM   6116 O OE2 . GLU B 1 243 ? -30.820 19.372 23.104  1.00 40.30 ? 243 GLU B OE2 1 
ATOM   6117 N N   . ILE B 1 244 ? -28.965 20.099 28.027  1.00 20.76 ? 244 ILE B N   1 
ATOM   6118 C CA  . ILE B 1 244 ? -27.714 20.788 28.317  1.00 25.09 ? 244 ILE B CA  1 
ATOM   6119 C C   . ILE B 1 244 ? -27.213 20.450 29.715  1.00 23.75 ? 244 ILE B C   1 
ATOM   6120 O O   . ILE B 1 244 ? -26.026 20.158 29.911  1.00 31.49 ? 244 ILE B O   1 
ATOM   6121 C CB  . ILE B 1 244 ? -27.900 22.307 28.155  1.00 21.83 ? 244 ILE B CB  1 
ATOM   6122 C CG1 . ILE B 1 244 ? -28.396 22.658 26.750  1.00 24.06 ? 244 ILE B CG1 1 
ATOM   6123 C CG2 . ILE B 1 244 ? -26.618 23.044 28.508  1.00 22.22 ? 244 ILE B CG2 1 
ATOM   6124 C CD1 . ILE B 1 244 ? -27.650 22.010 25.638  1.00 22.21 ? 244 ILE B CD1 1 
ATOM   6125 N N   . PHE B 1 245 ? -28.102 20.497 30.709  1.00 20.02 ? 245 PHE B N   1 
ATOM   6126 C CA  . PHE B 1 245 ? -27.692 20.440 32.109  1.00 22.69 ? 245 PHE B CA  1 
ATOM   6127 C C   . PHE B 1 245 ? -28.056 19.144 32.821  1.00 28.96 ? 245 PHE B C   1 
ATOM   6128 O O   . PHE B 1 245 ? -27.614 18.943 33.956  1.00 26.14 ? 245 PHE B O   1 
ATOM   6129 C CB  . PHE B 1 245 ? -28.297 21.623 32.879  1.00 24.26 ? 245 PHE B CB  1 
ATOM   6130 C CG  . PHE B 1 245 ? -27.865 22.964 32.343  1.00 23.02 ? 245 PHE B CG  1 
ATOM   6131 C CD1 . PHE B 1 245 ? -26.556 23.393 32.507  1.00 21.94 ? 245 PHE B CD1 1 
ATOM   6132 C CD2 . PHE B 1 245 ? -28.754 23.772 31.646  1.00 20.48 ? 245 PHE B CD2 1 
ATOM   6133 C CE1 . PHE B 1 245 ? -26.142 24.614 32.004  1.00 25.25 ? 245 PHE B CE1 1 
ATOM   6134 C CE2 . PHE B 1 245 ? -28.345 24.982 31.134  1.00 21.49 ? 245 PHE B CE2 1 
ATOM   6135 C CZ  . PHE B 1 245 ? -27.041 25.411 31.317  1.00 19.17 ? 245 PHE B CZ  1 
ATOM   6136 N N   . GLY B 1 246 ? -28.851 18.272 32.207  1.00 28.41 ? 246 GLY B N   1 
ATOM   6137 C CA  . GLY B 1 246 ? -29.163 17.004 32.838  1.00 30.22 ? 246 GLY B CA  1 
ATOM   6138 C C   . GLY B 1 246 ? -30.098 17.094 34.020  1.00 38.57 ? 246 GLY B C   1 
ATOM   6139 O O   . GLY B 1 246 ? -30.145 16.178 34.842  1.00 36.37 ? 246 GLY B O   1 
ATOM   6140 N N   . GLU B 1 247 ? -30.838 18.184 34.146  1.00 33.70 ? 247 GLU B N   1 
ATOM   6141 C CA  . GLU B 1 247 ? -31.907 18.262 35.123  1.00 40.96 ? 247 GLU B CA  1 
ATOM   6142 C C   . GLU B 1 247 ? -33.042 19.066 34.509  1.00 34.15 ? 247 GLU B C   1 
ATOM   6143 O O   . GLU B 1 247 ? -32.854 19.784 33.526  1.00 25.48 ? 247 GLU B O   1 
ATOM   6144 C CB  . GLU B 1 247 ? -31.443 18.906 36.429  1.00 49.93 ? 247 GLU B CB  1 
ATOM   6145 C CG  . GLU B 1 247 ? -30.599 20.156 36.243  1.00 57.96 ? 247 GLU B CG  1 
ATOM   6146 C CD  . GLU B 1 247 ? -30.118 20.680 37.561  1.00 69.96 ? 247 GLU B CD  1 
ATOM   6147 O OE1 . GLU B 1 247 ? -29.599 19.854 38.350  1.00 74.99 ? 247 GLU B OE1 1 
ATOM   6148 O OE2 . GLU B 1 247 ? -30.369 21.882 37.836  1.00 72.59 ? 247 GLU B OE2 1 
ATOM   6149 N N   . HIS B 1 248 ? -34.202 18.911 35.065  1.00 23.88 ? 248 HIS B N   1 
ATOM   6150 C CA  . HIS B 1 248 ? -35.248 19.769 34.546  1.00 23.95 ? 248 HIS B CA  1 
ATOM   6151 C C   . HIS B 1 248 ? -35.228 21.096 35.290  1.00 26.86 ? 248 HIS B C   1 
ATOM   6152 O O   . HIS B 1 248 ? -34.882 21.143 36.474  1.00 28.49 ? 248 HIS B O   1 
ATOM   6153 C CB  . HIS B 1 248 ? -36.608 19.092 34.685  1.00 26.71 ? 248 HIS B CB  1 
ATOM   6154 C CG  . HIS B 1 248 ? -36.786 17.931 33.755  1.00 39.72 ? 248 HIS B CG  1 
ATOM   6155 N ND1 . HIS B 1 248 ? -36.511 16.631 34.126  1.00 42.07 ? 248 HIS B ND1 1 
ATOM   6156 C CD2 . HIS B 1 248 ? -37.172 17.879 32.458  1.00 39.90 ? 248 HIS B CD2 1 
ATOM   6157 C CE1 . HIS B 1 248 ? -36.738 15.827 33.102  1.00 46.25 ? 248 HIS B CE1 1 
ATOM   6158 N NE2 . HIS B 1 248 ? -37.140 16.559 32.078  1.00 42.85 ? 248 HIS B NE2 1 
ATOM   6159 N N   . PRO B 1 249 ? -35.559 22.195 34.613  1.00 21.63 ? 249 PRO B N   1 
ATOM   6160 C CA  . PRO B 1 249 ? -35.422 23.511 35.247  1.00 18.92 ? 249 PRO B CA  1 
ATOM   6161 C C   . PRO B 1 249 ? -36.512 23.734 36.282  1.00 22.25 ? 249 PRO B C   1 
ATOM   6162 O O   . PRO B 1 249 ? -37.696 23.511 36.027  1.00 28.83 ? 249 PRO B O   1 
ATOM   6163 C CB  . PRO B 1 249 ? -35.552 24.487 34.070  1.00 20.15 ? 249 PRO B CB  1 
ATOM   6164 C CG  . PRO B 1 249 ? -36.423 23.759 33.101  1.00 22.65 ? 249 PRO B CG  1 
ATOM   6165 C CD  . PRO B 1 249 ? -36.040 22.300 33.224  1.00 22.84 ? 249 PRO B CD  1 
ATOM   6166 N N   . VAL B 1 250 ? -36.092 24.194 37.456  1.00 21.51 ? 250 VAL B N   1 
ATOM   6167 C CA  . VAL B 1 250 ? -37.003 24.521 38.538  1.00 20.29 ? 250 VAL B CA  1 
ATOM   6168 C C   . VAL B 1 250 ? -37.329 26.017 38.581  1.00 20.60 ? 250 VAL B C   1 
ATOM   6169 O O   . VAL B 1 250 ? -38.331 26.401 39.203  1.00 19.37 ? 250 VAL B O   1 
ATOM   6170 C CB  . VAL B 1 250 ? -36.389 24.020 39.866  1.00 29.66 ? 250 VAL B CB  1 
ATOM   6171 C CG1 . VAL B 1 250 ? -34.978 24.497 39.989  1.00 37.35 ? 250 VAL B CG1 1 
ATOM   6172 C CG2 . VAL B 1 250 ? -37.185 24.419 41.076  1.00 34.55 ? 250 VAL B CG2 1 
ATOM   6173 N N   . TYR B 1 251 ? -36.541 26.862 37.904  1.00 15.94 ? 251 TYR B N   1 
ATOM   6174 C CA  . TYR B 1 251 ? -36.798 28.294 37.782  1.00 18.41 ? 251 TYR B CA  1 
ATOM   6175 C C   . TYR B 1 251 ? -36.909 28.667 36.318  1.00 17.02 ? 251 TYR B C   1 
ATOM   6176 O O   . TYR B 1 251 ? -36.160 28.154 35.480  1.00 17.00 ? 251 TYR B O   1 
ATOM   6177 C CB  . TYR B 1 251 ? -35.668 29.138 38.385  1.00 23.25 ? 251 TYR B CB  1 
ATOM   6178 C CG  . TYR B 1 251 ? -34.943 28.423 39.465  1.00 18.41 ? 251 TYR B CG  1 
ATOM   6179 C CD1 . TYR B 1 251 ? -35.475 28.358 40.738  1.00 29.77 ? 251 TYR B CD1 1 
ATOM   6180 C CD2 . TYR B 1 251 ? -33.715 27.821 39.226  1.00 31.34 ? 251 TYR B CD2 1 
ATOM   6181 C CE1 . TYR B 1 251 ? -34.824 27.700 41.743  1.00 34.56 ? 251 TYR B CE1 1 
ATOM   6182 C CE2 . TYR B 1 251 ? -33.049 27.150 40.236  1.00 30.56 ? 251 TYR B CE2 1 
ATOM   6183 C CZ  . TYR B 1 251 ? -33.616 27.101 41.492  1.00 40.94 ? 251 TYR B CZ  1 
ATOM   6184 O OH  . TYR B 1 251 ? -32.990 26.434 42.509  1.00 56.36 ? 251 TYR B OH  1 
ATOM   6185 N N   . MET B 1 252 ? -37.814 29.588 36.021  1.00 15.94 ? 252 MET B N   1 
ATOM   6186 C CA  . MET B 1 252 ? -37.930 30.137 34.687  1.00 12.17 ? 252 MET B CA  1 
ATOM   6187 C C   . MET B 1 252 ? -38.004 31.653 34.774  1.00 13.92 ? 252 MET B C   1 
ATOM   6188 O O   . MET B 1 252 ? -38.512 32.212 35.746  1.00 14.80 ? 252 MET B O   1 
ATOM   6189 C CB  . MET B 1 252 ? -39.164 29.596 33.949  1.00 14.06 ? 252 MET B CB  1 
ATOM   6190 C CG  . MET B 1 252 ? -38.970 28.181 33.435  1.00 16.39 ? 252 MET B CG  1 
ATOM   6191 S SD  . MET B 1 252 ? -40.033 27.739 32.040  1.00 19.32 ? 252 MET B SD  1 
ATOM   6192 C CE  . MET B 1 252 ? -39.297 26.172 31.553  1.00 20.68 ? 252 MET B CE  1 
ATOM   6193 N N   . TRP B 1 253 ? -37.462 32.307 33.756  1.00 14.68 ? 253 TRP B N   1 
ATOM   6194 C CA  . TRP B 1 253 ? -37.670 33.727 33.570  1.00 16.94 ? 253 TRP B CA  1 
ATOM   6195 C C   . TRP B 1 253 ? -38.796 33.896 32.570  1.00 16.66 ? 253 TRP B C   1 
ATOM   6196 O O   . TRP B 1 253 ? -38.655 33.432 31.426  1.00 15.23 ? 253 TRP B O   1 
ATOM   6197 C CB  . TRP B 1 253 ? -36.403 34.411 33.061  1.00 13.46 ? 253 TRP B CB  1 
ATOM   6198 C CG  . TRP B 1 253 ? -36.686 35.818 32.617  1.00 11.48 ? 253 TRP B CG  1 
ATOM   6199 C CD1 . TRP B 1 253 ? -36.647 36.304 31.335  1.00 13.69 ? 253 TRP B CD1 1 
ATOM   6200 C CD2 . TRP B 1 253 ? -37.091 36.909 33.446  1.00 9.30  ? 253 TRP B CD2 1 
ATOM   6201 N NE1 . TRP B 1 253 ? -37.002 37.634 31.322  1.00 12.80 ? 253 TRP B NE1 1 
ATOM   6202 C CE2 . TRP B 1 253 ? -37.296 38.021 32.604  1.00 9.52  ? 253 TRP B CE2 1 
ATOM   6203 C CE3 . TRP B 1 253 ? -37.336 37.046 34.819  1.00 12.22 ? 253 TRP B CE3 1 
ATOM   6204 C CZ2 . TRP B 1 253 ? -37.700 39.267 33.090  1.00 12.89 ? 253 TRP B CZ2 1 
ATOM   6205 C CZ3 . TRP B 1 253 ? -37.740 38.284 35.300  1.00 12.75 ? 253 TRP B CZ3 1 
ATOM   6206 C CH2 . TRP B 1 253 ? -37.920 39.375 34.438  1.00 12.90 ? 253 TRP B CH2 1 
ATOM   6207 N N   . PRO B 1 254 ? -39.932 34.484 32.932  1.00 11.45 ? 254 PRO B N   1 
ATOM   6208 C CA  . PRO B 1 254 ? -40.997 34.647 31.952  1.00 14.28 ? 254 PRO B CA  1 
ATOM   6209 C C   . PRO B 1 254 ? -40.624 35.753 30.986  1.00 12.52 ? 254 PRO B C   1 
ATOM   6210 O O   . PRO B 1 254 ? -40.207 36.838 31.418  1.00 14.50 ? 254 PRO B O   1 
ATOM   6211 C CB  . PRO B 1 254 ? -42.222 35.016 32.805  1.00 17.72 ? 254 PRO B CB  1 
ATOM   6212 C CG  . PRO B 1 254 ? -41.651 35.646 34.046  1.00 16.48 ? 254 PRO B CG  1 
ATOM   6213 C CD  . PRO B 1 254 ? -40.278 35.022 34.261  1.00 10.24 ? 254 PRO B CD  1 
ATOM   6214 N N   . PRO B 1 255 ? -40.686 35.504 29.681  1.00 12.39 ? 255 PRO B N   1 
ATOM   6215 C CA  . PRO B 1 255 ? -40.261 36.532 28.724  1.00 12.15 ? 255 PRO B CA  1 
ATOM   6216 C C   . PRO B 1 255 ? -40.954 37.862 28.983  1.00 11.86 ? 255 PRO B C   1 
ATOM   6217 O O   . PRO B 1 255 ? -42.163 37.914 29.232  1.00 14.56 ? 255 PRO B O   1 
ATOM   6218 C CB  . PRO B 1 255 ? -40.667 35.941 27.374  1.00 14.00 ? 255 PRO B CB  1 
ATOM   6219 C CG  . PRO B 1 255 ? -40.567 34.463 27.599  1.00 15.27 ? 255 PRO B CG  1 
ATOM   6220 C CD  . PRO B 1 255 ? -41.036 34.241 29.015  1.00 14.37 ? 255 PRO B CD  1 
ATOM   6221 N N   . GLU B 1 256 ? -40.161 38.941 28.926  1.00 12.75 ? 256 GLU B N   1 
ATOM   6222 C CA  . GLU B 1 256 ? -40.617 40.307 29.196  1.00 14.09 ? 256 GLU B CA  1 
ATOM   6223 C C   . GLU B 1 256 ? -41.223 40.441 30.586  1.00 14.86 ? 256 GLU B C   1 
ATOM   6224 O O   . GLU B 1 256 ? -42.082 41.298 30.812  1.00 12.55 ? 256 GLU B O   1 
ATOM   6225 C CB  . GLU B 1 256 ? -41.617 40.791 28.140  1.00 16.14 ? 256 GLU B CB  1 
ATOM   6226 C CG  . GLU B 1 256 ? -41.194 40.506 26.698  1.00 12.86 ? 256 GLU B CG  1 
ATOM   6227 C CD  . GLU B 1 256 ? -39.954 41.282 26.258  1.00 17.07 ? 256 GLU B CD  1 
ATOM   6228 O OE1 . GLU B 1 256 ? -39.564 42.257 26.933  1.00 19.29 ? 256 GLU B OE1 1 
ATOM   6229 O OE2 . GLU B 1 256 ? -39.389 40.945 25.196  1.00 16.05 ? 256 GLU B OE2 1 
ATOM   6230 N N   . ALA B 1 257 ? -40.788 39.589 31.515  1.00 13.26 ? 257 ALA B N   1 
ATOM   6231 C CA  . ALA B 1 257 ? -41.340 39.526 32.865  1.00 12.49 ? 257 ALA B CA  1 
ATOM   6232 C C   . ALA B 1 257 ? -42.849 39.285 32.847  1.00 12.47 ? 257 ALA B C   1 
ATOM   6233 O O   . ALA B 1 257 ? -43.541 39.572 33.832  1.00 16.73 ? 257 ALA B O   1 
ATOM   6234 C CB  . ALA B 1 257 ? -41.023 40.796 33.657  1.00 16.53 ? 257 ALA B CB  1 
ATOM   6235 N N   . SER B 1 258 ? -43.381 38.752 31.750  1.00 12.62 ? 258 SER B N   1 
ATOM   6236 C CA  . SER B 1 258 ? -44.823 38.779 31.550  1.00 13.27 ? 258 SER B CA  1 
ATOM   6237 C C   . SER B 1 258 ? -45.511 37.686 32.357  1.00 15.07 ? 258 SER B C   1 
ATOM   6238 O O   . SER B 1 258 ? -45.177 36.502 32.243  1.00 15.32 ? 258 SER B O   1 
ATOM   6239 C CB  . SER B 1 258 ? -45.164 38.636 30.066  1.00 15.38 ? 258 SER B CB  1 
ATOM   6240 O OG  . SER B 1 258 ? -46.539 38.926 29.874  1.00 18.36 ? 258 SER B OG  1 
ATOM   6241 N N   . VAL B 1 259 ? -46.493 38.083 33.166  1.00 15.20 ? 259 VAL B N   1 
ATOM   6242 C CA  . VAL B 1 259 ? -47.293 37.138 33.925  1.00 12.21 ? 259 VAL B CA  1 
ATOM   6243 C C   . VAL B 1 259 ? -48.753 37.544 33.824  1.00 16.14 ? 259 VAL B C   1 
ATOM   6244 O O   . VAL B 1 259 ? -49.104 38.629 33.350  1.00 20.33 ? 259 VAL B O   1 
ATOM   6245 C CB  . VAL B 1 259 ? -46.858 37.028 35.403  1.00 13.90 ? 259 VAL B CB  1 
ATOM   6246 C CG1 . VAL B 1 259 ? -45.396 36.518 35.484  1.00 17.23 ? 259 VAL B CG1 1 
ATOM   6247 C CG2 . VAL B 1 259 ? -47.009 38.367 36.111  1.00 16.22 ? 259 VAL B CG2 1 
ATOM   6248 N N   . SER B 1 260 ? -49.592 36.610 34.245  1.00 14.92 ? 260 SER B N   1 
ATOM   6249 C CA  . SER B 1 260 ? -51.032 36.717 34.346  1.00 13.86 ? 260 SER B CA  1 
ATOM   6250 C C   . SER B 1 260 ? -51.421 35.569 35.258  1.00 18.39 ? 260 SER B C   1 
ATOM   6251 O O   . SER B 1 260 ? -50.606 34.681 35.522  1.00 18.38 ? 260 SER B O   1 
ATOM   6252 C CB  . SER B 1 260 ? -51.713 36.608 32.978  1.00 17.52 ? 260 SER B CB  1 
ATOM   6253 O OG  . SER B 1 260 ? -51.651 35.267 32.492  1.00 18.55 ? 260 SER B OG  1 
ATOM   6254 N N   . ASN B 1 261 ? -52.650 35.606 35.764  1.00 17.10 ? 261 ASN B N   1 
ATOM   6255 C CA  . ASN B 1 261 ? -53.088 34.519 36.629  1.00 17.15 ? 261 ASN B CA  1 
ATOM   6256 C C   . ASN B 1 261 ? -52.997 33.179 35.901  1.00 20.85 ? 261 ASN B C   1 
ATOM   6257 O O   . ASN B 1 261 ? -52.516 32.190 36.467  1.00 18.68 ? 261 ASN B O   1 
ATOM   6258 C CB  . ASN B 1 261 ? -54.509 34.779 37.129  1.00 17.57 ? 261 ASN B CB  1 
ATOM   6259 C CG  . ASN B 1 261 ? -54.585 35.929 38.121  1.00 18.23 ? 261 ASN B CG  1 
ATOM   6260 O OD1 . ASN B 1 261 ? -53.616 36.245 38.803  1.00 20.14 ? 261 ASN B OD1 1 
ATOM   6261 N ND2 . ASN B 1 261 ? -55.755 36.546 38.216  1.00 19.51 ? 261 ASN B ND2 1 
ATOM   6262 N N   . GLU B 1 262 ? -53.395 33.140 34.627  1.00 17.76 ? 262 GLU B N   1 
ATOM   6263 C CA  . GLU B 1 262 ? -53.344 31.882 33.884  1.00 19.51 ? 262 GLU B CA  1 
ATOM   6264 C C   . GLU B 1 262 ? -51.910 31.458 33.605  1.00 17.06 ? 262 GLU B C   1 
ATOM   6265 O O   . GLU B 1 262 ? -51.595 30.261 33.606  1.00 18.59 ? 262 GLU B O   1 
ATOM   6266 C CB  . GLU B 1 262 ? -54.111 32.005 32.571  1.00 21.38 ? 262 GLU B CB  1 
ATOM   6267 C CG  . GLU B 1 262 ? -55.593 32.062 32.779  1.00 21.34 ? 262 GLU B CG  1 
ATOM   6268 C CD  . GLU B 1 262 ? -56.363 32.145 31.474  1.00 38.79 ? 262 GLU B CD  1 
ATOM   6269 O OE1 . GLU B 1 262 ? -55.896 31.583 30.460  1.00 35.76 ? 262 GLU B OE1 1 
ATOM   6270 O OE2 . GLU B 1 262 ? -57.438 32.775 31.470  1.00 38.01 ? 262 GLU B OE2 1 
ATOM   6271 N N   . ALA B 1 263 ? -51.037 32.416 33.319  1.00 15.38 ? 263 ALA B N   1 
ATOM   6272 C CA  . ALA B 1 263 ? -49.646 32.062 33.052  1.00 17.95 ? 263 ALA B CA  1 
ATOM   6273 C C   . ALA B 1 263 ? -48.981 31.481 34.292  1.00 14.35 ? 263 ALA B C   1 
ATOM   6274 O O   . ALA B 1 263 ? -48.278 30.470 34.210  1.00 16.54 ? 263 ALA B O   1 
ATOM   6275 C CB  . ALA B 1 263 ? -48.871 33.279 32.557  1.00 18.12 ? 263 ALA B CB  1 
ATOM   6276 N N   . LEU B 1 264 ? -49.198 32.103 35.451  1.00 17.39 ? 264 LEU B N   1 
ATOM   6277 C CA  . LEU B 1 264 ? -48.658 31.549 36.690  1.00 15.28 ? 264 LEU B CA  1 
ATOM   6278 C C   . LEU B 1 264 ? -49.164 30.133 36.931  1.00 21.01 ? 264 LEU B C   1 
ATOM   6279 O O   . LEU B 1 264 ? -48.411 29.273 37.402  1.00 20.37 ? 264 LEU B O   1 
ATOM   6280 C CB  . LEU B 1 264 ? -49.007 32.459 37.862  1.00 13.23 ? 264 LEU B CB  1 
ATOM   6281 C CG  . LEU B 1 264 ? -48.289 33.815 37.764  1.00 14.34 ? 264 LEU B CG  1 
ATOM   6282 C CD1 . LEU B 1 264 ? -48.820 34.796 38.794  1.00 21.08 ? 264 LEU B CD1 1 
ATOM   6283 C CD2 . LEU B 1 264 ? -46.783 33.616 37.939  1.00 18.50 ? 264 LEU B CD2 1 
ATOM   6284 N N   . GLU B 1 265 ? -50.433 29.867 36.607  1.00 17.76 ? 265 GLU B N   1 
ATOM   6285 C CA  . GLU B 1 265 ? -50.949 28.509 36.732  1.00 18.70 ? 265 GLU B CA  1 
ATOM   6286 C C   . GLU B 1 265 ? -50.245 27.551 35.776  1.00 20.53 ? 265 GLU B C   1 
ATOM   6287 O O   . GLU B 1 265 ? -49.986 26.395 36.137  1.00 24.34 ? 265 GLU B O   1 
ATOM   6288 C CB  . GLU B 1 265 ? -52.461 28.493 36.494  1.00 22.20 ? 265 GLU B CB  1 
ATOM   6289 C CG  . GLU B 1 265 ? -53.263 29.162 37.598  1.00 25.70 ? 265 GLU B CG  1 
ATOM   6290 C CD  . GLU B 1 265 ? -54.758 28.938 37.453  1.00 40.73 ? 265 GLU B CD  1 
ATOM   6291 O OE1 . GLU B 1 265 ? -55.431 28.692 38.476  1.00 46.77 ? 265 GLU B OE1 1 
ATOM   6292 O OE2 . GLU B 1 265 ? -55.261 29.007 36.310  1.00 46.12 ? 265 GLU B OE2 1 
ATOM   6293 N N   . LEU B 1 266 ? -49.949 27.997 34.547  1.00 19.46 ? 266 LEU B N   1 
ATOM   6294 C CA  . LEU B 1 266 ? -49.279 27.117 33.591  1.00 18.16 ? 266 LEU B CA  1 
ATOM   6295 C C   . LEU B 1 266 ? -47.865 26.780 34.053  1.00 16.61 ? 266 LEU B C   1 
ATOM   6296 O O   . LEU B 1 266 ? -47.459 25.614 34.019  1.00 19.85 ? 266 LEU B O   1 
ATOM   6297 C CB  . LEU B 1 266 ? -49.254 27.756 32.198  1.00 18.52 ? 266 LEU B CB  1 
ATOM   6298 C CG  . LEU B 1 266 ? -48.388 27.037 31.160  1.00 21.48 ? 266 LEU B CG  1 
ATOM   6299 C CD1 . LEU B 1 266 ? -48.898 25.627 30.896  1.00 23.78 ? 266 LEU B CD1 1 
ATOM   6300 C CD2 . LEU B 1 266 ? -48.303 27.842 29.849  1.00 21.78 ? 266 LEU B CD2 1 
ATOM   6301 N N   . TYR B 1 267 ? -47.123 27.774 34.536  1.00 16.27 ? 267 TYR B N   1 
ATOM   6302 C CA  . TYR B 1 267 ? -45.784 27.503 35.057  1.00 18.89 ? 267 TYR B CA  1 
ATOM   6303 C C   . TYR B 1 267 ? -45.830 26.517 36.220  1.00 14.59 ? 267 TYR B C   1 
ATOM   6304 O O   . TYR B 1 267 ? -45.004 25.599 36.294  1.00 20.78 ? 267 TYR B O   1 
ATOM   6305 C CB  . TYR B 1 267 ? -45.114 28.800 35.496  1.00 15.47 ? 267 TYR B CB  1 
ATOM   6306 C CG  . TYR B 1 267 ? -44.651 29.670 34.354  1.00 19.31 ? 267 TYR B CG  1 
ATOM   6307 C CD1 . TYR B 1 267 ? -43.636 29.239 33.501  1.00 17.52 ? 267 TYR B CD1 1 
ATOM   6308 C CD2 . TYR B 1 267 ? -45.227 30.917 34.123  1.00 11.87 ? 267 TYR B CD2 1 
ATOM   6309 C CE1 . TYR B 1 267 ? -43.195 30.012 32.469  1.00 16.17 ? 267 TYR B CE1 1 
ATOM   6310 C CE2 . TYR B 1 267 ? -44.782 31.722 33.074  1.00 16.97 ? 267 TYR B CE2 1 
ATOM   6311 C CZ  . TYR B 1 267 ? -43.771 31.260 32.250  1.00 18.03 ? 267 TYR B CZ  1 
ATOM   6312 O OH  . TYR B 1 267 ? -43.318 32.018 31.200  1.00 18.04 ? 267 TYR B OH  1 
ATOM   6313 N N   . TYR B 1 268 ? -46.777 26.708 37.150  1.00 15.03 ? 268 TYR B N   1 
ATOM   6314 C CA  . TYR B 1 268 ? -46.966 25.765 38.252  1.00 18.39 ? 268 TYR B CA  1 
ATOM   6315 C C   . TYR B 1 268 ? -47.280 24.362 37.738  1.00 21.05 ? 268 TYR B C   1 
ATOM   6316 O O   . TYR B 1 268 ? -46.700 23.370 38.197  1.00 19.71 ? 268 TYR B O   1 
ATOM   6317 C CB  . TYR B 1 268 ? -48.090 26.259 39.176  1.00 17.82 ? 268 TYR B CB  1 
ATOM   6318 C CG  . TYR B 1 268 ? -48.756 25.153 39.954  1.00 19.58 ? 268 TYR B CG  1 
ATOM   6319 C CD1 . TYR B 1 268 ? -48.086 24.515 40.985  1.00 23.99 ? 268 TYR B CD1 1 
ATOM   6320 C CD2 . TYR B 1 268 ? -50.051 24.742 39.656  1.00 19.71 ? 268 TYR B CD2 1 
ATOM   6321 C CE1 . TYR B 1 268 ? -48.678 23.506 41.699  1.00 25.54 ? 268 TYR B CE1 1 
ATOM   6322 C CE2 . TYR B 1 268 ? -50.653 23.719 40.365  1.00 27.19 ? 268 TYR B CE2 1 
ATOM   6323 C CZ  . TYR B 1 268 ? -49.960 23.107 41.386  1.00 31.10 ? 268 TYR B CZ  1 
ATOM   6324 O OH  . TYR B 1 268 ? -50.545 22.088 42.101  1.00 31.77 ? 268 TYR B OH  1 
ATOM   6325 N N   . GLU B 1 269 ? -48.204 24.252 36.782  1.00 24.56 ? 269 GLU B N   1 
ATOM   6326 C CA  . GLU B 1 269 ? -48.598 22.927 36.323  1.00 25.94 ? 269 GLU B CA  1 
ATOM   6327 C C   . GLU B 1 269 ? -47.456 22.218 35.606  1.00 23.50 ? 269 GLU B C   1 
ATOM   6328 O O   . GLU B 1 269 ? -47.398 20.985 35.615  1.00 27.04 ? 269 GLU B O   1 
ATOM   6329 C CB  . GLU B 1 269 ? -49.834 23.018 35.425  1.00 25.06 ? 269 GLU B CB  1 
ATOM   6330 C CG  . GLU B 1 269 ? -51.142 23.264 36.180  1.00 28.87 ? 269 GLU B CG  1 
ATOM   6331 C CD  . GLU B 1 269 ? -51.557 22.120 37.113  1.00 40.59 ? 269 GLU B CD  1 
ATOM   6332 O OE1 . GLU B 1 269 ? -50.979 21.009 37.040  1.00 39.05 ? 269 GLU B OE1 1 
ATOM   6333 O OE2 . GLU B 1 269 ? -52.487 22.337 37.921  1.00 44.51 ? 269 GLU B OE2 1 
ATOM   6334 N N   . LYS B 1 270 ? -46.530 22.969 35.015  1.00 23.59 ? 270 LYS B N   1 
ATOM   6335 C CA  . LYS B 1 270 ? -45.365 22.390 34.358  1.00 23.08 ? 270 LYS B CA  1 
ATOM   6336 C C   . LYS B 1 270 ? -44.195 22.182 35.315  1.00 25.54 ? 270 LYS B C   1 
ATOM   6337 O O   . LYS B 1 270 ? -43.092 21.856 34.866  1.00 23.23 ? 270 LYS B O   1 
ATOM   6338 C CB  . LYS B 1 270 ? -44.932 23.272 33.184  1.00 22.38 ? 270 LYS B CB  1 
ATOM   6339 C CG  . LYS B 1 270 ? -45.946 23.339 32.054  1.00 23.47 ? 270 LYS B CG  1 
ATOM   6340 C CD  . LYS B 1 270 ? -46.169 21.972 31.420  1.00 33.00 ? 270 LYS B CD  1 
ATOM   6341 C CE  . LYS B 1 270 ? -47.201 22.050 30.300  1.00 37.76 ? 270 LYS B CE  1 
ATOM   6342 N NZ  . LYS B 1 270 ? -48.132 20.883 30.279  1.00 44.60 ? 270 LYS B NZ  1 
ATOM   6343 N N   . GLY B 1 271 ? -44.407 22.365 36.615  1.00 18.38 ? 271 GLY B N   1 
ATOM   6344 C CA  . GLY B 1 271 ? -43.402 22.037 37.598  1.00 22.54 ? 271 GLY B CA  1 
ATOM   6345 C C   . GLY B 1 271 ? -42.415 23.139 37.901  1.00 20.78 ? 271 GLY B C   1 
ATOM   6346 O O   . GLY B 1 271 ? -41.396 22.869 38.548  1.00 24.50 ? 271 GLY B O   1 
ATOM   6347 N N   . ILE B 1 272 ? -42.672 24.361 37.456  1.00 18.81 ? 272 ILE B N   1 
ATOM   6348 C CA  . ILE B 1 272 ? -41.807 25.487 37.791  1.00 18.24 ? 272 ILE B CA  1 
ATOM   6349 C C   . ILE B 1 272 ? -42.093 25.906 39.225  1.00 19.33 ? 272 ILE B C   1 
ATOM   6350 O O   . ILE B 1 272 ? -43.249 26.147 39.595  1.00 22.31 ? 272 ILE B O   1 
ATOM   6351 C CB  . ILE B 1 272 ? -42.026 26.657 36.817  1.00 17.02 ? 272 ILE B CB  1 
ATOM   6352 C CG1 . ILE B 1 272 ? -41.804 26.207 35.366  1.00 22.48 ? 272 ILE B CG1 1 
ATOM   6353 C CG2 . ILE B 1 272 ? -41.144 27.850 37.186  1.00 18.03 ? 272 ILE B CG2 1 
ATOM   6354 C CD1 . ILE B 1 272 ? -40.591 25.317 35.155  1.00 25.22 ? 272 ILE B CD1 1 
ATOM   6355 N N   . ASN B 1 273 ? -41.037 25.991 40.037  1.00 19.52 ? 273 ASN B N   1 
ATOM   6356 C CA  . ASN B 1 273 ? -41.167 26.306 41.455  1.00 17.98 ? 273 ASN B CA  1 
ATOM   6357 C C   . ASN B 1 273 ? -41.018 27.789 41.760  1.00 16.81 ? 273 ASN B C   1 
ATOM   6358 O O   . ASN B 1 273 ? -41.545 28.261 42.777  1.00 17.57 ? 273 ASN B O   1 
ATOM   6359 C CB  . ASN B 1 273 ? -40.120 25.534 42.247  1.00 17.22 ? 273 ASN B CB  1 
ATOM   6360 C CG  . ASN B 1 273 ? -40.602 25.145 43.616  1.00 43.21 ? 273 ASN B CG  1 
ATOM   6361 O OD1 . ASN B 1 273 ? -41.774 24.829 43.803  1.00 44.49 ? 273 ASN B OD1 1 
ATOM   6362 N ND2 . ASN B 1 273 ? -39.697 25.154 44.587  1.00 53.93 ? 273 ASN B ND2 1 
ATOM   6363 N N   A MET B 1 274 ? -40.303 28.533 40.922  0.54 16.83 ? 274 MET B N   1 
ATOM   6364 N N   B MET B 1 274 ? -40.296 28.532 40.928  0.46 16.84 ? 274 MET B N   1 
ATOM   6365 C CA  A MET B 1 274 ? -40.081 29.947 41.184  0.54 16.80 ? 274 MET B CA  1 
ATOM   6366 C CA  B MET B 1 274 ? -40.102 29.952 41.180  0.46 16.83 ? 274 MET B CA  1 
ATOM   6367 C C   A MET B 1 274 ? -39.848 30.678 39.872  0.54 16.21 ? 274 MET B C   1 
ATOM   6368 C C   B MET B 1 274 ? -39.864 30.672 39.863  0.46 16.26 ? 274 MET B C   1 
ATOM   6369 O O   A MET B 1 274 ? -39.234 30.141 38.949  0.54 18.41 ? 274 MET B O   1 
ATOM   6370 O O   B MET B 1 274 ? -39.261 30.130 38.936  0.46 18.31 ? 274 MET B O   1 
ATOM   6371 C CB  A MET B 1 274 ? -38.888 30.162 42.126  0.54 17.04 ? 274 MET B CB  1 
ATOM   6372 C CB  B MET B 1 274 ? -38.930 30.209 42.138  0.46 16.99 ? 274 MET B CB  1 
ATOM   6373 C CG  A MET B 1 274 ? -38.726 31.595 42.623  0.54 16.98 ? 274 MET B CG  1 
ATOM   6374 C CG  B MET B 1 274 ? -38.753 31.672 42.552  0.46 17.00 ? 274 MET B CG  1 
ATOM   6375 S SD  A MET B 1 274 ? -37.154 31.868 43.459  0.54 20.90 ? 274 MET B SD  1 
ATOM   6376 S SD  B MET B 1 274 ? -37.663 32.603 41.445  0.46 19.52 ? 274 MET B SD  1 
ATOM   6377 C CE  A MET B 1 274 ? -35.989 31.715 42.110  0.54 21.43 ? 274 MET B CE  1 
ATOM   6378 C CE  B MET B 1 274 ? -36.066 31.991 41.982  0.46 22.66 ? 274 MET B CE  1 
ATOM   6379 N N   . LEU B 1 275 ? -40.352 31.904 39.795  1.00 15.95 ? 275 LEU B N   1 
ATOM   6380 C CA  . LEU B 1 275 ? -40.034 32.801 38.703  1.00 14.74 ? 275 LEU B CA  1 
ATOM   6381 C C   . LEU B 1 275 ? -39.902 34.177 39.317  1.00 13.65 ? 275 LEU B C   1 
ATOM   6382 O O   . LEU B 1 275 ? -40.159 34.363 40.507  1.00 13.48 ? 275 LEU B O   1 
ATOM   6383 C CB  . LEU B 1 275 ? -41.085 32.770 37.590  1.00 16.82 ? 275 LEU B CB  1 
ATOM   6384 C CG  . LEU B 1 275 ? -42.562 32.916 37.921  1.00 18.97 ? 275 LEU B CG  1 
ATOM   6385 C CD1 . LEU B 1 275 ? -42.916 34.362 38.207  1.00 21.17 ? 275 LEU B CD1 1 
ATOM   6386 C CD2 . LEU B 1 275 ? -43.390 32.420 36.764  1.00 20.15 ? 275 LEU B CD2 1 
ATOM   6387 N N   . ALA B 1 276 ? -39.450 35.130 38.510  1.00 15.76 ? 276 ALA B N   1 
ATOM   6388 C CA  . ALA B 1 276 ? -39.460 36.532 38.891  1.00 14.68 ? 276 ALA B CA  1 
ATOM   6389 C C   . ALA B 1 276 ? -40.278 37.315 37.870  1.00 12.66 ? 276 ALA B C   1 
ATOM   6390 O O   . ALA B 1 276 ? -40.502 36.866 36.741  1.00 15.08 ? 276 ALA B O   1 
ATOM   6391 C CB  . ALA B 1 276 ? -38.038 37.102 38.996  1.00 11.79 ? 276 ALA B CB  1 
ATOM   6392 N N   . THR B 1 277 ? -40.741 38.488 38.274  1.00 12.86 ? 277 THR B N   1 
ATOM   6393 C CA  . THR B 1 277 ? -41.427 39.372 37.332  1.00 12.77 ? 277 THR B CA  1 
ATOM   6394 C C   . THR B 1 277 ? -41.112 40.806 37.758  1.00 14.24 ? 277 THR B C   1 
ATOM   6395 O O   . THR B 1 277 ? -40.107 41.053 38.434  1.00 15.23 ? 277 THR B O   1 
ATOM   6396 C CB  . THR B 1 277 ? -42.926 39.005 37.244  1.00 15.46 ? 277 THR B CB  1 
ATOM   6397 O OG1 . THR B 1 277 ? -43.613 39.897 36.355  1.00 14.94 ? 277 THR B OG1 1 
ATOM   6398 C CG2 . THR B 1 277 ? -43.579 39.073 38.592  1.00 14.37 ? 277 THR B CG2 1 
ATOM   6399 N N   . ASP B 1 278 ? -41.935 41.765 37.346  1.00 14.09 ? 278 ASP B N   1 
ATOM   6400 C CA  . ASP B 1 278 ? -41.547 43.166 37.442  1.00 14.26 ? 278 ASP B CA  1 
ATOM   6401 C C   . ASP B 1 278 ? -42.293 43.910 38.548  1.00 15.66 ? 278 ASP B C   1 
ATOM   6402 O O   . ASP B 1 278 ? -43.434 43.586 38.888  1.00 15.53 ? 278 ASP B O   1 
ATOM   6403 C CB  . ASP B 1 278 ? -41.780 43.893 36.119  1.00 15.98 ? 278 ASP B CB  1 
ATOM   6404 C CG  . ASP B 1 278 ? -41.306 45.333 36.170  1.00 19.59 ? 278 ASP B CG  1 
ATOM   6405 O OD1 . ASP B 1 278 ? -40.118 45.561 36.494  1.00 19.48 ? 278 ASP B OD1 1 
ATOM   6406 O OD2 . ASP B 1 278 ? -42.121 46.240 35.893  1.00 21.02 ? 278 ASP B OD2 1 
ATOM   6407 N N   . GLU B 1 279 ? -41.624 44.937 39.083  1.00 18.11 ? 279 GLU B N   1 
ATOM   6408 C CA  . GLU B 1 279 ? -42.178 45.727 40.178  1.00 17.91 ? 279 GLU B CA  1 
ATOM   6409 C C   . GLU B 1 279 ? -43.450 46.466 39.770  1.00 17.59 ? 279 GLU B C   1 
ATOM   6410 O O   . GLU B 1 279 ? -44.350 46.660 40.600  1.00 19.54 ? 279 GLU B O   1 
ATOM   6411 C CB  . GLU B 1 279 ? -41.121 46.716 40.680  1.00 16.24 ? 279 GLU B CB  1 
ATOM   6412 C CG  . GLU B 1 279 ? -41.527 47.430 41.939  1.00 18.86 ? 279 GLU B CG  1 
ATOM   6413 C CD  . GLU B 1 279 ? -40.404 48.256 42.537  1.00 21.24 ? 279 GLU B CD  1 
ATOM   6414 O OE1 . GLU B 1 279 ? -39.275 48.227 41.994  1.00 17.38 ? 279 GLU B OE1 1 
ATOM   6415 O OE2 . GLU B 1 279 ? -40.657 48.943 43.547  1.00 27.53 ? 279 GLU B OE2 1 
ATOM   6416 N N   . VAL B 1 280 ? -43.556 46.892 38.509  1.00 16.45 ? 280 VAL B N   1 
ATOM   6417 C CA  . VAL B 1 280 ? -44.772 47.587 38.091  1.00 17.29 ? 280 VAL B CA  1 
ATOM   6418 C C   . VAL B 1 280 ? -45.968 46.645 38.169  1.00 19.82 ? 280 VAL B C   1 
ATOM   6419 O O   . VAL B 1 280 ? -47.074 47.049 38.550  1.00 19.72 ? 280 VAL B O   1 
ATOM   6420 C CB  . VAL B 1 280 ? -44.603 48.187 36.681  1.00 19.82 ? 280 VAL B CB  1 
ATOM   6421 C CG1 . VAL B 1 280 ? -45.911 48.801 36.200  1.00 23.33 ? 280 VAL B CG1 1 
ATOM   6422 C CG2 . VAL B 1 280 ? -43.490 49.241 36.676  1.00 22.23 ? 280 VAL B CG2 1 
ATOM   6423 N N   . ILE B 1 281 ? -45.756 45.369 37.845  1.00 19.41 ? 281 ILE B N   1 
ATOM   6424 C CA  . ILE B 1 281 ? -46.836 44.391 37.952  1.00 21.40 ? 281 ILE B CA  1 
ATOM   6425 C C   . ILE B 1 281 ? -47.234 44.201 39.409  1.00 18.16 ? 281 ILE B C   1 
ATOM   6426 O O   . ILE B 1 281 ? -48.429 44.109 39.732  1.00 20.15 ? 281 ILE B O   1 
ATOM   6427 C CB  . ILE B 1 281 ? -46.426 43.066 37.280  1.00 17.31 ? 281 ILE B CB  1 
ATOM   6428 C CG1 . ILE B 1 281 ? -46.313 43.286 35.764  1.00 23.39 ? 281 ILE B CG1 1 
ATOM   6429 C CG2 . ILE B 1 281 ? -47.428 41.969 37.599  1.00 21.19 ? 281 ILE B CG2 1 
ATOM   6430 C CD1 . ILE B 1 281 ? -45.677 42.136 35.011  1.00 22.36 ? 281 ILE B CD1 1 
ATOM   6431 N N   . LEU B 1 282 ? -46.252 44.181 40.316  1.00 17.66 ? 282 LEU B N   1 
ATOM   6432 C CA  . LEU B 1 282 ? -46.566 44.106 41.742  1.00 16.05 ? 282 LEU B CA  1 
ATOM   6433 C C   . LEU B 1 282 ? -47.405 45.299 42.173  1.00 18.38 ? 282 LEU B C   1 
ATOM   6434 O O   . LEU B 1 282 ? -48.418 45.143 42.865  1.00 20.31 ? 282 LEU B O   1 
ATOM   6435 C CB  . LEU B 1 282 ? -45.284 44.028 42.573  1.00 18.75 ? 282 LEU B CB  1 
ATOM   6436 C CG  . LEU B 1 282 ? -45.485 44.008 44.091  1.00 19.87 ? 282 LEU B CG  1 
ATOM   6437 C CD1 . LEU B 1 282 ? -46.228 42.756 44.536  1.00 21.96 ? 282 LEU B CD1 1 
ATOM   6438 C CD2 . LEU B 1 282 ? -44.145 44.145 44.827  1.00 23.68 ? 282 LEU B CD2 1 
ATOM   6439 N N   . LYS B 1 283 ? -46.988 46.506 41.780  1.00 17.11 ? 283 LYS B N   1 
ATOM   6440 C CA  . LYS B 1 283 ? -47.722 47.703 42.179  1.00 22.13 ? 283 LYS B CA  1 
ATOM   6441 C C   . LYS B 1 283 ? -49.129 47.718 41.594  1.00 25.93 ? 283 LYS B C   1 
ATOM   6442 O O   . LYS B 1 283 ? -50.059 48.231 42.226  1.00 23.86 ? 283 LYS B O   1 
ATOM   6443 C CB  . LYS B 1 283 ? -46.940 48.949 41.768  1.00 25.02 ? 283 LYS B CB  1 
ATOM   6444 C CG  . LYS B 1 283 ? -45.629 49.089 42.536  1.00 30.83 ? 283 LYS B CG  1 
ATOM   6445 C CD  . LYS B 1 283 ? -44.616 49.973 41.825  1.00 37.29 ? 283 LYS B CD  1 
ATOM   6446 C CE  . LYS B 1 283 ? -45.116 51.396 41.656  1.00 51.60 ? 283 LYS B CE  1 
ATOM   6447 N NZ  . LYS B 1 283 ? -44.143 52.213 40.878  1.00 57.06 ? 283 LYS B NZ  1 
ATOM   6448 N N   . ASN B 1 284 ? -49.308 47.145 40.404  1.00 21.05 ? 284 ASN B N   1 
ATOM   6449 C CA  . ASN B 1 284 ? -50.631 47.065 39.797  1.00 24.89 ? 284 ASN B CA  1 
ATOM   6450 C C   . ASN B 1 284 ? -51.514 46.016 40.453  1.00 20.69 ? 284 ASN B C   1 
ATOM   6451 O O   . ASN B 1 284 ? -52.732 46.032 40.239  1.00 24.02 ? 284 ASN B O   1 
ATOM   6452 C CB  . ASN B 1 284 ? -50.520 46.725 38.307  1.00 21.85 ? 284 ASN B CB  1 
ATOM   6453 C CG  . ASN B 1 284 ? -50.060 47.889 37.470  1.00 25.59 ? 284 ASN B CG  1 
ATOM   6454 O OD1 . ASN B 1 284 ? -50.073 49.040 37.911  1.00 27.77 ? 284 ASN B OD1 1 
ATOM   6455 N ND2 . ASN B 1 284 ? -49.665 47.602 36.242  1.00 28.63 ? 284 ASN B ND2 1 
ATOM   6456 N N   . SER B 1 285 ? -50.926 45.098 41.222  1.00 18.30 ? 285 SER B N   1 
ATOM   6457 C CA  . SER B 1 285 ? -51.620 43.911 41.708  1.00 21.61 ? 285 SER B CA  1 
ATOM   6458 C C   . SER B 1 285 ? -51.827 43.893 43.212  1.00 26.05 ? 285 SER B C   1 
ATOM   6459 O O   . SER B 1 285 ? -52.803 43.305 43.677  1.00 29.10 ? 285 SER B O   1 
ATOM   6460 C CB  . SER B 1 285 ? -50.846 42.647 41.307  1.00 24.29 ? 285 SER B CB  1 
ATOM   6461 O OG  . SER B 1 285 ? -50.523 42.653 39.924  1.00 24.39 ? 285 SER B OG  1 
ATOM   6462 N N   . VAL B 1 286 ? -50.931 44.517 43.974  1.00 21.72 ? 286 VAL B N   1 
ATOM   6463 C CA  . VAL B 1 286 ? -50.928 44.478 45.433  1.00 24.84 ? 286 VAL B CA  1 
ATOM   6464 C C   . VAL B 1 286 ? -50.807 45.908 45.942  1.00 29.34 ? 286 VAL B C   1 
ATOM   6465 O O   . VAL B 1 286 ? -49.968 46.674 45.454  1.00 32.75 ? 286 VAL B O   1 
ATOM   6466 C CB  . VAL B 1 286 ? -49.764 43.617 45.968  1.00 24.77 ? 286 VAL B CB  1 
ATOM   6467 C CG1 . VAL B 1 286 ? -49.799 43.538 47.488  1.00 31.94 ? 286 VAL B CG1 1 
ATOM   6468 C CG2 . VAL B 1 286 ? -49.800 42.228 45.345  1.00 25.77 ? 286 VAL B CG2 1 
ATOM   6469 N N   . GLU B 1 287 ? -51.621 46.259 46.939  1.00 26.82 ? 287 GLU B N   1 
ATOM   6470 C CA  . GLU B 1 287 ? -51.631 47.628 47.450  1.00 33.06 ? 287 GLU B CA  1 
ATOM   6471 C C   . GLU B 1 287 ? -50.332 47.967 48.173  1.00 37.24 ? 287 GLU B C   1 
ATOM   6472 O O   . GLU B 1 287 ? -49.628 48.912 47.799  1.00 39.43 ? 287 GLU B O   1 
ATOM   6473 C CB  . GLU B 1 287 ? -52.825 47.821 48.373  1.00 35.83 ? 287 GLU B CB  1 
ATOM   6474 C CG  . GLU B 1 287 ? -54.132 47.766 47.645  1.00 46.16 ? 287 GLU B CG  1 
ATOM   6475 C CD  . GLU B 1 287 ? -55.110 48.724 48.233  1.00 59.61 ? 287 GLU B CD  1 
ATOM   6476 O OE1 . GLU B 1 287 ? -54.886 49.121 49.394  1.00 64.11 ? 287 GLU B OE1 1 
ATOM   6477 O OE2 . GLU B 1 287 ? -56.082 49.089 47.541  1.00 66.46 ? 287 GLU B OE2 1 
ATOM   6478 N N   . ARG B 1 288 ? -50.013 47.223 49.229  1.00 33.49 ? 288 ARG B N   1 
ATOM   6479 C CA  . ARG B 1 288 ? -48.752 47.396 49.946  1.00 40.41 ? 288 ARG B CA  1 
ATOM   6480 C C   . ARG B 1 288 ? -47.714 46.561 49.220  1.00 39.93 ? 288 ARG B C   1 
ATOM   6481 O O   . ARG B 1 288 ? -47.510 45.384 49.513  1.00 52.19 ? 288 ARG B O   1 
ATOM   6482 C CB  . ARG B 1 288 ? -48.888 46.987 51.403  1.00 45.37 ? 288 ARG B CB  1 
ATOM   6483 C CG  . ARG B 1 288 ? -49.732 47.932 52.203  1.00 42.56 ? 288 ARG B CG  1 
ATOM   6484 C CD  . ARG B 1 288 ? -49.761 47.516 53.642  1.00 45.70 ? 288 ARG B CD  1 
ATOM   6485 N NE  . ARG B 1 288 ? -50.660 46.394 53.872  1.00 46.29 ? 288 ARG B NE  1 
ATOM   6486 C CZ  . ARG B 1 288 ? -51.948 46.529 54.161  1.00 43.18 ? 288 ARG B CZ  1 
ATOM   6487 N NH1 . ARG B 1 288 ? -52.697 45.451 54.359  1.00 49.57 ? 288 ARG B NH1 1 
ATOM   6488 N NH2 . ARG B 1 288 ? -52.485 47.743 54.245  1.00 40.02 ? 288 ARG B NH2 1 
ATOM   6489 N N   . ALA B 1 289 ? -47.050 47.182 48.255  1.00 31.28 ? 289 ALA B N   1 
ATOM   6490 C CA  . ALA B 1 289 ? -46.247 46.455 47.281  1.00 33.05 ? 289 ALA B CA  1 
ATOM   6491 C C   . ALA B 1 289 ? -44.764 46.612 47.608  1.00 27.97 ? 289 ALA B C   1 
ATOM   6492 O O   . ALA B 1 289 ? -44.053 47.402 46.987  1.00 40.68 ? 289 ALA B O   1 
ATOM   6493 C CB  . ALA B 1 289 ? -46.570 46.951 45.877  1.00 42.09 ? 289 ALA B CB  1 
ATOM   6494 N N   . SER B 1 290 ? -44.277 45.820 48.571  1.00 20.60 ? 290 SER B N   1 
ATOM   6495 C CA  . SER B 1 290 ? -42.832 45.771 48.801  1.00 18.43 ? 290 SER B CA  1 
ATOM   6496 C C   . SER B 1 290 ? -42.190 44.718 47.907  1.00 19.97 ? 290 SER B C   1 
ATOM   6497 O O   . SER B 1 290 ? -42.585 43.546 47.966  1.00 19.24 ? 290 SER B O   1 
ATOM   6498 C CB  . SER B 1 290 ? -42.489 45.467 50.246  1.00 18.35 ? 290 SER B CB  1 
ATOM   6499 O OG  . SER B 1 290 ? -41.070 45.287 50.355  1.00 17.61 ? 290 SER B OG  1 
ATOM   6500 N N   . PRO B 1 291 ? -41.191 45.077 47.101  1.00 17.52 ? 291 PRO B N   1 
ATOM   6501 C CA  . PRO B 1 291 ? -40.493 44.097 46.269  1.00 17.12 ? 291 PRO B CA  1 
ATOM   6502 C C   . PRO B 1 291 ? -39.458 43.265 47.012  1.00 16.00 ? 291 PRO B C   1 
ATOM   6503 O O   . PRO B 1 291 ? -38.770 42.456 46.384  1.00 17.25 ? 291 PRO B O   1 
ATOM   6504 C CB  . PRO B 1 291 ? -39.822 44.990 45.213  1.00 20.82 ? 291 PRO B CB  1 
ATOM   6505 C CG  . PRO B 1 291 ? -39.546 46.265 45.957  1.00 19.47 ? 291 PRO B CG  1 
ATOM   6506 C CD  . PRO B 1 291 ? -40.693 46.451 46.896  1.00 23.05 ? 291 PRO B CD  1 
ATOM   6507 N N   . TYR B 1 292 ? -39.345 43.403 48.329  1.00 13.91 ? 292 TYR B N   1 
ATOM   6508 C CA  . TYR B 1 292 ? -38.253 42.767 49.051  1.00 13.89 ? 292 TYR B CA  1 
ATOM   6509 C C   . TYR B 1 292 ? -38.676 41.488 49.752  1.00 14.11 ? 292 TYR B C   1 
ATOM   6510 O O   . TYR B 1 292 ? -37.892 40.936 50.530  1.00 16.25 ? 292 TYR B O   1 
ATOM   6511 C CB  . TYR B 1 292 ? -37.651 43.769 50.038  1.00 15.04 ? 292 TYR B CB  1 
ATOM   6512 C CG  . TYR B 1 292 ? -37.233 45.008 49.295  1.00 15.74 ? 292 TYR B CG  1 
ATOM   6513 C CD1 . TYR B 1 292 ? -36.519 44.898 48.109  1.00 17.12 ? 292 TYR B CD1 1 
ATOM   6514 C CD2 . TYR B 1 292 ? -37.607 46.278 49.727  1.00 22.66 ? 292 TYR B CD2 1 
ATOM   6515 C CE1 . TYR B 1 292 ? -36.150 46.009 47.384  1.00 20.30 ? 292 TYR B CE1 1 
ATOM   6516 C CE2 . TYR B 1 292 ? -37.242 47.410 48.998  1.00 22.52 ? 292 TYR B CE2 1 
ATOM   6517 C CZ  . TYR B 1 292 ? -36.509 47.259 47.824  1.00 22.24 ? 292 TYR B CZ  1 
ATOM   6518 O OH  . TYR B 1 292 ? -36.125 48.358 47.073  1.00 24.84 ? 292 TYR B OH  1 
ATOM   6519 N N   . LEU B 1 293 ? -39.883 40.996 49.466  1.00 15.60 ? 293 LEU B N   1 
ATOM   6520 C CA  . LEU B 1 293 ? -40.451 39.793 50.057  1.00 15.85 ? 293 LEU B CA  1 
ATOM   6521 C C   . LEU B 1 293 ? -40.412 38.644 49.058  1.00 15.24 ? 293 LEU B C   1 
ATOM   6522 O O   . LEU B 1 293 ? -40.426 38.853 47.838  1.00 15.92 ? 293 LEU B O   1 
ATOM   6523 C CB  . LEU B 1 293 ? -41.920 40.026 50.475  1.00 13.81 ? 293 LEU B CB  1 
ATOM   6524 C CG  . LEU B 1 293 ? -42.238 40.752 51.786  1.00 27.87 ? 293 LEU B CG  1 
ATOM   6525 C CD1 . LEU B 1 293 ? -41.571 42.100 51.855  1.00 30.12 ? 293 LEU B CD1 1 
ATOM   6526 C CD2 . LEU B 1 293 ? -43.746 40.898 51.945  1.00 32.98 ? 293 LEU B CD2 1 
ATOM   6527 N N   . ARG B 1 294 ? -40.392 37.419 49.576  1.00 12.78 ? 294 ARG B N   1 
ATOM   6528 C CA  . ARG B 1 294 ? -40.719 36.270 48.737  1.00 14.06 ? 294 ARG B CA  1 
ATOM   6529 C C   . ARG B 1 294 ? -42.233 36.096 48.712  1.00 12.77 ? 294 ARG B C   1 
ATOM   6530 O O   . ARG B 1 294 ? -42.855 35.927 49.765  1.00 16.00 ? 294 ARG B O   1 
ATOM   6531 C CB  . ARG B 1 294 ? -40.043 34.998 49.245  1.00 13.82 ? 294 ARG B CB  1 
ATOM   6532 C CG  . ARG B 1 294 ? -40.296 33.790 48.300  1.00 17.79 ? 294 ARG B CG  1 
ATOM   6533 C CD  . ARG B 1 294 ? -39.408 32.577 48.608  1.00 19.54 ? 294 ARG B CD  1 
ATOM   6534 N NE  . ARG B 1 294 ? -39.597 32.117 49.976  1.00 17.09 ? 294 ARG B NE  1 
ATOM   6535 C CZ  . ARG B 1 294 ? -38.615 31.970 50.858  1.00 19.09 ? 294 ARG B CZ  1 
ATOM   6536 N NH1 . ARG B 1 294 ? -37.356 32.226 50.522  1.00 18.74 ? 294 ARG B NH1 1 
ATOM   6537 N NH2 . ARG B 1 294 ? -38.892 31.558 52.084  1.00 20.82 ? 294 ARG B NH2 1 
ATOM   6538 N N   . TYR B 1 295 ? -42.828 36.125 47.520  1.00 15.21 ? 295 TYR B N   1 
ATOM   6539 C CA  . TYR B 1 295 ? -44.273 35.986 47.381  1.00 15.85 ? 295 TYR B CA  1 
ATOM   6540 C C   . TYR B 1 295 ? -44.651 34.557 47.002  1.00 16.53 ? 295 TYR B C   1 
ATOM   6541 O O   . TYR B 1 295 ? -43.891 33.852 46.340  1.00 17.05 ? 295 TYR B O   1 
ATOM   6542 C CB  . TYR B 1 295 ? -44.816 36.963 46.338  1.00 18.43 ? 295 TYR B CB  1 
ATOM   6543 C CG  . TYR B 1 295 ? -44.851 38.389 46.840  1.00 13.71 ? 295 TYR B CG  1 
ATOM   6544 C CD1 . TYR B 1 295 ? -43.736 39.209 46.721  1.00 15.40 ? 295 TYR B CD1 1 
ATOM   6545 C CD2 . TYR B 1 295 ? -45.982 38.905 47.462  1.00 19.31 ? 295 TYR B CD2 1 
ATOM   6546 C CE1 . TYR B 1 295 ? -43.750 40.509 47.191  1.00 14.67 ? 295 TYR B CE1 1 
ATOM   6547 C CE2 . TYR B 1 295 ? -46.008 40.214 47.937  1.00 18.91 ? 295 TYR B CE2 1 
ATOM   6548 C CZ  . TYR B 1 295 ? -44.893 41.009 47.802  1.00 15.68 ? 295 TYR B CZ  1 
ATOM   6549 O OH  . TYR B 1 295 ? -44.920 42.305 48.280  1.00 19.77 ? 295 TYR B OH  1 
ATOM   6550 N N   . TYR B 1 296 ? -45.840 34.136 47.436  1.00 15.07 ? 296 TYR B N   1 
ATOM   6551 C CA  . TYR B 1 296 ? -46.399 32.834 47.090  1.00 14.66 ? 296 TYR B CA  1 
ATOM   6552 C C   . TYR B 1 296 ? -47.715 33.084 46.372  1.00 16.78 ? 296 TYR B C   1 
ATOM   6553 O O   . TYR B 1 296 ? -48.686 33.542 46.986  1.00 17.17 ? 296 TYR B O   1 
ATOM   6554 C CB  . TYR B 1 296 ? -46.612 31.968 48.331  1.00 14.97 ? 296 TYR B CB  1 
ATOM   6555 C CG  . TYR B 1 296 ? -45.355 31.714 49.124  1.00 15.10 ? 296 TYR B CG  1 
ATOM   6556 C CD1 . TYR B 1 296 ? -44.200 31.261 48.508  1.00 18.98 ? 296 TYR B CD1 1 
ATOM   6557 C CD2 . TYR B 1 296 ? -45.329 31.917 50.498  1.00 18.62 ? 296 TYR B CD2 1 
ATOM   6558 C CE1 . TYR B 1 296 ? -43.043 31.022 49.246  1.00 19.15 ? 296 TYR B CE1 1 
ATOM   6559 C CE2 . TYR B 1 296 ? -44.186 31.685 51.235  1.00 16.56 ? 296 TYR B CE2 1 
ATOM   6560 C CZ  . TYR B 1 296 ? -43.053 31.234 50.609  1.00 19.00 ? 296 TYR B CZ  1 
ATOM   6561 O OH  . TYR B 1 296 ? -41.920 31.006 51.349  1.00 24.88 ? 296 TYR B OH  1 
ATOM   6562 N N   . PHE B 1 297 ? -47.753 32.787 45.078  1.00 15.55 ? 297 PHE B N   1 
ATOM   6563 C CA  . PHE B 1 297 ? -48.971 33.003 44.307  1.00 15.74 ? 297 PHE B CA  1 
ATOM   6564 C C   . PHE B 1 297 ? -49.919 31.841 44.577  1.00 18.02 ? 297 PHE B C   1 
ATOM   6565 O O   . PHE B 1 297 ? -49.685 30.724 44.111  1.00 17.24 ? 297 PHE B O   1 
ATOM   6566 C CB  . PHE B 1 297 ? -48.664 33.131 42.818  1.00 14.54 ? 297 PHE B CB  1 
ATOM   6567 C CG  . PHE B 1 297 ? -49.895 33.296 41.979  1.00 15.28 ? 297 PHE B CG  1 
ATOM   6568 C CD1 . PHE B 1 297 ? -50.540 34.515 41.922  1.00 18.54 ? 297 PHE B CD1 1 
ATOM   6569 C CD2 . PHE B 1 297 ? -50.428 32.220 41.273  1.00 17.46 ? 297 PHE B CD2 1 
ATOM   6570 C CE1 . PHE B 1 297 ? -51.683 34.675 41.168  1.00 17.77 ? 297 PHE B CE1 1 
ATOM   6571 C CE2 . PHE B 1 297 ? -51.573 32.365 40.512  1.00 19.44 ? 297 PHE B CE2 1 
ATOM   6572 C CZ  . PHE B 1 297 ? -52.205 33.601 40.457  1.00 19.88 ? 297 PHE B CZ  1 
ATOM   6573 N N   . ARG B 1 298 ? -50.972 32.103 45.357  1.00 16.72 ? 298 ARG B N   1 
ATOM   6574 C CA  . ARG B 1 298 ? -51.983 31.088 45.699  1.00 17.54 ? 298 ARG B CA  1 
ATOM   6575 C C   . ARG B 1 298 ? -51.360 29.843 46.330  1.00 18.78 ? 298 ARG B C   1 
ATOM   6576 O O   . ARG B 1 298 ? -51.927 28.751 46.253  1.00 19.49 ? 298 ARG B O   1 
ATOM   6577 C CB  . ARG B 1 298 ? -52.819 30.707 44.476  1.00 18.07 ? 298 ARG B CB  1 
ATOM   6578 C CG  . ARG B 1 298 ? -53.489 31.906 43.837  1.00 20.44 ? 298 ARG B CG  1 
ATOM   6579 C CD  . ARG B 1 298 ? -54.440 31.527 42.699  1.00 22.27 ? 298 ARG B CD  1 
ATOM   6580 N NE  . ARG B 1 298 ? -55.033 32.737 42.143  1.00 21.67 ? 298 ARG B NE  1 
ATOM   6581 C CZ  . ARG B 1 298 ? -55.610 32.829 40.953  1.00 22.43 ? 298 ARG B CZ  1 
ATOM   6582 N NH1 . ARG B 1 298 ? -55.705 31.765 40.154  1.00 23.19 ? 298 ARG B NH1 1 
ATOM   6583 N NH2 . ARG B 1 298 ? -56.093 33.999 40.559  1.00 20.52 ? 298 ARG B NH2 1 
ATOM   6584 N N   . GLU B 1 299 ? -50.198 30.010 46.967  1.00 17.86 ? 299 GLU B N   1 
ATOM   6585 C CA  . GLU B 1 299 ? -49.434 28.929 47.594  1.00 22.17 ? 299 GLU B CA  1 
ATOM   6586 C C   . GLU B 1 299 ? -48.993 27.869 46.591  1.00 20.25 ? 299 GLU B C   1 
ATOM   6587 O O   . GLU B 1 299 ? -48.643 26.747 46.977  1.00 26.78 ? 299 GLU B O   1 
ATOM   6588 C CB  . GLU B 1 299 ? -50.211 28.273 48.744  1.00 19.46 ? 299 GLU B CB  1 
ATOM   6589 C CG  . GLU B 1 299 ? -50.487 29.185 49.925  1.00 19.84 ? 299 GLU B CG  1 
ATOM   6590 C CD  . GLU B 1 299 ? -49.258 29.462 50.776  1.00 25.23 ? 299 GLU B CD  1 
ATOM   6591 O OE1 . GLU B 1 299 ? -48.121 29.196 50.321  1.00 23.66 ? 299 GLU B OE1 1 
ATOM   6592 O OE2 . GLU B 1 299 ? -49.430 29.956 51.914  1.00 26.12 ? 299 GLU B OE2 1 
ATOM   6593 N N   . LEU B 1 300 ? -48.975 28.212 45.306  1.00 16.76 ? 300 LEU B N   1 
ATOM   6594 C CA  . LEU B 1 300 ? -48.649 27.268 44.247  1.00 17.44 ? 300 LEU B CA  1 
ATOM   6595 C C   . LEU B 1 300 ? -47.258 27.471 43.678  1.00 17.38 ? 300 LEU B C   1 
ATOM   6596 O O   . LEU B 1 300 ? -46.609 26.499 43.280  1.00 22.10 ? 300 LEU B O   1 
ATOM   6597 C CB  . LEU B 1 300 ? -49.659 27.374 43.105  1.00 22.72 ? 300 LEU B CB  1 
ATOM   6598 C CG  . LEU B 1 300 ? -51.123 27.171 43.458  1.00 27.77 ? 300 LEU B CG  1 
ATOM   6599 C CD1 . LEU B 1 300 ? -51.959 27.338 42.189  1.00 28.18 ? 300 LEU B CD1 1 
ATOM   6600 C CD2 . LEU B 1 300 ? -51.324 25.809 44.082  1.00 26.89 ? 300 LEU B CD2 1 
ATOM   6601 N N   . ILE B 1 301 ? -46.789 28.710 43.599  1.00 16.25 ? 301 ILE B N   1 
ATOM   6602 C CA  . ILE B 1 301 ? -45.505 28.978 42.968  1.00 14.65 ? 301 ILE B CA  1 
ATOM   6603 C C   . ILE B 1 301 ? -44.912 30.209 43.635  1.00 13.85 ? 301 ILE B C   1 
ATOM   6604 O O   . ILE B 1 301 ? -45.636 31.135 44.014  1.00 16.29 ? 301 ILE B O   1 
ATOM   6605 C CB  . ILE B 1 301 ? -45.664 29.135 41.433  1.00 18.39 ? 301 ILE B CB  1 
ATOM   6606 C CG1 . ILE B 1 301 ? -44.296 29.293 40.752  1.00 16.80 ? 301 ILE B CG1 1 
ATOM   6607 C CG2 . ILE B 1 301 ? -46.635 30.273 41.077  1.00 17.01 ? 301 ILE B CG2 1 
ATOM   6608 C CD1 . ILE B 1 301 ? -44.366 29.286 39.218  1.00 21.92 ? 301 ILE B CD1 1 
ATOM   6609 N N   . SER B 1 302 ? -43.593 30.204 43.819  1.00 15.48 ? 302 SER B N   1 
ATOM   6610 C CA  . SER B 1 302 ? -42.924 31.327 44.461  1.00 15.92 ? 302 SER B CA  1 
ATOM   6611 C C   . SER B 1 302 ? -42.607 32.385 43.412  1.00 19.02 ? 302 SER B C   1 
ATOM   6612 O O   . SER B 1 302 ? -42.241 32.062 42.278  1.00 16.86 ? 302 SER B O   1 
ATOM   6613 C CB  . SER B 1 302 ? -41.655 30.858 45.172  1.00 15.71 ? 302 SER B CB  1 
ATOM   6614 O OG  . SER B 1 302 ? -41.978 29.868 46.142  1.00 19.51 ? 302 SER B OG  1 
ATOM   6615 N N   . VAL B 1 303 ? -42.785 33.651 43.786  1.00 13.99 ? 303 VAL B N   1 
ATOM   6616 C CA  . VAL B 1 303 ? -42.634 34.778 42.869  1.00 13.63 ? 303 VAL B CA  1 
ATOM   6617 C C   . VAL B 1 303 ? -41.824 35.858 43.562  1.00 18.39 ? 303 VAL B C   1 
ATOM   6618 O O   . VAL B 1 303 ? -42.157 36.272 44.677  1.00 16.64 ? 303 VAL B O   1 
ATOM   6619 C CB  . VAL B 1 303 ? -43.993 35.360 42.417  1.00 13.42 ? 303 VAL B CB  1 
ATOM   6620 C CG1 . VAL B 1 303 ? -43.774 36.535 41.470  1.00 20.12 ? 303 VAL B CG1 1 
ATOM   6621 C CG2 . VAL B 1 303 ? -44.844 34.283 41.744  1.00 16.06 ? 303 VAL B CG2 1 
ATOM   6622 N N   . PHE B 1 304 ? -40.770 36.322 42.903  1.00 13.64 ? 304 PHE B N   1 
ATOM   6623 C CA  . PHE B 1 304 ? -40.083 37.531 43.320  1.00 11.45 ? 304 PHE B CA  1 
ATOM   6624 C C   . PHE B 1 304 ? -40.324 38.623 42.292  1.00 13.82 ? 304 PHE B C   1 
ATOM   6625 O O   . PHE B 1 304 ? -40.416 38.358 41.092  1.00 16.11 ? 304 PHE B O   1 
ATOM   6626 C CB  . PHE B 1 304 ? -38.570 37.307 43.458  1.00 12.44 ? 304 PHE B CB  1 
ATOM   6627 C CG  . PHE B 1 304 ? -38.172 36.540 44.688  1.00 13.23 ? 304 PHE B CG  1 
ATOM   6628 C CD1 . PHE B 1 304 ? -38.070 37.180 45.911  1.00 14.53 ? 304 PHE B CD1 1 
ATOM   6629 C CD2 . PHE B 1 304 ? -37.848 35.186 44.608  1.00 14.48 ? 304 PHE B CD2 1 
ATOM   6630 C CE1 . PHE B 1 304 ? -37.679 36.475 47.045  1.00 15.27 ? 304 PHE B CE1 1 
ATOM   6631 C CE2 . PHE B 1 304 ? -37.453 34.485 45.731  1.00 14.27 ? 304 PHE B CE2 1 
ATOM   6632 C CZ  . PHE B 1 304 ? -37.367 35.132 46.953  1.00 15.71 ? 304 PHE B CZ  1 
ATOM   6633 N N   . PHE B 1 305 ? -40.406 39.852 42.771  1.00 15.32 ? 305 PHE B N   1 
ATOM   6634 C CA  . PHE B 1 305 ? -40.566 41.016 41.914  1.00 13.39 ? 305 PHE B CA  1 
ATOM   6635 C C   . PHE B 1 305 ? -39.254 41.782 41.921  1.00 14.64 ? 305 PHE B C   1 
ATOM   6636 O O   . PHE B 1 305 ? -38.756 42.151 42.992  1.00 16.36 ? 305 PHE B O   1 
ATOM   6637 C CB  . PHE B 1 305 ? -41.725 41.883 42.398  1.00 12.79 ? 305 PHE B CB  1 
ATOM   6638 C CG  . PHE B 1 305 ? -43.050 41.157 42.385  1.00 18.61 ? 305 PHE B CG  1 
ATOM   6639 C CD1 . PHE B 1 305 ? -43.435 40.372 43.460  1.00 16.93 ? 305 PHE B CD1 1 
ATOM   6640 C CD2 . PHE B 1 305 ? -43.870 41.211 41.273  1.00 14.45 ? 305 PHE B CD2 1 
ATOM   6641 C CE1 . PHE B 1 305 ? -44.641 39.666 43.437  1.00 18.36 ? 305 PHE B CE1 1 
ATOM   6642 C CE2 . PHE B 1 305 ? -45.088 40.526 41.247  1.00 16.90 ? 305 PHE B CE2 1 
ATOM   6643 C CZ  . PHE B 1 305 ? -45.465 39.743 42.335  1.00 17.90 ? 305 PHE B CZ  1 
ATOM   6644 N N   . ARG B 1 306 ? -38.694 42.010 40.738  1.00 13.10 ? 306 ARG B N   1 
ATOM   6645 C CA  . ARG B 1 306 ? -37.388 42.648 40.662  1.00 14.05 ? 306 ARG B CA  1 
ATOM   6646 C C   . ARG B 1 306 ? -37.463 44.092 41.137  1.00 16.61 ? 306 ARG B C   1 
ATOM   6647 O O   . ARG B 1 306 ? -38.505 44.753 41.063  1.00 16.31 ? 306 ARG B O   1 
ATOM   6648 C CB  . ARG B 1 306 ? -36.844 42.586 39.232  1.00 12.13 ? 306 ARG B CB  1 
ATOM   6649 C CG  . ARG B 1 306 ? -37.539 43.534 38.306  1.00 16.92 ? 306 ARG B CG  1 
ATOM   6650 C CD  . ARG B 1 306 ? -36.924 43.547 36.914  1.00 17.51 ? 306 ARG B CD  1 
ATOM   6651 N NE  . ARG B 1 306 ? -37.594 44.610 36.200  1.00 20.29 ? 306 ARG B NE  1 
ATOM   6652 C CZ  . ARG B 1 306 ? -37.058 45.362 35.258  1.00 18.73 ? 306 ARG B CZ  1 
ATOM   6653 N NH1 . ARG B 1 306 ? -35.805 45.184 34.852  1.00 18.24 ? 306 ARG B NH1 1 
ATOM   6654 N NH2 . ARG B 1 306 ? -37.800 46.309 34.730  1.00 20.40 ? 306 ARG B NH2 1 
ATOM   6655 N N   . ASP B 1 307 ? -36.342 44.572 41.662  1.00 15.14 ? 307 ASP B N   1 
ATOM   6656 C CA  . ASP B 1 307 ? -36.214 45.982 42.003  1.00 14.43 ? 307 ASP B CA  1 
ATOM   6657 C C   . ASP B 1 307 ? -35.988 46.698 40.682  1.00 15.07 ? 307 ASP B C   1 
ATOM   6658 O O   . ASP B 1 307 ? -34.900 46.655 40.117  1.00 13.73 ? 307 ASP B O   1 
ATOM   6659 C CB  . ASP B 1 307 ? -35.074 46.215 42.990  1.00 16.85 ? 307 ASP B CB  1 
ATOM   6660 C CG  . ASP B 1 307 ? -34.991 47.672 43.448  1.00 19.95 ? 307 ASP B CG  1 
ATOM   6661 O OD1 . ASP B 1 307 ? -35.056 48.561 42.584  1.00 17.51 ? 307 ASP B OD1 1 
ATOM   6662 O OD2 . ASP B 1 307 ? -34.866 47.935 44.662  1.00 20.98 ? 307 ASP B OD2 1 
ATOM   6663 N N   . LYS B 1 308 ? -37.027 47.352 40.179  1.00 15.26 ? 308 LYS B N   1 
ATOM   6664 C CA  . LYS B 1 308 ? -36.941 47.923 38.843  1.00 16.34 ? 308 LYS B CA  1 
ATOM   6665 C C   . LYS B 1 308 ? -35.916 49.050 38.786  1.00 15.14 ? 308 LYS B C   1 
ATOM   6666 O O   . LYS B 1 308 ? -35.211 49.207 37.784  1.00 15.27 ? 308 LYS B O   1 
ATOM   6667 C CB  . LYS B 1 308 ? -38.320 48.407 38.410  1.00 13.12 ? 308 LYS B CB  1 
ATOM   6668 C CG  . LYS B 1 308 ? -38.319 49.313 37.208  1.00 18.44 ? 308 LYS B CG  1 
ATOM   6669 C CD  . LYS B 1 308 ? -39.746 49.686 36.853  1.00 21.96 ? 308 LYS B CD  1 
ATOM   6670 C CE  . LYS B 1 308 ? -39.810 50.808 35.825  1.00 30.58 ? 308 LYS B CE  1 
ATOM   6671 N NZ  . LYS B 1 308 ? -39.201 50.407 34.535  1.00 27.08 ? 308 LYS B NZ  1 
ATOM   6672 N N   . THR B 1 309 ? -35.824 49.856 39.844  1.00 13.13 ? 309 THR B N   1 
ATOM   6673 C CA  . THR B 1 309 ? -34.882 50.968 39.826  1.00 14.61 ? 309 THR B CA  1 
ATOM   6674 C C   . THR B 1 309 ? -33.453 50.465 39.704  1.00 16.04 ? 309 THR B C   1 
ATOM   6675 O O   . THR B 1 309 ? -32.691 50.928 38.849  1.00 17.73 ? 309 THR B O   1 
ATOM   6676 C CB  . THR B 1 309 ? -35.036 51.813 41.087  1.00 16.69 ? 309 THR B CB  1 
ATOM   6677 O OG1 . THR B 1 309 ? -36.315 52.440 41.063  1.00 21.49 ? 309 THR B OG1 1 
ATOM   6678 C CG2 . THR B 1 309 ? -33.946 52.893 41.148  1.00 21.97 ? 309 THR B CG2 1 
ATOM   6679 N N   . LEU B 1 310 ? -33.072 49.518 40.559  1.00 14.75 ? 310 LEU B N   1 
ATOM   6680 C CA  . LEU B 1 310 ? -31.703 49.012 40.522  1.00 12.47 ? 310 LEU B CA  1 
ATOM   6681 C C   . LEU B 1 310 ? -31.412 48.316 39.202  1.00 14.80 ? 310 LEU B C   1 
ATOM   6682 O O   . LEU B 1 310 ? -30.308 48.433 38.666  1.00 15.10 ? 310 LEU B O   1 
ATOM   6683 C CB  . LEU B 1 310 ? -31.463 48.050 41.678  1.00 15.74 ? 310 LEU B CB  1 
ATOM   6684 C CG  . LEU B 1 310 ? -31.517 48.695 43.065  1.00 18.55 ? 310 LEU B CG  1 
ATOM   6685 C CD1 . LEU B 1 310 ? -31.298 47.633 44.116  1.00 19.80 ? 310 LEU B CD1 1 
ATOM   6686 C CD2 . LEU B 1 310 ? -30.475 49.784 43.182  1.00 17.73 ? 310 LEU B CD2 1 
ATOM   6687 N N   . SER B 1 311 ? -32.391 47.577 38.681  1.00 14.60 ? 311 SER B N   1 
ATOM   6688 C CA  . SER B 1 311 ? -32.218 46.875 37.415  1.00 13.51 ? 311 SER B CA  1 
ATOM   6689 C C   . SER B 1 311 ? -32.069 47.862 36.262  1.00 15.91 ? 311 SER B C   1 
ATOM   6690 O O   . SER B 1 311 ? -31.239 47.663 35.365  1.00 18.61 ? 311 SER B O   1 
ATOM   6691 C CB  . SER B 1 311 ? -33.409 45.954 37.177  1.00 14.20 ? 311 SER B CB  1 
ATOM   6692 O OG  . SER B 1 311 ? -33.572 45.015 38.243  1.00 14.59 ? 311 SER B OG  1 
ATOM   6693 N N   . ASP B 1 312 ? -32.894 48.912 36.254  1.00 14.81 ? 312 ASP B N   1 
ATOM   6694 C CA  . ASP B 1 312 ? -32.788 49.917 35.201  1.00 16.06 ? 312 ASP B CA  1 
ATOM   6695 C C   . ASP B 1 312 ? -31.497 50.711 35.316  1.00 16.40 ? 312 ASP B C   1 
ATOM   6696 O O   . ASP B 1 312 ? -30.968 51.180 34.303  1.00 15.39 ? 312 ASP B O   1 
ATOM   6697 C CB  . ASP B 1 312 ? -33.979 50.874 35.249  1.00 17.16 ? 312 ASP B CB  1 
ATOM   6698 C CG  . ASP B 1 312 ? -35.242 50.273 34.663  1.00 17.51 ? 312 ASP B CG  1 
ATOM   6699 O OD1 . ASP B 1 312 ? -35.164 49.240 33.972  1.00 21.28 ? 312 ASP B OD1 1 
ATOM   6700 O OD2 . ASP B 1 312 ? -36.327 50.844 34.904  1.00 22.02 ? 312 ASP B OD2 1 
ATOM   6701 N N   . LEU B 1 313 ? -30.996 50.911 36.537  1.00 17.58 ? 313 LEU B N   1 
ATOM   6702 C CA  . LEU B 1 313 ? -29.771 51.685 36.690  1.00 15.29 ? 313 LEU B CA  1 
ATOM   6703 C C   . LEU B 1 313 ? -28.620 51.009 35.954  1.00 16.99 ? 313 LEU B C   1 
ATOM   6704 O O   . LEU B 1 313 ? -27.885 51.655 35.196  1.00 15.09 ? 313 LEU B O   1 
ATOM   6705 C CB  . LEU B 1 313 ? -29.441 51.876 38.170  1.00 14.06 ? 313 LEU B CB  1 
ATOM   6706 C CG  . LEU B 1 313 ? -30.227 53.002 38.863  1.00 18.43 ? 313 LEU B CG  1 
ATOM   6707 C CD1 . LEU B 1 313 ? -30.163 52.837 40.362  1.00 21.23 ? 313 LEU B CD1 1 
ATOM   6708 C CD2 . LEU B 1 313 ? -29.765 54.387 38.461  1.00 21.98 ? 313 LEU B CD2 1 
ATOM   6709 N N   . ILE B 1 314 ? -28.457 49.701 36.148  1.00 13.29 ? 314 ILE B N   1 
ATOM   6710 C CA  . ILE B 1 314 ? -27.407 49.003 35.413  1.00 16.08 ? 314 ILE B CA  1 
ATOM   6711 C C   . ILE B 1 314 ? -27.761 48.925 33.936  1.00 15.94 ? 314 ILE B C   1 
ATOM   6712 O O   . ILE B 1 314 ? -26.918 49.170 33.067  1.00 15.79 ? 314 ILE B O   1 
ATOM   6713 C CB  . ILE B 1 314 ? -27.177 47.604 36.003  1.00 12.89 ? 314 ILE B CB  1 
ATOM   6714 C CG1 . ILE B 1 314 ? -26.699 47.717 37.450  1.00 12.20 ? 314 ILE B CG1 1 
ATOM   6715 C CG2 . ILE B 1 314 ? -26.198 46.815 35.125  1.00 12.53 ? 314 ILE B CG2 1 
ATOM   6716 C CD1 . ILE B 1 314 ? -26.580 46.366 38.145  1.00 17.26 ? 314 ILE B CD1 1 
ATOM   6717 N N   . GLY B 1 315 ? -29.018 48.609 33.627  1.00 13.26 ? 315 GLY B N   1 
ATOM   6718 C CA  . GLY B 1 315 ? -29.372 48.308 32.250  1.00 14.97 ? 315 GLY B CA  1 
ATOM   6719 C C   . GLY B 1 315 ? -29.420 49.522 31.349  1.00 18.89 ? 315 GLY B C   1 
ATOM   6720 O O   . GLY B 1 315 ? -29.195 49.403 30.139  1.00 18.89 ? 315 GLY B O   1 
ATOM   6721 N N   . PHE B 1 316 ? -29.707 50.701 31.912  1.00 18.80 ? 316 PHE B N   1 
ATOM   6722 C CA  . PHE B 1 316 ? -29.890 51.898 31.088  1.00 19.12 ? 316 PHE B CA  1 
ATOM   6723 C C   . PHE B 1 316 ? -29.211 53.160 31.605  1.00 24.85 ? 316 PHE B C   1 
ATOM   6724 O O   . PHE B 1 316 ? -29.090 54.118 30.833  1.00 24.25 ? 316 PHE B O   1 
ATOM   6725 C CB  . PHE B 1 316 ? -31.387 52.196 30.914  1.00 21.76 ? 316 PHE B CB  1 
ATOM   6726 C CG  . PHE B 1 316 ? -32.147 51.081 30.276  1.00 29.23 ? 316 PHE B CG  1 
ATOM   6727 C CD1 . PHE B 1 316 ? -32.163 50.944 28.899  1.00 28.35 ? 316 PHE B CD1 1 
ATOM   6728 C CD2 . PHE B 1 316 ? -32.829 50.151 31.051  1.00 21.03 ? 316 PHE B CD2 1 
ATOM   6729 C CE1 . PHE B 1 316 ? -32.855 49.907 28.300  1.00 31.83 ? 316 PHE B CE1 1 
ATOM   6730 C CE2 . PHE B 1 316 ? -33.514 49.110 30.458  1.00 26.69 ? 316 PHE B CE2 1 
ATOM   6731 C CZ  . PHE B 1 316 ? -33.532 48.992 29.078  1.00 28.38 ? 316 PHE B CZ  1 
ATOM   6732 N N   . SER B 1 317 ? -28.777 53.226 32.865  1.00 19.44 ? 317 SER B N   1 
ATOM   6733 C CA  . SER B 1 317 ? -28.287 54.474 33.440  1.00 23.48 ? 317 SER B CA  1 
ATOM   6734 C C   . SER B 1 317 ? -26.767 54.576 33.494  1.00 20.79 ? 317 SER B C   1 
ATOM   6735 O O   . SER B 1 317 ? -26.196 55.557 33.014  1.00 19.06 ? 317 SER B O   1 
ATOM   6736 C CB  . SER B 1 317 ? -28.846 54.651 34.857  1.00 23.60 ? 317 SER B CB  1 
ATOM   6737 O OG  . SER B 1 317 ? -30.257 54.797 34.844  1.00 27.62 ? 317 SER B OG  1 
ATOM   6738 N N   . TYR B 1 318 ? -26.099 53.577 34.078  1.00 15.53 ? 318 TYR B N   1 
ATOM   6739 C CA  . TYR B 1 318 ? -24.722 53.731 34.524  1.00 16.01 ? 318 TYR B CA  1 
ATOM   6740 C C   . TYR B 1 318 ? -23.705 53.793 33.395  1.00 19.55 ? 318 TYR B C   1 
ATOM   6741 O O   . TYR B 1 318 ? -22.544 54.125 33.659  1.00 21.37 ? 318 TYR B O   1 
ATOM   6742 C CB  . TYR B 1 318 ? -24.364 52.585 35.463  1.00 15.58 ? 318 TYR B CB  1 
ATOM   6743 C CG  . TYR B 1 318 ? -24.969 52.684 36.842  1.00 18.18 ? 318 TYR B CG  1 
ATOM   6744 C CD1 . TYR B 1 318 ? -25.250 53.912 37.425  1.00 17.75 ? 318 TYR B CD1 1 
ATOM   6745 C CD2 . TYR B 1 318 ? -25.244 51.536 37.565  1.00 14.64 ? 318 TYR B CD2 1 
ATOM   6746 C CE1 . TYR B 1 318 ? -25.796 53.992 38.704  1.00 19.08 ? 318 TYR B CE1 1 
ATOM   6747 C CE2 . TYR B 1 318 ? -25.776 51.596 38.840  1.00 16.31 ? 318 TYR B CE2 1 
ATOM   6748 C CZ  . TYR B 1 318 ? -26.055 52.822 39.403  1.00 21.58 ? 318 TYR B CZ  1 
ATOM   6749 O OH  . TYR B 1 318 ? -26.587 52.843 40.665  1.00 18.28 ? 318 TYR B OH  1 
ATOM   6750 N N   . HIS B 1 319 ? -24.089 53.463 32.159  1.00 20.21 ? 319 HIS B N   1 
ATOM   6751 C CA  . HIS B 1 319 ? -23.201 53.758 31.042  1.00 16.65 ? 319 HIS B CA  1 
ATOM   6752 C C   . HIS B 1 319 ? -22.816 55.231 31.028  1.00 17.87 ? 319 HIS B C   1 
ATOM   6753 O O   . HIS B 1 319 ? -21.709 55.575 30.613  1.00 23.91 ? 319 HIS B O   1 
ATOM   6754 C CB  . HIS B 1 319 ? -23.854 53.397 29.713  1.00 18.98 ? 319 HIS B CB  1 
ATOM   6755 C CG  . HIS B 1 319 ? -24.914 54.365 29.290  1.00 18.36 ? 319 HIS B CG  1 
ATOM   6756 N ND1 . HIS B 1 319 ? -24.687 55.371 28.376  1.00 23.48 ? 319 HIS B ND1 1 
ATOM   6757 C CD2 . HIS B 1 319 ? -26.207 54.490 29.675  1.00 22.38 ? 319 HIS B CD2 1 
ATOM   6758 C CE1 . HIS B 1 319 ? -25.798 56.066 28.205  1.00 22.71 ? 319 HIS B CE1 1 
ATOM   6759 N NE2 . HIS B 1 319 ? -26.733 55.556 28.987  1.00 21.02 ? 319 HIS B NE2 1 
ATOM   6760 N N   . ALA B 1 320 ? -23.708 56.106 31.497  1.00 18.98 ? 320 ALA B N   1 
ATOM   6761 C CA  . ALA B 1 320 ? -23.500 57.550 31.488  1.00 23.02 ? 320 ALA B CA  1 
ATOM   6762 C C   . ALA B 1 320 ? -22.769 58.058 32.725  1.00 24.86 ? 320 ALA B C   1 
ATOM   6763 O O   . ALA B 1 320 ? -22.651 59.276 32.905  1.00 26.05 ? 320 ALA B O   1 
ATOM   6764 C CB  . ALA B 1 320 ? -24.847 58.269 31.352  1.00 23.58 ? 320 ALA B CB  1 
ATOM   6765 N N   . TRP B 1 321 ? -22.280 57.157 33.574  1.00 23.62 ? 321 TRP B N   1 
ATOM   6766 C CA  . TRP B 1 321 ? -21.592 57.494 34.809  1.00 27.24 ? 321 TRP B CA  1 
ATOM   6767 C C   . TRP B 1 321 ? -20.163 56.977 34.765  1.00 26.45 ? 321 TRP B C   1 
ATOM   6768 O O   . TRP B 1 321 ? -19.850 56.008 34.070  1.00 25.11 ? 321 TRP B O   1 
ATOM   6769 C CB  . TRP B 1 321 ? -22.265 56.858 36.025  1.00 22.89 ? 321 TRP B CB  1 
ATOM   6770 C CG  . TRP B 1 321 ? -23.686 57.199 36.299  1.00 22.54 ? 321 TRP B CG  1 
ATOM   6771 C CD1 . TRP B 1 321 ? -24.722 57.216 35.420  1.00 20.50 ? 321 TRP B CD1 1 
ATOM   6772 C CD2 . TRP B 1 321 ? -24.236 57.522 37.582  1.00 25.54 ? 321 TRP B CD2 1 
ATOM   6773 N NE1 . TRP B 1 321 ? -25.895 57.536 36.078  1.00 31.03 ? 321 TRP B NE1 1 
ATOM   6774 C CE2 . TRP B 1 321 ? -25.616 57.734 37.405  1.00 29.67 ? 321 TRP B CE2 1 
ATOM   6775 C CE3 . TRP B 1 321 ? -23.690 57.655 38.863  1.00 28.52 ? 321 TRP B CE3 1 
ATOM   6776 C CZ2 . TRP B 1 321 ? -26.456 58.076 38.458  1.00 33.83 ? 321 TRP B CZ2 1 
ATOM   6777 C CZ3 . TRP B 1 321 ? -24.527 57.997 39.906  1.00 28.31 ? 321 TRP B CZ3 1 
ATOM   6778 C CH2 . TRP B 1 321 ? -25.893 58.201 39.699  1.00 27.35 ? 321 TRP B CH2 1 
ATOM   6779 N N   . ASN B 1 322 ? -19.296 57.594 35.558  1.00 29.13 ? 322 ASN B N   1 
ATOM   6780 C CA  . ASN B 1 322 ? -18.018 56.950 35.812  1.00 32.70 ? 322 ASN B CA  1 
ATOM   6781 C C   . ASN B 1 322 ? -18.239 55.750 36.729  1.00 27.27 ? 322 ASN B C   1 
ATOM   6782 O O   . ASN B 1 322 ? -19.150 55.741 37.559  1.00 33.44 ? 322 ASN B O   1 
ATOM   6783 C CB  . ASN B 1 322 ? -17.030 57.934 36.434  1.00 50.02 ? 322 ASN B CB  1 
ATOM   6784 C CG  . ASN B 1 322 ? -15.964 57.241 37.251  1.00 61.54 ? 322 ASN B CG  1 
ATOM   6785 O OD1 . ASN B 1 322 ? -14.949 56.798 36.717  1.00 70.70 ? 322 ASN B OD1 1 
ATOM   6786 N ND2 . ASN B 1 322 ? -16.188 57.144 38.555  1.00 57.97 ? 322 ASN B ND2 1 
ATOM   6787 N N   . ALA B 1 323 ? -17.393 54.729 36.562  1.00 27.07 ? 323 ALA B N   1 
ATOM   6788 C CA  . ALA B 1 323 ? -17.616 53.436 37.216  1.00 27.15 ? 323 ALA B CA  1 
ATOM   6789 C C   . ALA B 1 323 ? -17.615 53.558 38.735  1.00 29.33 ? 323 ALA B C   1 
ATOM   6790 O O   . ALA B 1 323 ? -18.487 53.003 39.413  1.00 23.26 ? 323 ALA B O   1 
ATOM   6791 C CB  . ALA B 1 323 ? -16.555 52.435 36.766  1.00 30.45 ? 323 ALA B CB  1 
ATOM   6792 N N   . GLU B 1 324 ? -16.616 54.253 39.292  1.00 28.08 ? 324 GLU B N   1 
ATOM   6793 C CA  . GLU B 1 324 ? -16.547 54.427 40.741  1.00 25.42 ? 324 GLU B CA  1 
ATOM   6794 C C   . GLU B 1 324 ? -17.820 55.067 41.277  1.00 30.43 ? 324 GLU B C   1 
ATOM   6795 O O   . GLU B 1 324 ? -18.358 54.642 42.307  1.00 24.04 ? 324 GLU B O   1 
ATOM   6796 C CB  . GLU B 1 324 ? -15.331 55.280 41.107  1.00 35.06 ? 324 GLU B CB  1 
ATOM   6797 C CG  . GLU B 1 324 ? -15.182 55.561 42.596  1.00 49.66 ? 324 GLU B CG  1 
ATOM   6798 C CD  . GLU B 1 324 ? -14.473 54.440 43.328  1.00 65.74 ? 324 GLU B CD  1 
ATOM   6799 O OE1 . GLU B 1 324 ? -14.840 54.152 44.490  1.00 68.84 ? 324 GLU B OE1 1 
ATOM   6800 O OE2 . GLU B 1 324 ? -13.555 53.835 42.734  1.00 72.34 ? 324 GLU B OE2 1 
ATOM   6801 N N   . ASP B 1 325 ? -18.318 56.090 40.585  1.00 26.22 ? 325 ASP B N   1 
ATOM   6802 C CA  . ASP B 1 325 ? -19.505 56.789 41.051  1.00 26.01 ? 325 ASP B CA  1 
ATOM   6803 C C   . ASP B 1 325 ? -20.753 55.926 40.917  1.00 19.82 ? 325 ASP B C   1 
ATOM   6804 O O   . ASP B 1 325 ? -21.633 55.961 41.785  1.00 23.77 ? 325 ASP B O   1 
ATOM   6805 C CB  . ASP B 1 325 ? -19.648 58.090 40.277  1.00 30.38 ? 325 ASP B CB  1 
ATOM   6806 C CG  . ASP B 1 325 ? -18.428 58.990 40.440  1.00 39.90 ? 325 ASP B CG  1 
ATOM   6807 O OD1 . ASP B 1 325 ? -17.897 59.068 41.569  1.00 45.06 ? 325 ASP B OD1 1 
ATOM   6808 O OD2 . ASP B 1 325 ? -18.003 59.617 39.451  1.00 41.49 ? 325 ASP B OD2 1 
ATOM   6809 N N   . ALA B 1 326 ? -20.847 55.158 39.830  1.00 18.74 ? 326 ALA B N   1 
ATOM   6810 C CA  . ALA B 1 326 ? -21.976 54.257 39.635  1.00 19.14 ? 326 ALA B CA  1 
ATOM   6811 C C   . ALA B 1 326 ? -22.042 53.209 40.744  1.00 21.27 ? 326 ALA B C   1 
ATOM   6812 O O   . ALA B 1 326 ? -23.119 52.931 41.291  1.00 20.04 ? 326 ALA B O   1 
ATOM   6813 C CB  . ALA B 1 326 ? -21.871 53.589 38.265  1.00 22.86 ? 326 ALA B CB  1 
ATOM   6814 N N   . VAL B 1 327 ? -20.900 52.615 41.084  1.00 23.42 ? 327 VAL B N   1 
ATOM   6815 C CA  . VAL B 1 327 ? -20.876 51.611 42.143  1.00 22.74 ? 327 VAL B CA  1 
ATOM   6816 C C   . VAL B 1 327 ? -21.223 52.240 43.488  1.00 23.97 ? 327 VAL B C   1 
ATOM   6817 O O   . VAL B 1 327 ? -21.954 51.651 44.292  1.00 22.05 ? 327 VAL B O   1 
ATOM   6818 C CB  . VAL B 1 327 ? -19.507 50.908 42.164  1.00 18.44 ? 327 VAL B CB  1 
ATOM   6819 C CG1 . VAL B 1 327 ? -19.352 50.053 43.420  1.00 20.14 ? 327 VAL B CG1 1 
ATOM   6820 C CG2 . VAL B 1 327 ? -19.351 50.074 40.902  1.00 18.49 ? 327 VAL B CG2 1 
ATOM   6821 N N   . ARG B 1 328 ? -20.724 53.449 43.750  1.00 19.40 ? 328 ARG B N   1 
ATOM   6822 C CA  . ARG B 1 328 ? -21.083 54.120 44.997  1.00 18.39 ? 328 ARG B CA  1 
ATOM   6823 C C   . ARG B 1 328 ? -22.583 54.362 45.066  1.00 21.45 ? 328 ARG B C   1 
ATOM   6824 O O   . ARG B 1 328 ? -23.208 54.165 46.117  1.00 20.15 ? 328 ARG B O   1 
ATOM   6825 C CB  . ARG B 1 328 ? -20.319 55.441 45.132  1.00 23.36 ? 328 ARG B CB  1 
ATOM   6826 C CG  . ARG B 1 328 ? -20.607 56.182 46.426  1.00 33.05 ? 328 ARG B CG  1 
ATOM   6827 C CD  . ARG B 1 328 ? -19.849 57.510 46.510  1.00 39.64 ? 328 ARG B CD  1 
ATOM   6828 N NE  . ARG B 1 328 ? -20.221 58.429 45.441  1.00 43.39 ? 328 ARG B NE  1 
ATOM   6829 C CZ  . ARG B 1 328 ? -19.411 58.803 44.456  1.00 43.87 ? 328 ARG B CZ  1 
ATOM   6830 N NH1 . ARG B 1 328 ? -18.166 58.343 44.396  1.00 40.18 ? 328 ARG B NH1 1 
ATOM   6831 N NH2 . ARG B 1 328 ? -19.850 59.643 43.528  1.00 51.42 ? 328 ARG B NH2 1 
ATOM   6832 N N   . ASP B 1 329 ? -23.176 54.795 43.950  1.00 21.84 ? 329 ASP B N   1 
ATOM   6833 C CA  . ASP B 1 329 ? -24.613 55.020 43.911  1.00 22.92 ? 329 ASP B CA  1 
ATOM   6834 C C   . ASP B 1 329 ? -25.365 53.730 44.196  1.00 22.47 ? 329 ASP B C   1 
ATOM   6835 O O   . ASP B 1 329 ? -26.311 53.706 44.992  1.00 20.79 ? 329 ASP B O   1 
ATOM   6836 C CB  . ASP B 1 329 ? -25.019 55.576 42.546  1.00 21.92 ? 329 ASP B CB  1 
ATOM   6837 C CG  . ASP B 1 329 ? -26.499 55.878 42.465  1.00 25.53 ? 329 ASP B CG  1 
ATOM   6838 O OD1 . ASP B 1 329 ? -26.912 56.932 42.997  1.00 24.96 ? 329 ASP B OD1 1 
ATOM   6839 O OD2 . ASP B 1 329 ? -27.245 55.065 41.884  1.00 25.27 ? 329 ASP B OD2 1 
ATOM   6840 N N   . PHE B 1 330 ? -24.937 52.641 43.554  1.00 19.20 ? 330 PHE B N   1 
ATOM   6841 C CA  . PHE B 1 330 ? -25.631 51.361 43.653  1.00 20.67 ? 330 PHE B CA  1 
ATOM   6842 C C   . PHE B 1 330 ? -25.561 50.811 45.075  1.00 22.45 ? 330 PHE B C   1 
ATOM   6843 O O   . PHE B 1 330 ? -26.588 50.448 45.663  1.00 18.04 ? 330 PHE B O   1 
ATOM   6844 C CB  . PHE B 1 330 ? -25.015 50.381 42.650  1.00 16.64 ? 330 PHE B CB  1 
ATOM   6845 C CG  . PHE B 1 330 ? -25.794 49.113 42.472  1.00 16.73 ? 330 PHE B CG  1 
ATOM   6846 C CD1 . PHE B 1 330 ? -26.881 49.065 41.606  1.00 19.72 ? 330 PHE B CD1 1 
ATOM   6847 C CD2 . PHE B 1 330 ? -25.432 47.967 43.158  1.00 19.76 ? 330 PHE B CD2 1 
ATOM   6848 C CE1 . PHE B 1 330 ? -27.596 47.888 41.422  1.00 16.71 ? 330 PHE B CE1 1 
ATOM   6849 C CE2 . PHE B 1 330 ? -26.134 46.789 42.984  1.00 19.96 ? 330 PHE B CE2 1 
ATOM   6850 C CZ  . PHE B 1 330 ? -27.218 46.747 42.115  1.00 17.96 ? 330 PHE B CZ  1 
ATOM   6851 N N   . ILE B 1 331 ? -24.355 50.758 45.646  1.00 16.86 ? 331 ILE B N   1 
ATOM   6852 C CA  . ILE B 1 331 ? -24.203 50.326 47.038  1.00 19.48 ? 331 ILE B CA  1 
ATOM   6853 C C   . ILE B 1 331 ? -24.981 51.243 47.974  1.00 20.04 ? 331 ILE B C   1 
ATOM   6854 O O   . ILE B 1 331 ? -25.589 50.786 48.949  1.00 19.79 ? 331 ILE B O   1 
ATOM   6855 C CB  . ILE B 1 331 ? -22.712 50.275 47.426  1.00 24.09 ? 331 ILE B CB  1 
ATOM   6856 C CG1 . ILE B 1 331 ? -21.946 49.368 46.466  1.00 24.38 ? 331 ILE B CG1 1 
ATOM   6857 C CG2 . ILE B 1 331 ? -22.545 49.811 48.889  1.00 23.87 ? 331 ILE B CG2 1 
ATOM   6858 C CD1 . ILE B 1 331 ? -22.294 47.909 46.591  1.00 21.74 ? 331 ILE B CD1 1 
ATOM   6859 N N   . GLY B 1 332 ? -24.971 52.548 47.705  1.00 18.90 ? 332 GLY B N   1 
ATOM   6860 C CA  . GLY B 1 332 ? -25.706 53.463 48.565  1.00 21.95 ? 332 GLY B CA  1 
ATOM   6861 C C   . GLY B 1 332 ? -27.198 53.191 48.562  1.00 17.45 ? 332 GLY B C   1 
ATOM   6862 O O   . GLY B 1 332 ? -27.863 53.322 49.595  1.00 23.63 ? 332 GLY B O   1 
ATOM   6863 N N   . ARG B 1 333 ? -27.744 52.814 47.406  1.00 17.60 ? 333 ARG B N   1 
ATOM   6864 C CA  . ARG B 1 333 ? -29.160 52.457 47.348  1.00 21.09 ? 333 ARG B CA  1 
ATOM   6865 C C   . ARG B 1 333 ? -29.429 51.158 48.093  1.00 21.02 ? 333 ARG B C   1 
ATOM   6866 O O   . ARG B 1 333 ? -30.452 51.028 48.774  1.00 19.86 ? 333 ARG B O   1 
ATOM   6867 C CB  . ARG B 1 333 ? -29.620 52.358 45.894  1.00 16.47 ? 333 ARG B CB  1 
ATOM   6868 C CG  . ARG B 1 333 ? -29.722 53.735 45.223  1.00 17.55 ? 333 ARG B CG  1 
ATOM   6869 C CD  . ARG B 1 333 ? -29.766 53.571 43.708  1.00 17.89 ? 333 ARG B CD  1 
ATOM   6870 N NE  . ARG B 1 333 ? -29.724 54.840 42.987  1.00 21.95 ? 333 ARG B NE  1 
ATOM   6871 C CZ  . ARG B 1 333 ? -30.788 55.603 42.772  1.00 27.47 ? 333 ARG B CZ  1 
ATOM   6872 N NH1 . ARG B 1 333 ? -31.975 55.227 43.238  1.00 26.48 ? 333 ARG B NH1 1 
ATOM   6873 N NH2 . ARG B 1 333 ? -30.664 56.743 42.106  1.00 25.78 ? 333 ARG B NH2 1 
ATOM   6874 N N   . LEU B 1 334 ? -28.516 50.190 47.988  1.00 19.33 ? 334 LEU B N   1 
ATOM   6875 C CA  . LEU B 1 334 ? -28.653 48.969 48.776  1.00 14.13 ? 334 LEU B CA  1 
ATOM   6876 C C   . LEU B 1 334 ? -28.604 49.270 50.267  1.00 18.34 ? 334 LEU B C   1 
ATOM   6877 O O   . LEU B 1 334 ? -29.331 48.654 51.054  1.00 20.68 ? 334 LEU B O   1 
ATOM   6878 C CB  . LEU B 1 334 ? -27.559 47.970 48.409  1.00 14.07 ? 334 LEU B CB  1 
ATOM   6879 C CG  . LEU B 1 334 ? -27.598 47.382 47.001  1.00 17.26 ? 334 LEU B CG  1 
ATOM   6880 C CD1 . LEU B 1 334 ? -26.429 46.429 46.781  1.00 15.94 ? 334 LEU B CD1 1 
ATOM   6881 C CD2 . LEU B 1 334 ? -28.925 46.653 46.796  1.00 15.81 ? 334 LEU B CD2 1 
ATOM   6882 N N   . LYS B 1 335 ? -27.740 50.205 50.676  1.00 17.11 ? 335 LYS B N   1 
ATOM   6883 C CA  . LYS B 1 335 ? -27.677 50.565 52.088  1.00 22.66 ? 335 LYS B CA  1 
ATOM   6884 C C   . LYS B 1 335 ? -29.008 51.130 52.563  1.00 21.55 ? 335 LYS B C   1 
ATOM   6885 O O   . LYS B 1 335 ? -29.475 50.800 53.657  1.00 22.74 ? 335 LYS B O   1 
ATOM   6886 C CB  . LYS B 1 335 ? -26.552 51.572 52.325  1.00 18.99 ? 335 LYS B CB  1 
ATOM   6887 C CG  . LYS B 1 335 ? -26.567 52.196 53.707  1.00 26.67 ? 335 LYS B CG  1 
ATOM   6888 C CD  . LYS B 1 335 ? -25.338 53.065 53.910  1.00 34.55 ? 335 LYS B CD  1 
ATOM   6889 C CE  . LYS B 1 335 ? -25.409 53.806 55.227  1.00 41.74 ? 335 LYS B CE  1 
ATOM   6890 N NZ  . LYS B 1 335 ? -25.514 55.269 55.007  1.00 50.31 ? 335 LYS B NZ  1 
ATOM   6891 N N   . LYS B 1 336 ? -29.644 51.964 51.737  1.00 21.21 ? 336 LYS B N   1 
ATOM   6892 C CA  . LYS B 1 336 ? -30.909 52.580 52.126  1.00 25.95 ? 336 LYS B CA  1 
ATOM   6893 C C   . LYS B 1 336 ? -32.022 51.542 52.253  1.00 21.52 ? 336 LYS B C   1 
ATOM   6894 O O   . LYS B 1 336 ? -32.837 51.616 53.181  1.00 26.27 ? 336 LYS B O   1 
ATOM   6895 C CB  . LYS B 1 336 ? -31.281 53.670 51.117  1.00 29.35 ? 336 LYS B CB  1 
ATOM   6896 C CG  . LYS B 1 336 ? -30.491 54.971 51.286  1.00 34.06 ? 336 LYS B CG  1 
ATOM   6897 C CD  . LYS B 1 336 ? -30.627 55.884 50.073  1.00 45.11 ? 336 LYS B CD  1 
ATOM   6898 C CE  . LYS B 1 336 ? -29.718 57.106 50.185  1.00 54.70 ? 336 LYS B CE  1 
ATOM   6899 N NZ  . LYS B 1 336 ? -29.168 57.509 48.857  1.00 58.87 ? 336 LYS B NZ  1 
ATOM   6900 N N   . ILE B 1 337 ? -32.072 50.578 51.326  1.00 19.16 ? 337 ILE B N   1 
ATOM   6901 C CA  . ILE B 1 337 ? -33.001 49.447 51.434  1.00 18.89 ? 337 ILE B CA  1 
ATOM   6902 C C   . ILE B 1 337 ? -32.762 48.688 52.734  1.00 21.47 ? 337 ILE B C   1 
ATOM   6903 O O   . ILE B 1 337 ? -33.692 48.415 53.503  1.00 22.44 ? 337 ILE B O   1 
ATOM   6904 C CB  . ILE B 1 337 ? -32.850 48.507 50.223  1.00 18.72 ? 337 ILE B CB  1 
ATOM   6905 C CG1 . ILE B 1 337 ? -33.333 49.188 48.948  1.00 18.00 ? 337 ILE B CG1 1 
ATOM   6906 C CG2 . ILE B 1 337 ? -33.619 47.213 50.461  1.00 20.65 ? 337 ILE B CG2 1 
ATOM   6907 C CD1 . ILE B 1 337 ? -32.879 48.470 47.664  1.00 18.73 ? 337 ILE B CD1 1 
ATOM   6908 N N   . HIS B 1 338 ? -31.505 48.316 52.980  1.00 22.96 ? 338 HIS B N   1 
ATOM   6909 C CA  . HIS B 1 338 ? -31.138 47.572 54.182  1.00 22.92 ? 338 HIS B CA  1 
ATOM   6910 C C   . HIS B 1 338 ? -31.570 48.297 55.456  1.00 26.83 ? 338 HIS B C   1 
ATOM   6911 O O   . HIS B 1 338 ? -32.032 47.664 56.416  1.00 25.53 ? 338 HIS B O   1 
ATOM   6912 C CB  . HIS B 1 338 ? -29.625 47.347 54.160  1.00 24.35 ? 338 HIS B CB  1 
ATOM   6913 C CG  . HIS B 1 338 ? -29.094 46.600 55.336  1.00 31.13 ? 338 HIS B CG  1 
ATOM   6914 N ND1 . HIS B 1 338 ? -28.355 47.209 56.327  1.00 35.17 ? 338 HIS B ND1 1 
ATOM   6915 C CD2 . HIS B 1 338 ? -29.153 45.287 55.660  1.00 30.64 ? 338 HIS B CD2 1 
ATOM   6916 C CE1 . HIS B 1 338 ? -28.004 46.306 57.226  1.00 36.24 ? 338 HIS B CE1 1 
ATOM   6917 N NE2 . HIS B 1 338 ? -28.471 45.132 56.841  1.00 34.60 ? 338 HIS B NE2 1 
ATOM   6918 N N   . GLU B 1 339 ? -31.433 49.625 55.488  1.00 22.70 ? 339 GLU B N   1 
ATOM   6919 C CA  . GLU B 1 339 ? -31.787 50.380 56.683  1.00 28.76 ? 339 GLU B CA  1 
ATOM   6920 C C   . GLU B 1 339 ? -33.272 50.711 56.771  1.00 31.22 ? 339 GLU B C   1 
ATOM   6921 O O   . GLU B 1 339 ? -33.719 51.195 57.813  1.00 31.67 ? 339 GLU B O   1 
ATOM   6922 C CB  . GLU B 1 339 ? -30.971 51.673 56.740  1.00 31.32 ? 339 GLU B CB  1 
ATOM   6923 C CG  . GLU B 1 339 ? -29.482 51.440 56.906  1.00 39.32 ? 339 GLU B CG  1 
ATOM   6924 C CD  . GLU B 1 339 ? -28.673 52.713 56.771  1.00 51.42 ? 339 GLU B CD  1 
ATOM   6925 O OE1 . GLU B 1 339 ? -29.172 53.683 56.155  1.00 47.06 ? 339 GLU B OE1 1 
ATOM   6926 O OE2 . GLU B 1 339 ? -27.535 52.741 57.285  1.00 60.58 ? 339 GLU B OE2 1 
ATOM   6927 N N   . SER B 1 340 ? -34.046 50.456 55.722  1.00 31.08 ? 340 SER B N   1 
ATOM   6928 C CA  . SER B 1 340 ? -35.446 50.850 55.694  1.00 33.44 ? 340 SER B CA  1 
ATOM   6929 C C   . SER B 1 340 ? -36.389 49.758 56.179  1.00 33.82 ? 340 SER B C   1 
ATOM   6930 O O   . SER B 1 340 ? -37.576 50.034 56.378  1.00 34.51 ? 340 SER B O   1 
ATOM   6931 C CB  . SER B 1 340 ? -35.853 51.257 54.275  1.00 26.40 ? 340 SER B CB  1 
ATOM   6932 O OG  . SER B 1 340 ? -35.921 50.114 53.435  1.00 32.76 ? 340 SER B OG  1 
ATOM   6933 N N   . VAL B 1 341 ? -35.904 48.535 56.367  1.00 27.95 ? 341 VAL B N   1 
ATOM   6934 C CA  . VAL B 1 341 ? -36.748 47.422 56.780  1.00 30.06 ? 341 VAL B CA  1 
ATOM   6935 C C   . VAL B 1 341 ? -36.149 46.785 58.022  1.00 27.74 ? 341 VAL B C   1 
ATOM   6936 O O   . VAL B 1 341 ? -34.941 46.866 58.265  1.00 31.97 ? 341 VAL B O   1 
ATOM   6937 C CB  . VAL B 1 341 ? -36.910 46.363 55.664  1.00 27.27 ? 341 VAL B CB  1 
ATOM   6938 C CG1 . VAL B 1 341 ? -37.639 46.943 54.474  1.00 25.03 ? 341 VAL B CG1 1 
ATOM   6939 C CG2 . VAL B 1 341 ? -35.550 45.808 55.237  1.00 27.09 ? 341 VAL B CG2 1 
ATOM   6940 N N   . ASP B 1 342 ? -37.005 46.135 58.805  1.00 28.85 ? 342 ASP B N   1 
ATOM   6941 C CA  . ASP B 1 342 ? -36.582 45.443 60.014  1.00 33.17 ? 342 ASP B CA  1 
ATOM   6942 C C   . ASP B 1 342 ? -36.382 43.950 59.797  1.00 30.86 ? 342 ASP B C   1 
ATOM   6943 O O   . ASP B 1 342 ? -36.091 43.229 60.756  1.00 38.96 ? 342 ASP B O   1 
ATOM   6944 C CB  . ASP B 1 342 ? -37.600 45.676 61.138  1.00 44.30 ? 342 ASP B CB  1 
ATOM   6945 C CG  . ASP B 1 342 ? -39.014 45.295 60.733  1.00 61.02 ? 342 ASP B CG  1 
ATOM   6946 O OD1 . ASP B 1 342 ? -39.419 45.618 59.596  1.00 65.20 ? 342 ASP B OD1 1 
ATOM   6947 O OD2 . ASP B 1 342 ? -39.722 44.673 61.554  1.00 67.77 ? 342 ASP B OD2 1 
ATOM   6948 N N   . PHE B 1 343 ? -36.534 43.475 58.564  1.00 23.90 ? 343 PHE B N   1 
ATOM   6949 C CA  . PHE B 1 343 ? -36.277 42.100 58.173  1.00 21.12 ? 343 PHE B CA  1 
ATOM   6950 C C   . PHE B 1 343 ? -35.106 42.086 57.191  1.00 19.04 ? 343 PHE B C   1 
ATOM   6951 O O   . PHE B 1 343 ? -34.537 43.128 56.863  1.00 23.35 ? 343 PHE B O   1 
ATOM   6952 C CB  . PHE B 1 343 ? -37.541 41.469 57.572  1.00 24.58 ? 343 PHE B CB  1 
ATOM   6953 C CG  . PHE B 1 343 ? -38.122 42.242 56.414  1.00 21.41 ? 343 PHE B CG  1 
ATOM   6954 C CD1 . PHE B 1 343 ? -38.995 43.302 56.631  1.00 22.97 ? 343 PHE B CD1 1 
ATOM   6955 C CD2 . PHE B 1 343 ? -37.806 41.902 55.111  1.00 18.25 ? 343 PHE B CD2 1 
ATOM   6956 C CE1 . PHE B 1 343 ? -39.528 44.010 55.563  1.00 21.91 ? 343 PHE B CE1 1 
ATOM   6957 C CE2 . PHE B 1 343 ? -38.332 42.610 54.038  1.00 21.12 ? 343 PHE B CE2 1 
ATOM   6958 C CZ  . PHE B 1 343 ? -39.203 43.669 54.272  1.00 20.90 ? 343 PHE B CZ  1 
ATOM   6959 N N   . GLN B 1 344 ? -34.742 40.889 56.721  1.00 19.38 ? 344 GLN B N   1 
ATOM   6960 C CA  . GLN B 1 344 ? -33.688 40.757 55.721  1.00 16.90 ? 344 GLN B CA  1 
ATOM   6961 C C   . GLN B 1 344 ? -34.283 40.841 54.319  1.00 15.95 ? 344 GLN B C   1 
ATOM   6962 O O   . GLN B 1 344 ? -34.893 39.865 53.855  1.00 18.06 ? 344 GLN B O   1 
ATOM   6963 C CB  . GLN B 1 344 ? -32.936 39.450 55.907  1.00 18.08 ? 344 GLN B CB  1 
ATOM   6964 C CG  . GLN B 1 344 ? -32.298 39.355 57.288  1.00 17.87 ? 344 GLN B CG  1 
ATOM   6965 C CD  . GLN B 1 344 ? -31.389 38.158 57.449  1.00 23.88 ? 344 GLN B CD  1 
ATOM   6966 O OE1 . GLN B 1 344 ? -30.189 38.306 57.698  1.00 23.23 ? 344 GLN B OE1 1 
ATOM   6967 N NE2 . GLN B 1 344 ? -31.959 36.961 57.334  1.00 23.42 ? 344 GLN B NE2 1 
ATOM   6968 N N   . PRO B 1 345 ? -34.117 41.948 53.608  1.00 16.05 ? 345 PRO B N   1 
ATOM   6969 C CA  . PRO B 1 345 ? -34.770 42.088 52.303  1.00 19.49 ? 345 PRO B CA  1 
ATOM   6970 C C   . PRO B 1 345 ? -34.080 41.248 51.243  1.00 18.12 ? 345 PRO B C   1 
ATOM   6971 O O   . PRO B 1 345 ? -32.865 41.034 51.281  1.00 17.44 ? 345 PRO B O   1 
ATOM   6972 C CB  . PRO B 1 345 ? -34.622 43.578 52.001  1.00 18.28 ? 345 PRO B CB  1 
ATOM   6973 C CG  . PRO B 1 345 ? -33.287 43.910 52.635  1.00 16.52 ? 345 PRO B CG  1 
ATOM   6974 C CD  . PRO B 1 345 ? -33.222 43.083 53.906  1.00 17.14 ? 345 PRO B CD  1 
ATOM   6975 N N   . VAL B 1 346 ? -34.870 40.786 50.272  1.00 12.74 ? 346 VAL B N   1 
ATOM   6976 C CA  . VAL B 1 346 ? -34.357 40.099 49.091  1.00 11.69 ? 346 VAL B CA  1 
ATOM   6977 C C   . VAL B 1 346 ? -34.506 41.044 47.909  1.00 19.25 ? 346 VAL B C   1 
ATOM   6978 O O   . VAL B 1 346 ? -35.615 41.498 47.604  1.00 17.42 ? 346 VAL B O   1 
ATOM   6979 C CB  . VAL B 1 346 ? -35.080 38.768 48.836  1.00 13.66 ? 346 VAL B CB  1 
ATOM   6980 C CG1 . VAL B 1 346 ? -34.500 38.092 47.604  1.00 14.64 ? 346 VAL B CG1 1 
ATOM   6981 C CG2 . VAL B 1 346 ? -34.951 37.863 50.050  1.00 19.43 ? 346 VAL B CG2 1 
ATOM   6982 N N   . VAL B 1 347 ? -33.391 41.348 47.254  1.00 13.34 ? 347 VAL B N   1 
ATOM   6983 C CA  . VAL B 1 347 ? -33.340 42.369 46.213  1.00 14.37 ? 347 VAL B CA  1 
ATOM   6984 C C   . VAL B 1 347 ? -32.967 41.673 44.915  1.00 11.62 ? 347 VAL B C   1 
ATOM   6985 O O   . VAL B 1 347 ? -31.806 41.280 44.727  1.00 13.65 ? 347 VAL B O   1 
ATOM   6986 C CB  . VAL B 1 347 ? -32.341 43.485 46.549  1.00 11.14 ? 347 VAL B CB  1 
ATOM   6987 C CG1 . VAL B 1 347 ? -32.391 44.574 45.479  1.00 12.69 ? 347 VAL B CG1 1 
ATOM   6988 C CG2 . VAL B 1 347 ? -32.634 44.084 47.931  1.00 14.73 ? 347 VAL B CG2 1 
ATOM   6989 N N   . PHE B 1 348 ? -33.946 41.521 44.020  1.00 12.83 ? 348 PHE B N   1 
ATOM   6990 C CA  . PHE B 1 348 ? -33.713 40.887 42.731  1.00 12.88 ? 348 PHE B CA  1 
ATOM   6991 C C   . PHE B 1 348 ? -33.328 41.959 41.722  1.00 13.13 ? 348 PHE B C   1 
ATOM   6992 O O   . PHE B 1 348 ? -34.070 42.923 41.522  1.00 13.85 ? 348 PHE B O   1 
ATOM   6993 C CB  . PHE B 1 348 ? -34.947 40.126 42.254  1.00 13.67 ? 348 PHE B CB  1 
ATOM   6994 C CG  . PHE B 1 348 ? -34.912 38.657 42.568  1.00 14.47 ? 348 PHE B CG  1 
ATOM   6995 C CD1 . PHE B 1 348 ? -35.006 38.222 43.886  1.00 19.10 ? 348 PHE B CD1 1 
ATOM   6996 C CD2 . PHE B 1 348 ? -34.792 37.715 41.558  1.00 16.72 ? 348 PHE B CD2 1 
ATOM   6997 C CE1 . PHE B 1 348 ? -34.982 36.869 44.194  1.00 12.23 ? 348 PHE B CE1 1 
ATOM   6998 C CE2 . PHE B 1 348 ? -34.772 36.350 41.856  1.00 16.75 ? 348 PHE B CE2 1 
ATOM   6999 C CZ  . PHE B 1 348 ? -34.873 35.924 43.172  1.00 13.75 ? 348 PHE B CZ  1 
ATOM   7000 N N   . VAL B 1 349 ? -32.175 41.789 41.093  1.00 11.02 ? 349 VAL B N   1 
ATOM   7001 C CA  . VAL B 1 349 ? -31.721 42.669 40.028  1.00 12.26 ? 349 VAL B CA  1 
ATOM   7002 C C   . VAL B 1 349 ? -31.766 41.820 38.765  1.00 11.73 ? 349 VAL B C   1 
ATOM   7003 O O   . VAL B 1 349 ? -30.957 40.897 38.597  1.00 13.77 ? 349 VAL B O   1 
ATOM   7004 C CB  . VAL B 1 349 ? -30.321 43.234 40.307  1.00 10.41 ? 349 VAL B CB  1 
ATOM   7005 C CG1 . VAL B 1 349 ? -29.866 44.153 39.169  1.00 15.09 ? 349 VAL B CG1 1 
ATOM   7006 C CG2 . VAL B 1 349 ? -30.329 44.028 41.636  1.00 14.84 ? 349 VAL B CG2 1 
ATOM   7007 N N   . VAL B 1 350 ? -32.773 42.061 37.920  1.00 10.42 ? 350 VAL B N   1 
ATOM   7008 C CA  . VAL B 1 350 ? -33.032 41.206 36.766  1.00 11.06 ? 350 VAL B CA  1 
ATOM   7009 C C   . VAL B 1 350 ? -33.077 42.082 35.525  1.00 13.88 ? 350 VAL B C   1 
ATOM   7010 O O   . VAL B 1 350 ? -33.859 43.037 35.466  1.00 12.79 ? 350 VAL B O   1 
ATOM   7011 C CB  . VAL B 1 350 ? -34.349 40.416 36.901  1.00 11.77 ? 350 VAL B CB  1 
ATOM   7012 C CG1 . VAL B 1 350 ? -34.466 39.408 35.763  1.00 14.26 ? 350 VAL B CG1 1 
ATOM   7013 C CG2 . VAL B 1 350 ? -34.453 39.739 38.287  1.00 13.01 ? 350 VAL B CG2 1 
ATOM   7014 N N   . LEU B 1 351 ? -32.266 41.742 34.529  1.00 13.65 ? 351 LEU B N   1 
ATOM   7015 C CA  . LEU B 1 351 ? -32.208 42.533 33.310  1.00 14.07 ? 351 LEU B CA  1 
ATOM   7016 C C   . LEU B 1 351 ? -31.480 41.708 32.260  1.00 10.59 ? 351 LEU B C   1 
ATOM   7017 O O   . LEU B 1 351 ? -30.889 40.666 32.562  1.00 14.46 ? 351 LEU B O   1 
ATOM   7018 C CB  . LEU B 1 351 ? -31.510 43.878 33.535  1.00 12.83 ? 351 LEU B CB  1 
ATOM   7019 C CG  . LEU B 1 351 ? -30.030 43.836 33.931  1.00 18.26 ? 351 LEU B CG  1 
ATOM   7020 C CD1 . LEU B 1 351 ? -29.322 45.068 33.373  1.00 15.86 ? 351 LEU B CD1 1 
ATOM   7021 C CD2 . LEU B 1 351 ? -29.845 43.768 35.454  1.00 18.91 ? 351 LEU B CD2 1 
ATOM   7022 N N   . ASN B 1 352 ? -31.479 42.199 31.041  1.00 14.30 ? 352 ASN B N   1 
ATOM   7023 C CA  . ASN B 1 352 ? -30.775 41.524 29.981  1.00 12.31 ? 352 ASN B CA  1 
ATOM   7024 C C   . ASN B 1 352 ? -29.310 41.545 30.369  1.00 12.40 ? 352 ASN B C   1 
ATOM   7025 O O   . ASN B 1 352 ? -28.857 42.472 30.891  1.00 15.13 ? 352 ASN B O   1 
ATOM   7026 C CB  . ASN B 1 352 ? -30.984 42.188 28.609  1.00 15.86 ? 352 ASN B CB  1 
ATOM   7027 C CG  . ASN B 1 352 ? -32.454 42.313 28.211  1.00 30.30 ? 352 ASN B CG  1 
ATOM   7028 O OD1 . ASN B 1 352 ? -33.230 41.528 28.455  1.00 51.92 ? 352 ASN B OD1 1 
ATOM   7029 N ND2 . ASN B 1 352 ? -32.763 43.397 27.529  1.00 17.35 ? 352 ASN B ND2 1 
ATOM   7030 N N   . GLY B 1 353 ? -28.589 40.477 30.047  1.00 15.20 ? 353 GLY B N   1 
ATOM   7031 C CA  . GLY B 1 353 ? -27.204 40.367 30.450  1.00 16.30 ? 353 GLY B CA  1 
ATOM   7032 C C   . GLY B 1 353 ? -26.175 40.699 29.397  1.00 12.54 ? 353 GLY B C   1 
ATOM   7033 O O   . GLY B 1 353 ? -24.974 40.584 29.659  1.00 14.25 ? 353 GLY B O   1 
ATOM   7034 N N   . GLU B 1 354 ? -26.600 41.115 28.202  1.00 15.55 ? 354 GLU B N   1 
ATOM   7035 C CA  . GLU B 1 354 ? -25.661 41.244 27.096  1.00 11.68 ? 354 GLU B CA  1 
ATOM   7036 C C   . GLU B 1 354 ? -25.808 42.524 26.286  1.00 13.59 ? 354 GLU B C   1 
ATOM   7037 O O   . GLU B 1 354 ? -24.979 42.759 25.401  1.00 18.05 ? 354 GLU B O   1 
ATOM   7038 C CB  . GLU B 1 354 ? -25.806 40.037 26.142  1.00 13.59 ? 354 GLU B CB  1 
ATOM   7039 C CG  . GLU B 1 354 ? -26.968 40.128 25.145  1.00 11.95 ? 354 GLU B CG  1 
ATOM   7040 C CD  . GLU B 1 354 ? -28.304 39.649 25.725  1.00 14.21 ? 354 GLU B CD  1 
ATOM   7041 O OE1 . GLU B 1 354 ? -28.833 38.604 25.261  1.00 14.61 ? 354 GLU B OE1 1 
ATOM   7042 O OE2 . GLU B 1 354 ? -28.814 40.307 26.659  1.00 15.78 ? 354 GLU B OE2 1 
ATOM   7043 N N   . ASN B 1 355 ? -26.807 43.364 26.557  1.00 11.81 ? 355 ASN B N   1 
ATOM   7044 C CA  . ASN B 1 355 ? -27.093 44.506 25.694  1.00 11.91 ? 355 ASN B CA  1 
ATOM   7045 C C   . ASN B 1 355 ? -26.558 45.837 26.206  1.00 16.55 ? 355 ASN B C   1 
ATOM   7046 O O   . ASN B 1 355 ? -26.347 46.744 25.398  1.00 15.32 ? 355 ASN B O   1 
ATOM   7047 C CB  . ASN B 1 355 ? -28.602 44.627 25.492  1.00 15.24 ? 355 ASN B CB  1 
ATOM   7048 C CG  . ASN B 1 355 ? -29.145 43.472 24.710  1.00 15.60 ? 355 ASN B CG  1 
ATOM   7049 O OD1 . ASN B 1 355 ? -28.492 43.012 23.776  1.00 15.83 ? 355 ASN B OD1 1 
ATOM   7050 N ND2 . ASN B 1 355 ? -30.321 42.983 25.082  1.00 16.81 ? 355 ASN B ND2 1 
ATOM   7051 N N   . CYS B 1 356 ? -26.353 45.999 27.512  1.00 14.96 ? 356 CYS B N   1 
ATOM   7052 C CA  . CYS B 1 356 ? -25.975 47.315 28.027  1.00 10.36 ? 356 CYS B CA  1 
ATOM   7053 C C   . CYS B 1 356 ? -24.472 47.591 27.954  1.00 11.38 ? 356 CYS B C   1 
ATOM   7054 O O   . CYS B 1 356 ? -24.073 48.757 27.829  1.00 14.70 ? 356 CYS B O   1 
ATOM   7055 C CB  . CYS B 1 356 ? -26.467 47.465 29.474  1.00 15.73 ? 356 CYS B CB  1 
ATOM   7056 S SG  . CYS B 1 356 ? -25.977 46.134 30.629  1.00 14.91 ? 356 CYS B SG  1 
ATOM   7057 N N   . TRP B 1 357 ? -23.633 46.548 27.964  1.00 12.57 ? 357 TRP B N   1 
ATOM   7058 C CA  . TRP B 1 357 ? -22.194 46.744 28.165  1.00 16.65 ? 357 TRP B CA  1 
ATOM   7059 C C   . TRP B 1 357 ? -21.534 47.488 27.010  1.00 14.93 ? 357 TRP B C   1 
ATOM   7060 O O   . TRP B 1 357 ? -20.551 48.216 27.222  1.00 14.34 ? 357 TRP B O   1 
ATOM   7061 C CB  . TRP B 1 357 ? -21.507 45.392 28.381  1.00 12.50 ? 357 TRP B CB  1 
ATOM   7062 C CG  . TRP B 1 357 ? -22.278 44.572 29.355  1.00 10.34 ? 357 TRP B CG  1 
ATOM   7063 C CD1 . TRP B 1 357 ? -22.868 43.363 29.131  1.00 13.62 ? 357 TRP B CD1 1 
ATOM   7064 C CD2 . TRP B 1 357 ? -22.602 44.936 30.704  1.00 13.93 ? 357 TRP B CD2 1 
ATOM   7065 N NE1 . TRP B 1 357 ? -23.519 42.943 30.261  1.00 12.50 ? 357 TRP B NE1 1 
ATOM   7066 C CE2 . TRP B 1 357 ? -23.384 43.892 31.239  1.00 13.98 ? 357 TRP B CE2 1 
ATOM   7067 C CE3 . TRP B 1 357 ? -22.309 46.050 31.510  1.00 15.48 ? 357 TRP B CE3 1 
ATOM   7068 C CZ2 . TRP B 1 357 ? -23.876 43.915 32.552  1.00 14.08 ? 357 TRP B CZ2 1 
ATOM   7069 C CZ3 . TRP B 1 357 ? -22.795 46.076 32.809  1.00 15.54 ? 357 TRP B CZ3 1 
ATOM   7070 C CH2 . TRP B 1 357 ? -23.570 45.014 33.320  1.00 13.38 ? 357 TRP B CH2 1 
ATOM   7071 N N   . GLU B 1 358 ? -22.050 47.320 25.791  1.00 15.51 ? 358 GLU B N   1 
ATOM   7072 C CA  . GLU B 1 358 ? -21.446 47.980 24.637  1.00 13.03 ? 358 GLU B CA  1 
ATOM   7073 C C   . GLU B 1 358 ? -21.529 49.497 24.718  1.00 19.14 ? 358 GLU B C   1 
ATOM   7074 O O   . GLU B 1 358 ? -20.808 50.175 23.985  1.00 19.70 ? 358 GLU B O   1 
ATOM   7075 C CB  . GLU B 1 358 ? -22.103 47.481 23.339  1.00 17.79 ? 358 GLU B CB  1 
ATOM   7076 C CG  . GLU B 1 358 ? -23.600 47.762 23.264  1.00 14.90 ? 358 GLU B CG  1 
ATOM   7077 C CD  . GLU B 1 358 ? -24.330 46.805 22.331  1.00 19.20 ? 358 GLU B CD  1 
ATOM   7078 O OE1 . GLU B 1 358 ? -24.900 47.268 21.321  1.00 22.63 ? 358 GLU B OE1 1 
ATOM   7079 O OE2 . GLU B 1 358 ? -24.307 45.593 22.609  1.00 18.01 ? 358 GLU B OE2 1 
ATOM   7080 N N   . TYR B 1 359 ? -22.392 50.047 25.584  1.00 15.33 ? 359 TYR B N   1 
ATOM   7081 C CA  . TYR B 1 359 ? -22.469 51.489 25.785  1.00 13.28 ? 359 TYR B CA  1 
ATOM   7082 C C   . TYR B 1 359 ? -21.641 51.961 26.968  1.00 17.08 ? 359 TYR B C   1 
ATOM   7083 O O   . TYR B 1 359 ? -21.531 53.173 27.183  1.00 21.15 ? 359 TYR B O   1 
ATOM   7084 C CB  . TYR B 1 359 ? -23.932 51.919 25.971  1.00 15.12 ? 359 TYR B CB  1 
ATOM   7085 C CG  . TYR B 1 359 ? -24.836 51.449 24.842  1.00 16.25 ? 359 TYR B CG  1 
ATOM   7086 C CD1 . TYR B 1 359 ? -24.863 52.123 23.627  1.00 23.15 ? 359 TYR B CD1 1 
ATOM   7087 C CD2 . TYR B 1 359 ? -25.628 50.310 24.978  1.00 23.44 ? 359 TYR B CD2 1 
ATOM   7088 C CE1 . TYR B 1 359 ? -25.679 51.697 22.588  1.00 26.48 ? 359 TYR B CE1 1 
ATOM   7089 C CE2 . TYR B 1 359 ? -26.441 49.870 23.944  1.00 27.22 ? 359 TYR B CE2 1 
ATOM   7090 C CZ  . TYR B 1 359 ? -26.459 50.568 22.748  1.00 33.06 ? 359 TYR B CZ  1 
ATOM   7091 O OH  . TYR B 1 359 ? -27.266 50.141 21.709  1.00 33.14 ? 359 TYR B OH  1 
ATOM   7092 N N   . TYR B 1 360 ? -21.064 51.047 27.737  1.00 17.16 ? 360 TYR B N   1 
ATOM   7093 C CA  . TYR B 1 360 ? -20.193 51.420 28.839  1.00 20.85 ? 360 TYR B CA  1 
ATOM   7094 C C   . TYR B 1 360 ? -18.774 51.602 28.327  1.00 22.25 ? 360 TYR B C   1 
ATOM   7095 O O   . TYR B 1 360 ? -18.336 50.921 27.393  1.00 19.20 ? 360 TYR B O   1 
ATOM   7096 C CB  . TYR B 1 360 ? -20.156 50.345 29.928  1.00 17.23 ? 360 TYR B CB  1 
ATOM   7097 C CG  . TYR B 1 360 ? -21.300 50.256 30.909  1.00 20.97 ? 360 TYR B CG  1 
ATOM   7098 C CD1 . TYR B 1 360 ? -22.570 49.862 30.505  1.00 18.21 ? 360 TYR B CD1 1 
ATOM   7099 C CD2 . TYR B 1 360 ? -21.081 50.477 32.270  1.00 22.02 ? 360 TYR B CD2 1 
ATOM   7100 C CE1 . TYR B 1 360 ? -23.603 49.726 31.421  1.00 16.92 ? 360 TYR B CE1 1 
ATOM   7101 C CE2 . TYR B 1 360 ? -22.098 50.345 33.194  1.00 15.50 ? 360 TYR B CE2 1 
ATOM   7102 C CZ  . TYR B 1 360 ? -23.364 49.973 32.768  1.00 17.25 ? 360 TYR B CZ  1 
ATOM   7103 O OH  . TYR B 1 360 ? -24.382 49.829 33.685  1.00 14.15 ? 360 TYR B OH  1 
ATOM   7104 N N   . GLU B 1 361 ? -18.040 52.494 28.980  1.00 23.59 ? 361 GLU B N   1 
ATOM   7105 C CA  . GLU B 1 361 ? -16.603 52.550 28.766  1.00 26.54 ? 361 GLU B CA  1 
ATOM   7106 C C   . GLU B 1 361 ? -15.989 51.169 28.955  1.00 19.60 ? 361 GLU B C   1 
ATOM   7107 O O   . GLU B 1 361 ? -16.329 50.445 29.894  1.00 21.32 ? 361 GLU B O   1 
ATOM   7108 C CB  . GLU B 1 361 ? -15.971 53.550 29.733  1.00 35.98 ? 361 GLU B CB  1 
ATOM   7109 C CG  . GLU B 1 361 ? -16.417 54.969 29.484  1.00 43.21 ? 361 GLU B CG  1 
ATOM   7110 C CD  . GLU B 1 361 ? -16.092 55.432 28.079  1.00 52.00 ? 361 GLU B CD  1 
ATOM   7111 O OE1 . GLU B 1 361 ? -14.957 55.177 27.622  1.00 54.48 ? 361 GLU B OE1 1 
ATOM   7112 O OE2 . GLU B 1 361 ? -16.967 56.046 27.431  1.00 51.16 ? 361 GLU B OE2 1 
ATOM   7113 N N   . GLU B 1 362 ? -15.108 50.789 28.027  1.00 23.58 ? 362 GLU B N   1 
ATOM   7114 C CA  . GLU B 1 362 ? -14.375 49.536 28.128  1.00 20.42 ? 362 GLU B CA  1 
ATOM   7115 C C   . GLU B 1 362 ? -15.306 48.332 28.304  1.00 21.87 ? 362 GLU B C   1 
ATOM   7116 O O   . GLU B 1 362 ? -14.980 47.382 29.032  1.00 19.14 ? 362 GLU B O   1 
ATOM   7117 C CB  . GLU B 1 362 ? -13.362 49.598 29.275  1.00 25.05 ? 362 GLU B CB  1 
ATOM   7118 C CG  . GLU B 1 362 ? -12.099 48.791 29.057  1.00 42.79 ? 362 GLU B CG  1 
ATOM   7119 C CD  . GLU B 1 362 ? -11.011 49.142 30.061  1.00 57.60 ? 362 GLU B CD  1 
ATOM   7120 O OE1 . GLU B 1 362 ? -10.348 48.212 30.568  1.00 63.78 ? 362 GLU B OE1 1 
ATOM   7121 O OE2 . GLU B 1 362 ? -10.814 50.347 30.339  1.00 59.87 ? 362 GLU B OE2 1 
ATOM   7122 N N   . ASN B 1 363 ? -16.481 48.375 27.663  1.00 19.82 ? 363 ASN B N   1 
ATOM   7123 C CA  . ASN B 1 363 ? -17.385 47.219 27.601  1.00 18.58 ? 363 ASN B CA  1 
ATOM   7124 C C   . ASN B 1 363 ? -17.857 46.802 28.987  1.00 20.19 ? 363 ASN B C   1 
ATOM   7125 O O   . ASN B 1 363 ? -18.098 45.621 29.247  1.00 17.32 ? 363 ASN B O   1 
ATOM   7126 C CB  . ASN B 1 363 ? -16.720 46.040 26.873  1.00 20.93 ? 363 ASN B CB  1 
ATOM   7127 C CG  . ASN B 1 363 ? -17.703 44.926 26.493  1.00 16.26 ? 363 ASN B CG  1 
ATOM   7128 O OD1 . ASN B 1 363 ? -18.879 45.166 26.197  1.00 17.26 ? 363 ASN B OD1 1 
ATOM   7129 N ND2 . ASN B 1 363 ? -17.211 43.689 26.514  1.00 18.46 ? 363 ASN B ND2 1 
ATOM   7130 N N   . GLY B 1 364 ? -17.974 47.771 29.889  1.00 16.93 ? 364 GLY B N   1 
ATOM   7131 C CA  . GLY B 1 364 ? -18.500 47.530 31.221  1.00 16.95 ? 364 GLY B CA  1 
ATOM   7132 C C   . GLY B 1 364 ? -17.544 46.861 32.186  1.00 16.16 ? 364 GLY B C   1 
ATOM   7133 O O   . GLY B 1 364 ? -17.924 46.660 33.352  1.00 17.69 ? 364 GLY B O   1 
ATOM   7134 N N   . ILE B 1 365 ? -16.327 46.521 31.751  1.00 20.02 ? 365 ILE B N   1 
ATOM   7135 C CA  . ILE B 1 365 ? -15.411 45.788 32.622  1.00 20.34 ? 365 ILE B CA  1 
ATOM   7136 C C   . ILE B 1 365 ? -15.011 46.598 33.848  1.00 17.91 ? 365 ILE B C   1 
ATOM   7137 O O   . ILE B 1 365 ? -15.089 46.059 34.964  1.00 18.14 ? 365 ILE B O   1 
ATOM   7138 C CB  . ILE B 1 365 ? -14.204 45.284 31.811  1.00 20.35 ? 365 ILE B CB  1 
ATOM   7139 C CG1 . ILE B 1 365 ? -14.678 44.322 30.721  1.00 22.22 ? 365 ILE B CG1 1 
ATOM   7140 C CG2 . ILE B 1 365 ? -13.196 44.600 32.736  1.00 19.29 ? 365 ILE B CG2 1 
ATOM   7141 C CD1 . ILE B 1 365 ? -13.645 44.063 29.661  1.00 24.15 ? 365 ILE B CD1 1 
ATOM   7142 N N   . PRO B 1 366 ? -14.610 47.874 33.737  1.00 18.16 ? 366 PRO B N   1 
ATOM   7143 C CA  . PRO B 1 366 ? -14.382 48.652 34.963  1.00 21.15 ? 366 PRO B CA  1 
ATOM   7144 C C   . PRO B 1 366 ? -15.569 48.663 35.911  1.00 20.05 ? 366 PRO B C   1 
ATOM   7145 O O   . PRO B 1 366 ? -15.381 48.512 37.129  1.00 20.87 ? 366 PRO B O   1 
ATOM   7146 C CB  . PRO B 1 366 ? -14.079 50.062 34.429  1.00 24.83 ? 366 PRO B CB  1 
ATOM   7147 C CG  . PRO B 1 366 ? -13.491 49.819 33.066  1.00 21.59 ? 366 PRO B CG  1 
ATOM   7148 C CD  . PRO B 1 366 ? -14.282 48.658 32.528  1.00 19.30 ? 366 PRO B CD  1 
ATOM   7149 N N   . PHE B 1 367 ? -16.790 48.822 35.393  1.00 18.53 ? 367 PHE B N   1 
ATOM   7150 C CA  . PHE B 1 367 ? -17.959 48.878 36.266  1.00 17.68 ? 367 PHE B CA  1 
ATOM   7151 C C   . PHE B 1 367 ? -18.185 47.549 36.970  1.00 18.50 ? 367 PHE B C   1 
ATOM   7152 O O   . PHE B 1 367 ? -18.349 47.505 38.194  1.00 17.04 ? 367 PHE B O   1 
ATOM   7153 C CB  . PHE B 1 367 ? -19.213 49.259 35.476  1.00 16.00 ? 367 PHE B CB  1 
ATOM   7154 C CG  . PHE B 1 367 ? -20.472 49.140 36.280  1.00 15.94 ? 367 PHE B CG  1 
ATOM   7155 C CD1 . PHE B 1 367 ? -20.776 50.093 37.241  1.00 20.11 ? 367 PHE B CD1 1 
ATOM   7156 C CD2 . PHE B 1 367 ? -21.331 48.052 36.119  1.00 14.96 ? 367 PHE B CD2 1 
ATOM   7157 C CE1 . PHE B 1 367 ? -21.911 49.992 38.010  1.00 19.80 ? 367 PHE B CE1 1 
ATOM   7158 C CE2 . PHE B 1 367 ? -22.490 47.946 36.889  1.00 14.63 ? 367 PHE B CE2 1 
ATOM   7159 C CZ  . PHE B 1 367 ? -22.775 48.925 37.840  1.00 16.54 ? 367 PHE B CZ  1 
ATOM   7160 N N   . LEU B 1 368 ? -18.230 46.454 36.207  1.00 14.52 ? 368 LEU B N   1 
ATOM   7161 C CA  . LEU B 1 368 ? -18.550 45.162 36.809  1.00 13.23 ? 368 LEU B CA  1 
ATOM   7162 C C   . LEU B 1 368 ? -17.431 44.678 37.726  1.00 18.06 ? 368 LEU B C   1 
ATOM   7163 O O   . LEU B 1 368 ? -17.702 44.140 38.807  1.00 16.60 ? 368 LEU B O   1 
ATOM   7164 C CB  . LEU B 1 368 ? -18.839 44.135 35.718  1.00 14.43 ? 368 LEU B CB  1 
ATOM   7165 C CG  . LEU B 1 368 ? -20.229 44.225 35.085  1.00 13.42 ? 368 LEU B CG  1 
ATOM   7166 C CD1 . LEU B 1 368 ? -20.390 43.141 34.045  1.00 17.95 ? 368 LEU B CD1 1 
ATOM   7167 C CD2 . LEU B 1 368 ? -21.360 44.089 36.121  1.00 15.03 ? 368 LEU B CD2 1 
ATOM   7168 N N   . GLU B 1 369 ? -16.167 44.869 37.329  1.00 18.52 ? 369 GLU B N   1 
ATOM   7169 C CA  . GLU B 1 369 ? -15.079 44.458 38.211  1.00 17.49 ? 369 GLU B CA  1 
ATOM   7170 C C   . GLU B 1 369 ? -15.123 45.244 39.511  1.00 22.45 ? 369 GLU B C   1 
ATOM   7171 O O   . GLU B 1 369 ? -14.876 44.694 40.590  1.00 21.06 ? 369 GLU B O   1 
ATOM   7172 C CB  . GLU B 1 369 ? -13.719 44.623 37.523  1.00 21.71 ? 369 GLU B CB  1 
ATOM   7173 C CG  . GLU B 1 369 ? -13.467 43.544 36.479  1.00 21.18 ? 369 GLU B CG  1 
ATOM   7174 C CD  . GLU B 1 369 ? -12.081 43.576 35.875  1.00 23.85 ? 369 GLU B CD  1 
ATOM   7175 O OE1 . GLU B 1 369 ? -11.329 44.548 36.113  1.00 27.90 ? 369 GLU B OE1 1 
ATOM   7176 O OE2 . GLU B 1 369 ? -11.744 42.612 35.153  1.00 22.28 ? 369 GLU B OE2 1 
ATOM   7177 N N   . LYS B 1 370 ? -15.443 46.535 39.427  1.00 16.43 ? 370 LYS B N   1 
ATOM   7178 C CA  . LYS B 1 370 ? -15.539 47.345 40.634  1.00 17.20 ? 370 LYS B CA  1 
ATOM   7179 C C   . LYS B 1 370 ? -16.778 46.977 41.443  1.00 18.94 ? 370 LYS B C   1 
ATOM   7180 O O   . LYS B 1 370 ? -16.720 46.883 42.680  1.00 21.68 ? 370 LYS B O   1 
ATOM   7181 C CB  . LYS B 1 370 ? -15.547 48.828 40.249  1.00 22.54 ? 370 LYS B CB  1 
ATOM   7182 C CG  . LYS B 1 370 ? -15.999 49.751 41.354  1.00 35.84 ? 370 LYS B CG  1 
ATOM   7183 C CD  . LYS B 1 370 ? -14.868 50.513 42.004  1.00 53.69 ? 370 LYS B CD  1 
ATOM   7184 C CE  . LYS B 1 370 ? -15.303 50.988 43.381  1.00 64.60 ? 370 LYS B CE  1 
ATOM   7185 N NZ  . LYS B 1 370 ? -16.263 52.126 43.289  1.00 67.87 ? 370 LYS B NZ  1 
ATOM   7186 N N   . LEU B 1 371 ? -17.905 46.749 40.764  1.00 16.55 ? 371 LEU B N   1 
ATOM   7187 C CA  . LEU B 1 371 ? -19.121 46.349 41.464  1.00 14.46 ? 371 LEU B CA  1 
ATOM   7188 C C   . LEU B 1 371 ? -18.924 45.033 42.202  1.00 15.93 ? 371 LEU B C   1 
ATOM   7189 O O   . LEU B 1 371 ? -19.191 44.932 43.405  1.00 16.65 ? 371 LEU B O   1 
ATOM   7190 C CB  . LEU B 1 371 ? -20.279 46.237 40.469  1.00 17.19 ? 371 LEU B CB  1 
ATOM   7191 C CG  . LEU B 1 371 ? -21.581 45.708 41.064  1.00 17.17 ? 371 LEU B CG  1 
ATOM   7192 C CD1 . LEU B 1 371 ? -22.109 46.709 42.086  1.00 20.69 ? 371 LEU B CD1 1 
ATOM   7193 C CD2 . LEU B 1 371 ? -22.618 45.459 39.967  1.00 17.34 ? 371 LEU B CD2 1 
ATOM   7194 N N   . TYR B 1 372 ? -18.443 44.017 41.491  1.00 15.43 ? 372 TYR B N   1 
ATOM   7195 C CA  . TYR B 1 372 ? -18.279 42.695 42.081  1.00 15.37 ? 372 TYR B CA  1 
ATOM   7196 C C   . TYR B 1 372 ? -17.224 42.698 43.178  1.00 18.88 ? 372 TYR B C   1 
ATOM   7197 O O   . TYR B 1 372 ? -17.401 42.048 44.216  1.00 17.34 ? 372 TYR B O   1 
ATOM   7198 C CB  . TYR B 1 372 ? -17.905 41.690 40.989  1.00 18.14 ? 372 TYR B CB  1 
ATOM   7199 C CG  . TYR B 1 372 ? -19.001 41.407 39.983  1.00 17.26 ? 372 TYR B CG  1 
ATOM   7200 C CD1 . TYR B 1 372 ? -20.333 41.729 40.250  1.00 15.29 ? 372 TYR B CD1 1 
ATOM   7201 C CD2 . TYR B 1 372 ? -18.698 40.812 38.763  1.00 17.30 ? 372 TYR B CD2 1 
ATOM   7202 C CE1 . TYR B 1 372 ? -21.327 41.435 39.325  1.00 16.82 ? 372 TYR B CE1 1 
ATOM   7203 C CE2 . TYR B 1 372 ? -19.664 40.532 37.844  1.00 13.44 ? 372 TYR B CE2 1 
ATOM   7204 C CZ  . TYR B 1 372 ? -20.984 40.848 38.123  1.00 12.89 ? 372 TYR B CZ  1 
ATOM   7205 O OH  . TYR B 1 372 ? -21.958 40.572 37.201  1.00 12.28 ? 372 TYR B OH  1 
ATOM   7206 N N   . SER B 1 373 ? -16.107 43.402 42.958  1.00 19.86 ? 373 SER B N   1 
ATOM   7207 C CA  . SER B 1 373 ? -15.075 43.477 43.985  1.00 20.51 ? 373 SER B CA  1 
ATOM   7208 C C   . SER B 1 373 ? -15.619 44.151 45.233  1.00 22.14 ? 373 SER B C   1 
ATOM   7209 O O   . SER B 1 373 ? -15.304 43.749 46.359  1.00 23.18 ? 373 SER B O   1 
ATOM   7210 C CB  . SER B 1 373 ? -13.858 44.236 43.455  1.00 19.33 ? 373 SER B CB  1 
ATOM   7211 O OG  . SER B 1 373 ? -13.053 44.667 44.535  1.00 43.46 ? 373 SER B OG  1 
ATOM   7212 N N   . THR B 1 374 ? -16.459 45.166 45.047  1.00 16.98 ? 374 THR B N   1 
ATOM   7213 C CA  . THR B 1 374 ? -17.020 45.876 46.190  1.00 19.63 ? 374 THR B CA  1 
ATOM   7214 C C   . THR B 1 374 ? -18.033 45.016 46.933  1.00 19.74 ? 374 THR B C   1 
ATOM   7215 O O   . THR B 1 374 ? -18.042 44.990 48.172  1.00 22.66 ? 374 THR B O   1 
ATOM   7216 C CB  . THR B 1 374 ? -17.655 47.182 45.715  1.00 20.89 ? 374 THR B CB  1 
ATOM   7217 O OG1 . THR B 1 374 ? -16.640 47.997 45.112  1.00 20.23 ? 374 THR B OG1 1 
ATOM   7218 C CG2 . THR B 1 374 ? -18.293 47.939 46.886  1.00 25.29 ? 374 THR B CG2 1 
ATOM   7219 N N   . LEU B 1 375 ? -18.879 44.291 46.192  1.00 18.55 ? 375 LEU B N   1 
ATOM   7220 C CA  . LEU B 1 375 ? -19.919 43.480 46.820  1.00 18.97 ? 375 LEU B CA  1 
ATOM   7221 C C   . LEU B 1 375 ? -19.326 42.362 47.664  1.00 20.20 ? 375 LEU B C   1 
ATOM   7222 O O   . LEU B 1 375 ? -19.848 42.045 48.740  1.00 24.54 ? 375 LEU B O   1 
ATOM   7223 C CB  . LEU B 1 375 ? -20.849 42.900 45.753  1.00 20.64 ? 375 LEU B CB  1 
ATOM   7224 C CG  . LEU B 1 375 ? -21.802 43.869 45.065  1.00 21.53 ? 375 LEU B CG  1 
ATOM   7225 C CD1 . LEU B 1 375 ? -22.502 43.184 43.897  1.00 25.06 ? 375 LEU B CD1 1 
ATOM   7226 C CD2 . LEU B 1 375 ? -22.831 44.421 46.056  1.00 25.95 ? 375 LEU B CD2 1 
ATOM   7227 N N   . GLU B 1 376 ? -18.218 41.767 47.216  1.00 20.59 ? 376 GLU B N   1 
ATOM   7228 C CA  . GLU B 1 376 ? -17.657 40.667 47.987  1.00 28.54 ? 376 GLU B CA  1 
ATOM   7229 C C   . GLU B 1 376 ? -17.001 41.149 49.271  1.00 31.64 ? 376 GLU B C   1 
ATOM   7230 O O   . GLU B 1 376 ? -16.705 40.329 50.146  1.00 32.74 ? 376 GLU B O   1 
ATOM   7231 C CB  . GLU B 1 376 ? -16.671 39.857 47.134  1.00 33.63 ? 376 GLU B CB  1 
ATOM   7232 C CG  . GLU B 1 376 ? -15.388 40.561 46.758  1.00 38.25 ? 376 GLU B CG  1 
ATOM   7233 C CD  . GLU B 1 376 ? -14.551 39.758 45.768  1.00 37.51 ? 376 GLU B CD  1 
ATOM   7234 O OE1 . GLU B 1 376 ? -14.938 38.619 45.431  1.00 32.98 ? 376 GLU B OE1 1 
ATOM   7235 O OE2 . GLU B 1 376 ? -13.503 40.269 45.328  1.00 40.78 ? 376 GLU B OE2 1 
ATOM   7236 N N   . LYS B 1 377 ? -16.806 42.457 49.420  1.00 18.17 ? 377 LYS B N   1 
ATOM   7237 C CA  . LYS B 1 377 ? -16.236 43.004 50.638  1.00 19.82 ? 377 LYS B CA  1 
ATOM   7238 C C   . LYS B 1 377 ? -17.285 43.499 51.626  1.00 26.41 ? 377 LYS B C   1 
ATOM   7239 O O   . LYS B 1 377 ? -16.966 43.629 52.810  1.00 35.08 ? 377 LYS B O   1 
ATOM   7240 C CB  . LYS B 1 377 ? -15.248 44.132 50.299  1.00 27.58 ? 377 LYS B CB  1 
ATOM   7241 C CG  . LYS B 1 377 ? -14.025 43.635 49.522  1.00 35.17 ? 377 LYS B CG  1 
ATOM   7242 C CD  . LYS B 1 377 ? -12.871 44.624 49.549  1.00 47.32 ? 377 LYS B CD  1 
ATOM   7243 C CE  . LYS B 1 377 ? -12.189 44.733 48.184  1.00 54.19 ? 377 LYS B CE  1 
ATOM   7244 N NZ  . LYS B 1 377 ? -12.073 43.427 47.460  1.00 59.58 ? 377 LYS B NZ  1 
ATOM   7245 N N   . GLU B 1 378 ? -18.533 43.722 51.205  1.00 21.93 ? 378 GLU B N   1 
ATOM   7246 C CA  . GLU B 1 378 ? -19.563 44.197 52.132  1.00 20.04 ? 378 GLU B CA  1 
ATOM   7247 C C   . GLU B 1 378 ? -20.094 43.035 52.968  1.00 22.01 ? 378 GLU B C   1 
ATOM   7248 O O   . GLU B 1 378 ? -20.723 42.120 52.429  1.00 23.78 ? 378 GLU B O   1 
ATOM   7249 C CB  . GLU B 1 378 ? -20.719 44.855 51.379  1.00 21.61 ? 378 GLU B CB  1 
ATOM   7250 C CG  . GLU B 1 378 ? -20.314 45.923 50.383  1.00 25.12 ? 378 GLU B CG  1 
ATOM   7251 C CD  . GLU B 1 378 ? -20.013 47.276 51.013  1.00 30.80 ? 378 GLU B CD  1 
ATOM   7252 O OE1 . GLU B 1 378 ? -19.958 48.266 50.253  1.00 39.18 ? 378 GLU B OE1 1 
ATOM   7253 O OE2 . GLU B 1 378 ? -19.820 47.367 52.241  1.00 30.65 ? 378 GLU B OE2 1 
ATOM   7254 N N   . GLU B 1 379 ? -19.880 43.091 54.283  1.00 21.36 ? 379 GLU B N   1 
ATOM   7255 C CA  . GLU B 1 379 ? -20.298 42.000 55.158  1.00 23.89 ? 379 GLU B CA  1 
ATOM   7256 C C   . GLU B 1 379 ? -21.808 41.895 55.268  1.00 29.74 ? 379 GLU B C   1 
ATOM   7257 O O   . GLU B 1 379 ? -22.327 40.815 55.574  1.00 24.92 ? 379 GLU B O   1 
ATOM   7258 C CB  . GLU B 1 379 ? -19.709 42.186 56.558  1.00 28.15 ? 379 GLU B CB  1 
ATOM   7259 C CG  . GLU B 1 379 ? -18.211 41.929 56.673  1.00 32.48 ? 379 GLU B CG  1 
ATOM   7260 C CD  . GLU B 1 379 ? -17.714 42.108 58.101  1.00 37.86 ? 379 GLU B CD  1 
ATOM   7261 O OE1 . GLU B 1 379 ? -18.553 42.362 58.991  1.00 42.78 ? 379 GLU B OE1 1 
ATOM   7262 O OE2 . GLU B 1 379 ? -16.490 42.016 58.337  1.00 43.03 ? 379 GLU B OE2 1 
ATOM   7263 N N   . TRP B 1 380 ? -22.519 42.989 55.029  1.00 19.08 ? 380 TRP B N   1 
ATOM   7264 C CA  . TRP B 1 380 ? -23.954 43.048 55.241  1.00 19.75 ? 380 TRP B CA  1 
ATOM   7265 C C   . TRP B 1 380 ? -24.747 42.683 53.995  1.00 20.08 ? 380 TRP B C   1 
ATOM   7266 O O   . TRP B 1 380 ? -25.981 42.678 54.051  1.00 19.68 ? 380 TRP B O   1 
ATOM   7267 C CB  . TRP B 1 380 ? -24.350 44.448 55.725  1.00 20.75 ? 380 TRP B CB  1 
ATOM   7268 C CG  . TRP B 1 380 ? -23.802 45.543 54.863  1.00 22.69 ? 380 TRP B CG  1 
ATOM   7269 C CD1 . TRP B 1 380 ? -22.543 46.087 54.918  1.00 26.17 ? 380 TRP B CD1 1 
ATOM   7270 C CD2 . TRP B 1 380 ? -24.488 46.229 53.806  1.00 21.07 ? 380 TRP B CD2 1 
ATOM   7271 N NE1 . TRP B 1 380 ? -22.407 47.060 53.955  1.00 24.41 ? 380 TRP B NE1 1 
ATOM   7272 C CE2 . TRP B 1 380 ? -23.588 47.170 53.264  1.00 26.63 ? 380 TRP B CE2 1 
ATOM   7273 C CE3 . TRP B 1 380 ? -25.777 46.136 53.266  1.00 18.66 ? 380 TRP B CE3 1 
ATOM   7274 C CZ2 . TRP B 1 380 ? -23.936 48.014 52.205  1.00 27.11 ? 380 TRP B CZ2 1 
ATOM   7275 C CZ3 . TRP B 1 380 ? -26.124 46.980 52.214  1.00 22.10 ? 380 TRP B CZ3 1 
ATOM   7276 C CH2 . TRP B 1 380 ? -25.207 47.903 51.697  1.00 25.86 ? 380 TRP B CH2 1 
ATOM   7277 N N   . ILE B 1 381 ? -24.078 42.394 52.877  1.00 16.42 ? 381 ILE B N   1 
ATOM   7278 C CA  . ILE B 1 381 ? -24.717 41.908 51.661  1.00 16.64 ? 381 ILE B CA  1 
ATOM   7279 C C   . ILE B 1 381 ? -24.308 40.461 51.457  1.00 18.32 ? 381 ILE B C   1 
ATOM   7280 O O   . ILE B 1 381 ? -23.127 40.123 51.576  1.00 19.84 ? 381 ILE B O   1 
ATOM   7281 C CB  . ILE B 1 381 ? -24.330 42.738 50.425  1.00 18.02 ? 381 ILE B CB  1 
ATOM   7282 C CG1 . ILE B 1 381 ? -24.697 44.210 50.610  1.00 19.75 ? 381 ILE B CG1 1 
ATOM   7283 C CG2 . ILE B 1 381 ? -24.995 42.140 49.171  1.00 16.49 ? 381 ILE B CG2 1 
ATOM   7284 C CD1 . ILE B 1 381 ? -24.209 45.114 49.483  1.00 20.43 ? 381 ILE B CD1 1 
ATOM   7285 N N   . GLU B 1 382 ? -25.280 39.608 51.150  1.00 15.75 ? 382 GLU B N   1 
ATOM   7286 C CA  . GLU B 1 382 ? -25.014 38.238 50.743  1.00 17.93 ? 382 GLU B CA  1 
ATOM   7287 C C   . GLU B 1 382 ? -25.660 38.030 49.387  1.00 15.56 ? 382 GLU B C   1 
ATOM   7288 O O   . GLU B 1 382 ? -26.886 38.131 49.268  1.00 15.24 ? 382 GLU B O   1 
ATOM   7289 C CB  . GLU B 1 382 ? -25.570 37.249 51.766  1.00 17.12 ? 382 GLU B CB  1 
ATOM   7290 C CG  . GLU B 1 382 ? -25.387 35.792 51.404  1.00 28.10 ? 382 GLU B CG  1 
ATOM   7291 C CD  . GLU B 1 382 ? -25.571 34.888 52.607  1.00 45.88 ? 382 GLU B CD  1 
ATOM   7292 O OE1 . GLU B 1 382 ? -25.749 35.430 53.719  1.00 40.62 ? 382 GLU B OE1 1 
ATOM   7293 O OE2 . GLU B 1 382 ? -25.538 33.648 52.443  1.00 59.71 ? 382 GLU B OE2 1 
ATOM   7294 N N   . THR B 1 383 ? -24.846 37.781 48.363  1.00 15.79 ? 383 THR B N   1 
ATOM   7295 C CA  . THR B 1 383 ? -25.410 37.423 47.070  1.00 14.17 ? 383 THR B CA  1 
ATOM   7296 C C   . THR B 1 383 ? -25.862 35.970 47.125  1.00 15.46 ? 383 THR B C   1 
ATOM   7297 O O   . THR B 1 383 ? -25.228 35.134 47.781  1.00 17.13 ? 383 THR B O   1 
ATOM   7298 C CB  . THR B 1 383 ? -24.410 37.645 45.919  1.00 16.03 ? 383 THR B CB  1 
ATOM   7299 O OG1 . THR B 1 383 ? -23.181 36.945 46.171  1.00 16.00 ? 383 THR B OG1 1 
ATOM   7300 C CG2 . THR B 1 383 ? -24.118 39.139 45.734  1.00 18.21 ? 383 THR B CG2 1 
ATOM   7301 N N   . LEU B 1 384 ? -26.973 35.676 46.454  1.00 14.87 ? 384 LEU B N   1 
ATOM   7302 C CA  . LEU B 1 384 ? -27.587 34.352 46.493  1.00 12.00 ? 384 LEU B CA  1 
ATOM   7303 C C   . LEU B 1 384 ? -27.763 33.778 45.091  1.00 14.11 ? 384 LEU B C   1 
ATOM   7304 O O   . LEU B 1 384 ? -27.957 34.513 44.116  1.00 13.79 ? 384 LEU B O   1 
ATOM   7305 C CB  . LEU B 1 384 ? -28.972 34.383 47.184  1.00 15.82 ? 384 LEU B CB  1 
ATOM   7306 C CG  . LEU B 1 384 ? -29.079 34.916 48.621  1.00 13.99 ? 384 LEU B CG  1 
ATOM   7307 C CD1 . LEU B 1 384 ? -30.537 34.803 49.076  1.00 13.89 ? 384 LEU B CD1 1 
ATOM   7308 C CD2 . LEU B 1 384 ? -28.137 34.165 49.535  1.00 17.23 ? 384 LEU B CD2 1 
ATOM   7309 N N   . THR B 1 385 ? -27.679 32.451 44.999  1.00 15.50 ? 385 THR B N   1 
ATOM   7310 C CA  . THR B 1 385 ? -28.203 31.759 43.826  1.00 13.36 ? 385 THR B CA  1 
ATOM   7311 C C   . THR B 1 385 ? -29.730 31.797 43.850  1.00 12.74 ? 385 THR B C   1 
ATOM   7312 O O   . THR B 1 385 ? -30.353 32.073 44.883  1.00 14.15 ? 385 THR B O   1 
ATOM   7313 C CB  . THR B 1 385 ? -27.744 30.299 43.792  1.00 14.06 ? 385 THR B CB  1 
ATOM   7314 O OG1 . THR B 1 385 ? -28.354 29.587 44.881  1.00 17.79 ? 385 THR B OG1 1 
ATOM   7315 C CG2 . THR B 1 385 ? -26.225 30.198 43.896  1.00 17.50 ? 385 THR B CG2 1 
ATOM   7316 N N   . LEU B 1 386 ? -30.342 31.508 42.694  1.00 12.27 ? 386 LEU B N   1 
ATOM   7317 C CA  . LEU B 1 386 ? -31.799 31.385 42.657  1.00 12.80 ? 386 LEU B CA  1 
ATOM   7318 C C   . LEU B 1 386 ? -32.278 30.304 43.621  1.00 13.52 ? 386 LEU B C   1 
ATOM   7319 O O   . LEU B 1 386 ? -33.320 30.456 44.267  1.00 16.05 ? 386 LEU B O   1 
ATOM   7320 C CB  . LEU B 1 386 ? -32.275 31.060 41.237  1.00 12.66 ? 386 LEU B CB  1 
ATOM   7321 C CG  . LEU B 1 386 ? -31.913 32.064 40.142  1.00 12.66 ? 386 LEU B CG  1 
ATOM   7322 C CD1 . LEU B 1 386 ? -32.446 31.573 38.791  1.00 12.30 ? 386 LEU B CD1 1 
ATOM   7323 C CD2 . LEU B 1 386 ? -32.471 33.440 40.472  1.00 14.41 ? 386 LEU B CD2 1 
ATOM   7324 N N   . GLU B 1 387 ? -31.540 29.192 43.712  1.00 16.61 ? 387 GLU B N   1 
ATOM   7325 C CA  . GLU B 1 387 ? -31.903 28.122 44.634  1.00 16.78 ? 387 GLU B CA  1 
ATOM   7326 C C   . GLU B 1 387 ? -31.942 28.622 46.072  1.00 16.56 ? 387 GLU B C   1 
ATOM   7327 O O   . GLU B 1 387 ? -32.895 28.357 46.813  1.00 21.22 ? 387 GLU B O   1 
ATOM   7328 C CB  . GLU B 1 387 ? -30.906 26.962 44.508  1.00 19.87 ? 387 GLU B CB  1 
ATOM   7329 C CG  . GLU B 1 387 ? -31.092 25.889 45.563  1.00 32.18 ? 387 GLU B CG  1 
ATOM   7330 C CD  . GLU B 1 387 ? -31.769 24.661 45.014  1.00 52.83 ? 387 GLU B CD  1 
ATOM   7331 O OE1 . GLU B 1 387 ? -31.337 23.541 45.362  1.00 61.91 ? 387 GLU B OE1 1 
ATOM   7332 O OE2 . GLU B 1 387 ? -32.731 24.818 44.231  1.00 50.89 ? 387 GLU B OE2 1 
ATOM   7333 N N   . GLU B 1 388 ? -30.907 29.353 46.484  1.00 16.77 ? 388 GLU B N   1 
ATOM   7334 C CA  . GLU B 1 388 ? -30.870 29.876 47.846  1.00 14.91 ? 388 GLU B CA  1 
ATOM   7335 C C   . GLU B 1 388 ? -31.988 30.878 48.102  1.00 17.60 ? 388 GLU B C   1 
ATOM   7336 O O   . GLU B 1 388 ? -32.581 30.889 49.187  1.00 17.88 ? 388 GLU B O   1 
ATOM   7337 C CB  . GLU B 1 388 ? -29.510 30.520 48.114  1.00 17.46 ? 388 GLU B CB  1 
ATOM   7338 C CG  . GLU B 1 388 ? -28.393 29.509 48.071  1.00 16.46 ? 388 GLU B CG  1 
ATOM   7339 C CD  . GLU B 1 388 ? -27.008 30.120 48.074  1.00 22.88 ? 388 GLU B CD  1 
ATOM   7340 O OE1 . GLU B 1 388 ? -26.827 31.249 47.566  1.00 22.20 ? 388 GLU B OE1 1 
ATOM   7341 O OE2 . GLU B 1 388 ? -26.089 29.449 48.581  1.00 28.59 ? 388 GLU B OE2 1 
ATOM   7342 N N   . ALA B 1 389 ? -32.268 31.747 47.131  1.00 13.57 ? 389 ALA B N   1 
ATOM   7343 C CA  . ALA B 1 389 ? -33.329 32.736 47.299  1.00 14.64 ? 389 ALA B CA  1 
ATOM   7344 C C   . ALA B 1 389 ? -34.681 32.057 47.421  1.00 19.17 ? 389 ALA B C   1 
ATOM   7345 O O   . ALA B 1 389 ? -35.524 32.465 48.231  1.00 17.70 ? 389 ALA B O   1 
ATOM   7346 C CB  . ALA B 1 389 ? -33.332 33.711 46.121  1.00 16.02 ? 389 ALA B CB  1 
ATOM   7347 N N   . MET B 1 390 ? -34.885 30.996 46.636  1.00 16.41 ? 390 MET B N   1 
ATOM   7348 C CA  . MET B 1 390 ? -36.144 30.265 46.665  1.00 16.96 ? 390 MET B CA  1 
ATOM   7349 C C   . MET B 1 390 ? -36.398 29.639 48.030  1.00 22.08 ? 390 MET B C   1 
ATOM   7350 O O   . MET B 1 390 ? -37.539 29.612 48.498  1.00 21.11 ? 390 MET B O   1 
ATOM   7351 C CB  . MET B 1 390 ? -36.135 29.190 45.581  1.00 19.32 ? 390 MET B CB  1 
ATOM   7352 C CG  . MET B 1 390 ? -37.418 28.404 45.473  1.00 22.13 ? 390 MET B CG  1 
ATOM   7353 S SD  . MET B 1 390 ? -37.337 27.252 44.082  1.00 27.20 ? 390 MET B SD  1 
ATOM   7354 C CE  . MET B 1 390 ? -36.223 25.995 44.713  1.00 31.78 ? 390 MET B CE  1 
ATOM   7355 N N   . ARG B 1 391 ? -35.347 29.141 48.690  1.00 23.22 ? 391 ARG B N   1 
ATOM   7356 C CA  . ARG B 1 391 ? -35.517 28.333 49.891  1.00 18.99 ? 391 ARG B CA  1 
ATOM   7357 C C   . ARG B 1 391 ? -35.084 29.024 51.175  1.00 19.45 ? 391 ARG B C   1 
ATOM   7358 O O   . ARG B 1 391 ? -35.278 28.450 52.247  1.00 21.09 ? 391 ARG B O   1 
ATOM   7359 C CB  . ARG B 1 391 ? -34.763 27.003 49.753  1.00 30.99 ? 391 ARG B CB  1 
ATOM   7360 C CG  . ARG B 1 391 ? -35.009 26.312 48.422  1.00 36.92 ? 391 ARG B CG  1 
ATOM   7361 C CD  . ARG B 1 391 ? -34.166 25.067 48.223  1.00 43.43 ? 391 ARG B CD  1 
ATOM   7362 N NE  . ARG B 1 391 ? -34.936 24.046 47.516  1.00 55.64 ? 391 ARG B NE  1 
ATOM   7363 C CZ  . ARG B 1 391 ? -34.419 22.944 46.984  1.00 66.39 ? 391 ARG B CZ  1 
ATOM   7364 N NH1 . ARG B 1 391 ? -33.116 22.711 47.072  1.00 70.53 ? 391 ARG B NH1 1 
ATOM   7365 N NH2 . ARG B 1 391 ? -35.205 22.079 46.356  1.00 67.64 ? 391 ARG B NH2 1 
ATOM   7366 N N   . LYS B 1 392 ? -34.520 30.232 51.104  1.00 18.42 ? 392 LYS B N   1 
ATOM   7367 C CA  . LYS B 1 392 ? -34.024 30.890 52.312  1.00 20.66 ? 392 LYS B CA  1 
ATOM   7368 C C   . LYS B 1 392 ? -35.141 31.037 53.341  1.00 26.03 ? 392 LYS B C   1 
ATOM   7369 O O   . LYS B 1 392 ? -36.231 31.526 53.028  1.00 25.13 ? 392 LYS B O   1 
ATOM   7370 C CB  . LYS B 1 392 ? -33.442 32.258 51.960  1.00 22.86 ? 392 LYS B CB  1 
ATOM   7371 C CG  . LYS B 1 392 ? -32.660 32.896 53.081  1.00 28.27 ? 392 LYS B CG  1 
ATOM   7372 C CD  . LYS B 1 392 ? -31.361 33.472 52.566  1.00 42.65 ? 392 LYS B CD  1 
ATOM   7373 C CE  . LYS B 1 392 ? -30.236 32.471 52.680  1.00 37.86 ? 392 LYS B CE  1 
ATOM   7374 N NZ  . LYS B 1 392 ? -29.867 32.284 54.103  1.00 40.39 ? 392 LYS B NZ  1 
ATOM   7375 N N   . GLU B 1 393 ? -34.879 30.582 54.570  1.00 22.40 ? 393 GLU B N   1 
ATOM   7376 C CA  . GLU B 1 393 ? -35.924 30.604 55.589  1.00 24.26 ? 393 GLU B CA  1 
ATOM   7377 C C   . GLU B 1 393 ? -36.097 31.985 56.216  1.00 26.16 ? 393 GLU B C   1 
ATOM   7378 O O   . GLU B 1 393 ? -37.224 32.397 56.513  1.00 31.41 ? 393 GLU B O   1 
ATOM   7379 C CB  . GLU B 1 393 ? -35.613 29.583 56.686  1.00 30.30 ? 393 GLU B CB  1 
ATOM   7380 C CG  . GLU B 1 393 ? -36.520 28.370 56.691  1.00 38.80 ? 393 GLU B CG  1 
ATOM   7381 C CD  . GLU B 1 393 ? -35.968 27.247 57.546  1.00 60.38 ? 393 GLU B CD  1 
ATOM   7382 O OE1 . GLU B 1 393 ? -35.589 27.509 58.710  1.00 67.16 ? 393 GLU B OE1 1 
ATOM   7383 O OE2 . GLU B 1 393 ? -35.903 26.104 57.048  1.00 67.14 ? 393 GLU B OE2 1 
ATOM   7384 N N   . ASP B 1 394 ? -35.002 32.702 56.437  1.00 22.30 ? 394 ASP B N   1 
ATOM   7385 C CA  . ASP B 1 394 ? -35.033 33.931 57.229  1.00 25.20 ? 394 ASP B CA  1 
ATOM   7386 C C   . ASP B 1 394 ? -35.333 35.156 56.370  1.00 24.96 ? 394 ASP B C   1 
ATOM   7387 O O   . ASP B 1 394 ? -34.603 36.141 56.385  1.00 22.70 ? 394 ASP B O   1 
ATOM   7388 C CB  . ASP B 1 394 ? -33.712 34.092 57.973  1.00 25.85 ? 394 ASP B CB  1 
ATOM   7389 C CG  . ASP B 1 394 ? -32.510 33.711 57.121  1.00 46.66 ? 394 ASP B CG  1 
ATOM   7390 O OD1 . ASP B 1 394 ? -32.658 32.838 56.239  1.00 50.07 ? 394 ASP B OD1 1 
ATOM   7391 O OD2 . ASP B 1 394 ? -31.414 34.275 57.338  1.00 50.92 ? 394 ASP B OD2 1 
ATOM   7392 N N   . VAL B 1 395 ? -36.420 35.096 55.606  1.00 19.69 ? 395 VAL B N   1 
ATOM   7393 C CA  . VAL B 1 395 ? -36.879 36.212 54.792  1.00 17.30 ? 395 VAL B CA  1 
ATOM   7394 C C   . VAL B 1 395 ? -38.357 36.432 55.097  1.00 23.38 ? 395 VAL B C   1 
ATOM   7395 O O   . VAL B 1 395 ? -39.013 35.613 55.742  1.00 24.84 ? 395 VAL B O   1 
ATOM   7396 C CB  . VAL B 1 395 ? -36.651 35.975 53.283  1.00 19.05 ? 395 VAL B CB  1 
ATOM   7397 C CG1 . VAL B 1 395 ? -35.162 35.796 52.996  1.00 21.23 ? 395 VAL B CG1 1 
ATOM   7398 C CG2 . VAL B 1 395 ? -37.421 34.763 52.813  1.00 22.83 ? 395 VAL B CG2 1 
ATOM   7399 N N   . LYS B 1 396 ? -38.872 37.568 54.648  1.00 17.98 ? 396 LYS B N   1 
ATOM   7400 C CA  . LYS B 1 396 ? -40.273 37.889 54.854  1.00 18.90 ? 396 LYS B CA  1 
ATOM   7401 C C   . LYS B 1 396 ? -41.058 37.425 53.637  1.00 18.62 ? 396 LYS B C   1 
ATOM   7402 O O   . LYS B 1 396 ? -40.598 37.575 52.504  1.00 17.75 ? 396 LYS B O   1 
ATOM   7403 C CB  . LYS B 1 396 ? -40.457 39.392 55.070  1.00 19.27 ? 396 LYS B CB  1 
ATOM   7404 C CG  . LYS B 1 396 ? -41.866 39.789 55.466  1.00 20.52 ? 396 LYS B CG  1 
ATOM   7405 C CD  . LYS B 1 396 ? -41.925 41.234 55.952  1.00 31.20 ? 396 LYS B CD  1 
ATOM   7406 C CE  . LYS B 1 396 ? -43.361 41.686 56.193  1.00 28.28 ? 396 LYS B CE  1 
ATOM   7407 N NZ  . LYS B 1 396 ? -43.433 43.147 56.546  1.00 25.08 ? 396 LYS B NZ  1 
ATOM   7408 N N   . THR B 1 397 ? -42.236 36.846 53.877  1.00 14.52 ? 397 THR B N   1 
ATOM   7409 C CA  . THR B 1 397 ? -43.054 36.296 52.804  1.00 15.59 ? 397 THR B CA  1 
ATOM   7410 C C   . THR B 1 397 ? -44.470 36.847 52.861  1.00 18.88 ? 397 THR B C   1 
ATOM   7411 O O   . THR B 1 397 ? -44.911 37.404 53.872  1.00 23.53 ? 397 THR B O   1 
ATOM   7412 C CB  . THR B 1 397 ? -43.125 34.757 52.841  1.00 20.16 ? 397 THR B CB  1 
ATOM   7413 O OG1 . THR B 1 397 ? -43.827 34.326 54.016  1.00 22.45 ? 397 THR B OG1 1 
ATOM   7414 C CG2 . THR B 1 397 ? -41.731 34.141 52.830  1.00 21.64 ? 397 THR B CG2 1 
ATOM   7415 N N   . GLU B 1 398 ? -45.174 36.693 51.740  1.00 20.38 ? 398 GLU B N   1 
ATOM   7416 C CA  . GLU B 1 398 ? -46.562 37.119 51.623  1.00 17.56 ? 398 GLU B CA  1 
ATOM   7417 C C   . GLU B 1 398 ? -47.239 36.272 50.557  1.00 19.82 ? 398 GLU B C   1 
ATOM   7418 O O   . GLU B 1 398 ? -46.626 35.918 49.540  1.00 16.71 ? 398 GLU B O   1 
ATOM   7419 C CB  . GLU B 1 398 ? -46.653 38.617 51.282  1.00 18.96 ? 398 GLU B CB  1 
ATOM   7420 C CG  . GLU B 1 398 ? -48.049 39.158 50.984  1.00 19.79 ? 398 GLU B CG  1 
ATOM   7421 C CD  . GLU B 1 398 ? -48.059 40.675 50.855  1.00 28.97 ? 398 GLU B CD  1 
ATOM   7422 O OE1 . GLU B 1 398 ? -49.066 41.245 50.372  1.00 33.82 ? 398 GLU B OE1 1 
ATOM   7423 O OE2 . GLU B 1 398 ? -47.052 41.303 51.242  1.00 31.29 ? 398 GLU B OE2 1 
ATOM   7424 N N   . VAL B 1 399 ? -48.486 35.912 50.818  1.00 20.37 ? 399 VAL B N   1 
ATOM   7425 C CA  . VAL B 1 399 ? -49.320 35.213 49.849  1.00 20.00 ? 399 VAL B CA  1 
ATOM   7426 C C   . VAL B 1 399 ? -50.077 36.257 49.046  1.00 22.48 ? 399 VAL B C   1 
ATOM   7427 O O   . VAL B 1 399 ? -50.630 37.203 49.619  1.00 19.62 ? 399 VAL B O   1 
ATOM   7428 C CB  . VAL B 1 399 ? -50.303 34.265 50.555  1.00 22.41 ? 399 VAL B CB  1 
ATOM   7429 C CG1 . VAL B 1 399 ? -51.153 33.516 49.536  1.00 24.53 ? 399 VAL B CG1 1 
ATOM   7430 C CG2 . VAL B 1 399 ? -49.574 33.313 51.493  1.00 18.66 ? 399 VAL B CG2 1 
ATOM   7431 N N   . ILE B 1 400 ? -50.117 36.089 47.728  1.00 16.91 ? 400 ILE B N   1 
ATOM   7432 C CA  . ILE B 1 400 ? -50.948 36.941 46.888  1.00 20.00 ? 400 ILE B CA  1 
ATOM   7433 C C   . ILE B 1 400 ? -51.852 36.050 46.048  1.00 21.22 ? 400 ILE B C   1 
ATOM   7434 O O   . ILE B 1 400 ? -51.494 34.921 45.700  1.00 22.56 ? 400 ILE B O   1 
ATOM   7435 C CB  . ILE B 1 400 ? -50.125 37.899 45.999  1.00 24.53 ? 400 ILE B CB  1 
ATOM   7436 C CG1 . ILE B 1 400 ? -49.116 37.136 45.156  1.00 30.85 ? 400 ILE B CG1 1 
ATOM   7437 C CG2 . ILE B 1 400 ? -49.433 38.976 46.860  1.00 23.53 ? 400 ILE B CG2 1 
ATOM   7438 C CD1 . ILE B 1 400 ? -48.395 38.018 44.169  1.00 36.46 ? 400 ILE B CD1 1 
ATOM   7439 N N   . GLU B 1 401 ? -53.047 36.554 45.746  1.00 19.34 ? 401 GLU B N   1 
ATOM   7440 C CA  . GLU B 1 401 ? -54.061 35.733 45.110  1.00 20.88 ? 401 GLU B CA  1 
ATOM   7441 C C   . GLU B 1 401 ? -54.322 36.085 43.655  1.00 18.37 ? 401 GLU B C   1 
ATOM   7442 O O   . GLU B 1 401 ? -55.061 35.350 42.988  1.00 23.58 ? 401 GLU B O   1 
ATOM   7443 C CB  . GLU B 1 401 ? -55.376 35.825 45.890  1.00 23.53 ? 401 GLU B CB  1 
ATOM   7444 C CG  . GLU B 1 401 ? -55.223 35.513 47.371  1.00 33.14 ? 401 GLU B CG  1 
ATOM   7445 C CD  . GLU B 1 401 ? -54.991 34.032 47.655  1.00 41.24 ? 401 GLU B CD  1 
ATOM   7446 O OE1 . GLU B 1 401 ? -55.143 33.202 46.733  1.00 36.23 ? 401 GLU B OE1 1 
ATOM   7447 O OE2 . GLU B 1 401 ? -54.669 33.697 48.817  1.00 45.70 ? 401 GLU B OE2 1 
ATOM   7448 N N   . SER B 1 402 ? -53.753 37.174 43.148  1.00 19.60 ? 402 SER B N   1 
