data_9K7D
# 
_entry.id   9K7D 
# 
_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   9K7D         pdb_00009k7d 10.2210/pdb9k7d/pdb 
WWPDB D_1300052892 ?            ?                   
# 
_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                        9K7D 
_pdbx_database_status.recvd_initial_deposition_date   2024-10-23 
_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                 2 
_pdbx_contact_author.email              zhuzhimin@sinap.ac.cn 
_pdbx_contact_author.name_first         Zhimin 
_pdbx_contact_author.name_last          Zhu 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0009-0004-3840-9685 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Zhu, Z.M.'   1 ? 
'Wang, W.W.'  2 ? 
'Li, M.J.'    3 ? 
'Xu, Q.'      4 ? 
'Zhou, H.'    5 ? 
'Huang, L.Q.' 6 ? 
'Wang, Q.S.'  7 ? 
'Yu, F.'      8 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Commun Biol' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2399-3642 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            8 
_citation.language                  ? 
_citation.page_first                806 
_citation.page_last                 806 
_citation.title                     
'The crystal structure of GH57 family amylopullulanase reveals its dual binding pockets sharing the same catalytic dyad.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1038/s42003-025-08192-8 
_citation.pdbx_database_id_PubMed   40419759 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Zhu, Z.'   1 0009-0004-3840-9685 
primary 'Wang, W.'  2 0009-0007-7332-8217 
primary 'Li, M.'    3 ?                   
primary 'Xu, Q.'    4 ?                   
primary 'Zhou, H.'  5 ?                   
primary 'Huang, L.' 6 ?                   
primary 'Wang, Q.'  7 0000-0002-0614-6903 
primary 'Yu, F.'    8 0000-0002-9502-3277 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer  man 'Glycoside hydrolase family 57 N-terminal domain-containing protein' 57252.250 2   ? E256Q ? ? 
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
;
828.719   2   ? ?     ? ? 
3 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   ? ?     ? ? 
4 water    nat water 18.015    587 ? ?     ? ? 
# 
_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
YFEIFGEHPVYMWPPQASVSNEALELYYEKGINMLATDEVILKNSVERASPYLRYYFRELISVFFRDKTLSDLIGFSYHA
WNAEDAVRDFIGRLKKIHESVDFQPVVFVVLDGENCWEYYEENGIPFLEKLYSTLEKEEWIETLTLEEAMRKEDVKTEVI
ESVKAGTWFDGNFLKWIGNKEKNEYWKILIEAKKKAKNDYILVAEGSDWFWWQGEEKAPFVEVFDKLFRSFVRRAQE
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MKKLFLVFWWHMHQPLYREPYTGEYLLPWTFFHAVKDYYDMPAYLKDFEIKLNFNLTPVLIDQIQEYAQGKAKDVFLEAI
RKDPDDLEKEEVEKLIEFTKLNYEKPIYRFERIRELMNKEKLNREELLDLQTLNLLAWCGRTLRKDLKDLLNKGRNYTQE
EKEYVLNKYFEIIKKTLSIYREIKEEGKGSVSTSPYYHPLIPILLNPNCVYETTPNVKIPDFAVSFREDASKHVELAKEK
YFEIFGEHPVYMWPPQASVSNEALELYYEKGINMLATDEVILKNSVERASPYLRYYFRELISVFFRDKTLSDLIGFSYHA
WNAEDAVRDFIGRLKKIHESVDFQPVVFVVLDGENCWEYYEENGIPFLEKLYSTLEKEEWIETLTLEEAMRKEDVKTEVI
ESVKAGTWFDGNFLKWIGNKEKNEYWKILIEAKKKAKNDYILVAEGSDWFWWQGEEKAPFVEVFDKLFRSFVRRAQE
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
_pdbx_entity_nonpoly.entity_id   4 
_pdbx_entity_nonpoly.name        water 
_pdbx_entity_nonpoly.comp_id     HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   LYS n 
1 3   LYS n 
1 4   LEU n 
1 5   PHE n 
1 6   LEU n 
1 7   VAL n 
1 8   PHE n 
1 9   TRP n 
1 10  TRP n 
1 11  HIS n 
1 12  MET n 
1 13  HIS n 
1 14  GLN n 
1 15  PRO n 
1 16  LEU n 
1 17  TYR n 
1 18  ARG n 
1 19  GLU n 
1 20  PRO n 
1 21  TYR n 
1 22  THR n 
1 23  GLY n 
1 24  GLU n 
1 25  TYR n 
1 26  LEU n 
1 27  LEU n 
1 28  PRO n 
1 29  TRP n 
1 30  THR n 
1 31  PHE n 
1 32  PHE n 
1 33  HIS n 
1 34  ALA n 
1 35  VAL n 
1 36  LYS n 
1 37  ASP n 
1 38  TYR n 
1 39  TYR n 
1 40  ASP n 
1 41  MET n 
1 42  PRO n 
1 43  ALA n 
1 44  TYR n 
1 45  LEU n 
1 46  LYS n 
1 47  ASP n 
1 48  PHE n 
1 49  GLU n 
1 50  ILE n 
1 51  LYS n 
1 52  LEU n 
1 53  ASN n 
1 54  PHE n 
1 55  ASN n 
1 56  LEU n 
1 57  THR n 
1 58  PRO n 
1 59  VAL n 
1 60  LEU n 
1 61  ILE n 
1 62  ASP n 
1 63  GLN n 
1 64  ILE n 
1 65  GLN n 
1 66  GLU n 
1 67  TYR n 
1 68  ALA n 
1 69  GLN n 
1 70  GLY n 
1 71  LYS n 
1 72  ALA n 
1 73  LYS n 
1 74  ASP n 
1 75  VAL n 
1 76  PHE n 
1 77  LEU n 
1 78  GLU n 
1 79  ALA n 
1 80  ILE n 
1 81  ARG n 
1 82  LYS n 
1 83  ASP n 
1 84  PRO n 
1 85  ASP n 
1 86  ASP n 
1 87  LEU n 
1 88  GLU n 
1 89  LYS n 
1 90  GLU n 
1 91  GLU n 
1 92  VAL n 
1 93  GLU n 
1 94  LYS n 
1 95  LEU n 
1 96  ILE n 
1 97  GLU n 
1 98  PHE n 
1 99  THR n 
1 100 LYS n 
1 101 LEU n 
1 102 ASN n 
1 103 TYR n 
1 104 GLU n 
1 105 LYS n 
1 106 PRO n 
1 107 ILE n 
1 108 TYR n 
1 109 ARG n 
1 110 PHE n 
1 111 GLU n 
1 112 ARG n 
1 113 ILE n 
1 114 ARG n 
1 115 GLU n 
1 116 LEU n 
1 117 MET n 
1 118 ASN n 
1 119 LYS n 
1 120 GLU n 
1 121 LYS n 
1 122 LEU n 
1 123 ASN n 
1 124 ARG n 
1 125 GLU n 
1 126 GLU n 
1 127 LEU n 
1 128 LEU n 
1 129 ASP n 
1 130 LEU n 
1 131 GLN n 
1 132 THR n 
1 133 LEU n 
1 134 ASN n 
1 135 LEU n 
1 136 LEU n 
1 137 ALA n 
1 138 TRP n 
1 139 CYS n 
1 140 GLY n 
1 141 ARG n 
1 142 THR n 
1 143 LEU n 
1 144 ARG n 
1 145 LYS n 
1 146 ASP n 
1 147 LEU n 
1 148 LYS n 
1 149 ASP n 
1 150 LEU n 
1 151 LEU n 
1 152 ASN n 
1 153 LYS n 
1 154 GLY n 
1 155 ARG n 
1 156 ASN n 
1 157 TYR n 
1 158 THR n 
1 159 GLN n 
1 160 GLU n 
1 161 GLU n 
1 162 LYS n 
1 163 GLU n 
1 164 TYR n 
1 165 VAL n 
1 166 LEU n 
1 167 ASN n 
1 168 LYS n 
1 169 TYR n 
1 170 PHE n 
1 171 GLU n 
1 172 ILE n 
1 173 ILE n 
1 174 LYS n 
1 175 LYS n 
1 176 THR n 
1 177 LEU n 
1 178 SER n 
1 179 ILE n 
1 180 TYR n 
1 181 ARG n 
1 182 GLU n 
1 183 ILE n 
1 184 LYS n 
1 185 GLU n 
1 186 GLU n 
1 187 GLY n 
1 188 LYS n 
1 189 GLY n 
1 190 SER n 
1 191 VAL n 
1 192 SER n 
1 193 THR n 
1 194 SER n 
1 195 PRO n 
1 196 TYR n 
1 197 TYR n 
1 198 HIS n 
1 199 PRO n 
1 200 LEU n 
1 201 ILE n 
1 202 PRO n 
1 203 ILE n 
1 204 LEU n 
1 205 LEU n 
1 206 ASN n 
1 207 PRO n 
1 208 ASN n 
1 209 CYS n 
1 210 VAL n 
1 211 TYR n 
1 212 GLU n 
1 213 THR n 
1 214 THR n 
1 215 PRO n 
1 216 ASN n 
1 217 VAL n 
1 218 LYS n 
1 219 ILE n 
1 220 PRO n 
1 221 ASP n 
1 222 PHE n 
1 223 ALA n 
1 224 VAL n 
1 225 SER n 
1 226 PHE n 
1 227 ARG n 
1 228 GLU n 
1 229 ASP n 
1 230 ALA n 
1 231 SER n 
1 232 LYS n 
1 233 HIS n 
1 234 VAL n 
1 235 GLU n 
1 236 LEU n 
1 237 ALA n 
1 238 LYS n 
1 239 GLU n 
1 240 LYS n 
1 241 TYR n 
1 242 PHE n 
1 243 GLU n 
1 244 ILE n 
1 245 PHE n 
1 246 GLY n 
1 247 GLU n 
1 248 HIS n 
1 249 PRO n 
1 250 VAL n 
1 251 TYR n 
1 252 MET n 
1 253 TRP n 
1 254 PRO n 
1 255 PRO n 
1 256 GLN n 
1 257 ALA n 
1 258 SER n 
1 259 VAL n 
1 260 SER n 
1 261 ASN n 
1 262 GLU n 
1 263 ALA n 
1 264 LEU n 
1 265 GLU n 
1 266 LEU n 
1 267 TYR n 
1 268 TYR n 
1 269 GLU n 
1 270 LYS n 
1 271 GLY n 
1 272 ILE n 
1 273 ASN n 
1 274 MET n 
1 275 LEU n 
1 276 ALA n 
1 277 THR n 
1 278 ASP n 
1 279 GLU n 
1 280 VAL n 
1 281 ILE n 
1 282 LEU n 
1 283 LYS n 
1 284 ASN n 
1 285 SER n 
1 286 VAL n 
1 287 GLU n 
1 288 ARG n 
1 289 ALA n 
1 290 SER n 
1 291 PRO n 
1 292 TYR n 
1 293 LEU n 
1 294 ARG n 
1 295 TYR n 
1 296 TYR n 
1 297 PHE n 
1 298 ARG n 
1 299 GLU n 
1 300 LEU n 
1 301 ILE n 
1 302 SER n 
1 303 VAL n 
1 304 PHE n 
1 305 PHE n 
1 306 ARG n 
1 307 ASP n 
1 308 LYS n 
1 309 THR n 
1 310 LEU n 
1 311 SER n 
1 312 ASP n 
1 313 LEU n 
1 314 ILE n 
1 315 GLY n 
1 316 PHE n 
1 317 SER n 
1 318 TYR n 
1 319 HIS n 
1 320 ALA n 
1 321 TRP n 
1 322 ASN n 
1 323 ALA n 
1 324 GLU n 
1 325 ASP n 
1 326 ALA n 
1 327 VAL n 
1 328 ARG n 
1 329 ASP n 
1 330 PHE n 
1 331 ILE n 
1 332 GLY n 
1 333 ARG n 
1 334 LEU n 
1 335 LYS n 
1 336 LYS n 
1 337 ILE n 
1 338 HIS n 
1 339 GLU n 
1 340 SER n 
1 341 VAL n 
1 342 ASP n 
1 343 PHE n 
1 344 GLN n 
1 345 PRO n 
1 346 VAL n 
1 347 VAL n 
1 348 PHE n 
1 349 VAL n 
1 350 VAL n 
1 351 LEU n 
1 352 ASP n 
1 353 GLY n 
1 354 GLU n 
1 355 ASN n 
1 356 CYS n 
1 357 TRP n 
1 358 GLU n 
1 359 TYR n 
1 360 TYR n 
1 361 GLU n 
1 362 GLU n 
1 363 ASN n 
1 364 GLY n 
1 365 ILE n 
1 366 PRO n 
1 367 PHE n 
1 368 LEU n 
1 369 GLU n 
1 370 LYS n 
1 371 LEU n 
1 372 TYR n 
1 373 SER n 
1 374 THR n 
1 375 LEU n 
1 376 GLU n 
1 377 LYS n 
1 378 GLU n 
1 379 GLU n 
1 380 TRP n 
1 381 ILE n 
1 382 GLU n 
1 383 THR n 
1 384 LEU n 
1 385 THR n 
1 386 LEU n 
1 387 GLU n 
1 388 GLU n 
1 389 ALA n 
1 390 MET n 
1 391 ARG n 
1 392 LYS n 
1 393 GLU n 
1 394 ASP n 
1 395 VAL n 
1 396 LYS n 
1 397 THR n 
1 398 GLU n 
1 399 VAL n 
1 400 ILE n 
1 401 GLU n 
1 402 SER n 
1 403 VAL n 
1 404 LYS n 
1 405 ALA n 
1 406 GLY n 
1 407 THR n 
1 408 TRP n 
1 409 PHE n 
1 410 ASP n 
1 411 GLY n 
1 412 ASN n 
1 413 PHE n 
1 414 LEU n 
1 415 LYS n 
1 416 TRP n 
1 417 ILE n 
1 418 GLY n 
1 419 ASN n 
1 420 LYS n 
1 421 GLU n 
1 422 LYS n 
1 423 ASN n 
1 424 GLU n 
1 425 TYR n 
1 426 TRP n 
1 427 LYS n 
1 428 ILE n 
1 429 LEU n 
1 430 ILE n 
1 431 GLU n 
1 432 ALA n 
1 433 LYS n 
1 434 LYS n 
1 435 LYS n 
1 436 ALA n 
1 437 LYS n 
1 438 ASN n 
1 439 ASP n 
1 440 TYR n 
1 441 ILE n 
1 442 LEU n 
1 443 VAL n 
1 444 ALA n 
1 445 GLU n 
1 446 GLY n 
1 447 SER n 
1 448 ASP n 
1 449 TRP n 
1 450 PHE n 
1 451 TRP n 
1 452 TRP n 
1 453 GLN n 
1 454 GLY n 
1 455 GLU n 
1 456 GLU n 
1 457 LYS n 
1 458 ALA n 
1 459 PRO n 
1 460 PHE n 
1 461 VAL n 
1 462 GLU n 
1 463 VAL n 
1 464 PHE n 
1 465 ASP n 
1 466 LYS n 
1 467 LEU n 
1 468 PHE n 
1 469 ARG n 
1 470 SER n 
1 471 PHE n 
1 472 VAL n 
1 473 ARG n 
1 474 ARG n 
1 475 ALA n 
1 476 GLN n 
1 477 GLU n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   477 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 aq_720 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Aquifex aeolicus VF5' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     224324 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_pdbx_entity_branch.entity_id 
_pdbx_entity_branch.type 
2 oligosaccharide 
3 oligosaccharide 
# 
loop_
_pdbx_entity_branch_descriptor.ordinal 
_pdbx_entity_branch_descriptor.entity_id 
_pdbx_entity_branch_descriptor.descriptor 
_pdbx_entity_branch_descriptor.type 
_pdbx_entity_branch_descriptor.program 
_pdbx_entity_branch_descriptor.program_version 
1 2 DGlcpa1-4DGlcpa1-4DGlcpa1-4DGlcpa1-4DGlcpa1-ROH                                                                 
'Glycam Condensed Sequence' GMML       1.0   
2 2 'WURCS=2.0/1,5,4/[a2122h-1a_1-5]/1-1-1-1-1/a4-b1_b4-c1_c4-d1_d4-e1'                                             WURCS 
PDB2Glycan 1.1.0 
3 2 '[][a-D-Glcp]{[(4+1)][a-D-Glcp]{[(4+1)][a-D-Glcp]{[(4+1)][a-D-Glcp]{[(4+1)][a-D-Glcp]{}}}}}'                    LINUCS 
PDB-CARE   ?     
4 3 DGlcpa1-4DGlcpa1-4DGlcpa1-4DGlcpa1-4DGlcpa1-4DGlcpa1-ROH                                                        
'Glycam Condensed Sequence' GMML       1.0   
5 3 '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 
6 3 '[][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 3 2 GLC C1 O1 1 GLC O4 HO4 sing ? 
6 3 3 GLC C1 O1 2 GLC O4 HO4 sing ? 
7 3 4 GLC C1 O1 3 GLC O4 HO4 sing ? 
8 3 5 GLC C1 O1 4 GLC O4 HO4 sing ? 
9 3 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  
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 GLN 256 256 256 GLN GLN A . n 
A 1 257 ALA 257 257 257 ALA ALA A . n 
A 1 258 SER 258 258 258 SER SER A . n 
A 1 259 VAL 259 259 259 VAL VAL A . n 
A 1 260 SER 260 260 260 SER SER A . n 
A 1 261 ASN 261 261 261 ASN ASN A . n 
A 1 262 GLU 262 262 262 GLU GLU A . n 
A 1 263 ALA 263 263 263 ALA ALA A . n 
A 1 264 LEU 264 264 264 LEU LEU A . n 
A 1 265 GLU 265 265 265 GLU GLU A . n 
A 1 266 LEU 266 266 266 LEU LEU A . n 
A 1 267 TYR 267 267 267 TYR TYR A . n 
A 1 268 TYR 268 268 268 TYR TYR A . n 
A 1 269 GLU 269 269 269 GLU GLU A . n 
A 1 270 LYS 270 270 270 LYS LYS A . n 
A 1 271 GLY 271 271 271 GLY GLY A . n 
A 1 272 ILE 272 272 272 ILE ILE A . n 
A 1 273 ASN 273 273 273 ASN ASN A . n 
A 1 274 MET 274 274 274 MET MET A . n 
A 1 275 LEU 275 275 275 LEU LEU A . n 
A 1 276 ALA 276 276 276 ALA ALA A . n 
A 1 277 THR 277 277 277 THR THR A . n 
A 1 278 ASP 278 278 278 ASP ASP A . n 
A 1 279 GLU 279 279 279 GLU GLU A . n 
A 1 280 VAL 280 280 280 VAL VAL A . n 
A 1 281 ILE 281 281 281 ILE ILE A . n 
A 1 282 LEU 282 282 282 LEU LEU A . n 
A 1 283 LYS 283 283 283 LYS LYS A . n 
A 1 284 ASN 284 284 284 ASN ASN A . n 
A 1 285 SER 285 285 285 SER SER A . n 
A 1 286 VAL 286 286 286 VAL VAL A . n 
A 1 287 GLU 287 287 287 GLU GLU A . n 
A 1 288 ARG 288 288 288 ARG ARG A . n 
A 1 289 ALA 289 289 289 ALA ALA A . n 
A 1 290 SER 290 290 290 SER SER A . n 
A 1 291 PRO 291 291 291 PRO PRO A . n 
A 1 292 TYR 292 292 292 TYR TYR A . n 
A 1 293 LEU 293 293 293 LEU LEU A . n 
A 1 294 ARG 294 294 294 ARG ARG A . n 
A 1 295 TYR 295 295 295 TYR TYR A . n 
A 1 296 TYR 296 296 296 TYR TYR A . n 
A 1 297 PHE 297 297 297 PHE PHE A . n 
A 1 298 ARG 298 298 298 ARG ARG A . n 
A 1 299 GLU 299 299 299 GLU GLU A . n 
A 1 300 LEU 300 300 300 LEU LEU A . n 
A 1 301 ILE 301 301 301 ILE ILE A . n 
A 1 302 SER 302 302 302 SER SER A . n 
A 1 303 VAL 303 303 303 VAL VAL A . n 
A 1 304 PHE 304 304 304 PHE PHE A . n 
A 1 305 PHE 305 305 305 PHE PHE A . n 
A 1 306 ARG 306 306 306 ARG ARG A . n 
A 1 307 ASP 307 307 307 ASP ASP A . n 
A 1 308 LYS 308 308 308 LYS LYS A . n 
A 1 309 THR 309 309 309 THR THR A . n 
A 1 310 LEU 310 310 310 LEU LEU A . n 
A 1 311 SER 311 311 311 SER SER A . n 
A 1 312 ASP 312 312 312 ASP ASP A . n 
A 1 313 LEU 313 313 313 LEU LEU A . n 
A 1 314 ILE 314 314 314 ILE ILE A . n 
A 1 315 GLY 315 315 315 GLY GLY A . n 
A 1 316 PHE 316 316 316 PHE PHE A . n 
A 1 317 SER 317 317 317 SER SER A . n 
A 1 318 TYR 318 318 318 TYR TYR A . n 
A 1 319 HIS 319 319 319 HIS HIS A . n 
A 1 320 ALA 320 320 320 ALA ALA A . n 
A 1 321 TRP 321 321 321 TRP TRP A . n 
A 1 322 ASN 322 322 322 ASN ASN A . n 
A 1 323 ALA 323 323 323 ALA ALA A . n 
A 1 324 GLU 324 324 324 GLU GLU A . n 
A 1 325 ASP 325 325 325 ASP ASP A . n 
A 1 326 ALA 326 326 326 ALA ALA A . n 
A 1 327 VAL 327 327 327 VAL VAL A . n 
A 1 328 ARG 328 328 328 ARG ARG A . n 
A 1 329 ASP 329 329 329 ASP ASP A . n 
A 1 330 PHE 330 330 330 PHE PHE A . n 
A 1 331 ILE 331 331 331 ILE ILE A . n 
A 1 332 GLY 332 332 332 GLY GLY A . n 
A 1 333 ARG 333 333 333 ARG ARG A . n 
A 1 334 LEU 334 334 334 LEU LEU A . n 
A 1 335 LYS 335 335 335 LYS LYS A . n 
A 1 336 LYS 336 336 336 LYS LYS A . n 
A 1 337 ILE 337 337 337 ILE ILE A . n 
A 1 338 HIS 338 338 338 HIS HIS A . n 
A 1 339 GLU 339 339 339 GLU GLU A . n 
A 1 340 SER 340 340 340 SER SER A . n 
A 1 341 VAL 341 341 341 VAL VAL A . n 
A 1 342 ASP 342 342 342 ASP ASP A . n 
A 1 343 PHE 343 343 343 PHE PHE A . n 
A 1 344 GLN 344 344 344 GLN GLN A . n 
A 1 345 PRO 345 345 345 PRO PRO A . n 
A 1 346 VAL 346 346 346 VAL VAL A . n 
A 1 347 VAL 347 347 347 VAL VAL A . n 
A 1 348 PHE 348 348 348 PHE PHE A . n 
A 1 349 VAL 349 349 349 VAL VAL A . n 
A 1 350 VAL 350 350 350 VAL VAL A . n 
A 1 351 LEU 351 351 351 LEU LEU A . n 
A 1 352 ASP 352 352 352 ASP ASP A . n 
A 1 353 GLY 353 353 353 GLY GLY A . n 
A 1 354 GLU 354 354 354 GLU GLU A . n 
A 1 355 ASN 355 355 355 ASN ASN A . n 
A 1 356 CYS 356 356 356 CYS CYS A . n 
A 1 357 TRP 357 357 357 TRP TRP A . n 
A 1 358 GLU 358 358 358 GLU GLU A . n 
A 1 359 TYR 359 359 359 TYR TYR A . n 
A 1 360 TYR 360 360 360 TYR TYR A . n 
A 1 361 GLU 361 361 361 GLU GLU A . n 
A 1 362 GLU 362 362 362 GLU GLU A . n 
A 1 363 ASN 363 363 363 ASN ASN A . n 
A 1 364 GLY 364 364 364 GLY GLY A . n 
A 1 365 ILE 365 365 365 ILE ILE A . n 
A 1 366 PRO 366 366 366 PRO PRO A . n 
A 1 367 PHE 367 367 367 PHE PHE A . n 
A 1 368 LEU 368 368 368 LEU LEU A . n 
A 1 369 GLU 369 369 369 GLU GLU A . n 
A 1 370 LYS 370 370 370 LYS LYS A . n 
A 1 371 LEU 371 371 371 LEU LEU A . n 
A 1 372 TYR 372 372 372 TYR TYR A . n 
A 1 373 SER 373 373 373 SER SER A . n 
A 1 374 THR 374 374 374 THR THR A . n 
A 1 375 LEU 375 375 375 LEU LEU A . n 
A 1 376 GLU 376 376 376 GLU GLU A . n 
A 1 377 LYS 377 377 377 LYS LYS A . n 
A 1 378 GLU 378 378 378 GLU GLU A . n 
A 1 379 GLU 379 379 379 GLU GLU A . n 
A 1 380 TRP 380 380 380 TRP TRP A . n 
A 1 381 ILE 381 381 381 ILE ILE A . n 
A 1 382 GLU 382 382 382 GLU GLU A . n 
A 1 383 THR 383 383 383 THR THR A . n 
A 1 384 LEU 384 384 384 LEU LEU A . n 
A 1 385 THR 385 385 385 THR THR A . n 
A 1 386 LEU 386 386 386 LEU LEU A . n 
A 1 387 GLU 387 387 387 GLU GLU A . n 
A 1 388 GLU 388 388 388 GLU GLU A . n 
A 1 389 ALA 389 389 389 ALA ALA A . n 
A 1 390 MET 390 390 390 MET MET A . n 
A 1 391 ARG 391 391 391 ARG ARG A . n 
A 1 392 LYS 392 392 392 LYS LYS A . n 
A 1 393 GLU 393 393 393 GLU GLU A . n 
A 1 394 ASP 394 394 394 ASP ASP A . n 
A 1 395 VAL 395 395 395 VAL VAL A . n 
A 1 396 LYS 396 396 396 LYS LYS A . n 
A 1 397 THR 397 397 397 THR THR A . n 
A 1 398 GLU 398 398 398 GLU GLU A . n 
A 1 399 VAL 399 399 399 VAL VAL A . n 
A 1 400 ILE 400 400 400 ILE ILE A . n 
A 1 401 GLU 401 401 401 GLU GLU A . n 
A 1 402 SER 402 402 402 SER SER A . n 
A 1 403 VAL 403 403 403 VAL VAL A . n 
A 1 404 LYS 404 404 404 LYS LYS A . n 
A 1 405 ALA 405 405 405 ALA ALA A . n 
A 1 406 GLY 406 406 406 GLY GLY A . n 
A 1 407 THR 407 407 407 THR THR A . n 
A 1 408 TRP 408 408 408 TRP TRP A . n 
A 1 409 PHE 409 409 409 PHE PHE A . n 
A 1 410 ASP 410 410 410 ASP ASP A . n 
A 1 411 GLY 411 411 411 GLY GLY A . n 
A 1 412 ASN 412 412 412 ASN ASN A . n 
A 1 413 PHE 413 413 413 PHE PHE A . n 
A 1 414 LEU 414 414 414 LEU LEU A . n 
A 1 415 LYS 415 415 415 LYS LYS A . n 
A 1 416 TRP 416 416 416 TRP TRP A . n 
A 1 417 ILE 417 417 417 ILE ILE A . n 
A 1 418 GLY 418 418 418 GLY GLY A . n 
A 1 419 ASN 419 419 419 ASN ASN A . n 
A 1 420 LYS 420 420 420 LYS LYS A . n 
A 1 421 GLU 421 421 421 GLU GLU A . n 
A 1 422 LYS 422 422 422 LYS LYS A . n 
A 1 423 ASN 423 423 423 ASN ASN A . n 
A 1 424 GLU 424 424 424 GLU GLU A . n 
A 1 425 TYR 425 425 425 TYR TYR A . n 
A 1 426 TRP 426 426 426 TRP TRP A . n 
A 1 427 LYS 427 427 427 LYS LYS A . n 
A 1 428 ILE 428 428 428 ILE ILE A . n 
A 1 429 LEU 429 429 429 LEU LEU A . n 
A 1 430 ILE 430 430 430 ILE ILE A . n 
A 1 431 GLU 431 431 431 GLU GLU A . n 
A 1 432 ALA 432 432 432 ALA ALA A . n 
A 1 433 LYS 433 433 433 LYS LYS A . n 
A 1 434 LYS 434 434 434 LYS LYS A . n 
A 1 435 LYS 435 435 435 LYS LYS A . n 
A 1 436 ALA 436 436 436 ALA ALA A . n 
A 1 437 LYS 437 437 437 LYS LYS A . n 
A 1 438 ASN 438 438 438 ASN ASN A . n 
A 1 439 ASP 439 439 439 ASP ASP A . n 
A 1 440 TYR 440 440 440 TYR TYR A . n 
A 1 441 ILE 441 441 441 ILE ILE A . n 
A 1 442 LEU 442 442 442 LEU LEU A . n 
A 1 443 VAL 443 443 443 VAL VAL A . n 
A 1 444 ALA 444 444 444 ALA ALA A . n 
A 1 445 GLU 445 445 445 GLU GLU A . n 
A 1 446 GLY 446 446 446 GLY GLY A . n 
A 1 447 SER 447 447 447 SER SER A . n 
A 1 448 ASP 448 448 448 ASP ASP A . n 
A 1 449 TRP 449 449 449 TRP TRP A . n 
A 1 450 PHE 450 450 450 PHE PHE A . n 
A 1 451 TRP 451 451 451 TRP TRP A . n 
A 1 452 TRP 452 452 452 TRP TRP A . n 
A 1 453 GLN 453 453 453 GLN GLN A . n 
A 1 454 GLY 454 454 454 GLY GLY A . n 
A 1 455 GLU 455 455 455 GLU GLU A . n 
A 1 456 GLU 456 456 456 GLU GLU A . n 
A 1 457 LYS 457 457 457 LYS LYS A . n 
A 1 458 ALA 458 458 458 ALA ALA A . n 
A 1 459 PRO 459 459 459 PRO PRO A . n 
A 1 460 PHE 460 460 460 PHE PHE A . n 
A 1 461 VAL 461 461 461 VAL VAL A . n 
A 1 462 GLU 462 462 462 GLU GLU A . n 
A 1 463 VAL 463 463 463 VAL VAL A . n 
A 1 464 PHE 464 464 464 PHE PHE A . n 
A 1 465 ASP 465 465 465 ASP ASP A . n 
A 1 466 LYS 466 466 466 LYS LYS A . n 
A 1 467 LEU 467 467 467 LEU LEU A . n 
A 1 468 PHE 468 468 468 PHE PHE A . n 
A 1 469 ARG 469 469 469 ARG ARG A . n 
A 1 470 SER 470 470 470 SER SER A . n 
A 1 471 PHE 471 471 471 PHE PHE A . n 
A 1 472 VAL 472 472 472 VAL VAL A . n 
A 1 473 ARG 473 473 473 ARG ARG A . n 
A 1 474 ARG 474 474 474 ARG ARG A . n 
A 1 475 ALA 475 475 475 ALA ALA A . n 
A 1 476 GLN 476 476 476 GLN GLN A . n 
A 1 477 GLU 477 477 477 GLU GLU A . n 
B 1 1   MET 1   1   ?   ?   ?   B . n 
B 1 2   LYS 2   2   2   LYS LYS B . n 
B 1 3   LYS 3   3   3   LYS LYS B . n 
B 1 4   LEU 4   4   4   LEU LEU B . n 
B 1 5   PHE 5   5   5   PHE PHE B . n 
B 1 6   LEU 6   6   6   LEU LEU B . n 
B 1 7   VAL 7   7   7   VAL VAL B . n 
B 1 8   PHE 8   8   8   PHE PHE B . n 
B 1 9   TRP 9   9   9   TRP TRP B . n 
B 1 10  TRP 10  10  10  TRP TRP B . n 
B 1 11  HIS 11  11  11  HIS HIS B . n 
B 1 12  MET 12  12  12  MET MET B . n 
B 1 13  HIS 13  13  13  HIS HIS B . n 
B 1 14  GLN 14  14  14  GLN GLN B . n 
B 1 15  PRO 15  15  15  PRO PRO B . n 
B 1 16  LEU 16  16  16  LEU LEU B . n 
B 1 17  TYR 17  17  17  TYR TYR B . n 
B 1 18  ARG 18  18  18  ARG ARG B . n 
B 1 19  GLU 19  19  19  GLU GLU B . n 
B 1 20  PRO 20  20  20  PRO PRO B . n 
B 1 21  TYR 21  21  21  TYR TYR B . n 
B 1 22  THR 22  22  22  THR THR B . n 
B 1 23  GLY 23  23  23  GLY GLY B . n 
B 1 24  GLU 24  24  24  GLU GLU B . n 
B 1 25  TYR 25  25  25  TYR TYR B . n 
B 1 26  LEU 26  26  26  LEU LEU B . n 
B 1 27  LEU 27  27  27  LEU LEU B . n 
B 1 28  PRO 28  28  28  PRO PRO B . n 
B 1 29  TRP 29  29  29  TRP TRP B . n 
B 1 30  THR 30  30  30  THR THR B . n 
B 1 31  PHE 31  31  31  PHE PHE B . n 
B 1 32  PHE 32  32  32  PHE PHE B . n 
B 1 33  HIS 33  33  33  HIS HIS B . n 
B 1 34  ALA 34  34  34  ALA ALA B . n 
B 1 35  VAL 35  35  35  VAL VAL B . n 
B 1 36  LYS 36  36  36  LYS LYS B . n 
B 1 37  ASP 37  37  37  ASP ASP B . n 
B 1 38  TYR 38  38  38  TYR TYR B . n 
B 1 39  TYR 39  39  39  TYR TYR B . n 
B 1 40  ASP 40  40  40  ASP ASP B . n 
B 1 41  MET 41  41  41  MET MET B . n 
B 1 42  PRO 42  42  42  PRO PRO B . n 
B 1 43  ALA 43  43  43  ALA ALA B . n 
B 1 44  TYR 44  44  44  TYR TYR B . n 
B 1 45  LEU 45  45  45  LEU LEU B . n 
B 1 46  LYS 46  46  46  LYS LYS B . n 
B 1 47  ASP 47  47  47  ASP ASP B . n 
B 1 48  PHE 48  48  48  PHE PHE B . n 
B 1 49  GLU 49  49  49  GLU GLU B . n 
B 1 50  ILE 50  50  50  ILE ILE B . n 
B 1 51  LYS 51  51  51  LYS LYS B . n 
B 1 52  LEU 52  52  52  LEU LEU B . n 
B 1 53  ASN 53  53  53  ASN ASN B . n 
B 1 54  PHE 54  54  54  PHE PHE B . n 
B 1 55  ASN 55  55  55  ASN ASN B . n 
B 1 56  LEU 56  56  56  LEU LEU B . n 
B 1 57  THR 57  57  57  THR THR B . n 
B 1 58  PRO 58  58  58  PRO PRO B . n 
B 1 59  VAL 59  59  59  VAL VAL B . n 
B 1 60  LEU 60  60  60  LEU LEU B . n 
B 1 61  ILE 61  61  61  ILE ILE B . n 
B 1 62  ASP 62  62  62  ASP ASP B . n 
B 1 63  GLN 63  63  63  GLN GLN B . n 
B 1 64  ILE 64  64  64  ILE ILE B . n 
B 1 65  GLN 65  65  65  GLN GLN B . n 
B 1 66  GLU 66  66  66  GLU GLU B . n 
B 1 67  TYR 67  67  67  TYR TYR B . n 
B 1 68  ALA 68  68  68  ALA ALA B . n 
B 1 69  GLN 69  69  69  GLN GLN B . n 
B 1 70  GLY 70  70  70  GLY GLY B . n 
B 1 71  LYS 71  71  71  LYS LYS B . n 
B 1 72  ALA 72  72  72  ALA ALA B . n 
B 1 73  LYS 73  73  73  LYS LYS B . n 
B 1 74  ASP 74  74  74  ASP ASP B . n 
B 1 75  VAL 75  75  75  VAL VAL B . n 
B 1 76  PHE 76  76  76  PHE PHE B . n 
B 1 77  LEU 77  77  77  LEU LEU B . n 
B 1 78  GLU 78  78  78  GLU GLU B . n 
B 1 79  ALA 79  79  79  ALA ALA B . n 
B 1 80  ILE 80  80  80  ILE ILE B . n 
B 1 81  ARG 81  81  81  ARG ARG B . n 
B 1 82  LYS 82  82  82  LYS LYS B . n 
B 1 83  ASP 83  83  83  ASP ASP B . n 
B 1 84  PRO 84  84  84  PRO PRO B . n 
B 1 85  ASP 85  85  85  ASP ASP B . n 
B 1 86  ASP 86  86  86  ASP ASP B . n 
B 1 87  LEU 87  87  87  LEU LEU B . n 
B 1 88  GLU 88  88  88  GLU GLU B . n 
B 1 89  LYS 89  89  89  LYS LYS B . n 
B 1 90  GLU 90  90  90  GLU GLU B . n 
B 1 91  GLU 91  91  91  GLU GLU B . n 
B 1 92  VAL 92  92  92  VAL VAL B . n 
B 1 93  GLU 93  93  93  GLU GLU B . n 
B 1 94  LYS 94  94  94  LYS LYS B . n 
B 1 95  LEU 95  95  95  LEU LEU B . n 
B 1 96  ILE 96  96  96  ILE ILE B . n 
B 1 97  GLU 97  97  97  GLU GLU B . n 
B 1 98  PHE 98  98  98  PHE PHE B . n 
B 1 99  THR 99  99  99  THR THR B . n 
B 1 100 LYS 100 100 100 LYS LYS B . n 
B 1 101 LEU 101 101 101 LEU LEU B . n 
B 1 102 ASN 102 102 102 ASN ASN B . n 
B 1 103 TYR 103 103 103 TYR TYR B . n 
B 1 104 GLU 104 104 104 GLU GLU B . n 
B 1 105 LYS 105 105 105 LYS LYS B . n 
B 1 106 PRO 106 106 106 PRO PRO B . n 
B 1 107 ILE 107 107 107 ILE ILE B . n 
B 1 108 TYR 108 108 108 TYR TYR B . n 
B 1 109 ARG 109 109 109 ARG ARG B . n 
B 1 110 PHE 110 110 110 PHE PHE B . n 
B 1 111 GLU 111 111 111 GLU GLU B . n 
B 1 112 ARG 112 112 112 ARG ARG B . n 
B 1 113 ILE 113 113 113 ILE ILE B . n 
B 1 114 ARG 114 114 114 ARG ARG B . n 
B 1 115 GLU 115 115 115 GLU GLU B . n 
B 1 116 LEU 116 116 116 LEU LEU B . n 
B 1 117 MET 117 117 117 MET MET B . n 
B 1 118 ASN 118 118 118 ASN ASN B . n 
B 1 119 LYS 119 119 119 LYS LYS B . n 
B 1 120 GLU 120 120 120 GLU GLU B . n 
B 1 121 LYS 121 121 121 LYS LYS B . n 
B 1 122 LEU 122 122 122 LEU LEU B . n 
B 1 123 ASN 123 123 123 ASN ASN B . n 
B 1 124 ARG 124 124 124 ARG ARG B . n 
B 1 125 GLU 125 125 125 GLU GLU B . n 
B 1 126 GLU 126 126 126 GLU GLU B . n 
B 1 127 LEU 127 127 127 LEU LEU B . n 
B 1 128 LEU 128 128 128 LEU LEU B . n 
B 1 129 ASP 129 129 129 ASP ASP B . n 
B 1 130 LEU 130 130 130 LEU LEU B . n 
B 1 131 GLN 131 131 131 GLN GLN B . n 
B 1 132 THR 132 132 132 THR THR B . n 
B 1 133 LEU 133 133 133 LEU LEU B . n 
B 1 134 ASN 134 134 134 ASN ASN B . n 
B 1 135 LEU 135 135 135 LEU LEU B . n 
B 1 136 LEU 136 136 136 LEU LEU B . n 
B 1 137 ALA 137 137 137 ALA ALA B . n 
B 1 138 TRP 138 138 138 TRP TRP B . n 
B 1 139 CYS 139 139 139 CYS CYS B . n 
B 1 140 GLY 140 140 140 GLY GLY B . n 
B 1 141 ARG 141 141 141 ARG ARG B . n 
B 1 142 THR 142 142 142 THR THR B . n 
B 1 143 LEU 143 143 143 LEU LEU B . n 
B 1 144 ARG 144 144 144 ARG ARG B . n 
B 1 145 LYS 145 145 145 LYS LYS B . n 
B 1 146 ASP 146 146 146 ASP ASP B . n 
B 1 147 LEU 147 147 147 LEU LEU B . n 
B 1 148 LYS 148 148 148 LYS LYS B . n 
B 1 149 ASP 149 149 149 ASP ASP B . n 
B 1 150 LEU 150 150 150 LEU LEU B . n 
B 1 151 LEU 151 151 151 LEU LEU B . n 
B 1 152 ASN 152 152 152 ASN ASN B . n 
B 1 153 LYS 153 153 153 LYS LYS B . n 
B 1 154 GLY 154 154 154 GLY GLY B . n 
B 1 155 ARG 155 155 155 ARG ARG B . n 
B 1 156 ASN 156 156 156 ASN ASN B . n 
B 1 157 TYR 157 157 157 TYR TYR B . n 
B 1 158 THR 158 158 158 THR THR B . n 
B 1 159 GLN 159 159 159 GLN GLN B . n 
B 1 160 GLU 160 160 160 GLU GLU B . n 
B 1 161 GLU 161 161 161 GLU GLU B . n 
B 1 162 LYS 162 162 162 LYS LYS B . n 
B 1 163 GLU 163 163 163 GLU GLU B . n 
B 1 164 TYR 164 164 164 TYR TYR B . n 
B 1 165 VAL 165 165 165 VAL VAL B . n 
B 1 166 LEU 166 166 166 LEU LEU B . n 
B 1 167 ASN 167 167 167 ASN ASN B . n 
B 1 168 LYS 168 168 168 LYS LYS B . n 
B 1 169 TYR 169 169 169 TYR TYR B . n 
B 1 170 PHE 170 170 170 PHE PHE B . n 
B 1 171 GLU 171 171 171 GLU GLU B . n 
B 1 172 ILE 172 172 172 ILE ILE B . n 
B 1 173 ILE 173 173 173 ILE ILE B . n 
B 1 174 LYS 174 174 174 LYS LYS B . n 
B 1 175 LYS 175 175 175 LYS LYS B . n 
B 1 176 THR 176 176 176 THR THR B . n 
B 1 177 LEU 177 177 177 LEU LEU B . n 
B 1 178 SER 178 178 178 SER SER B . n 
B 1 179 ILE 179 179 179 ILE ILE B . n 
B 1 180 TYR 180 180 180 TYR TYR B . n 
B 1 181 ARG 181 181 181 ARG ARG B . n 
B 1 182 GLU 182 182 182 GLU GLU B . n 
B 1 183 ILE 183 183 183 ILE ILE B . n 
B 1 184 LYS 184 184 184 LYS LYS B . n 
B 1 185 GLU 185 185 185 GLU GLU B . n 
B 1 186 GLU 186 186 186 GLU GLU B . n 
B 1 187 GLY 187 187 187 GLY GLY B . n 
B 1 188 LYS 188 188 188 LYS LYS B . n 
B 1 189 GLY 189 189 189 GLY GLY B . n 
B 1 190 SER 190 190 190 SER SER B . n 
B 1 191 VAL 191 191 191 VAL VAL B . n 
B 1 192 SER 192 192 192 SER SER B . n 
B 1 193 THR 193 193 193 THR THR B . n 
B 1 194 SER 194 194 194 SER SER B . n 
B 1 195 PRO 195 195 195 PRO PRO B . n 
B 1 196 TYR 196 196 196 TYR TYR B . n 
B 1 197 TYR 197 197 197 TYR TYR B . n 
B 1 198 HIS 198 198 198 HIS HIS B . n 
B 1 199 PRO 199 199 199 PRO PRO B . n 
B 1 200 LEU 200 200 200 LEU LEU B . n 
B 1 201 ILE 201 201 201 ILE ILE B . n 
B 1 202 PRO 202 202 202 PRO PRO B . n 
B 1 203 ILE 203 203 203 ILE ILE B . n 
B 1 204 LEU 204 204 204 LEU LEU B . n 
B 1 205 LEU 205 205 205 LEU LEU B . n 
B 1 206 ASN 206 206 206 ASN ASN B . n 
B 1 207 PRO 207 207 207 PRO PRO B . n 
B 1 208 ASN 208 208 208 ASN ASN B . n 
B 1 209 CYS 209 209 209 CYS CYS B . n 
B 1 210 VAL 210 210 210 VAL VAL B . n 
B 1 211 TYR 211 211 211 TYR TYR B . n 
B 1 212 GLU 212 212 212 GLU GLU B . n 
B 1 213 THR 213 213 213 THR THR B . n 
B 1 214 THR 214 214 214 THR THR B . n 
B 1 215 PRO 215 215 215 PRO PRO B . n 
B 1 216 ASN 216 216 216 ASN ASN B . n 
B 1 217 VAL 217 217 217 VAL VAL B . n 
B 1 218 LYS 218 218 218 LYS LYS B . n 
B 1 219 ILE 219 219 219 ILE ILE B . n 
B 1 220 PRO 220 220 220 PRO PRO B . n 
B 1 221 ASP 221 221 221 ASP ASP B . n 
B 1 222 PHE 222 222 222 PHE PHE B . n 
B 1 223 ALA 223 223 223 ALA ALA B . n 
B 1 224 VAL 224 224 224 VAL VAL B . n 
B 1 225 SER 225 225 225 SER SER B . n 
B 1 226 PHE 226 226 226 PHE PHE B . n 
B 1 227 ARG 227 227 227 ARG ARG B . n 
B 1 228 GLU 228 228 228 GLU GLU B . n 
B 1 229 ASP 229 229 229 ASP ASP B . n 
B 1 230 ALA 230 230 230 ALA ALA B . n 
B 1 231 SER 231 231 231 SER SER B . n 
B 1 232 LYS 232 232 232 LYS LYS B . n 
B 1 233 HIS 233 233 233 HIS HIS B . n 
B 1 234 VAL 234 234 234 VAL VAL B . n 
B 1 235 GLU 235 235 235 GLU GLU B . n 
B 1 236 LEU 236 236 236 LEU LEU B . n 
B 1 237 ALA 237 237 237 ALA ALA B . n 
B 1 238 LYS 238 238 238 LYS LYS B . n 
B 1 239 GLU 239 239 239 GLU GLU B . n 
B 1 240 LYS 240 240 240 LYS LYS B . n 
B 1 241 TYR 241 241 241 TYR TYR B . n 
B 1 242 PHE 242 242 242 PHE PHE B . n 
B 1 243 GLU 243 243 243 GLU GLU B . n 
B 1 244 ILE 244 244 244 ILE ILE B . n 
B 1 245 PHE 245 245 245 PHE PHE B . n 
B 1 246 GLY 246 246 246 GLY GLY B . n 
B 1 247 GLU 247 247 247 GLU GLU B . n 
B 1 248 HIS 248 248 248 HIS HIS B . n 
B 1 249 PRO 249 249 249 PRO PRO B . n 
B 1 250 VAL 250 250 250 VAL VAL B . n 
B 1 251 TYR 251 251 251 TYR TYR B . n 
B 1 252 MET 252 252 252 MET MET B . n 
B 1 253 TRP 253 253 253 TRP TRP B . n 
B 1 254 PRO 254 254 254 PRO PRO B . n 
B 1 255 PRO 255 255 255 PRO PRO B . n 
B 1 256 GLN 256 256 256 GLN GLN B . n 
B 1 257 ALA 257 257 257 ALA ALA B . n 
B 1 258 SER 258 258 258 SER SER B . n 
B 1 259 VAL 259 259 259 VAL VAL B . n 
B 1 260 SER 260 260 260 SER SER B . n 
B 1 261 ASN 261 261 261 ASN ASN B . n 
B 1 262 GLU 262 262 262 GLU GLU B . n 
B 1 263 ALA 263 263 263 ALA ALA B . n 
B 1 264 LEU 264 264 264 LEU LEU B . n 
B 1 265 GLU 265 265 265 GLU GLU B . n 
B 1 266 LEU 266 266 266 LEU LEU B . n 
B 1 267 TYR 267 267 267 TYR TYR B . n 
B 1 268 TYR 268 268 268 TYR TYR B . n 
B 1 269 GLU 269 269 269 GLU GLU B . n 
B 1 270 LYS 270 270 270 LYS LYS B . n 
B 1 271 GLY 271 271 271 GLY GLY B . n 
B 1 272 ILE 272 272 272 ILE ILE B . n 
B 1 273 ASN 273 273 273 ASN ASN B . n 
B 1 274 MET 274 274 274 MET MET B . n 
B 1 275 LEU 275 275 275 LEU LEU B . n 
B 1 276 ALA 276 276 276 ALA ALA B . n 
B 1 277 THR 277 277 277 THR THR B . n 
B 1 278 ASP 278 278 278 ASP ASP B . n 
B 1 279 GLU 279 279 279 GLU GLU B . n 
B 1 280 VAL 280 280 280 VAL VAL B . n 
B 1 281 ILE 281 281 281 ILE ILE B . n 
B 1 282 LEU 282 282 282 LEU LEU B . n 
B 1 283 LYS 283 283 283 LYS LYS B . n 
B 1 284 ASN 284 284 284 ASN ASN B . n 
B 1 285 SER 285 285 285 SER SER B . n 
B 1 286 VAL 286 286 286 VAL VAL B . n 
B 1 287 GLU 287 287 287 GLU GLU B . n 
B 1 288 ARG 288 288 288 ARG ARG B . n 
B 1 289 ALA 289 289 289 ALA ALA B . n 
B 1 290 SER 290 290 290 SER SER B . n 
B 1 291 PRO 291 291 291 PRO PRO B . n 
B 1 292 TYR 292 292 292 TYR TYR B . n 
B 1 293 LEU 293 293 293 LEU LEU B . n 
B 1 294 ARG 294 294 294 ARG ARG B . n 
B 1 295 TYR 295 295 295 TYR TYR B . n 
B 1 296 TYR 296 296 296 TYR TYR B . n 
B 1 297 PHE 297 297 297 PHE PHE B . n 
B 1 298 ARG 298 298 298 ARG ARG B . n 
B 1 299 GLU 299 299 299 GLU GLU B . n 
B 1 300 LEU 300 300 300 LEU LEU B . n 
B 1 301 ILE 301 301 301 ILE ILE B . n 
B 1 302 SER 302 302 302 SER SER B . n 
B 1 303 VAL 303 303 303 VAL VAL B . n 
B 1 304 PHE 304 304 304 PHE PHE B . n 
B 1 305 PHE 305 305 305 PHE PHE B . n 
B 1 306 ARG 306 306 306 ARG ARG B . n 
B 1 307 ASP 307 307 307 ASP ASP B . n 
B 1 308 LYS 308 308 308 LYS LYS B . n 
B 1 309 THR 309 309 309 THR THR B . n 
B 1 310 LEU 310 310 310 LEU LEU B . n 
B 1 311 SER 311 311 311 SER SER B . n 
B 1 312 ASP 312 312 312 ASP ASP B . n 
B 1 313 LEU 313 313 313 LEU LEU B . n 
B 1 314 ILE 314 314 314 ILE ILE B . n 
B 1 315 GLY 315 315 315 GLY GLY B . n 
B 1 316 PHE 316 316 316 PHE PHE B . n 
B 1 317 SER 317 317 317 SER SER B . n 
B 1 318 TYR 318 318 318 TYR TYR B . n 
B 1 319 HIS 319 319 319 HIS HIS B . n 
B 1 320 ALA 320 320 320 ALA ALA B . n 
B 1 321 TRP 321 321 321 TRP TRP B . n 
B 1 322 ASN 322 322 322 ASN ASN B . n 
B 1 323 ALA 323 323 323 ALA ALA B . n 
B 1 324 GLU 324 324 324 GLU GLU B . n 
B 1 325 ASP 325 325 325 ASP ASP B . n 
B 1 326 ALA 326 326 326 ALA ALA B . n 
B 1 327 VAL 327 327 327 VAL VAL B . n 
B 1 328 ARG 328 328 328 ARG ARG B . n 
B 1 329 ASP 329 329 329 ASP ASP B . n 
B 1 330 PHE 330 330 330 PHE PHE B . n 
B 1 331 ILE 331 331 331 ILE ILE B . n 
B 1 332 GLY 332 332 332 GLY GLY B . n 
B 1 333 ARG 333 333 333 ARG ARG B . n 
B 1 334 LEU 334 334 334 LEU LEU B . n 
B 1 335 LYS 335 335 335 LYS LYS B . n 
B 1 336 LYS 336 336 336 LYS LYS B . n 
B 1 337 ILE 337 337 337 ILE ILE B . n 
B 1 338 HIS 338 338 338 HIS HIS B . n 
B 1 339 GLU 339 339 339 GLU GLU B . n 
B 1 340 SER 340 340 340 SER SER B . n 
B 1 341 VAL 341 341 341 VAL VAL B . n 
B 1 342 ASP 342 342 342 ASP ASP B . n 
B 1 343 PHE 343 343 343 PHE PHE B . n 
B 1 344 GLN 344 344 344 GLN GLN B . n 
B 1 345 PRO 345 345 345 PRO PRO B . n 
B 1 346 VAL 346 346 346 VAL VAL B . n 
B 1 347 VAL 347 347 347 VAL VAL B . n 
B 1 348 PHE 348 348 348 PHE PHE B . n 
B 1 349 VAL 349 349 349 VAL VAL B . n 
B 1 350 VAL 350 350 350 VAL VAL B . n 
B 1 351 LEU 351 351 351 LEU LEU B . n 
B 1 352 ASP 352 352 352 ASP ASP B . n 
B 1 353 GLY 353 353 353 GLY GLY B . n 
B 1 354 GLU 354 354 354 GLU GLU B . n 
B 1 355 ASN 355 355 355 ASN ASN B . n 
B 1 356 CYS 356 356 356 CYS CYS B . n 
B 1 357 TRP 357 357 357 TRP TRP B . n 
B 1 358 GLU 358 358 358 GLU GLU B . n 
B 1 359 TYR 359 359 359 TYR TYR B . n 
B 1 360 TYR 360 360 360 TYR TYR B . n 
B 1 361 GLU 361 361 361 GLU GLU B . n 
B 1 362 GLU 362 362 362 GLU GLU B . n 
B 1 363 ASN 363 363 363 ASN ASN B . n 
B 1 364 GLY 364 364 364 GLY GLY B . n 
B 1 365 ILE 365 365 365 ILE ILE B . n 
B 1 366 PRO 366 366 366 PRO PRO B . n 
B 1 367 PHE 367 367 367 PHE PHE B . n 
B 1 368 LEU 368 368 368 LEU LEU B . n 
B 1 369 GLU 369 369 369 GLU GLU B . n 
B 1 370 LYS 370 370 370 LYS LYS B . n 
B 1 371 LEU 371 371 371 LEU LEU B . n 
B 1 372 TYR 372 372 372 TYR TYR B . n 
B 1 373 SER 373 373 373 SER SER B . n 
B 1 374 THR 374 374 374 THR THR B . n 
B 1 375 LEU 375 375 375 LEU LEU B . n 
B 1 376 GLU 376 376 376 GLU GLU B . n 
B 1 377 LYS 377 377 377 LYS LYS B . n 
B 1 378 GLU 378 378 378 GLU GLU B . n 
B 1 379 GLU 379 379 379 GLU GLU B . n 
B 1 380 TRP 380 380 380 TRP TRP B . n 
B 1 381 ILE 381 381 381 ILE ILE B . n 
B 1 382 GLU 382 382 382 GLU GLU B . n 
B 1 383 THR 383 383 383 THR THR B . n 
B 1 384 LEU 384 384 384 LEU LEU B . n 
B 1 385 THR 385 385 385 THR THR B . n 
B 1 386 LEU 386 386 386 LEU LEU B . n 
B 1 387 GLU 387 387 387 GLU GLU B . n 
B 1 388 GLU 388 388 388 GLU GLU B . n 
B 1 389 ALA 389 389 389 ALA ALA B . n 
B 1 390 MET 390 390 390 MET MET B . n 
B 1 391 ARG 391 391 391 ARG ARG B . n 
B 1 392 LYS 392 392 392 LYS LYS B . n 
B 1 393 GLU 393 393 393 GLU GLU B . n 
B 1 394 ASP 394 394 394 ASP ASP B . n 
B 1 395 VAL 395 395 395 VAL VAL B . n 
B 1 396 LYS 396 396 396 LYS LYS B . n 
B 1 397 THR 397 397 397 THR THR B . n 
B 1 398 GLU 398 398 398 GLU GLU B . n 
B 1 399 VAL 399 399 399 VAL VAL B . n 
B 1 400 ILE 400 400 400 ILE ILE B . n 
B 1 401 GLU 401 401 401 GLU GLU B . n 
B 1 402 SER 402 402 402 SER SER B . n 
B 1 403 VAL 403 403 403 VAL VAL B . n 
B 1 404 LYS 404 404 404 LYS LYS B . n 
B 1 405 ALA 405 405 405 ALA ALA B . n 
B 1 406 GLY 406 406 406 GLY GLY B . n 
B 1 407 THR 407 407 407 THR THR B . n 
B 1 408 TRP 408 408 408 TRP TRP B . n 
B 1 409 PHE 409 409 409 PHE PHE B . n 
B 1 410 ASP 410 410 410 ASP ASP B . n 
B 1 411 GLY 411 411 411 GLY GLY B . n 
B 1 412 ASN 412 412 412 ASN ASN B . n 
B 1 413 PHE 413 413 413 PHE PHE B . n 
B 1 414 LEU 414 414 414 LEU LEU B . n 
B 1 415 LYS 415 415 415 LYS LYS B . n 
B 1 416 TRP 416 416 416 TRP TRP B . n 
B 1 417 ILE 417 417 417 ILE ILE B . n 
B 1 418 GLY 418 418 418 GLY GLY B . n 
B 1 419 ASN 419 419 419 ASN ASN B . n 
B 1 420 LYS 420 420 420 LYS LYS B . n 
B 1 421 GLU 421 421 421 GLU GLU B . n 
B 1 422 LYS 422 422 422 LYS LYS B . n 
B 1 423 ASN 423 423 423 ASN ASN B . n 
B 1 424 GLU 424 424 424 GLU GLU B . n 
B 1 425 TYR 425 425 425 TYR TYR B . n 
B 1 426 TRP 426 426 426 TRP TRP B . n 
B 1 427 LYS 427 427 427 LYS LYS B . n 
B 1 428 ILE 428 428 428 ILE ILE B . n 
B 1 429 LEU 429 429 429 LEU LEU B . n 
B 1 430 ILE 430 430 430 ILE ILE B . n 
B 1 431 GLU 431 431 431 GLU GLU B . n 
B 1 432 ALA 432 432 432 ALA ALA B . n 
B 1 433 LYS 433 433 433 LYS LYS B . n 
B 1 434 LYS 434 434 434 LYS LYS B . n 
B 1 435 LYS 435 435 435 LYS LYS B . n 
B 1 436 ALA 436 436 436 ALA ALA B . n 
B 1 437 LYS 437 437 437 LYS LYS B . n 
B 1 438 ASN 438 438 438 ASN ASN B . n 
B 1 439 ASP 439 439 439 ASP ASP B . n 
B 1 440 TYR 440 440 440 TYR TYR B . n 
B 1 441 ILE 441 441 441 ILE ILE B . n 
B 1 442 LEU 442 442 442 LEU LEU B . n 
B 1 443 VAL 443 443 443 VAL VAL B . n 
B 1 444 ALA 444 444 444 ALA ALA B . n 
B 1 445 GLU 445 445 445 GLU GLU B . n 
B 1 446 GLY 446 446 446 GLY GLY B . n 
B 1 447 SER 447 447 447 SER SER B . n 
B 1 448 ASP 448 448 448 ASP ASP B . n 
B 1 449 TRP 449 449 449 TRP TRP B . n 
B 1 450 PHE 450 450 450 PHE PHE B . n 
B 1 451 TRP 451 451 451 TRP TRP B . n 
B 1 452 TRP 452 452 452 TRP TRP B . n 
B 1 453 GLN 453 453 453 GLN GLN B . n 
B 1 454 GLY 454 454 454 GLY GLY B . n 
B 1 455 GLU 455 455 455 GLU GLU B . n 
B 1 456 GLU 456 456 456 GLU GLU B . n 
B 1 457 LYS 457 457 457 LYS LYS B . n 
B 1 458 ALA 458 458 458 ALA ALA B . n 
B 1 459 PRO 459 459 459 PRO PRO B . n 
B 1 460 PHE 460 460 460 PHE PHE B . n 
B 1 461 VAL 461 461 461 VAL VAL B . n 
B 1 462 GLU 462 462 462 GLU GLU B . n 
B 1 463 VAL 463 463 463 VAL VAL B . n 
B 1 464 PHE 464 464 464 PHE PHE B . n 
B 1 465 ASP 465 465 465 ASP ASP B . n 
B 1 466 LYS 466 466 466 LYS LYS B . n 
B 1 467 LEU 467 467 467 LEU LEU B . n 
B 1 468 PHE 468 468 468 PHE PHE B . n 
B 1 469 ARG 469 469 469 ARG ARG B . n 
B 1 470 SER 470 470 470 SER SER B . n 
B 1 471 PHE 471 471 471 PHE PHE B . n 
B 1 472 VAL 472 472 472 VAL VAL B . n 
B 1 473 ARG 473 473 473 ARG ARG B . n 
B 1 474 ARG 474 474 474 ARG ARG B . n 
B 1 475 ALA 475 475 475 ALA ALA B . n 
B 1 476 GLN 476 476 476 GLN GLN B . n 
B 1 477 GLU 477 477 477 GLU GLU B . n 
# 
loop_
_pdbx_branch_scheme.asym_id 
_pdbx_branch_scheme.entity_id 
_pdbx_branch_scheme.mon_id 
_pdbx_branch_scheme.num 
_pdbx_branch_scheme.pdb_asym_id 
_pdbx_branch_scheme.pdb_mon_id 
_pdbx_branch_scheme.pdb_seq_num 
_pdbx_branch_scheme.auth_asym_id 
_pdbx_branch_scheme.auth_mon_id 
_pdbx_branch_scheme.auth_seq_num 
_pdbx_branch_scheme.hetero 
C 2 GLC 1 C GLC 1 A GLC 491 n 
C 2 GLC 2 C GLC 2 A GLC 492 n 
C 2 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 
D 3 GLC 1 D GLC 1 A GLC 496 n 
D 3 GLC 2 D GLC 2 A GLC 497 n 
D 3 GLC 3 D GLC 3 A GLC 498 n 
D 3 GLC 4 D GLC 4 A GLC 499 n 
D 3 GLC 5 D GLC 5 A GLC 500 n 
D 3 GLC 6 D GLC 6 A GLC 501 n 
E 2 GLC 1 E GLC 1 B GLC 491 n 
E 2 GLC 2 E GLC 2 B GLC 492 n 
E 2 GLC 3 E GLC 3 B GLC 493 n 
E 2 GLC 4 E GLC 4 B GLC 494 n 
E 2 GLC 5 E GLC 5 B GLC 495 n 
F 3 GLC 1 F GLC 1 B GLC 496 n 
F 3 GLC 2 F GLC 2 B GLC 497 n 
F 3 GLC 3 F GLC 3 B GLC 498 n 
F 3 GLC 4 F GLC 4 B GLC 499 n 
F 3 GLC 5 F GLC 5 B GLC 500 n 
F 3 GLC 6 F GLC 6 B GLC 501 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 
G 4 HOH 1   501 134 HOH HOH A . 
G 4 HOH 2   502 524 HOH HOH A . 
G 4 HOH 3   503 346 HOH HOH A . 
G 4 HOH 4   504 280 HOH HOH A . 
G 4 HOH 5   505 479 HOH HOH A . 
G 4 HOH 6   506 398 HOH HOH A . 
G 4 HOH 7   507 377 HOH HOH A . 
G 4 HOH 8   508 283 HOH HOH A . 
G 4 HOH 9   509 105 HOH HOH A . 
G 4 HOH 10  510 414 HOH HOH A . 
G 4 HOH 11  511 270 HOH HOH A . 
G 4 HOH 12  512 580 HOH HOH A . 
G 4 HOH 13  513 247 HOH HOH A . 
G 4 HOH 14  514 394 HOH HOH A . 
G 4 HOH 15  515 562 HOH HOH A . 
G 4 HOH 16  516 151 HOH HOH A . 
G 4 HOH 17  517 316 HOH HOH A . 
G 4 HOH 18  518 371 HOH HOH A . 
G 4 HOH 19  519 282 HOH HOH A . 
G 4 HOH 20  520 427 HOH HOH A . 
G 4 HOH 21  521 222 HOH HOH A . 
G 4 HOH 22  522 37  HOH HOH A . 
G 4 HOH 23  523 140 HOH HOH A . 
G 4 HOH 24  524 152 HOH HOH A . 
G 4 HOH 25  525 328 HOH HOH A . 
G 4 HOH 26  526 326 HOH HOH A . 
G 4 HOH 27  527 155 HOH HOH A . 
G 4 HOH 28  528 324 HOH HOH A . 
G 4 HOH 29  529 276 HOH HOH A . 
G 4 HOH 30  530 57  HOH HOH A . 
G 4 HOH 31  531 48  HOH HOH A . 
G 4 HOH 32  532 130 HOH HOH A . 
G 4 HOH 33  533 178 HOH HOH A . 
G 4 HOH 34  534 481 HOH HOH A . 
G 4 HOH 35  535 207 HOH HOH A . 
G 4 HOH 36  536 341 HOH HOH A . 
G 4 HOH 37  537 196 HOH HOH A . 
G 4 HOH 38  538 172 HOH HOH A . 
G 4 HOH 39  539 127 HOH HOH A . 
G 4 HOH 40  540 255 HOH HOH A . 
G 4 HOH 41  541 552 HOH HOH A . 
G 4 HOH 42  542 167 HOH HOH A . 
G 4 HOH 43  543 42  HOH HOH A . 
G 4 HOH 44  544 553 HOH HOH A . 
G 4 HOH 45  545 162 HOH HOH A . 
G 4 HOH 46  546 16  HOH HOH A . 
G 4 HOH 47  547 250 HOH HOH A . 
G 4 HOH 48  548 426 HOH HOH A . 
G 4 HOH 49  549 390 HOH HOH A . 
G 4 HOH 50  550 198 HOH HOH A . 
G 4 HOH 51  551 471 HOH HOH A . 
G 4 HOH 52  552 43  HOH HOH A . 
G 4 HOH 53  553 415 HOH HOH A . 
G 4 HOH 54  554 77  HOH HOH A . 
G 4 HOH 55  555 467 HOH HOH A . 
G 4 HOH 56  556 228 HOH HOH A . 
G 4 HOH 57  557 80  HOH HOH A . 
G 4 HOH 58  558 463 HOH HOH A . 
G 4 HOH 59  559 75  HOH HOH A . 
G 4 HOH 60  560 204 HOH HOH A . 
G 4 HOH 61  561 475 HOH HOH A . 
G 4 HOH 62  562 10  HOH HOH A . 
G 4 HOH 63  563 153 HOH HOH A . 
G 4 HOH 64  564 438 HOH HOH A . 
G 4 HOH 65  565 56  HOH HOH A . 
G 4 HOH 66  566 437 HOH HOH A . 
G 4 HOH 67  567 107 HOH HOH A . 
G 4 HOH 68  568 271 HOH HOH A . 
G 4 HOH 69  569 125 HOH HOH A . 
G 4 HOH 70  570 47  HOH HOH A . 
G 4 HOH 71  571 428 HOH HOH A . 
G 4 HOH 72  572 321 HOH HOH A . 
G 4 HOH 73  573 12  HOH HOH A . 
G 4 HOH 74  574 78  HOH HOH A . 
G 4 HOH 75  575 106 HOH HOH A . 
G 4 HOH 76  576 302 HOH HOH A . 
G 4 HOH 77  577 120 HOH HOH A . 
G 4 HOH 78  578 245 HOH HOH A . 
G 4 HOH 79  579 356 HOH HOH A . 
G 4 HOH 80  580 18  HOH HOH A . 
G 4 HOH 81  581 254 HOH HOH A . 
G 4 HOH 82  582 220 HOH HOH A . 
G 4 HOH 83  583 112 HOH HOH A . 
G 4 HOH 84  584 36  HOH HOH A . 
G 4 HOH 85  585 25  HOH HOH A . 
G 4 HOH 86  586 69  HOH HOH A . 
G 4 HOH 87  587 315 HOH HOH A . 
G 4 HOH 88  588 1   HOH HOH A . 
G 4 HOH 89  589 320 HOH HOH A . 
G 4 HOH 90  590 229 HOH HOH A . 
G 4 HOH 91  591 452 HOH HOH A . 
G 4 HOH 92  592 495 HOH HOH A . 
G 4 HOH 93  593 332 HOH HOH A . 
G 4 HOH 94  594 65  HOH HOH A . 
G 4 HOH 95  595 338 HOH HOH A . 
G 4 HOH 96  596 113 HOH HOH A . 
G 4 HOH 97  597 157 HOH HOH A . 
G 4 HOH 98  598 29  HOH HOH A . 
G 4 HOH 99  599 335 HOH HOH A . 
G 4 HOH 100 600 27  HOH HOH A . 
G 4 HOH 101 601 135 HOH HOH A . 
G 4 HOH 102 602 238 HOH HOH A . 
G 4 HOH 103 603 171 HOH HOH A . 
G 4 HOH 104 604 544 HOH HOH A . 
G 4 HOH 105 605 121 HOH HOH A . 
G 4 HOH 106 606 8   HOH HOH A . 
G 4 HOH 107 607 26  HOH HOH A . 
G 4 HOH 108 608 55  HOH HOH A . 
G 4 HOH 109 609 126 HOH HOH A . 
G 4 HOH 110 610 32  HOH HOH A . 
G 4 HOH 111 611 6   HOH HOH A . 
G 4 HOH 112 612 430 HOH HOH A . 
G 4 HOH 113 613 160 HOH HOH A . 
G 4 HOH 114 614 28  HOH HOH A . 
G 4 HOH 115 615 349 HOH HOH A . 
G 4 HOH 116 616 417 HOH HOH A . 
G 4 HOH 117 617 35  HOH HOH A . 
G 4 HOH 118 618 361 HOH HOH A . 
G 4 HOH 119 619 298 HOH HOH A . 
G 4 HOH 120 620 38  HOH HOH A . 
G 4 HOH 121 621 54  HOH HOH A . 
G 4 HOH 122 622 84  HOH HOH A . 
G 4 HOH 123 623 129 HOH HOH A . 
G 4 HOH 124 624 73  HOH HOH A . 
G 4 HOH 125 625 462 HOH HOH A . 
G 4 HOH 126 626 138 HOH HOH A . 
G 4 HOH 127 627 94  HOH HOH A . 
G 4 HOH 128 628 334 HOH HOH A . 
G 4 HOH 129 629 192 HOH HOH A . 
G 4 HOH 130 630 411 HOH HOH A . 
G 4 HOH 131 631 239 HOH HOH A . 
G 4 HOH 132 632 201 HOH HOH A . 
G 4 HOH 133 633 40  HOH HOH A . 
G 4 HOH 134 634 82  HOH HOH A . 
G 4 HOH 135 635 195 HOH HOH A . 
G 4 HOH 136 636 221 HOH HOH A . 
G 4 HOH 137 637 523 HOH HOH A . 
G 4 HOH 138 638 354 HOH HOH A . 
G 4 HOH 139 639 70  HOH HOH A . 
G 4 HOH 140 640 24  HOH HOH A . 
G 4 HOH 141 641 506 HOH HOH A . 
G 4 HOH 142 642 509 HOH HOH A . 
G 4 HOH 143 643 190 HOH HOH A . 
G 4 HOH 144 644 231 HOH HOH A . 
G 4 HOH 145 645 382 HOH HOH A . 
G 4 HOH 146 646 297 HOH HOH A . 
G 4 HOH 147 647 253 HOH HOH A . 
G 4 HOH 148 648 401 HOH HOH A . 
G 4 HOH 149 649 318 HOH HOH A . 
G 4 HOH 150 650 364 HOH HOH A . 
G 4 HOH 151 651 177 HOH HOH A . 
G 4 HOH 152 652 30  HOH HOH A . 
G 4 HOH 153 653 357 HOH HOH A . 
G 4 HOH 154 654 72  HOH HOH A . 
G 4 HOH 155 655 202 HOH HOH A . 
G 4 HOH 156 656 469 HOH HOH A . 
G 4 HOH 157 657 359 HOH HOH A . 
G 4 HOH 158 658 44  HOH HOH A . 
G 4 HOH 159 659 67  HOH HOH A . 
G 4 HOH 160 660 9   HOH HOH A . 
G 4 HOH 161 661 33  HOH HOH A . 
G 4 HOH 162 662 266 HOH HOH A . 
G 4 HOH 163 663 174 HOH HOH A . 
G 4 HOH 164 664 114 HOH HOH A . 
G 4 HOH 165 665 154 HOH HOH A . 
G 4 HOH 166 666 149 HOH HOH A . 
G 4 HOH 167 667 478 HOH HOH A . 
G 4 HOH 168 668 143 HOH HOH A . 
G 4 HOH 169 669 277 HOH HOH A . 
G 4 HOH 170 670 208 HOH HOH A . 
G 4 HOH 171 671 197 HOH HOH A . 
G 4 HOH 172 672 480 HOH HOH A . 
G 4 HOH 173 673 419 HOH HOH A . 
G 4 HOH 174 674 58  HOH HOH A . 
G 4 HOH 175 675 402 HOH HOH A . 
G 4 HOH 176 676 200 HOH HOH A . 
G 4 HOH 177 677 224 HOH HOH A . 
G 4 HOH 178 678 182 HOH HOH A . 
G 4 HOH 179 679 133 HOH HOH A . 
G 4 HOH 180 680 294 HOH HOH A . 
G 4 HOH 181 681 358 HOH HOH A . 
G 4 HOH 182 682 3   HOH HOH A . 
G 4 HOH 183 683 128 HOH HOH A . 
G 4 HOH 184 684 137 HOH HOH A . 
G 4 HOH 185 685 570 HOH HOH A . 
G 4 HOH 186 686 278 HOH HOH A . 
G 4 HOH 187 687 169 HOH HOH A . 
G 4 HOH 188 688 299 HOH HOH A . 
G 4 HOH 189 689 21  HOH HOH A . 
G 4 HOH 190 690 193 HOH HOH A . 
G 4 HOH 191 691 223 HOH HOH A . 
G 4 HOH 192 692 409 HOH HOH A . 
G 4 HOH 193 693 123 HOH HOH A . 
G 4 HOH 194 694 241 HOH HOH A . 
G 4 HOH 195 695 179 HOH HOH A . 
G 4 HOH 196 696 248 HOH HOH A . 
G 4 HOH 197 697 60  HOH HOH A . 
G 4 HOH 198 698 4   HOH HOH A . 
G 4 HOH 199 699 89  HOH HOH A . 
G 4 HOH 200 700 369 HOH HOH A . 
G 4 HOH 201 701 117 HOH HOH A . 
G 4 HOH 202 702 13  HOH HOH A . 
G 4 HOH 203 703 392 HOH HOH A . 
G 4 HOH 204 704 161 HOH HOH A . 
G 4 HOH 205 705 232 HOH HOH A . 
G 4 HOH 206 706 441 HOH HOH A . 
G 4 HOH 207 707 307 HOH HOH A . 
G 4 HOH 208 708 273 HOH HOH A . 
G 4 HOH 209 709 533 HOH HOH A . 
G 4 HOH 210 710 587 HOH HOH A . 
G 4 HOH 211 711 540 HOH HOH A . 
G 4 HOH 212 712 343 HOH HOH A . 
G 4 HOH 213 713 586 HOH HOH A . 
G 4 HOH 214 714 150 HOH HOH A . 
G 4 HOH 215 715 15  HOH HOH A . 
G 4 HOH 216 716 237 HOH HOH A . 
G 4 HOH 217 717 115 HOH HOH A . 
G 4 HOH 218 718 408 HOH HOH A . 
G 4 HOH 219 719 279 HOH HOH A . 
G 4 HOH 220 720 472 HOH HOH A . 
G 4 HOH 221 721 118 HOH HOH A . 
G 4 HOH 222 722 404 HOH HOH A . 
G 4 HOH 223 723 261 HOH HOH A . 
G 4 HOH 224 724 34  HOH HOH A . 
G 4 HOH 225 725 194 HOH HOH A . 
G 4 HOH 226 726 109 HOH HOH A . 
G 4 HOH 227 727 412 HOH HOH A . 
G 4 HOH 228 728 242 HOH HOH A . 
G 4 HOH 229 729 213 HOH HOH A . 
G 4 HOH 230 730 146 HOH HOH A . 
G 4 HOH 231 731 319 HOH HOH A . 
G 4 HOH 232 732 240 HOH HOH A . 
G 4 HOH 233 733 337 HOH HOH A . 
G 4 HOH 234 734 407 HOH HOH A . 
G 4 HOH 235 735 532 HOH HOH A . 
G 4 HOH 236 736 300 HOH HOH A . 
G 4 HOH 237 737 536 HOH HOH A . 
G 4 HOH 238 738 559 HOH HOH A . 
G 4 HOH 239 739 191 HOH HOH A . 
G 4 HOH 240 740 216 HOH HOH A . 
G 4 HOH 241 741 170 HOH HOH A . 
G 4 HOH 242 742 131 HOH HOH A . 
G 4 HOH 243 743 314 HOH HOH A . 
G 4 HOH 244 744 50  HOH HOH A . 
G 4 HOH 245 745 303 HOH HOH A . 
G 4 HOH 246 746 83  HOH HOH A . 
G 4 HOH 247 747 405 HOH HOH A . 
G 4 HOH 248 748 497 HOH HOH A . 
G 4 HOH 249 749 515 HOH HOH A . 
G 4 HOH 250 750 366 HOH HOH A . 
G 4 HOH 251 751 293 HOH HOH A . 
G 4 HOH 252 752 494 HOH HOH A . 
G 4 HOH 253 753 488 HOH HOH A . 
G 4 HOH 254 754 365 HOH HOH A . 
G 4 HOH 255 755 569 HOH HOH A . 
G 4 HOH 256 756 489 HOH HOH A . 
G 4 HOH 257 757 313 HOH HOH A . 
G 4 HOH 258 758 212 HOH HOH A . 
G 4 HOH 259 759 508 HOH HOH A . 
G 4 HOH 260 760 264 HOH HOH A . 
G 4 HOH 261 761 510 HOH HOH A . 
G 4 HOH 262 762 445 HOH HOH A . 
G 4 HOH 263 763 423 HOH HOH A . 
G 4 HOH 264 764 448 HOH HOH A . 
G 4 HOH 265 765 265 HOH HOH A . 
G 4 HOH 266 766 499 HOH HOH A . 
G 4 HOH 267 767 468 HOH HOH A . 
G 4 HOH 268 768 124 HOH HOH A . 
G 4 HOH 269 769 74  HOH HOH A . 
G 4 HOH 270 770 518 HOH HOH A . 
G 4 HOH 271 771 378 HOH HOH A . 
G 4 HOH 272 772 389 HOH HOH A . 
G 4 HOH 273 773 548 HOH HOH A . 
G 4 HOH 274 774 431 HOH HOH A . 
G 4 HOH 275 775 388 HOH HOH A . 
G 4 HOH 276 776 268 HOH HOH A . 
G 4 HOH 277 777 519 HOH HOH A . 
G 4 HOH 278 778 492 HOH HOH A . 
G 4 HOH 279 779 455 HOH HOH A . 
G 4 HOH 280 780 345 HOH HOH A . 
G 4 HOH 281 781 331 HOH HOH A . 
G 4 HOH 282 782 502 HOH HOH A . 
G 4 HOH 283 783 543 HOH HOH A . 
G 4 HOH 284 784 387 HOH HOH A . 
G 4 HOH 285 785 474 HOH HOH A . 
G 4 HOH 286 786 158 HOH HOH A . 
G 4 HOH 287 787 450 HOH HOH A . 
G 4 HOH 288 788 517 HOH HOH A . 
G 4 HOH 289 789 564 HOH HOH A . 
G 4 HOH 290 790 287 HOH HOH A . 
G 4 HOH 291 791 560 HOH HOH A . 
G 4 HOH 292 792 246 HOH HOH A . 
G 4 HOH 293 793 482 HOH HOH A . 
G 4 HOH 294 794 372 HOH HOH A . 
G 4 HOH 295 795 575 HOH HOH A . 
G 4 HOH 296 796 122 HOH HOH A . 
G 4 HOH 297 797 496 HOH HOH A . 
G 4 HOH 298 798 504 HOH HOH A . 
G 4 HOH 299 799 520 HOH HOH A . 
G 4 HOH 300 800 571 HOH HOH A . 
G 4 HOH 301 801 503 HOH HOH A . 
G 4 HOH 302 802 234 HOH HOH A . 
G 4 HOH 303 803 99  HOH HOH A . 
G 4 HOH 304 804 383 HOH HOH A . 
G 4 HOH 305 805 367 HOH HOH A . 
G 4 HOH 306 806 93  HOH HOH A . 
G 4 HOH 307 807 442 HOH HOH A . 
G 4 HOH 308 808 386 HOH HOH A . 
G 4 HOH 309 809 539 HOH HOH A . 
G 4 HOH 310 810 490 HOH HOH A . 
G 4 HOH 311 811 573 HOH HOH A . 
G 4 HOH 312 812 550 HOH HOH A . 
G 4 HOH 313 813 145 HOH HOH A . 
G 4 HOH 314 814 579 HOH HOH A . 
G 4 HOH 315 815 460 HOH HOH A . 
G 4 HOH 316 816 188 HOH HOH A . 
G 4 HOH 317 817 183 HOH HOH A . 
G 4 HOH 318 818 375 HOH HOH A . 
H 4 HOH 1   501 470 HOH HOH B . 
H 4 HOH 2   502 301 HOH HOH B . 
H 4 HOH 3   503 406 HOH HOH B . 
H 4 HOH 4   504 317 HOH HOH B . 
H 4 HOH 5   505 529 HOH HOH B . 
H 4 HOH 6   506 500 HOH HOH B . 
H 4 HOH 7   507 181 HOH HOH B . 
H 4 HOH 8   508 184 HOH HOH B . 
H 4 HOH 9   509 413 HOH HOH B . 
H 4 HOH 10  510 168 HOH HOH B . 
H 4 HOH 11  511 306 HOH HOH B . 
H 4 HOH 12  512 292 HOH HOH B . 
H 4 HOH 13  513 108 HOH HOH B . 
H 4 HOH 14  514 110 HOH HOH B . 
H 4 HOH 15  515 512 HOH HOH B . 
H 4 HOH 16  516 584 HOH HOH B . 
H 4 HOH 17  517 267 HOH HOH B . 
H 4 HOH 18  518 403 HOH HOH B . 
H 4 HOH 19  519 432 HOH HOH B . 
H 4 HOH 20  520 225 HOH HOH B . 
H 4 HOH 21  521 464 HOH HOH B . 
H 4 HOH 22  522 534 HOH HOH B . 
H 4 HOH 23  523 274 HOH HOH B . 
H 4 HOH 24  524 230 HOH HOH B . 
H 4 HOH 25  525 501 HOH HOH B . 
H 4 HOH 26  526 81  HOH HOH B . 
H 4 HOH 27  527 421 HOH HOH B . 
H 4 HOH 28  528 582 HOH HOH B . 
H 4 HOH 29  529 304 HOH HOH B . 
H 4 HOH 30  530 226 HOH HOH B . 
H 4 HOH 31  531 19  HOH HOH B . 
H 4 HOH 32  532 288 HOH HOH B . 
H 4 HOH 33  533 59  HOH HOH B . 
H 4 HOH 34  534 360 HOH HOH B . 
H 4 HOH 35  535 218 HOH HOH B . 
H 4 HOH 36  536 583 HOH HOH B . 
H 4 HOH 37  537 132 HOH HOH B . 
H 4 HOH 38  538 454 HOH HOH B . 
H 4 HOH 39  539 487 HOH HOH B . 
H 4 HOH 40  540 381 HOH HOH B . 
H 4 HOH 41  541 244 HOH HOH B . 
H 4 HOH 42  542 546 HOH HOH B . 
H 4 HOH 43  543 41  HOH HOH B . 
H 4 HOH 44  544 541 HOH HOH B . 
H 4 HOH 45  545 71  HOH HOH B . 
H 4 HOH 46  546 344 HOH HOH B . 
H 4 HOH 47  547 76  HOH HOH B . 
H 4 HOH 48  548 351 HOH HOH B . 
H 4 HOH 49  549 339 HOH HOH B . 
H 4 HOH 50  550 236 HOH HOH B . 
H 4 HOH 51  551 111 HOH HOH B . 
H 4 HOH 52  552 7   HOH HOH B . 
H 4 HOH 53  553 581 HOH HOH B . 
H 4 HOH 54  554 555 HOH HOH B . 
H 4 HOH 55  555 166 HOH HOH B . 
H 4 HOH 56  556 391 HOH HOH B . 
H 4 HOH 57  557 90  HOH HOH B . 
H 4 HOH 58  558 275 HOH HOH B . 
H 4 HOH 59  559 14  HOH HOH B . 
H 4 HOH 60  560 148 HOH HOH B . 
H 4 HOH 61  561 187 HOH HOH B . 
H 4 HOH 62  562 384 HOH HOH B . 
H 4 HOH 63  563 102 HOH HOH B . 
H 4 HOH 64  564 211 HOH HOH B . 
H 4 HOH 65  565 46  HOH HOH B . 
H 4 HOH 66  566 466 HOH HOH B . 
H 4 HOH 67  567 281 HOH HOH B . 
H 4 HOH 68  568 23  HOH HOH B . 
H 4 HOH 69  569 542 HOH HOH B . 
H 4 HOH 70  570 98  HOH HOH B . 
H 4 HOH 71  571 340 HOH HOH B . 
H 4 HOH 72  572 64  HOH HOH B . 
H 4 HOH 73  573 96  HOH HOH B . 
H 4 HOH 74  574 45  HOH HOH B . 
H 4 HOH 75  575 249 HOH HOH B . 
H 4 HOH 76  576 61  HOH HOH B . 
H 4 HOH 77  577 147 HOH HOH B . 
H 4 HOH 78  578 88  HOH HOH B . 
H 4 HOH 79  579 424 HOH HOH B . 
H 4 HOH 80  580 199 HOH HOH B . 
H 4 HOH 81  581 568 HOH HOH B . 
H 4 HOH 82  582 511 HOH HOH B . 
H 4 HOH 83  583 355 HOH HOH B . 
H 4 HOH 84  584 309 HOH HOH B . 
H 4 HOH 85  585 585 HOH HOH B . 
H 4 HOH 86  586 233 HOH HOH B . 
H 4 HOH 87  587 567 HOH HOH B . 
H 4 HOH 88  588 327 HOH HOH B . 
H 4 HOH 89  589 217 HOH HOH B . 
H 4 HOH 90  590 243 HOH HOH B . 
H 4 HOH 91  591 51  HOH HOH B . 
H 4 HOH 92  592 39  HOH HOH B . 
H 4 HOH 93  593 348 HOH HOH B . 
H 4 HOH 94  594 68  HOH HOH B . 
H 4 HOH 95  595 164 HOH HOH B . 
H 4 HOH 96  596 574 HOH HOH B . 
H 4 HOH 97  597 439 HOH HOH B . 
H 4 HOH 98  598 336 HOH HOH B . 
H 4 HOH 99  599 513 HOH HOH B . 
H 4 HOH 100 600 119 HOH HOH B . 
H 4 HOH 101 601 262 HOH HOH B . 
H 4 HOH 102 602 322 HOH HOH B . 
H 4 HOH 103 603 206 HOH HOH B . 
H 4 HOH 104 604 214 HOH HOH B . 
H 4 HOH 105 605 31  HOH HOH B . 
H 4 HOH 106 606 456 HOH HOH B . 
H 4 HOH 107 607 310 HOH HOH B . 
H 4 HOH 108 608 449 HOH HOH B . 
H 4 HOH 109 609 91  HOH HOH B . 
H 4 HOH 110 610 219 HOH HOH B . 
H 4 HOH 111 611 535 HOH HOH B . 
H 4 HOH 112 612 52  HOH HOH B . 
H 4 HOH 113 613 252 HOH HOH B . 
H 4 HOH 114 614 235 HOH HOH B . 
H 4 HOH 115 615 209 HOH HOH B . 
H 4 HOH 116 616 66  HOH HOH B . 
H 4 HOH 117 617 22  HOH HOH B . 
H 4 HOH 118 618 370 HOH HOH B . 
H 4 HOH 119 619 210 HOH HOH B . 
H 4 HOH 120 620 443 HOH HOH B . 
H 4 HOH 121 621 5   HOH HOH B . 
H 4 HOH 122 622 86  HOH HOH B . 
H 4 HOH 123 623 572 HOH HOH B . 
H 4 HOH 124 624 227 HOH HOH B . 
H 4 HOH 125 625 176 HOH HOH B . 
H 4 HOH 126 626 136 HOH HOH B . 
H 4 HOH 127 627 269 HOH HOH B . 
H 4 HOH 128 628 103 HOH HOH B . 
H 4 HOH 129 629 95  HOH HOH B . 
H 4 HOH 130 630 289 HOH HOH B . 
H 4 HOH 131 631 373 HOH HOH B . 
H 4 HOH 132 632 101 HOH HOH B . 
H 4 HOH 133 633 97  HOH HOH B . 
H 4 HOH 134 634 62  HOH HOH B . 
H 4 HOH 135 635 526 HOH HOH B . 
H 4 HOH 136 636 49  HOH HOH B . 
H 4 HOH 137 637 116 HOH HOH B . 
H 4 HOH 138 638 473 HOH HOH B . 
H 4 HOH 139 639 436 HOH HOH B . 
H 4 HOH 140 640 353 HOH HOH B . 
H 4 HOH 141 641 521 HOH HOH B . 
H 4 HOH 142 642 20  HOH HOH B . 
H 4 HOH 143 643 291 HOH HOH B . 
H 4 HOH 144 644 141 HOH HOH B . 
H 4 HOH 145 645 507 HOH HOH B . 
H 4 HOH 146 646 159 HOH HOH B . 
H 4 HOH 147 647 551 HOH HOH B . 
H 4 HOH 148 648 251 HOH HOH B . 
H 4 HOH 149 649 104 HOH HOH B . 
H 4 HOH 150 650 165 HOH HOH B . 
H 4 HOH 151 651 362 HOH HOH B . 
H 4 HOH 152 652 175 HOH HOH B . 
H 4 HOH 153 653 203 HOH HOH B . 
H 4 HOH 154 654 2   HOH HOH B . 
H 4 HOH 155 655 563 HOH HOH B . 
H 4 HOH 156 656 11  HOH HOH B . 
H 4 HOH 157 657 458 HOH HOH B . 
H 4 HOH 158 658 215 HOH HOH B . 
H 4 HOH 159 659 189 HOH HOH B . 
H 4 HOH 160 660 435 HOH HOH B . 
H 4 HOH 161 661 63  HOH HOH B . 
H 4 HOH 162 662 53  HOH HOH B . 
H 4 HOH 163 663 418 HOH HOH B . 
H 4 HOH 164 664 85  HOH HOH B . 
H 4 HOH 165 665 284 HOH HOH B . 
H 4 HOH 166 666 173 HOH HOH B . 
H 4 HOH 167 667 531 HOH HOH B . 
H 4 HOH 168 668 399 HOH HOH B . 
H 4 HOH 169 669 258 HOH HOH B . 
H 4 HOH 170 670 395 HOH HOH B . 
H 4 HOH 171 671 379 HOH HOH B . 
H 4 HOH 172 672 374 HOH HOH B . 
H 4 HOH 173 673 180 HOH HOH B . 
H 4 HOH 174 674 329 HOH HOH B . 
H 4 HOH 175 675 285 HOH HOH B . 
H 4 HOH 176 676 290 HOH HOH B . 
H 4 HOH 177 677 263 HOH HOH B . 
H 4 HOH 178 678 491 HOH HOH B . 
H 4 HOH 179 679 142 HOH HOH B . 
H 4 HOH 180 680 538 HOH HOH B . 
H 4 HOH 181 681 465 HOH HOH B . 
H 4 HOH 182 682 400 HOH HOH B . 
H 4 HOH 183 683 272 HOH HOH B . 
H 4 HOH 184 684 92  HOH HOH B . 
H 4 HOH 185 685 323 HOH HOH B . 
H 4 HOH 186 686 416 HOH HOH B . 
H 4 HOH 187 687 259 HOH HOH B . 
H 4 HOH 188 688 350 HOH HOH B . 
H 4 HOH 189 689 186 HOH HOH B . 
H 4 HOH 190 690 312 HOH HOH B . 
H 4 HOH 191 691 144 HOH HOH B . 
H 4 HOH 192 692 17  HOH HOH B . 
H 4 HOH 193 693 498 HOH HOH B . 
H 4 HOH 194 694 420 HOH HOH B . 
H 4 HOH 195 695 410 HOH HOH B . 
H 4 HOH 196 696 380 HOH HOH B . 
H 4 HOH 197 697 433 HOH HOH B . 
H 4 HOH 198 698 185 HOH HOH B . 
H 4 HOH 199 699 363 HOH HOH B . 
H 4 HOH 200 700 330 HOH HOH B . 
H 4 HOH 201 701 308 HOH HOH B . 
H 4 HOH 202 702 368 HOH HOH B . 
H 4 HOH 203 703 100 HOH HOH B . 
H 4 HOH 204 704 549 HOH HOH B . 
H 4 HOH 205 705 396 HOH HOH B . 
H 4 HOH 206 706 446 HOH HOH B . 
H 4 HOH 207 707 577 HOH HOH B . 
H 4 HOH 208 708 296 HOH HOH B . 
H 4 HOH 209 709 325 HOH HOH B . 
H 4 HOH 210 710 561 HOH HOH B . 
H 4 HOH 211 711 79  HOH HOH B . 
H 4 HOH 212 712 528 HOH HOH B . 
H 4 HOH 213 713 451 HOH HOH B . 
H 4 HOH 214 714 516 HOH HOH B . 
H 4 HOH 215 715 576 HOH HOH B . 
H 4 HOH 216 716 257 HOH HOH B . 
H 4 HOH 217 717 556 HOH HOH B . 
H 4 HOH 218 718 483 HOH HOH B . 
H 4 HOH 219 719 347 HOH HOH B . 
H 4 HOH 220 720 163 HOH HOH B . 
H 4 HOH 221 721 425 HOH HOH B . 
H 4 HOH 222 722 376 HOH HOH B . 
H 4 HOH 223 723 493 HOH HOH B . 
H 4 HOH 224 724 527 HOH HOH B . 
H 4 HOH 225 725 256 HOH HOH B . 
H 4 HOH 226 726 397 HOH HOH B . 
H 4 HOH 227 727 530 HOH HOH B . 
H 4 HOH 228 728 565 HOH HOH B . 
H 4 HOH 229 729 477 HOH HOH B . 
H 4 HOH 230 730 554 HOH HOH B . 
H 4 HOH 231 731 429 HOH HOH B . 
H 4 HOH 232 732 459 HOH HOH B . 
H 4 HOH 233 733 486 HOH HOH B . 
H 4 HOH 234 734 505 HOH HOH B . 
H 4 HOH 235 735 422 HOH HOH B . 
H 4 HOH 236 736 525 HOH HOH B . 
H 4 HOH 237 737 453 HOH HOH B . 
H 4 HOH 238 738 87  HOH HOH B . 
H 4 HOH 239 739 444 HOH HOH B . 
H 4 HOH 240 740 476 HOH HOH B . 
H 4 HOH 241 741 305 HOH HOH B . 
H 4 HOH 242 742 545 HOH HOH B . 
H 4 HOH 243 743 260 HOH HOH B . 
H 4 HOH 244 744 352 HOH HOH B . 
H 4 HOH 245 745 522 HOH HOH B . 
H 4 HOH 246 746 558 HOH HOH B . 
H 4 HOH 247 747 440 HOH HOH B . 
H 4 HOH 248 748 139 HOH HOH B . 
H 4 HOH 249 749 333 HOH HOH B . 
H 4 HOH 250 750 461 HOH HOH B . 
H 4 HOH 251 751 484 HOH HOH B . 
H 4 HOH 252 752 447 HOH HOH B . 
H 4 HOH 253 753 537 HOH HOH B . 
H 4 HOH 254 754 547 HOH HOH B . 
H 4 HOH 255 755 385 HOH HOH B . 
H 4 HOH 256 756 311 HOH HOH B . 
H 4 HOH 257 757 578 HOH HOH B . 
H 4 HOH 258 758 295 HOH HOH B . 
H 4 HOH 259 759 434 HOH HOH B . 
H 4 HOH 260 760 286 HOH HOH B . 
H 4 HOH 261 761 156 HOH HOH B . 
H 4 HOH 262 762 557 HOH HOH B . 
H 4 HOH 263 763 393 HOH HOH B . 
H 4 HOH 264 764 342 HOH HOH B . 
H 4 HOH 265 765 514 HOH HOH B . 
H 4 HOH 266 766 457 HOH HOH B . 
H 4 HOH 267 767 205 HOH HOH B . 
H 4 HOH 268 768 485 HOH HOH B . 
H 4 HOH 269 769 566 HOH HOH B . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? '(1.13_2998: ???)' 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .                  2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .                  3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? .                  4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   95.99 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9K7D 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     61.420 
_cell.length_a_esd                 ? 
_cell.length_b                     40.790 
_cell.length_b_esd                 ? 
_cell.length_c                     196.760 
_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                         9K7D 
_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                   9K7D 
_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             2.08 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          40.75 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.1M Sodium citrate, pH 4.2, 20% PEG 3350' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            338 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 9M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2024-10-17 
_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 BL02U1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97918 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL02U1 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9K7D 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.72 
_reflns.d_resolution_low                               39.14 
_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                                     104038 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           100.0 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.7 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          10.1 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               0.94 
_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                                0.217 
_reflns.pdbx_Rpim_I_all                                0.085 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       696967 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.993 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.200 
_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                                    1.72 
_reflns_shell.d_res_low                                     1.76 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           52608 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             7655 
_reflns_shell.percent_possible_obs                          100.0 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               6.9 
_reflns_shell.pdbx_chi_squared                              0.91 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     1.5 
_reflns_shell.pdbx_Rrim_I_all                               1.457 
_reflns_shell.pdbx_Rpim_I_all                               0.549 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.567 
_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                                  1.348 
_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                                 9K7D 
_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                            1.720 
_refine.ls_d_res_low                             39.137 
_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                     104016 
_refine.ls_number_reflns_R_free                  5147 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.92 
_refine.ls_percent_reflns_R_free                 4.95 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1746 
_refine.ls_R_factor_R_free                       0.2127 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1726 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.34 
_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                 21.35 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.20 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.720 
_refine_hist.d_res_low                        39.137 
_refine_hist.number_atoms_solvent             587 
_refine_hist.number_atoms_total               8921 
_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        8334 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         0 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.008 ? 8596  ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.018 ? 11664 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 4.141 ? 7188  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.076 ? 1280  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.006 ? 1428  ? 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' 1.7200 1.7396 . . 175 3231 100.00 . . . . 0.2531 . . . . . . . . . . . 0.3045 
'X-RAY DIFFRACTION' 1.7396 1.7600 . . 150 3380 100.00 . . . . 0.2600 . . . . . . . . . . . 0.3127 
'X-RAY DIFFRACTION' 1.7600 1.7815 . . 163 3213 100.00 . . . . 0.2488 . . . . . . . . . . . 0.3186 
'X-RAY DIFFRACTION' 1.7815 1.8040 . . 163 3285 100.00 . . . . 0.2713 . . . . . . . . . . . 0.2992 
'X-RAY DIFFRACTION' 1.8040 1.8278 . . 176 3239 100.00 . . . . 0.2577 . . . . . . . . . . . 0.3270 
'X-RAY DIFFRACTION' 1.8278 1.8528 . . 196 3327 100.00 . . . . 0.2345 . . . . . . . . . . . 0.2897 
'X-RAY DIFFRACTION' 1.8528 1.8793 . . 180 3173 100.00 . . . . 0.2225 . . . . . . . . . . . 0.2626 
'X-RAY DIFFRACTION' 1.8793 1.9073 . . 161 3250 100.00 . . . . 0.1970 . . . . . . . . . . . 0.2493 
'X-RAY DIFFRACTION' 1.9073 1.9371 . . 185 3343 100.00 . . . . 0.2071 . . . . . . . . . . . 0.2477 
'X-RAY DIFFRACTION' 1.9371 1.9689 . . 165 3230 100.00 . . . . 0.1984 . . . . . . . . . . . 0.2621 
'X-RAY DIFFRACTION' 1.9689 2.0029 . . 177 3266 100.00 . . . . 0.2008 . . . . . . . . . . . 0.2438 
'X-RAY DIFFRACTION' 2.0029 2.0393 . . 187 3303 100.00 . . . . 0.1907 . . . . . . . . . . . 0.2464 
'X-RAY DIFFRACTION' 2.0393 2.0785 . . 166 3210 100.00 . . . . 0.1886 . . . . . . . . . . . 0.2524 
'X-RAY DIFFRACTION' 2.0785 2.1209 . . 177 3329 100.00 . . . . 0.1896 . . . . . . . . . . . 0.2646 
'X-RAY DIFFRACTION' 2.1209 2.1670 . . 203 3265 100.00 . . . . 0.1806 . . . . . . . . . . . 0.2209 
'X-RAY DIFFRACTION' 2.1670 2.2174 . . 161 3230 100.00 . . . . 0.1855 . . . . . . . . . . . 0.2141 
'X-RAY DIFFRACTION' 2.2174 2.2729 . . 188 3334 100.00 . . . . 0.1733 . . . . . . . . . . . 0.2066 
'X-RAY DIFFRACTION' 2.2729 2.3343 . . 158 3189 100.00 . . . . 0.1682 . . . . . . . . . . . 0.1988 
'X-RAY DIFFRACTION' 2.3343 2.4030 . . 174 3348 100.00 . . . . 0.1752 . . . . . . . . . . . 0.2253 
'X-RAY DIFFRACTION' 2.4030 2.4806 . . 160 3299 100.00 . . . . 0.1815 . . . . . . . . . . . 0.2322 
'X-RAY DIFFRACTION' 2.4806 2.5692 . . 170 3294 100.00 . . . . 0.1763 . . . . . . . . . . . 0.2226 
'X-RAY DIFFRACTION' 2.5692 2.6720 . . 163 3302 100.00 . . . . 0.1689 . . . . . . . . . . . 0.2100 
'X-RAY DIFFRACTION' 2.6720 2.7936 . . 166 3306 100.00 . . . . 0.1665 . . . . . . . . . . . 0.2031 
'X-RAY DIFFRACTION' 2.7936 2.9409 . . 151 3369 100.00 . . . . 0.1691 . . . . . . . . . . . 0.1927 
'X-RAY DIFFRACTION' 2.9409 3.1250 . . 162 3298 100.00 . . . . 0.1626 . . . . . . . . . . . 0.2198 
'X-RAY DIFFRACTION' 3.1250 3.3662 . . 183 3305 100.00 . . . . 0.1568 . . . . . . . . . . . 0.1802 
'X-RAY DIFFRACTION' 3.3662 3.7047 . . 178 3346 100.00 . . . . 0.1435 . . . . . . . . . . . 0.1760 
'X-RAY DIFFRACTION' 3.7047 4.2403 . . 155 3327 100.00 . . . . 0.1356 . . . . . . . . . . . 0.1546 
'X-RAY DIFFRACTION' 4.2403 5.3401 . . 170 3384 100.00 . . . . 0.1350 . . . . . . . . . . . 0.1643 
'X-RAY DIFFRACTION' 5.3401 39.137 . . 184 3494 99.00  . . . . 0.1755 . . . . . . . . . . . 0.2123 
# 
_struct.entry_id                     9K7D 
_struct.title                        
'Crystal structure of GH57 family amylopullulanase from Aquifex aeolicus mutant E256Q in complex with Maltohexaose' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        9K7D 
_struct_keywords.text            'GH57, amylopullulanase, Aquifex aeolicus, HYDROLASE' 
_struct_keywords.pdbx_keywords   HYDROLASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 2 ? 
F N N 3 ? 
G N N 4 ? 
H N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    O66934_AQUAE 
_struct_ref.pdbx_db_accession          O66934 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MKKLFLVFWWHMHQPLYREPYTGEYLLPWTFFHAVKDYYDMPAYLKDFEIKLNFNLTPVLIDQIQEYAQGKAKDVFLEAI
RKDPDDLEKEEVEKLIEFTKLNYEKPIYRFERIRELMNKEKLNREELLDLQTLNLLAWCGRTLRKDLKDLLNKGRNYTQE
EKEYVLNKYFEIIKKTLSIYREIKEEGKGSVSTSPYYHPLIPILLNPNCVYETTPNVKIPDFAVSFREDASKHVELAKEK
YFEIFGEHPVYMWPPEASVSNEALELYYEKGINMLATDEVILKNSVERASPYLRYYFRELISVFFRDKTLSDLIGFSYHA
WNAEDAVRDFIGRLKKIHESVDFQPVVFVVLDGENCWEYYEENGIPFLEKLYSTLEKEEWIETLTLEEAMRKEDVKTEVI
ESVKAGTWFDGNFLKWIGNKEKNEYWKILIEAKKKAKNDYILVAEGSDWFWWQGEEKAPFVEVFDKLFRSFVRRAQE
;
_struct_ref.pdbx_align_begin           1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9K7D A 1 ? 477 ? O66934 1 ? 477 ? 1 477 
2 1 9K7D 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 9K7D GLN A 256 ? UNP O66934 GLU 256 'engineered mutation' 256 1 
2 9K7D GLN B 256 ? UNP O66934 GLU 256 'engineered mutation' 256 2 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,G 
2 1 B,E,F,H 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 PRO A 28  ? ASP A 37  ? PRO A 28  ASP A 37  1 ? 10 
HELX_P HELX_P2  AA2 TYR A 39  ? TYR A 44  ? TYR A 39  TYR A 44  1 ? 6  
HELX_P HELX_P3  AA3 LEU A 45  ? ASP A 47  ? LEU A 45  ASP A 47  5 ? 3  
HELX_P HELX_P4  AA4 THR A 57  ? GLN A 69  ? THR A 57  GLN A 69  1 ? 13 
HELX_P HELX_P5  AA5 VAL A 75  ? LYS A 82  ? VAL A 75  LYS A 82  1 ? 8  
HELX_P HELX_P6  AA6 ASP A 83  ? LEU A 87  ? ASP A 83  LEU A 87  5 ? 5  
HELX_P HELX_P7  AA7 GLU A 88  ? TYR A 103 ? GLU A 88  TYR A 103 1 ? 16 
HELX_P HELX_P8  AA8 LYS A 105 ? ARG A 109 ? LYS A 105 ARG A 109 5 ? 5  
HELX_P HELX_P9  AA9 PHE A 110 ? ASN A 118 ? PHE A 110 ASN A 118 1 ? 9  
HELX_P HELX_P10 AB1 ASN A 123 ? TRP A 138 ? ASN A 123 TRP A 138 1 ? 16 
HELX_P HELX_P11 AB2 GLY A 140 ? LEU A 147 ? GLY A 140 LEU A 147 1 ? 8  
HELX_P HELX_P12 AB3 LEU A 147 ? GLY A 154 ? LEU A 147 GLY A 154 1 ? 8  
HELX_P HELX_P13 AB4 THR A 158 ? LYS A 175 ? THR A 158 LYS A 175 1 ? 18 
HELX_P HELX_P14 AB5 LYS A 175 ? GLU A 186 ? LYS A 175 GLU A 186 1 ? 12 
HELX_P HELX_P15 AB6 LEU A 200 ? ASN A 206 ? LEU A 200 ASN A 206 1 ? 7  
HELX_P HELX_P16 AB7 PRO A 207 ? THR A 213 ? PRO A 207 THR A 213 5 ? 7  
HELX_P HELX_P17 AB8 PHE A 226 ? GLY A 246 ? PHE A 226 GLY A 246 1 ? 21 
HELX_P HELX_P18 AB9 PRO A 254 ? SER A 258 ? PRO A 254 SER A 258 5 ? 5  
HELX_P HELX_P19 AC1 SER A 260 ? LYS A 270 ? SER A 260 LYS A 270 1 ? 11 
HELX_P HELX_P20 AC2 GLU A 279 ? VAL A 286 ? GLU A 279 VAL A 286 1 ? 8  
HELX_P HELX_P21 AC3 ASP A 307 ? SER A 317 ? ASP A 307 SER A 317 1 ? 11 
HELX_P HELX_P22 AC4 TYR A 318 ? TRP A 321 ? TYR A 318 TRP A 321 5 ? 4  
HELX_P HELX_P23 AC5 ASN A 322 ? VAL A 341 ? ASN A 322 VAL A 341 1 ? 20 
HELX_P HELX_P24 AC6 CYS A 356 ? ASN A 363 ? CYS A 356 ASN A 363 5 ? 8  
HELX_P HELX_P25 AC7 GLY A 364 ? GLU A 376 ? GLY A 364 GLU A 376 1 ? 13 
HELX_P HELX_P26 AC8 THR A 385 ? LYS A 392 ? THR A 385 LYS A 392 1 ? 8  
HELX_P HELX_P27 AC9 ASN A 419 ? LYS A 435 ? ASN A 419 LYS A 435 1 ? 17 
HELX_P HELX_P28 AD1 ASP A 439 ? 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 ? MET B 117 ? PHE B 110 MET B 117 1 ? 8  
HELX_P HELX_P40 AE4 ASN B 123 ? TRP B 138 ? ASN B 123 TRP B 138 1 ? 16 
HELX_P HELX_P41 AE5 THR B 142 ? LEU B 147 ? THR B 142 LEU B 147 1 ? 6  
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 378 ? GLY B 364 GLU B 378 1 ? 15 
HELX_P HELX_P56 AG2 THR B 385 ? LYS B 392 ? THR B 385 LYS B 392 1 ? 8  
HELX_P HELX_P57 AG3 ASN B 419 ? LYS B 434 ? ASN B 419 LYS B 434 1 ? 16 
HELX_P HELX_P58 AG4 ASP B 439 ? GLU B 445 ? ASP B 439 GLU B 445 1 ? 7  
HELX_P HELX_P59 AG5 GLY B 446 ? GLN B 453 ? GLY B 446 GLN B 453 1 ? 8  
HELX_P HELX_P60 AG6 PHE B 460 ? GLN B 476 ? PHE B 460 GLN B 476 1 ? 17 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
covale1  covale both ? C GLC . O4 ? ? ? 1_555 C GLC . C1 ? ? C GLC 1 C GLC 2 1_555 ? ? ? ? ? ? ? 1.381 ? ? 
covale2  covale both ? C GLC . O4 ? ? ? 1_555 C GLC . C1 ? ? C GLC 2 C GLC 3 1_555 ? ? ? ? ? ? ? 1.461 ? ? 
covale3  covale both ? C GLC . O4 ? ? ? 1_555 C GLC . C1 ? ? C GLC 3 C GLC 4 1_555 ? ? ? ? ? ? ? 1.443 ? ? 
covale4  covale both ? C GLC . O4 ? ? ? 1_555 C GLC . C1 ? ? C GLC 4 C GLC 5 1_555 ? ? ? ? ? ? ? 1.409 ? ? 
covale5  covale both ? D GLC . O4 ? ? ? 1_555 D GLC . C1 ? ? D GLC 1 D GLC 2 1_555 ? ? ? ? ? ? ? 1.452 ? ? 
covale6  covale both ? D GLC . O4 ? ? ? 1_555 D GLC . C1 ? ? D GLC 2 D GLC 3 1_555 ? ? ? ? ? ? ? 1.439 ? ? 
covale7  covale both ? D GLC . O4 ? ? ? 1_555 D GLC . C1 ? ? D GLC 3 D GLC 4 1_555 ? ? ? ? ? ? ? 1.438 ? ? 
covale8  covale both ? D GLC . O4 ? ? ? 1_555 D GLC . C1 ? ? D GLC 4 D GLC 5 1_555 ? ? ? ? ? ? ? 1.430 ? ? 
covale9  covale both ? D GLC . O4 ? ? ? 1_555 D GLC . C1 ? ? D GLC 5 D GLC 6 1_555 ? ? ? ? ? ? ? 1.443 ? ? 
covale10 covale both ? E GLC . O4 ? ? ? 1_555 E GLC . C1 ? ? E GLC 1 E GLC 2 1_555 ? ? ? ? ? ? ? 1.389 ? ? 
covale11 covale both ? E GLC . O4 ? ? ? 1_555 E GLC . C1 ? ? E GLC 2 E GLC 3 1_555 ? ? ? ? ? ? ? 1.442 ? ? 
covale12 covale both ? E GLC . O4 ? ? ? 1_555 E GLC . C1 ? ? E GLC 3 E GLC 4 1_555 ? ? ? ? ? ? ? 1.445 ? ? 
covale13 covale both ? E GLC . O4 ? ? ? 1_555 E GLC . C1 ? ? E GLC 4 E GLC 5 1_555 ? ? ? ? ? ? ? 1.457 ? ? 
covale14 covale both ? F GLC . O4 ? ? ? 1_555 F GLC . C1 ? ? F GLC 1 F GLC 2 1_555 ? ? ? ? ? ? ? 1.455 ? ? 
covale15 covale both ? F GLC . O4 ? ? ? 1_555 F GLC . C1 ? ? F GLC 2 F GLC 3 1_555 ? ? ? ? ? ? ? 1.439 ? ? 
covale16 covale both ? F GLC . O4 ? ? ? 1_555 F GLC . C1 ? ? F GLC 3 F GLC 4 1_555 ? ? ? ? ? ? ? 1.432 ? ? 
covale17 covale both ? F GLC . O4 ? ? ? 1_555 F GLC . C1 ? ? F GLC 4 F GLC 5 1_555 ? ? ? ? ? ? ? 1.428 ? ? 
covale18 covale both ? F GLC . O4 ? ? ? 1_555 F GLC . C1 ? ? F GLC 5 F GLC 6 1_555 ? ? ? ? ? ? ? 1.446 ? ? 
# 
_struct_conn_type.id          covale 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 4 ? 
AA3 ? 2 ? 
AA4 ? 5 ? 
AA5 ? 4 ? 
AA6 ? 4 ? 
AA7 ? 2 ? 
AA8 ? 5 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? parallel      
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA2 1 2 ? parallel      
AA2 2 3 ? parallel      
AA2 3 4 ? parallel      
AA3 1 2 ? parallel      
AA4 1 2 ? parallel      
AA4 2 3 ? parallel      
AA4 3 4 ? anti-parallel 
AA4 4 5 ? parallel      
AA5 1 2 ? parallel      
AA5 2 3 ? parallel      
AA5 3 4 ? parallel      
AA6 1 2 ? parallel      
AA6 2 3 ? parallel      
AA6 3 4 ? parallel      
AA7 1 2 ? parallel      
AA8 1 2 ? parallel      
AA8 2 3 ? parallel      
AA8 3 4 ? anti-parallel 
AA8 4 5 ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 VAL A 191 ? SER A 192 ? VAL A 191 SER A 192 
AA1 2 ASN A 53  ? LEU A 56  ? ASN A 53  LEU A 56  
AA1 3 LEU A 4   ? MET A 12  ? LEU A 4   MET A 12  
AA1 4 VAL A 346 ? ASP A 352 ? VAL A 346 ASP A 352 
AA2 1 VAL A 191 ? SER A 192 ? VAL A 191 SER A 192 
AA2 2 ASN A 53  ? LEU A 56  ? ASN A 53  LEU A 56  
AA2 3 LEU A 4   ? MET A 12  ? LEU A 4   MET A 12  
AA2 4 ILE A 381 ? THR A 383 ? ILE A 381 THR A 383 
AA3 1 GLU A 24  ? TYR A 25  ? GLU A 24  TYR A 25  
AA3 2 LYS A 73  ? ASP A 74  ? LYS A 73  ASP A 74  
AA4 1 TYR A 251 ? MET A 252 ? TYR A 251 MET A 252 
AA4 2 MET A 274 ? ASP A 278 ? MET A 274 ASP A 278 
AA4 3 ILE A 301 ? ARG A 306 ? ILE A 301 ARG A 306 
AA4 4 ARG A 294 ? PHE A 297 ? ARG A 294 PHE A 297 
AA4 5 THR A 397 ? ILE A 400 ? THR A 397 ILE A 400 
AA5 1 VAL B 191 ? SER B 192 ? VAL B 191 SER B 192 
AA5 2 ASN B 53  ? LEU B 56  ? ASN B 53  LEU B 56  
AA5 3 LEU B 4   ? MET B 12  ? LEU B 4   MET B 12  
AA5 4 VAL B 346 ? ASP B 352 ? VAL B 346 ASP B 352 
AA6 1 VAL B 191 ? SER B 192 ? VAL B 191 SER B 192 
AA6 2 ASN B 53  ? LEU B 56  ? ASN B 53  LEU B 56  
AA6 3 LEU B 4   ? MET B 12  ? LEU B 4   MET B 12  
AA6 4 ILE B 381 ? THR B 383 ? ILE B 381 THR B 383 
AA7 1 GLU B 24  ? TYR B 25  ? GLU B 24  TYR B 25  
AA7 2 LYS B 73  ? ASP B 74  ? LYS B 73  ASP B 74  
AA8 1 TYR B 251 ? MET B 252 ? TYR B 251 MET B 252 
AA8 2 MET B 274 ? THR B 277 ? MET B 274 THR B 277 
AA8 3 ILE B 301 ? PHE B 305 ? ILE B 301 PHE B 305 
AA8 4 ARG B 294 ? PHE B 297 ? ARG B 294 PHE B 297 
AA8 5 THR B 397 ? ILE B 400 ? THR B 397 ILE B 400 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O SER A 192 ? O SER A 192 N PHE A 54  ? N PHE A 54  
AA1 2 3 O ASN A 53  ? O ASN A 53  N TRP A 10  ? N TRP A 10  
AA1 3 4 N PHE A 5   ? N PHE A 5   O VAL A 347 ? O VAL A 347 
AA2 1 2 O SER A 192 ? O SER A 192 N PHE A 54  ? N PHE A 54  
AA2 2 3 O ASN A 53  ? O ASN A 53  N TRP A 10  ? N TRP A 10  
AA2 3 4 N LEU A 4   ? N LEU A 4   O GLU A 382 ? O GLU A 382 
AA3 1 2 N TYR A 25  ? N TYR A 25  O LYS A 73  ? O LYS A 73  
AA4 1 2 N MET A 252 ? N MET A 252 O MET A 274 ? O MET A 274 
AA4 2 3 N THR A 277 ? N THR A 277 O ARG A 306 ? O ARG A 306 
AA4 3 4 O 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 ILE B 400 ? O ILE B 400 
# 
_pdbx_entry_details.entry_id                   9K7D 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1  1 O   B HOH 507 ? ? O B HOH 701 ? ? 1.83 
2  1 O   B HOH 608 ? ? O B HOH 744 ? ? 1.83 
3  1 O4  C GLC 5   ? ? O A HOH 815 ? ? 1.92 
4  1 O   A HOH 646 ? ? O A HOH 712 ? ? 1.92 
5  1 O   A HOH 615 ? ? O A HOH 761 ? ? 1.97 
6  1 O   A HOH 736 ? ? O A HOH 756 ? ? 1.99 
7  1 O   B HOH 703 ? ? O B HOH 713 ? ? 2.02 
8  1 O   A HOH 789 ? ? O A HOH 790 ? ? 2.02 
9  1 OD2 B ASP 149 ? ? O B HOH 501 ? ? 2.02 
10 1 O   A HOH 502 ? ? O A HOH 738 ? ? 2.03 
11 1 O   A HOH 766 ? ? O A HOH 783 ? ? 2.04 
12 1 OE1 B GLU 387 ? ? O B HOH 502 ? ? 2.05 
13 1 O   A HOH 725 ? ? O A HOH 774 ? ? 2.08 
14 1 O   B HOH 719 ? ? O B HOH 739 ? ? 2.08 
15 1 OE2 A GLU 265 ? ? O A HOH 501 ? ? 2.10 
16 1 O   A HOH 802 ? ? O A HOH 806 ? ? 2.11 
17 1 N   A LYS 2   ? ? O A HOH 502 ? ? 2.12 
18 1 ND2 A ASN 322 ? ? O A HOH 503 ? ? 2.13 
19 1 O   A HOH 764 ? ? O A HOH 767 ? ? 2.14 
20 1 NZ  B LYS 188 ? ? O B HOH 503 ? ? 2.15 
21 1 O   B HOH 611 ? ? O B HOH 693 ? ? 2.16 
22 1 O   A HOH 551 ? ? O A HOH 778 ? ? 2.16 
23 1 NZ  A LYS 145 ? ? O A HOH 504 ? ? 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 642 ? ? 1_555 O B HOH 724 ? ? 1_545 1.99 
2 1 O A HOH 561 ? ? 1_555 O B HOH 733 ? ? 1_545 2.03 
# 
_pdbx_validate_rmsd_bond.id                        1 
_pdbx_validate_rmsd_bond.PDB_model_num             1 
_pdbx_validate_rmsd_bond.auth_atom_id_1            CD 
_pdbx_validate_rmsd_bond.auth_asym_id_1            A 
_pdbx_validate_rmsd_bond.auth_comp_id_1            GLU 
_pdbx_validate_rmsd_bond.auth_seq_id_1             379 
_pdbx_validate_rmsd_bond.PDB_ins_code_1            ? 
_pdbx_validate_rmsd_bond.label_alt_id_1            ? 
_pdbx_validate_rmsd_bond.auth_atom_id_2            OE2 
_pdbx_validate_rmsd_bond.auth_asym_id_2            A 
_pdbx_validate_rmsd_bond.auth_comp_id_2            GLU 
_pdbx_validate_rmsd_bond.auth_seq_id_2             379 
_pdbx_validate_rmsd_bond.PDB_ins_code_2            ? 
_pdbx_validate_rmsd_bond.label_alt_id_2            ? 
_pdbx_validate_rmsd_bond.bond_value                1.167 
_pdbx_validate_rmsd_bond.bond_target_value         1.252 
_pdbx_validate_rmsd_bond.bond_deviation            -0.085 
_pdbx_validate_rmsd_bond.bond_standard_deviation   0.011 
_pdbx_validate_rmsd_bond.linker_flag               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 ALA A 257 ? ? 59.78   19.41   
2  1 ASP A 394 ? ? -85.88  43.51   
3  1 ASP A 410 ? ? 57.89   16.96   
4  1 PHE A 460 ? ? 69.73   -9.70   
5  1 ASN B 206 ? ? -163.88 94.83   
6  1 THR B 277 ? ? -142.59 -159.78 
7  1 ARG B 288 ? ? 25.95   74.47   
8  1 ASP B 394 ? ? -93.23  47.58   
9  1 ASP B 410 ? ? 59.48   15.75   
10 1 GLU B 456 ? ? -49.81  150.94  
11 1 PHE B 460 ? ? 70.05   -8.67   
# 
_pdbx_validate_peptide_omega.id               1 
_pdbx_validate_peptide_omega.PDB_model_num    1 
_pdbx_validate_peptide_omega.auth_comp_id_1   PRO 
_pdbx_validate_peptide_omega.auth_asym_id_1   A 
_pdbx_validate_peptide_omega.auth_seq_id_1    195 
_pdbx_validate_peptide_omega.PDB_ins_code_1   ? 
_pdbx_validate_peptide_omega.label_alt_id_1   ? 
_pdbx_validate_peptide_omega.auth_comp_id_2   TYR 
_pdbx_validate_peptide_omega.auth_asym_id_2   A 
_pdbx_validate_peptide_omega.auth_seq_id_2    196 
_pdbx_validate_peptide_omega.PDB_ins_code_2   ? 
_pdbx_validate_peptide_omega.label_alt_id_2   ? 
_pdbx_validate_peptide_omega.omega            -149.92 
# 
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 -49.0356 42.3574 24.1526 0.1418 ? 0.0201  ? -0.0083 ? 0.2069 ? 0.0297  ? 0.2154 ? 2.0694 ? 0.0887 
? 0.1276  ? 1.5252 ? 0.2026  ? 3.0262 ? 0.0574  ? 0.3323  ? 0.1882  ? -0.1999 ? -0.0906 ? 0.1817  ? -0.2108 ? -0.3082 ? -0.0173 ? 
2  'X-RAY DIFFRACTION' ? refined -40.6052 36.6194 12.6566 0.1841 ? 0.0211  ? -0.0436 ? 0.2703 ? -0.0072 ? 0.1231 ? 3.5867 ? 0.3781 
? -0.0233 ? 2.1697 ? 0.0863  ? 3.2356 ? -0.0081 ? 0.5056  ? 0.0362  ? -0.2696 ? 0.0061  ? 0.0497  ? -0.1222 ? -0.0498 ? -0.0014 ? 
3  'X-RAY DIFFRACTION' ? refined -12.7166 15.6964 74.3637 0.1028 ? -0.0279 ? 0.0042  ? 0.1030 ? -0.0011 ? 0.1204 ? 1.1460 ? 
-0.0352 ? -0.3151 ? 0.3450 ? 0.0839  ? 0.7588 ? -0.0142 ? -0.0797 ? -0.0870 ? 0.0321  ? 0.0051  ? 0.0301  ? 0.0531  ? -0.0902 ? 
0.0095  ? 
4  'X-RAY DIFFRACTION' ? refined -21.8510 31.2230 87.6711 0.2075 ? -0.0201 ? 0.0382  ? 0.1779 ? -0.0411 ? 0.2065 ? 2.3981 ? 0.4390 
? -0.7358 ? 1.1972 ? -0.4387 ? 3.4438 ? 0.0996  ? -0.3219 ? 0.3521  ? 0.1370  ? -0.0280 ? 0.0491  ? -0.4855 ? -0.0416 ? -0.0382 ? 
5  'X-RAY DIFFRACTION' ? refined -26.0974 18.7083 75.7439 0.0903 ? -0.0300 ? -0.0002 ? 0.1498 ? 0.0028  ? 0.1627 ? 1.5878 ? 
-0.2872 ? -1.0905 ? 0.6718 ? 0.6429  ? 2.1245 ? 0.0322  ? 0.0921  ? -0.0157 ? 0.0142  ? -0.0631 ? 0.1023  ? 0.0418  ? -0.3324 ? 
0.0678  ? 
6  'X-RAY DIFFRACTION' ? refined 8.2175   13.0444 69.2389 0.1142 ? -0.0008 ? 0.0155  ? 0.0971 ? -0.0070 ? 0.1350 ? 1.4606 ? 0.1466 
? 0.3894  ? 0.5395 ? 0.0566  ? 1.1119 ? 0.0245  ? -0.0058 ? -0.0803 ? -0.0085 ? -0.0438 ? -0.0405 ? 0.0776  ? 0.1320  ? 0.0178  ? 
7  'X-RAY DIFFRACTION' ? refined 5.1092   27.6699 58.5226 0.1465 ? -0.0424 ? 0.0073  ? 0.1606 ? 0.0117  ? 0.2014 ? 1.4454 ? 
-0.9843 ? -0.2845 ? 1.4482 ? -0.0581 ? 1.0560 ? 0.0189  ? 0.1442  ? 0.2393  ? 0.0472  ? -0.0458 ? -0.1971 ? -0.0946 ? 0.1625  ? 
0.0160  ? 
8  'X-RAY DIFFRACTION' ? refined -8.2033  27.7304 54.5527 0.1449 ? -0.0198 ? -0.0010 ? 0.1302 ? 0.0174  ? 0.1398 ? 2.1705 ? 0.0610 
? -0.7226 ? 1.0930 ? -0.2322 ? 2.7322 ? 0.0635  ? 0.3300  ? 0.1269  ? -0.1809 ? 0.0367  ? 0.0036  ? -0.1530 ? -0.1538 ? -0.0871 ? 
9  'X-RAY DIFFRACTION' ? refined 12.0815  21.7823 77.2673 0.1133 ? -0.0338 ? -0.0025 ? 0.1546 ? -0.0080 ? 0.1918 ? 1.3534 ? 
-0.0485 ? 0.1404  ? 0.8384 ? 0.0735  ? 2.3494 ? -0.0139 ? -0.1502 ? 0.1370  ? 0.0876  ? -0.0472 ? -0.0486 ? -0.2272 ? 0.1104  ? 
0.0607  ? 
10 'X-RAY DIFFRACTION' ? refined 1.8375   16.2577 87.0416 0.1076 ? -0.0229 ? -0.0039 ? 0.1857 ? 0.0051  ? 0.1142 ? 3.5488 ? 
-0.8873 ? -0.1224 ? 3.0685 ? -0.4871 ? 2.5789 ? -0.0677 ? -0.2740 ? 0.0211  ? 0.1354  ? 0.0573  ? -0.0266 ? -0.0975 ? -0.0096 ? 
0.0241  ? 
11 'X-RAY DIFFRACTION' ? refined -25.9699 35.8035 27.2354 0.1583 ? 0.0034  ? -0.0039 ? 0.0976 ? 0.0063  ? 0.1322 ? 1.6016 ? 0.0961 
? 0.1287  ? 0.7036 ? 0.0306  ? 0.9293 ? 0.0611  ? 0.0917  ? -0.0926 ? -0.0172 ? -0.0177 ? -0.0303 ? 0.1626  ? 0.0172  ? -0.0204 ? 
12 'X-RAY DIFFRACTION' ? refined -19.6696 39.2477 5.7809  0.2484 ? -0.0131 ? -0.0184 ? 0.3662 ? -0.0151 ? 0.2024 ? 0.9031 ? 0.5038 
? -0.3683 ? 0.3229 ? 0.0157  ? 2.0917 ? 0.0175  ? 0.3635  ? -0.1133 ? -0.1844 ? 0.0351  ? -0.0352 ? 0.0847  ? 0.1875  ? -0.0023 ? 
13 'X-RAY DIFFRACTION' ? refined -12.9304 41.2197 18.3412 0.1588 ? -0.0092 ? -0.0078 ? 0.2394 ? -0.0268 ? 0.1792 ? 1.5765 ? 0.1306 
? -0.5775 ? 0.6885 ? -0.1890 ? 2.2687 ? 0.0224  ? 0.1721  ? 0.0342  ? -0.0838 ? 0.0084  ? -0.1291 ? -0.0608 ? 0.4241  ? -0.0133 ? 
14 'X-RAY DIFFRACTION' ? refined -45.4482 33.3987 30.7175 0.1369 ? -0.0511 ? -0.0096 ? 0.1328 ? -0.0016 ? 0.1449 ? 1.6998 ? 
-0.4276 ? -0.2702 ? 1.2750 ? 0.1558  ? 1.3975 ? 0.0620  ? 0.0598  ? -0.1440 ? -0.0089 ? -0.0706 ? 0.1660  ? 0.1572  ? -0.2823 ? 
-0.0101 ? 
15 'X-RAY DIFFRACTION' ? refined -38.7758 47.8743 41.2081 0.1437 ? 0.0001  ? -0.0102 ? 0.1204 ? -0.0126 ? 0.1587 ? 2.3681 ? 1.1387 
? -0.5894 ? 1.4117 ? -0.0990 ? 1.3618 ? 0.0337  ? -0.2534 ? 0.2127  ? 0.0479  ? -0.0894 ? 0.1243  ? -0.0966 ? -0.0569 ? 0.0242  ? 
16 'X-RAY DIFFRACTION' ? refined -27.1093 51.0859 41.5734 0.1889 ? 0.0077  ? -0.0102 ? 0.1398 ? -0.0179 ? 0.1753 ? 1.9049 ? 
-0.0151 ? -0.4696 ? 1.1735 ? -0.3578 ? 2.6564 ? 0.0149  ? -0.2238 ? 0.1915  ? 0.1291  ? 0.0086  ? -0.0568 ? -0.1952 ? -0.0270 ? 
-0.0699 ? 
17 'X-RAY DIFFRACTION' ? refined -23.2197 43.2327 44.9390 0.1756 ? -0.0050 ? -0.0364 ? 0.1381 ? -0.0042 ? 0.1555 ? 1.9812 ? 
-0.5290 ? 0.1085  ? 1.2598 ? 0.5598  ? 2.5491 ? 0.0561  ? -0.3579 ? -0.0139 ? 0.3171  ? -0.0026 ? -0.0533 ? 0.0537  ? 0.1086  ? 