ATOM   7449 C CA  . SER B 1 402 ? -54.103 37.630 41.808  1.00 19.19 ? 402 SER B CA  1 
ATOM   7450 C C   . SER B 1 402 ? -53.088 38.661 41.339  1.00 26.93 ? 402 SER B C   1 
ATOM   7451 O O   . SER B 1 402 ? -52.627 39.489 42.130  1.00 24.10 ? 402 SER B O   1 
ATOM   7452 C CB  . SER B 1 402 ? -55.513 38.239 41.801  1.00 20.33 ? 402 SER B CB  1 
ATOM   7453 O OG  . SER B 1 402 ? -55.919 38.603 40.493  1.00 26.92 ? 402 SER B OG  1 
ATOM   7454 N N   . VAL B 1 403 ? -52.746 38.615 40.052  1.00 18.27 ? 403 VAL B N   1 
ATOM   7455 C CA  . VAL B 1 403 ? -51.952 39.679 39.453  1.00 18.91 ? 403 VAL B CA  1 
ATOM   7456 C C   . VAL B 1 403 ? -52.728 40.266 38.288  1.00 21.07 ? 403 VAL B C   1 
ATOM   7457 O O   . VAL B 1 403 ? -53.588 39.611 37.693  1.00 20.35 ? 403 VAL B O   1 
ATOM   7458 C CB  . VAL B 1 403 ? -50.561 39.207 38.980  1.00 15.62 ? 403 VAL B CB  1 
ATOM   7459 C CG1 . VAL B 1 403 ? -49.795 38.582 40.132  1.00 19.43 ? 403 VAL B CG1 1 
ATOM   7460 C CG2 . VAL B 1 403 ? -50.687 38.224 37.826  1.00 19.39 ? 403 VAL B CG2 1 
ATOM   7461 N N   . LYS B 1 404 ? -52.423 41.524 37.985  1.00 20.60 ? 404 LYS B N   1 
ATOM   7462 C CA  . LYS B 1 404 ? -52.880 42.175 36.769  1.00 19.33 ? 404 LYS B CA  1 
ATOM   7463 C C   . LYS B 1 404 ? -51.874 41.884 35.663  1.00 17.86 ? 404 LYS B C   1 
ATOM   7464 O O   . LYS B 1 404 ? -50.682 42.187 35.800  1.00 20.52 ? 404 LYS B O   1 
ATOM   7465 C CB  . LYS B 1 404 ? -53.041 43.679 36.983  1.00 28.40 ? 404 LYS B CB  1 
ATOM   7466 C CG  . LYS B 1 404 ? -54.073 44.046 38.037  1.00 32.66 ? 404 LYS B CG  1 
ATOM   7467 C CD  . LYS B 1 404 ? -54.823 45.334 37.676  1.00 39.69 ? 404 LYS B CD  1 
ATOM   7468 C CE  . LYS B 1 404 ? -56.239 45.301 38.220  1.00 51.10 ? 404 LYS B CE  1 
ATOM   7469 N NZ  . LYS B 1 404 ? -56.756 43.899 38.296  1.00 61.15 ? 404 LYS B NZ  1 
ATOM   7470 N N   . ALA B 1 405 ? -52.353 41.279 34.578  1.00 18.67 ? 405 ALA B N   1 
ATOM   7471 C CA  . ALA B 1 405 ? -51.467 40.843 33.507  1.00 19.09 ? 405 ALA B CA  1 
ATOM   7472 C C   . ALA B 1 405 ? -50.674 42.015 32.949  1.00 17.13 ? 405 ALA B C   1 
ATOM   7473 O O   . ALA B 1 405 ? -51.205 43.110 32.764  1.00 18.47 ? 405 ALA B O   1 
ATOM   7474 C CB  . ALA B 1 405 ? -52.282 40.178 32.399  1.00 20.45 ? 405 ALA B CB  1 
ATOM   7475 N N   . GLY B 1 406 ? -49.401 41.777 32.664  1.00 17.86 ? 406 GLY B N   1 
ATOM   7476 C CA  . GLY B 1 406 ? -48.570 42.846 32.146  1.00 16.20 ? 406 GLY B CA  1 
ATOM   7477 C C   . GLY B 1 406 ? -47.198 42.325 31.791  1.00 16.97 ? 406 GLY B C   1 
ATOM   7478 O O   . GLY B 1 406 ? -46.965 41.120 31.756  1.00 15.35 ? 406 GLY B O   1 
ATOM   7479 N N   . THR B 1 407 ? -46.297 43.264 31.500  1.00 12.67 ? 407 THR B N   1 
ATOM   7480 C CA  . THR B 1 407 ? -44.896 42.999 31.205  1.00 14.05 ? 407 THR B CA  1 
ATOM   7481 C C   . THR B 1 407 ? -44.064 44.036 31.936  1.00 13.84 ? 407 THR B C   1 
ATOM   7482 O O   . THR B 1 407 ? -44.599 44.963 32.554  1.00 18.26 ? 407 THR B O   1 
ATOM   7483 C CB  . THR B 1 407 ? -44.567 43.098 29.711  1.00 14.22 ? 407 THR B CB  1 
ATOM   7484 O OG1 . THR B 1 407 ? -44.511 44.483 29.345  1.00 15.24 ? 407 THR B OG1 1 
ATOM   7485 C CG2 . THR B 1 407 ? -45.614 42.392 28.864  1.00 19.78 ? 407 THR B CG2 1 
ATOM   7486 N N   . TRP B 1 408 ? -42.739 43.923 31.819  1.00 14.04 ? 408 TRP B N   1 
ATOM   7487 C CA  . TRP B 1 408 ? -41.895 44.943 32.426  1.00 13.01 ? 408 TRP B CA  1 
ATOM   7488 C C   . TRP B 1 408 ? -41.792 46.219 31.598  1.00 19.34 ? 408 TRP B C   1 
ATOM   7489 O O   . TRP B 1 408 ? -41.056 47.127 31.992  1.00 19.29 ? 408 TRP B O   1 
ATOM   7490 C CB  . TRP B 1 408 ? -40.494 44.397 32.717  1.00 15.92 ? 408 TRP B CB  1 
ATOM   7491 C CG  . TRP B 1 408 ? -39.705 43.861 31.554  1.00 12.28 ? 408 TRP B CG  1 
ATOM   7492 C CD1 . TRP B 1 408 ? -40.045 43.866 30.231  1.00 17.80 ? 408 TRP B CD1 1 
ATOM   7493 C CD2 . TRP B 1 408 ? -38.427 43.221 31.641  1.00 12.29 ? 408 TRP B CD2 1 
ATOM   7494 N NE1 . TRP B 1 408 ? -39.050 43.263 29.488  1.00 18.14 ? 408 TRP B NE1 1 
ATOM   7495 C CE2 . TRP B 1 408 ? -38.048 42.858 30.330  1.00 16.32 ? 408 TRP B CE2 1 
ATOM   7496 C CE3 . TRP B 1 408 ? -37.569 42.920 32.700  1.00 14.57 ? 408 TRP B CE3 1 
ATOM   7497 C CZ2 . TRP B 1 408 ? -36.833 42.213 30.051  1.00 17.32 ? 408 TRP B CZ2 1 
ATOM   7498 C CZ3 . TRP B 1 408 ? -36.368 42.279 32.429  1.00 19.19 ? 408 TRP B CZ3 1 
ATOM   7499 C CH2 . TRP B 1 408 ? -36.008 41.931 31.106  1.00 19.42 ? 408 TRP B CH2 1 
ATOM   7500 N N   . PHE B 1 409 ? -42.516 46.333 30.486  1.00 17.81 ? 409 PHE B N   1 
ATOM   7501 C CA  . PHE B 1 409 ? -42.636 47.611 29.783  1.00 21.67 ? 409 PHE B CA  1 
ATOM   7502 C C   . PHE B 1 409 ? -43.954 48.240 30.225  1.00 20.52 ? 409 PHE B C   1 
ATOM   7503 O O   . PHE B 1 409 ? -45.027 47.878 29.735  1.00 20.26 ? 409 PHE B O   1 
ATOM   7504 C CB  . PHE B 1 409 ? -42.565 47.433 28.271  1.00 26.68 ? 409 PHE B CB  1 
ATOM   7505 C CG  . PHE B 1 409 ? -41.973 48.620 27.554  1.00 43.54 ? 409 PHE B CG  1 
ATOM   7506 C CD1 . PHE B 1 409 ? -42.711 49.773 27.350  1.00 50.77 ? 409 PHE B CD1 1 
ATOM   7507 C CD2 . PHE B 1 409 ? -40.667 48.587 27.101  1.00 51.61 ? 409 PHE B CD2 1 
ATOM   7508 C CE1 . PHE B 1 409 ? -42.155 50.865 26.692  1.00 55.52 ? 409 PHE B CE1 1 
ATOM   7509 C CE2 . PHE B 1 409 ? -40.104 49.663 26.449  1.00 58.58 ? 409 PHE B CE2 1 
ATOM   7510 C CZ  . PHE B 1 409 ? -40.847 50.807 26.244  1.00 60.41 ? 409 PHE B CZ  1 
ATOM   7511 N N   . ASP B 1 410 ? -43.868 49.166 31.179  1.00 23.66 ? 410 ASP B N   1 
ATOM   7512 C CA  . ASP B 1 410 ? -45.013 49.921 31.679  1.00 27.54 ? 410 ASP B CA  1 
ATOM   7513 C C   . ASP B 1 410 ? -46.136 49.034 32.198  1.00 25.51 ? 410 ASP B C   1 
ATOM   7514 O O   . ASP B 1 410 ? -47.285 49.475 32.267  1.00 28.15 ? 410 ASP B O   1 
ATOM   7515 C CB  . ASP B 1 410 ? -45.559 50.870 30.605  1.00 35.15 ? 410 ASP B CB  1 
ATOM   7516 C CG  . ASP B 1 410 ? -44.556 51.925 30.199  1.00 47.18 ? 410 ASP B CG  1 
ATOM   7517 O OD1 . ASP B 1 410 ? -43.673 52.257 31.021  1.00 49.71 ? 410 ASP B OD1 1 
ATOM   7518 O OD2 . ASP B 1 410 ? -44.657 52.426 29.061  1.00 50.29 ? 410 ASP B OD2 1 
ATOM   7519 N N   . GLY B 1 411 ? -45.837 47.787 32.561  1.00 23.54 ? 411 GLY B N   1 
ATOM   7520 C CA  . GLY B 1 411 ? -46.861 46.900 33.074  1.00 20.83 ? 411 GLY B CA  1 
ATOM   7521 C C   . GLY B 1 411 ? -47.933 46.513 32.084  1.00 24.73 ? 411 GLY B C   1 
ATOM   7522 O O   . GLY B 1 411 ? -48.998 46.051 32.494  1.00 22.65 ? 411 GLY B O   1 
ATOM   7523 N N   . ASN B 1 412 ? -47.698 46.691 30.786  1.00 21.08 ? 412 ASN B N   1 
ATOM   7524 C CA  . ASN B 1 412 ? -48.724 46.376 29.806  1.00 20.64 ? 412 ASN B CA  1 
ATOM   7525 C C   . ASN B 1 412 ? -48.083 45.733 28.584  1.00 21.07 ? 412 ASN B C   1 
ATOM   7526 O O   . ASN B 1 412 ? -46.873 45.465 28.548  1.00 21.38 ? 412 ASN B O   1 
ATOM   7527 C CB  . ASN B 1 412 ? -49.564 47.620 29.459  1.00 21.23 ? 412 ASN B CB  1 
ATOM   7528 C CG  . ASN B 1 412 ? -48.778 48.710 28.733  1.00 23.88 ? 412 ASN B CG  1 
ATOM   7529 O OD1 . ASN B 1 412 ? -48.019 48.445 27.796  1.00 23.55 ? 412 ASN B OD1 1 
ATOM   7530 N ND2 . ASN B 1 412 ? -48.996 49.957 29.145  1.00 25.04 ? 412 ASN B ND2 1 
ATOM   7531 N N   . PHE B 1 413 ? -48.912 45.495 27.568  1.00 19.59 ? 413 PHE B N   1 
ATOM   7532 C CA  . PHE B 1 413 ? -48.525 44.729 26.390  1.00 17.36 ? 413 PHE B CA  1 
ATOM   7533 C C   . PHE B 1 413 ? -48.368 45.587 25.141  1.00 21.46 ? 413 PHE B C   1 
ATOM   7534 O O   . PHE B 1 413 ? -48.237 45.036 24.041  1.00 19.38 ? 413 PHE B O   1 
ATOM   7535 C CB  . PHE B 1 413 ? -49.553 43.628 26.131  1.00 18.10 ? 413 PHE B CB  1 
ATOM   7536 C CG  . PHE B 1 413 ? -49.556 42.567 27.179  1.00 18.94 ? 413 PHE B CG  1 
ATOM   7537 C CD1 . PHE B 1 413 ? -48.628 41.537 27.140  1.00 19.01 ? 413 PHE B CD1 1 
ATOM   7538 C CD2 . PHE B 1 413 ? -50.479 42.605 28.219  1.00 16.70 ? 413 PHE B CD2 1 
ATOM   7539 C CE1 . PHE B 1 413 ? -48.625 40.553 28.117  1.00 19.44 ? 413 PHE B CE1 1 
ATOM   7540 C CE2 . PHE B 1 413 ? -50.483 41.621 29.200  1.00 19.16 ? 413 PHE B CE2 1 
ATOM   7541 C CZ  . PHE B 1 413 ? -49.551 40.601 29.152  1.00 17.38 ? 413 PHE B CZ  1 
ATOM   7542 N N   . LEU B 1 414 ? -48.361 46.915 25.288  1.00 19.93 ? 414 LEU B N   1 
ATOM   7543 C CA  . LEU B 1 414 ? -48.422 47.809 24.139  1.00 21.55 ? 414 LEU B CA  1 
ATOM   7544 C C   . LEU B 1 414 ? -47.161 47.788 23.288  1.00 23.09 ? 414 LEU B C   1 
ATOM   7545 O O   . LEU B 1 414 ? -47.206 48.244 22.143  1.00 24.57 ? 414 LEU B O   1 
ATOM   7546 C CB  . LEU B 1 414 ? -48.701 49.233 24.606  1.00 27.18 ? 414 LEU B CB  1 
ATOM   7547 C CG  . LEU B 1 414 ? -50.103 49.390 25.180  1.00 24.46 ? 414 LEU B CG  1 
ATOM   7548 C CD1 . LEU B 1 414 ? -50.362 50.842 25.554  1.00 22.42 ? 414 LEU B CD1 1 
ATOM   7549 C CD2 . LEU B 1 414 ? -51.127 48.908 24.169  1.00 24.31 ? 414 LEU B CD2 1 
ATOM   7550 N N   . LYS B 1 415 ? -46.038 47.283 23.803  1.00 19.72 ? 415 LYS B N   1 
ATOM   7551 C CA  . LYS B 1 415 ? -44.865 47.193 22.940  1.00 23.47 ? 415 LYS B CA  1 
ATOM   7552 C C   . LYS B 1 415 ? -44.968 46.057 21.935  1.00 18.81 ? 415 LYS B C   1 
ATOM   7553 O O   . LYS B 1 415 ? -44.141 45.986 21.021  1.00 18.87 ? 415 LYS B O   1 
ATOM   7554 C CB  . LYS B 1 415 ? -43.580 47.035 23.763  1.00 21.23 ? 415 LYS B CB  1 
ATOM   7555 C CG  . LYS B 1 415 ? -42.956 48.372 24.163  1.00 36.40 ? 415 LYS B CG  1 
ATOM   7556 C CD  . LYS B 1 415 ? -42.349 49.103 22.966  1.00 46.98 ? 415 LYS B CD  1 
ATOM   7557 C CE  . LYS B 1 415 ? -42.606 50.606 23.037  1.00 56.13 ? 415 LYS B CE  1 
ATOM   7558 N NZ  . LYS B 1 415 ? -41.677 51.395 22.172  1.00 55.49 ? 415 LYS B NZ  1 
ATOM   7559 N N   . TRP B 1 416 ? -45.971 45.185 22.058  1.00 20.26 ? 416 TRP B N   1 
ATOM   7560 C CA  . TRP B 1 416 ? -46.103 44.051 21.157  1.00 19.91 ? 416 TRP B CA  1 
ATOM   7561 C C   . TRP B 1 416 ? -47.458 43.931 20.481  1.00 19.26 ? 416 TRP B C   1 
ATOM   7562 O O   . TRP B 1 416 ? -47.611 43.062 19.613  1.00 18.73 ? 416 TRP B O   1 
ATOM   7563 C CB  . TRP B 1 416 ? -45.820 42.741 21.908  1.00 15.32 ? 416 TRP B CB  1 
ATOM   7564 C CG  . TRP B 1 416 ? -44.483 42.759 22.583  1.00 17.63 ? 416 TRP B CG  1 
ATOM   7565 C CD1 . TRP B 1 416 ? -43.299 42.313 22.074  1.00 18.36 ? 416 TRP B CD1 1 
ATOM   7566 C CD2 . TRP B 1 416 ? -44.187 43.286 23.885  1.00 16.97 ? 416 TRP B CD2 1 
ATOM   7567 N NE1 . TRP B 1 416 ? -42.285 42.512 22.985  1.00 16.92 ? 416 TRP B NE1 1 
ATOM   7568 C CE2 . TRP B 1 416 ? -42.805 43.104 24.106  1.00 17.49 ? 416 TRP B CE2 1 
ATOM   7569 C CE3 . TRP B 1 416 ? -44.961 43.884 24.887  1.00 18.07 ? 416 TRP B CE3 1 
ATOM   7570 C CZ2 . TRP B 1 416 ? -42.174 43.511 25.284  1.00 15.10 ? 416 TRP B CZ2 1 
ATOM   7571 C CZ3 . TRP B 1 416 ? -44.332 44.279 26.065  1.00 18.39 ? 416 TRP B CZ3 1 
ATOM   7572 C CH2 . TRP B 1 416 ? -42.955 44.090 26.249  1.00 17.89 ? 416 TRP B CH2 1 
ATOM   7573 N N   . ILE B 1 417 ? -48.443 44.754 20.841  1.00 19.00 ? 417 ILE B N   1 
ATOM   7574 C CA  . ILE B 1 417 ? -49.791 44.621 20.296  1.00 18.46 ? 417 ILE B CA  1 
ATOM   7575 C C   . ILE B 1 417 ? -50.520 45.935 20.534  1.00 25.20 ? 417 ILE B C   1 
ATOM   7576 O O   . ILE B 1 417 ? -50.157 46.713 21.420  1.00 26.41 ? 417 ILE B O   1 
ATOM   7577 C CB  . ILE B 1 417 ? -50.532 43.421 20.946  1.00 20.15 ? 417 ILE B CB  1 
ATOM   7578 C CG1 . ILE B 1 417 ? -51.723 42.978 20.096  1.00 22.74 ? 417 ILE B CG1 1 
ATOM   7579 C CG2 . ILE B 1 417 ? -50.966 43.747 22.384  1.00 20.80 ? 417 ILE B CG2 1 
ATOM   7580 C CD1 . ILE B 1 417 ? -52.279 41.637 20.523  1.00 19.43 ? 417 ILE B CD1 1 
ATOM   7581 N N   . GLY B 1 418 ? -51.541 46.203 19.723  1.00 24.99 ? 418 GLY B N   1 
ATOM   7582 C CA  . GLY B 1 418 ? -52.396 47.350 19.954  1.00 24.23 ? 418 GLY B CA  1 
ATOM   7583 C C   . GLY B 1 418 ? -52.223 48.525 19.015  1.00 33.94 ? 418 GLY B C   1 
ATOM   7584 O O   . GLY B 1 418 ? -52.978 49.496 19.140  1.00 39.87 ? 418 GLY B O   1 
ATOM   7585 N N   . ASN B 1 419 ? -51.263 48.494 18.097  1.00 29.66 ? 419 ASN B N   1 
ATOM   7586 C CA  . ASN B 1 419 ? -51.205 49.484 17.032  1.00 32.06 ? 419 ASN B CA  1 
ATOM   7587 C C   . ASN B 1 419 ? -51.364 48.768 15.695  1.00 27.32 ? 419 ASN B C   1 
ATOM   7588 O O   . ASN B 1 419 ? -51.364 47.538 15.628  1.00 26.41 ? 419 ASN B O   1 
ATOM   7589 C CB  . ASN B 1 419 ? -49.917 50.326 17.118  1.00 37.84 ? 419 ASN B CB  1 
ATOM   7590 C CG  . ASN B 1 419 ? -48.696 49.653 16.494  1.00 37.14 ? 419 ASN B CG  1 
ATOM   7591 O OD1 . ASN B 1 419 ? -48.718 48.485 16.129  1.00 33.97 ? 419 ASN B OD1 1 
ATOM   7592 N ND2 . ASN B 1 419 ? -47.609 50.410 16.388  1.00 43.97 ? 419 ASN B ND2 1 
ATOM   7593 N N   . LYS B 1 420 ? -51.504 49.546 14.623  1.00 30.12 ? 420 LYS B N   1 
ATOM   7594 C CA  . LYS B 1 420 ? -51.866 48.968 13.331  1.00 30.25 ? 420 LYS B CA  1 
ATOM   7595 C C   . LYS B 1 420 ? -50.821 47.965 12.847  1.00 30.22 ? 420 LYS B C   1 
ATOM   7596 O O   . LYS B 1 420 ? -51.162 46.860 12.407  1.00 29.81 ? 420 LYS B O   1 
ATOM   7597 C CB  . LYS B 1 420 ? -52.063 50.081 12.300  1.00 35.14 ? 420 LYS B CB  1 
ATOM   7598 C CG  . LYS B 1 420 ? -52.425 49.579 10.922  1.00 38.30 ? 420 LYS B CG  1 
ATOM   7599 C CD  . LYS B 1 420 ? -52.429 50.722 9.926   1.00 47.81 ? 420 LYS B CD  1 
ATOM   7600 C CE  . LYS B 1 420 ? -53.751 51.471 9.957   1.00 57.88 ? 420 LYS B CE  1 
ATOM   7601 N NZ  . LYS B 1 420 ? -54.426 51.449 8.629   1.00 64.58 ? 420 LYS B NZ  1 
ATOM   7602 N N   . GLU B 1 421 ? -49.536 48.327 12.933  1.00 30.16 ? 421 GLU B N   1 
ATOM   7603 C CA  . GLU B 1 421 ? -48.497 47.462 12.380  1.00 28.72 ? 421 GLU B CA  1 
ATOM   7604 C C   . GLU B 1 421 ? -48.280 46.219 13.242  1.00 21.50 ? 421 GLU B C   1 
ATOM   7605 O O   . GLU B 1 421 ? -48.128 45.112 12.713  1.00 27.41 ? 421 GLU B O   1 
ATOM   7606 C CB  . GLU B 1 421 ? -47.189 48.238 12.217  1.00 31.83 ? 421 GLU B CB  1 
ATOM   7607 C CG  . GLU B 1 421 ? -47.271 49.410 11.238  1.00 44.61 ? 421 GLU B CG  1 
ATOM   7608 C CD  . GLU B 1 421 ? -46.743 49.066 9.851   1.00 63.81 ? 421 GLU B CD  1 
ATOM   7609 O OE1 . GLU B 1 421 ? -46.822 49.932 8.950   1.00 72.90 ? 421 GLU B OE1 1 
ATOM   7610 O OE2 . GLU B 1 421 ? -46.250 47.934 9.659   1.00 69.15 ? 421 GLU B OE2 1 
ATOM   7611 N N   . LYS B 1 422 ? -48.253 46.371 14.566  1.00 20.17 ? 422 LYS B N   1 
ATOM   7612 C CA  . LYS B 1 422 ? -48.093 45.184 15.402  1.00 18.74 ? 422 LYS B CA  1 
ATOM   7613 C C   . LYS B 1 422 ? -49.319 44.281 15.324  1.00 23.86 ? 422 LYS B C   1 
ATOM   7614 O O   . LYS B 1 422 ? -49.183 43.054 15.370  1.00 24.78 ? 422 LYS B O   1 
ATOM   7615 C CB  . LYS B 1 422 ? -47.810 45.582 16.856  1.00 19.78 ? 422 LYS B CB  1 
ATOM   7616 C CG  . LYS B 1 422 ? -46.483 46.336 17.047  1.00 20.86 ? 422 LYS B CG  1 
ATOM   7617 C CD  . LYS B 1 422 ? -46.356 46.868 18.475  1.00 21.91 ? 422 LYS B CD  1 
ATOM   7618 C CE  . LYS B 1 422 ? -45.168 47.797 18.629  1.00 22.93 ? 422 LYS B CE  1 
ATOM   7619 N NZ  . LYS B 1 422 ? -43.879 47.119 18.314  1.00 19.22 ? 422 LYS B NZ  1 
ATOM   7620 N N   . ASN B 1 423 ? -50.515 44.862 15.183  1.00 22.44 ? 423 ASN B N   1 
ATOM   7621 C CA  . ASN B 1 423 ? -51.709 44.037 15.042  1.00 23.03 ? 423 ASN B CA  1 
ATOM   7622 C C   . ASN B 1 423 ? -51.666 43.216 13.759  1.00 26.18 ? 423 ASN B C   1 
ATOM   7623 O O   . ASN B 1 423 ? -52.152 42.080 13.725  1.00 23.73 ? 423 ASN B O   1 
ATOM   7624 C CB  . ASN B 1 423 ? -52.965 44.909 15.078  1.00 27.81 ? 423 ASN B CB  1 
ATOM   7625 C CG  . ASN B 1 423 ? -53.348 45.330 16.491  1.00 31.47 ? 423 ASN B CG  1 
ATOM   7626 O OD1 . ASN B 1 423 ? -52.719 44.918 17.468  1.00 26.44 ? 423 ASN B OD1 1 
ATOM   7627 N ND2 . ASN B 1 423 ? -54.378 46.170 16.599  1.00 30.96 ? 423 ASN B ND2 1 
ATOM   7628 N N   . GLU B 1 424 ? -51.094 43.773 12.689  1.00 28.28 ? 424 GLU B N   1 
ATOM   7629 C CA  . GLU B 1 424 ? -50.996 43.022 11.439  1.00 32.06 ? 424 GLU B CA  1 
ATOM   7630 C C   . GLU B 1 424 ? -50.134 41.772 11.607  1.00 30.38 ? 424 GLU B C   1 
ATOM   7631 O O   . GLU B 1 424 ? -50.420 40.730 11.004  1.00 26.03 ? 424 GLU B O   1 
ATOM   7632 C CB  . GLU B 1 424 ? -50.444 43.917 10.331  1.00 36.04 ? 424 GLU B CB  1 
ATOM   7633 C CG  . GLU B 1 424 ? -50.199 43.203 9.009   1.00 41.38 ? 424 GLU B CG  1 
ATOM   7634 C CD  . GLU B 1 424 ? -51.466 42.619 8.400   1.00 55.14 ? 424 GLU B CD  1 
ATOM   7635 O OE1 . GLU B 1 424 ? -51.366 41.597 7.689   1.00 59.65 ? 424 GLU B OE1 1 
ATOM   7636 O OE2 . GLU B 1 424 ? -52.559 43.186 8.620   1.00 57.64 ? 424 GLU B OE2 1 
ATOM   7637 N N   . TYR B 1 425 ? -49.081 41.847 12.429  1.00 26.12 ? 425 TYR B N   1 
ATOM   7638 C CA  . TYR B 1 425 ? -48.318 40.639 12.728  1.00 23.73 ? 425 TYR B CA  1 
ATOM   7639 C C   . TYR B 1 425 ? -49.183 39.598 13.431  1.00 25.95 ? 425 TYR B C   1 
ATOM   7640 O O   . TYR B 1 425 ? -49.136 38.410 13.092  1.00 24.59 ? 425 TYR B O   1 
ATOM   7641 C CB  . TYR B 1 425 ? -47.087 40.964 13.578  1.00 19.56 ? 425 TYR B CB  1 
ATOM   7642 C CG  . TYR B 1 425 ? -45.824 41.186 12.777  1.00 19.29 ? 425 TYR B CG  1 
ATOM   7643 C CD1 . TYR B 1 425 ? -45.873 41.643 11.463  1.00 19.90 ? 425 TYR B CD1 1 
ATOM   7644 C CD2 . TYR B 1 425 ? -44.579 40.938 13.341  1.00 22.97 ? 425 TYR B CD2 1 
ATOM   7645 C CE1 . TYR B 1 425 ? -44.703 41.856 10.736  1.00 25.08 ? 425 TYR B CE1 1 
ATOM   7646 C CE2 . TYR B 1 425 ? -43.417 41.144 12.629  1.00 19.10 ? 425 TYR B CE2 1 
ATOM   7647 C CZ  . TYR B 1 425 ? -43.481 41.595 11.325  1.00 20.29 ? 425 TYR B CZ  1 
ATOM   7648 O OH  . TYR B 1 425 ? -42.321 41.808 10.616  1.00 23.83 ? 425 TYR B OH  1 
ATOM   7649 N N   . TRP B 1 426 ? -49.965 40.013 14.432  1.00 20.88 ? 426 TRP B N   1 
ATOM   7650 C CA  . TRP B 1 426 ? -50.837 39.047 15.099  1.00 21.16 ? 426 TRP B CA  1 
ATOM   7651 C C   . TRP B 1 426 ? -51.870 38.480 14.130  1.00 29.10 ? 426 TRP B C   1 
ATOM   7652 O O   . TRP B 1 426 ? -52.122 37.266 14.124  1.00 24.00 ? 426 TRP B O   1 
ATOM   7653 C CB  . TRP B 1 426 ? -51.512 39.676 16.323  1.00 23.16 ? 426 TRP B CB  1 
ATOM   7654 C CG  . TRP B 1 426 ? -50.527 39.883 17.442  1.00 16.82 ? 426 TRP B CG  1 
ATOM   7655 C CD1 . TRP B 1 426 ? -49.886 41.040 17.762  1.00 21.41 ? 426 TRP B CD1 1 
ATOM   7656 C CD2 . TRP B 1 426 ? -50.031 38.885 18.349  1.00 16.97 ? 426 TRP B CD2 1 
ATOM   7657 N NE1 . TRP B 1 426 ? -49.039 40.835 18.821  1.00 18.76 ? 426 TRP B NE1 1 
ATOM   7658 C CE2 . TRP B 1 426 ? -49.108 39.521 19.200  1.00 17.77 ? 426 TRP B CE2 1 
ATOM   7659 C CE3 . TRP B 1 426 ? -50.286 37.520 18.526  1.00 24.96 ? 426 TRP B CE3 1 
ATOM   7660 C CZ2 . TRP B 1 426 ? -48.436 38.846 20.214  1.00 22.42 ? 426 TRP B CZ2 1 
ATOM   7661 C CZ3 . TRP B 1 426 ? -49.610 36.846 19.544  1.00 20.46 ? 426 TRP B CZ3 1 
ATOM   7662 C CH2 . TRP B 1 426 ? -48.702 37.511 20.370  1.00 20.70 ? 426 TRP B CH2 1 
ATOM   7663 N N   . LYS B 1 427 ? -52.459 39.337 13.284  1.00 26.32 ? 427 LYS B N   1 
ATOM   7664 C CA  . LYS B 1 427 ? -53.390 38.843 12.270  1.00 25.20 ? 427 LYS B CA  1 
ATOM   7665 C C   . LYS B 1 427 ? -52.722 37.803 11.378  1.00 26.91 ? 427 LYS B C   1 
ATOM   7666 O O   . LYS B 1 427 ? -53.308 36.747 11.091  1.00 27.04 ? 427 LYS B O   1 
ATOM   7667 C CB  . LYS B 1 427 ? -53.924 40.002 11.423  1.00 29.31 ? 427 LYS B CB  1 
ATOM   7668 C CG  . LYS B 1 427 ? -54.711 41.039 12.198  1.00 38.30 ? 427 LYS B CG  1 
ATOM   7669 C CD  . LYS B 1 427 ? -55.509 41.942 11.268  1.00 46.76 ? 427 LYS B CD  1 
ATOM   7670 C CE  . LYS B 1 427 ? -54.860 43.305 11.132  1.00 52.54 ? 427 LYS B CE  1 
ATOM   7671 N NZ  . LYS B 1 427 ? -54.879 43.791 9.723   1.00 55.75 ? 427 LYS B NZ  1 
ATOM   7672 N N   . ILE B 1 428 ? -51.493 38.088 10.937  1.00 26.65 ? 428 ILE B N   1 
ATOM   7673 C CA  . ILE B 1 428 ? -50.729 37.140 10.129  1.00 32.17 ? 428 ILE B CA  1 
ATOM   7674 C C   . ILE B 1 428 ? -50.511 35.847 10.896  1.00 29.60 ? 428 ILE B C   1 
ATOM   7675 O O   . ILE B 1 428 ? -50.637 34.748 10.343  1.00 31.27 ? 428 ILE B O   1 
ATOM   7676 C CB  . ILE B 1 428 ? -49.387 37.765 9.705   1.00 25.37 ? 428 ILE B CB  1 
ATOM   7677 C CG1 . ILE B 1 428 ? -49.590 38.847 8.641   1.00 26.52 ? 428 ILE B CG1 1 
ATOM   7678 C CG2 . ILE B 1 428 ? -48.414 36.691 9.219   1.00 27.35 ? 428 ILE B CG2 1 
ATOM   7679 C CD1 . ILE B 1 428 ? -48.414 39.795 8.541   1.00 26.56 ? 428 ILE B CD1 1 
ATOM   7680 N N   . LEU B 1 429 ? -50.177 35.957 12.183  1.00 21.83 ? 429 LEU B N   1 
ATOM   7681 C CA  . LEU B 1 429 ? -49.938 34.766 12.987  1.00 25.42 ? 429 LEU B CA  1 
ATOM   7682 C C   . LEU B 1 429 ? -51.222 33.970 13.196  1.00 25.68 ? 429 LEU B C   1 
ATOM   7683 O O   . LEU B 1 429 ? -51.207 32.736 13.136  1.00 27.93 ? 429 LEU B O   1 
ATOM   7684 C CB  . LEU B 1 429 ? -49.320 35.167 14.325  1.00 24.72 ? 429 LEU B CB  1 
ATOM   7685 C CG  . LEU B 1 429 ? -48.992 34.020 15.287  1.00 25.05 ? 429 LEU B CG  1 
ATOM   7686 C CD1 . LEU B 1 429 ? -47.902 33.132 14.722  1.00 28.04 ? 429 LEU B CD1 1 
ATOM   7687 C CD2 . LEU B 1 429 ? -48.603 34.554 16.659  1.00 26.43 ? 429 LEU B CD2 1 
ATOM   7688 N N   . ILE B 1 430 ? -52.341 34.659 13.442  1.00 26.41 ? 430 ILE B N   1 
ATOM   7689 C CA  . ILE B 1 430 ? -53.617 33.975 13.637  1.00 28.76 ? 430 ILE B CA  1 
ATOM   7690 C C   . ILE B 1 430 ? -54.004 33.202 12.386  1.00 27.20 ? 430 ILE B C   1 
ATOM   7691 O O   . ILE B 1 430 ? -54.451 32.052 12.462  1.00 35.42 ? 430 ILE B O   1 
ATOM   7692 C CB  . ILE B 1 430 ? -54.707 34.985 14.041  1.00 27.82 ? 430 ILE B CB  1 
ATOM   7693 C CG1 . ILE B 1 430 ? -54.462 35.475 15.467  1.00 27.42 ? 430 ILE B CG1 1 
ATOM   7694 C CG2 . ILE B 1 430 ? -56.099 34.370 13.907  1.00 30.06 ? 430 ILE B CG2 1 
ATOM   7695 C CD1 . ILE B 1 430 ? -54.910 36.904 15.711  1.00 29.00 ? 430 ILE B CD1 1 
ATOM   7696 N N   . GLU B 1 431 ? -53.843 33.819 11.215  1.00 29.68 ? 431 GLU B N   1 
ATOM   7697 C CA  . GLU B 1 431 ? -54.218 33.146 9.975   1.00 37.66 ? 431 GLU B CA  1 
ATOM   7698 C C   . GLU B 1 431 ? -53.330 31.935 9.718   1.00 37.02 ? 431 GLU B C   1 
ATOM   7699 O O   . GLU B 1 431 ? -53.816 30.876 9.299   1.00 35.43 ? 431 GLU B O   1 
ATOM   7700 C CB  . GLU B 1 431 ? -54.149 34.130 8.808   1.00 36.27 ? 431 GLU B CB  1 
ATOM   7701 C CG  . GLU B 1 431 ? -55.432 34.909 8.599   1.00 48.82 ? 431 GLU B CG  1 
ATOM   7702 C CD  . GLU B 1 431 ? -56.655 34.008 8.574   1.00 58.33 ? 431 GLU B CD  1 
ATOM   7703 O OE1 . GLU B 1 431 ? -57.577 34.233 9.386   1.00 60.36 ? 431 GLU B OE1 1 
ATOM   7704 O OE2 . GLU B 1 431 ? -56.689 33.070 7.746   1.00 61.08 ? 431 GLU B OE2 1 
ATOM   7705 N N   . ALA B 1 432 ? -52.027 32.074 9.980   1.00 34.65 ? 432 ALA B N   1 
ATOM   7706 C CA  . ALA B 1 432 ? -51.091 30.977 9.761   1.00 31.94 ? 432 ALA B CA  1 
ATOM   7707 C C   . ALA B 1 432 ? -51.302 29.846 10.760  1.00 30.64 ? 432 ALA B C   1 
ATOM   7708 O O   . ALA B 1 432 ? -51.109 28.674 10.417  1.00 33.72 ? 432 ALA B O   1 
ATOM   7709 C CB  . ALA B 1 432 ? -49.654 31.493 9.848   1.00 27.40 ? 432 ALA B CB  1 
ATOM   7710 N N   . LYS B 1 433 ? -51.680 30.177 11.999  1.00 28.92 ? 433 LYS B N   1 
ATOM   7711 C CA  . LYS B 1 433 ? -51.943 29.143 12.995  1.00 31.85 ? 433 LYS B CA  1 
ATOM   7712 C C   . LYS B 1 433 ? -53.044 28.193 12.529  1.00 34.35 ? 433 LYS B C   1 
ATOM   7713 O O   . LYS B 1 433 ? -52.963 26.982 12.760  1.00 36.40 ? 433 LYS B O   1 
ATOM   7714 C CB  . LYS B 1 433 ? -52.309 29.791 14.331  1.00 31.14 ? 433 LYS B CB  1 
ATOM   7715 C CG  . LYS B 1 433 ? -52.669 28.803 15.434  1.00 34.69 ? 433 LYS B CG  1 
ATOM   7716 C CD  . LYS B 1 433 ? -51.487 27.932 15.837  1.00 32.66 ? 433 LYS B CD  1 
ATOM   7717 C CE  . LYS B 1 433 ? -51.925 26.865 16.836  1.00 35.52 ? 433 LYS B CE  1 
ATOM   7718 N NZ  . LYS B 1 433 ? -50.854 25.863 17.112  1.00 35.30 ? 433 LYS B NZ  1 
ATOM   7719 N N   . LYS B 1 434 ? -54.068 28.723 11.848  1.00 37.50 ? 434 LYS B N   1 
ATOM   7720 C CA  . LYS B 1 434 ? -55.136 27.876 11.316  1.00 34.39 ? 434 LYS B CA  1 
ATOM   7721 C C   . LYS B 1 434 ? -54.603 26.806 10.372  1.00 40.72 ? 434 LYS B C   1 
ATOM   7722 O O   . LYS B 1 434 ? -55.174 25.712 10.287  1.00 44.03 ? 434 LYS B O   1 
ATOM   7723 C CB  . LYS B 1 434 ? -56.167 28.715 10.559  1.00 45.72 ? 434 LYS B CB  1 
ATOM   7724 C CG  . LYS B 1 434 ? -56.956 29.728 11.358  1.00 45.32 ? 434 LYS B CG  1 
ATOM   7725 C CD  . LYS B 1 434 ? -57.842 30.513 10.395  1.00 47.18 ? 434 LYS B CD  1 
ATOM   7726 C CE  . LYS B 1 434 ? -58.857 31.379 11.107  1.00 47.83 ? 434 LYS B CE  1 
ATOM   7727 N NZ  . LYS B 1 434 ? -58.201 32.314 12.051  1.00 51.04 ? 434 LYS B NZ  1 
ATOM   7728 N N   . LYS B 1 435 ? -53.535 27.112 9.632   1.00 40.36 ? 435 LYS B N   1 
ATOM   7729 C CA  . LYS B 1 435 ? -52.975 26.215 8.629   1.00 39.60 ? 435 LYS B CA  1 
ATOM   7730 C C   . LYS B 1 435 ? -51.621 25.646 9.043   1.00 42.28 ? 435 LYS B C   1 
ATOM   7731 O O   . LYS B 1 435 ? -50.890 25.123 8.197   1.00 42.79 ? 435 LYS B O   1 
ATOM   7732 C CB  . LYS B 1 435 ? -52.850 26.940 7.288   1.00 44.12 ? 435 LYS B CB  1 
ATOM   7733 C CG  . LYS B 1 435 ? -53.976 27.922 6.993   1.00 49.06 ? 435 LYS B CG  1 
ATOM   7734 C CD  . LYS B 1 435 ? -53.881 28.447 5.568   1.00 54.29 ? 435 LYS B CD  1 
ATOM   7735 C CE  . LYS B 1 435 ? -54.525 29.820 5.420   1.00 57.16 ? 435 LYS B CE  1 
ATOM   7736 N NZ  . LYS B 1 435 ? -54.689 30.198 3.981   1.00 58.96 ? 435 LYS B NZ  1 
ATOM   7737 N N   . ALA B 1 436 ? -51.277 25.728 10.324  1.00 33.11 ? 436 ALA B N   1 
ATOM   7738 C CA  . ALA B 1 436 ? -49.926 25.389 10.753  1.00 31.52 ? 436 ALA B CA  1 
ATOM   7739 C C   . ALA B 1 436 ? -49.716 23.880 10.739  1.00 37.64 ? 436 ALA B C   1 
ATOM   7740 O O   . ALA B 1 436 ? -50.606 23.108 11.110  1.00 38.98 ? 436 ALA B O   1 
ATOM   7741 C CB  . ALA B 1 436 ? -49.658 25.956 12.148  1.00 29.56 ? 436 ALA B CB  1 
ATOM   7742 N N   . LYS B 1 437 ? -48.529 23.460 10.286  1.00 34.57 ? 437 LYS B N   1 
ATOM   7743 C CA  . LYS B 1 437 ? -48.208 22.046 10.148  1.00 41.95 ? 437 LYS B CA  1 
ATOM   7744 C C   . LYS B 1 437 ? -46.962 21.615 10.913  1.00 39.79 ? 437 LYS B C   1 
ATOM   7745 O O   . LYS B 1 437 ? -46.697 20.408 10.990  1.00 44.60 ? 437 LYS B O   1 
ATOM   7746 C CB  . LYS B 1 437 ? -48.024 21.671 8.666   1.00 47.27 ? 437 LYS B CB  1 
ATOM   7747 C CG  . LYS B 1 437 ? -48.972 22.370 7.693   1.00 48.36 ? 437 LYS B CG  1 
ATOM   7748 C CD  . LYS B 1 437 ? -50.380 21.801 7.752   1.00 51.08 ? 437 LYS B CD  1 
ATOM   7749 C CE  . LYS B 1 437 ? -51.185 22.165 6.504   1.00 58.12 ? 437 LYS B CE  1 
ATOM   7750 N NZ  . LYS B 1 437 ? -51.345 23.642 6.331   1.00 57.00 ? 437 LYS B NZ  1 
ATOM   7751 N N   . ASN B 1 438 ? -46.193 22.545 11.472  1.00 33.97 ? 438 ASN B N   1 
ATOM   7752 C CA  . ASN B 1 438 ? -44.964 22.197 12.171  1.00 35.31 ? 438 ASN B CA  1 
ATOM   7753 C C   . ASN B 1 438 ? -44.660 23.266 13.214  1.00 35.52 ? 438 ASN B C   1 
ATOM   7754 O O   . ASN B 1 438 ? -45.357 24.279 13.321  1.00 34.70 ? 438 ASN B O   1 
ATOM   7755 C CB  . ASN B 1 438 ? -43.809 22.036 11.184  1.00 37.75 ? 438 ASN B CB  1 
ATOM   7756 C CG  . ASN B 1 438 ? -43.625 23.254 10.315  1.00 32.26 ? 438 ASN B CG  1 
ATOM   7757 O OD1 . ASN B 1 438 ? -43.243 24.308 10.802  1.00 30.10 ? 438 ASN B OD1 1 
ATOM   7758 N ND2 . ASN B 1 438 ? -43.892 23.114 9.020   1.00 36.50 ? 438 ASN B ND2 1 
ATOM   7759 N N   . ASP B 1 439 ? -43.586 23.045 13.971  1.00 30.76 ? 439 ASP B N   1 
ATOM   7760 C CA  . ASP B 1 439 ? -43.249 23.909 15.096  1.00 28.86 ? 439 ASP B CA  1 
ATOM   7761 C C   . ASP B 1 439 ? -42.638 25.237 14.682  1.00 27.92 ? 439 ASP B C   1 
ATOM   7762 O O   . ASP B 1 439 ? -42.314 26.053 15.556  1.00 25.09 ? 439 ASP B O   1 
ATOM   7763 C CB  . ASP B 1 439 ? -42.298 23.183 16.044  1.00 34.47 ? 439 ASP B CB  1 
ATOM   7764 C CG  . ASP B 1 439 ? -43.014 22.190 16.916  1.00 39.30 ? 439 ASP B CG  1 
ATOM   7765 O OD1 . ASP B 1 439 ? -44.265 22.219 16.928  1.00 36.38 ? 439 ASP B OD1 1 
ATOM   7766 O OD2 . ASP B 1 439 ? -42.332 21.379 17.578  1.00 49.33 ? 439 ASP B OD2 1 
ATOM   7767 N N   . TYR B 1 440 ? -42.468 25.496 13.386  1.00 27.35 ? 440 TYR B N   1 
ATOM   7768 C CA  . TYR B 1 440 ? -42.057 26.841 13.012  1.00 22.04 ? 440 TYR B CA  1 
ATOM   7769 C C   . TYR B 1 440 ? -43.100 27.872 13.413  1.00 26.93 ? 440 TYR B C   1 
ATOM   7770 O O   . TYR B 1 440 ? -42.773 29.053 13.520  1.00 22.40 ? 440 TYR B O   1 
ATOM   7771 C CB  . TYR B 1 440 ? -41.765 26.923 11.518  1.00 24.50 ? 440 TYR B CB  1 
ATOM   7772 C CG  . TYR B 1 440 ? -40.316 26.659 11.200  1.00 30.93 ? 440 TYR B CG  1 
ATOM   7773 C CD1 . TYR B 1 440 ? -39.343 27.606 11.494  1.00 33.33 ? 440 TYR B CD1 1 
ATOM   7774 C CD2 . TYR B 1 440 ? -39.914 25.454 10.631  1.00 32.44 ? 440 TYR B CD2 1 
ATOM   7775 C CE1 . TYR B 1 440 ? -38.012 27.369 11.215  1.00 39.21 ? 440 TYR B CE1 1 
ATOM   7776 C CE2 . TYR B 1 440 ? -38.579 25.207 10.345  1.00 36.61 ? 440 TYR B CE2 1 
ATOM   7777 C CZ  . TYR B 1 440 ? -37.634 26.174 10.643  1.00 42.61 ? 440 TYR B CZ  1 
ATOM   7778 O OH  . TYR B 1 440 ? -36.303 25.955 10.372  1.00 47.03 ? 440 TYR B OH  1 
ATOM   7779 N N   . ILE B 1 441 ? -44.343 27.454 13.668  1.00 23.95 ? 441 ILE B N   1 
ATOM   7780 C CA  . ILE B 1 441 ? -45.317 28.413 14.176  1.00 21.61 ? 441 ILE B CA  1 
ATOM   7781 C C   . ILE B 1 441 ? -44.923 28.874 15.575  1.00 20.07 ? 441 ILE B C   1 
ATOM   7782 O O   . ILE B 1 441 ? -45.184 30.023 15.956  1.00 19.37 ? 441 ILE B O   1 
ATOM   7783 C CB  . ILE B 1 441 ? -46.743 27.823 14.134  1.00 22.20 ? 441 ILE B CB  1 
ATOM   7784 C CG1 . ILE B 1 441 ? -47.779 28.940 14.297  1.00 21.93 ? 441 ILE B CG1 1 
ATOM   7785 C CG2 . ILE B 1 441 ? -46.935 26.735 15.190  1.00 25.50 ? 441 ILE B CG2 1 
ATOM   7786 C CD1 . ILE B 1 441 ? -47.924 29.808 13.047  1.00 22.26 ? 441 ILE B CD1 1 
ATOM   7787 N N   . LEU B 1 442 ? -44.261 28.013 16.350  1.00 19.01 ? 442 LEU B N   1 
ATOM   7788 C CA  . LEU B 1 442 ? -43.760 28.436 17.653  1.00 21.07 ? 442 LEU B CA  1 
ATOM   7789 C C   . LEU B 1 442 ? -42.671 29.487 17.502  1.00 21.80 ? 442 LEU B C   1 
ATOM   7790 O O   . LEU B 1 442 ? -42.577 30.415 18.314  1.00 20.16 ? 442 LEU B O   1 
ATOM   7791 C CB  . LEU B 1 442 ? -43.220 27.236 18.431  1.00 19.99 ? 442 LEU B CB  1 
ATOM   7792 C CG  . LEU B 1 442 ? -44.139 26.024 18.643  1.00 22.65 ? 442 LEU B CG  1 
ATOM   7793 C CD1 . LEU B 1 442 ? -43.413 24.923 19.398  1.00 27.68 ? 442 LEU B CD1 1 
ATOM   7794 C CD2 . LEU B 1 442 ? -45.401 26.438 19.378  1.00 25.91 ? 442 LEU B CD2 1 
ATOM   7795 N N   . VAL B 1 443 ? -41.821 29.336 16.486  1.00 18.18 ? 443 VAL B N   1 
ATOM   7796 C CA  . VAL B 1 443 ? -40.760 30.313 16.253  1.00 19.81 ? 443 VAL B CA  1 
ATOM   7797 C C   . VAL B 1 443 ? -41.363 31.685 16.003  1.00 21.59 ? 443 VAL B C   1 
ATOM   7798 O O   . VAL B 1 443 ? -40.880 32.699 16.524  1.00 17.54 ? 443 VAL B O   1 
ATOM   7799 C CB  . VAL B 1 443 ? -39.873 29.880 15.070  1.00 21.93 ? 443 VAL B CB  1 
ATOM   7800 C CG1 . VAL B 1 443 ? -38.776 30.902 14.843  1.00 16.94 ? 443 VAL B CG1 1 
ATOM   7801 C CG2 . VAL B 1 443 ? -39.279 28.497 15.309  1.00 22.34 ? 443 VAL B CG2 1 
ATOM   7802 N N   . ALA B 1 444 ? -42.427 31.732 15.195  1.00 19.38 ? 444 ALA B N   1 
ATOM   7803 C CA  . ALA B 1 444 ? -43.114 32.973 14.857  1.00 19.94 ? 444 ALA B CA  1 
ATOM   7804 C C   . ALA B 1 444 ? -43.858 33.571 16.040  1.00 22.05 ? 444 ALA B C   1 
ATOM   7805 O O   . ALA B 1 444 ? -44.268 34.731 15.968  1.00 21.27 ? 444 ALA B O   1 
ATOM   7806 C CB  . ALA B 1 444 ? -44.092 32.741 13.704  1.00 21.51 ? 444 ALA B CB  1 
ATOM   7807 N N   . GLU B 1 445 ? -44.050 32.815 17.114  1.00 16.39 ? 445 GLU B N   1 
ATOM   7808 C CA  . GLU B 1 445 ? -44.687 33.356 18.309  1.00 17.07 ? 445 GLU B CA  1 
ATOM   7809 C C   . GLU B 1 445 ? -43.710 34.110 19.211  1.00 19.02 ? 445 GLU B C   1 
ATOM   7810 O O   . GLU B 1 445 ? -44.143 34.696 20.214  1.00 19.91 ? 445 GLU B O   1 
ATOM   7811 C CB  . GLU B 1 445 ? -45.389 32.221 19.068  1.00 21.21 ? 445 GLU B CB  1 
ATOM   7812 C CG  . GLU B 1 445 ? -46.696 31.795 18.369  1.00 20.02 ? 445 GLU B CG  1 
ATOM   7813 C CD  . GLU B 1 445 ? -47.173 30.395 18.713  1.00 22.66 ? 445 GLU B CD  1 
ATOM   7814 O OE1 . GLU B 1 445 ? -46.673 29.799 19.689  1.00 20.27 ? 445 GLU B OE1 1 
ATOM   7815 O OE2 . GLU B 1 445 ? -48.068 29.889 17.995  1.00 24.70 ? 445 GLU B OE2 1 
ATOM   7816 N N   . GLY B 1 446 ? -42.423 34.140 18.860  1.00 18.07 ? 446 GLY B N   1 
ATOM   7817 C CA  . GLY B 1 446 ? -41.446 34.833 19.687  1.00 16.73 ? 446 GLY B CA  1 
ATOM   7818 C C   . GLY B 1 446 ? -41.725 36.319 19.786  1.00 21.13 ? 446 GLY B C   1 
ATOM   7819 O O   . GLY B 1 446 ? -42.230 36.948 18.849  1.00 22.89 ? 446 GLY B O   1 
ATOM   7820 N N   . SER B 1 447 ? -41.397 36.888 20.951  1.00 18.03 ? 447 SER B N   1 
ATOM   7821 C CA  . SER B 1 447 ? -41.773 38.276 21.214  1.00 20.69 ? 447 SER B CA  1 
ATOM   7822 C C   . SER B 1 447 ? -41.030 39.243 20.307  1.00 18.41 ? 447 SER B C   1 
ATOM   7823 O O   . SER B 1 447 ? -41.560 40.315 19.982  1.00 15.70 ? 447 SER B O   1 
ATOM   7824 C CB  . SER B 1 447 ? -41.517 38.629 22.681  1.00 17.79 ? 447 SER B CB  1 
ATOM   7825 O OG  . SER B 1 447 ? -40.127 38.603 22.999  1.00 17.30 ? 447 SER B OG  1 
ATOM   7826 N N   . ASP B 1 448 ? -39.820 38.874 19.880  1.00 14.65 ? 448 ASP B N   1 
ATOM   7827 C CA  . ASP B 1 448 ? -38.949 39.815 19.182  1.00 16.97 ? 448 ASP B CA  1 
ATOM   7828 C C   . ASP B 1 448 ? -39.581 40.356 17.909  1.00 15.57 ? 448 ASP B C   1 
ATOM   7829 O O   . ASP B 1 448 ? -39.406 41.534 17.590  1.00 15.05 ? 448 ASP B O   1 
ATOM   7830 C CB  . ASP B 1 448 ? -37.627 39.153 18.845  1.00 14.10 ? 448 ASP B CB  1 
ATOM   7831 C CG  . ASP B 1 448 ? -36.983 38.545 20.054  1.00 15.99 ? 448 ASP B CG  1 
ATOM   7832 O OD1 . ASP B 1 448 ? -37.463 37.464 20.471  1.00 16.76 ? 448 ASP B OD1 1 
ATOM   7833 O OD2 . ASP B 1 448 ? -36.029 39.153 20.590  1.00 16.08 ? 448 ASP B OD2 1 
ATOM   7834 N N   . TRP B 1 449 ? -40.281 39.510 17.150  1.00 16.76 ? 449 TRP B N   1 
ATOM   7835 C CA  . TRP B 1 449 ? -40.835 39.967 15.875  1.00 15.02 ? 449 TRP B CA  1 
ATOM   7836 C C   . TRP B 1 449 ? -41.803 41.119 16.085  1.00 18.20 ? 449 TRP B C   1 
ATOM   7837 O O   . TRP B 1 449 ? -41.780 42.112 15.345  1.00 18.50 ? 449 TRP B O   1 
ATOM   7838 C CB  . TRP B 1 449 ? -41.534 38.811 15.149  1.00 15.89 ? 449 TRP B CB  1 
ATOM   7839 C CG  . TRP B 1 449 ? -40.763 37.533 15.272  1.00 17.65 ? 449 TRP B CG  1 
ATOM   7840 C CD1 . TRP B 1 449 ? -41.190 36.367 15.844  1.00 17.53 ? 449 TRP B CD1 1 
ATOM   7841 C CD2 . TRP B 1 449 ? -39.412 37.305 14.850  1.00 16.51 ? 449 TRP B CD2 1 
ATOM   7842 N NE1 . TRP B 1 449 ? -40.196 35.423 15.786  1.00 20.67 ? 449 TRP B NE1 1 
ATOM   7843 C CE2 . TRP B 1 449 ? -39.089 35.972 15.191  1.00 15.23 ? 449 TRP B CE2 1 
ATOM   7844 C CE3 . TRP B 1 449 ? -38.447 38.092 14.220  1.00 15.58 ? 449 TRP B CE3 1 
ATOM   7845 C CZ2 . TRP B 1 449 ? -37.841 35.409 14.916  1.00 18.39 ? 449 TRP B CZ2 1 
ATOM   7846 C CZ3 . TRP B 1 449 ? -37.201 37.533 13.948  1.00 19.46 ? 449 TRP B CZ3 1 
ATOM   7847 C CH2 . TRP B 1 449 ? -36.908 36.204 14.299  1.00 16.20 ? 449 TRP B CH2 1 
ATOM   7848 N N   . PHE B 1 450 ? -42.656 41.003 17.104  1.00 16.27 ? 450 PHE B N   1 
ATOM   7849 C CA  . PHE B 1 450 ? -43.650 42.026 17.385  1.00 18.83 ? 450 PHE B CA  1 
ATOM   7850 C C   . PHE B 1 450 ? -43.018 43.264 17.983  1.00 17.50 ? 450 PHE B C   1 
ATOM   7851 O O   . PHE B 1 450 ? -43.507 44.377 17.761  1.00 19.34 ? 450 PHE B O   1 
ATOM   7852 C CB  . PHE B 1 450 ? -44.710 41.456 18.329  1.00 20.20 ? 450 PHE B CB  1 
ATOM   7853 C CG  . PHE B 1 450 ? -45.311 40.177 17.832  1.00 21.96 ? 450 PHE B CG  1 
ATOM   7854 C CD1 . PHE B 1 450 ? -44.728 38.954 18.135  1.00 22.58 ? 450 PHE B CD1 1 
ATOM   7855 C CD2 . PHE B 1 450 ? -46.444 40.199 17.028  1.00 20.83 ? 450 PHE B CD2 1 
ATOM   7856 C CE1 . PHE B 1 450 ? -45.268 37.780 17.662  1.00 23.47 ? 450 PHE B CE1 1 
ATOM   7857 C CE2 . PHE B 1 450 ? -46.991 39.026 16.555  1.00 23.36 ? 450 PHE B CE2 1 
ATOM   7858 C CZ  . PHE B 1 450 ? -46.398 37.813 16.868  1.00 18.40 ? 450 PHE B CZ  1 
ATOM   7859 N N   . TRP B 1 451 ? -41.934 43.078 18.736  1.00 17.07 ? 451 TRP B N   1 
ATOM   7860 C CA  . TRP B 1 451 ? -41.177 44.192 19.290  1.00 22.85 ? 451 TRP B CA  1 
ATOM   7861 C C   . TRP B 1 451 ? -40.742 45.172 18.200  1.00 21.60 ? 451 TRP B C   1 
ATOM   7862 O O   . TRP B 1 451 ? -40.952 46.384 18.317  1.00 22.03 ? 451 TRP B O   1 
ATOM   7863 C CB  . TRP B 1 451 ? -39.967 43.627 20.035  1.00 24.13 ? 451 TRP B CB  1 
ATOM   7864 C CG  . TRP B 1 451 ? -39.480 44.470 21.149  1.00 38.81 ? 451 TRP B CG  1 
ATOM   7865 C CD1 . TRP B 1 451 ? -39.878 44.419 22.453  1.00 47.55 ? 451 TRP B CD1 1 
ATOM   7866 C CD2 . TRP B 1 451 ? -38.478 45.483 21.073  1.00 40.22 ? 451 TRP B CD2 1 
ATOM   7867 N NE1 . TRP B 1 451 ? -39.192 45.349 23.193  1.00 49.45 ? 451 TRP B NE1 1 
ATOM   7868 C CE2 . TRP B 1 451 ? -38.323 46.014 22.369  1.00 44.94 ? 451 TRP B CE2 1 
ATOM   7869 C CE3 . TRP B 1 451 ? -37.698 45.996 20.036  1.00 38.74 ? 451 TRP B CE3 1 
ATOM   7870 C CZ2 . TRP B 1 451 ? -37.422 47.037 22.652  1.00 50.23 ? 451 TRP B CZ2 1 
ATOM   7871 C CZ3 . TRP B 1 451 ? -36.807 47.011 20.320  1.00 47.78 ? 451 TRP B CZ3 1 
ATOM   7872 C CH2 . TRP B 1 451 ? -36.673 47.520 21.616  1.00 51.53 ? 451 TRP B CH2 1 
ATOM   7873 N N   . TRP B 1 452 ? -40.135 44.661 17.128  1.00 18.48 ? 452 TRP B N   1 
ATOM   7874 C CA  . TRP B 1 452 ? -39.525 45.529 16.124  1.00 21.24 ? 452 TRP B CA  1 
ATOM   7875 C C   . TRP B 1 452 ? -40.549 46.051 15.135  1.00 22.13 ? 452 TRP B C   1 
ATOM   7876 O O   . TRP B 1 452 ? -40.359 47.128 14.558  1.00 20.87 ? 452 TRP B O   1 
ATOM   7877 C CB  . TRP B 1 452 ? -38.419 44.778 15.377  1.00 19.28 ? 452 TRP B CB  1 
ATOM   7878 C CG  . TRP B 1 452 ? -37.283 44.408 16.272  1.00 23.01 ? 452 TRP B CG  1 
ATOM   7879 C CD1 . TRP B 1 452 ? -36.950 43.153 16.709  1.00 18.62 ? 452 TRP B CD1 1 
ATOM   7880 C CD2 . TRP B 1 452 ? -36.325 45.304 16.854  1.00 20.26 ? 452 TRP B CD2 1 
ATOM   7881 N NE1 . TRP B 1 452 ? -35.860 43.219 17.543  1.00 18.23 ? 452 TRP B NE1 1 
ATOM   7882 C CE2 . TRP B 1 452 ? -35.447 44.524 17.637  1.00 18.62 ? 452 TRP B CE2 1 
ATOM   7883 C CE3 . TRP B 1 452 ? -36.125 46.687 16.790  1.00 26.78 ? 452 TRP B CE3 1 
ATOM   7884 C CZ2 . TRP B 1 452 ? -34.385 45.083 18.349  1.00 23.75 ? 452 TRP B CZ2 1 
ATOM   7885 C CZ3 . TRP B 1 452 ? -35.068 47.237 17.491  1.00 30.43 ? 452 TRP B CZ3 1 
ATOM   7886 C CH2 . TRP B 1 452 ? -34.212 46.436 18.265  1.00 26.96 ? 452 TRP B CH2 1 
ATOM   7887 N N   . GLN B 1 453 ? -41.640 45.321 14.950  1.00 22.25 ? 453 GLN B N   1 
ATOM   7888 C CA  . GLN B 1 453 ? -42.641 45.714 13.976  1.00 24.70 ? 453 GLN B CA  1 
ATOM   7889 C C   . GLN B 1 453 ? -43.301 47.026 14.385  1.00 27.91 ? 453 GLN B C   1 
ATOM   7890 O O   . GLN B 1 453 ? -43.621 47.251 15.555  1.00 27.93 ? 453 GLN B O   1 
ATOM   7891 C CB  . GLN B 1 453 ? -43.671 44.590 13.830  1.00 21.90 ? 453 GLN B CB  1 
ATOM   7892 C CG  . GLN B 1 453 ? -44.933 44.944 13.059  1.00 23.43 ? 453 GLN B CG  1 
ATOM   7893 C CD  . GLN B 1 453 ? -44.696 45.142 11.562  1.00 30.71 ? 453 GLN B CD  1 
ATOM   7894 O OE1 . GLN B 1 453 ? -43.557 45.096 11.084  1.00 30.67 ? 453 GLN B OE1 1 
ATOM   7895 N NE2 . GLN B 1 453 ? -45.780 45.345 10.817  1.00 29.96 ? 453 GLN B NE2 1 
ATOM   7896 N N   . GLY B 1 454 ? -43.444 47.904 13.430  1.00 32.31 ? 454 GLY B N   1 
ATOM   7897 C CA  . GLY B 1 454 ? -44.087 49.132 13.719  1.00 39.62 ? 454 GLY B CA  1 
ATOM   7898 C C   . GLY B 1 454 ? -43.287 50.131 14.474  1.00 53.61 ? 454 GLY B C   1 
ATOM   7899 O O   . GLY B 1 454 ? -43.833 50.878 15.271  1.00 56.98 ? 454 GLY B O   1 
ATOM   7900 N N   . GLU B 1 455 ? -41.989 50.138 14.217  1.00 58.76 ? 455 GLU B N   1 
ATOM   7901 C CA  . GLU B 1 455 ? -41.086 51.054 14.881  1.00 64.77 ? 455 GLU B CA  1 
ATOM   7902 C C   . GLU B 1 455 ? -40.593 52.087 13.886  1.00 73.48 ? 455 GLU B C   1 
ATOM   7903 O O   . GLU B 1 455 ? -41.400 52.637 13.209  1.00 79.89 ? 455 GLU B O   1 
ATOM   7904 C CB  . GLU B 1 455 ? -39.938 50.318 15.577  1.00 60.97 ? 455 GLU B CB  1 
ATOM   7905 N N   . GLU B 1 456 ? -39.271 52.290 13.759  1.00 75.01 ? 456 GLU B N   1 
ATOM   7906 C CA  . GLU B 1 456 ? -38.692 53.329 12.887  1.00 76.57 ? 456 GLU B CA  1 
ATOM   7907 C C   . GLU B 1 456 ? -37.635 53.046 11.769  1.00 77.41 ? 456 GLU B C   1 
ATOM   7908 O O   . GLU B 1 456 ? -36.510 53.530 11.848  1.00 81.29 ? 456 GLU B O   1 
ATOM   7909 C CB  . GLU B 1 456 ? -38.120 54.373 13.847  1.00 77.90 ? 456 GLU B CB  1 
ATOM   7910 N N   . LYS B 1 457 ? -38.002 52.304 10.730  1.00 73.48 ? 457 LYS B N   1 
ATOM   7911 C CA  . LYS B 1 457 ? -37.127 51.941 9.614   1.00 70.03 ? 457 LYS B CA  1 
ATOM   7912 C C   . LYS B 1 457 ? -35.647 51.865 9.917   1.00 75.28 ? 457 LYS B C   1 
ATOM   7913 O O   . LYS B 1 457 ? -34.828 51.895 9.004   1.00 80.76 ? 457 LYS B O   1 
ATOM   7914 C CB  . LYS B 1 457 ? -37.302 52.847 8.411   1.00 69.88 ? 457 LYS B CB  1 
ATOM   7915 N N   . ALA B 1 458 ? -35.306 51.762 11.194  1.00 72.05 ? 458 ALA B N   1 
ATOM   7916 C CA  . ALA B 1 458 ? -33.926 51.587 11.612  1.00 66.67 ? 458 ALA B CA  1 
ATOM   7917 C C   . ALA B 1 458 ? -33.267 50.531 10.732  1.00 61.01 ? 458 ALA B C   1 
ATOM   7918 O O   . ALA B 1 458 ? -33.955 49.707 10.185  1.00 57.85 ? 458 ALA B O   1 
ATOM   7919 C CB  . ALA B 1 458 ? -33.922 51.093 13.034  1.00 63.03 ? 458 ALA B CB  1 
ATOM   7920 N N   . PRO B 1 459 ? -31.888 50.589 10.607  1.00 57.01 ? 459 PRO B N   1 
ATOM   7921 C CA  . PRO B 1 459 ? -31.326 49.515 9.752   1.00 56.08 ? 459 PRO B CA  1 
ATOM   7922 C C   . PRO B 1 459 ? -31.626 48.075 10.325  1.00 55.39 ? 459 PRO B C   1 
ATOM   7923 O O   . PRO B 1 459 ? -31.795 47.830 11.475  1.00 49.95 ? 459 PRO B O   1 
ATOM   7924 C CB  . PRO B 1 459 ? -29.852 49.826 9.611   1.00 55.22 ? 459 PRO B CB  1 
ATOM   7925 C CG  . PRO B 1 459 ? -29.599 51.145 10.191  1.00 60.03 ? 459 PRO B CG  1 
ATOM   7926 C CD  . PRO B 1 459 ? -30.774 51.562 11.016  1.00 60.49 ? 459 PRO B CD  1 
ATOM   7927 N N   . PHE B 1 460 ? -31.757 47.140 9.420   1.00 55.27 ? 460 PHE B N   1 
ATOM   7928 C CA  . PHE B 1 460 ? -32.068 45.768 9.733   1.00 43.08 ? 460 PHE B CA  1 
ATOM   7929 C C   . PHE B 1 460 ? -33.452 45.421 10.169  1.00 38.50 ? 460 PHE B C   1 
ATOM   7930 O O   . PHE B 1 460 ? -33.789 44.324 10.192  1.00 39.18 ? 460 PHE B O   1 
ATOM   7931 C CB  . PHE B 1 460 ? -31.055 45.167 10.652  1.00 41.24 ? 460 PHE B CB  1 
ATOM   7932 C CG  . PHE B 1 460 ? -29.682 45.552 10.316  1.00 36.70 ? 460 PHE B CG  1 
ATOM   7933 C CD1 . PHE B 1 460 ? -29.298 45.689 9.043   1.00 39.42 ? 460 PHE B CD1 1 
ATOM   7934 C CD2 . PHE B 1 460 ? -28.774 45.720 11.292  1.00 43.53 ? 460 PHE B CD2 1 
ATOM   7935 C CE1 . PHE B 1 460 ? -28.042 46.076 8.719   1.00 46.34 ? 460 PHE B CE1 1 
ATOM   7936 C CE2 . PHE B 1 460 ? -27.509 46.091 10.993  1.00 46.00 ? 460 PHE B CE2 1 
ATOM   7937 C CZ  . PHE B 1 460 ? -27.136 46.291 9.694   1.00 49.89 ? 460 PHE B CZ  1 
ATOM   7938 N N   . VAL B 1 461 ? -34.264 46.383 10.493  1.00 42.51 ? 461 VAL B N   1 
ATOM   7939 C CA  . VAL B 1 461 ? -35.638 46.060 10.870  1.00 40.20 ? 461 VAL B CA  1 
ATOM   7940 C C   . VAL B 1 461 ? -36.284 45.207 9.788   1.00 40.32 ? 461 VAL B C   1 
ATOM   7941 O O   . VAL B 1 461 ? -37.059 44.289 10.079  1.00 39.85 ? 461 VAL B O   1 
ATOM   7942 C CB  . VAL B 1 461 ? -36.444 47.343 11.160  1.00 51.76 ? 461 VAL B CB  1 
ATOM   7943 C CG1 . VAL B 1 461 ? -37.005 47.969 9.880   1.00 54.03 ? 461 VAL B CG1 1 
ATOM   7944 C CG2 . VAL B 1 461 ? -37.561 47.051 12.149  1.00 51.69 ? 461 VAL B CG2 1 
ATOM   7945 N N   . GLU B 1 462 ? -35.932 45.458 8.522   1.00 29.96 ? 462 GLU B N   1 
ATOM   7946 C CA  . GLU B 1 462 ? -36.512 44.668 7.448   1.00 29.97 ? 462 GLU B CA  1 
ATOM   7947 C C   . GLU B 1 462 ? -36.076 43.210 7.534   1.00 31.74 ? 462 GLU B C   1 
ATOM   7948 O O   . GLU B 1 462 ? -36.809 42.321 7.084   1.00 31.55 ? 462 GLU B O   1 
ATOM   7949 C CB  . GLU B 1 462 ? -36.163 45.278 6.080   1.00 38.21 ? 462 GLU B CB  1 
ATOM   7950 C CG  . GLU B 1 462 ? -34.679 45.484 5.759   1.00 57.36 ? 462 GLU B CG  1 
ATOM   7951 C CD  . GLU B 1 462 ? -33.975 46.515 6.637   1.00 68.20 ? 462 GLU B CD  1 
ATOM   7952 O OE1 . GLU B 1 462 ? -32.763 46.346 6.875   1.00 71.68 ? 462 GLU B OE1 1 
ATOM   7953 O OE2 . GLU B 1 462 ? -34.622 47.484 7.089   1.00 72.06 ? 462 GLU B OE2 1 
ATOM   7954 N N   . VAL B 1 463 ? -34.909 42.939 8.133   1.00 23.01 ? 463 VAL B N   1 
ATOM   7955 C CA  . VAL B 1 463 ? -34.468 41.556 8.292   1.00 21.89 ? 463 VAL B CA  1 
ATOM   7956 C C   . VAL B 1 463 ? -35.358 40.820 9.291   1.00 25.80 ? 463 VAL B C   1 
ATOM   7957 O O   . VAL B 1 463 ? -35.718 39.653 9.077   1.00 20.33 ? 463 VAL B O   1 
ATOM   7958 C CB  . VAL B 1 463 ? -32.984 41.503 8.698   1.00 25.96 ? 463 VAL B CB  1 
ATOM   7959 C CG1 . VAL B 1 463 ? -32.562 40.064 8.915   1.00 28.49 ? 463 VAL B CG1 1 
ATOM   7960 C CG2 . VAL B 1 463 ? -32.108 42.157 7.635   1.00 29.99 ? 463 VAL B CG2 1 
ATOM   7961 N N   . PHE B 1 464 ? -35.740 41.486 10.392  1.00 18.03 ? 464 PHE B N   1 
ATOM   7962 C CA  . PHE B 1 464 ? -36.644 40.856 11.349  1.00 20.29 ? 464 PHE B CA  1 
ATOM   7963 C C   . PHE B 1 464 ? -37.986 40.548 10.699  1.00 20.97 ? 464 PHE B C   1 
ATOM   7964 O O   . PHE B 1 464 ? -38.600 39.514 10.984  1.00 21.58 ? 464 PHE B O   1 
ATOM   7965 C CB  . PHE B 1 464 ? -36.827 41.754 12.578  1.00 22.97 ? 464 PHE B CB  1 
ATOM   7966 C CG  . PHE B 1 464 ? -35.617 41.807 13.472  1.00 17.20 ? 464 PHE B CG  1 
ATOM   7967 C CD1 . PHE B 1 464 ? -35.426 40.847 14.451  1.00 19.14 ? 464 PHE B CD1 1 
ATOM   7968 C CD2 . PHE B 1 464 ? -34.658 42.801 13.321  1.00 20.38 ? 464 PHE B CD2 1 
ATOM   7969 C CE1 . PHE B 1 464 ? -34.297 40.880 15.273  1.00 16.87 ? 464 PHE B CE1 1 
ATOM   7970 C CE2 . PHE B 1 464 ? -33.535 42.845 14.139  1.00 19.44 ? 464 PHE B CE2 1 
ATOM   7971 C CZ  . PHE B 1 464 ? -33.355 41.884 15.121  1.00 21.97 ? 464 PHE B CZ  1 
ATOM   7972 N N   . ASP B 1 465 ? -38.443 41.427 9.805   1.00 19.92 ? 465 ASP B N   1 
ATOM   7973 C CA  . ASP B 1 465 ? -39.685 41.185 9.077   1.00 18.06 ? 465 ASP B CA  1 
ATOM   7974 C C   . ASP B 1 465 ? -39.538 40.000 8.125   1.00 21.64 ? 465 ASP B C   1 
ATOM   7975 O O   . ASP B 1 465 ? -40.442 39.157 8.022   1.00 21.66 ? 465 ASP B O   1 
ATOM   7976 C CB  . ASP B 1 465 ? -40.088 42.456 8.330   1.00 20.19 ? 465 ASP B CB  1 
ATOM   7977 C CG  . ASP B 1 465 ? -41.295 42.256 7.443   1.00 24.93 ? 465 ASP B CG  1 
ATOM   7978 O OD1 . ASP B 1 465 ? -42.423 42.228 7.972   1.00 25.01 ? 465 ASP B OD1 1 
ATOM   7979 O OD2 . ASP B 1 465 ? -41.113 42.141 6.213   1.00 24.38 ? 465 ASP B OD2 1 
ATOM   7980 N N   . LYS B 1 466 ? -38.401 39.915 7.430   1.00 20.66 ? 466 LYS B N   1 
ATOM   7981 C CA  . LYS B 1 466 ? -38.151 38.774 6.554   1.00 24.27 ? 466 LYS B CA  1 
ATOM   7982 C C   . LYS B 1 466 ? -38.136 37.469 7.339   1.00 22.45 ? 466 LYS B C   1 
ATOM   7983 O O   . LYS B 1 466 ? -38.705 36.461 6.900   1.00 23.27 ? 466 LYS B O   1 
ATOM   7984 C CB  . LYS B 1 466 ? -36.833 38.963 5.808   1.00 24.60 ? 466 LYS B CB  1 
ATOM   7985 C CG  . LYS B 1 466 ? -36.464 37.795 4.917   1.00 29.20 ? 466 LYS B CG  1 
ATOM   7986 C CD  . LYS B 1 466 ? -35.234 38.110 4.087   1.00 33.81 ? 466 LYS B CD  1 
ATOM   7987 C CE  . LYS B 1 466 ? -35.272 37.398 2.749   1.00 51.99 ? 466 LYS B CE  1 
ATOM   7988 N NZ  . LYS B 1 466 ? -34.198 36.377 2.631   1.00 60.66 ? 466 LYS B NZ  1 
ATOM   7989 N N   . LEU B 1 467 ? -37.490 37.465 8.505   1.00 17.88 ? 467 LEU B N   1 
ATOM   7990 C CA  . LEU B 1 467 ? -37.449 36.255 9.315   1.00 19.21 ? 467 LEU B CA  1 
ATOM   7991 C C   . LEU B 1 467 ? -38.845 35.852 9.774   1.00 19.98 ? 467 LEU B C   1 
ATOM   7992 O O   . LEU B 1 467 ? -39.262 34.705 9.575   1.00 22.32 ? 467 LEU B O   1 
ATOM   7993 C CB  . LEU B 1 467 ? -36.525 36.458 10.507  1.00 17.31 ? 467 LEU B CB  1 
ATOM   7994 C CG  . LEU B 1 467 ? -35.049 36.550 10.118  1.00 18.61 ? 467 LEU B CG  1 
ATOM   7995 C CD1 . LEU B 1 467 ? -34.256 37.161 11.268  1.00 17.50 ? 467 LEU B CD1 1 
ATOM   7996 C CD2 . LEU B 1 467 ? -34.499 35.182 9.727   1.00 23.23 ? 467 LEU B CD2 1 
ATOM   7997 N N   . PHE B 1 468 ? -39.581 36.784 10.390  1.00 20.04 ? 468 PHE B N   1 
ATOM   7998 C CA  . PHE B 1 468 ? -40.925 36.478 10.879  1.00 19.52 ? 468 PHE B CA  1 
ATOM   7999 C C   . PHE B 1 468 ? -41.783 35.874 9.779   1.00 20.63 ? 468 PHE B C   1 
ATOM   8000 O O   . PHE B 1 468 ? -42.369 34.800 9.946   1.00 19.91 ? 468 PHE B O   1 
ATOM   8001 C CB  . PHE B 1 468 ? -41.594 37.744 11.434  1.00 18.82 ? 468 PHE B CB  1 
ATOM   8002 C CG  . PHE B 1 468 ? -43.061 37.572 11.759  1.00 19.70 ? 468 PHE B CG  1 
ATOM   8003 C CD1 . PHE B 1 468 ? -43.457 36.847 12.876  1.00 22.04 ? 468 PHE B CD1 1 
ATOM   8004 C CD2 . PHE B 1 468 ? -44.041 38.129 10.950  1.00 19.36 ? 468 PHE B CD2 1 
ATOM   8005 C CE1 . PHE B 1 468 ? -44.796 36.691 13.172  1.00 21.55 ? 468 PHE B CE1 1 
ATOM   8006 C CE2 . PHE B 1 468 ? -45.388 37.965 11.246  1.00 19.67 ? 468 PHE B CE2 1 
ATOM   8007 C CZ  . PHE B 1 468 ? -45.760 37.259 12.359  1.00 19.06 ? 468 PHE B CZ  1 
ATOM   8008 N N   . ARG B 1 469 ? -41.856 36.549 8.631   1.00 19.52 ? 469 ARG B N   1 
ATOM   8009 C CA  . ARG B 1 469 ? -42.744 36.082 7.575   1.00 19.97 ? 469 ARG B CA  1 
ATOM   8010 C C   . ARG B 1 469 ? -42.254 34.773 6.966   1.00 22.24 ? 469 ARG B C   1 
ATOM   8011 O O   . ARG B 1 469 ? -43.071 33.958 6.523   1.00 25.46 ? 469 ARG B O   1 
ATOM   8012 C CB  . ARG B 1 469 ? -42.898 37.176 6.518   1.00 26.94 ? 469 ARG B CB  1 
ATOM   8013 C CG  . ARG B 1 469 ? -43.599 38.427 7.069   1.00 22.33 ? 469 ARG B CG  1 
ATOM   8014 C CD  . ARG B 1 469 ? -43.648 39.520 6.019   1.00 26.45 ? 469 ARG B CD  1 
ATOM   8015 N NE  . ARG B 1 469 ? -44.378 40.711 6.446   1.00 24.54 ? 469 ARG B NE  1 
ATOM   8016 C CZ  . ARG B 1 469 ? -45.678 40.902 6.240   1.00 28.31 ? 469 ARG B CZ  1 
ATOM   8017 N NH1 . ARG B 1 469 ? -46.399 39.971 5.629   1.00 27.98 ? 469 ARG B NH1 1 
ATOM   8018 N NH2 . ARG B 1 469 ? -46.261 42.028 6.634   1.00 28.52 ? 469 ARG B NH2 1 
ATOM   8019 N N   . SER B 1 470 ? -40.937 34.540 6.964   1.00 24.12 ? 470 SER B N   1 
ATOM   8020 C CA  . SER B 1 470 ? -40.406 33.267 6.482   1.00 25.81 ? 470 SER B CA  1 
ATOM   8021 C C   . SER B 1 470 ? -40.756 32.122 7.424   1.00 20.81 ? 470 SER B C   1 
ATOM   8022 O O   . SER B 1 470 ? -41.082 31.018 6.969   1.00 26.94 ? 470 SER B O   1 
ATOM   8023 C CB  . SER B 1 470 ? -38.890 33.361 6.304   1.00 27.67 ? 470 SER B CB  1 
ATOM   8024 O OG  . SER B 1 470 ? -38.563 34.309 5.306   1.00 29.41 ? 470 SER B OG  1 
ATOM   8025 N N   . PHE B 1 471 ? -40.678 32.358 8.737   1.00 20.63 ? 471 PHE B N   1 
ATOM   8026 C CA  . PHE B 1 471 ? -41.093 31.328 9.686   1.00 25.25 ? 471 PHE B CA  1 
ATOM   8027 C C   . PHE B 1 471 ? -42.582 31.037 9.548   1.00 28.15 ? 471 PHE B C   1 
ATOM   8028 O O   . PHE B 1 471 ? -43.002 29.873 9.584   1.00 26.62 ? 471 PHE B O   1 
ATOM   8029 C CB  . PHE B 1 471 ? -40.745 31.763 11.110  1.00 21.40 ? 471 PHE B CB  1 
ATOM   8030 C CG  . PHE B 1 471 ? -39.264 31.852 11.358  1.00 21.97 ? 471 PHE B CG  1 
ATOM   8031 C CD1 . PHE B 1 471 ? -38.431 30.818 10.975  1.00 20.48 ? 471 PHE B CD1 1 
ATOM   8032 C CD2 . PHE B 1 471 ? -38.704 32.964 11.980  1.00 21.58 ? 471 PHE B CD2 1 
ATOM   8033 C CE1 . PHE B 1 471 ? -37.063 30.883 11.201  1.00 28.15 ? 471 PHE B CE1 1 
ATOM   8034 C CE2 . PHE B 1 471 ? -37.341 33.037 12.209  1.00 24.20 ? 471 PHE B CE2 1 
ATOM   8035 C CZ  . PHE B 1 471 ? -36.517 32.000 11.812  1.00 30.02 ? 471 PHE B CZ  1 
ATOM   8036 N N   . VAL B 1 472 ? -43.386 32.087 9.351   1.00 23.60 ? 472 VAL B N   1 
ATOM   8037 C CA  . VAL B 1 472 ? -44.824 31.931 9.158   1.00 24.44 ? 472 VAL B CA  1 
ATOM   8038 C C   . VAL B 1 472 ? -45.103 31.112 7.907   1.00 26.90 ? 472 VAL B C   1 
ATOM   8039 O O   . VAL B 1 472 ? -45.955 30.214 7.906   1.00 32.92 ? 472 VAL B O   1 
ATOM   8040 C CB  . VAL B 1 472 ? -45.496 33.315 9.091   1.00 23.11 ? 472 VAL B CB  1 
ATOM   8041 C CG1 . VAL B 1 472 ? -46.875 33.219 8.460   1.00 26.22 ? 472 VAL B CG1 1 
ATOM   8042 C CG2 . VAL B 1 472 ? -45.556 33.935 10.487  1.00 21.16 ? 472 VAL B CG2 1 
ATOM   8043 N N   . ARG B 1 473 ? -44.383 31.401 6.825   1.00 26.98 ? 473 ARG B N   1 
ATOM   8044 C CA  . ARG B 1 473 ? -44.571 30.634 5.597   1.00 27.83 ? 473 ARG B CA  1 
ATOM   8045 C C   . ARG B 1 473 ? -44.119 29.193 5.785   1.00 27.36 ? 473 ARG B C   1 
ATOM   8046 O O   . ARG B 1 473 ? -44.821 28.254 5.388   1.00 29.73 ? 473 ARG B O   1 
ATOM   8047 C CB  . ARG B 1 473 ? -43.809 31.295 4.449   1.00 27.39 ? 473 ARG B CB  1 
ATOM   8048 C CG  . ARG B 1 473 ? -43.916 30.564 3.121   1.00 37.69 ? 473 ARG B CG  1 
ATOM   8049 C CD  . ARG B 1 473 ? -43.124 31.287 2.041   1.00 53.29 ? 473 ARG B CD  1 
ATOM   8050 N NE  . ARG B 1 473 ? -43.069 32.728 2.276   1.00 63.42 ? 473 ARG B NE  1 
ATOM   8051 C CZ  . ARG B 1 473 ? -41.959 33.401 2.576   1.00 69.83 ? 473 ARG B CZ  1 
ATOM   8052 N NH1 . ARG B 1 473 ? -40.798 32.767 2.677   1.00 70.97 ? 473 ARG B NH1 1 
ATOM   8053 N NH2 . ARG B 1 473 ? -42.011 34.711 2.779   1.00 67.77 ? 473 ARG B NH2 1 
ATOM   8054 N N   . ARG B 1 474 ? -42.956 29.003 6.406   1.00 26.59 ? 474 ARG B N   1 
ATOM   8055 C CA  . ARG B 1 474 ? -42.442 27.659 6.635   1.00 34.76 ? 474 ARG B CA  1 
ATOM   8056 C C   . ARG B 1 474 ? -43.380 26.845 7.517   1.00 33.30 ? 474 ARG B C   1 
ATOM   8057 O O   . ARG B 1 474 ? -43.498 25.627 7.344   1.00 30.53 ? 474 ARG B O   1 
ATOM   8058 C CB  . ARG B 1 474 ? -41.051 27.754 7.268   1.00 35.09 ? 474 ARG B CB  1 
ATOM   8059 C CG  . ARG B 1 474 ? -40.297 26.438 7.350   1.00 38.40 ? 474 ARG B CG  1 
ATOM   8060 C CD  . ARG B 1 474 ? -39.957 25.887 5.978   1.00 40.60 ? 474 ARG B CD  1 
ATOM   8061 N NE  . ARG B 1 474 ? -39.373 24.555 6.085   1.00 46.91 ? 474 ARG B NE  1 
ATOM   8062 C CZ  . ARG B 1 474 ? -40.085 23.440 6.208   1.00 63.53 ? 474 ARG B CZ  1 
ATOM   8063 N NH1 . ARG B 1 474 ? -41.411 23.499 6.239   1.00 67.48 ? 474 ARG B NH1 1 
ATOM   8064 N NH2 . ARG B 1 474 ? -39.474 22.267 6.299   1.00 69.97 ? 474 ARG B NH2 1 
ATOM   8065 N N   . ALA B 1 475 ? -44.063 27.505 8.454   1.00 29.06 ? 475 ALA B N   1 
ATOM   8066 C CA  . ALA B 1 475 ? -44.935 26.817 9.396   1.00 31.63 ? 475 ALA B CA  1 
ATOM   8067 C C   . ALA B 1 475 ? -46.110 26.123 8.717   1.00 34.35 ? 475 ALA B C   1 
ATOM   8068 O O   . ALA B 1 475 ? -46.701 25.213 9.309   1.00 32.80 ? 475 ALA B O   1 
ATOM   8069 C CB  . ALA B 1 475 ? -45.459 27.811 10.433  1.00 23.61 ? 475 ALA B CB  1 
ATOM   8070 N N   . GLN B 1 476 ? -46.468 26.529 7.498   1.00 31.20 ? 476 GLN B N   1 
ATOM   8071 C CA  . GLN B 1 476 ? -47.640 25.999 6.811   1.00 32.96 ? 476 GLN B CA  1 
ATOM   8072 C C   . GLN B 1 476 ? -47.281 24.984 5.731   1.00 37.97 ? 476 GLN B C   1 
ATOM   8073 O O   . GLN B 1 476 ? -48.127 24.655 4.893   1.00 44.70 ? 476 GLN B O   1 
ATOM   8074 C CB  . GLN B 1 476 ? -48.458 27.144 6.209   1.00 37.15 ? 476 GLN B CB  1 
ATOM   8075 C CG  . GLN B 1 476 ? -48.970 28.141 7.237   1.00 34.36 ? 476 GLN B CG  1 
ATOM   8076 C CD  . GLN B 1 476 ? -49.530 29.399 6.607   1.00 39.80 ? 476 GLN B CD  1 
ATOM   8077 O OE1 . GLN B 1 476 ? -50.632 29.393 6.052   1.00 41.40 ? 476 GLN B OE1 1 
ATOM   8078 N NE2 . GLN B 1 476 ? -48.774 30.489 6.688   1.00 35.26 ? 476 GLN B NE2 1 
ATOM   8079 N N   . GLU B 1 477 ? -46.052 24.481 5.738   1.00 41.43 ? 477 GLU B N   1 
ATOM   8080 C CA  . GLU B 1 477 ? -45.607 23.494 4.765   1.00 48.34 ? 477 GLU B CA  1 
ATOM   8081 C C   . GLU B 1 477 ? -45.232 22.198 5.463   1.00 52.49 ? 477 GLU B C   1 
ATOM   8082 O O   . GLU B 1 477 ? -44.638 22.228 6.542   1.00 53.22 ? 477 GLU B O   1 
ATOM   8083 C CB  . GLU B 1 477 ? -44.417 24.024 3.970   1.00 50.06 ? 477 GLU B CB  1 
ATOM   8084 C CG  . GLU B 1 477 ? -44.664 25.363 3.304   1.00 53.56 ? 477 GLU B CG  1 
ATOM   8085 C CD  . GLU B 1 477 ? -43.442 25.876 2.570   1.00 58.84 ? 477 GLU B CD  1 
ATOM   8086 O OE1 . GLU B 1 477 ? -43.605 26.710 1.655   1.00 60.80 ? 477 GLU B OE1 1 
ATOM   8087 O OE2 . GLU B 1 477 ? -42.319 25.441 2.904   1.00 57.64 ? 477 GLU B OE2 1 
HETATM 8088 C C1  . GLC C 2 .   ? 1.315   28.178 65.338  1.00 20.00 ? 1   GLC C C1  1 
HETATM 8089 C C2  . GLC C 2 .   ? 1.574   29.018 66.594  1.00 20.00 ? 1   GLC C C2  1 
HETATM 8090 C C3  . GLC C 2 .   ? 1.581   28.286 67.914  1.00 20.00 ? 1   GLC C C3  1 
HETATM 8091 C C4  . GLC C 2 .   ? 0.546   27.187 67.965  1.00 20.00 ? 1   GLC C C4  1 
HETATM 8092 C C5  . GLC C 2 .   ? 0.731   26.284 66.773  1.00 20.00 ? 1   GLC C C5  1 
HETATM 8093 C C6  . GLC C 2 .   ? -0.479  25.381 66.734  1.00 20.00 ? 1   GLC C C6  1 
HETATM 8094 O O1  . GLC C 2 .   ? 2.341   28.270 64.405  1.00 20.00 ? 1   GLC C O1  1 
HETATM 8095 O O2  . GLC C 2 .   ? 2.705   29.836 66.469  1.00 20.00 ? 1   GLC C O2  1 
HETATM 8096 O O3  . GLC C 2 .   ? 1.201   29.262 68.851  1.00 20.00 ? 1   GLC C O3  1 
HETATM 8097 O O4  . GLC C 2 .   ? 0.634   26.448 69.190  1.00 20.00 ? 1   GLC C O4  1 
HETATM 8098 O O5  . GLC C 2 .   ? 0.827   26.888 65.526  1.00 20.00 ? 1   GLC C O5  1 
HETATM 8099 O O6  . GLC C 2 .   ? -1.549  25.921 66.000  1.00 20.00 ? 1   GLC C O6  1 
HETATM 8100 C C1  . GLC C 2 .   ? 0.221   26.932 70.328  1.00 38.26 ? 2   GLC C C1  1 
HETATM 8101 C C2  . GLC C 2 .   ? 1.143   26.231 71.282  1.00 36.31 ? 2   GLC C C2  1 
HETATM 8102 C C3  . GLC C 2 .   ? 0.889   24.735 71.232  1.00 26.17 ? 2   GLC C C3  1 
HETATM 8103 C C4  . GLC C 2 .   ? -0.612  24.470 71.472  1.00 36.52 ? 2   GLC C C4  1 
HETATM 8104 C C5  . GLC C 2 .   ? -1.540  25.352 70.636  1.00 44.77 ? 2   GLC C C5  1 
HETATM 8105 C C6  . GLC C 2 .   ? -2.935  25.190 71.249  1.00 52.04 ? 2   GLC C C6  1 
HETATM 8106 O O2  . GLC C 2 .   ? 2.496   26.553 70.962  1.00 38.43 ? 2   GLC C O2  1 
HETATM 8107 O O3  . GLC C 2 .   ? 1.681   24.217 72.230  1.00 28.37 ? 2   GLC C O3  1 
HETATM 8108 O O4  . GLC C 2 .   ? -1.059  23.169 71.347  1.00 16.84 ? 2   GLC C O4  1 
HETATM 8109 O O5  . GLC C 2 .   ? -1.127  26.699 70.719  1.00 44.05 ? 2   GLC C O5  1 
HETATM 8110 O O6  . GLC C 2 .   ? -3.053  25.696 72.604  1.00 51.76 ? 2   GLC C O6  1 
HETATM 8111 C C1  . GLC C 2 .   ? -0.407  22.272 72.145  1.00 13.83 ? 3   GLC C C1  1 
HETATM 8112 C C2  . GLC C 2 .   ? -1.070  20.928 71.829  1.00 11.39 ? 3   GLC C C2  1 
HETATM 8113 C C3  . GLC C 2 .   ? -2.476  20.922 72.442  1.00 12.81 ? 3   GLC C C3  1 
HETATM 8114 C C4  . GLC C 2 .   ? -2.449  21.296 73.951  1.00 12.02 ? 3   GLC C C4  1 
HETATM 8115 C C5  . GLC C 2 .   ? -1.586  22.557 74.148  1.00 14.07 ? 3   GLC C C5  1 
HETATM 8116 C C6  . GLC C 2 .   ? -1.372  22.797 75.636  1.00 8.74  ? 3   GLC C C6  1 
HETATM 8117 O O2  . GLC C 2 .   ? -1.001  20.623 70.416  1.00 10.15 ? 3   GLC C O2  1 
HETATM 8118 O O3  . GLC C 2 .   ? -3.107  19.675 72.258  1.00 12.10 ? 3   GLC C O3  1 
HETATM 8119 O O4  . GLC C 2 .   ? -3.773  21.554 74.420  1.00 12.88 ? 3   GLC C O4  1 
HETATM 8120 O O5  . GLC C 2 .   ? -0.376  22.546 73.525  1.00 15.71 ? 3   GLC C O5  1 
HETATM 8121 O O6  . GLC C 2 .   ? -0.550  21.823 76.199  1.00 12.79 ? 3   GLC C O6  1 
HETATM 8122 C C1  . GLC C 2 .   ? -4.416  20.449 74.958  1.00 9.96  ? 4   GLC C C1  1 
HETATM 8123 C C2  . GLC C 2 .   ? -5.885  20.470 74.554  1.00 10.17 ? 4   GLC C C2  1 
HETATM 8124 C C3  . GLC C 2 .   ? -6.556  21.677 75.163  1.00 8.68  ? 4   GLC C C3  1 
HETATM 8125 C C4  . GLC C 2 .   ? -6.267  21.745 76.675  1.00 10.45 ? 4   GLC C C4  1 
HETATM 8126 C C5  . GLC C 2 .   ? -4.764  21.581 76.933  1.00 9.38  ? 4   GLC C C5  1 
HETATM 8127 C C6  . GLC C 2 .   ? -4.390  21.501 78.387  1.00 12.20 ? 4   GLC C C6  1 
HETATM 8128 O O2  . GLC C 2 .   ? -5.992  20.390 73.174  1.00 10.67 ? 4   GLC C O2  1 
HETATM 8129 O O3  . GLC C 2 .   ? -7.945  21.663 74.970  1.00 10.33 ? 4   GLC C O3  1 
HETATM 8130 O O4  . GLC C 2 .   ? -6.780  22.984 77.176  1.00 9.78  ? 4   GLC C O4  1 
HETATM 8131 O O5  . GLC C 2 .   ? -4.272  20.421 76.350  1.00 9.75  ? 4   GLC C O5  1 
HETATM 8132 O O6  . GLC C 2 .   ? -3.061  21.147 78.593  1.00 10.65 ? 4   GLC C O6  1 
HETATM 8133 C C1  . GLC C 2 .   ? -7.656  22.946 78.265  1.00 9.93  ? 5   GLC C C1  1 
HETATM 8134 C C2  . GLC C 2 .   ? -9.031  23.509 77.848  1.00 9.56  ? 5   GLC C C2  1 
HETATM 8135 C C3  . GLC C 2 .   ? -8.829  24.998 77.631  1.00 12.22 ? 5   GLC C C3  1 
HETATM 8136 C C4  . GLC C 2 .   ? -8.237  25.704 78.836  1.00 11.26 ? 5   GLC C C4  1 
HETATM 8137 C C5  . GLC C 2 .   ? -7.000  24.973 79.284  1.00 14.15 ? 5   GLC C C5  1 
HETATM 8138 C C6  . GLC C 2 .   ? -6.584  25.562 80.631  1.00 15.55 ? 5   GLC C C6  1 
HETATM 8139 O O2  . GLC C 2 .   ? -9.607  22.864 76.712  1.00 10.07 ? 5   GLC C O2  1 
HETATM 8140 O O3  . GLC C 2 .   ? -9.999  25.670 77.236  1.00 12.85 ? 5   GLC C O3  1 
HETATM 8141 O O4  . GLC C 2 .   ? -7.974  27.040 78.519  1.00 14.62 ? 5   GLC C O4  1 
HETATM 8142 O O5  . GLC C 2 .   ? -7.211  23.611 79.406  1.00 11.98 ? 5   GLC C O5  1 
HETATM 8143 O O6  . GLC C 2 .   ? -7.489  25.173 81.573  1.00 14.50 ? 5   GLC C O6  1 
HETATM 8144 C C1  . GLC C 2 .   ? -8.590  27.821 79.494  1.00 23.98 ? 6   GLC C C1  1 
HETATM 8145 C C2  . GLC C 2 .   ? -9.574  28.773 78.846  1.00 20.27 ? 6   GLC C C2  1 
HETATM 8146 C C3  . GLC C 2 .   ? -8.818  29.540 77.814  1.00 30.20 ? 6   GLC C C3  1 
HETATM 8147 C C4  . GLC C 2 .   ? -7.689  30.321 78.469  1.00 37.45 ? 6   GLC C C4  1 
HETATM 8148 C C5  . GLC C 2 .   ? -6.823  29.358 79.282  1.00 30.89 ? 6   GLC C C5  1 
HETATM 8149 C C6  . GLC C 2 .   ? -5.886  30.033 80.280  1.00 43.31 ? 6   GLC C C6  1 
HETATM 8150 O O2  . GLC C 2 .   ? -10.538 28.054 78.201  1.00 17.92 ? 6   GLC C O2  1 
HETATM 8151 O O3  . GLC C 2 .   ? -9.646  30.365 77.023  1.00 34.03 ? 6   GLC C O3  1 
HETATM 8152 O O4  . GLC C 2 .   ? -7.033  30.831 77.332  1.00 39.40 ? 6   GLC C O4  1 
HETATM 8153 O O5  . GLC C 2 .   ? -7.636  28.653 80.126  1.00 30.96 ? 6   GLC C O5  1 
HETATM 8154 O O6  . GLC C 2 .   ? -6.566  30.320 81.519  1.00 35.39 ? 6   GLC C O6  1 
HETATM 8155 C C1  . GLC D 2 .   ? -37.057 48.334 32.316  1.00 48.87 ? 1   GLC D C1  1 
HETATM 8156 C C2  . GLC D 2 .   ? -37.603 49.052 31.106  1.00 47.87 ? 1   GLC D C2  1 
HETATM 8157 C C3  . GLC D 2 .   ? -37.654 48.299 29.791  1.00 46.91 ? 1   GLC D C3  1 
HETATM 8158 C C4  . GLC D 2 .   ? -36.651 47.192 29.722  1.00 48.29 ? 1   GLC D C4  1 
HETATM 8159 C C5  . GLC D 2 .   ? -36.753 46.332 30.936  1.00 44.35 ? 1   GLC D C5  1 
HETATM 8160 C C6  . GLC D 2 .   ? -35.622 45.337 30.811  1.00 37.39 ? 1   GLC D C6  1 
HETATM 8161 O O1  . GLC D 2 .   ? -37.880 48.557 33.404  1.00 51.22 ? 1   GLC D O1  1 
HETATM 8162 O O2  . GLC D 2 .   ? -38.803 49.773 31.410  1.00 44.42 ? 1   GLC D O2  1 
HETATM 8163 O O3  . GLC D 2 .   ? -37.351 49.248 28.815  1.00 46.82 ? 1   GLC D O3  1 
HETATM 8164 O O4  . GLC D 2 .   ? -36.910 46.324 28.647  1.00 48.05 ? 1   GLC D O4  1 
HETATM 8165 O O5  . GLC D 2 .   ? -36.713 46.991 32.180  1.00 46.24 ? 1   GLC D O5  1 
HETATM 8166 O O6  . GLC D 2 .   ? -34.365 45.886 31.113  1.00 40.08 ? 1   GLC D O6  1 
HETATM 8167 C C1  . GLC D 2 .   ? -36.745 46.906 27.391  1.00 46.96 ? 2   GLC D C1  1 
HETATM 8168 C C2  . GLC D 2 .   ? -37.791 46.197 26.555  1.00 47.13 ? 2   GLC D C2  1 
HETATM 8169 C C3  . GLC D 2 .   ? -37.508 44.718 26.546  1.00 35.52 ? 2   GLC D C3  1 
HETATM 8170 C C4  . GLC D 2 .   ? -36.096 44.472 26.007  1.00 33.25 ? 2   GLC D C4  1 
HETATM 8171 C C5  . GLC D 2 .   ? -35.040 45.374 26.658  1.00 44.96 ? 2   GLC D C5  1 
HETATM 8172 C C6  . GLC D 2 .   ? -33.784 45.432 25.789  1.00 56.40 ? 2   GLC D C6  1 
HETATM 8173 O O2  . GLC D 2 .   ? -39.040 46.324 27.177  1.00 45.93 ? 2   GLC D O2  1 
HETATM 8174 O O3  . GLC D 2 .   ? -38.550 44.182 25.761  1.00 28.20 ? 2   GLC D O3  1 
HETATM 8175 O O4  . GLC D 2 .   ? -35.641 43.148 26.219  1.00 18.09 ? 2   GLC D O4  1 
HETATM 8176 O O5  . GLC D 2 .   ? -35.459 46.707 26.826  1.00 47.09 ? 2   GLC D O5  1 
HETATM 8177 O O6  . GLC D 2 .   ? -32.637 45.327 26.613  1.00 59.16 ? 2   GLC D O6  1 
HETATM 8178 C C1  . GLC D 2 .   ? -36.453 42.135 25.599  1.00 13.68 ? 3   GLC D C1  1 
HETATM 8179 C C2  . GLC D 2 .   ? -35.695 40.826 25.786  1.00 11.67 ? 3   GLC D C2  1 
HETATM 8180 C C3  . GLC D 2 .   ? -34.396 40.818 25.000  1.00 17.51 ? 3   GLC D C3  1 
HETATM 8181 C C4  . GLC D 2 .   ? -34.648 41.158 23.524  1.00 16.65 ? 3   GLC D C4  1 
HETATM 8182 C C5  . GLC D 2 .   ? -35.512 42.421 23.391  1.00 17.74 ? 3   GLC D C5  1 
HETATM 8183 C C6  . GLC D 2 .   ? -35.992 42.681 21.959  1.00 14.65 ? 3   GLC D C6  1 
HETATM 8184 O O2  . GLC D 2 .   ? -35.439 40.688 27.176  1.00 13.58 ? 3   GLC D O2  1 
HETATM 8185 O O3  . GLC D 2 .   ? -33.766 39.560 25.190  1.00 14.61 ? 3   GLC D O3  1 
HETATM 8186 O O4  . GLC D 2 .   ? -33.412 41.443 22.920  1.00 14.01 ? 3   GLC D O4  1 
HETATM 8187 O O5  . GLC D 2 .   ? -36.663 42.360 24.213  1.00 17.16 ? 3   GLC D O5  1 
HETATM 8188 O O6  . GLC D 2 .   ? -36.881 41.649 21.606  1.00 19.01 ? 3   GLC D O6  1 
HETATM 8189 C C1  . GLC D 2 .   ? -32.855 40.283 22.264  1.00 15.29 ? 4   GLC D C1  1 
HETATM 8190 C C2  . GLC D 2 .   ? -31.333 40.346 22.404  1.00 12.02 ? 4   GLC D C2  1 
HETATM 8191 C C3  . GLC D 2 .   ? -30.788 41.583 21.705  1.00 12.55 ? 4   GLC D C3  1 
HETATM 8192 C C4  . GLC D 2 .   ? -31.243 41.574 20.241  1.00 13.25 ? 4   GLC D C4  1 
HETATM 8193 C C5  . GLC D 2 .   ? -32.765 41.399 20.185  1.00 17.11 ? 4   GLC D C5  1 
HETATM 8194 C C6  . GLC D 2 .   ? -33.292 41.243 18.762  1.00 14.67 ? 4   GLC D C6  1 
HETATM 8195 O O2  . GLC D 2 .   ? -30.955 40.372 23.764  1.00 13.41 ? 4   GLC D O2  1 
HETATM 8196 O O3  . GLC D 2 .   ? -29.376 41.566 21.736  1.00 13.89 ? 4   GLC D O3  1 
HETATM 8197 O O4  . GLC D 2 .   ? -30.860 42.817 19.687  1.00 13.18 ? 4   GLC D O4  1 
HETATM 8198 O O5  . GLC D 2 .   ? -33.182 40.251 20.895  1.00 14.98 ? 4   GLC D O5  1 
HETATM 8199 O O6  . GLC D 2 .   ? -34.680 41.031 18.859  1.00 13.77 ? 4   GLC D O6  1 
HETATM 8200 C C1  . GLC D 2 .   ? -30.098 42.656 18.478  1.00 12.44 ? 5   GLC D C1  1 
HETATM 8201 C C2  . GLC D 2 .   ? -28.728 43.307 18.666  1.00 11.08 ? 5   GLC D C2  1 
HETATM 8202 C C3  . GLC D 2 .   ? -28.858 44.805 18.891  1.00 15.03 ? 5   GLC D C3  1 
HETATM 8203 C C4  . GLC D 2 .   ? -29.592 45.417 17.708  1.00 15.74 ? 5   GLC D C4  1 
HETATM 8204 C C5  . GLC D 2 .   ? -30.910 44.685 17.470  1.00 12.63 ? 5   GLC D C5  1 
HETATM 8205 C C6  . GLC D 2 .   ? -31.598 45.176 16.183  1.00 20.90 ? 5   GLC D C6  1 
HETATM 8206 O O2  . GLC D 2 .   ? -28.033 42.715 19.742  1.00 13.77 ? 5   GLC D O2  1 
HETATM 8207 O O3  . GLC D 2 .   ? -27.605 45.434 19.026  1.00 17.00 ? 5   GLC D O3  1 
HETATM 8208 O O4  . GLC D 2 .   ? -29.823 46.773 18.018  1.00 21.61 ? 5   GLC D O4  1 
HETATM 8209 O O5  . GLC D 2 .   ? -30.740 43.278 17.371  1.00 15.07 ? 5   GLC D O5  1 
HETATM 8210 O O6  . GLC D 2 .   ? -30.746 44.977 15.064  1.00 20.98 ? 5   GLC D O6  1 
HETATM 8211 C C1  . GLC D 2 .   ? -29.324 47.615 16.971  1.00 30.68 ? 6   GLC D C1  1 
HETATM 8212 C C2  . GLC D 2 .   ? -28.220 48.531 17.541  1.00 24.41 ? 6   GLC D C2  1 
HETATM 8213 C C3  . GLC D 2 .   ? -28.803 49.308 18.709  1.00 37.16 ? 6   GLC D C3  1 
HETATM 8214 C C4  . GLC D 2 .   ? -30.002 50.062 18.226  1.00 42.37 ? 6   GLC D C4  1 
HETATM 8215 C C5  . GLC D 2 .   ? -30.989 49.159 17.477  1.00 25.44 ? 6   GLC D C5  1 
HETATM 8216 C C6  . GLC D 2 .   ? -32.118 50.074 16.988  1.00 42.99 ? 6   GLC D C6  1 
HETATM 8217 O O2  . GLC D 2 .   ? -27.160 47.827 17.975  1.00 19.74 ? 6   GLC D O2  1 
HETATM 8218 O O3  . GLC D 2 .   ? -27.813 50.148 19.252  1.00 38.80 ? 6   GLC D O3  1 
HETATM 8219 O O4  . GLC D 2 .   ? -30.708 50.560 19.336  1.00 51.46 ? 6   GLC D O4  1 
HETATM 8220 O O5  . GLC D 2 .   ? -30.345 48.443 16.461  1.00 31.83 ? 6   GLC D O5  1 
HETATM 8221 O O6  . GLC D 2 .   ? -32.533 50.895 18.112  1.00 43.91 ? 6   GLC D O6  1 
HETATM 8222 C C1  . GOL E 3 .   ? 20.374  20.255 53.217  1.00 43.73 ? 501 GOL A C1  1 
HETATM 8223 O O1  . GOL E 3 .   ? 19.954  20.202 51.884  1.00 46.46 ? 501 GOL A O1  1 
HETATM 8224 C C2  . GOL E 3 .   ? 19.778  19.013 53.908  1.00 40.05 ? 501 GOL A C2  1 
HETATM 8225 O O2  . GOL E 3 .   ? 20.513  17.867 53.658  1.00 32.60 ? 501 GOL A O2  1 
HETATM 8226 C C3  . GOL E 3 .   ? 19.671  19.366 55.423  1.00 43.18 ? 501 GOL A C3  1 
HETATM 8227 O O3  . GOL E 3 .   ? 20.957  19.684 55.861  1.00 50.15 ? 501 GOL A O3  1 
HETATM 8228 C C1  . GOL F 3 .   ? -16.355 22.462 64.623  1.00 13.66 ? 502 GOL A C1  1 
HETATM 8229 O O1  . GOL F 3 .   ? -17.276 23.334 64.055  1.00 13.70 ? 502 GOL A O1  1 
HETATM 8230 C C2  . GOL F 3 .   ? -16.945 21.917 65.949  1.00 14.26 ? 502 GOL A C2  1 
HETATM 8231 O O2  . GOL F 3 .   ? -16.065 20.944 66.477  1.00 12.86 ? 502 GOL A O2  1 
HETATM 8232 C C3  . GOL F 3 .   ? -18.354 21.354 65.559  1.00 15.27 ? 502 GOL A C3  1 
HETATM 8233 O O3  . GOL F 3 .   ? -18.998 20.944 66.754  1.00 9.28  ? 502 GOL A O3  1 
HETATM 8234 C C1  . GOL G 3 .   ? 6.183   31.238 78.147  1.00 56.25 ? 503 GOL A C1  1 
HETATM 8235 O O1  . GOL G 3 .   ? 6.322   32.138 77.071  1.00 61.09 ? 503 GOL A O1  1 
HETATM 8236 C C2  . GOL G 3 .   ? 7.172   31.631 79.192  1.00 58.73 ? 503 GOL A C2  1 
HETATM 8237 O O2  . GOL G 3 .   ? 6.759   32.877 79.747  1.00 62.16 ? 503 GOL A O2  1 
HETATM 8238 C C3  . GOL G 3 .   ? 8.630   31.678 78.719  1.00 55.17 ? 503 GOL A C3  1 
HETATM 8239 O O3  . GOL G 3 .   ? 8.739   32.003 77.333  1.00 55.15 ? 503 GOL A O3  1 
HETATM 8240 C C1  . GOL H 3 .   ? -11.008 0.434  60.943  1.00 20.00 ? 504 GOL A C1  1 
HETATM 8241 O O1  . GOL H 3 .   ? -11.122 0.183  62.292  1.00 20.00 ? 504 GOL A O1  1 
HETATM 8242 C C2  . GOL H 3 .   ? -9.804  -0.365 60.546  1.00 20.00 ? 504 GOL A C2  1 
HETATM 8243 O O2  . GOL H 3 .   ? -8.650  0.132  61.117  1.00 20.00 ? 504 GOL A O2  1 
HETATM 8244 C C3  . GOL H 3 .   ? -9.719  -0.577 59.055  1.00 20.00 ? 504 GOL A C3  1 
HETATM 8245 O O3  . GOL H 3 .   ? -9.680  0.668  58.482  1.00 20.00 ? 504 GOL A O3  1 
HETATM 8246 C C1  . GOL I 3 .   ? -17.398 41.486 29.334  1.00 18.02 ? 501 GOL B C1  1 
HETATM 8247 O O1  . GOL I 3 .   ? -16.908 40.954 28.090  1.00 15.12 ? 501 GOL B O1  1 
HETATM 8248 C C2  . GOL I 3 .   ? -18.888 42.007 29.147  1.00 14.33 ? 501 GOL B C2  1 
HETATM 8249 O O2  . GOL I 3 .   ? -19.790 41.011 28.756  1.00 15.47 ? 501 GOL B O2  1 
HETATM 8250 C C3  . GOL I 3 .   ? -19.291 42.547 30.551  1.00 16.38 ? 501 GOL B C3  1 
HETATM 8251 O O3  . GOL I 3 .   ? -18.292 43.443 30.979  1.00 17.56 ? 501 GOL B O3  1 
HETATM 8252 C C1  . GOL J 3 .   ? -24.713 20.594 37.265  1.00 48.41 ? 502 GOL B C1  1 
HETATM 8253 O O1  . GOL J 3 .   ? -24.580 19.542 38.142  1.00 53.88 ? 502 GOL B O1  1 
HETATM 8254 C C2  . GOL J 3 .   ? -24.523 20.010 35.847  1.00 45.32 ? 502 GOL B C2  1 
HETATM 8255 O O2  . GOL J 3 .   ? -23.231 20.155 35.381  1.00 54.42 ? 502 GOL B O2  1 
HETATM 8256 C C3  . GOL J 3 .   ? -25.491 20.795 35.018  1.00 39.82 ? 502 GOL B C3  1 
HETATM 8257 O O3  . GOL J 3 .   ? -26.717 20.505 35.573  1.00 30.40 ? 502 GOL B O3  1 
HETATM 8258 O O   . HOH K 4 .   ? -6.334  27.204 84.118  1.00 34.13 ? 601 HOH A O   1 
HETATM 8259 O O   . HOH K 4 .   ? -17.126 40.012 80.608  1.00 42.88 ? 602 HOH A O   1 
HETATM 8260 O O   . HOH K 4 .   ? -18.198 14.365 91.823  1.00 55.25 ? 603 HOH A O   1 
HETATM 8261 O O   . HOH K 4 .   ? -17.425 21.075 40.790  1.00 43.63 ? 604 HOH A O   1 
HETATM 8262 O O   . HOH K 4 .   ? -30.988 26.994 68.035  1.00 40.77 ? 605 HOH A O   1 
HETATM 8263 O O   . HOH K 4 .   ? -23.535 39.785 83.281  1.00 37.87 ? 606 HOH A O   1 
HETATM 8264 O O   . HOH K 4 .   ? -18.960 37.001 72.686  1.00 49.58 ? 607 HOH A O   1 
HETATM 8265 O O   . HOH K 4 .   ? -24.675 27.281 63.081  1.00 42.53 ? 608 HOH A O   1 
HETATM 8266 O O   . HOH K 4 .   ? 24.947  16.719 77.884  1.00 33.49 ? 609 HOH A O   1 
HETATM 8267 O O   . HOH K 4 .   ? -15.760 41.692 53.995  1.00 41.15 ? 610 HOH A O   1 
HETATM 8268 O O   . HOH K 4 .   ? -1.649  23.494 41.826  1.00 28.50 ? 611 HOH A O   1 
HETATM 8269 O O   . HOH K 4 .   ? -8.790  28.499 90.313  1.00 46.08 ? 612 HOH A O   1 
HETATM 8270 O O   . HOH K 4 .   ? 3.911   1.369  63.534  1.00 40.31 ? 613 HOH A O   1 
HETATM 8271 O O   . HOH K 4 .   ? -2.927  12.757 40.427  1.00 41.82 ? 614 HOH A O   1 
HETATM 8272 O O   . HOH K 4 .   ? 16.836  30.556 80.700  1.00 26.81 ? 615 HOH A O   1 
HETATM 8273 O O   . HOH K 4 .   ? 16.581  22.530 49.097  1.00 45.32 ? 616 HOH A O   1 
HETATM 8274 O O   . HOH K 4 .   ? 4.278   -0.415 80.548  1.00 49.59 ? 617 HOH A O   1 
HETATM 8275 O O   . HOH K 4 .   ? -7.499  29.448 83.276  1.00 53.12 ? 618 HOH A O   1 
HETATM 8276 O O   . HOH K 4 .   ? -4.247  -1.278 74.493  1.00 40.15 ? 619 HOH A O   1 
HETATM 8277 O O   . HOH K 4 .   ? 1.938   25.047 87.304  1.00 46.95 ? 620 HOH A O   1 
HETATM 8278 O O   . HOH K 4 .   ? -3.686  17.855 36.916  1.00 43.98 ? 621 HOH A O   1 
HETATM 8279 O O   . HOH K 4 .   ? -13.251 7.604  50.291  1.00 43.20 ? 622 HOH A O   1 
HETATM 8280 O O   . HOH K 4 .   ? 14.447  26.510 88.647  1.00 29.76 ? 623 HOH A O   1 
HETATM 8281 O O   . HOH K 4 .   ? -2.955  5.040  92.976  1.00 49.74 ? 624 HOH A O   1 
HETATM 8282 O O   . HOH K 4 .   ? -19.992 12.505 52.278  1.00 50.69 ? 625 HOH A O   1 
HETATM 8283 O O   . HOH K 4 .   ? -11.547 19.689 46.642  1.00 25.81 ? 626 HOH A O   1 
HETATM 8284 O O   . HOH K 4 .   ? -6.902  14.675 96.020  1.00 37.09 ? 627 HOH A O   1 
HETATM 8285 O O   . HOH K 4 .   ? -22.224 15.104 59.875  1.00 39.42 ? 628 HOH A O   1 
HETATM 8286 O O   . HOH K 4 .   ? 14.582  2.072  71.283  1.00 36.74 ? 629 HOH A O   1 
HETATM 8287 O O   . HOH K 4 .   ? 3.423   29.609 55.376  1.00 25.44 ? 630 HOH A O   1 
HETATM 8288 O O   . HOH K 4 .   ? -22.095 18.642 50.453  1.00 39.23 ? 631 HOH A O   1 
HETATM 8289 O O   . HOH K 4 .   ? -26.275 10.650 81.296  1.00 31.16 ? 632 HOH A O   1 
HETATM 8290 O O   . HOH K 4 .   ? -29.324 15.743 92.659  1.00 32.67 ? 633 HOH A O   1 
HETATM 8291 O O   . HOH K 4 .   ? 10.355  31.406 59.248  1.00 50.35 ? 634 HOH A O   1 
HETATM 8292 O O   . HOH K 4 .   ? 9.590   9.725  45.529  1.00 27.73 ? 635 HOH A O   1 
HETATM 8293 O O   . HOH K 4 .   ? 5.140   27.842 63.958  1.00 26.51 ? 636 HOH A O   1 
HETATM 8294 O O   . HOH K 4 .   ? -32.094 35.192 93.112  1.00 52.47 ? 637 HOH A O   1 
HETATM 8295 O O   . HOH K 4 .   ? 9.917   4.806  58.035  1.00 42.29 ? 638 HOH A O   1 
HETATM 8296 O O   . HOH K 4 .   ? -16.381 12.738 71.790  1.00 21.16 ? 639 HOH A O   1 
HETATM 8297 O O   . HOH K 4 .   ? -28.692 11.966 82.207  1.00 35.54 ? 640 HOH A O   1 
HETATM 8298 O O   . HOH K 4 .   ? 2.124   21.220 75.437  1.00 15.19 ? 641 HOH A O   1 
HETATM 8299 O O   . HOH K 4 .   ? -39.592 18.245 79.443  1.00 26.46 ? 642 HOH A O   1 
HETATM 8300 O O   . HOH K 4 .   ? -13.013 24.956 70.737  1.00 11.45 ? 643 HOH A O   1 
HETATM 8301 O O   . HOH K 4 .   ? -21.031 36.836 89.517  1.00 48.38 ? 644 HOH A O   1 
HETATM 8302 O O   . HOH K 4 .   ? -8.855  14.141 93.852  1.00 35.75 ? 645 HOH A O   1 
HETATM 8303 O O   . HOH K 4 .   ? -23.962 11.861 63.153  1.00 32.10 ? 646 HOH A O   1 
HETATM 8304 O O   . HOH K 4 .   ? -18.914 0.308  81.833  1.00 41.56 ? 647 HOH A O   1 
HETATM 8305 O O   . HOH K 4 .   ? 5.747   29.370 52.526  1.00 48.25 ? 648 HOH A O   1 
HETATM 8306 O O   . HOH K 4 .   ? -13.876 41.431 52.774  1.00 40.06 ? 649 HOH A O   1 
HETATM 8307 O O   . HOH K 4 .   ? -12.057 4.496  86.524  1.00 41.62 ? 650 HOH A O   1 
HETATM 8308 O O   . HOH K 4 .   ? 0.715   32.757 42.375  1.00 36.44 ? 651 HOH A O   1 
HETATM 8309 O O   . HOH K 4 .   ? 1.011   2.322  54.528  1.00 46.23 ? 652 HOH A O   1 
HETATM 8310 O O   . HOH K 4 .   ? -29.233 24.959 66.925  1.00 34.43 ? 653 HOH A O   1 
HETATM 8311 O O   . HOH K 4 .   ? 16.465  23.748 69.621  1.00 13.57 ? 654 HOH A O   1 
HETATM 8312 O O   . HOH K 4 .   ? 18.999  4.537  61.274  1.00 46.93 ? 655 HOH A O   1 
HETATM 8313 O O   . HOH K 4 .   ? -39.422 25.408 82.104  1.00 29.78 ? 656 HOH A O   1 
HETATM 8314 O O   . HOH K 4 .   ? -23.505 28.702 71.868  1.00 20.89 ? 657 HOH A O   1 
HETATM 8315 O O   . HOH K 4 .   ? -12.872 8.332  87.129  1.00 18.04 ? 658 HOH A O   1 
HETATM 8316 O O   . HOH K 4 .   ? -29.303 15.527 98.956  1.00 38.43 ? 659 HOH A O   1 
HETATM 8317 O O   . HOH K 4 .   ? -22.080 34.974 78.210  1.00 28.76 ? 660 HOH A O   1 
HETATM 8318 O O   . HOH K 4 .   ? -3.597  6.829  80.400  1.00 22.46 ? 661 HOH A O   1 
HETATM 8319 O O   . HOH K 4 .   ? -22.759 17.679 71.611  1.00 13.22 ? 662 HOH A O   1 
HETATM 8320 O O   . HOH K 4 .   ? -34.996 26.680 85.587  1.00 19.83 ? 663 HOH A O   1 
HETATM 8321 O O   . HOH K 4 .   ? -18.896 38.909 53.226  1.00 44.63 ? 664 HOH A O   1 
HETATM 8322 O O   . HOH K 4 .   ? 22.855  28.680 78.079  1.00 31.22 ? 665 HOH A O   1 
HETATM 8323 O O   . HOH K 4 .   ? -17.451 4.138  69.689  1.00 16.69 ? 666 HOH A O   1 
HETATM 8324 O O   . HOH K 4 .   ? -7.684  24.375 67.544  1.00 11.98 ? 667 HOH A O   1 
HETATM 8325 O O   . HOH K 4 .   ? -39.420 15.660 78.769  1.00 32.82 ? 668 HOH A O   1 
HETATM 8326 O O   . HOH K 4 .   ? -13.958 18.048 86.437  1.00 15.94 ? 669 HOH A O   1 
HETATM 8327 O O   . HOH K 4 .   ? -36.124 33.165 82.934  1.00 39.05 ? 670 HOH A O   1 
HETATM 8328 O O   . HOH K 4 .   ? -31.892 9.457  82.108  1.00 46.78 ? 671 HOH A O   1 
HETATM 8329 O O   . HOH K 4 .   ? 7.886   16.502 77.692  1.00 26.92 ? 672 HOH A O   1 
HETATM 8330 O O   . HOH K 4 .   ? -1.733  26.904 63.806  1.00 25.89 ? 673 HOH A O   1 
HETATM 8331 O O   . HOH K 4 .   ? 18.572  13.229 80.224  1.00 20.25 ? 674 HOH A O   1 
HETATM 8332 O O   . HOH K 4 .   ? 11.540  26.965 53.943  1.00 28.84 ? 675 HOH A O   1 
HETATM 8333 O O   . HOH K 4 .   ? -5.033  19.850 70.236  1.00 17.24 ? 676 HOH A O   1 
HETATM 8334 O O   . HOH K 4 .   ? 8.451   14.209 68.747  1.00 10.95 ? 677 HOH A O   1 
HETATM 8335 O O   . HOH K 4 .   ? -0.466  13.585 37.407  1.00 37.80 ? 678 HOH A O   1 
HETATM 8336 O O   . HOH K 4 .   ? -13.376 29.845 43.519  1.00 37.19 ? 679 HOH A O   1 
HETATM 8337 O O   . HOH K 4 .   ? 19.830  6.133  54.919  1.00 27.86 ? 680 HOH A O   1 
HETATM 8338 O O   . HOH K 4 .   ? 14.551  29.780 52.797  1.00 27.98 ? 681 HOH A O   1 
HETATM 8339 O O   . HOH K 4 .   ? -28.624 13.159 64.449  1.00 45.59 ? 682 HOH A O   1 
HETATM 8340 O O   . HOH K 4 .   ? 24.090  26.740 71.230  1.00 29.76 ? 683 HOH A O   1 
HETATM 8341 O O   . HOH K 4 .   ? 7.437   27.036 47.047  1.00 28.22 ? 684 HOH A O   1 
HETATM 8342 O O   . HOH K 4 .   ? -11.216 17.176 47.623  1.00 21.27 ? 685 HOH A O   1 
HETATM 8343 O O   . HOH K 4 .   ? -23.456 14.215 62.473  1.00 25.36 ? 686 HOH A O   1 
HETATM 8344 O O   . HOH K 4 .   ? -7.194  16.329 53.852  1.00 13.45 ? 687 HOH A O   1 
HETATM 8345 O O   . HOH K 4 .   ? -2.443  34.016 61.601  1.00 34.62 ? 688 HOH A O   1 
HETATM 8346 O O   . HOH K 4 .   ? -6.495  6.754  51.529  1.00 26.08 ? 689 HOH A O   1 
HETATM 8347 O O   . HOH K 4 .   ? -18.346 18.011 92.304  1.00 19.04 ? 690 HOH A O   1 
HETATM 8348 O O   . HOH K 4 .   ? 11.001  29.548 79.100  1.00 30.14 ? 691 HOH A O   1 
HETATM 8349 O O   . HOH K 4 .   ? -1.788  27.320 37.173  1.00 48.99 ? 692 HOH A O   1 
HETATM 8350 O O   . HOH K 4 .   ? -30.388 30.401 72.587  1.00 38.89 ? 693 HOH A O   1 
HETATM 8351 O O   . HOH K 4 .   ? -10.431 25.034 74.591  1.00 17.66 ? 694 HOH A O   1 
HETATM 8352 O O   . HOH K 4 .   ? 0.399   24.114 40.814  1.00 33.87 ? 695 HOH A O   1 
HETATM 8353 O O   . HOH K 4 .   ? 22.897  11.565 56.827  1.00 42.78 ? 696 HOH A O   1 
HETATM 8354 O O   . HOH K 4 .   ? -6.697  5.006  53.491  1.00 44.81 ? 697 HOH A O   1 
HETATM 8355 O O   . HOH K 4 .   ? 2.701   2.183  55.191  1.00 47.64 ? 698 HOH A O   1 
HETATM 8356 O O   . HOH K 4 .   ? 16.927  14.994 70.296  1.00 14.47 ? 699 HOH A O   1 
HETATM 8357 O O   . HOH K 4 .   ? -6.169  5.178  90.252  1.00 42.03 ? 700 HOH A O   1 
HETATM 8358 O O   . HOH K 4 .   ? -20.157 35.434 75.289  1.00 22.50 ? 701 HOH A O   1 
HETATM 8359 O O   . HOH K 4 .   ? 1.456   25.771 35.404  1.00 51.66 ? 702 HOH A O   1 
HETATM 8360 O O   . HOH K 4 .   ? 16.205  3.665  52.917  1.00 26.36 ? 703 HOH A O   1 
HETATM 8361 O O   . HOH K 4 .   ? -10.844 32.580 79.310  1.00 35.10 ? 704 HOH A O   1 
HETATM 8362 O O   . HOH K 4 .   ? 16.990  6.297  83.318  1.00 32.79 ? 705 HOH A O   1 
HETATM 8363 O O   . HOH K 4 .   ? -23.720 26.992 57.431  1.00 40.65 ? 706 HOH A O   1 
HETATM 8364 O O   . HOH K 4 .   ? -20.699 24.886 71.072  1.00 12.65 ? 707 HOH A O   1 
HETATM 8365 O O   . HOH K 4 .   ? -14.034 34.308 78.526  1.00 21.88 ? 708 HOH A O   1 
HETATM 8366 O O   . HOH K 4 .   ? 21.068  7.363  59.667  1.00 42.31 ? 709 HOH A O   1 
HETATM 8367 O O   . HOH K 4 .   ? 17.907  11.682 78.165  1.00 17.90 ? 710 HOH A O   1 
HETATM 8368 O O   . HOH K 4 .   ? -18.956 10.626 83.666  1.00 39.14 ? 711 HOH A O   1 
HETATM 8369 O O   . HOH K 4 .   ? -12.257 15.922 81.505  1.00 13.41 ? 712 HOH A O   1 
HETATM 8370 O O   . HOH K 4 .   ? -26.276 23.820 58.022  1.00 47.26 ? 713 HOH A O   1 
HETATM 8371 O O   . HOH K 4 .   ? 6.556   19.730 53.064  1.00 16.29 ? 714 HOH A O   1 
HETATM 8372 O O   . HOH K 4 .   ? -34.714 34.564 87.181  1.00 38.44 ? 715 HOH A O   1 
HETATM 8373 O O   . HOH K 4 .   ? 16.287  29.163 55.334  1.00 28.90 ? 716 HOH A O   1 
HETATM 8374 O O   . HOH K 4 .   ? -34.527 16.490 90.986  1.00 35.43 ? 717 HOH A O   1 
HETATM 8375 O O   . HOH K 4 .   ? -9.150  -4.456 70.537  1.00 42.16 ? 718 HOH A O   1 
HETATM 8376 O O   . HOH K 4 .   ? -21.953 7.961  64.190  1.00 38.28 ? 719 HOH A O   1 
HETATM 8377 O O   . HOH K 4 .   ? -6.720  6.358  47.224  1.00 42.64 ? 720 HOH A O   1 
HETATM 8378 O O   . HOH K 4 .   ? -23.029 17.080 68.748  1.00 12.48 ? 721 HOH A O   1 
HETATM 8379 O O   . HOH K 4 .   ? 15.229  5.697  72.694  1.00 36.38 ? 722 HOH A O   1 
HETATM 8380 O O   . HOH K 4 .   ? -16.320 33.967 63.923  1.00 22.13 ? 723 HOH A O   1 
HETATM 8381 O O   . HOH K 4 .   ? -30.254 32.875 76.834  1.00 18.69 ? 724 HOH A O   1 
HETATM 8382 O O   . HOH K 4 .   ? -14.790 33.066 60.138  1.00 19.31 ? 725 HOH A O   1 
HETATM 8383 O O   . HOH K 4 .   ? -29.459 34.820 73.925  1.00 30.51 ? 726 HOH A O   1 
HETATM 8384 O O   . HOH K 4 .   ? -9.058  7.182  50.346  1.00 23.61 ? 727 HOH A O   1 
HETATM 8385 O O   . HOH K 4 .   ? 0.026   14.968 78.319  1.00 10.74 ? 728 HOH A O   1 
HETATM 8386 O O   . HOH K 4 .   ? -8.814  -0.407 77.054  1.00 40.11 ? 729 HOH A O   1 
HETATM 8387 O O   . HOH K 4 .   ? -36.259 26.164 67.366  1.00 45.69 ? 730 HOH A O   1 
HETATM 8388 O O   . HOH K 4 .   ? 18.373  17.886 65.358  1.00 17.26 ? 731 HOH A O   1 
HETATM 8389 O O   . HOH K 4 .   ? -27.438 23.778 97.193  1.00 30.92 ? 732 HOH A O   1 
HETATM 8390 O O   . HOH K 4 .   ? 0.919   18.826 69.387  1.00 10.10 ? 733 HOH A O   1 
HETATM 8391 O O   . HOH K 4 .   ? 14.997  26.026 72.376  1.00 16.67 ? 734 HOH A O   1 
HETATM 8392 O O   . HOH K 4 .   ? 13.893  4.278  81.725  1.00 29.94 ? 735 HOH A O   1 
HETATM 8393 O O   . HOH K 4 .   ? 4.940   18.510 45.227  1.00 18.31 ? 736 HOH A O   1 
HETATM 8394 O O   . HOH K 4 .   ? -39.432 19.062 81.948  1.00 15.02 ? 737 HOH A O   1 
HETATM 8395 O O   . HOH K 4 .   ? 3.915   17.585 40.299  1.00 28.11 ? 738 HOH A O   1 
HETATM 8396 O O   . HOH K 4 .   ? -1.609  23.008 92.931  1.00 19.79 ? 739 HOH A O   1 
HETATM 8397 O O   . HOH K 4 .   ? -0.013  9.023  42.344  1.00 40.44 ? 740 HOH A O   1 
HETATM 8398 O O   . HOH K 4 .   ? -34.156 11.770 82.901  1.00 39.15 ? 741 HOH A O   1 
HETATM 8399 O O   . HOH K 4 .   ? -20.325 17.424 62.837  1.00 13.23 ? 742 HOH A O   1 
HETATM 8400 O O   . HOH K 4 .   ? 14.160  27.123 53.850  1.00 23.99 ? 743 HOH A O   1 
HETATM 8401 O O   . HOH K 4 .   ? -8.256  5.728  55.357  1.00 23.62 ? 744 HOH A O   1 
HETATM 8402 O O   . HOH K 4 .   ? -22.051 32.031 68.603  1.00 31.26 ? 745 HOH A O   1 
HETATM 8403 O O   . HOH K 4 .   ? 11.338  4.461  85.221  1.00 38.35 ? 746 HOH A O   1 
HETATM 8404 O O   . HOH K 4 .   ? -5.278  8.375  86.949  1.00 19.06 ? 747 HOH A O   1 
HETATM 8405 O O   . HOH K 4 .   ? 17.306  5.576  79.054  1.00 23.07 ? 748 HOH A O   1 
HETATM 8406 O O   . HOH K 4 .   ? -0.572  34.254 83.643  1.00 48.04 ? 749 HOH A O   1 
HETATM 8407 O O   . HOH K 4 .   ? 11.338  12.632 94.222  1.00 36.02 ? 750 HOH A O   1 
HETATM 8408 O O   . HOH K 4 .   ? -12.929 32.123 86.655  1.00 40.60 ? 751 HOH A O   1 
HETATM 8409 O O   . HOH K 4 .   ? -25.111 25.032 98.633  1.00 37.42 ? 752 HOH A O   1 
HETATM 8410 O O   . HOH K 4 .   ? 7.368   15.828 70.746  1.00 15.47 ? 753 HOH A O   1 
HETATM 8411 O O   . HOH K 4 .   ? -13.700 18.772 60.630  1.00 14.77 ? 754 HOH A O   1 
HETATM 8412 O O   . HOH K 4 .   ? -4.866  12.910 41.411  1.00 43.14 ? 755 HOH A O   1 
HETATM 8413 O O   . HOH K 4 .   ? -9.060  38.409 51.867  1.00 33.22 ? 756 HOH A O   1 
HETATM 8414 O O   . HOH K 4 .   ? -11.067 20.501 90.519  1.00 34.74 ? 757 HOH A O   1 
HETATM 8415 O O   . HOH K 4 .   ? -7.834  30.288 68.743  1.00 27.90 ? 758 HOH A O   1 
HETATM 8416 O O   . HOH K 4 .   ? -35.148 31.962 70.862  1.00 48.38 ? 759 HOH A O   1 
HETATM 8417 O O   . HOH K 4 .   ? -6.870  -2.814 60.988  1.00 30.13 ? 760 HOH A O   1 
HETATM 8418 O O   . HOH K 4 .   ? 18.231  18.574 88.028  1.00 30.10 ? 761 HOH A O   1 
HETATM 8419 O O   . HOH K 4 .   ? -8.510  12.004 47.645  1.00 24.38 ? 762 HOH A O   1 
HETATM 8420 O O   . HOH K 4 .   ? 22.383  14.483 76.209  1.00 31.58 ? 763 HOH A O   1 
HETATM 8421 O O   . HOH K 4 .   ? 2.698   21.937 53.230  1.00 17.87 ? 764 HOH A O   1 
HETATM 8422 O O   . HOH K 4 .   ? 13.948  12.925 46.340  1.00 36.42 ? 765 HOH A O   1 
HETATM 8423 O O   . HOH K 4 .   ? 16.940  15.645 47.034  1.00 31.48 ? 766 HOH A O   1 
HETATM 8424 O O   . HOH K 4 .   ? -20.208 7.364  56.476  1.00 39.14 ? 767 HOH A O   1 
HETATM 8425 O O   . HOH K 4 .   ? 10.247  2.858  59.581  1.00 26.25 ? 768 HOH A O   1 
HETATM 8426 O O   . HOH K 4 .   ? 19.752  8.799  69.027  1.00 43.47 ? 769 HOH A O   1 
HETATM 8427 O O   . HOH K 4 .   ? 16.879  5.967  68.903  1.00 52.47 ? 770 HOH A O   1 
HETATM 8428 O O   . HOH K 4 .   ? -16.041 6.652  51.465  1.00 35.95 ? 771 HOH A O   1 
HETATM 8429 O O   . HOH K 4 .   ? -13.538 35.885 81.067  1.00 50.65 ? 772 HOH A O   1 
HETATM 8430 O O   . HOH K 4 .   ? 19.116  31.916 73.390  1.00 28.87 ? 773 HOH A O   1 
HETATM 8431 O O   . HOH K 4 .   ? 12.704  22.857 48.150  1.00 31.62 ? 774 HOH A O   1 
HETATM 8432 O O   . HOH K 4 .   ? -6.042  34.354 44.467  1.00 35.76 ? 775 HOH A O   1 
HETATM 8433 O O   . HOH K 4 .   ? -33.218 11.079 78.587  1.00 45.60 ? 776 HOH A O   1 
HETATM 8434 O O   . HOH K 4 .   ? 16.680  17.142 89.999  1.00 29.35 ? 777 HOH A O   1 
HETATM 8435 O O   . HOH K 4 .   ? 8.619   27.594 72.514  1.00 21.53 ? 778 HOH A O   1 
HETATM 8436 O O   . HOH K 4 .   ? -16.084 6.124  71.862  1.00 13.88 ? 779 HOH A O   1 
HETATM 8437 O O   . HOH K 4 .   ? -6.708  36.192 67.935  1.00 27.92 ? 780 HOH A O   1 
HETATM 8438 O O   . HOH K 4 .   ? -11.253 33.375 46.683  1.00 43.01 ? 781 HOH A O   1 
HETATM 8439 O O   . HOH K 4 .   ? 17.543  8.220  68.326  1.00 33.58 ? 782 HOH A O   1 
HETATM 8440 O O   . HOH K 4 .   ? -31.107 25.506 95.311  1.00 38.74 ? 783 HOH A O   1 
HETATM 8441 O O   . HOH K 4 .   ? 13.240  32.667 84.945  1.00 35.87 ? 784 HOH A O   1 
HETATM 8442 O O   . HOH K 4 .   ? -18.222 16.231 69.186  1.00 10.05 ? 785 HOH A O   1 
HETATM 8443 O O   . HOH K 4 .   ? 4.297   24.758 91.703  1.00 30.94 ? 786 HOH A O   1 
HETATM 8444 O O   . HOH K 4 .   ? -5.564  5.561  56.100  1.00 27.23 ? 787 HOH A O   1 
HETATM 8445 O O   . HOH K 4 .   ? -13.771 35.854 68.730  1.00 39.42 ? 788 HOH A O   1 
HETATM 8446 O O   . HOH K 4 .   ? -27.855 16.513 63.267  1.00 37.23 ? 789 HOH A O   1 
HETATM 8447 O O   . HOH K 4 .   ? -34.993 20.094 68.863  1.00 27.08 ? 790 HOH A O   1 
HETATM 8448 O O   . HOH K 4 .   ? -0.997  32.087 49.166  1.00 25.04 ? 791 HOH A O   1 
HETATM 8449 O O   . HOH K 4 .   ? 13.629  29.507 65.387  1.00 28.34 ? 792 HOH A O   1 
HETATM 8450 O O   . HOH K 4 .   ? -17.534 2.161  63.092  1.00 30.58 ? 793 HOH A O   1 
HETATM 8451 O O   . HOH K 4 .   ? -18.134 30.125 62.142  1.00 16.35 ? 794 HOH A O   1 
HETATM 8452 O O   . HOH K 4 .   ? -24.983 13.458 58.754  1.00 43.06 ? 795 HOH A O   1 
HETATM 8453 O O   . HOH K 4 .   ? 14.223  24.626 64.667  1.00 18.77 ? 796 HOH A O   1 
HETATM 8454 O O   . HOH K 4 .   ? 1.464   32.830 60.698  1.00 26.04 ? 797 HOH A O   1 
HETATM 8455 O O   . HOH K 4 .   ? 19.069  24.830 50.358  1.00 28.21 ? 798 HOH A O   1 
HETATM 8456 O O   . HOH K 4 .   ? -36.564 20.909 87.445  1.00 16.53 ? 799 HOH A O   1 
HETATM 8457 O O   . HOH K 4 .   ? 10.839  15.580 42.609  1.00 31.18 ? 800 HOH A O   1 
HETATM 8458 O O   . HOH K 4 .   ? 14.433  6.480  80.272  1.00 18.79 ? 801 HOH A O   1 
HETATM 8459 O O   . HOH K 4 .   ? 19.434  28.192 60.915  1.00 43.41 ? 802 HOH A O   1 
HETATM 8460 O O   . HOH K 4 .   ? -26.732 30.405 95.089  1.00 52.51 ? 803 HOH A O   1 
HETATM 8461 O O   . HOH K 4 .   ? 8.574   23.467 93.693  1.00 22.51 ? 804 HOH A O   1 
HETATM 8462 O O   . HOH K 4 .   ? 5.158   30.388 66.983  1.00 30.17 ? 805 HOH A O   1 
HETATM 8463 O O   . HOH K 4 .   ? 21.153  9.340  78.108  1.00 44.89 ? 806 HOH A O   1 
HETATM 8464 O O   . HOH K 4 .   ? 3.421   32.454 58.886  1.00 50.56 ? 807 HOH A O   1 
HETATM 8465 O O   . HOH K 4 .   ? 5.130   15.415 94.094  1.00 37.16 ? 808 HOH A O   1 
HETATM 8466 O O   . HOH K 4 .   ? 19.654  7.248  84.077  1.00 35.58 ? 809 HOH A O   1 
HETATM 8467 O O   . HOH K 4 .   ? 21.104  13.596 80.266  1.00 29.83 ? 810 HOH A O   1 
HETATM 8468 O O   . HOH K 4 .   ? 10.784  15.017 92.707  1.00 21.64 ? 811 HOH A O   1 
HETATM 8469 O O   . HOH K 4 .   ? 19.422  21.068 88.298  1.00 23.90 ? 812 HOH A O   1 
HETATM 8470 O O   . HOH K 4 .   ? -34.442 28.453 95.385  1.00 33.32 ? 813 HOH A O   1 
HETATM 8471 O O   . HOH K 4 .   ? -9.997  30.758 67.112  1.00 15.22 ? 814 HOH A O   1 
HETATM 8472 O O   . HOH K 4 .   ? -3.486  24.776 66.891  1.00 28.28 ? 815 HOH A O   1 
HETATM 8473 O O   . HOH K 4 .   ? -13.451 1.199  73.501  1.00 45.65 ? 816 HOH A O   1 
HETATM 8474 O O   . HOH K 4 .   ? -9.242  31.633 64.581  1.00 12.43 ? 817 HOH A O   1 
HETATM 8475 O O   . HOH K 4 .   ? -5.158  5.665  58.916  1.00 15.04 ? 818 HOH A O   1 
HETATM 8476 O O   . HOH K 4 .   ? 19.550  15.756 69.480  1.00 30.22 ? 819 HOH A O   1 
HETATM 8477 O O   . HOH K 4 .   ? -11.285 37.854 51.810  1.00 41.89 ? 820 HOH A O   1 
HETATM 8478 O O   . HOH K 4 .   ? 22.207  12.092 72.660  1.00 44.17 ? 821 HOH A O   1 
HETATM 8479 O O   . HOH K 4 .   ? 14.950  1.783  68.802  1.00 46.81 ? 822 HOH A O   1 
HETATM 8480 O O   . HOH K 4 .   ? -1.207  33.264 59.293  1.00 44.01 ? 823 HOH A O   1 
HETATM 8481 O O   . HOH K 4 .   ? 3.991   32.725 64.827  1.00 42.49 ? 824 HOH A O   1 
HETATM 8482 O O   . HOH K 4 .   ? -24.698 20.474 56.692  1.00 42.91 ? 825 HOH A O   1 
HETATM 8483 O O   . HOH K 4 .   ? 9.712   3.916  82.798  1.00 42.35 ? 826 HOH A O   1 
HETATM 8484 O O   . HOH K 4 .   ? 11.159  32.708 70.994  1.00 37.11 ? 827 HOH A O   1 
HETATM 8485 O O   . HOH K 4 .   ? 1.473   -3.842 69.805  1.00 44.84 ? 828 HOH A O   1 
HETATM 8486 O O   . HOH K 4 .   ? -16.089 12.226 53.030  1.00 32.21 ? 829 HOH A O   1 
HETATM 8487 O O   . HOH K 4 .   ? -26.964 11.712 70.587  1.00 43.89 ? 830 HOH A O   1 
HETATM 8488 O O   . HOH K 4 .   ? -19.004 12.101 86.174  1.00 49.77 ? 831 HOH A O   1 
HETATM 8489 O O   . HOH K 4 .   ? -0.959  32.117 51.963  1.00 27.72 ? 832 HOH A O   1 
HETATM 8490 O O   . HOH K 4 .   ? 1.361   22.837 85.511  1.00 19.80 ? 833 HOH A O   1 
HETATM 8491 O O   . HOH K 4 .   ? 23.408  18.038 71.112  1.00 44.17 ? 834 HOH A O   1 
HETATM 8492 O O   . HOH K 4 .   ? -15.613 40.392 62.260  1.00 48.00 ? 835 HOH A O   1 
HETATM 8493 O O   . HOH K 4 .   ? 15.433  5.223  86.519  1.00 47.51 ? 836 HOH A O   1 
HETATM 8494 O O   . HOH K 4 .   ? 22.516  12.950 63.653  1.00 36.35 ? 837 HOH A O   1 
HETATM 8495 O O   . HOH K 4 .   ? -13.722 35.426 73.413  1.00 46.36 ? 838 HOH A O   1 
HETATM 8496 O O   . HOH K 4 .   ? -26.109 7.991  77.162  1.00 33.67 ? 839 HOH A O   1 
HETATM 8497 O O   . HOH K 4 .   ? 16.413  27.686 86.426  1.00 38.15 ? 840 HOH A O   1 
HETATM 8498 O O   . HOH K 4 .   ? 0.746   30.310 52.395  1.00 35.27 ? 841 HOH A O   1 
HETATM 8499 O O   . HOH K 4 .   ? -15.340 25.898 42.304  1.00 43.15 ? 842 HOH A O   1 
HETATM 8500 O O   . HOH K 4 .   ? 6.427   17.585 93.633  1.00 23.66 ? 843 HOH A O   1 
HETATM 8501 O O   . HOH K 4 .   ? -30.113 39.981 86.060  1.00 36.44 ? 844 HOH A O   1 
HETATM 8502 O O   . HOH K 4 .   ? 20.917  17.034 66.504  1.00 42.73 ? 845 HOH A O   1 
HETATM 8503 O O   . HOH K 4 .   ? 20.919  23.869 53.435  1.00 36.08 ? 846 HOH A O   1 
HETATM 8504 O O   . HOH K 4 .   ? 5.517   28.806 45.963  1.00 42.15 ? 847 HOH A O   1 
HETATM 8505 O O   . HOH K 4 .   ? -33.647 24.408 60.786  1.00 49.11 ? 848 HOH A O   1 
HETATM 8506 O O   . HOH K 4 .   ? -0.886  13.320 80.420  1.00 14.37 ? 849 HOH A O   1 
HETATM 8507 O O   . HOH K 4 .   ? -19.041 34.472 60.836  1.00 25.99 ? 850 HOH A O   1 
HETATM 8508 O O   . HOH K 4 .   ? 3.384   0.659  85.091  1.00 29.14 ? 851 HOH A O   1 
HETATM 8509 O O   . HOH K 4 .   ? -1.317  5.668  61.139  1.00 28.23 ? 852 HOH A O   1 
HETATM 8510 O O   . HOH K 4 .   ? 17.566  -0.315 60.077  1.00 47.53 ? 853 HOH A O   1 
HETATM 8511 O O   . HOH K 4 .   ? 6.447   30.242 65.085  1.00 33.66 ? 854 HOH A O   1 
HETATM 8512 O O   . HOH K 4 .   ? 21.451  26.567 48.825  1.00 41.63 ? 855 HOH A O   1 
HETATM 8513 O O   . HOH K 4 .   ? -6.615  33.651 68.511  1.00 31.39 ? 856 HOH A O   1 
HETATM 8514 O O   . HOH K 4 .   ? 6.567   34.568 71.205  1.00 42.96 ? 857 HOH A O   1 
HETATM 8515 O O   . HOH K 4 .   ? 13.840  2.749  90.491  1.00 52.54 ? 858 HOH A O   1 
HETATM 8516 O O   . HOH K 4 .   ? -6.533  2.940  56.587  1.00 39.35 ? 859 HOH A O   1 
HETATM 8517 O O   . HOH K 4 .   ? -11.045 -0.675 54.055  1.00 46.44 ? 860 HOH A O   1 
HETATM 8518 O O   . HOH K 4 .   ? -11.573 2.819  81.121  1.00 35.20 ? 861 HOH A O   1 
HETATM 8519 O O   . HOH K 4 .   ? -24.388 29.640 69.620  1.00 40.12 ? 862 HOH A O   1 
HETATM 8520 O O   . HOH K 4 .   ? -16.050 5.184  88.712  1.00 47.12 ? 863 HOH A O   1 
HETATM 8521 O O   . HOH K 4 .   ? -25.440 32.499 94.250  1.00 44.94 ? 864 HOH A O   1 
HETATM 8522 O O   . HOH K 4 .   ? -18.370 8.426  82.658  1.00 33.42 ? 865 HOH A O   1 
HETATM 8523 O O   . HOH K 4 .   ? -33.479 33.492 75.985  1.00 50.13 ? 866 HOH A O   1 
HETATM 8524 O O   . HOH K 4 .   ? 21.650  12.337 75.258  1.00 38.85 ? 867 HOH A O   1 
HETATM 8525 O O   . HOH K 4 .   ? -19.522 41.323 77.763  1.00 43.86 ? 868 HOH A O   1 
HETATM 8526 O O   . HOH K 4 .   ? 19.390  15.414 67.329  1.00 20.39 ? 869 HOH A O   1 
HETATM 8527 O O   . HOH K 4 .   ? 24.823  14.995 86.549  1.00 41.22 ? 870 HOH A O   1 
HETATM 8528 O O   . HOH K 4 .   ? -36.672 33.290 89.631  1.00 47.85 ? 871 HOH A O   1 
HETATM 8529 O O   . HOH K 4 .   ? -16.561 0.707  65.196  1.00 31.27 ? 872 HOH A O   1 
HETATM 8530 O O   . HOH K 4 .   ? 1.856   0.490  94.681  1.00 52.77 ? 873 HOH A O   1 
HETATM 8531 O O   . HOH K 4 .   ? 0.107   -3.551 61.453  1.00 37.13 ? 874 HOH A O   1 
HETATM 8532 O O   . HOH K 4 .   ? -23.906 34.344 93.215  1.00 39.65 ? 875 HOH A O   1 
HETATM 8533 O O   . HOH K 4 .   ? -9.217  27.070 73.718  1.00 36.91 ? 876 HOH A O   1 
HETATM 8534 O O   . HOH K 4 .   ? -30.051 38.594 93.305  1.00 53.75 ? 877 HOH A O   1 
HETATM 8535 O O   . HOH K 4 .   ? -1.652  34.771 49.345  1.00 45.28 ? 878 HOH A O   1 
HETATM 8536 O O   . HOH K 4 .   ? 11.547  33.506 76.912  1.00 53.61 ? 879 HOH A O   1 
HETATM 8537 O O   . HOH K 4 .   ? -20.432 6.248  65.106  1.00 35.16 ? 880 HOH A O   1 
HETATM 8538 O O   . HOH K 4 .   ? -2.204  8.591  46.155  1.00 38.35 ? 881 HOH A O   1 
HETATM 8539 O O   . HOH K 4 .   ? -23.595 35.021 91.126  1.00 46.07 ? 882 HOH A O   1 
HETATM 8540 O O   . HOH K 4 .   ? 12.626  19.659 93.596  1.00 55.87 ? 883 HOH A O   1 
HETATM 8541 O O   . HOH K 4 .   ? 8.988   3.303  84.946  1.00 50.69 ? 884 HOH A O   1 
HETATM 8542 O O   . HOH K 4 .   ? -8.256  0.493  55.509  1.00 50.30 ? 885 HOH A O   1 
HETATM 8543 O O   . HOH K 4 .   ? 7.258   13.772 94.687  1.00 42.63 ? 886 HOH A O   1 
HETATM 8544 O O   . HOH K 4 .   ? 20.315  11.279 77.154  1.00 32.69 ? 887 HOH A O   1 
HETATM 8545 O O   . HOH K 4 .   ? -6.478  28.166 69.350  1.00 53.26 ? 888 HOH A O   1 
HETATM 8546 O O   . HOH K 4 .   ? -27.951 14.397 63.159  1.00 41.63 ? 889 HOH A O   1 
HETATM 8547 O O   . HOH K 4 .   ? 7.067   8.844  44.127  1.00 47.02 ? 890 HOH A O   1 
HETATM 8548 O O   . HOH K 4 .   ? -30.034 40.439 92.029  1.00 40.15 ? 891 HOH A O   1 
HETATM 8549 O O   . HOH K 4 .   ? 13.634  0.552  56.055  1.00 49.28 ? 892 HOH A O   1 
HETATM 8550 O O   . HOH K 4 .   ? 16.189  29.381 85.440  1.00 41.98 ? 893 HOH A O   1 
HETATM 8551 O O   . HOH K 4 .   ? -21.375 8.908  56.356  1.00 50.86 ? 894 HOH A O   1 
HETATM 8552 O O   . HOH K 4 .   ? -18.781 2.712  73.761  1.00 42.95 ? 895 HOH A O   1 
HETATM 8553 O O   . HOH K 4 .   ? -37.763 23.238 87.587  1.00 42.37 ? 896 HOH A O   1 
HETATM 8554 O O   . HOH K 4 .   ? -2.901  4.271  58.995  1.00 27.92 ? 897 HOH A O   1 
HETATM 8555 O O   . HOH K 4 .   ? -25.626 8.385  80.388  1.00 50.48 ? 898 HOH A O   1 
HETATM 8556 O O   . HOH K 4 .   ? -15.602 1.832  71.065  1.00 41.46 ? 899 HOH A O   1 
HETATM 8557 O O   . HOH K 4 .   ? -22.915 24.207 53.450  1.00 46.55 ? 900 HOH A O   1 
HETATM 8558 O O   . HOH K 4 .   ? -20.697 2.230  69.577  1.00 54.94 ? 901 HOH A O   1 
HETATM 8559 O O   . HOH K 4 .   ? 21.818  16.035 68.077  1.00 42.36 ? 902 HOH A O   1 
HETATM 8560 O O   . HOH K 4 .   ? -5.716  26.312 67.664  1.00 28.85 ? 903 HOH A O   1 
HETATM 8561 O O   . HOH K 4 .   ? -32.843 17.385 99.137  1.00 47.92 ? 904 HOH A O   1 
HETATM 8562 O O   . HOH K 4 .   ? -14.934 2.054  74.705  1.00 48.47 ? 905 HOH A O   1 
HETATM 8563 O O   . HOH K 4 .   ? -2.770  3.537  56.233  1.00 55.74 ? 906 HOH A O   1 
HETATM 8564 O O   . HOH K 4 .   ? 15.540  31.640 78.316  1.00 46.10 ? 907 HOH A O   1 
HETATM 8565 O O   . HOH K 4 .   ? 7.490   32.109 64.216  1.00 39.93 ? 908 HOH A O   1 
HETATM 8566 O O   . HOH K 4 .   ? -21.343 11.936 85.403  1.00 45.22 ? 909 HOH A O   1 
HETATM 8567 O O   . HOH K 4 .   ? -17.212 32.535 61.546  1.00 20.86 ? 910 HOH A O   1 
HETATM 8568 O O   . HOH K 4 .   ? 24.875  17.042 72.442  1.00 40.74 ? 911 HOH A O   1 
HETATM 8569 O O   . HOH K 4 .   ? -22.493 26.237 52.744  1.00 50.23 ? 912 HOH A O   1 
HETATM 8570 O O   . HOH K 4 .   ? -14.008 -2.723 67.514  1.00 41.08 ? 913 HOH A O   1 
HETATM 8571 O O   . HOH K 4 .   ? -27.452 36.880 72.894  1.00 50.49 ? 914 HOH A O   1 
HETATM 8572 O O   . HOH K 4 .   ? -5.905  39.463 54.849  1.00 43.82 ? 915 HOH A O   1 
HETATM 8573 O O   . HOH K 4 .   ? -17.958 0.081  70.015  1.00 44.27 ? 916 HOH A O   1 
HETATM 8574 O O   . HOH K 4 .   ? 18.448  28.661 63.896  1.00 51.16 ? 917 HOH A O   1 
HETATM 8575 O O   . HOH K 4 .   ? -11.371 34.703 83.132  1.00 50.90 ? 918 HOH A O   1 
HETATM 8576 O O   . HOH K 4 .   ? -15.327 8.053  49.859  1.00 46.63 ? 919 HOH A O   1 
HETATM 8577 O O   . HOH K 4 .   ? -3.182  7.199  44.536  1.00 43.50 ? 920 HOH A O   1 
HETATM 8578 O O   . HOH K 4 .   ? 0.005   38.357 54.313  1.00 63.55 ? 921 HOH A O   1 
HETATM 8579 O O   . HOH K 4 .   ? -16.415 19.710 93.694  1.00 38.10 ? 922 HOH A O   1 
HETATM 8580 O O   . HOH K 4 .   ? 12.638  31.707 78.496  1.00 38.25 ? 923 HOH A O   1 
HETATM 8581 O O   . HOH K 4 .   ? -23.050 3.812  70.256  1.00 48.12 ? 924 HOH A O   1 
HETATM 8582 O O   . HOH K 4 .   ? -12.246 34.523 85.496  1.00 47.38 ? 925 HOH A O   1 
HETATM 8583 O O   . HOH K 4 .   ? -6.963  3.588  91.695  1.00 54.03 ? 926 HOH A O   1 
HETATM 8584 O O   . HOH K 4 .   ? 17.209  4.294  81.560  1.00 49.45 ? 927 HOH A O   1 
HETATM 8585 O O   . HOH K 4 .   ? -4.618  2.591  86.691  1.00 46.55 ? 928 HOH A O   1 
HETATM 8586 O O   . HOH K 4 .   ? 22.070  10.860 80.333  1.00 51.84 ? 929 HOH A O   1 
HETATM 8587 O O   . HOH K 4 .   ? -16.337 38.774 65.195  1.00 47.00 ? 930 HOH A O   1 
HETATM 8588 O O   . HOH K 4 .   ? 14.320  18.762 93.326  1.00 52.98 ? 931 HOH A O   1 
HETATM 8589 O O   . HOH K 4 .   ? -12.437 34.596 76.051  1.00 45.26 ? 932 HOH A O   1 
HETATM 8590 O O   . HOH K 4 .   ? -31.287 32.639 74.488  1.00 40.13 ? 933 HOH A O   1 
HETATM 8591 O O   . HOH K 4 .   ? -25.831 17.595 61.542  1.00 44.14 ? 934 HOH A O   1 
HETATM 8592 O O   . HOH K 4 .   ? 17.777  32.712 81.266  1.00 45.06 ? 935 HOH A O   1 
HETATM 8593 O O   . HOH K 4 .   ? -0.962  11.682 36.092  1.00 44.50 ? 936 HOH A O   1 
HETATM 8594 O O   . HOH K 4 .   ? 14.931  33.313 71.273  1.00 50.71 ? 937 HOH A O   1 
HETATM 8595 O O   . HOH K 4 .   ? -8.988  34.119 71.147  1.00 56.69 ? 938 HOH A O   1 
HETATM 8596 O O   . HOH K 4 .   ? 1.727   32.192 48.033  1.00 36.76 ? 939 HOH A O   1 
HETATM 8597 O O   . HOH K 4 .   ? -15.765 3.463  73.376  1.00 41.66 ? 940 HOH A O   1 
HETATM 8598 O O   . HOH K 4 .   ? 16.443  32.610 75.217  1.00 48.45 ? 941 HOH A O   1 
HETATM 8599 O O   . HOH K 4 .   ? 17.045  19.415 92.329  1.00 49.06 ? 942 HOH A O   1 
HETATM 8600 O O   . HOH K 4 .   ? 14.419  33.915 73.268  1.00 48.26 ? 943 HOH A O   1 
HETATM 8601 O O   . HOH L 4 .   ? -54.799 49.582 51.372  1.00 39.24 ? 601 HOH B O   1 
HETATM 8602 O O   . HOH L 4 .   ? -24.573 32.396 51.048  1.00 51.67 ? 602 HOH B O   1 
HETATM 8603 O O   . HOH L 4 .   ? -32.587 46.545 13.016  1.00 38.69 ? 603 HOH B O   1 
HETATM 8604 O O   . HOH L 4 .   ? -40.133 46.863 57.926  1.00 38.87 ? 604 HOH B O   1 
HETATM 8605 O O   . HOH L 4 .   ? -49.394 43.451 50.885  1.00 40.05 ? 605 HOH B O   1 
HETATM 8606 O O   . HOH L 4 .   ? -16.825 32.813 50.193  1.00 43.38 ? 606 HOH B O   1 
HETATM 8607 O O   . HOH L 4 .   ? -39.665 50.123 45.346  1.00 46.48 ? 607 HOH B O   1 
HETATM 8608 O O   . HOH L 4 .   ? -55.693 37.192 33.020  1.00 42.37 ? 608 HOH B O   1 
HETATM 8609 O O   . HOH L 4 .   ? -24.432 40.445 59.284  1.00 45.29 ? 609 HOH B O   1 
HETATM 8610 O O   . HOH L 4 .   ? -17.427 30.208 48.733  1.00 42.54 ? 610 HOH B O   1 
HETATM 8611 O O   . HOH L 4 .   ? -39.361 41.106 22.794  1.00 22.54 ? 611 HOH B O   1 
HETATM 8612 O O   . HOH L 4 .   ? -13.824 55.215 38.152  1.00 39.74 ? 612 HOH B O   1 
HETATM 8613 O O   . HOH L 4 .   ? -6.845  35.782 26.736  1.00 31.57 ? 613 HOH B O   1 
HETATM 8614 O O   . HOH L 4 .   ? -40.131 25.535 46.944  1.00 44.26 ? 614 HOH B O   1 
HETATM 8615 O O   . HOH L 4 .   ? -45.913 43.871 50.588  1.00 24.60 ? 615 HOH B O   1 
HETATM 8616 O O   . HOH L 4 .   ? -6.807  28.045 24.748  1.00 49.07 ? 616 HOH B O   1 
HETATM 8617 O O   . HOH L 4 .   ? -28.981 19.295 20.452  1.00 47.40 ? 617 HOH B O   1 
HETATM 8618 O O   . HOH L 4 .   ? -11.333 35.160 0.940   1.00 39.94 ? 618 HOH B O   1 
HETATM 8619 O O   . HOH L 4 .   ? -45.246 36.449 21.572  1.00 30.93 ? 619 HOH B O   1 
HETATM 8620 O O   . HOH L 4 .   ? -21.753 40.489 49.073  1.00 27.13 ? 620 HOH B O   1 
HETATM 8621 O O   . HOH L 4 .   ? -20.526 32.645 23.781  1.00 36.78 ? 621 HOH B O   1 
HETATM 8622 O O   . HOH L 4 .   ? -43.167 33.791 56.364  1.00 53.80 ? 622 HOH B O   1 
HETATM 8623 O O   . HOH L 4 .   ? -37.597 50.008 42.678  1.00 28.64 ? 623 HOH B O   1 
HETATM 8624 O O   . HOH L 4 .   ? -40.296 47.072 51.993  1.00 35.05 ? 624 HOH B O   1 
HETATM 8625 O O   . HOH L 4 .   ? -0.046  38.047 9.424   1.00 37.75 ? 625 HOH B O   1 
HETATM 8626 O O   . HOH L 4 .   ? -52.922 43.768 30.753  1.00 24.28 ? 626 HOH B O   1 
HETATM 8627 O O   . HOH L 4 .   ? -34.517 26.658 17.364  1.00 30.04 ? 627 HOH B O   1 
HETATM 8628 O O   . HOH L 4 .   ? -59.540 44.825 20.949  1.00 37.53 ? 628 HOH B O   1 
HETATM 8629 O O   . HOH L 4 .   ? -44.484 25.348 41.716  1.00 26.54 ? 629 HOH B O   1 
HETATM 8630 O O   . HOH L 4 .   ? -11.923 34.480 31.871  1.00 37.92 ? 630 HOH B O   1 
HETATM 8631 O O   . HOH L 4 .   ? -5.758  44.183 26.033  1.00 42.40 ? 631 HOH B O   1 
HETATM 8632 O O   . HOH L 4 .   ? -40.780 48.172 34.344  1.00 29.81 ? 632 HOH B O   1 
HETATM 8633 O O   . HOH L 4 .   ? -13.970 43.256 -3.394  1.00 34.41 ? 633 HOH B O   1 
HETATM 8634 O O   . HOH L 4 .   ? -55.038 50.606 20.271  1.00 34.95 ? 634 HOH B O   1 
HETATM 8635 O O   . HOH L 4 .   ? -12.936 30.323 12.629  1.00 43.94 ? 635 HOH B O   1 
HETATM 8636 O O   . HOH L 4 .   ? -23.474 44.845 24.967  1.00 16.10 ? 636 HOH B O   1 
HETATM 8637 O O   . HOH L 4 .   ? -16.490 56.973 45.859  1.00 45.79 ? 637 HOH B O   1 
HETATM 8638 O O   . HOH L 4 .   ? -40.124 29.063 47.810  1.00 26.37 ? 638 HOH B O   1 
HETATM 8639 O O   . HOH L 4 .   ? -15.286 37.515 31.860  1.00 21.53 ? 639 HOH B O   1 
HETATM 8640 O O   . HOH L 4 .   ? -22.209 37.573 3.048   1.00 26.45 ? 640 HOH B O   1 
HETATM 8641 O O   . HOH L 4 .   ? -28.555 36.753 59.058  1.00 45.36 ? 641 HOH B O   1 
HETATM 8642 O O   . HOH L 4 .   ? -57.538 33.019 45.647  1.00 44.67 ? 642 HOH B O   1 
HETATM 8643 O O   . HOH L 4 .   ? -22.373 55.640 26.786  1.00 41.13 ? 643 HOH B O   1 
HETATM 8644 O O   . HOH L 4 .   ? -42.016 30.624 53.957  1.00 26.49 ? 644 HOH B O   1 
HETATM 8645 O O   . HOH L 4 .   ? -12.564 35.325 34.477  1.00 37.72 ? 645 HOH B O   1 
HETATM 8646 O O   . HOH L 4 .   ? -26.533 28.026 9.279   1.00 27.22 ? 646 HOH B O   1 
HETATM 8647 O O   . HOH L 4 .   ? -16.671 35.937 -3.121  1.00 43.95 ? 647 HOH B O   1 
HETATM 8648 O O   . HOH L 4 .   ? -21.878 37.855 48.297  1.00 22.58 ? 648 HOH B O   1 
HETATM 8649 O O   . HOH L 4 .   ? -31.459 34.010 2.979   1.00 37.41 ? 649 HOH B O   1 
HETATM 8650 O O   . HOH L 4 .   ? -53.298 35.058 30.417  1.00 23.31 ? 650 HOH B O   1 
HETATM 8651 O O   . HOH L 4 .   ? -49.203 19.045 35.378  1.00 51.73 ? 651 HOH B O   1 
HETATM 8652 O O   . HOH L 4 .   ? -17.245 55.153 19.168  1.00 32.87 ? 652 HOH B O   1 
HETATM 8653 O O   . HOH L 4 .   ? -55.364 31.355 22.943  1.00 27.12 ? 653 HOH B O   1 
HETATM 8654 O O   . HOH L 4 .   ? -30.537 47.312 13.770  1.00 41.22 ? 654 HOH B O   1 
HETATM 8655 O O   . HOH L 4 .   ? -4.841  31.496 9.274   1.00 44.53 ? 655 HOH B O   1 
HETATM 8656 O O   . HOH L 4 .   ? -10.145 31.388 22.272  1.00 45.29 ? 656 HOH B O   1 
HETATM 8657 O O   . HOH L 4 .   ? -53.789 38.140 35.456  1.00 20.97 ? 657 HOH B O   1 
HETATM 8658 O O   . HOH L 4 .   ? -44.686 34.241 30.570  1.00 15.65 ? 658 HOH B O   1 
HETATM 8659 O O   . HOH L 4 .   ? -20.352 53.253 34.947  1.00 22.13 ? 659 HOH B O   1 
HETATM 8660 O O   . HOH L 4 .   ? -21.427 38.395 52.753  1.00 37.22 ? 660 HOH B O   1 
HETATM 8661 O O   . HOH L 4 .   ? -21.280 39.054 35.080  1.00 17.42 ? 661 HOH B O   1 
HETATM 8662 O O   . HOH L 4 .   ? -49.163 49.389 20.682  1.00 30.81 ? 662 HOH B O   1 
HETATM 8663 O O   . HOH L 4 .   ? -14.153 37.550 22.808  1.00 22.73 ? 663 HOH B O   1 
HETATM 8664 O O   . HOH L 4 .   ? -19.389 24.161 25.659  1.00 26.76 ? 664 HOH B O   1 
HETATM 8665 O O   . HOH L 4 .   ? -37.825 34.782 19.837  1.00 16.81 ? 665 HOH B O   1 
HETATM 8666 O O   . HOH L 4 .   ? -13.210 48.469 22.135  1.00 33.42 ? 666 HOH B O   1 
HETATM 8667 O O   . HOH L 4 .   ? -27.427 55.533 51.097  1.00 43.04 ? 667 HOH B O   1 
HETATM 8668 O O   . HOH L 4 .   ? -19.447 54.165 31.105  1.00 32.71 ? 668 HOH B O   1 
HETATM 8669 O O   . HOH L 4 .   ? -13.459 36.952 25.571  1.00 20.38 ? 669 HOH B O   1 
HETATM 8670 O O   . HOH L 4 .   ? -38.615 42.565 5.068   1.00 24.20 ? 670 HOH B O   1 
HETATM 8671 O O   . HOH L 4 .   ? -26.037 26.180 41.319  1.00 31.57 ? 671 HOH B O   1 
HETATM 8672 O O   . HOH L 4 .   ? -14.207 43.578 26.512  1.00 23.88 ? 672 HOH B O   1 
HETATM 8673 O O   . HOH L 4 .   ? -57.886 29.291 37.463  1.00 42.92 ? 673 HOH B O   1 
HETATM 8674 O O   . HOH L 4 .   ? -39.524 44.751 11.144  1.00 41.54 ? 674 HOH B O   1 
HETATM 8675 O O   . HOH L 4 .   ? -6.220  35.865 1.605   1.00 42.58 ? 675 HOH B O   1 
HETATM 8676 O O   . HOH L 4 .   ? -55.060 25.231 22.165  1.00 29.96 ? 676 HOH B O   1 
HETATM 8677 O O   . HOH L 4 .   ? -51.897 45.941 27.927  1.00 26.80 ? 677 HOH B O   1 
HETATM 8678 O O   . HOH L 4 .   ? -33.262 24.813 7.310   1.00 51.57 ? 678 HOH B O   1 
HETATM 8679 O O   . HOH L 4 .   ? -16.220 41.983 61.052  1.00 40.15 ? 679 HOH B O   1 
HETATM 8680 O O   . HOH L 4 .   ? -49.657 49.442 44.640  1.00 30.08 ? 680 HOH B O   1 
HETATM 8681 O O   . HOH L 4 .   ? -26.841 36.692 42.770  1.00 15.22 ? 681 HOH B O   1 
HETATM 8682 O O   . HOH L 4 .   ? -15.623 44.907 23.506  1.00 22.85 ? 682 HOH B O   1 
HETATM 8683 O O   . HOH L 4 .   ? -31.511 39.932 26.905  1.00 21.60 ? 683 HOH B O   1 
HETATM 8684 O O   . HOH L 4 .   ? 0.958   45.612 18.982  1.00 35.53 ? 684 HOH B O   1 
HETATM 8685 O O   . HOH L 4 .   ? -49.407 49.651 33.989  1.00 33.26 ? 685 HOH B O   1 
HETATM 8686 O O   . HOH L 4 .   ? -40.292 40.288 45.505  1.00 16.62 ? 686 HOH B O   1 
HETATM 8687 O O   . HOH L 4 .   ? -19.389 20.672 29.658  1.00 35.30 ? 687 HOH B O   1 
HETATM 8688 O O   . HOH L 4 .   ? -37.388 39.317 52.838  1.00 13.58 ? 688 HOH B O   1 
HETATM 8689 O O   . HOH L 4 .   ? -20.530 35.187 0.397   1.00 41.78 ? 689 HOH B O   1 
HETATM 8690 O O   . HOH L 4 .   ? -25.436 37.707 9.540   1.00 18.60 ? 690 HOH B O   1 
HETATM 8691 O O   . HOH L 4 .   ? -35.816 38.487 57.568  1.00 26.07 ? 691 HOH B O   1 
HETATM 8692 O O   . HOH L 4 .   ? -62.597 39.735 23.103  1.00 31.06 ? 692 HOH B O   1 
HETATM 8693 O O   . HOH L 4 .   ? -46.584 34.180 53.816  1.00 29.90 ? 693 HOH B O   1 
HETATM 8694 O O   . HOH L 4 .   ? -24.667 32.512 48.756  1.00 28.83 ? 694 HOH B O   1 
HETATM 8695 O O   . HOH L 4 .   ? -40.528 33.452 56.587  1.00 46.99 ? 695 HOH B O   1 
HETATM 8696 O O   . HOH L 4 .   ? -25.291 18.453 27.043  1.00 36.33 ? 696 HOH B O   1 
HETATM 8697 O O   . HOH L 4 .   ? -37.349 38.834 28.649  1.00 12.40 ? 697 HOH B O   1 
HETATM 8698 O O   . HOH L 4 .   ? -40.008 52.626 33.077  1.00 43.48 ? 698 HOH B O   1 
HETATM 8699 O O   . HOH L 4 .   ? -43.931 35.798 28.415  1.00 22.15 ? 699 HOH B O   1 
HETATM 8700 O O   . HOH L 4 .   ? -26.279 35.588 14.773  1.00 17.34 ? 700 HOH B O   1 
HETATM 8701 O O   . HOH L 4 .   ? -29.434 56.332 29.190  1.00 37.00 ? 701 HOH B O   1 
HETATM 8702 O O   . HOH L 4 .   ? -33.647 46.996 33.343  1.00 29.55 ? 702 HOH B O   1 
HETATM 8703 O O   . HOH L 4 .   ? -56.839 32.850 21.214  1.00 36.53 ? 703 HOH B O   1 
HETATM 8704 O O   . HOH L 4 .   ? -16.735 44.556 -7.174  1.00 34.07 ? 704 HOH B O   1 
HETATM 8705 O O   . HOH L 4 .   ? -26.801 44.883 21.582  1.00 22.35 ? 705 HOH B O   1 
HETATM 8706 O O   . HOH L 4 .   ? -48.812 42.942 5.969   1.00 35.60 ? 706 HOH B O   1 
HETATM 8707 O O   . HOH L 4 .   ? -34.345 22.451 43.724  1.00 46.23 ? 707 HOH B O   1 
HETATM 8708 O O   . HOH L 4 .   ? -33.976 27.974 10.550  1.00 26.67 ? 708 HOH B O   1 
HETATM 8709 O O   . HOH L 4 .   ? -25.046 58.773 43.972  1.00 39.18 ? 709 HOH B O   1 
HETATM 8710 O O   . HOH L 4 .   ? -53.312 40.050 44.783  1.00 36.25 ? 710 HOH B O   1 
HETATM 8711 O O   . HOH L 4 .   ? -20.850 26.143 23.756  1.00 21.17 ? 711 HOH B O   1 
HETATM 8712 O O   . HOH L 4 .   ? -28.377 44.453 28.973  1.00 13.04 ? 712 HOH B O   1 
HETATM 8713 O O   . HOH L 4 .   ? -42.760 44.621 54.262  1.00 24.74 ? 713 HOH B O   1 
HETATM 8714 O O   . HOH L 4 .   ? -9.687  31.299 26.061  1.00 45.56 ? 714 HOH B O   1 
HETATM 8715 O O   . HOH L 4 .   ? -27.176 27.102 45.426  1.00 28.08 ? 715 HOH B O   1 
HETATM 8716 O O   . HOH L 4 .   ? -32.836 53.881 35.481  1.00 29.75 ? 716 HOH B O   1 
HETATM 8717 O O   . HOH L 4 .   ? -28.693 26.008 41.424  1.00 33.39 ? 717 HOH B O   1 
HETATM 8718 O O   . HOH L 4 .   ? -10.787 32.162 6.577   1.00 41.55 ? 718 HOH B O   1 
HETATM 8719 O O   . HOH L 4 .   ? -36.471 42.581 44.661  1.00 21.02 ? 719 HOH B O   1 
HETATM 8720 O O   . HOH L 4 .   ? -3.778  52.146 2.129   1.00 48.26 ? 720 HOH B O   1 
HETATM 8721 O O   . HOH L 4 .   ? -19.354 19.807 13.429  1.00 42.06 ? 721 HOH B O   1 
HETATM 8722 O O   . HOH L 4 .   ? -29.101 39.733 5.881   1.00 34.81 ? 722 HOH B O   1 
HETATM 8723 O O   . HOH L 4 .   ? -45.545 47.665 26.675  1.00 35.76 ? 723 HOH B O   1 
HETATM 8724 O O   . HOH L 4 .   ? -34.877 16.860 36.889  1.00 39.86 ? 724 HOH B O   1 
HETATM 8725 O O   . HOH L 4 .   ? -17.005 36.061 49.143  1.00 31.46 ? 725 HOH B O   1 
HETATM 8726 O O   . HOH L 4 .   ? -60.800 42.994 16.521  1.00 36.20 ? 726 HOH B O   1 
HETATM 8727 O O   . HOH L 4 .   ? -18.136 36.115 25.872  1.00 17.96 ? 727 HOH B O   1 
HETATM 8728 O O   . HOH L 4 .   ? -58.188 34.208 38.665  1.00 40.73 ? 728 HOH B O   1 
HETATM 8729 O O   . HOH L 4 .   ? -26.454 26.867 49.686  1.00 44.10 ? 729 HOH B O   1 
HETATM 8730 O O   . HOH L 4 .   ? -24.564 27.500 46.114  1.00 25.58 ? 730 HOH B O   1 
HETATM 8731 O O   . HOH L 4 .   ? -17.781 32.743 42.485  1.00 30.53 ? 731 HOH B O   1 
HETATM 8732 O O   . HOH L 4 .   ? -28.464 50.331 27.559  1.00 30.26 ? 732 HOH B O   1 
HETATM 8733 O O   . HOH L 4 .   ? -15.848 54.838 15.908  1.00 40.19 ? 733 HOH B O   1 
HETATM 8734 O O   . HOH L 4 .   ? -52.108 23.928 18.782  1.00 30.16 ? 734 HOH B O   1 
HETATM 8735 O O   . HOH L 4 .   ? -43.383 48.949 44.687  1.00 37.90 ? 735 HOH B O   1 
HETATM 8736 O O   . HOH L 4 .   ? -12.099 45.954 22.154  1.00 26.58 ? 736 HOH B O   1 
HETATM 8737 O O   . HOH L 4 .   ? -49.645 36.714 53.298  1.00 32.75 ? 737 HOH B O   1 
HETATM 8738 O O   . HOH L 4 .   ? -8.587  55.443 0.114   1.00 47.03 ? 738 HOH B O   1 
HETATM 8739 O O   . HOH L 4 .   ? -44.893 23.317 40.420  1.00 35.46 ? 739 HOH B O   1 
HETATM 8740 O O   . HOH L 4 .   ? -23.638 54.020 17.130  1.00 29.19 ? 740 HOH B O   1 
HETATM 8741 O O   . HOH L 4 .   ? -4.424  46.186 6.218   1.00 32.31 ? 741 HOH B O   1 
HETATM 8742 O O   . HOH L 4 .   ? -58.895 40.306 13.221  1.00 44.01 ? 742 HOH B O   1 
HETATM 8743 O O   . HOH L 4 .   ? -27.738 23.770 39.985  1.00 45.77 ? 743 HOH B O   1 
HETATM 8744 O O   . HOH L 4 .   ? -11.062 47.378 36.523  1.00 43.28 ? 744 HOH B O   1 
HETATM 8745 O O   . HOH L 4 .   ? -27.170 52.218 16.900  1.00 42.22 ? 745 HOH B O   1 
HETATM 8746 O O   . HOH L 4 .   ? -53.810 46.108 11.561  1.00 44.12 ? 746 HOH B O   1 
HETATM 8747 O O   . HOH L 4 .   ? -5.407  37.743 -1.569  1.00 49.60 ? 747 HOH B O   1 
HETATM 8748 O O   . HOH L 4 .   ? -7.749  54.269 19.004  1.00 37.30 ? 748 HOH B O   1 
HETATM 8749 O O   . HOH L 4 .   ? -6.946  47.489 -3.129  1.00 37.68 ? 749 HOH B O   1 
HETATM 8750 O O   . HOH L 4 .   ? -3.312  39.950 4.300   1.00 33.40 ? 750 HOH B O   1 
HETATM 8751 O O   . HOH L 4 .   ? -46.488 37.086 5.718   1.00 30.46 ? 751 HOH B O   1 
HETATM 8752 O O   . HOH L 4 .   ? -50.831 34.270 7.501   1.00 33.82 ? 752 HOH B O   1 
HETATM 8753 O O   . HOH L 4 .   ? -51.931 25.804 28.126  1.00 39.02 ? 753 HOH B O   1 
HETATM 8754 O O   . HOH L 4 .   ? -9.594  45.142 33.870  1.00 50.15 ? 754 HOH B O   1 
HETATM 8755 O O   . HOH L 4 .   ? -17.273 50.195 32.623  1.00 21.41 ? 755 HOH B O   1 
HETATM 8756 O O   . HOH L 4 .   ? -59.638 33.922 25.476  1.00 45.75 ? 756 HOH B O   1 
HETATM 8757 O O   . HOH L 4 .   ? -60.830 50.614 14.688  1.00 45.99 ? 757 HOH B O   1 
HETATM 8758 O O   . HOH L 4 .   ? -7.256  52.357 15.820  1.00 25.66 ? 758 HOH B O   1 
HETATM 8759 O O   . HOH L 4 .   ? -29.487 25.971 38.355  1.00 23.14 ? 759 HOH B O   1 
HETATM 8760 O O   . HOH L 4 .   ? -20.448 31.767 8.530   1.00 45.00 ? 760 HOH B O   1 
HETATM 8761 O O   . HOH L 4 .   ? -12.650 48.777 38.097  1.00 37.96 ? 761 HOH B O   1 
HETATM 8762 O O   . HOH L 4 .   ? -14.112 28.173 30.964  1.00 47.67 ? 762 HOH B O   1 
HETATM 8763 O O   . HOH L 4 .   ? -9.605  33.903 35.283  1.00 57.03 ? 763 HOH B O   1 
HETATM 8764 O O   . HOH L 4 .   ? -2.516  53.401 8.386   1.00 53.72 ? 764 HOH B O   1 
HETATM 8765 O O   . HOH L 4 .   ? -59.499 38.885 20.288  1.00 42.70 ? 765 HOH B O   1 
HETATM 8766 O O   . HOH L 4 .   ? -46.772 41.458 54.145  1.00 49.43 ? 766 HOH B O   1 
HETATM 8767 O O   . HOH L 4 .   ? -34.252 16.331 26.517  1.00 43.30 ? 767 HOH B O   1 
HETATM 8768 O O   . HOH L 4 .   ? -52.233 26.135 20.337  1.00 25.26 ? 768 HOH B O   1 
HETATM 8769 O O   . HOH L 4 .   ? -34.891 50.854 44.832  1.00 37.13 ? 769 HOH B O   1 
HETATM 8770 O O   . HOH L 4 .   ? -48.657 20.207 43.321  1.00 40.68 ? 770 HOH B O   1 
HETATM 8771 O O   . HOH L 4 .   ? -49.642 44.850 35.138  1.00 21.83 ? 771 HOH B O   1 
HETATM 8772 O O   . HOH L 4 .   ? -14.461 52.281 25.580  1.00 40.73 ? 772 HOH B O   1 
HETATM 8773 O O   . HOH L 4 .   ? -20.459 28.080 12.463  1.00 33.28 ? 773 HOH B O   1 
HETATM 8774 O O   . HOH L 4 .   ? -36.530 53.029 36.863  1.00 38.47 ? 774 HOH B O   1 
HETATM 8775 O O   . HOH L 4 .   ? -47.380 52.381 27.948  1.00 41.81 ? 775 HOH B O   1 
HETATM 8776 O O   . HOH L 4 .   ? -41.841 44.100 58.831  1.00 32.64 ? 776 HOH B O   1 
HETATM 8777 O O   . HOH L 4 .   ? -41.223 50.444 31.490  1.00 35.51 ? 777 HOH B O   1 
HETATM 8778 O O   . HOH L 4 .   ? -9.906  59.843 6.704   1.00 42.14 ? 778 HOH B O   1 
HETATM 8779 O O   . HOH L 4 .   ? -32.649 52.686 47.679  1.00 30.36 ? 779 HOH B O   1 
HETATM 8780 O O   . HOH L 4 .   ? -53.531 44.092 47.603  1.00 44.56 ? 780 HOH B O   1 
HETATM 8781 O O   . HOH L 4 .   ? -57.966 38.151 12.859  1.00 47.77 ? 781 HOH B O   1 
HETATM 8782 O O   . HOH L 4 .   ? -28.701 23.657 16.977  1.00 41.47 ? 782 HOH B O   1 
HETATM 8783 O O   . HOH L 4 .   ? -32.320 44.904 30.123  1.00 30.27 ? 783 HOH B O   1 
HETATM 8784 O O   . HOH L 4 .   ? -26.400 51.748 31.355  1.00 19.64 ? 784 HOH B O   1 
HETATM 8785 O O   . HOH L 4 .   ? -53.718 39.197 46.980  1.00 30.39 ? 785 HOH B O   1 
HETATM 8786 O O   . HOH L 4 .   ? -16.574 44.709 -4.272  1.00 47.28 ? 786 HOH B O   1 
HETATM 8787 O O   . HOH L 4 .   ? -15.613 26.474 29.527  1.00 34.18 ? 787 HOH B O   1 
HETATM 8788 O O   . HOH L 4 .   ? -32.241 29.156 54.942  1.00 39.97 ? 788 HOH B O   1 
HETATM 8789 O O   . HOH L 4 .   ? -40.270 42.526 12.733  1.00 28.93 ? 789 HOH B O   1 
HETATM 8790 O O   . HOH L 4 .   ? -26.019 50.857 28.835  1.00 19.14 ? 790 HOH B O   1 
HETATM 8791 O O   . HOH L 4 .   ? -29.137 57.452 45.823  1.00 46.92 ? 791 HOH B O   1 
HETATM 8792 O O   . HOH L 4 .   ? -4.580  53.581 4.746   1.00 51.87 ? 792 HOH B O   1 
HETATM 8793 O O   . HOH L 4 .   ? -31.942 24.379 38.588  1.00 44.25 ? 793 HOH B O   1 
HETATM 8794 O O   . HOH L 4 .   ? -47.405 20.317 25.535  1.00 47.93 ? 794 HOH B O   1 
HETATM 8795 O O   . HOH L 4 .   ? -16.997 31.703 9.917   1.00 42.93 ? 795 HOH B O   1 
HETATM 8796 O O   . HOH L 4 .   ? -55.832 25.862 17.699  1.00 44.25 ? 796 HOH B O   1 
HETATM 8797 O O   . HOH L 4 .   ? -46.174 43.479 55.235  1.00 36.50 ? 797 HOH B O   1 
HETATM 8798 O O   . HOH L 4 .   ? -17.945 22.060 32.224  1.00 42.55 ? 798 HOH B O   1 
HETATM 8799 O O   . HOH L 4 .   ? -21.218 21.515 25.082  1.00 37.75 ? 799 HOH B O   1 
HETATM 8800 O O   . HOH L 4 .   ? -37.237 33.154 17.629  1.00 18.29 ? 800 HOH B O   1 
HETATM 8801 O O   . HOH L 4 .   ? -16.969 53.594 0.484   1.00 55.17 ? 801 HOH B O   1 
HETATM 8802 O O   . HOH L 4 .   ? -7.493  31.258 4.230   1.00 51.39 ? 802 HOH B O   1 
HETATM 8803 O O   . HOH L 4 .   ? -55.275 35.436 33.719  1.00 20.84 ? 803 HOH B O   1 
HETATM 8804 O O   . HOH L 4 .   ? -16.210 54.448 33.704  1.00 38.47 ? 804 HOH B O   1 
HETATM 8805 O O   . HOH L 4 .   ? -42.331 20.203 13.916  1.00 44.70 ? 805 HOH B O   1 
HETATM 8806 O O   . HOH L 4 .   ? -43.073 36.450 56.845  1.00 30.97 ? 806 HOH B O   1 
HETATM 8807 O O   . HOH L 4 .   ? -42.265 49.638 19.162  1.00 37.36 ? 807 HOH B O   1 
HETATM 8808 O O   . HOH L 4 .   ? -47.396 19.966 27.399  1.00 50.78 ? 808 HOH B O   1 
HETATM 8809 O O   . HOH L 4 .   ? -11.866 27.639 16.727  1.00 41.46 ? 809 HOH B O   1 
HETATM 8810 O O   . HOH L 4 .   ? -56.805 40.489 37.315  1.00 41.41 ? 810 HOH B O   1 
HETATM 8811 O O   . HOH L 4 .   ? -14.773 22.165 15.336  1.00 56.71 ? 811 HOH B O   1 
HETATM 8812 O O   . HOH L 4 .   ? -27.238 56.225 46.630  1.00 35.87 ? 812 HOH B O   1 
HETATM 8813 O O   . HOH L 4 .   ? -43.861 52.586 34.143  1.00 43.58 ? 813 HOH B O   1 
HETATM 8814 O O   . HOH L 4 .   ? -3.631  51.511 4.667   1.00 48.30 ? 814 HOH B O   1 
HETATM 8815 O O   . HOH L 4 .   ? -53.013 48.165 43.310  1.00 49.71 ? 815 HOH B O   1 
HETATM 8816 O O   . HOH L 4 .   ? -47.737 23.519 17.233  1.00 42.32 ? 816 HOH B O   1 
HETATM 8817 O O   . HOH L 4 .   ? -45.574 18.568 36.536  1.00 46.93 ? 817 HOH B O   1 
HETATM 8818 O O   . HOH L 4 .   ? -38.306 36.119 58.802  1.00 57.65 ? 818 HOH B O   1 
HETATM 8819 O O   . HOH L 4 .   ? -60.322 27.995 14.350  1.00 50.77 ? 819 HOH B O   1 
HETATM 8820 O O   . HOH L 4 .   ? -36.682 32.118 0.804   1.00 42.76 ? 820 HOH B O   1 
HETATM 8821 O O   . HOH L 4 .   ? -30.305 46.523 29.167  1.00 30.08 ? 821 HOH B O   1 
HETATM 8822 O O   . HOH L 4 .   ? -27.226 31.012 51.582  1.00 55.32 ? 822 HOH B O   1 
HETATM 8823 O O   . HOH L 4 .   ? -43.376 17.566 23.895  1.00 54.70 ? 823 HOH B O   1 
HETATM 8824 O O   . HOH L 4 .   ? -5.592  29.576 10.797  1.00 49.44 ? 824 HOH B O   1 
HETATM 8825 O O   . HOH L 4 .   ? -57.853 35.237 36.067  1.00 44.34 ? 825 HOH B O   1 
HETATM 8826 O O   . HOH L 4 .   ? -59.080 33.496 22.005  1.00 37.92 ? 826 HOH B O   1 
HETATM 8827 O O   . HOH L 4 .   ? -50.022 19.612 26.668  1.00 48.25 ? 827 HOH B O   1 
HETATM 8828 O O   . HOH L 4 .   ? -55.694 35.600 31.503  1.00 38.73 ? 828 HOH B O   1 
HETATM 8829 O O   . HOH L 4 .   ? -54.491 46.774 51.772  1.00 46.85 ? 829 HOH B O   1 
HETATM 8830 O O   . HOH L 4 .   ? -33.625 53.810 37.466  1.00 39.87 ? 830 HOH B O   1 
HETATM 8831 O O   . HOH L 4 .   ? -14.636 49.640 -2.069  1.00 52.07 ? 831 HOH B O   1 
HETATM 8832 O O   . HOH L 4 .   ? -33.120 52.729 45.141  1.00 36.32 ? 832 HOH B O   1 
HETATM 8833 O O   . HOH L 4 .   ? -47.871 31.723 54.297  1.00 48.91 ? 833 HOH B O   1 
HETATM 8834 O O   . HOH L 4 .   ? -28.256 47.001 22.363  1.00 43.20 ? 834 HOH B O   1 
HETATM 8835 O O   . HOH L 4 .   ? -50.885 50.550 31.856  1.00 44.78 ? 835 HOH B O   1 
HETATM 8836 O O   . HOH L 4 .   ? -8.122  29.485 10.041  1.00 45.37 ? 836 HOH B O   1 
HETATM 8837 O O   . HOH L 4 .   ? -17.305 57.774 20.599  1.00 42.24 ? 837 HOH B O   1 
HETATM 8838 O O   . HOH L 4 .   ? -2.129  42.542 4.162   1.00 40.07 ? 838 HOH B O   1 
HETATM 8839 O O   . HOH L 4 .   ? -58.303 34.252 43.372  1.00 43.84 ? 839 HOH B O   1 
HETATM 8840 O O   . HOH L 4 .   ? -35.026 19.641 23.241  1.00 44.68 ? 840 HOH B O   1 
HETATM 8841 O O   . HOH L 4 .   ? -34.963 20.709 21.509  1.00 49.91 ? 841 HOH B O   1 
HETATM 8842 O O   . HOH L 4 .   ? -17.409 55.369 4.312   1.00 57.61 ? 842 HOH B O   1 
HETATM 8843 O O   . HOH L 4 .   ? -46.005 35.411 5.195   1.00 43.67 ? 843 HOH B O   1 
HETATM 8844 O O   . HOH L 4 .   ? -15.456 51.147 -1.333  1.00 50.61 ? 844 HOH B O   1 
HETATM 8845 O O   . HOH L 4 .   ? -23.218 42.425 58.939  1.00 34.48 ? 845 HOH B O   1 
HETATM 8846 O O   . HOH L 4 .   ? -30.763 23.614 41.484  1.00 51.07 ? 846 HOH B O   1 
HETATM 8847 O O   . HOH L 4 .   ? -57.299 36.667 34.934  1.00 46.96 ? 847 HOH B O   1 
HETATM 8848 O O   . HOH L 4 .   ? -47.161 23.539 46.105  1.00 49.95 ? 848 HOH B O   1 
HETATM 8849 O O   . HOH L 4 .   ? -33.369 55.890 36.581  1.00 55.28 ? 849 HOH B O   1 
HETATM 8850 O O   . HOH L 4 .   ? -38.338 31.189 0.322   1.00 43.89 ? 850 HOH B O   1 
HETATM 8851 O O   . HOH L 4 .   ? -12.006 50.295 22.394  1.00 40.65 ? 851 HOH B O   1 
HETATM 8852 O O   . HOH L 4 .   ? -18.134 52.737 33.249  1.00 26.11 ? 852 HOH B O   1 
HETATM 8853 O O   . HOH L 4 .   ? -50.694 51.792 21.231  1.00 56.34 ? 853 HOH B O   1 
HETATM 8854 O O   . HOH L 4 .   ? -41.003 51.197 17.959  1.00 43.46 ? 854 HOH B O   1 
HETATM 8855 O O   . HOH L 4 .   ? -11.649 46.945 40.527  1.00 53.37 ? 855 HOH B O   1 
HETATM 8856 O O   . HOH L 4 .   ? -8.477  32.383 36.121  1.00 55.44 ? 856 HOH B O   1 
HETATM 8857 O O   . HOH L 4 .   ? -5.687  46.158 25.254  1.00 44.59 ? 857 HOH B O   1 
HETATM 8858 O O   . HOH L 4 .   ? -10.917 44.430 40.449  1.00 56.60 ? 858 HOH B O   1 
HETATM 8859 O O   . HOH L 4 .   ? -22.560 34.738 2.797   1.00 38.83 ? 859 HOH B O   1 
HETATM 8860 O O   . HOH L 4 .   ? -30.940 46.360 22.730  1.00 50.88 ? 860 HOH B O   1 
HETATM 8861 O O   . HOH L 4 .   ? -9.789  45.231 50.449  1.00 46.59 ? 861 HOH B O   1 
HETATM 8862 O O   . HOH L 4 .   ? -29.319 39.180 3.311   1.00 44.24 ? 862 HOH B O   1 
HETATM 8863 O O   . HOH L 4 .   ? -24.973 54.163 19.519  1.00 60.69 ? 863 HOH B O   1 
HETATM 8864 O O   . HOH L 4 .   ? -6.574  52.082 18.408  1.00 40.97 ? 864 HOH B O   1 
HETATM 8865 O O   . HOH L 4 .   ? -28.382 25.660 47.738  1.00 46.02 ? 865 HOH B O   1 
HETATM 8866 O O   . HOH L 4 .   ? -13.523 53.895 33.773  1.00 50.60 ? 866 HOH B O   1 
HETATM 8867 O O   . HOH L 4 .   ? -13.858 46.848 24.468  1.00 40.98 ? 867 HOH B O   1 
HETATM 8868 O O   . HOH L 4 .   ? -33.167 56.116 38.470  1.00 55.29 ? 868 HOH B O   1 
HETATM 8869 O O   . HOH L 4 .   ? -42.335 52.907 36.786  1.00 43.91 ? 869 HOH B O   1 
HETATM 8870 O O   . HOH L 4 .   ? -44.366 19.424 23.876  1.00 52.59 ? 870 HOH B O   1 
HETATM 8871 O O   . HOH L 4 .   ? -58.401 24.304 19.380  1.00 42.91 ? 871 HOH B O   1 
HETATM 8872 O O   . HOH L 4 .   ? -11.504 51.527 37.561  1.00 50.52 ? 872 HOH B O   1 
HETATM 8873 O O   . HOH L 4 .   ? -12.133 53.004 35.256  1.00 49.88 ? 873 HOH B O   1 
HETATM 8874 O O   . HOH L 4 .   ? -33.030 45.779 21.968  1.00 52.01 ? 874 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   ? 0.3461 0.4605 0.2417 -0.0187 0.0295  -0.0001 2   LYS A N   
2    C CA  . LYS A 2   ? 0.3591 0.4606 0.2635 -0.0210 0.0324  0.0004  2   LYS A CA  
3    C C   . LYS A 2   ? 0.3205 0.4128 0.2320 -0.0203 0.0293  0.0029  2   LYS A C   
4    O O   . LYS A 2   ? 0.3583 0.4484 0.2666 -0.0176 0.0284  0.0108  2   LYS A O   
5    C CB  . LYS A 2   ? 0.3928 0.4904 0.2933 -0.0214 0.0382  0.0083  2   LYS A CB  
6    C CG  . LYS A 2   ? 0.4361 0.5229 0.3456 -0.0244 0.0413  0.0083  2   LYS A CG  
7    C CD  . LYS A 2   ? 0.5690 0.6465 0.4766 -0.0241 0.0444  0.0186  2   LYS A CD  
8    C CE  . LYS A 2   ? 0.5591 0.6396 0.4577 -0.0245 0.0499  0.0249  2   LYS A CE  
9    N NZ  . LYS A 2   ? 0.4287 0.4976 0.3252 -0.0246 0.0537  0.0350  2   LYS A NZ  
10   N N   . LYS A 3   ? 0.2021 0.2889 0.1228 -0.0224 0.0277  -0.0037 3   LYS A N   
11   C CA  . LYS A 3   ? 0.2267 0.3056 0.1542 -0.0220 0.0248  -0.0023 3   LYS A CA  
12   C C   . LYS A 3   ? 0.1861 0.2537 0.1204 -0.0235 0.0278  0.0005  3   LYS A C   
13   O O   . LYS A 3   ? 0.2228 0.2892 0.1587 -0.0255 0.0316  -0.0011 3   LYS A O   
14   C CB  . LYS A 3   ? 0.2323 0.3126 0.1654 -0.0234 0.0209  -0.0111 3   LYS A CB  
15   C CG  . LYS A 3   ? 0.2904 0.3829 0.2178 -0.0232 0.0180  -0.0162 3   LYS A CG  
16   C CD  . LYS A 3   ? 0.4311 0.5290 0.3559 -0.0209 0.0140  -0.0120 3   LYS A CD  
17   C CE  . LYS A 3   ? 0.5291 0.6383 0.4524 -0.0224 0.0102  -0.0201 3   LYS A CE  
18   N NZ  . LYS A 3   ? 0.6416 0.7443 0.5729 -0.0261 0.0094  -0.0289 3   LYS A NZ  
19   N N   . LEU A 4   ? 0.1943 0.2547 0.1325 -0.0225 0.0260  0.0044  4   LEU A N   
20   C CA  . LEU A 4   ? 0.1786 0.2290 0.1246 -0.0242 0.0275  0.0049  4   LEU A CA  
21   C C   . LEU A 4   ? 0.1660 0.2148 0.1196 -0.0247 0.0238  -0.0013 4   LEU A C   
22   O O   . LEU A 4   ? 0.2035 0.2545 0.1569 -0.0233 0.0200  -0.0017 4   LEU A O   
23   C CB  . LEU A 4   ? 0.1778 0.2202 0.1229 -0.0228 0.0286  0.0131  4   LEU A CB  
24   C CG  . LEU A 4   ? 0.1713 0.2040 0.1243 -0.0249 0.0300  0.0130  4   LEU A CG  
25   C CD1 . LEU A 4   ? 0.1984 0.2231 0.1483 -0.0252 0.0341  0.0206  4   LEU A CD1 
26   C CD2 . LEU A 4   ? 0.1943 0.2240 0.1531 -0.0237 0.0258  0.0113  4   LEU A CD2 
27   N N   . PHE A 5   ? 0.1838 0.2294 0.1437 -0.0266 0.0252  -0.0059 5   PHE A N   
28   C CA  . PHE A 5   ? 0.1908 0.2336 0.1574 -0.0268 0.0224  -0.0112 5   PHE A CA  
29   C C   . PHE A 5   ? 0.1785 0.2134 0.1510 -0.0270 0.0221  -0.0080 5   PHE A C   
30   O O   . PHE A 5   ? 0.2380 0.2696 0.2130 -0.0281 0.0251  -0.0061 5   PHE A O   
31   C CB  . PHE A 5   ? 0.1903 0.2343 0.1598 -0.0276 0.0240  -0.0179 5   PHE A CB  
32   C CG  . PHE A 5   ? 0.1857 0.2372 0.1495 -0.0276 0.0244  -0.0224 5   PHE A CG  
33   C CD1 . PHE A 5   ? 0.2107 0.2663 0.1711 -0.0275 0.0212  -0.0250 5   PHE A CD1 
34   C CD2 . PHE A 5   ? 0.2082 0.2637 0.1703 -0.0278 0.0279  -0.0246 5   PHE A CD2 
35   C CE1 . PHE A 5   ? 0.2035 0.2666 0.1581 -0.0278 0.0216  -0.0299 5   PHE A CE1 
36   C CE2 . PHE A 5   ? 0.2485 0.3110 0.2049 -0.0276 0.0285  -0.0292 5   PHE A CE2 
37   C CZ  . PHE A 5   ? 0.2176 0.2838 0.1702 -0.0278 0.0253  -0.0320 5   PHE A CZ  
38   N N   . LEU A 6   ? 0.1436 0.1763 0.1185 -0.0261 0.0188  -0.0077 6   LEU A N   
39   C CA  . LEU A 6   ? 0.1453 0.1713 0.1251 -0.0259 0.0183  -0.0046 6   LEU A CA  
40   C C   . LEU A 6   ? 0.1693 0.1929 0.1554 -0.0263 0.0162  -0.0092 6   LEU A C   
41   O O   . LEU A 6   ? 0.1666 0.1928 0.1526 -0.0264 0.0138  -0.0127 6   LEU A O   
42   C CB  . LEU A 6   ? 0.1529 0.1788 0.1295 -0.0238 0.0164  0.0007  6   LEU A CB  
43   C CG  . LEU A 6   ? 0.1513 0.1702 0.1321 -0.0231 0.0161  0.0040  6   LEU A CG  
44   C CD1 . LEU A 6   ? 0.1767 0.1894 0.1586 -0.0247 0.0200  0.0064  6   LEU A CD1 
45   C CD2 . LEU A 6   ? 0.1478 0.1679 0.1248 -0.0200 0.0144  0.0090  6   LEU A CD2 
46   N N   . VAL A 7   ? 0.1272 0.1462 0.1188 -0.0268 0.0173  -0.0092 7   VAL A N   
47   C CA  . VAL A 7   ? 0.1221 0.1386 0.1192 -0.0267 0.0160  -0.0130 7   VAL A CA  
48   C C   . VAL A 7   ? 0.1331 0.1450 0.1345 -0.0265 0.0152  -0.0101 7   VAL A C   
49   O O   . VAL A 7   ? 0.1638 0.1741 0.1673 -0.0270 0.0172  -0.0087 7   VAL A O   
50   C CB  . VAL A 7   ? 0.1566 0.1740 0.1562 -0.0266 0.0181  -0.0168 7   VAL A CB  
51   C CG1 . VAL A 7   ? 0.1609 0.1749 0.1648 -0.0256 0.0169  -0.0201 7   VAL A CG1 
52   C CG2 . VAL A 7   ? 0.1526 0.1748 0.1474 -0.0267 0.0195  -0.0197 7   VAL A CG2 
53   N N   . PHE A 8   ? 0.1231 0.1338 0.1257 -0.0259 0.0126  -0.0097 8   PHE A N   
54   C CA  . PHE A 8   ? 0.1472 0.1540 0.1539 -0.0255 0.0118  -0.0078 8   PHE A CA  
55   C C   . PHE A 8   ? 0.1246 0.1296 0.1360 -0.0254 0.0116  -0.0109 8   PHE A C   
56   O O   . PHE A 8   ? 0.1638 0.1688 0.1753 -0.0255 0.0108  -0.0140 8   PHE A O   
57   C CB  . PHE A 8   ? 0.1231 0.1305 0.1293 -0.0248 0.0093  -0.0058 8   PHE A CB  
58   C CG  . PHE A 8   ? 0.1502 0.1586 0.1520 -0.0235 0.0096  -0.0014 8   PHE A CG  
59   C CD1 . PHE A 8   ? 0.1608 0.1648 0.1631 -0.0225 0.0108  0.0024  8   PHE A CD1 
60   C CD2 . PHE A 8   ? 0.1697 0.1835 0.1666 -0.0229 0.0089  -0.0011 8   PHE A CD2 
61   C CE1 . PHE A 8   ? 0.1807 0.1839 0.1784 -0.0206 0.0117  0.0070  8   PHE A CE1 
62   C CE2 . PHE A 8   ? 0.1630 0.1777 0.1551 -0.0208 0.0093  0.0038  8   PHE A CE2 
63   C CZ  . PHE A 8   ? 0.1650 0.1736 0.1575 -0.0194 0.0109  0.0081  8   PHE A CZ  
64   N N   . TRP A 9   ? 0.1035 0.1067 0.1184 -0.0252 0.0124  -0.0099 9   TRP A N   
65   C CA  . TRP A 9   ? 0.1141 0.1161 0.1330 -0.0241 0.0121  -0.0118 9   TRP A CA  
66   C C   . TRP A 9   ? 0.1233 0.1237 0.1451 -0.0239 0.0113  -0.0096 9   TRP A C   
67   O O   . TRP A 9   ? 0.1102 0.1113 0.1330 -0.0245 0.0125  -0.0087 9   TRP A O   
68   C CB  . TRP A 9   ? 0.1048 0.1093 0.1251 -0.0234 0.0140  -0.0139 9   TRP A CB  
69   C CG  . TRP A 9   ? 0.1411 0.1447 0.1644 -0.0211 0.0140  -0.0159 9   TRP A CG  
70   C CD1 . TRP A 9   ? 0.1758 0.1755 0.2007 -0.0200 0.0128  -0.0155 9   TRP A CD1 
71   C CD2 . TRP A 9   ? 0.1377 0.1443 0.1625 -0.0191 0.0157  -0.0180 9   TRP A CD2 
72   N NE1 . TRP A 9   ? 0.1398 0.1388 0.1665 -0.0171 0.0137  -0.0169 9   TRP A NE1 
73   C CE2 . TRP A 9   ? 0.1631 0.1667 0.1899 -0.0161 0.0154  -0.0185 9   TRP A CE2 
74   C CE3 . TRP A 9   ? 0.1692 0.1812 0.1937 -0.0193 0.0177  -0.0193 9   TRP A CE3 
75   C CZ2 . TRP A 9   ? 0.1241 0.1300 0.1527 -0.0125 0.0168  -0.0201 9   TRP A CZ2 
76   C CZ3 . TRP A 9   ? 0.1130 0.1284 0.1397 -0.0162 0.0191  -0.0214 9   TRP A CZ3 
77   C CH2 . TRP A 9   ? 0.1241 0.1364 0.1528 -0.0124 0.0185  -0.0217 9   TRP A CH2 
78   N N   . TRP A 10  ? 0.1123 0.1109 0.1351 -0.0236 0.0096  -0.0091 10  TRP A N   
79   C CA  . TRP A 10  ? 0.0925 0.0900 0.1175 -0.0232 0.0088  -0.0072 10  TRP A CA  
80   C C   . TRP A 10  ? 0.0923 0.0895 0.1205 -0.0219 0.0088  -0.0080 10  TRP A C   
81   O O   . TRP A 10  ? 0.1436 0.1391 0.1722 -0.0213 0.0085  -0.0089 10  TRP A O   
82   C CB  . TRP A 10  ? 0.0926 0.0899 0.1170 -0.0234 0.0070  -0.0060 10  TRP A CB  
83   C CG  . TRP A 10  ? 0.1198 0.1188 0.1407 -0.0236 0.0066  -0.0046 10  TRP A CG  
84   C CD1 . TRP A 10  ? 0.1334 0.1353 0.1522 -0.0242 0.0055  -0.0057 10  TRP A CD1 
85   C CD2 . TRP A 10  ? 0.1321 0.1303 0.1512 -0.0228 0.0074  -0.0018 10  TRP A CD2 
86   N NE1 . TRP A 10  ? 0.1559 0.1600 0.1713 -0.0233 0.0052  -0.0032 10  TRP A NE1 
87   C CE2 . TRP A 10  ? 0.1337 0.1346 0.1492 -0.0222 0.0066  -0.0004 10  TRP A CE2 
88   C CE3 . TRP A 10  ? 0.1505 0.1457 0.1704 -0.0226 0.0089  -0.0004 10  TRP A CE3 
89   C CZ2 . TRP A 10  ? 0.1144 0.1142 0.1267 -0.0206 0.0074  0.0031  10  TRP A CZ2 
90   C CZ3 . TRP A 10  ? 0.1535 0.1463 0.1704 -0.0218 0.0101  0.0025  10  TRP A CZ3 
91   C CH2 . TRP A 10  ? 0.1606 0.1552 0.1735 -0.0204 0.0094  0.0047  10  TRP A CH2 
92   N N   . HIS A 11  ? 0.0972 0.0961 0.1273 -0.0216 0.0093  -0.0075 11  HIS A N   
93   C CA  . HIS A 11  ? 0.1131 0.1139 0.1459 -0.0198 0.0093  -0.0080 11  HIS A CA  
94   C C   . HIS A 11  ? 0.1057 0.1058 0.1397 -0.0192 0.0083  -0.0064 11  HIS A C   
95   O O   . HIS A 11  ? 0.1159 0.1164 0.1499 -0.0203 0.0081  -0.0058 11  HIS A O   
96   C CB  . HIS A 11  ? 0.1157 0.1214 0.1499 -0.0200 0.0105  -0.0093 11  HIS A CB  
97   C CG  . HIS A 11  ? 0.1129 0.1230 0.1499 -0.0180 0.0101  -0.0095 11  HIS A CG  
98   N ND1 . HIS A 11  ? 0.0879 0.0986 0.1256 -0.0146 0.0098  -0.0091 11  HIS A ND1 
99   C CD2 . HIS A 11  ? 0.1272 0.1415 0.1659 -0.0189 0.0100  -0.0100 11  HIS A CD2 
100  C CE1 . HIS A 11  ? 0.1373 0.1533 0.1769 -0.0129 0.0093  -0.0088 11  HIS A CE1 
101  N NE2 . HIS A 11  ? 0.1269 0.1457 0.1672 -0.0157 0.0093  -0.0098 11  HIS A NE2 
102  N N   . MET A 12  ? 0.1172 0.1157 0.1518 -0.0176 0.0079  -0.0057 12  MET A N   
103  C CA  . MET A 12  ? 0.1019 0.1001 0.1373 -0.0172 0.0072  -0.0040 12  MET A CA  
104  C C   . MET A 12  ? 0.1107 0.1114 0.1473 -0.0144 0.0074  -0.0032 12  MET A C   
105  O O   . MET A 12  ? 0.1164 0.1158 0.1528 -0.0121 0.0081  -0.0031 12  MET A O   
106  C CB  . MET A 12  ? 0.0866 0.0807 0.1214 -0.0181 0.0069  -0.0033 12  MET A CB  
107  C CG  . MET A 12  ? 0.1107 0.1040 0.1441 -0.0204 0.0065  -0.0043 12  MET A CG  
108  S SD  . MET A 12  ? 0.1272 0.1231 0.1602 -0.0210 0.0057  -0.0032 12  MET A SD  
109  C CE  . MET A 12  ? 0.1654 0.1621 0.1967 -0.0227 0.0047  -0.0037 12  MET A CE  
110  N N   . HIS A 13  ? 0.0891 0.0936 0.1266 -0.0141 0.0069  -0.0027 13  HIS A N   
111  C CA  . HIS A 13  ? 0.0836 0.0928 0.1218 -0.0111 0.0069  -0.0020 13  HIS A CA  
112  C C   . HIS A 13  ? 0.0814 0.0940 0.1199 -0.0112 0.0063  -0.0012 13  HIS A C   
113  O O   . HIS A 13  ? 0.0952 0.1080 0.1339 -0.0135 0.0061  -0.0025 13  HIS A O   
114  C CB  . HIS A 13  ? 0.0819 0.0976 0.1214 -0.0105 0.0071  -0.0043 13  HIS A CB  
115  C CG  . HIS A 13  ? 0.1002 0.1240 0.1408 -0.0077 0.0066  -0.0040 13  HIS A CG  
116  N ND1 . HIS A 13  ? 0.0850 0.1091 0.1248 -0.0032 0.0066  -0.0013 13  HIS A ND1 
117  C CD2 . HIS A 13  ? 0.1179 0.1503 0.1599 -0.0087 0.0061  -0.0062 13  HIS A CD2 
118  C CE1 . HIS A 13  ? 0.0846 0.1183 0.1252 -0.0009 0.0059  -0.0014 13  HIS A CE1 
119  N NE2 . HIS A 13  ? 0.0986 0.1380 0.1407 -0.0045 0.0054  -0.0049 13  HIS A NE2 
120  N N   . GLN A 14  ? 0.0829 0.0976 0.1209 -0.0082 0.0062  0.0010  14  GLN A N   
121  C CA  . GLN A 14  ? 0.0818 0.1025 0.1198 -0.0076 0.0057  0.0013  14  GLN A CA  
122  C C   . GLN A 14  ? 0.1364 0.1633 0.1740 -0.0033 0.0055  0.0028  14  GLN A C   
123  O O   . GLN A 14  ? 0.0978 0.1209 0.1343 -0.0002 0.0062  0.0056  14  GLN A O   
124  C CB  . GLN A 14  ? 0.0944 0.1116 0.1315 -0.0083 0.0059  0.0036  14  GLN A CB  
125  C CG  . GLN A 14  ? 0.0806 0.0936 0.1182 -0.0115 0.0059  0.0025  14  GLN A CG  
126  C CD  . GLN A 14  ? 0.1223 0.1382 0.1605 -0.0130 0.0057  -0.0003 14  GLN A CD  
127  O OE1 . GLN A 14  ? 0.1115 0.1332 0.1497 -0.0124 0.0055  -0.0018 14  GLN A OE1 
128  N NE2 . GLN A 14  ? 0.1084 0.1202 0.1466 -0.0149 0.0058  -0.0012 14  GLN A NE2 
129  N N   . PRO A 15  ? 0.1296 0.1663 0.1677 -0.0028 0.0046  0.0008  15  PRO A N   
130  C CA  . PRO A 15  ? 0.1039 0.1490 0.1413 0.0020  0.0041  0.0028  15  PRO A CA  
131  C C   . PRO A 15  ? 0.1117 0.1539 0.1464 0.0044  0.0047  0.0074  15  PRO A C   
132  O O   . PRO A 15  ? 0.1152 0.1514 0.1494 0.0017  0.0052  0.0081  15  PRO A O   
133  C CB  . PRO A 15  ? 0.0831 0.1401 0.1218 0.0004  0.0030  -0.0015 15  PRO A CB  
134  C CG  . PRO A 15  ? 0.0856 0.1374 0.1243 -0.0046 0.0034  -0.0040 15  PRO A CG  
135  C CD  . PRO A 15  ? 0.1000 0.1404 0.1391 -0.0066 0.0043  -0.0031 15  PRO A CD  
136  N N   . LEU A 16  ? 0.0935 0.1410 0.1265 0.0097  0.0046  0.0108  16  LEU A N   
137  C CA  . LEU A 16  ? 0.1143 0.1583 0.1441 0.0123  0.0058  0.0161  16  LEU A CA  
138  C C   . LEU A 16  ? 0.1373 0.1893 0.1661 0.0111  0.0050  0.0151  16  LEU A C   
139  O O   . LEU A 16  ? 0.1277 0.1921 0.1560 0.0133  0.0036  0.0137  16  LEU A O   
140  C CB  . LEU A 16  ? 0.1055 0.1514 0.1329 0.0194  0.0064  0.0208  16  LEU A CB  
141  C CG  . LEU A 16  ? 0.1133 0.1526 0.1368 0.0223  0.0085  0.0274  16  LEU A CG  
142  C CD1 . LEU A 16  ? 0.1280 0.1520 0.1517 0.0178  0.0107  0.0284  16  LEU A CD1 
143  C CD2 . LEU A 16  ? 0.1358 0.1757 0.1564 0.0303  0.0096  0.0328  16  LEU A CD2 
144  N N   . TYR A 17  ? 0.1058 0.1517 0.1343 0.0077  0.0059  0.0155  17  TYR A N   
145  C CA  . TYR A 17  ? 0.1183 0.1711 0.1457 0.0067  0.0056  0.0145  17  TYR A CA  
146  C C   . TYR A 17  ? 0.1610 0.2160 0.1847 0.0104  0.0067  0.0201  17  TYR A C   
147  O O   . TYR A 17  ? 0.1396 0.2014 0.1617 0.0102  0.0066  0.0196  17  TYR A O   
148  C CB  . TYR A 17  ? 0.0951 0.1420 0.1242 0.0019  0.0061  0.0122  17  TYR A CB  
149  C CG  . TYR A 17  ? 0.1013 0.1458 0.1332 -0.0015 0.0054  0.0071  17  TYR A CG  
150  C CD1 . TYR A 17  ? 0.0882 0.1400 0.1209 -0.0027 0.0044  0.0022  17  TYR A CD1 
151  C CD2 . TYR A 17  ? 0.1270 0.1622 0.1605 -0.0039 0.0059  0.0072  17  TYR A CD2 
152  C CE1 . TYR A 17  ? 0.1012 0.1497 0.1362 -0.0061 0.0043  -0.0020 17  TYR A CE1 
153  C CE2 . TYR A 17  ? 0.0880 0.1208 0.1233 -0.0067 0.0054  0.0033  17  TYR A CE2 
154  C CZ  . TYR A 17  ? 0.0806 0.1195 0.1166 -0.0077 0.0048  -0.0010 17  TYR A CZ  
155  O OH  . TYR A 17  ? 0.1278 0.1634 0.1652 -0.0107 0.0050  -0.0043 17  TYR A OH  
156  N N   . ARG A 18  ? 0.1339 0.1826 0.1556 0.0139  0.0081  0.0255  18  ARG A N   
157  C CA  . ARG A 18  ? 0.1568 0.2049 0.1744 0.0175  0.0101  0.0321  18  ARG A CA  
158  C C   . ARG A 18  ? 0.1438 0.2051 0.1584 0.0235  0.0088  0.0339  18  ARG A C   
159  O O   . ARG A 18  ? 0.1262 0.1893 0.1403 0.0283  0.0082  0.0355  18  ARG A O   
160  C CB  . ARG A 18  ? 0.1540 0.1881 0.1705 0.0187  0.0127  0.0370  18  ARG A CB  
161  C CG  . ARG A 18  ? 0.1886 0.2180 0.2005 0.0213  0.0158  0.0444  18  ARG A CG  
162  C CD  . ARG A 18  ? 0.2876 0.3017 0.2984 0.0224  0.0187  0.0483  18  ARG A CD  
163  N NE  . ARG A 18  ? 0.2740 0.2802 0.2807 0.0231  0.0226  0.0552  18  ARG A NE  
164  C CZ  . ARG A 18  ? 0.2671 0.2755 0.2686 0.0298  0.0241  0.0619  18  ARG A CZ  
165  N NH1 . ARG A 18  ? 0.3273 0.3471 0.3274 0.0366  0.0217  0.0624  18  ARG A NH1 
166  N NH2 . ARG A 18  ? 0.4080 0.4077 0.4056 0.0295  0.0283  0.0684  18  ARG A NH2 
167  N N   . GLU A 19  ? 0.1323 0.2035 0.1446 0.0238  0.0083  0.0338  19  GLU A N   
168  C CA  . GLU A 19  ? 0.1581 0.2441 0.1671 0.0295  0.0069  0.0354  19  GLU A CA  
169  C C   . GLU A 19  ? 0.1717 0.2534 0.1759 0.0364  0.0090  0.0444  19  GLU A C   
170  O O   . GLU A 19  ? 0.1598 0.2305 0.1614 0.0360  0.0121  0.0500  19  GLU A O   
171  C CB  . GLU A 19  ? 0.1612 0.2572 0.1681 0.0278  0.0066  0.0334  19  GLU A CB  
172  C CG  . GLU A 19  ? 0.2627 0.3777 0.2682 0.0305  0.0039  0.0297  19  GLU A CG  
173  C CD  . GLU A 19  ? 0.3892 0.5130 0.3889 0.0383  0.0041  0.0370  19  GLU A CD  
174  O OE1 . GLU A 19  ? 0.2830 0.3979 0.2788 0.0406  0.0070  0.0448  19  GLU A OE1 
175  O OE2 . GLU A 19  ? 0.4004 0.5403 0.3993 0.0420  0.0016  0.0351  19  GLU A OE2 
176  N N   . PRO A 20  ? 0.1892 0.2790 0.1922 0.0430  0.0076  0.0463  20  PRO A N   
177  C CA  . PRO A 20  ? 0.2413 0.3230 0.2402 0.0502  0.0101  0.0550  20  PRO A CA  
178  C C   . PRO A 20  ? 0.2664 0.3511 0.2585 0.0552  0.0121  0.0629  20  PRO A C   
179  O O   . PRO A 20  ? 0.3961 0.4686 0.3842 0.0595  0.0156  0.0710  20  PRO A O   
180  C CB  . PRO A 20  ? 0.2602 0.3529 0.2606 0.0562  0.0077  0.0536  20  PRO A CB  
181  C CG  . PRO A 20  ? 0.1564 0.2686 0.1593 0.0532  0.0039  0.0458  20  PRO A CG  
182  C CD  . PRO A 20  ? 0.1535 0.2589 0.1595 0.0438  0.0041  0.0400  20  PRO A CD  
183  N N   . TYR A 21  ? 0.2087 0.3087 0.1989 0.0546  0.0103  0.0609  21  TYR A N   
184  C CA  . TYR A 21  ? 0.2400 0.3444 0.2232 0.0596  0.0122  0.0687  21  TYR A CA  
185  C C   . TYR A 21  ? 0.2710 0.3641 0.2528 0.0539  0.0157  0.0710  21  TYR A C   
186  O O   . TYR A 21  ? 0.3269 0.4115 0.3034 0.0570  0.0196  0.0799  21  TYR A O   
187  C CB  . TYR A 21  ? 0.2159 0.3441 0.1970 0.0622  0.0087  0.0653  21  TYR A CB  
188  C CG  . TYR A 21  ? 0.2851 0.4271 0.2667 0.0691  0.0056  0.0646  21  TYR A CG  
189  C CD1 . TYR A 21  ? 0.3398 0.4873 0.3153 0.0795  0.0063  0.0736  21  TYR A CD1 
190  C CD2 . TYR A 21  ? 0.2535 0.4032 0.2416 0.0653  0.0023  0.0553  21  TYR A CD2 
191  C CE1 . TYR A 21  ? 0.3379 0.5001 0.3142 0.0865  0.0034  0.0731  21  TYR A CE1 
192  C CE2 . TYR A 21  ? 0.2341 0.3984 0.2232 0.0714  -0.0004 0.0544  21  TYR A CE2 
193  C CZ  . TYR A 21  ? 0.3253 0.4965 0.3088 0.0821  0.0000  0.0633  21  TYR A CZ  
194  O OH  . TYR A 21  ? 0.3235 0.5110 0.3083 0.0889  -0.0028 0.0625  21  TYR A OH  
195  N N   . THR A 22  ? 0.1932 0.2862 0.1799 0.0458  0.0147  0.0634  22  THR A N   
196  C CA  . THR A 22  ? 0.2027 0.2876 0.1892 0.0402  0.0177  0.0645  22  THR A CA  
197  C C   . THR A 22  ? 0.2309 0.2968 0.2213 0.0349  0.0201  0.0647  22  THR A C   
198  O O   . THR A 22  ? 0.2591 0.3171 0.2490 0.0310  0.0234  0.0675  22  THR A O   
199  C CB  . THR A 22  ? 0.2710 0.3664 0.2604 0.0349  0.0155  0.0561  22  THR A CB  
200  O OG1 . THR A 22  ? 0.2165 0.3101 0.2123 0.0307  0.0129  0.0479  22  THR A OG1 
201  C CG2 . THR A 22  ? 0.2577 0.3728 0.2430 0.0390  0.0134  0.0549  22  THR A CG2 
202  N N   . GLY A 23  ? 0.1864 0.2462 0.1809 0.0344  0.0186  0.0612  23  GLY A N   
203  C CA  . GLY A 23  ? 0.2232 0.2673 0.2217 0.0288  0.0203  0.0596  23  GLY A CA  
204  C C   . GLY A 23  ? 0.2660 0.3115 0.2697 0.0214  0.0189  0.0524  23  GLY A C   
205  O O   . GLY A 23  ? 0.2914 0.3259 0.2985 0.0165  0.0201  0.0508  23  GLY A O   
206  N N   . GLU A 24  ? 0.1935 0.2521 0.1978 0.0207  0.0166  0.0477  24  GLU A N   
207  C CA  . GLU A 24  ? 0.1289 0.1883 0.1374 0.0147  0.0158  0.0414  24  GLU A CA  
208  C C   . GLU A 24  ? 0.1444 0.2021 0.1576 0.0124  0.0132  0.0348  24  GLU A C   
209  O O   . GLU A 24  ? 0.1469 0.2113 0.1603 0.0150  0.0109  0.0323  24  GLU A O   
210  C CB  . GLU A 24  ? 0.1935 0.2664 0.2003 0.0151  0.0149  0.0388  24  GLU A CB  
211  C CG  . GLU A 24  ? 0.2664 0.3420 0.2684 0.0167  0.0178  0.0451  24  GLU A CG  
212  C CD  . GLU A 24  ? 0.3792 0.4694 0.3789 0.0176  0.0169  0.0420  24  GLU A CD  
213  O OE1 . GLU A 24  ? 0.5263 0.6200 0.5222 0.0185  0.0194  0.0465  24  GLU A OE1 
214  O OE2 . GLU A 24  ? 0.4574 0.5554 0.4589 0.0171  0.0141  0.0348  24  GLU A OE2 
215  N N   . TYR A 25  ? 0.1117 0.1616 0.1288 0.0074  0.0136  0.0321  25  TYR A N   
216  C CA  . TYR A 25  ? 0.1245 0.1730 0.1456 0.0049  0.0114  0.0260  25  TYR A CA  
217  C C   . TYR A 25  ? 0.1006 0.1581 0.1225 0.0036  0.0101  0.0205  25  TYR A C   
218  O O   . TYR A 25  ? 0.1391 0.1971 0.1617 0.0015  0.0111  0.0197  25  TYR A O   
219  C CB  . TYR A 25  ? 0.1505 0.1886 0.1747 0.0007  0.0123  0.0254  25  TYR A CB  
220  C CG  . TYR A 25  ? 0.1063 0.1348 0.1305 0.0013  0.0131  0.0280  25  TYR A CG  
221  C CD1 . TYR A 25  ? 0.1612 0.1837 0.1825 0.0030  0.0158  0.0340  25  TYR A CD1 
222  C CD2 . TYR A 25  ? 0.1452 0.1700 0.1718 0.0003  0.0117  0.0245  25  TYR A CD2 
223  C CE1 . TYR A 25  ? 0.1770 0.1894 0.1979 0.0038  0.0170  0.0359  25  TYR A CE1 
224  C CE2 . TYR A 25  ? 0.1091 0.1254 0.1354 0.0012  0.0127  0.0263  25  TYR A CE2 
225  C CZ  . TYR A 25  ? 0.1899 0.1996 0.2134 0.0029  0.0153  0.0317  25  TYR A CZ  
226  O OH  . TYR A 25  ? 0.2064 0.2061 0.2293 0.0039  0.0168  0.0331  25  TYR A OH  
227  N N   . LEU A 26  ? 0.1161 0.1811 0.1380 0.0049  0.0082  0.0166  26  LEU A N   
228  C CA  . LEU A 26  ? 0.1242 0.1979 0.1459 0.0038  0.0074  0.0111  26  LEU A CA  
229  C C   . LEU A 26  ? 0.1064 0.1750 0.1315 -0.0001 0.0072  0.0055  26  LEU A C   
230  O O   . LEU A 26  ? 0.1301 0.2030 0.1549 -0.0012 0.0074  0.0011  26  LEU A O   
231  C CB  . LEU A 26  ? 0.1215 0.2064 0.1418 0.0061  0.0056  0.0085  26  LEU A CB  
232  C CG  . LEU A 26  ? 0.1742 0.2666 0.1903 0.0112  0.0055  0.0141  26  LEU A CG  
233  C CD1 . LEU A 26  ? 0.1941 0.3009 0.2093 0.0133  0.0033  0.0104  26  LEU A CD1 
234  C CD2 . LEU A 26  ? 0.1694 0.2641 0.1820 0.0123  0.0073  0.0178  26  LEU A CD2 
235  N N   . LEU A 27  ? 0.0888 0.1484 0.1166 -0.0019 0.0071  0.0056  27  LEU A N   
236  C CA  . LEU A 27  ? 0.0935 0.1470 0.1239 -0.0049 0.0072  0.0018  27  LEU A CA  
237  C C   . LEU A 27  ? 0.1681 0.2130 0.2000 -0.0060 0.0078  0.0053  27  LEU A C   
238  O O   . LEU A 27  ? 0.1291 0.1708 0.1607 -0.0052 0.0080  0.0090  27  LEU A O   
239  C CB  . LEU A 27  ? 0.1152 0.1679 0.1470 -0.0064 0.0062  -0.0025 27  LEU A CB  
240  C CG  . LEU A 27  ? 0.1285 0.1903 0.1593 -0.0068 0.0057  -0.0075 27  LEU A CG  
241  C CD1 . LEU A 27  ? 0.1693 0.2317 0.2018 -0.0088 0.0051  -0.0114 27  LEU A CD1 
242  C CD2 . LEU A 27  ? 0.1847 0.2463 0.2151 -0.0081 0.0069  -0.0113 27  LEU A CD2 
243  N N   . PRO A 28  ? 0.1328 0.1744 0.1665 -0.0076 0.0084  0.0039  28  PRO A N   
244  C CA  . PRO A 28  ? 0.0911 0.1270 0.1265 -0.0090 0.0088  0.0066  28  PRO A CA  
245  C C   . PRO A 28  ? 0.0832 0.1127 0.1201 -0.0105 0.0079  0.0053  28  PRO A C   
246  O O   . PRO A 28  ? 0.1182 0.1443 0.1565 -0.0119 0.0080  0.0064  28  PRO A O   
247  C CB  . PRO A 28  ? 0.1023 0.1406 0.1388 -0.0092 0.0096  0.0054  28  PRO A CB  
248  C CG  . PRO A 28  ? 0.1098 0.1493 0.1457 -0.0085 0.0094  0.0007  28  PRO A CG  
249  C CD  . PRO A 28  ? 0.1706 0.2144 0.2044 -0.0078 0.0088  -0.0002 28  PRO A CD  
250  N N   . TRP A 29  ? 0.1126 0.1415 0.1491 -0.0104 0.0072  0.0030  29  TRP A N   
251  C CA  . TRP A 29  ? 0.1009 0.1244 0.1384 -0.0119 0.0067  0.0015  29  TRP A CA  
252  C C   . TRP A 29  ? 0.1148 0.1338 0.1528 -0.0126 0.0066  0.0039  29  TRP A C   
253  O O   . TRP A 29  ? 0.1097 0.1249 0.1485 -0.0139 0.0063  0.0034  29  TRP A O   
254  C CB  . TRP A 29  ? 0.0970 0.1218 0.1342 -0.0122 0.0064  -0.0017 29  TRP A CB  
255  C CG  . TRP A 29  ? 0.1431 0.1710 0.1799 -0.0127 0.0070  -0.0055 29  TRP A CG  
256  C CD1 . TRP A 29  ? 0.1269 0.1611 0.1631 -0.0127 0.0068  -0.0083 29  TRP A CD1 
257  C CD2 . TRP A 29  ? 0.1452 0.1698 0.1820 -0.0131 0.0080  -0.0074 29  TRP A CD2 
258  N NE1 . TRP A 29  ? 0.1208 0.1553 0.1566 -0.0139 0.0078  -0.0124 29  TRP A NE1 
259  C CE2 . TRP A 29  ? 0.1378 0.1656 0.1739 -0.0138 0.0088  -0.0117 29  TRP A CE2 
260  C CE3 . TRP A 29  ? 0.1563 0.1761 0.1937 -0.0126 0.0085  -0.0060 29  TRP A CE3 
261  C CZ2 . TRP A 29  ? 0.2197 0.2438 0.2552 -0.0141 0.0104  -0.0147 29  TRP A CZ2 
262  C CZ3 . TRP A 29  ? 0.1116 0.1288 0.1485 -0.0120 0.0099  -0.0083 29  TRP A CZ3 
263  C CH2 . TRP A 29  ? 0.1707 0.1890 0.2065 -0.0127 0.0110  -0.0126 29  TRP A CH2 
264  N N   . THR A 30  ? 0.1131 0.1320 0.1502 -0.0116 0.0069  0.0065  30  THR A N   
265  C CA  . THR A 30  ? 0.1098 0.1229 0.1471 -0.0126 0.0073  0.0082  30  THR A CA  
266  C C   . THR A 30  ? 0.0961 0.1080 0.1346 -0.0149 0.0078  0.0092  30  THR A C   
267  O O   . THR A 30  ? 0.1228 0.1315 0.1623 -0.0170 0.0076  0.0085  30  THR A O   
268  C CB  . THR A 30  ? 0.1080 0.1198 0.1438 -0.0105 0.0082  0.0111  30  THR A CB  
269  O OG1 . THR A 30  ? 0.1305 0.1457 0.1658 -0.0081 0.0074  0.0098  30  THR A OG1 
270  C CG2 . THR A 30  ? 0.1384 0.1424 0.1742 -0.0118 0.0092  0.0123  30  THR A CG2 
271  N N   . PHE A 31  ? 0.0974 0.1134 0.1361 -0.0147 0.0085  0.0106  31  PHE A N   
272  C CA  . PHE A 31  ? 0.0943 0.1113 0.1348 -0.0171 0.0091  0.0112  31  PHE A CA  
273  C C   . PHE A 31  ? 0.1371 0.1554 0.1792 -0.0176 0.0078  0.0088  31  PHE A C   
274  O O   . PHE A 31  ? 0.1159 0.1338 0.1594 -0.0197 0.0075  0.0084  31  PHE A O   
275  C CB  . PHE A 31  ? 0.1056 0.1282 0.1461 -0.0165 0.0103  0.0129  31  PHE A CB  
276  C CG  . PHE A 31  ? 0.1158 0.1420 0.1588 -0.0188 0.0109  0.0131  31  PHE A CG  
277  C CD1 . PHE A 31  ? 0.1666 0.1908 0.2105 -0.0223 0.0124  0.0149  31  PHE A CD1 
278  C CD2 . PHE A 31  ? 0.1145 0.1462 0.1591 -0.0176 0.0103  0.0113  31  PHE A CD2 
279  C CE1 . PHE A 31  ? 0.1230 0.1526 0.1699 -0.0251 0.0130  0.0146  31  PHE A CE1 
280  C CE2 . PHE A 31  ? 0.1300 0.1672 0.1775 -0.0193 0.0108  0.0115  31  PHE A CE2 
281  C CZ  . PHE A 31  ? 0.1502 0.1873 0.1991 -0.0233 0.0119  0.0130  31  PHE A CZ  
282  N N   . PHE A 32  ? 0.0905 0.1104 0.1321 -0.0155 0.0073  0.0070  32  PHE A N   
283  C CA  . PHE A 32  ? 0.0809 0.1014 0.1234 -0.0151 0.0067  0.0055  32  PHE A CA  
284  C C   . PHE A 32  ? 0.1096 0.1257 0.1516 -0.0160 0.0058  0.0048  32  PHE A C   
285  O O   . PHE A 32  ? 0.1072 0.1243 0.1499 -0.0164 0.0051  0.0048  32  PHE A O   
286  C CB  . PHE A 32  ? 0.1221 0.1435 0.1637 -0.0128 0.0071  0.0037  32  PHE A CB  
287  C CG  . PHE A 32  ? 0.1307 0.1576 0.1731 -0.0115 0.0080  0.0040  32  PHE A CG  
288  C CD1 . PHE A 32  ? 0.1215 0.1527 0.1660 -0.0116 0.0082  0.0053  32  PHE A CD1 
289  C CD2 . PHE A 32  ? 0.1451 0.1742 0.1861 -0.0103 0.0088  0.0026  32  PHE A CD2 
290  C CE1 . PHE A 32  ? 0.1463 0.1835 0.1917 -0.0103 0.0093  0.0054  32  PHE A CE1 
291  C CE2 . PHE A 32  ? 0.1544 0.1890 0.1957 -0.0089 0.0098  0.0026  32  PHE A CE2 
292  C CZ  . PHE A 32  ? 0.0993 0.1378 0.1429 -0.0088 0.0102  0.0042  32  PHE A CZ  
293  N N   . HIS A 33  ? 0.0813 0.0937 0.1219 -0.0162 0.0057  0.0041  33  HIS A N   
294  C CA  . HIS A 33  ? 0.0938 0.1028 0.1338 -0.0172 0.0051  0.0034  33  HIS A CA  
295  C C   . HIS A 33  ? 0.1009 0.1088 0.1414 -0.0194 0.0049  0.0040  33  HIS A C   
296  O O   . HIS A 33  ? 0.1090 0.1159 0.1491 -0.0204 0.0043  0.0031  33  HIS A O   
297  C CB  . HIS A 33  ? 0.0781 0.0848 0.1170 -0.0169 0.0053  0.0021  33  HIS A CB  
298  C CG  . HIS A 33  ? 0.0957 0.1022 0.1340 -0.0162 0.0057  0.0005  33  HIS A CG  
299  N ND1 . HIS A 33  ? 0.1006 0.1044 0.1380 -0.0161 0.0060  0.0002  33  HIS A ND1 
300  C CD2 . HIS A 33  ? 0.0997 0.1081 0.1379 -0.0156 0.0063  -0.0010 33  HIS A CD2 
301  C CE1 . HIS A 33  ? 0.1254 0.1278 0.1622 -0.0158 0.0071  -0.0014 33  HIS A CE1 
302  N NE2 . HIS A 33  ? 0.1339 0.1395 0.1713 -0.0158 0.0072  -0.0026 33  HIS A NE2 
303  N N   . ALA A 34  ? 0.0929 0.1007 0.1340 -0.0202 0.0058  0.0053  34  ALA A N   
304  C CA  . ALA A 34  ? 0.0996 0.1057 0.1414 -0.0232 0.0063  0.0054  34  ALA A CA  
305  C C   . ALA A 34  ? 0.1138 0.1252 0.1575 -0.0250 0.0055  0.0048  34  ALA A C   
306  O O   . ALA A 34  ? 0.1099 0.1217 0.1538 -0.0273 0.0049  0.0033  34  ALA A O   
307  C CB  . ALA A 34  ? 0.1474 0.1508 0.1889 -0.0238 0.0081  0.0074  34  ALA A CB  
308  N N   . VAL A 35  ? 0.0962 0.1131 0.1413 -0.0239 0.0056  0.0058  35  VAL A N   
309  C CA  . VAL A 35  ? 0.1257 0.1497 0.1731 -0.0251 0.0049  0.0054  35  VAL A CA  
310  C C   . VAL A 35  ? 0.1233 0.1495 0.1701 -0.0228 0.0032  0.0046  35  VAL A C   
311  O O   . VAL A 35  ? 0.1123 0.1445 0.1604 -0.0237 0.0022  0.0039  35  VAL A O   
312  C CB  . VAL A 35  ? 0.1246 0.1547 0.1740 -0.0242 0.0058  0.0066  35  VAL A CB  
313  C CG1 . VAL A 35  ? 0.1158 0.1433 0.1649 -0.0263 0.0078  0.0082  35  VAL A CG1 
314  C CG2 . VAL A 35  ? 0.1337 0.1644 0.1820 -0.0196 0.0056  0.0068  35  VAL A CG2 
315  N N   . LYS A 36  ? 0.1320 0.1536 0.1766 -0.0200 0.0032  0.0046  36  LYS A N   
316  C CA  . LYS A 36  ? 0.0911 0.1130 0.1343 -0.0175 0.0023  0.0046  36  LYS A CA  
317  C C   . LYS A 36  ? 0.1613 0.1797 0.2023 -0.0188 0.0017  0.0037  36  LYS A C   
318  O O   . LYS A 36  ? 0.1493 0.1709 0.1895 -0.0181 0.0006  0.0039  36  LYS A O   
319  C CB  . LYS A 36  ? 0.1140 0.1323 0.1557 -0.0143 0.0032  0.0049  36  LYS A CB  
320  C CG  . LYS A 36  ? 0.1228 0.1406 0.1629 -0.0111 0.0031  0.0058  36  LYS A CG  
321  C CD  . LYS A 36  ? 0.1237 0.1368 0.1625 -0.0083 0.0048  0.0056  36  LYS A CD  
322  C CE  . LYS A 36  ? 0.1145 0.1205 0.1513 -0.0099 0.0058  0.0042  36  LYS A CE  
323  N NZ  . LYS A 36  ? 0.1283 0.1306 0.1626 -0.0101 0.0057  0.0050  36  LYS A NZ  
324  N N   . ASP A 37  ? 0.0807 0.0935 0.1207 -0.0202 0.0023  0.0029  37  ASP A N   
325  C CA  . ASP A 37  ? 0.0973 0.1066 0.1349 -0.0207 0.0022  0.0020  37  ASP A CA  
326  C C   . ASP A 37  ? 0.1147 0.1217 0.1522 -0.0234 0.0024  0.0004  37  ASP A C   
327  O O   . ASP A 37  ? 0.1185 0.1256 0.1545 -0.0245 0.0019  -0.0009 37  ASP A O   
328  C CB  . ASP A 37  ? 0.1195 0.1244 0.1557 -0.0191 0.0032  0.0020  37  ASP A CB  
329  C CG  . ASP A 37  ? 0.1301 0.1350 0.1661 -0.0167 0.0037  0.0029  37  ASP A CG  
330  O OD1 . ASP A 37  ? 0.1335 0.1391 0.1682 -0.0151 0.0034  0.0040  37  ASP A OD1 
331  O OD2 . ASP A 37  ? 0.1188 0.1234 0.1557 -0.0162 0.0044  0.0026  37  ASP A OD2 
332  N N   . TYR A 38  ? 0.1173 0.1217 0.1559 -0.0242 0.0034  0.0006  38  TYR A N   
333  C CA  . TYR A 38  ? 0.1391 0.1387 0.1769 -0.0256 0.0043  -0.0008 38  TYR A CA  
334  C C   . TYR A 38  ? 0.1405 0.1407 0.1785 -0.0292 0.0042  -0.0027 38  TYR A C   
335  O O   . TYR A 38  ? 0.1220 0.1185 0.1586 -0.0304 0.0048  -0.0048 38  TYR A O   
336  C CB  . TYR A 38  ? 0.1018 0.0979 0.1400 -0.0246 0.0057  0.0007  38  TYR A CB  
337  C CG  . TYR A 38  ? 0.1245 0.1212 0.1623 -0.0215 0.0057  0.0014  38  TYR A CG  
338  C CD1 . TYR A 38  ? 0.1045 0.1015 0.1412 -0.0207 0.0052  0.0002  38  TYR A CD1 
339  C CD2 . TYR A 38  ? 0.1386 0.1363 0.1768 -0.0199 0.0062  0.0032  38  TYR A CD2 
340  C CE1 . TYR A 38  ? 0.1132 0.1115 0.1499 -0.0189 0.0055  0.0001  38  TYR A CE1 
341  C CE2 . TYR A 38  ? 0.1194 0.1193 0.1573 -0.0176 0.0061  0.0031  38  TYR A CE2 
342  C CZ  . TYR A 38  ? 0.1376 0.1379 0.1751 -0.0175 0.0057  0.0013  38  TYR A CZ  
343  O OH  . TYR A 38  ? 0.1314 0.1347 0.1691 -0.0162 0.0058  0.0004  38  TYR A OH  
344  N N   . TYR A 39  ? 0.1169 0.1225 0.1569 -0.0310 0.0036  -0.0025 39  TYR A N   
345  C CA  . TYR A 39  ? 0.1472 0.1561 0.1878 -0.0350 0.0032  -0.0051 39  TYR A CA  
346  C C   . TYR A 39  ? 0.1330 0.1487 0.1724 -0.0340 0.0011  -0.0060 39  TYR A C   
347  O O   . TYR A 39  ? 0.0967 0.1137 0.1346 -0.0363 0.0006  -0.0088 39  TYR A O   
348  C CB  . TYR A 39  ? 0.0994 0.1131 0.1431 -0.0380 0.0037  -0.0048 39  TYR A CB  
349  C CG  . TYR A 39  ? 0.1181 0.1379 0.1631 -0.0429 0.0031  -0.0082 39  TYR A CG  
350  C CD1 . TYR A 39  ? 0.1250 0.1390 0.1697 -0.0478 0.0049  -0.0112 39  TYR A CD1 
351  C CD2 . TYR A 39  ? 0.1274 0.1590 0.1737 -0.0424 0.0008  -0.0086 39  TYR A CD2 
352  C CE1 . TYR A 39  ? 0.1484 0.1688 0.1945 -0.0532 0.0045  -0.0152 39  TYR A CE1 
353  C CE2 . TYR A 39  ? 0.1484 0.1882 0.1962 -0.0471 -0.0001 -0.0121 39  TYR A CE2 
354  C CZ  . TYR A 39  ? 0.1856 0.2200 0.2334 -0.0530 0.0018  -0.0159 39  TYR A CZ  
355  O OH  . TYR A 39  ? 0.2177 0.2607 0.2669 -0.0585 0.0010  -0.0204 39  TYR A OH  
356  N N   . ASP A 40  ? 0.1289 0.1487 0.1683 -0.0304 0.0000  -0.0035 40  ASP A N   
357  C CA  . ASP A 40  ? 0.1205 0.1476 0.1587 -0.0289 -0.0018 -0.0034 40  ASP A CA  
358  C C   . ASP A 40  ? 0.1071 0.1309 0.1414 -0.0276 -0.0019 -0.0037 40  ASP A C   
359  O O   . ASP A 40  ? 0.1151 0.1448 0.1475 -0.0275 -0.0033 -0.0044 40  ASP A O   
360  C CB  . ASP A 40  ? 0.0865 0.1178 0.1258 -0.0249 -0.0023 -0.0004 40  ASP A CB  
361  C CG  . ASP A 40  ? 0.1286 0.1688 0.1717 -0.0263 -0.0028 -0.0006 40  ASP A CG  
362  O OD1 . ASP A 40  ? 0.1319 0.1811 0.1756 -0.0279 -0.0044 -0.0021 40  ASP A OD1 
363  O OD2 . ASP A 40  ? 0.1582 0.1973 0.2036 -0.0263 -0.0017 0.0004  40  ASP A OD2 
364  N N   . MET A 41  ? 0.1083 0.1241 0.1413 -0.0265 -0.0005 -0.0032 41  MET A N   
365  C CA  . MET A 41  ? 0.0976 0.1112 0.1271 -0.0256 -0.0003 -0.0036 41  MET A CA  
366  C C   . MET A 41  ? 0.1205 0.1351 0.1486 -0.0286 -0.0005 -0.0071 41  MET A C   
367  O O   . MET A 41  ? 0.1289 0.1483 0.1542 -0.0284 -0.0015 -0.0075 41  MET A O   
368  C CB  . MET A 41  ? 0.1019 0.1088 0.1311 -0.0242 0.0014  -0.0028 41  MET A CB  
369  C CG  . MET A 41  ? 0.1053 0.1113 0.1345 -0.0214 0.0018  0.0000  41  MET A CG  
370  S SD  . MET A 41  ? 0.1179 0.1246 0.1429 -0.0192 0.0019  0.0022  41  MET A SD  
371  C CE  . MET A 41  ? 0.1309 0.1330 0.1539 -0.0205 0.0037  0.0008  41  MET A CE  
372  N N   . PRO A 42  ? 0.1333 0.1436 0.1628 -0.0313 0.0006  -0.0096 42  PRO A N   
373  C CA  . PRO A 42  ? 0.1012 0.1124 0.1292 -0.0347 0.0006  -0.0138 42  PRO A CA  
374  C C   . PRO A 42  ? 0.1027 0.1233 0.1316 -0.0374 -0.0012 -0.0155 42  PRO A C   
375  O O   . PRO A 42  ? 0.1357 0.1606 0.1624 -0.0396 -0.0019 -0.0190 42  PRO A O   
376  C CB  . PRO A 42  ? 0.1421 0.1449 0.1716 -0.0365 0.0028  -0.0155 42  PRO A CB  
377  C CG  . PRO A 42  ? 0.1177 0.1188 0.1501 -0.0350 0.0031  -0.0119 42  PRO A CG  
378  C CD  . PRO A 42  ? 0.1255 0.1293 0.1571 -0.0311 0.0022  -0.0088 42  PRO A CD  
379  N N   . ALA A 43  ? 0.1238 0.1492 0.1558 -0.0373 -0.0020 -0.0136 43  ALA A N   
380  C CA  . ALA A 43  ? 0.1477 0.1841 0.1811 -0.0401 -0.0038 -0.0156 43  ALA A CA  
381  C C   . ALA A 43  ? 0.1565 0.2026 0.1870 -0.0373 -0.0061 -0.0148 43  ALA A C   
382  O O   . ALA A 43  ? 0.1411 0.1980 0.1720 -0.0398 -0.0078 -0.0174 43  ALA A O   
383  C CB  . ALA A 43  ? 0.1382 0.1788 0.1760 -0.0403 -0.0039 -0.0137 43  ALA A CB  
384  N N   . TYR A 44  ? 0.1041 0.1469 0.1316 -0.0325 -0.0060 -0.0111 44  TYR A N   
385  C CA  . TYR A 44  ? 0.1129 0.1632 0.1364 -0.0296 -0.0076 -0.0097 44  TYR A CA  
386  C C   . TYR A 44  ? 0.1321 0.1864 0.1527 -0.0331 -0.0082 -0.0144 44  TYR A C   
387  O O   . TYR A 44  ? 0.1521 0.2174 0.1702 -0.0322 -0.0102 -0.0147 44  TYR A O   
388  C CB  . TYR A 44  ? 0.1029 0.1461 0.1231 -0.0250 -0.0063 -0.0054 44  TYR A CB  
389  C CG  . TYR A 44  ? 0.1012 0.1434 0.1222 -0.0204 -0.0061 -0.0005 44  TYR A CG  
390  C CD1 . TYR A 44  ? 0.1182 0.1675 0.1368 -0.0159 -0.0074 0.0030  44  TYR A CD1 
391  C CD2 . TYR A 44  ? 0.1125 0.1467 0.1364 -0.0201 -0.0045 0.0005  44  TYR A CD2 
392  C CE1 . TYR A 44  ? 0.1168 0.1636 0.1359 -0.0112 -0.0066 0.0073  44  TYR A CE1 
393  C CE2 . TYR A 44  ? 0.1533 0.1860 0.1777 -0.0160 -0.0040 0.0042  44  TYR A CE2 
394  C CZ  . TYR A 44  ? 0.1525 0.1906 0.1745 -0.0116 -0.0049 0.0075  44  TYR A CZ  
395  O OH  . TYR A 44  ? 0.1552 0.1904 0.1776 -0.0072 -0.0039 0.0109  44  TYR A OH  
396  N N   . LEU A 45  ? 0.1092 0.1551 0.1300 -0.0366 -0.0063 -0.0182 45  LEU A N   
397  C CA  . LEU A 45  ? 0.1274 0.1756 0.1452 -0.0400 -0.0063 -0.0235 45  LEU A CA  
398  C C   . LEU A 45  ? 0.1685 0.2272 0.1883 -0.0450 -0.0079 -0.0284 45  LEU A C   
399  O O   . LEU A 45  ? 0.1875 0.2516 0.2043 -0.0478 -0.0085 -0.0332 45  LEU A O   
400  C CB  . LEU A 45  ? 0.1164 0.1520 0.1344 -0.0419 -0.0035 -0.0263 45  LEU A CB  
401  C CG  . LEU A 45  ? 0.1142 0.1420 0.1301 -0.0378 -0.0019 -0.0229 45  LEU A CG  
402  C CD1 . LEU A 45  ? 0.1330 0.1497 0.1503 -0.0389 0.0008  -0.0252 45  LEU A CD1 
403  C CD2 . LEU A 45  ? 0.1651 0.1981 0.1756 -0.0363 -0.0023 -0.0233 45  LEU A CD2 
404  N N   . LYS A 46  ? 0.1808 0.2433 0.2053 -0.0465 -0.0085 -0.0277 46  LYS A N   
405  C CA  . LYS A 46  ? 0.1981 0.2733 0.2249 -0.0515 -0.0101 -0.0322 46  LYS A CA  
406  C C   . LYS A 46  ? 0.2389 0.3311 0.2636 -0.0482 -0.0135 -0.0308 46  LYS A C   
407  O O   . LYS A 46  ? 0.2400 0.3455 0.2652 -0.0523 -0.0154 -0.0357 46  LYS A O   
408  C CB  . LYS A 46  ? 0.1893 0.2651 0.2221 -0.0539 -0.0095 -0.0313 46  LYS A CB  
409  C CG  . LYS A 46  ? 0.3285 0.3899 0.3634 -0.0584 -0.0061 -0.0336 46  LYS A CG  
410  C CD  . LYS A 46  ? 0.4285 0.4897 0.4684 -0.0593 -0.0052 -0.0308 46  LYS A CD  
411  C CE  . LYS A 46  ? 0.5930 0.6540 0.6363 -0.0677 -0.0032 -0.0360 46  LYS A CE  
412  N NZ  . LYS A 46  ? 0.6828 0.7313 0.7235 -0.0720 -0.0005 -0.0410 46  LYS A NZ  
413  N N   . ASP A 47  ? 0.1740 0.2659 0.1960 -0.0409 -0.0142 -0.0242 47  ASP A N   
414  C CA  . ASP A 47  ? 0.1878 0.2947 0.2075 -0.0362 -0.0171 -0.0211 47  ASP A CA  
415  C C   . ASP A 47  ? 0.1917 0.2988 0.2043 -0.0321 -0.0174 -0.0189 47  ASP A C   
416  O O   . ASP A 47  ? 0.1979 0.3190 0.2075 -0.0288 -0.0199 -0.0173 47  ASP A O   
417  C CB  . ASP A 47  ? 0.1868 0.2940 0.2091 -0.0302 -0.0174 -0.0145 47  ASP A CB  
418  C CG  . ASP A 47  ? 0.2776 0.3891 0.3068 -0.0336 -0.0174 -0.0164 47  ASP A CG  
419  O OD1 . ASP A 47  ? 0.2611 0.3831 0.2929 -0.0396 -0.0185 -0.0220 47  ASP A OD1 
420  O OD2 . ASP A 47  ? 0.3438 0.4484 0.3755 -0.0307 -0.0161 -0.0125 47  ASP A OD2 
421  N N   . PHE A 48  ? 0.1670 0.2600 0.1768 -0.0321 -0.0149 -0.0185 48  PHE A N   
422  C CA  . PHE A 48  ? 0.1760 0.2679 0.1791 -0.0284 -0.0144 -0.0158 48  PHE A CA  
423  C C   . PHE A 48  ? 0.1768 0.2629 0.1777 -0.0329 -0.0127 -0.0217 48  PHE A C   
424  O O   . PHE A 48  ? 0.1699 0.2442 0.1738 -0.0360 -0.0105 -0.0242 48  PHE A O   
425  C CB  . PHE A 48  ? 0.1498 0.2302 0.1517 -0.0230 -0.0123 -0.0087 48  PHE A CB  
426  C CG  . PHE A 48  ? 0.1826 0.2674 0.1861 -0.0178 -0.0135 -0.0031 48  PHE A CG  
427  C CD1 . PHE A 48  ? 0.2205 0.3155 0.2195 -0.0123 -0.0151 0.0013  48  PHE A CD1 
428  C CD2 . PHE A 48  ? 0.1571 0.2367 0.1663 -0.0179 -0.0128 -0.0022 48  PHE A CD2 
429  C CE1 . PHE A 48  ? 0.1814 0.2803 0.1819 -0.0066 -0.0159 0.0066  48  PHE A CE1 
430  C CE2 . PHE A 48  ? 0.2019 0.2857 0.2126 -0.0128 -0.0136 0.0025  48  PHE A CE2 
431  C CZ  . PHE A 48  ? 0.1530 0.2461 0.1594 -0.0069 -0.0151 0.0069  48  PHE A CZ  
432  N N   . GLU A 49  ? 0.1806 0.2755 0.1759 -0.0329 -0.0137 -0.0237 49  GLU A N   
433  C CA  . GLU A 49  ? 0.2472 0.3386 0.2400 -0.0372 -0.0122 -0.0303 49  GLU A CA  
434  C C   . GLU A 49  ? 0.2122 0.2936 0.2010 -0.0340 -0.0095 -0.0268 49  GLU A C   
435  O O   . GLU A 49  ? 0.2659 0.3523 0.2486 -0.0324 -0.0093 -0.0265 49  GLU A O   
436  C CB  . GLU A 49  ? 0.2839 0.3914 0.2728 -0.0395 -0.0146 -0.0354 49  GLU A CB  
437  C CG  . GLU A 49  ? 0.5113 0.6268 0.5049 -0.0458 -0.0163 -0.0424 49  GLU A CG  
438  C CD  . GLU A 49  ? 0.7146 0.8175 0.7112 -0.0523 -0.0134 -0.0496 49  GLU A CD  
439  O OE1 . GLU A 49  ? 0.7720 0.8678 0.7648 -0.0529 -0.0113 -0.0528 49  GLU A OE1 
440  O OE2 . GLU A 49  ? 0.7837 0.8836 0.7861 -0.0564 -0.0131 -0.0519 49  GLU A OE2 
441  N N   . ILE A 50  ? 0.1629 0.2311 0.1553 -0.0331 -0.0073 -0.0241 50  ILE A N   
442  C CA  . ILE A 50  ? 0.1429 0.2014 0.1332 -0.0311 -0.0044 -0.0217 50  ILE A CA  
443  C C   . ILE A 50  ? 0.1794 0.2266 0.1742 -0.0338 -0.0022 -0.0255 50  ILE A C   
444  O O   . ILE A 50  ? 0.2081 0.2538 0.2069 -0.0370 -0.0027 -0.0291 50  ILE A O   
445  C CB  . ILE A 50  ? 0.1511 0.2056 0.1411 -0.0264 -0.0037 -0.0137 50  ILE A CB  
446  C CG1 . ILE A 50  ? 0.2037 0.2528 0.2000 -0.0264 -0.0040 -0.0122 50  ILE A CG1 
447  C CG2 . ILE A 50  ? 0.1717 0.2365 0.1567 -0.0227 -0.0055 -0.0092 50  ILE A CG2 
448  C CD1 . ILE A 50  ? 0.2928 0.3378 0.2892 -0.0222 -0.0033 -0.0053 50  ILE A CD1 
449  N N   . LYS A 51  ? 0.1393 0.1791 0.1332 -0.0325 0.0004  -0.0246 51  LYS A N   
450  C CA  . LYS A 51  ? 0.1376 0.1671 0.1355 -0.0334 0.0026  -0.0268 51  LYS A CA  
451  C C   . LYS A 51  ? 0.1436 0.1672 0.1447 -0.0309 0.0034  -0.0213 51  LYS A C   
452  O O   . LYS A 51  ? 0.1482 0.1725 0.1471 -0.0286 0.0041  -0.0170 51  LYS A O   
453  C CB  . LYS A 51  ? 0.1712 0.1981 0.1666 -0.0335 0.0051  -0.0305 51  LYS A CB  
454  C CG  . LYS A 51  ? 0.1617 0.1953 0.1525 -0.0358 0.0046  -0.0362 51  LYS A CG  
455  C CD  . LYS A 51  ? 0.1740 0.2068 0.1671 -0.0398 0.0037  -0.0420 51  LYS A CD  
456  C CE  . LYS A 51  ? 0.2605 0.2980 0.2493 -0.0426 0.0042  -0.0494 51  LYS A CE  
457  N NZ  . LYS A 51  ? 0.3803 0.4163 0.3714 -0.0475 0.0038  -0.0556 51  LYS A NZ  
458  N N   . LEU A 52  ? 0.1309 0.1485 0.1369 -0.0315 0.0036  -0.0218 52  LEU A N   
459  C CA  . LEU A 52  ? 0.1308 0.1432 0.1400 -0.0295 0.0044  -0.0178 52  LEU A CA  
460  C C   . LEU A 52  ? 0.1241 0.1295 0.1366 -0.0297 0.0060  -0.0200 52  LEU A C   
461  O O   . LEU A 52  ? 0.1568 0.1598 0.1708 -0.0316 0.0059  -0.0230 52  LEU A O   
462  C CB  . LEU A 52  ? 0.1517 0.1659 0.1632 -0.0290 0.0026  -0.0145 52  LEU A CB  
463  C CG  . LEU A 52  ? 0.1635 0.1843 0.1721 -0.0273 0.0010  -0.0112 52  LEU A CG  
464  C CD1 . LEU A 52  ? 0.1514 0.1740 0.1633 -0.0266 -0.0005 -0.0089 52  LEU A CD1 
465  C CD2 . LEU A 52  ? 0.1172 0.1358 0.1229 -0.0249 0.0027  -0.0072 52  LEU A CD2 
466  N N   . ASN A 53  ? 0.1098 0.1122 0.1234 -0.0277 0.0077  -0.0185 53  ASN A N   
467  C CA  . ASN A 53  ? 0.1273 0.1244 0.1438 -0.0266 0.0091  -0.0199 53  ASN A CA  
468  C C   . ASN A 53  ? 0.1341 0.1293 0.1541 -0.0253 0.0088  -0.0166 53  ASN A C   
469  O O   . ASN A 53  ? 0.1211 0.1185 0.1414 -0.0250 0.0081  -0.0135 53  ASN A O   
470  C CB  . ASN A 53  ? 0.1334 0.1311 0.1488 -0.0250 0.0112  -0.0214 53  ASN A CB  
471  C CG  . ASN A 53  ? 0.1167 0.1173 0.1280 -0.0262 0.0117  -0.0247 53  ASN A CG  
472  O OD1 . ASN A 53  ? 0.1300 0.1281 0.1404 -0.0273 0.0120  -0.0287 53  ASN A OD1 
473  N ND2 . ASN A 53  ? 0.1264 0.1320 0.1347 -0.0264 0.0118  -0.0231 53  ASN A ND2 
474  N N   . PHE A 54  ? 0.1054 0.0961 0.1279 -0.0241 0.0096  -0.0172 54  PHE A N   
475  C CA  . PHE A 54  ? 0.1016 0.0911 0.1270 -0.0229 0.0092  -0.0143 54  PHE A CA  
476  C C   . PHE A 54  ? 0.1287 0.1161 0.1558 -0.0198 0.0107  -0.0143 54  PHE A C   
477  O O   . PHE A 54  ? 0.1313 0.1150 0.1576 -0.0186 0.0122  -0.0165 54  PHE A O   
478  C CB  . PHE A 54  ? 0.1024 0.0897 0.1288 -0.0247 0.0083  -0.0138 54  PHE A CB  
479  C CG  . PHE A 54  ? 0.1030 0.0947 0.1284 -0.0269 0.0066  -0.0134 54  PHE A CG  
480  C CD1 . PHE A 54  ? 0.1726 0.1675 0.1990 -0.0261 0.0054  -0.0103 54  PHE A CD1 
481  C CD2 . PHE A 54  ? 0.1492 0.1429 0.1724 -0.0292 0.0061  -0.0163 54  PHE A CD2 
482  C CE1 . PHE A 54  ? 0.1597 0.1591 0.1850 -0.0269 0.0039  -0.0095 54  PHE A CE1 
483  C CE2 . PHE A 54  ? 0.1652 0.1650 0.1873 -0.0304 0.0043  -0.0157 54  PHE A CE2 
484  C CZ  . PHE A 54  ? 0.1435 0.1461 0.1667 -0.0289 0.0032  -0.0119 54  PHE A CZ  
485  N N   . ASN A 55  ? 0.1341 0.1242 0.1633 -0.0182 0.0104  -0.0120 55  ASN A N   
486  C CA  . ASN A 55  ? 0.1071 0.0970 0.1380 -0.0147 0.0113  -0.0113 55  ASN A CA  
487  C C   . ASN A 55  ? 0.1208 0.1091 0.1530 -0.0142 0.0106  -0.0087 55  ASN A C   
488  O O   . ASN A 55  ? 0.1433 0.1342 0.1761 -0.0158 0.0093  -0.0074 55  ASN A O   
489  C CB  . ASN A 55  ? 0.1116 0.1085 0.1441 -0.0135 0.0115  -0.0114 55  ASN A CB  
490  C CG  . ASN A 55  ? 0.1193 0.1184 0.1536 -0.0091 0.0122  -0.0109 55  ASN A CG  
491  O OD1 . ASN A 55  ? 0.1173 0.1139 0.1511 -0.0063 0.0136  -0.0120 55  ASN A OD1 
492  N ND2 . ASN A 55  ? 0.1234 0.1278 0.1598 -0.0082 0.0114  -0.0094 55  ASN A ND2 
493  N N   . LEU A 56  ? 0.1233 0.1070 0.1555 -0.0116 0.0117  -0.0077 56  LEU A N   
494  C CA  . LEU A 56  ? 0.1405 0.1227 0.1734 -0.0107 0.0115  -0.0047 56  LEU A CA  
495  C C   . LEU A 56  ? 0.1311 0.1157 0.1647 -0.0055 0.0122  -0.0029 56  LEU A C   
496  O O   . LEU A 56  ? 0.1682 0.1489 0.2010 -0.0022 0.0139  -0.0032 56  LEU A O   
497  C CB  . LEU A 56  ? 0.1373 0.1112 0.1691 -0.0125 0.0127  -0.0044 56  LEU A CB  
498  C CG  . LEU A 56  ? 0.1652 0.1386 0.1967 -0.0176 0.0118  -0.0063 56  LEU A CG  
499  C CD1 . LEU A 56  ? 0.1763 0.1417 0.2070 -0.0201 0.0135  -0.0070 56  LEU A CD1 
500  C CD2 . LEU A 56  ? 0.1872 0.1667 0.2200 -0.0192 0.0098  -0.0047 56  LEU A CD2 
501  N N   . THR A 57  ? 0.1106 0.1021 0.1456 -0.0044 0.0110  -0.0013 57  THR A N   
502  C CA  . THR A 57  ? 0.1020 0.0972 0.1374 0.0010  0.0114  0.0005  57  THR A CA  
503  C C   . THR A 57  ? 0.1374 0.1255 0.1710 0.0037  0.0128  0.0043  57  THR A C   
504  O O   . THR A 57  ? 0.1093 0.0927 0.1422 0.0007  0.0129  0.0056  57  THR A O   
505  C CB  . THR A 57  ? 0.1205 0.1266 0.1576 0.0013  0.0098  0.0006  57  THR A CB  
506  O OG1 . THR A 57  ? 0.1238 0.1294 0.1606 -0.0006 0.0090  0.0023  57  THR A OG1 
507  C CG2 . THR A 57  ? 0.0912 0.1028 0.1299 -0.0022 0.0092  -0.0030 57  THR A CG2 
508  N N   . PRO A 58  ? 0.1150 0.1023 0.1478 0.0097  0.0142  0.0062  58  PRO A N   
509  C CA  . PRO A 58  ? 0.1238 0.1023 0.1541 0.0126  0.0162  0.0104  58  PRO A CA  
510  C C   . PRO A 58  ? 0.1214 0.1043 0.1514 0.0124  0.0152  0.0138  58  PRO A C   
511  O O   . PRO A 58  ? 0.1545 0.1296 0.1827 0.0108  0.0167  0.0165  58  PRO A O   
512  C CB  . PRO A 58  ? 0.1309 0.1098 0.1603 0.0204  0.0177  0.0121  58  PRO A CB  
513  C CG  . PRO A 58  ? 0.1292 0.1125 0.1606 0.0198  0.0172  0.0074  58  PRO A CG  
514  C CD  . PRO A 58  ? 0.1160 0.1089 0.1498 0.0141  0.0145  0.0047  58  PRO A CD  
515  N N   . VAL A 59  ? 0.1145 0.1101 0.1461 0.0134  0.0129  0.0133  59  VAL A N   
516  C CA  . VAL A 59  ? 0.1484 0.1488 0.1793 0.0133  0.0120  0.0160  59  VAL A CA  
517  C C   . VAL A 59  ? 0.1182 0.1151 0.1497 0.0068  0.0116  0.0147  59  VAL A C   
518  O O   . VAL A 59  ? 0.1240 0.1190 0.1541 0.0062  0.0123  0.0177  59  VAL A O   
519  C CB  . VAL A 59  ? 0.1074 0.1229 0.1398 0.0155  0.0098  0.0147  59  VAL A CB  
520  C CG1 . VAL A 59  ? 0.0994 0.1206 0.1349 0.0109  0.0083  0.0092  59  VAL A CG1 
521  C CG2 . VAL A 59  ? 0.1560 0.1773 0.1873 0.0157  0.0090  0.0170  59  VAL A CG2 
522  N N   . LEU A 60  ? 0.1060 0.1022 0.1392 0.0023  0.0108  0.0107  60  LEU A N   
523  C CA  . LEU A 60  ? 0.1027 0.0956 0.1363 -0.0029 0.0105  0.0099  60  LEU A CA  
524  C C   . LEU A 60  ? 0.1374 0.1200 0.1697 -0.0045 0.0127  0.0117  60  LEU A C   
525  O O   . LEU A 60  ? 0.1354 0.1168 0.1676 -0.0070 0.0131  0.0133  60  LEU A O   
526  C CB  . LEU A 60  ? 0.1082 0.1024 0.1433 -0.0066 0.0094  0.0060  60  LEU A CB  
527  C CG  . LEU A 60  ? 0.1095 0.1009 0.1449 -0.0111 0.0091  0.0053  60  LEU A CG  
528  C CD1 . LEU A 60  ? 0.1368 0.1328 0.1728 -0.0116 0.0084  0.0068  60  LEU A CD1 
529  C CD2 . LEU A 60  ? 0.1174 0.1099 0.1533 -0.0136 0.0081  0.0022  60  LEU A CD2 
530  N N   . ILE A 61  ? 0.1302 0.1055 0.1615 -0.0033 0.0143  0.0110  61  ILE A N   
531  C CA  . ILE A 61  ? 0.1679 0.1321 0.1977 -0.0055 0.0169  0.0120  61  ILE A CA  
532  C C   . ILE A 61  ? 0.1436 0.1046 0.1716 -0.0035 0.0189  0.0171  61  ILE A C   
533  O O   . ILE A 61  ? 0.1432 0.0994 0.1710 -0.0076 0.0204  0.0180  61  ILE A O   
534  C CB  . ILE A 61  ? 0.1417 0.0978 0.1702 -0.0037 0.0189  0.0102  61  ILE A CB  
535  C CG1 . ILE A 61  ? 0.1351 0.0943 0.1649 -0.0067 0.0173  0.0052  61  ILE A CG1 
536  C CG2 . ILE A 61  ? 0.1760 0.1191 0.2027 -0.0063 0.0223  0.0110  61  ILE A CG2 
537  C CD1 . ILE A 61  ? 0.1317 0.0842 0.1601 -0.0043 0.0192  0.0029  61  ILE A CD1 
538  N N   . ASP A 62  ? 0.1309 0.0952 0.1575 0.0028  0.0190  0.0204  62  ASP A N   
539  C CA  . ASP A 62  ? 0.1635 0.1256 0.1875 0.0055  0.0209  0.0261  62  ASP A CA  
540  C C   . ASP A 62  ? 0.1848 0.1523 0.2099 0.0011  0.0200  0.0266  62  ASP A C   
541  O O   . ASP A 62  ? 0.1683 0.1302 0.1918 -0.0007 0.0225  0.0299  62  ASP A O   
542  C CB  . ASP A 62  ? 0.1646 0.1348 0.1873 0.0131  0.0200  0.0292  62  ASP A CB  
543  C CG  . ASP A 62  ? 0.2484 0.2121 0.2692 0.0193  0.0220  0.0309  62  ASP A CG  
544  O OD1 . ASP A 62  ? 0.2433 0.1930 0.2625 0.0181  0.0252  0.0312  62  ASP A OD1 
545  O OD2 . ASP A 62  ? 0.1938 0.1668 0.2146 0.0255  0.0206  0.0316  62  ASP A OD2 
546  N N   . GLN A 63  ? 0.1216 0.0998 0.1491 -0.0003 0.0168  0.0235  63  GLN A N   
547  C CA  . GLN A 63  ? 0.1245 0.1085 0.1528 -0.0033 0.0161  0.0239  63  GLN A CA  
548  C C   . GLN A 63  ? 0.1182 0.0978 0.1483 -0.0096 0.0168  0.0221  63  GLN A C   
549  O O   . GLN A 63  ? 0.1645 0.1448 0.1946 -0.0119 0.0180  0.0240  63  GLN A O   
550  C CB  . GLN A 63  ? 0.1525 0.1477 0.1826 -0.0029 0.0130  0.0207  63  GLN A CB  
551  C CG  . GLN A 63  ? 0.1382 0.1406 0.1671 0.0025  0.0120  0.0215  63  GLN A CG  
552  C CD  . GLN A 63  ? 0.1406 0.1529 0.1716 0.0014  0.0095  0.0173  63  GLN A CD  
553  O OE1 . GLN A 63  ? 0.1617 0.1788 0.1930 -0.0003 0.0088  0.0165  63  GLN A OE1 
554  N NE2 . GLN A 63  ? 0.1175 0.1323 0.1498 0.0022  0.0084  0.0144  63  GLN A NE2 
555  N N   . ILE A 64  ? 0.1347 0.1113 0.1663 -0.0123 0.0161  0.0182  64  ILE A N   
556  C CA  . ILE A 64  ? 0.1395 0.1137 0.1728 -0.0182 0.0166  0.0161  64  ILE A CA  
557  C C   . ILE A 64  ? 0.1793 0.1446 0.2112 -0.0204 0.0202  0.0187  64  ILE A C   
558  O O   . ILE A 64  ? 0.1555 0.1221 0.1888 -0.0249 0.0212  0.0190  64  ILE A O   
559  C CB  . ILE A 64  ? 0.1392 0.1117 0.1734 -0.0201 0.0154  0.0116  64  ILE A CB  
560  C CG1 . ILE A 64  ? 0.1186 0.0995 0.1541 -0.0190 0.0124  0.0094  64  ILE A CG1 
561  C CG2 . ILE A 64  ? 0.1527 0.1232 0.1883 -0.0261 0.0160  0.0092  64  ILE A CG2 
562  C CD1 . ILE A 64  ? 0.1677 0.1477 0.2034 -0.0204 0.0113  0.0057  64  ILE A CD1 
563  N N   . GLN A 65  ? 0.1765 0.1327 0.2057 -0.0171 0.0225  0.0209  65  GLN A N   
564  C CA  . GLN A 65  ? 0.1467 0.0917 0.1738 -0.0190 0.0268  0.0239  65  GLN A CA  
565  C C   . GLN A 65  ? 0.1490 0.0971 0.1750 -0.0185 0.0283  0.0290  65  GLN A C   
566  O O   . GLN A 65  ? 0.1907 0.1346 0.2169 -0.0235 0.0311  0.0302  65  GLN A O   
567  C CB  . GLN A 65  ? 0.1569 0.0911 0.1807 -0.0139 0.0293  0.0258  65  GLN A CB  
568  C CG  . GLN A 65  ? 0.1622 0.0909 0.1867 -0.0153 0.0292  0.0207  65  GLN A CG  
569  C CD  . GLN A 65  ? 0.2510 0.1690 0.2721 -0.0094 0.0320  0.0228  65  GLN A CD  
570  O OE1 . GLN A 65  ? 0.2986 0.2215 0.3188 -0.0022 0.0308  0.0252  65  GLN A OE1 
571  N NE2 . GLN A 65  ? 0.3278 0.2313 0.3472 -0.0122 0.0361  0.0217  65  GLN A NE2 
572  N N   . GLU A 66  ? 0.1447 0.1011 0.1696 -0.0128 0.0264  0.0317  66  GLU A N   
573  C CA  . GLU A 66  ? 0.1620 0.1221 0.1850 -0.0117 0.0278  0.0366  66  GLU A CA  
574  C C   . GLU A 66  ? 0.1858 0.1537 0.2120 -0.0174 0.0270  0.0346  66  GLU A C   
575  O O   . GLU A 66  ? 0.1724 0.1393 0.1979 -0.0201 0.0298  0.0377  66  GLU A O   
576  C CB  . GLU A 66  ? 0.1592 0.1285 0.1803 -0.0046 0.0257  0.0389  66  GLU A CB  
577  C CG  . GLU A 66  ? 0.2943 0.2663 0.3120 -0.0021 0.0277  0.0449  66  GLU A CG  
578  C CD  . GLU A 66  ? 0.3116 0.2929 0.3265 0.0054  0.0258  0.0473  66  GLU A CD  
579  O OE1 . GLU A 66  ? 0.3337 0.3199 0.3455 0.0079  0.0269  0.0519  66  GLU A OE1 
580  O OE2 . GLU A 66  ? 0.2317 0.2165 0.2477 0.0086  0.0232  0.0444  66  GLU A OE2 
581  N N   . TYR A 67  ? 0.1443 0.1199 0.1739 -0.0191 0.0235  0.0295  67  TYR A N   
582  C CA  . TYR A 67  ? 0.1551 0.1382 0.1880 -0.0238 0.0228  0.0275  67  TYR A CA  
583  C C   . TYR A 67  ? 0.1667 0.1442 0.2014 -0.0305 0.0252  0.0263  67  TYR A C   
584  O O   . TYR A 67  ? 0.1813 0.1628 0.2176 -0.0343 0.0268  0.0272  67  TYR A O   
585  C CB  . TYR A 67  ? 0.1299 0.1209 0.1655 -0.0233 0.0189  0.0229  67  TYR A CB  
586  C CG  . TYR A 67  ? 0.1389 0.1384 0.1738 -0.0190 0.0169  0.0231  67  TYR A CG  
587  C CD1 . TYR A 67  ? 0.1242 0.1319 0.1601 -0.0194 0.0168  0.0233  67  TYR A CD1 
588  C CD2 . TYR A 67  ? 0.1051 0.1050 0.1385 -0.0147 0.0154  0.0225  67  TYR A CD2 
589  C CE1 . TYR A 67  ? 0.1178 0.1328 0.1528 -0.0158 0.0153  0.0226  67  TYR A CE1 
590  C CE2 . TYR A 67  ? 0.1688 0.1768 0.2016 -0.0117 0.0137  0.0218  67  TYR A CE2 
591  C CZ  . TYR A 67  ? 0.1412 0.1562 0.1747 -0.0123 0.0137  0.0216  67  TYR A CZ  
592  O OH  . TYR A 67  ? 0.1598 0.1822 0.1925 -0.0097 0.0123  0.0200  67  TYR A OH  
593  N N   . ALA A 68  ? 0.1362 0.1059 0.1711 -0.0323 0.0255  0.0234  68  ALA A N   
594  C CA  . ALA A 68  ? 0.1736 0.1384 0.2102 -0.0395 0.0277  0.0210  68  ALA A CA  
595  C C   . ALA A 68  ? 0.2101 0.1663 0.2447 -0.0422 0.0327  0.0251  68  ALA A C   
596  O O   . ALA A 68  ? 0.2280 0.1849 0.2650 -0.0492 0.0349  0.0238  68  ALA A O   
597  C CB  . ALA A 68  ? 0.1883 0.1452 0.2243 -0.0401 0.0274  0.0171  68  ALA A CB  
598  N N   . GLN A 69  ? 0.1918 0.1407 0.2222 -0.0368 0.0348  0.0304  69  GLN A N   
599  C CA  . GLN A 69  ? 0.2239 0.1630 0.2513 -0.0385 0.0401  0.0355  69  GLN A CA  
600  C C   . GLN A 69  ? 0.2489 0.1971 0.2762 -0.0386 0.0410  0.0396  69  GLN A C   
601  O O   . GLN A 69  ? 0.3008 0.2419 0.3253 -0.0400 0.0457  0.0447  69  GLN A O   
602  C CB  . GLN A 69  ? 0.2863 0.2133 0.3084 -0.0316 0.0424  0.0401  69  GLN A CB  
603  C CG  . GLN A 69  ? 0.3190 0.2343 0.3406 -0.0321 0.0432  0.0363  69  GLN A CG  
604  C CD  . GLN A 69  ? 0.4993 0.4066 0.5165 -0.0232 0.0441  0.0402  69  GLN A CD  
605  O OE1 . GLN A 69  ? 0.5479 0.4576 0.5619 -0.0169 0.0445  0.0462  69  GLN A OE1 
606  N NE2 . GLN A 69  ? 0.4327 0.3315 0.4495 -0.0224 0.0444  0.0365  69  GLN A NE2 
607  N N   . GLY A 70  ? 0.2274 0.1904 0.2574 -0.0370 0.0369  0.0377  70  GLY A N   
608  C CA  . GLY A 70  ? 0.2664 0.2390 0.2962 -0.0365 0.0375  0.0409  70  GLY A CA  
609  C C   . GLY A 70  ? 0.3049 0.2775 0.3296 -0.0293 0.0382  0.0468  70  GLY A C   
610  O O   . GLY A 70  ? 0.3608 0.3387 0.3839 -0.0291 0.0402  0.0507  70  GLY A O   
611  N N   . LYS A 71  ? 0.3113 0.2793 0.3331 -0.0231 0.0367  0.0475  71  LYS A N   
612  C CA  . LYS A 71  ? 0.2972 0.2661 0.3139 -0.0157 0.0372  0.0532  71  LYS A CA  
613  C C   . LYS A 71  ? 0.3085 0.2912 0.3256 -0.0106 0.0325  0.0509  71  LYS A C   
614  O O   . LYS A 71  ? 0.3384 0.3256 0.3514 -0.0048 0.0324  0.0549  71  LYS A O   
615  C CB  . LYS A 71  ? 0.2646 0.2204 0.2776 -0.0113 0.0391  0.0561  71  LYS A CB  
616  C CG  . LYS A 71  ? 0.3814 0.3206 0.3925 -0.0154 0.0448  0.0592  71  LYS A CG  
617  C CD  . LYS A 71  ? 0.4724 0.3983 0.4804 -0.0104 0.0463  0.0607  71  LYS A CD  
618  C CE  . LYS A 71  ? 0.5826 0.4894 0.5880 -0.0143 0.0527  0.0634  71  LYS A CE  
619  N NZ  . LYS A 71  ? 0.5948 0.4882 0.5975 -0.0091 0.0542  0.0639  71  LYS A NZ  
620  N N   . ALA A 72  ? 0.2090 0.1983 0.2305 -0.0127 0.0288  0.0446  72  ALA A N   
621  C CA  . ALA A 72  ? 0.2018 0.2022 0.2237 -0.0087 0.0248  0.0417  72  ALA A CA  
622  C C   . ALA A 72  ? 0.2784 0.2898 0.3002 -0.0089 0.0248  0.0421  72  ALA A C   
623  O O   . ALA A 72  ? 0.2784 0.2930 0.3033 -0.0133 0.0251  0.0400  72  ALA A O   
624  C CB  . ALA A 72  ? 0.1975 0.1993 0.2237 -0.0110 0.0217  0.0353  72  ALA A CB  
625  N N   . LYS A 73  ? 0.1772 0.1956 0.1952 -0.0037 0.0242  0.0446  73  LYS A N   
626  C CA  . LYS A 73  ? 0.1417 0.1714 0.1588 -0.0032 0.0241  0.0443  73  LYS A CA  
627  C C   . LYS A 73  ? 0.1891 0.2273 0.2086 -0.0023 0.0203  0.0378  73  LYS A C   
628  O O   . LYS A 73  ? 0.2069 0.2508 0.2243 0.0017  0.0183  0.0367  73  LYS A O   
629  C CB  . LYS A 73  ? 0.2154 0.2489 0.2267 0.0017  0.0258  0.0504  73  LYS A CB  
630  C CG  . LYS A 73  ? 0.4582 0.5022 0.4678 0.0015  0.0268  0.0511  73  LYS A CG  
631  C CD  . LYS A 73  ? 0.6629 0.7047 0.6758 -0.0045 0.0293  0.0509  73  LYS A CD  
632  C CE  . LYS A 73  ? 0.7100 0.7643 0.7240 -0.0050 0.0288  0.0477  73  LYS A CE  
633  N NZ  . LYS A 73  ? 0.7519 0.8122 0.7677 -0.0031 0.0248  0.0409  73  LYS A NZ  
634  N N   . ASP A 74  ? 0.1796 0.2187 0.2033 -0.0060 0.0195  0.0334  74  ASP A N   
635  C CA  . ASP A 74  ? 0.1380 0.1816 0.1640 -0.0057 0.0166  0.0272  74  ASP A CA  
636  C C   . ASP A 74  ? 0.1309 0.1842 0.1566 -0.0051 0.0168  0.0252  74  ASP A C   
637  O O   . ASP A 74  ? 0.1539 0.2090 0.1815 -0.0073 0.0183  0.0254  74  ASP A O   
638  C CB  . ASP A 74  ? 0.1072 0.1449 0.1375 -0.0091 0.0157  0.0242  74  ASP A CB  
639  C CG  . ASP A 74  ? 0.1156 0.1557 0.1479 -0.0088 0.0134  0.0187  74  ASP A CG  
640  O OD1 . ASP A 74  ? 0.1646 0.2112 0.1964 -0.0076 0.0131  0.0162  74  ASP A OD1 
641  O OD2 . ASP A 74  ? 0.1550 0.1895 0.1890 -0.0100 0.0122  0.0169  74  ASP A OD2 
642  N N   . VAL A 75  ? 0.1823 0.2427 0.2057 -0.0022 0.0154  0.0227  75  VAL A N   
643  C CA  . VAL A 75  ? 0.2014 0.2711 0.2233 -0.0013 0.0160  0.0208  75  VAL A CA  
644  C C   . VAL A 75  ? 0.2065 0.2765 0.2320 -0.0030 0.0157  0.0156  75  VAL A C   
645  O O   . VAL A 75  ? 0.2142 0.2889 0.2402 -0.0033 0.0174  0.0155  75  VAL A O   
646  C CB  . VAL A 75  ? 0.2357 0.3139 0.2539 0.0019  0.0146  0.0188  75  VAL A CB  
647  C CG1 . VAL A 75  ? 0.2788 0.3579 0.2930 0.0050  0.0151  0.0251  75  VAL A CG1 
648  C CG2 . VAL A 75  ? 0.3421 0.4193 0.3623 0.0014  0.0122  0.0129  75  VAL A CG2 
649  N N   A PHE A 76  ? 0.1593 0.2242 0.1873 -0.0039 0.0140  0.0117  76  PHE A N   
650  N N   B PHE A 76  ? 0.1593 0.2242 0.1873 -0.0039 0.0140  0.0117  76  PHE A N   
651  C CA  A PHE A 76  ? 0.1382 0.2019 0.1690 -0.0047 0.0141  0.0077  76  PHE A CA  
652  C CA  B PHE A 76  ? 0.1382 0.2019 0.1690 -0.0047 0.0141  0.0077  76  PHE A CA  
653  C C   A PHE A 76  ? 0.1906 0.2525 0.2245 -0.0064 0.0152  0.0104  76  PHE A C   
654  C C   B PHE A 76  ? 0.1906 0.2525 0.2245 -0.0064 0.0152  0.0104  76  PHE A C   
655  O O   A PHE A 76  ? 0.1686 0.2345 0.2042 -0.0060 0.0162  0.0090  76  PHE A O   
656  O O   B PHE A 76  ? 0.1686 0.2345 0.2042 -0.0060 0.0162  0.0090  76  PHE A O   
657  C CB  A PHE A 76  ? 0.1796 0.2372 0.2118 -0.0053 0.0124  0.0038  76  PHE A CB  
658  C CB  B PHE A 76  ? 0.1796 0.2372 0.2118 -0.0053 0.0124  0.0038  76  PHE A CB  
659  C CG  A PHE A 76  ? 0.2677 0.3284 0.2982 -0.0045 0.0119  -0.0013 76  PHE A CG  
660  C CG  B PHE A 76  ? 0.2677 0.3284 0.2982 -0.0045 0.0119  -0.0013 76  PHE A CG  
661  C CD1 A PHE A 76  ? 0.2800 0.3439 0.3084 -0.0041 0.0108  -0.0016 76  PHE A CD1 
662  C CD1 B PHE A 76  ? 0.2800 0.3439 0.3084 -0.0041 0.0108  -0.0016 76  PHE A CD1 
663  C CD2 A PHE A 76  ? 0.3375 0.3980 0.3683 -0.0042 0.0128  -0.0061 76  PHE A CD2 
664  C CD2 B PHE A 76  ? 0.3375 0.3980 0.3683 -0.0042 0.0128  -0.0061 76  PHE A CD2 
665  C CE1 A PHE A 76  ? 0.2760 0.3443 0.3032 -0.0043 0.0103  -0.0071 76  PHE A CE1 
666  C CE1 B PHE A 76  ? 0.2760 0.3443 0.3032 -0.0043 0.0103  -0.0071 76  PHE A CE1 
667  C CE2 A PHE A 76  ? 0.3690 0.4315 0.3981 -0.0044 0.0128  -0.0117 76  PHE A CE2 
668  C CE2 B PHE A 76  ? 0.3690 0.4315 0.3981 -0.0044 0.0128  -0.0117 76  PHE A CE2 
669  C CZ  A PHE A 76  ? 0.3346 0.4017 0.3621 -0.0050 0.0114  -0.0125 76  PHE A CZ  
670  C CZ  B PHE A 76  ? 0.3346 0.4017 0.3621 -0.0050 0.0114  -0.0125 76  PHE A CZ  
671  N N   . LEU A 77  ? 0.1711 0.2278 0.2059 -0.0085 0.0152  0.0140  77  LEU A N   
672  C CA  . LEU A 77  ? 0.2085 0.2647 0.2465 -0.0111 0.0163  0.0159  77  LEU A CA  
673  C C   . LEU A 77  ? 0.2066 0.2699 0.2442 -0.0116 0.0188  0.0185  77  LEU A C   
674  O O   . LEU A 77  ? 0.1805 0.2482 0.2213 -0.0130 0.0198  0.0182  77  LEU A O   
675  C CB  . LEU A 77  ? 0.1876 0.2360 0.2261 -0.0137 0.0162  0.0185  77  LEU A CB  
676  C CG  . LEU A 77  ? 0.2858 0.3334 0.3280 -0.0175 0.0168  0.0188  77  LEU A CG  
677  C CD1 . LEU A 77  ? 0.2147 0.2655 0.2600 -0.0167 0.0152  0.0152  77  LEU A CD1 
678  C CD2 . LEU A 77  ? 0.2482 0.2870 0.2902 -0.0199 0.0166  0.0201  77  LEU A CD2 
679  N N   . GLU A 78  ? 0.2138 0.2794 0.2474 -0.0103 0.0200  0.0213  78  GLU A N   
680  C CA  . GLU A 78  ? 0.2050 0.2780 0.2376 -0.0106 0.0227  0.0240  78  GLU A CA  
681  C C   . GLU A 78  ? 0.1969 0.2784 0.2306 -0.0086 0.0229  0.0199  78  GLU A C   
682  O O   . GLU A 78  ? 0.2335 0.3216 0.2692 -0.0097 0.0249  0.0207  78  GLU A O   
683  C CB  . GLU A 78  ? 0.2649 0.3392 0.2919 -0.0085 0.0238  0.0281  78  GLU A CB  
684  C CG  . GLU A 78  ? 0.5011 0.5695 0.5267 -0.0108 0.0265  0.0345  78  GLU A CG  
685  C CD  . GLU A 78  ? 0.6409 0.7124 0.6694 -0.0149 0.0295  0.0363  78  GLU A CD  
686  O OE1 . GLU A 78  ? 0.7153 0.7820 0.7479 -0.0190 0.0298  0.0357  78  GLU A OE1 
687  O OE2 . GLU A 78  ? 0.6834 0.7632 0.7100 -0.0143 0.0318  0.0380  78  GLU A OE2 
688  N N   . ALA A 79  ? 0.2007 0.2824 0.2335 -0.0059 0.0210  0.0151  79  ALA A N   
689  C CA  . ALA A 79  ? 0.1428 0.2303 0.1765 -0.0038 0.0215  0.0107  79  ALA A CA  
690  C C   . ALA A 79  ? 0.1849 0.2715 0.2236 -0.0043 0.0214  0.0093  79  ALA A C   
691  O O   . ALA A 79  ? 0.2155 0.3085 0.2559 -0.0023 0.0227  0.0072  79  ALA A O   
692  C CB  . ALA A 79  ? 0.1802 0.2663 0.2117 -0.0015 0.0201  0.0053  79  ALA A CB  
693  N N   . ILE A 80  ? 0.1496 0.2294 0.1908 -0.0064 0.0199  0.0105  80  ILE A N   
694  C CA  . ILE A 80  ? 0.1545 0.2356 0.2003 -0.0068 0.0196  0.0097  80  ILE A CA  
695  C C   . ILE A 80  ? 0.1527 0.2406 0.2014 -0.0099 0.0215  0.0129  80  ILE A C   
696  O O   . ILE A 80  ? 0.1428 0.2385 0.1951 -0.0091 0.0222  0.0120  80  ILE A O   
697  C CB  . ILE A 80  ? 0.1348 0.2071 0.1816 -0.0079 0.0173  0.0092  80  ILE A CB  
698  C CG1 . ILE A 80  ? 0.1937 0.2602 0.2383 -0.0050 0.0161  0.0056  80  ILE A CG1 
699  C CG2 . ILE A 80  ? 0.1250 0.2002 0.1763 -0.0088 0.0168  0.0094  80  ILE A CG2 
700  C CD1 . ILE A 80  ? 0.2599 0.3189 0.3055 -0.0055 0.0142  0.0048  80  ILE A CD1 
701  N N   . ARG A 81  ? 0.1535 0.2387 0.2007 -0.0135 0.0226  0.0168  81  ARG A N   
702  C CA  . ARG A 81  ? 0.1931 0.2828 0.2433 -0.0180 0.0247  0.0196  81  ARG A CA  
703  C C   . ARG A 81  ? 0.1418 0.2427 0.1924 -0.0174 0.0276  0.0205  81  ARG A C   
704  O O   . ARG A 81  ? 0.1810 0.2899 0.2359 -0.0200 0.0291  0.0208  81  ARG A O   
705  C CB  . ARG A 81  ? 0.1884 0.2697 0.2362 -0.0217 0.0258  0.0237  81  ARG A CB  
706  C CG  . ARG A 81  ? 0.2965 0.3804 0.3468 -0.0275 0.0289  0.0266  81  ARG A CG  
707  C CD  . ARG A 81  ? 0.4275 0.5009 0.4743 -0.0305 0.0309  0.0309  81  ARG A CD  
708  N NE  . ARG A 81  ? 0.5099 0.5735 0.5577 -0.0327 0.0292  0.0297  81  ARG A NE  
709  C CZ  . ARG A 81  ? 0.5614 0.6255 0.6137 -0.0379 0.0293  0.0279  81  ARG A CZ  
710  N NH1 . ARG A 81  ? 0.5060 0.5806 0.5626 -0.0414 0.0310  0.0272  81  ARG A NH1 
711  N NH2 . ARG A 81  ? 0.5454 0.6006 0.5978 -0.0395 0.0278  0.0265  81  ARG A NH2 
712  N N   . LYS A 82  ? 0.1568 0.2597 0.2029 -0.0142 0.0284  0.0207  82  LYS A N   
713  C CA  . LYS A 82  ? 0.1206 0.2341 0.1660 -0.0139 0.0315  0.0219  82  LYS A CA  
714  C C   . LYS A 82  ? 0.1413 0.2651 0.1913 -0.0117 0.0319  0.0184  82  LYS A C   
715  O O   . LYS A 82  ? 0.1422 0.2642 0.1936 -0.0081 0.0297  0.0143  82  LYS A O   
716  C CB  . LYS A 82  ? 0.1851 0.3001 0.2244 -0.0101 0.0318  0.0216  82  LYS A CB  
717  C CG  . LYS A 82  ? 0.3386 0.4478 0.3725 -0.0109 0.0323  0.0262  82  LYS A CG  
718  C CD  . LYS A 82  ? 0.2869 0.4007 0.3154 -0.0065 0.0318  0.0243  82  LYS A CD  
719  C CE  . LYS A 82  ? 0.3509 0.4617 0.3735 -0.0058 0.0321  0.0291  82  LYS A CE  
720  N NZ  . LYS A 82  ? 0.3197 0.4396 0.3370 -0.0020 0.0323  0.0273  82  LYS A NZ  
721  N N   . ASP A 83  ? 0.1356 0.2700 0.1875 -0.0136 0.0350  0.0201  83  ASP A N   
722  C CA  . ASP A 83  ? 0.1182 0.2646 0.1733 -0.0100 0.0361  0.0169  83  ASP A CA  
723  C C   . ASP A 83  ? 0.1402 0.2856 0.1906 -0.0040 0.0356  0.0132  83  ASP A C   
724  O O   . ASP A 83  ? 0.1077 0.2507 0.1524 -0.0039 0.0361  0.0145  83  ASP A O   
725  C CB  . ASP A 83  ? 0.1609 0.3197 0.2178 -0.0131 0.0401  0.0196  83  ASP A CB  
726  C CG  . ASP A 83  ? 0.2335 0.4064 0.2950 -0.0095 0.0413  0.0163  83  ASP A CG  
727  O OD1 . ASP A 83  ? 0.1936 0.3691 0.2526 -0.0036 0.0415  0.0129  83  ASP A OD1 
728  O OD2 . ASP A 83  ? 0.2577 0.4398 0.3254 -0.0127 0.0423  0.0169  83  ASP A OD2 
729  N N   . PRO A 84  ? 0.1814 0.3282 0.2338 0.0009  0.0346  0.0084  84  PRO A N   
730  C CA  . PRO A 84  ? 0.1232 0.2676 0.1709 0.0058  0.0345  0.0040  84  PRO A CA  
731  C C   . PRO A 84  ? 0.1238 0.2777 0.1677 0.0066  0.0375  0.0041  84  PRO A C   
732  O O   . PRO A 84  ? 0.1727 0.3242 0.2113 0.0087  0.0372  0.0012  84  PRO A O   
733  C CB  . PRO A 84  ? 0.1724 0.3176 0.2236 0.0110  0.0342  -0.0003 84  PRO A CB  
734  C CG  . PRO A 84  ? 0.1405 0.2835 0.1968 0.0088  0.0322  0.0020  84  PRO A CG  
735  C CD  . PRO A 84  ? 0.2089 0.3581 0.2672 0.0026  0.0334  0.0068  84  PRO A CD  
736  N N   . ASP A 85  ? 0.1085 0.2740 0.1549 0.0048  0.0403  0.0069  85  ASP A N   
737  C CA  . ASP A 85  ? 0.1377 0.3127 0.1798 0.0054  0.0434  0.0076  85  ASP A CA  
738  C C   . ASP A 85  ? 0.1457 0.3158 0.1814 0.0028  0.0432  0.0116  85  ASP A C   
739  O O   . ASP A 85  ? 0.1336 0.3100 0.1638 0.0045  0.0449  0.0114  85  ASP A O   
740  C CB  . ASP A 85  ? 0.1509 0.3392 0.1972 0.0030  0.0469  0.0105  85  ASP A CB  
741  C CG  . ASP A 85  ? 0.2474 0.4452 0.2993 0.0074  0.0478  0.0062  85  ASP A CG  
742  O OD1 . ASP A 85  ? 0.2285 0.4225 0.2793 0.0132  0.0466  0.0008  85  ASP A OD1 
743  O OD2 . ASP A 85  ? 0.3287 0.5380 0.3859 0.0052  0.0500  0.0082  85  ASP A OD2 
744  N N   . ASP A 86  ? 0.1334 0.2932 0.1694 -0.0007 0.0413  0.0153  86  ASP A N   
745  C CA  . ASP A 86  ? 0.1285 0.2831 0.1586 -0.0024 0.0411  0.0198  86  ASP A CA  
746  C C   . ASP A 86  ? 0.1873 0.3338 0.2137 0.0002  0.0377  0.0165  86  ASP A C   
747  O O   . ASP A 86  ? 0.1810 0.3243 0.2024 0.0000  0.0371  0.0198  86  ASP A O   
748  C CB  . ASP A 86  ? 0.1789 0.3265 0.2113 -0.0078 0.0416  0.0258  86  ASP A CB  
749  C CG  . ASP A 86  ? 0.2371 0.3931 0.2719 -0.0118 0.0458  0.0300  86  ASP A CG  
750  O OD1 . ASP A 86  ? 0.3210 0.4880 0.3535 -0.0103 0.0487  0.0302  86  ASP A OD1 
751  O OD2 . ASP A 86  ? 0.3105 0.4622 0.3492 -0.0169 0.0465  0.0328  86  ASP A OD2 
752  N N   . LEU A 87  ? 0.1263 0.2696 0.1550 0.0028  0.0356  0.0102  87  LEU A N   
753  C CA  . LEU A 87  ? 0.1113 0.2469 0.1373 0.0043  0.0327  0.0065  87  LEU A CA  
754  C C   . LEU A 87  ? 0.1159 0.2578 0.1355 0.0067  0.0331  0.0036  87  LEU A C   
755  O O   . LEU A 87  ? 0.1457 0.2963 0.1639 0.0090  0.0351  0.0002  87  LEU A O   
756  C CB  . LEU A 87  ? 0.1153 0.2452 0.1450 0.0063  0.0313  0.0007  87  LEU A CB  
757  C CG  . LEU A 87  ? 0.1176 0.2396 0.1524 0.0042  0.0297  0.0028  87  LEU A CG  
758  C CD1 . LEU A 87  ? 0.1315 0.2499 0.1695 0.0073  0.0291  -0.0021 87  LEU A CD1 
759  C CD2 . LEU A 87  ? 0.1836 0.2960 0.2167 0.0019  0.0272  0.0050  87  LEU A CD2 
760  N N   . GLU A 88  ? 0.1164 0.2548 0.1322 0.0064  0.0310  0.0046  88  GLU A N   
761  C CA  . GLU A 88  ? 0.1305 0.2753 0.1408 0.0085  0.0304  0.0004  88  GLU A CA  
762  C C   . GLU A 88  ? 0.1449 0.2859 0.1564 0.0096  0.0294  -0.0086 88  GLU A C   
763  O O   . GLU A 88  ? 0.1349 0.2660 0.1507 0.0088  0.0282  -0.0103 88  GLU A O   
764  C CB  . GLU A 88  ? 0.1969 0.3401 0.2034 0.0082  0.0282  0.0040  88  GLU A CB  
765  C CG  . GLU A 88  ? 0.1810 0.3246 0.1858 0.0074  0.0297  0.0135  88  GLU A CG  
766  C CD  . GLU A 88  ? 0.3124 0.4505 0.3149 0.0077  0.0277  0.0180  88  GLU A CD  
767  O OE1 . GLU A 88  ? 0.2891 0.4235 0.2923 0.0079  0.0247  0.0138  88  GLU A OE1 
768  O OE2 . GLU A 88  ? 0.3556 0.4929 0.3555 0.0076  0.0294  0.0260  88  GLU A OE2 
769  N N   . LYS A 89  ? 0.1346 0.2834 0.1420 0.0113  0.0301  -0.0145 89  LYS A N   
770  C CA  . LYS A 89  ? 0.1848 0.3288 0.1925 0.0116  0.0296  -0.0236 89  LYS A CA  
771  C C   . LYS A 89  ? 0.1534 0.2880 0.1623 0.0094  0.0266  -0.0245 89  LYS A C   
772  O O   . LYS A 89  ? 0.1939 0.3183 0.2059 0.0088  0.0264  -0.0286 89  LYS A O   
773  C CB  . LYS A 89  ? 0.2199 0.3745 0.2220 0.0128  0.0306  -0.0302 89  LYS A CB  
774  C CG  . LYS A 89  ? 0.2753 0.4405 0.2756 0.0152  0.0338  -0.0301 89  LYS A CG  
775  C CD  . LYS A 89  ? 0.3458 0.5226 0.3397 0.0161  0.0344  -0.0365 89  LYS A CD  
776  C CE  . LYS A 89  ? 0.3959 0.5859 0.3865 0.0183  0.0374  -0.0342 89  LYS A CE  
777  N NZ  . LYS A 89  ? 0.3998 0.5882 0.3944 0.0204  0.0406  -0.0365 89  LYS A NZ  
778  N N   . GLU A 90  ? 0.1330 0.2708 0.1395 0.0085  0.0246  -0.0201 90  GLU A N   
779  C CA  . GLU A 90  ? 0.1473 0.2777 0.1551 0.0066  0.0218  -0.0207 90  GLU A CA  
780  C C   . GLU A 90  ? 0.2048 0.3227 0.2180 0.0054  0.0213  -0.0172 90  GLU A C   
781  O O   . GLU A 90  ? 0.1739 0.2835 0.1892 0.0038  0.0200  -0.0202 90  GLU A O   
782  C CB  . GLU A 90  ? 0.1706 0.3076 0.1750 0.0070  0.0199  -0.0158 90  GLU A CB  
783  C CG  . GLU A 90  ? 0.3979 0.5479 0.3971 0.0079  0.0192  -0.0206 90  GLU A CG  
784  C CD  . GLU A 90  ? 0.5646 0.7221 0.5601 0.0096  0.0173  -0.0144 90  GLU A CD  
785  O OE1 . GLU A 90  ? 0.5141 0.6642 0.5116 0.0097  0.0165  -0.0076 90  GLU A OE1 
786  O OE2 . GLU A 90  ? 0.5684 0.7395 0.5588 0.0113  0.0168  -0.0163 90  GLU A OE2 
787  N N   . GLU A 91  ? 0.1443 0.2615 0.1595 0.0057  0.0226  -0.0109 91  GLU A N   
788  C CA  . GLU A 91  ? 0.1224 0.2296 0.1425 0.0043  0.0220  -0.0078 91  GLU A CA  
789  C C   . GLU A 91  ? 0.1452 0.2468 0.1685 0.0052  0.0228  -0.0126 91  GLU A C   
790  O O   . GLU A 91  ? 0.1430 0.2353 0.1693 0.0043  0.0217  -0.0128 91  GLU A O   
791  C CB  . GLU A 91  ? 0.1115 0.2207 0.1329 0.0036  0.0232  -0.0004 91  GLU A CB  
792  C CG  . GLU A 91  ? 0.2095 0.3200 0.2278 0.0030  0.0227  0.0057  91  GLU A CG  
793  C CD  . GLU A 91  ? 0.2242 0.3360 0.2431 0.0017  0.0250  0.0127  91  GLU A CD  
794  O OE1 . GLU A 91  ? 0.1761 0.2954 0.1949 0.0021  0.0275  0.0130  91  GLU A OE1 
795  O OE2 . GLU A 91  ? 0.2341 0.3392 0.2537 -0.0001 0.0247  0.0177  91  GLU A OE2 
796  N N   . VAL A 92  ? 0.1471 0.2542 0.1697 0.0074  0.0250  -0.0163 92  VAL A N   
797  C CA  . VAL A 92  ? 0.1738 0.2749 0.1987 0.0093  0.0263  -0.0211 92  VAL A CA  
798  C C   . VAL A 92  ? 0.1807 0.2731 0.2044 0.0083  0.0254  -0.0268 92  VAL A C   
799  O O   . VAL A 92  ? 0.1768 0.2589 0.2028 0.0085  0.0253  -0.0278 92  VAL A O   
800  C CB  . VAL A 92  ? 0.1481 0.2572 0.1719 0.0125  0.0292  -0.0245 92  VAL A CB  
801  C CG1 . VAL A 92  ? 0.2060 0.3074 0.2315 0.0154  0.0308  -0.0297 92  VAL A CG1 
802  C CG2 . VAL A 92  ? 0.1295 0.2480 0.1554 0.0130  0.0305  -0.0186 92  VAL A CG2 
803  N N   . GLU A 93  ? 0.1673 0.2643 0.1871 0.0069  0.0249  -0.0307 93  GLU A N   
804  C CA  . GLU A 93  ? 0.1681 0.2582 0.1870 0.0047  0.0242  -0.0366 93  GLU A CA  
805  C C   . GLU A 93  ? 0.1838 0.2655 0.2052 0.0024  0.0220  -0.0329 93  GLU A C   
806  O O   . GLU A 93  ? 0.2311 0.3024 0.2538 0.0014  0.0224  -0.0359 93  GLU A O   
807  C CB  . GLU A 93  ? 0.2152 0.3151 0.2299 0.0031  0.0236  -0.0410 93  GLU A CB  
808  C CG  . GLU A 93  ? 0.2860 0.3918 0.2977 0.0047  0.0261  -0.0476 93  GLU A CG  
809  C CD  . GLU A 93  ? 0.4511 0.5711 0.4581 0.0040  0.0252  -0.0501 93  GLU A CD  
810  O OE1 . GLU A 93  ? 0.4745 0.6015 0.4785 0.0053  0.0273  -0.0553 93  GLU A OE1 
811  O OE2 . GLU A 93  ? 0.4686 0.5934 0.4749 0.0025  0.0225  -0.0469 93  GLU A OE2 
812  N N   . LYS A 94  ? 0.1628 0.2483 0.1847 0.0018  0.0201  -0.0263 94  LYS A N   
813  C CA  . LYS A 94  ? 0.2167 0.2949 0.2409 0.0000  0.0181  -0.0229 94  LYS A CA  
814  C C   . LYS A 94  ? 0.1647 0.2333 0.1924 0.0006  0.0187  -0.0212 94  LYS A C   
815  O O   . LYS A 94  ? 0.2061 0.2661 0.2350 -0.0008 0.0180  -0.0221 94  LYS A O   
816  C CB  . LYS A 94  ? 0.2308 0.3137 0.2545 -0.0002 0.0166  -0.0160 94  LYS A CB  
817  C CG  . LYS A 94  ? 0.2912 0.3815 0.3119 -0.0005 0.0152  -0.0162 94  LYS A CG  
818  C CD  . LYS A 94  ? 0.4295 0.5216 0.4496 0.0003  0.0144  -0.0083 94  LYS A CD  
819  C CE  . LYS A 94  ? 0.4812 0.5787 0.4988 0.0009  0.0126  -0.0074 94  LYS A CE  
820  N NZ  . LYS A 94  ? 0.5574 0.6664 0.5714 0.0017  0.0124  -0.0123 94  LYS A NZ  
821  N N   . LEU A 95  ? 0.1252 0.1966 0.1545 0.0028  0.0199  -0.0186 95  LEU A N   
822  C CA  . LEU A 95  ? 0.1702 0.2352 0.2028 0.0041  0.0202  -0.0168 95  LEU A CA  
823  C C   . LEU A 95  ? 0.1987 0.2548 0.2308 0.0056  0.0216  -0.0219 95  LEU A C   
824  O O   . LEU A 95  ? 0.1513 0.1987 0.1848 0.0055  0.0212  -0.0209 95  LEU A O   
825  C CB  . LEU A 95  ? 0.2205 0.2929 0.2550 0.0064  0.0216  -0.0142 95  LEU A CB  
826  C CG  . LEU A 95  ? 0.3706 0.4496 0.4066 0.0046  0.0210  -0.0082 95  LEU A CG  
827  C CD1 . LEU A 95  ? 0.4161 0.5031 0.4545 0.0066  0.0229  -0.0070 95  LEU A CD1 
828  C CD2 . LEU A 95  ? 0.4156 0.4885 0.4540 0.0022  0.0191  -0.0045 95  LEU A CD2 
829  N N   . ILE A 96  ? 0.1876 0.2454 0.2175 0.0070  0.0238  -0.0274 96  ILE A N   
830  C CA  . ILE A 96  ? 0.1841 0.2317 0.2130 0.0084  0.0260  -0.0326 96  ILE A CA  
831  C C   . ILE A 96  ? 0.1840 0.2231 0.2118 0.0044  0.0253  -0.0351 96  ILE A C   
832  O O   . ILE A 96  ? 0.2050 0.2328 0.2333 0.0047  0.0262  -0.0353 96  ILE A O   
833  C CB  . ILE A 96  ? 0.2102 0.2615 0.2365 0.0103  0.0288  -0.0388 96  ILE A CB  
834  C CG1 . ILE A 96  ? 0.1911 0.2497 0.2191 0.0149  0.0301  -0.0364 96  ILE A CG1 
835  C CG2 . ILE A 96  ? 0.1997 0.2383 0.2242 0.0107  0.0317  -0.0452 96  ILE A CG2 
836  C CD1 . ILE A 96  ? 0.2818 0.3479 0.3070 0.0165  0.0324  -0.0417 96  ILE A CD1 
837  N N   . GLU A 97  ? 0.1595 0.2049 0.1860 0.0009  0.0236  -0.0365 97  GLU A N   
838  C CA  . GLU A 97  ? 0.1940 0.2339 0.2200 -0.0032 0.0229  -0.0392 97  GLU A CA  
839  C C   . GLU A 97  ? 0.1924 0.2258 0.2207 -0.0040 0.0213  -0.0338 97  GLU A C   
840  O O   . GLU A 97  ? 0.1989 0.2225 0.2272 -0.0058 0.0222  -0.0355 97  GLU A O   
841  C CB  . GLU A 97  ? 0.2156 0.2668 0.2400 -0.0059 0.0211  -0.0411 97  GLU A CB  
842  C CG  . GLU A 97  ? 0.3778 0.4271 0.4023 -0.0102 0.0200  -0.0439 97  GLU A CG  
843  C CD  . GLU A 97  ? 0.6230 0.6860 0.6460 -0.0117 0.0179  -0.0452 97  GLU A CD  
844  O OE1 . GLU A 97  ? 0.6992 0.7646 0.7219 -0.0154 0.0178  -0.0508 97  GLU A OE1 
845  O OE2 . GLU A 97  ? 0.6265 0.6984 0.6487 -0.0090 0.0166  -0.0405 97  GLU A OE2 
846  N N   . PHE A 98  ? 0.1415 0.1799 0.1715 -0.0028 0.0192  -0.0275 98  PHE A N   
847  C CA  . PHE A 98  ? 0.1561 0.1891 0.1882 -0.0034 0.0178  -0.0227 98  PHE A CA  
848  C C   . PHE A 98  ? 0.1608 0.1845 0.1936 -0.0010 0.0193  -0.0222 98  PHE A C   
849  O O   . PHE A 98  ? 0.1548 0.1707 0.1878 -0.0021 0.0191  -0.0211 98  PHE A O   
850  C CB  . PHE A 98  ? 0.1716 0.2112 0.2052 -0.0028 0.0160  -0.0168 98  PHE A CB  
851  C CG  . PHE A 98  ? 0.1870 0.2224 0.2221 -0.0044 0.0142  -0.0130 98  PHE A CG  
852  C CD1 . PHE A 98  ? 0.1469 0.1821 0.1814 -0.0068 0.0128  -0.0130 98  PHE A CD1 
853  C CD2 . PHE A 98  ? 0.1707 0.2034 0.2078 -0.0032 0.0139  -0.0097 98  PHE A CD2 
854  C CE1 . PHE A 98  ? 0.1316 0.1630 0.1674 -0.0080 0.0115  -0.0099 98  PHE A CE1 
855  C CE2 . PHE A 98  ? 0.1332 0.1626 0.1714 -0.0048 0.0124  -0.0068 98  PHE A CE2 
856  C CZ  . PHE A 98  ? 0.1461 0.1742 0.1835 -0.0072 0.0113  -0.0069 98  PHE A CZ  
857  N N   . THR A 99  ? 0.1556 0.1808 0.1886 0.0028  0.0209  -0.0225 99  THR A N   
858  C CA  . THR A 99  ? 0.1614 0.1785 0.1948 0.0064  0.0225  -0.0215 99  THR A CA  
859  C C   . THR A 99  ? 0.1778 0.1825 0.2087 0.0054  0.0250  -0.0258 99  THR A C   
860  O O   . THR A 99  ? 0.1704 0.1659 0.2009 0.0062  0.0256  -0.0236 99  THR A O   
861  C CB  . THR A 99  ? 0.1595 0.1818 0.1937 0.0113  0.0241  -0.0216 99  THR A CB  
862  O OG1 . THR A 99  ? 0.1784 0.2126 0.2150 0.0110  0.0223  -0.0178 99  THR A OG1 
863  C CG2 . THR A 99  ? 0.1541 0.1697 0.1888 0.0162  0.0255  -0.0195 99  THR A CG2 
864  N N   . LYS A 100 ? 0.2062 0.2108 0.2351 0.0034  0.0267  -0.0319 100 LYS A N   
865  C CA  . LYS A 100 ? 0.1712 0.1636 0.1977 0.0013  0.0298  -0.0370 100 LYS A CA  
866  C C   . LYS A 100 ? 0.1750 0.1624 0.2017 -0.0034 0.0287  -0.0360 100 LYS A C   
867  O O   . LYS A 100 ? 0.2286 0.2034 0.2539 -0.0040 0.0312  -0.0366 100 LYS A O   
868  C CB  . LYS A 100 ? 0.2362 0.2322 0.2608 -0.0012 0.0314  -0.0446 100 LYS A CB  
869  C CG  . LYS A 100 ? 0.3366 0.3327 0.3600 0.0033  0.0341  -0.0477 100 LYS A CG  
870  C CD  . LYS A 100 ? 0.4752 0.4717 0.4959 -0.0001 0.0364  -0.0567 100 LYS A CD  
871  C CE  . LYS A 100 ? 0.5808 0.5862 0.6005 0.0035  0.0374  -0.0594 100 LYS A CE  
872  N NZ  . LYS A 100 ? 0.6577 0.6562 0.6775 0.0104  0.0403  -0.0578 100 LYS A NZ  
873  N N   . LEU A 101 ? 0.1893 0.1862 0.2174 -0.0065 0.0255  -0.0345 101 LEU A N   
874  C CA  . LEU A 101 ? 0.1693 0.1630 0.1979 -0.0106 0.0244  -0.0335 101 LEU A CA  
875  C C   . LEU A 101 ? 0.2056 0.1914 0.2346 -0.0085 0.0244  -0.0280 101 LEU A C   
876  O O   . LEU A 101 ? 0.2042 0.1817 0.2323 -0.0110 0.0257  -0.0282 101 LEU A O   
877  C CB  . LEU A 101 ? 0.1818 0.1876 0.2119 -0.0125 0.0209  -0.0318 101 LEU A CB  
878  C CG  . LEU A 101 ? 0.2252 0.2300 0.2564 -0.0156 0.0195  -0.0300 101 LEU A CG  
879  C CD1 . LEU A 101 ? 0.3153 0.3167 0.3458 -0.0206 0.0214  -0.0360 101 LEU A CD1 
880  C CD2 . LEU A 101 ? 0.2250 0.2408 0.2575 -0.0156 0.0162  -0.0271 101 LEU A CD2 
881  N N   . ASN A 102 ? 0.1560 0.1452 0.1861 -0.0040 0.0230  -0.0232 102 ASN A N   
882  C CA  . ASN A 102 ? 0.1418 0.1274 0.1725 -0.0019 0.0221  -0.0178 102 ASN A CA  
883  C C   . ASN A 102 ? 0.1281 0.1052 0.1573 0.0031  0.0247  -0.0164 102 ASN A C   
884  O O   . ASN A 102 ? 0.1509 0.1251 0.1798 0.0054  0.0241  -0.0119 102 ASN A O   
885  C CB  . ASN A 102 ? 0.1366 0.1327 0.1698 -0.0007 0.0189  -0.0136 102 ASN A CB  
886  C CG  . ASN A 102 ? 0.2414 0.2434 0.2757 -0.0048 0.0165  -0.0133 102 ASN A CG  
887  O OD1 . ASN A 102 ? 0.2247 0.2233 0.2587 -0.0072 0.0159  -0.0126 102 ASN A OD1 
888  N ND2 . ASN A 102 ? 0.2123 0.2232 0.2475 -0.0050 0.0154  -0.0134 102 ASN A ND2 
889  N N   . TYR A 103 ? 0.1838 0.1406 0.2867 -0.0568 0.0600  -0.0680 103 TYR A N   
890  C CA  . TYR A 103 ? 0.2636 0.1966 0.3656 -0.0495 0.0706  -0.0618 103 TYR A CA  
891  C C   . TYR A 103 ? 0.2182 0.1259 0.3220 -0.0464 0.0826  -0.0512 103 TYR A C   
892  O O   . TYR A 103 ? 0.2453 0.1394 0.3448 -0.0342 0.0865  -0.0372 103 TYR A O   
893  C CB  . TYR A 103 ? 0.2220 0.1494 0.3286 -0.0566 0.0800  -0.0793 103 TYR A CB  
894  C CG  . TYR A 103 ? 0.2780 0.1805 0.3839 -0.0487 0.0925  -0.0746 103 TYR A CG  
895  C CD1 . TYR A 103 ? 0.3082 0.2164 0.4084 -0.0380 0.0872  -0.0680 103 TYR A CD1 
896  C CD2 . TYR A 103 ? 0.3683 0.2516 0.4760 -0.0486 0.1074  -0.0728 103 TYR A CD2 
897  C CE1 . TYR A 103 ? 0.3156 0.2029 0.4158 -0.0294 0.0989  -0.0635 103 TYR A CE1 
898  C CE2 . TYR A 103 ? 0.4086 0.2720 0.5147 -0.0398 0.1188  -0.0669 103 TYR A CE2 
899  C CZ  . TYR A 103 ? 0.4295 0.2929 0.5327 -0.0303 0.1150  -0.0630 103 TYR A CZ  
900  O OH  . TYR A 103 ? 0.4647 0.3111 0.5660 -0.0202 0.1260  -0.0561 103 TYR A OH  
901  N N   . GLU A 104 ? 0.2160 0.1240 0.3227 -0.0536 0.0869  -0.0555 104 GLU A N   
902  C CA  . GLU A 104 ? 0.2664 0.1541 0.3715 -0.0488 0.0988  -0.0451 104 GLU A CA  
903  C C   . GLU A 104 ? 0.2366 0.1251 0.3373 -0.0428 0.0929  -0.0298 104 GLU A C   
904  O O   . GLU A 104 ? 0.2782 0.1519 0.3756 -0.0368 0.1019  -0.0194 104 GLU A O   
905  C CB  . GLU A 104 ? 0.2777 0.1648 0.3883 -0.0589 0.1084  -0.0574 104 GLU A CB  
906  C CG  . GLU A 104 ? 0.3066 0.1898 0.4216 -0.0645 0.1178  -0.0716 104 GLU A CG  
907  C CD  . GLU A 104 ? 0.5943 0.4514 0.7070 -0.0557 0.1323  -0.0628 104 GLU A CD  
908  O OE1 . GLU A 104 ? 0.6182 0.4605 0.7256 -0.0452 0.1367  -0.0460 104 GLU A OE1 
909  O OE2 . GLU A 104 ? 0.7180 0.5709 0.8332 -0.0584 0.1392  -0.0724 104 GLU A OE2 
910  N N   . LYS A 105 ? 0.1988 0.1053 0.2992 -0.0440 0.0790  -0.0283 105 LYS A N   
911  C CA  . LYS A 105 ? 0.1942 0.1048 0.2895 -0.0383 0.0729  -0.0146 105 LYS A CA  
912  C C   . LYS A 105 ? 0.2116 0.1150 0.2986 -0.0229 0.0724  0.0021  105 LYS A C   
913  O O   . LYS A 105 ? 0.1940 0.1005 0.2792 -0.0166 0.0695  0.0030  105 LYS A O   
914  C CB  . LYS A 105 ? 0.1637 0.1016 0.2570 -0.0409 0.0564  -0.0174 105 LYS A CB  
915  C CG  . LYS A 105 ? 0.2053 0.1556 0.3062 -0.0538 0.0557  -0.0321 105 LYS A CG  
916  C CD  . LYS A 105 ? 0.1447 0.1215 0.2423 -0.0534 0.0404  -0.0340 105 LYS A CD  
917  C CE  . LYS A 105 ? 0.1757 0.1701 0.2796 -0.0631 0.0387  -0.0479 105 LYS A CE  
918  N NZ  . LYS A 105 ? 0.1683 0.1866 0.2686 -0.0604 0.0255  -0.0471 105 LYS A NZ  
919  N N   . PRO A 106 ? 0.2161 0.1119 0.2980 -0.0160 0.0757  0.0152  106 PRO A N   
920  C CA  . PRO A 106 ? 0.2016 0.0960 0.2754 -0.0001 0.0745  0.0307  106 PRO A CA  
921  C C   . PRO A 106 ? 0.1979 0.1165 0.2685 0.0044  0.0585  0.0321  106 PRO A C   
922  O O   . PRO A 106 ? 0.2404 0.1613 0.3082 0.0156  0.0577  0.0394  106 PRO A O   
923  C CB  . PRO A 106 ? 0.2188 0.1075 0.2868 0.0045  0.0781  0.0423  106 PRO A CB  
924  C CG  . PRO A 106 ? 0.2940 0.1722 0.3670 -0.0069 0.0879  0.0327  106 PRO A CG  
925  C CD  . PRO A 106 ? 0.2683 0.1566 0.3510 -0.0212 0.0828  0.0155  106 PRO A CD  
926  N N   . ILE A 107 ? 0.1793 0.1160 0.2507 -0.0035 0.0467  0.0254  107 ILE A N   
927  C CA  . ILE A 107 ? 0.1424 0.0987 0.2111 0.0000  0.0343  0.0266  107 ILE A CA  
928  C C   . ILE A 107 ? 0.1793 0.1385 0.2514 -0.0004 0.0338  0.0199  107 ILE A C   
929  O O   . ILE A 107 ? 0.1824 0.1554 0.2532 0.0038  0.0263  0.0220  107 ILE A O   
930  C CB  . ILE A 107 ? 0.1246 0.0964 0.1921 -0.0069 0.0239  0.0227  107 ILE A CB  
931  C CG1 . ILE A 107 ? 0.1421 0.1149 0.2145 -0.0178 0.0247  0.0110  107 ILE A CG1 
932  C CG2 . ILE A 107 ? 0.1430 0.1148 0.2058 -0.0044 0.0233  0.0306  107 ILE A CG2 
933  C CD1 . ILE A 107 ? 0.1488 0.1389 0.2194 -0.0216 0.0144  0.0078  107 ILE A CD1 
934  N N   . TYR A 108 ? 0.1895 0.1361 0.2662 -0.0055 0.0426  0.0113  108 TYR A N   
935  C CA  . TYR A 108 ? 0.2216 0.1691 0.3008 -0.0053 0.0440  0.0044  108 TYR A CA  
936  C C   . TYR A 108 ? 0.1876 0.1185 0.2674 0.0044  0.0550  0.0103  108 TYR A C   
937  O O   . TYR A 108 ? 0.1937 0.1199 0.2761 0.0044  0.0598  0.0037  108 TYR A O   
938  C CB  . TYR A 108 ? 0.1670 0.1146 0.2506 -0.0172 0.0465  -0.0112 108 TYR A CB  
939  C CG  . TYR A 108 ? 0.1379 0.1076 0.2195 -0.0220 0.0344  -0.0170 108 TYR A CG  
940  C CD1 . TYR A 108 ? 0.1455 0.1259 0.2252 -0.0248 0.0269  -0.0145 108 TYR A CD1 
941  C CD2 . TYR A 108 ? 0.1538 0.1328 0.2346 -0.0226 0.0318  -0.0242 108 TYR A CD2 
942  C CE1 . TYR A 108 ? 0.1426 0.1410 0.2194 -0.0270 0.0177  -0.0179 108 TYR A CE1 
943  C CE2 . TYR A 108 ? 0.1467 0.1445 0.2239 -0.0248 0.0223  -0.0273 108 TYR A CE2 
944  C CZ  . TYR A 108 ? 0.1478 0.1546 0.2230 -0.0266 0.0157  -0.0238 108 TYR A CZ  
945  O OH  . TYR A 108 ? 0.1495 0.1726 0.2202 -0.0270 0.0081  -0.0254 108 TYR A OH  
946  N N   . ARG A 109 ? 0.1838 0.1056 0.2604 0.0140  0.0598  0.0231  109 ARG A N   
947  C CA  . ARG A 109 ? 0.2247 0.1294 0.3008 0.0259  0.0720  0.0310  109 ARG A CA  
948  C C   . ARG A 109 ? 0.2623 0.1841 0.3374 0.0373  0.0648  0.0372  109 ARG A C   
949  O O   . ARG A 109 ? 0.2755 0.2081 0.3468 0.0488  0.0606  0.0491  109 ARG A O   
950  C CB  . ARG A 109 ? 0.2706 0.1600 0.3421 0.0336  0.0809  0.0436  109 ARG A CB  
951  C CG  . ARG A 109 ? 0.4198 0.2830 0.4907 0.0416  0.0990  0.0483  109 ARG A CG  
952  C CD  . ARG A 109 ? 0.5538 0.4093 0.6173 0.0452  0.1063  0.0575  109 ARG A CD  
953  N NE  . ARG A 109 ? 0.6412 0.4863 0.7086 0.0299  0.1124  0.0471  109 ARG A NE  
954  C CZ  . ARG A 109 ? 0.6440 0.4885 0.7076 0.0284  0.1137  0.0516  109 ARG A CZ  
955  N NH1 . ARG A 109 ? 0.6610 0.5141 0.7156 0.0408  0.1091  0.0660  109 ARG A NH1 
956  N NH2 . ARG A 109 ? 0.6085 0.4468 0.6774 0.0145  0.1192  0.0406  109 ARG A NH2 
957  N N   . PHE A 110 ? 0.2261 0.1532 0.3050 0.0336  0.0632  0.0278  110 PHE A N   
958  C CA  . PHE A 110 ? 0.2124 0.1536 0.2926 0.0431  0.0595  0.0314  110 PHE A CA  
959  C C   . PHE A 110 ? 0.2219 0.1457 0.3051 0.0463  0.0721  0.0266  110 PHE A C   
960  O O   . PHE A 110 ? 0.2205 0.1356 0.3058 0.0351  0.0759  0.0134  110 PHE A O   
961  C CB  . PHE A 110 ? 0.2025 0.1668 0.2840 0.0354  0.0467  0.0242  110 PHE A CB  
962  C CG  . PHE A 110 ? 0.1690 0.1505 0.2481 0.0317  0.0349  0.0273  110 PHE A CG  
963  C CD1 . PHE A 110 ? 0.1871 0.1878 0.2665 0.0393  0.0280  0.0348  110 PHE A CD1 
964  C CD2 . PHE A 110 ? 0.2566 0.2373 0.3338 0.0203  0.0309  0.0213  110 PHE A CD2 
965  C CE1 . PHE A 110 ? 0.1750 0.1906 0.2524 0.0345  0.0183  0.0356  110 PHE A CE1 
966  C CE2 . PHE A 110 ? 0.2404 0.2350 0.3152 0.0172  0.0214  0.0238  110 PHE A CE2 
967  C CZ  . PHE A 110 ? 0.2011 0.2117 0.2758 0.0238  0.0156  0.0305  110 PHE A CZ  
968  N N   . GLU A 111 ? 0.2582 0.1790 0.3417 0.0619  0.0785  0.0366  111 GLU A N   
969  C CA  . GLU A 111 ? 0.2522 0.1548 0.3384 0.0663  0.0919  0.0324  111 GLU A CA  
970  C C   . GLU A 111 ? 0.2530 0.1666 0.3423 0.0568  0.0870  0.0184  111 GLU A C   
971  O O   . GLU A 111 ? 0.2440 0.1412 0.3349 0.0512  0.0969  0.0072  111 GLU A O   
972  C CB  . GLU A 111 ? 0.3268 0.2317 0.4127 0.0867  0.0970  0.0466  111 GLU A CB  
973  C CG  . GLU A 111 ? 0.5663 0.4587 0.6525 0.0898  0.1078  0.0421  111 GLU A CG  
974  C CD  . GLU A 111 ? 0.8410 0.7035 0.9218 0.0873  0.1235  0.0424  111 GLU A CD  
975  O OE1 . GLU A 111 ? 0.9518 0.8094 1.0261 0.0942  0.1271  0.0547  111 GLU A OE1 
976  O OE2 . GLU A 111 ? 0.9302 0.7761 1.0133 0.0780  0.1328  0.0297  111 GLU A OE2 
977  N N   . ARG A 112 ? 0.2059 0.1471 0.2957 0.0547  0.0728  0.0184  112 ARG A N   
978  C CA  . ARG A 112 ? 0.1965 0.1486 0.2877 0.0477  0.0690  0.0073  112 ARG A CA  
979  C C   . ARG A 112 ? 0.2246 0.1702 0.3137 0.0323  0.0689  -0.0069 112 ARG A C   
980  O O   . ARG A 112 ? 0.2564 0.2008 0.3454 0.0277  0.0724  -0.0182 112 ARG A O   
981  C CB  . ARG A 112 ? 0.1920 0.1726 0.2843 0.0479  0.0558  0.0109  112 ARG A CB  
982  C CG  . ARG A 112 ? 0.2016 0.1937 0.2943 0.0421  0.0530  0.0018  112 ARG A CG  
983  C CD  . ARG A 112 ? 0.2184 0.2046 0.3140 0.0497  0.0627  -0.0008 112 ARG A CD  
984  N NE  . ARG A 112 ? 0.2261 0.2294 0.3223 0.0469  0.0588  -0.0057 112 ARG A NE  
985  C CZ  . ARG A 112 ? 0.3045 0.3056 0.4016 0.0500  0.0660  -0.0114 112 ARG A CZ  
986  N NH1 . ARG A 112 ? 0.3181 0.2996 0.4162 0.0559  0.0779  -0.0137 112 ARG A NH1 
987  N NH2 . ARG A 112 ? 0.3110 0.3286 0.4079 0.0472  0.0625  -0.0147 112 ARG A NH2 
988  N N   . ILE A 113 ? 0.2150 0.1587 0.3022 0.0247  0.0650  -0.0071 113 ILE A N   
989  C CA  . ILE A 113 ? 0.2074 0.1490 0.2938 0.0109  0.0647  -0.0211 113 ILE A CA  
990  C C   . ILE A 113 ? 0.2443 0.1629 0.3335 0.0074  0.0796  -0.0313 113 ILE A C   
991  O O   . ILE A 113 ? 0.2394 0.1603 0.3288 -0.0017 0.0813  -0.0466 113 ILE A O   
992  C CB  . ILE A 113 ? 0.2056 0.1513 0.2907 0.0045  0.0580  -0.0186 113 ILE A CB  
993  C CG1 . ILE A 113 ? 0.2080 0.1766 0.2900 0.0045  0.0440  -0.0137 113 ILE A CG1 
994  C CG2 . ILE A 113 ? 0.2154 0.1576 0.3017 -0.0086 0.0606  -0.0332 113 ILE A CG2 
995  C CD1 . ILE A 113 ? 0.2874 0.2609 0.3676 -0.0012 0.0375  -0.0118 113 ILE A CD1 
996  N N   . ARG A 114 ? 0.2349 0.1309 0.3259 0.0149  0.0918  -0.0235 114 ARG A N   
997  C CA  . ARG A 114 ? 0.3257 0.1956 0.4200 0.0117  0.1091  -0.0332 114 ARG A CA  
998  C C   . ARG A 114 ? 0.3386 0.2089 0.4332 0.0151  0.1136  -0.0408 114 ARG A C   
999  O O   . ARG A 114 ? 0.3022 0.1637 0.3987 0.0055  0.1217  -0.0577 114 ARG A O   
1000 C CB  . ARG A 114 ? 0.3913 0.2359 0.4856 0.0220  0.1226  -0.0198 114 ARG A CB  
1001 C CG  . ARG A 114 ? 0.6073 0.4327 0.7016 0.0148  0.1378  -0.0271 114 ARG A CG  
1002 C CD  . ARG A 114 ? 0.7177 0.5273 0.8081 0.0231  0.1479  -0.0115 114 ARG A CD  
1003 N NE  . ARG A 114 ? 0.7721 0.5804 0.8581 0.0417  0.1500  0.0044  114 ARG A NE  
1004 C CZ  . ARG A 114 ? 0.8893 0.6826 0.9737 0.0476  0.1633  0.0067  114 ARG A CZ  
1005 N NH1 . ARG A 114 ? 0.9420 0.7191 1.0295 0.0357  0.1762  -0.0062 114 ARG A NH1 
1006 N NH2 . ARG A 114 ? 0.9214 0.7180 1.0017 0.0653  0.1637  0.0214  114 ARG A NH2 
1007 N N   . GLU A 115 ? 0.2980 0.1808 0.3914 0.0280  0.1083  -0.0297 115 GLU A N   
1008 C CA  . GLU A 115 ? 0.3495 0.2352 0.4434 0.0319  0.1121  -0.0362 115 GLU A CA  
1009 C C   . GLU A 115 ? 0.2706 0.1745 0.3618 0.0193  0.1037  -0.0517 115 GLU A C   
1010 O O   . GLU A 115 ? 0.3432 0.2412 0.4342 0.0147  0.1114  -0.0660 115 GLU A O   
1011 C CB  . GLU A 115 ? 0.3472 0.2488 0.4419 0.0471  0.1065  -0.0216 115 GLU A CB  
1012 C CG  . GLU A 115 ? 0.3791 0.2708 0.4751 0.0624  0.1124  -0.0045 115 GLU A CG  
1013 C CD  . GLU A 115 ? 0.4749 0.3893 0.5733 0.0766  0.1058  0.0071  115 GLU A CD  
1014 O OE1 . GLU A 115 ? 0.5159 0.4292 0.6143 0.0911  0.1087  0.0215  115 GLU A OE1 
1015 O OE2 . GLU A 115 ? 0.4274 0.3626 0.5270 0.0727  0.0976  0.0015  115 GLU A OE2 
1016 N N   . LEU A 116 ? 0.2885 0.2149 0.3769 0.0145  0.0885  -0.0490 116 LEU A N   
1017 C CA  . LEU A 116 ? 0.2704 0.2162 0.3543 0.0060  0.0804  -0.0605 116 LEU A CA  
1018 C C   . LEU A 116 ? 0.3534 0.2943 0.4371 -0.0071 0.0847  -0.0787 116 LEU A C   
1019 O O   . LEU A 116 ? 0.3008 0.2504 0.3811 -0.0119 0.0853  -0.0925 116 LEU A O   
1020 C CB  . LEU A 116 ? 0.2395 0.2067 0.3203 0.0050  0.0655  -0.0521 116 LEU A CB  
1021 C CG  . LEU A 116 ? 0.2285 0.2064 0.3106 0.0152  0.0607  -0.0380 116 LEU A CG  
1022 C CD1 . LEU A 116 ? 0.2152 0.2077 0.2956 0.0128  0.0488  -0.0299 116 LEU A CD1 
1023 C CD2 . LEU A 116 ? 0.2806 0.2693 0.3609 0.0182  0.0617  -0.0418 116 LEU A CD2 
1024 N N   . MET A 117 ? 0.3056 0.2345 0.3929 -0.0134 0.0880  -0.0798 117 MET A N   
1025 C CA  . MET A 117 ? 0.3133 0.2414 0.4027 -0.0274 0.0920  -0.0988 117 MET A CA  
1026 C C   . MET A 117 ? 0.4129 0.3190 0.5062 -0.0309 0.1091  -0.1130 117 MET A C   
1027 O O   . MET A 117 ? 0.4547 0.3679 0.5495 -0.0435 0.1108  -0.1285 117 MET A O   
1028 C CB  . MET A 117 ? 0.2867 0.2096 0.3803 -0.0340 0.0914  -0.0963 117 MET A CB  
1029 C CG  . MET A 117 ? 0.3386 0.2833 0.4283 -0.0325 0.0752  -0.0855 117 MET A CG  
1030 S SD  . MET A 117 ? 0.4092 0.3879 0.4913 -0.0356 0.0609  -0.0938 117 MET A SD  
1031 C CE  . MET A 117 ? 0.4931 0.4808 0.5794 -0.0509 0.0633  -0.1165 117 MET A CE  
1032 N N   . ASN A 118 ? 0.3397 0.2268 0.4337 -0.0196 0.1191  -0.1034 118 ASN A N   
1033 C CA  . ASN A 118 ? 0.4595 0.3319 0.5543 -0.0215 0.1318  -0.1094 118 ASN A CA  
1034 C C   . ASN A 118 ? 0.4805 0.3632 0.5711 -0.0183 0.1310  -0.1176 118 ASN A C   
1035 O O   . ASN A 118 ? 0.5074 0.3781 0.5981 -0.0190 0.1413  -0.1229 118 ASN A O   
1036 C CB  . ASN A 118 ? 0.4202 0.2672 0.5165 -0.0099 0.1434  -0.0922 118 ASN A CB  
1037 C CG  . ASN A 118 ? 0.6210 0.4514 0.7210 -0.0178 0.1537  -0.0919 118 ASN A CG  
1038 O OD1 . ASN A 118 ? 0.7009 0.5330 0.8023 -0.0205 0.1497  -0.0864 118 ASN A OD1 
1039 N ND2 . ASN A 118 ? 0.6809 0.4952 0.7828 -0.0216 0.1681  -0.0980 118 ASN A ND2 
1040 N N   . LYS A 119 ? 0.4446 0.3490 0.5310 -0.0146 0.1200  -0.1184 119 LYS A N   
1041 C CA  . LYS A 119 ? 0.4131 0.3291 0.4946 -0.0096 0.1195  -0.1234 119 LYS A CA  
1042 C C   . LYS A 119 ? 0.3525 0.2898 0.4280 -0.0216 0.1134  -0.1422 119 LYS A C   
1043 O O   . LYS A 119 ? 0.4715 0.4257 0.5454 -0.0293 0.1039  -0.1476 119 LYS A O   
1044 C CB  . LYS A 119 ? 0.4328 0.3672 0.5115 0.0014  0.1076  -0.1053 119 LYS A CB  
1045 C CG  . LYS A 119 ? 0.5433 0.4637 0.6273 0.0157  0.1138  -0.0882 119 LYS A CG  
1046 C CD  . LYS A 119 ? 0.6133 0.5528 0.6956 0.0252  0.1076  -0.0793 119 LYS A CD  
1047 C CE  . LYS A 119 ? 0.7065 0.6570 0.7825 0.0208  0.1087  -0.0940 119 LYS A CE  
1048 N NZ  . LYS A 119 ? 0.7252 0.6838 0.8021 0.0317  0.1110  -0.0874 119 LYS A NZ  
1049 N N   . GLU A 120 ? 0.4538 0.3920 0.5256 -0.0222 0.1185  -0.1514 120 GLU A N   
1050 C CA  . GLU A 120 ? 0.5232 0.4839 0.5888 -0.0322 0.1128  -0.1686 120 GLU A CA  
1051 C C   . GLU A 120 ? 0.5219 0.5120 0.5778 -0.0283 0.1000  -0.1675 120 GLU A C   
1052 O O   . GLU A 120 ? 0.5066 0.5197 0.5579 -0.0355 0.0905  -0.1758 120 GLU A O   
1053 C CB  . GLU A 120 ? 0.5259 0.4798 0.5894 -0.0326 0.1220  -0.1781 120 GLU A CB  
1054 C CG  . GLU A 120 ? 0.5912 0.5241 0.6633 -0.0421 0.1342  -0.1859 120 GLU A CG  
1055 C CD  . GLU A 120 ? 0.7557 0.6776 0.8262 -0.0409 0.1451  -0.1938 120 GLU A CD  
1056 O OE1 . GLU A 120 ? 0.7873 0.7190 0.8497 -0.0327 0.1424  -0.1932 120 GLU A OE1 
1057 O OE2 . GLU A 120 ? 0.8104 0.7140 0.8878 -0.0483 0.1573  -0.2005 120 GLU A OE2 
1058 N N   . LYS A 121 ? 0.5048 0.4965 0.5582 -0.0162 0.0993  -0.1547 121 LYS A N   
1059 C CA  . LYS A 121 ? 0.4240 0.4420 0.4678 -0.0116 0.0867  -0.1458 121 LYS A CA  
1060 C C   . LYS A 121 ? 0.4149 0.4294 0.4631 -0.0022 0.0825  -0.1227 121 LYS A C   
1061 O O   . LYS A 121 ? 0.4506 0.4478 0.5065 0.0044  0.0901  -0.1148 121 LYS A O   
1062 C CB  . LYS A 121 ? 0.5073 0.5383 0.5413 -0.0082 0.0896  -0.1544 121 LYS A CB  
1063 C CG  . LYS A 121 ? 0.6099 0.6701 0.6307 -0.0062 0.0783  -0.1514 121 LYS A CG  
1064 C CD  . LYS A 121 ? 0.7099 0.7860 0.7191 -0.0083 0.0802  -0.1687 121 LYS A CD  
1065 C CE  . LYS A 121 ? 0.7281 0.8111 0.7388 -0.0201 0.0760  -0.1834 121 LYS A CE  
1066 N NZ  . LYS A 121 ? 0.7074 0.8211 0.7081 -0.0205 0.0634  -0.1838 121 LYS A NZ  
1067 N N   . LEU A 122 ? 0.3647 0.3965 0.4080 -0.0013 0.0710  -0.1124 122 LEU A N   
1068 C CA  . LEU A 122 ? 0.2869 0.3183 0.3346 0.0052  0.0664  -0.0930 122 LEU A CA  
1069 C C   . LEU A 122 ? 0.3249 0.3718 0.3661 0.0111  0.0642  -0.0860 122 LEU A C   
1070 O O   . LEU A 122 ? 0.2946 0.3574 0.3247 0.0098  0.0600  -0.0899 122 LEU A O   
1071 C CB  . LEU A 122 ? 0.2832 0.3185 0.3317 0.0010  0.0570  -0.0862 122 LEU A CB  
1072 C CG  . LEU A 122 ? 0.3224 0.3430 0.3776 -0.0055 0.0597  -0.0924 122 LEU A CG  
1073 C CD1 . LEU A 122 ? 0.3674 0.3959 0.4219 -0.0099 0.0501  -0.0874 122 LEU A CD1 
1074 C CD2 . LEU A 122 ? 0.3458 0.3449 0.4106 -0.0001 0.0678  -0.0846 122 LEU A CD2 
1075 N N   . ASN A 123 ? 0.2627 0.3061 0.3108 0.0181  0.0678  -0.0756 123 ASN A N   
1076 C CA  . ASN A 123 ? 0.1937 0.2510 0.2381 0.0225  0.0670  -0.0680 123 ASN A CA  
1077 C C   . ASN A 123 ? 0.1951 0.2593 0.2413 0.0214  0.0590  -0.0550 123 ASN A C   
1078 O O   . ASN A 123 ? 0.1963 0.2558 0.2450 0.0177  0.0534  -0.0526 123 ASN A O   
1079 C CB  . ASN A 123 ? 0.3043 0.3587 0.3569 0.0299  0.0753  -0.0650 123 ASN A CB  
1080 C CG  . ASN A 123 ? 0.3151 0.3611 0.3813 0.0342  0.0758  -0.0558 123 ASN A CG  
1081 O OD1 . ASN A 123 ? 0.2650 0.3122 0.3348 0.0322  0.0688  -0.0478 123 ASN A OD1 
1082 N ND2 . ASN A 123 ? 0.3806 0.4192 0.4537 0.0416  0.0845  -0.0565 123 ASN A ND2 
1083 N N   . ARG A 124 ? 0.2490 0.3233 0.2946 0.0241  0.0599  -0.0471 124 ARG A N   
1084 C CA  . ARG A 124 ? 0.1910 0.2706 0.2372 0.0218  0.0543  -0.0367 124 ARG A CA  
1085 C C   . ARG A 124 ? 0.1627 0.2376 0.2219 0.0212  0.0507  -0.0301 124 ARG A C   
1086 O O   . ARG A 124 ? 0.1817 0.2555 0.2403 0.0175  0.0445  -0.0260 124 ARG A O   
1087 C CB  . ARG A 124 ? 0.1617 0.2508 0.2065 0.0239  0.0590  -0.0304 124 ARG A CB  
1088 C CG  . ARG A 124 ? 0.2370 0.3288 0.2832 0.0205  0.0559  -0.0208 124 ARG A CG  
1089 C CD  . ARG A 124 ? 0.2066 0.3056 0.2527 0.0213  0.0634  -0.0152 124 ARG A CD  
1090 N NE  . ARG A 124 ? 0.2312 0.3300 0.2810 0.0168  0.0625  -0.0074 124 ARG A NE  
1091 C CZ  . ARG A 124 ? 0.3432 0.4452 0.4084 0.0133  0.0611  -0.0049 124 ARG A CZ  
1092 N NH1 . ARG A 124 ? 0.3058 0.4127 0.3834 0.0157  0.0603  -0.0077 124 ARG A NH1 
1093 N NH2 . ARG A 124 ? 0.2576 0.3588 0.3253 0.0079  0.0612  0.0002  124 ARG A NH2 
1094 N N   . GLU A 125 ? 0.1941 0.2680 0.2644 0.0260  0.0547  -0.0285 125 GLU A N   
1095 C CA  . GLU A 125 ? 0.1852 0.2581 0.2664 0.0274  0.0510  -0.0219 125 GLU A CA  
1096 C C   . GLU A 125 ? 0.1765 0.2360 0.2555 0.0255  0.0479  -0.0242 125 GLU A C   
1097 O O   . GLU A 125 ? 0.1902 0.2493 0.2722 0.0237  0.0423  -0.0186 125 GLU A O   
1098 C CB  . GLU A 125 ? 0.2468 0.3231 0.3393 0.0357  0.0562  -0.0195 125 GLU A CB  
1099 C CG  . GLU A 125 ? 0.4497 0.5417 0.5485 0.0381  0.0602  -0.0175 125 GLU A CG  
1100 C CD  . GLU A 125 ? 0.6846 0.7833 0.7962 0.0477  0.0638  -0.0142 125 GLU A CD  
1101 O OE1 . GLU A 125 ? 0.7707 0.8569 0.8830 0.0539  0.0659  -0.0142 125 GLU A OE1 
1102 O OE2 . GLU A 125 ? 0.7452 0.8619 0.8667 0.0495  0.0655  -0.0115 125 GLU A OE2 
1103 N N   . GLU A 126 ? 0.1603 0.2087 0.2346 0.0252  0.0525  -0.0331 126 GLU A N   
1104 C CA  . GLU A 126 ? 0.1642 0.1989 0.2378 0.0220  0.0518  -0.0368 126 GLU A CA  
1105 C C   . GLU A 126 ? 0.1697 0.2089 0.2366 0.0144  0.0439  -0.0377 126 GLU A C   
1106 O O   . GLU A 126 ? 0.1799 0.2133 0.2490 0.0120  0.0404  -0.0346 126 GLU A O   
1107 C CB  . GLU A 126 ? 0.1764 0.1987 0.2479 0.0217  0.0605  -0.0488 126 GLU A CB  
1108 C CG  . GLU A 126 ? 0.1941 0.2052 0.2735 0.0307  0.0698  -0.0458 126 GLU A CG  
1109 C CD  . GLU A 126 ? 0.3205 0.3225 0.3976 0.0319  0.0803  -0.0577 126 GLU A CD  
1110 O OE1 . GLU A 126 ? 0.3073 0.3136 0.3763 0.0249  0.0799  -0.0697 126 GLU A OE1 
1111 O OE2 . GLU A 126 ? 0.3491 0.3409 0.4322 0.0407  0.0893  -0.0550 126 GLU A OE2 
1112 N N   . LEU A 127 ? 0.1475 0.1977 0.2056 0.0120  0.0417  -0.0407 127 LEU A N   
1113 C CA  . LEU A 127 ? 0.1446 0.2009 0.1960 0.0074  0.0346  -0.0398 127 LEU A CA  
1114 C C   . LEU A 127 ? 0.1485 0.2072 0.2037 0.0073  0.0298  -0.0282 127 LEU A C   
1115 O O   . LEU A 127 ? 0.1562 0.2136 0.2101 0.0040  0.0247  -0.0262 127 LEU A O   
1116 C CB  . LEU A 127 ? 0.2023 0.2706 0.2417 0.0078  0.0345  -0.0436 127 LEU A CB  
1117 C CG  . LEU A 127 ? 0.2389 0.3095 0.2724 0.0060  0.0371  -0.0581 127 LEU A CG  
1118 C CD1 . LEU A 127 ? 0.2199 0.3039 0.2412 0.0096  0.0388  -0.0605 127 LEU A CD1 
1119 C CD2 . LEU A 127 ? 0.2259 0.2984 0.2581 0.0001  0.0320  -0.0649 127 LEU A CD2 
1120 N N   . LEU A 128 ? 0.1248 0.1884 0.1851 0.0103  0.0319  -0.0217 128 LEU A N   
1121 C CA  . LEU A 128 ? 0.1282 0.1952 0.1938 0.0088  0.0280  -0.0134 128 LEU A CA  
1122 C C   . LEU A 128 ? 0.1209 0.1815 0.1928 0.0089  0.0247  -0.0112 128 LEU A C   
1123 O O   . LEU A 128 ? 0.1507 0.2110 0.2221 0.0057  0.0198  -0.0075 128 LEU A O   
1124 C CB  . LEU A 128 ? 0.1230 0.1990 0.1961 0.0109  0.0316  -0.0093 128 LEU A CB  
1125 C CG  . LEU A 128 ? 0.1845 0.2669 0.2534 0.0085  0.0346  -0.0065 128 LEU A CG  
1126 C CD1 . LEU A 128 ? 0.2037 0.2961 0.2833 0.0099  0.0398  -0.0050 128 LEU A CD1 
1127 C CD2 . LEU A 128 ? 0.2521 0.3330 0.3189 0.0037  0.0310  -0.0020 128 LEU A CD2 
1128 N N   . ASP A 129 ? 0.1154 0.1692 0.1921 0.0133  0.0284  -0.0130 129 ASP A N   
1129 C CA  . ASP A 129 ? 0.1155 0.1612 0.1963 0.0150  0.0271  -0.0096 129 ASP A CA  
1130 C C   . ASP A 129 ? 0.1670 0.2038 0.2423 0.0092  0.0249  -0.0136 129 ASP A C   
1131 O O   . ASP A 129 ? 0.1510 0.1855 0.2272 0.0078  0.0211  -0.0091 129 ASP A O   
1132 C CB  . ASP A 129 ? 0.1276 0.1650 0.2135 0.0226  0.0342  -0.0096 129 ASP A CB  
1133 C CG  . ASP A 129 ? 0.1757 0.2254 0.2697 0.0302  0.0348  -0.0031 129 ASP A CG  
1134 O OD1 . ASP A 129 ? 0.1714 0.2364 0.2679 0.0275  0.0300  -0.0004 129 ASP A OD1 
1135 O OD2 . ASP A 129 ? 0.1850 0.2300 0.2834 0.0391  0.0408  -0.0009 129 ASP A OD2 
1136 N N   . LEU A 130 ? 0.1228 0.1570 0.1927 0.0056  0.0270  -0.0228 130 LEU A N   
1137 C CA  . LEU A 130 ? 0.1234 0.1538 0.1899 -0.0005 0.0248  -0.0282 130 LEU A CA  
1138 C C   . LEU A 130 ? 0.1641 0.2033 0.2266 -0.0033 0.0173  -0.0233 130 LEU A C   
1139 O O   . LEU A 130 ? 0.1578 0.1935 0.2212 -0.0062 0.0145  -0.0218 130 LEU A O   
1140 C CB  . LEU A 130 ? 0.1336 0.1658 0.1954 -0.0039 0.0279  -0.0410 130 LEU A CB  
1141 C CG  . LEU A 130 ? 0.1902 0.2212 0.2513 -0.0112 0.0272  -0.0506 130 LEU A CG  
1142 C CD1 . LEU A 130 ? 0.1983 0.2110 0.2670 -0.0128 0.0335  -0.0511 130 LEU A CD1 
1143 C CD2 . LEU A 130 ? 0.2143 0.2535 0.2705 -0.0143 0.0295  -0.0649 130 LEU A CD2 
1144 N N   . GLN A 131 ? 0.1587 0.2078 0.2168 -0.0020 0.0155  -0.0202 131 GLN A N   
1145 C CA  . GLN A 131 ? 0.1222 0.1767 0.1760 -0.0035 0.0108  -0.0148 131 GLN A CA  
1146 C C   . GLN A 131 ? 0.1118 0.1632 0.1717 -0.0040 0.0083  -0.0076 131 GLN A C   
1147 O O   . GLN A 131 ? 0.1110 0.1608 0.1694 -0.0064 0.0047  -0.0056 131 GLN A O   
1148 C CB  . GLN A 131 ? 0.1000 0.1619 0.1485 -0.0014 0.0126  -0.0116 131 GLN A CB  
1149 C CG  . GLN A 131 ? 0.1233 0.1917 0.1627 0.0004  0.0144  -0.0173 131 GLN A CG  
1150 C CD  . GLN A 131 ? 0.1487 0.2219 0.1832 0.0036  0.0187  -0.0125 131 GLN A CD  
1151 O OE1 . GLN A 131 ? 0.1303 0.2022 0.1717 0.0039  0.0223  -0.0093 131 GLN A OE1 
1152 N NE2 . GLN A 131 ? 0.1627 0.2425 0.1853 0.0066  0.0190  -0.0115 131 GLN A NE2 
1153 N N   . THR A 132 ? 0.1192 0.1722 0.1856 -0.0013 0.0101  -0.0040 132 THR A N   
1154 C CA  . THR A 132 ? 0.1035 0.1589 0.1750 -0.0014 0.0072  0.0017  132 THR A CA  
1155 C C   . THR A 132 ? 0.1273 0.1752 0.2005 -0.0002 0.0058  0.0030  132 THR A C   
1156 O O   . THR A 132 ? 0.0940 0.1426 0.1672 -0.0018 0.0022  0.0065  132 THR A O   
1157 C CB  . THR A 132 ? 0.1157 0.1802 0.1948 0.0017  0.0092  0.0038  132 THR A CB  
1158 O OG1 . THR A 132 ? 0.1088 0.1783 0.1860 0.0001  0.0125  0.0024  132 THR A OG1 
1159 C CG2 . THR A 132 ? 0.1191 0.1921 0.2035 0.0004  0.0056  0.0075  132 THR A CG2 
1160 N N   . LEU A 133 ? 0.0941 0.1335 0.1686 0.0024  0.0100  0.0002  133 LEU A N   
1161 C CA  . LEU A 133 ? 0.1241 0.1531 0.1996 0.0037  0.0113  0.0022  133 LEU A CA  
1162 C C   . LEU A 133 ? 0.1574 0.1821 0.2291 -0.0027 0.0091  -0.0012 133 LEU A C   
1163 O O   . LEU A 133 ? 0.1388 0.1584 0.2107 -0.0030 0.0085  0.0025  133 LEU A O   
1164 C CB  . LEU A 133 ? 0.1242 0.1415 0.2024 0.0080  0.0193  -0.0002 133 LEU A CB  
1165 C CG  . LEU A 133 ? 0.1760 0.1977 0.2590 0.0174  0.0216  0.0061  133 LEU A CG  
1166 C CD1 . LEU A 133 ? 0.1967 0.2060 0.2817 0.0223  0.0311  0.0030  133 LEU A CD1 
1167 C CD2 . LEU A 133 ? 0.1421 0.1665 0.2263 0.0230  0.0192  0.0154  133 LEU A CD2 
1168 N N   . ASN A 134 ? 0.1300 0.1588 0.1978 -0.0071 0.0081  -0.0078 134 ASN A N   
1169 C CA  . ASN A 134 ? 0.1184 0.1486 0.1834 -0.0120 0.0050  -0.0104 134 ASN A CA  
1170 C C   . ASN A 134 ? 0.1436 0.1783 0.2065 -0.0120 0.0000  -0.0034 134 ASN A C   
1171 O O   . ASN A 134 ? 0.1858 0.2178 0.2487 -0.0141 -0.0016 -0.0019 134 ASN A O   
1172 C CB  . ASN A 134 ? 0.1187 0.1574 0.1792 -0.0145 0.0042  -0.0185 134 ASN A CB  
1173 C CG  . ASN A 134 ? 0.1548 0.1895 0.2180 -0.0185 0.0086  -0.0292 134 ASN A CG  
1174 O OD1 . ASN A 134 ? 0.1423 0.1766 0.2077 -0.0233 0.0085  -0.0336 134 ASN A OD1 
1175 N ND2 . ASN A 134 ? 0.1568 0.1883 0.2208 -0.0172 0.0136  -0.0344 134 ASN A ND2 
1176 N N   . LEU A 135 ? 0.1101 0.1510 0.1720 -0.0103 -0.0014 0.0004  135 LEU A N   
1177 C CA  . LEU A 135 ? 0.0994 0.1429 0.1603 -0.0114 -0.0044 0.0055  135 LEU A CA  
1178 C C   . LEU A 135 ? 0.1481 0.1894 0.2127 -0.0102 -0.0056 0.0093  135 LEU A C   
1179 O O   . LEU A 135 ? 0.1435 0.1833 0.2062 -0.0120 -0.0078 0.0113  135 LEU A O   
1180 C CB  . LEU A 135 ? 0.1718 0.2212 0.2331 -0.0111 -0.0032 0.0074  135 LEU A CB  
1181 C CG  . LEU A 135 ? 0.2582 0.3092 0.3133 -0.0119 -0.0016 0.0080  135 LEU A CG  
1182 C CD1 . LEU A 135 ? 0.2356 0.2899 0.2941 -0.0133 0.0017  0.0101  135 LEU A CD1 
1183 C CD2 . LEU A 135 ? 0.1660 0.2142 0.2160 -0.0130 -0.0035 0.0098  135 LEU A CD2 
1184 N N   . LEU A 136 ? 0.1281 0.1703 0.1971 -0.0060 -0.0038 0.0111  136 LEU A N   
1185 C CA  . LEU A 136 ? 0.0934 0.1374 0.1644 -0.0024 -0.0051 0.0161  136 LEU A CA  
1186 C C   . LEU A 136 ? 0.1210 0.1540 0.1900 -0.0014 -0.0031 0.0179  136 LEU A C   
1187 O O   . LEU A 136 ? 0.1334 0.1675 0.2011 0.0010  -0.0046 0.0226  136 LEU A O   
1188 C CB  . LEU A 136 ? 0.1299 0.1805 0.2060 0.0043  -0.0034 0.0183  136 LEU A CB  
1189 C CG  . LEU A 136 ? 0.1544 0.2199 0.2349 0.0028  -0.0052 0.0169  136 LEU A CG  
1190 C CD1 . LEU A 136 ? 0.1814 0.2543 0.2679 0.0098  -0.0025 0.0180  136 LEU A CD1 
1191 C CD2 . LEU A 136 ? 0.1116 0.1888 0.1931 0.0002  -0.0098 0.0177  136 LEU A CD2 
1192 N N   . ALA A 137 ? 0.1308 0.1538 0.1998 -0.0035 0.0010  0.0135  137 ALA A N   
1193 C CA  . ALA A 137 ? 0.1235 0.1349 0.1921 -0.0046 0.0049  0.0139  137 ALA A CA  
1194 C C   . ALA A 137 ? 0.1411 0.1551 0.2068 -0.0086 0.0009  0.0150  137 ALA A C   
1195 O O   . ALA A 137 ? 0.1468 0.1540 0.2115 -0.0078 0.0034  0.0187  137 ALA A O   
1196 C CB  . ALA A 137 ? 0.1364 0.1398 0.2072 -0.0090 0.0103  0.0054  137 ALA A CB  
1197 N N   . TRP A 138 ? 0.1220 0.1448 0.1855 -0.0120 -0.0041 0.0129  138 TRP A N   
1198 C CA  . TRP A 138 ? 0.1357 0.1607 0.1963 -0.0149 -0.0071 0.0138  138 TRP A CA  
1199 C C   . TRP A 138 ? 0.1379 0.1687 0.1964 -0.0135 -0.0105 0.0182  138 TRP A C   
1200 O O   . TRP A 138 ? 0.1434 0.1760 0.1990 -0.0159 -0.0126 0.0182  138 TRP A O   
1201 C CB  . TRP A 138 ? 0.1176 0.1477 0.1764 -0.0182 -0.0088 0.0091  138 TRP A CB  
1202 C CG  . TRP A 138 ? 0.1100 0.1390 0.1715 -0.0208 -0.0061 0.0023  138 TRP A CG  
1203 C CD1 . TRP A 138 ? 0.1267 0.1567 0.1894 -0.0209 -0.0041 -0.0030 138 TRP A CD1 
1204 C CD2 . TRP A 138 ? 0.1376 0.1658 0.2016 -0.0248 -0.0045 -0.0015 138 TRP A CD2 
1205 N NE1 . TRP A 138 ? 0.1462 0.1765 0.2121 -0.0253 -0.0015 -0.0111 138 TRP A NE1 
1206 C CE2 . TRP A 138 ? 0.1046 0.1342 0.1722 -0.0281 -0.0015 -0.0104 138 TRP A CE2 
1207 C CE3 . TRP A 138 ? 0.1305 0.1577 0.1947 -0.0263 -0.0047 0.0009  138 TRP A CE3 
1208 C CZ2 . TRP A 138 ? 0.1181 0.1498 0.1910 -0.0341 0.0013  -0.0181 138 TRP A CZ2 
1209 C CZ3 . TRP A 138 ? 0.1218 0.1502 0.1909 -0.0314 -0.0017 -0.0053 138 TRP A CZ3 
1210 C CH2 . TRP A 138 ? 0.1488 0.1801 0.2229 -0.0357 0.0012  -0.0152 138 TRP A CH2 
1211 N N   . CYS A 139 ? 0.0944 0.1294 0.1546 -0.0093 -0.0108 0.0211  139 CYS A N   
1212 C CA  . CYS A 139 ? 0.0928 0.1377 0.1523 -0.0091 -0.0143 0.0226  139 CYS A CA  
1213 C C   . CYS A 139 ? 0.1139 0.1575 0.1692 -0.0084 -0.0152 0.0255  139 CYS A C   
1214 O O   . CYS A 139 ? 0.1213 0.1591 0.1751 -0.0041 -0.0127 0.0298  139 CYS A O   
1215 C CB  . CYS A 139 ? 0.0979 0.1527 0.1612 -0.0037 -0.0148 0.0244  139 CYS A CB  
1216 S SG  . CYS A 139 ? 0.1480 0.2220 0.2138 -0.0060 -0.0192 0.0218  139 CYS A SG  
1217 N N   . GLY A 140 ? 0.1248 0.1726 0.1777 -0.0124 -0.0176 0.0234  140 GLY A N   
1218 C CA  . GLY A 140 ? 0.1295 0.1779 0.1776 -0.0118 -0.0185 0.0254  140 GLY A CA  
1219 C C   . GLY A 140 ? 0.1202 0.1817 0.1670 -0.0072 -0.0212 0.0274  140 GLY A C   
1220 O O   . GLY A 140 ? 0.1105 0.1833 0.1613 -0.0046 -0.0229 0.0267  140 GLY A O   
1221 N N   . ARG A 141 ? 0.1028 0.1654 0.1435 -0.0055 -0.0218 0.0296  141 ARG A N   
1222 C CA  . ARG A 141 ? 0.1156 0.1932 0.1527 0.0011  -0.0245 0.0325  141 ARG A CA  
1223 C C   . ARG A 141 ? 0.0849 0.1824 0.1259 -0.0023 -0.0291 0.0251  141 ARG A C   
1224 O O   . ARG A 141 ? 0.1127 0.2273 0.1557 0.0037  -0.0319 0.0262  141 ARG A O   
1225 C CB  . ARG A 141 ? 0.1135 0.1888 0.1420 0.0025  -0.0238 0.0352  141 ARG A CB  
1226 C CG  . ARG A 141 ? 0.1277 0.2221 0.1498 0.0096  -0.0273 0.0373  141 ARG A CG  
1227 C CD  . ARG A 141 ? 0.1602 0.2489 0.1725 0.0120  -0.0249 0.0415  141 ARG A CD  
1228 N NE  . ARG A 141 ? 0.1975 0.3066 0.2015 0.0189  -0.0286 0.0426  141 ARG A NE  
1229 C CZ  . ARG A 141 ? 0.1638 0.2875 0.1650 0.0134  -0.0328 0.0334  141 ARG A CZ  
1230 N NH1 . ARG A 141 ? 0.1395 0.2560 0.1457 0.0014  -0.0324 0.0238  141 ARG A NH1 
1231 N NH2 . ARG A 141 ? 0.2085 0.3543 0.2015 0.0205  -0.0365 0.0339  141 ARG A NH2 
1232 N N   . THR A 142 ? 0.1120 0.2076 0.1547 -0.0119 -0.0289 0.0173  142 THR A N   
1233 C CA  . THR A 142 ? 0.0849 0.1979 0.1324 -0.0178 -0.0312 0.0082  142 THR A CA  
1234 C C   . THR A 142 ? 0.0959 0.2182 0.1525 -0.0171 -0.0316 0.0070  142 THR A C   
1235 O O   . THR A 142 ? 0.1423 0.2877 0.2033 -0.0152 -0.0352 0.0036  142 THR A O   
1236 C CB  . THR A 142 ? 0.1319 0.2338 0.1796 -0.0281 -0.0275 0.0011  142 THR A CB  
1237 O OG1 . THR A 142 ? 0.1477 0.2431 0.1873 -0.0282 -0.0269 0.0016  142 THR A OG1 
1238 C CG2 . THR A 142 ? 0.1349 0.2519 0.1893 -0.0365 -0.0272 -0.0101 142 THR A CG2 
1239 N N   . LEU A 143 ? 0.1208 0.2275 0.1802 -0.0182 -0.0280 0.0094  143 LEU A N   
1240 C CA  . LEU A 143 ? 0.1252 0.2389 0.1926 -0.0178 -0.0273 0.0082  143 LEU A CA  
1241 C C   . LEU A 143 ? 0.1821 0.3017 0.2505 -0.0068 -0.0287 0.0153  143 LEU A C   
1242 O O   . LEU A 143 ? 0.1592 0.2908 0.2348 -0.0047 -0.0289 0.0140  143 LEU A O   
1243 C CB  . LEU A 143 ? 0.1144 0.2108 0.1830 -0.0224 -0.0225 0.0080  143 LEU A CB  
1244 C CG  . LEU A 143 ? 0.0845 0.1756 0.1534 -0.0319 -0.0188 0.0017  143 LEU A CG  
1245 C CD1 . LEU A 143 ? 0.0999 0.1755 0.1679 -0.0333 -0.0136 0.0036  143 LEU A CD1 
1246 C CD2 . LEU A 143 ? 0.1289 0.2383 0.2060 -0.0383 -0.0185 -0.0068 143 LEU A CD2 
1247 N N   . ARG A 144 ? 0.1357 0.2462 0.1971 0.0007  -0.0283 0.0228  144 ARG A N   
1248 C CA  . ARG A 144 ? 0.1832 0.2984 0.2447 0.0126  -0.0277 0.0303  144 ARG A CA  
1249 C C   . ARG A 144 ? 0.2253 0.3697 0.2890 0.0185  -0.0327 0.0294  144 ARG A C   
1250 O O   . ARG A 144 ? 0.1958 0.3515 0.2632 0.0281  -0.0327 0.0336  144 ARG A O   
1251 C CB  . ARG A 144 ? 0.1771 0.2751 0.2305 0.0190  -0.0239 0.0388  144 ARG A CB  
1252 C CG  . ARG A 144 ? 0.2606 0.3345 0.3152 0.0161  -0.0180 0.0396  144 ARG A CG  
1253 C CD  . ARG A 144 ? 0.2196 0.2766 0.2680 0.0187  -0.0130 0.0455  144 ARG A CD  
1254 N NE  . ARG A 144 ? 0.2097 0.2473 0.2607 0.0152  -0.0069 0.0441  144 ARG A NE  
1255 C CZ  . ARG A 144 ? 0.2848 0.3105 0.3372 0.0210  0.0001  0.0481  144 ARG A CZ  
1256 N NH1 . ARG A 144 ? 0.2841 0.3145 0.3346 0.0329  0.0021  0.0559  144 ARG A NH1 
1257 N NH2 . ARG A 144 ? 0.2936 0.3035 0.3491 0.0155  0.0056  0.0439  144 ARG A NH2 
1258 N N   . LYS A 145 ? 0.1723 0.3311 0.2340 0.0131  -0.0369 0.0231  145 LYS A N   
1259 C CA  . LYS A 145 ? 0.2581 0.4410 0.3202 0.0157  -0.0404 0.0177  145 LYS A CA  
1260 C C   . LYS A 145 ? 0.2548 0.4460 0.3274 0.0069  -0.0398 0.0077  145 LYS A C   
1261 O O   . LYS A 145 ? 0.2345 0.4402 0.3112 0.0122  -0.0404 0.0071  145 LYS A O   
1262 C CB  . LYS A 145 ? 0.3343 0.5244 0.3886 0.0119  -0.0429 0.0124  145 LYS A CB  
1263 C CG  . LYS A 145 ? 0.5466 0.7267 0.5897 0.0179  -0.0427 0.0211  145 LYS A CG  
1264 C CD  . LYS A 145 ? 0.6711 0.8370 0.7108 0.0302  -0.0391 0.0357  145 LYS A CD  
1265 C CE  . LYS A 145 ? 0.6712 0.8150 0.7017 0.0301  -0.0352 0.0418  145 LYS A CE  
1266 N NZ  . LYS A 145 ? 0.5894 0.7060 0.6205 0.0332  -0.0278 0.0498  145 LYS A NZ  
1267 N N   . ASP A 146 ? 0.2355 0.4165 0.3122 -0.0060 -0.0374 0.0005  146 ASP A N   
1268 C CA  . ASP A 146 ? 0.1893 0.3754 0.2748 -0.0151 -0.0347 -0.0090 146 ASP A CA  