-0.0395 ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1  'X-RAY DIFFRACTION' 1  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 397 through 435 )
;
2  'X-RAY DIFFRACTION' 2  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 436 through 477 )
;
3  'X-RAY DIFFRACTION' 3  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 2 through 88 )
;
4  'X-RAY DIFFRACTION' 4  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 89 through 123 )
;
5  'X-RAY DIFFRACTION' 5  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 124 through 185 )
;
6  'X-RAY DIFFRACTION' 6  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 186 through 278 )
;
7  'X-RAY DIFFRACTION' 7  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 279 through 322 )
;
8  'X-RAY DIFFRACTION' 8  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 323 through 396 )
;
9  'X-RAY DIFFRACTION' 9  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 397 through 435 )
;
10 'X-RAY DIFFRACTION' 10 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 436 through 477 )
;
11 'X-RAY DIFFRACTION' 11 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 2 through 68 )
;
12 'X-RAY DIFFRACTION' 12 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 69 through 102 )
;
13 'X-RAY DIFFRACTION' 13 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 103 through 194 )
;
14 'X-RAY DIFFRACTION' 14 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 195 through 278 )
;
15 'X-RAY DIFFRACTION' 15 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 279 through 322 )
;
16 'X-RAY DIFFRACTION' 16 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 323 through 360 )
;
17 'X-RAY DIFFRACTION' 17 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 361 through 396 )
;
# 
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 
HIS N    N N N 161 
HIS CA   C N S 162 
HIS C    C N N 163 
HIS O    O N N 164 
HIS CB   C N N 165 
HIS CG   C Y N 166 
HIS ND1  N Y N 167 
HIS CD2  C Y N 168 
HIS CE1  C Y N 169 
HIS NE2  N Y N 170 
HIS OXT  O N N 171 
HIS H    H N N 172 
HIS H2   H N N 173 
HIS HA   H N N 174 
HIS HB2  H N N 175 
HIS HB3  H N N 176 
HIS HD1  H N N 177 
HIS HD2  H N N 178 
HIS HE1  H N N 179 
HIS HE2  H N N 180 
HIS HXT  H N N 181 
HOH O    O N N 182 
HOH H1   H N N 183 
HOH H2   H N N 184 
ILE N    N N N 185 
ILE CA   C N S 186 
ILE C    C N N 187 
ILE O    O N N 188 
ILE CB   C N S 189 
ILE CG1  C N N 190 
ILE CG2  C N N 191 
ILE CD1  C N N 192 
ILE OXT  O N N 193 
ILE H    H N N 194 
ILE H2   H N N 195 
ILE HA   H N N 196 
ILE HB   H N N 197 
ILE HG12 H N N 198 
ILE HG13 H N N 199 
ILE HG21 H N N 200 
ILE HG22 H N N 201 
ILE HG23 H N N 202 
ILE HD11 H N N 203 
ILE HD12 H N N 204 
ILE HD13 H N N 205 
ILE HXT  H N N 206 
LEU N    N N N 207 
LEU CA   C N S 208 
LEU C    C N N 209 
LEU O    O N N 210 
LEU CB   C N N 211 
LEU CG   C N N 212 
LEU CD1  C N N 213 
LEU CD2  C N N 214 
LEU OXT  O N N 215 
LEU H    H N N 216 
LEU H2   H N N 217 
LEU HA   H N N 218 
LEU HB2  H N N 219 
LEU HB3  H N N 220 
LEU HG   H N N 221 
LEU HD11 H N N 222 
LEU HD12 H N N 223 
LEU HD13 H N N 224 
LEU HD21 H N N 225 
LEU HD22 H N N 226 
LEU HD23 H N N 227 
LEU HXT  H N N 228 
LYS N    N N N 229 
LYS CA   C N S 230 
LYS C    C N N 231 
LYS O    O N N 232 
LYS CB   C N N 233 
LYS CG   C N N 234 
LYS CD   C N N 235 
LYS CE   C N N 236 
LYS NZ   N N N 237 
LYS OXT  O N N 238 
LYS H    H N N 239 
LYS H2   H N N 240 
LYS HA   H N N 241 
LYS HB2  H N N 242 
LYS HB3  H N N 243 
LYS HG2  H N N 244 
LYS HG3  H N N 245 
LYS HD2  H N N 246 
LYS HD3  H N N 247 
LYS HE2  H N N 248 
LYS HE3  H N N 249 
LYS HZ1  H N N 250 
LYS HZ2  H N N 251 
LYS HZ3  H N N 252 
LYS HXT  H N N 253 
MET N    N N N 254 
MET CA   C N S 255 
MET C    C N N 256 
MET O    O N N 257 
MET CB   C N N 258 
MET CG   C N N 259 
MET SD   S N N 260 
MET CE   C N N 261 
MET OXT  O N N 262 
MET H    H N N 263 
MET H2   H N N 264 
MET HA   H N N 265 
MET HB2  H N N 266 
MET HB3  H N N 267 
MET HG2  H N N 268 
MET HG3  H N N 269 
MET HE1  H N N 270 
MET HE2  H N N 271 
MET HE3  H N N 272 
MET HXT  H N N 273 
PHE N    N N N 274 
PHE CA   C N S 275 
PHE C    C N N 276 
PHE O    O N N 277 
PHE CB   C N N 278 
PHE CG   C Y N 279 
PHE CD1  C Y N 280 
PHE CD2  C Y N 281 
PHE CE1  C Y N 282 
PHE CE2  C Y N 283 
PHE CZ   C Y N 284 
PHE OXT  O N N 285 
PHE H    H N N 286 
PHE H2   H N N 287 
PHE HA   H N N 288 
PHE HB2  H N N 289 
PHE HB3  H N N 290 
PHE HD1  H N N 291 
PHE HD2  H N N 292 
PHE HE1  H N N 293 
PHE HE2  H N N 294 
PHE HZ   H N N 295 
PHE HXT  H N N 296 
PRO N    N N N 297 
PRO CA   C N S 298 
PRO C    C N N 299 
PRO O    O N N 300 
PRO CB   C N N 301 
PRO CG   C N N 302 
PRO CD   C N N 303 
PRO OXT  O N N 304 
PRO H    H N N 305 
PRO HA   H N N 306 
PRO HB2  H N N 307 
PRO HB3  H N N 308 
PRO HG2  H N N 309 
PRO HG3  H N N 310 
PRO HD2  H N N 311 
PRO HD3  H N N 312 
PRO HXT  H N N 313 
SER N    N N N 314 
SER CA   C N S 315 
SER C    C N N 316 
SER O    O N N 317 
SER CB   C N N 318 
SER OG   O N N 319 
SER OXT  O N N 320 
SER H    H N N 321 
SER H2   H N N 322 
SER HA   H N N 323 
SER HB2  H N N 324 
SER HB3  H N N 325 
SER HG   H N N 326 
SER HXT  H N N 327 
THR N    N N N 328 
THR CA   C N S 329 
THR C    C N N 330 
THR O    O N N 331 
THR CB   C N R 332 
THR OG1  O N N 333 
THR CG2  C N N 334 
THR OXT  O N N 335 
THR H    H N N 336 
THR H2   H N N 337 
THR HA   H N N 338 
THR HB   H N N 339 
THR HG1  H N N 340 
THR HG21 H N N 341 
THR HG22 H N N 342 
THR HG23 H N N 343 
THR HXT  H N N 344 
TRP N    N N N 345 
TRP CA   C N S 346 
TRP C    C N N 347 
TRP O    O N N 348 
TRP CB   C N N 349 
TRP CG   C Y N 350 
TRP CD1  C Y N 351 
TRP CD2  C Y N 352 
TRP NE1  N Y N 353 
TRP CE2  C Y N 354 
TRP CE3  C Y N 355 
TRP CZ2  C Y N 356 
TRP CZ3  C Y N 357 
TRP CH2  C Y N 358 
TRP OXT  O N N 359 
TRP H    H N N 360 
TRP H2   H N N 361 
TRP HA   H N N 362 
TRP HB2  H N N 363 
TRP HB3  H N N 364 
TRP HD1  H N N 365 
TRP HE1  H N N 366 
TRP HE3  H N N 367 
TRP HZ2  H N N 368 
TRP HZ3  H N N 369 
TRP HH2  H N N 370 
TRP HXT  H N N 371 
TYR N    N N N 372 
TYR CA   C N S 373 
TYR C    C N N 374 
TYR O    O N N 375 
TYR CB   C N N 376 
TYR CG   C Y N 377 
TYR CD1  C Y N 378 
TYR CD2  C Y N 379 
TYR CE1  C Y N 380 
TYR CE2  C Y N 381 
TYR CZ   C Y N 382 
TYR OH   O N N 383 
TYR OXT  O N N 384 
TYR H    H N N 385 
TYR H2   H N N 386 
TYR HA   H N N 387 
TYR HB2  H N N 388 
TYR HB3  H N N 389 
TYR HD1  H N N 390 
TYR HD2  H N N 391 
TYR HE1  H N N 392 
TYR HE2  H N N 393 
TYR HH   H N N 394 
TYR HXT  H N N 395 
VAL N    N N N 396 
VAL CA   C N S 397 
VAL C    C N N 398 
VAL O    O N N 399 
VAL CB   C N N 400 
VAL CG1  C N N 401 
VAL CG2  C N N 402 
VAL OXT  O N N 403 
VAL H    H N N 404 
VAL H2   H N N 405 
VAL HA   H N N 406 
VAL HB   H N N 407 
VAL HG11 H N N 408 
VAL HG12 H N N 409 
VAL HG13 H N N 410 
VAL HG21 H N N 411 
VAL HG22 H N N 412 
VAL HG23 H N N 413 
VAL HXT  H N N 414 
# 
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 
HIS N   CA   sing N N 153 
HIS N   H    sing N N 154 
HIS N   H2   sing N N 155 
HIS CA  C    sing N N 156 
HIS CA  CB   sing N N 157 
HIS CA  HA   sing N N 158 
HIS C   O    doub N N 159 
HIS C   OXT  sing N N 160 
HIS CB  CG   sing N N 161 
HIS CB  HB2  sing N N 162 
HIS CB  HB3  sing N N 163 
HIS CG  ND1  sing Y N 164 
HIS CG  CD2  doub Y N 165 
HIS ND1 CE1  doub Y N 166 
HIS ND1 HD1  sing N N 167 
HIS CD2 NE2  sing Y N 168 
HIS CD2 HD2  sing N N 169 
HIS CE1 NE2  sing Y N 170 
HIS CE1 HE1  sing N N 171 
HIS NE2 HE2  sing N N 172 
HIS OXT HXT  sing N N 173 
HOH O   H1   sing N N 174 
HOH O   H2   sing N N 175 
ILE N   CA   sing N N 176 
ILE N   H    sing N N 177 
ILE N   H2   sing N N 178 
ILE CA  C    sing N N 179 
ILE CA  CB   sing N N 180 
ILE CA  HA   sing N N 181 
ILE C   O    doub N N 182 
ILE C   OXT  sing N N 183 
ILE CB  CG1  sing N N 184 
ILE CB  CG2  sing N N 185 
ILE CB  HB   sing N N 186 
ILE CG1 CD1  sing N N 187 
ILE CG1 HG12 sing N N 188 
ILE CG1 HG13 sing N N 189 
ILE CG2 HG21 sing N N 190 
ILE CG2 HG22 sing N N 191 
ILE CG2 HG23 sing N N 192 
ILE CD1 HD11 sing N N 193 
ILE CD1 HD12 sing N N 194 
ILE CD1 HD13 sing N N 195 
ILE OXT HXT  sing N N 196 
LEU N   CA   sing N N 197 
LEU N   H    sing N N 198 
LEU N   H2   sing N N 199 
LEU CA  C    sing N N 200 
LEU CA  CB   sing N N 201 
LEU CA  HA   sing N N 202 
LEU C   O    doub N N 203 
LEU C   OXT  sing N N 204 
LEU CB  CG   sing N N 205 
LEU CB  HB2  sing N N 206 
LEU CB  HB3  sing N N 207 
LEU CG  CD1  sing N N 208 
LEU CG  CD2  sing N N 209 
LEU CG  HG   sing N N 210 
LEU CD1 HD11 sing N N 211 
LEU CD1 HD12 sing N N 212 
LEU CD1 HD13 sing N N 213 
LEU CD2 HD21 sing N N 214 
LEU CD2 HD22 sing N N 215 
LEU CD2 HD23 sing N N 216 
LEU OXT HXT  sing N N 217 
LYS N   CA   sing N N 218 
LYS N   H    sing N N 219 
LYS N   H2   sing N N 220 
LYS CA  C    sing N N 221 
LYS CA  CB   sing N N 222 
LYS CA  HA   sing N N 223 
LYS C   O    doub N N 224 
LYS C   OXT  sing N N 225 
LYS CB  CG   sing N N 226 
LYS CB  HB2  sing N N 227 
LYS CB  HB3  sing N N 228 
LYS CG  CD   sing N N 229 
LYS CG  HG2  sing N N 230 
LYS CG  HG3  sing N N 231 
LYS CD  CE   sing N N 232 
LYS CD  HD2  sing N N 233 
LYS CD  HD3  sing N N 234 
LYS CE  NZ   sing N N 235 
LYS CE  HE2  sing N N 236 
LYS CE  HE3  sing N N 237 
LYS NZ  HZ1  sing N N 238 
LYS NZ  HZ2  sing N N 239 
LYS NZ  HZ3  sing N N 240 
LYS OXT HXT  sing N N 241 
MET N   CA   sing N N 242 
MET N   H    sing N N 243 
MET N   H2   sing N N 244 
MET CA  C    sing N N 245 
MET CA  CB   sing N N 246 
MET CA  HA   sing N N 247 
MET C   O    doub N N 248 
MET C   OXT  sing N N 249 
MET CB  CG   sing N N 250 
MET CB  HB2  sing N N 251 
MET CB  HB3  sing N N 252 
MET CG  SD   sing N N 253 
MET CG  HG2  sing N N 254 
MET CG  HG3  sing N N 255 
MET SD  CE   sing N N 256 
MET CE  HE1  sing N N 257 
MET CE  HE2  sing N N 258 
MET CE  HE3  sing N N 259 
MET OXT HXT  sing N N 260 
PHE N   CA   sing N N 261 
PHE N   H    sing N N 262 
PHE N   H2   sing N N 263 
PHE CA  C    sing N N 264 
PHE CA  CB   sing N N 265 
PHE CA  HA   sing N N 266 
PHE C   O    doub N N 267 
PHE C   OXT  sing N N 268 
PHE CB  CG   sing N N 269 
PHE CB  HB2  sing N N 270 
PHE CB  HB3  sing N N 271 
PHE CG  CD1  doub Y N 272 
PHE CG  CD2  sing Y N 273 
PHE CD1 CE1  sing Y N 274 
PHE CD1 HD1  sing N N 275 
PHE CD2 CE2  doub Y N 276 
PHE CD2 HD2  sing N N 277 
PHE CE1 CZ   doub Y N 278 
PHE CE1 HE1  sing N N 279 
PHE CE2 CZ   sing Y N 280 
PHE CE2 HE2  sing N N 281 
PHE CZ  HZ   sing N N 282 
PHE OXT HXT  sing N N 283 
PRO N   CA   sing N N 284 
PRO N   CD   sing N N 285 
PRO N   H    sing N N 286 
PRO CA  C    sing N N 287 
PRO CA  CB   sing N N 288 
PRO CA  HA   sing N N 289 
PRO C   O    doub N N 290 
PRO C   OXT  sing N N 291 
PRO CB  CG   sing N N 292 
PRO CB  HB2  sing N N 293 
PRO CB  HB3  sing N N 294 
PRO CG  CD   sing N N 295 
PRO CG  HG2  sing N N 296 
PRO CG  HG3  sing N N 297 
PRO CD  HD2  sing N N 298 
PRO CD  HD3  sing N N 299 
PRO OXT HXT  sing N N 300 
SER N   CA   sing N N 301 
SER N   H    sing N N 302 
SER N   H2   sing N N 303 
SER CA  C    sing N N 304 
SER CA  CB   sing N N 305 
SER CA  HA   sing N N 306 
SER C   O    doub N N 307 
SER C   OXT  sing N N 308 
SER CB  OG   sing N N 309 
SER CB  HB2  sing N N 310 
SER CB  HB3  sing N N 311 
SER OG  HG   sing N N 312 
SER OXT HXT  sing N N 313 
THR N   CA   sing N N 314 
THR N   H    sing N N 315 
THR N   H2   sing N N 316 
THR CA  C    sing N N 317 
THR CA  CB   sing N N 318 
THR CA  HA   sing N N 319 
THR C   O    doub N N 320 
THR C   OXT  sing N N 321 
THR CB  OG1  sing N N 322 
THR CB  CG2  sing N N 323 
THR CB  HB   sing N N 324 
THR OG1 HG1  sing N N 325 
THR CG2 HG21 sing N N 326 
THR CG2 HG22 sing N N 327 
THR CG2 HG23 sing N N 328 
THR OXT HXT  sing N N 329 
TRP N   CA   sing N N 330 
TRP N   H    sing N N 331 
TRP N   H2   sing N N 332 
TRP CA  C    sing N N 333 
TRP CA  CB   sing N N 334 
TRP CA  HA   sing N N 335 
TRP C   O    doub N N 336 
TRP C   OXT  sing N N 337 
TRP CB  CG   sing N N 338 
TRP CB  HB2  sing N N 339 
TRP CB  HB3  sing N N 340 
TRP CG  CD1  doub Y N 341 
TRP CG  CD2  sing Y N 342 
TRP CD1 NE1  sing Y N 343 
TRP CD1 HD1  sing N N 344 
TRP CD2 CE2  doub Y N 345 
TRP CD2 CE3  sing Y N 346 
TRP NE1 CE2  sing Y N 347 
TRP NE1 HE1  sing N N 348 
TRP CE2 CZ2  sing Y N 349 
TRP CE3 CZ3  doub Y N 350 
TRP CE3 HE3  sing N N 351 
TRP CZ2 CH2  doub Y N 352 
TRP CZ2 HZ2  sing N N 353 
TRP CZ3 CH2  sing Y N 354 
TRP CZ3 HZ3  sing N N 355 
TRP CH2 HH2  sing N N 356 
TRP OXT HXT  sing N N 357 
TYR N   CA   sing N N 358 
TYR N   H    sing N N 359 
TYR N   H2   sing N N 360 
TYR CA  C    sing N N 361 
TYR CA  CB   sing N N 362 
TYR CA  HA   sing N N 363 
TYR C   O    doub N N 364 
TYR C   OXT  sing N N 365 
TYR CB  CG   sing N N 366 
TYR CB  HB2  sing N N 367 
TYR CB  HB3  sing N N 368 
TYR CG  CD1  doub Y N 369 
TYR CG  CD2  sing Y N 370 
TYR CD1 CE1  sing Y N 371 
TYR CD1 HD1  sing N N 372 
TYR CD2 CE2  doub Y N 373 
TYR CD2 HD2  sing N N 374 
TYR CE1 CZ   doub Y N 375 
TYR CE1 HE1  sing N N 376 
TYR CE2 CZ   sing Y N 377 
TYR CE2 HE2  sing N N 378 
TYR CZ  OH   sing N N 379 
TYR OH  HH   sing N N 380 
TYR OXT HXT  sing N N 381 
VAL N   CA   sing N N 382 
VAL N   H    sing N N 383 
VAL N   H2   sing N N 384 
VAL CA  C    sing N N 385 
VAL CA  CB   sing N N 386 
VAL CA  HA   sing N N 387 
VAL C   O    doub N N 388 
VAL C   OXT  sing N N 389 
VAL CB  CG1  sing N N 390 
VAL CB  CG2  sing N N 391 
VAL CB  HB   sing N N 392 
VAL CG1 HG11 sing N N 393 
VAL CG1 HG12 sing N N 394 
VAL CG1 HG13 sing N N 395 
VAL CG2 HG21 sing N N 396 
VAL CG2 HG22 sing N N 397 
VAL CG2 HG23 sing N N 398 
VAL OXT HXT  sing N N 399 
# 
_pdbx_audit_support.funding_organization   'Other government' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
loop_
_pdbx_entity_branch_list.entity_id 
_pdbx_entity_branch_list.comp_id 
_pdbx_entity_branch_list.num 
_pdbx_entity_branch_list.hetero 
2 GLC 1 n 
2 GLC 2 n 
2 GLC 3 n 
2 GLC 4 n 
2 GLC 5 n 
3 GLC 1 n 
3 GLC 2 n 
3 GLC 3 n 
3 GLC 4 n 
3 GLC 5 n 
3 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                    9K7D 
_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]   0.016281 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.001708 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.024516 
_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]   0.005110 
_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   ? -3.714  26.975 38.071  1.00 40.88 ? 2   LYS A N   1 
ATOM   2    C CA  . LYS A 1 2   ? -2.835  27.233 39.207  1.00 29.90 ? 2   LYS A CA  1 
ATOM   3    C C   . LYS A 1 2   ? -3.623  27.323 40.502  1.00 26.07 ? 2   LYS A C   1 
ATOM   4    O O   . LYS A 1 2   ? -4.372  28.283 40.732  1.00 33.15 ? 2   LYS A O   1 
ATOM   5    C CB  . LYS A 1 2   ? -2.044  28.518 38.987  1.00 38.81 ? 2   LYS A CB  1 
ATOM   6    C CG  . LYS A 1 2   ? -1.007  28.782 40.072  1.00 40.42 ? 2   LYS A CG  1 
ATOM   7    C CD  . LYS A 1 2   ? -0.334  30.121 39.856  1.00 50.75 ? 2   LYS A CD  1 
ATOM   8    C CE  . LYS A 1 2   ? -1.304  31.280 40.071  1.00 52.54 ? 2   LYS A CE  1 
ATOM   9    N NZ  . LYS A 1 2   ? -0.578  32.588 40.161  1.00 52.24 ? 2   LYS A NZ  1 
ATOM   10   N N   . LYS A 1 3   ? -3.463  26.318 41.352  1.00 19.77 ? 3   LYS A N   1 
ATOM   11   C CA  . LYS A 1 3   ? -4.213  26.225 42.594  1.00 19.66 ? 3   LYS A CA  1 
ATOM   12   C C   . LYS A 1 3   ? -3.357  26.669 43.771  1.00 21.18 ? 3   LYS A C   1 
ATOM   13   O O   . LYS A 1 3   ? -2.134  26.659 43.715  1.00 24.65 ? 3   LYS A O   1 
ATOM   14   C CB  . LYS A 1 3   ? -4.696  24.791 42.838  1.00 28.03 ? 3   LYS A CB  1 
ATOM   15   C CG  . LYS A 1 3   ? -5.447  24.156 41.671  1.00 34.27 ? 3   LYS A CG  1 
ATOM   16   C CD  . LYS A 1 3   ? -6.940  24.364 41.806  1.00 40.77 ? 3   LYS A CD  1 
ATOM   17   C CE  . LYS A 1 3   ? -7.729  23.406 40.919  1.00 37.84 ? 3   LYS A CE  1 
ATOM   18   N NZ  . LYS A 1 3   ? -9.064  23.127 41.509  1.00 43.37 ? 3   LYS A NZ  1 
ATOM   19   N N   . LEU A 1 4   ? -4.034  27.103 44.823  1.00 19.72 ? 4   LEU A N   1 
ATOM   20   C CA  . LEU A 1 4   ? -3.450  27.219 46.150  1.00 19.14 ? 4   LEU A CA  1 
ATOM   21   C C   . LEU A 1 4   ? -3.849  25.978 46.937  1.00 19.24 ? 4   LEU A C   1 
ATOM   22   O O   . LEU A 1 4   ? -5.041  25.670 47.067  1.00 18.19 ? 4   LEU A O   1 
ATOM   23   C CB  . LEU A 1 4   ? -3.937  28.489 46.862  1.00 18.82 ? 4   LEU A CB  1 
ATOM   24   C CG  . LEU A 1 4   ? -3.355  28.691 48.260  1.00 16.28 ? 4   LEU A CG  1 
ATOM   25   C CD1 . LEU A 1 4   ? -3.214  30.180 48.568  1.00 21.51 ? 4   LEU A CD1 1 
ATOM   26   C CD2 . LEU A 1 4   ? -4.207  28.026 49.349  1.00 17.72 ? 4   LEU A CD2 1 
ATOM   27   N N   . PHE A 1 5   ? -2.858  25.284 47.482  1.00 17.14 ? 5   PHE A N   1 
ATOM   28   C CA  . PHE A 1 5   ? -3.095  24.067 48.242  1.00 12.88 ? 5   PHE A CA  1 
ATOM   29   C C   . PHE A 1 5   ? -3.178  24.444 49.710  1.00 14.00 ? 5   PHE A C   1 
ATOM   30   O O   . PHE A 1 5   ? -2.197  24.918 50.293  1.00 23.01 ? 5   PHE A O   1 
ATOM   31   C CB  . PHE A 1 5   ? -1.974  23.049 47.994  1.00 19.21 ? 5   PHE A CB  1 
ATOM   32   C CG  . PHE A 1 5   ? -1.963  22.488 46.584  1.00 19.62 ? 5   PHE A CG  1 
ATOM   33   C CD1 . PHE A 1 5   ? -3.152  22.097 45.973  1.00 20.44 ? 5   PHE A CD1 1 
ATOM   34   C CD2 . PHE A 1 5   ? -0.772  22.336 45.887  1.00 17.56 ? 5   PHE A CD2 1 
ATOM   35   C CE1 . PHE A 1 5   ? -3.157  21.567 44.683  1.00 25.74 ? 5   PHE A CE1 1 
ATOM   36   C CE2 . PHE A 1 5   ? -0.764  21.808 44.586  1.00 21.20 ? 5   PHE A CE2 1 
ATOM   37   C CZ  . PHE A 1 5   ? -1.958  21.421 43.987  1.00 20.65 ? 5   PHE A CZ  1 
ATOM   38   N N   . LEU A 1 6   ? -4.341  24.229 50.299  1.00 19.14 ? 6   LEU A N   1 
ATOM   39   C CA  . LEU A 1 6   ? -4.630  24.637 51.663  1.00 19.27 ? 6   LEU A CA  1 
ATOM   40   C C   . LEU A 1 6   ? -4.779  23.387 52.515  1.00 15.22 ? 6   LEU A C   1 
ATOM   41   O O   . LEU A 1 6   ? -5.551  22.493 52.160  1.00 16.09 ? 6   LEU A O   1 
ATOM   42   C CB  . LEU A 1 6   ? -5.917  25.452 51.686  1.00 15.31 ? 6   LEU A CB  1 
ATOM   43   C CG  . LEU A 1 6   ? -6.357  26.002 53.045  1.00 14.73 ? 6   LEU A CG  1 
ATOM   44   C CD1 . LEU A 1 6   ? -5.277  26.915 53.615  1.00 18.73 ? 6   LEU A CD1 1 
ATOM   45   C CD2 . LEU A 1 6   ? -7.685  26.757 52.854  1.00 15.01 ? 6   LEU A CD2 1 
ATOM   46   N N   . VAL A 1 7   ? -4.037  23.310 53.622  1.00 10.55 ? 7   VAL A N   1 
ATOM   47   C CA  . VAL A 1 7   ? -4.021  22.112 54.464  1.00 10.24 ? 7   VAL A CA  1 
ATOM   48   C C   . VAL A 1 7   ? -4.311  22.534 55.900  1.00 14.69 ? 7   VAL A C   1 
ATOM   49   O O   . VAL A 1 7   ? -3.432  23.106 56.560  1.00 18.24 ? 7   VAL A O   1 
ATOM   50   C CB  . VAL A 1 7   ? -2.670  21.386 54.385  1.00 15.64 ? 7   VAL A CB  1 
ATOM   51   C CG1 . VAL A 1 7   ? -2.766  19.991 55.025  1.00 21.37 ? 7   VAL A CG1 1 
ATOM   52   C CG2 . VAL A 1 7   ? -2.221  21.281 52.922  1.00 17.08 ? 7   VAL A CG2 1 
ATOM   53   N N   . PHE A 1 8   ? -5.521  22.225 56.398  1.00 14.05 ? 8   PHE A N   1 
ATOM   54   C CA  . PHE A 1 8   ? -5.845  22.407 57.811  1.00 11.11 ? 8   PHE A CA  1 
ATOM   55   C C   . PHE A 1 8   ? -5.408  21.189 58.592  1.00 13.66 ? 8   PHE A C   1 
ATOM   56   O O   . PHE A 1 8   ? -5.637  20.066 58.152  1.00 13.76 ? 8   PHE A O   1 
ATOM   57   C CB  . PHE A 1 8   ? -7.348  22.582 58.014  1.00 12.90 ? 8   PHE A CB  1 
ATOM   58   C CG  . PHE A 1 8   ? -7.868  23.900 57.567  1.00 16.71 ? 8   PHE A CG  1 
ATOM   59   C CD1 . PHE A 1 8   ? -7.837  24.999 58.415  1.00 14.73 ? 8   PHE A CD1 1 
ATOM   60   C CD2 . PHE A 1 8   ? -8.412  24.035 56.301  1.00 19.09 ? 8   PHE A CD2 1 
ATOM   61   C CE1 . PHE A 1 8   ? -8.328  26.225 57.994  1.00 16.41 ? 8   PHE A CE1 1 
ATOM   62   C CE2 . PHE A 1 8   ? -8.913  25.252 55.880  1.00 15.15 ? 8   PHE A CE2 1 
ATOM   63   C CZ  . PHE A 1 8   ? -8.869  26.344 56.720  1.00 15.18 ? 8   PHE A CZ  1 
ATOM   64   N N   . TRP A 1 9   ? -4.779  21.419 59.746  1.00 10.86 ? 9   TRP A N   1 
ATOM   65   C CA  . TRP A 1 9   ? -4.368  20.329 60.638  1.00 10.52 ? 9   TRP A CA  1 
ATOM   66   C C   . TRP A 1 9   ? -4.736  20.747 62.062  1.00 13.72 ? 9   TRP A C   1 
ATOM   67   O O   . TRP A 1 9   ? -4.036  21.555 62.684  1.00 12.00 ? 9   TRP A O   1 
ATOM   68   C CB  . TRP A 1 9   ? -2.872  20.061 60.484  1.00 12.86 ? 9   TRP A CB  1 
ATOM   69   C CG  . TRP A 1 9   ? -2.383  18.725 61.001  1.00 14.51 ? 9   TRP A CG  1 
ATOM   70   C CD1 . TRP A 1 9   ? -3.088  17.821 61.763  1.00 16.26 ? 9   TRP A CD1 1 
ATOM   71   C CD2 . TRP A 1 9   ? -1.081  18.178 60.824  1.00 15.26 ? 9   TRP A CD2 1 
ATOM   72   N NE1 . TRP A 1 9   ? -2.285  16.742 62.075  1.00 13.99 ? 9   TRP A NE1 1 
ATOM   73   C CE2 . TRP A 1 9   ? -1.048  16.938 61.507  1.00 13.90 ? 9   TRP A CE2 1 
ATOM   74   C CE3 . TRP A 1 9   ? 0.070   18.615 60.155  1.00 14.88 ? 9   TRP A CE3 1 
ATOM   75   C CZ2 . TRP A 1 9   ? 0.095   16.129 61.533  1.00 15.35 ? 9   TRP A CZ2 1 
ATOM   76   C CZ3 . TRP A 1 9   ? 1.201   17.801 60.170  1.00 20.32 ? 9   TRP A CZ3 1 
ATOM   77   C CH2 . TRP A 1 9   ? 1.208   16.578 60.872  1.00 16.94 ? 9   TRP A CH2 1 
ATOM   78   N N   . TRP A 1 10  ? -5.856  20.225 62.553  1.00 12.80 ? 10  TRP A N   1 
ATOM   79   C CA  . TRP A 1 10  ? -6.426  20.595 63.842  1.00 12.71 ? 10  TRP A CA  1 
ATOM   80   C C   . TRP A 1 10  ? -5.911  19.617 64.904  1.00 11.11 ? 10  TRP A C   1 
ATOM   81   O O   . TRP A 1 10  ? -6.236  18.421 64.862  1.00 15.41 ? 10  TRP A O   1 
ATOM   82   C CB  . TRP A 1 10  ? -7.949  20.527 63.779  1.00 12.99 ? 10  TRP A CB  1 
ATOM   83   C CG  . TRP A 1 10  ? -8.634  21.476 62.787  1.00 12.35 ? 10  TRP A CG  1 
ATOM   84   C CD1 . TRP A 1 10  ? -9.349  21.127 61.676  1.00 16.24 ? 10  TRP A CD1 1 
ATOM   85   C CD2 . TRP A 1 10  ? -8.705  22.904 62.878  1.00 12.65 ? 10  TRP A CD2 1 
ATOM   86   N NE1 . TRP A 1 10  ? -9.863  22.266 61.055  1.00 11.75 ? 10  TRP A NE1 1 
ATOM   87   C CE2 . TRP A 1 10  ? -9.492  23.361 61.792  1.00 11.61 ? 10  TRP A CE2 1 
ATOM   88   C CE3 . TRP A 1 10  ? -8.205  23.837 63.785  1.00 11.57 ? 10  TRP A CE3 1 
ATOM   89   C CZ2 . TRP A 1 10  ? -9.762  24.712 61.584  1.00 12.14 ? 10  TRP A CZ2 1 
ATOM   90   C CZ3 . TRP A 1 10  ? -8.480  25.190 63.573  1.00 12.42 ? 10  TRP A CZ3 1 
ATOM   91   C CH2 . TRP A 1 10  ? -9.269  25.605 62.481  1.00 11.14 ? 10  TRP A CH2 1 
ATOM   92   N N   . HIS A 1 11  ? -5.158  20.125 65.880  1.00 10.76 ? 11  HIS A N   1 
ATOM   93   C CA  . HIS A 1 11  ? -4.488  19.294 66.883  1.00 9.50  ? 11  HIS A CA  1 
ATOM   94   C C   . HIS A 1 11  ? -5.340  19.194 68.144  1.00 11.93 ? 11  HIS A C   1 
ATOM   95   O O   . HIS A 1 11  ? -5.646  20.224 68.761  1.00 14.35 ? 11  HIS A O   1 
ATOM   96   C CB  . HIS A 1 11  ? -3.126  19.907 67.219  1.00 10.29 ? 11  HIS A CB  1 
ATOM   97   C CG  . HIS A 1 11  ? -2.580  19.480 68.549  1.00 10.60 ? 11  HIS A CG  1 
ATOM   98   N ND1 . HIS A 1 11  ? -2.194  18.181 68.812  1.00 13.45 ? 11  HIS A ND1 1 
ATOM   99   C CD2 . HIS A 1 11  ? -2.354  20.181 69.686  1.00 14.85 ? 11  HIS A CD2 1 
ATOM   100  C CE1 . HIS A 1 11  ? -1.745  18.103 70.057  1.00 12.36 ? 11  HIS A CE1 1 
ATOM   101  N NE2 . HIS A 1 11  ? -1.845  19.301 70.613  1.00 11.34 ? 11  HIS A NE2 1 
ATOM   102  N N   . MET A 1 12  ? -5.700  17.961 68.537  1.00 10.74 ? 12  MET A N   1 
ATOM   103  C CA  . MET A 1 12  ? -6.559  17.685 69.690  1.00 8.83  ? 12  MET A CA  1 
ATOM   104  C C   . MET A 1 12  ? -5.764  16.959 70.779  1.00 16.20 ? 12  MET A C   1 
ATOM   105  O O   . MET A 1 12  ? -5.112  15.934 70.508  1.00 12.46 ? 12  MET A O   1 
ATOM   106  C CB  . MET A 1 12  ? -7.753  16.806 69.285  1.00 8.33  ? 12  MET A CB  1 
ATOM   107  C CG  . MET A 1 12  ? -8.485  17.243 68.003  1.00 9.75  ? 12  MET A CG  1 
ATOM   108  S SD  . MET A 1 12  ? -9.162  18.894 68.269  1.00 12.60 ? 12  MET A SD  1 
ATOM   109  C CE  . MET A 1 12  ? -10.365 18.960 66.910  1.00 14.84 ? 12  MET A CE  1 
ATOM   110  N N   . HIS A 1 13  ? -5.883  17.433 72.024  1.00 12.39 ? 13  HIS A N   1 
ATOM   111  C CA  . HIS A 1 13  ? -5.082  16.848 73.089  1.00 12.40 ? 13  HIS A CA  1 
ATOM   112  C C   . HIS A 1 13  ? -5.718  17.188 74.433  1.00 10.18 ? 13  HIS A C   1 
ATOM   113  O O   . HIS A 1 13  ? -6.226  18.291 74.611  1.00 11.77 ? 13  HIS A O   1 
ATOM   114  C CB  . HIS A 1 13  ? -3.645  17.402 73.068  1.00 10.24 ? 13  HIS A CB  1 
ATOM   115  C CG  . HIS A 1 13  ? -2.827  17.013 74.269  1.00 11.91 ? 13  HIS A CG  1 
ATOM   116  N ND1 . HIS A 1 13  ? -2.652  15.701 74.661  1.00 12.13 ? 13  HIS A ND1 1 
ATOM   117  C CD2 . HIS A 1 13  ? -2.124  17.770 75.156  1.00 14.60 ? 13  HIS A CD2 1 
ATOM   118  C CE1 . HIS A 1 13  ? -1.902  15.667 75.749  1.00 12.17 ? 13  HIS A CE1 1 
ATOM   119  N NE2 . HIS A 1 13  ? -1.548  16.906 76.060  1.00 14.24 ? 13  HIS A NE2 1 
ATOM   120  N N   . GLN A 1 14  ? -5.602  16.265 75.400  1.00 9.14  ? 14  GLN A N   1 
ATOM   121  C CA  . GLN A 1 14  ? -5.782  16.572 76.839  1.00 10.37 ? 14  GLN A CA  1 
ATOM   122  C C   . GLN A 1 14  ? -4.767  15.720 77.594  1.00 12.10 ? 14  GLN A C   1 
ATOM   123  O O   . GLN A 1 14  ? -4.567  14.542 77.253  1.00 13.93 ? 14  GLN A O   1 
ATOM   124  C CB  . GLN A 1 14  ? -7.193  16.260 77.382  1.00 13.99 ? 14  GLN A CB  1 
ATOM   125  C CG  . GLN A 1 14  ? -8.361  17.093 76.762  1.00 12.17 ? 14  GLN A CG  1 
ATOM   126  C CD  . GLN A 1 14  ? -8.268  18.591 77.089  1.00 15.59 ? 14  GLN A CD  1 
ATOM   127  O OE1 . GLN A 1 14  ? -7.661  19.019 78.104  1.00 13.38 ? 14  GLN A OE1 1 
ATOM   128  N NE2 . GLN A 1 14  ? -8.811  19.401 76.185  1.00 14.54 ? 14  GLN A NE2 1 
ATOM   129  N N   . PRO A 1 15  ? -4.100  16.275 78.604  1.00 13.58 ? 15  PRO A N   1 
ATOM   130  C CA  . PRO A 1 15  ? -3.312  15.434 79.499  1.00 13.04 ? 15  PRO A CA  1 
ATOM   131  C C   . PRO A 1 15  ? -4.235  14.542 80.328  1.00 9.75  ? 15  PRO A C   1 
ATOM   132  O O   . PRO A 1 15  ? -5.457  14.726 80.388  1.00 15.43 ? 15  PRO A O   1 
ATOM   133  C CB  . PRO A 1 15  ? -2.571  16.443 80.377  1.00 14.45 ? 15  PRO A CB  1 
ATOM   134  C CG  . PRO A 1 15  ? -3.500  17.599 80.471  1.00 12.09 ? 15  PRO A CG  1 
ATOM   135  C CD  . PRO A 1 15  ? -4.129  17.678 79.053  1.00 12.47 ? 15  PRO A CD  1 
ATOM   136  N N   . LEU A 1 16  ? -3.631  13.565 80.987  1.00 15.55 ? 16  LEU A N   1 
ATOM   137  C CA  . LEU A 1 16  ? -4.407  12.567 81.725  1.00 16.13 ? 16  LEU A CA  1 
ATOM   138  C C   . LEU A 1 16  ? -4.940  13.168 83.026  1.00 18.32 ? 16  LEU A C   1 
ATOM   139  O O   . LEU A 1 16  ? -4.172  13.429 83.958  1.00 15.13 ? 16  LEU A O   1 
ATOM   140  C CB  . LEU A 1 16  ? -3.552  11.328 81.993  1.00 16.70 ? 16  LEU A CB  1 
ATOM   141  C CG  . LEU A 1 16  ? -4.324  10.199 82.674  1.00 13.66 ? 16  LEU A CG  1 
ATOM   142  C CD1 . LEU A 1 16  ? -5.552  9.847  81.823  1.00 12.43 ? 16  LEU A CD1 1 
ATOM   143  C CD2 . LEU A 1 16  ? -3.428  8.970  82.917  1.00 17.51 ? 16  LEU A CD2 1 
ATOM   144  N N   . TYR A 1 17  ? -6.264  13.347 83.111  1.00 17.02 ? 17  TYR A N   1 
ATOM   145  C CA  . TYR A 1 17  ? -6.897  13.896 84.314  1.00 15.13 ? 17  TYR A CA  1 
ATOM   146  C C   . TYR A 1 17  ? -7.256  12.834 85.338  1.00 14.45 ? 17  TYR A C   1 
ATOM   147  O O   . TYR A 1 17  ? -7.722  13.187 86.423  1.00 17.74 ? 17  TYR A O   1 
ATOM   148  C CB  . TYR A 1 17  ? -8.162  14.700 83.944  1.00 17.86 ? 17  TYR A CB  1 
ATOM   149  C CG  . TYR A 1 17  ? -7.870  15.896 83.071  1.00 15.31 ? 17  TYR A CG  1 
ATOM   150  C CD1 . TYR A 1 17  ? -7.045  16.928 83.539  1.00 15.77 ? 17  TYR A CD1 1 
ATOM   151  C CD2 . TYR A 1 17  ? -8.394  15.986 81.770  1.00 12.16 ? 17  TYR A CD2 1 
ATOM   152  C CE1 . TYR A 1 17  ? -6.770  18.038 82.750  1.00 15.98 ? 17  TYR A CE1 1 
ATOM   153  C CE2 . TYR A 1 17  ? -8.123  17.089 80.964  1.00 10.14 ? 17  TYR A CE2 1 
ATOM   154  C CZ  . TYR A 1 17  ? -7.291  18.101 81.456  1.00 17.80 ? 17  TYR A CZ  1 
ATOM   155  O OH  . TYR A 1 17  ? -7.020  19.183 80.664  1.00 14.06 ? 17  TYR A OH  1 
ATOM   156  N N   . ARG A 1 18  ? -7.029  11.558 85.038  1.00 14.93 ? 18  ARG A N   1 
ATOM   157  C CA  . ARG A 1 18  ? -7.422  10.460 85.914  1.00 15.19 ? 18  ARG A CA  1 
ATOM   158  C C   . ARG A 1 18  ? -6.325  10.223 86.949  1.00 19.39 ? 18  ARG A C   1 
ATOM   159  O O   . ARG A 1 18  ? -5.228  9.737  86.628  1.00 17.18 ? 18  ARG A O   1 
ATOM   160  C CB  . ARG A 1 18  ? -7.703  9.194  85.109  1.00 15.06 ? 18  ARG A CB  1 
ATOM   161  C CG  . ARG A 1 18  ? -8.204  8.001  85.946  1.00 18.04 ? 18  ARG A CG  1 
ATOM   162  C CD  . ARG A 1 18  ? -8.252  6.713  85.087  1.00 19.21 ? 18  ARG A CD  1 
ATOM   163  N NE  . ARG A 1 18  ? -8.844  5.587  85.811  1.00 20.60 ? 18  ARG A NE  1 
ATOM   164  C CZ  . ARG A 1 18  ? -8.214  4.832  86.711  1.00 28.88 ? 18  ARG A CZ  1 
ATOM   165  N NH1 . ARG A 1 18  ? -6.940  5.062  87.035  1.00 27.49 ? 18  ARG A NH1 1 
ATOM   166  N NH2 . ARG A 1 18  ? -8.865  3.833  87.294  1.00 34.01 ? 18  ARG A NH2 1 
ATOM   167  N N   . GLU A 1 19  ? -6.635  10.551 88.185  1.00 16.56 ? 19  GLU A N   1 
ATOM   168  C CA  . GLU A 1 19  ? -5.710  10.350 89.282  1.00 23.25 ? 19  GLU A CA  1 
ATOM   169  C C   . GLU A 1 19  ? -5.576  8.857  89.556  1.00 23.92 ? 19  GLU A C   1 
ATOM   170  O O   . GLU A 1 19  ? -6.589  8.160  89.619  1.00 23.64 ? 19  GLU A O   1 
ATOM   171  C CB  . GLU A 1 19  ? -6.239  11.083 90.515  1.00 21.82 ? 19  GLU A CB  1 
ATOM   172  C CG  . GLU A 1 19  ? -5.155  11.566 91.461  1.00 28.33 ? 19  GLU A CG  1 
ATOM   173  C CD  . GLU A 1 19  ? -4.866  10.549 92.537  1.00 33.38 ? 19  GLU A CD  1 
ATOM   174  O OE1 . GLU A 1 19  ? -5.495  9.470  92.511  1.00 31.16 ? 19  GLU A OE1 1 
ATOM   175  O OE2 . GLU A 1 19  ? -4.014  10.827 93.402  1.00 35.33 ? 19  GLU A OE2 1 
ATOM   176  N N   . PRO A 1 20  ? -4.359  8.333  89.713  1.00 25.13 ? 20  PRO A N   1 
ATOM   177  C CA  . PRO A 1 20  ? -4.173  6.876  89.688  1.00 25.07 ? 20  PRO A CA  1 
ATOM   178  C C   . PRO A 1 20  ? -4.514  6.171  90.982  1.00 30.80 ? 20  PRO A C   1 
ATOM   179  O O   . PRO A 1 20  ? -4.731  4.952  90.951  1.00 37.52 ? 20  PRO A O   1 
ATOM   180  C CB  . PRO A 1 20  ? -2.683  6.723  89.380  1.00 27.64 ? 20  PRO A CB  1 
ATOM   181  C CG  . PRO A 1 20  ? -2.065  7.970  89.953  1.00 30.44 ? 20  PRO A CG  1 
ATOM   182  C CD  . PRO A 1 20  ? -3.073  9.060  89.727  1.00 24.08 ? 20  PRO A CD  1 
ATOM   183  N N   . TYR A 1 21  ? -4.555  6.878  92.110  1.00 24.36 ? 21  TYR A N   1 
ATOM   184  C CA  . TYR A 1 21  ? -4.920  6.234  93.365  1.00 28.44 ? 21  TYR A CA  1 
ATOM   185  C C   . TYR A 1 21  ? -6.427  6.210  93.576  1.00 29.56 ? 21  TYR A C   1 
ATOM   186  O O   . TYR A 1 21  ? -6.958  5.219  94.082  1.00 39.88 ? 21  TYR A O   1 
ATOM   187  C CB  . TYR A 1 21  ? -4.219  6.934  94.529  1.00 27.56 ? 21  TYR A CB  1 
ATOM   188  C CG  . TYR A 1 21  ? -2.733  6.763  94.449  1.00 31.29 ? 21  TYR A CG  1 
ATOM   189  C CD1 . TYR A 1 21  ? -2.133  5.602  94.911  1.00 35.53 ? 21  TYR A CD1 1 
ATOM   190  C CD2 . TYR A 1 21  ? -1.921  7.734  93.861  1.00 28.36 ? 21  TYR A CD2 1 
ATOM   191  C CE1 . TYR A 1 21  ? -0.783  5.415  94.824  1.00 32.20 ? 21  TYR A CE1 1 
ATOM   192  C CE2 . TYR A 1 21  ? -0.549  7.554  93.771  1.00 30.27 ? 21  TYR A CE2 1 
ATOM   193  C CZ  . TYR A 1 21  ? 0.008   6.389  94.254  1.00 31.32 ? 21  TYR A CZ  1 
ATOM   194  O OH  . TYR A 1 21  ? 1.355   6.177  94.184  1.00 31.29 ? 21  TYR A OH  1 
ATOM   195  N N   . THR A 1 22  ? -7.137  7.267  93.176  1.00 30.04 ? 22  THR A N   1 
ATOM   196  C CA  . THR A 1 22  ? -8.585  7.301  93.324  1.00 30.11 ? 22  THR A CA  1 
ATOM   197  C C   . THR A 1 22  ? -9.320  6.902  92.061  1.00 30.55 ? 22  THR A C   1 
ATOM   198  O O   . THR A 1 22  ? -10.509 6.580  92.136  1.00 28.19 ? 22  THR A O   1 
ATOM   199  C CB  . THR A 1 22  ? -9.057  8.697  93.721  1.00 29.35 ? 22  THR A CB  1 
ATOM   200  O OG1 . THR A 1 22  ? -8.736  9.616  92.661  1.00 27.34 ? 22  THR A OG1 1 
ATOM   201  C CG2 . THR A 1 22  ? -8.395  9.129  95.006  1.00 30.55 ? 22  THR A CG2 1 
ATOM   202  N N   . GLY A 1 23  ? -8.650  6.934  90.911  1.00 25.67 ? 23  GLY A N   1 
ATOM   203  C CA  . GLY A 1 23  ? -9.317  6.646  89.661  1.00 29.84 ? 23  GLY A CA  1 
ATOM   204  C C   . GLY A 1 23  ? -10.276 7.712  89.197  1.00 28.60 ? 23  GLY A C   1 
ATOM   205  O O   . GLY A 1 23  ? -11.004 7.486  88.228  1.00 31.78 ? 23  GLY A O   1 
ATOM   206  N N   . GLU A 1 24  ? -10.292 8.877  89.845  1.00 22.05 ? 24  GLU A N   1 
ATOM   207  C CA  . GLU A 1 24  ? -11.221 9.949  89.500  1.00 20.02 ? 24  GLU A CA  1 
ATOM   208  C C   . GLU A 1 24  ? -10.595 10.919 88.514  1.00 18.89 ? 24  GLU A C   1 
ATOM   209  O O   . GLU A 1 24  ? -9.418  11.279 88.647  1.00 21.41 ? 24  GLU A O   1 
ATOM   210  C CB  . GLU A 1 24  ? -11.638 10.719 90.752  1.00 21.49 ? 24  GLU A CB  1 
ATOM   211  C CG  . GLU A 1 24  ? -12.291 9.829  91.782  1.00 31.35 ? 24  GLU A CG  1 
ATOM   212  C CD  . GLU A 1 24  ? -12.405 10.488 93.135  1.00 43.25 ? 24  GLU A CD  1 
ATOM   213  O OE1 . GLU A 1 24  ? -13.252 10.035 93.928  1.00 61.62 ? 24  GLU A OE1 1 
ATOM   214  O OE2 . GLU A 1 24  ? -11.648 11.442 93.413  1.00 51.99 ? 24  GLU A OE2 1 
ATOM   215  N N   . TYR A 1 25  ? -11.397 11.357 87.537  1.00 14.62 ? 25  TYR A N   1 
ATOM   216  C CA  . TYR A 1 25  ? -11.017 12.472 86.678  1.00 12.23 ? 25  TYR A CA  1 
ATOM   217  C C   . TYR A 1 25  ? -11.200 13.762 87.475  1.00 15.60 ? 25  TYR A C   1 
ATOM   218  O O   . TYR A 1 25  ? -12.332 14.147 87.804  1.00 18.90 ? 25  TYR A O   1 
ATOM   219  C CB  . TYR A 1 25  ? -11.840 12.495 85.393  1.00 18.52 ? 25  TYR A CB  1 
ATOM   220  C CG  . TYR A 1 25  ? -11.340 11.481 84.363  1.00 20.78 ? 25  TYR A CG  1 
ATOM   221  C CD1 . TYR A 1 25  ? -11.563 10.113 84.542  1.00 18.13 ? 25  TYR A CD1 1 
ATOM   222  C CD2 . TYR A 1 25  ? -10.655 11.900 83.219  1.00 16.01 ? 25  TYR A CD2 1 
ATOM   223  C CE1 . TYR A 1 25  ? -11.120 9.177  83.613  1.00 18.02 ? 25  TYR A CE1 1 
ATOM   224  C CE2 . TYR A 1 25  ? -10.187 10.964 82.284  1.00 14.39 ? 25  TYR A CE2 1 
ATOM   225  C CZ  . TYR A 1 25  ? -10.431 9.619  82.487  1.00 20.11 ? 25  TYR A CZ  1 
ATOM   226  O OH  . TYR A 1 25  ? -9.969  8.695  81.572  1.00 19.36 ? 25  TYR A OH  1 
ATOM   227  N N   . LEU A 1 26  ? -10.089 14.442 87.776  1.00 17.17 ? 26  LEU A N   1 
ATOM   228  C CA  . LEU A 1 26  ? -10.133 15.581 88.693  1.00 18.28 ? 26  LEU A CA  1 
ATOM   229  C C   . LEU A 1 26  ? -10.496 16.895 88.022  1.00 20.82 ? 26  LEU A C   1 
ATOM   230  O O   . LEU A 1 26  ? -10.850 17.849 88.725  1.00 18.79 ? 26  LEU A O   1 
ATOM   231  C CB  . LEU A 1 26  ? -8.786  15.742 89.417  1.00 14.23 ? 26  LEU A CB  1 
ATOM   232  C CG  . LEU A 1 26  ? -8.373  14.532 90.246  1.00 17.18 ? 26  LEU A CG  1 
ATOM   233  C CD1 . LEU A 1 26  ? -6.996  14.790 90.897  1.00 21.70 ? 26  LEU A CD1 1 
ATOM   234  C CD2 . LEU A 1 26  ? -9.423  14.193 91.314  1.00 22.58 ? 26  LEU A CD2 1 
ATOM   235  N N   . LEU A 1 27  ? -10.389 16.980 86.696  1.00 16.46 ? 27  LEU A N   1 
ATOM   236  C CA  . LEU A 1 27  ? -10.925 18.106 85.947  1.00 18.13 ? 27  LEU A CA  1 
ATOM   237  C C   . LEU A 1 27  ? -11.835 17.562 84.850  1.00 14.36 ? 27  LEU A C   1 
ATOM   238  O O   . LEU A 1 27  ? -11.644 16.427 84.387  1.00 16.60 ? 27  LEU A O   1 
ATOM   239  C CB  . LEU A 1 27  ? -9.805  18.955 85.311  1.00 13.97 ? 27  LEU A CB  1 
ATOM   240  C CG  . LEU A 1 27  ? -8.999  19.764 86.340  1.00 19.27 ? 27  LEU A CG  1 
ATOM   241  C CD1 . LEU A 1 27  ? -7.707  20.356 85.730  1.00 21.95 ? 27  LEU A CD1 1 
ATOM   242  C CD2 . LEU A 1 27  ? -9.841  20.856 86.978  1.00 21.32 ? 27  LEU A CD2 1 
ATOM   243  N N   . PRO A 1 28  ? -12.804 18.350 84.396  1.00 17.04 ? 28  PRO A N   1 
ATOM   244  C CA  . PRO A 1 28  ? -13.765 17.873 83.386  1.00 18.70 ? 28  PRO A CA  1 
ATOM   245  C C   . PRO A 1 28  ? -13.419 18.251 81.950  1.00 17.38 ? 28  PRO A C   1 
ATOM   246  O O   . PRO A 1 28  ? -14.279 18.108 81.087  1.00 14.81 ? 28  PRO A O   1 
ATOM   247  C CB  . PRO A 1 28  ? -15.050 18.588 83.817  1.00 18.51 ? 28  PRO A CB  1 
ATOM   248  C CG  . PRO A 1 28  ? -14.558 19.923 84.269  1.00 16.65 ? 28  PRO A CG  1 
ATOM   249  C CD  . PRO A 1 28  ? -13.223 19.641 84.979  1.00 16.60 ? 28  PRO A CD  1 
ATOM   250  N N   . TRP A 1 29  ? -12.211 18.743 81.690  1.00 13.38 ? 29  TRP A N   1 
ATOM   251  C CA  . TRP A 1 29  ? -11.931 19.378 80.407  1.00 14.49 ? 29  TRP A CA  1 
ATOM   252  C C   . TRP A 1 29  ? -12.012 18.402 79.243  1.00 14.41 ? 29  TRP A C   1 
ATOM   253  O O   . TRP A 1 29  ? -12.411 18.800 78.141  1.00 14.66 ? 29  TRP A O   1 
ATOM   254  C CB  . TRP A 1 29  ? -10.558 20.031 80.442  1.00 13.34 ? 29  TRP A CB  1 
ATOM   255  C CG  . TRP A 1 29  ? -10.394 21.164 81.422  1.00 16.15 ? 29  TRP A CG  1 
ATOM   256  C CD1 . TRP A 1 29  ? -9.423  21.276 82.388  1.00 16.08 ? 29  TRP A CD1 1 
ATOM   257  C CD2 . TRP A 1 29  ? -11.179 22.371 81.504  1.00 16.17 ? 29  TRP A CD2 1 
ATOM   258  N NE1 . TRP A 1 29  ? -9.578  22.461 83.077  1.00 18.61 ? 29  TRP A NE1 1 
ATOM   259  C CE2 . TRP A 1 29  ? -10.629 23.160 82.534  1.00 19.23 ? 29  TRP A CE2 1 
ATOM   260  C CE3 . TRP A 1 29  ? -12.263 22.875 80.775  1.00 20.52 ? 29  TRP A CE3 1 
ATOM   261  C CZ2 . TRP A 1 29  ? -11.152 24.409 82.877  1.00 18.36 ? 29  TRP A CZ2 1 
ATOM   262  C CZ3 . TRP A 1 29  ? -12.772 24.108 81.109  1.00 25.37 ? 29  TRP A CZ3 1 
ATOM   263  C CH2 . TRP A 1 29  ? -12.214 24.864 82.153  1.00 26.04 ? 29  TRP A CH2 1 
ATOM   264  N N   . THR A 1 30  ? -11.629 17.135 79.450  1.00 11.38 ? 30  THR A N   1 
ATOM   265  C CA  . THR A 1 30  ? -11.799 16.155 78.380  1.00 11.65 ? 30  THR A CA  1 
ATOM   266  C C   . THR A 1 30  ? -13.275 15.967 78.061  1.00 14.34 ? 30  THR A C   1 
ATOM   267  O O   . THR A 1 30  ? -13.662 15.947 76.890  1.00 16.84 ? 30  THR A O   1 
ATOM   268  C CB  . THR A 1 30  ? -11.163 14.822 78.760  1.00 19.12 ? 30  THR A CB  1 
ATOM   269  O OG1 . THR A 1 30  ? -9.757  15.002 78.939  1.00 16.92 ? 30  THR A OG1 1 
ATOM   270  C CG2 . THR A 1 30  ? -11.435 13.752 77.680  1.00 15.85 ? 30  THR A CG2 1 
ATOM   271  N N   . PHE A 1 31  ? -14.119 15.853 79.096  1.00 12.85 ? 31  PHE A N   1 
ATOM   272  C CA  . PHE A 1 31  ? -15.547 15.718 78.846  1.00 13.97 ? 31  PHE A CA  1 
ATOM   273  C C   . PHE A 1 31  ? -16.076 16.910 78.056  1.00 15.13 ? 31  PHE A C   1 
ATOM   274  O O   . PHE A 1 31  ? -16.819 16.752 77.074  1.00 16.24 ? 31  PHE A O   1 
ATOM   275  C CB  . PHE A 1 31  ? -16.308 15.585 80.172  1.00 13.29 ? 31  PHE A CB  1 
ATOM   276  C CG  . PHE A 1 31  ? -17.798 15.574 79.993  1.00 15.46 ? 31  PHE A CG  1 
ATOM   277  C CD1 . PHE A 1 31  ? -18.430 14.432 79.565  1.00 16.20 ? 31  PHE A CD1 1 
ATOM   278  C CD2 . PHE A 1 31  ? -18.554 16.742 80.179  1.00 18.86 ? 31  PHE A CD2 1 
ATOM   279  C CE1 . PHE A 1 31  ? -19.819 14.397 79.369  1.00 16.43 ? 31  PHE A CE1 1 
ATOM   280  C CE2 . PHE A 1 31  ? -19.949 16.725 79.979  1.00 15.23 ? 31  PHE A CE2 1 
ATOM   281  C CZ  . PHE A 1 31  ? -20.578 15.552 79.585  1.00 13.88 ? 31  PHE A CZ  1 
ATOM   282  N N   . PHE A 1 32  ? -15.731 18.120 78.491  1.00 15.09 ? 32  PHE A N   1 
ATOM   283  C CA  . PHE A 1 32  ? -16.370 19.289 77.901  1.00 15.53 ? 32  PHE A CA  1 
ATOM   284  C C   . PHE A 1 32  ? -15.868 19.529 76.483  1.00 14.06 ? 32  PHE A C   1 
ATOM   285  O O   . PHE A 1 32  ? -16.644 19.925 75.608  1.00 15.46 ? 32  PHE A O   1 
ATOM   286  C CB  . PHE A 1 32  ? -16.129 20.506 78.794  1.00 11.25 ? 32  PHE A CB  1 
ATOM   287  C CG  . PHE A 1 32  ? -17.085 20.611 79.957  1.00 11.99 ? 32  PHE A CG  1 
ATOM   288  C CD1 . PHE A 1 32  ? -18.472 20.525 79.762  1.00 16.99 ? 32  PHE A CD1 1 
ATOM   289  C CD2 . PHE A 1 32  ? -16.602 20.799 81.237  1.00 16.61 ? 32  PHE A CD2 1 
ATOM   290  C CE1 . PHE A 1 32  ? -19.352 20.637 80.856  1.00 17.43 ? 32  PHE A CE1 1 
ATOM   291  C CE2 . PHE A 1 32  ? -17.468 20.916 82.333  1.00 22.50 ? 32  PHE A CE2 1 
ATOM   292  C CZ  . PHE A 1 32  ? -18.854 20.824 82.137  1.00 18.30 ? 32  PHE A CZ  1 
ATOM   293  N N   . HIS A 1 33  ? -14.582 19.292 76.223  1.00 14.67 ? 33  HIS A N   1 
ATOM   294  C CA  . HIS A 1 33  ? -14.111 19.425 74.843  1.00 13.23 ? 33  HIS A CA  1 
ATOM   295  C C   . HIS A 1 33  ? -14.564 18.261 73.973  1.00 13.40 ? 33  HIS A C   1 
ATOM   296  O O   . HIS A 1 33  ? -14.707 18.433 72.754  1.00 14.77 ? 33  HIS A O   1 
ATOM   297  C CB  . HIS A 1 33  ? -12.590 19.601 74.815  1.00 13.33 ? 33  HIS A CB  1 
ATOM   298  C CG  . HIS A 1 33  ? -12.162 20.973 75.240  1.00 15.11 ? 33  HIS A CG  1 
ATOM   299  N ND1 . HIS A 1 33  ? -12.411 22.093 74.476  1.00 11.79 ? 33  HIS A ND1 1 
ATOM   300  C CD2 . HIS A 1 33  ? -11.535 21.413 76.359  1.00 11.93 ? 33  HIS A CD2 1 
ATOM   301  C CE1 . HIS A 1 33  ? -11.940 23.162 75.095  1.00 13.84 ? 33  HIS A CE1 1 
ATOM   302  N NE2 . HIS A 1 33  ? -11.403 22.777 76.239  1.00 12.37 ? 33  HIS A NE2 1 
ATOM   303  N N   . ALA A 1 34  ? -14.830 17.086 74.556  1.00 13.10 ? 34  ALA A N   1 
ATOM   304  C CA  . ALA A 1 34  ? -15.414 16.015 73.749  1.00 13.17 ? 34  ALA A CA  1 
ATOM   305  C C   . ALA A 1 34  ? -16.809 16.403 73.259  1.00 17.45 ? 34  ALA A C   1 
ATOM   306  O O   . ALA A 1 34  ? -17.123 16.240 72.070  1.00 14.48 ? 34  ALA A O   1 
ATOM   307  C CB  . ALA A 1 34  ? -15.463 14.693 74.533  1.00 13.59 ? 34  ALA A CB  1 
ATOM   308  N N   . VAL A 1 35  ? -17.649 16.947 74.152  1.00 14.35 ? 35  VAL A N   1 
ATOM   309  C CA  . VAL A 1 35  ? -19.040 17.227 73.753  1.00 13.87 ? 35  VAL A CA  1 
ATOM   310  C C   . VAL A 1 35  ? -19.114 18.476 72.892  1.00 13.23 ? 35  VAL A C   1 
ATOM   311  O O   . VAL A 1 35  ? -20.049 18.627 72.092  1.00 14.46 ? 35  VAL A O   1 
ATOM   312  C CB  . VAL A 1 35  ? -19.967 17.365 74.982  1.00 16.73 ? 35  VAL A CB  1 
ATOM   313  C CG1 . VAL A 1 35  ? -19.929 16.099 75.835  1.00 13.26 ? 35  VAL A CG1 1 
ATOM   314  C CG2 . VAL A 1 35  ? -19.597 18.577 75.825  1.00 15.77 ? 35  VAL A CG2 1 
ATOM   315  N N   . LYS A 1 36  ? -18.154 19.390 73.049  1.00 11.76 ? 36  LYS A N   1 
ATOM   316  C CA  . LYS A 1 36  ? -18.165 20.657 72.321  1.00 11.77 ? 36  LYS A CA  1 
ATOM   317  C C   . LYS A 1 36  ? -17.383 20.578 71.010  1.00 12.89 ? 36  LYS A C   1 
ATOM   318  O O   . LYS A 1 36  ? -17.824 21.124 69.989  1.00 15.73 ? 36  LYS A O   1 
ATOM   319  C CB  . LYS A 1 36  ? -17.584 21.770 73.211  1.00 14.31 ? 36  LYS A CB  1 
ATOM   320  C CG  . LYS A 1 36  ? -17.708 23.162 72.571  1.00 13.09 ? 36  LYS A CG  1 
ATOM   321  C CD  . LYS A 1 36  ? -17.428 24.303 73.536  1.00 13.76 ? 36  LYS A CD  1 
ATOM   322  C CE  . LYS A 1 36  ? -15.943 24.646 73.596  1.00 12.63 ? 36  LYS A CE  1 
ATOM   323  N NZ  . LYS A 1 36  ? -15.425 25.037 72.236  1.00 10.82 ? 36  LYS A NZ  1 
ATOM   324  N N   . ASP A 1 37  ? -16.223 19.900 71.003  1.00 12.55 ? 37  ASP A N   1 
ATOM   325  C CA  . ASP A 1 37  ? -15.299 20.030 69.866  1.00 11.24 ? 37  ASP A CA  1 
ATOM   326  C C   . ASP A 1 37  ? -14.868 18.717 69.221  1.00 14.33 ? 37  ASP A C   1 
ATOM   327  O O   . ASP A 1 37  ? -14.659 18.676 68.005  1.00 11.87 ? 37  ASP A O   1 
ATOM   328  C CB  . ASP A 1 37  ? -14.022 20.780 70.337  1.00 13.04 ? 37  ASP A CB  1 
ATOM   329  C CG  . ASP A 1 37  ? -14.347 22.047 71.078  1.00 15.81 ? 37  ASP A CG  1 
ATOM   330  O OD1 . ASP A 1 37  ? -14.877 22.965 70.432  1.00 15.23 ? 37  ASP A OD1 1 
ATOM   331  O OD2 . ASP A 1 37  ? -14.086 22.122 72.297  1.00 15.84 ? 37  ASP A OD2 1 
ATOM   332  N N   . TYR A 1 38  ? -14.626 17.664 69.999  1.00 15.15 ? 38  TYR A N   1 
ATOM   333  C CA  . TYR A 1 38  ? -13.918 16.526 69.405  1.00 11.22 ? 38  TYR A CA  1 
ATOM   334  C C   . TYR A 1 38  ? -14.788 15.724 68.437  1.00 11.55 ? 38  TYR A C   1 
ATOM   335  O O   . TYR A 1 38  ? -14.261 15.172 67.459  1.00 14.22 ? 38  TYR A O   1 
ATOM   336  C CB  . TYR A 1 38  ? -13.341 15.615 70.494  1.00 15.87 ? 38  TYR A CB  1 
ATOM   337  C CG  . TYR A 1 38  ? -12.256 16.292 71.326  1.00 13.84 ? 38  TYR A CG  1 
ATOM   338  C CD1 . TYR A 1 38  ? -11.412 17.273 70.781  1.00 13.48 ? 38  TYR A CD1 1 
ATOM   339  C CD2 . TYR A 1 38  ? -12.100 15.971 72.675  1.00 13.88 ? 38  TYR A CD2 1 
ATOM   340  C CE1 . TYR A 1 38  ? -10.408 17.868 71.549  1.00 10.31 ? 38  TYR A CE1 1 
ATOM   341  C CE2 . TYR A 1 38  ? -11.139 16.595 73.454  1.00 14.26 ? 38  TYR A CE2 1 
ATOM   342  C CZ  . TYR A 1 38  ? -10.309 17.539 72.901  1.00 11.91 ? 38  TYR A CZ  1 
ATOM   343  O OH  . TYR A 1 38  ? -9.349  18.128 73.678  1.00 13.51 ? 38  TYR A OH  1 
ATOM   344  N N   . TYR A 1 39  ? -16.098 15.641 68.668  1.00 13.26 ? 39  TYR A N   1 
ATOM   345  C CA  . TYR A 1 39  ? -16.959 15.072 67.635  1.00 12.39 ? 39  TYR A CA  1 
ATOM   346  C C   . TYR A 1 39  ? -17.263 16.103 66.556  1.00 13.85 ? 39  TYR A C   1 
ATOM   347  O O   . TYR A 1 39  ? -17.211 15.807 65.352  1.00 12.17 ? 39  TYR A O   1 
ATOM   348  C CB  . TYR A 1 39  ? -18.267 14.569 68.255  1.00 10.68 ? 39  TYR A CB  1 
ATOM   349  C CG  . TYR A 1 39  ? -19.247 14.131 67.202  1.00 17.88 ? 39  TYR A CG  1 
ATOM   350  C CD1 . TYR A 1 39  ? -19.196 12.840 66.688  1.00 16.71 ? 39  TYR A CD1 1 
ATOM   351  C CD2 . TYR A 1 39  ? -20.222 15.003 66.716  1.00 15.54 ? 39  TYR A CD2 1 
ATOM   352  C CE1 . TYR A 1 39  ? -20.087 12.424 65.710  1.00 16.93 ? 39  TYR A CE1 1 
ATOM   353  C CE2 . TYR A 1 39  ? -21.107 14.597 65.731  1.00 18.21 ? 39  TYR A CE2 1 
ATOM   354  C CZ  . TYR A 1 39  ? -21.043 13.307 65.246  1.00 19.52 ? 39  TYR A CZ  1 
ATOM   355  O OH  . TYR A 1 39  ? -21.926 12.906 64.275  1.00 17.87 ? 39  TYR A OH  1 
ATOM   356  N N   . ASP A 1 40  ? -17.551 17.323 66.978  1.00 12.67 ? 40  ASP A N   1 
ATOM   357  C CA  . ASP A 1 40  ? -18.094 18.309 66.054  1.00 11.93 ? 40  ASP A CA  1 
ATOM   358  C C   . ASP A 1 40  ? -17.088 18.817 65.035  1.00 14.94 ? 40  ASP A C   1 
ATOM   359  O O   . ASP A 1 40  ? -17.482 19.133 63.907  1.00 14.04 ? 40  ASP A O   1 
ATOM   360  C CB  . ASP A 1 40  ? -18.687 19.443 66.859  1.00 15.33 ? 40  ASP A CB  1 
ATOM   361  C CG  . ASP A 1 40  ? -20.106 19.115 67.273  1.00 17.68 ? 40  ASP A CG  1 
ATOM   362  O OD1 . ASP A 1 40  ? -20.948 19.027 66.358  1.00 16.23 ? 40  ASP A OD1 1 
ATOM   363  O OD2 . ASP A 1 40  ? -20.356 18.883 68.478  1.00 17.02 ? 40  ASP A OD2 1 
ATOM   364  N N   . MET A 1 41  ? -15.795 18.891 65.385  1.00 15.04 ? 41  MET A N   1 
ATOM   365  C CA  . MET A 1 41  ? -14.832 19.425 64.422  1.00 11.69 ? 41  MET A CA  1 
ATOM   366  C C   . MET A 1 41  ? -14.688 18.523 63.209  1.00 13.87 ? 41  MET A C   1 
ATOM   367  O O   . MET A 1 41  ? -14.771 19.037 62.075  1.00 14.10 ? 41  MET A O   1 
ATOM   368  C CB  . MET A 1 41  ? -13.489 19.691 65.116  1.00 10.63 ? 41  MET A CB  1 
ATOM   369  C CG  . MET A 1 41  ? -13.520 20.979 65.949  1.00 13.47 ? 41  MET A CG  1 
ATOM   370  S SD  . MET A 1 41  ? -13.563 22.477 64.948  1.00 13.96 ? 41  MET A SD  1 
ATOM   371  C CE  . MET A 1 41  ? -11.846 22.595 64.407  1.00 14.63 ? 41  MET A CE  1 
ATOM   372  N N   . PRO A 1 42  ? -14.518 17.201 63.341  1.00 11.32 ? 42  PRO A N   1 
ATOM   373  C CA  . PRO A 1 42  ? -14.538 16.364 62.125  1.00 13.38 ? 42  PRO A CA  1 
ATOM   374  C C   . PRO A 1 42  ? -15.936 16.211 61.537  1.00 13.34 ? 42  PRO A C   1 
ATOM   375  O O   . PRO A 1 42  ? -16.054 15.937 60.334  1.00 13.18 ? 42  PRO A O   1 
ATOM   376  C CB  . PRO A 1 42  ? -13.963 15.025 62.594  1.00 12.38 ? 42  PRO A CB  1 
ATOM   377  C CG  . PRO A 1 42  ? -14.253 14.999 64.093  1.00 13.23 ? 42  PRO A CG  1 
ATOM   378  C CD  . PRO A 1 42  ? -14.114 16.430 64.531  1.00 14.33 ? 42  PRO A CD  1 
ATOM   379  N N   . ALA A 1 43  ? -17.004 16.425 62.329  1.00 14.49 ? 43  ALA A N   1 
ATOM   380  C CA  . ALA A 1 43  ? -18.370 16.302 61.797  1.00 12.76 ? 43  ALA A CA  1 
ATOM   381  C C   . ALA A 1 43  ? -18.716 17.383 60.778  1.00 16.63 ? 43  ALA A C   1 
ATOM   382  O O   . ALA A 1 43  ? -19.652 17.192 59.988  1.00 14.98 ? 43  ALA A O   1 
ATOM   383  C CB  . ALA A 1 43  ? -19.395 16.346 62.942  1.00 14.15 ? 43  ALA A CB  1 
ATOM   384  N N   . TYR A 1 44  ? -18.012 18.516 60.785  1.00 15.43 ? 44  TYR A N   1 
ATOM   385  C CA  . TYR A 1 44  ? -18.194 19.491 59.712  1.00 15.26 ? 44  TYR A CA  1 
ATOM   386  C C   . TYR A 1 44  ? -18.016 18.847 58.341  1.00 13.88 ? 44  TYR A C   1 
ATOM   387  O O   . TYR A 1 44  ? -18.584 19.326 57.351  1.00 15.16 ? 44  TYR A O   1 
ATOM   388  C CB  . TYR A 1 44  ? -17.178 20.638 59.849  1.00 10.43 ? 44  TYR A CB  1 
ATOM   389  C CG  . TYR A 1 44  ? -17.540 21.720 60.854  1.00 12.36 ? 44  TYR A CG  1 
ATOM   390  C CD1 . TYR A 1 44  ? -18.391 22.758 60.508  1.00 19.76 ? 44  TYR A CD1 1 
ATOM   391  C CD2 . TYR A 1 44  ? -17.030 21.685 62.144  1.00 12.82 ? 44  TYR A CD2 1 
ATOM   392  C CE1 . TYR A 1 44  ? -18.722 23.742 61.428  1.00 17.62 ? 44  TYR A CE1 1 
ATOM   393  C CE2 . TYR A 1 44  ? -17.329 22.665 63.059  1.00 12.19 ? 44  TYR A CE2 1 
ATOM   394  C CZ  . TYR A 1 44  ? -18.183 23.693 62.702  1.00 16.74 ? 44  TYR A CZ  1 
ATOM   395  O OH  . TYR A 1 44  ? -18.501 24.673 63.631  1.00 16.69 ? 44  TYR A OH  1 
ATOM   396  N N   . LEU A 1 45  ? -17.205 17.787 58.254  1.00 11.50 ? 45  LEU A N   1 
ATOM   397  C CA  . LEU A 1 45  ? -16.942 17.174 56.952  1.00 14.94 ? 45  LEU A CA  1 
ATOM   398  C C   . LEU A 1 45  ? -18.159 16.439 56.395  1.00 20.46 ? 45  LEU A C   1 
ATOM   399  O O   . LEU A 1 45  ? -18.176 16.087 55.206  1.00 19.59 ? 45  LEU A O   1 
ATOM   400  C CB  . LEU A 1 45  ? -15.745 16.223 57.046  1.00 14.47 ? 45  LEU A CB  1 
ATOM   401  C CG  . LEU A 1 45  ? -14.387 16.860 57.369  1.00 15.10 ? 45  LEU A CG  1 
ATOM   402  C CD1 . LEU A 1 45  ? -13.351 15.818 57.736  1.00 15.46 ? 45  LEU A CD1 1 
ATOM   403  C CD2 . LEU A 1 45  ? -13.891 17.676 56.162  1.00 15.53 ? 45  LEU A CD2 1 
ATOM   404  N N   . LYS A 1 46  ? -19.181 16.195 57.216  1.00 18.76 ? 46  LYS A N   1 
ATOM   405  C CA  . LYS A 1 46  ? -20.418 15.637 56.683  1.00 16.86 ? 46  LYS A CA  1 
ATOM   406  C C   . LYS A 1 46  ? -21.208 16.652 55.853  1.00 18.71 ? 46  LYS A C   1 
ATOM   407  O O   . LYS A 1 46  ? -22.033 16.253 55.024  1.00 22.76 ? 46  LYS A O   1 
ATOM   408  C CB  . LYS A 1 46  ? -21.272 15.094 57.830  1.00 21.29 ? 46  LYS A CB  1 
ATOM   409  C CG  . LYS A 1 46  ? -20.472 14.191 58.739  1.00 27.47 ? 46  LYS A CG  1 
ATOM   410  C CD  . LYS A 1 46  ? -21.345 13.246 59.522  1.00 42.40 ? 46  LYS A CD  1 
ATOM   411  C CE  . LYS A 1 46  ? -22.212 13.993 60.511  1.00 49.62 ? 46  LYS A CE  1 
ATOM   412  N NZ  . LYS A 1 46  ? -23.468 13.241 60.796  1.00 60.27 ? 46  LYS A NZ  1 
ATOM   413  N N   . ASP A 1 47  ? -20.978 17.950 56.060  1.00 20.47 ? 47  ASP A N   1 
ATOM   414  C CA  . ASP A 1 47  ? -21.792 18.987 55.444  1.00 17.25 ? 47  ASP A CA  1 
ATOM   415  C C   . ASP A 1 47  ? -21.032 19.830 54.438  1.00 24.52 ? 47  ASP A C   1 
ATOM   416  O O   . ASP A 1 47  ? -21.666 20.547 53.651  1.00 23.27 ? 47  ASP A O   1 
ATOM   417  C CB  . ASP A 1 47  ? -22.365 19.920 56.521  1.00 16.70 ? 47  ASP A CB  1 
ATOM   418  C CG  . ASP A 1 47  ? -23.282 19.193 57.488  1.00 31.42 ? 47  ASP A CG  1 
ATOM   419  O OD1 . ASP A 1 47  ? -23.954 18.231 57.054  1.00 31.64 ? 47  ASP A OD1 1 
ATOM   420  O OD2 . ASP A 1 47  ? -23.346 19.594 58.667  1.00 38.33 ? 47  ASP A OD2 1 
ATOM   421  N N   . PHE A 1 48  ? -19.701 19.762 54.444  1.00 15.75 ? 48  PHE A N   1 
ATOM   422  C CA  . PHE A 1 48  ? -18.855 20.598 53.607  1.00 16.24 ? 48  PHE A CA  1 
ATOM   423  C C   . PHE A 1 48  ? -17.871 19.718 52.864  1.00 20.38 ? 48  PHE A C   1 
ATOM   424  O O   . PHE A 1 48  ? -17.242 18.838 53.460  1.00 21.68 ? 48  PHE A O   1 
ATOM   425  C CB  . PHE A 1 48  ? -18.127 21.641 54.461  1.00 19.76 ? 48  PHE A CB  1 
ATOM   426  C CG  . PHE A 1 48  ? -19.069 22.567 55.155  1.00 20.51 ? 48  PHE A CG  1 
ATOM   427  C CD1 . PHE A 1 48  ? -19.676 23.593 54.444  1.00 19.17 ? 48  PHE A CD1 1 
ATOM   428  C CD2 . PHE A 1 48  ? -19.416 22.373 56.476  1.00 20.70 ? 48  PHE A CD2 1 
ATOM   429  C CE1 . PHE A 1 48  ? -20.572 24.437 55.051  1.00 23.02 ? 48  PHE A CE1 1 
ATOM   430  C CE2 . PHE A 1 48  ? -20.327 23.220 57.098  1.00 19.22 ? 48  PHE A CE2 1 
ATOM   431  C CZ  . PHE A 1 48  ? -20.899 24.249 56.388  1.00 21.45 ? 48  PHE A CZ  1 
ATOM   432  N N   . GLU A 1 49  ? -17.762 19.958 51.564  1.00 20.59 ? 49  GLU A N   1 
ATOM   433  C CA  . GLU A 1 49  ? -16.992 19.122 50.650  1.00 17.38 ? 49  GLU A CA  1 
ATOM   434  C C   . GLU A 1 49  ? -15.571 19.669 50.532  1.00 21.27 ? 49  GLU A C   1 
ATOM   435  O O   . GLU A 1 49  ? -15.119 20.100 49.478  1.00 24.16 ? 49  GLU A O   1 
ATOM   436  C CB  . GLU A 1 49  ? -17.687 19.065 49.294  1.00 22.26 ? 49  GLU A CB  1 
ATOM   437  C CG  . GLU A 1 49  ? -19.051 18.340 49.314  1.00 32.18 ? 49  GLU A CG  1 
ATOM   438  C CD  . GLU A 1 49  ? -20.114 19.017 50.204  1.00 45.28 ? 49  GLU A CD  1 
ATOM   439  O OE1 . GLU A 1 49  ? -20.755 18.312 51.025  1.00 41.80 ? 49  GLU A OE1 1 
ATOM   440  O OE2 . GLU A 1 49  ? -20.298 20.255 50.088  1.00 44.20 ? 49  GLU A OE2 1 
ATOM   441  N N   . ILE A 1 50  ? -14.896 19.683 51.674  1.00 16.78 ? 50  ILE A N   1 
ATOM   442  C CA  . ILE A 1 50  ? -13.497 20.074 51.794  1.00 20.67 ? 50  ILE A CA  1 
ATOM   443  C C   . ILE A 1 50  ? -12.764 18.941 52.497  1.00 16.36 ? 50  ILE A C   1 
ATOM   444  O O   . ILE A 1 50  ? -13.375 17.991 52.981  1.00 20.77 ? 50  ILE A O   1 
ATOM   445  C CB  . ILE A 1 50  ? -13.331 21.398 52.566  1.00 20.98 ? 50  ILE A CB  1 
ATOM   446  C CG1 . ILE A 1 50  ? -14.086 21.311 53.899  1.00 23.45 ? 50  ILE A CG1 1 
ATOM   447  C CG2 . ILE A 1 50  ? -13.911 22.549 51.753  1.00 20.62 ? 50  ILE A CG2 1 
ATOM   448  C CD1 . ILE A 1 50  ? -13.649 22.283 54.937  1.00 26.70 ? 50  ILE A CD1 1 
ATOM   449  N N   . LYS A 1 51  ? -11.437 19.046 52.534  1.00 19.44 ? 51  LYS A N   1 
ATOM   450  C CA  . LYS A 1 51  ? -10.586 18.161 53.313  1.00 14.26 ? 51  LYS A CA  1 
ATOM   451  C C   . LYS A 1 51  ? -10.175 18.887 54.585  1.00 11.50 ? 51  LYS A C   1 
ATOM   452  O O   . LYS A 1 51  ? -9.854  20.078 54.542  1.00 16.98 ? 51  LYS A O   1 
ATOM   453  C CB  . LYS A 1 51  ? -9.320  17.760 52.524  1.00 14.41 ? 51  LYS A CB  1 
ATOM   454  C CG  . LYS A 1 51  ? -9.560  17.166 51.129  1.00 19.64 ? 51  LYS A CG  1 
ATOM   455  C CD  . LYS A 1 51  ? -10.450 15.931 51.201  1.00 21.44 ? 51  LYS A CD  1 
ATOM   456  C CE  . LYS A 1 51  ? -10.543 15.222 49.841  1.00 27.69 ? 51  LYS A CE  1 
ATOM   457  N NZ  . LYS A 1 51  ? -11.125 16.111 48.805  1.00 36.17 ? 51  LYS A NZ  1 
ATOM   458  N N   . LEU A 1 52  ? -10.201 18.177 55.717  1.00 10.47 ? 52  LEU A N   1 
ATOM   459  C CA  . LEU A 1 52  ? -9.676  18.688 56.981  1.00 11.07 ? 52  LEU A CA  1 
ATOM   460  C C   . LEU A 1 52  ? -8.925  17.561 57.663  1.00 13.01 ? 52  LEU A C   1 
ATOM   461  O O   . LEU A 1 52  ? -9.408  16.423 57.658  1.00 16.51 ? 52  LEU A O   1 
ATOM   462  C CB  . LEU A 1 52  ? -10.779 19.148 57.940  1.00 13.53 ? 52  LEU A CB  1 
ATOM   463  C CG  . LEU A 1 52  ? -11.697 20.282 57.466  1.00 17.98 ? 52  LEU A CG  1 
ATOM   464  C CD1 . LEU A 1 52  ? -12.909 20.412 58.430  1.00 13.87 ? 52  LEU A CD1 1 
ATOM   465  C CD2 . LEU A 1 52  ? -10.922 21.590 57.362  1.00 16.07 ? 52  LEU A CD2 1 
ATOM   466  N N   . ASN A 1 53  ? -7.796  17.879 58.309  1.00 11.92 ? 53  ASN A N   1 
ATOM   467  C CA  . ASN A 1 53  ? -6.969  16.856 58.951  1.00 10.29 ? 53  ASN A CA  1 
ATOM   468  C C   . ASN A 1 53  ? -6.934  17.075 60.455  1.00 11.19 ? 53  ASN A C   1 
ATOM   469  O O   . ASN A 1 53  ? -7.112  18.195 60.946  1.00 14.99 ? 53  ASN A O   1 
ATOM   470  C CB  . ASN A 1 53  ? -5.558  16.865 58.388  1.00 15.10 ? 53  ASN A CB  1 
ATOM   471  C CG  . ASN A 1 53  ? -5.549  16.804 56.879  1.00 12.96 ? 53  ASN A CG  1 
ATOM   472  O OD1 . ASN A 1 53  ? -5.809  15.762 56.283  1.00 15.19 ? 53  ASN A OD1 1 
ATOM   473  N ND2 . ASN A 1 53  ? -5.302  17.950 56.248  1.00 12.05 ? 53  ASN A ND2 1 
ATOM   474  N N   . PHE A 1 54  ? -6.630  16.000 61.184  1.00 12.64 ? 54  PHE A N   1 
ATOM   475  C CA  . PHE A 1 54  ? -6.733  16.028 62.639  1.00 13.31 ? 54  PHE A CA  1 
ATOM   476  C C   . PHE A 1 54  ? -5.565  15.286 63.270  1.00 13.60 ? 54  PHE A C   1 
ATOM   477  O O   . PHE A 1 54  ? -5.170  14.227 62.784  1.00 14.14 ? 54  PHE A O   1 
ATOM   478  C CB  . PHE A 1 54  ? -8.070  15.392 63.077  1.00 12.66 ? 54  PHE A CB  1 
ATOM   479  C CG  . PHE A 1 54  ? -9.274  16.133 62.550  1.00 12.78 ? 54  PHE A CG  1 
ATOM   480  C CD1 . PHE A 1 54  ? -9.790  17.225 63.246  1.00 17.62 ? 54  PHE A CD1 1 
ATOM   481  C CD2 . PHE A 1 54  ? -9.859  15.774 61.347  1.00 10.49 ? 54  PHE A CD2 1 
ATOM   482  C CE1 . PHE A 1 54  ? -10.885 17.934 62.751  1.00 16.78 ? 54  PHE A CE1 1 
ATOM   483  C CE2 . PHE A 1 54  ? -10.950 16.478 60.842  1.00 18.46 ? 54  PHE A CE2 1 
ATOM   484  C CZ  . PHE A 1 54  ? -11.455 17.552 61.539  1.00 16.09 ? 54  PHE A CZ  1 
ATOM   485  N N   . ASN A 1 55  ? -5.032  15.841 64.366  1.00 10.57 ? 55  ASN A N   1 
ATOM   486  C CA  . ASN A 1 55  ? -4.122  15.116 65.241  1.00 9.83  ? 55  ASN A CA  1 
ATOM   487  C C   . ASN A 1 55  ? -4.876  14.715 66.507  1.00 10.52 ? 55  ASN A C   1 
ATOM   488  O O   . ASN A 1 55  ? -5.603  15.530 67.071  1.00 13.95 ? 55  ASN A O   1 
ATOM   489  C CB  . ASN A 1 55  ? -2.924  15.974 65.626  1.00 11.65 ? 55  ASN A CB  1 
ATOM   490  C CG  . ASN A 1 55  ? -1.893  15.168 66.379  1.00 13.57 ? 55  ASN A CG  1 
ATOM   491  O OD1 . ASN A 1 55  ? -1.353  14.229 65.822  1.00 14.97 ? 55  ASN A OD1 1 
ATOM   492  N ND2 . ASN A 1 55  ? -1.665  15.485 67.669  1.00 12.13 ? 55  ASN A ND2 1 
ATOM   493  N N   . LEU A 1 56  ? -4.747  13.457 66.914  1.00 12.87 ? 56  LEU A N   1 
ATOM   494  C CA  . LEU A 1 56  ? -5.304  12.973 68.178  1.00 9.36  ? 56  LEU A CA  1 
ATOM   495  C C   . LEU A 1 56  ? -4.149  12.408 68.989  1.00 14.13 ? 56  LEU A C   1 
ATOM   496  O O   . LEU A 1 56  ? -3.516  11.440 68.557  1.00 15.01 ? 56  LEU A O   1 
ATOM   497  C CB  . LEU A 1 56  ? -6.328  11.877 67.957  1.00 9.60  ? 56  LEU A CB  1 
ATOM   498  C CG  . LEU A 1 56  ? -7.625  12.258 67.230  1.00 16.92 ? 56  LEU A CG  1 
ATOM   499  C CD1 . LEU A 1 56  ? -8.428  10.996 66.968  1.00 19.23 ? 56  LEU A CD1 1 
ATOM   500  C CD2 . LEU A 1 56  ? -8.446  13.243 68.068  1.00 16.30 ? 56  LEU A CD2 1 
ATOM   501  N N   . THR A 1 57  ? -3.896  12.971 70.164  1.00 15.00 ? 57  THR A N   1 
ATOM   502  C CA  . THR A 1 57  ? -2.865  12.364 70.992  1.00 12.98 ? 57  THR A CA  1 
ATOM   503  C C   . THR A 1 57  ? -3.393  11.068 71.619  1.00 12.56 ? 57  THR A C   1 
ATOM   504  O O   . THR A 1 57  ? -4.592  10.921 71.865  1.00 12.53 ? 57  THR A O   1 
ATOM   505  C CB  . THR A 1 57  ? -2.377  13.316 72.090  1.00 12.85 ? 57  THR A CB  1 
ATOM   506  O OG1 . THR A 1 57  ? -3.427  13.552 73.041  1.00 10.80 ? 57  THR A OG1 1 
ATOM   507  C CG2 . THR A 1 57  ? -1.893  14.636 71.520  1.00 11.47 ? 57  THR A CG2 1 
ATOM   508  N N   . PRO A 1 58  ? -2.523  10.086 71.830  1.00 13.40 ? 58  PRO A N   1 
ATOM   509  C CA  . PRO A 1 58  ? -3.002  8.813  72.383  1.00 14.28 ? 58  PRO A CA  1 
ATOM   510  C C   . PRO A 1 58  ? -3.592  8.946  73.775  1.00 12.94 ? 58  PRO A C   1 
ATOM   511  O O   . PRO A 1 58  ? -4.559  8.243  74.088  1.00 13.01 ? 58  PRO A O   1 
ATOM   512  C CB  . PRO A 1 58  ? -1.751  7.932  72.371  1.00 12.17 ? 58  PRO A CB  1 
ATOM   513  C CG  . PRO A 1 58  ? -0.947  8.480  71.216  1.00 13.41 ? 58  PRO A CG  1 
ATOM   514  C CD  . PRO A 1 58  ? -1.151  9.983  71.298  1.00 15.14 ? 58  PRO A CD  1 
ATOM   515  N N   . VAL A 1 59  ? -3.054  9.833  74.616  1.00 10.15 ? 59  VAL A N   1 
ATOM   516  C CA  . VAL A 1 59  ? -3.636  9.993  75.950  1.00 13.06 ? 59  VAL A CA  1 
ATOM   517  C C   . VAL A 1 59  ? -5.043  10.607 75.869  1.00 14.33 ? 59  VAL A C   1 
ATOM   518  O O   . VAL A 1 59  ? -5.921  10.279 76.684  1.00 12.52 ? 59  VAL A O   1 
ATOM   519  C CB  . VAL A 1 59  ? -2.665  10.796 76.846  1.00 14.30 ? 59  VAL A CB  1 
ATOM   520  C CG1 . VAL A 1 59  ? -2.294  12.153 76.236  1.00 14.73 ? 59  VAL A CG1 1 
ATOM   521  C CG2 . VAL A 1 59  ? -3.244  10.985 78.297  1.00 11.98 ? 59  VAL A CG2 1 
ATOM   522  N N   . LEU A 1 60  ? -5.302  11.467 74.885  1.00 12.44 ? 60  LEU A N   1 
ATOM   523  C CA  . LEU A 1 60  ? -6.676  11.914 74.660  1.00 13.47 ? 60  LEU A CA  1 
ATOM   524  C C   . LEU A 1 60  ? -7.572  10.756 74.234  1.00 16.19 ? 60  LEU A C   1 
ATOM   525  O O   . LEU A 1 60  ? -8.677  10.600 74.762  1.00 13.22 ? 60  LEU A O   1 
ATOM   526  C CB  . LEU A 1 60  ? -6.730  13.032 73.618  1.00 15.06 ? 60  LEU A CB  1 
ATOM   527  C CG  . LEU A 1 60  ? -8.146  13.456 73.202  1.00 15.89 ? 60  LEU A CG  1 
ATOM   528  C CD1 . LEU A 1 60  ? -8.933  13.975 74.394  1.00 20.43 ? 60  LEU A CD1 1 
ATOM   529  C CD2 . LEU A 1 60  ? -8.115  14.516 72.085  1.00 14.21 ? 60  LEU A CD2 1 
ATOM   530  N N   . ILE A 1 61  ? -7.123  9.949  73.262  1.00 14.26 ? 61  ILE A N   1 
ATOM   531  C CA  . ILE A 1 61  ? -7.915  8.794  72.834  1.00 9.68  ? 61  ILE A CA  1 
ATOM   532  C C   . ILE A 1 61  ? -8.271  7.912  74.025  1.00 13.90 ? 61  ILE A C   1 
ATOM   533  O O   . ILE A 1 61  ? -9.404  7.423  74.126  1.00 15.28 ? 61  ILE A O   1 
ATOM   534  C CB  . ILE A 1 61  ? -7.167  7.987  71.757  1.00 12.67 ? 61  ILE A CB  1 
ATOM   535  C CG1 . ILE A 1 61  ? -6.981  8.831  70.492  1.00 15.86 ? 61  ILE A CG1 1 
ATOM   536  C CG2 . ILE A 1 61  ? -7.925  6.678  71.446  1.00 16.21 ? 61  ILE A CG2 1 
ATOM   537  C CD1 . ILE A 1 61  ? -6.113  8.142  69.438  1.00 13.14 ? 61  ILE A CD1 1 
ATOM   538  N N   . ASP A 1 62  ? -7.303  7.685  74.938  1.00 13.63 ? 62  ASP A N   1 
ATOM   539  C CA  . ASP A 1 62  ? -7.557  6.822  76.093  1.00 15.59 ? 62  ASP A CA  1 
ATOM   540  C C   . ASP A 1 62  ? -8.733  7.337  76.902  1.00 13.64 ? 62  ASP A C   1 
ATOM   541  O O   . ASP A 1 62  ? -9.582  6.559  77.355  1.00 14.65 ? 62  ASP A O   1 
ATOM   542  C CB  . ASP A 1 62  ? -6.337  6.750  77.006  1.00 16.65 ? 62  ASP A CB  1 
ATOM   543  C CG  . ASP A 1 62  ? -5.298  5.753  76.528  1.00 22.26 ? 62  ASP A CG  1 
ATOM   544  O OD1 . ASP A 1 62  ? -5.673  4.851  75.752  1.00 23.95 ? 62  ASP A OD1 1 
ATOM   545  O OD2 . ASP A 1 62  ? -4.109  5.861  76.943  1.00 22.97 ? 62  ASP A OD2 1 
ATOM   546  N N   . GLN A 1 63  ? -8.765  8.653  77.122  1.00 14.37 ? 63  GLN A N   1 
ATOM   547  C CA  . GLN A 1 63  ? -9.809  9.246  77.942  1.00 12.31 ? 63  GLN A CA  1 
ATOM   548  C C   . GLN A 1 63  ? -11.143 9.265  77.210  1.00 13.90 ? 63  GLN A C   1 
ATOM   549  O O   . GLN A 1 63  ? -12.185 9.032  77.822  1.00 17.93 ? 63  GLN A O   1 
ATOM   550  C CB  . GLN A 1 63  ? -9.401  10.663 78.356  1.00 11.52 ? 63  GLN A CB  1 
ATOM   551  C CG  . GLN A 1 63  ? -8.122  10.723 79.182  1.00 15.04 ? 63  GLN A CG  1 
ATOM   552  C CD  . GLN A 1 63  ? -7.709  12.162 79.429  1.00 17.05 ? 63  GLN A CD  1 
ATOM   553  O OE1 . GLN A 1 63  ? -8.313  12.856 80.246  1.00 19.32 ? 63  GLN A OE1 1 
ATOM   554  N NE2 . GLN A 1 63  ? -6.702  12.628 78.693  1.00 14.20 ? 63  GLN A NE2 1 
ATOM   555  N N   . ILE A 1 64  ? -11.143 9.567  75.909  1.00 13.57 ? 64  ILE A N   1 
ATOM   556  C CA  . ILE A 1 64  ? -12.404 9.504  75.170  1.00 11.75 ? 64  ILE A CA  1 
ATOM   557  C C   . ILE A 1 64  ? -13.004 8.104  75.281  1.00 14.38 ? 64  ILE A C   1 
ATOM   558  O O   . ILE A 1 64  ? -14.209 7.945  75.536  1.00 15.04 ? 64  ILE A O   1 
ATOM   559  C CB  . ILE A 1 64  ? -12.202 9.940  73.703  1.00 11.06 ? 64  ILE A CB  1 
ATOM   560  C CG1 . ILE A 1 64  ? -11.839 11.422 73.648  1.00 13.18 ? 64  ILE A CG1 1 
ATOM   561  C CG2 . ILE A 1 64  ? -13.501 9.621  72.834  1.00 13.01 ? 64  ILE A CG2 1 
ATOM   562  C CD1 . ILE A 1 64  ? -11.497 11.958 72.257  1.00 17.05 ? 64  ILE A CD1 1 
ATOM   563  N N   . GLN A 1 65  ? -12.159 7.070  75.177  1.00 15.77 ? 65  GLN A N   1 
ATOM   564  C CA  . GLN A 1 65  ? -12.645 5.700  75.316  1.00 15.29 ? 65  GLN A CA  1 
ATOM   565  C C   . GLN A 1 65  ? -13.272 5.449  76.689  1.00 15.60 ? 65  GLN A C   1 
ATOM   566  O O   . GLN A 1 65  ? -14.306 4.783  76.787  1.00 16.11 ? 65  GLN A O   1 
ATOM   567  C CB  . GLN A 1 65  ? -11.515 4.706  75.092  1.00 18.68 ? 65  GLN A CB  1 
ATOM   568  C CG  . GLN A 1 65  ? -11.055 4.570  73.650  1.00 17.31 ? 65  GLN A CG  1 
ATOM   569  C CD  . GLN A 1 65  ? -9.920  3.574  73.547  1.00 23.62 ? 65  GLN A CD  1 
ATOM   570  O OE1 . GLN A 1 65  ? -8.852  3.772  74.131  1.00 28.05 ? 65  GLN A OE1 1 
ATOM   571  N NE2 . GLN A 1 65  ? -10.156 2.480  72.841  1.00 25.81 ? 65  GLN A NE2 1 
ATOM   572  N N   . GLU A 1 66  ? -12.650 5.953  77.761  1.00 16.03 ? 66  GLU A N   1 
ATOM   573  C CA  . GLU A 1 66  ? -13.196 5.715  79.095  1.00 16.74 ? 66  GLU A CA  1 
ATOM   574  C C   . GLU A 1 66  ? -14.529 6.433  79.275  1.00 13.90 ? 66  GLU A C   1 
ATOM   575  O O   . GLU A 1 66  ? -15.468 5.863  79.843  1.00 19.41 ? 66  GLU A O   1 
ATOM   576  C CB  . GLU A 1 66  ? -12.178 6.135  80.175  1.00 22.87 ? 66  GLU A CB  1 
ATOM   577  C CG  . GLU A 1 66  ? -12.518 5.635  81.607  1.00 41.93 ? 66  GLU A CG  1 
ATOM   578  C CD  . GLU A 1 66  ? -11.335 5.679  82.596  1.00 36.70 ? 66  GLU A CD  1 
ATOM   579  O OE1 . GLU A 1 66  ? -11.513 5.266  83.781  1.00 41.51 ? 66  GLU A OE1 1 
ATOM   580  O OE2 . GLU A 1 66  ? -10.242 6.130  82.208  1.00 24.87 ? 66  GLU A OE2 1 
ATOM   581  N N   . TYR A 1 67  ? -14.646 7.675  78.793  1.00 13.80 ? 67  TYR A N   1 
ATOM   582  C CA  . TYR A 1 67  ? -15.938 8.353  78.882  1.00 17.40 ? 67  TYR A CA  1 
ATOM   583  C C   . TYR A 1 67  ? -16.998 7.622  78.060  1.00 19.77 ? 67  TYR A C   1 
ATOM   584  O O   . TYR A 1 67  ? -18.123 7.417  78.519  1.00 20.81 ? 67  TYR A O   1 
ATOM   585  C CB  . TYR A 1 67  ? -15.819 9.802  78.421  1.00 14.49 ? 67  TYR A CB  1 
ATOM   586  C CG  . TYR A 1 67  ? -15.361 10.748 79.495  1.00 13.46 ? 67  TYR A CG  1 
ATOM   587  C CD1 . TYR A 1 67  ? -16.265 11.274 80.426  1.00 16.95 ? 67  TYR A CD1 1 
ATOM   588  C CD2 . TYR A 1 67  ? -14.023 11.101 79.601  1.00 13.13 ? 67  TYR A CD2 1 
ATOM   589  C CE1 . TYR A 1 67  ? -15.825 12.146 81.431  1.00 14.81 ? 67  TYR A CE1 1 
ATOM   590  C CE2 . TYR A 1 67  ? -13.580 11.967 80.586  1.00 16.70 ? 67  TYR A CE2 1 
ATOM   591  C CZ  . TYR A 1 67  ? -14.486 12.481 81.497  1.00 17.19 ? 67  TYR A CZ  1 
ATOM   592  O OH  . TYR A 1 67  ? -14.021 13.348 82.470  1.00 17.08 ? 67  TYR A OH  1 
ATOM   593  N N   . ALA A 1 68  ? -16.653 7.225  76.832  1.00 19.50 ? 68  ALA A N   1 
ATOM   594  C CA  . ALA A 1 68  ? -17.616 6.529  75.979  1.00 19.04 ? 68  ALA A CA  1 
ATOM   595  C C   . ALA A 1 68  ? -18.086 5.223  76.594  1.00 20.87 ? 68  ALA A C   1 
ATOM   596  O O   . ALA A 1 68  ? -19.245 4.826  76.410  1.00 23.96 ? 68  ALA A O   1 
ATOM   597  C CB  . ALA A 1 68  ? -16.993 6.266  74.607  1.00 21.88 ? 68  ALA A CB  1 
ATOM   598  N N   . GLN A 1 69  ? -17.205 4.536  77.307  1.00 20.49 ? 69  GLN A N   1 
ATOM   599  C CA  . GLN A 1 69  ? -17.496 3.243  77.895  1.00 24.65 ? 69  GLN A CA  1 
ATOM   600  C C   . GLN A 1 69  ? -18.216 3.380  79.224  1.00 27.07 ? 69  GLN A C   1 
ATOM   601  O O   . GLN A 1 69  ? -18.638 2.369  79.795  1.00 24.45 ? 69  GLN A O   1 
ATOM   602  C CB  . GLN A 1 69  ? -16.187 2.441  78.039  1.00 24.13 ? 69  GLN A CB  1 
ATOM   603  C CG  . GLN A 1 69  ? -15.644 1.901  76.696  1.00 31.89 ? 69  GLN A CG  1 
ATOM   604  C CD  . GLN A 1 69  ? -14.122 1.649  76.683  1.00 40.68 ? 69  GLN A CD  1 
ATOM   605  O OE1 . GLN A 1 69  ? -13.493 1.508  77.728  1.00 43.28 ? 69  GLN A OE1 1 
ATOM   606  N NE2 . GLN A 1 69  ? -13.534 1.608  75.481  1.00 34.35 ? 69  GLN A NE2 1 
ATOM   607  N N   . GLY A 1 70  ? -18.399 4.609  79.701  1.00 24.02 ? 70  GLY A N   1 
ATOM   608  C CA  . GLY A 1 70  ? -19.054 4.831  80.967  1.00 28.30 ? 70  GLY A CA  1 
ATOM   609  C C   . GLY A 1 70  ? -18.222 4.497  82.183  1.00 28.21 ? 70  GLY A C   1 
ATOM   610  O O   . GLY A 1 70  ? -18.784 4.268  83.250  1.00 30.48 ? 70  GLY A O   1 
ATOM   611  N N   . LYS A 1 71  ? -16.895 4.464  82.069  1.00 25.72 ? 71  LYS A N   1 
ATOM   612  C CA  . LYS A 1 71  ? -16.067 4.159  83.227  1.00 31.94 ? 71  LYS A CA  1 
ATOM   613  C C   . LYS A 1 71  ? -15.341 5.366  83.806  1.00 32.60 ? 71  LYS A C   1 
ATOM   614  O O   . LYS A 1 71  ? -14.694 5.231  84.850  1.00 30.28 ? 71  LYS A O   1 
ATOM   615  C CB  . LYS A 1 71  ? -15.063 3.052  82.900  1.00 37.38 ? 71  LYS A CB  1 
ATOM   616  C CG  . LYS A 1 71  ? -14.633 3.003  81.475  1.00 46.95 ? 71  LYS A CG  1 
ATOM   617  C CD  . LYS A 1 71  ? -14.078 1.636  81.134  1.00 47.31 ? 71  LYS A CD  1 
ATOM   618  C CE  . LYS A 1 71  ? -13.162 1.116  82.216  1.00 55.11 ? 71  LYS A CE  1 
ATOM   619  N NZ  . LYS A 1 71  ? -12.614 -0.210 81.826  1.00 61.95 ? 71  LYS A NZ  1 
ATOM   620  N N   . ALA A 1 72  ? -15.451 6.544  83.200  1.00 23.75 ? 72  ALA A N   1 
ATOM   621  C CA  . ALA A 1 72  ? -14.794 7.718  83.769  1.00 23.53 ? 72  ALA A CA  1 
ATOM   622  C C   . ALA A 1 72  ? -15.601 8.227  84.962  1.00 25.78 ? 72  ALA A C   1 
ATOM   623  O O   . ALA A 1 72  ? -16.788 8.550  84.829  1.00 28.04 ? 72  ALA A O   1 
ATOM   624  C CB  . ALA A 1 72  ? -14.625 8.808  82.711  1.00 23.55 ? 72  ALA A CB  1 
ATOM   625  N N   . LYS A 1 73  ? -14.957 8.288  86.132  1.00 18.34 ? 73  LYS A N   1 
ATOM   626  C CA  . LYS A 1 73  ? -15.545 8.880  87.338  1.00 16.30 ? 73  LYS A CA  1 
ATOM   627  C C   . LYS A 1 73  ? -15.112 10.342 87.393  1.00 24.82 ? 73  LYS A C   1 
ATOM   628  O O   . LYS A 1 73  ? -14.048 10.675 87.913  1.00 26.76 ? 73  LYS A O   1 
ATOM   629  C CB  . LYS A 1 73  ? -15.090 8.112  88.578  1.00 21.33 ? 73  LYS A CB  1 
ATOM   630  C CG  . LYS A 1 73  ? -15.436 6.632  88.515  1.00 36.86 ? 73  LYS A CG  1 
ATOM   631  C CD  . LYS A 1 73  ? -14.632 5.780  89.513  1.00 48.59 ? 73  LYS A CD  1 
ATOM   632  C CE  . LYS A 1 73  ? -13.358 5.192  88.886  1.00 52.51 ? 73  LYS A CE  1 
ATOM   633  N NZ  . LYS A 1 73  ? -13.617 4.529  87.572  1.00 52.28 ? 73  LYS A NZ  1 
ATOM   634  N N   . ASP A 1 74  ? -15.944 11.230 86.850  1.00 20.89 ? 74  ASP A N   1 
ATOM   635  C CA  . ASP A 1 74  ? -15.615 12.651 86.701  1.00 21.35 ? 74  ASP A CA  1 
ATOM   636  C C   . ASP A 1 74  ? -16.244 13.422 87.859  1.00 22.19 ? 74  ASP A C   1 
ATOM   637  O O   . ASP A 1 74  ? -17.474 13.483 87.969  1.00 21.57 ? 74  ASP A O   1 
ATOM   638  C CB  . ASP A 1 74  ? -16.126 13.161 85.348  1.00 18.47 ? 74  ASP A CB  1 
ATOM   639  C CG  . ASP A 1 74  ? -15.687 14.595 85.038  1.00 18.55 ? 74  ASP A CG  1 
ATOM   640  O OD1 . ASP A 1 74  ? -15.823 15.491 85.910  1.00 19.82 ? 74  ASP A OD1 1 
ATOM   641  O OD2 . ASP A 1 74  ? -15.234 14.840 83.904  1.00 20.65 ? 74  ASP A OD2 1 
ATOM   642  N N   . VAL A 1 75  ? -15.409 14.005 88.730  1.00 21.02 ? 75  VAL A N   1 
ATOM   643  C CA  . VAL A 1 75  ? -15.940 14.531 89.989  1.00 26.14 ? 75  VAL A CA  1 
ATOM   644  C C   . VAL A 1 75  ? -16.733 15.809 89.742  1.00 18.58 ? 75  VAL A C   1 
ATOM   645  O O   . VAL A 1 75  ? -17.777 16.039 90.362  1.00 22.18 ? 75  VAL A O   1 
ATOM   646  C CB  . VAL A 1 75  ? -14.812 14.731 91.026  1.00 28.98 ? 75  VAL A CB  1 
ATOM   647  C CG1 . VAL A 1 75  ? -14.087 13.424 91.264  1.00 27.78 ? 75  VAL A CG1 1 
ATOM   648  C CG2 . VAL A 1 75  ? -13.832 15.802 90.590  1.00 26.49 ? 75  VAL A CG2 1 
ATOM   649  N N   . PHE A 1 76  ? -16.290 16.626 88.793  1.00 21.31 ? 76  PHE A N   1 
ATOM   650  C CA  . PHE A 1 76  ? -17.041 17.821 88.449  1.00 20.82 ? 76  PHE A CA  1 
ATOM   651  C C   . PHE A 1 76  ? -18.376 17.460 87.816  1.00 22.06 ? 76  PHE A C   1 
ATOM   652  O O   . PHE A 1 76  ? -19.411 18.052 88.144  1.00 19.06 ? 76  PHE A O   1 
ATOM   653  C CB  . PHE A 1 76  ? -16.221 18.694 87.504  1.00 23.67 ? 76  PHE A CB  1 
ATOM   654  C CG  . PHE A 1 76  ? -16.736 20.060 87.391  1.00 28.22 ? 76  PHE A CG  1 
ATOM   655  C CD1 . PHE A 1 76  ? -16.332 21.031 88.291  1.00 29.12 ? 76  PHE A CD1 1 
ATOM   656  C CD2 . PHE A 1 76  ? -17.659 20.383 86.393  1.00 27.13 ? 76  PHE A CD2 1 
ATOM   657  C CE1 . PHE A 1 76  ? -16.832 22.309 88.211  1.00 34.69 ? 76  PHE A CE1 1 
ATOM   658  C CE2 . PHE A 1 76  ? -18.165 21.666 86.296  1.00 28.63 ? 76  PHE A CE2 1 
ATOM   659  C CZ  . PHE A 1 76  ? -17.759 22.629 87.212  1.00 34.10 ? 76  PHE A CZ  1 
ATOM   660  N N   . LEU A 1 77  ? -18.371 16.484 86.910  1.00 16.03 ? 77  LEU A N   1 
ATOM   661  C CA  . LEU A 1 77  ? -19.616 16.064 86.272  1.00 21.13 ? 77  LEU A CA  1 
ATOM   662  C C   . LEU A 1 77  ? -20.593 15.433 87.268  1.00 23.14 ? 77  LEU A C   1 
ATOM   663  O O   . LEU A 1 77  ? -21.814 15.561 87.107  1.00 20.65 ? 77  LEU A O   1 
ATOM   664  C CB  . LEU A 1 77  ? -19.271 15.098 85.142  1.00 25.85 ? 77  LEU A CB  1 
ATOM   665  C CG  . LEU A 1 77  ? -20.287 14.804 84.048  1.00 30.92 ? 77  LEU A CG  1 
ATOM   666  C CD1 . LEU A 1 77  ? -20.950 16.081 83.475  1.00 19.43 ? 77  LEU A CD1 1 
ATOM   667  C CD2 . LEU A 1 77  ? -19.524 14.029 82.983  1.00 23.69 ? 77  LEU A CD2 1 
ATOM   668  N N   . GLU A 1 78  ? -20.088 14.745 88.296  1.00 21.47 ? 78  GLU A N   1 
ATOM   669  C CA  . GLU A 1 78  ? -20.977 14.207 89.322  1.00 22.60 ? 78  GLU A CA  1 
ATOM   670  C C   . GLU A 1 78  ? -21.718 15.323 90.044  1.00 23.40 ? 78  GLU A C   1 
ATOM   671  O O   . GLU A 1 78  ? -22.892 15.172 90.393  1.00 28.83 ? 78  GLU A O   1 
ATOM   672  C CB  . GLU A 1 78  ? -20.184 13.360 90.322  1.00 25.97 ? 78  GLU A CB  1 
ATOM   673  C CG  . GLU A 1 78  ? -19.763 12.005 89.759  1.00 43.38 ? 78  GLU A CG  1 
ATOM   674  C CD  . GLU A 1 78  ? -18.739 11.286 90.628  1.00 55.54 ? 78  GLU A CD  1 
ATOM   675  O OE1 . GLU A 1 78  ? -18.119 10.327 90.118  1.00 56.75 ? 78  GLU A OE1 1 
ATOM   676  O OE2 . GLU A 1 78  ? -18.560 11.665 91.811  1.00 49.70 ? 78  GLU A OE2 1 
ATOM   677  N N   . ALA A 1 79  ? -21.050 16.453 90.273  1.00 22.13 ? 79  ALA A N   1 
ATOM   678  C CA  . ALA A 1 79  ? -21.714 17.586 90.899  1.00 21.06 ? 79  ALA A CA  1 
ATOM   679  C C   . ALA A 1 79  ? -22.751 18.214 89.977  1.00 21.05 ? 79  ALA A C   1 
ATOM   680  O O   . ALA A 1 79  ? -23.745 18.757 90.454  1.00 19.40 ? 79  ALA A O   1 
ATOM   681  C CB  . ALA A 1 79  ? -20.689 18.627 91.327  1.00 23.34 ? 79  ALA A CB  1 
ATOM   682  N N   . ILE A 1 80  ? -22.541 18.167 88.668  1.00 14.74 ? 80  ILE A N   1 
ATOM   683  C CA  . ILE A 1 80  ? -23.567 18.654 87.743  1.00 18.67 ? 80  ILE A CA  1 
ATOM   684  C C   . ILE A 1 80  ? -24.784 17.728 87.751  1.00 17.78 ? 80  ILE A C   1 
ATOM   685  O O   . ILE A 1 80  ? -25.941 18.179 87.752  1.00 18.85 ? 80  ILE A O   1 
ATOM   686  C CB  . ILE A 1 80  ? -22.970 18.791 86.326  1.00 16.26 ? 80  ILE A CB  1 
ATOM   687  C CG1 . ILE A 1 80  ? -21.981 19.954 86.260  1.00 28.48 ? 80  ILE A CG1 1 
ATOM   688  C CG2 . ILE A 1 80  ? -24.086 18.922 85.250  1.00 14.85 ? 80  ILE A CG2 1 
ATOM   689  C CD1 . ILE A 1 80  ? -22.619 21.273 86.209  1.00 39.71 ? 80  ILE A CD1 1 
ATOM   690  N N   . ARG A 1 81  ? -24.545 16.419 87.754  1.00 17.11 ? 81  ARG A N   1 
ATOM   691  C CA  . ARG A 1 81  ? -25.636 15.457 87.625  1.00 22.23 ? 81  ARG A CA  1 
ATOM   692  C C   . ARG A 1 81  ? -26.566 15.455 88.836  1.00 20.83 ? 81  ARG A C   1 
ATOM   693  O O   . ARG A 1 81  ? -27.777 15.290 88.673  1.00 25.04 ? 81  ARG A O   1 
ATOM   694  C CB  . ARG A 1 81  ? -25.052 14.058 87.383  1.00 19.52 ? 81  ARG A CB  1 
ATOM   695  C CG  . ARG A 1 81  ? -26.118 12.959 87.289  1.00 28.06 ? 81  ARG A CG  1 
ATOM   696  C CD  . ARG A 1 81  ? -25.503 11.570 87.096  1.00 38.57 ? 81  ARG A CD  1 
ATOM   697  N NE  . ARG A 1 81  ? -24.925 11.378 85.763  1.00 36.92 ? 81  ARG A NE  1 
ATOM   698  C CZ  . ARG A 1 81  ? -25.638 11.211 84.650  1.00 41.58 ? 81  ARG A CZ  1 
ATOM   699  N NH1 . ARG A 1 81  ? -26.974 11.216 84.692  1.00 52.17 ? 81  ARG A NH1 1 
ATOM   700  N NH2 . ARG A 1 81  ? -25.021 11.036 83.489  1.00 32.61 ? 81  ARG A NH2 1 
ATOM   701  N N   . LYS A 1 82  ? -26.026 15.652 90.042  1.00 18.19 ? 82  LYS A N   1 
ATOM   702  C CA  . LYS A 1 82  ? -26.774 15.484 91.287  1.00 22.28 ? 82  LYS A CA  1 
ATOM   703  C C   . LYS A 1 82  ? -27.976 16.417 91.367  1.00 17.61 ? 82  LYS A C   1 
ATOM   704  O O   . LYS A 1 82  ? -27.940 17.552 90.888  1.00 21.40 ? 82  LYS A O   1 
ATOM   705  C CB  . LYS A 1 82  ? -25.885 15.803 92.490  1.00 27.84 ? 82  LYS A CB  1 
ATOM   706  C CG  . LYS A 1 82  ? -24.893 14.763 92.902  1.00 31.51 ? 82  LYS A CG  1 
ATOM   707  C CD  . LYS A 1 82  ? -24.113 15.354 94.065  1.00 26.51 ? 82  LYS A CD  1 
ATOM   708  C CE  . LYS A 1 82  ? -23.056 14.412 94.602  1.00 49.16 ? 82  LYS A CE  1 
ATOM   709  N NZ  . LYS A 1 82  ? -22.754 14.832 95.995  1.00 56.63 ? 82  LYS A NZ  1 
ATOM   710  N N   . ASP A 1 83  ? -29.019 15.957 92.054  1.00 16.80 ? 83  ASP A N   1 
ATOM   711  C CA  . ASP A 1 83  ? -30.050 16.879 92.510  1.00 20.32 ? 83  ASP A CA  1 
ATOM   712  C C   . ASP A 1 83  ? -29.403 17.957 93.384  1.00 25.34 ? 83  ASP A C   1 
ATOM   713  O O   . ASP A 1 83  ? -28.553 17.639 94.230  1.00 27.54 ? 83  ASP A O   1 
ATOM   714  C CB  . ASP A 1 83  ? -31.117 16.125 93.307  1.00 23.74 ? 83  ASP A CB  1 
ATOM   715  C CG  . ASP A 1 83  ? -32.297 17.001 93.689  1.00 32.04 ? 83  ASP A CG  1 
ATOM   716  O OD1 . ASP A 1 83  ? -32.112 17.982 94.437  1.00 24.42 ? 83  ASP A OD1 1 
ATOM   717  O OD2 . ASP A 1 83  ? -33.436 16.689 93.247  1.00 37.04 ? 83  ASP A OD2 1 
ATOM   718  N N   . PRO A 1 84  ? -29.746 19.236 93.194  1.00 22.49 ? 84  PRO A N   1 
ATOM   719  C CA  . PRO A 1 84  ? -29.067 20.285 93.973  1.00 26.46 ? 84  PRO A CA  1 
ATOM   720  C C   . PRO A 1 84  ? -29.192 20.102 95.478  1.00 25.24 ? 84  PRO A C   1 
ATOM   721  O O   . PRO A 1 84  ? -28.295 20.533 96.221  1.00 25.21 ? 84  PRO A O   1 
ATOM   722  C CB  . PRO A 1 84  ? -29.747 21.577 93.500  1.00 26.48 ? 84  PRO A CB  1 
ATOM   723  C CG  . PRO A 1 84  ? -30.249 21.259 92.160  1.00 23.31 ? 84  PRO A CG  1 
ATOM   724  C CD  . PRO A 1 84  ? -30.667 19.805 92.190  1.00 23.06 ? 84  PRO A CD  1 
ATOM   725  N N   . ASP A 1 85  ? -30.270 19.463 95.950  1.00 22.54 ? 85  ASP A N   1 
ATOM   726  C CA  . ASP A 1 85  ? -30.422 19.195 97.377  1.00 23.86 ? 85  ASP A CA  1 
ATOM   727  C C   . ASP A 1 85  ? -29.290 18.335 97.932  1.00 21.31 ? 85  ASP A C   1 
ATOM   728  O O   . ASP A 1 85  ? -29.045 18.359 99.147  1.00 20.26 ? 85  ASP A O   1 
ATOM   729  C CB  . ASP A 1 85  ? -31.745 18.492 97.648  1.00 28.55 ? 85  ASP A CB  1 
ATOM   730  C CG  . ASP A 1 85  ? -32.937 19.413 97.503  1.00 38.76 ? 85  ASP A CG  1 
ATOM   731  O OD1 . ASP A 1 85  ? -32.748 20.647 97.532  1.00 36.72 ? 85  ASP A OD1 1 
ATOM   732  O OD2 . ASP A 1 85  ? -34.065 18.895 97.364  1.00 41.19 ? 85  ASP A OD2 1 
ATOM   733  N N   . ASP A 1 86  ? -28.611 17.569 97.079  1.00 19.63 ? 86  ASP A N   1 
ATOM   734  C CA  . ASP A 1 86  ? -27.544 16.679 97.514  1.00 26.82 ? 86  ASP A CA  1 
ATOM   735  C C   . ASP A 1 86  ? -26.154 17.267 97.308  1.00 25.93 ? 86  ASP A C   1 
ATOM   736  O O   . ASP A 1 86  ? -25.165 16.574 97.562  1.00 29.00 ? 86  ASP A O   1 
ATOM   737  C CB  . ASP A 1 86  ? -27.634 15.334 96.779  1.00 28.31 ? 86  ASP A CB  1 
ATOM   738  C CG  . ASP A 1 86  ? -28.962 14.641 96.975  1.00 39.69 ? 86  ASP A CG  1 
ATOM   739  O OD1 . ASP A 1 86  ? -29.579 14.783 98.055  1.00 42.43 ? 86  ASP A OD1 1 
ATOM   740  O OD2 . ASP A 1 86  ? -29.392 13.947 96.031  1.00 41.67 ? 86  ASP A OD2 1 
ATOM   741  N N   . LEU A 1 87  ? -26.047 18.506 96.831  1.00 20.41 ? 87  LEU A N   1 
ATOM   742  C CA  . LEU A 1 87  ? -24.735 19.109 96.616  1.00 17.66 ? 87  LEU A CA  1 
ATOM   743  C C   . LEU A 1 87  ? -24.051 19.455 97.936  1.00 18.28 ? 87  LEU A C   1 
ATOM   744  O O   . LEU A 1 87  ? -24.657 20.061 98.826  1.00 20.88 ? 87  LEU A O   1 
ATOM   745  C CB  . LEU A 1 87  ? -24.859 20.374 95.775  1.00 17.16 ? 87  LEU A CB  1 
ATOM   746  C CG  . LEU A 1 87  ? -25.123 20.111 94.302  1.00 17.92 ? 87  LEU A CG  1 
ATOM   747  C CD1 . LEU A 1 87  ? -25.535 21.400 93.604  1.00 22.64 ? 87  LEU A CD1 1 
ATOM   748  C CD2 . LEU A 1 87  ? -23.890 19.545 93.646  1.00 17.85 ? 87  LEU A CD2 1 
ATOM   749  N N   . GLU A 1 88  ? -22.777 19.086 98.050  1.00 18.38 ? 88  GLU A N   1 
ATOM   750  C CA  . GLU A 1 88  ? -21.947 19.603 99.129  1.00 18.79 ? 88  GLU A CA  1 
ATOM   751  C C   . GLU A 1 88  ? -21.608 21.061 98.862  1.00 24.04 ? 88  GLU A C   1 
ATOM   752  O O   . GLU A 1 88  ? -21.547 21.494 97.710  1.00 20.31 ? 88  GLU A O   1 
ATOM   753  C CB  . GLU A 1 88  ? -20.638 18.820 99.230  1.00 23.58 ? 88  GLU A CB  1 
ATOM   754  C CG  . GLU A 1 88  ? -20.792 17.340 99.471  1.00 28.87 ? 88  GLU A CG  1 
ATOM   755  C CD  . GLU A 1 88  ? -19.518 16.585 99.128  1.00 37.62 ? 88  GLU A CD  1 
ATOM   756  O OE1 . GLU A 1 88  ? -19.465 15.372 99.388  1.00 47.01 ? 88  GLU A OE1 1 
ATOM   757  O OE2 . GLU A 1 88  ? -18.564 17.206 98.604  1.00 36.47 ? 88  GLU A OE2 1 
ATOM   758  N N   . LYS A 1 89  ? -21.337 21.810 99.938  1.00 21.26 ? 89  LYS A N   1 
ATOM   759  C CA  . LYS A 1 89  ? -20.843 23.179 99.771  1.00 21.21 ? 89  LYS A CA  1 
ATOM   760  C C   . LYS A 1 89  ? -19.612 23.233 98.870  1.00 23.46 ? 89  LYS A C   1 
ATOM   761  O O   . LYS A 1 89  ? -19.479 24.139 98.036  1.00 24.07 ? 89  LYS A O   1 
ATOM   762  C CB  . LYS A 1 89  ? -20.519 23.792 101.139 1.00 22.89 ? 89  LYS A CB  1 
ATOM   763  C CG  . LYS A 1 89  ? -21.757 24.025 101.985 1.00 26.41 ? 89  LYS A CG  1 
ATOM   764  C CD  . LYS A 1 89  ? -21.417 24.887 103.214 1.00 28.09 ? 89  LYS A CD  1 
ATOM   765  C CE  . LYS A 1 89  ? -22.467 24.769 104.306 1.00 41.44 ? 89  LYS A CE  1 
ATOM   766  N NZ  . LYS A 1 89  ? -23.849 25.006 103.815 1.00 46.30 ? 89  LYS A NZ  1 
ATOM   767  N N   . GLU A 1 90  ? -18.688 22.285 99.031  1.00 23.02 ? 90  GLU A N   1 
ATOM   768  C CA  . GLU A 1 90  ? -17.497 22.302 98.196  1.00 25.42 ? 90  GLU A CA  1 
ATOM   769  C C   . GLU A 1 90  ? -17.843 22.133 96.732  1.00 23.26 ? 90  GLU A C   1 
ATOM   770  O O   . GLU A 1 90  ? -17.186 22.728 95.876  1.00 20.00 ? 90  GLU A O   1 
ATOM   771  C CB  . GLU A 1 90  ? -16.547 21.187 98.617  1.00 29.30 ? 90  GLU A CB  1 
ATOM   772  C CG  . GLU A 1 90  ? -15.993 21.468 99.960  1.00 50.48 ? 90  GLU A CG  1 
ATOM   773  C CD  . GLU A 1 90  ? -15.169 20.334 100.485 1.00 68.19 ? 90  GLU A CD  1 
ATOM   774  O OE1 . GLU A 1 90  ? -15.118 20.168 101.734 1.00 68.86 ? 90  GLU A OE1 1 
ATOM   775  O OE2 . GLU A 1 90  ? -14.559 19.621 99.668  1.00 74.12 ? 90  GLU A OE2 1 
ATOM   776  N N   . GLU A 1 91  ? -18.862 21.317 96.436  1.00 21.33 ? 91  GLU A N   1 
ATOM   777  C CA  . GLU A 1 91  ? -19.289 21.148 95.055  1.00 17.45 ? 91  GLU A CA  1 
ATOM   778  C C   . GLU A 1 91  ? -19.941 22.417 94.522  1.00 17.19 ? 91  GLU A C   1 
ATOM   779  O O   . GLU A 1 91  ? -19.764 22.759 93.351  1.00 17.42 ? 91  GLU A O   1 
ATOM   780  C CB  . GLU A 1 91  ? -20.237 19.955 94.949  1.00 20.40 ? 91  GLU A CB  1 
ATOM   781  C CG  . GLU A 1 91  ? -19.567 18.628 95.170  1.00 23.30 ? 91  GLU A CG  1 
ATOM   782  C CD  . GLU A 1 91  ? -20.521 17.458 95.133  1.00 29.68 ? 91  GLU A CD  1 
ATOM   783  O OE1 . GLU A 1 91  ? -21.534 17.472 95.872  1.00 29.44 ? 91  GLU A OE1 1 
ATOM   784  O OE2 . GLU A 1 91  ? -20.247 16.520 94.356  1.00 27.09 ? 91  GLU A OE2 1 
ATOM   785  N N   . VAL A 1 92  ? -20.676 23.144 95.361  1.00 18.87 ? 92  VAL A N   1 
ATOM   786  C CA  . VAL A 1 92  ? -21.238 24.414 94.912  1.00 18.77 ? 92  VAL A CA  1 
ATOM   787  C C   . VAL A 1 92  ? -20.123 25.416 94.648  1.00 21.31 ? 92  VAL A C   1 
ATOM   788  O O   . VAL A 1 92  ? -20.130 26.133 93.638  1.00 18.42 ? 92  VAL A O   1 
ATOM   789  C CB  . VAL A 1 92  ? -22.246 24.974 95.935  1.00 19.50 ? 92  VAL A CB  1 
ATOM   790  C CG1 . VAL A 1 92  ? -22.759 26.336 95.448  1.00 21.68 ? 92  VAL A CG1 1 
ATOM   791  C CG2 . VAL A 1 92  ? -23.376 23.990 96.171  1.00 20.66 ? 92  VAL A CG2 1 
ATOM   792  N N   . GLU A 1 93  ? -19.148 25.484 95.547  1.00 19.38 ? 93  GLU A N   1 
ATOM   793  C CA  . GLU A 1 93  ? -18.034 26.406 95.343  1.00 18.33 ? 93  GLU A CA  1 
ATOM   794  C C   . GLU A 1 93  ? -17.277 26.102 94.051  1.00 23.11 ? 93  GLU A C   1 
ATOM   795  O O   . GLU A 1 93  ? -16.886 27.023 93.324  1.00 23.26 ? 93  GLU A O   1 
ATOM   796  C CB  . GLU A 1 93  ? -17.096 26.353 96.539  1.00 22.21 ? 93  GLU A CB  1 
ATOM   797  C CG  . GLU A 1 93  ? -17.713 26.906 97.815  1.00 32.51 ? 93  GLU A CG  1 
ATOM   798  C CD  . GLU A 1 93  ? -16.793 26.730 99.024  1.00 50.72 ? 93  GLU A CD  1 
ATOM   799  O OE1 . GLU A 1 93  ? -17.309 26.604 100.164 1.00 50.69 ? 93  GLU A OE1 1 
ATOM   800  O OE2 . GLU A 1 93  ? -15.554 26.709 98.826  1.00 58.37 ? 93  GLU A OE2 1 
ATOM   801  N N   . LYS A 1 94  ? -17.052 24.820 93.749  1.00 21.54 ? 94  LYS A N   1 
ATOM   802  C CA  . LYS A 1 94  ? -16.338 24.472 92.519  1.00 23.50 ? 94  LYS A CA  1 
ATOM   803  C C   . LYS A 1 94  ? -17.145 24.851 91.289  1.00 24.99 ? 94  LYS A C   1 
ATOM   804  O O   . LYS A 1 94  ? -16.584 25.298 90.284  1.00 21.93 ? 94  LYS A O   1 
ATOM   805  C CB  . LYS A 1 94  ? -16.011 22.980 92.485  1.00 23.98 ? 94  LYS A CB  1 
ATOM   806  C CG  . LYS A 1 94  ? -14.932 22.567 93.481  1.00 34.42 ? 94  LYS A CG  1 
ATOM   807  C CD  . LYS A 1 94  ? -14.537 21.112 93.275  1.00 43.27 ? 94  LYS A CD  1 
ATOM   808  C CE  . LYS A 1 94  ? -13.365 20.739 94.168  1.00 42.81 ? 94  LYS A CE  1 
ATOM   809  N NZ  . LYS A 1 94  ? -13.683 21.002 95.604  1.00 47.39 ? 94  LYS A NZ  1 
ATOM   810  N N   . LEU A 1 95  ? -18.458 24.646 91.346  1.00 17.52 ? 95  LEU A N   1 
ATOM   811  C CA  . LEU A 1 95  ? -19.334 25.040 90.248  1.00 18.31 ? 95  LEU A CA  1 
ATOM   812  C C   . LEU A 1 95  ? -19.350 26.558 90.054  1.00 16.94 ? 95  LEU A C   1 
ATOM   813  O O   . LEU A 1 95  ? -19.321 27.045 88.916  1.00 16.03 ? 95  LEU A O   1 
ATOM   814  C CB  . LEU A 1 95  ? -20.731 24.497 90.521  1.00 19.94 ? 95  LEU A CB  1 
ATOM   815  C CG  . LEU A 1 95  ? -21.854 24.652 89.500  1.00 36.27 ? 95  LEU A CG  1 
ATOM   816  C CD1 . LEU A 1 95  ? -21.417 24.094 88.155  1.00 29.69 ? 95  LEU A CD1 1 
ATOM   817  C CD2 . LEU A 1 95  ? -23.099 23.952 90.003  1.00 41.77 ? 95  LEU A CD2 1 
ATOM   818  N N   . ILE A 1 96  ? -19.419 27.321 91.146  1.00 16.90 ? 96  ILE A N   1 
ATOM   819  C CA  . ILE A 1 96  ? -19.332 28.779 91.049  1.00 20.23 ? 96  ILE A CA  1 
ATOM   820  C C   . ILE A 1 96  ? -17.991 29.197 90.465  1.00 22.58 ? 96  ILE A C   1 
ATOM   821  O O   . ILE A 1 96  ? -17.910 30.085 89.603  1.00 20.99 ? 96  ILE A O   1 
ATOM   822  C CB  . ILE A 1 96  ? -19.544 29.426 92.431  1.00 25.21 ? 96  ILE A CB  1 
ATOM   823  C CG1 . ILE A 1 96  ? -20.923 29.092 92.982  1.00 33.81 ? 96  ILE A CG1 1 
ATOM   824  C CG2 . ILE A 1 96  ? -19.336 30.934 92.337  1.00 24.82 ? 96  ILE A CG2 1 
ATOM   825  C CD1 . ILE A 1 96  ? -22.004 29.791 92.275  1.00 41.05 ? 96  ILE A CD1 1 
ATOM   826  N N   . GLU A 1 97  ? -16.908 28.582 90.952  1.00 20.24 ? 97  GLU A N   1 
ATOM   827  C CA  . GLU A 1 97  ? -15.578 28.971 90.511  1.00 18.27 ? 97  GLU A CA  1 
ATOM   828  C C   . GLU A 1 97  ? -15.388 28.652 89.037  1.00 18.73 ? 97  GLU A C   1 
ATOM   829  O O   . GLU A 1 97  ? -14.758 29.422 88.300  1.00 22.75 ? 97  GLU A O   1 
ATOM   830  C CB  . GLU A 1 97  ? -14.533 28.253 91.359  1.00 23.94 ? 97  GLU A CB  1 
ATOM   831  C CG  . GLU A 1 97  ? -13.113 28.482 90.931  1.00 39.44 ? 97  GLU A CG  1 
ATOM   832  C CD  . GLU A 1 97  ? -12.130 27.731 91.807  1.00 48.21 ? 97  GLU A CD  1 
ATOM   833  O OE1 . GLU A 1 97  ? -10.908 27.889 91.602  1.00 52.08 ? 97  GLU A OE1 1 
ATOM   834  O OE2 . GLU A 1 97  ? -12.585 26.989 92.704  1.00 51.87 ? 97  GLU A OE2 1 
ATOM   835  N N   . PHE A 1 98  ? -15.925 27.514 88.606  1.00 16.83 ? 98  PHE A N   1 
ATOM   836  C CA  . PHE A 1 98  ? -15.862 27.124 87.203  1.00 15.42 ? 98  PHE A CA  1 
ATOM   837  C C   . PHE A 1 98  ? -16.645 28.104 86.340  1.00 18.01 ? 98  PHE A C   1 
ATOM   838  O O   . PHE A 1 98  ? -16.177 28.515 85.270  1.00 20.32 ? 98  PHE A O   1 
ATOM   839  C CB  . PHE A 1 98  ? -16.413 25.710 87.069  1.00 19.98 ? 98  PHE A CB  1 
ATOM   840  C CG  . PHE A 1 98  ? -16.188 25.082 85.724  1.00 25.27 ? 98  PHE A CG  1 
ATOM   841  C CD1 . PHE A 1 98  ? -14.959 24.539 85.402  1.00 20.55 ? 98  PHE A CD1 1 
ATOM   842  C CD2 . PHE A 1 98  ? -17.218 24.997 84.817  1.00 19.35 ? 98  PHE A CD2 1 
ATOM   843  C CE1 . PHE A 1 98  ? -14.748 23.939 84.184  1.00 24.89 ? 98  PHE A CE1 1 
ATOM   844  C CE2 . PHE A 1 98  ? -17.019 24.395 83.578  1.00 27.87 ? 98  PHE A CE2 1 
ATOM   845  C CZ  . PHE A 1 98  ? -15.772 23.869 83.270  1.00 21.56 ? 98  PHE A CZ  1 
ATOM   846  N N   . THR A 1 99  ? -17.839 28.493 86.797  1.00 20.07 ? 99  THR A N   1 
ATOM   847  C CA  . THR A 1 99  ? -18.612 29.509 86.088  1.00 17.04 ? 99  THR A CA  1 
ATOM   848  C C   . THR A 1 99  ? -17.830 30.812 85.986  1.00 19.38 ? 99  THR A C   1 
ATOM   849  O O   . THR A 1 99  ? -17.737 31.406 84.906  1.00 21.72 ? 99  THR A O   1 
ATOM   850  C CB  . THR A 1 99  ? -19.957 29.753 86.786  1.00 20.49 ? 99  THR A CB  1 
ATOM   851  O OG1 . THR A 1 99  ? -20.651 28.513 86.968  1.00 19.53 ? 99  THR A OG1 1 
ATOM   852  C CG2 . THR A 1 99  ? -20.822 30.661 85.925  1.00 18.24 ? 99  THR A CG2 1 
ATOM   853  N N   . LYS A 1 100 ? -17.237 31.265 87.099  1.00 17.58 ? 100 LYS A N   1 
ATOM   854  C CA  . LYS A 1 100 ? -16.505 32.525 87.071  1.00 17.77 ? 100 LYS A CA  1 
ATOM   855  C C   . LYS A 1 100 ? -15.305 32.454 86.139  1.00 20.24 ? 100 LYS A C   1 
ATOM   856  O O   . LYS A 1 100 ? -14.943 33.457 85.516  1.00 22.42 ? 100 LYS A O   1 
ATOM   857  C CB  . LYS A 1 100 ? -16.051 32.909 88.486  1.00 21.78 ? 100 LYS A CB  1 
ATOM   858  C CG  . LYS A 1 100 ? -17.173 33.536 89.311  1.00 31.10 ? 100 LYS A CG  1 
ATOM   859  C CD  . LYS A 1 100 ? -16.703 33.920 90.705  1.00 40.12 ? 100 LYS A CD  1 
ATOM   860  C CE  . LYS A 1 100 ? -17.863 34.445 91.541  1.00 46.14 ? 100 LYS A CE  1 
ATOM   861  N NZ  . LYS A 1 100 ? -17.765 35.914 91.827  1.00 52.86 ? 100 LYS A NZ  1 
ATOM   862  N N   . LEU A 1 101 ? -14.679 31.278 86.035  1.00 22.04 ? 101 LEU A N   1 
ATOM   863  C CA  . LEU A 1 101 ? -13.550 31.109 85.133  1.00 20.37 ? 101 LEU A CA  1 
ATOM   864  C C   . LEU A 1 101 ? -13.960 31.364 83.687  1.00 19.39 ? 101 LEU A C   1 
ATOM   865  O O   . LEU A 1 101 ? -13.207 31.965 82.915  1.00 25.35 ? 101 LEU A O   1 
ATOM   866  C CB  . LEU A 1 101 ? -12.979 29.696 85.302  1.00 24.79 ? 101 LEU A CB  1 
ATOM   867  C CG  . LEU A 1 101 ? -11.743 29.295 84.482  1.00 32.08 ? 101 LEU A CG  1 
ATOM   868  C CD1 . LEU A 1 101 ? -10.572 30.223 84.764  1.00 30.37 ? 101 LEU A CD1 1 
ATOM   869  C CD2 . LEU A 1 101 ? -11.362 27.843 84.788  1.00 26.81 ? 101 LEU A CD2 1 
ATOM   870  N N   . ASN A 1 102 ? -15.165 30.941 83.317  1.00 19.03 ? 102 ASN A N   1 
ATOM   871  C CA  . ASN A 1 102 ? -15.615 30.925 81.930  1.00 19.77 ? 102 ASN A CA  1 
ATOM   872  C C   . ASN A 1 102 ? -16.595 32.042 81.615  1.00 17.79 ? 102 ASN A C   1 
ATOM   873  O O   . ASN A 1 102 ? -17.038 32.153 80.462  1.00 14.89 ? 102 ASN A O   1 
ATOM   874  C CB  . ASN A 1 102 ? -16.255 29.569 81.631  1.00 16.72 ? 102 ASN A CB  1 
ATOM   875  C CG  . ASN A 1 102 ? -15.254 28.437 81.653  1.00 18.77 ? 102 ASN A CG  1 
ATOM   876  O OD1 . ASN A 1 102 ? -14.268 28.458 80.913  1.00 23.82 ? 102 ASN A OD1 1 
ATOM   877  N ND2 . ASN A 1 102 ? -15.499 27.438 82.494  1.00 17.76 ? 102 ASN A ND2 1 
ATOM   878  N N   . TYR A 1 103 ? -16.869 32.900 82.606  1.00 19.93 ? 103 TYR A N   1 
ATOM   879  C CA  . TYR A 1 103 ? -17.976 33.856 82.607  1.00 24.99 ? 103 TYR A CA  1 
ATOM   880  C C   . TYR A 1 103 ? -17.961 34.797 81.406  1.00 21.28 ? 103 TYR A C   1 
ATOM   881  O O   . TYR A 1 103 ? -19.023 35.171 80.883  1.00 21.46 ? 103 TYR A O   1 
ATOM   882  C CB  . TYR A 1 103 ? -17.900 34.660 83.925  1.00 21.16 ? 103 TYR A CB  1 
ATOM   883  C CG  . TYR A 1 103 ? -18.969 35.695 84.144  1.00 28.06 ? 103 TYR A CG  1 
ATOM   884  C CD1 . TYR A 1 103 ? -18.848 36.987 83.627  1.00 27.40 ? 103 TYR A CD1 1 
ATOM   885  C CD2 . TYR A 1 103 ? -20.099 35.389 84.884  1.00 31.59 ? 103 TYR A CD2 1 
ATOM   886  C CE1 . TYR A 1 103 ? -19.838 37.937 83.844  1.00 33.73 ? 103 TYR A CE1 1 
ATOM   887  C CE2 . TYR A 1 103 ? -21.085 36.329 85.114  1.00 37.36 ? 103 TYR A CE2 1 
ATOM   888  C CZ  . TYR A 1 103 ? -20.955 37.599 84.595  1.00 40.23 ? 103 TYR A CZ  1 
ATOM   889  O OH  . TYR A 1 103 ? -21.956 38.521 84.825  1.00 37.83 ? 103 TYR A OH  1 
ATOM   890  N N   . GLU A 1 104 ? -16.785 35.249 80.990  1.00 21.33 ? 104 GLU A N   1 
ATOM   891  C CA  . GLU A 1 104 ? -16.714 36.256 79.945  1.00 23.34 ? 104 GLU A CA  1 
ATOM   892  C C   . GLU A 1 104 ? -16.656 35.664 78.546  1.00 18.71 ? 104 GLU A C   1 
ATOM   893  O O   . GLU A 1 104 ? -16.706 36.417 77.568  1.00 21.15 ? 104 GLU A O   1 
ATOM   894  C CB  . GLU A 1 104 ? -15.494 37.163 80.160  1.00 24.88 ? 104 GLU A CB  1 
ATOM   895  C CG  . GLU A 1 104 ? -15.498 37.884 81.500  1.00 28.78 ? 104 GLU A CG  1 
ATOM   896  C CD  . GLU A 1 104 ? -16.473 39.046 81.534  1.00 45.19 ? 104 GLU A CD  1 
ATOM   897  O OE1 . GLU A 1 104 ? -16.889 39.513 80.449  1.00 54.64 ? 104 GLU A OE1 1 
ATOM   898  O OE2 . GLU A 1 104 ? -16.810 39.508 82.644  1.00 51.20 ? 104 GLU A OE2 1 
ATOM   899  N N   . LYS A 1 105 ? -16.565 34.353 78.417  1.00 17.22 ? 105 LYS A N   1 
ATOM   900  C CA  . LYS A 1 105 ? -16.516 33.766 77.084  1.00 16.27 ? 105 LYS A CA  1 
ATOM   901  C C   . LYS A 1 105 ? -17.902 33.813 76.436  1.00 20.19 ? 105 LYS A C   1 
ATOM   902  O O   . LYS A 1 105 ? -18.915 33.635 77.105  1.00 17.10 ? 105 LYS A O   1 
ATOM   903  C CB  . LYS A 1 105 ? -16.023 32.320 77.157  1.00 15.16 ? 105 LYS A CB  1 
ATOM   904  C CG  . LYS A 1 105 ? -14.621 32.213 77.775  1.00 18.86 ? 105 LYS A CG  1 
ATOM   905  C CD  . LYS A 1 105 ? -14.298 30.774 78.156  1.00 22.01 ? 105 LYS A CD  1 
ATOM   906  C CE  . LYS A 1 105 ? -12.906 30.703 78.840  1.00 19.95 ? 105 LYS A CE  1 
ATOM   907  N NZ  . LYS A 1 105 ? -12.556 29.311 79.221  1.00 20.55 ? 105 LYS A NZ  1 
ATOM   908  N N   . PRO A 1 106 ? -17.982 34.059 75.137  1.00 19.77 ? 106 PRO A N   1 
ATOM   909  C CA  . PRO A 1 106 ? -19.302 34.148 74.493  1.00 16.99 ? 106 PRO A CA  1 
ATOM   910  C C   . PRO A 1 106 ? -20.142 32.895 74.631  1.00 15.93 ? 106 PRO A C   1 
ATOM   911  O O   . PRO A 1 106 ? -21.368 32.998 74.564  1.00 18.95 ? 106 PRO A O   1 
ATOM   912  C CB  . PRO A 1 106 ? -18.948 34.438 73.026  1.00 17.72 ? 106 PRO A CB  1 
ATOM   913  C CG  . PRO A 1 106 ? -17.641 35.179 73.128  1.00 22.52 ? 106 PRO A CG  1 
ATOM   914  C CD  . PRO A 1 106 ? -16.892 34.479 74.240  1.00 17.41 ? 106 PRO A CD  1 
ATOM   915  N N   . ILE A 1 107 ? -19.550 31.712 74.818  1.00 14.91 ? 107 ILE A N   1 
ATOM   916  C CA  . ILE A 1 107 ? -20.381 30.524 74.976  1.00 14.16 ? 107 ILE A CA  1 
ATOM   917  C C   . ILE A 1 107 ? -21.109 30.511 76.319  1.00 17.22 ? 107 ILE A C   1 
ATOM   918  O O   . ILE A 1 107 ? -22.037 29.715 76.507  1.00 15.68 ? 107 ILE A O   1 
ATOM   919  C CB  . ILE A 1 107 ? -19.583 29.214 74.805  1.00 18.96 ? 107 ILE A CB  1 
ATOM   920  C CG1 . ILE A 1 107 ? -18.479 29.071 75.849  1.00 15.15 ? 107 ILE A CG1 1 
ATOM   921  C CG2 . ILE A 1 107 ? -19.019 29.111 73.361  1.00 15.07 ? 107 ILE A CG2 1 
ATOM   922  C CD1 . ILE A 1 107 ? -17.857 27.678 75.875  1.00 15.86 ? 107 ILE A CD1 1 
ATOM   923  N N   . TYR A 1 108 ? -20.716 31.382 77.248  1.00 17.69 ? 108 TYR A N   1 
ATOM   924  C CA  . TYR A 1 108 ? -21.401 31.568 78.524  1.00 16.31 ? 108 TYR A CA  1 
ATOM   925  C C   . TYR A 1 108 ? -22.334 32.770 78.512  1.00 20.60 ? 108 TYR A C   1 
ATOM   926  O O   . TYR A 1 108 ? -22.840 33.157 79.571  1.00 20.92 ? 108 TYR A O   1 
ATOM   927  C CB  . TYR A 1 108 ? -20.378 31.697 79.668  1.00 15.49 ? 108 TYR A CB  1 
ATOM   928  C CG  . TYR A 1 108 ? -19.995 30.350 80.254  1.00 14.32 ? 108 TYR A CG  1 
ATOM   929  C CD1 . TYR A 1 108 ? -19.163 29.477 79.555  1.00 14.43 ? 108 TYR A CD1 1 
ATOM   930  C CD2 . TYR A 1 108 ? -20.490 29.942 81.486  1.00 14.76 ? 108 TYR A CD2 1 
ATOM   931  C CE1 . TYR A 1 108 ? -18.833 28.217 80.081  1.00 16.40 ? 108 TYR A CE1 1 
ATOM   932  C CE2 . TYR A 1 108 ? -20.172 28.697 82.020  1.00 18.35 ? 108 TYR A CE2 1 
ATOM   933  C CZ  . TYR A 1 108 ? -19.339 27.842 81.314  1.00 16.65 ? 108 TYR A CZ  1 
ATOM   934  O OH  . TYR A 1 108 ? -19.026 26.606 81.844  1.00 16.39 ? 108 TYR A OH  1 
ATOM   935  N N   . ARG A 1 109 ? -22.615 33.340 77.337  1.00 19.25 ? 109 ARG A N   1 
ATOM   936  C CA  . ARG A 1 109 ? -23.468 34.528 77.242  1.00 24.01 ? 109 ARG A CA  1 
ATOM   937  C C   . ARG A 1 109 ? -24.934 34.119 77.416  1.00 22.85 ? 109 ARG A C   1 
ATOM   938  O O   . ARG A 1 109 ? -25.723 34.032 76.472  1.00 23.08 ? 109 ARG A O   1 
ATOM   939  C CB  . ARG A 1 109 ? -23.246 35.261 75.922  1.00 23.99 ? 109 ARG A CB  1 
ATOM   940  C CG  . ARG A 1 109 ? -23.628 36.722 75.995  1.00 37.33 ? 109 ARG A CG  1 
ATOM   941  C CD  . ARG A 1 109 ? -23.186 37.480 74.746  1.00 49.78 ? 109 ARG A CD  1 
ATOM   942  N NE  . ARG A 1 109 ? -21.757 37.787 74.775  1.00 53.72 ? 109 ARG A NE  1 
ATOM   943  C CZ  . ARG A 1 109 ? -20.968 37.788 73.706  1.00 50.85 ? 109 ARG A CZ  1 
ATOM   944  N NH1 . ARG A 1 109 ? -21.468 37.511 72.506  1.00 54.40 ? 109 ARG A NH1 1 
ATOM   945  N NH2 . ARG A 1 109 ? -19.679 38.083 73.837  1.00 48.60 ? 109 ARG A NH2 1 
ATOM   946  N N   . PHE A 1 110 ? -25.286 33.839 78.666  1.00 22.80 ? 110 PHE A N   1 
ATOM   947  C CA  . PHE A 1 110 ? -26.665 33.646 79.077  1.00 20.40 ? 110 PHE A CA  1 
ATOM   948  C C   . PHE A 1 110 ? -26.980 34.703 80.117  1.00 19.09 ? 110 PHE A C   1 
ATOM   949  O O   . PHE A 1 110 ? -26.256 34.820 81.106  1.00 23.90 ? 110 PHE A O   1 
ATOM   950  C CB  . PHE A 1 110 ? -26.874 32.262 79.694  1.00 22.75 ? 110 PHE A CB  1 
ATOM   951  C CG  . PHE A 1 110 ? -26.677 31.112 78.745  1.00 18.64 ? 110 PHE A CG  1 
ATOM   952  C CD1 . PHE A 1 110 ? -27.729 30.659 77.964  1.00 19.98 ? 110 PHE A CD1 1 
ATOM   953  C CD2 . PHE A 1 110 ? -25.466 30.438 78.696  1.00 18.74 ? 110 PHE A CD2 1 
ATOM   954  C CE1 . PHE A 1 110 ? -27.568 29.577 77.113  1.00 17.80 ? 110 PHE A CE1 1 
ATOM   955  C CE2 . PHE A 1 110 ? -25.295 29.361 77.841  1.00 23.90 ? 110 PHE A CE2 1 
ATOM   956  C CZ  . PHE A 1 110 ? -26.344 28.933 77.051  1.00 20.97 ? 110 PHE A CZ  1 
ATOM   957  N N   . GLU A 1 111 ? -28.064 35.455 79.913  1.00 21.80 ? 111 GLU A N   1 
ATOM   958  C CA  . GLU A 1 111 ? -28.459 36.444 80.908  1.00 22.04 ? 111 GLU A CA  1 
ATOM   959  C C   . GLU A 1 111 ? -28.656 35.808 82.281  1.00 25.78 ? 111 GLU A C   1 
ATOM   960  O O   . GLU A 1 111 ? -28.357 36.435 83.304  1.00 25.23 ? 111 GLU A O   1 
ATOM   961  C CB  . GLU A 1 111 ? -29.738 37.159 80.442  1.00 23.93 ? 111 GLU A CB  1 
ATOM   962  C CG  . GLU A 1 111 ? -30.492 37.889 81.530  1.00 44.93 ? 111 GLU A CG  1 
ATOM   963  C CD  . GLU A 1 111 ? -29.785 39.148 81.988  1.00 56.84 ? 111 GLU A CD  1 
ATOM   964  O OE1 . GLU A 1 111 ? -28.803 39.556 81.321  1.00 63.12 ? 111 GLU A OE1 1 
ATOM   965  O OE2 . GLU A 1 111 ? -30.210 39.723 83.018  1.00 60.56 ? 111 GLU A OE2 1 
ATOM   966  N N   . ARG A 1 112 ? -29.128 34.562 82.322  1.00 20.32 ? 112 ARG A N   1 
ATOM   967  C CA  . ARG A 1 112 ? -29.362 33.906 83.606  1.00 26.76 ? 112 ARG A CA  1 
ATOM   968  C C   . ARG A 1 112 ? -28.053 33.648 84.350  1.00 23.88 ? 112 ARG A C   1 
ATOM   969  O O   . ARG A 1 112 ? -28.027 33.676 85.587  1.00 22.27 ? 112 ARG A O   1 
ATOM   970  C CB  . ARG A 1 112 ? -30.150 32.606 83.376  1.00 19.17 ? 112 ARG A CB  1 
ATOM   971  C CG  . ARG A 1 112 ? -30.401 31.720 84.608  1.00 18.71 ? 112 ARG A CG  1 
ATOM   972  C CD  . ARG A 1 112 ? -31.155 32.459 85.721  1.00 25.03 ? 112 ARG A CD  1 
ATOM   973  N NE  . ARG A 1 112 ? -31.836 31.525 86.621  1.00 27.97 ? 112 ARG A NE  1 
ATOM   974  C CZ  . ARG A 1 112 ? -32.550 31.899 87.680  1.00 30.56 ? 112 ARG A CZ  1 
ATOM   975  N NH1 . ARG A 1 112 ? -32.663 33.187 87.977  1.00 23.74 ? 112 ARG A NH1 1 
ATOM   976  N NH2 . ARG A 1 112 ? -33.151 30.985 88.443  1.00 26.55 ? 112 ARG A NH2 1 
ATOM   977  N N   . ILE A 1 113 ? -26.951 33.425 83.632  1.00 23.39 ? 113 ILE A N   1 
ATOM   978  C CA  . ILE A 1 113 ? -25.673 33.262 84.326  1.00 18.61 ? 113 ILE A CA  1 
ATOM   979  C C   . ILE A 1 113 ? -25.285 34.557 85.029  1.00 18.60 ? 113 ILE A C   1 
ATOM   980  O O   . ILE A 1 113 ? -24.792 34.543 86.171  1.00 25.77 ? 113 ILE A O   1 
ATOM   981  C CB  . ILE A 1 113 ? -24.580 32.794 83.355  1.00 27.28 ? 113 ILE A CB  1 
ATOM   982  C CG1 . ILE A 1 113 ? -24.761 31.314 83.036  1.00 27.98 ? 113 ILE A CG1 1 
ATOM   983  C CG2 . ILE A 1 113 ? -23.203 33.042 83.962  1.00 24.12 ? 113 ILE A CG2 1 
ATOM   984  C CD1 . ILE A 1 113 ? -23.764 30.802 82.049  1.00 39.80 ? 113 ILE A CD1 1 
ATOM   985  N N   . ARG A 1 114 ? -25.530 35.698 84.379  1.00 19.85 ? 114 ARG A N   1 
ATOM   986  C CA  . ARG A 1 114 ? -25.256 36.977 85.018  1.00 22.36 ? 114 ARG A CA  1 
ATOM   987  C C   . ARG A 1 114 ? -26.076 37.128 86.291  1.00 27.15 ? 114 ARG A C   1 
ATOM   988  O O   . ARG A 1 114 ? -25.565 37.600 87.314  1.00 28.72 ? 114 ARG A O   1 
ATOM   989  C CB  . ARG A 1 114 ? -25.537 38.126 84.041  1.00 26.15 ? 114 ARG A CB  1 
ATOM   990  C CG  . ARG A 1 114 ? -24.712 38.034 82.753  1.00 42.78 ? 114 ARG A CG  1 
ATOM   991  C CD  . ARG A 1 114 ? -24.740 39.344 81.944  1.00 59.68 ? 114 ARG A CD  1 
ATOM   992  N NE  . ARG A 1 114 ? -25.657 39.288 80.802  1.00 64.62 ? 114 ARG A NE  1 
ATOM   993  C CZ  . ARG A 1 114 ? -25.491 38.499 79.738  1.00 63.92 ? 114 ARG A CZ  1 
ATOM   994  N NH1 . ARG A 1 114 ? -24.445 37.678 79.660  1.00 60.44 ? 114 ARG A NH1 1 
ATOM   995  N NH2 . ARG A 1 114 ? -26.379 38.525 78.751  1.00 61.92 ? 114 ARG A NH2 1 
ATOM   996  N N   . GLU A 1 115 ? -27.347 36.715 86.247  1.00 33.96 ? 115 GLU A N   1 
ATOM   997  C CA  . GLU A 1 115 ? -28.204 36.801 87.425  1.00 34.96 ? 115 GLU A CA  1 
ATOM   998  C C   . GLU A 1 115 ? -27.679 35.926 88.554  1.00 30.26 ? 115 GLU A C   1 
ATOM   999  O O   . GLU A 1 115 ? -27.643 36.353 89.715  1.00 35.66 ? 115 GLU A O   1 
ATOM   1000 C CB  . GLU A 1 115 ? -29.633 36.392 87.073  1.00 37.85 ? 115 GLU A CB  1 
ATOM   1001 C CG  . GLU A 1 115 ? -30.242 37.121 85.894  1.00 44.34 ? 115 GLU A CG  1 
ATOM   1002 C CD  . GLU A 1 115 ? -31.652 36.640 85.577  1.00 47.94 ? 115 GLU A CD  1 
ATOM   1003 O OE1 . GLU A 1 115 ? -32.241 37.147 84.600  1.00 47.77 ? 115 GLU A OE1 1 
ATOM   1004 O OE2 . GLU A 1 115 ? -32.168 35.756 86.303  1.00 45.37 ? 115 GLU A OE2 1 
ATOM   1005 N N   . LEU A 1 116 ? -27.267 34.697 88.236  1.00 23.43 ? 116 LEU A N   1 
ATOM   1006 C CA  . LEU A 1 116 ? -26.859 33.772 89.284  1.00 24.90 ? 116 LEU A CA  1 
ATOM   1007 C C   . LEU A 1 116 ? -25.562 34.225 89.947  1.00 32.06 ? 116 LEU A C   1 
ATOM   1008 O O   . LEU A 1 116 ? -25.406 34.091 91.169  1.00 34.36 ? 116 LEU A O   1 
ATOM   1009 C CB  . LEU A 1 116 ? -26.712 32.364 88.717  1.00 24.54 ? 116 LEU A CB  1 
ATOM   1010 C CG  . LEU A 1 116 ? -27.946 31.705 88.107  1.00 24.65 ? 116 LEU A CG  1 
ATOM   1011 C CD1 . LEU A 1 116 ? -27.589 30.364 87.460  1.00 20.34 ? 116 LEU A CD1 1 
ATOM   1012 C CD2 . LEU A 1 116 ? -29.049 31.509 89.145  1.00 23.78 ? 116 LEU A CD2 1 
ATOM   1013 N N   . MET A 1 117 ? -24.618 34.769 89.168  1.00 24.90 ? 117 MET A N   1 
ATOM   1014 C CA  . MET A 1 117 ? -23.367 35.224 89.771  1.00 29.72 ? 117 MET A CA  1 
ATOM   1015 C C   . MET A 1 117 ? -23.529 36.502 90.591  1.00 33.08 ? 117 MET A C   1 
ATOM   1016 O O   . MET A 1 117 ? -22.600 36.866 91.318  1.00 39.82 ? 117 MET A O   1 
ATOM   1017 C CB  . MET A 1 117 ? -22.297 35.422 88.685  1.00 29.53 ? 117 MET A CB  1 
ATOM   1018 C CG  . MET A 1 117 ? -21.886 34.119 87.957  1.00 27.91 ? 117 MET A CG  1 
ATOM   1019 S SD  . MET A 1 117 ? -21.224 32.815 89.033  1.00 32.53 ? 117 MET A SD  1 
ATOM   1020 C CE  . MET A 1 117 ? -22.646 31.768 89.281  1.00 30.25 ? 117 MET A CE  1 
ATOM   1021 N N   . ASN A 1 118 ? -24.672 37.184 90.513  1.00 32.90 ? 118 ASN A N   1 
ATOM   1022 C CA  . ASN A 1 118 ? -24.938 38.363 91.327  1.00 34.59 ? 118 ASN A CA  1 
ATOM   1023 C C   . ASN A 1 118 ? -25.853 38.061 92.512  1.00 37.60 ? 118 ASN A C   1 
ATOM   1024 O O   . ASN A 1 118 ? -26.393 38.988 93.119  1.00 47.95 ? 118 ASN A O   1 
ATOM   1025 C CB  . ASN A 1 118 ? -25.544 39.478 90.475  1.00 41.49 ? 118 ASN A CB  1 
ATOM   1026 C CG  . ASN A 1 118 ? -24.571 40.025 89.464  1.00 51.72 ? 118 ASN A CG  1 
ATOM   1027 O OD1 . ASN A 1 118 ? -23.367 39.784 89.552  1.00 62.07 ? 118 ASN A OD1 1 
ATOM   1028 N ND2 . ASN A 1 118 ? -25.084 40.766 88.489  1.00 58.69 ? 118 ASN A ND2 1 
ATOM   1029 N N   . LYS A 1 119 ? -26.028 36.788 92.856  1.00 36.81 ? 119 LYS A N   1 
ATOM   1030 C CA  . LYS A 1 119 ? -26.861 36.377 93.981  1.00 38.90 ? 119 LYS A CA  1 
ATOM   1031 C C   . LYS A 1 119 ? -25.981 36.032 95.172  1.00 40.81 ? 119 LYS A C   1 
ATOM   1032 O O   . LYS A 1 119 ? -25.002 35.294 95.031  1.00 36.41 ? 119 LYS A O   1 
ATOM   1033 C CB  . LYS A 1 119 ? -27.714 35.164 93.616  1.00 35.44 ? 119 LYS A CB  1 
ATOM   1034 C CG  . LYS A 1 119 ? -28.738 35.437 92.560  1.00 36.66 ? 119 LYS A CG  1 
ATOM   1035 C CD  . LYS A 1 119 ? -29.996 35.998 93.167  1.00 44.53 ? 119 LYS A CD  1 
ATOM   1036 C CE  . LYS A 1 119 ? -31.093 36.059 92.115  1.00 49.22 ? 119 LYS A CE  1 
ATOM   1037 N NZ  . LYS A 1 119 ? -31.113 34.790 91.338  1.00 43.21 ? 119 LYS A NZ  1 
ATOM   1038 N N   . GLU A 1 120 ? -26.348 36.544 96.346  1.00 43.99 ? 120 GLU A N   1 
ATOM   1039 C CA  . GLU A 1 120 ? -25.624 36.185 97.561  1.00 49.20 ? 120 GLU A CA  1 
ATOM   1040 C C   . GLU A 1 120 ? -25.776 34.698 97.878  1.00 45.22 ? 120 GLU A C   1 
ATOM   1041 O O   . GLU A 1 120 ? -24.803 34.035 98.256  1.00 40.41 ? 120 GLU A O   1 
ATOM   1042 C CB  . GLU A 1 120 ? -26.115 37.051 98.725  1.00 54.23 ? 120 GLU A CB  1 
ATOM   1043 C CG  . GLU A 1 120 ? -26.187 38.544 98.393  1.00 56.26 ? 120 GLU A CG  1 
ATOM   1044 C CD  . GLU A 1 120 ? -26.343 39.421 99.628  1.00 70.52 ? 120 GLU A CD  1 
ATOM   1045 O OE1 . GLU A 1 120 ? -27.489 39.786 99.975  1.00 72.09 ? 120 GLU A OE1 1 
ATOM   1046 O OE2 . GLU A 1 120 ? -25.311 39.747 100.251 1.00 75.95 ? 120 GLU A OE2 1 
ATOM   1047 N N   . LYS A 1 121 ? -26.978 34.152 97.685  1.00 40.83 ? 121 LYS A N   1 
ATOM   1048 C CA  . LYS A 1 121 ? -27.312 32.776 98.028  1.00 36.52 ? 121 LYS A CA  1 
ATOM   1049 C C   . LYS A 1 121 ? -28.116 32.151 96.897  1.00 33.95 ? 121 LYS A C   1 
ATOM   1050 O O   . LYS A 1 121 ? -28.985 32.810 96.318  1.00 42.45 ? 121 LYS A O   1 
ATOM   1051 C CB  . LYS A 1 121 ? -28.137 32.734 99.317  1.00 38.62 ? 121 LYS A CB  1 
ATOM   1052 C CG  . LYS A 1 121 ? -27.865 31.559 100.204 1.00 46.00 ? 121 LYS A CG  1 
ATOM   1053 C CD  . LYS A 1 121 ? -28.536 31.761 101.549 1.00 51.32 ? 121 LYS A CD  1 
ATOM   1054 C CE  . LYS A 1 121 ? -27.890 32.890 102.339 1.00 58.57 ? 121 LYS A CE  1 
ATOM   1055 N NZ  . LYS A 1 121 ? -28.551 33.094 103.667 1.00 62.53 ? 121 LYS A NZ  1 
ATOM   1056 N N   . LEU A 1 122 ? -27.860 30.876 96.606  1.00 31.16 ? 122 LEU A N   1 
ATOM   1057 C CA  . LEU A 1 122 ? -28.544 30.166 95.526  1.00 24.76 ? 122 LEU A CA  1 
ATOM   1058 C C   . LEU A 1 122 ? -29.491 29.118 96.097  1.00 29.00 ? 122 LEU A C   1 
ATOM   1059 O O   . LEU A 1 122 ? -29.081 28.294 96.920  1.00 31.12 ? 122 LEU A O   1 
ATOM   1060 C CB  . LEU A 1 122 ? -27.540 29.495 94.583  1.00 24.84 ? 122 LEU A CB  1 
ATOM   1061 C CG  . LEU A 1 122 ? -26.610 30.398 93.789  1.00 31.65 ? 122 LEU A CG  1 
ATOM   1062 C CD1 . LEU A 1 122 ? -25.878 29.560 92.751  1.00 34.66 ? 122 LEU A CD1 1 
ATOM   1063 C CD2 . LEU A 1 122 ? -27.424 31.497 93.126  1.00 26.21 ? 122 LEU A CD2 1 
ATOM   1064 N N   . ASN A 1 123 ? -30.751 29.139 95.652  1.00 24.02 ? 123 ASN A N   1 
ATOM   1065 C CA  . ASN A 1 123 ? -31.712 28.122 96.056  1.00 23.10 ? 123 ASN A CA  1 
ATOM   1066 C C   . ASN A 1 123 ? -31.640 26.934 95.088  1.00 20.86 ? 123 ASN A C   1 
ATOM   1067 O O   . ASN A 1 123 ? -30.762 26.852 94.222  1.00 21.75 ? 123 ASN A O   1 
ATOM   1068 C CB  . ASN A 1 123 ? -33.131 28.700 96.161  1.00 25.85 ? 123 ASN A CB  1 
ATOM   1069 C CG  . ASN A 1 123 ? -33.653 29.298 94.846  1.00 25.56 ? 123 ASN A CG  1 
ATOM   1070 O OD1 . ASN A 1 123 ? -33.415 28.787 93.752  1.00 23.62 ? 123 ASN A OD1 1 
ATOM   1071 N ND2 . ASN A 1 123 ? -34.390 30.393 94.969  1.00 29.30 ? 123 ASN A ND2 1 
ATOM   1072 N N   . ARG A 1 124 ? -32.575 25.989 95.235  1.00 19.82 ? 124 ARG A N   1 
ATOM   1073 C CA  . ARG A 1 124 ? -32.504 24.753 94.458  1.00 18.83 ? 124 ARG A CA  1 
ATOM   1074 C C   . ARG A 1 124 ? -32.730 25.018 92.979  1.00 19.50 ? 124 ARG A C   1 
ATOM   1075 O O   . ARG A 1 124 ? -32.033 24.457 92.126  1.00 18.67 ? 124 ARG A O   1 
ATOM   1076 C CB  . ARG A 1 124 ? -33.530 23.737 94.970  1.00 26.05 ? 124 ARG A CB  1 
ATOM   1077 C CG  . ARG A 1 124 ? -33.557 22.432 94.159  1.00 28.54 ? 124 ARG A CG  1 
ATOM   1078 C CD  . ARG A 1 124 ? -34.524 21.391 94.735  1.00 27.91 ? 124 ARG A CD  1 
ATOM   1079 N NE  . ARG A 1 124 ? -34.454 20.103 94.034  1.00 26.91 ? 124 ARG A NE  1 
ATOM   1080 C CZ  . ARG A 1 124 ? -35.004 19.878 92.845  1.00 31.75 ? 124 ARG A CZ  1 
ATOM   1081 N NH1 . ARG A 1 124 ? -35.641 20.860 92.223  1.00 38.05 ? 124 ARG A NH1 1 
ATOM   1082 N NH2 . ARG A 1 124 ? -34.905 18.685 92.265  1.00 37.67 ? 124 ARG A NH2 1 
ATOM   1083 N N   . GLU A 1 125 ? -33.698 25.871 92.646  1.00 23.33 ? 125 GLU A N   1 
ATOM   1084 C CA  . GLU A 1 125 ? -33.957 26.111 91.229  1.00 23.99 ? 125 GLU A CA  1 
ATOM   1085 C C   . GLU A 1 125 ? -32.828 26.895 90.586  1.00 20.73 ? 125 GLU A C   1 
ATOM   1086 O O   . GLU A 1 125 ? -32.529 26.698 89.397  1.00 20.77 ? 125 GLU A O   1 
ATOM   1087 C CB  . GLU A 1 125 ? -35.290 26.840 91.043  1.00 24.30 ? 125 GLU A CB  1 
ATOM   1088 C CG  . GLU A 1 125 ? -36.511 25.954 91.255  1.00 40.78 ? 125 GLU A CG  1 
ATOM   1089 C CD  . GLU A 1 125 ? -36.606 25.374 92.669  1.00 59.09 ? 125 GLU A CD  1 
ATOM   1090 O OE1 . GLU A 1 125 ? -36.422 26.132 93.656  1.00 62.18 ? 125 GLU A OE1 1 
ATOM   1091 O OE2 . GLU A 1 125 ? -36.863 24.155 92.795  1.00 64.09 ? 125 GLU A OE2 1 
ATOM   1092 N N   . GLU A 1 126 ? -32.186 27.777 91.352  1.00 19.99 ? 126 GLU A N   1 
ATOM   1093 C CA  . GLU A 1 126 ? -31.039 28.517 90.839  1.00 19.66 ? 126 GLU A CA  1 
ATOM   1094 C C   . GLU A 1 126 ? -29.825 27.611 90.656  1.00 21.06 ? 126 GLU A C   1 
ATOM   1095 O O   . GLU A 1 126 ? -29.081 27.748 89.679  1.00 17.18 ? 126 GLU A O   1 
ATOM   1096 C CB  . GLU A 1 126 ? -30.730 29.678 91.790  1.00 20.65 ? 126 GLU A CB  1 
ATOM   1097 C CG  . GLU A 1 126 ? -31.710 30.824 91.627  1.00 24.20 ? 126 GLU A CG  1 
ATOM   1098 C CD  . GLU A 1 126 ? -31.860 31.690 92.863  1.00 29.41 ? 126 GLU A CD  1 
ATOM   1099 O OE1 . GLU A 1 126 ? -31.133 31.475 93.860  1.00 31.53 ? 126 GLU A OE1 1 
ATOM   1100 O OE2 . GLU A 1 126 ? -32.713 32.606 92.821  1.00 27.35 ? 126 GLU A OE2 1 
ATOM   1101 N N   . LEU A 1 127 ? -29.613 26.674 91.577  1.00 19.12 ? 127 LEU A N   1 
ATOM   1102 C CA  . LEU A 1 127 ? -28.513 25.728 91.414  1.00 18.81 ? 127 LEU A CA  1 
ATOM   1103 C C   . LEU A 1 127 ? -28.743 24.825 90.208  1.00 17.86 ? 127 LEU A C   1 
ATOM   1104 O O   . LEU A 1 127 ? -27.806 24.520 89.459  1.00 21.79 ? 127 LEU A O   1 
ATOM   1105 C CB  . LEU A 1 127 ? -28.356 24.899 92.686  1.00 19.82 ? 127 LEU A CB  1 
ATOM   1106 C CG  . LEU A 1 127 ? -27.624 25.649 93.804  1.00 19.89 ? 127 LEU A CG  1 
ATOM   1107 C CD1 . LEU A 1 127 ? -27.835 24.916 95.127  1.00 20.02 ? 127 LEU A CD1 1 
ATOM   1108 C CD2 . LEU A 1 127 ? -26.142 25.823 93.482  1.00 23.71 ? 127 LEU A CD2 1 
ATOM   1109 N N   . LEU A 1 128 ? -29.990 24.396 90.000  1.00 16.63 ? 128 LEU A N   1 
ATOM   1110 C CA  . LEU A 1 128 ? -30.293 23.594 88.818  1.00 17.52 ? 128 LEU A CA  1 
ATOM   1111 C C   . LEU A 1 128 ? -29.957 24.358 87.550  1.00 16.80 ? 128 LEU A C   1 
ATOM   1112 O O   . LEU A 1 128 ? -29.465 23.772 86.572  1.00 15.97 ? 128 LEU A O   1 
ATOM   1113 C CB  . LEU A 1 128 ? -31.776 23.199 88.808  1.00 19.79 ? 128 LEU A CB  1 
ATOM   1114 C CG  . LEU A 1 128 ? -32.129 21.757 89.167  1.00 26.87 ? 128 LEU A CG  1 
ATOM   1115 C CD1 . LEU A 1 128 ? -33.631 21.599 89.170  1.00 26.90 ? 128 LEU A CD1 1 
ATOM   1116 C CD2 . LEU A 1 128 ? -31.472 20.790 88.202  1.00 25.85 ? 128 LEU A CD2 1 
ATOM   1117 N N   . ASP A 1 129 ? -30.277 25.661 87.519  1.00 16.89 ? 129 ASP A N   1 
ATOM   1118 C CA  . ASP A 1 129 ? -29.920 26.454 86.346  1.00 18.02 ? 129 ASP A CA  1 
ATOM   1119 C C   . ASP A 1 129 ? -28.413 26.568 86.223  1.00 17.36 ? 129 ASP A C   1 
ATOM   1120 O O   . ASP A 1 129 ? -27.862 26.510 85.115  1.00 17.23 ? 129 ASP A O   1 
ATOM   1121 C CB  . ASP A 1 129 ? -30.554 27.841 86.431  1.00 20.59 ? 129 ASP A CB  1 
ATOM   1122 C CG  . ASP A 1 129 ? -32.024 27.840 86.038  1.00 24.77 ? 129 ASP A CG  1 
ATOM   1123 O OD1 . ASP A 1 129 ? -32.567 26.744 85.729  1.00 25.09 ? 129 ASP A OD1 1 
ATOM   1124 O OD2 . ASP A 1 129 ? -32.641 28.930 86.045  1.00 26.61 ? 129 ASP A OD2 1 
ATOM   1125 N N   . LEU A 1 130 ? -27.723 26.752 87.353  1.00 16.78 ? 130 LEU A N   1 
ATOM   1126 C CA  . LEU A 1 130 ? -26.275 26.848 87.300  1.00 20.99 ? 130 LEU A CA  1 
ATOM   1127 C C   . LEU A 1 130 ? -25.671 25.574 86.720  1.00 16.67 ? 130 LEU A C   1 
ATOM   1128 O O   . LEU A 1 130 ? -24.803 25.629 85.840  1.00 17.50 ? 130 LEU A O   1 
ATOM   1129 C CB  . LEU A 1 130 ? -25.722 27.138 88.687  1.00 20.19 ? 130 LEU A CB  1 
ATOM   1130 C CG  . LEU A 1 130 ? -24.251 27.551 88.621  1.00 20.76 ? 130 LEU A CG  1 
ATOM   1131 C CD1 . LEU A 1 130 ? -24.053 28.787 87.753  1.00 20.66 ? 130 LEU A CD1 1 
ATOM   1132 C CD2 . LEU A 1 130 ? -23.767 27.798 90.040  1.00 28.05 ? 130 LEU A CD2 1 
ATOM   1133 N N   . GLN A 1 131 ? -26.134 24.414 87.197  1.00 17.30 ? 131 GLN A N   1 
ATOM   1134 C CA  . GLN A 1 131 ? -25.661 23.138 86.666  1.00 14.54 ? 131 GLN A CA  1 
ATOM   1135 C C   . GLN A 1 131 ? -25.960 23.012 85.182  1.00 18.71 ? 131 GLN A C   1 
ATOM   1136 O O   . GLN A 1 131 ? -25.099 22.612 84.393  1.00 17.81 ? 131 GLN A O   1 
ATOM   1137 C CB  . GLN A 1 131 ? -26.332 21.976 87.388  1.00 15.18 ? 131 GLN A CB  1 
ATOM   1138 C CG  . GLN A 1 131 ? -26.011 21.857 88.874  1.00 17.79 ? 131 GLN A CG  1 
ATOM   1139 C CD  . GLN A 1 131 ? -26.899 20.837 89.544  1.00 16.48 ? 131 GLN A CD  1 
ATOM   1140 O OE1 . GLN A 1 131 ? -28.136 20.826 89.351  1.00 18.22 ? 131 GLN A OE1 1 
ATOM   1141 N NE2 . GLN A 1 131 ? -26.286 19.956 90.333  1.00 17.88 ? 131 GLN A NE2 1 
ATOM   1142 N N   . THR A 1 132 ? -27.209 23.264 84.798  1.00 12.88 ? 132 THR A N   1 
ATOM   1143 C CA  . THR A 1 132 ? -27.618 22.973 83.430  1.00 13.99 ? 132 THR A CA  1 
ATOM   1144 C C   . THR A 1 132 ? -27.015 23.966 82.449  1.00 16.89 ? 132 THR A C   1 
ATOM   1145 O O   . THR A 1 132 ? -26.668 23.599 81.316  1.00 15.30 ? 132 THR A O   1 
ATOM   1146 C CB  . THR A 1 132 ? -29.143 22.989 83.342  1.00 12.93 ? 132 THR A CB  1 
ATOM   1147 O OG1 . THR A 1 132 ? -29.694 22.125 84.359  1.00 17.70 ? 132 THR A OG1 1 
ATOM   1148 C CG2 . THR A 1 132 ? -29.628 22.520 81.940  1.00 16.29 ? 132 THR A CG2 1 
ATOM   1149 N N   . LEU A 1 133 ? -26.906 25.233 82.844  1.00 18.61 ? 133 LEU A N   1 
ATOM   1150 C CA  . LEU A 1 133 ? -26.317 26.204 81.928  1.00 19.18 ? 133 LEU A CA  1 
ATOM   1151 C C   . LEU A 1 133 ? -24.822 25.978 81.759  1.00 15.70 ? 133 LEU A C   1 
ATOM   1152 O O   . LEU A 1 133 ? -24.275 26.246 80.686  1.00 17.90 ? 133 LEU A O   1 
ATOM   1153 C CB  . LEU A 1 133 ? -26.603 27.631 82.405  1.00 17.80 ? 133 LEU A CB  1 
ATOM   1154 C CG  . LEU A 1 133 ? -28.050 28.091 82.202  1.00 21.16 ? 133 LEU A CG  1 
ATOM   1155 C CD1 . LEU A 1 133 ? -28.398 29.296 83.103  1.00 20.88 ? 133 LEU A CD1 1 
ATOM   1156 C CD2 . LEU A 1 133 ? -28.337 28.407 80.723  1.00 23.93 ? 133 LEU A CD2 1 
ATOM   1157 N N   . ASN A 1 134 ? -24.138 25.470 82.782  1.00 14.31 ? 134 ASN A N   1 
ATOM   1158 C CA  . ASN A 1 134 ? -22.749 25.087 82.568  1.00 15.81 ? 134 ASN A CA  1 
ATOM   1159 C C   . ASN A 1 134 ? -22.646 23.975 81.531  1.00 17.18 ? 134 ASN A C   1 
ATOM   1160 O O   . ASN A 1 134 ? -21.795 24.034 80.636  1.00 20.51 ? 134 ASN A O   1 
ATOM   1161 C CB  . ASN A 1 134 ? -22.104 24.692 83.898  1.00 16.12 ? 134 ASN A CB  1 
ATOM   1162 C CG  . ASN A 1 134 ? -21.398 25.855 84.537  1.00 15.77 ? 134 ASN A CG  1 
ATOM   1163 O OD1 . ASN A 1 134 ? -20.222 26.129 84.246  1.00 15.34 ? 134 ASN A OD1 1 
ATOM   1164 N ND2 . ASN A 1 134 ? -22.119 26.595 85.371  1.00 14.76 ? 134 ASN A ND2 1 
ATOM   1165 N N   . LEU A 1 135 ? -23.540 22.987 81.597  1.00 15.51 ? 135 LEU A N   1 
ATOM   1166 C CA  . LEU A 1 135 ? -23.586 21.943 80.572  1.00 18.90 ? 135 LEU A CA  1 
ATOM   1167 C C   . LEU A 1 135 ? -23.817 22.527 79.182  1.00 20.71 ? 135 LEU A C   1 
ATOM   1168 O O   . LEU A 1 135 ? -23.055 22.261 78.231  1.00 17.32 ? 135 LEU A O   1 
ATOM   1169 C CB  . LEU A 1 135 ? -24.716 20.957 80.887  1.00 20.93 ? 135 LEU A CB  1 
ATOM   1170 C CG  . LEU A 1 135 ? -24.508 19.738 81.777  1.00 24.97 ? 135 LEU A CG  1 
ATOM   1171 C CD1 . LEU A 1 135 ? -25.768 18.860 81.695  1.00 21.01 ? 135 LEU A CD1 1 
ATOM   1172 C CD2 . LEU A 1 135 ? -23.294 18.934 81.362  1.00 18.60 ? 135 LEU A CD2 1 
ATOM   1173 N N   . LEU A 1 136 ? -24.895 23.299 79.046  1.00 14.05 ? 136 LEU A N   1 
ATOM   1174 C CA  . LEU A 1 136 ? -25.331 23.806 77.753  1.00 15.33 ? 136 LEU A CA  1 
ATOM   1175 C C   . LEU A 1 136 ? -24.353 24.815 77.165  1.00 20.92 ? 136 LEU A C   1 
ATOM   1176 O O   . LEU A 1 136 ? -24.299 24.975 75.938  1.00 17.52 ? 136 LEU A O   1 
ATOM   1177 C CB  . LEU A 1 136 ? -26.707 24.434 77.897  1.00 13.93 ? 136 LEU A CB  1 
ATOM   1178 C CG  . LEU A 1 136 ? -27.903 23.476 78.023  1.00 19.08 ? 136 LEU A CG  1 
ATOM   1179 C CD1 . LEU A 1 136 ? -29.174 24.243 78.277  1.00 16.69 ? 136 LEU A CD1 1 
ATOM   1180 C CD2 . LEU A 1 136 ? -27.994 22.662 76.716  1.00 15.54 ? 136 LEU A CD2 1 
ATOM   1181 N N   . ALA A 1 137 ? -23.622 25.551 78.009  1.00 14.29 ? 137 ALA A N   1 
ATOM   1182 C CA  . ALA A 1 137 ? -22.575 26.428 77.479  1.00 17.97 ? 137 ALA A CA  1 
ATOM   1183 C C   . ALA A 1 137 ? -21.586 25.675 76.585  1.00 17.81 ? 137 ALA A C   1 
ATOM   1184 O O   . ALA A 1 137 ? -21.036 26.263 75.641  1.00 19.00 ? 137 ALA A O   1 
ATOM   1185 C CB  . ALA A 1 137 ? -21.823 27.115 78.629  1.00 16.07 ? 137 ALA A CB  1 
ATOM   1186 N N   . TRP A 1 138 ? -21.337 24.391 76.866  1.00 14.74 ? 138 TRP A N   1 
ATOM   1187 C CA  . TRP A 1 138 ? -20.388 23.590 76.109  1.00 15.83 ? 138 TRP A CA  1 
ATOM   1188 C C   . TRP A 1 138 ? -21.046 22.790 74.998  1.00 16.53 ? 138 TRP A C   1 
ATOM   1189 O O   . TRP A 1 138 ? -20.414 21.879 74.454  1.00 15.64 ? 138 TRP A O   1 
ATOM   1190 C CB  . TRP A 1 138 ? -19.605 22.659 77.062  1.00 16.85 ? 138 TRP A CB  1 
ATOM   1191 C CG  . TRP A 1 138 ? -18.768 23.496 77.992  1.00 15.72 ? 138 TRP A CG  1 
ATOM   1192 C CD1 . TRP A 1 138 ? -19.195 24.082 79.166  1.00 16.12 ? 138 TRP A CD1 1 
ATOM   1193 C CD2 . TRP A 1 138 ? -17.396 23.891 77.821  1.00 16.11 ? 138 TRP A CD2 1 
ATOM   1194 N NE1 . TRP A 1 138 ? -18.173 24.813 79.725  1.00 17.92 ? 138 TRP A NE1 1 
ATOM   1195 C CE2 . TRP A 1 138 ? -17.062 24.721 78.921  1.00 16.49 ? 138 TRP A CE2 1 
ATOM   1196 C CE3 . TRP A 1 138 ? -16.413 23.625 76.851  1.00 18.42 ? 138 TRP A CE3 1 
ATOM   1197 C CZ2 . TRP A 1 138 ? -15.791 25.271 79.084  1.00 21.71 ? 138 TRP A CZ2 1 
ATOM   1198 C CZ3 . TRP A 1 138 ? -15.151 24.184 77.017  1.00 23.88 ? 138 TRP A CZ3 1 
ATOM   1199 C CH2 . TRP A 1 138 ? -14.850 24.987 78.127  1.00 23.44 ? 138 TRP A CH2 1 
ATOM   1200 N N   . CYS A 1 139 ? -22.288 23.111 74.634  1.00 14.84 ? 139 CYS A N   1 
ATOM   1201 C CA  . CYS A 1 139 ? -22.979 22.347 73.604  1.00 10.03 ? 139 CYS A CA  1 
ATOM   1202 C C   . CYS A 1 139 ? -22.294 22.515 72.256  1.00 10.08 ? 139 CYS A C   1 
ATOM   1203 O O   . CYS A 1 139 ? -21.960 23.636 71.843  1.00 15.89 ? 139 CYS A O   1 
ATOM   1204 C CB  . CYS A 1 139 ? -24.442 22.790 73.505  1.00 16.33 ? 139 CYS A CB  1 
ATOM   1205 S SG  . CYS A 1 139 ? -25.498 21.690 72.551  1.00 19.05 ? 139 CYS A SG  1 
ATOM   1206 N N   . GLY A 1 140 ? -22.075 21.392 71.565  1.00 14.42 ? 140 GLY A N   1 
ATOM   1207 C CA  . GLY A 1 140 ? -21.514 21.442 70.227  1.00 17.27 ? 140 GLY A CA  1 
ATOM   1208 C C   . GLY A 1 140 ? -22.522 21.749 69.132  1.00 13.58 ? 140 GLY A C   1 
ATOM   1209 O O   . GLY A 1 140 ? -23.732 21.858 69.334  1.00 20.08 ? 140 GLY A O   1 
ATOM   1210 N N   . ARG A 1 141 ? -21.980 21.936 67.927  1.00 10.90 ? 141 ARG A N   1 
ATOM   1211 C CA  . ARG A 1 141 ? -22.777 22.307 66.764  1.00 11.69 ? 141 ARG A CA  1 
ATOM   1212 C C   . ARG A 1 141 ? -23.917 21.327 66.503  1.00 13.15 ? 141 ARG A C   1 
ATOM   1213 O O   . ARG A 1 141 ? -25.047 21.746 66.227  1.00 13.53 ? 141 ARG A O   1 
ATOM   1214 C CB  . ARG A 1 141 ? -21.837 22.405 65.557  1.00 14.23 ? 141 ARG A CB  1 
ATOM   1215 C CG  . ARG A 1 141 ? -22.525 22.645 64.244  1.00 15.60 ? 141 ARG A CG  1 
ATOM   1216 C CD  . ARG A 1 141 ? -21.457 22.743 63.149  1.00 14.27 ? 141 ARG A CD  1 
ATOM   1217 N NE  . ARG A 1 141 ? -22.100 22.873 61.855  1.00 16.72 ? 141 ARG A NE  1 
ATOM   1218 C CZ  . ARG A 1 141 ? -22.252 21.873 60.990  1.00 19.46 ? 141 ARG A CZ  1 
ATOM   1219 N NH1 . ARG A 1 141 ? -21.754 20.666 61.258  1.00 18.40 ? 141 ARG A NH1 1 
ATOM   1220 N NH2 . ARG A 1 141 ? -22.882 22.101 59.841  1.00 19.56 ? 141 ARG A NH2 1 
ATOM   1221 N N   . THR A 1 142 ? -23.634 20.021 66.565  1.00 14.71 ? 142 THR A N   1 
ATOM   1222 C CA  . THR A 1 142 ? -24.648 19.019 66.219  1.00 14.36 ? 142 THR A CA  1 
ATOM   1223 C C   . THR A 1 142 ? -25.847 19.103 67.158  1.00 15.53 ? 142 THR A C   1 
ATOM   1224 O O   . THR A 1 142 ? -27.005 19.140 66.718  1.00 18.22 ? 142 THR A O   1 
ATOM   1225 C CB  . THR A 1 142 ? -24.029 17.611 66.267  1.00 17.11 ? 142 THR A CB  1 
ATOM   1226 O OG1 . THR A 1 142 ? -22.974 17.503 65.292  1.00 19.15 ? 142 THR A OG1 1 
ATOM   1227 C CG2 . THR A 1 142 ? -25.077 16.540 66.000  1.00 19.43 ? 142 THR A CG2 1 
ATOM   1228 N N   . LEU A 1 143 ? -25.590 19.123 68.464  1.00 17.74 ? 143 LEU A N   1 
ATOM   1229 C CA  . LEU A 1 143 ? -26.693 19.195 69.412  1.00 17.69 ? 143 LEU A CA  1 
ATOM   1230 C C   . LEU A 1 143 ? -27.246 20.601 69.581  1.00 22.54 ? 143 LEU A C   1 
ATOM   1231 O O   . LEU A 1 143 ? -28.346 20.745 70.114  1.00 22.03 ? 143 LEU A O   1 
ATOM   1232 C CB  . LEU A 1 143 ? -26.263 18.655 70.776  1.00 15.35 ? 143 LEU A CB  1 
ATOM   1233 C CG  . LEU A 1 143 ? -26.064 17.148 70.799  1.00 11.46 ? 143 LEU A CG  1 
ATOM   1234 C CD1 . LEU A 1 143 ? -25.676 16.726 72.230  1.00 11.78 ? 143 LEU A CD1 1 
ATOM   1235 C CD2 . LEU A 1 143 ? -27.307 16.377 70.326  1.00 15.32 ? 143 LEU A CD2 1 
ATOM   1236 N N   . ARG A 1 144 ? -26.498 21.644 69.202  1.00 19.03 ? 144 ARG A N   1 
ATOM   1237 C CA  . ARG A 1 144 ? -27.094 22.975 69.230  1.00 24.19 ? 144 ARG A CA  1 
ATOM   1238 C C   . ARG A 1 144 ? -28.301 23.052 68.315  1.00 25.81 ? 144 ARG A C   1 
ATOM   1239 O O   . ARG A 1 144 ? -29.269 23.767 68.615  1.00 27.67 ? 144 ARG A O   1 
ATOM   1240 C CB  . ARG A 1 144 ? -26.080 24.051 68.858  1.00 20.97 ? 144 ARG A CB  1 
ATOM   1241 C CG  . ARG A 1 144 ? -25.192 24.468 70.056  1.00 29.14 ? 144 ARG A CG  1 
ATOM   1242 C CD  . ARG A 1 144 ? -24.195 25.529 69.657  1.00 25.28 ? 144 ARG A CD  1 
ATOM   1243 N NE  . ARG A 1 144 ? -23.390 26.001 70.771  1.00 29.18 ? 144 ARG A NE  1 
ATOM   1244 C CZ  . ARG A 1 144 ? -23.483 27.220 71.299  1.00 23.53 ? 144 ARG A CZ  1 
ATOM   1245 N NH1 . ARG A 1 144 ? -24.374 28.089 70.836  1.00 28.09 ? 144 ARG A NH1 1 
ATOM   1246 N NH2 . ARG A 1 144 ? -22.697 27.564 72.316  1.00 25.38 ? 144 ARG A NH2 1 
ATOM   1247 N N   . LYS A 1 145 ? -28.292 22.311 67.210  1.00 30.39 ? 145 LYS A N   1 
ATOM   1248 C CA  . LYS A 1 145 ? -29.513 22.222 66.417  1.00 27.75 ? 145 LYS A CA  1 
ATOM   1249 C C   . LYS A 1 145 ? -30.571 21.412 67.133  1.00 24.33 ? 145 LYS A C   1 
ATOM   1250 O O   . LYS A 1 145 ? -31.734 21.810 67.176  1.00 31.73 ? 145 LYS A O   1 
ATOM   1251 C CB  . LYS A 1 145 ? -29.254 21.574 65.048  1.00 43.98 ? 145 LYS A CB  1 
ATOM   1252 C CG  . LYS A 1 145 ? -29.312 22.525 63.881  1.00 56.53 ? 145 LYS A CG  1 
ATOM   1253 C CD  . LYS A 1 145 ? -28.390 23.661 64.172  1.00 58.72 ? 145 LYS A CD  1 
ATOM   1254 C CE  . LYS A 1 145 ? -27.001 23.151 64.006  1.00 59.06 ? 145 LYS A CE  1 
ATOM   1255 N NZ  . LYS A 1 145 ? -25.979 24.110 64.512  1.00 62.22 ? 145 LYS A NZ  1 
ATOM   1256 N N   . ASP A 1 146 ? -30.187 20.263 67.685  1.00 29.26 ? 146 ASP A N   1 
ATOM   1257 C CA  . ASP A 1 146 ? -31.155 19.333 68.256  1.00 25.47 ? 146 ASP A CA  1 
ATOM   1258 C C   . ASP A 1 146 ? -31.744 19.829 69.579  1.00 34.68 ? 146 ASP A C   1 
ATOM   1259 O O   . ASP A 1 146 ? -32.912 19.545 69.872  1.00 42.29 ? 146 ASP A O   1 
ATOM   1260 C CB  . ASP A 1 146 ? -30.500 17.972 68.457  1.00 30.43 ? 146 ASP A CB  1 
ATOM   1261 C CG  . ASP A 1 146 ? -29.972 17.371 67.161  1.00 39.82 ? 146 ASP A CG  1 
ATOM   1262 O OD1 . ASP A 1 146 ? -30.281 17.888 66.061  1.00 47.56 ? 146 ASP A OD1 1 
ATOM   1263 O OD2 . ASP A 1 146 ? -29.243 16.367 67.251  1.00 40.35 ? 146 ASP A OD2 1 
ATOM   1264 N N   . LEU A 1 147 ? -30.960 20.542 70.402  1.00 25.07 ? 147 LEU A N   1 
ATOM   1265 C CA  . LEU A 1 147 ? -31.399 21.031 71.707  1.00 22.81 ? 147 LEU A CA  1 
ATOM   1266 C C   . LEU A 1 147 ? -31.825 22.500 71.670  1.00 26.14 ? 147 LEU A C   1 
ATOM   1267 O O   . LEU A 1 147 ? -31.909 23.147 72.725  1.00 21.49 ? 147 LEU A O   1 
ATOM   1268 C CB  . LEU A 1 147 ? -30.295 20.838 72.746  1.00 19.46 ? 147 LEU A CB  1 
ATOM   1269 C CG  . LEU A 1 147 ? -29.762 19.425 72.984  1.00 24.86 ? 147 LEU A CG  1 
ATOM   1270 C CD1 . LEU A 1 147 ? -28.593 19.426 73.950  1.00 25.59 ? 147 LEU A CD1 1 
ATOM   1271 C CD2 . LEU A 1 147 ? -30.868 18.526 73.485  1.00 37.35 ? 147 LEU A CD2 1 
ATOM   1272 N N   . LYS A 1 148 ? -32.095 23.031 70.471  1.00 22.01 ? 148 LYS A N   1 
ATOM   1273 C CA  . LYS A 1 148 ? -32.450 24.439 70.305  1.00 27.59 ? 148 LYS A CA  1 
ATOM   1274 C C   . LYS A 1 148 ? -33.524 24.885 71.292  1.00 26.79 ? 148 LYS A C   1 
ATOM   1275 O O   . LYS A 1 148 ? -33.447 25.989 71.847  1.00 27.18 ? 148 LYS A O   1 
ATOM   1276 C CB  . LYS A 1 148 ? -32.949 24.668 68.876  1.00 30.75 ? 148 LYS A CB  1 
ATOM   1277 C CG  . LYS A 1 148 ? -32.428 25.917 68.197  1.00 45.65 ? 148 LYS A CG  1 
ATOM   1278 C CD  . LYS A 1 148 ? -33.046 26.054 66.809  1.00 51.02 ? 148 LYS A CD  1 
ATOM   1279 C CE  . LYS A 1 148 ? -34.334 26.877 66.835  1.00 56.93 ? 148 LYS A CE  1 
ATOM   1280 N NZ  . LYS A 1 148 ? -34.830 27.156 65.450  1.00 58.27 ? 148 LYS A NZ  1 
ATOM   1281 N N   . ASP A 1 149 ? -34.553 24.054 71.490  1.00 26.12 ? 149 ASP A N   1 
ATOM   1282 C CA  . ASP A 1 149 ? -35.637 24.406 72.403  1.00 27.06 ? 149 ASP A CA  1 
ATOM   1283 C C   . ASP A 1 149 ? -35.095 24.661 73.803  1.00 25.59 ? 149 ASP A C   1 
ATOM   1284 O O   . ASP A 1 149 ? -35.416 25.675 74.434  1.00 29.75 ? 149 ASP A O   1 
ATOM   1285 C CB  . ASP A 1 149 ? -36.683 23.288 72.443  1.00 34.60 ? 149 ASP A CB  1 
ATOM   1286 C CG  . ASP A 1 149 ? -37.493 23.181 71.154  1.00 39.12 ? 149 ASP A CG  1 
ATOM   1287 O OD1 . ASP A 1 149 ? -37.314 24.032 70.248  1.00 33.86 ? 149 ASP A OD1 1 
ATOM   1288 O OD2 . ASP A 1 149 ? -38.303 22.227 71.044  1.00 38.09 ? 149 ASP A OD2 1 
ATOM   1289 N N   . LEU A 1 150 ? -34.267 23.742 74.307  1.00 18.55 ? 150 LEU A N   1 
ATOM   1290 C CA  . LEU A 1 150 ? -33.741 23.900 75.659  1.00 23.19 ? 150 LEU A CA  1 
ATOM   1291 C C   . LEU A 1 150 ? -32.726 25.033 75.739  1.00 25.27 ? 150 LEU A C   1 
ATOM   1292 O O   . LEU A 1 150 ? -32.621 25.707 76.772  1.00 22.79 ? 150 LEU A O   1 
ATOM   1293 C CB  . LEU A 1 150 ? -33.105 22.592 76.120  1.00 25.88 ? 150 LEU A CB  1 
ATOM   1294 C CG  . LEU A 1 150 ? -34.058 21.474 76.544  1.00 27.94 ? 150 LEU A CG  1 
ATOM   1295 C CD1 . LEU A 1 150 ? -33.219 20.299 77.065  1.00 23.32 ? 150 LEU A CD1 1 
ATOM   1296 C CD2 . LEU A 1 150 ? -35.040 21.963 77.615  1.00 17.50 ? 150 LEU A CD2 1 
ATOM   1297 N N   . LEU A 1 151 ? -31.978 25.266 74.662  1.00 22.81 ? 151 LEU A N   1 
ATOM   1298 C CA  . LEU A 1 151 ? -30.960 26.314 74.687  1.00 19.20 ? 151 LEU A CA  1 
ATOM   1299 C C   . LEU A 1 151 ? -31.583 27.698 74.750  1.00 29.13 ? 151 LEU A C   1 
ATOM   1300 O O   . LEU A 1 151 ? -31.063 28.584 75.437  1.00 27.17 ? 151 LEU A O   1 
ATOM   1301 C CB  . LEU A 1 151 ? -30.075 26.199 73.445  1.00 21.18 ? 151 LEU A CB  1 
ATOM   1302 C CG  . LEU A 1 151 ? -28.831 25.335 73.565  1.00 21.03 ? 151 LEU A CG  1 
ATOM   1303 C CD1 . LEU A 1 151 ? -28.259 25.210 72.169  1.00 30.36 ? 151 LEU A CD1 1 
ATOM   1304 C CD2 . LEU A 1 151 ? -27.830 25.965 74.521  1.00 21.72 ? 151 LEU A CD2 1 
ATOM   1305 N N   . ASN A 1 152 ? -32.692 27.908 74.026  1.00 29.72 ? 152 ASN A N   1 
ATOM   1306 C CA  . ASN A 1 152 ? -33.361 29.207 74.006  1.00 29.45 ? 152 ASN A CA  1 
ATOM   1307 C C   . ASN A 1 152 ? -34.140 29.493 75.280  1.00 28.13 ? 152 ASN A C   1 
ATOM   1308 O O   . ASN A 1 152 ? -34.433 30.657 75.564  1.00 36.28 ? 152 ASN A O   1 
ATOM   1309 C CB  . ASN A 1 152 ? -34.315 29.307 72.807  1.00 28.50 ? 152 ASN A CB  1 
ATOM   1310 C CG  . ASN A 1 152 ? -33.586 29.335 71.481  1.00 39.13 ? 152 ASN A CG  1 
ATOM   1311 O OD1 . ASN A 1 152 ? -32.397 29.654 71.423  1.00 54.48 ? 152 ASN A OD1 1 
ATOM   1312 N ND2 . ASN A 1 152 ? -34.299 29.019 70.403  1.00 48.91 ? 152 ASN A ND2 1 
ATOM   1313 N N   . LYS A 1 153 ? -34.499 28.458 76.035  1.00 31.89 ? 153 LYS A N   1 
ATOM   1314 C CA  . LYS A 1 153 ? -35.195 28.662 77.297  1.00 28.48 ? 153 LYS A CA  1 
ATOM   1315 C C   . LYS A 1 153 ? -34.352 29.537 78.226  1.00 31.96 ? 153 LYS A C   1 
ATOM   1316 O O   . LYS A 1 153 ? -34.848 30.510 78.811  1.00 28.42 ? 153 LYS A O   1 
ATOM   1317 C CB  . LYS A 1 153 ? -35.520 27.288 77.896  1.00 26.39 ? 153 LYS A CB  1 
ATOM   1318 C CG  . LYS A 1 153 ? -36.121 27.297 79.255  1.00 33.04 ? 153 LYS A CG  1 
ATOM   1319 C CD  . LYS A 1 153 ? -36.118 25.898 79.880  1.00 25.68 ? 153 LYS A CD  1 
ATOM   1320 C CE  . LYS A 1 153 ? -37.130 25.875 80.987  1.00 26.56 ? 153 LYS A CE  1 
ATOM   1321 N NZ  . LYS A 1 153 ? -37.494 24.508 81.435  1.00 49.83 ? 153 LYS A NZ  1 
ATOM   1322 N N   . GLY A 1 154 ? -33.058 29.232 78.325  1.00 31.13 ? 154 GLY A N   1 
ATOM   1323 C CA  . GLY A 1 154 ? -32.076 30.049 79.023  1.00 29.00 ? 154 GLY A CA  1 
ATOM   1324 C C   . GLY A 1 154 ? -32.160 30.045 80.534  1.00 21.29 ? 154 GLY A C   1 
ATOM   1325 O O   . GLY A 1 154 ? -31.317 30.681 81.180  1.00 22.75 ? 154 GLY A O   1 
ATOM   1326 N N   . ARG A 1 155 ? -33.134 29.359 81.122  1.00 20.38 ? 155 ARG A N   1 
ATOM   1327 C CA  . ARG A 1 155 ? -33.376 29.458 82.558  1.00 23.31 ? 155 ARG A CA  1 
ATOM   1328 C C   . ARG A 1 155 ? -34.465 28.456 82.903  1.00 22.52 ? 155 ARG A C   1 
ATOM   1329 O O   . ARG A 1 155 ? -35.049 27.836 82.018  1.00 28.09 ? 155 ARG A O   1 
ATOM   1330 C CB  . ARG A 1 155 ? -33.795 30.872 82.962  1.00 28.49 ? 155 ARG A CB  1 
ATOM   1331 C CG  . ARG A 1 155 ? -35.179 31.229 82.442  1.00 27.22 ? 155 ARG A CG  1 
ATOM   1332 C CD  . ARG A 1 155 ? -35.552 32.644 82.794  1.00 34.66 ? 155 ARG A CD  1 
ATOM   1333 N NE  . ARG A 1 155 ? -34.616 33.597 82.215  1.00 43.12 ? 155 ARG A NE  1 
ATOM   1334 C CZ  . ARG A 1 155 ? -33.970 34.508 82.931  1.00 42.14 ? 155 ARG A CZ  1 
ATOM   1335 N NH1 . ARG A 1 155 ? -33.123 35.340 82.340  1.00 48.75 ? 155 ARG A NH1 1 
ATOM   1336 N NH2 . ARG A 1 155 ? -34.174 34.579 84.237  1.00 35.23 ? 155 ARG A NH2 1 
ATOM   1337 N N   . ASN A 1 156 ? -34.711 28.288 84.199  1.00 23.59 ? 156 ASN A N   1 
ATOM   1338 C CA  . ASN A 1 156 ? -35.805 27.452 84.704  1.00 25.97 ? 156 ASN A CA  1 
ATOM   1339 C C   . ASN A 1 156 ? -35.680 26.001 84.240  1.00 24.86 ? 156 ASN A C   1 
ATOM   1340 O O   . ASN A 1 156 ? -36.661 25.379 83.842  1.00 30.17 ? 156 ASN A O   1 
ATOM   1341 C CB  . ASN A 1 156 ? -37.172 28.022 84.297  1.00 29.01 ? 156 ASN A CB  1 
ATOM   1342 C CG  . ASN A 1 156 ? -37.376 29.435 84.785  1.00 33.08 ? 156 ASN A CG  1 
ATOM   1343 O OD1 . ASN A 1 156 ? -36.977 29.779 85.896  1.00 32.57 ? 156 ASN A OD1 1 
ATOM   1344 N ND2 . ASN A 1 156 ? -37.982 30.268 83.949  1.00 30.58 ? 156 ASN A ND2 1 
ATOM   1345 N N   . TYR A 1 157 ? -34.478 25.444 84.311  1.00 20.06 ? 157 TYR A N   1 
ATOM   1346 C CA  . TYR A 1 157 ? -34.294 24.060 83.908  1.00 19.35 ? 157 TYR A CA  1 
ATOM   1347 C C   . TYR A 1 157 ? -34.716 23.105 85.015  1.00 21.49 ? 157 TYR A C   1 
ATOM   1348 O O   . TYR A 1 157 ? -34.628 23.413 86.205  1.00 21.95 ? 157 TYR A O   1 
ATOM   1349 C CB  . TYR A 1 157 ? -32.843 23.800 83.529  1.00 13.87 ? 157 TYR A CB  1 
ATOM   1350 C CG  . TYR A 1 157 ? -32.440 24.577 82.313  1.00 15.18 ? 157 TYR A CG  1 
ATOM   1351 C CD1 . TYR A 1 157 ? -32.818 24.146 81.051  1.00 13.93 ? 157 TYR A CD1 1 
ATOM   1352 C CD2 . TYR A 1 157 ? -31.721 25.765 82.426  1.00 17.89 ? 157 TYR A CD2 1 
ATOM   1353 C CE1 . TYR A 1 157 ? -32.465 24.862 79.915  1.00 17.21 ? 157 TYR A CE1 1 
ATOM   1354 C CE2 . TYR A 1 157 ? -31.371 26.493 81.299  1.00 17.25 ? 157 TYR A CE2 1 
ATOM   1355 C CZ  . TYR A 1 157 ? -31.747 26.027 80.050  1.00 20.12 ? 157 TYR A CZ  1 
ATOM   1356 O OH  . TYR A 1 157 ? -31.403 26.730 78.911  1.00 16.30 ? 157 TYR A OH  1 
ATOM   1357 N N   . THR A 1 158 ? -35.197 21.940 84.606  1.00 17.31 ? 158 THR A N   1 
ATOM   1358 C CA  . THR A 1 158 ? -35.587 20.891 85.534  1.00 16.50 ? 158 THR A CA  1 
ATOM   1359 C C   . THR A 1 158 ? -34.525 19.800 85.548  1.00 20.48 ? 158 THR A C   1 
ATOM   1360 O O   . THR A 1 158 ? -33.664 19.709 84.654  1.00 17.42 ? 158 THR A O   1 
ATOM   1361 C CB  . THR A 1 158 ? -36.935 20.284 85.147  1.00 16.47 ? 158 THR A CB  1 
ATOM   1362 O OG1 . THR A 1 158 ? -36.789 19.578 83.900  1.00 16.39 ? 158 THR A OG1 1 
ATOM   1363 C CG2 . THR A 1 158 ? -38.003 21.370 85.006  1.00 18.96 ? 158 THR A CG2 1 
ATOM   1364 N N   . GLN A 1 159 ? -34.590 18.956 86.585  1.00 19.82 ? 159 GLN A N   1 
ATOM   1365 C CA  . GLN A 1 159 ? -33.667 17.821 86.658  1.00 16.48 ? 159 GLN A CA  1 
ATOM   1366 C C   . GLN A 1 159 ? -33.846 16.900 85.452  1.00 18.81 ? 159 GLN A C   1 
ATOM   1367 O O   . GLN A 1 159 ? -32.869 16.359 84.922  1.00 18.36 ? 159 GLN A O   1 
ATOM   1368 C CB  . GLN A 1 159 ? -33.885 17.058 87.975  1.00 21.70 ? 159 GLN A CB  1 
ATOM   1369 C CG  . GLN A 1 159 ? -33.034 15.793 88.153  1.00 22.62 ? 159 GLN A CG  1 
ATOM   1370 C CD  . GLN A 1 159 ? -31.591 16.099 88.542  1.00 28.19 ? 159 GLN A CD  1 
ATOM   1371 O OE1 . GLN A 1 159 ? -31.297 17.165 89.076  1.00 21.81 ? 159 GLN A OE1 1 
ATOM   1372 N NE2 . GLN A 1 159 ? -30.684 15.153 88.275  1.00 23.02 ? 159 GLN A NE2 1 
ATOM   1373 N N   . GLU A 1 160 ? -35.090 16.733 84.974  1.00 16.71 ? 160 GLU A N   1 
ATOM   1374 C CA  . GLU A 1 160 ? -35.297 15.866 83.814  1.00 18.20 ? 160 GLU A CA  1 
ATOM   1375 C C   . GLU A 1 160 ? -34.627 16.436 82.575  1.00 17.12 ? 160 GLU A C   1 
ATOM   1376 O O   . GLU A 1 160 ? -34.062 15.687 81.766  1.00 15.82 ? 160 GLU A O   1 
ATOM   1377 C CB  . GLU A 1 160 ? -36.789 15.646 83.548  1.00 25.32 ? 160 GLU A CB  1 
ATOM   1378 C CG  . GLU A 1 160 ? -37.061 14.746 82.346  1.00 30.37 ? 160 GLU A CG  1 
ATOM   1379 C CD  . GLU A 1 160 ? -37.068 13.263 82.711  1.00 53.14 ? 160 GLU A CD  1 
ATOM   1380 O OE1 . GLU A 1 160 ? -37.458 12.442 81.851  1.00 63.28 ? 160 GLU A OE1 1 
ATOM   1381 O OE2 . GLU A 1 160 ? -36.692 12.917 83.859  1.00 56.67 ? 160 GLU A OE2 1 
ATOM   1382 N N   . GLU A 1 161 ? -34.685 17.756 82.398  1.00 18.26 ? 161 GLU A N   1 
ATOM   1383 C CA  . GLU A 1 161 ? -34.055 18.359 81.225  1.00 17.82 ? 161 GLU A CA  1 
ATOM   1384 C C   . GLU A 1 161 ? -32.540 18.253 81.295  1.00 19.75 ? 161 GLU A C   1 
ATOM   1385 O O   . GLU A 1 161 ? -31.872 17.950 80.297  1.00 14.81 ? 161 GLU A O   1 
ATOM   1386 C CB  . GLU A 1 161 ? -34.494 19.823 81.100  1.00 17.04 ? 161 GLU A CB  1 
ATOM   1387 C CG  . GLU A 1 161 ? -35.971 19.949 80.707  1.00 17.63 ? 161 GLU A CG  1 
ATOM   1388 C CD  . GLU A 1 161 ? -36.532 21.345 80.906  1.00 20.22 ? 161 GLU A CD  1 
ATOM   1389 O OE1 . GLU A 1 161 ? -35.884 22.154 81.587  1.00 20.62 ? 161 GLU A OE1 1 
ATOM   1390 O OE2 . GLU A 1 161 ? -37.650 21.622 80.385  1.00 22.24 ? 161 GLU A OE2 1 
ATOM   1391 N N   . LYS A 1 162 ? -31.979 18.516 82.470  1.00 15.87 ? 162 LYS A N   1 
ATOM   1392 C CA  . LYS A 1 162 ? -30.544 18.373 82.656  1.00 16.77 ? 162 LYS A CA  1 
ATOM   1393 C C   . LYS A 1 162 ? -30.085 16.955 82.304  1.00 15.24 ? 162 LYS A C   1 
ATOM   1394 O O   . LYS A 1 162 ? -29.099 16.774 81.578  1.00 17.31 ? 162 LYS A O   1 
ATOM   1395 C CB  . LYS A 1 162 ? -30.200 18.733 84.102  1.00 13.77 ? 162 LYS A CB  1 
ATOM   1396 C CG  . LYS A 1 162 ? -28.702 18.569 84.400  1.00 12.44 ? 162 LYS A CG  1 
ATOM   1397 C CD  . LYS A 1 162 ? -28.415 18.966 85.850  1.00 18.53 ? 162 LYS A CD  1 
ATOM   1398 C CE  . LYS A 1 162 ? -29.080 18.050 86.834  1.00 18.19 ? 162 LYS A CE  1 
ATOM   1399 N NZ  . LYS A 1 162 ? -28.805 18.456 88.269  1.00 17.06 ? 162 LYS A NZ  1 
ATOM   1400 N N   . GLU A 1 163 ? -30.813 15.939 82.788  1.00 14.01 ? 163 GLU A N   1 
ATOM   1401 C CA  . GLU A 1 163 ? -30.459 14.545 82.499  1.00 17.32 ? 163 GLU A CA  1 
ATOM   1402 C C   . GLU A 1 163 ? -30.597 14.213 81.018  1.00 20.91 ? 163 GLU A C   1 
ATOM   1403 O O   . GLU A 1 163 ? -29.810 13.412 80.476  1.00 20.06 ? 163 GLU A O   1 
ATOM   1404 C CB  . GLU A 1 163 ? -31.326 13.598 83.335  1.00 26.84 ? 163 GLU A CB  1 
ATOM   1405 C CG  . GLU A 1 163 ? -31.004 13.640 84.836  1.00 22.29 ? 163 GLU A CG  1 
ATOM   1406 C CD  . GLU A 1 163 ? -31.944 12.779 85.667  1.00 32.30 ? 163 GLU A CD  1 
ATOM   1407 O OE1 . GLU A 1 163 ? -31.806 12.783 86.910  1.00 32.00 ? 163 GLU A OE1 1 
ATOM   1408 O OE2 . GLU A 1 163 ? -32.824 12.102 85.086  1.00 37.33 ? 163 GLU A OE2 1 
ATOM   1409 N N   . TYR A 1 164 ? -31.582 14.815 80.343  1.00 18.21 ? 164 TYR A N   1 
ATOM   1410 C CA  . TYR A 1 164 ? -31.737 14.601 78.911  1.00 18.62 ? 164 TYR A CA  1 
ATOM   1411 C C   . TYR A 1 164 ? -30.525 15.133 78.157  1.00 20.55 ? 164 TYR A C   1 
ATOM   1412 O O   . TYR A 1 164 ? -30.001 14.467 77.262  1.00 17.77 ? 164 TYR A O   1 
ATOM   1413 C CB  . TYR A 1 164 ? -33.022 15.278 78.436  1.00 19.66 ? 164 TYR A CB  1 
ATOM   1414 C CG  . TYR A 1 164 ? -33.307 15.164 76.947  1.00 23.74 ? 164 TYR A CG  1 
ATOM   1415 C CD1 . TYR A 1 164 ? -33.931 14.040 76.433  1.00 26.31 ? 164 TYR A CD1 1 
ATOM   1416 C CD2 . TYR A 1 164 ? -32.965 16.188 76.066  1.00 24.79 ? 164 TYR A CD2 1 
ATOM   1417 C CE1 . TYR A 1 164 ? -34.204 13.925 75.074  1.00 33.14 ? 164 TYR A CE1 1 
ATOM   1418 C CE2 . TYR A 1 164 ? -33.229 16.080 74.704  1.00 29.63 ? 164 TYR A CE2 1 
ATOM   1419 C CZ  . TYR A 1 164 ? -33.851 14.944 74.220  1.00 32.91 ? 164 TYR A CZ  1 
ATOM   1420 O OH  . TYR A 1 164 ? -34.129 14.802 72.872  1.00 32.94 ? 164 TYR A OH  1 
ATOM   1421 N N   . VAL A 1 165 ? -30.065 16.333 78.515  1.00 15.00 ? 165 VAL A N   1 
ATOM   1422 C CA  . VAL A 1 165 ? -28.850 16.900 77.931  1.00 14.06 ? 165 VAL A CA  1 
ATOM   1423 C C   . VAL A 1 165 ? -27.651 15.991 78.187  1.00 18.16 ? 165 VAL A C   1 
ATOM   1424 O O   . VAL A 1 165 ? -26.867 15.689 77.272  1.00 15.35 ? 165 VAL A O   1 
ATOM   1425 C CB  . VAL A 1 165 ? -28.606 18.316 78.480  1.00 18.36 ? 165 VAL A CB  1 
ATOM   1426 C CG1 . VAL A 1 165 ? -27.228 18.794 78.059  1.00 17.97 ? 165 VAL A CG1 1 
ATOM   1427 C CG2 . VAL A 1 165 ? -29.698 19.285 78.001  1.00 16.68 ? 165 VAL A CG2 1 
ATOM   1428 N N   . LEU A 1 166 ? -27.506 15.525 79.428  1.00 15.85 ? 166 LEU A N   1 
ATOM   1429 C CA  . LEU A 1 166 ? -26.401 14.633 79.760  1.00 14.49 ? 166 LEU A CA  1 
ATOM   1430 C C   . LEU A 1 166 ? -26.412 13.391 78.892  1.00 14.00 ? 166 LEU A C   1 
ATOM   1431 O O   . LEU A 1 166 ? -25.354 12.949 78.408  1.00 16.18 ? 166 LEU A O   1 
ATOM   1432 C CB  . LEU A 1 166 ? -26.469 14.222 81.227  1.00 15.61 ? 166 LEU A CB  1 
ATOM   1433 C CG  . LEU A 1 166 ? -25.805 15.207 82.170  1.00 24.54 ? 166 LEU A CG  1 
ATOM   1434 C CD1 . LEU A 1 166 ? -26.166 14.829 83.598  1.00 22.48 ? 166 LEU A CD1 1 
ATOM   1435 C CD2 . LEU A 1 166 ? -24.301 15.186 81.958  1.00 26.04 ? 166 LEU A CD2 1 
ATOM   1436 N N   . ASN A 1 167 ? -27.598 12.814 78.679  1.00 14.53 ? 167 ASN A N   1 
ATOM   1437 C CA  . ASN A 1 167 ? -27.677 11.607 77.869  1.00 22.49 ? 167 ASN A CA  1 
ATOM   1438 C C   . ASN A 1 167 ? -27.279 11.890 76.430  1.00 20.15 ? 167 ASN A C   1 
ATOM   1439 O O   . ASN A 1 167 ? -26.554 11.096 75.818  1.00 17.82 ? 167 ASN A O   1 
ATOM   1440 C CB  . ASN A 1 167 ? -29.081 11.005 77.927  1.00 22.25 ? 167 ASN A CB  1 
ATOM   1441 C CG  . ASN A 1 167 ? -29.385 10.382 79.269  1.00 41.03 ? 167 ASN A CG  1 
ATOM   1442 O OD1 . ASN A 1 167 ? -28.460 10.024 79.995  1.00 45.75 ? 167 ASN A OD1 1 
ATOM   1443 N ND2 . ASN A 1 167 ? -30.671 10.281 79.622  1.00 47.36 ? 167 ASN A ND2 1 
ATOM   1444 N N   . LYS A 1 168 ? -27.754 13.005 75.869  1.00 16.17 ? 168 LYS A N   1 
ATOM   1445 C CA  . LYS A 1 168 ? -27.368 13.325 74.498  1.00 18.19 ? 168 LYS A CA  1 
ATOM   1446 C C   . LYS A 1 168 ? -25.861 13.557 74.395  1.00 20.02 ? 168 LYS A C   1 
ATOM   1447 O O   . LYS A 1 168 ? -25.226 13.146 73.418  1.00 14.91 ? 168 LYS A O   1 
ATOM   1448 C CB  . LYS A 1 168 ? -28.152 14.543 73.998  1.00 19.06 ? 168 LYS A CB  1 
ATOM   1449 C CG  . LYS A 1 168 ? -29.645 14.295 73.800  1.00 23.43 ? 168 LYS A CG  1 
ATOM   1450 C CD  . LYS A 1 168 ? -29.893 13.476 72.532  1.00 37.55 ? 168 LYS A CD  1 
ATOM   1451 C CE  . LYS A 1 168 ? -31.101 12.575 72.670  1.00 43.52 ? 168 LYS A CE  1 
ATOM   1452 N NZ  . LYS A 1 168 ? -31.111 11.517 71.602  1.00 45.90 ? 168 LYS A NZ  1 
ATOM   1453 N N   . TYR A 1 169 ? -25.269 14.190 75.408  1.00 16.82 ? 169 TYR A N   1 
ATOM   1454 C CA  . TYR A 1 169 ? -23.827 14.442 75.403  1.00 17.39 ? 169 TYR A CA  1 
ATOM   1455 C C   . TYR A 1 169 ? -23.032 13.143 75.369  1.00 17.05 ? 169 TYR A C   1 
ATOM   1456 O O   . TYR A 1 169 ? -22.034 13.046 74.646  1.00 16.33 ? 169 TYR A O   1 
ATOM   1457 C CB  . TYR A 1 169 ? -23.433 15.272 76.628  1.00 12.66 ? 169 TYR A CB  1 
ATOM   1458 C CG  . TYR A 1 169 ? -23.668 16.772 76.481  1.00 12.68 ? 169 TYR A CG  1 
ATOM   1459 C CD1 . TYR A 1 169 ? -24.481 17.284 75.470  1.00 10.88 ? 169 TYR A CD1 1 
ATOM   1460 C CD2 . TYR A 1 169 ? -23.057 17.663 77.354  1.00 17.26 ? 169 TYR A CD2 1 
ATOM   1461 C CE1 . TYR A 1 169 ? -24.700 18.652 75.349  1.00 12.97 ? 169 TYR A CE1 1 
ATOM   1462 C CE2 . TYR A 1 169 ? -23.257 19.037 77.243  1.00 18.92 ? 169 TYR A CE2 1 
ATOM   1463 C CZ  . TYR A 1 169 ? -24.078 19.518 76.239  1.00 15.45 ? 169 TYR A CZ  1 
ATOM   1464 O OH  . TYR A 1 169 ? -24.265 20.867 76.138  1.00 17.51 ? 169 TYR A OH  1 
ATOM   1465 N N   . PHE A 1 170 ? -23.453 12.131 76.137  1.00 14.45 ? 170 PHE A N   1 
ATOM   1466 C CA  . PHE A 1 170 ? -22.695 10.888 76.122  1.00 17.41 ? 170 PHE A CA  1 
ATOM   1467 C C   . PHE A 1 170 ? -22.893 10.139 74.811  1.00 17.45 ? 170 PHE A C   1 
ATOM   1468 O O   . PHE A 1 170 ? -21.983 9.427  74.374  1.00 17.87 ? 170 PHE A O   1 
ATOM   1469 C CB  . PHE A 1 170 ? -23.036 10.022 77.337  1.00 19.53 ? 170 PHE A CB  1 
ATOM   1470 C CG  . PHE A 1 170 ? -22.212 10.387 78.566  1.00 21.26 ? 170 PHE A CG  1 
ATOM   1471 C CD1 . PHE A 1 170 ? -20.909 9.904  78.720  1.00 22.23 ? 170 PHE A CD1 1 
ATOM   1472 C CD2 . PHE A 1 170 ? -22.715 11.262 79.524  1.00 24.83 ? 170 PHE A CD2 1 
ATOM   1473 C CE1 . PHE A 1 170 ? -20.129 10.255 79.844  1.00 28.59 ? 170 PHE A CE1 1 
ATOM   1474 C CE2 . PHE A 1 170 ? -21.961 11.603 80.653  1.00 22.94 ? 170 PHE A CE2 1 
ATOM   1475 C CZ  . PHE A 1 170 ? -20.664 11.109 80.809  1.00 22.68 ? 170 PHE A CZ  1 
ATOM   1476 N N   . GLU A 1 171 ? -24.033 10.338 74.142  1.00 17.87 ? 171 GLU A N   1 
ATOM   1477 C CA  . GLU A 1 171 ? -24.217 9.744  72.818  1.00 20.39 ? 171 GLU A CA  1 
ATOM   1478 C C   . GLU A 1 171 ? -23.209 10.316 71.834  1.00 16.89 ? 171 GLU A C   1 
ATOM   1479 O O   . GLU A 1 171 ? -22.641 9.577  71.020  1.00 18.09 ? 171 GLU A O   1 
ATOM   1480 C CB  . GLU A 1 171 ? -25.651 9.971  72.316  1.00 18.69 ? 171 GLU A CB  1 
ATOM   1481 C CG  . GLU A 1 171 ? -26.715 9.078  72.961  1.00 31.20 ? 171 GLU A CG  1 
ATOM   1482 C CD  . GLU A 1 171 ? -28.148 9.420  72.525  1.00 45.94 ? 171 GLU A CD  1 
ATOM   1483 O OE1 . GLU A 1 171 ? -28.340 10.306 71.662  1.00 46.92 ? 171 GLU A OE1 1 
ATOM   1484 O OE2 . GLU A 1 171 ? -29.095 8.797  73.062  1.00 55.85 ? 171 GLU A OE2 1 
ATOM   1485 N N   . ILE A 1 172 ? -22.950 11.626 71.930  1.00 13.46 ? 172 ILE A N   1 
ATOM   1486 C CA  . ILE A 1 172 ? -21.954 12.279 71.083  1.00 17.17 ? 172 ILE A CA  1 
ATOM   1487 C C   . ILE A 1 172 ? -20.573 11.691 71.363  1.00 15.44 ? 172 ILE A C   1 
ATOM   1488 O O   . ILE A 1 172 ? -19.819 11.344 70.449  1.00 18.86 ? 172 ILE A O   1 
ATOM   1489 C CB  . ILE A 1 172 ? -21.976 13.804 71.310  1.00 15.69 ? 172 ILE A CB  1 
ATOM   1490 C CG1 . ILE A 1 172 ? -23.225 14.438 70.682  1.00 21.29 ? 172 ILE A CG1 1 
ATOM   1491 C CG2 . ILE A 1 172 ? -20.687 14.488 70.789  1.00 19.69 ? 172 ILE A CG2 1 
ATOM   1492 C CD1 . ILE A 1 172 ? -23.314 14.351 69.141  1.00 21.41 ? 172 ILE A CD1 1 
ATOM   1493 N N   . ILE A 1 173 ? -20.232 11.561 72.637  1.00 15.72 ? 173 ILE A N   1 
ATOM   1494 C CA  . ILE A 1 173 ? -18.936 10.988 72.977  1.00 12.57 ? 173 ILE A CA  1 
ATOM   1495 C C   . ILE A 1 173 ? -18.801 9.578  72.410  1.00 11.24 ? 173 ILE A C   1 
ATOM   1496 O O   . ILE A 1 173 ? -17.752 9.209  71.869  1.00 17.12 ? 173 ILE A O   1 
ATOM   1497 C CB  . ILE A 1 173 ? -18.729 11.017 74.497  1.00 17.46 ? 173 ILE A CB  1 
ATOM   1498 C CG1 . ILE A 1 173 ? -18.645 12.478 74.957  1.00 14.81 ? 173 ILE A CG1 1 
ATOM   1499 C CG2 . ILE A 1 173 ? -17.457 10.263 74.868  1.00 19.65 ? 173 ILE A CG2 1 
ATOM   1500 C CD1 . ILE A 1 173 ? -18.562 12.640 76.496  1.00 16.13 ? 173 ILE A CD1 1 
ATOM   1501 N N   . LYS A 1 174 ? -19.850 8.762  72.539  1.00 15.18 ? 174 LYS A N   1 
ATOM   1502 C CA  . LYS A 1 174 ? -19.771 7.391  72.043  1.00 14.84 ? 174 LYS A CA  1 
ATOM   1503 C C   . LYS A 1 174 ? -19.520 7.319  70.539  1.00 16.00 ? 174 LYS A C   1 
ATOM   1504 O O   . LYS A 1 174 ? -19.025 6.293  70.058  1.00 18.12 ? 174 LYS A O   1 
ATOM   1505 C CB  . LYS A 1 174 ? -21.066 6.641  72.371  1.00 15.42 ? 174 LYS A CB  1 
ATOM   1506 C CG  . LYS A 1 174 ? -21.232 6.319  73.846  1.00 15.19 ? 174 LYS A CG  1 
ATOM   1507 C CD  . LYS A 1 174 ? -22.397 5.351  74.063  1.00 29.44 ? 174 LYS A CD  1 
ATOM   1508 C CE  . LYS A 1 174 ? -23.065 5.567  75.411  1.00 43.34 ? 174 LYS A CE  1 
ATOM   1509 N NZ  . LYS A 1 174 ? -22.083 5.444  76.529  1.00 52.16 ? 174 LYS A NZ  1 
ATOM   1510 N N   . LYS A 1 175 ? -19.882 8.356  69.790  1.00 16.80 ? 175 LYS A N   1 
ATOM   1511 C CA  . LYS A 1 175 ? -19.711 8.385  68.334  1.00 19.49 ? 175 LYS A CA  1 
ATOM   1512 C C   . LYS A 1 175 ? -18.393 9.030  67.880  1.00 19.34 ? 175 LYS A C   1 
ATOM   1513 O O   . LYS A 1 175 ? -18.157 9.157  66.669  1.00 17.16 ? 175 LYS A O   1 
ATOM   1514 C CB  . LYS A 1 175 ? -20.883 9.144  67.700  1.00 18.18 ? 175 LYS A CB  1 
ATOM   1515 C CG  . LYS A 1 175 ? -22.183 8.342  67.705  1.00 35.47 ? 175 LYS A CG  1 
ATOM   1516 C CD  . LYS A 1 175 ? -23.414 9.250  67.673  1.00 44.23 ? 175 LYS A CD  1 
ATOM   1517 C CE  . LYS A 1 175 ? -23.315 10.299 66.593  1.00 48.30 ? 175 LYS A CE  1 
ATOM   1518 N NZ  . LYS A 1 175 ? -24.663 10.834 66.228  1.00 61.54 ? 175 LYS A NZ  1 
ATOM   1519 N N   . THR A 1 176 ? -17.527 9.424  68.810  1.00 14.83 ? 176 THR A N   1 
ATOM   1520 C CA  . THR A 1 176 ? -16.446 10.351 68.451  1.00 16.41 ? 176 THR A CA  1 
ATOM   1521 C C   . THR A 1 176 ? -15.279 9.650  67.733  1.00 18.88 ? 176 THR A C   1 
ATOM   1522 O O   . THR A 1 176 ? -14.836 10.105 66.668  1.00 19.01 ? 176 THR A O   1 
ATOM   1523 C CB  . THR A 1 176 ? -15.970 11.089 69.701  1.00 19.48 ? 176 THR A CB  1 
ATOM   1524 O OG1 . THR A 1 176 ? -17.000 11.992 70.144  1.00 17.30 ? 176 THR A OG1 1 
ATOM   1525 C CG2 . THR A 1 176 ? -14.695 11.898 69.414  1.00 11.06 ? 176 THR A CG2 1 
ATOM   1526 N N   . LEU A 1 177 ? -14.742 8.556  68.290  1.00 17.37 ? 177 LEU A N   1 
ATOM   1527 C CA  . LEU A 1 177 ? -13.650 7.888  67.582  1.00 14.18 ? 177 LEU A CA  1 
ATOM   1528 C C   . LEU A 1 177 ? -14.112 7.353  66.233  1.00 14.48 ? 177 LEU A C   1 
ATOM   1529 O O   . LEU A 1 177 ? -13.338 7.354  65.260  1.00 16.53 ? 177 LEU A O   1 
ATOM   1530 C CB  . LEU A 1 177 ? -13.060 6.767  68.446  1.00 16.08 ? 177 LEU A CB  1 
ATOM   1531 C CG  . LEU A 1 177 ? -12.350 7.320  69.691  1.00 19.31 ? 177 LEU A CG  1 
ATOM   1532 C CD1 . LEU A 1 177 ? -11.818 6.191  70.608  1.00 23.14 ? 177 LEU A CD1 1 
ATOM   1533 C CD2 . LEU A 1 177 ? -11.223 8.295  69.309  1.00 20.35 ? 177 LEU A CD2 1 
ATOM   1534 N N   . SER A 1 178 ? -15.390 6.976  66.130  1.00 15.29 ? 178 SER A N   1 
ATOM   1535 C CA  . SER A 1 178 ? -15.903 6.430  64.875  1.00 17.71 ? 178 SER A CA  1 
ATOM   1536 C C   . SER A 1 178 ? -15.915 7.481  63.772  1.00 22.36 ? 178 SER A C   1 
ATOM   1537 O O   . SER A 1 178 ? -15.654 7.163  62.607  1.00 19.17 ? 178 SER A O   1 
ATOM   1538 C CB  . SER A 1 178 ? -17.310 5.865  65.073  1.00 19.51 ? 178 SER A CB  1 
ATOM   1539 O OG  . SER A 1 178 ? -17.277 4.666  65.831  1.00 24.15 ? 178 SER A OG  1 
ATOM   1540 N N   . ILE A 1 179 ? -16.233 8.738  64.106  1.00 17.98 ? 179 ILE A N   1 
ATOM   1541 C CA  . ILE A 1 179 ? -16.283 9.736  63.035  1.00 16.52 ? 179 ILE A CA  1 
ATOM   1542 C C   . ILE A 1 179 ? -14.885 10.021 62.501  1.00 14.98 ? 179 ILE A C   1 
ATOM   1543 O O   . ILE A 1 179 ? -14.708 10.263 61.297  1.00 14.78 ? 179 ILE A O   1 
ATOM   1544 C CB  . ILE A 1 179 ? -17.017 11.025 63.476  1.00 18.71 ? 179 ILE A CB  1 
ATOM   1545 C CG1 . ILE A 1 179 ? -17.408 11.819 62.221  1.00 19.67 ? 179 ILE A CG1 1 
ATOM   1546 C CG2 . ILE A 1 179 ? -16.181 11.871 64.432  1.00 16.20 ? 179 ILE A CG2 1 
ATOM   1547 C CD1 . ILE A 1 179 ? -18.425 12.875 62.455  1.00 33.63 ? 179 ILE A CD1 1 
ATOM   1548 N N   . TYR A 1 180 ? -13.862 9.983  63.363  1.00 14.62 ? 180 TYR A N   1 
ATOM   1549 C CA  . TYR A 1 180 ? -12.502 10.140 62.858  1.00 13.49 ? 180 TYR A CA  1 
ATOM   1550 C C   . TYR A 1 180 ? -12.145 8.990  61.931  1.00 12.07 ? 180 TYR A C   1 
ATOM   1551 O O   . TYR A 1 180 ? -11.491 9.192  60.903  1.00 15.41 ? 180 TYR A O   1 
ATOM   1552 C CB  . TYR A 1 180 ? -11.499 10.225 64.012  1.00 14.45 ? 180 TYR A CB  1 
ATOM   1553 C CG  . TYR A 1 180 ? -11.530 11.551 64.752  1.00 11.96 ? 180 TYR A CG  1 
ATOM   1554 C CD1 . TYR A 1 180 ? -10.952 12.686 64.201  1.00 11.99 ? 180 TYR A CD1 1 
ATOM   1555 C CD2 . TYR A 1 180 ? -12.171 11.672 65.987  1.00 14.80 ? 180 TYR A CD2 1 
ATOM   1556 C CE1 . TYR A 1 180 ? -10.965 13.903 64.858  1.00 15.12 ? 180 TYR A CE1 1 
ATOM   1557 C CE2 . TYR A 1 180 ? -12.207 12.896 66.659  1.00 14.33 ? 180 TYR A CE2 1 
ATOM   1558 C CZ  . TYR A 1 180 ? -11.605 14.011 66.068  1.00 14.38 ? 180 TYR A CZ  1 
ATOM   1559 O OH  . TYR A 1 180 ? -11.608 15.262 66.683  1.00 13.34 ? 180 TYR A OH  1 
ATOM   1560 N N   . ARG A 1 181 ? -12.504 7.772  62.313  1.00 12.29 ? 181 ARG A N   1 
ATOM   1561 C CA  . ARG A 1 181 ? -12.247 6.641  61.431  1.00 13.58 ? 181 ARG A CA  1 
ATOM   1562 C C   . ARG A 1 181 ? -13.015 6.798  60.124  1.00 16.83 ? 181 ARG A C   1 
ATOM   1563 O O   . ARG A 1 181 ? -12.473 6.529  59.038  1.00 16.66 ? 181 ARG A O   1 
ATOM   1564 C CB  . ARG A 1 181 ? -12.630 5.341  62.138  1.00 13.73 ? 181 ARG A CB  1 
ATOM   1565 C CG  . ARG A 1 181 ? -12.367 4.103  61.343  1.00 22.00 ? 181 ARG A CG  1 
ATOM   1566 C CD  . ARG A 1 181 ? -12.811 2.862  62.117  1.00 20.17 ? 181 ARG A CD  1 
ATOM   1567 N NE  . ARG A 1 181 ? -12.148 2.797  63.412  1.00 17.17 ? 181 ARG A NE  1 
ATOM   1568 C CZ  . ARG A 1 181 ? -12.769 2.888  64.585  1.00 18.76 ? 181 ARG A CZ  1 
ATOM   1569 N NH1 . ARG A 1 181 ? -14.087 3.038  64.652  1.00 22.61 ? 181 ARG A NH1 1 
ATOM   1570 N NH2 . ARG A 1 181 ? -12.063 2.821  65.714  1.00 16.01 ? 181 ARG A NH2 1 
ATOM   1571 N N   . GLU A 1 182 ? -14.280 7.249  60.204  1.00 15.65 ? 182 GLU A N   1 
ATOM   1572 C CA  . GLU A 1 182 ? -15.066 7.417  58.980  1.00 15.88 ? 182 GLU A CA  1 
ATOM   1573 C C   . GLU A 1 182 ? -14.433 8.456  58.052  1.00 15.65 ? 182 GLU A C   1 
ATOM   1574 O O   . GLU A 1 182 ? -14.234 8.192  56.862  1.00 14.78 ? 182 GLU A O   1 
ATOM   1575 C CB  . GLU A 1 182 ? -16.523 7.804  59.291  1.00 21.15 ? 182 GLU A CB  1 
ATOM   1576 C CG  . GLU A 1 182 ? -17.348 8.040  57.995  1.00 22.04 ? 182 GLU A CG  1 
ATOM   1577 C CD  . GLU A 1 182 ? -18.843 8.359  58.207  1.00 28.96 ? 182 GLU A CD  1 
ATOM   1578 O OE1 . GLU A 1 182 ? -19.591 8.440  57.189  1.00 25.03 ? 182 GLU A OE1 1 
ATOM   1579 O OE2 . GLU A 1 182 ? -19.280 8.530  59.367  1.00 25.68 ? 182 GLU A OE2 1 
ATOM   1580 N N   . ILE A 1 183 ? -14.148 9.662  58.555  1.00 14.05 ? 183 ILE A N   1 
ATOM   1581 C CA  . ILE A 1 183 ? -13.638 10.670 57.622  1.00 18.59 ? 183 ILE A CA  1 
ATOM   1582 C C   . ILE A 1 183 ? -12.289 10.246 57.058  1.00 18.06 ? 183 ILE A C   1 
ATOM   1583 O O   . ILE A 1 183 ? -11.957 10.587 55.913  1.00 17.79 ? 183 ILE A O   1 
ATOM   1584 C CB  . ILE A 1 183 ? -13.580 12.081 58.251  1.00 15.73 ? 183 ILE A CB  1 
ATOM   1585 C CG1 . ILE A 1 183 ? -12.578 12.145 59.420  1.00 19.11 ? 183 ILE A CG1 1 
ATOM   1586 C CG2 . ILE A 1 183 ? -14.979 12.509 58.715  1.00 15.70 ? 183 ILE A CG2 1 
ATOM   1587 C CD1 . ILE A 1 183 ? -11.184 12.715 59.056  1.00 18.17 ? 183 ILE A CD1 1 
ATOM   1588 N N   . LYS A 1 184 ? -11.503 9.472  57.822  1.00 15.66 ? 184 LYS A N   1 
ATOM   1589 C CA  . LYS A 1 184 ? -10.260 8.928  57.285  1.00 17.21 ? 184 LYS A CA  1 
ATOM   1590 C C   . LYS A 1 184 ? -10.530 7.923  56.169  1.00 13.97 ? 184 LYS A C   1 
ATOM   1591 O O   . LYS A 1 184 ? -9.961  8.022  55.069  1.00 16.13 ? 184 LYS A O   1 
ATOM   1592 C CB  . LYS A 1 184 ? -9.448  8.283  58.420  1.00 18.69 ? 184 LYS A CB  1 
ATOM   1593 C CG  . LYS A 1 184 ? -8.192  7.583  57.937  1.00 17.04 ? 184 LYS A CG  1 
ATOM   1594 C CD  . LYS A 1 184 ? -7.313  7.119  59.102  1.00 20.10 ? 184 LYS A CD  1 
ATOM   1595 C CE  . LYS A 1 184 ? -6.100  6.348  58.584  1.00 26.04 ? 184 LYS A CE  1 
ATOM   1596 N NZ  . LYS A 1 184 ? -6.454  5.098  57.859  1.00 29.62 ? 184 LYS A NZ  1 
ATOM   1597 N N   . GLU A 1 185 ? -11.414 6.951  56.427  1.00 18.07 ? 185 GLU A N   1 
ATOM   1598 C CA  . GLU A 1 185 ? -11.714 5.931  55.418  1.00 18.46 ? 185 GLU A CA  1 
ATOM   1599 C C   . GLU A 1 185 ? -12.293 6.563  54.157  1.00 18.34 ? 185 GLU A C   1 
ATOM   1600 O O   . GLU A 1 185 ? -12.048 6.083  53.042  1.00 19.68 ? 185 GLU A O   1 
ATOM   1601 C CB  . GLU A 1 185 ? -12.664 4.862  55.983  1.00 19.57 ? 185 GLU A CB  1 
ATOM   1602 C CG  . GLU A 1 185 ? -12.959 3.682  55.022  1.00 34.99 ? 185 GLU A CG  1 
ATOM   1603 C CD  . GLU A 1 185 ? -13.906 4.019  53.882  1.00 50.05 ? 185 GLU A CD  1 
ATOM   1604 O OE1 . GLU A 1 185 ? -14.079 3.162  52.981  1.00 43.39 ? 185 GLU A OE1 1 
ATOM   1605 O OE2 . GLU A 1 185 ? -14.515 5.107  53.944  1.00 54.33 ? 185 GLU A OE2 1 
ATOM   1606 N N   . GLU A 1 186 ? -13.094 7.612  54.312  1.00 14.42 ? 186 GLU A N   1 
ATOM   1607 C CA  . GLU A 1 186 ? -13.747 8.211  53.156  1.00 14.87 ? 186 GLU A CA  1 
ATOM   1608 C C   . GLU A 1 186 ? -12.833 9.158  52.386  1.00 18.60 ? 186 GLU A C   1 
ATOM   1609 O O   . GLU A 1 186 ? -13.260 9.688  51.361  1.00 21.77 ? 186 GLU A O   1 
ATOM   1610 C CB  . GLU A 1 186 ? -15.022 8.951  53.607  1.00 17.54 ? 186 GLU A CB  1 
ATOM   1611 C CG  . GLU A 1 186 ? -16.028 8.039  54.324  1.00 20.14 ? 186 GLU A CG  1 
ATOM   1612 C CD  . GLU A 1 186 ? -17.357 8.734  54.719  1.00 23.13 ? 186 GLU A CD  1 
ATOM   1613 O OE1 . GLU A 1 186 ? -17.418 9.970  54.899  1.00 20.96 ? 186 GLU A OE1 1 
ATOM   1614 O OE2 . GLU A 1 186 ? -18.357 8.014  54.861  1.00 23.42 ? 186 GLU A OE2 1 
ATOM   1615 N N   . GLY A 1 187 ? -11.600 9.377  52.846  1.00 16.53 ? 187 GLY A N   1 
ATOM   1616 C CA  . GLY A 1 187 ? -10.699 10.296 52.162  1.00 19.49 ? 187 GLY A CA  1 
ATOM   1617 C C   . GLY A 1 187 ? -11.004 11.755 52.397  1.00 18.30 ? 187 GLY A C   1 
ATOM   1618 O O   . GLY A 1 187 ? -10.516 12.615 51.650  1.00 18.13 ? 187 GLY A O   1 
ATOM   1619 N N   . LYS A 1 188 ? -11.817 12.064 53.408  1.00 16.99 ? 188 LYS A N   1 
ATOM   1620 C CA  . LYS A 1 188 ? -12.127 13.449 53.732  1.00 15.41 ? 188 LYS A CA  1 
ATOM   1621 C C   . LYS A 1 188 ? -11.039 14.096 54.581  1.00 14.05 ? 188 LYS A C   1 
ATOM   1622 O O   . LYS A 1 188 ? -10.950 15.325 54.631  1.00 16.49 ? 188 LYS A O   1 
ATOM   1623 C CB  . LYS A 1 188 ? -13.475 13.521 54.460  1.00 15.22 ? 188 LYS A CB  1 
ATOM   1624 C CG  . LYS A 1 188 ? -14.698 13.145 53.588  1.00 17.57 ? 188 LYS A CG  1 
ATOM   1625 C CD  . LYS A 1 188 ? -15.996 13.213 54.405  1.00 17.81 ? 188 LYS A CD  1 
ATOM   1626 C CE  . LYS A 1 188 ? -17.195 13.150 53.485  1.00 23.55 ? 188 LYS A CE  1 
ATOM   1627 N NZ  . LYS A 1 188 ? -17.194 11.879 52.743  1.00 20.33 ? 188 LYS A NZ  1 
ATOM   1628 N N   . GLY A 1 189 ? -10.202 13.306 55.237  1.00 13.18 ? 189 GLY A N   1 
ATOM   1629 C CA  . GLY A 1 189 ? -9.083  13.873 55.972  1.00 15.96 ? 189 GLY A CA  1 
ATOM   1630 C C   . GLY A 1 189 ? -8.115  12.781 56.350  1.00 17.34 ? 189 GLY A C   1 
ATOM   1631 O O   . GLY A 1 189 ? -8.449  11.596 56.296  1.00 19.84 ? 189 GLY A O   1 
ATOM   1632 N N   . SER A 1 190 ? -6.895  13.193 56.712  1.00 13.59 ? 190 SER A N   1 
ATOM   1633 C CA  . SER A 1 190 ? -5.936  12.279 57.315  1.00 16.35 ? 190 SER A CA  1 
ATOM   1634 C C   . SER A 1 190 ? -5.963  12.484 58.821  1.00 15.22 ? 190 SER A C   1 
ATOM   1635 O O   . SER A 1 190 ? -6.341  13.555 59.303  1.00 16.00 ? 190 SER A O   1 
ATOM   1636 C CB  . SER A 1 190 ? -4.514  12.508 56.784  1.00 18.83 ? 190 SER A CB  1 
ATOM   1637 O OG  . SER A 1 190 ? -4.406  12.259 55.384  1.00 18.31 ? 190 SER A OG  1 
ATOM   1638 N N   . VAL A 1 191 ? -5.590  11.441 59.567  1.00 14.68 ? 191 VAL A N   1 
ATOM   1639 C CA  . VAL A 1 191 ? -5.488  11.542 61.022  1.00 13.06 ? 191 VAL A CA  1 
ATOM   1640 C C   . VAL A 1 191 ? -4.055  11.219 61.417  1.00 13.63 ? 191 VAL A C   1 
ATOM   1641 O O   . VAL A 1 191 ? -3.508  10.197 60.994  1.00 15.35 ? 191 VAL A O   1 
ATOM   1642 C CB  . VAL A 1 191 ? -6.475  10.614 61.752  1.00 15.28 ? 191 VAL A CB  1 
ATOM   1643 C CG1 . VAL A 1 191 ? -6.371  10.824 63.280  1.00 11.75 ? 191 VAL A CG1 1 
ATOM   1644 C CG2 . VAL A 1 191 ? -7.901  10.881 61.301  1.00 19.46 ? 191 VAL A CG2 1 
ATOM   1645 N N   . SER A 1 192 ? -3.460  12.081 62.218  1.00 14.16 ? 192 SER A N   1 
ATOM   1646 C CA  . SER A 1 192 ? -2.120  11.887 62.746  1.00 16.27 ? 192 SER A CA  1 
ATOM   1647 C C   . SER A 1 192 ? -2.213  11.603 64.237  1.00 13.70 ? 192 SER A C   1 
ATOM   1648 O O   . SER A 1 192 ? -3.287  11.649 64.842  1.00 12.76 ? 192 SER A O   1 
ATOM   1649 C CB  . SER A 1 192 ? -1.256  13.118 62.495  1.00 14.67 ? 192 SER A CB  1 
ATOM   1650 O OG  . SER A 1 192 ? -1.793  14.236 63.212  1.00 14.73 ? 192 SER A OG  1 
ATOM   1651 N N   . THR A 1 193 ? -1.066  11.300 64.839  1.00 13.36 ? 193 THR A N   1 
ATOM   1652 C CA  . THR A 1 193 ? -0.994  11.247 66.297  1.00 11.56 ? 193 THR A CA  1 
ATOM   1653 C C   . THR A 1 193 ? 0.317   11.892 66.728  1.00 15.09 ? 193 THR A C   1 
ATOM   1654 O O   . THR A 1 193 ? 1.081   12.386 65.898  1.00 13.94 ? 193 THR A O   1 
ATOM   1655 C CB  . THR A 1 193 ? -1.138  9.802  66.818  1.00 15.97 ? 193 THR A CB  1 
ATOM   1656 O OG1 . THR A 1 193 ? -1.409  9.832  68.224  1.00 16.49 ? 193 THR A OG1 1 
ATOM   1657 C CG2 . THR A 1 193 ? 0.124   8.977  66.570  1.00 13.99 ? 193 THR A CG2 1 
ATOM   1658 N N   . SER A 1 194 ? 0.543   11.941 68.034  1.00 12.94 ? 194 SER A N   1 
ATOM   1659 C CA  . SER A 1 194 ? 1.746   12.486 68.641  1.00 13.49 ? 194 SER A CA  1 
ATOM   1660 C C   . SER A 1 194 ? 2.335   11.431 69.562  1.00 15.95 ? 194 SER A C   1 
ATOM   1661 O O   . SER A 1 194 ? 1.614   10.540 70.024  1.00 13.32 ? 194 SER A O   1 
ATOM   1662 C CB  . SER A 1 194 ? 1.453   13.747 69.472  1.00 13.58 ? 194 SER A CB  1 
ATOM   1663 O OG  . SER A 1 194 ? 1.003   14.836 68.676  1.00 13.89 ? 194 SER A OG  1 
ATOM   1664 N N   . PRO A 1 195 ? 3.628   11.541 69.905  1.00 15.75 ? 195 PRO A N   1 
ATOM   1665 C CA  . PRO A 1 195 ? 4.184   10.725 71.000  1.00 14.04 ? 195 PRO A CA  1 
ATOM   1666 C C   . PRO A 1 195 ? 3.251   10.753 72.202  1.00 13.23 ? 195 PRO A C   1 
ATOM   1667 O O   . PRO A 1 195 ? 2.688   11.802 72.527  1.00 14.73 ? 195 PRO A O   1 
ATOM   1668 C CB  . PRO A 1 195 ? 5.528   11.404 71.320  1.00 14.83 ? 195 PRO A CB  1 
ATOM   1669 C CG  . PRO A 1 195 ? 5.883   12.161 70.085  1.00 29.90 ? 195 PRO A CG  1 
ATOM   1670 C CD  . PRO A 1 195 ? 4.611   12.486 69.342  1.00 17.23 ? 195 PRO A CD  1 
ATOM   1671 N N   . TYR A 1 196 ? 3.159   9.605  72.895  1.00 11.56 ? 196 TYR A N   1 
ATOM   1672 C CA  . TYR A 1 196 ? 1.953   9.191  73.621  1.00 13.54 ? 196 TYR A CA  1 
ATOM   1673 C C   . TYR A 1 196 ? 1.387   10.262 74.561  1.00 12.76 ? 196 TYR A C   1 
ATOM   1674 O O   . TYR A 1 196 ? 0.215   10.610 74.456  1.00 12.71 ? 196 TYR A O   1 
ATOM   1675 C CB  . TYR A 1 196 ? 2.230   7.903  74.406  1.00 12.83 ? 196 TYR A CB  1 
ATOM   1676 C CG  . TYR A 1 196 ? 0.977   7.096  74.669  1.00 14.35 ? 196 TYR A CG  1 
ATOM   1677 C CD1 . TYR A 1 196 ? 0.067   7.470  75.661  1.00 12.87 ? 196 TYR A CD1 1 
ATOM   1678 C CD2 . TYR A 1 196 ? 0.705   5.955  73.922  1.00 13.28 ? 196 TYR A CD2 1 
ATOM   1679 C CE1 . TYR A 1 196 ? -1.101  6.713  75.891  1.00 12.79 ? 196 TYR A CE1 1 
ATOM   1680 C CE2 . TYR A 1 196 ? -0.444  5.210  74.131  1.00 12.87 ? 196 TYR A CE2 1 
ATOM   1681 C CZ  . TYR A 1 196 ? -1.340  5.591  75.129  1.00 14.73 ? 196 TYR A CZ  1 
ATOM   1682 O OH  . TYR A 1 196 ? -2.494  4.837  75.341  1.00 18.92 ? 196 TYR A OH  1 
ATOM   1683 N N   . TYR A 1 197 ? 2.177   10.750 75.528  1.00 13.44 ? 197 TYR A N   1 
ATOM   1684 C CA  . TYR A 1 197 ? 1.659   11.709 76.509  1.00 12.42 ? 197 TYR A CA  1 
ATOM   1685 C C   . TYR A 1 197 ? 2.014   13.161 76.171  1.00 16.90 ? 197 TYR A C   1 
ATOM   1686 O O   . TYR A 1 197 ? 2.048   14.018 77.066  1.00 14.05 ? 197 TYR A O   1 
ATOM   1687 C CB  . TYR A 1 197 ? 2.123   11.327 77.925  1.00 13.39 ? 197 TYR A CB  1 
ATOM   1688 C CG  . TYR A 1 197 ? 1.511   9.998  78.325  1.00 14.82 ? 197 TYR A CG  1 
ATOM   1689 C CD1 . TYR A 1 197 ? 0.188   9.915  78.728  1.00 14.09 ? 197 TYR A CD1 1 
ATOM   1690 C CD2 . TYR A 1 197 ? 2.257   8.821  78.239  1.00 17.85 ? 197 TYR A CD2 1 
ATOM   1691 C CE1 . TYR A 1 197 ? -0.395  8.682  79.049  1.00 17.37 ? 197 TYR A CE1 1 
ATOM   1692 C CE2 . TYR A 1 197 ? 1.703   7.600  78.573  1.00 16.26 ? 197 TYR A CE2 1 
ATOM   1693 C CZ  . TYR A 1 197 ? 0.394   7.532  78.971  1.00 17.87 ? 197 TYR A CZ  1 
ATOM   1694 O OH  . TYR A 1 197 ? -0.136  6.303  79.283  1.00 21.19 ? 197 TYR A OH  1 
ATOM   1695 N N   . HIS A 1 198 ? 2.240   13.468 74.872  1.00 12.89 ? 198 HIS A N   1 
ATOM   1696 C CA  . HIS A 1 198 ? 2.536   14.839 74.427  1.00 12.98 ? 198 HIS A CA  1 
ATOM   1697 C C   . HIS A 1 198 ? 3.782   15.427 75.117  1.00 13.12 ? 198 HIS A C   1 
ATOM   1698 O O   . HIS A 1 198 ? 3.717   16.550 75.631  1.00 12.93 ? 198 HIS A O   1 
ATOM   1699 C CB  . HIS A 1 198 ? 1.292   15.698 74.689  1.00 13.19 ? 198 HIS A CB  1 
ATOM   1700 C CG  . HIS A 1 198 ? 1.215   16.984 73.911  1.00 16.38 ? 198 HIS A CG  1 
ATOM   1701 N ND1 . HIS A 1 198 ? 1.637   18.189 74.429  1.00 18.52 ? 198 HIS A ND1 1 
ATOM   1702 C CD2 . HIS A 1 198 ? 0.680   17.266 72.695  1.00 15.36 ? 198 HIS A CD2 1 
ATOM   1703 C CE1 . HIS A 1 198 ? 1.432   19.148 73.539  1.00 18.91 ? 198 HIS A CE1 1 
ATOM   1704 N NE2 . HIS A 1 198 ? 0.830   18.618 72.489  1.00 16.91 ? 198 HIS A NE2 1 
ATOM   1705 N N   . PRO A 1 199 ? 4.919   14.713 75.176  1.00 12.24 ? 199 PRO A N   1 
ATOM   1706 C CA  . PRO A 1 199 ? 6.137   15.280 75.776  1.00 13.03 ? 199 PRO A CA  1 
ATOM   1707 C C   . PRO A 1 199 ? 6.874   16.197 74.800  1.00 24.20 ? 199 PRO A C   1 
ATOM   1708 O O   . PRO A 1 199 ? 6.565   16.273 73.602  1.00 21.70 ? 199 PRO A O   1 
ATOM   1709 C CB  . PRO A 1 199 ? 7.000   14.035 76.033  1.00 14.01 ? 199 PRO A CB  1 
ATOM   1710 C CG  . PRO A 1 199 ? 6.706   13.177 74.854  1.00 17.18 ? 199 PRO A CG  1 
ATOM   1711 C CD  . PRO A 1 199 ? 5.207   13.394 74.574  1.00 14.91 ? 199 PRO A CD  1 
ATOM   1712 N N   . LEU A 1 200 ? 7.930   16.833 75.323  1.00 20.46 ? 200 LEU A N   1 
ATOM   1713 C CA  . LEU A 1 200 ? 8.888   17.585 74.497  1.00 19.34 ? 200 LEU A CA  1 
ATOM   1714 C C   . LEU A 1 200 ? 10.027  16.650 74.107  1.00 17.33 ? 200 LEU A C   1 
ATOM   1715 O O   . LEU A 1 200 ? 11.038  16.531 74.804  1.00 16.30 ? 200 LEU A O   1 
ATOM   1716 C CB  . LEU A 1 200 ? 9.421   18.801 75.241  1.00 21.27 ? 200 LEU A CB  1 
ATOM   1717 C CG  . LEU A 1 200 ? 8.419   19.905 75.551  1.00 24.05 ? 200 LEU A CG  1 
ATOM   1718 C CD1 . LEU A 1 200 ? 9.043   20.862 76.550  1.00 27.13 ? 200 LEU A CD1 1 
ATOM   1719 C CD2 . LEU A 1 200 ? 8.006   20.621 74.268  1.00 24.12 ? 200 LEU A CD2 1 
ATOM   1720 N N   . ILE A 1 201 ? 9.864   15.973 72.974  1.00 15.34 ? 201 ILE A N   1 
ATOM   1721 C CA  . ILE A 1 201 ? 10.836  14.980 72.525  1.00 15.46 ? 201 ILE A CA  1 
ATOM   1722 C C   . ILE A 1 201 ? 12.255  15.551 72.440  1.00 14.81 ? 201 ILE A C   1 
ATOM   1723 O O   . ILE A 1 201 ? 13.196  14.870 72.868  1.00 16.76 ? 201 ILE A O   1 
ATOM   1724 C CB  . ILE A 1 201 ? 10.399  14.374 71.180  1.00 15.60 ? 201 ILE A CB  1 
ATOM   1725 C CG1 . ILE A 1 201 ? 9.130   13.518 71.362  1.00 16.59 ? 201 ILE A CG1 1 
ATOM   1726 C CG2 . ILE A 1 201 ? 11.549  13.574 70.555  1.00 11.49 ? 201 ILE A CG2 1 
ATOM   1727 C CD1 . ILE A 1 201 ? 9.301   12.275 72.255  1.00 17.11 ? 201 ILE A CD1 1 
ATOM   1728 N N   . PRO A 1 202 ? 12.488  16.768 71.924  1.00 14.24 ? 202 PRO A N   1 
ATOM   1729 C CA  . PRO A 1 202 ? 13.884  17.253 71.884  1.00 17.17 ? 202 PRO A CA  1 
ATOM   1730 C C   . PRO A 1 202 ? 14.569  17.302 73.247  1.00 16.43 ? 202 PRO A C   1 
ATOM   1731 O O   . PRO A 1 202 ? 15.746  16.940 73.348  1.00 17.76 ? 202 PRO A O   1 
ATOM   1732 C CB  . PRO A 1 202 ? 13.754  18.652 71.264  1.00 20.64 ? 202 PRO A CB  1 
ATOM   1733 C CG  . PRO A 1 202 ? 12.518  18.569 70.412  1.00 11.61 ? 202 PRO A CG  1 
ATOM   1734 C CD  . PRO A 1 202 ? 11.578  17.691 71.205  1.00 14.70 ? 202 PRO A CD  1 
ATOM   1735 N N   . ILE A 1 203 ? 13.862  17.716 74.302  1.00 12.27 ? 203 ILE A N   1 
ATOM   1736 C CA  . ILE A 1 203 ? 14.487  17.759 75.626  1.00 12.33 ? 203 ILE A CA  1 
ATOM   1737 C C   . ILE A 1 203 ? 14.765  16.349 76.148  1.00 14.28 ? 203 ILE A C   1 
ATOM   1738 O O   . ILE A 1 203 ? 15.833  16.093 76.720  1.00 16.00 ? 203 ILE A O   1 
ATOM   1739 C CB  . ILE A 1 203 ? 13.618  18.563 76.604  1.00 15.21 ? 203 ILE A CB  1 
ATOM   1740 C CG1 . ILE A 1 203 ? 13.561  20.033 76.177  1.00 19.26 ? 203 ILE A CG1 1 
ATOM   1741 C CG2 . ILE A 1 203 ? 14.172  18.443 78.044  1.00 15.36 ? 203 ILE A CG2 1 
ATOM   1742 C CD1 . ILE A 1 203 ? 12.654  20.901 77.064  1.00 20.47 ? 203 ILE A CD1 1 
ATOM   1743 N N   . LEU A 1 204 ? 13.829  15.415 75.955  1.00 14.64 ? 204 LEU A N   1 
ATOM   1744 C CA  . LEU A 1 204 ? 14.051  14.044 76.418  1.00 15.92 ? 204 LEU A CA  1 
ATOM   1745 C C   . LEU A 1 204 ? 15.268  13.428 75.734  1.00 18.14 ? 204 LEU A C   1 
ATOM   1746 O O   . LEU A 1 204 ? 16.048  12.705 76.367  1.00 15.62 ? 204 LEU A O   1 
ATOM   1747 C CB  . LEU A 1 204 ? 12.805  13.187 76.164  1.00 16.00 ? 204 LEU A CB  1 
ATOM   1748 C CG  . LEU A 1 204 ? 11.463  13.554 76.816  1.00 17.54 ? 204 LEU A CG  1 
ATOM   1749 C CD1 . LEU A 1 204 ? 10.510  12.376 76.691  1.00 16.38 ? 204 LEU A CD1 1 
ATOM   1750 C CD2 . LEU A 1 204 ? 11.643  13.934 78.304  1.00 16.15 ? 204 LEU A CD2 1 
ATOM   1751 N N   . LEU A 1 205 ? 15.449  13.716 74.437  1.00 18.04 ? 205 LEU A N   1 
ATOM   1752 C CA  . LEU A 1 205 ? 16.615  13.219 73.713  1.00 11.42 ? 205 LEU A CA  1 
ATOM   1753 C C   . LEU A 1 205 ? 17.891  13.901 74.182  1.00 18.70 ? 205 LEU A C   1 
ATOM   1754 O O   . LEU A 1 205 ? 18.924  13.245 74.341  1.00 18.61 ? 205 LEU A O   1 
ATOM   1755 C CB  . LEU A 1 205 ? 16.438  13.441 72.209  1.00 11.87 ? 205 LEU A CB  1 
ATOM   1756 C CG  . LEU A 1 205 ? 15.409  12.466 71.622  1.00 17.37 ? 205 LEU A CG  1 
ATOM   1757 C CD1 . LEU A 1 205 ? 15.077  12.780 70.174  1.00 12.63 ? 205 LEU A CD1 1 
ATOM   1758 C CD2 . LEU A 1 205 ? 15.984  11.053 71.725  1.00 21.09 ? 205 LEU A CD2 1 
ATOM   1759 N N   . ASN A 1 206 ? 17.854  15.218 74.352  1.00 18.05 ? 206 ASN A N   1 
ATOM   1760 C CA  . ASN A 1 206 ? 19.070  15.979 74.595  1.00 14.28 ? 206 ASN A CA  1 
ATOM   1761 C C   . ASN A 1 206 ? 18.686  17.300 75.247  1.00 15.05 ? 206 ASN A C   1 
ATOM   1762 O O   . ASN A 1 206 ? 18.367  18.279 74.542  1.00 15.91 ? 206 ASN A O   1 
ATOM   1763 C CB  . ASN A 1 206 ? 19.834  16.235 73.294  1.00 17.21 ? 206 ASN A CB  1 
ATOM   1764 C CG  . ASN A 1 206 ? 21.014  17.184 73.484  1.00 18.36 ? 206 ASN A CG  1 
ATOM   1765 O OD1 . ASN A 1 206 ? 21.541  17.327 74.592  1.00 17.53 ? 206 ASN A OD1 1 
ATOM   1766 N ND2 . ASN A 1 206 ? 21.420  17.857 72.400  1.00 19.99 ? 206 ASN A ND2 1 
ATOM   1767 N N   . PRO A 1 207 ? 18.655  17.355 76.581  1.00 18.58 ? 207 PRO A N   1 
ATOM   1768 C CA  . PRO A 1 207 ? 18.296  18.613 77.249  1.00 18.93 ? 207 PRO A CA  1 
ATOM   1769 C C   . PRO A 1 207 ? 19.198  19.774 76.851  1.00 17.59 ? 207 PRO A C   1 
ATOM   1770 O O   . PRO A 1 207 ? 18.787  20.930 76.979  1.00 20.01 ? 207 PRO A O   1 
ATOM   1771 C CB  . PRO A 1 207 ? 18.435  18.273 78.742  1.00 19.09 ? 207 PRO A CB  1 
ATOM   1772 C CG  . PRO A 1 207 ? 18.323  16.795 78.816  1.00 21.27 ? 207 PRO A CG  1 
ATOM   1773 C CD  . PRO A 1 207 ? 18.951  16.276 77.546  1.00 20.59 ? 207 PRO A CD  1 
ATOM   1774 N N   . ASN A 1 208 ? 20.416  19.511 76.364  1.00 18.57 ? 208 ASN A N   1 
ATOM   1775 C CA  . ASN A 1 208 ? 21.280  20.623 76.002  1.00 16.57 ? 208 ASN A CA  1 
ATOM   1776 C C   . ASN A 1 208 ? 20.797  21.353 74.759  1.00 18.58 ? 208 ASN A C   1 
ATOM   1777 O O   . ASN A 1 208 ? 21.321  22.434 74.463  1.00 16.96 ? 208 ASN A O   1 
ATOM   1778 C CB  . ASN A 1 208 ? 22.722  20.141 75.800  1.00 19.35 ? 208 ASN A CB  1 
ATOM   1779 C CG  . ASN A 1 208 ? 23.334  19.607 77.087  1.00 21.64 ? 208 ASN A CG  1 
ATOM   1780 O OD1 . ASN A 1 208 ? 22.949  20.018 78.184  1.00 25.12 ? 208 ASN A OD1 1 
ATOM   1781 N ND2 . ASN A 1 208 ? 24.267  18.683 76.961  1.00 25.80 ? 208 ASN A ND2 1 
ATOM   1782 N N   . CYS A 1 209 ? 19.795  20.822 74.043  1.00 16.88 ? 209 CYS A N   1 
ATOM   1783 C CA  . CYS A 1 209 ? 19.347  21.524 72.846  1.00 16.56 ? 209 CYS A CA  1 
ATOM   1784 C C   . CYS A 1 209 ? 18.697  22.857 73.177  1.00 20.29 ? 209 CYS A C   1 
ATOM   1785 O O   . CYS A 1 209 ? 18.619  23.715 72.290  1.00 18.49 ? 209 CYS A O   1 
ATOM   1786 C CB  . CYS A 1 209 ? 18.365  20.652 72.029  1.00 21.54 ? 209 CYS A CB  1 
ATOM   1787 S SG  . CYS A 1 209 ? 16.714  20.429 72.721  1.00 24.54 ? 209 CYS A SG  1 
ATOM   1788 N N   . VAL A 1 210 ? 18.242  23.061 74.427  1.00 20.70 ? 210 VAL A N   1 
ATOM   1789 C CA  . VAL A 1 210 ? 17.619  24.337 74.778  1.00 21.63 ? 210 VAL A CA  1 
ATOM   1790 C C   . VAL A 1 210 ? 18.602  25.482 74.593  1.00 20.52 ? 210 VAL A C   1 
ATOM   1791 O O   . VAL A 1 210 ? 18.194  26.632 74.374  1.00 22.02 ? 210 VAL A O   1 
ATOM   1792 C CB  . VAL A 1 210 ? 17.054  24.315 76.221  1.00 19.54 ? 210 VAL A CB  1 
ATOM   1793 C CG1 . VAL A 1 210 ? 16.070  23.164 76.418  1.00 14.64 ? 210 VAL A CG1 1 
ATOM   1794 C CG2 . VAL A 1 210 ? 18.158  24.229 77.248  1.00 18.50 ? 210 VAL A CG2 1 
ATOM   1795 N N   . TYR A 1 211 ? 19.902  25.192 74.645  1.00 16.36 ? 211 TYR A N   1 
ATOM   1796 C CA  . TYR A 1 211 ? 20.899  26.246 74.523  1.00 18.63 ? 211 TYR A CA  1 
ATOM   1797 C C   . TYR A 1 211 ? 21.042  26.769 73.103  1.00 18.23 ? 211 TYR A C   1 
ATOM   1798 O O   . TYR A 1 211 ? 21.662  27.823 72.914  1.00 21.83 ? 211 TYR A O   1 
ATOM   1799 C CB  . TYR A 1 211 ? 22.238  25.729 75.042  1.00 18.83 ? 211 TYR A CB  1 
ATOM   1800 C CG  . TYR A 1 211 ? 22.142  25.323 76.488  1.00 21.59 ? 211 TYR A CG  1 
ATOM   1801 C CD1 . TYR A 1 211 ? 21.686  26.214 77.444  1.00 25.76 ? 211 TYR A CD1 1 
ATOM   1802 C CD2 . TYR A 1 211 ? 22.485  24.047 76.882  1.00 16.91 ? 211 TYR A CD2 1 
ATOM   1803 C CE1 . TYR A 1 211 ? 21.592  25.833 78.767  1.00 24.75 ? 211 TYR A CE1 1 
ATOM   1804 C CE2 . TYR A 1 211 ? 22.408  23.659 78.186  1.00 23.40 ? 211 TYR A CE2 1 
ATOM   1805 C CZ  . TYR A 1 211 ? 21.951  24.547 79.123  1.00 34.38 ? 211 TYR A CZ  1 
ATOM   1806 O OH  . TYR A 1 211 ? 21.882  24.142 80.440  1.00 49.34 ? 211 TYR A OH  1 
ATOM   1807 N N   . GLU A 1 212 ? 20.473  26.087 72.111  1.00 20.79 ? 212 GLU A N   1 
ATOM   1808 C CA  . GLU A 1 212 ? 20.536  26.594 70.743  1.00 26.21 ? 212 GLU A CA  1 
ATOM   1809 C C   . GLU A 1 212 ? 19.724  27.877 70.563  1.00 27.63 ? 212 GLU A C   1 
ATOM   1810 O O   . GLU A 1 212 ? 20.011  28.648 69.641  1.00 32.11 ? 212 GLU A O   1 
ATOM   1811 C CB  . GLU A 1 212 ? 20.063  25.504 69.762  1.00 24.93 ? 212 GLU A CB  1 
ATOM   1812 C CG  . GLU A 1 212 ? 20.928  24.259 69.826  1.00 27.97 ? 212 GLU A CG  1 
ATOM   1813 C CD  . GLU A 1 212 ? 20.381  23.107 69.017  1.00 36.01 ? 212 GLU A CD  1 
ATOM   1814 O OE1 . GLU A 1 212 ? 20.793  21.951 69.277  1.00 39.11 ? 212 GLU A OE1 1 
ATOM   1815 O OE2 . GLU A 1 212 ? 19.551  23.353 68.118  1.00 31.25 ? 212 GLU A OE2 1 
ATOM   1816 N N   . THR A 1 213 ? 18.739  28.135 71.430  1.00 20.80 ? 213 THR A N   1 
ATOM   1817 C CA  . THR A 1 213 ? 17.928  29.348 71.362  1.00 19.33 ? 213 THR A CA  1 
ATOM   1818 C C   . THR A 1 213 ? 18.008  30.222 72.604  1.00 25.35 ? 213 THR A C   1 
ATOM   1819 O O   . THR A 1 213 ? 17.852  31.438 72.474  1.00 30.55 ? 213 THR A O   1 
ATOM   1820 C CB  . THR A 1 213 ? 16.445  29.022 71.116  1.00 22.45 ? 213 THR A CB  1 
ATOM   1821 O OG1 . THR A 1 213 ? 15.986  28.087 72.104  1.00 23.31 ? 213 THR A OG1 1 
ATOM   1822 C CG2 . THR A 1 213 ? 16.251  28.430 69.724  1.00 24.05 ? 213 THR A CG2 1 
ATOM   1823 N N   . THR A 1 214 ? 18.225  29.656 73.800  1.00 23.17 ? 214 THR A N   1 
ATOM   1824 C CA  . THR A 1 214 ? 18.355  30.449 75.032  1.00 27.60 ? 214 THR A CA  1 
ATOM   1825 C C   . THR A 1 214 ? 19.645  30.083 75.765  1.00 26.92 ? 214 THR A C   1 
ATOM   1826 O O   . THR A 1 214 ? 19.624  29.342 76.763  1.00 22.08 ? 214 THR A O   1 
ATOM   1827 C CB  . THR A 1 214 ? 17.135  30.262 75.945  1.00 22.67 ? 214 THR A CB  1 
ATOM   1828 O OG1 . THR A 1 214 ? 16.993  28.882 76.309  1.00 22.30 ? 214 THR A OG1 1 
ATOM   1829 C CG2 . THR A 1 214 ? 15.869  30.704 75.237  1.00 21.72 ? 214 THR A CG2 1 
ATOM   1830 N N   . PRO A 1 215 ? 20.790  30.609 75.315  1.00 25.66 ? 215 PRO A N   1 
ATOM   1831 C CA  . PRO A 1 215 ? 22.068  30.187 75.919  1.00 25.51 ? 215 PRO A CA  1 
ATOM   1832 C C   . PRO A 1 215 ? 22.189  30.495 77.405  1.00 27.40 ? 215 PRO A C   1 
ATOM   1833 O O   . PRO A 1 215 ? 22.985  29.839 78.091  1.00 28.31 ? 215 PRO A O   1 
ATOM   1834 C CB  . PRO A 1 215 ? 23.122  30.952 75.097  1.00 34.85 ? 215 PRO A CB  1 
ATOM   1835 C CG  . PRO A 1 215 ? 22.388  32.064 74.429  1.00 25.11 ? 215 PRO A CG  1 
ATOM   1836 C CD  . PRO A 1 215 ? 20.982  31.559 74.205  1.00 22.90 ? 215 PRO A CD  1 
ATOM   1837 N N   . ASN A 1 216 ? 21.417  31.441 77.931  1.00 24.37 ? 216 ASN A N   1 
ATOM   1838 C CA  . ASN A 1 216 ? 21.568  31.870 79.318  1.00 32.45 ? 216 ASN A CA  1 
ATOM   1839 C C   . ASN A 1 216 ? 20.729  31.065 80.299  1.00 31.74 ? 216 ASN A C   1 
ATOM   1840 O O   . ASN A 1 216 ? 20.849  31.280 81.510  1.00 31.46 ? 216 ASN A O   1 
ATOM   1841 C CB  . ASN A 1 216 ? 21.211  33.353 79.448  1.00 38.78 ? 216 ASN A CB  1 
ATOM   1842 C CG  . ASN A 1 216 ? 22.157  34.233 78.674  1.00 44.56 ? 216 ASN A CG  1 
ATOM   1843 O OD1 . ASN A 1 216 ? 23.325  33.881 78.488  1.00 39.83 ? 216 ASN A OD1 1 
ATOM   1844 N ND2 . ASN A 1 216 ? 21.664  35.373 78.204  1.00 51.49 ? 216 ASN A ND2 1 
ATOM   1845 N N   . VAL A 1 217 ? 19.899  30.147 79.812  1.00 31.81 ? 217 VAL A N   1 
ATOM   1846 C CA  . VAL A 1 217 ? 18.929  29.464 80.659  1.00 26.28 ? 217 VAL A CA  1 
ATOM   1847 C C   . VAL A 1 217 ? 19.637  28.527 81.636  1.00 28.98 ? 217 VAL A C   1 
ATOM   1848 O O   . VAL A 1 217 ? 20.675  27.927 81.320  1.00 24.80 ? 217 VAL A O   1 
ATOM   1849 C CB  . VAL A 1 217 ? 17.916  28.719 79.766  1.00 21.50 ? 217 VAL A CB  1 
ATOM   1850 C CG1 . VAL A 1 217 ? 18.509  27.435 79.202  1.00 27.50 ? 217 VAL A CG1 1 
ATOM   1851 C CG2 . VAL A 1 217 ? 16.622  28.432 80.516  1.00 26.99 ? 217 VAL A CG2 1 
ATOM   1852 N N   . LYS A 1 218 ? 19.100  28.427 82.851  1.00 19.19 ? 218 LYS A N   1 
ATOM   1853 C CA  . LYS A 1 218 ? 19.545  27.439 83.828  1.00 18.68 ? 218 LYS A CA  1 
ATOM   1854 C C   . LYS A 1 218 ? 18.646  26.206 83.747  1.00 20.47 ? 218 LYS A C   1 
ATOM   1855 O O   . LYS A 1 218 ? 17.416  26.336 83.727  1.00 22.99 ? 218 LYS A O   1 
ATOM   1856 C CB  . LYS A 1 218 ? 19.506  28.020 85.242  1.00 22.25 ? 218 LYS A CB  1 
ATOM   1857 C CG  . LYS A 1 218 ? 20.535  29.103 85.513  1.00 27.61 ? 218 LYS A CG  1 
ATOM   1858 C CD  . LYS A 1 218 ? 20.523  29.524 86.983  1.00 35.75 ? 218 LYS A CD  1 
ATOM   1859 C CE  . LYS A 1 218 ? 20.763  28.331 87.908  1.00 42.18 ? 218 LYS A CE  1 
ATOM   1860 N NZ  . LYS A 1 218 ? 21.107  28.744 89.313  1.00 51.98 ? 218 LYS A NZ  1 
ATOM   1861 N N   . ILE A 1 219 ? 19.246  25.018 83.701  1.00 20.88 ? 219 ILE A N   1 
ATOM   1862 C CA  . ILE A 1 219 ? 18.475  23.773 83.734  1.00 20.61 ? 219 ILE A CA  1 
ATOM   1863 C C   . ILE A 1 219 ? 19.049  22.871 84.816  1.00 22.85 ? 219 ILE A C   1 
ATOM   1864 O O   . ILE A 1 219 ? 20.215  23.014 85.217  1.00 25.12 ? 219 ILE A O   1 
ATOM   1865 C CB  . ILE A 1 219 ? 18.468  23.045 82.367  1.00 19.94 ? 219 ILE A CB  1 
ATOM   1866 C CG1 . ILE A 1 219 ? 19.857  22.493 82.012  1.00 22.34 ? 219 ILE A CG1 1 
ATOM   1867 C CG2 . ILE A 1 219 ? 17.837  23.923 81.259  1.00 16.63 ? 219 ILE A CG2 1 
ATOM   1868 C CD1 . ILE A 1 219 ? 19.830  21.584 80.763  1.00 29.29 ? 219 ILE A CD1 1 
ATOM   1869 N N   . PRO A 1 220 ? 18.241  21.948 85.334  1.00 22.43 ? 220 PRO A N   1 
ATOM   1870 C CA  . PRO A 1 220 ? 18.740  21.033 86.363  1.00 21.16 ? 220 PRO A CA  1 
ATOM   1871 C C   . PRO A 1 220 ? 19.753  20.050 85.792  1.00 19.13 ? 220 PRO A C   1 
ATOM   1872 O O   . PRO A 1 220 ? 20.002  19.974 84.589  1.00 20.88 ? 220 PRO A O   1 
ATOM   1873 C CB  . PRO A 1 220 ? 17.481  20.326 86.875  1.00 23.85 ? 220 PRO A CB  1 
ATOM   1874 C CG  . PRO A 1 220 ? 16.433  20.580 85.871  1.00 25.98 ? 220 PRO A CG  1 
ATOM   1875 C CD  . PRO A 1 220 ? 16.774  21.870 85.185  1.00 25.09 ? 220 PRO A CD  1 
ATOM   1876 N N   . ASP A 1 221 ? 20.382  19.329 86.713  1.00 21.24 ? 221 ASP A N   1 
ATOM   1877 C CA  . ASP A 1 221 ? 21.352  18.284 86.403  1.00 18.28 ? 221 ASP A CA  1 
ATOM   1878 C C   . ASP A 1 221 ? 20.591  17.055 85.910  1.00 19.42 ? 221 ASP A C   1 
ATOM   1879 O O   . ASP A 1 221 ? 19.952  16.352 86.695  1.00 21.95 ? 221 ASP A O   1 
ATOM   1880 C CB  . ASP A 1 221 ? 22.165  17.970 87.655  1.00 18.75 ? 221 ASP A CB  1 
ATOM   1881 C CG  . ASP A 1 221 ? 23.205  16.916 87.420  1.00 24.66 ? 221 ASP A CG  1 
ATOM   1882 O OD1 . ASP A 1 221 ? 23.764  16.868 86.310  1.00 22.98 ? 221 ASP A OD1 1 
ATOM   1883 O OD2 . ASP A 1 221 ? 23.445  16.124 88.350  1.00 27.66 ? 221 ASP A OD2 1 
ATOM   1884 N N   . PHE A 1 222 ? 20.632  16.793 84.604  1.00 15.69 ? 222 PHE A N   1 
ATOM   1885 C CA  . PHE A 1 222 ? 19.931  15.641 84.030  1.00 16.97 ? 222 PHE A CA  1 
ATOM   1886 C C   . PHE A 1 222 ? 20.790  14.386 84.204  1.00 18.12 ? 222 PHE A C   1 
ATOM   1887 O O   . PHE A 1 222 ? 21.397  13.869 83.267  1.00 19.93 ? 222 PHE A O   1 
ATOM   1888 C CB  . PHE A 1 222 ? 19.597  15.899 82.563  1.00 21.18 ? 222 PHE A CB  1 
ATOM   1889 C CG  . PHE A 1 222 ? 18.321  16.662 82.367  1.00 19.45 ? 222 PHE A CG  1 
ATOM   1890 C CD1 . PHE A 1 222 ? 18.303  18.040 82.486  1.00 22.16 ? 222 PHE A CD1 1 
ATOM   1891 C CD2 . PHE A 1 222 ? 17.145  15.994 82.084  1.00 16.94 ? 222 PHE A CD2 1 
ATOM   1892 C CE1 . PHE A 1 222 ? 17.135  18.740 82.312  1.00 18.82 ? 222 PHE A CE1 1 
ATOM   1893 C CE2 . PHE A 1 222 ? 15.964  16.683 81.897  1.00 15.57 ? 222 PHE A CE2 1 
ATOM   1894 C CZ  . PHE A 1 222 ? 15.954  18.065 82.012  1.00 19.98 ? 222 PHE A CZ  1 
ATOM   1895 N N   . ALA A 1 223 ? 20.827  13.896 85.447  1.00 19.28 ? 223 ALA A N   1 
ATOM   1896 C CA  . ALA A 1 223 ? 21.636  12.752 85.857  1.00 22.80 ? 223 ALA A CA  1 
ATOM   1897 C C   . ALA A 1 223 ? 21.114  11.404 85.340  1.00 25.02 ? 223 ALA A C   1 
ATOM   1898 O O   . ALA A 1 223 ? 21.721  10.379 85.646  1.00 29.91 ? 223 ALA A O   1 
ATOM   1899 C CB  . ALA A 1 223 ? 21.731  12.716 87.391  1.00 21.59 ? 223 ALA A CB  1 
ATOM   1900 N N   . VAL A 1 224 ? 20.026  11.369 84.574  1.00 19.04 ? 224 VAL A N   1 
ATOM   1901 C CA  . VAL A 1 224 ? 19.476  10.136 84.019  1.00 23.18 ? 224 VAL A CA  1 
ATOM   1902 C C   . VAL A 1 224 ? 19.114  10.392 82.568  1.00 18.49 ? 224 VAL A C   1 
ATOM   1903 O O   . VAL A 1 224 ? 18.764  11.512 82.196  1.00 25.39 ? 224 VAL A O   1 
ATOM   1904 C CB  . VAL A 1 224 ? 18.217  9.651  84.766  1.00 21.84 ? 224 VAL A CB  1 
ATOM   1905 C CG1 . VAL A 1 224 ? 18.535  9.322  86.176  1.00 38.35 ? 224 VAL A CG1 1 
ATOM   1906 C CG2 . VAL A 1 224 ? 17.115  10.723 84.668  1.00 23.63 ? 224 VAL A CG2 1 
ATOM   1907 N N   . SER A 1 225 ? 19.167  9.343  81.754  1.00 24.26 ? 225 SER A N   1 
ATOM   1908 C CA  . SER A 1 225 ? 18.859  9.464  80.332  1.00 20.51 ? 225 SER A CA  1 
ATOM   1909 C C   . SER A 1 225 ? 17.365  9.284  80.112  1.00 14.84 ? 225 SER A C   1 
ATOM   1910 O O   . SER A 1 225 ? 16.763  8.359  80.664  1.00 21.03 ? 225 SER A O   1 
ATOM   1911 C CB  . SER A 1 225 ? 19.625  8.420  79.518  1.00 21.40 ? 225 SER A CB  1 
ATOM   1912 O OG  . SER A 1 225 ? 19.212  8.460  78.165  1.00 23.02 ? 225 SER A OG  1 
ATOM   1913 N N   . PHE A 1 226 ? 16.768  10.173 79.323  1.00 15.79 ? 226 PHE A N   1 
ATOM   1914 C CA  . PHE A 1 226 ? 15.376  10.025 78.915  1.00 13.82 ? 226 PHE A CA  1 
ATOM   1915 C C   . PHE A 1 226 ? 15.254  9.580  77.457  1.00 14.38 ? 226 PHE A C   1 
ATOM   1916 O O   . PHE A 1 226 ? 14.137  9.582  76.905  1.00 17.18 ? 226 PHE A O   1 
ATOM   1917 C CB  . PHE A 1 226 ? 14.609  11.334 79.116  1.00 16.96 ? 226 PHE A CB  1 
ATOM   1918 C CG  . PHE A 1 226 ? 14.329  11.676 80.562  1.00 18.94 ? 226 PHE A CG  1 
ATOM   1919 C CD1 . PHE A 1 226 ? 13.264  11.107 81.228  1.00 21.65 ? 226 PHE A CD1 1 
ATOM   1920 C CD2 . PHE A 1 226 ? 15.121  12.597 81.227  1.00 20.37 ? 226 PHE A CD2 1 
ATOM   1921 C CE1 . PHE A 1 226 ? 13.008  11.424 82.556  1.00 21.75 ? 226 PHE A CE1 1 
ATOM   1922 C CE2 . PHE A 1 226 ? 14.866  12.921 82.552  1.00 17.68 ? 226 PHE A CE2 1 
ATOM   1923 C CZ  . PHE A 1 226 ? 13.819  12.330 83.210  1.00 17.57 ? 226 PHE A CZ  1 
ATOM   1924 N N   . ARG A 1 227 ? 16.367  9.159  76.832  1.00 14.68 ? 227 ARG A N   1 
ATOM   1925 C CA  . ARG A 1 227 ? 16.354  8.854  75.402  1.00 14.78 ? 227 ARG A CA  1 
ATOM   1926 C C   . ARG A 1 227 ? 15.470  7.655  75.100  1.00 19.45 ? 227 ARG A C   1 
ATOM   1927 O O   . ARG A 1 227 ? 14.665  7.698  74.161  1.00 19.22 ? 227 ARG A O   1 
ATOM   1928 C CB  . ARG A 1 227 ? 17.780  8.616  74.891  1.00 23.84 ? 227 ARG A CB  1 
ATOM   1929 C CG  . ARG A 1 227 ? 18.676  9.847  74.947  1.00 21.59 ? 227 ARG A CG  1 
ATOM   1930 C CD  . ARG A 1 227 ? 20.082  9.554  74.402  1.00 29.41 ? 227 ARG A CD  1 
ATOM   1931 N NE  . ARG A 1 227 ? 20.056  9.143  73.001  1.00 28.68 ? 227 ARG A NE  1 
ATOM   1932 C CZ  . ARG A 1 227 ? 19.957  9.977  71.973  1.00 31.32 ? 227 ARG A CZ  1 
ATOM   1933 N NH1 . ARG A 1 227 ? 19.868  11.286 72.174  1.00 31.81 ? 227 ARG A NH1 1 
ATOM   1934 N NH2 . ARG A 1 227 ? 19.944  9.499  70.737  1.00 32.82 ? 227 ARG A NH2 1 
ATOM   1935 N N   . GLU A 1 228 ? 15.556  6.601  75.914  1.00 16.31 ? 228 GLU A N   1 
ATOM   1936 C CA  . GLU A 1 228 ? 14.689  5.452  75.676  1.00 19.79 ? 228 GLU A CA  1 
ATOM   1937 C C   . GLU A 1 228 ? 13.224  5.786  75.941  1.00 21.59 ? 228 GLU A C   1 
ATOM   1938 O O   . GLU A 1 228 ? 12.338  5.262  75.257  1.00 18.27 ? 228 GLU A O   1 
ATOM   1939 C CB  . GLU A 1 228 ? 15.150  4.260  76.524  1.00 25.52 ? 228 GLU A CB  1 
ATOM   1940 C CG  . GLU A 1 228 ? 14.165  3.096  76.564  1.00 42.61 ? 228 GLU A CG  1 
ATOM   1941 C CD  . GLU A 1 228 ? 14.240  2.170  75.351  1.00 58.06 ? 228 GLU A CD  1 
ATOM   1942 O OE1 . GLU A 1 228 ? 14.597  2.631  74.242  1.00 60.60 ? 228 GLU A OE1 1 
ATOM   1943 O OE2 . GLU A 1 228 ? 13.935  0.966  75.516  1.00 65.20 ? 228 GLU A OE2 1 
ATOM   1944 N N   . ASP A 1 229 ? 12.933  6.672  76.897  1.00 16.94 ? 229 ASP A N   1 
ATOM   1945 C CA  . ASP A 1 229 ? 11.536  7.049  77.090  1.00 15.91 ? 229 ASP A CA  1 
ATOM   1946 C C   . ASP A 1 229 ? 10.995  7.802  75.877  1.00 17.24 ? 229 ASP A C   1 
ATOM   1947 O O   . ASP A 1 229 ? 9.834   7.619  75.490  1.00 17.83 ? 229 ASP A O   1 
ATOM   1948 C CB  . ASP A 1 229 ? 11.369  7.888  78.350  1.00 17.99 ? 229 ASP A CB  1 
ATOM   1949 C CG  . ASP A 1 229 ? 11.268  7.036  79.587  1.00 23.16 ? 229 ASP A CG  1 
ATOM   1950 O OD1 . ASP A 1 229 ? 11.342  5.789  79.453  1.00 21.99 ? 229 ASP A OD1 1 
ATOM   1951 O OD2 . ASP A 1 229 ? 11.094  7.603  80.692  1.00 24.31 ? 229 ASP A OD2 1 
ATOM   1952 N N   . ALA A 1 230 ? 11.817  8.656  75.268  1.00 15.50 ? 230 ALA A N   1 
ATOM   1953 C CA  . ALA A 1 230 ? 11.381  9.355  74.067  1.00 11.97 ? 230 ALA A CA  1 
ATOM   1954 C C   . ALA A 1 230 ? 11.001  8.362  72.983  1.00 14.29 ? 230 ALA A C   1 
ATOM   1955 O O   . ALA A 1 230 ? 9.982   8.530  72.308  1.00 13.09 ? 230 ALA A O   1 
ATOM   1956 C CB  . ALA A 1 230 ? 12.480  10.294 73.566  1.00 15.59 ? 230 ALA A CB  1 
ATOM   1957 N N   . SER A 1 231 ? 11.812  7.312  72.807  1.00 15.17 ? 231 SER A N   1 
ATOM   1958 C CA  . SER A 1 231 ? 11.477  6.280  71.828  1.00 15.58 ? 231 SER A CA  1 
ATOM   1959 C C   . SER A 1 231 ? 10.159  5.605  72.181  1.00 17.13 ? 231 SER A C   1 
ATOM   1960 O O   . SER A 1 231 ? 9.321   5.360  71.306  1.00 16.84 ? 231 SER A O   1 
ATOM   1961 C CB  . SER A 1 231 ? 12.591  5.235  71.766  1.00 19.80 ? 231 SER A CB  1 
ATOM   1962 O OG  . SER A 1 231 ? 13.621  5.669  70.918  1.00 33.97 ? 231 SER A OG  1 
ATOM   1963 N N   . LYS A 1 232 ? 9.969   5.299  73.467  1.00 15.69 ? 232 LYS A N   1 
ATOM   1964 C CA  . LYS A 1 232 ? 8.747   4.654  73.939  1.00 15.18 ? 232 LYS A CA  1 
ATOM   1965 C C   . LYS A 1 232 ? 7.518   5.519  73.708  1.00 17.46 ? 232 LYS A C   1 
ATOM   1966 O O   . LYS A 1 232 ? 6.440   4.999  73.386  1.00 16.64 ? 232 LYS A O   1 
ATOM   1967 C CB  . LYS A 1 232 ? 8.859   4.326  75.430  1.00 19.05 ? 232 LYS A CB  1 
ATOM   1968 C CG  . LYS A 1 232 ? 9.706   3.109  75.755  1.00 29.16 ? 232 LYS A CG  1 
ATOM   1969 C CD  . LYS A 1 232 ? 9.416   2.603  77.167  1.00 38.88 ? 232 LYS A CD  1 
ATOM   1970 C CE  . LYS A 1 232 ? 10.673  2.000  77.803  1.00 55.22 ? 232 LYS A CE  1 
ATOM   1971 N NZ  . LYS A 1 232 ? 11.144  2.776  79.000  1.00 62.87 ? 232 LYS A NZ  1 
ATOM   1972 N N   . HIS A 1 233 ? 7.625   6.830  73.933  1.00 13.86 ? 233 HIS A N   1 
ATOM   1973 C CA  . HIS A 1 233 ? 6.484   7.684  73.617  1.00 16.56 ? 233 HIS A CA  1 
ATOM   1974 C C   . HIS A 1 233 ? 6.074   7.499  72.167  1.00 21.33 ? 233 HIS A C   1 
ATOM   1975 O O   . HIS A 1 233 ? 4.882   7.372  71.862  1.00 15.93 ? 233 HIS A O   1 
ATOM   1976 C CB  . HIS A 1 233 ? 6.794   9.157  73.870  1.00 14.09 ? 233 HIS A CB  1 
ATOM   1977 C CG  . HIS A 1 233 ? 6.703   9.570  75.302  1.00 16.92 ? 233 HIS A CG  1 
ATOM   1978 N ND1 . HIS A 1 233 ? 5.514   9.927  75.915  1.00 12.65 ? 233 HIS A ND1 1 
ATOM   1979 C CD2 . HIS A 1 233 ? 7.668   9.703  76.242  1.00 16.45 ? 233 HIS A CD2 1 
ATOM   1980 C CE1 . HIS A 1 233 ? 5.757   10.256 77.172  1.00 15.76 ? 233 HIS A CE1 1 
ATOM   1981 N NE2 . HIS A 1 233 ? 7.053   10.135 77.393  1.00 13.92 ? 233 HIS A NE2 1 
ATOM   1982 N N   . VAL A 1 234 ? 7.053   7.454  71.255  1.00 14.60 ? 234 VAL A N   1 
ATOM   1983 C CA  . VAL A 1 234 ? 6.702   7.319  69.842  1.00 15.54 ? 234 VAL A CA  1 
ATOM   1984 C C   . VAL A 1 234 ? 6.167   5.926  69.540  1.00 15.02 ? 234 VAL A C   1 
ATOM   1985 O O   . VAL A 1 234 ? 5.149   5.780  68.849  1.00 15.50 ? 234 VAL A O   1 
ATOM   1986 C CB  . VAL A 1 234 ? 7.899   7.691  68.953  1.00 11.87 ? 234 VAL A CB  1 
ATOM   1987 C CG1 . VAL A 1 234 ? 7.539   7.520  67.465  1.00 13.83 ? 234 VAL A CG1 1 
ATOM   1988 C CG2 . VAL A 1 234 ? 8.297   9.115  69.239  1.00 16.08 ? 234 VAL A CG2 1 
ATOM   1989 N N   . GLU A 1 235 ? 6.811   4.886  70.074  1.00 12.32 ? 235 GLU A N   1 
ATOM   1990 C CA  . GLU A 1 235 ? 6.401   3.522  69.749  1.00 15.21 ? 235 GLU A CA  1 
ATOM   1991 C C   . GLU A 1 235 ? 5.018   3.184  70.319  1.00 19.01 ? 235 GLU A C   1 
ATOM   1992 O O   . GLU A 1 235 ? 4.179   2.590  69.628  1.00 19.16 ? 235 GLU A O   1 
ATOM   1993 C CB  . GLU A 1 235 ? 7.450   2.530  70.247  1.00 17.45 ? 235 GLU A CB  1 
ATOM   1994 C CG  . GLU A 1 235 ? 7.392   1.196  69.505  1.00 42.84 ? 235 GLU A CG  1 
ATOM   1995 C CD  . GLU A 1 235 ? 8.281   1.176  68.268  1.00 49.12 ? 235 GLU A CD  1 
ATOM   1996 O OE1 . GLU A 1 235 ? 7.807   1.594  67.197  1.00 43.56 ? 235 GLU A OE1 1 
ATOM   1997 O OE2 . GLU A 1 235 ? 9.453   0.735  68.362  1.00 56.71 ? 235 GLU A OE2 1 
ATOM   1998 N N   . LEU A 1 236 ? 4.750   3.566  71.566  1.00 13.88 ? 236 LEU A N   1 
ATOM   1999 C CA  . LEU A 1 236 ? 3.424   3.341  72.127  1.00 16.46 ? 236 LEU A CA  1 
ATOM   2000 C C   . LEU A 1 236 ? 2.346   4.122  71.374  1.00 15.34 ? 236 LEU A C   1 
ATOM   2001 O O   . LEU A 1 236 ? 1.212   3.638  71.232  1.00 15.08 ? 236 LEU A O   1 
ATOM   2002 C CB  . LEU A 1 236 ? 3.433   3.716  73.615  1.00 15.53 ? 236 LEU A CB  1 
ATOM   2003 C CG  . LEU A 1 236 ? 4.281   2.759  74.454  1.00 21.44 ? 236 LEU A CG  1 
ATOM   2004 C CD1 . LEU A 1 236 ? 4.364   3.258  75.906  1.00 24.12 ? 236 LEU A CD1 1 
ATOM   2005 C CD2 . LEU A 1 236 ? 3.712   1.331  74.379  1.00 24.19 ? 236 LEU A CD2 1 
ATOM   2006 N N   . ALA A 1 237 ? 2.677   5.319  70.881  1.00 15.29 ? 237 ALA A N   1 
ATOM   2007 C CA  . ALA A 1 237 ? 1.725   6.076  70.076  1.00 15.99 ? 237 ALA A CA  1 
ATOM   2008 C C   . ALA A 1 237 ? 1.390   5.340  68.782  1.00 17.79 ? 237 ALA A C   1 
ATOM   2009 O O   . ALA A 1 237 ? 0.225   5.312  68.357  1.00 13.58 ? 237 ALA A O   1 