1269 C C   . ASP A 146 ? 0.2628 0.4486 0.3561 -0.0114 -0.0326 -0.0053 146 ASP A C   
1270 O O   . ASP A 146 ? 0.2368 0.4356 0.3372 -0.0130 -0.0317 -0.0105 146 ASP A O   
1271 C CB  . ASP A 146 ? 0.2027 0.3726 0.2886 -0.0280 -0.0302 -0.0152 146 ASP A CB  
1272 C CG  . ASP A 146 ? 0.2865 0.4570 0.3655 -0.0322 -0.0314 -0.0202 146 ASP A CG  
1273 O OD1 . ASP A 146 ? 0.3366 0.5236 0.4112 -0.0266 -0.0358 -0.0209 146 ASP A OD1 
1274 O OD2 . ASP A 146 ? 0.3792 0.5336 0.4566 -0.0404 -0.0271 -0.0232 146 ASP A OD2 
1275 N N   . LEU A 147 ? 0.1801 0.3526 0.2724 -0.0064 -0.0312 0.0032  147 LEU A N   
1276 C CA  . LEU A 147 ? 0.1632 0.3339 0.2622 -0.0027 -0.0282 0.0066  147 LEU A CA  
1277 C C   . LEU A 147 ? 0.1837 0.3594 0.2815 0.0124  -0.0292 0.0157  147 LEU A C   
1278 O O   . LEU A 147 ? 0.1789 0.3417 0.2776 0.0168  -0.0250 0.0199  147 LEU A O   
1279 C CB  . LEU A 147 ? 0.2136 0.3561 0.3078 -0.0072 -0.0233 0.0087  147 LEU A CB  
1280 C CG  . LEU A 147 ? 0.2175 0.3490 0.3101 -0.0191 -0.0204 0.0031  147 LEU A CG  
1281 C CD1 . LEU A 147 ? 0.2566 0.3639 0.3426 -0.0194 -0.0166 0.0068  147 LEU A CD1 
1282 C CD2 . LEU A 147 ? 0.3955 0.5400 0.4982 -0.0272 -0.0172 -0.0047 147 LEU A CD2 
1283 N N   . LYS A 148 ? 0.1538 0.3404 0.2456 0.0203  -0.0325 0.0180  148 LYS A N   
1284 C CA  . LYS A 148 ? 0.1769 0.3618 0.2642 0.0360  -0.0311 0.0289  148 LYS A CA  
1285 C C   . LYS A 148 ? 0.2332 0.4238 0.3280 0.0425  -0.0281 0.0302  148 LYS A C   
1286 O O   . LYS A 148 ? 0.2245 0.4026 0.3180 0.0531  -0.0234 0.0389  148 LYS A O   
1287 C CB  . LYS A 148 ? 0.2160 0.4140 0.2942 0.0435  -0.0344 0.0310  148 LYS A CB  
1288 C CG  . LYS A 148 ? 0.2757 0.4998 0.3578 0.0425  -0.0377 0.0232  148 LYS A CG  
1289 C CD  . LYS A 148 ? 0.4713 0.7080 0.5470 0.0586  -0.0376 0.0313  148 LYS A CD  
1290 C CE  . LYS A 148 ? 0.4897 0.7197 0.5517 0.0666  -0.0371 0.0394  148 LYS A CE  
1291 N NZ  . LYS A 148 ? 0.5812 0.8262 0.6357 0.0822  -0.0362 0.0467  148 LYS A NZ  
1292 N N   . ASP A 149 ? 0.1741 0.3813 0.2769 0.0361  -0.0296 0.0214  149 ASP A N   
1293 C CA  . ASP A 149 ? 0.2622 0.4769 0.3722 0.0427  -0.0267 0.0225  149 ASP A CA  
1294 C C   . ASP A 149 ? 0.2250 0.4232 0.3403 0.0411  -0.0212 0.0243  149 ASP A C   
1295 O O   . ASP A 149 ? 0.1935 0.3868 0.3104 0.0517  -0.0167 0.0302  149 ASP A O   
1296 C CB  . ASP A 149 ? 0.2545 0.4910 0.3729 0.0350  -0.0287 0.0124  149 ASP A CB  
1297 C CG  . ASP A 149 ? 0.3325 0.5892 0.4463 0.0365  -0.0338 0.0092  149 ASP A CG  
1298 O OD1 . ASP A 149 ? 0.2990 0.5595 0.4041 0.0495  -0.0352 0.0172  149 ASP A OD1 
1299 O OD2 . ASP A 149 ? 0.4226 0.6908 0.5410 0.0247  -0.0353 -0.0015 149 ASP A OD2 
1300 N N   . LEU A 150 ? 0.2106 0.3998 0.3280 0.0284  -0.0203 0.0193  150 LEU A N   
1301 C CA  . LEU A 150 ? 0.1884 0.3547 0.3044 0.0255  -0.0143 0.0198  150 LEU A CA  
1302 C C   . LEU A 150 ? 0.1466 0.2870 0.2528 0.0322  -0.0112 0.0268  150 LEU A C   
1303 O O   . LEU A 150 ? 0.1760 0.3016 0.2815 0.0357  -0.0055 0.0281  150 LEU A O   
1304 C CB  . LEU A 150 ? 0.2008 0.3567 0.3154 0.0109  -0.0132 0.0132  150 LEU A CB  
1305 C CG  . LEU A 150 ? 0.2385 0.4123 0.3635 0.0020  -0.0119 0.0055  150 LEU A CG  
1306 C CD1 . LEU A 150 ? 0.2116 0.3689 0.3324 -0.0101 -0.0083 0.0016  150 LEU A CD1 
1307 C CD2 . LEU A 150 ? 0.2623 0.4444 0.3954 0.0068  -0.0077 0.0055  150 LEU A CD2 
1308 N N   . LEU A 151 ? 0.1875 0.3221 0.2862 0.0332  -0.0138 0.0303  151 LEU A N   
1309 C CA  . LEU A 151 ? 0.2123 0.3226 0.3030 0.0385  -0.0092 0.0365  151 LEU A CA  
1310 C C   . LEU A 151 ? 0.2865 0.3958 0.3781 0.0536  -0.0041 0.0442  151 LEU A C   
1311 O O   . LEU A 151 ? 0.2268 0.3133 0.3160 0.0564  0.0036  0.0461  151 LEU A O   
1312 C CB  . LEU A 151 ? 0.2769 0.3842 0.3601 0.0374  -0.0123 0.0394  151 LEU A CB  
1313 C CG  . LEU A 151 ? 0.3358 0.4297 0.4149 0.0248  -0.0134 0.0342  151 LEU A CG  
1314 C CD1 . LEU A 151 ? 0.3709 0.4692 0.4441 0.0240  -0.0174 0.0360  151 LEU A CD1 
1315 C CD2 . LEU A 151 ? 0.3216 0.3904 0.3974 0.0231  -0.0074 0.0344  151 LEU A CD2 
1316 N N   . ASN A 152 ? 0.2675 0.4024 0.3629 0.0639  -0.0075 0.0482  152 ASN A N   
1317 C CA  . ASN A 152 ? 0.2181 0.3542 0.3137 0.0815  -0.0021 0.0576  152 ASN A CA  
1318 C C   . ASN A 152 ? 0.2198 0.3550 0.3232 0.0843  0.0031  0.0552  152 ASN A C   
1319 O O   . ASN A 152 ? 0.2515 0.3753 0.3521 0.0964  0.0106  0.0615  152 ASN A O   
1320 C CB  . ASN A 152 ? 0.3444 0.5034 0.4347 0.0873  -0.0078 0.0587  152 ASN A CB  
1321 C CG  . ASN A 152 ? 0.4596 0.6142 0.5382 0.0901  -0.0093 0.0641  152 ASN A CG  
1322 O OD1 . ASN A 152 ? 0.5236 0.6573 0.5983 0.0873  -0.0062 0.0673  152 ASN A OD1 
1323 N ND2 . ASN A 152 ? 0.5208 0.6961 0.5939 0.0957  -0.0134 0.0650  152 ASN A ND2 
1324 N N   . LYS A 153 ? 0.1874 0.3319 0.2980 0.0724  0.0003  0.0455  153 LYS A N   
1325 C CA  . LYS A 153 ? 0.2499 0.3892 0.3661 0.0733  0.0063  0.0425  153 LYS A CA  
1326 C C   . LYS A 153 ? 0.2935 0.3983 0.4027 0.0744  0.0154  0.0438  153 LYS A C   
1327 O O   . LYS A 153 ? 0.2863 0.3823 0.3968 0.0853  0.0235  0.0475  153 LYS A O   
1328 C CB  . LYS A 153 ? 0.2509 0.3969 0.3720 0.0583  0.0038  0.0325  153 LYS A CB  
1329 C CG  . LYS A 153 ? 0.2421 0.4215 0.3741 0.0556  -0.0014 0.0282  153 LYS A CG  
1330 C CD  . LYS A 153 ? 0.3112 0.4887 0.4459 0.0400  -0.0007 0.0195  153 LYS A CD  
1331 C CE  . LYS A 153 ? 0.2436 0.3995 0.3747 0.0387  0.0064  0.0181  153 LYS A CE  
1332 N NZ  . LYS A 153 ? 0.2592 0.4263 0.3988 0.0457  0.0114  0.0176  153 LYS A NZ  
1333 N N   . GLY A 154 ? 0.2295 0.3156 0.3320 0.0629  0.0148  0.0398  154 GLY A N   
1334 C CA  . GLY A 154 ? 0.2545 0.3111 0.3516 0.0604  0.0227  0.0380  154 GLY A CA  
1335 C C   . GLY A 154 ? 0.2333 0.2818 0.3325 0.0565  0.0281  0.0303  154 GLY A C   
1336 O O   . GLY A 154 ? 0.2116 0.2380 0.3071 0.0531  0.0348  0.0261  154 GLY A O   
1337 N N   . ARG A 155 ? 0.1555 0.2221 0.2607 0.0562  0.0259  0.0274  155 ARG A N   
1338 C CA  . ARG A 155 ? 0.1684 0.2298 0.2751 0.0545  0.0315  0.0209  155 ARG A CA  
1339 C C   . ARG A 155 ? 0.1671 0.2524 0.2806 0.0521  0.0277  0.0186  155 ARG A C   
1340 O O   . ARG A 155 ? 0.1914 0.2973 0.3101 0.0521  0.0215  0.0214  155 ARG A O   
1341 C CB  . ARG A 155 ? 0.2291 0.2782 0.3374 0.0668  0.0418  0.0238  155 ARG A CB  
1342 C CG  . ARG A 155 ? 0.2841 0.3527 0.3997 0.0812  0.0416  0.0323  155 ARG A CG  
1343 C CD  . ARG A 155 ? 0.3510 0.4042 0.4672 0.0954  0.0535  0.0367  155 ARG A CD  
1344 N NE  . ARG A 155 ? 0.3717 0.3974 0.4808 0.0982  0.0604  0.0408  155 ARG A NE  
1345 C CZ  . ARG A 155 ? 0.3816 0.3780 0.4871 0.0950  0.0714  0.0351  155 ARG A CZ  
1346 N NH1 . ARG A 155 ? 0.4667 0.4385 0.5673 0.0965  0.0790  0.0387  155 ARG A NH1 
1347 N NH2 . ARG A 155 ? 0.3553 0.3476 0.4623 0.0898  0.0757  0.0250  155 ARG A NH2 
1348 N N   . ASN A 156 ? 0.1772 0.2600 0.2908 0.0495  0.0324  0.0128  156 ASN A N   
1349 C CA  . ASN A 156 ? 0.1693 0.2723 0.2903 0.0483  0.0323  0.0107  156 ASN A CA  
1350 C C   . ASN A 156 ? 0.1431 0.2587 0.2650 0.0374  0.0260  0.0091  156 ASN A C   
1351 O O   . ASN A 156 ? 0.1841 0.3216 0.3155 0.0366  0.0241  0.0093  156 ASN A O   
1352 C CB  . ASN A 156 ? 0.2429 0.3648 0.3747 0.0606  0.0336  0.0158  156 ASN A CB  
1353 C CG  . ASN A 156 ? 0.2994 0.4069 0.4304 0.0734  0.0420  0.0187  156 ASN A CG  
1354 O OD1 . ASN A 156 ? 0.3230 0.4111 0.4485 0.0715  0.0488  0.0135  156 ASN A OD1 
1355 N ND2 . ASN A 156 ? 0.2494 0.3674 0.3857 0.0872  0.0424  0.0267  156 ASN A ND2 
1356 N N   . TYR A 157 ? 0.0995 0.2017 0.2120 0.0288  0.0238  0.0068  157 TYR A N   
1357 C CA  . TYR A 157 ? 0.1259 0.2350 0.2379 0.0193  0.0198  0.0059  157 TYR A CA  
1358 C C   . TYR A 157 ? 0.1200 0.2325 0.2314 0.0142  0.0245  0.0027  157 TYR A C   
1359 O O   . TYR A 157 ? 0.1525 0.2574 0.2587 0.0161  0.0293  0.0003  157 TYR A O   
1360 C CB  . TYR A 157 ? 0.1076 0.2016 0.2096 0.0140  0.0162  0.0060  157 TYR A CB  
1361 C CG  . TYR A 157 ? 0.0876 0.1791 0.1899 0.0179  0.0122  0.0099  157 TYR A CG  
1362 C CD1 . TYR A 157 ? 0.1002 0.2062 0.2077 0.0173  0.0073  0.0123  157 TYR A CD1 
1363 C CD2 . TYR A 157 ? 0.0953 0.1707 0.1930 0.0221  0.0144  0.0107  157 TYR A CD2 
1364 C CE1 . TYR A 157 ? 0.1172 0.2223 0.2233 0.0223  0.0039  0.0168  157 TYR A CE1 
1365 C CE2 . TYR A 157 ? 0.1023 0.1739 0.1995 0.0265  0.0125  0.0157  157 TYR A CE2 
1366 C CZ  . TYR A 157 ? 0.1243 0.2111 0.2248 0.0274  0.0070  0.0194  157 TYR A CZ  
1367 O OH  . TYR A 157 ? 0.1326 0.2172 0.2309 0.0331  0.0054  0.0251  157 TYR A OH  
1368 N N   . THR A 158 ? 0.0853 0.2089 0.2019 0.0073  0.0242  0.0023  158 THR A N   
1369 C CA  . THR A 158 ? 0.0882 0.2125 0.2034 0.0020  0.0307  0.0007  158 THR A CA  
1370 C C   . THR A 158 ? 0.0886 0.2003 0.1933 -0.0046 0.0305  0.0018  158 THR A C   
1371 O O   . THR A 158 ? 0.1104 0.2172 0.2124 -0.0068 0.0251  0.0029  158 THR A O   
1372 C CB  . THR A 158 ? 0.0867 0.2314 0.2166 -0.0019 0.0338  -0.0013 158 THR A CB  
1373 O OG1 . THR A 158 ? 0.1062 0.2571 0.2407 -0.0091 0.0298  -0.0024 158 THR A OG1 
1374 C CG2 . THR A 158 ? 0.1033 0.2651 0.2448 0.0065  0.0331  -0.0016 158 THR A CG2 
1375 N N   . GLN A 159 ? 0.0948 0.2017 0.1931 -0.0067 0.0374  0.0024  159 GLN A N   
1376 C CA  . GLN A 159 ? 0.0981 0.1934 0.1858 -0.0107 0.0392  0.0051  159 GLN A CA  
1377 C C   . GLN A 159 ? 0.0946 0.1923 0.1896 -0.0185 0.0391  0.0050  159 GLN A C   
1378 O O   . GLN A 159 ? 0.1158 0.2040 0.2041 -0.0205 0.0363  0.0068  159 GLN A O   
1379 C CB  . GLN A 159 ? 0.1172 0.2088 0.1970 -0.0098 0.0487  0.0072  159 GLN A CB  
1380 C CG  . GLN A 159 ? 0.1598 0.2392 0.2273 -0.0112 0.0527  0.0122  159 GLN A CG  
1381 C CD  . GLN A 159 ? 0.2064 0.2792 0.2598 -0.0057 0.0464  0.0132  159 GLN A CD  
1382 O OE1 . GLN A 159 ? 0.1834 0.2594 0.2348 -0.0016 0.0415  0.0094  159 GLN A OE1 
1383 N NE2 . GLN A 159 ? 0.2189 0.2831 0.2634 -0.0057 0.0475  0.0179  159 GLN A NE2 
1384 N N   . GLU A 160 ? 0.0933 0.2053 0.2027 -0.0231 0.0421  0.0017  160 GLU A N   
1385 C CA  . GLU A 160 ? 0.0916 0.2087 0.2095 -0.0320 0.0424  -0.0014 160 GLU A CA  
1386 C C   . GLU A 160 ? 0.0941 0.2135 0.2119 -0.0307 0.0319  -0.0021 160 GLU A C   
1387 O O   . GLU A 160 ? 0.1594 0.2717 0.2742 -0.0361 0.0311  -0.0026 160 GLU A O   
1388 C CB  . GLU A 160 ? 0.1310 0.2693 0.2666 -0.0372 0.0468  -0.0071 160 GLU A CB  
1389 C CG  . GLU A 160 ? 0.2299 0.3743 0.3737 -0.0476 0.0475  -0.0126 160 GLU A CG  
1390 C CD  . GLU A 160 ? 0.5274 0.6854 0.6754 -0.0452 0.0354  -0.0153 160 GLU A CD  
1391 O OE1 . GLU A 160 ? 0.5682 0.7221 0.7140 -0.0511 0.0332  -0.0183 160 GLU A OE1 
1392 O OE2 . GLU A 160 ? 0.6093 0.7806 0.7612 -0.0364 0.0292  -0.0140 160 GLU A OE2 
1393 N N   . GLU A 161 ? 0.0777 0.2051 0.1977 -0.0229 0.0249  -0.0015 161 GLU A N   
1394 C CA  . GLU A 161 ? 0.0828 0.2110 0.2012 -0.0203 0.0162  -0.0007 161 GLU A CA  
1395 C C   . GLU A 161 ? 0.0842 0.1921 0.1887 -0.0197 0.0142  0.0027  161 GLU A C   
1396 O O   . GLU A 161 ? 0.1025 0.2074 0.2046 -0.0224 0.0103  0.0028  161 GLU A O   
1397 C CB  . GLU A 161 ? 0.0705 0.2082 0.1930 -0.0103 0.0118  0.0010  161 GLU A CB  
1398 C CG  . GLU A 161 ? 0.0709 0.2347 0.2085 -0.0096 0.0119  -0.0022 161 GLU A CG  
1399 C CD  . GLU A 161 ? 0.1681 0.3399 0.3092 0.0026  0.0105  0.0009  161 GLU A CD  
1400 O OE1 . GLU A 161 ? 0.1263 0.2805 0.2587 0.0091  0.0116  0.0046  161 GLU A OE1 
1401 O OE2 . GLU A 161 ? 0.1722 0.3693 0.3256 0.0057  0.0090  -0.0009 161 GLU A OE2 
1402 N N   . LYS A 162 ? 0.0764 0.1726 0.1719 -0.0159 0.0168  0.0048  162 LYS A N   
1403 C CA  . LYS A 162 ? 0.0773 0.1590 0.1608 -0.0152 0.0149  0.0069  162 LYS A CA  
1404 C C   . LYS A 162 ? 0.1192 0.1943 0.1986 -0.0209 0.0180  0.0082  162 LYS A C   
1405 O O   . LYS A 162 ? 0.1148 0.1833 0.1893 -0.0217 0.0145  0.0094  162 LYS A O   
1406 C CB  . LYS A 162 ? 0.0828 0.1588 0.1580 -0.0107 0.0177  0.0069  162 LYS A CB  
1407 C CG  . LYS A 162 ? 0.0842 0.1509 0.1480 -0.0093 0.0150  0.0076  162 LYS A CG  
1408 C CD  . LYS A 162 ? 0.1922 0.2584 0.2481 -0.0052 0.0171  0.0054  162 LYS A CD  
1409 C CE  . LYS A 162 ? 0.2164 0.2849 0.2690 -0.0043 0.0243  0.0074  162 LYS A CE  
1410 N NZ  . LYS A 162 ? 0.1578 0.2278 0.1995 0.0005  0.0263  0.0053  162 LYS A NZ  
1411 N N   . GLU A 163 ? 0.1071 0.1825 0.1885 -0.0246 0.0262  0.0082  163 GLU A N   
1412 C CA  . GLU A 163 ? 0.1725 0.2377 0.2498 -0.0296 0.0323  0.0100  163 GLU A CA  
1413 C C   . GLU A 163 ? 0.1785 0.2477 0.2635 -0.0365 0.0297  0.0059  163 GLU A C   
1414 O O   . GLU A 163 ? 0.1390 0.1974 0.2186 -0.0389 0.0313  0.0072  163 GLU A O   
1415 C CB  . GLU A 163 ? 0.1879 0.2506 0.2664 -0.0324 0.0441  0.0110  163 GLU A CB  
1416 C CG  . GLU A 163 ? 0.1697 0.2272 0.2363 -0.0246 0.0477  0.0160  163 GLU A CG  
1417 C CD  . GLU A 163 ? 0.2533 0.3073 0.3196 -0.0264 0.0608  0.0184  163 GLU A CD  
1418 O OE1 . GLU A 163 ? 0.3280 0.3797 0.3836 -0.0194 0.0645  0.0225  163 GLU A OE1 
1419 O OE2 . GLU A 163 ? 0.3306 0.3849 0.4074 -0.0352 0.0682  0.0155  163 GLU A OE2 
1420 N N   . TYR A 164 ? 0.1612 0.2476 0.2586 -0.0390 0.0258  0.0009  164 TYR A N   
1421 C CA  . TYR A 164 ? 0.1862 0.2813 0.2903 -0.0448 0.0219  -0.0042 164 TYR A CA  
1422 C C   . TYR A 164 ? 0.1962 0.2843 0.2918 -0.0406 0.0141  -0.0013 164 TYR A C   
1423 O O   . TYR A 164 ? 0.1205 0.2026 0.2135 -0.0451 0.0145  -0.0029 164 TYR A O   
1424 C CB  . TYR A 164 ? 0.1271 0.2472 0.2449 -0.0450 0.0177  -0.0094 164 TYR A CB  
1425 C CG  . TYR A 164 ? 0.1740 0.3058 0.2963 -0.0494 0.0126  -0.0152 164 TYR A CG  
1426 C CD1 . TYR A 164 ? 0.2347 0.3648 0.3591 -0.0577 0.0176  -0.0213 164 TYR A CD1 
1427 C CD2 . TYR A 164 ? 0.1947 0.3355 0.3152 -0.0431 0.0032  -0.0137 164 TYR A CD2 
1428 C CE1 . TYR A 164 ? 0.2560 0.3951 0.3811 -0.0604 0.0127  -0.0273 164 TYR A CE1 
1429 C CE2 . TYR A 164 ? 0.1507 0.2997 0.2709 -0.0448 -0.0015 -0.0182 164 TYR A CE2 
1430 C CZ  . TYR A 164 ? 0.2218 0.3709 0.3443 -0.0537 0.0030  -0.0257 164 TYR A CZ  
1431 O OH  . TYR A 164 ? 0.2826 0.4424 0.4044 -0.0558 -0.0013 -0.0319 164 TYR A OH  
1432 N N   . VAL A 165 ? 0.1221 0.2099 0.2137 -0.0323 0.0082  0.0025  165 VAL A N   
1433 C CA  . VAL A 165 ? 0.1238 0.2041 0.2081 -0.0288 0.0024  0.0052  165 VAL A CA  
1434 C C   . VAL A 165 ? 0.1262 0.1906 0.2007 -0.0300 0.0054  0.0077  165 VAL A C   
1435 O O   . VAL A 165 ? 0.1246 0.1844 0.1957 -0.0316 0.0034  0.0079  165 VAL A O   
1436 C CB  . VAL A 165 ? 0.1036 0.1832 0.1861 -0.0209 -0.0012 0.0080  165 VAL A CB  
1437 C CG1 . VAL A 165 ? 0.1167 0.1866 0.1921 -0.0185 -0.0050 0.0104  165 VAL A CG1 
1438 C CG2 . VAL A 165 ? 0.1003 0.1954 0.1916 -0.0171 -0.0037 0.0073  165 VAL A CG2 
1439 N N   . LEU A 166 ? 0.1125 0.1697 0.1817 -0.0281 0.0107  0.0102  166 LEU A N   
1440 C CA  . LEU A 166 ? 0.1038 0.1485 0.1628 -0.0266 0.0141  0.0139  166 LEU A CA  
1441 C C   . LEU A 166 ? 0.1390 0.1769 0.1988 -0.0325 0.0197  0.0131  166 LEU A C   
1442 O O   . LEU A 166 ? 0.1206 0.1501 0.1744 -0.0315 0.0195  0.0151  166 LEU A O   
1443 C CB  . LEU A 166 ? 0.1063 0.1477 0.1590 -0.0224 0.0198  0.0172  166 LEU A CB  
1444 C CG  . LEU A 166 ? 0.1843 0.2291 0.2315 -0.0160 0.0153  0.0174  166 LEU A CG  
1445 C CD1 . LEU A 166 ? 0.2745 0.3196 0.3155 -0.0120 0.0215  0.0196  166 LEU A CD1 
1446 C CD2 . LEU A 166 ? 0.2820 0.3238 0.3219 -0.0128 0.0110  0.0189  166 LEU A CD2 
1447 N N   . ASN A 167 ? 0.1094 0.1510 0.1774 -0.0393 0.0254  0.0091  167 ASN A N   
1448 C CA  . ASN A 167 ? 0.1114 0.1451 0.1813 -0.0468 0.0329  0.0061  167 ASN A CA  
1449 C C   . ASN A 167 ? 0.1162 0.1549 0.1884 -0.0500 0.0260  0.0015  167 ASN A C   
1450 O O   . ASN A 167 ? 0.1648 0.1918 0.2324 -0.0522 0.0299  0.0014  167 ASN A O   
1451 C CB  . ASN A 167 ? 0.1344 0.1742 0.2153 -0.0554 0.0410  0.0003  167 ASN A CB  
1452 C CG  . ASN A 167 ? 0.3435 0.3724 0.4200 -0.0532 0.0522  0.0057  167 ASN A CG  
1453 O OD1 . ASN A 167 ? 0.4662 0.4806 0.5300 -0.0459 0.0560  0.0138  167 ASN A OD1 
1454 N ND2 . ASN A 167 ? 0.4006 0.4384 0.4874 -0.0589 0.0580  0.0015  167 ASN A ND2 
1455 N N   . LYS A 168 ? 0.1203 0.1758 0.1983 -0.0489 0.0166  -0.0014 168 LYS A N   
1456 C CA  . LYS A 168 ? 0.0816 0.1431 0.1597 -0.0503 0.0101  -0.0046 168 LYS A CA  
1457 C C   . LYS A 168 ? 0.1208 0.1702 0.1886 -0.0443 0.0069  0.0013  168 LYS A C   
1458 O O   . LYS A 168 ? 0.1344 0.1800 0.1991 -0.0464 0.0064  -0.0004 168 LYS A O   
1459 C CB  . LYS A 168 ? 0.0852 0.1673 0.1699 -0.0474 0.0016  -0.0065 168 LYS A CB  
1460 C CG  . LYS A 168 ? 0.1360 0.2375 0.2331 -0.0529 0.0030  -0.0137 168 LYS A CG  
1461 C CD  . LYS A 168 ? 0.2087 0.3081 0.3067 -0.0610 0.0074  -0.0215 168 LYS A CD  
1462 C CE  . LYS A 168 ? 0.3425 0.4513 0.4378 -0.0604 0.0006  -0.0254 168 LYS A CE  
1463 N NZ  . LYS A 168 ? 0.4396 0.5510 0.5368 -0.0684 0.0048  -0.0354 168 LYS A NZ  
1464 N N   . TYR A 169 ? 0.0990 0.1441 0.1620 -0.0374 0.0051  0.0070  169 TYR A N   
1465 C CA  . TYR A 169 ? 0.1112 0.1485 0.1664 -0.0325 0.0023  0.0112  169 TYR A CA  
1466 C C   . TYR A 169 ? 0.1032 0.1276 0.1521 -0.0328 0.0088  0.0132  169 TYR A C   
1467 O O   . TYR A 169 ? 0.1284 0.1487 0.1734 -0.0318 0.0072  0.0140  169 TYR A O   
1468 C CB  . TYR A 169 ? 0.0888 0.1267 0.1414 -0.0265 0.0001  0.0143  169 TYR A CB  
1469 C CG  . TYR A 169 ? 0.0991 0.1442 0.1557 -0.0242 -0.0056 0.0135  169 TYR A CG  
1470 C CD1 . TYR A 169 ? 0.1235 0.1769 0.1855 -0.0254 -0.0085 0.0118  169 TYR A CD1 
1471 C CD2 . TYR A 169 ? 0.0974 0.1412 0.1519 -0.0202 -0.0072 0.0142  169 TYR A CD2 
1472 C CE1 . TYR A 169 ? 0.1276 0.1852 0.1919 -0.0210 -0.0118 0.0132  169 TYR A CE1 
1473 C CE2 . TYR A 169 ? 0.1300 0.1760 0.1879 -0.0181 -0.0096 0.0138  169 TYR A CE2 
1474 C CZ  . TYR A 169 ? 0.1268 0.1783 0.1892 -0.0176 -0.0114 0.0144  169 TYR A CZ  
1475 O OH  . TYR A 169 ? 0.1223 0.1737 0.1869 -0.0133 -0.0121 0.0158  169 TYR A OH  
1476 N N   . PHE A 170 ? 0.1573 0.1743 0.2045 -0.0334 0.0172  0.0149  170 PHE A N   
1477 C CA  . PHE A 170 ? 0.1683 0.1705 0.2086 -0.0318 0.0257  0.0184  170 PHE A CA  
1478 C C   . PHE A 170 ? 0.1827 0.1790 0.2261 -0.0396 0.0301  0.0128  170 PHE A C   
1479 O O   . PHE A 170 ? 0.1404 0.1253 0.1780 -0.0374 0.0343  0.0150  170 PHE A O   
1480 C CB  . PHE A 170 ? 0.1728 0.1668 0.2091 -0.0291 0.0355  0.0231  170 PHE A CB  
1481 C CG  . PHE A 170 ? 0.1993 0.1960 0.2269 -0.0185 0.0330  0.0299  170 PHE A CG  
1482 C CD1 . PHE A 170 ? 0.2417 0.2331 0.2600 -0.0103 0.0343  0.0359  170 PHE A CD1 
1483 C CD2 . PHE A 170 ? 0.2376 0.2448 0.2665 -0.0165 0.0288  0.0294  170 PHE A CD2 
1484 C CE1 . PHE A 170 ? 0.2596 0.2593 0.2705 -0.0005 0.0308  0.0404  170 PHE A CE1 
1485 C CE2 . PHE A 170 ? 0.2032 0.2159 0.2241 -0.0076 0.0260  0.0333  170 PHE A CE2 
1486 C CZ  . PHE A 170 ? 0.2398 0.2504 0.2518 0.0002  0.0266  0.0384  170 PHE A CZ  
1487 N N   . GLU A 171 ? 0.1470 0.1530 0.1998 -0.0483 0.0292  0.0047  171 GLU A N   
1488 C CA  . GLU A 171 ? 0.1762 0.1821 0.2324 -0.0565 0.0312  -0.0034 171 GLU A CA  
1489 C C   . GLU A 171 ? 0.1809 0.1891 0.2322 -0.0528 0.0234  -0.0025 171 GLU A C   
1490 O O   . GLU A 171 ? 0.1649 0.1632 0.2127 -0.0550 0.0281  -0.0049 171 GLU A O   
1491 C CB  . GLU A 171 ? 0.2318 0.2564 0.2996 -0.0651 0.0284  -0.0131 171 GLU A CB  
1492 C CG  . GLU A 171 ? 0.3210 0.3428 0.3933 -0.0693 0.0369  -0.0158 171 GLU A CG  
1493 C CD  . GLU A 171 ? 0.4630 0.5053 0.5444 -0.0743 0.0322  -0.0253 171 GLU A CD  
1494 O OE1 . GLU A 171 ? 0.4680 0.5270 0.5513 -0.0736 0.0225  -0.0290 171 GLU A OE1 
1495 O OE2 . GLU A 171 ? 0.5204 0.5623 0.6062 -0.0781 0.0388  -0.0287 171 GLU A OE2 
1496 N N   . ILE A 172 ? 0.1348 0.1543 0.1857 -0.0472 0.0130  0.0008  172 ILE A N   
1497 C CA  . ILE A 172 ? 0.1510 0.1721 0.1975 -0.0435 0.0069  0.0025  172 ILE A CA  
1498 C C   . ILE A 172 ? 0.1628 0.1697 0.2017 -0.0384 0.0112  0.0080  172 ILE A C   
1499 O O   . ILE A 172 ? 0.1204 0.1224 0.1558 -0.0386 0.0125  0.0069  172 ILE A O   
1500 C CB  . ILE A 172 ? 0.0924 0.1245 0.1403 -0.0384 -0.0018 0.0058  172 ILE A CB  
1501 C CG1 . ILE A 172 ? 0.1400 0.1883 0.1939 -0.0410 -0.0064 0.0013  172 ILE A CG1 
1502 C CG2 . ILE A 172 ? 0.1646 0.1943 0.2075 -0.0340 -0.0055 0.0093  172 ILE A CG2 
1503 C CD1 . ILE A 172 ? 0.1887 0.2451 0.2416 -0.0441 -0.0089 -0.0039 172 ILE A CD1 
1504 N N   . ILE A 173 ? 0.1185 0.1208 0.1546 -0.0327 0.0136  0.0139  173 ILE A N   
1505 C CA  . ILE A 173 ? 0.1471 0.1406 0.1760 -0.0256 0.0171  0.0198  173 ILE A CA  
1506 C C   . ILE A 173 ? 0.1681 0.1461 0.1937 -0.0275 0.0277  0.0191  173 ILE A C   
1507 O O   . ILE A 173 ? 0.1409 0.1130 0.1622 -0.0237 0.0296  0.0210  173 ILE A O   
1508 C CB  . ILE A 173 ? 0.1250 0.1198 0.1505 -0.0185 0.0181  0.0256  173 ILE A CB  
1509 C CG1 . ILE A 173 ? 0.1532 0.1617 0.1821 -0.0174 0.0087  0.0245  173 ILE A CG1 
1510 C CG2 . ILE A 173 ? 0.1806 0.1697 0.1982 -0.0092 0.0223  0.0322  173 ILE A CG2 
1511 C CD1 . ILE A 173 ? 0.1756 0.1889 0.2007 -0.0108 0.0086  0.0281  173 ILE A CD1 
1512 N N   . LYS A 174 ? 0.1361 0.1070 0.1647 -0.0339 0.0358  0.0156  174 LYS A N   
1513 C CA  . LYS A 174 ? 0.1499 0.1021 0.1759 -0.0366 0.0491  0.0142  174 LYS A CA  
1514 C C   . LYS A 174 ? 0.1966 0.1483 0.2241 -0.0432 0.0484  0.0060  174 LYS A C   
1515 O O   . LYS A 174 ? 0.2236 0.1584 0.2471 -0.0432 0.0589  0.0055  174 LYS A O   
1516 C CB  . LYS A 174 ? 0.1759 0.1209 0.2068 -0.0444 0.0593  0.0105  174 LYS A CB  
1517 C CG  . LYS A 174 ? 0.1765 0.1176 0.2033 -0.0368 0.0637  0.0198  174 LYS A CG  
1518 C CD  . LYS A 174 ? 0.3389 0.2749 0.3704 -0.0438 0.0729  0.0153  174 LYS A CD  
1519 C CE  . LYS A 174 ? 0.4864 0.4188 0.5123 -0.0354 0.0776  0.0251  174 LYS A CE  
1520 N NZ  . LYS A 174 ? 0.6573 0.5841 0.6866 -0.0404 0.0865  0.0207  174 LYS A NZ  
1521 N N   . LYS A 175 ? 0.1722 0.1416 0.2045 -0.0479 0.0374  -0.0001 175 LYS A N   
1522 C CA  . LYS A 175 ? 0.1700 0.1429 0.2024 -0.0534 0.0357  -0.0082 175 LYS A CA  
1523 C C   . LYS A 175 ? 0.2050 0.1805 0.2317 -0.0458 0.0293  -0.0031 175 LYS A C   
1524 O O   . LYS A 175 ? 0.1701 0.1492 0.1953 -0.0489 0.0275  -0.0085 175 LYS A O   
1525 C CB  . LYS A 175 ? 0.2392 0.2327 0.2788 -0.0611 0.0278  -0.0171 175 LYS A CB  
1526 C CG  . LYS A 175 ? 0.3047 0.3005 0.3526 -0.0706 0.0341  -0.0250 175 LYS A CG  
1527 C CD  . LYS A 175 ? 0.3856 0.4075 0.4405 -0.0756 0.0248  -0.0336 175 LYS A CD  
1528 C CE  . LYS A 175 ? 0.5412 0.5781 0.5942 -0.0672 0.0120  -0.0265 175 LYS A CE  
1529 N NZ  . LYS A 175 ? 0.6750 0.7380 0.7347 -0.0694 0.0040  -0.0323 175 LYS A NZ  
1530 N N   . THR A 176 ? 0.1579 0.1337 0.1819 -0.0366 0.0260  0.0064  176 THR A N   
1531 C CA  . THR A 176 ? 0.1697 0.1524 0.1913 -0.0312 0.0191  0.0098  176 THR A CA  
1532 C C   . THR A 176 ? 0.1602 0.1326 0.1767 -0.0282 0.0252  0.0104  176 THR A C   
1533 O O   . THR A 176 ? 0.1783 0.1550 0.1935 -0.0297 0.0223  0.0073  176 THR A O   
1534 C CB  . THR A 176 ? 0.1357 0.1249 0.1577 -0.0240 0.0142  0.0169  176 THR A CB  
1535 O OG1 . THR A 176 ? 0.1559 0.1551 0.1828 -0.0270 0.0082  0.0154  176 THR A OG1 
1536 C CG2 . THR A 176 ? 0.1537 0.1496 0.1750 -0.0196 0.0093  0.0194  176 THR A CG2 
1537 N N   . LEU A 177 ? 0.2027 0.1612 0.2154 -0.0226 0.0345  0.0151  177 LEU A N   
1538 C CA  . LEU A 177 ? 0.1728 0.1211 0.1808 -0.0185 0.0412  0.0159  177 LEU A CA  
1539 C C   . LEU A 177 ? 0.1944 0.1355 0.2021 -0.0282 0.0462  0.0055  177 LEU A C   
1540 O O   . LEU A 177 ? 0.2054 0.1449 0.2100 -0.0273 0.0474  0.0032  177 LEU A O   
1541 C CB  . LEU A 177 ? 0.1746 0.1082 0.1775 -0.0088 0.0520  0.0241  177 LEU A CB  
1542 C CG  . LEU A 177 ? 0.2202 0.1663 0.2224 0.0020  0.0461  0.0333  177 LEU A CG  
1543 C CD1 . LEU A 177 ? 0.2349 0.1698 0.2303 0.0147  0.0566  0.0429  177 LEU A CD1 
1544 C CD2 . LEU A 177 ? 0.2699 0.2331 0.2747 0.0049  0.0364  0.0335  177 LEU A CD2 
1545 N N   . SER A 178 ? 0.1677 0.1069 0.1792 -0.0379 0.0491  -0.0021 178 SER A N   
1546 C CA  . SER A 178 ? 0.1924 0.1295 0.2048 -0.0486 0.0533  -0.0148 178 SER A CA  
1547 C C   . SER A 178 ? 0.2128 0.1693 0.2247 -0.0509 0.0418  -0.0195 178 SER A C   
1548 O O   . SER A 178 ? 0.2029 0.1583 0.2115 -0.0546 0.0445  -0.0271 178 SER A O   
1549 C CB  . SER A 178 ? 0.2149 0.1516 0.2338 -0.0595 0.0579  -0.0234 178 SER A CB  
1550 O OG  . SER A 178 ? 0.3363 0.2491 0.3540 -0.0592 0.0735  -0.0212 178 SER A OG  
1551 N N   . ILE A 179 ? 0.1604 0.1340 0.1748 -0.0481 0.0300  -0.0148 179 ILE A N   
1552 C CA  . ILE A 179 ? 0.1457 0.1357 0.1582 -0.0490 0.0213  -0.0179 179 ILE A CA  
1553 C C   . ILE A 179 ? 0.1980 0.1841 0.2047 -0.0425 0.0217  -0.0131 179 ILE A C   
1554 O O   . ILE A 179 ? 0.1816 0.1742 0.1840 -0.0442 0.0201  -0.0178 179 ILE A O   
1555 C CB  . ILE A 179 ? 0.1873 0.1942 0.2035 -0.0470 0.0108  -0.0138 179 ILE A CB  
1556 C CG1 . ILE A 179 ? 0.2501 0.2739 0.2631 -0.0478 0.0039  -0.0176 179 ILE A CG1 
1557 C CG2 . ILE A 179 ? 0.1793 0.1845 0.1957 -0.0388 0.0074  -0.0030 179 ILE A CG2 
1558 C CD1 . ILE A 179 ? 0.3536 0.3945 0.3706 -0.0472 -0.0038 -0.0168 179 ILE A CD1 
1559 N N   . TYR A 180 ? 0.1664 0.1443 0.1730 -0.0347 0.0241  -0.0041 180 TYR A N   
1560 C CA  . TYR A 180 ? 0.1496 0.1253 0.1524 -0.0288 0.0258  -0.0005 180 TYR A CA  
1561 C C   . TYR A 180 ? 0.1992 0.1619 0.1972 -0.0308 0.0356  -0.0068 180 TYR A C   
1562 O O   . TYR A 180 ? 0.1970 0.1624 0.1908 -0.0302 0.0357  -0.0091 180 TYR A O   
1563 C CB  . TYR A 180 ? 0.1693 0.1436 0.1743 -0.0199 0.0262  0.0090  180 TYR A CB  
1564 C CG  . TYR A 180 ? 0.1173 0.1055 0.1269 -0.0187 0.0170  0.0133  180 TYR A CG  
1565 C CD1 . TYR A 180 ? 0.1737 0.1713 0.1839 -0.0180 0.0126  0.0146  180 TYR A CD1 
1566 C CD2 . TYR A 180 ? 0.1320 0.1225 0.1452 -0.0185 0.0143  0.0156  180 TYR A CD2 
1567 C CE1 . TYR A 180 ? 0.1490 0.1559 0.1639 -0.0178 0.0066  0.0177  180 TYR A CE1 
1568 C CE2 . TYR A 180 ? 0.0969 0.0984 0.1145 -0.0180 0.0072  0.0182  180 TYR A CE2 
1569 C CZ  . TYR A 180 ? 0.1450 0.1538 0.1638 -0.0179 0.0039  0.0190  180 TYR A CZ  
1570 O OH  . TYR A 180 ? 0.1664 0.1827 0.1899 -0.0181 -0.0007 0.0208  180 TYR A OH  
1571 N N   . ARG A 181 ? 0.1971 0.1441 0.1952 -0.0332 0.0453  -0.0098 181 ARG A N   
1572 C CA  . ARG A 181 ? 0.2039 0.1361 0.1978 -0.0365 0.0565  -0.0177 181 ARG A CA  
1573 C C   . ARG A 181 ? 0.2068 0.1502 0.1991 -0.0467 0.0528  -0.0307 181 ARG A C   
1574 O O   . ARG A 181 ? 0.2419 0.1825 0.2288 -0.0474 0.0568  -0.0364 181 ARG A O   
1575 C CB  . ARG A 181 ? 0.2646 0.1754 0.2594 -0.0389 0.0698  -0.0195 181 ARG A CB  
1576 C CG  . ARG A 181 ? 0.2675 0.1662 0.2609 -0.0264 0.0758  -0.0061 181 ARG A CG  
1577 C CD  . ARG A 181 ? 0.3192 0.1923 0.3114 -0.0276 0.0926  -0.0068 181 ARG A CD  
1578 N NE  . ARG A 181 ? 0.4443 0.3122 0.4346 -0.0145 0.0954  0.0077  181 ARG A NE  
1579 C CZ  . ARG A 181 ? 0.3810 0.2514 0.3738 -0.0150 0.0936  0.0119  181 ARG A CZ  
1580 N NH1 . ARG A 181 ? 0.4091 0.2861 0.4078 -0.0281 0.0898  0.0027  181 ARG A NH1 
1581 N NH2 . ARG A 181 ? 0.4587 0.3268 0.4478 -0.0014 0.0960  0.0252  181 ARG A NH2 
1582 N N   . GLU A 182 ? 0.1976 0.1558 0.1941 -0.0536 0.0453  -0.0356 182 GLU A N   
1583 C CA  . GLU A 182 ? 0.2045 0.1780 0.1995 -0.0625 0.0416  -0.0488 182 GLU A CA  
1584 C C   . GLU A 182 ? 0.1813 0.1695 0.1697 -0.0573 0.0334  -0.0458 182 GLU A C   
1585 O O   . GLU A 182 ? 0.2005 0.1924 0.1828 -0.0605 0.0355  -0.0549 182 GLU A O   
1586 C CB  . GLU A 182 ? 0.2111 0.2011 0.2131 -0.0689 0.0347  -0.0533 182 GLU A CB  
1587 C CG  . GLU A 182 ? 0.2953 0.3080 0.2959 -0.0764 0.0292  -0.0669 182 GLU A CG  
1588 C CD  . GLU A 182 ? 0.4526 0.4836 0.4619 -0.0834 0.0242  -0.0736 182 GLU A CD  
1589 O OE1 . GLU A 182 ? 0.4949 0.5466 0.5049 -0.0910 0.0213  -0.0877 182 GLU A OE1 
1590 O OE2 . GLU A 182 ? 0.4719 0.4990 0.4873 -0.0810 0.0231  -0.0655 182 GLU A OE2 
1591 N N   . ILE A 183 ? 0.2079 0.2038 0.1972 -0.0493 0.0253  -0.0334 183 ILE A N   
1592 C CA  . ILE A 183 ? 0.1721 0.1804 0.1550 -0.0447 0.0196  -0.0300 183 ILE A CA  
1593 C C   . ILE A 183 ? 0.2104 0.2074 0.1882 -0.0406 0.0265  -0.0285 183 ILE A C   
1594 O O   . ILE A 183 ? 0.2320 0.2364 0.2024 -0.0397 0.0259  -0.0311 183 ILE A O   
1595 C CB  . ILE A 183 ? 0.1746 0.1917 0.1605 -0.0386 0.0115  -0.0183 183 ILE A CB  
1596 C CG1 . ILE A 183 ? 0.2119 0.2175 0.2029 -0.0331 0.0139  -0.0086 183 ILE A CG1 
1597 C CG2 . ILE A 183 ? 0.1964 0.2254 0.1869 -0.0418 0.0052  -0.0204 183 ILE A CG2 
1598 C CD1 . ILE A 183 ? 0.2327 0.2386 0.2214 -0.0272 0.0147  -0.0020 183 ILE A CD1 
1599 N N   . LYS A 184 ? 0.1832 0.1633 0.1641 -0.0372 0.0339  -0.0242 184 LYS A N   
1600 C CA  . LYS A 184 ? 0.1778 0.1473 0.1546 -0.0325 0.0418  -0.0233 184 LYS A CA  
1601 C C   . LYS A 184 ? 0.2078 0.1699 0.1787 -0.0390 0.0499  -0.0368 184 LYS A C   
1602 O O   . LYS A 184 ? 0.2297 0.1950 0.1937 -0.0381 0.0516  -0.0404 184 LYS A O   
1603 C CB  . LYS A 184 ? 0.2066 0.1625 0.1879 -0.0253 0.0479  -0.0149 184 LYS A CB  
1604 C CG  . LYS A 184 ? 0.2348 0.1820 0.2133 -0.0177 0.0560  -0.0120 184 LYS A CG  
1605 C CD  . LYS A 184 ? 0.2170 0.1541 0.1994 -0.0086 0.0616  -0.0030 184 LYS A CD  
1606 C CE  . LYS A 184 ? 0.2502 0.1785 0.2299 0.0007  0.0712  0.0002  184 LYS A CE  
1607 N NZ  . LYS A 184 ? 0.3433 0.2544 0.3164 -0.0038 0.0826  -0.0101 184 LYS A NZ  
1608 N N   . GLU A 185 ? 0.2135 0.1659 0.1871 -0.0466 0.0557  -0.0455 185 GLU A N   
1609 C CA  . GLU A 185 ? 0.2281 0.1718 0.1975 -0.0548 0.0654  -0.0609 185 GLU A CA  
1610 C C   . GLU A 185 ? 0.2405 0.2067 0.2041 -0.0610 0.0578  -0.0720 185 GLU A C   
1611 O O   . GLU A 185 ? 0.2729 0.2372 0.2296 -0.0643 0.0636  -0.0827 185 GLU A O   
1612 C CB  . GLU A 185 ? 0.2399 0.1693 0.2153 -0.0634 0.0741  -0.0685 185 GLU A CB  
1613 C CG  . GLU A 185 ? 0.2792 0.1957 0.2520 -0.0735 0.0871  -0.0861 185 GLU A CG  
1614 C CD  . GLU A 185 ? 0.3301 0.2220 0.3088 -0.0794 0.1016  -0.0901 185 GLU A CD  
1615 O OE1 . GLU A 185 ? 0.4472 0.3321 0.4270 -0.0892 0.1121  -0.1042 185 GLU A OE1 
1616 O OE2 . GLU A 185 ? 0.3789 0.2625 0.3619 -0.0730 0.1021  -0.0769 185 GLU A OE2 
1617 N N   . GLU A 186 ? 0.1873 0.2164 0.1919 -0.0467 0.0129  -0.0624 186 GLU A N   
1618 C CA  . GLU A 186 ? 0.2130 0.2560 0.2136 -0.0516 0.0059  -0.0603 186 GLU A CA  
1619 C C   . GLU A 186 ? 0.1968 0.2449 0.1887 -0.0551 0.0010  -0.0512 186 GLU A C   
1620 O O   . GLU A 186 ? 0.2035 0.2640 0.1898 -0.0615 -0.0065 -0.0466 186 GLU A O   
1621 C CB  . GLU A 186 ? 0.2230 0.2695 0.2332 -0.0483 -0.0032 -0.0584 186 GLU A CB  
1622 C CG  . GLU A 186 ? 0.2263 0.2745 0.2436 -0.0483 0.0021  -0.0686 186 GLU A CG  
1623 C CD  . GLU A 186 ? 0.2939 0.3507 0.3237 -0.0447 -0.0063 -0.0705 186 GLU A CD  
1624 O OE1 . GLU A 186 ? 0.2457 0.3011 0.2831 -0.0389 -0.0161 -0.0646 186 GLU A OE1 
1625 O OE2 . GLU A 186 ? 0.3045 0.3699 0.3385 -0.0477 -0.0035 -0.0791 186 GLU A OE2 
1626 N N   . GLY A 187 ? 0.1985 0.2392 0.1886 -0.0527 0.0046  -0.0480 187 GLY A N   
1627 C CA  . GLY A 187 ? 0.2211 0.2690 0.2021 -0.0583 0.0005  -0.0393 187 GLY A CA  
1628 C C   . GLY A 187 ? 0.2280 0.2722 0.2107 -0.0581 -0.0136 -0.0250 187 GLY A C   
1629 O O   . GLY A 187 ? 0.1983 0.2505 0.1714 -0.0667 -0.0206 -0.0148 187 GLY A O   
1630 N N   . LYS A 188 ? 0.1640 0.1975 0.1598 -0.0494 -0.0189 -0.0245 188 LYS A N   
1631 C CA  . LYS A 188 ? 0.1698 0.1974 0.1725 -0.0473 -0.0345 -0.0131 188 LYS A CA  
1632 C C   . LYS A 188 ? 0.1970 0.2129 0.2019 -0.0437 -0.0355 -0.0066 188 LYS A C   
1633 O O   . LYS A 188 ? 0.1756 0.1850 0.1849 -0.0439 -0.0495 0.0043  188 LYS A O   
1634 C CB  . LYS A 188 ? 0.1655 0.1914 0.1851 -0.0391 -0.0407 -0.0193 188 LYS A CB  
1635 C CG  . LYS A 188 ? 0.1758 0.2146 0.1941 -0.0430 -0.0405 -0.0257 188 LYS A CG  
1636 C CD  . LYS A 188 ? 0.2233 0.2644 0.2599 -0.0353 -0.0464 -0.0336 188 LYS A CD  
1637 C CE  . LYS A 188 ? 0.3716 0.4268 0.4065 -0.0401 -0.0475 -0.0391 188 LYS A CE  
1638 N NZ  . LYS A 188 ? 0.5029 0.5641 0.5576 -0.0329 -0.0566 -0.0464 188 LYS A NZ  
1639 N N   . GLY A 189 ? 0.1606 0.1727 0.1635 -0.0407 -0.0225 -0.0129 189 GLY A N   
1640 C CA  . GLY A 189 ? 0.1557 0.1587 0.1600 -0.0378 -0.0221 -0.0078 189 GLY A CA  
1641 C C   . GLY A 189 ? 0.1568 0.1591 0.1571 -0.0361 -0.0076 -0.0154 189 GLY A C   
1642 O O   . GLY A 189 ? 0.1910 0.1951 0.1917 -0.0349 0.0009  -0.0251 189 GLY A O   
1643 N N   . SER A 190 ? 0.1460 0.1450 0.1434 -0.0365 -0.0062 -0.0106 190 SER A N   
1644 C CA  . SER A 190 ? 0.1385 0.1345 0.1361 -0.0327 0.0049  -0.0172 190 SER A CA  
1645 C C   . SER A 190 ? 0.1662 0.1505 0.1736 -0.0245 0.0043  -0.0170 190 SER A C   
1646 O O   . SER A 190 ? 0.1662 0.1461 0.1802 -0.0223 -0.0046 -0.0118 190 SER A O   
1647 C CB  . SER A 190 ? 0.1731 0.1766 0.1625 -0.0382 0.0078  -0.0144 190 SER A CB  
1648 O OG  . SER A 190 ? 0.1833 0.2035 0.1635 -0.0474 0.0097  -0.0173 190 SER A OG  
1649 N N   . VAL A 191 ? 0.1523 0.1323 0.1617 -0.0206 0.0127  -0.0231 191 VAL A N   
1650 C CA  . VAL A 191 ? 0.1301 0.1029 0.1465 -0.0151 0.0135  -0.0233 191 VAL A CA  
1651 C C   . VAL A 191 ? 0.1598 0.1294 0.1738 -0.0136 0.0188  -0.0225 191 VAL A C   
1652 O O   . VAL A 191 ? 0.1845 0.1541 0.1960 -0.0142 0.0243  -0.0270 191 VAL A O   
1653 C CB  . VAL A 191 ? 0.1393 0.1115 0.1601 -0.0139 0.0168  -0.0296 191 VAL A CB  
1654 C CG1 . VAL A 191 ? 0.1273 0.0974 0.1540 -0.0106 0.0175  -0.0300 191 VAL A CG1 
1655 C CG2 . VAL A 191 ? 0.1873 0.1659 0.2118 -0.0153 0.0119  -0.0325 191 VAL A CG2 
1656 N N   . SER A 192 ? 0.1673 0.1340 0.1842 -0.0112 0.0161  -0.0180 192 SER A N   
1657 C CA  . SER A 192 ? 0.1389 0.1038 0.1549 -0.0094 0.0202  -0.0171 192 SER A CA  
1658 C C   . SER A 192 ? 0.1381 0.0981 0.1594 -0.0054 0.0213  -0.0180 192 SER A C   
1659 O O   . SER A 192 ? 0.1302 0.0913 0.1561 -0.0049 0.0193  -0.0203 192 SER A O   
1660 C CB  . SER A 192 ? 0.1134 0.0812 0.1271 -0.0121 0.0162  -0.0108 192 SER A CB  
1661 O OG  . SER A 192 ? 0.1476 0.1106 0.1676 -0.0104 0.0087  -0.0069 192 SER A OG  
1662 N N   . THR A 193 ? 0.1413 0.0991 0.1625 -0.0034 0.0241  -0.0169 193 THR A N   
1663 C CA  . THR A 193 ? 0.1129 0.0692 0.1377 -0.0013 0.0243  -0.0163 193 THR A CA  
1664 C C   . THR A 193 ? 0.1800 0.1368 0.2056 0.0005  0.0240  -0.0131 193 THR A C   
1665 O O   . THR A 193 ? 0.1516 0.1106 0.1748 -0.0006 0.0238  -0.0115 193 THR A O   
1666 C CB  . THR A 193 ? 0.1470 0.0995 0.1705 -0.0023 0.0273  -0.0173 193 THR A CB  
1667 O OG1 . THR A 193 ? 0.1457 0.1017 0.1708 -0.0034 0.0270  -0.0167 193 THR A OG1 
1668 C CG2 . THR A 193 ? 0.1594 0.1065 0.1825 -0.0002 0.0287  -0.0165 193 THR A CG2 
1669 N N   . SER A 194 ? 0.1673 0.1247 0.1959 0.0019  0.0239  -0.0128 194 SER A N   
1670 C CA  . SER A 194 ? 0.1445 0.1032 0.1746 0.0034  0.0235  -0.0104 194 SER A CA  
1671 C C   . SER A 194 ? 0.1640 0.1219 0.1931 0.0043  0.0258  -0.0094 194 SER A C   
1672 O O   . SER A 194 ? 0.1680 0.1245 0.1953 0.0022  0.0264  -0.0095 194 SER A O   
1673 C CB  . SER A 194 ? 0.1234 0.0850 0.1600 0.0039  0.0196  -0.0119 194 SER A CB  
1674 O OG  . SER A 194 ? 0.1188 0.0781 0.1583 0.0030  0.0140  -0.0109 194 SER A OG  
1675 N N   . PRO A 195 ? 0.1261 0.0852 0.1562 0.0062  0.0260  -0.0074 195 PRO A N   
1676 C CA  . PRO A 195 ? 0.1146 0.0732 0.1446 0.0068  0.0257  -0.0049 195 PRO A CA  
1677 C C   . PRO A 195 ? 0.1823 0.1461 0.2111 0.0028  0.0253  -0.0051 195 PRO A C   
1678 O O   . PRO A 195 ? 0.1507 0.1208 0.1829 0.0022  0.0251  -0.0093 195 PRO A O   
1679 C CB  . PRO A 195 ? 0.2349 0.1978 0.2675 0.0092  0.0255  -0.0041 195 PRO A CB  
1680 C CG  . PRO A 195 ? 0.3070 0.2718 0.3399 0.0093  0.0266  -0.0061 195 PRO A CG  
1681 C CD  . PRO A 195 ? 0.1755 0.1380 0.2063 0.0066  0.0258  -0.0068 195 PRO A CD  
1682 N N   . TYR A 196 ? 0.1470 0.1093 0.1720 -0.0006 0.0242  -0.0010 196 TYR A N   
1683 C CA  . TYR A 196 ? 0.1494 0.1182 0.1706 -0.0079 0.0247  -0.0015 196 TYR A CA  
1684 C C   . TYR A 196 ? 0.1643 0.1491 0.1889 -0.0101 0.0262  -0.0085 196 TYR A C   
1685 O O   . TYR A 196 ? 0.1283 0.1208 0.1556 -0.0122 0.0275  -0.0154 196 TYR A O   
1686 C CB  . TYR A 196 ? 0.1492 0.1150 0.1645 -0.0139 0.0213  0.0070  196 TYR A CB  
1687 C CG  . TYR A 196 ? 0.1249 0.0942 0.1340 -0.0239 0.0212  0.0087  196 TYR A CG  
1688 C CD1 . TYR A 196 ? 0.1253 0.1145 0.1320 -0.0318 0.0241  0.0037  196 TYR A CD1 
1689 C CD2 . TYR A 196 ? 0.1357 0.0903 0.1426 -0.0262 0.0180  0.0138  196 TYR A CD2 
1690 C CE1 . TYR A 196 ? 0.1310 0.1277 0.1315 -0.0430 0.0247  0.0044  196 TYR A CE1 
1691 C CE2 . TYR A 196 ? 0.1597 0.1176 0.1601 -0.0372 0.0176  0.0162  196 TYR A CE2 
1692 C CZ  . TYR A 196 ? 0.1827 0.1627 0.1791 -0.0462 0.0213  0.0120  196 TYR A CZ  
1693 O OH  . TYR A 196 ? 0.2004 0.1875 0.1899 -0.0590 0.0215  0.0137  196 TYR A OH  
1694 N N   . TYR A 197 ? 0.1535 0.1455 0.1796 -0.0097 0.0258  -0.0086 197 TYR A N   
1695 C CA  . TYR A 197 ? 0.1378 0.1471 0.1696 -0.0119 0.0268  -0.0179 197 TYR A CA  
1696 C C   . TYR A 197 ? 0.1260 0.1327 0.1681 -0.0048 0.0251  -0.0237 197 TYR A C   
1697 O O   . TYR A 197 ? 0.1213 0.1396 0.1707 -0.0050 0.0245  -0.0314 197 TYR A O   
1698 C CB  . TYR A 197 ? 0.1100 0.1330 0.1366 -0.0187 0.0270  -0.0156 197 TYR A CB  
1699 C CG  . TYR A 197 ? 0.1408 0.1685 0.1569 -0.0292 0.0268  -0.0094 197 TYR A CG  
1700 C CD1 . TYR A 197 ? 0.1279 0.1731 0.1439 -0.0369 0.0296  -0.0175 197 TYR A CD1 
1701 C CD2 . TYR A 197 ? 0.1703 0.1851 0.1781 -0.0319 0.0227  0.0044  197 TYR A CD2 
1702 C CE1 . TYR A 197 ? 0.1611 0.2114 0.1659 -0.0493 0.0292  -0.0105 197 TYR A CE1 
1703 C CE2 . TYR A 197 ? 0.1403 0.1567 0.1383 -0.0434 0.0204  0.0124  197 TYR A CE2 
1704 C CZ  . TYR A 197 ? 0.1743 0.2087 0.1694 -0.0531 0.0241  0.0057  197 TYR A CZ  
1705 O OH  . TYR A 197 ? 0.2068 0.2446 0.1907 -0.0674 0.0216  0.0145  197 TYR A OH  
1706 N N   . HIS A 198 ? 0.1186 0.1112 0.1617 0.0000  0.0236  -0.0204 198 HIS A N   
1707 C CA  . HIS A 198 ? 0.1297 0.1178 0.1811 0.0040  0.0200  -0.0229 198 HIS A CA  
1708 C C   . HIS A 198 ? 0.0958 0.0867 0.1494 0.0046  0.0193  -0.0221 198 HIS A C   
1709 O O   . HIS A 198 ? 0.1008 0.0955 0.1645 0.0056  0.0159  -0.0287 198 HIS A O   
1710 C CB  . HIS A 198 ? 0.1332 0.1273 0.1963 0.0050  0.0165  -0.0333 198 HIS A CB  
1711 C CG  . HIS A 198 ? 0.0844 0.0681 0.1564 0.0084  0.0092  -0.0333 198 HIS A CG  
1712 N ND1 . HIS A 198 ? 0.0965 0.0798 0.1800 0.0101  0.0035  -0.0375 198 HIS A ND1 
1713 C CD2 . HIS A 198 ? 0.1161 0.0899 0.1880 0.0090  0.0050  -0.0291 198 HIS A CD2 
1714 C CE1 . HIS A 198 ? 0.1332 0.1043 0.2228 0.0113  -0.0049 -0.0342 198 HIS A CE1 
1715 N NE2 . HIS A 198 ? 0.1196 0.0859 0.2018 0.0103  -0.0042 -0.0288 198 HIS A NE2 
1716 N N   . PRO A 199 ? 0.0887 0.0781 0.1353 0.0043  0.0215  -0.0152 199 PRO A N   
1717 C CA  . PRO A 199 ? 0.0898 0.0831 0.1386 0.0048  0.0208  -0.0145 199 PRO A CA  
1718 C C   . PRO A 199 ? 0.1795 0.1655 0.2303 0.0059  0.0187  -0.0116 199 PRO A C   
1719 O O   . PRO A 199 ? 0.1691 0.1480 0.2175 0.0058  0.0182  -0.0087 199 PRO A O   
1720 C CB  . PRO A 199 ? 0.1480 0.1423 0.1898 0.0045  0.0225  -0.0082 199 PRO A CB  
1721 C CG  . PRO A 199 ? 0.1722 0.1563 0.2102 0.0061  0.0232  -0.0046 199 PRO A CG  
1722 C CD  . PRO A 199 ? 0.1421 0.1257 0.1808 0.0043  0.0234  -0.0088 199 PRO A CD  
1723 N N   . LEU A 200 ? 0.1427 0.1326 0.1969 0.0052  0.0176  -0.0119 200 LEU A N   
1724 C CA  . LEU A 200 ? 0.1251 0.1117 0.1792 0.0034  0.0160  -0.0077 200 LEU A CA  
1725 C C   . LEU A 200 ? 0.1376 0.1287 0.1863 0.0046  0.0200  -0.0043 200 LEU A C   
1726 O O   . LEU A 200 ? 0.1609 0.1593 0.2108 0.0053  0.0209  -0.0044 200 LEU A O   
1727 C CB  . LEU A 200 ? 0.1650 0.1540 0.2263 0.0014  0.0124  -0.0103 200 LEU A CB  
1728 C CG  . LEU A 200 ? 0.1769 0.1601 0.2487 0.0014  0.0059  -0.0159 200 LEU A CG  
1729 C CD1 . LEU A 200 ? 0.1654 0.1524 0.2466 0.0002  0.0025  -0.0213 200 LEU A CD1 
1730 C CD2 . LEU A 200 ? 0.2167 0.1875 0.2884 -0.0017 -0.0001 -0.0097 200 LEU A CD2 
1731 N N   . ILE A 201 ? 0.1628 0.1510 0.2074 0.0052  0.0219  -0.0027 201 ILE A N   
1732 C CA  . ILE A 201 ? 0.1354 0.1288 0.1794 0.0079  0.0246  -0.0031 201 ILE A CA  
1733 C C   . ILE A 201 ? 0.1210 0.1248 0.1673 0.0059  0.0254  -0.0037 201 ILE A C   
1734 O O   . ILE A 201 ? 0.1412 0.1517 0.1913 0.0099  0.0259  -0.0055 201 ILE A O   
1735 C CB  . ILE A 201 ? 0.1082 0.0990 0.1496 0.0082  0.0264  -0.0043 201 ILE A CB  
1736 C CG1 . ILE A 201 ? 0.1397 0.1212 0.1793 0.0103  0.0258  -0.0040 201 ILE A CG1 
1737 C CG2 . ILE A 201 ? 0.1380 0.1377 0.1834 0.0114  0.0286  -0.0088 201 ILE A CG2 
1738 C CD1 . ILE A 201 ? 0.1595 0.1386 0.2007 0.0141  0.0247  -0.0031 201 ILE A CD1 
1739 N N   . PRO A 202 ? 0.1188 0.1251 0.1635 -0.0009 0.0243  -0.0018 202 PRO A N   
1740 C CA  . PRO A 202 ? 0.0884 0.1076 0.1347 -0.0047 0.0256  -0.0026 202 PRO A CA  
1741 C C   . PRO A 202 ? 0.1031 0.1263 0.1543 -0.0018 0.0248  -0.0038 202 PRO A C   
1742 O O   . PRO A 202 ? 0.1076 0.1436 0.1623 -0.0006 0.0266  -0.0067 202 PRO A O   
1743 C CB  . PRO A 202 ? 0.1177 0.1346 0.1599 -0.0151 0.0221  0.0028  202 PRO A CB  
1744 C CG  . PRO A 202 ? 0.1367 0.1448 0.1745 -0.0159 0.0209  0.0049  202 PRO A CG  
1745 C CD  . PRO A 202 ? 0.1215 0.1201 0.1627 -0.0067 0.0211  0.0020  202 PRO A CD  
1746 N N   . ILE A 203 ? 0.1462 0.1615 0.1988 -0.0008 0.0219  -0.0031 203 ILE A N   
1747 C CA  . ILE A 203 ? 0.1097 0.1313 0.1662 0.0006  0.0212  -0.0049 203 ILE A CA  
1748 C C   . ILE A 203 ? 0.0840 0.1097 0.1406 0.0068  0.0221  -0.0051 203 ILE A C   
1749 O O   . ILE A 203 ? 0.1041 0.1395 0.1640 0.0085  0.0216  -0.0058 203 ILE A O   
1750 C CB  . ILE A 203 ? 0.1102 0.1262 0.1699 -0.0008 0.0180  -0.0073 203 ILE A CB  
1751 C CG1 . ILE A 203 ? 0.1398 0.1496 0.2030 -0.0070 0.0136  -0.0064 203 ILE A CG1 
1752 C CG2 . ILE A 203 ? 0.1480 0.1738 0.2104 0.0002  0.0180  -0.0107 203 ILE A CG2 
1753 C CD1 . ILE A 203 ? 0.1563 0.1607 0.2283 -0.0069 0.0087  -0.0122 203 ILE A CD1 
1754 N N   . LEU A 204 ? 0.0834 0.1011 0.1371 0.0097  0.0220  -0.0038 204 LEU A N   
1755 C CA  . LEU A 204 ? 0.1626 0.1807 0.2167 0.0142  0.0201  -0.0016 204 LEU A CA  
1756 C C   . LEU A 204 ? 0.1358 0.1598 0.1963 0.0189  0.0196  -0.0038 204 LEU A C   
1757 O O   . LEU A 204 ? 0.1510 0.1787 0.2161 0.0227  0.0156  -0.0025 204 LEU A O   
1758 C CB  . LEU A 204 ? 0.1667 0.1740 0.2167 0.0148  0.0196  0.0006  204 LEU A CB  
1759 C CG  . LEU A 204 ? 0.1144 0.1203 0.1601 0.0104  0.0200  0.0003  204 LEU A CG  
1760 C CD1 . LEU A 204 ? 0.1592 0.1572 0.2005 0.0101  0.0191  0.0034  204 LEU A CD1 
1761 C CD2 . LEU A 204 ? 0.1510 0.1676 0.1963 0.0071  0.0188  -0.0002 204 LEU A CD2 
1762 N N   . LEU A 205 ? 0.0998 0.1266 0.1617 0.0182  0.0228  -0.0079 205 LEU A N   
1763 C CA  . LEU A 205 ? 0.0958 0.1338 0.1665 0.0225  0.0231  -0.0141 205 LEU A CA  
1764 C C   . LEU A 205 ? 0.1357 0.1895 0.2106 0.0204  0.0238  -0.0166 205 LEU A C   
1765 O O   . LEU A 205 ? 0.1167 0.1811 0.2017 0.0261  0.0217  -0.0216 205 LEU A O   
1766 C CB  . LEU A 205 ? 0.0872 0.1295 0.1573 0.0202  0.0272  -0.0196 205 LEU A CB  
1767 C CG  . LEU A 205 ? 0.1367 0.1659 0.2055 0.0235  0.0264  -0.0197 205 LEU A CG  
1768 C CD1 . LEU A 205 ? 0.1306 0.1672 0.1972 0.0192  0.0309  -0.0254 205 LEU A CD1 
1769 C CD2 . LEU A 205 ? 0.1741 0.1998 0.2543 0.0329  0.0211  -0.0230 205 LEU A CD2 
1770 N N   . ASN A 206 ? 0.1002 0.1556 0.1691 0.0125  0.0257  -0.0139 206 ASN A N   
1771 C CA  . ASN A 206 ? 0.0953 0.1662 0.1677 0.0085  0.0266  -0.0163 206 ASN A CA  
1772 C C   . ASN A 206 ? 0.1126 0.1775 0.1797 0.0008  0.0258  -0.0117 206 ASN A C   
1773 O O   . ASN A 206 ? 0.1344 0.1962 0.1971 -0.0073 0.0262  -0.0094 206 ASN A O   
1774 C CB  . ASN A 206 ? 0.1264 0.2142 0.2010 0.0039  0.0307  -0.0225 206 ASN A CB  
1775 C CG  . ASN A 206 ? 0.2371 0.3421 0.3134 -0.0036 0.0320  -0.0242 206 ASN A CG  
1776 O OD1 . ASN A 206 ? 0.1770 0.2830 0.2562 -0.0019 0.0297  -0.0229 206 ASN A OD1 
1777 N ND2 . ASN A 206 ? 0.2696 0.3895 0.3428 -0.0138 0.0357  -0.0266 206 ASN A ND2 
1778 N N   . PRO A 207 ? 0.1167 0.1803 0.1851 0.0026  0.0233  -0.0106 207 PRO A N   
1779 C CA  . PRO A 207 ? 0.1265 0.1850 0.1938 -0.0036 0.0216  -0.0097 207 PRO A CA  
1780 C C   . PRO A 207 ? 0.1828 0.2476 0.2512 -0.0124 0.0215  -0.0097 207 PRO A C   
1781 O O   . PRO A 207 ? 0.2186 0.2738 0.2872 -0.0185 0.0182  -0.0081 207 PRO A O   
1782 C CB  . PRO A 207 ? 0.1334 0.1977 0.2029 -0.0005 0.0198  -0.0111 207 PRO A CB  
1783 C CG  . PRO A 207 ? 0.1335 0.1967 0.2018 0.0066  0.0190  -0.0088 207 PRO A CG  
1784 C CD  . PRO A 207 ? 0.1612 0.2275 0.2327 0.0096  0.0206  -0.0102 207 PRO A CD  
1785 N N   . ASN A 208 ? 0.0912 0.1724 0.1616 -0.0139 0.0241  -0.0119 208 ASN A N   
1786 C CA  . ASN A 208 ? 0.1282 0.2184 0.1982 -0.0252 0.0242  -0.0112 208 ASN A CA  
1787 C C   . ASN A 208 ? 0.1265 0.2110 0.1897 -0.0351 0.0237  -0.0061 208 ASN A C   
1788 O O   . ASN A 208 ? 0.1211 0.2104 0.1819 -0.0477 0.0220  -0.0026 208 ASN A O   
1789 C CB  . ASN A 208 ? 0.1363 0.2508 0.2116 -0.0247 0.0275  -0.0170 208 ASN A CB  
1790 C CG  . ASN A 208 ? 0.1490 0.2696 0.2309 -0.0170 0.0259  -0.0202 208 ASN A CG  
1791 O OD1 . ASN A 208 ? 0.2028 0.3155 0.2844 -0.0180 0.0231  -0.0185 208 ASN A OD1 
1792 N ND2 . ASN A 208 ? 0.2324 0.3683 0.3217 -0.0092 0.0267  -0.0257 208 ASN A ND2 
1793 N N   . CYS A 209 ? 0.1578 0.2323 0.2171 -0.0311 0.0242  -0.0046 209 CYS A N   
1794 C CA  . CYS A 209 ? 0.1851 0.2548 0.2369 -0.0416 0.0225  0.0015  209 CYS A CA  
1795 C C   . CYS A 209 ? 0.1324 0.1828 0.1837 -0.0491 0.0141  0.0091  209 CYS A C   
1796 O O   . CYS A 209 ? 0.1274 0.1743 0.1725 -0.0616 0.0098  0.0170  209 CYS A O   
1797 C CB  . CYS A 209 ? 0.2040 0.2679 0.2526 -0.0352 0.0246  0.0005  209 CYS A CB  
1798 S SG  . CYS A 209 ? 0.2103 0.2492 0.2602 -0.0265 0.0203  0.0028  209 CYS A SG  
1799 N N   . VAL A 210 ? 0.1421 0.1818 0.2009 -0.0430 0.0106  0.0064  210 VAL A N   
1800 C CA  . VAL A 210 ? 0.1619 0.1835 0.2254 -0.0488 0.0010  0.0103  210 VAL A CA  
1801 C C   . VAL A 210 ? 0.1428 0.1685 0.2050 -0.0635 -0.0032 0.0161  210 VAL A C   
1802 O O   . VAL A 210 ? 0.1470 0.1566 0.2106 -0.0730 -0.0135 0.0237  210 VAL A O   
1803 C CB  . VAL A 210 ? 0.1677 0.1831 0.2419 -0.0396 -0.0010 0.0020  210 VAL A CB  
1804 C CG1 . VAL A 210 ? 0.1684 0.1823 0.2420 -0.0280 0.0031  -0.0026 210 VAL A CG1 
1805 C CG2 . VAL A 210 ? 0.2184 0.2488 0.2962 -0.0393 0.0024  -0.0033 210 VAL A CG2 
1806 N N   . TYR A 211 ? 0.1399 0.1873 0.2003 -0.0665 0.0034  0.0129  211 TYR A N   
1807 C CA  . TYR A 211 ? 0.1410 0.1952 0.1995 -0.0824 -0.0001 0.0182  211 TYR A CA  
1808 C C   . TYR A 211 ? 0.1983 0.2592 0.2452 -0.0983 -0.0012 0.0278  211 TYR A C   
1809 O O   . TYR A 211 ? 0.2449 0.3106 0.2873 -0.1128 -0.0049 0.0337  211 TYR A O   
1810 C CB  . TYR A 211 ? 0.1327 0.2114 0.1943 -0.0805 0.0074  0.0103  211 TYR A CB  
1811 C CG  . TYR A 211 ? 0.1593 0.2317 0.2309 -0.0691 0.0063  0.0029  211 TYR A CG  
1812 C CD1 . TYR A 211 ? 0.2408 0.2963 0.3195 -0.0733 -0.0024 0.0038  211 TYR A CD1 
1813 C CD2 . TYR A 211 ? 0.2215 0.3036 0.2959 -0.0546 0.0124  -0.0048 211 TYR A CD2 
1814 C CE1 . TYR A 211 ? 0.2237 0.2770 0.3116 -0.0642 -0.0031 -0.0050 211 TYR A CE1 
1815 C CE2 . TYR A 211 ? 0.1984 0.2776 0.2797 -0.0469 0.0110  -0.0107 211 TYR A CE2 
1816 C CZ  . TYR A 211 ? 0.2573 0.3241 0.3451 -0.0518 0.0043  -0.0118 211 TYR A CZ  
1817 O OH  . TYR A 211 ? 0.3912 0.4597 0.4864 -0.0454 0.0035  -0.0202 211 TYR A OH  
1818 N N   . GLU A 212 ? 0.1642 0.2261 0.2046 -0.0951 0.0020  0.0289  212 GLU A N   
1819 C CA  . GLU A 212 ? 0.1668 0.2345 0.1939 -0.1102 -0.0002 0.0379  212 GLU A CA  
1820 C C   . GLU A 212 ? 0.2737 0.3134 0.2972 -0.1164 -0.0148 0.0501  212 GLU A C   
1821 O O   . GLU A 212 ? 0.2911 0.3340 0.3014 -0.1281 -0.0196 0.0583  212 GLU A O   
1822 C CB  . GLU A 212 ? 0.2296 0.3070 0.2520 -0.1055 0.0067  0.0344  212 GLU A CB  
1823 C CG  . GLU A 212 ? 0.2360 0.3410 0.2629 -0.0956 0.0192  0.0197  212 GLU A CG  
1824 C CD  . GLU A 212 ? 0.3434 0.4538 0.3688 -0.0865 0.0251  0.0132  212 GLU A CD  
1825 O OE1 . GLU A 212 ? 0.3918 0.5086 0.4260 -0.0708 0.0310  0.0017  212 GLU A OE1 
1826 O OE2 . GLU A 212 ? 0.3577 0.4656 0.3737 -0.0955 0.0227  0.0198  212 GLU A OE2 
1827 N N   . THR A 213 ? 0.2698 0.2838 0.3056 -0.1083 -0.0229 0.0502  213 THR A N   
1828 C CA  . THR A 213 ? 0.2239 0.2120 0.2604 -0.1103 -0.0378 0.0588  213 THR A CA  
1829 C C   . THR A 213 ? 0.2909 0.2634 0.3414 -0.1074 -0.0459 0.0555  213 THR A C   
1830 O O   . THR A 213 ? 0.3924 0.3504 0.4422 -0.1130 -0.0581 0.0633  213 THR A O   
1831 C CB  . THR A 213 ? 0.2396 0.2109 0.2798 -0.1007 -0.0425 0.0592  213 THR A CB  
1832 O OG1 . THR A 213 ? 0.2808 0.2500 0.3348 -0.0878 -0.0370 0.0479  213 THR A OG1 
1833 C CG2 . THR A 213 ? 0.2060 0.1903 0.2314 -0.1058 -0.0375 0.0640  213 THR A CG2 
1834 N N   . THR A 214 ? 0.2060 0.1821 0.2699 -0.0990 -0.0405 0.0439  214 THR A N   
1835 C CA  . THR A 214 ? 0.2128 0.1767 0.2913 -0.0952 -0.0475 0.0373  214 THR A CA  
1836 C C   . THR A 214 ? 0.1876 0.1726 0.2692 -0.0988 -0.0389 0.0307  214 THR A C   
1837 O O   . THR A 214 ? 0.2363 0.2314 0.3254 -0.0872 -0.0315 0.0191  214 THR A O   
1838 C CB  . THR A 214 ? 0.2315 0.1817 0.3259 -0.0799 -0.0513 0.0265  214 THR A CB  
1839 O OG1 . THR A 214 ? 0.1937 0.1586 0.2896 -0.0711 -0.0398 0.0182  214 THR A OG1 
1840 C CG2 . THR A 214 ? 0.2653 0.1979 0.3580 -0.0759 -0.0607 0.0326  214 THR A CG2 
1841 N N   . PRO A 215 ? 0.2736 0.2687 0.3464 -0.1109 -0.0382 0.0364  215 PRO A N   
1842 C CA  . PRO A 215 ? 0.2491 0.2686 0.3240 -0.1137 -0.0293 0.0294  215 PRO A CA  
1843 C C   . PRO A 215 ? 0.3056 0.3205 0.3976 -0.1083 -0.0327 0.0188  215 PRO A C   
1844 O O   . PRO A 215 ? 0.2903 0.3266 0.3840 -0.1035 -0.0237 0.0100  215 PRO A O   
1845 C CB  . PRO A 215 ? 0.2753 0.3032 0.3373 -0.1280 -0.0302 0.0380  215 PRO A CB  
1846 C CG  . PRO A 215 ? 0.3507 0.3526 0.4080 -0.1331 -0.0435 0.0496  215 PRO A CG  
1847 C CD  . PRO A 215 ? 0.2725 0.2601 0.3326 -0.1228 -0.0459 0.0496  215 PRO A CD  
1848 N N   . ASN A 216 ? 0.2231 0.2126 0.3250 -0.1041 -0.0437 0.0166  216 ASN A N   
1849 C CA  . ASN A 216 ? 0.3445 0.3315 0.4622 -0.0992 -0.0470 0.0040  216 ASN A CA  
1850 C C   . ASN A 216 ? 0.3450 0.3344 0.4764 -0.0838 -0.0444 -0.0105 216 ASN A C   
1851 O O   . ASN A 216 ? 0.3865 0.3795 0.5299 -0.0782 -0.0451 -0.0238 216 ASN A O   
1852 C CB  . ASN A 216 ? 0.4389 0.4011 0.5612 -0.1015 -0.0600 0.0067  216 ASN A CB  
1853 C CG  . ASN A 216 ? 0.5776 0.5413 0.6908 -0.1170 -0.0626 0.0176  216 ASN A CG  
1854 O OD1 . ASN A 216 ? 0.6342 0.6204 0.7405 -0.1247 -0.0536 0.0183  216 ASN A OD1 
1855 N ND2 . ASN A 216 ? 0.6587 0.6001 0.7726 -0.1211 -0.0757 0.0262  216 ASN A ND2 
1856 N N   . VAL A 217 ? 0.2469 0.2376 0.3716 -0.0751 -0.0389 -0.0091 217 VAL A N   
1857 C CA  . VAL A 217 ? 0.2604 0.2544 0.3926 -0.0600 -0.0349 -0.0224 217 VAL A CA  
1858 C C   . VAL A 217 ? 0.2596 0.2796 0.3878 -0.0542 -0.0232 -0.0310 217 VAL A C   
1859 O O   . VAL A 217 ? 0.2266 0.2624 0.3435 -0.0575 -0.0157 -0.0253 217 VAL A O   
1860 C CB  . VAL A 217 ? 0.2239 0.2115 0.3482 -0.0538 -0.0326 -0.0172 217 VAL A CB  
1861 C CG1 . VAL A 217 ? 0.2905 0.2953 0.3971 -0.0527 -0.0203 -0.0107 217 VAL A CG1 
1862 C CG2 . VAL A 217 ? 0.3101 0.2972 0.4448 -0.0415 -0.0322 -0.0305 217 VAL A CG2 
1863 N N   . LYS A 218 ? 0.2019 0.2284 0.3408 -0.0465 -0.0227 -0.0456 218 LYS A N   
1864 C CA  . LYS A 218 ? 0.1679 0.2191 0.3019 -0.0414 -0.0131 -0.0525 218 LYS A CA  
1865 C C   . LYS A 218 ? 0.1358 0.1919 0.2615 -0.0327 -0.0069 -0.0520 218 LYS A C   
1866 O O   . LYS A 218 ? 0.1557 0.2021 0.2875 -0.0285 -0.0100 -0.0569 218 LYS A O   
1867 C CB  . LYS A 218 ? 0.1782 0.2391 0.3268 -0.0408 -0.0157 -0.0690 218 LYS A CB  
1868 C CG  . LYS A 218 ? 0.1836 0.2406 0.3411 -0.0498 -0.0219 -0.0705 218 LYS A CG  
1869 C CD  . LYS A 218 ? 0.2524 0.3206 0.4218 -0.0475 -0.0231 -0.0878 218 LYS A CD  
1870 C CE  . LYS A 218 ? 0.3770 0.4350 0.5522 -0.0545 -0.0302 -0.0872 218 LYS A CE  
1871 N NZ  . LYS A 218 ? 0.4955 0.5676 0.6782 -0.0512 -0.0288 -0.1031 218 LYS A NZ  
1872 N N   . ILE A 219 ? 0.1074 0.1779 0.2208 -0.0301 0.0006  -0.0461 219 ILE A N   
1873 C CA  . ILE A 219 ? 0.1022 0.1772 0.2081 -0.0232 0.0052  -0.0453 219 ILE A CA  
1874 C C   . ILE A 219 ? 0.1532 0.2499 0.2545 -0.0217 0.0092  -0.0475 219 ILE A C   
1875 O O   . ILE A 219 ? 0.1417 0.2498 0.2436 -0.0246 0.0096  -0.0474 219 ILE A O   
1876 C CB  . ILE A 219 ? 0.1334 0.1994 0.2292 -0.0210 0.0077  -0.0338 219 ILE A CB  
1877 C CG1 . ILE A 219 ? 0.1761 0.2543 0.2659 -0.0214 0.0114  -0.0280 219 ILE A CG1 
1878 C CG2 . ILE A 219 ? 0.1671 0.2138 0.2653 -0.0250 0.0028  -0.0293 219 ILE A CG2 
1879 C CD1 . ILE A 219 ? 0.2078 0.2825 0.2902 -0.0180 0.0144  -0.0208 219 ILE A CD1 
1880 N N   . PRO A 220 ? 0.0975 0.2010 0.1938 -0.0186 0.0113  -0.0488 220 PRO A N   
1881 C CA  . PRO A 220 ? 0.1154 0.2390 0.2053 -0.0191 0.0130  -0.0477 220 PRO A CA  
1882 C C   . PRO A 220 ? 0.0910 0.2156 0.1736 -0.0157 0.0133  -0.0359 220 PRO A C   
1883 O O   . PRO A 220 ? 0.1105 0.2233 0.1925 -0.0129 0.0139  -0.0301 220 PRO A O   
1884 C CB  . PRO A 220 ? 0.2016 0.3308 0.2869 -0.0192 0.0141  -0.0506 220 PRO A CB  
1885 C CG  . PRO A 220 ? 0.2195 0.3298 0.3069 -0.0160 0.0141  -0.0501 220 PRO A CG  
1886 C CD  . PRO A 220 ? 0.1506 0.2465 0.2478 -0.0163 0.0112  -0.0526 220 PRO A CD  
1887 N N   . ASP A 221 ? 0.0954 0.2365 0.1739 -0.0165 0.0120  -0.0335 221 ASP A N   
1888 C CA  . ASP A 221 ? 0.0937 0.2379 0.1695 -0.0122 0.0096  -0.0242 221 ASP A CA  
1889 C C   . ASP A 221 ? 0.1133 0.2463 0.1828 -0.0079 0.0080  -0.0156 221 ASP A C   
1890 O O   . ASP A 221 ? 0.1337 0.2717 0.1961 -0.0108 0.0057  -0.0118 221 ASP A O   
1891 C CB  . ASP A 221 ? 0.1199 0.2849 0.1944 -0.0153 0.0063  -0.0238 221 ASP A CB  
1892 C CG  . ASP A 221 ? 0.1892 0.3583 0.2656 -0.0098 0.0015  -0.0159 221 ASP A CG  
1893 O OD1 . ASP A 221 ? 0.1556 0.3175 0.2379 -0.0046 0.0026  -0.0157 221 ASP A OD1 
1894 O OD2 . ASP A 221 ? 0.3108 0.4924 0.3838 -0.0113 -0.0043 -0.0106 221 ASP A OD2 
1895 N N   . PHE A 222 ? 0.0988 0.2183 0.1705 -0.0025 0.0090  -0.0126 222 PHE A N   
1896 C CA  . PHE A 222 ? 0.0891 0.1964 0.1565 0.0018  0.0071  -0.0056 222 PHE A CA  
1897 C C   . PHE A 222 ? 0.1390 0.2503 0.2083 0.0065  0.0000  0.0016  222 PHE A C   
1898 O O   . PHE A 222 ? 0.1375 0.2447 0.2141 0.0135  -0.0018 0.0019  222 PHE A O   
1899 C CB  . PHE A 222 ? 0.0853 0.1786 0.1549 0.0050  0.0108  -0.0071 222 PHE A CB  
1900 C CG  . PHE A 222 ? 0.0849 0.1686 0.1516 0.0013  0.0141  -0.0105 222 PHE A CG  
1901 C CD1 . PHE A 222 ? 0.1066 0.1917 0.1773 -0.0032 0.0156  -0.0169 222 PHE A CD1 
1902 C CD2 . PHE A 222 ? 0.1292 0.2022 0.1908 0.0025  0.0142  -0.0076 222 PHE A CD2 
1903 C CE1 . PHE A 222 ? 0.1162 0.1916 0.1881 -0.0052 0.0161  -0.0211 222 PHE A CE1 
1904 C CE2 . PHE A 222 ? 0.1521 0.2181 0.2135 0.0000  0.0163  -0.0120 222 PHE A CE2 
1905 C CZ  . PHE A 222 ? 0.1440 0.2110 0.2115 -0.0032 0.0167  -0.0190 222 PHE A CZ  
1906 N N   . ALA A 223 ? 0.1280 0.2485 0.1915 0.0020  -0.0051 0.0070  223 ALA A N   
1907 C CA  . ALA A 223 ? 0.1497 0.2743 0.2157 0.0050  -0.0152 0.0157  223 ALA A CA  
1908 C C   . ALA A 223 ? 0.1822 0.2901 0.2466 0.0085  -0.0227 0.0257  223 ALA A C   
1909 O O   . ALA A 223 ? 0.2269 0.3343 0.2943 0.0107  -0.0342 0.0349  223 ALA A O   
1910 C CB  . ALA A 223 ? 0.2114 0.3542 0.2700 -0.0038 -0.0191 0.0192  223 ALA A CB  
1911 N N   . VAL A 224 ? 0.1747 0.2684 0.2355 0.0087  -0.0177 0.0245  224 VAL A N   
1912 C CA  . VAL A 224 ? 0.1369 0.2131 0.1969 0.0114  -0.0240 0.0327  224 VAL A CA  
1913 C C   . VAL A 224 ? 0.1492 0.2132 0.2154 0.0183  -0.0172 0.0248  224 VAL A C   
1914 O O   . VAL A 224 ? 0.1620 0.2297 0.2278 0.0172  -0.0077 0.0161  224 VAL A O   
1915 C CB  . VAL A 224 ? 0.2460 0.3217 0.2907 0.0000  -0.0249 0.0406  224 VAL A CB  
1916 C CG1 . VAL A 224 ? 0.2056 0.2798 0.2456 -0.0031 -0.0135 0.0317  224 VAL A CG1 
1917 C CG2 . VAL A 224 ? 0.4043 0.4639 0.4473 -0.0004 -0.0365 0.0539  224 VAL A CG2 
1918 N N   . SER A 225 ? 0.1567 0.2061 0.2292 0.0247  -0.0234 0.0279  225 SER A N   
1919 C CA  . SER A 225 ? 0.1240 0.1643 0.2024 0.0305  -0.0176 0.0199  225 SER A CA  
1920 C C   . SER A 225 ? 0.1357 0.1628 0.2035 0.0254  -0.0147 0.0237  225 SER A C   
1921 O O   . SER A 225 ? 0.1848 0.2029 0.2472 0.0217  -0.0222 0.0337  225 SER A O   
1922 C CB  . SER A 225 ? 0.1909 0.2254 0.2861 0.0414  -0.0257 0.0168  225 SER A CB  
1923 O OG  . SER A 225 ? 0.1734 0.2010 0.2729 0.0453  -0.0201 0.0085  225 SER A OG  
1924 N N   . PHE A 226 ? 0.1210 0.1477 0.1859 0.0243  -0.0049 0.0164  226 PHE A N   
1925 C CA  . PHE A 226 ? 0.1215 0.1372 0.1790 0.0209  -0.0016 0.0175  226 PHE A CA  
1926 C C   . PHE A 226 ? 0.1104 0.1164 0.1749 0.0273  -0.0004 0.0124  226 PHE A C   
1927 O O   . PHE A 226 ? 0.1597 0.1578 0.2189 0.0250  0.0033  0.0116  226 PHE A O   
1928 C CB  . PHE A 226 ? 0.1138 0.1355 0.1649 0.0151  0.0065  0.0126  226 PHE A CB  
1929 C CG  . PHE A 226 ? 0.1601 0.1932 0.2050 0.0079  0.0061  0.0144  226 PHE A CG  
1930 C CD1 . PHE A 226 ? 0.1795 0.2132 0.2156 0.0008  0.0045  0.0191  226 PHE A CD1 
1931 C CD2 . PHE A 226 ? 0.1846 0.2305 0.2324 0.0068  0.0077  0.0101  226 PHE A CD2 
1932 C CE1 . PHE A 226 ? 0.1495 0.1998 0.1801 -0.0074 0.0049  0.0182  226 PHE A CE1 
1933 C CE2 . PHE A 226 ? 0.2215 0.2811 0.2648 -0.0002 0.0077  0.0090  226 PHE A CE2 
1934 C CZ  . PHE A 226 ? 0.1626 0.2259 0.1974 -0.0074 0.0066  0.0123  226 PHE A CZ  
1935 N N   . ARG A 227 ? 0.1278 0.1367 0.2050 0.0351  -0.0037 0.0073  227 ARG A N   
1936 C CA  . ARG A 227 ? 0.1473 0.1529 0.2325 0.0404  -0.0013 -0.0013 227 ARG A CA  
1937 C C   . ARG A 227 ? 0.1754 0.1632 0.2614 0.0419  -0.0071 0.0025  227 ARG A C   
1938 O O   . ARG A 227 ? 0.1885 0.1716 0.2732 0.0417  -0.0024 -0.0024 227 ARG A O   
1939 C CB  . ARG A 227 ? 0.1952 0.2132 0.2972 0.0484  -0.0037 -0.0112 227 ARG A CB  
1940 C CG  . ARG A 227 ? 0.2081 0.2457 0.3089 0.0449  0.0034  -0.0162 227 ARG A CG  
1941 C CD  . ARG A 227 ? 0.2467 0.3013 0.3650 0.0520  0.0017  -0.0280 227 ARG A CD  
1942 N NE  . ARG A 227 ? 0.2667 0.3254 0.3948 0.0562  0.0041  -0.0403 227 ARG A NE  
1943 C CZ  . ARG A 227 ? 0.3379 0.4105 0.4616 0.0501  0.0137  -0.0479 227 ARG A CZ  
1944 N NH1 . ARG A 227 ? 0.2284 0.3078 0.3387 0.0400  0.0202  -0.0428 227 ARG A NH1 
1945 N NH2 . ARG A 227 ? 0.4015 0.4795 0.5308 0.0518  0.0154  -0.0589 227 ARG A NH2 
1946 N N   . GLU A 228 ? 0.1472 0.1246 0.2351 0.0423  -0.0182 0.0120  228 GLU A N   
1947 C CA  . GLU A 228 ? 0.1920 0.1506 0.2800 0.0417  -0.0250 0.0173  228 GLU A CA  
1948 C C   . GLU A 228 ? 0.1783 0.1333 0.2490 0.0316  -0.0182 0.0226  228 GLU A C   
1949 O O   . GLU A 228 ? 0.1916 0.1361 0.2615 0.0310  -0.0172 0.0209  228 GLU A O   
1950 C CB  . GLU A 228 ? 0.2220 0.1691 0.3149 0.0418  -0.0409 0.0293  228 GLU A CB  
1951 C CG  . GLU A 228 ? 0.4591 0.3847 0.5489 0.0370  -0.0499 0.0390  228 GLU A CG  
1952 C CD  . GLU A 228 ? 0.7672 0.6829 0.8716 0.0452  -0.0544 0.0285  228 GLU A CD  
1953 O OE1 . GLU A 228 ? 0.8336 0.7575 0.9441 0.0510  -0.0448 0.0131  228 GLU A OE1 
1954 O OE2 . GLU A 228 ? 0.8840 0.7870 0.9916 0.0434  -0.0668 0.0349  228 GLU A OE2 
1955 N N   . ASP A 229 ? 0.1765 0.1421 0.2350 0.0238  -0.0136 0.0271  229 ASP A N   
1956 C CA  . ASP A 229 ? 0.1513 0.1178 0.1970 0.0153  -0.0072 0.0285  229 ASP A CA  
1957 C C   . ASP A 229 ? 0.1736 0.1402 0.2204 0.0181  0.0017  0.0187  229 ASP A C   
1958 O O   . ASP A 229 ? 0.1748 0.1354 0.2164 0.0145  0.0040  0.0187  229 ASP A O   
1959 C CB  . ASP A 229 ? 0.1284 0.1103 0.1654 0.0079  -0.0039 0.0302  229 ASP A CB  
1960 C CG  . ASP A 229 ? 0.1793 0.1634 0.2090 -0.0006 -0.0122 0.0421  229 ASP A CG  
1961 O OD1 . ASP A 229 ? 0.2565 0.2267 0.2876 -0.0011 -0.0220 0.0512  229 ASP A OD1 
1962 O OD2 . ASP A 229 ? 0.2085 0.2088 0.2313 -0.0078 -0.0098 0.0424  229 ASP A OD2 
1963 N N   . ALA A 230 ? 0.1444 0.1193 0.1972 0.0230  0.0062  0.0110  230 ALA A N   
1964 C CA  . ALA A 230 ? 0.1640 0.1400 0.2168 0.0237  0.0129  0.0038  230 ALA A CA  
1965 C C   . ALA A 230 ? 0.1299 0.0956 0.1866 0.0267  0.0113  0.0010  230 ALA A C   
1966 O O   . ALA A 230 ? 0.1718 0.1336 0.2234 0.0238  0.0148  -0.0004 230 ALA A O   
1967 C CB  . ALA A 230 ? 0.1859 0.1740 0.2443 0.0262  0.0163  -0.0027 230 ALA A CB  
1968 N N   . SER A 231 ? 0.1510 0.1121 0.2186 0.0329  0.0048  -0.0007 231 SER A N   
1969 C CA  . SER A 231 ? 0.1629 0.1132 0.2377 0.0365  0.0016  -0.0051 231 SER A CA  
1970 C C   . SER A 231 ? 0.2145 0.1505 0.2803 0.0301  -0.0013 0.0037  231 SER A C   
1971 O O   . SER A 231 ? 0.2236 0.1540 0.2885 0.0291  0.0011  -0.0002 231 SER A O   
1972 C CB  . SER A 231 ? 0.2378 0.1837 0.3301 0.0452  -0.0082 -0.0087 231 SER A CB  
1973 O OG  . SER A 231 ? 0.3778 0.3388 0.4809 0.0510  -0.0043 -0.0232 231 SER A OG  
1974 N N   . LYS A 232 ? 0.1774 0.1099 0.2362 0.0245  -0.0065 0.0152  232 LYS A N   
1975 C CA  . LYS A 232 ? 0.1923 0.1154 0.2414 0.0156  -0.0094 0.0240  232 LYS A CA  
1976 C C   . LYS A 232 ? 0.1982 0.1284 0.2375 0.0102  0.0003  0.0201  232 LYS A C   
1977 O O   . LYS A 232 ? 0.1813 0.1040 0.2173 0.0062  0.0004  0.0206  232 LYS A O   
1978 C CB  . LYS A 232 ? 0.2168 0.1417 0.2581 0.0076  -0.0160 0.0367  232 LYS A CB  
1979 C CG  . LYS A 232 ? 0.3438 0.2560 0.3947 0.0110  -0.0303 0.0444  232 LYS A CG  
1980 C CD  . LYS A 232 ? 0.4382 0.3509 0.4774 -0.0013 -0.0387 0.0607  232 LYS A CD  
1981 C CE  . LYS A 232 ? 0.6204 0.5333 0.6447 -0.0155 -0.0361 0.0669  232 LYS A CE  
1982 N NZ  . LYS A 232 ? 0.7471 0.6486 0.7644 -0.0280 -0.0505 0.0849  232 LYS A NZ  
1983 N N   . HIS A 233 ? 0.1705 0.1145 0.2065 0.0100  0.0073  0.0161  233 HIS A N   
1984 C CA  . HIS A 233 ? 0.1624 0.1120 0.1931 0.0065  0.0140  0.0116  233 HIS A CA  
1985 C C   . HIS A 233 ? 0.1407 0.0840 0.1744 0.0098  0.0164  0.0057  233 HIS A C   
1986 O O   . HIS A 233 ? 0.1606 0.1019 0.1902 0.0058  0.0182  0.0048  233 HIS A O   
1987 C CB  . HIS A 233 ? 0.1568 0.1182 0.1879 0.0075  0.0185  0.0072  233 HIS A CB  
1988 C CG  . HIS A 233 ? 0.1544 0.1265 0.1821 0.0025  0.0181  0.0092  233 HIS A CG  
1989 N ND1 . HIS A 233 ? 0.1590 0.1397 0.1832 -0.0036 0.0203  0.0063  233 HIS A ND1 
1990 C CD2 . HIS A 233 ? 0.1515 0.1304 0.1802 0.0026  0.0162  0.0116  233 HIS A CD2 
1991 C CE1 . HIS A 233 ? 0.1325 0.1259 0.1554 -0.0075 0.0201  0.0061  233 HIS A CE1 
1992 N NE2 . HIS A 233 ? 0.1328 0.1245 0.1576 -0.0040 0.0175  0.0101  233 HIS A NE2 
1993 N N   . VAL A 234 ? 0.1890 0.1323 0.2303 0.0163  0.0165  0.0005  234 VAL A N   
1994 C CA  . VAL A 234 ? 0.1895 0.1316 0.2334 0.0181  0.0192  -0.0068 234 VAL A CA  
1995 C C   . VAL A 234 ? 0.1888 0.1176 0.2356 0.0180  0.0148  -0.0065 234 VAL A C   
1996 O O   . VAL A 234 ? 0.1649 0.0911 0.2085 0.0151  0.0170  -0.0090 234 VAL A O   
1997 C CB  . VAL A 234 ? 0.1834 0.1351 0.2349 0.0231  0.0212  -0.0148 234 VAL A CB  
1998 C CG1 . VAL A 234 ? 0.1882 0.1431 0.2415 0.0231  0.0244  -0.0235 234 VAL A CG1 
1999 C CG2 . VAL A 234 ? 0.1597 0.1231 0.2069 0.0207  0.0248  -0.0133 234 VAL A CG2 
2000 N N   . GLU A 235 ? 0.1395 0.0589 0.1933 0.0207  0.0070  -0.0028 235 GLU A N   
2001 C CA  . GLU A 235 ? 0.1544 0.0577 0.2138 0.0204  -0.0001 -0.0020 235 GLU A CA  
2002 C C   . GLU A 235 ? 0.2206 0.1180 0.2679 0.0101  -0.0003 0.0066  235 GLU A C   
2003 O O   . GLU A 235 ? 0.2245 0.1145 0.2720 0.0076  -0.0005 0.0040  235 GLU A O   
2004 C CB  . GLU A 235 ? 0.2040 0.0999 0.2706 0.0241  -0.0109 0.0023  235 GLU A CB  
2005 C CG  . GLU A 235 ? 0.4702 0.3710 0.5501 0.0330  -0.0133 -0.0100 235 GLU A CG  
2006 C CD  . GLU A 235 ? 0.5887 0.4874 0.6711 0.0330  -0.0118 -0.0189 235 GLU A CD  
2007 O OE1 . GLU A 235 ? 0.6195 0.5317 0.7086 0.0374  -0.0068 -0.0321 235 GLU A OE1 
2008 O OE2 . GLU A 235 ? 0.6810 0.5662 0.7586 0.0274  -0.0158 -0.0126 235 GLU A OE2 
2009 N N   . LEU A 236 ? 0.1624 0.0662 0.1997 0.0032  0.0001  0.0156  236 LEU A N   
2010 C CA  . LEU A 236 ? 0.1872 0.0916 0.2134 -0.0082 0.0006  0.0218  236 LEU A CA  
2011 C C   . LEU A 236 ? 0.1783 0.0914 0.2010 -0.0092 0.0092  0.0136  236 LEU A C   
2012 O O   . LEU A 236 ? 0.1756 0.0866 0.1936 -0.0166 0.0093  0.0148  236 LEU A O   
2013 C CB  . LEU A 236 ? 0.1893 0.1053 0.2065 -0.0161 0.0002  0.0297  236 LEU A CB  
2014 C CG  . LEU A 236 ? 0.2368 0.1449 0.2544 -0.0189 -0.0105 0.0415  236 LEU A CG  
2015 C CD1 . LEU A 236 ? 0.2443 0.1704 0.2526 -0.0265 -0.0086 0.0462  236 LEU A CD1 
2016 C CD2 . LEU A 236 ? 0.2751 0.1661 0.2903 -0.0278 -0.0206 0.0519  236 LEU A CD2 
2017 N N   . ALA A 237 ? 0.1578 0.0809 0.1828 -0.0031 0.0152  0.0063  237 ALA A N   
2018 C CA  . ALA A 237 ? 0.1818 0.1115 0.2050 -0.0035 0.0207  -0.0003 237 ALA A CA  
2019 C C   . ALA A 237 ? 0.1687 0.0902 0.1951 -0.0020 0.0204  -0.0050 237 ALA A C   
2020 O O   . ALA A 237 ? 0.1875 0.1105 0.2108 -0.0062 0.0224  -0.0073 237 ALA A O   
2021 C CB  . ALA A 237 ? 0.1690 0.1080 0.1942 0.0014  0.0241  -0.0045 237 ALA A CB  
2022 N N   . LYS A 238 ? 0.1926 0.1077 0.2269 0.0040  0.0180  -0.0085 238 LYS A N   
2023 C CA  . LYS A 238 ? 0.2015 0.1101 0.2412 0.0054  0.0172  -0.0156 238 LYS A CA  
2024 C C   . LYS A 238 ? 0.2175 0.1131 0.2551 -0.0013 0.0126  -0.0106 238 LYS A C   
2025 O O   . LYS A 238 ? 0.2229 0.1173 0.2596 -0.0043 0.0143  -0.0152 238 LYS A O   
2026 C CB  . LYS A 238 ? 0.1656 0.0736 0.2164 0.0132  0.0136  -0.0225 238 LYS A CB  
2027 C CG  . LYS A 238 ? 0.1771 0.1013 0.2301 0.0173  0.0197  -0.0301 238 LYS A CG  
2028 C CD  . LYS A 238 ? 0.2254 0.1549 0.2897 0.0242  0.0161  -0.0376 238 LYS A CD  
2029 C CE  . LYS A 238 ? 0.3041 0.2310 0.3760 0.0261  0.0125  -0.0462 238 LYS A CE  
2030 N NZ  . LYS A 238 ? 0.3022 0.2398 0.3876 0.0324  0.0103  -0.0569 238 LYS A NZ  
2031 N N   . GLU A 239 ? 0.1937 0.0802 0.2297 -0.0055 0.0059  -0.0003 239 GLU A N   
2032 C CA  . GLU A 239 ? 0.2140 0.0884 0.2464 -0.0152 0.0001  0.0072  239 GLU A CA  
2033 C C   . GLU A 239 ? 0.2681 0.1548 0.2888 -0.0249 0.0062  0.0084  239 GLU A C   
2034 O O   . GLU A 239 ? 0.2314 0.1131 0.2502 -0.0316 0.0053  0.0080  239 GLU A O   
2035 C CB  . GLU A 239 ? 0.2431 0.1083 0.2736 -0.0197 -0.0096 0.0201  239 GLU A CB  
2036 C CG  . GLU A 239 ? 0.4143 0.2743 0.4548 -0.0086 -0.0160 0.0174  239 GLU A CG  
2037 C CD  . GLU A 239 ? 0.7048 0.5588 0.7433 -0.0132 -0.0260 0.0309  239 GLU A CD  
2038 O OE1 . GLU A 239 ? 0.7812 0.6333 0.8094 -0.0262 -0.0295 0.0423  239 GLU A OE1 
2039 O OE2 . GLU A 239 ? 0.7710 0.6251 0.8182 -0.0047 -0.0307 0.0298  239 GLU A OE2 
2040 N N   . LYS A 240 ? 0.2232 0.1271 0.2381 -0.0258 0.0118  0.0084  240 LYS A N   
2041 C CA  . LYS A 240 ? 0.1887 0.1072 0.1968 -0.0339 0.0168  0.0063  240 LYS A CA  
2042 C C   . LYS A 240 ? 0.2115 0.1330 0.2226 -0.0302 0.0212  -0.0033 240 LYS A C   
2043 O O   . LYS A 240 ? 0.2307 0.1555 0.2388 -0.0374 0.0223  -0.0051 240 LYS A O   
2044 C CB  . LYS A 240 ? 0.1657 0.1026 0.1715 -0.0341 0.0206  0.0049  240 LYS A CB  
2045 C CG  . LYS A 240 ? 0.2025 0.1585 0.2053 -0.0419 0.0249  -0.0006 240 LYS A CG  
2046 C CD  . LYS A 240 ? 0.2091 0.1707 0.2030 -0.0573 0.0228  0.0067  240 LYS A CD  
2047 C CE  . LYS A 240 ? 0.2480 0.2319 0.2407 -0.0658 0.0276  -0.0018 240 LYS A CE  
2048 N NZ  . LYS A 240 ? 0.2423 0.2356 0.2243 -0.0842 0.0258  0.0060  240 LYS A NZ  
2049 N N   . TYR A 241 ? 0.1894 0.1114 0.2055 -0.0204 0.0233  -0.0091 241 TYR A N   
2050 C CA  . TYR A 241 ? 0.1952 0.1208 0.2130 -0.0181 0.0262  -0.0168 241 TYR A CA  
2051 C C   . TYR A 241 ? 0.2248 0.1393 0.2444 -0.0211 0.0241  -0.0191 241 TYR A C   
2052 O O   . TYR A 241 ? 0.2102 0.1290 0.2282 -0.0249 0.0260  -0.0233 241 TYR A O   
2053 C CB  . TYR A 241 ? 0.1503 0.0795 0.1714 -0.0101 0.0277  -0.0205 241 TYR A CB  
2054 C CG  . TYR A 241 ? 0.1448 0.0808 0.1656 -0.0095 0.0298  -0.0266 241 TYR A CG  
2055 C CD1 . TYR A 241 ? 0.1565 0.0892 0.1795 -0.0095 0.0302  -0.0329 241 TYR A CD1 
2056 C CD2 . TYR A 241 ? 0.1619 0.1077 0.1812 -0.0092 0.0299  -0.0264 241 TYR A CD2 
2057 C CE1 . TYR A 241 ? 0.2353 0.1773 0.2565 -0.0106 0.0319  -0.0381 241 TYR A CE1 
2058 C CE2 . TYR A 241 ? 0.1684 0.1203 0.1863 -0.0101 0.0298  -0.0296 241 TYR A CE2 
2059 C CZ  . TYR A 241 ? 0.1581 0.1095 0.1757 -0.0114 0.0313  -0.0351 241 TYR A CZ  
2060 O OH  . TYR A 241 ? 0.2032 0.1637 0.2178 -0.0140 0.0310  -0.0378 241 TYR A OH  
2061 N N   . PHE A 242 ? 0.1972 0.0971 0.2219 -0.0192 0.0192  -0.0171 242 PHE A N   
2062 C CA  . PHE A 242 ? 0.2705 0.1566 0.3002 -0.0218 0.0150  -0.0200 242 PHE A CA  
2063 C C   . PHE A 242 ? 0.2446 0.1280 0.2672 -0.0341 0.0132  -0.0137 242 PHE A C   
2064 O O   . PHE A 242 ? 0.2720 0.1525 0.2955 -0.0382 0.0134  -0.0185 242 PHE A O   
2065 C CB  . PHE A 242 ? 0.2578 0.1309 0.2947 -0.0161 0.0064  -0.0178 242 PHE A CB  
2066 C CG  . PHE A 242 ? 0.3256 0.1869 0.3670 -0.0162 0.0001  -0.0215 242 PHE A CG  
2067 C CD1 . PHE A 242 ? 0.3730 0.2413 0.4196 -0.0121 0.0031  -0.0341 242 PHE A CD1 
2068 C CD2 . PHE A 242 ? 0.4963 0.3412 0.5375 -0.0206 -0.0086 -0.0125 242 PHE A CD2 
2069 C CE1 . PHE A 242 ? 0.4721 0.3304 0.5249 -0.0118 -0.0023 -0.0389 242 PHE A CE1 
2070 C CE2 . PHE A 242 ? 0.5444 0.3783 0.5925 -0.0202 -0.0143 -0.0163 242 PHE A CE2 
2071 C CZ  . PHE A 242 ? 0.5070 0.3471 0.5613 -0.0154 -0.0112 -0.0302 242 PHE A CZ  
2072 N N   . GLU A 243 ? 0.2260 0.1127 0.2412 -0.0417 0.0117  -0.0034 243 GLU A N   
2073 C CA  . GLU A 243 ? 0.2530 0.1434 0.2599 -0.0564 0.0108  0.0023  243 GLU A CA  
2074 C C   . GLU A 243 ? 0.3124 0.2201 0.3172 -0.0583 0.0181  -0.0069 243 GLU A C   
2075 O O   . GLU A 243 ? 0.2833 0.1901 0.2860 -0.0674 0.0176  -0.0078 243 GLU A O   
2076 C CB  . GLU A 243 ? 0.3254 0.2261 0.3238 -0.0648 0.0101  0.0119  243 GLU A CB  
2077 C CG  . GLU A 243 ? 0.4089 0.3230 0.3973 -0.0828 0.0109  0.0162  243 GLU A CG  
2078 C CD  . GLU A 243 ? 0.4899 0.4279 0.4707 -0.0904 0.0144  0.0186  243 GLU A CD  
2079 O OE1 . GLU A 243 ? 0.3860 0.3228 0.3670 -0.0856 0.0124  0.0232  243 GLU A OE1 
2080 O OE2 . GLU A 243 ? 0.4443 0.4051 0.4201 -0.1018 0.0191  0.0143  243 GLU A OE2 
2081 N N   . ILE A 244 ? 0.2063 0.1291 0.2129 -0.0500 0.0236  -0.0136 244 ILE A N   
2082 C CA  . ILE A 244 ? 0.2204 0.1605 0.2272 -0.0511 0.0282  -0.0217 244 ILE A CA  
2083 C C   . ILE A 244 ? 0.2285 0.1639 0.2388 -0.0470 0.0288  -0.0288 244 ILE A C   
2084 O O   . ILE A 244 ? 0.2366 0.1785 0.2462 -0.0529 0.0300  -0.0331 244 ILE A O   
2085 C CB  . ILE A 244 ? 0.2134 0.1690 0.2232 -0.0441 0.0308  -0.0256 244 ILE A CB  
2086 C CG1 . ILE A 244 ? 0.2459 0.2101 0.2530 -0.0486 0.0309  -0.0212 244 ILE A CG1 
2087 C CG2 . ILE A 244 ? 0.2116 0.1835 0.2253 -0.0438 0.0326  -0.0345 244 ILE A CG2 
2088 C CD1 . ILE A 244 ? 0.3114 0.2877 0.3127 -0.0634 0.0316  -0.0197 244 ILE A CD1 
2089 N N   . PHE A 245 ? 0.1900 0.1176 0.2042 -0.0379 0.0283  -0.0311 245 PHE A N   
2090 C CA  . PHE A 245 ? 0.2116 0.1418 0.2283 -0.0343 0.0298  -0.0392 245 PHE A CA  
2091 C C   . PHE A 245 ? 0.2176 0.1340 0.2391 -0.0341 0.0276  -0.0436 245 PHE A C   
2092 O O   . PHE A 245 ? 0.2328 0.1540 0.2563 -0.0330 0.0292  -0.0521 245 PHE A O   
2093 C CB  . PHE A 245 ? 0.1609 0.0992 0.1784 -0.0263 0.0311  -0.0407 245 PHE A CB  
2094 C CG  . PHE A 245 ? 0.2005 0.1507 0.2170 -0.0254 0.0311  -0.0384 245 PHE A CG  
2095 C CD1 . PHE A 245 ? 0.2398 0.2009 0.2570 -0.0278 0.0306  -0.0422 245 PHE A CD1 
2096 C CD2 . PHE A 245 ? 0.1665 0.1173 0.1837 -0.0219 0.0306  -0.0339 245 PHE A CD2 
2097 C CE1 . PHE A 245 ? 0.1963 0.1680 0.2173 -0.0256 0.0286  -0.0425 245 PHE A CE1 
2098 C CE2 . PHE A 245 ? 0.1762 0.1377 0.1961 -0.0205 0.0293  -0.0343 245 PHE A CE2 
2099 C CZ  . PHE A 245 ? 0.1986 0.1701 0.2216 -0.0219 0.0278  -0.0391 245 PHE A CZ  
2100 N N   . GLY A 246 ? 0.2075 0.0945 0.3215 -0.0393 0.0242  -0.0128 246 GLY A N   
2101 C CA  . GLY A 246 ? 0.2220 0.0988 0.3420 -0.0386 0.0249  -0.0172 246 GLY A CA  
2102 C C   . GLY A 246 ? 0.3069 0.1797 0.4211 -0.0345 0.0246  -0.0243 246 GLY A C   
2103 O O   . GLY A 246 ? 0.2921 0.1561 0.4106 -0.0334 0.0251  -0.0288 246 GLY A O   
2104 N N   . GLU A 247 ? 0.2878 0.1668 0.3927 -0.0321 0.0241  -0.0256 247 GLU A N   
2105 C CA  . GLU A 247 ? 0.2717 0.1485 0.3711 -0.0278 0.0244  -0.0316 247 GLU A CA  
2106 C C   . GLU A 247 ? 0.2869 0.1687 0.3814 -0.0237 0.0266  -0.0259 247 GLU A C   
2107 O O   . GLU A 247 ? 0.2422 0.1306 0.3351 -0.0251 0.0267  -0.0200 247 GLU A O   
2108 C CB  . GLU A 247 ? 0.3529 0.2333 0.4451 -0.0299 0.0204  -0.0429 247 GLU A CB  
2109 C CG  . GLU A 247 ? 0.4100 0.3009 0.4948 -0.0326 0.0180  -0.0431 247 GLU A CG  
2110 C CD  . GLU A 247 ? 0.5804 0.4757 0.6597 -0.0352 0.0140  -0.0530 247 GLU A CD  
2111 O OE1 . GLU A 247 ? 0.5918 0.4938 0.6626 -0.0339 0.0130  -0.0566 247 GLU A OE1 
2112 O OE2 . GLU A 247 ? 0.6449 0.5375 0.7288 -0.0384 0.0120  -0.0572 247 GLU A OE2 
2113 N N   . HIS A 248 ? 0.2223 0.1011 0.3144 -0.0186 0.0284  -0.0283 248 HIS A N   
2114 C CA  . HIS A 248 ? 0.2417 0.1256 0.3291 -0.0148 0.0304  -0.0243 248 HIS A CA  
2115 C C   . HIS A 248 ? 0.2674 0.1591 0.3457 -0.0172 0.0275  -0.0309 248 HIS A C   
2116 O O   . HIS A 248 ? 0.2652 0.1574 0.3398 -0.0190 0.0249  -0.0399 248 HIS A O   
2117 C CB  . HIS A 248 ? 0.2436 0.1226 0.3322 -0.0078 0.0336  -0.0241 248 HIS A CB  
2118 C CG  . HIS A 248 ? 0.3276 0.2005 0.4245 -0.0043 0.0371  -0.0151 248 HIS A CG  
2119 N ND1 . HIS A 248 ? 0.4143 0.2782 0.5169 -0.0029 0.0379  -0.0173 248 HIS A ND1 
2120 C CD2 . HIS A 248 ? 0.3376 0.2129 0.4380 -0.0018 0.0400  -0.0035 248 HIS A CD2 
2121 C CE1 . HIS A 248 ? 0.4509 0.3117 0.5605 0.0002  0.0413  -0.0072 248 HIS A CE1 
2122 N NE2 . HIS A 248 ? 0.4034 0.2718 0.5116 0.0012  0.0427  0.0015  248 HIS A NE2 
2123 N N   . PRO A 249 ? 0.2063 0.1067 0.2793 -0.0168 0.0275  -0.0259 249 PRO A N   
2124 C CA  . PRO A 249 ? 0.1677 0.0777 0.2309 -0.0188 0.0244  -0.0305 249 PRO A CA  
2125 C C   . PRO A 249 ? 0.2798 0.1927 0.3370 -0.0148 0.0247  -0.0357 249 PRO A C   
2126 O O   . PRO A 249 ? 0.2659 0.1785 0.3238 -0.0096 0.0271  -0.0327 249 PRO A O   
2127 C CB  . PRO A 249 ? 0.2078 0.1269 0.2671 -0.0184 0.0242  -0.0224 249 PRO A CB  
2128 C CG  . PRO A 249 ? 0.1638 0.0810 0.2276 -0.0132 0.0274  -0.0146 249 PRO A CG  
2129 C CD  . PRO A 249 ? 0.1905 0.0953 0.2644 -0.0135 0.0295  -0.0150 249 PRO A CD  
2130 N N   . VAL A 250 ? 0.2353 0.1521 0.2867 -0.0169 0.0224  -0.0433 250 VAL A N   
2131 C CA  . VAL A 250 ? 0.2201 0.1426 0.2650 -0.0133 0.0227  -0.0472 250 VAL A CA  
2132 C C   . VAL A 250 ? 0.1594 0.0934 0.1964 -0.0145 0.0213  -0.0450 250 VAL A C   
2133 O O   . VAL A 250 ? 0.2325 0.1729 0.2647 -0.0117 0.0219  -0.0464 250 VAL A O   
2134 C CB  . VAL A 250 ? 0.2820 0.2012 0.3261 -0.0132 0.0219  -0.0578 250 VAL A CB  
2135 C CG1 . VAL A 250 ? 0.3135 0.2199 0.3664 -0.0115 0.0236  -0.0606 250 VAL A CG1 
2136 C CG2 . VAL A 250 ? 0.2925 0.2147 0.3343 -0.0185 0.0186  -0.0624 250 VAL A CG2 
2137 N N   . TYR A 251 ? 0.2025 0.1394 0.2387 -0.0184 0.0196  -0.0414 251 TYR A N   
2138 C CA  . TYR A 251 ? 0.1968 0.1430 0.2270 -0.0194 0.0184  -0.0384 251 TYR A CA  
2139 C C   . TYR A 251 ? 0.2106 0.1584 0.2426 -0.0191 0.0187  -0.0307 251 TYR A C   
2140 O O   . TYR A 251 ? 0.1900 0.1333 0.2267 -0.0203 0.0189  -0.0276 251 TYR A O   
2141 C CB  . TYR A 251 ? 0.2248 0.1741 0.2514 -0.0236 0.0159  -0.0413 251 TYR A CB  
2142 C CG  . TYR A 251 ? 0.2082 0.1554 0.2343 -0.0242 0.0150  -0.0494 251 TYR A CG  
2143 C CD1 . TYR A 251 ? 0.3883 0.3388 0.4104 -0.0210 0.0159  -0.0540 251 TYR A CD1 
2144 C CD2 . TYR A 251 ? 0.3078 0.2506 0.3379 -0.0277 0.0134  -0.0530 251 TYR A CD2 
2145 C CE1 . TYR A 251 ? 0.4281 0.3778 0.4492 -0.0207 0.0150  -0.0623 251 TYR A CE1 
2146 C CE2 . TYR A 251 ? 0.3138 0.2554 0.3436 -0.0281 0.0121  -0.0619 251 TYR A CE2 
2147 C CZ  . TYR A 251 ? 0.4577 0.4028 0.4825 -0.0243 0.0129  -0.0667 251 TYR A CZ  
2148 O OH  . TYR A 251 ? 0.5773 0.5224 0.6011 -0.0239 0.0115  -0.0764 251 TYR A OH  
2149 N N   . MET A 252 ? 0.1489 0.1038 0.1775 -0.0175 0.0188  -0.0278 252 MET A N   
2150 C CA  . MET A 252 ? 0.1404 0.0989 0.1697 -0.0172 0.0184  -0.0219 252 MET A CA  
2151 C C   . MET A 252 ? 0.1632 0.1287 0.1878 -0.0190 0.0168  -0.0216 252 MET A C   
2152 O O   . MET A 252 ? 0.1500 0.1194 0.1718 -0.0191 0.0168  -0.0240 252 MET A O   
2153 C CB  . MET A 252 ? 0.2048 0.1649 0.2367 -0.0126 0.0202  -0.0181 252 MET A CB  
2154 C CG  . MET A 252 ? 0.2400 0.1927 0.2778 -0.0103 0.0222  -0.0157 252 MET A CG  
2155 S SD  . MET A 252 ? 0.2099 0.1675 0.2503 -0.0046 0.0239  -0.0084 252 MET A SD  
2156 C CE  . MET A 252 ? 0.2270 0.1743 0.2752 -0.0032 0.0266  -0.0042 252 MET A CE  
2157 N N   . TRP A 253 ? 0.1555 0.1228 0.1797 -0.0202 0.0155  -0.0183 253 TRP A N   
2158 C CA  . TRP A 253 ? 0.1369 0.1100 0.1581 -0.0214 0.0140  -0.0177 253 TRP A CA  
2159 C C   . TRP A 253 ? 0.1114 0.0896 0.1339 -0.0185 0.0141  -0.0150 253 TRP A C   
2160 O O   . TRP A 253 ? 0.1422 0.1208 0.1665 -0.0164 0.0142  -0.0117 253 TRP A O   
2161 C CB  . TRP A 253 ? 0.1249 0.0975 0.1445 -0.0238 0.0123  -0.0166 253 TRP A CB  
2162 C CG  . TRP A 253 ? 0.1309 0.1080 0.1483 -0.0244 0.0109  -0.0158 253 TRP A CG  
2163 C CD1 . TRP A 253 ? 0.1149 0.0949 0.1324 -0.0232 0.0098  -0.0136 253 TRP A CD1 
2164 C CD2 . TRP A 253 ? 0.1306 0.1102 0.1462 -0.0260 0.0105  -0.0175 253 TRP A CD2 
2165 N NE1 . TRP A 253 ? 0.1483 0.1312 0.1643 -0.0243 0.0084  -0.0148 253 TRP A NE1 
2166 C CE2 . TRP A 253 ? 0.1303 0.1126 0.1456 -0.0263 0.0090  -0.0165 253 TRP A CE2 
2167 C CE3 . TRP A 253 ? 0.1989 0.1790 0.2131 -0.0271 0.0114  -0.0194 253 TRP A CE3 
2168 C CZ2 . TRP A 253 ? 0.1481 0.1322 0.1631 -0.0281 0.0085  -0.0172 253 TRP A CZ2 
2169 C CZ3 . TRP A 253 ? 0.1333 0.1164 0.1467 -0.0286 0.0112  -0.0191 253 TRP A CZ3 
2170 C CH2 . TRP A 253 ? 0.1287 0.1131 0.1431 -0.0294 0.0098  -0.0179 253 TRP A CH2 
2171 N N   . PRO A 254 ? 0.1334 0.1167 0.1557 -0.0180 0.0141  -0.0160 254 PRO A N   
2172 C CA  . PRO A 254 ? 0.1478 0.1377 0.1718 -0.0155 0.0135  -0.0142 254 PRO A CA  
2173 C C   . PRO A 254 ? 0.1092 0.1018 0.1319 -0.0168 0.0112  -0.0137 254 PRO A C   
2174 O O   . PRO A 254 ? 0.1428 0.1345 0.1639 -0.0201 0.0100  -0.0153 254 PRO A O   
2175 C CB  . PRO A 254 ? 0.1445 0.1395 0.1695 -0.0158 0.0140  -0.0160 254 PRO A CB  
2176 C CG  . PRO A 254 ? 0.1750 0.1671 0.1976 -0.0192 0.0143  -0.0181 254 PRO A CG  
2177 C CD  . PRO A 254 ? 0.1420 0.1266 0.1628 -0.0197 0.0146  -0.0187 254 PRO A CD  
2178 N N   . PRO A 255 ? 0.0969 0.0931 0.1202 -0.0138 0.0106  -0.0113 255 PRO A N   
2179 C CA  . PRO A 255 ? 0.1104 0.1096 0.1321 -0.0143 0.0083  -0.0116 255 PRO A CA  
2180 C C   . PRO A 255 ? 0.1143 0.1172 0.1364 -0.0168 0.0064  -0.0150 255 PRO A C   
2181 O O   . PRO A 255 ? 0.1186 0.1266 0.1432 -0.0164 0.0064  -0.0161 255 PRO A O   
2182 C CB  . PRO A 255 ? 0.1343 0.1396 0.1565 -0.0095 0.0083  -0.0086 255 PRO A CB  
2183 C CG  . PRO A 255 ? 0.1804 0.1813 0.2047 -0.0073 0.0112  -0.0051 255 PRO A CG  
2184 C CD  . PRO A 255 ? 0.1332 0.1303 0.1586 -0.0094 0.0123  -0.0078 255 PRO A CD  
2185 N N   . GLU A 256 ? 0.1245 0.1247 0.1449 -0.0194 0.0050  -0.0165 256 GLU A N   
2186 C CA  . GLU A 256 ? 0.1109 0.1125 0.1327 -0.0223 0.0033  -0.0195 256 GLU A CA  
2187 C C   . GLU A 256 ? 0.1138 0.1144 0.1377 -0.0251 0.0048  -0.0197 256 GLU A C   
2188 O O   . GLU A 256 ? 0.1317 0.1356 0.1591 -0.0272 0.0041  -0.0214 256 GLU A O   
2189 C CB  . GLU A 256 ? 0.1386 0.1481 0.1628 -0.0207 0.0010  -0.0218 256 GLU A CB  
2190 C CG  . GLU A 256 ? 0.1574 0.1709 0.1791 -0.0165 -0.0004 -0.0214 256 GLU A CG  
2191 C CD  . GLU A 256 ? 0.1792 0.1884 0.1979 -0.0171 -0.0014 -0.0221 256 GLU A CD  
2192 O OE1 . GLU A 256 ? 0.1834 0.1875 0.2027 -0.0207 -0.0020 -0.0240 256 GLU A OE1 
2193 O OE2 . GLU A 256 ? 0.1932 0.2047 0.2092 -0.0136 -0.0015 -0.0202 256 GLU A OE2 
2194 N N   . ALA A 257 ? 0.1063 0.1031 0.1286 -0.0250 0.0070  -0.0183 257 ALA A N   
2195 C CA  . ALA A 257 ? 0.1749 0.1721 0.1982 -0.0265 0.0089  -0.0184 257 ALA A CA  
2196 C C   . ALA A 257 ? 0.1333 0.1374 0.1605 -0.0252 0.0093  -0.0187 257 ALA A C   
2197 O O   . ALA A 257 ? 0.1802 0.1871 0.2094 -0.0266 0.0107  -0.0187 257 ALA A O   
2198 C CB  . ALA A 257 ? 0.1302 0.1259 0.1537 -0.0301 0.0088  -0.0185 257 ALA A CB  
2199 N N   . SER A 258 ? 0.1109 0.1192 0.1393 -0.0221 0.0084  -0.0186 258 SER A N   
2200 C CA  . SER A 258 ? 0.1177 0.1347 0.1503 -0.0210 0.0080  -0.0192 258 SER A CA  
2201 C C   . SER A 258 ? 0.1290 0.1477 0.1624 -0.0183 0.0106  -0.0180 258 SER A C   
2202 O O   . SER A 258 ? 0.1510 0.1664 0.1827 -0.0148 0.0120  -0.0166 258 SER A O   
2203 C CB  . SER A 258 ? 0.1414 0.1642 0.1746 -0.0179 0.0057  -0.0195 258 SER A CB  
2204 O OG  . SER A 258 ? 0.1658 0.1985 0.2037 -0.0176 0.0047  -0.0209 258 SER A OG  
2205 N N   . VAL A 259 ? 0.1267 0.1508 0.1636 -0.0198 0.0116  -0.0184 259 VAL A N   
2206 C CA  . VAL A 259 ? 0.0941 0.1214 0.1319 -0.0166 0.0142  -0.0176 259 VAL A CA  
2207 C C   . VAL A 259 ? 0.1420 0.1808 0.1857 -0.0167 0.0137  -0.0177 259 VAL A C   
2208 O O   . VAL A 259 ? 0.1400 0.1833 0.1875 -0.0202 0.0115  -0.0189 259 VAL A O   
2209 C CB  . VAL A 259 ? 0.1100 0.1329 0.1453 -0.0177 0.0167  -0.0178 259 VAL A CB  
2210 C CG1 . VAL A 259 ? 0.1341 0.1467 0.1642 -0.0179 0.0168  -0.0184 259 VAL A CG1 
2211 C CG2 . VAL A 259 ? 0.1465 0.1729 0.1841 -0.0221 0.0169  -0.0175 259 VAL A CG2 
2212 N N   . SER A 260 ? 0.1118 0.1554 0.1568 -0.0125 0.0158  -0.0168 260 SER A N   
2213 C CA  . SER A 260 ? 0.1203 0.1761 0.1710 -0.0116 0.0161  -0.0164 260 SER A CA  
2214 C C   . SER A 260 ? 0.1087 0.1647 0.1582 -0.0068 0.0196  -0.0154 260 SER A C   
2215 O O   . SER A 260 ? 0.1521 0.1986 0.1970 -0.0042 0.0211  -0.0156 260 SER A O   
2216 C CB  . SER A 260 ? 0.1385 0.2028 0.1922 -0.0091 0.0135  -0.0166 260 SER A CB  
2217 O OG  . SER A 260 ? 0.1219 0.1834 0.1723 -0.0028 0.0145  -0.0147 260 SER A OG  
2218 N N   . ASN A 261 ? 0.0982 0.1653 0.1525 -0.0055 0.0209  -0.0147 261 ASN A N   
2219 C CA  . ASN A 261 ? 0.1303 0.1983 0.1834 0.0000  0.0244  -0.0142 261 ASN A CA  
2220 C C   . ASN A 261 ? 0.1370 0.2006 0.1881 0.0064  0.0248  -0.0133 261 ASN A C   
2221 O O   . ASN A 261 ? 0.1496 0.2048 0.1973 0.0101  0.0271  -0.0139 261 ASN A O   
2222 C CB  . ASN A 261 ? 0.1086 0.1912 0.1679 0.0009  0.0256  -0.0131 261 ASN A CB  
2223 C CG  . ASN A 261 ? 0.1324 0.2191 0.1944 -0.0049 0.0264  -0.0127 261 ASN A CG  
2224 O OD1 . ASN A 261 ? 0.1487 0.2270 0.2064 -0.0075 0.0273  -0.0131 261 ASN A OD1 
2225 N ND2 . ASN A 261 ? 0.1905 0.2909 0.2605 -0.0069 0.0262  -0.0114 261 ASN A ND2 
2226 N N   . GLU A 262 ? 0.1035 0.1726 0.1569 0.0078  0.0224  -0.0120 262 GLU A N   
2227 C CA  . GLU A 262 ? 0.1086 0.1747 0.1607 0.0144  0.0232  -0.0097 262 GLU A CA  
2228 C C   . GLU A 262 ? 0.1477 0.1987 0.1951 0.0136  0.0233  -0.0097 262 GLU A C   
2229 O O   . GLU A 262 ? 0.1468 0.1899 0.1931 0.0182  0.0256  -0.0084 262 GLU A O   
2230 C CB  . GLU A 262 ? 0.1049 0.1828 0.1602 0.0164  0.0204  -0.0081 262 GLU A CB  
2231 C CG  . GLU A 262 ? 0.1358 0.2300 0.1968 0.0184  0.0206  -0.0078 262 GLU A CG  
2232 C CD  . GLU A 262 ? 0.3130 0.4210 0.3772 0.0214  0.0177  -0.0067 262 GLU A CD  
2233 O OE1 . GLU A 262 ? 0.2965 0.4020 0.3579 0.0260  0.0174  -0.0041 262 GLU A OE1 
2234 O OE2 . GLU A 262 ? 0.3659 0.4881 0.4356 0.0193  0.0158  -0.0082 262 GLU A OE2 
2235 N N   . ALA A 263 ? 0.1159 0.1628 0.1613 0.0078  0.0209  -0.0111 263 ALA A N   
2236 C CA  . ALA A 263 ? 0.1084 0.1425 0.1499 0.0068  0.0210  -0.0109 263 ALA A CA  
2237 C C   . ALA A 263 ? 0.1302 0.1544 0.1694 0.0065  0.0234  -0.0130 263 ALA A C   
2238 O O   . ALA A 263 ? 0.1430 0.1574 0.1812 0.0085  0.0247  -0.0126 263 ALA A O   
2239 C CB  . ALA A 263 ? 0.1064 0.1390 0.1462 0.0012  0.0180  -0.0122 263 ALA A CB  
2240 N N   . LEU A 264 ? 0.1659 0.1931 0.2047 0.0039  0.0241  -0.0154 264 LEU A N   
2241 C CA  . LEU A 264 ? 0.1690 0.1888 0.2049 0.0044  0.0263  -0.0182 264 LEU A CA  
2242 C C   . LEU A 264 ? 0.1539 0.1713 0.1911 0.0110  0.0289  -0.0183 264 LEU A C   
2243 O O   . LEU A 264 ? 0.1672 0.1743 0.2027 0.0123  0.0301  -0.0207 264 LEU A O   
2244 C CB  . LEU A 264 ? 0.1508 0.1770 0.1861 0.0014  0.0269  -0.0196 264 LEU A CB  
2245 C CG  . LEU A 264 ? 0.1589 0.1845 0.1928 -0.0050 0.0248  -0.0195 264 LEU A CG  
2246 C CD1 . LEU A 264 ? 0.1891 0.2227 0.2241 -0.0073 0.0260  -0.0192 264 LEU A CD1 
2247 C CD2 . LEU A 264 ? 0.1725 0.1871 0.2018 -0.0069 0.0242  -0.0214 264 LEU A CD2 
2248 N N   . GLU A 265 ? 0.1441 0.1709 0.1847 0.0153  0.0298  -0.0161 265 GLU A N   
2249 C CA  . GLU A 265 ? 0.1889 0.2129 0.2311 0.0224  0.0326  -0.0156 265 GLU A CA  
2250 C C   . GLU A 265 ? 0.1956 0.2087 0.2385 0.0245  0.0327  -0.0133 265 GLU A C   
2251 O O   . GLU A 265 ? 0.1615 0.1641 0.2047 0.0276  0.0348  -0.0149 265 GLU A O   
2252 C CB  . GLU A 265 ? 0.2127 0.2505 0.2589 0.0269  0.0333  -0.0128 265 GLU A CB  
2253 C CG  . GLU A 265 ? 0.2788 0.3272 0.3256 0.0256  0.0341  -0.0146 265 GLU A CG  
2254 C CD  . GLU A 265 ? 0.4470 0.4932 0.4926 0.0308  0.0376  -0.0172 265 GLU A CD  
2255 O OE1 . GLU A 265 ? 0.3196 0.3552 0.3646 0.0357  0.0392  -0.0181 265 GLU A OE1 
2256 O OE2 . GLU A 265 ? 0.4031 0.4585 0.4487 0.0303  0.0388  -0.0184 265 GLU A OE2 
2257 N N   . LEU A 266 ? 0.1456 0.1609 0.1890 0.0228  0.0306  -0.0098 266 LEU A N   
2258 C CA  . LEU A 266 ? 0.1447 0.1513 0.1894 0.0251  0.0312  -0.0063 266 LEU A CA  
2259 C C   . LEU A 266 ? 0.1682 0.1606 0.2114 0.0213  0.0313  -0.0092 266 LEU A C   
2260 O O   . LEU A 266 ? 0.1637 0.1457 0.2094 0.0240  0.0334  -0.0084 266 LEU A O   
2261 C CB  . LEU A 266 ? 0.1399 0.1537 0.1846 0.0243  0.0288  -0.0022 266 LEU A CB  
2262 C CG  . LEU A 266 ? 0.1880 0.1941 0.2338 0.0260  0.0295  0.0024  266 LEU A CG  
2263 C CD1 . LEU A 266 ? 0.2048 0.2080 0.2545 0.0336  0.0329  0.0069  266 LEU A CD1 
2264 C CD2 . LEU A 266 ? 0.1786 0.1933 0.2230 0.0250  0.0268  0.0054  266 LEU A CD2 
2265 N N   . TYR A 267 ? 0.1666 0.1586 0.2064 0.0150  0.0292  -0.0126 267 TYR A N   
2266 C CA  . TYR A 267 ? 0.1514 0.1318 0.1897 0.0114  0.0291  -0.0159 267 TYR A CA  
2267 C C   . TYR A 267 ? 0.1694 0.1431 0.2081 0.0140  0.0312  -0.0207 267 TYR A C   
2268 O O   . TYR A 267 ? 0.1785 0.1409 0.2192 0.0138  0.0320  -0.0225 267 TYR A O   
2269 C CB  . TYR A 267 ? 0.1648 0.1477 0.1991 0.0051  0.0266  -0.0186 267 TYR A CB  
2270 C CG  . TYR A 267 ? 0.1406 0.1265 0.1744 0.0020  0.0243  -0.0153 267 TYR A CG  
2271 C CD1 . TYR A 267 ? 0.1620 0.1412 0.1968 0.0012  0.0239  -0.0129 267 TYR A CD1 
2272 C CD2 . TYR A 267 ? 0.1548 0.1501 0.1874 -0.0002 0.0224  -0.0149 267 TYR A CD2 
2273 C CE1 . TYR A 267 ? 0.1534 0.1362 0.1871 -0.0009 0.0219  -0.0102 267 TYR A CE1 
2274 C CE2 . TYR A 267 ? 0.1457 0.1435 0.1776 -0.0025 0.0201  -0.0130 267 TYR A CE2 
2275 C CZ  . TYR A 267 ? 0.1624 0.1541 0.1943 -0.0025 0.0199  -0.0108 267 TYR A CZ  
2276 O OH  . TYR A 267 ? 0.1488 0.1437 0.1795 -0.0040 0.0177  -0.0091 267 TYR A OH  
2277 N N   . TYR A 268 ? 0.1550 0.1360 0.1924 0.0163  0.0323  -0.0230 268 TYR A N   
2278 C CA  . TYR A 268 ? 0.1775 0.1535 0.2149 0.0201  0.0345  -0.0280 268 TYR A CA  
2279 C C   . TYR A 268 ? 0.1931 0.1610 0.2355 0.0260  0.0369  -0.0260 268 TYR A C   
2280 O O   . TYR A 268 ? 0.1764 0.1326 0.2206 0.0269  0.0379  -0.0301 268 TYR A O   
2281 C CB  . TYR A 268 ? 0.1793 0.1671 0.2148 0.0226  0.0356  -0.0295 268 TYR A CB  
2282 C CG  . TYR A 268 ? 0.2145 0.1992 0.2508 0.0290  0.0384  -0.0334 268 TYR A CG  
2283 C CD1 . TYR A 268 ? 0.2554 0.2319 0.2893 0.0289  0.0387  -0.0405 268 TYR A CD1 
2284 C CD2 . TYR A 268 ? 0.2235 0.2139 0.2629 0.0356  0.0407  -0.0304 268 TYR A CD2 
2285 C CE1 . TYR A 268 ? 0.2935 0.2667 0.3280 0.0353  0.0412  -0.0452 268 TYR A CE1 
2286 C CE2 . TYR A 268 ? 0.2978 0.2849 0.3380 0.0423  0.0435  -0.0342 268 TYR A CE2 
2287 C CZ  . TYR A 268 ? 0.3523 0.3303 0.3900 0.0421  0.0437  -0.0419 268 TYR A CZ  
2288 O OH  . TYR A 268 ? 0.4457 0.4200 0.4839 0.0490  0.0463  -0.0468 268 TYR A OH  
2289 N N   . GLU A 269 ? 0.2029 0.1771 0.2482 0.0301  0.0377  -0.0197 269 GLU A N   
2290 C CA  . GLU A 269 ? 0.2118 0.1791 0.2622 0.0365  0.0404  -0.0162 269 GLU A CA  
2291 C C   . GLU A 269 ? 0.1699 0.1236 0.2238 0.0344  0.0406  -0.0143 269 GLU A C   
2292 O O   . GLU A 269 ? 0.2594 0.2021 0.3183 0.0384  0.0431  -0.0140 269 GLU A O   
2293 C CB  . GLU A 269 ? 0.2203 0.1995 0.2726 0.0414  0.0410  -0.0092 269 GLU A CB  
2294 C CG  . GLU A 269 ? 0.2811 0.2727 0.3325 0.0452  0.0418  -0.0108 269 GLU A CG  
2295 C CD  . GLU A 269 ? 0.4708 0.4783 0.5233 0.0470  0.0407  -0.0054 269 GLU A CD  
2296 O OE1 . GLU A 269 ? 0.4622 0.4711 0.5156 0.0465  0.0394  -0.0003 269 GLU A OE1 
2297 O OE2 . GLU A 269 ? 0.4960 0.5157 0.5485 0.0490  0.0410  -0.0063 269 GLU A OE2 
2298 N N   . LYS A 270 ? 0.1726 0.1267 0.2248 0.0282  0.0381  -0.0129 270 LYS A N   
2299 C CA  . LYS A 270 ? 0.1999 0.1427 0.2562 0.0257  0.0383  -0.0106 270 LYS A CA  
2300 C C   . LYS A 270 ? 0.2257 0.1582 0.2816 0.0204  0.0372  -0.0182 270 LYS A C   
2301 O O   . LYS A 270 ? 0.2406 0.1651 0.3001 0.0166  0.0368  -0.0171 270 LYS A O   
2302 C CB  . LYS A 270 ? 0.2053 0.1546 0.2603 0.0226  0.0364  -0.0046 270 LYS A CB  
2303 C CG  . LYS A 270 ? 0.2545 0.2141 0.3104 0.0284  0.0373  0.0030  270 LYS A CG  
2304 C CD  . LYS A 270 ? 0.3404 0.2933 0.4027 0.0351  0.0410  0.0087  270 LYS A CD  
2305 C CE  . LYS A 270 ? 0.4712 0.4366 0.5338 0.0414  0.0417  0.0167  270 LYS A CE  
2306 N NZ  . LYS A 270 ? 0.5965 0.5626 0.6623 0.0496  0.0448  0.0188  270 LYS A NZ  
2307 N N   . GLY A 271 ? 0.2070 0.1406 0.2593 0.0205  0.0369  -0.0259 271 GLY A N   
2308 C CA  . GLY A 271 ? 0.2908 0.2155 0.3431 0.0170  0.0359  -0.0341 271 GLY A CA  
2309 C C   . GLY A 271 ? 0.2737 0.2024 0.3211 0.0100  0.0326  -0.0369 271 GLY A C   
2310 O O   . GLY A 271 ? 0.2408 0.1624 0.2890 0.0063  0.0313  -0.0428 271 GLY A O   
2311 N N   . ILE A 272 ? 0.1923 0.1320 0.2351 0.0081  0.0312  -0.0332 272 ILE A N   
2312 C CA  . ILE A 272 ? 0.2045 0.1482 0.2427 0.0021  0.0284  -0.0351 272 ILE A CA  
2313 C C   . ILE A 272 ? 0.1900 0.1393 0.2227 0.0022  0.0280  -0.0415 272 ILE A C   
2314 O O   . ILE A 272 ? 0.2477 0.2046 0.2786 0.0058  0.0294  -0.0410 272 ILE A O   
2315 C CB  . ILE A 272 ? 0.1942 0.1465 0.2306 0.0003  0.0271  -0.0288 272 ILE A CB  
2316 C CG1 . ILE A 272 ? 0.2003 0.1494 0.2414 0.0015  0.0278  -0.0219 272 ILE A CG1 
2317 C CG2 . ILE A 272 ? 0.1674 0.1228 0.1993 -0.0053 0.0245  -0.0306 272 ILE A CG2 
2318 C CD1 . ILE A 272 ? 0.2708 0.2092 0.3165 -0.0011 0.0279  -0.0220 272 ILE A CD1 
2319 N N   . ASN A 273 ? 0.1593 0.1061 0.1897 -0.0013 0.0263  -0.0472 273 ASN A N   
2320 C CA  . ASN A 273 ? 0.2077 0.1602 0.2325 -0.0005 0.0261  -0.0535 273 ASN A CA  
2321 C C   . ASN A 273 ? 0.2202 0.1832 0.2394 -0.0036 0.0248  -0.0512 273 ASN A C   
2322 O O   . ASN A 273 ? 0.1974 0.1686 0.2123 -0.0017 0.0256  -0.0531 273 ASN A O   
2323 C CB  . ASN A 273 ? 0.2460 0.1915 0.2712 -0.0020 0.0247  -0.0618 273 ASN A CB  
2324 C CG  . ASN A 273 ? 0.4142 0.3498 0.4444 0.0021  0.0264  -0.0666 273 ASN A CG  
2325 O OD1 . ASN A 273 ? 0.5203 0.4557 0.5525 0.0072  0.0290  -0.0638 273 ASN A OD1 
2326 N ND2 . ASN A 273 ? 0.5020 0.4296 0.5349 0.0001  0.0249  -0.0740 273 ASN A ND2 
2327 N N   A MET A 274 ? 0.2247 0.1877 0.2443 -0.0079 0.0230  -0.0468 274 MET A N   
2328 N N   B MET A 274 ? 0.2196 0.1825 0.2391 -0.0079 0.0230  -0.0469 274 MET A N   
2329 C CA  A MET A 274 ? 0.1903 0.1614 0.2054 -0.0108 0.0218  -0.0445 274 MET A CA  
2330 C CA  B MET A 274 ? 0.1918 0.1629 0.2068 -0.0109 0.0218  -0.0445 274 MET A CA  
2331 C C   A MET A 274 ? 0.2080 0.1790 0.2248 -0.0137 0.0207  -0.0384 274 MET A C   
2332 C C   B MET A 274 ? 0.2078 0.1789 0.2248 -0.0136 0.0207  -0.0383 274 MET A C   
2333 O O   A MET A 274 ? 0.1840 0.1487 0.2041 -0.0149 0.0199  -0.0370 274 MET A O   
2334 O O   B MET A 274 ? 0.1817 0.1464 0.2021 -0.0146 0.0201  -0.0368 274 MET A O   
2335 C CB  A MET A 274 ? 0.2079 0.1796 0.2190 -0.0134 0.0201  -0.0493 274 MET A CB  
2336 C CB  B MET A 274 ? 0.2037 0.1756 0.2148 -0.0135 0.0200  -0.0491 274 MET A CB  
2337 C CG  A MET A 274 ? 0.1981 0.1784 0.2045 -0.0154 0.0195  -0.0464 274 MET A CG  
2338 C CG  B MET A 274 ? 0.1983 0.1788 0.2048 -0.0156 0.0194  -0.0460 274 MET A CG  
2339 S SD  A MET A 274 ? 0.2502 0.2332 0.2517 -0.0173 0.0174  -0.0515 274 MET A SD  
2340 S SD  B MET A 274 ? 0.1927 0.1713 0.2002 -0.0203 0.0172  -0.0408 274 MET A SD  
2341 C CE  A MET A 274 ? 0.1685 0.1436 0.1737 -0.0217 0.0148  -0.0507 274 MET A CE  
2342 C CE  B MET A 274 ? 0.2599 0.2344 0.2667 -0.0227 0.0149  -0.0461 274 MET A CE  
2343 N N   . LEU A 275 ? 0.1516 0.1301 0.1668 -0.0146 0.0206  -0.0348 275 LEU A N   
2344 C CA  . LEU A 275 ? 0.1206 0.0997 0.1365 -0.0174 0.0190  -0.0304 275 LEU A CA  
2345 C C   . LEU A 275 ? 0.1765 0.1615 0.1893 -0.0199 0.0185  -0.0294 275 LEU A C   
2346 O O   . LEU A 275 ? 0.1657 0.1551 0.1758 -0.0192 0.0195  -0.0312 275 LEU A O   
2347 C CB  . LEU A 275 ? 0.1977 0.1790 0.2172 -0.0154 0.0195  -0.0267 275 LEU A CB  
2348 C CG  . LEU A 275 ? 0.2965 0.2852 0.3173 -0.0129 0.0210  -0.0260 275 LEU A CG  
2349 C CD1 . LEU A 275 ? 0.3543 0.3501 0.3745 -0.0157 0.0203  -0.0241 275 LEU A CD1 
2350 C CD2 . LEU A 275 ? 0.2705 0.2601 0.2951 -0.0095 0.0216  -0.0233 275 LEU A CD2 
2351 N N   . ALA A 276 ? 0.1998 0.1851 0.2129 -0.0224 0.0169  -0.0263 276 ALA A N   
2352 C CA  . ALA A 276 ? 0.1305 0.1202 0.1420 -0.0247 0.0167  -0.0244 276 ALA A CA  
2353 C C   . ALA A 276 ? 0.1432 0.1353 0.1582 -0.0255 0.0160  -0.0215 276 ALA A C   
2354 O O   . ALA A 276 ? 0.1567 0.1470 0.1737 -0.0245 0.0151  -0.0209 276 ALA A O   
2355 C CB  . ALA A 276 ? 0.1437 0.1312 0.1522 -0.0270 0.0152  -0.0243 276 ALA A CB  
2356 N N   . THR A 277 ? 0.1394 0.1358 0.1552 -0.0273 0.0164  -0.0196 277 THR A N   
2357 C CA  . THR A 277 ? 0.1212 0.1198 0.1411 -0.0289 0.0152  -0.0180 277 THR A CA  
2358 C C   . THR A 277 ? 0.1438 0.1426 0.1639 -0.0319 0.0152  -0.0159 277 THR A C   
2359 O O   . THR A 277 ? 0.1905 0.1875 0.2068 -0.0323 0.0156  -0.0154 277 THR A O   
2360 C CB  . THR A 277 ? 0.1223 0.1271 0.1463 -0.0274 0.0162  -0.0179 277 THR A CB  
2361 O OG1 . THR A 277 ? 0.1580 0.1658 0.1865 -0.0292 0.0146  -0.0173 277 THR A OG1 
2362 C CG2 . THR A 277 ? 0.1731 0.1833 0.1974 -0.0273 0.0188  -0.0170 277 THR A CG2 
2363 N N   . ASP A 278 ? 0.1576 0.1590 0.1827 -0.0340 0.0146  -0.0148 278 ASP A N   
2364 C CA  . ASP A 278 ? 0.1418 0.1413 0.1685 -0.0369 0.0144  -0.0127 278 ASP A CA  
2365 C C   . ASP A 278 ? 0.1789 0.1833 0.2092 -0.0386 0.0170  -0.0096 278 ASP A C   
2366 O O   . ASP A 278 ? 0.1701 0.1808 0.2038 -0.0383 0.0183  -0.0094 278 ASP A O   
2367 C CB  . ASP A 278 ? 0.1392 0.1369 0.1700 -0.0385 0.0118  -0.0142 278 ASP A CB  
2368 C CG  . ASP A 278 ? 0.1957 0.1894 0.2287 -0.0412 0.0115  -0.0125 278 ASP A CG  
2369 O OD1 . ASP A 278 ? 0.1958 0.1854 0.2242 -0.0406 0.0118  -0.0110 278 ASP A OD1 
2370 O OD2 . ASP A 278 ? 0.2589 0.2536 0.2986 -0.0439 0.0109  -0.0128 278 ASP A OD2 
2371 N N   . GLU A 279 ? 0.1836 0.1859 0.2135 -0.0402 0.0179  -0.0063 279 GLU A N   
2372 C CA  . GLU A 279 ? 0.1876 0.1946 0.2215 -0.0418 0.0209  -0.0017 279 GLU A CA  
2373 C C   . GLU A 279 ? 0.1846 0.1947 0.2283 -0.0451 0.0209  -0.0012 279 GLU A C   
2374 O O   . GLU A 279 ? 0.1811 0.1981 0.2294 -0.0460 0.0236  0.0021  279 GLU A O   
2375 C CB  . GLU A 279 ? 0.1564 0.1597 0.1886 -0.0424 0.0218  0.0023  279 GLU A CB  
2376 C CG  . GLU A 279 ? 0.2220 0.2313 0.2558 -0.0426 0.0257  0.0083  279 GLU A CG  
2377 C CD  . GLU A 279 ? 0.3068 0.3134 0.3384 -0.0422 0.0269  0.0133  279 GLU A CD  
2378 O OE1 . GLU A 279 ? 0.2317 0.2319 0.2593 -0.0415 0.0247  0.0115  279 GLU A OE1 
2379 O OE2 . GLU A 279 ? 0.3184 0.3300 0.3526 -0.0424 0.0304  0.0196  279 GLU A OE2 
2380 N N   . VAL A 280 ? 0.1603 0.1662 0.2076 -0.0468 0.0177  -0.0045 280 VAL A N   
2381 C CA  . VAL A 280 ? 0.1837 0.1932 0.2411 -0.0504 0.0171  -0.0051 280 VAL A CA  
2382 C C   . VAL A 280 ? 0.1488 0.1675 0.2083 -0.0491 0.0176  -0.0064 280 VAL A C   
2383 O O   . VAL A 280 ? 0.1643 0.1898 0.2322 -0.0517 0.0188  -0.0047 280 VAL A O   
2384 C CB  . VAL A 280 ? 0.2208 0.2249 0.2809 -0.0518 0.0131  -0.0097 280 VAL A CB  
2385 C CG1 . VAL A 280 ? 0.1883 0.1978 0.2589 -0.0553 0.0116  -0.0121 280 VAL A CG1 
2386 C CG2 . VAL A 280 ? 0.2464 0.2415 0.3062 -0.0532 0.0130  -0.0080 280 VAL A CG2 
2387 N N   . ILE A 281 ? 0.1846 0.2039 0.2372 -0.0449 0.0169  -0.0090 281 ILE A N   
2388 C CA  . ILE A 281 ? 0.1639 0.1914 0.2179 -0.0426 0.0176  -0.0100 281 ILE A CA  
2389 C C   . ILE A 281 ? 0.1498 0.1836 0.2041 -0.0419 0.0217  -0.0061 281 ILE A C   
2390 O O   . ILE A 281 ? 0.1712 0.2139 0.2314 -0.0422 0.0231  -0.0050 281 ILE A O   
2391 C CB  . ILE A 281 ? 0.1482 0.1732 0.1955 -0.0381 0.0163  -0.0131 281 ILE A CB  
2392 C CG1 . ILE A 281 ? 0.1982 0.2210 0.2468 -0.0385 0.0125  -0.0163 281 ILE A CG1 
2393 C CG2 . ILE A 281 ? 0.2039 0.2365 0.2518 -0.0346 0.0179  -0.0133 281 ILE A CG2 
2394 C CD1 . ILE A 281 ? 0.2679 0.2875 0.3104 -0.0343 0.0113  -0.0180 281 ILE A CD1 
2395 N N   . LEU A 282 ? 0.1211 0.1516 0.1690 -0.0406 0.0236  -0.0040 282 LEU A N   
2396 C CA  . LEU A 282 ? 0.1465 0.1840 0.1940 -0.0394 0.0276  0.0000  282 LEU A CA  
2397 C C   . LEU A 282 ? 0.1513 0.1944 0.2088 -0.0438 0.0295  0.0048  282 LEU A C   
2398 O O   . LEU A 282 ? 0.1475 0.2005 0.2097 -0.0434 0.0320  0.0071  282 LEU A O   
2399 C CB  . LEU A 282 ? 0.1706 0.2045 0.2100 -0.0376 0.0288  0.0015  282 LEU A CB  
2400 C CG  . LEU A 282 ? 0.1523 0.1949 0.1894 -0.0353 0.0329  0.0053  282 LEU A CG  
2401 C CD1 . LEU A 282 ? 0.1843 0.2334 0.2191 -0.0310 0.0341  0.0022  282 LEU A CD1 
2402 C CD2 . LEU A 282 ? 0.1931 0.2329 0.2219 -0.0333 0.0333  0.0062  282 LEU A CD2 
2403 N N   . LYS A 283 ? 0.1334 0.1701 0.1950 -0.0478 0.0284  0.0066  283 LYS A N   
2404 C CA  . LYS A 283 ? 0.1479 0.1886 0.2206 -0.0525 0.0304  0.0117  283 LYS A CA  
2405 C C   . LYS A 283 ? 0.1611 0.2089 0.2438 -0.0551 0.0292  0.0094  283 LYS A C   
2406 O O   . LYS A 283 ? 0.1800 0.2359 0.2720 -0.0580 0.0319  0.0138  283 LYS A O   
2407 C CB  . LYS A 283 ? 0.2524 0.2829 0.3282 -0.0560 0.0292  0.0130  283 LYS A CB  
2408 C CG  . LYS A 283 ? 0.4454 0.4720 0.5135 -0.0536 0.0314  0.0175  283 LYS A CG  
2409 C CD  . LYS A 283 ? 0.5734 0.5907 0.6457 -0.0566 0.0311  0.0204  283 LYS A CD  
2410 C CE  . LYS A 283 ? 0.6753 0.6853 0.7370 -0.0532 0.0297  0.0192  283 LYS A CE  
2411 N NZ  . LYS A 283 ? 0.7133 0.7130 0.7762 -0.0547 0.0258  0.0146  283 LYS A NZ  
2412 N N   . ASN A 284 ? 0.1601 0.2062 0.2415 -0.0542 0.0252  0.0029  284 ASN A N   
2413 C CA  . ASN A 284 ? 0.1702 0.2245 0.2602 -0.0559 0.0234  0.0001  284 ASN A CA  
2414 C C   . ASN A 284 ? 0.1520 0.2178 0.2412 -0.0521 0.0258  0.0012  284 ASN A C   
2415 O O   . ASN A 284 ? 0.1534 0.2293 0.2517 -0.0539 0.0255  0.0009  284 ASN A O   
2416 C CB  . ASN A 284 ? 0.1181 0.1685 0.2058 -0.0549 0.0185  -0.0067 284 ASN A CB  
2417 C CG  . ASN A 284 ? 0.2454 0.2874 0.3373 -0.0591 0.0154  -0.0091 284 ASN A CG  
2418 O OD1 . ASN A 284 ? 0.2494 0.2885 0.3485 -0.0637 0.0168  -0.0059 284 ASN A OD1 
2419 N ND2 . ASN A 284 ? 0.1752 0.2136 0.2632 -0.0573 0.0114  -0.0148 284 ASN A ND2 
2420 N N   . SER A 285 ? 0.1495 0.2145 0.2285 -0.0468 0.0280  0.0019  285 SER A N   
2421 C CA  . SER A 285 ? 0.1483 0.2223 0.2250 -0.0419 0.0300  0.0016  285 SER A CA  
2422 C C   . SER A 285 ? 0.1901 0.2728 0.2675 -0.0406 0.0350  0.0069  285 SER A C   
2423 O O   . SER A 285 ? 0.2202 0.3135 0.2996 -0.0375 0.0370  0.0074  285 SER A O   
2424 C CB  . SER A 285 ? 0.1996 0.2667 0.2650 -0.0362 0.0290  -0.0023 285 SER A CB  
2425 O OG  . SER A 285 ? 0.2017 0.2619 0.2661 -0.0367 0.0249  -0.0063 285 SER A OG  
2426 N N   . VAL A 286 ? 0.1404 0.2196 0.2154 -0.0419 0.0372  0.0111  286 VAL A N   
2427 C CA  . VAL A 286 ? 0.1401 0.2282 0.2137 -0.0396 0.0421  0.0165  286 VAL A CA  
2428 C C   . VAL A 286 ? 0.1808 0.2694 0.2623 -0.0450 0.0443  0.0236  286 VAL A C   
2429 O O   . VAL A 286 ? 0.2317 0.3095 0.3125 -0.0479 0.0424  0.0238  286 VAL A O   
2430 C CB  . VAL A 286 ? 0.2191 0.3035 0.2793 -0.0339 0.0431  0.0147  286 VAL A CB  
2431 C CG1 . VAL A 286 ? 0.2848 0.3809 0.3428 -0.0302 0.0481  0.0194  286 VAL A CG1 
2432 C CG2 . VAL A 286 ? 0.2348 0.3146 0.2881 -0.0294 0.0405  0.0073  286 VAL A CG2 
2433 N N   . GLU A 287 ? 0.2383 0.3392 0.3277 -0.0461 0.0484  0.0299  287 GLU A N   
2434 C CA  . GLU A 287 ? 0.2889 0.3905 0.3879 -0.0514 0.0511  0.0379  287 GLU A CA  
2435 C C   . GLU A 287 ? 0.3108 0.4056 0.4015 -0.0496 0.0527  0.0417  287 GLU A C   
2436 O O   . GLU A 287 ? 0.3115 0.3966 0.4060 -0.0538 0.0516  0.0439  287 GLU A O   
2437 C CB  . GLU A 287 ? 0.2914 0.4093 0.3994 -0.0519 0.0561  0.0450  287 GLU A CB  
2438 C CG  . GLU A 287 ? 0.3175 0.4424 0.4382 -0.0559 0.0544  0.0427  287 GLU A CG  
2439 C CD  . GLU A 287 ? 0.3236 0.4632 0.4519 -0.0558 0.0587  0.0485  287 GLU A CD  
2440 O OE1 . GLU A 287 ? 0.3454 0.4915 0.4672 -0.0508 0.0632  0.0537  287 GLU A OE1 
2441 O OE2 . GLU A 287 ? 0.2716 0.4152 0.4109 -0.0600 0.0570  0.0467  287 GLU A OE2 
2442 N N   . ARG A 288 ? 0.2517 0.3519 0.3309 -0.0431 0.0551  0.0422  288 ARG A N   
2443 C CA  . ARG A 288 ? 0.1382 0.2351 0.2089 -0.0405 0.0566  0.0458  288 ARG A CA  
2444 C C   . ARG A 288 ? 0.2126 0.3063 0.2685 -0.0344 0.0543  0.0381  288 ARG A C   
2445 O O   . ARG A 288 ? 0.3136 0.4161 0.3641 -0.0291 0.0558  0.0356  288 ARG A O   
2446 C CB  . ARG A 288 ? 0.2162 0.3265 0.2889 -0.0385 0.0629  0.0560  288 ARG A CB  
2447 C CG  . ARG A 288 ? 0.2020 0.3104 0.2671 -0.0358 0.0646  0.0612  288 ARG A CG  
2448 C CD  . ARG A 288 ? 0.2338 0.3586 0.2960 -0.0308 0.0706  0.0692  288 ARG A CD  
2449 N NE  . ARG A 288 ? 0.2768 0.4102 0.3281 -0.0238 0.0705  0.0624  288 ARG A NE  
2450 C CZ  . ARG A 288 ? 0.3248 0.4733 0.3762 -0.0197 0.0744  0.0651  288 ARG A CZ  
2451 N NH1 . ARG A 288 ? 0.2885 0.4409 0.3488 -0.0218 0.0767  0.0726  288 ARG A NH1 
2452 N NH2 . ARG A 288 ? 0.3233 0.4785 0.3645 -0.0130 0.0742  0.0580  288 ARG A NH2 
2453 N N   . ALA A 289 ? 0.1814 0.2628 0.2317 -0.0350 0.0506  0.0342  289 ALA A N   
2454 C CA  . ALA A 289 ? 0.2191 0.2966 0.2572 -0.0302 0.0481  0.0267  289 ALA A CA  
2455 C C   . ALA A 289 ? 0.2209 0.2890 0.2533 -0.0306 0.0459  0.0264  289 ALA A C   
2456 O O   . ALA A 289 ? 0.2255 0.2845 0.2631 -0.0350 0.0440  0.0276  289 ALA A O   
2457 C CB  . ALA A 289 ? 0.2730 0.3452 0.3116 -0.0303 0.0444  0.0186  289 ALA A CB  
2458 N N   . SER A 290 ? 0.1831 0.2538 0.2049 -0.0258 0.0460  0.0240  290 SER A N   
2459 C CA  . SER A 290 ? 0.1968 0.2603 0.2126 -0.0256 0.0437  0.0231  290 SER A CA  
2460 C C   . SER A 290 ? 0.1741 0.2282 0.1852 -0.0253 0.0391  0.0139  290 SER A C   
2461 O O   . SER A 290 ? 0.1890 0.2451 0.1967 -0.0225 0.0385  0.0079  290 SER A O   
2462 C CB  . SER A 290 ? 0.2224 0.2955 0.2296 -0.0206 0.0460  0.0258  290 SER A CB  
2463 O OG  . SER A 290 ? 0.2212 0.2890 0.2214 -0.0196 0.0430  0.0226  290 SER A OG  
2464 N N   . PRO A 291 ? 0.1875 0.2315 0.1985 -0.0278 0.0360  0.0129  291 PRO A N   
2465 C CA  . PRO A 291 ? 0.1845 0.2206 0.1916 -0.0275 0.0321  0.0052  291 PRO A CA  
2466 C C   . PRO A 291 ? 0.1785 0.2167 0.1765 -0.0240 0.0310  0.0011  291 PRO A C   
2467 O O   . PRO A 291 ? 0.1841 0.2156 0.1796 -0.0242 0.0279  -0.0047 291 PRO A O   
2468 C CB  . PRO A 291 ? 0.2583 0.2849 0.2690 -0.0312 0.0298  0.0068  291 PRO A CB  
2469 C CG  . PRO A 291 ? 0.2780 0.3074 0.2898 -0.0316 0.0323  0.0145  291 PRO A CG  
2470 C CD  . PRO A 291 ? 0.2305 0.2705 0.2451 -0.0305 0.0365  0.0192  291 PRO A CD  
2471 N N   . TYR A 292 ? 0.1664 0.2143 0.1595 -0.0207 0.0334  0.0036  292 TYR A N   
2472 C CA  . TYR A 292 ? 0.1601 0.2114 0.1447 -0.0174 0.0319  -0.0011 292 TYR A CA  
2473 C C   . TYR A 292 ? 0.1978 0.2547 0.1784 -0.0135 0.0322  -0.0080 292 TYR A C   
2474 O O   . TYR A 292 ? 0.1784 0.2402 0.1519 -0.0103 0.0312  -0.0128 292 TYR A O   
2475 C CB  . TYR A 292 ? 0.1929 0.2525 0.1737 -0.0153 0.0338  0.0055  292 TYR A CB  
2476 C CG  . TYR A 292 ? 0.2244 0.2771 0.2099 -0.0187 0.0337  0.0122  292 TYR A CG  
2477 C CD1 . TYR A 292 ? 0.1902 0.2317 0.1774 -0.0217 0.0301  0.0088  292 TYR A CD1 
2478 C CD2 . TYR A 292 ? 0.2838 0.3410 0.2726 -0.0187 0.0373  0.0220  292 TYR A CD2 
2479 C CE1 . TYR A 292 ? 0.2595 0.2945 0.2509 -0.0242 0.0299  0.0140  292 TYR A CE1 
2480 C CE2 . TYR A 292 ? 0.2836 0.3330 0.2774 -0.0216 0.0371  0.0276  292 TYR A CE2 
2481 C CZ  . TYR A 292 ? 0.2916 0.3297 0.2863 -0.0242 0.0333  0.0230  292 TYR A CZ  
2482 O OH  . TYR A 292 ? 0.3317 0.3619 0.3312 -0.0265 0.0330  0.0275  292 TYR A OH  
2483 N N   . LEU A 293 ? 0.1757 0.2321 0.1605 -0.0135 0.0336  -0.0090 293 LEU A N   
2484 C CA  . LEU A 293 ? 0.1722 0.2326 0.1542 -0.0095 0.0341  -0.0156 293 LEU A CA  
2485 C C   . LEU A 293 ? 0.1822 0.2312 0.1665 -0.0107 0.0313  -0.0225 293 LEU A C   
2486 O O   . LEU A 293 ? 0.1549 0.1953 0.1442 -0.0145 0.0296  -0.0208 293 LEU A O   
2487 C CB  . LEU A 293 ? 0.1623 0.2315 0.1481 -0.0078 0.0382  -0.0112 293 LEU A CB  
2488 C CG  . LEU A 293 ? 0.2312 0.3150 0.2142 -0.0045 0.0422  -0.0050 293 LEU A CG  
2489 C CD1 . LEU A 293 ? 0.2754 0.3599 0.2604 -0.0075 0.0432  0.0039  293 LEU A CD1 
2490 C CD2 . LEU A 293 ? 0.3064 0.3982 0.2946 -0.0032 0.0460  -0.0016 293 LEU A CD2 
2491 N N   . ARG A 294 ? 0.1696 0.2191 0.1506 -0.0070 0.0309  -0.0302 294 ARG A N   
2492 C CA  . ARG A 294 ? 0.1697 0.2096 0.1541 -0.0071 0.0294  -0.0354 294 ARG A CA  
2493 C C   . ARG A 294 ? 0.1887 0.2325 0.1773 -0.0051 0.0322  -0.0331 294 ARG A C   
2494 O O   . ARG A 294 ? 0.1808 0.2345 0.1669 -0.0010 0.0349  -0.0335 294 ARG A O   
2495 C CB  . ARG A 294 ? 0.1802 0.2170 0.1606 -0.0043 0.0276  -0.0450 294 ARG A CB  
2496 C CG  . ARG A 294 ? 0.1841 0.2097 0.1691 -0.0043 0.0265  -0.0495 294 ARG A CG  
2497 C CD  . ARG A 294 ? 0.1925 0.2123 0.1755 -0.0031 0.0242  -0.0590 294 ARG A CD  
2498 N NE  . ARG A 294 ? 0.2887 0.3169 0.2662 0.0019  0.0253  -0.0650 294 ARG A NE  
2499 C CZ  . ARG A 294 ? 0.2537 0.2863 0.2258 0.0029  0.0234  -0.0711 294 ARG A CZ  
2500 N NH1 . ARG A 294 ? 0.2314 0.2606 0.2034 -0.0012 0.0202  -0.0718 294 ARG A NH1 
2501 N NH2 . ARG A 294 ? 0.2648 0.3063 0.2315 0.0084  0.0245  -0.0769 294 ARG A NH2 
2502 N N   . TYR A 295 ? 0.1600 0.1978 0.1549 -0.0077 0.0316  -0.0307 295 TYR A N   
2503 C CA  . TYR A 295 ? 0.1877 0.2305 0.1874 -0.0059 0.0340  -0.0285 295 TYR A CA  
2504 C C   . TYR A 295 ? 0.1964 0.2331 0.1971 -0.0025 0.0336  -0.0340 295 TYR A C   
2505 O O   . TYR A 295 ? 0.1928 0.2191 0.1935 -0.0035 0.0312  -0.0376 295 TYR A O   
2506 C CB  . TYR A 295 ? 0.1793 0.2216 0.1859 -0.0105 0.0336  -0.0223 295 TYR A CB  
2507 C CG  . TYR A 295 ? 0.1576 0.2069 0.1652 -0.0131 0.0351  -0.0159 295 TYR A CG  
2508 C CD1 . TYR A 295 ? 0.1528 0.1984 0.1576 -0.0159 0.0337  -0.0141 295 TYR A CD1 
2509 C CD2 . TYR A 295 ? 0.1913 0.2512 0.2032 -0.0127 0.0383  -0.0111 295 TYR A CD2 
2510 C CE1 . TYR A 295 ? 0.1831 0.2344 0.1894 -0.0179 0.0356  -0.0075 295 TYR A CE1 
2511 C CE2 . TYR A 295 ? 0.2068 0.2727 0.2209 -0.0153 0.0403  -0.0042 295 TYR A CE2 
2512 C CZ  . TYR A 295 ? 0.2297 0.2907 0.2410 -0.0178 0.0389  -0.0024 295 TYR A CZ  
2513 O OH  . TYR A 295 ? 0.2332 0.2993 0.2472 -0.0199 0.0413  0.0052  295 TYR A OH  
2514 N N   . TYR A 296 ? 0.1580 0.2018 0.1602 0.0018  0.0362  -0.0343 296 TYR A N   
2515 C CA  . TYR A 296 ? 0.1610 0.1997 0.1652 0.0058  0.0365  -0.0384 296 TYR A CA  
2516 C C   . TYR A 296 ? 0.1965 0.2403 0.2073 0.0057  0.0377  -0.0332 296 TYR A C   
2517 O O   . TYR A 296 ? 0.1974 0.2530 0.2100 0.0070  0.0402  -0.0299 296 TYR A O   
2518 C CB  . TYR A 296 ? 0.1737 0.2165 0.1736 0.0123  0.0386  -0.0444 296 TYR A CB  
2519 C CG  . TYR A 296 ? 0.2039 0.2441 0.1970 0.0127  0.0371  -0.0505 296 TYR A CG  
2520 C CD1 . TYR A 296 ? 0.2166 0.2444 0.2096 0.0099  0.0339  -0.0547 296 TYR A CD1 
2521 C CD2 . TYR A 296 ? 0.2906 0.3422 0.2778 0.0160  0.0389  -0.0520 296 TYR A CD2 
2522 C CE1 . TYR A 296 ? 0.2303 0.2571 0.2179 0.0100  0.0321  -0.0610 296 TYR A CE1 
2523 C CE2 . TYR A 296 ? 0.2527 0.3039 0.2336 0.0167  0.0371  -0.0583 296 TYR A CE2 
2524 C CZ  . TYR A 296 ? 0.2876 0.3263 0.2689 0.0135  0.0335  -0.0632 296 TYR A CZ  
2525 O OH  . TYR A 296 ? 0.2557 0.2954 0.2314 0.0141  0.0314  -0.0700 296 TYR A OH  
2526 N N   . PHE A 297 ? 0.1933 0.2297 0.2083 0.0042  0.0358  -0.0323 297 PHE A N   
2527 C CA  . PHE A 297 ? 0.1417 0.1839 0.1630 0.0046  0.0363  -0.0282 297 PHE A CA  
2528 C C   . PHE A 297 ? 0.1620 0.2064 0.1842 0.0115  0.0386  -0.0306 297 PHE A C   
2529 O O   . PHE A 297 ? 0.2029 0.2376 0.2248 0.0145  0.0381  -0.0338 297 PHE A O   
2530 C CB  . PHE A 297 ? 0.1653 0.2005 0.1898 0.0012  0.0334  -0.0263 297 PHE A CB  
2531 C CG  . PHE A 297 ? 0.1353 0.1775 0.1660 0.0020  0.0334  -0.0230 297 PHE A CG  
2532 C CD1 . PHE A 297 ? 0.1505 0.2024 0.1857 -0.0017 0.0332  -0.0194 297 PHE A CD1 
2533 C CD2 . PHE A 297 ? 0.1840 0.2236 0.2167 0.0067  0.0336  -0.0235 297 PHE A CD2 
2534 C CE1 . PHE A 297 ? 0.1411 0.2010 0.1826 -0.0012 0.0326  -0.0171 297 PHE A CE1 
2535 C CE2 . PHE A 297 ? 0.1910 0.2389 0.2291 0.0080  0.0333  -0.0205 297 PHE A CE2 
2536 C CZ  . PHE A 297 ? 0.1312 0.1899 0.1738 0.0039  0.0326  -0.0178 297 PHE A CZ  
2537 N N   . ARG A 298 ? 0.1521 0.2092 0.1761 0.0142  0.0413  -0.0287 298 ARG A N   
2538 C CA  . ARG A 298 ? 0.1825 0.2441 0.2077 0.0215  0.0439  -0.0304 298 ARG A CA  
2539 C C   . ARG A 298 ? 0.2206 0.2733 0.2404 0.0267  0.0447  -0.0375 298 ARG A C   
2540 O O   . ARG A 298 ? 0.2095 0.2600 0.2307 0.0330  0.0462  -0.0398 298 ARG A O   
2541 C CB  . ARG A 298 ? 0.1924 0.2537 0.2236 0.0230  0.0431  -0.0278 298 ARG A CB  
2542 C CG  . ARG A 298 ? 0.1573 0.2292 0.1946 0.0182  0.0421  -0.0222 298 ARG A CG  
2543 C CD  . ARG A 298 ? 0.2432 0.3180 0.2861 0.0205  0.0412  -0.0199 298 ARG A CD  
2544 N NE  . ARG A 298 ? 0.2205 0.3053 0.2695 0.0150  0.0394  -0.0160 298 ARG A NE  
2545 C CZ  . ARG A 298 ? 0.2371 0.3257 0.2910 0.0148  0.0373  -0.0141 298 ARG A CZ  
2546 N NH1 . ARG A 298 ? 0.2440 0.3278 0.2973 0.0202  0.0370  -0.0145 298 ARG A NH1 
2547 N NH2 . ARG A 298 ? 0.2614 0.3591 0.3212 0.0093  0.0354  -0.0119 298 ARG A NH2 
2548 N N   . GLU A 299 ? 0.2183 0.2660 0.2324 0.0245  0.0436  -0.0413 299 GLU A N   
2549 C CA  . GLU A 299 ? 0.2044 0.2430 0.2140 0.0283  0.0434  -0.0493 299 GLU A CA  
2550 C C   . GLU A 299 ? 0.2580 0.2814 0.2709 0.0287  0.0418  -0.0514 299 GLU A C   
2551 O O   . GLU A 299 ? 0.2818 0.2969 0.2938 0.0330  0.0423  -0.0579 299 GLU A O   
2552 C CB  . GLU A 299 ? 0.2238 0.2702 0.2308 0.0361  0.0466  -0.0535 299 GLU A CB  
2553 C CG  . GLU A 299 ? 0.3084 0.3716 0.3125 0.0366  0.0489  -0.0506 299 GLU A CG  
2554 C CD  . GLU A 299 ? 0.3885 0.4526 0.3852 0.0351  0.0480  -0.0544 299 GLU A CD  
2555 O OE1 . GLU A 299 ? 0.4075 0.4847 0.3999 0.0388  0.0505  -0.0546 299 GLU A OE1 
2556 O OE2 . GLU A 299 ? 0.3117 0.3650 0.3069 0.0307  0.0448  -0.0569 299 GLU A OE2 
2557 N N   . LEU A 300 ? 0.1754 0.1954 0.1926 0.0246  0.0401  -0.0460 300 LEU A N   
2558 C CA  . LEU A 300 ? 0.2137 0.2210 0.2345 0.0251  0.0391  -0.0460 300 LEU A CA  
2559 C C   . LEU A 300 ? 0.2201 0.2173 0.2399 0.0192  0.0362  -0.0470 300 LEU A C   
2560 O O   . LEU A 300 ? 0.2399 0.2251 0.2614 0.0199  0.0356  -0.0502 300 LEU A O   
2561 C CB  . LEU A 300 ? 0.1663 0.1781 0.1924 0.0256  0.0392  -0.0392 300 LEU A CB  
2562 C CG  . LEU A 300 ? 0.2575 0.2808 0.2861 0.0313  0.0419  -0.0372 300 LEU A CG  
2563 C CD1 . LEU A 300 ? 0.2394 0.2677 0.2733 0.0313  0.0412  -0.0309 300 LEU A CD1 
2564 C CD2 . LEU A 300 ? 0.3387 0.3562 0.3671 0.0390  0.0444  -0.0420 300 LEU A CD2 
2565 N N   . ILE A 301 ? 0.1783 0.1802 0.1962 0.0135  0.0344  -0.0440 301 ILE A N   
2566 C CA  . ILE A 301 ? 0.1581 0.1523 0.1755 0.0081  0.0317  -0.0437 301 ILE A CA  
2567 C C   . ILE A 301 ? 0.1800 0.1806 0.1929 0.0039  0.0306  -0.0433 301 ILE A C   
2568 O O   . ILE A 301 ? 0.1774 0.1885 0.1901 0.0035  0.0317  -0.0399 301 ILE A O   
2569 C CB  . ILE A 301 ? 0.1784 0.1701 0.2002 0.0063  0.0306  -0.0379 301 ILE A CB  
2570 C CG1 . ILE A 301 ? 0.1604 0.1453 0.1816 0.0011  0.0280  -0.0372 301 ILE A CG1 
2571 C CG2 . ILE A 301 ? 0.1867 0.1899 0.2100 0.0054  0.0307  -0.0329 301 ILE A CG2 
2572 C CD1 . ILE A 301 ? 0.2139 0.1957 0.2393 0.0008  0.0272  -0.0321 301 ILE A CD1 
2573 N N   . SER A 302 ? 0.1746 0.1696 0.1848 0.0008  0.0286  -0.0464 302 SER A N   
2574 C CA  . SER A 302 ? 0.1791 0.1798 0.1851 -0.0027 0.0276  -0.0454 302 SER A CA  
2575 C C   . SER A 302 ? 0.1816 0.1816 0.1896 -0.0075 0.0260  -0.0396 302 SER A C   
2576 O O   . SER A 302 ? 0.1728 0.1657 0.1838 -0.0090 0.0246  -0.0384 302 SER A O   
2577 C CB  . SER A 302 ? 0.2042 0.2007 0.2063 -0.0036 0.0259  -0.0516 302 SER A CB  
2578 O OG  . SER A 302 ? 0.2313 0.2297 0.2308 0.0011  0.0272  -0.0582 302 SER A OG  
2579 N N   . VAL A 303 ? 0.1781 0.1859 0.1847 -0.0097 0.0263  -0.0358 303 VAL A N   
2580 C CA  . VAL A 303 ? 0.1807 0.1883 0.1895 -0.0140 0.0249  -0.0308 303 VAL A CA  
2581 C C   . VAL A 303 ? 0.2017 0.2125 0.2067 -0.0164 0.0245  -0.0295 303 VAL A C   
2582 O O   . VAL A 303 ? 0.1985 0.2170 0.2010 -0.0149 0.0265  -0.0289 303 VAL A O   
2583 C CB  . VAL A 303 ? 0.1640 0.1782 0.1776 -0.0141 0.0260  -0.0265 303 VAL A CB  
2584 C CG1 . VAL A 303 ? 0.2134 0.2265 0.2295 -0.0186 0.0241  -0.0228 303 VAL A CG1 
2585 C CG2 . VAL A 303 ? 0.1876 0.2008 0.2047 -0.0106 0.0266  -0.0274 303 VAL A CG2 
2586 N N   . PHE A 304 ? 0.1224 0.1280 0.1268 -0.0196 0.0223  -0.0285 304 PHE A N   
2587 C CA  . PHE A 304 ? 0.1150 0.1237 0.1170 -0.0218 0.0220  -0.0255 304 PHE A CA  
2588 C C   . PHE A 304 ? 0.1523 0.1596 0.1585 -0.0250 0.0213  -0.0209 304 PHE A C   
2589 O O   . PHE A 304 ? 0.1831 0.1856 0.1922 -0.0258 0.0198  -0.0212 304 PHE A O   
2590 C CB  . PHE A 304 ? 0.1362 0.1412 0.1342 -0.0227 0.0200  -0.0283 304 PHE A CB  
2591 C CG  . PHE A 304 ? 0.1311 0.1397 0.1245 -0.0200 0.0204  -0.0333 304 PHE A CG  
2592 C CD1 . PHE A 304 ? 0.1553 0.1729 0.1444 -0.0185 0.0218  -0.0319 304 PHE A CD1 
2593 C CD2 . PHE A 304 ? 0.1849 0.1881 0.1785 -0.0188 0.0192  -0.0396 304 PHE A CD2 
2594 C CE1 . PHE A 304 ? 0.2135 0.2358 0.1975 -0.0154 0.0218  -0.0375 304 PHE A CE1 
2595 C CE2 . PHE A 304 ? 0.2016 0.2079 0.1912 -0.0164 0.0191  -0.0457 304 PHE A CE2 
2596 C CZ  . PHE A 304 ? 0.2010 0.2175 0.1852 -0.0144 0.0202  -0.0451 304 PHE A CZ  
2597 N N   . PHE A 305 ? 0.1451 0.1568 0.1518 -0.0266 0.0224  -0.0166 305 PHE A N   
2598 C CA  . PHE A 305 ? 0.1262 0.1359 0.1374 -0.0298 0.0216  -0.0129 305 PHE A CA  
2599 C C   . PHE A 305 ? 0.1257 0.1322 0.1339 -0.0311 0.0205  -0.0112 305 PHE A C   
2600 O O   . PHE A 305 ? 0.1716 0.1822 0.1764 -0.0302 0.0218  -0.0093 305 PHE A O   
2601 C CB  . PHE A 305 ? 0.1340 0.1503 0.1502 -0.0310 0.0239  -0.0088 305 PHE A CB  
2602 C CG  . PHE A 305 ? 0.1972 0.2185 0.2166 -0.0293 0.0251  -0.0101 305 PHE A CG  
2603 C CD1 . PHE A 305 ? 0.1913 0.2185 0.2077 -0.0258 0.0274  -0.0114 305 PHE A CD1 
2604 C CD2 . PHE A 305 ? 0.1670 0.1880 0.1923 -0.0307 0.0238  -0.0104 305 PHE A CD2 
2605 C CE1 . PHE A 305 ? 0.1459 0.1779 0.1654 -0.0236 0.0287  -0.0124 305 PHE A CE1 
2606 C CE2 . PHE A 305 ? 0.1226 0.1494 0.1511 -0.0287 0.0249  -0.0113 305 PHE A CE2 
2607 C CZ  . PHE A 305 ? 0.1592 0.1911 0.1848 -0.0251 0.0274  -0.0121 305 PHE A CZ  
2608 N N   . ARG A 306 ? 0.1434 0.1436 0.1527 -0.0326 0.0181  -0.0117 306 ARG A N   
2609 C CA  . ARG A 306 ? 0.1439 0.1412 0.1504 -0.0333 0.0169  -0.0104 306 ARG A CA  
2610 C C   . ARG A 306 ? 0.1854 0.1843 0.1938 -0.0346 0.0184  -0.0052 306 ARG A C   
2611 O O   . ARG A 306 ? 0.1673 0.1674 0.1813 -0.0362 0.0196  -0.0029 306 ARG A O   
2612 C CB  . ARG A 306 ? 0.1566 0.1477 0.1640 -0.0341 0.0143  -0.0119 306 ARG A CB  
2613 C CG  . ARG A 306 ? 0.1986 0.1878 0.2111 -0.0358 0.0137  -0.0106 306 ARG A CG  
2614 C CD  . ARG A 306 ? 0.2555 0.2402 0.2680 -0.0356 0.0112  -0.0122 306 ARG A CD  
2615 N NE  . ARG A 306 ? 0.2513 0.2348 0.2684 -0.0371 0.0104  -0.0118 306 ARG A NE  
2616 C CZ  . ARG A 306 ? 0.1620 0.1419 0.1797 -0.0372 0.0085  -0.0124 306 ARG A CZ  
2617 N NH1 . ARG A 306 ? 0.1606 0.1381 0.1743 -0.0357 0.0075  -0.0126 306 ARG A NH1 
2618 N NH2 . ARG A 306 ? 0.1934 0.1723 0.2160 -0.0387 0.0077  -0.0132 306 ARG A NH2 
2619 N N   . ASP A 307 ? 0.1792 0.1785 0.1837 -0.0338 0.0185  -0.0031 307 ASP A N   
2620 C CA  . ASP A 307 ? 0.1885 0.1873 0.1953 -0.0347 0.0198  0.0026  307 ASP A CA  
2621 C C   . ASP A 307 ? 0.1425 0.1335 0.1530 -0.0365 0.0177  0.0020  307 ASP A C   
2622 O O   . ASP A 307 ? 0.1591 0.1467 0.1667 -0.0357 0.0157  0.0006  307 ASP A O   
2623 C CB  . ASP A 307 ? 0.2031 0.2055 0.2041 -0.0324 0.0204  0.0051  307 ASP A CB  
2624 C CG  . ASP A 307 ? 0.2235 0.2264 0.2270 -0.0325 0.0227  0.0125  307 ASP A CG  
2625 O OD1 . ASP A 307 ? 0.2138 0.2097 0.2223 -0.0344 0.0222  0.0142  307 ASP A OD1 
2626 O OD2 . ASP A 307 ? 0.2875 0.2979 0.2881 -0.0303 0.0252  0.0166  307 ASP A OD2 
2627 N N   . LYS A 308 ? 0.1790 0.1680 0.1963 -0.0388 0.0181  0.0027  308 LYS A N   
2628 C CA  . LYS A 308 ? 0.1519 0.1344 0.1729 -0.0402 0.0158  0.0008  308 LYS A CA  
2629 C C   . LYS A 308 ? 0.1607 0.1383 0.1812 -0.0397 0.0157  0.0039  308 LYS A C   
2630 O O   . LYS A 308 ? 0.1844 0.1574 0.2033 -0.0388 0.0134  0.0014  308 LYS A O   
2631 C CB  . LYS A 308 ? 0.1336 0.1163 0.1629 -0.0431 0.0160  0.0004  308 LYS A CB  