ATOM   2010 C CB  . ALA A 1 237 ? 2.283   7.468  69.761  1.00 12.90 ? 237 ALA A CB  1 
ATOM   2011 N N   . LYS A 1 238 ? 2.408   4.785  68.115  1.00 13.89 ? 238 LYS A N   1 
ATOM   2012 C CA  . LYS A 1 238 ? 2.152   3.980  66.920  1.00 13.37 ? 238 LYS A CA  1 
ATOM   2013 C C   . LYS A 1 238 ? 1.204   2.827  67.233  1.00 14.18 ? 238 LYS A C   1 
ATOM   2014 O O   . LYS A 1 238 ? 0.291   2.514  66.443  1.00 15.52 ? 238 LYS A O   1 
ATOM   2015 C CB  . LYS A 1 238 ? 3.467   3.427  66.358  1.00 19.25 ? 238 LYS A CB  1 
ATOM   2016 C CG  . LYS A 1 238 ? 4.407   4.483  65.786  1.00 18.01 ? 238 LYS A CG  1 
ATOM   2017 C CD  . LYS A 1 238 ? 5.780   3.894  65.457  1.00 21.93 ? 238 LYS A CD  1 
ATOM   2018 C CE  . LYS A 1 238 ? 5.684   2.739  64.461  1.00 24.30 ? 238 LYS A CE  1 
ATOM   2019 N NZ  . LYS A 1 238 ? 7.044   2.379  63.959  1.00 28.63 ? 238 LYS A NZ  1 
ATOM   2020 N N   . GLU A 1 239 ? 1.420   2.161  68.370  1.00 14.84 ? 239 GLU A N   1 
ATOM   2021 C CA  . GLU A 1 239 ? 0.585   1.016  68.729  1.00 16.07 ? 239 GLU A CA  1 
ATOM   2022 C C   . GLU A 1 239 ? -0.867  1.428  68.977  1.00 17.30 ? 239 GLU A C   1 
ATOM   2023 O O   . GLU A 1 239 ? -1.804  0.743  68.548  1.00 15.02 ? 239 GLU A O   1 
ATOM   2024 C CB  . GLU A 1 239 ? 1.164   0.331  69.969  1.00 17.83 ? 239 GLU A CB  1 
ATOM   2025 C CG  . GLU A 1 239 ? 2.438   -0.445 69.685  1.00 24.08 ? 239 GLU A CG  1 
ATOM   2026 C CD  . GLU A 1 239 ? 2.994   -1.083 70.943  1.00 42.13 ? 239 GLU A CD  1 
ATOM   2027 O OE1 . GLU A 1 239 ? 4.201   -1.408 70.961  1.00 51.03 ? 239 GLU A OE1 1 
ATOM   2028 O OE2 . GLU A 1 239 ? 2.220   -1.239 71.914  1.00 38.75 ? 239 GLU A OE2 1 
ATOM   2029 N N   . LYS A 1 240 ? -1.078  2.516  69.726  1.00 13.82 ? 240 LYS A N   1 
ATOM   2030 C CA  . LYS A 1 240 ? -2.441  2.971  69.979  1.00 18.38 ? 240 LYS A CA  1 
ATOM   2031 C C   . LYS A 1 240 ? -3.111  3.423  68.689  1.00 13.02 ? 240 LYS A C   1 
ATOM   2032 O O   . LYS A 1 240 ? -4.288  3.130  68.457  1.00 15.00 ? 240 LYS A O   1 
ATOM   2033 C CB  . LYS A 1 240 ? -2.429  4.111  70.998  1.00 18.26 ? 240 LYS A CB  1 
ATOM   2034 C CG  . LYS A 1 240 ? -3.808  4.548  71.416  1.00 17.48 ? 240 LYS A CG  1 
ATOM   2035 C CD  . LYS A 1 240 ? -4.483  3.456  72.225  1.00 17.14 ? 240 LYS A CD  1 
ATOM   2036 C CE  . LYS A 1 240 ? -5.861  3.863  72.672  1.00 23.65 ? 240 LYS A CE  1 
ATOM   2037 N NZ  . LYS A 1 240 ? -6.447  2.775  73.530  1.00 22.57 ? 240 LYS A NZ  1 
ATOM   2038 N N   . TYR A 1 241 ? -2.380  4.157  67.851  1.00 15.30 ? 241 TYR A N   1 
ATOM   2039 C CA  . TYR A 1 241 ? -2.929  4.593  66.570  1.00 15.46 ? 241 TYR A CA  1 
ATOM   2040 C C   . TYR A 1 241 ? -3.324  3.389  65.723  1.00 16.81 ? 241 TYR A C   1 
ATOM   2041 O O   . TYR A 1 241 ? -4.381  3.385  65.078  1.00 16.98 ? 241 TYR A O   1 
ATOM   2042 C CB  . TYR A 1 241 ? -1.912  5.465  65.835  1.00 12.86 ? 241 TYR A CB  1 
ATOM   2043 C CG  . TYR A 1 241 ? -2.431  6.047  64.539  1.00 12.56 ? 241 TYR A CG  1 
ATOM   2044 C CD1 . TYR A 1 241 ? -2.374  5.312  63.363  1.00 12.33 ? 241 TYR A CD1 1 
ATOM   2045 C CD2 . TYR A 1 241 ? -2.954  7.335  64.487  1.00 18.81 ? 241 TYR A CD2 1 
ATOM   2046 C CE1 . TYR A 1 241 ? -2.850  5.825  62.171  1.00 14.72 ? 241 TYR A CE1 1 
ATOM   2047 C CE2 . TYR A 1 241 ? -3.429  7.866  63.279  1.00 15.33 ? 241 TYR A CE2 1 
ATOM   2048 C CZ  . TYR A 1 241 ? -3.363  7.090  62.129  1.00 17.50 ? 241 TYR A CZ  1 
ATOM   2049 O OH  . TYR A 1 241 ? -3.811  7.566  60.923  1.00 16.01 ? 241 TYR A OH  1 
ATOM   2050 N N   . PHE A 1 242 ? -2.483  2.354  65.716  1.00 14.61 ? 242 PHE A N   1 
ATOM   2051 C CA  . PHE A 1 242 ? -2.811  1.139  64.976  1.00 13.62 ? 242 PHE A CA  1 
ATOM   2052 C C   . PHE A 1 242 ? -4.111  0.514  65.471  1.00 15.71 ? 242 PHE A C   1 
ATOM   2053 O O   . PHE A 1 242 ? -4.932  0.048  64.667  1.00 17.52 ? 242 PHE A O   1 
ATOM   2054 C CB  . PHE A 1 242 ? -1.661  0.130  65.085  1.00 14.70 ? 242 PHE A CB  1 
ATOM   2055 C CG  . PHE A 1 242 ? -1.906  -1.139 64.332  1.00 17.47 ? 242 PHE A CG  1 
ATOM   2056 C CD1 . PHE A 1 242 ? -1.502  -1.253 63.017  1.00 21.59 ? 242 PHE A CD1 1 
ATOM   2057 C CD2 . PHE A 1 242 ? -2.514  -2.233 64.942  1.00 16.27 ? 242 PHE A CD2 1 
ATOM   2058 C CE1 . PHE A 1 242 ? -1.722  -2.441 62.298  1.00 20.00 ? 242 PHE A CE1 1 
ATOM   2059 C CE2 . PHE A 1 242 ? -2.717  -3.407 64.249  1.00 16.51 ? 242 PHE A CE2 1 
ATOM   2060 C CZ  . PHE A 1 242 ? -2.328  -3.507 62.914  1.00 19.83 ? 242 PHE A CZ  1 
ATOM   2061 N N   . GLU A 1 243 ? -4.302  0.459  66.793  1.00 15.66 ? 243 GLU A N   1 
ATOM   2062 C CA  . GLU A 1 243 ? -5.533  -0.110 67.330  1.00 14.37 ? 243 GLU A CA  1 
ATOM   2063 C C   . GLU A 1 243 ? -6.753  0.612  66.770  1.00 14.74 ? 243 GLU A C   1 
ATOM   2064 O O   . GLU A 1 243 ? -7.725  -0.026 66.351  1.00 16.28 ? 243 GLU A O   1 
ATOM   2065 C CB  . GLU A 1 243 ? -5.554  -0.039 68.864  1.00 14.70 ? 243 GLU A CB  1 
ATOM   2066 C CG  . GLU A 1 243 ? -6.912  -0.536 69.407  1.00 20.58 ? 243 GLU A CG  1 
ATOM   2067 C CD  . GLU A 1 243 ? -7.197  -0.151 70.845  1.00 21.83 ? 243 GLU A CD  1 
ATOM   2068 O OE1 . GLU A 1 243 ? -8.161  -0.717 71.394  1.00 27.05 ? 243 GLU A OE1 1 
ATOM   2069 O OE2 . GLU A 1 243 ? -6.471  0.680  71.430  1.00 22.64 ? 243 GLU A OE2 1 
ATOM   2070 N N   . ILE A 1 244 ? -6.699  1.942  66.723  1.00 16.07 ? 244 ILE A N   1 
ATOM   2071 C CA  . ILE A 1 244 ? -7.889  2.728  66.421  1.00 17.96 ? 244 ILE A CA  1 
ATOM   2072 C C   . ILE A 1 244 ? -8.115  2.828  64.919  1.00 18.55 ? 244 ILE A C   1 
ATOM   2073 O O   . ILE A 1 244 ? -9.266  2.776  64.450  1.00 16.88 ? 244 ILE A O   1 
ATOM   2074 C CB  . ILE A 1 244 ? -7.782  4.120  67.066  1.00 16.40 ? 244 ILE A CB  1 
ATOM   2075 C CG1 . ILE A 1 244 ? -7.656  4.013  68.597  1.00 20.20 ? 244 ILE A CG1 1 
ATOM   2076 C CG2 . ILE A 1 244 ? -8.986  4.984  66.658  1.00 20.57 ? 244 ILE A CG2 1 
ATOM   2077 C CD1 . ILE A 1 244 ? -8.785  3.213  69.260  1.00 15.58 ? 244 ILE A CD1 1 
ATOM   2078 N N   . PHE A 1 245 ? -7.030  2.950  64.148  1.00 15.35 ? 245 PHE A N   1 
ATOM   2079 C CA  . PHE A 1 245 ? -7.124  3.246  62.724  1.00 16.43 ? 245 PHE A CA  1 
ATOM   2080 C C   . PHE A 1 245 ? -6.532  2.190  61.803  1.00 21.51 ? 245 PHE A C   1 
ATOM   2081 O O   . PHE A 1 245 ? -6.749  2.277  60.592  1.00 21.54 ? 245 PHE A O   1 
ATOM   2082 C CB  . PHE A 1 245 ? -6.458  4.596  62.428  1.00 16.77 ? 245 PHE A CB  1 
ATOM   2083 C CG  . PHE A 1 245 ? -7.097  5.722  63.145  1.00 16.80 ? 245 PHE A CG  1 
ATOM   2084 C CD1 . PHE A 1 245 ? -8.366  6.135  62.787  1.00 19.61 ? 245 PHE A CD1 1 
ATOM   2085 C CD2 . PHE A 1 245 ? -6.456  6.353  64.196  1.00 19.14 ? 245 PHE A CD2 1 
ATOM   2086 C CE1 . PHE A 1 245 ? -8.990  7.166  63.460  1.00 16.88 ? 245 PHE A CE1 1 
ATOM   2087 C CE2 . PHE A 1 245 ? -7.072  7.385  64.884  1.00 17.55 ? 245 PHE A CE2 1 
ATOM   2088 C CZ  . PHE A 1 245 ? -8.332  7.799  64.516  1.00 22.95 ? 245 PHE A CZ  1 
ATOM   2089 N N   . GLY A 1 246 ? -5.813  1.199  62.315  1.00 13.82 ? 246 GLY A N   1 
ATOM   2090 C CA  . GLY A 1 246 ? -5.523  0.036  61.487  1.00 15.65 ? 246 GLY A CA  1 
ATOM   2091 C C   . GLY A 1 246 ? -4.276  0.126  60.638  1.00 18.94 ? 246 GLY A C   1 
ATOM   2092 O O   . GLY A 1 246 ? -4.088  -0.713 59.746  1.00 20.49 ? 246 GLY A O   1 
ATOM   2093 N N   . GLU A 1 247 ? -3.416  1.101  60.888  1.00 18.97 ? 247 GLU A N   1 
ATOM   2094 C CA  . GLU A 1 247 ? -2.138  1.194  60.206  1.00 21.94 ? 247 GLU A CA  1 
ATOM   2095 C C   . GLU A 1 247 ? -1.196  1.883  61.165  1.00 18.91 ? 247 GLU A C   1 
ATOM   2096 O O   . GLU A 1 247 ? -1.623  2.518  62.127  1.00 18.44 ? 247 GLU A O   1 
ATOM   2097 C CB  . GLU A 1 247 ? -2.240  1.982  58.892  1.00 24.70 ? 247 GLU A CB  1 
ATOM   2098 C CG  . GLU A 1 247 ? -2.613  3.447  59.089  1.00 26.60 ? 247 GLU A CG  1 
ATOM   2099 C CD  . GLU A 1 247 ? -3.047  4.131  57.798  1.00 35.18 ? 247 GLU A CD  1 
ATOM   2100 O OE1 . GLU A 1 247 ? -2.555  5.243  57.519  1.00 43.43 ? 247 GLU A OE1 1 
ATOM   2101 O OE2 . GLU A 1 247 ? -3.874  3.556  57.066  1.00 43.24 ? 247 GLU A OE2 1 
ATOM   2102 N N   . HIS A 1 248 ? 0.087   1.747  60.916  1.00 20.39 ? 248 HIS A N   1 
ATOM   2103 C CA  . HIS A 1 248 ? 1.017   2.558  61.666  1.00 19.35 ? 248 HIS A CA  1 
ATOM   2104 C C   . HIS A 1 248 ? 0.965   3.987  61.138  1.00 17.45 ? 248 HIS A C   1 
ATOM   2105 O O   . HIS A 1 248 ? 0.861   4.193  59.931  1.00 21.77 ? 248 HIS A O   1 
ATOM   2106 C CB  . HIS A 1 248 ? 2.425   1.978  61.567  1.00 25.08 ? 248 HIS A CB  1 
ATOM   2107 C CG  . HIS A 1 248 ? 2.589   0.713  62.351  1.00 43.30 ? 248 HIS A CG  1 
ATOM   2108 N ND1 . HIS A 1 248 ? 2.584   0.695  63.731  1.00 45.48 ? 248 HIS A ND1 1 
ATOM   2109 C CD2 . HIS A 1 248 ? 2.721   -0.577 61.957  1.00 48.88 ? 248 HIS A CD2 1 
ATOM   2110 C CE1 . HIS A 1 248 ? 2.733   -0.548 64.153  1.00 50.10 ? 248 HIS A CE1 1 
ATOM   2111 N NE2 . HIS A 1 248 ? 2.815   -1.341 63.097  1.00 51.33 ? 248 HIS A NE2 1 
ATOM   2112 N N   . PRO A 1 249 ? 0.981   4.985  62.015  1.00 15.65 ? 249 PRO A N   1 
ATOM   2113 C CA  . PRO A 1 249 ? 0.842   6.371  61.550  1.00 18.84 ? 249 PRO A CA  1 
ATOM   2114 C C   . PRO A 1 249 ? 2.079   6.779  60.771  1.00 17.88 ? 249 PRO A C   1 
ATOM   2115 O O   . PRO A 1 249 ? 3.210   6.592  61.233  1.00 27.08 ? 249 PRO A O   1 
ATOM   2116 C CB  . PRO A 1 249 ? 0.698   7.176  62.848  1.00 17.00 ? 249 PRO A CB  1 
ATOM   2117 C CG  . PRO A 1 249 ? 1.401   6.337  63.883  1.00 16.73 ? 249 PRO A CG  1 
ATOM   2118 C CD  . PRO A 1 249 ? 1.183   4.894  63.472  1.00 17.50 ? 249 PRO A CD  1 
ATOM   2119 N N   . VAL A 1 250 ? 1.864   7.336  59.582  1.00 14.33 ? 250 VAL A N   1 
ATOM   2120 C CA  . VAL A 1 250 ? 2.977   7.904  58.823  1.00 20.69 ? 250 VAL A CA  1 
ATOM   2121 C C   . VAL A 1 250 ? 3.074   9.413  58.976  1.00 18.00 ? 250 VAL A C   1 
ATOM   2122 O O   . VAL A 1 250 ? 4.084   9.995  58.555  1.00 18.36 ? 250 VAL A O   1 
ATOM   2123 C CB  . VAL A 1 250 ? 2.912   7.523  57.328  1.00 30.40 ? 250 VAL A CB  1 
ATOM   2124 C CG1 . VAL A 1 250 ? 3.106   6.006  57.170  1.00 36.06 ? 250 VAL A CG1 1 
ATOM   2125 C CG2 . VAL A 1 250 ? 1.615   7.980  56.714  1.00 23.14 ? 250 VAL A CG2 1 
ATOM   2126 N N   . TYR A 1 251 ? 2.084   10.062 59.604  1.00 14.95 ? 251 TYR A N   1 
ATOM   2127 C CA  . TYR A 1 251 ? 2.181   11.474 59.944  1.00 14.90 ? 251 TYR A CA  1 
ATOM   2128 C C   . TYR A 1 251 ? 2.082   11.622 61.450  1.00 12.23 ? 251 TYR A C   1 
ATOM   2129 O O   . TYR A 1 251 ? 1.312   10.912 62.107  1.00 14.98 ? 251 TYR A O   1 
ATOM   2130 C CB  . TYR A 1 251 ? 1.061   12.316 59.272  1.00 20.41 ? 251 TYR A CB  1 
ATOM   2131 C CG  . TYR A 1 251 ? 0.707   11.802 57.904  1.00 25.72 ? 251 TYR A CG  1 
ATOM   2132 C CD1 . TYR A 1 251 ? 1.609   11.926 56.866  1.00 29.53 ? 251 TYR A CD1 1 
ATOM   2133 C CD2 . TYR A 1 251 ? -0.502  11.164 57.657  1.00 32.43 ? 251 TYR A CD2 1 
ATOM   2134 C CE1 . TYR A 1 251 ? 1.328   11.454 55.623  1.00 30.73 ? 251 TYR A CE1 1 
ATOM   2135 C CE2 . TYR A 1 251 ? -0.798  10.688 56.394  1.00 24.23 ? 251 TYR A CE2 1 
ATOM   2136 C CZ  . TYR A 1 251 ? 0.137   10.840 55.386  1.00 31.32 ? 251 TYR A CZ  1 
ATOM   2137 O OH  . TYR A 1 251 ? -0.075  10.375 54.110  1.00 37.99 ? 251 TYR A OH  1 
ATOM   2138 N N   . MET A 1 252 ? 2.891   12.524 61.994  1.00 12.93 ? 252 MET A N   1 
ATOM   2139 C CA  . MET A 1 252 ? 2.803   12.849 63.410  1.00 16.34 ? 252 MET A CA  1 
ATOM   2140 C C   . MET A 1 252 ? 2.922   14.348 63.580  1.00 18.36 ? 252 MET A C   1 
ATOM   2141 O O   . MET A 1 252 ? 3.673   15.010 62.850  1.00 15.32 ? 252 MET A O   1 
ATOM   2142 C CB  . MET A 1 252 ? 3.898   12.162 64.236  1.00 22.05 ? 252 MET A CB  1 
ATOM   2143 C CG  . MET A 1 252 ? 3.552   10.754 64.642  1.00 23.71 ? 252 MET A CG  1 
ATOM   2144 S SD  . MET A 1 252 ? 4.571   10.207 66.023  1.00 20.59 ? 252 MET A SD  1 
ATOM   2145 C CE  . MET A 1 252 ? 3.875   8.555  66.235  1.00 22.36 ? 252 MET A CE  1 
ATOM   2146 N N   . TRP A 1 253 ? 2.175   14.875 64.549  1.00 13.23 ? 253 TRP A N   1 
ATOM   2147 C CA  . TRP A 1 253 ? 2.335   16.251 64.967  1.00 8.59  ? 253 TRP A CA  1 
ATOM   2148 C C   . TRP A 1 253 ? 3.274   16.277 66.163  1.00 12.80 ? 253 TRP A C   1 
ATOM   2149 O O   . TRP A 1 253 ? 2.950   15.679 67.205  1.00 14.23 ? 253 TRP A O   1 
ATOM   2150 C CB  . TRP A 1 253 ? 0.988   16.851 65.339  1.00 8.56  ? 253 TRP A CB  1 
ATOM   2151 C CG  . TRP A 1 253 ? 1.121   18.178 66.023  1.00 12.62 ? 253 TRP A CG  1 
ATOM   2152 C CD1 . TRP A 1 253 ? 0.835   18.464 67.346  1.00 12.76 ? 253 TRP A CD1 1 
ATOM   2153 C CD2 . TRP A 1 253 ? 1.599   19.399 65.441  1.00 13.62 ? 253 TRP A CD2 1 
ATOM   2154 N NE1 . TRP A 1 253 ? 1.092   19.793 67.599  1.00 14.51 ? 253 TRP A NE1 1 
ATOM   2155 C CE2 . TRP A 1 253 ? 1.567   20.387 66.455  1.00 15.28 ? 253 TRP A CE2 1 
ATOM   2156 C CE3 . TRP A 1 253 ? 2.064   19.756 64.159  1.00 13.89 ? 253 TRP A CE3 1 
ATOM   2157 C CZ2 . TRP A 1 253 ? 1.982   21.702 66.231  1.00 16.56 ? 253 TRP A CZ2 1 
ATOM   2158 C CZ3 . TRP A 1 253 ? 2.474   21.055 63.939  1.00 12.63 ? 253 TRP A CZ3 1 
ATOM   2159 C CH2 . TRP A 1 253 ? 2.423   22.019 64.962  1.00 14.56 ? 253 TRP A CH2 1 
ATOM   2160 N N   . PRO A 1 254 ? 4.436   16.909 66.068  1.00 12.88 ? 254 PRO A N   1 
ATOM   2161 C CA  . PRO A 1 254 ? 5.321   16.994 67.238  1.00 16.84 ? 254 PRO A CA  1 
ATOM   2162 C C   . PRO A 1 254 ? 4.740   17.953 68.256  1.00 12.34 ? 254 PRO A C   1 
ATOM   2163 O O   . PRO A 1 254 ? 4.402   19.089 67.901  1.00 13.01 ? 254 PRO A O   1 
ATOM   2164 C CB  . PRO A 1 254 ? 6.636   17.533 66.652  1.00 14.94 ? 254 PRO A CB  1 
ATOM   2165 C CG  . PRO A 1 254 ? 6.198   18.302 65.414  1.00 20.67 ? 254 PRO A CG  1 
ATOM   2166 C CD  . PRO A 1 254 ? 4.982   17.603 64.875  1.00 14.92 ? 254 PRO A CD  1 
ATOM   2167 N N   . PRO A 1 255 ? 4.594   17.547 69.517  1.00 12.32 ? 255 PRO A N   1 
ATOM   2168 C CA  . PRO A 1 255 ? 3.979   18.442 70.510  1.00 14.47 ? 255 PRO A CA  1 
ATOM   2169 C C   . PRO A 1 255 ? 4.645   19.809 70.557  1.00 14.20 ? 255 PRO A C   1 
ATOM   2170 O O   . PRO A 1 255 ? 5.866   19.920 70.562  1.00 14.53 ? 255 PRO A O   1 
ATOM   2171 C CB  . PRO A 1 255 ? 4.150   17.676 71.828  1.00 12.46 ? 255 PRO A CB  1 
ATOM   2172 C CG  . PRO A 1 255 ? 4.126   16.283 71.433  1.00 9.16  ? 255 PRO A CG  1 
ATOM   2173 C CD  . PRO A 1 255 ? 4.830   16.213 70.064  1.00 11.97 ? 255 PRO A CD  1 
ATOM   2174 N N   . GLN A 1 256 ? 3.816   20.855 70.563  1.00 14.04 ? 256 GLN A N   1 
ATOM   2175 C CA  . GLN A 1 256 ? 4.265   22.246 70.578  1.00 16.05 ? 256 GLN A CA  1 
ATOM   2176 C C   . GLN A 1 256 ? 5.092   22.586 69.339  1.00 14.18 ? 256 GLN A C   1 
ATOM   2177 O O   . GLN A 1 256 ? 5.908   23.505 69.367  1.00 13.45 ? 256 GLN A O   1 
ATOM   2178 C CB  . GLN A 1 256 ? 5.045   22.566 71.867  1.00 14.35 ? 256 GLN A CB  1 
ATOM   2179 C CG  . GLN A 1 256 ? 4.375   22.063 73.174  1.00 16.84 ? 256 GLN A CG  1 
ATOM   2180 C CD  . GLN A 1 256 ? 3.106   22.831 73.508  1.00 22.53 ? 256 GLN A CD  1 
ATOM   2181 O OE1 . GLN A 1 256 ? 2.805   23.868 72.907  1.00 23.06 ? 256 GLN A OE1 1 
ATOM   2182 N NE2 . GLN A 1 256 ? 2.362   22.334 74.452  1.00 17.49 ? 256 GLN A NE2 1 
ATOM   2183 N N   . ALA A 1 257 ? 4.881   21.855 68.236  1.00 10.98 ? 257 ALA A N   1 
ATOM   2184 C CA  . ALA A 1 257 ? 5.675   22.000 67.010  1.00 12.92 ? 257 ALA A CA  1 
ATOM   2185 C C   . ALA A 1 257 ? 7.158   21.721 67.264  1.00 15.61 ? 257 ALA A C   1 
ATOM   2186 O O   . ALA A 1 257 ? 8.016   22.106 66.466  1.00 15.25 ? 257 ALA A O   1 
ATOM   2187 C CB  . ALA A 1 257 ? 5.505   23.395 66.378  1.00 12.03 ? 257 ALA A CB  1 
ATOM   2188 N N   . SER A 1 258 ? 7.482   21.033 68.353  1.00 13.32 ? 258 SER A N   1 
ATOM   2189 C CA  . SER A 1 258 ? 8.857   20.993 68.831  1.00 12.03 ? 258 SER A CA  1 
ATOM   2190 C C   . SER A 1 258 ? 9.676   19.979 68.053  1.00 15.07 ? 258 SER A C   1 
ATOM   2191 O O   . SER A 1 258 ? 9.329   18.791 67.998  1.00 15.70 ? 258 SER A O   1 
ATOM   2192 C CB  . SER A 1 258 ? 8.905   20.652 70.308  1.00 16.81 ? 258 SER A CB  1 
ATOM   2193 O OG  . SER A 1 258 ? 10.210  20.906 70.754  1.00 20.44 ? 258 SER A OG  1 
ATOM   2194 N N   . VAL A 1 259 ? 10.775  20.448 67.473  1.00 15.15 ? 259 VAL A N   1 
ATOM   2195 C CA  . VAL A 1 259 ? 11.678  19.625 66.683  1.00 13.55 ? 259 VAL A CA  1 
ATOM   2196 C C   . VAL A 1 259 ? 13.106  19.975 67.067  1.00 16.17 ? 259 VAL A C   1 
ATOM   2197 O O   . VAL A 1 259 ? 13.374  20.980 67.730  1.00 17.12 ? 259 VAL A O   1 
ATOM   2198 C CB  . VAL A 1 259 ? 11.470  19.812 65.160  1.00 19.69 ? 259 VAL A CB  1 
ATOM   2199 C CG1 . VAL A 1 259 ? 10.169  19.163 64.714  1.00 17.54 ? 259 VAL A CG1 1 
ATOM   2200 C CG2 . VAL A 1 259 ? 11.462  21.294 64.804  1.00 25.46 ? 259 VAL A CG2 1 
ATOM   2201 N N   . SER A 1 260 ? 14.019  19.111 66.633  1.00 16.94 ? 260 SER A N   1 
ATOM   2202 C CA  . SER A 1 260 ? 15.457  19.255 66.750  1.00 14.30 ? 260 SER A CA  1 
ATOM   2203 C C   . SER A 1 260 ? 16.033  18.249 65.768  1.00 14.04 ? 260 SER A C   1 
ATOM   2204 O O   . SER A 1 260 ? 15.313  17.386 65.263  1.00 13.46 ? 260 SER A O   1 
ATOM   2205 C CB  . SER A 1 260 ? 15.951  18.966 68.164  1.00 19.01 ? 260 SER A CB  1 
ATOM   2206 O OG  . SER A 1 260 ? 15.769  17.578 68.443  1.00 17.11 ? 260 SER A OG  1 
ATOM   2207 N N   . ASN A 1 261 ? 17.326  18.373 65.478  1.00 15.83 ? 261 ASN A N   1 
ATOM   2208 C CA  . ASN A 1 261 ? 17.947  17.392 64.590  1.00 14.71 ? 261 ASN A CA  1 
ATOM   2209 C C   . ASN A 1 261 ? 17.747  15.980 65.142  1.00 15.30 ? 261 ASN A C   1 
ATOM   2210 O O   . ASN A 1 261 ? 17.382  15.052 64.413  1.00 17.11 ? 261 ASN A O   1 
ATOM   2211 C CB  . ASN A 1 261 ? 19.436  17.703 64.424  1.00 15.71 ? 261 ASN A CB  1 
ATOM   2212 C CG  . ASN A 1 261 ? 19.678  18.950 63.603  1.00 20.31 ? 261 ASN A CG  1 
ATOM   2213 O OD1 . ASN A 1 261 ? 18.871  19.311 62.754  1.00 20.48 ? 261 ASN A OD1 1 
ATOM   2214 N ND2 . ASN A 1 261 ? 20.782  19.612 63.858  1.00 23.34 ? 261 ASN A ND2 1 
ATOM   2215 N N   . GLU A 1 262 ? 17.970  15.801 66.445  1.00 15.67 ? 262 GLU A N   1 
ATOM   2216 C CA  . GLU A 1 262 ? 17.845  14.463 67.012  1.00 17.53 ? 262 GLU A CA  1 
ATOM   2217 C C   . GLU A 1 262 ? 16.392  13.990 66.993  1.00 21.42 ? 262 GLU A C   1 
ATOM   2218 O O   . GLU A 1 262 ? 16.126  12.820 66.689  1.00 19.07 ? 262 GLU A O   1 
ATOM   2219 C CB  . GLU A 1 262 ? 18.428  14.430 68.435  1.00 15.93 ? 262 GLU A CB  1 
ATOM   2220 C CG  . GLU A 1 262 ? 19.918  14.733 68.471  1.00 21.41 ? 262 GLU A CG  1 
ATOM   2221 C CD  . GLU A 1 262 ? 20.538  14.442 69.817  1.00 29.35 ? 262 GLU A CD  1 
ATOM   2222 O OE1 . GLU A 1 262 ? 19.910  13.715 70.626  1.00 33.07 ? 262 GLU A OE1 1 
ATOM   2223 O OE2 . GLU A 1 262 ? 21.629  14.965 70.080  1.00 29.15 ? 262 GLU A OE2 1 
ATOM   2224 N N   . ALA A 1 263 ? 15.432  14.883 67.291  1.00 14.14 ? 263 ALA A N   1 
ATOM   2225 C CA  . ALA A 1 263 ? 14.028  14.485 67.246  1.00 16.02 ? 263 ALA A CA  1 
ATOM   2226 C C   . ALA A 1 263 ? 13.598  14.091 65.837  1.00 13.96 ? 263 ALA A C   1 
ATOM   2227 O O   . ALA A 1 263 ? 12.884  13.104 65.663  1.00 15.65 ? 263 ALA A O   1 
ATOM   2228 C CB  . ALA A 1 263 ? 13.133  15.589 67.814  1.00 14.47 ? 263 ALA A CB  1 
ATOM   2229 N N   . LEU A 1 264 ? 14.016  14.852 64.815  1.00 13.48 ? 264 LEU A N   1 
ATOM   2230 C CA  . LEU A 1 264 ? 13.684  14.478 63.447  1.00 16.08 ? 264 LEU A CA  1 
ATOM   2231 C C   . LEU A 1 264 ? 14.277  13.116 63.097  1.00 17.36 ? 264 LEU A C   1 
ATOM   2232 O O   . LEU A 1 264 ? 13.641  12.306 62.408  1.00 19.87 ? 264 LEU A O   1 
ATOM   2233 C CB  . LEU A 1 264 ? 14.151  15.566 62.478  1.00 15.60 ? 264 LEU A CB  1 
ATOM   2234 C CG  . LEU A 1 264 ? 13.383  16.884 62.624  1.00 18.72 ? 264 LEU A CG  1 
ATOM   2235 C CD1 . LEU A 1 264 ? 14.082  18.024 61.881  1.00 18.89 ? 264 LEU A CD1 1 
ATOM   2236 C CD2 . LEU A 1 264 ? 11.968  16.709 62.102  1.00 24.00 ? 264 LEU A CD2 1 
ATOM   2237 N N   . GLU A 1 265 ? 15.487  12.837 63.573  1.00 16.46 ? 265 GLU A N   1 
ATOM   2238 C CA  . GLU A 1 265 ? 16.058  11.516 63.347  1.00 20.70 ? 265 GLU A CA  1 
ATOM   2239 C C   . GLU A 1 265 ? 15.222  10.421 64.012  1.00 16.90 ? 265 GLU A C   1 
ATOM   2240 O O   . GLU A 1 265 ? 15.001  9.361  63.416  1.00 16.83 ? 265 GLU A O   1 
ATOM   2241 C CB  . GLU A 1 265 ? 17.499  11.482 63.853  1.00 22.62 ? 265 GLU A CB  1 
ATOM   2242 C CG  . GLU A 1 265 ? 18.143  10.099 63.840  1.00 35.55 ? 265 GLU A CG  1 
ATOM   2243 C CD  . GLU A 1 265 ? 18.665  9.686  62.465  1.00 47.33 ? 265 GLU A CD  1 
ATOM   2244 O OE1 . GLU A 1 265 ? 18.661  8.472  62.171  1.00 49.56 ? 265 GLU A OE1 1 
ATOM   2245 O OE2 . GLU A 1 265 ? 19.074  10.567 61.680  1.00 54.05 ? 265 GLU A OE2 1 
ATOM   2246 N N   . LEU A 1 266 ? 14.748  10.655 65.245  1.00 16.60 ? 266 LEU A N   1 
ATOM   2247 C CA  . LEU A 1 266 ? 13.931  9.643  65.922  1.00 14.42 ? 266 LEU A CA  1 
ATOM   2248 C C   . LEU A 1 266 ? 12.632  9.386  65.162  1.00 16.17 ? 266 LEU A C   1 
ATOM   2249 O O   . LEU A 1 266 ? 12.257  8.236  64.924  1.00 16.38 ? 266 LEU A O   1 
ATOM   2250 C CB  . LEU A 1 266 ? 13.633  10.068 67.354  1.00 15.83 ? 266 LEU A CB  1 
ATOM   2251 C CG  . LEU A 1 266 ? 12.665  9.166  68.138  1.00 15.00 ? 266 LEU A CG  1 
ATOM   2252 C CD1 . LEU A 1 266 ? 13.258  7.767  68.332  1.00 18.54 ? 266 LEU A CD1 1 
ATOM   2253 C CD2 . LEU A 1 266 ? 12.307  9.804  69.498  1.00 14.21 ? 266 LEU A CD2 1 
ATOM   2254 N N   . TYR A 1 267 ? 11.927  10.452 64.778  1.00 13.73 ? 267 TYR A N   1 
ATOM   2255 C CA  . TYR A 1 267 ? 10.709  10.280 63.987  1.00 12.45 ? 267 TYR A CA  1 
ATOM   2256 C C   . TYR A 1 267 ? 10.980  9.459  62.732  1.00 18.21 ? 267 TYR A C   1 
ATOM   2257 O O   . TYR A 1 267 ? 10.213  8.546  62.394  1.00 16.25 ? 267 TYR A O   1 
ATOM   2258 C CB  . TYR A 1 267 ? 10.143  11.646 63.618  1.00 11.23 ? 267 TYR A CB  1 
ATOM   2259 C CG  . TYR A 1 267 ? 9.469   12.315 64.784  1.00 14.38 ? 267 TYR A CG  1 
ATOM   2260 C CD1 . TYR A 1 267 ? 8.356   11.737 65.395  1.00 16.53 ? 267 TYR A CD1 1 
ATOM   2261 C CD2 . TYR A 1 267 ? 9.906   13.540 65.239  1.00 12.98 ? 267 TYR A CD2 1 
ATOM   2262 C CE1 . TYR A 1 267 ? 7.734   12.360 66.480  1.00 18.58 ? 267 TYR A CE1 1 
ATOM   2263 C CE2 . TYR A 1 267 ? 9.305   14.173 66.333  1.00 13.93 ? 267 TYR A CE2 1 
ATOM   2264 C CZ  . TYR A 1 267 ? 8.206   13.579 66.932  1.00 21.83 ? 267 TYR A CZ  1 
ATOM   2265 O OH  . TYR A 1 267 ? 7.580   14.211 67.981  1.00 21.05 ? 267 TYR A OH  1 
ATOM   2266 N N   . TYR A 1 268 ? 12.090  9.745  62.049  1.00 16.76 ? 268 TYR A N   1 
ATOM   2267 C CA  . TYR A 1 268 ? 12.441  8.976  60.857  1.00 16.79 ? 268 TYR A CA  1 
ATOM   2268 C C   . TYR A 1 268 ? 12.694  7.509  61.194  1.00 17.99 ? 268 TYR A C   1 
ATOM   2269 O O   . TYR A 1 268 ? 12.181  6.607  60.520  1.00 20.11 ? 268 TYR A O   1 
ATOM   2270 C CB  . TYR A 1 268 ? 13.669  9.590  60.176  1.00 15.86 ? 268 TYR A CB  1 
ATOM   2271 C CG  . TYR A 1 268 ? 14.516  8.554  59.468  1.00 23.52 ? 268 TYR A CG  1 
ATOM   2272 C CD1 . TYR A 1 268 ? 14.141  8.063  58.220  1.00 25.41 ? 268 TYR A CD1 1 
ATOM   2273 C CD2 . TYR A 1 268 ? 15.675  8.056  60.054  1.00 17.97 ? 268 TYR A CD2 1 
ATOM   2274 C CE1 . TYR A 1 268 ? 14.908  7.103  57.564  1.00 29.31 ? 268 TYR A CE1 1 
ATOM   2275 C CE2 . TYR A 1 268 ? 16.433  7.092  59.418  1.00 21.33 ? 268 TYR A CE2 1 
ATOM   2276 C CZ  . TYR A 1 268 ? 16.051  6.621  58.175  1.00 26.69 ? 268 TYR A CZ  1 
ATOM   2277 O OH  . TYR A 1 268 ? 16.833  5.668  57.531  1.00 29.48 ? 268 TYR A OH  1 
ATOM   2278 N N   . GLU A 1 269 ? 13.496  7.253  62.231  1.00 15.80 ? 269 GLU A N   1 
ATOM   2279 C CA  . GLU A 1 269 ? 13.792  5.878  62.639  1.00 20.87 ? 269 GLU A CA  1 
ATOM   2280 C C   . GLU A 1 269 ? 12.530  5.105  63.021  1.00 19.31 ? 269 GLU A C   1 
ATOM   2281 O O   . GLU A 1 269 ? 12.499  3.879  62.893  1.00 22.57 ? 269 GLU A O   1 
ATOM   2282 C CB  . GLU A 1 269 ? 14.756  5.871  63.828  1.00 20.31 ? 269 GLU A CB  1 
ATOM   2283 C CG  . GLU A 1 269 ? 16.160  6.297  63.496  1.00 18.63 ? 269 GLU A CG  1 
ATOM   2284 C CD  . GLU A 1 269 ? 16.938  6.706  64.729  1.00 36.46 ? 269 GLU A CD  1 
ATOM   2285 O OE1 . GLU A 1 269 ? 16.381  6.638  65.853  1.00 38.33 ? 269 GLU A OE1 1 
ATOM   2286 O OE2 . GLU A 1 269 ? 18.105  7.108  64.572  1.00 38.46 ? 269 GLU A OE2 1 
ATOM   2287 N N   . LYS A 1 270 ? 11.489  5.788  63.490  1.00 16.76 ? 270 LYS A N   1 
ATOM   2288 C CA  . LYS A 1 270 ? 10.263  5.117  63.884  1.00 20.01 ? 270 LYS A CA  1 
ATOM   2289 C C   . LYS A 1 270 ? 9.259   5.048  62.738  1.00 17.65 ? 270 LYS A C   1 
ATOM   2290 O O   . LYS A 1 270 ? 8.106   4.675  62.960  1.00 19.63 ? 270 LYS A O   1 
ATOM   2291 C CB  . LYS A 1 270 ? 9.648   5.799  65.124  1.00 15.96 ? 270 LYS A CB  1 
ATOM   2292 C CG  . LYS A 1 270 ? 10.525  5.709  66.390  1.00 17.34 ? 270 LYS A CG  1 
ATOM   2293 C CD  . LYS A 1 270 ? 11.032  4.271  66.629  1.00 25.32 ? 270 LYS A CD  1 
ATOM   2294 C CE  . LYS A 1 270 ? 11.713  4.119  67.987  1.00 25.10 ? 270 LYS A CE  1 
ATOM   2295 N NZ  . LYS A 1 270 ? 12.415  2.819  68.153  1.00 39.57 ? 270 LYS A NZ  1 
ATOM   2296 N N   . GLY A 1 271 ? 9.677   5.375  61.513  1.00 20.19 ? 271 GLY A N   1 
ATOM   2297 C CA  . GLY A 1 271 ? 8.835   5.212  60.345  1.00 18.33 ? 271 GLY A CA  1 
ATOM   2298 C C   . GLY A 1 271 ? 7.903   6.357  60.032  1.00 17.97 ? 271 GLY A C   1 
ATOM   2299 O O   . GLY A 1 271 ? 6.991   6.179  59.210  1.00 25.07 ? 271 GLY A O   1 
ATOM   2300 N N   . ILE A 1 272 ? 8.066   7.520  60.664  1.00 16.73 ? 272 ILE A N   1 
ATOM   2301 C CA  . ILE A 1 272 ? 7.218   8.667  60.339  1.00 13.55 ? 272 ILE A CA  1 
ATOM   2302 C C   . ILE A 1 272 ? 7.728   9.265  59.040  1.00 17.41 ? 272 ILE A C   1 
ATOM   2303 O O   . ILE A 1 272 ? 8.932   9.510  58.901  1.00 21.83 ? 272 ILE A O   1 
ATOM   2304 C CB  . ILE A 1 272 ? 7.245   9.727  61.456  1.00 13.27 ? 272 ILE A CB  1 
ATOM   2305 C CG1 . ILE A 1 272 ? 6.803   9.148  62.812  1.00 19.85 ? 272 ILE A CG1 1 
ATOM   2306 C CG2 . ILE A 1 272 ? 6.450   10.998 61.020  1.00 17.73 ? 272 ILE A CG2 1 
ATOM   2307 C CD1 . ILE A 1 272 ? 5.555   8.333  62.773  1.00 24.90 ? 272 ILE A CD1 1 
ATOM   2308 N N   . ASN A 1 273 ? 6.822   9.500  58.083  1.00 17.11 ? 273 ASN A N   1 
ATOM   2309 C CA  . ASN A 1 273 ? 7.242   10.010 56.785  1.00 17.02 ? 273 ASN A CA  1 
ATOM   2310 C C   . ASN A 1 273 ? 7.092   11.522 56.652  1.00 14.49 ? 273 ASN A C   1 
ATOM   2311 O O   . ASN A 1 273 ? 7.763   12.109 55.797  1.00 17.25 ? 273 ASN A O   1 
ATOM   2312 C CB  . ASN A 1 273 ? 6.449   9.344  55.659  1.00 22.74 ? 273 ASN A CB  1 
ATOM   2313 C CG  . ASN A 1 273 ? 6.771   7.869  55.513  1.00 40.00 ? 273 ASN A CG  1 
ATOM   2314 O OD1 . ASN A 1 273 ? 7.900   7.432  55.765  1.00 42.56 ? 273 ASN A OD1 1 
ATOM   2315 N ND2 . ASN A 1 273 ? 5.777   7.092  55.108  1.00 44.71 ? 273 ASN A ND2 1 
ATOM   2316 N N   A MET A 1 274 ? 6.249   12.158 57.468  0.52 17.93 ? 274 MET A N   1 
ATOM   2317 N N   B MET A 1 274 ? 6.265   12.162 57.483  0.48 17.66 ? 274 MET A N   1 
ATOM   2318 C CA  A MET A 1 274 ? 6.002   13.595 57.373  0.52 16.78 ? 274 MET A CA  1 
ATOM   2319 C CA  B MET A 1 274 ? 6.007   13.594 57.364  0.48 16.79 ? 274 MET A CA  1 
ATOM   2320 C C   A MET A 1 274 ? 5.563   14.145 58.724  0.52 18.86 ? 274 MET A C   1 
ATOM   2321 C C   B MET A 1 274 ? 5.537   14.158 58.701  0.48 18.62 ? 274 MET A C   1 
ATOM   2322 O O   A MET A 1 274 ? 4.828   13.488 59.470  0.52 17.47 ? 274 MET A O   1 
ATOM   2323 O O   B MET A 1 274 ? 4.757   13.520 59.418  0.48 17.79 ? 274 MET A O   1 
ATOM   2324 C CB  A MET A 1 274 ? 4.925   13.929 56.331  0.52 18.62 ? 274 MET A CB  1 
ATOM   2325 C CB  B MET A 1 274 ? 4.953   13.892 56.289  0.48 18.87 ? 274 MET A CB  1 
ATOM   2326 C CG  A MET A 1 274 ? 4.784   15.434 56.070  0.52 20.15 ? 274 MET A CG  1 
ATOM   2327 C CG  B MET A 1 274 ? 4.837   15.381 55.971  0.48 20.82 ? 274 MET A CG  1 
ATOM   2328 S SD  A MET A 1 274 ? 3.596   16.285 57.139  0.52 21.81 ? 274 MET A SD  1 
ATOM   2329 S SD  B MET A 1 274 ? 3.543   15.789 54.786  0.48 21.81 ? 274 MET A SD  1 
ATOM   2330 C CE  A MET A 1 274 ? 2.097   16.036 56.190  0.52 21.18 ? 274 MET A CE  1 
ATOM   2331 C CE  B MET A 1 274 ? 2.097   15.699 55.825  0.48 20.33 ? 274 MET A CE  1 
ATOM   2332 N N   . LEU A 1 275 ? 6.010   15.362 59.022  1.00 17.58 ? 275 LEU A N   1 
ATOM   2333 C CA  . LEU A 1 275 ? 5.493   16.112 60.150  1.00 14.95 ? 275 LEU A CA  1 
ATOM   2334 C C   . LEU A 1 275 ? 5.407   17.580 59.743  1.00 17.06 ? 275 LEU A C   1 
ATOM   2335 O O   . LEU A 1 275 ? 5.880   17.981 58.672  1.00 16.38 ? 275 LEU A O   1 
ATOM   2336 C CB  . LEU A 1 275 ? 6.369   15.897 61.387  1.00 18.38 ? 275 LEU A CB  1 
ATOM   2337 C CG  . LEU A 1 275 ? 7.861   16.173 61.248  1.00 23.71 ? 275 LEU A CG  1 
ATOM   2338 C CD1 . LEU A 1 275 ? 8.103   17.642 61.408  1.00 19.74 ? 275 LEU A CD1 1 
ATOM   2339 C CD2 . LEU A 1 275 ? 8.641   15.381 62.297  1.00 29.79 ? 275 LEU A CD2 1 
ATOM   2340 N N   . ALA A 1 276 ? 4.835   18.402 60.614  1.00 12.69 ? 276 ALA A N   1 
ATOM   2341 C CA  . ALA A 1 276 ? 4.884   19.842 60.402  1.00 16.05 ? 276 ALA A CA  1 
ATOM   2342 C C   . ALA A 1 276 ? 5.497   20.492 61.631  1.00 14.70 ? 276 ALA A C   1 
ATOM   2343 O O   . ALA A 1 276 ? 5.516   19.915 62.722  1.00 16.74 ? 276 ALA A O   1 
ATOM   2344 C CB  . ALA A 1 276 ? 3.499   20.450 60.129  1.00 15.62 ? 276 ALA A CB  1 
ATOM   2345 N N   . THR A 1 277 ? 6.026   21.691 61.444  1.00 15.02 ? 277 THR A N   1 
ATOM   2346 C CA  . THR A 1 277 ? 6.511   22.459 62.588  1.00 13.87 ? 277 THR A CA  1 
ATOM   2347 C C   . THR A 1 277 ? 6.302   23.924 62.251  1.00 16.12 ? 277 THR A C   1 
ATOM   2348 O O   . THR A 1 277 ? 5.582   24.258 61.308  1.00 17.37 ? 277 THR A O   1 
ATOM   2349 C CB  . THR A 1 277 ? 7.964   22.103 62.928  1.00 14.56 ? 277 THR A CB  1 
ATOM   2350 O OG1 . THR A 1 277 ? 8.384   22.870 64.066  1.00 15.19 ? 277 THR A OG1 1 
ATOM   2351 C CG2 . THR A 1 277 ? 8.898   22.365 61.709  1.00 17.52 ? 277 THR A CG2 1 
ATOM   2352 N N   . ASP A 1 278 ? 6.909   24.807 63.028  1.00 16.14 ? 278 ASP A N   1 
ATOM   2353 C CA  . ASP A 1 278 ? 6.539   26.209 62.944  1.00 20.35 ? 278 ASP A CA  1 
ATOM   2354 C C   . ASP A 1 278 ? 7.482   26.990 62.045  1.00 22.19 ? 278 ASP A C   1 
ATOM   2355 O O   . ASP A 1 278 ? 8.685   26.708 61.949  1.00 17.64 ? 278 ASP A O   1 
ATOM   2356 C CB  . ASP A 1 278 ? 6.492   26.851 64.336  1.00 21.58 ? 278 ASP A CB  1 
ATOM   2357 C CG  . ASP A 1 278 ? 5.866   28.248 64.328  1.00 28.62 ? 278 ASP A CG  1 
ATOM   2358 O OD1 . ASP A 1 278 ? 4.973   28.545 63.515  1.00 27.63 ? 278 ASP A OD1 1 
ATOM   2359 O OD2 . ASP A 1 278 ? 6.305   29.085 65.140  1.00 34.37 ? 278 ASP A OD2 1 
ATOM   2360 N N   . GLU A 1 279 ? 6.901   28.007 61.405  1.00 27.22 ? 279 GLU A N   1 
ATOM   2361 C CA  . GLU A 1 279 ? 7.656   28.907 60.548  1.00 35.45 ? 279 GLU A CA  1 
ATOM   2362 C C   . GLU A 1 279 ? 8.863   29.526 61.252  1.00 31.01 ? 279 GLU A C   1 
ATOM   2363 O O   . GLU A 1 279 ? 9.884   29.789 60.605  1.00 31.83 ? 279 GLU A O   1 
ATOM   2364 C CB  . GLU A 1 279 ? 6.707   29.998 60.038  1.00 38.00 ? 279 GLU A CB  1 
ATOM   2365 C CG  . GLU A 1 279 ? 7.226   30.722 58.848  1.00 38.84 ? 279 GLU A CG  1 
ATOM   2366 C CD  . GLU A 1 279 ? 6.184   31.602 58.196  1.00 41.52 ? 279 GLU A CD  1 
ATOM   2367 O OE1 . GLU A 1 279 ? 4.966   31.458 58.506  1.00 28.36 ? 279 GLU A OE1 1 
ATOM   2368 O OE2 . GLU A 1 279 ? 6.598   32.426 57.355  1.00 40.10 ? 279 GLU A OE2 1 
ATOM   2369 N N   . VAL A 1 280 ? 8.779   29.757 62.570  1.00 27.49 ? 280 VAL A N   1 
ATOM   2370 C CA  . VAL A 1 280 ? 9.905   30.368 63.284  1.00 26.90 ? 280 VAL A CA  1 
ATOM   2371 C C   . VAL A 1 280 ? 11.132  29.476 63.235  1.00 23.70 ? 280 VAL A C   1 
ATOM   2372 O O   . VAL A 1 280 ? 12.261  29.969 63.199  1.00 28.47 ? 280 VAL A O   1 
ATOM   2373 C CB  . VAL A 1 280 ? 9.544   30.693 64.750  1.00 28.85 ? 280 VAL A CB  1 
ATOM   2374 C CG1 . VAL A 1 280 ? 9.409   29.413 65.570  1.00 36.52 ? 280 VAL A CG1 1 
ATOM   2375 C CG2 . VAL A 1 280 ? 10.612  31.588 65.382  1.00 33.74 ? 280 VAL A CG2 1 
ATOM   2376 N N   . ILE A 1 281 ? 10.941  28.156 63.260  1.00 26.24 ? 281 ILE A N   1 
ATOM   2377 C CA  . ILE A 1 281 ? 12.082  27.252 63.200  1.00 23.87 ? 281 ILE A CA  1 
ATOM   2378 C C   . ILE A 1 281 ? 12.708  27.316 61.814  1.00 24.90 ? 281 ILE A C   1 
ATOM   2379 O O   . ILE A 1 281 ? 13.940  27.327 61.666  1.00 23.98 ? 281 ILE A O   1 
ATOM   2380 C CB  . ILE A 1 281 ? 11.645  25.821 63.580  1.00 31.37 ? 281 ILE A CB  1 
ATOM   2381 C CG1 . ILE A 1 281 ? 11.122  25.795 65.025  1.00 42.82 ? 281 ILE A CG1 1 
ATOM   2382 C CG2 . ILE A 1 281 ? 12.774  24.819 63.390  1.00 30.12 ? 281 ILE A CG2 1 
ATOM   2383 C CD1 . ILE A 1 281 ? 9.967   24.850 65.244  1.00 51.68 ? 281 ILE A CD1 1 
ATOM   2384 N N   . LEU A 1 282 ? 11.862  27.397 60.778  1.00 28.38 ? 282 LEU A N   1 
ATOM   2385 C CA  . LEU A 1 282 ? 12.360  27.594 59.421  1.00 32.46 ? 282 LEU A CA  1 
ATOM   2386 C C   . LEU A 1 282 ? 13.180  28.879 59.332  1.00 28.17 ? 282 LEU A C   1 
ATOM   2387 O O   . LEU A 1 282 ? 14.321  28.868 58.859  1.00 31.17 ? 282 LEU A O   1 
ATOM   2388 C CB  . LEU A 1 282 ? 11.184  27.621 58.428  1.00 27.91 ? 282 LEU A CB  1 
ATOM   2389 C CG  . LEU A 1 282 ? 11.623  27.781 56.971  1.00 32.77 ? 282 LEU A CG  1 
ATOM   2390 C CD1 . LEU A 1 282 ? 12.575  26.649 56.559  1.00 31.63 ? 282 LEU A CD1 1 
ATOM   2391 C CD2 . LEU A 1 282 ? 10.434  27.909 56.013  1.00 30.33 ? 282 LEU A CD2 1 
ATOM   2392 N N   . LYS A 1 283 ? 12.607  29.998 59.797  1.00 34.14 ? 283 LYS A N   1 
ATOM   2393 C CA  . LYS A 1 283 ? 13.320  31.274 59.785  1.00 30.70 ? 283 LYS A CA  1 
ATOM   2394 C C   . LYS A 1 283 ? 14.579  31.226 60.640  1.00 32.12 ? 283 LYS A C   1 
ATOM   2395 O O   . LYS A 1 283 ? 15.580  31.867 60.304  1.00 37.18 ? 283 LYS A O   1 
ATOM   2396 C CB  . LYS A 1 283 ? 12.404  32.395 60.286  1.00 38.88 ? 283 LYS A CB  1 
ATOM   2397 C CG  . LYS A 1 283 ? 11.072  32.525 59.523  1.00 48.05 ? 283 LYS A CG  1 
ATOM   2398 C CD  . LYS A 1 283 ? 11.277  32.499 58.005  1.00 51.22 ? 283 LYS A CD  1 
ATOM   2399 C CE  . LYS A 1 283 ? 10.001  32.871 57.272  1.00 45.48 ? 283 LYS A CE  1 
ATOM   2400 N NZ  . LYS A 1 283 ? 9.330   34.018 57.953  1.00 56.07 ? 283 LYS A NZ  1 
ATOM   2401 N N   . ASN A 1 284 ? 14.551  30.473 61.741  1.00 24.62 ? 284 ASN A N   1 
ATOM   2402 C CA  . ASN A 1 284 ? 15.716  30.364 62.607  1.00 30.49 ? 284 ASN A CA  1 
ATOM   2403 C C   . ASN A 1 284 ? 16.810  29.518 61.980  1.00 24.75 ? 284 ASN A C   1 
ATOM   2404 O O   . ASN A 1 284 ? 17.967  29.604 62.404  1.00 33.04 ? 284 ASN A O   1 
ATOM   2405 C CB  . ASN A 1 284 ? 15.317  29.741 63.945  1.00 41.50 ? 284 ASN A CB  1 
ATOM   2406 C CG  . ASN A 1 284 ? 14.835  30.762 64.960  1.00 45.62 ? 284 ASN A CG  1 
ATOM   2407 O OD1 . ASN A 1 284 ? 14.764  31.958 64.677  1.00 38.51 ? 284 ASN A OD1 1 
ATOM   2408 N ND2 . ASN A 1 284 ? 14.478  30.280 66.154  1.00 37.23 ? 284 ASN A ND2 1 
ATOM   2409 N N   . SER A 1 285 ? 16.471  28.678 61.002  1.00 24.91 ? 285 SER A N   1 
ATOM   2410 C CA  . SER A 1 285 ? 17.387  27.645 60.546  1.00 27.94 ? 285 SER A CA  1 
ATOM   2411 C C   . SER A 1 285 ? 17.961  27.892 59.161  1.00 30.15 ? 285 SER A C   1 
ATOM   2412 O O   . SER A 1 285 ? 19.050  27.380 58.865  1.00 29.15 ? 285 SER A O   1 
ATOM   2413 C CB  . SER A 1 285 ? 16.692  26.272 60.572  1.00 25.25 ? 285 SER A CB  1 
ATOM   2414 O OG  . SER A 1 285 ? 16.072  26.039 61.838  1.00 24.33 ? 285 SER A OG  1 
ATOM   2415 N N   . VAL A 1 286 ? 17.276  28.671 58.325  1.00 34.12 ? 286 VAL A N   1 
ATOM   2416 C CA  . VAL A 1 286 ? 17.665  28.895 56.936  1.00 40.58 ? 286 VAL A CA  1 
ATOM   2417 C C   . VAL A 1 286 ? 17.301  30.325 56.549  1.00 40.08 ? 286 VAL A C   1 
ATOM   2418 O O   . VAL A 1 286 ? 16.157  30.756 56.743  1.00 37.97 ? 286 VAL A O   1 
ATOM   2419 C CB  . VAL A 1 286 ? 16.983  27.880 55.997  1.00 36.20 ? 286 VAL A CB  1 
ATOM   2420 C CG1 . VAL A 1 286 ? 17.003  28.376 54.558  1.00 33.70 ? 286 VAL A CG1 1 
ATOM   2421 C CG2 . VAL A 1 286 ? 17.677  26.522 56.108  1.00 38.65 ? 286 VAL A CG2 1 
ATOM   2422 N N   . GLU A 1 287 ? 18.269  31.049 55.981  1.00 37.47 ? 287 GLU A N   1 
ATOM   2423 C CA  . GLU A 1 287 ? 18.070  32.464 55.674  1.00 47.96 ? 287 GLU A CA  1 
ATOM   2424 C C   . GLU A 1 287 ? 16.945  32.666 54.662  1.00 49.29 ? 287 GLU A C   1 
ATOM   2425 O O   . GLU A 1 287 ? 15.956  33.358 54.938  1.00 46.88 ? 287 GLU A O   1 
ATOM   2426 C CB  . GLU A 1 287 ? 19.371  33.069 55.158  1.00 51.56 ? 287 GLU A CB  1 
ATOM   2427 C CG  . GLU A 1 287 ? 19.456  34.572 55.320  1.00 57.74 ? 287 GLU A CG  1 
ATOM   2428 C CD  . GLU A 1 287 ? 20.887  35.052 55.433  1.00 62.23 ? 287 GLU A CD  1 
ATOM   2429 O OE1 . GLU A 1 287 ? 21.797  34.195 55.481  1.00 68.32 ? 287 GLU A OE1 1 
ATOM   2430 O OE2 . GLU A 1 287 ? 21.106  36.279 55.466  1.00 63.64 ? 287 GLU A OE2 1 
ATOM   2431 N N   . ARG A 1 288 ? 17.084  32.075 53.478  1.00 51.19 ? 288 ARG A N   1 
ATOM   2432 C CA  . ARG A 1 288 ? 16.105  32.217 52.404  1.00 56.23 ? 288 ARG A CA  1 
ATOM   2433 C C   . ARG A 1 288 ? 15.254  30.955 52.367  1.00 52.26 ? 288 ARG A C   1 
ATOM   2434 O O   . ARG A 1 288 ? 15.726  29.892 51.947  1.00 52.13 ? 288 ARG A O   1 
ATOM   2435 C CB  . ARG A 1 288 ? 16.800  32.454 51.065  1.00 58.44 ? 288 ARG A CB  1 
ATOM   2436 C CG  . ARG A 1 288 ? 15.946  32.156 49.844  1.00 52.12 ? 288 ARG A CG  1 
ATOM   2437 C CD  . ARG A 1 288 ? 16.804  32.190 48.601  1.00 50.30 ? 288 ARG A CD  1 
ATOM   2438 N NE  . ARG A 1 288 ? 17.201  30.863 48.127  1.00 54.69 ? 288 ARG A NE  1 
ATOM   2439 C CZ  . ARG A 1 288 ? 18.274  30.644 47.363  1.00 52.01 ? 288 ARG A CZ  1 
ATOM   2440 N NH1 . ARG A 1 288 ? 19.052  31.658 47.020  1.00 38.40 ? 288 ARG A NH1 1 
ATOM   2441 N NH2 . ARG A 1 288 ? 18.576  29.415 46.955  1.00 52.30 ? 288 ARG A NH2 1 
ATOM   2442 N N   . ALA A 1 289 ? 14.001  31.068 52.802  1.00 41.86 ? 289 ALA A N   1 
ATOM   2443 C CA  . ALA A 1 289 ? 13.167  29.882 52.944  1.00 37.78 ? 289 ALA A CA  1 
ATOM   2444 C C   . ALA A 1 289 ? 11.705  30.283 52.828  1.00 31.96 ? 289 ALA A C   1 
ATOM   2445 O O   . ALA A 1 289 ? 11.183  31.005 53.682  1.00 37.72 ? 289 ALA A O   1 
ATOM   2446 C CB  . ALA A 1 289 ? 13.445  29.189 54.270  1.00 37.69 ? 289 ALA A CB  1 
ATOM   2447 N N   . SER A 1 290 ? 11.052  29.811 51.777  1.00 29.61 ? 290 SER A N   1 
ATOM   2448 C CA  . SER A 1 290 ? 9.619   30.007 51.645  1.00 20.76 ? 290 SER A CA  1 
ATOM   2449 C C   . SER A 1 290 ? 8.882   28.926 52.429  1.00 22.63 ? 290 SER A C   1 
ATOM   2450 O O   . SER A 1 290 ? 9.296   27.766 52.415  1.00 22.92 ? 290 SER A O   1 
ATOM   2451 C CB  . SER A 1 290 ? 9.210   29.938 50.172  1.00 19.95 ? 290 SER A CB  1 
ATOM   2452 O OG  . SER A 1 290 ? 7.803   29.792 50.044  1.00 24.63 ? 290 SER A OG  1 
ATOM   2453 N N   . PRO A 1 291 ? 7.807   29.266 53.144  1.00 23.18 ? 291 PRO A N   1 
ATOM   2454 C CA  . PRO A 1 291 ? 7.041   28.236 53.843  1.00 21.14 ? 291 PRO A CA  1 
ATOM   2455 C C   . PRO A 1 291 ? 6.060   27.483 52.963  1.00 21.20 ? 291 PRO A C   1 
ATOM   2456 O O   . PRO A 1 291 ? 5.320   26.652 53.484  1.00 16.15 ? 291 PRO A O   1 
ATOM   2457 C CB  . PRO A 1 291 ? 6.303   29.047 54.921  1.00 25.07 ? 291 PRO A CB  1 
ATOM   2458 C CG  . PRO A 1 291 ? 6.056   30.360 54.270  1.00 22.14 ? 291 PRO A CG  1 
ATOM   2459 C CD  . PRO A 1 291 ? 7.244   30.614 53.362  1.00 23.61 ? 291 PRO A CD  1 
ATOM   2460 N N   . TYR A 1 292 ? 6.037   27.727 51.649  1.00 19.42 ? 292 TYR A N   1 
ATOM   2461 C CA  . TYR A 1 292 ? 5.043   27.151 50.754  1.00 18.92 ? 292 TYR A CA  1 
ATOM   2462 C C   . TYR A 1 292 ? 5.553   25.919 50.019  1.00 16.82 ? 292 TYR A C   1 
ATOM   2463 O O   . TYR A 1 292 ? 4.859   25.411 49.128  1.00 17.36 ? 292 TYR A O   1 
ATOM   2464 C CB  . TYR A 1 292 ? 4.571   28.196 49.726  1.00 16.48 ? 292 TYR A CB  1 
ATOM   2465 C CG  . TYR A 1 292 ? 4.021   29.470 50.324  1.00 20.43 ? 292 TYR A CG  1 
ATOM   2466 C CD1 . TYR A 1 292 ? 3.260   29.451 51.476  1.00 22.14 ? 292 TYR A CD1 1 
ATOM   2467 C CD2 . TYR A 1 292 ? 4.273   30.705 49.719  1.00 31.61 ? 292 TYR A CD2 1 
ATOM   2468 C CE1 . TYR A 1 292 ? 2.750   30.634 52.028  1.00 21.32 ? 292 TYR A CE1 1 
ATOM   2469 C CE2 . TYR A 1 292 ? 3.768   31.878 50.255  1.00 30.79 ? 292 TYR A CE2 1 
ATOM   2470 C CZ  . TYR A 1 292 ? 3.011   31.834 51.402  1.00 25.83 ? 292 TYR A CZ  1 
ATOM   2471 O OH  . TYR A 1 292 ? 2.512   33.010 51.934  1.00 34.81 ? 292 TYR A OH  1 
ATOM   2472 N N   . LEU A 1 293 ? 6.718   25.410 50.399  1.00 15.53 ? 293 LEU A N   1 
ATOM   2473 C CA  . LEU A 1 293 ? 7.371   24.270 49.787  1.00 16.59 ? 293 LEU A CA  1 
ATOM   2474 C C   . LEU A 1 293 ? 7.252   23.057 50.701  1.00 24.73 ? 293 LEU A C   1 
ATOM   2475 O O   . LEU A 1 293 ? 7.085   23.194 51.914  1.00 19.38 ? 293 LEU A O   1 
ATOM   2476 C CB  . LEU A 1 293 ? 8.868   24.576 49.556  1.00 17.82 ? 293 LEU A CB  1 
ATOM   2477 C CG  . LEU A 1 293 ? 9.413   25.366 48.361  1.00 33.62 ? 293 LEU A CG  1 
ATOM   2478 C CD1 . LEU A 1 293 ? 8.526   26.514 47.926  1.00 26.54 ? 293 LEU A CD1 1 
ATOM   2479 C CD2 . LEU A 1 293 ? 10.831  25.858 48.666  1.00 33.97 ? 293 LEU A CD2 1 
ATOM   2480 N N   . ARG A 1 294 ? 7.394   21.867 50.116  1.00 19.62 ? 294 ARG A N   1 
ATOM   2481 C CA  . ARG A 1 294 ? 7.634   20.652 50.891  1.00 17.20 ? 294 ARG A CA  1 
ATOM   2482 C C   . ARG A 1 294 ? 9.136   20.498 51.111  1.00 15.26 ? 294 ARG A C   1 
ATOM   2483 O O   . ARG A 1 294 ? 9.895   20.411 50.142  1.00 19.30 ? 294 ARG A O   1 
ATOM   2484 C CB  . ARG A 1 294 ? 7.093   19.422 50.160  1.00 15.05 ? 294 ARG A CB  1 
ATOM   2485 C CG  . ARG A 1 294 ? 7.125   18.137 51.000  1.00 14.70 ? 294 ARG A CG  1 
ATOM   2486 C CD  . ARG A 1 294 ? 6.257   17.063 50.343  1.00 26.38 ? 294 ARG A CD  1 
ATOM   2487 N NE  . ARG A 1 294 ? 6.658   16.770 48.976  1.00 29.21 ? 294 ARG A NE  1 
ATOM   2488 C CZ  . ARG A 1 294 ? 5.821   16.659 47.946  1.00 26.70 ? 294 ARG A CZ  1 
ATOM   2489 N NH1 . ARG A 1 294 ? 4.508   16.839 48.117  1.00 23.19 ? 294 ARG A NH1 1 
ATOM   2490 N NH2 . ARG A 1 294 ? 6.293   16.377 46.734  1.00 28.23 ? 294 ARG A NH2 1 
ATOM   2491 N N   . TYR A 1 295 ? 9.564   20.472 52.372  1.00 16.95 ? 295 TYR A N   1 
ATOM   2492 C CA  . TYR A 1 295 ? 10.966  20.293 52.714  1.00 16.39 ? 295 TYR A CA  1 
ATOM   2493 C C   . TYR A 1 295 ? 11.257  18.831 53.028  1.00 17.21 ? 295 TYR A C   1 
ATOM   2494 O O   . TYR A 1 295 ? 10.392  18.087 53.505  1.00 19.75 ? 295 TYR A O   1 
ATOM   2495 C CB  . TYR A 1 295 ? 11.362  21.172 53.913  1.00 15.24 ? 295 TYR A CB  1 
ATOM   2496 C CG  . TYR A 1 295 ? 11.407  22.637 53.568  1.00 16.02 ? 295 TYR A CG  1 
ATOM   2497 C CD1 . TYR A 1 295 ? 10.236  23.384 53.460  1.00 15.78 ? 295 TYR A CD1 1 
ATOM   2498 C CD2 . TYR A 1 295 ? 12.620  23.274 53.330  1.00 20.60 ? 295 TYR A CD2 1 
ATOM   2499 C CE1 . TYR A 1 295 ? 10.269  24.729 53.129  1.00 16.74 ? 295 TYR A CE1 1 
ATOM   2500 C CE2 . TYR A 1 295 ? 12.664  24.629 52.993  1.00 23.40 ? 295 TYR A CE2 1 
ATOM   2501 C CZ  . TYR A 1 295 ? 11.485  25.351 52.911  1.00 19.46 ? 295 TYR A CZ  1 
ATOM   2502 O OH  . TYR A 1 295 ? 11.552  26.698 52.569  1.00 22.50 ? 295 TYR A OH  1 
ATOM   2503 N N   . TYR A 1 296 ? 12.487  18.422 52.725  1.00 17.57 ? 296 TYR A N   1 
ATOM   2504 C CA  . TYR A 1 296 ? 12.991  17.104 53.067  1.00 15.95 ? 296 TYR A CA  1 
ATOM   2505 C C   . TYR A 1 296 ? 14.190  17.286 53.975  1.00 19.46 ? 296 TYR A C   1 
ATOM   2506 O O   . TYR A 1 296 ? 15.178  17.921 53.591  1.00 22.62 ? 296 TYR A O   1 
ATOM   2507 C CB  . TYR A 1 296 ? 13.383  16.313 51.826  1.00 18.49 ? 296 TYR A CB  1 
ATOM   2508 C CG  . TYR A 1 296 ? 12.199  16.028 50.939  1.00 22.98 ? 296 TYR A CG  1 
ATOM   2509 C CD1 . TYR A 1 296 ? 11.433  14.885 51.111  1.00 32.67 ? 296 TYR A CD1 1 
ATOM   2510 C CD2 . TYR A 1 296 ? 11.830  16.908 49.949  1.00 44.37 ? 296 TYR A CD2 1 
ATOM   2511 C CE1 . TYR A 1 296 ? 10.344  14.625 50.297  1.00 34.65 ? 296 TYR A CE1 1 
ATOM   2512 C CE2 . TYR A 1 296 ? 10.748  16.648 49.142  1.00 45.79 ? 296 TYR A CE2 1 
ATOM   2513 C CZ  . TYR A 1 296 ? 10.012  15.516 49.317  1.00 38.57 ? 296 TYR A CZ  1 
ATOM   2514 O OH  . TYR A 1 296 ? 8.945   15.293 48.481  1.00 48.45 ? 296 TYR A OH  1 
ATOM   2515 N N   . PHE A 1 297 ? 14.096  16.752 55.178  1.00 20.19 ? 297 PHE A N   1 
ATOM   2516 C CA  . PHE A 1 297 ? 15.162  16.907 56.154  1.00 17.39 ? 297 PHE A CA  1 
ATOM   2517 C C   . PHE A 1 297 ? 16.152  15.777 55.932  1.00 18.24 ? 297 PHE A C   1 
ATOM   2518 O O   . PHE A 1 297 ? 15.845  14.612 56.216  1.00 21.86 ? 297 PHE A O   1 
ATOM   2519 C CB  . PHE A 1 297 ? 14.623  16.880 57.581  1.00 19.13 ? 297 PHE A CB  1 
ATOM   2520 C CG  . PHE A 1 297 ? 15.703  16.927 58.618  1.00 16.35 ? 297 PHE A CG  1 
ATOM   2521 C CD1 . PHE A 1 297 ? 16.349  18.117 58.901  1.00 16.96 ? 297 PHE A CD1 1 
ATOM   2522 C CD2 . PHE A 1 297 ? 16.072  15.788 59.297  1.00 16.52 ? 297 PHE A CD2 1 
ATOM   2523 C CE1 . PHE A 1 297 ? 17.356  18.167 59.850  1.00 17.48 ? 297 PHE A CE1 1 
ATOM   2524 C CE2 . PHE A 1 297 ? 17.079  15.818 60.251  1.00 19.86 ? 297 PHE A CE2 1 
ATOM   2525 C CZ  . PHE A 1 297 ? 17.741  17.013 60.527  1.00 19.76 ? 297 PHE A CZ  1 
ATOM   2526 N N   . ARG A 1 298 ? 17.327  16.118 55.405  1.00 19.37 ? 298 ARG A N   1 
ATOM   2527 C CA  . ARG A 1 298 ? 18.392  15.142 55.140  1.00 18.39 ? 298 ARG A CA  1 
ATOM   2528 C C   . ARG A 1 298 ? 17.890  13.994 54.268  1.00 19.86 ? 298 ARG A C   1 
ATOM   2529 O O   . ARG A 1 298 ? 18.423  12.884 54.325  1.00 21.07 ? 298 ARG A O   1 
ATOM   2530 C CB  . ARG A 1 298 ? 18.990  14.606 56.448  1.00 21.84 ? 298 ARG A CB  1 
ATOM   2531 C CG  . ARG A 1 298 ? 19.549  15.704 57.358  1.00 23.98 ? 298 ARG A CG  1 
ATOM   2532 C CD  . ARG A 1 298 ? 20.370  15.149 58.548  1.00 25.56 ? 298 ARG A CD  1 
ATOM   2533 N NE  . ARG A 1 298 ? 20.847  16.253 59.381  1.00 23.52 ? 298 ARG A NE  1 
ATOM   2534 C CZ  . ARG A 1 298 ? 21.150  16.156 60.665  1.00 27.53 ? 298 ARG A CZ  1 
ATOM   2535 N NH1 . ARG A 1 298 ? 21.036  14.991 61.291  1.00 25.34 ? 298 ARG A NH1 1 
ATOM   2536 N NH2 . ARG A 1 298 ? 21.576  17.229 61.326  1.00 30.28 ? 298 ARG A NH2 1 
ATOM   2537 N N   . GLU A 1 299 ? 16.854  14.266 53.460  1.00 23.27 ? 299 GLU A N   1 
ATOM   2538 C CA  . GLU A 1 299 ? 16.200  13.249 52.611  1.00 19.44 ? 299 GLU A CA  1 
ATOM   2539 C C   . GLU A 1 299 ? 15.773  12.022 53.426  1.00 23.15 ? 299 GLU A C   1 
ATOM   2540 O O   . GLU A 1 299 ? 15.743  10.898 52.918  1.00 21.12 ? 299 GLU A O   1 
ATOM   2541 C CB  . GLU A 1 299 ? 17.113  12.848 51.446  1.00 30.06 ? 299 GLU A CB  1 
ATOM   2542 C CG  . GLU A 1 299 ? 17.610  14.068 50.687  1.00 34.80 ? 299 GLU A CG  1 
ATOM   2543 C CD  . GLU A 1 299 ? 18.251  13.739 49.371  1.00 54.04 ? 299 GLU A CD  1 
ATOM   2544 O OE1 . GLU A 1 299 ? 17.869  14.372 48.362  1.00 58.18 ? 299 GLU A OE1 1 
ATOM   2545 O OE2 . GLU A 1 299 ? 19.149  12.869 49.348  1.00 55.36 ? 299 GLU A OE2 1 
ATOM   2546 N N   . LEU A 1 300 ? 15.455  12.226 54.711  1.00 17.02 ? 300 LEU A N   1 
ATOM   2547 C CA  . LEU A 1 300 ? 14.947  11.172 55.590  1.00 19.89 ? 300 LEU A CA  1 
ATOM   2548 C C   . LEU A 1 300 ? 13.450  11.271 55.849  1.00 21.48 ? 300 LEU A C   1 
ATOM   2549 O O   . LEU A 1 300 ? 12.782  10.240 56.026  1.00 22.11 ? 300 LEU A O   1 
ATOM   2550 C CB  . LEU A 1 300 ? 15.649  11.212 56.954  1.00 23.23 ? 300 LEU A CB  1 
ATOM   2551 C CG  . LEU A 1 300 ? 17.167  11.210 57.049  1.00 22.26 ? 300 LEU A CG  1 
ATOM   2552 C CD1 . LEU A 1 300 ? 17.586  11.533 58.477  1.00 28.47 ? 300 LEU A CD1 1 
ATOM   2553 C CD2 . LEU A 1 300 ? 17.704  9.850  56.631  1.00 23.07 ? 300 LEU A CD2 1 
ATOM   2554 N N   . ILE A 1 301 ? 12.923  12.488 55.929  1.00 18.89 ? 301 ILE A N   1 
ATOM   2555 C CA  . ILE A 1 301 ? 11.568  12.727 56.411  1.00 19.03 ? 301 ILE A CA  1 
ATOM   2556 C C   . ILE A 1 301 ? 11.111  14.061 55.835  1.00 24.12 ? 301 ILE A C   1 
ATOM   2557 O O   . ILE A 1 301 ? 11.909  14.991 55.682  1.00 20.72 ? 301 ILE A O   1 
ATOM   2558 C CB  . ILE A 1 301 ? 11.513  12.695 57.962  1.00 20.76 ? 301 ILE A CB  1 
ATOM   2559 C CG1 . ILE A 1 301 ? 10.083  12.820 58.475  1.00 20.71 ? 301 ILE A CG1 1 
ATOM   2560 C CG2 . ILE A 1 301 ? 12.411  13.770 58.567  1.00 16.68 ? 301 ILE A CG2 1 
ATOM   2561 C CD1 . ILE A 1 301 ? 9.965   12.568 60.011  1.00 20.16 ? 301 ILE A CD1 1 
ATOM   2562 N N   . SER A 1 302 ? 9.841   14.128 55.464  1.00 16.02 ? 302 SER A N   1 
ATOM   2563 C CA  . SER A 1 302 ? 9.280   15.348 54.904  1.00 18.62 ? 302 SER A CA  1 
ATOM   2564 C C   . SER A 1 302 ? 8.819   16.261 56.031  1.00 16.30 ? 302 SER A C   1 
ATOM   2565 O O   . SER A 1 302 ? 8.380   15.798 57.083  1.00 14.90 ? 302 SER A O   1 
ATOM   2566 C CB  . SER A 1 302 ? 8.104   15.036 53.971  1.00 16.26 ? 302 SER A CB  1 
ATOM   2567 O OG  . SER A 1 302 ? 8.559   14.294 52.842  1.00 21.32 ? 302 SER A OG  1 
ATOM   2568 N N   . VAL A 1 303 ? 8.953   17.567 55.813  1.00 17.89 ? 303 VAL A N   1 
ATOM   2569 C CA  . VAL A 1 303 ? 8.579   18.569 56.803  1.00 15.91 ? 303 VAL A CA  1 
ATOM   2570 C C   . VAL A 1 303 ? 7.847   19.689 56.081  1.00 14.27 ? 303 VAL A C   1 
ATOM   2571 O O   . VAL A 1 303 ? 8.306   20.167 55.039  1.00 20.42 ? 303 VAL A O   1 
ATOM   2572 C CB  . VAL A 1 303 ? 9.806   19.132 57.550  1.00 18.98 ? 303 VAL A CB  1 
ATOM   2573 C CG1 . VAL A 1 303 ? 9.358   20.191 58.585  1.00 17.50 ? 303 VAL A CG1 1 
ATOM   2574 C CG2 . VAL A 1 303 ? 10.637  18.003 58.239  1.00 17.97 ? 303 VAL A CG2 1 
ATOM   2575 N N   . PHE A 1 304 ? 6.708   20.102 56.619  1.00 14.30 ? 304 PHE A N   1 
ATOM   2576 C CA  . PHE A 1 304 ? 6.061   21.332 56.201  1.00 14.71 ? 304 PHE A CA  1 
ATOM   2577 C C   . PHE A 1 304 ? 6.136   22.336 57.336  1.00 17.46 ? 304 PHE A C   1 
ATOM   2578 O O   . PHE A 1 304 ? 6.032   21.963 58.505  1.00 18.51 ? 304 PHE A O   1 
ATOM   2579 C CB  . PHE A 1 304 ? 4.583   21.102 55.850  1.00 16.05 ? 304 PHE A CB  1 
ATOM   2580 C CG  . PHE A 1 304 ? 4.360   20.548 54.469  1.00 17.04 ? 304 PHE A CG  1 
ATOM   2581 C CD1 . PHE A 1 304 ? 4.469   21.369 53.348  1.00 19.87 ? 304 PHE A CD1 1 
ATOM   2582 C CD2 . PHE A 1 304 ? 4.037   19.221 54.292  1.00 18.11 ? 304 PHE A CD2 1 
ATOM   2583 C CE1 . PHE A 1 304 ? 4.239   20.861 52.068  1.00 21.40 ? 304 PHE A CE1 1 
ATOM   2584 C CE2 . PHE A 1 304 ? 3.803   18.709 53.018  1.00 24.54 ? 304 PHE A CE2 1 
ATOM   2585 C CZ  . PHE A 1 304 ? 3.904   19.531 51.908  1.00 21.01 ? 304 PHE A CZ  1 
ATOM   2586 N N   . PHE A 1 305 ? 6.293   23.601 56.991  1.00 17.57 ? 305 PHE A N   1 
ATOM   2587 C CA  . PHE A 1 305 ? 6.298   24.678 57.971  1.00 17.32 ? 305 PHE A CA  1 
ATOM   2588 C C   . PHE A 1 305 ? 4.984   25.423 57.870  1.00 17.21 ? 305 PHE A C   1 
ATOM   2589 O O   . PHE A 1 305 ? 4.589   25.837 56.782  1.00 19.31 ? 305 PHE A O   1 
ATOM   2590 C CB  . PHE A 1 305 ? 7.492   25.610 57.739  1.00 20.25 ? 305 PHE A CB  1 
ATOM   2591 C CG  . PHE A 1 305 ? 8.815   24.921 57.914  1.00 20.51 ? 305 PHE A CG  1 
ATOM   2592 C CD1 . PHE A 1 305 ? 9.374   24.781 59.172  1.00 17.71 ? 305 PHE A CD1 1 
ATOM   2593 C CD2 . PHE A 1 305 ? 9.471   24.357 56.821  1.00 21.56 ? 305 PHE A CD2 1 
ATOM   2594 C CE1 . PHE A 1 305 ? 10.568  24.134 59.352  1.00 16.92 ? 305 PHE A CE1 1 
ATOM   2595 C CE2 . PHE A 1 305 ? 10.673  23.699 56.990  1.00 19.93 ? 305 PHE A CE2 1 
ATOM   2596 C CZ  . PHE A 1 305 ? 11.234  23.583 58.254  1.00 18.24 ? 305 PHE A CZ  1 
ATOM   2597 N N   . ARG A 1 306 ? 4.284   25.539 58.992  1.00 14.38 ? 306 ARG A N   1 
ATOM   2598 C CA  . ARG A 1 306 ? 2.956   26.113 58.948  1.00 16.13 ? 306 ARG A CA  1 
ATOM   2599 C C   . ARG A 1 306 ? 3.051   27.607 58.683  1.00 18.87 ? 306 ARG A C   1 
ATOM   2600 O O   . ARG A 1 306 ? 4.046   28.274 59.010  1.00 17.22 ? 306 ARG A O   1 
ATOM   2601 C CB  . ARG A 1 306 ? 2.204   25.860 60.259  1.00 13.28 ? 306 ARG A CB  1 
ATOM   2602 C CG  . ARG A 1 306 ? 2.734   26.664 61.382  1.00 20.55 ? 306 ARG A CG  1 
ATOM   2603 C CD  . ARG A 1 306 ? 1.822   26.638 62.593  1.00 24.78 ? 306 ARG A CD  1 
ATOM   2604 N NE  . ARG A 1 306 ? 2.378   27.579 63.547  1.00 20.70 ? 306 ARG A NE  1 
ATOM   2605 C CZ  . ARG A 1 306 ? 1.722   28.176 64.526  1.00 17.39 ? 306 ARG A CZ  1 
ATOM   2606 N NH1 . ARG A 1 306 ? 0.433   27.920 64.755  1.00 17.47 ? 306 ARG A NH1 1 
ATOM   2607 N NH2 . ARG A 1 306 ? 2.395   29.024 65.293  1.00 17.78 ? 306 ARG A NH2 1 
ATOM   2608 N N   . ASP A 1 307 ? 1.993   28.122 58.090  1.00 13.52 ? 307 ASP A N   1 
ATOM   2609 C CA  . ASP A 1 307 ? 1.806   29.555 57.914  1.00 13.99 ? 307 ASP A CA  1 
ATOM   2610 C C   . ASP A 1 307 ? 1.337   30.095 59.261  1.00 17.46 ? 307 ASP A C   1 
ATOM   2611 O O   . ASP A 1 307 ? 0.168   29.945 59.644  1.00 16.60 ? 307 ASP A O   1 
ATOM   2612 C CB  . ASP A 1 307 ? 0.798   29.806 56.803  1.00 15.30 ? 307 ASP A CB  1 
ATOM   2613 C CG  . ASP A 1 307 ? 0.719   31.253 56.400  1.00 24.45 ? 307 ASP A CG  1 
ATOM   2614 O OD1 . ASP A 1 307 ? 0.567   32.105 57.297  1.00 20.96 ? 307 ASP A OD1 1 
ATOM   2615 O OD2 . ASP A 1 307 ? 0.783   31.533 55.181  1.00 23.43 ? 307 ASP A OD2 1 
ATOM   2616 N N   . LYS A 1 308 ? 2.273   30.686 60.001  1.00 16.13 ? 308 LYS A N   1 
ATOM   2617 C CA  . LYS A 1 308 ? 1.988   31.160 61.350  1.00 19.33 ? 308 LYS A CA  1 
ATOM   2618 C C   . LYS A 1 308 ? 0.904   32.241 61.344  1.00 18.81 ? 308 LYS A C   1 
ATOM   2619 O O   . LYS A 1 308 ? -0.013  32.217 62.175  1.00 17.87 ? 308 LYS A O   1 
ATOM   2620 C CB  . LYS A 1 308 ? 3.296   31.671 61.981  1.00 18.71 ? 308 LYS A CB  1 
ATOM   2621 C CG  . LYS A 1 308 ? 3.123   32.313 63.345  1.00 22.74 ? 308 LYS A CG  1 
ATOM   2622 C CD  . LYS A 1 308 ? 4.447   32.797 63.890  1.00 26.78 ? 308 LYS A CD  1 
ATOM   2623 C CE  . LYS A 1 308 ? 4.215   33.713 65.076  1.00 31.16 ? 308 LYS A CE  1 
ATOM   2624 N NZ  . LYS A 1 308 ? 5.399   34.574 65.334  1.00 42.61 ? 308 LYS A NZ  1 
ATOM   2625 N N   . THR A 1 309 ? 0.968   33.168 60.382  1.00 15.51 ? 309 THR A N   1 
ATOM   2626 C CA  . THR A 1 309 ? 0.017   34.276 60.352  1.00 19.55 ? 309 THR A CA  1 
ATOM   2627 C C   . THR A 1 309 ? -1.424  33.772 60.212  1.00 14.50 ? 309 THR A C   1 
ATOM   2628 O O   . THR A 1 309 ? -2.304  34.156 60.992  1.00 14.32 ? 309 THR A O   1 
ATOM   2629 C CB  . THR A 1 309 ? 0.392   35.240 59.217  1.00 21.36 ? 309 THR A CB  1 
ATOM   2630 O OG1 . THR A 1 309 ? 1.605   35.911 59.569  1.00 22.03 ? 309 THR A OG1 1 
ATOM   2631 C CG2 . THR A 1 309 ? -0.685  36.287 59.013  1.00 25.99 ? 309 THR A CG2 1 
ATOM   2632 N N   . LEU A 1 310 ? -1.684  32.897 59.232  1.00 13.59 ? 310 LEU A N   1 
ATOM   2633 C CA  . LEU A 1 310 ? -3.034  32.370 59.056  1.00 13.32 ? 310 LEU A CA  1 
ATOM   2634 C C   . LEU A 1 310 ? -3.485  31.558 60.266  1.00 13.39 ? 310 LEU A C   1 
ATOM   2635 O O   . LEU A 1 310 ? -4.658  31.610 60.655  1.00 15.73 ? 310 LEU A O   1 
ATOM   2636 C CB  . LEU A 1 310 ? -3.102  31.502 57.799  1.00 13.10 ? 310 LEU A CB  1 
ATOM   2637 C CG  . LEU A 1 310 ? -2.795  32.233 56.490  1.00 18.47 ? 310 LEU A CG  1 
ATOM   2638 C CD1 . LEU A 1 310 ? -2.788  31.253 55.346  1.00 20.32 ? 310 LEU A CD1 1 
ATOM   2639 C CD2 . LEU A 1 310 ? -3.775  33.333 56.201  1.00 17.91 ? 310 LEU A CD2 1 
ATOM   2640 N N   . SER A 1 311 ? -2.572  30.771 60.851  1.00 12.64 ? 311 SER A N   1 
ATOM   2641 C CA  . SER A 1 311 ? -2.934  29.966 62.011  1.00 14.79 ? 311 SER A CA  1 
ATOM   2642 C C   . SER A 1 311 ? -3.271  30.854 63.205  1.00 13.02 ? 311 SER A C   1 
ATOM   2643 O O   . SER A 1 311 ? -4.183  30.547 63.983  1.00 15.84 ? 311 SER A O   1 
ATOM   2644 C CB  . SER A 1 311 ? -1.803  28.997 62.356  1.00 12.66 ? 311 SER A CB  1 
ATOM   2645 O OG  . SER A 1 311 ? -1.368  28.261 61.207  1.00 13.82 ? 311 SER A OG  1 
ATOM   2646 N N   . ASP A 1 312 ? -2.556  31.956 63.355  1.00 13.16 ? 312 ASP A N   1 
ATOM   2647 C CA  . ASP A 1 312 ? -2.785  32.844 64.483  1.00 13.61 ? 312 ASP A CA  1 
ATOM   2648 C C   . ASP A 1 312 ? -4.005  33.737 64.263  1.00 15.67 ? 312 ASP A C   1 
ATOM   2649 O O   . ASP A 1 312 ? -4.611  34.191 65.237  1.00 15.19 ? 312 ASP A O   1 
ATOM   2650 C CB  . ASP A 1 312 ? -1.547  33.702 64.753  1.00 16.16 ? 312 ASP A CB  1 
ATOM   2651 C CG  . ASP A 1 312 ? -0.426  32.937 65.456  1.00 18.89 ? 312 ASP A CG  1 
ATOM   2652 O OD1 . ASP A 1 312 ? -0.672  31.850 66.025  1.00 19.99 ? 312 ASP A OD1 1 
ATOM   2653 O OD2 . ASP A 1 312 ? 0.719   33.452 65.440  1.00 21.77 ? 312 ASP A OD2 1 
ATOM   2654 N N   . LEU A 1 313 ? -4.371  34.030 63.009  1.00 13.77 ? 313 LEU A N   1 
ATOM   2655 C CA  . LEU A 1 313 ? -5.635  34.732 62.766  1.00 14.30 ? 313 LEU A CA  1 
ATOM   2656 C C   . LEU A 1 313 ? -6.810  33.969 63.380  1.00 14.83 ? 313 LEU A C   1 
ATOM   2657 O O   . LEU A 1 313 ? -7.660  34.541 64.074  1.00 14.04 ? 313 LEU A O   1 
ATOM   2658 C CB  . LEU A 1 313 ? -5.854  34.895 61.265  1.00 17.13 ? 313 LEU A CB  1 
ATOM   2659 C CG  . LEU A 1 313 ? -5.122  36.027 60.569  1.00 19.24 ? 313 LEU A CG  1 
ATOM   2660 C CD1 . LEU A 1 313 ? -5.347  35.912 59.065  1.00 15.74 ? 313 LEU A CD1 1 
ATOM   2661 C CD2 . LEU A 1 313 ? -5.533  37.390 61.118  1.00 16.83 ? 313 LEU A CD2 1 
ATOM   2662 N N   . ILE A 1 314 ? -6.868  32.664 63.120  1.00 18.07 ? 314 ILE A N   1 
ATOM   2663 C CA  . ILE A 1 314 ? -7.930  31.848 63.683  1.00 14.03 ? 314 ILE A CA  1 
ATOM   2664 C C   . ILE A 1 314 ? -7.744  31.689 65.181  1.00 15.85 ? 314 ILE A C   1 
ATOM   2665 O O   . ILE A 1 314 ? -8.708  31.809 65.953  1.00 13.85 ? 314 ILE A O   1 
ATOM   2666 C CB  . ILE A 1 314 ? -7.973  30.484 62.981  1.00 13.93 ? 314 ILE A CB  1 
ATOM   2667 C CG1 . ILE A 1 314 ? -8.288  30.692 61.500  1.00 14.93 ? 314 ILE A CG1 1 
ATOM   2668 C CG2 . ILE A 1 314 ? -9.023  29.584 63.632  1.00 12.79 ? 314 ILE A CG2 1 
ATOM   2669 C CD1 . ILE A 1 314 ? -8.272  29.403 60.717  1.00 17.83 ? 314 ILE A CD1 1 
ATOM   2670 N N   . GLY A 1 315 ? -6.502  31.438 65.618  1.00 14.97 ? 315 GLY A N   1 
ATOM   2671 C CA  . GLY A 1 315 ? -6.267  31.200 67.036  1.00 14.05 ? 315 GLY A CA  1 
ATOM   2672 C C   . GLY A 1 315 ? -6.486  32.413 67.932  1.00 14.77 ? 315 GLY A C   1 
ATOM   2673 O O   . GLY A 1 315 ? -6.865  32.255 69.104  1.00 14.39 ? 315 GLY A O   1 
ATOM   2674 N N   . PHE A 1 316 ? -6.212  33.619 67.429  1.00 14.32 ? 316 PHE A N   1 
ATOM   2675 C CA  . PHE A 1 316 ? -6.131  34.794 68.298  1.00 16.52 ? 316 PHE A CA  1 
ATOM   2676 C C   . PHE A 1 316 ? -6.946  36.009 67.850  1.00 18.45 ? 316 PHE A C   1 
ATOM   2677 O O   . PHE A 1 316 ? -7.357  36.813 68.699  1.00 16.15 ? 316 PHE A O   1 
ATOM   2678 C CB  . PHE A 1 316 ? -4.658  35.212 68.471  1.00 16.60 ? 316 PHE A CB  1 
ATOM   2679 C CG  . PHE A 1 316 ? -3.846  34.190 69.201  1.00 17.57 ? 316 PHE A CG  1 
ATOM   2680 C CD1 . PHE A 1 316 ? -4.040  33.985 70.563  1.00 17.37 ? 316 PHE A CD1 1 
ATOM   2681 C CD2 . PHE A 1 316 ? -2.942  33.395 68.533  1.00 19.86 ? 316 PHE A CD2 1 
ATOM   2682 C CE1 . PHE A 1 316 ? -3.321  33.018 71.234  1.00 17.64 ? 316 PHE A CE1 1 
ATOM   2683 C CE2 . PHE A 1 316 ? -2.215  32.428 69.205  1.00 20.10 ? 316 PHE A CE2 1 
ATOM   2684 C CZ  . PHE A 1 316 ? -2.409  32.240 70.552  1.00 20.38 ? 316 PHE A CZ  1 
ATOM   2685 N N   . SER A 1 317 ? -7.169  36.185 66.546  1.00 15.48 ? 317 SER A N   1 
ATOM   2686 C CA  . SER A 1 317 ? -7.824  37.398 66.051  1.00 15.63 ? 317 SER A CA  1 
ATOM   2687 C C   . SER A 1 317 ? -9.339  37.237 65.879  1.00 16.24 ? 317 SER A C   1 
ATOM   2688 O O   . SER A 1 317 ? -10.121 38.017 66.437  1.00 16.77 ? 317 SER A O   1 
ATOM   2689 C CB  . SER A 1 317 ? -7.199  37.830 64.715  1.00 20.71 ? 317 SER A CB  1 
ATOM   2690 O OG  . SER A 1 317 ? -5.796  38.013 64.864  1.00 20.47 ? 317 SER A OG  1 
ATOM   2691 N N   . TYR A 1 318 ? -9.761  36.244 65.094  1.00 15.02 ? 318 TYR A N   1 
ATOM   2692 C CA  . TYR A 1 318 ? -11.117 36.253 64.549  1.00 15.13 ? 318 TYR A CA  1 
ATOM   2693 C C   . TYR A 1 318 ? -12.220 36.077 65.596  1.00 15.83 ? 318 TYR A C   1 
ATOM   2694 O O   . TYR A 1 318 ? -13.383 36.401 65.290  1.00 17.27 ? 318 TYR A O   1 
ATOM   2695 C CB  . TYR A 1 318 ? -11.254 35.173 63.490  1.00 14.89 ? 318 TYR A CB  1 
ATOM   2696 C CG  . TYR A 1 318 ? -10.546 35.477 62.185  1.00 14.57 ? 318 TYR A CG  1 
ATOM   2697 C CD1 . TYR A 1 318 ? -10.198 36.776 61.827  1.00 15.25 ? 318 TYR A CD1 1 
ATOM   2698 C CD2 . TYR A 1 318 ? -10.243 34.442 61.300  1.00 14.15 ? 318 TYR A CD2 1 
ATOM   2699 C CE1 . TYR A 1 318 ? -9.557  37.037 60.608  1.00 15.11 ? 318 TYR A CE1 1 
ATOM   2700 C CE2 . TYR A 1 318 ? -9.600  34.696 60.105  1.00 18.88 ? 318 TYR A CE2 1 
ATOM   2701 C CZ  . TYR A 1 318 ? -9.264  35.986 59.765  1.00 19.06 ? 318 TYR A CZ  1 
ATOM   2702 O OH  . TYR A 1 318 ? -8.634  36.211 58.568  1.00 21.84 ? 318 TYR A OH  1 
ATOM   2703 N N   . HIS A 1 319 ? -11.915 35.577 66.809  1.00 15.40 ? 319 HIS A N   1 
ATOM   2704 C CA  . HIS A 1 319 ? -12.949 35.524 67.851  1.00 15.86 ? 319 HIS A CA  1 
ATOM   2705 C C   . HIS A 1 319 ? -13.581 36.892 68.096  1.00 19.92 ? 319 HIS A C   1 
ATOM   2706 O O   . HIS A 1 319 ? -14.751 36.971 68.488  1.00 20.35 ? 319 HIS A O   1 
ATOM   2707 C CB  . HIS A 1 319 ? -12.368 35.031 69.179  1.00 15.96 ? 319 HIS A CB  1 
ATOM   2708 C CG  . HIS A 1 319 ? -11.495 36.046 69.851  1.00 17.86 ? 319 HIS A CG  1 
ATOM   2709 N ND1 . HIS A 1 319 ? -11.926 36.838 70.896  1.00 25.06 ? 319 HIS A ND1 1 
ATOM   2710 C CD2 . HIS A 1 319 ? -10.217 36.418 69.602  1.00 16.31 ? 319 HIS A CD2 1 
ATOM   2711 C CE1 . HIS A 1 319 ? -10.955 37.659 71.260  1.00 17.60 ? 319 HIS A CE1 1 
ATOM   2712 N NE2 . HIS A 1 319 ? -9.906  37.424 70.490  1.00 25.59 ? 319 HIS A NE2 1 
ATOM   2713 N N   . ALA A 1 320 ? -12.823 37.968 67.907  1.00 16.82 ? 320 ALA A N   1 
ATOM   2714 C CA  . ALA A 1 320 ? -13.312 39.314 68.181  1.00 21.40 ? 320 ALA A CA  1 
ATOM   2715 C C   . ALA A 1 320 ? -14.025 39.940 66.995  1.00 20.40 ? 320 ALA A C   1 
ATOM   2716 O O   . ALA A 1 320 ? -14.474 41.091 67.096  1.00 21.66 ? 320 ALA A O   1 
ATOM   2717 C CB  . ALA A 1 320 ? -12.165 40.226 68.614  1.00 18.04 ? 320 ALA A CB  1 
ATOM   2718 N N   . TRP A 1 321 ? -14.106 39.232 65.876  1.00 17.29 ? 321 TRP A N   1 
ATOM   2719 C CA  . TRP A 1 321 ? -14.670 39.771 64.655  1.00 19.90 ? 321 TRP A CA  1 
ATOM   2720 C C   . TRP A 1 321 ? -16.040 39.169 64.406  1.00 23.04 ? 321 TRP A C   1 
ATOM   2721 O O   . TRP A 1 321 ? -16.381 38.098 64.917  1.00 24.57 ? 321 TRP A O   1 
ATOM   2722 C CB  . TRP A 1 321 ? -13.797 39.455 63.433  1.00 16.95 ? 321 TRP A CB  1 
ATOM   2723 C CG  . TRP A 1 321 ? -12.363 39.900 63.468  1.00 19.17 ? 321 TRP A CG  1 
ATOM   2724 C CD1 . TRP A 1 321 ? -11.551 40.049 64.557  1.00 24.69 ? 321 TRP A CD1 1 
ATOM   2725 C CD2 . TRP A 1 321 ? -11.582 40.253 62.328  1.00 19.60 ? 321 TRP A CD2 1 
ATOM   2726 N NE1 . TRP A 1 321 ? -10.302 40.474 64.155  1.00 22.74 ? 321 TRP A NE1 1 
ATOM   2727 C CE2 . TRP A 1 321 ? -10.297 40.599 62.789  1.00 19.73 ? 321 TRP A CE2 1 
ATOM   2728 C CE3 . TRP A 1 321 ? -11.851 40.305 60.954  1.00 19.12 ? 321 TRP A CE3 1 
ATOM   2729 C CZ2 . TRP A 1 321 ? -9.278  41.000 61.924  1.00 23.66 ? 321 TRP A CZ2 1 
ATOM   2730 C CZ3 . TRP A 1 321 ? -10.838 40.700 60.091  1.00 27.16 ? 321 TRP A CZ3 1 
ATOM   2731 C CH2 . TRP A 1 321 ? -9.570  41.041 60.582  1.00 19.49 ? 321 TRP A CH2 1 
ATOM   2732 N N   . ASN A 1 322 ? -16.803 39.856 63.568  1.00 21.55 ? 322 ASN A N   1 
ATOM   2733 C CA  . ASN A 1 322 ? -17.985 39.258 62.972  1.00 24.08 ? 322 ASN A CA  1 
ATOM   2734 C C   . ASN A 1 322 ? -17.565 38.166 61.981  1.00 23.09 ? 322 ASN A C   1 
ATOM   2735 O O   . ASN A 1 322 ? -16.497 38.234 61.365  1.00 23.51 ? 322 ASN A O   1 
ATOM   2736 C CB  . ASN A 1 322 ? -18.803 40.357 62.296  1.00 36.69 ? 322 ASN A CB  1 
ATOM   2737 C CG  . ASN A 1 322 ? -19.654 39.849 61.180  1.00 51.34 ? 322 ASN A CG  1 
ATOM   2738 O OD1 . ASN A 1 322 ? -19.205 39.762 60.040  1.00 52.50 ? 322 ASN A OD1 1 
ATOM   2739 N ND2 . ASN A 1 322 ? -20.904 39.516 61.493  1.00 52.77 ? 322 ASN A ND2 1 
ATOM   2740 N N   . ALA A 1 323 ? -18.407 37.137 61.830  1.00 19.61 ? 323 ALA A N   1 
ATOM   2741 C CA  . ALA A 1 323 ? -17.983 35.966 61.055  1.00 17.64 ? 323 ALA A CA  1 
ATOM   2742 C C   . ALA A 1 323 ? -17.693 36.314 59.595  1.00 18.14 ? 323 ALA A C   1 
ATOM   2743 O O   . ALA A 1 323 ? -16.721 35.810 59.015  1.00 23.27 ? 323 ALA A O   1 
ATOM   2744 C CB  . ALA A 1 323 ? -19.035 34.855 61.154  1.00 20.99 ? 323 ALA A CB  1 
ATOM   2745 N N   . GLU A 1 324 ? -18.514 37.159 58.969  1.00 24.62 ? 324 GLU A N   1 
ATOM   2746 C CA  . GLU A 1 324 ? -18.243 37.424 57.557  1.00 34.12 ? 324 GLU A CA  1 
ATOM   2747 C C   . GLU A 1 324 ? -17.054 38.369 57.365  1.00 29.95 ? 324 GLU A C   1 
ATOM   2748 O O   . GLU A 1 324 ? -16.286 38.194 56.410  1.00 29.20 ? 324 GLU A O   1 
ATOM   2749 C CB  . GLU A 1 324 ? -19.513 37.931 56.848  1.00 45.25 ? 324 GLU A CB  1 
ATOM   2750 C CG  . GLU A 1 324 ? -19.927 39.360 57.118  1.00 50.86 ? 324 GLU A CG  1 
ATOM   2751 C CD  . GLU A 1 324 ? -19.507 40.298 55.996  1.00 64.23 ? 324 GLU A CD  1 
ATOM   2752 O OE1 . GLU A 1 324 ? -18.613 39.907 55.215  1.00 67.55 ? 324 GLU A OE1 1 
ATOM   2753 O OE2 . GLU A 1 324 ? -20.081 41.408 55.879  1.00 55.22 ? 324 GLU A OE2 1 
ATOM   2754 N N   . ASP A 1 325 ? -16.863 39.348 58.260  1.00 30.95 ? 325 ASP A N   1 
ATOM   2755 C CA  . ASP A 1 325 ? -15.620 40.124 58.265  1.00 28.69 ? 325 ASP A CA  1 
ATOM   2756 C C   . ASP A 1 325 ? -14.403 39.202 58.299  1.00 26.28 ? 325 ASP A C   1 
ATOM   2757 O O   . ASP A 1 325 ? -13.439 39.379 57.541  1.00 22.36 ? 325 ASP A O   1 
ATOM   2758 C CB  . ASP A 1 325 ? -15.577 41.067 59.473  1.00 35.17 ? 325 ASP A CB  1 
ATOM   2759 C CG  . ASP A 1 325 ? -16.568 42.216 59.376  1.00 43.50 ? 325 ASP A CG  1 
ATOM   2760 O OD1 . ASP A 1 325 ? -17.452 42.181 58.502  1.00 44.21 ? 325 ASP A OD1 1 
ATOM   2761 O OD2 . ASP A 1 325 ? -16.470 43.146 60.206  1.00 43.04 ? 325 ASP A OD2 1 
ATOM   2762 N N   . ALA A 1 326 ? -14.436 38.205 59.181  1.00 19.74 ? 326 ALA A N   1 
ATOM   2763 C CA  . ALA A 1 326 ? -13.282 37.338 59.375  1.00 20.09 ? 326 ALA A CA  1 
ATOM   2764 C C   . ALA A 1 326 ? -13.037 36.459 58.152  1.00 21.48 ? 326 ALA A C   1 
ATOM   2765 O O   . ALA A 1 326 ? -11.896 36.325 57.685  1.00 20.57 ? 326 ALA A O   1 
ATOM   2766 C CB  . ALA A 1 326 ? -13.494 36.472 60.618  1.00 16.42 ? 326 ALA A CB  1 
ATOM   2767 N N   . VAL A 1 327 ? -14.098 35.839 57.625  1.00 17.92 ? 327 VAL A N   1 
ATOM   2768 C CA  . VAL A 1 327 ? -13.939 34.961 56.465  1.00 17.31 ? 327 VAL A CA  1 
ATOM   2769 C C   . VAL A 1 327 ? -13.482 35.754 55.242  1.00 20.48 ? 327 VAL A C   1 
ATOM   2770 O O   . VAL A 1 327 ? -12.637 35.287 54.468  1.00 18.41 ? 327 VAL A O   1 
ATOM   2771 C CB  . VAL A 1 327 ? -15.246 34.188 56.187  1.00 22.53 ? 327 VAL A CB  1 
ATOM   2772 C CG1 . VAL A 1 327 ? -15.125 33.370 54.895  1.00 23.58 ? 327 VAL A CG1 1 
ATOM   2773 C CG2 . VAL A 1 327 ? -15.567 33.246 57.339  1.00 18.94 ? 327 VAL A CG2 1 
ATOM   2774 N N   . ARG A 1 328 ? -14.057 36.942 55.012  1.00 23.00 ? 328 ARG A N   1 
ATOM   2775 C CA  . ARG A 1 328 ? -13.607 37.747 53.876  1.00 26.08 ? 328 ARG A CA  1 
ATOM   2776 C C   . ARG A 1 328 ? -12.125 38.080 53.995  1.00 29.03 ? 328 ARG A C   1 
ATOM   2777 O O   . ARG A 1 328 ? -11.393 38.092 52.997  1.00 22.52 ? 328 ARG A O   1 
ATOM   2778 C CB  . ARG A 1 328 ? -14.416 39.042 53.787  1.00 33.09 ? 328 ARG A CB  1 
ATOM   2779 C CG  . ARG A 1 328 ? -15.723 38.946 53.038  1.00 42.70 ? 328 ARG A CG  1 
ATOM   2780 C CD  . ARG A 1 328 ? -16.257 40.367 52.787  1.00 43.18 ? 328 ARG A CD  1 
ATOM   2781 N NE  . ARG A 1 328 ? -17.580 40.380 52.177  1.00 56.30 ? 328 ARG A NE  1 
ATOM   2782 C CZ  . ARG A 1 328 ? -18.277 41.488 51.941  1.00 61.37 ? 328 ARG A CZ  1 
ATOM   2783 N NH1 . ARG A 1 328 ? -17.769 42.669 52.267  1.00 56.68 ? 328 ARG A NH1 1 
ATOM   2784 N NH2 . ARG A 1 328 ? -19.477 41.418 51.375  1.00 64.21 ? 328 ARG A NH2 1 
ATOM   2785 N N   . ASP A 1 329 ? -11.675 38.364 55.220  1.00 24.26 ? 329 ASP A N   1 
ATOM   2786 C CA  . ASP A 1 329 ? -10.281 38.690 55.473  1.00 24.95 ? 329 ASP A CA  1 
ATOM   2787 C C   . ASP A 1 329 ? -9.380  37.495 55.177  1.00 21.90 ? 329 ASP A C   1 
ATOM   2788 O O   . ASP A 1 329 ? -8.342  37.636 54.522  1.00 23.79 ? 329 ASP A O   1 
ATOM   2789 C CB  . ASP A 1 329 ? -10.148 39.150 56.925  1.00 22.93 ? 329 ASP A CB  1 
ATOM   2790 C CG  . ASP A 1 329 ? -8.734  39.510 57.302  1.00 20.80 ? 329 ASP A CG  1 
ATOM   2791 O OD1 . ASP A 1 329 ? -8.007  38.608 57.757  1.00 19.45 ? 329 ASP A OD1 1 
ATOM   2792 O OD2 . ASP A 1 329 ? -8.363  40.706 57.153  1.00 25.50 ? 329 ASP A OD2 1 
ATOM   2793 N N   . PHE A 1 330 ? -9.775  36.305 55.647  1.00 18.23 ? 330 PHE A N   1 
ATOM   2794 C CA  . PHE A 1 330 ? -8.999  35.084 55.430  1.00 18.69 ? 330 PHE A CA  1 
ATOM   2795 C C   . PHE A 1 330 ? -8.909  34.748 53.951  1.00 22.05 ? 330 PHE A C   1 
ATOM   2796 O O   . PHE A 1 330 ? -7.826  34.455 53.434  1.00 20.59 ? 330 PHE A O   1 
ATOM   2797 C CB  . PHE A 1 330 ? -9.642  33.936 56.221  1.00 14.47 ? 330 PHE A CB  1 
ATOM   2798 C CG  . PHE A 1 330 ? -8.745  32.726 56.439  1.00 17.70 ? 330 PHE A CG  1 
ATOM   2799 C CD1 . PHE A 1 330 ? -7.791  32.720 57.450  1.00 19.84 ? 330 PHE A CD1 1 
ATOM   2800 C CD2 . PHE A 1 330 ? -8.891  31.592 55.663  1.00 18.59 ? 330 PHE A CD2 1 
ATOM   2801 C CE1 . PHE A 1 330 ? -6.973  31.607 57.671  1.00 20.09 ? 330 PHE A CE1 1 
ATOM   2802 C CE2 . PHE A 1 330 ? -8.080  30.458 55.880  1.00 17.66 ? 330 PHE A CE2 1 
ATOM   2803 C CZ  . PHE A 1 330 ? -7.122  30.472 56.883  1.00 19.67 ? 330 PHE A CZ  1 
ATOM   2804 N N   . ILE A 1 331 ? -10.049 34.766 53.254  1.00 23.20 ? 331 ILE A N   1 
ATOM   2805 C CA  . ILE A 1 331 ? -10.042 34.489 51.818  1.00 20.74 ? 331 ILE A CA  1 
ATOM   2806 C C   . ILE A 1 331 ? -9.173  35.510 51.093  1.00 24.33 ? 331 ILE A C   1 
ATOM   2807 O O   . ILE A 1 331 ? -8.386  35.160 50.199  1.00 21.66 ? 331 ILE A O   1 
ATOM   2808 C CB  . ILE A 1 331 ? -11.483 34.467 51.264  1.00 24.43 ? 331 ILE A CB  1 
ATOM   2809 C CG1 . ILE A 1 331 ? -12.285 33.305 51.866  1.00 26.53 ? 331 ILE A CG1 1 
ATOM   2810 C CG2 . ILE A 1 331 ? -11.483 34.456 49.726  1.00 28.29 ? 331 ILE A CG2 1 
ATOM   2811 C CD1 . ILE A 1 331 ? -11.789 31.894 51.496  1.00 20.45 ? 331 ILE A CD1 1 
ATOM   2812 N N   . GLY A 1 332 ? -9.294  36.785 51.479  1.00 21.65 ? 332 GLY A N   1 
ATOM   2813 C CA  . GLY A 1 332 ? -8.472  37.821 50.876  1.00 25.25 ? 332 GLY A CA  1 
ATOM   2814 C C   . GLY A 1 332 ? -6.986  37.556 51.027  1.00 20.54 ? 332 GLY A C   1 
ATOM   2815 O O   . GLY A 1 332 ? -6.218  37.723 50.082  1.00 24.35 ? 332 GLY A O   1 
ATOM   2816 N N   . ARG A 1 333 ? -6.567  37.130 52.215  1.00 17.75 ? 333 ARG A N   1 
ATOM   2817 C CA  . ARG A 1 333 ? -5.167  36.789 52.437  1.00 20.55 ? 333 ARG A CA  1 
ATOM   2818 C C   . ARG A 1 333 ? -4.739  35.607 51.577  1.00 19.40 ? 333 ARG A C   1 
ATOM   2819 O O   . ARG A 1 333 ? -3.641  35.609 51.005  1.00 21.09 ? 333 ARG A O   1 
ATOM   2820 C CB  . ARG A 1 333 ? -4.949  36.491 53.918  1.00 21.30 ? 333 ARG A CB  1 
ATOM   2821 C CG  . ARG A 1 333 ? -5.306  37.688 54.773  1.00 32.12 ? 333 ARG A CG  1 
ATOM   2822 C CD  . ARG A 1 333 ? -4.793  37.571 56.197  1.00 43.29 ? 333 ARG A CD  1 
ATOM   2823 N NE  . ARG A 1 333 ? -3.468  38.178 56.349  1.00 39.70 ? 333 ARG A NE  1 
ATOM   2824 C CZ  . ARG A 1 333 ? -2.332  37.641 55.910  1.00 49.05 ? 333 ARG A CZ  1 
ATOM   2825 N NH1 . ARG A 1 333 ? -2.318  36.453 55.314  1.00 55.66 ? 333 ARG A NH1 1 
ATOM   2826 N NH2 . ARG A 1 333 ? -1.193  38.296 56.090  1.00 41.36 ? 333 ARG A NH2 1 
ATOM   2827 N N   . LEU A 1 334 ? -5.593  34.589 51.471  1.00 17.81 ? 334 LEU A N   1 
ATOM   2828 C CA  . LEU A 1 334 ? -5.272  33.449 50.616  1.00 15.98 ? 334 LEU A CA  1 
ATOM   2829 C C   . LEU A 1 334 ? -5.148  33.875 49.164  1.00 21.33 ? 334 LEU A C   1 
ATOM   2830 O O   . LEU A 1 334 ? -4.309  33.351 48.415  1.00 18.53 ? 334 LEU A O   1 
ATOM   2831 C CB  . LEU A 1 334 ? -6.343  32.370 50.762  1.00 17.93 ? 334 LEU A CB  1 
ATOM   2832 C CG  . LEU A 1 334 ? -6.393  31.639 52.102  1.00 17.52 ? 334 LEU A CG  1 
ATOM   2833 C CD1 . LEU A 1 334 ? -7.531  30.613 52.072  1.00 20.00 ? 334 LEU A CD1 1 
ATOM   2834 C CD2 . LEU A 1 334 ? -5.035  30.965 52.417  1.00 17.49 ? 334 LEU A CD2 1 
ATOM   2835 N N   . LYS A 1 335 ? -5.986  34.817 48.740  1.00 20.60 ? 335 LYS A N   1 
ATOM   2836 C CA  . LYS A 1 335 ? -5.899  35.290 47.370  1.00 19.25 ? 335 LYS A CA  1 
ATOM   2837 C C   . LYS A 1 335 ? -4.582  36.011 47.143  1.00 20.50 ? 335 LYS A C   1 
ATOM   2838 O O   . LYS A 1 335 ? -3.949  35.857 46.087  1.00 20.69 ? 335 LYS A O   1 
ATOM   2839 C CB  . LYS A 1 335 ? -7.084  36.202 47.049  1.00 20.45 ? 335 LYS A CB  1 
ATOM   2840 C CG  . LYS A 1 335 ? -7.164  36.587 45.591  1.00 28.90 ? 335 LYS A CG  1 
ATOM   2841 C CD  . LYS A 1 335 ? -8.450  37.351 45.304  1.00 33.68 ? 335 LYS A CD  1 
ATOM   2842 C CE  . LYS A 1 335 ? -8.469  37.927 43.893  1.00 47.46 ? 335 LYS A CE  1 
ATOM   2843 N NZ  . LYS A 1 335 ? -8.180  39.388 43.859  1.00 53.54 ? 335 LYS A NZ  1 
ATOM   2844 N N   . LYS A 1 336 ? -4.140  36.785 48.133  1.00 19.92 ? 336 LYS A N   1 
ATOM   2845 C CA  . LYS A 1 336 ? -2.871  37.483 47.995  1.00 20.78 ? 336 LYS A CA  1 
ATOM   2846 C C   . LYS A 1 336 ? -1.715  36.492 47.885  1.00 22.18 ? 336 LYS A C   1 
ATOM   2847 O O   . LYS A 1 336 ? -0.783  36.709 47.104  1.00 27.02 ? 336 LYS A O   1 
ATOM   2848 C CB  . LYS A 1 336 ? -2.661  38.442 49.173  1.00 37.64 ? 336 LYS A CB  1 
ATOM   2849 C CG  . LYS A 1 336 ? -1.231  38.963 49.296  1.00 44.32 ? 336 LYS A CG  1 
ATOM   2850 C CD  . LYS A 1 336 ? -1.119  40.151 50.254  1.00 53.48 ? 336 LYS A CD  1 
ATOM   2851 C CE  . LYS A 1 336 ? 0.253   40.833 50.158  1.00 60.68 ? 336 LYS A CE  1 
ATOM   2852 N NZ  . LYS A 1 336 ? 1.241   40.302 51.159  1.00 62.90 ? 336 LYS A NZ  1 
ATOM   2853 N N   . ILE A 1 337 ? -1.764  35.393 48.650  1.00 20.36 ? 337 ILE A N   1 
ATOM   2854 C CA  . ILE A 1 337 ? -0.756  34.340 48.498  1.00 18.64 ? 337 ILE A CA  1 
ATOM   2855 C C   . ILE A 1 337 ? -0.828  33.734 47.097  1.00 18.59 ? 337 ILE A C   1 
ATOM   2856 O O   . ILE A 1 337 ? 0.188   33.597 46.414  1.00 23.17 ? 337 ILE A O   1 
ATOM   2857 C CB  . ILE A 1 337 ? -0.935  33.255 49.575  1.00 26.38 ? 337 ILE A CB  1 
ATOM   2858 C CG1 . ILE A 1 337 ? -0.690  33.816 50.983  1.00 22.18 ? 337 ILE A CG1 1 
ATOM   2859 C CG2 . ILE A 1 337 ? -0.028  32.059 49.267  1.00 19.02 ? 337 ILE A CG2 1 
ATOM   2860 C CD1 . ILE A 1 337 ? -1.129  32.843 52.128  1.00 21.66 ? 337 ILE A CD1 1 
ATOM   2861 N N   . HIS A 1 338 ? -2.046  33.370 46.654  1.00 20.30 ? 338 HIS A N   1 
ATOM   2862 C CA  . HIS A 1 338 ? -2.249  32.780 45.327  1.00 22.66 ? 338 HIS A CA  1 
ATOM   2863 C C   . HIS A 1 338 ? -1.663  33.663 44.233  1.00 25.14 ? 338 HIS A C   1 
ATOM   2864 O O   . HIS A 1 338 ? -1.048  33.169 43.275  1.00 26.81 ? 338 HIS A O   1 
ATOM   2865 C CB  . HIS A 1 338 ? -3.753  32.547 45.097  1.00 21.66 ? 338 HIS A CB  1 
ATOM   2866 C CG  . HIS A 1 338 ? -4.106  32.042 43.721  1.00 25.50 ? 338 HIS A CG  1 
ATOM   2867 N ND1 . HIS A 1 338 ? -4.840  32.782 42.819  1.00 27.89 ? 338 HIS A ND1 1 
ATOM   2868 C CD2 . HIS A 1 338 ? -3.874  30.849 43.120  1.00 20.12 ? 338 HIS A CD2 1 
ATOM   2869 C CE1 . HIS A 1 338 ? -5.019  32.080 41.711  1.00 27.92 ? 338 HIS A CE1 1 
ATOM   2870 N NE2 . HIS A 1 338 ? -4.435  30.903 41.867  1.00 25.96 ? 338 HIS A NE2 1 
ATOM   2871 N N   . GLU A 1 339 ? -1.830  34.974 44.359  1.00 24.27 ? 339 GLU A N   1 
ATOM   2872 C CA  . GLU A 1 339 ? -1.358  35.888 43.334  1.00 24.56 ? 339 GLU A CA  1 
ATOM   2873 C C   . GLU A 1 339 ? 0.099   36.284 43.507  1.00 28.26 ? 339 GLU A C   1 
ATOM   2874 O O   . GLU A 1 339 ? 0.659   36.925 42.615  1.00 30.55 ? 339 GLU A O   1 
ATOM   2875 C CB  . GLU A 1 339 ? -2.242  37.140 43.317  1.00 25.79 ? 339 GLU A CB  1 
ATOM   2876 C CG  . GLU A 1 339 ? -3.680  36.825 42.979  1.00 34.29 ? 339 GLU A CG  1 
ATOM   2877 C CD  . GLU A 1 339 ? -4.572  38.037 43.073  1.00 42.88 ? 339 GLU A CD  1 
ATOM   2878 O OE1 . GLU A 1 339 ? -4.252  38.940 43.872  1.00 51.03 ? 339 GLU A OE1 1 
ATOM   2879 O OE2 . GLU A 1 339 ? -5.580  38.090 42.342  1.00 51.18 ? 339 GLU A OE2 1 
ATOM   2880 N N   . SER A 1 340 ? 0.730   35.912 44.609  1.00 30.23 ? 340 SER A N   1 
ATOM   2881 C CA  . SER A 1 340 ? 2.086   36.363 44.884  1.00 27.03 ? 340 SER A CA  1 
ATOM   2882 C C   . SER A 1 340 ? 3.164   35.428 44.349  1.00 32.36 ? 340 SER A C   1 
ATOM   2883 O O   . SER A 1 340 ? 4.333   35.827 44.306  1.00 38.61 ? 340 SER A O   1 
ATOM   2884 C CB  . SER A 1 340 ? 2.284   36.533 46.387  1.00 25.26 ? 340 SER A CB  1 
ATOM   2885 O OG  . SER A 1 340 ? 2.364   35.262 46.994  1.00 28.70 ? 340 SER A OG  1 
ATOM   2886 N N   . VAL A 1 341 ? 2.822   34.197 43.964  1.00 27.76 ? 341 VAL A N   1 
ATOM   2887 C CA  . VAL A 1 341 ? 3.801   33.274 43.407  1.00 29.05 ? 341 VAL A CA  1 
ATOM   2888 C C   . VAL A 1 341 ? 3.249   32.643 42.136  1.00 30.62 ? 341 VAL A C   1 
ATOM   2889 O O   . VAL A 1 341 ? 2.039   32.586 41.912  1.00 27.16 ? 341 VAL A O   1 
ATOM   2890 C CB  . VAL A 1 341 ? 4.208   32.173 44.408  1.00 26.28 ? 341 VAL A CB  1 
ATOM   2891 C CG1 . VAL A 1 341 ? 4.872   32.790 45.637  1.00 29.27 ? 341 VAL A CG1 1 
ATOM   2892 C CG2 . VAL A 1 341 ? 3.010   31.354 44.797  1.00 30.74 ? 341 VAL A CG2 1 
ATOM   2893 N N   . ASP A 1 342 ? 4.167   32.148 41.307  1.00 30.90 ? 342 ASP A N   1 
ATOM   2894 C CA  . ASP A 1 342 ? 3.800   31.522 40.042  1.00 26.73 ? 342 ASP A CA  1 
ATOM   2895 C C   . ASP A 1 342 ? 3.701   29.996 40.119  1.00 35.26 ? 342 ASP A C   1 
ATOM   2896 O O   . ASP A 1 342 ? 3.199   29.377 39.176  1.00 46.69 ? 342 ASP A O   1 
ATOM   2897 C CB  . ASP A 1 342 ? 4.799   31.938 38.951  1.00 30.56 ? 342 ASP A CB  1 
ATOM   2898 C CG  . ASP A 1 342 ? 4.526   33.345 38.419  1.00 42.36 ? 342 ASP A CG  1 
ATOM   2899 O OD1 . ASP A 1 342 ? 3.448   33.902 38.722  1.00 48.37 ? 342 ASP A OD1 1 
ATOM   2900 O OD2 . ASP A 1 342 ? 5.389   33.905 37.715  1.00 45.95 ? 342 ASP A OD2 1 
ATOM   2901 N N   . PHE A 1 343 ? 4.144   29.376 41.207  1.00 23.25 ? 343 PHE A N   1 
ATOM   2902 C CA  . PHE A 1 343 ? 3.972   27.944 41.404  1.00 22.59 ? 343 PHE A CA  1 
ATOM   2903 C C   . PHE A 1 343 ? 2.736   27.709 42.266  1.00 22.57 ? 343 PHE A C   1 
ATOM   2904 O O   . PHE A 1 343 ? 2.012   28.643 42.615  1.00 22.89 ? 343 PHE A O   1 
ATOM   2905 C CB  . PHE A 1 343 ? 5.232   27.322 42.024  1.00 28.37 ? 343 PHE A CB  1 
ATOM   2906 C CG  . PHE A 1 343 ? 5.562   27.841 43.399  1.00 27.58 ? 343 PHE A CG  1 
ATOM   2907 C CD1 . PHE A 1 343 ? 5.061   27.212 44.533  1.00 23.13 ? 343 PHE A CD1 1 
ATOM   2908 C CD2 . PHE A 1 343 ? 6.399   28.942 43.558  1.00 25.66 ? 343 PHE A CD2 1 
ATOM   2909 C CE1 . PHE A 1 343 ? 5.364   27.681 45.814  1.00 23.92 ? 343 PHE A CE1 1 
ATOM   2910 C CE2 . PHE A 1 343 ? 6.704   29.428 44.837  1.00 32.71 ? 343 PHE A CE2 1 
ATOM   2911 C CZ  . PHE A 1 343 ? 6.190   28.789 45.970  1.00 28.30 ? 343 PHE A CZ  1 
ATOM   2912 N N   . GLN A 1 344 ? 2.467   26.443 42.594  1.00 20.55 ? 344 GLN A N   1 
ATOM   2913 C CA  . GLN A 1 344 ? 1.333   26.147 43.462  1.00 19.57 ? 344 GLN A CA  1 
ATOM   2914 C C   . GLN A 1 344 ? 1.819   26.014 44.894  1.00 22.69 ? 344 GLN A C   1 
ATOM   2915 O O   . GLN A 1 344 ? 2.497   25.023 45.218  1.00 19.16 ? 344 GLN A O   1 
ATOM   2916 C CB  . GLN A 1 344 ? 0.621   24.872 43.005  1.00 21.01 ? 344 GLN A CB  1 
ATOM   2917 C CG  . GLN A 1 344 ? 0.002   25.077 41.602  1.00 24.00 ? 344 GLN A CG  1 
ATOM   2918 C CD  . GLN A 1 344 ? -0.763  23.879 41.082  1.00 28.43 ? 344 GLN A CD  1 
ATOM   2919 O OE1 . GLN A 1 344 ? -1.899  24.014 40.641  1.00 29.66 ? 344 GLN A OE1 1 
ATOM   2920 N NE2 . GLN A 1 344 ? -0.140  22.706 41.108  1.00 30.19 ? 344 GLN A NE2 1 
ATOM   2921 N N   . PRO A 1 345 ? 1.511   26.975 45.769  1.00 17.42 ? 345 PRO A N   1 
ATOM   2922 C CA  . PRO A 1 345 ? 1.992   26.932 47.150  1.00 18.03 ? 345 PRO A CA  1 
ATOM   2923 C C   . PRO A 1 345 ? 1.195   25.963 48.002  1.00 19.70 ? 345 PRO A C   1 
ATOM   2924 O O   . PRO A 1 345 ? 0.000   25.760 47.790  1.00 17.71 ? 345 PRO A O   1 
ATOM   2925 C CB  . PRO A 1 345 ? 1.766   28.371 47.634  1.00 16.38 ? 345 PRO A CB  1 
ATOM   2926 C CG  . PRO A 1 345 ? 0.566   28.815 46.883  1.00 17.12 ? 345 PRO A CG  1 
ATOM   2927 C CD  . PRO A 1 345 ? 0.687   28.169 45.515  1.00 22.56 ? 345 PRO A CD  1 
ATOM   2928 N N   . VAL A 1 346 ? 1.874   25.373 48.989  1.00 15.12 ? 346 VAL A N   1 
ATOM   2929 C CA  . VAL A 1 346 ? 1.213   24.575 50.014  1.00 14.11 ? 346 VAL A CA  1 
ATOM   2930 C C   . VAL A 1 346 ? 1.158   25.420 51.269  1.00 15.00 ? 346 VAL A C   1 
ATOM   2931 O O   . VAL A 1 346 ? 2.194   25.875 51.766  1.00 19.56 ? 346 VAL A O   1 
ATOM   2932 C CB  . VAL A 1 346 ? 1.940   23.251 50.279  1.00 14.34 ? 346 VAL A CB  1 
ATOM   2933 C CG1 . VAL A 1 346 ? 1.136   22.422 51.270  1.00 20.79 ? 346 VAL A CG1 1 
ATOM   2934 C CG2 . VAL A 1 346 ? 2.138   22.463 48.963  1.00 15.37 ? 346 VAL A CG2 1 
ATOM   2935 N N   . VAL A 1 347 ? -0.042  25.613 51.796  1.00 18.42 ? 347 VAL A N   1 
ATOM   2936 C CA  . VAL A 1 347 ? -0.284  26.535 52.896  1.00 19.01 ? 347 VAL A CA  1 
ATOM   2937 C C   . VAL A 1 347 ? -0.834  25.727 54.057  1.00 12.91 ? 347 VAL A C   1 
ATOM   2938 O O   . VAL A 1 347 ? -1.988  25.297 54.021  1.00 15.03 ? 347 VAL A O   1 
ATOM   2939 C CB  . VAL A 1 347 ? -1.256  27.655 52.491  1.00 15.02 ? 347 VAL A CB  1 
ATOM   2940 C CG1 . VAL A 1 347 ? -1.441  28.630 53.660  1.00 17.45 ? 347 VAL A CG1 1 
ATOM   2941 C CG2 . VAL A 1 347 ? -0.757  28.343 51.202  1.00 13.92 ? 347 VAL A CG2 1 
ATOM   2942 N N   . PHE A 1 348 ? -0.010  25.511 55.085  1.00 14.73 ? 348 PHE A N   1 
ATOM   2943 C CA  . PHE A 1 348 ? -0.432  24.728 56.239  1.00 15.70 ? 348 PHE A CA  1 
ATOM   2944 C C   . PHE A 1 348 ? -0.997  25.660 57.305  1.00 13.92 ? 348 PHE A C   1 
ATOM   2945 O O   . PHE A 1 348 ? -0.330  26.609 57.713  1.00 15.79 ? 348 PHE A O   1 
ATOM   2946 C CB  . PHE A 1 348 ? 0.741   23.915 56.813  1.00 12.42 ? 348 PHE A CB  1 
ATOM   2947 C CG  . PHE A 1 348 ? 0.789   22.484 56.309  1.00 15.52 ? 348 PHE A CG  1 
ATOM   2948 C CD1 . PHE A 1 348 ? 1.096   22.223 54.986  1.00 15.57 ? 348 PHE A CD1 1 
ATOM   2949 C CD2 . PHE A 1 348 ? 0.555   21.418 57.166  1.00 14.56 ? 348 PHE A CD2 1 
ATOM   2950 C CE1 . PHE A 1 348 ? 1.123   20.902 54.514  1.00 14.92 ? 348 PHE A CE1 1 
ATOM   2951 C CE2 . PHE A 1 348 ? 0.584   20.110 56.709  1.00 16.22 ? 348 PHE A CE2 1 
ATOM   2952 C CZ  . PHE A 1 348 ? 0.882   19.848 55.380  1.00 14.13 ? 348 PHE A CZ  1 
ATOM   2953 N N   . VAL A 1 349 ? -2.208  25.366 57.765  1.00 11.68 ? 349 VAL A N   1 
ATOM   2954 C CA  . VAL A 1 349 ? -2.835  26.082 58.878  1.00 10.70 ? 349 VAL A CA  1 
ATOM   2955 C C   . VAL A 1 349 ? -2.908  25.087 60.022  1.00 11.71 ? 349 VAL A C   1 
ATOM   2956 O O   . VAL A 1 349 ? -3.669  24.119 59.942  1.00 14.44 ? 349 VAL A O   1 
ATOM   2957 C CB  . VAL A 1 349 ? -4.239  26.585 58.509  1.00 13.30 ? 349 VAL A CB  1 
ATOM   2958 C CG1 . VAL A 1 349 ? -4.868  27.339 59.679  1.00 11.44 ? 349 VAL A CG1 1 
ATOM   2959 C CG2 . VAL A 1 349 ? -4.162  27.509 57.281  1.00 16.42 ? 349 VAL A CG2 1 
ATOM   2960 N N   . VAL A 1 350 ? -2.122  25.299 61.073  1.00 10.66 ? 350 VAL A N   1 
ATOM   2961 C CA  . VAL A 1 350 ? -2.006  24.324 62.153  1.00 9.19  ? 350 VAL A CA  1 
ATOM   2962 C C   . VAL A 1 350 ? -2.133  25.043 63.490  1.00 9.21  ? 350 VAL A C   1 
ATOM   2963 O O   . VAL A 1 350 ? -1.363  25.970 63.772  1.00 13.27 ? 350 VAL A O   1 
ATOM   2964 C CB  . VAL A 1 350 ? -0.677  23.554 62.078  1.00 17.24 ? 350 VAL A CB  1 
ATOM   2965 C CG1 . VAL A 1 350 ? -0.680  22.448 63.107  1.00 17.81 ? 350 VAL A CG1 1 
ATOM   2966 C CG2 . VAL A 1 350 ? -0.434  22.991 60.642  1.00 14.82 ? 350 VAL A CG2 1 
ATOM   2967 N N   . LEU A 1 351 ? -3.079  24.595 64.324  1.00 13.65 ? 351 LEU A N   1 
ATOM   2968 C CA  . LEU A 1 351 ? -3.248  25.121 65.673  1.00 12.48 ? 351 LEU A CA  1 
ATOM   2969 C C   . LEU A 1 351 ? -4.052  24.094 66.469  1.00 14.79 ? 351 LEU A C   1 
ATOM   2970 O O   . LEU A 1 351 ? -4.464  23.057 65.938  1.00 13.06 ? 351 LEU A O   1 
ATOM   2971 C CB  . LEU A 1 351 ? -3.926  26.502 65.663  1.00 14.24 ? 351 LEU A CB  1 
ATOM   2972 C CG  . LEU A 1 351 ? -5.329  26.591 65.047  1.00 16.00 ? 351 LEU A CG  1 
ATOM   2973 C CD1 . LEU A 1 351 ? -6.199  27.658 65.770  1.00 16.52 ? 351 LEU A CD1 1 
ATOM   2974 C CD2 . LEU A 1 351 ? -5.266  26.921 63.522  1.00 15.43 ? 351 LEU A CD2 1 
ATOM   2975 N N   . ASP A 1 352 ? -4.249  24.368 67.761  1.00 13.23 ? 352 ASP A N   1 
ATOM   2976 C CA  . ASP A 1 352 ? -5.100  23.492 68.553  1.00 12.44 ? 352 ASP A CA  1 
ATOM   2977 C C   . ASP A 1 352 ? -6.485  23.489 67.943  1.00 12.48 ? 352 ASP A C   1 
ATOM   2978 O O   . ASP A 1 352 ? -6.975  24.523 67.485  1.00 17.06 ? 352 ASP A O   1 
ATOM   2979 C CB  . ASP A 1 352 ? -5.195  23.968 70.011  1.00 13.49 ? 352 ASP A CB  1 
ATOM   2980 C CG  . ASP A 1 352 ? -3.882  23.920 70.747  1.00 14.48 ? 352 ASP A CG  1 
ATOM   2981 O OD1 . ASP A 1 352 ? -2.874  23.397 70.207  1.00 17.32 ? 352 ASP A OD1 1 
ATOM   2982 O OD2 . ASP A 1 352 ? -3.854  24.432 71.898  1.00 17.50 ? 352 ASP A OD2 1 
ATOM   2983 N N   . GLY A 1 353 ? -7.114  22.331 67.945  1.00 11.28 ? 353 GLY A N   1 
ATOM   2984 C CA  . GLY A 1 353 ? -8.428  22.236 67.334  1.00 11.87 ? 353 GLY A CA  1 
ATOM   2985 C C   . GLY A 1 353 ? -9.589  22.486 68.266  1.00 15.18 ? 353 GLY A C   1 
ATOM   2986 O O   . GLY A 1 353 ? -10.732 22.484 67.811  1.00 14.23 ? 353 GLY A O   1 
ATOM   2987 N N   . GLU A 1 354 ? -9.361  22.684 69.560  1.00 14.24 ? 354 GLU A N   1 
ATOM   2988 C CA  . GLU A 1 354 ? -10.490 22.755 70.484  1.00 14.19 ? 354 GLU A CA  1 
ATOM   2989 C C   . GLU A 1 354 ? -10.444 23.950 71.419  1.00 14.55 ? 354 GLU A C   1 
ATOM   2990 O O   . GLU A 1 354 ? -11.379 24.123 72.200  1.00 14.10 ? 354 GLU A O   1 
ATOM   2991 C CB  . GLU A 1 354 ? -10.608 21.450 71.321  1.00 13.63 ? 354 GLU A CB  1 
ATOM   2992 C CG  . GLU A 1 354 ? -9.592  21.304 72.498  1.00 13.06 ? 354 GLU A CG  1 
ATOM   2993 C CD  . GLU A 1 354 ? -8.209  20.851 72.046  1.00 13.41 ? 354 GLU A CD  1 
ATOM   2994 O OE1 . GLU A 1 354 ? -7.815  19.704 72.369  1.00 13.20 ? 354 GLU A OE1 1 
ATOM   2995 O OE2 . GLU A 1 354 ? -7.518  21.633 71.355  1.00 14.31 ? 354 GLU A OE2 1 
ATOM   2996 N N   . ASN A 1 355 ? -9.408  24.790 71.363  1.00 10.74 ? 355 ASN A N   1 
ATOM   2997 C CA  . ASN A 1 355 ? -9.251  25.798 72.404  1.00 13.00 ? 355 ASN A CA  1 
ATOM   2998 C C   . ASN A 1 355 ? -9.685  27.212 72.009  1.00 15.98 ? 355 ASN A C   1 
ATOM   2999 O O   . ASN A 1 355 ? -9.866  28.048 72.911  1.00 14.32 ? 355 ASN A O   1 
ATOM   3000 C CB  . ASN A 1 355 ? -7.794  25.796 72.890  1.00 16.05 ? 355 ASN A CB  1 
ATOM   3001 C CG  . ASN A 1 355 ? -7.462  24.524 73.660  1.00 15.61 ? 355 ASN A CG  1 
ATOM   3002 O OD1 . ASN A 1 355 ? -8.260  24.073 74.491  1.00 16.21 ? 355 ASN A OD1 1 
ATOM   3003 N ND2 . ASN A 1 355 ? -6.297  23.940 73.395  1.00 14.05 ? 355 ASN A ND2 1 
ATOM   3004 N N   . CYS A 1 356 ? -9.865  27.514 70.717  1.00 16.83 ? 356 CYS A N   1 
ATOM   3005 C CA  . CYS A 1 356 ? -10.190 28.884 70.307  1.00 14.09 ? 356 CYS A CA  1 
ATOM   3006 C C   . CYS A 1 356 ? -11.689 29.158 70.183  1.00 11.80 ? 356 CYS A C   1 
ATOM   3007 O O   . CYS A 1 356 ? -12.107 30.319 70.325  1.00 11.43 ? 356 CYS A O   1 
ATOM   3008 C CB  . CYS A 1 356 ? -9.489  29.222 68.976  1.00 13.22 ? 356 CYS A CB  1 
ATOM   3009 S SG  . CYS A 1 356 ? -9.862  28.059 67.619  1.00 15.61 ? 356 CYS A SG  1 
ATOM   3010 N N   . TRP A 1 357 ? -12.511 28.123 69.976  1.00 12.60 ? 357 TRP A N   1 
ATOM   3011 C CA  . TRP A 1 357 ? -13.921 28.318 69.627  1.00 15.15 ? 357 TRP A CA  1 
ATOM   3012 C C   . TRP A 1 357 ? -14.738 28.889 70.776  1.00 12.23 ? 357 TRP A C   1 
ATOM   3013 O O   . TRP A 1 357 ? -15.686 29.641 70.531  1.00 15.56 ? 357 TRP A O   1 
ATOM   3014 C CB  . TRP A 1 357 ? -14.520 26.995 69.145  1.00 13.06 ? 357 TRP A CB  1 
ATOM   3015 C CG  . TRP A 1 357 ? -13.628 26.354 68.172  1.00 12.22 ? 357 TRP A CG  1 
ATOM   3016 C CD1 . TRP A 1 357 ? -13.016 25.131 68.291  1.00 15.78 ? 357 TRP A CD1 1 
ATOM   3017 C CD2 . TRP A 1 357 ? -13.170 26.913 66.921  1.00 11.46 ? 357 TRP A CD2 1 
ATOM   3018 N NE1 . TRP A 1 357 ? -12.230 24.898 67.193  1.00 12.00 ? 357 TRP A NE1 1 
ATOM   3019 C CE2 . TRP A 1 357 ? -12.308 25.968 66.340  1.00 12.56 ? 357 TRP A CE2 1 
ATOM   3020 C CE3 . TRP A 1 357 ? -13.396 28.128 66.256  1.00 10.01 ? 357 TRP A CE3 1 
ATOM   3021 C CZ2 . TRP A 1 357 ? -11.646 26.200 65.128  1.00 12.80 ? 357 TRP A CZ2 1 
ATOM   3022 C CZ3 . TRP A 1 357 ? -12.763 28.355 65.041  1.00 15.90 ? 357 TRP A CZ3 1 
ATOM   3023 C CH2 . TRP A 1 357 ? -11.898 27.381 64.488  1.00 13.54 ? 357 TRP A CH2 1 
ATOM   3024 N N   . GLU A 1 358 ? -14.394 28.547 72.026  1.00 11.82 ? 358 GLU A N   1 
ATOM   3025 C CA  . GLU A 1 358 ? -15.114 29.091 73.178  1.00 12.75 ? 358 GLU A CA  1 
ATOM   3026 C C   . GLU A 1 358 ? -15.099 30.624 73.231  1.00 15.38 ? 358 GLU A C   1 
ATOM   3027 O O   . GLU A 1 358 ? -15.978 31.227 73.882  1.00 14.51 ? 358 GLU A O   1 
ATOM   3028 C CB  . GLU A 1 358 ? -14.524 28.513 74.476  1.00 15.44 ? 358 GLU A CB  1 
ATOM   3029 C CG  . GLU A 1 358 ? -13.060 28.883 74.742  1.00 14.51 ? 358 GLU A CG  1 
ATOM   3030 C CD  . GLU A 1 358 ? -12.357 27.858 75.659  1.00 19.07 ? 358 GLU A CD  1 
ATOM   3031 O OE1 . GLU A 1 358 ? -11.862 28.236 76.744  1.00 23.51 ? 358 GLU A OE1 1 
ATOM   3032 O OE2 . GLU A 1 358 ? -12.312 26.674 75.293  1.00 19.86 ? 358 GLU A OE2 1 
ATOM   3033 N N   . TYR A 1 359 ? -14.129 31.271 72.574  1.00 14.16 ? 359 TYR A N   1 
ATOM   3034 C CA  . TYR A 1 359 ? -14.034 32.733 72.559  1.00 16.61 ? 359 TYR A CA  1 
ATOM   3035 C C   . TYR A 1 359 ? -14.788 33.368 71.409  1.00 15.93 ? 359 TYR A C   1 
ATOM   3036 O O   . TYR A 1 359 ? -14.918 34.602 71.376  1.00 16.54 ? 359 TYR A O   1 
ATOM   3037 C CB  . TYR A 1 359 ? -12.578 33.186 72.472  1.00 15.51 ? 359 TYR A CB  1 
ATOM   3038 C CG  . TYR A 1 359 ? -11.801 32.820 73.704  1.00 17.74 ? 359 TYR A CG  1 
ATOM   3039 C CD1 . TYR A 1 359 ? -11.840 33.634 74.827  1.00 22.86 ? 359 TYR A CD1 1 
ATOM   3040 C CD2 . TYR A 1 359 ? -11.066 31.644 73.766  1.00 19.01 ? 359 TYR A CD2 1 
ATOM   3041 C CE1 . TYR A 1 359 ? -11.150 33.302 75.965  1.00 23.82 ? 359 TYR A CE1 1 
ATOM   3042 C CE2 . TYR A 1 359 ? -10.375 31.298 74.921  1.00 19.37 ? 359 TYR A CE2 1 
ATOM   3043 C CZ  . TYR A 1 359 ? -10.425 32.131 76.008  1.00 27.28 ? 359 TYR A CZ  1 
ATOM   3044 O OH  . TYR A 1 359 ? -9.742  31.813 77.178  1.00 24.81 ? 359 TYR A OH  1 
ATOM   3045 N N   . TYR A 1 360 ? -15.272 32.569 70.476  1.00 16.49 ? 360 TYR A N   1 
ATOM   3046 C CA  . TYR A 1 360 ? -16.065 33.068 69.365  1.00 18.84 ? 360 TYR A CA  1 
ATOM   3047 C C   . TYR A 1 360 ? -17.543 33.069 69.715  1.00 15.04 ? 360 TYR A C   1 
ATOM   3048 O O   . TYR A 1 360 ? -18.019 32.224 70.479  1.00 17.28 ? 360 TYR A O   1 
ATOM   3049 C CB  . TYR A 1 360 ? -15.902 32.180 68.138  1.00 15.99 ? 360 TYR A CB  1 
ATOM   3050 C CG  . TYR A 1 360 ? -14.618 32.243 67.362  1.00 16.37 ? 360 TYR A CG  1 
ATOM   3051 C CD1 . TYR A 1 360 ? -13.406 31.833 67.914  1.00 16.71 ? 360 TYR A CD1 1 
ATOM   3052 C CD2 . TYR A 1 360 ? -14.643 32.625 66.020  1.00 18.03 ? 360 TYR A CD2 1 
ATOM   3053 C CE1 . TYR A 1 360 ? -12.239 31.853 67.159  1.00 12.58 ? 360 TYR A CE1 1 
ATOM   3054 C CE2 . TYR A 1 360 ? -13.518 32.626 65.261  1.00 13.56 ? 360 TYR A CE2 1 
ATOM   3055 C CZ  . TYR A 1 360 ? -12.316 32.243 65.814  1.00 14.52 ? 360 TYR A CZ  1 
ATOM   3056 O OH  . TYR A 1 360 ? -11.217 32.257 65.001  1.00 13.34 ? 360 TYR A OH  1 
ATOM   3057 N N   . GLU A 1 361 ? -18.271 34.023 69.128  1.00 16.08 ? 361 GLU A N   1 
ATOM   3058 C CA  . GLU A 1 361 ? -19.724 33.995 69.156  1.00 21.16 ? 361 GLU A CA  1 
ATOM   3059 C C   . GLU A 1 361 ? -20.247 32.629 68.722  1.00 17.64 ? 361 GLU A C   1 
ATOM   3060 O O   . GLU A 1 361 ? -19.828 32.086 67.697  1.00 19.46 ? 361 GLU A O   1 
ATOM   3061 C CB  . GLU A 1 361 ? -20.267 35.085 68.230  1.00 26.29 ? 361 GLU A CB  1 
ATOM   3062 C CG  . GLU A 1 361 ? -21.778 35.075 68.058  1.00 40.74 ? 361 GLU A CG  1 
ATOM   3063 C CD  . GLU A 1 361 ? -22.511 35.503 69.315  1.00 59.62 ? 361 GLU A CD  1 
ATOM   3064 O OE1 . GLU A 1 361 ? -21.864 36.073 70.226  1.00 58.99 ? 361 GLU A OE1 1 
ATOM   3065 O OE2 . GLU A 1 361 ? -23.741 35.272 69.390  1.00 70.33 ? 361 GLU A OE2 1 
ATOM   3066 N N   . GLU A 1 362 ? -21.135 32.059 69.537  1.00 18.35 ? 362 GLU A N   1 
ATOM   3067 C CA  . GLU A 1 362 ? -21.797 30.794 69.224  1.00 18.80 ? 362 GLU A CA  1 
ATOM   3068 C C   . GLU A 1 362 ? -20.782 29.697 68.928  1.00 20.94 ? 362 GLU A C   1 
ATOM   3069 O O   . GLU A 1 362 ? -20.936 28.902 67.994  1.00 17.99 ? 362 GLU A O   1 
ATOM   3070 C CB  . GLU A 1 362 ? -22.782 30.962 68.061  1.00 23.35 ? 362 GLU A CB  1 
ATOM   3071 C CG  . GLU A 1 362 ? -24.129 31.515 68.493  1.00 36.03 ? 362 GLU A CG  1 
ATOM   3072 C CD  . GLU A 1 362 ? -25.100 31.700 67.337  1.00 45.42 ? 362 GLU A CD  1 
ATOM   3073 O OE1 . GLU A 1 362 ? -26.210 32.212 67.583  1.00 51.32 ? 362 GLU A OE1 1 
ATOM   3074 O OE2 . GLU A 1 362 ? -24.760 31.328 66.193  1.00 46.71 ? 362 GLU A OE2 1 
ATOM   3075 N N   . ASN A 1 363 ? -19.719 29.662 69.722  1.00 15.78 ? 363 ASN A N   1 
ATOM   3076 C CA  . ASN A 1 363 ? -18.728 28.584 69.647  1.00 13.18 ? 363 ASN A CA  1 
ATOM   3077 C C   . ASN A 1 363 ? -18.072 28.495 68.266  1.00 12.51 ? 363 ASN A C   1 
ATOM   3078 O O   . ASN A 1 363 ? -17.665 27.416 67.818  1.00 19.22 ? 363 ASN A O   1 
ATOM   3079 C CB  . ASN A 1 363 ? -19.353 27.241 70.018  1.00 18.55 ? 363 ASN A CB  1 
ATOM   3080 C CG  . ASN A 1 363 ? -18.321 26.230 70.345  1.00 20.94 ? 363 ASN A CG  1 
ATOM   3081 O OD1 . ASN A 1 363 ? -17.302 26.552 70.979  1.00 15.22 ? 363 ASN A OD1 1 
ATOM   3082 N ND2 . ASN A 1 363 ? -18.528 25.004 69.873  1.00 22.63 ? 363 ASN A ND2 1 
ATOM   3083 N N   . GLY A 1 364 ? -17.985 29.622 67.582  1.00 12.85 ? 364 GLY A N   1 
ATOM   3084 C CA  . GLY A 1 364 ? -17.350 29.660 66.272  1.00 16.52 ? 364 GLY A CA  1 
ATOM   3085 C C   . GLY A 1 364 ? -18.108 28.999 65.154  1.00 19.05 ? 364 GLY A C   1 
ATOM   3086 O O   . GLY A 1 364 ? -17.557 28.864 64.051  1.00 15.27 ? 364 GLY A O   1 
ATOM   3087 N N   . ILE A 1 365 ? -19.358 28.603 65.385  1.00 17.82 ? 365 ILE A N   1 
ATOM   3088 C CA  . ILE A 1 365 ? -20.111 27.844 64.389  1.00 14.26 ? 365 ILE A CA  1 
ATOM   3089 C C   . ILE A 1 365 ? -20.452 28.750 63.207  1.00 18.78 ? 365 ILE A C   1 
ATOM   3090 O O   . ILE A 1 365 ? -20.270 28.334 62.053  1.00 19.24 ? 365 ILE A O   1 
ATOM   3091 C CB  . ILE A 1 365 ? -21.345 27.186 65.032  1.00 17.18 ? 365 ILE A CB  1 
ATOM   3092 C CG1 . ILE A 1 365 ? -20.855 26.087 65.989  1.00 18.71 ? 365 ILE A CG1 1 
ATOM   3093 C CG2 . ILE A 1 365 ? -22.299 26.631 63.961  1.00 15.12 ? 365 ILE A CG2 1 
ATOM   3094 C CD1 . ILE A 1 365 ? -21.796 25.776 67.127  1.00 19.20 ? 365 ILE A CD1 1 
ATOM   3095 N N   . PRO A 1 366 ? -20.893 29.998 63.423  1.00 15.17 ? 366 PRO A N   1 
ATOM   3096 C CA  . PRO A 1 366 ? -21.068 30.899 62.271  1.00 17.86 ? 366 PRO A CA  1 
ATOM   3097 C C   . PRO A 1 366 ? -19.778 31.115 61.484  1.00 16.50 ? 366 PRO A C   1 
ATOM   3098 O O   . PRO A 1 366 ? -19.801 31.163 60.241  1.00 21.36 ? 366 PRO A O   1 
ATOM   3099 C CB  . PRO A 1 366 ? -21.568 32.197 62.919  1.00 17.07 ? 366 PRO A CB  1 
ATOM   3100 C CG  . PRO A 1 366 ? -22.268 31.747 64.166  1.00 25.06 ? 366 PRO A CG  1 
ATOM   3101 C CD  . PRO A 1 366 ? -21.443 30.590 64.672  1.00 16.75 ? 366 PRO A CD  1 
ATOM   3102 N N   . PHE A 1 367 ? -18.650 31.256 62.179  1.00 15.22 ? 367 PHE A N   1 
ATOM   3103 C CA  . PHE A 1 367 ? -17.386 31.455 61.481  1.00 18.11 ? 367 PHE A CA  1 
ATOM   3104 C C   . PHE A 1 367 ? -17.009 30.226 60.658  1.00 17.37 ? 367 PHE A C   1 
ATOM   3105 O O   . PHE A 1 367 ? -16.734 30.331 59.452  1.00 15.61 ? 367 PHE A O   1 
ATOM   3106 C CB  . PHE A 1 367 ? -16.267 31.800 62.465  1.00 18.65 ? 367 PHE A CB  1 
ATOM   3107 C CG  . PHE A 1 367 ? -14.918 31.777 61.835  1.00 17.13 ? 367 PHE A CG  1 
ATOM   3108 C CD1 . PHE A 1 367 ? -14.523 32.792 60.979  1.00 21.33 ? 367 PHE A CD1 1 
ATOM   3109 C CD2 . PHE A 1 367 ? -14.053 30.715 62.060  1.00 15.27 ? 367 PHE A CD2 1 
ATOM   3110 C CE1 . PHE A 1 367 ? -13.285 32.749 60.372  1.00 17.70 ? 367 PHE A CE1 1 
ATOM   3111 C CE2 . PHE A 1 367 ? -12.817 30.668 61.459  1.00 16.10 ? 367 PHE A CE2 1 
ATOM   3112 C CZ  . PHE A 1 367 ? -12.431 31.685 60.613  1.00 12.93 ? 367 PHE A CZ  1 
ATOM   3113 N N   . LEU A 1 368 ? -16.995 29.044 61.285  1.00 15.33 ? 368 LEU A N   1 
ATOM   3114 C CA  . LEU A 1 368 ? -16.553 27.859 60.553  1.00 12.84 ? 368 LEU A CA  1 
ATOM   3115 C C   . LEU A 1 368 ? -17.529 27.472 59.439  1.00 16.66 ? 368 LEU A C   1 
ATOM   3116 O O   . LEU A 1 368 ? -17.097 27.016 58.368  1.00 18.57 ? 368 LEU A O   1 
ATOM   3117 C CB  . LEU A 1 368 ? -16.341 26.693 61.519  1.00 11.21 ? 368 LEU A CB  1 
ATOM   3118 C CG  . LEU A 1 368 ? -15.071 26.762 62.364  1.00 12.47 ? 368 LEU A CG  1 
ATOM   3119 C CD1 . LEU A 1 368 ? -15.016 25.509 63.217  1.00 18.43 ? 368 LEU A CD1 1 
ATOM   3120 C CD2 . LEU A 1 368 ? -13.831 26.847 61.450  1.00 15.91 ? 368 LEU A CD2 1 
ATOM   3121 N N   . GLU A 1 369 ? -18.835 27.623 59.660  1.00 13.55 ? 369 GLU A N   1 
ATOM   3122 C CA  . GLU A 1 369 ? -19.786 27.287 58.596  1.00 14.58 ? 369 GLU A CA  1 
ATOM   3123 C C   . GLU A 1 369 ? -19.584 28.198 57.395  1.00 20.25 ? 369 GLU A C   1 
ATOM   3124 O O   . GLU A 1 369 ? -19.584 27.738 56.247  1.00 18.18 ? 369 GLU A O   1 
ATOM   3125 C CB  . GLU A 1 369 ? -21.227 27.373 59.100  1.00 22.24 ? 369 GLU A CB  1 
ATOM   3126 C CG  . GLU A 1 369 ? -21.650 26.124 59.850  1.00 20.41 ? 369 GLU A CG  1 
ATOM   3127 C CD  . GLU A 1 369 ? -23.043 26.200 60.405  1.00 24.34 ? 369 GLU A CD  1 
ATOM   3128 O OE1 . GLU A 1 369 ? -23.692 27.272 60.278  1.00 24.35 ? 369 GLU A OE1 1 
ATOM   3129 O OE2 . GLU A 1 369 ? -23.506 25.180 60.955  1.00 23.85 ? 369 GLU A OE2 1 
ATOM   3130 N N   . LYS A 1 370 ? -19.348 29.487 57.644  1.00 16.61 ? 370 LYS A N   1 
ATOM   3131 C CA  . LYS A 1 370 ? -19.127 30.419 56.537  1.00 17.82 ? 370 LYS A CA  1 
ATOM   3132 C C   . LYS A 1 370 ? -17.751 30.219 55.908  1.00 21.29 ? 370 LYS A C   1 
ATOM   3133 O O   . LYS A 1 370 ? -17.602 30.298 54.676  1.00 19.80 ? 370 LYS A O   1 
ATOM   3134 C CB  . LYS A 1 370 ? -19.302 31.856 57.030  1.00 23.05 ? 370 LYS A CB  1 
ATOM   3135 C CG  . LYS A 1 370 ? -19.279 32.907 55.916  1.00 30.60 ? 370 LYS A CG  1 
ATOM   3136 C CD  . LYS A 1 370 ? -19.329 34.306 56.508  1.00 42.47 ? 370 LYS A CD  1 
ATOM   3137 C CE  . LYS A 1 370 ? -20.605 34.525 57.316  1.00 46.63 ? 370 LYS A CE  1 
ATOM   3138 N NZ  . LYS A 1 370 ? -21.801 34.506 56.431  1.00 48.67 ? 370 LYS A NZ  1 
ATOM   3139 N N   . LEU A 1 371 ? -16.731 29.961 56.729  1.00 14.92 ? 371 LEU A N   1 
ATOM   3140 C CA  . LEU A 1 371 ? -15.401 29.705 56.194  1.00 15.17 ? 371 LEU A CA  1 
ATOM   3141 C C   . LEU A 1 371 ? -15.414 28.491 55.279  1.00 16.58 ? 371 LEU A C   1 
ATOM   3142 O O   . LEU A 1 371 ? -14.972 28.558 54.125  1.00 18.91 ? 371 LEU A O   1 
ATOM   3143 C CB  . LEU A 1 371 ? -14.411 29.496 57.344  1.00 15.17 ? 371 LEU A CB  1 
ATOM   3144 C CG  . LEU A 1 371 ? -13.021 29.064 56.880  1.00 15.08 ? 371 LEU A CG  1 
ATOM   3145 C CD1 . LEU A 1 371 ? -12.407 30.198 56.051  1.00 23.05 ? 371 LEU A CD1 1 
ATOM   3146 C CD2 . LEU A 1 371 ? -12.114 28.690 58.070  1.00 14.30 ? 371 LEU A CD2 1 
ATOM   3147 N N   . TYR A 1 372 ? -15.940 27.372 55.778  1.00 19.36 ? 372 TYR A N   1 
ATOM   3148 C CA  . TYR A 1 372 ? -15.934 26.135 55.008  1.00 16.38 ? 372 TYR A CA  1 
ATOM   3149 C C   . TYR A 1 372 ? -16.831 26.249 53.781  1.00 21.12 ? 372 TYR A C   1 
ATOM   3150 O O   . TYR A 1 372 ? -16.476 25.756 52.704  1.00 17.73 ? 372 TYR A O   1 
ATOM   3151 C CB  . TYR A 1 372 ? -16.370 24.977 55.903  1.00 13.94 ? 372 TYR A CB  1 
ATOM   3152 C CG  . TYR A 1 372 ? -15.380 24.608 57.024  1.00 17.13 ? 372 TYR A CG  1 
ATOM   3153 C CD1 . TYR A 1 372 ? -14.043 25.014 56.988  1.00 14.41 ? 372 TYR A CD1 1 
ATOM   3154 C CD2 . TYR A 1 372 ? -15.793 23.849 58.101  1.00 12.35 ? 372 TYR A CD2 1 
ATOM   3155 C CE1 . TYR A 1 372 ? -13.136 24.638 58.001  1.00 14.54 ? 372 TYR A CE1 1 
ATOM   3156 C CE2 . TYR A 1 372 ? -14.892 23.473 59.119  1.00 11.64 ? 372 TYR A CE2 1 
ATOM   3157 C CZ  . TYR A 1 372 ? -13.577 23.870 59.061  1.00 13.27 ? 372 TYR A CZ  1 
ATOM   3158 O OH  . TYR A 1 372 ? -12.683 23.509 60.047  1.00 14.25 ? 372 TYR A OH  1 
ATOM   3159 N N   . SER A 1 373 ? -17.988 26.911 53.917  1.00 19.49 ? 373 SER A N   1 
ATOM   3160 C CA  . SER A 1 373 ? -18.850 27.117 52.756  1.00 16.94 ? 373 SER A CA  1 
ATOM   3161 C C   . SER A 1 373 ? -18.154 27.956 51.693  1.00 17.34 ? 373 SER A C   1 
ATOM   3162 O O   . SER A 1 373 ? -18.340 27.720 50.494  1.00 22.02 ? 373 SER A O   1 
ATOM   3163 C CB  . SER A 1 373 ? -20.156 27.790 53.176  1.00 19.12 ? 373 SER A CB  1 
ATOM   3164 O OG  . SER A 1 373 ? -20.930 28.101 52.040  1.00 27.92 ? 373 SER A OG  1 
ATOM   3165 N N   . THR A 1 374 ? -17.397 28.973 52.111  1.00 21.18 ? 374 THR A N   1 
ATOM   3166 C CA  . THR A 1 374 ? -16.730 29.850 51.144  1.00 21.26 ? 374 THR A CA  1 
ATOM   3167 C C   . THR A 1 374 ? -15.511 29.166 50.533  1.00 20.26 ? 374 THR A C   1 
ATOM   3168 O O   . THR A 1 374 ? -15.264 29.276 49.323  1.00 21.78 ? 374 THR A O   1 
ATOM   3169 C CB  . THR A 1 374 ? -16.307 31.163 51.812  1.00 25.23 ? 374 THR A CB  1 
ATOM   3170 O OG1 . THR A 1 374 ? -17.419 31.762 52.484  1.00 23.65 ? 374 THR A OG1 1 
ATOM   3171 C CG2 . THR A 1 374 ? -15.779 32.147 50.786  1.00 26.12 ? 374 THR A CG2 1 
ATOM   3172 N N   . LEU A 1 375 ? -14.746 28.446 51.349  1.00 19.80 ? 375 LEU A N   1 
ATOM   3173 C CA  . LEU A 1 375 ? -13.582 27.723 50.837  1.00 18.46 ? 375 LEU A CA  1 
ATOM   3174 C C   . LEU A 1 375 ? -13.988 26.741 49.753  1.00 25.27 ? 375 LEU A C   1 
ATOM   3175 O O   . LEU A 1 375 ? -13.386 26.701 48.671  1.00 25.09 ? 375 LEU A O   1 
ATOM   3176 C CB  . LEU A 1 375 ? -12.895 26.973 51.974  1.00 15.29 ? 375 LEU A CB  1 
ATOM   3177 C CG  . LEU A 1 375 ? -12.048 27.831 52.886  1.00 20.12 ? 375 LEU A CG  1 
ATOM   3178 C CD1 . LEU A 1 375 ? -11.513 26.899 53.956  1.00 22.01 ? 375 LEU A CD1 1 
ATOM   3179 C CD2 . LEU A 1 375 ? -10.938 28.468 52.083  1.00 24.09 ? 375 LEU A CD2 1 
ATOM   3180 N N   . GLU A 1 376 ? -15.040 25.964 50.010  1.00 21.48 ? 376 GLU A N   1 
ATOM   3181 C CA  . GLU A 1 376 ? -15.402 24.916 49.071  1.00 24.96 ? 376 GLU A CA  1 
ATOM   3182 C C   . GLU A 1 376 ? -15.888 25.456 47.731  1.00 25.69 ? 376 GLU A C   1 
ATOM   3183 O O   . GLU A 1 376 ? -16.041 24.666 46.794  1.00 27.73 ? 376 GLU A O   1 
ATOM   3184 C CB  . GLU A 1 376 ? -16.470 24.002 49.684  1.00 23.81 ? 376 GLU A CB  1 
ATOM   3185 C CG  . GLU A 1 376 ? -17.881 24.573 49.659  1.00 27.03 ? 376 GLU A CG  1 
ATOM   3186 C CD  . GLU A 1 376 ? -18.875 23.729 50.452  1.00 32.43 ? 376 GLU A CD  1 
ATOM   3187 O OE1 . GLU A 1 376 ? -19.997 24.208 50.695  1.00 30.90 ? 376 GLU A OE1 1 
ATOM   3188 O OE2 . GLU A 1 376 ? -18.531 22.589 50.839  1.00 38.14 ? 376 GLU A OE2 1 
ATOM   3189 N N   . LYS A 1 377 ? -16.101 26.768 47.606  1.00 26.97 ? 377 LYS A N   1 
ATOM   3190 C CA  . LYS A 1 377 ? -16.646 27.367 46.394  1.00 29.39 ? 377 LYS A CA  1 
ATOM   3191 C C   . LYS A 1 377 ? -15.626 28.194 45.620  1.00 27.49 ? 377 LYS A C   1 
ATOM   3192 O O   . LYS A 1 377 ? -15.982 28.803 44.602  1.00 31.49 ? 377 LYS A O   1 
ATOM   3193 C CB  . LYS A 1 377 ? -17.862 28.237 46.737  1.00 29.84 ? 377 LYS A CB  1 
ATOM   3194 C CG  . LYS A 1 377 ? -19.062 27.438 47.250  1.00 33.59 ? 377 LYS A CG  1 
ATOM   3195 C CD  . LYS A 1 377 ? -20.117 28.359 47.891  1.00 37.21 ? 377 LYS A CD  1 
ATOM   3196 C CE  . LYS A 1 377 ? -21.353 27.582 48.334  1.00 30.30 ? 377 LYS A CE  1 
ATOM   3197 N NZ  . LYS A 1 377 ? -21.011 26.593 49.406  1.00 28.14 ? 377 LYS A NZ  1 
ATOM   3198 N N   . GLU A 1 378 ? -14.375 28.250 46.071  1.00 24.47 ? 378 GLU A N   1 
ATOM   3199 C CA  . GLU A 1 378 ? -13.329 28.973 45.360  1.00 26.14 ? 378 GLU A CA  1 
ATOM   3200 C C   . GLU A 1 378 ? -12.598 27.992 44.457  1.00 26.18 ? 378 GLU A C   1 
ATOM   3201 O O   . GLU A 1 378 ? -12.019 27.021 44.936  1.00 26.58 ? 378 GLU A O   1 
ATOM   3202 C CB  . GLU A 1 378 ? -12.352 29.617 46.340  1.00 23.44 ? 378 GLU A CB  1 
ATOM   3203 C CG  . GLU A 1 378 ? -12.976 30.567 47.296  1.00 25.65 ? 378 GLU A CG  1 
ATOM   3204 C CD  . GLU A 1 378 ? -13.261 31.910 46.667  1.00 32.12 ? 378 GLU A CD  1 
ATOM   3205 O OE1 . GLU A 1 378 ? -13.180 32.041 45.431  1.00 38.51 ? 378 GLU A OE1 1 
ATOM   3206 O OE2 . GLU A 1 378 ? -13.550 32.845 47.432  1.00 40.27 ? 378 GLU A OE2 1 
ATOM   3207 N N   . GLU A 1 379 ? -12.620 28.233 43.154  1.00 30.75 ? 379 GLU A N   1 
ATOM   3208 C CA  . GLU A 1 379 ? -12.051 27.232 42.258  1.00 27.26 ? 379 GLU A CA  1 
ATOM   3209 C C   . GLU A 1 379 ? -10.515 27.229 42.334  1.00 28.41 ? 379 GLU A C   1 
ATOM   3210 O O   . GLU A 1 379 ? -9.878  26.241 41.952  1.00 27.81 ? 379 GLU A O   1 
ATOM   3211 C CB  . GLU A 1 379 ? -12.531 27.495 40.820  1.00 35.68 ? 379 GLU A CB  1 
ATOM   3212 C CG  . GLU A 1 379 ? -12.369 29.058 40.545  1.00 45.43 ? 379 GLU A CG  1 
ATOM   3213 C CD  . GLU A 1 379 ? -12.300 29.439 39.093  1.00 66.83 ? 379 GLU A CD  1 
ATOM   3214 O OE1 . GLU A 1 379 ? -11.384 30.181 38.658  1.00 68.17 ? 379 GLU A OE1 1 
ATOM   3215 O OE2 . GLU A 1 379 ? -13.166 29.035 38.423  1.00 66.02 ? 379 GLU A OE2 1 
ATOM   3216 N N   . TRP A 1 380 ? -9.892  28.316 42.811  1.00 27.11 ? 380 TRP A N   1 
ATOM   3217 C CA  . TRP A 1 380 ? -8.434  28.383 42.865  1.00 23.48 ? 380 TRP A CA  1 
ATOM   3218 C C   . TRP A 1 380 ? -7.854  27.835 44.170  1.00 22.65 ? 380 TRP A C   1 
ATOM   3219 O O   . TRP A 1 380 ? -6.628  27.875 44.351  1.00 21.91 ? 380 TRP A O   1 
ATOM   3220 C CB  . TRP A 1 380 ? -7.941  29.828 42.646  1.00 26.53 ? 380 TRP A CB  1 
ATOM   3221 C CG  . TRP A 1 380 ? -8.687  30.837 43.454  1.00 22.50 ? 380 TRP A CG  1 
ATOM   3222 C CD1 . TRP A 1 380 ? -9.883  31.427 43.144  1.00 26.41 ? 380 TRP A CD1 1 
ATOM   3223 C CD2 . TRP A 1 380 ? -8.314  31.334 44.739  1.00 24.60 ? 380 TRP A CD2 1 
ATOM   3224 N NE1 . TRP A 1 380 ? -10.262 32.282 44.153  1.00 22.63 ? 380 TRP A NE1 1 
ATOM   3225 C CE2 . TRP A 1 380 ? -9.303  32.253 45.138  1.00 22.99 ? 380 TRP A CE2 1 
ATOM   3226 C CE3 . TRP A 1 380 ? -7.207  31.130 45.568  1.00 19.61 ? 380 TRP A CE3 1 
ATOM   3227 C CZ2 . TRP A 1 380 ? -9.238  32.940 46.351  1.00 23.13 ? 380 TRP A CZ2 1 
ATOM   3228 C CZ3 . TRP A 1 380 ? -7.147  31.821 46.788  1.00 25.09 ? 380 TRP A CZ3 1 
ATOM   3229 C CH2 . TRP A 1 380 ? -8.160  32.712 47.158  1.00 21.29 ? 380 TRP A CH2 1 
ATOM   3230 N N   . ILE A 1 381 ? -8.695  27.342 45.082  1.00 17.76 ? 381 ILE A N   1 
ATOM   3231 C CA  . ILE A 1 381 ? -8.252  26.708 46.322  1.00 16.37 ? 381 ILE A CA  1 
ATOM   3232 C C   . ILE A 1 381 ? -8.587  25.231 46.240  1.00 23.12 ? 381 ILE A C   1 
ATOM   3233 O O   . ILE A 1 381 ? -9.718  24.868 45.880  1.00 24.20 ? 381 ILE A O   1 
ATOM   3234 C CB  . ILE A 1 381 ? -8.930  27.325 47.557  1.00 18.10 ? 381 ILE A CB  1 
ATOM   3235 C CG1 . ILE A 1 381 ? -8.486  28.770 47.744  1.00 22.62 ? 381 ILE A CG1 1 
ATOM   3236 C CG2 . ILE A 1 381 ? -8.587  26.514 48.841  1.00 15.71 ? 381 ILE A CG2 1 
ATOM   3237 C CD1 . ILE A 1 381 ? -9.401  29.569 48.705  1.00 21.35 ? 381 ILE A CD1 1 
ATOM   3238 N N   . GLU A 1 382 ? -7.619  24.380 46.586  1.00 16.62 ? 382 GLU A N   1 
ATOM   3239 C CA  . GLU A 1 382 ? -7.874  22.957 46.753  1.00 19.29 ? 382 GLU A CA  1 
ATOM   3240 C C   . GLU A 1 382 ? -7.397  22.577 48.152  1.00 19.99 ? 382 GLU A C   1 
ATOM   3241 O O   . GLU A 1 382 ? -6.191  22.668 48.453  1.00 18.42 ? 382 GLU A O   1 
ATOM   3242 C CB  . GLU A 1 382 ? -7.174  22.122 45.674  1.00 19.96 ? 382 GLU A CB  1 
ATOM   3243 C CG  . GLU A 1 382 ? -7.278  20.655 45.979  1.00 19.40 ? 382 GLU A CG  1 
ATOM   3244 C CD  . GLU A 1 382 ? -6.772  19.749 44.888  1.00 32.27 ? 382 GLU A CD  1 
ATOM   3245 O OE1 . GLU A 1 382 ? -6.308  20.239 43.840  1.00 36.18 ? 382 GLU A OE1 1 
ATOM   3246 O OE2 . GLU A 1 382 ? -6.834  18.520 45.103  1.00 35.65 ? 382 GLU A OE2 1 
ATOM   3247 N N   . THR A 1 383 ? -8.337  22.219 49.027  1.00 14.70 ? 383 THR A N   1 
ATOM   3248 C CA  . THR A 1 383 ? -7.939  21.717 50.333  1.00 13.34 ? 383 THR A CA  1 
ATOM   3249 C C   . THR A 1 383 ? -7.420  20.288 50.172  1.00 13.73 ? 383 THR A C   1 
ATOM   3250 O O   . THR A 1 383 ? -7.893  19.529 49.328  1.00 17.67 ? 383 THR A O   1 
ATOM   3251 C CB  . THR A 1 383 ? -9.095  21.763 51.349  1.00 14.12 ? 383 THR A CB  1 
ATOM   3252 O OG1 . THR A 1 383 ? -10.265 21.070 50.852  1.00 15.29 ? 383 THR A OG1 1 
ATOM   3253 C CG2 . THR A 1 383 ? -9.454  23.227 51.677  1.00 17.43 ? 383 THR A CG2 1 
ATOM   3254 N N   . LEU A 1 384 ? -6.431  19.922 50.996  1.00 13.66 ? 384 LEU A N   1 
ATOM   3255 C CA  . LEU A 1 384 ? -5.747  18.640 50.843  1.00 16.41 ? 384 LEU A CA  1 
ATOM   3256 C C   . LEU A 1 384 ? -5.750  17.866 52.156  1.00 15.19 ? 384 LEU A C   1 
ATOM   3257 O O   . LEU A 1 384 ? -5.675  18.458 53.239  1.00 14.47 ? 384 LEU A O   1 
ATOM   3258 C CB  . LEU A 1 384 ? -4.282  18.824 50.437  1.00 19.29 ? 384 LEU A CB  1 
ATOM   3259 C CG  . LEU A 1 384 ? -3.982  19.480 49.096  1.00 18.67 ? 384 LEU A CG  1 
ATOM   3260 C CD1 . LEU A 1 384 ? -2.450  19.451 48.863  1.00 18.61 ? 384 LEU A CD1 1 
ATOM   3261 C CD2 . LEU A 1 384 ? -4.733  18.772 47.992  1.00 18.34 ? 384 LEU A CD2 1 
ATOM   3262 N N   . THR A 1 385 ? -5.802  16.537 52.043  1.00 16.29 ? 385 THR A N   1 
ATOM   3263 C CA  . THR A 1 385 ? -5.422  15.689 53.167  1.00 14.11 ? 385 THR A CA  1 
ATOM   3264 C C   . THR A 1 385 ? -3.905  15.731 53.370  1.00 14.99 ? 385 THR A C   1 
ATOM   3265 O O   . THR A 1 385 ? -3.140  16.133 52.486  1.00 15.87 ? 385 THR A O   1 
ATOM   3266 C CB  . THR A 1 385 ? -5.836  14.234 52.947  1.00 15.33 ? 385 THR A CB  1 
ATOM   3267 O OG1 . THR A 1 385 ? -5.056  13.666 51.881  1.00 16.45 ? 385 THR A OG1 1 
ATOM   3268 C CG2 . THR A 1 385 ? -7.327  14.119 52.603  1.00 17.23 ? 385 THR A CG2 1 
ATOM   3269 N N   . LEU A 1 386 ? -3.468  15.318 54.567  1.00 13.84 ? 386 LEU A N   1 
ATOM   3270 C CA  . LEU A 1 386 ? -2.027  15.155 54.789  1.00 15.48 ? 386 LEU A CA  1 
ATOM   3271 C C   . LEU A 1 386 ? -1.420  14.209 53.761  1.00 15.51 ? 386 LEU A C   1 
ATOM   3272 O O   . LEU A 1 386 ? -0.316  14.445 53.261  1.00 20.51 ? 386 LEU A O   1 
ATOM   3273 C CB  . LEU A 1 386 ? -1.758  14.647 56.210  1.00 16.46 ? 386 LEU A CB  1 
ATOM   3274 C CG  . LEU A 1 386 ? -2.318  15.470 57.374  1.00 12.90 ? 386 LEU A CG  1 
ATOM   3275 C CD1 . LEU A 1 386 ? -1.901  14.893 58.731  1.00 13.08 ? 386 LEU A CD1 1 
ATOM   3276 C CD2 . LEU A 1 386 ? -1.898  16.945 57.253  1.00 13.86 ? 386 LEU A CD2 1 
ATOM   3277 N N   . GLU A 1 387 ? -2.128  13.123 53.434  1.00 18.55 ? 387 GLU A N   1 
ATOM   3278 C CA  . GLU A 1 387 ? -1.632  12.191 52.427  1.00 18.30 ? 387 GLU A CA  1 
ATOM   3279 C C   . GLU A 1 387 ? -1.433  12.883 51.087  1.00 18.15 ? 387 GLU A C   1 
ATOM   3280 O O   . GLU A 1 387 ? -0.398  12.695 50.423  1.00 20.49 ? 387 GLU A O   1 
ATOM   3281 C CB  . GLU A 1 387 ? -2.601  11.017 52.296  1.00 19.03 ? 387 GLU A CB  1 
ATOM   3282 C CG  . GLU A 1 387 ? -2.270  10.078 51.143  1.00 27.68 ? 387 GLU A CG  1 
ATOM   3283 C CD  . GLU A 1 387 ? -1.586  8.824  51.611  1.00 51.62 ? 387 GLU A CD  1 
ATOM   3284 O OE1 . GLU A 1 387 ? -0.749  8.922  52.537  1.00 53.10 ? 387 GLU A OE1 1 
ATOM   3285 O OE2 . GLU A 1 387 ? -1.867  7.745  51.043  1.00 65.30 ? 387 GLU A OE2 1 
ATOM   3286 N N   . GLU A 1 388 ? -2.394  13.710 50.681  1.00 19.75 ? 388 GLU A N   1 
ATOM   3287 C CA  . GLU A 1 388 ? -2.253  14.418 49.410  1.00 21.63 ? 388 GLU A CA  1 
ATOM   3288 C C   . GLU A 1 388 ? -1.104  15.425 49.456  1.00 18.12 ? 388 GLU A C   1 
ATOM   3289 O O   . GLU A 1 388 ? -0.351  15.558 48.483  1.00 24.19 ? 388 GLU A O   1 
ATOM   3290 C CB  . GLU A 1 388 ? -3.576  15.102 49.053  1.00 19.22 ? 388 GLU A CB  1 
ATOM   3291 C CG  . GLU A 1 388 ? -4.672  14.094 48.654  1.00 24.47 ? 388 GLU A CG  1 
ATOM   3292 C CD  . GLU A 1 388 ? -6.118  14.642 48.705  1.00 34.04 ? 388 GLU A CD  1 
ATOM   3293 O OE1 . GLU A 1 388 ? -6.379  15.722 49.282  1.00 22.57 ? 388 GLU A OE1 1 
ATOM   3294 O OE2 . GLU A 1 388 ? -7.011  13.967 48.138  1.00 39.41 ? 388 GLU A OE2 1 
ATOM   3295 N N   . ALA A 1 389 ? -0.941  16.139 50.568  1.00 17.37 ? 389 ALA A N   1 
ATOM   3296 C CA  . ALA A 1 389 ? 0.148   17.107 50.649  1.00 21.39 ? 389 ALA A CA  1 
ATOM   3297 C C   . ALA A 1 389 ? 1.501   16.403 50.617  1.00 28.11 ? 389 ALA A C   1 
ATOM   3298 O O   . ALA A 1 389 ? 2.460   16.919 50.032  1.00 23.63 ? 389 ALA A O   1 
ATOM   3299 C CB  . ALA A 1 389 ? 0.004   17.964 51.903  1.00 17.72 ? 389 ALA A CB  1 
ATOM   3300 N N   . MET A 1 390 ? 1.566   15.195 51.172  1.00 23.36 ? 390 MET A N   1 
ATOM   3301 C CA  . MET A 1 390 ? 2.815   14.444 51.196  1.00 26.20 ? 390 MET A CA  1 
ATOM   3302 C C   . MET A 1 390 ? 3.184   13.947 49.806  1.00 23.91 ? 390 MET A C   1 
ATOM   3303 O O   . MET A 1 390 ? 4.366   13.938 49.435  1.00 28.89 ? 390 MET A O   1 
ATOM   3304 C CB  . MET A 1 390 ? 2.705   13.272 52.178  1.00 24.95 ? 390 MET A CB  1 
ATOM   3305 C CG  . MET A 1 390 ? 4.040   12.601 52.472  1.00 40.44 ? 390 MET A CG  1 
ATOM   3306 S SD  . MET A 1 390 ? 3.906   11.049 53.389  1.00 44.82 ? 390 MET A SD  1 
ATOM   3307 C CE  . MET A 1 390 ? 3.088   9.996  52.193  1.00 42.09 ? 390 MET A CE  1 
ATOM   3308 N N   . ARG A 1 391 ? 2.189   13.540 49.020  1.00 21.93 ? 391 ARG A N   1 
ATOM   3309 C CA  . ARG A 1 391 ? 2.428   12.841 47.765  1.00 24.75 ? 391 ARG A CA  1 
ATOM   3310 C C   . ARG A 1 391 ? 2.329   13.738 46.531  1.00 30.26 ? 391 ARG A C   1 
ATOM   3311 O O   . ARG A 1 391 ? 2.813   13.338 45.461  1.00 28.31 ? 391 ARG A O   1 
ATOM   3312 C CB  . ARG A 1 391 ? 1.422   11.686 47.626  1.00 33.53 ? 391 ARG A CB  1 
ATOM   3313 C CG  . ARG A 1 391 ? 1.710   10.464 48.501  1.00 39.77 ? 391 ARG A CG  1 
ATOM   3314 C CD  . ARG A 1 391 ? 0.548   9.460  48.470  1.00 50.89 ? 391 ARG A CD  1 
ATOM   3315 N NE  . ARG A 1 391 ? -0.046  9.293  47.137  1.00 64.15 ? 391 ARG A NE  1 
ATOM   3316 C CZ  . ARG A 1 391 ? -1.254  9.745  46.790  1.00 65.13 ? 391 ARG A CZ  1 
ATOM   3317 N NH1 . ARG A 1 391 ? -2.004  10.405 47.666  1.00 57.09 ? 391 ARG A NH1 1 
ATOM   3318 N NH2 . ARG A 1 391 ? -1.714  9.545  45.557  1.00 62.91 ? 391 ARG A NH2 1 
ATOM   3319 N N   . LYS A 1 392 ? 1.729   14.930 46.657  1.00 27.39 ? 392 LYS A N   1 
ATOM   3320 C CA  . LYS A 1 392 ? 1.465   15.811 45.516  1.00 29.34 ? 392 LYS A CA  1 
ATOM   3321 C C   . LYS A 1 392 ? 2.737   16.063 44.709  1.00 30.28 ? 392 LYS A C   1 
ATOM   3322 O O   . LYS A 1 392 ? 3.768   16.455 45.263  1.00 28.40 ? 392 LYS A O   1 
ATOM   3323 C CB  . LYS A 1 392 ? 0.903   17.146 46.024  1.00 31.71 ? 392 LYS A CB  1 
ATOM   3324 C CG  . LYS A 1 392 ? -0.161  17.782 45.139  1.00 39.05 ? 392 LYS A CG  1 
ATOM   3325 C CD  . LYS A 1 392 ? -1.438  16.959 45.148  1.00 42.79 ? 392 LYS A CD  1 
ATOM   3326 C CE  . LYS A 1 392 ? -2.649  17.825 44.816  1.00 45.80 ? 392 LYS A CE  1 
ATOM   3327 N NZ  . LYS A 1 392 ? -3.519  17.172 43.793  1.00 52.19 ? 392 LYS A NZ  1 
ATOM   3328 N N   . GLU A 1 393 ? 2.657   15.846 43.393  1.00 30.26 ? 393 GLU A N   1 
ATOM   3329 C CA  . GLU A 1 393 ? 3.825   16.027 42.540  1.00 29.59 ? 393 GLU A CA  1 
ATOM   3330 C C   . GLU A 1 393 ? 4.009   17.468 42.071  1.00 31.12 ? 393 GLU A C   1 
ATOM   3331 O O   . GLU A 1 393 ? 5.154   17.924 41.942  1.00 33.76 ? 393 GLU A O   1 
ATOM   3332 C CB  . GLU A 1 393 ? 3.746   15.087 41.329  1.00 35.01 ? 393 GLU A CB  1 
ATOM   3333 C CG  . GLU A 1 393 ? 3.744   13.616 41.727  1.00 46.42 ? 393 GLU A CG  1 
ATOM   3334 C CD  . GLU A 1 393 ? 3.785   12.661 40.544  1.00 56.01 ? 393 GLU A CD  1 
ATOM   3335 O OE1 . GLU A 1 393 ? 3.683   13.111 39.378  1.00 64.01 ? 393 GLU A OE1 1 
ATOM   3336 O OE2 . GLU A 1 393 ? 3.914   11.444 40.787  1.00 63.89 ? 393 GLU A OE2 1 
ATOM   3337 N N   . ASP A 1 394 ? 2.922   18.205 41.836  1.00 25.50 ? 394 ASP A N   1 
ATOM   3338 C CA  . ASP A 1 394 ? 3.027   19.547 41.251  1.00 27.41 ? 394 ASP A CA  1 
ATOM   3339 C C   . ASP A 1 394 ? 3.267   20.620 42.314  1.00 34.64 ? 394 ASP A C   1 
ATOM   3340 O O   . ASP A 1 394 ? 2.666   21.699 42.286  1.00 34.70 ? 394 ASP A O   1 
ATOM   3341 C CB  . ASP A 1 394 ? 1.776   19.851 40.424  1.00 38.04 ? 394 ASP A CB  1 
ATOM   3342 C CG  . ASP A 1 394 ? 0.482   19.486 41.157  1.00 48.45 ? 394 ASP A CG  1 
ATOM   3343 O OD1 . ASP A 1 394 ? 0.570   18.810 42.202  1.00 54.18 ? 394 ASP A OD1 1 
ATOM   3344 O OD2 . ASP A 1 394 ? -0.621  19.869 40.693  1.00 47.09 ? 394 ASP A OD2 1 
ATOM   3345 N N   . VAL A 1 395 ? 4.160   20.320 43.254  1.00 26.93 ? 395 VAL A N   1 
ATOM   3346 C CA  . VAL A 1 395 ? 4.516   21.154 44.392  1.00 31.37 ? 395 VAL A CA  1 
ATOM   3347 C C   . VAL A 1 395 ? 6.023   21.384 44.330  1.00 34.12 ? 395 VAL A C   1 
ATOM   3348 O O   . VAL A 1 395 ? 6.750   20.614 43.693  1.00 36.03 ? 395 VAL A O   1 
ATOM   3349 C CB  . VAL A 1 395 ? 4.069   20.455 45.700  1.00 32.13 ? 395 VAL A CB  1 
ATOM   3350 C CG1 . VAL A 1 395 ? 4.832   20.925 46.923  1.00 45.23 ? 395 VAL A CG1 1 
ATOM   3351 C CG2 . VAL A 1 395 ? 2.570   20.645 45.885  1.00 26.89 ? 395 VAL A CG2 1 
ATOM   3352 N N   . LYS A 1 396 ? 6.489   22.475 44.939  1.00 21.35 ? 396 LYS A N   1 
ATOM   3353 C CA  . LYS A 1 396 ? 7.913   22.762 44.948  1.00 26.96 ? 396 LYS A CA  1 
ATOM   3354 C C   . LYS A 1 396 ? 8.532   22.238 46.240  1.00 24.33 ? 396 LYS A C   1 
ATOM   3355 O O   . LYS A 1 396 ? 7.869   22.137 47.282  1.00 22.03 ? 396 LYS A O   1 
ATOM   3356 C CB  . LYS A 1 396 ? 8.175   24.260 44.786  1.00 24.15 ? 396 LYS A CB  1 
ATOM   3357 C CG  . LYS A 1 396 ? 7.628   24.849 43.479  1.00 24.43 ? 396 LYS A CG  1 
ATOM   3358 C CD  . LYS A 1 396 ? 8.137   24.110 42.239  1.00 32.13 ? 396 LYS A CD  1 
ATOM   3359 C CE  . LYS A 1 396 ? 7.456   24.617 40.965  1.00 36.23 ? 396 LYS A CE  1 
ATOM   3360 N NZ  . LYS A 1 396 ? 7.931   23.904 39.746  1.00 40.20 ? 396 LYS A NZ  1 
ATOM   3361 N N   . THR A 1 397 ? 9.824   21.937 46.168  1.00 22.94 ? 397 THR A N   1 
ATOM   3362 C CA  . THR A 1 397 ? 10.466  21.082 47.151  1.00 22.34 ? 397 THR A CA  1 
ATOM   3363 C C   . THR A 1 397 ? 11.868  21.612 47.458  1.00 22.79 ? 397 THR A C   1 
ATOM   3364 O O   . THR A 1 397 ? 12.476  22.296 46.634  1.00 24.17 ? 397 THR A O   1 
ATOM   3365 C CB  . THR A 1 397 ? 10.472  19.660 46.559  1.00 37.88 ? 397 THR A CB  1 
ATOM   3366 O OG1 . THR A 1 397 ? 9.189   19.036 46.765  1.00 33.76 ? 397 THR A OG1 1 
ATOM   3367 C CG2 . THR A 1 397 ? 11.543  18.846 47.106  1.00 52.55 ? 397 THR A CG2 1 
ATOM   3368 N N   . GLU A 1 398 ? 12.369  21.317 48.653  1.00 20.13 ? 398 GLU A N   1 
ATOM   3369 C CA  . GLU A 1 398 ? 13.687  21.786 49.056  1.00 24.66 ? 398 GLU A CA  1 
ATOM   3370 C C   . GLU A 1 398 ? 14.263  20.852 50.113  1.00 23.44 ? 398 GLU A C   1 
ATOM   3371 O O   . GLU A 1 398 ? 13.531  20.266 50.904  1.00 21.25 ? 398 GLU A O   1 
ATOM   3372 C CB  . GLU A 1 398 ? 13.635  23.222 49.590  1.00 25.99 ? 398 GLU A CB  1 
ATOM   3373 C CG  . GLU A 1 398 ? 15.018  23.833 49.808  1.00 37.95 ? 398 GLU A CG  1 
ATOM   3374 C CD  . GLU A 1 398 ? 15.903  23.718 48.572  1.00 52.19 ? 398 GLU A CD  1 
ATOM   3375 O OE1 . GLU A 1 398 ? 15.851  24.629 47.721  1.00 57.58 ? 398 GLU A OE1 1 
ATOM   3376 O OE2 . GLU A 1 398 ? 16.632  22.713 48.438  1.00 51.37 ? 398 GLU A OE2 1 
ATOM   3377 N N   . VAL A 1 399 ? 15.583  20.737 50.127  1.00 22.14 ? 399 VAL A N   1 
ATOM   3378 C CA  . VAL A 1 399 ? 16.277  19.921 51.123  1.00 26.45 ? 399 VAL A CA  1 
ATOM   3379 C C   . VAL A 1 399 ? 16.809  20.836 52.215  1.00 26.18 ? 399 VAL A C   1 
ATOM   3380 O O   . VAL A 1 399 ? 17.352  21.907 51.930  1.00 29.41 ? 399 VAL A O   1 
ATOM   3381 C CB  . VAL A 1 399 ? 17.416  19.112 50.469  1.00 29.59 ? 399 VAL A CB  1 
ATOM   3382 C CG1 . VAL A 1 399 ? 18.154  18.250 51.525  1.00 31.25 ? 399 VAL A CG1 1 
ATOM   3383 C CG2 . VAL A 1 399 ? 16.859  18.248 49.347  1.00 33.00 ? 399 VAL A CG2 1 
ATOM   3384 N N   . ILE A 1 400 ? 16.658  20.422 53.470  1.00 23.61 ? 400 ILE A N   1 
ATOM   3385 C CA  . ILE A 1 400 ? 17.284  21.117 54.585  1.00 20.81 ? 400 ILE A CA  1 
ATOM   3386 C C   . ILE A 1 400 ? 18.082  20.102 55.381  1.00 19.08 ? 400 ILE A C   1 
ATOM   3387 O O   . ILE A 1 400 ? 17.664  18.946 55.529  1.00 20.88 ? 400 ILE A O   1 
ATOM   3388 C CB  . ILE A 1 400 ? 16.257  21.840 55.483  1.00 24.34 ? 400 ILE A CB  1 
ATOM   3389 C CG1 . ILE A 1 400 ? 15.116  20.904 55.873  1.00 26.66 ? 400 ILE A CG1 1 
ATOM   3390 C CG2 . ILE A 1 400 ? 15.738  23.092 54.763  1.00 34.27 ? 400 ILE A CG2 1 
ATOM   3391 C CD1 . ILE A 1 400 ? 14.112  21.537 56.804  1.00 32.60 ? 400 ILE A CD1 1 
ATOM   3392 N N   . GLU A 1 401 ? 19.224  20.535 55.902  1.00 17.73 ? 401 GLU A N   1 
ATOM   3393 C CA  . GLU A 1 401 ? 20.137  19.616 56.564  1.00 18.57 ? 401 GLU A CA  1 
ATOM   3394 C C   . GLU A 1 401 ? 20.233  19.815 58.067  1.00 19.41 ? 401 GLU A C   1 
ATOM   3395 O O   . GLU A 1 401 ? 20.788  18.944 58.742  1.00 20.09 ? 401 GLU A O   1 
ATOM   3396 C CB  . GLU A 1 401 ? 21.540  19.716 55.953  1.00 29.25 ? 401 GLU A CB  1 
ATOM   3397 C CG  . GLU A 1 401 ? 21.579  19.500 54.440  1.00 33.40 ? 401 GLU A CG  1 
ATOM   3398 C CD  . GLU A 1 401 ? 21.284  18.069 54.009  1.00 40.26 ? 401 GLU A CD  1 
ATOM   3399 O OE1 . GLU A 1 401 ? 21.274  17.157 54.860  1.00 40.62 ? 401 GLU A OE1 1 
ATOM   3400 O OE2 . GLU A 1 401 ? 21.071  17.858 52.799  1.00 43.17 ? 401 GLU A OE2 1 
ATOM   3401 N N   . SER A 1 402 ? 19.708  20.913 58.616  1.00 23.43 ? 402 SER A N   1 
ATOM   3402 C CA  . SER A 1 402 ? 19.813  21.136 60.058  1.00 23.96 ? 402 SER A CA  1 
ATOM   3403 C C   . SER A 1 402 ? 18.740  22.137 60.478  1.00 22.07 ? 402 SER A C   1 
ATOM   3404 O O   . SER A 1 402 ? 18.456  23.086 59.744  1.00 19.00 ? 402 SER A O   1 
ATOM   3405 C CB  . SER A 1 402 ? 21.217  21.651 60.435  1.00 19.52 ? 402 SER A CB  1 
ATOM   3406 O OG  . SER A 1 402 ? 21.357  21.801 61.846  1.00 21.57 ? 402 SER A OG  1 
ATOM   3407 N N   . VAL A 1 403 ? 18.136  21.917 61.649  1.00 20.05 ? 403 VAL A N   1 
ATOM   3408 C CA  . VAL A 1 403 ? 17.189  22.876 62.213  1.00 16.63 ? 403 VAL A CA  1 
ATOM   3409 C C   . VAL A 1 403 ? 17.706  23.294 63.579  1.00 22.65 ? 403 VAL A C   1 
ATOM   3410 O O   . VAL A 1 403 ? 18.463  22.564 64.230  1.00 23.05 ? 403 VAL A O   1 
ATOM   3411 C CB  . VAL A 1 403 ? 15.747  22.329 62.329  1.00 19.46 ? 403 VAL A CB  1 
ATOM   3412 C CG1 . VAL A 1 403 ? 15.220  21.881 60.953  1.00 17.82 ? 403 VAL A CG1 1 
ATOM   3413 C CG2 . VAL A 1 403 ? 15.647  21.201 63.357  1.00 21.19 ? 403 VAL A CG2 1 
ATOM   3414 N N   . LYS A 1 404 ? 17.304  24.487 64.011  1.00 19.67 ? 404 LYS A N   1 
ATOM   3415 C CA  . LYS A 1 404 ? 17.586  24.929 65.369  1.00 19.73 ? 404 LYS A CA  1 
ATOM   3416 C C   . LYS A 1 404 ? 16.420  24.495 66.240  1.00 19.64 ? 404 LYS A C   1 
ATOM   3417 O O   . LYS A 1 404 ? 15.262  24.830 65.945  1.00 24.94 ? 404 LYS A O   1 
ATOM   3418 C CB  . LYS A 1 404 ? 17.774  26.443 65.451  1.00 24.54 ? 404 LYS A CB  1 
ATOM   3419 C CG  . LYS A 1 404 ? 19.199  26.918 65.310  1.00 46.37 ? 404 LYS A CG  1 
ATOM   3420 C CD  . LYS A 1 404 ? 19.368  28.285 65.960  1.00 50.79 ? 404 LYS A CD  1 
ATOM   3421 C CE  . LYS A 1 404 ? 20.798  28.777 65.842  1.00 54.22 ? 404 LYS A CE  1 
ATOM   3422 N NZ  . LYS A 1 404 ? 21.153  29.110 64.438  1.00 59.18 ? 404 LYS A NZ  1 
ATOM   3423 N N   . ALA A 1 405 ? 16.727  23.757 67.304  1.00 16.50 ? 405 ALA A N   1 
ATOM   3424 C CA  . ALA A 1 405 ? 15.699  23.211 68.175  1.00 16.99 ? 405 ALA A CA  1 
ATOM   3425 C C   . ALA A 1 405 ? 14.809  24.317 68.726  1.00 15.81 ? 405 ALA A C   1 
ATOM   3426 O O   . ALA A 1 405 ? 15.287  25.388 69.109  1.00 16.45 ? 405 ALA A O   1 
ATOM   3427 C CB  . ALA A 1 405 ? 16.353  22.443 69.331  1.00 17.11 ? 405 ALA A CB  1 
ATOM   3428 N N   . GLY A 1 406 ? 13.512  24.053 68.784  1.00 18.13 ? 406 GLY A N   1 
ATOM   3429 C CA  . GLY A 1 406 ? 12.605  25.047 69.338  1.00 16.94 ? 406 GLY A CA  1 
ATOM   3430 C C   . GLY A 1 406 ? 11.181  24.550 69.357  1.00 18.71 ? 406 GLY A C   1 
ATOM   3431 O O   . GLY A 1 406 ? 10.914  23.366 69.142  1.00 13.70 ? 406 GLY A O   1 
ATOM   3432 N N   . THR A 1 407 ? 10.268  25.485 69.647  1.00 15.34 ? 407 THR A N   1 
ATOM   3433 C CA  . THR A 1 407 ? 8.835   25.228 69.697  1.00 15.93 ? 407 THR A CA  1 
ATOM   3434 C C   . THR A 1 407 ? 8.121   26.381 69.016  1.00 15.44 ? 407 THR A C   1 
ATOM   3435 O O   . THR A 1 407 ? 8.734   27.384 68.651  1.00 17.46 ? 407 THR A O   1 
ATOM   3436 C CB  . THR A 1 407 ? 8.286   25.115 71.135  1.00 14.14 ? 407 THR A CB  1 
ATOM   3437 O OG1 . THR A 1 407 ? 8.239   26.428 71.710  1.00 16.45 ? 407 THR A OG1 1 
ATOM   3438 C CG2 . THR A 1 407 ? 9.146   24.171 72.012  1.00 14.65 ? 407 THR A CG2 1 
ATOM   3439 N N   . TRP A 1 408 ? 6.805   26.260 68.873  1.00 13.69 ? 408 TRP A N   1 
ATOM   3440 C CA  . TRP A 1 408 ? 6.058   27.373 68.304  1.00 14.31 ? 408 TRP A CA  1 
ATOM   3441 C C   . TRP A 1 408 ? 5.792   28.489 69.313  1.00 15.27 ? 408 TRP A C   1 
ATOM   3442 O O   . TRP A 1 408 ? 5.126   29.464 68.972  1.00 18.36 ? 408 TRP A O   1 
ATOM   3443 C CB  . TRP A 1 408 ? 4.750   26.873 67.674  1.00 17.09 ? 408 TRP A CB  1 
ATOM   3444 C CG  . TRP A 1 408 ? 3.698   26.227 68.578  1.00 15.46 ? 408 TRP A CG  1 
ATOM   3445 C CD1 . TRP A 1 408 ? 3.707   26.106 69.944  1.00 16.90 ? 408 TRP A CD1 1 
ATOM   3446 C CD2 . TRP A 1 408 ? 2.474   25.629 68.130  1.00 14.07 ? 408 TRP A CD2 1 
ATOM   3447 N NE1 . TRP A 1 408 ? 2.543   25.467 70.374  1.00 14.76 ? 408 TRP A NE1 1 
ATOM   3448 C CE2 . TRP A 1 408 ? 1.783   25.165 69.271  1.00 14.83 ? 408 TRP A CE2 1 
ATOM   3449 C CE3 . TRP A 1 408 ? 1.895   25.434 66.856  1.00 15.09 ? 408 TRP A CE3 1 
ATOM   3450 C CZ2 . TRP A 1 408 ? 0.543   24.527 69.180  1.00 17.63 ? 408 TRP A CZ2 1 
ATOM   3451 C CZ3 . TRP A 1 408 ? 0.685   24.808 66.769  1.00 18.39 ? 408 TRP A CZ3 1 
ATOM   3452 C CH2 . TRP A 1 408 ? 0.008   24.362 67.929  1.00 16.49 ? 408 TRP A CH2 1 
ATOM   3453 N N   . PHE A 1 409 ? 6.273   28.371 70.545  1.00 17.09 ? 409 PHE A N   1 
ATOM   3454 C CA  . PHE A 1 409 ? 6.144   29.440 71.535  1.00 15.70 ? 409 PHE A CA  1 
ATOM   3455 C C   . PHE A 1 409 ? 7.488   30.171 71.573  1.00 22.50 ? 409 PHE A C   1 
ATOM   3456 O O   . PHE A 1 409 ? 8.440   29.694 72.192  1.00 22.80 ? 409 PHE A O   1 
ATOM   3457 C CB  . PHE A 1 409 ? 5.756   28.859 72.898  1.00 16.55 ? 409 PHE A CB  1 
ATOM   3458 C CG  . PHE A 1 409 ? 5.173   29.875 73.853  1.00 23.11 ? 409 PHE A CG  1 
ATOM   3459 C CD1 . PHE A 1 409 ? 5.903   30.995 74.230  1.00 28.26 ? 409 PHE A CD1 1 
ATOM   3460 C CD2 . PHE A 1 409 ? 3.902   29.699 74.377  1.00 26.20 ? 409 PHE A CD2 1 
ATOM   3461 C CE1 . PHE A 1 409 ? 5.372   31.931 75.096  1.00 35.04 ? 409 PHE A CE1 1 
ATOM   3462 C CE2 . PHE A 1 409 ? 3.364   30.637 75.262  1.00 29.38 ? 409 PHE A CE2 1 
ATOM   3463 C CZ  . PHE A 1 409 ? 4.097   31.751 75.613  1.00 24.93 ? 409 PHE A CZ  1 
ATOM   3464 N N   . ASP A 1 410 ? 7.566   31.316 70.887  1.00 20.91 ? 410 ASP A N   1 
ATOM   3465 C CA  . ASP A 1 410 ? 8.780   32.147 70.799  1.00 29.95 ? 410 ASP A CA  1 
ATOM   3466 C C   . ASP A 1 410 ? 9.996   31.406 70.228  1.00 27.33 ? 410 ASP A C   1 
ATOM   3467 O O   . ASP A 1 410 ? 11.133  31.878 70.383  1.00 26.25 ? 410 ASP A O   1 
ATOM   3468 C CB  . ASP A 1 410 ? 9.164   32.742 72.166  1.00 31.92 ? 410 ASP A CB  1 
ATOM   3469 C CG  . ASP A 1 410 ? 8.129   33.722 72.699  1.00 43.95 ? 410 ASP A CG  1 
ATOM   3470 O OD1 . ASP A 1 410 ? 7.389   34.314 71.882  1.00 43.85 ? 410 ASP A OD1 1 
ATOM   3471 O OD2 . ASP A 1 410 ? 8.061   33.898 73.942  1.00 40.23 ? 410 ASP A OD2 1 
ATOM   3472 N N   . GLY A 1 411 ? 9.803   30.268 69.565  1.00 19.31 ? 411 GLY A N   1 
ATOM   3473 C CA  . GLY A 1 411 ? 10.908  29.471 69.058  1.00 19.43 ? 411 GLY A CA  1 
ATOM   3474 C C   . GLY A 1 411 ? 11.782  28.804 70.098  1.00 24.87 ? 411 GLY A C   1 
ATOM   3475 O O   . GLY A 1 411 ? 12.851  28.294 69.743  1.00 22.48 ? 411 GLY A O   1 
ATOM   3476 N N   . ASN A 1 412 ? 11.377  28.784 71.376  1.00 18.61 ? 412 ASN A N   1 
ATOM   3477 C CA  . ASN A 1 412 ? 12.275  28.307 72.436  1.00 16.49 ? 412 ASN A CA  1 
ATOM   3478 C C   . ASN A 1 412 ? 11.484  27.462 73.435  1.00 17.65 ? 412 ASN A C   1 
ATOM   3479 O O   . ASN A 1 412 ? 10.274  27.249 73.277  1.00 18.50 ? 412 ASN A O   1 
ATOM   3480 C CB  . ASN A 1 412 ? 13.032  29.481 73.095  1.00 17.44 ? 412 ASN A CB  1 
ATOM   3481 C CG  . ASN A 1 412 ? 12.127  30.450 73.858  1.00 16.73 ? 412 ASN A CG  1 
ATOM   3482 O OD1 . ASN A 1 412 ? 11.254  30.043 74.618  1.00 20.33 ? 412 ASN A OD1 1 
ATOM   3483 N ND2 . ASN A 1 412 ? 12.376  31.760 73.682  1.00 24.37 ? 412 ASN A ND2 1 
ATOM   3484 N N   . PHE A 1 413 ? 12.170  27.002 74.489  1.00 14.21 ? 413 PHE A N   1 
ATOM   3485 C CA  . PHE A 1 413 ? 11.575  26.069 75.440  1.00 14.17 ? 413 PHE A CA  1 
ATOM   3486 C C   . PHE A 1 413 ? 11.238  26.703 76.787  1.00 17.41 ? 413 PHE A C   1 
ATOM   3487 O O   . PHE A 1 413 ? 10.913  25.969 77.734  1.00 16.41 ? 413 PHE A O   1 
ATOM   3488 C CB  . PHE A 1 413 ? 12.500  24.868 75.654  1.00 14.54 ? 413 PHE A CB  1 
ATOM   3489 C CG  . PHE A 1 413 ? 12.675  24.021 74.442  1.00 15.44 ? 413 PHE A CG  1 
ATOM   3490 C CD1 . PHE A 1 413 ? 11.783  22.979 74.168  1.00 13.87 ? 413 PHE A CD1 1 
ATOM   3491 C CD2 . PHE A 1 413 ? 13.730  24.253 73.553  1.00 20.32 ? 413 PHE A CD2 1 
ATOM   3492 C CE1 . PHE A 1 413 ? 11.952  22.177 73.027  1.00 16.08 ? 413 PHE A CE1 1 
ATOM   3493 C CE2 . PHE A 1 413 ? 13.889  23.465 72.412  1.00 15.76 ? 413 PHE A CE2 1 
ATOM   3494 C CZ  . PHE A 1 413 ? 13.004  22.427 72.157  1.00 16.83 ? 413 PHE A CZ  1 
ATOM   3495 N N   . LEU A 1 414 ? 11.270  28.032 76.893  1.00 16.33 ? 414 LEU A N   1 
ATOM   3496 C CA  . LEU A 1 414 ? 11.159  28.677 78.201  1.00 19.67 ? 414 LEU A CA  1 
ATOM   3497 C C   . LEU A 1 414 ? 9.801   28.467 78.863  1.00 16.39 ? 414 LEU A C   1 
ATOM   3498 O O   . LEU A 1 414 ? 9.698   28.638 80.088  1.00 17.60 ? 414 LEU A O   1 
ATOM   3499 C CB  . LEU A 1 414 ? 11.454  30.180 78.075  1.00 20.86 ? 414 LEU A CB  1 
ATOM   3500 C CG  . LEU A 1 414 ? 12.892  30.561 77.719  1.00 26.21 ? 414 LEU A CG  1 
ATOM   3501 C CD1 . LEU A 1 414 ? 13.035  32.081 77.661  1.00 26.98 ? 414 LEU A CD1 1 
ATOM   3502 C CD2 . LEU A 1 414 ? 13.895  29.965 78.710  1.00 22.04 ? 414 LEU A CD2 1 
ATOM   3503 N N   . LYS A 1 415 ? 8.754   28.100 78.102  1.00 16.74 ? 415 LYS A N   1 
ATOM   3504 C CA  . LYS A 1 415 ? 7.460   27.839 78.737  1.00 15.43 ? 415 LYS A CA  1 
ATOM   3505 C C   . LYS A 1 415 ? 7.434   26.533 79.514  1.00 14.99 ? 415 LYS A C   1 
ATOM   3506 O O   . LYS A 1 415 ? 6.473   26.301 80.263  1.00 17.81 ? 415 LYS A O   1 
ATOM   3507 C CB  . LYS A 1 415 ? 6.315   27.800 77.704  1.00 16.63 ? 415 LYS A CB  1 
ATOM   3508 C CG  . LYS A 1 415 ? 5.735   29.156 77.368  1.00 27.45 ? 415 LYS A CG  1 
ATOM   3509 C CD  . LYS A 1 415 ? 5.012   29.783 78.581  1.00 31.59 ? 415 LYS A CD  1 
ATOM   3510 C CE  . LYS A 1 415 ? 3.800   28.949 78.998  1.00 34.82 ? 415 LYS A CE  1 
ATOM   3511 N NZ  . LYS A 1 415 ? 2.962   29.589 80.060  1.00 37.60 ? 415 LYS A NZ  1 
ATOM   3512 N N   . TRP A 1 416 ? 8.429   25.671 79.338  1.00 14.40 ? 416 TRP A N   1 
ATOM   3513 C CA  . TRP A 1 416 ? 8.451   24.376 80.010  1.00 14.00 ? 416 TRP A CA  1 
ATOM   3514 C C   . TRP A 1 416 ? 9.674   24.143 80.883  1.00 13.88 ? 416 TRP A C   1 
ATOM   3515 O O   . TRP A 1 416 ? 9.707   23.137 81.607  1.00 14.77 ? 416 TRP A O   1 
ATOM   3516 C CB  . TRP A 1 416 ? 8.349   23.241 78.980  1.00 13.47 ? 416 TRP A CB  1 
ATOM   3517 C CG  . TRP A 1 416 ? 7.116   23.393 78.133  1.00 15.12 ? 416 TRP A CG  1 
ATOM   3518 C CD1 . TRP A 1 416 ? 5.888   22.881 78.393  1.00 12.86 ? 416 TRP A CD1 1 
ATOM   3519 C CD2 . TRP A 1 416 ? 7.005   24.128 76.909  1.00 12.88 ? 416 TRP A CD2 1 
ATOM   3520 N NE1 . TRP A 1 416 ? 4.997   23.255 77.403  1.00 14.00 ? 416 TRP A NE1 1 
ATOM   3521 C CE2 . TRP A 1 416 ? 5.667   24.022 76.479  1.00 12.93 ? 416 TRP A CE2 1 
ATOM   3522 C CE3 . TRP A 1 416 ? 7.910   24.872 76.144  1.00 17.88 ? 416 TRP A CE3 1 
ATOM   3523 C CZ2 . TRP A 1 416 ? 5.209   24.626 75.306  1.00 17.11 ? 416 TRP A CZ2 1 
ATOM   3524 C CZ3 . TRP A 1 416 ? 7.459   25.479 74.982  1.00 20.68 ? 416 TRP A CZ3 1 
ATOM   3525 C CH2 . TRP A 1 416 ? 6.115   25.346 74.569  1.00 17.22 ? 416 TRP A CH2 1 
ATOM   3526 N N   . ILE A 1 417 ? 10.682  25.012 80.820  1.00 15.95 ? 417 ILE A N   1 
ATOM   3527 C CA  . ILE A 1 417 ? 11.927  24.814 81.555  1.00 16.82 ? 417 ILE A CA  1 
ATOM   3528 C C   . ILE A 1 417 ? 12.606  26.172 81.688  1.00 17.78 ? 417 ILE A C   1 
ATOM   3529 O O   . ILE A 1 417 ? 12.339  27.096 80.914  1.00 23.80 ? 417 ILE A O   1 
ATOM   3530 C CB  . ILE A 1 417 ? 12.827  23.755 80.856  1.00 14.00 ? 417 ILE A CB  1 
ATOM   3531 C CG1 . ILE A 1 417 ? 13.904  23.233 81.819  1.00 15.85 ? 417 ILE A CG1 1 
ATOM   3532 C CG2 . ILE A 1 417 ? 13.455  24.274 79.563  1.00 16.10 ? 417 ILE A CG2 1 
ATOM   3533 C CD1 . ILE A 1 417 ? 14.615  21.980 81.309  1.00 15.19 ? 417 ILE A CD1 1 
ATOM   3534 N N   . GLY A 1 418 ? 13.447  26.326 82.714  1.00 17.89 ? 418 GLY A N   1 
ATOM   3535 C CA  . GLY A 1 418 ? 14.304  27.493 82.835  1.00 23.51 ? 418 GLY A CA  1 
ATOM   3536 C C   . GLY A 1 418 ? 14.048  28.401 84.021  1.00 28.24 ? 418 GLY A C   1 
ATOM   3537 O O   . GLY A 1 418 ? 14.929  29.195 84.360  1.00 41.25 ? 418 GLY A O   1 
ATOM   3538 N N   . ASN A 1 419 ? 12.892  28.350 84.671  1.00 26.54 ? 419 ASN A N   1 
ATOM   3539 C CA  . ASN A 1 419 ? 12.757  29.121 85.902  1.00 26.25 ? 419 ASN A CA  1 
ATOM   3540 C C   . ASN A 1 419 ? 12.747  28.171 87.097  1.00 26.15 ? 419 ASN A C   1 
ATOM   3541 O O   . ASN A 1 419 ? 12.697  26.947 86.942  1.00 22.98 ? 419 ASN A O   1 
ATOM   3542 C CB  . ASN A 1 419 ? 11.525  30.045 85.858  1.00 22.04 ? 419 ASN A CB  1 
ATOM   3543 C CG  . ASN A 1 419 ? 10.198  29.319 86.043  1.00 29.47 ? 419 ASN A CG  1 
ATOM   3544 O OD1 . ASN A 1 419 ? 10.140  28.157 86.439  1.00 27.48 ? 419 ASN A OD1 1 
ATOM   3545 N ND2 . ASN A 1 419 ? 9.108   30.029 85.759  1.00 30.27 ? 419 ASN A ND2 1 
ATOM   3546 N N   . LYS A 1 420 ? 12.801  28.745 88.304  1.00 24.18 ? 420 LYS A N   1 
ATOM   3547 C CA  . LYS A 1 420 ? 12.988  27.901 89.482  1.00 21.56 ? 420 LYS A CA  1 
ATOM   3548 C C   . LYS A 1 420 ? 11.891  26.852 89.597  1.00 26.30 ? 420 LYS A C   1 
ATOM   3549 O O   . LYS A 1 420 ? 12.182  25.670 89.834  1.00 24.50 ? 420 LYS A O   1 
ATOM   3550 C CB  . LYS A 1 420 ? 13.050  28.740 90.768  1.00 22.05 ? 420 LYS A CB  1 
ATOM   3551 C CG  . LYS A 1 420 ? 13.469  27.879 91.951  1.00 36.44 ? 420 LYS A CG  1 
ATOM   3552 C CD  . LYS A 1 420 ? 13.744  28.684 93.230  1.00 46.36 ? 420 LYS A CD  1 
ATOM   3553 C CE  . LYS A 1 420 ? 14.257  27.771 94.341  1.00 48.70 ? 420 LYS A CE  1 
ATOM   3554 N NZ  . LYS A 1 420 ? 14.176  28.402 95.695  1.00 49.19 ? 420 LYS A NZ  1 
ATOM   3555 N N   . GLU A 1 421 ? 10.627  27.254 89.382  1.00 24.25 ? 421 GLU A N   1 
ATOM   3556 C CA  . GLU A 1 421 ? 9.504   26.346 89.624  1.00 27.12 ? 421 GLU A CA  1 
ATOM   3557 C C   . GLU A 1 421 ? 9.400   25.269 88.550  1.00 20.04 ? 421 GLU A C   1 
ATOM   3558 O O   . GLU A 1 421 ? 9.139   24.102 88.858  1.00 19.65 ? 421 GLU A O   1 
ATOM   3559 C CB  . GLU A 1 421 ? 8.191   27.126 89.707  1.00 27.43 ? 421 GLU A CB  1 
ATOM   3560 C CG  . GLU A 1 421 ? 8.058   28.011 90.939  1.00 28.99 ? 421 GLU A CG  1 
ATOM   3561 C CD  . GLU A 1 421 ? 8.679   29.379 90.729  1.00 46.81 ? 421 GLU A CD  1 
ATOM   3562 O OE1 . GLU A 1 421 ? 8.999   29.726 89.568  1.00 44.78 ? 421 GLU A OE1 1 
ATOM   3563 O OE2 . GLU A 1 421 ? 8.869   30.104 91.731  1.00 47.69 ? 421 GLU A OE2 1 
ATOM   3564 N N   . LYS A 1 422 ? 9.560   25.639 87.285  1.00 17.98 ? 422 LYS A N   1 
ATOM   3565 C CA  . LYS A 1 422 ? 9.537   24.621 86.240  1.00 19.71 ? 422 LYS A CA  1 
ATOM   3566 C C   . LYS A 1 422 ? 10.740  23.685 86.359  1.00 17.53 ? 422 LYS A C   1 
ATOM   3567 O O   . LYS A 1 422 ? 10.613  22.475 86.131  1.00 15.52 ? 422 LYS A O   1 
ATOM   3568 C CB  . LYS A 1 422 ? 9.498   25.283 84.861  1.00 20.78 ? 422 LYS A CB  1 
ATOM   3569 C CG  . LYS A 1 422 ? 8.230   26.112 84.607  1.00 18.55 ? 422 LYS A CG  1 
ATOM   3570 C CD  . LYS A 1 422 ? 8.299   26.834 83.234  1.00 20.27 ? 422 LYS A CD  1 
ATOM   3571 C CE  . LYS A 1 422 ? 7.216   27.913 83.113  1.00 21.88 ? 422 LYS A CE  1 
ATOM   3572 N NZ  . LYS A 1 422 ? 5.863   27.283 82.843  1.00 17.84 ? 422 LYS A NZ  1 
ATOM   3573 N N   . ASN A 1 423 ? 11.900  24.226 86.734  1.00 18.19 ? 423 ASN A N   1 
ATOM   3574 C CA  . ASN A 1 423 ? 13.084  23.391 86.952  1.00 17.38 ? 423 ASN A CA  1 
ATOM   3575 C C   . ASN A 1 423 ? 12.873  22.406 88.094  1.00 17.29 ? 423 ASN A C   1 
ATOM   3576 O O   . ASN A 1 423 ? 13.349  21.269 88.035  1.00 21.76 ? 423 ASN A O   1 
ATOM   3577 C CB  . ASN A 1 423 ? 14.312  24.266 87.213  1.00 18.37 ? 423 ASN A CB  1 
ATOM   3578 C CG  . ASN A 1 423 ? 14.859  24.886 85.936  1.00 21.64 ? 423 ASN A CG  1 
ATOM   3579 O OD1 . ASN A 1 423 ? 14.351  24.618 84.838  1.00 22.32 ? 423 ASN A OD1 1 
ATOM   3580 N ND2 . ASN A 1 423 ? 15.911  25.691 86.067  1.00 22.79 ? 423 ASN A ND2 1 
ATOM   3581 N N   . GLU A 1 424 ? 12.160  22.816 89.143  1.00 17.54 ? 424 GLU A N   1 
ATOM   3582 C CA  . GLU A 1 424 ? 11.865  21.876 90.218  1.00 17.91 ? 424 GLU A CA  1 
ATOM   3583 C C   . GLU A 1 424 ? 11.046  20.687 89.723  1.00 17.33 ? 424 GLU A C   1 
ATOM   3584 O O   . GLU A 1 424 ? 11.246  19.558 90.185  1.00 19.13 ? 424 GLU A O   1 
ATOM   3585 C CB  . GLU A 1 424 ? 11.154  22.592 91.374  1.00 23.26 ? 424 GLU A CB  1 
ATOM   3586 C CG  . GLU A 1 424 ? 10.632  21.663 92.485  1.00 25.82 ? 424 GLU A CG  1 
ATOM   3587 C CD  . GLU A 1 424 ? 11.736  21.059 93.365  1.00 38.23 ? 424 GLU A CD  1 
ATOM   3588 O OE1 . GLU A 1 424 ? 11.391  20.314 94.317  1.00 42.83 ? 424 GLU A OE1 1 
ATOM   3589 O OE2 . GLU A 1 424 ? 12.938  21.311 93.109  1.00 35.38 ? 424 GLU A OE2 1 
ATOM   3590 N N   . TYR A 1 425 ? 10.130  20.903 88.780  1.00 16.55 ? 425 TYR A N   1 
ATOM   3591 C CA  . TYR A 1 425 ? 9.403   19.763 88.224  1.00 16.96 ? 425 TYR A CA  1 
ATOM   3592 C C   . TYR A 1 425 ? 10.350  18.819 87.496  1.00 18.01 ? 425 TYR A C   1 
ATOM   3593 O O   . TYR A 1 425 ? 10.240  17.594 87.638  1.00 17.55 ? 425 TYR A O   1 
ATOM   3594 C CB  . TYR A 1 425 ? 8.304   20.227 87.264  1.00 18.27 ? 425 TYR A CB  1 
ATOM   3595 C CG  . TYR A 1 425 ? 6.928   20.362 87.849  1.00 17.65 ? 425 TYR A CG  1 
ATOM   3596 C CD1 . TYR A 1 425 ? 6.729   20.675 89.201  1.00 16.99 ? 425 TYR A CD1 1 
ATOM   3597 C CD2 . TYR A 1 425 ? 5.811   20.234 87.026  1.00 16.90 ? 425 TYR A CD2 1 
ATOM   3598 C CE1 . TYR A 1 425 ? 5.433   20.810 89.709  1.00 18.64 ? 425 TYR A CE1 1 
ATOM   3599 C CE2 . TYR A 1 425 ? 4.532   20.375 87.518  1.00 17.32 ? 425 TYR A CE2 1 
ATOM   3600 C CZ  . TYR A 1 425 ? 4.350   20.666 88.850  1.00 17.42 ? 425 TYR A CZ  1 
ATOM   3601 O OH  . TYR A 1 425 ? 3.069   20.805 89.306  1.00 18.00 ? 425 TYR A OH  1 
ATOM   3602 N N   . TRP A 1 426 ? 11.297  19.370 86.713  1.00 15.04 ? 426 TRP A N   1 
ATOM   3603 C CA  . TRP A 1 426 ? 12.263  18.509 86.037  1.00 16.65 ? 426 TRP A CA  1 
ATOM   3604 C C   . TRP A 1 426 ? 13.120  17.760 87.049  1.00 20.71 ? 426 TRP A C   1 
ATOM   3605 O O   . TRP A 1 426 ? 13.432  16.581 86.843  1.00 17.82 ? 426 TRP A O   1 
ATOM   3606 C CB  . TRP A 1 426 ? 13.140  19.318 85.073  1.00 22.03 ? 426 TRP A CB  1 
ATOM   3607 C CG  . TRP A 1 426 ? 12.383  19.704 83.815  1.00 19.70 ? 426 TRP A CG  1 
ATOM   3608 C CD1 . TRP A 1 426 ? 11.853  20.930 83.516  1.00 15.19 ? 426 TRP A CD1 1 
ATOM   3609 C CD2 . TRP A 1 426 ? 12.059  18.847 82.711  1.00 20.24 ? 426 TRP A CD2 1 
ATOM   3610 N NE1 . TRP A 1 426 ? 11.215  20.880 82.295  1.00 14.29 ? 426 TRP A NE1 1 
ATOM   3611 C CE2 . TRP A 1 426 ? 11.322  19.619 81.783  1.00 14.84 ? 426 TRP A CE2 1 
ATOM   3612 C CE3 . TRP A 1 426 ? 12.314  17.503 82.419  1.00 18.98 ? 426 TRP A CE3 1 
ATOM   3613 C CZ2 . TRP A 1 426 ? 10.840  19.092 80.573  1.00 18.14 ? 426 TRP A CZ2 1 
ATOM   3614 C CZ3 . TRP A 1 426 ? 11.840  16.978 81.212  1.00 19.56 ? 426 TRP A CZ3 1 
ATOM   3615 C CH2 . TRP A 1 426 ? 11.109  17.780 80.305  1.00 20.15 ? 426 TRP A CH2 1 
ATOM   3616 N N   . LYS A 1 427 ? 13.488  18.424 88.161  1.00 17.97 ? 427 LYS A N   1 
ATOM   3617 C CA  . LYS A 1 427 ? 14.270  17.756 89.204  1.00 18.84 ? 427 LYS A CA  1 
ATOM   3618 C C   . LYS A 1 427 ? 13.496  16.597 89.812  1.00 19.57 ? 427 LYS A C   1 
ATOM   3619 O O   . LYS A 1 427 ? 14.063  15.526 90.074  1.00 18.70 ? 427 LYS A O   1 
ATOM   3620 C CB  . LYS A 1 427 ? 14.651  18.749 90.312  1.00 17.71 ? 427 LYS A CB  1 
ATOM   3621 C CG  . LYS A 1 427 ? 15.764  19.716 89.990  1.00 39.21 ? 427 LYS A CG  1 
ATOM   3622 C CD  . LYS A 1 427 ? 16.140  20.537 91.233  1.00 41.77 ? 427 LYS A CD  1 
ATOM   3623 C CE  . LYS A 1 427 ? 16.378  21.996 90.881  1.00 52.30 ? 427 LYS A CE  1 
ATOM   3624 N NZ  . LYS A 1 427 ? 17.234  22.155 89.668  1.00 58.27 ? 427 LYS A NZ  1 
ATOM   3625 N N   . ILE A 1 428 ? 12.208  16.814 90.091  1.00 19.51 ? 428 ILE A N   1 
ATOM   3626 C CA  . ILE A 1 428 ? 11.366  15.748 90.626  1.00 18.13 ? 428 ILE A CA  1 
ATOM   3627 C C   . ILE A 1 428 ? 11.291  14.590 89.647  1.00 19.66 ? 428 ILE A C   1 
ATOM   3628 O O   . ILE A 1 428 ? 11.351  13.416 90.038  1.00 19.87 ? 428 ILE A O   1 
ATOM   3629 C CB  . ILE A 1 428 ? 9.963   16.291 90.952  1.00 21.73 ? 428 ILE A CB  1 
ATOM   3630 C CG1 . ILE A 1 428 ? 10.052  17.254 92.128  1.00 20.43 ? 428 ILE A CG1 1 
ATOM   3631 C CG2 . ILE A 1 428 ? 8.996   15.141 91.192  1.00 17.65 ? 428 ILE A CG2 1 
ATOM   3632 C CD1 . ILE A 1 428 ? 8.892   18.223 92.242  1.00 23.56 ? 428 ILE A CD1 1 
ATOM   3633 N N   . LEU A 1 429 ? 11.163  14.905 88.358  1.00 18.80 ? 429 LEU A N   1 
ATOM   3634 C CA  . LEU A 1 429 ? 11.069  13.870 87.342  1.00 18.59 ? 429 LEU A CA  1 
ATOM   3635 C C   . LEU A 1 429 ? 12.384  13.113 87.200  1.00 19.38 ? 429 LEU A C   1 
ATOM   3636 O O   . LEU A 1 429 ? 12.385  11.888 87.039  1.00 18.81 ? 429 LEU A O   1 
ATOM   3637 C CB  . LEU A 1 429 ? 10.649  14.506 86.015  1.00 15.89 ? 429 LEU A CB  1 
ATOM   3638 C CG  . LEU A 1 429 ? 10.444  13.527 84.853  1.00 17.83 ? 429 LEU A CG  1 
ATOM   3639 C CD1 . LEU A 1 429 ? 9.168   12.743 85.066  1.00 20.28 ? 429 LEU A CD1 1 
ATOM   3640 C CD2 . LEU A 1 429 ? 10.482  14.267 83.505  1.00 16.54 ? 429 LEU A CD2 1 
ATOM   3641 N N   . ILE A 1 430 ? 13.513  13.828 87.251  1.00 16.96 ? 430 ILE A N   1 
ATOM   3642 C CA  . ILE A 1 430 ? 14.817  13.175 87.143  1.00 15.90 ? 430 ILE A CA  1 
ATOM   3643 C C   . ILE A 1 430 ? 15.022  12.206 88.294  1.00 16.84 ? 430 ILE A C   1 
ATOM   3644 O O   . ILE A 1 430 ? 15.485  11.077 88.098  1.00 23.17 ? 430 ILE A O   1 
ATOM   3645 C CB  . ILE A 1 430 ? 15.943  14.223 87.090  1.00 16.29 ? 430 ILE A CB  1 
ATOM   3646 C CG1 . ILE A 1 430 ? 15.945  14.938 85.743  1.00 16.11 ? 430 ILE A CG1 1 
ATOM   3647 C CG2 . ILE A 1 430 ? 17.303  13.588 87.386  1.00 20.34 ? 430 ILE A CG2 1 
ATOM   3648 C CD1 . ILE A 1 430 ? 16.605  16.313 85.821  1.00 18.41 ? 430 ILE A CD1 1 
ATOM   3649 N N   . GLU A 1 431 ? 14.704  12.640 89.521  1.00 17.44 ? 431 GLU A N   1 
ATOM   3650 C CA  . GLU A 1 431 ? 14.888  11.760 90.671  1.00 22.32 ? 431 GLU A CA  1 
ATOM   3651 C C   . GLU A 1 431 ? 13.917  10.587 90.610  1.00 21.21 ? 431 GLU A C   1 
ATOM   3652 O O   . GLU A 1 431 ? 14.284  9.449  90.931  1.00 24.31 ? 431 GLU A O   1 
ATOM   3653 C CB  . GLU A 1 431 ? 14.708  12.559 91.963  1.00 30.09 ? 431 GLU A CB  1 
ATOM   3654 C CG  . GLU A 1 431 ? 15.077  11.811 93.237  1.00 51.40 ? 431 GLU A CG  1 
ATOM   3655 C CD  . GLU A 1 431 ? 16.410  11.083 93.149  1.00 55.66 ? 431 GLU A CD  1 
ATOM   3656 O OE1 . GLU A 1 431 ? 17.413  11.698 92.711  1.00 47.75 ? 431 GLU A OE1 1 
ATOM   3657 O OE2 . GLU A 1 431 ? 16.450  9.892  93.531  1.00 60.22 ? 431 GLU A OE2 1 
ATOM   3658 N N   . ALA A 1 432 ? 12.684  10.849 90.176  1.00 17.98 ? 432 ALA A N   1 
ATOM   3659 C CA  . ALA A 1 432 ? 11.686  9.790  90.057  1.00 20.22 ? 432 ALA A CA  1 
ATOM   3660 C C   . ALA A 1 432 ? 12.096  8.771  89.005  1.00 24.83 ? 432 ALA A C   1 
ATOM   3661 O O   . ALA A 1 432 ? 11.897  7.563  89.187  1.00 21.34 ? 432 ALA A O   1 
ATOM   3662 C CB  . ALA A 1 432 ? 10.329  10.386 89.703  1.00 20.19 ? 432 ALA A CB  1 
ATOM   3663 N N   . LYS A 1 433 ? 12.680  9.250  87.900  1.00 21.04 ? 433 LYS A N   1 
ATOM   3664 C CA  . LYS A 1 433 ? 13.072  8.370  86.804  1.00 19.94 ? 433 LYS A CA  1 
ATOM   3665 C C   . LYS A 1 433 ? 14.125  7.359  87.239  1.00 23.99 ? 433 LYS A C   1 
ATOM   3666 O O   . LYS A 1 433 ? 14.122  6.218  86.766  1.00 27.12 ? 433 LYS A O   1 
ATOM   3667 C CB  . LYS A 1 433 ? 13.587  9.203  85.630  1.00 19.39 ? 433 LYS A CB  1 
ATOM   3668 C CG  . LYS A 1 433 ? 14.251  8.359  84.540  1.00 23.44 ? 433 LYS A CG  1 
ATOM   3669 C CD  . LYS A 1 433 ? 13.223  7.574  83.733  1.00 24.15 ? 433 LYS A CD  1 
ATOM   3670 C CE  . LYS A 1 433 ? 13.910  6.775  82.625  1.00 22.07 ? 433 LYS A CE  1 
ATOM   3671 N NZ  . LYS A 1 433 ? 13.024  5.719  82.054  1.00 20.55 ? 433 LYS A NZ  1 
ATOM   3672 N N   . LYS A 1 434 ? 15.027  7.746  88.144  1.00 23.06 ? 434 LYS A N   1 
ATOM   3673 C CA  . LYS A 1 434 ? 16.026  6.798  88.612  1.00 28.41 ? 434 LYS A CA  1 
ATOM   3674 C C   . LYS A 1 434 ? 15.390  5.610  89.315  1.00 30.87 ? 434 LYS A C   1 
ATOM   3675 O O   . LYS A 1 434 ? 15.993  4.535  89.378  1.00 31.35 ? 434 LYS A O   1 
ATOM   3676 C CB  . LYS A 1 434 ? 17.012  7.469  89.564  1.00 28.84 ? 434 LYS A CB  1 
ATOM   3677 C CG  . LYS A 1 434 ? 17.377  8.883  89.242  1.00 27.45 ? 434 LYS A CG  1 
ATOM   3678 C CD  . LYS A 1 434 ? 18.503  9.344  90.158  1.00 38.66 ? 434 LYS A CD  1 
ATOM   3679 C CE  . LYS A 1 434 ? 18.939  10.767 89.860  1.00 40.92 ? 434 LYS A CE  1 
ATOM   3680 N NZ  . LYS A 1 434 ? 19.915  11.248 90.893  1.00 47.77 ? 434 LYS A NZ  1 
ATOM   3681 N N   . LYS A 1 435 ? 14.182  5.778  89.852  1.00 29.50 ? 435 LYS A N   1 
ATOM   3682 C CA  . LYS A 1 435 ? 13.534  4.722  90.622  1.00 32.70 ? 435 LYS A CA  1 
ATOM   3683 C C   . LYS A 1 435 ? 12.260  4.218  89.960  1.00 29.65 ? 435 LYS A C   1 
ATOM   3684 O O   . LYS A 1 435 ? 11.497  3.482  90.591  1.00 27.97 ? 435 LYS A O   1 
ATOM   3685 C CB  . LYS A 1 435 ? 13.232  5.218  92.044  1.00 33.39 ? 435 LYS A CB  1 
ATOM   3686 C CG  . LYS A 1 435 ? 14.432  5.857  92.719  1.00 42.09 ? 435 LYS A CG  1 
ATOM   3687 C CD  . LYS A 1 435 ? 14.237  6.001  94.210  1.00 53.51 ? 435 LYS A CD  1 
ATOM   3688 C CE  . LYS A 1 435 ? 13.592  7.330  94.561  1.00 56.87 ? 435 LYS A CE  1 
ATOM   3689 N NZ  . LYS A 1 435 ? 13.475  7.488  96.043  1.00 61.92 ? 435 LYS A NZ  1 
ATOM   3690 N N   . ALA A 1 436 ? 12.020  4.586  88.710  1.00 25.72 ? 436 ALA A N   1 
ATOM   3691 C CA  . ALA A 1 436 ? 10.731  4.333  88.087  1.00 20.60 ? 436 ALA A CA  1 
ATOM   3692 C C   . ALA A 1 436 ? 10.537  2.847  87.824  1.00 25.75 ? 436 ALA A C   1 
ATOM   3693 O O   . ALA A 1 436 ? 11.468  2.141  87.425  1.00 28.63 ? 436 ALA A O   1 
ATOM   3694 C CB  . ALA A 1 436 ? 10.611  5.121  86.786  1.00 25.36 ? 436 ALA A CB  1 
ATOM   3695 N N   . LYS A 1 437 ? 9.310   2.370  88.051  1.00 26.22 ? 437 LYS A N   1 
ATOM   3696 C CA  . LYS A 1 437 ? 8.998   0.964  87.883  1.00 27.42 ? 437 LYS A CA  1 
ATOM   3697 C C   . LYS A 1 437 ? 7.956   0.687  86.817  1.00 26.77 ? 437 LYS A C   1 
ATOM   3698 O O   . LYS A 1 437 ? 7.775   -0.478 86.457  1.00 29.87 ? 437 LYS A O   1 
ATOM   3699 C CB  . LYS A 1 437 ? 8.533   0.355  89.217  1.00 24.37 ? 437 LYS A CB  1 
ATOM   3700 C CG  . LYS A 1 437 ? 9.607   0.413  90.297  1.00 35.19 ? 437 LYS A CG  1 
ATOM   3701 C CD  . LYS A 1 437 ? 10.882  -0.274 89.839  1.00 45.82 ? 437 LYS A CD  1 
ATOM   3702 C CE  . LYS A 1 437 ? 11.985  -0.170 90.888  1.00 53.63 ? 437 LYS A CE  1 
ATOM   3703 N NZ  . LYS A 1 437 ? 13.101  -1.129 90.640  1.00 58.09 ? 437 LYS A NZ  1 
ATOM   3704 N N   . ASN A 1 438 ? 7.269   1.703  86.302  1.00 25.62 ? 438 ASN A N   1 
ATOM   3705 C CA  . ASN A 1 438 ? 6.183   1.490  85.359  1.00 20.52 ? 438 ASN A CA  1 
ATOM   3706 C C   . ASN A 1 438 ? 6.059   2.725  84.474  1.00 22.27 ? 438 ASN A C   1 
ATOM   3707 O O   . ASN A 1 438 ? 6.772   3.716  84.648  1.00 24.10 ? 438 ASN A O   1 
ATOM   3708 C CB  . ASN A 1 438 ? 4.879   1.193  86.093  1.00 19.84 ? 438 ASN A CB  1 
ATOM   3709 C CG  . ASN A 1 438 ? 4.511   2.288  87.083  1.00 24.76 ? 438 ASN A CG  1 
ATOM   3710 O OD1 . ASN A 1 438 ? 4.225   3.411  86.680  1.00 18.36 ? 438 ASN A OD1 1 
ATOM   3711 N ND2 . ASN A 1 438 ? 4.520   1.969  88.382  1.00 25.93 ? 438 ASN A ND2 1 
ATOM   3712 N N   . ASP A 1 439 ? 5.120   2.661  83.528  1.00 27.24 ? 439 ASP A N   1 
ATOM   3713 C CA  . ASP A 1 439 ? 4.895   3.686  82.513  1.00 25.23 ? 439 ASP A CA  1 
ATOM   3714 C C   . ASP A 1 439 ? 4.223   4.948  83.041  1.00 19.28 ? 439 ASP A C   1 
ATOM   3715 O O   . ASP A 1 439 ? 3.989   5.872  82.256  1.00 18.81 ? 439 ASP A O   1 
ATOM   3716 C CB  . ASP A 1 439 ? 4.053   3.106  81.372  1.00 25.36 ? 439 ASP A CB  1 
ATOM   3717 C CG  . ASP A 1 439 ? 4.870   2.251  80.433  1.00 34.25 ? 439 ASP A CG  1 
ATOM   3718 O OD1 . ASP A 1 439 ? 6.098   2.155  80.639  1.00 28.08 ? 439 ASP A OD1 1 
ATOM   3719 O OD2 . ASP A 1 439 ? 4.283   1.668  79.490  1.00 39.27 ? 439 ASP A OD2 1 
ATOM   3720 N N   . TYR A 1 440 ? 3.893   5.042  84.329  1.00 17.44 ? 440 TYR A N   1 
ATOM   3721 C CA  . TYR A 1 440 ? 3.428   6.332  84.813  1.00 16.40 ? 440 TYR A CA  1 
ATOM   3722 C C   . TYR A 1 440 ? 4.526   7.381  84.771  1.00 16.42 ? 440 TYR A C   1 
ATOM   3723 O O   . TYR A 1 440 ? 4.225   8.576  84.830  1.00 18.51 ? 440 TYR A O   1 
ATOM   3724 C CB  . TYR A 1 440 ? 2.858   6.193  86.240  1.00 15.82 ? 440 TYR A CB  1 
ATOM   3725 C CG  . TYR A 1 440 ? 1.387   5.845  86.223  1.00 20.78 ? 440 TYR A CG  1 
ATOM   3726 C CD1 . TYR A 1 440 ? 0.440   6.799  85.867  1.00 24.06 ? 440 TYR A CD1 1 
ATOM   3727 C CD2 . TYR A 1 440 ? 0.945   4.569  86.537  1.00 23.49 ? 440 TYR A CD2 1 
ATOM   3728 C CE1 . TYR A 1 440 ? -0.904  6.500  85.840  1.00 26.07 ? 440 TYR A CE1 1 
ATOM   3729 C CE2 . TYR A 1 440 ? -0.412  4.250  86.501  1.00 26.91 ? 440 TYR A CE2 1 
ATOM   3730 C CZ  . TYR A 1 440 ? -1.328  5.228  86.160  1.00 27.13 ? 440 TYR A CZ  1 
ATOM   3731 O OH  . TYR A 1 440 ? -2.670  4.944  86.132  1.00 29.22 ? 440 TYR A OH  1 
ATOM   3732 N N   . ILE A 1 441 ? 5.793   6.969  84.655  1.00 14.06 ? 441 ILE A N   1 
ATOM   3733 C CA  . ILE A 1 441 ? 6.853   7.943  84.435  1.00 17.12 ? 441 ILE A CA  1 
ATOM   3734 C C   . ILE A 1 441 ? 6.645   8.629  83.090  1.00 18.32 ? 441 ILE A C   1 
ATOM   3735 O O   . ILE A 1 441 ? 6.920   9.826  82.947  1.00 17.56 ? 441 ILE A O   1 
ATOM   3736 C CB  . ILE A 1 441 ? 8.245   7.262  84.559  1.00 16.69 ? 441 ILE A CB  1 
ATOM   3737 C CG1 . ILE A 1 441 ? 9.355   8.299  84.762  1.00 15.38 ? 441 ILE A CG1 1 
ATOM   3738 C CG2 . ILE A 1 441 ? 8.566   6.338  83.371  1.00 16.85 ? 441 ILE A CG2 1 
ATOM   3739 C CD1 . ILE A 1 441 ? 9.327   8.978  86.133  1.00 19.39 ? 441 ILE A CD1 1 
ATOM   3740 N N   . LEU A 1 442 ? 6.086   7.907  82.107  1.00 18.73 ? 442 LEU A N   1 
ATOM   3741 C CA  . LEU A 1 442 ? 5.810   8.512  80.806  1.00 15.65 ? 442 LEU A CA  1 
ATOM   3742 C C   . LEU A 1 442 ? 4.687   9.538  80.909  1.00 17.22 ? 442 LEU A C   1 
ATOM   3743 O O   . LEU A 1 442 ? 4.749   10.601 80.279  1.00 16.33 ? 442 LEU A O   1 
ATOM   3744 C CB  . LEU A 1 442 ? 5.461   7.431  79.776  1.00 14.74 ? 442 LEU A CB  1 
ATOM   3745 C CG  . LEU A 1 442 ? 6.421   6.255  79.593  1.00 18.54 ? 442 LEU A CG  1 
ATOM   3746 C CD1 . LEU A 1 442 ? 5.820   5.265  78.584  1.00 17.87 ? 442 LEU A CD1 1 
ATOM   3747 C CD2 . LEU A 1 442 ? 7.798   6.716  79.135  1.00 15.89 ? 442 LEU A CD2 1 
ATOM   3748 N N   . VAL A 1 443 ? 3.647   9.234  81.692  1.00 13.53 ? 443 VAL A N   1 
ATOM   3749 C CA  . VAL A 1 443 ? 2.574   10.199 81.912  1.00 13.20 ? 443 VAL A CA  1 
ATOM   3750 C C   . VAL A 1 443 ? 3.143   11.496 82.483  1.00 20.29 ? 443 VAL A C   1 
ATOM   3751 O O   . VAL A 1 443 ? 2.771   12.602 82.060  1.00 15.64 ? 443 VAL A O   1 
ATOM   3752 C CB  . VAL A 1 443 ? 1.497   9.595  82.840  1.00 12.64 ? 443 VAL A CB  1 
ATOM   3753 C CG1 . VAL A 1 443 ? 0.333   10.568 83.041  1.00 15.51 ? 443 VAL A CG1 1 
ATOM   3754 C CG2 . VAL A 1 443 ? 1.003   8.250  82.308  1.00 12.83 ? 443 VAL A CG2 1 
ATOM   3755 N N   . ALA A 1 444 ? 4.077   11.379 83.431  1.00 15.30 ? 444 ALA A N   1 
ATOM   3756 C CA  . ALA A 1 444 ? 4.671   12.551 84.069  1.00 15.38 ? 444 ALA A CA  1 
ATOM   3757 C C   . ALA A 1 444 ? 5.543   13.353 83.121  1.00 16.54 ? 444 ALA A C   1 
ATOM   3758 O O   . ALA A 1 444 ? 5.865   14.506 83.424  1.00 16.04 ? 444 ALA A O   1 
ATOM   3759 C CB  . ALA A 1 444 ? 5.512   12.120 85.271  1.00 13.74 ? 444 ALA A CB  1 
ATOM   3760 N N   . GLU A 1 445 ? 5.960   12.766 82.004  1.00 15.79 ? 445 GLU A N   1 
ATOM   3761 C CA  . GLU A 1 445 ? 6.791   13.492 81.045  1.00 15.31 ? 445 GLU A CA  1 
ATOM   3762 C C   . GLU A 1 445 ? 5.965   14.363 80.095  1.00 15.79 ? 445 GLU A C   1 
ATOM   3763 O O   . GLU A 1 445 ? 6.549   15.060 79.250  1.00 14.22 ? 445 GLU A O   1 
ATOM   3764 C CB  . GLU A 1 445 ? 7.670   12.498 80.261  1.00 16.70 ? 445 GLU A CB  1 
ATOM   3765 C CG  . GLU A 1 445 ? 8.858   11.926 81.087  1.00 14.50 ? 445 GLU A CG  1 
ATOM   3766 C CD  . GLU A 1 445 ? 9.380   10.582 80.591  1.00 22.99 ? 445 GLU A CD  1 
ATOM   3767 O OE1 . GLU A 1 445 ? 9.017   10.168 79.471  1.00 19.53 ? 445 GLU A OE1 1 
ATOM   3768 O OE2 . GLU A 1 445 ? 10.184  9.939  81.314  1.00 19.95 ? 445 GLU A OE2 1 
ATOM   3769 N N   . GLY A 1 446 ? 4.636   14.338 80.200  1.00 16.45 ? 446 GLY A N   1 
ATOM   3770 C CA  . GLY A 1 446 ? 3.809   15.200 79.360  1.00 12.83 ? 446 GLY A CA  1 
ATOM   3771 C C   . GLY A 1 446 ? 4.146   16.669 79.532  1.00 17.67 ? 446 GLY A C   1 
ATOM   3772 O O   . GLY A 1 446 ? 4.535   17.118 80.609  1.00 18.96 ? 446 GLY A O   1 
ATOM   3773 N N   . SER A 1 447 ? 4.017   17.429 78.441  1.00 16.60 ? 447 SER A N   1 
ATOM   3774 C CA  . SER A 1 447 ? 4.424   18.833 78.485  1.00 15.97 ? 447 SER A CA  1 
ATOM   3775 C C   . SER A 1 447 ? 3.501   19.668 79.368  1.00 17.77 ? 447 SER A C   1 
ATOM   3776 O O   . SER A 1 447 ? 3.934   20.689 79.934  1.00 15.62 ? 447 SER A O   1 
ATOM   3777 C CB  . SER A 1 447 ? 4.464   19.417 77.067  1.00 15.60 ? 447 SER A CB  1 
ATOM   3778 O OG  . SER A 1 447 ? 3.147   19.546 76.530  1.00 16.99 ? 447 SER A OG  1 
ATOM   3779 N N   . ASP A 1 448 ? 2.242   19.241 79.496  1.00 16.85 ? 448 ASP A N   1 
ATOM   3780 C CA  . ASP A 1 448 ? 1.221   20.051 80.165  1.00 16.03 ? 448 ASP A CA  1 
ATOM   3781 C C   . ASP A 1 448 ? 1.602   20.381 81.596  1.00 14.06 ? 448 ASP A C   1 
ATOM   3782 O O   . ASP A 1 448 ? 1.375   21.509 82.052  1.00 13.70 ? 448 ASP A O   1 
ATOM   3783 C CB  . ASP A 1 448 ? -0.121  19.329 80.140  1.00 15.28 ? 448 ASP A CB  1 
ATOM   3784 C CG  . ASP A 1 448 ? -0.540  18.962 78.743  1.00 14.26 ? 448 ASP A CG  1 
ATOM   3785 O OD1 . ASP A 1 448 ? -0.087  17.910 78.234  1.00 18.81 ? 448 ASP A OD1 1 
ATOM   3786 O OD2 . ASP A 1 448 ? -1.282  19.765 78.130  1.00 17.34 ? 448 ASP A OD2 1 
ATOM   3787 N N   . TRP A 1 449 ? 2.183   19.419 82.323  1.00 13.46 ? 449 TRP A N   1 
ATOM   3788 C CA  . TRP A 1 449 ? 2.503   19.667 83.735  1.00 12.69 ? 449 TRP A CA  1 
ATOM   3789 C C   . TRP A 1 449 ? 3.481   20.823 83.869  1.00 11.72 ? 449 TRP A C   1 
ATOM   3790 O O   . TRP A 1 449 ? 3.344   21.665 84.769  1.00 14.32 ? 449 TRP A O   1 
ATOM   3791 C CB  . TRP A 1 449 ? 3.084   18.405 84.396  1.00 13.44 ? 449 TRP A CB  1 
ATOM   3792 C CG  . TRP A 1 449 ? 2.397   17.162 83.965  1.00 11.33 ? 449 TRP A CG  1 
ATOM   3793 C CD1 . TRP A 1 449 ? 2.954   16.093 83.296  1.00 12.46 ? 449 TRP A CD1 1 
ATOM   3794 C CD2 . TRP A 1 449 ? 1.005   16.865 84.117  1.00 12.71 ? 449 TRP A CD2 1 
ATOM   3795 N NE1 . TRP A 1 449 ? 1.980   15.146 83.046  1.00 17.58 ? 449 TRP A NE1 1 
ATOM   3796 C CE2 . TRP A 1 449 ? 0.779   15.603 83.526  1.00 14.83 ? 449 TRP A CE2 1 
ATOM   3797 C CE3 . TRP A 1 449 ? -0.083  17.550 84.704  1.00 16.44 ? 449 TRP A CE3 1 
ATOM   3798 C CZ2 . TRP A 1 449 ? -0.469  15.005 83.511  1.00 15.17 ? 449 TRP A CZ2 1 
ATOM   3799 C CZ3 . TRP A 1 449 ? -1.322  16.957 84.678  1.00 15.23 ? 449 TRP A CZ3 1 
ATOM   3800 C CH2 . TRP A 1 449 ? -1.513  15.694 84.078  1.00 11.45 ? 449 TRP A CH2 1 
ATOM   3801 N N   . PHE A 1 450 ? 4.450   20.902 82.955  1.00 13.45 ? 450 PHE A N   1 
ATOM   3802 C CA  . PHE A 1 450 ? 5.473   21.942 83.010  1.00 13.02 ? 450 PHE A CA  1 
ATOM   3803 C C   . PHE A 1 450 ? 4.937   23.289 82.537  1.00 14.31 ? 450 PHE A C   1 
ATOM   3804 O O   . PHE A 1 450 ? 5.392   24.346 83.009  1.00 16.73 ? 450 PHE A O   1 
ATOM   3805 C CB  . PHE A 1 450 ? 6.686   21.502 82.180  1.00 14.87 ? 450 PHE A CB  1 
ATOM   3806 C CG  . PHE A 1 450 ? 7.253   20.182 82.609  1.00 13.74 ? 450 PHE A CG  1 
ATOM   3807 C CD1 . PHE A 1 450 ? 6.756   18.995 82.106  1.00 12.76 ? 450 PHE A CD1 1 
ATOM   3808 C CD2 . PHE A 1 450 ? 8.286   20.131 83.530  1.00 13.41 ? 450 PHE A CD2 1 
ATOM   3809 C CE1 . PHE A 1 450 ? 7.261   17.765 82.529  1.00 14.89 ? 450 PHE A CE1 1 
ATOM   3810 C CE2 . PHE A 1 450 ? 8.795   18.912 83.958  1.00 15.01 ? 450 PHE A CE2 1 
ATOM   3811 C CZ  . PHE A 1 450 ? 8.281   17.731 83.465  1.00 18.67 ? 450 PHE A CZ  1 
ATOM   3812 N N   . TRP A 1 451 ? 3.999   23.261 81.584  1.00 13.56 ? 451 TRP A N   1 
ATOM   3813 C CA  . TRP A 1 451 ? 3.374   24.480 81.085  1.00 14.49 ? 451 TRP A CA  1 
ATOM   3814 C C   . TRP A 1 451 ? 2.719   25.261 82.220  1.00 14.92 ? 451 TRP A C   1 
ATOM   3815 O O   . TRP A 1 451 ? 2.921   26.474 82.341  1.00 16.21 ? 451 TRP A O   1 
ATOM   3816 C CB  . TRP A 1 451 ? 2.350   24.108 80.003  1.00 14.23 ? 451 TRP A CB  1 
ATOM   3817 C CG  . TRP A 1 451 ? 1.439   25.221 79.550  1.00 18.91 ? 451 TRP A CG  1 
ATOM   3818 C CD1 . TRP A 1 451 ? 0.311   25.672 80.180  1.00 19.81 ? 451 TRP A CD1 1 
ATOM   3819 C CD2 . TRP A 1 451 ? 1.555   25.989 78.345  1.00 19.89 ? 451 TRP A CD2 1 
ATOM   3820 N NE1 . TRP A 1 451 ? -0.266  26.684 79.453  1.00 19.74 ? 451 TRP A NE1 1 
ATOM   3821 C CE2 . TRP A 1 451 ? 0.486   26.910 78.330  1.00 22.25 ? 451 TRP A CE2 1 
ATOM   3822 C CE3 . TRP A 1 451 ? 2.485   26.018 77.300  1.00 30.00 ? 451 TRP A CE3 1 
ATOM   3823 C CZ2 . TRP A 1 451 ? 0.302   27.833 77.297  1.00 29.30 ? 451 TRP A CZ2 1 
ATOM   3824 C CZ3 . TRP A 1 451 ? 2.298   26.935 76.265  1.00 42.03 ? 451 TRP A CZ3 1 
ATOM   3825 C CH2 . TRP A 1 451 ? 1.216   27.828 76.273  1.00 41.33 ? 451 TRP A CH2 1 
ATOM   3826 N N   . TRP A 1 452 ? 1.941   24.569 83.077  1.00 14.62 ? 452 TRP A N   1 
ATOM   3827 C CA  . TRP A 1 452 ? 1.172   25.239 84.127  1.00 14.74 ? 452 TRP A CA  1 
ATOM   3828 C C   . TRP A 1 452 ? 2.017   25.584 85.344  1.00 18.28 ? 452 TRP A C   1 
ATOM   3829 O O   . TRP A 1 452 ? 1.668   26.517 86.091  1.00 16.75 ? 452 TRP A O   1 
ATOM   3830 C CB  . TRP A 1 452 ? -0.006  24.351 84.556  1.00 13.98 ? 452 TRP A CB  1 
ATOM   3831 C CG  . TRP A 1 452 ? -0.949  24.133 83.428  1.00 14.55 ? 452 TRP A CG  1 
ATOM   3832 C CD1 . TRP A 1 452 ? -1.176  22.967 82.760  1.00 17.03 ? 452 TRP A CD1 1 
ATOM   3833 C CD2 . TRP A 1 452 ? -1.766  25.127 82.794  1.00 14.73 ? 452 TRP A CD2 1 
ATOM   3834 N NE1 . TRP A 1 452 ? -2.108  23.168 81.761  1.00 16.06 ? 452 TRP A NE1 1 
ATOM   3835 C CE2 . TRP A 1 452 ? -2.471  24.489 81.755  1.00 14.42 ? 452 TRP A CE2 1 
ATOM   3836 C CE3 . TRP A 1 452 ? -1.970  26.494 83.007  1.00 18.06 ? 452 TRP A CE3 1 
ATOM   3837 C CZ2 . TRP A 1 452 ? -3.381  25.169 80.936  1.00 15.92 ? 452 TRP A CZ2 1 
ATOM   3838 C CZ3 . TRP A 1 452 ? -2.867  27.169 82.196  1.00 19.97 ? 452 TRP A CZ3 1 
ATOM   3839 C CH2 . TRP A 1 452 ? -3.560  26.506 81.168  1.00 18.40 ? 452 TRP A CH2 1 
ATOM   3840 N N   . GLN A 1 453 ? 3.127   24.881 85.547  1.00 15.02 ? 453 GLN A N   1 
ATOM   3841 C CA  . GLN A 1 453 ? 3.950   25.111 86.732  1.00 15.91 ? 453 GLN A CA  1 
ATOM   3842 C C   . GLN A 1 453 ? 4.688   26.449 86.633  1.00 17.58 ? 453 GLN A C   1 
ATOM   3843 O O   . GLN A 1 453 ? 5.099   26.886 85.551  1.00 21.19 ? 453 GLN A O   1 
ATOM   3844 C CB  . GLN A 1 453 ? 4.953   23.953 86.893  1.00 16.85 ? 453 GLN A CB  1 
ATOM   3845 C CG  . GLN A 1 453 ? 6.097   24.185 87.881  1.00 20.18 ? 453 GLN A CG  1 
ATOM   3846 C CD  . GLN A 1 453 ? 5.636   24.115 89.322  1.00 24.52 ? 453 GLN A CD  1 
ATOM   3847 O OE1 . GLN A 1 453 ? 4.440   24.150 89.595  1.00 25.03 ? 453 GLN A OE1 1 
ATOM   3848 N NE2 . GLN A 1 453 ? 6.588   24.044 90.256  1.00 20.85 ? 453 GLN A NE2 1 
ATOM   3849 N N   . GLY A 1 454 ? 4.856   27.110 87.774  1.00 18.99 ? 454 GLY A N   1 
ATOM   3850 C CA  . GLY A 1 454 ? 5.686   28.293 87.794  1.00 25.05 ? 454 GLY A CA  1 
ATOM   3851 C C   . GLY A 1 454 ? 5.124   29.450 87.010  1.00 30.84 ? 454 GLY A C   1 
ATOM   3852 O O   . GLY A 1 454 ? 5.881   30.182 86.352  1.00 33.56 ? 454 GLY A O   1 
ATOM   3853 N N   . GLU A 1 455 ? 3.809   29.615 87.038  1.00 35.60 ? 455 GLU A N   1 
ATOM   3854 C CA  . GLU A 1 455 ? 3.132   30.781 86.499  1.00 38.57 ? 455 GLU A CA  1 
ATOM   3855 C C   . GLU A 1 455 ? 2.466   31.509 87.660  1.00 45.12 ? 455 GLU A C   1 
ATOM   3856 O O   . GLU A 1 455 ? 2.557   31.079 88.815  1.00 38.98 ? 455 GLU A O   1 
ATOM   3857 C CB  . GLU A 1 455 ? 2.133   30.366 85.418  1.00 33.22 ? 455 GLU A CB  1 
ATOM   3858 C CG  . GLU A 1 455 ? 2.753   29.497 84.310  1.00 34.12 ? 455 GLU A CG  1 
ATOM   3859 C CD  . GLU A 1 455 ? 3.658   30.293 83.359  1.00 39.23 ? 455 GLU A CD  1 
ATOM   3860 O OE1 . GLU A 1 455 ? 3.601   31.548 83.374  1.00 39.00 ? 455 GLU A OE1 1 
ATOM   3861 O OE2 . GLU A 1 455 ? 4.428   29.659 82.598  1.00 29.94 ? 455 GLU A OE2 1 
ATOM   3862 N N   . GLU A 1 456 ? 1.825   32.635 87.361  1.00 48.67 ? 456 GLU A N   1 
ATOM   3863 C CA  . GLU A 1 456 ? 1.043   33.310 88.383  1.00 52.04 ? 456 GLU A CA  1 
ATOM   3864 C C   . GLU A 1 456 ? -0.178  32.462 88.706  1.00 52.40 ? 456 GLU A C   1 
ATOM   3865 O O   . GLU A 1 456 ? -0.747  31.810 87.824  1.00 49.26 ? 456 GLU A O   1 
ATOM   3866 C CB  . GLU A 1 456 ? 0.636   34.712 87.921  1.00 57.00 ? 456 GLU A CB  1 
ATOM   3867 C CG  . GLU A 1 456 ? 0.845   35.796 88.990  1.00 66.52 ? 456 GLU A CG  1 
ATOM   3868 C CD  . GLU A 1 456 ? 0.756   37.216 88.439  1.00 74.11 ? 456 GLU A CD  1 
ATOM   3869 O OE1 . GLU A 1 456 ? -0.068  37.457 87.526  1.00 73.42 ? 456 GLU A OE1 1 
ATOM   3870 O OE2 . GLU A 1 456 ? 1.508   38.092 88.925  1.00 77.41 ? 456 GLU A OE2 1 
ATOM   3871 N N   . LYS A 1 457 ? -0.561  32.450 89.983  1.00 47.16 ? 457 LYS A N   1 
ATOM   3872 C CA  . LYS A 1 457 ? -1.645  31.584 90.431  1.00 42.71 ? 457 LYS A CA  1 
ATOM   3873 C C   . LYS A 1 457 ? -2.907  31.838 89.616  1.00 43.56 ? 457 LYS A C   1 
ATOM   3874 O O   . LYS A 1 457 ? -3.213  32.974 89.239  1.00 39.60 ? 457 LYS A O   1 
ATOM   3875 C CB  . LYS A 1 457 ? -1.925  31.801 91.923  1.00 52.11 ? 457 LYS A CB  1 
ATOM   3876 C CG  . LYS A 1 457 ? -2.698  30.661 92.589  1.00 56.67 ? 457 LYS A CG  1 
ATOM   3877 C CD  . LYS A 1 457 ? -4.212  30.857 92.504  1.00 61.76 ? 457 LYS A CD  1 
ATOM   3878 C CE  . LYS A 1 457 ? -4.967  29.787 93.283  1.00 66.12 ? 457 LYS A CE  1 
ATOM   3879 N NZ  . LYS A 1 457 ? -5.240  28.579 92.449  1.00 64.85 ? 457 LYS A NZ  1 
ATOM   3880 N N   . ALA A 1 458 ? -3.630  30.761 89.331  1.00 37.21 ? 458 ALA A N   1 
ATOM   3881 C CA  . ALA A 1 458 ? -4.836  30.789 88.522  1.00 35.77 ? 458 ALA A CA  1 
ATOM   3882 C C   . ALA A 1 458 ? -5.729  29.665 89.012  1.00 34.86 ? 458 ALA A C   1 
ATOM   3883 O O   . ALA A 1 458 ? -5.220  28.664 89.528  1.00 32.63 ? 458 ALA A O   1 
ATOM   3884 C CB  . ALA A 1 458 ? -4.510  30.606 87.030  1.00 31.20 ? 458 ALA A CB  1 
ATOM   3885 N N   . PRO A 1 459 ? -7.046  29.782 88.868  1.00 30.94 ? 459 PRO A N   1 
ATOM   3886 C CA  . PRO A 1 459 ? -7.922  28.723 89.385  1.00 39.57 ? 459 PRO A CA  1 
ATOM   3887 C C   . PRO A 1 459 ? -7.615  27.358 88.766  1.00 38.25 ? 459 PRO A C   1 
ATOM   3888 O O   . PRO A 1 459 ? -7.194  27.249 87.609  1.00 30.82 ? 459 PRO A O   1 
ATOM   3889 C CB  . PRO A 1 459 ? -9.333  29.211 89.028  1.00 41.81 ? 459 PRO A CB  1 
ATOM   3890 C CG  . PRO A 1 459 ? -9.149  30.395 88.130  1.00 38.88 ? 459 PRO A CG  1 
ATOM   3891 C CD  . PRO A 1 459 ? -7.806  30.963 88.431  1.00 33.46 ? 459 PRO A CD  1 
ATOM   3892 N N   . PHE A 1 460 ? -7.775  26.316 89.589  1.00 33.32 ? 460 PHE A N   1 
ATOM   3893 C CA  . PHE A 1 460 ? -7.694  24.906 89.205  1.00 29.93 ? 460 PHE A CA  1 
ATOM   3894 C C   . PHE A 1 460 ? -6.305  24.405 88.834  1.00 24.09 ? 460 PHE A C   1 
ATOM   3895 O O   . PHE A 1 460 ? -6.121  23.190 88.694  1.00 24.12 ? 460 PHE A O   1 
ATOM   3896 C CB  . PHE A 1 460 ? -8.660  24.610 88.052  1.00 32.01 ? 460 PHE A CB  1 
ATOM   3897 C CG  . PHE A 1 460 ? -10.098 24.767 88.433  1.00 36.67 ? 460 PHE A CG  1 
ATOM   3898 C CD1 . PHE A 1 460 ? -10.671 23.934 89.376  1.00 43.35 ? 460 PHE A CD1 1 
ATOM   3899 C CD2 . PHE A 1 460 ? -10.873 25.775 87.880  1.00 36.06 ? 460 PHE A CD2 1 
ATOM   3900 C CE1 . PHE A 1 460 ? -11.993 24.087 89.748  1.00 41.61 ? 460 PHE A CE1 1 
ATOM   3901 C CE2 . PHE A 1 460 ? -12.192 25.939 88.255  1.00 33.75 ? 460 PHE A CE2 1 
ATOM   3902 C CZ  . PHE A 1 460 ? -12.757 25.094 89.185  1.00 34.14 ? 460 PHE A CZ  1 
ATOM   3903 N N   . VAL A 1 461 ? -5.312  25.284 88.688  1.00 31.48 ? 461 VAL A N   1 
ATOM   3904 C CA  . VAL A 1 461 ? -3.996  24.780 88.297  1.00 35.19 ? 461 VAL A CA  1 
ATOM   3905 C C   . VAL A 1 461 ? -3.340  23.975 89.411  1.00 30.44 ? 461 VAL A C   1 
ATOM   3906 O O   . VAL A 1 461 ? -2.447  23.165 89.142  1.00 32.84 ? 461 VAL A O   1 
ATOM   3907 C CB  . VAL A 1 461 ? -3.058  25.912 87.854  1.00 46.42 ? 461 VAL A CB  1 
ATOM   3908 C CG1 . VAL A 1 461 ? -3.614  26.597 86.614  1.00 40.06 ? 461 VAL A CG1 1 
ATOM   3909 C CG2 . VAL A 1 461 ? -2.815  26.879 88.993  1.00 51.69 ? 461 VAL A CG2 1 
ATOM   3910 N N   . GLU A 1 462 ? -3.774  24.150 90.661  1.00 20.97 ? 462 GLU A N   1 
ATOM   3911 C CA  . GLU A 1 462 ? -3.326  23.236 91.704  1.00 27.69 ? 462 GLU A CA  1 
ATOM   3912 C C   . GLU A 1 462 ? -3.688  21.791 91.366  1.00 24.68 ? 462 GLU A C   1 
ATOM   3913 O O   . GLU A 1 462 ? -3.013  20.864 91.815  1.00 23.23 ? 462 GLU A O   1 
ATOM   3914 C CB  . GLU A 1 462 ? -3.911  23.645 93.057  1.00 36.12 ? 462 GLU A CB  1 
ATOM   3915 C CG  . GLU A 1 462 ? -5.425  23.564 93.145  1.00 51.19 ? 462 GLU A CG  1 
ATOM   3916 C CD  . GLU A 1 462 ? -6.120  24.834 92.665  1.00 62.95 ? 462 GLU A CD  1 
ATOM   3917 O OE1 . GLU A 1 462 ? -7.367  24.886 92.737  1.00 70.55 ? 462 GLU A OE1 1 
ATOM   3918 O OE2 . GLU A 1 462 ? -5.429  25.775 92.210  1.00 64.06 ? 462 GLU A OE2 1 
ATOM   3919 N N   . VAL A 1 463 ? -4.738  21.572 90.570  1.00 17.90 ? 463 VAL A N   1 
ATOM   3920 C CA  . VAL A 1 463 ? -5.096  20.202 90.215  1.00 20.69 ? 463 VAL A CA  1 
ATOM   3921 C C   . VAL A 1 463 ? -4.045  19.596 89.291  1.00 18.13 ? 463 VAL A C   1 
ATOM   3922 O O   . VAL A 1 463 ? -3.686  18.423 89.425  1.00 15.62 ? 463 VAL A O   1 
ATOM   3923 C CB  . VAL A 1 463 ? -6.508  20.160 89.597  1.00 21.93 ? 463 VAL A CB  1 
ATOM   3924 C CG1 . VAL A 1 463 ? -6.915  18.733 89.294  1.00 25.90 ? 463 VAL A CG1 1 
ATOM   3925 C CG2 . VAL A 1 463 ? -7.496  20.792 90.555  1.00 21.68 ? 463 VAL A CG2 1 
ATOM   3926 N N   . PHE A 1 464 ? -3.524  20.382 88.346  1.00 14.55 ? 464 PHE A N   1 
ATOM   3927 C CA  . PHE A 1 464 ? -2.442  19.883 87.507  1.00 16.61 ? 464 PHE A CA  1 
ATOM   3928 C C   . PHE A 1 464 ? -1.248  19.465 88.342  1.00 15.82 ? 464 PHE A C   1 
ATOM   3929 O O   . PHE A 1 464 ? -0.609  18.448 88.059  1.00 14.47 ? 464 PHE A O   1 
ATOM   3930 C CB  . PHE A 1 464 ? -2.034  20.942 86.486  1.00 12.46 ? 464 PHE A CB  1 
ATOM   3931 C CG  . PHE A 1 464 ? -3.065  21.156 85.420  1.00 15.71 ? 464 PHE A CG  1 
ATOM   3932 C CD1 . PHE A 1 464 ? -3.056  20.374 84.269  1.00 12.03 ? 464 PHE A CD1 1 
ATOM   3933 C CD2 . PHE A 1 464 ? -4.068  22.113 85.579  1.00 13.56 ? 464 PHE A CD2 1 
ATOM   3934 C CE1 . PHE A 1 464 ? -4.004  20.570 83.276  1.00 12.91 ? 464 PHE A CE1 1 
ATOM   3935 C CE2 . PHE A 1 464 ? -5.027  22.308 84.588  1.00 13.93 ? 464 PHE A CE2 1 
ATOM   3936 C CZ  . PHE A 1 464 ? -4.979  21.532 83.431  1.00 13.39 ? 464 PHE A CZ  1 
ATOM   3937 N N   . ASP A 1 465 ? -0.961  20.219 89.396  1.00 14.94 ? 465 ASP A N   1 
ATOM   3938 C CA  . ASP A 1 465 ? 0.158   19.885 90.261  1.00 16.14 ? 465 ASP A CA  1 
ATOM   3939 C C   . ASP A 1 465 ? -0.121  18.596 91.027  1.00 17.07 ? 465 ASP A C   1 
ATOM   3940 O O   . ASP A 1 465 ? 0.766   17.746 91.163  1.00 16.91 ? 465 ASP A O   1 
ATOM   3941 C CB  . ASP A 1 465 ? 0.422   21.062 91.191  1.00 17.94 ? 465 ASP A CB  1 
ATOM   3942 C CG  . ASP A 1 465 ? 1.446   20.756 92.234  1.00 22.60 ? 465 ASP A CG  1 
ATOM   3943 O OD1 . ASP A 1 465 ? 2.651   20.779 91.905  1.00 17.49 ? 465 ASP A OD1 1 
ATOM   3944 O OD2 . ASP A 1 465 ? 1.041   20.459 93.376  1.00 22.39 ? 465 ASP A OD2 1 
ATOM   3945 N N   . LYS A 1 466 ? -1.362  18.416 91.502  1.00 17.75 ? 466 LYS A N   1 
ATOM   3946 C CA  . LYS A 1 466 ? -1.696  17.190 92.216  1.00 15.16 ? 466 LYS A CA  1 
ATOM   3947 C C   . LYS A 1 466 ? -1.594  15.984 91.296  1.00 17.88 ? 466 LYS A C   1 
ATOM   3948 O O   . LYS A 1 466 ? -1.040  14.943 91.685  1.00 19.80 ? 466 LYS A O   1 
ATOM   3949 C CB  . LYS A 1 466 ? -3.076  17.307 92.865  1.00 19.00 ? 466 LYS A CB  1 
ATOM   3950 C CG  . LYS A 1 466 ? -3.593  15.959 93.374  1.00 21.98 ? 466 LYS A CG  1 
ATOM   3951 C CD  . LYS A 1 466 ? -4.942  16.065 94.042  1.00 35.33 ? 466 LYS A CD  1 
ATOM   3952 C CE  . LYS A 1 466 ? -5.003  15.216 95.300  1.00 44.26 ? 466 LYS A CE  1 
ATOM   3953 N NZ  . LYS A 1 466 ? -6.145  15.677 96.117  1.00 47.44 ? 466 LYS A NZ  1 
ATOM   3954 N N   . LEU A 1 467 ? -2.075  16.128 90.060  1.00 18.25 ? 467 LEU A N   1 
ATOM   3955 C CA  . LEU A 1 467 ? -1.950  15.047 89.084  1.00 17.04 ? 467 LEU A CA  1 
ATOM   3956 C C   . LEU A 1 467 ? -0.488  14.692 88.817  1.00 16.83 ? 467 LEU A C   1 
ATOM   3957 O O   . LEU A 1 467 ? -0.093  13.519 88.910  1.00 15.39 ? 467 LEU A O   1 
ATOM   3958 C CB  . LEU A 1 467 ? -2.654  15.424 87.770  1.00 15.13 ? 467 LEU A CB  1 
ATOM   3959 C CG  . LEU A 1 467 ? -4.190  15.392 87.867  1.00 13.06 ? 467 LEU A CG  1 
ATOM   3960 C CD1 . LEU A 1 467 ? -4.864  16.168 86.706  1.00 12.54 ? 467 LEU A CD1 1 
ATOM   3961 C CD2 . LEU A 1 467 ? -4.738  13.948 87.966  1.00 13.86 ? 467 LEU A CD2 1 
ATOM   3962 N N   . PHE A 1 468 ? 0.331   15.694 88.476  1.00 15.94 ? 468 PHE A N   1 
ATOM   3963 C CA  . PHE A 1 468 ? 1.737   15.443 88.171  1.00 17.31 ? 468 PHE A CA  1 
ATOM   3964 C C   . PHE A 1 468 ? 2.419   14.717 89.317  1.00 18.90 ? 468 PHE A C   1 
ATOM   3965 O O   . PHE A 1 468 ? 3.160   13.744 89.113  1.00 17.95 ? 468 PHE A O   1 
ATOM   3966 C CB  . PHE A 1 468 ? 2.458   16.767 87.877  1.00 18.20 ? 468 PHE A CB  1 
ATOM   3967 C CG  . PHE A 1 468 ? 3.948   16.639 87.790  1.00 18.50 ? 468 PHE A CG  1 
ATOM   3968 C CD1 . PHE A 1 468 ? 4.559   16.141 86.638  1.00 15.33 ? 468 PHE A CD1 1 
ATOM   3969 C CD2 . PHE A 1 468 ? 4.760   17.046 88.847  1.00 19.91 ? 468 PHE A CD2 1 
ATOM   3970 C CE1 . PHE A 1 468 ? 5.951   16.049 86.557  1.00 12.20 ? 468 PHE A CE1 1 
ATOM   3971 C CE2 . PHE A 1 468 ? 6.133   16.940 88.766  1.00 19.69 ? 468 PHE A CE2 1 
ATOM   3972 C CZ  . PHE A 1 468 ? 6.727   16.439 87.630  1.00 16.56 ? 468 PHE A CZ  1 
ATOM   3973 N N   . ARG A 1 469 ? 2.181   15.178 90.538  1.00 15.01 ? 469 ARG A N   1 
ATOM   3974 C CA  . ARG A 1 469 ? 2.907   14.606 91.659  1.00 13.54 ? 469 ARG A CA  1 
ATOM   3975 C C   . ARG A 1 469 ? 2.401   13.210 91.978  1.00 16.33 ? 469 ARG A C   1 
ATOM   3976 O O   . ARG A 1 469 ? 3.176   12.362 92.457  1.00 17.89 ? 469 ARG A O   1 
ATOM   3977 C CB  . ARG A 1 469 ? 2.811   15.543 92.864  1.00 18.67 ? 469 ARG A CB  1 
ATOM   3978 C CG  . ARG A 1 469 ? 3.667   16.815 92.670  1.00 18.88 ? 469 ARG A CG  1 
ATOM   3979 C CD  . ARG A 1 469 ? 3.493   17.765 93.850  1.00 17.22 ? 469 ARG A CD  1 
ATOM   3980 N NE  . ARG A 1 469 ? 4.237   19.013 93.684  1.00 18.50 ? 469 ARG A NE  1 
ATOM   3981 C CZ  . ARG A 1 469 ? 5.461   19.222 94.156  1.00 20.85 ? 469 ARG A CZ  1 
ATOM   3982 N NH1 . ARG A 1 469 ? 6.101   18.261 94.817  1.00 18.86 ? 469 ARG A NH1 1 
ATOM   3983 N NH2 . ARG A 1 469 ? 6.046   20.404 93.963  1.00 21.68 ? 469 ARG A NH2 1 
ATOM   3984 N N   . SER A 1 470 ? 1.123   12.944 91.681  1.00 19.27 ? 470 SER A N   1 
ATOM   3985 C CA  . SER A 1 470 ? 0.575   11.610 91.861  1.00 21.49 ? 470 SER A CA  1 
ATOM   3986 C C   . SER A 1 470 ? 1.143   10.654 90.829  1.00 18.76 ? 470 SER A C   1 
ATOM   3987 O O   . SER A 1 470 ? 1.413   9.488  91.140  1.00 20.30 ? 470 SER A O   1 
ATOM   3988 C CB  . SER A 1 470 ? -0.954  11.640 91.757  1.00 21.27 ? 470 SER A CB  1 
ATOM   3989 O OG  . SER A 1 470 ? -1.533  12.334 92.848  1.00 33.81 ? 470 SER A OG  1 
ATOM   3990 N N   . PHE A 1 471 ? 1.300   11.115 89.580  1.00 13.22 ? 471 PHE A N   1 
ATOM   3991 C CA  . PHE A 1 471 ? 1.873   10.229 88.575  1.00 17.26 ? 471 PHE A CA  1 
ATOM   3992 C C   . PHE A 1 471 ? 3.318   9.905  88.920  1.00 18.89 ? 471 PHE A C   1 
ATOM   3993 O O   . PHE A 1 471 ? 3.768   8.758  88.785  1.00 17.20 ? 471 PHE A O   1 
ATOM   3994 C CB  . PHE A 1 471 ? 1.769   10.875 87.194  1.00 15.32 ? 471 PHE A CB  1 
ATOM   3995 C CG  . PHE A 1 471 ? 0.354   11.033 86.707  1.00 14.24 ? 471 PHE A CG  1 
ATOM   3996 C CD1 . PHE A 1 471 ? -0.553  9.984  86.794  1.00 17.35 ? 471 PHE A CD1 1 
ATOM   3997 C CD2 . PHE A 1 471 ? -0.072  12.240 86.170  1.00 13.81 ? 471 PHE A CD2 1 
ATOM   3998 C CE1 . PHE A 1 471 ? -1.876  10.124 86.334  1.00 22.23 ? 471 PHE A CE1 1 
ATOM   3999 C CE2 . PHE A 1 471 ? -1.377  12.383 85.714  1.00 13.62 ? 471 PHE A CE2 1 
ATOM   4000 C CZ  . PHE A 1 471 ? -2.280  11.320 85.800  1.00 15.76 ? 471 PHE A CZ  1 
ATOM   4001 N N   . VAL A 1 472 ? 4.047   10.904 89.405  1.00 17.59 ? 472 VAL A N   1 
ATOM   4002 C CA  . VAL A 1 472 ? 5.437   10.699 89.800  1.00 17.35 ? 472 VAL A CA  1 
ATOM   4003 C C   . VAL A 1 472 ? 5.531   9.678  90.931  1.00 19.48 ? 472 VAL A C   1 
ATOM   4004 O O   . VAL A 1 472 ? 6.403   8.801  90.927  1.00 20.56 ? 472 VAL A O   1 
ATOM   4005 C CB  . VAL A 1 472 ? 6.063   12.049 90.187  1.00 19.24 ? 472 VAL A CB  1 
ATOM   4006 C CG1 . VAL A 1 472 ? 7.310   11.835 91.005  1.00 24.04 ? 472 VAL A CG1 1 
ATOM   4007 C CG2 . VAL A 1 472 ? 6.326   12.903 88.907  1.00 16.07 ? 472 VAL A CG2 1 
ATOM   4008 N N   . ARG A 1 473 ? 4.648   9.778  91.925  1.00 17.04 ? 473 ARG A N   1 
ATOM   4009 C CA  . ARG A 1 473 ? 4.670   8.804  93.012  1.00 17.87 ? 473 ARG A CA  1 
ATOM   4010 C C   . ARG A 1 473 ? 4.293   7.412  92.519  1.00 21.12 ? 473 ARG A C   1 
ATOM   4011 O O   . ARG A 1 473 ? 4.942   6.421  92.873  1.00 20.38 ? 473 ARG A O   1 
ATOM   4012 C CB  . ARG A 1 473 ? 3.736   9.259  94.127  1.00 26.45 ? 473 ARG A CB  1 
ATOM   4013 C CG  . ARG A 1 473 ? 3.684   8.328  95.314  1.00 32.06 ? 473 ARG A CG  1 
ATOM   4014 C CD  . ARG A 1 473 ? 3.106   9.060  96.495  1.00 38.35 ? 473 ARG A CD  1 
ATOM   4015 N NE  . ARG A 1 473 ? 1.649   8.994  96.542  1.00 53.02 ? 473 ARG A NE  1 
ATOM   4016 C CZ  . ARG A 1 473 ? 0.962   7.991  97.088  1.00 59.65 ? 473 ARG A CZ  1 
ATOM   4017 N NH1 . ARG A 1 473 ? 1.604   6.954  97.616  1.00 52.32 ? 473 ARG A NH1 1 
ATOM   4018 N NH2 . ARG A 1 473 ? -0.368  8.021  97.099  1.00 59.57 ? 473 ARG A NH2 1 
ATOM   4019 N N   . ARG A 1 474 ? 3.234   7.316  91.714  1.00 21.49 ? 474 ARG A N   1 
ATOM   4020 C CA  . ARG A 1 474 ? 2.765   6.020  91.230  1.00 21.65 ? 474 ARG A CA  1 
ATOM   4021 C C   . ARG A 1 474 ? 3.813   5.339  90.356  1.00 18.30 ? 474 ARG A C   1 
ATOM   4022 O O   . ARG A 1 474 ? 3.907   4.103  90.336  1.00 21.07 ? 474 ARG A O   1 
ATOM   4023 C CB  . ARG A 1 474 ? 1.458   6.217  90.462  1.00 21.59 ? 474 ARG A CB  1 
ATOM   4024 C CG  . ARG A 1 474 ? 0.857   4.936  89.906  1.00 25.08 ? 474 ARG A CG  1 
ATOM   4025 C CD  . ARG A 1 474 ? 0.340   4.033  91.024  1.00 32.22 ? 474 ARG A CD  1 
ATOM   4026 N NE  . ARG A 1 474 ? -0.312  2.833  90.503  1.00 37.55 ? 474 ARG A NE  1 
ATOM   4027 C CZ  . ARG A 1 474 ? 0.329   1.737  90.094  1.00 51.26 ? 474 ARG A CZ  1 
ATOM   4028 N NH1 . ARG A 1 474 ? 1.657   1.666  90.141  1.00 40.59 ? 474 ARG A NH1 1 
ATOM   4029 N NH2 . ARG A 1 474 ? -0.365  0.700  89.636  1.00 59.53 ? 474 ARG A NH2 1 
ATOM   4030 N N   . ALA A 1 475 ? 4.616   6.135  89.652  1.00 18.25 ? 475 ALA A N   1 
ATOM   4031 C CA  . ALA A 1 475 ? 5.692   5.647  88.792  1.00 16.94 ? 475 ALA A CA  1 
ATOM   4032 C C   . ALA A 1 475 ? 6.758   4.879  89.559  1.00 22.61 ? 475 ALA A C   1 
ATOM   4033 O O   . ALA A 1 475 ? 7.469   4.056  88.966  1.00 21.90 ? 475 ALA A O   1 
ATOM   4034 C CB  . ALA A 1 475 ? 6.359   6.823  88.093  1.00 14.84 ? 475 ALA A CB  1 
ATOM   4035 N N   . GLN A 1 476 ? 6.898   5.146  90.850  1.00 22.64 ? 476 GLN A N   1 
ATOM   4036 C CA  . GLN A 1 476 ? 7.923   4.518  91.664  1.00 20.99 ? 476 GLN A CA  1 
ATOM   4037 C C   . GLN A 1 476 ? 7.392   3.343  92.472  1.00 23.87 ? 476 GLN A C   1 
ATOM   4038 O O   . GLN A 1 476 ? 8.162   2.713  93.201  1.00 28.56 ? 476 GLN A O   1 
ATOM   4039 C CB  . GLN A 1 476 ? 8.550   5.566  92.587  1.00 23.47 ? 476 GLN A CB  1 
ATOM   4040 C CG  . GLN A 1 476 ? 9.195   6.708  91.786  1.00 21.49 ? 476 GLN A CG  1 
ATOM   4041 C CD  . GLN A 1 476 ? 9.588   7.889  92.655  1.00 25.87 ? 476 GLN A CD  1 
ATOM   4042 O OE1 . GLN A 1 476 ? 10.617  7.860  93.305  1.00 27.11 ? 476 GLN A OE1 1 
ATOM   4043 N NE2 . GLN A 1 476 ? 8.760   8.932  92.668  1.00 25.98 ? 476 GLN A NE2 1 
ATOM   4044 N N   . GLU A 1 477 ? 6.105   3.015  92.351  1.00 25.63 ? 477 GLU A N   1 
ATOM   4045 C CA  . GLU A 1 477 ? 5.570   1.884  93.110  1.00 35.42 ? 477 GLU A CA  1 
ATOM   4046 C C   . GLU A 1 477 ? 5.389   0.647  92.244  1.00 43.31 ? 477 GLU A C   1 
ATOM   4047 O O   . GLU A 1 477 ? 4.940   0.750  91.101  1.00 35.14 ? 477 GLU A O   1 
ATOM   4048 C CB  . GLU A 1 477 ? 4.245   2.267  93.745  1.00 42.72 ? 477 GLU A CB  1 
ATOM   4049 C CG  . GLU A 1 477 ? 4.344   3.436  94.686  1.00 54.56 ? 477 GLU A CG  1 
ATOM   4050 C CD  . GLU A 1 477 ? 2.980   3.882  95.158  1.00 53.27 ? 477 GLU A CD  1 
ATOM   4051 O OE1 . GLU A 1 477 ? 1.993   3.177  94.856  1.00 55.40 ? 477 GLU A OE1 1 
ATOM   4052 O OE2 . GLU A 1 477 ? 2.897   4.927  95.833  1.00 54.30 ? 477 GLU A OE2 1 
ATOM   4053 N N   . LYS B 1 2   ? -27.559 46.609 60.345  1.00 29.60 ? 2   LYS B N   1 
ATOM   4054 C CA  . LYS B 1 2   ? -28.538 46.910 59.290  1.00 29.76 ? 2   LYS B CA  1 
ATOM   4055 C C   . LYS B 1 2   ? -27.878 47.048 57.923  1.00 30.17 ? 2   LYS B C   1 
ATOM   4056 O O   . LYS B 1 2   ? -27.236 48.059 57.624  1.00 32.63 ? 2   LYS B O   1 
ATOM   4057 C CB  . LYS B 1 2   ? -29.309 48.189 59.610  1.00 38.74 ? 2   LYS B CB  1 
ATOM   4058 C CG  . LYS B 1 2   ? -30.571 48.357 58.773  1.00 46.89 ? 2   LYS B CG  1 
ATOM   4059 C CD  . LYS B 1 2   ? -30.609 49.703 58.071  1.00 54.12 ? 2   LYS B CD  1 
ATOM   4060 C CE  . LYS B 1 2   ? -31.256 50.763 58.934  1.00 56.97 ? 2   LYS B CE  1 
ATOM   4061 N NZ  . LYS B 1 2   ? -30.985 52.131 58.409  1.00 51.40 ? 2   LYS B NZ  1 
ATOM   4062 N N   . LYS B 1 3   ? -28.032 46.026 57.099  1.00 25.53 ? 3   LYS B N   1 
ATOM   4063 C CA  . LYS B 1 3   ? -27.439 45.992 55.774  1.00 26.21 ? 3   LYS B CA  1 
ATOM   4064 C C   . LYS B 1 3   ? -28.450 46.413 54.717  1.00 25.72 ? 3   LYS B C   1 
ATOM   4065 O O   . LYS B 1 3   ? -29.666 46.388 54.932  1.00 26.46 ? 3   LYS B O   1 
ATOM   4066 C CB  . LYS B 1 3   ? -26.923 44.588 55.438  1.00 27.37 ? 3   LYS B CB  1 
ATOM   4067 C CG  . LYS B 1 3   ? -25.994 44.003 56.522  1.00 31.91 ? 3   LYS B CG  1 
ATOM   4068 C CD  . LYS B 1 3   ? -24.671 43.604 55.919  1.00 41.42 ? 3   LYS B CD  1 
ATOM   4069 C CE  . LYS B 1 3   ? -23.796 42.845 56.910  1.00 46.10 ? 3   LYS B CE  1 
ATOM   4070 N NZ  . LYS B 1 3   ? -22.900 41.925 56.154  1.00 51.85 ? 3   LYS B NZ  1 
ATOM   4071 N N   . LEU B 1 4   ? -27.925 46.803 53.564  1.00 20.23 ? 4   LEU B N   1 
ATOM   4072 C CA  . LEU B 1 4   ? -28.714 46.869 52.343  1.00 19.28 ? 4   LEU B CA  1 
ATOM   4073 C C   . LEU B 1 4   ? -28.395 45.635 51.520  1.00 18.35 ? 4   LEU B C   1 
ATOM   4074 O O   . LEU B 1 4   ? -27.219 45.290 51.334  1.00 23.65 ? 4   LEU B O   1 
ATOM   4075 C CB  . LEU B 1 4   ? -28.409 48.135 51.543  1.00 23.29 ? 4   LEU B CB  1 
ATOM   4076 C CG  . LEU B 1 4   ? -29.132 48.319 50.205  1.00 17.98 ? 4   LEU B CG  1 
ATOM   4077 C CD1 . LEU B 1 4   ? -29.390 49.796 49.927  1.00 21.60 ? 4   LEU B CD1 1 
ATOM   4078 C CD2 . LEU B 1 4   ? -28.317 47.697 49.040  1.00 16.89 ? 4   LEU B CD2 1 
ATOM   4079 N N   . PHE B 1 5   ? -29.434 44.991 50.998  1.00 17.95 ? 5   PHE B N   1 
ATOM   4080 C CA  . PHE B 1 5   ? -29.270 43.821 50.151  1.00 17.16 ? 5   PHE B CA  1 
ATOM   4081 C C   . PHE B 1 5   ? -29.413 44.233 48.696  1.00 17.70 ? 5   PHE B C   1 
ATOM   4082 O O   . PHE B 1 5   ? -30.419 44.835 48.311  1.00 21.27 ? 5   PHE B O   1 
ATOM   4083 C CB  . PHE B 1 5   ? -30.303 42.758 50.520  1.00 17.49 ? 5   PHE B CB  1 
ATOM   4084 C CG  . PHE B 1 5   ? -30.130 42.231 51.918  1.00 22.75 ? 5   PHE B CG  1 
ATOM   4085 C CD1 . PHE B 1 5   ? -28.896 41.733 52.328  1.00 27.73 ? 5   PHE B CD1 1 
ATOM   4086 C CD2 . PHE B 1 5   ? -31.169 42.274 52.821  1.00 19.46 ? 5   PHE B CD2 1 
ATOM   4087 C CE1 . PHE B 1 5   ? -28.718 41.260 53.620  1.00 26.16 ? 5   PHE B CE1 1 
ATOM   4088 C CE2 . PHE B 1 5   ? -31.015 41.808 54.126  1.00 23.84 ? 5   PHE B CE2 1 
ATOM   4089 C CZ  . PHE B 1 5   ? -29.785 41.298 54.535  1.00 22.56 ? 5   PHE B CZ  1 
ATOM   4090 N N   . LEU B 1 6   ? -28.424 43.874 47.898  1.00 15.49 ? 6   LEU B N   1 
ATOM   4091 C CA  . LEU B 1 6   ? -28.329 44.275 46.501  1.00 15.68 ? 6   LEU B CA  1 
ATOM   4092 C C   . LEU B 1 6   ? -28.333 43.031 45.634  1.00 22.15 ? 6   LEU B C   1 
ATOM   4093 O O   . LEU B 1 6   ? -27.558 42.107 45.880  1.00 16.51 ? 6   LEU B O   1 
ATOM   4094 C CB  . LEU B 1 6   ? -27.050 45.074 46.272  1.00 14.71 ? 6   LEU B CB  1 
ATOM   4095 C CG  . LEU B 1 6   ? -26.804 45.642 44.871  1.00 14.24 ? 6   LEU B CG  1 
ATOM   4096 C CD1 . LEU B 1 6   ? -27.928 46.607 44.478  1.00 19.08 ? 6   LEU B CD1 1 
ATOM   4097 C CD2 . LEU B 1 6   ? -25.468 46.357 44.867  1.00 15.16 ? 6   LEU B CD2 1 
ATOM   4098 N N   . VAL B 1 7   ? -29.212 42.998 44.638  1.00 14.68 ? 7   VAL B N   1 
ATOM   4099 C CA  . VAL B 1 7   ? -29.390 41.826 43.788  1.00 13.05 ? 7   VAL B CA  1 
ATOM   4100 C C   . VAL B 1 7   ? -29.282 42.288 42.345  1.00 13.76 ? 7   VAL B C   1 
ATOM   4101 O O   . VAL B 1 7   ? -30.164 43.013 41.861  1.00 14.82 ? 7   VAL B O   1 
ATOM   4102 C CB  . VAL B 1 7   ? -30.740 41.134 44.050  1.00 13.34 ? 7   VAL B CB  1 
ATOM   4103 C CG1 . VAL B 1 7   ? -30.799 39.801 43.348  1.00 16.55 ? 7   VAL B CG1 1 
ATOM   4104 C CG2 . VAL B 1 7   ? -30.929 40.917 45.534  1.00 15.97 ? 7   VAL B CG2 1 
ATOM   4105 N N   . PHE B 1 8   ? -28.211 41.873 41.651  1.00 17.25 ? 8   PHE B N   1 
ATOM   4106 C CA  . PHE B 1 8   ? -28.083 42.104 40.217  1.00 14.98 ? 8   PHE B CA  1 
ATOM   4107 C C   . PHE B 1 8   ? -28.664 40.904 39.489  1.00 14.66 ? 8   PHE B C   1 
ATOM   4108 O O   . PHE B 1 8   ? -28.375 39.761 39.841  1.00 14.13 ? 8   PHE B O   1 
ATOM   4109 C CB  . PHE B 1 8   ? -26.635 42.283 39.768  1.00 14.18 ? 8   PHE B CB  1 
ATOM   4110 C CG  . PHE B 1 8   ? -25.994 43.573 40.228  1.00 15.09 ? 8   PHE B CG  1 
ATOM   4111 C CD1 . PHE B 1 8   ? -26.091 44.717 39.458  1.00 17.33 ? 8   PHE B CD1 1 
ATOM   4112 C CD2 . PHE B 1 8   ? -25.288 43.620 41.420  1.00 17.08 ? 8   PHE B CD2 1 
ATOM   4113 C CE1 . PHE B 1 8   ? -25.502 45.903 39.869  1.00 17.86 ? 8   PHE B CE1 1 
ATOM   4114 C CE2 . PHE B 1 8   ? -24.685 44.799 41.840  1.00 19.02 ? 8   PHE B CE2 1 
ATOM   4115 C CZ  . PHE B 1 8   ? -24.804 45.946 41.065  1.00 19.70 ? 8   PHE B CZ  1 
ATOM   4116 N N   . TRP B 1 9   ? -29.474 41.163 38.475  1.00 11.50 ? 9   TRP B N   1 
ATOM   4117 C CA  . TRP B 1 9   ? -30.027 40.084 37.656  1.00 13.36 ? 9   TRP B CA  1 
ATOM   4118 C C   . TRP B 1 9   ? -29.868 40.527 36.207  1.00 15.92 ? 9   TRP B C   1 
ATOM   4119 O O   . TRP B 1 9   ? -30.641 41.353 35.713  1.00 14.98 ? 9   TRP B O   1 
ATOM   4120 C CB  . TRP B 1 9   ? -31.480 39.825 38.026  1.00 14.94 ? 9   TRP B CB  1 
ATOM   4121 C CG  . TRP B 1 9   ? -32.103 38.531 37.586  1.00 15.48 ? 9   TRP B CG  1 
ATOM   4122 C CD1 . TRP B 1 9   ? -31.588 37.597 36.714  1.00 20.39 ? 9   TRP B CD1 1 
ATOM   4123 C CD2 . TRP B 1 9   ? -33.387 38.045 37.984  1.00 14.52 ? 9   TRP B CD2 1 
ATOM   4124 N NE1 . TRP B 1 9   ? -32.480 36.566 36.555  1.00 12.98 ? 9   TRP B NE1 1 
ATOM   4125 C CE2 . TRP B 1 9   ? -33.590 36.809 37.331  1.00 15.29 ? 9   TRP B CE2 1 
ATOM   4126 C CE3 . TRP B 1 9   ? -34.372 38.520 38.859  1.00 18.86 ? 9   TRP B CE3 1 
ATOM   4127 C CZ2 . TRP B 1 9   ? -34.755 36.063 37.495  1.00 15.25 ? 9   TRP B CZ2 1 
ATOM   4128 C CZ3 . TRP B 1 9   ? -35.525 37.769 39.034  1.00 18.30 ? 9   TRP B CZ3 1 
ATOM   4129 C CH2 . TRP B 1 9   ? -35.706 36.557 38.360  1.00 19.21 ? 9   TRP B CH2 1 
ATOM   4130 N N   . TRP B 1 10  ? -28.886 39.939 35.530  1.00 12.98 ? 10  TRP B N   1 
ATOM   4131 C CA  . TRP B 1 10  ? -28.521 40.321 34.170  1.00 13.79 ? 10  TRP B CA  1 
ATOM   4132 C C   . TRP B 1 10  ? -29.227 39.376 33.203  1.00 17.67 ? 10  TRP B C   1 
ATOM   4133 O O   . TRP B 1 10  ? -28.989 38.168 33.242  1.00 14.30 ? 10  TRP B O   1 
ATOM   4134 C CB  . TRP B 1 10  ? -27.012 40.234 33.969  1.00 14.18 ? 10  TRP B CB  1 
ATOM   4135 C CG  . TRP B 1 10  ? -26.139 41.158 34.840  1.00 13.96 ? 10  TRP B CG  1 
ATOM   4136 C CD1 . TRP B 1 10  ? -25.232 40.758 35.788  1.00 13.48 ? 10  TRP B CD1 1 
ATOM   4137 C CD2 . TRP B 1 10  ? -26.048 42.588 34.776  1.00 15.60 ? 10  TRP B CD2 1 
ATOM   4138 N NE1 . TRP B 1 10  ? -24.612 41.850 36.346  1.00 12.42 ? 10  TRP B NE1 1 
ATOM   4139 C CE2 . TRP B 1 10  ? -25.087 42.989 35.744  1.00 14.24 ? 10  TRP B CE2 1 
ATOM   4140 C CE3 . TRP B 1 10  ? -26.699 43.574 34.016  1.00 15.39 ? 10  TRP B CE3 1 
ATOM   4141 C CZ2 . TRP B 1 10  ? -24.752 44.327 35.954  1.00 14.34 ? 10  TRP B CZ2 1 
ATOM   4142 C CZ3 . TRP B 1 10  ? -26.378 44.905 34.239  1.00 15.78 ? 10  TRP B CZ3 1 
ATOM   4143 C CH2 . TRP B 1 10  ? -25.399 45.269 35.190  1.00 15.67 ? 10  TRP B CH2 1 
ATOM   4144 N N   . HIS B 1 11  ? -30.090 39.919 32.348  1.00 10.55 ? 11  HIS B N   1 
ATOM   4145 C CA  . HIS B 1 11  ? -30.922 39.110 31.460  1.00 13.68 ? 11  HIS B CA  1 
ATOM   4146 C C   . HIS B 1 11  ? -30.282 38.985 30.070  1.00 10.13 ? 11  HIS B C   1 
ATOM   4147 O O   . HIS B 1 11  ? -30.009 39.990 29.413  1.00 13.64 ? 11  HIS B O   1 
ATOM   4148 C CB  . HIS B 1 11  ? -32.326 39.715 31.379  1.00 12.59 ? 11  HIS B CB  1 
ATOM   4149 C CG  . HIS B 1 11  ? -33.077 39.322 30.150  1.00 11.57 ? 11  HIS B CG  1 
ATOM   4150 N ND1 . HIS B 1 11  ? -33.520 38.038 29.920  1.00 12.54 ? 11  HIS B ND1 1 
ATOM   4151 C CD2 . HIS B 1 11  ? -33.463 40.057 29.077  1.00 13.17 ? 11  HIS B CD2 1 
ATOM   4152 C CE1 . HIS B 1 11  ? -34.141 37.992 28.753  1.00 15.15 ? 11  HIS B CE1 1 
ATOM   4153 N NE2 . HIS B 1 11  ? -34.123 39.205 28.222  1.00 13.56 ? 11  HIS B NE2 1 
ATOM   4154 N N   . MET B 1 12  ? -30.016 37.752 29.647  1.00 13.19 ? 12  MET B N   1 
ATOM   4155 C CA  . MET B 1 12  ? -29.350 37.447 28.375  1.00 10.97 ? 12  MET B CA  1 
ATOM   4156 C C   . MET B 1 12  ? -30.349 36.773 27.439  1.00 15.94 ? 12  MET B C   1 
ATOM   4157 O O   . MET B 1 12  ? -30.949 35.749 27.805  1.00 14.43 ? 12  MET B O   1 
ATOM   4158 C CB  . MET B 1 12  ? -28.156 36.511 28.599  1.00 15.02 ? 12  MET B CB  1 
ATOM   4159 C CG  . MET B 1 12  ? -27.182 36.956 29.709  1.00 14.63 ? 12  MET B CG  1 
ATOM   4160 S SD  . MET B 1 12  ? -26.529 38.595 29.362  1.00 15.50 ? 12  MET B SD  1 
ATOM   4161 C CE  . MET B 1 12  ? -25.122 38.628 30.495  1.00 16.63 ? 12  MET B CE  1 
ATOM   4162 N N   . HIS B 1 13  ? -30.496 37.308 26.218  1.00 13.89 ? 13  HIS B N   1 
ATOM   4163 C CA  . HIS B 1 13  ? -31.473 36.763 25.285  1.00 13.95 ? 13  HIS B CA  1 
ATOM   4164 C C   . HIS B 1 13  ? -31.084 37.113 23.847  1.00 14.85 ? 13  HIS B C   1 
ATOM   4165 O O   . HIS B 1 13  ? -30.562 38.205 23.603  1.00 13.49 ? 13  HIS B O   1 
ATOM   4166 C CB  . HIS B 1 13  ? -32.868 37.326 25.595  1.00 14.85 ? 13  HIS B CB  1 
ATOM   4167 C CG  . HIS B 1 13  ? -33.877 37.010 24.533  1.00 12.81 ? 13  HIS B CG  1 
ATOM   4168 N ND1 . HIS B 1 13  ? -34.175 35.718 24.153  1.00 11.89 ? 13  HIS B ND1 1 
ATOM   4169 C CD2 . HIS B 1 13  ? -34.657 37.820 23.776  1.00 13.57 ? 13  HIS B CD2 1 
ATOM   4170 C CE1 . HIS B 1 13  ? -35.099 35.752 23.203  1.00 14.96 ? 13  HIS B CE1 1 
ATOM   4171 N NE2 . HIS B 1 13  ? -35.413 37.013 22.962  1.00 12.51 ? 13  HIS B NE2 1 
ATOM   4172 N N   . GLN B 1 14  ? -31.337 36.184 22.903  1.00 11.57 ? 14  GLN B N   1 
ATOM   4173 C CA  . GLN B 1 14  ? -31.399 36.494 21.439  1.00 12.54 ? 14  GLN B CA  1 
ATOM   4174 C C   . GLN B 1 14  ? -32.556 35.702 20.842  1.00 15.87 ? 14  GLN B C   1 
ATOM   4175 O O   . GLN B 1 14  ? -32.684 34.494 21.119  1.00 12.88 ? 14  GLN B O   1 
ATOM   4176 C CB  . GLN B 1 14  ? -30.110 36.131 20.663  1.00 15.19 ? 14  GLN B CB  1 
ATOM   4177 C CG  . GLN B 1 14  ? -28.843 36.884 21.069  1.00 13.96 ? 14  GLN B CG  1 
ATOM   4178 C CD  . GLN B 1 14  ? -28.901 38.376 20.804  1.00 14.20 ? 14  GLN B CD  1 
ATOM   4179 O OE1 . GLN B 1 14  ? -29.637 38.852 19.935  1.00 15.93 ? 14  GLN B OE1 1 
ATOM   4180 N NE2 . GLN B 1 14  ? -28.130 39.132 21.580  1.00 13.10 ? 14  GLN B NE2 1 
ATOM   4181 N N   . PRO B 1 15  ? -33.393 36.321 20.012  1.00 14.84 ? 15  PRO B N   1 
ATOM   4182 C CA  . PRO B 1 15  ? -34.356 35.542 19.228  1.00 15.71 ? 15  PRO B CA  1 
ATOM   4183 C C   . PRO B 1 15  ? -33.616 34.617 18.266  1.00 15.59 ? 15  PRO B C   1 