2632 C CG  . LYS A 308 ? 0.1725 0.1490 0.2063 -0.0446 0.0135  -0.0024 308 LYS A CG  
2633 C CD  . LYS A 308 ? 0.2089 0.1872 0.2521 -0.0480 0.0134  -0.0034 308 LYS A CD  
2634 C CE  . LYS A 308 ? 0.2612 0.2330 0.3099 -0.0497 0.0110  -0.0064 308 LYS A CE  
2635 N NZ  . LYS A 308 ? 0.2541 0.2240 0.2971 -0.0469 0.0078  -0.0115 308 LYS A NZ  
2636 N N   . THR A 309 ? 0.1678 0.1466 0.1895 -0.0397 0.0185  0.0098  309 THR A N   
2637 C CA  . THR A 309 ? 0.1581 0.1321 0.1799 -0.0386 0.0189  0.0136  309 THR A CA  
2638 C C   . THR A 309 ? 0.1610 0.1358 0.1751 -0.0355 0.0172  0.0123  309 THR A C   
2639 O O   . THR A 309 ? 0.1762 0.1457 0.1900 -0.0345 0.0155  0.0113  309 THR A O   
2640 C CB  . THR A 309 ? 0.1764 0.1534 0.2005 -0.0384 0.0227  0.0216  309 THR A CB  
2641 O OG1 . THR A 309 ? 0.2191 0.1950 0.2522 -0.0419 0.0244  0.0233  309 THR A OG1 
2642 C CG2 . THR A 309 ? 0.2324 0.2044 0.2563 -0.0364 0.0234  0.0264  309 THR A CG2 
2643 N N   . LEU A 310 ? 0.1316 0.1136 0.1397 -0.0339 0.0176  0.0120  310 LEU A N   
2644 C CA  . LEU A 310 ? 0.1171 0.1011 0.1191 -0.0316 0.0158  0.0104  310 LEU A CA  
2645 C C   . LEU A 310 ? 0.1313 0.1114 0.1332 -0.0321 0.0128  0.0049  310 LEU A C   
2646 O O   . LEU A 310 ? 0.1293 0.1081 0.1291 -0.0306 0.0113  0.0045  310 LEU A O   
2647 C CB  . LEU A 310 ? 0.1240 0.1166 0.1205 -0.0302 0.0163  0.0095  310 LEU A CB  
2648 C CG  . LEU A 310 ? 0.1618 0.1609 0.1567 -0.0283 0.0193  0.0156  310 LEU A CG  
2649 C CD1 . LEU A 310 ? 0.2368 0.2454 0.2258 -0.0265 0.0193  0.0128  310 LEU A CD1 
2650 C CD2 . LEU A 310 ? 0.2016 0.2000 0.1954 -0.0260 0.0197  0.0209  310 LEU A CD2 
2651 N N   . SER A 311 ? 0.1464 0.1258 0.1504 -0.0338 0.0122  0.0011  311 SER A N   
2652 C CA  . SER A 311 ? 0.1391 0.1162 0.1431 -0.0337 0.0098  -0.0032 311 SER A CA  
2653 C C   . SER A 311 ? 0.1531 0.1248 0.1597 -0.0335 0.0086  -0.0034 311 SER A C   
2654 O O   . SER A 311 ? 0.1562 0.1269 0.1609 -0.0320 0.0070  -0.0048 311 SER A O   
2655 C CB  . SER A 311 ? 0.1469 0.1251 0.1530 -0.0348 0.0098  -0.0063 311 SER A CB  
2656 O OG  . SER A 311 ? 0.1414 0.1241 0.1450 -0.0345 0.0110  -0.0069 311 SER A OG  
2657 N N   . ASP A 312 ? 0.1751 0.1435 0.1865 -0.0348 0.0095  -0.0020 312 ASP A N   
2658 C CA  . ASP A 312 ? 0.1791 0.1417 0.1936 -0.0344 0.0081  -0.0033 312 ASP A CA  
2659 C C   . ASP A 312 ? 0.1890 0.1488 0.2013 -0.0321 0.0084  -0.0001 312 ASP A C   
2660 O O   . ASP A 312 ? 0.1598 0.1158 0.1724 -0.0304 0.0069  -0.0021 312 ASP A O   
2661 C CB  . ASP A 312 ? 0.1762 0.1356 0.1979 -0.0371 0.0088  -0.0032 312 ASP A CB  
2662 C CG  . ASP A 312 ? 0.2580 0.2201 0.2828 -0.0390 0.0077  -0.0074 312 ASP A CG  
2663 O OD1 . ASP A 312 ? 0.2426 0.2079 0.2642 -0.0377 0.0062  -0.0105 312 ASP A OD1 
2664 O OD2 . ASP A 312 ? 0.2456 0.2072 0.2771 -0.0418 0.0084  -0.0070 312 ASP A OD2 
2665 N N   . LEU A 313 ? 0.1475 0.1098 0.1577 -0.0313 0.0105  0.0049  313 LEU A N   
2666 C CA  . LEU A 313 ? 0.1595 0.1204 0.1674 -0.0283 0.0108  0.0083  313 LEU A CA  
2667 C C   . LEU A 313 ? 0.1760 0.1396 0.1795 -0.0262 0.0086  0.0055  313 LEU A C   
2668 O O   . LEU A 313 ? 0.1769 0.1373 0.1802 -0.0237 0.0077  0.0054  313 LEU A O   
2669 C CB  . LEU A 313 ? 0.1394 0.1055 0.1449 -0.0272 0.0132  0.0143  313 LEU A CB  
2670 C CG  . LEU A 313 ? 0.2071 0.1701 0.2181 -0.0284 0.0162  0.0195  313 LEU A CG  
2671 C CD1 . LEU A 313 ? 0.1893 0.1606 0.1970 -0.0272 0.0188  0.0251  313 LEU A CD1 
2672 C CD2 . LEU A 313 ? 0.1947 0.1491 0.2098 -0.0269 0.0168  0.0226  313 LEU A CD2 
2673 N N   . ILE A 314 ? 0.1354 0.1048 0.1358 -0.0270 0.0077  0.0032  314 ILE A N   
2674 C CA  . ILE A 314 ? 0.1398 0.1122 0.1374 -0.0256 0.0059  0.0012  314 ILE A CA  
2675 C C   . ILE A 314 ? 0.1815 0.1505 0.1810 -0.0253 0.0044  -0.0024 314 ILE A C   
2676 O O   . ILE A 314 ? 0.1886 0.1575 0.1871 -0.0228 0.0034  -0.0027 314 ILE A O   
2677 C CB  . ILE A 314 ? 0.1484 0.1268 0.1438 -0.0270 0.0055  -0.0006 314 ILE A CB  
2678 C CG1 . ILE A 314 ? 0.1217 0.1055 0.1141 -0.0264 0.0066  0.0022  314 ILE A CG1 
2679 C CG2 . ILE A 314 ? 0.1634 0.1444 0.1580 -0.0264 0.0038  -0.0025 314 ILE A CG2 
2680 C CD1 . ILE A 314 ? 0.1596 0.1492 0.1501 -0.0278 0.0059  -0.0009 314 ILE A CD1 
2681 N N   . GLY A 315 ? 0.1551 0.1225 0.1572 -0.0272 0.0043  -0.0050 315 GLY A N   
2682 C CA  . GLY A 315 ? 0.1612 0.1279 0.1642 -0.0264 0.0027  -0.0085 315 GLY A CA  
2683 C C   . GLY A 315 ? 0.1917 0.1537 0.1967 -0.0247 0.0019  -0.0101 315 GLY A C   
2684 O O   . GLY A 315 ? 0.1900 0.1531 0.1941 -0.0224 0.0004  -0.0127 315 GLY A O   
2685 N N   . PHE A 316 ? 0.1642 0.1211 0.1720 -0.0254 0.0028  -0.0085 316 PHE A N   
2686 C CA  . PHE A 316 ? 0.1838 0.1346 0.1949 -0.0243 0.0019  -0.0111 316 PHE A CA  
2687 C C   . PHE A 316 ? 0.1881 0.1334 0.2001 -0.0224 0.0031  -0.0076 316 PHE A C   
2688 O O   . PHE A 316 ? 0.2603 0.2005 0.2739 -0.0201 0.0021  -0.0102 316 PHE A O   
2689 C CB  . PHE A 316 ? 0.1840 0.1323 0.2009 -0.0276 0.0016  -0.0139 316 PHE A CB  
2690 C CG  . PHE A 316 ? 0.2872 0.2409 0.3037 -0.0284 0.0001  -0.0178 316 PHE A CG  
2691 C CD1 . PHE A 316 ? 0.3365 0.2920 0.3520 -0.0258 -0.0023 -0.0226 316 PHE A CD1 
2692 C CD2 . PHE A 316 ? 0.3244 0.2822 0.3411 -0.0308 0.0011  -0.0164 316 PHE A CD2 
2693 C CE1 . PHE A 316 ? 0.3718 0.3333 0.3866 -0.0257 -0.0034 -0.0251 316 PHE A CE1 
2694 C CE2 . PHE A 316 ? 0.4300 0.3928 0.4464 -0.0308 0.0000  -0.0193 316 PHE A CE2 
2695 C CZ  . PHE A 316 ? 0.4202 0.3850 0.4358 -0.0282 -0.0022 -0.0233 316 PHE A CZ  
2696 N N   . SER A 317 ? 0.1657 0.1121 0.1767 -0.0229 0.0053  -0.0019 317 SER A N   
2697 C CA  . SER A 317 ? 0.1342 0.0753 0.1471 -0.0209 0.0070  0.0027  317 SER A CA  
2698 C C   . SER A 317 ? 0.1681 0.1127 0.1758 -0.0166 0.0071  0.0058  317 SER A C   
2699 O O   . SER A 317 ? 0.1881 0.1277 0.1966 -0.0131 0.0071  0.0063  317 SER A O   
2700 C CB  . SER A 317 ? 0.2010 0.1422 0.2166 -0.0234 0.0098  0.0083  317 SER A CB  
2701 O OG  . SER A 317 ? 0.2764 0.2144 0.2982 -0.0274 0.0099  0.0059  317 SER A OG  
2702 N N   . TYR A 318 ? 0.1556 0.1089 0.1586 -0.0166 0.0071  0.0076  318 TYR A N   
2703 C CA  . TYR A 318 ? 0.1565 0.1148 0.1557 -0.0130 0.0075  0.0117  318 TYR A CA  
2704 C C   . TYR A 318 ? 0.1962 0.1556 0.1935 -0.0094 0.0059  0.0095  318 TYR A C   
2705 O O   . TYR A 318 ? 0.1892 0.1518 0.1844 -0.0056 0.0062  0.0130  318 TYR A O   
2706 C CB  . TYR A 318 ? 0.1791 0.1472 0.1745 -0.0145 0.0074  0.0128  318 TYR A CB  
2707 C CG  . TYR A 318 ? 0.1853 0.1551 0.1809 -0.0161 0.0095  0.0167  318 TYR A CG  
2708 C CD1 . TYR A 318 ? 0.2099 0.1746 0.2084 -0.0150 0.0120  0.0219  318 TYR A CD1 
2709 C CD2 . TYR A 318 ? 0.1594 0.1363 0.1525 -0.0183 0.0092  0.0152  318 TYR A CD2 
2710 C CE1 . TYR A 318 ? 0.1818 0.1500 0.1804 -0.0159 0.0143  0.0264  318 TYR A CE1 
2711 C CE2 . TYR A 318 ? 0.1440 0.1244 0.1365 -0.0190 0.0112  0.0185  318 TYR A CE2 
2712 C CZ  . TYR A 318 ? 0.2019 0.1786 0.1969 -0.0177 0.0139  0.0244  318 TYR A CZ  
2713 O OH  . TYR A 318 ? 0.2076 0.1895 0.2019 -0.0180 0.0162  0.0285  318 TYR A OH  
2714 N N   . HIS A 319 ? 0.2026 0.1607 0.2005 -0.0098 0.0042  0.0041  319 HIS A N   
2715 C CA  . HIS A 319 ? 0.1967 0.1560 0.1931 -0.0054 0.0031  0.0025  319 HIS A CA  
2716 C C   . HIS A 319 ? 0.1957 0.1477 0.1935 -0.0012 0.0040  0.0041  319 HIS A C   
2717 O O   . HIS A 319 ? 0.2200 0.1748 0.2158 0.0035  0.0038  0.0052  319 HIS A O   
2718 C CB  . HIS A 319 ? 0.1673 0.1260 0.1643 -0.0057 0.0014  -0.0034 319 HIS A CB  
2719 C CG  . HIS A 319 ? 0.1764 0.1260 0.1772 -0.0061 0.0010  -0.0073 319 HIS A CG  
2720 N ND1 . HIS A 319 ? 0.2505 0.1947 0.2522 -0.0020 0.0003  -0.0103 319 HIS A ND1 
2721 C CD2 . HIS A 319 ? 0.1817 0.1269 0.1864 -0.0103 0.0011  -0.0091 319 HIS A CD2 
2722 C CE1 . HIS A 319 ? 0.2252 0.1618 0.2315 -0.0040 -0.0003 -0.0144 319 HIS A CE1 
2723 N NE2 . HIS A 319 ? 0.2620 0.1994 0.2705 -0.0092 0.0002  -0.0134 319 HIS A NE2 
2724 N N   . ALA A 320 ? 0.1886 0.1315 0.1908 -0.0028 0.0051  0.0047  320 ALA A N   
2725 C CA  . ALA A 320 ? 0.1844 0.1182 0.1896 0.0008  0.0063  0.0063  320 ALA A CA  
2726 C C   . ALA A 320 ? 0.2522 0.1873 0.2568 0.0030  0.0088  0.0146  320 ALA A C   
2727 O O   . ALA A 320 ? 0.2381 0.1650 0.2459 0.0063  0.0103  0.0175  320 ALA A O   
2728 C CB  . ALA A 320 ? 0.1934 0.1164 0.2054 -0.0024 0.0064  0.0030  320 ALA A CB  
2729 N N   . TRP A 321 ? 0.2344 0.1795 0.2351 0.0017  0.0091  0.0183  321 TRP A N   
2730 C CA  . TRP A 321 ? 0.2363 0.1859 0.2354 0.0041  0.0112  0.0261  321 TRP A CA  
2731 C C   . TRP A 321 ? 0.2096 0.1705 0.2036 0.0078  0.0100  0.0275  321 TRP A C   
2732 O O   . TRP A 321 ? 0.2582 0.2256 0.2500 0.0066  0.0079  0.0232  321 TRP A O   
2733 C CB  . TRP A 321 ? 0.2197 0.1747 0.2181 0.0000  0.0122  0.0288  321 TRP A CB  
2734 C CG  . TRP A 321 ? 0.2127 0.1599 0.2163 -0.0041 0.0138  0.0290  321 TRP A CG  
2735 C CD1 . TRP A 321 ? 0.2080 0.1476 0.2160 -0.0076 0.0127  0.0231  321 TRP A CD1 
2736 C CD2 . TRP A 321 ? 0.2458 0.1945 0.2509 -0.0053 0.0166  0.0354  321 TRP A CD2 
2737 N NE1 . TRP A 321 ? 0.2430 0.1788 0.2560 -0.0112 0.0147  0.0256  321 TRP A NE1 
2738 C CE2 . TRP A 321 ? 0.2256 0.1668 0.2369 -0.0098 0.0173  0.0335  321 TRP A CE2 
2739 C CE3 . TRP A 321 ? 0.2575 0.2144 0.2593 -0.0025 0.0186  0.0429  321 TRP A CE3 
2740 C CZ2 . TRP A 321 ? 0.2780 0.2193 0.2928 -0.0119 0.0204  0.0393  321 TRP A CZ2 
2741 C CZ3 . TRP A 321 ? 0.2384 0.1957 0.2428 -0.0040 0.0217  0.0487  321 TRP A CZ3 
2742 C CH2 . TRP A 321 ? 0.2929 0.2422 0.3040 -0.0088 0.0228  0.0471  321 TRP A CH2 
2743 N N   . ASN A 322 ? 0.2337 0.1975 0.2266 0.0124  0.0117  0.0342  322 ASN A N   
2744 C CA  . ASN A 322 ? 0.2428 0.2203 0.2313 0.0152  0.0108  0.0368  322 ASN A CA  
2745 C C   . ASN A 322 ? 0.3135 0.3011 0.2993 0.0104  0.0096  0.0354  322 ASN A C   
2746 O O   . ASN A 322 ? 0.2681 0.2535 0.2547 0.0070  0.0108  0.0362  322 ASN A O   
2747 C CB  . ASN A 322 ? 0.3742 0.3523 0.3624 0.0212  0.0132  0.0452  322 ASN A CB  
2748 C CG  . ASN A 322 ? 0.4722 0.4663 0.4561 0.0235  0.0126  0.0492  322 ASN A CG  
2749 O OD1 . ASN A 322 ? 0.4302 0.4314 0.4120 0.0208  0.0127  0.0505  322 ASN A OD1 
2750 N ND2 . ASN A 322 ? 0.4625 0.4629 0.4449 0.0291  0.0121  0.0514  322 ASN A ND2 
2751 N N   . ALA A 323 ? 0.2691 0.1829 0.2728 0.0547  0.0258  0.0617  323 ALA A N   
2752 C CA  . ALA A 323 ? 0.2327 0.1701 0.2414 0.0444  0.0159  0.0575  323 ALA A CA  
2753 C C   . ALA A 323 ? 0.2094 0.1527 0.2098 0.0473  0.0112  0.0653  323 ALA A C   
2754 O O   . ALA A 323 ? 0.2267 0.1723 0.2232 0.0364  0.0081  0.0616  323 ALA A O   
2755 C CB  . ALA A 323 ? 0.2482 0.2155 0.2725 0.0455  0.0091  0.0537  323 ALA A CB  
2756 N N   . GLU A 324 ? 0.2515 0.1990 0.2485 0.0633  0.0108  0.0764  324 GLU A N   
2757 C CA  . GLU A 324 ? 0.2816 0.2356 0.2677 0.0676  0.0065  0.0851  324 GLU A CA  
2758 C C   . GLU A 324 ? 0.3167 0.2405 0.2867 0.0603  0.0146  0.0876  324 GLU A C   
2759 O O   . GLU A 324 ? 0.2957 0.2260 0.2589 0.0534  0.0110  0.0875  324 GLU A O   
2760 C CB  . GLU A 324 ? 0.4331 0.3967 0.4170 0.0859  0.0052  0.0953  324 GLU A CB  
2761 C CG  . GLU A 324 ? 0.7276 0.7301 0.7272 0.0936  -0.0044 0.0945  324 GLU A CG  
2762 C CD  . GLU A 324 ? 0.9742 0.9763 0.9867 0.0993  0.0003  0.0912  324 GLU A CD  
2763 O OE1 . GLU A 324 ? 1.0731 1.0835 1.0878 0.1122  0.0011  0.0953  324 GLU A OE1 
2764 O OE2 . GLU A 324 ? 1.0237 1.0174 1.0434 0.0898  0.0037  0.0833  324 GLU A OE2 
2765 N N   . ASP A 325 ? 0.3100 0.2055 0.2754 0.0585  0.0249  0.0853  325 ASP A N   
2766 C CA  . ASP A 325 ? 0.3181 0.1902 0.2719 0.0480  0.0324  0.0839  325 ASP A CA  
2767 C C   . ASP A 325 ? 0.2820 0.1549 0.2379 0.0312  0.0317  0.0753  325 ASP A C   
2768 O O   . ASP A 325 ? 0.2788 0.1475 0.2268 0.0233  0.0336  0.0759  325 ASP A O   
2769 C CB  . ASP A 325 ? 0.2944 0.1409 0.2457 0.0475  0.0427  0.0802  325 ASP A CB  
2770 C CG  . ASP A 325 ? 0.5505 0.3912 0.4971 0.0642  0.0460  0.0896  325 ASP A CG  
2771 O OD1 . ASP A 325 ? 0.6392 0.4953 0.5826 0.0752  0.0402  0.0993  325 ASP A OD1 
2772 O OD2 . ASP A 325 ? 0.6513 0.4729 0.5969 0.0664  0.0544  0.0868  325 ASP A OD2 
2773 N N   . ALA A 326 ? 0.2415 0.1205 0.2086 0.0258  0.0299  0.0669  326 ALA A N   
2774 C CA  . ALA A 326 ? 0.2661 0.1532 0.2378 0.0100  0.0272  0.0560  326 ALA A CA  
2775 C C   . ALA A 326 ? 0.2671 0.1767 0.2391 0.0077  0.0186  0.0562  326 ALA A C   
2776 O O   . ALA A 326 ? 0.2281 0.1377 0.1967 -0.0021 0.0196  0.0526  326 ALA A O   
2777 C CB  . ALA A 326 ? 0.2495 0.1457 0.2333 0.0061  0.0245  0.0460  326 ALA A CB  
2778 N N   . VAL A 327 ? 0.1821 0.1128 0.1587 0.0163  0.0104  0.0593  327 VAL A N   
2779 C CA  . VAL A 327 ? 0.2112 0.1628 0.1871 0.0133  0.0025  0.0577  327 VAL A CA  
2780 C C   . VAL A 327 ? 0.2168 0.1615 0.1770 0.0157  0.0054  0.0662  327 VAL A C   
2781 O O   . VAL A 327 ? 0.2491 0.1997 0.2050 0.0081  0.0042  0.0625  327 VAL A O   
2782 C CB  . VAL A 327 ? 0.1994 0.1769 0.1843 0.0200  -0.0066 0.0574  327 VAL A CB  
2783 C CG1 . VAL A 327 ? 0.2117 0.2093 0.1928 0.0172  -0.0141 0.0553  327 VAL A CG1 
2784 C CG2 . VAL A 327 ? 0.2199 0.2042 0.2194 0.0142  -0.0084 0.0481  327 VAL A CG2 
2785 N N   . ARG A 328 ? 0.2190 0.1500 0.1697 0.0270  0.0103  0.0781  328 ARG A N   
2786 C CA  . ARG A 328 ? 0.2770 0.1971 0.2101 0.0297  0.0152  0.0883  328 ARG A CA  
2787 C C   . ARG A 328 ? 0.2657 0.1669 0.1940 0.0155  0.0243  0.0839  328 ARG A C   
2788 O O   . ARG A 328 ? 0.2971 0.2023 0.2164 0.0106  0.0253  0.0851  328 ARG A O   
2789 C CB  . ARG A 328 ? 0.2762 0.1817 0.2018 0.0435  0.0199  0.0994  328 ARG A CB  
2790 C CG  . ARG A 328 ? 0.3631 0.2599 0.2727 0.0452  0.0240  0.1073  328 ARG A CG  
2791 C CD  . ARG A 328 ? 0.4988 0.3834 0.4036 0.0586  0.0281  0.1158  328 ARG A CD  
2792 N NE  . ARG A 328 ? 0.5743 0.4303 0.4816 0.0540  0.0388  0.1122  328 ARG A NE  
2793 C CZ  . ARG A 328 ? 0.6506 0.5002 0.5656 0.0614  0.0409  0.1106  328 ARG A CZ  
2794 N NH1 . ARG A 328 ? 0.5846 0.4556 0.5074 0.0739  0.0330  0.1129  328 ARG A NH1 
2795 N NH2 . ARG A 328 ? 0.6897 0.5138 0.6049 0.0558  0.0510  0.1058  328 ARG A NH2 
2796 N N   . ASP A 329 ? 0.2653 0.1488 0.2001 0.0082  0.0311  0.0777  329 ASP A N   
2797 C CA  . ASP A 329 ? 0.2505 0.1247 0.1858 -0.0069 0.0379  0.0699  329 ASP A CA  
2798 C C   . ASP A 329 ? 0.2611 0.1550 0.2017 -0.0164 0.0329  0.0615  329 ASP A C   
2799 O O   . ASP A 329 ? 0.2587 0.1530 0.1936 -0.0240 0.0372  0.0612  329 ASP A O   
2800 C CB  . ASP A 329 ? 0.2401 0.1040 0.1851 -0.0126 0.0415  0.0604  329 ASP A CB  
2801 C CG  . ASP A 329 ? 0.3107 0.1712 0.2581 -0.0268 0.0471  0.0518  329 ASP A CG  
2802 O OD1 . ASP A 329 ? 0.3217 0.1691 0.2616 -0.0283 0.0542  0.0558  329 ASP A OD1 
2803 O OD2 . ASP A 329 ? 0.3128 0.1857 0.2698 -0.0357 0.0444  0.0416  329 ASP A OD2 
2804 N N   . PHE A 330 ? 0.2173 0.1296 0.1705 -0.0158 0.0238  0.0536  330 PHE A N   
2805 C CA  . PHE A 330 ? 0.2490 0.1801 0.2093 -0.0230 0.0184  0.0442  330 PHE A CA  
2806 C C   . PHE A 330 ? 0.3067 0.2506 0.2587 -0.0208 0.0151  0.0470  330 PHE A C   
2807 O O   . PHE A 330 ? 0.2311 0.1799 0.1810 -0.0277 0.0176  0.0432  330 PHE A O   
2808 C CB  . PHE A 330 ? 0.2086 0.1522 0.1816 -0.0211 0.0108  0.0376  330 PHE A CB  
2809 C CG  . PHE A 330 ? 0.2037 0.1604 0.1843 -0.0275 0.0073  0.0282  330 PHE A CG  
2810 C CD1 . PHE A 330 ? 0.2665 0.2212 0.2530 -0.0345 0.0104  0.0219  330 PHE A CD1 
2811 C CD2 . PHE A 330 ? 0.2061 0.1775 0.1877 -0.0260 0.0010  0.0254  330 PHE A CD2 
2812 C CE1 . PHE A 330 ? 0.2248 0.1921 0.2180 -0.0374 0.0072  0.0148  330 PHE A CE1 
2813 C CE2 . PHE A 330 ? 0.2344 0.2139 0.2222 -0.0301 -0.0008 0.0174  330 PHE A CE2 
2814 C CZ  . PHE A 330 ? 0.2226 0.2001 0.2161 -0.0345 0.0022  0.0131  330 PHE A CZ  
2815 N N   . ILE A 331 ? 0.2380 0.1898 0.1851 -0.0111 0.0094  0.0533  331 ILE A N   
2816 C CA  . ILE A 331 ? 0.2560 0.2213 0.1927 -0.0089 0.0059  0.0555  331 ILE A CA  
2817 C C   . ILE A 331 ? 0.2948 0.2473 0.2163 -0.0108 0.0151  0.0632  331 ILE A C   
2818 O O   . ILE A 331 ? 0.2417 0.2029 0.1567 -0.0151 0.0160  0.0605  331 ILE A O   
2819 C CB  . ILE A 331 ? 0.3323 0.3116 0.2662 0.0022  -0.0023 0.0610  331 ILE A CB  
2820 C CG1 . ILE A 331 ? 0.3987 0.3926 0.3487 0.0013  -0.0102 0.0521  331 ILE A CG1 
2821 C CG2 . ILE A 331 ? 0.3522 0.3467 0.2724 0.0044  -0.0061 0.0630  331 ILE A CG2 
2822 C CD1 . ILE A 331 ? 0.3677 0.3725 0.3235 -0.0077 -0.0136 0.0396  331 ILE A CD1 
2823 N N   . GLY A 332 ? 0.2522 0.1824 0.1673 -0.0079 0.0233  0.0728  332 GLY A N   
2824 C CA  . GLY A 332 ? 0.3089 0.2233 0.2088 -0.0109 0.0342  0.0811  332 GLY A CA  
2825 C C   . GLY A 332 ? 0.3318 0.2460 0.2373 -0.0259 0.0408  0.0719  332 GLY A C   
2826 O O   . GLY A 332 ? 0.2995 0.2141 0.1946 -0.0303 0.0471  0.0749  332 GLY A O   
2827 N N   . ARG A 333 ? 0.2889 0.2054 0.2108 -0.0332 0.0394  0.0608  333 ARG A N   
2828 C CA  . ARG A 333 ? 0.2339 0.1571 0.1633 -0.0459 0.0441  0.0514  333 ARG A CA  
2829 C C   . ARG A 333 ? 0.2089 0.1556 0.1400 -0.0457 0.0382  0.0452  333 ARG A C   
2830 O O   . ARG A 333 ? 0.2411 0.1941 0.1700 -0.0524 0.0442  0.0429  333 ARG A O   
2831 C CB  . ARG A 333 ? 0.2157 0.1383 0.1606 -0.0518 0.0429  0.0418  333 ARG A CB  
2832 C CG  . ARG A 333 ? 0.2200 0.1242 0.1667 -0.0535 0.0491  0.0428  333 ARG A CG  
2833 C CD  . ARG A 333 ? 0.2338 0.1414 0.1939 -0.0559 0.0451  0.0330  333 ARG A CD  
2834 N NE  . ARG A 333 ? 0.2645 0.1567 0.2253 -0.0568 0.0498  0.0317  333 ARG A NE  
2835 C CZ  . ARG A 333 ? 0.3207 0.2122 0.2848 -0.0661 0.0551  0.0250  333 ARG A CZ  
2836 N NH1 . ARG A 333 ? 0.2945 0.2024 0.2637 -0.0741 0.0558  0.0194  333 ARG A NH1 
2837 N NH2 . ARG A 333 ? 0.3296 0.2046 0.2917 -0.0674 0.0601  0.0231  333 ARG A NH2 
2838 N N   . LEU A 334 ? 0.2199 0.1790 0.1546 -0.0383 0.0276  0.0420  334 LEU A N   
2839 C CA  . LEU A 334 ? 0.2217 0.1990 0.1558 -0.0377 0.0230  0.0354  334 LEU A CA  
2840 C C   . LEU A 334 ? 0.2167 0.1966 0.1331 -0.0358 0.0265  0.0419  334 LEU A C   
2841 O O   . LEU A 334 ? 0.2539 0.2445 0.1677 -0.0392 0.0292  0.0366  334 LEU A O   
2842 C CB  . LEU A 334 ? 0.1689 0.1558 0.1088 -0.0319 0.0122  0.0309  334 LEU A CB  
2843 C CG  . LEU A 334 ? 0.2011 0.1870 0.1569 -0.0334 0.0089  0.0245  334 LEU A CG  
2844 C CD1 . LEU A 334 ? 0.2041 0.1986 0.1645 -0.0290 0.0000  0.0208  334 LEU A CD1 
2845 C CD2 . LEU A 334 ? 0.2043 0.1961 0.1689 -0.0390 0.0118  0.0160  334 LEU A CD2 
2846 N N   . LYS A 335 ? 0.2340 0.2049 0.1373 -0.0289 0.0268  0.0539  335 LYS A N   
2847 C CA  . LYS A 335 ? 0.2772 0.2500 0.1605 -0.0259 0.0306  0.0622  335 LYS A CA  
2848 C C   . LYS A 335 ? 0.3059 0.2708 0.1844 -0.0351 0.0438  0.0639  335 LYS A C   
2849 O O   . LYS A 335 ? 0.2920 0.2669 0.1597 -0.0367 0.0472  0.0634  335 LYS A O   
2850 C CB  . LYS A 335 ? 0.2984 0.2612 0.1686 -0.0149 0.0296  0.0770  335 LYS A CB  
2851 C CG  . LYS A 335 ? 0.4880 0.4553 0.3347 -0.0085 0.0315  0.0877  335 LYS A CG  
2852 C CD  . LYS A 335 ? 0.5341 0.5048 0.3719 0.0065  0.0237  0.0990  335 LYS A CD  
2853 C CE  . LYS A 335 ? 0.6877 0.6588 0.5048 0.0127  0.0250  0.1086  335 LYS A CE  
2854 N NZ  . LYS A 335 ? 0.7579 0.7017 0.5704 0.0104  0.0366  0.1185  335 LYS A NZ  
2855 N N   . LYS A 336 ? 0.2578 0.2062 0.1444 -0.0424 0.0518  0.0648  336 LYS A N   
2856 C CA  . LYS A 336 ? 0.2806 0.2235 0.1651 -0.0534 0.0650  0.0655  336 LYS A CA  
2857 C C   . LYS A 336 ? 0.2589 0.2239 0.1554 -0.0608 0.0650  0.0522  336 LYS A C   
2858 O O   . LYS A 336 ? 0.3051 0.2778 0.1961 -0.0650 0.0726  0.0522  336 LYS A O   
2859 C CB  . LYS A 336 ? 0.3564 0.2833 0.2544 -0.0579 0.0695  0.0652  336 LYS A CB  
2860 C CG  . LYS A 336 ? 0.4858 0.3924 0.3735 -0.0503 0.0718  0.0781  336 LYS A CG  
2861 C CD  . LYS A 336 ? 0.6564 0.5463 0.5537 -0.0574 0.0784  0.0757  336 LYS A CD  
2862 C CE  . LYS A 336 ? 0.7666 0.6659 0.6732 -0.0707 0.0854  0.0671  336 LYS A CE  
2863 N NZ  . LYS A 336 ? 0.7799 0.6695 0.6990 -0.0792 0.0886  0.0589  336 LYS A NZ  
2864 N N   . ILE A 337 ? 0.2609 0.2373 0.1749 -0.0602 0.0563  0.0411  337 ILE A N   
2865 C CA  . ILE A 337 ? 0.2784 0.2760 0.2034 -0.0629 0.0553  0.0293  337 ILE A CA  
2866 C C   . ILE A 337 ? 0.2563 0.2654 0.1684 -0.0572 0.0535  0.0285  337 ILE A C   
2867 O O   . ILE A 337 ? 0.3187 0.3396 0.2289 -0.0607 0.0605  0.0249  337 ILE A O   
2868 C CB  . ILE A 337 ? 0.2328 0.2373 0.1751 -0.0600 0.0458  0.0202  337 ILE A CB  
2869 C CG1 . ILE A 337 ? 0.1943 0.1897 0.1478 -0.0662 0.0476  0.0196  337 ILE A CG1 
2870 C CG2 . ILE A 337 ? 0.2599 0.2842 0.2118 -0.0596 0.0452  0.0097  337 ILE A CG2 
2871 C CD1 . ILE A 337 ? 0.2404 0.2390 0.2066 -0.0618 0.0381  0.0136  337 ILE A CD1 
2872 N N   . HIS A 338 ? 0.2279 0.2356 0.1313 -0.0486 0.0444  0.0309  338 HIS A N   
2873 C CA  . HIS A 338 ? 0.2366 0.2557 0.1257 -0.0437 0.0415  0.0288  338 HIS A CA  
2874 C C   . HIS A 338 ? 0.3048 0.3241 0.1757 -0.0460 0.0519  0.0365  338 HIS A C   
2875 O O   . HIS A 338 ? 0.3291 0.3616 0.1934 -0.0464 0.0550  0.0304  338 HIS A O   
2876 C CB  . HIS A 338 ? 0.2942 0.3124 0.1765 -0.0358 0.0306  0.0323  338 HIS A CB  
2877 C CG  . HIS A 338 ? 0.3879 0.4195 0.2540 -0.0315 0.0263  0.0296  338 HIS A CG  
2878 N ND1 . HIS A 338 ? 0.3645 0.4081 0.2337 -0.0323 0.0228  0.0155  338 HIS A ND1 
2879 C CD2 . HIS A 338 ? 0.4325 0.4675 0.2779 -0.0260 0.0248  0.0389  338 HIS A CD2 
2880 C CE1 . HIS A 338 ? 0.3654 0.4199 0.2169 -0.0292 0.0193  0.0144  338 HIS A CE1 
2881 N NE2 . HIS A 338 ? 0.4445 0.4961 0.2811 -0.0249 0.0199  0.0289  338 HIS A NE2 
2882 N N   . GLU A 339 ? 0.2770 0.2801 0.1386 -0.0473 0.0587  0.0500  339 GLU A N   
2883 C CA  . GLU A 339 ? 0.2977 0.2978 0.1392 -0.0492 0.0697  0.0597  339 GLU A CA  
2884 C C   . GLU A 339 ? 0.3813 0.3842 0.2357 -0.0583 0.0813  0.0554  339 GLU A C   
2885 O O   . GLU A 339 ? 0.4023 0.4078 0.2474 -0.0580 0.0893  0.0602  339 GLU A O   
2886 C CB  . GLU A 339 ? 0.3497 0.3296 0.1798 -0.0424 0.0715  0.0765  339 GLU A CB  
2887 C CG  . GLU A 339 ? 0.4750 0.4578 0.2909 -0.0307 0.0595  0.0822  339 GLU A CG  
2888 C CD  . GLU A 339 ? 0.6844 0.6486 0.4967 -0.0239 0.0587  0.0966  339 GLU A CD  
2889 O OE1 . GLU A 339 ? 0.7387 0.7061 0.5399 -0.0127 0.0492  0.1015  339 GLU A OE1 
2890 O OE2 . GLU A 339 ? 0.7059 0.6531 0.5295 -0.0294 0.0663  0.1000  339 GLU A OE2 
2891 N N   . SER A 340 ? 0.4048 0.4108 0.2811 -0.0657 0.0816  0.0463  340 SER A N   
2892 C CA  . SER A 340 ? 0.3717 0.3828 0.2630 -0.0743 0.0906  0.0423  340 SER A CA  
2893 C C   . SER A 340 ? 0.3515 0.3871 0.2498 -0.0757 0.0931  0.0313  340 SER A C   
2894 O O   . SER A 340 ? 0.3715 0.4154 0.2807 -0.0820 0.1007  0.0285  340 SER A O   
2895 C CB  . SER A 340 ? 0.4035 0.4097 0.3154 -0.0807 0.0885  0.0371  340 SER A CB  
2896 O OG  . SER A 340 ? 0.3594 0.3830 0.2853 -0.0807 0.0822  0.0252  340 SER A OG  
2897 N N   . VAL A 341 ? 0.3269 0.3747 0.2200 -0.0696 0.0868  0.0241  341 VAL A N   
2898 C CA  . VAL A 341 ? 0.3406 0.4098 0.2401 -0.0681 0.0895  0.0130  341 VAL A CA  
2899 C C   . VAL A 341 ? 0.3243 0.3972 0.2036 -0.0602 0.0862  0.0111  341 VAL A C   
2900 O O   . VAL A 341 ? 0.3607 0.4251 0.2265 -0.0559 0.0782  0.0150  341 VAL A O   
2901 C CB  . VAL A 341 ? 0.3062 0.3889 0.2274 -0.0677 0.0850  0.0011  341 VAL A CB  
2902 C CG1 . VAL A 341 ? 0.3289 0.4127 0.2705 -0.0754 0.0871  0.0011  341 VAL A CG1 
2903 C CG2 . VAL A 341 ? 0.2683 0.3400 0.1899 -0.0597 0.0712  -0.0006 341 VAL A CG2 
2904 N N   . ASP A 342 ? 0.3221 0.4086 0.1996 -0.0580 0.0918  0.0048  342 ASP A N   
2905 C CA  . ASP A 342 ? 0.3396 0.4300 0.1986 -0.0508 0.0886  0.0002  342 ASP A CA  
2906 C C   . ASP A 342 ? 0.4333 0.5328 0.3005 -0.0458 0.0833  -0.0153 342 ASP A C   
2907 O O   . ASP A 342 ? 0.4782 0.5797 0.3321 -0.0405 0.0804  -0.0223 342 ASP A O   
2908 C CB  . ASP A 342 ? 0.4668 0.5629 0.3147 -0.0503 0.0986  0.0027  342 ASP A CB  
2909 C CG  . ASP A 342 ? 0.5786 0.6885 0.4456 -0.0537 0.1078  -0.0031 342 ASP A CG  
2910 O OD1 . ASP A 342 ? 0.6372 0.7510 0.5261 -0.0577 0.1071  -0.0057 342 ASP A OD1 
2911 O OD2 . ASP A 342 ? 0.6794 0.7979 0.5397 -0.0519 0.1155  -0.0051 342 ASP A OD2 
2912 N N   . PHE A 343 ? 0.2894 0.3926 0.1778 -0.0466 0.0820  -0.0210 343 PHE A N   
2913 C CA  . PHE A 343 ? 0.2730 0.3760 0.1706 -0.0391 0.0752  -0.0331 343 PHE A CA  
2914 C C   . PHE A 343 ? 0.2681 0.3559 0.1707 -0.0382 0.0628  -0.0301 343 PHE A C   
2915 O O   . PHE A 343 ? 0.2597 0.3389 0.1587 -0.0421 0.0597  -0.0194 343 PHE A O   
2916 C CB  . PHE A 343 ? 0.2740 0.3906 0.1932 -0.0363 0.0808  -0.0403 343 PHE A CB  
2917 C CG  . PHE A 343 ? 0.2475 0.3674 0.1863 -0.0415 0.0804  -0.0345 343 PHE A CG  
2918 C CD1 . PHE A 343 ? 0.2309 0.3430 0.1832 -0.0384 0.0711  -0.0351 343 PHE A CD1 
2919 C CD2 . PHE A 343 ? 0.2551 0.3858 0.1988 -0.0500 0.0895  -0.0292 343 PHE A CD2 
2920 C CE1 . PHE A 343 ? 0.2554 0.3725 0.2243 -0.0437 0.0705  -0.0312 343 PHE A CE1 
2921 C CE2 . PHE A 343 ? 0.2710 0.4055 0.2327 -0.0563 0.0888  -0.0261 343 PHE A CE2 
2922 C CZ  . PHE A 343 ? 0.2895 0.4192 0.2630 -0.0534 0.0797  -0.0278 343 PHE A CZ  
2923 N N   . GLN A 344 ? 0.2565 0.3398 0.1668 -0.0326 0.0568  -0.0396 344 GLN A N   
2924 C CA  . GLN A 344 ? 0.2188 0.2891 0.1343 -0.0321 0.0461  -0.0377 344 GLN A CA  
2925 C C   . GLN A 344 ? 0.2189 0.2885 0.1556 -0.0315 0.0452  -0.0357 344 GLN A C   
2926 O O   . GLN A 344 ? 0.2044 0.2775 0.1524 -0.0260 0.0470  -0.0428 344 GLN A O   
2927 C CB  . GLN A 344 ? 0.2123 0.2761 0.1229 -0.0284 0.0411  -0.0489 344 GLN A CB  
2928 C CG  . GLN A 344 ? 0.2328 0.3010 0.1213 -0.0297 0.0412  -0.0529 344 GLN A CG  
2929 C CD  . GLN A 344 ? 0.3394 0.4012 0.2222 -0.0293 0.0358  -0.0656 344 GLN A CD  
2930 O OE1 . GLN A 344 ? 0.3359 0.3989 0.2085 -0.0324 0.0280  -0.0652 344 GLN A OE1 
2931 N NE2 . GLN A 344 ? 0.3001 0.3555 0.1894 -0.0254 0.0404  -0.0772 344 GLN A NE2 
2932 N N   . PRO A 345 ? 0.1796 0.2449 0.1209 -0.0363 0.0429  -0.0264 345 PRO A N   
2933 C CA  . PRO A 345 ? 0.1854 0.2524 0.1452 -0.0367 0.0418  -0.0253 345 PRO A CA  
2934 C C   . PRO A 345 ? 0.1530 0.2099 0.1199 -0.0319 0.0334  -0.0280 345 PRO A C   
2935 O O   . PRO A 345 ? 0.1923 0.2388 0.1513 -0.0314 0.0276  -0.0278 345 PRO A O   
2936 C CB  . PRO A 345 ? 0.2262 0.2879 0.1843 -0.0445 0.0431  -0.0154 345 PRO A CB  
2937 C CG  . PRO A 345 ? 0.1986 0.2495 0.1392 -0.0439 0.0394  -0.0098 345 PRO A CG  
2938 C CD  . PRO A 345 ? 0.2310 0.2891 0.1594 -0.0405 0.0415  -0.0162 345 PRO A CD  
2939 N N   . VAL A 346 ? 0.1426 0.2047 0.1244 -0.0283 0.0332  -0.0302 346 VAL A N   
2940 C CA  . VAL A 346 ? 0.1339 0.1860 0.1225 -0.0239 0.0267  -0.0308 346 VAL A CA  
2941 C C   . VAL A 346 ? 0.1224 0.1753 0.1196 -0.0282 0.0239  -0.0249 346 VAL A C   
2942 O O   . VAL A 346 ? 0.1595 0.2264 0.1663 -0.0298 0.0269  -0.0250 346 VAL A O   
2943 C CB  . VAL A 346 ? 0.1639 0.2188 0.1600 -0.0142 0.0286  -0.0368 346 VAL A CB  
2944 C CG1 . VAL A 346 ? 0.1751 0.2156 0.1750 -0.0099 0.0232  -0.0360 346 VAL A CG1 
2945 C CG2 . VAL A 346 ? 0.2107 0.2639 0.1975 -0.0105 0.0335  -0.0443 346 VAL A CG2 
2946 N N   . VAL A 347 ? 0.1361 0.1761 0.1305 -0.0302 0.0184  -0.0209 347 VAL A N   
2947 C CA  . VAL A 347 ? 0.1221 0.1598 0.1215 -0.0349 0.0166  -0.0158 347 VAL A CA  
2948 C C   . VAL A 347 ? 0.1144 0.1463 0.1204 -0.0305 0.0113  -0.0160 347 VAL A C   
2949 O O   . VAL A 347 ? 0.1401 0.1609 0.1425 -0.0292 0.0074  -0.0151 347 VAL A O   
2950 C CB  . VAL A 347 ? 0.1350 0.1623 0.1245 -0.0394 0.0161  -0.0095 347 VAL A CB  
2951 C CG1 . VAL A 347 ? 0.1456 0.1675 0.1395 -0.0440 0.0163  -0.0054 347 VAL A CG1 
2952 C CG2 . VAL A 347 ? 0.2045 0.2357 0.1840 -0.0427 0.0221  -0.0078 347 VAL A CG2 
2953 N N   . PHE A 348 ? 0.1357 0.1776 0.1514 -0.0285 0.0114  -0.0172 348 PHE A N   
2954 C CA  . PHE A 348 ? 0.1340 0.1717 0.1543 -0.0235 0.0072  -0.0163 348 PHE A CA  
2955 C C   . PHE A 348 ? 0.1414 0.1757 0.1629 -0.0293 0.0050  -0.0131 348 PHE A C   
2956 O O   . PHE A 348 ? 0.1704 0.2138 0.1954 -0.0353 0.0071  -0.0139 348 PHE A O   
2957 C CB  . PHE A 348 ? 0.1378 0.1901 0.1661 -0.0159 0.0078  -0.0184 348 PHE A CB  
2958 C CG  . PHE A 348 ? 0.1424 0.1872 0.1688 -0.0058 0.0090  -0.0201 348 PHE A CG  
2959 C CD1 . PHE A 348 ? 0.1324 0.1756 0.1543 -0.0046 0.0130  -0.0242 348 PHE A CD1 
2960 C CD2 . PHE A 348 ? 0.1399 0.1773 0.1674 0.0024  0.0072  -0.0175 348 PHE A CD2 
2961 C CE1 . PHE A 348 ? 0.1907 0.2234 0.2099 0.0041  0.0156  -0.0272 348 PHE A CE1 
2962 C CE2 . PHE A 348 ? 0.1745 0.1998 0.1991 0.0114  0.0102  -0.0189 348 PHE A CE2 
2963 C CZ  . PHE A 348 ? 0.1508 0.1728 0.1714 0.0120  0.0145  -0.0245 348 PHE A CZ  
2964 N N   . VAL A 349 ? 0.1211 0.1424 0.1401 -0.0281 0.0018  -0.0105 349 VAL A N   
2965 C CA  . VAL A 349 ? 0.1213 0.1377 0.1410 -0.0316 0.0003  -0.0080 349 VAL A CA  
2966 C C   . VAL A 349 ? 0.1265 0.1435 0.1494 -0.0261 -0.0023 -0.0076 349 VAL A C   
2967 O O   . VAL A 349 ? 0.1301 0.1377 0.1514 -0.0223 -0.0035 -0.0062 349 VAL A O   
2968 C CB  . VAL A 349 ? 0.1379 0.1418 0.1524 -0.0335 -0.0006 -0.0046 349 VAL A CB  
2969 C CG1 . VAL A 349 ? 0.2059 0.2038 0.2211 -0.0354 -0.0010 -0.0024 349 VAL A CG1 
2970 C CG2 . VAL A 349 ? 0.1893 0.1923 0.1976 -0.0369 0.0022  -0.0031 349 VAL A CG2 
2971 N N   . VAL A 350 ? 0.1112 0.1401 0.1380 -0.0260 -0.0029 -0.0090 350 VAL A N   
2972 C CA  . VAL A 350 ? 0.1036 0.1362 0.1315 -0.0187 -0.0052 -0.0074 350 VAL A CA  
2973 C C   . VAL A 350 ? 0.1054 0.1421 0.1330 -0.0226 -0.0066 -0.0080 350 VAL A C   
2974 O O   . VAL A 350 ? 0.0966 0.1453 0.1269 -0.0289 -0.0061 -0.0123 350 VAL A O   
2975 C CB  . VAL A 350 ? 0.0926 0.1419 0.1248 -0.0113 -0.0052 -0.0087 350 VAL A CB  
2976 C CG1 . VAL A 350 ? 0.1385 0.1886 0.1692 -0.0009 -0.0072 -0.0045 350 VAL A CG1 
2977 C CG2 . VAL A 350 ? 0.0875 0.1334 0.1196 -0.0082 -0.0023 -0.0101 350 VAL A CG2 
2978 N N   . LEU A 351 ? 0.1132 0.1403 0.1374 -0.0198 -0.0076 -0.0047 351 LEU A N   
2979 C CA  . LEU A 351 ? 0.1293 0.1600 0.1515 -0.0229 -0.0084 -0.0062 351 LEU A CA  
2980 C C   . LEU A 351 ? 0.1130 0.1362 0.1311 -0.0167 -0.0088 -0.0012 351 LEU A C   
2981 O O   . LEU A 351 ? 0.1197 0.1324 0.1372 -0.0121 -0.0078 0.0030  351 LEU A O   
2982 C CB  . LEU A 351 ? 0.0997 0.1205 0.1208 -0.0315 -0.0059 -0.0086 351 LEU A CB  
2983 C CG  . LEU A 351 ? 0.1210 0.1250 0.1407 -0.0307 -0.0047 -0.0044 351 LEU A CG  
2984 C CD1 . LEU A 351 ? 0.1425 0.1371 0.1600 -0.0345 -0.0022 -0.0051 351 LEU A CD1 
2985 C CD2 . LEU A 351 ? 0.1970 0.1977 0.2175 -0.0317 -0.0040 -0.0036 351 LEU A CD2 
2986 N N   . ASN A 352 ? 0.1286 0.1566 0.1429 -0.0176 -0.0095 -0.0022 352 ASN A N   
2987 C CA  . ASN A 352 ? 0.1539 0.1742 0.1630 -0.0129 -0.0084 0.0029  352 ASN A CA  
2988 C C   . ASN A 352 ? 0.1444 0.1477 0.1552 -0.0158 -0.0055 0.0051  352 ASN A C   
2989 O O   . ASN A 352 ? 0.1375 0.1365 0.1509 -0.0213 -0.0046 0.0022  352 ASN A O   
2990 C CB  . ASN A 352 ? 0.1785 0.2073 0.1819 -0.0147 -0.0090 -0.0001 352 ASN A CB  
2991 C CG  . ASN A 352 ? 0.2424 0.2946 0.2446 -0.0129 -0.0132 -0.0037 352 ASN A CG  
2992 O OD1 . ASN A 352 ? 0.1838 0.2462 0.1873 -0.0054 -0.0155 -0.0004 352 ASN A OD1 
2993 N ND2 . ASN A 352 ? 0.3389 0.4005 0.3383 -0.0196 -0.0138 -0.0113 352 ASN A ND2 
2994 N N   . GLY A 353 ? 0.1314 0.1257 0.1410 -0.0118 -0.0035 0.0105  353 GLY A N   
2995 C CA  . GLY A 353 ? 0.1501 0.1335 0.1634 -0.0152 -0.0011 0.0117  353 GLY A CA  
2996 C C   . GLY A 353 ? 0.1368 0.1179 0.1492 -0.0167 0.0018  0.0132  353 GLY A C   
2997 O O   . GLY A 353 ? 0.1484 0.1248 0.1659 -0.0195 0.0037  0.0138  353 GLY A O   
2998 N N   . GLU A 354 ? 0.1268 0.1135 0.1331 -0.0150 0.0023  0.0129  354 GLU A N   
2999 C CA  . GLU A 354 ? 0.1242 0.1087 0.1283 -0.0153 0.0064  0.0146  354 GLU A CA  
3000 C C   . GLU A 354 ? 0.1573 0.1469 0.1575 -0.0168 0.0071  0.0094  354 GLU A C   
3001 O O   . GLU A 354 ? 0.1609 0.1490 0.1595 -0.0166 0.0113  0.0099  354 GLU A O   
3002 C CB  . GLU A 354 ? 0.1399 0.1221 0.1368 -0.0107 0.0094  0.0215  354 GLU A CB  
3003 C CG  . GLU A 354 ? 0.1288 0.1209 0.1147 -0.0055 0.0075  0.0224  354 GLU A CG  
3004 C CD  . GLU A 354 ? 0.1720 0.1709 0.1568 -0.0006 0.0026  0.0229  354 GLU A CD  
3005 O OE1 . GLU A 354 ? 0.1475 0.1467 0.1250 0.0074  0.0031  0.0299  354 GLU A OE1 
3006 O OE2 . GLU A 354 ? 0.1637 0.1679 0.1548 -0.0039 -0.0010 0.0170  354 GLU A OE2 
3007 N N   . ASN A 355 ? 0.1144 0.1092 0.1132 -0.0191 0.0041  0.0036  355 ASN A N   
3008 C CA  . ASN A 355 ? 0.1308 0.1290 0.1238 -0.0218 0.0055  -0.0032 355 ASN A CA  
3009 C C   . ASN A 355 ? 0.1484 0.1370 0.1452 -0.0260 0.0083  -0.0080 355 ASN A C   
3010 O O   . ASN A 355 ? 0.1558 0.1412 0.1479 -0.0276 0.0121  -0.0134 355 ASN A O   
3011 C CB  . ASN A 355 ? 0.1597 0.1720 0.1479 -0.0231 0.0011  -0.0078 355 ASN A CB  
3012 C CG  . ASN A 355 ? 0.1304 0.1529 0.1116 -0.0161 -0.0011 -0.0020 355 ASN A CG  
3013 O OD1 . ASN A 355 ? 0.1457 0.1643 0.1212 -0.0126 0.0024  0.0027  355 ASN A OD1 
3014 N ND2 . ASN A 355 ? 0.1546 0.1905 0.1360 -0.0130 -0.0060 -0.0014 355 ASN A ND2 
3015 N N   . CYS A 356 ? 0.1179 0.1009 0.1215 -0.0270 0.0072  -0.0062 356 CYS A N   
3016 C CA  . CYS A 356 ? 0.1182 0.0905 0.1230 -0.0295 0.0105  -0.0092 356 CYS A CA  
3017 C C   . CYS A 356 ? 0.1184 0.0836 0.1270 -0.0247 0.0142  -0.0055 356 CYS A C   
3018 O O   . CYS A 356 ? 0.1330 0.0879 0.1399 -0.0239 0.0189  -0.0081 356 CYS A O   
3019 C CB  . CYS A 356 ? 0.1477 0.1179 0.1560 -0.0320 0.0084  -0.0081 356 CYS A CB  
3020 S SG  . CYS A 356 ? 0.1453 0.1195 0.1597 -0.0285 0.0042  -0.0012 356 CYS A SG  
3021 N N   . TRP A 357 ? 0.1383 0.1090 0.1521 -0.0213 0.0130  -0.0001 357 TRP A N   
3022 C CA  . TRP A 357 ? 0.1731 0.1431 0.1941 -0.0172 0.0153  0.0034  357 TRP A CA  
3023 C C   . TRP A 357 ? 0.1591 0.1268 0.1784 -0.0138 0.0214  0.0012  357 TRP A C   
3024 O O   . TRP A 357 ? 0.1296 0.0947 0.1538 -0.0087 0.0243  0.0027  357 TRP A O   
3025 C CB  . TRP A 357 ? 0.1600 0.1385 0.1881 -0.0173 0.0131  0.0079  357 TRP A CB  
3026 C CG  . TRP A 357 ? 0.1019 0.0808 0.1296 -0.0202 0.0083  0.0086  357 TRP A CG  
3027 C CD1 . TRP A 357 ? 0.1460 0.1261 0.1715 -0.0216 0.0072  0.0099  357 TRP A CD1 
3028 C CD2 . TRP A 357 ? 0.1457 0.1226 0.1740 -0.0210 0.0051  0.0084  357 TRP A CD2 
3029 N NE1 . TRP A 357 ? 0.1371 0.1164 0.1627 -0.0229 0.0034  0.0095  357 TRP A NE1 
3030 C CE2 . TRP A 357 ? 0.1425 0.1209 0.1697 -0.0232 0.0020  0.0083  357 TRP A CE2 
3031 C CE3 . TRP A 357 ? 0.1959 0.1686 0.2242 -0.0192 0.0053  0.0090  357 TRP A CE3 
3032 C CZ2 . TRP A 357 ? 0.1496 0.1278 0.1763 -0.0245 -0.0008 0.0077  357 TRP A CZ2 
3033 C CZ3 . TRP A 357 ? 0.1980 0.1697 0.2246 -0.0207 0.0025  0.0096  357 TRP A CZ3 
3034 C CH2 . TRP A 357 ? 0.1462 0.1216 0.1723 -0.0238 -0.0006 0.0084  357 TRP A CH2 
3035 N N   . GLU A 358 ? 0.1297 0.0993 0.1416 -0.0153 0.0237  -0.0022 358 GLU A N   
3036 C CA  . GLU A 358 ? 0.1443 0.1120 0.1532 -0.0120 0.0305  -0.0054 358 GLU A CA  
3037 C C   . GLU A 358 ? 0.1519 0.1056 0.1573 -0.0108 0.0348  -0.0109 358 GLU A C   
3038 O O   . GLU A 358 ? 0.1573 0.1067 0.1620 -0.0059 0.0416  -0.0132 358 GLU A O   
3039 C CB  . GLU A 358 ? 0.1578 0.1310 0.1562 -0.0142 0.0317  -0.0084 358 GLU A CB  
3040 C CG  . GLU A 358 ? 0.1737 0.1468 0.1624 -0.0194 0.0281  -0.0147 358 GLU A CG  
3041 C CD  . GLU A 358 ? 0.1688 0.1537 0.1486 -0.0196 0.0257  -0.0134 358 GLU A CD  
3042 O OE1 . GLU A 358 ? 0.2507 0.2395 0.2194 -0.0209 0.0276  -0.0200 358 GLU A OE1 
3043 O OE2 . GLU A 358 ? 0.1990 0.1885 0.1818 -0.0179 0.0224  -0.0057 358 GLU A OE2 
3044 N N   . TYR A 359 ? 0.1793 0.1246 0.1821 -0.0150 0.0324  -0.0130 359 TYR A N   
3045 C CA  . TYR A 359 ? 0.1899 0.1170 0.1884 -0.0149 0.0382  -0.0175 359 TYR A CA  
3046 C C   . TYR A 359 ? 0.2084 0.1277 0.2132 -0.0083 0.0387  -0.0100 359 TYR A C   
3047 O O   . TYR A 359 ? 0.2245 0.1251 0.2252 -0.0056 0.0451  -0.0113 359 TYR A O   
3048 C CB  . TYR A 359 ? 0.1667 0.0887 0.1579 -0.0253 0.0370  -0.0250 359 TYR A CB  
3049 C CG  . TYR A 359 ? 0.1857 0.1201 0.1698 -0.0310 0.0351  -0.0326 359 TYR A CG  
3050 C CD1 . TYR A 359 ? 0.3047 0.2335 0.2799 -0.0327 0.0412  -0.0421 359 TYR A CD1 
3051 C CD2 . TYR A 359 ? 0.2737 0.2257 0.2588 -0.0334 0.0275  -0.0302 359 TYR A CD2 
3052 C CE1 . TYR A 359 ? 0.2928 0.2361 0.2599 -0.0372 0.0387  -0.0488 359 TYR A CE1 
3053 C CE2 . TYR A 359 ? 0.2820 0.2477 0.2595 -0.0363 0.0252  -0.0355 359 TYR A CE2 
3054 C CZ  . TYR A 359 ? 0.3730 0.3357 0.3412 -0.0384 0.0303  -0.0447 359 TYR A CZ  
3055 O OH  . TYR A 359 ? 0.4609 0.4403 0.4197 -0.0407 0.0273  -0.0498 359 TYR A OH  
3056 N N   . TYR A 360 ? 0.1787 0.1113 0.1923 -0.0054 0.0326  -0.0023 360 TYR A N   
3057 C CA  . TYR A 360 ? 0.1783 0.1094 0.1975 0.0023  0.0320  0.0051  360 TYR A CA  
3058 C C   . TYR A 360 ? 0.1571 0.0962 0.1841 0.0124  0.0354  0.0081  360 TYR A C   
3059 O O   . TYR A 360 ? 0.1634 0.1146 0.1944 0.0116  0.0361  0.0062  360 TYR A O   
3060 C CB  . TYR A 360 ? 0.1514 0.0963 0.1763 0.0000  0.0238  0.0101  360 TYR A CB  
3061 C CG  . TYR A 360 ? 0.2074 0.1477 0.2272 -0.0069 0.0203  0.0096  360 TYR A CG  
3062 C CD1 . TYR A 360 ? 0.1863 0.1273 0.2018 -0.0153 0.0191  0.0039  360 TYR A CD1 
3063 C CD2 . TYR A 360 ? 0.1578 0.0969 0.1774 -0.0042 0.0178  0.0153  360 TYR A CD2 
3064 C CE1 . TYR A 360 ? 0.1499 0.0905 0.1628 -0.0211 0.0163  0.0032  360 TYR A CE1 
3065 C CE2 . TYR A 360 ? 0.2010 0.1380 0.2163 -0.0106 0.0155  0.0148  360 TYR A CE2 
3066 C CZ  . TYR A 360 ? 0.1401 0.0780 0.1530 -0.0190 0.0151  0.0086  360 TYR A CZ  
3067 O OH  . TYR A 360 ? 0.1904 0.1290 0.2006 -0.0247 0.0134  0.0079  360 TYR A OH  
3068 N N   . GLU A 361 ? 0.2386 0.1722 0.2678 0.0226  0.0377  0.0137  361 GLU A N   
3069 C CA  . GLU A 361 ? 0.2498 0.1976 0.2895 0.0340  0.0396  0.0176  361 GLU A CA  
3070 C C   . GLU A 361 ? 0.1848 0.1604 0.2368 0.0304  0.0323  0.0197  361 GLU A C   
3071 O O   . GLU A 361 ? 0.1824 0.1647 0.2354 0.0247  0.0250  0.0217  361 GLU A O   
3072 C CB  . GLU A 361 ? 0.3142 0.2549 0.3541 0.0474  0.0415  0.0254  361 GLU A CB  
3073 C CG  . GLU A 361 ? 0.5180 0.4259 0.5453 0.0513  0.0514  0.0236  361 GLU A CG  
3074 C CD  . GLU A 361 ? 0.6822 0.5820 0.7079 0.0541  0.0607  0.0161  361 GLU A CD  
3075 O OE1 . GLU A 361 ? 0.7009 0.6193 0.7372 0.0629  0.0620  0.0175  361 GLU A OE1 
3076 O OE2 . GLU A 361 ? 0.7311 0.6076 0.7449 0.0468  0.0671  0.0078  361 GLU A OE2 
3077 N N   . GLU A 362 ? 0.1940 0.1849 0.2550 0.0327  0.0355  0.0184  362 GLU A N   
3078 C CA  . GLU A 362 ? 0.1871 0.2036 0.2609 0.0278  0.0309  0.0195  362 GLU A CA  
3079 C C   . GLU A 362 ? 0.1839 0.1979 0.2529 0.0148  0.0257  0.0174  362 GLU A C   
3080 O O   . GLU A 362 ? 0.1366 0.1632 0.2121 0.0100  0.0197  0.0188  362 GLU A O   
3081 C CB  . GLU A 362 ? 0.1757 0.2126 0.2616 0.0350  0.0256  0.0248  362 GLU A CB  
3082 C CG  . GLU A 362 ? 0.2770 0.3154 0.3667 0.0514  0.0306  0.0287  362 GLU A CG  
3083 C CD  . GLU A 362 ? 0.4829 0.5531 0.5887 0.0596  0.0254  0.0336  362 GLU A CD  
3084 O OE1 . GLU A 362 ? 0.5441 0.6196 0.6546 0.0757  0.0290  0.0380  362 GLU A OE1 
3085 O OE2 . GLU A 362 ? 0.4947 0.5855 0.6084 0.0503  0.0179  0.0324  362 GLU A OE2 
3086 N N   . ASN A 363 ? 0.1329 0.1308 0.1898 0.0096  0.0282  0.0136  363 ASN A N   
3087 C CA  . ASN A 363 ? 0.1140 0.1105 0.1660 -0.0002 0.0246  0.0122  363 ASN A CA  
3088 C C   . ASN A 363 ? 0.1486 0.1437 0.2000 -0.0037 0.0175  0.0137  363 ASN A C   
3089 O O   . ASN A 363 ? 0.1578 0.1570 0.2104 -0.0099 0.0142  0.0137  363 ASN A O   
3090 C CB  . ASN A 363 ? 0.1127 0.1224 0.1718 -0.0044 0.0265  0.0131  363 ASN A CB  
3091 C CG  . ASN A 363 ? 0.1712 0.1748 0.2221 -0.0115 0.0255  0.0128  363 ASN A CG  
3092 O OD1 . ASN A 363 ? 0.1818 0.1750 0.2212 -0.0119 0.0252  0.0107  363 ASN A OD1 
3093 N ND2 . ASN A 363 ? 0.1103 0.1205 0.1671 -0.0170 0.0254  0.0148  363 ASN A ND2 
3094 N N   . GLY A 364 ? 0.1571 0.1450 0.2057 0.0008  0.0162  0.0152  364 GLY A N   
3095 C CA  . GLY A 364 ? 0.1360 0.1229 0.1823 -0.0018 0.0104  0.0169  364 GLY A CA  
3096 C C   . GLY A 364 ? 0.1342 0.1383 0.1896 -0.0017 0.0050  0.0192  364 GLY A C   
3097 O O   . GLY A 364 ? 0.1391 0.1437 0.1916 -0.0045 0.0003  0.0196  364 GLY A O   
3098 N N   . ILE A 365 ? 0.1488 0.1691 0.2153 0.0007  0.0058  0.0198  365 ILE A N   
3099 C CA  . ILE A 365 ? 0.0959 0.1364 0.1722 -0.0021 0.0004  0.0197  365 ILE A CA  
3100 C C   . ILE A 365 ? 0.1313 0.1788 0.2067 0.0057  -0.0045 0.0239  365 ILE A C   
3101 O O   . ILE A 365 ? 0.1275 0.1817 0.2014 0.0015  -0.0104 0.0228  365 ILE A O   
3102 C CB  . ILE A 365 ? 0.1114 0.1707 0.2016 -0.0032 0.0033  0.0185  365 ILE A CB  
3103 C CG1 . ILE A 365 ? 0.1394 0.1902 0.2276 -0.0124 0.0079  0.0156  365 ILE A CG1 
3104 C CG2 . ILE A 365 ? 0.1283 0.2134 0.2306 -0.0063 -0.0026 0.0171  365 ILE A CG2 
3105 C CD1 . ILE A 365 ? 0.1963 0.2586 0.2939 -0.0126 0.0143  0.0154  365 ILE A CD1 
3106 N N   . PRO A 366 ? 0.1345 0.1794 0.2090 0.0177  -0.0017 0.0289  366 PRO A N   
3107 C CA  . PRO A 366 ? 0.1255 0.1744 0.1958 0.0266  -0.0059 0.0351  366 PRO A CA  
3108 C C   . PRO A 366 ? 0.1211 0.1528 0.1773 0.0219  -0.0077 0.0356  366 PRO A C   
3109 O O   . PRO A 366 ? 0.1526 0.1945 0.2058 0.0230  -0.0135 0.0381  366 PRO A O   
3110 C CB  . PRO A 366 ? 0.1671 0.2064 0.2359 0.0409  0.0005  0.0408  366 PRO A CB  
3111 C CG  . PRO A 366 ? 0.1563 0.2021 0.2353 0.0402  0.0057  0.0366  366 PRO A CG  
3112 C CD  . PRO A 366 ? 0.1236 0.1624 0.2002 0.0250  0.0059  0.0297  366 PRO A CD  
3113 N N   . PHE A 367 ? 0.1246 0.1334 0.1725 0.0163  -0.0028 0.0329  367 PHE A N   
3114 C CA  . PHE A 367 ? 0.1697 0.1653 0.2064 0.0109  -0.0035 0.0327  367 PHE A CA  
3115 C C   . PHE A 367 ? 0.1585 0.1664 0.1970 0.0024  -0.0097 0.0283  367 PHE A C   
3116 O O   . PHE A 367 ? 0.1575 0.1694 0.1903 0.0025  -0.0134 0.0302  367 PHE A O   
3117 C CB  . PHE A 367 ? 0.1684 0.1433 0.1985 0.0052  0.0024  0.0288  367 PHE A CB  
3118 C CG  . PHE A 367 ? 0.1963 0.1631 0.2182 -0.0017 0.0017  0.0273  367 PHE A CG  
3119 C CD1 . PHE A 367 ? 0.2312 0.1874 0.2440 0.0011  0.0039  0.0325  367 PHE A CD1 
3120 C CD2 . PHE A 367 ? 0.1796 0.1501 0.2027 -0.0101 -0.0004 0.0216  367 PHE A CD2 
3121 C CE1 . PHE A 367 ? 0.2062 0.1571 0.2121 -0.0057 0.0044  0.0311  367 PHE A CE1 
3122 C CE2 . PHE A 367 ? 0.1496 0.1159 0.1666 -0.0154 -0.0006 0.0200  367 PHE A CE2 
3123 C CZ  . PHE A 367 ? 0.1620 0.1195 0.1709 -0.0139 0.0019  0.0244  367 PHE A CZ  
3124 N N   . LEU A 368 ? 0.1406 0.1530 0.1857 -0.0048 -0.0098 0.0227  368 LEU A N   
3125 C CA  . LEU A 368 ? 0.1303 0.1482 0.1757 -0.0128 -0.0136 0.0179  368 LEU A CA  
3126 C C   . LEU A 368 ? 0.1433 0.1818 0.1943 -0.0131 -0.0194 0.0169  368 LEU A C   
3127 O O   . LEU A 368 ? 0.1440 0.1858 0.1902 -0.0170 -0.0230 0.0140  368 LEU A O   
3128 C CB  . LEU A 368 ? 0.1474 0.1615 0.1969 -0.0192 -0.0109 0.0136  368 LEU A CB  
3129 C CG  . LEU A 368 ? 0.1296 0.1278 0.1714 -0.0205 -0.0074 0.0129  368 LEU A CG  
3130 C CD1 . LEU A 368 ? 0.1457 0.1413 0.1896 -0.0243 -0.0049 0.0107  368 LEU A CD1 
3131 C CD2 . LEU A 368 ? 0.1127 0.1056 0.1470 -0.0226 -0.0091 0.0117  368 LEU A CD2 
3132 N N   . GLU A 369 ? 0.1324 0.1875 0.1937 -0.0090 -0.0204 0.0184  369 GLU A N   
3133 C CA  . GLU A 369 ? 0.1267 0.2072 0.1943 -0.0096 -0.0269 0.0165  369 GLU A CA  
3134 C C   . GLU A 369 ? 0.1429 0.2272 0.2002 -0.0020 -0.0314 0.0218  369 GLU A C   
3135 O O   . GLU A 369 ? 0.1747 0.2738 0.2298 -0.0058 -0.0374 0.0180  369 GLU A O   
3136 C CB  . GLU A 369 ? 0.1152 0.2176 0.1977 -0.0055 -0.0270 0.0175  369 GLU A CB  
3137 C CG  . GLU A 369 ? 0.1180 0.2206 0.2108 -0.0157 -0.0223 0.0117  369 GLU A CG  
3138 C CD  . GLU A 369 ? 0.1759 0.3056 0.2858 -0.0143 -0.0220 0.0110  369 GLU A CD  
3139 O OE1 . GLU A 369 ? 0.1906 0.3378 0.3050 -0.0024 -0.0249 0.0161  369 GLU A OE1 
3140 O OE2 . GLU A 369 ? 0.1816 0.3155 0.3006 -0.0248 -0.0182 0.0059  369 GLU A OE2 
3141 N N   . LYS A 370 ? 0.1411 0.2113 0.1905 0.0084  -0.0280 0.0303  370 LYS A N   
3142 C CA  . LYS A 370 ? 0.1647 0.2345 0.2016 0.0158  -0.0306 0.0371  370 LYS A CA  
3143 C C   . LYS A 370 ? 0.1811 0.2376 0.2063 0.0076  -0.0301 0.0337  370 LYS A C   
3144 O O   . LYS A 370 ? 0.1792 0.2459 0.1963 0.0079  -0.0347 0.0341  370 LYS A O   
3145 C CB  . LYS A 370 ? 0.2137 0.2656 0.2438 0.0282  -0.0246 0.0473  370 LYS A CB  
3146 C CG  . LYS A 370 ? 0.4028 0.4704 0.4427 0.0405  -0.0252 0.0524  370 LYS A CG  
3147 C CD  . LYS A 370 ? 0.5411 0.5913 0.5716 0.0558  -0.0195 0.0640  370 LYS A CD  
3148 C CE  . LYS A 370 ? 0.5844 0.6474 0.6276 0.0677  -0.0178 0.0669  370 LYS A CE  
3149 N NZ  . LYS A 370 ? 0.5307 0.6343 0.5850 0.0744  -0.0272 0.0683  370 LYS A NZ  
3150 N N   . LEU A 371 ? 0.1402 0.1764 0.1641 0.0010  -0.0246 0.0301  371 LEU A N   
3151 C CA  . LEU A 371 ? 0.1275 0.1533 0.1423 -0.0058 -0.0233 0.0267  371 LEU A CA  
3152 C C   . LEU A 371 ? 0.1870 0.2267 0.2033 -0.0129 -0.0285 0.0186  371 LEU A C   
3153 O O   . LEU A 371 ? 0.1663 0.2100 0.1730 -0.0137 -0.0306 0.0179  371 LEU A O   
3154 C CB  . LEU A 371 ? 0.1448 0.1532 0.1611 -0.0110 -0.0177 0.0235  371 LEU A CB  
3155 C CG  . LEU A 371 ? 0.1807 0.1822 0.1905 -0.0170 -0.0161 0.0196  371 LEU A CG  
3156 C CD1 . LEU A 371 ? 0.2155 0.2114 0.2136 -0.0145 -0.0139 0.0252  371 LEU A CD1 
3157 C CD2 . LEU A 371 ? 0.1728 0.1634 0.1856 -0.0208 -0.0119 0.0164  371 LEU A CD2 
3158 N N   . TYR A 372 ? 0.1424 0.1889 0.1699 -0.0186 -0.0295 0.0122  372 TYR A N   
3159 C CA  . TYR A 372 ? 0.1892 0.2437 0.2178 -0.0272 -0.0324 0.0029  372 TYR A CA  
3160 C C   . TYR A 372 ? 0.2176 0.2961 0.2451 -0.0264 -0.0395 0.0012  372 TYR A C   
3161 O O   . TYR A 372 ? 0.2034 0.2868 0.2240 -0.0314 -0.0420 -0.0054 372 TYR A O   
3162 C CB  . TYR A 372 ? 0.1531 0.2057 0.1933 -0.0340 -0.0299 -0.0025 372 TYR A CB  
3163 C CG  . TYR A 372 ? 0.1178 0.1494 0.1567 -0.0347 -0.0237 -0.0016 372 TYR A CG  
3164 C CD1 . TYR A 372 ? 0.1190 0.1376 0.1488 -0.0323 -0.0215 0.0003  372 TYR A CD1 
3165 C CD2 . TYR A 372 ? 0.1415 0.1687 0.1883 -0.0380 -0.0201 -0.0027 372 TYR A CD2 
3166 C CE1 . TYR A 372 ? 0.1282 0.1331 0.1577 -0.0326 -0.0170 0.0005  372 TYR A CE1 
3167 C CE2 . TYR A 372 ? 0.1320 0.1431 0.1762 -0.0374 -0.0154 -0.0013 372 TYR A CE2 
3168 C CZ  . TYR A 372 ? 0.0839 0.0854 0.1198 -0.0344 -0.0145 0.0001  372 TYR A CZ  
3169 O OH  . TYR A 372 ? 0.1261 0.1168 0.1601 -0.0333 -0.0109 0.0011  372 TYR A OH  
3170 N N   . SER A 373 ? 0.1592 0.2548 0.1933 -0.0194 -0.0428 0.0067  373 SER A N   
3171 C CA  . SER A 373 ? 0.1590 0.2828 0.1920 -0.0167 -0.0509 0.0061  373 SER A CA  
3172 C C   . SER A 373 ? 0.2300 0.3511 0.2450 -0.0104 -0.0525 0.0117  373 SER A C   
3173 O O   . SER A 373 ? 0.2067 0.3459 0.2150 -0.0129 -0.0585 0.0068  373 SER A O   
3174 C CB  . SER A 373 ? 0.2060 0.3496 0.2499 -0.0069 -0.0535 0.0129  373 SER A CB  
3175 O OG  . SER A 373 ? 0.3227 0.4979 0.3651 -0.0021 -0.0623 0.0135  373 SER A OG  
3176 N N   . THR A 374 ? 0.1563 0.2552 0.1626 -0.0031 -0.0467 0.0215  374 THR A N   
3177 C CA  . THR A 374 ? 0.2288 0.3221 0.2172 0.0022  -0.0461 0.0283  374 THR A CA  
3178 C C   . THR A 374 ? 0.2039 0.2898 0.1842 -0.0077 -0.0443 0.0195  374 THR A C   
3179 O O   . THR A 374 ? 0.2207 0.3171 0.1884 -0.0074 -0.0475 0.0185  374 THR A O   
3180 C CB  . THR A 374 ? 0.2197 0.2884 0.2023 0.0100  -0.0383 0.0400  374 THR A CB  
3181 O OG1 . THR A 374 ? 0.2209 0.2945 0.2107 0.0207  -0.0387 0.0477  374 THR A OG1 
3182 C CG2 . THR A 374 ? 0.2364 0.2985 0.2001 0.0150  -0.0361 0.0484  374 THR A CG2 
3183 N N   . LEU A 375 ? 0.2163 0.2852 0.2031 -0.0153 -0.0392 0.0131  375 LEU A N   
3184 C CA  . LEU A 375 ? 0.2114 0.2722 0.1917 -0.0224 -0.0363 0.0053  375 LEU A CA  
3185 C C   . LEU A 375 ? 0.2653 0.3424 0.2440 -0.0289 -0.0415 -0.0061 375 LEU A C   
3186 O O   . LEU A 375 ? 0.2632 0.3419 0.2298 -0.0308 -0.0412 -0.0104 375 LEU A O   
3187 C CB  . LEU A 375 ? 0.2057 0.2487 0.1945 -0.0271 -0.0306 0.0014  375 LEU A CB  
3188 C CG  . LEU A 375 ? 0.2311 0.2576 0.2188 -0.0239 -0.0245 0.0088  375 LEU A CG  
3189 C CD1 . LEU A 375 ? 0.2223 0.2381 0.2190 -0.0278 -0.0210 0.0043  375 LEU A CD1 
3190 C CD2 . LEU A 375 ? 0.2676 0.2893 0.2428 -0.0235 -0.0206 0.0114  375 LEU A CD2 
3191 N N   . GLU A 376 ? 0.2709 0.3607 0.2616 -0.0334 -0.0457 -0.0122 376 GLU A N   
3192 C CA  . GLU A 376 ? 0.2649 0.3684 0.2552 -0.0426 -0.0496 -0.0257 376 GLU A CA  
3193 C C   . GLU A 376 ? 0.2722 0.3997 0.2503 -0.0395 -0.0568 -0.0257 376 GLU A C   
3194 O O   . GLU A 376 ? 0.3716 0.5057 0.3449 -0.0462 -0.0581 -0.0372 376 GLU A O   
3195 C CB  . GLU A 376 ? 0.3248 0.4378 0.3318 -0.0501 -0.0514 -0.0324 376 GLU A CB  
3196 C CG  . GLU A 376 ? 0.3471 0.4868 0.3622 -0.0446 -0.0581 -0.0268 376 GLU A CG  
3197 C CD  . GLU A 376 ? 0.3691 0.5122 0.4013 -0.0512 -0.0562 -0.0326 376 GLU A CD  
3198 O OE1 . GLU A 376 ? 0.2947 0.4582 0.3364 -0.0462 -0.0598 -0.0283 376 GLU A OE1 
3199 O OE2 . GLU A 376 ? 0.3793 0.5039 0.4147 -0.0605 -0.0502 -0.0405 376 GLU A OE2 
3200 N N   . LYS A 377 ? 0.2241 0.3595 0.1964 -0.0277 -0.0594 -0.0120 377 LYS A N   
3201 C CA  . LYS A 377 ? 0.2640 0.4221 0.2227 -0.0218 -0.0659 -0.0089 377 LYS A CA  
3202 C C   . LYS A 377 ? 0.3032 0.4497 0.2413 -0.0164 -0.0618 -0.0014 377 LYS A C   
3203 O O   . LYS A 377 ? 0.2920 0.4520 0.2168 -0.0113 -0.0651 0.0011  377 LYS A O   
3204 C CB  . LYS A 377 ? 0.2969 0.4710 0.2619 -0.0097 -0.0703 0.0027  377 LYS A CB  
3205 C CG  . LYS A 377 ? 0.3248 0.5143 0.3097 -0.0149 -0.0733 -0.0055 377 LYS A CG  
3206 C CD  . LYS A 377 ? 0.3838 0.5875 0.3767 -0.0020 -0.0761 0.0061  377 LYS A CD  
3207 C CE  . LYS A 377 ? 0.4280 0.6465 0.4419 -0.0084 -0.0774 -0.0021 377 LYS A CE  
3208 N NZ  . LYS A 377 ? 0.3469 0.5480 0.3733 -0.0157 -0.0719 -0.0048 377 LYS A NZ  
3209 N N   . GLU A 378 ? 0.3131 0.4313 0.2503 -0.0170 -0.0525 0.0022  378 GLU A N   
3210 C CA  . GLU A 378 ? 0.3201 0.4272 0.2396 -0.0137 -0.0466 0.0087  378 GLU A CA  
3211 C C   . GLU A 378 ? 0.3206 0.4297 0.2319 -0.0223 -0.0453 -0.0053 378 GLU A C   
3212 O O   . GLU A 378 ? 0.3768 0.4722 0.2968 -0.0293 -0.0405 -0.0149 378 GLU A O   
3213 C CB  . GLU A 378 ? 0.4206 0.5008 0.3441 -0.0126 -0.0371 0.0165  378 GLU A CB  
3214 C CG  . GLU A 378 ? 0.5401 0.6127 0.4692 -0.0042 -0.0362 0.0296  378 GLU A CG  
3215 C CD  . GLU A 378 ? 0.6031 0.6743 0.5150 0.0063  -0.0343 0.0449  378 GLU A CD  
3216 O OE1 . GLU A 378 ? 0.5756 0.6542 0.4707 0.0069  -0.0344 0.0459  378 GLU A OE1 
3217 O OE2 . GLU A 378 ? 0.6007 0.6616 0.5148 0.0145  -0.0318 0.0563  378 GLU A OE2 
3218 N N   . GLU A 379 ? 0.3255 0.4513 0.2189 -0.0204 -0.0487 -0.0062 379 GLU A N   
3219 C CA  . GLU A 379 ? 0.4049 0.5337 0.2900 -0.0282 -0.0472 -0.0215 379 GLU A CA  
3220 C C   . GLU A 379 ? 0.3438 0.4515 0.2252 -0.0301 -0.0363 -0.0223 379 GLU A C   
3221 O O   . GLU A 379 ? 0.4316 0.5348 0.3123 -0.0365 -0.0328 -0.0363 379 GLU A O   
3222 C CB  . GLU A 379 ? 0.5017 0.6455 0.3720 -0.0236 -0.0504 -0.0203 379 GLU A CB  
3223 C CG  . GLU A 379 ? 0.7534 0.9142 0.6253 -0.0149 -0.0582 -0.0099 379 GLU A CG  
3224 C CD  . GLU A 379 ? 0.8638 1.0362 0.7558 -0.0207 -0.0644 -0.0201 379 GLU A CD  
3225 O OE1 . GLU A 379 ? 0.8354 1.0119 0.7390 -0.0156 -0.0675 -0.0118 379 GLU A OE1 
3226 O OE2 . GLU A 379 ? 0.9114 1.0869 0.8072 -0.0306 -0.0648 -0.0362 379 GLU A OE2 
3227 N N   . TRP A 380 ? 0.2806 0.3758 0.1590 -0.0245 -0.0301 -0.0079 380 TRP A N   
3228 C CA  . TRP A 380 ? 0.2909 0.3720 0.1659 -0.0264 -0.0196 -0.0081 380 TRP A CA  
3229 C C   . TRP A 380 ? 0.2615 0.3258 0.1559 -0.0294 -0.0148 -0.0108 380 TRP A C   
3230 O O   . TRP A 380 ? 0.2964 0.3527 0.1916 -0.0310 -0.0066 -0.0122 380 TRP A O   
3231 C CB  . TRP A 380 ? 0.3079 0.3848 0.1687 -0.0209 -0.0138 0.0079  380 TRP A CB  
3232 C CG  . TRP A 380 ? 0.3106 0.3790 0.1776 -0.0153 -0.0150 0.0221  380 TRP A CG  
3233 C CD1 . TRP A 380 ? 0.3792 0.4578 0.2417 -0.0076 -0.0226 0.0307  380 TRP A CD1 
3234 C CD2 . TRP A 380 ? 0.3076 0.3566 0.1865 -0.0165 -0.0082 0.0283  380 TRP A CD2 
3235 N NE1 . TRP A 380 ? 0.3665 0.4300 0.2371 -0.0031 -0.0198 0.0423  380 TRP A NE1 
3236 C CE2 . TRP A 380 ? 0.2907 0.3353 0.1707 -0.0094 -0.0109 0.0403  380 TRP A CE2 
3237 C CE3 . TRP A 380 ? 0.2857 0.3225 0.1743 -0.0225 0.0000  0.0244  380 TRP A CE3 
3238 C CZ2 . TRP A 380 ? 0.2856 0.3109 0.1750 -0.0094 -0.0051 0.0472  380 TRP A CZ2 
3239 C CZ3 . TRP A 380 ? 0.3117 0.3333 0.2102 -0.0233 0.0045  0.0310  380 TRP A CZ3 
3240 C CH2 . TRP A 380 ? 0.3448 0.3591 0.2430 -0.0173 0.0023  0.0417  380 TRP A CH2 
3241 N N   . ILE A 381 ? 0.1993 0.2607 0.1090 -0.0300 -0.0196 -0.0113 381 ILE A N   
3242 C CA  . ILE A 381 ? 0.1947 0.2423 0.1212 -0.0324 -0.0162 -0.0145 381 ILE A CA  
3243 C C   . ILE A 381 ? 0.2094 0.2575 0.1426 -0.0372 -0.0187 -0.0284 381 ILE A C   
3244 O O   . ILE A 381 ? 0.2415 0.2997 0.1754 -0.0397 -0.0254 -0.0330 381 ILE A O   
3245 C CB  . ILE A 381 ? 0.2666 0.3081 0.2041 -0.0298 -0.0179 -0.0050 381 ILE A CB  
3246 C CG1 . ILE A 381 ? 0.2617 0.2970 0.1917 -0.0258 -0.0133 0.0082  381 ILE A CG1 
3247 C CG2 . ILE A 381 ? 0.2387 0.2687 0.1916 -0.0322 -0.0153 -0.0091 381 ILE A CG2 
3248 C CD1 . ILE A 381 ? 0.2970 0.3244 0.2354 -0.0224 -0.0141 0.0169  381 ILE A CD1 
3249 N N   . GLU A 382 ? 0.2011 0.2384 0.1394 -0.0385 -0.0128 -0.0352 382 GLU A N   
3250 C CA  . GLU A 382 ? 0.2034 0.2336 0.1482 -0.0423 -0.0127 -0.0470 382 GLU A CA  
3251 C C   . GLU A 382 ? 0.2118 0.2283 0.1704 -0.0401 -0.0091 -0.0435 382 GLU A C   
3252 O O   . GLU A 382 ? 0.2016 0.2136 0.1618 -0.0363 -0.0035 -0.0417 382 GLU A O   
3253 C CB  . GLU A 382 ? 0.2815 0.3099 0.2164 -0.0436 -0.0079 -0.0589 382 GLU A CB  
3254 C CG  . GLU A 382 ? 0.2981 0.3136 0.2379 -0.0475 -0.0056 -0.0714 382 GLU A CG  
3255 C CD  . GLU A 382 ? 0.4332 0.4449 0.3618 -0.0482 0.0001  -0.0845 382 GLU A CD  
3256 O OE1 . GLU A 382 ? 0.4898 0.5147 0.4047 -0.0481 -0.0005 -0.0860 382 GLU A OE1 
3257 O OE2 . GLU A 382 ? 0.5184 0.5125 0.4506 -0.0479 0.0061  -0.0928 382 GLU A OE2 
3258 N N   . THR A 383 ? 0.1825 0.1954 0.1510 -0.0422 -0.0124 -0.0422 383 THR A N   
3259 C CA  . THR A 383 ? 0.1397 0.1400 0.1188 -0.0397 -0.0090 -0.0393 383 THR A CA  
3260 C C   . THR A 383 ? 0.1559 0.1428 0.1351 -0.0399 -0.0038 -0.0486 383 THR A C   
3261 O O   . THR A 383 ? 0.2001 0.1845 0.1746 -0.0451 -0.0037 -0.0587 383 THR A O   
3262 C CB  . THR A 383 ? 0.1822 0.1822 0.1707 -0.0417 -0.0127 -0.0347 383 THR A CB  
3263 O OG1 . THR A 383 ? 0.1865 0.1902 0.1759 -0.0484 -0.0157 -0.0422 383 THR A OG1 
3264 C CG2 . THR A 383 ? 0.1925 0.2013 0.1813 -0.0390 -0.0159 -0.0246 383 THR A CG2 
3265 N N   . LEU A 384 ? 0.1756 0.1539 0.1597 -0.0336 0.0009  -0.0454 384 LEU A N   
3266 C CA  . LEU A 384 ? 0.1887 0.1524 0.1718 -0.0300 0.0073  -0.0521 384 LEU A CA  
3267 C C   . LEU A 384 ? 0.1957 0.1461 0.1865 -0.0261 0.0096  -0.0471 384 LEU A C   
3268 O O   . LEU A 384 ? 0.1717 0.1277 0.1684 -0.0235 0.0071  -0.0382 384 LEU A O   
3269 C CB  . LEU A 384 ? 0.2141 0.1825 0.1944 -0.0225 0.0121  -0.0530 384 LEU A CB  
3270 C CG  . LEU A 384 ? 0.2134 0.1949 0.1843 -0.0250 0.0120  -0.0568 384 LEU A CG  
3271 C CD1 . LEU A 384 ? 0.2176 0.2051 0.1891 -0.0173 0.0181  -0.0568 384 LEU A CD1 
3272 C CD2 . LEU A 384 ? 0.1978 0.1744 0.1589 -0.0309 0.0122  -0.0686 384 LEU A CD2 
3273 N N   . THR A 385 ? 0.1868 0.1179 0.1758 -0.0255 0.0152  -0.0529 385 THR A N   
3274 C CA  . THR A 385 ? 0.2049 0.1210 0.1977 -0.0180 0.0197  -0.0468 385 THR A CA  
3275 C C   . THR A 385 ? 0.2254 0.1470 0.2191 -0.0049 0.0226  -0.0430 385 THR A C   
3276 O O   . THR A 385 ? 0.2082 0.1403 0.1991 -0.0028 0.0236  -0.0475 385 THR A O   
3277 C CB  . THR A 385 ? 0.2071 0.0967 0.1963 -0.0205 0.0270  -0.0534 385 THR A CB  
3278 O OG1 . THR A 385 ? 0.2259 0.1064 0.2080 -0.0164 0.0330  -0.0626 385 THR A OG1 
3279 C CG2 . THR A 385 ? 0.3011 0.1896 0.2910 -0.0359 0.0244  -0.0599 385 THR A CG2 
3280 N N   . LEU A 386 ? 0.1811 0.0979 0.1786 0.0043  0.0243  -0.0347 386 LEU A N   
3281 C CA  . LEU A 386 ? 0.2442 0.1699 0.2438 0.0180  0.0269  -0.0315 386 LEU A CA  
3282 C C   . LEU A 386 ? 0.2391 0.1514 0.2334 0.0249  0.0348  -0.0393 386 LEU A C   
3283 O O   . LEU A 386 ? 0.2210 0.1479 0.2169 0.0324  0.0366  -0.0414 386 LEU A O   
3284 C CB  . LEU A 386 ? 0.2168 0.1397 0.2193 0.0281  0.0271  -0.0213 386 LEU A CB  
3285 C CG  . LEU A 386 ? 0.2078 0.1432 0.2145 0.0224  0.0203  -0.0143 386 LEU A CG  
3286 C CD1 . LEU A 386 ? 0.2093 0.1426 0.2161 0.0340  0.0212  -0.0047 386 LEU A CD1 
3287 C CD2 . LEU A 386 ? 0.1965 0.1586 0.2083 0.0175  0.0146  -0.0152 386 LEU A CD2 
3288 N N   . GLU A 387 ? 0.2274 0.1117 0.2154 0.0218  0.0406  -0.0446 387 GLU A N   
3289 C CA  . GLU A 387 ? 0.3053 0.1724 0.2867 0.0277  0.0496  -0.0538 387 GLU A CA  
3290 C C   . GLU A 387 ? 0.2495 0.1319 0.2273 0.0210  0.0482  -0.0644 387 GLU A C   
3291 O O   . GLU A 387 ? 0.2728 0.1584 0.2485 0.0304  0.0537  -0.0691 387 GLU A O   
3292 C CB  . GLU A 387 ? 0.2815 0.1136 0.2563 0.0214  0.0567  -0.0593 387 GLU A CB  
3293 C CG  . GLU A 387 ? 0.3778 0.1934 0.3466 0.0297  0.0644  -0.0646 387 GLU A CG  
3294 C CD  . GLU A 387 ? 0.7148 0.5114 0.6784 0.0168  0.0664  -0.0716 387 GLU A CD  
3295 O OE1 . GLU A 387 ? 0.8093 0.6021 0.7669 0.0136  0.0693  -0.0832 387 GLU A OE1 
3296 O OE2 . GLU A 387 ? 0.8036 0.5906 0.7690 0.0099  0.0657  -0.0658 387 GLU A OE2 
3297 N N   . GLU A 388 ? 0.2368 0.1295 0.2132 0.0060  0.0414  -0.0679 388 GLU A N   
3298 C CA  . GLU A 388 ? 0.2355 0.1434 0.2058 0.0001  0.0398  -0.0765 388 GLU A CA  
3299 C C   . GLU A 388 ? 0.2486 0.1825 0.2232 0.0068  0.0380  -0.0705 388 GLU A C   
3300 O O   . GLU A 388 ? 0.2855 0.2281 0.2551 0.0093  0.0419  -0.0768 388 GLU A O   
3301 C CB  . GLU A 388 ? 0.2898 0.2057 0.2575 -0.0152 0.0321  -0.0793 388 GLU A CB  
3302 C CG  . GLU A 388 ? 0.3458 0.2411 0.3090 -0.0252 0.0347  -0.0897 388 GLU A CG  
3303 C CD  . GLU A 388 ? 0.3689 0.2760 0.3340 -0.0389 0.0263  -0.0903 388 GLU A CD  
3304 O OE1 . GLU A 388 ? 0.2543 0.1784 0.2257 -0.0387 0.0192  -0.0797 388 GLU A OE1 
3305 O OE2 . GLU A 388 ? 0.4376 0.3417 0.3999 -0.0473 0.0254  -0.0974 388 GLU A OE2 
3306 N N   . ALA A 389 ? 0.2227 0.1694 0.2065 0.0088  0.0329  -0.0593 389 ALA A N   
3307 C CA  . ALA A 389 ? 0.1875 0.1590 0.1769 0.0127  0.0319  -0.0545 389 ALA A CA  
3308 C C   . ALA A 389 ? 0.2772 0.2528 0.2705 0.0271  0.0389  -0.0558 389 ALA A C   
3309 O O   . ALA A 389 ? 0.2901 0.2850 0.2850 0.0294  0.0416  -0.0579 389 ALA A O   
3310 C CB  . ALA A 389 ? 0.1669 0.1489 0.1647 0.0108  0.0256  -0.0443 389 ALA A CB  
3311 N N   . MET A 390 ? 0.2601 0.2180 0.2548 0.0377  0.0425  -0.0538 390 MET A N   
3312 C CA  . MET A 390 ? 0.2544 0.2159 0.2530 0.0548  0.0494  -0.0537 390 MET A CA  
3313 C C   . MET A 390 ? 0.3067 0.2609 0.2976 0.0576  0.0578  -0.0653 390 MET A C   
3314 O O   . MET A 390 ? 0.3312 0.3023 0.3266 0.0685  0.0627  -0.0668 390 MET A O   
3315 C CB  . MET A 390 ? 0.2741 0.2138 0.2730 0.0668  0.0522  -0.0472 390 MET A CB  
3316 C CG  . MET A 390 ? 0.5126 0.4588 0.5165 0.0882  0.0583  -0.0441 390 MET A CG  
3317 S SD  . MET A 390 ? 0.5600 0.4770 0.5607 0.1045  0.0626  -0.0337 390 MET A SD  
3318 C CE  . MET A 390 ? 0.5240 0.3939 0.5107 0.0971  0.0717  -0.0439 390 MET A CE  
3319 N N   . ARG A 391 ? 0.2744 0.2067 0.2538 0.0472  0.0595  -0.0745 391 ARG A N   
3320 C CA  . ARG A 391 ? 0.3505 0.2708 0.3200 0.0496  0.0683  -0.0875 391 ARG A CA  
3321 C C   . ARG A 391 ? 0.3763 0.3131 0.3378 0.0376  0.0664  -0.0955 391 ARG A C   
3322 O O   . ARG A 391 ? 0.3632 0.2948 0.3155 0.0399  0.0739  -0.1070 391 ARG A O   
3323 C CB  . ARG A 391 ? 0.4167 0.2986 0.3771 0.0462  0.0735  -0.0949 391 ARG A CB  
3324 C CG  . ARG A 391 ? 0.5397 0.4010 0.5050 0.0588  0.0767  -0.0854 391 ARG A CG  
3325 C CD  . ARG A 391 ? 0.6446 0.4748 0.6026 0.0529  0.0788  -0.0894 391 ARG A CD  
3326 N NE  . ARG A 391 ? 0.7587 0.5717 0.7204 0.0642  0.0814  -0.0780 391 ARG A NE  
3327 C CZ  . ARG A 391 ? 0.8372 0.6471 0.8013 0.0824  0.0868  -0.0736 391 ARG A CZ  
3328 N NH1 . ARG A 391 ? 0.8644 0.6878 0.8292 0.0913  0.0907  -0.0805 391 ARG A NH1 
3329 N NH2 . ARG A 391 ? 0.8468 0.6419 0.8124 0.0916  0.0886  -0.0620 391 ARG A NH2 
3330 N N   . LYS A 392 ? 0.3334 0.2885 0.2966 0.0261  0.0573  -0.0896 392 LYS A N   
3331 C CA  . LYS A 392 ? 0.3514 0.3209 0.3047 0.0157  0.0554  -0.0948 392 LYS A CA  
3332 C C   . LYS A 392 ? 0.3218 0.3078 0.2730 0.0229  0.0632  -0.0990 392 LYS A C   
3333 O O   . LYS A 392 ? 0.3239 0.3278 0.2868 0.0310  0.0653  -0.0922 392 LYS A O   
3334 C CB  . LYS A 392 ? 0.3860 0.3724 0.3432 0.0064  0.0460  -0.0841 392 LYS A CB  
3335 C CG  . LYS A 392 ? 0.4527 0.4431 0.3973 -0.0057 0.0410  -0.0876 392 LYS A CG  
3336 C CD  . LYS A 392 ? 0.4262 0.4007 0.3692 -0.0133 0.0354  -0.0906 392 LYS A CD  
3337 C CE  . LYS A 392 ? 0.5283 0.5107 0.4582 -0.0237 0.0304  -0.0965 392 LYS A CE  
3338 N NZ  . LYS A 392 ? 0.6665 0.6331 0.5912 -0.0307 0.0301  -0.1090 392 LYS A NZ  
3339 N N   . GLU A 393 ? 0.3065 0.2890 0.2431 0.0194  0.0679  -0.1111 393 GLU A N   
3340 C CA  . GLU A 393 ? 0.3246 0.3222 0.2582 0.0266  0.0770  -0.1163 393 GLU A CA  
3341 C C   . GLU A 393 ? 0.3498 0.3743 0.2797 0.0188  0.0749  -0.1106 393 GLU A C   
3342 O O   . GLU A 393 ? 0.4192 0.4639 0.3551 0.0245  0.0813  -0.1084 393 GLU A O   
3343 C CB  . GLU A 393 ? 0.4492 0.4289 0.3676 0.0278  0.0827  -0.1296 393 GLU A CB  
3344 C CG  . GLU A 393 ? 0.5220 0.4740 0.4443 0.0390  0.0875  -0.1327 393 GLU A CG  
3345 C CD  . GLU A 393 ? 0.7337 0.6672 0.6417 0.0397  0.0916  -0.1442 393 GLU A CD  
3346 O OE1 . GLU A 393 ? 0.7700 0.7157 0.6663 0.0358  0.0931  -0.1498 393 GLU A OE1 
3347 O OE2 . GLU A 393 ? 0.7797 0.6863 0.6881 0.0438  0.0934  -0.1474 393 GLU A OE2 
3348 N N   . ASP A 394 ? 0.3283 0.3541 0.2491 0.0065  0.0667  -0.1074 394 ASP A N   
3349 C CA  . ASP A 394 ? 0.3729 0.4189 0.2851 -0.0004 0.0663  -0.1018 394 ASP A CA  
3350 C C   . ASP A 394 ? 0.3614 0.4197 0.2867 -0.0033 0.0622  -0.0868 394 ASP A C   
3351 O O   . ASP A 394 ? 0.2965 0.3584 0.2157 -0.0115 0.0566  -0.0788 394 ASP A O   
3352 C CB  . ASP A 394 ? 0.3886 0.4312 0.2822 -0.0101 0.0600  -0.1058 394 ASP A CB  
3353 C CG  . ASP A 394 ? 0.5961 0.6234 0.4935 -0.0150 0.0502  -0.1054 394 ASP A CG  
3354 O OD1 . ASP A 394 ? 0.6634 0.6780 0.5754 -0.0106 0.0499  -0.1035 394 ASP A OD1 
3355 O OD2 . ASP A 394 ? 0.5312 0.5611 0.4171 -0.0230 0.0431  -0.1066 394 ASP A OD2 
3356 N N   . VAL A 395 ? 0.2797 0.3448 0.2228 0.0039  0.0652  -0.0832 395 VAL A N   
3357 C CA  . VAL A 395 ? 0.2654 0.3436 0.2221 0.0005  0.0624  -0.0718 395 VAL A CA  
3358 C C   . VAL A 395 ? 0.2908 0.3925 0.2588 0.0055  0.0713  -0.0722 395 VAL A C   
3359 O O   . VAL A 395 ? 0.2985 0.4047 0.2663 0.0145  0.0790  -0.0804 395 VAL A O   
3360 C CB  . VAL A 395 ? 0.2553 0.3230 0.2248 0.0029  0.0549  -0.0669 395 VAL A CB  
3361 C CG1 . VAL A 395 ? 0.2606 0.3086 0.2210 -0.0032 0.0468  -0.0665 395 VAL A CG1 
3362 C CG2 . VAL A 395 ? 0.2656 0.3294 0.2448 0.0165  0.0586  -0.0716 395 VAL A CG2 
3363 N N   . LYS A 396 ? 0.2327 0.3501 0.2111 -0.0010 0.0709  -0.0640 396 LYS A N   
3364 C CA  . LYS A 396 ? 0.1916 0.3364 0.1847 0.0015  0.0786  -0.0646 396 LYS A CA  
3365 C C   . LYS A 396 ? 0.1800 0.3332 0.1928 0.0112  0.0750  -0.0640 396 LYS A C   
3366 O O   . LYS A 396 ? 0.1691 0.3102 0.1854 0.0103  0.0664  -0.0593 396 LYS A O   
3367 C CB  . LYS A 396 ? 0.3000 0.4581 0.2947 -0.0124 0.0813  -0.0573 396 LYS A CB  
3368 C CG  . LYS A 396 ? 0.3804 0.5349 0.3552 -0.0203 0.0872  -0.0558 396 LYS A CG  
3369 C CD  . LYS A 396 ? 0.4581 0.6250 0.4316 -0.0152 0.0960  -0.0605 396 LYS A CD  
3370 C CE  . LYS A 396 ? 0.4718 0.6382 0.4308 -0.0248 0.1014  -0.0541 396 LYS A CE  
3371 N NZ  . LYS A 396 ? 0.4457 0.6207 0.3998 -0.0194 0.1096  -0.0589 396 LYS A NZ  
3372 N N   . THR A 397 ? 0.2094 0.2408 0.1515 -0.0249 0.0124  0.0075  397 THR A N   
3373 C CA  . THR A 397 ? 0.2119 0.2441 0.1664 -0.0226 0.0160  0.0039  397 THR A CA  
3374 C C   . THR A 397 ? 0.2189 0.2614 0.1776 -0.0219 0.0242  0.0065  397 THR A C   
3375 O O   . THR A 397 ? 0.2669 0.3160 0.2163 -0.0235 0.0283  0.0095  397 THR A O   
3376 C CB  . THR A 397 ? 0.2793 0.3029 0.2253 -0.0192 0.0161  -0.0048 397 THR A CB  
3377 O OG1 . THR A 397 ? 0.2973 0.3220 0.2285 -0.0141 0.0218  -0.0082 397 THR A OG1 
3378 C CG2 . THR A 397 ? 0.2438 0.2591 0.1822 -0.0241 0.0081  -0.0077 397 THR A CG2 
3379 N N   . GLU A 398 ? 0.1821 0.2287 0.1547 -0.0203 0.0265  0.0053  398 GLU A N   
3380 C CA  . GLU A 398 ? 0.2300 0.2920 0.2091 -0.0208 0.0337  0.0072  398 GLU A CA  
3381 C C   . GLU A 398 ? 0.1942 0.2607 0.1839 -0.0145 0.0356  0.0023  398 GLU A C   
3382 O O   . GLU A 398 ? 0.2055 0.2614 0.2019 -0.0139 0.0311  0.0007  398 GLU A O   
3383 C CB  . GLU A 398 ? 0.2574 0.3199 0.2421 -0.0299 0.0332  0.0151  398 GLU A CB  
3384 C CG  . GLU A 398 ? 0.2413 0.3217 0.2318 -0.0352 0.0401  0.0175  398 GLU A CG  
3385 C CD  . GLU A 398 ? 0.3561 0.4291 0.3445 -0.0469 0.0391  0.0254  398 GLU A CD  
3386 O OE1 . GLU A 398 ? 0.3660 0.4202 0.3443 -0.0482 0.0340  0.0296  398 GLU A OE1 
3387 O OE2 . GLU A 398 ? 0.3334 0.4183 0.3280 -0.0545 0.0431  0.0274  398 GLU A OE2 
3388 N N   . VAL A 399 ? 0.1826 0.2671 0.1730 -0.0094 0.0424  0.0002  399 VAL A N   
3389 C CA  . VAL A 399 ? 0.1975 0.2894 0.1970 -0.0015 0.0443  -0.0036 399 VAL A CA  
3390 C C   . VAL A 399 ? 0.2345 0.3436 0.2500 -0.0094 0.0463  0.0011  399 VAL A C   
3391 O O   . VAL A 399 ? 0.2630 0.3885 0.2790 -0.0179 0.0502  0.0055  399 VAL A O   
3392 C CB  . VAL A 399 ? 0.1878 0.2925 0.1779 0.0121  0.0501  -0.0094 399 VAL A CB  
3393 C CG1 . VAL A 399 ? 0.2537 0.3689 0.2528 0.0221  0.0518  -0.0124 399 VAL A CG1 
3394 C CG2 . VAL A 399 ? 0.2511 0.3317 0.2207 0.0194  0.0475  -0.0151 399 VAL A CG2 
3395 N N   . ILE A 400 ? 0.1962 0.3010 0.2228 -0.0080 0.0436  0.0002  400 ILE A N   
3396 C CA  . ILE A 400 ? 0.2174 0.3388 0.2578 -0.0147 0.0453  0.0032  400 ILE A CA  
3397 C C   . ILE A 400 ? 0.1755 0.3102 0.2231 -0.0035 0.0469  -0.0013 400 ILE A C   
3398 O O   . ILE A 400 ? 0.1914 0.3108 0.2333 0.0077  0.0448  -0.0057 400 ILE A O   
3399 C CB  . ILE A 400 ? 0.2434 0.3476 0.2895 -0.0241 0.0400  0.0071  400 ILE A CB  
3400 C CG1 . ILE A 400 ? 0.3252 0.4092 0.3718 -0.0181 0.0345  0.0041  400 ILE A CG1 
3401 C CG2 . ILE A 400 ? 0.2607 0.3550 0.2977 -0.0339 0.0388  0.0127  400 ILE A CG2 
3402 C CD1 . ILE A 400 ? 0.4234 0.4953 0.4760 -0.0243 0.0297  0.0072  400 ILE A CD1 
3403 N N   . GLU A 401 ? 0.1582 0.3216 0.2161 -0.0072 0.0507  0.0001  401 GLU A N   
3404 C CA  . GLU A 401 ? 0.1077 0.2914 0.1719 0.0052  0.0526  -0.0038 401 GLU A CA  
3405 C C   . GLU A 401 ? 0.1091 0.2943 0.1862 0.0006  0.0495  -0.0028 401 GLU A C   
3406 O O   . GLU A 401 ? 0.1415 0.3310 0.2203 0.0126  0.0483  -0.0058 401 GLU A O   
3407 C CB  . GLU A 401 ? 0.1448 0.3596 0.2089 0.0063  0.0566  -0.0038 401 GLU A CB  
3408 C CG  . GLU A 401 ? 0.2852 0.5057 0.3371 0.0118  0.0611  -0.0053 401 GLU A CG  
3409 C CD  . GLU A 401 ? 0.3964 0.6059 0.4360 0.0339  0.0623  -0.0119 401 GLU A CD  
3410 O OE1 . GLU A 401 ? 0.4194 0.6152 0.4441 0.0374  0.0634  -0.0137 401 GLU A OE1 
3411 O OE2 . GLU A 401 ? 0.3971 0.6014 0.4373 0.0467  0.0596  -0.0151 401 GLU A OE2 
3412 N N   . SER A 402 ? 0.0968 0.2716 0.1784 -0.0153 0.0469  0.0014  402 SER A N   
3413 C CA  . SER A 402 ? 0.0881 0.2594 0.1774 -0.0203 0.0431  0.0021  402 SER A CA  
3414 C C   . SER A 402 ? 0.1590 0.3087 0.2488 -0.0324 0.0400  0.0053  402 SER A C   
3415 O O   . SER A 402 ? 0.1847 0.3244 0.2669 -0.0413 0.0402  0.0088  402 SER A O   
3416 C CB  . SER A 402 ? 0.1168 0.3064 0.2065 -0.0267 0.0433  0.0031  402 SER A CB  
3417 O OG  . SER A 402 ? 0.1879 0.3760 0.2830 -0.0291 0.0397  0.0026  402 SER A OG  
3418 N N   . VAL A 403 ? 0.1380 0.2770 0.2335 -0.0310 0.0363  0.0043  403 VAL A N   
3419 C CA  . VAL A 403 ? 0.1376 0.2550 0.2315 -0.0398 0.0326  0.0066  403 VAL A CA  
3420 C C   . VAL A 403 ? 0.1432 0.2614 0.2404 -0.0440 0.0304  0.0064  403 VAL A C   
3421 O O   . VAL A 403 ? 0.1573 0.2883 0.2593 -0.0376 0.0304  0.0042  403 VAL A O   
3422 C CB  . VAL A 403 ? 0.1531 0.2482 0.2456 -0.0319 0.0285  0.0053  403 VAL A CB  
3423 C CG1 . VAL A 403 ? 0.1407 0.2280 0.2250 -0.0273 0.0286  0.0054  403 VAL A CG1 
3424 C CG2 . VAL A 403 ? 0.1502 0.2487 0.2492 -0.0231 0.0275  0.0020  403 VAL A CG2 
3425 N N   . LYS A 404 ? 0.1364 0.2386 0.2280 -0.0545 0.0284  0.0087  404 LYS A N   
3426 C CA  . LYS A 404 ? 0.1154 0.2131 0.2071 -0.0591 0.0258  0.0080  404 LYS A CA  
3427 C C   . LYS A 404 ? 0.1381 0.2240 0.2346 -0.0532 0.0228  0.0063  404 LYS A C   
3428 O O   . LYS A 404 ? 0.1300 0.1980 0.2223 -0.0523 0.0215  0.0067  404 LYS A O   
3429 C CB  . LYS A 404 ? 0.1334 0.2163 0.2119 -0.0737 0.0252  0.0108  404 LYS A CB  
3430 C CG  . LYS A 404 ? 0.2006 0.2787 0.2760 -0.0804 0.0226  0.0092  404 LYS A CG  
3431 C CD  . LYS A 404 ? 0.3710 0.4374 0.4296 -0.0961 0.0225  0.0117  404 LYS A CD  
3432 C CE  . LYS A 404 ? 0.4338 0.5274 0.4934 -0.1013 0.0252  0.0121  404 LYS A CE  
3433 N NZ  . LYS A 404 ? 0.5569 0.6571 0.6115 -0.1120 0.0235  0.0104  404 LYS A NZ  
3434 N N   . ALA A 405 ? 0.1210 0.2152 0.2237 -0.0467 0.0212  0.0044  405 ALA A N   
3435 C CA  . ALA A 405 ? 0.0998 0.1857 0.2036 -0.0403 0.0186  0.0023  405 ALA A CA  
3436 C C   . ALA A 405 ? 0.0730 0.1391 0.1739 -0.0456 0.0171  0.0012  405 ALA A C   
3437 O O   . ALA A 405 ? 0.1508 0.2102 0.2457 -0.0560 0.0168  0.0015  405 ALA A O   
3438 C CB  . ALA A 405 ? 0.1331 0.2301 0.2403 -0.0351 0.0173  0.0015  405 ALA A CB  
3439 N N   . GLY A 406 ? 0.0957 0.1509 0.1982 -0.0376 0.0156  0.0005  406 GLY A N   
3440 C CA  . GLY A 406 ? 0.1222 0.1578 0.2163 -0.0365 0.0127  0.0003  406 GLY A CA  
3441 C C   . GLY A 406 ? 0.0928 0.1272 0.1903 -0.0261 0.0110  -0.0005 406 GLY A C   
3442 O O   . GLY A 406 ? 0.0826 0.1288 0.1882 -0.0226 0.0119  -0.0010 406 GLY A O   
3443 N N   . THR A 407 ? 0.0867 0.1062 0.1757 -0.0212 0.0085  -0.0007 407 THR A N   
3444 C CA  . THR A 407 ? 0.1012 0.1248 0.1931 -0.0111 0.0066  -0.0015 407 THR A CA  
3445 C C   . THR A 407 ? 0.1342 0.1421 0.2132 -0.0052 0.0039  0.0006  407 THR A C   
3446 O O   . THR A 407 ? 0.1618 0.1501 0.2271 -0.0097 0.0035  0.0025  407 THR A O   
3447 C CB  . THR A 407 ? 0.1056 0.1330 0.2005 -0.0058 0.0061  -0.0049 407 THR A CB  
3448 O OG1 . THR A 407 ? 0.1269 0.1337 0.2076 -0.0025 0.0042  -0.0061 407 THR A OG1 
3449 C CG2 . THR A 407 ? 0.0966 0.1343 0.1997 -0.0115 0.0082  -0.0065 407 THR A CG2 
3450 N N   . TRP A 408 ? 0.1017 0.1183 0.1831 0.0050  0.0017  0.0001  408 TRP A N   
3451 C CA  . TRP A 408 ? 0.1349 0.1374 0.2024 0.0145  -0.0016 0.0020  408 TRP A CA  
3452 C C   . TRP A 408 ? 0.1729 0.1535 0.2250 0.0230  -0.0035 0.0000  408 TRP A C   
3453 O O   . TRP A 408 ? 0.1882 0.1513 0.2238 0.0337  -0.0067 0.0015  408 TRP A O   
3454 C CB  . TRP A 408 ? 0.1123 0.1369 0.1874 0.0234  -0.0039 0.0021  408 TRP A CB  
3455 C CG  . TRP A 408 ? 0.1542 0.2030 0.2414 0.0288  -0.0037 -0.0012 408 TRP A CG  
3456 C CD1 . TRP A 408 ? 0.1476 0.1982 0.2382 0.0294  -0.0018 -0.0045 408 TRP A CD1 
3457 C CD2 . TRP A 408 ? 0.1305 0.2077 0.2269 0.0329  -0.0053 -0.0015 408 TRP A CD2 
3458 N NE1 . TRP A 408 ? 0.0872 0.1659 0.1886 0.0338  -0.0018 -0.0064 408 TRP A NE1 
3459 C CE2 . TRP A 408 ? 0.0774 0.1739 0.1828 0.0350  -0.0039 -0.0046 408 TRP A CE2 
3460 C CE3 . TRP A 408 ? 0.0853 0.1756 0.1828 0.0333  -0.0080 0.0006  408 TRP A CE3 
3461 C CZ2 . TRP A 408 ? 0.0819 0.2123 0.1976 0.0364  -0.0047 -0.0054 408 TRP A CZ2 
3462 C CZ3 . TRP A 408 ? 0.1355 0.2590 0.2432 0.0348  -0.0095 -0.0006 408 TRP A CZ3 
3463 C CH2 . TRP A 408 ? 0.1087 0.2529 0.2257 0.0354  -0.0076 -0.0035 408 TRP A CH2 
3464 N N   . PHE A 409 ? 0.1442 0.1226 0.1982 0.0195  -0.0019 -0.0035 409 PHE A N   
3465 C CA  . PHE A 409 ? 0.2221 0.1730 0.2566 0.0257  -0.0037 -0.0060 409 PHE A CA  
3466 C C   . PHE A 409 ? 0.2411 0.1655 0.2610 0.0101  -0.0032 -0.0043 409 PHE A C   
3467 O O   . PHE A 409 ? 0.2072 0.1385 0.2345 -0.0025 -0.0010 -0.0059 409 PHE A O   
3468 C CB  . PHE A 409 ? 0.2168 0.1796 0.2585 0.0301  -0.0026 -0.0111 409 PHE A CB  
3469 C CG  . PHE A 409 ? 0.4690 0.4060 0.4890 0.0431  -0.0051 -0.0148 409 PHE A CG  
3470 C CD1 . PHE A 409 ? 0.5667 0.4689 0.5655 0.0351  -0.0059 -0.0164 409 PHE A CD1 
3471 C CD2 . PHE A 409 ? 0.5592 0.5067 0.5776 0.0634  -0.0066 -0.0170 409 PHE A CD2 
3472 C CE1 . PHE A 409 ? 0.5680 0.4399 0.5416 0.0477  -0.0085 -0.0204 409 PHE A CE1 
3473 C CE2 . PHE A 409 ? 0.6291 0.5511 0.6244 0.0788  -0.0088 -0.0211 409 PHE A CE2 
3474 C CZ  . PHE A 409 ? 0.6033 0.4839 0.5746 0.0712  -0.0098 -0.0229 409 PHE A CZ  
3475 N N   . ASP A 410 ? 0.2770 0.1732 0.2755 0.0103  -0.0053 -0.0006 410 ASP A N   
3476 C CA  . ASP A 410 ? 0.3116 0.1799 0.2912 -0.0066 -0.0050 0.0018  410 ASP A CA  
3477 C C   . ASP A 410 ? 0.3021 0.1948 0.2992 -0.0250 -0.0010 0.0037  410 ASP A C   
3478 O O   . ASP A 410 ? 0.3361 0.2185 0.3238 -0.0423 0.0001  0.0045  410 ASP A O   
3479 C CB  . ASP A 410 ? 0.3299 0.1708 0.2907 -0.0105 -0.0063 -0.0024 410 ASP A CB  
3480 C CG  . ASP A 410 ? 0.5175 0.3292 0.4554 0.0102  -0.0101 -0.0050 410 ASP A CG  
3481 O OD1 . ASP A 410 ? 0.5371 0.3353 0.4622 0.0234  -0.0126 -0.0016 410 ASP A OD1 
3482 O OD2 . ASP A 410 ? 0.5765 0.3788 0.5075 0.0146  -0.0108 -0.0106 410 ASP A OD2 
3483 N N   . GLY A 411 ? 0.2232 0.1485 0.2436 -0.0217 0.0009  0.0044  411 GLY A N   
3484 C CA  . GLY A 411 ? 0.2345 0.1837 0.2703 -0.0343 0.0047  0.0054  411 GLY A CA  
3485 C C   . GLY A 411 ? 0.2361 0.2009 0.2831 -0.0419 0.0064  0.0018  411 GLY A C   
3486 O O   . GLY A 411 ? 0.2019 0.1847 0.2573 -0.0524 0.0092  0.0026  411 GLY A O   
3487 N N   . ASN A 412 ? 0.1518 0.1123 0.1985 -0.0359 0.0049  -0.0023 412 ASN A N   
3488 C CA  . ASN A 412 ? 0.1649 0.1385 0.2193 -0.0436 0.0059  -0.0055 412 ASN A CA  
3489 C C   . ASN A 412 ? 0.1739 0.1597 0.2394 -0.0320 0.0055  -0.0092 412 ASN A C   
3490 O O   . ASN A 412 ? 0.1631 0.1511 0.2319 -0.0197 0.0049  -0.0091 412 ASN A O   
3491 C CB  . ASN A 412 ? 0.2007 0.1503 0.2350 -0.0566 0.0043  -0.0068 412 ASN A CB  
3492 C CG  . ASN A 412 ? 0.2311 0.1465 0.2440 -0.0474 0.0010  -0.0095 412 ASN A CG  
3493 O OD1 . ASN A 412 ? 0.2301 0.1505 0.2487 -0.0333 0.0003  -0.0130 412 ASN A OD1 
3494 N ND2 . ASN A 412 ? 0.3059 0.1851 0.2913 -0.0554 -0.0010 -0.0081 412 ASN A ND2 
3495 N N   . PHE A 413 ? 0.1437 0.1405 0.2148 -0.0370 0.0060  -0.0121 413 PHE A N   
3496 C CA  . PHE A 413 ? 0.1110 0.1222 0.1927 -0.0284 0.0063  -0.0148 413 PHE A CA  
3497 C C   . PHE A 413 ? 0.1539 0.1505 0.2241 -0.0250 0.0044  -0.0194 413 PHE A C   
3498 O O   . PHE A 413 ? 0.1369 0.1466 0.2145 -0.0198 0.0049  -0.0218 413 PHE A O   
3499 C CB  . PHE A 413 ? 0.0828 0.1188 0.1784 -0.0332 0.0079  -0.0145 413 PHE A CB  
3500 C CG  . PHE A 413 ? 0.0849 0.1346 0.1903 -0.0318 0.0099  -0.0111 413 PHE A CG  
3501 C CD1 . PHE A 413 ? 0.1024 0.1588 0.2147 -0.0236 0.0106  -0.0102 413 PHE A CD1 
3502 C CD2 . PHE A 413 ? 0.1091 0.1643 0.2145 -0.0397 0.0111  -0.0089 413 PHE A CD2 
3503 C CE1 . PHE A 413 ? 0.0895 0.1504 0.2005 -0.0216 0.0114  -0.0072 413 PHE A CE1 
3504 C CE2 . PHE A 413 ? 0.1295 0.1935 0.2366 -0.0354 0.0124  -0.0059 413 PHE A CE2 
3505 C CZ  . PHE A 413 ? 0.0804 0.1446 0.1889 -0.0263 0.0123  -0.0054 413 PHE A CZ  
3506 N N   . LEU A 414 ? 0.1521 0.1190 0.2013 -0.0272 0.0023  -0.0207 414 LEU A N   
3507 C CA  . LEU A 414 ? 0.1807 0.1286 0.2140 -0.0252 0.0003  -0.0260 414 LEU A CA  
3508 C C   . LEU A 414 ? 0.1798 0.1300 0.2136 -0.0066 0.0003  -0.0291 414 LEU A C   
3509 O O   . LEU A 414 ? 0.2097 0.1510 0.2334 -0.0029 -0.0006 -0.0342 414 LEU A O   
3510 C CB  . LEU A 414 ? 0.2240 0.1321 0.2289 -0.0320 -0.0024 -0.0265 414 LEU A CB  
3511 C CG  . LEU A 414 ? 0.2685 0.1759 0.2698 -0.0545 -0.0023 -0.0242 414 LEU A CG  
3512 C CD1 . LEU A 414 ? 0.3193 0.1812 0.2869 -0.0636 -0.0050 -0.0241 414 LEU A CD1 
3513 C CD2 . LEU A 414 ? 0.3045 0.2338 0.3155 -0.0651 -0.0022 -0.0276 414 LEU A CD2 
3514 N N   . LYS A 415 ? 0.1576 0.1216 0.2018 0.0045  0.0013  -0.0264 415 LYS A N   
3515 C CA  . LYS A 415 ? 0.1746 0.1503 0.2216 0.0206  0.0018  -0.0293 415 LYS A CA  
3516 C C   . LYS A 415 ? 0.1780 0.1827 0.2423 0.0182  0.0043  -0.0302 415 LYS A C   
3517 O O   . LYS A 415 ? 0.1859 0.2029 0.2519 0.0289  0.0053  -0.0330 415 LYS A O   
3518 C CB  . LYS A 415 ? 0.1982 0.1846 0.2508 0.0318  0.0017  -0.0262 415 LYS A CB  
3519 C CG  . LYS A 415 ? 0.4885 0.4528 0.5205 0.0490  -0.0010 -0.0284 415 LYS A CG  
3520 C CD  . LYS A 415 ? 0.5925 0.5688 0.6225 0.0653  -0.0003 -0.0338 415 LYS A CD  
3521 C CE  . LYS A 415 ? 0.7365 0.6858 0.7408 0.0857  -0.0034 -0.0368 415 LYS A CE  
3522 N NZ  . LYS A 415 ? 0.7874 0.7304 0.7787 0.0982  -0.0030 -0.0439 415 LYS A NZ  
3523 N N   . TRP A 416 ? 0.1176 0.1340 0.1933 0.0056  0.0054  -0.0278 416 TRP A N   
3524 C CA  . TRP A 416 ? 0.0878 0.1277 0.1766 0.0040  0.0074  -0.0276 416 TRP A CA  
3525 C C   . TRP A 416 ? 0.1327 0.1737 0.2207 -0.0051 0.0068  -0.0291 416 TRP A C   
3526 O O   . TRP A 416 ? 0.1157 0.1727 0.2107 -0.0050 0.0080  -0.0290 416 TRP A O   
3527 C CB  . TRP A 416 ? 0.1213 0.1783 0.2241 0.0013  0.0090  -0.0226 416 TRP A CB  
3528 C CG  . TRP A 416 ? 0.0770 0.1378 0.1815 0.0083  0.0091  -0.0211 416 TRP A CG  
3529 C CD1 . TRP A 416 ? 0.0710 0.1495 0.1807 0.0146  0.0103  -0.0213 416 TRP A CD1 
3530 C CD2 . TRP A 416 ? 0.1310 0.1808 0.2317 0.0093  0.0076  -0.0190 416 TRP A CD2 
3531 N NE1 . TRP A 416 ? 0.0905 0.1724 0.2008 0.0201  0.0093  -0.0199 416 TRP A NE1 
3532 C CE2 . TRP A 416 ? 0.1126 0.1752 0.2167 0.0177  0.0075  -0.0184 416 TRP A CE2 
3533 C CE3 . TRP A 416 ? 0.1295 0.1620 0.2233 0.0032  0.0065  -0.0174 416 TRP A CE3 
3534 C CZ2 . TRP A 416 ? 0.1118 0.1691 0.2126 0.0217  0.0057  -0.0162 416 TRP A CZ2 
3535 C CZ3 . TRP A 416 ? 0.1196 0.1443 0.2089 0.0065  0.0053  -0.0149 416 TRP A CZ3 
3536 C CH2 . TRP A 416 ? 0.1479 0.1841 0.2405 0.0165  0.0046  -0.0144 416 TRP A CH2 
3537 N N   . ILE A 417 ? 0.1339 0.1597 0.2127 -0.0140 0.0048  -0.0303 417 ILE A N   
3538 C CA  . ILE A 417 ? 0.1400 0.1728 0.2191 -0.0242 0.0037  -0.0318 417 ILE A CA  
3539 C C   . ILE A 417 ? 0.1597 0.1689 0.2211 -0.0343 0.0011  -0.0347 417 ILE A C   
3540 O O   . ILE A 417 ? 0.1772 0.1659 0.2283 -0.0354 0.0006  -0.0335 417 ILE A O   
3541 C CB  . ILE A 417 ? 0.1272 0.1820 0.2212 -0.0292 0.0048  -0.0273 417 ILE A CB  
3542 C CG1 . ILE A 417 ? 0.1085 0.1798 0.2054 -0.0350 0.0035  -0.0287 417 ILE A CG1 
3543 C CG2 . ILE A 417 ? 0.1070 0.1560 0.1995 -0.0368 0.0048  -0.0247 417 ILE A CG2 
3544 C CD1 . ILE A 417 ? 0.1063 0.1999 0.2161 -0.0321 0.0047  -0.0246 417 ILE A CD1 
3545 N N   . GLY A 418 ? 0.1792 0.1893 0.2342 -0.0426 -0.0009 -0.0386 418 GLY A N   
3546 C CA  . GLY A 418 ? 0.2045 0.1944 0.2416 -0.0579 -0.0037 -0.0412 418 GLY A CA  
3547 C C   . GLY A 418 ? 0.3192 0.2798 0.3321 -0.0577 -0.0063 -0.0479 418 GLY A C   
3548 O O   . GLY A 418 ? 0.4917 0.4344 0.4867 -0.0738 -0.0092 -0.0507 418 GLY A O   
3549 N N   . ASN A 419 ? 0.2491 0.2037 0.2585 -0.0410 -0.0055 -0.0510 419 ASN A N   
3550 C CA  . ASN A 419 ? 0.2797 0.2095 0.2655 -0.0400 -0.0079 -0.0585 419 ASN A CA  
3551 C C   . ASN A 419 ? 0.2737 0.2299 0.2704 -0.0356 -0.0072 -0.0611 419 ASN A C   
3552 O O   . ASN A 419 ? 0.2735 0.2627 0.2938 -0.0321 -0.0048 -0.0566 419 ASN A O   
3553 C CB  . ASN A 419 ? 0.3272 0.2229 0.2916 -0.0231 -0.0080 -0.0615 419 ASN A CB  
3554 C CG  . ASN A 419 ? 0.3964 0.3137 0.3759 -0.0017 -0.0045 -0.0606 419 ASN A CG  
3555 O OD1 . ASN A 419 ? 0.3784 0.3297 0.3792 0.0000  -0.0021 -0.0589 419 ASN A OD1 
3556 N ND2 . ASN A 419 ? 0.3647 0.2611 0.3301 0.0149  -0.0046 -0.0619 419 ASN A ND2 
3557 N N   . LYS A 420 ? 0.2668 0.2049 0.2429 -0.0368 -0.0095 -0.0684 420 LYS A N   
3558 C CA  . LYS A 420 ? 0.2978 0.2591 0.2806 -0.0358 -0.0096 -0.0712 420 LYS A CA  
3559 C C   . LYS A 420 ? 0.3135 0.2999 0.3141 -0.0185 -0.0052 -0.0682 420 LYS A C   
3560 O O   . LYS A 420 ? 0.2788 0.2953 0.2967 -0.0198 -0.0041 -0.0647 420 LYS A O   
3561 C CB  . LYS A 420 ? 0.3826 0.3149 0.3359 -0.0369 -0.0126 -0.0805 420 LYS A CB  
3562 C CG  . LYS A 420 ? 0.5142 0.4688 0.4709 -0.0378 -0.0133 -0.0839 420 LYS A CG  
3563 C CD  . LYS A 420 ? 0.6252 0.5483 0.5496 -0.0437 -0.0173 -0.0938 420 LYS A CD  
3564 C CE  . LYS A 420 ? 0.6518 0.6000 0.5798 -0.0503 -0.0194 -0.0967 420 LYS A CE  
3565 N NZ  . LYS A 420 ? 0.7019 0.6228 0.5994 -0.0472 -0.0216 -0.1071 420 LYS A NZ  
3566 N N   . GLU A 421 ? 0.2812 0.2561 0.2763 -0.0026 -0.0028 -0.0692 421 GLU A N   
3567 C CA  . GLU A 421 ? 0.2436 0.2442 0.2527 0.0116  0.0015  -0.0673 421 GLU A CA  
3568 C C   . GLU A 421 ? 0.1824 0.2084 0.2164 0.0094  0.0039  -0.0586 421 GLU A C   
3569 O O   . GLU A 421 ? 0.1943 0.2458 0.2416 0.0104  0.0064  -0.0552 421 GLU A O   
3570 C CB  . GLU A 421 ? 0.2900 0.2763 0.2856 0.0301  0.0031  -0.0715 421 GLU A CB  
3571 C CG  . GLU A 421 ? 0.4328 0.3926 0.4001 0.0369  0.0012  -0.0811 421 GLU A CG  
3572 C CD  . GLU A 421 ? 0.6183 0.5318 0.5583 0.0302  -0.0034 -0.0850 421 GLU A CD  
3573 O OE1 . GLU A 421 ? 0.7158 0.6005 0.6278 0.0324  -0.0058 -0.0933 421 GLU A OE1 
3574 O OE2 . GLU A 421 ? 0.5972 0.5007 0.5406 0.0217  -0.0048 -0.0799 421 GLU A OE2 
3575 N N   . LYS A 422 ? 0.1951 0.2119 0.2325 0.0063  0.0033  -0.0550 422 LYS A N   
3576 C CA  . LYS A 422 ? 0.1320 0.1699 0.1900 0.0039  0.0053  -0.0476 422 LYS A CA  
3577 C C   . LYS A 422 ? 0.1534 0.2076 0.2217 -0.0070 0.0045  -0.0444 422 LYS A C   
3578 O O   . LYS A 422 ? 0.1412 0.2144 0.2221 -0.0058 0.0065  -0.0396 422 LYS A O   
3579 C CB  . LYS A 422 ? 0.1616 0.1861 0.2195 0.0027  0.0046  -0.0446 422 LYS A CB  
3580 C CG  . LYS A 422 ? 0.1477 0.1608 0.1971 0.0170  0.0052  -0.0464 422 LYS A CG  
3581 C CD  . LYS A 422 ? 0.1585 0.1555 0.2047 0.0151  0.0038  -0.0432 422 LYS A CD  
3582 C CE  . LYS A 422 ? 0.2132 0.1893 0.2424 0.0304  0.0027  -0.0460 422 LYS A CE  
3583 N NZ  . LYS A 422 ? 0.2012 0.2039 0.2426 0.0449  0.0052  -0.0450 422 LYS A NZ  
3584 N N   . ASN A 423 ? 0.1214 0.1681 0.1822 -0.0176 0.0012  -0.0471 423 ASN A N   
3585 C CA  . ASN A 423 ? 0.1275 0.1949 0.1977 -0.0254 -0.0001 -0.0446 423 ASN A CA  
3586 C C   . ASN A 423 ? 0.1718 0.2543 0.2434 -0.0201 0.0005  -0.0450 423 ASN A C   
3587 O O   . ASN A 423 ? 0.1476 0.2486 0.2287 -0.0199 0.0006  -0.0405 423 ASN A O   
3588 C CB  . ASN A 423 ? 0.1245 0.1863 0.1858 -0.0394 -0.0040 -0.0481 423 ASN A CB  
3589 C CG  . ASN A 423 ? 0.1691 0.2235 0.2312 -0.0482 -0.0043 -0.0455 423 ASN A CG  
3590 O OD1 . ASN A 423 ? 0.1429 0.1965 0.2131 -0.0426 -0.0018 -0.0412 423 ASN A OD1 
3591 N ND2 . ASN A 423 ? 0.1846 0.2344 0.2373 -0.0637 -0.0074 -0.0482 423 ASN A ND2 
3592 N N   . GLU A 424 ? 0.1880 0.2618 0.2481 -0.0145 0.0010  -0.0501 424 GLU A N   
3593 C CA  . GLU A 424 ? 0.1735 0.2622 0.2338 -0.0097 0.0023  -0.0500 424 GLU A CA  
3594 C C   . GLU A 424 ? 0.1376 0.2406 0.2097 -0.0043 0.0061  -0.0431 424 GLU A C   
3595 O O   . GLU A 424 ? 0.1296 0.2458 0.2046 -0.0047 0.0063  -0.0391 424 GLU A O   
3596 C CB  . GLU A 424 ? 0.1654 0.2431 0.2104 -0.0030 0.0030  -0.0571 424 GLU A CB  
3597 C CG  . GLU A 424 ? 0.2877 0.3820 0.3314 0.0018  0.0051  -0.0570 424 GLU A CG  
3598 C CD  . GLU A 424 ? 0.4092 0.5149 0.4522 -0.0055 0.0016  -0.0562 424 GLU A CD  
3599 O OE1 . GLU A 424 ? 0.4128 0.5329 0.4560 -0.0024 0.0031  -0.0533 424 GLU A OE1 
3600 O OE2 . GLU A 424 ? 0.3939 0.4959 0.4352 -0.0147 -0.0029 -0.0581 424 GLU A OE2 
3601 N N   . TYR A 425 ? 0.1321 0.2313 0.2089 0.0000  0.0087  -0.0413 425 TYR A N   
3602 C CA  . TYR A 425 ? 0.0963 0.2077 0.1822 0.0016  0.0119  -0.0349 425 TYR A CA  
3603 C C   . TYR A 425 ? 0.1243 0.2386 0.2167 -0.0034 0.0106  -0.0291 425 TYR A C   
3604 O O   . TYR A 425 ? 0.0888 0.2097 0.1815 -0.0034 0.0119  -0.0242 425 TYR A O   
3605 C CB  . TYR A 425 ? 0.1272 0.2368 0.2173 0.0059  0.0140  -0.0345 425 TYR A CB  
3606 C CG  . TYR A 425 ? 0.0791 0.1993 0.1664 0.0136  0.0172  -0.0370 425 TYR A CG  
3607 C CD1 . TYR A 425 ? 0.1038 0.2264 0.1816 0.0183  0.0179  -0.0422 425 TYR A CD1 
3608 C CD2 . TYR A 425 ? 0.0941 0.2253 0.1882 0.0167  0.0196  -0.0347 425 TYR A CD2 
3609 C CE1 . TYR A 425 ? 0.1170 0.2542 0.1925 0.0270  0.0214  -0.0448 425 TYR A CE1 
3610 C CE2 . TYR A 425 ? 0.1115 0.2597 0.2045 0.0245  0.0227  -0.0372 425 TYR A CE2 
3611 C CZ  . TYR A 425 ? 0.1017 0.2537 0.1856 0.0304  0.0239  -0.0423 425 TYR A CZ  
3612 O OH  . TYR A 425 ? 0.1032 0.2760 0.1859 0.0394  0.0275  -0.0448 425 TYR A OH  
3613 N N   . TRP A 426 ? 0.1041 0.2127 0.1998 -0.0071 0.0082  -0.0295 426 TRP A N   
3614 C CA  . TRP A 426 ? 0.0760 0.1906 0.1771 -0.0089 0.0071  -0.0248 426 TRP A CA  
3615 C C   . TRP A 426 ? 0.1175 0.2426 0.2150 -0.0081 0.0050  -0.0241 426 TRP A C   
3616 O O   . TRP A 426 ? 0.0790 0.2076 0.1757 -0.0045 0.0051  -0.0190 426 TRP A O   
3617 C CB  . TRP A 426 ? 0.0753 0.1870 0.1804 -0.0137 0.0055  -0.0257 426 TRP A CB  
3618 C CG  . TRP A 426 ? 0.0971 0.1992 0.2055 -0.0130 0.0074  -0.0242 426 TRP A CG  
3619 C CD1 . TRP A 426 ? 0.1279 0.2172 0.2325 -0.0137 0.0073  -0.0271 426 TRP A CD1 
3620 C CD2 . TRP A 426 ? 0.1020 0.2042 0.2144 -0.0108 0.0091  -0.0191 426 TRP A CD2 
3621 N NE1 . TRP A 426 ? 0.0912 0.1770 0.2002 -0.0119 0.0088  -0.0241 426 TRP A NE1 
3622 C CE2 . TRP A 426 ? 0.1151 0.2088 0.2287 -0.0110 0.0099  -0.0194 426 TRP A CE2 
3623 C CE3 . TRP A 426 ? 0.0951 0.1998 0.2061 -0.0081 0.0095  -0.0143 426 TRP A CE3 
3624 C CZ2 . TRP A 426 ? 0.1286 0.2170 0.2397 -0.0097 0.0106  -0.0146 426 TRP A CZ2 
3625 C CZ3 . TRP A 426 ? 0.1367 0.2347 0.2469 -0.0074 0.0107  -0.0107 426 TRP A CZ3 
3626 C CH2 . TRP A 426 ? 0.1604 0.2507 0.2694 -0.0088 0.0110  -0.0107 426 TRP A CH2 
3627 N N   . LYS A 427 ? 0.1021 0.2299 0.1943 -0.0109 0.0026  -0.0292 427 LYS A N   
3628 C CA  . LYS A 427 ? 0.1446 0.2847 0.2326 -0.0096 0.0000  -0.0287 427 LYS A CA  
3629 C C   . LYS A 427 ? 0.1081 0.2480 0.1904 -0.0040 0.0024  -0.0245 427 LYS A C   
3630 O O   . LYS A 427 ? 0.1290 0.2746 0.2076 0.0000  0.0010  -0.0199 427 LYS A O   
3631 C CB  . LYS A 427 ? 0.1756 0.3163 0.2563 -0.0150 -0.0029 -0.0358 427 LYS A CB  
3632 C CG  . LYS A 427 ? 0.2736 0.4216 0.3566 -0.0238 -0.0068 -0.0386 427 LYS A CG  
3633 C CD  . LYS A 427 ? 0.3900 0.5326 0.4615 -0.0320 -0.0099 -0.0462 427 LYS A CD  
3634 C CE  . LYS A 427 ? 0.5681 0.6850 0.6319 -0.0362 -0.0087 -0.0506 427 LYS A CE  
3635 N NZ  . LYS A 427 ? 0.6625 0.7626 0.7094 -0.0352 -0.0093 -0.0578 427 LYS A NZ  
3636 N N   . ILE A 428 ? 0.1123 0.2463 0.1918 -0.0034 0.0060  -0.0259 428 ILE A N   
3637 C CA  . ILE A 428 ? 0.1174 0.2533 0.1908 -0.0015 0.0091  -0.0215 428 ILE A CA  
3638 C C   . ILE A 428 ? 0.1281 0.2581 0.2018 -0.0015 0.0103  -0.0140 428 ILE A C   
3639 O O   . ILE A 428 ? 0.1223 0.2495 0.1862 -0.0002 0.0102  -0.0085 428 ILE A O   
3640 C CB  . ILE A 428 ? 0.0830 0.2205 0.1558 -0.0009 0.0132  -0.0248 428 ILE A CB  
3641 C CG1 . ILE A 428 ? 0.1311 0.2707 0.1966 0.0013  0.0122  -0.0322 428 ILE A CG1 
3642 C CG2 . ILE A 428 ? 0.1287 0.2712 0.1973 -0.0027 0.0174  -0.0190 428 ILE A CG2 
3643 C CD1 . ILE A 428 ? 0.1698 0.3092 0.2341 0.0059  0.0154  -0.0375 428 ILE A CD1 
3644 N N   . LEU A 429 ? 0.0765 0.2012 0.1583 -0.0028 0.0111  -0.0136 429 LEU A N   
3645 C CA  . LEU A 429 ? 0.0794 0.1950 0.1589 -0.0032 0.0120  -0.0076 429 LEU A CA  
3646 C C   . LEU A 429 ? 0.0918 0.2046 0.1662 0.0024  0.0087  -0.0044 429 LEU A C   
3647 O O   . LEU A 429 ? 0.1280 0.2292 0.1903 0.0047  0.0088  0.0012  429 LEU A O   
3648 C CB  . LEU A 429 ? 0.0893 0.2014 0.1782 -0.0052 0.0131  -0.0087 429 LEU A CB  
3649 C CG  . LEU A 429 ? 0.1095 0.2103 0.1947 -0.0066 0.0139  -0.0036 429 LEU A CG  
3650 C CD1 . LEU A 429 ? 0.1413 0.2389 0.2184 -0.0129 0.0168  0.0000  429 LEU A CD1 
3651 C CD2 . LEU A 429 ? 0.1252 0.2243 0.2201 -0.0074 0.0139  -0.0054 429 LEU A CD2 
3652 N N   . ILE A 430 ? 0.0884 0.2117 0.1699 0.0047  0.0055  -0.0080 430 ILE A N   
3653 C CA  . ILE A 430 ? 0.0896 0.2185 0.1681 0.0121  0.0022  -0.0056 430 ILE A CA  
3654 C C   . ILE A 430 ? 0.1073 0.2357 0.1719 0.0177  0.0005  -0.0022 430 ILE A C   
3655 O O   . ILE A 430 ? 0.1772 0.2969 0.2301 0.0262  -0.0009 0.0030  430 ILE A O   
3656 C CB  . ILE A 430 ? 0.0814 0.2290 0.1708 0.0102  -0.0007 -0.0106 430 ILE A CB  
3657 C CG1 . ILE A 430 ? 0.0822 0.2272 0.1815 0.0061  0.0010  -0.0119 430 ILE A CG1 
3658 C CG2 . ILE A 430 ? 0.0889 0.2528 0.1757 0.0189  -0.0047 -0.0089 430 ILE A CG2 
3659 C CD1 . ILE A 430 ? 0.1318 0.2880 0.2390 -0.0026 -0.0007 -0.0174 430 ILE A CD1 
3660 N N   . GLU A 431 ? 0.0936 0.2295 0.1568 0.0140  0.0002  -0.0052 431 GLU A N   
3661 C CA  . GLU A 431 ? 0.1165 0.2524 0.1652 0.0187  -0.0015 -0.0017 431 GLU A CA  
3662 C C   . GLU A 431 ? 0.2285 0.3435 0.2619 0.0179  0.0017  0.0051  431 GLU A C   
3663 O O   . GLU A 431 ? 0.2020 0.3060 0.2183 0.0248  -0.0001 0.0111  431 GLU A O   
3664 C CB  . GLU A 431 ? 0.1300 0.2776 0.1794 0.0140  -0.0021 -0.0072 431 GLU A CB  
3665 C CG  . GLU A 431 ? 0.2782 0.4289 0.3128 0.0185  -0.0042 -0.0042 431 GLU A CG  
3666 C CD  . GLU A 431 ? 0.4519 0.6140 0.4833 0.0283  -0.0101 -0.0021 431 GLU A CD  
3667 O OE1 . GLU A 431 ? 0.5281 0.6862 0.5433 0.0357  -0.0121 0.0033  431 GLU A OE1 
3668 O OE2 . GLU A 431 ? 0.3840 0.5611 0.4282 0.0288  -0.0128 -0.0056 431 GLU A OE2 
3669 N N   . ALA A 432 ? 0.1707 0.2796 0.2078 0.0091  0.0064  0.0046  432 ALA A N   
3670 C CA  . ALA A 432 ? 0.1748 0.2662 0.1966 0.0040  0.0096  0.0112  432 ALA A CA  
3671 C C   . ALA A 432 ? 0.2426 0.3120 0.2534 0.0081  0.0083  0.0164  432 ALA A C   
3672 O O   . ALA A 432 ? 0.2347 0.2823 0.2232 0.0073  0.0086  0.0231  432 ALA A O   
3673 C CB  . ALA A 432 ? 0.1496 0.2468 0.1801 -0.0064 0.0145  0.0090  432 ALA A CB  
3674 N N   . LYS A 433 ? 0.1640 0.2364 0.1873 0.0126  0.0069  0.0134  433 LYS A N   
3675 C CA  . LYS A 433 ? 0.1909 0.2421 0.2026 0.0182  0.0059  0.0173  433 LYS A CA  
3676 C C   . LYS A 433 ? 0.2218 0.2626 0.2143 0.0324  0.0020  0.0215  433 LYS A C   
3677 O O   . LYS A 433 ? 0.2426 0.2545 0.2126 0.0373  0.0014  0.0266  433 LYS A O   
3678 C CB  . LYS A 433 ? 0.1613 0.2224 0.1910 0.0203  0.0057  0.0128  433 LYS A CB  
3679 C CG  . LYS A 433 ? 0.2121 0.2551 0.2305 0.0296  0.0045  0.0153  433 LYS A CG  
3680 C CD  . LYS A 433 ? 0.2134 0.2257 0.2135 0.0218  0.0067  0.0194  433 LYS A CD  
3681 C CE  . LYS A 433 ? 0.2320 0.2228 0.2183 0.0321  0.0053  0.0207  433 LYS A CE  
3682 N NZ  . LYS A 433 ? 0.2819 0.2359 0.2431 0.0234  0.0066  0.0248  433 LYS A NZ  
3683 N N   . LYS A 434 ? 0.2501 0.3129 0.2487 0.0397  -0.0012 0.0194  434 LYS A N   
3684 C CA  . LYS A 434 ? 0.2983 0.3559 0.2786 0.0554  -0.0057 0.0235  434 LYS A CA  
3685 C C   . LYS A 434 ? 0.3123 0.3387 0.2623 0.0540  -0.0051 0.0311  434 LYS A C   
3686 O O   . LYS A 434 ? 0.4065 0.4107 0.3317 0.0679  -0.0082 0.0365  434 LYS A O   
3687 C CB  . LYS A 434 ? 0.2699 0.3610 0.2626 0.0600  -0.0094 0.0195  434 LYS A CB  
3688 C CG  . LYS A 434 ? 0.3468 0.4689 0.3647 0.0601  -0.0108 0.0128  434 LYS A CG  
3689 C CD  . LYS A 434 ? 0.4006 0.5537 0.4269 0.0601  -0.0148 0.0088  434 LYS A CD  
3690 C CE  . LYS A 434 ? 0.4142 0.5981 0.4627 0.0560  -0.0163 0.0023  434 LYS A CE  
3691 N NZ  . LYS A 434 ? 0.4504 0.6601 0.5049 0.0499  -0.0199 -0.0026 434 LYS A NZ  
3692 N N   . LYS A 435 ? 0.2475 0.2716 0.1971 0.0380  -0.0011 0.0318  435 LYS A N   
3693 C CA  . LYS A 435 ? 0.3093 0.3077 0.2303 0.0323  0.0001  0.0393  435 LYS A CA  
3694 C C   . LYS A 435 ? 0.3252 0.3002 0.2360 0.0153  0.0049  0.0425  435 LYS A C   
3695 O O   . LYS A 435 ? 0.3667 0.3244 0.2555 0.0046  0.0071  0.0485  435 LYS A O   
3696 C CB  . LYS A 435 ? 0.3780 0.3977 0.3033 0.0268  0.0011  0.0381  435 LYS A CB  
3697 C CG  . LYS A 435 ? 0.5022 0.5426 0.4309 0.0414  -0.0045 0.0359  435 LYS A CG  
3698 C CD  . LYS A 435 ? 0.6089 0.6755 0.5490 0.0341  -0.0032 0.0313  435 LYS A CD  
3699 C CE  . LYS A 435 ? 0.6658 0.7633 0.6346 0.0348  -0.0049 0.0216  435 LYS A CE  
3700 N NZ  . LYS A 435 ? 0.7339 0.8304 0.7205 0.0289  -0.0019 0.0180  435 LYS A NZ  
3701 N N   . ALA A 436 ? 0.2000 0.3285 0.2820 0.1035  -0.0153 0.1051  436 ALA A N   
3702 C CA  . ALA A 436 ? 0.2226 0.3101 0.3033 0.0965  -0.0058 0.1096  436 ALA A CA  
3703 C C   . ALA A 436 ? 0.2514 0.2872 0.3307 0.1082  -0.0006 0.1249  436 ALA A C   
3704 O O   . ALA A 436 ? 0.2943 0.3214 0.3815 0.1265  -0.0022 0.1236  436 ALA A O   
3705 C CB  . ALA A 436 ? 0.2050 0.2867 0.2963 0.0859  0.0003  0.0833  436 ALA A CB  
3706 N N   . LYS A 437 ? 0.2731 0.2737 0.3437 0.0947  0.0060  0.1378  437 LYS A N   
3707 C CA  . LYS A 437 ? 0.3611 0.3068 0.4306 0.0973  0.0113  0.1499  437 LYS A CA  
3708 C C   . LYS A 437 ? 0.3195 0.2174 0.3993 0.0796  0.0194  0.1383  437 LYS A C   
3709 O O   . LYS A 437 ? 0.3995 0.2477 0.4810 0.0796  0.0221  0.1402  437 LYS A O   
3710 C CB  . LYS A 437 ? 0.3653 0.3115 0.4155 0.0922  0.0124  0.1757  437 LYS A CB  
3711 C CG  . LYS A 437 ? 0.5140 0.4860 0.5531 0.1131  0.0033  0.1887  437 LYS A CG  
3712 C CD  . LYS A 437 ? 0.6772 0.6629 0.6923 0.1063  0.0050  0.2100  437 LYS A CD  
3713 C CE  . LYS A 437 ? 0.7103 0.7482 0.7116 0.1194  -0.0068 0.2115  437 LYS A CE  
3714 N NZ  . LYS A 437 ? 0.7264 0.7839 0.7011 0.1110  -0.0037 0.2251  437 LYS A NZ  
3715 N N   . ASN A 438 ? 0.2903 0.2065 0.3718 0.0597  0.0200  0.1167  438 ASN A N   
3716 C CA  . ASN A 438 ? 0.3389 0.2201 0.4282 0.0384  0.0239  0.1010  438 ASN A CA  
3717 C C   . ASN A 438 ? 0.2429 0.1509 0.3314 0.0292  0.0206  0.0708  438 ASN A C   
3718 O O   . ASN A 438 ? 0.2611 0.2100 0.3446 0.0363  0.0175  0.0647  438 ASN A O   
3719 C CB  . ASN A 438 ? 0.3680 0.2428 0.4582 0.0159  0.0296  0.1200  438 ASN A CB  
3720 C CG  . ASN A 438 ? 0.2569 0.1859 0.3361 0.0083  0.0295  0.1239  438 ASN A CG  
3721 O OD1 . ASN A 438 ? 0.2177 0.1729 0.2975 0.0001  0.0261  0.1019  438 ASN A OD1 
3722 N ND2 . ASN A 438 ? 0.2838 0.2278 0.3502 0.0126  0.0334  0.1522  438 ASN A ND2 
3723 N N   . ASP A 439 ? 0.3012 0.1859 0.3952 0.0119  0.0204  0.0530  439 ASP A N   
3724 C CA  . ASP A 439 ? 0.2802 0.1836 0.3696 0.0061  0.0164  0.0261  439 ASP A CA  
3725 C C   . ASP A 439 ? 0.2291 0.1746 0.3151 -0.0068 0.0145  0.0269  439 ASP A C   
3726 O O   . ASP A 439 ? 0.1774 0.1380 0.2581 -0.0109 0.0108  0.0092  439 ASP A O   
3727 C CB  . ASP A 439 ? 0.2588 0.1261 0.3533 -0.0068 0.0134  0.0050  439 ASP A CB  
3728 C CG  . ASP A 439 ? 0.3888 0.2163 0.4807 0.0106  0.0145  -0.0094 439 ASP A CG  
3729 O OD1 . ASP A 439 ? 0.4270 0.2623 0.5154 0.0347  0.0186  -0.0034 439 ASP A OD1 
3730 O OD2 . ASP A 439 ? 0.4530 0.2436 0.5478 0.0008  0.0109  -0.0292 439 ASP A OD2 
3731 N N   . TYR A 440 ? 0.1748 0.1385 0.2612 -0.0115 0.0172  0.0468  440 TYR A N   
3732 C CA  . TYR A 440 ? 0.1775 0.1795 0.2589 -0.0178 0.0157  0.0433  440 TYR A CA  
3733 C C   . TYR A 440 ? 0.1109 0.1362 0.1836 -0.0062 0.0123  0.0351  440 TYR A C   
3734 O O   . TYR A 440 ? 0.1436 0.1891 0.2127 -0.0113 0.0101  0.0260  440 TYR A O   
3735 C CB  . TYR A 440 ? 0.1360 0.1560 0.2151 -0.0224 0.0208  0.0631  440 TYR A CB  
3736 C CG  . TYR A 440 ? 0.1918 0.2100 0.2850 -0.0412 0.0256  0.0658  440 TYR A CG  
3737 C CD1 . TYR A 440 ? 0.2252 0.2660 0.3253 -0.0501 0.0229  0.0508  440 TYR A CD1 
3738 C CD2 . TYR A 440 ? 0.2992 0.2942 0.4024 -0.0501 0.0330  0.0848  440 TYR A CD2 
3739 C CE1 . TYR A 440 ? 0.2409 0.2881 0.3561 -0.0649 0.0260  0.0501  440 TYR A CE1 
3740 C CE2 . TYR A 440 ? 0.2828 0.2820 0.3989 -0.0680 0.0369  0.0830  440 TYR A CE2 
3741 C CZ  . TYR A 440 ? 0.2772 0.3054 0.3988 -0.0742 0.0329  0.0641  440 TYR A CZ  
3742 O OH  . TYR A 440 ? 0.2995 0.3375 0.4334 -0.0890 0.0363  0.0601  440 TYR A OH  
3743 N N   . ILE A 441 ? 0.1416 0.1640 0.2144 0.0093  0.0123  0.0382  441 ILE A N   
3744 C CA  . ILE A 441 ? 0.1003 0.1495 0.1722 0.0160  0.0104  0.0297  441 ILE A CA  
3745 C C   . ILE A 441 ? 0.1246 0.1686 0.1930 0.0114  0.0118  0.0118  441 ILE A C   
3746 O O   . ILE A 441 ? 0.1080 0.1728 0.1740 0.0083  0.0116  0.0065  441 ILE A O   
3747 C CB  . ILE A 441 ? 0.1133 0.1704 0.1923 0.0350  0.0104  0.0369  441 ILE A CB  
3748 C CG1 . ILE A 441 ? 0.1313 0.2290 0.2163 0.0368  0.0078  0.0323  441 ILE A CG1 
3749 C CG2 . ILE A 441 ? 0.2116 0.2405 0.2948 0.0471  0.0152  0.0283  441 ILE A CG2 
3750 C CD1 . ILE A 441 ? 0.1467 0.2710 0.2273 0.0297  0.0007  0.0381  441 ILE A CD1 
3751 N N   . LEU A 442 ? 0.1192 0.1345 0.1859 0.0103  0.0125  0.0025  442 LEU A N   
3752 C CA  . LEU A 442 ? 0.1148 0.1284 0.1714 0.0070  0.0119  -0.0145 442 LEU A CA  
3753 C C   . LEU A 442 ? 0.1060 0.1320 0.1589 -0.0066 0.0069  -0.0157 442 LEU A C   
3754 O O   . LEU A 442 ? 0.1246 0.1619 0.1670 -0.0070 0.0063  -0.0215 442 LEU A O   
3755 C CB  . LEU A 442 ? 0.1491 0.1291 0.2027 0.0083  0.0108  -0.0286 442 LEU A CB  
3756 C CG  . LEU A 442 ? 0.1883 0.1463 0.2464 0.0256  0.0161  -0.0293 442 LEU A CG  
3757 C CD1 . LEU A 442 ? 0.2300 0.1466 0.2843 0.0242  0.0135  -0.0484 442 LEU A CD1 
3758 C CD2 . LEU A 442 ? 0.1723 0.1562 0.2267 0.0423  0.0235  -0.0328 442 LEU A CD2 
3759 N N   . VAL A 443 ? 0.1142 0.1390 0.1761 -0.0163 0.0044  -0.0088 443 VAL A N   
3760 C CA  . VAL A 443 ? 0.1051 0.1461 0.1679 -0.0250 0.0004  -0.0101 443 VAL A CA  
3761 C C   . VAL A 443 ? 0.1188 0.1786 0.1754 -0.0211 0.0015  -0.0068 443 VAL A C   
3762 O O   . VAL A 443 ? 0.0905 0.1561 0.1411 -0.0220 -0.0015 -0.0112 443 VAL A O   
3763 C CB  . VAL A 443 ? 0.1026 0.1477 0.1796 -0.0345 0.0017  -0.0011 443 VAL A CB  
3764 C CG1 . VAL A 443 ? 0.0978 0.1658 0.1792 -0.0389 -0.0014 -0.0040 443 VAL A CG1 
3765 C CG2 . VAL A 443 ? 0.1313 0.1528 0.2204 -0.0439 0.0008  -0.0034 443 VAL A CG2 
3766 N N   . ALA A 444 ? 0.1051 0.1734 0.1635 -0.0167 0.0046  0.0013  444 ALA A N   
3767 C CA  . ALA A 444 ? 0.0839 0.1685 0.1401 -0.0164 0.0040  0.0016  444 ALA A CA  
3768 C C   . ALA A 444 ? 0.1249 0.2109 0.1780 -0.0152 0.0060  -0.0024 444 ALA A C   
3769 O O   . ALA A 444 ? 0.1250 0.2156 0.1771 -0.0188 0.0054  -0.0029 444 ALA A O   
3770 C CB  . ALA A 444 ? 0.1182 0.2165 0.1771 -0.0123 0.0037  0.0092  444 ALA A CB  
3771 N N   . GLU A 445 ? 0.1091 0.1874 0.1592 -0.0100 0.0094  -0.0055 445 GLU A N   
3772 C CA  . GLU A 445 ? 0.1171 0.2013 0.1616 -0.0083 0.0149  -0.0075 445 GLU A CA  
3773 C C   . GLU A 445 ? 0.0907 0.1664 0.1191 -0.0115 0.0132  -0.0100 445 GLU A C   
3774 O O   . GLU A 445 ? 0.1128 0.1929 0.1316 -0.0106 0.0193  -0.0078 445 GLU A O   
3775 C CB  . GLU A 445 ? 0.1070 0.1901 0.1516 0.0029  0.0212  -0.0118 445 GLU A CB  
3776 C CG  . GLU A 445 ? 0.1233 0.2229 0.1861 0.0103  0.0231  -0.0058 445 GLU A CG  
3777 C CD  . GLU A 445 ? 0.1417 0.2309 0.2077 0.0261  0.0270  -0.0095 445 GLU A CD  
3778 O OE1 . GLU A 445 ? 0.1172 0.1860 0.1700 0.0306  0.0298  -0.0206 445 GLU A OE1 
3779 O OE2 . GLU A 445 ? 0.1374 0.2389 0.2186 0.0359  0.0263  -0.0021 445 GLU A OE2 
3780 N N   . GLY A 446 ? 0.0916 0.1595 0.1179 -0.0144 0.0054  -0.0125 446 GLY A N   
3781 C CA  . GLY A 446 ? 0.1052 0.1696 0.1174 -0.0140 0.0007  -0.0132 446 GLY A CA  
3782 C C   . GLY A 446 ? 0.1070 0.1709 0.1154 -0.0157 0.0036  -0.0039 446 GLY A C   
3783 O O   . GLY A 446 ? 0.1030 0.1681 0.1239 -0.0201 0.0048  -0.0012 446 GLY A O   
3784 N N   . SER A 447 ? 0.1002 0.1600 0.0891 -0.0123 0.0042  0.0010  447 SER A N   
3785 C CA  . SER A 447 ? 0.1280 0.1797 0.1127 -0.0151 0.0089  0.0139  447 SER A CA  
3786 C C   . SER A 447 ? 0.1562 0.1964 0.1499 -0.0143 0.0013  0.0152  447 SER A C   
3787 O O   . SER A 447 ? 0.1430 0.1704 0.1434 -0.0195 0.0047  0.0210  447 SER A O   
3788 C CB  . SER A 447 ? 0.1393 0.1882 0.0958 -0.0093 0.0115  0.0233  447 SER A CB  
3789 O OG  . SER A 447 ? 0.1828 0.2305 0.1260 -0.0004 -0.0019 0.0204  447 SER A OG  
3790 N N   . ASP A 448 ? 0.1213 0.1669 0.1181 -0.0080 -0.0086 0.0083  448 ASP A N   
3791 C CA  . ASP A 448 ? 0.1213 0.1608 0.1264 -0.0020 -0.0146 0.0089  448 ASP A CA  
3792 C C   . ASP A 448 ? 0.1377 0.1711 0.1573 -0.0072 -0.0103 0.0041  448 ASP A C   
3793 O O   . ASP A 448 ? 0.1148 0.1304 0.1360 -0.0033 -0.0111 0.0057  448 ASP A O   
3794 C CB  . ASP A 448 ? 0.1433 0.2016 0.1581 0.0033  -0.0238 0.0009  448 ASP A CB  
3795 C CG  . ASP A 448 ? 0.1056 0.1726 0.1060 0.0069  -0.0320 0.0005  448 ASP A CG  
3796 O OD1 . ASP A 448 ? 0.1300 0.2002 0.1247 0.0006  -0.0298 -0.0060 448 ASP A OD1 
3797 O OD2 . ASP A 448 ? 0.1238 0.1941 0.1174 0.0177  -0.0415 0.0056  448 ASP A OD2 
3798 N N   . TRP A 449 ? 0.0987 0.1453 0.1274 -0.0141 -0.0070 -0.0025 449 TRP A N   
3799 C CA  . TRP A 449 ? 0.0897 0.1365 0.1275 -0.0176 -0.0057 -0.0094 449 TRP A CA  
3800 C C   . TRP A 449 ? 0.1262 0.1549 0.1645 -0.0254 -0.0033 -0.0076 449 TRP A C   
3801 O O   . TRP A 449 ? 0.1303 0.1454 0.1722 -0.0257 -0.0052 -0.0155 449 TRP A O   
3802 C CB  . TRP A 449 ? 0.1413 0.2071 0.1846 -0.0219 -0.0038 -0.0124 449 TRP A CB  
3803 C CG  . TRP A 449 ? 0.1172 0.1932 0.1622 -0.0191 -0.0043 -0.0109 449 TRP A CG  
3804 C CD1 . TRP A 449 ? 0.1223 0.2002 0.1666 -0.0208 -0.0027 -0.0086 449 TRP A CD1 
3805 C CD2 . TRP A 449 ? 0.0559 0.1405 0.1069 -0.0153 -0.0066 -0.0130 449 TRP A CD2 
3806 N NE1 . TRP A 449 ? 0.0951 0.1764 0.1442 -0.0210 -0.0048 -0.0099 449 TRP A NE1 
3807 C CE2 . TRP A 449 ? 0.0528 0.1393 0.1067 -0.0184 -0.0069 -0.0111 449 TRP A CE2 
3808 C CE3 . TRP A 449 ? 0.0633 0.1535 0.1196 -0.0085 -0.0077 -0.0168 449 TRP A CE3 
3809 C CZ2 . TRP A 449 ? 0.0821 0.1748 0.1452 -0.0189 -0.0084 -0.0111 449 TRP A CZ2 
3810 C CZ3 . TRP A 449 ? 0.0639 0.1722 0.1325 -0.0067 -0.0083 -0.0170 449 TRP A CZ3 
3811 C CH2 . TRP A 449 ? 0.1112 0.2158 0.1813 -0.0137 -0.0085 -0.0127 449 TRP A CH2 
3812 N N   . PHE A 450 ? 0.1064 0.1348 0.1425 -0.0324 0.0020  0.0016  450 PHE A N   
3813 C CA  . PHE A 450 ? 0.1589 0.1738 0.2015 -0.0447 0.0064  0.0062  450 PHE A CA  
3814 C C   . PHE A 450 ? 0.1586 0.1399 0.1923 -0.0417 0.0068  0.0163  450 PHE A C   
3815 O O   . PHE A 450 ? 0.1720 0.1292 0.2140 -0.0520 0.0082  0.0169  450 PHE A O   
3816 C CB  . PHE A 450 ? 0.1377 0.1715 0.1837 -0.0522 0.0153  0.0147  450 PHE A CB  
3817 C CG  . PHE A 450 ? 0.1328 0.1962 0.1882 -0.0503 0.0144  0.0071  450 PHE A CG  
3818 C CD1 . PHE A 450 ? 0.1545 0.2257 0.2001 -0.0389 0.0136  0.0056  450 PHE A CD1 
3819 C CD2 . PHE A 450 ? 0.1089 0.1874 0.1819 -0.0570 0.0122  0.0014  450 PHE A CD2 
3820 C CE1 . PHE A 450 ? 0.1116 0.2014 0.1654 -0.0353 0.0131  0.0015  450 PHE A CE1 
3821 C CE2 . PHE A 450 ? 0.1286 0.2236 0.2038 -0.0469 0.0094  -0.0015 450 PHE A CE2 
3822 C CZ  . PHE A 450 ? 0.1172 0.2141 0.1824 -0.0362 0.0106  -0.0004 450 PHE A CZ  
3823 N N   . TRP A 451 ? 0.1646 0.1430 0.1823 -0.0277 0.0041  0.0242  451 TRP A N   
3824 C CA  . TRP A 451 ? 0.1872 0.1351 0.1936 -0.0192 0.0025  0.0375  451 TRP A CA  
3825 C C   . TRP A 451 ? 0.2323 0.1547 0.2489 -0.0133 -0.0027 0.0272  451 TRP A C   
3826 O O   . TRP A 451 ? 0.2429 0.1270 0.2601 -0.0161 -0.0007 0.0347  451 TRP A O   
3827 C CB  . TRP A 451 ? 0.1858 0.1474 0.1752 -0.0028 -0.0042 0.0432  451 TRP A CB  
3828 C CG  . TRP A 451 ? 0.4417 0.3826 0.4108 0.0066  -0.0049 0.0640  451 TRP A CG  
3829 C CD1 . TRP A 451 ? 0.5073 0.4511 0.4534 0.0046  0.0016  0.0811  451 TRP A CD1 
3830 C CD2 . TRP A 451 ? 0.5471 0.4617 0.5137 0.0229  -0.0122 0.0722  451 TRP A CD2 
3831 N NE1 . TRP A 451 ? 0.5267 0.4472 0.4531 0.0175  -0.0016 0.1023  451 TRP A NE1 
3832 C CE2 . TRP A 451 ? 0.5227 0.4233 0.4630 0.0298  -0.0110 0.0977  451 TRP A CE2 
3833 C CE3 . TRP A 451 ? 0.5065 0.4093 0.4894 0.0351  -0.0188 0.0608  451 TRP A CE3 
3834 C CZ2 . TRP A 451 ? 0.5607 0.4326 0.4915 0.0490  -0.0179 0.1147  451 TRP A CZ2 
3835 C CZ3 . TRP A 451 ? 0.6035 0.4784 0.5803 0.0551  -0.0247 0.0744  451 TRP A CZ3 
3836 C CH2 . TRP A 451 ? 0.6862 0.5445 0.6376 0.0622  -0.0252 0.1023  451 TRP A CH2 
3837 N N   . TRP A 452 ? 0.1810 0.1225 0.2054 -0.0050 -0.0080 0.0098  452 TRP A N   
3838 C CA  . TRP A 452 ? 0.2320 0.1547 0.2628 0.0064  -0.0116 -0.0028 452 TRP A CA  
3839 C C   . TRP A 452 ? 0.2093 0.1184 0.2484 -0.0072 -0.0101 -0.0196 452 TRP A C   
3840 O O   . TRP A 452 ? 0.2421 0.1211 0.2836 -0.0004 -0.0121 -0.0314 452 TRP A O   
3841 C CB  . TRP A 452 ? 0.1929 0.1491 0.2290 0.0210  -0.0150 -0.0132 452 TRP A CB  
3842 C CG  . TRP A 452 ? 0.1907 0.1619 0.2233 0.0337  -0.0204 -0.0007 452 TRP A CG  
3843 C CD1 . TRP A 452 ? 0.1890 0.1930 0.2211 0.0299  -0.0227 0.0015  452 TRP A CD1 
3844 C CD2 . TRP A 452 ? 0.2021 0.1557 0.2309 0.0526  -0.0263 0.0102  452 TRP A CD2 
3845 N NE1 . TRP A 452 ? 0.1760 0.1880 0.2040 0.0431  -0.0311 0.0105  452 TRP A NE1 
3846 C CE2 . TRP A 452 ? 0.1973 0.1818 0.2229 0.0588  -0.0339 0.0177  452 TRP A CE2 
3847 C CE3 . TRP A 452 ? 0.2655 0.1781 0.2934 0.0660  -0.0271 0.0141  452 TRP A CE3 
3848 C CZ2 . TRP A 452 ? 0.2169 0.2005 0.2377 0.0789  -0.0437 0.0300  452 TRP A CZ2 
3849 C CZ3 . TRP A 452 ? 0.3509 0.2569 0.3743 0.0882  -0.0351 0.0293  452 TRP A CZ3 
3850 C CH2 . TRP A 452 ? 0.2577 0.2030 0.2772 0.0951  -0.0441 0.0376  452 TRP A CH2 
3851 N N   . GLN A 453 ? 0.2044 0.1358 0.2484 -0.0248 -0.0080 -0.0227 453 GLN A N   
3852 C CA  . GLN A 453 ? 0.2528 0.1825 0.3048 -0.0374 -0.0106 -0.0416 453 GLN A CA  
3853 C C   . GLN A 453 ? 0.2773 0.1639 0.3374 -0.0518 -0.0100 -0.0406 453 GLN A C   
3854 O O   . GLN A 453 ? 0.3147 0.1860 0.3764 -0.0603 -0.0041 -0.0193 453 GLN A O   
3855 C CB  . GLN A 453 ? 0.2381 0.2084 0.2959 -0.0496 -0.0105 -0.0424 453 GLN A CB  
3856 C CG  . GLN A 453 ? 0.3772 0.3535 0.4463 -0.0666 -0.0159 -0.0585 453 GLN A CG  
3857 C CD  . GLN A 453 ? 0.3141 0.2965 0.3740 -0.0586 -0.0230 -0.0828 453 GLN A CD  
3858 O OE1 . GLN A 453 ? 0.3096 0.2877 0.3576 -0.0403 -0.0212 -0.0872 453 GLN A OE1 
3859 N NE2 . GLN A 453 ? 0.2939 0.2906 0.3538 -0.0676 -0.0301 -0.0923 453 GLN A NE2 
3860 N N   . GLY A 454 ? 0.3834 0.2483 0.4473 -0.0550 -0.0155 -0.0639 454 GLY A N   
3861 C CA  . GLY A 454 ? 0.4630 0.2853 0.5342 -0.0721 -0.0157 -0.0639 454 GLY A CA  
3862 C C   . GLY A 454 ? 0.6390 0.4103 0.7058 -0.0634 -0.0105 -0.0436 454 GLY A C   
3863 O O   . GLY A 454 ? 0.6284 0.3781 0.6958 -0.0799 -0.0051 -0.0248 454 GLY A O   
3864 N N   . GLU A 455 ? 0.6921 0.4506 0.7507 -0.0354 -0.0120 -0.0440 455 GLU A N   
3865 C CA  . GLU A 455 ? 0.7457 0.4551 0.7969 -0.0194 -0.0100 -0.0258 455 GLU A CA  
3866 C C   . GLU A 455 ? 0.8210 0.4949 0.8641 -0.0015 -0.0121 -0.0461 455 GLU A C   
3867 O O   . GLU A 455 ? 0.9235 0.5462 0.9582 0.0009  -0.0088 -0.0348 455 GLU A O   
3868 C CB  . GLU A 455 ? 0.6782 0.4137 0.7182 0.0033  -0.0101 -0.0037 455 GLU A CB  
3869 C CG  . GLU A 455 ? 0.6100 0.3796 0.6439 -0.0112 -0.0048 0.0191  455 GLU A CG  
3870 C CD  . GLU A 455 ? 0.7171 0.4514 0.7505 -0.0301 0.0035  0.0442  455 GLU A CD  
3871 O OE1 . GLU A 455 ? 0.6072 0.3710 0.6412 -0.0481 0.0109  0.0556  455 GLU A OE1 
3872 O OE2 . GLU A 455 ? 0.7591 0.4407 0.7873 -0.0258 0.0040  0.0523  455 GLU A OE2 
3873 N N   . GLU A 456 ? 0.8519 0.5507 0.8943 0.0127  -0.0153 -0.0743 456 GLU A N   
3874 C CA  . GLU A 456 ? 0.8910 0.6481 0.9377 0.0189  -0.0179 -0.0849 456 GLU A CA  
3875 C C   . GLU A 456 ? 0.9060 0.6857 0.9505 0.0479  -0.0170 -0.0703 456 GLU A C   
3876 O O   . GLU A 456 ? 0.9046 0.7187 0.9474 0.0435  -0.0164 -0.0499 456 GLU A O   
3877 C CB  . GLU A 456 ? 0.9150 0.6964 0.9533 0.0189  -0.0188 -0.1161 456 GLU A CB  
3878 N N   . LYS A 457 ? 0.9373 0.7049 0.9828 0.0772  -0.0169 -0.0792 457 LYS A N   
3879 C CA  . LYS A 457 ? 0.9067 0.6527 0.9460 0.0890  -0.0121 -0.1005 457 LYS A CA  
3880 C C   . LYS A 457 ? 0.9470 0.6921 0.9927 0.1210  -0.0100 -0.0880 457 LYS A C   
3881 O O   . LYS A 457 ? 1.0655 0.7684 1.1112 0.1274  -0.0101 -0.0679 457 LYS A O   
3882 C CB  . LYS A 457 ? 0.8794 0.5650 0.9110 0.0717  -0.0108 -0.1061 457 LYS A CB  
3883 N N   . ALA A 458 ? 0.8120 0.6085 0.8645 0.1394  -0.0069 -0.0976 458 ALA A N   
3884 C CA  . ALA A 458 ? 0.8126 0.6360 0.8797 0.1668  -0.0060 -0.0859 458 ALA A CA  
3885 C C   . ALA A 458 ? 0.7474 0.6429 0.8227 0.1677  -0.0025 -0.0936 458 ALA A C   
3886 O O   . ALA A 458 ? 0.6653 0.5822 0.7333 0.1484  -0.0020 -0.1011 458 ALA A O   
3887 C CB  . ALA A 458 ? 0.7753 0.5909 0.8466 0.1714  -0.0146 -0.0545 458 ALA A CB  
3888 N N   . PRO A 459 ? 0.6934 0.6285 0.7857 0.1872  0.0009  -0.0906 459 PRO A N   
3889 C CA  . PRO A 459 ? 0.6710 0.6737 0.7734 0.1818  0.0063  -0.0931 459 PRO A CA  
3890 C C   . PRO A 459 ? 0.6892 0.7181 0.7925 0.1616  -0.0003 -0.0795 459 PRO A C   
3891 O O   . PRO A 459 ? 0.7173 0.7378 0.8236 0.1613  -0.0107 -0.0620 459 PRO A O   
3892 C CB  . PRO A 459 ? 0.6372 0.6727 0.7643 0.2033  0.0076  -0.0857 459 PRO A CB  
3893 C CG  . PRO A 459 ? 0.6447 0.6332 0.7743 0.2215  0.0003  -0.0757 459 PRO A CG  
3894 C CD  . PRO A 459 ? 0.7006 0.6213 0.8070 0.2133  0.0009  -0.0840 459 PRO A CD  
3895 N N   . PHE A 460 ? 0.6881 0.7459 0.7855 0.1446  0.0061  -0.0872 460 PHE A N   
3896 C CA  . PHE A 460 ? 0.5048 0.5988 0.6067 0.1247  0.0049  -0.0768 460 PHE A CA  
3897 C C   . PHE A 460 ? 0.4452 0.5159 0.5340 0.1082  0.0000  -0.0775 460 PHE A C   
3898 O O   . PHE A 460 ? 0.4739 0.5698 0.5628 0.0889  0.0011  -0.0687 460 PHE A O   
3899 C CB  . PHE A 460 ? 0.4030 0.5254 0.5244 0.1248  -0.0026 -0.0589 460 PHE A CB  
3900 C CG  . PHE A 460 ? 0.3225 0.4706 0.4636 0.1410  0.0004  -0.0581 460 PHE A CG  
3901 C CD1 . PHE A 460 ? 0.3285 0.4966 0.4731 0.1467  0.0139  -0.0693 460 PHE A CD1 
3902 C CD2 . PHE A 460 ? 0.3261 0.4802 0.4817 0.1519  -0.0105 -0.0461 460 PHE A CD2 
3903 C CE1 . PHE A 460 ? 0.3857 0.5806 0.5526 0.1632  0.0179  -0.0693 460 PHE A CE1 
3904 C CE2 . PHE A 460 ? 0.3227 0.5046 0.5014 0.1681  -0.0084 -0.0463 460 PHE A CE2 
3905 C CZ  . PHE A 460 ? 0.3310 0.5335 0.5174 0.1740  0.0065  -0.0582 460 PHE A CZ  
3906 N N   . VAL A 461 ? 0.4149 0.4314 0.4889 0.1055  -0.0043 -0.0812 461 VAL A N   
3907 C CA  . VAL A 461 ? 0.4514 0.4505 0.5114 0.0787  -0.0064 -0.0770 461 VAL A CA  
3908 C C   . VAL A 461 ? 0.4025 0.4303 0.4547 0.0679  -0.0003 -0.0894 461 VAL A C   
3909 O O   . VAL A 461 ? 0.3748 0.4140 0.4220 0.0487  -0.0012 -0.0814 461 VAL A O   
3910 C CB  . VAL A 461 ? 0.5482 0.4883 0.5994 0.0733  -0.0104 -0.0801 461 VAL A CB  
3911 C CG1 . VAL A 461 ? 0.5680 0.4845 0.6139 0.0833  -0.0081 -0.1077 461 VAL A CG1 
3912 C CG2 . VAL A 461 ? 0.5659 0.5005 0.6105 0.0450  -0.0120 -0.0727 461 VAL A CG2 
3913 N N   . GLU A 462 ? 0.2300 0.2722 0.2792 0.0829  0.0066  -0.1083 462 GLU A N   
3914 C CA  . GLU A 462 ? 0.2238 0.2985 0.2600 0.0748  0.0128  -0.1157 462 GLU A CA  
3915 C C   . GLU A 462 ? 0.2442 0.3634 0.2910 0.0666  0.0182  -0.0959 462 GLU A C   
3916 O O   . GLU A 462 ? 0.2138 0.3498 0.2497 0.0532  0.0203  -0.0907 462 GLU A O   
3917 C CB  . GLU A 462 ? 0.3031 0.3821 0.3272 0.0873  0.0192  -0.1295 462 GLU A CB  
3918 C CG  . GLU A 462 ? 0.5759 0.6782 0.6149 0.1051  0.0278  -0.1241 462 GLU A CG  
3919 C CD  . GLU A 462 ? 0.6577 0.7326 0.7133 0.1212  0.0231  -0.1219 462 GLU A CD  
3920 O OE1 . GLU A 462 ? 0.6430 0.7447 0.7173 0.1330  0.0275  -0.1131 462 GLU A OE1 
3921 O OE2 . GLU A 462 ? 0.6527 0.6793 0.7037 0.1210  0.0149  -0.1267 462 GLU A OE2 
3922 N N   . VAL A 463 ? 0.1412 0.2749 0.2088 0.0718  0.0181  -0.0824 463 VAL A N   
3923 C CA  . VAL A 463 ? 0.1151 0.2781 0.1930 0.0576  0.0206  -0.0637 463 VAL A CA  
3924 C C   . VAL A 463 ? 0.1247 0.2779 0.2019 0.0413  0.0139  -0.0543 463 VAL A C   
3925 O O   . VAL A 463 ? 0.1131 0.2756 0.1859 0.0269  0.0167  -0.0436 463 VAL A O   
3926 C CB  . VAL A 463 ? 0.1406 0.3199 0.2406 0.0639  0.0195  -0.0551 463 VAL A CB  
3927 C CG1 . VAL A 463 ? 0.1941 0.3931 0.3048 0.0459  0.0215  -0.0397 463 VAL A CG1 
3928 C CG2 . VAL A 463 ? 0.1420 0.3335 0.2459 0.0812  0.0276  -0.0640 463 VAL A CG2 
3929 N N   . PHE A 464 ? 0.1185 0.2381 0.1919 0.0407  0.0043  -0.0522 464 PHE A N   
3930 C CA  . PHE A 464 ? 0.1193 0.2242 0.1858 0.0246  -0.0008 -0.0420 464 PHE A CA  
3931 C C   . PHE A 464 ? 0.1351 0.2370 0.1883 0.0140  0.0016  -0.0454 464 PHE A C   
3932 O O   . PHE A 464 ? 0.1209 0.2288 0.1729 0.0031  0.0015  -0.0364 464 PHE A O   
3933 C CB  . PHE A 464 ? 0.1709 0.2429 0.2323 0.0265  -0.0080 -0.0375 464 PHE A CB  
3934 C CG  . PHE A 464 ? 0.1073 0.1866 0.1778 0.0370  -0.0141 -0.0301 464 PHE A CG  
3935 C CD1 . PHE A 464 ? 0.1432 0.2213 0.2220 0.0568  -0.0159 -0.0340 464 PHE A CD1 
3936 C CD2 . PHE A 464 ? 0.1310 0.2201 0.2015 0.0293  -0.0193 -0.0211 464 PHE A CD2 
3937 C CE1 . PHE A 464 ? 0.1601 0.2518 0.2489 0.0689  -0.0245 -0.0263 464 PHE A CE1 
3938 C CE2 . PHE A 464 ? 0.1075 0.2089 0.1846 0.0391  -0.0285 -0.0164 464 PHE A CE2 
3939 C CZ  . PHE A 464 ? 0.1070 0.2125 0.1943 0.0589  -0.0319 -0.0176 464 PHE A CZ  
3940 N N   . ASP A 465 ? 0.1276 0.2210 0.1709 0.0185  0.0023  -0.0599 465 ASP A N   
3941 C CA  . ASP A 465 ? 0.1222 0.2197 0.1528 0.0094  0.0008  -0.0652 465 ASP A CA  
3942 C C   . ASP A 465 ? 0.1150 0.2465 0.1396 0.0098  0.0074  -0.0587 465 ASP A C   
3943 O O   . ASP A 465 ? 0.1372 0.2767 0.1562 0.0018  0.0053  -0.0503 465 ASP A O   
3944 C CB  . ASP A 465 ? 0.1348 0.2138 0.1554 0.0133  -0.0026 -0.0870 465 ASP A CB  
3945 C CG  . ASP A 465 ? 0.1709 0.2633 0.1774 0.0055  -0.0072 -0.0966 465 ASP A CG  
3946 O OD1 . ASP A 465 ? 0.1829 0.2682 0.1946 -0.0086 -0.0145 -0.0936 465 ASP A OD1 
3947 O OD2 . ASP A 465 ? 0.2016 0.3164 0.1920 0.0144  -0.0034 -0.1066 465 ASP A OD2 
3948 N N   . LYS A 466 ? 0.1094 0.2624 0.1367 0.0200  0.0165  -0.0600 466 LYS A N   
3949 C CA  . LYS A 466 ? 0.0972 0.2777 0.1200 0.0178  0.0250  -0.0465 466 LYS A CA  
3950 C C   . LYS A 466 ? 0.0869 0.2616 0.1214 0.0056  0.0236  -0.0260 466 LYS A C   
3951 O O   . LYS A 466 ? 0.1328 0.3116 0.1590 0.0004  0.0252  -0.0133 466 LYS A O   
3952 C CB  . LYS A 466 ? 0.1319 0.3258 0.1596 0.0269  0.0334  -0.0466 466 LYS A CB  
3953 C CG  . LYS A 466 ? 0.1201 0.3319 0.1463 0.0210  0.0424  -0.0281 466 LYS A CG  
3954 C CD  . LYS A 466 ? 0.2295 0.4614 0.2627 0.0294  0.0534  -0.0297 466 LYS A CD  
3955 C CE  . LYS A 466 ? 0.4678 0.7189 0.4850 0.0283  0.0641  -0.0188 466 LYS A CE  
3956 N NZ  . LYS A 466 ? 0.5422 0.8037 0.5795 0.0172  0.0738  0.0010  466 LYS A NZ  
3957 N N   . LEU A 467 ? 0.0796 0.2413 0.1309 0.0030  0.0196  -0.0235 467 LEU A N   
3958 C CA  . LEU A 467 ? 0.0706 0.2186 0.1292 -0.0071 0.0169  -0.0104 467 LEU A CA  
3959 C C   . LEU A 467 ? 0.0958 0.2305 0.1457 -0.0118 0.0123  -0.0075 467 LEU A C   
3960 O O   . LEU A 467 ? 0.1282 0.2613 0.1768 -0.0160 0.0143  0.0034  467 LEU A O   
3961 C CB  . LEU A 467 ? 0.0502 0.1905 0.1231 -0.0070 0.0112  -0.0123 467 LEU A CB  
3962 C CG  . LEU A 467 ? 0.0630 0.2219 0.1522 -0.0040 0.0152  -0.0116 467 LEU A CG  
3963 C CD1 . LEU A 467 ? 0.0789 0.2373 0.1800 0.0003  0.0061  -0.0152 467 LEU A CD1 
3964 C CD2 . LEU A 467 ? 0.0907 0.2542 0.1909 -0.0150 0.0207  -0.0013 467 LEU A CD2 
3965 N N   . PHE A 468 ? 0.0759 0.2027 0.1236 -0.0110 0.0067  -0.0162 468 PHE A N   
3966 C CA  . PHE A 468 ? 0.0929 0.2099 0.1359 -0.0152 0.0028  -0.0131 468 PHE A CA  
3967 C C   . PHE A 468 ? 0.0944 0.2298 0.1300 -0.0145 0.0037  -0.0084 468 PHE A C   
3968 O O   . PHE A 468 ? 0.1163 0.2501 0.1530 -0.0150 0.0037  0.0027  468 PHE A O   
3969 C CB  . PHE A 468 ? 0.0817 0.1893 0.1253 -0.0173 -0.0020 -0.0226 468 PHE A CB  
3970 C CG  . PHE A 468 ? 0.0459 0.1506 0.0883 -0.0218 -0.0046 -0.0199 468 PHE A CG  
3971 C CD1 . PHE A 468 ? 0.0962 0.1909 0.1410 -0.0220 -0.0029 -0.0116 468 PHE A CD1 
3972 C CD2 . PHE A 468 ? 0.0718 0.1866 0.1116 -0.0243 -0.0091 -0.0278 468 PHE A CD2 
3973 C CE1 . PHE A 468 ? 0.1034 0.2021 0.1520 -0.0235 -0.0035 -0.0095 468 PHE A CE1 
3974 C CE2 . PHE A 468 ? 0.1309 0.2473 0.1749 -0.0275 -0.0117 -0.0243 468 PHE A CE2 
3975 C CZ  . PHE A 468 ? 0.1262 0.2364 0.1766 -0.0264 -0.0080 -0.0146 468 PHE A CZ  
3976 N N   . ARG A 469 ? 0.0959 0.2456 0.1200 -0.0105 0.0038  -0.0171 469 ARG A N   
3977 C CA  . ARG A 469 ? 0.0920 0.2604 0.1011 -0.0075 0.0019  -0.0126 469 ARG A CA  
3978 C C   . ARG A 469 ? 0.1267 0.3053 0.1323 -0.0054 0.0108  0.0077  469 ARG A C   
3979 O O   . ARG A 469 ? 0.1352 0.3216 0.1316 -0.0021 0.0085  0.0208  469 ARG A O   
3980 C CB  . ARG A 469 ? 0.1327 0.3124 0.1247 -0.0030 -0.0009 -0.0310 469 ARG A CB  
3981 C CG  . ARG A 469 ? 0.1469 0.3116 0.1447 -0.0091 -0.0114 -0.0494 469 ARG A CG  
3982 C CD  . ARG A 469 ? 0.2019 0.3681 0.1843 -0.0050 -0.0146 -0.0712 469 ARG A CD  
3983 N NE  . ARG A 469 ? 0.1596 0.3005 0.1521 -0.0134 -0.0226 -0.0863 469 ARG A NE  
3984 C CZ  . ARG A 469 ? 0.1792 0.3210 0.1743 -0.0207 -0.0314 -0.0899 469 ARG A CZ  
3985 N NH1 . ARG A 469 ? 0.1631 0.3304 0.1509 -0.0178 -0.0350 -0.0809 469 ARG A NH1 
3986 N NH2 . ARG A 469 ? 0.1808 0.2980 0.1863 -0.0310 -0.0372 -0.1019 469 ARG A NH2 
3987 N N   . SER A 470 ? 0.1392 0.3158 0.1539 -0.0075 0.0198  0.0120  470 SER A N   
3988 C CA  . SER A 470 ? 0.1192 0.2939 0.1356 -0.0100 0.0274  0.0319  470 SER A CA  
3989 C C   . SER A 470 ? 0.1037 0.2591 0.1332 -0.0155 0.0259  0.0444  470 SER A C   
3990 O O   . SER A 470 ? 0.1388 0.2915 0.1643 -0.0147 0.0299  0.0641  470 SER A O   
3991 C CB  . SER A 470 ? 0.1604 0.3354 0.1892 -0.0129 0.0349  0.0300  470 SER A CB  
3992 O OG  . SER A 470 ? 0.1974 0.3915 0.2143 -0.0048 0.0385  0.0197  470 SER A OG  
3993 N N   . PHE A 471 ? 0.1081 0.2466 0.1514 -0.0193 0.0204  0.0337  471 PHE A N   
3994 C CA  . PHE A 471 ? 0.1025 0.2215 0.1562 -0.0220 0.0184  0.0400  471 PHE A CA  
3995 C C   . PHE A 471 ? 0.1248 0.2433 0.1689 -0.0126 0.0135  0.0455  471 PHE A C   