ATOM   4184 O O   . PRO B 1 15  ? -32.420 34.782 17.988  1.00 15.53 ? 15  PRO B O   1 
ATOM   4185 C CB  . PRO B 1 15  ? -35.150 36.614 18.460  1.00 15.75 ? 15  PRO B CB  1 
ATOM   4186 C CG  . PRO B 1 15  ? -34.159 37.742 18.312  1.00 14.54 ? 15  PRO B CG  1 
ATOM   4187 C CD  . PRO B 1 15  ? -33.352 37.737 19.600  1.00 13.43 ? 15  PRO B CD  1 
ATOM   4188 N N   . LEU B 1 16  ? -34.346 33.649 17.718  1.00 14.53 ? 16  LEU B N   1 
ATOM   4189 C CA  . LEU B 1 16  ? -33.727 32.651 16.836  1.00 14.42 ? 16  LEU B CA  1 
ATOM   4190 C C   . LEU B 1 16  ? -33.406 33.270 15.473  1.00 17.78 ? 16  LEU B C   1 
ATOM   4191 O O   . LEU B 1 16  ? -34.316 33.580 14.696  1.00 19.56 ? 16  LEU B O   1 
ATOM   4192 C CB  . LEU B 1 16  ? -34.656 31.447 16.691  1.00 15.07 ? 16  LEU B CB  1 
ATOM   4193 C CG  . LEU B 1 16  ? -34.087 30.244 15.913  1.00 20.40 ? 16  LEU B CG  1 
ATOM   4194 C CD1 . LEU B 1 16  ? -32.777 29.745 16.564  1.00 17.83 ? 16  LEU B CD1 1 
ATOM   4195 C CD2 . LEU B 1 16  ? -35.107 29.112 15.835  1.00 19.16 ? 16  LEU B CD2 1 
ATOM   4196 N N   . TYR B 1 17  ? -32.116 33.439 15.168  1.00 21.28 ? 17  TYR B N   1 
ATOM   4197 C CA  . TYR B 1 17  ? -31.679 34.001 13.894  1.00 17.64 ? 17  TYR B CA  1 
ATOM   4198 C C   . TYR B 1 17  ? -31.522 32.949 12.802  1.00 18.66 ? 17  TYR B C   1 
ATOM   4199 O O   . TYR B 1 17  ? -31.172 33.299 11.669  1.00 18.36 ? 17  TYR B O   1 
ATOM   4200 C CB  . TYR B 1 17  ? -30.348 34.745 14.060  1.00 24.21 ? 17  TYR B CB  1 
ATOM   4201 C CG  . TYR B 1 17  ? -30.446 35.942 14.980  1.00 21.69 ? 17  TYR B CG  1 
ATOM   4202 C CD1 . TYR B 1 17  ? -31.325 36.986 14.699  1.00 20.82 ? 17  TYR B CD1 1 
ATOM   4203 C CD2 . TYR B 1 17  ? -29.651 36.027 16.124  1.00 15.76 ? 17  TYR B CD2 1 
ATOM   4204 C CE1 . TYR B 1 17  ? -31.429 38.095 15.541  1.00 22.61 ? 17  TYR B CE1 1 
ATOM   4205 C CE2 . TYR B 1 17  ? -29.732 37.143 16.967  1.00 16.59 ? 17  TYR B CE2 1 
ATOM   4206 C CZ  . TYR B 1 17  ? -30.629 38.163 16.679  1.00 20.26 ? 17  TYR B CZ  1 
ATOM   4207 O OH  . TYR B 1 17  ? -30.736 39.263 17.513  1.00 20.17 ? 17  TYR B OH  1 
ATOM   4208 N N   . ARG B 1 18  ? -31.763 31.685 13.120  1.00 22.81 ? 18  ARG B N   1 
ATOM   4209 C CA  . ARG B 1 18  ? -31.534 30.574 12.203  1.00 23.05 ? 18  ARG B CA  1 
ATOM   4210 C C   . ARG B 1 18  ? -32.777 30.341 11.351  1.00 25.32 ? 18  ARG B C   1 
ATOM   4211 O O   . ARG B 1 18  ? -33.803 29.859 11.844  1.00 21.29 ? 18  ARG B O   1 
ATOM   4212 C CB  . ARG B 1 18  ? -31.155 29.328 12.995  1.00 20.80 ? 18  ARG B CB  1 
ATOM   4213 C CG  . ARG B 1 18  ? -30.949 28.109 12.150  1.00 21.84 ? 18  ARG B CG  1 
ATOM   4214 C CD  . ARG B 1 18  ? -30.870 26.874 13.020  1.00 25.25 ? 18  ARG B CD  1 
ATOM   4215 N NE  . ARG B 1 18  ? -30.213 25.780 12.304  1.00 33.95 ? 18  ARG B NE  1 
ATOM   4216 C CZ  . ARG B 1 18  ? -30.842 24.919 11.510  1.00 35.06 ? 18  ARG B CZ  1 
ATOM   4217 N NH1 . ARG B 1 18  ? -32.154 25.025 11.310  1.00 32.32 ? 18  ARG B NH1 1 
ATOM   4218 N NH2 . ARG B 1 18  ? -30.163 23.954 10.899  1.00 37.34 ? 18  ARG B NH2 1 
ATOM   4219 N N   . GLU B 1 19  ? -32.676 30.669 10.065  1.00 20.12 ? 19  GLU B N   1 
ATOM   4220 C CA  . GLU B 1 19  ? -33.795 30.493 9.148   1.00 24.71 ? 19  GLU B CA  1 
ATOM   4221 C C   . GLU B 1 19  ? -34.052 29.002 8.952   1.00 28.73 ? 19  GLU B C   1 
ATOM   4222 O O   . GLU B 1 19  ? -33.103 28.246 8.690   1.00 29.24 ? 19  GLU B O   1 
ATOM   4223 C CB  . GLU B 1 19  ? -33.483 31.154 7.810   1.00 25.01 ? 19  GLU B CB  1 
ATOM   4224 C CG  . GLU B 1 19  ? -34.705 31.630 7.035   1.00 30.68 ? 19  GLU B CG  1 
ATOM   4225 C CD  . GLU B 1 19  ? -35.197 30.599 6.024   1.00 35.96 ? 19  GLU B CD  1 
ATOM   4226 O OE1 . GLU B 1 19  ? -34.581 29.519 5.901   1.00 36.52 ? 19  GLU B OE1 1 
ATOM   4227 O OE2 . GLU B 1 19  ? -36.201 30.883 5.336   1.00 41.21 ? 19  GLU B OE2 1 
ATOM   4228 N N   . PRO B 1 20  ? -35.301 28.538 9.062   1.00 25.89 ? 20  PRO B N   1 
ATOM   4229 C CA  . PRO B 1 20  ? -35.538 27.082 9.114   1.00 31.63 ? 20  PRO B CA  1 
ATOM   4230 C C   . PRO B 1 20  ? -35.382 26.362 7.776   1.00 36.36 ? 20  PRO B C   1 
ATOM   4231 O O   . PRO B 1 20  ? -35.166 25.144 7.773   1.00 39.30 ? 20  PRO B O   1 
ATOM   4232 C CB  . PRO B 1 20  ? -36.970 26.981 9.657   1.00 29.62 ? 20  PRO B CB  1 
ATOM   4233 C CG  . PRO B 1 20  ? -37.596 28.295 9.334   1.00 30.85 ? 20  PRO B CG  1 
ATOM   4234 C CD  . PRO B 1 20  ? -36.520 29.321 9.321   1.00 26.76 ? 20  PRO B CD  1 
ATOM   4235 N N   . TYR B 1 21  ? -35.471 27.052 6.646   1.00 29.85 ? 21  TYR B N   1 
ATOM   4236 C CA  . TYR B 1 21  ? -35.316 26.359 5.373   1.00 33.74 ? 21  TYR B CA  1 
ATOM   4237 C C   . TYR B 1 21  ? -33.855 26.253 4.945   1.00 47.67 ? 21  TYR B C   1 
ATOM   4238 O O   . TYR B 1 21  ? -33.418 25.188 4.490   1.00 54.47 ? 21  TYR B O   1 
ATOM   4239 C CB  . TYR B 1 21  ? -36.152 27.062 4.305   1.00 27.27 ? 21  TYR B CB  1 
ATOM   4240 C CG  . TYR B 1 21  ? -37.623 26.958 4.603   1.00 26.78 ? 21  TYR B CG  1 
ATOM   4241 C CD1 . TYR B 1 21  ? -38.363 25.865 4.167   1.00 31.56 ? 21  TYR B CD1 1 
ATOM   4242 C CD2 . TYR B 1 21  ? -38.270 27.931 5.354   1.00 35.33 ? 21  TYR B CD2 1 
ATOM   4243 C CE1 . TYR B 1 21  ? -39.712 25.754 4.456   1.00 38.61 ? 21  TYR B CE1 1 
ATOM   4244 C CE2 . TYR B 1 21  ? -39.622 27.825 5.656   1.00 37.04 ? 21  TYR B CE2 1 
ATOM   4245 C CZ  . TYR B 1 21  ? -40.336 26.734 5.201   1.00 40.40 ? 21  TYR B CZ  1 
ATOM   4246 O OH  . TYR B 1 21  ? -41.676 26.614 5.483   1.00 42.80 ? 21  TYR B OH  1 
ATOM   4247 N N   . THR B 1 22  ? -33.081 27.324 5.100   1.00 42.41 ? 22  THR B N   1 
ATOM   4248 C CA  . THR B 1 22  ? -31.675 27.285 4.739   1.00 34.15 ? 22  THR B CA  1 
ATOM   4249 C C   . THR B 1 22  ? -30.786 26.863 5.895   1.00 37.55 ? 22  THR B C   1 
ATOM   4250 O O   . THR B 1 22  ? -29.636 26.476 5.663   1.00 33.39 ? 22  THR B O   1 
ATOM   4251 C CB  . THR B 1 22  ? -31.219 28.653 4.229   1.00 37.09 ? 22  THR B CB  1 
ATOM   4252 O OG1 . THR B 1 22  ? -31.278 29.612 5.295   1.00 32.24 ? 22  THR B OG1 1 
ATOM   4253 C CG2 . THR B 1 22  ? -32.123 29.114 3.088   1.00 32.98 ? 22  THR B CG2 1 
ATOM   4254 N N   . GLY B 1 23  ? -31.283 26.920 7.127   1.00 32.31 ? 23  GLY B N   1 
ATOM   4255 C CA  . GLY B 1 23  ? -30.388 26.696 8.242   1.00 29.86 ? 23  GLY B CA  1 
ATOM   4256 C C   . GLY B 1 23  ? -29.422 27.824 8.512   1.00 31.47 ? 23  GLY B C   1 
ATOM   4257 O O   . GLY B 1 23  ? -28.576 27.694 9.400   1.00 33.63 ? 23  GLY B O   1 
ATOM   4258 N N   . GLU B 1 24  ? -29.531 28.948 7.809   1.00 25.92 ? 24  GLU B N   1 
ATOM   4259 C CA  . GLU B 1 24  ? -28.552 30.022 7.943   1.00 22.75 ? 24  GLU B CA  1 
ATOM   4260 C C   . GLU B 1 24  ? -28.933 30.986 9.055   1.00 22.32 ? 24  GLU B C   1 
ATOM   4261 O O   . GLU B 1 24  ? -30.088 31.415 9.145   1.00 26.69 ? 24  GLU B O   1 
ATOM   4262 C CB  . GLU B 1 24  ? -28.391 30.785 6.628   1.00 31.75 ? 24  GLU B CB  1 
ATOM   4263 C CG  . GLU B 1 24  ? -27.915 29.899 5.491   1.00 36.12 ? 24  GLU B CG  1 
ATOM   4264 C CD  . GLU B 1 24  ? -28.104 30.532 4.124   1.00 50.10 ? 24  GLU B CD  1 
ATOM   4265 O OE1 . GLU B 1 24  ? -28.909 31.481 3.991   1.00 54.29 ? 24  GLU B OE1 1 
ATOM   4266 O OE2 . GLU B 1 24  ? -27.457 30.057 3.172   1.00 58.25 ? 24  GLU B OE2 1 
ATOM   4267 N N   . TYR B 1 25  ? -27.950 31.337 9.881   1.00 22.58 ? 25  TYR B N   1 
ATOM   4268 C CA  . TYR B 1 25  ? -28.093 32.436 10.835  1.00 18.87 ? 25  TYR B CA  1 
ATOM   4269 C C   . TYR B 1 25  ? -28.018 33.743 10.054  1.00 27.84 ? 25  TYR B C   1 
ATOM   4270 O O   . TYR B 1 25  ? -26.957 34.086 9.510   1.00 23.90 ? 25  TYR B O   1 
ATOM   4271 C CB  . TYR B 1 25  ? -27.006 32.364 11.906  1.00 19.40 ? 25  TYR B CB  1 
ATOM   4272 C CG  . TYR B 1 25  ? -27.331 31.354 12.996  1.00 23.38 ? 25  TYR B CG  1 
ATOM   4273 C CD1 . TYR B 1 25  ? -27.203 29.988 12.763  1.00 24.36 ? 25  TYR B CD1 1 
ATOM   4274 C CD2 . TYR B 1 25  ? -27.773 31.768 14.251  1.00 22.45 ? 25  TYR B CD2 1 
ATOM   4275 C CE1 . TYR B 1 25  ? -27.504 29.059 13.743  1.00 27.23 ? 25  TYR B CE1 1 
ATOM   4276 C CE2 . TYR B 1 25  ? -28.074 30.848 15.241  1.00 25.81 ? 25  TYR B CE2 1 
ATOM   4277 C CZ  . TYR B 1 25  ? -27.939 29.493 14.981  1.00 28.38 ? 25  TYR B CZ  1 
ATOM   4278 O OH  . TYR B 1 25  ? -28.234 28.558 15.959  1.00 26.03 ? 25  TYR B OH  1 
ATOM   4279 N N   . LEU B 1 26  ? -29.149 34.459 9.972   1.00 23.32 ? 26  LEU B N   1 
ATOM   4280 C CA  . LEU B 1 26  ? -29.261 35.605 9.073   1.00 26.50 ? 26  LEU B CA  1 
ATOM   4281 C C   . LEU B 1 26  ? -28.755 36.907 9.680   1.00 23.49 ? 26  LEU B C   1 
ATOM   4282 O O   . LEU B 1 26  ? -28.601 37.894 8.943   1.00 26.31 ? 26  LEU B O   1 
ATOM   4283 C CB  . LEU B 1 26  ? -30.718 35.783 8.620   1.00 27.55 ? 26  LEU B CB  1 
ATOM   4284 C CG  . LEU B 1 26  ? -31.364 34.630 7.838   1.00 29.66 ? 26  LEU B CG  1 
ATOM   4285 C CD1 . LEU B 1 26  ? -32.763 35.023 7.316   1.00 27.56 ? 26  LEU B CD1 1 
ATOM   4286 C CD2 . LEU B 1 26  ? -30.467 34.144 6.682   1.00 25.97 ? 26  LEU B CD2 1 
ATOM   4287 N N   . LEU B 1 27  ? -28.525 36.946 10.991  1.00 18.66 ? 27  LEU B N   1 
ATOM   4288 C CA  . LEU B 1 27  ? -27.842 38.044 11.649  1.00 23.00 ? 27  LEU B CA  1 
ATOM   4289 C C   . LEU B 1 27  ? -26.824 37.458 12.612  1.00 20.64 ? 27  LEU B C   1 
ATOM   4290 O O   . LEU B 1 27  ? -27.033 36.361 13.136  1.00 20.49 ? 27  LEU B O   1 
ATOM   4291 C CB  . LEU B 1 27  ? -28.819 38.943 12.426  1.00 18.38 ? 27  LEU B CB  1 
ATOM   4292 C CG  . LEU B 1 27  ? -29.765 39.770 11.548  1.00 21.34 ? 27  LEU B CG  1 
ATOM   4293 C CD1 . LEU B 1 27  ? -30.888 40.313 12.415  1.00 21.99 ? 27  LEU B CD1 1 
ATOM   4294 C CD2 . LEU B 1 27  ? -29.024 40.889 10.844  1.00 23.13 ? 27  LEU B CD2 1 
ATOM   4295 N N   . PRO B 1 28  ? -25.718 38.166 12.868  1.00 19.11 ? 28  PRO B N   1 
ATOM   4296 C CA  . PRO B 1 28  ? -24.649 37.598 13.699  1.00 15.74 ? 28  PRO B CA  1 
ATOM   4297 C C   . PRO B 1 28  ? -24.723 37.991 15.163  1.00 17.49 ? 28  PRO B C   1 
ATOM   4298 O O   . PRO B 1 28  ? -23.754 37.784 15.902  1.00 20.07 ? 28  PRO B O   1 
ATOM   4299 C CB  . PRO B 1 28  ? -23.389 38.182 13.052  1.00 20.09 ? 28  PRO B CB  1 
ATOM   4300 C CG  . PRO B 1 28  ? -23.841 39.577 12.679  1.00 21.86 ? 28  PRO B CG  1 
ATOM   4301 C CD  . PRO B 1 28  ? -25.312 39.456 12.277  1.00 19.62 ? 28  PRO B CD  1 
ATOM   4302 N N   . TRP B 1 29  ? -25.859 38.528 15.618  1.00 22.79 ? 29  TRP B N   1 
ATOM   4303 C CA  . TRP B 1 29  ? -25.885 39.127 16.954  1.00 19.44 ? 29  TRP B CA  1 
ATOM   4304 C C   . TRP B 1 29  ? -25.604 38.118 18.065  1.00 19.54 ? 29  TRP B C   1 
ATOM   4305 O O   . TRP B 1 29  ? -25.011 38.482 19.095  1.00 18.18 ? 29  TRP B O   1 
ATOM   4306 C CB  . TRP B 1 29  ? -27.226 39.809 17.201  1.00 20.16 ? 29  TRP B CB  1 
ATOM   4307 C CG  . TRP B 1 29  ? -27.489 40.967 16.257  1.00 19.63 ? 29  TRP B CG  1 
ATOM   4308 C CD1 . TRP B 1 29  ? -28.559 41.116 15.459  1.00 18.72 ? 29  TRP B CD1 1 
ATOM   4309 C CD2 . TRP B 1 29  ? -26.657 42.129 16.045  1.00 21.19 ? 29  TRP B CD2 1 
ATOM   4310 N NE1 . TRP B 1 29  ? -28.475 42.297 14.764  1.00 19.51 ? 29  TRP B NE1 1 
ATOM   4311 C CE2 . TRP B 1 29  ? -27.318 42.941 15.110  1.00 22.94 ? 29  TRP B CE2 1 
ATOM   4312 C CE3 . TRP B 1 29  ? -25.438 42.574 16.586  1.00 23.73 ? 29  TRP B CE3 1 
ATOM   4313 C CZ2 . TRP B 1 29  ? -26.803 44.173 14.679  1.00 21.89 ? 29  TRP B CZ2 1 
ATOM   4314 C CZ3 . TRP B 1 29  ? -24.915 43.794 16.155  1.00 26.02 ? 29  TRP B CZ3 1 
ATOM   4315 C CH2 . TRP B 1 29  ? -25.596 44.579 15.213  1.00 28.93 ? 29  TRP B CH2 1 
ATOM   4316 N N   . THR B 1 30  ? -26.029 36.862 17.906  1.00 18.45 ? 30  THR B N   1 
ATOM   4317 C CA  . THR B 1 30  ? -25.711 35.882 18.942  1.00 16.58 ? 30  THR B CA  1 
ATOM   4318 C C   . THR B 1 30  ? -24.212 35.650 19.032  1.00 17.48 ? 30  THR B C   1 
ATOM   4319 O O   . THR B 1 30  ? -23.663 35.570 20.136  1.00 19.01 ? 30  THR B O   1 
ATOM   4320 C CB  . THR B 1 30  ? -26.439 34.560 18.697  1.00 20.70 ? 30  THR B CB  1 
ATOM   4321 O OG1 . THR B 1 30  ? -27.841 34.782 18.769  1.00 18.30 ? 30  THR B OG1 1 
ATOM   4322 C CG2 . THR B 1 30  ? -26.054 33.524 19.761  1.00 19.17 ? 30  THR B CG2 1 
ATOM   4323 N N   . PHE B 1 31  ? -23.531 35.542 17.883  1.00 17.68 ? 31  PHE B N   1 
ATOM   4324 C CA  . PHE B 1 31  ? -22.075 35.381 17.893  1.00 18.01 ? 31  PHE B CA  1 
ATOM   4325 C C   . PHE B 1 31  ? -21.398 36.567 18.567  1.00 18.29 ? 31  PHE B C   1 
ATOM   4326 O O   . PHE B 1 31  ? -20.544 36.398 19.437  1.00 15.42 ? 31  PHE B O   1 
ATOM   4327 C CB  . PHE B 1 31  ? -21.549 35.222 16.463  1.00 17.17 ? 31  PHE B CB  1 
ATOM   4328 C CG  . PHE B 1 31  ? -20.033 35.176 16.368  1.00 19.33 ? 31  PHE B CG  1 
ATOM   4329 C CD1 . PHE B 1 31  ? -19.358 33.988 16.564  1.00 19.01 ? 31  PHE B CD1 1 
ATOM   4330 C CD2 . PHE B 1 31  ? -19.304 36.315 16.066  1.00 16.45 ? 31  PHE B CD2 1 
ATOM   4331 C CE1 . PHE B 1 31  ? -17.968 33.922 16.463  1.00 22.44 ? 31  PHE B CE1 1 
ATOM   4332 C CE2 . PHE B 1 31  ? -17.922 36.274 15.992  1.00 20.35 ? 31  PHE B CE2 1 
ATOM   4333 C CZ  . PHE B 1 31  ? -17.245 35.067 16.184  1.00 19.53 ? 31  PHE B CZ  1 
ATOM   4334 N N   . PHE B 1 32  ? -21.780 37.782 18.184  1.00 16.27 ? 32  PHE B N   1 
ATOM   4335 C CA  . PHE B 1 32  ? -21.077 38.960 18.677  1.00 15.74 ? 32  PHE B CA  1 
ATOM   4336 C C   . PHE B 1 32  ? -21.297 39.166 20.172  1.00 19.00 ? 32  PHE B C   1 
ATOM   4337 O O   . PHE B 1 32  ? -20.352 39.485 20.911  1.00 16.04 ? 32  PHE B O   1 
ATOM   4338 C CB  . PHE B 1 32  ? -21.501 40.183 17.853  1.00 13.23 ? 32  PHE B CB  1 
ATOM   4339 C CG  . PHE B 1 32  ? -20.751 40.282 16.560  1.00 24.58 ? 32  PHE B CG  1 
ATOM   4340 C CD1 . PHE B 1 32  ? -19.368 40.253 16.575  1.00 19.06 ? 32  PHE B CD1 1 
ATOM   4341 C CD2 . PHE B 1 32  ? -21.412 40.318 15.339  1.00 24.58 ? 32  PHE B CD2 1 
ATOM   4342 C CE1 . PHE B 1 32  ? -18.634 40.318 15.386  1.00 26.53 ? 32  PHE B CE1 1 
ATOM   4343 C CE2 . PHE B 1 32  ? -20.690 40.368 14.149  1.00 27.90 ? 32  PHE B CE2 1 
ATOM   4344 C CZ  . PHE B 1 32  ? -19.305 40.369 14.168  1.00 21.79 ? 32  PHE B CZ  1 
ATOM   4345 N N   . HIS B 1 33  ? -22.521 38.976 20.645  1.00 15.33 ? 33  HIS B N   1 
ATOM   4346 C CA  . HIS B 1 33  ? -22.740 39.131 22.077  1.00 15.10 ? 33  HIS B CA  1 
ATOM   4347 C C   . HIS B 1 33  ? -22.189 37.955 22.872  1.00 15.98 ? 33  HIS B C   1 
ATOM   4348 O O   . HIS B 1 33  ? -21.854 38.115 24.062  1.00 14.92 ? 33  HIS B O   1 
ATOM   4349 C CB  . HIS B 1 33  ? -24.221 39.337 22.350  1.00 16.55 ? 33  HIS B CB  1 
ATOM   4350 C CG  . HIS B 1 33  ? -24.701 40.716 22.014  1.00 16.48 ? 33  HIS B CG  1 
ATOM   4351 N ND1 . HIS B 1 33  ? -24.271 41.842 22.692  1.00 17.50 ? 33  HIS B ND1 1 
ATOM   4352 C CD2 . HIS B 1 33  ? -25.579 41.147 21.078  1.00 12.47 ? 33  HIS B CD2 1 
ATOM   4353 C CE1 . HIS B 1 33  ? -24.868 42.907 22.181  1.00 17.23 ? 33  HIS B CE1 1 
ATOM   4354 N NE2 . HIS B 1 33  ? -25.673 42.510 21.207  1.00 15.25 ? 33  HIS B NE2 1 
ATOM   4355 N N   . ALA B 1 34  ? -22.034 36.789 22.240  1.00 17.11 ? 34  ALA B N   1 
ATOM   4356 C CA  . ALA B 1 34  ? -21.382 35.675 22.924  1.00 16.62 ? 34  ALA B CA  1 
ATOM   4357 C C   . ALA B 1 34  ? -19.909 35.972 23.174  1.00 19.11 ? 34  ALA B C   1 
ATOM   4358 O O   . ALA B 1 34  ? -19.416 35.775 24.290  1.00 17.91 ? 34  ALA B O   1 
ATOM   4359 C CB  . ALA B 1 34  ? -21.543 34.374 22.127  1.00 16.29 ? 34  ALA B CB  1 
ATOM   4360 N N   . VAL B 1 35  ? -19.187 36.464 22.155  1.00 16.20 ? 35  VAL B N   1 
ATOM   4361 C CA  . VAL B 1 35  ? -17.762 36.711 22.361  1.00 14.80 ? 35  VAL B CA  1 
ATOM   4362 C C   . VAL B 1 35  ? -17.528 37.946 23.223  1.00 18.26 ? 35  VAL B C   1 
ATOM   4363 O O   . VAL B 1 35  ? -16.492 38.041 23.883  1.00 17.10 ? 35  VAL B O   1 
ATOM   4364 C CB  . VAL B 1 35  ? -17.000 36.820 21.019  1.00 17.79 ? 35  VAL B CB  1 
ATOM   4365 C CG1 . VAL B 1 35  ? -17.254 35.575 20.176  1.00 24.73 ? 35  VAL B CG1 1 
ATOM   4366 C CG2 . VAL B 1 35  ? -17.403 38.085 20.237  1.00 17.44 ? 35  VAL B CG2 1 
ATOM   4367 N N   . LYS B 1 36  ? -18.477 38.877 23.266  1.00 16.41 ? 36  LYS B N   1 
ATOM   4368 C CA  . LYS B 1 36  ? -18.281 40.129 23.976  1.00 13.61 ? 36  LYS B CA  1 
ATOM   4369 C C   . LYS B 1 36  ? -18.854 40.097 25.386  1.00 16.70 ? 36  LYS B C   1 
ATOM   4370 O O   . LYS B 1 36  ? -18.204 40.590 26.318  1.00 19.48 ? 36  LYS B O   1 
ATOM   4371 C CB  . LYS B 1 36  ? -18.903 41.298 23.190  1.00 16.33 ? 36  LYS B CB  1 
ATOM   4372 C CG  . LYS B 1 36  ? -18.572 42.670 23.808  1.00 18.57 ? 36  LYS B CG  1 
ATOM   4373 C CD  . LYS B 1 36  ? -19.041 43.856 22.979  1.00 16.21 ? 36  LYS B CD  1 
ATOM   4374 C CE  . LYS B 1 36  ? -20.532 44.172 23.143  1.00 20.47 ? 36  LYS B CE  1 
ATOM   4375 N NZ  . LYS B 1 36  ? -20.947 44.624 24.523  1.00 16.67 ? 36  LYS B NZ  1 
ATOM   4376 N N   . ASP B 1 37  ? -20.045 39.512 25.571  1.00 17.66 ? 37  ASP B N   1 
ATOM   4377 C CA  . ASP B 1 37  ? -20.787 39.632 26.835  1.00 11.95 ? 37  ASP B CA  1 
ATOM   4378 C C   . ASP B 1 37  ? -21.140 38.304 27.501  1.00 15.46 ? 37  ASP B C   1 
ATOM   4379 O O   . ASP B 1 37  ? -21.085 38.208 28.725  1.00 17.14 ? 37  ASP B O   1 
ATOM   4380 C CB  . ASP B 1 37  ? -22.078 40.435 26.590  1.00 16.52 ? 37  ASP B CB  1 
ATOM   4381 C CG  . ASP B 1 37  ? -21.804 41.703 25.819  1.00 21.16 ? 37  ASP B CG  1 
ATOM   4382 O OD1 . ASP B 1 37  ? -21.011 42.542 26.352  1.00 17.06 ? 37  ASP B OD1 1 
ATOM   4383 O OD2 . ASP B 1 37  ? -22.321 41.829 24.678  1.00 16.40 ? 37  ASP B OD2 1 
ATOM   4384 N N   . TYR B 1 38  ? -21.567 37.272 26.757  1.00 15.73 ? 38  TYR B N   1 
ATOM   4385 C CA  . TYR B 1 38  ? -22.195 36.137 27.450  1.00 11.72 ? 38  TYR B CA  1 
ATOM   4386 C C   . TYR B 1 38  ? -21.196 35.323 28.273  1.00 12.74 ? 38  TYR B C   1 
ATOM   4387 O O   . TYR B 1 38  ? -21.574 34.743 29.298  1.00 16.04 ? 38  TYR B O   1 
ATOM   4388 C CB  . TYR B 1 38  ? -22.926 35.230 26.456  1.00 11.18 ? 38  TYR B CB  1 
ATOM   4389 C CG  . TYR B 1 38  ? -24.107 35.943 25.802  1.00 16.28 ? 38  TYR B CG  1 
ATOM   4390 C CD1 . TYR B 1 38  ? -24.845 36.893 26.501  1.00 14.34 ? 38  TYR B CD1 1 
ATOM   4391 C CD2 . TYR B 1 38  ? -24.457 35.678 24.483  1.00 13.28 ? 38  TYR B CD2 1 
ATOM   4392 C CE1 . TYR B 1 38  ? -25.907 37.574 25.896  1.00 17.29 ? 38  TYR B CE1 1 
ATOM   4393 C CE2 . TYR B 1 38  ? -25.509 36.341 23.876  1.00 15.08 ? 38  TYR B CE2 1 
ATOM   4394 C CZ  . TYR B 1 38  ? -26.237 37.269 24.585  1.00 17.58 ? 38  TYR B CZ  1 
ATOM   4395 O OH  . TYR B 1 38  ? -27.278 37.921 23.977  1.00 16.86 ? 38  TYR B OH  1 
ATOM   4396 N N   . TYR B 1 39  ? -19.944 35.222 27.836  1.00 13.97 ? 39  TYR B N   1 
ATOM   4397 C CA  . TYR B 1 39  ? -18.947 34.559 28.680  1.00 13.87 ? 39  TYR B CA  1 
ATOM   4398 C C   . TYR B 1 39  ? -18.399 35.526 29.720  1.00 18.00 ? 39  TYR B C   1 
ATOM   4399 O O   . TYR B 1 39  ? -18.224 35.163 30.890  1.00 16.08 ? 39  TYR B O   1 
ATOM   4400 C CB  . TYR B 1 39  ? -17.796 34.004 27.838  1.00 15.87 ? 39  TYR B CB  1 
ATOM   4401 C CG  . TYR B 1 39  ? -16.646 33.483 28.676  1.00 18.90 ? 39  TYR B CG  1 
ATOM   4402 C CD1 . TYR B 1 39  ? -16.629 32.162 29.091  1.00 20.16 ? 39  TYR B CD1 1 
ATOM   4403 C CD2 . TYR B 1 39  ? -15.582 34.314 29.055  1.00 16.47 ? 39  TYR B CD2 1 
ATOM   4404 C CE1 . TYR B 1 39  ? -15.584 31.667 29.861  1.00 20.07 ? 39  TYR B CE1 1 
ATOM   4405 C CE2 . TYR B 1 39  ? -14.529 33.819 29.837  1.00 14.71 ? 39  TYR B CE2 1 
ATOM   4406 C CZ  . TYR B 1 39  ? -14.551 32.500 30.221  1.00 17.78 ? 39  TYR B CZ  1 
ATOM   4407 O OH  . TYR B 1 39  ? -13.538 31.979 30.995  1.00 22.14 ? 39  TYR B OH  1 
ATOM   4408 N N   . ASP B 1 40  ? -18.135 36.763 29.309  1.00 15.24 ? 40  ASP B N   1 
ATOM   4409 C CA  . ASP B 1 40  ? -17.391 37.677 30.162  1.00 15.98 ? 40  ASP B CA  1 
ATOM   4410 C C   . ASP B 1 40  ? -18.222 38.209 31.328  1.00 19.02 ? 40  ASP B C   1 
ATOM   4411 O O   . ASP B 1 40  ? -17.660 38.516 32.387  1.00 15.92 ? 40  ASP B O   1 
ATOM   4412 C CB  . ASP B 1 40  ? -16.829 38.818 29.315  1.00 16.86 ? 40  ASP B CB  1 
ATOM   4413 C CG  . ASP B 1 40  ? -15.502 38.438 28.676  1.00 20.99 ? 40  ASP B CG  1 
ATOM   4414 O OD1 . ASP B 1 40  ? -14.525 38.279 29.437  1.00 19.27 ? 40  ASP B OD1 1 
ATOM   4415 O OD2 . ASP B 1 40  ? -15.446 38.240 27.432  1.00 20.26 ? 40  ASP B OD2 1 
ATOM   4416 N N   . MET B 1 41  ? -19.547 38.352 31.167  1.00 13.84 ? 41  MET B N   1 
ATOM   4417 C CA  . MET B 1 41  ? -20.322 38.905 32.280  1.00 13.93 ? 41  MET B CA  1 
ATOM   4418 C C   . MET B 1 41  ? -20.311 37.980 33.498  1.00 12.90 ? 41  MET B C   1 
ATOM   4419 O O   . MET B 1 41  ? -19.984 38.457 34.600  1.00 13.70 ? 41  MET B O   1 
ATOM   4420 C CB  . MET B 1 41  ? -21.741 39.259 31.811  1.00 13.01 ? 41  MET B CB  1 
ATOM   4421 C CG  . MET B 1 41  ? -21.797 40.566 30.991  1.00 13.15 ? 41  MET B CG  1 
ATOM   4422 S SD  . MET B 1 41  ? -21.594 42.065 32.001  1.00 15.52 ? 41  MET B SD  1 
ATOM   4423 C CE  . MET B 1 41  ? -23.197 42.120 32.841  1.00 13.12 ? 41  MET B CE  1 
ATOM   4424 N N   . PRO B 1 42  ? -20.603 36.669 33.389  1.00 18.80 ? 42  PRO B N   1 
ATOM   4425 C CA  . PRO B 1 42  ? -20.377 35.788 34.552  1.00 17.01 ? 42  PRO B CA  1 
ATOM   4426 C C   . PRO B 1 42  ? -18.911 35.628 34.922  1.00 17.16 ? 42  PRO B C   1 
ATOM   4427 O O   . PRO B 1 42  ? -18.615 35.375 36.096  1.00 17.44 ? 42  PRO B O   1 
ATOM   4428 C CB  . PRO B 1 42  ? -20.989 34.445 34.116  1.00 18.34 ? 42  PRO B CB  1 
ATOM   4429 C CG  . PRO B 1 42  ? -21.002 34.511 32.603  1.00 15.22 ? 42  PRO B CG  1 
ATOM   4430 C CD  . PRO B 1 42  ? -21.297 35.941 32.305  1.00 13.40 ? 42  PRO B CD  1 
ATOM   4431 N N   . ALA B 1 43  ? -17.984 35.755 33.971  1.00 15.69 ? 43  ALA B N   1 
ATOM   4432 C CA  . ALA B 1 43  ? -16.566 35.574 34.295  1.00 12.75 ? 43  ALA B CA  1 
ATOM   4433 C C   . ALA B 1 43  ? -16.025 36.635 35.255  1.00 15.93 ? 43  ALA B C   1 
ATOM   4434 O O   . ALA B 1 43  ? -14.972 36.416 35.875  1.00 12.70 ? 43  ALA B O   1 
ATOM   4435 C CB  . ALA B 1 43  ? -15.719 35.565 33.005  1.00 14.75 ? 43  ALA B CB  1 
ATOM   4436 N N   . TYR B 1 44  ? -16.690 37.788 35.379  1.00 14.50 ? 44  TYR B N   1 
ATOM   4437 C CA  . TYR B 1 44  ? -16.293 38.747 36.406  1.00 14.12 ? 44  TYR B CA  1 
ATOM   4438 C C   . TYR B 1 44  ? -16.329 38.118 37.791  1.00 13.49 ? 44  TYR B C   1 
ATOM   4439 O O   . TYR B 1 44  ? -15.579 38.542 38.682  1.00 16.62 ? 44  TYR B O   1 
ATOM   4440 C CB  . TYR B 1 44  ? -17.209 39.974 36.406  1.00 12.41 ? 44  TYR B CB  1 
ATOM   4441 C CG  . TYR B 1 44  ? -16.957 41.058 35.361  1.00 13.17 ? 44  TYR B CG  1 
ATOM   4442 C CD1 . TYR B 1 44  ? -16.037 42.074 35.593  1.00 18.62 ? 44  TYR B CD1 1 
ATOM   4443 C CD2 . TYR B 1 44  ? -17.702 41.100 34.183  1.00 17.25 ? 44  TYR B CD2 1 
ATOM   4444 C CE1 . TYR B 1 44  ? -15.830 43.086 34.653  1.00 17.74 ? 44  TYR B CE1 1 
ATOM   4445 C CE2 . TYR B 1 44  ? -17.497 42.101 33.237  1.00 18.43 ? 44  TYR B CE2 1 
ATOM   4446 C CZ  . TYR B 1 44  ? -16.568 43.091 33.479  1.00 18.90 ? 44  TYR B CZ  1 
ATOM   4447 O OH  . TYR B 1 44  ? -16.377 44.085 32.532  1.00 17.11 ? 44  TYR B OH  1 
ATOM   4448 N N   . LEU B 1 45  ? -17.204 37.133 38.002  1.00 14.81 ? 45  LEU B N   1 
ATOM   4449 C CA  . LEU B 1 45  ? -17.302 36.498 39.314  1.00 15.73 ? 45  LEU B CA  1 
ATOM   4450 C C   . LEU B 1 45  ? -16.035 35.734 39.684  1.00 20.19 ? 45  LEU B C   1 
ATOM   4451 O O   . LEU B 1 45  ? -15.834 35.427 40.863  1.00 20.79 ? 45  LEU B O   1 
ATOM   4452 C CB  . LEU B 1 45  ? -18.517 35.564 39.360  1.00 16.98 ? 45  LEU B CB  1 
ATOM   4453 C CG  . LEU B 1 45  ? -19.893 36.248 39.304  1.00 16.66 ? 45  LEU B CG  1 
ATOM   4454 C CD1 . LEU B 1 45  ? -20.969 35.245 38.939  1.00 17.31 ? 45  LEU B CD1 1 
ATOM   4455 C CD2 . LEU B 1 45  ? -20.206 36.946 40.635  1.00 19.38 ? 45  LEU B CD2 1 
ATOM   4456 N N   . LYS B 1 46  ? -15.171 35.424 38.713  1.00 17.17 ? 46  LYS B N   1 
ATOM   4457 C CA  . LYS B 1 46  ? -13.911 34.775 39.039  1.00 19.49 ? 46  LYS B CA  1 
ATOM   4458 C C   . LYS B 1 46  ? -12.930 35.722 39.708  1.00 19.37 ? 46  LYS B C   1 
ATOM   4459 O O   . LYS B 1 46  ? -12.061 35.263 40.465  1.00 20.07 ? 46  LYS B O   1 
ATOM   4460 C CB  . LYS B 1 46  ? -13.287 34.191 37.757  1.00 20.65 ? 46  LYS B CB  1 
ATOM   4461 C CG  . LYS B 1 46  ? -14.223 33.226 37.022  1.00 21.92 ? 46  LYS B CG  1 
ATOM   4462 C CD  . LYS B 1 46  ? -14.453 31.956 37.844  1.00 42.71 ? 46  LYS B CD  1 
ATOM   4463 C CE  . LYS B 1 46  ? -15.722 31.198 37.420  1.00 51.82 ? 46  LYS B CE  1 
ATOM   4464 N NZ  . LYS B 1 46  ? -15.456 29.776 36.991  1.00 57.17 ? 46  LYS B NZ  1 
ATOM   4465 N N   . ASP B 1 47  ? -13.065 37.032 39.477  1.00 22.02 ? 47  ASP B N   1 
ATOM   4466 C CA  . ASP B 1 47  ? -12.113 38.004 40.000  1.00 18.71 ? 47  ASP B CA  1 
ATOM   4467 C C   . ASP B 1 47  ? -12.660 38.857 41.129  1.00 20.22 ? 47  ASP B C   1 
ATOM   4468 O O   . ASP B 1 47  ? -11.868 39.474 41.846  1.00 22.10 ? 47  ASP B O   1 
ATOM   4469 C CB  . ASP B 1 47  ? -11.631 38.940 38.880  1.00 19.22 ? 47  ASP B CB  1 
ATOM   4470 C CG  . ASP B 1 47  ? -10.911 38.185 37.767  1.00 30.36 ? 47  ASP B CG  1 
ATOM   4471 O OD1 . ASP B 1 47  ? -10.161 37.240 38.080  1.00 26.60 ? 47  ASP B OD1 1 
ATOM   4472 O OD2 . ASP B 1 47  ? -11.087 38.540 36.586  1.00 29.15 ? 47  ASP B OD2 1 
ATOM   4473 N N   . PHE B 1 48  ? -13.973 38.886 41.319  1.00 18.60 ? 48  PHE B N   1 
ATOM   4474 C CA  . PHE B 1 48  ? -14.615 39.774 42.287  1.00 19.73 ? 48  PHE B CA  1 
ATOM   4475 C C   . PHE B 1 48  ? -15.515 38.970 43.209  1.00 16.11 ? 48  PHE B C   1 
ATOM   4476 O O   . PHE B 1 48  ? -16.334 38.175 42.743  1.00 20.38 ? 48  PHE B O   1 
ATOM   4477 C CB  . PHE B 1 48  ? -15.402 40.857 41.550  1.00 13.95 ? 48  PHE B CB  1 
ATOM   4478 C CG  . PHE B 1 48  ? -14.509 41.777 40.759  1.00 18.73 ? 48  PHE B CG  1 
ATOM   4479 C CD1 . PHE B 1 48  ? -13.716 42.711 41.421  1.00 17.98 ? 48  PHE B CD1 1 
ATOM   4480 C CD2 . PHE B 1 48  ? -14.409 41.668 39.396  1.00 15.61 ? 48  PHE B CD2 1 
ATOM   4481 C CE1 . PHE B 1 48  ? -12.864 43.544 40.705  1.00 21.02 ? 48  PHE B CE1 1 
ATOM   4482 C CE2 . PHE B 1 48  ? -13.587 42.496 38.679  1.00 17.18 ? 48  PHE B CE2 1 
ATOM   4483 C CZ  . PHE B 1 48  ? -12.801 43.433 39.334  1.00 23.12 ? 48  PHE B CZ  1 
ATOM   4484 N N   . GLU B 1 49  ? -15.362 39.189 44.520  1.00 15.78 ? 49  GLU B N   1 
ATOM   4485 C CA  . GLU B 1 49  ? -16.022 38.367 45.535  1.00 16.76 ? 49  GLU B CA  1 
ATOM   4486 C C   . GLU B 1 49  ? -17.387 38.960 45.891  1.00 20.61 ? 49  GLU B C   1 
ATOM   4487 O O   . GLU B 1 49  ? -17.641 39.437 47.000  1.00 21.91 ? 49  GLU B O   1 
ATOM   4488 C CB  . GLU B 1 49  ? -15.118 38.231 46.757  1.00 22.95 ? 49  GLU B CB  1 
ATOM   4489 C CG  . GLU B 1 49  ? -15.447 37.051 47.619  1.00 38.17 ? 49  GLU B CG  1 
ATOM   4490 C CD  . GLU B 1 49  ? -14.887 35.754 47.076  1.00 51.74 ? 49  GLU B CD  1 
ATOM   4491 O OE1 . GLU B 1 49  ? -13.913 35.794 46.291  1.00 46.41 ? 49  GLU B OE1 1 
ATOM   4492 O OE2 . GLU B 1 49  ? -15.427 34.692 47.450  1.00 59.98 ? 49  GLU B OE2 1 
ATOM   4493 N N   . ILE B 1 50  ? -18.281 38.910 44.903  1.00 16.87 ? 50  ILE B N   1 
ATOM   4494 C CA  . ILE B 1 50  ? -19.655 39.384 45.015  1.00 19.84 ? 50  ILE B CA  1 
ATOM   4495 C C   . ILE B 1 50  ? -20.550 38.294 44.434  1.00 21.51 ? 50  ILE B C   1 
ATOM   4496 O O   . ILE B 1 50  ? -20.066 37.300 43.893  1.00 19.94 ? 50  ILE B O   1 
ATOM   4497 C CB  . ILE B 1 50  ? -19.857 40.716 44.272  1.00 18.18 ? 50  ILE B CB  1 
ATOM   4498 C CG1 . ILE B 1 50  ? -19.429 40.552 42.812  1.00 16.83 ? 50  ILE B CG1 1 
ATOM   4499 C CG2 . ILE B 1 50  ? -19.002 41.820 44.902  1.00 20.53 ? 50  ILE B CG2 1 
ATOM   4500 C CD1 . ILE B 1 50  ? -19.921 41.636 41.900  1.00 17.03 ? 50  ILE B CD1 1 
ATOM   4501 N N   . LYS B 1 51  ? -21.866 38.485 44.546  1.00 17.55 ? 51  LYS B N   1 
ATOM   4502 C CA  . LYS B 1 51  ? -22.845 37.617 43.887  1.00 16.01 ? 51  LYS B CA  1 
ATOM   4503 C C   . LYS B 1 51  ? -23.439 38.351 42.706  1.00 15.70 ? 51  LYS B C   1 
ATOM   4504 O O   . LYS B 1 51  ? -23.765 39.531 42.821  1.00 15.25 ? 51  LYS B O   1 
ATOM   4505 C CB  . LYS B 1 51  ? -23.992 37.203 44.830  1.00 13.94 ? 51  LYS B CB  1 
ATOM   4506 C CG  . LYS B 1 51  ? -23.571 36.603 46.167  1.00 19.64 ? 51  LYS B CG  1 
ATOM   4507 C CD  . LYS B 1 51  ? -22.853 35.290 45.979  1.00 19.53 ? 51  LYS B CD  1 
ATOM   4508 C CE  . LYS B 1 51  ? -22.769 34.569 47.312  1.00 30.58 ? 51  LYS B CE  1 
ATOM   4509 N NZ  . LYS B 1 51  ? -21.526 33.750 47.368  1.00 45.49 ? 51  LYS B NZ  1 
ATOM   4510 N N   . LEU B 1 52  ? -23.588 37.653 41.575  1.00 14.91 ? 52  LEU B N   1 
ATOM   4511 C CA  . LEU B 1 52  ? -24.276 38.209 40.416  1.00 15.04 ? 52  LEU B CA  1 
ATOM   4512 C C   . LEU B 1 52  ? -25.175 37.123 39.841  1.00 14.84 ? 52  LEU B C   1 
ATOM   4513 O O   . LEU B 1 52  ? -24.752 35.973 39.722  1.00 15.74 ? 52  LEU B O   1 
ATOM   4514 C CB  . LEU B 1 52  ? -23.298 38.691 39.321  1.00 13.04 ? 52  LEU B CB  1 
ATOM   4515 C CG  . LEU B 1 52  ? -22.383 39.861 39.683  1.00 11.94 ? 52  LEU B CG  1 
ATOM   4516 C CD1 . LEU B 1 52  ? -21.324 40.065 38.580  1.00 13.92 ? 52  LEU B CD1 1 
ATOM   4517 C CD2 . LEU B 1 52  ? -23.182 41.137 39.894  1.00 13.11 ? 52  LEU B CD2 1 
ATOM   4518 N N   . ASN B 1 53  ? -26.394 37.486 39.464  1.00 13.89 ? 53  ASN B N   1 
ATOM   4519 C CA  . ASN B 1 53  ? -27.348 36.530 38.914  1.00 12.45 ? 53  ASN B CA  1 
ATOM   4520 C C   . ASN B 1 53  ? -27.582 36.771 37.431  1.00 13.55 ? 53  ASN B C   1 
ATOM   4521 O O   . ASN B 1 53  ? -27.363 37.863 36.903  1.00 15.74 ? 53  ASN B O   1 
ATOM   4522 C CB  . ASN B 1 53  ? -28.689 36.607 39.669  1.00 12.60 ? 53  ASN B CB  1 
ATOM   4523 C CG  . ASN B 1 53  ? -28.490 36.489 41.175  1.00 15.70 ? 53  ASN B CG  1 
ATOM   4524 O OD1 . ASN B 1 53  ? -28.221 35.411 41.687  1.00 17.11 ? 53  ASN B OD1 1 
ATOM   4525 N ND2 . ASN B 1 53  ? -28.569 37.620 41.882  1.00 16.10 ? 53  ASN B ND2 1 
ATOM   4526 N N   . PHE B 1 54  ? -28.041 35.718 36.763  1.00 12.55 ? 54  PHE B N   1 
ATOM   4527 C CA  . PHE B 1 54  ? -28.194 35.755 35.315  1.00 15.20 ? 54  PHE B CA  1 
ATOM   4528 C C   . PHE B 1 54  ? -29.473 35.058 34.895  1.00 10.78 ? 54  PHE B C   1 
ATOM   4529 O O   . PHE B 1 54  ? -29.859 34.052 35.487  1.00 15.04 ? 54  PHE B O   1 
ATOM   4530 C CB  . PHE B 1 54  ? -26.994 35.074 34.640  1.00 14.70 ? 54  PHE B CB  1 
ATOM   4531 C CG  . PHE B 1 54  ? -25.720 35.759 34.931  1.00 12.14 ? 54  PHE B CG  1 
ATOM   4532 C CD1 . PHE B 1 54  ? -25.288 36.790 34.116  1.00 17.63 ? 54  PHE B CD1 1 
ATOM   4533 C CD2 . PHE B 1 54  ? -24.982 35.430 36.053  1.00 14.02 ? 54  PHE B CD2 1 
ATOM   4534 C CE1 . PHE B 1 54  ? -24.127 37.480 34.399  1.00 17.92 ? 54  PHE B CE1 1 
ATOM   4535 C CE2 . PHE B 1 54  ? -23.825 36.128 36.356  1.00 18.36 ? 54  PHE B CE2 1 
ATOM   4536 C CZ  . PHE B 1 54  ? -23.389 37.152 35.508  1.00 17.21 ? 54  PHE B CZ  1 
ATOM   4537 N N   . ASN B 1 55  ? -30.106 35.581 33.843  1.00 14.92 ? 55  ASN B N   1 
ATOM   4538 C CA  . ASN B 1 55  ? -31.155 34.875 33.129  1.00 13.73 ? 55  ASN B CA  1 
ATOM   4539 C C   . ASN B 1 55  ? -30.618 34.456 31.770  1.00 13.87 ? 55  ASN B C   1 
ATOM   4540 O O   . ASN B 1 55  ? -30.000 35.272 31.078  1.00 14.28 ? 55  ASN B O   1 
ATOM   4541 C CB  . ASN B 1 55  ? -32.375 35.766 32.924  1.00 14.90 ? 55  ASN B CB  1 
ATOM   4542 C CG  . ASN B 1 55  ? -33.537 35.017 32.345  1.00 15.65 ? 55  ASN B CG  1 
ATOM   4543 O OD1 . ASN B 1 55  ? -34.087 34.100 32.988  1.00 15.40 ? 55  ASN B OD1 1 
ATOM   4544 N ND2 . ASN B 1 55  ? -33.949 35.411 31.132  1.00 15.25 ? 55  ASN B ND2 1 
ATOM   4545 N N   . LEU B 1 56  ? -30.863 33.203 31.388  1.00 14.07 ? 56  LEU B N   1 
ATOM   4546 C CA  . LEU B 1 56  ? -30.560 32.713 30.044  1.00 16.34 ? 56  LEU B CA  1 
ATOM   4547 C C   . LEU B 1 56  ? -31.853 32.204 29.422  1.00 17.37 ? 56  LEU B C   1 
ATOM   4548 O O   . LEU B 1 56  ? -32.474 31.276 29.953  1.00 13.77 ? 56  LEU B O   1 
ATOM   4549 C CB  . LEU B 1 56  ? -29.514 31.591 30.080  1.00 17.56 ? 56  LEU B CB  1 
ATOM   4550 C CG  . LEU B 1 56  ? -28.135 31.864 30.674  1.00 20.23 ? 56  LEU B CG  1 
ATOM   4551 C CD1 . LEU B 1 56  ? -27.308 30.563 30.703  1.00 16.35 ? 56  LEU B CD1 1 
ATOM   4552 C CD2 . LEU B 1 56  ? -27.425 32.951 29.897  1.00 22.09 ? 56  LEU B CD2 1 
ATOM   4553 N N   . THR B 1 57  ? -32.278 32.809 28.317  1.00 16.74 ? 57  THR B N   1 
ATOM   4554 C CA  . THR B 1 57  ? -33.434 32.241 27.651  1.00 12.16 ? 57  THR B CA  1 
ATOM   4555 C C   . THR B 1 57  ? -33.050 30.953 26.915  1.00 15.53 ? 57  THR B C   1 
ATOM   4556 O O   . THR B 1 57  ? -31.929 30.810 26.413  1.00 14.94 ? 57  THR B O   1 
ATOM   4557 C CB  . THR B 1 57  ? -34.086 33.236 26.683  1.00 13.01 ? 57  THR B CB  1 
ATOM   4558 O OG1 . THR B 1 57  ? -33.250 33.460 25.553  1.00 15.62 ? 57  THR B OG1 1 
ATOM   4559 C CG2 . THR B 1 57  ? -34.351 34.540 27.401  1.00 15.13 ? 57  THR B CG2 1 
ATOM   4560 N N   . PRO B 1 58  ? -33.970 29.995 26.841  1.00 15.77 ? 58  PRO B N   1 
ATOM   4561 C CA  . PRO B 1 58  ? -33.626 28.719 26.210  1.00 13.35 ? 58  PRO B CA  1 
ATOM   4562 C C   . PRO B 1 58  ? -33.297 28.856 24.734  1.00 14.12 ? 58  PRO B C   1 
ATOM   4563 O O   . PRO B 1 58  ? -32.435 28.111 24.251  1.00 14.72 ? 58  PRO B O   1 
ATOM   4564 C CB  . PRO B 1 58  ? -34.867 27.858 26.468  1.00 15.19 ? 58  PRO B CB  1 
ATOM   4565 C CG  . PRO B 1 58  ? -35.548 28.515 27.698  1.00 16.17 ? 58  PRO B CG  1 
ATOM   4566 C CD  . PRO B 1 58  ? -35.289 29.967 27.510  1.00 19.60 ? 58  PRO B CD  1 
ATOM   4567 N N   . VAL B 1 59  ? -33.926 29.794 24.013  1.00 16.46 ? 59  VAL B N   1 
ATOM   4568 C CA  . VAL B 1 59  ? -33.589 29.990 22.597  1.00 20.76 ? 59  VAL B CA  1 
ATOM   4569 C C   . VAL B 1 59  ? -32.169 30.543 22.448  1.00 15.36 ? 59  VAL B C   1 
ATOM   4570 O O   . VAL B 1 59  ? -31.446 30.165 21.517  1.00 14.37 ? 59  VAL B O   1 
ATOM   4571 C CB  . VAL B 1 59  ? -34.640 30.879 21.893  1.00 13.36 ? 59  VAL B CB  1 
ATOM   4572 C CG1 . VAL B 1 59  ? -34.802 32.197 22.607  1.00 16.08 ? 59  VAL B CG1 1 
ATOM   4573 C CG2 . VAL B 1 59  ? -34.291 31.112 20.413  1.00 13.66 ? 59  VAL B CG2 1 
ATOM   4574 N N   . LEU B 1 60  ? -31.725 31.405 23.374  1.00 15.90 ? 60  LEU B N   1 
ATOM   4575 C CA  . LEU B 1 60  ? -30.308 31.793 23.373  1.00 14.75 ? 60  LEU B CA  1 
ATOM   4576 C C   . LEU B 1 60  ? -29.409 30.586 23.626  1.00 16.66 ? 60  LEU B C   1 
ATOM   4577 O O   . LEU B 1 60  ? -28.391 30.405 22.942  1.00 17.46 ? 60  LEU B O   1 
ATOM   4578 C CB  . LEU B 1 60  ? -30.018 32.872 24.423  1.00 14.41 ? 60  LEU B CB  1 
ATOM   4579 C CG  . LEU B 1 60  ? -28.516 33.238 24.563  1.00 14.15 ? 60  LEU B CG  1 
ATOM   4580 C CD1 . LEU B 1 60  ? -27.939 33.748 23.230  1.00 17.64 ? 60  LEU B CD1 1 
ATOM   4581 C CD2 . LEU B 1 60  ? -28.256 34.287 25.623  1.00 14.69 ? 60  LEU B CD2 1 
ATOM   4582 N N   . ILE B 1 61  ? -29.755 29.764 24.619  1.00 14.56 ? 61  ILE B N   1 
ATOM   4583 C CA  . ILE B 1 61  ? -28.949 28.578 24.909  1.00 15.55 ? 61  ILE B CA  1 
ATOM   4584 C C   . ILE B 1 61  ? -28.772 27.721 23.661  1.00 22.32 ? 61  ILE B C   1 
ATOM   4585 O O   . ILE B 1 61  ? -27.661 27.264 23.352  1.00 15.28 ? 61  ILE B O   1 
ATOM   4586 C CB  . ILE B 1 61  ? -29.571 27.775 26.060  1.00 17.24 ? 61  ILE B CB  1 
ATOM   4587 C CG1 . ILE B 1 61  ? -29.460 28.577 27.352  1.00 17.45 ? 61  ILE B CG1 1 
ATOM   4588 C CG2 . ILE B 1 61  ? -28.849 26.420 26.208  1.00 18.23 ? 61  ILE B CG2 1 
ATOM   4589 C CD1 . ILE B 1 61  ? -30.135 27.909 28.548  1.00 17.55 ? 61  ILE B CD1 1 
ATOM   4590 N N   . ASP B 1 62  ? -29.864 27.499 22.926  1.00 16.80 ? 62  ASP B N   1 
ATOM   4591 C CA  . ASP B 1 62  ? -29.812 26.644 21.741  1.00 17.22 ? 62  ASP B CA  1 
ATOM   4592 C C   . ASP B 1 62  ? -28.791 27.168 20.743  1.00 16.01 ? 62  ASP B C   1 
ATOM   4593 O O   . ASP B 1 62  ? -28.061 26.396 20.105  1.00 17.82 ? 62  ASP B O   1 
ATOM   4594 C CB  . ASP B 1 62  ? -31.184 26.597 21.070  1.00 20.81 ? 62  ASP B CB  1 
ATOM   4595 C CG  . ASP B 1 62  ? -32.136 25.618 21.717  1.00 28.25 ? 62  ASP B CG  1 
ATOM   4596 O OD1 . ASP B 1 62  ? -31.670 24.631 22.336  1.00 29.73 ? 62  ASP B OD1 1 
ATOM   4597 O OD2 . ASP B 1 62  ? -33.363 25.817 21.555  1.00 23.64 ? 62  ASP B OD2 1 
ATOM   4598 N N   . GLN B 1 63  ? -28.743 28.489 20.585  1.00 17.81 ? 63  GLN B N   1 
ATOM   4599 C CA  . GLN B 1 63  ? -27.865 29.083 19.587  1.00 14.63 ? 63  GLN B CA  1 
ATOM   4600 C C   . GLN B 1 63  ? -26.413 29.035 20.031  1.00 17.48 ? 63  GLN B C   1 
ATOM   4601 O O   . GLN B 1 63  ? -25.517 28.781 19.216  1.00 20.07 ? 63  GLN B O   1 
ATOM   4602 C CB  . GLN B 1 63  ? -28.314 30.523 19.321  1.00 14.58 ? 63  GLN B CB  1 
ATOM   4603 C CG  . GLN B 1 63  ? -29.694 30.606 18.665  1.00 18.36 ? 63  GLN B CG  1 
ATOM   4604 C CD  . GLN B 1 63  ? -30.160 32.042 18.546  1.00 20.25 ? 63  GLN B CD  1 
ATOM   4605 O OE1 . GLN B 1 63  ? -29.715 32.770 17.667  1.00 25.50 ? 63  GLN B OE1 1 
ATOM   4606 N NE2 . GLN B 1 63  ? -31.029 32.472 19.471  1.00 16.96 ? 63  GLN B NE2 1 
ATOM   4607 N N   . ILE B 1 64  ? -26.155 29.287 21.313  1.00 16.06 ? 64  ILE B N   1 
ATOM   4608 C CA  . ILE B 1 64  ? -24.792 29.148 21.822  1.00 16.70 ? 64  ILE B CA  1 
ATOM   4609 C C   . ILE B 1 64  ? -24.292 27.730 21.599  1.00 18.85 ? 64  ILE B C   1 
ATOM   4610 O O   . ILE B 1 64  ? -23.152 27.523 21.162  1.00 19.02 ? 64  ILE B O   1 
ATOM   4611 C CB  . ILE B 1 64  ? -24.720 29.548 23.308  1.00 15.52 ? 64  ILE B CB  1 
ATOM   4612 C CG1 . ILE B 1 64  ? -25.010 31.043 23.474  1.00 15.18 ? 64  ILE B CG1 1 
ATOM   4613 C CG2 . ILE B 1 64  ? -23.330 29.204 23.896  1.00 19.78 ? 64  ILE B CG2 1 
ATOM   4614 C CD1 . ILE B 1 64  ? -25.066 31.510 24.946  1.00 16.51 ? 64  ILE B CD1 1 
ATOM   4615 N N   . GLN B 1 65  ? -25.131 26.725 21.890  1.00 18.44 ? 65  GLN B N   1 
ATOM   4616 C CA  . GLN B 1 65  ? -24.716 25.342 21.666  1.00 20.12 ? 65  GLN B CA  1 
ATOM   4617 C C   . GLN B 1 65  ? -24.350 25.091 20.206  1.00 21.06 ? 65  GLN B C   1 
ATOM   4618 O O   . GLN B 1 65  ? -23.398 24.352 19.917  1.00 19.11 ? 65  GLN B O   1 
ATOM   4619 C CB  . GLN B 1 65  ? -25.819 24.377 22.091  1.00 22.89 ? 65  GLN B CB  1 
ATOM   4620 C CG  . GLN B 1 65  ? -26.002 24.288 23.609  1.00 21.96 ? 65  GLN B CG  1 
ATOM   4621 C CD  . GLN B 1 65  ? -27.094 23.323 23.988  1.00 24.98 ? 65  GLN B CD  1 
ATOM   4622 O OE1 . GLN B 1 65  ? -28.225 23.436 23.508  1.00 23.05 ? 65  GLN B OE1 1 
ATOM   4623 N NE2 . GLN B 1 65  ? -26.762 22.349 24.842  1.00 27.27 ? 65  GLN B NE2 1 
ATOM   4624 N N   . GLU B 1 66  ? -25.105 25.686 19.268  1.00 18.09 ? 66  GLU B N   1 
ATOM   4625 C CA  . GLU B 1 66  ? -24.844 25.437 17.850  1.00 20.26 ? 66  GLU B CA  1 
ATOM   4626 C C   . GLU B 1 66  ? -23.531 26.081 17.406  1.00 19.19 ? 66  GLU B C   1 
ATOM   4627 O O   . GLU B 1 66  ? -22.750 25.453 16.680  1.00 21.86 ? 66  GLU B O   1 
ATOM   4628 C CB  . GLU B 1 66  ? -26.023 25.934 16.995  1.00 24.39 ? 66  GLU B CB  1 
ATOM   4629 C CG  . GLU B 1 66  ? -25.914 25.591 15.491  1.00 32.08 ? 66  GLU B CG  1 
ATOM   4630 C CD  . GLU B 1 66  ? -27.249 25.675 14.742  1.00 35.77 ? 66  GLU B CD  1 
ATOM   4631 O OE1 . GLU B 1 66  ? -28.266 26.031 15.364  1.00 29.77 ? 66  GLU B OE1 1 
ATOM   4632 O OE2 . GLU B 1 66  ? -27.283 25.378 13.516  1.00 37.22 ? 66  GLU B OE2 1 
ATOM   4633 N N   . TYR B 1 67  ? -23.275 27.332 17.819  1.00 16.50 ? 67  TYR B N   1 
ATOM   4634 C CA  . TYR B 1 67  ? -21.994 27.963 17.510  1.00 17.29 ? 67  TYR B CA  1 
ATOM   4635 C C   . TYR B 1 67  ? -20.847 27.185 18.142  1.00 22.40 ? 67  TYR B C   1 
ATOM   4636 O O   . TYR B 1 67  ? -19.809 26.974 17.508  1.00 24.38 ? 67  TYR B O   1 
ATOM   4637 C CB  . TYR B 1 67  ? -21.965 29.411 18.002  1.00 16.29 ? 67  TYR B CB  1 
ATOM   4638 C CG  . TYR B 1 67  ? -22.629 30.415 17.071  1.00 17.64 ? 67  TYR B CG  1 
ATOM   4639 C CD1 . TYR B 1 67  ? -21.937 30.948 15.980  1.00 18.41 ? 67  TYR B CD1 1 
ATOM   4640 C CD2 . TYR B 1 67  ? -23.947 30.817 17.277  1.00 23.64 ? 67  TYR B CD2 1 
ATOM   4641 C CE1 . TYR B 1 67  ? -22.544 31.880 15.125  1.00 20.33 ? 67  TYR B CE1 1 
ATOM   4642 C CE2 . TYR B 1 67  ? -24.564 31.731 16.420  1.00 24.63 ? 67  TYR B CE2 1 
ATOM   4643 C CZ  . TYR B 1 67  ? -23.854 32.259 15.355  1.00 23.77 ? 67  TYR B CZ  1 
ATOM   4644 O OH  . TYR B 1 67  ? -24.460 33.174 14.530  1.00 21.70 ? 67  TYR B OH  1 
ATOM   4645 N N   . ALA B 1 68  ? -21.028 26.731 19.390  1.00 21.88 ? 68  ALA B N   1 
ATOM   4646 C CA  . ALA B 1 68  ? -19.958 26.016 20.083  1.00 20.13 ? 68  ALA B CA  1 
ATOM   4647 C C   . ALA B 1 68  ? -19.610 24.706 19.399  1.00 21.15 ? 68  ALA B C   1 
ATOM   4648 O O   . ALA B 1 68  ? -18.460 24.260 19.464  1.00 30.24 ? 68  ALA B O   1 
ATOM   4649 C CB  . ALA B 1 68  ? -20.348 25.757 21.544  1.00 21.14 ? 68  ALA B CB  1 
ATOM   4650 N N   . GLN B 1 69  ? -20.578 24.060 18.761  1.00 24.62 ? 69  GLN B N   1 
ATOM   4651 C CA  . GLN B 1 69  ? -20.308 22.816 18.058  1.00 26.07 ? 69  GLN B CA  1 
ATOM   4652 C C   . GLN B 1 69  ? -19.797 23.042 16.644  1.00 32.60 ? 69  GLN B C   1 
ATOM   4653 O O   . GLN B 1 69  ? -19.546 22.065 15.932  1.00 37.56 ? 69  GLN B O   1 
ATOM   4654 C CB  . GLN B 1 69  ? -21.565 21.947 18.024  1.00 29.54 ? 69  GLN B CB  1 
ATOM   4655 C CG  . GLN B 1 69  ? -21.938 21.393 19.389  1.00 41.89 ? 69  GLN B CG  1 
ATOM   4656 C CD  . GLN B 1 69  ? -23.356 20.863 19.443  1.00 55.80 ? 69  GLN B CD  1 
ATOM   4657 O OE1 . GLN B 1 69  ? -23.893 20.376 18.444  1.00 63.45 ? 69  GLN B OE1 1 
ATOM   4658 N NE2 . GLN B 1 69  ? -23.972 20.955 20.613  1.00 58.20 ? 69  GLN B NE2 1 
ATOM   4659 N N   . GLY B 1 70  ? -19.637 24.296 16.223  1.00 28.79 ? 70  GLY B N   1 
ATOM   4660 C CA  . GLY B 1 70  ? -19.257 24.589 14.858  1.00 32.86 ? 70  GLY B CA  1 
ATOM   4661 C C   . GLY B 1 70  ? -20.356 24.374 13.842  1.00 33.31 ? 70  GLY B C   1 
ATOM   4662 O O   . GLY B 1 70  ? -20.069 24.328 12.643  1.00 42.20 ? 70  GLY B O   1 
ATOM   4663 N N   . LYS B 1 71  ? -21.609 24.249 14.283  1.00 30.50 ? 71  LYS B N   1 
ATOM   4664 C CA  . LYS B 1 71  ? -22.724 23.955 13.389  1.00 34.59 ? 71  LYS B CA  1 
ATOM   4665 C C   . LYS B 1 71  ? -23.364 25.197 12.779  1.00 35.79 ? 71  LYS B C   1 
ATOM   4666 O O   . LYS B 1 71  ? -24.045 25.080 11.755  1.00 36.59 ? 71  LYS B O   1 
ATOM   4667 C CB  . LYS B 1 71  ? -23.818 23.165 14.124  1.00 34.27 ? 71  LYS B CB  1 
ATOM   4668 C CG  . LYS B 1 71  ? -23.358 21.885 14.796  1.00 43.90 ? 71  LYS B CG  1 
ATOM   4669 C CD  . LYS B 1 71  ? -22.860 20.887 13.780  1.00 50.77 ? 71  LYS B CD  1 
ATOM   4670 C CE  . LYS B 1 71  ? -24.004 20.217 13.042  1.00 55.68 ? 71  LYS B CE  1 
ATOM   4671 N NZ  . LYS B 1 71  ? -23.499 19.331 11.956  1.00 62.00 ? 71  LYS B NZ  1 
ATOM   4672 N N   . ALA B 1 72  ? -23.177 26.374 13.373  1.00 30.46 ? 72  ALA B N   1 
ATOM   4673 C CA  . ALA B 1 72  ? -23.919 27.556 12.956  1.00 26.71 ? 72  ALA B CA  1 
ATOM   4674 C C   . ALA B 1 72  ? -23.352 28.092 11.645  1.00 24.34 ? 72  ALA B C   1 
ATOM   4675 O O   . ALA B 1 72  ? -22.167 28.437 11.565  1.00 31.87 ? 72  ALA B O   1 
ATOM   4676 C CB  . ALA B 1 72  ? -23.872 28.627 14.046  1.00 26.09 ? 72  ALA B CB  1 
ATOM   4677 N N   . LYS B 1 73  ? -24.195 28.138 10.616  1.00 23.23 ? 73  LYS B N   1 
ATOM   4678 C CA  . LYS B 1 73  ? -23.845 28.749 9.336   1.00 23.44 ? 73  LYS B CA  1 
ATOM   4679 C C   . LYS B 1 73  ? -24.284 30.208 9.393   1.00 25.52 ? 73  LYS B C   1 
ATOM   4680 O O   . LYS B 1 73  ? -25.439 30.542 9.137   1.00 29.13 ? 73  LYS B O   1 
ATOM   4681 C CB  . LYS B 1 73  ? -24.503 27.993 8.189   1.00 28.14 ? 73  LYS B CB  1 
ATOM   4682 C CG  . LYS B 1 73  ? -23.726 28.056 6.890   1.00 40.45 ? 73  LYS B CG  1 
ATOM   4683 C CD  . LYS B 1 73  ? -24.467 27.380 5.742   1.00 50.60 ? 73  LYS B CD  1 
ATOM   4684 C CE  . LYS B 1 73  ? -24.576 28.312 4.537   1.00 51.10 ? 73  LYS B CE  1 
ATOM   4685 N NZ  . LYS B 1 73  ? -23.240 28.754 4.047   1.00 50.90 ? 73  LYS B NZ  1 
ATOM   4686 N N   . ASP B 1 74  ? -23.348 31.089 9.735   1.00 24.82 ? 74  ASP B N   1 
ATOM   4687 C CA  . ASP B 1 74  ? -23.639 32.498 10.009  1.00 27.10 ? 74  ASP B CA  1 
ATOM   4688 C C   . ASP B 1 74  ? -23.199 33.316 8.802   1.00 28.39 ? 74  ASP B C   1 
ATOM   4689 O O   . ASP B 1 74  ? -21.998 33.442 8.548   1.00 24.73 ? 74  ASP B O   1 
ATOM   4690 C CB  . ASP B 1 74  ? -22.910 32.941 11.278  1.00 21.18 ? 74  ASP B CB  1 
ATOM   4691 C CG  . ASP B 1 74  ? -23.183 34.393 11.660  1.00 23.48 ? 74  ASP B CG  1 
ATOM   4692 O OD1 . ASP B 1 74  ? -23.184 35.273 10.759  1.00 25.39 ? 74  ASP B OD1 1 
ATOM   4693 O OD2 . ASP B 1 74  ? -23.363 34.666 12.881  1.00 20.16 ? 74  ASP B OD2 1 
ATOM   4694 N N   . VAL B 1 75  ? -24.163 33.891 8.069   1.00 22.95 ? 75  VAL B N   1 
ATOM   4695 C CA  . VAL B 1 75  ? -23.827 34.453 6.760   1.00 21.74 ? 75  VAL B CA  1 
ATOM   4696 C C   . VAL B 1 75  ? -22.897 35.651 6.902   1.00 29.37 ? 75  VAL B C   1 
ATOM   4697 O O   . VAL B 1 75  ? -21.952 35.815 6.119   1.00 27.03 ? 75  VAL B O   1 
ATOM   4698 C CB  . VAL B 1 75  ? -25.101 34.798 5.958   1.00 25.67 ? 75  VAL B CB  1 
ATOM   4699 C CG1 . VAL B 1 75  ? -25.948 33.562 5.791   1.00 32.30 ? 75  VAL B CG1 1 
ATOM   4700 C CG2 . VAL B 1 75  ? -25.896 35.909 6.607   1.00 31.59 ? 75  VAL B CG2 1 
ATOM   4701 N N   . PHE B 1 76  ? -23.141 36.503 7.894   1.00 26.75 ? 76  PHE B N   1 
ATOM   4702 C CA  . PHE B 1 76  ? -22.293 37.668 8.083   1.00 24.84 ? 76  PHE B CA  1 
ATOM   4703 C C   . PHE B 1 76  ? -20.892 37.250 8.511   1.00 27.90 ? 76  PHE B C   1 
ATOM   4704 O O   . PHE B 1 76  ? -19.896 37.793 8.024   1.00 24.00 ? 76  PHE B O   1 
ATOM   4705 C CB  . PHE B 1 76  ? -22.926 38.605 9.115   1.00 26.13 ? 76  PHE B CB  1 
ATOM   4706 C CG  . PHE B 1 76  ? -22.249 39.923 9.213   1.00 27.82 ? 76  PHE B CG  1 
ATOM   4707 C CD1 . PHE B 1 76  ? -22.641 40.972 8.398   1.00 29.74 ? 76  PHE B CD1 1 
ATOM   4708 C CD2 . PHE B 1 76  ? -21.201 40.113 10.105  1.00 29.49 ? 76  PHE B CD2 1 
ATOM   4709 C CE1 . PHE B 1 76  ? -22.006 42.189 8.475   1.00 32.30 ? 76  PHE B CE1 1 
ATOM   4710 C CE2 . PHE B 1 76  ? -20.562 41.326 10.187  1.00 32.19 ? 76  PHE B CE2 1 
ATOM   4711 C CZ  . PHE B 1 76  ? -20.963 42.365 9.368   1.00 31.72 ? 76  PHE B CZ  1 
ATOM   4712 N N   . LEU B 1 77  ? -20.802 36.277 9.420   1.00 24.71 ? 77  LEU B N   1 
ATOM   4713 C CA  . LEU B 1 77  ? -19.503 35.775 9.842   1.00 24.83 ? 77  LEU B CA  1 
ATOM   4714 C C   . LEU B 1 77  ? -18.731 35.206 8.661   1.00 32.29 ? 77  LEU B C   1 
ATOM   4715 O O   . LEU B 1 77  ? -17.517 35.402 8.561   1.00 24.99 ? 77  LEU B O   1 
ATOM   4716 C CB  . LEU B 1 77  ? -19.687 34.719 10.935  1.00 24.38 ? 77  LEU B CB  1 
ATOM   4717 C CG  . LEU B 1 77  ? -18.477 34.433 11.815  1.00 28.83 ? 77  LEU B CG  1 
ATOM   4718 C CD1 . LEU B 1 77  ? -17.817 35.737 12.302  1.00 31.33 ? 77  LEU B CD1 1 
ATOM   4719 C CD2 . LEU B 1 77  ? -18.906 33.566 12.992  1.00 26.72 ? 77  LEU B CD2 1 
ATOM   4720 N N   . GLU B 1 78  ? -19.429 34.520 7.744   1.00 27.80 ? 78  GLU B N   1 
ATOM   4721 C CA  . GLU B 1 78  ? -18.770 33.956 6.566   1.00 35.45 ? 78  GLU B CA  1 
ATOM   4722 C C   . GLU B 1 78  ? -18.122 35.041 5.715   1.00 32.33 ? 78  GLU B C   1 
ATOM   4723 O O   . GLU B 1 78  ? -17.029 34.841 5.168   1.00 35.85 ? 78  GLU B O   1 
ATOM   4724 C CB  . GLU B 1 78  ? -19.770 33.155 5.732   1.00 40.28 ? 78  GLU B CB  1 
ATOM   4725 C CG  . GLU B 1 78  ? -20.034 31.767 6.289   1.00 46.89 ? 78  GLU B CG  1 
ATOM   4726 C CD  . GLU B 1 78  ? -21.200 31.058 5.611   1.00 59.65 ? 78  GLU B CD  1 
ATOM   4727 O OE1 . GLU B 1 78  ? -21.871 31.658 4.737   1.00 61.07 ? 78  GLU B OE1 1 
ATOM   4728 O OE2 . GLU B 1 78  ? -21.442 29.888 5.965   1.00 66.10 ? 78  GLU B OE2 1 
ATOM   4729 N N   . ALA B 1 79  ? -18.773 36.199 5.595   1.00 25.11 ? 79  ALA B N   1 
ATOM   4730 C CA  . ALA B 1 79  ? -18.164 37.298 4.855   1.00 25.54 ? 79  ALA B CA  1 
ATOM   4731 C C   . ALA B 1 79  ? -16.949 37.857 5.589   1.00 28.89 ? 79  ALA B C   1 
ATOM   4732 O O   . ALA B 1 79  ? -15.982 38.288 4.952   1.00 33.76 ? 79  ALA B O   1 
ATOM   4733 C CB  . ALA B 1 79  ? -19.194 38.396 4.606   1.00 25.12 ? 79  ALA B CB  1 
ATOM   4734 N N   . ILE B 1 80  ? -16.969 37.840 6.919   1.00 21.99 ? 80  ILE B N   1 
ATOM   4735 C CA  . ILE B 1 80  ? -15.782 38.238 7.675   1.00 21.96 ? 80  ILE B CA  1 
ATOM   4736 C C   . ILE B 1 80  ? -14.632 37.266 7.437   1.00 31.39 ? 80  ILE B C   1 
ATOM   4737 O O   . ILE B 1 80  ? -13.473 37.671 7.269   1.00 26.37 ? 80  ILE B O   1 
ATOM   4738 C CB  . ILE B 1 80  ? -16.107 38.324 9.175   1.00 21.17 ? 80  ILE B CB  1 
ATOM   4739 C CG1 . ILE B 1 80  ? -16.987 39.535 9.474   1.00 35.64 ? 80  ILE B CG1 1 
ATOM   4740 C CG2 . ILE B 1 80  ? -14.807 38.354 9.973   1.00 25.18 ? 80  ILE B CG2 1 
ATOM   4741 C CD1 . ILE B 1 80  ? -16.244 40.837 9.418   1.00 37.00 ? 80  ILE B CD1 1 
ATOM   4742 N N   . ARG B 1 81  ? -14.918 35.966 7.466   1.00 28.22 ? 81  ARG B N   1 
ATOM   4743 C CA  . ARG B 1 81  ? -13.841 34.986 7.427   1.00 25.98 ? 81  ARG B CA  1 
ATOM   4744 C C   . ARG B 1 81  ? -13.140 34.981 6.072   1.00 28.86 ? 81  ARG B C   1 
ATOM   4745 O O   . ARG B 1 81  ? -11.906 34.901 6.010   1.00 30.50 ? 81  ARG B O   1 
ATOM   4746 C CB  . ARG B 1 81  ? -14.394 33.605 7.759   1.00 28.67 ? 81  ARG B CB  1 
ATOM   4747 C CG  . ARG B 1 81  ? -13.363 32.497 7.732   1.00 31.42 ? 81  ARG B CG  1 
ATOM   4748 C CD  . ARG B 1 81  ? -13.981 31.146 8.046   1.00 38.60 ? 81  ARG B CD  1 
ATOM   4749 N NE  . ARG B 1 81  ? -14.360 30.996 9.455   1.00 44.49 ? 81  ARG B NE  1 
ATOM   4750 C CZ  . ARG B 1 81  ? -13.498 30.766 10.444  1.00 47.37 ? 81  ARG B CZ  1 
ATOM   4751 N NH1 . ARG B 1 81  ? -12.200 30.671 10.193  1.00 41.17 ? 81  ARG B NH1 1 
ATOM   4752 N NH2 . ARG B 1 81  ? -13.934 30.632 11.689  1.00 47.87 ? 81  ARG B NH2 1 
ATOM   4753 N N   . LYS B 1 82  ? -13.908 35.088 4.985   1.00 29.53 ? 82  LYS B N   1 
ATOM   4754 C CA  . LYS B 1 82  ? -13.378 34.941 3.633   1.00 29.35 ? 82  LYS B CA  1 
ATOM   4755 C C   . LYS B 1 82  ? -12.246 35.925 3.347   1.00 33.16 ? 82  LYS B C   1 
ATOM   4756 O O   . LYS B 1 82  ? -12.210 37.044 3.871   1.00 27.36 ? 82  LYS B O   1 
ATOM   4757 C CB  . LYS B 1 82  ? -14.493 35.159 2.605   1.00 31.84 ? 82  LYS B CB  1 
ATOM   4758 C CG  . LYS B 1 82  ? -15.423 33.984 2.429   1.00 41.42 ? 82  LYS B CG  1 
ATOM   4759 C CD  . LYS B 1 82  ? -16.783 34.406 1.870   1.00 40.84 ? 82  LYS B CD  1 
ATOM   4760 C CE  . LYS B 1 82  ? -16.667 35.192 0.592   1.00 43.82 ? 82  LYS B CE  1 
ATOM   4761 N NZ  . LYS B 1 82  ? -17.916 35.059 -0.243  1.00 50.12 ? 82  LYS B NZ  1 
ATOM   4762 N N   . ASP B 1 83  ? -11.323 35.495 2.483   1.00 37.13 ? 83  ASP B N   1 
ATOM   4763 C CA  . ASP B 1 83  ? -10.366 36.418 1.892   1.00 30.98 ? 83  ASP B CA  1 
ATOM   4764 C C   . ASP B 1 83  ? -11.127 37.524 1.165   1.00 32.06 ? 83  ASP B C   1 
ATOM   4765 O O   . ASP B 1 83  ? -12.055 37.225 0.395   1.00 31.32 ? 83  ASP B O   1 
ATOM   4766 C CB  . ASP B 1 83  ? -9.447  35.695 0.909   1.00 32.75 ? 83  ASP B CB  1 
ATOM   4767 C CG  . ASP B 1 83  ? -8.290  36.574 0.440   1.00 44.23 ? 83  ASP B CG  1 
ATOM   4768 O OD1 . ASP B 1 83  ? -8.527  37.585 -0.257  1.00 37.38 ? 83  ASP B OD1 1 
ATOM   4769 O OD2 . ASP B 1 83  ? -7.136  36.259 0.804   1.00 44.64 ? 83  ASP B OD2 1 
ATOM   4770 N N   . PRO B 1 84  ? -10.772 38.798 1.368   1.00 30.51 ? 84  PRO B N   1 
ATOM   4771 C CA  . PRO B 1 84  ? -11.512 39.879 0.694   1.00 30.81 ? 84  PRO B CA  1 
ATOM   4772 C C   . PRO B 1 84  ? -11.563 39.744 -0.807  1.00 27.75 ? 84  PRO B C   1 
ATOM   4773 O O   . PRO B 1 84  ? -12.465 40.319 -1.424  1.00 30.48 ? 84  PRO B O   1 
ATOM   4774 C CB  . PRO B 1 84  ? -10.747 41.140 1.104   1.00 32.87 ? 84  PRO B CB  1 
ATOM   4775 C CG  . PRO B 1 84  ? -10.149 40.792 2.401   1.00 26.49 ? 84  PRO B CG  1 
ATOM   4776 C CD  . PRO B 1 84  ? -9.773  39.324 2.312   1.00 27.07 ? 84  PRO B CD  1 
ATOM   4777 N N   . ASP B 1 85  ? -10.616 39.029 -1.427  1.00 28.75 ? 85  ASP B N   1 
ATOM   4778 C CA  . ASP B 1 85  ? -10.692 38.817 -2.871  1.00 29.65 ? 85  ASP B CA  1 
ATOM   4779 C C   . ASP B 1 85  ? -11.919 38.016 -3.265  1.00 34.33 ? 85  ASP B C   1 
ATOM   4780 O O   . ASP B 1 85  ? -12.303 38.034 -4.439  1.00 33.63 ? 85  ASP B O   1 
ATOM   4781 C CB  . ASP B 1 85  ? -9.449  38.090 -3.389  1.00 36.95 ? 85  ASP B CB  1 
ATOM   4782 C CG  . ASP B 1 85  ? -8.228  38.973 -3.416  1.00 46.05 ? 85  ASP B CG  1 
ATOM   4783 O OD1 . ASP B 1 85  ? -8.389  40.208 -3.340  1.00 50.02 ? 85  ASP B OD1 1 
ATOM   4784 O OD2 . ASP B 1 85  ? -7.107  38.428 -3.517  1.00 42.76 ? 85  ASP B OD2 1 
ATOM   4785 N N   . ASP B 1 86  ? -12.523 37.299 -2.323  1.00 32.70 ? 86  ASP B N   1 
ATOM   4786 C CA  . ASP B 1 86  ? -13.699 36.485 -2.588  1.00 35.09 ? 86  ASP B CA  1 
ATOM   4787 C C   . ASP B 1 86  ? -15.006 37.157 -2.187  1.00 33.61 ? 86  ASP B C   1 
ATOM   4788 O O   . ASP B 1 86  ? -16.064 36.546 -2.352  1.00 32.17 ? 86  ASP B O   1 
ATOM   4789 C CB  . ASP B 1 86  ? -13.586 35.143 -1.859  1.00 43.78 ? 86  ASP B CB  1 
ATOM   4790 C CG  . ASP B 1 86  ? -12.390 34.326 -2.315  1.00 51.47 ? 86  ASP B CG  1 
ATOM   4791 O OD1 . ASP B 1 86  ? -11.958 34.468 -3.486  1.00 56.32 ? 86  ASP B OD1 1 
ATOM   4792 O OD2 . ASP B 1 86  ? -11.893 33.523 -1.501  1.00 55.10 ? 86  ASP B OD2 1 
ATOM   4793 N N   . LEU B 1 87  ? -14.969 38.383 -1.665  1.00 28.28 ? 87  LEU B N   1 
ATOM   4794 C CA  . LEU B 1 87  ? -16.194 39.047 -1.236  1.00 26.36 ? 87  LEU B CA  1 
ATOM   4795 C C   . LEU B 1 87  ? -17.044 39.484 -2.427  1.00 26.79 ? 87  LEU B C   1 
ATOM   4796 O O   . LEU B 1 87  ? -16.557 40.156 -3.343  1.00 28.65 ? 87  LEU B O   1 
ATOM   4797 C CB  . LEU B 1 87  ? -15.860 40.268 -0.390  1.00 25.71 ? 87  LEU B CB  1 
ATOM   4798 C CG  . LEU B 1 87  ? -15.366 39.981 1.025   1.00 25.09 ? 87  LEU B CG  1 
ATOM   4799 C CD1 . LEU B 1 87  ? -14.927 41.264 1.699   1.00 26.15 ? 87  LEU B CD1 1 
ATOM   4800 C CD2 . LEU B 1 87  ? -16.470 39.318 1.799   1.00 25.74 ? 87  LEU B CD2 1 
ATOM   4801 N N   . GLU B 1 88  ? -18.321 39.126 -2.404  1.00 26.55 ? 88  GLU B N   1 
ATOM   4802 C CA  . GLU B 1 88  ? -19.283 39.740 -3.319  1.00 26.87 ? 88  GLU B CA  1 
ATOM   4803 C C   . GLU B 1 88  ? -19.518 41.203 -2.950  1.00 27.51 ? 88  GLU B C   1 
ATOM   4804 O O   . GLU B 1 88  ? -19.363 41.600 -1.792  1.00 25.63 ? 88  GLU B O   1 
ATOM   4805 C CB  . GLU B 1 88  ? -20.620 39.005 -3.268  1.00 27.20 ? 88  GLU B CB  1 
ATOM   4806 C CG  . GLU B 1 88  ? -20.518 37.522 -3.400  1.00 36.42 ? 88  GLU B CG  1 
ATOM   4807 C CD  . GLU B 1 88  ? -21.791 36.830 -2.964  1.00 44.20 ? 88  GLU B CD  1 
ATOM   4808 O OE1 . GLU B 1 88  ? -21.937 35.628 -3.244  1.00 53.45 ? 88  GLU B OE1 1 
ATOM   4809 O OE2 . GLU B 1 88  ? -22.641 37.485 -2.326  1.00 52.28 ? 88  GLU B OE2 1 
ATOM   4810 N N   . LYS B 1 89  ? -19.903 42.010 -3.950  1.00 26.99 ? 89  LYS B N   1 
ATOM   4811 C CA  . LYS B 1 89  ? -20.308 43.389 -3.671  1.00 26.74 ? 89  LYS B CA  1 
ATOM   4812 C C   . LYS B 1 89  ? -21.358 43.451 -2.564  1.00 38.80 ? 89  LYS B C   1 
ATOM   4813 O O   . LYS B 1 89  ? -21.299 44.321 -1.691  1.00 30.29 ? 89  LYS B O   1 
ATOM   4814 C CB  . LYS B 1 89  ? -20.871 44.052 -4.933  1.00 27.62 ? 89  LYS B CB  1 
ATOM   4815 C CG  . LYS B 1 89  ? -19.898 44.228 -6.053  1.00 34.90 ? 89  LYS B CG  1 
ATOM   4816 C CD  . LYS B 1 89  ? -20.596 44.951 -7.212  1.00 33.21 ? 89  LYS B CD  1 
ATOM   4817 C CE  . LYS B 1 89  ? -19.778 44.846 -8.475  1.00 38.58 ? 89  LYS B CE  1 
ATOM   4818 N NZ  . LYS B 1 89  ? -18.353 45.114 -8.154  1.00 43.43 ? 89  LYS B NZ  1 
ATOM   4819 N N   . GLU B 1 90  ? -22.337 42.542 -2.599  1.00 25.87 ? 90  GLU B N   1 
ATOM   4820 C CA  . GLU B 1 90  ? -23.379 42.518 -1.571  1.00 35.29 ? 90  GLU B CA  1 
ATOM   4821 C C   . GLU B 1 90  ? -22.780 42.314 -0.187  1.00 34.77 ? 90  GLU B C   1 
ATOM   4822 O O   . GLU B 1 90  ? -23.263 42.881 0.805   1.00 29.01 ? 90  GLU B O   1 
ATOM   4823 C CB  . GLU B 1 90  ? -24.390 41.410 -1.886  1.00 35.06 ? 90  GLU B CB  1 
ATOM   4824 C CG  . GLU B 1 90  ? -25.382 41.087 -0.765  1.00 53.18 ? 90  GLU B CG  1 
ATOM   4825 C CD  . GLU B 1 90  ? -24.945 39.893 0.103   1.00 64.84 ? 90  GLU B CD  1 
ATOM   4826 O OE1 . GLU B 1 90  ? -25.282 39.868 1.312   1.00 54.42 ? 90  GLU B OE1 1 
ATOM   4827 O OE2 . GLU B 1 90  ? -24.265 38.979 -0.425  1.00 72.07 ? 90  GLU B OE2 1 
ATOM   4828 N N   . GLU B 1 91  ? -21.746 41.487 -0.100  1.00 24.29 ? 91  GLU B N   1 
ATOM   4829 C CA  . GLU B 1 91  ? -21.109 41.230 1.188   1.00 23.57 ? 91  GLU B CA  1 
ATOM   4830 C C   . GLU B 1 91  ? -20.304 42.437 1.662   1.00 23.32 ? 91  GLU B C   1 
ATOM   4831 O O   . GLU B 1 91  ? -20.311 42.760 2.855   1.00 24.13 ? 91  GLU B O   1 
ATOM   4832 C CB  . GLU B 1 91  ? -20.222 39.992 1.087   1.00 25.09 ? 91  GLU B CB  1 
ATOM   4833 C CG  . GLU B 1 91  ? -20.993 38.698 0.918   1.00 29.79 ? 91  GLU B CG  1 
ATOM   4834 C CD  . GLU B 1 91  ? -20.092 37.483 0.795   1.00 34.94 ? 91  GLU B CD  1 
ATOM   4835 O OE1 . GLU B 1 91  ? -19.284 37.426 -0.156  1.00 28.13 ? 91  GLU B OE1 1 
ATOM   4836 O OE2 . GLU B 1 91  ? -20.172 36.596 1.673   1.00 34.48 ? 91  GLU B OE2 1 
ATOM   4837 N N   . VAL B 1 92  ? -19.600 43.116 0.747   1.00 23.96 ? 92  VAL B N   1 
ATOM   4838 C CA  . VAL B 1 92  ? -18.883 44.330 1.132   1.00 27.33 ? 92  VAL B CA  1 
ATOM   4839 C C   . VAL B 1 92  ? -19.863 45.386 1.619   1.00 23.54 ? 92  VAL B C   1 
ATOM   4840 O O   . VAL B 1 92  ? -19.611 46.088 2.611   1.00 26.71 ? 92  VAL B O   1 
ATOM   4841 C CB  . VAL B 1 92  ? -18.030 44.844 -0.043  1.00 27.79 ? 92  VAL B CB  1 
ATOM   4842 C CG1 . VAL B 1 92  ? -17.331 46.134 0.335   1.00 24.81 ? 92  VAL B CG1 1 
ATOM   4843 C CG2 . VAL B 1 92  ? -17.027 43.801 -0.432  1.00 27.63 ? 92  VAL B CG2 1 
ATOM   4844 N N   . GLU B 1 93  ? -21.006 45.503 0.943   1.00 27.31 ? 93  GLU B N   1 
ATOM   4845 C CA  . GLU B 1 93  ? -22.017 46.471 1.349   1.00 26.89 ? 93  GLU B CA  1 
ATOM   4846 C C   . GLU B 1 93  ? -22.516 46.190 2.761   1.00 29.23 ? 93  GLU B C   1 
ATOM   4847 O O   . GLU B 1 93  ? -22.597 47.101 3.590   1.00 34.81 ? 93  GLU B O   1 
ATOM   4848 C CB  . GLU B 1 93  ? -23.182 46.446 0.361   1.00 37.35 ? 93  GLU B CB  1 
ATOM   4849 C CG  . GLU B 1 93  ? -23.031 47.393 -0.797  1.00 47.41 ? 93  GLU B CG  1 
ATOM   4850 C CD  . GLU B 1 93  ? -23.902 46.986 -1.965  1.00 51.85 ? 93  GLU B CD  1 
ATOM   4851 O OE1 . GLU B 1 93  ? -24.865 46.217 -1.751  1.00 53.15 ? 93  GLU B OE1 1 
ATOM   4852 O OE2 . GLU B 1 93  ? -23.627 47.443 -3.091  1.00 55.46 ? 93  GLU B OE2 1 
ATOM   4853 N N   . LYS B 1 94  ? -22.859 44.926 3.051   1.00 27.36 ? 94  LYS B N   1 
ATOM   4854 C CA  . LYS B 1 94  ? -23.331 44.566 4.388   1.00 25.14 ? 94  LYS B CA  1 
ATOM   4855 C C   . LYS B 1 94  ? -22.271 44.842 5.448   1.00 25.60 ? 94  LYS B C   1 
ATOM   4856 O O   . LYS B 1 94  ? -22.601 45.246 6.573   1.00 25.37 ? 94  LYS B O   1 
ATOM   4857 C CB  . LYS B 1 94  ? -23.740 43.092 4.439   1.00 30.24 ? 94  LYS B CB  1 
ATOM   4858 C CG  . LYS B 1 94  ? -24.835 42.698 3.463   1.00 41.14 ? 94  LYS B CG  1 
ATOM   4859 C CD  . LYS B 1 94  ? -26.102 43.522 3.644   1.00 45.61 ? 94  LYS B CD  1 
ATOM   4860 C CE  . LYS B 1 94  ? -27.104 43.236 2.519   1.00 50.04 ? 94  LYS B CE  1 
ATOM   4861 N NZ  . LYS B 1 94  ? -26.636 43.653 1.149   1.00 56.32 ? 94  LYS B NZ  1 
ATOM   4862 N N   . LEU B 1 95  ? -20.995 44.602 5.122   1.00 24.41 ? 95  LEU B N   1 
ATOM   4863 C CA  . LEU B 1 95  ? -19.924 44.856 6.080   1.00 23.38 ? 95  LEU B CA  1 
ATOM   4864 C C   . LEU B 1 95  ? -19.793 46.349 6.373   1.00 25.76 ? 95  LEU B C   1 
ATOM   4865 O O   . LEU B 1 95  ? -19.610 46.749 7.526   1.00 25.83 ? 95  LEU B O   1 
ATOM   4866 C CB  . LEU B 1 95  ? -18.612 44.280 5.547   1.00 23.62 ? 95  LEU B CB  1 
ATOM   4867 C CG  . LEU B 1 95  ? -17.369 44.419 6.419   1.00 35.49 ? 95  LEU B CG  1 
ATOM   4868 C CD1 . LEU B 1 95  ? -17.577 43.692 7.738   1.00 36.03 ? 95  LEU B CD1 1 
ATOM   4869 C CD2 . LEU B 1 95  ? -16.135 43.894 5.677   1.00 38.32 ? 95  LEU B CD2 1 
ATOM   4870 N N   . ILE B 1 96  ? -19.887 47.184 5.340   1.00 21.77 ? 96  ILE B N   1 
ATOM   4871 C CA  . ILE B 1 96  ? -19.840 48.630 5.529   1.00 25.83 ? 96  ILE B CA  1 
ATOM   4872 C C   . ILE B 1 96  ? -21.071 49.099 6.292   1.00 28.15 ? 96  ILE B C   1 
ATOM   4873 O O   . ILE B 1 96  ? -20.979 49.940 7.196   1.00 23.50 ? 96  ILE B O   1 
ATOM   4874 C CB  . ILE B 1 96  ? -19.716 49.327 4.161   1.00 28.26 ? 96  ILE B CB  1 
ATOM   4875 C CG1 . ILE B 1 96  ? -18.373 48.995 3.518   1.00 28.69 ? 96  ILE B CG1 1 
ATOM   4876 C CG2 . ILE B 1 96  ? -19.897 50.836 4.298   1.00 24.84 ? 96  ILE B CG2 1 
ATOM   4877 C CD1 . ILE B 1 96  ? -18.095 49.794 2.254   1.00 30.89 ? 96  ILE B CD1 1 
ATOM   4878 N N   . GLU B 1 97  ? -22.237 48.531 5.959   1.00 23.80 ? 97  GLU B N   1 
ATOM   4879 C CA  . GLU B 1 97  ? -23.488 48.849 6.638   1.00 23.75 ? 97  GLU B CA  1 
ATOM   4880 C C   . GLU B 1 97  ? -23.415 48.528 8.124   1.00 22.64 ? 97  GLU B C   1 
ATOM   4881 O O   . GLU B 1 97  ? -23.867 49.310 8.969   1.00 21.34 ? 97  GLU B O   1 
ATOM   4882 C CB  . GLU B 1 97  ? -24.613 48.056 5.980   1.00 36.04 ? 97  GLU B CB  1 
ATOM   4883 C CG  . GLU B 1 97  ? -26.002 48.553 6.205   1.00 42.65 ? 97  GLU B CG  1 
ATOM   4884 C CD  . GLU B 1 97  ? -26.901 48.105 5.077   1.00 61.94 ? 97  GLU B CD  1 
ATOM   4885 O OE1 . GLU B 1 97  ? -27.082 46.876 4.929   1.00 63.81 ? 97  GLU B OE1 1 
ATOM   4886 O OE2 . GLU B 1 97  ? -27.393 48.971 4.318   1.00 71.26 ? 97  GLU B OE2 1 
ATOM   4887 N N   . PHE B 1 98  ? -22.883 47.352 8.453   1.00 20.61 ? 98  PHE B N   1 
ATOM   4888 C CA  . PHE B 1 98  ? -22.717 46.955 9.847   1.00 20.41 ? 98  PHE B CA  1 
ATOM   4889 C C   . PHE B 1 98  ? -21.741 47.878 10.565  1.00 20.41 ? 98  PHE B C   1 
ATOM   4890 O O   . PHE B 1 98  ? -21.945 48.225 11.737  1.00 21.70 ? 98  PHE B O   1 
ATOM   4891 C CB  . PHE B 1 98  ? -22.223 45.512 9.871   1.00 25.04 ? 98  PHE B CB  1 
ATOM   4892 C CG  . PHE B 1 98  ? -22.213 44.865 11.223  1.00 19.39 ? 98  PHE B CG  1 
ATOM   4893 C CD1 . PHE B 1 98  ? -23.337 44.198 11.699  1.00 27.82 ? 98  PHE B CD1 1 
ATOM   4894 C CD2 . PHE B 1 98  ? -21.059 44.861 11.984  1.00 18.25 ? 98  PHE B CD2 1 
ATOM   4895 C CE1 . PHE B 1 98  ? -23.307 43.560 12.936  1.00 23.54 ? 98  PHE B CE1 1 
ATOM   4896 C CE2 . PHE B 1 98  ? -21.025 44.232 13.238  1.00 20.66 ? 98  PHE B CE2 1 
ATOM   4897 C CZ  . PHE B 1 98  ? -22.133 43.589 13.702  1.00 21.74 ? 98  PHE B CZ  1 
ATOM   4898 N N   . THR B 1 99  ? -20.657 48.266 9.881   1.00 21.47 ? 99  THR B N   1 
ATOM   4899 C CA  . THR B 1 99  ? -19.713 49.203 10.470  1.00 24.48 ? 99  THR B CA  1 
ATOM   4900 C C   . THR B 1 99  ? -20.379 50.545 10.735  1.00 22.96 ? 99  THR B C   1 
ATOM   4901 O O   . THR B 1 99  ? -20.196 51.132 11.808  1.00 24.29 ? 99  THR B O   1 
ATOM   4902 C CB  . THR B 1 99  ? -18.489 49.380 9.564   1.00 23.32 ? 99  THR B CB  1 
ATOM   4903 O OG1 . THR B 1 99  ? -17.914 48.098 9.249   1.00 23.85 ? 99  THR B OG1 1 
ATOM   4904 C CG2 . THR B 1 99  ? -17.446 50.238 10.262  1.00 21.69 ? 99  THR B CG2 1 
ATOM   4905 N N   . LYS B 1 100 ? -21.171 51.036 9.776   1.00 23.73 ? 100 LYS B N   1 
ATOM   4906 C CA  . LYS B 1 100 ? -21.801 52.345 9.922   1.00 21.76 ? 100 LYS B CA  1 
ATOM   4907 C C   . LYS B 1 100 ? -22.785 52.350 11.075  1.00 24.06 ? 100 LYS B C   1 
ATOM   4908 O O   . LYS B 1 100 ? -22.906 53.347 11.794  1.00 23.09 ? 100 LYS B O   1 
ATOM   4909 C CB  . LYS B 1 100 ? -22.521 52.730 8.629   1.00 24.88 ? 100 LYS B CB  1 
ATOM   4910 C CG  . LYS B 1 100 ? -21.634 53.001 7.427   1.00 39.52 ? 100 LYS B CG  1 
ATOM   4911 C CD  . LYS B 1 100 ? -22.331 53.977 6.479   1.00 47.04 ? 100 LYS B CD  1 
ATOM   4912 C CE  . LYS B 1 100 ? -21.347 54.771 5.626   1.00 51.36 ? 100 LYS B CE  1 
ATOM   4913 N NZ  . LYS B 1 100 ? -20.139 53.956 5.313   1.00 61.91 ? 100 LYS B NZ  1 
ATOM   4914 N N   . LEU B 1 101 ? -23.501 51.237 11.252  1.00 20.04 ? 101 LEU B N   1 
ATOM   4915 C CA  . LEU B 1 101 ? -24.487 51.104 12.313  1.00 23.42 ? 101 LEU B CA  1 
ATOM   4916 C C   . LEU B 1 101 ? -23.857 51.192 13.700  1.00 22.27 ? 101 LEU B C   1 
ATOM   4917 O O   . LEU B 1 101 ? -24.498 51.690 14.632  1.00 22.99 ? 101 LEU B O   1 
ATOM   4918 C CB  . LEU B 1 101 ? -25.223 49.778 12.147  1.00 28.33 ? 101 LEU B CB  1 
ATOM   4919 C CG  . LEU B 1 101 ? -26.243 49.377 13.202  1.00 28.94 ? 101 LEU B CG  1 
ATOM   4920 C CD1 . LEU B 1 101 ? -27.453 50.305 13.154  1.00 34.52 ? 101 LEU B CD1 1 
ATOM   4921 C CD2 . LEU B 1 101 ? -26.666 47.935 12.972  1.00 29.75 ? 101 LEU B CD2 1 
ATOM   4922 N N   . ASN B 1 102 ? -22.621 50.715 13.856  1.00 20.56 ? 102 ASN B N   1 
ATOM   4923 C CA  . ASN B 1 102 ? -21.935 50.679 15.148  1.00 19.00 ? 102 ASN B CA  1 
ATOM   4924 C C   . ASN B 1 102 ? -20.869 51.755 15.298  1.00 19.98 ? 102 ASN B C   1 
ATOM   4925 O O   . ASN B 1 102 ? -20.217 51.828 16.356  1.00 22.42 ? 102 ASN B O   1 
ATOM   4926 C CB  . ASN B 1 102 ? -21.287 49.306 15.362  1.00 24.17 ? 102 ASN B CB  1 
ATOM   4927 C CG  . ASN B 1 102 ? -22.297 48.175 15.410  1.00 25.96 ? 102 ASN B CG  1 
ATOM   4928 O OD1 . ASN B 1 102 ? -23.234 48.195 16.208  1.00 28.31 ? 102 ASN B OD1 1 
ATOM   4929 N ND2 . ASN B 1 102 ? -22.105 47.177 14.565  1.00 29.74 ? 102 ASN B ND2 1 
ATOM   4930 N N   . TYR B 1 103 ? -20.728 52.620 14.297  1.00 21.95 ? 103 TYR B N   1 
ATOM   4931 C CA  . TYR B 1 103 ? -19.554 53.474 14.136  1.00 27.63 ? 103 TYR B CA  1 
ATOM   4932 C C   . TYR B 1 103 ? -19.362 54.434 15.309  1.00 24.86 ? 103 TYR B C   1 
ATOM   4933 O O   . TYR B 1 103 ? -18.227 54.728 15.696  1.00 21.44 ? 103 TYR B O   1 
ATOM   4934 C CB  . TYR B 1 103 ? -19.697 54.242 12.811  1.00 31.90 ? 103 TYR B CB  1 
ATOM   4935 C CG  . TYR B 1 103 ? -18.592 55.213 12.477  1.00 34.43 ? 103 TYR B CG  1 
ATOM   4936 C CD1 . TYR B 1 103 ? -18.641 56.535 12.917  1.00 41.51 ? 103 TYR B CD1 1 
ATOM   4937 C CD2 . TYR B 1 103 ? -17.519 54.829 11.687  1.00 39.47 ? 103 TYR B CD2 1 
ATOM   4938 C CE1 . TYR B 1 103 ? -17.637 57.431 12.602  1.00 43.32 ? 103 TYR B CE1 1 
ATOM   4939 C CE2 . TYR B 1 103 ? -16.512 55.716 11.370  1.00 38.92 ? 103 TYR B CE2 1 
ATOM   4940 C CZ  . TYR B 1 103 ? -16.576 57.016 11.828  1.00 44.41 ? 103 TYR B CZ  1 
ATOM   4941 O OH  . TYR B 1 103 ? -15.571 57.902 11.509  1.00 58.62 ? 103 TYR B OH  1 
ATOM   4942 N N   . GLU B 1 104 ? -20.448 54.946 15.875  1.00 23.96 ? 104 GLU B N   1 
ATOM   4943 C CA  . GLU B 1 104 ? -20.327 55.915 16.957  1.00 33.17 ? 104 GLU B CA  1 
ATOM   4944 C C   . GLU B 1 104 ? -20.116 55.276 18.324  1.00 28.55 ? 104 GLU B C   1 
ATOM   4945 O O   . GLU B 1 104 ? -19.874 55.999 19.298  1.00 31.27 ? 104 GLU B O   1 
ATOM   4946 C CB  . GLU B 1 104 ? -21.573 56.795 17.007  1.00 33.92 ? 104 GLU B CB  1 
ATOM   4947 C CG  . GLU B 1 104 ? -21.921 57.423 15.683  1.00 37.82 ? 104 GLU B CG  1 
ATOM   4948 C CD  . GLU B 1 104 ? -21.135 58.681 15.428  1.00 47.37 ? 104 GLU B CD  1 
ATOM   4949 O OE1 . GLU B 1 104 ? -20.589 59.233 16.404  1.00 44.87 ? 104 GLU B OE1 1 
ATOM   4950 O OE2 . GLU B 1 104 ? -21.071 59.124 14.256  1.00 56.61 ? 104 GLU B OE2 1 
ATOM   4951 N N   . LYS B 1 105 ? -20.205 53.977 18.429  1.00 21.28 ? 105 LYS B N   1 
ATOM   4952 C CA  . LYS B 1 105 ? -20.086 53.379 19.753  1.00 20.80 ? 105 LYS B CA  1 
ATOM   4953 C C   . LYS B 1 105 ? -18.615 53.318 20.174  1.00 25.64 ? 105 LYS B C   1 
ATOM   4954 O O   . LYS B 1 105 ? -17.733 53.047 19.345  1.00 22.24 ? 105 LYS B O   1 
ATOM   4955 C CB  . LYS B 1 105 ? -20.705 51.981 19.759  1.00 23.94 ? 105 LYS B CB  1 
ATOM   4956 C CG  . LYS B 1 105 ? -22.145 51.950 19.241  1.00 24.25 ? 105 LYS B CG  1 
ATOM   4957 C CD  . LYS B 1 105 ? -22.634 50.540 18.959  1.00 20.94 ? 105 LYS B CD  1 
ATOM   4958 C CE  . LYS B 1 105 ? -24.123 50.546 18.520  1.00 23.39 ? 105 LYS B CE  1 
ATOM   4959 N NZ  . LYS B 1 105 ? -24.626 49.155 18.311  1.00 23.31 ? 105 LYS B NZ  1 
ATOM   4960 N N   . PRO B 1 106 ? -18.320 53.563 21.454  1.00 21.79 ? 106 PRO B N   1 
ATOM   4961 C CA  . PRO B 1 106 ? -16.914 53.564 21.890  1.00 19.62 ? 106 PRO B CA  1 
ATOM   4962 C C   . PRO B 1 106 ? -16.154 52.279 21.579  1.00 19.48 ? 106 PRO B C   1 
ATOM   4963 O O   . PRO B 1 106 ? -14.929 52.335 21.419  1.00 25.85 ? 106 PRO B O   1 
ATOM   4964 C CB  . PRO B 1 106 ? -17.023 53.806 23.406  1.00 21.55 ? 106 PRO B CB  1 
ATOM   4965 C CG  . PRO B 1 106 ? -18.295 54.584 23.564  1.00 23.32 ? 106 PRO B CG  1 
ATOM   4966 C CD  . PRO B 1 106 ? -19.241 54.031 22.510  1.00 18.53 ? 106 PRO B CD  1 
ATOM   4967 N N   . ILE B 1 107 ? -16.817 51.122 21.509  1.00 16.96 ? 107 ILE B N   1 
ATOM   4968 C CA  . ILE B 1 107 ? -16.089 49.897 21.189  1.00 16.43 ? 107 ILE B CA  1 
ATOM   4969 C C   . ILE B 1 107 ? -15.589 49.874 19.746  1.00 19.95 ? 107 ILE B C   1 
ATOM   4970 O O   . ILE B 1 107 ? -14.773 49.010 19.400  1.00 19.19 ? 107 ILE B O   1 
ATOM   4971 C CB  . ILE B 1 107 ? -16.908 48.613 21.466  1.00 18.09 ? 107 ILE B CB  1 
ATOM   4972 C CG1 . ILE B 1 107 ? -18.195 48.550 20.647  1.00 20.88 ? 107 ILE B CG1 1 
ATOM   4973 C CG2 . ILE B 1 107 ? -17.185 48.464 22.978  1.00 16.10 ? 107 ILE B CG2 1 
ATOM   4974 C CD1 . ILE B 1 107 ? -18.795 47.135 20.588  1.00 18.18 ? 107 ILE B CD1 1 
ATOM   4975 N N   . TYR B 1 108 ? -16.056 50.794 18.900  1.00 19.94 ? 108 TYR B N   1 
ATOM   4976 C CA  . TYR B 1 108 ? -15.558 50.946 17.534  1.00 20.54 ? 108 TYR B CA  1 
ATOM   4977 C C   . TYR B 1 108 ? -14.558 52.088 17.398  1.00 22.66 ? 108 TYR B C   1 
ATOM   4978 O O   . TYR B 1 108 ? -14.226 52.476 16.274  1.00 25.34 ? 108 TYR B O   1 
ATOM   4979 C CB  . TYR B 1 108 ? -16.731 51.151 16.560  1.00 20.29 ? 108 TYR B CB  1 
ATOM   4980 C CG  . TYR B 1 108 ? -17.263 49.840 16.007  1.00 20.32 ? 108 TYR B CG  1 
ATOM   4981 C CD1 . TYR B 1 108 ? -18.020 48.992 16.795  1.00 17.04 ? 108 TYR B CD1 1 
ATOM   4982 C CD2 . TYR B 1 108 ? -16.971 49.434 14.711  1.00 19.46 ? 108 TYR B CD2 1 
ATOM   4983 C CE1 . TYR B 1 108 ? -18.483 47.770 16.308  1.00 19.61 ? 108 TYR B CE1 1 
ATOM   4984 C CE2 . TYR B 1 108 ? -17.430 48.225 14.214  1.00 16.94 ? 108 TYR B CE2 1 
ATOM   4985 C CZ  . TYR B 1 108 ? -18.182 47.395 15.015  1.00 19.20 ? 108 TYR B CZ  1 
ATOM   4986 O OH  . TYR B 1 108 ? -18.625 46.193 14.510  1.00 17.99 ? 108 TYR B OH  1 
ATOM   4987 N N   . ARG B 1 109 ? -14.052 52.634 18.505  1.00 19.66 ? 109 ARG B N   1 
ATOM   4988 C CA  . ARG B 1 109 ? -13.146 53.782 18.418  1.00 26.21 ? 109 ARG B CA  1 
ATOM   4989 C C   . ARG B 1 109 ? -11.748 53.299 18.031  1.00 29.17 ? 109 ARG B C   1 
ATOM   4990 O O   . ARG B 1 109 ? -10.850 53.136 18.857  1.00 26.80 ? 109 ARG B O   1 
ATOM   4991 C CB  . ARG B 1 109 ? -13.130 54.571 19.723  1.00 28.30 ? 109 ARG B CB  1 
ATOM   4992 C CG  . ARG B 1 109 ? -13.113 56.076 19.484  1.00 36.50 ? 109 ARG B CG  1 
ATOM   4993 C CD  . ARG B 1 109 ? -12.719 56.865 20.729  1.00 49.07 ? 109 ARG B CD  1 
ATOM   4994 N NE  . ARG B 1 109 ? -13.561 56.584 21.896  1.00 56.17 ? 109 ARG B NE  1 
ATOM   4995 C CZ  . ARG B 1 109 ? -14.777 57.091 22.088  1.00 55.50 ? 109 ARG B CZ  1 
ATOM   4996 N NH1 . ARG B 1 109 ? -15.318 57.898 21.184  1.00 62.78 ? 109 ARG B NH1 1 
ATOM   4997 N NH2 . ARG B 1 109 ? -15.455 56.796 23.187  1.00 43.66 ? 109 ARG B NH2 1 
ATOM   4998 N N   . PHE B 1 110 ? -11.579 53.041 16.736  1.00 27.63 ? 110 PHE B N   1 
ATOM   4999 C CA  . PHE B 1 110 ? -10.284 52.761 16.131  1.00 24.81 ? 110 PHE B CA  1 
ATOM   5000 C C   . PHE B 1 110 ? -10.066 53.799 15.045  1.00 27.90 ? 110 PHE B C   1 
ATOM   5001 O O   . PHE B 1 110 ? -10.969 54.040 14.235  1.00 29.12 ? 110 PHE B O   1 
ATOM   5002 C CB  . PHE B 1 110 ? -10.225 51.366 15.498  1.00 23.17 ? 110 PHE B CB  1 
ATOM   5003 C CG  . PHE B 1 110 ? -10.361 50.232 16.470  1.00 20.33 ? 110 PHE B CG  1 
ATOM   5004 C CD1 . PHE B 1 110 ? -9.242  49.664 17.047  1.00 25.83 ? 110 PHE B CD1 1 
ATOM   5005 C CD2 . PHE B 1 110 ? -11.605 49.688 16.759  1.00 25.58 ? 110 PHE B CD2 1 
ATOM   5006 C CE1 . PHE B 1 110 ? -9.356  48.600 17.930  1.00 26.84 ? 110 PHE B CE1 1 
ATOM   5007 C CE2 . PHE B 1 110 ? -11.724 48.626 17.645  1.00 29.15 ? 110 PHE B CE2 1 
ATOM   5008 C CZ  . PHE B 1 110 ? -10.594 48.083 18.227  1.00 29.18 ? 110 PHE B CZ  1 
ATOM   5009 N N   . GLU B 1 111 ? -8.882  54.416 15.032  1.00 28.10 ? 111 GLU B N   1 
ATOM   5010 C CA  . GLU B 1 111 ? -8.584  55.395 13.991  1.00 30.35 ? 111 GLU B CA  1 
ATOM   5011 C C   . GLU B 1 111 ? -8.715  54.773 12.607  1.00 31.34 ? 111 GLU B C   1 
ATOM   5012 O O   . GLU B 1 111 ? -9.232  55.406 11.679  1.00 30.09 ? 111 GLU B O   1 
ATOM   5013 C CB  . GLU B 1 111 ? -7.186  55.975 14.212  1.00 40.55 ? 111 GLU B CB  1 
ATOM   5014 C CG  . GLU B 1 111 ? -6.597  56.743 13.036  1.00 52.37 ? 111 GLU B CG  1 
ATOM   5015 C CD  . GLU B 1 111 ? -7.383  57.992 12.693  1.00 57.68 ? 111 GLU B CD  1 
ATOM   5016 O OE1 . GLU B 1 111 ? -8.208  58.435 13.525  1.00 62.67 ? 111 GLU B OE1 1 
ATOM   5017 O OE2 . GLU B 1 111 ? -7.173  58.529 11.585  1.00 65.27 ? 111 GLU B OE2 1 
ATOM   5018 N N   . ARG B 1 112 ? -8.291  53.515 12.463  1.00 30.07 ? 112 ARG B N   1 
ATOM   5019 C CA  . ARG B 1 112 ? -8.307  52.876 11.152  1.00 29.43 ? 112 ARG B CA  1 
ATOM   5020 C C   . ARG B 1 112 ? -9.724  52.731 10.618  1.00 26.97 ? 112 ARG B C   1 
ATOM   5021 O O   . ARG B 1 112 ? -9.939  52.829 9.402   1.00 27.06 ? 112 ARG B O   1 
ATOM   5022 C CB  . ARG B 1 112 ? -7.617  51.517 11.218  1.00 25.99 ? 112 ARG B CB  1 
ATOM   5023 C CG  . ARG B 1 112 ? -7.585  50.766 9.886   1.00 25.34 ? 112 ARG B CG  1 
ATOM   5024 C CD  . ARG B 1 112 ? -6.919  51.553 8.771   1.00 26.25 ? 112 ARG B CD  1 
ATOM   5025 N NE  . ARG B 1 112 ? -6.481  50.634 7.725   1.00 26.49 ? 112 ARG B NE  1 
ATOM   5026 C CZ  . ARG B 1 112 ? -6.157  50.983 6.486   1.00 39.00 ? 112 ARG B CZ  1 
ATOM   5027 N NH1 . ARG B 1 112 ? -6.230  52.254 6.106   1.00 44.80 ? 112 ARG B NH1 1 
ATOM   5028 N NH2 . ARG B 1 112 ? -5.759  50.054 5.624   1.00 38.73 ? 112 ARG B NH2 1 
ATOM   5029 N N   . ILE B 1 113 ? -10.703 52.528 11.506  1.00 25.52 ? 113 ILE B N   1 
ATOM   5030 C CA  . ILE B 1 113 ? -12.098 52.485 11.073  1.00 28.26 ? 113 ILE B CA  1 
ATOM   5031 C C   . ILE B 1 113 ? -12.532 53.842 10.531  1.00 31.62 ? 113 ILE B C   1 
ATOM   5032 O O   . ILE B 1 113 ? -13.245 53.922 9.523   1.00 32.80 ? 113 ILE B O   1 
ATOM   5033 C CB  . ILE B 1 113 ? -13.006 52.019 12.225  1.00 27.21 ? 113 ILE B CB  1 
ATOM   5034 C CG1 . ILE B 1 113 ? -12.779 50.541 12.520  1.00 29.50 ? 113 ILE B CG1 1 
ATOM   5035 C CG2 . ILE B 1 113 ? -14.479 52.238 11.873  1.00 25.77 ? 113 ILE B CG2 1 
ATOM   5036 C CD1 . ILE B 1 113 ? -13.624 50.057 13.658  1.00 37.61 ? 113 ILE B CD1 1 
ATOM   5037 N N   . ARG B 1 114 ? -12.115 54.930 11.188  1.00 30.47 ? 114 ARG B N   1 
ATOM   5038 C CA  . ARG B 1 114 ? -12.447 56.261 10.683  1.00 31.43 ? 114 ARG B CA  1 
ATOM   5039 C C   . ARG B 1 114 ? -11.875 56.473 9.289   1.00 27.34 ? 114 ARG B C   1 
ATOM   5040 O O   . ARG B 1 114 ? -12.545 57.032 8.412   1.00 34.31 ? 114 ARG B O   1 
ATOM   5041 C CB  . ARG B 1 114 ? -11.942 57.341 11.641  1.00 31.38 ? 114 ARG B CB  1 
ATOM   5042 C CG  . ARG B 1 114 ? -12.775 57.454 12.910  1.00 48.85 ? 114 ARG B CG  1 
ATOM   5043 C CD  . ARG B 1 114 ? -12.416 58.682 13.763  1.00 56.86 ? 114 ARG B CD  1 
ATOM   5044 N NE  . ARG B 1 114 ? -11.454 58.385 14.830  1.00 62.07 ? 114 ARG B NE  1 
ATOM   5045 C CZ  . ARG B 1 114 ? -11.653 57.527 15.834  1.00 57.06 ? 114 ARG B CZ  1 
ATOM   5046 N NH1 . ARG B 1 114 ? -12.792 56.845 15.943  1.00 50.52 ? 114 ARG B NH1 1 
ATOM   5047 N NH2 . ARG B 1 114 ? -10.700 57.350 16.737  1.00 53.66 ? 114 ARG B NH2 1 
ATOM   5048 N N   . GLU B 1 115 ? -10.635 56.029 9.066   1.00 28.06 ? 115 GLU B N   1 
ATOM   5049 C CA  . GLU B 1 115 ? -10.024 56.168 7.748   1.00 30.23 ? 115 GLU B CA  1 
ATOM   5050 C C   . GLU B 1 115 ? -10.762 55.344 6.702   1.00 32.77 ? 115 GLU B C   1 
ATOM   5051 O O   . GLU B 1 115 ? -10.967 55.799 5.569   1.00 31.46 ? 115 GLU B O   1 
ATOM   5052 C CB  . GLU B 1 115 ? -8.561  55.737 7.791   1.00 37.41 ? 115 GLU B CB  1 
ATOM   5053 C CG  . GLU B 1 115 ? -7.666  56.578 8.659   1.00 45.74 ? 115 GLU B CG  1 
ATOM   5054 C CD  . GLU B 1 115 ? -6.308  55.932 8.848   1.00 52.02 ? 115 GLU B CD  1 
ATOM   5055 O OE1 . GLU B 1 115 ? -5.965  55.026 8.052   1.00 46.03 ? 115 GLU B OE1 1 
ATOM   5056 O OE2 . GLU B 1 115 ? -5.590  56.333 9.788   1.00 56.29 ? 115 GLU B OE2 1 
ATOM   5057 N N   . LEU B 1 116 ? -11.140 54.115 7.058   1.00 35.52 ? 116 LEU B N   1 
ATOM   5058 C CA  . LEU B 1 116 ? -11.749 53.210 6.087   1.00 35.98 ? 116 LEU B CA  1 
ATOM   5059 C C   . LEU B 1 116 ? -13.104 53.726 5.626   1.00 35.83 ? 116 LEU B C   1 
ATOM   5060 O O   . LEU B 1 116 ? -13.446 53.626 4.439   1.00 33.44 ? 116 LEU B O   1 
ATOM   5061 C CB  . LEU B 1 116 ? -11.884 51.812 6.691   1.00 29.20 ? 116 LEU B CB  1 
ATOM   5062 C CG  . LEU B 1 116 ? -10.558 51.085 6.885   1.00 30.86 ? 116 LEU B CG  1 
ATOM   5063 C CD1 . LEU B 1 116 ? -10.738 49.783 7.672   1.00 36.56 ? 116 LEU B CD1 1 
ATOM   5064 C CD2 . LEU B 1 116 ? -9.910  50.851 5.539   1.00 35.76 ? 116 LEU B CD2 1 
ATOM   5065 N N   . MET B 1 117 ? -13.882 54.288 6.550   1.00 31.02 ? 117 MET B N   1 
ATOM   5066 C CA  . MET B 1 117 ? -15.220 54.766 6.233   1.00 36.24 ? 117 MET B CA  1 
ATOM   5067 C C   . MET B 1 117 ? -15.219 56.075 5.461   1.00 46.67 ? 117 MET B C   1 
ATOM   5068 O O   . MET B 1 117 ? -16.292 56.516 5.035   1.00 44.94 ? 117 MET B O   1 
ATOM   5069 C CB  . MET B 1 117 ? -16.037 54.930 7.516   1.00 32.83 ? 117 MET B CB  1 
ATOM   5070 C CG  . MET B 1 117 ? -16.305 53.619 8.260   1.00 32.36 ? 117 MET B CG  1 
ATOM   5071 S SD  . MET B 1 117 ? -17.317 52.492 7.273   1.00 36.50 ? 117 MET B SD  1 
ATOM   5072 C CE  . MET B 1 117 ? -16.080 51.345 6.678   1.00 39.70 ? 117 MET B CE  1 
ATOM   5073 N N   . ASN B 1 118 ? -14.051 56.658 5.299   1.00 44.61 ? 118 ASN B N   1 
ATOM   5074 C CA  . ASN B 1 118 ? -13.918 57.864 4.526   1.00 48.72 ? 118 ASN B CA  1 
ATOM   5075 C C   . ASN B 1 118 ? -13.512 57.591 3.080   1.00 46.03 ? 118 ASN B C   1 
ATOM   5076 O O   . ASN B 1 118 ? -13.450 58.477 2.296   1.00 51.15 ? 118 ASN B O   1 
ATOM   5077 C CB  . ASN B 1 118 ? -12.918 58.768 5.185   1.00 52.95 ? 118 ASN B CB  1 
ATOM   5078 C CG  . ASN B 1 118 ? -13.566 59.731 6.131   1.00 56.55 ? 118 ASN B CG  1 
ATOM   5079 O OD1 . ASN B 1 118 ? -14.703 60.046 5.978   1.00 65.88 ? 118 ASN B OD1 1 
ATOM   5080 N ND2 . ASN B 1 118 ? -12.845 60.168 7.118   1.00 57.11 ? 118 ASN B ND2 1 
ATOM   5081 N N   . LYS B 1 119 ? -13.265 56.344 2.732   1.00 48.43 ? 119 LYS B N   1 
ATOM   5082 C CA  . LYS B 1 119 ? -12.848 56.003 1.379   1.00 52.78 ? 119 LYS B CA  1 
ATOM   5083 C C   . LYS B 1 119 ? -13.863 55.591 0.384   1.00 51.62 ? 119 LYS B C   1 
ATOM   5084 O O   . LYS B 1 119 ? -14.785 54.868 0.646   1.00 49.03 ? 119 LYS B O   1 
ATOM   5085 C CB  . LYS B 1 119 ? -11.780 54.941 1.410   1.00 51.19 ? 119 LYS B CB  1 
ATOM   5086 C CG  . LYS B 1 119 ? -10.633 55.417 2.196   1.00 53.19 ? 119 LYS B CG  1 
ATOM   5087 C CD  . LYS B 1 119 ? -9.587  54.365 2.324   1.00 52.49 ? 119 LYS B CD  1 
ATOM   5088 C CE  . LYS B 1 119 ? -8.343  55.074 2.790   1.00 56.56 ? 119 LYS B CE  1 
ATOM   5089 N NZ  . LYS B 1 119 ? -7.256  54.142 2.729   1.00 52.58 ? 119 LYS B NZ  1 
ATOM   5090 N N   . GLU B 1 120 ? -13.639 56.065 -0.820  1.00 59.46 ? 120 GLU B N   1 
ATOM   5091 C CA  . GLU B 1 120 ? -14.516 55.781 -1.902  1.00 63.08 ? 120 GLU B CA  1 
ATOM   5092 C C   . GLU B 1 120 ? -14.500 54.300 -2.175  1.00 52.96 ? 120 GLU B C   1 
ATOM   5093 O O   . GLU B 1 120 ? -15.519 53.692 -2.264  1.00 56.01 ? 120 GLU B O   1 
ATOM   5094 C CB  . GLU B 1 120 ? -14.048 56.546 -3.148  1.00 70.72 ? 120 GLU B CB  1 
ATOM   5095 C CG  . GLU B 1 120 ? -14.714 57.902 -3.388  1.00 75.98 ? 120 GLU B CG  1 
ATOM   5096 C CD  . GLU B 1 120 ? -14.710 58.283 -4.864  1.00 87.98 ? 120 GLU B CD  1 
ATOM   5097 O OE1 . GLU B 1 120 ? -14.091 57.559 -5.653  1.00 89.77 ? 120 GLU B OE1 1 
ATOM   5098 O OE2 . GLU B 1 120 ? -15.336 59.289 -5.249  1.00 92.63 ? 120 GLU B OE2 1 
ATOM   5099 N N   . LYS B 1 121 ? -13.320 53.740 -2.321  1.00 46.28 ? 121 LYS B N   1 
ATOM   5100 C CA  . LYS B 1 121 ? -13.190 52.340 -2.627  1.00 47.05 ? 121 LYS B CA  1 
ATOM   5101 C C   . LYS B 1 121 ? -12.154 51.714 -1.735  1.00 47.04 ? 121 LYS B C   1 
ATOM   5102 O O   . LYS B 1 121 ? -11.197 52.339 -1.404  1.00 49.84 ? 121 LYS B O   1 
ATOM   5103 C CB  . LYS B 1 121 ? -12.742 52.088 -4.068  1.00 40.97 ? 121 LYS B CB  1 
ATOM   5104 C CG  . LYS B 1 121 ? -13.543 52.749 -5.165  1.00 58.10 ? 121 LYS B CG  1 
ATOM   5105 C CD  . LYS B 1 121 ? -14.936 52.164 -5.356  1.00 64.26 ? 121 LYS B CD  1 
ATOM   5106 C CE  . LYS B 1 121 ? -15.762 52.945 -6.374  1.00 64.56 ? 121 LYS B CE  1 
ATOM   5107 N NZ  . LYS B 1 121 ? -16.168 52.111 -7.534  1.00 63.38 ? 121 LYS B NZ  1 
ATOM   5108 N N   . LEU B 1 122 ? -12.348 50.446 -1.418  1.00 41.10 ? 122 LEU B N   1 
ATOM   5109 C CA  . LEU B 1 122 ? -11.459 49.724 -0.543  1.00 37.45 ? 122 LEU B CA  1 
ATOM   5110 C C   . LEU B 1 122 ? -10.742 48.614 -1.225  1.00 36.10 ? 122 LEU B C   1 
ATOM   5111 O O   . LEU B 1 122 ? -11.337 47.844 -1.859  1.00 41.58 ? 122 LEU B O   1 
ATOM   5112 C CB  . LEU B 1 122 ? -12.248 49.129 0.623   1.00 31.74 ? 122 LEU B CB  1 
ATOM   5113 C CG  . LEU B 1 122 ? -13.170 50.037 1.406   1.00 38.11 ? 122 LEU B CG  1 
ATOM   5114 C CD1 . LEU B 1 122 ? -13.941 49.271 2.430   1.00 41.32 ? 122 LEU B CD1 1 
ATOM   5115 C CD2 . LEU B 1 122 ? -12.438 51.125 2.109   1.00 42.70 ? 122 LEU B CD2 1 
ATOM   5116 N N   . ASN B 1 123 ? -9.450  48.534 -1.061  1.00 33.41 ? 123 ASN B N   1 
ATOM   5117 C CA  . ASN B 1 123 ? -8.652  47.478 -1.670  1.00 31.48 ? 123 ASN B CA  1 
ATOM   5118 C C   . ASN B 1 123 ? -8.621  46.266 -0.733  1.00 33.46 ? 123 ASN B C   1 
ATOM   5119 O O   . ASN B 1 123 ? -9.292  46.237 0.308   1.00 32.88 ? 123 ASN B O   1 
ATOM   5120 C CB  . ASN B 1 123 ? -7.254  47.995 -2.036  1.00 34.01 ? 123 ASN B CB  1 
ATOM   5121 C CG  . ASN B 1 123 ? -6.403  48.367 -0.816  1.00 36.84 ? 123 ASN B CG  1 
ATOM   5122 O OD1 . ASN B 1 123 ? -6.612  47.878 0.291   1.00 34.23 ? 123 ASN B OD1 1 
ATOM   5123 N ND2 . ASN B 1 123 ? -5.415  49.227 -1.036  1.00 38.80 ? 123 ASN B ND2 1 
ATOM   5124 N N   . ARG B 1 124 ? -7.829  45.247 -1.091  1.00 39.78 ? 124 ARG B N   1 
ATOM   5125 C CA  . ARG B 1 124 ? -7.855  43.997 -0.331  1.00 38.59 ? 124 ARG B CA  1 
ATOM   5126 C C   . ARG B 1 124 ? -7.394  44.212 1.102   1.00 31.89 ? 124 ARG B C   1 
ATOM   5127 O O   . ARG B 1 124 ? -8.014  43.711 2.050   1.00 29.66 ? 124 ARG B O   1 
ATOM   5128 C CB  . ARG B 1 124 ? -6.985  42.939 -1.014  1.00 36.06 ? 124 ARG B CB  1 
ATOM   5129 C CG  . ARG B 1 124 ? -6.827  41.678 -0.174  1.00 41.08 ? 124 ARG B CG  1 
ATOM   5130 C CD  . ARG B 1 124 ? -6.035  40.580 -0.871  1.00 37.96 ? 124 ARG B CD  1 
ATOM   5131 N NE  . ARG B 1 124 ? -5.979  39.360 -0.063  1.00 36.15 ? 124 ARG B NE  1 
ATOM   5132 C CZ  . ARG B 1 124 ? -5.183  39.197 0.988   1.00 35.77 ? 124 ARG B CZ  1 
ATOM   5133 N NH1 . ARG B 1 124 ? -4.382  40.180 1.364   1.00 37.73 ? 124 ARG B NH1 1 
ATOM   5134 N NH2 . ARG B 1 124 ? -5.190  38.060 1.672   1.00 42.49 ? 124 ARG B NH2 1 
ATOM   5135 N N   . GLU B 1 125 ? -6.313  44.965 1.280   1.00 30.50 ? 125 GLU B N   1 
ATOM   5136 C CA  . GLU B 1 125 ? -5.763  45.169 2.614   1.00 30.49 ? 125 GLU B CA  1 
ATOM   5137 C C   . GLU B 1 125 ? -6.703  46.022 3.457   1.00 28.93 ? 125 GLU B C   1 
ATOM   5138 O O   . GLU B 1 125 ? -6.848  45.804 4.669   1.00 28.92 ? 125 GLU B O   1 
ATOM   5139 C CB  . GLU B 1 125 ? -4.376  45.812 2.500   1.00 36.60 ? 125 GLU B CB  1 
ATOM   5140 C CG  . GLU B 1 125 ? -3.319  44.941 1.799   1.00 44.26 ? 125 GLU B CG  1 
ATOM   5141 C CD  . GLU B 1 125 ? -3.672  44.563 0.350   1.00 57.33 ? 125 GLU B CD  1 
ATOM   5142 O OE1 . GLU B 1 125 ? -3.871  43.352 0.083   1.00 59.42 ? 125 GLU B OE1 1 
ATOM   5143 O OE2 . GLU B 1 125 ? -3.762  45.468 -0.516  1.00 49.43 ? 125 GLU B OE2 1 
ATOM   5144 N N   . GLU B 1 126 ? -7.382  46.976 2.825   1.00 27.15 ? 126 GLU B N   1 
ATOM   5145 C CA  . GLU B 1 126 ? -8.356  47.774 3.555   1.00 28.74 ? 126 GLU B CA  1 
ATOM   5146 C C   . GLU B 1 126 ? -9.528  46.915 3.995   1.00 28.50 ? 126 GLU B C   1 
ATOM   5147 O O   . GLU B 1 126 ? -10.026 47.056 5.122   1.00 28.39 ? 126 GLU B O   1 
ATOM   5148 C CB  . GLU B 1 126 ? -8.812  48.952 2.694   1.00 28.34 ? 126 GLU B CB  1 
ATOM   5149 C CG  . GLU B 1 126 ? -7.824  50.125 2.746   1.00 34.93 ? 126 GLU B CG  1 
ATOM   5150 C CD  . GLU B 1 126 ? -7.732  50.910 1.458   1.00 38.86 ? 126 GLU B CD  1 
ATOM   5151 O OE1 . GLU B 1 126 ? -8.495  50.627 0.508   1.00 39.27 ? 126 GLU B OE1 1 
ATOM   5152 O OE2 . GLU B 1 126 ? -6.877  51.823 1.398   1.00 44.30 ? 126 GLU B OE2 1 
ATOM   5153 N N   . LEU B 1 127 ? -9.954  45.984 3.141   1.00 26.49 ? 127 LEU B N   1 
ATOM   5154 C CA  . LEU B 1 127 ? -11.083 45.137 3.505   1.00 28.30 ? 127 LEU B CA  1 
ATOM   5155 C C   . LEU B 1 127 ? -10.702 44.166 4.619   1.00 28.19 ? 127 LEU B C   1 
ATOM   5156 O O   . LEU B 1 127 ? -11.512 43.894 5.514   1.00 28.20 ? 127 LEU B O   1 
ATOM   5157 C CB  . LEU B 1 127 ? -11.593 44.390 2.272   1.00 26.35 ? 127 LEU B CB  1 
ATOM   5158 C CG  . LEU B 1 127 ? -12.404 45.225 1.275   1.00 30.21 ? 127 LEU B CG  1 
ATOM   5159 C CD1 . LEU B 1 127 ? -12.681 44.422 0.030   1.00 29.75 ? 127 LEU B CD1 1 
ATOM   5160 C CD2 . LEU B 1 127 ? -13.697 45.685 1.907   1.00 30.12 ? 127 LEU B CD2 1 
ATOM   5161 N N   . LEU B 1 128 ? -9.470  43.642 4.582   1.00 27.66 ? 128 LEU B N   1 
ATOM   5162 C CA  . LEU B 1 128 ? -8.967  42.809 5.673   1.00 27.37 ? 128 LEU B CA  1 
ATOM   5163 C C   . LEU B 1 128 ? -8.990  43.558 6.993   1.00 26.14 ? 128 LEU B C   1 
ATOM   5164 O O   . LEU B 1 128 ? -9.350  42.988 8.028   1.00 26.48 ? 128 LEU B O   1 
ATOM   5165 C CB  . LEU B 1 128 ? -7.544  42.333 5.369   1.00 31.79 ? 128 LEU B CB  1 
ATOM   5166 C CG  . LEU B 1 128 ? -7.401  40.872 4.936   1.00 34.01 ? 128 LEU B CG  1 
ATOM   5167 C CD1 . LEU B 1 128 ? -5.962  40.583 4.540   1.00 31.94 ? 128 LEU B CD1 1 
ATOM   5168 C CD2 . LEU B 1 128 ? -7.877  39.895 6.019   1.00 35.15 ? 128 LEU B CD2 1 
ATOM   5169 N N   . ASP B 1 129 ? -8.587  44.832 6.988   1.00 25.93 ? 129 ASP B N   1 
ATOM   5170 C CA  . ASP B 1 129 ? -8.654  45.615 8.219   1.00 27.30 ? 129 ASP B CA  1 
ATOM   5171 C C   . ASP B 1 129 ? -10.097 45.841 8.641   1.00 26.25 ? 129 ASP B C   1 
ATOM   5172 O O   . ASP B 1 129 ? -10.413 45.805 9.837   1.00 24.54 ? 129 ASP B O   1 
ATOM   5173 C CB  . ASP B 1 129 ? -7.931  46.955 8.048   1.00 23.47 ? 129 ASP B CB  1 
ATOM   5174 C CG  . ASP B 1 129 ? -6.434  46.808 8.045   1.00 35.52 ? 129 ASP B CG  1 
ATOM   5175 O OD1 . ASP B 1 129 ? -5.946  45.659 8.194   1.00 35.92 ? 129 ASP B OD1 1 
ATOM   5176 O OD2 . ASP B 1 129 ? -5.733  47.829 7.871   1.00 33.90 ? 129 ASP B OD2 1 
ATOM   5177 N N   . LEU B 1 130 ? -10.991 46.061 7.673   1.00 23.99 ? 130 LEU B N   1 
ATOM   5178 C CA  . LEU B 1 130 ? -12.402 46.239 8.001   1.00 26.80 ? 130 LEU B CA  1 
ATOM   5179 C C   . LEU B 1 130 ? -12.988 44.977 8.622   1.00 27.87 ? 130 LEU B C   1 
ATOM   5180 O O   . LEU B 1 130 ? -13.749 45.051 9.598   1.00 23.49 ? 130 LEU B O   1 
ATOM   5181 C CB  . LEU B 1 130 ? -13.197 46.640 6.749   1.00 25.95 ? 130 LEU B CB  1 
ATOM   5182 C CG  . LEU B 1 130 ? -14.626 47.110 7.031   1.00 28.12 ? 130 LEU B CG  1 
ATOM   5183 C CD1 . LEU B 1 130 ? -14.601 48.235 8.043   1.00 26.30 ? 130 LEU B CD1 1 
ATOM   5184 C CD2 . LEU B 1 130 ? -15.344 47.556 5.759   1.00 27.92 ? 130 LEU B CD2 1 
ATOM   5185 N N   . GLN B 1 131 ? -12.648 43.807 8.077   1.00 21.42 ? 131 GLN B N   1 
ATOM   5186 C CA  . GLN B 1 131 ? -13.161 42.568 8.660   1.00 23.70 ? 131 GLN B CA  1 
ATOM   5187 C C   . GLN B 1 131 ? -12.614 42.366 10.064  1.00 25.74 ? 131 GLN B C   1 
ATOM   5188 O O   . GLN B 1 131 ? -13.352 42.014 10.993  1.00 24.69 ? 131 GLN B O   1 
ATOM   5189 C CB  . GLN B 1 131 ? -12.787 41.365 7.790   1.00 26.14 ? 131 GLN B CB  1 
ATOM   5190 C CG  . GLN B 1 131 ? -13.421 41.320 6.403   1.00 24.80 ? 131 GLN B CG  1 
ATOM   5191 C CD  . GLN B 1 131 ? -12.712 40.299 5.533   1.00 26.35 ? 131 GLN B CD  1 
ATOM   5192 O OE1 . GLN B 1 131 ? -11.483 40.157 5.602   1.00 22.29 ? 131 GLN B OE1 1 
ATOM   5193 N NE2 . GLN B 1 131 ? -13.473 39.571 4.718   1.00 22.65 ? 131 GLN B NE2 1 
ATOM   5194 N N   . THR B 1 132 ? -11.307 42.569 10.229  1.00 19.20 ? 132 THR B N   1 
ATOM   5195 C CA  . THR B 1 132 ? -10.656 42.227 11.489  1.00 22.23 ? 132 THR B CA  1 
ATOM   5196 C C   . THR B 1 132 ? -11.047 43.204 12.586  1.00 26.11 ? 132 THR B C   1 
ATOM   5197 O O   . THR B 1 132 ? -11.286 42.800 13.733  1.00 24.88 ? 132 THR B O   1 
ATOM   5198 C CB  . THR B 1 132 ? -9.142  42.205 11.288  1.00 22.19 ? 132 THR B CB  1 
ATOM   5199 O OG1 . THR B 1 132 ? -8.839  41.358 10.176  1.00 23.67 ? 132 THR B OG1 1 
ATOM   5200 C CG2 . THR B 1 132 ? -8.438  41.667 12.509  1.00 21.45 ? 132 THR B CG2 1 
ATOM   5201 N N   . LEU B 1 133 ? -11.129 44.494 12.255  1.00 20.91 ? 133 LEU B N   1 
ATOM   5202 C CA  . LEU B 1 133 ? -11.470 45.468 13.285  1.00 21.25 ? 133 LEU B CA  1 
ATOM   5203 C C   . LEU B 1 133 ? -12.922 45.334 13.711  1.00 22.28 ? 133 LEU B C   1 
ATOM   5204 O O   . LEU B 1 133 ? -13.251 45.578 14.876  1.00 21.80 ? 133 LEU B O   1 
ATOM   5205 C CB  . LEU B 1 133 ? -11.163 46.882 12.789  1.00 20.08 ? 133 LEU B CB  1 
ATOM   5206 C CG  . LEU B 1 133 ? -9.669  47.194 12.728  1.00 29.92 ? 133 LEU B CG  1 
ATOM   5207 C CD1 . LEU B 1 133 ? -9.406  48.380 11.825  1.00 34.84 ? 133 LEU B CD1 1 
ATOM   5208 C CD2 . LEU B 1 133 ? -9.105  47.439 14.152  1.00 23.05 ? 133 LEU B CD2 1 
ATOM   5209 N N   . ASN B 1 134 ? -13.804 44.944 12.790  1.00 22.06 ? 134 ASN B N   1 
ATOM   5210 C CA  . ASN B 1 134 ? -15.153 44.594 13.198  1.00 21.56 ? 134 ASN B CA  1 
ATOM   5211 C C   . ASN B 1 134 ? -15.136 43.466 14.224  1.00 22.60 ? 134 ASN B C   1 
ATOM   5212 O O   . ASN B 1 134 ? -15.839 43.535 15.235  1.00 24.32 ? 134 ASN B O   1 
ATOM   5213 C CB  . ASN B 1 134 ? -15.993 44.240 11.969  1.00 20.48 ? 134 ASN B CB  1 
ATOM   5214 C CG  . ASN B 1 134 ? -16.818 45.422 11.472  1.00 22.59 ? 134 ASN B CG  1 
ATOM   5215 O OD1 . ASN B 1 134 ? -17.871 45.741 12.036  1.00 20.26 ? 134 ASN B OD1 1 
ATOM   5216 N ND2 . ASN B 1 134 ? -16.320 46.102 10.437  1.00 25.68 ? 134 ASN B ND2 1 
ATOM   5217 N N   . LEU B 1 135 ? -14.308 42.444 14.015  1.00 19.66 ? 135 LEU B N   1 
ATOM   5218 C CA  . LEU B 1 135 ? -14.154 41.404 15.032  1.00 22.05 ? 135 LEU B CA  1 
ATOM   5219 C C   . LEU B 1 135 ? -13.588 41.984 16.324  1.00 17.35 ? 135 LEU B C   1 
ATOM   5220 O O   . LEU B 1 135 ? -14.127 41.752 17.414  1.00 21.29 ? 135 LEU B O   1 
ATOM   5221 C CB  . LEU B 1 135 ? -13.229 40.290 14.531  1.00 24.37 ? 135 LEU B CB  1 
ATOM   5222 C CG  . LEU B 1 135 ? -13.722 39.301 13.484  1.00 23.17 ? 135 LEU B CG  1 
ATOM   5223 C CD1 . LEU B 1 135 ? -12.548 38.346 13.154  1.00 23.12 ? 135 LEU B CD1 1 
ATOM   5224 C CD2 . LEU B 1 135 ? -14.918 38.537 14.002  1.00 19.04 ? 135 LEU B CD2 1 
ATOM   5225 N N   . LEU B 1 136 ? -12.476 42.722 16.222  1.00 17.05 ? 136 LEU B N   1 
ATOM   5226 C CA  . LEU B 1 136 ? -11.790 43.183 17.427  1.00 17.06 ? 136 LEU B CA  1 
ATOM   5227 C C   . LEU B 1 136 ? -12.654 44.148 18.232  1.00 21.04 ? 136 LEU B C   1 
ATOM   5228 O O   . LEU B 1 136 ? -12.503 44.227 19.463  1.00 16.48 ? 136 LEU B O   1 
ATOM   5229 C CB  . LEU B 1 136 ? -10.453 43.824 17.062  1.00 21.32 ? 136 LEU B CB  1 
ATOM   5230 C CG  . LEU B 1 136 ? -9.396  42.796 16.655  1.00 21.66 ? 136 LEU B CG  1 
ATOM   5231 C CD1 . LEU B 1 136 ? -8.100  43.451 16.159  1.00 19.02 ? 136 LEU B CD1 1 
ATOM   5232 C CD2 . LEU B 1 136 ? -9.095  41.887 17.841  1.00 23.85 ? 136 LEU B CD2 1 
ATOM   5233 N N   . ALA B 1 137 ? -13.578 44.859 17.566  1.00 19.11 ? 137 ALA B N   1 
ATOM   5234 C CA  . ALA B 1 137 ? -14.433 45.810 18.273  1.00 23.82 ? 137 ALA B CA  1 
ATOM   5235 C C   . ALA B 1 137 ? -15.292 45.113 19.312  1.00 17.56 ? 137 ALA B C   1 
ATOM   5236 O O   . ALA B 1 137 ? -15.638 45.714 20.339  1.00 18.10 ? 137 ALA B O   1 
ATOM   5237 C CB  . ALA B 1 137 ? -15.322 46.564 17.283  1.00 21.69 ? 137 ALA B CB  1 
ATOM   5238 N N   . TRP B 1 138 ? -15.631 43.849 19.071  1.00 19.49 ? 138 TRP B N   1 
ATOM   5239 C CA  . TRP B 1 138 ? -16.475 43.067 19.965  1.00 19.30 ? 138 TRP B CA  1 
ATOM   5240 C C   . TRP B 1 138 ? -15.654 42.185 20.903  1.00 19.09 ? 138 TRP B C   1 
ATOM   5241 O O   . TRP B 1 138 ? -16.191 41.243 21.501  1.00 18.01 ? 138 TRP B O   1 
ATOM   5242 C CB  . TRP B 1 138 ? -17.461 42.225 19.145  1.00 17.14 ? 138 TRP B CB  1 
ATOM   5243 C CG  . TRP B 1 138 ? -18.439 43.082 18.373  1.00 19.12 ? 138 TRP B CG  1 
ATOM   5244 C CD1 . TRP B 1 138 ? -18.225 43.678 17.158  1.00 16.71 ? 138 TRP B CD1 1 
ATOM   5245 C CD2 . TRP B 1 138 ? -19.765 43.458 18.772  1.00 19.28 ? 138 TRP B CD2 1 
ATOM   5246 N NE1 . TRP B 1 138 ? -19.330 44.407 16.786  1.00 18.77 ? 138 TRP B NE1 1 
ATOM   5247 C CE2 . TRP B 1 138 ? -20.291 44.284 17.755  1.00 19.71 ? 138 TRP B CE2 1 
ATOM   5248 C CE3 . TRP B 1 138 ? -20.566 43.162 19.879  1.00 21.78 ? 138 TRP B CE3 1 
ATOM   5249 C CZ2 . TRP B 1 138 ? -21.571 44.818 17.816  1.00 18.81 ? 138 TRP B CZ2 1 
ATOM   5250 C CZ3 . TRP B 1 138 ? -21.840 43.705 19.942  1.00 25.51 ? 138 TRP B CZ3 1 
ATOM   5251 C CH2 . TRP B 1 138 ? -22.326 44.525 18.924  1.00 24.46 ? 138 TRP B CH2 1 
ATOM   5252 N N   . CYS B 1 139 ? -14.368 42.481 21.068  1.00 17.13 ? 139 CYS B N   1 
ATOM   5253 C CA  . CYS B 1 139 ? -13.548 41.692 21.989  1.00 14.31 ? 139 CYS B CA  1 
ATOM   5254 C C   . CYS B 1 139 ? -14.056 41.849 23.424  1.00 18.88 ? 139 CYS B C   1 
ATOM   5255 O O   . CYS B 1 139 ? -14.306 42.964 23.893  1.00 18.75 ? 139 CYS B O   1 
ATOM   5256 C CB  . CYS B 1 139 ? -12.089 42.121 21.898  1.00 17.00 ? 139 CYS B CB  1 
ATOM   5257 S SG  . CYS B 1 139 ? -10.969 40.993 22.702  1.00 24.54 ? 139 CYS B SG  1 
ATOM   5258 N N   . GLY B 1 140 ? -14.227 40.725 24.121  1.00 16.97 ? 140 GLY B N   1 
ATOM   5259 C CA  . GLY B 1 140 ? -14.607 40.800 25.522  1.00 13.50 ? 140 GLY B CA  1 
ATOM   5260 C C   . GLY B 1 140 ? -13.421 40.986 26.459  1.00 19.77 ? 140 GLY B C   1 
ATOM   5261 O O   . GLY B 1 140 ? -12.257 40.991 26.077  1.00 18.97 ? 140 GLY B O   1 
ATOM   5262 N N   . ARG B 1 141 ? -13.758 41.167 27.738  1.00 14.78 ? 141 ARG B N   1 
ATOM   5263 C CA  . ARG B 1 141 ? -12.757 41.482 28.755  1.00 14.85 ? 141 ARG B CA  1 
ATOM   5264 C C   . ARG B 1 141 ? -11.654 40.433 28.819  1.00 15.46 ? 141 ARG B C   1 
ATOM   5265 O O   . ARG B 1 141 ? -10.473 40.777 28.939  1.00 16.40 ? 141 ARG B O   1 
ATOM   5266 C CB  . ARG B 1 141 ? -13.458 41.622 30.114  1.00 14.68 ? 141 ARG B CB  1 
ATOM   5267 C CG  . ARG B 1 141 ? -12.553 41.781 31.306  1.00 17.04 ? 141 ARG B CG  1 
ATOM   5268 C CD  . ARG B 1 141 ? -13.400 42.091 32.558  1.00 15.82 ? 141 ARG B CD  1 
ATOM   5269 N NE  . ARG B 1 141 ? -12.593 42.056 33.766  1.00 16.97 ? 141 ARG B NE  1 
ATOM   5270 C CZ  . ARG B 1 141 ? -12.477 40.990 34.551  1.00 19.52 ? 141 ARG B CZ  1 
ATOM   5271 N NH1 . ARG B 1 141 ? -13.116 39.871 34.253  1.00 18.26 ? 141 ARG B NH1 1 
ATOM   5272 N NH2 . ARG B 1 141 ? -11.716 41.046 35.619  1.00 28.18 ? 141 ARG B NH2 1 
ATOM   5273 N N   . THR B 1 142 ? -12.016 39.149 28.759  1.00 17.50 ? 142 THR B N   1 
ATOM   5274 C CA  . THR B 1 142 ? -11.022 38.092 28.970  1.00 18.10 ? 142 THR B CA  1 
ATOM   5275 C C   . THR B 1 142 ? -9.978  38.095 27.864  1.00 22.83 ? 142 THR B C   1 
ATOM   5276 O O   . THR B 1 142 ? -8.774  37.972 28.123  1.00 23.75 ? 142 THR B O   1 
ATOM   5277 C CB  . THR B 1 142 ? -11.711 36.731 29.022  1.00 22.77 ? 142 THR B CB  1 
ATOM   5278 O OG1 . THR B 1 142 ? -12.564 36.678 30.164  1.00 21.74 ? 142 THR B OG1 1 
ATOM   5279 C CG2 . THR B 1 142 ? -10.691 35.604 29.091  1.00 27.11 ? 142 THR B CG2 1 
ATOM   5280 N N   . LEU B 1 143 ? -10.423 38.225 26.620  1.00 23.22 ? 143 LEU B N   1 
ATOM   5281 C CA  . LEU B 1 143 ? -9.480  38.152 25.517  1.00 24.68 ? 143 LEU B CA  1 
ATOM   5282 C C   . LEU B 1 143 ? -8.783  39.477 25.254  1.00 22.99 ? 143 LEU B C   1 
ATOM   5283 O O   . LEU B 1 143 ? -7.831  39.505 24.469  1.00 26.11 ? 143 LEU B O   1 
ATOM   5284 C CB  . LEU B 1 143 ? -10.186 37.663 24.247  1.00 23.28 ? 143 LEU B CB  1 
ATOM   5285 C CG  . LEU B 1 143 ? -10.463 36.165 24.165  1.00 16.82 ? 143 LEU B CG  1 
ATOM   5286 C CD1 . LEU B 1 143 ? -11.100 35.871 22.809  1.00 18.27 ? 143 LEU B CD1 1 
ATOM   5287 C CD2 . LEU B 1 143 ? -9.208  35.346 24.366  1.00 27.90 ? 143 LEU B CD2 1 
ATOM   5288 N N   . ARG B 1 144 ? -9.200  40.563 25.911  1.00 24.59 ? 144 ARG B N   1 
ATOM   5289 C CA  . ARG B 1 144 ? -8.547  41.846 25.681  1.00 33.02 ? 144 ARG B CA  1 
ATOM   5290 C C   . ARG B 1 144 ? -7.092  41.847 26.143  1.00 40.04 ? 144 ARG B C   1 
ATOM   5291 O O   . ARG B 1 144 ? -6.293  42.645 25.634  1.00 39.67 ? 144 ARG B O   1 
ATOM   5292 C CB  . ARG B 1 144 ? -9.347  42.976 26.350  1.00 32.22 ? 144 ARG B CB  1 
ATOM   5293 C CG  . ARG B 1 144 ? -10.264 43.696 25.351  1.00 35.20 ? 144 ARG B CG  1 
ATOM   5294 C CD  . ARG B 1 144 ? -11.339 44.515 26.039  1.00 40.15 ? 144 ARG B CD  1 
ATOM   5295 N NE  . ARG B 1 144 ? -12.360 45.037 25.117  1.00 39.63 ? 144 ARG B NE  1 
ATOM   5296 C CZ  . ARG B 1 144 ? -12.384 46.286 24.649  1.00 39.29 ? 144 ARG B CZ  1 
ATOM   5297 N NH1 . ARG B 1 144 ? -11.434 47.144 24.994  1.00 43.32 ? 144 ARG B NH1 1 
ATOM   5298 N NH2 . ARG B 1 144 ? -13.363 46.686 23.834  1.00 37.57 ? 144 ARG B NH2 1 
ATOM   5299 N N   . LYS B 1 145 ? -6.704  40.943 27.045  1.00 40.96 ? 145 LYS B N   1 
ATOM   5300 C CA  . LYS B 1 145 ? -5.279  40.807 27.325  1.00 41.53 ? 145 LYS B CA  1 
ATOM   5301 C C   . LYS B 1 145 ? -4.579  39.854 26.354  1.00 42.90 ? 145 LYS B C   1 
ATOM   5302 O O   . LYS B 1 145 ? -3.483  40.167 25.866  1.00 37.70 ? 145 LYS B O   1 
ATOM   5303 C CB  . LYS B 1 145 ? -5.065  40.360 28.771  1.00 59.32 ? 145 LYS B CB  1 
ATOM   5304 C CG  . LYS B 1 145 ? -5.881  41.172 29.796  1.00 70.49 ? 145 LYS B CG  1 
ATOM   5305 C CD  . LYS B 1 145 ? -7.093  40.397 30.303  1.00 60.90 ? 145 LYS B CD  1 
ATOM   5306 C CE  . LYS B 1 145 ? -7.418  40.781 31.750  1.00 59.72 ? 145 LYS B CE  1 
ATOM   5307 N NZ  . LYS B 1 145 ? -8.786  40.341 32.190  1.00 56.47 ? 145 LYS B NZ  1 
ATOM   5308 N N   . ASP B 1 146 ? -5.209  38.722 26.011  1.00 39.14 ? 146 ASP B N   1 
ATOM   5309 C CA  . ASP B 1 146 ? -4.602  37.794 25.055  1.00 38.18 ? 146 ASP B CA  1 
ATOM   5310 C C   . ASP B 1 146 ? -4.370  38.455 23.697  1.00 42.79 ? 146 ASP B C   1 
ATOM   5311 O O   . ASP B 1 146 ? -3.387  38.155 23.008  1.00 43.08 ? 146 ASP B O   1 
ATOM   5312 C CB  . ASP B 1 146 ? -5.493  36.564 24.885  1.00 45.00 ? 146 ASP B CB  1 
ATOM   5313 C CG  . ASP B 1 146 ? -4.881  35.305 25.467  1.00 55.78 ? 146 ASP B CG  1 
ATOM   5314 O OD1 . ASP B 1 146 ? -3.929  35.416 26.272  1.00 57.22 ? 146 ASP B OD1 1 
ATOM   5315 O OD2 . ASP B 1 146 ? -5.357  34.203 25.119  1.00 56.98 ? 146 ASP B OD2 1 
ATOM   5316 N N   . LEU B 1 147 ? -5.273  39.344 23.285  1.00 33.14 ? 147 LEU B N   1 
ATOM   5317 C CA  . LEU B 1 147 ? -5.219  39.959 21.966  1.00 25.42 ? 147 LEU B CA  1 
ATOM   5318 C C   . LEU B 1 147 ? -4.695  41.397 22.010  1.00 24.66 ? 147 LEU B C   1 
ATOM   5319 O O   . LEU B 1 147 ? -4.876  42.143 21.042  1.00 33.65 ? 147 LEU B O   1 
ATOM   5320 C CB  . LEU B 1 147 ? -6.602  39.909 21.317  1.00 28.17 ? 147 LEU B CB  1 
ATOM   5321 C CG  . LEU B 1 147 ? -7.243  38.525 21.160  1.00 26.54 ? 147 LEU B CG  1 
ATOM   5322 C CD1 . LEU B 1 147 ? -8.641  38.611 20.567  1.00 26.49 ? 147 LEU B CD1 1 
ATOM   5323 C CD2 . LEU B 1 147 ? -6.363  37.645 20.289  1.00 40.63 ? 147 LEU B CD2 1 
ATOM   5324 N N   . LYS B 1 148 ? -4.028  41.797 23.101  1.00 28.64 ? 148 LYS B N   1 
ATOM   5325 C CA  . LYS B 1 148 ? -3.602  43.191 23.219  1.00 30.35 ? 148 LYS B CA  1 
ATOM   5326 C C   . LYS B 1 148 ? -2.657  43.584 22.087  1.00 30.37 ? 148 LYS B C   1 
ATOM   5327 O O   . LYS B 1 148 ? -2.714  44.712 21.586  1.00 25.56 ? 148 LYS B O   1 
ATOM   5328 C CB  . LYS B 1 148 ? -2.966  43.442 24.589  1.00 24.87 ? 148 LYS B CB  1 
ATOM   5329 C CG  . LYS B 1 148 ? -2.220  44.777 24.725  1.00 25.43 ? 148 LYS B CG  1 
ATOM   5330 C CD  . LYS B 1 148 ? -1.603  44.928 26.130  1.00 34.74 ? 148 LYS B CD  1 
ATOM   5331 C CE  . LYS B 1 148 ? -1.770  46.351 26.685  1.00 46.93 ? 148 LYS B CE  1 
ATOM   5332 N NZ  . LYS B 1 148 ? -1.859  47.403 25.615  1.00 54.61 ? 148 LYS B NZ  1 
ATOM   5333 N N   . ASP B 1 149 ? -1.792  42.667 21.656  1.00 29.87 ? 149 ASP B N   1 
ATOM   5334 C CA  . ASP B 1 149 ? -0.911  42.972 20.531  1.00 34.04 ? 149 ASP B CA  1 
ATOM   5335 C C   . ASP B 1 149 ? -1.714  43.322 19.281  1.00 33.24 ? 149 ASP B C   1 
ATOM   5336 O O   . ASP B 1 149 ? -1.453  44.335 18.616  1.00 36.96 ? 149 ASP B O   1 
ATOM   5337 C CB  . ASP B 1 149 ? 0.018   41.790 20.247  1.00 39.23 ? 149 ASP B CB  1 
ATOM   5338 C CG  . ASP B 1 149 ? 1.034   41.579 21.348  1.00 62.84 ? 149 ASP B CG  1 
ATOM   5339 O OD1 . ASP B 1 149 ? 1.354   42.570 22.037  1.00 73.91 ? 149 ASP B OD1 1 
ATOM   5340 O OD2 . ASP B 1 149 ? 1.531   40.442 21.508  1.00 66.85 ? 149 ASP B OD2 1 
ATOM   5341 N N   . LEU B 1 150 ? -2.702  42.491 18.945  1.00 26.71 ? 150 LEU B N   1 
ATOM   5342 C CA  . LEU B 1 150 ? -3.519  42.766 17.768  1.00 22.49 ? 150 LEU B CA  1 
ATOM   5343 C C   . LEU B 1 150 ? -4.332  44.038 17.953  1.00 23.50 ? 150 LEU B C   1 
ATOM   5344 O O   . LEU B 1 150 ? -4.428  44.855 17.031  1.00 26.85 ? 150 LEU B O   1 
ATOM   5345 C CB  . LEU B 1 150 ? -4.409  41.569 17.469  1.00 27.41 ? 150 LEU B CB  1 
ATOM   5346 C CG  . LEU B 1 150 ? -3.598  40.432 16.840  1.00 33.82 ? 150 LEU B CG  1 
ATOM   5347 C CD1 . LEU B 1 150 ? -4.427  39.165 16.651  1.00 27.22 ? 150 LEU B CD1 1 
ATOM   5348 C CD2 . LEU B 1 150 ? -2.993  40.898 15.511  1.00 33.03 ? 150 LEU B CD2 1 
ATOM   5349 N N   . LEU B 1 151 ? -4.901  44.238 19.149  1.00 24.03 ? 151 LEU B N   1 
ATOM   5350 C CA  . LEU B 1 151 ? -5.711  45.426 19.394  1.00 26.87 ? 151 LEU B CA  1 
ATOM   5351 C C   . LEU B 1 151 ? -4.894  46.690 19.198  1.00 34.79 ? 151 LEU B C   1 
ATOM   5352 O O   . LEU B 1 151 ? -5.372  47.660 18.596  1.00 36.74 ? 151 LEU B O   1 
ATOM   5353 C CB  . LEU B 1 151 ? -6.280  45.384 20.816  1.00 27.18 ? 151 LEU B CB  1 
ATOM   5354 C CG  . LEU B 1 151 ? -7.501  44.487 20.982  1.00 28.96 ? 151 LEU B CG  1 
ATOM   5355 C CD1 . LEU B 1 151 ? -7.736  44.175 22.461  1.00 30.74 ? 151 LEU B CD1 1 
ATOM   5356 C CD2 . LEU B 1 151 ? -8.736  45.125 20.346  1.00 21.92 ? 151 LEU B CD2 1 
ATOM   5357 N N   . ASN B 1 152 ? -3.661  46.707 19.722  1.00 29.75 ? 152 ASN B N   1 
ATOM   5358 C CA  . ASN B 1 152 ? -2.812  47.878 19.587  1.00 27.02 ? 152 ASN B CA  1 
ATOM   5359 C C   . ASN B 1 152 ? -2.210  48.009 18.199  1.00 31.05 ? 152 ASN B C   1 
ATOM   5360 O O   . ASN B 1 152 ? -1.785  49.109 17.837  1.00 35.79 ? 152 ASN B O   1 
ATOM   5361 C CB  . ASN B 1 152 ? -1.657  47.852 20.598  1.00 34.59 ? 152 ASN B CB  1 
ATOM   5362 C CG  . ASN B 1 152 ? -2.122  48.000 22.035  1.00 43.23 ? 152 ASN B CG  1 
ATOM   5363 O OD1 . ASN B 1 152 ? -3.294  48.280 22.303  1.00 47.00 ? 152 ASN B OD1 1 
ATOM   5364 N ND2 . ASN B 1 152 ? -1.203  47.810 22.966  1.00 45.96 ? 152 ASN B ND2 1 
ATOM   5365 N N   . LYS B 1 153 ? -2.093  46.908 17.452  1.00 35.25 ? 153 LYS B N   1 
ATOM   5366 C CA  . LYS B 1 153 ? -1.606  47.007 16.080  1.00 32.68 ? 153 LYS B CA  1 
ATOM   5367 C C   . LYS B 1 153 ? -2.446  47.998 15.283  1.00 35.14 ? 153 LYS B C   1 
ATOM   5368 O O   . LYS B 1 153 ? -1.905  48.833 14.545  1.00 37.83 ? 153 LYS B O   1 
ATOM   5369 C CB  . LYS B 1 153 ? -1.615  45.628 15.413  1.00 29.89 ? 153 LYS B CB  1 
ATOM   5370 C CG  . LYS B 1 153 ? -0.988  45.609 14.022  1.00 29.18 ? 153 LYS B CG  1 
ATOM   5371 C CD  . LYS B 1 153 ? -1.036  44.213 13.412  1.00 36.67 ? 153 LYS B CD  1 
ATOM   5372 C CE  . LYS B 1 153 ? -0.215  44.146 12.141  1.00 38.69 ? 153 LYS B CE  1 
ATOM   5373 N NZ  . LYS B 1 153 ? -0.061  42.753 11.630  1.00 47.30 ? 153 LYS B NZ  1 
ATOM   5374 N N   . GLY B 1 154 ? -3.772  47.923 15.424  1.00 29.51 ? 154 GLY B N   1 
ATOM   5375 C CA  . GLY B 1 154 ? -4.671  48.927 14.898  1.00 31.83 ? 154 GLY B CA  1 
ATOM   5376 C C   . GLY B 1 154 ? -4.945  48.874 13.406  1.00 34.31 ? 154 GLY B C   1 
ATOM   5377 O O   . GLY B 1 154 ? -5.915  49.493 12.958  1.00 32.42 ? 154 GLY B O   1 
ATOM   5378 N N   . ARG B 1 155 ? -4.142  48.158 12.619  1.00 31.85 ? 155 ARG B N   1 
ATOM   5379 C CA  . ARG B 1 155 ? -4.280  48.196 11.166  1.00 28.48 ? 155 ARG B CA  1 
ATOM   5380 C C   . ARG B 1 155 ? -3.331  47.178 10.543  1.00 34.23 ? 155 ARG B C   1 
ATOM   5381 O O   . ARG B 1 155 ? -2.508  46.559 11.228  1.00 36.29 ? 155 ARG B O   1 
ATOM   5382 C CB  . ARG B 1 155 ? -3.990  49.592 10.625  1.00 37.47 ? 155 ARG B CB  1 
ATOM   5383 C CG  . ARG B 1 155 ? -2.527  49.972 10.706  1.00 43.44 ? 155 ARG B CG  1 
ATOM   5384 C CD  . ARG B 1 155 ? -2.286  51.359 10.119  1.00 52.72 ? 155 ARG B CD  1 
ATOM   5385 N NE  . ARG B 1 155 ? -3.064  52.371 10.831  1.00 54.32 ? 155 ARG B NE  1 
ATOM   5386 C CZ  . ARG B 1 155 ? -3.624  53.429 10.252  1.00 47.06 ? 155 ARG B CZ  1 
ATOM   5387 N NH1 . ARG B 1 155 ? -4.319  54.295 10.986  1.00 47.05 ? 155 ARG B NH1 1 
ATOM   5388 N NH2 . ARG B 1 155 ? -3.489  53.616 8.945   1.00 44.06 ? 155 ARG B NH2 1 
ATOM   5389 N N   . ASN B 1 156 ? -3.426  47.050 9.213   1.00 30.28 ? 156 ASN B N   1 
ATOM   5390 C CA  . ASN B 1 156 ? -2.592  46.144 8.403   1.00 32.79 ? 156 ASN B CA  1 
ATOM   5391 C C   . ASN B 1 156 ? -2.641  44.717 8.941   1.00 32.80 ? 156 ASN B C   1 
ATOM   5392 O O   . ASN B 1 156 ? -1.620  44.052 9.110   1.00 35.70 ? 156 ASN B O   1 
ATOM   5393 C CB  . ASN B 1 156 ? -1.146  46.632 8.304   1.00 42.72 ? 156 ASN B CB  1 
ATOM   5394 C CG  . ASN B 1 156 ? -1.041  48.103 7.967   1.00 48.15 ? 156 ASN B CG  1 
ATOM   5395 O OD1 . ASN B 1 156 ? -0.488  48.881 8.745   1.00 66.72 ? 156 ASN B OD1 1 
ATOM   5396 N ND2 . ASN B 1 156 ? -1.565  48.495 6.822   1.00 46.34 ? 156 ASN B ND2 1 
ATOM   5397 N N   . TYR B 1 157 ? -3.852  44.248 9.213   1.00 25.76 ? 157 TYR B N   1 
ATOM   5398 C CA  . TYR B 1 157 ? -4.068  42.880 9.657   1.00 27.16 ? 157 TYR B CA  1 
ATOM   5399 C C   . TYR B 1 157 ? -3.921  41.908 8.490   1.00 28.78 ? 157 TYR B C   1 
ATOM   5400 O O   . TYR B 1 157 ? -4.145  42.264 7.331   1.00 30.35 ? 157 TYR B O   1 
ATOM   5401 C CB  . TYR B 1 157 ? -5.459  42.758 10.280  1.00 22.98 ? 157 TYR B CB  1 
ATOM   5402 C CG  . TYR B 1 157 ? -5.595  43.589 11.539  1.00 22.47 ? 157 TYR B CG  1 
ATOM   5403 C CD1 . TYR B 1 157 ? -5.066  43.143 12.737  1.00 22.36 ? 157 TYR B CD1 1 
ATOM   5404 C CD2 . TYR B 1 157 ? -6.242  44.813 11.518  1.00 32.10 ? 157 TYR B CD2 1 
ATOM   5405 C CE1 . TYR B 1 157 ? -5.184  43.902 13.897  1.00 24.98 ? 157 TYR B CE1 1 
ATOM   5406 C CE2 . TYR B 1 157 ? -6.366  45.580 12.672  1.00 32.91 ? 157 TYR B CE2 1 
ATOM   5407 C CZ  . TYR B 1 157 ? -5.831  45.118 13.853  1.00 27.49 ? 157 TYR B CZ  1 
ATOM   5408 O OH  . TYR B 1 157 ? -5.960  45.890 14.989  1.00 24.89 ? 157 TYR B OH  1 
ATOM   5409 N N   . THR B 1 158 ? -3.515  40.681 8.803   1.00 27.30 ? 158 THR B N   1 
ATOM   5410 C CA  . THR B 1 158 ? -3.383  39.619 7.815   1.00 28.09 ? 158 THR B CA  1 
ATOM   5411 C C   . THR B 1 158 ? -4.526  38.619 7.946   1.00 32.80 ? 158 THR B C   1 
ATOM   5412 O O   . THR B 1 158 ? -5.219  38.562 8.963   1.00 23.76 ? 158 THR B O   1 
ATOM   5413 C CB  . THR B 1 158 ? -2.059  38.865 7.965   1.00 31.96 ? 158 THR B CB  1 
ATOM   5414 O OG1 . THR B 1 158 ? -2.065  38.162 9.217   1.00 32.27 ? 158 THR B OG1 1 
ATOM   5415 C CG2 . THR B 1 158 ? -0.867  39.816 7.909   1.00 32.90 ? 158 THR B CG2 1 
ATOM   5416 N N   . GLN B 1 159 ? -4.706  37.811 6.892   1.00 33.23 ? 159 GLN B N   1 
ATOM   5417 C CA  . GLN B 1 159 ? -5.720  36.761 6.940   1.00 27.72 ? 159 GLN B CA  1 
ATOM   5418 C C   . GLN B 1 159 ? -5.449  35.793 8.086   1.00 26.44 ? 159 GLN B C   1 
ATOM   5419 O O   . GLN B 1 159 ? -6.376  35.392 8.801   1.00 26.84 ? 159 GLN B O   1 
ATOM   5420 C CB  . GLN B 1 159 ? -5.780  36.008 5.602   1.00 30.36 ? 159 GLN B CB  1 
ATOM   5421 C CG  . GLN B 1 159 ? -6.735  34.800 5.605   1.00 31.45 ? 159 GLN B CG  1 
ATOM   5422 C CD  . GLN B 1 159 ? -8.205  35.199 5.512   1.00 36.30 ? 159 GLN B CD  1 
ATOM   5423 O OE1 . GLN B 1 159 ? -8.541  36.280 5.022   1.00 29.75 ? 159 GLN B OE1 1 
ATOM   5424 N NE2 . GLN B 1 159 ? -9.088  34.326 6.000   1.00 33.31 ? 159 GLN B NE2 1 
ATOM   5425 N N   . GLU B 1 160 ? -4.181  35.425 8.297   1.00 28.37 ? 160 GLU B N   1 
ATOM   5426 C CA  . GLU B 1 160 ? -3.856  34.519 9.396   1.00 30.48 ? 160 GLU B CA  1 
ATOM   5427 C C   . GLU B 1 160 ? -4.196  35.136 10.752  1.00 31.12 ? 160 GLU B C   1 
ATOM   5428 O O   . GLU B 1 160 ? -4.698  34.442 11.649  1.00 30.75 ? 160 GLU B O   1 
ATOM   5429 C CB  . GLU B 1 160 ? -2.379  34.116 9.352   1.00 36.40 ? 160 GLU B CB  1 
ATOM   5430 C CG  . GLU B 1 160 ? -2.024  33.173 10.499  1.00 45.86 ? 160 GLU B CG  1 
ATOM   5431 C CD  . GLU B 1 160 ? -0.603  32.648 10.456  1.00 53.16 ? 160 GLU B CD  1 
ATOM   5432 O OE1 . GLU B 1 160 ? 0.214   33.209 9.698   1.00 56.50 ? 160 GLU B OE1 1 
ATOM   5433 O OE2 . GLU B 1 160 ? -0.305  31.685 11.205  1.00 48.63 ? 160 GLU B OE2 1 
ATOM   5434 N N   . GLU B 1 161 ? -3.926  36.435 10.935  1.00 24.30 ? 161 GLU B N   1 
ATOM   5435 C CA  . GLU B 1 161 ? -4.272  37.064 12.218  1.00 23.33 ? 161 GLU B CA  1 
ATOM   5436 C C   . GLU B 1 161 ? -5.783  37.109 12.425  1.00 24.55 ? 161 GLU B C   1 
ATOM   5437 O O   . GLU B 1 161 ? -6.274  36.887 13.542  1.00 22.51 ? 161 GLU B O   1 
ATOM   5438 C CB  . GLU B 1 161 ? -3.679  38.472 12.303  1.00 27.04 ? 161 GLU B CB  1 
ATOM   5439 C CG  . GLU B 1 161 ? -2.184  38.482 12.547  1.00 29.81 ? 161 GLU B CG  1 
ATOM   5440 C CD  . GLU B 1 161 ? -1.535  39.834 12.339  1.00 34.81 ? 161 GLU B CD  1 
ATOM   5441 O OE1 . GLU B 1 161 ? -2.121  40.708 11.660  1.00 28.61 ? 161 GLU B OE1 1 
ATOM   5442 O OE2 . GLU B 1 161 ? -0.407  40.016 12.843  1.00 44.93 ? 161 GLU B OE2 1 
ATOM   5443 N N   . LYS B 1 162 ? -6.538  37.394 11.358  1.00 28.19 ? 162 LYS B N   1 
ATOM   5444 C CA  . LYS B 1 162 ? -7.996  37.363 11.433  1.00 25.75 ? 162 LYS B CA  1 
ATOM   5445 C C   . LYS B 1 162 ? -8.498  35.972 11.814  1.00 28.10 ? 162 LYS B C   1 
ATOM   5446 O O   . LYS B 1 162 ? -9.398  35.834 12.654  1.00 23.36 ? 162 LYS B O   1 
ATOM   5447 C CB  . LYS B 1 162 ? -8.595  37.810 10.089  1.00 26.30 ? 162 LYS B CB  1 
ATOM   5448 C CG  . LYS B 1 162 ? -10.112 37.890 10.068  1.00 27.18 ? 162 LYS B CG  1 
ATOM   5449 C CD  . LYS B 1 162 ? -10.623 38.339 8.705   1.00 26.19 ? 162 LYS B CD  1 
ATOM   5450 C CE  . LYS B 1 162 ? -10.214 37.363 7.608   1.00 28.43 ? 162 LYS B CE  1 
ATOM   5451 N NZ  . LYS B 1 162 ? -10.924 37.665 6.321   1.00 24.39 ? 162 LYS B NZ  1 
ATOM   5452 N N   . GLU B 1 163 ? -7.907  34.927 11.230  1.00 26.11 ? 163 GLU B N   1 
ATOM   5453 C CA  . GLU B 1 163 ? -8.293  33.567 11.599  1.00 28.08 ? 163 GLU B CA  1 
ATOM   5454 C C   . GLU B 1 163 ? -7.917  33.248 13.034  1.00 27.84 ? 163 GLU B C   1 
ATOM   5455 O O   . GLU B 1 163 ? -8.601  32.463 13.697  1.00 24.80 ? 163 GLU B O   1 
ATOM   5456 C CB  . GLU B 1 163 ? -7.640  32.558 10.658  1.00 23.99 ? 163 GLU B CB  1 
ATOM   5457 C CG  . GLU B 1 163 ? -8.291  32.536 9.294   1.00 25.49 ? 163 GLU B CG  1 
ATOM   5458 C CD  . GLU B 1 163 ? -7.460  31.807 8.247   1.00 39.81 ? 163 GLU B CD  1 
ATOM   5459 O OE1 . GLU B 1 163 ? -6.449  31.169 8.607   1.00 48.82 ? 163 GLU B OE1 1 
ATOM   5460 O OE2 . GLU B 1 163 ? -7.825  31.880 7.058   1.00 46.16 ? 163 GLU B OE2 1 
ATOM   5461 N N   . TYR B 1 164 ? -6.831  33.836 13.523  1.00 29.85 ? 164 TYR B N   1 
ATOM   5462 C CA  . TYR B 1 164 ? -6.436  33.624 14.908  1.00 29.78 ? 164 TYR B CA  1 
ATOM   5463 C C   . TYR B 1 164 ? -7.471  34.209 15.860  1.00 24.26 ? 164 TYR B C   1 
ATOM   5464 O O   . TYR B 1 164 ? -7.873  33.559 16.829  1.00 22.29 ? 164 TYR B O   1 
ATOM   5465 C CB  . TYR B 1 164 ? -5.060  34.242 15.153  1.00 22.63 ? 164 TYR B CB  1 
ATOM   5466 C CG  . TYR B 1 164 ? -4.595  34.119 16.578  1.00 31.19 ? 164 TYR B CG  1 
ATOM   5467 C CD1 . TYR B 1 164 ? -4.125  32.910 17.075  1.00 35.79 ? 164 TYR B CD1 1 
ATOM   5468 C CD2 . TYR B 1 164 ? -4.635  35.206 17.435  1.00 36.58 ? 164 TYR B CD2 1 
ATOM   5469 C CE1 . TYR B 1 164 ? -3.697  32.791 18.389  1.00 42.39 ? 164 TYR B CE1 1 
ATOM   5470 C CE2 . TYR B 1 164 ? -4.205  35.096 18.746  1.00 46.34 ? 164 TYR B CE2 1 
ATOM   5471 C CZ  . TYR B 1 164 ? -3.741  33.887 19.215  1.00 46.79 ? 164 TYR B CZ  1 
ATOM   5472 O OH  . TYR B 1 164 ? -3.316  33.778 20.518  1.00 55.43 ? 164 TYR B OH  1 
ATOM   5473 N N   . VAL B 1 165 ? -7.904  35.445 15.600  1.00 25.36 ? 165 VAL B N   1 
ATOM   5474 C CA  . VAL B 1 165 ? -8.960  36.065 16.404  1.00 26.02 ? 165 VAL B CA  1 
ATOM   5475 C C   . VAL B 1 165 ? -10.204 35.179 16.410  1.00 23.07 ? 165 VAL B C   1 
ATOM   5476 O O   . VAL B 1 165 ? -10.794 34.914 17.463  1.00 22.88 ? 165 VAL B O   1 
ATOM   5477 C CB  . VAL B 1 165 ? -9.287  37.476 15.875  1.00 21.47 ? 165 VAL B CB  1 
ATOM   5478 C CG1 . VAL B 1 165 ? -10.485 38.058 16.615  1.00 21.44 ? 165 VAL B CG1 1 
ATOM   5479 C CG2 . VAL B 1 165 ? -8.091  38.400 16.017  1.00 18.80 ? 165 VAL B CG2 1 
ATOM   5480 N N   . LEU B 1 166 ? -10.604 34.686 15.233  1.00 22.50 ? 166 LEU B N   1 
ATOM   5481 C CA  . LEU B 1 166 ? -11.809 33.855 15.137  1.00 18.80 ? 166 LEU B CA  1 
ATOM   5482 C C   . LEU B 1 166 ? -11.681 32.585 15.967  1.00 21.96 ? 166 LEU B C   1 
ATOM   5483 O O   . LEU B 1 166 ? -12.638 32.178 16.637  1.00 25.94 ? 166 LEU B O   1 
ATOM   5484 C CB  . LEU B 1 166 ? -12.109 33.496 13.675  1.00 20.08 ? 166 LEU B CB  1 
ATOM   5485 C CG  . LEU B 1 166 ? -12.772 34.562 12.792  1.00 22.08 ? 166 LEU B CG  1 
ATOM   5486 C CD1 . LEU B 1 166 ? -12.650 34.167 11.309  1.00 27.75 ? 166 LEU B CD1 1 
ATOM   5487 C CD2 . LEU B 1 166 ? -14.239 34.792 13.152  1.00 26.97 ? 166 LEU B CD2 1 
ATOM   5488 N N   . ASN B 1 167 ? -10.524 31.922 15.901  1.00 20.49 ? 167 ASN B N   1 
ATOM   5489 C CA  . ASN B 1 167 ? -10.302 30.717 16.694  1.00 22.81 ? 167 ASN B CA  1 
ATOM   5490 C C   . ASN B 1 167 ? -10.409 31.019 18.180  1.00 23.66 ? 167 ASN B C   1 
ATOM   5491 O O   . ASN B 1 167 ? -10.994 30.240 18.935  1.00 24.55 ? 167 ASN B O   1 
ATOM   5492 C CB  . ASN B 1 167 ? -8.937  30.111 16.389  1.00 30.54 ? 167 ASN B CB  1 
ATOM   5493 C CG  . ASN B 1 167 ? -8.917  29.365 15.073  1.00 45.72 ? 167 ASN B CG  1 
ATOM   5494 O OD1 . ASN B 1 167 ? -9.969  29.133 14.462  1.00 51.57 ? 167 ASN B OD1 1 
ATOM   5495 N ND2 . ASN B 1 167 ? -7.717  28.986 14.617  1.00 41.84 ? 167 ASN B ND2 1 
ATOM   5496 N N   . LYS B 1 168 ? -9.836  32.134 18.625  1.00 25.48 ? 168 LYS B N   1 
ATOM   5497 C CA  . LYS B 1 168 ? -9.941  32.439 20.050  1.00 25.11 ? 168 LYS B CA  1 
ATOM   5498 C C   . LYS B 1 168 ? -11.373 32.793 20.435  1.00 23.05 ? 168 LYS B C   1 
ATOM   5499 O O   . LYS B 1 168 ? -11.819 32.457 21.542  1.00 18.13 ? 168 LYS B O   1 
ATOM   5500 C CB  . LYS B 1 168 ? -8.956  33.551 20.436  1.00 20.97 ? 168 LYS B CB  1 
ATOM   5501 C CG  . LYS B 1 168 ? -7.480  33.195 20.203  1.00 27.03 ? 168 LYS B CG  1 
ATOM   5502 C CD  . LYS B 1 168 ? -6.699  32.906 21.482  1.00 38.16 ? 168 LYS B CD  1 
ATOM   5503 C CE  . LYS B 1 168 ? -7.363  31.868 22.364  1.00 42.83 ? 168 LYS B CE  1 
ATOM   5504 N NZ  . LYS B 1 168 ? -6.388  31.122 23.244  1.00 45.70 ? 168 LYS B NZ  1 
ATOM   5505 N N   . TYR B 1 169 ? -12.113 33.459 19.543  1.00 20.11 ? 169 TYR B N   1 
ATOM   5506 C CA  . TYR B 1 169 ? -13.518 33.756 19.828  1.00 21.36 ? 169 TYR B CA  1 
ATOM   5507 C C   . TYR B 1 169 ? -14.335 32.481 19.955  1.00 20.67 ? 169 TYR B C   1 
ATOM   5508 O O   . TYR B 1 169 ? -15.201 32.366 20.830  1.00 18.75 ? 169 TYR B O   1 
ATOM   5509 C CB  . TYR B 1 169 ? -14.106 34.634 18.726  1.00 22.60 ? 169 TYR B CB  1 
ATOM   5510 C CG  . TYR B 1 169 ? -13.758 36.091 18.859  1.00 19.49 ? 169 TYR B CG  1 
ATOM   5511 C CD1 . TYR B 1 169 ? -12.779 36.517 19.762  1.00 18.99 ? 169 TYR B CD1 1 
ATOM   5512 C CD2 . TYR B 1 169 ? -14.418 37.048 18.100  1.00 17.58 ? 169 TYR B CD2 1 
ATOM   5513 C CE1 . TYR B 1 169 ? -12.467 37.872 19.895  1.00 19.95 ? 169 TYR B CE1 1 
ATOM   5514 C CE2 . TYR B 1 169 ? -14.106 38.393 18.212  1.00 23.06 ? 169 TYR B CE2 1 
ATOM   5515 C CZ  . TYR B 1 169 ? -13.127 38.801 19.100  1.00 21.66 ? 169 TYR B CZ  1 
ATOM   5516 O OH  . TYR B 1 169 ? -12.822 40.142 19.210  1.00 16.89 ? 169 TYR B OH  1 
ATOM   5517 N N   . PHE B 1 170 ? -14.076 31.503 19.088  1.00 16.99 ? 170 PHE B N   1 
ATOM   5518 C CA  . PHE B 1 170 ? -14.843 30.272 19.190  1.00 19.43 ? 170 PHE B CA  1 
ATOM   5519 C C   . PHE B 1 170 ? -14.446 29.480 20.434  1.00 21.51 ? 170 PHE B C   1 
ATOM   5520 O O   . PHE B 1 170 ? -15.282 28.774 21.004  1.00 20.64 ? 170 PHE B O   1 
ATOM   5521 C CB  . PHE B 1 170 ? -14.695 29.459 17.906  1.00 20.71 ? 170 PHE B CB  1 
ATOM   5522 C CG  . PHE B 1 170 ? -15.698 29.855 16.850  1.00 24.90 ? 170 PHE B CG  1 
ATOM   5523 C CD1 . PHE B 1 170 ? -17.022 29.442 16.955  1.00 26.26 ? 170 PHE B CD1 1 
ATOM   5524 C CD2 . PHE B 1 170 ? -15.338 30.688 15.793  1.00 26.62 ? 170 PHE B CD2 1 
ATOM   5525 C CE1 . PHE B 1 170 ? -17.956 29.815 15.994  1.00 33.33 ? 170 PHE B CE1 1 
ATOM   5526 C CE2 . PHE B 1 170 ? -16.263 31.066 14.836  1.00 32.36 ? 170 PHE B CE2 1 
ATOM   5527 C CZ  . PHE B 1 170 ? -17.573 30.629 14.936  1.00 33.73 ? 170 PHE B CZ  1 
ATOM   5528 N N   . GLU B 1 171 ? -13.200 29.621 20.902  1.00 20.85 ? 171 GLU B N   1 
ATOM   5529 C CA  . GLU B 1 171 ? -12.837 29.027 22.186  1.00 22.62 ? 171 GLU B CA  1 
ATOM   5530 C C   . GLU B 1 171 ? -13.685 29.604 23.314  1.00 20.75 ? 171 GLU B C   1 
ATOM   5531 O O   . GLU B 1 171 ? -14.117 28.870 24.212  1.00 23.84 ? 171 GLU B O   1 
ATOM   5532 C CB  . GLU B 1 171 ? -11.354 29.242 22.473  1.00 20.98 ? 171 GLU B CB  1 
ATOM   5533 C CG  . GLU B 1 171 ? -10.444 28.372 21.637  1.00 33.70 ? 171 GLU B CG  1 
ATOM   5534 C CD  . GLU B 1 171 ? -8.967  28.655 21.887  1.00 46.43 ? 171 GLU B CD  1 
ATOM   5535 O OE1 . GLU B 1 171 ? -8.638  29.200 22.962  1.00 44.98 ? 171 GLU B OE1 1 
ATOM   5536 O OE2 . GLU B 1 171 ? -8.138  28.328 21.002  1.00 53.67 ? 171 GLU B OE2 1 
ATOM   5537 N N   . ILE B 1 172 ? -13.938 30.917 23.282  1.00 20.25 ? 172 ILE B N   1 
ATOM   5538 C CA  . ILE B 1 172 ? -14.747 31.562 24.320  1.00 22.78 ? 172 ILE B CA  1 
ATOM   5539 C C   . ILE B 1 172 ? -16.186 31.059 24.271  1.00 21.06 ? 172 ILE B C   1 
ATOM   5540 O O   . ILE B 1 172 ? -16.825 30.823 25.308  1.00 19.87 ? 172 ILE B O   1 
ATOM   5541 C CB  . ILE B 1 172 ? -14.680 33.097 24.169  1.00 25.49 ? 172 ILE B CB  1 
ATOM   5542 C CG1 . ILE B 1 172 ? -13.298 33.620 24.572  1.00 25.59 ? 172 ILE B CG1 1 
ATOM   5543 C CG2 . ILE B 1 172 ? -15.760 33.788 25.001  1.00 22.78 ? 172 ILE B CG2 1 
ATOM   5544 C CD1 . ILE B 1 172 ? -13.071 33.712 26.082  1.00 23.83 ? 172 ILE B CD1 1 
ATOM   5545 N N   . ILE B 1 173 ? -16.724 30.892 23.065  1.00 18.35 ? 173 ILE B N   1 
ATOM   5546 C CA  . ILE B 1 173 ? -18.084 30.395 22.938  1.00 14.69 ? 173 ILE B CA  1 
ATOM   5547 C C   . ILE B 1 173 ? -18.188 28.974 23.484  1.00 15.43 ? 173 ILE B C   1 
ATOM   5548 O O   . ILE B 1 173 ? -19.174 28.620 24.155  1.00 21.04 ? 173 ILE B O   1 
ATOM   5549 C CB  . ILE B 1 173 ? -18.554 30.488 21.470  1.00 18.28 ? 173 ILE B CB  1 
ATOM   5550 C CG1 . ILE B 1 173 ? -18.804 31.945 21.093  1.00 16.20 ? 173 ILE B CG1 1 
ATOM   5551 C CG2 . ILE B 1 173 ? -19.804 29.634 21.244  1.00 24.40 ? 173 ILE B CG2 1 
ATOM   5552 C CD1 . ILE B 1 173 ? -18.936 32.199 19.611  1.00 22.13 ? 173 ILE B CD1 1 
ATOM   5553 N N   . LYS B 1 174 ? -17.192 28.134 23.189  1.00 18.62 ? 174 LYS B N   1 
ATOM   5554 C CA  . LYS B 1 174 ? -17.201 26.753 23.648  1.00 17.34 ? 174 LYS B CA  1 
ATOM   5555 C C   . LYS B 1 174 ? -17.136 26.639 25.166  1.00 23.01 ? 174 LYS B C   1 
ATOM   5556 O O   . LYS B 1 174 ? -17.526 25.601 25.709  1.00 22.69 ? 174 LYS B O   1 
ATOM   5557 C CB  . LYS B 1 174 ? -16.024 25.984 23.025  1.00 18.52 ? 174 LYS B CB  1 
ATOM   5558 C CG  . LYS B 1 174 ? -16.275 25.525 21.619  1.00 23.52 ? 174 LYS B CG  1 
ATOM   5559 C CD  . LYS B 1 174 ? -15.145 24.639 21.113  1.00 38.27 ? 174 LYS B CD  1 
ATOM   5560 C CE  . LYS B 1 174 ? -14.049 25.470 20.469  1.00 47.11 ? 174 LYS B CE  1 
ATOM   5561 N NZ  . LYS B 1 174 ? -13.904 25.178 19.007  1.00 52.22 ? 174 LYS B NZ  1 
ATOM   5562 N N   . LYS B 1 175 ? -16.641 27.667 25.856  1.00 18.75 ? 175 LYS B N   1 
ATOM   5563 C CA  . LYS B 1 175 ? -16.568 27.683 27.316  1.00 18.48 ? 175 LYS B CA  1 
ATOM   5564 C C   . LYS B 1 175 ? -17.737 28.413 27.968  1.00 21.92 ? 175 LYS B C   1 
ATOM   5565 O O   . LYS B 1 175 ? -17.764 28.530 29.200  1.00 19.63 ? 175 LYS B O   1 
ATOM   5566 C CB  . LYS B 1 175 ? -15.257 28.349 27.777  1.00 20.66 ? 175 LYS B CB  1 
ATOM   5567 C CG  . LYS B 1 175 ? -14.044 27.446 27.788  1.00 30.86 ? 175 LYS B CG  1 
ATOM   5568 C CD  . LYS B 1 175 ? -12.763 28.193 27.391  1.00 46.62 ? 175 LYS B CD  1 
ATOM   5569 C CE  . LYS B 1 175 ? -12.406 29.324 28.352  1.00 50.86 ? 175 LYS B CE  1 
ATOM   5570 N NZ  . LYS B 1 175 ? -10.949 29.713 28.235  1.00 61.41 ? 175 LYS B NZ  1 
ATOM   5571 N N   . THR B 1 176 ? -18.692 28.917 27.187  1.00 17.38 ? 176 THR B N   1 
ATOM   5572 C CA  . THR B 1 176 ? -19.664 29.863 27.739  1.00 15.39 ? 176 THR B CA  1 
ATOM   5573 C C   . THR B 1 176 ? -20.671 29.169 28.653  1.00 19.62 ? 176 THR B C   1 
ATOM   5574 O O   . THR B 1 176 ? -20.885 29.600 29.792  1.00 17.58 ? 176 THR B O   1 
ATOM   5575 C CB  . THR B 1 176 ? -20.363 30.621 26.610  1.00 19.88 ? 176 THR B CB  1 
ATOM   5576 O OG1 . THR B 1 176 ? -19.433 31.548 26.031  1.00 17.94 ? 176 THR B OG1 1 
ATOM   5577 C CG2 . THR B 1 176 ? -21.548 31.412 27.140  1.00 18.08 ? 176 THR B CG2 1 
ATOM   5578 N N   . LEU B 1 177 ? -21.293 28.081 28.192  1.00 17.72 ? 177 LEU B N   1 
ATOM   5579 C CA  . LEU B 1 177 ? -22.289 27.455 29.063  1.00 20.54 ? 177 LEU B CA  1 
ATOM   5580 C C   . LEU B 1 177 ? -21.630 26.841 30.298  1.00 19.79 ? 177 LEU B C   1 
ATOM   5581 O O   . LEU B 1 177 ? -22.216 26.878 31.390  1.00 20.07 ? 177 LEU B O   1 
ATOM   5582 C CB  . LEU B 1 177 ? -23.106 26.414 28.278  1.00 20.53 ? 177 LEU B CB  1 
ATOM   5583 C CG  . LEU B 1 177 ? -24.030 27.059 27.229  1.00 18.49 ? 177 LEU B CG  1 
ATOM   5584 C CD1 . LEU B 1 177 ? -24.692 26.003 26.358  1.00 25.99 ? 177 LEU B CD1 1 
ATOM   5585 C CD2 . LEU B 1 177 ? -25.093 27.925 27.866  1.00 21.04 ? 177 LEU B CD2 1 
ATOM   5586 N N   . SER B 1 178 ? -20.400 26.335 30.157  1.00 18.16 ? 178 SER B N   1 
ATOM   5587 C CA  . SER B 1 178 ? -19.653 25.826 31.314  1.00 17.19 ? 178 SER B CA  1 
ATOM   5588 C C   . SER B 1 178 ? -19.481 26.884 32.390  1.00 16.59 ? 178 SER B C   1 
ATOM   5589 O O   . SER B 1 178 ? -19.488 26.566 33.590  1.00 17.06 ? 178 SER B O   1 
ATOM   5590 C CB  . SER B 1 178 ? -18.282 25.316 30.883  1.00 18.07 ? 178 SER B CB  1 
ATOM   5591 O OG  . SER B 1 178 ? -18.409 24.108 30.146  1.00 24.77 ? 178 SER B OG  1 
ATOM   5592 N N   . ILE B 1 179 ? -19.270 28.142 32.006  1.00 15.72 ? 179 ILE B N   1 
ATOM   5593 C CA  . ILE B 1 179 ? -18.987 29.095 33.079  1.00 19.67 ? 179 ILE B CA  1 
ATOM   5594 C C   . ILE B 1 179 ? -20.264 29.430 33.847  1.00 14.93 ? 179 ILE B C   1 
ATOM   5595 O O   . ILE B 1 179 ? -20.216 29.684 35.059  1.00 16.33 ? 179 ILE B O   1 
ATOM   5596 C CB  . ILE B 1 179 ? -18.259 30.354 32.561  1.00 20.79 ? 179 ILE B CB  1 
ATOM   5597 C CG1 . ILE B 1 179 ? -17.631 31.088 33.754  1.00 28.94 ? 179 ILE B CG1 1 
ATOM   5598 C CG2 . ILE B 1 179 ? -19.196 31.292 31.814  1.00 22.34 ? 179 ILE B CG2 1 
ATOM   5599 C CD1 . ILE B 1 179 ? -16.422 31.917 33.408  1.00 35.93 ? 179 ILE B CD1 1 
ATOM   5600 N N   . TYR B 1 180 ? -21.428 29.381 33.192  1.00 16.52 ? 180 TYR B N   1 
ATOM   5601 C CA  . TYR B 1 180 ? -22.679 29.543 33.925  1.00 20.07 ? 180 TYR B CA  1 
ATOM   5602 C C   . TYR B 1 180 ? -22.909 28.367 34.867  1.00 21.23 ? 180 TYR B C   1 
ATOM   5603 O O   . TYR B 1 180 ? -23.375 28.557 35.995  1.00 19.03 ? 180 TYR B O   1 
ATOM   5604 C CB  . TYR B 1 180 ? -23.860 29.692 32.964  1.00 14.72 ? 180 TYR B CB  1 
ATOM   5605 C CG  . TYR B 1 180 ? -23.893 31.047 32.288  1.00 15.58 ? 180 TYR B CG  1 
ATOM   5606 C CD1 . TYR B 1 180 ? -24.380 32.162 32.958  1.00 17.56 ? 180 TYR B CD1 1 
ATOM   5607 C CD2 . TYR B 1 180 ? -23.409 31.224 30.994  1.00 15.81 ? 180 TYR B CD2 1 
ATOM   5608 C CE1 . TYR B 1 180 ? -24.395 33.407 32.362  1.00 16.37 ? 180 TYR B CE1 1 
ATOM   5609 C CE2 . TYR B 1 180 ? -23.431 32.498 30.379  1.00 12.27 ? 180 TYR B CE2 1 
ATOM   5610 C CZ  . TYR B 1 180 ? -23.925 33.564 31.063  1.00 13.10 ? 180 TYR B CZ  1 
ATOM   5611 O OH  . TYR B 1 180 ? -23.942 34.829 30.500  1.00 15.15 ? 180 TYR B OH  1 
ATOM   5612 N N   . ARG B 1 181 ? -22.611 27.144 34.407  1.00 20.50 ? 181 ARG B N   1 
ATOM   5613 C CA  . ARG B 1 181 ? -22.680 25.980 35.290  1.00 20.07 ? 181 ARG B CA  1 
ATOM   5614 C C   . ARG B 1 181 ? -21.797 26.187 36.512  1.00 22.43 ? 181 ARG B C   1 
ATOM   5615 O O   . ARG B 1 181 ? -22.214 25.932 37.651  1.00 22.14 ? 181 ARG B O   1 
ATOM   5616 C CB  . ARG B 1 181 ? -22.244 24.716 34.548  1.00 22.82 ? 181 ARG B CB  1 
ATOM   5617 C CG  . ARG B 1 181 ? -23.287 24.068 33.617  1.00 27.62 ? 181 ARG B CG  1 
ATOM   5618 C CD  . ARG B 1 181 ? -22.831 22.673 33.119  1.00 24.58 ? 181 ARG B CD  1 
ATOM   5619 N NE  . ARG B 1 181 ? -23.602 22.273 31.927  1.00 27.52 ? 181 ARG B NE  1 
ATOM   5620 C CZ  . ARG B 1 181 ? -23.225 22.496 30.673  1.00 30.31 ? 181 ARG B CZ  1 
ATOM   5621 N NH1 . ARG B 1 181 ? -22.064 23.088 30.418  1.00 30.34 ? 181 ARG B NH1 1 
ATOM   5622 N NH2 . ARG B 1 181 ? -24.013 22.119 29.660  1.00 40.77 ? 181 ARG B NH2 1 
ATOM   5623 N N   . GLU B 1 182 ? -20.577 26.673 36.290  1.00 17.28 ? 182 GLU B N   1 
ATOM   5624 C CA  . GLU B 1 182 ? -19.616 26.810 37.377  1.00 18.94 ? 182 GLU B CA  1 
ATOM   5625 C C   . GLU B 1 182 ? -20.062 27.845 38.402  1.00 19.75 ? 182 GLU B C   1 
ATOM   5626 O O   . GLU B 1 182 ? -19.978 27.599 39.610  1.00 18.54 ? 182 GLU B O   1 
ATOM   5627 C CB  . GLU B 1 182 ? -18.241 27.172 36.813  1.00 26.88 ? 182 GLU B CB  1 
ATOM   5628 C CG  . GLU B 1 182 ? -17.518 25.974 36.230  1.00 43.48 ? 182 GLU B CG  1 
ATOM   5629 C CD  . GLU B 1 182 ? -16.665 26.331 35.030  1.00 55.28 ? 182 GLU B CD  1 
ATOM   5630 O OE1 . GLU B 1 182 ? -16.325 27.528 34.875  1.00 53.09 ? 182 GLU B OE1 1 
ATOM   5631 O OE2 . GLU B 1 182 ? -16.333 25.413 34.246  1.00 56.43 ? 182 GLU B OE2 1 
ATOM   5632 N N   . ILE B 1 183 ? -20.501 29.022 37.955  1.00 19.01 ? 183 ILE B N   1 
ATOM   5633 C CA  . ILE B 1 183 ? -20.812 30.033 38.964  1.00 19.13 ? 183 ILE B CA  1 
ATOM   5634 C C   . ILE B 1 183 ? -22.067 29.638 39.731  1.00 24.19 ? 183 ILE B C   1 
ATOM   5635 O O   . ILE B 1 183 ? -22.208 29.970 40.917  1.00 18.66 ? 183 ILE B O   1 
ATOM   5636 C CB  . ILE B 1 183 ? -20.923 31.449 38.359  1.00 18.77 ? 183 ILE B CB  1 
ATOM   5637 C CG1 . ILE B 1 183 ? -22.105 31.588 37.390  1.00 21.33 ? 183 ILE B CG1 1 
ATOM   5638 C CG2 . ILE B 1 183 ? -19.583 31.878 37.771  1.00 18.57 ? 183 ILE B CG2 1 
ATOM   5639 C CD1 . ILE B 1 183 ? -23.297 32.294 38.047  1.00 25.29 ? 183 ILE B CD1 1 
ATOM   5640 N N   . LYS B 1 184 ? -22.970 28.890 39.093  1.00 18.22 ? 184 LYS B N   1 
ATOM   5641 C CA  . LYS B 1 184 ? -24.125 28.349 39.803  1.00 23.94 ? 184 LYS B CA  1 
ATOM   5642 C C   . LYS B 1 184 ? -23.691 27.292 40.813  1.00 22.75 ? 184 LYS B C   1 
ATOM   5643 O O   . LYS B 1 184 ? -24.078 27.334 41.991  1.00 23.37 ? 184 LYS B O   1 
ATOM   5644 C CB  . LYS B 1 184 ? -25.119 27.766 38.789  1.00 20.02 ? 184 LYS B CB  1 
ATOM   5645 C CG  . LYS B 1 184 ? -26.395 27.192 39.405  1.00 26.71 ? 184 LYS B CG  1 
ATOM   5646 C CD  . LYS B 1 184 ? -27.269 26.518 38.360  1.00 22.49 ? 184 LYS B CD  1 
ATOM   5647 C CE  . LYS B 1 184 ? -28.472 25.850 39.007  1.00 28.47 ? 184 LYS B CE  1 
ATOM   5648 N NZ  . LYS B 1 184 ? -28.001 25.036 40.131  1.00 38.21 ? 184 LYS B NZ  1 
ATOM   5649 N N   . GLU B 1 185 ? -22.880 26.334 40.373  1.00 18.84 ? 185 GLU B N   1 
ATOM   5650 C CA  . GLU B 1 185 ? -22.458 25.276 41.287  1.00 23.74 ? 185 GLU B CA  1 
ATOM   5651 C C   . GLU B 1 185 ? -21.655 25.837 42.450  1.00 30.95 ? 185 GLU B C   1 
ATOM   5652 O O   . GLU B 1 185 ? -21.667 25.263 43.549  1.00 27.60 ? 185 GLU B O   1 
ATOM   5653 C CB  . GLU B 1 185 ? -21.648 24.213 40.540  1.00 25.92 ? 185 GLU B CB  1 
ATOM   5654 C CG  . GLU B 1 185 ? -22.518 23.317 39.655  1.00 39.63 ? 185 GLU B CG  1 
ATOM   5655 C CD  . GLU B 1 185 ? -23.526 22.490 40.454  1.00 55.59 ? 185 GLU B CD  1 
ATOM   5656 O OE1 . GLU B 1 185 ? -23.108 21.604 41.238  1.00 56.21 ? 185 GLU B OE1 1 
ATOM   5657 O OE2 . GLU B 1 185 ? -24.744 22.729 40.298  1.00 59.12 ? 185 GLU B OE2 1 
ATOM   5658 N N   . GLU B 1 186 ? -20.965 26.958 42.242  1.00 19.37 ? 186 GLU B N   1 
ATOM   5659 C CA  . GLU B 1 186 ? -20.157 27.557 43.295  1.00 22.79 ? 186 GLU B CA  1 
ATOM   5660 C C   . GLU B 1 186 ? -20.928 28.575 44.125  1.00 25.28 ? 186 GLU B C   1 
ATOM   5661 O O   . GLU B 1 186 ? -20.330 29.237 44.980  1.00 23.53 ? 186 GLU B O   1 
ATOM   5662 C CB  . GLU B 1 186 ? -18.916 28.210 42.692  1.00 23.42 ? 186 GLU B CB  1 
ATOM   5663 C CG  . GLU B 1 186 ? -17.954 27.192 42.128  1.00 31.03 ? 186 GLU B CG  1 
ATOM   5664 C CD  . GLU B 1 186 ? -17.062 27.760 41.040  1.00 36.71 ? 186 GLU B CD  1 
ATOM   5665 O OE1 . GLU B 1 186 ? -16.944 28.997 40.955  1.00 34.62 ? 186 GLU B OE1 1 
ATOM   5666 O OE2 . GLU B 1 186 ? -16.462 26.960 40.281  1.00 39.12 ? 186 GLU B OE2 1 
ATOM   5667 N N   . GLY B 1 187 ? -22.233 28.724 43.900  1.00 20.83 ? 187 GLY B N   1 
ATOM   5668 C CA  . GLY B 1 187 ? -22.974 29.678 44.715  1.00 19.91 ? 187 GLY B CA  1 
ATOM   5669 C C   . GLY B 1 187 ? -22.563 31.119 44.510  1.00 24.30 ? 187 GLY B C   1 
ATOM   5670 O O   . GLY B 1 187 ? -22.917 31.975 45.326  1.00 22.31 ? 187 GLY B O   1 
ATOM   5671 N N   . LYS B 1 188 ? -21.846 31.418 43.417  1.00 19.35 ? 188 LYS B N   1 
ATOM   5672 C CA  . LYS B 1 188 ? -21.507 32.795 43.083  1.00 16.92 ? 188 LYS B CA  1 
ATOM   5673 C C   . LYS B 1 188 ? -22.673 33.527 42.437  1.00 17.89 ? 188 LYS B C   1 
ATOM   5674 O O   . LYS B 1 188 ? -22.681 34.764 42.424  1.00 17.93 ? 188 LYS B O   1 
ATOM   5675 C CB  . LYS B 1 188 ? -20.275 32.842 42.154  1.00 16.52 ? 188 LYS B CB  1 
ATOM   5676 C CG  . LYS B 1 188 ? -18.972 32.353 42.832  1.00 25.88 ? 188 LYS B CG  1 
ATOM   5677 C CD  . LYS B 1 188 ? -17.764 32.423 41.876  1.00 30.49 ? 188 LYS B CD  1 
ATOM   5678 C CE  . LYS B 1 188 ? -16.516 31.827 42.520  1.00 36.60 ? 188 LYS B CE  1 
ATOM   5679 N NZ  . LYS B 1 188 ? -16.060 32.584 43.727  1.00 45.90 ? 188 LYS B NZ  1 
ATOM   5680 N N   . GLY B 1 189 ? -23.641 32.796 41.889  1.00 15.81 ? 189 GLY B N   1 
ATOM   5681 C CA  . GLY B 1 189 ? -24.836 33.415 41.350  1.00 16.39 ? 189 GLY B CA  1 
ATOM   5682 C C   . GLY B 1 189 ? -25.911 32.371 41.176  1.00 18.97 ? 189 GLY B C   1 
ATOM   5683 O O   . GLY B 1 189 ? -25.627 31.168 41.129  1.00 21.19 ? 189 GLY B O   1 
ATOM   5684 N N   . SER B 1 190 ? -27.161 32.838 41.102  1.00 17.67 ? 190 SER B N   1 
ATOM   5685 C CA  . SER B 1 190 ? -28.238 31.968 40.646  1.00 15.25 ? 190 SER B CA  1 
ATOM   5686 C C   . SER B 1 190 ? -28.422 32.155 39.149  1.00 16.72 ? 190 SER B C   1 
ATOM   5687 O O   . SER B 1 190 ? -28.110 33.212 38.607  1.00 13.83 ? 190 SER B O   1 
ATOM   5688 C CB  . SER B 1 190 ? -29.547 32.257 41.383  1.00 18.44 ? 190 SER B CB  1 
ATOM   5689 O OG  . SER B 1 190 ? -29.417 31.986 42.771  1.00 18.23 ? 190 SER B OG  1 
ATOM   5690 N N   . VAL B 1 191 ? -28.927 31.123 38.477  1.00 15.44 ? 191 VAL B N   1 
ATOM   5691 C CA  . VAL B 1 191 ? -29.263 31.230 37.057  1.00 15.21 ? 191 VAL B CA  1 
ATOM   5692 C C   . VAL B 1 191 ? -30.746 30.914 36.882  1.00 17.40 ? 191 VAL B C   1 
ATOM   5693 O O   . VAL B 1 191 ? -31.238 29.893 37.380  1.00 17.62 ? 191 VAL B O   1 
ATOM   5694 C CB  . VAL B 1 191 ? -28.403 30.311 36.171  1.00 15.39 ? 191 VAL B CB  1 
ATOM   5695 C CG1 . VAL B 1 191 ? -28.725 30.583 34.684  1.00 17.02 ? 191 VAL B CG1 1 
ATOM   5696 C CG2 . VAL B 1 191 ? -26.928 30.566 36.423  1.00 18.34 ? 191 VAL B CG2 1 
ATOM   5697 N N   . SER B 1 192 ? -31.458 31.801 36.198  1.00 14.34 ? 192 SER B N   1 
ATOM   5698 C CA  . SER B 1 192 ? -32.873 31.648 35.922  1.00 17.27 ? 192 SER B CA  1 
ATOM   5699 C C   . SER B 1 192 ? -33.054 31.377 34.438  1.00 14.56 ? 192 SER B C   1 
ATOM   5700 O O   . SER B 1 192 ? -32.097 31.430 33.665  1.00 15.98 ? 192 SER B O   1 
ATOM   5701 C CB  . SER B 1 192 ? -33.635 32.913 36.330  1.00 19.63 ? 192 SER B CB  1 
ATOM   5702 O OG  . SER B 1 192 ? -33.208 34.001 35.515  1.00 17.66 ? 192 SER B OG  1 
ATOM   5703 N N   . THR B 1 193 ? -34.298 31.124 34.031  1.00 14.17 ? 193 THR B N   1 
ATOM   5704 C CA  . THR B 1 193 ? -34.596 31.128 32.596  1.00 14.16 ? 193 THR B CA  1 
ATOM   5705 C C   . THR B 1 193 ? -35.940 31.810 32.378  1.00 18.92 ? 193 THR B C   1 
ATOM   5706 O O   . THR B 1 193 ? -36.562 32.331 33.308  1.00 17.42 ? 193 THR B O   1 
ATOM   5707 C CB  . THR B 1 193 ? -34.516 29.723 31.985  1.00 14.79 ? 193 THR B CB  1 
ATOM   5708 O OG1 . THR B 1 193 ? -34.559 29.822 30.553  1.00 17.45 ? 193 THR B OG1 1 
ATOM   5709 C CG2 . THR B 1 193 ? -35.631 28.791 32.467  1.00 17.93 ? 193 THR B CG2 1 
ATOM   5710 N N   . SER B 1 194 ? -36.336 31.884 31.118  1.00 16.62 ? 194 SER B N   1 
ATOM   5711 C CA  . SER B 1 194 ? -37.581 32.485 30.684  1.00 14.93 ? 194 SER B CA  1 
ATOM   5712 C C   . SER B 1 194 ? -38.381 31.456 29.899  1.00 15.83 ? 194 SER B C   1 
ATOM   5713 O O   . SER B 1 194 ? -37.809 30.497 29.365  1.00 15.99 ? 194 SER B O   1 
ATOM   5714 C CB  . SER B 1 194 ? -37.311 33.705 29.787  1.00 15.60 ? 194 SER B CB  1 
ATOM   5715 O OG  . SER B 1 194 ? -36.736 34.761 30.544  1.00 16.71 ? 194 SER B OG  1 
ATOM   5716 N N   . PRO B 1 195 ? -39.703 31.652 29.760  1.00 17.56 ? 195 PRO B N   1 
ATOM   5717 C CA  . PRO B 1 195 ? -40.452 30.856 28.778  1.00 17.84 ? 195 PRO B CA  1 
ATOM   5718 C C   . PRO B 1 195 ? -39.692 30.842 27.459  1.00 17.36 ? 195 PRO B C   1 
ATOM   5719 O O   . PRO B 1 195 ? -39.055 31.830 27.086  1.00 16.72 ? 195 PRO B O   1 
ATOM   5720 C CB  . PRO B 1 195 ? -41.791 31.595 28.662  1.00 19.58 ? 195 PRO B CB  1 
ATOM   5721 C CG  . PRO B 1 195 ? -41.891 32.423 29.876  1.00 34.09 ? 195 PRO B CG  1 
ATOM   5722 C CD  . PRO B 1 195 ? -40.490 32.830 30.178  1.00 27.12 ? 195 PRO B CD  1 
ATOM   5723 N N   . TYR B 1 196 ? -39.779 29.705 26.755  1.00 17.37 ? 196 TYR B N   1 
ATOM   5724 C CA  . TYR B 1 196 ? -38.721 29.265 25.835  1.00 17.92 ? 196 TYR B CA  1 
ATOM   5725 C C   . TYR B 1 196 ? -38.283 30.324 24.819  1.00 21.12 ? 196 TYR B C   1 
ATOM   5726 O O   . TYR B 1 196 ? -37.078 30.577 24.662  1.00 15.76 ? 196 TYR B O   1 
ATOM   5727 C CB  . TYR B 1 196 ? -39.160 27.994 25.095  1.00 15.41 ? 196 TYR B CB  1 
ATOM   5728 C CG  . TYR B 1 196 ? -37.987 27.162 24.613  1.00 16.53 ? 196 TYR B CG  1 
ATOM   5729 C CD1 . TYR B 1 196 ? -37.227 27.560 23.515  1.00 14.91 ? 196 TYR B CD1 1 
ATOM   5730 C CD2 . TYR B 1 196 ? -37.629 25.989 25.263  1.00 17.20 ? 196 TYR B CD2 1 
ATOM   5731 C CE1 . TYR B 1 196 ? -36.140 26.803 23.057  1.00 17.54 ? 196 TYR B CE1 1 
ATOM   5732 C CE2 . TYR B 1 196 ? -36.540 25.218 24.815  1.00 15.43 ? 196 TYR B CE2 1 
ATOM   5733 C CZ  . TYR B 1 196 ? -35.809 25.629 23.722  1.00 15.29 ? 196 TYR B CZ  1 
ATOM   5734 O OH  . TYR B 1 196 ? -34.750 24.861 23.296  1.00 20.52 ? 196 TYR B OH  1 
ATOM   5735 N N   . TYR B 1 197 ? -39.225 30.897 24.062  1.00 15.52 ? 197 TYR B N   1 
ATOM   5736 C CA  . TYR B 1 197 ? -38.879 31.834 22.989  1.00 12.94 ? 197 TYR B CA  1 
ATOM   5737 C C   . TYR B 1 197 ? -39.098 33.286 23.390  1.00 13.14 ? 197 TYR B C   1 
ATOM   5738 O O   . TYR B 1 197 ? -39.243 34.156 22.517  1.00 14.30 ? 197 TYR B O   1 
ATOM   5739 C CB  . TYR B 1 197 ? -39.649 31.494 21.694  1.00 14.34 ? 197 TYR B CB  1 
ATOM   5740 C CG  . TYR B 1 197 ? -39.156 30.179 21.154  1.00 15.22 ? 197 TYR B CG  1 
ATOM   5741 C CD1 . TYR B 1 197 ? -37.898 30.096 20.577  1.00 14.82 ? 197 TYR B CD1 1 
ATOM   5742 C CD2 . TYR B 1 197 ? -39.896 29.009 21.321  1.00 14.53 ? 197 TYR B CD2 1 
ATOM   5743 C CE1 . TYR B 1 197 ? -37.390 28.885 20.134  1.00 17.34 ? 197 TYR B CE1 1 
ATOM   5744 C CE2 . TYR B 1 197 ? -39.402 27.787 20.881  1.00 20.50 ? 197 TYR B CE2 1 
ATOM   5745 C CZ  . TYR B 1 197 ? -38.151 27.730 20.290  1.00 18.88 ? 197 TYR B CZ  1 
ATOM   5746 O OH  . TYR B 1 197 ? -37.637 26.542 19.845  1.00 23.07 ? 197 TYR B OH  1 
ATOM   5747 N N   . HIS B 1 198 ? -39.122 33.565 24.688  1.00 14.55 ? 198 HIS B N   1 
ATOM   5748 C CA  . HIS B 1 198 ? -39.260 34.925 25.204  1.00 14.97 ? 198 HIS B CA  1 
ATOM   5749 C C   . HIS B 1 198 ? -40.564 35.579 24.728  1.00 20.83 ? 198 HIS B C   1 
ATOM   5750 O O   . HIS B 1 198 ? -40.532 36.707 24.217  1.00 18.67 ? 198 HIS B O   1 
ATOM   5751 C CB  . HIS B 1 198 ? -38.023 35.746 24.773  1.00 13.10 ? 198 HIS B CB  1 
ATOM   5752 C CG  . HIS B 1 198 ? -37.817 37.034 25.515  1.00 14.22 ? 198 HIS B CG  1 
ATOM   5753 N ND1 . HIS B 1 198 ? -38.293 38.242 25.054  1.00 18.51 ? 198 HIS B ND1 1 
ATOM   5754 C CD2 . HIS B 1 198 ? -37.120 37.314 26.647  1.00 16.09 ? 198 HIS B CD2 1 
ATOM   5755 C CE1 . HIS B 1 198 ? -37.929 39.206 25.884  1.00 17.49 ? 198 HIS B CE1 1 
ATOM   5756 N NE2 . HIS B 1 198 ? -37.201 38.672 26.848  1.00 16.13 ? 198 HIS B NE2 1 
ATOM   5757 N N   . PRO B 1 199 ? -41.718 34.924 24.877  1.00 17.71 ? 199 PRO B N   1 
ATOM   5758 C CA  . PRO B 1 199 ? -42.988 35.530 24.475  1.00 14.92 ? 199 PRO B CA  1 
ATOM   5759 C C   . PRO B 1 199 ? -43.569 36.424 25.568  1.00 25.40 ? 199 PRO B C   1 
ATOM   5760 O O   . PRO B 1 199 ? -43.124 36.416 26.718  1.00 24.08 ? 199 PRO B O   1 
ATOM   5761 C CB  . PRO B 1 199 ? -43.882 34.301 24.283  1.00 20.83 ? 199 PRO B CB  1 
ATOM   5762 C CG  . PRO B 1 199 ? -43.419 33.373 25.434  1.00 15.96 ? 199 PRO B CG  1 
ATOM   5763 C CD  . PRO B 1 199 ? -41.935 33.621 25.561  1.00 18.80 ? 199 PRO B CD  1 
ATOM   5764 N N   . LEU B 1 200 ? -44.649 37.131 25.206  1.00 23.99 ? 200 LEU B N   1 
ATOM   5765 C CA  . LEU B 1 200 ? -45.449 37.887 26.175  1.00 23.75 ? 200 LEU B CA  1 
ATOM   5766 C C   . LEU B 1 200 ? -46.529 36.962 26.726  1.00 24.43 ? 200 LEU B C   1 
ATOM   5767 O O   . LEU B 1 200 ? -47.654 36.890 26.219  1.00 21.60 ? 200 LEU B O   1 
ATOM   5768 C CB  . LEU B 1 200 ? -46.054 39.129 25.534  1.00 26.72 ? 200 LEU B CB  1 
ATOM   5769 C CG  . LEU B 1 200 ? -45.073 40.220 25.106  1.00 21.18 ? 200 LEU B CG  1 
ATOM   5770 C CD1 . LEU B 1 200 ? -45.836 41.361 24.455  1.00 24.53 ? 200 LEU B CD1 1 
ATOM   5771 C CD2 . LEU B 1 200 ? -44.260 40.755 26.267  1.00 25.33 ? 200 LEU B CD2 1 
ATOM   5772 N N   . ILE B 1 201 ? -46.191 36.253 27.797  1.00 19.03 ? 201 ILE B N   1 
ATOM   5773 C CA  . ILE B 1 201 ? -47.101 35.265 28.385  1.00 21.77 ? 201 ILE B CA  1 
ATOM   5774 C C   . ILE B 1 201 ? -48.477 35.850 28.730  1.00 21.00 ? 201 ILE B C   1 
ATOM   5775 O O   . ILE B 1 201 ? -49.489 35.218 28.386  1.00 20.43 ? 201 ILE B O   1 
ATOM   5776 C CB  . ILE B 1 201 ? -46.447 34.601 29.607  1.00 17.81 ? 201 ILE B CB  1 
ATOM   5777 C CG1 . ILE B 1 201 ? -45.295 33.688 29.158  1.00 20.01 ? 201 ILE B CG1 1 
ATOM   5778 C CG2 . ILE B 1 201 ? -47.492 33.797 30.390  1.00 18.36 ? 201 ILE B CG2 1 
ATOM   5779 C CD1 . ILE B 1 201 ? -45.733 32.438 28.429  1.00 19.65 ? 201 ILE B CD1 1 
ATOM   5780 N N   . PRO B 1 202 ? -48.598 37.057 29.336  1.00 20.79 ? 202 PRO B N   1 
ATOM   5781 C CA  . PRO B 1 202 ? -49.951 37.583 29.657  1.00 16.21 ? 202 PRO B CA  1 
ATOM   5782 C C   . PRO B 1 202 ? -50.912 37.667 28.475  1.00 20.32 ? 202 PRO B C   1 
ATOM   5783 O O   . PRO B 1 202 ? -52.101 37.380 28.647  1.00 20.79 ? 202 PRO B O   1 
ATOM   5784 C CB  . PRO B 1 202 ? -49.655 38.970 30.230  1.00 20.38 ? 202 PRO B CB  1 
ATOM   5785 C CG  . PRO B 1 202 ? -48.315 38.834 30.857  1.00 17.39 ? 202 PRO B CG  1 
ATOM   5786 C CD  . PRO B 1 202 ? -47.536 37.907 29.922  1.00 21.57 ? 202 PRO B CD  1 
ATOM   5787 N N   . ILE B 1 203 ? -50.428 38.060 27.289  1.00 18.68 ? 203 ILE B N   1 
ATOM   5788 C CA  . ILE B 1 203 ? -51.275 38.148 26.107  1.00 18.41 ? 203 ILE B CA  1 
ATOM   5789 C C   . ILE B 1 203 ? -51.679 36.760 25.628  1.00 17.95 ? 203 ILE B C   1 
ATOM   5790 O O   . ILE B 1 203 ? -52.841 36.528 25.276  1.00 22.67 ? 203 ILE B O   1 
ATOM   5791 C CB  . ILE B 1 203 ? -50.558 38.946 25.001  1.00 23.10 ? 203 ILE B CB  1 
ATOM   5792 C CG1 . ILE B 1 203 ? -50.408 40.410 25.428  1.00 23.70 ? 203 ILE B CG1 1 
ATOM   5793 C CG2 . ILE B 1 203 ? -51.316 38.815 23.672  1.00 20.89 ? 203 ILE B CG2 1 
ATOM   5794 C CD1 . ILE B 1 203 ? -49.572 41.282 24.489  1.00 24.22 ? 203 ILE B CD1 1 
ATOM   5795 N N   . LEU B 1 204 ? -50.737 35.817 25.611  1.00 18.98 ? 204 LEU B N   1 
ATOM   5796 C CA  . LEU B 1 204 ? -51.065 34.452 25.199  1.00 17.45 ? 204 LEU B CA  1 
ATOM   5797 C C   . LEU B 1 204 ? -52.153 33.850 26.084  1.00 25.41 ? 204 LEU B C   1 
ATOM   5798 O O   . LEU B 1 204 ? -53.049 33.133 25.596  1.00 20.35 ? 204 LEU B O   1 
ATOM   5799 C CB  . LEU B 1 204 ? -49.799 33.589 25.244  1.00 17.46 ? 204 LEU B CB  1 
ATOM   5800 C CG  . LEU B 1 204 ? -48.661 33.934 24.300  1.00 20.52 ? 204 LEU B CG  1 
ATOM   5801 C CD1 . LEU B 1 204 ? -47.619 32.828 24.350  1.00 20.55 ? 204 LEU B CD1 1 
ATOM   5802 C CD2 . LEU B 1 204 ? -49.167 34.117 22.865  1.00 19.71 ? 204 LEU B CD2 1 
ATOM   5803 N N   . LEU B 1 205 ? -52.100 34.139 27.390  1.00 23.07 ? 205 LEU B N   1 
ATOM   5804 C CA  . LEU B 1 205 ? -53.121 33.621 28.296  1.00 23.43 ? 205 LEU B CA  1 
ATOM   5805 C C   . LEU B 1 205 ? -54.441 34.360 28.123  1.00 24.17 ? 205 LEU B C   1 
ATOM   5806 O O   . LEU B 1 205 ? -55.512 33.748 28.178  1.00 22.31 ? 205 LEU B O   1 
ATOM   5807 C CB  . LEU B 1 205 ? -52.649 33.729 29.749  1.00 19.46 ? 205 LEU B CB  1 
ATOM   5808 C CG  . LEU B 1 205 ? -51.609 32.698 30.170  1.00 22.24 ? 205 LEU B CG  1 
ATOM   5809 C CD1 . LEU B 1 205 ? -50.980 33.145 31.498  1.00 22.16 ? 205 LEU B CD1 1 
ATOM   5810 C CD2 . LEU B 1 205 ? -52.236 31.297 30.273  1.00 20.34 ? 205 LEU B CD2 1 
ATOM   5811 N N   . ASN B 1 206 ? -54.383 35.664 27.901  1.00 24.46 ? 206 ASN B N   1 
ATOM   5812 C CA  . ASN B 1 206 ? -55.590 36.478 27.896  1.00 22.40 ? 206 ASN B CA  1 
ATOM   5813 C C   . ASN B 1 206 ? -55.294 37.818 27.236  1.00 23.51 ? 206 ASN B C   1 
ATOM   5814 O O   . ASN B 1 206 ? -54.808 38.750 27.890  1.00 21.77 ? 206 ASN B O   1 
ATOM   5815 C CB  . ASN B 1 206 ? -56.106 36.684 29.319  1.00 23.24 ? 206 ASN B CB  1 
ATOM   5816 C CG  . ASN B 1 206 ? -57.283 37.633 29.381  1.00 33.11 ? 206 ASN B CG  1 
ATOM   5817 O OD1 . ASN B 1 206 ? -58.030 37.786 28.412  1.00 30.57 ? 206 ASN B OD1 1 
ATOM   5818 N ND2 . ASN B 1 206 ? -57.449 38.288 30.527  1.00 35.16 ? 206 ASN B ND2 1 
ATOM   5819 N N   . PRO B 1 207 ? -55.563 37.951 25.938  1.00 28.31 ? 207 PRO B N   1 
ATOM   5820 C CA  . PRO B 1 207 ? -55.254 39.221 25.259  1.00 29.37 ? 207 PRO B CA  1 
ATOM   5821 C C   . PRO B 1 207 ? -56.023 40.413 25.810  1.00 22.64 ? 207 PRO B C   1 
ATOM   5822 O O   . PRO B 1 207 ? -55.549 41.548 25.667  1.00 27.37 ? 207 PRO B O   1 
ATOM   5823 C CB  . PRO B 1 207 ? -55.617 38.935 23.795  1.00 29.71 ? 207 PRO B CB  1 
ATOM   5824 C CG  . PRO B 1 207 ? -55.446 37.452 23.669  1.00 29.24 ? 207 PRO B CG  1 
ATOM   5825 C CD  . PRO B 1 207 ? -55.935 36.891 24.988  1.00 30.33 ? 207 PRO B CD  1 
ATOM   5826 N N   . ASN B 1 208 ? -57.169 40.190 26.456  1.00 24.50 ? 208 ASN B N   1 
ATOM   5827 C CA  . ASN B 1 208 ? -57.949 41.279 27.038  1.00 26.94 ? 208 ASN B CA  1 
ATOM   5828 C C   . ASN B 1 208 ? -57.201 41.990 28.167  1.00 22.32 ? 208 ASN B C   1 
ATOM   5829 O O   . ASN B 1 208 ? -57.631 43.072 28.578  1.00 27.58 ? 208 ASN B O   1 
ATOM   5830 C CB  . ASN B 1 208 ? -59.294 40.752 27.559  1.00 29.15 ? 208 ASN B CB  1 
ATOM   5831 C CG  . ASN B 1 208 ? -60.421 40.823 26.517  1.00 44.57 ? 208 ASN B CG  1 
ATOM   5832 O OD1 . ASN B 1 208 ? -60.192 40.719 25.308  1.00 38.64 ? 208 ASN B OD1 1 
ATOM   5833 N ND2 . ASN B 1 208 ? -61.656 40.988 27.001  1.00 49.46 ? 208 ASN B ND2 1 
ATOM   5834 N N   . CYS B 1 209 ? -56.105 41.414 28.675  1.00 24.88 ? 209 CYS B N   1 
ATOM   5835 C CA  . CYS B 1 209 ? -55.332 42.090 29.720  1.00 28.52 ? 209 CYS B CA  1 
ATOM   5836 C C   . CYS B 1 209 ? -54.706 43.398 29.241  1.00 24.45 ? 209 CYS B C   1 
ATOM   5837 O O   . CYS B 1 209 ? -54.372 44.240 30.080  1.00 27.04 ? 209 CYS B O   1 
ATOM   5838 C CB  . CYS B 1 209 ? -54.245 41.169 30.290  1.00 21.82 ? 209 CYS B CB  1 
ATOM   5839 S SG  . CYS B 1 209 ? -52.807 40.854 29.233  1.00 26.95 ? 209 CYS B SG  1 
ATOM   5840 N N   . VAL B 1 210 ? -54.576 43.607 27.922  1.00 23.74 ? 210 VAL B N   1 
ATOM   5841 C CA  . VAL B 1 210 ? -54.040 44.867 27.404  1.00 20.69 ? 210 VAL B CA  1 
ATOM   5842 C C   . VAL B 1 210 ? -54.938 46.045 27.776  1.00 25.52 ? 210 VAL B C   1 
ATOM   5843 O O   . VAL B 1 210 ? -54.471 47.189 27.859  1.00 27.34 ? 210 VAL B O   1 
ATOM   5844 C CB  . VAL B 1 210 ? -53.837 44.779 25.872  1.00 22.48 ? 210 VAL B CB  1 
ATOM   5845 C CG1 . VAL B 1 210 ? -52.923 43.617 25.530  1.00 26.00 ? 210 VAL B CG1 1 
ATOM   5846 C CG2 . VAL B 1 210 ? -55.165 44.649 25.148  1.00 32.12 ? 210 VAL B CG2 1 
ATOM   5847 N N   . TYR B 1 211 ? -56.234 45.797 27.985  1.00 23.22 ? 211 TYR B N   1 
ATOM   5848 C CA  . TYR B 1 211 ? -57.154 46.867 28.352  1.00 27.45 ? 211 TYR B CA  1 
ATOM   5849 C C   . TYR B 1 211 ? -56.945 47.355 29.777  1.00 24.70 ? 211 TYR B C   1 
ATOM   5850 O O   . TYR B 1 211 ? -57.466 48.421 30.125  1.00 26.41 ? 211 TYR B O   1 
ATOM   5851 C CB  . TYR B 1 211 ? -58.604 46.404 28.176  1.00 31.33 ? 211 TYR B CB  1 
ATOM   5852 C CG  . TYR B 1 211 ? -58.960 45.983 26.761  1.00 33.86 ? 211 TYR B CG  1 
ATOM   5853 C CD1 . TYR B 1 211 ? -58.710 46.820 25.684  1.00 35.37 ? 211 TYR B CD1 1 
ATOM   5854 C CD2 . TYR B 1 211 ? -59.530 44.743 26.507  1.00 32.57 ? 211 TYR B CD2 1 
ATOM   5855 C CE1 . TYR B 1 211 ? -59.023 46.434 24.385  1.00 35.28 ? 211 TYR B CE1 1 
ATOM   5856 C CE2 . TYR B 1 211 ? -59.848 44.344 25.201  1.00 38.25 ? 211 TYR B CE2 1 
ATOM   5857 C CZ  . TYR B 1 211 ? -59.599 45.201 24.153  1.00 32.91 ? 211 TYR B CZ  1 
ATOM   5858 O OH  . TYR B 1 211 ? -59.911 44.827 22.860  1.00 35.47 ? 211 TYR B OH  1 
ATOM   5859 N N   . GLU B 1 212 ? -56.193 46.620 30.603  1.00 24.30 ? 212 GLU B N   1 
ATOM   5860 C CA  . GLU B 1 212 ? -56.026 47.034 31.993  1.00 24.06 ? 212 GLU B CA  1 
ATOM   5861 C C   . GLU B 1 212 ? -55.250 48.346 32.114  1.00 29.72 ? 212 GLU B C   1 
ATOM   5862 O O   . GLU B 1 212 ? -55.542 49.147 33.009  1.00 31.00 ? 212 GLU B O   1 
ATOM   5863 C CB  . GLU B 1 212 ? -55.362 45.907 32.792  1.00 25.64 ? 212 GLU B CB  1 
ATOM   5864 C CG  . GLU B 1 212 ? -56.350 44.785 33.118  1.00 30.13 ? 212 GLU B CG  1 
ATOM   5865 C CD  . GLU B 1 212 ? -55.691 43.513 33.607  1.00 33.50 ? 212 GLU B CD  1 
ATOM   5866 O OE1 . GLU B 1 212 ? -56.222 42.419 33.323  1.00 37.20 ? 212 GLU B OE1 1 
ATOM   5867 O OE2 . GLU B 1 212 ? -54.652 43.597 34.284  1.00 28.67 ? 212 GLU B OE2 1 
ATOM   5868 N N   . THR B 1 213 ? -54.279 48.594 31.222  1.00 29.28 ? 213 THR B N   1 
ATOM   5869 C CA  . THR B 1 213 ? -53.485 49.817 31.242  1.00 33.67 ? 213 THR B CA  1 
ATOM   5870 C C   . THR B 1 213 ? -53.718 50.742 30.056  1.00 39.33 ? 213 THR B C   1 
ATOM   5871 O O   . THR B 1 213 ? -53.430 51.937 30.172  1.00 42.13 ? 213 THR B O   1 
ATOM   5872 C CB  . THR B 1 213 ? -51.986 49.491 31.292  1.00 33.19 ? 213 THR B CB  1 
ATOM   5873 O OG1 . THR B 1 213 ? -51.650 48.668 30.169  1.00 38.61 ? 213 THR B OG1 1 
ATOM   5874 C CG2 . THR B 1 213 ? -51.641 48.770 32.580  1.00 31.74 ? 213 THR B CG2 1 
ATOM   5875 N N   . THR B 1 214 ? -54.181 50.227 28.915  1.00 35.13 ? 214 THR B N   1 
ATOM   5876 C CA  . THR B 1 214 ? -54.490 51.039 27.739  1.00 29.30 ? 214 THR B CA  1 
ATOM   5877 C C   . THR B 1 214 ? -55.886 50.634 27.279  1.00 35.86 ? 214 THR B C   1 
ATOM   5878 O O   . THR B 1 214 ? -56.038 49.834 26.348  1.00 29.51 ? 214 THR B O   1 
ATOM   5879 C CB  . THR B 1 214 ? -53.446 50.855 26.631  1.00 27.56 ? 214 THR B CB  1 
ATOM   5880 O OG1 . THR B 1 214 ? -53.445 49.493 26.190  1.00 29.08 ? 214 THR B OG1 1 
ATOM   5881 C CG2 . THR B 1 214 ? -52.042 51.211 27.151  1.00 22.82 ? 214 THR B CG2 1 
ATOM   5882 N N   . PRO B 1 215 ? -56.935 51.169 27.919  1.00 38.27 ? 215 PRO B N   1 
ATOM   5883 C CA  . PRO B 1 215 ? -58.303 50.716 27.603  1.00 38.59 ? 215 PRO B CA  1 
ATOM   5884 C C   . PRO B 1 215 ? -58.800 51.112 26.229  1.00 36.16 ? 215 PRO B C   1 
ATOM   5885 O O   . PRO B 1 215 ? -59.778 50.516 25.766  1.00 41.28 ? 215 PRO B O   1 
ATOM   5886 C CB  . PRO B 1 215 ? -59.157 51.377 28.695  1.00 40.91 ? 215 PRO B CB  1 
ATOM   5887 C CG  . PRO B 1 215 ? -58.343 52.550 29.148  1.00 40.93 ? 215 PRO B CG  1 
ATOM   5888 C CD  . PRO B 1 215 ? -56.916 52.120 29.043  1.00 40.90 ? 215 PRO B CD  1 
ATOM   5889 N N   . ASN B 1 216 ? -58.191 52.095 25.565  1.00 34.04 ? 216 ASN B N   1 
ATOM   5890 C CA  . ASN B 1 216 ? -58.652 52.537 24.253  1.00 37.53 ? 216 ASN B CA  1 
ATOM   5891 C C   . ASN B 1 216 ? -57.876 51.901 23.106  1.00 35.04 ? 216 ASN B C   1 
ATOM   5892 O O   . ASN B 1 216 ? -58.048 52.307 21.958  1.00 38.72 ? 216 ASN B O   1 
ATOM   5893 C CB  . ASN B 1 216 ? -58.581 54.062 24.155  1.00 44.04 ? 216 ASN B CB  1 
ATOM   5894 C CG  . ASN B 1 216 ? -59.370 54.743 25.249  1.00 54.17 ? 216 ASN B CG  1 
ATOM   5895 O OD1 . ASN B 1 216 ? -60.388 54.224 25.703  1.00 49.89 ? 216 ASN B OD1 1 
ATOM   5896 N ND2 . ASN B 1 216 ? -58.904 55.909 25.685  1.00 62.00 ? 216 ASN B ND2 1 
ATOM   5897 N N   . VAL B 1 217 ? -57.024 50.918 23.394  1.00 36.24 ? 217 VAL B N   1 
ATOM   5898 C CA  . VAL B 1 217 ? -56.243 50.266 22.353  1.00 35.52 ? 217 VAL B CA  1 
ATOM   5899 C C   . VAL B 1 217 ? -57.168 49.448 21.460  1.00 36.71 ? 217 VAL B C   1 
ATOM   5900 O O   . VAL B 1 217 ? -58.231 48.977 21.887  1.00 40.09 ? 217 VAL B O   1 
ATOM   5901 C CB  . VAL B 1 217 ? -55.143 49.387 22.982  1.00 34.34 ? 217 VAL B CB  1 
ATOM   5902 C CG1 . VAL B 1 217 ? -55.746 48.207 23.728  1.00 39.16 ? 217 VAL B CG1 1 
ATOM   5903 C CG2 . VAL B 1 217 ? -54.167 48.890 21.929  1.00 33.66 ? 217 VAL B CG2 1 
ATOM   5904 N N   . LYS B 1 218 ? -56.787 49.316 20.193  1.00 31.06 ? 218 LYS B N   1 
ATOM   5905 C CA  . LYS B 1 218 ? -57.449 48.406 19.272  1.00 32.89 ? 218 LYS B CA  1 
ATOM   5906 C C   . LYS B 1 218 ? -56.521 47.229 19.025  1.00 36.60 ? 218 LYS B C   1 
ATOM   5907 O O   . LYS B 1 218 ? -55.345 47.422 18.702  1.00 40.00 ? 218 LYS B O   1 
ATOM   5908 C CB  . LYS B 1 218 ? -57.800 49.095 17.951  1.00 35.37 ? 218 LYS B CB  1 
ATOM   5909 C CG  . LYS B 1 218 ? -59.136 49.812 17.960  1.00 44.10 ? 218 LYS B CG  1 
ATOM   5910 C CD  . LYS B 1 218 ? -59.770 49.766 16.585  1.00 49.69 ? 218 LYS B CD  1 
ATOM   5911 C CE  . LYS B 1 218 ? -60.579 51.018 16.335  1.00 56.69 ? 218 LYS B CE  1 
ATOM   5912 N NZ  . LYS B 1 218 ? -60.887 51.690 17.629  1.00 57.77 ? 218 LYS B NZ  1 
ATOM   5913 N N   . ILE B 1 219 ? -57.039 46.019 19.196  1.00 41.84 ? 219 ILE B N   1 
ATOM   5914 C CA  . ILE B 1 219 ? -56.216 44.825 19.023  1.00 39.97 ? 219 ILE B CA  1 
ATOM   5915 C C   . ILE B 1 219 ? -56.945 43.862 18.098  1.00 33.66 ? 219 ILE B C   1 
ATOM   5916 O O   . ILE B 1 219 ? -58.163 43.979 17.885  1.00 37.13 ? 219 ILE B O   1 
ATOM   5917 C CB  . ILE B 1 219 ? -55.890 44.156 20.378  1.00 39.59 ? 219 ILE B CB  1 
ATOM   5918 C CG1 . ILE B 1 219 ? -57.172 43.788 21.111  1.00 32.61 ? 219 ILE B CG1 1 
ATOM   5919 C CG2 . ILE B 1 219 ? -54.992 45.052 21.224  1.00 40.90 ? 219 ILE B CG2 1 
ATOM   5920 C CD1 . ILE B 1 219 ? -56.932 42.871 22.275  1.00 32.98 ? 219 ILE B CD1 1 
ATOM   5921 N N   . PRO B 1 220 ? -56.227 42.904 17.520  1.00 34.79 ? 220 PRO B N   1 
ATOM   5922 C CA  . PRO B 1 220 ? -56.872 41.952 16.614  1.00 40.90 ? 220 PRO B CA  1 
ATOM   5923 C C   . PRO B 1 220 ? -57.857 41.048 17.344  1.00 40.30 ? 220 PRO B C   1 
ATOM   5924 O O   . PRO B 1 220 ? -57.945 41.014 18.576  1.00 39.11 ? 220 PRO B O   1 
ATOM   5925 C CB  . PRO B 1 220 ? -55.694 41.156 16.034  1.00 39.66 ? 220 PRO B CB  1 
ATOM   5926 C CG  . PRO B 1 220 ? -54.566 41.404 16.944  1.00 40.39 ? 220 PRO B CG  1 
ATOM   5927 C CD  . PRO B 1 220 ? -54.760 42.776 17.481  1.00 37.81 ? 220 PRO B CD  1 
ATOM   5928 N N   . ASP B 1 221 ? -58.611 40.310 16.533  1.00 37.20 ? 221 ASP B N   1 
ATOM   5929 C CA  . ASP B 1 221 ? -59.564 39.305 16.992  1.00 36.20 ? 221 ASP B CA  1 
ATOM   5930 C C   . ASP B 1 221 ? -58.810 37.999 17.243  1.00 34.54 ? 221 ASP B C   1 
ATOM   5931 O O   . ASP B 1 221 ? -58.370 37.342 16.296  1.00 38.79 ? 221 ASP B O   1 
ATOM   5932 C CB  . ASP B 1 221 ? -60.652 39.122 15.936  1.00 38.74 ? 221 ASP B CB  1 
ATOM   5933 C CG  . ASP B 1 221 ? -61.801 38.267 16.413  1.00 45.36 ? 221 ASP B CG  1 
ATOM   5934 O OD1 . ASP B 1 221 ? -61.987 38.128 17.646  1.00 45.85 ? 221 ASP B OD1 1 
ATOM   5935 O OD2 . ASP B 1 221 ? -62.530 37.735 15.551  1.00 44.85 ? 221 ASP B OD2 1 
ATOM   5936 N N   . PHE B 1 222 ? -58.667 37.615 18.512  1.00 28.68 ? 222 PHE B N   1 
ATOM   5937 C CA  . PHE B 1 222 ? -57.974 36.372 18.875  1.00 31.06 ? 222 PHE B CA  1 
ATOM   5938 C C   . PHE B 1 222 ? -58.970 35.213 18.860  1.00 35.99 ? 222 PHE B C   1 
ATOM   5939 O O   . PHE B 1 222 ? -59.417 34.706 19.888  1.00 36.57 ? 222 PHE B O   1 
ATOM   5940 C CB  . PHE B 1 222 ? -57.296 36.506 20.233  1.00 29.94 ? 222 PHE B CB  1 
ATOM   5941 C CG  . PHE B 1 222 ? -56.052 37.332 20.208  1.00 27.67 ? 222 PHE B CG  1 
ATOM   5942 C CD1 . PHE B 1 222 ? -56.120 38.716 20.146  1.00 30.66 ? 222 PHE B CD1 1 
ATOM   5943 C CD2 . PHE B 1 222 ? -54.795 36.725 20.254  1.00 19.56 ? 222 PHE B CD2 1 
ATOM   5944 C CE1 . PHE B 1 222 ? -54.954 39.487 20.123  1.00 27.55 ? 222 PHE B CE1 1 
ATOM   5945 C CE2 . PHE B 1 222 ? -53.642 37.480 20.227  1.00 24.39 ? 222 PHE B CE2 1 
ATOM   5946 C CZ  . PHE B 1 222 ? -53.722 38.862 20.170  1.00 27.74 ? 222 PHE B CZ  1 
ATOM   5947 N N   . ALA B 1 223 ? -59.306 34.790 17.648  1.00 36.80 ? 223 ALA B N   1 
ATOM   5948 C CA  . ALA B 1 223 ? -60.258 33.713 17.425  1.00 41.21 ? 223 ALA B CA  1 
ATOM   5949 C C   . ALA B 1 223 ? -59.654 32.329 17.649  1.00 39.99 ? 223 ALA B C   1 
ATOM   5950 O O   . ALA B 1 223 ? -60.201 31.336 17.149  1.00 42.89 ? 223 ALA B O   1 
ATOM   5951 C CB  . ALA B 1 223 ? -60.830 33.815 16.007  1.00 41.89 ? 223 ALA B CB  1 
ATOM   5952 N N   . VAL B 1 224 ? -58.537 32.245 18.369  1.00 33.85 ? 224 VAL B N   1 
ATOM   5953 C CA  . VAL B 1 224 ? -57.896 30.979 18.692  1.00 34.86 ? 224 VAL B CA  1 
ATOM   5954 C C   . VAL B 1 224 ? -57.190 31.153 20.030  1.00 28.49 ? 224 VAL B C   1 
ATOM   5955 O O   . VAL B 1 224 ? -56.773 32.257 20.391  1.00 31.85 ? 224 VAL B O   1 
ATOM   5956 C CB  . VAL B 1 224 ? -56.918 30.536 17.579  1.00 43.85 ? 224 VAL B CB  1 
ATOM   5957 C CG1 . VAL B 1 224 ? -55.709 31.451 17.544  1.00 37.62 ? 224 VAL B CG1 1 
ATOM   5958 C CG2 . VAL B 1 224 ? -56.492 29.091 17.779  1.00 42.79 ? 224 VAL B CG2 1 
ATOM   5959 N N   . SER B 1 225 ? -57.085 30.064 20.786  1.00 29.77 ? 225 SER B N   1 
ATOM   5960 C CA  . SER B 1 225 ? -56.502 30.123 22.123  1.00 26.25 ? 225 SER B CA  1 
ATOM   5961 C C   . SER B 1 225 ? -55.003 29.866 22.073  1.00 24.43 ? 225 SER B C   1 
ATOM   5962 O O   . SER B 1 225 ? -54.549 28.918 21.422  1.00 29.41 ? 225 SER B O   1 
ATOM   5963 C CB  . SER B 1 225 ? -57.160 29.105 23.055  1.00 30.31 ? 225 SER B CB  1 
ATOM   5964 O OG  . SER B 1 225 ? -56.347 28.881 24.204  1.00 31.72 ? 225 SER B OG  1 
ATOM   5965 N N   . PHE B 1 226 ? -54.245 30.711 22.767  1.00 23.87 ? 226 PHE B N   1 
ATOM   5966 C CA  . PHE B 1 226 ? -52.815 30.517 22.943  1.00 21.34 ? 226 PHE B CA  1 
ATOM   5967 C C   . PHE B 1 226 ? -52.469 30.024 24.341  1.00 21.83 ? 226 PHE B C   1 
ATOM   5968 O O   . PHE B 1 226 ? -51.290 30.034 24.716  1.00 26.00 ? 226 PHE B O   1 
ATOM   5969 C CB  . PHE B 1 226 ? -52.071 31.819 22.641  1.00 24.84 ? 226 PHE B CB  1 
ATOM   5970 C CG  . PHE B 1 226 ? -52.025 32.162 21.169  1.00 26.20 ? 226 PHE B CG  1 
ATOM   5971 C CD1 . PHE B 1 226 ? -51.142 31.509 20.319  1.00 25.81 ? 226 PHE B CD1 1 
ATOM   5972 C CD2 . PHE B 1 226 ? -52.853 33.135 20.646  1.00 28.76 ? 226 PHE B CD2 1 
ATOM   5973 C CE1 . PHE B 1 226 ? -51.089 31.824 18.969  1.00 29.66 ? 226 PHE B CE1 1 
ATOM   5974 C CE2 . PHE B 1 226 ? -52.809 33.449 19.292  1.00 28.33 ? 226 PHE B CE2 1 
ATOM   5975 C CZ  . PHE B 1 226 ? -51.928 32.790 18.459  1.00 27.25 ? 226 PHE B CZ  1 
ATOM   5976 N N   . ARG B 1 227 ? -53.459 29.592 25.131  1.00 24.99 ? 227 ARG B N   1 
ATOM   5977 C CA  . ARG B 1 227 ? -53.171 29.277 26.530  1.00 23.85 ? 227 ARG B CA  1 
ATOM   5978 C C   . ARG B 1 227 ? -52.272 28.048 26.653  1.00 22.38 ? 227 ARG B C   1 
ATOM   5979 O O   . ARG B 1 227 ? -51.357 28.022 27.491  1.00 23.13 ? 227 ARG B O   1 
ATOM   5980 C CB  . ARG B 1 227 ? -54.477 29.101 27.308  1.00 34.46 ? 227 ARG B CB  1 
ATOM   5981 C CG  . ARG B 1 227 ? -55.373 30.347 27.289  1.00 32.09 ? 227 ARG B CG  1 
ATOM   5982 C CD  . ARG B 1 227 ? -56.669 30.161 28.111  1.00 37.22 ? 227 ARG B CD  1 
ATOM   5983 N NE  . ARG B 1 227 ? -56.400 29.858 29.517  1.00 40.05 ? 227 ARG B NE  1 
ATOM   5984 C CZ  . ARG B 1 227 ? -56.188 30.771 30.462  1.00 38.66 ? 227 ARG B CZ  1 
ATOM   5985 N NH1 . ARG B 1 227 ? -56.205 32.063 30.168  1.00 39.04 ? 227 ARG B NH1 1 
ATOM   5986 N NH2 . ARG B 1 227 ? -55.952 30.391 31.711  1.00 48.12 ? 227 ARG B NH2 1 
ATOM   5987 N N   . GLU B 1 228 ? -52.503 27.028 25.825  1.00 26.38 ? 228 GLU B N   1 
ATOM   5988 C CA  . GLU B 1 228 ? -51.658 25.842 25.885  1.00 32.13 ? 228 GLU B CA  1 
ATOM   5989 C C   . GLU B 1 228 ? -50.229 26.168 25.474  1.00 27.66 ? 228 GLU B C   1 
ATOM   5990 O O   . GLU B 1 228 ? -49.273 25.686 26.098  1.00 21.77 ? 228 GLU B O   1 
ATOM   5991 C CB  . GLU B 1 228 ? -52.244 24.733 25.008  1.00 34.45 ? 228 GLU B CB  1 
ATOM   5992 C CG  . GLU B 1 228 ? -53.344 23.903 25.673  1.00 52.65 ? 228 GLU B CG  1 
ATOM   5993 C CD  . GLU B 1 228 ? -53.465 22.496 25.083  1.00 64.50 ? 228 GLU B CD  1 
ATOM   5994 O OE1 . GLU B 1 228 ? -53.024 22.290 23.930  1.00 66.91 ? 228 GLU B OE1 1 
ATOM   5995 O OE2 . GLU B 1 228 ? -54.007 21.597 25.768  1.00 69.93 ? 228 GLU B OE2 1 
ATOM   5996 N N   . ASP B 1 229 ? -50.054 27.021 24.459  1.00 21.98 ? 229 ASP B N   1 
ATOM   5997 C CA  . ASP B 1 229 ? -48.696 27.414 24.079  1.00 20.84 ? 229 ASP B CA  1 
ATOM   5998 C C   . ASP B 1 229 ? -47.982 28.129 25.220  1.00 16.15 ? 229 ASP B C   1 
ATOM   5999 O O   . ASP B 1 229 ? -46.769 27.947 25.420  1.00 20.83 ? 229 ASP B O   1 
ATOM   6000 C CB  . ASP B 1 229 ? -48.721 28.299 22.835  1.00 18.71 ? 229 ASP B CB  1 
ATOM   6001 C CG  . ASP B 1 229 ? -48.963 27.513 21.570  1.00 27.91 ? 229 ASP B CG  1 
ATOM   6002 O OD1 . ASP B 1 229 ? -49.042 26.272 21.639  1.00 31.06 ? 229 ASP B OD1 1 
ATOM   6003 O OD2 . ASP B 1 229 ? -49.062 28.142 20.500  1.00 25.59 ? 229 ASP B OD2 1 
ATOM   6004 N N   . ALA B 1 230 ? -48.709 28.956 25.983  1.00 21.58 ? 230 ALA B N   1 
ATOM   6005 C CA  . ALA B 1 230 ? -48.069 29.647 27.089  1.00 17.30 ? 230 ALA B CA  1 
ATOM   6006 C C   . ALA B 1 230 ? -47.501 28.639 28.079  1.00 21.38 ? 230 ALA B C   1 
ATOM   6007 O O   . ALA B 1 230 ? -46.357 28.771 28.519  1.00 17.61 ? 230 ALA B O   1 
ATOM   6008 C CB  . ALA B 1 230 ? -49.052 30.599 27.778  1.00 20.49 ? 230 ALA B CB  1 
ATOM   6009 N N   . SER B 1 231 ? -48.284 27.605 28.402  1.00 22.77 ? 231 SER B N   1 
ATOM   6010 C CA  . SER B 1 231 ? -47.801 26.540 29.275  1.00 23.29 ? 231 SER B CA  1 
ATOM   6011 C C   . SER B 1 231 ? -46.624 25.802 28.645  1.00 21.08 ? 231 SER B C   1 
ATOM   6012 O O   . SER B 1 231 ? -45.646 25.471 29.334  1.00 24.24 ? 231 SER B O   1 
ATOM   6013 C CB  . SER B 1 231 ? -48.953 25.586 29.579  1.00 26.28 ? 231 SER B CB  1 
ATOM   6014 O OG  . SER B 1 231 ? -48.541 24.554 30.436  1.00 43.06 ? 231 SER B OG  1 
ATOM   6015 N N   . LYS B 1 232 ? -46.681 25.576 27.330  1.00 18.33 ? 232 LYS B N   1 
ATOM   6016 C CA  . LYS B 1 232 ? -45.605 24.877 26.629  1.00 19.18 ? 232 LYS B CA  1 
ATOM   6017 C C   . LYS B 1 232 ? -44.294 25.654 26.675  1.00 21.80 ? 232 LYS B C   1 
ATOM   6018 O O   . LYS B 1 232 ? -43.219 25.058 26.843  1.00 21.58 ? 232 LYS B O   1 
ATOM   6019 C CB  . LYS B 1 232 ? -46.005 24.623 25.173  1.00 23.44 ? 232 LYS B CB  1 
ATOM   6020 C CG  . LYS B 1 232 ? -46.794 23.362 24.940  1.00 32.69 ? 232 LYS B CG  1 
ATOM   6021 C CD  . LYS B 1 232 ? -46.686 22.890 23.479  1.00 35.43 ? 232 LYS B CD  1 
ATOM   6022 C CE  . LYS B 1 232 ? -45.421 22.054 23.256  1.00 42.47 ? 232 LYS B CE  1 
ATOM   6023 N NZ  . LYS B 1 232 ? -45.443 21.270 21.977  1.00 51.36 ? 232 LYS B NZ  1 
ATOM   6024 N N   . HIS B 1 233 ? -44.346 26.980 26.478  1.00 17.13 ? 233 HIS B N   1 
ATOM   6025 C CA  . HIS B 1 233 ? -43.123 27.773 26.591  1.00 17.52 ? 233 HIS B CA  1 
ATOM   6026 C C   . HIS B 1 233 ? -42.467 27.550 27.951  1.00 19.80 ? 233 HIS B C   1 
ATOM   6027 O O   . HIS B 1 233 ? -41.242 27.473 28.061  1.00 16.88 ? 233 HIS B O   1 
ATOM   6028 C CB  . HIS B 1 233 ? -43.409 29.272 26.426  1.00 19.43 ? 233 HIS B CB  1 
ATOM   6029 C CG  . HIS B 1 233 ? -43.639 29.721 25.020  1.00 20.32 ? 233 HIS B CG  1 
ATOM   6030 N ND1 . HIS B 1 233 ? -42.615 30.102 24.178  1.00 17.18 ? 233 HIS B ND1 1 
ATOM   6031 C CD2 . HIS B 1 233 ? -44.788 29.907 24.326  1.00 14.42 ? 233 HIS B CD2 1 
ATOM   6032 C CE1 . HIS B 1 233 ? -43.121 30.480 23.016  1.00 18.68 ? 233 HIS B CE1 1 
ATOM   6033 N NE2 . HIS B 1 233 ? -44.438 30.366 23.077  1.00 20.28 ? 233 HIS B NE2 1 
ATOM   6034 N N   . VAL B 1 234 ? -43.272 27.451 29.005  1.00 18.18 ? 234 VAL B N   1 
ATOM   6035 C CA  . VAL B 1 234 ? -42.708 27.322 30.345  1.00 17.31 ? 234 VAL B CA  1 
ATOM   6036 C C   . VAL B 1 234 ? -42.166 25.921 30.565  1.00 18.86 ? 234 VAL B C   1 
ATOM   6037 O O   . VAL B 1 234 ? -41.049 25.751 31.067  1.00 21.29 ? 234 VAL B O   1 
ATOM   6038 C CB  . VAL B 1 234 ? -43.750 27.711 31.411  1.00 16.16 ? 234 VAL B CB  1 
ATOM   6039 C CG1 . VAL B 1 234 ? -43.172 27.499 32.819  1.00 15.78 ? 234 VAL B CG1 1 
ATOM   6040 C CG2 . VAL B 1 234 ? -44.134 29.174 31.238  1.00 14.56 ? 234 VAL B CG2 1 
ATOM   6041 N N   . GLU B 1 235 ? -42.937 24.905 30.182  1.00 15.08 ? 235 GLU B N   1 
ATOM   6042 C CA  . GLU B 1 235 ? -42.522 23.525 30.406  1.00 21.62 ? 235 GLU B CA  1 
ATOM   6043 C C   . GLU B 1 235 ? -41.289 23.176 29.579  1.00 20.80 ? 235 GLU B C   1 
ATOM   6044 O O   . GLU B 1 235 ? -40.364 22.527 30.081  1.00 24.38 ? 235 GLU B O   1 
ATOM   6045 C CB  . GLU B 1 235 ? -43.677 22.564 30.104  1.00 22.23 ? 235 GLU B CB  1 
ATOM   6046 C CG  . GLU B 1 235 ? -43.409 21.119 30.578  1.00 38.14 ? 235 GLU B CG  1 
ATOM   6047 C CD  . GLU B 1 235 ? -42.837 21.040 32.003  1.00 51.80 ? 235 GLU B CD  1 
ATOM   6048 O OE1 . GLU B 1 235 ? -43.441 21.635 32.930  1.00 51.65 ? 235 GLU B OE1 1 
ATOM   6049 O OE2 . GLU B 1 235 ? -41.774 20.390 32.190  1.00 47.05 ? 235 GLU B OE2 1 
ATOM   6050 N N   . LEU B 1 236 ? -41.228 23.646 28.331  1.00 18.20 ? 236 LEU B N   1 
ATOM   6051 C CA  . LEU B 1 236 ? -40.039 23.402 27.516  1.00 23.66 ? 236 LEU B CA  1 
ATOM   6052 C C   . LEU B 1 236 ? -38.814 24.119 28.081  1.00 16.50 ? 236 LEU B C   1 
ATOM   6053 O O   . LEU B 1 236 ? -37.702 23.579 28.047  1.00 19.81 ? 236 LEU B O   1 
ATOM   6054 C CB  . LEU B 1 236 ? -40.306 23.821 26.065  1.00 20.91 ? 236 LEU B CB  1 
ATOM   6055 C CG  . LEU B 1 236 ? -41.271 22.887 25.340  1.00 24.63 ? 236 LEU B CG  1 
ATOM   6056 C CD1 . LEU B 1 236 ? -41.653 23.488 23.996  1.00 23.68 ? 236 LEU B CD1 1 
ATOM   6057 C CD2 . LEU B 1 236 ? -40.656 21.501 25.172  1.00 24.44 ? 236 LEU B CD2 1 
ATOM   6058 N N   . ALA B 1 237 ? -39.004 25.334 28.606  1.00 15.10 ? 237 ALA B N   1 
ATOM   6059 C CA  . ALA B 1 237 ? -37.917 26.055 29.255  1.00 19.56 ? 237 ALA B CA  1 
ATOM   6060 C C   . ALA B 1 237 ? -37.378 25.275 30.442  1.00 16.39 ? 237 ALA B C   1 
ATOM   6061 O O   . ALA B 1 237 ? -36.159 25.219 30.658  1.00 16.61 ? 237 ALA B O   1 
ATOM   6062 C CB  . ALA B 1 237 ? -38.398 27.429 29.705  1.00 12.18 ? 237 ALA B CB  1 
ATOM   6063 N N   . LYS B 1 238 ? -38.273 24.672 31.233  1.00 19.58 ? 238 LYS B N   1 
ATOM   6064 C CA  . LYS B 1 238 ? -37.814 23.891 32.375  1.00 18.61 ? 238 LYS B CA  1 
ATOM   6065 C C   . LYS B 1 238 ? -36.969 22.711 31.922  1.00 21.75 ? 238 LYS B C   1 
ATOM   6066 O O   . LYS B 1 238 ? -35.940 22.406 32.535  1.00 19.52 ? 238 LYS B O   1 
ATOM   6067 C CB  . LYS B 1 238 ? -39.007 23.421 33.208  1.00 18.00 ? 238 LYS B CB  1 
ATOM   6068 C CG  . LYS B 1 238 ? -39.730 24.579 33.899  1.00 19.22 ? 238 LYS B CG  1 
ATOM   6069 C CD  . LYS B 1 238 ? -41.010 24.105 34.578  1.00 25.00 ? 238 LYS B CD  1 
ATOM   6070 C CE  . LYS B 1 238 ? -40.735 22.953 35.537  1.00 33.03 ? 238 LYS B CE  1 
ATOM   6071 N NZ  . LYS B 1 238 ? -41.972 22.566 36.255  1.00 31.24 ? 238 LYS B NZ  1 
ATOM   6072 N N   . GLU B 1 239 ? -37.373 22.046 30.837  1.00 16.69 ? 239 GLU B N   1 
ATOM   6073 C CA  . GLU B 1 239 ? -36.605 20.909 30.352  1.00 17.61 ? 239 GLU B CA  1 
ATOM   6074 C C   . GLU B 1 239 ? -35.239 21.332 29.830  1.00 20.61 ? 239 GLU B C   1 
ATOM   6075 O O   . GLU B 1 239 ? -34.246 20.641 30.080  1.00 20.08 ? 239 GLU B O   1 
ATOM   6076 C CB  . GLU B 1 239 ? -37.410 20.144 29.292  1.00 20.49 ? 239 GLU B CB  1 
ATOM   6077 C CG  . GLU B 1 239 ? -38.713 19.601 29.865  1.00 35.07 ? 239 GLU B CG  1 
ATOM   6078 C CD  . GLU B 1 239 ? -39.686 19.104 28.818  1.00 49.19 ? 239 GLU B CD  1 
ATOM   6079 O OE1 . GLU B 1 239 ? -40.893 19.015 29.140  1.00 58.21 ? 239 GLU B OE1 1 
ATOM   6080 O OE2 . GLU B 1 239 ? -39.257 18.797 27.688  1.00 49.96 ? 239 GLU B OE2 1 
ATOM   6081 N N   . LYS B 1 240 ? -35.164 22.455 29.107  1.00 18.13 ? 240 LYS B N   1 
ATOM   6082 C CA  . LYS B 1 240 ? -33.872 22.926 28.621  1.00 23.65 ? 240 LYS B CA  1 
ATOM   6083 C C   . LYS B 1 240 ? -32.974 23.350 29.779  1.00 24.26 ? 240 LYS B C   1 
ATOM   6084 O O   . LYS B 1 240 ? -31.763 23.088 29.767  1.00 18.31 ? 240 LYS B O   1 
ATOM   6085 C CB  . LYS B 1 240 ? -34.059 24.089 27.646  1.00 19.96 ? 240 LYS B CB  1 
ATOM   6086 C CG  . LYS B 1 240 ? -32.757 24.508 26.946  1.00 23.31 ? 240 LYS B CG  1 
ATOM   6087 C CD  . LYS B 1 240 ? -32.388 23.472 25.869  1.00 24.12 ? 240 LYS B CD  1 
ATOM   6088 C CE  . LYS B 1 240 ? -30.987 23.709 25.311  1.00 27.80 ? 240 LYS B CE  1 
ATOM   6089 N NZ  . LYS B 1 240 ? -30.600 22.687 24.260  1.00 25.55 ? 240 LYS B NZ  1 
ATOM   6090 N N   . TYR B 1 241 ? -33.544 24.043 30.765  1.00 18.03 ? 241 TYR B N   1 
ATOM   6091 C CA  . TYR B 1 241 ? -32.767 24.422 31.937  1.00 19.98 ? 241 TYR B CA  1 
ATOM   6092 C C   . TYR B 1 241 ? -32.219 23.186 32.633  1.00 17.20 ? 241 TYR B C   1 
ATOM   6093 O O   . TYR B 1 241 ? -31.062 23.172 33.064  1.00 18.20 ? 241 TYR B O   1 
ATOM   6094 C CB  . TYR B 1 241 ? -33.633 25.260 32.884  1.00 15.76 ? 241 TYR B CB  1 
ATOM   6095 C CG  . TYR B 1 241 ? -32.889 25.829 34.084  1.00 14.34 ? 241 TYR B CG  1 
ATOM   6096 C CD1 . TYR B 1 241 ? -32.711 25.067 35.233  1.00 17.91 ? 241 TYR B CD1 1 
ATOM   6097 C CD2 . TYR B 1 241 ? -32.378 27.122 34.063  1.00 17.11 ? 241 TYR B CD2 1 
ATOM   6098 C CE1 . TYR B 1 241 ? -32.028 25.562 36.314  1.00 18.89 ? 241 TYR B CE1 1 
ATOM   6099 C CE2 . TYR B 1 241 ? -31.678 27.636 35.159  1.00 16.75 ? 241 TYR B CE2 1 
ATOM   6100 C CZ  . TYR B 1 241 ? -31.520 26.853 36.273  1.00 17.85 ? 241 TYR B CZ  1 
ATOM   6101 O OH  . TYR B 1 241 ? -30.852 27.357 37.355  1.00 19.41 ? 241 TYR B OH  1 
ATOM   6102 N N   . PHE B 1 242 ? -33.025 22.127 32.733  1.00 14.55 ? 242 PHE B N   1 
ATOM   6103 C CA  . PHE B 1 242 ? -32.528 20.910 33.376  1.00 15.62 ? 242 PHE B CA  1 
ATOM   6104 C C   . PHE B 1 242 ? -31.384 20.298 32.576  1.00 17.61 ? 242 PHE B C   1 
ATOM   6105 O O   . PHE B 1 242 ? -30.411 19.802 33.153  1.00 18.62 ? 242 PHE B O   1 
ATOM   6106 C CB  . PHE B 1 242 ? -33.649 19.877 33.532  1.00 16.67 ? 242 PHE B CB  1 
ATOM   6107 C CG  . PHE B 1 242 ? -33.199 18.617 34.217  1.00 17.74 ? 242 PHE B CG  1 
ATOM   6108 C CD1 . PHE B 1 242 ? -32.605 17.584 33.494  1.00 19.24 ? 242 PHE B CD1 1 
ATOM   6109 C CD2 . PHE B 1 242 ? -33.356 18.468 35.581  1.00 21.09 ? 242 PHE B CD2 1 
ATOM   6110 C CE1 . PHE B 1 242 ? -32.164 16.432 34.119  1.00 19.92 ? 242 PHE B CE1 1 
ATOM   6111 C CE2 . PHE B 1 242 ? -32.930 17.308 36.216  1.00 23.52 ? 242 PHE B CE2 1 
ATOM   6112 C CZ  . PHE B 1 242 ? -32.326 16.293 35.484  1.00 22.36 ? 242 PHE B CZ  1 
ATOM   6113 N N   . GLU B 1 243 ? -31.501 20.281 31.244  1.00 19.28 ? 243 GLU B N   1 
ATOM   6114 C CA  . GLU B 1 243 ? -30.401 19.760 30.434  1.00 19.53 ? 243 GLU B CA  1 
ATOM   6115 C C   . GLU B 1 243 ? -29.078 20.410 30.836  1.00 21.45 ? 243 GLU B C   1 
ATOM   6116 O O   . GLU B 1 243 ? -28.072 19.726 31.067  1.00 23.95 ? 243 GLU B O   1 
ATOM   6117 C CB  . GLU B 1 243 ? -30.672 19.986 28.946  1.00 16.81 ? 243 GLU B CB  1 
ATOM   6118 C CG  . GLU B 1 243 ? -29.443 19.615 28.068  1.00 28.79 ? 243 GLU B CG  1 
ATOM   6119 C CD  . GLU B 1 243 ? -29.533 20.098 26.614  1.00 37.28 ? 243 GLU B CD  1 
ATOM   6120 O OE1 . GLU B 1 243 ? -28.500 20.028 25.901  1.00 45.54 ? 243 GLU B OE1 1 
ATOM   6121 O OE2 . GLU B 1 243 ? -30.616 20.542 26.176  1.00 33.17 ? 243 GLU B OE2 1 
ATOM   6122 N N   . ILE B 1 244 ? -29.076 21.734 30.966  1.00 20.18 ? 244 ILE B N   1 
ATOM   6123 C CA  . ILE B 1 244 ? -27.824 22.442 31.186  1.00 20.20 ? 244 ILE B CA  1 
ATOM   6124 C C   . ILE B 1 244 ? -27.387 22.333 32.643  1.00 19.35 ? 244 ILE B C   1 
ATOM   6125 O O   . ILE B 1 244 ? -26.225 22.027 32.940  1.00 18.07 ? 244 ILE B O   1 
ATOM   6126 C CB  . ILE B 1 244 ? -27.964 23.911 30.749  1.00 23.34 ? 244 ILE B CB  1 
ATOM   6127 C CG1 . ILE B 1 244 ? -28.350 23.985 29.266  1.00 21.26 ? 244 ILE B CG1 1 
ATOM   6128 C CG2 . ILE B 1 244 ? -26.677 24.682 31.056  1.00 17.58 ? 244 ILE B CG2 1 
ATOM   6129 C CD1 . ILE B 1 244 ? -27.460 23.111 28.350  1.00 22.28 ? 244 ILE B CD1 1 
ATOM   6130 N N   . PHE B 1 245 ? -28.310 22.569 33.584  1.00 17.62 ? 245 PHE B N   1 
ATOM   6131 C CA  . PHE B 1 245 ? -27.920 22.756 34.978  1.00 17.89 ? 245 PHE B CA  1 
ATOM   6132 C C   . PHE B 1 245 ? -28.269 21.595 35.896  1.00 22.24 ? 245 PHE B C   1 
ATOM   6133 O O   . PHE B 1 245 ? -27.844 21.598 37.065  1.00 21.45 ? 245 PHE B O   1 
ATOM   6134 C CB  . PHE B 1 245 ? -28.552 24.057 35.500  1.00 15.26 ? 245 PHE B CB  1 
ATOM   6135 C CG  . PHE B 1 245 ? -28.108 25.271 34.740  1.00 16.63 ? 245 PHE B CG  1 
ATOM   6136 C CD1 . PHE B 1 245 ? -26.818 25.756 34.899  1.00 21.85 ? 245 PHE B CD1 1 
ATOM   6137 C CD2 . PHE B 1 245 ? -28.956 25.911 33.843  1.00 16.42 ? 245 PHE B CD2 1 
ATOM   6138 C CE1 . PHE B 1 245 ? -26.381 26.877 34.182  1.00 19.43 ? 245 PHE B CE1 1 
ATOM   6139 C CE2 . PHE B 1 245 ? -28.530 27.023 33.132  1.00 15.86 ? 245 PHE B CE2 1 
ATOM   6140 C CZ  . PHE B 1 245 ? -27.237 27.507 33.303  1.00 17.01 ? 245 PHE B CZ  1 
ATOM   6141 N N   . GLY B 1 246 ? -29.002 20.598 35.409  1.00 17.88 ? 246 GLY B N   1 
ATOM   6142 C CA  . GLY B 1 246 ? -29.313 19.448 36.241  1.00 19.82 ? 246 GLY B CA  1 
ATOM   6143 C C   . GLY B 1 246 ? -30.311 19.685 37.364  1.00 24.56 ? 246 GLY B C   1 
ATOM   6144 O O   . GLY B 1 246 ? -30.345 18.903 38.326  1.00 26.00 ? 246 GLY B O   1 
ATOM   6145 N N   . GLU B 1 247 ? -31.123 20.739 37.269  1.00 23.53 ? 247 GLU B N   1 
ATOM   6146 C CA  . GLU B 1 247 ? -32.198 21.029 38.215  1.00 28.00 ? 247 GLU B CA  1 
ATOM   6147 C C   . GLU B 1 247 ? -33.369 21.624 37.454  1.00 20.85 ? 247 GLU B C   1 
ATOM   6148 O O   . GLU B 1 247 ? -33.190 22.220 36.393  1.00 22.40 ? 247 GLU B O   1 
ATOM   6149 C CB  . GLU B 1 247 ? -31.782 22.051 39.300  1.00 37.32 ? 247 GLU B CB  1 
ATOM   6150 C CG  . GLU B 1 247 ? -30.655 21.647 40.235  1.00 47.05 ? 247 GLU B CG  1 
ATOM   6151 C CD  . GLU B 1 247 ? -30.295 22.772 41.193  1.00 46.81 ? 247 GLU B CD  1 
ATOM   6152 O OE1 . GLU B 1 247 ? -30.730 23.917 40.952  1.00 38.97 ? 247 GLU B OE1 1 
ATOM   6153 O OE2 . GLU B 1 247 ? -29.600 22.509 42.199  1.00 52.36 ? 247 GLU B OE2 1 
ATOM   6154 N N   . HIS B 1 248 ? -34.570 21.498 38.011  1.00 21.34 ? 248 HIS B N   1 
ATOM   6155 C CA  . HIS B 1 248 ? -35.673 22.314 37.507  1.00 22.65 ? 248 HIS B CA  1 
ATOM   6156 C C   . HIS B 1 248 ? -35.476 23.756 37.979  1.00 23.73 ? 248 HIS B C   1 
ATOM   6157 O O   . HIS B 1 248 ? -35.058 23.981 39.123  1.00 25.31 ? 248 HIS B O   1 
ATOM   6158 C CB  . HIS B 1 248 ? -37.029 21.784 37.982  1.00 25.65 ? 248 HIS B CB  1 
ATOM   6159 C CG  . HIS B 1 248 ? -37.392 20.444 37.419  1.00 42.51 ? 248 HIS B CG  1 
ATOM   6160 N ND1 . HIS B 1 248 ? -37.475 19.306 38.199  1.00 48.40 ? 248 HIS B ND1 1 
ATOM   6161 C CD2 . HIS B 1 248 ? -37.703 20.059 36.159  1.00 47.42 ? 248 HIS B CD2 1 
ATOM   6162 C CE1 . HIS B 1 248 ? -37.819 18.278 37.443  1.00 46.88 ? 248 HIS B CE1 1 
ATOM   6163 N NE2 . HIS B 1 248 ? -37.963 18.708 36.201  1.00 47.51 ? 248 HIS B NE2 1 
ATOM   6164 N N   . PRO B 1 249 ? -35.718 24.749 37.120  1.00 18.77 ? 249 PRO B N   1 
ATOM   6165 C CA  . PRO B 1 249 ? -35.497 26.141 37.539  1.00 20.73 ? 249 PRO B CA  1 
ATOM   6166 C C   . PRO B 1 249 ? -36.614 26.565 38.483  1.00 21.88 ? 249 PRO B C   1 
ATOM   6167 O O   . PRO B 1 249 ? -37.783 26.281 38.237  1.00 28.18 ? 249 PRO B O   1 
ATOM   6168 C CB  . PRO B 1 249 ? -35.531 26.923 36.218  1.00 19.33 ? 249 PRO B CB  1 
ATOM   6169 C CG  . PRO B 1 249 ? -36.497 26.103 35.355  1.00 24.89 ? 249 PRO B CG  1 
ATOM   6170 C CD  . PRO B 1 249 ? -36.296 24.653 35.761  1.00 20.14 ? 249 PRO B CD  1 
ATOM   6171 N N   . VAL B 1 250 ? -36.252 27.220 39.583  1.00 19.59 ? 250 VAL B N   1 
ATOM   6172 C CA  . VAL B 1 250 ? -37.265 27.749 40.490  1.00 22.73 ? 250 VAL B CA  1 
ATOM   6173 C C   . VAL B 1 250 ? -37.361 29.259 40.429  1.00 18.85 ? 250 VAL B C   1 
ATOM   6174 O O   . VAL B 1 250 ? -38.248 29.842 41.083  1.00 17.87 ? 250 VAL B O   1 
ATOM   6175 C CB  . VAL B 1 250 ? -37.041 27.283 41.940  1.00 23.10 ? 250 VAL B CB  1 
ATOM   6176 C CG1 . VAL B 1 250 ? -37.302 25.793 42.053  1.00 30.49 ? 250 VAL B CG1 1 
ATOM   6177 C CG2 . VAL B 1 250 ? -35.627 27.638 42.402  1.00 23.43 ? 250 VAL B CG2 1 
ATOM   6178 N N   . TYR B 1 251 ? -36.497 29.916 39.657  1.00 15.36 ? 251 TYR B N   1 
ATOM   6179 C CA  . TYR B 1 251 ? -36.609 31.337 39.381  1.00 13.89 ? 251 TYR B CA  1 
ATOM   6180 C C   . TYR B 1 251 ? -36.800 31.497 37.889  1.00 14.18 ? 251 TYR B C   1 
ATOM   6181 O O   . TYR B 1 251 ? -36.177 30.777 37.099  1.00 16.91 ? 251 TYR B O   1 
ATOM   6182 C CB  . TYR B 1 251 ? -35.361 32.126 39.834  1.00 17.57 ? 251 TYR B CB  1 
ATOM   6183 C CG  . TYR B 1 251 ? -34.920 31.664 41.199  1.00 22.17 ? 251 TYR B CG  1 
ATOM   6184 C CD1 . TYR B 1 251 ? -35.731 31.887 42.301  1.00 28.44 ? 251 TYR B CD1 1 
ATOM   6185 C CD2 . TYR B 1 251 ? -33.744 30.945 41.372  1.00 23.76 ? 251 TYR B CD2 1 
ATOM   6186 C CE1 . TYR B 1 251 ? -35.383 31.431 43.543  1.00 23.99 ? 251 TYR B CE1 1 
ATOM   6187 C CE2 . TYR B 1 251 ? -33.375 30.495 42.625  1.00 22.13 ? 251 TYR B CE2 1 
ATOM   6188 C CZ  . TYR B 1 251 ? -34.203 30.745 43.704  1.00 24.99 ? 251 TYR B CZ  1 
ATOM   6189 O OH  . TYR B 1 251 ? -33.892 30.304 44.963  1.00 32.29 ? 251 TYR B OH  1 
ATOM   6190 N N   . MET B 1 252 ? -37.698 32.401 37.507  1.00 15.93 ? 252 MET B N   1 
ATOM   6191 C CA  . MET B 1 252 ? -37.803 32.778 36.112  1.00 14.70 ? 252 MET B CA  1 
ATOM   6192 C C   . MET B 1 252 ? -37.915 34.280 35.957  1.00 17.56 ? 252 MET B C   1 
ATOM   6193 O O   . MET B 1 252 ? -38.499 34.974 36.799  1.00 17.22 ? 252 MET B O   1 
ATOM   6194 C CB  . MET B 1 252 ? -38.993 32.113 35.386  1.00 23.44 ? 252 MET B CB  1 
ATOM   6195 C CG  . MET B 1 252 ? -38.711 30.683 34.938  1.00 27.26 ? 252 MET B CG  1 
ATOM   6196 S SD  . MET B 1 252 ? -40.044 30.045 33.906  1.00 26.47 ? 252 MET B SD  1 
ATOM   6197 C CE  . MET B 1 252 ? -40.007 31.120 32.658  1.00 48.04 ? 252 MET B CE  1 
ATOM   6198 N N   . TRP B 1 253 ? -37.325 34.768 34.859  1.00 14.96 ? 253 TRP B N   1 
ATOM   6199 C CA  . TRP B 1 253 ? -37.458 36.157 34.465  1.00 16.05 ? 253 TRP B CA  1 
ATOM   6200 C C   . TRP B 1 253 ? -38.583 36.252 33.445  1.00 16.74 ? 253 TRP B C   1 
ATOM   6201 O O   . TRP B 1 253 ? -38.487 35.650 32.357  1.00 16.53 ? 253 TRP B O   1 
ATOM   6202 C CB  . TRP B 1 253 ? -36.154 36.700 33.877  1.00 16.42 ? 253 TRP B CB  1 
ATOM   6203 C CG  . TRP B 1 253 ? -36.360 38.039 33.228  1.00 14.90 ? 253 TRP B CG  1 
ATOM   6204 C CD1 . TRP B 1 253 ? -36.302 38.320 31.894  1.00 17.02 ? 253 TRP B CD1 1 
ATOM   6205 C CD2 . TRP B 1 253 ? -36.723 39.265 33.880  1.00 17.77 ? 253 TRP B CD2 1 
ATOM   6206 N NE1 . TRP B 1 253 ? -36.586 39.639 31.674  1.00 15.59 ? 253 TRP B NE1 1 
ATOM   6207 C CE2 . TRP B 1 253 ? -36.840 40.246 32.877  1.00 14.08 ? 253 TRP B CE2 1 
ATOM   6208 C CE3 . TRP B 1 253 ? -36.956 39.627 35.219  1.00 19.34 ? 253 TRP B CE3 1 
ATOM   6209 C CZ2 . TRP B 1 253 ? -37.186 41.560 33.154  1.00 11.35 ? 253 TRP B CZ2 1 
ATOM   6210 C CZ3 . TRP B 1 253 ? -37.295 40.939 35.503  1.00 19.18 ? 253 TRP B CZ3 1 
ATOM   6211 C CH2 . TRP B 1 253 ? -37.414 41.895 34.473  1.00 15.88 ? 253 TRP B CH2 1 
ATOM   6212 N N   . PRO B 1 254 ? -39.662 36.948 33.748  1.00 12.26 ? 254 PRO B N   1 
ATOM   6213 C CA  . PRO B 1 254 ? -40.759 37.084 32.765  1.00 11.14 ? 254 PRO B CA  1 
ATOM   6214 C C   . PRO B 1 254 ? -40.326 38.036 31.670  1.00 15.54 ? 254 PRO B C   1 
ATOM   6215 O O   . PRO B 1 254 ? -39.815 39.121 31.970  1.00 15.97 ? 254 PRO B O   1 
ATOM   6216 C CB  . PRO B 1 254 ? -41.911 37.661 33.599  1.00 17.68 ? 254 PRO B CB  1 
ATOM   6217 C CG  . PRO B 1 254 ? -41.256 38.313 34.748  1.00 21.50 ? 254 PRO B CG  1 
ATOM   6218 C CD  . PRO B 1 254 ? -39.958 37.616 35.031  1.00 16.98 ? 254 PRO B CD  1 
ATOM   6219 N N   . PRO B 1 255 ? -40.443 37.649 30.401  1.00 16.92 ? 255 PRO B N   1 
ATOM   6220 C CA  . PRO B 1 255 ? -39.927 38.504 29.315  1.00 14.58 ? 255 PRO B CA  1 
ATOM   6221 C C   . PRO B 1 255 ? -40.560 39.893 29.341  1.00 15.44 ? 255 PRO B C   1 
ATOM   6222 O O   . PRO B 1 255 ? -41.771 40.042 29.537  1.00 17.30 ? 255 PRO B O   1 
ATOM   6223 C CB  . PRO B 1 255 ? -40.315 37.732 28.043  1.00 15.55 ? 255 PRO B CB  1 
ATOM   6224 C CG  . PRO B 1 255 ? -40.368 36.300 28.480  1.00 15.85 ? 255 PRO B CG  1 
ATOM   6225 C CD  . PRO B 1 255 ? -40.923 36.342 29.915  1.00 15.64 ? 255 PRO B CD  1 
ATOM   6226 N N   . GLN B 1 256 ? -39.715 40.916 29.141  1.00 15.76 ? 256 GLN B N   1 
ATOM   6227 C CA  . GLN B 1 256 ? -40.102 42.322 29.240  1.00 18.80 ? 256 GLN B CA  1 
ATOM   6228 C C   . GLN B 1 256 ? -40.734 42.653 30.600  1.00 17.65 ? 256 GLN B C   1 
ATOM   6229 O O   . GLN B 1 256 ? -41.512 43.607 30.717  1.00 14.99 ? 256 GLN B O   1 
ATOM   6230 C CB  . GLN B 1 256 ? -41.045 42.713 28.091  1.00 20.00 ? 256 GLN B CB  1 
ATOM   6231 C CG  . GLN B 1 256 ? -40.604 42.182 26.721  1.00 17.55 ? 256 GLN B CG  1 
ATOM   6232 C CD  . GLN B 1 256 ? -39.395 42.930 26.208  1.00 25.51 ? 256 GLN B CD  1 
ATOM   6233 O OE1 . GLN B 1 256 ? -38.966 43.922 26.805  1.00 25.88 ? 256 GLN B OE1 1 
ATOM   6234 N NE2 . GLN B 1 256 ? -38.835 42.466 25.110  1.00 25.62 ? 256 GLN B NE2 1 
ATOM   6235 N N   . ALA B 1 257 ? -40.388 41.882 31.643  1.00 12.40 ? 257 ALA B N   1 
ATOM   6236 C CA  . ALA B 1 257 ? -40.968 42.015 32.981  1.00 14.45 ? 257 ALA B CA  1 
ATOM   6237 C C   . ALA B 1 257 ? -42.485 41.803 32.970  1.00 15.62 ? 257 ALA B C   1 
ATOM   6238 O O   . ALA B 1 257 ? -43.187 42.210 33.903  1.00 15.83 ? 257 ALA B O   1 
ATOM   6239 C CB  . ALA B 1 257 ? -40.630 43.379 33.606  1.00 20.67 ? 257 ALA B CB  1 
ATOM   6240 N N   . SER B 1 258 ? -43.017 41.150 31.942  1.00 15.16 ? 258 SER B N   1 
ATOM   6241 C CA  . SER B 1 258 ? -44.465 41.162 31.730  1.00 16.12 ? 258 SER B CA  1 
ATOM   6242 C C   . SER B 1 258 ? -45.168 40.197 32.676  1.00 14.99 ? 258 SER B C   1 
ATOM   6243 O O   . SER B 1 258 ? -44.865 38.997 32.697  1.00 18.43 ? 258 SER B O   1 
ATOM   6244 C CB  . SER B 1 258 ? -44.800 40.797 30.288  1.00 20.21 ? 258 SER B CB  1 
ATOM   6245 O OG  . SER B 1 258 ? -46.183 41.022 30.087  1.00 28.90 ? 258 SER B OG  1 
ATOM   6246 N N   . VAL B 1 259 ? -46.115 40.712 33.460  1.00 17.79 ? 259 VAL B N   1 
ATOM   6247 C CA  . VAL B 1 259 ? -46.913 39.878 34.351  1.00 16.83 ? 259 VAL B CA  1 
ATOM   6248 C C   . VAL B 1 259 ? -48.377 40.291 34.254  1.00 15.70 ? 259 VAL B C   1 
ATOM   6249 O O   . VAL B 1 259 ? -48.723 41.336 33.704  1.00 19.76 ? 259 VAL B O   1 
ATOM   6250 C CB  . VAL B 1 259 ? -46.439 39.962 35.825  1.00 19.03 ? 259 VAL B CB  1 
ATOM   6251 C CG1 . VAL B 1 259 ? -44.977 39.534 35.956  1.00 17.44 ? 259 VAL B CG1 1 
ATOM   6252 C CG2 . VAL B 1 259 ? -46.659 41.355 36.364  1.00 18.28 ? 259 VAL B CG2 1 
ATOM   6253 N N   . SER B 1 260 ? -49.225 39.438 34.815  1.00 14.63 ? 260 SER B N   1 
ATOM   6254 C CA  . SER B 1 260 ? -50.667 39.592 34.963  1.00 16.67 ? 260 SER B CA  1 
ATOM   6255 C C   . SER B 1 260 ? -51.044 38.584 36.027  1.00 18.80 ? 260 SER B C   1 
ATOM   6256 O O   . SER B 1 260 ? -50.248 37.691 36.344  1.00 20.83 ? 260 SER B O   1 
ATOM   6257 C CB  . SER B 1 260 ? -51.426 39.310 33.658  1.00 18.76 ? 260 SER B CB  1 
ATOM   6258 O OG  . SER B 1 260 ? -51.309 37.937 33.319  1.00 20.98 ? 260 SER B OG  1 
ATOM   6259 N N   . ASN B 1 261 ? -52.234 38.748 36.603  1.00 17.82 ? 261 ASN B N   1 
ATOM   6260 C CA  . ASN B 1 261 ? -52.690 37.781 37.596  1.00 18.21 ? 261 ASN B CA  1 
ATOM   6261 C C   . ASN B 1 261 ? -52.634 36.364 37.037  1.00 23.68 ? 261 ASN B C   1 
ATOM   6262 O O   . ASN B 1 261 ? -52.153 35.439 37.703  1.00 21.77 ? 261 ASN B O   1 
ATOM   6263 C CB  . ASN B 1 261 ? -54.102 38.132 38.053  1.00 21.21 ? 261 ASN B CB  1 
ATOM   6264 C CG  . ASN B 1 261 ? -54.138 39.437 38.828  1.00 20.99 ? 261 ASN B CG  1 
ATOM   6265 O OD1 . ASN B 1 261 ? -53.123 39.837 39.425  1.00 21.03 ? 261 ASN B OD1 1 
ATOM   6266 N ND2 . ASN B 1 261 ? -55.282 40.129 38.797  1.00 21.69 ? 261 ASN B ND2 1 
ATOM   6267 N N   . GLU B 1 262 ? -53.066 36.188 35.786  1.00 19.64 ? 262 GLU B N   1 
ATOM   6268 C CA  . GLU B 1 262 ? -53.099 34.848 35.201  1.00 21.16 ? 262 GLU B CA  1 
ATOM   6269 C C   . GLU B 1 262 ? -51.697 34.306 34.920  1.00 23.21 ? 262 GLU B C   1 
ATOM   6270 O O   . GLU B 1 262 ? -51.442 33.111 35.132  1.00 17.25 ? 262 GLU B O   1 
ATOM   6271 C CB  . GLU B 1 262 ? -53.948 34.862 33.936  1.00 19.77 ? 262 GLU B CB  1 
ATOM   6272 C CG  . GLU B 1 262 ? -55.427 35.044 34.207  1.00 27.44 ? 262 GLU B CG  1 
ATOM   6273 C CD  . GLU B 1 262 ? -56.235 34.984 32.928  1.00 40.51 ? 262 GLU B CD  1 
ATOM   6274 O OE1 . GLU B 1 262 ? -55.879 34.171 32.045  1.00 33.49 ? 262 GLU B OE1 1 
ATOM   6275 O OE2 . GLU B 1 262 ? -57.212 35.758 32.807  1.00 51.22 ? 262 GLU B OE2 1 
ATOM   6276 N N   . ALA B 1 263 ? -50.772 35.162 34.462  1.00 19.30 ? 263 ALA B N   1 
ATOM   6277 C CA  . ALA B 1 263 ? -49.397 34.715 34.236  1.00 18.84 ? 263 ALA B CA  1 
ATOM   6278 C C   . ALA B 1 263 ? -48.713 34.325 35.542  1.00 20.02 ? 263 ALA B C   1 
ATOM   6279 O O   . ALA B 1 263 ? -47.993 33.323 35.594  1.00 20.54 ? 263 ALA B O   1 
ATOM   6280 C CB  . ALA B 1 263 ? -48.600 35.802 33.513  1.00 15.03 ? 263 ALA B CB  1 
ATOM   6281 N N   . LEU B 1 264 ? -48.935 35.094 36.615  1.00 16.17 ? 264 LEU B N   1 
ATOM   6282 C CA  . LEU B 1 264 ? -48.351 34.730 37.902  1.00 22.74 ? 264 LEU B CA  1 
ATOM   6283 C C   . LEU B 1 264 ? -48.866 33.376 38.380  1.00 24.21 ? 264 LEU B C   1 
ATOM   6284 O O   . LEU B 1 264 ? -48.095 32.569 38.919  1.00 22.23 ? 264 LEU B O   1 
ATOM   6285 C CB  . LEU B 1 264 ? -48.626 35.825 38.932  1.00 19.02 ? 264 LEU B CB  1 
ATOM   6286 C CG  . LEU B 1 264 ? -47.834 37.104 38.645  1.00 19.30 ? 264 LEU B CG  1 
ATOM   6287 C CD1 . LEU B 1 264 ? -48.366 38.275 39.460  1.00 20.89 ? 264 LEU B CD1 1 
ATOM   6288 C CD2 . LEU B 1 264 ? -46.366 36.886 38.947  1.00 32.64 ? 264 LEU B CD2 1 
ATOM   6289 N N   . GLU B 1 265 ? -50.167 33.096 38.176  1.00 17.58 ? 265 GLU B N   1 
ATOM   6290 C CA  . GLU B 1 265 ? -50.709 31.785 38.535  1.00 23.19 ? 265 GLU B CA  1 
ATOM   6291 C C   . GLU B 1 265 ? -50.082 30.671 37.703  1.00 20.75 ? 265 GLU B C   1 
ATOM   6292 O O   . GLU B 1 265 ? -49.832 29.578 38.219  1.00 20.94 ? 265 GLU B O   1 
ATOM   6293 C CB  . GLU B 1 265 ? -52.233 31.775 38.369  1.00 31.57 ? 265 GLU B CB  1 
ATOM   6294 C CG  . GLU B 1 265 ? -52.863 30.380 38.469  1.00 41.78 ? 265 GLU B CG  1 
ATOM   6295 C CD  . GLU B 1 265 ? -53.069 29.934 39.915  1.00 45.43 ? 265 GLU B CD  1 
ATOM   6296 O OE1 . GLU B 1 265 ? -53.066 30.812 40.804  1.00 39.47 ? 265 GLU B OE1 1 
ATOM   6297 O OE2 . GLU B 1 265 ? -53.239 28.713 40.156  1.00 44.64 ? 265 GLU B OE2 1 
ATOM   6298 N N   . LEU B 1 266 ? -49.833 30.919 36.409  1.00 24.67 ? 266 LEU B N   1 
ATOM   6299 C CA  . LEU B 1 266 ? -49.160 29.919 35.581  1.00 14.75 ? 266 LEU B CA  1 
ATOM   6300 C C   . LEU B 1 266 ? -47.751 29.632 36.100  1.00 15.39 ? 266 LEU B C   1 
ATOM   6301 O O   . LEU B 1 266 ? -47.368 28.467 36.243  1.00 19.36 ? 266 LEU B O   1 
ATOM   6302 C CB  . LEU B 1 266 ? -49.112 30.373 34.117  1.00 15.46 ? 266 LEU B CB  1 
ATOM   6303 C CG  . LEU B 1 266 ? -48.304 29.502 33.140  1.00 18.15 ? 266 LEU B CG  1 
ATOM   6304 C CD1 . LEU B 1 266 ? -48.811 28.063 33.095  1.00 21.52 ? 266 LEU B CD1 1 
ATOM   6305 C CD2 . LEU B 1 266 ? -48.283 30.100 31.732  1.00 18.46 ? 266 LEU B CD2 1 
ATOM   6306 N N   . TYR B 1 267 ? -46.959 30.677 36.368  1.00 16.92 ? 267 TYR B N   1 
ATOM   6307 C CA  . TYR B 1 267 ? -45.603 30.454 36.878  1.00 16.19 ? 267 TYR B CA  1 
ATOM   6308 C C   . TYR B 1 267 ? -45.641 29.643 38.173  1.00 19.30 ? 267 TYR B C   1 
ATOM   6309 O O   . TYR B 1 267 ? -44.897 28.669 38.337  1.00 19.00 ? 267 TYR B O   1 
ATOM   6310 C CB  . TYR B 1 267 ? -44.874 31.789 37.079  1.00 17.15 ? 267 TYR B CB  1 
ATOM   6311 C CG  . TYR B 1 267 ? -44.440 32.483 35.783  1.00 15.07 ? 267 TYR B CG  1 
ATOM   6312 C CD1 . TYR B 1 267 ? -43.524 31.896 34.927  1.00 20.99 ? 267 TYR B CD1 1 
ATOM   6313 C CD2 . TYR B 1 267 ? -44.939 33.738 35.452  1.00 19.25 ? 267 TYR B CD2 1 
ATOM   6314 C CE1 . TYR B 1 267 ? -43.116 32.546 33.746  1.00 21.74 ? 267 TYR B CE1 1 
ATOM   6315 C CE2 . TYR B 1 267 ? -44.548 34.390 34.300  1.00 14.83 ? 267 TYR B CE2 1 
ATOM   6316 C CZ  . TYR B 1 267 ? -43.648 33.781 33.441  1.00 22.37 ? 267 TYR B CZ  1 
ATOM   6317 O OH  . TYR B 1 267 ? -43.275 34.429 32.288  1.00 18.37 ? 267 TYR B OH  1 
ATOM   6318 N N   . TYR B 1 268 ? -46.543 30.003 39.086  1.00 18.98 ? 268 TYR B N   1 
ATOM   6319 C CA  . TYR B 1 268 ? -46.691 29.226 40.310  1.00 20.14 ? 268 TYR B CA  1 
ATOM   6320 C C   . TYR B 1 268 ? -47.049 27.773 40.010  1.00 18.70 ? 268 TYR B C   1 
ATOM   6321 O O   . TYR B 1 268 ? -46.463 26.848 40.581  1.00 21.34 ? 268 TYR B O   1 
ATOM   6322 C CB  . TYR B 1 268 ? -47.742 29.866 41.207  1.00 19.87 ? 268 TYR B CB  1 
ATOM   6323 C CG  . TYR B 1 268 ? -48.378 28.887 42.172  1.00 27.10 ? 268 TYR B CG  1 
ATOM   6324 C CD1 . TYR B 1 268 ? -47.682 28.421 43.279  1.00 25.23 ? 268 TYR B CD1 1 
ATOM   6325 C CD2 . TYR B 1 268 ? -49.667 28.436 41.968  1.00 27.81 ? 268 TYR B CD2 1 
ATOM   6326 C CE1 . TYR B 1 268 ? -48.250 27.532 44.153  1.00 23.37 ? 268 TYR B CE1 1 
ATOM   6327 C CE2 . TYR B 1 268 ? -50.260 27.543 42.853  1.00 37.08 ? 268 TYR B CE2 1 
ATOM   6328 C CZ  . TYR B 1 268 ? -49.540 27.091 43.937  1.00 33.07 ? 268 TYR B CZ  1 
ATOM   6329 O OH  . TYR B 1 268 ? -50.107 26.199 44.827  1.00 34.56 ? 268 TYR B OH  1 
ATOM   6330 N N   . GLU B 1 269 ? -48.011 27.545 39.105  1.00 18.99 ? 269 GLU B N   1 
ATOM   6331 C CA  . GLU B 1 269 ? -48.436 26.177 38.815  1.00 22.60 ? 269 GLU B CA  1 
ATOM   6332 C C   . GLU B 1 269 ? -47.315 25.345 38.211  1.00 20.99 ? 269 GLU B C   1 
ATOM   6333 O O   . GLU B 1 269 ? -47.292 24.125 38.390  1.00 25.21 ? 269 GLU B O   1 
ATOM   6334 C CB  . GLU B 1 269 ? -49.634 26.190 37.873  1.00 25.72 ? 269 GLU B CB  1 
ATOM   6335 C CG  . GLU B 1 269 ? -50.927 26.488 38.598  1.00 34.22 ? 269 GLU B CG  1 
ATOM   6336 C CD  . GLU B 1 269 ? -52.088 26.613 37.648  1.00 52.78 ? 269 GLU B CD  1 
ATOM   6337 O OE1 . GLU B 1 269 ? -51.887 26.339 36.442  1.00 55.93 ? 269 GLU B OE1 1 
ATOM   6338 O OE2 . GLU B 1 269 ? -53.196 26.973 38.108  1.00 54.71 ? 269 GLU B OE2 1 
ATOM   6339 N N   . LYS B 1 270 ? -46.386 25.976 37.493  1.00 21.26 ? 270 LYS B N   1 
ATOM   6340 C CA  . LYS B 1 270 ? -45.249 25.291 36.896  1.00 22.59 ? 270 LYS B CA  1 
ATOM   6341 C C   . LYS B 1 270 ? -44.027 25.228 37.819  1.00 22.28 ? 270 LYS B C   1 
ATOM   6342 O O   . LYS B 1 270 ? -42.933 24.875 37.361  1.00 22.72 ? 270 LYS B O   1 
ATOM   6343 C CB  . LYS B 1 270 ? -44.878 25.968 35.584  1.00 23.38 ? 270 LYS B CB  1 
ATOM   6344 C CG  . LYS B 1 270 ? -45.937 25.849 34.505  1.00 25.98 ? 270 LYS B CG  1 
ATOM   6345 C CD  . LYS B 1 270 ? -46.403 24.410 34.324  1.00 42.63 ? 270 LYS B CD  1 
ATOM   6346 C CE  . LYS B 1 270 ? -47.533 24.329 33.309  1.00 47.33 ? 270 LYS B CE  1 
ATOM   6347 N NZ  . LYS B 1 270 ? -48.607 23.348 33.678  1.00 55.58 ? 270 LYS B NZ  1 
ATOM   6348 N N   . GLY B 1 271 ? -44.184 25.549 39.100  1.00 21.38 ? 271 GLY B N   1 
ATOM   6349 C CA  . GLY B 1 271 ? -43.130 25.334 40.065  1.00 20.73 ? 271 GLY B CA  1 
ATOM   6350 C C   . GLY B 1 271 ? -42.161 26.474 40.274  1.00 22.54 ? 271 GLY B C   1 
ATOM   6351 O O   . GLY B 1 271 ? -41.136 26.272 40.936  1.00 21.94 ? 271 GLY B O   1 
ATOM   6352 N N   . ILE B 1 272 ? -42.438 27.656 39.733  1.00 19.25 ? 272 ILE B N   1 
ATOM   6353 C CA  . ILE B 1 272 ? -41.589 28.820 39.951  1.00 18.44 ? 272 ILE B CA  1 
ATOM   6354 C C   . ILE B 1 272 ? -41.902 29.400 41.322  1.00 19.81 ? 272 ILE B C   1 
ATOM   6355 O O   . ILE B 1 272 ? -43.069 29.642 41.658  1.00 23.01 ? 272 ILE B O   1 
ATOM   6356 C CB  . ILE B 1 272 ? -41.806 29.869 38.846  1.00 18.44 ? 272 ILE B CB  1 