3996 O O   . PHE A 471 ? 0.1457 0.2493 0.1923 -0.0087 0.0146  0.0587  471 PHE A O   
3997 C CB  . PHE A 471 ? 0.0675 0.1741 0.1302 -0.0253 0.0130  0.0248  471 PHE A CB  
3998 C CG  . PHE A 471 ? 0.1016 0.2042 0.1736 -0.0308 0.0136  0.0185  471 PHE A CG  
3999 C CD1 . PHE A 471 ? 0.1397 0.2407 0.2242 -0.0395 0.0190  0.0268  471 PHE A CD1 
4000 C CD2 . PHE A 471 ? 0.1177 0.2194 0.1884 -0.0272 0.0086  0.0067  471 PHE A CD2 
4001 C CE1 . PHE A 471 ? 0.1710 0.2764 0.2700 -0.0451 0.0187  0.0194  471 PHE A CE1 
4002 C CE2 . PHE A 471 ? 0.0967 0.2031 0.1800 -0.0296 0.0072  0.0034  471 PHE A CE2 
4003 C CZ  . PHE A 471 ? 0.1545 0.2652 0.2542 -0.0386 0.0117  0.0081  471 PHE A CZ  
4004 N N   . VAL A 472 ? 0.0766 0.2116 0.1128 -0.0086 0.0072  0.0351  472 VAL A N   
4005 C CA  . VAL A 472 ? 0.0922 0.2385 0.1250 -0.0004 0.0002  0.0389  472 VAL A CA  
4006 C C   . VAL A 472 ? 0.1076 0.2647 0.1259 0.0078  0.0011  0.0581  472 VAL A C   
4007 O O   . VAL A 472 ? 0.1566 0.3113 0.1766 0.0178  -0.0020 0.0719  472 VAL A O   
4008 C CB  . VAL A 472 ? 0.1521 0.3161 0.1830 -0.0031 -0.0077 0.0217  472 VAL A CB  
4009 C CG1 . VAL A 472 ? 0.2090 0.3964 0.2361 0.0039  -0.0171 0.0244  472 VAL A CG1 
4010 C CG2 . VAL A 472 ? 0.1362 0.2813 0.1786 -0.0094 -0.0071 0.0102  472 VAL A CG2 
4011 N N   . ARG A 473 ? 0.1361 0.3064 0.1389 0.0060  0.0065  0.0610  473 ARG A N   
4012 C CA  . ARG A 473 ? 0.1720 0.3547 0.1548 0.0139  0.0097  0.0830  473 ARG A CA  
4013 C C   . ARG A 473 ? 0.1881 0.3426 0.1806 0.0130  0.0185  0.1078  473 ARG A C   
4014 O O   . ARG A 473 ? 0.2082 0.3560 0.1949 0.0240  0.0159  0.1267  473 ARG A O   
4015 C CB  . ARG A 473 ? 0.2482 0.4475 0.2164 0.0119  0.0166  0.0761  473 ARG A CB  
4016 C CG  . ARG A 473 ? 0.3730 0.5839 0.3210 0.0205  0.0187  0.0901  473 ARG A CG  
4017 C CD  . ARG A 473 ? 0.4900 0.7211 0.4220 0.0219  0.0221  0.0740  473 ARG A CD  
4018 N NE  . ARG A 473 ? 0.6263 0.8521 0.5707 0.0141  0.0335  0.0679  473 ARG A NE  
4019 C CZ  . ARG A 473 ? 0.6517 0.8797 0.6028 0.0122  0.0317  0.0442  473 ARG A CZ  
4020 N NH1 . ARG A 473 ? 0.5676 0.7925 0.5327 0.0078  0.0413  0.0409  473 ARG A NH1 
4021 N NH2 . ARG A 473 ? 0.6766 0.9084 0.6225 0.0147  0.0200  0.0236  473 ARG A NH2 
4022 N N   . ARG A 474 ? 0.1676 0.3022 0.1785 -0.0002 0.0273  0.1049  474 ARG A N   
4023 C CA  . ARG A 474 ? 0.1988 0.3018 0.2223 -0.0060 0.0354  0.1246  474 ARG A CA  
4024 C C   . ARG A 474 ? 0.2227 0.2954 0.2557 0.0031  0.0284  0.1261  474 ARG A C   
4025 O O   . ARG A 474 ? 0.2234 0.2674 0.2585 0.0069  0.0325  0.1478  474 ARG A O   
4026 C CB  . ARG A 474 ? 0.2061 0.2994 0.2509 -0.0234 0.0411  0.1121  474 ARG A CB  
4027 C CG  . ARG A 474 ? 0.2883 0.3466 0.3489 -0.0342 0.0470  0.1239  474 ARG A CG  
4028 C CD  . ARG A 474 ? 0.4526 0.5123 0.5019 -0.0354 0.0564  0.1438  474 ARG A CD  
4029 N NE  . ARG A 474 ? 0.5583 0.5821 0.6242 -0.0495 0.0620  0.1527  474 ARG A NE  
4030 C CZ  . ARG A 474 ? 0.7308 0.7141 0.7978 -0.0450 0.0603  0.1656  474 ARG A CZ  
4031 N NH1 . ARG A 474 ? 0.7248 0.7035 0.7790 -0.0245 0.0534  0.1725  474 ARG A NH1 
4032 N NH2 . ARG A 474 ? 0.8265 0.7740 0.9078 -0.0603 0.0647  0.1698  474 ARG A NH2 
4033 N N   . ALA A 475 ? 0.1675 0.2453 0.2065 0.0079  0.0192  0.1041  475 ALA A N   
4034 C CA  . ALA A 475 ? 0.1734 0.2293 0.2225 0.0194  0.0149  0.1021  475 ALA A CA  
4035 C C   . ALA A 475 ? 0.2086 0.2698 0.2499 0.0392  0.0107  0.1230  475 ALA A C   
4036 O O   . ALA A 475 ? 0.2666 0.3035 0.3177 0.0525  0.0098  0.1276  475 ALA A O   
4037 C CB  . ALA A 475 ? 0.1740 0.2452 0.2297 0.0204  0.0090  0.0778  475 ALA A CB  
4038 N N   . GLN A 476 ? 0.1949 0.2882 0.2173 0.0440  0.0072  0.1349  476 GLN A N   
4039 C CA  . GLN A 476 ? 0.2228 0.3286 0.2362 0.0630  -0.0001 0.1492  476 GLN A CA  
4040 C C   . GLN A 476 ? 0.3460 0.4298 0.3458 0.0646  0.0074  0.1731  476 GLN A C   
4041 O O   . GLN A 476 ? 0.3780 0.4710 0.3660 0.0790  0.0015  0.1843  476 GLN A O   
4042 C CB  . GLN A 476 ? 0.2644 0.4176 0.2661 0.0639  -0.0107 0.1337  476 GLN A CB  
4043 C CG  . GLN A 476 ? 0.2592 0.4308 0.2786 0.0588  -0.0176 0.1082  476 GLN A CG  
4044 C CD  . GLN A 476 ? 0.2772 0.4825 0.2870 0.0516  -0.0258 0.0883  476 GLN A CD  
4045 O OE1 . GLN A 476 ? 0.2621 0.4872 0.2705 0.0586  -0.0349 0.0854  476 GLN A OE1 
4046 N NE2 . GLN A 476 ? 0.1826 0.3914 0.1869 0.0379  -0.0233 0.0736  476 GLN A NE2 
4047 N N   . GLU A 477 ? 0.3196 0.3755 0.3228 0.0489  0.0197  0.1806  477 GLU A N   
4048 C CA  . GLU A 477 ? 0.4221 0.4559 0.4155 0.0460  0.0285  0.2029  477 GLU A CA  
4049 C C   . GLU A 477 ? 0.4331 0.4101 0.4448 0.0403  0.0344  0.2097  477 GLU A C   
4050 O O   . GLU A 477 ? 0.4612 0.4090 0.4665 0.0426  0.0386  0.2302  477 GLU A O   
4051 C CB  . GLU A 477 ? 0.4608 0.5149 0.4449 0.0294  0.0386  0.2026  477 GLU A CB  
4052 C CG  . GLU A 477 ? 0.5221 0.6260 0.4889 0.0334  0.0328  0.1872  477 GLU A CG  
4053 C CD  . GLU A 477 ? 0.6618 0.7834 0.6231 0.0200  0.0437  0.1818  477 GLU A CD  
4054 O OE1 . GLU A 477 ? 0.6991 0.8546 0.6396 0.0258  0.0414  0.1740  477 GLU A OE1 
4055 O OE2 . GLU A 477 ? 0.7142 0.8165 0.6935 0.0041  0.0539  0.1827  477 GLU A OE2 
4056 N N   . LYS B 2   ? 0.4739 0.5677 0.3239 -0.0815 0.0092  -0.0358 2   LYS B N   
4057 C CA  . LYS B 2   ? 0.4165 0.4838 0.2768 -0.0761 0.0139  -0.0383 2   LYS B CA  
4058 C C   . LYS B 2   ? 0.3510 0.4144 0.2223 -0.0720 0.0112  -0.0385 2   LYS B C   
4059 O O   . LYS B 2   ? 0.4157 0.4848 0.2862 -0.0799 0.0116  -0.0455 2   LYS B O   
4060 C CB  . LYS B 2   ? 0.4838 0.5367 0.3404 -0.0852 0.0229  -0.0501 2   LYS B CB  
4061 C CG  . LYS B 2   ? 0.5368 0.5653 0.4039 -0.0790 0.0283  -0.0517 2   LYS B CG  
4062 C CD  . LYS B 2   ? 0.6626 0.6782 0.5335 -0.0845 0.0340  -0.0621 2   LYS B CD  
4063 C CE  . LYS B 2   ? 0.6915 0.7058 0.5511 -0.0966 0.0416  -0.0732 2   LYS B CE  
4064 N NZ  . LYS B 2   ? 0.7316 0.7279 0.5948 -0.1004 0.0491  -0.0827 2   LYS B NZ  
4065 N N   . LYS B 3   ? 0.2513 0.3048 0.1321 -0.0604 0.0088  -0.0310 3   LYS B N   
4066 C CA  . LYS B 3   ? 0.2395 0.2903 0.1302 -0.0555 0.0059  -0.0299 3   LYS B CA  
4067 C C   . LYS B 3   ? 0.2713 0.2994 0.1708 -0.0538 0.0108  -0.0348 3   LYS B C   
4068 O O   . LYS B 3   ? 0.3093 0.3234 0.2097 -0.0526 0.0154  -0.0358 3   LYS B O   
4069 C CB  . LYS B 3   ? 0.3145 0.3703 0.2092 -0.0434 0.0000  -0.0183 3   LYS B CB  
4070 C CG  . LYS B 3   ? 0.3877 0.4664 0.2746 -0.0420 -0.0049 -0.0107 3   LYS B CG  
4071 C CD  . LYS B 3   ? 0.4606 0.5611 0.3485 -0.0439 -0.0098 -0.0105 3   LYS B CD  
4072 C CE  . LYS B 3   ? 0.4881 0.6139 0.3695 -0.0406 -0.0151 -0.0012 3   LYS B CE  
4073 N NZ  . LYS B 3   ? 0.5743 0.7261 0.4500 -0.0520 -0.0175 -0.0062 3   LYS B NZ  
4074 N N   . LEU B 4   ? 0.2163 0.2423 0.1223 -0.0538 0.0099  -0.0374 4   LEU B N   
4075 C CA  . LEU B 4   ? 0.2265 0.2345 0.1427 -0.0485 0.0121  -0.0380 4   LEU B CA  
4076 C C   . LEU B 4   ? 0.2502 0.2603 0.1728 -0.0381 0.0063  -0.0295 4   LEU B C   
4077 O O   . LEU B 4   ? 0.2343 0.2588 0.1564 -0.0367 0.0015  -0.0264 4   LEU B O   
4078 C CB  . LEU B 4   ? 0.2167 0.2194 0.1355 -0.0547 0.0154  -0.0456 4   LEU B CB  
4079 C CG  . LEU B 4   ? 0.2359 0.2221 0.1650 -0.0493 0.0175  -0.0457 4   LEU B CG  
4080 C CD1 . LEU B 4   ? 0.2856 0.2601 0.2141 -0.0565 0.0247  -0.0542 4   LEU B CD1 
4081 C CD2 . LEU B 4   ? 0.1882 0.1801 0.1235 -0.0434 0.0118  -0.0407 4   LEU B CD2 
4082 N N   . PHE B 5   ? 0.2130 0.2093 0.1411 -0.0312 0.0072  -0.0261 5   PHE B N   
4083 C CA  . PHE B 5   ? 0.2133 0.2078 0.1466 -0.0219 0.0029  -0.0192 5   PHE B CA  
4084 C C   . PHE B 5   ? 0.2317 0.2176 0.1738 -0.0202 0.0034  -0.0219 5   PHE B C   
4085 O O   . PHE B 5   ? 0.2532 0.2268 0.1997 -0.0213 0.0073  -0.0253 5   PHE B O   
4086 C CB  . PHE B 5   ? 0.1990 0.1839 0.1319 -0.0167 0.0037  -0.0141 5   PHE B CB  
4087 C CG  . PHE B 5   ? 0.2274 0.2206 0.1513 -0.0172 0.0031  -0.0098 5   PHE B CG  
4088 C CD1 . PHE B 5   ? 0.2246 0.2332 0.1439 -0.0143 -0.0014 -0.0044 5   PHE B CD1 
4089 C CD2 . PHE B 5   ? 0.2544 0.2416 0.1744 -0.0204 0.0070  -0.0107 5   PHE B CD2 
4090 C CE1 . PHE B 5   ? 0.2400 0.2577 0.1505 -0.0142 -0.0021 0.0008  5   PHE B CE1 
4091 C CE2 . PHE B 5   ? 0.2467 0.2421 0.1576 -0.0210 0.0066  -0.0061 5   PHE B CE2 
4092 C CZ  . PHE B 5   ? 0.2664 0.2770 0.1722 -0.0178 0.0018  -0.0001 5   PHE B CZ  
4093 N N   . LEU B 6   ? 0.1949 0.1883 0.1395 -0.0169 -0.0005 -0.0196 6   LEU B N   
4094 C CA  . LEU B 6   ? 0.1952 0.1832 0.1468 -0.0159 -0.0005 -0.0217 6   LEU B CA  
4095 C C   . LEU B 6   ? 0.1847 0.1690 0.1404 -0.0069 -0.0037 -0.0162 6   LEU B C   
4096 O O   . LEU B 6   ? 0.1990 0.1917 0.1522 -0.0020 -0.0070 -0.0113 6   LEU B O   
4097 C CB  . LEU B 6   ? 0.1954 0.1960 0.1459 -0.0212 -0.0016 -0.0247 6   LEU B CB  
4098 C CG  . LEU B 6   ? 0.1844 0.1802 0.1411 -0.0214 -0.0011 -0.0268 6   LEU B CG  
4099 C CD1 . LEU B 6   ? 0.2308 0.2101 0.1906 -0.0241 0.0043  -0.0312 6   LEU B CD1 
4100 C CD2 . LEU B 6   ? 0.1964 0.2065 0.1508 -0.0281 -0.0020 -0.0296 6   LEU B CD2 
4101 N N   . VAL B 7   ? 0.1581 0.1300 0.1197 -0.0047 -0.0024 -0.0170 7   VAL B N   
4102 C CA  . VAL B 7   ? 0.1523 0.1188 0.1167 0.0025  -0.0047 -0.0130 7   VAL B CA  
4103 C C   . VAL B 7   ? 0.2050 0.1693 0.1753 0.0032  -0.0052 -0.0148 7   VAL B C   
4104 O O   . VAL B 7   ? 0.2318 0.1887 0.2065 0.0011  -0.0028 -0.0173 7   VAL B O   
4105 C CB  . VAL B 7   ? 0.1606 0.1153 0.1254 0.0040  -0.0030 -0.0117 7   VAL B CB  
4106 C CG1 . VAL B 7   ? 0.2082 0.1570 0.1735 0.0103  -0.0050 -0.0081 7   VAL B CG1 
4107 C CG2 . VAL B 7   ? 0.2022 0.1585 0.1606 0.0021  -0.0016 -0.0101 7   VAL B CG2 
4108 N N   . PHE B 8   ? 0.1898 0.1616 0.1604 0.0067  -0.0080 -0.0130 8   PHE B N   
4109 C CA  . PHE B 8   ? 0.1972 0.1674 0.1726 0.0080  -0.0086 -0.0139 8   PHE B CA  
4110 C C   . PHE B 8   ? 0.1858 0.1473 0.1622 0.0138  -0.0097 -0.0116 8   PHE B C   
4111 O O   . PHE B 8   ? 0.2142 0.1755 0.1871 0.0187  -0.0108 -0.0085 8   PHE B O   
4112 C CB  . PHE B 8   ? 0.1438 0.1270 0.1189 0.0087  -0.0107 -0.0133 8   PHE B CB  
4113 C CG  . PHE B 8   ? 0.1999 0.1915 0.1742 0.0010  -0.0094 -0.0166 8   PHE B CG  
4114 C CD1 . PHE B 8   ? 0.2043 0.1919 0.1816 -0.0036 -0.0072 -0.0198 8   PHE B CD1 
4115 C CD2 . PHE B 8   ? 0.2051 0.2084 0.1748 -0.0020 -0.0101 -0.0165 8   PHE B CD2 
4116 C CE1 . PHE B 8   ? 0.2137 0.2065 0.1891 -0.0118 -0.0050 -0.0236 8   PHE B CE1 
4117 C CE2 . PHE B 8   ? 0.2073 0.2185 0.1751 -0.0106 -0.0086 -0.0206 8   PHE B CE2 
4118 C CZ  . PHE B 8   ? 0.2200 0.2248 0.1904 -0.0159 -0.0058 -0.0245 8   PHE B CZ  
4119 N N   . TRP B 9   ? 0.1631 0.1180 0.1440 0.0131  -0.0091 -0.0131 9   TRP B N   
4120 C CA  . TRP B 9   ? 0.1782 0.1260 0.1595 0.0169  -0.0101 -0.0120 9   TRP B CA  
4121 C C   . TRP B 9   ? 0.2214 0.1713 0.2065 0.0171  -0.0110 -0.0129 9   TRP B C   
4122 O O   . TRP B 9   ? 0.1901 0.1381 0.1795 0.0144  -0.0100 -0.0139 9   TRP B O   
4123 C CB  . TRP B 9   ? 0.1746 0.1140 0.1571 0.0149  -0.0086 -0.0124 9   TRP B CB  
4124 C CG  . TRP B 9   ? 0.1652 0.0969 0.1459 0.0169  -0.0092 -0.0117 9   TRP B CG  
4125 C CD1 . TRP B 9   ? 0.1912 0.1208 0.1693 0.0207  -0.0105 -0.0113 9   TRP B CD1 
4126 C CD2 . TRP B 9   ? 0.2043 0.1289 0.1852 0.0144  -0.0079 -0.0119 9   TRP B CD2 
4127 N NE1 . TRP B 9   ? 0.2033 0.1233 0.1790 0.0202  -0.0098 -0.0118 9   TRP B NE1 
4128 C CE2 . TRP B 9   ? 0.2179 0.1355 0.1956 0.0159  -0.0084 -0.0120 9   TRP B CE2 
4129 C CE3 . TRP B 9   ? 0.2154 0.1392 0.1988 0.0107  -0.0058 -0.0123 9   TRP B CE3 
4130 C CZ2 . TRP B 9   ? 0.2276 0.1376 0.2043 0.0126  -0.0072 -0.0126 9   TRP B CZ2 
4131 C CZ3 . TRP B 9   ? 0.2525 0.1704 0.2358 0.0083  -0.0048 -0.0123 9   TRP B CZ3 
4132 C CH2 . TRP B 9   ? 0.2009 0.1121 0.1809 0.0087  -0.0056 -0.0125 9   TRP B CH2 
4133 N N   . TRP B 10  ? 0.1701 0.1243 0.1535 0.0208  -0.0125 -0.0121 10  TRP B N   
4134 C CA  . TRP B 10  ? 0.1641 0.1218 0.1500 0.0209  -0.0133 -0.0126 10  TRP B CA  
4135 C C   . TRP B 10  ? 0.1773 0.1287 0.1627 0.0230  -0.0141 -0.0129 10  TRP B C   
4136 O O   . TRP B 10  ? 0.1926 0.1403 0.1738 0.0268  -0.0142 -0.0128 10  TRP B O   
4137 C CB  . TRP B 10  ? 0.1422 0.1101 0.1266 0.0235  -0.0141 -0.0118 10  TRP B CB  
4138 C CG  . TRP B 10  ? 0.1472 0.1247 0.1316 0.0202  -0.0137 -0.0119 10  TRP B CG  
4139 C CD1 . TRP B 10  ? 0.1606 0.1463 0.1422 0.0222  -0.0144 -0.0103 10  TRP B CD1 
4140 C CD2 . TRP B 10  ? 0.1869 0.1677 0.1736 0.0139  -0.0123 -0.0137 10  TRP B CD2 
4141 N NE1 . TRP B 10  ? 0.1780 0.1735 0.1600 0.0165  -0.0140 -0.0116 10  TRP B NE1 
4142 C CE2 . TRP B 10  ? 0.1824 0.1736 0.1671 0.0110  -0.0123 -0.0141 10  TRP B CE2 
4143 C CE3 . TRP B 10  ? 0.1668 0.1424 0.1566 0.0105  -0.0107 -0.0146 10  TRP B CE3 
4144 C CZ2 . TRP B 10  ? 0.2112 0.2063 0.1962 0.0034  -0.0104 -0.0166 10  TRP B CZ2 
4145 C CZ3 . TRP B 10  ? 0.1812 0.1588 0.1714 0.0044  -0.0083 -0.0163 10  TRP B CZ3 
4146 C CH2 . TRP B 10  ? 0.2068 0.1933 0.1943 0.0002  -0.0080 -0.0179 10  TRP B CH2 
4147 N N   . HIS B 11  ? 0.1469 0.0974 0.1361 0.0205  -0.0142 -0.0133 11  HIS B N   
4148 C CA  . HIS B 11  ? 0.1517 0.0981 0.1402 0.0207  -0.0153 -0.0140 11  HIS B CA  
4149 C C   . HIS B 11  ? 0.1741 0.1253 0.1616 0.0223  -0.0164 -0.0142 11  HIS B C   
4150 O O   . HIS B 11  ? 0.1982 0.1551 0.1888 0.0213  -0.0165 -0.0130 11  HIS B O   
4151 C CB  . HIS B 11  ? 0.2149 0.1604 0.2085 0.0173  -0.0150 -0.0135 11  HIS B CB  
4152 C CG  . HIS B 11  ? 0.2103 0.1573 0.2047 0.0163  -0.0168 -0.0137 11  HIS B CG  
4153 N ND1 . HIS B 11  ? 0.2053 0.1477 0.1954 0.0154  -0.0175 -0.0159 11  HIS B ND1 
4154 C CD2 . HIS B 11  ? 0.1935 0.1466 0.1920 0.0157  -0.0178 -0.0119 11  HIS B CD2 
4155 C CE1 . HIS B 11  ? 0.1879 0.1351 0.1792 0.0134  -0.0193 -0.0160 11  HIS B CE1 
4156 N NE2 . HIS B 11  ? 0.1948 0.1492 0.1914 0.0141  -0.0197 -0.0131 11  HIS B NE2 
4157 N N   . MET B 12  ? 0.1784 0.1260 0.1609 0.0245  -0.0167 -0.0158 12  MET B N   
4158 C CA  . MET B 12  ? 0.1953 0.1468 0.1752 0.0264  -0.0172 -0.0166 12  MET B CA  
4159 C C   . MET B 12  ? 0.2023 0.1505 0.1798 0.0239  -0.0182 -0.0187 12  MET B C   
4160 O O   . MET B 12  ? 0.1947 0.1342 0.1685 0.0229  -0.0175 -0.0209 12  MET B O   
4161 C CB  . MET B 12  ? 0.1940 0.1443 0.1689 0.0319  -0.0158 -0.0173 12  MET B CB  
4162 C CG  . MET B 12  ? 0.1728 0.1285 0.1495 0.0342  -0.0152 -0.0150 12  MET B CG  
4163 S SD  . MET B 12  ? 0.1982 0.1667 0.1804 0.0309  -0.0159 -0.0135 12  MET B SD  
4164 C CE  . MET B 12  ? 0.2106 0.1880 0.1924 0.0341  -0.0154 -0.0119 12  MET B CE  
4165 N N   . HIS B 13  ? 0.1558 0.1111 0.1348 0.0223  -0.0196 -0.0180 13  HIS B N   
4166 C CA  . HIS B 13  ? 0.1934 0.1491 0.1702 0.0189  -0.0211 -0.0198 13  HIS B CA  
4167 C C   . HIS B 13  ? 0.2002 0.1648 0.1760 0.0189  -0.0223 -0.0189 13  HIS B C   
4168 O O   . HIS B 13  ? 0.1939 0.1649 0.1737 0.0200  -0.0224 -0.0154 13  HIS B O   
4169 C CB  . HIS B 13  ? 0.1727 0.1303 0.1553 0.0151  -0.0224 -0.0180 13  HIS B CB  
4170 C CG  . HIS B 13  ? 0.1571 0.1208 0.1391 0.0111  -0.0247 -0.0187 13  HIS B CG  
4171 N ND1 . HIS B 13  ? 0.1800 0.1394 0.1546 0.0078  -0.0248 -0.0235 13  HIS B ND1 
4172 C CD2 . HIS B 13  ? 0.1863 0.1607 0.1737 0.0095  -0.0269 -0.0150 13  HIS B CD2 
4173 C CE1 . HIS B 13  ? 0.2029 0.1718 0.1781 0.0035  -0.0275 -0.0232 13  HIS B CE1 
4174 N NE2 . HIS B 13  ? 0.1801 0.1592 0.1636 0.0050  -0.0290 -0.0175 13  HIS B NE2 
4175 N N   . GLN B 14  ? 0.1777 0.1421 0.1473 0.0169  -0.0229 -0.0223 14  GLN B N   
4176 C CA  . GLN B 14  ? 0.1610 0.1354 0.1291 0.0154  -0.0247 -0.0213 14  GLN B CA  
4177 C C   . GLN B 14  ? 0.1939 0.1694 0.1579 0.0099  -0.0265 -0.0245 14  GLN B C   
4178 O O   . GLN B 14  ? 0.2133 0.1788 0.1710 0.0080  -0.0249 -0.0299 14  GLN B O   
4179 C CB  . GLN B 14  ? 0.1948 0.1705 0.1570 0.0185  -0.0229 -0.0232 14  GLN B CB  
4180 C CG  . GLN B 14  ? 0.2123 0.1906 0.1782 0.0228  -0.0213 -0.0202 14  GLN B CG  
4181 C CD  . GLN B 14  ? 0.2327 0.2192 0.2050 0.0216  -0.0225 -0.0145 14  GLN B CD  
4182 O OE1 . GLN B 14  ? 0.2090 0.2017 0.1819 0.0192  -0.0244 -0.0120 14  GLN B OE1 
4183 N NE2 . GLN B 14  ? 0.1684 0.1551 0.1452 0.0231  -0.0210 -0.0123 14  GLN B NE2 
4184 N N   . PRO B 15  ? 0.1936 0.1812 0.1604 0.0070  -0.0295 -0.0212 15  PRO B N   
4185 C CA  . PRO B 15  ? 0.2117 0.2045 0.1736 0.0007  -0.0317 -0.0245 15  PRO B CA  
4186 C C   . PRO B 15  ? 0.2390 0.2300 0.1900 -0.0004 -0.0305 -0.0301 15  PRO B C   
4187 O O   . PRO B 15  ? 0.2397 0.2287 0.1883 0.0043  -0.0283 -0.0300 15  PRO B O   
4188 C CB  . PRO B 15  ? 0.2075 0.2168 0.1763 -0.0001 -0.0353 -0.0175 15  PRO B CB  
4189 C CG  . PRO B 15  ? 0.1957 0.2066 0.1678 0.0058  -0.0341 -0.0121 15  PRO B CG  
4190 C CD  . PRO B 15  ? 0.2150 0.2125 0.1887 0.0094  -0.0307 -0.0140 15  PRO B CD  
4191 N N   . LEU B 16  ? 0.2623 0.2546 0.2062 -0.0073 -0.0314 -0.0354 16  LEU B N   
4192 C CA  . LEU B 16  ? 0.2246 0.2124 0.1563 -0.0091 -0.0292 -0.0423 16  LEU B CA  
4193 C C   . LEU B 16  ? 0.2293 0.2327 0.1592 -0.0090 -0.0314 -0.0391 16  LEU B C   
4194 O O   . LEU B 16  ? 0.2607 0.2790 0.1911 -0.0142 -0.0355 -0.0370 16  LEU B O   
4195 C CB  . LEU B 16  ? 0.2146 0.1968 0.1378 -0.0181 -0.0287 -0.0502 16  LEU B CB  
4196 C CG  . LEU B 16  ? 0.2318 0.2048 0.1406 -0.0202 -0.0247 -0.0590 16  LEU B CG  
4197 C CD1 . LEU B 16  ? 0.2658 0.2215 0.1719 -0.0113 -0.0189 -0.0607 16  LEU B CD1 
4198 C CD2 . LEU B 16  ? 0.2522 0.2182 0.1517 -0.0310 -0.0238 -0.0675 16  LEU B CD2 
4199 N N   . TYR B 17  ? 0.2742 0.2758 0.2023 -0.0031 -0.0288 -0.0384 17  TYR B N   
4200 C CA  . TYR B 17  ? 0.2218 0.2367 0.1470 -0.0027 -0.0300 -0.0354 17  TYR B CA  
4201 C C   . TYR B 17  ? 0.2709 0.2862 0.1827 -0.0075 -0.0286 -0.0433 17  TYR B C   
4202 O O   . TYR B 17  ? 0.2754 0.3032 0.1832 -0.0085 -0.0297 -0.0414 17  TYR B O   
4203 C CB  . TYR B 17  ? 0.2197 0.2336 0.1489 0.0047  -0.0274 -0.0314 17  TYR B CB  
4204 C CG  . TYR B 17  ? 0.2209 0.2351 0.1622 0.0082  -0.0284 -0.0239 17  TYR B CG  
4205 C CD1 . TYR B 17  ? 0.2094 0.2342 0.1573 0.0071  -0.0318 -0.0163 17  TYR B CD1 
4206 C CD2 . TYR B 17  ? 0.2154 0.2194 0.1608 0.0128  -0.0257 -0.0243 17  TYR B CD2 
4207 C CE1 . TYR B 17  ? 0.2169 0.2398 0.1749 0.0102  -0.0317 -0.0102 17  TYR B CE1 
4208 C CE2 . TYR B 17  ? 0.2159 0.2199 0.1711 0.0150  -0.0262 -0.0185 17  TYR B CE2 
4209 C CZ  . TYR B 17  ? 0.1880 0.2004 0.1491 0.0134  -0.0289 -0.0119 17  TYR B CZ  
4210 O OH  . TYR B 17  ? 0.2093 0.2196 0.1791 0.0154  -0.0283 -0.0067 17  TYR B OH  
4211 N N   . ARG B 18  ? 0.2727 0.2740 0.1767 -0.0108 -0.0256 -0.0521 18  ARG B N   
4212 C CA  . ARG B 18  ? 0.2510 0.2481 0.1406 -0.0155 -0.0225 -0.0614 18  ARG B CA  
4213 C C   . ARG B 18  ? 0.2524 0.2633 0.1367 -0.0263 -0.0270 -0.0634 18  ARG B C   
4214 O O   . ARG B 18  ? 0.3164 0.3242 0.2002 -0.0333 -0.0284 -0.0668 18  ARG B O   
4215 C CB  . ARG B 18  ? 0.2793 0.2532 0.1625 -0.0146 -0.0166 -0.0695 18  ARG B CB  
4216 C CG  . ARG B 18  ? 0.3751 0.3389 0.2429 -0.0162 -0.0107 -0.0794 18  ARG B CG  
4217 C CD  . ARG B 18  ? 0.4165 0.3549 0.2775 -0.0156 -0.0043 -0.0869 18  ARG B CD  
4218 N NE  . ARG B 18  ? 0.4441 0.3705 0.2897 -0.0165 0.0026  -0.0968 18  ARG B NE  
4219 C CZ  . ARG B 18  ? 0.4676 0.3937 0.3003 -0.0277 0.0033  -0.1056 18  ARG B CZ  
4220 N NH1 . ARG B 18  ? 0.4702 0.4096 0.3042 -0.0390 -0.0032 -0.1052 18  ARG B NH1 
4221 N NH2 . ARG B 18  ? 0.5846 0.4977 0.4028 -0.0276 0.0107  -0.1150 18  ARG B NH2 
4222 N N   . GLU B 19  ? 0.2992 0.3263 0.1790 -0.0281 -0.0292 -0.0615 19  GLU B N   
4223 C CA  . GLU B 19  ? 0.3008 0.3444 0.1746 -0.0384 -0.0338 -0.0632 19  GLU B CA  
4224 C C   . GLU B 19  ? 0.3451 0.3763 0.2042 -0.0477 -0.0301 -0.0767 19  GLU B C   
4225 O O   . GLU B 19  ? 0.3959 0.4125 0.2445 -0.0456 -0.0237 -0.0844 19  GLU B O   
4226 C CB  . GLU B 19  ? 0.3532 0.4153 0.2233 -0.0378 -0.0359 -0.0586 19  GLU B CB  
4227 C CG  . GLU B 19  ? 0.3819 0.4687 0.2529 -0.0448 -0.0430 -0.0531 19  GLU B CG  
4228 C CD  . GLU B 19  ? 0.5136 0.6078 0.3687 -0.0562 -0.0433 -0.0628 19  GLU B CD  
4229 O OE1 . GLU B 19  ? 0.4571 0.5330 0.3011 -0.0584 -0.0371 -0.0741 19  GLU B OE1 
4230 O OE2 . GLU B 19  ? 0.6053 0.7195 0.4631 -0.0608 -0.0483 -0.0572 19  GLU B OE2 
4231 N N   . PRO B 20  ? 0.3788 0.4151 0.2364 -0.0582 -0.0333 -0.0800 20  PRO B N   
4232 C CA  . PRO B 20  ? 0.4237 0.4422 0.2681 -0.0672 -0.0283 -0.0931 20  PRO B CA  
4233 C C   . PRO B 20  ? 0.4520 0.4718 0.2849 -0.0720 -0.0256 -0.0990 20  PRO B C   
4234 O O   . PRO B 20  ? 0.5022 0.5009 0.3259 -0.0741 -0.0188 -0.1082 20  PRO B O   
4235 C CB  . PRO B 20  ? 0.4319 0.4585 0.2839 -0.0755 -0.0329 -0.0911 20  PRO B CB  
4236 C CG  . PRO B 20  ? 0.4075 0.4643 0.2698 -0.0748 -0.0412 -0.0800 20  PRO B CG  
4237 C CD  . PRO B 20  ? 0.3966 0.4537 0.2658 -0.0615 -0.0407 -0.0715 20  PRO B CD  
4238 N N   . TYR B 21  ? 0.4232 0.4663 0.2561 -0.0734 -0.0301 -0.0938 21  TYR B N   
4239 C CA  . TYR B 21  ? 0.5160 0.5606 0.3374 -0.0788 -0.0274 -0.0999 21  TYR B CA  
4240 C C   . TYR B 21  ? 0.4784 0.5129 0.2915 -0.0709 -0.0214 -0.1031 21  TYR B C   
4241 O O   . TYR B 21  ? 0.4886 0.5090 0.2905 -0.0730 -0.0152 -0.1121 21  TYR B O   
4242 C CB  . TYR B 21  ? 0.4890 0.5636 0.3138 -0.0845 -0.0344 -0.0928 21  TYR B CB  
4243 C CG  . TYR B 21  ? 0.5004 0.5863 0.3321 -0.0932 -0.0390 -0.0910 21  TYR B CG  
4244 C CD1 . TYR B 21  ? 0.4651 0.5492 0.2896 -0.1046 -0.0370 -0.0991 21  TYR B CD1 
4245 C CD2 . TYR B 21  ? 0.4907 0.5893 0.3364 -0.0900 -0.0448 -0.0813 21  TYR B CD2 
4246 C CE1 . TYR B 21  ? 0.4539 0.5500 0.2849 -0.1130 -0.0408 -0.0976 21  TYR B CE1 
4247 C CE2 . TYR B 21  ? 0.4636 0.5740 0.3164 -0.0975 -0.0485 -0.0795 21  TYR B CE2 
4248 C CZ  . TYR B 21  ? 0.4861 0.5959 0.3316 -0.1092 -0.0464 -0.0877 21  TYR B CZ  
4249 O OH  . TYR B 21  ? 0.5117 0.6349 0.3642 -0.1171 -0.0497 -0.0859 21  TYR B OH  
4250 N N   . THR B 22  ? 0.4009 0.4422 0.2197 -0.0617 -0.0228 -0.0957 22  THR B N   
4251 C CA  . THR B 22  ? 0.4408 0.4751 0.2534 -0.0537 -0.0169 -0.0979 22  THR B CA  
4252 C C   . THR B 22  ? 0.4418 0.4535 0.2553 -0.0449 -0.0104 -0.1019 22  THR B C   
4253 O O   . THR B 22  ? 0.4803 0.4825 0.2877 -0.0382 -0.0036 -0.1059 22  THR B O   
4254 C CB  . THR B 22  ? 0.4263 0.4830 0.2448 -0.0487 -0.0214 -0.0870 22  THR B CB  
4255 O OG1 . THR B 22  ? 0.4177 0.4775 0.2513 -0.0424 -0.0252 -0.0773 22  THR B OG1 
4256 C CG2 . THR B 22  ? 0.3751 0.4544 0.1934 -0.0558 -0.0273 -0.0816 22  THR B CG2 
4257 N N   . GLY B 23  ? 0.3779 0.3809 0.2012 -0.0432 -0.0119 -0.0990 23  GLY B N   
4258 C CA  . GLY B 23  ? 0.4222 0.4053 0.2517 -0.0322 -0.0065 -0.0981 23  GLY B CA  
4259 C C   . GLY B 23  ? 0.4347 0.4265 0.2763 -0.0208 -0.0075 -0.0877 23  GLY B C   
4260 O O   . GLY B 23  ? 0.4646 0.4435 0.3114 -0.0113 -0.0031 -0.0865 23  GLY B O   
4261 N N   . GLU B 24  ? 0.3818 0.3957 0.2281 -0.0217 -0.0130 -0.0798 24  GLU B N   
4262 C CA  . GLU B 24  ? 0.3815 0.4037 0.2382 -0.0127 -0.0135 -0.0702 24  GLU B CA  
4263 C C   . GLU B 24  ? 0.3310 0.3531 0.2032 -0.0091 -0.0174 -0.0614 24  GLU B C   
4264 O O   . GLU B 24  ? 0.3246 0.3534 0.2015 -0.0144 -0.0228 -0.0581 24  GLU B O   
4265 C CB  . GLU B 24  ? 0.3834 0.4271 0.2379 -0.0153 -0.0170 -0.0647 24  GLU B CB  
4266 C CG  . GLU B 24  ? 0.5319 0.5787 0.3702 -0.0196 -0.0133 -0.0731 24  GLU B CG  
4267 C CD  . GLU B 24  ? 0.6439 0.7124 0.4805 -0.0210 -0.0164 -0.0660 24  GLU B CD  
4268 O OE1 . GLU B 24  ? 0.7449 0.8155 0.5787 -0.0160 -0.0120 -0.0658 24  GLU B OE1 
4269 O OE2 . GLU B 24  ? 0.6700 0.7542 0.5085 -0.0266 -0.0231 -0.0599 24  GLU B OE2 
4270 N N   . TYR B 25  ? 0.2763 0.2922 0.1565 -0.0002 -0.0146 -0.0578 25  TYR B N   
4271 C CA  . TYR B 25  ? 0.2533 0.2708 0.1476 0.0032  -0.0179 -0.0491 25  TYR B CA  
4272 C C   . TYR B 25  ? 0.2507 0.2857 0.1503 0.0032  -0.0215 -0.0398 25  TYR B C   
4273 O O   . TYR B 25  ? 0.2641 0.3045 0.1631 0.0068  -0.0190 -0.0375 25  TYR B O   
4274 C CB  . TYR B 25  ? 0.3137 0.3204 0.2135 0.0116  -0.0137 -0.0487 25  TYR B CB  
4275 C CG  . TYR B 25  ? 0.3156 0.3046 0.2142 0.0125  -0.0113 -0.0541 25  TYR B CG  
4276 C CD1 . TYR B 25  ? 0.3563 0.3321 0.2430 0.0115  -0.0064 -0.0634 25  TYR B CD1 
4277 C CD2 . TYR B 25  ? 0.2809 0.2648 0.1893 0.0142  -0.0132 -0.0498 25  TYR B CD2 
4278 C CE1 . TYR B 25  ? 0.3592 0.3166 0.2439 0.0123  -0.0035 -0.0677 25  TYR B CE1 
4279 C CE2 . TYR B 25  ? 0.3188 0.2864 0.2254 0.0149  -0.0108 -0.0539 25  TYR B CE2 
4280 C CZ  . TYR B 25  ? 0.3213 0.2753 0.2162 0.0141  -0.0059 -0.0625 25  TYR B CZ  
4281 O OH  . TYR B 25  ? 0.3948 0.3306 0.2873 0.0148  -0.0028 -0.0659 25  TYR B OH  
4282 N N   . LEU B 26  ? 0.2298 0.2736 0.1344 -0.0009 -0.0268 -0.0341 26  LEU B N   
4283 C CA  . LEU B 26  ? 0.2751 0.3348 0.1827 -0.0011 -0.0299 -0.0249 26  LEU B CA  
4284 C C   . LEU B 26  ? 0.2816 0.3405 0.2002 0.0045  -0.0292 -0.0163 26  LEU B C   
4285 O O   . LEU B 26  ? 0.2513 0.3203 0.1714 0.0051  -0.0300 -0.0087 26  LEU B O   
4286 C CB  . LEU B 26  ? 0.2266 0.2974 0.1358 -0.0064 -0.0356 -0.0211 26  LEU B CB  
4287 C CG  . LEU B 26  ? 0.2299 0.3057 0.1272 -0.0143 -0.0369 -0.0292 26  LEU B CG  
4288 C CD1 . LEU B 26  ? 0.2823 0.3759 0.1823 -0.0193 -0.0432 -0.0230 26  LEU B CD1 
4289 C CD2 . LEU B 26  ? 0.3075 0.3871 0.1925 -0.0153 -0.0339 -0.0336 26  LEU B CD2 
4290 N N   . LEU B 27  ? 0.2358 0.2829 0.1616 0.0079  -0.0275 -0.0173 27  LEU B N   
4291 C CA  . LEU B 27  ? 0.2365 0.2814 0.1712 0.0121  -0.0260 -0.0113 27  LEU B CA  
4292 C C   . LEU B 27  ? 0.2244 0.2591 0.1599 0.0160  -0.0222 -0.0167 27  LEU B C   
4293 O O   . LEU B 27  ? 0.2578 0.2835 0.1895 0.0162  -0.0212 -0.0235 27  LEU B O   
4294 C CB  . LEU B 27  ? 0.2361 0.2794 0.1806 0.0121  -0.0286 -0.0052 27  LEU B CB  
4295 C CG  . LEU B 27  ? 0.2613 0.3162 0.2075 0.0104  -0.0319 0.0030  27  LEU B CG  
4296 C CD1 . LEU B 27  ? 0.2696 0.3221 0.2251 0.0111  -0.0339 0.0075  27  LEU B CD1 
4297 C CD2 . LEU B 27  ? 0.3160 0.3767 0.2624 0.0120  -0.0302 0.0103  27  LEU B CD2 
4298 N N   . PRO B 28  ? 0.2011 0.2375 0.1410 0.0191  -0.0197 -0.0136 28  PRO B N   
4299 C CA  . PRO B 28  ? 0.1919 0.2229 0.1324 0.0235  -0.0162 -0.0178 28  PRO B CA  
4300 C C   . PRO B 28  ? 0.2589 0.2830 0.2078 0.0251  -0.0164 -0.0161 28  PRO B C   
4301 O O   . PRO B 28  ? 0.2206 0.2440 0.1717 0.0288  -0.0139 -0.0173 28  PRO B O   
4302 C CB  . PRO B 28  ? 0.2507 0.2920 0.1911 0.0245  -0.0135 -0.0150 28  PRO B CB  
4303 C CG  . PRO B 28  ? 0.2652 0.3113 0.2101 0.0210  -0.0156 -0.0070 28  PRO B CG  
4304 C CD  . PRO B 28  ? 0.2514 0.2961 0.1945 0.0182  -0.0195 -0.0060 28  PRO B CD  
4305 N N   . TRP B 29  ? 0.2101 0.2306 0.1636 0.0226  -0.0192 -0.0131 29  TRP B N   
4306 C CA  . TRP B 29  ? 0.1986 0.2137 0.1598 0.0235  -0.0191 -0.0110 29  TRP B CA  
4307 C C   . TRP B 29  ? 0.2379 0.2446 0.1985 0.0267  -0.0178 -0.0159 29  TRP B C   
4308 O O   . TRP B 29  ? 0.2214 0.2268 0.1867 0.0284  -0.0168 -0.0148 29  TRP B O   
4309 C CB  . TRP B 29  ? 0.1907 0.2036 0.1566 0.0209  -0.0217 -0.0071 29  TRP B CB  
4310 C CG  . TRP B 29  ? 0.1808 0.2007 0.1486 0.0192  -0.0224 -0.0003 29  TRP B CG  
4311 C CD1 . TRP B 29  ? 0.1975 0.2223 0.1648 0.0176  -0.0251 0.0032  29  TRP B CD1 
4312 C CD2 . TRP B 29  ? 0.2457 0.2685 0.2159 0.0189  -0.0201 0.0043  29  TRP B CD2 
4313 N NE1 . TRP B 29  ? 0.2025 0.2320 0.1718 0.0176  -0.0244 0.0105  29  TRP B NE1 
4314 C CE2 . TRP B 29  ? 0.2144 0.2414 0.1851 0.0179  -0.0210 0.0110  29  TRP B CE2 
4315 C CE3 . TRP B 29  ? 0.2418 0.2647 0.2137 0.0190  -0.0172 0.0037  29  TRP B CE3 
4316 C CZ2 . TRP B 29  ? 0.2019 0.2301 0.1741 0.0170  -0.0185 0.0171  29  TRP B CZ2 
4317 C CZ3 . TRP B 29  ? 0.2536 0.2791 0.2271 0.0168  -0.0149 0.0088  29  TRP B CZ3 
4318 C CH2 . TRP B 29  ? 0.1900 0.2166 0.1632 0.0158  -0.0153 0.0154  29  TRP B CH2 
4319 N N   . THR B 30  ? 0.2104 0.2109 0.1647 0.0270  -0.0177 -0.0210 30  THR B N   
4320 C CA  . THR B 30  ? 0.2154 0.2062 0.1682 0.0309  -0.0155 -0.0248 30  THR B CA  
4321 C C   . THR B 30  ? 0.2101 0.2053 0.1622 0.0366  -0.0122 -0.0253 30  THR B C   
4322 O O   . THR B 30  ? 0.2018 0.1957 0.1576 0.0404  -0.0111 -0.0242 30  THR B O   
4323 C CB  . THR B 30  ? 0.2665 0.2474 0.2114 0.0294  -0.0149 -0.0305 30  THR B CB  
4324 O OG1 . THR B 30  ? 0.2321 0.2119 0.1791 0.0238  -0.0182 -0.0297 30  THR B OG1 
4325 C CG2 . THR B 30  ? 0.2989 0.2675 0.2414 0.0343  -0.0116 -0.0336 30  THR B CG2 
4326 N N   . PHE B 31  ? 0.2381 0.2405 0.1858 0.0374  -0.0105 -0.0265 31  PHE B N   
4327 C CA  . PHE B 31  ? 0.2054 0.2153 0.1536 0.0430  -0.0071 -0.0264 31  PHE B CA  
4328 C C   . PHE B 31  ? 0.1891 0.2082 0.1460 0.0424  -0.0081 -0.0213 31  PHE B C   
4329 O O   . PHE B 31  ? 0.1910 0.2129 0.1511 0.0470  -0.0066 -0.0207 31  PHE B O   
4330 C CB  . PHE B 31  ? 0.2148 0.2329 0.1574 0.0426  -0.0053 -0.0279 31  PHE B CB  
4331 C CG  . PHE B 31  ? 0.2378 0.2669 0.1821 0.0479  -0.0017 -0.0273 31  PHE B CG  
4332 C CD1 . PHE B 31  ? 0.2398 0.2650 0.1805 0.0557  0.0027  -0.0309 31  PHE B CD1 
4333 C CD2 . PHE B 31  ? 0.2063 0.2496 0.1558 0.0453  -0.0021 -0.0227 31  PHE B CD2 
4334 C CE1 . PHE B 31  ? 0.2454 0.2834 0.1887 0.0615  0.0062  -0.0298 31  PHE B CE1 
4335 C CE2 . PHE B 31  ? 0.1840 0.2401 0.1358 0.0495  0.0012  -0.0220 31  PHE B CE2 
4336 C CZ  . PHE B 31  ? 0.2165 0.2713 0.1658 0.0580  0.0052  -0.0254 31  PHE B CZ  
4337 N N   . PHE B 32  ? 0.1790 0.2029 0.1394 0.0366  -0.0103 -0.0175 32  PHE B N   
4338 C CA  . PHE B 32  ? 0.1513 0.1835 0.1183 0.0347  -0.0100 -0.0136 32  PHE B CA  
4339 C C   . PHE B 32  ? 0.1880 0.2147 0.1598 0.0346  -0.0111 -0.0130 32  PHE B C   
4340 O O   . PHE B 32  ? 0.1709 0.2052 0.1467 0.0351  -0.0103 -0.0118 32  PHE B O   
4341 C CB  . PHE B 32  ? 0.1853 0.2211 0.1535 0.0288  -0.0109 -0.0095 32  PHE B CB  
4342 C CG  . PHE B 32  ? 0.1827 0.2287 0.1473 0.0284  -0.0090 -0.0088 32  PHE B CG  
4343 C CD1 . PHE B 32  ? 0.2037 0.2610 0.1695 0.0305  -0.0063 -0.0094 32  PHE B CD1 
4344 C CD2 . PHE B 32  ? 0.2183 0.2646 0.1784 0.0260  -0.0100 -0.0073 32  PHE B CD2 
4345 C CE1 . PHE B 32  ? 0.2486 0.3162 0.2110 0.0300  -0.0041 -0.0088 32  PHE B CE1 
4346 C CE2 . PHE B 32  ? 0.2912 0.3474 0.2472 0.0254  -0.0081 -0.0065 32  PHE B CE2 
4347 C CZ  . PHE B 32  ? 0.2548 0.3210 0.2119 0.0273  -0.0049 -0.0075 32  PHE B CZ  
4348 N N   . HIS B 33  ? 0.1798 0.1951 0.1513 0.0336  -0.0130 -0.0137 33  HIS B N   
4349 C CA  . HIS B 33  ? 0.2066 0.2167 0.1818 0.0338  -0.0136 -0.0134 33  HIS B CA  
4350 C C   . HIS B 33  ? 0.2435 0.2515 0.2166 0.0401  -0.0123 -0.0155 33  HIS B C   
4351 O O   . HIS B 33  ? 0.1952 0.2047 0.1714 0.0413  -0.0123 -0.0144 33  HIS B O   
4352 C CB  . HIS B 33  ? 0.1685 0.1686 0.1447 0.0306  -0.0156 -0.0131 33  HIS B CB  
4353 C CG  . HIS B 33  ? 0.1543 0.1561 0.1343 0.0258  -0.0161 -0.0095 33  HIS B CG  
4354 N ND1 . HIS B 33  ? 0.1841 0.1878 0.1684 0.0231  -0.0150 -0.0076 33  HIS B ND1 
4355 C CD2 . HIS B 33  ? 0.1899 0.1919 0.1697 0.0235  -0.0171 -0.0072 33  HIS B CD2 
4356 C CE1 . HIS B 33  ? 0.2045 0.2069 0.1907 0.0196  -0.0145 -0.0044 33  HIS B CE1 
4357 N NE2 . HIS B 33  ? 0.1762 0.1784 0.1602 0.0204  -0.0160 -0.0034 33  HIS B NE2 
4358 N N   . ALA B 34  ? 0.1947 0.1990 0.1621 0.0445  -0.0106 -0.0185 34  ALA B N   
4359 C CA  . ALA B 34  ? 0.2289 0.2303 0.1940 0.0521  -0.0082 -0.0196 34  ALA B CA  
4360 C C   . ALA B 34  ? 0.2257 0.2431 0.1949 0.0560  -0.0068 -0.0170 34  ALA B C   
4361 O O   . ALA B 34  ? 0.2164 0.2369 0.1881 0.0601  -0.0066 -0.0150 34  ALA B O   
4362 C CB  . ALA B 34  ? 0.2316 0.2237 0.1887 0.0557  -0.0054 -0.0239 34  ALA B CB  
4363 N N   . VAL B 35  ? 0.1925 0.2218 0.1625 0.0544  -0.0061 -0.0167 35  VAL B N   
4364 C CA  . VAL B 35  ? 0.1869 0.2339 0.1611 0.0576  -0.0045 -0.0145 35  VAL B CA  
4365 C C   . VAL B 35  ? 0.2301 0.2863 0.2106 0.0517  -0.0068 -0.0115 35  VAL B C   
4366 O O   . VAL B 35  ? 0.2154 0.2855 0.1997 0.0543  -0.0064 -0.0096 35  VAL B O   
4367 C CB  . VAL B 35  ? 0.2251 0.2828 0.1979 0.0570  -0.0025 -0.0151 35  VAL B CB  
4368 C CG1 . VAL B 35  ? 0.2466 0.2943 0.2116 0.0621  0.0002  -0.0190 35  VAL B CG1 
4369 C CG2 . VAL B 35  ? 0.2664 0.3259 0.2404 0.0475  -0.0044 -0.0137 35  VAL B CG2 
4370 N N   . LYS B 36  ? 0.1608 0.2098 0.1422 0.0437  -0.0088 -0.0113 36  LYS B N   
4371 C CA  . LYS B 36  ? 0.1619 0.2175 0.1480 0.0370  -0.0098 -0.0095 36  LYS B CA  
4372 C C   . LYS B 36  ? 0.1724 0.2208 0.1594 0.0371  -0.0113 -0.0094 36  LYS B C   
4373 O O   . LYS B 36  ? 0.1714 0.2301 0.1614 0.0353  -0.0117 -0.0084 36  LYS B O   
4374 C CB  . LYS B 36  ? 0.1766 0.2274 0.1630 0.0288  -0.0100 -0.0087 36  LYS B CB  
4375 C CG  . LYS B 36  ? 0.1744 0.2326 0.1645 0.0209  -0.0094 -0.0076 36  LYS B CG  
4376 C CD  . LYS B 36  ? 0.1798 0.2321 0.1696 0.0137  -0.0082 -0.0060 36  LYS B CD  
4377 C CE  . LYS B 36  ? 0.1907 0.2260 0.1800 0.0129  -0.0091 -0.0056 36  LYS B CE  
4378 N NZ  . LYS B 36  ? 0.1778 0.2080 0.1690 0.0104  -0.0093 -0.0069 36  LYS B NZ  
4379 N N   . ASP B 37  ? 0.1740 0.2065 0.1584 0.0387  -0.0122 -0.0106 37  ASP B N   
4380 C CA  . ASP B 37  ? 0.1576 0.1823 0.1428 0.0370  -0.0134 -0.0104 37  ASP B CA  
4381 C C   . ASP B 37  ? 0.2126 0.2281 0.1947 0.0436  -0.0132 -0.0108 37  ASP B C   
4382 O O   . ASP B 37  ? 0.1935 0.2095 0.1763 0.0444  -0.0137 -0.0096 37  ASP B O   
4383 C CB  . ASP B 37  ? 0.1473 0.1611 0.1332 0.0309  -0.0141 -0.0109 37  ASP B CB  
4384 C CG  . ASP B 37  ? 0.1803 0.1994 0.1682 0.0249  -0.0133 -0.0098 37  ASP B CG  
4385 O OD1 . ASP B 37  ? 0.2081 0.2351 0.1982 0.0205  -0.0124 -0.0094 37  ASP B OD1 
4386 O OD2 . ASP B 37  ? 0.1620 0.1776 0.1488 0.0242  -0.0133 -0.0093 37  ASP B OD2 
4387 N N   . TYR B 38  ? 0.1734 0.1796 0.1512 0.0478  -0.0122 -0.0126 38  TYR B N   
4388 C CA  . TYR B 38  ? 0.1721 0.1645 0.1460 0.0517  -0.0116 -0.0133 38  TYR B CA  
4389 C C   . TYR B 38  ? 0.1891 0.1854 0.1619 0.0601  -0.0099 -0.0110 38  TYR B C   
4390 O O   . TYR B 38  ? 0.2282 0.2152 0.1988 0.0627  -0.0094 -0.0099 38  TYR B O   
4391 C CB  . TYR B 38  ? 0.1871 0.1674 0.1556 0.0522  -0.0105 -0.0167 38  TYR B CB  
4392 C CG  . TYR B 38  ? 0.1807 0.1573 0.1503 0.0446  -0.0127 -0.0178 38  TYR B CG  
4393 C CD1 . TYR B 38  ? 0.2016 0.1775 0.1757 0.0396  -0.0145 -0.0163 38  TYR B CD1 
4394 C CD2 . TYR B 38  ? 0.2136 0.1886 0.1797 0.0429  -0.0126 -0.0202 38  TYR B CD2 
4395 C CE1 . TYR B 38  ? 0.1731 0.1468 0.1490 0.0341  -0.0160 -0.0163 38  TYR B CE1 
4396 C CE2 . TYR B 38  ? 0.1632 0.1377 0.1309 0.0368  -0.0149 -0.0201 38  TYR B CE2 
4397 C CZ  . TYR B 38  ? 0.1760 0.1498 0.1490 0.0331  -0.0165 -0.0178 38  TYR B CZ  
4398 O OH  . TYR B 38  ? 0.1851 0.1594 0.1603 0.0285  -0.0182 -0.0167 38  TYR B OH  
4399 N N   . TYR B 39  ? 0.1766 0.1876 0.1512 0.0646  -0.0087 -0.0096 39  TYR B N   
4400 C CA  . TYR B 39  ? 0.2343 0.2538 0.2095 0.0731  -0.0074 -0.0059 39  TYR B CA  
4401 C C   . TYR B 39  ? 0.2489 0.2851 0.2295 0.0690  -0.0101 -0.0030 39  TYR B C   
4402 O O   . TYR B 39  ? 0.2005 0.2392 0.1810 0.0726  -0.0105 0.0003  39  TYR B O   
4403 C CB  . TYR B 39  ? 0.2045 0.2339 0.1797 0.0809  -0.0044 -0.0056 39  TYR B CB  
4404 C CG  . TYR B 39  ? 0.2494 0.2932 0.2271 0.0906  -0.0031 -0.0006 39  TYR B CG  
4405 C CD1 . TYR B 39  ? 0.2278 0.2968 0.2121 0.0885  -0.0051 0.0023  39  TYR B CD1 
4406 C CD2 . TYR B 39  ? 0.2773 0.3100 0.2507 0.1016  0.0004  0.0015  39  TYR B CD2 
4407 C CE1 . TYR B 39  ? 0.2230 0.3090 0.2103 0.0975  -0.0044 0.0076  39  TYR B CE1 
4408 C CE2 . TYR B 39  ? 0.2781 0.3254 0.2542 0.1120  0.0017  0.0074  39  TYR B CE2 
4409 C CZ  . TYR B 39  ? 0.2930 0.3686 0.2766 0.1100  -0.0011 0.0107  39  TYR B CZ  
4410 O OH  . TYR B 39  ? 0.3205 0.4145 0.3076 0.1203  -0.0003 0.0173  39  TYR B OH  
4411 N N   . ASP B 40  ? 0.2326 0.2796 0.2170 0.0608  -0.0115 -0.0042 40  ASP B N   
4412 C CA  . ASP B 40  ? 0.1989 0.2641 0.1875 0.0561  -0.0132 -0.0023 40  ASP B CA  
4413 C C   . ASP B 40  ? 0.1346 0.1930 0.1226 0.0500  -0.0150 -0.0026 40  ASP B C   
4414 O O   . ASP B 40  ? 0.1747 0.2464 0.1642 0.0486  -0.0162 -0.0006 40  ASP B O   
4415 C CB  . ASP B 40  ? 0.1968 0.2732 0.1885 0.0484  -0.0132 -0.0039 40  ASP B CB  
4416 C CG  . ASP B 40  ? 0.2491 0.3436 0.2432 0.0538  -0.0117 -0.0023 40  ASP B CG  
4417 O OD1 . ASP B 40  ? 0.2275 0.3408 0.2246 0.0567  -0.0123 0.0006  40  ASP B OD1 
4418 O OD2 . ASP B 40  ? 0.2318 0.3228 0.2245 0.0557  -0.0099 -0.0038 40  ASP B OD2 
4419 N N   . MET B 41  ? 0.1740 0.2135 0.1599 0.0463  -0.0150 -0.0050 41  MET B N   
4420 C CA  . MET B 41  ? 0.1678 0.2011 0.1533 0.0410  -0.0160 -0.0053 41  MET B CA  
4421 C C   . MET B 41  ? 0.1724 0.2048 0.1552 0.0473  -0.0162 -0.0023 41  MET B C   
4422 O O   . MET B 41  ? 0.1974 0.2397 0.1807 0.0442  -0.0174 -0.0010 41  MET B O   
4423 C CB  . MET B 41  ? 0.1383 0.1537 0.1230 0.0366  -0.0157 -0.0079 41  MET B CB  
4424 C CG  . MET B 41  ? 0.1613 0.1782 0.1487 0.0288  -0.0153 -0.0097 41  MET B CG  
4425 S SD  . MET B 41  ? 0.1676 0.1909 0.1566 0.0193  -0.0148 -0.0108 41  MET B SD  
4426 C CE  . MET B 41  ? 0.1659 0.1720 0.1537 0.0178  -0.0143 -0.0118 41  MET B CE  
4427 N N   . PRO B 42  ? 0.1724 0.1934 0.1518 0.0556  -0.0149 -0.0009 42  PRO B N   
4428 C CA  . PRO B 42  ? 0.2252 0.2468 0.2020 0.0624  -0.0145 0.0034  42  PRO B CA  
4429 C C   . PRO B 42  ? 0.1946 0.2385 0.1738 0.0683  -0.0150 0.0077  42  PRO B C   
4430 O O   . PRO B 42  ? 0.2182 0.2698 0.1964 0.0715  -0.0159 0.0120  42  PRO B O   
4431 C CB  . PRO B 42  ? 0.1918 0.1934 0.1637 0.0693  -0.0118 0.0033  42  PRO B CB  
4432 C CG  . PRO B 42  ? 0.1781 0.1765 0.1506 0.0685  -0.0109 -0.0006 42  PRO B CG  
4433 C CD  . PRO B 42  ? 0.1759 0.1812 0.1526 0.0582  -0.0132 -0.0034 42  PRO B CD  
4434 N N   . ALA B 43  ? 0.1608 0.2172 0.1433 0.0699  -0.0146 0.0071  43  ALA B N   
4435 C CA  . ALA B 43  ? 0.1689 0.2494 0.1546 0.0761  -0.0150 0.0117  43  ALA B CA  
4436 C C   . ALA B 43  ? 0.1933 0.2945 0.1818 0.0681  -0.0181 0.0127  43  ALA B C   
4437 O O   . ALA B 43  ? 0.2324 0.3553 0.2231 0.0732  -0.0191 0.0176  43  ALA B O   
4438 C CB  . ALA B 43  ? 0.2248 0.3154 0.2137 0.0785  -0.0134 0.0104  43  ALA B CB  
4439 N N   . TYR B 44  ? 0.1917 0.2872 0.1798 0.0558  -0.0193 0.0082  44  TYR B N   
4440 C CA  . TYR B 44  ? 0.1845 0.2962 0.1732 0.0471  -0.0215 0.0080  44  TYR B CA  
4441 C C   . TYR B 44  ? 0.1998 0.3163 0.1855 0.0525  -0.0227 0.0131  44  TYR B C   
4442 O O   . TYR B 44  ? 0.2040 0.3424 0.1904 0.0488  -0.0249 0.0149  44  TYR B O   
4443 C CB  . TYR B 44  ? 0.1611 0.2592 0.1483 0.0346  -0.0211 0.0023  44  TYR B CB  
4444 C CG  . TYR B 44  ? 0.1466 0.2479 0.1365 0.0257  -0.0202 -0.0019 44  TYR B CG  
4445 C CD1 . TYR B 44  ? 0.1472 0.2676 0.1385 0.0161  -0.0208 -0.0036 44  TYR B CD1 
4446 C CD2 . TYR B 44  ? 0.1771 0.2623 0.1676 0.0262  -0.0185 -0.0041 44  TYR B CD2 
4447 C CE1 . TYR B 44  ? 0.1835 0.3044 0.1765 0.0073  -0.0191 -0.0072 44  TYR B CE1 
4448 C CE2 . TYR B 44  ? 0.1818 0.2690 0.1741 0.0185  -0.0173 -0.0068 44  TYR B CE2 
4449 C CZ  . TYR B 44  ? 0.1776 0.2813 0.1711 0.0091  -0.0173 -0.0083 44  TYR B CZ  
4450 O OH  . TYR B 44  ? 0.1867 0.2898 0.1813 0.0012  -0.0153 -0.0108 44  TYR B OH  
4451 N N   . LEU B 45  ? 0.1836 0.2802 0.1656 0.0605  -0.0213 0.0153  45  LEU B N   
4452 C CA  . LEU B 45  ? 0.1773 0.2761 0.1557 0.0661  -0.0220 0.0210  45  LEU B CA  
4453 C C   . LEU B 45  ? 0.2245 0.3457 0.2049 0.0772  -0.0226 0.0286  45  LEU B C   
4454 O O   . LEU B 45  ? 0.2675 0.3981 0.2454 0.0812  -0.0239 0.0346  45  LEU B O   
4455 C CB  . LEU B 45  ? 0.1926 0.2630 0.1661 0.0712  -0.0195 0.0216  45  LEU B CB  
4456 C CG  . LEU B 45  ? 0.2065 0.2576 0.1782 0.0610  -0.0191 0.0155  45  LEU B CG  
4457 C CD1 . LEU B 45  ? 0.2257 0.2504 0.1938 0.0655  -0.0164 0.0151  45  LEU B CD1 
4458 C CD2 . LEU B 45  ? 0.2072 0.2645 0.1764 0.0535  -0.0206 0.0156  45  LEU B CD2 
4459 N N   . LYS B 46  ? 0.2324 0.3638 0.2173 0.0827  -0.0216 0.0291  46  LYS B N   
4460 C CA  . LYS B 46  ? 0.2410 0.3983 0.2293 0.0933  -0.0220 0.0366  46  LYS B CA  
4461 C C   . LYS B 46  ? 0.2501 0.4403 0.2418 0.0846  -0.0261 0.0375  46  LYS B C   
4462 O O   . LYS B 46  ? 0.2424 0.4509 0.2358 0.0893  -0.0255 0.0434  46  LYS B O   
4463 C CB  . LYS B 46  ? 0.2840 0.4446 0.2766 0.1009  -0.0193 0.0363  46  LYS B CB  
4464 C CG  . LYS B 46  ? 0.4008 0.5326 0.3891 0.1116  -0.0146 0.0363  46  LYS B CG  
4465 C CD  . LYS B 46  ? 0.5576 0.6943 0.5492 0.1175  -0.0112 0.0350  46  LYS B CD  
4466 C CE  . LYS B 46  ? 0.7004 0.8084 0.6862 0.1270  -0.0054 0.0344  46  LYS B CE  
4467 N NZ  . LYS B 46  ? 0.7899 0.8931 0.7720 0.1363  -0.0017 0.0411  46  LYS B NZ  
4468 N N   . ASP B 47  ? 0.2149 0.4064 0.2070 0.0687  -0.0276 0.0300  47  ASP B N   
4469 C CA  . ASP B 47  ? 0.2207 0.4423 0.2153 0.0578  -0.0307 0.0289  47  ASP B CA  
4470 C C   . ASP B 47  ? 0.2577 0.4771 0.2469 0.0456  -0.0325 0.0255  47  ASP B C   
4471 O O   . ASP B 47  ? 0.2663 0.5121 0.2559 0.0371  -0.0353 0.0254  47  ASP B O   
4472 C CB  . ASP B 47  ? 0.2210 0.4480 0.2198 0.0479  -0.0298 0.0225  47  ASP B CB  
4473 C CG  . ASP B 47  ? 0.3909 0.6254 0.3951 0.0589  -0.0279 0.0255  47  ASP B CG  
4474 O OD1 . ASP B 47  ? 0.3401 0.5865 0.3462 0.0703  -0.0266 0.0322  47  ASP B OD1 
4475 O OD2 . ASP B 47  ? 0.4044 0.6281 0.4100 0.0550  -0.0258 0.0207  47  ASP B OD2 
4476 N N   . PHE B 48  ? 0.2490 0.4390 0.2331 0.0442  -0.0309 0.0227  48  PHE B N   
4477 C CA  . PHE B 48  ? 0.2529 0.4382 0.2316 0.0328  -0.0317 0.0188  48  PHE B CA  
4478 C C   . PHE B 48  ? 0.2602 0.4289 0.2337 0.0410  -0.0311 0.0235  48  PHE B C   
4479 O O   . PHE B 48  ? 0.2887 0.4324 0.2616 0.0482  -0.0287 0.0239  48  PHE B O   
4480 C CB  . PHE B 48  ? 0.2400 0.4052 0.2181 0.0206  -0.0293 0.0096  48  PHE B CB  
4481 C CG  . PHE B 48  ? 0.2473 0.4262 0.2294 0.0115  -0.0291 0.0052  48  PHE B CG  
4482 C CD1 . PHE B 48  ? 0.2505 0.4491 0.2311 -0.0017 -0.0302 0.0015  48  PHE B CD1 
4483 C CD2 . PHE B 48  ? 0.2375 0.4099 0.2242 0.0155  -0.0275 0.0045  48  PHE B CD2 
4484 C CE1 . PHE B 48  ? 0.2231 0.4336 0.2068 -0.0113 -0.0294 -0.0027 48  PHE B CE1 
4485 C CE2 . PHE B 48  ? 0.2344 0.4193 0.2243 0.0068  -0.0269 0.0010  48  PHE B CE2 
4486 C CZ  . PHE B 48  ? 0.2575 0.4612 0.2461 -0.0068 -0.0277 -0.0026 48  PHE B CZ  
4487 N N   . GLU B 49  ? 0.2386 0.4224 0.2080 0.0397  -0.0334 0.0274  49  GLU B N   
4488 C CA  . GLU B 49  ? 0.2364 0.4065 0.2002 0.0475  -0.0327 0.0330  49  GLU B CA  
4489 C C   . GLU B 49  ? 0.2261 0.3745 0.1850 0.0368  -0.0309 0.0261  49  GLU B C   
4490 O O   . GLU B 49  ? 0.2903 0.4462 0.2441 0.0292  -0.0319 0.0251  49  GLU B O   
4491 C CB  . GLU B 49  ? 0.4050 0.6024 0.3664 0.0524  -0.0358 0.0418  49  GLU B CB  
4492 C CG  . GLU B 49  ? 0.5398 0.7224 0.4954 0.0636  -0.0345 0.0500  49  GLU B CG  
4493 C CD  . GLU B 49  ? 0.7179 0.9202 0.6749 0.0712  -0.0345 0.0592  49  GLU B CD  
4494 O OE1 . GLU B 49  ? 0.7346 0.9552 0.6989 0.0750  -0.0339 0.0613  49  GLU B OE1 
4495 O OE2 . GLU B 49  ? 0.7300 0.9280 0.6809 0.0730  -0.0343 0.0641  49  GLU B OE2 
4496 N N   . ILE B 50  ? 0.1991 0.3214 0.1598 0.0363  -0.0280 0.0212  50  ILE B N   
4497 C CA  . ILE B 50  ? 0.2479 0.3473 0.2055 0.0291  -0.0256 0.0155  50  ILE B CA  
4498 C C   . ILE B 50  ? 0.2220 0.2959 0.1799 0.0378  -0.0232 0.0174  50  ILE B C   
4499 O O   . ILE B 50  ? 0.2968 0.3696 0.2564 0.0484  -0.0230 0.0220  50  ILE B O   
4500 C CB  . ILE B 50  ? 0.2301 0.3258 0.1901 0.0167  -0.0243 0.0064  50  ILE B CB  
4501 C CG1 . ILE B 50  ? 0.2175 0.3095 0.1836 0.0198  -0.0238 0.0050  50  ILE B CG1 
4502 C CG2 . ILE B 50  ? 0.2914 0.4101 0.2495 0.0059  -0.0259 0.0034  50  ILE B CG2 
4503 C CD1 . ILE B 50  ? 0.2883 0.3705 0.2564 0.0095  -0.0216 -0.0027 50  ILE B CD1 
4504 N N   . LYS B 51  ? 0.1793 0.2332 0.1351 0.0331  -0.0210 0.0136  51  LYS B N   
4505 C CA  . LYS B 51  ? 0.1913 0.2214 0.1474 0.0383  -0.0187 0.0138  51  LYS B CA  
4506 C C   . LYS B 51  ? 0.2159 0.2357 0.1768 0.0326  -0.0176 0.0069  51  LYS B C   
4507 O O   . LYS B 51  ? 0.1993 0.2202 0.1612 0.0233  -0.0170 0.0017  51  LYS B O   
4508 C CB  . LYS B 51  ? 0.1767 0.1927 0.1276 0.0374  -0.0168 0.0152  51  LYS B CB  
4509 C CG  . LYS B 51  ? 0.2025 0.2289 0.1475 0.0412  -0.0178 0.0222  51  LYS B CG  
4510 C CD  . LYS B 51  ? 0.2493 0.2796 0.1936 0.0541  -0.0182 0.0303  51  LYS B CD  
4511 C CE  . LYS B 51  ? 0.2925 0.3295 0.2302 0.0591  -0.0184 0.0388  51  LYS B CE  
4512 N NZ  . LYS B 51  ? 0.4475 0.4863 0.3845 0.0733  -0.0179 0.0476  51  LYS B NZ  
4513 N N   . LEU B 52  ? 0.1856 0.1950 0.1488 0.0383  -0.0168 0.0071  52  LEU B N   
4514 C CA  . LEU B 52  ? 0.2286 0.2281 0.1958 0.0341  -0.0160 0.0018  52  LEU B CA  
4515 C C   . LEU B 52  ? 0.1987 0.1797 0.1647 0.0390  -0.0144 0.0024  52  LEU B C   
4516 O O   . LEU B 52  ? 0.2090 0.1872 0.1721 0.0472  -0.0139 0.0063  52  LEU B O   
4517 C CB  . LEU B 52  ? 0.1976 0.2088 0.1689 0.0341  -0.0170 0.0005  52  LEU B CB  
4518 C CG  . LEU B 52  ? 0.1904 0.2209 0.1630 0.0277  -0.0183 -0.0009 52  LEU B CG  
4519 C CD1 . LEU B 52  ? 0.1969 0.2386 0.1734 0.0289  -0.0190 -0.0013 52  LEU B CD1 
4520 C CD2 . LEU B 52  ? 0.1954 0.2204 0.1682 0.0170  -0.0167 -0.0062 52  LEU B CD2 
4521 N N   . ASN B 53  ? 0.1748 0.1437 0.1425 0.0340  -0.0134 -0.0013 53  ASN B N   
4522 C CA  . ASN B 53  ? 0.1781 0.1308 0.1444 0.0362  -0.0120 -0.0016 53  ASN B CA  
4523 C C   . ASN B 53  ? 0.1926 0.1427 0.1627 0.0347  -0.0124 -0.0051 53  ASN B C   
4524 O O   . ASN B 53  ? 0.1864 0.1438 0.1607 0.0307  -0.0132 -0.0072 53  ASN B O   
4525 C CB  . ASN B 53  ? 0.1787 0.1218 0.1439 0.0315  -0.0105 -0.0024 53  ASN B CB  
4526 C CG  . ASN B 53  ? 0.1829 0.1302 0.1438 0.0322  -0.0101 0.0012  53  ASN B CG  
4527 O OD1 . ASN B 53  ? 0.2034 0.1463 0.1593 0.0381  -0.0094 0.0056  53  ASN B OD1 
4528 N ND2 . ASN B 53  ? 0.2019 0.1576 0.1638 0.0265  -0.0103 -0.0005 53  ASN B ND2 
4529 N N   . PHE B 54  ? 0.1881 0.1269 0.1557 0.0377  -0.0114 -0.0055 54  PHE B N   
4530 C CA  . PHE B 54  ? 0.1836 0.1212 0.1533 0.0370  -0.0120 -0.0084 54  PHE B CA  
4531 C C   . PHE B 54  ? 0.2041 0.1285 0.1720 0.0343  -0.0110 -0.0106 54  PHE B C   
4532 O O   . PHE B 54  ? 0.2487 0.1622 0.2118 0.0357  -0.0091 -0.0097 54  PHE B O   
4533 C CB  . PHE B 54  ? 0.1882 0.1297 0.1556 0.0440  -0.0116 -0.0074 54  PHE B CB  
4534 C CG  . PHE B 54  ? 0.1951 0.1530 0.1652 0.0456  -0.0129 -0.0054 54  PHE B CG  
4535 C CD1 . PHE B 54  ? 0.2109 0.1789 0.1854 0.0419  -0.0141 -0.0071 54  PHE B CD1 
4536 C CD2 . PHE B 54  ? 0.1976 0.1617 0.1657 0.0499  -0.0127 -0.0014 54  PHE B CD2 
4537 C CE1 . PHE B 54  ? 0.1777 0.1614 0.1544 0.0415  -0.0150 -0.0058 54  PHE B CE1 
4538 C CE2 . PHE B 54  ? 0.2259 0.2084 0.1967 0.0499  -0.0142 0.0002  54  PHE B CE2 
4539 C CZ  . PHE B 54  ? 0.1726 0.1645 0.1477 0.0450  -0.0153 -0.0025 54  PHE B CZ  
4540 N N   . ASN B 55  ? 0.1886 0.1147 0.1603 0.0303  -0.0122 -0.0132 55  ASN B N   
4541 C CA  . ASN B 55  ? 0.1948 0.1124 0.1649 0.0271  -0.0119 -0.0157 55  ASN B CA  
4542 C C   . ASN B 55  ? 0.2103 0.1294 0.1785 0.0289  -0.0124 -0.0178 55  ASN B C   
4543 O O   . ASN B 55  ? 0.1963 0.1254 0.1680 0.0294  -0.0138 -0.0174 55  ASN B O   
4544 C CB  . ASN B 55  ? 0.1838 0.1049 0.1600 0.0211  -0.0129 -0.0163 55  ASN B CB  
4545 C CG  . ASN B 55  ? 0.2150 0.1303 0.1899 0.0167  -0.0129 -0.0187 55  ASN B CG  
4546 O OD1 . ASN B 55  ? 0.2202 0.1258 0.1908 0.0151  -0.0112 -0.0194 55  ASN B OD1 
4547 N ND2 . ASN B 55  ? 0.2245 0.1464 0.2024 0.0143  -0.0149 -0.0199 55  ASN B ND2 
4548 N N   . LEU B 56  ? 0.1930 0.1013 0.1547 0.0294  -0.0107 -0.0201 56  LEU B N   
4549 C CA  . LEU B 56  ? 0.1851 0.0934 0.1434 0.0300  -0.0106 -0.0232 56  LEU B CA  
4550 C C   . LEU B 56  ? 0.2077 0.1101 0.1636 0.0230  -0.0109 -0.0269 56  LEU B C   
4551 O O   . LEU B 56  ? 0.2585 0.1481 0.2093 0.0208  -0.0085 -0.0285 56  LEU B O   
4552 C CB  . LEU B 56  ? 0.2197 0.1199 0.1710 0.0373  -0.0073 -0.0235 56  LEU B CB  
4553 C CG  . LEU B 56  ? 0.2985 0.2073 0.2519 0.0449  -0.0070 -0.0194 56  LEU B CG  
4554 C CD1 . LEU B 56  ? 0.2945 0.1934 0.2409 0.0533  -0.0028 -0.0189 56  LEU B CD1 
4555 C CD2 . LEU B 56  ? 0.3366 0.2612 0.2952 0.0449  -0.0093 -0.0192 56  LEU B CD2 
4556 N N   . THR B 57  ? 0.1984 0.1106 0.1576 0.0192  -0.0136 -0.0281 57  THR B N   
4557 C CA  . THR B 57  ? 0.2191 0.1291 0.1757 0.0120  -0.0142 -0.0317 57  THR B CA  
4558 C C   . THR B 57  ? 0.2533 0.1526 0.1994 0.0121  -0.0115 -0.0367 57  THR B C   
4559 O O   . THR B 57  ? 0.2196 0.1191 0.1627 0.0179  -0.0101 -0.0371 57  THR B O   
4560 C CB  . THR B 57  ? 0.2376 0.1629 0.2005 0.0083  -0.0180 -0.0305 57  THR B CB  
4561 O OG1 . THR B 57  ? 0.2318 0.1636 0.1930 0.0113  -0.0187 -0.0306 57  THR B OG1 
4562 C CG2 . THR B 57  ? 0.2040 0.1377 0.1768 0.0090  -0.0195 -0.0256 57  THR B CG2 
4563 N N   . PRO B 58  ? 0.2694 0.1589 0.2097 0.0054  -0.0099 -0.0410 58  PRO B N   
4564 C CA  . PRO B 58  ? 0.2583 0.1344 0.1870 0.0050  -0.0061 -0.0468 58  PRO B CA  
4565 C C   . PRO B 58  ? 0.2268 0.1128 0.1533 0.0043  -0.0077 -0.0496 58  PRO B C   
4566 O O   . PRO B 58  ? 0.2674 0.1454 0.1861 0.0085  -0.0041 -0.0528 58  PRO B O   
4567 C CB  . PRO B 58  ? 0.2753 0.1415 0.1990 -0.0050 -0.0047 -0.0511 58  PRO B CB  
4568 C CG  . PRO B 58  ? 0.2843 0.1538 0.2162 -0.0061 -0.0062 -0.0463 58  PRO B CG  
4569 C CD  . PRO B 58  ? 0.2517 0.1403 0.1948 -0.0019 -0.0107 -0.0410 58  PRO B CD  
4570 N N   . VAL B 59  ? 0.2449 0.1483 0.1778 -0.0005 -0.0127 -0.0480 59  VAL B N   
4571 C CA  . VAL B 59  ? 0.2780 0.1918 0.2081 -0.0013 -0.0143 -0.0499 59  VAL B CA  
4572 C C   . VAL B 59  ? 0.2830 0.2013 0.2154 0.0080  -0.0136 -0.0465 59  VAL B C   
4573 O O   . VAL B 59  ? 0.2618 0.1807 0.1880 0.0099  -0.0120 -0.0495 59  VAL B O   
4574 C CB  . VAL B 59  ? 0.2228 0.1553 0.1595 -0.0078 -0.0198 -0.0475 59  VAL B CB  
4575 C CG1 . VAL B 59  ? 0.2495 0.1924 0.1987 -0.0040 -0.0225 -0.0399 59  VAL B CG1 
4576 C CG2 . VAL B 59  ? 0.2489 0.1927 0.1814 -0.0090 -0.0215 -0.0490 59  VAL B CG2 
4577 N N   . LEU B 60  ? 0.2318 0.1534 0.1725 0.0134  -0.0143 -0.0408 60  LEU B N   
4578 C CA  . LEU B 60  ? 0.2123 0.1380 0.1546 0.0213  -0.0131 -0.0382 60  LEU B CA  
4579 C C   . LEU B 60  ? 0.2710 0.1836 0.2052 0.0274  -0.0080 -0.0413 60  LEU B C   
4580 O O   . LEU B 60  ? 0.2618 0.1776 0.1928 0.0319  -0.0061 -0.0423 60  LEU B O   
4581 C CB  . LEU B 60  ? 0.1923 0.1235 0.1438 0.0244  -0.0145 -0.0324 60  LEU B CB  
4582 C CG  . LEU B 60  ? 0.2053 0.1420 0.1584 0.0316  -0.0131 -0.0299 60  LEU B CG  
4583 C CD1 . LEU B 60  ? 0.2186 0.1668 0.1715 0.0317  -0.0140 -0.0298 60  LEU B CD1 
4584 C CD2 . LEU B 60  ? 0.1846 0.1268 0.1455 0.0328  -0.0144 -0.0252 60  LEU B CD2 
4585 N N   . ILE B 61  ? 0.2413 0.1386 0.1719 0.0279  -0.0051 -0.0423 61  ILE B N   
4586 C CA  . ILE B 61  ? 0.2536 0.1363 0.1764 0.0350  0.0006  -0.0442 61  ILE B CA  
4587 C C   . ILE B 61  ? 0.2606 0.1367 0.1733 0.0336  0.0040  -0.0509 61  ILE B C   
4588 O O   . ILE B 61  ? 0.3054 0.1793 0.2142 0.0414  0.0079  -0.0517 61  ILE B O   
4589 C CB  . ILE B 61  ? 0.2552 0.1207 0.1747 0.0346  0.0034  -0.0438 61  ILE B CB  
4590 C CG1 . ILE B 61  ? 0.2787 0.1512 0.2070 0.0374  0.0009  -0.0371 61  ILE B CG1 
4591 C CG2 . ILE B 61  ? 0.2989 0.1460 0.2088 0.0425  0.0105  -0.0455 61  ILE B CG2 
4592 C CD1 . ILE B 61  ? 0.3060 0.1636 0.2315 0.0353  0.0031  -0.0363 61  ILE B CD1 
4593 N N   . ASP B 62  ? 0.2757 0.1497 0.1838 0.0234  0.0026  -0.0560 62  ASP B N   
4594 C CA  . ASP B 62  ? 0.3166 0.1860 0.2141 0.0200  0.0055  -0.0634 62  ASP B CA  
4595 C C   . ASP B 62  ? 0.3352 0.2192 0.2343 0.0251  0.0047  -0.0623 62  ASP B C   
4596 O O   . ASP B 62  ? 0.3287 0.2060 0.2195 0.0294  0.0098  -0.0666 62  ASP B O   
4597 C CB  . ASP B 62  ? 0.3210 0.1954 0.2162 0.0070  0.0018  -0.0676 62  ASP B CB  
4598 C CG  . ASP B 62  ? 0.3720 0.2287 0.2609 -0.0003 0.0046  -0.0719 62  ASP B CG  
4599 O OD1 . ASP B 62  ? 0.4256 0.2619 0.3087 0.0048  0.0107  -0.0730 62  ASP B OD1 
4600 O OD2 . ASP B 62  ? 0.3622 0.2263 0.2521 -0.0112 0.0009  -0.0738 62  ASP B OD2 
4601 N N   . GLN B 63  ? 0.2788 0.1823 0.1880 0.0245  -0.0010 -0.0566 63  GLN B N   
4602 C CA  . GLN B 63  ? 0.2778 0.1957 0.1884 0.0279  -0.0016 -0.0552 63  GLN B CA  
4603 C C   . GLN B 63  ? 0.2907 0.2085 0.2035 0.0390  0.0020  -0.0523 63  GLN B C   
4604 O O   . GLN B 63  ? 0.2748 0.1957 0.1833 0.0434  0.0053  -0.0545 63  GLN B O   
4605 C CB  . GLN B 63  ? 0.2157 0.1520 0.1359 0.0241  -0.0079 -0.0495 63  GLN B CB  
4606 C CG  . GLN B 63  ? 0.2822 0.2228 0.2021 0.0144  -0.0120 -0.0507 63  GLN B CG  
4607 C CD  . GLN B 63  ? 0.2697 0.2272 0.1997 0.0128  -0.0172 -0.0436 63  GLN B CD  
4608 O OE1 . GLN B 63  ? 0.2889 0.2580 0.2198 0.0140  -0.0183 -0.0411 63  GLN B OE1 
4609 N NE2 . GLN B 63  ? 0.2337 0.1917 0.1711 0.0104  -0.0198 -0.0403 63  GLN B NE2 
4610 N N   . ILE B 64  ? 0.2794 0.1958 0.1992 0.0436  0.0016  -0.0473 64  ILE B N   
4611 C CA  . ILE B 64  ? 0.2523 0.1708 0.1744 0.0542  0.0049  -0.0441 64  ILE B CA  
4612 C C   . ILE B 64  ? 0.3144 0.2174 0.2262 0.0606  0.0121  -0.0488 64  ILE B C   
4613 O O   . ILE B 64  ? 0.2908 0.1994 0.2019 0.0686  0.0156  -0.0485 64  ILE B O   
4614 C CB  . ILE B 64  ? 0.2236 0.1419 0.1529 0.0570  0.0032  -0.0384 64  ILE B CB  
4615 C CG1 . ILE B 64  ? 0.2267 0.1615 0.1661 0.0523  -0.0025 -0.0338 64  ILE B CG1 
4616 C CG2 . ILE B 64  ? 0.2761 0.1948 0.2059 0.0685  0.0073  -0.0352 64  ILE B CG2 
4617 C CD1 . ILE B 64  ? 0.2654 0.2001 0.2108 0.0531  -0.0041 -0.0293 64  ILE B CD1 
4618 N N   . GLN B 65  ? 0.2801 0.1630 0.1834 0.0569  0.0150  -0.0536 65  GLN B N   
4619 C CA  . GLN B 65  ? 0.3379 0.2024 0.2302 0.0628  0.0231  -0.0586 65  GLN B CA  
4620 C C   . GLN B 65  ? 0.3830 0.2514 0.2681 0.0612  0.0255  -0.0648 65  GLN B C   
4621 O O   . GLN B 65  ? 0.3814 0.2452 0.2616 0.0702  0.0320  -0.0666 65  GLN B O   
4622 C CB  . GLN B 65  ? 0.3832 0.2238 0.2667 0.0572  0.0262  -0.0631 65  GLN B CB  
4623 C CG  . GLN B 65  ? 0.3711 0.2061 0.2611 0.0605  0.0263  -0.0562 65  GLN B CG  
4624 C CD  . GLN B 65  ? 0.4433 0.2622 0.3292 0.0510  0.0279  -0.0592 65  GLN B CD  
4625 O OE1 . GLN B 65  ? 0.4525 0.2716 0.3362 0.0401  0.0242  -0.0633 65  GLN B OE1 
4626 N NE2 . GLN B 65  ? 0.4518 0.2578 0.3365 0.0550  0.0334  -0.0570 65  GLN B NE2 
4627 N N   . GLU B 66  ? 0.3474 0.2252 0.2317 0.0501  0.0206  -0.0678 66  GLU B N   
4628 C CA  . GLU B 66  ? 0.3542 0.2370 0.2307 0.0474  0.0225  -0.0737 66  GLU B CA  
4629 C C   . GLU B 66  ? 0.3173 0.2176 0.1996 0.0558  0.0230  -0.0695 66  GLU B C   
4630 O O   . GLU B 66  ? 0.3561 0.2540 0.2312 0.0608  0.0289  -0.0738 66  GLU B O   
4631 C CB  . GLU B 66  ? 0.3201 0.2133 0.1959 0.0342  0.0161  -0.0758 66  GLU B CB  
4632 C CG  . GLU B 66  ? 0.3663 0.2647 0.2321 0.0297  0.0178  -0.0823 66  GLU B CG  
4633 C CD  . GLU B 66  ? 0.4081 0.3117 0.2691 0.0159  0.0130  -0.0862 66  GLU B CD  
4634 O OE1 . GLU B 66  ? 0.3848 0.2908 0.2523 0.0102  0.0078  -0.0830 66  GLU B OE1 
4635 O OE2 . GLU B 66  ? 0.4807 0.3874 0.3314 0.0107  0.0145  -0.0926 66  GLU B OE2 
4636 N N   . TYR B 67  ? 0.3051 0.2228 0.2001 0.0572  0.0174  -0.0615 67  TYR B N   
4637 C CA  . TYR B 67  ? 0.2833 0.2185 0.1842 0.0642  0.0181  -0.0574 67  TYR B CA  
4638 C C   . TYR B 67  ? 0.3242 0.2535 0.2249 0.0771  0.0247  -0.0564 67  TYR B C   
4639 O O   . TYR B 67  ? 0.3326 0.2682 0.2309 0.0836  0.0294  -0.0577 67  TYR B O   
4640 C CB  . TYR B 67  ? 0.2363 0.1888 0.1500 0.0618  0.0114  -0.0496 67  TYR B CB  
4641 C CG  . TYR B 67  ? 0.2877 0.2523 0.2031 0.0523  0.0060  -0.0486 67  TYR B CG  
4642 C CD1 . TYR B 67  ? 0.2894 0.2693 0.2049 0.0521  0.0062  -0.0476 67  TYR B CD1 
4643 C CD2 . TYR B 67  ? 0.2406 0.2024 0.1579 0.0443  0.0011  -0.0478 67  TYR B CD2 
4644 C CE1 . TYR B 67  ? 0.2765 0.2670 0.1932 0.0443  0.0015  -0.0453 67  TYR B CE1 
4645 C CE2 . TYR B 67  ? 0.2935 0.2673 0.2129 0.0371  -0.0036 -0.0455 67  TYR B CE2 
4646 C CZ  . TYR B 67  ? 0.2645 0.2519 0.1832 0.0374  -0.0033 -0.0440 67  TYR B CZ  
4647 O OH  . TYR B 67  ? 0.2757 0.2743 0.1959 0.0311  -0.0075 -0.0406 67  TYR B OH  
4648 N N   . ALA B 68  ? 0.3256 0.2434 0.2285 0.0814  0.0255  -0.0535 68  ALA B N   
4649 C CA  . ALA B 68  ? 0.3488 0.2620 0.2522 0.0948  0.0315  -0.0506 68  ALA B CA  
4650 C C   . ALA B 68  ? 0.3918 0.2901 0.2842 0.1001  0.0402  -0.0569 68  ALA B C   
4651 O O   . ALA B 68  ? 0.3860 0.2908 0.2822 0.1095  0.0447  -0.0535 68  ALA B O   
4652 C CB  . ALA B 68  ? 0.3257 0.2259 0.2309 0.0972  0.0310  -0.0467 68  ALA B CB  
4653 N N   . GLN B 69  ? 0.3720 0.2541 0.2542 0.0910  0.0418  -0.0646 69  GLN B N   
4654 C CA  . GLN B 69  ? 0.4216 0.2910 0.2962 0.0913  0.0495  -0.0704 69  GLN B CA  
4655 C C   . GLN B 69  ? 0.4408 0.3212 0.3099 0.0900  0.0512  -0.0758 69  GLN B C   
4656 O O   . GLN B 69  ? 0.5073 0.3782 0.3693 0.0893  0.0576  -0.0819 69  GLN B O   
4657 C CB  . GLN B 69  ? 0.4919 0.3397 0.3584 0.0809  0.0507  -0.0766 69  GLN B CB  
4658 C CG  . GLN B 69  ? 0.5005 0.3366 0.3716 0.0817  0.0499  -0.0712 69  GLN B CG  
4659 C CD  . GLN B 69  ? 0.6608 0.4789 0.5248 0.0699  0.0501  -0.0771 69  GLN B CD  
4660 O OE1 . GLN B 69  ? 0.6786 0.4916 0.5339 0.0616  0.0519  -0.0857 69  GLN B OE1 
4661 N NE2 . GLN B 69  ? 0.7567 0.5670 0.6245 0.0684  0.0483  -0.0726 69  GLN B NE2 
4662 N N   . GLY B 70  ? 0.4459 0.3465 0.3179 0.0894  0.0458  -0.0739 70  GLY B N   
4663 C CA  . GLY B 70  ? 0.4701 0.3837 0.3376 0.0870  0.0470  -0.0778 70  GLY B CA  
4664 C C   . GLY B 70  ? 0.5004 0.4062 0.3557 0.0743  0.0462  -0.0864 70  GLY B C   
4665 O O   . GLY B 70  ? 0.5660 0.4766 0.4132 0.0729  0.0497  -0.0918 70  GLY B O   
4666 N N   . LYS B 71  ? 0.4670 0.3626 0.3205 0.0645  0.0417  -0.0878 71  LYS B N   
4667 C CA  . LYS B 71  ? 0.5176 0.4085 0.3599 0.0513  0.0402  -0.0957 71  LYS B CA  
4668 C C   . LYS B 71  ? 0.5074 0.4200 0.3566 0.0412  0.0302  -0.0912 71  LYS B C   
4669 O O   . LYS B 71  ? 0.5092 0.4242 0.3501 0.0304  0.0280  -0.0965 71  LYS B O   
4670 C CB  . LYS B 71  ? 0.5038 0.3712 0.3400 0.0453  0.0420  -0.1006 71  LYS B CB  
4671 C CG  . LYS B 71  ? 0.5841 0.4347 0.4222 0.0523  0.0502  -0.1013 71  LYS B CG  
4672 C CD  . LYS B 71  ? 0.6721 0.5050 0.5091 0.0451  0.0499  -0.1031 71  LYS B CD  
4673 C CE  . LYS B 71  ? 0.7270 0.5411 0.5608 0.0491  0.0582  -0.1062 71  LYS B CE  
4674 N NZ  . LYS B 71  ? 0.7917 0.6087 0.6205 0.0544  0.0643  -0.1107 71  LYS B NZ  
4675 N N   . ALA B 72  ? 0.4350 0.3635 0.2986 0.0445  0.0246  -0.0815 72  ALA B N   
4676 C CA  . ALA B 72  ? 0.3990 0.3450 0.2692 0.0360  0.0160  -0.0764 72  ALA B CA  
4677 C C   . ALA B 72  ? 0.3914 0.3552 0.2590 0.0345  0.0155  -0.0759 72  ALA B C   
4678 O O   . ALA B 72  ? 0.4592 0.4320 0.3307 0.0421  0.0183  -0.0728 72  ALA B O   
4679 C CB  . ALA B 72  ? 0.3954 0.3490 0.2805 0.0394  0.0112  -0.0669 72  ALA B CB  
4680 N N   . LYS B 73  ? 0.3929 0.3633 0.2539 0.0245  0.0119  -0.0785 73  LYS B N   
4681 C CA  . LYS B 73  ? 0.4060 0.3947 0.2643 0.0218  0.0104  -0.0767 73  LYS B CA  
4682 C C   . LYS B 73  ? 0.3407 0.3456 0.2109 0.0190  0.0027  -0.0663 73  LYS B C   
4683 O O   . LYS B 73  ? 0.3830 0.3929 0.2532 0.0112  -0.0029 -0.0646 73  LYS B O   
4684 C CB  . LYS B 73  ? 0.4810 0.4690 0.3243 0.0126  0.0111  -0.0852 73  LYS B CB  
4685 C CG  . LYS B 73  ? 0.6818 0.6504 0.5116 0.0147  0.0201  -0.0966 73  LYS B CG  
4686 C CD  . LYS B 73  ? 0.8241 0.7842 0.6401 0.0027  0.0199  -0.1061 73  LYS B CD  
4687 C CE  . LYS B 73  ? 0.8477 0.7889 0.6650 0.0001  0.0198  -0.1086 73  LYS B CE  
4688 N NZ  . LYS B 73  ? 0.8535 0.7731 0.6715 0.0111  0.0277  -0.1104 73  LYS B NZ  
4689 N N   . ASP B 74  ? 0.3279 0.3414 0.2080 0.0253  0.0029  -0.0593 74  ASP B N   
4690 C CA  . ASP B 74  ? 0.2909 0.3156 0.1824 0.0236  -0.0027 -0.0495 74  ASP B CA  
4691 C C   . ASP B 74  ? 0.3687 0.4103 0.2585 0.0212  -0.0037 -0.0450 74  ASP B C   
4692 O O   . ASP B 74  ? 0.3271 0.3749 0.2161 0.0254  0.0004  -0.0449 74  ASP B O   
4693 C CB  . ASP B 74  ? 0.2791 0.3013 0.1817 0.0305  -0.0016 -0.0452 74  ASP B CB  
4694 C CG  . ASP B 74  ? 0.3319 0.3619 0.2456 0.0283  -0.0064 -0.0362 74  ASP B CG  
4695 O OD1 . ASP B 74  ? 0.2599 0.3017 0.1743 0.0251  -0.0083 -0.0311 74  ASP B OD1 
4696 O OD2 . ASP B 74  ? 0.3123 0.3355 0.2334 0.0301  -0.0077 -0.0342 74  ASP B OD2 
4697 N N   . VAL B 75  ? 0.3674 0.4172 0.2569 0.0149  -0.0090 -0.0405 75  VAL B N   
4698 C CA  . VAL B 75  ? 0.3716 0.4369 0.2569 0.0119  -0.0100 -0.0361 75  VAL B CA  
4699 C C   . VAL B 75  ? 0.3558 0.4287 0.2498 0.0153  -0.0089 -0.0279 75  VAL B C   
4700 O O   . VAL B 75  ? 0.3381 0.4199 0.2283 0.0162  -0.0056 -0.0275 75  VAL B O   
4701 C CB  . VAL B 75  ? 0.3884 0.4615 0.2724 0.0052  -0.0161 -0.0319 75  VAL B CB  
4702 C CG1 . VAL B 75  ? 0.4882 0.5770 0.3718 0.0037  -0.0178 -0.0230 75  VAL B CG1 
4703 C CG2 . VAL B 75  ? 0.3592 0.4298 0.2309 -0.0005 -0.0164 -0.0412 75  VAL B CG2 
4704 N N   . PHE B 76  ? 0.2986 0.3683 0.2039 0.0164  -0.0113 -0.0217 76  PHE B N   
4705 C CA  . PHE B 76  ? 0.2872 0.3624 0.2003 0.0181  -0.0099 -0.0147 76  PHE B CA  
4706 C C   . PHE B 76  ? 0.2929 0.3683 0.2074 0.0232  -0.0048 -0.0188 76  PHE B C   
4707 O O   . PHE B 76  ? 0.3070 0.3922 0.2229 0.0235  -0.0021 -0.0156 76  PHE B O   
4708 C CB  . PHE B 76  ? 0.2884 0.3579 0.2122 0.0179  -0.0127 -0.0088 76  PHE B CB  
4709 C CG  . PHE B 76  ? 0.3749 0.4486 0.3000 0.0144  -0.0164 -0.0008 76  PHE B CG  
4710 C CD1 . PHE B 76  ? 0.2938 0.3674 0.2163 0.0121  -0.0205 -0.0013 76  PHE B CD1 
4711 C CD2 . PHE B 76  ? 0.4242 0.5024 0.3532 0.0134  -0.0154 0.0077  76  PHE B CD2 
4712 C CE1 . PHE B 76  ? 0.3638 0.4435 0.2882 0.0102  -0.0238 0.0072  76  PHE B CE1 
4713 C CE2 . PHE B 76  ? 0.4216 0.5025 0.3518 0.0117  -0.0180 0.0162  76  PHE B CE2 
4714 C CZ  . PHE B 76  ? 0.3968 0.4795 0.3251 0.0108  -0.0224 0.0163  76  PHE B CZ  
4715 N N   . LEU B 77  ? 0.2757 0.3410 0.1902 0.0273  -0.0032 -0.0253 77  LEU B N   
4716 C CA  . LEU B 77  ? 0.3072 0.3741 0.2236 0.0336  0.0017  -0.0282 77  LEU B CA  
4717 C C   . LEU B 77  ? 0.3332 0.4077 0.2407 0.0351  0.0064  -0.0323 77  LEU B C   
4718 O O   . LEU B 77  ? 0.3567 0.4402 0.2670 0.0393  0.0105  -0.0318 77  LEU B O   
4719 C CB  . LEU B 77  ? 0.3448 0.3980 0.2623 0.0386  0.0028  -0.0331 77  LEU B CB  
4720 C CG  . LEU B 77  ? 0.4145 0.4703 0.3372 0.0464  0.0070  -0.0336 77  LEU B CG  
4721 C CD1 . LEU B 77  ? 0.3208 0.3887 0.2540 0.0451  0.0056  -0.0266 77  LEU B CD1 
4722 C CD2 . LEU B 77  ? 0.3546 0.3956 0.2780 0.0512  0.0076  -0.0369 77  LEU B CD2 
4723 N N   . GLU B 78  ? 0.3193 0.3918 0.2160 0.0313  0.0058  -0.0364 78  GLU B N   
4724 C CA  . GLU B 78  ? 0.4090 0.4893 0.2959 0.0317  0.0104  -0.0405 78  GLU B CA  
4725 C C   . GLU B 78  ? 0.3506 0.4476 0.2398 0.0291  0.0105  -0.0333 78  GLU B C   
4726 O O   . GLU B 78  ? 0.3685 0.4748 0.2553 0.0320  0.0156  -0.0348 78  GLU B O   
4727 C CB  . GLU B 78  ? 0.4277 0.5035 0.3018 0.0262  0.0091  -0.0464 78  GLU B CB  
4728 C CG  . GLU B 78  ? 0.5872 0.6502 0.4518 0.0296  0.0147  -0.0573 78  GLU B CG  
4729 C CD  . GLU B 78  ? 0.7477 0.8156 0.6102 0.0369  0.0224  -0.0603 78  GLU B CD  
4730 O OE1 . GLU B 78  ? 0.8159 0.8991 0.6761 0.0352  0.0236  -0.0576 78  GLU B OE1 
4731 O OE2 . GLU B 78  ? 0.8171 0.8744 0.6807 0.0448  0.0274  -0.0648 78  GLU B OE2 
4732 N N   . ALA B 79  ? 0.3276 0.4280 0.2215 0.0239  0.0055  -0.0251 79  ALA B N   
4733 C CA  . ALA B 79  ? 0.3142 0.4277 0.2103 0.0210  0.0060  -0.0172 79  ALA B CA  
4734 C C   . ALA B 79  ? 0.3514 0.4699 0.2575 0.0239  0.0091  -0.0145 79  ALA B C   
4735 O O   . ALA B 79  ? 0.2918 0.4221 0.1987 0.0216  0.0115  -0.0099 79  ALA B O   
4736 C CB  . ALA B 79  ? 0.3097 0.4226 0.2085 0.0158  0.0006  -0.0087 79  ALA B CB  
4737 N N   . ILE B 80  ? 0.2678 0.3786 0.1812 0.0282  0.0090  -0.0170 80  ILE B N   
4738 C CA  . ILE B 80  ? 0.2162 0.3344 0.1389 0.0307  0.0116  -0.0151 80  ILE B CA  
4739 C C   . ILE B 80  ? 0.2936 0.4197 0.2139 0.0374  0.0174  -0.0205 80  ILE B C   
4740 O O   . ILE B 80  ? 0.2569 0.3978 0.1812 0.0378  0.0208  -0.0182 80  ILE B O   
4741 C CB  . ILE B 80  ? 0.2278 0.3360 0.1590 0.0324  0.0087  -0.0146 80  ILE B CB  
4742 C CG1 . ILE B 80  ? 0.3621 0.4636 0.2964 0.0262  0.0042  -0.0087 80  ILE B CG1 
4743 C CG2 . ILE B 80  ? 0.2320 0.3499 0.1719 0.0356  0.0114  -0.0138 80  ILE B CG2 
4744 C CD1 . ILE B 80  ? 0.4731 0.5804 0.4151 0.0220  0.0047  -0.0027 80  ILE B CD1 
4745 N N   . ARG B 81  ? 0.2980 0.4144 0.2116 0.0426  0.0192  -0.0278 81  ARG B N   
4746 C CA  . ARG B 81  ? 0.3443 0.4652 0.2563 0.0511  0.0256  -0.0330 81  ARG B CA  
4747 C C   . ARG B 81  ? 0.3179 0.4526 0.2232 0.0502  0.0303  -0.0340 81  ARG B C   
4748 O O   . ARG B 81  ? 0.3398 0.4882 0.2491 0.0552  0.0353  -0.0338 81  ARG B O   
4749 C CB  . ARG B 81  ? 0.2983 0.4012 0.2032 0.0564  0.0273  -0.0407 81  ARG B CB  
4750 C CG  . ARG B 81  ? 0.4357 0.5402 0.3380 0.0667  0.0352  -0.0461 81  ARG B CG  
4751 C CD  . ARG B 81  ? 0.4728 0.5558 0.3662 0.0711  0.0380  -0.0540 81  ARG B CD  
4752 N NE  . ARG B 81  ? 0.5328 0.6039 0.4331 0.0753  0.0358  -0.0525 81  ARG B NE  
4753 C CZ  . ARG B 81  ? 0.5544 0.6289 0.4626 0.0851  0.0390  -0.0504 81  ARG B CZ  
4754 N NH1 . ARG B 81  ? 0.6076 0.6982 0.5188 0.0921  0.0445  -0.0495 81  ARG B NH1 
4755 N NH2 . ARG B 81  ? 0.5203 0.5837 0.4334 0.0881  0.0366  -0.0486 81  ARG B NH2 
4756 N N   . LYS B 82  ? 0.3122 0.4455 0.2074 0.0438  0.0287  -0.0347 82  LYS B N   
4757 C CA  . LYS B 82  ? 0.2873 0.4324 0.1737 0.0427  0.0334  -0.0366 82  LYS B CA  
4758 C C   . LYS B 82  ? 0.2907 0.4553 0.1843 0.0413  0.0357  -0.0302 82  LYS B C   
4759 O O   . LYS B 82  ? 0.2703 0.4386 0.1728 0.0366  0.0321  -0.0228 82  LYS B O   
4760 C CB  . LYS B 82  ? 0.2945 0.4379 0.1701 0.0344  0.0296  -0.0358 82  LYS B CB  
4761 C CG  . LYS B 82  ? 0.4444 0.5733 0.3092 0.0339  0.0288  -0.0440 82  LYS B CG  
4762 C CD  . LYS B 82  ? 0.4258 0.5601 0.2798 0.0254  0.0255  -0.0424 82  LYS B CD  
4763 C CE  . LYS B 82  ? 0.5582 0.6799 0.4026 0.0221  0.0228  -0.0495 82  LYS B CE  
4764 N NZ  . LYS B 82  ? 0.5847 0.7156 0.4201 0.0135  0.0183  -0.0461 82  LYS B NZ  
4765 N N   . ASP B 83  ? 0.3005 0.4771 0.1898 0.0448  0.0424  -0.0334 83  ASP B N   
4766 C CA  . ASP B 83  ? 0.3092 0.5057 0.2016 0.0408  0.0449  -0.0276 83  ASP B CA  
4767 C C   . ASP B 83  ? 0.2791 0.4754 0.1658 0.0305  0.0404  -0.0213 83  ASP B C   
4768 O O   . ASP B 83  ? 0.2981 0.4867 0.1736 0.0280  0.0384  -0.0240 83  ASP B O   
4769 C CB  . ASP B 83  ? 0.3555 0.5641 0.2415 0.0459  0.0531  -0.0329 83  ASP B CB  
4770 C CG  . ASP B 83  ? 0.4441 0.6729 0.3373 0.0423  0.0558  -0.0268 83  ASP B CG  
4771 O OD1 . ASP B 83  ? 0.3687 0.6030 0.2588 0.0331  0.0537  -0.0207 83  ASP B OD1 
4772 O OD2 . ASP B 83  ? 0.4594 0.6986 0.3613 0.0486  0.0601  -0.0277 83  ASP B OD2 
4773 N N   . PRO B 84  ? 0.2838 0.4880 0.1777 0.0243  0.0387  -0.0126 84  PRO B N   
4774 C CA  . PRO B 84  ? 0.2685 0.4705 0.1571 0.0158  0.0349  -0.0052 84  PRO B CA  
4775 C C   . PRO B 84  ? 0.3265 0.5367 0.2016 0.0132  0.0375  -0.0059 84  PRO B C   
4776 O O   . PRO B 84  ? 0.3659 0.5718 0.2337 0.0083  0.0334  -0.0017 84  PRO B O   
4777 C CB  . PRO B 84  ? 0.3387 0.5484 0.2369 0.0102  0.0356  0.0031  84  PRO B CB  
4778 C CG  . PRO B 84  ? 0.2528 0.4616 0.1630 0.0150  0.0356  0.0000  84  PRO B CG  
4779 C CD  . PRO B 84  ? 0.2600 0.4727 0.1674 0.0244  0.0397  -0.0089 84  PRO B CD  
4780 N N   . ASP B 85  ? 0.3493 0.5711 0.2209 0.0167  0.0440  -0.0111 85  ASP B N   
4781 C CA  . ASP B 85  ? 0.3953 0.6198 0.2565 0.0141  0.0457  -0.0130 85  ASP B CA  
4782 C C   . ASP B 85  ? 0.3007 0.5122 0.1508 0.0144  0.0426  -0.0195 85  ASP B C   
4783 O O   . ASP B 85  ? 0.3084 0.5211 0.1487 0.0098  0.0416  -0.0190 85  ASP B O   
4784 C CB  . ASP B 85  ? 0.4680 0.7019 0.3309 0.0188  0.0529  -0.0183 85  ASP B CB  
4785 C CG  . ASP B 85  ? 0.4833 0.7336 0.3551 0.0155  0.0559  -0.0114 85  ASP B CG  
4786 O OD1 . ASP B 85  ? 0.3979 0.6507 0.2713 0.0080  0.0532  -0.0024 85  ASP B OD1 
4787 O OD2 . ASP B 85  ? 0.4468 0.7069 0.3237 0.0203  0.0613  -0.0149 85  ASP B OD2 
4788 N N   . ASP B 86  ? 0.2966 0.4963 0.1479 0.0195  0.0412  -0.0257 86  ASP B N   
4789 C CA  . ASP B 86  ? 0.3530 0.5394 0.1943 0.0189  0.0385  -0.0327 86  ASP B CA  
4790 C C   . ASP B 86  ? 0.3340 0.5147 0.1749 0.0141  0.0304  -0.0273 86  ASP B C   
4791 O O   . ASP B 86  ? 0.3654 0.5368 0.1990 0.0121  0.0272  -0.0324 86  ASP B O   
4792 C CB  . ASP B 86  ? 0.3774 0.5517 0.2194 0.0271  0.0423  -0.0430 86  ASP B CB  
4793 C CG  . ASP B 86  ? 0.4765 0.6555 0.3201 0.0338  0.0507  -0.0477 86  ASP B CG  
4794 O OD1 . ASP B 86  ? 0.5129 0.7024 0.3528 0.0308  0.0537  -0.0462 86  ASP B OD1 
4795 O OD2 . ASP B 86  ? 0.4915 0.6638 0.3404 0.0424  0.0543  -0.0524 86  ASP B OD2 
4796 N N   . LEU B 87  ? 0.2746 0.4576 0.1260 0.0117  0.0270  -0.0169 87  LEU B N   
4797 C CA  . LEU B 87  ? 0.2650 0.4393 0.1199 0.0083  0.0196  -0.0108 87  LEU B CA  
4798 C C   . LEU B 87  ? 0.3071 0.4881 0.1510 0.0023  0.0160  -0.0062 87  LEU B C   
4799 O O   . LEU B 87  ? 0.3019 0.4942 0.1412 -0.0009 0.0181  -0.0008 87  LEU B O   
4800 C CB  . LEU B 87  ? 0.2526 0.4264 0.1206 0.0072  0.0183  -0.0011 87  LEU B CB  
4801 C CG  . LEU B 87  ? 0.2413 0.4073 0.1215 0.0120  0.0190  -0.0042 87  LEU B CG  
4802 C CD1 . LEU B 87  ? 0.2808 0.4479 0.1718 0.0090  0.0186  0.0047  87  LEU B CD1 
4803 C CD2 . LEU B 87  ? 0.2826 0.4335 0.1642 0.0142  0.0145  -0.0087 87  LEU B CD2 
4804 N N   . GLU B 88  ? 0.2901 0.4639 0.1310 0.0005  0.0103  -0.0078 88  GLU B N   
4805 C CA  . GLU B 88  ? 0.3344 0.5152 0.1686 -0.0048 0.0053  -0.0011 88  GLU B CA  
4806 C C   . GLU B 88  ? 0.2733 0.4552 0.1159 -0.0055 0.0022  0.0131  88  GLU B C   
4807 O O   . GLU B 88  ? 0.2616 0.4337 0.1166 -0.0029 0.0021  0.0155  88  GLU B O   
4808 C CB  . GLU B 88  ? 0.3528 0.5270 0.1831 -0.0067 0.0002  -0.0072 88  GLU B CB  
4809 C CG  . GLU B 88  ? 0.4031 0.5691 0.2263 -0.0056 0.0043  -0.0221 88  GLU B CG  
4810 C CD  . GLU B 88  ? 0.5042 0.6609 0.3248 -0.0081 -0.0001 -0.0286 88  GLU B CD  
4811 O OE1 . GLU B 88  ? 0.5768 0.7259 0.3890 -0.0094 0.0030  -0.0401 88  GLU B OE1 
4812 O OE2 . GLU B 88  ? 0.4681 0.6246 0.2951 -0.0090 -0.0061 -0.0222 88  GLU B OE2 
4813 N N   . LYS B 89  ? 0.2810 0.4713 0.1197 -0.0090 0.0000  0.0222  89  LYS B N   
4814 C CA  . LYS B 89  ? 0.3633 0.5531 0.2081 -0.0092 -0.0023 0.0365  89  LYS B CA  
4815 C C   . LYS B 89  ? 0.3686 0.5475 0.2226 -0.0068 -0.0072 0.0378  89  LYS B C   
4816 O O   . LYS B 89  ? 0.3368 0.5061 0.2017 -0.0050 -0.0064 0.0440  89  LYS B O   
4817 C CB  . LYS B 89  ? 0.3148 0.5128 0.1551 -0.0120 -0.0047 0.0453  89  LYS B CB  
4818 C CG  . LYS B 89  ? 0.3898 0.5970 0.2220 -0.0148 -0.0005 0.0427  89  LYS B CG  
4819 C CD  . LYS B 89  ? 0.4503 0.6663 0.2779 -0.0173 -0.0036 0.0517  89  LYS B CD  
4820 C CE  . LYS B 89  ? 0.4933 0.7191 0.3113 -0.0205 -0.0001 0.0476  89  LYS B CE  
4821 N NZ  . LYS B 89  ? 0.4870 0.7136 0.3057 -0.0205 0.0069  0.0473  89  LYS B NZ  
4822 N N   . GLU B 90  ? 0.2941 0.4729 0.1446 -0.0074 -0.0117 0.0312  90  GLU B N   
4823 C CA  . GLU B 90  ? 0.2905 0.4591 0.1507 -0.0054 -0.0161 0.0318  90  GLU B CA  
4824 C C   . GLU B 90  ? 0.2840 0.4377 0.1547 -0.0020 -0.0133 0.0256  90  GLU B C   
4825 O O   . GLU B 90  ? 0.2999 0.4441 0.1810 0.0001  -0.0153 0.0295  90  GLU B O   
4826 C CB  . GLU B 90  ? 0.3728 0.5457 0.2262 -0.0082 -0.0210 0.0246  90  GLU B CB  
4827 C CG  . GLU B 90  ? 0.5421 0.7278 0.3899 -0.0118 -0.0242 0.0302  90  GLU B CG  
4828 C CD  . GLU B 90  ? 0.6770 0.8653 0.5217 -0.0158 -0.0287 0.0228  90  GLU B CD  
4829 O OE1 . GLU B 90  ? 0.7272 0.9263 0.5712 -0.0183 -0.0325 0.0286  90  GLU B OE1 
4830 O OE2 . GLU B 90  ? 0.7293 0.9088 0.5722 -0.0165 -0.0281 0.0113  90  GLU B OE2 
4831 N N   . GLU B 91  ? 0.3090 0.4612 0.1772 -0.0009 -0.0084 0.0163  91  GLU B N   
4832 C CA  . GLU B 91  ? 0.2799 0.4207 0.1579 0.0028  -0.0058 0.0114  91  GLU B CA  
4833 C C   . GLU B 91  ? 0.2619 0.4020 0.1486 0.0031  -0.0030 0.0195  91  GLU B C   
4834 O O   . GLU B 91  ? 0.2662 0.3967 0.1631 0.0048  -0.0031 0.0199  91  GLU B O   
4835 C CB  . GLU B 91  ? 0.2771 0.4179 0.1499 0.0051  -0.0011 -0.0003 91  GLU B CB  
4836 C CG  . GLU B 91  ? 0.2955 0.4305 0.1607 0.0047  -0.0028 -0.0105 91  GLU B CG  
4837 C CD  . GLU B 91  ? 0.3786 0.5121 0.2365 0.0076  0.0033  -0.0216 91  GLU B CD  
4838 O OE1 . GLU B 91  ? 0.3248 0.4689 0.1761 0.0072  0.0074  -0.0219 91  GLU B OE1 
4839 O OE2 . GLU B 91  ? 0.3961 0.5173 0.2549 0.0107  0.0044  -0.0298 91  GLU B OE2 
4840 N N   . VAL B 92  ? 0.2739 0.4239 0.1560 0.0005  -0.0001 0.0256  92  VAL B N   
4841 C CA  . VAL B 92  ? 0.3015 0.4497 0.1907 -0.0010 0.0028  0.0339  92  VAL B CA  
4842 C C   . VAL B 92  ? 0.2892 0.4275 0.1847 -0.0011 -0.0005 0.0428  92  VAL B C   
4843 O O   . VAL B 92  ? 0.2658 0.3945 0.1704 -0.0011 0.0009  0.0449  92  VAL B O   
4844 C CB  . VAL B 92  ? 0.2884 0.4487 0.1701 -0.0045 0.0067  0.0396  92  VAL B CB  
4845 C CG1 . VAL B 92  ? 0.3088 0.4656 0.1971 -0.0076 0.0104  0.0482  92  VAL B CG1 
4846 C CG2 . VAL B 92  ? 0.3176 0.4879 0.1939 -0.0036 0.0109  0.0302  92  VAL B CG2 
4847 N N   . GLU B 93  ? 0.3016 0.4429 0.1921 -0.0010 -0.0049 0.0479  93  GLU B N   
4848 C CA  . GLU B 93  ? 0.2978 0.4312 0.1946 0.0005  -0.0079 0.0567  93  GLU B CA  
4849 C C   . GLU B 93  ? 0.2824 0.4033 0.1889 0.0029  -0.0096 0.0509  93  GLU B C   
4850 O O   . GLU B 93  ? 0.2954 0.4054 0.2100 0.0036  -0.0083 0.0557  93  GLU B O   
4851 C CB  . GLU B 93  ? 0.3225 0.4656 0.2127 0.0008  -0.0131 0.0617  93  GLU B CB  
4852 C CG  . GLU B 93  ? 0.5335 0.6881 0.4148 -0.0011 -0.0118 0.0716  93  GLU B CG  
4853 C CD  . GLU B 93  ? 0.6164 0.7855 0.4894 -0.0016 -0.0174 0.0745  93  GLU B CD  
4854 O OE1 . GLU B 93  ? 0.6778 0.8466 0.5545 0.0000  -0.0225 0.0730  93  GLU B OE1 
4855 O OE2 . GLU B 93  ? 0.7334 0.9137 0.5976 -0.0040 -0.0166 0.0776  93  GLU B OE2 
4856 N N   . LYS B 94  ? 0.2775 0.3987 0.1825 0.0040  -0.0120 0.0403  94  LYS B N   
4857 C CA  . LYS B 94  ? 0.3166 0.4264 0.2300 0.0062  -0.0134 0.0346  94  LYS B CA  
4858 C C   . LYS B 94  ? 0.2809 0.3832 0.2016 0.0065  -0.0092 0.0329  94  LYS B C   
4859 O O   . LYS B 94  ? 0.2497 0.3417 0.1786 0.0074  -0.0095 0.0340  94  LYS B O   
4860 C CB  . LYS B 94  ? 0.3526 0.4630 0.2613 0.0068  -0.0152 0.0233  94  LYS B CB  
4861 C CG  . LYS B 94  ? 0.3915 0.5074 0.2949 0.0052  -0.0203 0.0234  94  LYS B CG  
4862 C CD  . LYS B 94  ? 0.5405 0.6525 0.4396 0.0047  -0.0212 0.0113  94  LYS B CD  
4863 C CE  . LYS B 94  ? 0.6189 0.7374 0.5133 0.0014  -0.0265 0.0110  94  LYS B CE  
4864 N NZ  . LYS B 94  ? 0.6238 0.7582 0.5090 -0.0017 -0.0280 0.0163  94  LYS B NZ  
4865 N N   . LEU B 95  ? 0.2556 0.3646 0.1734 0.0055  -0.0051 0.0296  95  LEU B N   
4866 C CA  . LEU B 95  ? 0.2820 0.3880 0.2067 0.0050  -0.0014 0.0279  95  LEU B CA  
4867 C C   . LEU B 95  ? 0.2553 0.3548 0.1851 0.0018  0.0004  0.0367  95  LEU B C   
4868 O O   . LEU B 95  ? 0.2660 0.3570 0.2033 0.0012  0.0013  0.0357  95  LEU B O   
4869 C CB  . LEU B 95  ? 0.2820 0.3999 0.2027 0.0045  0.0028  0.0241  95  LEU B CB  
4870 C CG  . LEU B 95  ? 0.4238 0.5447 0.3512 0.0043  0.0065  0.0208  95  LEU B CG  
4871 C CD1 . LEU B 95  ? 0.4671 0.5823 0.3994 0.0091  0.0050  0.0132  95  LEU B CD1 
4872 C CD2 . LEU B 95  ? 0.4817 0.6176 0.4046 0.0038  0.0110  0.0189  95  LEU B CD2 
4873 N N   . ILE B 96  ? 0.2739 0.3764 0.1989 -0.0005 0.0015  0.0455  96  ILE B N   
4874 C CA  . ILE B 96  ? 0.2522 0.3459 0.1806 -0.0036 0.0046  0.0544  96  ILE B CA  
4875 C C   . ILE B 96  ? 0.2773 0.3579 0.2114 -0.0008 0.0021  0.0578  96  ILE B C   
4876 O O   . ILE B 96  ? 0.2909 0.3597 0.2308 -0.0025 0.0048  0.0592  96  ILE B O   
4877 C CB  . ILE B 96  ? 0.2782 0.3780 0.1992 -0.0060 0.0069  0.0638  96  ILE B CB  
4878 C CG1 . ILE B 96  ? 0.3416 0.4538 0.2585 -0.0097 0.0109  0.0605  96  ILE B CG1 
4879 C CG2 . ILE B 96  ? 0.3001 0.3868 0.2235 -0.0082 0.0105  0.0742  96  ILE B CG2 
4880 C CD1 . ILE B 96  ? 0.3766 0.4986 0.2840 -0.0116 0.0125  0.0679  96  ILE B CD1 
4881 N N   . GLU B 97  ? 0.3210 0.4041 0.2532 0.0031  -0.0029 0.0585  97  GLU B N   
4882 C CA  . GLU B 97  ? 0.3159 0.3891 0.2543 0.0063  -0.0054 0.0613  97  GLU B CA  
4883 C C   . GLU B 97  ? 0.2883 0.3527 0.2338 0.0067  -0.0055 0.0530  97  GLU B C   
4884 O O   . GLU B 97  ? 0.3128 0.3653 0.2644 0.0073  -0.0043 0.0555  97  GLU B O   
4885 C CB  . GLU B 97  ? 0.3328 0.4144 0.2682 0.0094  -0.0112 0.0620  97  GLU B CB  
4886 C CG  . GLU B 97  ? 0.5811 0.6735 0.5094 0.0096  -0.0123 0.0713  97  GLU B CG  
4887 C CD  . GLU B 97  ? 0.7818 0.8857 0.7067 0.0111  -0.0185 0.0698  97  GLU B CD  
4888 O OE1 . GLU B 97  ? 0.8216 0.9218 0.7527 0.0134  -0.0217 0.0686  97  GLU B OE1 
4889 O OE2 . GLU B 97  ? 0.8457 0.9631 0.7614 0.0091  -0.0201 0.0693  97  GLU B OE2 
4890 N N   . PHE B 98  ? 0.2429 0.3128 0.1873 0.0068  -0.0068 0.0432  98  PHE B N   
4891 C CA  . PHE B 98  ? 0.2514 0.3141 0.2019 0.0076  -0.0070 0.0360  98  PHE B CA  
4892 C C   . PHE B 98  ? 0.2719 0.3289 0.2268 0.0040  -0.0024 0.0369  98  PHE B C   
4893 O O   . PHE B 98  ? 0.2411 0.2882 0.2018 0.0037  -0.0020 0.0357  98  PHE B O   
4894 C CB  . PHE B 98  ? 0.2667 0.3359 0.2142 0.0093  -0.0081 0.0265  98  PHE B CB  
4895 C CG  . PHE B 98  ? 0.2484 0.3106 0.2013 0.0113  -0.0091 0.0200  98  PHE B CG  
4896 C CD1 . PHE B 98  ? 0.2064 0.2624 0.1608 0.0134  -0.0126 0.0180  98  PHE B CD1 
4897 C CD2 . PHE B 98  ? 0.2399 0.3034 0.1962 0.0109  -0.0065 0.0161  98  PHE B CD2 
4898 C CE1 . PHE B 98  ? 0.2230 0.2721 0.1816 0.0152  -0.0132 0.0126  98  PHE B CE1 
4899 C CE2 . PHE B 98  ? 0.2269 0.2848 0.1875 0.0132  -0.0074 0.0109  98  PHE B CE2 
4900 C CZ  . PHE B 98  ? 0.2728 0.3226 0.2343 0.0153  -0.0106 0.0093  98  PHE B CZ  
4901 N N   . THR B 99  ? 0.2517 0.3154 0.2035 0.0003  0.0012  0.0388  99  THR B N   
4902 C CA  . THR B 99  ? 0.2396 0.2993 0.1949 -0.0051 0.0058  0.0396  99  THR B CA  
4903 C C   . THR B 99  ? 0.2573 0.3018 0.2145 -0.0068 0.0082  0.0466  99  THR B C   
4904 O O   . THR B 99  ? 0.2756 0.3105 0.2373 -0.0098 0.0105  0.0447  99  THR B O   
4905 C CB  . THR B 99  ? 0.2583 0.3292 0.2095 -0.0094 0.0095  0.0412  99  THR B CB  
4906 O OG1 . THR B 99  ? 0.2505 0.3353 0.1995 -0.0065 0.0080  0.0348  99  THR B OG1 
4907 C CG2 . THR B 99  ? 0.2556 0.3246 0.2104 -0.0165 0.0141  0.0404  99  THR B CG2 
4908 N N   . LYS B 100 ? 0.2699 0.3123 0.2236 -0.0048 0.0081  0.0551  100 LYS B N   
4909 C CA  . LYS B 100 ? 0.3223 0.3493 0.2775 -0.0049 0.0115  0.0632  100 LYS B CA  
4910 C C   . LYS B 100 ? 0.2898 0.3064 0.2513 -0.0013 0.0097  0.0606  100 LYS B C   
4911 O O   . LYS B 100 ? 0.3161 0.3178 0.2804 -0.0031 0.0140  0.0625  100 LYS B O   
4912 C CB  . LYS B 100 ? 0.3710 0.4006 0.3215 -0.0014 0.0109  0.0737  100 LYS B CB  
4913 C CG  . LYS B 100 ? 0.4983 0.5259 0.4435 -0.0062 0.0167  0.0812  100 LYS B CG  
4914 C CD  . LYS B 100 ? 0.5860 0.6223 0.5249 -0.0028 0.0151  0.0907  100 LYS B CD  
4915 C CE  . LYS B 100 ? 0.6601 0.6933 0.5930 -0.0079 0.0215  0.0986  100 LYS B CE  
4916 N NZ  . LYS B 100 ? 0.7110 0.7570 0.6364 -0.0055 0.0196  0.1068  100 LYS B NZ  
4917 N N   . LEU B 101 ? 0.2724 0.2959 0.2355 0.0033  0.0038  0.0560  101 LEU B N   
4918 C CA  . LEU B 101 ? 0.2902 0.3053 0.2591 0.0066  0.0020  0.0534  101 LEU B CA  
4919 C C   . LEU B 101 ? 0.2556 0.2637 0.2282 0.0028  0.0043  0.0462  101 LEU B C   
4920 O O   . LEU B 101 ? 0.2638 0.2600 0.2405 0.0032  0.0061  0.0462  101 LEU B O   
4921 C CB  . LEU B 101 ? 0.3254 0.3502 0.2942 0.0107  -0.0044 0.0492  101 LEU B CB  
4922 C CG  . LEU B 101 ? 0.3258 0.3442 0.3005 0.0134  -0.0067 0.0454  101 LEU B CG  
4923 C CD1 . LEU B 101 ? 0.3531 0.3639 0.3319 0.0169  -0.0055 0.0535  101 LEU B CD1 
4924 C CD2 . LEU B 101 ? 0.2957 0.3230 0.2689 0.0153  -0.0121 0.0392  101 LEU B CD2 
4925 N N   . ASN B 102 ? 0.2161 0.2327 0.1872 -0.0008 0.0045  0.0402  102 ASN B N   
4926 C CA  . ASN B 102 ? 0.1956 0.2105 0.1700 -0.0043 0.0057  0.0332  102 ASN B CA  
4927 C C   . ASN B 102 ? 0.2833 0.2944 0.2570 -0.0122 0.0115  0.0341  102 ASN B C   
4928 O O   . ASN B 102 ? 0.2819 0.2927 0.2579 -0.0165 0.0127  0.0286  102 ASN B O   
4929 C CB  . ASN B 102 ? 0.2473 0.2758 0.2212 -0.0024 0.0024  0.0263  102 ASN B CB  
4930 C CG  . ASN B 102 ? 0.2870 0.3155 0.2615 0.0038  -0.0025 0.0233  102 ASN B CG  
4931 O OD1 . ASN B 102 ? 0.2800 0.3006 0.2582 0.0051  -0.0036 0.0214  102 ASN B OD1 
4932 N ND2 . ASN B 102 ? 0.2752 0.3124 0.2455 0.0067  -0.0050 0.0224  102 ASN B ND2 
4933 N N   . TYR B 103 ? 0.2688 0.2740 0.2736 0.0283  0.0261  0.0251  103 TYR B N   
4934 C CA  . TYR B 103 ? 0.2545 0.2348 0.2552 0.0193  0.0331  0.0274  103 TYR B CA  
4935 C C   . TYR B 103 ? 0.3065 0.2479 0.2991 0.0072  0.0452  0.0149  103 TYR B C   
4936 O O   . TYR B 103 ? 0.3882 0.3167 0.3724 -0.0118 0.0453  0.0070  103 TYR B O   
4937 C CB  . TYR B 103 ? 0.3247 0.3043 0.3333 0.0336  0.0414  0.0483  103 TYR B CB  
4938 C CG  . TYR B 103 ? 0.3769 0.3303 0.3821 0.0238  0.0510  0.0535  103 TYR B CG  
4939 C CD1 . TYR B 103 ? 0.3742 0.3454 0.3774 0.0137  0.0425  0.0553  103 TYR B CD1 
4940 C CD2 . TYR B 103 ? 0.4206 0.3296 0.4243 0.0241  0.0713  0.0567  103 TYR B CD2 
4941 C CE1 . TYR B 103 ? 0.4241 0.3754 0.4260 0.0019  0.0519  0.0605  103 TYR B CE1 
4942 C CE2 . TYR B 103 ? 0.4618 0.3432 0.4610 0.0110  0.0822  0.0604  103 TYR B CE2 
4943 C CZ  . TYR B 103 ? 0.4796 0.3852 0.4789 -0.0013 0.0713  0.0625  103 TYR B CZ  
4944 O OH  . TYR B 103 ? 0.4289 0.3110 0.4253 -0.0173 0.0826  0.0663  103 TYR B OH  
4945 N N   . GLU B 104 ? 0.2952 0.2202 0.2894 0.0164  0.0563  0.0125  104 GLU B N   
4946 C CA  . GLU B 104 ? 0.3309 0.2123 0.3132 0.0053  0.0724  -0.0007 104 GLU B CA  
4947 C C   . GLU B 104 ? 0.3301 0.2143 0.2990 -0.0113 0.0651  -0.0207 104 GLU B C   
4948 O O   . GLU B 104 ? 0.3549 0.2060 0.3085 -0.0253 0.0770  -0.0352 104 GLU B O   
4949 C CB  . GLU B 104 ? 0.3857 0.2432 0.3752 0.0262  0.0933  0.0076  104 GLU B CB  
4950 C CG  . GLU B 104 ? 0.5944 0.4474 0.5966 0.0463  0.1038  0.0322  104 GLU B CG  
4951 C CD  . GLU B 104 ? 0.7206 0.5276 0.7121 0.0331  0.1191  0.0324  104 GLU B CD  
4952 O OE1 . GLU B 104 ? 0.7965 0.6033 0.7960 0.0449  0.1242  0.0534  104 GLU B OE1 
4953 O OE2 . GLU B 104 ? 0.8044 0.5769 0.7782 0.0089  0.1263  0.0115  104 GLU B OE2 
4954 N N   . LYS B 105 ? 0.3240 0.2439 0.2954 -0.0107 0.0478  -0.0220 105 LYS B N   
4955 C CA  . LYS B 105 ? 0.3248 0.2482 0.2831 -0.0236 0.0419  -0.0368 105 LYS B CA  
4956 C C   . LYS B 105 ? 0.3716 0.2958 0.3174 -0.0458 0.0351  -0.0441 105 LYS B C   
4957 O O   . LYS B 105 ? 0.3074 0.2467 0.2594 -0.0485 0.0278  -0.0359 105 LYS B O   
4958 C CB  . LYS B 105 ? 0.2497 0.2055 0.2136 -0.0161 0.0288  -0.0342 105 LYS B CB  
4959 C CG  . LYS B 105 ? 0.2672 0.2331 0.2444 0.0010  0.0337  -0.0280 105 LYS B CG  
4960 C CD  . LYS B 105 ? 0.2445 0.2410 0.2254 0.0031  0.0217  -0.0269 105 LYS B CD  
4961 C CE  . LYS B 105 ? 0.2378 0.2542 0.2335 0.0156  0.0254  -0.0209 105 LYS B CE  
4962 N NZ  . LYS B 105 ? 0.2421 0.2855 0.2383 0.0116  0.0154  -0.0232 105 LYS B NZ  
4963 N N   . PRO B 106 ? 0.3085 0.2216 0.2365 -0.0627 0.0373  -0.0587 106 PRO B N   
4964 C CA  . PRO B 106 ? 0.3166 0.2422 0.2335 -0.0863 0.0289  -0.0643 106 PRO B CA  
4965 C C   . PRO B 106 ? 0.2829 0.2509 0.2090 -0.0825 0.0110  -0.0530 106 PRO B C   
4966 O O   . PRO B 106 ? 0.3475 0.3339 0.2755 -0.0953 0.0046  -0.0495 106 PRO B O   
4967 C CB  . PRO B 106 ? 0.4386 0.3545 0.3328 -0.1018 0.0322  -0.0808 106 PRO B CB  
4968 C CG  . PRO B 106 ? 0.4454 0.3245 0.3375 -0.0899 0.0511  -0.0869 106 PRO B CG  
4969 C CD  . PRO B 106 ? 0.3423 0.2332 0.2587 -0.0624 0.0494  -0.0705 106 PRO B CD  
4970 N N   . ILE B 107 ? 0.2740 0.2573 0.2059 -0.0656 0.0048  -0.0470 107 ILE B N   
4971 C CA  . ILE B 107 ? 0.2468 0.2618 0.1849 -0.0598 -0.0071 -0.0364 107 ILE B CA  
4972 C C   . ILE B 107 ? 0.2727 0.2966 0.2254 -0.0515 -0.0082 -0.0255 107 ILE B C   
4973 O O   . ILE B 107 ? 0.2647 0.3137 0.2226 -0.0481 -0.0151 -0.0166 107 ILE B O   
4974 C CB  . ILE B 107 ? 0.2241 0.2446 0.1607 -0.0465 -0.0097 -0.0343 107 ILE B CB  
4975 C CG1 . ILE B 107 ? 0.2353 0.2431 0.1798 -0.0338 -0.0036 -0.0349 107 ILE B CG1 
4976 C CG2 . ILE B 107 ? 0.2534 0.2725 0.1739 -0.0551 -0.0099 -0.0415 107 ILE B CG2 
4977 C CD1 . ILE B 107 ? 0.3059 0.3210 0.2499 -0.0246 -0.0059 -0.0329 107 ILE B CD1 
4978 N N   . TYR B 108 ? 0.2409 0.2457 0.1996 -0.0470 0.0001  -0.0241 108 TYR B N   
4979 C CA  . TYR B 108 ? 0.2705 0.2836 0.2403 -0.0404 0.0002  -0.0126 108 TYR B CA  
4980 C C   . TYR B 108 ? 0.2566 0.2623 0.2273 -0.0564 0.0051  -0.0115 108 TYR B C   
4981 O O   . TYR B 108 ? 0.3086 0.3142 0.2874 -0.0518 0.0089  -0.0013 108 TYR B O   
4982 C CB  . TYR B 108 ? 0.3176 0.3215 0.2940 -0.0240 0.0060  -0.0069 108 TYR B CB  
4983 C CG  . TYR B 108 ? 0.2229 0.2475 0.2013 -0.0116 -0.0010 -0.0038 108 TYR B CG  
4984 C CD1 . TYR B 108 ? 0.2335 0.2598 0.2063 -0.0104 -0.0038 -0.0115 108 TYR B CD1 
4985 C CD2 . TYR B 108 ? 0.2456 0.2858 0.2283 -0.0037 -0.0030 0.0057  108 TYR B CD2 
4986 C CE1 . TYR B 108 ? 0.2281 0.2672 0.1993 -0.0036 -0.0074 -0.0113 108 TYR B CE1 
4987 C CE2 . TYR B 108 ? 0.2090 0.2638 0.1881 0.0034  -0.0072 0.0048  108 TYR B CE2 
4988 C CZ  . TYR B 108 ? 0.2431 0.2953 0.2163 0.0024  -0.0089 -0.0045 108 TYR B CZ  
4989 O OH  . TYR B 108 ? 0.2579 0.3185 0.2246 0.0054  -0.0103 -0.0078 108 TYR B OH  
4990 N N   . ARG B 109 ? 0.3059 0.3067 0.2666 -0.0775 0.0055  -0.0220 109 ARG B N   
4991 C CA  . ARG B 109 ? 0.3511 0.3405 0.3095 -0.0995 0.0122  -0.0248 109 ARG B CA  
4992 C C   . ARG B 109 ? 0.3583 0.3902 0.3268 -0.1082 0.0019  -0.0155 109 ARG B C   
4993 O O   . ARG B 109 ? 0.3941 0.4523 0.3587 -0.1281 -0.0056 -0.0200 109 ARG B O   
4994 C CB  . ARG B 109 ? 0.3933 0.3601 0.3327 -0.1230 0.0182  -0.0430 109 ARG B CB  
4995 C CG  . ARG B 109 ? 0.5912 0.5211 0.5229 -0.1449 0.0342  -0.0504 109 ARG B CG  
4996 C CD  . ARG B 109 ? 0.7567 0.6602 0.6635 -0.1711 0.0424  -0.0728 109 ARG B CD  
4997 N NE  . ARG B 109 ? 0.8355 0.7002 0.7328 -0.1551 0.0554  -0.0804 109 ARG B NE  
4998 C CZ  . ARG B 109 ? 0.8557 0.7216 0.7364 -0.1605 0.0532  -0.0939 109 ARG B CZ  
4999 N NH1 . ARG B 109 ? 0.8330 0.7378 0.7035 -0.1810 0.0373  -0.1001 109 ARG B NH1 
5000 N NH2 . ARG B 109 ? 0.8697 0.7021 0.7447 -0.1445 0.0674  -0.0993 109 ARG B NH2 
5001 N N   . PHE B 110 ? 0.2600 0.3036 0.2418 -0.0924 0.0019  -0.0013 110 PHE B N   
5002 C CA  . PHE B 110 ? 0.3015 0.3822 0.2956 -0.0979 -0.0030 0.0098  110 PHE B CA  
5003 C C   . PHE B 110 ? 0.2931 0.3552 0.2921 -0.1048 0.0085  0.0163  110 PHE B C   
5004 O O   . PHE B 110 ? 0.3362 0.3729 0.3352 -0.0880 0.0165  0.0224  110 PHE B O   
5005 C CB  . PHE B 110 ? 0.3267 0.4354 0.3292 -0.0733 -0.0093 0.0211  110 PHE B CB  
5006 C CG  . PHE B 110 ? 0.2740 0.3990 0.2720 -0.0651 -0.0177 0.0184  110 PHE B CG  
5007 C CD1 . PHE B 110 ? 0.2498 0.4156 0.2538 -0.0705 -0.0253 0.0246  110 PHE B CD1 
5008 C CD2 . PHE B 110 ? 0.3277 0.4305 0.3168 -0.0512 -0.0171 0.0122  110 PHE B CD2 
5009 C CE1 . PHE B 110 ? 0.2475 0.4265 0.2468 -0.0598 -0.0308 0.0262  110 PHE B CE1 
5010 C CE2 . PHE B 110 ? 0.3676 0.4807 0.3513 -0.0441 -0.0222 0.0111  110 PHE B CE2 
5011 C CZ  . PHE B 110 ? 0.3260 0.4744 0.3139 -0.0471 -0.0285 0.0189  110 PHE B CZ  
5012 N N   . GLU B 111 ? 0.2885 0.3665 0.2918 -0.1302 0.0096  0.0166  111 GLU B N   
5013 C CA  . GLU B 111 ? 0.4000 0.4592 0.4076 -0.1394 0.0226  0.0242  111 GLU B CA  
5014 C C   . GLU B 111 ? 0.3580 0.4303 0.3761 -0.1131 0.0236  0.0422  111 GLU B C   
5015 O O   . GLU B 111 ? 0.3072 0.3504 0.3240 -0.1058 0.0357  0.0509  111 GLU B O   
5016 C CB  . GLU B 111 ? 0.3829 0.4708 0.3963 -0.1733 0.0214  0.0225  111 GLU B CB  
5017 C CG  . GLU B 111 ? 0.6084 0.6744 0.6254 -0.1878 0.0371  0.0301  111 GLU B CG  
5018 C CD  . GLU B 111 ? 0.8286 0.8219 0.8296 -0.1898 0.0566  0.0235  111 GLU B CD  
5019 O OE1 . GLU B 111 ? 0.9110 0.8784 0.9149 -0.1740 0.0693  0.0384  111 GLU B OE1 
5020 O OE2 . GLU B 111 ? 0.9074 0.8699 0.8920 -0.2055 0.0605  0.0048  111 GLU B OE2 
5021 N N   . ARG B 112 ? 0.2868 0.4016 0.3132 -0.0978 0.0128  0.0486  112 ARG B N   
5022 C CA  . ARG B 112 ? 0.3028 0.4306 0.3346 -0.0761 0.0153  0.0629  112 ARG B CA  
5023 C C   . ARG B 112 ? 0.2807 0.3792 0.3027 -0.0546 0.0184  0.0635  112 ARG B C   
5024 O O   . ARG B 112 ? 0.2972 0.3931 0.3189 -0.0434 0.0246  0.0756  112 ARG B O   
5025 C CB  . ARG B 112 ? 0.2692 0.4414 0.3088 -0.0636 0.0071  0.0675  112 ARG B CB  
5026 C CG  . ARG B 112 ? 0.2418 0.4267 0.2824 -0.0423 0.0118  0.0788  112 ARG B CG  
5027 C CD  . ARG B 112 ? 0.2657 0.4560 0.3132 -0.0503 0.0213  0.0915  112 ARG B CD  
5028 N NE  . ARG B 112 ? 0.2466 0.4624 0.2959 -0.0328 0.0257  0.1020  112 ARG B NE  
5029 C CZ  . ARG B 112 ? 0.3082 0.5284 0.3585 -0.0321 0.0351  0.1146  112 ARG B CZ  
5030 N NH1 . ARG B 112 ? 0.4030 0.6011 0.4540 -0.0472 0.0418  0.1201  112 ARG B NH1 
5031 N NH2 . ARG B 112 ? 0.3383 0.5817 0.3869 -0.0159 0.0402  0.1220  112 ARG B NH2 
5032 N N   . ILE B 113 ? 0.2568 0.3380 0.2708 -0.0495 0.0141  0.0521  113 ILE B N   
5033 C CA  . ILE B 113 ? 0.2348 0.2975 0.2427 -0.0310 0.0161  0.0535  113 ILE B CA  
5034 C C   . ILE B 113 ? 0.3360 0.3670 0.3434 -0.0314 0.0291  0.0619  113 ILE B C   
5035 O O   . ILE B 113 ? 0.3368 0.3675 0.3437 -0.0145 0.0325  0.0742  113 ILE B O   
5036 C CB  . ILE B 113 ? 0.2639 0.3179 0.2655 -0.0277 0.0102  0.0399  113 ILE B CB  
5037 C CG1 . ILE B 113 ? 0.2587 0.3393 0.2591 -0.0211 0.0009  0.0363  113 ILE B CG1 
5038 C CG2 . ILE B 113 ? 0.3177 0.3559 0.3166 -0.0123 0.0136  0.0421  113 ILE B CG2 
5039 C CD1 . ILE B 113 ? 0.3527 0.4248 0.3461 -0.0179 -0.0037 0.0247  113 ILE B CD1 
5040 N N   . ARG B 114 ? 0.2898 0.2937 0.2959 -0.0510 0.0378  0.0561  114 ARG B N   
5041 C CA  . ARG B 114 ? 0.3584 0.3227 0.3626 -0.0511 0.0553  0.0651  114 ARG B CA  
5042 C C   . ARG B 114 ? 0.3926 0.3675 0.4020 -0.0480 0.0613  0.0844  114 ARG B C   
5043 O O   . ARG B 114 ? 0.4068 0.3641 0.4156 -0.0323 0.0722  0.1010  114 ARG B O   
5044 C CB  . ARG B 114 ? 0.4564 0.3843 0.4534 -0.0784 0.0663  0.0511  114 ARG B CB  
5045 C CG  . ARG B 114 ? 0.6073 0.5261 0.5954 -0.0845 0.0613  0.0309  114 ARG B CG  
5046 C CD  . ARG B 114 ? 0.7588 0.6321 0.7334 -0.1116 0.0769  0.0156  114 ARG B CD  
5047 N NE  . ARG B 114 ? 0.8181 0.7160 0.7896 -0.1451 0.0683  0.0030  114 ARG B NE  
5048 C CZ  . ARG B 114 ? 0.8554 0.7732 0.8191 -0.1584 0.0563  -0.0131 114 ARG B CZ  
5049 N NH1 . ARG B 114 ? 0.8218 0.7321 0.7793 -0.1417 0.0529  -0.0200 114 ARG B NH1 
5050 N NH2 . ARG B 114 ? 0.8585 0.8084 0.8210 -0.1887 0.0476  -0.0208 114 ARG B NH2 
5051 N N   . GLU B 115 ? 0.3632 0.3701 0.3786 -0.0617 0.0553  0.0847  115 GLU B N   
5052 C CA  . GLU B 115 ? 0.3685 0.3909 0.3888 -0.0588 0.0613  0.1030  115 GLU B CA  
5053 C C   . GLU B 115 ? 0.3298 0.3722 0.3468 -0.0306 0.0565  0.1153  115 GLU B C   
5054 O O   . GLU B 115 ? 0.4168 0.4516 0.4313 -0.0196 0.0659  0.1337  115 GLU B O   
5055 C CB  . GLU B 115 ? 0.3363 0.3992 0.3665 -0.0757 0.0550  0.1011  115 GLU B CB  
5056 C CG  . GLU B 115 ? 0.4109 0.4660 0.4443 -0.1093 0.0585  0.0902  115 GLU B CG  
5057 C CD  . GLU B 115 ? 0.4783 0.5871 0.5260 -0.1241 0.0512  0.0924  115 GLU B CD  
5058 O OE1 . GLU B 115 ? 0.3601 0.5051 0.4149 -0.1053 0.0470  0.1034  115 GLU B OE1 
5059 O OE2 . GLU B 115 ? 0.5443 0.6615 0.5958 -0.1550 0.0506  0.0833  115 GLU B OE2 
5060 N N   . LEU B 116 ? 0.2814 0.3496 0.2962 -0.0201 0.0427  0.1054  116 LEU B N   
5061 C CA  . LEU B 116 ? 0.3428 0.4336 0.3505 0.0004  0.0379  0.1126  116 LEU B CA  
5062 C C   . LEU B 116 ? 0.3519 0.4282 0.3548 0.0159  0.0410  0.1223  116 LEU B C   
5063 O O   . LEU B 116 ? 0.3588 0.4519 0.3558 0.0291  0.0422  0.1373  116 LEU B O   
5064 C CB  . LEU B 116 ? 0.2790 0.3903 0.2828 0.0049  0.0261  0.0972  116 LEU B CB  
5065 C CG  . LEU B 116 ? 0.3125 0.4471 0.3224 -0.0024 0.0241  0.0931  116 LEU B CG  
5066 C CD1 . LEU B 116 ? 0.3165 0.4593 0.3213 0.0044  0.0161  0.0794  116 LEU B CD1 
5067 C CD2 . LEU B 116 ? 0.3486 0.5060 0.3580 0.0024  0.0305  0.1061  116 LEU B CD2 
5068 N N   . MET B 117 ? 0.3232 0.3720 0.3284 0.0155  0.0432  0.1153  117 MET B N   
5069 C CA  . MET B 117 ? 0.3340 0.3758 0.3387 0.0338  0.0467  0.1265  117 MET B CA  
5070 C C   . MET B 117 ? 0.4580 0.4749 0.4648 0.0407  0.0640  0.1497  117 MET B C   
5071 O O   . MET B 117 ? 0.4806 0.5012 0.4887 0.0611  0.0680  0.1669  117 MET B O   
5072 C CB  . MET B 117 ? 0.3149 0.3370 0.3220 0.0332  0.0457  0.1116  117 MET B CB  
5073 C CG  . MET B 117 ? 0.3807 0.4259 0.3846 0.0295  0.0302  0.0921  117 MET B CG  
5074 S SD  . MET B 117 ? 0.4342 0.5245 0.4312 0.0427  0.0182  0.0963  117 MET B SD  
5075 C CE  . MET B 117 ? 0.4718 0.5672 0.4756 0.0596  0.0201  0.1071  117 MET B CE  
5076 N N   . ASN B 118 ? 0.5098 0.5038 0.5176 0.0242  0.0752  0.1521  118 ASN B N   
5077 C CA  . ASN B 118 ? 0.6143 0.5796 0.6220 0.0286  0.0948  0.1753  118 ASN B CA  
5078 C C   . ASN B 118 ? 0.5970 0.5931 0.6017 0.0331  0.0942  0.1943  118 ASN B C   
5079 O O   . ASN B 118 ? 0.6499 0.6243 0.6537 0.0352  0.1113  0.2159  118 ASN B O   
5080 C CB  . ASN B 118 ? 0.7307 0.6477 0.7386 0.0029  0.1107  0.1657  118 ASN B CB  
5081 C CG  . ASN B 118 ? 0.8553 0.7275 0.8611 0.0024  0.1206  0.1534  118 ASN B CG  
5082 O OD1 . ASN B 118 ? 0.9195 0.7894 0.9270 0.0271  0.1222  0.1616  118 ASN B OD1 
5083 N ND2 . ASN B 118 ? 0.9095 0.7493 0.9109 -0.0266 0.1279  0.1335  118 ASN B ND2 
5084 N N   . LYS B 119 ? 0.4931 0.5354 0.4943 0.0345  0.0778  0.1868  119 LYS B N   
5085 C CA  . LYS B 119 ? 0.5309 0.6047 0.5254 0.0399  0.0780  0.2027  119 LYS B CA  
5086 C C   . LYS B 119 ? 0.5486 0.6510 0.5337 0.0633  0.0721  0.2186  119 LYS B C   
5087 O O   . LYS B 119 ? 0.5555 0.6697 0.5401 0.0722  0.0613  0.2098  119 LYS B O   
5088 C CB  . LYS B 119 ? 0.4730 0.5789 0.4663 0.0292  0.0675  0.1858  119 LYS B CB  
5089 C CG  . LYS B 119 ? 0.5346 0.6309 0.5392 0.0062  0.0734  0.1783  119 LYS B CG  
5090 C CD  . LYS B 119 ? 0.5694 0.7028 0.5756 0.0022  0.0648  0.1663  119 LYS B CD  
5091 C CE  . LYS B 119 ? 0.6231 0.7582 0.6446 -0.0206 0.0666  0.1579  119 LYS B CE  
5092 N NZ  . LYS B 119 ? 0.6047 0.7478 0.6333 -0.0328 0.0796  0.1738  119 LYS B NZ  
5093 N N   . GLU B 120 ? 0.5960 0.7138 0.5736 0.0717  0.0790  0.2422  120 GLU B N   
5094 C CA  . GLU B 120 ? 0.6035 0.7558 0.5758 0.0894  0.0700  0.2489  120 GLU B CA  
5095 C C   . GLU B 120 ? 0.6018 0.7980 0.5602 0.0859  0.0541  0.2312  120 GLU B C   
5096 O O   . GLU B 120 ? 0.6224 0.8473 0.5767 0.0928  0.0426  0.2253  120 GLU B O   
5097 C CB  . GLU B 120 ? 0.6216 0.7723 0.5946 0.0974  0.0813  0.2709  120 GLU B CB  
5098 N N   . LYS B 121 ? 0.4740 0.6754 0.4259 0.0740  0.0554  0.2213  121 LYS B N   
5099 C CA  . LYS B 121 ? 0.5113 0.7431 0.4477 0.0705  0.0457  0.2020  121 LYS B CA  
5100 C C   . LYS B 121 ? 0.4892 0.7127 0.4270 0.0593  0.0479  0.1871  121 LYS B C   
5101 O O   . LYS B 121 ? 0.5076 0.7139 0.4597 0.0507  0.0571  0.1922  121 LYS B O   
5102 C CB  . LYS B 121 ? 0.4765 0.7319 0.4013 0.0728  0.0486  0.2083  121 LYS B CB  
5103 N N   . LEU B 122 ? 0.4304 0.6653 0.3570 0.0575  0.0396  0.1650  122 LEU B N   
5104 C CA  . LEU B 122 ? 0.3401 0.5658 0.2741 0.0499  0.0406  0.1456  122 LEU B CA  
5105 C C   . LEU B 122 ? 0.3980 0.6434 0.3138 0.0519  0.0467  0.1387  122 LEU B C   
5106 O O   . LEU B 122 ? 0.4287 0.6854 0.3230 0.0541  0.0430  0.1286  122 LEU B O   
5107 C CB  . LEU B 122 ? 0.3416 0.5547 0.2778 0.0477  0.0306  0.1247  122 LEU B CB  
5108 C CG  . LEU B 122 ? 0.4764 0.6672 0.4290 0.0455  0.0257  0.1245  122 LEU B CG  
5109 C CD1 . LEU B 122 ? 0.4537 0.6247 0.4241 0.0393  0.0339  0.1372  122 LEU B CD1 
5110 C CD2 . LEU B 122 ? 0.5558 0.7570 0.5019 0.0538  0.0198  0.1324  122 LEU B CD2 
5111 N N   . ASN B 123 ? 0.3184 0.5662 0.2460 0.0495  0.0562  0.1409  123 ASN B N   
5112 C CA  . ASN B 123 ? 0.3019 0.5637 0.2164 0.0542  0.0656  0.1331  123 ASN B CA  
5113 C C   . ASN B 123 ? 0.3181 0.5692 0.2305 0.0566  0.0650  0.1121  123 ASN B C   
5114 O O   . ASN B 123 ? 0.3115 0.5462 0.2325 0.0532  0.0549  0.1028  123 ASN B O   
5115 C CB  . ASN B 123 ? 0.3299 0.6037 0.2624 0.0524  0.0767  0.1468  123 ASN B CB  
5116 C CG  . ASN B 123 ? 0.4121 0.6858 0.3745 0.0443  0.0767  0.1506  123 ASN B CG  
5117 O OD1 . ASN B 123 ? 0.3571 0.6201 0.3270 0.0436  0.0692  0.1367  123 ASN B OD1 
5118 N ND2 . ASN B 123 ? 0.4610 0.7454 0.4412 0.0354  0.0840  0.1674  123 ASN B ND2 
5119 N N   . ARG B 124 ? 0.2963 0.5888 0.2523 -0.0153 0.0234  0.0535  124 ARG B N   
5120 C CA  . ARG B 124 ? 0.2442 0.5292 0.1950 -0.0069 0.0202  0.0382  124 ARG B CA  
5121 C C   . ARG B 124 ? 0.2810 0.5599 0.2474 -0.0044 0.0210  0.0321  124 ARG B C   
5122 O O   . ARG B 124 ? 0.2482 0.5112 0.2164 0.0004  0.0164  0.0259  124 ARG B O   
5123 C CB  . ARG B 124 ? 0.2989 0.5975 0.2339 -0.0015 0.0249  0.0284  124 ARG B CB  
5124 C CG  . ARG B 124 ? 0.2434 0.5316 0.1744 0.0094  0.0250  0.0138  124 ARG B CG  
5125 C CD  . ARG B 124 ? 0.2827 0.5788 0.1959 0.0172  0.0326  0.0042  124 ARG B CD  
5126 N NE  . ARG B 124 ? 0.2945 0.5753 0.2026 0.0292  0.0342  -0.0079 124 ARG B NE  
5127 C CZ  . ARG B 124 ? 0.3715 0.6601 0.2937 0.0389  0.0377  -0.0105 124 ARG B CZ  
5128 N NH1 . ARG B 124 ? 0.3931 0.7061 0.3345 0.0354  0.0395  -0.0034 124 ARG B NH1 
5129 N NH2 . ARG B 124 ? 0.3763 0.6492 0.2925 0.0511  0.0398  -0.0195 124 ARG B NH2 
5130 N N   . GLU B 125 ? 0.3010 0.5944 0.2777 -0.0090 0.0269  0.0338  125 GLU B N   
5131 C CA  . GLU B 125 ? 0.2621 0.5553 0.2519 -0.0093 0.0272  0.0281  125 GLU B CA  
5132 C C   . GLU B 125 ? 0.2482 0.5173 0.2464 -0.0150 0.0247  0.0321  125 GLU B C   
5133 O O   . GLU B 125 ? 0.2307 0.4905 0.2345 -0.0125 0.0218  0.0254  125 GLU B O   
5134 C CB  . GLU B 125 ? 0.3328 0.6516 0.3310 -0.0168 0.0339  0.0299  125 GLU B CB  
5135 C CG  . GLU B 125 ? 0.4599 0.8064 0.4527 -0.0087 0.0383  0.0256  125 GLU B CG  
5136 C CD  . GLU B 125 ? 0.5666 0.9134 0.5429 -0.0056 0.0401  0.0284  125 GLU B CD  
5137 O OE1 . GLU B 125 ? 0.5832 0.9297 0.5468 0.0060  0.0409  0.0204  125 GLU B OE1 
5138 O OE2 . GLU B 125 ? 0.5297 0.8753 0.5039 -0.0152 0.0414  0.0387  125 GLU B OE2 
5139 N N   . GLU B 126 ? 0.2498 0.5081 0.2485 -0.0215 0.0266  0.0441  126 GLU B N   
5140 C CA  . GLU B 126 ? 0.2481 0.4810 0.2539 -0.0243 0.0267  0.0492  126 GLU B CA  
5141 C C   . GLU B 126 ? 0.2305 0.4500 0.2338 -0.0152 0.0191  0.0463  126 GLU B C   
5142 O O   . GLU B 126 ? 0.1962 0.3988 0.2057 -0.0143 0.0181  0.0428  126 GLU B O   
5143 C CB  . GLU B 126 ? 0.2913 0.5158 0.2982 -0.0304 0.0328  0.0654  126 GLU B CB  
5144 C CG  . GLU B 126 ? 0.2959 0.5211 0.3069 -0.0433 0.0424  0.0678  126 GLU B CG  
5145 C CD  . GLU B 126 ? 0.3451 0.5712 0.3532 -0.0485 0.0494  0.0837  126 GLU B CD  
5146 O OE1 . GLU B 126 ? 0.3621 0.5915 0.3652 -0.0415 0.0461  0.0942  126 GLU B OE1 
5147 O OE2 . GLU B 126 ? 0.3884 0.6133 0.3982 -0.0609 0.0583  0.0860  126 GLU B OE2 
5148 N N   . LEU B 127 ? 0.2256 0.4525 0.2183 -0.0100 0.0141  0.0469  127 LEU B N   
5149 C CA  . LEU B 127 ? 0.1996 0.4153 0.1886 -0.0043 0.0068  0.0435  127 LEU B CA  
5150 C C   . LEU B 127 ? 0.2176 0.4285 0.2054 0.0016  0.0047  0.0284  127 LEU B C   
5151 O O   . LEU B 127 ? 0.2144 0.4104 0.2048 0.0046  0.0007  0.0254  127 LEU B O   
5152 C CB  . LEU B 127 ? 0.2342 0.4600 0.2086 -0.0041 0.0022  0.0465  127 LEU B CB  
5153 C CG  . LEU B 127 ? 0.2523 0.4837 0.2291 -0.0081 0.0020  0.0650  127 LEU B CG  
5154 C CD1 . LEU B 127 ? 0.2859 0.5348 0.2453 -0.0109 -0.0020 0.0670  127 LEU B CD1 
5155 C CD2 . LEU B 127 ? 0.2301 0.4486 0.2177 -0.0058 -0.0011 0.0739  127 LEU B CD2 
5156 N N   . LEU B 128 ? 0.1937 0.4187 0.1782 0.0042  0.0079  0.0203  128 LEU B N   
5157 C CA  . LEU B 128 ? 0.1865 0.4097 0.1714 0.0119  0.0071  0.0089  128 LEU B CA  
5158 C C   . LEU B 128 ? 0.1767 0.3913 0.1748 0.0087  0.0067  0.0085  128 LEU B C   
5159 O O   . LEU B 128 ? 0.1893 0.3925 0.1877 0.0142  0.0034  0.0025  128 LEU B O   
5160 C CB  . LEU B 128 ? 0.2395 0.4850 0.2221 0.0165  0.0124  0.0042  128 LEU B CB  
5161 C CG  . LEU B 128 ? 0.3134 0.5588 0.2794 0.0268  0.0142  -0.0035 128 LEU B CG  
5162 C CD1 . LEU B 128 ? 0.2322 0.5031 0.1987 0.0325  0.0218  -0.0051 128 LEU B CD1 
5163 C CD2 . LEU B 128 ? 0.3428 0.5693 0.3043 0.0360  0.0116  -0.0116 128 LEU B CD2 
5164 N N   . ASP B 129 ? 0.2179 0.4362 0.2248 -0.0012 0.0110  0.0142  129 ASP B N   
5165 C CA  . ASP B 129 ? 0.1758 0.3821 0.1914 -0.0072 0.0122  0.0129  129 ASP B CA  
5166 C C   . ASP B 129 ? 0.2486 0.4291 0.2653 -0.0052 0.0099  0.0165  129 ASP B C   
5167 O O   . ASP B 129 ? 0.1709 0.3396 0.1902 -0.0036 0.0082  0.0112  129 ASP B O   
5168 C CB  . ASP B 129 ? 0.2305 0.4411 0.2514 -0.0208 0.0193  0.0178  129 ASP B CB  
5169 C CG  . ASP B 129 ? 0.2612 0.5015 0.2846 -0.0252 0.0212  0.0132  129 ASP B CG  
5170 O OD1 . ASP B 129 ? 0.2626 0.5206 0.2840 -0.0144 0.0179  0.0081  129 ASP B OD1 
5171 O OD2 . ASP B 129 ? 0.2693 0.5155 0.2963 -0.0394 0.0268  0.0153  129 ASP B OD2 
5172 N N   . LEU B 130 ? 0.2171 0.3918 0.2320 -0.0049 0.0100  0.0266  130 LEU B N   
5173 C CA  . LEU B 130 ? 0.2115 0.3678 0.2297 -0.0018 0.0081  0.0326  130 LEU B CA  
5174 C C   . LEU B 130 ? 0.1949 0.3478 0.2085 0.0054  0.0008  0.0243  130 LEU B C   
5175 O O   . LEU B 130 ? 0.2163 0.3544 0.2344 0.0072  0.0000  0.0226  130 LEU B O   
5176 C CB  . LEU B 130 ? 0.1980 0.3575 0.2158 -0.0017 0.0085  0.0474  130 LEU B CB  
5177 C CG  . LEU B 130 ? 0.2301 0.3758 0.2552 0.0020  0.0086  0.0582  130 LEU B CG  
5178 C CD1 . LEU B 130 ? 0.3127 0.4361 0.3463 -0.0002 0.0184  0.0610  130 LEU B CD1 
5179 C CD2 . LEU B 130 ? 0.2404 0.3979 0.2652 0.0032  0.0073  0.0750  130 LEU B CD2 
5180 N N   . GLN B 131 ? 0.2119 0.3760 0.2149 0.0091  -0.0032 0.0185  131 GLN B N   
5181 C CA  . GLN B 131 ? 0.1798 0.3363 0.1753 0.0150  -0.0083 0.0099  131 GLN B CA  
5182 C C   . GLN B 131 ? 0.2328 0.3834 0.2324 0.0188  -0.0075 0.0014  131 GLN B C   
5183 O O   . GLN B 131 ? 0.1745 0.3111 0.1750 0.0213  -0.0102 -0.0011 131 GLN B O   
5184 C CB  . GLN B 131 ? 0.1789 0.3437 0.1589 0.0179  -0.0092 0.0039  131 GLN B CB  
5185 C CG  . GLN B 131 ? 0.1884 0.3602 0.1594 0.0128  -0.0116 0.0107  131 GLN B CG  
5186 C CD  . GLN B 131 ? 0.2391 0.4182 0.1923 0.0146  -0.0094 0.0029  131 GLN B CD  
5187 O OE1 . GLN B 131 ? 0.2247 0.4125 0.1782 0.0193  -0.0040 -0.0018 131 GLN B OE1 
5188 N NE2 . GLN B 131 ? 0.2293 0.4058 0.1660 0.0104  -0.0129 0.0010  131 GLN B NE2 
5189 N N   . THR B 132 ? 0.1899 0.3545 0.1921 0.0188  -0.0041 -0.0022 132 THR B N   
5190 C CA  . THR B 132 ? 0.1570 0.3233 0.1621 0.0228  -0.0043 -0.0091 132 THR B CA  
5191 C C   . THR B 132 ? 0.1796 0.3345 0.1931 0.0161  -0.0035 -0.0080 132 THR B C   
5192 O O   . THR B 132 ? 0.1654 0.3124 0.1790 0.0195  -0.0056 -0.0124 132 THR B O   
5193 C CB  . THR B 132 ? 0.1576 0.3496 0.1647 0.0240  -0.0010 -0.0112 132 THR B CB  
5194 O OG1 . THR B 132 ? 0.1857 0.3856 0.1834 0.0307  0.0006  -0.0120 132 THR B OG1 
5195 C CG2 . THR B 132 ? 0.1542 0.3546 0.1639 0.0304  -0.0020 -0.0160 132 THR B CG2 
5196 N N   . LEU B 133 ? 0.2146 0.3660 0.2335 0.0065  0.0009  -0.0021 133 LEU B N   
5197 C CA  . LEU B 133 ? 0.1919 0.3271 0.2155 -0.0005 0.0045  -0.0022 133 LEU B CA  
5198 C C   . LEU B 133 ? 0.2152 0.3294 0.2398 0.0046  0.0029  0.0007  133 LEU B C   
5199 O O   . LEU B 133 ? 0.2355 0.3363 0.2616 0.0029  0.0046  -0.0025 133 LEU B O   
5200 C CB  . LEU B 133 ? 0.1690 0.2999 0.1956 -0.0117 0.0124  0.0036  133 LEU B CB  
5201 C CG  . LEU B 133 ? 0.2380 0.3902 0.2647 -0.0211 0.0146  -0.0009 133 LEU B CG  
5202 C CD1 . LEU B 133 ? 0.3008 0.4502 0.3281 -0.0322 0.0226  0.0058  133 LEU B CD1 
5203 C CD2 . LEU B 133 ? 0.2026 0.3555 0.2289 -0.0284 0.0147  -0.0093 133 LEU B CD2 
5204 N N   . ASN B 134 ? 0.1601 0.2735 0.1834 0.0096  -0.0003 0.0069  134 ASN B N   
5205 C CA  . ASN B 134 ? 0.1750 0.2750 0.2000 0.0139  -0.0029 0.0099  134 ASN B CA  
5206 C C   . ASN B 134 ? 0.2212 0.3177 0.2412 0.0187  -0.0076 0.0003  134 ASN B C   
5207 O O   . ASN B 134 ? 0.1973 0.2807 0.2201 0.0195  -0.0070 -0.0005 134 ASN B O   
5208 C CB  . ASN B 134 ? 0.1918 0.2984 0.2149 0.0157  -0.0069 0.0183  134 ASN B CB  
5209 C CG  . ASN B 134 ? 0.2134 0.3166 0.2456 0.0145  -0.0020 0.0329  134 ASN B CG  
5210 O OD1 . ASN B 134 ? 0.2041 0.2978 0.2434 0.0172  -0.0004 0.0392  134 ASN B OD1 
5211 N ND2 . ASN B 134 ? 0.2288 0.3401 0.2611 0.0114  0.0017  0.0396  134 ASN B ND2 
5212 N N   . LEU B 135 ? 0.2069 0.3141 0.2191 0.0227  -0.0106 -0.0063 135 LEU B N   
5213 C CA  . LEU B 135 ? 0.2353 0.3381 0.2422 0.0291  -0.0133 -0.0137 135 LEU B CA  
5214 C C   . LEU B 135 ? 0.2310 0.3341 0.2427 0.0271  -0.0113 -0.0170 135 LEU B C   
5215 O O   . LEU B 135 ? 0.2196 0.3114 0.2304 0.0293  -0.0126 -0.0193 135 LEU B O   
5216 C CB  . LEU B 135 ? 0.2589 0.3723 0.2566 0.0361  -0.0137 -0.0186 135 LEU B CB  
5217 C CG  . LEU B 135 ? 0.2663 0.3736 0.2520 0.0383  -0.0153 -0.0197 135 LEU B CG  
5218 C CD1 . LEU B 135 ? 0.2616 0.3764 0.2372 0.0469  -0.0121 -0.0252 135 LEU B CD1 
5219 C CD2 . LEU B 135 ? 0.2282 0.3162 0.2083 0.0384  -0.0186 -0.0211 135 LEU B CD2 
5220 N N   . LEU B 136 ? 0.1972 0.3144 0.2126 0.0210  -0.0082 -0.0175 136 LEU B N   
5221 C CA  . LEU B 136 ? 0.1732 0.2964 0.1903 0.0162  -0.0071 -0.0217 136 LEU B CA  
5222 C C   . LEU B 136 ? 0.2175 0.3201 0.2364 0.0086  -0.0032 -0.0215 136 LEU B C   
5223 O O   . LEU B 136 ? 0.1770 0.2782 0.1938 0.0056  -0.0031 -0.0261 136 LEU B O   
5224 C CB  . LEU B 136 ? 0.1608 0.3075 0.1805 0.0084  -0.0048 -0.0222 136 LEU B CB  
5225 C CG  . LEU B 136 ? 0.1568 0.3294 0.1758 0.0174  -0.0071 -0.0225 136 LEU B CG  
5226 C CD1 . LEU B 136 ? 0.1831 0.3819 0.2066 0.0080  -0.0042 -0.0213 136 LEU B CD1 
5227 C CD2 . LEU B 136 ? 0.1520 0.3341 0.1692 0.0272  -0.0104 -0.0250 136 LEU B CD2 
5228 N N   . ALA B 137 ? 0.1528 0.2403 0.1751 0.0060  0.0011  -0.0155 137 ALA B N   
5229 C CA  . ALA B 137 ? 0.2003 0.2653 0.2243 0.0022  0.0073  -0.0140 137 ALA B CA  
5230 C C   . ALA B 137 ? 0.2066 0.2623 0.2293 0.0088  0.0039  -0.0162 137 ALA B C   
5231 O O   . ALA B 137 ? 0.2123 0.2536 0.2337 0.0052  0.0089  -0.0187 137 ALA B O   
5232 C CB  . ALA B 137 ? 0.2257 0.2794 0.2555 0.0034  0.0125  -0.0034 137 ALA B CB  
5233 N N   . TRP B 138 ? 0.2001 0.2616 0.2210 0.0175  -0.0033 -0.0159 138 TRP B N   
5234 C CA  . TRP B 138 ? 0.1833 0.2348 0.2020 0.0228  -0.0062 -0.0172 138 TRP B CA  
5235 C C   . TRP B 138 ? 0.1805 0.2394 0.1925 0.0265  -0.0100 -0.0237 138 TRP B C   
5236 O O   . TRP B 138 ? 0.2097 0.2604 0.2179 0.0319  -0.0126 -0.0245 138 TRP B O   
5237 C CB  . TRP B 138 ? 0.2231 0.2725 0.2418 0.0277  -0.0105 -0.0123 138 TRP B CB  
5238 C CG  . TRP B 138 ? 0.1726 0.2190 0.1999 0.0255  -0.0072 -0.0026 138 TRP B CG  
5239 C CD1 . TRP B 138 ? 0.2453 0.3003 0.2756 0.0236  -0.0061 0.0036  138 TRP B CD1 
5240 C CD2 . TRP B 138 ? 0.1859 0.2222 0.2207 0.0264  -0.0035 0.0041  138 TRP B CD2 
5241 N NE1 . TRP B 138 ? 0.2280 0.2791 0.2675 0.0242  -0.0021 0.0149  138 TRP B NE1 
5242 C CE2 . TRP B 138 ? 0.1714 0.2117 0.2144 0.0264  -0.0002 0.0155  138 TRP B CE2 
5243 C CE3 . TRP B 138 ? 0.2027 0.2283 0.2383 0.0281  -0.0021 0.0028  138 TRP B CE3 
5244 C CZ2 . TRP B 138 ? 0.2187 0.2545 0.2723 0.0296  0.0050  0.0265  138 TRP B CZ2 
5245 C CZ3 . TRP B 138 ? 0.1909 0.2113 0.2364 0.0301  0.0032  0.0123  138 TRP B CZ3 
5246 C CH2 . TRP B 138 ? 0.1868 0.2129 0.2419 0.0316  0.0069  0.0245  138 TRP B CH2 
5247 N N   . CYS B 139 ? 0.1893 0.2653 0.2001 0.0234  -0.0100 -0.0271 139 CYS B N   
5248 C CA  . CYS B 139 ? 0.1581 0.2470 0.1643 0.0284  -0.0133 -0.0303 139 CYS B CA  
5249 C C   . CYS B 139 ? 0.1747 0.2530 0.1778 0.0260  -0.0126 -0.0324 139 CYS B C   
5250 O O   . CYS B 139 ? 0.2422 0.3128 0.2455 0.0156  -0.0079 -0.0346 139 CYS B O   
5251 C CB  . CYS B 139 ? 0.1630 0.2785 0.1709 0.0228  -0.0133 -0.0318 139 CYS B CB  
5252 S SG  . CYS B 139 ? 0.2296 0.3719 0.2349 0.0319  -0.0177 -0.0314 139 CYS B SG  
5253 N N   . GLY B 140 ? 0.1708 0.2468 0.1692 0.0355  -0.0159 -0.0319 140 GLY B N   
5254 C CA  . GLY B 140 ? 0.1892 0.2579 0.1832 0.0341  -0.0155 -0.0332 140 GLY B CA  
5255 C C   . GLY B 140 ? 0.1802 0.2718 0.1709 0.0295  -0.0170 -0.0352 140 GLY B C   
5256 O O   . GLY B 140 ? 0.1883 0.3051 0.1812 0.0291  -0.0190 -0.0346 140 GLY B O   
5257 N N   . ARG B 141 ? 0.1978 0.2833 0.1827 0.0254  -0.0161 -0.0370 141 ARG B N   
5258 C CA  . ARG B 141 ? 0.1922 0.3014 0.1718 0.0176  -0.0180 -0.0390 141 ARG B CA  
5259 C C   . ARG B 141 ? 0.1882 0.3277 0.1691 0.0293  -0.0239 -0.0329 141 ARG B C   
5260 O O   . ARG B 141 ? 0.1796 0.3514 0.1620 0.0230  -0.0264 -0.0325 141 ARG B O   
5261 C CB  . ARG B 141 ? 0.1784 0.2742 0.1493 0.0133  -0.0160 -0.0412 141 ARG B CB  
5262 C CG  . ARG B 141 ? 0.1874 0.3094 0.1499 0.0049  -0.0191 -0.0426 141 ARG B CG  
5263 C CD  . ARG B 141 ? 0.2357 0.3391 0.1878 -0.0012 -0.0152 -0.0462 141 ARG B CD  
5264 N NE  . ARG B 141 ? 0.2414 0.3713 0.1830 -0.0089 -0.0191 -0.0465 141 ARG B NE  
5265 C CZ  . ARG B 141 ? 0.2090 0.3543 0.1479 0.0028  -0.0246 -0.0385 141 ARG B CZ  
5266 N NH1 . ARG B 141 ? 0.2254 0.3570 0.1695 0.0221  -0.0256 -0.0308 141 ARG B NH1 
5267 N NH2 . ARG B 141 ? 0.2647 0.4388 0.1938 -0.0061 -0.0285 -0.0378 141 ARG B NH2 
5268 N N   . THR B 142 ? 0.1679 0.2978 0.1480 0.0465  -0.0251 -0.0274 142 THR B N   
5269 C CA  . THR B 142 ? 0.2363 0.3910 0.2166 0.0614  -0.0279 -0.0197 142 THR B CA  
5270 C C   . THR B 142 ? 0.2362 0.4148 0.2242 0.0647  -0.0281 -0.0180 142 THR B C   
5271 O O   . THR B 142 ? 0.2767 0.4926 0.2684 0.0686  -0.0305 -0.0123 142 THR B O   
5272 C CB  . THR B 142 ? 0.2876 0.4172 0.2625 0.0786  -0.0260 -0.0151 142 THR B CB  
5273 O OG1 . THR B 142 ? 0.2848 0.3983 0.2529 0.0760  -0.0260 -0.0150 142 THR B OG1 
5274 C CG2 . THR B 142 ? 0.3031 0.4534 0.2779 0.0977  -0.0258 -0.0057 142 THR B CG2 
5275 N N   . LEU B 143 ? 0.1620 0.3231 0.1529 0.0632  -0.0254 -0.0217 143 LEU B N   
5276 C CA  . LEU B 143 ? 0.2273 0.4078 0.2240 0.0681  -0.0245 -0.0198 143 LEU B CA  
5277 C C   . LEU B 143 ? 0.2395 0.4471 0.2426 0.0514  -0.0254 -0.0224 143 LEU B C   
5278 O O   . LEU B 143 ? 0.2407 0.4706 0.2497 0.0540  -0.0246 -0.0202 143 LEU B O   
5279 C CB  . LEU B 143 ? 0.2328 0.3851 0.2276 0.0724  -0.0214 -0.0224 143 LEU B CB  
5280 C CG  . LEU B 143 ? 0.2230 0.3558 0.2096 0.0902  -0.0187 -0.0197 143 LEU B CG  
5281 C CD1 . LEU B 143 ? 0.1797 0.2903 0.1621 0.0901  -0.0161 -0.0234 143 LEU B CD1 
5282 C CD2 . LEU B 143 ? 0.2873 0.4456 0.2747 0.1072  -0.0167 -0.0126 143 LEU B CD2 
5283 N N   . ARG B 144 ? 0.2291 0.4341 0.2297 0.0336  -0.0259 -0.0274 144 ARG B N   
5284 C CA  . ARG B 144 ? 0.2605 0.4882 0.2639 0.0147  -0.0255 -0.0308 144 ARG B CA  
5285 C C   . ARG B 144 ? 0.3057 0.5836 0.3142 0.0161  -0.0297 -0.0250 144 ARG B C   
5286 O O   . ARG B 144 ? 0.3464 0.6485 0.3594 0.0031  -0.0293 -0.0262 144 ARG B O   
5287 C CB  . ARG B 144 ? 0.3579 0.5704 0.3533 -0.0048 -0.0233 -0.0382 144 ARG B CB  
5288 C CG  . ARG B 144 ? 0.4169 0.5854 0.4101 -0.0077 -0.0172 -0.0424 144 ARG B CG  
5289 C CD  . ARG B 144 ? 0.4952 0.6465 0.4787 -0.0237 -0.0126 -0.0493 144 ARG B CD  
5290 N NE  . ARG B 144 ? 0.5620 0.7294 0.5387 -0.0230 -0.0173 -0.0490 144 ARG B NE  
5291 C CZ  . ARG B 144 ? 0.6557 0.8367 0.6223 -0.0412 -0.0170 -0.0546 144 ARG B CZ  
5292 N NH1 . ARG B 144 ? 0.6772 0.8536 0.6385 -0.0625 -0.0111 -0.0622 144 ARG B NH1 
5293 N NH2 . ARG B 144 ? 0.6972 0.8956 0.6573 -0.0392 -0.0220 -0.0525 144 ARG B NH2 
5294 N N   . LYS B 145 ? 0.2581 0.5540 0.2665 0.0317  -0.0331 -0.0175 145 LYS B N   
5295 C CA  . LYS B 145 ? 0.2472 0.5973 0.2629 0.0352  -0.0369 -0.0088 145 LYS B CA  
5296 C C   . LYS B 145 ? 0.2553 0.6139 0.2789 0.0540  -0.0325 -0.0019 145 LYS B C   
5297 O O   . LYS B 145 ? 0.2106 0.5969 0.2400 0.0474  -0.0303 0.0007  145 LYS B O   
5298 C CB  . LYS B 145 ? 0.4106 0.7709 0.4217 0.0431  -0.0386 -0.0012 145 LYS B CB  
5299 C CG  . LYS B 145 ? 0.5307 0.8864 0.5429 0.0720  -0.0349 0.0102  145 LYS B CG  
5300 C CD  . LYS B 145 ? 0.6097 0.9705 0.6163 0.0783  -0.0362 0.0177  145 LYS B CD  
5301 C CE  . LYS B 145 ? 0.6687 1.0069 0.6719 0.1062  -0.0308 0.0266  145 LYS B CE  
5302 N NZ  . LYS B 145 ? 0.6745 0.9667 0.6721 0.1138  -0.0299 0.0193  145 LYS B NZ  
5303 N N   . ASP B 146 ? 0.2357 0.5667 0.2570 0.0758  -0.0296 0.0001  146 ASP B N   
5304 C CA  . ASP B 146 ? 0.2457 0.5779 0.2696 0.0928  -0.0232 0.0049  146 ASP B CA  
5305 C C   . ASP B 146 ? 0.2865 0.6213 0.3159 0.0820  -0.0222 -0.0012 146 ASP B C   
5306 O O   . ASP B 146 ? 0.2752 0.6284 0.3083 0.0874  -0.0177 0.0031  146 ASP B O   
5307 C CB  . ASP B 146 ? 0.3176 0.6114 0.3333 0.1143  -0.0188 0.0057  146 ASP B CB  
5308 C CG  . ASP B 146 ? 0.5809 0.8741 0.5904 0.1305  -0.0153 0.0158  146 ASP B CG  
5309 O OD1 . ASP B 146 ? 0.6484 0.9769 0.6620 0.1296  -0.0153 0.0243  146 ASP B OD1 
5310 O OD2 . ASP B 146 ? 0.6642 0.9215 0.6642 0.1434  -0.0120 0.0158  146 ASP B OD2 
5311 N N   . LEU B 147 ? 0.1938 0.4977 0.2186 0.0642  -0.0228 -0.0103 147 LEU B N   
5312 C CA  . LEU B 147 ? 0.1802 0.4753 0.2069 0.0537  -0.0200 -0.0148 147 LEU B CA  
5313 C C   . LEU B 147 ? 0.1502 0.4683 0.1815 0.0297  -0.0212 -0.0176 147 LEU B C   
5314 O O   . LEU B 147 ? 0.1932 0.5007 0.2252 0.0188  -0.0181 -0.0207 147 LEU B O   
5315 C CB  . LEU B 147 ? 0.1703 0.4169 0.1895 0.0515  -0.0184 -0.0205 147 LEU B CB  
5316 C CG  . LEU B 147 ? 0.2064 0.4265 0.2183 0.0703  -0.0162 -0.0197 147 LEU B CG  
5317 C CD1 . LEU B 147 ? 0.2016 0.3829 0.2079 0.0640  -0.0159 -0.0242 147 LEU B CD1 
5318 C CD2 . LEU B 147 ? 0.2521 0.4866 0.2646 0.0833  -0.0118 -0.0168 147 LEU B CD2 
5319 N N   . LYS B 148 ? 0.2006 0.5507 0.2337 0.0203  -0.0253 -0.0160 148 LYS B N   
5320 C CA  . LYS B 148 ? 0.2552 0.6221 0.2883 -0.0071 -0.0256 -0.0208 148 LYS B CA  
5321 C C   . LYS B 148 ? 0.2319 0.6239 0.2730 -0.0135 -0.0228 -0.0186 148 LYS B C   
5322 O O   . LYS B 148 ? 0.2192 0.5985 0.2576 -0.0339 -0.0192 -0.0242 148 LYS B O   
5323 C CB  . LYS B 148 ? 0.2396 0.6403 0.2708 -0.0167 -0.0300 -0.0185 148 LYS B CB  
5324 C CG  . LYS B 148 ? 0.2133 0.6268 0.2399 -0.0479 -0.0283 -0.0244 148 LYS B CG  
5325 C CD  . LYS B 148 ? 0.2928 0.7197 0.3103 -0.0604 -0.0301 -0.0246 148 LYS B CD  
5326 C CE  . LYS B 148 ? 0.3573 0.8005 0.3678 -0.0909 -0.0270 -0.0291 148 LYS B CE  
5327 N NZ  . LYS B 148 ? 0.3955 0.8065 0.3998 -0.1119 -0.0220 -0.0409 148 LYS B NZ  
5328 N N   . ASP B 149 ? 0.1716 0.5902 0.2192 0.0045  -0.0215 -0.0099 149 ASP B N   
5329 C CA  . ASP B 149 ? 0.1989 0.6378 0.2511 -0.0014 -0.0175 -0.0073 149 ASP B CA  
5330 C C   . ASP B 149 ? 0.1726 0.5846 0.2262 -0.0038 -0.0142 -0.0123 149 ASP B C   
5331 O O   . ASP B 149 ? 0.1712 0.5887 0.2263 -0.0216 -0.0111 -0.0140 149 ASP B O   
5332 C CB  . ASP B 149 ? 0.3905 0.8515 0.4445 0.0209  -0.0144 0.0031  149 ASP B CB  
5333 C CG  . ASP B 149 ? 0.5723 1.0076 0.6246 0.0471  -0.0114 0.0041  149 ASP B CG  
5334 O OD1 . ASP B 149 ? 0.6255 1.0351 0.6738 0.0562  -0.0135 0.0016  149 ASP B OD1 
5335 O OD2 . ASP B 149 ? 0.6340 1.0732 0.6872 0.0574  -0.0063 0.0069  149 ASP B OD2 
5336 N N   . LEU B 150 ? 0.1498 0.5211 0.1969 0.0124  -0.0129 -0.0139 150 LEU B N   
5337 C CA  . LEU B 150 ? 0.2002 0.5369 0.2427 0.0101  -0.0088 -0.0168 150 LEU B CA  
5338 C C   . LEU B 150 ? 0.2209 0.5274 0.2585 -0.0104 -0.0076 -0.0220 150 LEU B C   
5339 O O   . LEU B 150 ? 0.2434 0.5370 0.2803 -0.0205 -0.0032 -0.0221 150 LEU B O   
5340 C CB  . LEU B 150 ? 0.1828 0.4893 0.2187 0.0308  -0.0082 -0.0169 150 LEU B CB  
5341 C CG  . LEU B 150 ? 0.2291 0.5539 0.2657 0.0523  -0.0051 -0.0125 150 LEU B CG  
5342 C CD1 . LEU B 150 ? 0.2108 0.4980 0.2359 0.0681  -0.0033 -0.0150 150 LEU B CD1 
5343 C CD2 . LEU B 150 ? 0.1541 0.5036 0.1955 0.0492  -0.0006 -0.0099 150 LEU B CD2 
5344 N N   . LEU B 151 ? 0.1896 0.4839 0.2229 -0.0162 -0.0100 -0.0258 151 LEU B N   
5345 C CA  . LEU B 151 ? 0.2147 0.4794 0.2420 -0.0351 -0.0061 -0.0311 151 LEU B CA  
5346 C C   . LEU B 151 ? 0.3235 0.6080 0.3508 -0.0592 -0.0028 -0.0333 151 LEU B C   
5347 O O   . LEU B 151 ? 0.4034 0.6622 0.4265 -0.0734 0.0043  -0.0354 151 LEU B O   
5348 C CB  . LEU B 151 ? 0.2375 0.4859 0.2586 -0.0357 -0.0084 -0.0352 151 LEU B CB  
5349 C CG  . LEU B 151 ? 0.2243 0.4467 0.2438 -0.0157 -0.0105 -0.0335 151 LEU B CG  
5350 C CD1 . LEU B 151 ? 0.2679 0.4855 0.2822 -0.0149 -0.0135 -0.0362 151 LEU B CD1 
5351 C CD2 . LEU B 151 ? 0.2777 0.4618 0.2958 -0.0161 -0.0056 -0.0332 151 LEU B CD2 
5352 N N   . ASN B 152 ? 0.2237 0.5547 0.2557 -0.0644 -0.0071 -0.0320 152 ASN B N   
5353 C CA  . ASN B 152 ? 0.2106 0.5669 0.2424 -0.0901 -0.0046 -0.0340 152 ASN B CA  
5354 C C   . ASN B 152 ? 0.3057 0.6664 0.3428 -0.0920 0.0005  -0.0299 152 ASN B C   
5355 O O   . ASN B 152 ? 0.3359 0.6930 0.3691 -0.1154 0.0064  -0.0326 152 ASN B O   
5356 C CB  . ASN B 152 ? 0.3081 0.7231 0.3463 -0.0932 -0.0117 -0.0307 152 ASN B CB  
5357 C CG  . ASN B 152 ? 0.3962 0.8088 0.4226 -0.1085 -0.0140 -0.0365 152 ASN B CG  
5358 O OD1 . ASN B 152 ? 0.3692 0.7439 0.3871 -0.1106 -0.0126 -0.0432 152 ASN B OD1 
5359 N ND2 . ASN B 152 ? 0.4305 0.8759 0.4520 -0.1167 -0.0151 -0.0324 152 ASN B ND2 
5360 N N   . LYS B 153 ? 0.2887 0.6565 0.3329 -0.0687 -0.0007 -0.0236 153 LYS B N   
5361 C CA  . LYS B 153 ? 0.2624 0.6385 0.3108 -0.0691 0.0040  -0.0191 153 LYS B CA  
5362 C C   . LYS B 153 ? 0.2600 0.5910 0.3010 -0.0797 0.0111  -0.0205 153 LYS B C   
5363 O O   . LYS B 153 ? 0.3373 0.6715 0.3777 -0.0972 0.0170  -0.0193 153 LYS B O   
5364 C CB  . LYS B 153 ? 0.2459 0.6309 0.2988 -0.0415 0.0025  -0.0138 153 LYS B CB  
5365 C CG  . LYS B 153 ? 0.3184 0.7153 0.3743 -0.0395 0.0074  -0.0092 153 LYS B CG  
5366 C CD  . LYS B 153 ? 0.2597 0.6529 0.3142 -0.0128 0.0077  -0.0066 153 LYS B CD  
5367 C CE  . LYS B 153 ? 0.2822 0.7082 0.3418 -0.0079 0.0124  -0.0015 153 LYS B CE  
5368 N NZ  . LYS B 153 ? 0.3126 0.7329 0.3673 0.0174  0.0147  -0.0007 153 LYS B NZ  
5369 N N   . GLY B 154 ? 0.2605 0.5503 0.2964 -0.0687 0.0112  -0.0214 154 GLY B N   
5370 C CA  . GLY B 154 ? 0.3173 0.5649 0.3474 -0.0760 0.0185  -0.0205 154 GLY B CA  
5371 C C   . GLY B 154 ? 0.2268 0.4672 0.2585 -0.0687 0.0217  -0.0129 154 GLY B C   
5372 O O   . GLY B 154 ? 0.2763 0.4824 0.3046 -0.0681 0.0266  -0.0091 154 GLY B O   
5373 N N   . ARG B 155 ? 0.2722 0.5452 0.3086 -0.0623 0.0198  -0.0095 155 ARG B N   
5374 C CA  . ARG B 155 ? 0.2348 0.5049 0.2705 -0.0587 0.0235  -0.0025 155 ARG B CA  
5375 C C   . ARG B 155 ? 0.2307 0.5373 0.2701 -0.0461 0.0208  -0.0011 155 ARG B C   
5376 O O   . ARG B 155 ? 0.2361 0.5721 0.2804 -0.0415 0.0174  -0.0039 155 ARG B O   
5377 C CB  . ARG B 155 ? 0.2953 0.5603 0.3296 -0.0795 0.0322  0.0010  155 ARG B CB  
5378 C CG  . ARG B 155 ? 0.2749 0.5788 0.3135 -0.0956 0.0331  -0.0016 155 ARG B CG  
5379 C CD  . ARG B 155 ? 0.3718 0.6651 0.4064 -0.1198 0.0429  0.0006  155 ARG B CD  
5380 N NE  . ARG B 155 ? 0.4469 0.6943 0.4728 -0.1306 0.0493  -0.0024 155 ARG B NE  
5381 C CZ  . ARG B 155 ? 0.4434 0.6521 0.4638 -0.1326 0.0586  0.0042  155 ARG B CZ  
5382 N NH1 . ARG B 155 ? 0.4738 0.6400 0.4862 -0.1403 0.0665  0.0016  155 ARG B NH1 
5383 N NH2 . ARG B 155 ? 0.3804 0.5934 0.4028 -0.1260 0.0610  0.0144  155 ARG B NH2 
5384 N N   . ASN B 156 ? 0.1984 0.5035 0.2347 -0.0401 0.0233  0.0043  156 ASN B N   
5385 C CA  . ASN B 156 ? 0.2604 0.5971 0.2977 -0.0295 0.0241  0.0058  156 ASN B CA  
5386 C C   . ASN B 156 ? 0.2322 0.5743 0.2679 -0.0090 0.0199  0.0013  156 ASN B C   
5387 O O   . ASN B 156 ? 0.2216 0.5962 0.2628 -0.0012 0.0206  0.0010  156 ASN B O   
5388 C CB  . ASN B 156 ? 0.2806 0.6566 0.3263 -0.0423 0.0277  0.0076  156 ASN B CB  
5389 C CG  . ASN B 156 ? 0.4016 0.7678 0.4465 -0.0646 0.0336  0.0116  156 ASN B CG  
5390 O OD1 . ASN B 156 ? 0.4175 0.7560 0.4562 -0.0654 0.0367  0.0165  156 ASN B OD1 
5391 N ND2 . ASN B 156 ? 0.4240 0.8134 0.4744 -0.0836 0.0357  0.0104  156 ASN B ND2 
5392 N N   . TYR B 157 ? 0.1890 0.4992 0.2171 0.0000  0.0165  -0.0011 157 TYR B N   
5393 C CA  . TYR B 157 ? 0.2061 0.5123 0.2293 0.0183  0.0140  -0.0055 157 TYR B CA  
5394 C C   . TYR B 157 ? 0.2080 0.5176 0.2213 0.0306  0.0179  -0.0058 157 TYR B C   
5395 O O   . TYR B 157 ? 0.2320 0.5361 0.2391 0.0253  0.0199  -0.0029 157 TYR B O   
5396 C CB  . TYR B 157 ? 0.1827 0.4534 0.2009 0.0200  0.0092  -0.0083 157 TYR B CB  
5397 C CG  . TYR B 157 ? 0.1757 0.4409 0.2011 0.0095  0.0068  -0.0095 157 TYR B CG  
5398 C CD1 . TYR B 157 ? 0.2426 0.5217 0.2720 0.0141  0.0043  -0.0125 157 TYR B CD1 
5399 C CD2 . TYR B 157 ? 0.1823 0.4290 0.2092 -0.0049 0.0084  -0.0069 157 TYR B CD2 
5400 C CE1 . TYR B 157 ? 0.1901 0.4652 0.2231 0.0025  0.0024  -0.0146 157 TYR B CE1 
5401 C CE2 . TYR B 157 ? 0.1754 0.4134 0.2053 -0.0154 0.0084  -0.0096 157 TYR B CE2 
5402 C CZ  . TYR B 157 ? 0.1901 0.4432 0.2223 -0.0128 0.0049  -0.0142 157 TYR B CZ  
5403 O OH  . TYR B 157 ? 0.1768 0.4224 0.2092 -0.0250 0.0049  -0.0179 157 TYR B OH  
5404 N N   . THR B 158 ? 0.2272 0.5444 0.2373 0.0476  0.0202  -0.0090 158 THR B N   
5405 C CA  . THR B 158 ? 0.2198 0.5329 0.2161 0.0605  0.0262  -0.0115 158 THR B CA  
5406 C C   . THR B 158 ? 0.2094 0.4850 0.1900 0.0678  0.0241  -0.0177 158 THR B C   
5407 O O   . THR B 158 ? 0.2528 0.5114 0.2360 0.0676  0.0187  -0.0193 158 THR B O   
5408 C CB  . THR B 158 ? 0.2166 0.5593 0.2171 0.0766  0.0337  -0.0103 158 THR B CB  
5409 O OG1 . THR B 158 ? 0.2531 0.5924 0.2571 0.0887  0.0320  -0.0112 158 THR B OG1 
5410 C CG2 . THR B 158 ? 0.2511 0.6371 0.2680 0.0675  0.0354  -0.0037 158 THR B CG2 
5411 N N   . GLN B 159 ? 0.2423 0.5056 0.2051 0.0727  0.0291  -0.0216 159 GLN B N   
5412 C CA  . GLN B 159 ? 0.2434 0.4718 0.1878 0.0776  0.0285  -0.0287 159 GLN B CA  
5413 C C   . GLN B 159 ? 0.2851 0.5047 0.2294 0.0937  0.0317  -0.0317 159 GLN B C   
5414 O O   . GLN B 159 ? 0.2922 0.4848 0.2306 0.0938  0.0277  -0.0352 159 GLN B O   
5415 C CB  . GLN B 159 ? 0.2635 0.4830 0.1853 0.0791  0.0355  -0.0339 159 GLN B CB  
5416 C CG  . GLN B 159 ? 0.3214 0.5039 0.2197 0.0815  0.0367  -0.0431 159 GLN B CG  
5417 C CD  . GLN B 159 ? 0.3627 0.5286 0.2585 0.0656  0.0257  -0.0423 159 GLN B CD  
5418 O OE1 . GLN B 159 ? 0.2740 0.4539 0.1804 0.0535  0.0191  -0.0347 159 GLN B OE1 
5419 N NE2 . GLN B 159 ? 0.3724 0.5085 0.2542 0.0662  0.0247  -0.0491 159 GLN B NE2 
5420 N N   . GLU B 160 ? 0.2378 0.4825 0.1897 0.1078  0.0392  -0.0288 160 GLU B N   
5421 C CA  . GLU B 160 ? 0.2854 0.5257 0.2385 0.1257  0.0432  -0.0284 160 GLU B CA  
5422 C C   . GLU B 160 ? 0.2961 0.5403 0.2647 0.1198  0.0332  -0.0248 160 GLU B C   
5423 O O   . GLU B 160 ? 0.2926 0.5143 0.2558 0.1278  0.0326  -0.0265 160 GLU B O   
5424 C CB  . GLU B 160 ? 0.3305 0.6018 0.2921 0.1411  0.0520  -0.0220 160 GLU B CB  
5425 C CG  . GLU B 160 ? 0.5171 0.7717 0.4607 0.1496  0.0633  -0.0255 160 GLU B CG  
5426 C CD  . GLU B 160 ? 0.6013 0.8649 0.5382 0.1362  0.0642  -0.0286 160 GLU B CD  
5427 O OE1 . GLU B 160 ? 0.4680 0.7590 0.4191 0.1218  0.0573  -0.0247 160 GLU B OE1 
5428 O OE2 . GLU B 160 ? 0.6474 0.8891 0.5635 0.1389  0.0726  -0.0348 160 GLU B OE2 
5429 N N   . GLU B 161 ? 0.2381 0.5082 0.2239 0.1049  0.0263  -0.0202 161 GLU B N   
5430 C CA  . GLU B 161 ? 0.2337 0.5053 0.2309 0.0971  0.0180  -0.0183 161 GLU B CA  
5431 C C   . GLU B 161 ? 0.2581 0.4904 0.2463 0.0894  0.0123  -0.0229 161 GLU B C   
5432 O O   . GLU B 161 ? 0.2439 0.4629 0.2324 0.0928  0.0091  -0.0236 161 GLU B O   
5433 C CB  . GLU B 161 ? 0.2364 0.5379 0.2493 0.0797  0.0141  -0.0142 161 GLU B CB  
5434 C CG  . GLU B 161 ? 0.2652 0.6137 0.2914 0.0854  0.0172  -0.0080 161 GLU B CG  
5435 C CD  . GLU B 161 ? 0.3196 0.6979 0.3568 0.0664  0.0163  -0.0049 161 GLU B CD  
5436 O OE1 . GLU B 161 ? 0.2638 0.6229 0.2982 0.0495  0.0140  -0.0070 161 GLU B OE1 
5437 O OE2 . GLU B 161 ? 0.3438 0.7621 0.3910 0.0678  0.0181  0.0007  161 GLU B OE2 
5438 N N   . LYS B 162 ? 0.2285 0.4452 0.2091 0.0791  0.0112  -0.0249 162 LYS B N   
5439 C CA  . LYS B 162 ? 0.1888 0.3739 0.1619 0.0721  0.0061  -0.0276 162 LYS B CA  
5440 C C   . LYS B 162 ? 0.2355 0.3942 0.1937 0.0837  0.0085  -0.0330 162 LYS B C   
5441 O O   . LYS B 162 ? 0.2327 0.3720 0.1902 0.0816  0.0042  -0.0340 162 LYS B O   
5442 C CB  . LYS B 162 ? 0.1921 0.3721 0.1586 0.0614  0.0051  -0.0267 162 LYS B CB  
5443 C CG  . LYS B 162 ? 0.2281 0.3841 0.1900 0.0528  -0.0008 -0.0264 162 LYS B CG  
5444 C CD  . LYS B 162 ? 0.2445 0.4036 0.2011 0.0430  -0.0021 -0.0225 162 LYS B CD  
5445 C CE  . LYS B 162 ? 0.2869 0.4470 0.2251 0.0472  0.0031  -0.0277 162 LYS B CE  
5446 N NZ  . LYS B 162 ? 0.2535 0.4183 0.1842 0.0363  0.0008  -0.0234 162 LYS B NZ  
5447 N N   . GLU B 163 ? 0.2687 0.4240 0.2134 0.0957  0.0169  -0.0364 163 GLU B N   
5448 C CA  . GLU B 163 ? 0.2574 0.3813 0.1843 0.1061  0.0220  -0.0421 163 GLU B CA  
5449 C C   . GLU B 163 ? 0.3110 0.4359 0.2458 0.1188  0.0226  -0.0386 163 GLU B C   
5450 O O   . GLU B 163 ? 0.3323 0.4280 0.2569 0.1219  0.0230  -0.0415 163 GLU B O   
5451 C CB  . GLU B 163 ? 0.3776 0.4945 0.2860 0.1170  0.0340  -0.0469 163 GLU B CB  
5452 C CG  . GLU B 163 ? 0.4202 0.5267 0.3126 0.1030  0.0333  -0.0523 163 GLU B CG  
5453 C CD  . GLU B 163 ? 0.4752 0.5799 0.3495 0.1118  0.0459  -0.0573 163 GLU B CD  
5454 O OE1 . GLU B 163 ? 0.4670 0.5669 0.3266 0.0995  0.0455  -0.0616 163 GLU B OE1 
5455 O OE2 . GLU B 163 ? 0.4870 0.5963 0.3615 0.1313  0.0569  -0.0562 163 GLU B OE2 
5456 N N   . TYR B 164 ? 0.2809 0.4410 0.2334 0.1248  0.0225  -0.0318 164 TYR B N   
5457 C CA  . TYR B 164 ? 0.3014 0.4699 0.2628 0.1348  0.0212  -0.0265 164 TYR B CA  
5458 C C   . TYR B 164 ? 0.2829 0.4377 0.2489 0.1215  0.0115  -0.0274 164 TYR B C   
5459 O O   . TYR B 164 ? 0.3120 0.4487 0.2733 0.1283  0.0114  -0.0270 164 TYR B O   
5460 C CB  . TYR B 164 ? 0.2454 0.4623 0.2256 0.1389  0.0211  -0.0185 164 TYR B CB  
5461 C CG  . TYR B 164 ? 0.3413 0.5755 0.3318 0.1459  0.0177  -0.0117 164 TYR B CG  
5462 C CD1 . TYR B 164 ? 0.4466 0.6693 0.4295 0.1642  0.0236  -0.0059 164 TYR B CD1 
5463 C CD2 . TYR B 164 ? 0.4130 0.6675 0.4165 0.1296  0.0083  -0.0099 164 TYR B CD2 
5464 C CE1 . TYR B 164 ? 0.4300 0.6663 0.4191 0.1671  0.0194  0.0023  164 TYR B CE1 
5465 C CE2 . TYR B 164 ? 0.4436 0.7165 0.4543 0.1341  0.0047  -0.0039 164 TYR B CE2 
5466 C CZ  . TYR B 164 ? 0.4502 0.7135 0.4529 0.1521  0.0098  0.0028  164 TYR B CZ  
5467 O OH  . TYR B 164 ? 0.4871 0.7649 0.4929 0.1532  0.0060  0.0103  164 TYR B OH  
5468 N N   . VAL B 165 ? 0.2080 0.3699 0.1824 0.1034  0.0048  -0.0279 165 VAL B N   
5469 C CA  . VAL B 165 ? 0.2344 0.3816 0.2127 0.0916  -0.0021 -0.0286 165 VAL B CA  
5470 C C   . VAL B 165 ? 0.2301 0.3404 0.1939 0.0923  -0.0021 -0.0328 165 VAL B C   
5471 O O   . VAL B 165 ? 0.2476 0.3432 0.2105 0.0933  -0.0043 -0.0327 165 VAL B O   
5472 C CB  . VAL B 165 ? 0.2118 0.3675 0.1993 0.0742  -0.0060 -0.0276 165 VAL B CB  
5473 C CG1 . VAL B 165 ? 0.1977 0.3351 0.1884 0.0643  -0.0106 -0.0278 165 VAL B CG1 
5474 C CG2 . VAL B 165 ? 0.2004 0.3906 0.2004 0.0700  -0.0056 -0.0243 165 VAL B CG2 
5475 N N   . LEU B 166 ? 0.2658 0.3622 0.2170 0.0902  0.0006  -0.0367 166 LEU B N   
5476 C CA  . LEU B 166 ? 0.2854 0.3491 0.2209 0.0869  0.0004  -0.0414 166 LEU B CA  
5477 C C   . LEU B 166 ? 0.2946 0.3373 0.2185 0.1009  0.0064  -0.0433 166 LEU B C   
5478 O O   . LEU B 166 ? 0.3335 0.3529 0.2513 0.0978  0.0047  -0.0448 166 LEU B O   
5479 C CB  . LEU B 166 ? 0.2757 0.3317 0.1964 0.0807  0.0028  -0.0459 166 LEU B CB  
5480 C CG  . LEU B 166 ? 0.2592 0.3288 0.1880 0.0654  -0.0038 -0.0423 166 LEU B CG  
5481 C CD1 . LEU B 166 ? 0.3322 0.4032 0.2460 0.0616  -0.0005 -0.0456 166 LEU B CD1 
5482 C CD2 . LEU B 166 ? 0.3431 0.4001 0.2745 0.0544  -0.0105 -0.0403 166 LEU B CD2 
5483 N N   . ASN B 167 ? 0.3052 0.3563 0.2262 0.1174  0.0146  -0.0421 167 ASN B N   
5484 C CA  . ASN B 167 ? 0.3402 0.3707 0.2504 0.1340  0.0225  -0.0414 167 ASN B CA  
5485 C C   . ASN B 167 ? 0.3161 0.3526 0.2382 0.1358  0.0168  -0.0354 167 ASN B C   
5486 O O   . ASN B 167 ? 0.3554 0.3635 0.2673 0.1384  0.0186  -0.0361 167 ASN B O   
5487 C CB  . ASN B 167 ? 0.4003 0.4455 0.3092 0.1542  0.0333  -0.0380 167 ASN B CB  
5488 C CG  . ASN B 167 ? 0.5923 0.6191 0.4813 0.1553  0.0430  -0.0457 167 ASN B CG  
5489 O OD1 . ASN B 167 ? 0.6675 0.6652 0.5392 0.1416  0.0421  -0.0542 167 ASN B OD1 
5490 N ND2 . ASN B 167 ? 0.5595 0.6047 0.4514 0.1684  0.0514  -0.0416 167 ASN B ND2 
5491 N N   . LYS B 168 ? 0.2979 0.3705 0.2400 0.1326  0.0104  -0.0298 168 LYS B N   
5492 C CA  . LYS B 168 ? 0.3081 0.3883 0.2592 0.1321  0.0050  -0.0249 168 LYS B CA  
5493 C C   . LYS B 168 ? 0.2851 0.3413 0.2339 0.1172  -0.0008 -0.0288 168 LYS B C   
5494 O O   . LYS B 168 ? 0.2832 0.3267 0.2296 0.1195  -0.0017 -0.0268 168 LYS B O   
5495 C CB  . LYS B 168 ? 0.2051 0.3282 0.1747 0.1267  -0.0003 -0.0203 168 LYS B CB  
5496 C CG  . LYS B 168 ? 0.2458 0.4020 0.2214 0.1415  0.0047  -0.0140 168 LYS B CG  
5497 C CD  . LYS B 168 ? 0.3346 0.4890 0.3056 0.1633  0.0106  -0.0064 168 LYS B CD  
5498 C CE  . LYS B 168 ? 0.3346 0.5054 0.3133 0.1607  0.0037  -0.0005 168 LYS B CE  
5499 N NZ  . LYS B 168 ? 0.4915 0.6647 0.4649 0.1752  0.0090  0.0109  168 LYS B NZ  
5500 N N   . TYR B 169 ? 0.2116 0.2635 0.1615 0.1025  -0.0042 -0.0329 169 TYR B N   
5501 C CA  . TYR B 169 ? 0.2533 0.2871 0.2032 0.0897  -0.0090 -0.0345 169 TYR B CA  
5502 C C   . TYR B 169 ? 0.2572 0.2576 0.1901 0.0921  -0.0057 -0.0376 169 TYR B C   
5503 O O   . TYR B 169 ? 0.2809 0.2677 0.2133 0.0892  -0.0076 -0.0365 169 TYR B O   
5504 C CB  . TYR B 169 ? 0.2386 0.2785 0.1937 0.0762  -0.0124 -0.0353 169 TYR B CB  
5505 C CG  . TYR B 169 ? 0.2872 0.3502 0.2589 0.0689  -0.0153 -0.0320 169 TYR B CG  
5506 C CD1 . TYR B 169 ? 0.2491 0.3306 0.2284 0.0724  -0.0152 -0.0302 169 TYR B CD1 
5507 C CD2 . TYR B 169 ? 0.2148 0.2806 0.1929 0.0577  -0.0173 -0.0301 169 TYR B CD2 
5508 C CE1 . TYR B 169 ? 0.2526 0.3510 0.2431 0.0623  -0.0165 -0.0289 169 TYR B CE1 
5509 C CE2 . TYR B 169 ? 0.2023 0.2824 0.1926 0.0506  -0.0173 -0.0273 169 TYR B CE2 
5510 C CZ  . TYR B 169 ? 0.1767 0.2708 0.1720 0.0517  -0.0167 -0.0279 169 TYR B CZ  
5511 O OH  . TYR B 169 ? 0.2140 0.3182 0.2177 0.0415  -0.0154 -0.0268 169 TYR B OH  
5512 N N   . PHE B 170 ? 0.2644 0.2495 0.1812 0.0965  0.0004  -0.0421 170 PHE B N   
5513 C CA  . PHE B 170 ? 0.3207 0.2695 0.2175 0.0961  0.0052  -0.0465 170 PHE B CA  
5514 C C   . PHE B 170 ? 0.3357 0.2713 0.2281 0.1113  0.0107  -0.0425 170 PHE B C   
5515 O O   . PHE B 170 ? 0.3188 0.2260 0.1998 0.1082  0.0126  -0.0438 170 PHE B O   
5516 C CB  . PHE B 170 ? 0.3183 0.2502 0.1948 0.0959  0.0124  -0.0537 170 PHE B CB  
5517 C CG  . PHE B 170 ? 0.3295 0.2618 0.2020 0.0759  0.0064  -0.0579 170 PHE B CG  
5518 C CD1 . PHE B 170 ? 0.3903 0.3011 0.2519 0.0616  0.0039  -0.0611 170 PHE B CD1 
5519 C CD2 . PHE B 170 ? 0.4255 0.3837 0.3065 0.0709  0.0028  -0.0569 170 PHE B CD2 
5520 C CE1 . PHE B 170 ? 0.3888 0.3073 0.2485 0.0429  -0.0027 -0.0626 170 PHE B CE1 
5521 C CE2 . PHE B 170 ? 0.4288 0.3916 0.3071 0.0535  -0.0032 -0.0580 170 PHE B CE2 
5522 C CZ  . PHE B 170 ? 0.4064 0.3515 0.2746 0.0397  -0.0063 -0.0604 170 PHE B CZ  
5523 N N   . GLU B 171 ? 0.3308 0.2889 0.2324 0.1272  0.0132  -0.0364 171 GLU B N   
5524 C CA  . GLU B 171 ? 0.3496 0.3028 0.2499 0.1424  0.0172  -0.0293 171 GLU B CA  
5525 C C   . GLU B 171 ? 0.3662 0.3212 0.2750 0.1326  0.0093  -0.0266 171 GLU B C   
5526 O O   . GLU B 171 ? 0.3427 0.2742 0.2422 0.1369  0.0125  -0.0242 171 GLU B O   
5527 C CB  . GLU B 171 ? 0.3741 0.3633 0.2867 0.1589  0.0191  -0.0212 171 GLU B CB  
5528 C CG  . GLU B 171 ? 0.5564 0.5508 0.4704 0.1730  0.0218  -0.0102 171 GLU B CG  
5529 C CD  . GLU B 171 ? 0.7143 0.7479 0.6397 0.1840  0.0234  -0.0004 171 GLU B CD  
5530 O OE1 . GLU B 171 ? 0.7803 0.8310 0.7102 0.1917  0.0231  0.0103  171 GLU B OE1 
5531 O OE2 . GLU B 171 ? 0.7013 0.7505 0.6306 0.1841  0.0251  -0.0032 171 GLU B OE2 
5532 N N   . ILE B 172 ? 0.2879 0.2685 0.2132 0.1197  0.0004  -0.0269 172 ILE B N   
5533 C CA  . ILE B 172 ? 0.3133 0.2941 0.2457 0.1097  -0.0054 -0.0254 172 ILE B CA  
5534 C C   . ILE B 172 ? 0.2768 0.2253 0.1988 0.1001  -0.0048 -0.0290 172 ILE B C   
5535 O O   . ILE B 172 ? 0.3198 0.2545 0.2382 0.1000  -0.0044 -0.0264 172 ILE B O   
5536 C CB  . ILE B 172 ? 0.2691 0.2761 0.2179 0.0971  -0.0117 -0.0263 172 ILE B CB  
5537 C CG1 . ILE B 172 ? 0.2848 0.3256 0.2431 0.1026  -0.0130 -0.0224 172 ILE B CG1 
5538 C CG2 . ILE B 172 ? 0.2986 0.2980 0.2522 0.0855  -0.0152 -0.0263 172 ILE B CG2 
5539 C CD1 . ILE B 172 ? 0.3023 0.3521 0.2611 0.1078  -0.0142 -0.0171 172 ILE B CD1 
5540 N N   . ILE B 173 ? 0.2524 0.1910 0.1689 0.0906  -0.0049 -0.0344 173 ILE B N   
5541 C CA  . ILE B 173 ? 0.2708 0.1852 0.1780 0.0781  -0.0054 -0.0374 173 ILE B CA  
5542 C C   . ILE B 173 ? 0.3198 0.2004 0.2072 0.0850  0.0023  -0.0383 173 ILE B C   
5543 O O   . ILE B 173 ? 0.3592 0.2232 0.2424 0.0783  0.0021  -0.0372 173 ILE B O   
5544 C CB  . ILE B 173 ? 0.2959 0.2107 0.1987 0.0659  -0.0074 -0.0423 173 ILE B CB  
5545 C CG1 . ILE B 173 ? 0.2712 0.2158 0.1941 0.0586  -0.0142 -0.0390 173 ILE B CG1 
5546 C CG2 . ILE B 173 ? 0.3749 0.2660 0.2642 0.0517  -0.0074 -0.0457 173 ILE B CG2 
5547 C CD1 . ILE B 173 ? 0.2865 0.2373 0.2062 0.0480  -0.0165 -0.0413 173 ILE B CD1 
5548 N N   . LYS B 174 ? 0.3537 0.2229 0.2284 0.0994  0.0106  -0.0394 174 LYS B N   
5549 C CA  . LYS B 174 ? 0.3656 0.1970 0.2189 0.1083  0.0211  -0.0396 174 LYS B CA  
5550 C C   . LYS B 174 ? 0.4158 0.2469 0.2737 0.1186  0.0217  -0.0306 174 LYS B C   
5551 O O   . LYS B 174 ? 0.4240 0.2210 0.2654 0.1207  0.0289  -0.0296 174 LYS B O   
5552 C CB  . LYS B 174 ? 0.3918 0.2137 0.2325 0.1254  0.0321  -0.0409 174 LYS B CB  
5553 C CG  . LYS B 174 ? 0.4597 0.2682 0.2856 0.1142  0.0350  -0.0516 174 LYS B CG  
5554 C CD  . LYS B 174 ? 0.5947 0.3826 0.4057 0.1244  0.0487  -0.0517 174 LYS B CD  
5555 C CE  . LYS B 174 ? 0.7240 0.5399 0.5438 0.1359  0.0504  -0.0506 174 LYS B CE  
5556 N NZ  . LYS B 174 ? 0.7541 0.5565 0.5568 0.1251  0.0545  -0.0619 174 LYS B NZ  
5557 N N   . LYS B 175 ? 0.3484 0.2157 0.2263 0.1236  0.0148  -0.0241 175 LYS B N   
5558 C CA  . LYS B 175 ? 0.3998 0.2725 0.2817 0.1314  0.0142  -0.0153 175 LYS B CA  
5559 C C   . LYS B 175 ? 0.3053 0.1810 0.1952 0.1152  0.0070  -0.0159 175 LYS B C   
5560 O O   . LYS B 175 ? 0.3303 0.2125 0.2231 0.1192  0.0059  -0.0094 175 LYS B O   
5561 C CB  . LYS B 175 ? 0.3860 0.2990 0.2824 0.1441  0.0111  -0.0081 175 LYS B CB  
5562 C CG  . LYS B 175 ? 0.5037 0.4199 0.3950 0.1628  0.0195  -0.0028 175 LYS B CG  
5563 C CD  . LYS B 175 ? 0.6482 0.6129 0.5562 0.1713  0.0150  0.0045  175 LYS B CD  
5564 C CE  . LYS B 175 ? 0.7234 0.7177 0.6470 0.1565  0.0036  0.0015  175 LYS B CE  
5565 N NZ  . LYS B 175 ? 0.8077 0.8499 0.7455 0.1606  -0.0008 0.0071  175 LYS B NZ  
5566 N N   . THR B 176 ? 0.3257 0.1987 0.2191 0.0977  0.0028  -0.0224 176 THR B N   
5567 C CA  . THR B 176 ? 0.3068 0.1905 0.2123 0.0849  -0.0031 -0.0214 176 THR B CA  
5568 C C   . THR B 176 ? 0.3365 0.1957 0.2325 0.0808  -0.0001 -0.0188 176 THR B C   
5569 O O   . THR B 176 ? 0.3558 0.2230 0.2575 0.0814  -0.0014 -0.0142 176 THR B O   
5570 C CB  . THR B 176 ? 0.2714 0.1651 0.1862 0.0701  -0.0079 -0.0259 176 THR B CB  
5571 O OG1 . THR B 176 ? 0.3187 0.2376 0.2443 0.0736  -0.0106 -0.0268 176 THR B OG1 
5572 C CG2 . THR B 176 ? 0.2633 0.1645 0.1901 0.0588  -0.0113 -0.0234 176 THR B CG2 
5573 N N   . LEU B 177 ? 0.3362 0.1650 0.2160 0.0748  0.0045  -0.0223 177 LEU B N   
5574 C CA  . LEU B 177 ? 0.3474 0.1523 0.2174 0.0694  0.0081  -0.0194 177 LEU B CA  
5575 C C   . LEU B 177 ? 0.3987 0.1952 0.2618 0.0864  0.0134  -0.0116 177 LEU B C   
5576 O O   . LEU B 177 ? 0.4008 0.1941 0.2643 0.0841  0.0137  -0.0064 177 LEU B O   
5577 C CB  . LEU B 177 ? 0.4104 0.1813 0.2604 0.0576  0.0133  -0.0254 177 LEU B CB  
5578 C CG  . LEU B 177 ? 0.4445 0.2289 0.3015 0.0374  0.0067  -0.0308 177 LEU B CG  
5579 C CD1 . LEU B 177 ? 0.5344 0.2865 0.3685 0.0214  0.0115  -0.0374 177 LEU B CD1 
5580 C CD2 . LEU B 177 ? 0.4366 0.2463 0.3142 0.0282  0.0000  -0.0257 177 LEU B CD2 
5581 N N   . SER B 178 ? 0.4021 0.1987 0.2598 0.1044  0.0179  -0.0091 178 SER B N   
5582 C CA  . SER B 178 ? 0.4347 0.2282 0.2868 0.1231  0.0231  0.0013  178 SER B CA  
5583 C C   . SER B 178 ? 0.3798 0.2086 0.2474 0.1240  0.0156  0.0075  178 SER B C   
5584 O O   . SER B 178 ? 0.4035 0.2280 0.2657 0.1311  0.0181  0.0163  178 SER B O   
5585 C CB  . SER B 178 ? 0.4409 0.2419 0.2910 0.1394  0.0286  0.0045  178 SER B CB  
5586 O OG  . SER B 178 ? 0.5927 0.3588 0.4254 0.1378  0.0392  0.0020  178 SER B OG  
5587 N N   . ILE B 179 ? 0.3259 0.1875 0.2106 0.1162  0.0073  0.0029  179 ILE B N   
5588 C CA  . ILE B 179 ? 0.3262 0.2175 0.2214 0.1149  0.0018  0.0068  179 ILE B CA  
5589 C C   . ILE B 179 ? 0.3364 0.2173 0.2315 0.1020  0.0014  0.0064  179 ILE B C   
5590 O O   . ILE B 179 ? 0.3564 0.2475 0.2507 0.1037  0.0008  0.0119  179 ILE B O   
5591 C CB  . ILE B 179 ? 0.3018 0.2268 0.2122 0.1096  -0.0045 0.0019  179 ILE B CB  
5592 C CG1 . ILE B 179 ? 0.4462 0.4017 0.3615 0.1107  -0.0084 0.0063  179 ILE B CG1 
5593 C CG2 . ILE B 179 ? 0.2642 0.1876 0.1839 0.0927  -0.0074 -0.0062 179 ILE B CG2 
5594 C CD1 . ILE B 179 ? 0.4143 0.4032 0.3405 0.1080  -0.0130 0.0030  179 ILE B CD1 
5595 N N   . TYR B 180 ? 0.3125 0.1753 0.2078 0.0889  0.0020  0.0009  180 TYR B N   
5596 C CA  . TYR B 180 ? 0.3290 0.1830 0.2246 0.0778  0.0029  0.0022  180 TYR B CA  
5597 C C   . TYR B 180 ? 0.3562 0.1854 0.2358 0.0840  0.0090  0.0094  180 TYR B C   
5598 O O   . TYR B 180 ? 0.3429 0.1759 0.2221 0.0825  0.0096  0.0143  180 TYR B O   
5599 C CB  . TYR B 180 ? 0.2922 0.1385 0.1929 0.0623  0.0019  -0.0031 180 TYR B CB  
5600 C CG  . TYR B 180 ? 0.3255 0.1979 0.2441 0.0562  -0.0029 -0.0069 180 TYR B CG  
5601 C CD1 . TYR B 180 ? 0.2490 0.1366 0.1788 0.0516  -0.0031 -0.0055 180 TYR B CD1 
5602 C CD2 . TYR B 180 ? 0.2625 0.1423 0.1852 0.0559  -0.0057 -0.0114 180 TYR B CD2 
5603 C CE1 . TYR B 180 ? 0.2518 0.1580 0.1963 0.0474  -0.0049 -0.0082 180 TYR B CE1 
5604 C CE2 . TYR B 180 ? 0.2375 0.1389 0.1758 0.0512  -0.0089 -0.0133 180 TYR B CE2 
5605 C CZ  . TYR B 180 ? 0.2213 0.1343 0.1703 0.0474  -0.0080 -0.0115 180 TYR B CZ  
5606 O OH  . TYR B 180 ? 0.2224 0.1514 0.1851 0.0438  -0.0086 -0.0127 180 TYR B OH  
5607 N N   . ARG B 181 ? 0.3756 0.1772 0.2402 0.0912  0.0148  0.0104  181 ARG B N   
5608 C CA  . ARG B 181 ? 0.4129 0.1878 0.2607 0.0998  0.0225  0.0189  181 ARG B CA  
5609 C C   . ARG B 181 ? 0.3808 0.1781 0.2304 0.1160  0.0215  0.0294  181 ARG B C   
5610 O O   . ARG B 181 ? 0.4252 0.2148 0.2670 0.1188  0.0246  0.0379  181 ARG B O   
5611 C CB  . ARG B 181 ? 0.4952 0.2333 0.3245 0.1076  0.0317  0.0181  181 ARG B CB  
5612 C CG  . ARG B 181 ? 0.4728 0.1855 0.2942 0.0894  0.0336  0.0075  181 ARG B CG  
5613 C CD  . ARG B 181 ? 0.5126 0.1955 0.3162 0.0933  0.0443  0.0061  181 ARG B CD  
5614 N NE  . ARG B 181 ? 0.5853 0.2495 0.3799 0.0756  0.0451  -0.0056 181 ARG B NE  
5615 C CZ  . ARG B 181 ? 0.5824 0.2536 0.3781 0.0764  0.0435  -0.0130 181 ARG B CZ  
5616 N NH1 . ARG B 181 ? 0.5426 0.2390 0.3492 0.0945  0.0417  -0.0097 181 ARG B NH1 
5617 N NH2 . ARG B 181 ? 0.6184 0.2733 0.4033 0.0579  0.0439  -0.0235 181 ARG B NH2 
5618 N N   . GLU B 182 ? 0.3700 0.1978 0.2292 0.1255  0.0168  0.0295  182 GLU B N   
5619 C CA  . GLU B 182 ? 0.3638 0.2187 0.2239 0.1399  0.0151  0.0404  182 GLU B CA  
5620 C C   . GLU B 182 ? 0.3603 0.2385 0.2262 0.1291  0.0095  0.0407  182 GLU B C   
5621 O O   . GLU B 182 ? 0.3594 0.2419 0.2178 0.1352  0.0109  0.0509  182 GLU B O   
5622 C CB  . GLU B 182 ? 0.4159 0.3016 0.2856 0.1497  0.0113  0.0400  182 GLU B CB  
5623 C CG  . GLU B 182 ? 0.5762 0.5008 0.4494 0.1613  0.0075  0.0514  182 GLU B CG  
5624 C CD  . GLU B 182 ? 0.6998 0.6586 0.5838 0.1693  0.0039  0.0516  182 GLU B CD  
5625 O OE1 . GLU B 182 ? 0.7244 0.6723 0.6116 0.1682  0.0056  0.0434  182 GLU B OE1 
5626 O OE2 . GLU B 182 ? 0.7502 0.7492 0.6389 0.1754  -0.0009 0.0603  182 GLU B OE2 
5627 N N   . ILE B 183 ? 0.3408 0.2338 0.2189 0.1135  0.0043  0.0300  183 ILE B N   
5628 C CA  . ILE B 183 ? 0.3541 0.2660 0.2351 0.1038  0.0015  0.0292  183 ILE B CA  
5629 C C   . ILE B 183 ? 0.3831 0.2715 0.2562 0.0980  0.0064  0.0325  183 ILE B C   
5630 O O   . ILE B 183 ? 0.3553 0.2540 0.2236 0.0960  0.0066  0.0368  183 ILE B O   
5631 C CB  . ILE B 183 ? 0.3718 0.2996 0.2663 0.0902  -0.0022 0.0177  183 ILE B CB  
5632 C CG1 . ILE B 183 ? 0.3313 0.2378 0.2323 0.0803  -0.0002 0.0113  183 ILE B CG1 
5633 C CG2 . ILE B 183 ? 0.3207 0.2730 0.2217 0.0949  -0.0068 0.0153  183 ILE B CG2 
5634 C CD1 . ILE B 183 ? 0.3145 0.2174 0.2192 0.0684  0.0026  0.0093  183 ILE B CD1 
5635 N N   . LYS B 184 ? 0.3341 0.1918 0.2039 0.0944  0.0106  0.0310  184 LYS B N   
5636 C CA  . LYS B 184 ? 0.3712 0.2074 0.2338 0.0871  0.0157  0.0347  184 LYS B CA  
5637 C C   . LYS B 184 ? 0.4226 0.2452 0.2689 0.0999  0.0206  0.0474  184 LYS B C   
5638 O O   . LYS B 184 ? 0.4365 0.2625 0.2775 0.0978  0.0223  0.0535  184 LYS B O   
5639 C CB  . LYS B 184 ? 0.4346 0.2454 0.2975 0.0767  0.0182  0.0291  184 LYS B CB  
5640 C CG  . LYS B 184 ? 0.5230 0.3115 0.3784 0.0671  0.0236  0.0327  184 LYS B CG  
5641 C CD  . LYS B 184 ? 0.4650 0.2355 0.3210 0.0540  0.0244  0.0262  184 LYS B CD  
5642 C CE  . LYS B 184 ? 0.5207 0.2707 0.3693 0.0411  0.0298  0.0297  184 LYS B CE  
5643 N NZ  . LYS B 184 ? 0.6199 0.3449 0.4491 0.0524  0.0368  0.0390  184 LYS B NZ  
5644 N N   . GLU B 185 ? 0.4285 0.2358 0.2661 0.1145  0.0241  0.0526  185 GLU B N   
5645 C CA  . GLU B 185 ? 0.4499 0.2431 0.2722 0.1294  0.0304  0.0674  185 GLU B CA  
5646 C C   . GLU B 185 ? 0.4232 0.2559 0.2478 0.1389  0.0251  0.0766  185 GLU B C   
5647 O O   . GLU B 185 ? 0.4894 0.3198 0.3032 0.1457  0.0285  0.0894  185 GLU B O   
5648 C CB  . GLU B 185 ? 0.5522 0.3192 0.3652 0.1438  0.0381  0.0708  185 GLU B CB  
5649 C CG  . GLU B 185 ? 0.8183 0.5668 0.6194 0.1506  0.0476  0.0818  185 GLU B CG  
5650 C CD  . GLU B 185 ? 1.0091 0.7918 0.8129 0.1667  0.0452  0.0957  185 GLU B CD  
5651 O OE1 . GLU B 185 ? 1.0650 0.8436 0.8610 0.1694  0.0491  0.1065  185 GLU B OE1 
5652 O OE2 . GLU B 185 ? 1.0263 0.8432 0.8404 0.1752  0.0391  0.0960  185 GLU B OE2 
5653 N N   . GLU B 186 ? 0.3474 0.3527 0.2909 0.1623  -0.0375 0.0388  186 GLU B N   
5654 C CA  . GLU B 186 ? 0.3656 0.4067 0.3151 0.1648  -0.0461 0.0403  186 GLU B CA  
5655 C C   . GLU B 186 ? 0.3201 0.3678 0.2590 0.1527  -0.0504 0.0387  186 GLU B C   
5656 O O   . GLU B 186 ? 0.3633 0.4397 0.3038 0.1544  -0.0587 0.0387  186 GLU B O   
5657 C CB  . GLU B 186 ? 0.3603 0.4325 0.3315 0.1629  -0.0474 0.0312  186 GLU B CB  
5658 C CG  . GLU B 186 ? 0.3778 0.4581 0.3611 0.1799  -0.0452 0.0350  186 GLU B CG  
5659 C CD  . GLU B 186 ? 0.4904 0.5987 0.4962 0.1764  -0.0432 0.0270  186 GLU B CD  
5660 O OE1 . GLU B 186 ? 0.4674 0.5861 0.4799 0.1596  -0.0439 0.0187  186 GLU B OE1 
5661 O OE2 . GLU B 186 ? 0.5215 0.6387 0.5381 0.1865  -0.0393 0.0289  186 GLU B OE2 
5662 N N   . GLY B 187 ? 0.3243 0.3480 0.2523 0.1415  -0.0452 0.0369  187 GLY B N   
5663 C CA  . GLY B 187 ? 0.3592 0.3895 0.2766 0.1315  -0.0477 0.0347  187 GLY B CA  
5664 C C   . GLY B 187 ? 0.3683 0.4192 0.2959 0.1199  -0.0507 0.0203  187 GLY B C   
5665 O O   . GLY B 187 ? 0.2981 0.3602 0.2178 0.1142  -0.0546 0.0161  187 GLY B O   
5666 N N   . LYS B 188 ? 0.2873 0.3430 0.2320 0.1166  -0.0486 0.0127  188 LYS B N   
5667 C CA  . LYS B 188 ? 0.2555 0.3292 0.2125 0.1049  -0.0516 0.0003  188 LYS B CA  
5668 C C   . LYS B 188 ? 0.2341 0.2890 0.1882 0.0921  -0.0455 -0.0064 188 LYS B C   
5669 O O   . LYS B 188 ? 0.2261 0.2904 0.1864 0.0822  -0.0482 -0.0162 188 LYS B O   
5670 C CB  . LYS B 188 ? 0.2639 0.3560 0.2429 0.1066  -0.0520 -0.0027 188 LYS B CB  
5671 C CG  . LYS B 188 ? 0.2753 0.3940 0.2612 0.1189  -0.0595 0.0029  188 LYS B CG  
5672 C CD  . LYS B 188 ? 0.2662 0.4073 0.2766 0.1205  -0.0589 0.0007  188 LYS B CD  
5673 C CE  . LYS B 188 ? 0.4241 0.5961 0.4437 0.1332  -0.0672 0.0064  188 LYS B CE  
5674 N NZ  . LYS B 188 ? 0.4422 0.6483 0.4894 0.1276  -0.0705 0.0011  188 LYS B NZ  
5675 N N   . GLY B 189 ? 0.2359 0.2642 0.1812 0.0924  -0.0382 -0.0015 189 GLY B N   
5676 C CA  . GLY B 189 ? 0.2269 0.2393 0.1691 0.0815  -0.0329 -0.0063 189 GLY B CA  
5677 C C   . GLY B 189 ? 0.2923 0.2782 0.2235 0.0829  -0.0270 0.0010  189 GLY B C   
5678 O O   . GLY B 189 ? 0.3025 0.2783 0.2311 0.0918  -0.0260 0.0081  189 GLY B O   
5679 N N   . SER B 190 ? 0.2647 0.2395 0.1900 0.0742  -0.0236 -0.0008 190 SER B N   
5680 C CA  . SER B 190 ? 0.2464 0.1973 0.1649 0.0719  -0.0184 0.0044  190 SER B CA  
5681 C C   . SER B 190 ? 0.2865 0.2292 0.2131 0.0666  -0.0146 -0.0019 190 SER B C   
5682 O O   . SER B 190 ? 0.2152 0.1695 0.1513 0.0621  -0.0148 -0.0091 190 SER B O   
5683 C CB  . SER B 190 ? 0.2372 0.1848 0.1466 0.0657  -0.0166 0.0072  190 SER B CB  
5684 O OG  . SER B 190 ? 0.2604 0.2162 0.1596 0.0711  -0.0192 0.0147  190 SER B OG  
5685 N N   . VAL B 191 ? 0.2635 0.1857 0.1859 0.0671  -0.0116 0.0011  191 VAL B N   
5686 C CA  . VAL B 191 ? 0.2549 0.1687 0.1810 0.0624  -0.0082 -0.0044 191 VAL B CA  
5687 C C   . VAL B 191 ? 0.2434 0.1405 0.1631 0.0546  -0.0065 -0.0023 191 VAL B C   
5688 O O   . VAL B 191 ? 0.2766 0.1583 0.1893 0.0557  -0.0068 0.0040  191 VAL B O   
5689 C CB  . VAL B 191 ? 0.2328 0.1398 0.1599 0.0710  -0.0069 -0.0056 191 VAL B CB  
5690 C CG1 . VAL B 191 ? 0.2493 0.1516 0.1782 0.0666  -0.0035 -0.0116 191 VAL B CG1 
5691 C CG2 . VAL B 191 ? 0.2643 0.1916 0.2002 0.0794  -0.0086 -0.0060 191 VAL B CG2 
5692 N N   . SER B 192 ? 0.2191 0.1197 0.1427 0.0467  -0.0048 -0.0066 192 SER B N   
5693 C CA  . SER B 192 ? 0.2348 0.1248 0.1555 0.0387  -0.0036 -0.0052 192 SER B CA  
5694 C C   . SER B 192 ? 0.2940 0.1758 0.2152 0.0368  -0.0027 -0.0101 192 SER B C   
5695 O O   . SER B 192 ? 0.2549 0.1404 0.1783 0.0419  -0.0019 -0.0141 192 SER B O   
5696 C CB  . SER B 192 ? 0.2714 0.1738 0.1957 0.0328  -0.0026 -0.0059 192 SER B CB  
5697 O OG  . SER B 192 ? 0.2649 0.1768 0.1968 0.0316  -0.0020 -0.0121 192 SER B OG  
5698 N N   . THR B 193 ? 0.2201 0.0934 0.1395 0.0293  -0.0029 -0.0095 193 THR B N   
5699 C CA  . THR B 193 ? 0.2243 0.0943 0.1433 0.0266  -0.0030 -0.0146 193 THR B CA  
5700 C C   . THR B 193 ? 0.2394 0.1157 0.1625 0.0178  -0.0031 -0.0133 193 THR B C   
5701 O O   . THR B 193 ? 0.2542 0.1367 0.1805 0.0146  -0.0024 -0.0089 193 THR B O   
5702 C CB  . THR B 193 ? 0.2975 0.1473 0.2082 0.0282  -0.0049 -0.0174 193 THR B CB  
5703 O OG1 . THR B 193 ? 0.2981 0.1485 0.2058 0.0283  -0.0049 -0.0238 193 THR B OG1 
5704 C CG2 . THR B 193 ? 0.3181 0.1539 0.2269 0.0199  -0.0075 -0.0134 193 THR B CG2 
5705 N N   . SER B 194 ? 0.2565 0.1331 0.1792 0.0151  -0.0039 -0.0168 194 SER B N   
5706 C CA  . SER B 194 ? 0.2456 0.1296 0.1730 0.0082  -0.0048 -0.0154 194 SER B CA  
5707 C C   . SER B 194 ? 0.2392 0.1127 0.1613 0.0028  -0.0090 -0.0179 194 SER B C   
5708 O O   . SER B 194 ? 0.2905 0.1510 0.2041 0.0060  -0.0105 -0.0229 194 SER B O   
5709 C CB  . SER B 194 ? 0.2111 0.1075 0.1431 0.0103  -0.0029 -0.0166 194 SER B CB  
5710 O OG  . SER B 194 ? 0.2426 0.1476 0.1811 0.0132  -0.0002 -0.0155 194 SER B OG  
5711 N N   . PRO B 195 ? 0.2438 0.1236 0.1711 -0.0050 -0.0112 -0.0155 195 PRO B N   
5712 C CA  . PRO B 195 ? 0.2484 0.1218 0.1717 -0.0112 -0.0168 -0.0194 195 PRO B CA  
5713 C C   . PRO B 195 ? 0.2530 0.1256 0.1670 -0.0053 -0.0176 -0.0261 195 PRO B C   
5714 O O   . PRO B 195 ? 0.2570 0.1413 0.1729 0.0003  -0.0139 -0.0248 195 PRO B O   
5715 C CB  . PRO B 195 ? 0.2965 0.1869 0.2304 -0.0181 -0.0183 -0.0147 195 PRO B CB  
5716 C CG  . PRO B 195 ? 0.3493 0.2484 0.2914 -0.0169 -0.0130 -0.0080 195 PRO B CG  
5717 C CD  . PRO B 195 ? 0.2747 0.1691 0.2120 -0.0080 -0.0090 -0.0095 195 PRO B CD  
5718 N N   . TYR B 196 ? 0.2947 0.1533 0.1987 -0.0072 -0.0224 -0.0333 196 TYR B N   
5719 C CA  . TYR B 196 ? 0.3356 0.1871 0.2268 0.0015  -0.0216 -0.0410 196 TYR B CA  
5720 C C   . TYR B 196 ? 0.3392 0.2087 0.2289 0.0071  -0.0183 -0.0398 196 TYR B C   
5721 O O   . TYR B 196 ? 0.2845 0.1577 0.1729 0.0155  -0.0127 -0.0393 196 TYR B O   
5722 C CB  . TYR B 196 ? 0.2943 0.1289 0.1739 -0.0023 -0.0286 -0.0508 196 TYR B CB  
5723 C CG  . TYR B 196 ? 0.3088 0.1286 0.1741 0.0084  -0.0270 -0.0600 196 TYR B CG  
5724 C CD1 . TYR B 196 ? 0.3254 0.1568 0.1813 0.0174  -0.0237 -0.0638 196 TYR B CD1 
5725 C CD2 . TYR B 196 ? 0.3310 0.1260 0.1924 0.0103  -0.0280 -0.0638 196 TYR B CD2 
5726 C CE1 . TYR B 196 ? 0.3664 0.1872 0.2093 0.0286  -0.0210 -0.0722 196 TYR B CE1 
5727 C CE2 . TYR B 196 ? 0.3785 0.1693 0.2339 0.0209  -0.0250 -0.0698 196 TYR B CE2 
5728 C CZ  . TYR B 196 ? 0.4154 0.2194 0.2616 0.0300  -0.0214 -0.0744 196 TYR B CZ  
5729 O OH  . TYR B 196 ? 0.3805 0.1821 0.2214 0.0409  -0.0176 -0.0801 196 TYR B OH  
5730 N N   . TYR B 197 ? 0.2705 0.1524 0.1613 0.0025  -0.0218 -0.0384 197 TYR B N   
5731 C CA  . TYR B 197 ? 0.2996 0.1971 0.1880 0.0081  -0.0187 -0.0355 197 TYR B CA  
5732 C C   . TYR B 197 ? 0.2654 0.1773 0.1685 0.0075  -0.0151 -0.0256 197 TYR B C   
5733 O O   . TYR B 197 ? 0.2335 0.1582 0.1373 0.0096  -0.0142 -0.0208 197 TYR B O   
5734 C CB  . TYR B 197 ? 0.3318 0.2342 0.2084 0.0065  -0.0250 -0.0403 197 TYR B CB  
5735 C CG  . TYR B 197 ? 0.3265 0.2139 0.1854 0.0102  -0.0274 -0.0523 197 TYR B CG  
5736 C CD1 . TYR B 197 ? 0.2974 0.1860 0.1460 0.0211  -0.0211 -0.0549 197 TYR B CD1 
5737 C CD2 . TYR B 197 ? 0.3536 0.2251 0.2075 0.0031  -0.0355 -0.0612 197 TYR B CD2 
5738 C CE1 . TYR B 197 ? 0.3395 0.2140 0.1714 0.0267  -0.0224 -0.0669 197 TYR B CE1 
5739 C CE2 . TYR B 197 ? 0.3776 0.2314 0.2148 0.0074  -0.0379 -0.0739 197 TYR B CE2 
5740 C CZ  . TYR B 197 ? 0.3559 0.2113 0.1814 0.0203  -0.0311 -0.0772 197 TYR B CZ  
5741 O OH  . TYR B 197 ? 0.4376 0.2766 0.2475 0.0264  -0.0325 -0.0903 197 TYR B OH  
5742 N N   . HIS B 198 ? 0.2778 0.1872 0.1918 0.0055  -0.0128 -0.0225 198 HIS B N   
5743 C CA  . HIS B 198 ? 0.2174 0.1373 0.1442 0.0061  -0.0091 -0.0155 198 HIS B CA  
5744 C C   . HIS B 198 ? 0.2366 0.1686 0.1694 0.0029  -0.0123 -0.0110 198 HIS B C   
5745 O O   . HIS B 198 ? 0.2361 0.1770 0.1740 0.0064  -0.0100 -0.0057 198 HIS B O   
5746 C CB  . HIS B 198 ? 0.2004 0.1244 0.1284 0.0124  -0.0037 -0.0132 198 HIS B CB  
5747 C CG  . HIS B 198 ? 0.1928 0.1210 0.1338 0.0131  0.0001  -0.0090 198 HIS B CG  
5748 N ND1 . HIS B 198 ? 0.2251 0.1607 0.1742 0.0136  0.0012  -0.0033 198 HIS B ND1 
5749 C CD2 . HIS B 198 ? 0.2337 0.1589 0.1801 0.0140  0.0024  -0.0105 198 HIS B CD2 
5750 C CE1 . HIS B 198 ? 0.2898 0.2245 0.2488 0.0144  0.0041  -0.0027 198 HIS B CE1 
5751 N NE2 . HIS B 198 ? 0.2516 0.1814 0.2087 0.0143  0.0045  -0.0074 198 HIS B NE2 
5752 N N   . PRO B 199 ? 0.2448 0.1780 0.1789 -0.0038 -0.0177 -0.0121 199 PRO B N   
5753 C CA  . PRO B 199 ? 0.2571 0.2059 0.1993 -0.0063 -0.0212 -0.0072 199 PRO B CA  
5754 C C   . PRO B 199 ? 0.2738 0.2306 0.2307 -0.0058 -0.0173 -0.0018 199 PRO B C   
5755 O O   . PRO B 199 ? 0.2584 0.2087 0.2178 -0.0052 -0.0131 -0.0025 199 PRO B O   
5756 C CB  . PRO B 199 ? 0.2521 0.1994 0.1911 -0.0151 -0.0290 -0.0116 199 PRO B CB  
5757 C CG  . PRO B 199 ? 0.2335 0.1644 0.1710 -0.0183 -0.0272 -0.0149 199 PRO B CG  
5758 C CD  . PRO B 199 ? 0.2647 0.1856 0.1950 -0.0099 -0.0212 -0.0169 199 PRO B CD  
5759 N N   . LEU B 200 ? 0.2811 0.2537 0.2473 -0.0050 -0.0191 0.0036  200 LEU B N   
5760 C CA  . LEU B 200 ? 0.2301 0.2132 0.2103 -0.0038 -0.0157 0.0080  200 LEU B CA  
5761 C C   . LEU B 200 ? 0.2538 0.2444 0.2398 -0.0128 -0.0193 0.0084  200 LEU B C   
5762 O O   . LEU B 200 ? 0.2208 0.2270 0.2138 -0.0166 -0.0246 0.0114  200 LEU B O   
5763 C CB  . LEU B 200 ? 0.3053 0.3018 0.2942 0.0030  -0.0153 0.0143  200 LEU B CB  
5764 C CG  . LEU B 200 ? 0.2740 0.2616 0.2609 0.0110  -0.0108 0.0159  200 LEU B CG  
5765 C CD1 . LEU B 200 ? 0.2899 0.2888 0.2842 0.0175  -0.0117 0.0238  200 LEU B CD1 
5766 C CD2 . LEU B 200 ? 0.2811 0.2596 0.2722 0.0142  -0.0044 0.0129  200 LEU B CD2 
5767 N N   . ILE B 201 ? 0.2052 0.1857 0.1891 -0.0166 -0.0167 0.0065  201 ILE B N   
5768 C CA  . ILE B 201 ? 0.2322 0.2174 0.2222 -0.0268 -0.0194 0.0086  201 ILE B CA  
5769 C C   . ILE B 201 ? 0.2293 0.2393 0.2360 -0.0276 -0.0182 0.0154  201 ILE B C   
5770 O O   . ILE B 201 ? 0.2057 0.2272 0.2206 -0.0371 -0.0238 0.0178  201 ILE B O   
5771 C CB  . ILE B 201 ? 0.2371 0.2076 0.2220 -0.0287 -0.0153 0.0080  201 ILE B CB  
5772 C CG1 . ILE B 201 ? 0.2340 0.1816 0.2040 -0.0281 -0.0177 0.0014  201 ILE B CG1 
5773 C CG2 . ILE B 201 ? 0.2077 0.1850 0.2019 -0.0394 -0.0161 0.0137  201 ILE B CG2 
5774 C CD1 . ILE B 201 ? 0.2462 0.1844 0.2111 -0.0368 -0.0258 -0.0030 201 ILE B CD1 
5775 N N   . PRO B 202 ? 0.1934 0.2133 0.2067 -0.0183 -0.0114 0.0183  202 PRO B N   
5776 C CA  . PRO B 202 ? 0.1672 0.2129 0.1972 -0.0179 -0.0097 0.0249  202 PRO B CA  
5777 C C   . PRO B 202 ? 0.1750 0.2377 0.2133 -0.0192 -0.0169 0.0277  202 PRO B C   
5778 O O   . PRO B 202 ? 0.1835 0.2686 0.2365 -0.0250 -0.0191 0.0330  202 PRO B O   
5779 C CB  . PRO B 202 ? 0.1699 0.2177 0.2017 -0.0048 -0.0013 0.0245  202 PRO B CB  
5780 C CG  . PRO B 202 ? 0.2021 0.2271 0.2197 -0.0036 0.0017  0.0188  202 PRO B CG  
5781 C CD  . PRO B 202 ? 0.1926 0.2013 0.1997 -0.0088 -0.0047 0.0153  202 PRO B CD  
5782 N N   . ILE B 203 ? 0.1821 0.2369 0.2119 -0.0143 -0.0208 0.0252  203 ILE B N   
5783 C CA  . ILE B 203 ? 0.2041 0.2762 0.2393 -0.0149 -0.0287 0.0284  203 ILE B CA  
5784 C C   . ILE B 203 ? 0.2325 0.3055 0.2647 -0.0290 -0.0384 0.0250  203 ILE B C   
5785 O O   . ILE B 203 ? 0.1972 0.2929 0.2414 -0.0347 -0.0453 0.0285  203 ILE B O   
5786 C CB  . ILE B 203 ? 0.2330 0.2968 0.2584 -0.0050 -0.0292 0.0286  203 ILE B CB  
5787 C CG1 . ILE B 203 ? 0.2718 0.3370 0.3051 0.0082  -0.0211 0.0328  203 ILE B CG1 
5788 C CG2 . ILE B 203 ? 0.2205 0.3009 0.2462 -0.0064 -0.0389 0.0315  203 ILE B CG2 
5789 C CD1 . ILE B 203 ? 0.3634 0.4163 0.3887 0.0169  -0.0200 0.0345  203 ILE B CD1 
5790 N N   . LEU B 204 ? 0.2186 0.2674 0.2359 -0.0347 -0.0397 0.0177  204 LEU B N   
5791 C CA  . LEU B 204 ? 0.2616 0.3059 0.2751 -0.0481 -0.0493 0.0124  204 LEU B CA  
5792 C C   . LEU B 204 ? 0.2266 0.2844 0.2577 -0.0603 -0.0506 0.0170  204 LEU B C   
5793 O O   . LEU B 204 ? 0.2530 0.3205 0.2904 -0.0721 -0.0604 0.0155  204 LEU B O   
5794 C CB  . LEU B 204 ? 0.2285 0.2419 0.2234 -0.0497 -0.0488 0.0038  204 LEU B CB  
5795 C CG  . LEU B 204 ? 0.2151 0.2153 0.1920 -0.0395 -0.0475 -0.0012 204 LEU B CG  
5796 C CD1 . LEU B 204 ? 0.2634 0.2363 0.2241 -0.0419 -0.0481 -0.0102 204 LEU B CD1 
5797 C CD2 . LEU B 204 ? 0.2591 0.2743 0.2316 -0.0373 -0.0551 -0.0014 204 LEU B CD2 
5798 N N   . LEU B 205 ? 0.2037 0.2637 0.2430 -0.0580 -0.0409 0.0228  205 LEU B N   
5799 C CA  . LEU B 205 ? 0.2109 0.2859 0.2675 -0.0694 -0.0401 0.0295  205 LEU B CA  
5800 C C   . LEU B 205 ? 0.1951 0.3073 0.2729 -0.0680 -0.0409 0.0374  205 LEU B C   
5801 O O   . LEU B 205 ? 0.2073 0.3384 0.3017 -0.0810 -0.0460 0.0418  205 LEU B O   
5802 C CB  . LEU B 205 ? 0.1973 0.2635 0.2526 -0.0663 -0.0289 0.0336  205 LEU B CB  
5803 C CG  . LEU B 205 ? 0.2067 0.2398 0.2458 -0.0700 -0.0285 0.0287  205 LEU B CG  
5804 C CD1 . LEU B 205 ? 0.2133 0.2425 0.2495 -0.0633 -0.0174 0.0335  205 LEU B CD1 
5805 C CD2 . LEU B 205 ? 0.2284 0.2535 0.2724 -0.0876 -0.0361 0.0290  205 LEU B CD2 
5806 N N   . ASN B 206 ? 0.1842 0.3073 0.2631 -0.0525 -0.0361 0.0394  206 ASN B N   
5807 C CA  . ASN B 206 ? 0.1786 0.3370 0.2782 -0.0474 -0.0351 0.0475  206 ASN B CA  
5808 C C   . ASN B 206 ? 0.2096 0.3692 0.3049 -0.0297 -0.0328 0.0476  206 ASN B C   
5809 O O   . ASN B 206 ? 0.1899 0.3440 0.2836 -0.0172 -0.0227 0.0482  206 ASN B O   
5810 C CB  . ASN B 206 ? 0.2190 0.3935 0.3327 -0.0466 -0.0243 0.0547  206 ASN B CB  
5811 C CG  . ASN B 206 ? 0.3306 0.5456 0.4683 -0.0416 -0.0228 0.0634  206 ASN B CG  
5812 O OD1 . ASN B 206 ? 0.2955 0.5263 0.4396 -0.0374 -0.0302 0.0646  206 ASN B OD1 
5813 N ND2 . ASN B 206 ? 0.3959 0.6299 0.5467 -0.0408 -0.0129 0.0702  206 ASN B ND2 
5814 N N   . PRO B 207 ? 0.2039 0.3702 0.2969 -0.0281 -0.0421 0.0474  207 PRO B N   
5815 C CA  . PRO B 207 ? 0.1924 0.3576 0.2814 -0.0113 -0.0398 0.0498  207 PRO B CA  
5816 C C   . PRO B 207 ? 0.1965 0.3839 0.3036 0.0019  -0.0323 0.0573  207 PRO B C   
5817 O O   . PRO B 207 ? 0.2001 0.3783 0.3038 0.0168  -0.0272 0.0586  207 PRO B O   
5818 C CB  . PRO B 207 ? 0.2292 0.4049 0.3142 -0.0141 -0.0524 0.0502  207 PRO B CB  
5819 C CG  . PRO B 207 ? 0.2399 0.4093 0.3189 -0.0322 -0.0611 0.0431  207 PRO B CG  
5820 C CD  . PRO B 207 ? 0.2001 0.3732 0.2922 -0.0417 -0.0557 0.0444  207 PRO B CD  
5821 N N   . ASN B 208 ? 0.1734 0.3895 0.3005 -0.0028 -0.0312 0.0625  208 ASN B N   
5822 C CA  . ASN B 208 ? 0.2047 0.4430 0.3487 0.0118  -0.0226 0.0688  208 ASN B CA  
5823 C C   . ASN B 208 ? 0.2292 0.4469 0.3648 0.0221  -0.0096 0.0644  208 ASN B C   
5824 O O   . ASN B 208 ? 0.2038 0.4320 0.3486 0.0378  -0.0021 0.0668  208 ASN B O   
5825 C CB  . ASN B 208 ? 0.2257 0.5020 0.3936 0.0033  -0.0231 0.0758  208 ASN B CB  
5826 C CG  . ASN B 208 ? 0.2734 0.5770 0.4540 -0.0044 -0.0367 0.0804  208 ASN B CG  
5827 O OD1 . ASN B 208 ? 0.2107 0.5222 0.3921 0.0069  -0.0418 0.0835  208 ASN B OD1 
5828 N ND2 . ASN B 208 ? 0.3524 0.6697 0.5426 -0.0241 -0.0435 0.0810  208 ASN B ND2 
5829 N N   . CYS B 209 ? 0.1719 0.3609 0.2902 0.0145  -0.0074 0.0573  209 CYS B N   
5830 C CA  . CYS B 209 ? 0.2157 0.3871 0.3252 0.0238  0.0033  0.0522  209 CYS B CA  
5831 C C   . CYS B 209 ? 0.2332 0.3881 0.3371 0.0399  0.0059  0.0493  209 CYS B C   
5832 O O   . CYS B 209 ? 0.2120 0.3575 0.3128 0.0503  0.0144  0.0447  209 CYS B O   
5833 C CB  . CYS B 209 ? 0.2065 0.3514 0.2987 0.0130  0.0037  0.0461  209 CYS B CB  
5834 S SG  . CYS B 209 ? 0.2554 0.3665 0.3272 0.0100  -0.0033 0.0393  209 CYS B SG  
5835 N N   . VAL B 210 ? 0.2456 0.3968 0.3481 0.0422  -0.0013 0.0521  210 VAL B N   
5836 C CA  . VAL B 210 ? 0.1683 0.3025 0.2672 0.0566  0.0012  0.0518  210 VAL B CA  
5837 C C   . VAL B 210 ? 0.1734 0.3239 0.2880 0.0730  0.0075  0.0552  210 VAL B C   
5838 O O   . VAL B 210 ? 0.2205 0.3526 0.3329 0.0858  0.0128  0.0520  210 VAL B O   
5839 C CB  . VAL B 210 ? 0.2183 0.3488 0.3123 0.0557  -0.0075 0.0568  210 VAL B CB  
5840 C CG1 . VAL B 210 ? 0.2285 0.3430 0.3057 0.0413  -0.0129 0.0519  210 VAL B CG1 
5841 C CG2 . VAL B 210 ? 0.2802 0.4439 0.3892 0.0571  -0.0144 0.0660  210 VAL B CG2 
5842 N N   . TYR B 211 ? 0.1715 0.3567 0.3032 0.0731  0.0072  0.0614  211 TYR B N   
5843 C CA  . TYR B 211 ? 0.2045 0.4084 0.3522 0.0908  0.0138  0.0649  211 TYR B CA  
5844 C C   . TYR B 211 ? 0.2245 0.4221 0.3691 0.0981  0.0254  0.0567  211 TYR B C   
5845 O O   . TYR B 211 ? 0.2137 0.4186 0.3673 0.1158  0.0323  0.0563  211 TYR B O   
5846 C CB  . TYR B 211 ? 0.1804 0.4284 0.3496 0.0884  0.0100  0.0746  211 TYR B CB  
5847 C CG  . TYR B 211 ? 0.1745 0.4328 0.3462 0.0818  -0.0030 0.0818  211 TYR B CG  
5848 C CD1 . TYR B 211 ? 0.2458 0.4939 0.4150 0.0939  -0.0068 0.0864  211 TYR B CD1 
5849 C CD2 . TYR B 211 ? 0.1778 0.4562 0.3541 0.0633  -0.0118 0.0842  211 TYR B CD2 
5850 C CE1 . TYR B 211 ? 0.2618 0.5221 0.4310 0.0890  -0.0189 0.0934  211 TYR B CE1 
5851 C CE2 . TYR B 211 ? 0.1721 0.4613 0.3487 0.0576  -0.0247 0.0889  211 TYR B CE2 
5852 C CZ  . TYR B 211 ? 0.2258 0.5070 0.3977 0.0710  -0.0281 0.0936  211 TYR B CZ  
5853 O OH  . TYR B 211 ? 0.2978 0.5915 0.4673 0.0663  -0.0410 0.0986  211 TYR B OH  
5854 N N   . GLU B 212 ? 0.2056 0.3893 0.3365 0.0864  0.0277  0.0500  212 GLU B N   
5855 C CA  . GLU B 212 ? 0.2443 0.4247 0.3699 0.0937  0.0382  0.0423  212 GLU B CA  
5856 C C   . GLU B 212 ? 0.2644 0.4151 0.3810 0.1085  0.0419  0.0328  212 GLU B C   
5857 O O   . GLU B 212 ? 0.3398 0.4938 0.4574 0.1223  0.0505  0.0267  212 GLU B O   
5858 C CB  . GLU B 212 ? 0.1974 0.3693 0.3094 0.0782  0.0388  0.0388  212 GLU B CB  
5859 C CG  . GLU B 212 ? 0.2114 0.4125 0.3342 0.0644  0.0375  0.0478  212 GLU B CG  
5860 C CD  . GLU B 212 ? 0.3559 0.5433 0.4650 0.0490  0.0370  0.0459  212 GLU B CD  
5861 O OE1 . GLU B 212 ? 0.4094 0.6001 0.5213 0.0329  0.0300  0.0510  212 GLU B OE1 
5862 O OE2 . GLU B 212 ? 0.3447 0.5175 0.4400 0.0536  0.0432  0.0389  212 GLU B OE2 
5863 N N   . THR B 213 ? 0.2618 0.3839 0.3700 0.1057  0.0358  0.0313  213 THR B N   
5864 C CA  . THR B 213 ? 0.3161 0.4082 0.4188 0.1173  0.0381  0.0238  213 THR B CA  
5865 C C   . THR B 213 ? 0.3505 0.4381 0.4636 0.1281  0.0348  0.0315  213 THR B C   
5866 O O   . THR B 213 ? 0.4065 0.4769 0.5220 0.1427  0.0387  0.0269  213 THR B O   
5867 C CB  . THR B 213 ? 0.3075 0.3685 0.3936 0.1062  0.0348  0.0168  213 THR B CB  
5868 O OG1 . THR B 213 ? 0.3493 0.4102 0.4329 0.0933  0.0270  0.0245  213 THR B OG1 
5869 C CG2 . THR B 213 ? 0.2498 0.3112 0.3245 0.0999  0.0387  0.0081  213 THR B CG2 
5870 N N   . THR B 214 ? 0.2527 0.3543 0.3713 0.1217  0.0274  0.0430  214 THR B N   
5871 C CA  . THR B 214 ? 0.3065 0.4077 0.4343 0.1322  0.0236  0.0532  214 THR B CA  
5872 C C   . THR B 214 ? 0.3494 0.4910 0.4930 0.1340  0.0199  0.0642  214 THR B C   
5873 O O   . THR B 214 ? 0.3105 0.4642 0.4535 0.1241  0.0111  0.0721  214 THR B O   
5874 C CB  . THR B 214 ? 0.3099 0.3887 0.4266 0.1232  0.0170  0.0573  214 THR B CB  
5875 O OG1 . THR B 214 ? 0.2802 0.3711 0.3893 0.1060  0.0109  0.0586  214 THR B OG1 
5876 C CG2 . THR B 214 ? 0.3536 0.3951 0.4588 0.1216  0.0207  0.0474  214 THR B CG2 
5877 N N   . PRO B 215 ? 0.3228 0.4878 0.4811 0.1471  0.0261  0.0647  215 PRO B N   
5878 C CA  . PRO B 215 ? 0.2693 0.4786 0.4457 0.1472  0.0226  0.0751  215 PRO B CA  
5879 C C   . PRO B 215 ? 0.3248 0.5399 0.5067 0.1512  0.0141  0.0860  215 PRO B C   
5880 O O   . PRO B 215 ? 0.2880 0.5370 0.4810 0.1456  0.0077  0.0938  215 PRO B O   
5881 C CB  . PRO B 215 ? 0.2800 0.5013 0.4634 0.1575  0.0322  0.0693  215 PRO B CB  
5882 C CG  . PRO B 215 ? 0.3368 0.5188 0.5091 0.1693  0.0379  0.0584  215 PRO B CG  
5883 C CD  . PRO B 215 ? 0.2948 0.4464 0.4521 0.1609  0.0359  0.0541  215 PRO B CD  
5884 N N   . ASN B 216 ? 0.3162 0.4998 0.4904 0.1595  0.0134  0.0868  216 ASN B N   
5885 C CA  . ASN B 216 ? 0.3552 0.5432 0.5327 0.1643  0.0061  0.0980  216 ASN B CA  
5886 C C   . ASN B 216 ? 0.3213 0.4981 0.4867 0.1550  -0.0021 0.1047  216 ASN B C   
5887 O O   . ASN B 216 ? 0.3384 0.5146 0.5023 0.1588  -0.0077 0.1142  216 ASN B O   
5888 C CB  . ASN B 216 ? 0.4735 0.6363 0.6522 0.1802  0.0108  0.0966  216 ASN B CB  
5889 C CG  . ASN B 216 ? 0.4867 0.6641 0.6772 0.1914  0.0179  0.0908  216 ASN B CG  
5890 O OD1 . ASN B 216 ? 0.5506 0.7035 0.7383 0.2001  0.0249  0.0804  216 ASN B OD1 
5891 N ND2 . ASN B 216 ? 0.5087 0.7268 0.7124 0.1906  0.0158  0.0967  216 ASN B ND2 
5892 N N   . VAL B 217 ? 0.2976 0.4662 0.4535 0.1433  -0.0027 0.1001  217 VAL B N   
5893 C CA  . VAL B 217 ? 0.2971 0.4524 0.4368 0.1317  -0.0100 0.1033  217 VAL B CA  
5894 C C   . VAL B 217 ? 0.2930 0.4835 0.4362 0.1252  -0.0212 0.1117  217 VAL B C   
5895 O O   . VAL B 217 ? 0.2945 0.5171 0.4503 0.1209  -0.0237 0.1110  217 VAL B O   
5896 C CB  . VAL B 217 ? 0.2701 0.4024 0.3928 0.1153  -0.0077 0.0907  217 VAL B CB  
5897 C CG1 . VAL B 217 ? 0.2875 0.4424 0.4111 0.1006  -0.0106 0.0848  217 VAL B CG1 
5898 C CG2 . VAL B 217 ? 0.3232 0.4354 0.4289 0.1079  -0.0120 0.0935  217 VAL B CG2 
5899 N N   . LYS B 218 ? 0.2449 0.4311 0.3773 0.1245  -0.0282 0.1200  218 LYS B N   
5900 C CA  . LYS B 218 ? 0.2290 0.4454 0.3594 0.1167  -0.0405 0.1255  218 LYS B CA  
5901 C C   . LYS B 218 ? 0.3203 0.5225 0.4288 0.0985  -0.0447 0.1167  218 LYS B C   
5902 O O   . LYS B 218 ? 0.3117 0.4858 0.4042 0.0980  -0.0416 0.1165  218 LYS B O   
5903 C CB  . LYS B 218 ? 0.2707 0.4882 0.3974 0.1255  -0.0442 0.1363  218 LYS B CB  
5904 C CG  . LYS B 218 ? 0.3363 0.5605 0.4799 0.1399  -0.0394 0.1403  218 LYS B CG  
5905 C CD  . LYS B 218 ? 0.4442 0.6720 0.5847 0.1481  -0.0441 0.1520  218 LYS B CD  
5906 C CE  . LYS B 218 ? 0.4916 0.7220 0.6483 0.1637  -0.0390 0.1559  218 LYS B CE  
5907 N NZ  . LYS B 218 ? 0.5798 0.8179 0.7346 0.1717  -0.0447 0.1685  218 LYS B NZ  
5908 N N   . ILE B 219 ? 0.2385 0.4598 0.3478 0.0835  -0.0511 0.1093  219 ILE B N   
5909 C CA  . ILE B 219 ? 0.2671 0.4755 0.3561 0.0672  -0.0559 0.0998  219 ILE B CA  
5910 C C   . ILE B 219 ? 0.3205 0.5589 0.4082 0.0587  -0.0703 0.1009  219 ILE B C   
5911 O O   . ILE B 219 ? 0.3116 0.5832 0.4174 0.0633  -0.0761 0.1084  219 ILE B O   
5912 C CB  . ILE B 219 ? 0.2886 0.4821 0.3768 0.0552  -0.0498 0.0870  219 ILE B CB  
5913 C CG1 . ILE B 219 ? 0.3165 0.5397 0.4226 0.0466  -0.0537 0.0854  219 ILE B CG1 
5914 C CG2 . ILE B 219 ? 0.3243 0.4931 0.4151 0.0644  -0.0369 0.0850  219 ILE B CG2 
5915 C CD1 . ILE B 219 ? 0.3574 0.5674 0.4617 0.0339  -0.0483 0.0752  219 ILE B CD1 
5916 N N   . PRO B 220 ? 0.2772 0.5064 0.3441 0.0472  -0.0769 0.0934  220 PRO B N   
5917 C CA  . PRO B 220 ? 0.2852 0.5417 0.3491 0.0383  -0.0921 0.0918  220 PRO B CA  
5918 C C   . PRO B 220 ? 0.2598 0.5353 0.3409 0.0237  -0.0971 0.0848  220 PRO B C   
5919 O O   . PRO B 220 ? 0.2717 0.5392 0.3647 0.0201  -0.0882 0.0814  220 PRO B O   
5920 C CB  . PRO B 220 ? 0.3485 0.5835 0.3833 0.0309  -0.0954 0.0827  220 PRO B CB  
5921 C CG  . PRO B 220 ? 0.3492 0.5483 0.3760 0.0319  -0.0821 0.0781  220 PRO B CG  
5922 C CD  . PRO B 220 ? 0.3150 0.5104 0.3593 0.0451  -0.0713 0.0876  220 PRO B CD  
5923 N N   . ASP B 221 ? 0.2579 0.5600 0.3397 0.0147  -0.1121 0.0830  221 ASP B N   
5924 C CA  . ASP B 221 ? 0.3435 0.6657 0.4421 -0.0024 -0.1196 0.0767  221 ASP B CA  
5925 C C   . ASP B 221 ? 0.2753 0.5684 0.3562 -0.0195 -0.1214 0.0611  221 ASP B C   
5926 O O   . ASP B 221 ? 0.2988 0.5849 0.3582 -0.0251 -0.1312 0.0528  221 ASP B O   
5927 C CB  . ASP B 221 ? 0.3715 0.7253 0.4768 -0.0049 -0.1331 0.0785  221 ASP B CB  
5928 C CG  . ASP B 221 ? 0.4756 0.8475 0.6003 -0.0234 -0.1399 0.0721  221 ASP B CG  
5929 O OD1 . ASP B 221 ? 0.5338 0.8906 0.6551 -0.0402 -0.1417 0.0619  221 ASP B OD1 
5930 O OD2 . ASP B 221 ? 0.4877 0.8879 0.6312 -0.0213 -0.1433 0.0777  221 ASP B OD2 
5931 N N   . PHE B 222 ? 0.2296 0.5059 0.3186 -0.0267 -0.1117 0.0571  222 PHE B N   
5932 C CA  . PHE B 222 ? 0.2502 0.4979 0.3253 -0.0422 -0.1127 0.0437  222 PHE B CA  
5933 C C   . PHE B 222 ? 0.3086 0.5766 0.3981 -0.0618 -0.1257 0.0388  222 PHE B C   
5934 O O   . PHE B 222 ? 0.4143 0.6885 0.5237 -0.0722 -0.1221 0.0406  222 PHE B O   
5935 C CB  . PHE B 222 ? 0.2664 0.4887 0.3436 -0.0408 -0.0974 0.0432  222 PHE B CB  
5936 C CG  . PHE B 222 ? 0.2714 0.4654 0.3300 -0.0270 -0.0870 0.0430  222 PHE B CG  
5937 C CD1 . PHE B 222 ? 0.2425 0.4428 0.3065 -0.0098 -0.0797 0.0531  222 PHE B CD1 
5938 C CD2 . PHE B 222 ? 0.2338 0.3945 0.2714 -0.0312 -0.0843 0.0331  222 PHE B CD2 
5939 C CE1 . PHE B 222 ? 0.2280 0.4017 0.2774 0.0008  -0.0706 0.0533  222 PHE B CE1 
5940 C CE2 . PHE B 222 ? 0.2458 0.3837 0.2692 -0.0198 -0.0749 0.0336  222 PHE B CE2 
5941 C CZ  . PHE B 222 ? 0.2420 0.3863 0.2717 -0.0048 -0.0683 0.0437  222 PHE B CZ  
5942 N N   . ALA B 223 ? 0.3499 0.6288 0.4286 -0.0675 -0.1413 0.0326  223 ALA B N   
5943 C CA  . ALA B 223 ? 0.4175 0.7139 0.5090 -0.0864 -0.1554 0.0261  223 ALA B CA  
5944 C C   . ALA B 223 ? 0.4462 0.7092 0.5227 -0.1034 -0.1601 0.0099  223 ALA B C   
5945 O O   . ALA B 223 ? 0.4308 0.6946 0.5107 -0.1163 -0.1704 0.0002  223 ALA B O   
5946 C CB  . ALA B 223 ? 0.4708 0.7878 0.5569 -0.0806 -0.1668 0.0248  223 ALA B CB  
5947 N N   . VAL B 224 ? 0.4083 0.6339 0.4672 -0.0995 -0.1492 0.0056  224 VAL B N   
5948 C CA  . VAL B 224 ? 0.3828 0.5729 0.4290 -0.1131 -0.1512 -0.0082 224 VAL B CA  
5949 C C   . VAL B 224 ? 0.3589 0.5255 0.4102 -0.1104 -0.1343 -0.0029 224 VAL B C   
5950 O O   . VAL B 224 ? 0.3264 0.4955 0.3796 -0.0950 -0.1215 0.0067  224 VAL B O   
5951 C CB  . VAL B 224 ? 0.4991 0.6642 0.5102 -0.1076 -0.1562 -0.0222 224 VAL B CB  
5952 C CG1 . VAL B 224 ? 0.5369 0.6820 0.5310 -0.0887 -0.1409 -0.0179 224 VAL B CG1 
5953 C CG2 . VAL B 224 ? 0.5205 0.6541 0.5208 -0.1235 -0.1633 -0.0389 224 VAL B CG2 
5954 N N   . SER B 225 ? 0.3726 0.5164 0.4264 -0.1256 -0.1348 -0.0091 225 SER B N   
5955 C CA  . SER B 225 ? 0.3543 0.4776 0.4124 -0.1240 -0.1200 -0.0035 225 SER B CA  
5956 C C   . SER B 225 ? 0.2884 0.3722 0.3186 -0.1145 -0.1134 -0.0121 225 SER B C   
5957 O O   . SER B 225 ? 0.3551 0.4167 0.3664 -0.1190 -0.1215 -0.0256 225 SER B O   
5958 C CB  . SER B 225 ? 0.3432 0.4623 0.4196 -0.1445 -0.1227 -0.0024 225 SER B CB  
5959 O OG  . SER B 225 ? 0.3499 0.4459 0.4250 -0.1419 -0.1089 0.0026  225 SER B OG  
5960 N N   . PHE B 226 ? 0.2688 0.3450 0.2970 -0.1013 -0.0989 -0.0050 226 PHE B N   
5961 C CA  . PHE B 226 ? 0.2694 0.3118 0.2759 -0.0926 -0.0914 -0.0112 226 PHE B CA  
5962 C C   . PHE B 226 ? 0.2669 0.2898 0.2788 -0.0974 -0.0827 -0.0080 226 PHE B C   
5963 O O   . PHE B 226 ? 0.2758 0.2745 0.2734 -0.0891 -0.0752 -0.0107 226 PHE B O   
5964 C CB  . PHE B 226 ? 0.2521 0.2990 0.2505 -0.0740 -0.0825 -0.0064 226 PHE B CB  
5965 C CG  . PHE B 226 ? 0.2592 0.3169 0.2445 -0.0670 -0.0897 -0.0095 226 PHE B CG  
5966 C CD1 . PHE B 226 ? 0.3344 0.3721 0.2951 -0.0638 -0.0926 -0.0203 226 PHE B CD1 
5967 C CD2 . PHE B 226 ? 0.3545 0.4435 0.3515 -0.0621 -0.0929 -0.0008 226 PHE B CD2 
5968 C CE1 . PHE B 226 ? 0.3812 0.4308 0.3278 -0.0566 -0.0984 -0.0220 226 PHE B CE1 
5969 C CE2 . PHE B 226 ? 0.3742 0.4741 0.3580 -0.0550 -0.0994 -0.0017 226 PHE B CE2 
5970 C CZ  . PHE B 226 ? 0.3790 0.4597 0.3369 -0.0525 -0.1021 -0.0121 226 PHE B CZ  
5971 N N   . ARG B 227 ? 0.3123 0.3470 0.3449 -0.1106 -0.0837 -0.0012 227 ARG B N   
5972 C CA  . ARG B 227 ? 0.2666 0.2874 0.3048 -0.1138 -0.0742 0.0053  227 ARG B CA  
5973 C C   . ARG B 227 ? 0.3142 0.2959 0.3367 -0.1190 -0.0764 -0.0035 227 ARG B C   
5974 O O   . ARG B 227 ? 0.3366 0.2990 0.3512 -0.1122 -0.0673 -0.0011 227 ARG B O   
5975 C CB  . ARG B 227 ? 0.2668 0.3124 0.3317 -0.1275 -0.0743 0.0163  227 ARG B CB  
5976 C CG  . ARG B 227 ? 0.2983 0.3837 0.3803 -0.1193 -0.0696 0.0260  227 ARG B CG  
5977 C CD  . ARG B 227 ? 0.3101 0.4242 0.4200 -0.1327 -0.0691 0.0374  227 ARG B CD  
5978 N NE  . ARG B 227 ? 0.4158 0.5172 0.5287 -0.1372 -0.0591 0.0451  227 ARG B NE  
5979 C CZ  . ARG B 227 ? 0.4490 0.5587 0.5627 -0.1252 -0.0453 0.0532  227 ARG B CZ  
5980 N NH1 . ARG B 227 ? 0.3964 0.5243 0.5097 -0.1083 -0.0400 0.0537  227 ARG B NH1 
5981 N NH2 . ARG B 227 ? 0.5201 0.6190 0.6344 -0.1297 -0.0371 0.0607  227 ARG B NH2 
5982 N N   . GLU B 228 ? 0.3111 0.2805 0.3285 -0.1303 -0.0890 -0.0142 228 GLU B N   
5983 C CA  . GLU B 228 ? 0.3346 0.2639 0.3362 -0.1333 -0.0914 -0.0240 228 GLU B CA  
5984 C C   . GLU B 228 ? 0.3615 0.2729 0.3392 -0.1150 -0.0855 -0.0312 228 GLU B C   
5985 O O   . GLU B 228 ? 0.3622 0.2463 0.3304 -0.1103 -0.0797 -0.0322 228 GLU B O   
5986 C CB  . GLU B 228 ? 0.4359 0.3550 0.4353 -0.1481 -0.1070 -0.0368 228 GLU B CB  
5987 C CG  . GLU B 228 ? 0.6145 0.4922 0.5987 -0.1469 -0.1071 -0.0481 228 GLU B CG  
5988 C CD  . GLU B 228 ? 0.8053 0.6631 0.7968 -0.1487 -0.0974 -0.0374 228 GLU B CD  
5989 O OE1 . GLU B 228 ? 0.8672 0.6995 0.8427 -0.1366 -0.0908 -0.0401 228 GLU B OE1 
5990 O OE2 . GLU B 228 ? 0.8832 0.7532 0.8965 -0.1612 -0.0958 -0.0255 228 GLU B OE2 
5991 N N   . ASP B 229 ? 0.3184 0.2466 0.2872 -0.1044 -0.0867 -0.0347 229 ASP B N   
5992 C CA  . ASP B 229 ? 0.3125 0.2283 0.2613 -0.0878 -0.0802 -0.0396 229 ASP B CA  
5993 C C   . ASP B 229 ? 0.3185 0.2321 0.2711 -0.0782 -0.0670 -0.0299 229 ASP B C   
5994 O O   . ASP B 229 ? 0.3136 0.2073 0.2531 -0.0690 -0.0616 -0.0336 229 ASP B O   
5995 C CB  . ASP B 229 ? 0.3108 0.2488 0.2527 -0.0793 -0.0829 -0.0411 229 ASP B CB  
5996 C CG  . ASP B 229 ? 0.3886 0.3227 0.3160 -0.0839 -0.0956 -0.0547 229 ASP B CG  
5997 O OD1 . ASP B 229 ? 0.3855 0.2961 0.3079 -0.0935 -0.1022 -0.0648 229 ASP B OD1 
5998 O OD2 . ASP B 229 ? 0.3847 0.3381 0.3048 -0.0775 -0.0991 -0.0554 229 ASP B OD2 
5999 N N   . ALA B 230 ? 0.3368 0.2724 0.3072 -0.0796 -0.0618 -0.0180 230 ALA B N   
6000 C CA  . ALA B 230 ? 0.3097 0.2439 0.2825 -0.0709 -0.0503 -0.0103 230 ALA B CA  
6001 C C   . ALA B 230 ? 0.3220 0.2306 0.2911 -0.0746 -0.0477 -0.0099 230 ALA B C   
6002 O O   . ALA B 230 ? 0.2998 0.1953 0.2596 -0.0647 -0.0411 -0.0102 230 ALA B O   
6003 C CB  . ALA B 230 ? 0.2765 0.2389 0.2683 -0.0718 -0.0456 0.0009  230 ALA B CB  
6004 N N   . SER B 231 ? 0.3115 0.2131 0.2889 -0.0891 -0.0530 -0.0084 231 SER B N   
6005 C CA  . SER B 231 ? 0.3033 0.1769 0.2768 -0.0929 -0.0514 -0.0070 231 SER B CA  
6006 C C   . SER B 231 ? 0.3186 0.1628 0.2720 -0.0848 -0.0538 -0.0193 231 SER B C   
6007 O O   . SER B 231 ? 0.3928 0.2187 0.3387 -0.0772 -0.0483 -0.0175 231 SER B O   
6008 C CB  . SER B 231 ? 0.3646 0.2335 0.3517 -0.1119 -0.0582 -0.0036 231 SER B CB  
6009 O OG  . SER B 231 ? 0.5112 0.4001 0.5158 -0.1177 -0.0517 0.0116  231 SER B OG  
6010 N N   . LYS B 232 ? 0.3364 0.1774 0.2805 -0.0856 -0.0621 -0.0317 232 LYS B N   
6011 C CA  . LYS B 232 ? 0.3479 0.1632 0.2720 -0.0768 -0.0640 -0.0445 232 LYS B CA  
6012 C C   . LYS B 232 ? 0.3638 0.1827 0.2788 -0.0594 -0.0544 -0.0431 232 LYS B C   
6013 O O   . LYS B 232 ? 0.3957 0.1930 0.3002 -0.0509 -0.0513 -0.0470 232 LYS B O   
6014 C CB  . LYS B 232 ? 0.3815 0.1994 0.2955 -0.0794 -0.0740 -0.0580 232 LYS B CB  
6015 C CG  . LYS B 232 ? 0.5598 0.3634 0.4772 -0.0936 -0.0843 -0.0659 232 LYS B CG  
6016 C CD  . LYS B 232 ? 0.5107 0.3249 0.4175 -0.0930 -0.0930 -0.0794 232 LYS B CD  
6017 C CE  . LYS B 232 ? 0.7315 0.5299 0.6382 -0.0993 -0.0987 -0.0914 232 LYS B CE  
6018 N NZ  . LYS B 232 ? 0.8558 0.6589 0.7844 -0.1181 -0.1045 -0.0860 232 LYS B NZ  
6019 N N   . HIS B 233 ? 0.3033 0.1492 0.2233 -0.0539 -0.0501 -0.0376 233 HIS B N   
6020 C CA  . HIS B 233 ? 0.2863 0.1364 0.2009 -0.0398 -0.0416 -0.0356 233 HIS B CA  
6021 C C   . HIS B 233 ? 0.3328 0.1716 0.2503 -0.0366 -0.0353 -0.0293 233 HIS B C   
6022 O O   . HIS B 233 ? 0.3071 0.1357 0.2161 -0.0262 -0.0313 -0.0318 233 HIS B O   
6023 C CB  . HIS B 233 ? 0.2840 0.1616 0.2071 -0.0364 -0.0380 -0.0289 233 HIS B CB  
6024 C CG  . HIS B 233 ? 0.2964 0.1860 0.2128 -0.0335 -0.0418 -0.0336 233 HIS B CG  
6025 N ND1 . HIS B 233 ? 0.3218 0.2104 0.2262 -0.0227 -0.0384 -0.0373 233 HIS B ND1 
6026 C CD2 . HIS B 233 ? 0.2777 0.1830 0.1979 -0.0395 -0.0486 -0.0336 233 HIS B CD2 
6027 C CE1 . HIS B 233 ? 0.3219 0.2242 0.2215 -0.0221 -0.0425 -0.0389 233 HIS B CE1 
6028 N NE2 . HIS B 233 ? 0.3051 0.2177 0.2139 -0.0318 -0.0493 -0.0370 233 HIS B NE2 
6029 N N   . VAL B 234 ? 0.3180 0.1612 0.2477 -0.0450 -0.0343 -0.0200 234 VAL B N   
6030 C CA  . VAL B 234 ? 0.3313 0.1674 0.2625 -0.0414 -0.0284 -0.0123 234 VAL B CA  
6031 C C   . VAL B 234 ? 0.3675 0.1731 0.2906 -0.0416 -0.0309 -0.0152 234 VAL B C   
6032 O O   . VAL B 234 ? 0.3455 0.1406 0.2620 -0.0315 -0.0270 -0.0143 234 VAL B O   
6033 C CB  . VAL B 234 ? 0.3300 0.1826 0.2753 -0.0494 -0.0255 -0.0006 234 VAL B CB  
6034 C CG1 . VAL B 234 ? 0.2943 0.1406 0.2383 -0.0452 -0.0196 0.0081  234 VAL B CG1 
6035 C CG2 . VAL B 234 ? 0.2884 0.1694 0.2413 -0.0462 -0.0224 0.0014  234 VAL B CG2 
6036 N N   . GLU B 235 ? 0.3277 0.1181 0.2518 -0.0529 -0.0380 -0.0191 235 GLU B N   
6037 C CA  . GLU B 235 ? 0.3591 0.1159 0.2765 -0.0536 -0.0408 -0.0219 235 GLU B CA  
6038 C C   . GLU B 235 ? 0.3742 0.1197 0.2775 -0.0388 -0.0400 -0.0337 235 GLU B C   
6039 O O   . GLU B 235 ? 0.3826 0.1161 0.2836 -0.0294 -0.0361 -0.0319 235 GLU B O   
6040 C CB  . GLU B 235 ? 0.4243 0.1724 0.3496 -0.0694 -0.0486 -0.0247 235 GLU B CB  
6041 C CG  . GLU B 235 ? 0.6158 0.3397 0.5428 -0.0692 -0.0485 -0.0255 235 GLU B CG  
6042 C CD  . GLU B 235 ? 0.7108 0.4273 0.6424 -0.0668 -0.0419 -0.0103 235 GLU B CD  
6043 O OE1 . GLU B 235 ? 0.6834 0.4146 0.6222 -0.0731 -0.0388 0.0029  235 GLU B OE1 
6044 O OE2 . GLU B 235 ? 0.7428 0.4402 0.6706 -0.0580 -0.0397 -0.0110 235 GLU B OE2 
6045 N N   . LEU B 236 ? 0.3915 0.1464 0.2870 -0.0356 -0.0427 -0.0444 236 LEU B N   
6046 C CA  . LEU B 236 ? 0.4074 0.1592 0.2917 -0.0212 -0.0402 -0.0541 236 LEU B CA  
6047 C C   . LEU B 236 ? 0.3645 0.1237 0.2467 -0.0077 -0.0324 -0.0491 236 LEU B C   
6048 O O   . LEU B 236 ? 0.3574 0.1114 0.2353 0.0039  -0.0289 -0.0525 236 LEU B O   
6049 C CB  . LEU B 236 ? 0.3669 0.1300 0.2422 -0.0210 -0.0442 -0.0647 236 LEU B CB  
6050 C CG  . LEU B 236 ? 0.3898 0.1467 0.2655 -0.0324 -0.0530 -0.0730 236 LEU B CG  
6051 C CD1 . LEU B 236 ? 0.4526 0.2266 0.3189 -0.0327 -0.0578 -0.0807 236 LEU B CD1 
6052 C CD2 . LEU B 236 ? 0.4873 0.2234 0.3590 -0.0281 -0.0533 -0.0816 236 LEU B CD2 
6053 N N   . ALA B 237 ? 0.3237 0.1008 0.2122 -0.0091 -0.0291 -0.0408 237 ALA B N   
6054 C CA  . ALA B 237 ? 0.3161 0.1045 0.2066 0.0018  -0.0222 -0.0354 237 ALA B CA  
6055 C C   . ALA B 237 ? 0.3582 0.1302 0.2491 0.0056  -0.0206 -0.0292 237 ALA B C   
6056 O O   . ALA B 237 ? 0.3429 0.1131 0.2301 0.0178  -0.0173 -0.0298 237 ALA B O   
6057 C CB  . ALA B 237 ? 0.3244 0.1391 0.2258 -0.0016 -0.0189 -0.0277 237 ALA B CB  
6058 N N   . LYS B 238 ? 0.3400 0.1020 0.2363 -0.0046 -0.0228 -0.0219 238 LYS B N   
6059 C CA  . LYS B 238 ? 0.4188 0.1635 0.3146 -0.0012 -0.0215 -0.0139 238 LYS B CA  
6060 C C   . LYS B 238 ? 0.3722 0.1034 0.2650 0.0076  -0.0221 -0.0210 238 LYS B C   
6061 O O   . LYS B 238 ? 0.4080 0.1364 0.2996 0.0189  -0.0192 -0.0173 238 LYS B O   
6062 C CB  . LYS B 238 ? 0.3925 0.1299 0.2961 -0.0155 -0.0234 -0.0038 238 LYS B CB  
6063 C CG  . LYS B 238 ? 0.4109 0.1772 0.3241 -0.0209 -0.0194 0.0064  238 LYS B CG  
6064 C CD  . LYS B 238 ? 0.4271 0.1911 0.3498 -0.0360 -0.0205 0.0165  238 LYS B CD  
6065 C CE  . LYS B 238 ? 0.4828 0.2220 0.4041 -0.0369 -0.0202 0.0268  238 LYS B CE  
6066 N NZ  . LYS B 238 ? 0.5402 0.2749 0.4727 -0.0543 -0.0219 0.0363  238 LYS B NZ  
6067 N N   . GLU B 239 ? 0.3978 0.1217 0.2886 0.0034  -0.0259 -0.0316 239 GLU B N   
6068 C CA  . GLU B 239 ? 0.4332 0.1428 0.3200 0.0120  -0.0261 -0.0398 239 GLU B CA  
6069 C C   . GLU B 239 ? 0.4357 0.1579 0.3164 0.0276  -0.0217 -0.0449 239 GLU B C   
6070 O O   . GLU B 239 ? 0.4676 0.1823 0.3474 0.0387  -0.0193 -0.0451 239 GLU B O   
6071 C CB  . GLU B 239 ? 0.4684 0.1686 0.3530 0.0035  -0.0316 -0.0513 239 GLU B CB  
6072 C CG  . GLU B 239 ? 0.6638 0.3528 0.5574 -0.0134 -0.0363 -0.0463 239 GLU B CG  
6073 C CD  . GLU B 239 ? 0.8664 0.5494 0.7583 -0.0228 -0.0430 -0.0588 239 GLU B CD  
6074 O OE1 . GLU B 239 ? 0.9107 0.5885 0.8119 -0.0382 -0.0475 -0.0555 239 GLU B OE1 
6075 O OE2 . GLU B 239 ? 0.9041 0.5891 0.7856 -0.0151 -0.0437 -0.0717 239 GLU B OE2 
6076 N N   . LYS B 240 ? 0.4128 0.1547 0.2904 0.0285  -0.0204 -0.0484 240 LYS B N   
6077 C CA  . LYS B 240 ? 0.4458 0.2021 0.3197 0.0420  -0.0155 -0.0519 240 LYS B CA  
6078 C C   . LYS B 240 ? 0.3926 0.1564 0.2718 0.0504  -0.0116 -0.0429 240 LYS B C   
6079 O O   . LYS B 240 ? 0.4069 0.1736 0.2857 0.0627  -0.0085 -0.0442 240 LYS B O   
6080 C CB  . LYS B 240 ? 0.4086 0.1839 0.2793 0.0402  -0.0146 -0.0554 240 LYS B CB  
6081 C CG  . LYS B 240 ? 0.4775 0.2688 0.3454 0.0528  -0.0089 -0.0582 240 LYS B CG  
6082 C CD  . LYS B 240 ? 0.4670 0.2516 0.3264 0.0599  -0.0086 -0.0681 240 LYS B CD  
6083 C CE  . LYS B 240 ? 0.4458 0.2461 0.3043 0.0740  -0.0018 -0.0690 240 LYS B CE  
6084 N NZ  . LYS B 240 ? 0.4719 0.2679 0.3200 0.0807  -0.0010 -0.0796 240 LYS B NZ  
6085 N N   . TYR B 241 ? 0.3978 0.1659 0.2816 0.0445  -0.0118 -0.0340 241 TYR B N   
6086 C CA  . TYR B 241 ? 0.3792 0.1537 0.2664 0.0524  -0.0093 -0.0257 241 TYR B CA  
6087 C C   . TYR B 241 ? 0.4358 0.1942 0.3231 0.0591  -0.0099 -0.0217 241 TYR B C   
6088 O O   . TYR B 241 ? 0.3781 0.1432 0.2667 0.0714  -0.0078 -0.0195 241 TYR B O   
6089 C CB  . TYR B 241 ? 0.3894 0.1692 0.2795 0.0440  -0.0098 -0.0173 241 TYR B CB  
6090 C CG  . TYR B 241 ? 0.3689 0.1638 0.2638 0.0500  -0.0079 -0.0087 241 TYR B CG  
6091 C CD1 . TYR B 241 ? 0.4101 0.1923 0.3030 0.0534  -0.0089 0.0006  241 TYR B CD1 
6092 C CD2 . TYR B 241 ? 0.3191 0.1408 0.2202 0.0518  -0.0058 -0.0095 241 TYR B CD2 
6093 C CE1 . TYR B 241 ? 0.3927 0.1910 0.2880 0.0593  -0.0081 0.0083  241 TYR B CE1 
6094 C CE2 . TYR B 241 ? 0.3067 0.1431 0.2115 0.0564  -0.0056 -0.0034 241 TYR B CE2 
6095 C CZ  . TYR B 241 ? 0.3315 0.1575 0.2325 0.0607  -0.0070 0.0053  241 TYR B CZ  
6096 O OH  . TYR B 241 ? 0.3380 0.1805 0.2406 0.0660  -0.0077 0.0113  241 TYR B OH  
6097 N N   . PHE B 242 ? 0.4307 0.1683 0.3180 0.0511  -0.0129 -0.0205 242 PHE B N   
6098 C CA  . PHE B 242 ? 0.4540 0.1734 0.3426 0.0570  -0.0134 -0.0161 242 PHE B CA  
6099 C C   . PHE B 242 ? 0.4789 0.1959 0.3651 0.0698  -0.0118 -0.0253 242 PHE B C   
6100 O O   . PHE B 242 ? 0.4519 0.1633 0.3397 0.0808  -0.0107 -0.0210 242 PHE B O   
6101 C CB  . PHE B 242 ? 0.4444 0.1416 0.3357 0.0443  -0.0167 -0.0138 242 PHE B CB  
6102 C CG  . PHE B 242 ? 0.4697 0.1458 0.3642 0.0492  -0.0170 -0.0074 242 PHE B CG  
6103 C CD1 . PHE B 242 ? 0.4760 0.1514 0.3734 0.0511  -0.0160 0.0082  242 PHE B CD1 
6104 C CD2 . PHE B 242 ? 0.4811 0.1381 0.3751 0.0528  -0.0181 -0.0167 242 PHE B CD2 
6105 C CE1 . PHE B 242 ? 0.5155 0.1717 0.4167 0.0563  -0.0161 0.0158  242 PHE B CE1 
6106 C CE2 . PHE B 242 ? 0.5451 0.1806 0.4433 0.0579  -0.0181 -0.0105 242 PHE B CE2 
6107 C CZ  . PHE B 242 ? 0.5461 0.1814 0.4487 0.0596  -0.0172 0.0065  242 PHE B CZ  
6108 N N   . GLU B 243 ? 0.4479 0.1691 0.3297 0.0689  -0.0116 -0.0374 243 GLU B N   
6109 C CA  . GLU B 243 ? 0.4579 0.1789 0.3360 0.0816  -0.0092 -0.0462 243 GLU B CA  
6110 C C   . GLU B 243 ? 0.4636 0.2056 0.3447 0.0952  -0.0048 -0.0420 243 GLU B C   
6111 O O   . GLU B 243 ? 0.4770 0.2161 0.3590 0.1079  -0.0029 -0.0425 243 GLU B O   
6112 C CB  . GLU B 243 ? 0.4908 0.2172 0.3617 0.0784  -0.0094 -0.0586 243 GLU B CB  
6113 C CG  . GLU B 243 ? 0.5904 0.3213 0.4558 0.0924  -0.0055 -0.0676 243 GLU B CG  
6114 C CD  . GLU B 243 ? 0.6894 0.4355 0.5469 0.0913  -0.0041 -0.0765 243 GLU B CD  
6115 O OE1 . GLU B 243 ? 0.6867 0.4483 0.5416 0.1029  0.0011  -0.0796 243 GLU B OE1 
6116 O OE2 . GLU B 243 ? 0.6444 0.3882 0.4986 0.0792  -0.0080 -0.0796 243 GLU B OE2 
6117 N N   . ILE B 244 ? 0.3804 0.1440 0.2643 0.0925  -0.0035 -0.0378 244 ILE B N   
6118 C CA  . ILE B 244 ? 0.4259 0.2127 0.3148 0.1038  0.0002  -0.0348 244 ILE B CA  
6119 C C   . ILE B 244 ? 0.4073 0.1938 0.3013 0.1099  -0.0011 -0.0242 244 ILE B C   
6120 O O   . ILE B 244 ? 0.5009 0.2966 0.3990 0.1229  0.0006  -0.0223 244 ILE B O   
6121 C CB  . ILE B 244 ? 0.3764 0.1850 0.2679 0.0982  0.0018  -0.0350 244 ILE B CB  
6122 C CG1 . ILE B 244 ? 0.4061 0.2164 0.2915 0.0931  0.0030  -0.0439 244 ILE B CG1 
6123 C CG2 . ILE B 244 ? 0.3703 0.2040 0.2700 0.1086  0.0052  -0.0317 244 ILE B CG2 
6124 C CD1 . ILE B 244 ? 0.3845 0.1943 0.2651 0.1028  0.0059  -0.0517 244 ILE B CD1 
6125 N N   . PHE B 245 ? 0.3630 0.1411 0.2566 0.1011  -0.0041 -0.0163 245 PHE B N   
6126 C CA  . PHE B 245 ? 0.3942 0.1772 0.2907 0.1067  -0.0055 -0.0048 245 PHE B CA  
6127 C C   . PHE B 245 ? 0.4820 0.2416 0.3770 0.1062  -0.0077 0.0036  245 PHE B C   
6128 O O   . PHE B 245 ? 0.4442 0.2084 0.3406 0.1127  -0.0089 0.0144  245 PHE B O   
6129 C CB  . PHE B 245 ? 0.4099 0.2055 0.3063 0.0992  -0.0065 0.0000  245 PHE B CB  
6130 C CG  . PHE B 245 ? 0.3851 0.2039 0.2856 0.1001  -0.0044 -0.0067 245 PHE B CG  
6131 C CD1 . PHE B 245 ? 0.3609 0.2035 0.2694 0.1109  -0.0034 -0.0064 245 PHE B CD1 
6132 C CD2 . PHE B 245 ? 0.3519 0.1740 0.2523 0.0879  -0.0035 -0.0123 245 PHE B CD2 
6133 C CE1 . PHE B 245 ? 0.3911 0.2597 0.3084 0.1074  -0.0011 -0.0112 245 PHE B CE1 
6134 C CE2 . PHE B 245 ? 0.3541 0.2007 0.2616 0.0861  -0.0011 -0.0166 245 PHE B CE2 
6135 C CZ  . PHE B 245 ? 0.3143 0.1833 0.2306 0.0950  0.0003  -0.0159 245 PHE B CZ  
6136 N N   . GLY B 246 ? 0.4218 0.2055 0.4522 0.1530  0.0097  -0.0157 246 GLY B N   
6137 C CA  . GLY B 246 ? 0.4587 0.2083 0.4811 0.1558  0.0069  -0.0068 246 GLY B CA  
6138 C C   . GLY B 246 ? 0.5733 0.3128 0.5796 0.1463  -0.0011 0.0081  246 GLY B C   
6139 O O   . GLY B 246 ? 0.5536 0.2721 0.5560 0.1513  -0.0046 0.0205  246 GLY B O   
6140 N N   . GLU B 247 ? 0.5100 0.2639 0.5066 0.1330  -0.0037 0.0077  247 GLU B N   
6141 C CA  . GLU B 247 ? 0.6118 0.3539 0.5908 0.1212  -0.0089 0.0195  247 GLU B CA  
6142 C C   . GLU B 247 ? 0.5291 0.2720 0.4963 0.1020  -0.0064 0.0103  247 GLU B C   
6143 O O   . GLU B 247 ? 0.4123 0.1712 0.3846 0.1002  -0.0029 -0.0026 247 GLU B O   
6144 C CB  . GLU B 247 ? 0.7162 0.4836 0.6975 0.1294  -0.0194 0.0336  247 GLU B CB  
6145 C CG  . GLU B 247 ? 0.7985 0.6074 0.7964 0.1355  -0.0235 0.0270  247 GLU B CG  
6146 C CD  . GLU B 247 ? 0.9410 0.7757 0.9414 0.1426  -0.0359 0.0390  247 GLU B CD  
6147 O OE1 . GLU B 247 ? 1.0062 0.8353 1.0078 0.1537  -0.0406 0.0509  247 GLU B OE1 
6148 O OE2 . GLU B 247 ? 0.9671 0.8250 0.9659 0.1357  -0.0415 0.0363  247 GLU B OE2 
6149 N N   . HIS B 248 ? 0.4094 0.1360 0.3619 0.0878  -0.0074 0.0174  248 HIS B N   
6150 C CA  . HIS B 248 ? 0.4109 0.1434 0.3554 0.0702  -0.0065 0.0094  248 HIS B CA  
6151 C C   . HIS B 248 ? 0.4392 0.1985 0.3829 0.0710  -0.0136 0.0152  248 HIS B C   
6152 O O   . HIS B 248 ? 0.4581 0.2245 0.4001 0.0791  -0.0195 0.0283  248 HIS B O   
6153 C CB  . HIS B 248 ? 0.4578 0.1658 0.3914 0.0516  -0.0038 0.0122  248 HIS B CB  
6154 C CG  . HIS B 248 ? 0.6302 0.3135 0.5653 0.0473  0.0018  0.0018  248 HIS B CG  
6155 N ND1 . HIS B 248 ? 0.6682 0.3252 0.6051 0.0538  0.0038  0.0083  248 HIS B ND1 
6156 C CD2 . HIS B 248 ? 0.6336 0.3145 0.5679 0.0380  0.0047  -0.0153 248 HIS B CD2 
6157 C CE1 . HIS B 248 ? 0.7273 0.3651 0.6651 0.0482  0.0078  -0.0054 248 HIS B CE1 
6158 N NE2 . HIS B 248 ? 0.6798 0.3329 0.6153 0.0385  0.0082  -0.0201 248 HIS B NE2 
6159 N N   . PRO B 249 ? 0.3623 0.1478 0.3117 0.0605  -0.0128 0.0054  249 PRO B N   
6160 C CA  . PRO B 249 ? 0.3131 0.1354 0.2703 0.0587  -0.0180 0.0084  249 PRO B CA  
6161 C C   . PRO B 249 ? 0.3590 0.1811 0.3052 0.0468  -0.0202 0.0181  249 PRO B C   
6162 O O   . PRO B 249 ? 0.4489 0.2585 0.3880 0.0320  -0.0164 0.0173  249 PRO B O   
6163 C CB  . PRO B 249 ? 0.3194 0.1619 0.2844 0.0508  -0.0144 -0.0041 249 PRO B CB  
6164 C CG  . PRO B 249 ? 0.3629 0.1804 0.3172 0.0409  -0.0094 -0.0113 249 PRO B CG  
6165 C CD  . PRO B 249 ? 0.3792 0.1616 0.3271 0.0504  -0.0074 -0.0091 249 PRO B CD  
6166 N N   . VAL B 250 ? 0.3444 0.1831 0.2899 0.0532  -0.0264 0.0266  250 VAL B N   
6167 C CA  . VAL B 250 ? 0.3318 0.1741 0.2650 0.0442  -0.0272 0.0354  250 VAL B CA  
6168 C C   . VAL B 250 ? 0.3230 0.1967 0.2631 0.0361  -0.0281 0.0285  250 VAL B C   
6169 O O   . VAL B 250 ? 0.3089 0.1865 0.2407 0.0263  -0.0257 0.0324  250 VAL B O   
6170 C CB  . VAL B 250 ? 0.4560 0.2934 0.3776 0.0571  -0.0336 0.0493  250 VAL B CB  
6171 C CG1 . VAL B 250 ? 0.5408 0.4026 0.4757 0.0722  -0.0424 0.0456  250 VAL B CG1 
6172 C CG2 . VAL B 250 ? 0.5212 0.3650 0.4264 0.0498  -0.0337 0.0583  250 VAL B CG2 
6173 N N   . TYR B 251 ? 0.2517 0.1463 0.2076 0.0398  -0.0298 0.0185  251 TYR B N   
6174 C CA  . TYR B 251 ? 0.2722 0.1912 0.2361 0.0323  -0.0294 0.0115  251 TYR B CA  
6175 C C   . TYR B 251 ? 0.2502 0.1721 0.2244 0.0275  -0.0240 0.0024  251 TYR B C   
6176 O O   . TYR B 251 ? 0.2499 0.1661 0.2299 0.0342  -0.0222 -0.0017 251 TYR B O   
6177 C CB  . TYR B 251 ? 0.3221 0.2650 0.2961 0.0398  -0.0363 0.0086  251 TYR B CB  
6178 C CG  . TYR B 251 ? 0.2641 0.2047 0.2307 0.0514  -0.0444 0.0167  251 TYR B CG  
6179 C CD1 . TYR B 251 ? 0.4153 0.3530 0.3627 0.0502  -0.0477 0.0249  251 TYR B CD1 
6180 C CD2 . TYR B 251 ? 0.4232 0.3660 0.4015 0.0650  -0.0486 0.0170  251 TYR B CD2 
6181 C CE1 . TYR B 251 ? 0.4803 0.4158 0.4170 0.0620  -0.0561 0.0343  251 TYR B CE1 
6182 C CE2 . TYR B 251 ? 0.4159 0.3579 0.3876 0.0780  -0.0577 0.0263  251 TYR B CE2 
6183 C CZ  . TYR B 251 ? 0.5561 0.4939 0.5054 0.0763  -0.0621 0.0354  251 TYR B CZ  
6184 O OH  . TYR B 251 ? 0.7555 0.6920 0.6940 0.0900  -0.0719 0.0466  251 TYR B OH  
6185 N N   . MET B 252 ? 0.2329 0.1644 0.2084 0.0175  -0.0210 -0.0005 252 MET B N   
6186 C CA  . MET B 252 ? 0.1810 0.1180 0.1634 0.0138  -0.0168 -0.0073 252 MET B CA  
6187 C C   . MET B 252 ? 0.1937 0.1503 0.1847 0.0107  -0.0160 -0.0097 252 MET B C   
6188 O O   . MET B 252 ? 0.2037 0.1663 0.1924 0.0078  -0.0174 -0.0074 252 MET B O   
6189 C CB  . MET B 252 ? 0.2116 0.1366 0.1862 0.0046  -0.0144 -0.0079 252 MET B CB  
6190 C CG  . MET B 252 ? 0.2513 0.1530 0.2186 0.0066  -0.0136 -0.0097 252 MET B CG  
6191 S SD  . MET B 252 ? 0.2938 0.1861 0.2544 -0.0043 -0.0121 -0.0170 252 MET B SD  
6192 C CE  . MET B 252 ? 0.3240 0.1855 0.2763 0.0022  -0.0101 -0.0222 252 MET B CE  
6193 N N   . TRP B 253 ? 0.1979 0.1623 0.1978 0.0116  -0.0125 -0.0143 253 TRP B N   
6194 C CA  . TRP B 253 ? 0.2198 0.1966 0.2272 0.0077  -0.0099 -0.0156 253 TRP B CA  
6195 C C   . TRP B 253 ? 0.2192 0.1931 0.2206 0.0026  -0.0069 -0.0145 253 TRP B C   
6196 O O   . TRP B 253 ? 0.2043 0.1733 0.2012 0.0033  -0.0047 -0.0164 253 TRP B O   
6197 C CB  . TRP B 253 ? 0.1676 0.1548 0.1890 0.0109  -0.0066 -0.0192 253 TRP B CB  
6198 C CG  . TRP B 253 ? 0.1385 0.1319 0.1660 0.0062  -0.0018 -0.0192 253 TRP B CG  
6199 C CD1 . TRP B 253 ? 0.1661 0.1597 0.1942 0.0054  0.0050  -0.0180 253 TRP B CD1 
6200 C CD2 . TRP B 253 ? 0.1082 0.1055 0.1398 0.0027  -0.0026 -0.0199 253 TRP B CD2 
6201 N NE1 . TRP B 253 ? 0.1523 0.1482 0.1857 0.0019  0.0083  -0.0161 253 TRP B NE1 
6202 C CE2 . TRP B 253 ? 0.1093 0.1067 0.1457 0.0002  0.0039  -0.0182 253 TRP B CE2 
6203 C CE3 . TRP B 253 ? 0.1455 0.1445 0.1743 0.0020  -0.0076 -0.0217 253 TRP B CE3 
6204 C CZ2 . TRP B 253 ? 0.1504 0.1475 0.1919 -0.0024 0.0058  -0.0190 253 TRP B CZ2 
6205 C CZ3 . TRP B 253 ? 0.1506 0.1510 0.1829 -0.0011 -0.0055 -0.0243 253 TRP B CZ3 
6206 C CH2 . TRP B 253 ? 0.1506 0.1490 0.1905 -0.0031 0.0012  -0.0232 253 TRP B CH2 
6207 N N   . PRO B 254 ? 0.1523 0.1301 0.1528 -0.0019 -0.0071 -0.0118 254 PRO B N   
6208 C CA  . PRO B 254 ? 0.1885 0.1681 0.1859 -0.0056 -0.0064 -0.0102 254 PRO B CA  
6209 C C   . PRO B 254 ? 0.1630 0.1480 0.1645 -0.0032 -0.0024 -0.0097 254 PRO B C   
6210 O O   . PRO B 254 ? 0.1838 0.1729 0.1941 -0.0017 0.0005  -0.0094 254 PRO B O   
6211 C CB  . PRO B 254 ? 0.2291 0.2151 0.2291 -0.0090 -0.0069 -0.0070 254 PRO B CB  
6212 C CG  . PRO B 254 ? 0.2116 0.1996 0.2151 -0.0062 -0.0057 -0.0082 254 PRO B CG  
6213 C CD  . PRO B 254 ? 0.1348 0.1174 0.1369 -0.0026 -0.0080 -0.0108 254 PRO B CD  
6214 N N   . PRO B 255 ? 0.1646 0.1480 0.1583 -0.0030 -0.0017 -0.0098 255 PRO B N   
6215 C CA  . PRO B 255 ? 0.1602 0.1469 0.1545 -0.0003 0.0038  -0.0069 255 PRO B CA  
6216 C C   . PRO B 255 ? 0.1523 0.1443 0.1541 0.0003  0.0051  -0.0013 255 PRO B C   
6217 O O   . PRO B 255 ? 0.1847 0.1816 0.1870 -0.0008 0.0010  0.0011  255 PRO B O   
6218 C CB  . PRO B 255 ? 0.1895 0.1744 0.1680 -0.0006 0.0022  -0.0075 255 PRO B CB  
6219 C CG  . PRO B 255 ? 0.2106 0.1866 0.1832 -0.0027 -0.0014 -0.0144 255 PRO B CG  
6220 C CD  . PRO B 255 ? 0.1961 0.1722 0.1779 -0.0056 -0.0051 -0.0133 255 PRO B CD  
6221 N N   . GLU B 256 ? 0.1613 0.1520 0.1711 0.0019  0.0117  0.0006  256 GLU B N   
6222 C CA  . GLU B 256 ? 0.1759 0.1658 0.1939 0.0033  0.0149  0.0052  256 GLU B CA  
6223 C C   . GLU B 256 ? 0.1826 0.1743 0.2075 0.0025  0.0118  0.0015  256 GLU B C   
6224 O O   . GLU B 256 ? 0.1519 0.1439 0.1811 0.0052  0.0133  0.0047  256 GLU B O   
6225 C CB  . GLU B 256 ? 0.2037 0.1954 0.2141 0.0071  0.0144  0.0141  256 GLU B CB  
6226 C CG  . GLU B 256 ? 0.1673 0.1580 0.1632 0.0084  0.0166  0.0179  256 GLU B CG  
6227 C CD  . GLU B 256 ? 0.2217 0.2056 0.2213 0.0083  0.0276  0.0210  256 GLU B CD  
6228 O OE1 . GLU B 256 ? 0.2466 0.2253 0.2610 0.0069  0.0327  0.0213  256 GLU B OE1 
6229 O OE2 . GLU B 256 ? 0.2130 0.1966 0.2004 0.0091  0.0320  0.0227  256 GLU B OE2 
6230 N N   . ALA B 257 ? 0.1621 0.1548 0.1868 0.0001  0.0083  -0.0047 257 ALA B N   
6231 C CA  . ALA B 257 ? 0.1514 0.1460 0.1770 -0.0007 0.0059  -0.0078 257 ALA B CA  
6232 C C   . ALA B 257 ? 0.1500 0.1505 0.1733 -0.0004 0.0044  -0.0036 257 ALA B C   
6233 O O   . ALA B 257 ? 0.2021 0.2059 0.2277 0.0002  0.0059  -0.0047 257 ALA B O   
6234 C CB  . ALA B 257 ? 0.2009 0.1925 0.2347 -0.0002 0.0097  -0.0121 257 ALA B CB  
6235 N N   . SER B 258 ? 0.1522 0.1560 0.1712 -0.0011 0.0016  0.0004  258 SER B N   
6236 C CA  . SER B 258 ? 0.1558 0.1703 0.1782 -0.0009 -0.0006 0.0046  258 SER B CA  
6237 C C   . SER B 258 ? 0.1773 0.1963 0.1991 -0.0066 -0.0030 0.0030  258 SER B C   
6238 O O   . SER B 258 ? 0.1851 0.1977 0.1993 -0.0115 -0.0062 0.0008  258 SER B O   
6239 C CB  . SER B 258 ? 0.1829 0.2018 0.1998 -0.0002 -0.0047 0.0087  258 SER B CB  
6240 O OG  . SER B 258 ? 0.2131 0.2469 0.2377 0.0015  -0.0080 0.0134  258 SER B OG  
6241 N N   . VAL B 259 ? 0.1729 0.2016 0.2031 -0.0057 0.0000  0.0046  259 VAL B N   
6242 C CA  . VAL B 259 ? 0.1325 0.1674 0.1639 -0.0121 0.0002  0.0050  259 VAL B CA  
6243 C C   . VAL B 259 ? 0.1706 0.2258 0.2170 -0.0112 0.0014  0.0089  259 VAL B C   
6244 O O   . VAL B 259 ? 0.2184 0.2809 0.2733 -0.0033 0.0021  0.0114  259 VAL B O   
6245 C CB  . VAL B 259 ? 0.1585 0.1864 0.1831 -0.0120 0.0051  0.0027  259 VAL B CB  
6246 C CG1 . VAL B 259 ? 0.2099 0.2220 0.2228 -0.0120 0.0018  -0.0005 259 VAL B CG1 
6247 C CG2 . VAL B 259 ? 0.1852 0.2165 0.2146 -0.0049 0.0114  0.0004  259 VAL B CG2 
6248 N N   . SER B 260 ? 0.1506 0.2147 0.2017 -0.0194 0.0017  0.0102  260 SER B N   
6249 C CA  . SER B 260 ? 0.1229 0.2112 0.1926 -0.0211 0.0036  0.0136  260 SER B CA  
6250 C C   . SER B 260 ? 0.1807 0.2687 0.2495 -0.0321 0.0081  0.0146  260 SER B C   
6251 O O   . SER B 260 ? 0.1926 0.2602 0.2455 -0.0373 0.0071  0.0134  260 SER B O   
6252 C CB  . SER B 260 ? 0.1605 0.2648 0.2402 -0.0231 -0.0064 0.0153  260 SER B CB  
6253 O OG  . SER B 260 ? 0.1778 0.2759 0.2510 -0.0359 -0.0130 0.0123  260 SER B OG  
6254 N N   . ASN B 261 ? 0.1510 0.2613 0.2374 -0.0349 0.0142  0.0177  261 ASN B N   
6255 C CA  . ASN B 261 ? 0.1520 0.2618 0.2380 -0.0468 0.0207  0.0206  261 ASN B CA  
6256 C C   . ASN B 261 ? 0.2034 0.3026 0.2864 -0.0607 0.0123  0.0198  261 ASN B C   
6257 O O   . ASN B 261 ? 0.1877 0.2656 0.2563 -0.0677 0.0152  0.0214  261 ASN B O   
6258 C CB  . ASN B 261 ? 0.1387 0.2795 0.2494 -0.0486 0.0296  0.0243  261 ASN B CB  
6259 C CG  . ASN B 261 ? 0.1459 0.2916 0.2553 -0.0351 0.0415  0.0237  261 ASN B CG  
6260 O OD1 . ASN B 261 ? 0.1848 0.3089 0.2716 -0.0289 0.0446  0.0209  261 ASN B OD1 
6261 N ND2 . ASN B 261 ? 0.1437 0.3192 0.2784 -0.0303 0.0480  0.0255  261 ASN B ND2 
6262 N N   . GLU B 262 ? 0.1565 0.2678 0.2503 -0.0639 0.0015  0.0168  262 GLU B N   
6263 C CA  . GLU B 262 ? 0.1841 0.2837 0.2737 -0.0777 -0.0066 0.0130  262 GLU B CA  
6264 C C   . GLU B 262 ? 0.1729 0.2389 0.2365 -0.0738 -0.0099 0.0092  262 GLU B C   
6265 O O   . GLU B 262 ? 0.2027 0.2470 0.2568 -0.0833 -0.0107 0.0073  262 GLU B O   
6266 C CB  . GLU B 262 ? 0.1951 0.3180 0.2994 -0.0813 -0.0190 0.0092  262 GLU B CB  
6267 C CG  . GLU B 262 ? 0.1720 0.3313 0.3074 -0.0887 -0.0176 0.0122  262 GLU B CG  
6268 C CD  . GLU B 262 ? 0.3790 0.5653 0.5294 -0.0922 -0.0329 0.0083  262 GLU B CD  
6269 O OE1 . GLU B 262 ? 0.3509 0.5227 0.4853 -0.0973 -0.0442 0.0012  262 GLU B OE1 
6270 O OE2 . GLU B 262 ? 0.3499 0.5690 0.5253 -0.0871 -0.0331 0.0115  262 GLU B OE2 
6271 N N   . ALA B 263 ? 0.1566 0.2176 0.2103 -0.0601 -0.0112 0.0080  263 ALA B N   
6272 C CA  . ALA B 263 ? 0.2048 0.2389 0.2383 -0.0557 -0.0132 0.0045  263 ALA B CA  
6273 C C   . ALA B 263 ? 0.1694 0.1841 0.1919 -0.0555 -0.0065 0.0076  263 ALA B C   
6274 O O   . ALA B 263 ? 0.2087 0.2007 0.2192 -0.0581 -0.0081 0.0059  263 ALA B O   
6275 C CB  . ALA B 263 ? 0.2080 0.2435 0.2370 -0.0426 -0.0143 0.0036  263 ALA B CB  
6276 N N   . LEU B 264 ? 0.2044 0.2271 0.2292 -0.0513 0.0010  0.0120  264 LEU B N   
6277 C CA  . LEU B 264 ? 0.1876 0.1943 0.1986 -0.0507 0.0065  0.0162  264 LEU B CA  
6278 C C   . LEU B 264 ? 0.2647 0.2592 0.2742 -0.0633 0.0088  0.0208  264 LEU B C   
6279 O O   . LEU B 264 ? 0.2697 0.2404 0.2639 -0.0627 0.0092  0.0240  264 LEU B O   
6280 C CB  . LEU B 264 ? 0.1572 0.1767 0.1687 -0.0451 0.0148  0.0189  264 LEU B CB  
6281 C CG  . LEU B 264 ? 0.1704 0.1936 0.1809 -0.0332 0.0131  0.0134  264 LEU B CG  
6282 C CD1 . LEU B 264 ? 0.2510 0.2867 0.2633 -0.0279 0.0217  0.0132  264 LEU B CD1 
6283 C CD2 . LEU B 264 ? 0.2344 0.2391 0.2294 -0.0277 0.0083  0.0110  264 LEU B CD2 
6284 N N   . GLU B 265 ? 0.2126 0.2231 0.2393 -0.0750 0.0101  0.0215  265 GLU B N   
6285 C CA  . GLU B 265 ? 0.2284 0.2256 0.2566 -0.0901 0.0126  0.0250  265 GLU B CA  
6286 C C   . GLU B 265 ? 0.2634 0.2343 0.2821 -0.0934 0.0044  0.0186  265 GLU B C   
6287 O O   . GLU B 265 ? 0.3241 0.2676 0.3330 -0.0994 0.0073  0.0223  265 GLU B O   
6288 C CB  . GLU B 265 ? 0.2548 0.2800 0.3089 -0.1035 0.0146  0.0253  265 GLU B CB  
6289 C CG  . GLU B 265 ? 0.2877 0.3365 0.3522 -0.1016 0.0267  0.0325  265 GLU B CG  
6290 C CD  . GLU B 265 ? 0.4583 0.5366 0.5527 -0.1163 0.0303  0.0340  265 GLU B CD  
6291 O OE1 . GLU B 265 ? 0.5300 0.6162 0.6307 -0.1228 0.0439  0.0422  265 GLU B OE1 
6292 O OE2 . GLU B 265 ? 0.5150 0.6104 0.6268 -0.1213 0.0195  0.0272  265 GLU B OE2 
6293 N N   . LEU B 266 ? 0.2475 0.2245 0.2674 -0.0890 -0.0048 0.0095  266 LEU B N   
6294 C CA  . LEU B 266 ? 0.2429 0.1954 0.2516 -0.0910 -0.0111 0.0015  266 LEU B CA  
6295 C C   . LEU B 266 ? 0.2385 0.1637 0.2289 -0.0790 -0.0089 0.0037  266 LEU B C   
6296 O O   . LEU B 266 ? 0.2923 0.1885 0.2735 -0.0821 -0.0083 0.0028  266 LEU B O   
6297 C CB  . LEU B 266 ? 0.2421 0.2093 0.2522 -0.0875 -0.0202 -0.0077 266 LEU B CB  
6298 C CG  . LEU B 266 ? 0.2930 0.2359 0.2871 -0.0859 -0.0251 -0.0176 266 LEU B CG  
6299 C CD1 . LEU B 266 ? 0.3292 0.2516 0.3227 -0.1019 -0.0268 -0.0235 266 LEU B CD1 
6300 C CD2 . LEU B 266 ? 0.2925 0.2519 0.2833 -0.0802 -0.0324 -0.0245 266 LEU B CD2 
6301 N N   . TYR B 267 ? 0.2324 0.1667 0.2191 -0.0653 -0.0076 0.0065  267 TYR B N   
6302 C CA  . TYR B 267 ? 0.2765 0.1916 0.2497 -0.0536 -0.0069 0.0088  267 TYR B CA  
6303 C C   . TYR B 267 ? 0.2316 0.1268 0.1962 -0.0564 -0.0019 0.0187  267 TYR B C   
6304 O O   . TYR B 267 ? 0.3220 0.1913 0.2763 -0.0513 -0.0026 0.0203  267 TYR B O   
6305 C CB  . TYR B 267 ? 0.2274 0.1591 0.2011 -0.0416 -0.0069 0.0093  267 TYR B CB  
6306 C CG  . TYR B 267 ? 0.2709 0.2135 0.2492 -0.0361 -0.0106 0.0017  267 TYR B CG  
6307 C CD1 . TYR B 267 ? 0.2545 0.1841 0.2271 -0.0307 -0.0130 -0.0040 267 TYR B CD1 
6308 C CD2 . TYR B 267 ? 0.1662 0.1309 0.1539 -0.0354 -0.0102 0.0010  267 TYR B CD2 
6309 C CE1 . TYR B 267 ? 0.2335 0.1726 0.2082 -0.0261 -0.0142 -0.0093 267 TYR B CE1 
6310 C CE2 . TYR B 267 ? 0.2277 0.1995 0.2175 -0.0302 -0.0124 -0.0034 267 TYR B CE2 
6311 C CZ  . TYR B 267 ? 0.2478 0.2072 0.2302 -0.0263 -0.0140 -0.0082 267 TYR B CZ  
6312 O OH  . TYR B 267 ? 0.2458 0.2117 0.2281 -0.0216 -0.0142 -0.0112 267 TYR B OH  
6313 N N   . TYR B 268 ? 0.2319 0.1389 0.2001 -0.0631 0.0043  0.0265  268 TYR B N   
6314 C CA  . TYR B 268 ? 0.2842 0.1724 0.2422 -0.0674 0.0110  0.0383  268 TYR B CA  
6315 C C   . TYR B 268 ? 0.3270 0.1873 0.2856 -0.0794 0.0118  0.0383  268 TYR B C   
6316 O O   . TYR B 268 ? 0.3247 0.1542 0.2698 -0.0761 0.0138  0.0456  268 TYR B O   
6317 C CB  . TYR B 268 ? 0.2680 0.1774 0.2316 -0.0743 0.0199  0.0455  268 TYR B CB  
6318 C CG  . TYR B 268 ? 0.2976 0.1900 0.2565 -0.0861 0.0293  0.0576  268 TYR B CG  
6319 C CD1 . TYR B 268 ? 0.3688 0.2372 0.3054 -0.0791 0.0328  0.0697  268 TYR B CD1 
6320 C CD2 . TYR B 268 ? 0.2901 0.1911 0.2677 -0.1044 0.0348  0.0579  268 TYR B CD2 
6321 C CE1 . TYR B 268 ? 0.3969 0.2464 0.3271 -0.0898 0.0429  0.0832  268 TYR B CE1 
6322 C CE2 . TYR B 268 ? 0.3912 0.2754 0.3663 -0.1171 0.0452  0.0698  268 TYR B CE2 
6323 C CZ  . TYR B 268 ? 0.4573 0.3157 0.4088 -0.1082 0.0497  0.0826  268 TYR B CZ  
6324 O OH  . TYR B 268 ? 0.4687 0.3160 0.4223 -0.1147 0.0590  0.0945  268 TYR B OH  
6325 N N   . GLU B 269 ? 0.3631 0.2329 0.3372 -0.0934 0.0098  0.0300  269 GLU B N   
6326 C CA  . GLU B 269 ? 0.3891 0.2317 0.3647 -0.1079 0.0105  0.0277  269 GLU B CA  
6327 C C   . GLU B 269 ? 0.3731 0.1840 0.3357 -0.0989 0.0054  0.0202  269 GLU B C   
6328 O O   . GLU B 269 ? 0.4267 0.2122 0.3884 -0.1004 0.0081  0.0210  269 GLU B O   
6329 C CB  . GLU B 269 ? 0.3626 0.2295 0.3600 -0.1234 0.0069  0.0180  269 GLU B CB  
6330 C CG  . GLU B 269 ? 0.3955 0.2897 0.4116 -0.1341 0.0146  0.0262  269 GLU B CG  
6331 C CD  . GLU B 269 ? 0.5500 0.4248 0.5673 -0.1409 0.0250  0.0374  269 GLU B CD  
6332 O OE1 . GLU B 269 ? 0.5454 0.3856 0.5528 -0.1394 0.0248  0.0378  269 GLU B OE1 
6333 O OE2 . GLU B 269 ? 0.5888 0.4841 0.6183 -0.1472 0.0342  0.0462  269 GLU B OE2 
6334 N N   . LYS B 270 ? 0.3721 0.1935 0.3307 -0.0839 -0.0006 0.0127  270 LYS B N   
6335 C CA  . LYS B 270 ? 0.3778 0.1737 0.3256 -0.0727 -0.0035 0.0055  270 LYS B CA  
6336 C C   . LYS B 270 ? 0.4176 0.1984 0.3545 -0.0554 -0.0014 0.0160  270 LYS B C   
6337 O O   . LYS B 270 ? 0.3951 0.1610 0.3265 -0.0422 -0.0034 0.0111  270 LYS B O   
6338 C CB  . LYS B 270 ? 0.3613 0.1778 0.3113 -0.0658 -0.0094 -0.0072 270 LYS B CB  
6339 C CG  . LYS B 270 ? 0.3688 0.1976 0.3254 -0.0804 -0.0141 -0.0186 270 LYS B CG  
6340 C CD  . LYS B 270 ? 0.4992 0.3013 0.4533 -0.0889 -0.0143 -0.0276 270 LYS B CD  
6341 C CE  . LYS B 270 ? 0.5500 0.3724 0.5125 -0.1015 -0.0211 -0.0395 270 LYS B CE  
6342 N NZ  . LYS B 270 ? 0.6361 0.4487 0.6098 -0.1157 -0.0205 -0.0424 270 LYS B NZ  
6343 N N   . GLY B 271 ? 0.3262 0.1125 0.2596 -0.0544 0.0024  0.0302  271 GLY B N   
6344 C CA  . GLY B 271 ? 0.3880 0.1597 0.3086 -0.0388 0.0026  0.0417  271 GLY B CA  
6345 C C   . GLY B 271 ? 0.3571 0.1546 0.2777 -0.0229 -0.0029 0.0404  271 GLY B C   
6346 O O   . GLY B 271 ? 0.4099 0.1989 0.3222 -0.0080 -0.0057 0.0474  271 GLY B O   
6347 N N   . ILE B 272 ? 0.3184 0.1469 0.2492 -0.0254 -0.0049 0.0319  272 ILE B N   
6348 C CA  . ILE B 272 ? 0.3027 0.1548 0.2355 -0.0134 -0.0092 0.0300  272 ILE B CA  
6349 C C   . ILE B 272 ? 0.3162 0.1784 0.2398 -0.0125 -0.0075 0.0401  272 ILE B C   
6350 O O   . ILE B 272 ? 0.3510 0.2214 0.2752 -0.0234 -0.0018 0.0433  272 ILE B O   
6351 C CB  . ILE B 272 ? 0.2748 0.1515 0.2203 -0.0166 -0.0104 0.0187  272 ILE B CB  
6352 C CG1 . ILE B 272 ? 0.3461 0.2127 0.2954 -0.0178 -0.0114 0.0087  272 ILE B CG1 
6353 C CG2 . ILE B 272 ? 0.2792 0.1773 0.2286 -0.0066 -0.0137 0.0163  272 ILE B CG2 
6354 C CD1 . ILE B 272 ? 0.3892 0.2349 0.3340 -0.0059 -0.0124 0.0075  272 ILE B CD1 
6355 N N   . ASN B 273 ? 0.3209 0.1847 0.2360 0.0008  -0.0126 0.0446  273 ASN B N   
6356 C CA  . ASN B 273 ? 0.3039 0.1754 0.2040 0.0034  -0.0122 0.0537  273 ASN B CA  
6357 C C   . ASN B 273 ? 0.2779 0.1786 0.1823 0.0052  -0.0150 0.0451  273 ASN B C   
6358 O O   . ASN B 273 ? 0.2883 0.1981 0.1810 0.0032  -0.0117 0.0487  273 ASN B O   
6359 C CB  . ASN B 273 ? 0.3037 0.1612 0.1894 0.0175  -0.0184 0.0639  273 ASN B CB  
6360 C CG  . ASN B 273 ? 0.6434 0.4929 0.5056 0.0171  -0.0147 0.0791  273 ASN B CG  
6361 O OD1 . ASN B 273 ? 0.6639 0.5050 0.5216 0.0046  -0.0044 0.0853  273 ASN B OD1 
6362 N ND2 . ASN B 273 ? 0.7828 0.6365 0.6296 0.0307  -0.0231 0.0857  273 ASN B ND2 
6363 N N   A MET B 274 ? 0.2685 0.1824 0.1886 0.0088  -0.0197 0.0337  274 MET B N   
6364 N N   B MET B 274 ? 0.2687 0.1825 0.1887 0.0089  -0.0197 0.0337  274 MET B N   
6365 C CA  A MET B 274 ? 0.2586 0.1955 0.1841 0.0099  -0.0219 0.0251  274 MET B CA  
6366 C CA  B MET B 274 ? 0.2589 0.1959 0.1845 0.0097  -0.0217 0.0251  274 MET B CA  
6367 C C   A MET B 274 ? 0.2415 0.1875 0.1868 0.0079  -0.0216 0.0146  274 MET B C   
6368 C C   B MET B 274 ? 0.2422 0.1881 0.1874 0.0078  -0.0215 0.0146  274 MET B C   
6369 O O   A MET B 274 ? 0.2693 0.2081 0.2221 0.0110  -0.0231 0.0126  274 MET B O   
6370 O O   B MET B 274 ? 0.2681 0.2067 0.2209 0.0108  -0.0230 0.0126  274 MET B O   
6371 C CB  A MET B 274 ? 0.2613 0.2067 0.1796 0.0204  -0.0312 0.0249  274 MET B CB  
6372 C CB  B MET B 274 ? 0.2605 0.2064 0.1786 0.0200  -0.0310 0.0247  274 MET B CB  
6373 C CG  A MET B 274 ? 0.2528 0.2188 0.1734 0.0193  -0.0335 0.0148  274 MET B CG  
6374 C CG  B MET B 274 ? 0.2525 0.2190 0.1744 0.0188  -0.0331 0.0140  274 MET B CG  
6375 S SD  A MET B 274 ? 0.2982 0.2789 0.2170 0.0297  -0.0479 0.0107  274 MET B SD  
6376 S SD  B MET B 274 ? 0.2706 0.2513 0.2195 0.0200  -0.0371 0.0013  274 MET B SD  
6377 C CE  A MET B 274 ? 0.2939 0.2792 0.2412 0.0340  -0.0512 0.0055  274 MET B CE  
6378 C CE  B MET B 274 ? 0.3077 0.2952 0.2579 0.0320  -0.0500 0.0032  274 MET B CE  
6379 N N   . LEU B 275 ? 0.2312 0.1916 0.1832 0.0036  -0.0185 0.0084  275 LEU B N   
6380 C CA  . LEU B 275 ? 0.2076 0.1767 0.1757 0.0029  -0.0180 0.0003  275 LEU B CA  
6381 C C   . LEU B 275 ? 0.1885 0.1707 0.1596 0.0032  -0.0180 -0.0061 275 LEU B C   
6382 O O   . LEU B 275 ? 0.1894 0.1741 0.1486 0.0037  -0.0183 -0.0055 275 LEU B O   
6383 C CB  . LEU B 275 ? 0.2326 0.1998 0.2068 -0.0038 -0.0130 0.0005  275 LEU B CB  
6384 C CG  . LEU B 275 ? 0.2589 0.2303 0.2317 -0.0106 -0.0077 0.0039  275 LEU B CG  
6385 C CD1 . LEU B 275 ? 0.2801 0.2652 0.2591 -0.0095 -0.0045 -0.0004 275 LEU B CD1 
6386 C CD2 . LEU B 275 ? 0.2724 0.2417 0.2514 -0.0171 -0.0067 0.0045  275 LEU B CD2 
6387 N N   . ALA B 276 ? 0.2081 0.1969 0.1936 0.0028  -0.0172 -0.0125 276 ALA B N   
6388 C CA  . ALA B 276 ? 0.1903 0.1866 0.1810 0.0014  -0.0153 -0.0195 276 ALA B CA  
6389 C C   . ALA B 276 ? 0.1615 0.1576 0.1618 -0.0013 -0.0085 -0.0193 276 ALA B C   
6390 O O   . ALA B 276 ? 0.1919 0.1854 0.1958 -0.0021 -0.0072 -0.0154 276 ALA B O   
6391 C CB  . ALA B 276 ? 0.1478 0.1514 0.1489 0.0029  -0.0206 -0.0268 276 ALA B CB  
6392 N N   . THR B 277 ? 0.1626 0.1608 0.1654 -0.0017 -0.0044 -0.0236 277 THR B N   
6393 C CA  . THR B 277 ? 0.1582 0.1558 0.1710 -0.0018 0.0015  -0.0222 277 THR B CA  
6394 C C   . THR B 277 ? 0.1758 0.1707 0.1948 -0.0014 0.0047  -0.0301 277 THR B C   
6395 O O   . THR B 277 ? 0.1882 0.1833 0.2070 -0.0031 0.0008  -0.0378 277 THR B O   
6396 C CB  . THR B 277 ? 0.1918 0.1932 0.2023 -0.0019 0.0050  -0.0160 277 THR B CB  
6397 O OG1 . THR B 277 ? 0.1811 0.1846 0.2020 0.0004  0.0091  -0.0134 277 THR B OG1 
6398 C CG2 . THR B 277 ? 0.1798 0.1842 0.1820 -0.0013 0.0083  -0.0179 277 THR B CG2 
6399 N N   . ASP B 278 ? 0.1726 0.1645 0.1982 0.0009  0.0112  -0.0287 278 ASP B N   
6400 C CA  . ASP B 278 ? 0.1751 0.1582 0.2087 0.0009  0.0155  -0.0355 278 ASP B CA  
6401 C C   . ASP B 278 ? 0.1955 0.1751 0.2243 0.0040  0.0204  -0.0429 278 ASP B C   
6402 O O   . ASP B 278 ? 0.1934 0.1793 0.2173 0.0079  0.0237  -0.0392 278 ASP B O   
6403 C CB  . ASP B 278 ? 0.1953 0.1723 0.2396 0.0032  0.0207  -0.0280 278 ASP B CB  
6404 C CG  . ASP B 278 ? 0.2427 0.2053 0.2961 0.0022  0.0265  -0.0337 278 ASP B CG  
6405 O OD1 . ASP B 278 ? 0.2408 0.2008 0.2987 -0.0044 0.0243  -0.0419 278 ASP B OD1 
6406 O OD2 . ASP B 278 ? 0.2623 0.2162 0.3201 0.0081  0.0331  -0.0302 278 ASP B OD2 
6407 N N   . GLU B 279 ? 0.2363 0.1968 0.2551 0.0507  -0.0015 -0.0090 279 GLU B N   
6408 C CA  . GLU B 279 ? 0.2318 0.1922 0.2566 0.0549  0.0052  -0.0141 279 GLU B CA  
6409 C C   . GLU B 279 ? 0.2213 0.1871 0.2599 0.0646  0.0063  -0.0098 279 GLU B C   
6410 O O   . GLU B 279 ? 0.2403 0.2143 0.2878 0.0687  0.0117  -0.0129 279 GLU B O   
6411 C CB  . GLU B 279 ? 0.2187 0.1625 0.2359 0.0530  0.0102  -0.0197 279 GLU B CB  
6412 C CG  . GLU B 279 ? 0.2520 0.1935 0.2713 0.0545  0.0188  -0.0279 279 GLU B CG  
6413 C CD  . GLU B 279 ? 0.2909 0.2169 0.2993 0.0485  0.0235  -0.0350 279 GLU B CD  
6414 O OE1 . GLU B 279 ? 0.2467 0.1663 0.2474 0.0433  0.0195  -0.0325 279 GLU B OE1 
6415 O OE2 . GLU B 279 ? 0.3725 0.2936 0.3797 0.0480  0.0318  -0.0436 279 GLU B OE2 
6416 N N   . VAL B 280 ? 0.2069 0.1700 0.2482 0.0687  0.0016  -0.0017 280 VAL B N   
6417 C CA  . VAL B 280 ? 0.2096 0.1810 0.2664 0.0790  0.0018  0.0053  280 VAL B CA  
6418 C C   . VAL B 280 ? 0.2300 0.2266 0.2964 0.0783  -0.0015 0.0081  280 VAL B C   
6419 O O   . VAL B 280 ? 0.2196 0.2284 0.3014 0.0864  0.0023  0.0099  280 VAL B O   
6420 C CB  . VAL B 280 ? 0.2435 0.2094 0.3001 0.0823  -0.0039 0.0157  280 VAL B CB  
6421 C CG1 . VAL B 280 ? 0.2775 0.2567 0.3524 0.0936  -0.0051 0.0262  280 VAL B CG1 
6422 C CG2 . VAL B 280 ? 0.2854 0.2255 0.3337 0.0827  0.0006  0.0132  280 VAL B CG2 
6423 N N   . ILE B 281 ? 0.2251 0.2295 0.2828 0.0682  -0.0075 0.0080  281 ILE B N   
6424 C CA  . ILE B 281 ? 0.2405 0.2673 0.3051 0.0645  -0.0104 0.0097  281 ILE B CA  
6425 C C   . ILE B 281 ? 0.1961 0.2286 0.2653 0.0647  -0.0031 0.0026  281 ILE B C   
6426 O O   . ILE B 281 ? 0.2102 0.2624 0.2929 0.0677  -0.0017 0.0047  281 ILE B O   
6427 C CB  . ILE B 281 ? 0.1926 0.2205 0.2445 0.0526  -0.0169 0.0098  281 ILE B CB  
6428 C CG1 . ILE B 281 ? 0.2710 0.2988 0.3190 0.0518  -0.0239 0.0172  281 ILE B CG1 
6429 C CG2 . ILE B 281 ? 0.2338 0.2810 0.2904 0.0460  -0.0185 0.0097  281 ILE B CG2 
6430 C CD1 . ILE B 281 ? 0.2648 0.2875 0.2972 0.0403  -0.0279 0.0150  281 ILE B CD1 
6431 N N   . LEU B 282 ? 0.1982 0.2161 0.2567 0.0611  0.0018  -0.0052 282 LEU B N   
6432 C CA  . LEU B 282 ? 0.1753 0.1988 0.2358 0.0603  0.0092  -0.0121 282 LEU B CA  
6433 C C   . LEU B 282 ? 0.1991 0.2257 0.2734 0.0713  0.0171  -0.0138 282 LEU B C   
6434 O O   . LEU B 282 ? 0.2147 0.2581 0.2991 0.0732  0.0217  -0.0152 282 LEU B O   
6435 C CB  . LEU B 282 ? 0.2193 0.2282 0.2651 0.0540  0.0122  -0.0189 282 LEU B CB  
6436 C CG  . LEU B 282 ? 0.2320 0.2467 0.2763 0.0511  0.0199  -0.0262 282 LEU B CG  
6437 C CD1 . LEU B 282 ? 0.2515 0.2846 0.2983 0.0450  0.0182  -0.0239 282 LEU B CD1 
6438 C CD2 . LEU B 282 ? 0.2894 0.2915 0.3190 0.0444  0.0218  -0.0317 282 LEU B CD2 
6439 N N   . LYS B 283 ? 0.1886 0.1979 0.2636 0.0787  0.0199  -0.0136 283 LYS B N   
6440 C CA  . LYS B 283 ? 0.2485 0.2555 0.3370 0.0907  0.0294  -0.0155 283 LYS B CA  
6441 C C   . LYS B 283 ? 0.2819 0.3120 0.3915 0.1000  0.0271  -0.0057 283 LYS B C   
6442 O O   . LYS B 283 ? 0.2476 0.2868 0.3720 0.1089  0.0360  -0.0076 283 LYS B O   
6443 C CB  . LYS B 283 ? 0.2952 0.2758 0.3795 0.0958  0.0325  -0.0161 283 LYS B CB  
6444 C CG  . LYS B 283 ? 0.3817 0.3428 0.4469 0.0860  0.0363  -0.0268 283 LYS B CG  
6445 C CD  . LYS B 283 ? 0.4742 0.4111 0.5316 0.0862  0.0353  -0.0252 283 LYS B CD  
6446 C CE  . LYS B 283 ? 0.6570 0.5780 0.7255 0.0987  0.0437  -0.0240 283 LYS B CE  
6447 N NZ  . LYS B 283 ? 0.7366 0.6357 0.7958 0.0961  0.0407  -0.0208 283 LYS B NZ  
6448 N N   . ASN B 284 ? 0.2158 0.2572 0.3269 0.0974  0.0158  0.0048  284 ASN B N   
6449 C CA  . ASN B 284 ? 0.2488 0.3174 0.3794 0.1037  0.0116  0.0156  284 ASN B CA  
6450 C C   . ASN B 284 ? 0.1851 0.2797 0.3214 0.0971  0.0118  0.0135  284 ASN B C   
6451 O O   . ASN B 284 ? 0.2120 0.3332 0.3675 0.1027  0.0107  0.0212  284 ASN B O   
6452 C CB  . ASN B 284 ? 0.2096 0.2840 0.3366 0.0995  -0.0011 0.0268  284 ASN B CB  
6453 C CG  . ASN B 284 ? 0.2625 0.3195 0.3905 0.1085  -0.0019 0.0339  284 ASN B CG  
6454 O OD1 . ASN B 284 ? 0.2922 0.3348 0.4284 0.1202  0.0072  0.0325  284 ASN B OD1 
6455 N ND2 . ASN B 284 ? 0.3039 0.3613 0.4227 0.1025  -0.0122 0.0415  284 ASN B ND2 
6456 N N   . SER B 285 ? 0.1619 0.2508 0.2826 0.0851  0.0127  0.0047  285 SER B N   
6457 C CA  . SER B 285 ? 0.1961 0.3067 0.3183 0.0755  0.0112  0.0040  285 SER B CA  
6458 C C   . SER B 285 ? 0.2511 0.3648 0.3737 0.0748  0.0220  -0.0052 285 SER B C   
6459 O O   . SER B 285 ? 0.2788 0.4162 0.4106 0.0715  0.0236  -0.0041 285 SER B O   
6460 C CB  . SER B 285 ? 0.2388 0.3416 0.3426 0.0609  0.0031  0.0035  285 SER B CB  
6461 O OG  . SER B 285 ? 0.2431 0.3410 0.3427 0.0599  -0.0057 0.0100  285 SER B OG  
6462 N N   . VAL B 286 ? 0.2073 0.2990 0.3190 0.0762  0.0293  -0.0141 286 VAL B N   
6463 C CA  . VAL B 286 ? 0.2482 0.3410 0.3547 0.0726  0.0392  -0.0239 286 VAL B CA  
6464 C C   . VAL B 286 ? 0.3092 0.3867 0.4188 0.0832  0.0509  -0.0317 286 VAL B C   
6465 O O   . VAL B 286 ? 0.3622 0.4167 0.4654 0.0867  0.0502  -0.0325 286 VAL B O   
6466 C CB  . VAL B 286 ? 0.2585 0.3393 0.3434 0.0592  0.0360  -0.0279 286 VAL B CB  
6467 C CG1 . VAL B 286 ? 0.3500 0.4356 0.4281 0.0537  0.0453  -0.0366 286 VAL B CG1 
6468 C CG2 . VAL B 286 ? 0.2696 0.3588 0.3509 0.0496  0.0257  -0.0205 286 VAL B CG2 
6469 N N   . GLU B 287 ? 0.2706 0.3596 0.3889 0.0873  0.0627  -0.0381 287 GLU B N   
6470 C CA  . GLU B 287 ? 0.3537 0.4266 0.4757 0.0977  0.0764  -0.0470 287 GLU B CA  
6471 C C   . GLU B 287 ? 0.4232 0.4704 0.5214 0.0885  0.0804  -0.0586 287 GLU B C   
6472 O O   . GLU B 287 ? 0.4609 0.4829 0.5543 0.0925  0.0822  -0.0611 287 GLU B O   
6473 C CB  . GLU B 287 ? 0.3773 0.4703 0.5137 0.1035  0.0895  -0.0522 287 GLU B CB  
6474 C CG  . GLU B 287 ? 0.4901 0.6098 0.6539 0.1149  0.0872  -0.0403 287 GLU B CG  
6475 C CD  . GLU B 287 ? 0.6533 0.7792 0.8325 0.1271  0.1005  -0.0455 287 GLU B CD  
6476 O OE1 . GLU B 287 ? 0.7187 0.8333 0.8838 0.1237  0.1119  -0.0590 287 GLU B OE1 
6477 O OE2 . GLU B 287 ? 0.7281 0.8688 0.9283 0.1372  0.0967  -0.0362 287 GLU B OE2 
6478 N N   . ARG B 288 ? 0.3783 0.4328 0.4616 0.0752  0.0816  -0.0649 288 ARG B N   
6479 C CA  . ARG B 288 ? 0.4796 0.5160 0.5397 0.0638  0.0831  -0.0740 288 ARG B CA  
6480 C C   . ARG B 288 ? 0.4785 0.5102 0.5284 0.0560  0.0684  -0.0653 288 ARG B C   
6481 O O   . ARG B 288 ? 0.6319 0.6761 0.6749 0.0461  0.0617  -0.0610 288 ARG B O   
6482 C CB  . ARG B 288 ? 0.5418 0.5912 0.5907 0.0530  0.0907  -0.0829 288 ARG B CB  
6483 C CG  . ARG B 288 ? 0.5038 0.5539 0.5593 0.0599  0.1080  -0.0947 288 ARG B CG  
6484 C CD  . ARG B 288 ? 0.5441 0.6075 0.5847 0.0467  0.1152  -0.1038 288 ARG B CD  
6485 N NE  . ARG B 288 ? 0.5389 0.6317 0.5882 0.0439  0.1121  -0.0961 288 ARG B NE  
6486 C CZ  . ARG B 288 ? 0.4877 0.5990 0.5538 0.0516  0.1222  -0.0980 288 ARG B CZ  
6487 N NH1 . ARG B 288 ? 0.5574 0.6960 0.6302 0.0466  0.1184  -0.0904 288 ARG B NH1 
6488 N NH2 . ARG B 288 ? 0.4486 0.5487 0.5233 0.0641  0.1339  -0.1042 288 ARG B NH2 
6489 N N   . ALA B 289 ? 0.3754 0.3881 0.4249 0.0606  0.0641  -0.0624 289 ALA B N   
6490 C CA  . ALA B 289 ? 0.4007 0.4100 0.4451 0.0565  0.0511  -0.0530 289 ALA B CA  
6491 C C   . ALA B 289 ? 0.3476 0.3415 0.3737 0.0469  0.0494  -0.0575 289 ALA B C   
6492 O O   . ALA B 289 ? 0.5158 0.4913 0.5387 0.0491  0.0487  -0.0578 289 ALA B O   
6493 C CB  . ALA B 289 ? 0.5129 0.5163 0.5699 0.0674  0.0465  -0.0447 289 ALA B CB  
6494 N N   . SER B 290 ? 0.2550 0.2583 0.2693 0.0355  0.0482  -0.0594 290 SER B N   
6495 C CA  . SER B 290 ? 0.2354 0.2304 0.2344 0.0259  0.0443  -0.0603 290 SER B CA  
6496 C C   . SER B 290 ? 0.2540 0.2512 0.2535 0.0246  0.0331  -0.0491 290 SER B C   
6497 O O   . SER B 290 ? 0.2394 0.2496 0.2418 0.0227  0.0290  -0.0429 290 SER B O   
6498 C CB  . SER B 290 ? 0.2352 0.2409 0.2212 0.0140  0.0477  -0.0657 290 SER B CB  
6499 O OG  . SER B 290 ? 0.2308 0.2336 0.2048 0.0050  0.0418  -0.0633 290 SER B OG  
6500 N N   . PRO B 291 ? 0.2286 0.2126 0.2246 0.0249  0.0289  -0.0468 291 PRO B N   
6501 C CA  . PRO B 291 ? 0.2232 0.2083 0.2189 0.0238  0.0202  -0.0376 291 PRO B CA  
6502 C C   . PRO B 291 ? 0.2092 0.2023 0.1962 0.0148  0.0170  -0.0345 291 PRO B C   
6503 O O   . PRO B 291 ? 0.2250 0.2178 0.2125 0.0147  0.0114  -0.0271 291 PRO B O   
6504 C CB  . PRO B 291 ? 0.2756 0.2446 0.2708 0.0273  0.0188  -0.0373 291 PRO B CB  
6505 C CG  . PRO B 291 ? 0.2638 0.2231 0.2527 0.0245  0.0260  -0.0467 291 PRO B CG  
6506 C CD  . PRO B 291 ? 0.3058 0.2719 0.2981 0.0263  0.0334  -0.0531 291 PRO B CD  
6507 N N   . TYR B 292 ? 0.1825 0.1840 0.1620 0.0074  0.0207  -0.0392 292 TYR B N   
6508 C CA  . TYR B 292 ? 0.1816 0.1931 0.1532 -0.0014 0.0169  -0.0344 292 TYR B CA  
6509 C C   . TYR B 292 ? 0.1791 0.2056 0.1515 -0.0043 0.0151  -0.0274 292 TYR B C   
6510 O O   . TYR B 292 ? 0.2044 0.2421 0.1709 -0.0115 0.0122  -0.0217 292 TYR B O   
6511 C CB  . TYR B 292 ? 0.1998 0.2123 0.1595 -0.0107 0.0211  -0.0431 292 TYR B CB  
6512 C CG  . TYR B 292 ? 0.2149 0.2093 0.1738 -0.0084 0.0234  -0.0493 292 TYR B CG  
6513 C CD1 . TYR B 292 ? 0.2334 0.2201 0.1969 -0.0040 0.0180  -0.0427 292 TYR B CD1 
6514 C CD2 . TYR B 292 ? 0.3081 0.2913 0.2616 -0.0103 0.0320  -0.0618 292 TYR B CD2 
6515 C CE1 . TYR B 292 ? 0.2796 0.2496 0.2421 -0.0025 0.0200  -0.0469 292 TYR B CE1 
6516 C CE2 . TYR B 292 ? 0.3131 0.2764 0.2661 -0.0080 0.0345  -0.0662 292 TYR B CE2 
6517 C CZ  . TYR B 292 ? 0.3100 0.2677 0.2674 -0.0044 0.0279  -0.0580 292 TYR B CZ  
6518 O OH  . TYR B 292 ? 0.3497 0.2881 0.3061 -0.0030 0.0301  -0.0610 292 TYR B OH  
6519 N N   . LEU B 293 ? 0.1950 0.2228 0.1751 0.0005  0.0163  -0.0264 293 LEU B N   
6520 C CA  . LEU B 293 ? 0.1936 0.2336 0.1750 -0.0028 0.0154  -0.0199 293 LEU B CA  
6521 C C   . LEU B 293 ? 0.1857 0.2197 0.1736 0.0010  0.0102  -0.0108 293 LEU B C   
6522 O O   . LEU B 293 ? 0.1964 0.2193 0.1892 0.0071  0.0085  -0.0116 293 LEU B O   
6523 C CB  . LEU B 293 ? 0.1638 0.2114 0.1495 -0.0018 0.0214  -0.0259 293 LEU B CB  
6524 C CG  . LEU B 293 ? 0.3413 0.3984 0.3194 -0.0076 0.0289  -0.0348 293 LEU B CG  
6525 C CD1 . LEU B 293 ? 0.3755 0.4219 0.3469 -0.0080 0.0326  -0.0446 293 LEU B CD1 
6526 C CD2 . LEU B 293 ? 0.4005 0.4654 0.3871 -0.0039 0.0355  -0.0396 293 LEU B CD2 
6527 N N   . ARG B 294 ? 0.1526 0.1932 0.1397 -0.0032 0.0084  -0.0022 294 ARG B N   
6528 C CA  . ARG B 294 ? 0.1694 0.2026 0.1621 -0.0009 0.0061  0.0042  294 ARG B CA  
6529 C C   . ARG B 294 ? 0.1495 0.1887 0.1470 -0.0021 0.0085  0.0011  294 ARG B C   
6530 O O   . ARG B 294 ? 0.1867 0.2387 0.1825 -0.0074 0.0113  0.0013  294 ARG B O   
6531 C CB  . ARG B 294 ? 0.1666 0.2009 0.1576 -0.0043 0.0041  0.0158  294 ARG B CB  
6532 C CG  . ARG B 294 ? 0.2199 0.2406 0.2153 -0.0024 0.0034  0.0209  294 ARG B CG  
6533 C CD  . ARG B 294 ? 0.2436 0.2594 0.2393 -0.0026 0.0026  0.0333  294 ARG B CD  
6534 N NE  . ARG B 294 ? 0.2091 0.2385 0.2017 -0.0089 0.0028  0.0409  294 ARG B NE  
6535 C CZ  . ARG B 294 ? 0.2318 0.2710 0.2225 -0.0100 0.0009  0.0503  294 ARG B CZ  
6536 N NH1 . ARG B 294 ? 0.2271 0.2647 0.2202 -0.0048 -0.0012 0.0534  294 ARG B NH1 
6537 N NH2 . ARG B 294 ? 0.2506 0.3035 0.2371 -0.0170 0.0009  0.0577  294 ARG B NH2 
6538 N N   . TYR B 295 ? 0.1807 0.2132 0.1842 0.0019  0.0072  -0.0011 295 TYR B N   
6539 C CA  . TYR B 295 ? 0.1834 0.2252 0.1934 0.0005  0.0086  -0.0030 295 TYR B CA  
6540 C C   . TYR B 295 ? 0.1932 0.2314 0.2035 -0.0052 0.0066  0.0031  295 TYR B C   
6541 O O   . TYR B 295 ? 0.2058 0.2291 0.2128 -0.0052 0.0044  0.0067  295 TYR B O   
6542 C CB  . TYR B 295 ? 0.2141 0.2549 0.2311 0.0074  0.0079  -0.0081 295 TYR B CB  
6543 C CG  . TYR B 295 ? 0.1527 0.1969 0.1713 0.0127  0.0123  -0.0149 295 TYR B CG  
6544 C CD1 . TYR B 295 ? 0.1799 0.2124 0.1930 0.0158  0.0122  -0.0176 295 TYR B CD1 
6545 C CD2 . TYR B 295 ? 0.2165 0.2750 0.2421 0.0141  0.0177  -0.0190 295 TYR B CD2 
6546 C CE1 . TYR B 295 ? 0.1710 0.2026 0.1839 0.0192  0.0174  -0.0249 295 TYR B CE1 
6547 C CE2 . TYR B 295 ? 0.2113 0.2691 0.2380 0.0193  0.0238  -0.0265 295 TYR B CE2 
6548 C CZ  . TYR B 295 ? 0.1779 0.2207 0.1973 0.0214  0.0237  -0.0298 295 TYR B CZ  
6549 O OH  . TYR B 295 ? 0.2312 0.2696 0.2502 0.0252  0.0310  -0.0383 295 TYR B OH  
6550 N N   . TYR B 296 ? 0.1690 0.2203 0.1832 -0.0107 0.0084  0.0037  296 TYR B N   
6551 C CA  . TYR B 296 ? 0.1649 0.2130 0.1791 -0.0185 0.0071  0.0083  296 TYR B CA  
6552 C C   . TYR B 296 ? 0.1846 0.2454 0.2074 -0.0198 0.0061  0.0049  296 TYR B C   
6553 O O   . TYR B 296 ? 0.1807 0.2613 0.2105 -0.0202 0.0089  0.0030  296 TYR B O   
6554 C CB  . TYR B 296 ? 0.1677 0.2225 0.1786 -0.0265 0.0099  0.0144  296 TYR B CB  
6555 C CG  . TYR B 296 ? 0.1742 0.2216 0.1780 -0.0255 0.0100  0.0205  296 TYR B CG  
6556 C CD1 . TYR B 296 ? 0.2305 0.2590 0.2316 -0.0216 0.0079  0.0244  296 TYR B CD1 
6557 C CD2 . TYR B 296 ? 0.2152 0.2771 0.2153 -0.0289 0.0124  0.0228  296 TYR B CD2 
6558 C CE1 . TYR B 296 ? 0.2347 0.2609 0.2319 -0.0201 0.0076  0.0320  296 TYR B CE1 
6559 C CE2 . TYR B 296 ? 0.1920 0.2516 0.1857 -0.0291 0.0114  0.0300  296 TYR B CE2 
6560 C CZ  . TYR B 296 ? 0.2285 0.2713 0.2220 -0.0242 0.0086  0.0354  296 TYR B CZ  
6561 O OH  . TYR B 296 ? 0.3036 0.3483 0.2934 -0.0238 0.0070  0.0445  296 TYR B OH  
6562 N N   . PHE B 297 ? 0.1723 0.2237 0.1946 -0.0208 0.0023  0.0042  297 PHE B N   
6563 C CA  . PHE B 297 ? 0.1670 0.2337 0.1974 -0.0231 -0.0002 0.0026  297 PHE B CA  
6564 C C   . PHE B 297 ? 0.1930 0.2679 0.2238 -0.0361 0.0004  0.0055  297 PHE B C   
6565 O O   . PHE B 297 ? 0.1912 0.2498 0.2139 -0.0446 -0.0005 0.0069  297 PHE B O   
6566 C CB  . PHE B 297 ? 0.1563 0.2124 0.1838 -0.0216 -0.0049 0.0010  297 PHE B CB  
6567 C CG  . PHE B 297 ? 0.1566 0.2317 0.1921 -0.0254 -0.0090 0.0013  297 PHE B CG  
6568 C CD1 . PHE B 297 ? 0.1873 0.2818 0.2355 -0.0163 -0.0098 0.0017  297 PHE B CD1 
6569 C CD2 . PHE B 297 ? 0.1861 0.2605 0.2167 -0.0386 -0.0117 0.0017  297 PHE B CD2 
6570 C CE1 . PHE B 297 ? 0.1670 0.2834 0.2250 -0.0191 -0.0142 0.0043  297 PHE B CE1 
6571 C CE2 . PHE B 297 ? 0.2014 0.2979 0.2394 -0.0439 -0.0166 0.0029  297 PHE B CE2 
6572 C CZ  . PHE B 297 ? 0.1943 0.3139 0.2471 -0.0335 -0.0183 0.0052  297 PHE B CZ  
6573 N N   . ARG B 298 ? 0.1653 0.2644 0.2054 -0.0378 0.0029  0.0061  298 ARG B N   
6574 C CA  . ARG B 298 ? 0.1711 0.2824 0.2130 -0.0513 0.0039  0.0092  298 ARG B CA  
6575 C C   . ARG B 298 ? 0.1974 0.2888 0.2275 -0.0598 0.0062  0.0135  298 ARG B C   
6576 O O   . ARG B 298 ? 0.2080 0.2974 0.2352 -0.0730 0.0064  0.0163  298 ARG B O   
6577 C CB  . ARG B 298 ? 0.1742 0.2930 0.2192 -0.0597 -0.0013 0.0088  298 ARG B CB  
6578 C CG  . ARG B 298 ? 0.1921 0.3336 0.2509 -0.0507 -0.0044 0.0077  298 ARG B CG  
6579 C CD  . ARG B 298 ? 0.2089 0.3656 0.2716 -0.0610 -0.0106 0.0091  298 ARG B CD  
6580 N NE  . ARG B 298 ? 0.1884 0.3686 0.2664 -0.0501 -0.0138 0.0108  298 ARG B NE  
6581 C CZ  . ARG B 298 ? 0.1918 0.3864 0.2739 -0.0543 -0.0210 0.0133  298 ARG B CZ  
6582 N NH1 . ARG B 298 ? 0.2078 0.3952 0.2779 -0.0711 -0.0254 0.0123  298 ARG B NH1 
6583 N NH2 . ARG B 298 ? 0.1553 0.3711 0.2532 -0.0419 -0.0234 0.0172  298 ARG B NH2 
6584 N N   . GLU B 299 ? 0.1925 0.2697 0.2162 -0.0528 0.0082  0.0151  299 GLU B N   
6585 C CA  . GLU B 299 ? 0.2565 0.3151 0.2708 -0.0577 0.0102  0.0218  299 GLU B CA  
6586 C C   . GLU B 299 ? 0.2433 0.2751 0.2508 -0.0626 0.0091  0.0228  299 GLU B C   
6587 O O   . GLU B 299 ? 0.3337 0.3486 0.3352 -0.0684 0.0117  0.0293  299 GLU B O   
6588 C CB  . GLU B 299 ? 0.2176 0.2900 0.2320 -0.0681 0.0136  0.0274  299 GLU B CB  
6589 C CG  . GLU B 299 ? 0.2132 0.3094 0.2312 -0.0643 0.0169  0.0261  299 GLU B CG  
6590 C CD  . GLU B 299 ? 0.2864 0.3753 0.2969 -0.0583 0.0178  0.0294  299 GLU B CD  
6591 O OE1 . GLU B 299 ? 0.2753 0.3427 0.2810 -0.0535 0.0152  0.0322  299 GLU B OE1 
6592 O OE2 . GLU B 299 ? 0.2923 0.3987 0.3014 -0.0590 0.0213  0.0290  299 GLU B OE2 
6593 N N   . LEU B 300 ? 0.2009 0.2273 0.2086 -0.0601 0.0060  0.0167  300 LEU B N   
6594 C CA  . LEU B 300 ? 0.2204 0.2219 0.2201 -0.0661 0.0062  0.0149  300 LEU B CA  
6595 C C   . LEU B 300 ? 0.2284 0.2086 0.2235 -0.0555 0.0067  0.0136  300 LEU B C   
6596 O O   . LEU B 300 ? 0.2991 0.2533 0.2872 -0.0577 0.0101  0.0146  300 LEU B O   
6597 C CB  . LEU B 300 ? 0.2834 0.2956 0.2842 -0.0742 0.0023  0.0090  300 LEU B CB  
6598 C CG  . LEU B 300 ? 0.3367 0.3744 0.3441 -0.0859 0.0013  0.0102  300 LEU B CG  
6599 C CD1 . LEU B 300 ? 0.3372 0.3876 0.3459 -0.0934 -0.0039 0.0054  300 LEU B CD1 
6600 C CD2 . LEU B 300 ? 0.3322 0.3563 0.3333 -0.0991 0.0057  0.0146  300 LEU B CD2 
6601 N N   . ILE B 301 ? 0.2095 0.1993 0.2086 -0.0441 0.0042  0.0113  301 ILE B N   
6602 C CA  . ILE B 301 ? 0.1962 0.1690 0.1916 -0.0350 0.0045  0.0098  301 ILE B CA  
6603 C C   . ILE B 301 ? 0.1805 0.1653 0.1805 -0.0242 0.0033  0.0106  301 ILE B C   
6604 O O   . ILE B 301 ? 0.2029 0.2075 0.2086 -0.0226 0.0017  0.0084  301 ILE B O   
6605 C CB  . ILE B 301 ? 0.2469 0.2137 0.2381 -0.0372 0.0021  0.0030  301 ILE B CB  
6606 C CG1 . ILE B 301 ? 0.2344 0.1829 0.2210 -0.0288 0.0038  0.0014  301 ILE B CG1 
6607 C CG2 . ILE B 301 ? 0.2188 0.2104 0.2169 -0.0360 -0.0031 0.0001  301 ILE B CG2 
6608 C CD1 . ILE B 301 ? 0.3043 0.2449 0.2836 -0.0328 0.0025  -0.0054 301 ILE B CD1 
6609 N N   . SER B 302 ? 0.2057 0.1788 0.2035 -0.0173 0.0047  0.0137  302 SER B N   
6610 C CA  . SER B 302 ? 0.2072 0.1904 0.2073 -0.0095 0.0036  0.0139  302 SER B CA  
6611 C C   . SER B 302 ? 0.2468 0.2285 0.2473 -0.0035 0.0014  0.0078  302 SER B C   
6612 O O   . SER B 302 ? 0.2251 0.1932 0.2221 -0.0031 0.0013  0.0058  302 SER B O   
6613 C CB  . SER B 302 ? 0.2072 0.1836 0.2061 -0.0061 0.0053  0.0216  302 SER B CB  
6614 O OG  . SER B 302 ? 0.2551 0.2329 0.2535 -0.0118 0.0071  0.0292  302 SER B OG  
6615 N N   . VAL B 303 ? 0.1778 0.1723 0.1815 0.0007  0.0004  0.0046  303 VAL B N   
6616 C CA  . VAL B 303 ? 0.1733 0.1667 0.1780 0.0063  -0.0016 0.0001  303 VAL B CA  
6617 C C   . VAL B 303 ? 0.2327 0.2289 0.2372 0.0113  -0.0006 -0.0012 303 VAL B C   
6618 O O   . VAL B 303 ? 0.2065 0.2135 0.2124 0.0104  0.0014  -0.0022 303 VAL B O   
6619 C CB  . VAL B 303 ? 0.1643 0.1703 0.1752 0.0061  -0.0034 -0.0028 303 VAL B CB  
6620 C CG1 . VAL B 303 ? 0.2496 0.2533 0.2617 0.0126  -0.0056 -0.0051 303 VAL B CG1 
6621 C CG2 . VAL B 303 ? 0.1979 0.2043 0.2080 -0.0020 -0.0051 -0.0020 303 VAL B CG2 
6622 N N   . PHE B 304 ? 0.1765 0.1633 0.1783 0.0153  -0.0014 -0.0017 304 PHE B N   
6623 C CA  . PHE B 304 ? 0.1486 0.1369 0.1495 0.0185  -0.0008 -0.0042 304 PHE B CA  
6624 C C   . PHE B 304 ? 0.1796 0.1637 0.1820 0.0228  -0.0019 -0.0078 304 PHE B C   
6625 O O   . PHE B 304 ? 0.2108 0.1890 0.2125 0.0234  -0.0041 -0.0069 304 PHE B O   
6626 C CB  . PHE B 304 ? 0.1639 0.1474 0.1614 0.0188  -0.0008 -0.0006 304 PHE B CB  
6627 C CG  . PHE B 304 ? 0.1716 0.1626 0.1685 0.0154  -0.0001 0.0050  304 PHE B CG  
6628 C CD1 . PHE B 304 ? 0.1852 0.1874 0.1795 0.0121  0.0006  0.0037  304 PHE B CD1 
6629 C CD2 . PHE B 304 ? 0.1888 0.1746 0.1868 0.0151  0.0003  0.0120  304 PHE B CD2 
6630 C CE1 . PHE B 304 ? 0.1918 0.2038 0.1845 0.0080  0.0004  0.0105  304 PHE B CE1 
6631 C CE2 . PHE B 304 ? 0.1835 0.1768 0.1819 0.0127  0.0005  0.0199  304 PHE B CE2 
6632 C CZ  . PHE B 304 ? 0.1978 0.2059 0.1933 0.0088  -0.0001 0.0198  304 PHE B CZ  
6633 N N   . PHE B 305 ? 0.1974 0.1836 0.2010 0.0253  0.0000  -0.0117 305 PHE B N   
6634 C CA  . PHE B 305 ? 0.1743 0.1545 0.1800 0.0303  -0.0003 -0.0136 305 PHE B CA  
6635 C C   . PHE B 305 ? 0.1950 0.1661 0.1951 0.0300  0.0005  -0.0150 305 PHE B C   
6636 O O   . PHE B 305 ? 0.2172 0.1904 0.2140 0.0270  0.0032  -0.0180 305 PHE B O   
6637 C CB  . PHE B 305 ? 0.1621 0.1489 0.1750 0.0343  0.0029  -0.0169 305 PHE B CB  
6638 C CG  . PHE B 305 ? 0.2289 0.2289 0.2491 0.0338  0.0019  -0.0148 305 PHE B CG  
6639 C CD1 . PHE B 305 ? 0.2045 0.2144 0.2245 0.0290  0.0041  -0.0154 305 PHE B CD1 
6640 C CD2 . PHE B 305 ? 0.1727 0.1770 0.1992 0.0368  -0.0017 -0.0112 305 PHE B CD2 
6641 C CE1 . PHE B 305 ? 0.2160 0.2390 0.2426 0.0268  0.0033  -0.0133 305 PHE B CE1 
6642 C CE2 . PHE B 305 ? 0.1964 0.2160 0.2298 0.0345  -0.0032 -0.0090 305 PHE B CE2 
6643 C CZ  . PHE B 305 ? 0.2061 0.2345 0.2397 0.0293  -0.0004 -0.0104 305 PHE B CZ  
6644 N N   . ARG B 306 ? 0.1791 0.1418 0.1771 0.0317  -0.0018 -0.0128 306 ARG B N   
6645 C CA  . ARG B 306 ? 0.1950 0.1507 0.1880 0.0300  -0.0010 -0.0133 306 ARG B CA  
6646 C C   . ARG B 306 ? 0.2297 0.1795 0.2221 0.0308  0.0023  -0.0181 306 ARG B C   
6647 O O   . ARG B 306 ? 0.2248 0.1727 0.2223 0.0356  0.0041  -0.0196 306 ARG B O   
6648 C CB  . ARG B 306 ? 0.1739 0.1225 0.1643 0.0311  -0.0034 -0.0100 306 ARG B CB  
6649 C CG  . ARG B 306 ? 0.2359 0.1791 0.2280 0.0350  -0.0046 -0.0090 306 ARG B CG  
6650 C CD  . ARG B 306 ? 0.2470 0.1843 0.2340 0.0343  -0.0068 -0.0055 306 ARG B CD  
6651 N NE  . ARG B 306 ? 0.2829 0.2160 0.2719 0.0382  -0.0082 -0.0027 306 ARG B NE  
6652 C CZ  . ARG B 306 ? 0.2671 0.1924 0.2520 0.0380  -0.0090 0.0007  306 ARG B CZ  
6653 N NH1 . ARG B 306 ? 0.2644 0.1862 0.2425 0.0338  -0.0081 0.0006  306 ARG B NH1 
6654 N NH2 . ARG B 306 ? 0.2881 0.2102 0.2766 0.0426  -0.0104 0.0052  306 ARG B NH2 
6655 N N   . ASP B 307 ? 0.2137 0.1610 0.2005 0.0258  0.0038  -0.0203 307 ASP B N   
6656 C CA  . ASP B 307 ? 0.2091 0.1462 0.1928 0.0244  0.0080  -0.0259 307 ASP B CA  
6657 C C   . ASP B 307 ? 0.2213 0.1459 0.2052 0.0277  0.0067  -0.0225 307 ASP B C   
6658 O O   . ASP B 307 ? 0.2063 0.1293 0.1861 0.0241  0.0048  -0.0197 307 ASP B O   
6659 C CB  . ASP B 307 ? 0.2411 0.1819 0.2172 0.0149  0.0093  -0.0295 307 ASP B CB  
6660 C CG  . ASP B 307 ? 0.2867 0.2142 0.2573 0.0111  0.0150  -0.0376 307 ASP B CG  
6661 O OD1 . ASP B 307 ? 0.2605 0.1726 0.2321 0.0147  0.0165  -0.0372 307 ASP B OD1 
6662 O OD2 . ASP B 307 ? 0.3004 0.2319 0.2647 0.0037  0.0186  -0.0444 307 ASP B OD2 
6663 N N   . LYS B 308 ? 0.2244 0.1419 0.2137 0.0348  0.0080  -0.0217 308 LYS B N   
6664 C CA  . LYS B 308 ? 0.2410 0.1490 0.2307 0.0383  0.0057  -0.0158 308 LYS B CA  
6665 C C   . LYS B 308 ? 0.2330 0.1260 0.2160 0.0335  0.0087  -0.0177 308 LYS B C   
6666 O O   . LYS B 308 ? 0.2374 0.1260 0.2167 0.0316  0.0062  -0.0127 308 LYS B O   
6667 C CB  . LYS B 308 ? 0.1976 0.1043 0.1966 0.0476  0.0060  -0.0123 308 LYS B CB  
6668 C CG  . LYS B 308 ? 0.2685 0.1640 0.2683 0.0516  0.0045  -0.0051 308 LYS B CG  
6669 C CD  . LYS B 308 ? 0.3076 0.2070 0.3196 0.0619  0.0041  0.0006  308 LYS B CD  
6670 C CE  . LYS B 308 ? 0.4204 0.3070 0.4346 0.0673  0.0035  0.0095  308 LYS B CE  
6671 N NZ  . LYS B 308 ? 0.3776 0.2675 0.3837 0.0623  -0.0034 0.0168  308 LYS B NZ  
6672 N N   . THR B 309 ? 0.2112 0.0961 0.1916 0.0302  0.0147  -0.0255 309 THR B N   
6673 C CA  . THR B 309 ? 0.2378 0.1067 0.2107 0.0235  0.0181  -0.0283 309 THR B CA  
6674 C C   . THR B 309 ? 0.2551 0.1332 0.2213 0.0138  0.0144  -0.0266 309 THR B C   
6675 O O   . THR B 309 ? 0.2799 0.1509 0.2427 0.0107  0.0134  -0.0225 309 THR B O   
6676 C CB  . THR B 309 ? 0.2689 0.1276 0.2377 0.0193  0.0261  -0.0392 309 THR B CB  
6677 O OG1 . THR B 309 ? 0.3306 0.1784 0.3077 0.0302  0.0314  -0.0400 309 THR B OG1 
6678 C CG2 . THR B 309 ? 0.3447 0.1867 0.3034 0.0087  0.0298  -0.0434 309 THR B CG2 
6679 N N   . LEU B 310 ? 0.2332 0.1287 0.1985 0.0092  0.0126  -0.0287 310 LEU B N   
6680 C CA  . LEU B 310 ? 0.2014 0.1090 0.1635 0.0014  0.0095  -0.0257 310 LEU B CA  
6681 C C   . LEU B 310 ? 0.2285 0.1399 0.1941 0.0063  0.0057  -0.0176 310 LEU B C   
6682 O O   . LEU B 310 ? 0.2322 0.1460 0.1955 0.0014  0.0051  -0.0145 310 LEU B O   
6683 C CB  . LEU B 310 ? 0.2362 0.1631 0.1989 -0.0025 0.0080  -0.0267 310 LEU B CB  
6684 C CG  . LEU B 310 ? 0.2740 0.2008 0.2298 -0.0110 0.0118  -0.0355 310 LEU B CG  
6685 C CD1 . LEU B 310 ? 0.2824 0.2314 0.2387 -0.0147 0.0090  -0.0336 310 LEU B CD1 
6686 C CD2 . LEU B 310 ? 0.2687 0.1885 0.2162 -0.0227 0.0139  -0.0395 310 LEU B CD2 
6687 N N   . SER B 311 ? 0.2237 0.1370 0.1942 0.0147  0.0037  -0.0146 311 SER B N   
6688 C CA  . SER B 311 ? 0.2087 0.1246 0.1799 0.0180  0.0010  -0.0087 311 SER B CA  
6689 C C   . SER B 311 ? 0.2444 0.1480 0.2120 0.0179  0.0011  -0.0053 311 SER B C   
6690 O O   . SER B 311 ? 0.2790 0.1847 0.2435 0.0154  0.0006  -0.0017 311 SER B O   
6691 C CB  . SER B 311 ? 0.2146 0.1348 0.1901 0.0244  -0.0010 -0.0074 311 SER B CB  
6692 O OG  . SER B 311 ? 0.2151 0.1457 0.1937 0.0240  -0.0009 -0.0094 311 SER B OG  
6693 N N   . ASP B 312 ? 0.2346 0.1251 0.2030 0.0211  0.0025  -0.0058 312 ASP B N   
6694 C CA  . ASP B 312 ? 0.2560 0.1333 0.2211 0.0213  0.0025  -0.0005 312 ASP B CA  
6695 C C   . ASP B 312 ? 0.2646 0.1349 0.2235 0.0119  0.0053  -0.0020 312 ASP B C   
6696 O O   . ASP B 312 ? 0.2552 0.1197 0.2098 0.0092  0.0049  0.0035  312 ASP B O   
6697 C CB  . ASP B 312 ? 0.2726 0.1368 0.2426 0.0285  0.0042  0.0007  312 ASP B CB  
6698 C CG  . ASP B 312 ? 0.2717 0.1451 0.2483 0.0371  0.0001  0.0060  312 ASP B CG  
6699 O OD1 . ASP B 312 ? 0.3161 0.2017 0.2906 0.0358  -0.0042 0.0087  312 ASP B OD1 
6700 O OD2 . ASP B 312 ? 0.3279 0.1966 0.3122 0.0446  0.0016  0.0072  312 ASP B OD2 
6701 N N   . LEU B 313 ? 0.2796 0.1512 0.2371 0.0055  0.0082  -0.0091 313 LEU B N   
6702 C CA  . LEU B 313 ? 0.2543 0.1214 0.2054 -0.0058 0.0105  -0.0108 313 LEU B CA  
6703 C C   . LEU B 313 ? 0.2709 0.1532 0.2215 -0.0098 0.0081  -0.0056 313 LEU B C   
6704 O O   . LEU B 313 ? 0.2502 0.1268 0.1965 -0.0155 0.0090  -0.0020 313 LEU B O   
6705 C CB  . LEU B 313 ? 0.2384 0.1091 0.1868 -0.0140 0.0131  -0.0196 313 LEU B CB  
6706 C CG  . LEU B 313 ? 0.3020 0.1511 0.2473 -0.0140 0.0190  -0.0271 313 LEU B CG  
6707 C CD1 . LEU B 313 ? 0.3356 0.1935 0.2775 -0.0210 0.0212  -0.0365 313 LEU B CD1 
6708 C CD2 . LEU B 313 ? 0.3570 0.1827 0.2956 -0.0209 0.0234  -0.0277 313 LEU B CD2 
6709 N N   . ILE B 314 ? 0.2161 0.1173 0.1716 -0.0066 0.0058  -0.0048 314 ILE B N   
6710 C CA  . ILE B 314 ? 0.2463 0.1614 0.2032 -0.0083 0.0054  0.0000  314 ILE B CA  
6711 C C   . ILE B 314 ? 0.2477 0.1560 0.2018 -0.0035 0.0049  0.0049  314 ILE B C   
6712 O O   . ILE B 314 ? 0.2465 0.1564 0.1972 -0.0079 0.0063  0.0085  314 ILE B O   
6713 C CB  . ILE B 314 ? 0.1973 0.1312 0.1612 -0.0046 0.0044  0.0003  314 ILE B CB  
6714 C CG1 . ILE B 314 ? 0.1845 0.1292 0.1500 -0.0113 0.0040  -0.0026 314 ILE B CG1 
6715 C CG2 . ILE B 314 ? 0.1876 0.1337 0.1547 -0.0035 0.0060  0.0050  314 ILE B CG2 
6716 C CD1 . ILE B 314 ? 0.2400 0.2028 0.2131 -0.0069 0.0026  -0.0001 314 ILE B CD1 
6717 N N   . GLY B 315 ? 0.2155 0.1180 0.1703 0.0043  0.0029  0.0053  315 GLY B N   
6718 C CA  . GLY B 315 ? 0.2389 0.1400 0.1900 0.0074  0.0016  0.0100  315 GLY B CA  
6719 C C   . GLY B 315 ? 0.2948 0.1830 0.2399 0.0049  0.0012  0.0155  315 GLY B C   
6720 O O   . GLY B 315 ? 0.2961 0.1861 0.2354 0.0034  0.0008  0.0202  315 GLY B O   
6721 N N   . PHE B 316 ? 0.2982 0.1721 0.2439 0.0041  0.0022  0.0151  316 PHE B N   
6722 C CA  . PHE B 316 ? 0.3092 0.1671 0.2503 0.0032  0.0022  0.0221  316 PHE B CA  
6723 C C   . PHE B 316 ? 0.3879 0.2301 0.3261 -0.0044 0.0063  0.0204  316 PHE B C   
6724 O O   . PHE B 316 ? 0.3865 0.2148 0.3199 -0.0071 0.0071  0.0273  316 PHE B O   
6725 C CB  . PHE B 316 ? 0.3435 0.1939 0.2893 0.0130  -0.0004 0.0263  316 PHE B CB  
6726 C CG  . PHE B 316 ? 0.4328 0.2980 0.3798 0.0181  -0.0050 0.0287  316 PHE B CG  
6727 C CD1 . PHE B 316 ? 0.4224 0.2922 0.3626 0.0165  -0.0081 0.0364  316 PHE B CD1 
6728 C CD2 . PHE B 316 ? 0.3236 0.1985 0.2770 0.0227  -0.0059 0.0228  316 PHE B CD2 
6729 C CE1 . PHE B 316 ? 0.4625 0.3456 0.4014 0.0185  -0.0120 0.0372  316 PHE B CE1 
6730 C CE2 . PHE B 316 ? 0.3912 0.2785 0.3444 0.0251  -0.0098 0.0242  316 PHE B CE2 
6731 C CZ  . PHE B 316 ? 0.4139 0.3050 0.3595 0.0226  -0.0128 0.0309  316 PHE B CZ  
6732 N N   . SER B 317 ? 0.3184 0.1619 0.2581 -0.0094 0.0090  0.0118  317 SER B N   
6733 C CA  . SER B 317 ? 0.3770 0.2028 0.3122 -0.0183 0.0135  0.0083  317 SER B CA  
6734 C C   . SER B 317 ? 0.3413 0.1768 0.2717 -0.0322 0.0148  0.0072  317 SER B C   
6735 O O   . SER B 317 ? 0.3259 0.1480 0.2502 -0.0405 0.0172  0.0104  317 SER B O   
6736 C CB  . SER B 317 ? 0.3797 0.1999 0.3173 -0.0173 0.0165  -0.0016 317 SER B CB  
6737 O OG  . SER B 317 ? 0.4321 0.2418 0.3754 -0.0047 0.0169  -0.0004 317 SER B OG  
6738 N N   . TYR B 318 ? 0.2655 0.1251 0.1996 -0.0348 0.0132  0.0037  318 TYR B N   
6739 C CA  . TYR B 318 ? 0.2677 0.1404 0.2001 -0.0485 0.0144  0.0018  318 TYR B CA  
6740 C C   . TYR B 318 ? 0.3104 0.1912 0.2410 -0.0541 0.0149  0.0089  318 TYR B C   
6741 O O   . TYR B 318 ? 0.3304 0.2218 0.2599 -0.0669 0.0162  0.0084  318 TYR B O   
6742 C CB  . TYR B 318 ? 0.2512 0.1501 0.1906 -0.0476 0.0121  -0.0012 318 TYR B CB  
6743 C CG  . TYR B 318 ? 0.2855 0.1811 0.2242 -0.0484 0.0123  -0.0093 318 TYR B CG  
6744 C CD1 . TYR B 318 ? 0.2900 0.1634 0.2208 -0.0560 0.0161  -0.0162 318 TYR B CD1 
6745 C CD2 . TYR B 318 ? 0.2326 0.1461 0.1777 -0.0422 0.0097  -0.0102 318 TYR B CD2 
6746 C CE1 . TYR B 318 ? 0.3085 0.1795 0.2371 -0.0577 0.0177  -0.0250 318 TYR B CE1 
6747 C CE2 . TYR B 318 ? 0.2545 0.1674 0.1978 -0.0442 0.0102  -0.0173 318 TYR B CE2 
6748 C CZ  . TYR B 318 ? 0.3310 0.2233 0.2656 -0.0520 0.0143  -0.0252 318 TYR B CZ  
6749 O OH  . TYR B 318 ? 0.2901 0.1828 0.2217 -0.0544 0.0159  -0.0334 318 TYR B OH  
6750 N N   . HIS B 319 ? 0.3196 0.1985 0.2496 -0.0462 0.0141  0.0154  319 HIS B N   
6751 C CA  . HIS B 319 ? 0.2747 0.1574 0.2003 -0.0531 0.0158  0.0220  319 HIS B CA  
6752 C C   . HIS B 319 ? 0.2995 0.1622 0.2174 -0.0654 0.0184  0.0233  319 HIS B C   
6753 O O   . HIS B 319 ? 0.3742 0.2449 0.2894 -0.0768 0.0205  0.0265  319 HIS B O   
6754 C CB  . HIS B 319 ? 0.3064 0.1858 0.2287 -0.0445 0.0145  0.0285  319 HIS B CB  
6755 C CG  . HIS B 319 ? 0.3089 0.1627 0.2260 -0.0409 0.0132  0.0333  319 HIS B CG  
6756 N ND1 . HIS B 319 ? 0.3810 0.2208 0.2902 -0.0470 0.0144  0.0415  319 HIS B ND1 
6757 C CD2 . HIS B 319 ? 0.3632 0.2039 0.2833 -0.0311 0.0111  0.0322  319 HIS B CD2 
6758 C CE1 . HIS B 319 ? 0.3786 0.1973 0.2869 -0.0401 0.0129  0.0462  319 HIS B CE1 
6759 N NE2 . HIS B 319 ? 0.3545 0.1742 0.2701 -0.0302 0.0111  0.0404  319 HIS B NE2 
6760 N N   . ALA B 320 ? 0.3234 0.1596 0.2382 -0.0634 0.0192  0.0208  320 ALA B N   
6761 C CA  . ALA B 320 ? 0.3859 0.1958 0.2928 -0.0740 0.0231  0.0216  320 ALA B CA  
6762 C C   . ALA B 320 ? 0.4104 0.2197 0.3146 -0.0887 0.0260  0.0119  320 ALA B C   
6763 O O   . ALA B 320 ? 0.4366 0.2199 0.3331 -0.0988 0.0304  0.0099  320 ALA B O   
6764 C CB  . ALA B 320 ? 0.4033 0.1831 0.3097 -0.0632 0.0241  0.0241  320 ALA B CB  
6765 N N   . TRP B 321 ? 0.3835 0.2204 0.2933 -0.0907 0.0237  0.0063  321 TRP B N   
6766 C CA  . TRP B 321 ? 0.4283 0.2716 0.3351 -0.1057 0.0250  -0.0025 321 TRP B CA  
6767 C C   . TRP B 321 ? 0.4052 0.2833 0.3164 -0.1166 0.0229  0.0008  321 TRP B C   
6768 O O   . TRP B 321 ? 0.3779 0.2787 0.2974 -0.1082 0.0208  0.0076  321 TRP B O   
6769 C CB  . TRP B 321 ? 0.3695 0.2201 0.2800 -0.0991 0.0234  -0.0107 321 TRP B CB  
6770 C CG  . TRP B 321 ? 0.3746 0.1981 0.2837 -0.0875 0.0259  -0.0152 321 TRP B CG  
6771 C CD1 . TRP B 321 ? 0.3530 0.1606 0.2653 -0.0723 0.0258  -0.0090 321 TRP B CD1 
6772 C CD2 . TRP B 321 ? 0.4174 0.2304 0.3226 -0.0903 0.0291  -0.0266 321 TRP B CD2 
6773 N NE1 . TRP B 321 ? 0.4924 0.2810 0.4053 -0.0640 0.0288  -0.0152 321 TRP B NE1 
6774 C CE2 . TRP B 321 ? 0.4763 0.2667 0.3844 -0.0748 0.0316  -0.0267 321 TRP B CE2 
6775 C CE3 . TRP B 321 ? 0.4539 0.2766 0.3530 -0.1051 0.0301  -0.0365 321 TRP B CE3 
6776 C CZ2 . TRP B 321 ? 0.5345 0.3103 0.4403 -0.0727 0.0366  -0.0372 321 TRP B CZ2 
6777 C CZ3 . TRP B 321 ? 0.4581 0.2653 0.3524 -0.1044 0.0347  -0.0476 321 TRP B CZ3 
6778 C CH2 . TRP B 321 ? 0.4526 0.2360 0.3506 -0.0878 0.0385  -0.0483 321 TRP B CH2 
6779 N N   . ASN B 322 ? 0.4390 0.3227 0.3452 -0.1356 0.0240  -0.0043 322 ASN B N   
6780 C CA  . ASN B 322 ? 0.4679 0.3924 0.3820 -0.1445 0.0210  -0.0010 322 ASN B CA  
6781 C C   . ASN B 322 ? 0.3873 0.3375 0.3112 -0.1349 0.0167  -0.0025 322 ASN B C   
6782 O O   . ASN B 322 ? 0.4712 0.4080 0.3913 -0.1303 0.0164  -0.0098 322 ASN B O   
6783 C CB  . ASN B 322 ? 0.6891 0.6164 0.5949 -0.1698 0.0224  -0.0055 322 ASN B CB  
6784 C CG  . ASN B 322 ? 0.8169 0.7898 0.7317 -0.1791 0.0178  -0.0040 322 ASN B CG  
6785 O OD1 . ASN B 322 ? 0.9191 0.9230 0.8443 -0.1813 0.0166  0.0047  322 ASN B OD1 
6786 N ND2 . ASN B 322 ? 0.7707 0.7496 0.6822 -0.1845 0.0154  -0.0117 322 ASN B ND2 
6787 N N   . ALA B 323 ? 0.3886 0.3200 0.3200 -0.1218 -0.0121 -0.0080 323 ALA B N   
6788 C CA  . ALA B 323 ? 0.3783 0.3341 0.3193 -0.1090 -0.0157 -0.0083 323 ALA B CA  
6789 C C   . ALA B 323 ? 0.4082 0.3654 0.3409 -0.1175 -0.0184 -0.0168 323 ALA B C   
6790 O O   . ALA B 323 ? 0.3332 0.2856 0.2649 -0.1059 -0.0185 -0.0205 323 ALA B O   
6791 C CB  . ALA B 323 ? 0.4010 0.3981 0.3579 -0.1065 -0.0184 0.0002  323 ALA B CB  
6792 N N   . GLU B 324 ? 0.3913 0.3576 0.3179 -0.1389 -0.0207 -0.0200 324 GLU B N   
6793 C CA  . GLU B 324 ? 0.3600 0.3296 0.2764 -0.1488 -0.0236 -0.0287 324 GLU B CA  
6794 C C   . GLU B 324 ? 0.4420 0.3707 0.3436 -0.1414 -0.0182 -0.0379 324 GLU B C   
6795 O O   . GLU B 324 ? 0.3616 0.2926 0.2592 -0.1362 -0.0193 -0.0431 324 GLU B O   
6796 C CB  . GLU B 324 ? 0.4792 0.4619 0.3912 -0.1663 -0.0241 -0.0294 324 GLU B CB  
6797 C CG  . GLU B 324 ? 0.6661 0.6535 0.5672 -0.1736 -0.0256 -0.0371 324 GLU B CG  
6798 C CD  . GLU B 324 ? 0.8506 0.8850 0.7623 -0.1726 -0.0325 -0.0320 324 GLU B CD  
6799 O OE1 . GLU B 324 ? 0.8909 0.9286 0.7962 -0.1701 -0.0341 -0.0367 324 GLU B OE1 
6800 O OE2 . GLU B 324 ? 0.9176 0.9865 0.8444 -0.1727 -0.0358 -0.0223 324 GLU B OE2 
6801 N N   . ASP B 325 ? 0.4028 0.2963 0.2972 -0.1394 -0.0119 -0.0387 325 ASP B N   
6802 C CA  . ASP B 325 ? 0.4157 0.2740 0.2986 -0.1299 -0.0059 -0.0458 325 ASP B CA  
6803 C C   . ASP B 325 ? 0.3377 0.1899 0.2256 -0.1110 -0.0051 -0.0452 325 ASP B C   
6804 O O   . ASP B 325 ? 0.3932 0.2348 0.2753 -0.1030 -0.0025 -0.0514 325 ASP B O   
6805 C CB  . ASP B 325 ? 0.4840 0.3106 0.3598 -0.1310 0.0005  -0.0446 325 ASP B CB  
6806 C CG  . ASP B 325 ? 0.6055 0.4358 0.4746 -0.1511 0.0003  -0.0460 325 ASP B CG  
6807 O OD1 . ASP B 325 ? 0.6684 0.5120 0.5317 -0.1621 -0.0020 -0.0523 325 ASP B OD1 
6808 O OD2 . ASP B 325 ? 0.6287 0.4497 0.4980 -0.1562 0.0027  -0.0405 325 ASP B OD2 
6809 N N   . ALA B 326 ? 0.3165 0.1789 0.2167 -0.1018 -0.0068 -0.0367 326 ALA B N   
6810 C CA  . ALA B 326 ? 0.3176 0.1829 0.2268 -0.0808 -0.0061 -0.0339 326 ALA B CA  
6811 C C   . ALA B 326 ? 0.3353 0.2242 0.2486 -0.0772 -0.0095 -0.0364 326 ALA B C   
6812 O O   . ALA B 326 ? 0.3231 0.2036 0.2345 -0.0665 -0.0072 -0.0400 326 ALA B O   
6813 C CB  . ALA B 326 ? 0.3551 0.2349 0.2784 -0.0711 -0.0072 -0.0237 326 ALA B CB  
6814 N N   . VAL B 327 ? 0.3502 0.2703 0.2693 -0.0857 -0.0148 -0.0332 327 VAL B N   
6815 C CA  . VAL B 327 ? 0.3328 0.2762 0.2550 -0.0820 -0.0181 -0.0334 327 VAL B CA  
6816 C C   . VAL B 327 ? 0.3582 0.2886 0.2641 -0.0902 -0.0170 -0.0440 327 VAL B C   
6817 O O   . VAL B 327 ? 0.3335 0.2663 0.2379 -0.0817 -0.0162 -0.0460 327 VAL B O   
6818 C CB  . VAL B 327 ? 0.2621 0.2439 0.1946 -0.0878 -0.0236 -0.0260 327 VAL B CB  
6819 C CG1 . VAL B 327 ? 0.2756 0.2812 0.2083 -0.0860 -0.0272 -0.0253 327 VAL B CG1 
6820 C CG2 . VAL B 327 ? 0.2538 0.2470 0.2017 -0.0755 -0.0230 -0.0164 327 VAL B CG2 
6821 N N   . ARG B 328 ? 0.3100 0.2250 0.2020 -0.1076 -0.0162 -0.0512 328 ARG B N   
6822 C CA  . ARG B 328 ? 0.3066 0.2084 0.1837 -0.1122 -0.0133 -0.0609 328 ARG B CA  
6823 C C   . ARG B 328 ? 0.3567 0.2291 0.2293 -0.0967 -0.0062 -0.0653 328 ARG B C   
6824 O O   . ARG B 328 ? 0.3421 0.2148 0.2086 -0.0923 -0.0045 -0.0705 328 ARG B O   
6825 C CB  . ARG B 328 ? 0.3760 0.2673 0.2443 -0.1270 -0.0112 -0.0645 328 ARG B CB  
6826 C CG  . ARG B 328 ? 0.5078 0.3867 0.3612 -0.1316 -0.0078 -0.0741 328 ARG B CG  
6827 C CD  . ARG B 328 ? 0.5994 0.4648 0.4421 -0.1476 -0.0053 -0.0782 328 ARG B CD  
6828 N NE  . ARG B 328 ? 0.6579 0.4913 0.4995 -0.1435 0.0007  -0.0768 328 ARG B NE  
6829 C CZ  . ARG B 328 ? 0.6622 0.4968 0.5079 -0.1519 -0.0002 -0.0711 328 ARG B CZ  
6830 N NH1 . ARG B 328 ? 0.6022 0.4700 0.4546 -0.1649 -0.0066 -0.0666 328 ARG B NH1 
6831 N NH2 . ARG B 328 ? 0.7686 0.5730 0.6121 -0.1467 0.0056  -0.0691 328 ARG B NH2 
6832 N N   . ASP B 329 ? 0.3676 0.2180 0.2443 -0.0875 -0.0019 -0.0620 329 ASP B N   
6833 C CA  . ASP B 329 ? 0.3883 0.2177 0.2648 -0.0707 0.0045  -0.0637 329 ASP B CA  
6834 C C   . ASP B 329 ? 0.3760 0.2191 0.2585 -0.0594 0.0032  -0.0627 329 ASP B C   
6835 O O   . ASP B 329 ? 0.3574 0.1960 0.2365 -0.0512 0.0072  -0.0671 329 ASP B O   
6836 C CB  . ASP B 329 ? 0.3798 0.1912 0.2619 -0.0622 0.0077  -0.0575 329 ASP B CB  
6837 C CG  . ASP B 329 ? 0.4297 0.2259 0.3142 -0.0442 0.0137  -0.0576 329 ASP B CG  
6838 O OD1 . ASP B 329 ? 0.4313 0.2095 0.3074 -0.0431 0.0190  -0.0624 329 ASP B OD1 
6839 O OD2 . ASP B 329 ? 0.4205 0.2244 0.3153 -0.0314 0.0131  -0.0527 329 ASP B OD2 
6840 N N   . PHE B 330 ? 0.3209 0.1898 0.2188 -0.0556 -0.0020 -0.0534 330 PHE B N   
6841 C CA  . PHE B 330 ? 0.3296 0.2163 0.2394 -0.0423 -0.0028 -0.0486 330 PHE B CA  
6842 C C   . PHE B 330 ? 0.3492 0.2508 0.2532 -0.0456 -0.0041 -0.0520 330 PHE B C   
6843 O O   . PHE B 330 ? 0.2942 0.1937 0.1974 -0.0369 -0.0006 -0.0541 330 PHE B O   
6844 C CB  . PHE B 330 ? 0.2663 0.1744 0.1916 -0.0387 -0.0072 -0.0386 330 PHE B CB  
6845 C CG  . PHE B 330 ? 0.2597 0.1793 0.1965 -0.0256 -0.0068 -0.0338 330 PHE B CG  
6846 C CD1 . PHE B 330 ? 0.2990 0.2085 0.2418 -0.0148 -0.0040 -0.0324 330 PHE B CD1 
6847 C CD2 . PHE B 330 ? 0.2897 0.2304 0.2306 -0.0246 -0.0092 -0.0302 330 PHE B CD2 
6848 C CE1 . PHE B 330 ? 0.2542 0.1742 0.2066 -0.0057 -0.0036 -0.0289 330 PHE B CE1 
6849 C CE2 . PHE B 330 ? 0.2871 0.2343 0.2370 -0.0142 -0.0080 -0.0260 330 PHE B CE2 
6850 C CZ  . PHE B 330 ? 0.2634 0.2001 0.2188 -0.0059 -0.0052 -0.0261 330 PHE B CZ  
6851 N N   . ILE B 331 ? 0.2738 0.1931 0.1737 -0.0585 -0.0092 -0.0519 331 ILE B N   
6852 C CA  . ILE B 331 ? 0.3042 0.2396 0.1962 -0.0628 -0.0110 -0.0545 331 ILE B CA  
6853 C C   . ILE B 331 ? 0.3251 0.2375 0.1990 -0.0659 -0.0054 -0.0667 331 ILE B C   
6854 O O   . ILE B 331 ? 0.3216 0.2398 0.1906 -0.0614 -0.0034 -0.0688 331 ILE B O   
6855 C CB  . ILE B 331 ? 0.3545 0.3159 0.2449 -0.0773 -0.0181 -0.0520 331 ILE B CB  
6856 C CG1 . ILE B 331 ? 0.3444 0.3286 0.2533 -0.0718 -0.0221 -0.0397 331 ILE B CG1 
6857 C CG2 . ILE B 331 ? 0.3481 0.3296 0.2294 -0.0814 -0.0208 -0.0534 331 ILE B CG2 
6858 C CD1 . ILE B 331 ? 0.3018 0.3023 0.2217 -0.0571 -0.0222 -0.0307 331 ILE B CD1 
6859 N N   . GLY B 332 ? 0.3234 0.2083 0.1865 -0.0730 -0.0017 -0.0745 332 GLY B N   
6860 C CA  . GLY B 332 ? 0.3716 0.2381 0.2243 -0.0705 0.0049  -0.0825 332 GLY B CA  
6861 C C   . GLY B 332 ? 0.3170 0.1728 0.1732 -0.0532 0.0114  -0.0830 332 GLY B C   
6862 O O   . GLY B 332 ? 0.3986 0.2524 0.2470 -0.0499 0.0157  -0.0886 332 GLY B O   
6863 N N   . ARG B 333 ? 0.3163 0.1676 0.1849 -0.0421 0.0123  -0.0768 333 ARG B N   
6864 C CA  . ARG B 333 ? 0.3594 0.2073 0.2345 -0.0258 0.0179  -0.0758 333 ARG B CA  
6865 C C   . ARG B 333 ? 0.3491 0.2212 0.2285 -0.0227 0.0163  -0.0727 333 ARG B C   
6866 O O   . ARG B 333 ? 0.3354 0.2069 0.2122 -0.0151 0.0220  -0.0759 333 ARG B O   
6867 C CB  . ARG B 333 ? 0.2978 0.1407 0.1871 -0.0153 0.0180  -0.0683 333 ARG B CB  
6868 C CG  . ARG B 333 ? 0.3181 0.1412 0.2075 -0.0134 0.0209  -0.0678 333 ARG B CG  
6869 C CD  . ARG B 333 ? 0.3186 0.1413 0.2198 -0.0072 0.0187  -0.0592 333 ARG B CD  
6870 N NE  . ARG B 333 ? 0.3767 0.1810 0.2764 -0.0065 0.0212  -0.0572 333 ARG B NE  
6871 C CZ  . ARG B 333 ? 0.4494 0.2427 0.3515 0.0054  0.0265  -0.0560 333 ARG B CZ  
6872 N NH1 . ARG B 333 ? 0.4323 0.2338 0.3398 0.0170  0.0297  -0.0570 333 ARG B NH1 
6873 N NH2 . ARG B 333 ? 0.4353 0.2101 0.3340 0.0057  0.0289  -0.0534 333 ARG B NH2 
6874 N N   . LEU B 334 ? 0.3170 0.2128 0.2046 -0.0276 0.0090  -0.0651 334 LEU B N   
6875 C CA  . LEU B 334 ? 0.2424 0.1608 0.1338 -0.0249 0.0076  -0.0601 334 LEU B CA  
6876 C C   . LEU B 334 ? 0.3009 0.2216 0.1744 -0.0321 0.0094  -0.0677 334 LEU B C   
6877 O O   . LEU B 334 ? 0.3281 0.2572 0.2003 -0.0267 0.0127  -0.0668 334 LEU B O   
6878 C CB  . LEU B 334 ? 0.2308 0.1716 0.1324 -0.0277 0.0003  -0.0500 334 LEU B CB  
6879 C CG  . LEU B 334 ? 0.2651 0.2071 0.1836 -0.0201 -0.0011 -0.0422 334 LEU B CG  
6880 C CD1 . LEU B 334 ? 0.2385 0.2020 0.1650 -0.0220 -0.0067 -0.0330 334 LEU B CD1 
6881 C CD2 . LEU B 334 ? 0.2443 0.1848 0.1716 -0.0088 0.0033  -0.0398 334 LEU B CD2 
6882 N N   . LYS B 335 ? 0.2925 0.2065 0.1510 -0.0455 0.0074  -0.0753 335 LYS B N   
6883 C CA  . LYS B 335 ? 0.3690 0.2846 0.2074 -0.0541 0.0091  -0.0843 335 LYS B CA  
6884 C C   . LYS B 335 ? 0.3633 0.2599 0.1957 -0.0445 0.0188  -0.0918 335 LYS B C   
6885 O O   . LYS B 335 ? 0.3781 0.2838 0.2022 -0.0430 0.0218  -0.0940 335 LYS B O   
6886 C CB  . LYS B 335 ? 0.3262 0.2393 0.1561 -0.0693 0.0050  -0.0892 335 LYS B CB  
6887 C CG  . LYS B 335 ? 0.4287 0.3412 0.2433 -0.0757 0.0072  -0.0972 335 LYS B CG  
6888 C CD  . LYS B 335 ? 0.5300 0.4444 0.3385 -0.0921 0.0026  -0.1003 335 LYS B CD  
6889 C CE  . LYS B 335 ? 0.6284 0.5375 0.4199 -0.0991 0.0057  -0.1099 335 LYS B CE  
6890 N NZ  . LYS B 335 ? 0.7501 0.6273 0.5341 -0.1029 0.0115  -0.1185 335 LYS B NZ  
6891 N N   . LYS B 336 ? 0.3643 0.2382 0.2033 -0.0362 0.0236  -0.0933 336 LYS B N   
6892 C CA  . LYS B 336 ? 0.4293 0.2897 0.2669 -0.0249 0.0324  -0.0982 336 LYS B CA  
6893 C C   . LYS B 336 ? 0.3667 0.2394 0.2116 -0.0130 0.0369  -0.0943 336 LYS B C   
6894 O O   . LYS B 336 ? 0.4281 0.3030 0.2671 -0.0079 0.0431  -0.0984 336 LYS B O   
6895 C CB  . LYS B 336 ? 0.4776 0.3155 0.3223 -0.0180 0.0355  -0.0979 336 LYS B CB  
6896 C CG  . LYS B 336 ? 0.5470 0.3669 0.3802 -0.0289 0.0351  -0.1038 336 LYS B CG  
6897 C CD  . LYS B 336 ? 0.6912 0.4909 0.5318 -0.0237 0.0370  -0.1004 336 LYS B CD  
6898 C CE  . LYS B 336 ? 0.8230 0.6041 0.6511 -0.0369 0.0371  -0.1056 336 LYS B CE  
6899 N NZ  . LYS B 336 ? 0.8765 0.6484 0.7120 -0.0390 0.0346  -0.0990 336 LYS B NZ  
6900 N N   . ILE B 337 ? 0.3287 0.2113 0.1881 -0.0085 0.0339  -0.0856 337 ILE B N   
6901 C CA  . ILE B 337 ? 0.3144 0.2161 0.1874 0.0008  0.0358  -0.0780 337 ILE B CA  
6902 C C   . ILE B 337 ? 0.3440 0.2642 0.2078 -0.0051 0.0350  -0.0770 337 ILE B C   
6903 O O   . ILE B 337 ? 0.3550 0.2815 0.2161 0.0001  0.0416  -0.0782 337 ILE B O   
6904 C CB  . ILE B 337 ? 0.3015 0.2147 0.1951 0.0042  0.0297  -0.0666 337 ILE B CB  
6905 C CG1 . ILE B 337 ? 0.2941 0.1928 0.1971 0.0119  0.0312  -0.0663 337 ILE B CG1 
6906 C CG2 . ILE B 337 ? 0.3158 0.2482 0.2207 0.0093  0.0312  -0.0591 337 ILE B CG2 
6907 C CD1 . ILE B 337 ? 0.2953 0.2024 0.2141 0.0121  0.0243  -0.0572 337 ILE B CD1 
6908 N N   . HIS B 338 ? 0.3604 0.2921 0.2199 -0.0155 0.0270  -0.0735 338 HIS B N   
6909 C CA  . HIS B 338 ? 0.3562 0.3081 0.2066 -0.0208 0.0251  -0.0702 338 HIS B CA  
6910 C C   . HIS B 338 ? 0.4149 0.3609 0.2435 -0.0242 0.0317  -0.0818 338 HIS B C   
6911 O O   . HIS B 338 ? 0.3955 0.3556 0.2188 -0.0226 0.0349  -0.0792 338 HIS B O   
6912 C CB  . HIS B 338 ? 0.3703 0.3357 0.2189 -0.0312 0.0152  -0.0654 338 HIS B CB  
6913 C CG  . HIS B 338 ? 0.4514 0.4406 0.2908 -0.0361 0.0118  -0.0599 338 HIS B CG  
6914 N ND1 . HIS B 338 ? 0.5069 0.5031 0.3263 -0.0485 0.0088  -0.0671 338 HIS B ND1 
6915 C CD2 . HIS B 338 ? 0.4365 0.4444 0.2833 -0.0307 0.0108  -0.0470 338 HIS B CD2 
6916 C CE1 . HIS B 338 ? 0.5135 0.5347 0.3288 -0.0495 0.0056  -0.0582 338 HIS B CE1 
6917 N NE2 . HIS B 338 ? 0.4853 0.5123 0.3169 -0.0382 0.0071  -0.0454 338 HIS B NE2 
6918 N N   . GLU B 339 ? 0.3744 0.2984 0.1896 -0.0290 0.0344  -0.0944 339 GLU B N   
6919 C CA  . GLU B 339 ? 0.4573 0.3767 0.2586 -0.0300 0.0389  -0.1028 339 GLU B CA  
6920 C C   . GLU B 339 ? 0.4906 0.3998 0.2957 -0.0158 0.0496  -0.1064 339 GLU B C   
6921 O O   . GLU B 339 ? 0.5009 0.4084 0.2942 -0.0147 0.0547  -0.1130 339 GLU B O   
6922 C CB  . GLU B 339 ? 0.4980 0.4012 0.2909 -0.0396 0.0357  -0.1107 339 GLU B CB  
6923 C CG  . GLU B 339 ? 0.5953 0.5148 0.3841 -0.0549 0.0253  -0.1075 339 GLU B CG  
6924 C CD  . GLU B 339 ? 0.7558 0.6591 0.5388 -0.0658 0.0231  -0.1145 339 GLU B CD  
6925 O OE1 . GLU B 339 ? 0.7086 0.5854 0.4939 -0.0604 0.0286  -0.1193 339 GLU B OE1 
6926 O OE2 . GLU B 339 ? 0.8690 0.7874 0.6455 -0.0798 0.0160  -0.1143 339 GLU B OE2 
6927 N N   . SER B 340 ? 0.4847 0.3897 0.3064 -0.0048 0.0530  -0.1017 340 SER B N   
6928 C CA  . SER B 340 ? 0.5139 0.4138 0.3430 0.0093  0.0623  -0.1037 340 SER B CA  
6929 C C   . SER B 340 ? 0.5103 0.4307 0.3441 0.0153  0.0684  -0.0987 340 SER B C   
6930 O O   . SER B 340 ? 0.5164 0.4390 0.3558 0.0262  0.0765  -0.1003 340 SER B O   
6931 C CB  . SER B 340 ? 0.4227 0.3109 0.2694 0.0185  0.0622  -0.1001 340 SER B CB  
6932 O OG  . SER B 340 ? 0.4948 0.3948 0.3550 0.0206  0.0599  -0.0911 340 SER B OG  
6933 N N   . VAL B 341 ? 0.4297 0.3681 0.2642 0.0086  0.0641  -0.0907 341 VAL B N   
6934 C CA  . VAL B 341 ? 0.4459 0.4061 0.2901 0.0130  0.0677  -0.0819 341 VAL B CA  
6935 C C   . VAL B 341 ? 0.4167 0.3922 0.2453 0.0038  0.0655  -0.0791 341 VAL B C   
6936 O O   . VAL B 341 ? 0.4738 0.4496 0.2914 -0.0059 0.0577  -0.0797 341 VAL B O   
6937 C CB  . VAL B 341 ? 0.3988 0.3693 0.2679 0.0160  0.0624  -0.0689 341 VAL B CB  
6938 C CG1 . VAL B 341 ? 0.3686 0.3293 0.2531 0.0255  0.0646  -0.0705 341 VAL B CG1 
6939 C CG2 . VAL B 341 ? 0.3953 0.3677 0.2663 0.0078  0.0512  -0.0621 341 VAL B CG2 
6940 N N   . ASP B 342 ? 0.4256 0.4166 0.2538 0.0069  0.0724  -0.0751 342 ASP B N   
6941 C CA  . ASP B 342 ? 0.4797 0.4873 0.2931 -0.0003 0.0713  -0.0701 342 ASP B CA  
6942 C C   . ASP B 342 ? 0.4405 0.4638 0.2681 -0.0014 0.0663  -0.0529 342 ASP B C   
6943 O O   . ASP B 342 ? 0.5417 0.5797 0.3589 -0.0058 0.0657  -0.0454 342 ASP B O   
6944 C CB  . ASP B 342 ? 0.6229 0.6371 0.4233 0.0030  0.0834  -0.0761 342 ASP B CB  
6945 C CG  . ASP B 342 ? 0.8258 0.8471 0.6457 0.0130  0.0921  -0.0716 342 ASP B CG  
6946 O OD1 . ASP B 342 ? 0.8758 0.8881 0.7135 0.0197  0.0918  -0.0725 342 ASP B OD1 
6947 O OD2 . ASP B 342 ? 0.9065 0.9446 0.7240 0.0134  0.0992  -0.0667 342 ASP B OD2 
6948 N N   . PHE B 343 ? 0.3464 0.3657 0.1960 0.0024  0.0631  -0.0464 343 PHE B N   
6949 C CA  . PHE B 343 ? 0.3042 0.3314 0.1667 0.0014  0.0589  -0.0315 343 PHE B CA  
6950 C C   . PHE B 343 ? 0.2782 0.2978 0.1476 -0.0003 0.0487  -0.0290 343 PHE B C   
6951 O O   . PHE B 343 ? 0.3377 0.3476 0.2020 -0.0020 0.0450  -0.0382 343 PHE B O   
6952 C CB  . PHE B 343 ? 0.3408 0.3709 0.2221 0.0059  0.0650  -0.0269 343 PHE B CB  
6953 C CG  . PHE B 343 ? 0.2992 0.3199 0.1944 0.0116  0.0655  -0.0343 343 PHE B CG  
6954 C CD1 . PHE B 343 ? 0.3205 0.3394 0.2129 0.0175  0.0730  -0.0447 343 PHE B CD1 
6955 C CD2 . PHE B 343 ? 0.2562 0.2705 0.1668 0.0121  0.0592  -0.0304 343 PHE B CD2 
6956 C CE1 . PHE B 343 ? 0.3053 0.3167 0.2106 0.0246  0.0736  -0.0494 343 PHE B CE1 
6957 C CE2 . PHE B 343 ? 0.2907 0.2985 0.2132 0.0176  0.0593  -0.0359 343 PHE B CE2 
6958 C CZ  . PHE B 343 ? 0.2890 0.2959 0.2092 0.0242  0.0663  -0.0447 343 PHE B CZ  
6959 N N   . GLN B 344 ? 0.2777 0.3007 0.1580 0.0000  0.0451  -0.0163 344 GLN B N   
6960 C CA  . GLN B 344 ? 0.2453 0.2628 0.1338 -0.0001 0.0369  -0.0131 344 GLN B CA  
6961 C C   . GLN B 344 ? 0.2312 0.2377 0.1372 0.0038  0.0374  -0.0158 344 GLN B C   
6962 O O   . GLN B 344 ? 0.2540 0.2606 0.1717 0.0054  0.0401  -0.0091 344 GLN B O   
6963 C CB  . GLN B 344 ? 0.2574 0.2823 0.1472 0.0002  0.0338  0.0017  344 GLN B CB  
6964 C CG  . GLN B 344 ? 0.2556 0.2955 0.1278 -0.0030 0.0322  0.0063  344 GLN B CG  
6965 C CD  . GLN B 344 ? 0.3286 0.3767 0.2018 -0.0004 0.0286  0.0226  344 GLN B CD  
6966 O OE1 . GLN B 344 ? 0.3185 0.3783 0.1859 -0.0017 0.0214  0.0260  344 GLN B OE1 
6967 N NE2 . GLN B 344 ? 0.3224 0.3648 0.2026 0.0032  0.0340  0.0333  344 GLN B NE2 
6968 N N   . PRO B 345 ? 0.2351 0.2321 0.1427 0.0045  0.0349  -0.0249 345 PRO B N   
6969 C CA  . PRO B 345 ? 0.2760 0.2653 0.1992 0.0088  0.0354  -0.0268 345 PRO B CA  
6970 C C   . PRO B 345 ? 0.2557 0.2428 0.1898 0.0086  0.0299  -0.0194 345 PRO B C   
6971 O O   . PRO B 345 ? 0.2480 0.2367 0.1781 0.0065  0.0246  -0.0153 345 PRO B O   
6972 C CB  . PRO B 345 ? 0.2664 0.2442 0.1842 0.0098  0.0346  -0.0375 345 PRO B CB  
6973 C CG  . PRO B 345 ? 0.2486 0.2270 0.1521 0.0029  0.0294  -0.0388 345 PRO B CG  
6974 C CD  . PRO B 345 ? 0.2547 0.2472 0.1492 0.0003  0.0309  -0.0330 345 PRO B CD  
6975 N N   . VAL B 346 ? 0.1837 0.1688 0.1314 0.0109  0.0315  -0.0180 346 VAL B N   
6976 C CA  . VAL B 346 ? 0.1689 0.1492 0.1259 0.0111  0.0274  -0.0135 346 VAL B CA  
6977 C C   . VAL B 346 ? 0.2645 0.2389 0.2281 0.0135  0.0248  -0.0197 346 VAL B C   
6978 O O   . VAL B 346 ? 0.2387 0.2149 0.2082 0.0163  0.0278  -0.0236 346 VAL B O   
6979 C CB  . VAL B 346 ? 0.1909 0.1721 0.1560 0.0096  0.0311  -0.0076 346 VAL B CB  
6980 C CG1 . VAL B 346 ? 0.2036 0.1770 0.1755 0.0097  0.0277  -0.0047 346 VAL B CG1 
6981 C CG2 . VAL B 346 ? 0.2654 0.2504 0.2226 0.0077  0.0347  0.0001  346 VAL B CG2 
6982 N N   . VAL B 347 ? 0.1916 0.1609 0.1544 0.0131  0.0194  -0.0194 347 VAL B N   
6983 C CA  . VAL B 347 ? 0.2058 0.1682 0.1719 0.0149  0.0168  -0.0242 347 VAL B CA  
6984 C C   . VAL B 347 ? 0.1686 0.1296 0.1433 0.0153  0.0136  -0.0204 347 VAL B C   
6985 O O   . VAL B 347 ? 0.1949 0.1558 0.1681 0.0140  0.0105  -0.0166 347 VAL B O   
6986 C CB  . VAL B 347 ? 0.1702 0.1270 0.1259 0.0121  0.0139  -0.0282 347 VAL B CB  
6987 C CG1 . VAL B 347 ? 0.1925 0.1390 0.1507 0.0141  0.0126  -0.0321 347 VAL B CG1 
6988 C CG2 . VAL B 347 ? 0.2197 0.1767 0.1634 0.0105  0.0176  -0.0333 347 VAL B CG2 
6989 N N   . PHE B 348 ? 0.1807 0.1427 0.1643 0.0172  0.0146  -0.0214 348 PHE B N   
6990 C CA  . PHE B 348 ? 0.1798 0.1401 0.1696 0.0167  0.0121  -0.0194 348 PHE B CA  
6991 C C   . PHE B 348 ? 0.1841 0.1403 0.1744 0.0189  0.0085  -0.0216 348 PHE B C   
6992 O O   . PHE B 348 ? 0.1928 0.1489 0.1845 0.0221  0.0091  -0.0244 348 PHE B O   
6993 C CB  . PHE B 348 ? 0.1853 0.1512 0.1831 0.0152  0.0144  -0.0197 348 PHE B CB  
6994 C CG  . PHE B 348 ? 0.1962 0.1598 0.1937 0.0111  0.0174  -0.0160 348 PHE B CG  
6995 C CD1 . PHE B 348 ? 0.2560 0.2209 0.2490 0.0099  0.0212  -0.0129 348 PHE B CD1 
6996 C CD2 . PHE B 348 ? 0.2258 0.1841 0.2256 0.0083  0.0171  -0.0156 348 PHE B CD2 
6997 C CE1 . PHE B 348 ? 0.1713 0.1309 0.1627 0.0065  0.0248  -0.0081 348 PHE B CE1 
6998 C CE2 . PHE B 348 ? 0.2293 0.1801 0.2269 0.0045  0.0213  -0.0123 348 PHE B CE2 
6999 C CZ  . PHE B 348 ? 0.1926 0.1434 0.1864 0.0039  0.0252  -0.0078 348 PHE B CZ  
7000 N N   . VAL B 349 ? 0.1589 0.1121 0.1479 0.0178  0.0055  -0.0194 349 VAL B N   
7001 C CA  . VAL B 349 ? 0.1756 0.1252 0.1648 0.0187  0.0025  -0.0201 349 VAL B CA  
7002 C C   . VAL B 349 ? 0.1667 0.1182 0.1608 0.0189  0.0015  -0.0188 349 VAL B C   
7003 O O   . VAL B 349 ? 0.1928 0.1438 0.1864 0.0180  0.0018  -0.0164 349 VAL B O   
7004 C CB  . VAL B 349 ? 0.1550 0.1024 0.1383 0.0159  0.0002  -0.0190 349 VAL B CB  
7005 C CG1 . VAL B 349 ? 0.2159 0.1587 0.1989 0.0156  -0.0021 -0.0189 349 VAL B CG1 
7006 C CG2 . VAL B 349 ? 0.2144 0.1593 0.1900 0.0136  0.0013  -0.0221 349 VAL B CG2 
7007 N N   . VAL B 350 ? 0.1476 0.1023 0.1461 0.0204  0.0009  -0.0204 350 VAL B N   
7008 C CA  . VAL B 350 ? 0.1535 0.1115 0.1551 0.0187  0.0000  -0.0208 350 VAL B CA  
7009 C C   . VAL B 350 ? 0.1884 0.1485 0.1903 0.0210  -0.0032 -0.0203 350 VAL B C   
7010 O O   . VAL B 350 ? 0.1728 0.1362 0.1769 0.0247  -0.0040 -0.0199 350 VAL B O   
7011 C CB  . VAL B 350 ? 0.1584 0.1236 0.1650 0.0158  0.0019  -0.0227 350 VAL B CB  
7012 C CG1 . VAL B 350 ? 0.1897 0.1556 0.1964 0.0113  0.0014  -0.0247 350 VAL B CG1 
7013 C CG2 . VAL B 350 ? 0.1753 0.1381 0.1809 0.0139  0.0059  -0.0219 350 VAL B CG2 
7014 N N   . LEU B 351 ? 0.1870 0.1454 0.1862 0.0198  -0.0044 -0.0196 351 LEU B N   
7015 C CA  . LEU B 351 ? 0.1919 0.1527 0.1899 0.0216  -0.0073 -0.0180 351 LEU B CA  
7016 C C   . LEU B 351 ? 0.1489 0.1099 0.1435 0.0193  -0.0072 -0.0188 351 LEU B C   
7017 O O   . LEU B 351 ? 0.1998 0.1565 0.1931 0.0178  -0.0044 -0.0201 351 LEU B O   
7018 C CB  . LEU B 351 ? 0.1796 0.1334 0.1743 0.0237  -0.0079 -0.0150 351 LEU B CB  
7019 C CG  . LEU B 351 ? 0.2512 0.2003 0.2424 0.0209  -0.0072 -0.0137 351 LEU B CG  
7020 C CD1 . LEU B 351 ? 0.2237 0.1680 0.2109 0.0201  -0.0084 -0.0105 351 LEU B CD1 
7021 C CD2 . LEU B 351 ? 0.2604 0.2069 0.2510 0.0195  -0.0056 -0.0149 351 LEU B CD2 
7022 N N   . ASN B 352 ? 0.1951 0.1607 0.1875 0.0200  -0.0097 -0.0175 352 ASN B N   
7023 C CA  . ASN B 352 ? 0.1715 0.1373 0.1589 0.0183  -0.0088 -0.0187 352 ASN B CA  
7024 C C   . ASN B 352 ? 0.1750 0.1353 0.1608 0.0194  -0.0064 -0.0161 352 ASN B C   
7025 O O   . ASN B 352 ? 0.2099 0.1683 0.1968 0.0200  -0.0072 -0.0125 352 ASN B O   
7026 C CB  . ASN B 352 ? 0.2152 0.1883 0.1990 0.0192  -0.0120 -0.0163 352 ASN B CB  
7027 C CG  . ASN B 352 ? 0.3933 0.3780 0.3799 0.0191  -0.0156 -0.0169 352 ASN B CG  
7028 O OD1 . ASN B 352 ? 0.6652 0.6560 0.6515 0.0228  -0.0186 -0.0118 352 ASN B OD1 
7029 N ND2 . ASN B 352 ? 0.2271 0.2158 0.2164 0.0148  -0.0151 -0.0222 352 ASN B ND2 
7030 N N   . GLY B 353 ? 0.2120 0.1702 0.1953 0.0194  -0.0029 -0.0180 353 GLY B N   
7031 C CA  . GLY B 353 ? 0.2259 0.1839 0.2097 0.0217  -0.0003 -0.0146 353 GLY B CA  
7032 C C   . GLY B 353 ? 0.1773 0.1409 0.1582 0.0226  0.0006  -0.0120 353 GLY B C   
7033 O O   . GLY B 353 ? 0.1969 0.1649 0.1797 0.0246  0.0030  -0.0085 353 GLY B O   
7034 N N   . GLU B 354 ? 0.2160 0.1824 0.1924 0.0212  -0.0012 -0.0128 354 GLU B N   
7035 C CA  . GLU B 354 ? 0.1664 0.1387 0.1385 0.0219  0.0009  -0.0107 354 GLU B CA  
7036 C C   . GLU B 354 ? 0.1902 0.1667 0.1593 0.0199  -0.0026 -0.0061 354 GLU B C   
7037 O O   . GLU B 354 ? 0.2460 0.2286 0.2113 0.0196  -0.0007 -0.0030 354 GLU B O   
7038 C CB  . GLU B 354 ? 0.1936 0.1640 0.1586 0.0229  0.0047  -0.0170 354 GLU B CB  
7039 C CG  . GLU B 354 ? 0.1741 0.1471 0.1329 0.0193  0.0012  -0.0209 354 GLU B CG  
7040 C CD  . GLU B 354 ? 0.2030 0.1724 0.1644 0.0162  -0.0013 -0.0257 354 GLU B CD  
7041 O OE1 . GLU B 354 ? 0.2112 0.1772 0.1668 0.0127  0.0006  -0.0332 354 GLU B OE1 
7042 O OE2 . GLU B 354 ? 0.2205 0.1900 0.1891 0.0166  -0.0044 -0.0224 354 GLU B OE2 
7043 N N   . ASN B 355 ? 0.1682 0.1418 0.1387 0.0192  -0.0068 -0.0045 355 ASN B N   
7044 C CA  . ASN B 355 ? 0.1703 0.1457 0.1367 0.0192  -0.0094 0.0010  355 ASN B CA  
7045 C C   . ASN B 355 ? 0.2311 0.1993 0.1984 0.0176  -0.0096 0.0074  355 ASN B C   
7046 O O   . ASN B 355 ? 0.2173 0.1849 0.1798 0.0169  -0.0099 0.0136  355 ASN B O   
7047 C CB  . ASN B 355 ? 0.2115 0.1895 0.1782 0.0213  -0.0133 0.0000  355 ASN B CB  
7048 C CG  . ASN B 355 ? 0.2145 0.2008 0.1776 0.0197  -0.0137 -0.0063 355 ASN B CG  
7049 O OD1 . ASN B 355 ? 0.2184 0.2083 0.1746 0.0184  -0.0115 -0.0078 355 ASN B OD1 
7050 N ND2 . ASN B 355 ? 0.2275 0.2170 0.1943 0.0190  -0.0158 -0.0106 355 ASN B ND2 
7051 N N   . CYS B 356 ? 0.2116 0.1733 0.1835 0.0161  -0.0092 0.0059  356 CYS B N   
7052 C CA  . CYS B 356 ? 0.1572 0.1089 0.1276 0.0127  -0.0092 0.0101  356 CYS B CA  
7053 C C   . CYS B 356 ? 0.1688 0.1249 0.1386 0.0061  -0.0073 0.0134  356 CYS B C   
7054 O O   . CYS B 356 ? 0.2150 0.1630 0.1807 0.0011  -0.0068 0.0181  356 CYS B O   
7055 C CB  . CYS B 356 ? 0.2270 0.1703 0.2004 0.0128  -0.0096 0.0062  356 CYS B CB  
7056 S SG  . CYS B 356 ? 0.2121 0.1633 0.1912 0.0118  -0.0087 0.0010  356 CYS B SG  
7057 N N   . TRP B 357 ? 0.1784 0.1473 0.1520 0.0062  -0.0055 0.0117  357 TRP B N   
7058 C CA  . TRP B 357 ? 0.2259 0.2047 0.2020 0.0003  -0.0038 0.0151  357 TRP B CA  
7059 C C   . TRP B 357 ? 0.2042 0.1868 0.1761 -0.0040 -0.0021 0.0213  357 TRP B C   
7060 O O   . TRP B 357 ? 0.1953 0.1817 0.1679 -0.0124 -0.0014 0.0252  357 TRP B O   
7061 C CB  . TRP B 357 ? 0.1667 0.1598 0.1486 0.0047  -0.0014 0.0133  357 TRP B CB  
7062 C CG  . TRP B 357 ? 0.1404 0.1277 0.1248 0.0093  -0.0023 0.0082  357 TRP B CG  
7063 C CD1 . TRP B 357 ? 0.1827 0.1680 0.1669 0.0158  -0.0005 0.0041  357 TRP B CD1 
7064 C CD2 . TRP B 357 ? 0.1874 0.1686 0.1732 0.0064  -0.0048 0.0066  357 TRP B CD2 
7065 N NE1 . TRP B 357 ? 0.1697 0.1489 0.1563 0.0171  -0.0016 0.0011  357 TRP B NE1 
7066 C CE2 . TRP B 357 ? 0.1888 0.1663 0.1763 0.0121  -0.0042 0.0026  357 TRP B CE2 
7067 C CE3 . TRP B 357 ? 0.2088 0.1861 0.1932 -0.0013 -0.0068 0.0075  357 TRP B CE3 
7068 C CZ2 . TRP B 357 ? 0.1913 0.1639 0.1797 0.0112  -0.0057 0.0004  357 TRP B CZ2 
7069 C CZ3 . TRP B 357 ? 0.2116 0.1832 0.1958 -0.0021 -0.0082 0.0040  357 TRP B CZ3 
7070 C CH2 . TRP B 357 ? 0.1838 0.1543 0.1703 0.0047  -0.0077 0.0010  357 TRP B CH2 
7071 N N   . GLU B 358 ? 0.2132 0.1962 0.1800 0.0006  -0.0016 0.0224  358 GLU B N   
7072 C CA  . GLU B 358 ? 0.1820 0.1697 0.1435 -0.0030 0.0005  0.0292  358 GLU B CA  
7073 C C   . GLU B 358 ? 0.2661 0.2385 0.2227 -0.0096 -0.0003 0.0352  358 GLU B C   
7074 O O   . GLU B 358 ? 0.2737 0.2487 0.2262 -0.0155 0.0021  0.0421  358 GLU B O   
7075 C CB  . GLU B 358 ? 0.2430 0.2348 0.1979 0.0031  0.0007  0.0288  358 GLU B CB  
7076 C CG  . GLU B 358 ? 0.2112 0.1922 0.1627 0.0077  -0.0034 0.0278  358 GLU B CG  
7077 C CD  . GLU B 358 ? 0.2643 0.2539 0.2113 0.0127  -0.0043 0.0234  358 GLU B CD  
7078 O OE1 . GLU B 358 ? 0.3094 0.3014 0.2490 0.0142  -0.0061 0.0279  358 GLU B OE1 
7079 O OE2 . GLU B 358 ? 0.2470 0.2406 0.1967 0.0146  -0.0029 0.0156  358 GLU B OE2 
7080 N N   . TYR B 359 ? 0.2238 0.1788 0.1798 -0.0087 -0.0026 0.0330  359 TYR B N   
7081 C CA  . TYR B 359 ? 0.2067 0.1415 0.1565 -0.0143 -0.0019 0.0377  359 TYR B CA  
7082 C C   . TYR B 359 ? 0.2559 0.1857 0.2073 -0.0253 -0.0013 0.0349  359 TYR B C   
7083 O O   . TYR B 359 ? 0.3164 0.2266 0.2609 -0.0327 0.0004  0.0376  359 TYR B O   
7084 C CB  . TYR B 359 ? 0.2367 0.1545 0.1834 -0.0054 -0.0035 0.0371  359 TYR B CB  
7085 C CG  . TYR B 359 ? 0.2484 0.1755 0.1937 0.0044  -0.0054 0.0398  359 TYR B CG  
7086 C CD1 . TYR B 359 ? 0.3389 0.2644 0.2765 0.0056  -0.0045 0.0492  359 TYR B CD1 
7087 C CD2 . TYR B 359 ? 0.3337 0.2725 0.2844 0.0109  -0.0080 0.0332  359 TYR B CD2 
7088 C CE1 . TYR B 359 ? 0.3777 0.3154 0.3129 0.0135  -0.0071 0.0517  359 TYR B CE1 
7089 C CE2 . TYR B 359 ? 0.3787 0.3283 0.3271 0.0172  -0.0103 0.0346  359 TYR B CE2 
7090 C CZ  . TYR B 359 ? 0.4550 0.4054 0.3956 0.0186  -0.0102 0.0437  359 TYR B CZ  
7091 O OH  . TYR B 359 ? 0.4524 0.4170 0.3897 0.0240  -0.0132 0.0451  359 TYR B OH  
7092 N N   . TYR B 360 ? 0.2487 0.1951 0.2080 -0.0267 -0.0023 0.0298  360 TYR B N   
7093 C CA  . TYR B 360 ? 0.2943 0.2426 0.2553 -0.0381 -0.0027 0.0275  360 TYR B CA  
7094 C C   . TYR B 360 ? 0.3051 0.2718 0.2687 -0.0485 -0.0009 0.0330  360 TYR B C   
7095 O O   . TYR B 360 ? 0.2590 0.2441 0.2266 -0.0438 0.0009  0.0366  360 TYR B O   
7096 C CB  . TYR B 360 ? 0.2413 0.2033 0.2100 -0.0343 -0.0049 0.0215  360 TYR B CB  
7097 C CG  . TYR B 360 ? 0.2943 0.2413 0.2611 -0.0288 -0.0065 0.0152  360 TYR B CG  
7098 C CD1 . TYR B 360 ? 0.2620 0.2012 0.2285 -0.0173 -0.0067 0.0138  360 TYR B CD1 
7099 C CD2 . TYR B 360 ? 0.3086 0.2536 0.2744 -0.0355 -0.0079 0.0105  360 TYR B CD2 
7100 C CE1 . TYR B 360 ? 0.2490 0.1786 0.2154 -0.0123 -0.0075 0.0085  360 TYR B CE1 
7101 C CE2 . TYR B 360 ? 0.2304 0.1640 0.1943 -0.0301 -0.0085 0.0048  360 TYR B CE2 
7102 C CZ  . TYR B 360 ? 0.2548 0.1808 0.2196 -0.0182 -0.0080 0.0041  360 TYR B CZ  
7103 O OH  . TYR B 360 ? 0.2186 0.1363 0.1826 -0.0131 -0.0080 -0.0010 360 TYR B OH  
7104 N N   . GLU B 361 ? 0.3277 0.2832 0.2856 -0.0601 0.0289  0.0402  361 GLU B N   
7105 C CA  . GLU B 361 ? 0.3553 0.3366 0.3165 -0.0777 0.0284  0.0398  361 GLU B CA  
7106 C C   . GLU B 361 ? 0.2482 0.2721 0.2242 -0.0726 0.0201  0.0308  361 GLU B C   
7107 O O   . GLU B 361 ? 0.2690 0.2921 0.2492 -0.0656 0.0151  0.0218  361 GLU B O   
7108 C CB  . GLU B 361 ? 0.4865 0.4431 0.4376 -0.1000 0.0325  0.0360  361 GLU B CB  
7109 C CG  . GLU B 361 ? 0.5990 0.5092 0.5336 -0.1064 0.0426  0.0452  361 GLU B CG  
7110 C CD  . GLU B 361 ? 0.7079 0.6271 0.6406 -0.1088 0.0473  0.0600  361 GLU B CD  
7111 O OE1 . GLU B 361 ? 0.7249 0.6804 0.6645 -0.1212 0.0454  0.0607  361 GLU B OE1 
7112 O OE2 . GLU B 361 ? 0.7090 0.6016 0.6333 -0.0977 0.0530  0.0717  361 GLU B OE2 
7113 N N   . GLU B 362 ? 0.2840 0.3444 0.2674 -0.0746 0.0193  0.0340  362 GLU B N   
7114 C CA  . GLU B 362 ? 0.2260 0.3269 0.2229 -0.0688 0.0130  0.0264  362 GLU B CA  
7115 C C   . GLU B 362 ? 0.2426 0.3433 0.2452 -0.0480 0.0078  0.0198  362 GLU B C   
7116 O O   . GLU B 362 ? 0.2004 0.3158 0.2108 -0.0431 0.0026  0.0118  362 GLU B O   
7117 C CB  . GLU B 362 ? 0.2799 0.3922 0.2798 -0.0840 0.0104  0.0200  362 GLU B CB  
7118 C CG  . GLU B 362 ? 0.4835 0.6458 0.4966 -0.0844 0.0069  0.0177  362 GLU B CG  
7119 C CD  . GLU B 362 ? 0.6651 0.8435 0.6801 -0.1036 0.0050  0.0141  362 GLU B CD  
7120 O OE1 . GLU B 362 ? 0.7284 0.9401 0.7546 -0.0976 -0.0006 0.0093  362 GLU B OE1 
7121 O OE2 . GLU B 362 ? 0.7040 0.8621 0.7087 -0.1249 0.0092  0.0163  362 GLU B OE2 
7122 N N   . ASN B 363 ? 0.2236 0.3077 0.2218 -0.0363 0.0093  0.0238  363 ASN B N   
7123 C CA  . ASN B 363 ? 0.2052 0.2926 0.2084 -0.0188 0.0048  0.0179  363 ASN B CA  
7124 C C   . ASN B 363 ? 0.2310 0.3009 0.2352 -0.0163 0.0013  0.0102  363 ASN B C   
7125 O O   . ASN B 363 ? 0.1897 0.2683 0.2002 -0.0061 -0.0032 0.0034  363 ASN B O   
7126 C CB  . ASN B 363 ? 0.2199 0.3433 0.2322 -0.0111 0.0021  0.0130  363 ASN B CB  
7127 C CG  . ASN B 363 ? 0.1596 0.2840 0.1742 0.0047  -0.0011 0.0071  363 ASN B CG  
7128 O OD1 . ASN B 363 ? 0.1791 0.2880 0.1888 0.0098  -0.0005 0.0101  363 ASN B OD1 
7129 N ND2 . ASN B 363 ? 0.1788 0.3219 0.2006 0.0123  -0.0040 -0.0014 363 ASN B ND2 
7130 N N   . GLY B 364 ? 0.2009 0.2446 0.1976 -0.0263 0.0039  0.0113  364 GLY B N   
7131 C CA  . GLY B 364 ? 0.2075 0.2336 0.2028 -0.0247 0.0015  0.0047  364 GLY B CA  
7132 C C   . GLY B 364 ? 0.1896 0.2338 0.1905 -0.0298 -0.0034 -0.0021 364 GLY B C   
7133 O O   . GLY B 364 ? 0.2140 0.2455 0.2127 -0.0294 -0.0055 -0.0071 364 GLY B O   
7134 N N   . ILE B 365 ? 0.2255 0.3014 0.2337 -0.0338 -0.0051 -0.0018 365 ILE B N   
7135 C CA  . ILE B 365 ? 0.2196 0.3185 0.2347 -0.0353 -0.0101 -0.0066 365 ILE B CA  
7136 C C   . ILE B 365 ? 0.1943 0.2837 0.2025 -0.0519 -0.0103 -0.0091 365 ILE B C   
7137 O O   . ILE B 365 ? 0.1970 0.2866 0.2056 -0.0494 -0.0145 -0.0135 365 ILE B O   
7138 C CB  . ILE B 365 ? 0.2032 0.3418 0.2282 -0.0340 -0.0109 -0.0051 365 ILE B CB  
7139 C CG1 . ILE B 365 ? 0.2229 0.3685 0.2527 -0.0165 -0.0108 -0.0056 365 ILE B CG1 
7140 C CG2 . ILE B 365 ? 0.1780 0.3442 0.2109 -0.0342 -0.0160 -0.0081 365 ILE B CG2 
7141 C CD1 . ILE B 365 ? 0.2333 0.4143 0.2702 -0.0150 -0.0091 -0.0038 365 ILE B CD1 
7142 N N   . PRO B 366 ? 0.2034 0.2829 0.2037 -0.0699 -0.0056 -0.0067 366 PRO B N   
7143 C CA  . PRO B 366 ? 0.2493 0.3141 0.2400 -0.0869 -0.0052 -0.0116 366 PRO B CA  
7144 C C   . PRO B 366 ? 0.2494 0.2809 0.2317 -0.0801 -0.0049 -0.0162 366 PRO B C   
7145 O O   . PRO B 366 ? 0.2598 0.2940 0.2390 -0.0857 -0.0083 -0.0222 366 PRO B O   
7146 C CB  . PRO B 366 ? 0.3054 0.3523 0.2860 -0.1053 0.0020  -0.0077 366 PRO B CB  
7147 C CG  . PRO B 366 ? 0.2518 0.3268 0.2417 -0.1020 0.0029  -0.0004 366 PRO B CG  
7148 C CD  . PRO B 366 ? 0.2180 0.2991 0.2162 -0.0773 -0.0002 0.0003  366 PRO B CD  
7149 N N   . PHE B 367 ? 0.2404 0.2445 0.2190 -0.0679 -0.0009 -0.0132 367 PHE B N   
7150 C CA  . PHE B 367 ? 0.2417 0.2171 0.2131 -0.0611 0.0004  -0.0172 367 PHE B CA  
7151 C C   . PHE B 367 ? 0.2439 0.2360 0.2231 -0.0496 -0.0063 -0.0208 367 PHE B C   
7152 O O   . PHE B 367 ? 0.2295 0.2147 0.2031 -0.0529 -0.0078 -0.0261 367 PHE B O   
7153 C CB  . PHE B 367 ? 0.2297 0.1802 0.1980 -0.0486 0.0057  -0.0116 367 PHE B CB  
7154 C CG  . PHE B 367 ? 0.2376 0.1665 0.2015 -0.0386 0.0070  -0.0150 367 PHE B CG  
7155 C CD1 . PHE B 367 ? 0.3048 0.2040 0.2554 -0.0462 0.0123  -0.0197 367 PHE B CD1 
7156 C CD2 . PHE B 367 ? 0.2189 0.1580 0.1915 -0.0227 0.0033  -0.0144 367 PHE B CD2 
7157 C CE1 . PHE B 367 ? 0.3077 0.1904 0.2544 -0.0366 0.0141  -0.0230 367 PHE B CE1 
7158 C CE2 . PHE B 367 ? 0.2212 0.1442 0.1904 -0.0148 0.0047  -0.0171 367 PHE B CE2 
7159 C CZ  . PHE B 367 ? 0.2586 0.1548 0.2153 -0.0210 0.0103  -0.0211 367 PHE B CZ  
7160 N N   . LEU B 368 ? 0.1830 0.1951 0.1736 -0.0360 -0.0099 -0.0180 368 LEU B N   
7161 C CA  . LEU B 368 ? 0.1616 0.1828 0.1582 -0.0244 -0.0150 -0.0204 368 LEU B CA  
7162 C C   . LEU B 368 ? 0.2138 0.2590 0.2134 -0.0299 -0.0203 -0.0225 368 LEU B C   
7163 O O   . LEU B 368 ? 0.1965 0.2398 0.1943 -0.0270 -0.0233 -0.0246 368 LEU B O   
7164 C CB  . LEU B 368 ? 0.1699 0.2026 0.1758 -0.0100 -0.0165 -0.0183 368 LEU B CB  
7165 C CG  . LEU B 368 ? 0.1641 0.1779 0.1680 -0.0015 -0.0134 -0.0168 368 LEU B CG  
7166 C CD1 . LEU B 368 ? 0.2140 0.2423 0.2257 0.0097  -0.0154 -0.0169 368 LEU B CD1 
7167 C CD2 . LEU B 368 ? 0.1924 0.1867 0.1919 0.0019  -0.0131 -0.0192 368 LEU B CD2 
7168 N N   . GLU B 369 ? 0.2093 0.2806 0.2138 -0.0379 -0.0215 -0.0210 369 GLU B N   
7169 C CA  . GLU B 369 ? 0.1853 0.2856 0.1936 -0.0428 -0.0268 -0.0218 369 GLU B CA  
7170 C C   . GLU B 369 ? 0.2562 0.3445 0.2525 -0.0578 -0.0270 -0.0265 369 GLU B C   
7171 O O   . GLU B 369 ? 0.2342 0.3359 0.2302 -0.0569 -0.0318 -0.0275 369 GLU B O   
7172 C CB  . GLU B 369 ? 0.2245 0.3596 0.2408 -0.0499 -0.0275 -0.0192 369 GLU B CB  
7173 C CG  . GLU B 369 ? 0.2070 0.3622 0.2356 -0.0323 -0.0282 -0.0160 369 GLU B CG  
7174 C CD  . GLU B 369 ? 0.2241 0.4201 0.2621 -0.0369 -0.0286 -0.0132 369 GLU B CD  
7175 O OE1 . GLU B 369 ? 0.2720 0.4807 0.3073 -0.0565 -0.0281 -0.0131 369 GLU B OE1 
7176 O OE2 . GLU B 369 ? 0.1943 0.4100 0.2421 -0.0211 -0.0290 -0.0116 369 GLU B OE2 
7177 N N   . LYS B 370 ? 0.1923 0.2543 0.1776 -0.0714 -0.0211 -0.0292 370 LYS B N   
7178 C CA  . LYS B 370 ? 0.2122 0.2579 0.1834 -0.0864 -0.0199 -0.0360 370 LYS B CA  
7179 C C   . LYS B 370 ? 0.2442 0.2663 0.2093 -0.0753 -0.0192 -0.0385 370 LYS B C   
7180 O O   . LYS B 370 ? 0.2798 0.3058 0.2380 -0.0806 -0.0219 -0.0430 370 LYS B O   
7181 C CB  . LYS B 370 ? 0.2929 0.3110 0.2524 -0.1030 -0.0122 -0.0383 370 LYS B CB  
7182 C CG  . LYS B 370 ? 0.4777 0.4647 0.4192 -0.1155 -0.0079 -0.0470 370 LYS B CG  
7183 C CD  . LYS B 370 ? 0.7027 0.7018 0.6356 -0.1417 -0.0087 -0.0536 370 LYS B CD  
7184 C CE  . LYS B 370 ? 0.8536 0.8314 0.7693 -0.1507 -0.0069 -0.0644 370 LYS B CE  
7185 N NZ  . LYS B 370 ? 0.9185 0.8422 0.8182 -0.1525 0.0041  -0.0687 370 LYS B NZ  
7186 N N   . LEU B 371 ? 0.2199 0.2212 0.1875 -0.0605 -0.0158 -0.0355 371 LEU B N   
7187 C CA  . LEU B 371 ? 0.2009 0.1841 0.1645 -0.0500 -0.0149 -0.0371 371 LEU B CA  
7188 C C   . LEU B 371 ? 0.2098 0.2156 0.1797 -0.0421 -0.0218 -0.0355 371 LEU B C   
7189 O O   . LEU B 371 ? 0.2225 0.2254 0.1848 -0.0446 -0.0229 -0.0386 371 LEU B O   
7190 C CB  . LEU B 371 ? 0.2397 0.2058 0.2075 -0.0360 -0.0110 -0.0331 371 LEU B CB  
7191 C CG  . LEU B 371 ? 0.2442 0.1975 0.2106 -0.0249 -0.0100 -0.0339 371 LEU B CG  
7192 C CD1 . LEU B 371 ? 0.3016 0.2311 0.2535 -0.0319 -0.0045 -0.0397 371 LEU B CD1 
7193 C CD2 . LEU B 371 ? 0.2465 0.1929 0.2196 -0.0119 -0.0077 -0.0294 371 LEU B CD2 
7194 N N   . TYR B 372 ? 0.1922 0.2194 0.1748 -0.0321 -0.0260 -0.0305 372 TYR B N   
7195 C CA  . TYR B 372 ? 0.1839 0.2278 0.1723 -0.0219 -0.0315 -0.0272 372 TYR B CA  
7196 C C   . TYR B 372 ? 0.2211 0.2897 0.2067 -0.0308 -0.0365 -0.0274 372 TYR B C   
7197 O O   . TYR B 372 ? 0.2013 0.2740 0.1837 -0.0268 -0.0396 -0.0257 372 TYR B O   
7198 C CB  . TYR B 372 ? 0.2099 0.2683 0.2112 -0.0089 -0.0334 -0.0229 372 TYR B CB  
7199 C CG  . TYR B 372 ? 0.2043 0.2434 0.2083 0.0006  -0.0298 -0.0229 372 TYR B CG  
7200 C CD1 . TYR B 372 ? 0.1898 0.2039 0.1874 0.0011  -0.0263 -0.0246 372 TYR B CD1 
7201 C CD2 . TYR B 372 ? 0.1983 0.2477 0.2112 0.0092  -0.0299 -0.0215 372 TYR B CD2 
7202 C CE1 . TYR B 372 ? 0.2117 0.2147 0.2128 0.0092  -0.0239 -0.0242 372 TYR B CE1 
7203 C CE2 . TYR B 372 ? 0.1534 0.1893 0.1679 0.0162  -0.0273 -0.0222 372 TYR B CE2 
7204 C CZ  . TYR B 372 ? 0.1555 0.1695 0.1645 0.0158  -0.0247 -0.0232 372 TYR B CZ  
7205 O OH  . TYR B 372 ? 0.1497 0.1560 0.1609 0.0219  -0.0228 -0.0237 372 TYR B OH  
7206 N N   . SER B 373 ? 0.2267 0.3148 0.2132 -0.0436 -0.0374 -0.0288 373 SER B N   
7207 C CA  . SER B 373 ? 0.2260 0.3434 0.2097 -0.0544 -0.0427 -0.0294 373 SER B CA  
7208 C C   . SER B 373 ? 0.2578 0.3580 0.2252 -0.0662 -0.0414 -0.0361 373 SER B C   
7209 O O   . SER B 373 ? 0.2660 0.3852 0.2295 -0.0679 -0.0464 -0.0353 373 SER B O   
7210 C CB  . SER B 373 ? 0.2018 0.3435 0.1891 -0.0695 -0.0432 -0.0306 373 SER B CB  
7211 O OG  . SER B 373 ? 0.5018 0.6671 0.4823 -0.0862 -0.0473 -0.0340 373 SER B OG  
7212 N N   . THR B 374 ? 0.2077 0.2723 0.1650 -0.0731 -0.0342 -0.0424 374 THR B N   
7213 C CA  . THR B 374 ? 0.2535 0.2985 0.1938 -0.0834 -0.0311 -0.0505 374 THR B CA  
7214 C C   . THR B 374 ? 0.2582 0.2951 0.1966 -0.0695 -0.0318 -0.0480 374 THR B C   
7215 O O   . THR B 374 ? 0.2965 0.3402 0.2244 -0.0753 -0.0337 -0.0512 374 THR B O   
7216 C CB  . THR B 374 ? 0.2859 0.2921 0.2159 -0.0913 -0.0219 -0.0570 374 THR B CB  
7217 O OG1 . THR B 374 ? 0.2751 0.2885 0.2052 -0.1072 -0.0210 -0.0587 374 THR B OG1 
7218 C CG2 . THR B 374 ? 0.3559 0.3380 0.2668 -0.1001 -0.0170 -0.0670 374 THR B CG2 
7219 N N   . LEU B 375 ? 0.2441 0.2688 0.1919 -0.0525 -0.0302 -0.0423 375 LEU B N   
7220 C CA  . LEU B 375 ? 0.2528 0.2687 0.1991 -0.0411 -0.0299 -0.0395 375 LEU B CA  
7221 C C   . LEU B 375 ? 0.2586 0.3014 0.2075 -0.0366 -0.0371 -0.0330 375 LEU B C   
7222 O O   . LEU B 375 ? 0.3169 0.3581 0.2575 -0.0358 -0.0374 -0.0324 375 LEU B O   
7223 C CB  . LEU B 375 ? 0.2756 0.2767 0.2321 -0.0266 -0.0272 -0.0351 375 LEU B CB  
7224 C CG  . LEU B 375 ? 0.2968 0.2709 0.2502 -0.0265 -0.0196 -0.0390 375 LEU B CG  
7225 C CD1 . LEU B 375 ? 0.3391 0.3090 0.3041 -0.0134 -0.0189 -0.0340 375 LEU B CD1 
7226 C CD2 . LEU B 375 ? 0.3634 0.3184 0.3041 -0.0284 -0.0141 -0.0442 375 LEU B CD2 
7227 N N   . GLU B 376 ? 0.2510 0.3204 0.2108 -0.0329 -0.0427 -0.0272 376 GLU B N   
7228 C CA  . GLU B 376 ? 0.3425 0.4370 0.3050 -0.0252 -0.0492 -0.0188 376 GLU B CA  
7229 C C   . GLU B 376 ? 0.3780 0.4951 0.3293 -0.0388 -0.0531 -0.0214 376 GLU B C   
7230 O O   . GLU B 376 ? 0.3855 0.5227 0.3356 -0.0329 -0.0582 -0.0136 376 GLU B O   
7231 C CB  . GLU B 376 ? 0.3942 0.5115 0.3719 -0.0141 -0.0531 -0.0116 376 GLU B CB  
7232 C CG  . GLU B 376 ? 0.4417 0.5876 0.4240 -0.0250 -0.0556 -0.0140 376 GLU B CG  
7233 C CD  . GLU B 376 ? 0.4201 0.5871 0.4181 -0.0114 -0.0576 -0.0074 376 GLU B CD  
7234 O OE1 . GLU B 376 ? 0.3641 0.5210 0.3682 0.0067  -0.0571 -0.0016 376 GLU B OE1 
7235 O OE2 . GLU B 376 ? 0.4506 0.6443 0.4544 -0.0194 -0.0591 -0.0085 376 GLU B OE2 
7236 N N   . LYS B 377 ? 0.2121 0.3247 0.1536 -0.0573 -0.0505 -0.0320 377 LYS B N   
7237 C CA  . LYS B 377 ? 0.2307 0.3634 0.1589 -0.0735 -0.0538 -0.0373 377 LYS B CA  
7238 C C   . LYS B 377 ? 0.3284 0.4364 0.2387 -0.0793 -0.0488 -0.0452 377 LYS B C   
7239 O O   . LYS B 377 ? 0.4360 0.5627 0.3340 -0.0892 -0.0521 -0.0481 377 LYS B O   
7240 C CB  . LYS B 377 ? 0.3257 0.4703 0.2518 -0.0937 -0.0539 -0.0456 377 LYS B CB  
7241 C CG  . LYS B 377 ? 0.4043 0.5834 0.3484 -0.0885 -0.0587 -0.0370 377 LYS B CG  
7242 C CD  . LYS B 377 ? 0.5530 0.7477 0.4971 -0.1065 -0.0565 -0.0411 377 LYS B CD  
7243 C CE  . LYS B 377 ? 0.6320 0.8371 0.5899 -0.1060 -0.0558 -0.0382 377 LYS B CE  
7244 N NZ  . LYS B 377 ? 0.6886 0.9119 0.6632 -0.0836 -0.0603 -0.0275 377 LYS B NZ  
7245 N N   . GLU B 378 ? 0.2846 0.3552 0.1933 -0.0724 -0.0410 -0.0482 378 GLU B N   
7246 C CA  . GLU B 378 ? 0.2733 0.3225 0.1657 -0.0760 -0.0350 -0.0558 378 GLU B CA  
7247 C C   . GLU B 378 ? 0.2950 0.3544 0.1870 -0.0645 -0.0378 -0.0465 378 GLU B C   
7248 O O   . GLU B 378 ? 0.3165 0.3674 0.2198 -0.0493 -0.0373 -0.0375 378 GLU B O   
7249 C CB  . GLU B 378 ? 0.3064 0.3164 0.1984 -0.0710 -0.0253 -0.0609 378 GLU B CB  
7250 C CG  . GLU B 378 ? 0.3556 0.3501 0.2488 -0.0794 -0.0215 -0.0668 378 GLU B CG  
7251 C CD  . GLU B 378 ? 0.4384 0.4195 0.3124 -0.0992 -0.0167 -0.0808 378 GLU B CD  
7252 O OE1 . GLU B 378 ? 0.5531 0.5107 0.4248 -0.1056 -0.0109 -0.0858 378 GLU B OE1 
7253 O OE2 . GLU B 378 ? 0.4366 0.4296 0.2985 -0.1076 -0.0182 -0.0858 378 GLU B OE2 
7254 N N   . GLU B 379 ? 0.2858 0.3626 0.1634 -0.0730 -0.0404 -0.0489 379 GLU B N   
7255 C CA  . GLU B 379 ? 0.3145 0.4034 0.1900 -0.0633 -0.0431 -0.0383 379 GLU B CA  
7256 C C   . GLU B 379 ? 0.3992 0.4596 0.2712 -0.0556 -0.0349 -0.0392 379 GLU B C   
7257 O O   . GLU B 379 ? 0.3360 0.3993 0.2114 -0.0450 -0.0359 -0.0278 379 GLU B O   
7258 C CB  . GLU B 379 ? 0.3645 0.4818 0.2233 -0.0755 -0.0476 -0.0409 379 GLU B CB  
7259 C CG  . GLU B 379 ? 0.4039 0.5594 0.2707 -0.0788 -0.0565 -0.0343 379 GLU B CG  
7260 C CD  . GLU B 379 ? 0.4674 0.6456 0.3254 -0.0870 -0.0577 -0.0347 379 GLU B CD  
7261 O OE1 . GLU B 379 ? 0.5386 0.7052 0.3816 -0.0905 -0.0530 -0.0402 379 GLU B OE1 
7262 O OE2 . GLU B 379 ? 0.5199 0.7293 0.3858 -0.0901 -0.0627 -0.0299 379 GLU B OE2 
7263 N N   . TRP B 380 ? 0.2754 0.3089 0.1405 -0.0607 -0.0263 -0.0518 380 TRP B N   
7264 C CA  . TRP B 380 ? 0.2925 0.3044 0.1534 -0.0539 -0.0178 -0.0538 380 TRP B CA  
7265 C C   . TRP B 380 ? 0.2973 0.2908 0.1749 -0.0411 -0.0146 -0.0484 380 TRP B C   
7266 O O   . TRP B 380 ? 0.2970 0.2767 0.1741 -0.0347 -0.0078 -0.0489 380 TRP B O   
7267 C CB  . TRP B 380 ? 0.3175 0.3104 0.1606 -0.0640 -0.0091 -0.0705 380 TRP B CB  
7268 C CG  . TRP B 380 ? 0.3475 0.3233 0.1911 -0.0716 -0.0067 -0.0796 380 TRP B CG  
7269 C CD1 . TRP B 380 ? 0.3895 0.3769 0.2279 -0.0868 -0.0114 -0.0854 380 TRP B CD1 
7270 C CD2 . TRP B 380 ? 0.3352 0.2807 0.1847 -0.0649 0.0011  -0.0827 380 TRP B CD2 
7271 N NE1 . TRP B 380 ? 0.3747 0.3380 0.2149 -0.0910 -0.0065 -0.0918 380 TRP B NE1 
7272 C CE2 . TRP B 380 ? 0.4096 0.3462 0.2561 -0.0768 0.0012  -0.0897 380 TRP B CE2 
7273 C CE3 . TRP B 380 ? 0.3081 0.2358 0.1650 -0.0504 0.0079  -0.0793 380 TRP B CE3 
7274 C CZ2 . TRP B 380 ? 0.4243 0.3318 0.2741 -0.0734 0.0083  -0.0924 380 TRP B CZ2 
7275 C CZ3 . TRP B 380 ? 0.3587 0.2612 0.2197 -0.0461 0.0143  -0.0821 380 TRP B CZ3 
7276 C CH2 . TRP B 380 ? 0.4116 0.3026 0.2685 -0.0570 0.0145  -0.0880 380 TRP B CH2 
7277 N N   . ILE B 381 ? 0.2452 0.2412 0.1373 -0.0375 -0.0192 -0.0436 381 ILE B N   
7278 C CA  . ILE B 381 ? 0.2470 0.2304 0.1546 -0.0261 -0.0175 -0.0382 381 ILE B CA  
7279 C C   . ILE B 381 ? 0.2598 0.2575 0.1786 -0.0179 -0.0244 -0.0258 381 ILE B C   
7280 O O   . ILE B 381 ? 0.2721 0.2888 0.1928 -0.0194 -0.0311 -0.0218 381 ILE B O   
7281 C CB  . ILE B 381 ? 0.2661 0.2385 0.1801 -0.0277 -0.0159 -0.0430 381 ILE B CB  
7282 C CG1 . ILE B 381 ? 0.2990 0.2511 0.2003 -0.0351 -0.0079 -0.0547 381 ILE B CG1 
7283 C CG2 . ILE B 381 ? 0.2444 0.2085 0.1736 -0.0160 -0.0150 -0.0371 381 ILE B CG2 
7284 C CD1 . ILE B 381 ? 0.3105 0.2502 0.2155 -0.0386 -0.0060 -0.0581 381 ILE B CD1 
7285 N N   . GLU B 382 ? 0.2280 0.2167 0.1537 -0.0093 -0.0223 -0.0197 382 GLU B N   
7286 C CA  . GLU B 382 ? 0.2508 0.2438 0.1867 -0.0008 -0.0269 -0.0091 382 GLU B CA  
7287 C C   . GLU B 382 ? 0.2215 0.2003 0.1695 0.0051  -0.0243 -0.0102 382 GLU B C   
7288 O O   . GLU B 382 ? 0.2208 0.1890 0.1693 0.0057  -0.0190 -0.0120 382 GLU B O   
7289 C CB  . GLU B 382 ? 0.2417 0.2366 0.1721 0.0013  -0.0268 -0.0003 382 GLU B CB  
7290 C CG  . GLU B 382 ? 0.3791 0.3710 0.3176 0.0102  -0.0300 0.0110  382 GLU B CG  
7291 C CD  . GLU B 382 ? 0.6057 0.6019 0.5358 0.0111  -0.0307 0.0221  382 GLU B CD  
7292 O OE1 . GLU B 382 ? 0.5397 0.5459 0.4577 0.0045  -0.0296 0.0205  382 GLU B OE1 
7293 O OE2 . GLU B 382 ? 0.7821 0.7702 0.7163 0.0182  -0.0319 0.0324  382 GLU B OE2 
7294 N N   . THR B 383 ? 0.2202 0.2022 0.1777 0.0092  -0.0277 -0.0093 383 THR B N   
7295 C CA  . THR B 383 ? 0.1997 0.1710 0.1675 0.0146  -0.0259 -0.0101 383 THR B CA  
7296 C C   . THR B 383 ? 0.2172 0.1820 0.1881 0.0201  -0.0265 -0.0029 383 THR B C   
7297 O O   . THR B 383 ? 0.2376 0.2071 0.2061 0.0235  -0.0299 0.0045  383 THR B O   
7298 C CB  . THR B 383 ? 0.2186 0.1960 0.1943 0.0170  -0.0284 -0.0122 383 THR B CB  
7299 O OG1 . THR B 383 ? 0.2129 0.2045 0.1906 0.0209  -0.0337 -0.0068 383 THR B OG1 
7300 C CG2 . THR B 383 ? 0.2471 0.2256 0.2190 0.0095  -0.0264 -0.0190 383 THR B CG2 
7301 N N   . LEU B 384 ? 0.2118 0.1659 0.1874 0.0206  -0.0231 -0.0046 384 LEU B N   
7302 C CA  . LEU B 384 ? 0.1782 0.1224 0.1553 0.0222  -0.0225 0.0007  384 LEU B CA  
7303 C C   . LEU B 384 ? 0.2046 0.1412 0.1903 0.0252  -0.0224 -0.0027 384 LEU B C   
7304 O O   . LEU B 384 ? 0.1977 0.1381 0.1883 0.0249  -0.0215 -0.0089 384 LEU B O   
7305 C CB  . LEU B 384 ? 0.2287 0.1705 0.2020 0.0164  -0.0179 0.0017  384 LEU B CB  
7306 C CG  . LEU B 384 ? 0.2066 0.1557 0.1694 0.0126  -0.0164 0.0038  384 LEU B CG  
7307 C CD1 . LEU B 384 ? 0.2059 0.1545 0.1672 0.0080  -0.0109 0.0047  384 LEU B CD1 
7308 C CD2 . LEU B 384 ? 0.2488 0.2008 0.2052 0.0147  -0.0204 0.0125  384 LEU B CD2 
7309 N N   . THR B 385 ? 0.2261 0.1507 0.2121 0.0281  -0.0228 0.0016  385 THR B N   
7310 C CA  . THR B 385 ? 0.2008 0.1148 0.1918 0.0276  -0.0214 -0.0032 385 THR B CA  
7311 C C   . THR B 385 ? 0.1930 0.1064 0.1847 0.0185  -0.0179 -0.0051 385 THR B C   
7312 O O   . THR B 385 ? 0.2109 0.1283 0.1985 0.0140  -0.0160 -0.0011 385 THR B O   
7313 C CB  . THR B 385 ? 0.2166 0.1123 0.2055 0.0326  -0.0214 0.0011  385 THR B CB  
7314 O OG1 . THR B 385 ? 0.2697 0.1543 0.2520 0.0281  -0.0194 0.0092  385 THR B OG1 
7315 C CG2 . THR B 385 ? 0.2582 0.1595 0.2475 0.0441  -0.0246 0.0049  385 THR B CG2 
7316 N N   . LEU B 386 ? 0.1860 0.0976 0.1827 0.0154  -0.0170 -0.0114 386 LEU B N   
7317 C CA  . LEU B 386 ? 0.1908 0.1062 0.1893 0.0059  -0.0141 -0.0127 386 LEU B CA  
7318 C C   . LEU B 386 ? 0.2064 0.1080 0.1992 -0.0008 -0.0119 -0.0062 386 LEU B C   
7319 O O   . LEU B 386 ? 0.2358 0.1459 0.2283 -0.0081 -0.0090 -0.0034 386 LEU B O   
7320 C CB  . LEU B 386 ? 0.1867 0.1041 0.1904 0.0023  -0.0144 -0.0207 386 LEU B CB  
7321 C CG  . LEU B 386 ? 0.1800 0.1121 0.1888 0.0082  -0.0162 -0.0260 386 LEU B CG  
7322 C CD1 . LEU B 386 ? 0.1730 0.1092 0.1852 0.0034  -0.0167 -0.0337 386 LEU B CD1 
7323 C CD2 . LEU B 386 ? 0.1957 0.1449 0.2070 0.0097  -0.0148 -0.0239 386 LEU B CD2 
7324 N N   . GLU B 387 ? 0.2542 0.1346 0.2424 0.0023  -0.0124 -0.0028 387 GLU B N   
7325 C CA  . GLU B 387 ? 0.2646 0.1274 0.2457 -0.0034 -0.0097 0.0055  387 GLU B CA  
7326 C C   . GLU B 387 ? 0.2598 0.1333 0.2361 -0.0030 -0.0093 0.0147  387 GLU B C   
7327 O O   . GLU B 387 ? 0.3196 0.1942 0.2927 -0.0124 -0.0059 0.0196  387 GLU B O   
7328 C CB  . GLU B 387 ? 0.3142 0.1503 0.2903 0.0044  -0.0099 0.0090  387 GLU B CB  
7329 C CG  . GLU B 387 ? 0.4804 0.2949 0.4474 0.0011  -0.0069 0.0208  387 GLU B CG  
7330 C CD  . GLU B 387 ? 0.7525 0.5388 0.7158 -0.0093 -0.0026 0.0176  387 GLU B CD  
7331 O OE1 . GLU B 387 ? 0.8805 0.6363 0.8355 -0.0055 0.0000  0.0253  387 GLU B OE1 
7332 O OE2 . GLU B 387 ? 0.7236 0.5182 0.6917 -0.0215 -0.0017 0.0076  387 GLU B OE2 
7333 N N   . GLU B 388 ? 0.2596 0.1430 0.2345 0.0066  -0.0125 0.0165  388 GLU B N   
7334 C CA  . GLU B 388 ? 0.2344 0.1295 0.2026 0.0062  -0.0123 0.0234  388 GLU B CA  
7335 C C   . GLU B 388 ? 0.2621 0.1745 0.2320 -0.0006 -0.0090 0.0189  388 GLU B C   
7336 O O   . GLU B 388 ? 0.2658 0.1840 0.2296 -0.0055 -0.0061 0.0243  388 GLU B O   
7337 C CB  . GLU B 388 ? 0.2639 0.1691 0.2305 0.0156  -0.0167 0.0242  388 GLU B CB  
7338 C CG  . GLU B 388 ? 0.2557 0.1488 0.2208 0.0250  -0.0194 0.0312  388 GLU B CG  
7339 C CD  . GLU B 388 ? 0.3313 0.2403 0.2978 0.0339  -0.0243 0.0308  388 GLU B CD  
7340 O OE1 . GLU B 388 ? 0.3166 0.2394 0.2875 0.0323  -0.0254 0.0220  388 GLU B OE1 
7341 O OE2 . GLU B 388 ? 0.4049 0.3131 0.3682 0.0425  -0.0267 0.0403  388 GLU B OE2 
7342 N N   . ALA B 389 ? 0.2055 0.1273 0.1830 0.0004  -0.0090 0.0096  389 ALA B N   
7343 C CA  . ALA B 389 ? 0.2128 0.1508 0.1925 -0.0028 -0.0051 0.0059  389 ALA B CA  
7344 C C   . ALA B 389 ? 0.2684 0.2097 0.2504 -0.0123 -0.0011 0.0083  389 ALA B C   
7345 O O   . ALA B 389 ? 0.2460 0.2004 0.2260 -0.0155 0.0032  0.0102  389 ALA B O   
7346 C CB  . ALA B 389 ? 0.2252 0.1708 0.2126 0.0018  -0.0058 -0.0023 389 ALA B CB  
7347 N N   . MET B 390 ? 0.2359 0.1660 0.2216 -0.0177 -0.0020 0.0077  390 MET B N   
7348 C CA  . MET B 390 ? 0.2409 0.1744 0.2289 -0.0302 0.0016  0.0094  390 MET B CA  
7349 C C   . MET B 390 ? 0.3104 0.2386 0.2897 -0.0363 0.0048  0.0196  390 MET B C   
7350 O O   . MET B 390 ? 0.2928 0.2358 0.2734 -0.0454 0.0093  0.0221  390 MET B O   
7351 C CB  . MET B 390 ? 0.2755 0.1925 0.2659 -0.0364 0.0001  0.0053  390 MET B CB  
7352 C CG  . MET B 390 ? 0.3091 0.2300 0.3018 -0.0528 0.0035  0.0054  390 MET B CG  
7353 S SD  . MET B 390 ? 0.3802 0.2798 0.3734 -0.0612 0.0019  -0.0033 390 MET B SD  
7354 C CE  . MET B 390 ? 0.4570 0.3129 0.4375 -0.0575 0.0027  0.0045  390 MET B CE  
7355 N N   . ARG B 391 ? 0.3338 0.2441 0.3042 -0.0310 0.0028  0.0267  391 ARG B N   
7356 C CA  . ARG B 391 ? 0.2863 0.1882 0.2471 -0.0368 0.0056  0.0387  391 ARG B CA  
7357 C C   . ARG B 391 ? 0.2907 0.2055 0.2430 -0.0309 0.0056  0.0443  391 ARG B C   
7358 O O   . ARG B 391 ? 0.3152 0.2277 0.2585 -0.0356 0.0082  0.0552  391 ARG B O   
7359 C CB  . ARG B 391 ? 0.4508 0.3207 0.4058 -0.0355 0.0043  0.0454  391 ARG B CB  
7360 C CG  . ARG B 391 ? 0.5296 0.3828 0.4904 -0.0409 0.0044  0.0372  391 ARG B CG  
7361 C CD  . ARG B 391 ? 0.6263 0.4436 0.5803 -0.0364 0.0042  0.0421  391 ARG B CD  
7362 N NE  . ARG B 391 ? 0.7881 0.5844 0.7417 -0.0506 0.0078  0.0378  391 ARG B NE  
7363 C CZ  . ARG B 391 ? 0.9380 0.6986 0.8861 -0.0489 0.0092  0.0372  391 ARG B CZ  
7364 N NH1 . ARG B 391 ? 0.9969 0.7417 0.9411 -0.0311 0.0071  0.0420  391 ARG B NH1 
7365 N NH2 . ARG B 391 ? 0.9607 0.7022 0.9070 -0.0650 0.0130  0.0312  391 ARG B NH2 
7366 N N   . LYS B 392 ? 0.2727 0.2008 0.2263 -0.0221 0.0032  0.0372  392 LYS B N   
7367 C CA  . LYS B 392 ? 0.3006 0.2402 0.2442 -0.0183 0.0029  0.0404  392 LYS B CA  
7368 C C   . LYS B 392 ? 0.3654 0.3200 0.3035 -0.0259 0.0092  0.0440  392 LYS B C   
7369 O O   . LYS B 392 ? 0.3474 0.3149 0.2924 -0.0295 0.0137  0.0380  392 LYS B O   
7370 C CB  . LYS B 392 ? 0.3244 0.2740 0.2701 -0.0111 0.0008  0.0297  392 LYS B CB  
7371 C CG  . LYS B 392 ? 0.3937 0.3527 0.3277 -0.0085 -0.0007 0.0309  392 LYS B CG  
7372 C CD  . LYS B 392 ? 0.5757 0.5337 0.5113 -0.0020 -0.0064 0.0255  392 LYS B CD  
7373 C CE  . LYS B 392 ? 0.5178 0.4692 0.4516 0.0027  -0.0121 0.0352  392 LYS B CE  
7374 N NZ  . LYS B 392 ? 0.5507 0.5125 0.4714 0.0016  -0.0132 0.0443  392 LYS B NZ  
7375 N N   . GLU B 393 ? 0.3232 0.2788 0.2491 -0.0276 0.0097  0.0547  393 GLU B N   
7376 C CA  . GLU B 393 ? 0.3438 0.3148 0.2634 -0.0354 0.0163  0.0593  393 GLU B CA  
7377 C C   . GLU B 393 ? 0.3625 0.3547 0.2769 -0.0319 0.0194  0.0501  393 GLU B C   
7378 O O   . GLU B 393 ? 0.4231 0.4315 0.3388 -0.0356 0.0263  0.0471  393 GLU B O   
7379 C CB  . GLU B 393 ? 0.4265 0.3912 0.3334 -0.0388 0.0162  0.0756  393 GLU B CB  
7380 C CG  . GLU B 393 ? 0.5376 0.4911 0.4455 -0.0504 0.0207  0.0858  393 GLU B CG  
7381 C CD  . GLU B 393 ? 0.8204 0.7583 0.7156 -0.0511 0.0198  0.1040  393 GLU B CD  
7382 O OE1 . GLU B 393 ? 0.9056 0.8580 0.7883 -0.0482 0.0195  0.1110  393 GLU B OE1 
7383 O OE2 . GLU B 393 ? 0.9146 0.8250 0.8113 -0.0542 0.0198  0.1112  393 GLU B OE2 
7384 N N   . ASP B 394 ? 0.3156 0.3082 0.2236 -0.0251 0.0150  0.0452  394 ASP B N   
7385 C CA  . ASP B 394 ? 0.3505 0.3585 0.2486 -0.0234 0.0185  0.0364  394 ASP B CA  
7386 C C   . ASP B 394 ? 0.3448 0.3527 0.2510 -0.0183 0.0211  0.0217  394 ASP B C   
7387 O O   . ASP B 394 ? 0.3185 0.3246 0.2195 -0.0146 0.0196  0.0126  394 ASP B O   
7388 C CB  . ASP B 394 ? 0.3621 0.3724 0.2475 -0.0215 0.0125  0.0382  394 ASP B CB  
7389 C CG  . ASP B 394 ? 0.6276 0.6251 0.5201 -0.0164 0.0041  0.0402  394 ASP B CG  
7390 O OD1 . ASP B 394 ? 0.6718 0.6552 0.5754 -0.0152 0.0027  0.0452  394 ASP B OD1 
7391 O OD2 . ASP B 394 ? 0.6817 0.6847 0.5685 -0.0141 -0.0008 0.0362  394 ASP B OD2 
7392 N N   . VAL B 395 ? 0.2730 0.2834 0.1918 -0.0185 0.0253  0.0200  395 VAL B N   
7393 C CA  . VAL B 395 ? 0.2392 0.2518 0.1661 -0.0118 0.0287  0.0089  395 VAL B CA  
7394 C C   . VAL B 395 ? 0.3089 0.3403 0.2393 -0.0123 0.0378  0.0084  395 VAL B C   
7395 O O   . VAL B 395 ? 0.3243 0.3666 0.2531 -0.0198 0.0406  0.0167  395 VAL B O   
7396 C CB  . VAL B 395 ? 0.2602 0.2622 0.2016 -0.0093 0.0236  0.0076  395 VAL B CB  
7397 C CG1 . VAL B 395 ? 0.2937 0.2807 0.2322 -0.0077 0.0155  0.0079  395 VAL B CG1 
7398 C CG2 . VAL B 395 ? 0.3041 0.3083 0.2552 -0.0164 0.0233  0.0149  395 VAL B CG2 
7399 N N   . LYS B 396 ? 0.2374 0.2735 0.1723 -0.0036 0.0429  -0.0005 396 LYS B N   
7400 C CA  . LYS B 396 ? 0.2400 0.2979 0.1800 -0.0007 0.0521  -0.0012 396 LYS B CA  
7401 C C   . LYS B 396 ? 0.2269 0.2948 0.1858 -0.0016 0.0506  0.0021  396 LYS B C   
7402 O O   . LYS B 396 ? 0.2171 0.2736 0.1836 0.0021  0.0452  -0.0005 396 LYS B O   
7403 C CB  . LYS B 396 ? 0.2470 0.3042 0.1807 0.0115  0.0598  -0.0121 396 LYS B CB  
7404 C CG  . LYS B 396 ? 0.2534 0.3357 0.1908 0.0176  0.0708  -0.0129 396 LYS B CG  
7405 C CD  . LYS B 396 ? 0.3948 0.4702 0.3205 0.0303  0.0800  -0.0244 396 LYS B CD  
7406 C CE  . LYS B 396 ? 0.3469 0.4488 0.2786 0.0405  0.0919  -0.0250 396 LYS B CE  
7407 N NZ  . LYS B 396 ? 0.3146 0.4038 0.2344 0.0557  0.1023  -0.0371 396 LYS B NZ  
7408 N N   . THR B 397 ? 0.2412 0.1465 0.1641 0.0140  -0.0001 -0.0316 397 THR B N   
7409 C CA  . THR B 397 ? 0.2511 0.1564 0.1849 0.0127  0.0034  -0.0266 397 THR B CA  
7410 C C   . THR B 397 ? 0.2883 0.2022 0.2270 0.0102  0.0138  -0.0265 397 THR B C   
7411 O O   . THR B 397 ? 0.3494 0.2663 0.2785 0.0115  0.0191  -0.0296 397 THR B O   
7412 C CB  . THR B 397 ? 0.3187 0.2100 0.2371 0.0112  -0.0004 -0.0187 397 THR B CB  
7413 O OG1 . THR B 397 ? 0.3559 0.2420 0.2552 0.0049  0.0032  -0.0147 397 THR B OG1 
7414 C CG2 . THR B 397 ? 0.3427 0.2271 0.2524 0.0208  -0.0106 -0.0185 397 THR B CG2 
7415 N N   . GLU B 398 ? 0.3000 0.2212 0.2531 0.0083  0.0166  -0.0231 398 GLU B N   
7416 C CA  . GLU B 398 ? 0.2555 0.1953 0.2164 0.0079  0.0259  -0.0214 398 GLU B CA  
7417 C C   . GLU B 398 ? 0.2786 0.2262 0.2483 -0.0006 0.0254  -0.0142 398 GLU B C   
7418 O O   . GLU B 398 ? 0.2409 0.1778 0.2162 -0.0009 0.0193  -0.0140 398 GLU B O   
7419 C CB  . GLU B 398 ? 0.2693 0.2119 0.2393 0.0188  0.0297  -0.0284 398 GLU B CB  
7420 C CG  . GLU B 398 ? 0.2691 0.2349 0.2481 0.0256  0.0390  -0.0266 398 GLU B CG  
7421 C CD  . GLU B 398 ? 0.3897 0.3451 0.3659 0.0408  0.0419  -0.0341 398 GLU B CD  
7422 O OE1 . GLU B 398 ? 0.4430 0.4153 0.4265 0.0521  0.0482  -0.0329 398 GLU B OE1 
7423 O OE2 . GLU B 398 ? 0.4322 0.3612 0.3955 0.0411  0.0372  -0.0409 398 GLU B OE2 
7424 N N   . VAL B 399 ? 0.2790 0.2475 0.2476 -0.0088 0.0317  -0.0082 399 VAL B N   
7425 C CA  . VAL B 399 ? 0.2677 0.2492 0.2430 -0.0212 0.0313  -0.0010 399 VAL B CA  
7426 C C   . VAL B 399 ? 0.2815 0.2929 0.2798 -0.0116 0.0371  -0.0025 399 VAL B C   
7427 O O   . VAL B 399 ? 0.2370 0.2691 0.2394 0.0007  0.0449  -0.0053 399 VAL B O   
7428 C CB  . VAL B 399 ? 0.2986 0.2939 0.2591 -0.0400 0.0343  0.0081  399 VAL B CB  
7429 C CG1 . VAL B 399 ? 0.3200 0.3281 0.2837 -0.0585 0.0323  0.0159  399 VAL B CG1 
7430 C CG2 . VAL B 399 ? 0.2724 0.2325 0.2041 -0.0469 0.0286  0.0103  399 VAL B CG2 
7431 N N   . ILE B 400 ? 0.2069 0.2191 0.2167 -0.0148 0.0331  -0.0007 400 ILE B N   
7432 C CA  . ILE B 400 ? 0.2293 0.2718 0.2589 -0.0063 0.0376  0.0001  400 ILE B CA  
7433 C C   . ILE B 400 ? 0.2357 0.3005 0.2700 -0.0245 0.0355  0.0085  400 ILE B C   
7434 O O   . ILE B 400 ? 0.2654 0.3058 0.2861 -0.0409 0.0284  0.0112  400 ILE B O   
7435 C CB  . ILE B 400 ? 0.2897 0.3140 0.3284 0.0079  0.0345  -0.0060 400 ILE B CB  
7436 C CG1 . ILE B 400 ? 0.3792 0.3777 0.4151 -0.0002 0.0258  -0.0064 400 ILE B CG1 
7437 C CG2 . ILE B 400 ? 0.2861 0.2913 0.3166 0.0223  0.0366  -0.0139 400 ILE B CG2 
7438 C CD1 . ILE B 400 ? 0.4501 0.4394 0.4960 0.0096  0.0232  -0.0103 400 ILE B CD1 
7439 N N   . GLU B 401 ? 0.1912 0.3025 0.2411 -0.0209 0.0414  0.0128  401 GLU B N   
7440 C CA  . GLU B 401 ? 0.1986 0.3424 0.2525 -0.0425 0.0396  0.0219  401 GLU B CA  
7441 C C   . GLU B 401 ? 0.1565 0.3146 0.2269 -0.0385 0.0363  0.0231  401 GLU B C   
7442 O O   . GLU B 401 ? 0.2143 0.3957 0.2858 -0.0595 0.0326  0.0302  401 GLU B O   
7443 C CB  . GLU B 401 ? 0.2105 0.4133 0.2702 -0.0463 0.0483  0.0288  401 GLU B CB  
7444 C CG  . GLU B 401 ? 0.3411 0.5348 0.3833 -0.0507 0.0526  0.0285  401 GLU B CG  
7445 C CD  . GLU B 401 ? 0.4624 0.6255 0.4792 -0.0829 0.0455  0.0344  401 GLU B CD  
7446 O OE1 . GLU B 401 ? 0.4042 0.5575 0.4149 -0.1042 0.0378  0.0392  401 GLU B OE1 
7447 O OE2 . GLU B 401 ? 0.5311 0.6758 0.5293 -0.0866 0.0471  0.0344  401 GLU B OE2 
7448 N N   . SER B 402 ? 0.1736 0.3174 0.2536 -0.0150 0.0367  0.0169  402 SER B N   
7449 C CA  . SER B 402 ? 0.1578 0.3190 0.2526 -0.0090 0.0344  0.0191  402 SER B CA  
7450 C C   . SER B 402 ? 0.2672 0.3930 0.3629 0.0113  0.0330  0.0122  402 SER B C   
7451 O O   . SER B 402 ? 0.2396 0.3468 0.3292 0.0271  0.0368  0.0066  402 SER B O   
7452 C CB  . SER B 402 ? 0.1461 0.3700 0.2565 0.0017  0.0409  0.0254  402 SER B CB  
7453 O OG  . SER B 402 ? 0.2183 0.4625 0.3420 0.0069  0.0376  0.0289  402 SER B OG  
7454 N N   . VAL B 403 ? 0.1592 0.2753 0.2597 0.0084  0.0272  0.0128  403 VAL B N   
7455 C CA  . VAL B 403 ? 0.1754 0.2661 0.2769 0.0245  0.0261  0.0087  403 VAL B CA  
7456 C C   . VAL B 403 ? 0.1900 0.3071 0.3033 0.0331  0.0255  0.0140  403 VAL B C   
7457 O O   . VAL B 403 ? 0.1669 0.3180 0.2883 0.0217  0.0235  0.0201  403 VAL B O   
7458 C CB  . VAL B 403 ? 0.1487 0.2021 0.2428 0.0160  0.0199  0.0042  403 VAL B CB  
7459 C CG1 . VAL B 403 ? 0.2086 0.2396 0.2902 0.0101  0.0196  -0.0002 403 VAL B CG1 
7460 C CG2 . VAL B 403 ? 0.1944 0.2531 0.2894 0.0016  0.0142  0.0073  403 VAL B CG2 
7461 N N   . LYS B 404 ? 0.1910 0.2904 0.3014 0.0523  0.0265  0.0124  404 LYS B N   
7462 C CA  . LYS B 404 ? 0.1686 0.2807 0.2851 0.0625  0.0245  0.0175  404 LYS B CA  
7463 C C   . LYS B 404 ? 0.1586 0.2461 0.2738 0.0499  0.0181  0.0167  404 LYS B C   
7464 O O   . LYS B 404 ? 0.2075 0.2588 0.3134 0.0482  0.0168  0.0118  404 LYS B O   
7465 C CB  . LYS B 404 ? 0.2928 0.3881 0.3982 0.0899  0.0281  0.0168  404 LYS B CB  
7466 C CG  . LYS B 404 ? 0.3413 0.4581 0.4415 0.1037  0.0337  0.0156  404 LYS B CG  
7467 C CD  . LYS B 404 ? 0.4369 0.5483 0.5229 0.1247  0.0331  0.0172  404 LYS B CD  
7468 C CE  . LYS B 404 ? 0.5648 0.7231 0.6536 0.1343  0.0375  0.0205  404 LYS B CE  
7469 N NZ  . LYS B 404 ? 0.6684 0.8769 0.7781 0.1131  0.0380  0.0250  404 LYS B NZ  
7470 N N   . ALA B 405 ? 0.1580 0.2695 0.2817 0.0403  0.0140  0.0216  405 ALA B N   
7471 C CA  . ALA B 405 ? 0.1706 0.2633 0.2913 0.0289  0.0085  0.0202  405 ALA B CA  
7472 C C   . ALA B 405 ? 0.1565 0.2230 0.2713 0.0398  0.0081  0.0202  405 ALA B C   
7473 O O   . ALA B 405 ? 0.1737 0.2417 0.2865 0.0561  0.0095  0.0244  405 ALA B O   
7474 C CB  . ALA B 405 ? 0.1757 0.2987 0.3027 0.0185  0.0040  0.0256  405 ALA B CB  
7475 N N   . GLY B 406 ? 0.1757 0.2184 0.2847 0.0309  0.0058  0.0162  406 GLY B N   
7476 C CA  . GLY B 406 ? 0.1647 0.1849 0.2660 0.0348  0.0050  0.0174  406 GLY B CA  
7477 C C   . GLY B 406 ? 0.1785 0.1892 0.2772 0.0229  0.0027  0.0135  406 GLY B C   
7478 O O   . GLY B 406 ? 0.1548 0.1730 0.2555 0.0161  0.0014  0.0099  406 GLY B O   
7479 N N   . THR B 407 ? 0.1323 0.1261 0.2229 0.0209  0.0021  0.0149  407 THR B N   
7480 C CA  . THR B 407 ? 0.1503 0.1444 0.2392 0.0107  0.0007  0.0124  407 THR B CA  
7481 C C   . THR B 407 ? 0.1583 0.1316 0.2360 0.0054  0.0007  0.0119  407 THR B C   
7482 O O   . THR B 407 ? 0.2253 0.1759 0.2924 0.0111  0.0016  0.0129  407 THR B O   
7483 C CB  . THR B 407 ? 0.1491 0.1535 0.2377 0.0063  -0.0011 0.0172  407 THR B CB  
7484 O OG1 . THR B 407 ? 0.1717 0.1580 0.2492 0.0047  -0.0018 0.0238  407 THR B OG1 
7485 C CG2 . THR B 407 ? 0.2123 0.2323 0.3069 0.0104  -0.0024 0.0190  407 THR B CG2 
7486 N N   . TRP B 408 ? 0.1580 0.1401 0.2351 -0.0056 -0.0006 0.0106  408 TRP B N   
7487 C CA  . TRP B 408 ? 0.1551 0.1202 0.2190 -0.0170 -0.0020 0.0111  408 TRP B CA  
7488 C C   . TRP B 408 ? 0.2475 0.1922 0.2950 -0.0260 -0.0039 0.0189  408 TRP B C   
7489 O O   . TRP B 408 ? 0.2593 0.1844 0.2893 -0.0408 -0.0063 0.0204  408 TRP B O   
7490 C CB  . TRP B 408 ? 0.1815 0.1725 0.2509 -0.0269 -0.0033 0.0080  408 TRP B CB  
7491 C CG  . TRP B 408 ? 0.1214 0.1461 0.1992 -0.0302 -0.0033 0.0103  408 TRP B CG  
7492 C CD1 . TRP B 408 ? 0.1887 0.2198 0.2679 -0.0287 -0.0026 0.0150  408 TRP B CD1 
7493 C CD2 . TRP B 408 ? 0.1073 0.1678 0.1917 -0.0329 -0.0037 0.0078  408 TRP B CD2 
7494 N NE1 . TRP B 408 ? 0.1791 0.2461 0.2642 -0.0304 -0.0019 0.0148  408 TRP B NE1 
7495 C CE2 . TRP B 408 ? 0.1479 0.2355 0.2368 -0.0314 -0.0025 0.0105  408 TRP B CE2 
7496 C CE3 . TRP B 408 ? 0.1305 0.2063 0.2167 -0.0344 -0.0053 0.0037  408 TRP B CE3 
7497 C CZ2 . TRP B 408 ? 0.1441 0.2753 0.2388 -0.0289 -0.0018 0.0089  408 TRP B CZ2 
7498 C CZ3 . TRP B 408 ? 0.1716 0.2924 0.2650 -0.0321 -0.0055 0.0029  408 TRP B CZ3 
7499 C CH2 . TRP B 408 ? 0.1637 0.3129 0.2613 -0.0281 -0.0033 0.0054  408 TRP B CH2 
7500 N N   . PHE B 409 ? 0.2275 0.1730 0.2761 -0.0192 -0.0037 0.0246  409 PHE B N   
7501 C CA  . PHE B 409 ? 0.2934 0.2095 0.3203 -0.0241 -0.0060 0.0331  409 PHE B CA  
7502 C C   . PHE B 409 ? 0.2934 0.1781 0.3082 -0.0042 -0.0054 0.0337  409 PHE B C   
7503 O O   . PHE B 409 ? 0.2812 0.1812 0.3072 0.0118  -0.0043 0.0357  409 PHE B O   
7504 C CB  . PHE B 409 ? 0.3480 0.2853 0.3803 -0.0274 -0.0065 0.0399  409 PHE B CB  
7505 C CG  . PHE B 409 ? 0.5775 0.4915 0.5853 -0.0441 -0.0095 0.0494  409 PHE B CG  
7506 C CD1 . PHE B 409 ? 0.6934 0.5614 0.6743 -0.0373 -0.0121 0.0564  409 PHE B CD1 
7507 C CD2 . PHE B 409 ? 0.6714 0.6100 0.6797 -0.0664 -0.0099 0.0522  409 PHE B CD2 
7508 C CE1 . PHE B 409 ? 0.7735 0.6114 0.7247 -0.0554 -0.0158 0.0663  409 PHE B CE1 
7509 C CE2 . PHE B 409 ? 0.7745 0.6933 0.7578 -0.0871 -0.0129 0.0624  409 PHE B CE2 
7510 C CZ  . PHE B 409 ? 0.8265 0.6900 0.7789 -0.0832 -0.0162 0.0697  409 PHE B CZ  
7511 N N   . ASP B 410 ? 0.3550 0.1986 0.3453 -0.0048 -0.0064 0.0317  410 ASP B N   
7512 C CA  . ASP B 410 ? 0.4220 0.2313 0.3933 0.0180  -0.0055 0.0317  410 ASP B CA  
7513 C C   . ASP B 410 ? 0.3769 0.2195 0.3730 0.0389  -0.0009 0.0271  410 ASP B C   
7514 O O   . ASP B 410 ? 0.4152 0.2504 0.4039 0.0624  0.0007  0.0291  410 ASP B O   
7515 C CB  . ASP B 410 ? 0.5346 0.3168 0.4840 0.0274  -0.0083 0.0416  410 ASP B CB  
7516 C CG  . ASP B 410 ? 0.7135 0.4511 0.6280 0.0045  -0.0134 0.0476  410 ASP B CG  
7517 O OD1 . ASP B 410 ? 0.7533 0.4785 0.6569 -0.0139 -0.0143 0.0421  410 ASP B OD1 
7518 O OD2 . ASP B 410 ? 0.7599 0.4883 0.6626 0.0032  -0.0160 0.0570  410 ASP B OD2 
7519 N N   . GLY B 411 ? 0.3305 0.2106 0.3531 0.0313  0.0010  0.0216  411 GLY B N   
7520 C CA  . GLY B 411 ? 0.2799 0.1898 0.3219 0.0447  0.0047  0.0184  411 GLY B CA  
7521 C C   . GLY B 411 ? 0.3144 0.2544 0.3707 0.0547  0.0047  0.0243  411 GLY B C   
7522 O O   . GLY B 411 ? 0.2758 0.2410 0.3436 0.0660  0.0073  0.0238  411 GLY B O   
7523 N N   . ASN B 412 ? 0.2676 0.2100 0.3232 0.0493  0.0015  0.0304  412 ASN B N   
7524 C CA  . ASN B 412 ? 0.2483 0.2203 0.3155 0.0579  0.0003  0.0363  412 ASN B CA  
7525 C C   . ASN B 412 ? 0.2460 0.2338 0.3209 0.0425  -0.0026 0.0382  412 ASN B C   
7526 O O   . ASN B 412 ? 0.2524 0.2341 0.3259 0.0278  -0.0028 0.0348  412 ASN B O   
7527 C CB  . ASN B 412 ? 0.2674 0.2220 0.3174 0.0790  -0.0006 0.0438  412 ASN B CB  
7528 C CG  . ASN B 412 ? 0.3237 0.2361 0.3476 0.0733  -0.0042 0.0496  412 ASN B CG  
7529 O OD1 . ASN B 412 ? 0.3162 0.2352 0.3435 0.0560  -0.0065 0.0523  412 ASN B OD1 
7530 N ND2 . ASN B 412 ? 0.3637 0.2305 0.3571 0.0885  -0.0047 0.0518  412 ASN B ND2 
7531 N N   . PHE B 413 ? 0.2167 0.2290 0.2986 0.0472  -0.0049 0.0438  413 PHE B N   
7532 C CA  . PHE B 413 ? 0.1804 0.2110 0.2681 0.0348  -0.0076 0.0445  413 PHE B CA  
7533 C C   . PHE B 413 ? 0.2392 0.2612 0.3150 0.0355  -0.0105 0.0533  413 PHE B C   
7534 O O   . PHE B 413 ? 0.2057 0.2460 0.2846 0.0280  -0.0127 0.0548  413 PHE B O   
7535 C CB  . PHE B 413 ? 0.1736 0.2392 0.2750 0.0338  -0.0094 0.0436  413 PHE B CB  
7536 C CG  . PHE B 413 ? 0.1802 0.2511 0.2884 0.0271  -0.0075 0.0356  413 PHE B CG  
7537 C CD1 . PHE B 413 ? 0.1842 0.2486 0.2896 0.0152  -0.0080 0.0285  413 PHE B CD1 
7538 C CD2 . PHE B 413 ? 0.1460 0.2282 0.2603 0.0345  -0.0051 0.0356  413 PHE B CD2 
7539 C CE1 . PHE B 413 ? 0.1902 0.2524 0.2961 0.0100  -0.0071 0.0221  413 PHE B CE1 
7540 C CE2 . PHE B 413 ? 0.1752 0.2601 0.2925 0.0261  -0.0035 0.0295  413 PHE B CE2 
7541 C CZ  . PHE B 413 ? 0.1591 0.2304 0.2708 0.0135  -0.0050 0.0230  413 PHE B CZ  
7542 N N   . LEU B 414 ? 0.2368 0.2265 0.2941 0.0441  -0.0108 0.0592  414 LEU B N   
7543 C CA  . LEU B 414 ? 0.2674 0.2435 0.3078 0.0470  -0.0143 0.0697  414 LEU B CA  
7544 C C   . LEU B 414 ? 0.2903 0.2628 0.3240 0.0261  -0.0149 0.0716  414 LEU B C   
7545 O O   . LEU B 414 ? 0.3135 0.2841 0.3360 0.0249  -0.0178 0.0805  414 LEU B O   
7546 C CB  . LEU B 414 ? 0.3633 0.2934 0.3761 0.0621  -0.0151 0.0752  414 LEU B CB  
7547 C CG  . LEU B 414 ? 0.3234 0.2656 0.3404 0.0900  -0.0143 0.0756  414 LEU B CG  
7548 C CD1 . LEU B 414 ? 0.3276 0.2159 0.3085 0.1106  -0.0154 0.0805  414 LEU B CD1 
7549 C CD2 . LEU B 414 ? 0.3005 0.2894 0.3339 0.0987  -0.0173 0.0818  414 LEU B CD2 
7550 N N   . LYS B 415 ? 0.2446 0.2204 0.2842 0.0107  -0.0122 0.0642  415 LYS B N   
7551 C CA  . LYS B 415 ? 0.2899 0.2761 0.3256 -0.0071 -0.0119 0.0665  415 LYS B CA  
7552 C C   . LYS B 415 ? 0.2139 0.2373 0.2633 -0.0073 -0.0119 0.0638  415 LYS B C   
7553 O O   . LYS B 415 ? 0.2117 0.2489 0.2565 -0.0180 -0.0113 0.0663  415 LYS B O   
7554 C CB  . LYS B 415 ? 0.2606 0.2478 0.2982 -0.0216 -0.0093 0.0603  415 LYS B CB  
7555 C CG  . LYS B 415 ? 0.4736 0.4231 0.4865 -0.0347 -0.0109 0.0664  415 LYS B CG  
7556 C CD  . LYS B 415 ? 0.6149 0.5607 0.6094 -0.0511 -0.0127 0.0777  415 LYS B CD  
7557 C CE  . LYS B 415 ? 0.7626 0.6498 0.7205 -0.0545 -0.0170 0.0875  415 LYS B CE  
7558 N NZ  . LYS B 415 ? 0.7658 0.6432 0.6993 -0.0808 -0.0192 0.0990  415 LYS B NZ  
7559 N N   . TRP B 416 ? 0.2226 0.2622 0.2850 0.0029  -0.0129 0.0590  416 TRP B N   
7560 C CA  . TRP B 416 ? 0.2074 0.2737 0.2755 0.0007  -0.0142 0.0551  416 TRP B CA  
7561 C C   . TRP B 416 ? 0.1938 0.2741 0.2641 0.0077  -0.0188 0.0599  416 TRP B C   
7562 O O   . TRP B 416 ? 0.1811 0.2797 0.2507 0.0033  -0.0211 0.0571  416 TRP B O   
7563 C CB  . TRP B 416 ? 0.1440 0.2176 0.2203 -0.0006 -0.0125 0.0430  416 TRP B CB  
7564 C CG  . TRP B 416 ? 0.1750 0.2438 0.2509 -0.0053 -0.0086 0.0383  416 TRP B CG  
7565 C CD1 . TRP B 416 ? 0.1804 0.2645 0.2529 -0.0096 -0.0064 0.0350  416 TRP B CD1 
7566 C CD2 . TRP B 416 ? 0.1713 0.2241 0.2496 -0.0056 -0.0068 0.0370  416 TRP B CD2 
7567 N NE1 . TRP B 416 ? 0.1613 0.2452 0.2363 -0.0132 -0.0038 0.0323  416 TRP B NE1 
7568 C CE2 . TRP B 416 ? 0.1749 0.2370 0.2526 -0.0123 -0.0044 0.0333  416 TRP B CE2 
7569 C CE3 . TRP B 416 ? 0.1910 0.2252 0.2704 0.0004  -0.0069 0.0382  416 TRP B CE3 
7570 C CZ2 . TRP B 416 ? 0.1476 0.2002 0.2259 -0.0165 -0.0032 0.0312  416 TRP B CZ2 
7571 C CZ3 . TRP B 416 ? 0.2009 0.2198 0.2782 -0.0025 -0.0051 0.0351  416 TRP B CZ3 
7572 C CH2 . TRP B 416 ? 0.1918 0.2195 0.2687 -0.0125 -0.0038 0.0318  416 TRP B CH2 
7573 N N   . ILE B 417 ? 0.1923 0.2667 0.2630 0.0196  -0.0204 0.0667  417 ILE B N   
7574 C CA  . ILE B 417 ? 0.1754 0.2749 0.2513 0.0278  -0.0251 0.0719  417 ILE B CA  
7575 C C   . ILE B 417 ? 0.2673 0.3541 0.3360 0.0467  -0.0261 0.0818  417 ILE B C   
7576 O O   . ILE B 417 ? 0.2960 0.3512 0.3561 0.0528  -0.0229 0.0814  417 ILE B O   
7577 C CB  . ILE B 417 ? 0.1840 0.3075 0.2742 0.0239  -0.0257 0.0643  417 ILE B CB  
7578 C CG1 . ILE B 417 ? 0.2033 0.3629 0.2978 0.0227  -0.0319 0.0690  417 ILE B CG1 
7579 C CG2 . ILE B 417 ? 0.1915 0.3095 0.2894 0.0340  -0.0221 0.0626  417 ILE B CG2 
7580 C CD1 . ILE B 417 ? 0.1526 0.3319 0.2538 0.0092  -0.0340 0.0616  417 ILE B CD1 
7581 N N   . GLY B 418 ? 0.2573 0.3665 0.3255 0.0574  -0.0310 0.0906  418 GLY B N   
7582 C CA  . GLY B 418 ? 0.2534 0.3545 0.3127 0.0824  -0.0324 0.0999  418 GLY B CA  
7583 C C   . GLY B 418 ? 0.3947 0.4666 0.4282 0.0913  -0.0360 0.1120  418 GLY B C   
7584 O O   . GLY B 418 ? 0.4785 0.5382 0.4982 0.1168  -0.0380 0.1201  418 GLY B O   
7585 N N   . ASN B 419 ? 0.3484 0.4072 0.3714 0.0730  -0.0368 0.1138  419 ASN B N   
7586 C CA  . ASN B 419 ? 0.3948 0.4315 0.3919 0.0781  -0.0412 0.1272  419 ASN B CA  
7587 C C   . ASN B 419 ? 0.3192 0.3950 0.3237 0.0677  -0.0452 0.1297  419 ASN B C   
7588 O O   . ASN B 419 ? 0.2896 0.3998 0.3141 0.0548  -0.0444 0.1200  419 ASN B O   
7589 C CB  . ASN B 419 ? 0.4946 0.4779 0.4653 0.0636  -0.0387 0.1299  419 ASN B CB  
7590 C CG  . ASN B 419 ? 0.4791 0.4766 0.4552 0.0354  -0.0359 0.1256  419 ASN B CG  
7591 O OD1 . ASN B 419 ? 0.4184 0.4566 0.4156 0.0282  -0.0350 0.1180  419 ASN B OD1 
7592 N ND2 . ASN B 419 ? 0.5849 0.5477 0.5380 0.0192  -0.0345 0.1307  419 ASN B ND2 
7593 N N   . LYS B 420 ? 0.3656 0.4305 0.3483 0.0736  -0.0501 0.1429  420 LYS B N   
7594 C CA  . LYS B 420 ? 0.3529 0.4567 0.3397 0.0675  -0.0552 0.1465  420 LYS B CA  
7595 C C   . LYS B 420 ? 0.3464 0.4625 0.3393 0.0411  -0.0515 0.1366  420 LYS B C   
7596 O O   . LYS B 420 ? 0.3246 0.4775 0.3307 0.0334  -0.0536 0.1295  420 LYS B O   
7597 C CB  . LYS B 420 ? 0.4315 0.5146 0.3890 0.0784  -0.0610 0.1635  420 LYS B CB  
7598 C CG  . LYS B 420 ? 0.4587 0.5793 0.4173 0.0717  -0.0662 0.1663  420 LYS B CG  
7599 C CD  . LYS B 420 ? 0.6002 0.6897 0.5265 0.0781  -0.0702 0.1790  420 LYS B CD  
7600 C CE  . LYS B 420 ? 0.7300 0.8176 0.6517 0.1056  -0.0752 0.1811  420 LYS B CE  
7601 N NZ  . LYS B 420 ? 0.8070 0.9226 0.7242 0.1080  -0.0816 0.1863  420 LYS B NZ  
7602 N N   . GLU B 421 ? 0.3598 0.4459 0.3402 0.0270  -0.0461 0.1360  421 GLU B N   
7603 C CA  . GLU B 421 ? 0.3349 0.4381 0.3182 0.0071  -0.0420 0.1279  421 GLU B CA  
7604 C C   . GLU B 421 ? 0.2310 0.3501 0.2359 0.0025  -0.0379 0.1110  421 GLU B C   
7605 O O   . GLU B 421 ? 0.2968 0.4392 0.3054 -0.0046 -0.0378 0.1021  421 GLU B O   
7606 C CB  . GLU B 421 ? 0.3890 0.4667 0.3536 -0.0077 -0.0375 0.1338  421 GLU B CB  
7607 C CG  . GLU B 421 ? 0.5680 0.6236 0.5033 -0.0080 -0.0419 0.1517  421 GLU B CG  
7608 C CD  . GLU B 421 ? 0.8055 0.8873 0.7318 -0.0214 -0.0414 0.1550  421 GLU B CD  
7609 O OE1 . GLU B 421 ? 0.9341 1.0007 0.8350 -0.0231 -0.0453 0.1704  421 GLU B OE1 
7610 O OE2 . GLU B 421 ? 0.8572 0.9722 0.7980 -0.0286 -0.0371 0.1424  421 GLU B OE2 
7611 N N   . LYS B 422 ? 0.2165 0.3188 0.2310 0.0071  -0.0348 0.1062  422 LYS B N   
7612 C CA  . LYS B 422 ? 0.1887 0.3029 0.2202 0.0034  -0.0317 0.0914  422 LYS B CA  
7613 C C   . LYS B 422 ? 0.2412 0.3817 0.2836 0.0073  -0.0368 0.0873  422 LYS B C   
7614 O O   . LYS B 422 ? 0.2483 0.3991 0.2940 -0.0009 -0.0365 0.0761  422 LYS B O   
7615 C CB  . LYS B 422 ? 0.2076 0.2986 0.2452 0.0068  -0.0276 0.0879  422 LYS B CB  
7616 C CG  . LYS B 422 ? 0.2330 0.3009 0.2588 -0.0038 -0.0234 0.0906  422 LYS B CG  
7617 C CD  . LYS B 422 ? 0.2548 0.2957 0.2819 -0.0006 -0.0211 0.0880  422 LYS B CD  
7618 C CE  . LYS B 422 ? 0.2819 0.2975 0.2919 -0.0152 -0.0190 0.0929  422 LYS B CE  
7619 N NZ  . LYS B 422 ? 0.2238 0.2665 0.2399 -0.0310 -0.0149 0.0876  422 LYS B NZ  
7620 N N   . ASN B 423 ? 0.2188 0.3704 0.2633 0.0193  -0.0420 0.0968  423 ASN B N   
7621 C CA  . ASN B 423 ? 0.2110 0.3980 0.2661 0.0187  -0.0477 0.0949  423 ASN B CA  
7622 C C   . ASN B 423 ? 0.2483 0.4529 0.2936 0.0054  -0.0524 0.0923  423 ASN B C   
7623 O O   . ASN B 423 ? 0.2108 0.4329 0.2581 -0.0058 -0.0562 0.0844  423 ASN B O   
7624 C CB  . ASN B 423 ? 0.2637 0.4694 0.3235 0.0376  -0.0523 0.1071  423 ASN B CB  
7625 C CG  . ASN B 423 ? 0.3090 0.5073 0.3795 0.0518  -0.0482 0.1060  423 ASN B CG  
7626 O OD1 . ASN B 423 ? 0.2496 0.4296 0.3254 0.0445  -0.0426 0.0962  423 ASN B OD1 
7627 N ND2 . ASN B 423 ? 0.2986 0.5087 0.3689 0.0734  -0.0501 0.1144  423 ASN B ND2 
7628 N N   . GLU B 424 ? 0.2823 0.4796 0.3125 0.0050  -0.0526 0.0989  424 GLU B N   
7629 C CA  . GLU B 424 ? 0.3294 0.5420 0.3466 -0.0063 -0.0565 0.0957  424 GLU B CA  
7630 C C   . GLU B 424 ? 0.3136 0.5158 0.3248 -0.0176 -0.0524 0.0793  424 GLU B C   
7631 O O   . GLU B 424 ? 0.2594 0.4706 0.2591 -0.0271 -0.0571 0.0716  424 GLU B O   
7632 C CB  . GLU B 424 ? 0.3875 0.5938 0.3880 -0.0046 -0.0562 0.1066  424 GLU B CB  
7633 C CG  . GLU B 424 ? 0.4559 0.6768 0.4397 -0.0151 -0.0589 0.1028  424 GLU B CG  
7634 C CD  . GLU B 424 ? 0.6208 0.8708 0.6035 -0.0185 -0.0693 0.1035  424 GLU B CD  
7635 O OE1 . GLU B 424 ? 0.6805 0.9370 0.6487 -0.0302 -0.0721 0.0938  424 GLU B OE1 
7636 O OE2 . GLU B 424 ? 0.6427 0.9106 0.6367 -0.0091 -0.0751 0.1137  424 GLU B OE2 
7637 N N   . TYR B 425 ? 0.2653 0.4469 0.2803 -0.0160 -0.0443 0.0738  425 TYR B N   
7638 C CA  . TYR B 425 ? 0.2405 0.4123 0.2488 -0.0208 -0.0407 0.0584  425 TYR B CA  
7639 C C   . TYR B 425 ? 0.2683 0.4383 0.2794 -0.0261 -0.0454 0.0500  425 TYR B C   
7640 O O   . TYR B 425 ? 0.2598 0.4218 0.2526 -0.0334 -0.0482 0.0391  425 TYR B O   
7641 C CB  . TYR B 425 ? 0.1903 0.3480 0.2048 -0.0171 -0.0320 0.0554  425 TYR B CB  
7642 C CG  . TYR B 425 ? 0.1885 0.3527 0.1917 -0.0183 -0.0265 0.0561  425 TYR B CG  
7643 C CD1 . TYR B 425 ? 0.1961 0.3731 0.1870 -0.0214 -0.0284 0.0646  425 TYR B CD1 
7644 C CD2 . TYR B 425 ? 0.2348 0.3983 0.2395 -0.0164 -0.0192 0.0491  425 TYR B CD2 
7645 C CE1 . TYR B 425 ? 0.2611 0.4504 0.2414 -0.0242 -0.0224 0.0662  425 TYR B CE1 
7646 C CE2 . TYR B 425 ? 0.1828 0.3639 0.1791 -0.0181 -0.0135 0.0507  425 TYR B CE2 
7647 C CZ  . TYR B 425 ? 0.1977 0.3919 0.1815 -0.0227 -0.0147 0.0592  425 TYR B CZ  
7648 O OH  . TYR B 425 ? 0.2375 0.4551 0.2126 -0.0260 -0.0083 0.0617  425 TYR B OH  
7649 N N   . TRP B 426 ? 0.1963 0.3709 0.2260 -0.0231 -0.0462 0.0549  426 TRP B N   
7650 C CA  . TRP B 426 ? 0.1979 0.3764 0.2296 -0.0322 -0.0506 0.0489  426 TRP B CA  
7651 C C   . TRP B 426 ? 0.2946 0.4955 0.3156 -0.0449 -0.0604 0.0506  426 TRP B C   
7652 O O   . TRP B 426 ? 0.2389 0.4303 0.2429 -0.0602 -0.0652 0.0414  426 TRP B O   
7653 C CB  . TRP B 426 ? 0.2128 0.4005 0.2668 -0.0251 -0.0487 0.0548  426 TRP B CB  
7654 C CG  . TRP B 426 ? 0.1394 0.3008 0.1990 -0.0182 -0.0406 0.0496  426 TRP B CG  
7655 C CD1 . TRP B 426 ? 0.1993 0.3493 0.2650 -0.0072 -0.0352 0.0551  426 TRP B CD1 
7656 C CD2 . TRP B 426 ? 0.1495 0.2908 0.2044 -0.0234 -0.0381 0.0383  426 TRP B CD2 
7657 N NE1 . TRP B 426 ? 0.1713 0.3015 0.2398 -0.0065 -0.0296 0.0477  426 TRP B NE1 
7658 C CE2 . TRP B 426 ? 0.1622 0.2878 0.2251 -0.0143 -0.0310 0.0376  426 TRP B CE2 
7659 C CE3 . TRP B 426 ? 0.2591 0.3901 0.2994 -0.0359 -0.0420 0.0292  426 TRP B CE3 
7660 C CZ2 . TRP B 426 ? 0.2281 0.3348 0.2888 -0.0145 -0.0276 0.0284  426 TRP B CZ2 
7661 C CZ3 . TRP B 426 ? 0.2128 0.3174 0.2472 -0.0351 -0.0384 0.0203  426 TRP B CZ3 
7662 C CH2 . TRP B 426 ? 0.2145 0.3107 0.2612 -0.0232 -0.0312 0.0201  426 TRP B CH2 
7663 N N   . LYS B 427 ? 0.2487 0.4763 0.2749 -0.0397 -0.0644 0.0626  427 LYS B N   
7664 C CA  . LYS B 427 ? 0.2294 0.4835 0.2447 -0.0527 -0.0747 0.0649  427 LYS B CA  
7665 C C   . LYS B 427 ? 0.2693 0.4998 0.2534 -0.0647 -0.0767 0.0529  427 LYS B C   
7666 O O   . LYS B 427 ? 0.2771 0.5077 0.2426 -0.0835 -0.0848 0.0464  427 LYS B O   
7667 C CB  . LYS B 427 ? 0.2694 0.5526 0.2917 -0.0408 -0.0783 0.0803  427 LYS B CB  
7668 C CG  . LYS B 427 ? 0.3708 0.6690 0.4156 -0.0234 -0.0747 0.0903  427 LYS B CG  
7669 C CD  . LYS B 427 ? 0.4715 0.7899 0.5154 -0.0116 -0.0768 0.1018  427 LYS B CD  
7670 C CE  . LYS B 427 ? 0.5526 0.8504 0.5932 0.0086  -0.0740 0.1125  427 LYS B CE  
7671 N NZ  . LYS B 427 ? 0.5972 0.8989 0.6222 0.0106  -0.0780 0.1205  427 LYS B NZ  
7672 N N   . ILE B 428 ? 0.2758 0.4861 0.2506 -0.0545 -0.0695 0.0499  428 ILE B N   
7673 C CA  . ILE B 428 ? 0.3637 0.5521 0.3067 -0.0592 -0.0693 0.0375  428 ILE B CA  
7674 C C   . ILE B 428 ? 0.3481 0.5030 0.2737 -0.0660 -0.0695 0.0224  428 ILE B C   
7675 O O   . ILE B 428 ? 0.3872 0.5218 0.2790 -0.0772 -0.0757 0.0119  428 ILE B O   
7676 C CB  . ILE B 428 ? 0.2800 0.4630 0.2211 -0.0454 -0.0596 0.0384  428 ILE B CB  
7677 C CG1 . ILE B 428 ? 0.2854 0.4928 0.2294 -0.0430 -0.0614 0.0528  428 ILE B CG1 
7678 C CG2 . ILE B 428 ? 0.3231 0.4833 0.2327 -0.0432 -0.0564 0.0228  428 ILE B CG2 
7679 C CD1 . ILE B 428 ? 0.2849 0.4906 0.2337 -0.0337 -0.0517 0.0591  428 ILE B CD1 
7680 N N   . LEU B 429 ? 0.2475 0.3911 0.1908 -0.0593 -0.0634 0.0211  429 LEU B N   
7681 C CA  . LEU B 429 ? 0.3111 0.4190 0.2356 -0.0639 -0.0637 0.0081  429 LEU B CA  
7682 C C   . LEU B 429 ? 0.3183 0.4255 0.2318 -0.0872 -0.0743 0.0075  429 LEU B C   
7683 O O   . LEU B 429 ? 0.3717 0.4416 0.2479 -0.0990 -0.0796 -0.0039 429 LEU B O   
7684 C CB  . LEU B 429 ? 0.2969 0.3978 0.2445 -0.0519 -0.0551 0.0086  429 LEU B CB  
7685 C CG  . LEU B 429 ? 0.3202 0.3827 0.2488 -0.0533 -0.0549 -0.0032 429 LEU B CG  
7686 C CD1 . LEU B 429 ? 0.3810 0.4112 0.2733 -0.0423 -0.0529 -0.0165 429 LEU B CD1 
7687 C CD2 . LEU B 429 ? 0.3283 0.3921 0.2839 -0.0438 -0.0478 -0.0004 429 LEU B CD2 
7688 N N   . ILE B 430 ? 0.3045 0.4526 0.2464 -0.0942 -0.0779 0.0201  430 ILE B N   
7689 C CA  . ILE B 430 ? 0.3316 0.4941 0.2670 -0.1197 -0.0881 0.0219  430 ILE B CA  
7690 C C   . ILE B 430 ? 0.3260 0.4807 0.2268 -0.1375 -0.0974 0.0173  430 ILE B C   
7691 O O   . ILE B 430 ? 0.4490 0.5742 0.3225 -0.1569 -0.1009 0.0106  430 ILE B O   
7692 C CB  . ILE B 430 ? 0.2879 0.5062 0.2631 -0.1163 -0.0878 0.0373  430 ILE B CB  
7693 C CG1 . ILE B 430 ? 0.2747 0.4916 0.2755 -0.1032 -0.0796 0.0392  430 ILE B CG1 
7694 C CG2 . ILE B 430 ? 0.3117 0.5483 0.2820 -0.1366 -0.0907 0.0409  430 ILE B CG2 
7695 C CD1 . ILE B 430 ? 0.2700 0.5263 0.3056 -0.0826 -0.0752 0.0526  430 ILE B CD1 
7696 N N   . GLU B 431 ? 0.3508 0.5250 0.2521 -0.1288 -0.0982 0.0215  431 GLU B N   
7697 C CA  . GLU B 431 ? 0.4650 0.6294 0.3365 -0.1419 -0.1038 0.0171  431 GLU B CA  
7698 C C   . GLU B 431 ? 0.4941 0.5967 0.3156 -0.1447 -0.1052 -0.0007 431 GLU B C   
7699 O O   . GLU B 431 ? 0.4939 0.5680 0.2843 -0.1621 -0.1103 -0.0074 431 GLU B O   
7700 C CB  . GLU B 431 ? 0.4331 0.6299 0.3151 -0.1296 -0.1035 0.0258  431 GLU B CB  
7701 C CG  . GLU B 431 ? 0.5647 0.8123 0.4778 -0.1309 -0.1047 0.0411  431 GLU B CG  
7702 C CD  . GLU B 431 ? 0.6858 0.9405 0.5901 -0.1559 -0.1099 0.0407  431 GLU B CD  
7703 O OE1 . GLU B 431 ? 0.6932 0.9780 0.6221 -0.1592 -0.1078 0.0490  431 GLU B OE1 
7704 O OE2 . GLU B 431 ? 0.7403 0.9700 0.6104 -0.1721 -0.1156 0.0322  431 GLU B OE2 
7705 N N   . ALA B 432 ? 0.4743 0.5540 0.2883 -0.1243 -0.0983 -0.0080 432 ALA B N   
7706 C CA  . ALA B 432 ? 0.4760 0.4965 0.2412 -0.1173 -0.0969 -0.0254 432 ALA B CA  
7707 C C   . ALA B 432 ? 0.4837 0.4555 0.2250 -0.1292 -0.1001 -0.0337 432 ALA B C   
7708 O O   . ALA B 432 ? 0.5549 0.4738 0.2524 -0.1303 -0.1019 -0.0456 432 ALA B O   
7709 C CB  . ALA B 432 ? 0.4147 0.4338 0.1927 -0.0849 -0.0828 -0.0282 432 ALA B CB  
7710 N N   . LYS B 433 ? 0.4462 0.4340 0.2184 -0.1347 -0.0989 -0.0264 433 LYS B N   
7711 C CA  . LYS B 433 ? 0.5036 0.4484 0.2582 -0.1459 -0.0997 -0.0310 433 LYS B CA  
7712 C C   . LYS B 433 ? 0.5472 0.4779 0.2799 -0.1725 -0.1061 -0.0291 433 LYS B C   
7713 O O   . LYS B 433 ? 0.6056 0.4788 0.2988 -0.1792 -0.1076 -0.0362 433 LYS B O   
7714 C CB  . LYS B 433 ? 0.4703 0.4464 0.2664 -0.1488 -0.0969 -0.0214 433 LYS B CB  
7715 C CG  . LYS B 433 ? 0.5327 0.4715 0.3138 -0.1619 -0.0967 -0.0228 433 LYS B CG  
7716 C CD  . LYS B 433 ? 0.5430 0.4134 0.2846 -0.1444 -0.0938 -0.0366 433 LYS B CD  
7717 C CE  . LYS B 433 ? 0.5990 0.4298 0.3210 -0.1587 -0.0943 -0.0349 433 LYS B CE  
7718 N NZ  . LYS B 433 ? 0.6333 0.3950 0.3129 -0.1385 -0.0919 -0.0461 433 LYS B NZ  
7719 N N   . LYS B 434 ? 0.5623 0.5446 0.3178 -0.1870 -0.1097 -0.0182 434 LYS B N   
7720 C CA  . LYS B 434 ? 0.5326 0.5081 0.2661 -0.2147 -0.1159 -0.0152 434 LYS B CA  
7721 C C   . LYS B 434 ? 0.6517 0.5655 0.3298 -0.2145 -0.1199 -0.0288 434 LYS B C   
7722 O O   . LYS B 434 ? 0.7173 0.5947 0.3608 -0.2371 -0.1247 -0.0295 434 LYS B O   
7723 C CB  . LYS B 434 ? 0.6425 0.6868 0.4080 -0.2236 -0.1184 -0.0022 434 LYS B CB  
7724 C CG  . LYS B 434 ? 0.5983 0.7079 0.4156 -0.2220 -0.1142 0.0128  434 LYS B CG  
7725 C CD  . LYS B 434 ? 0.5938 0.7641 0.4346 -0.2235 -0.1164 0.0242  434 LYS B CD  
7726 C CE  . LYS B 434 ? 0.5662 0.8003 0.4507 -0.2204 -0.1118 0.0393  434 LYS B CE  
7727 N NZ  . LYS B 434 ? 0.5940 0.8360 0.5091 -0.1945 -0.1048 0.0408  434 LYS B NZ  
7728 N N   . LYS B 435 ? 0.6544 0.5577 0.3215 -0.1891 -0.1173 -0.0385 435 LYS B N   
7729 C CA  . LYS B 435 ? 0.6787 0.5310 0.2951 -0.1823 -0.1195 -0.0520 435 LYS B CA  
7730 C C   . LYS B 435 ? 0.7410 0.5378 0.3277 -0.1533 -0.1130 -0.0660 435 LYS B C   
7731 O O   . LYS B 435 ? 0.7704 0.5345 0.3208 -0.1362 -0.1117 -0.0778 435 LYS B O   
7732 C CB  . LYS B 435 ? 0.7214 0.6107 0.3441 -0.1737 -0.1204 -0.0518 435 LYS B CB  
7733 C CG  . LYS B 435 ? 0.7459 0.7060 0.4122 -0.1905 -0.1240 -0.0352 435 LYS B CG  
7734 C CD  . LYS B 435 ? 0.8043 0.7909 0.4677 -0.1833 -0.1258 -0.0346 435 LYS B CD  
7735 C CE  . LYS B 435 ? 0.7988 0.8594 0.5138 -0.1830 -0.1253 -0.0170 435 LYS B CE  
7736 N NZ  . LYS B 435 ? 0.8156 0.9001 0.5245 -0.1817 -0.1286 -0.0142 435 LYS B NZ  
7737 N N   . ALA B 436 ? 0.4282 0.4652 0.3645 -0.1882 -0.1188 -0.0797 436 ALA B N   
7738 C CA  . ALA B 436 ? 0.4345 0.4161 0.3471 -0.1757 -0.1115 -0.0853 436 ALA B CA  
7739 C C   . ALA B 436 ? 0.5376 0.4537 0.4390 -0.1903 -0.1140 -0.1018 436 ALA B C   
7740 O O   . ALA B 436 ? 0.5523 0.4598 0.4690 -0.2161 -0.1171 -0.0970 436 ALA B O   
7741 C CB  . ALA B 436 ? 0.4057 0.3899 0.3276 -0.1718 -0.1024 -0.0623 436 ALA B CB  
7742 N N   . LYS B 437 ? 0.5217 0.3926 0.3993 -0.1720 -0.1114 -0.1216 437 LYS B N   
7743 C CA  . LYS B 437 ? 0.6396 0.4443 0.5099 -0.1778 -0.1129 -0.1414 437 LYS B CA  
7744 C C   . LYS B 437 ? 0.6362 0.3785 0.4971 -0.1577 -0.1056 -0.1382 437 LYS B C   
7745 O O   . LYS B 437 ? 0.7170 0.3991 0.5785 -0.1592 -0.1061 -0.1489 437 LYS B O   
7746 C CB  . LYS B 437 ? 0.7111 0.5183 0.5667 -0.1713 -0.1177 -0.1768 437 LYS B CB  
7747 C CG  . LYS B 437 ? 0.7030 0.5753 0.5591 -0.1792 -0.1281 -0.1774 437 LYS B CG  
7748 C CD  . LYS B 437 ? 0.7266 0.6104 0.6039 -0.2115 -0.1394 -0.1739 437 LYS B CD  
7749 C CE  . LYS B 437 ? 0.8009 0.7344 0.6731 -0.2170 -0.1536 -0.1832 437 LYS B CE  
7750 N NZ  . LYS B 437 ? 0.7651 0.7606 0.6400 -0.2014 -0.1524 -0.1606 437 LYS B NZ  
7751 N N   . ASN B 438 ? 0.5604 0.3146 0.4157 -0.1367 -0.1004 -0.1233 438 ASN B N   
7752 C CA  . ASN B 438 ? 0.5952 0.2991 0.4475 -0.1104 -0.0959 -0.1182 438 ASN B CA  
7753 C C   . ASN B 438 ? 0.5798 0.3246 0.4454 -0.0949 -0.0879 -0.0867 438 ASN B C   
7754 O O   . ASN B 438 ? 0.5473 0.3499 0.4212 -0.1033 -0.0856 -0.0738 438 ASN B O   
7755 C CB  . ASN B 438 ? 0.6338 0.3260 0.4746 -0.0812 -0.0897 -0.1492 438 ASN B CB  
7756 C CG  . ASN B 438 ? 0.5451 0.3037 0.3769 -0.0715 -0.0837 -0.1564 438 ASN B CG  
7757 O OD1 . ASN B 438 ? 0.5006 0.2996 0.3436 -0.0569 -0.0768 -0.1347 438 ASN B OD1 
7758 N ND2 . ASN B 438 ? 0.5948 0.3769 0.4152 -0.0787 -0.0825 -0.1820 438 ASN B ND2 
7759 N N   . ASP B 439 ? 0.5284 0.2431 0.3971 -0.0703 -0.0850 -0.0763 439 ASP B N   
7760 C CA  . ASP B 439 ? 0.4912 0.2367 0.3687 -0.0585 -0.0800 -0.0484 439 ASP B CA  
7761 C C   . ASP B 439 ? 0.4591 0.2604 0.3415 -0.0382 -0.0721 -0.0528 439 ASP B C   
7762 O O   . ASP B 439 ? 0.4123 0.2394 0.3017 -0.0289 -0.0685 -0.0345 439 ASP B O   
7763 C CB  . ASP B 439 ? 0.5780 0.2751 0.4566 -0.0405 -0.0841 -0.0340 439 ASP B CB  
7764 C CG  . ASP B 439 ? 0.6570 0.3065 0.5296 -0.0651 -0.0914 -0.0124 439 ASP B CG  
7765 O OD1 . ASP B 439 ? 0.6146 0.2814 0.4864 -0.0978 -0.0903 -0.0072 439 ASP B OD1 
7766 O OD2 . ASP B 439 ? 0.8021 0.3993 0.6730 -0.0525 -0.0987 0.0012  439 ASP B OD2 
7767 N N   . TYR B 440 ? 0.4477 0.2676 0.3239 -0.0333 -0.0694 -0.0762 440 TYR B N   
7768 C CA  . TYR B 440 ? 0.3616 0.2344 0.2416 -0.0209 -0.0622 -0.0737 440 TYR B CA  
7769 C C   . TYR B 440 ? 0.4070 0.3211 0.2951 -0.0351 -0.0629 -0.0552 440 TYR B C   
7770 O O   . TYR B 440 ? 0.3360 0.2838 0.2314 -0.0245 -0.0580 -0.0463 440 TYR B O   
7771 C CB  . TYR B 440 ? 0.3922 0.2806 0.2580 -0.0169 -0.0587 -0.0983 440 TYR B CB  
7772 C CG  . TYR B 440 ? 0.4763 0.3553 0.3435 0.0092  -0.0497 -0.1135 440 TYR B CG  
7773 C CD1 . TYR B 440 ? 0.4912 0.4029 0.3724 0.0262  -0.0418 -0.1022 440 TYR B CD1 
7774 C CD2 . TYR B 440 ? 0.5117 0.3505 0.3705 0.0168  -0.0490 -0.1412 440 TYR B CD2 
7775 C CE1 . TYR B 440 ? 0.5618 0.4761 0.4520 0.0495  -0.0327 -0.1159 440 TYR B CE1 
7776 C CE2 . TYR B 440 ? 0.5620 0.3998 0.4291 0.0446  -0.0388 -0.1575 440 TYR B CE2 
7777 C CZ  . TYR B 440 ? 0.6179 0.4984 0.5026 0.0605  -0.0305 -0.1435 440 TYR B CZ  
7778 O OH  . TYR B 440 ? 0.6652 0.5562 0.5655 0.0874  -0.0195 -0.1590 440 TYR B OH  
7779 N N   . ILE B 441 ? 0.3690 0.2814 0.2597 -0.0587 -0.0684 -0.0498 441 ILE B N   
7780 C CA  . ILE B 441 ? 0.3197 0.2761 0.2253 -0.0675 -0.0669 -0.0336 441 ILE B CA  
7781 C C   . ILE B 441 ? 0.2978 0.2553 0.2097 -0.0578 -0.0600 -0.0160 441 ILE B C   
7782 O O   . ILE B 441 ? 0.2731 0.2666 0.1963 -0.0521 -0.0552 -0.0081 441 ILE B O   
7783 C CB  . ILE B 441 ? 0.3219 0.2868 0.2349 -0.0967 -0.0731 -0.0326 441 ILE B CB  
7784 C CG1 . ILE B 441 ? 0.2913 0.3154 0.2266 -0.1002 -0.0716 -0.0215 441 ILE B CG1 
7785 C CG2 . ILE B 441 ? 0.3773 0.3029 0.2886 -0.1126 -0.0723 -0.0220 441 ILE B CG2 
7786 C CD1 . ILE B 441 ? 0.2834 0.3426 0.2197 -0.0920 -0.0783 -0.0281 441 ILE B CD1 
7787 N N   . LEU B 442 ? 0.3005 0.2175 0.2041 -0.0545 -0.0608 -0.0104 442 LEU B N   
7788 C CA  . LEU B 442 ? 0.3257 0.2462 0.2287 -0.0452 -0.0570 0.0055  442 LEU B CA  
7789 C C   . LEU B 442 ? 0.3268 0.2670 0.2347 -0.0224 -0.0543 0.0008  442 LEU B C   
7790 O O   . LEU B 442 ? 0.2972 0.2602 0.2085 -0.0179 -0.0505 0.0083  442 LEU B O   
7791 C CB  . LEU B 442 ? 0.3321 0.2037 0.2236 -0.0451 -0.0627 0.0164  442 LEU B CB  
7792 C CG  . LEU B 442 ? 0.3793 0.2169 0.2643 -0.0713 -0.0665 0.0247  442 LEU B CG  
7793 C CD1 . LEU B 442 ? 0.4658 0.2469 0.3389 -0.0661 -0.0746 0.0398  442 LEU B CD1 
7794 C CD2 . LEU B 442 ? 0.4069 0.2824 0.2954 -0.0948 -0.0587 0.0386  442 LEU B CD2 
7795 N N   . VAL B 443 ? 0.2834 0.2156 0.1916 -0.0096 -0.0553 -0.0131 443 VAL B N   
7796 C CA  . VAL B 443 ? 0.2939 0.2489 0.2098 0.0075  -0.0515 -0.0162 443 VAL B CA  
7797 C C   . VAL B 443 ? 0.3022 0.2932 0.2249 0.0031  -0.0475 -0.0129 443 VAL B C   
7798 O O   . VAL B 443 ? 0.2431 0.2498 0.1734 0.0099  -0.0451 -0.0080 443 VAL B O   
7799 C CB  . VAL B 443 ? 0.3231 0.2721 0.2381 0.0192  -0.0493 -0.0332 443 VAL B CB  
7800 C CG1 . VAL B 443 ? 0.2462 0.2252 0.1724 0.0320  -0.0434 -0.0336 443 VAL B CG1 
7801 C CG2 . VAL B 443 ? 0.3425 0.2500 0.2563 0.0288  -0.0538 -0.0389 443 VAL B CG2 
7802 N N   . ALA B 444 ? 0.2708 0.2735 0.1922 -0.0081 -0.0489 -0.0159 444 ALA B N   
7803 C CA  . ALA B 444 ? 0.2639 0.2983 0.1952 -0.0092 -0.0482 -0.0104 444 ALA B CA  
7804 C C   . ALA B 444 ? 0.2822 0.3297 0.2258 -0.0113 -0.0452 -0.0019 444 ALA B C   
7805 O O   . ALA B 444 ? 0.2608 0.3296 0.2176 -0.0061 -0.0439 0.0016  444 ALA B O   
7806 C CB  . ALA B 444 ? 0.2804 0.3287 0.2083 -0.0203 -0.0544 -0.0146 444 ALA B CB  
7807 N N   . GLU B 445 ? 0.2165 0.2511 0.1550 -0.0182 -0.0434 0.0015  445 GLU B N   
7808 C CA  . GLU B 445 ? 0.2172 0.2693 0.1620 -0.0206 -0.0369 0.0070  445 GLU B CA  
7809 C C   . GLU B 445 ? 0.2447 0.2932 0.1847 -0.0089 -0.0343 0.0065  445 GLU B C   
7810 O O   . GLU B 445 ? 0.2508 0.3142 0.1917 -0.0091 -0.0277 0.0061  445 GLU B O   
7811 C CB  . GLU B 445 ? 0.2750 0.3193 0.2116 -0.0382 -0.0351 0.0141  445 GLU B CB  
7812 C CG  . GLU B 445 ? 0.2492 0.3121 0.1994 -0.0549 -0.0368 0.0132  445 GLU B CG  
7813 C CD  . GLU B 445 ? 0.2927 0.3344 0.2338 -0.0779 -0.0382 0.0201  445 GLU B CD  
7814 O OE1 . GLU B 445 ? 0.2772 0.2922 0.2007 -0.0808 -0.0364 0.0303  445 GLU B OE1 
7815 O OE2 . GLU B 445 ? 0.3119 0.3632 0.2635 -0.0950 -0.0430 0.0168  445 GLU B OE2 
7816 N N   . GLY B 446 ? 0.2388 0.2728 0.1750 0.0006  -0.0388 0.0042  446 GLY B N   
7817 C CA  . GLY B 446 ? 0.2221 0.2569 0.1568 0.0082  -0.0393 0.0028  446 GLY B CA  
7818 C C   . GLY B 446 ? 0.2686 0.3186 0.2156 0.0120  -0.0349 -0.0027 446 GLY B C   
7819 O O   . GLY B 446 ? 0.2840 0.3414 0.2443 0.0142  -0.0339 -0.0027 446 GLY B O   
7820 N N   . SER B 447 ? 0.2306 0.2828 0.1715 0.0130  -0.0339 -0.0076 447 SER B N   
7821 C CA  . SER B 447 ? 0.2583 0.3172 0.2105 0.0173  -0.0290 -0.0173 447 SER B CA  
7822 C C   . SER B 447 ? 0.2268 0.2777 0.1949 0.0213  -0.0328 -0.0177 447 SER B C   
7823 O O   . SER B 447 ? 0.1881 0.2368 0.1714 0.0262  -0.0305 -0.0203 447 SER B O   
7824 C CB  . SER B 447 ? 0.2260 0.2876 0.1623 0.0154  -0.0274 -0.0275 447 SER B CB  
7825 O OG  . SER B 447 ? 0.2244 0.2795 0.1535 0.0139  -0.0374 -0.0279 447 SER B OG  
7826 N N   . ASP B 448 ? 0.1807 0.2282 0.1476 0.0197  -0.0383 -0.0136 448 ASP B N   
7827 C CA  . ASP B 448 ? 0.2063 0.2512 0.1872 0.0184  -0.0399 -0.0124 448 ASP B CA  
7828 C C   . ASP B 448 ? 0.1861 0.2293 0.1764 0.0199  -0.0377 -0.0034 448 ASP B C   
7829 O O   . ASP B 448 ? 0.1787 0.2124 0.1806 0.0185  -0.0382 -0.0004 448 ASP B O   
7830 C CB  . ASP B 448 ? 0.1666 0.2200 0.1493 0.0173  -0.0432 -0.0096 448 ASP B CB  
7831 C CG  . ASP B 448 ? 0.1918 0.2492 0.1666 0.0182  -0.0500 -0.0139 448 ASP B CG  
7832 O OD1 . ASP B 448 ? 0.2080 0.2607 0.1682 0.0213  -0.0512 -0.0106 448 ASP B OD1 
7833 O OD2 . ASP B 448 ? 0.1878 0.2527 0.1706 0.0139  -0.0556 -0.0189 448 ASP B OD2 
7834 N N   . TRP B 449 ? 0.2009 0.2512 0.1848 0.0210  -0.0371 0.0021  449 TRP B N   
7835 C CA  . TRP B 449 ? 0.1762 0.2303 0.1643 0.0214  -0.0386 0.0127  449 TRP B CA  
7836 C C   . TRP B 449 ? 0.2128 0.2618 0.2168 0.0281  -0.0401 0.0152  449 TRP B C   
7837 O O   . TRP B 449 ? 0.2165 0.2574 0.2289 0.0296  -0.0435 0.0268  449 TRP B O   
7838 C CB  . TRP B 449 ? 0.1874 0.2522 0.1643 0.0192  -0.0403 0.0138  449 TRP B CB  
7839 C CG  . TRP B 449 ? 0.2151 0.2762 0.1793 0.0170  -0.0385 0.0063  449 TRP B CG  
7840 C CD1 . TRP B 449 ? 0.2182 0.2732 0.1749 0.0148  -0.0394 0.0012  449 TRP B CD1 
7841 C CD2 . TRP B 449 ? 0.2009 0.2636 0.1627 0.0180  -0.0356 0.0039  449 TRP B CD2 
7842 N NE1 . TRP B 449 ? 0.2634 0.3090 0.2129 0.0173  -0.0392 -0.0039 449 TRP B NE1 
7843 C CE2 . TRP B 449 ? 0.1898 0.2444 0.1445 0.0210  -0.0361 -0.0041 449 TRP B CE2 
7844 C CE3 . TRP B 449 ? 0.1842 0.2560 0.1517 0.0161  -0.0318 0.0087  449 TRP B CE3 
7845 C CZ2 . TRP B 449 ? 0.2278 0.2858 0.1850 0.0271  -0.0333 -0.0101 449 TRP B CZ2 
7846 C CZ3 . TRP B 449 ? 0.2291 0.3117 0.1986 0.0183  -0.0268 0.0028  449 TRP B CZ3 
7847 C CH2 . TRP B 449 ? 0.1908 0.2678 0.1571 0.0263  -0.0277 -0.0080 449 TRP B CH2 
7848 N N   . PHE B 450 ? 0.1851 0.2390 0.1941 0.0329  -0.0370 0.0052  450 PHE B N   
7849 C CA  . PHE B 450 ? 0.2108 0.2644 0.2404 0.0442  -0.0362 0.0026  450 PHE B CA  
7850 C C   . PHE B 450 ? 0.2000 0.2277 0.2372 0.0477  -0.0352 -0.0057 450 PHE B C   
7851 O O   . PHE B 450 ? 0.2215 0.2348 0.2784 0.0584  -0.0375 -0.0034 450 PHE B O   
7852 C CB  . PHE B 450 ? 0.2199 0.2951 0.2527 0.0467  -0.0289 -0.0082 450 PHE B CB  
7853 C CG  . PHE B 450 ? 0.2372 0.3337 0.2635 0.0378  -0.0308 -0.0012 450 PHE B CG  
7854 C CD1 . PHE B 450 ? 0.2542 0.3457 0.2579 0.0259  -0.0298 -0.0021 450 PHE B CD1 
7855 C CD2 . PHE B 450 ? 0.2090 0.3286 0.2537 0.0412  -0.0360 0.0066  450 PHE B CD2 
7856 C CE1 . PHE B 450 ? 0.2642 0.3656 0.2621 0.0158  -0.0324 0.0022  450 PHE B CE1 
7857 C CE2 . PHE B 450 ? 0.2370 0.3747 0.2758 0.0288  -0.0396 0.0102  450 PHE B CE2 
7858 C CZ  . PHE B 450 ? 0.1866 0.3114 0.2011 0.0151  -0.0371 0.0070  450 PHE B CZ  
7859 N N   . TRP B 451 ? 0.2017 0.2219 0.2250 0.0386  -0.0337 -0.0155 451 TRP B N   
7860 C CA  . TRP B 451 ? 0.2812 0.2770 0.3100 0.0360  -0.0351 -0.0259 451 TRP B CA  
7861 C C   . TRP B 451 ? 0.2681 0.2418 0.3107 0.0327  -0.0405 -0.0097 451 TRP B C   
7862 O O   . TRP B 451 ? 0.2780 0.2227 0.3362 0.0379  -0.0424 -0.0132 451 TRP B O   
7863 C CB  . TRP B 451 ? 0.3007 0.3028 0.3133 0.0240  -0.0370 -0.0340 451 TRP B CB  
7864 C CG  . TRP B 451 ? 0.4922 0.4793 0.5030 0.0196  -0.0386 -0.0543 451 TRP B CG  
7865 C CD1 . TRP B 451 ? 0.6061 0.5985 0.6019 0.0223  -0.0348 -0.0747 451 TRP B CD1 
7866 C CD2 . TRP B 451 ? 0.5135 0.4795 0.5354 0.0082  -0.0446 -0.0577 451 TRP B CD2 
7867 N NE1 . TRP B 451 ? 0.6366 0.6112 0.6309 0.0147  -0.0393 -0.0941 451 TRP B NE1 
7868 C CE2 . TRP B 451 ? 0.5794 0.5359 0.5922 0.0049  -0.0462 -0.0839 451 TRP B CE2 
7869 C CE3 . TRP B 451 ? 0.4930 0.4490 0.5301 -0.0024 -0.0482 -0.0410 451 TRP B CE3 
7870 C CZ2 . TRP B 451 ? 0.6511 0.5850 0.6724 -0.0094 -0.0535 -0.0960 451 TRP B CZ2 
7871 C CZ3 . TRP B 451 ? 0.6109 0.5459 0.6588 -0.0178 -0.0537 -0.0491 451 TRP B CZ3 
7872 C CH2 . TRP B 451 ? 0.6647 0.5871 0.7060 -0.0216 -0.0575 -0.0774 451 TRP B CH2 
7873 N N   . TRP B 452 ? 0.2270 0.2124 0.2628 0.0239  -0.0423 0.0083  452 TRP B N   
7874 C CA  . TRP B 452 ? 0.2649 0.2343 0.3077 0.0149  -0.0455 0.0272  452 TRP B CA  
7875 C C   . TRP B 452 ? 0.2768 0.2381 0.3261 0.0248  -0.0506 0.0472  452 TRP B C   
7876 O O   . TRP B 452 ? 0.2667 0.2013 0.3248 0.0210  -0.0553 0.0643  452 TRP B O   
7877 C CB  . TRP B 452 ? 0.2359 0.2294 0.2675 0.0015  -0.0422 0.0364  452 TRP B CB  
7878 C CG  . TRP B 452 ? 0.2790 0.2832 0.3120 -0.0068 -0.0408 0.0208  452 TRP B CG  
7879 C CD1 . TRP B 452 ? 0.2186 0.2464 0.2423 -0.0034 -0.0394 0.0111  452 TRP B CD1 
7880 C CD2 . TRP B 452 ? 0.2440 0.2355 0.2904 -0.0203 -0.0435 0.0142  452 TRP B CD2 
7881 N NE1 . TRP B 452 ? 0.2089 0.2440 0.2399 -0.0112 -0.0425 0.0005  452 TRP B NE1 
7882 C CE2 . TRP B 452 ? 0.2154 0.2317 0.2604 -0.0235 -0.0450 0.0008  452 TRP B CE2 
7883 C CE3 . TRP B 452 ? 0.3326 0.2916 0.3931 -0.0310 -0.0466 0.0189  452 TRP B CE3 
7884 C CZ2 . TRP B 452 ? 0.2755 0.2936 0.3332 -0.0381 -0.0504 -0.0093 452 TRP B CZ2 
7885 C CZ3 . TRP B 452 ? 0.3764 0.3311 0.4488 -0.0482 -0.0505 0.0070  452 TRP B CZ3 
7886 C CH2 . TRP B 452 ? 0.3217 0.3099 0.3928 -0.0521 -0.0528 -0.0077 452 TRP B CH2 
7887 N N   . GLN B 453 ? 0.2716 0.2556 0.3183 0.0363  -0.0517 0.0471  453 GLN B N   
7888 C CA  . GLN B 453 ? 0.2992 0.2857 0.3535 0.0464  -0.0604 0.0674  453 GLN B CA  
7889 C C   . GLN B 453 ? 0.3410 0.2963 0.4230 0.0629  -0.0650 0.0672  453 GLN B C   
7890 O O   . GLN B 453 ? 0.3394 0.2872 0.4348 0.0727  -0.0591 0.0429  453 GLN B O   
7891 C CB  . GLN B 453 ? 0.2529 0.2760 0.3031 0.0520  -0.0615 0.0630  453 GLN B CB  
7892 C CG  . GLN B 453 ? 0.2627 0.2995 0.3282 0.0652  -0.0734 0.0797  453 GLN B CG  
7893 C CD  . GLN B 453 ? 0.3601 0.3992 0.4076 0.0573  -0.0841 0.1084  453 GLN B CD  
7894 O OE1 . GLN B 453 ? 0.3701 0.4005 0.3949 0.0416  -0.0792 0.1153  453 GLN B OE1 
7895 N NE2 . GLN B 453 ? 0.3438 0.3977 0.3970 0.0661  -0.0951 0.1197  453 GLN B NE2 
7896 N N   . GLY B 454 ? 0.4009 0.3364 0.4901 0.0664  -0.0757 0.0945  454 GLY B N   
7897 C CA  . GLY B 454 ? 0.4958 0.3942 0.6154 0.0862  -0.0822 0.0961  454 GLY B CA  
7898 C C   . GLY B 454 ? 0.6871 0.5363 0.8136 0.0786  -0.0775 0.0814  454 GLY B C   
7899 O O   . GLY B 454 ? 0.7308 0.5533 0.8807 0.0963  -0.0760 0.0602  454 GLY B O   
7900 N N   . GLU B 455 ? 0.7614 0.6017 0.8696 0.0521  -0.0747 0.0893  455 GLU B N   
7901 C CA  . GLU B 455 ? 0.8497 0.6463 0.9649 0.0375  -0.0729 0.0776  455 GLU B CA  
7902 C C   . GLU B 455 ? 0.9727 0.7260 1.0931 0.0259  -0.0821 0.1137  455 GLU B C   
7903 O O   . GLU B 455 ? 1.0556 0.7974 1.1827 0.0434  -0.0900 0.1340  455 GLU B O   
7904 C CB  . GLU B 455 ? 0.7976 0.6231 0.8958 0.0155  -0.0640 0.0597  455 GLU B CB  
7905 N N   . GLU B 456 ? 0.9990 0.7375 1.1136 -0.0045 -0.0794 0.1222  456 GLU B N   
7906 C CA  . GLU B 456 ? 1.0318 0.7297 1.1478 -0.0200 -0.0842 0.1534  456 GLU B CA  
7907 C C   . GLU B 456 ? 1.0380 0.7682 1.1349 -0.0531 -0.0775 0.1793  456 GLU B C   
7908 O O   . GLU B 456 ? 1.0885 0.8086 1.1916 -0.0814 -0.0726 0.1765  456 GLU B O   
7909 C CB  . GLU B 456 ? 1.0618 0.7029 1.1950 -0.0259 -0.0846 0.1313  456 GLU B CB  
7910 N N   . LYS B 457 ? 0.9808 0.7568 1.0545 -0.0494 -0.0758 0.2002  457 LYS B N   
7911 C CA  . LYS B 457 ? 0.9318 0.7479 0.9810 -0.0745 -0.0661 0.2233  457 LYS B CA  
7912 C C   . LYS B 457 ? 0.9912 0.8198 1.0492 -0.1071 -0.0547 0.2174  457 LYS B C   
7913 O O   . LYS B 457 ? 1.0587 0.9037 1.1060 -0.1300 -0.0456 0.2367  457 LYS B O   
7914 C CB  . LYS B 457 ? 0.9408 0.7399 0.9744 -0.0773 -0.0697 0.2546  457 LYS B CB  
7915 N N   . ALA B 458 ? 0.9427 0.7765 1.0184 -0.1051 -0.0527 0.1806  458 ALA B N   
7916 C CA  . ALA B 458 ? 0.8606 0.7244 0.9481 -0.1317 -0.0433 0.1675  458 ALA B CA  
7917 C C   . ALA B 458 ? 0.7722 0.7040 0.8418 -0.1393 -0.0287 0.1778  458 ALA B C   
7918 O O   . ALA B 458 ? 0.7317 0.6881 0.7785 -0.1191 -0.0271 0.1782  458 ALA B O   
7919 C CB  . ALA B 458 ? 0.8079 0.6786 0.9084 -0.1208 -0.0460 0.1240  458 ALA B CB  
7920 N N   . PRO B 459 ? 0.7066 0.6721 0.7875 -0.1687 -0.0173 0.1846  459 PRO B N   
7921 C CA  . PRO B 459 ? 0.6758 0.7117 0.7432 -0.1718 -0.0001 0.1870  459 PRO B CA  
7922 C C   . PRO B 459 ? 0.6576 0.7261 0.7211 -0.1428 0.0005  0.1530  459 PRO B C   
7923 O O   . PRO B 459 ? 0.5875 0.6434 0.6669 -0.1315 -0.0086 0.1264  459 PRO B O   
7924 C CB  . PRO B 459 ? 0.6448 0.7143 0.7391 -0.2032 0.0111  0.1879  459 PRO B CB  
7925 C CG  . PRO B 459 ? 0.7184 0.7289 0.8335 -0.2190 -0.0011 0.1884  459 PRO B CG  
7926 C CD  . PRO B 459 ? 0.7501 0.6911 0.8570 -0.1993 -0.0187 0.1888  459 PRO B CD  
7927 N N   . PHE B 460 ? 0.6519 0.7583 0.6900 -0.1318 0.0104  0.1546  460 PHE B N   
7928 C CA  . PHE B 460 ? 0.4902 0.6260 0.5206 -0.1072 0.0130  0.1269  460 PHE B CA  
7929 C C   . PHE B 460 ? 0.4484 0.5489 0.4655 -0.0828 -0.0013 0.1169  460 PHE B C   
7930 O O   . PHE B 460 ? 0.4548 0.5720 0.4620 -0.0650 -0.0004 0.0979  460 PHE B O   
7931 C CB  . PHE B 460 ? 0.4465 0.6130 0.5076 -0.1051 0.0156  0.1010  460 PHE B CB  
7932 C CG  . PHE B 460 ? 0.3661 0.5762 0.4520 -0.1300 0.0291  0.1086  460 PHE B CG  
7933 C CD1 . PHE B 460 ? 0.3949 0.6370 0.4659 -0.1455 0.0468  0.1291  460 PHE B CD1 
7934 C CD2 . PHE B 460 ? 0.4354 0.6596 0.5590 -0.1406 0.0239  0.0960  460 PHE B CD2 
7935 C CE1 . PHE B 460 ? 0.4600 0.7456 0.5552 -0.1686 0.0613  0.1353  460 PHE B CE1 
7936 C CE2 . PHE B 460 ? 0.4408 0.7132 0.5939 -0.1663 0.0362  0.1036  460 PHE B CE2 
7937 C CZ  . PHE B 460 ? 0.4855 0.7859 0.6243 -0.1784 0.0559  0.1221  460 PHE B CZ  
7938 N N   . VAL B 461 ? 0.5143 0.5671 0.5337 -0.0811 -0.0139 0.1288  461 VAL B N   
7939 C CA  . VAL B 461 ? 0.4949 0.5266 0.5060 -0.0577 -0.0248 0.1201  461 VAL B CA  
7940 C C   . VAL B 461 ? 0.4978 0.5546 0.4798 -0.0498 -0.0232 0.1269  461 VAL B C   
7941 O O   . VAL B 461 ? 0.4919 0.5550 0.4671 -0.0337 -0.0270 0.1102  461 VAL B O   
7942 C CB  . VAL B 461 ? 0.6544 0.6350 0.6772 -0.0540 -0.0371 0.1328  461 VAL B CB  
7943 C CG1 . VAL B 461 ? 0.6923 0.6617 0.6990 -0.0571 -0.0426 0.1687  461 VAL B CG1 
7944 C CG2 . VAL B 461 ? 0.6558 0.6223 0.6857 -0.0304 -0.0446 0.1109  461 VAL B CG2 
7945 N N   . GLU B 462 ? 0.3676 0.4414 0.3295 -0.0642 -0.0171 0.1508  462 GLU B N   
7946 C CA  . GLU B 462 ? 0.3702 0.4701 0.2983 -0.0593 -0.0167 0.1543  462 GLU B CA  
7947 C C   . GLU B 462 ? 0.3839 0.5171 0.3051 -0.0520 -0.0056 0.1232  462 GLU B C   
7948 O O   . GLU B 462 ? 0.3854 0.5290 0.2843 -0.0430 -0.0093 0.1130  462 GLU B O   
7949 C CB  . GLU B 462 ? 0.4785 0.5912 0.3820 -0.0771 -0.0114 0.1834  462 GLU B CB  
7950 C CG  . GLU B 462 ? 0.7104 0.8498 0.6192 -0.0983 0.0082  0.1867  462 GLU B CG  
7951 C CD  . GLU B 462 ? 0.8443 0.9593 0.7878 -0.1141 0.0082  0.1983  462 GLU B CD  
7952 O OE1 . GLU B 462 ? 0.8717 1.0173 0.8345 -0.1269 0.0230  0.1873  462 GLU B OE1 
7953 O OE2 . GLU B 462 ? 0.9056 0.9703 0.8619 -0.1116 -0.0074 0.2125  462 GLU B OE2 
7954 N N   . VAL B 463 ? 0.2610 0.4094 0.2039 -0.0551 0.0058  0.1073  463 VAL B N   
7955 C CA  . VAL B 463 ? 0.2386 0.4123 0.1810 -0.0433 0.0143  0.0785  463 VAL B CA  
7956 C C   . VAL B 463 ? 0.2945 0.4436 0.2421 -0.0257 0.0019  0.0602  463 VAL B C   
7957 O O   . VAL B 463 ? 0.2284 0.3828 0.1611 -0.0158 0.0024  0.0433  463 VAL B O   
7958 C CB  . VAL B 463 ? 0.2710 0.4730 0.2424 -0.0485 0.0269  0.0692  463 VAL B CB  
7959 C CG1 . VAL B 463 ? 0.2948 0.5171 0.2706 -0.0304 0.0330  0.0404  463 VAL B CG1 
7960 C CG2 . VAL B 463 ? 0.3125 0.5480 0.2790 -0.0698 0.0431  0.0879  463 VAL B CG2 
7961 N N   . PHE B 464 ? 0.1989 0.3199 0.1662 -0.0233 -0.0085 0.0625  464 PHE B N   
7962 C CA  . PHE B 464 ? 0.2329 0.3358 0.2024 -0.0097 -0.0176 0.0482  464 PHE B CA  
7963 C C   . PHE B 464 ? 0.2491 0.3484 0.1993 -0.0054 -0.0247 0.0527  464 PHE B C   
7964 O O   . PHE B 464 ? 0.2592 0.3573 0.2033 0.0015  -0.0278 0.0387  464 PHE B O   
7965 C CB  . PHE B 464 ? 0.2681 0.3465 0.2579 -0.0089 -0.0247 0.0478  464 PHE B CB  
7966 C CG  . PHE B 464 ? 0.1867 0.2718 0.1949 -0.0132 -0.0226 0.0375  464 PHE B CG  
7967 C CD1 . PHE B 464 ? 0.2091 0.2986 0.2195 -0.0039 -0.0253 0.0211  464 PHE B CD1 
7968 C CD2 . PHE B 464 ? 0.2206 0.3095 0.2442 -0.0284 -0.0196 0.0464  464 PHE B CD2 
7969 C CE1 . PHE B 464 ? 0.1705 0.2722 0.1982 -0.0070 -0.0273 0.0133  464 PHE B CE1 
7970 C CE2 . PHE B 464 ? 0.1973 0.3001 0.2415 -0.0345 -0.0204 0.0360  464 PHE B CE2 
7971 C CZ  . PHE B 464 ? 0.2257 0.3371 0.2720 -0.0224 -0.0253 0.0192  464 PHE B CZ  
7972 N N   . ASP B 465 ? 0.2391 0.3374 0.1803 -0.0111 -0.0291 0.0742  465 ASP B N   
7973 C CA  . ASP B 465 ? 0.2193 0.3231 0.1438 -0.0080 -0.0394 0.0808  465 ASP B CA  
7974 C C   . ASP B 465 ? 0.2666 0.3939 0.1617 -0.0120 -0.0344 0.0682  465 ASP B C   
7975 O O   . ASP B 465 ? 0.2689 0.3962 0.1577 -0.0089 -0.0410 0.0555  465 ASP B O   
7976 C CB  . ASP B 465 ? 0.2494 0.3465 0.1712 -0.0118 -0.0480 0.1112  465 ASP B CB  
7977 C CG  . ASP B 465 ? 0.3108 0.4157 0.2205 -0.0084 -0.0586 0.1145  465 ASP B CG  
7978 O OD1 . ASP B 465 ? 0.3076 0.4077 0.2351 0.0024  -0.0683 0.1096  465 ASP B OD1 
7979 O OD2 . ASP B 465 ? 0.3078 0.4258 0.1925 -0.0170 -0.0560 0.1197  465 ASP B OD2 
7980 N N   . LYS B 466 ? 0.2528 0.3981 0.1342 -0.0196 -0.0208 0.0677  466 LYS B N   
7981 C CA  . LYS B 466 ? 0.3007 0.4640 0.1574 -0.0205 -0.0126 0.0476  466 LYS B CA  
7982 C C   . LYS B 466 ? 0.2783 0.4326 0.1419 -0.0100 -0.0117 0.0194  466 LYS B C   
7983 O O   . LYS B 466 ? 0.2956 0.4443 0.1441 -0.0092 -0.0150 0.0022  466 LYS B O   
7984 C CB  . LYS B 466 ? 0.2989 0.4886 0.1472 -0.0284 0.0059  0.0493  466 LYS B CB  
7985 C CG  . LYS B 466 ? 0.3587 0.5634 0.1874 -0.0257 0.0170  0.0230  466 LYS B CG  
7986 C CD  . LYS B 466 ? 0.4081 0.6443 0.2322 -0.0336 0.0365  0.0260  466 LYS B CD  
7987 C CE  . LYS B 466 ? 0.6450 0.8924 0.4378 -0.0354 0.0430  0.0103  466 LYS B CE  
7988 N NZ  . LYS B 466 ? 0.7465 1.0126 0.5455 -0.0250 0.0621  -0.0203 466 LYS B NZ  
7989 N N   . LEU B 467 ? 0.2146 0.3572 0.1075 -0.0027 -0.0084 0.0142  467 LEU B N   
7990 C CA  . LEU B 467 ? 0.2339 0.3605 0.1356 0.0079  -0.0096 -0.0071 467 LEU B CA  
7991 C C   . LEU B 467 ? 0.2513 0.3578 0.1499 0.0070  -0.0230 -0.0080 467 LEU B C   
7992 O O   . LEU B 467 ? 0.2885 0.3848 0.1747 0.0072  -0.0256 -0.0240 467 LEU B O   
7993 C CB  . LEU B 467 ? 0.2013 0.3240 0.1324 0.0146  -0.0073 -0.0073 467 LEU B CB  
7994 C CG  . LEU B 467 ? 0.2043 0.3557 0.1472 0.0160  0.0065  -0.0113 467 LEU B CG  
7995 C CD1 . LEU B 467 ? 0.1791 0.3328 0.1532 0.0165  0.0038  -0.0057 467 LEU B CD1 
7996 C CD2 . LEU B 467 ? 0.2621 0.4196 0.2011 0.0293  0.0147  -0.0353 467 LEU B CD2 
7997 N N   . PHE B 468 ? 0.2495 0.3504 0.1617 0.0054  -0.0308 0.0077  468 PHE B N   
7998 C CA  . PHE B 468 ? 0.2443 0.3371 0.1605 0.0042  -0.0408 0.0073  468 PHE B CA  
7999 C C   . PHE B 468 ? 0.2616 0.3647 0.1575 -0.0036 -0.0479 0.0028  468 PHE B C   
8000 O O   . PHE B 468 ? 0.2568 0.3513 0.1485 -0.0081 -0.0520 -0.0103 468 PHE B O   
8001 C CB  . PHE B 468 ? 0.2288 0.3218 0.1643 0.0069  -0.0460 0.0230  468 PHE B CB  
8002 C CG  . PHE B 468 ? 0.2348 0.3338 0.1800 0.0064  -0.0543 0.0236  468 PHE B CG  
8003 C CD1 . PHE B 468 ? 0.2643 0.3559 0.2174 0.0056  -0.0522 0.0140  468 PHE B CD1 
8004 C CD2 . PHE B 468 ? 0.2245 0.3380 0.1731 0.0058  -0.0635 0.0350  468 PHE B CD2 
8005 C CE1 . PHE B 468 ? 0.2490 0.3549 0.2150 0.0023  -0.0570 0.0149  468 PHE B CE1 
8006 C CE2 . PHE B 468 ? 0.2183 0.3451 0.1840 0.0057  -0.0699 0.0342  468 PHE B CE2 
8007 C CZ  . PHE B 468 ? 0.2065 0.3359 0.1819 0.0030  -0.0667 0.0244  468 PHE B CZ  
8008 N N   . ARG B 469 ? 0.2472 0.3617 0.1327 -0.0073 -0.0487 0.0138  469 ARG B N   
8009 C CA  . ARG B 469 ? 0.2560 0.3763 0.1264 -0.0146 -0.0561 0.0099  469 ARG B CA  
8010 C C   . ARG B 469 ? 0.2947 0.4096 0.1408 -0.0188 -0.0507 -0.0141 469 ARG B C   
8011 O O   . ARG B 469 ? 0.3398 0.4513 0.1763 -0.0261 -0.0588 -0.0255 469 ARG B O   
8012 C CB  . ARG B 469 ? 0.3426 0.4761 0.2049 -0.0165 -0.0598 0.0298  469 ARG B CB  
8013 C CG  . ARG B 469 ? 0.2759 0.4082 0.1643 -0.0097 -0.0682 0.0510  469 ARG B CG  
8014 C CD  . ARG B 469 ? 0.3293 0.4679 0.2079 -0.0110 -0.0732 0.0736  469 ARG B CD  
8015 N NE  . ARG B 469 ? 0.2986 0.4309 0.2030 -0.0013 -0.0831 0.0929  469 ARG B NE  
8016 C CZ  . ARG B 469 ? 0.3388 0.4808 0.2562 0.0043  -0.0969 0.0980  469 ARG B CZ  
8017 N NH1 . ARG B 469 ? 0.3326 0.4918 0.2388 -0.0026 -0.1035 0.0866  469 ARG B NH1 
8018 N NH2 . ARG B 469 ? 0.3349 0.4700 0.2786 0.0172  -0.1049 0.1137  469 ARG B NH2 
8019 N N   . SER B 470 ? 0.3207 0.4361 0.1595 -0.0134 -0.0371 -0.0241 470 SER B N   
8020 C CA  . SER B 470 ? 0.3512 0.4578 0.1716 -0.0121 -0.0299 -0.0517 470 SER B CA  
8021 C C   . SER B 470 ? 0.2946 0.3735 0.1225 -0.0103 -0.0357 -0.0690 470 SER B C   
8022 O O   . SER B 470 ? 0.3835 0.4438 0.1964 -0.0155 -0.0387 -0.0897 470 SER B O   
8023 C CB  . SER B 470 ? 0.3700 0.4913 0.1902 -0.0027 -0.0118 -0.0590 470 SER B CB  
8024 O OG  . SER B 470 ? 0.3874 0.5340 0.1960 -0.0094 -0.0055 -0.0431 470 SER B OG  
8025 N N   . PHE B 471 ? 0.2873 0.3568 0.1396 -0.0040 -0.0373 -0.0591 471 PHE B N   
8026 C CA  . PHE B 471 ? 0.3534 0.3898 0.2162 -0.0050 -0.0426 -0.0665 471 PHE B CA  
8027 C C   . PHE B 471 ? 0.3912 0.4286 0.2498 -0.0228 -0.0557 -0.0653 471 PHE B C   
8028 O O   . PHE B 471 ? 0.3826 0.3935 0.2352 -0.0320 -0.0606 -0.0801 471 PHE B O   
8029 C CB  . PHE B 471 ? 0.2989 0.3275 0.1865 0.0034  -0.0410 -0.0509 471 PHE B CB  
8030 C CG  . PHE B 471 ? 0.3025 0.3323 0.2000 0.0192  -0.0317 -0.0538 471 PHE B CG  
8031 C CD1 . PHE B 471 ? 0.2895 0.3052 0.1833 0.0301  -0.0263 -0.0734 471 PHE B CD1 
8032 C CD2 . PHE B 471 ? 0.2863 0.3328 0.2006 0.0235  -0.0289 -0.0389 471 PHE B CD2 
8033 C CE1 . PHE B 471 ? 0.3772 0.4039 0.2884 0.0467  -0.0181 -0.0763 471 PHE B CE1 
8034 C CE2 . PHE B 471 ? 0.3117 0.3673 0.2403 0.0352  -0.0222 -0.0417 471 PHE B CE2 
8035 C CZ  . PHE B 471 ? 0.3870 0.4373 0.3163 0.0476  -0.0167 -0.0593 471 PHE B CZ  
8036 N N   . VAL B 472 ? 0.3213 0.3893 0.1862 -0.0280 -0.0621 -0.0477 472 VAL B N   
8037 C CA  . VAL B 472 ? 0.3259 0.4036 0.1992 -0.0411 -0.0735 -0.0436 472 VAL B CA  
8038 C C   . VAL B 472 ? 0.3660 0.4391 0.2171 -0.0504 -0.0789 -0.0606 472 VAL B C   
8039 O O   . VAL B 472 ? 0.4441 0.5095 0.2972 -0.0650 -0.0876 -0.0711 472 VAL B O   
8040 C CB  . VAL B 472 ? 0.2932 0.3988 0.1863 -0.0355 -0.0767 -0.0209 472 VAL B CB  
8041 C CG1 . VAL B 472 ? 0.3231 0.4494 0.2238 -0.0456 -0.0889 -0.0187 472 VAL B CG1 
8042 C CG2 . VAL B 472 ? 0.2594 0.3675 0.1772 -0.0287 -0.0729 -0.0096 472 VAL B CG2 
8043 N N   . ARG B 473 ? 0.3724 0.4512 0.2016 -0.0442 -0.0733 -0.0639 473 ARG B N   
8044 C CA  . ARG B 473 ? 0.3932 0.4683 0.1958 -0.0522 -0.0775 -0.0824 473 ARG B CA  
8045 C C   . ARG B 473 ? 0.4041 0.4408 0.1948 -0.0543 -0.0744 -0.1119 473 ARG B C   
8046 O O   . ARG B 473 ? 0.4415 0.4637 0.2244 -0.0668 -0.0845 -0.1286 473 ARG B O   
8047 C CB  . ARG B 473 ? 0.3894 0.4822 0.1690 -0.0463 -0.0689 -0.0783 473 ARG B CB  
8048 C CG  . ARG B 473 ? 0.5312 0.6234 0.2774 -0.0538 -0.0717 -0.0987 473 ARG B CG  
8049 C CD  . ARG B 473 ? 0.7292 0.8442 0.4515 -0.0500 -0.0609 -0.0918 473 ARG B CD  
8050 N NE  . ARG B 473 ? 0.8446 0.9810 0.5840 -0.0460 -0.0603 -0.0592 473 ARG B NE  
8051 C CZ  . ARG B 473 ? 0.9215 1.0637 0.6681 -0.0382 -0.0452 -0.0493 473 ARG B CZ  
8052 N NH1 . ARG B 473 ? 0.9399 1.0754 0.6814 -0.0314 -0.0284 -0.0694 473 ARG B NH1 
8053 N NH2 . ARG B 473 ? 0.8862 1.0410 0.6477 -0.0367 -0.0474 -0.0202 473 ARG B NH2 
8054 N N   . ARG B 474 ? 0.3998 0.4181 0.1925 -0.0414 -0.0613 -0.1193 474 ARG B N   
8055 C CA  . ARG B 474 ? 0.5203 0.4940 0.3065 -0.0385 -0.0575 -0.1472 474 ARG B CA  
8056 C C   . ARG B 474 ? 0.5072 0.4506 0.3074 -0.0540 -0.0708 -0.1498 474 ARG B C   
8057 O O   . ARG B 474 ? 0.4882 0.3902 0.2818 -0.0596 -0.0753 -0.1723 474 ARG B O   
8058 C CB  . ARG B 474 ? 0.5215 0.4904 0.3214 -0.0155 -0.0425 -0.1510 474 ARG B CB  
8059 C CG  . ARG B 474 ? 0.5783 0.5010 0.3798 -0.0021 -0.0363 -0.1783 474 ARG B CG  
8060 C CD  . ARG B 474 ? 0.6156 0.5361 0.3908 -0.0022 -0.0264 -0.2015 474 ARG B CD  
8061 N NE  . ARG B 474 ? 0.7104 0.5809 0.4911 0.0105  -0.0206 -0.2272 474 ARG B NE  
8062 C CZ  . ARG B 474 ? 0.9399 0.7591 0.7149 -0.0036 -0.0303 -0.2403 474 ARG B CZ  
8063 N NH1 . ARG B 474 ? 0.9940 0.8119 0.7580 -0.0325 -0.0466 -0.2313 474 ARG B NH1 
8064 N NH2 . ARG B 474 ? 1.0348 0.8051 0.8185 0.0106  -0.0239 -0.2607 474 ARG B NH2 
8065 N N   . ALA B 475 ? 0.4402 0.4026 0.2613 -0.0626 -0.0759 -0.1253 475 ALA B N   
8066 C CA  . ALA B 475 ? 0.4757 0.4127 0.3135 -0.0799 -0.0835 -0.1176 475 ALA B CA  
8067 C C   . ALA B 475 ? 0.5084 0.4496 0.3471 -0.1023 -0.0951 -0.1287 475 ALA B C   
8068 O O   . ALA B 475 ? 0.4957 0.4063 0.3444 -0.1210 -0.1000 -0.1292 475 ALA B O   
8069 C CB  . ALA B 475 ? 0.3550 0.3234 0.2189 -0.0792 -0.0822 -0.0867 475 ALA B CB  
8070 N N   . GLN B 476 ? 0.4603 0.4359 0.2894 -0.1007 -0.1003 -0.1331 476 GLN B N   
8071 C CA  . GLN B 476 ? 0.4782 0.4646 0.3098 -0.1204 -0.1137 -0.1409 476 GLN B CA  
8072 C C   . GLN B 476 ? 0.5609 0.5167 0.3649 -0.1208 -0.1175 -0.1732 476 GLN B C   
8073 O O   . GLN B 476 ? 0.6440 0.6126 0.4418 -0.1354 -0.1302 -0.1826 476 GLN B O   
8074 C CB  . GLN B 476 ? 0.5101 0.5527 0.3489 -0.1198 -0.1207 -0.1212 476 GLN B CB  
8075 C CG  . GLN B 476 ? 0.4538 0.5271 0.3245 -0.1171 -0.1180 -0.0928 476 GLN B CG  
8076 C CD  . GLN B 476 ? 0.5047 0.6241 0.3833 -0.1081 -0.1234 -0.0739 476 GLN B CD  
8077 O OE1 . GLN B 476 ? 0.5125 0.6597 0.4009 -0.1190 -0.1361 -0.0721 476 GLN B OE1 
8078 N NE2 . GLN B 476 ? 0.4460 0.5717 0.3220 -0.0887 -0.1149 -0.0592 476 GLN B NE2 
8079 N N   . GLU B 477 ? 0.6235 0.5395 0.4111 -0.1040 -0.1071 -0.1915 477 GLU B N   
8080 C CA  . GLU B 477 ? 0.7327 0.6126 0.4915 -0.0998 -0.1088 -0.2241 477 GLU B CA  
8081 C C   . GLU B 477 ? 0.8000 0.6189 0.5754 -0.0984 -0.1076 -0.2450 477 GLU B C   
8082 O O   . GLU B 477 ? 0.8053 0.6120 0.6050 -0.0910 -0.0939 -0.2357 477 GLU B O   
8083 C CB  . GLU B 477 ? 0.7633 0.6507 0.4880 -0.0791 -0.0927 -0.2280 477 GLU B CB  
8084 C CG  . GLU B 477 ? 0.7891 0.7383 0.5078 -0.0792 -0.0917 -0.2051 477 GLU B CG  
8085 C CD  . GLU B 477 ? 0.8587 0.8231 0.5537 -0.0626 -0.0722 -0.2077 477 GLU B CD  
8086 O OE1 . GLU B 477 ? 0.8750 0.8801 0.5548 -0.0652 -0.0728 -0.1956 477 GLU B OE1 
8087 O OE2 . GLU B 477 ? 0.8521 0.7904 0.5475 -0.0475 -0.0554 -0.2212 477 GLU B OE2 
# 