ATOM   6357 C CG1 . ILE B 1 272 ? -41.612 29.258 37.449  1.00 21.72 ? 272 ILE B CG1 1 
ATOM   6358 C CG2 . ILE B 1 272 ? -40.946 31.133 39.109  1.00 19.13 ? 272 ILE B CG2 1 
ATOM   6359 C CD1 . ILE B 1 272 ? -40.361 28.448 37.254  1.00 22.98 ? 272 ILE B CD1 1 
ATOM   6360 N N   . ASN B 1 273 ? -40.857 29.593 42.127  1.00 17.87 ? 273 ASN B N   1 
ATOM   6361 C CA  . ASN B 1 273 ? -40.988 30.106 43.480  1.00 20.77 ? 273 ASN B CA  1 
ATOM   6362 C C   . ASN B 1 273 ? -40.781 31.610 43.571  1.00 20.38 ? 273 ASN B C   1 
ATOM   6363 O O   . ASN B 1 273 ? -41.325 32.237 44.486  1.00 21.35 ? 273 ASN B O   1 
ATOM   6364 C CB  . ASN B 1 273 ? -39.982 29.401 44.407  1.00 23.49 ? 273 ASN B CB  1 
ATOM   6365 C CG  . ASN B 1 273 ? -40.316 27.929 44.637  1.00 41.69 ? 273 ASN B CG  1 
ATOM   6366 O OD1 . ASN B 1 273 ? -41.489 27.529 44.647  1.00 41.31 ? 273 ASN B OD1 1 
ATOM   6367 N ND2 . ASN B 1 273 ? -39.282 27.120 44.839  1.00 53.29 ? 273 ASN B ND2 1 
ATOM   6368 N N   A MET B 1 274 ? -39.993 32.201 42.674  0.58 21.45 ? 274 MET B N   1 
ATOM   6369 N N   B MET B 1 274 ? -40.050 32.203 42.630  0.42 21.91 ? 274 MET B N   1 
ATOM   6370 C CA  A MET B 1 274 ? -39.799 33.641 42.683  0.58 20.37 ? 274 MET B CA  1 
ATOM   6371 C CA  B MET B 1 274 ? -39.759 33.626 42.684  0.42 20.65 ? 274 MET B CA  1 
ATOM   6372 C C   A MET B 1 274 ? -39.571 34.139 41.264  0.58 21.31 ? 274 MET B C   1 
ATOM   6373 C C   B MET B 1 274 ? -39.521 34.160 41.279  0.42 21.10 ? 274 MET B C   1 
ATOM   6374 O O   A MET B 1 274 ? -38.975 33.451 40.432  0.58 19.46 ? 274 MET B O   1 
ATOM   6375 O O   B MET B 1 274 ? -38.871 33.504 40.461  0.42 20.48 ? 274 MET B O   1 
ATOM   6376 C CB  A MET B 1 274 ? -38.620 34.064 43.567  0.58 18.72 ? 274 MET B CB  1 
ATOM   6377 C CB  B MET B 1 274 ? -38.539 33.891 43.567  0.42 18.96 ? 274 MET B CB  1 
ATOM   6378 C CG  A MET B 1 274 ? -38.431 35.588 43.666  0.58 18.30 ? 274 MET B CG  1 
ATOM   6379 C CG  B MET B 1 274 ? -38.406 35.323 44.048  0.42 20.05 ? 274 MET B CG  1 
ATOM   6380 S SD  A MET B 1 274 ? -37.255 36.246 42.450  0.58 23.27 ? 274 MET B SD  1 
ATOM   6381 S SD  B MET B 1 274 ? -36.758 35.602 44.707  0.42 21.46 ? 274 MET B SD  1 
ATOM   6382 C CE  A MET B 1 274 ? -35.724 35.803 43.272  0.58 23.91 ? 274 MET B CE  1 
ATOM   6383 C CE  B MET B 1 274 ? -35.851 35.931 43.200  0.42 23.35 ? 274 MET B CE  1 
ATOM   6384 N N   . LEU B 1 275 ? -40.059 35.350 41.004  1.00 18.42 ? 275 LEU B N   1 
ATOM   6385 C CA  . LEU B 1 275 ? -39.750 36.078 39.786  1.00 13.11 ? 275 LEU B CA  1 
ATOM   6386 C C   . LEU B 1 275 ? -39.582 37.540 40.177  1.00 15.75 ? 275 LEU B C   1 
ATOM   6387 O O   . LEU B 1 275 ? -39.856 37.938 41.320  1.00 15.78 ? 275 LEU B O   1 
ATOM   6388 C CB  . LEU B 1 275 ? -40.834 35.881 38.729  1.00 15.12 ? 275 LEU B CB  1 
ATOM   6389 C CG  . LEU B 1 275 ? -42.287 36.217 39.045  1.00 23.08 ? 275 LEU B CG  1 
ATOM   6390 C CD1 . LEU B 1 275 ? -42.534 37.710 38.957  1.00 20.65 ? 275 LEU B CD1 1 
ATOM   6391 C CD2 . LEU B 1 275 ? -43.165 35.481 38.053  1.00 24.34 ? 275 LEU B CD2 1 
ATOM   6392 N N   . ALA B 1 276 ? -39.130 38.354 39.229  1.00 14.89 ? 276 ALA B N   1 
ATOM   6393 C CA  . ALA B 1 276 ? -39.153 39.794 39.432  1.00 15.56 ? 276 ALA B CA  1 
ATOM   6394 C C   . ALA B 1 276 ? -39.973 40.436 38.322  1.00 14.99 ? 276 ALA B C   1 
ATOM   6395 O O   . ALA B 1 276 ? -40.164 39.853 37.251  1.00 16.15 ? 276 ALA B O   1 
ATOM   6396 C CB  . ALA B 1 276 ? -37.738 40.403 39.452  1.00 19.22 ? 276 ALA B CB  1 
ATOM   6397 N N   . THR B 1 277 ? -40.466 41.640 38.587  1.00 16.68 ? 277 THR B N   1 
ATOM   6398 C CA  . THR B 1 277 ? -41.105 42.444 37.542  1.00 15.22 ? 277 THR B CA  1 
ATOM   6399 C C   . THR B 1 277 ? -40.718 43.901 37.788  1.00 17.67 ? 277 THR B C   1 
ATOM   6400 O O   . THR B 1 277 ? -39.718 44.194 38.453  1.00 17.52 ? 277 THR B O   1 
ATOM   6401 C CB  . THR B 1 277 ? -42.625 42.185 37.481  1.00 18.58 ? 277 THR B CB  1 
ATOM   6402 O OG1 . THR B 1 277 ? -43.195 42.970 36.426  1.00 17.07 ? 277 THR B OG1 1 
ATOM   6403 C CG2 . THR B 1 277 ? -43.309 42.523 38.782  1.00 15.71 ? 277 THR B CG2 1 
ATOM   6404 N N   . ASP B 1 278 ? -41.493 44.839 37.235  1.00 16.30 ? 278 ASP B N   1 
ATOM   6405 C CA  . ASP B 1 278 ? -41.067 46.230 37.173  1.00 15.45 ? 278 ASP B CA  1 
ATOM   6406 C C   . ASP B 1 278 ? -41.762 47.097 38.208  1.00 17.01 ? 278 ASP B C   1 
ATOM   6407 O O   . ASP B 1 278 ? -42.908 46.853 38.590  1.00 19.10 ? 278 ASP B O   1 
ATOM   6408 C CB  . ASP B 1 278 ? -41.329 46.830 35.794  1.00 17.00 ? 278 ASP B CB  1 
ATOM   6409 C CG  . ASP B 1 278 ? -40.729 48.226 35.654  1.00 23.45 ? 278 ASP B CG  1 
ATOM   6410 O OD1 . ASP B 1 278 ? -39.563 48.426 36.048  1.00 22.35 ? 278 ASP B OD1 1 
ATOM   6411 O OD2 . ASP B 1 278 ? -41.430 49.139 35.177  1.00 25.41 ? 278 ASP B OD2 1 
ATOM   6412 N N   . GLU B 1 279 ? -41.047 48.149 38.623  1.00 23.48 ? 279 GLU B N   1 
ATOM   6413 C CA  . GLU B 1 279 ? -41.583 49.111 39.573  1.00 25.99 ? 279 GLU B CA  1 
ATOM   6414 C C   . GLU B 1 279 ? -42.850 49.792 39.056  1.00 23.84 ? 279 GLU B C   1 
ATOM   6415 O O   . GLU B 1 279 ? -43.744 50.104 39.848  1.00 20.07 ? 279 GLU B O   1 
ATOM   6416 C CB  . GLU B 1 279 ? -40.507 50.151 39.911  1.00 23.00 ? 279 GLU B CB  1 
ATOM   6417 C CG  . GLU B 1 279 ? -40.847 50.974 41.122  1.00 26.66 ? 279 GLU B CG  1 
ATOM   6418 C CD  . GLU B 1 279 ? -39.680 51.801 41.628  1.00 35.92 ? 279 GLU B CD  1 
ATOM   6419 O OE1 . GLU B 1 279 ? -38.549 51.611 41.134  1.00 25.02 ? 279 GLU B OE1 1 
ATOM   6420 O OE2 . GLU B 1 279 ? -39.902 52.642 42.529  1.00 43.06 ? 279 GLU B OE2 1 
ATOM   6421 N N   . VAL B 1 280 ? -42.963 50.027 37.749  1.00 20.85 ? 280 VAL B N   1 
ATOM   6422 C CA  . VAL B 1 280 ? -44.179 50.676 37.276  1.00 22.06 ? 280 VAL B CA  1 
ATOM   6423 C C   . VAL B 1 280 ? -45.382 49.761 37.488  1.00 23.01 ? 280 VAL B C   1 
ATOM   6424 O O   . VAL B 1 280 ? -46.478 50.232 37.809  1.00 27.19 ? 280 VAL B O   1 
ATOM   6425 C CB  . VAL B 1 280 ? -44.037 51.122 35.810  1.00 22.58 ? 280 VAL B CB  1 
ATOM   6426 C CG1 . VAL B 1 280 ? -45.379 51.654 35.271  1.00 22.58 ? 280 VAL B CG1 1 
ATOM   6427 C CG2 . VAL B 1 280 ? -42.990 52.210 35.692  1.00 24.72 ? 280 VAL B CG2 1 
ATOM   6428 N N   . ILE B 1 281 ? -45.200 48.448 37.347  1.00 24.45 ? 281 ILE B N   1 
ATOM   6429 C CA  . ILE B 1 281 ? -46.285 47.512 37.660  1.00 24.96 ? 281 ILE B CA  1 
ATOM   6430 C C   . ILE B 1 281 ? -46.714 47.663 39.115  1.00 24.62 ? 281 ILE B C   1 
ATOM   6431 O O   . ILE B 1 281 ? -47.907 47.683 39.432  1.00 22.21 ? 281 ILE B O   1 
ATOM   6432 C CB  . ILE B 1 281 ? -45.861 46.061 37.366  1.00 29.46 ? 281 ILE B CB  1 
ATOM   6433 C CG1 . ILE B 1 281 ? -45.313 45.927 35.940  1.00 32.02 ? 281 ILE B CG1 1 
ATOM   6434 C CG2 . ILE B 1 281 ? -47.028 45.117 37.626  1.00 24.25 ? 281 ILE B CG2 1 
ATOM   6435 C CD1 . ILE B 1 281 ? -46.295 46.203 34.903  1.00 32.26 ? 281 ILE B CD1 1 
ATOM   6436 N N   . LEU B 1 282 ? -45.744 47.747 40.025  1.00 23.08 ? 282 LEU B N   1 
ATOM   6437 C CA  . LEU B 1 282 ? -46.078 47.916 41.437  1.00 28.03 ? 282 LEU B CA  1 
ATOM   6438 C C   . LEU B 1 282 ? -46.872 49.196 41.660  1.00 22.41 ? 282 LEU B C   1 
ATOM   6439 O O   . LEU B 1 282 ? -47.924 49.182 42.311  1.00 24.79 ? 282 LEU B O   1 
ATOM   6440 C CB  . LEU B 1 282 ? -44.803 47.930 42.290  1.00 23.12 ? 282 LEU B CB  1 
ATOM   6441 C CG  . LEU B 1 282 ? -45.055 48.099 43.791  1.00 23.54 ? 282 LEU B CG  1 
ATOM   6442 C CD1 . LEU B 1 282 ? -45.932 46.964 44.315  1.00 24.56 ? 282 LEU B CD1 1 
ATOM   6443 C CD2 . LEU B 1 282 ? -43.723 48.130 44.552  1.00 22.23 ? 282 LEU B CD2 1 
ATOM   6444 N N   . LYS B 1 283 ? -46.377 50.315 41.118  1.00 20.54 ? 283 LYS B N   1 
ATOM   6445 C CA  . LYS B 1 283 ? -47.062 51.601 41.270  1.00 23.50 ? 283 LYS B CA  1 
ATOM   6446 C C   . LYS B 1 283 ? -48.475 51.547 40.706  1.00 28.05 ? 283 LYS B C   1 
ATOM   6447 O O   . LYS B 1 283 ? -49.401 52.150 41.262  1.00 25.28 ? 283 LYS B O   1 
ATOM   6448 C CB  . LYS B 1 283 ? -46.277 52.707 40.557  1.00 32.13 ? 283 LYS B CB  1 
ATOM   6449 C CG  . LYS B 1 283 ? -44.901 53.001 41.143  1.00 40.79 ? 283 LYS B CG  1 
ATOM   6450 C CD  . LYS B 1 283 ? -44.908 52.892 42.666  1.00 52.00 ? 283 LYS B CD  1 
ATOM   6451 C CE  . LYS B 1 283 ? -43.493 52.956 43.236  1.00 48.63 ? 283 LYS B CE  1 
ATOM   6452 N NZ  . LYS B 1 283 ? -42.615 53.845 42.422  1.00 54.24 ? 283 LYS B NZ  1 
ATOM   6453 N N   . ASN B 1 284 ? -48.656 50.838 39.586  1.00 18.97 ? 284 ASN B N   1 
ATOM   6454 C CA  . ASN B 1 284 ? -49.970 50.716 38.976  1.00 26.19 ? 284 ASN B CA  1 
ATOM   6455 C C   . ASN B 1 284 ? -50.908 49.844 39.802  1.00 27.66 ? 284 ASN B C   1 
ATOM   6456 O O   . ASN B 1 284 ? -52.125 49.903 39.597  1.00 24.74 ? 284 ASN B O   1 
ATOM   6457 C CB  . ASN B 1 284 ? -49.843 50.130 37.561  1.00 24.90 ? 284 ASN B CB  1 
ATOM   6458 C CG  . ASN B 1 284 ? -49.327 51.137 36.525  1.00 30.71 ? 284 ASN B CG  1 
ATOM   6459 O OD1 . ASN B 1 284 ? -49.323 52.358 36.741  1.00 26.42 ? 284 ASN B OD1 1 
ATOM   6460 N ND2 . ASN B 1 284 ? -48.911 50.612 35.370  1.00 28.33 ? 284 ASN B ND2 1 
ATOM   6461 N N   . SER B 1 285 ? -50.381 49.023 40.709  1.00 27.84 ? 285 SER B N   1 
ATOM   6462 C CA  . SER B 1 285 ? -51.203 48.019 41.377  1.00 28.16 ? 285 SER B CA  1 
ATOM   6463 C C   . SER B 1 285 ? -51.482 48.313 42.842  1.00 26.65 ? 285 SER B C   1 
ATOM   6464 O O   . SER B 1 285 ? -52.539 47.920 43.348  1.00 26.92 ? 285 SER B O   1 
ATOM   6465 C CB  . SER B 1 285 ? -50.548 46.640 41.248  1.00 26.76 ? 285 SER B CB  1 
ATOM   6466 O OG  . SER B 1 285 ? -50.174 46.414 39.892  1.00 23.60 ? 285 SER B OG  1 
ATOM   6467 N N   . VAL B 1 286 ? -50.567 48.999 43.521  1.00 21.72 ? 286 VAL B N   1 
ATOM   6468 C CA  . VAL B 1 286 ? -50.675 49.312 44.940  1.00 31.86 ? 286 VAL B CA  1 
ATOM   6469 C C   . VAL B 1 286 ? -50.339 50.782 45.111  1.00 32.73 ? 286 VAL B C   1 
ATOM   6470 O O   . VAL B 1 286 ? -49.346 51.265 44.558  1.00 41.80 ? 286 VAL B O   1 
ATOM   6471 C CB  . VAL B 1 286 ? -49.730 48.429 45.792  1.00 31.79 ? 286 VAL B CB  1 
ATOM   6472 C CG1 . VAL B 1 286 ? -50.022 48.608 47.275  1.00 39.39 ? 286 VAL B CG1 1 
ATOM   6473 C CG2 . VAL B 1 286 ? -49.863 46.955 45.395  1.00 27.56 ? 286 VAL B CG2 1 
ATOM   6474 N N   . GLU B 1 287 ? -51.165 51.494 45.869  1.00 35.60 ? 287 GLU B N   1 
ATOM   6475 C CA  . GLU B 1 287 ? -50.938 52.920 46.072  1.00 45.95 ? 287 GLU B CA  1 
ATOM   6476 C C   . GLU B 1 287 ? -49.603 53.186 46.766  1.00 42.69 ? 287 GLU B C   1 
ATOM   6477 O O   . GLU B 1 287 ? -49.403 52.795 47.922  1.00 35.31 ? 287 GLU B O   1 
ATOM   6478 C CB  . GLU B 1 287 ? -52.092 53.537 46.861  1.00 52.07 ? 287 GLU B CB  1 
ATOM   6479 C CG  . GLU B 1 287 ? -52.569 52.742 48.065  1.00 58.24 ? 287 GLU B CG  1 
ATOM   6480 C CD  . GLU B 1 287 ? -53.903 53.258 48.597  1.00 66.63 ? 287 GLU B CD  1 
ATOM   6481 O OE1 . GLU B 1 287 ? -54.809 53.530 47.771  1.00 65.65 ? 287 GLU B OE1 1 
ATOM   6482 O OE2 . GLU B 1 287 ? -54.040 53.405 49.834  1.00 69.07 ? 287 GLU B OE2 1 
ATOM   6483 N N   . ARG B 1 288 ? -48.693 53.849 46.042  1.00 49.13 ? 288 ARG B N   1 
ATOM   6484 C CA  . ARG B 1 288 ? -47.300 54.114 46.414  1.00 49.35 ? 288 ARG B CA  1 
ATOM   6485 C C   . ARG B 1 288 ? -46.710 53.102 47.389  1.00 54.55 ? 288 ARG B C   1 
ATOM   6486 O O   . ARG B 1 288 ? -46.537 53.387 48.579  1.00 57.80 ? 288 ARG B O   1 
ATOM   6487 C CB  . ARG B 1 288 ? -47.156 55.531 46.967  1.00 52.32 ? 288 ARG B CB  1 
ATOM   6488 C CG  . ARG B 1 288 ? -46.754 56.512 45.870  1.00 58.56 ? 288 ARG B CG  1 
ATOM   6489 C CD  . ARG B 1 288 ? -46.526 57.914 46.387  1.00 58.39 ? 288 ARG B CD  1 
ATOM   6490 N NE  . ARG B 1 288 ? -47.330 58.872 45.636  1.00 66.86 ? 288 ARG B NE  1 
ATOM   6491 C CZ  . ARG B 1 288 ? -47.070 60.172 45.534  1.00 67.70 ? 288 ARG B CZ  1 
ATOM   6492 N NH1 . ARG B 1 288 ? -46.006 60.688 46.125  1.00 68.45 ? 288 ARG B NH1 1 
ATOM   6493 N NH2 . ARG B 1 288 ? -47.887 60.957 44.835  1.00 69.50 ? 288 ARG B NH2 1 
ATOM   6494 N N   . ALA B 1 289 ? -46.406 51.917 46.875  1.00 48.62 ? 289 ALA B N   1 
ATOM   6495 C CA  . ALA B 1 289 ? -45.724 50.871 47.612  1.00 47.02 ? 289 ALA B CA  1 
ATOM   6496 C C   . ALA B 1 289 ? -44.228 50.940 47.328  1.00 35.93 ? 289 ALA B C   1 
ATOM   6497 O O   . ALA B 1 289 ? -43.774 51.582 46.377  1.00 42.82 ? 289 ALA B O   1 
ATOM   6498 C CB  . ALA B 1 289 ? -46.286 49.493 47.238  1.00 40.91 ? 289 ALA B CB  1 
ATOM   6499 N N   . SER B 1 290 ? -43.483 50.253 48.134  1.00 29.17 ? 290 SER B N   1 
ATOM   6500 C CA  . SER B 1 290 ? -42.022 50.319 48.133  1.00 26.82 ? 290 SER B CA  1 
ATOM   6501 C C   . SER B 1 290 ? -41.435 49.135 47.381  1.00 22.56 ? 290 SER B C   1 
ATOM   6502 O O   . SER B 1 290 ? -41.876 47.998 47.601  1.00 27.19 ? 290 SER B O   1 
ATOM   6503 C CB  . SER B 1 290 ? -41.502 50.317 49.564  1.00 25.96 ? 290 SER B CB  1 
ATOM   6504 O OG  . SER B 1 290 ? -40.181 49.805 49.626  1.00 31.79 ? 290 SER B OG  1 
ATOM   6505 N N   . PRO B 1 291 ? -40.453 49.324 46.500  1.00 24.90 ? 291 PRO B N   1 
ATOM   6506 C CA  . PRO B 1 291 ? -39.835 48.178 45.825  1.00 22.00 ? 291 PRO B CA  1 
ATOM   6507 C C   . PRO B 1 291 ? -38.795 47.454 46.664  1.00 15.20 ? 291 PRO B C   1 
ATOM   6508 O O   . PRO B 1 291 ? -38.099 46.585 46.139  1.00 22.64 ? 291 PRO B O   1 
ATOM   6509 C CB  . PRO B 1 291 ? -39.185 48.826 44.588  1.00 20.00 ? 291 PRO B CB  1 
ATOM   6510 C CG  . PRO B 1 291 ? -38.784 50.201 45.083  1.00 26.98 ? 291 PRO B CG  1 
ATOM   6511 C CD  . PRO B 1 291 ? -39.811 50.602 46.128  1.00 29.83 ? 291 PRO B CD  1 
ATOM   6512 N N   . TYR B 1 292 ? -38.672 47.772 47.952  1.00 15.85 ? 292 TYR B N   1 
ATOM   6513 C CA  . TYR B 1 292 ? -37.592 47.242 48.766  1.00 20.68 ? 292 TYR B CA  1 
ATOM   6514 C C   . TYR B 1 292 ? -38.022 46.056 49.616  1.00 15.13 ? 292 TYR B C   1 
ATOM   6515 O O   . TYR B 1 292 ? -37.230 45.577 50.431  1.00 17.87 ? 292 TYR B O   1 
ATOM   6516 C CB  . TYR B 1 292 ? -37.021 48.352 49.653  1.00 23.04 ? 292 TYR B CB  1 
ATOM   6517 C CG  . TYR B 1 292 ? -36.563 49.545 48.857  1.00 18.30 ? 292 TYR B CG  1 
ATOM   6518 C CD1 . TYR B 1 292 ? -35.826 49.383 47.700  1.00 20.04 ? 292 TYR B CD1 1 
ATOM   6519 C CD2 . TYR B 1 292 ? -36.879 50.836 49.269  1.00 28.23 ? 292 TYR B CD2 1 
ATOM   6520 C CE1 . TYR B 1 292 ? -35.422 50.477 46.960  1.00 26.17 ? 292 TYR B CE1 1 
ATOM   6521 C CE2 . TYR B 1 292 ? -36.473 51.934 48.546  1.00 26.22 ? 292 TYR B CE2 1 
ATOM   6522 C CZ  . TYR B 1 292 ? -35.755 51.752 47.398  1.00 32.37 ? 292 TYR B CZ  1 
ATOM   6523 O OH  . TYR B 1 292 ? -35.367 52.866 46.694  1.00 37.46 ? 292 TYR B OH  1 
ATOM   6524 N N   . LEU B 1 293 ? -39.240 45.560 49.418  1.00 20.21 ? 293 LEU B N   1 
ATOM   6525 C CA  . LEU B 1 293 ? -39.805 44.437 50.153  1.00 25.36 ? 293 LEU B CA  1 
ATOM   6526 C C   . LEU B 1 293 ? -39.772 43.176 49.291  1.00 18.17 ? 293 LEU B C   1 
ATOM   6527 O O   . LEU B 1 293 ? -39.707 43.237 48.059  1.00 19.79 ? 293 LEU B O   1 
ATOM   6528 C CB  . LEU B 1 293 ? -41.259 44.741 50.552  1.00 26.01 ? 293 LEU B CB  1 
ATOM   6529 C CG  . LEU B 1 293 ? -41.622 45.737 51.648  1.00 27.14 ? 293 LEU B CG  1 
ATOM   6530 C CD1 . LEU B 1 293 ? -41.007 47.113 51.458  1.00 37.77 ? 293 LEU B CD1 1 
ATOM   6531 C CD2 . LEU B 1 293 ? -43.140 45.838 51.734  1.00 24.73 ? 293 LEU B CD2 1 
ATOM   6532 N N   . ARG B 1 294 ? -39.855 42.020 49.950  1.00 21.19 ? 294 ARG B N   1 
ATOM   6533 C CA  . ARG B 1 294 ? -40.177 40.780 49.248  1.00 17.25 ? 294 ARG B CA  1 
ATOM   6534 C C   . ARG B 1 294 ? -41.683 40.596 49.287  1.00 18.01 ? 294 ARG B C   1 
ATOM   6535 O O   . ARG B 1 294 ? -42.269 40.468 50.375  1.00 21.22 ? 294 ARG B O   1 
ATOM   6536 C CB  . ARG B 1 294 ? -39.481 39.569 49.870  1.00 21.51 ? 294 ARG B CB  1 
ATOM   6537 C CG  . ARG B 1 294 ? -39.849 38.253 49.151  1.00 20.80 ? 294 ARG B CG  1 
ATOM   6538 C CD  . ARG B 1 294 ? -38.990 37.075 49.583  1.00 22.12 ? 294 ARG B CD  1 
ATOM   6539 N NE  . ARG B 1 294 ? -39.242 36.673 50.970  1.00 26.60 ? 294 ARG B NE  1 
ATOM   6540 C CZ  . ARG B 1 294 ? -38.288 36.610 51.895  1.00 29.03 ? 294 ARG B CZ  1 
ATOM   6541 N NH1 . ARG B 1 294 ? -37.040 36.928 51.581  1.00 26.39 ? 294 ARG B NH1 1 
ATOM   6542 N NH2 . ARG B 1 294 ? -38.583 36.233 53.133  1.00 34.51 ? 294 ARG B NH2 1 
ATOM   6543 N N   . TYR B 1 295 ? -42.316 40.589 48.116  1.00 18.44 ? 295 TYR B N   1 
ATOM   6544 C CA  . TYR B 1 295 ? -43.767 40.467 48.060  1.00 17.80 ? 295 TYR B CA  1 
ATOM   6545 C C   . TYR B 1 295 ? -44.176 39.016 47.849  1.00 23.89 ? 295 TYR B C   1 
ATOM   6546 O O   . TYR B 1 295 ? -43.441 38.217 47.255  1.00 20.72 ? 295 TYR B O   1 
ATOM   6547 C CB  . TYR B 1 295 ? -44.357 41.334 46.935  1.00 17.47 ? 295 TYR B CB  1 
ATOM   6548 C CG  . TYR B 1 295 ? -44.326 42.819 47.258  1.00 21.61 ? 295 TYR B CG  1 
ATOM   6549 C CD1 . TYR B 1 295 ? -43.196 43.593 46.979  1.00 17.97 ? 295 TYR B CD1 1 
ATOM   6550 C CD2 . TYR B 1 295 ? -45.420 43.447 47.847  1.00 20.46 ? 295 TYR B CD2 1 
ATOM   6551 C CE1 . TYR B 1 295 ? -43.165 44.944 47.281  1.00 15.92 ? 295 TYR B CE1 1 
ATOM   6552 C CE2 . TYR B 1 295 ? -45.397 44.791 48.150  1.00 19.15 ? 295 TYR B CE2 1 
ATOM   6553 C CZ  . TYR B 1 295 ? -44.272 45.534 47.863  1.00 20.57 ? 295 TYR B CZ  1 
ATOM   6554 O OH  . TYR B 1 295 ? -44.271 46.873 48.173  1.00 25.68 ? 295 TYR B OH  1 
ATOM   6555 N N   . TYR B 1 296 ? -45.362 38.678 48.361  1.00 23.41 ? 296 TYR B N   1 
ATOM   6556 C CA  . TYR B 1 296 ? -45.975 37.362 48.188  1.00 20.82 ? 296 TYR B CA  1 
ATOM   6557 C C   . TYR B 1 296 ? -47.285 37.560 47.445  1.00 18.31 ? 296 TYR B C   1 
ATOM   6558 O O   . TYR B 1 296 ? -48.245 38.108 47.999  1.00 24.94 ? 296 TYR B O   1 
ATOM   6559 C CB  . TYR B 1 296 ? -46.220 36.675 49.539  1.00 22.05 ? 296 TYR B CB  1 
ATOM   6560 C CG  . TYR B 1 296 ? -44.957 36.371 50.313  1.00 26.60 ? 296 TYR B CG  1 
ATOM   6561 C CD1 . TYR B 1 296 ? -43.889 35.736 49.706  1.00 33.59 ? 296 TYR B CD1 1 
ATOM   6562 C CD2 . TYR B 1 296 ? -44.838 36.712 51.657  1.00 40.66 ? 296 TYR B CD2 1 
ATOM   6563 C CE1 . TYR B 1 296 ? -42.724 35.446 50.411  1.00 31.79 ? 296 TYR B CE1 1 
ATOM   6564 C CE2 . TYR B 1 296 ? -43.678 36.434 52.367  1.00 45.66 ? 296 TYR B CE2 1 
ATOM   6565 C CZ  . TYR B 1 296 ? -42.622 35.798 51.729  1.00 44.38 ? 296 TYR B CZ  1 
ATOM   6566 O OH  . TYR B 1 296 ? -41.457 35.505 52.415  1.00 42.50 ? 296 TYR B OH  1 
ATOM   6567 N N   . PHE B 1 297 ? -47.324 37.118 46.192  1.00 17.52 ? 297 PHE B N   1 
ATOM   6568 C CA  . PHE B 1 297 ? -48.518 37.269 45.383  1.00 14.55 ? 297 PHE B CA  1 
ATOM   6569 C C   . PHE B 1 297 ? -49.489 36.164 45.778  1.00 16.47 ? 297 PHE B C   1 
ATOM   6570 O O   . PHE B 1 297 ? -49.243 34.978 45.505  1.00 17.41 ? 297 PHE B O   1 
ATOM   6571 C CB  . PHE B 1 297 ? -48.187 37.220 43.892  1.00 14.57 ? 297 PHE B CB  1 
ATOM   6572 C CG  . PHE B 1 297 ? -49.396 37.297 43.027  1.00 16.80 ? 297 PHE B CG  1 
ATOM   6573 C CD1 . PHE B 1 297 ? -50.044 38.505 42.842  1.00 18.59 ? 297 PHE B CD1 1 
ATOM   6574 C CD2 . PHE B 1 297 ? -49.895 36.157 42.408  1.00 15.56 ? 297 PHE B CD2 1 
ATOM   6575 C CE1 . PHE B 1 297 ? -51.195 38.574 42.033  1.00 17.07 ? 297 PHE B CE1 1 
ATOM   6576 C CE2 . PHE B 1 297 ? -51.014 36.218 41.601  1.00 20.64 ? 297 PHE B CE2 1 
ATOM   6577 C CZ  . PHE B 1 297 ? -51.676 37.430 41.424  1.00 20.30 ? 297 PHE B CZ  1 
ATOM   6578 N N   . ARG B 1 298 ? -50.563 36.553 46.470  1.00 15.97 ? 298 ARG B N   1 
ATOM   6579 C CA  . ARG B 1 298 ? -51.615 35.639 46.908  1.00 16.82 ? 298 ARG B CA  1 
ATOM   6580 C C   . ARG B 1 298 ? -51.073 34.502 47.774  1.00 19.19 ? 298 ARG B C   1 
ATOM   6581 O O   . ARG B 1 298 ? -51.661 33.422 47.836  1.00 25.58 ? 298 ARG B O   1 
ATOM   6582 C CB  . ARG B 1 298 ? -52.377 35.092 45.702  1.00 21.59 ? 298 ARG B CB  1 
ATOM   6583 C CG  . ARG B 1 298 ? -52.981 36.214 44.845  1.00 23.67 ? 298 ARG B CG  1 
ATOM   6584 C CD  . ARG B 1 298 ? -53.800 35.699 43.629  1.00 23.58 ? 298 ARG B CD  1 
ATOM   6585 N NE  . ARG B 1 298 ? -54.536 36.813 43.026  1.00 23.41 ? 298 ARG B NE  1 
ATOM   6586 C CZ  . ARG B 1 298 ? -55.290 36.745 41.930  1.00 26.37 ? 298 ARG B CZ  1 
ATOM   6587 N NH1 . ARG B 1 298 ? -55.446 35.609 41.265  1.00 24.56 ? 298 ARG B NH1 1 
ATOM   6588 N NH2 . ARG B 1 298 ? -55.898 37.841 41.501  1.00 27.00 ? 298 ARG B NH2 1 
ATOM   6589 N N   . GLU B 1 299 ? -49.952 34.736 48.447  1.00 20.92 ? 299 GLU B N   1 
ATOM   6590 C CA  . GLU B 1 299 ? -49.258 33.714 49.242  1.00 19.43 ? 299 GLU B CA  1 
ATOM   6591 C C   . GLU B 1 299 ? -48.892 32.475 48.424  1.00 24.78 ? 299 GLU B C   1 
ATOM   6592 O O   . GLU B 1 299 ? -48.772 31.382 48.987  1.00 25.11 ? 299 GLU B O   1 
ATOM   6593 C CB  . GLU B 1 299 ? -50.073 33.292 50.476  1.00 24.11 ? 299 GLU B CB  1 
ATOM   6594 C CG  . GLU B 1 299 ? -50.378 34.421 51.449  1.00 26.51 ? 299 GLU B CG  1 
ATOM   6595 C CD  . GLU B 1 299 ? -49.215 34.686 52.390  1.00 51.34 ? 299 GLU B CD  1 
ATOM   6596 O OE1 . GLU B 1 299 ? -48.221 33.910 52.341  1.00 46.25 ? 299 GLU B OE1 1 
ATOM   6597 O OE2 . GLU B 1 299 ? -49.326 35.612 53.218  1.00 62.26 ? 299 GLU B OE2 1 
ATOM   6598 N N   . LEU B 1 300 ? -48.696 32.623 47.110  1.00 18.06 ? 300 LEU B N   1 
ATOM   6599 C CA  . LEU B 1 300 ? -48.329 31.514 46.220  1.00 19.94 ? 300 LEU B CA  1 
ATOM   6600 C C   . LEU B 1 300 ? -46.911 31.599 45.675  1.00 24.63 ? 300 LEU B C   1 
ATOM   6601 O O   . LEU B 1 300 ? -46.228 30.576 45.553  1.00 26.16 ? 300 LEU B O   1 
ATOM   6602 C CB  . LEU B 1 300 ? -49.278 31.449 45.019  1.00 21.04 ? 300 LEU B CB  1 
ATOM   6603 C CG  . LEU B 1 300 ? -50.764 31.337 45.334  1.00 23.36 ? 300 LEU B CG  1 
ATOM   6604 C CD1 . LEU B 1 300 ? -51.582 31.458 44.048  1.00 28.08 ? 300 LEU B CD1 1 
ATOM   6605 C CD2 . LEU B 1 300 ? -51.033 30.000 46.035  1.00 18.33 ? 300 LEU B CD2 1 
ATOM   6606 N N   . ILE B 1 301 ? -46.457 32.791 45.311  1.00 20.55 ? 301 ILE B N   1 
ATOM   6607 C CA  . ILE B 1 301 ? -45.188 32.954 44.613  1.00 20.65 ? 301 ILE B CA  1 
ATOM   6608 C C   . ILE B 1 301 ? -44.575 34.266 45.074  1.00 18.89 ? 301 ILE B C   1 
ATOM   6609 O O   . ILE B 1 301 ? -45.286 35.241 45.314  1.00 22.60 ? 301 ILE B O   1 
ATOM   6610 C CB  . ILE B 1 301 ? -45.400 32.890 43.080  1.00 22.05 ? 301 ILE B CB  1 
ATOM   6611 C CG1 . ILE B 1 301 ? -44.065 32.998 42.334  1.00 19.66 ? 301 ILE B CG1 1 
ATOM   6612 C CG2 . ILE B 1 301 ? -46.405 33.971 42.603  1.00 23.29 ? 301 ILE B CG2 1 
ATOM   6613 C CD1 . ILE B 1 301 ? -44.195 32.843 40.817  1.00 23.60 ? 301 ILE B CD1 1 
ATOM   6614 N N   . SER B 1 302 ? -43.258 34.279 45.247  1.00 18.48 ? 302 SER B N   1 
ATOM   6615 C CA  . SER B 1 302 ? -42.584 35.489 45.690  1.00 13.89 ? 302 SER B CA  1 
ATOM   6616 C C   . SER B 1 302 ? -42.318 36.390 44.497  1.00 14.02 ? 302 SER B C   1 
ATOM   6617 O O   . SER B 1 302 ? -42.026 35.916 43.395  1.00 18.23 ? 302 SER B O   1 
ATOM   6618 C CB  . SER B 1 302 ? -41.281 35.146 46.413  1.00 27.26 ? 302 SER B CB  1 
ATOM   6619 O OG  . SER B 1 302 ? -41.535 34.445 47.628  1.00 27.64 ? 302 SER B OG  1 
ATOM   6620 N N   . VAL B 1 303 ? -42.457 37.695 44.709  1.00 14.02 ? 303 VAL B N   1 
ATOM   6621 C CA  . VAL B 1 303 ? -42.269 38.683 43.652  1.00 14.54 ? 303 VAL B CA  1 
ATOM   6622 C C   . VAL B 1 303 ? -41.387 39.804 44.196  1.00 14.23 ? 303 VAL B C   1 
ATOM   6623 O O   . VAL B 1 303 ? -41.655 40.352 45.272  1.00 18.66 ? 303 VAL B O   1 
ATOM   6624 C CB  . VAL B 1 303 ? -43.614 39.250 43.146  1.00 19.43 ? 303 VAL B CB  1 
ATOM   6625 C CG1 . VAL B 1 303 ? -43.394 40.295 42.059  1.00 14.98 ? 303 VAL B CG1 1 
ATOM   6626 C CG2 . VAL B 1 303 ? -44.506 38.127 42.615  1.00 17.62 ? 303 VAL B CG2 1 
ATOM   6627 N N   . PHE B 1 304 ? -40.353 40.158 43.440  1.00 15.78 ? 304 PHE B N   1 
ATOM   6628 C CA  . PHE B 1 304 ? -39.562 41.346 43.719  1.00 16.41 ? 304 PHE B CA  1 
ATOM   6629 C C   . PHE B 1 304 ? -39.792 42.350 42.605  1.00 16.45 ? 304 PHE B C   1 
ATOM   6630 O O   . PHE B 1 304 ? -39.882 41.976 41.439  1.00 19.29 ? 304 PHE B O   1 
ATOM   6631 C CB  . PHE B 1 304 ? -38.073 41.018 43.828  1.00 21.43 ? 304 PHE B CB  1 
ATOM   6632 C CG  . PHE B 1 304 ? -37.670 40.438 45.156  1.00 16.48 ? 304 PHE B CG  1 
ATOM   6633 C CD1 . PHE B 1 304 ? -37.505 41.248 46.255  1.00 17.91 ? 304 PHE B CD1 1 
ATOM   6634 C CD2 . PHE B 1 304 ? -37.427 39.082 45.282  1.00 17.97 ? 304 PHE B CD2 1 
ATOM   6635 C CE1 . PHE B 1 304 ? -37.112 40.714 47.481  1.00 17.90 ? 304 PHE B CE1 1 
ATOM   6636 C CE2 . PHE B 1 304 ? -37.024 38.542 46.483  1.00 15.25 ? 304 PHE B CE2 1 
ATOM   6637 C CZ  . PHE B 1 304 ? -36.869 39.359 47.596  1.00 18.63 ? 304 PHE B CZ  1 
ATOM   6638 N N   . PHE B 1 305 ? -39.946 43.611 42.974  1.00 18.40 ? 305 PHE B N   1 
ATOM   6639 C CA  . PHE B 1 305 ? -40.104 44.687 42.008  1.00 16.97 ? 305 PHE B CA  1 
ATOM   6640 C C   . PHE B 1 305 ? -38.765 45.392 41.881  1.00 15.53 ? 305 PHE B C   1 
ATOM   6641 O O   . PHE B 1 305 ? -38.210 45.859 42.880  1.00 17.44 ? 305 PHE B O   1 
ATOM   6642 C CB  . PHE B 1 305 ? -41.214 45.636 42.451  1.00 16.85 ? 305 PHE B CB  1 
ATOM   6643 C CG  . PHE B 1 305 ? -42.547 44.980 42.480  1.00 18.49 ? 305 PHE B CG  1 
ATOM   6644 C CD1 . PHE B 1 305 ? -42.996 44.338 43.627  1.00 19.07 ? 305 PHE B CD1 1 
ATOM   6645 C CD2 . PHE B 1 305 ? -43.331 44.936 41.336  1.00 17.34 ? 305 PHE B CD2 1 
ATOM   6646 C CE1 . PHE B 1 305 ? -44.234 43.703 43.643  1.00 20.42 ? 305 PHE B CE1 1 
ATOM   6647 C CE2 . PHE B 1 305 ? -44.574 44.301 41.348  1.00 18.08 ? 305 PHE B CE2 1 
ATOM   6648 C CZ  . PHE B 1 305 ? -45.017 43.683 42.504  1.00 19.64 ? 305 PHE B CZ  1 
ATOM   6649 N N   . ARG B 1 306 ? -38.228 45.431 40.662  1.00 16.14 ? 306 ARG B N   1 
ATOM   6650 C CA  . ARG B 1 306 ? -36.894 45.975 40.486  1.00 16.49 ? 306 ARG B CA  1 
ATOM   6651 C C   . ARG B 1 306 ? -36.879 47.471 40.771  1.00 14.85 ? 306 ARG B C   1 
ATOM   6652 O O   . ARG B 1 306 ? -37.881 48.168 40.626  1.00 17.58 ? 306 ARG B O   1 
ATOM   6653 C CB  . ARG B 1 306 ? -36.384 45.712 39.074  1.00 20.82 ? 306 ARG B CB  1 
ATOM   6654 C CG  . ARG B 1 306 ? -36.957 46.682 38.074  1.00 21.11 ? 306 ARG B CG  1 
ATOM   6655 C CD  . ARG B 1 306 ? -36.371 46.538 36.681  1.00 19.90 ? 306 ARG B CD  1 
ATOM   6656 N NE  . ARG B 1 306 ? -37.062 47.492 35.829  1.00 22.68 ? 306 ARG B NE  1 
ATOM   6657 C CZ  . ARG B 1 306 ? -36.536 48.098 34.772  1.00 20.99 ? 306 ARG B CZ  1 
ATOM   6658 N NH1 . ARG B 1 306 ? -35.286 47.835 34.370  1.00 16.77 ? 306 ARG B NH1 1 
ATOM   6659 N NH2 . ARG B 1 306 ? -37.286 48.964 34.105  1.00 17.85 ? 306 ARG B NH2 1 
ATOM   6660 N N   . ASP B 1 307 ? -35.730 47.952 41.234  1.00 16.04 ? 307 ASP B N   1 
ATOM   6661 C CA  . ASP B 1 307 ? -35.516 49.388 41.377  1.00 15.59 ? 307 ASP B CA  1 
ATOM   6662 C C   . ASP B 1 307 ? -35.304 49.962 39.981  1.00 20.44 ? 307 ASP B C   1 
ATOM   6663 O O   . ASP B 1 307 ? -34.233 49.809 39.386  1.00 17.26 ? 307 ASP B O   1 
ATOM   6664 C CB  . ASP B 1 307 ? -34.323 49.666 42.282  1.00 18.08 ? 307 ASP B CB  1 
ATOM   6665 C CG  . ASP B 1 307 ? -34.168 51.144 42.595  1.00 24.50 ? 307 ASP B CG  1 
ATOM   6666 O OD1 . ASP B 1 307 ? -34.227 51.957 41.657  1.00 22.69 ? 307 ASP B OD1 1 
ATOM   6667 O OD2 . ASP B 1 307 ? -34.001 51.498 43.776  1.00 26.52 ? 307 ASP B OD2 1 
ATOM   6668 N N   . LYS B 1 308 ? -36.334 50.625 39.453  1.00 16.38 ? 308 LYS B N   1 
ATOM   6669 C CA  . LYS B 1 308 ? -36.287 51.062 38.059  1.00 18.53 ? 308 LYS B CA  1 
ATOM   6670 C C   . LYS B 1 308 ? -35.207 52.117 37.821  1.00 25.48 ? 308 LYS B C   1 
ATOM   6671 O O   . LYS B 1 308 ? -34.497 52.060 36.806  1.00 15.49 ? 308 LYS B O   1 
ATOM   6672 C CB  . LYS B 1 308 ? -37.654 51.587 37.633  1.00 15.96 ? 308 LYS B CB  1 
ATOM   6673 C CG  . LYS B 1 308 ? -37.683 52.327 36.306  1.00 22.44 ? 308 LYS B CG  1 
ATOM   6674 C CD  . LYS B 1 308 ? -39.084 52.858 36.101  1.00 29.10 ? 308 LYS B CD  1 
ATOM   6675 C CE  . LYS B 1 308 ? -39.137 53.909 35.026  1.00 40.30 ? 308 LYS B CE  1 
ATOM   6676 N NZ  . LYS B 1 308 ? -38.632 53.385 33.748  1.00 35.43 ? 308 LYS B NZ  1 
ATOM   6677 N N   . THR B 1 309 ? -35.080 53.111 38.710  1.00 20.77 ? 309 THR B N   1 
ATOM   6678 C CA  . THR B 1 309 ? -34.139 54.178 38.390  1.00 20.32 ? 309 THR B CA  1 
ATOM   6679 C C   . THR B 1 309 ? -32.713 53.664 38.441  1.00 13.46 ? 309 THR B C   1 
ATOM   6680 O O   . THR B 1 309 ? -31.890 54.045 37.606  1.00 19.20 ? 309 THR B O   1 
ATOM   6681 C CB  . THR B 1 309 ? -34.296 55.393 39.312  1.00 31.60 ? 309 THR B CB  1 
ATOM   6682 O OG1 . THR B 1 309 ? -33.797 55.078 40.610  1.00 47.01 ? 309 THR B OG1 1 
ATOM   6683 C CG2 . THR B 1 309 ? -35.736 55.847 39.399  1.00 26.75 ? 309 THR B CG2 1 
ATOM   6684 N N   . LEU B 1 310 ? -32.407 52.758 39.381  1.00 14.25 ? 310 LEU B N   1 
ATOM   6685 C CA  . LEU B 1 310 ? -31.051 52.223 39.435  1.00 16.12 ? 310 LEU B CA  1 
ATOM   6686 C C   . LEU B 1 310 ? -30.750 51.373 38.206  1.00 14.74 ? 310 LEU B C   1 
ATOM   6687 O O   . LEU B 1 310 ? -29.637 51.421 37.656  1.00 19.13 ? 310 LEU B O   1 
ATOM   6688 C CB  . LEU B 1 310 ? -30.869 51.390 40.703  1.00 17.64 ? 310 LEU B CB  1 
ATOM   6689 C CG  . LEU B 1 310 ? -30.901 52.174 42.008  1.00 24.56 ? 310 LEU B CG  1 
ATOM   6690 C CD1 . LEU B 1 310 ? -30.715 51.194 43.151  1.00 17.49 ? 310 LEU B CD1 1 
ATOM   6691 C CD2 . LEU B 1 310 ? -29.785 53.220 42.023  1.00 31.24 ? 310 LEU B CD2 1 
ATOM   6692 N N   . SER B 1 311 ? -31.733 50.588 37.767  1.00 14.39 ? 311 SER B N   1 
ATOM   6693 C CA  . SER B 1 311 ? -31.556 49.788 36.561  1.00 16.37 ? 311 SER B CA  1 
ATOM   6694 C C   . SER B 1 311 ? -31.385 50.678 35.334  1.00 17.74 ? 311 SER B C   1 
ATOM   6695 O O   . SER B 1 311 ? -30.542 50.405 34.467  1.00 16.77 ? 311 SER B O   1 
ATOM   6696 C CB  . SER B 1 311 ? -32.745 48.835 36.409  1.00 16.74 ? 311 SER B CB  1 
ATOM   6697 O OG  . SER B 1 311 ? -32.905 48.045 37.594  1.00 14.14 ? 311 SER B OG  1 
ATOM   6698 N N   . ASP B 1 312 ? -32.155 51.762 35.254  1.00 15.01 ? 312 ASP B N   1 
ATOM   6699 C CA  . ASP B 1 312 ? -32.036 52.654 34.101  1.00 13.05 ? 312 ASP B CA  1 
ATOM   6700 C C   . ASP B 1 312 ? -30.771 53.505 34.138  1.00 19.04 ? 312 ASP B C   1 
ATOM   6701 O O   . ASP B 1 312 ? -30.306 53.951 33.081  1.00 15.62 ? 312 ASP B O   1 
ATOM   6702 C CB  . ASP B 1 312 ? -33.276 53.544 34.005  1.00 14.43 ? 312 ASP B CB  1 
ATOM   6703 C CG  . ASP B 1 312 ? -34.467 52.800 33.447  1.00 23.34 ? 312 ASP B CG  1 
ATOM   6704 O OD1 . ASP B 1 312 ? -34.271 51.692 32.896  1.00 18.76 ? 312 ASP B OD1 1 
ATOM   6705 O OD2 . ASP B 1 312 ? -35.597 53.317 33.559  1.00 20.14 ? 312 ASP B OD2 1 
ATOM   6706 N N   . LEU B 1 313 ? -30.204 53.773 35.323  1.00 14.94 ? 313 LEU B N   1 
ATOM   6707 C CA  . LEU B 1 313 ? -28.920 54.473 35.353  1.00 19.28 ? 313 LEU B CA  1 
ATOM   6708 C C   . LEU B 1 313 ? -27.873 53.706 34.559  1.00 15.75 ? 313 LEU B C   1 
ATOM   6709 O O   . LEU B 1 313 ? -27.197 54.260 33.684  1.00 18.07 ? 313 LEU B O   1 
ATOM   6710 C CB  . LEU B 1 313 ? -28.442 54.646 36.800  1.00 20.91 ? 313 LEU B CB  1 
ATOM   6711 C CG  . LEU B 1 313 ? -29.026 55.774 37.629  1.00 27.01 ? 313 LEU B CG  1 
ATOM   6712 C CD1 . LEU B 1 313 ? -28.489 55.622 39.034  1.00 26.05 ? 313 LEU B CD1 1 
ATOM   6713 C CD2 . LEU B 1 313 ? -28.627 57.099 37.050  1.00 21.15 ? 313 LEU B CD2 1 
ATOM   6714 N N   . ILE B 1 314 ? -27.730 52.415 34.855  1.00 13.90 ? 314 ILE B N   1 
ATOM   6715 C CA  . ILE B 1 314 ? -26.763 51.583 34.147  1.00 16.99 ? 314 ILE B CA  1 
ATOM   6716 C C   . ILE B 1 314 ? -27.130 51.473 32.674  1.00 21.05 ? 314 ILE B C   1 
ATOM   6717 O O   . ILE B 1 314 ? -26.270 51.605 31.787  1.00 19.64 ? 314 ILE B O   1 
ATOM   6718 C CB  . ILE B 1 314 ? -26.689 50.200 34.817  1.00 18.54 ? 314 ILE B CB  1 
ATOM   6719 C CG1 . ILE B 1 314 ? -26.129 50.361 36.234  1.00 16.85 ? 314 ILE B CG1 1 
ATOM   6720 C CG2 . ILE B 1 314 ? -25.864 49.229 33.969  1.00 14.86 ? 314 ILE B CG2 1 
ATOM   6721 C CD1 . ILE B 1 314 ? -26.050 49.056 37.021  1.00 18.54 ? 314 ILE B CD1 1 
ATOM   6722 N N   . GLY B 1 315 ? -28.419 51.283 32.389  1.00 16.39 ? 315 GLY B N   1 
ATOM   6723 C CA  . GLY B 1 315 ? -28.837 51.017 31.024  1.00 13.97 ? 315 GLY B CA  1 
ATOM   6724 C C   . GLY B 1 315 ? -28.837 52.220 30.107  1.00 17.24 ? 315 GLY B C   1 
ATOM   6725 O O   . GLY B 1 315 ? -28.655 52.061 28.894  1.00 17.62 ? 315 GLY B O   1 
ATOM   6726 N N   . PHE B 1 316 ? -29.055 53.432 30.647  1.00 16.14 ? 316 PHE B N   1 
ATOM   6727 C CA  . PHE B 1 316 ? -29.206 54.589 29.762  1.00 17.28 ? 316 PHE B CA  1 
ATOM   6728 C C   . PHE B 1 316 ? -28.301 55.772 30.098  1.00 16.13 ? 316 PHE B C   1 
ATOM   6729 O O   . PHE B 1 316 ? -27.943 56.545 29.195  1.00 22.24 ? 316 PHE B O   1 
ATOM   6730 C CB  . PHE B 1 316 ? -30.668 55.068 29.739  1.00 18.22 ? 316 PHE B CB  1 
ATOM   6731 C CG  . PHE B 1 316 ? -31.614 54.045 29.212  1.00 19.47 ? 316 PHE B CG  1 
ATOM   6732 C CD1 . PHE B 1 316 ? -31.585 53.701 27.873  1.00 18.29 ? 316 PHE B CD1 1 
ATOM   6733 C CD2 . PHE B 1 316 ? -32.501 53.392 30.050  1.00 19.11 ? 316 PHE B CD2 1 
ATOM   6734 C CE1 . PHE B 1 316 ? -32.444 52.735 27.373  1.00 21.89 ? 316 PHE B CE1 1 
ATOM   6735 C CE2 . PHE B 1 316 ? -33.366 52.423 29.560  1.00 23.13 ? 316 PHE B CE2 1 
ATOM   6736 C CZ  . PHE B 1 316 ? -33.337 52.096 28.217  1.00 24.92 ? 316 PHE B CZ  1 
ATOM   6737 N N   . SER B 1 317 ? -27.919 55.959 31.366  1.00 15.55 ? 317 SER B N   1 
ATOM   6738 C CA  . SER B 1 317 ? -27.210 57.190 31.711  1.00 14.97 ? 317 SER B CA  1 
ATOM   6739 C C   . SER B 1 317 ? -25.693 57.021 31.832  1.00 17.25 ? 317 SER B C   1 
ATOM   6740 O O   . SER B 1 317 ? -24.936 57.803 31.251  1.00 18.42 ? 317 SER B O   1 
ATOM   6741 C CB  . SER B 1 317 ? -27.778 57.776 33.015  1.00 15.66 ? 317 SER B CB  1 
ATOM   6742 O OG  . SER B 1 317 ? -27.236 59.076 33.237  1.00 23.46 ? 317 SER B OG  1 
ATOM   6743 N N   . TYR B 1 318 ? -25.221 56.003 32.551  1.00 14.63 ? 318 TYR B N   1 
ATOM   6744 C CA  . TYR B 1 318 ? -23.819 55.971 32.976  1.00 15.94 ? 318 TYR B CA  1 
ATOM   6745 C C   . TYR B 1 318 ? -22.818 55.785 31.829  1.00 14.49 ? 318 TYR B C   1 
ATOM   6746 O O   . TYR B 1 318 ? -21.619 56.025 32.036  1.00 19.15 ? 318 TYR B O   1 
ATOM   6747 C CB  . TYR B 1 318 ? -23.610 54.837 33.992  1.00 15.58 ? 318 TYR B CB  1 
ATOM   6748 C CG  . TYR B 1 318 ? -24.058 55.127 35.395  1.00 13.96 ? 318 TYR B CG  1 
ATOM   6749 C CD1 . TYR B 1 318 ? -24.280 56.423 35.827  1.00 14.32 ? 318 TYR B CD1 1 
ATOM   6750 C CD2 . TYR B 1 318 ? -24.219 54.083 36.310  1.00 13.37 ? 318 TYR B CD2 1 
ATOM   6751 C CE1 . TYR B 1 318 ? -24.682 56.685 37.148  1.00 16.28 ? 318 TYR B CE1 1 
ATOM   6752 C CE2 . TYR B 1 318 ? -24.611 54.336 37.614  1.00 18.87 ? 318 TYR B CE2 1 
ATOM   6753 C CZ  . TYR B 1 318 ? -24.844 55.627 38.026  1.00 17.40 ? 318 TYR B CZ  1 
ATOM   6754 O OH  . TYR B 1 318 ? -25.243 55.860 39.336  1.00 21.03 ? 318 TYR B OH  1 
ATOM   6755 N N   . HIS B 1 319 ? -23.258 55.346 30.642  1.00 14.36 ? 319 HIS B N   1 
ATOM   6756 C CA  . HIS B 1 319 ? -22.314 55.165 29.537  1.00 17.89 ? 319 HIS B CA  1 
ATOM   6757 C C   . HIS B 1 319 ? -21.559 56.453 29.230  1.00 16.28 ? 319 HIS B C   1 
ATOM   6758 O O   . HIS B 1 319 ? -20.416 56.412 28.749  1.00 19.69 ? 319 HIS B O   1 
ATOM   6759 C CB  . HIS B 1 319 ? -23.037 54.690 28.270  1.00 21.81 ? 319 HIS B CB  1 
ATOM   6760 C CG  . HIS B 1 319 ? -23.893 55.746 27.628  1.00 21.52 ? 319 HIS B CG  1 
ATOM   6761 N ND1 . HIS B 1 319 ? -25.183 55.997 28.038  1.00 19.18 ? 319 HIS B ND1 1 
ATOM   6762 C CD2 . HIS B 1 319 ? -23.637 56.632 26.628  1.00 24.26 ? 319 HIS B CD2 1 
ATOM   6763 C CE1 . HIS B 1 319 ? -25.692 56.978 27.313  1.00 23.97 ? 319 HIS B CE1 1 
ATOM   6764 N NE2 . HIS B 1 319 ? -24.783 57.374 26.441  1.00 24.02 ? 319 HIS B NE2 1 
ATOM   6765 N N   . ALA B 1 320 ? -22.176 57.605 29.500  1.00 18.51 ? 320 ALA B N   1 
ATOM   6766 C CA  . ALA B 1 320 ? -21.583 58.894 29.184  1.00 21.59 ? 320 ALA B CA  1 
ATOM   6767 C C   . ALA B 1 320 ? -20.859 59.524 30.372  1.00 19.42 ? 320 ALA B C   1 
ATOM   6768 O O   . ALA B 1 320 ? -20.388 60.657 30.256  1.00 22.82 ? 320 ALA B O   1 
ATOM   6769 C CB  . ALA B 1 320 ? -22.656 59.848 28.642  1.00 23.53 ? 320 ALA B CB  1 
ATOM   6770 N N   . TRP B 1 321 ? -20.743 58.816 31.499  1.00 16.79 ? 321 TRP B N   1 
ATOM   6771 C CA  . TRP B 1 321 ? -20.075 59.328 32.691  1.00 21.32 ? 321 TRP B CA  1 
ATOM   6772 C C   . TRP B 1 321 ? -18.672 58.748 32.821  1.00 21.74 ? 321 TRP B C   1 
ATOM   6773 O O   . TRP B 1 321 ? -18.397 57.631 32.373  1.00 27.22 ? 321 TRP B O   1 
ATOM   6774 C CB  . TRP B 1 321 ? -20.817 58.966 33.982  1.00 17.21 ? 321 TRP B CB  1 
ATOM   6775 C CG  . TRP B 1 321 ? -22.212 59.478 34.182  1.00 19.63 ? 321 TRP B CG  1 
ATOM   6776 C CD1 . TRP B 1 321 ? -23.198 59.612 33.245  1.00 19.12 ? 321 TRP B CD1 1 
ATOM   6777 C CD2 . TRP B 1 321 ? -22.791 59.868 35.434  1.00 19.67 ? 321 TRP B CD2 1 
ATOM   6778 N NE1 . TRP B 1 321 ? -24.350 60.082 33.838  1.00 23.44 ? 321 TRP B NE1 1 
ATOM   6779 C CE2 . TRP B 1 321 ? -24.129 60.240 35.180  1.00 23.24 ? 321 TRP B CE2 1 
ATOM   6780 C CE3 . TRP B 1 321 ? -22.301 59.954 36.742  1.00 22.46 ? 321 TRP B CE3 1 
ATOM   6781 C CZ2 . TRP B 1 321 ? -24.986 60.691 36.185  1.00 23.79 ? 321 TRP B CZ2 1 
ATOM   6782 C CZ3 . TRP B 1 321 ? -23.162 60.397 37.750  1.00 26.61 ? 321 TRP B CZ3 1 
ATOM   6783 C CH2 . TRP B 1 321 ? -24.494 60.760 37.454  1.00 26.47 ? 321 TRP B CH2 1 
ATOM   6784 N N   . ASN B 1 322 ? -17.807 59.499 33.489  1.00 24.09 ? 322 ASN B N   1 
ATOM   6785 C CA  . ASN B 1 322 ? -16.569 58.943 34.007  1.00 25.48 ? 322 ASN B CA  1 
ATOM   6786 C C   . ASN B 1 322 ? -16.882 57.763 34.923  1.00 24.18 ? 322 ASN B C   1 
ATOM   6787 O O   . ASN B 1 322 ? -17.774 57.848 35.769  1.00 31.26 ? 322 ASN B O   1 
ATOM   6788 C CB  . ASN B 1 322 ? -15.814 60.038 34.760  1.00 28.65 ? 322 ASN B CB  1 
ATOM   6789 C CG  . ASN B 1 322 ? -14.659 59.507 35.538  1.00 32.20 ? 322 ASN B CG  1 
ATOM   6790 O OD1 . ASN B 1 322 ? -14.784 59.206 36.724  1.00 40.79 ? 322 ASN B OD1 1 
ATOM   6791 N ND2 . ASN B 1 322 ? -13.518 59.376 34.878  1.00 36.31 ? 322 ASN B ND2 1 
ATOM   6792 N N   . ALA B 1 323 ? -16.166 56.650 34.733  1.00 20.14 ? 323 ALA B N   1 
ATOM   6793 C CA  . ALA B 1 323 ? -16.477 55.422 35.470  1.00 21.45 ? 323 ALA B CA  1 
ATOM   6794 C C   . ALA B 1 323 ? -16.395 55.628 36.985  1.00 23.01 ? 323 ALA B C   1 
ATOM   6795 O O   . ALA B 1 323 ? -17.249 55.142 37.733  1.00 19.26 ? 323 ALA B O   1 
ATOM   6796 C CB  . ALA B 1 323 ? -15.528 54.307 35.036  1.00 26.24 ? 323 ALA B CB  1 
ATOM   6797 N N   . GLU B 1 324 ? -15.355 56.318 37.459  1.00 19.92 ? 324 GLU B N   1 
ATOM   6798 C CA  . GLU B 1 324 ? -15.245 56.581 38.887  1.00 21.99 ? 324 GLU B CA  1 
ATOM   6799 C C   . GLU B 1 324 ? -16.432 57.395 39.383  1.00 21.17 ? 324 GLU B C   1 
ATOM   6800 O O   . GLU B 1 324 ? -17.024 57.074 40.423  1.00 24.77 ? 324 GLU B O   1 
ATOM   6801 C CB  . GLU B 1 324 ? -13.919 57.284 39.191  1.00 28.44 ? 324 GLU B CB  1 
ATOM   6802 C CG  . GLU B 1 324 ? -13.705 57.538 40.665  1.00 39.45 ? 324 GLU B CG  1 
ATOM   6803 C CD  . GLU B 1 324 ? -13.337 56.266 41.400  1.00 61.02 ? 324 GLU B CD  1 
ATOM   6804 O OE1 . GLU B 1 324 ? -12.898 55.311 40.722  1.00 68.72 ? 324 GLU B OE1 1 
ATOM   6805 O OE2 . GLU B 1 324 ? -13.498 56.214 42.645  1.00 61.68 ? 324 GLU B OE2 1 
ATOM   6806 N N   . ASP B 1 325 ? -16.797 58.453 38.650  1.00 20.35 ? 325 ASP B N   1 
ATOM   6807 C CA  . ASP B 1 325 ? -17.932 59.276 39.069  1.00 27.76 ? 325 ASP B CA  1 
ATOM   6808 C C   . ASP B 1 325 ? -19.233 58.485 39.071  1.00 27.39 ? 325 ASP B C   1 
ATOM   6809 O O   . ASP B 1 325 ? -20.097 58.699 39.937  1.00 23.46 ? 325 ASP B O   1 
ATOM   6810 C CB  . ASP B 1 325 ? -18.087 60.497 38.168  1.00 25.80 ? 325 ASP B CB  1 
ATOM   6811 C CG  . ASP B 1 325 ? -16.878 61.406 38.201  1.00 34.02 ? 325 ASP B CG  1 
ATOM   6812 O OD1 . ASP B 1 325 ? -16.139 61.408 39.214  1.00 35.67 ? 325 ASP B OD1 1 
ATOM   6813 O OD2 . ASP B 1 325 ? -16.686 62.148 37.213  1.00 40.73 ? 325 ASP B OD2 1 
ATOM   6814 N N   . ALA B 1 326 ? -19.418 57.601 38.086  1.00 18.01 ? 326 ALA B N   1 
ATOM   6815 C CA  . ALA B 1 326 ? -20.664 56.838 38.035  1.00 20.09 ? 326 ALA B CA  1 
ATOM   6816 C C   . ALA B 1 326 ? -20.758 55.859 39.195  1.00 18.95 ? 326 ALA B C   1 
ATOM   6817 O O   . ALA B 1 326 ? -21.827 55.690 39.782  1.00 18.59 ? 326 ALA B O   1 
ATOM   6818 C CB  . ALA B 1 326 ? -20.791 56.090 36.710  1.00 16.53 ? 326 ALA B CB  1 
ATOM   6819 N N   . VAL B 1 327 ? -19.656 55.188 39.527  1.00 16.53 ? 327 VAL B N   1 
ATOM   6820 C CA  . VAL B 1 327 ? -19.682 54.252 40.641  1.00 16.31 ? 327 VAL B CA  1 
ATOM   6821 C C   . VAL B 1 327 ? -19.934 54.990 41.952  1.00 18.88 ? 327 VAL B C   1 
ATOM   6822 O O   . VAL B 1 327 ? -20.706 54.524 42.795  1.00 21.08 ? 327 VAL B O   1 
ATOM   6823 C CB  . VAL B 1 327 ? -18.382 53.426 40.687  1.00 16.54 ? 327 VAL B CB  1 
ATOM   6824 C CG1 . VAL B 1 327 ? -18.303 52.627 41.986  1.00 19.02 ? 327 VAL B CG1 1 
ATOM   6825 C CG2 . VAL B 1 327 ? -18.300 52.496 39.441  1.00 16.08 ? 327 VAL B CG2 1 
ATOM   6826 N N   . ARG B 1 328 ? -19.312 56.161 42.145  1.00 18.34 ? 328 ARG B N   1 
ATOM   6827 C CA  . ARG B 1 328 ? -19.598 56.927 43.360  1.00 19.36 ? 328 ARG B CA  1 
ATOM   6828 C C   . ARG B 1 328 ? -21.065 57.350 43.418  1.00 26.54 ? 328 ARG B C   1 
ATOM   6829 O O   . ARG B 1 328 ? -21.684 57.319 44.488  1.00 23.95 ? 328 ARG B O   1 
ATOM   6830 C CB  . ARG B 1 328 ? -18.680 58.147 43.443  1.00 23.22 ? 328 ARG B CB  1 
ATOM   6831 C CG  . ARG B 1 328 ? -18.915 59.003 44.677  1.00 36.73 ? 328 ARG B CG  1 
ATOM   6832 C CD  . ARG B 1 328 ? -17.732 59.912 44.962  1.00 52.41 ? 328 ARG B CD  1 
ATOM   6833 N NE  . ARG B 1 328 ? -17.766 61.132 44.164  1.00 62.09 ? 328 ARG B NE  1 
ATOM   6834 C CZ  . ARG B 1 328 ? -17.126 62.254 44.487  1.00 67.84 ? 328 ARG B CZ  1 
ATOM   6835 N NH1 . ARG B 1 328 ? -16.400 62.313 45.602  1.00 65.74 ? 328 ARG B NH1 1 
ATOM   6836 N NH2 . ARG B 1 328 ? -17.213 63.320 43.696  1.00 71.84 ? 328 ARG B NH2 1 
ATOM   6837 N N   . ASP B 1 329 ? -21.631 57.762 42.276  1.00 21.58 ? 329 ASP B N   1 
ATOM   6838 C CA  . ASP B 1 329 ? -23.042 58.129 42.221  1.00 23.85 ? 329 ASP B CA  1 
ATOM   6839 C C   . ASP B 1 329 ? -23.924 56.959 42.633  1.00 19.48 ? 329 ASP B C   1 
ATOM   6840 O O   . ASP B 1 329 ? -24.866 57.117 43.423  1.00 22.71 ? 329 ASP B O   1 
ATOM   6841 C CB  . ASP B 1 329 ? -23.404 58.599 40.809  1.00 19.51 ? 329 ASP B CB  1 
ATOM   6842 C CG  . ASP B 1 329 ? -24.872 59.038 40.688  1.00 19.72 ? 329 ASP B CG  1 
ATOM   6843 O OD1 . ASP B 1 329 ? -25.197 60.188 41.069  1.00 26.76 ? 329 ASP B OD1 1 
ATOM   6844 O OD2 . ASP B 1 329 ? -25.704 58.237 40.222  1.00 23.06 ? 329 ASP B OD2 1 
ATOM   6845 N N   . PHE B 1 330 ? -23.624 55.770 42.097  1.00 17.62 ? 330 PHE B N   1 
ATOM   6846 C CA  . PHE B 1 330 ? -24.440 54.583 42.341  1.00 15.54 ? 330 PHE B CA  1 
ATOM   6847 C C   . PHE B 1 330 ? -24.408 54.185 43.815  1.00 17.99 ? 330 PHE B C   1 
ATOM   6848 O O   . PHE B 1 330 ? -25.454 53.919 44.424  1.00 18.60 ? 330 PHE B O   1 
ATOM   6849 C CB  . PHE B 1 330 ? -23.923 53.454 41.452  1.00 18.74 ? 330 PHE B CB  1 
ATOM   6850 C CG  . PHE B 1 330 ? -24.803 52.251 41.392  1.00 17.54 ? 330 PHE B CG  1 
ATOM   6851 C CD1 . PHE B 1 330 ? -25.909 52.232 40.583  1.00 22.19 ? 330 PHE B CD1 1 
ATOM   6852 C CD2 . PHE B 1 330 ? -24.493 51.118 42.159  1.00 20.05 ? 330 PHE B CD2 1 
ATOM   6853 C CE1 . PHE B 1 330 ? -26.713 51.103 40.507  1.00 26.06 ? 330 PHE B CE1 1 
ATOM   6854 C CE2 . PHE B 1 330 ? -25.295 49.993 42.090  1.00 23.67 ? 330 PHE B CE2 1 
ATOM   6855 C CZ  . PHE B 1 330 ? -26.410 49.991 41.265  1.00 24.49 ? 330 PHE B CZ  1 
ATOM   6856 N N   . ILE B 1 331 ? -23.210 54.129 44.404  1.00 19.62 ? 331 ILE B N   1 
ATOM   6857 C CA  . ILE B 1 331 ? -23.095 53.798 45.827  1.00 20.35 ? 331 ILE B CA  1 
ATOM   6858 C C   . ILE B 1 331 ? -23.805 54.849 46.667  1.00 22.64 ? 331 ILE B C   1 
ATOM   6859 O O   . ILE B 1 331 ? -24.419 54.539 47.697  1.00 18.80 ? 331 ILE B O   1 
ATOM   6860 C CB  . ILE B 1 331 ? -21.610 53.671 46.228  1.00 21.38 ? 331 ILE B CB  1 
ATOM   6861 C CG1 . ILE B 1 331 ? -20.892 52.578 45.421  1.00 21.79 ? 331 ILE B CG1 1 
ATOM   6862 C CG2 . ILE B 1 331 ? -21.462 53.451 47.741  1.00 25.17 ? 331 ILE B CG2 1 
ATOM   6863 C CD1 . ILE B 1 331 ? -21.420 51.168 45.642  1.00 22.89 ? 331 ILE B CD1 1 
ATOM   6864 N N   . GLY B 1 332 ? -23.686 56.116 46.268  1.00 20.71 ? 332 GLY B N   1 
ATOM   6865 C CA  . GLY B 1 332 ? -24.347 57.176 47.002  1.00 21.67 ? 332 GLY B CA  1 
ATOM   6866 C C   . GLY B 1 332 ? -25.852 57.026 46.997  1.00 20.14 ? 332 GLY B C   1 
ATOM   6867 O O   . GLY B 1 332 ? -26.517 57.355 47.984  1.00 24.57 ? 332 GLY B O   1 
ATOM   6868 N N   . ARG B 1 333 ? -26.406 56.520 45.901  1.00 18.33 ? 333 ARG B N   1 
ATOM   6869 C CA  . ARG B 1 333 ? -27.839 56.248 45.877  1.00 26.28 ? 333 ARG B CA  1 
ATOM   6870 C C   . ARG B 1 333 ? -28.215 55.103 46.807  1.00 24.65 ? 333 ARG B C   1 
ATOM   6871 O O   . ARG B 1 333 ? -29.254 55.165 47.472  1.00 23.18 ? 333 ARG B O   1 
ATOM   6872 C CB  . ARG B 1 333 ? -28.285 55.956 44.456  1.00 22.82 ? 333 ARG B CB  1 
ATOM   6873 C CG  . ARG B 1 333 ? -28.176 57.196 43.619  1.00 32.83 ? 333 ARG B CG  1 
ATOM   6874 C CD  . ARG B 1 333 ? -28.477 56.884 42.203  1.00 40.32 ? 333 ARG B CD  1 
ATOM   6875 N NE  . ARG B 1 333 ? -28.099 57.990 41.334  1.00 41.62 ? 333 ARG B NE  1 
ATOM   6876 C CZ  . ARG B 1 333 ? -28.937 58.938 40.953  1.00 44.94 ? 333 ARG B CZ  1 
ATOM   6877 N NH1 . ARG B 1 333 ? -30.194 58.912 41.382  1.00 49.43 ? 333 ARG B NH1 1 
ATOM   6878 N NH2 . ARG B 1 333 ? -28.516 59.906 40.153  1.00 43.01 ? 333 ARG B NH2 1 
ATOM   6879 N N   . LEU B 1 334 ? -27.400 54.045 46.847  1.00 22.94 ? 334 LEU B N   1 
ATOM   6880 C CA  . LEU B 1 334 ? -27.638 52.970 47.804  1.00 21.76 ? 334 LEU B CA  1 
ATOM   6881 C C   . LEU B 1 334 ? -27.552 53.479 49.234  1.00 19.24 ? 334 LEU B C   1 
ATOM   6882 O O   . LEU B 1 334 ? -28.317 53.043 50.100  1.00 20.81 ? 334 LEU B O   1 
ATOM   6883 C CB  . LEU B 1 334 ? -26.642 51.832 47.582  1.00 17.23 ? 334 LEU B CB  1 
ATOM   6884 C CG  . LEU B 1 334 ? -26.799 51.192 46.189  1.00 16.79 ? 334 LEU B CG  1 
ATOM   6885 C CD1 . LEU B 1 334 ? -25.751 50.120 45.953  1.00 22.49 ? 334 LEU B CD1 1 
ATOM   6886 C CD2 . LEU B 1 334 ? -28.201 50.623 45.950  1.00 19.20 ? 334 LEU B CD2 1 
ATOM   6887 N N   . LYS B 1 335 ? -26.603 54.380 49.511  1.00 20.38 ? 335 LYS B N   1 
ATOM   6888 C CA  . LYS B 1 335 ? -26.523 54.958 50.849  1.00 23.97 ? 335 LYS B CA  1 
ATOM   6889 C C   . LYS B 1 335 ? -27.809 55.689 51.208  1.00 24.61 ? 335 LYS B C   1 
ATOM   6890 O O   . LYS B 1 335 ? -28.295 55.586 52.341  1.00 23.13 ? 335 LYS B O   1 
ATOM   6891 C CB  . LYS B 1 335 ? -25.328 55.904 50.957  1.00 23.95 ? 335 LYS B CB  1 
ATOM   6892 C CG  . LYS B 1 335 ? -25.279 56.665 52.300  1.00 24.66 ? 335 LYS B CG  1 
ATOM   6893 C CD  . LYS B 1 335 ? -24.168 57.719 52.343  1.00 38.50 ? 335 LYS B CD  1 
ATOM   6894 C CE  . LYS B 1 335 ? -24.357 58.802 51.280  1.00 36.39 ? 335 LYS B CE  1 
ATOM   6895 N NZ  . LYS B 1 335 ? -23.568 60.033 51.625  1.00 36.81 ? 335 LYS B NZ  1 
ATOM   6896 N N   . LYS B 1 336 ? -28.377 56.434 50.259  1.00 27.33 ? 336 LYS B N   1 
ATOM   6897 C CA  . LYS B 1 336 ? -29.600 57.168 50.567  1.00 33.13 ? 336 LYS B CA  1 
ATOM   6898 C C   . LYS B 1 336 ? -30.752 56.211 50.844  1.00 24.53 ? 336 LYS B C   1 
ATOM   6899 O O   . LYS B 1 336 ? -31.516 56.427 51.792  1.00 27.06 ? 336 LYS B O   1 
ATOM   6900 C CB  . LYS B 1 336 ? -29.942 58.139 49.436  1.00 37.72 ? 336 LYS B CB  1 
ATOM   6901 C CG  . LYS B 1 336 ? -28.940 59.286 49.281  1.00 39.13 ? 336 LYS B CG  1 
ATOM   6902 C CD  . LYS B 1 336 ? -29.196 60.402 50.294  1.00 51.03 ? 336 LYS B CD  1 
ATOM   6903 C CE  . LYS B 1 336 ? -27.893 61.092 50.724  1.00 47.67 ? 336 LYS B CE  1 
ATOM   6904 N NZ  . LYS B 1 336 ? -27.914 61.530 52.157  1.00 54.40 ? 336 LYS B NZ  1 
ATOM   6905 N N   . ILE B 1 337 ? -30.865 55.130 50.056  1.00 23.04 ? 337 ILE B N   1 
ATOM   6906 C CA  . ILE B 1 337 ? -31.850 54.083 50.333  1.00 22.11 ? 337 ILE B CA  1 
ATOM   6907 C C   . ILE B 1 337 ? -31.635 53.518 51.733  1.00 25.42 ? 337 ILE B C   1 
ATOM   6908 O O   . ILE B 1 337 ? -32.572 53.419 52.540  1.00 27.08 ? 337 ILE B O   1 
ATOM   6909 C CB  . ILE B 1 337 ? -31.777 52.968 49.270  1.00 25.96 ? 337 ILE B CB  1 
ATOM   6910 C CG1 . ILE B 1 337 ? -32.163 53.472 47.865  1.00 26.44 ? 337 ILE B CG1 1 
ATOM   6911 C CG2 . ILE B 1 337 ? -32.668 51.785 49.672  1.00 28.20 ? 337 ILE B CG2 1 
ATOM   6912 C CD1 . ILE B 1 337 ? -31.774 52.498 46.718  1.00 23.84 ? 337 ILE B CD1 1 
ATOM   6913 N N   . HIS B 1 338 ? -30.384 53.150 52.037  1.00 20.81 ? 338 HIS B N   1 
ATOM   6914 C CA  . HIS B 1 338 ? -30.053 52.554 53.330  1.00 21.42 ? 338 HIS B CA  1 
ATOM   6915 C C   . HIS B 1 338 ? -30.460 53.462 54.490  1.00 23.97 ? 338 HIS B C   1 
ATOM   6916 O O   . HIS B 1 338 ? -31.040 52.995 55.483  1.00 27.34 ? 338 HIS B O   1 
ATOM   6917 C CB  . HIS B 1 338 ? -28.551 52.245 53.366  1.00 26.99 ? 338 HIS B CB  1 
ATOM   6918 C CG  . HIS B 1 338 ? -28.088 51.579 54.628  1.00 35.47 ? 338 HIS B CG  1 
ATOM   6919 N ND1 . HIS B 1 338 ? -27.673 52.286 55.735  1.00 41.53 ? 338 HIS B ND1 1 
ATOM   6920 C CD2 . HIS B 1 338 ? -27.969 50.270 54.951  1.00 34.16 ? 338 HIS B CD2 1 
ATOM   6921 C CE1 . HIS B 1 338 ? -27.323 51.440 56.689  1.00 43.92 ? 338 HIS B CE1 1 
ATOM   6922 N NE2 . HIS B 1 338 ? -27.489 50.210 56.235  1.00 39.05 ? 338 HIS B NE2 1 
ATOM   6923 N N   . GLU B 1 339 ? -30.181 54.764 54.382  1.00 30.32 ? 339 GLU B N   1 
ATOM   6924 C CA  . GLU B 1 339 ? -30.590 55.702 55.428  1.00 32.70 ? 339 GLU B CA  1 
ATOM   6925 C C   . GLU B 1 339 ? -32.093 55.934 55.452  1.00 40.73 ? 339 GLU B C   1 
ATOM   6926 O O   . GLU B 1 339 ? -32.619 56.402 56.469  1.00 46.04 ? 339 GLU B O   1 
ATOM   6927 C CB  . GLU B 1 339 ? -29.897 57.059 55.249  1.00 37.24 ? 339 GLU B CB  1 
ATOM   6928 C CG  . GLU B 1 339 ? -28.381 57.030 55.307  1.00 41.53 ? 339 GLU B CG  1 
ATOM   6929 C CD  . GLU B 1 339 ? -27.759 58.271 54.682  1.00 55.16 ? 339 GLU B CD  1 
ATOM   6930 O OE1 . GLU B 1 339 ? -26.543 58.509 54.895  1.00 55.33 ? 339 GLU B OE1 1 
ATOM   6931 O OE2 . GLU B 1 339 ? -28.489 59.009 53.974  1.00 58.54 ? 339 GLU B OE2 1 
ATOM   6932 N N   . SER B 1 340 ? -32.798 55.633 54.365  1.00 43.64 ? 340 SER B N   1 
ATOM   6933 C CA  . SER B 1 340 ? -34.184 56.067 54.242  1.00 34.37 ? 340 SER B CA  1 
ATOM   6934 C C   . SER B 1 340 ? -35.163 55.154 54.964  1.00 41.43 ? 340 SER B C   1 
ATOM   6935 O O   . SER B 1 340 ? -36.312 55.557 55.182  1.00 45.80 ? 340 SER B O   1 
ATOM   6936 C CB  . SER B 1 340 ? -34.573 56.181 52.765  1.00 33.99 ? 340 SER B CB  1 
ATOM   6937 O OG  . SER B 1 340 ? -34.873 54.908 52.209  1.00 36.37 ? 340 SER B OG  1 
ATOM   6938 N N   . VAL B 1 341 ? -34.742 53.954 55.357  1.00 34.64 ? 341 VAL B N   1 
ATOM   6939 C CA  . VAL B 1 341 ? -35.635 52.983 55.975  1.00 35.16 ? 341 VAL B CA  1 
ATOM   6940 C C   . VAL B 1 341 ? -34.960 52.399 57.207  1.00 36.90 ? 341 VAL B C   1 
ATOM   6941 O O   . VAL B 1 341 ? -33.728 52.349 57.299  1.00 39.47 ? 341 VAL B O   1 
ATOM   6942 C CB  . VAL B 1 341 ? -36.033 51.858 54.989  1.00 35.15 ? 341 VAL B CB  1 
ATOM   6943 C CG1 . VAL B 1 341 ? -36.874 52.423 53.859  1.00 37.82 ? 341 VAL B CG1 1 
ATOM   6944 C CG2 . VAL B 1 341 ? -34.790 51.157 54.443  1.00 33.83 ? 341 VAL B CG2 1 
ATOM   6945 N N   . ASP B 1 342 ? -35.780 51.955 58.165  1.00 35.94 ? 342 ASP B N   1 
ATOM   6946 C CA  . ASP B 1 342 ? -35.270 51.362 59.395  1.00 39.18 ? 342 ASP B CA  1 
ATOM   6947 C C   . ASP B 1 342 ? -35.068 49.854 59.296  1.00 42.91 ? 342 ASP B C   1 
ATOM   6948 O O   . ASP B 1 342 ? -34.466 49.266 60.203  1.00 46.73 ? 342 ASP B O   1 
ATOM   6949 C CB  . ASP B 1 342 ? -36.209 51.689 60.571  1.00 45.39 ? 342 ASP B CB  1 
ATOM   6950 C CG  . ASP B 1 342 ? -37.636 51.252 60.317  1.00 61.00 ? 342 ASP B CG  1 
ATOM   6951 O OD1 . ASP B 1 342 ? -38.087 51.358 59.160  1.00 69.83 ? 342 ASP B OD1 1 
ATOM   6952 O OD2 . ASP B 1 342 ? -38.320 50.820 61.274  1.00 74.22 ? 342 ASP B OD2 1 
ATOM   6953 N N   . PHE B 1 343 ? -35.541 49.220 58.224  1.00 36.51 ? 343 PHE B N   1 
ATOM   6954 C CA  . PHE B 1 343 ? -35.356 47.798 57.982  1.00 31.13 ? 343 PHE B CA  1 
ATOM   6955 C C   . PHE B 1 343 ? -34.278 47.602 56.915  1.00 24.65 ? 343 PHE B C   1 
ATOM   6956 O O   . PHE B 1 343 ? -33.718 48.563 56.385  1.00 26.43 ? 343 PHE B O   1 
ATOM   6957 C CB  . PHE B 1 343 ? -36.674 47.153 57.543  1.00 28.60 ? 343 PHE B CB  1 
ATOM   6958 C CG  . PHE B 1 343 ? -37.231 47.725 56.276  1.00 26.49 ? 343 PHE B CG  1 
ATOM   6959 C CD1 . PHE B 1 343 ? -38.003 48.882 56.295  1.00 27.78 ? 343 PHE B CD1 1 
ATOM   6960 C CD2 . PHE B 1 343 ? -36.974 47.113 55.058  1.00 22.71 ? 343 PHE B CD2 1 
ATOM   6961 C CE1 . PHE B 1 343 ? -38.525 49.412 55.109  1.00 24.84 ? 343 PHE B CE1 1 
ATOM   6962 C CE2 . PHE B 1 343 ? -37.481 47.634 53.873  1.00 25.66 ? 343 PHE B CE2 1 
ATOM   6963 C CZ  . PHE B 1 343 ? -38.258 48.783 53.897  1.00 24.74 ? 343 PHE B CZ  1 
ATOM   6964 N N   . GLN B 1 344 ? -34.000 46.340 56.579  1.00 22.91 ? 344 GLN B N   1 
ATOM   6965 C CA  . GLN B 1 344 ? -32.977 46.034 55.583  1.00 21.67 ? 344 GLN B CA  1 
ATOM   6966 C C   . GLN B 1 344 ? -33.627 45.934 54.216  1.00 24.03 ? 344 GLN B C   1 
ATOM   6967 O O   . GLN B 1 344 ? -34.403 45.000 53.983  1.00 23.97 ? 344 GLN B O   1 
ATOM   6968 C CB  . GLN B 1 344 ? -32.249 44.744 55.934  1.00 23.18 ? 344 GLN B CB  1 
ATOM   6969 C CG  . GLN B 1 344 ? -31.457 44.897 57.236  1.00 23.53 ? 344 GLN B CG  1 
ATOM   6970 C CD  . GLN B 1 344 ? -30.663 43.666 57.607  1.00 30.94 ? 344 GLN B CD  1 
ATOM   6971 O OE1 . GLN B 1 344 ? -29.449 43.748 57.853  1.00 29.71 ? 344 GLN B OE1 1 
ATOM   6972 N NE2 . GLN B 1 344 ? -31.337 42.516 57.660  1.00 24.89 ? 344 GLN B NE2 1 
ATOM   6973 N N   . PRO B 1 345 ? -33.372 46.869 53.309  1.00 19.82 ? 345 PRO B N   1 
ATOM   6974 C CA  . PRO B 1 345 ? -34.072 46.866 52.026  1.00 23.01 ? 345 PRO B CA  1 
ATOM   6975 C C   . PRO B 1 345 ? -33.403 45.901 51.064  1.00 19.21 ? 345 PRO B C   1 
ATOM   6976 O O   . PRO B 1 345 ? -32.208 45.614 51.166  1.00 22.06 ? 345 PRO B O   1 
ATOM   6977 C CB  . PRO B 1 345 ? -33.934 48.317 51.541  1.00 20.03 ? 345 PRO B CB  1 
ATOM   6978 C CG  . PRO B 1 345 ? -32.655 48.801 52.180  1.00 21.88 ? 345 PRO B CG  1 
ATOM   6979 C CD  . PRO B 1 345 ? -32.512 48.053 53.497  1.00 20.24 ? 345 PRO B CD  1 
ATOM   6980 N N   . VAL B 1 346 ? -34.216 45.353 50.160  1.00 21.85 ? 346 VAL B N   1 
ATOM   6981 C CA  . VAL B 1 346 ? -33.731 44.504 49.077  1.00 21.62 ? 346 VAL B CA  1 
ATOM   6982 C C   . VAL B 1 346 ? -33.868 45.309 47.799  1.00 17.44 ? 346 VAL B C   1 
ATOM   6983 O O   . VAL B 1 346 ? -34.970 45.769 47.464  1.00 17.81 ? 346 VAL B O   1 
ATOM   6984 C CB  . VAL B 1 346 ? -34.509 43.184 48.991  1.00 22.72 ? 346 VAL B CB  1 
ATOM   6985 C CG1 . VAL B 1 346 ? -33.902 42.283 47.901  1.00 24.17 ? 346 VAL B CG1 1 
ATOM   6986 C CG2 . VAL B 1 346 ? -34.512 42.492 50.347  1.00 22.45 ? 346 VAL B CG2 1 
ATOM   6987 N N   . VAL B 1 347 ? -32.754 45.496 47.095  1.00 17.86 ? 347 VAL B N   1 
ATOM   6988 C CA  . VAL B 1 347 ? -32.701 46.360 45.926  1.00 16.94 ? 347 VAL B CA  1 
ATOM   6989 C C   . VAL B 1 347 ? -32.350 45.491 44.721  1.00 14.34 ? 347 VAL B C   1 
ATOM   6990 O O   . VAL B 1 347 ? -31.200 45.051 44.596  1.00 17.56 ? 347 VAL B O   1 
ATOM   6991 C CB  . VAL B 1 347 ? -31.681 47.491 46.109  1.00 14.71 ? 347 VAL B CB  1 
ATOM   6992 C CG1 . VAL B 1 347 ? -31.686 48.398 44.908  1.00 15.43 ? 347 VAL B CG1 1 
ATOM   6993 C CG2 . VAL B 1 347 ? -31.985 48.275 47.399  1.00 21.04 ? 347 VAL B CG2 1 
ATOM   6994 N N   . PHE B 1 348 ? -33.344 45.234 43.847  1.00 14.15 ? 348 PHE B N   1 
ATOM   6995 C CA  . PHE B 1 348 ? -33.154 44.455 42.621  1.00 13.76 ? 348 PHE B CA  1 
ATOM   6996 C C   . PHE B 1 348 ? -32.729 45.403 41.506  1.00 17.29 ? 348 PHE B C   1 
ATOM   6997 O O   . PHE B 1 348 ? -33.421 46.379 41.218  1.00 18.57 ? 348 PHE B O   1 
ATOM   6998 C CB  . PHE B 1 348 ? -34.429 43.693 42.217  1.00 18.52 ? 348 PHE B CB  1 
ATOM   6999 C CG  . PHE B 1 348 ? -34.485 42.271 42.755  1.00 18.74 ? 348 PHE B CG  1 
ATOM   7000 C CD1 . PHE B 1 348 ? -34.629 42.031 44.111  1.00 15.30 ? 348 PHE B CD1 1 
ATOM   7001 C CD2 . PHE B 1 348 ? -34.357 41.189 41.895  1.00 18.84 ? 348 PHE B CD2 1 
ATOM   7002 C CE1 . PHE B 1 348 ? -34.625 40.729 44.610  1.00 15.91 ? 348 PHE B CE1 1 
ATOM   7003 C CE2 . PHE B 1 348 ? -34.382 39.891 42.371  1.00 18.05 ? 348 PHE B CE2 1 
ATOM   7004 C CZ  . PHE B 1 348 ? -34.505 39.651 43.740  1.00 16.04 ? 348 PHE B CZ  1 
ATOM   7005 N N   . VAL B 1 349 ? -31.591 45.115 40.880  1.00 14.62 ? 349 VAL B N   1 
ATOM   7006 C CA  . VAL B 1 349 ? -31.151 45.829 39.690  1.00 13.09 ? 349 VAL B CA  1 
ATOM   7007 C C   . VAL B 1 349 ? -31.258 44.835 38.544  1.00 17.26 ? 349 VAL B C   1 
ATOM   7008 O O   . VAL B 1 349 ? -30.511 43.849 38.509  1.00 14.61 ? 349 VAL B O   1 
ATOM   7009 C CB  . VAL B 1 349 ? -29.718 46.359 39.831  1.00 12.20 ? 349 VAL B CB  1 
ATOM   7010 C CG1 . VAL B 1 349 ? -29.330 47.082 38.557  1.00 16.29 ? 349 VAL B CG1 1 
ATOM   7011 C CG2 . VAL B 1 349 ? -29.638 47.267 41.043  1.00 15.24 ? 349 VAL B CG2 1 
ATOM   7012 N N   . VAL B 1 350 ? -32.214 45.056 37.639  1.00 14.19 ? 350 VAL B N   1 
ATOM   7013 C CA  . VAL B 1 350 ? -32.532 44.090 36.595  1.00 15.50 ? 350 VAL B CA  1 
ATOM   7014 C C   . VAL B 1 350 ? -32.588 44.815 35.257  1.00 12.68 ? 350 VAL B C   1 
ATOM   7015 O O   . VAL B 1 350 ? -33.342 45.779 35.098  1.00 15.98 ? 350 VAL B O   1 
ATOM   7016 C CB  . VAL B 1 350 ? -33.873 43.382 36.862  1.00 18.06 ? 350 VAL B CB  1 
ATOM   7017 C CG1 . VAL B 1 350 ? -34.061 42.223 35.890  1.00 16.71 ? 350 VAL B CG1 1 
ATOM   7018 C CG2 . VAL B 1 350 ? -33.967 42.906 38.320  1.00 17.22 ? 350 VAL B CG2 1 
ATOM   7019 N N   . LEU B 1 351 ? -31.825 44.324 34.279  1.00 12.59 ? 351 LEU B N   1 
ATOM   7020 C CA  . LEU B 1 351 ? -31.890 44.880 32.931  1.00 12.71 ? 351 LEU B CA  1 
ATOM   7021 C C   . LEU B 1 351 ? -31.259 43.858 32.004  1.00 12.88 ? 351 LEU B C   1 
ATOM   7022 O O   . LEU B 1 351 ? -30.783 42.811 32.452  1.00 16.87 ? 351 LEU B O   1 
ATOM   7023 C CB  . LEU B 1 351 ? -31.198 46.255 32.862  1.00 20.25 ? 351 LEU B CB  1 
ATOM   7024 C CG  . LEU B 1 351 ? -29.714 46.349 33.239  1.00 18.25 ? 351 LEU B CG  1 
ATOM   7025 C CD1 . LEU B 1 351 ? -29.003 47.411 32.373  1.00 19.86 ? 351 LEU B CD1 1 
ATOM   7026 C CD2 . LEU B 1 351 ? -29.494 46.653 34.733  1.00 16.35 ? 351 LEU B CD2 1 
ATOM   7027 N N   . ASP B 1 352 ? -31.251 44.162 30.711  1.00 13.26 ? 352 ASP B N   1 
ATOM   7028 C CA  . ASP B 1 352 ? -30.535 43.294 29.781  1.00 16.66 ? 352 ASP B CA  1 
ATOM   7029 C C   . ASP B 1 352 ? -29.067 43.252 30.179  1.00 15.87 ? 352 ASP B C   1 
ATOM   7030 O O   . ASP B 1 352 ? -28.500 44.261 30.596  1.00 18.91 ? 352 ASP B O   1 
ATOM   7031 C CB  . ASP B 1 352 ? -30.655 43.808 28.344  1.00 14.93 ? 352 ASP B CB  1 
ATOM   7032 C CG  . ASP B 1 352 ? -32.076 43.771 27.802  1.00 19.28 ? 352 ASP B CG  1 
ATOM   7033 O OD1 . ASP B 1 352 ? -32.992 43.237 28.466  1.00 17.56 ? 352 ASP B OD1 1 
ATOM   7034 O OD2 . ASP B 1 352 ? -32.274 44.331 26.694  1.00 19.72 ? 352 ASP B OD2 1 
ATOM   7035 N N   . GLY B 1 353 ? -28.440 42.081 30.036  1.00 15.65 ? 353 GLY B N   1 
ATOM   7036 C CA  . GLY B 1 353 ? -27.056 41.944 30.437  1.00 14.15 ? 353 GLY B CA  1 
ATOM   7037 C C   . GLY B 1 353 ? -26.018 42.160 29.347  1.00 19.01 ? 353 GLY B C   1 
ATOM   7038 O O   . GLY B 1 353 ? -24.814 42.144 29.631  1.00 15.03 ? 353 GLY B O   1 
ATOM   7039 N N   . GLU B 1 354 ? -26.433 42.382 28.095  1.00 18.24 ? 354 GLU B N   1 
ATOM   7040 C CA  . GLU B 1 354 ? -25.484 42.464 26.990  1.00 14.10 ? 354 GLU B CA  1 
ATOM   7041 C C   . GLU B 1 354 ? -25.658 43.679 26.084  1.00 14.13 ? 354 GLU B C   1 
ATOM   7042 O O   . GLU B 1 354 ? -24.877 43.828 25.139  1.00 17.75 ? 354 GLU B O   1 
ATOM   7043 C CB  . GLU B 1 354 ? -25.544 41.175 26.132  1.00 15.02 ? 354 GLU B CB  1 
ATOM   7044 C CG  . GLU B 1 354 ? -26.741 41.094 25.122  1.00 15.62 ? 354 GLU B CG  1 
ATOM   7045 C CD  . GLU B 1 354 ? -28.039 40.693 25.815  1.00 15.59 ? 354 GLU B CD  1 
ATOM   7046 O OE1 . GLU B 1 354 ? -28.555 39.570 25.541  1.00 16.43 ? 354 GLU B OE1 1 
ATOM   7047 O OE2 . GLU B 1 354 ? -28.532 41.496 26.650  1.00 14.89 ? 354 GLU B OE2 1 
ATOM   7048 N N   . ASN B 1 355 ? -26.626 44.557 26.335  1.00 13.83 ? 355 ASN B N   1 
ATOM   7049 C CA  . ASN B 1 355 ? -26.941 45.582 25.335  1.00 16.46 ? 355 ASN B CA  1 
ATOM   7050 C C   . ASN B 1 355 ? -26.454 46.986 25.683  1.00 13.83 ? 355 ASN B C   1 
ATOM   7051 O O   . ASN B 1 355 ? -26.373 47.828 24.780  1.00 16.48 ? 355 ASN B O   1 
ATOM   7052 C CB  . ASN B 1 355 ? -28.452 45.618 25.080  1.00 16.98 ? 355 ASN B CB  1 
ATOM   7053 C CG  . ASN B 1 355 ? -28.937 44.365 24.408  1.00 15.19 ? 355 ASN B CG  1 
ATOM   7054 O OD1 . ASN B 1 355 ? -28.303 43.877 23.473  1.00 16.52 ? 355 ASN B OD1 1 
ATOM   7055 N ND2 . ASN B 1 355 ? -30.068 43.822 24.882  1.00 17.85 ? 355 ASN B ND2 1 
ATOM   7056 N N   . CYS B 1 356 ? -26.079 47.259 26.932  1.00 16.70 ? 356 CYS B N   1 
ATOM   7057 C CA  . CYS B 1 356 ? -25.621 48.601 27.303  1.00 16.06 ? 356 CYS B CA  1 
ATOM   7058 C C   . CYS B 1 356 ? -24.110 48.805 27.187  1.00 14.47 ? 356 CYS B C   1 
ATOM   7059 O O   . CYS B 1 356 ? -23.667 49.941 26.959  1.00 15.69 ? 356 CYS B O   1 
ATOM   7060 C CB  . CYS B 1 356 ? -26.070 48.936 28.738  1.00 14.37 ? 356 CYS B CB  1 
ATOM   7061 S SG  . CYS B 1 356 ? -25.486 47.781 29.999  1.00 17.99 ? 356 CYS B SG  1 
ATOM   7062 N N   . TRP B 1 357 ? -23.305 47.742 27.301  1.00 17.59 ? 357 TRP B N   1 
ATOM   7063 C CA  . TRP B 1 357 ? -21.860 47.920 27.461  1.00 16.20 ? 357 TRP B CA  1 
ATOM   7064 C C   . TRP B 1 357 ? -21.197 48.500 26.218  1.00 16.57 ? 357 TRP B C   1 
ATOM   7065 O O   . TRP B 1 357 ? -20.187 49.203 26.337  1.00 14.54 ? 357 TRP B O   1 
ATOM   7066 C CB  . TRP B 1 357 ? -21.208 46.581 27.842  1.00 13.58 ? 357 TRP B CB  1 
ATOM   7067 C CG  . TRP B 1 357 ? -21.965 45.952 28.912  1.00 13.09 ? 357 TRP B CG  1 
ATOM   7068 C CD1 . TRP B 1 357 ? -22.630 44.750 28.868  1.00 14.28 ? 357 TRP B CD1 1 
ATOM   7069 C CD2 . TRP B 1 357 ? -22.234 46.515 30.200  1.00 17.21 ? 357 TRP B CD2 1 
ATOM   7070 N NE1 . TRP B 1 357 ? -23.280 44.530 30.071  1.00 13.77 ? 357 TRP B NE1 1 
ATOM   7071 C CE2 . TRP B 1 357 ? -23.038 45.593 30.902  1.00 15.53 ? 357 TRP B CE2 1 
ATOM   7072 C CE3 . TRP B 1 357 ? -21.856 47.706 30.836  1.00 17.62 ? 357 TRP B CE3 1 
ATOM   7073 C CZ2 . TRP B 1 357 ? -23.495 45.839 32.206  1.00 15.49 ? 357 TRP B CZ2 1 
ATOM   7074 C CZ3 . TRP B 1 357 ? -22.302 47.936 32.135  1.00 16.91 ? 357 TRP B CZ3 1 
ATOM   7075 C CH2 . TRP B 1 357 ? -23.093 47.001 32.801  1.00 15.92 ? 357 TRP B CH2 1 
ATOM   7076 N N   . GLU B 1 358 ? -21.754 48.241 25.029  1.00 15.59 ? 358 GLU B N   1 
ATOM   7077 C CA  . GLU B 1 358 ? -21.144 48.745 23.801  1.00 17.83 ? 358 GLU B CA  1 
ATOM   7078 C C   . GLU B 1 358 ? -21.109 50.271 23.745  1.00 18.87 ? 358 GLU B C   1 
ATOM   7079 O O   . GLU B 1 358 ? -20.303 50.832 22.991  1.00 19.45 ? 358 GLU B O   1 
ATOM   7080 C CB  . GLU B 1 358 ? -21.887 48.202 22.582  1.00 18.22 ? 358 GLU B CB  1 
ATOM   7081 C CG  . GLU B 1 358 ? -23.346 48.634 22.523  1.00 15.66 ? 358 GLU B CG  1 
ATOM   7082 C CD  . GLU B 1 358 ? -24.230 47.651 21.747  1.00 27.11 ? 358 GLU B CD  1 
ATOM   7083 O OE1 . GLU B 1 358 ? -24.953 48.106 20.838  1.00 25.43 ? 358 GLU B OE1 1 
ATOM   7084 O OE2 . GLU B 1 358 ? -24.190 46.433 22.047  1.00 20.32 ? 358 GLU B OE2 1 
ATOM   7085 N N   . TYR B 1 359 ? -21.954 50.954 24.525  1.00 16.25 ? 359 TYR B N   1 
ATOM   7086 C CA  . TYR B 1 359 ? -21.969 52.410 24.559  1.00 15.59 ? 359 TYR B CA  1 
ATOM   7087 C C   . TYR B 1 359 ? -21.001 52.981 25.584  1.00 16.41 ? 359 TYR B C   1 
ATOM   7088 O O   . TYR B 1 359 ? -20.809 54.195 25.612  1.00 18.47 ? 359 TYR B O   1 
ATOM   7089 C CB  . TYR B 1 359 ? -23.393 52.918 24.855  1.00 15.40 ? 359 TYR B CB  1 
ATOM   7090 C CG  . TYR B 1 359 ? -24.366 52.559 23.746  1.00 19.40 ? 359 TYR B CG  1 
ATOM   7091 C CD1 . TYR B 1 359 ? -24.441 53.335 22.599  1.00 27.39 ? 359 TYR B CD1 1 
ATOM   7092 C CD2 . TYR B 1 359 ? -25.167 51.438 23.832  1.00 18.73 ? 359 TYR B CD2 1 
ATOM   7093 C CE1 . TYR B 1 359 ? -25.292 53.012 21.562  1.00 25.21 ? 359 TYR B CE1 1 
ATOM   7094 C CE2 . TYR B 1 359 ? -26.045 51.105 22.780  1.00 21.29 ? 359 TYR B CE2 1 
ATOM   7095 C CZ  . TYR B 1 359 ? -26.093 51.901 21.658  1.00 28.35 ? 359 TYR B CZ  1 
ATOM   7096 O OH  . TYR B 1 359 ? -26.947 51.609 20.604  1.00 30.97 ? 359 TYR B OH  1 
ATOM   7097 N N   . TYR B 1 360 ? -20.416 52.147 26.434  1.00 17.40 ? 360 TYR B N   1 
ATOM   7098 C CA  . TYR B 1 360 ? -19.463 52.588 27.440  1.00 19.36 ? 360 TYR B CA  1 
ATOM   7099 C C   . TYR B 1 360 ? -18.044 52.560 26.891  1.00 21.96 ? 360 TYR B C   1 
ATOM   7100 O O   . TYR B 1 360 ? -17.708 51.744 26.024  1.00 18.67 ? 360 TYR B O   1 
ATOM   7101 C CB  . TYR B 1 360 ? -19.498 51.677 28.665  1.00 14.62 ? 360 TYR B CB  1 
ATOM   7102 C CG  . TYR B 1 360 ? -20.640 51.784 29.638  1.00 15.49 ? 360 TYR B CG  1 
ATOM   7103 C CD1 . TYR B 1 360 ? -21.950 51.472 29.264  1.00 13.61 ? 360 TYR B CD1 1 
ATOM   7104 C CD2 . TYR B 1 360 ? -20.392 52.119 30.968  1.00 15.08 ? 360 TYR B CD2 1 
ATOM   7105 C CE1 . TYR B 1 360 ? -22.993 51.535 30.190  1.00 13.19 ? 360 TYR B CE1 1 
ATOM   7106 C CE2 . TYR B 1 360 ? -21.414 52.164 31.913  1.00 14.48 ? 360 TYR B CE2 1 
ATOM   7107 C CZ  . TYR B 1 360 ? -22.709 51.868 31.523  1.00 18.07 ? 360 TYR B CZ  1 
ATOM   7108 O OH  . TYR B 1 360 ? -23.714 51.932 32.450  1.00 16.92 ? 360 TYR B OH  1 
ATOM   7109 N N   . GLU B 1 361 ? -17.205 53.450 27.427  1.00 19.51 ? 361 GLU B N   1 
ATOM   7110 C CA  . GLU B 1 361 ? -15.767 53.387 27.174  1.00 23.86 ? 361 GLU B CA  1 
ATOM   7111 C C   . GLU B 1 361 ? -15.230 51.986 27.466  1.00 22.40 ? 361 GLU B C   1 
ATOM   7112 O O   . GLU B 1 361 ? -15.513 51.418 28.525  1.00 20.27 ? 361 GLU B O   1 
ATOM   7113 C CB  . GLU B 1 361 ? -15.055 54.430 28.047  1.00 33.08 ? 361 GLU B CB  1 
ATOM   7114 C CG  . GLU B 1 361 ? -13.534 54.271 28.084  1.00 49.01 ? 361 GLU B CG  1 
ATOM   7115 C CD  . GLU B 1 361 ? -12.814 55.602 27.979  1.00 63.44 ? 361 GLU B CD  1 
ATOM   7116 O OE1 . GLU B 1 361 ? -13.514 56.633 27.901  1.00 63.57 ? 361 GLU B OE1 1 
ATOM   7117 O OE2 . GLU B 1 361 ? -11.556 55.622 27.970  1.00 71.39 ? 361 GLU B OE2 1 
ATOM   7118 N N   . GLU B 1 362 ? -14.490 51.419 26.508  1.00 19.79 ? 362 GLU B N   1 
ATOM   7119 C CA  . GLU B 1 362 ? -13.884 50.095 26.651  1.00 21.32 ? 362 GLU B CA  1 
ATOM   7120 C C   . GLU B 1 362 ? -14.890 49.042 27.111  1.00 16.44 ? 362 GLU B C   1 
ATOM   7121 O O   . GLU B 1 362 ? -14.603 48.203 27.972  1.00 16.72 ? 362 GLU B O   1 
ATOM   7122 C CB  . GLU B 1 362 ? -12.644 50.140 27.568  1.00 24.14 ? 362 GLU B CB  1 
ATOM   7123 C CG  . GLU B 1 362 ? -11.536 51.037 27.011  1.00 39.56 ? 362 GLU B CG  1 
ATOM   7124 C CD  . GLU B 1 362 ? -10.434 51.332 28.005  1.00 57.08 ? 362 GLU B CD  1 
ATOM   7125 O OE1 . GLU B 1 362 ? -9.318  50.805 27.798  1.00 64.94 ? 362 GLU B OE1 1 
ATOM   7126 O OE2 . GLU B 1 362 ? -10.670 52.097 28.967  1.00 55.89 ? 362 GLU B OE2 1 
ATOM   7127 N N   . ASN B 1 363 ? -16.080 49.084 26.520  1.00 17.39 ? 363 ASN B N   1 
ATOM   7128 C CA  . ASN B 1 363 ? -17.084 48.044 26.708  1.00 15.90 ? 363 ASN B CA  1 
ATOM   7129 C C   . ASN B 1 363 ? -17.511 47.900 28.172  1.00 19.61 ? 363 ASN B C   1 
ATOM   7130 O O   . ASN B 1 363 ? -17.870 46.806 28.626  1.00 17.47 ? 363 ASN B O   1 
ATOM   7131 C CB  . ASN B 1 363 ? -16.594 46.695 26.172  1.00 15.61 ? 363 ASN B CB  1 
ATOM   7132 C CG  . ASN B 1 363 ? -17.721 45.697 26.009  1.00 20.08 ? 363 ASN B CG  1 
ATOM   7133 O OD1 . ASN B 1 363 ? -18.835 46.051 25.608  1.00 20.17 ? 363 ASN B OD1 1 
ATOM   7134 N ND2 . ASN B 1 363 ? -17.444 44.445 26.350  1.00 23.76 ? 363 ASN B ND2 1 
ATOM   7135 N N   . GLY B 1 364 ? -17.488 48.998 28.916  1.00 13.69 ? 364 GLY B N   1 
ATOM   7136 C CA  . GLY B 1 364 ? -17.933 48.958 30.292  1.00 12.82 ? 364 GLY B CA  1 
ATOM   7137 C C   . GLY B 1 364 ? -16.971 48.321 31.264  1.00 19.00 ? 364 GLY B C   1 
ATOM   7138 O O   . GLY B 1 364 ? -17.299 48.218 32.443  1.00 19.38 ? 364 GLY B O   1 
ATOM   7139 N N   . ILE B 1 365 ? -15.794 47.890 30.811  1.00 15.48 ? 365 ILE B N   1 
ATOM   7140 C CA  . ILE B 1 365 ? -14.863 47.206 31.713  1.00 20.12 ? 365 ILE B CA  1 
ATOM   7141 C C   . ILE B 1 365 ? -14.376 48.125 32.827  1.00 19.33 ? 365 ILE B C   1 
ATOM   7142 O O   . ILE B 1 365 ? -14.428 47.716 34.002  1.00 19.94 ? 365 ILE B O   1 
ATOM   7143 C CB  . ILE B 1 365 ? -13.715 46.566 30.906  1.00 16.12 ? 365 ILE B CB  1 
ATOM   7144 C CG1 . ILE B 1 365 ? -14.295 45.524 29.956  1.00 18.40 ? 365 ILE B CG1 1 
ATOM   7145 C CG2 . ILE B 1 365 ? -12.710 45.937 31.876  1.00 17.30 ? 365 ILE B CG2 1 
ATOM   7146 C CD1 . ILE B 1 365 ? -13.342 45.108 28.829  1.00 24.23 ? 365 ILE B CD1 1 
ATOM   7147 N N   . PRO B 1 366 ? -13.928 49.357 32.557  1.00 15.02 ? 366 PRO B N   1 
ATOM   7148 C CA  . PRO B 1 366 ? -13.592 50.240 33.682  1.00 15.74 ? 366 PRO B CA  1 
ATOM   7149 C C   . PRO B 1 366 ? -14.740 50.436 34.654  1.00 20.73 ? 366 PRO B C   1 
ATOM   7150 O O   . PRO B 1 366 ? -14.513 50.426 35.873  1.00 20.45 ? 366 PRO B O   1 
ATOM   7151 C CB  . PRO B 1 366 ? -13.180 51.549 32.995  1.00 23.86 ? 366 PRO B CB  1 
ATOM   7152 C CG  . PRO B 1 366 ? -12.657 51.108 31.658  1.00 23.12 ? 366 PRO B CG  1 
ATOM   7153 C CD  . PRO B 1 366 ? -13.570 49.968 31.261  1.00 15.84 ? 366 PRO B CD  1 
ATOM   7154 N N   . PHE B 1 367 ? -15.973 50.577 34.151  1.00 15.25 ? 367 PHE B N   1 
ATOM   7155 C CA  . PHE B 1 367 ? -17.124 50.772 35.025  1.00 19.14 ? 367 PHE B CA  1 
ATOM   7156 C C   . PHE B 1 367 ? -17.385 49.536 35.883  1.00 19.16 ? 367 PHE B C   1 
ATOM   7157 O O   . PHE B 1 367 ? -17.529 49.637 37.107  1.00 16.13 ? 367 PHE B O   1 
ATOM   7158 C CB  . PHE B 1 367 ? -18.376 51.132 34.205  1.00 17.51 ? 367 PHE B CB  1 
ATOM   7159 C CG  . PHE B 1 367 ? -19.631 51.182 35.029  1.00 15.34 ? 367 PHE B CG  1 
ATOM   7160 C CD1 . PHE B 1 367 ? -19.900 52.278 35.834  1.00 17.44 ? 367 PHE B CD1 1 
ATOM   7161 C CD2 . PHE B 1 367 ? -20.514 50.104 35.055  1.00 14.80 ? 367 PHE B CD2 1 
ATOM   7162 C CE1 . PHE B 1 367 ? -21.047 52.317 36.634  1.00 21.39 ? 367 PHE B CE1 1 
ATOM   7163 C CE2 . PHE B 1 367 ? -21.666 50.145 35.839  1.00 19.24 ? 367 PHE B CE2 1 
ATOM   7164 C CZ  . PHE B 1 367 ? -21.930 51.253 36.629  1.00 17.28 ? 367 PHE B CZ  1 
ATOM   7165 N N   . LEU B 1 368 ? -17.453 48.355 35.265  1.00 14.94 ? 368 LEU B N   1 
ATOM   7166 C CA  . LEU B 1 368 ? -17.801 47.171 36.040  1.00 13.17 ? 368 LEU B CA  1 
ATOM   7167 C C   . LEU B 1 368 ? -16.668 46.757 36.974  1.00 14.56 ? 368 LEU B C   1 
ATOM   7168 O O   . LEU B 1 368 ? -16.917 46.311 38.099  1.00 15.89 ? 368 LEU B O   1 
ATOM   7169 C CB  . LEU B 1 368 ? -18.180 46.027 35.098  1.00 16.50 ? 368 LEU B CB  1 
ATOM   7170 C CG  . LEU B 1 368 ? -19.568 46.188 34.458  1.00 17.50 ? 368 LEU B CG  1 
ATOM   7171 C CD1 . LEU B 1 368 ? -19.845 45.031 33.496  1.00 17.29 ? 368 LEU B CD1 1 
ATOM   7172 C CD2 . LEU B 1 368 ? -20.689 46.319 35.527  1.00 18.00 ? 368 LEU B CD2 1 
ATOM   7173 N N   . GLU B 1 369 ? -15.414 46.871 36.527  1.00 15.09 ? 369 GLU B N   1 
ATOM   7174 C CA  . GLU B 1 369 ? -14.308 46.552 37.431  1.00 18.47 ? 369 GLU B CA  1 
ATOM   7175 C C   . GLU B 1 369 ? -14.315 47.477 38.638  1.00 22.98 ? 369 GLU B C   1 
ATOM   7176 O O   . GLU B 1 369 ? -14.077 47.035 39.770  1.00 19.72 ? 369 GLU B O   1 
ATOM   7177 C CB  . GLU B 1 369 ? -12.979 46.625 36.692  1.00 21.45 ? 369 GLU B CB  1 
ATOM   7178 C CG  . GLU B 1 369 ? -12.812 45.443 35.745  1.00 19.78 ? 369 GLU B CG  1 
ATOM   7179 C CD  . GLU B 1 369 ? -11.438 45.374 35.122  1.00 24.36 ? 369 GLU B CD  1 
ATOM   7180 O OE1 . GLU B 1 369 ? -10.720 46.397 35.168  1.00 24.68 ? 369 GLU B OE1 1 
ATOM   7181 O OE2 . GLU B 1 369 ? -11.089 44.309 34.557  1.00 25.01 ? 369 GLU B OE2 1 
ATOM   7182 N N   . LYS B 1 370 ? -14.674 48.746 38.428  1.00 16.04 ? 370 LYS B N   1 
ATOM   7183 C CA  . LYS B 1 370 ? -14.737 49.690 39.538  1.00 19.03 ? 370 LYS B CA  1 
ATOM   7184 C C   . LYS B 1 370 ? -15.911 49.381 40.452  1.00 16.17 ? 370 LYS B C   1 
ATOM   7185 O O   . LYS B 1 370 ? -15.762 49.356 41.682  1.00 18.36 ? 370 LYS B O   1 
ATOM   7186 C CB  . LYS B 1 370 ? -14.857 51.116 39.012  1.00 18.54 ? 370 LYS B CB  1 
ATOM   7187 C CG  . LYS B 1 370 ? -14.824 52.158 40.127  1.00 23.78 ? 370 LYS B CG  1 
ATOM   7188 C CD  . LYS B 1 370 ? -13.468 52.158 40.851  1.00 38.60 ? 370 LYS B CD  1 
ATOM   7189 C CE  . LYS B 1 370 ? -13.596 52.706 42.265  1.00 43.76 ? 370 LYS B CE  1 
ATOM   7190 N NZ  . LYS B 1 370 ? -12.270 52.948 42.921  1.00 41.24 ? 370 LYS B NZ  1 
ATOM   7191 N N   . LEU B 1 371 ? -17.102 49.202 39.863  1.00 16.51 ? 371 LEU B N   1 
ATOM   7192 C CA  . LEU B 1 371 ? -18.292 48.881 40.648  1.00 14.76 ? 371 LEU B CA  1 
ATOM   7193 C C   . LEU B 1 371 ? -18.088 47.615 41.472  1.00 12.86 ? 371 LEU B C   1 
ATOM   7194 O O   . LEU B 1 371 ? -18.372 47.582 42.677  1.00 14.62 ? 371 LEU B O   1 
ATOM   7195 C CB  . LEU B 1 371 ? -19.494 48.705 39.715  1.00 13.38 ? 371 LEU B CB  1 
ATOM   7196 C CG  . LEU B 1 371 ? -20.813 48.303 40.377  1.00 15.13 ? 371 LEU B CG  1 
ATOM   7197 C CD1 . LEU B 1 371 ? -21.270 49.441 41.262  1.00 15.77 ? 371 LEU B CD1 1 
ATOM   7198 C CD2 . LEU B 1 371 ? -21.850 48.042 39.320  1.00 13.36 ? 371 LEU B CD2 1 
ATOM   7199 N N   . TYR B 1 372 ? -17.610 46.555 40.832  1.00 12.78 ? 372 TYR B N   1 
ATOM   7200 C CA  . TYR B 1 372 ? -17.461 45.279 41.524  1.00 17.51 ? 372 TYR B CA  1 
ATOM   7201 C C   . TYR B 1 372 ? -16.308 45.314 42.524  1.00 15.05 ? 372 TYR B C   1 
ATOM   7202 O O   . TYR B 1 372 ? -16.381 44.674 43.583  1.00 17.12 ? 372 TYR B O   1 
ATOM   7203 C CB  . TYR B 1 372 ? -17.251 44.167 40.485  1.00 18.58 ? 372 TYR B CB  1 
ATOM   7204 C CG  . TYR B 1 372 ? -18.425 43.878 39.559  1.00 16.11 ? 372 TYR B CG  1 
ATOM   7205 C CD1 . TYR B 1 372 ? -19.714 44.320 39.854  1.00 13.72 ? 372 TYR B CD1 1 
ATOM   7206 C CD2 . TYR B 1 372 ? -18.235 43.135 38.380  1.00 13.95 ? 372 TYR B CD2 1 
ATOM   7207 C CE1 . TYR B 1 372 ? -20.795 44.037 39.013  1.00 13.19 ? 372 TYR B CE1 1 
ATOM   7208 C CE2 . TYR B 1 372 ? -19.305 42.842 37.540  1.00 14.26 ? 372 TYR B CE2 1 
ATOM   7209 C CZ  . TYR B 1 372 ? -20.580 43.288 37.852  1.00 14.71 ? 372 TYR B CZ  1 
ATOM   7210 O OH  . TYR B 1 372 ? -21.641 42.976 37.013  1.00 13.79 ? 372 TYR B OH  1 
ATOM   7211 N N   . SER B 1 373 ? -15.235 46.048 42.205  1.00 16.35 ? 373 SER B N   1 
ATOM   7212 C CA  . SER B 1 373 ? -14.149 46.245 43.161  1.00 18.29 ? 373 SER B CA  1 
ATOM   7213 C C   . SER B 1 373 ? -14.654 46.945 44.419  1.00 21.61 ? 373 SER B C   1 
ATOM   7214 O O   . SER B 1 373 ? -14.273 46.588 45.547  1.00 22.52 ? 373 SER B O   1 
ATOM   7215 C CB  . SER B 1 373 ? -13.031 47.077 42.521  1.00 25.10 ? 373 SER B CB  1 
ATOM   7216 O OG  . SER B 1 373 ? -12.010 47.332 43.458  1.00 47.93 ? 373 SER B OG  1 
ATOM   7217 N N   . THR B 1 374 ? -15.507 47.955 44.237  1.00 16.44 ? 374 THR B N   1 
ATOM   7218 C CA  . THR B 1 374 ? -16.056 48.678 45.377  1.00 19.42 ? 374 THR B CA  1 
ATOM   7219 C C   . THR B 1 374 ? -17.005 47.797 46.174  1.00 18.57 ? 374 THR B C   1 
ATOM   7220 O O   . THR B 1 374 ? -16.881 47.682 47.397  1.00 19.97 ? 374 THR B O   1 
ATOM   7221 C CB  . THR B 1 374 ? -16.761 49.940 44.894  1.00 21.19 ? 374 THR B CB  1 
ATOM   7222 O OG1 . THR B 1 374 ? -15.834 50.753 44.167  1.00 21.58 ? 374 THR B OG1 1 
ATOM   7223 C CG2 . THR B 1 374 ? -17.275 50.749 46.072  1.00 20.09 ? 374 THR B CG2 1 
ATOM   7224 N N   . LEU B 1 375 ? -17.946 47.144 45.491  1.00 17.46 ? 375 LEU B N   1 
ATOM   7225 C CA  . LEU B 1 375 ? -18.933 46.327 46.190  1.00 19.22 ? 375 LEU B CA  1 
ATOM   7226 C C   . LEU B 1 375 ? -18.274 45.227 47.020  1.00 20.07 ? 375 LEU B C   1 
ATOM   7227 O O   . LEU B 1 375 ? -18.684 44.984 48.160  1.00 19.74 ? 375 LEU B O   1 
ATOM   7228 C CB  . LEU B 1 375 ? -19.927 45.744 45.179  1.00 20.66 ? 375 LEU B CB  1 
ATOM   7229 C CG  . LEU B 1 375 ? -20.927 46.756 44.596  1.00 19.66 ? 375 LEU B CG  1 
ATOM   7230 C CD1 . LEU B 1 375 ? -21.828 46.106 43.573  1.00 16.77 ? 375 LEU B CD1 1 
ATOM   7231 C CD2 . LEU B 1 375 ? -21.765 47.433 45.697  1.00 19.27 ? 375 LEU B CD2 1 
ATOM   7232 N N   . GLU B 1 376 ? -17.241 44.560 46.485  1.00 17.97 ? 376 GLU B N   1 
ATOM   7233 C CA  . GLU B 1 376 ? -16.641 43.445 47.226  1.00 22.29 ? 376 GLU B CA  1 
ATOM   7234 C C   . GLU B 1 376 ? -16.023 43.888 48.549  1.00 25.02 ? 376 GLU B C   1 
ATOM   7235 O O   . GLU B 1 376 ? -15.846 43.057 49.448  1.00 23.78 ? 376 GLU B O   1 
ATOM   7236 C CB  . GLU B 1 376 ? -15.592 42.714 46.361  1.00 21.90 ? 376 GLU B CB  1 
ATOM   7237 C CG  . GLU B 1 376 ? -14.288 43.442 46.125  1.00 26.73 ? 376 GLU B CG  1 
ATOM   7238 C CD  . GLU B 1 376 ? -13.281 42.593 45.350  1.00 31.73 ? 376 GLU B CD  1 
ATOM   7239 O OE1 . GLU B 1 376 ? -13.518 41.373 45.177  1.00 27.65 ? 376 GLU B OE1 1 
ATOM   7240 O OE2 . GLU B 1 376 ? -12.242 43.140 44.925  1.00 33.02 ? 376 GLU B OE2 1 
ATOM   7241 N N   . LYS B 1 377 ? -15.688 45.169 48.688  1.00 20.17 ? 377 LYS B N   1 
ATOM   7242 C CA  . LYS B 1 377 ? -15.134 45.675 49.927  1.00 20.89 ? 377 LYS B CA  1 
ATOM   7243 C C   . LYS B 1 377 ? -16.194 46.206 50.882  1.00 25.13 ? 377 LYS B C   1 
ATOM   7244 O O   . LYS B 1 377 ? -15.903 46.358 52.064  1.00 24.03 ? 377 LYS B O   1 
ATOM   7245 C CB  . LYS B 1 377 ? -14.126 46.789 49.638  1.00 24.78 ? 377 LYS B CB  1 
ATOM   7246 C CG  . LYS B 1 377 ? -12.876 46.309 48.892  1.00 34.70 ? 377 LYS B CG  1 
ATOM   7247 C CD  . LYS B 1 377 ? -12.222 47.427 48.089  1.00 42.17 ? 377 LYS B CD  1 
ATOM   7248 C CE  . LYS B 1 377 ? -11.180 46.860 47.102  1.00 47.13 ? 377 LYS B CE  1 
ATOM   7249 N NZ  . LYS B 1 377 ? -11.725 45.750 46.242  1.00 33.73 ? 377 LYS B NZ  1 
ATOM   7250 N N   . GLU B 1 378 ? -17.400 46.529 50.427  1.00 22.07 ? 378 GLU B N   1 
ATOM   7251 C CA  . GLU B 1 378 ? -18.355 47.119 51.366  1.00 20.75 ? 378 GLU B CA  1 
ATOM   7252 C C   . GLU B 1 378 ? -18.978 46.047 52.253  1.00 26.76 ? 378 GLU B C   1 
ATOM   7253 O O   . GLU B 1 378 ? -19.398 44.986 51.777  1.00 32.51 ? 378 GLU B O   1 
ATOM   7254 C CB  . GLU B 1 378 ? -19.468 47.876 50.637  1.00 20.34 ? 378 GLU B CB  1 
ATOM   7255 C CG  . GLU B 1 378 ? -19.001 48.918 49.652  1.00 19.91 ? 378 GLU B CG  1 
ATOM   7256 C CD  . GLU B 1 378 ? -18.156 50.013 50.288  1.00 37.30 ? 378 GLU B CD  1 
ATOM   7257 O OE1 . GLU B 1 378 ? -18.263 50.237 51.512  1.00 32.42 ? 378 GLU B OE1 1 
ATOM   7258 O OE2 . GLU B 1 378 ? -17.358 50.646 49.552  1.00 40.92 ? 378 GLU B OE2 1 
ATOM   7259 N N   . GLU B 1 379 ? -19.047 46.337 53.553  1.00 25.84 ? 379 GLU B N   1 
ATOM   7260 C CA  . GLU B 1 379 ? -19.694 45.435 54.489  1.00 29.53 ? 379 GLU B CA  1 
ATOM   7261 C C   . GLU B 1 379 ? -21.156 45.781 54.720  1.00 28.78 ? 379 GLU B C   1 
ATOM   7262 O O   . GLU B 1 379 ? -21.928 44.899 55.122  1.00 31.02 ? 379 GLU B O   1 
ATOM   7263 C CB  . GLU B 1 379 ? -18.957 45.445 55.828  1.00 34.68 ? 379 GLU B CB  1 
ATOM   7264 C CG  . GLU B 1 379 ? -17.503 44.963 55.756  1.00 42.39 ? 379 GLU B CG  1 
ATOM   7265 C CD  . GLU B 1 379 ? -16.823 45.051 57.111  1.00 45.57 ? 379 GLU B CD  1 
ATOM   7266 O OE1 . GLU B 1 379 ? -17.534 45.365 58.096  1.00 63.09 ? 379 GLU B OE1 1 
ATOM   7267 O OE2 . GLU B 1 379 ? -15.597 44.810 57.199  1.00 42.97 ? 379 GLU B OE2 1 
ATOM   7268 N N   . TRP B 1 380 ? -21.555 47.037 54.491  1.00 23.35 ? 380 TRP B N   1 
ATOM   7269 C CA  . TRP B 1 380 ? -22.931 47.445 54.731  1.00 22.60 ? 380 TRP B CA  1 
ATOM   7270 C C   . TRP B 1 380 ? -23.838 47.143 53.546  1.00 24.14 ? 380 TRP B C   1 
ATOM   7271 O O   . TRP B 1 380 ? -25.062 47.203 53.702  1.00 24.48 ? 380 TRP B O   1 
ATOM   7272 C CB  . TRP B 1 380 ? -22.998 48.937 55.083  1.00 23.18 ? 380 TRP B CB  1 
ATOM   7273 C CG  . TRP B 1 380 ? -22.529 49.820 53.979  1.00 22.84 ? 380 TRP B CG  1 
ATOM   7274 C CD1 . TRP B 1 380 ? -21.233 50.134 53.666  1.00 22.97 ? 380 TRP B CD1 1 
ATOM   7275 C CD2 . TRP B 1 380 ? -23.350 50.478 53.009  1.00 20.73 ? 380 TRP B CD2 1 
ATOM   7276 N NE1 . TRP B 1 380 ? -21.200 50.964 52.566  1.00 25.51 ? 380 TRP B NE1 1 
ATOM   7277 C CE2 . TRP B 1 380 ? -22.482 51.184 52.137  1.00 20.93 ? 380 TRP B CE2 1 
ATOM   7278 C CE3 . TRP B 1 380 ? -24.731 50.555 52.803  1.00 23.01 ? 380 TRP B CE3 1 
ATOM   7279 C CZ2 . TRP B 1 380 ? -22.950 51.959 51.082  1.00 18.94 ? 380 TRP B CZ2 1 
ATOM   7280 C CZ3 . TRP B 1 380 ? -25.196 51.316 51.743  1.00 20.88 ? 380 TRP B CZ3 1 
ATOM   7281 C CH2 . TRP B 1 380 ? -24.308 52.012 50.902  1.00 23.99 ? 380 TRP B CH2 1 
ATOM   7282 N N   . ILE B 1 381 ? -23.262 46.843 52.378  1.00 19.76 ? 381 ILE B N   1 
ATOM   7283 C CA  . ILE B 1 381 ? -23.975 46.263 51.245  1.00 17.51 ? 381 ILE B CA  1 
ATOM   7284 C C   . ILE B 1 381 ? -23.629 44.786 51.192  1.00 23.50 ? 381 ILE B C   1 
ATOM   7285 O O   . ILE B 1 381 ? -22.444 44.413 51.252  1.00 22.91 ? 381 ILE B O   1 
ATOM   7286 C CB  . ILE B 1 381 ? -23.576 46.938 49.918  1.00 16.13 ? 381 ILE B CB  1 
ATOM   7287 C CG1 . ILE B 1 381 ? -23.974 48.414 49.905  1.00 19.12 ? 381 ILE B CG1 1 
ATOM   7288 C CG2 . ILE B 1 381 ? -24.205 46.193 48.734  1.00 16.81 ? 381 ILE B CG2 1 
ATOM   7289 C CD1 . ILE B 1 381 ? -23.249 49.201 48.809  1.00 22.42 ? 381 ILE B CD1 1 
ATOM   7290 N N   . GLU B 1 382 ? -24.643 43.943 51.063  1.00 18.72 ? 382 GLU B N   1 
ATOM   7291 C CA  . GLU B 1 382 ? -24.437 42.521 50.824  1.00 18.32 ? 382 GLU B CA  1 
ATOM   7292 C C   . GLU B 1 382 ? -25.095 42.175 49.490  1.00 17.61 ? 382 GLU B C   1 
ATOM   7293 O O   . GLU B 1 382 ? -26.323 42.264 49.364  1.00 19.29 ? 382 GLU B O   1 
ATOM   7294 C CB  . GLU B 1 382 ? -25.024 41.693 51.968  1.00 22.45 ? 382 GLU B CB  1 
ATOM   7295 C CG  . GLU B 1 382 ? -24.879 40.202 51.783  1.00 31.52 ? 382 GLU B CG  1 
ATOM   7296 C CD  . GLU B 1 382 ? -24.958 39.432 53.087  1.00 48.73 ? 382 GLU B CD  1 
ATOM   7297 O OE1 . GLU B 1 382 ? -25.225 40.048 54.148  1.00 46.59 ? 382 GLU B OE1 1 
ATOM   7298 O OE2 . GLU B 1 382 ? -24.757 38.200 53.038  1.00 59.54 ? 382 GLU B OE2 1 
ATOM   7299 N N   . THR B 1 383 ? -24.299 41.791 48.480  1.00 16.50 ? 383 THR B N   1 
ATOM   7300 C CA  . THR B 1 383 ? -24.905 41.274 47.249  1.00 15.55 ? 383 THR B CA  1 
ATOM   7301 C C   . THR B 1 383 ? -25.382 39.844 47.473  1.00 20.92 ? 383 THR B C   1 
ATOM   7302 O O   . THR B 1 383 ? -24.722 39.064 48.168  1.00 17.64 ? 383 THR B O   1 
ATOM   7303 C CB  . THR B 1 383 ? -23.925 41.299 46.069  1.00 15.12 ? 383 THR B CB  1 
ATOM   7304 O OG1 . THR B 1 383 ? -22.740 40.541 46.384  1.00 15.99 ? 383 THR B OG1 1 
ATOM   7305 C CG2 . THR B 1 383 ? -23.548 42.731 45.740  1.00 19.13 ? 383 THR B CG2 1 
ATOM   7306 N N   . LEU B 1 384 ? -26.528 39.503 46.870  1.00 14.40 ? 384 LEU B N   1 
ATOM   7307 C CA  . LEU B 1 384 ? -27.190 38.222 47.104  1.00 15.21 ? 384 LEU B CA  1 
ATOM   7308 C C   . LEU B 1 384 ? -27.384 37.460 45.806  1.00 15.64 ? 384 LEU B C   1 
ATOM   7309 O O   . LEU B 1 384 ? -27.572 38.057 44.735  1.00 18.07 ? 384 LEU B O   1 
ATOM   7310 C CB  . LEU B 1 384 ? -28.578 38.386 47.744  1.00 15.89 ? 384 LEU B CB  1 
ATOM   7311 C CG  . LEU B 1 384 ? -28.630 39.068 49.113  1.00 20.13 ? 384 LEU B CG  1 
ATOM   7312 C CD1 . LEU B 1 384 ? -30.065 39.146 49.592  1.00 23.97 ? 384 LEU B CD1 1 
ATOM   7313 C CD2 . LEU B 1 384 ? -27.754 38.314 50.119  1.00 19.73 ? 384 LEU B CD2 1 
ATOM   7314 N N   . THR B 1 385 ? -27.384 36.136 45.927  1.00 15.49 ? 385 THR B N   1 
ATOM   7315 C CA  . THR B 1 385 ? -27.966 35.307 44.873  1.00 21.74 ? 385 THR B CA  1 
ATOM   7316 C C   . THR B 1 385 ? -29.492 35.417 44.904  1.00 19.47 ? 385 THR B C   1 
ATOM   7317 O O   . THR B 1 385 ? -30.089 35.861 45.888  1.00 17.59 ? 385 THR B O   1 
ATOM   7318 C CB  . THR B 1 385 ? -27.560 33.838 45.023  1.00 16.47 ? 385 THR B CB  1 
ATOM   7319 O OG1 . THR B 1 385 ? -28.126 33.293 46.234  1.00 17.95 ? 385 THR B OG1 1 
ATOM   7320 C CG2 . THR B 1 385 ? -25.995 33.678 45.043  1.00 16.38 ? 385 THR B CG2 1 
ATOM   7321 N N   . LEU B 1 386 ? -30.133 35.004 43.803  1.00 18.10 ? 386 LEU B N   1 
ATOM   7322 C CA  . LEU B 1 386 ? -31.595 34.938 43.789  1.00 18.17 ? 386 LEU B CA  1 
ATOM   7323 C C   . LEU B 1 386 ? -32.101 34.036 44.901  1.00 18.92 ? 386 LEU B C   1 
ATOM   7324 O O   . LEU B 1 386 ? -33.101 34.343 45.565  1.00 20.10 ? 386 LEU B O   1 
ATOM   7325 C CB  . LEU B 1 386 ? -32.102 34.419 42.444  1.00 18.71 ? 386 LEU B CB  1 
ATOM   7326 C CG  . LEU B 1 386 ? -31.702 35.254 41.230  1.00 15.62 ? 386 LEU B CG  1 
ATOM   7327 C CD1 . LEU B 1 386 ? -32.389 34.688 39.911  1.00 14.47 ? 386 LEU B CD1 1 
ATOM   7328 C CD2 . LEU B 1 386 ? -32.093 36.722 41.447  1.00 17.58 ? 386 LEU B CD2 1 
ATOM   7329 N N   . GLU B 1 387 ? -31.410 32.916 45.112  1.00 18.53 ? 387 GLU B N   1 
ATOM   7330 C CA  . GLU B 1 387 ? -31.758 31.983 46.177  1.00 20.37 ? 387 GLU B CA  1 
ATOM   7331 C C   . GLU B 1 387 ? -31.649 32.636 47.547  1.00 20.84 ? 387 GLU B C   1 
ATOM   7332 O O   . GLU B 1 387 ? -32.512 32.431 48.410  1.00 22.49 ? 387 GLU B O   1 
ATOM   7333 C CB  . GLU B 1 387 ? -30.851 30.761 46.079  1.00 25.54 ? 387 GLU B CB  1 
ATOM   7334 C CG  . GLU B 1 387 ? -31.311 29.553 46.854  1.00 32.09 ? 387 GLU B CG  1 
ATOM   7335 C CD  . GLU B 1 387 ? -30.623 29.420 48.187  1.00 56.51 ? 387 GLU B CD  1 
ATOM   7336 O OE1 . GLU B 1 387 ? -30.131 30.445 48.720  1.00 68.96 ? 387 GLU B OE1 1 
ATOM   7337 O OE2 . GLU B 1 387 ? -30.537 28.282 48.696  1.00 60.97 ? 387 GLU B OE2 1 
ATOM   7338 N N   . GLU B 1 388 ? -30.589 33.413 47.779  1.00 19.89 ? 388 GLU B N   1 
ATOM   7339 C CA  . GLU B 1 388 ? -30.473 34.097 49.064  1.00 26.15 ? 388 GLU B CA  1 
ATOM   7340 C C   . GLU B 1 388 ? -31.567 35.148 49.226  1.00 24.58 ? 388 GLU B C   1 
ATOM   7341 O O   . GLU B 1 388 ? -32.114 35.314 50.322  1.00 27.16 ? 388 GLU B O   1 
ATOM   7342 C CB  . GLU B 1 388 ? -29.084 34.722 49.206  1.00 19.60 ? 388 GLU B CB  1 
ATOM   7343 C CG  . GLU B 1 388 ? -27.979 33.681 49.417  1.00 25.11 ? 388 GLU B CG  1 
ATOM   7344 C CD  . GLU B 1 388 ? -26.570 34.250 49.227  1.00 30.77 ? 388 GLU B CD  1 
ATOM   7345 O OE1 . GLU B 1 388 ? -26.422 35.309 48.574  1.00 20.78 ? 388 GLU B OE1 1 
ATOM   7346 O OE2 . GLU B 1 388 ? -25.606 33.633 49.754  1.00 38.56 ? 388 GLU B OE2 1 
ATOM   7347 N N   . ALA B 1 389 ? -31.892 35.872 48.148  1.00 23.60 ? 389 ALA B N   1 
ATOM   7348 C CA  . ALA B 1 389 ? -32.953 36.875 48.219  1.00 23.03 ? 389 ALA B CA  1 
ATOM   7349 C C   . ALA B 1 389 ? -34.291 36.233 48.548  1.00 23.53 ? 389 ALA B C   1 
ATOM   7350 O O   . ALA B 1 389 ? -35.116 36.814 49.267  1.00 27.09 ? 389 ALA B O   1 
ATOM   7351 C CB  . ALA B 1 389 ? -33.045 37.647 46.905  1.00 19.20 ? 389 ALA B CB  1 
ATOM   7352 N N   . MET B 1 390 ? -34.517 35.022 48.045  1.00 22.21 ? 390 MET B N   1 
ATOM   7353 C CA  . MET B 1 390 ? -35.797 34.370 48.264  1.00 23.46 ? 390 MET B CA  1 
ATOM   7354 C C   . MET B 1 390 ? -35.931 33.863 49.691  1.00 31.88 ? 390 MET B C   1 
ATOM   7355 O O   . MET B 1 390 ? -37.041 33.856 50.244  1.00 32.70 ? 390 MET B O   1 
ATOM   7356 C CB  . MET B 1 390 ? -35.971 33.213 47.280  1.00 25.47 ? 390 MET B CB  1 
ATOM   7357 C CG  . MET B 1 390 ? -37.199 32.367 47.555  1.00 38.15 ? 390 MET B CG  1 
ATOM   7358 S SD  . MET B 1 390 ? -37.560 31.252 46.195  1.00 58.94 ? 390 MET B SD  1 
ATOM   7359 C CE  . MET B 1 390 ? -36.571 29.818 46.631  1.00 54.73 ? 390 MET B CE  1 
ATOM   7360 N N   . ARG B 1 391 ? -34.829 33.442 50.311  1.00 33.42 ? 391 ARG B N   1 
ATOM   7361 C CA  . ARG B 1 391 ? -34.919 32.801 51.618  1.00 34.55 ? 391 ARG B CA  1 
ATOM   7362 C C   . ARG B 1 391 ? -34.532 33.702 52.782  1.00 31.22 ? 391 ARG B C   1 
ATOM   7363 O O   . ARG B 1 391 ? -34.714 33.293 53.936  1.00 31.90 ? 391 ARG B O   1 
ATOM   7364 C CB  . ARG B 1 391 ? -34.047 31.538 51.657  1.00 40.69 ? 391 ARG B CB  1 
ATOM   7365 C CG  . ARG B 1 391 ? -34.413 30.498 50.603  1.00 47.71 ? 391 ARG B CG  1 
ATOM   7366 C CD  . ARG B 1 391 ? -33.188 29.726 50.167  1.00 56.64 ? 391 ARG B CD  1 
ATOM   7367 N NE  . ARG B 1 391 ? -33.208 28.320 50.550  1.00 64.64 ? 391 ARG B NE  1 
ATOM   7368 C CZ  . ARG B 1 391 ? -32.150 27.645 51.001  1.00 65.45 ? 391 ARG B CZ  1 
ATOM   7369 N NH1 . ARG B 1 391 ? -30.971 28.259 51.117  1.00 65.29 ? 391 ARG B NH1 1 
ATOM   7370 N NH2 . ARG B 1 391 ? -32.256 26.364 51.314  1.00 64.31 ? 391 ARG B NH2 1 
ATOM   7371 N N   . LYS B 1 392 ? -34.026 34.903 52.520  1.00 30.86 ? 392 LYS B N   1 
ATOM   7372 C CA  . LYS B 1 392 ? -33.566 35.781 53.593  1.00 34.82 ? 392 LYS B CA  1 
ATOM   7373 C C   . LYS B 1 392 ? -34.695 36.088 54.565  1.00 30.83 ? 392 LYS B C   1 
ATOM   7374 O O   . LYS B 1 392 ? -35.766 36.545 54.167  1.00 30.82 ? 392 LYS B O   1 
ATOM   7375 C CB  . LYS B 1 392 ? -33.017 37.085 53.014  1.00 41.27 ? 392 LYS B CB  1 
ATOM   7376 C CG  . LYS B 1 392 ? -31.835 37.645 53.787  1.00 51.75 ? 392 LYS B CG  1 
ATOM   7377 C CD  . LYS B 1 392 ? -30.620 36.767 53.573  1.00 51.27 ? 392 LYS B CD  1 
ATOM   7378 C CE  . LYS B 1 392 ? -29.378 37.351 54.210  1.00 50.82 ? 392 LYS B CE  1 
ATOM   7379 N NZ  . LYS B 1 392 ? -28.173 36.962 53.425  1.00 57.53 ? 392 LYS B NZ  1 
ATOM   7380 N N   . GLU B 1 393 ? -34.451 35.853 55.849  1.00 34.23 ? 393 GLU B N   1 
ATOM   7381 C CA  . GLU B 1 393 ? -35.520 36.031 56.823  1.00 43.54 ? 393 GLU B CA  1 
ATOM   7382 C C   . GLU B 1 393 ? -35.594 37.442 57.395  1.00 43.03 ? 393 GLU B C   1 
ATOM   7383 O O   . GLU B 1 393 ? -36.680 37.862 57.805  1.00 42.93 ? 393 GLU B O   1 
ATOM   7384 C CB  . GLU B 1 393 ? -35.369 35.011 57.954  1.00 49.93 ? 393 GLU B CB  1 
ATOM   7385 C CG  . GLU B 1 393 ? -35.301 33.574 57.447  1.00 56.20 ? 393 GLU B CG  1 
ATOM   7386 C CD  . GLU B 1 393 ? -36.132 32.603 58.271  1.00 68.59 ? 393 GLU B CD  1 
ATOM   7387 O OE1 . GLU B 1 393 ? -35.958 32.571 59.510  1.00 72.93 ? 393 GLU B OE1 1 
ATOM   7388 O OE2 . GLU B 1 393 ? -36.953 31.864 57.679  1.00 71.71 ? 393 GLU B OE2 1 
ATOM   7389 N N   . ASP B 1 394 ? -34.498 38.199 57.392  1.00 32.74 ? 394 ASP B N   1 
ATOM   7390 C CA  . ASP B 1 394 ? -34.482 39.504 58.059  1.00 36.17 ? 394 ASP B CA  1 
ATOM   7391 C C   . ASP B 1 394 ? -34.830 40.641 57.097  1.00 35.17 ? 394 ASP B C   1 
ATOM   7392 O O   . ASP B 1 394 ? -34.165 41.675 57.056  1.00 41.79 ? 394 ASP B O   1 
ATOM   7393 C CB  . ASP B 1 394 ? -33.123 39.736 58.714  1.00 44.41 ? 394 ASP B CB  1 
ATOM   7394 C CG  . ASP B 1 394 ? -31.959 39.281 57.834  1.00 52.41 ? 394 ASP B CG  1 
ATOM   7395 O OD1 . ASP B 1 394 ? -32.178 38.402 56.972  1.00 49.88 ? 394 ASP B OD1 1 
ATOM   7396 O OD2 . ASP B 1 394 ? -30.825 39.790 58.007  1.00 51.33 ? 394 ASP B OD2 1 
ATOM   7397 N N   . VAL B 1 395 ? -35.902 40.463 56.322  1.00 33.62 ? 395 VAL B N   1 
ATOM   7398 C CA  . VAL B 1 395 ? -36.342 41.436 55.331  1.00 27.58 ? 395 VAL B CA  1 
ATOM   7399 C C   . VAL B 1 395 ? -37.828 41.682 55.547  1.00 36.11 ? 395 VAL B C   1 
ATOM   7400 O O   . VAL B 1 395 ? -38.531 40.867 56.144  1.00 35.41 ? 395 VAL B O   1 
ATOM   7401 C CB  . VAL B 1 395 ? -36.077 40.955 53.885  1.00 34.71 ? 395 VAL B CB  1 
ATOM   7402 C CG1 . VAL B 1 395 ? -34.584 40.723 53.652  1.00 34.62 ? 395 VAL B CG1 1 
ATOM   7403 C CG2 . VAL B 1 395 ? -36.861 39.686 53.608  1.00 41.30 ? 395 VAL B CG2 1 
ATOM   7404 N N   . LYS B 1 396 ? -38.304 42.833 55.076  1.00 26.39 ? 396 LYS B N   1 
ATOM   7405 C CA  . LYS B 1 396 ? -39.716 43.154 55.197  1.00 29.69 ? 396 LYS B CA  1 
ATOM   7406 C C   . LYS B 1 396 ? -40.484 42.512 54.050  1.00 28.94 ? 396 LYS B C   1 
ATOM   7407 O O   . LYS B 1 396 ? -39.990 42.437 52.918  1.00 25.52 ? 396 LYS B O   1 
ATOM   7408 C CB  . LYS B 1 396 ? -39.939 44.667 55.207  1.00 37.13 ? 396 LYS B CB  1 
ATOM   7409 C CG  . LYS B 1 396 ? -41.359 45.070 55.614  1.00 41.30 ? 396 LYS B CG  1 
ATOM   7410 C CD  . LYS B 1 396 ? -41.644 46.559 55.453  1.00 38.56 ? 396 LYS B CD  1 
ATOM   7411 C CE  . LYS B 1 396 ? -40.973 47.387 56.546  1.00 40.17 ? 396 LYS B CE  1 
ATOM   7412 N NZ  . LYS B 1 396 ? -41.587 47.272 57.897  1.00 45.74 ? 396 LYS B NZ  1 
ATOM   7413 N N   . THR B 1 397 ? -41.682 42.024 54.353  1.00 27.19 ? 397 THR B N   1 
ATOM   7414 C CA  . THR B 1 397 ? -42.511 41.343 53.367  1.00 24.64 ? 397 THR B CA  1 
ATOM   7415 C C   . THR B 1 397 ? -43.904 41.956 53.346  1.00 29.19 ? 397 THR B C   1 
ATOM   7416 O O   . THR B 1 397 ? -44.313 42.696 54.249  1.00 28.01 ? 397 THR B O   1 
ATOM   7417 C CB  . THR B 1 397 ? -42.637 39.845 53.661  1.00 27.13 ? 397 THR B CB  1 
ATOM   7418 O OG1 . THR B 1 397 ? -43.217 39.690 54.957  1.00 27.84 ? 397 THR B OG1 1 
ATOM   7419 C CG2 . THR B 1 397 ? -41.293 39.143 53.620  1.00 31.40 ? 397 THR B CG2 1 
ATOM   7420 N N   . GLU B 1 398 ? -44.657 41.605 52.313  1.00 23.36 ? 398 GLU B N   1 
ATOM   7421 C CA  . GLU B 1 398 ? -46.012 42.108 52.168  1.00 29.94 ? 398 GLU B CA  1 
ATOM   7422 C C   . GLU B 1 398 ? -46.741 41.186 51.204  1.00 28.57 ? 398 GLU B C   1 
ATOM   7423 O O   . GLU B 1 398 ? -46.129 40.670 50.271  1.00 25.61 ? 398 GLU B O   1 
ATOM   7424 C CB  . GLU B 1 398 ? -46.013 43.556 51.657  1.00 30.70 ? 398 GLU B CB  1 
ATOM   7425 C CG  . GLU B 1 398 ? -47.396 44.149 51.364  1.00 37.53 ? 398 GLU B CG  1 
ATOM   7426 C CD  . GLU B 1 398 ? -47.336 45.635 51.044  1.00 45.93 ? 398 GLU B CD  1 
ATOM   7427 O OE1 . GLU B 1 398 ? -46.379 46.299 51.492  1.00 53.82 ? 398 GLU B OE1 1 
ATOM   7428 O OE2 . GLU B 1 398 ? -48.234 46.144 50.342  1.00 47.10 ? 398 GLU B OE2 1 
ATOM   7429 N N   . VAL B 1 399 ? -48.017 40.928 51.483  1.00 22.64 ? 399 VAL B N   1 
ATOM   7430 C CA  . VAL B 1 399 ? -48.857 40.157 50.575  1.00 21.54 ? 399 VAL B CA  1 
ATOM   7431 C C   . VAL B 1 399 ? -49.443 41.116 49.545  1.00 29.30 ? 399 VAL B C   1 
ATOM   7432 O O   . VAL B 1 399 ? -49.861 42.232 49.876  1.00 28.18 ? 399 VAL B O   1 
ATOM   7433 C CB  . VAL B 1 399 ? -49.961 39.410 51.354  1.00 24.16 ? 399 VAL B CB  1 
ATOM   7434 C CG1 . VAL B 1 399 ? -50.993 38.765 50.414  1.00 25.10 ? 399 VAL B CG1 1 
ATOM   7435 C CG2 . VAL B 1 399 ? -49.375 38.380 52.294  1.00 25.57 ? 399 VAL B CG2 1 
ATOM   7436 N N   . ILE B 1 400 ? -49.450 40.707 48.287  1.00 27.21 ? 400 ILE B N   1 
ATOM   7437 C CA  . ILE B 1 400 ? -50.109 41.480 47.243  1.00 26.40 ? 400 ILE B CA  1 
ATOM   7438 C C   . ILE B 1 400 ? -51.160 40.588 46.594  1.00 28.18 ? 400 ILE B C   1 
ATOM   7439 O O   . ILE B 1 400 ? -50.911 39.407 46.329  1.00 26.47 ? 400 ILE B O   1 
ATOM   7440 C CB  . ILE B 1 400 ? -49.085 42.025 46.223  1.00 22.92 ? 400 ILE B CB  1 
ATOM   7441 C CG1 . ILE B 1 400 ? -49.783 42.776 45.088  1.00 24.12 ? 400 ILE B CG1 1 
ATOM   7442 C CG2 . ILE B 1 400 ? -48.235 40.915 45.680  1.00 25.09 ? 400 ILE B CG2 1 
ATOM   7443 C CD1 . ILE B 1 400 ? -48.821 43.538 44.194  1.00 27.35 ? 400 ILE B CD1 1 
ATOM   7444 N N   . GLU B 1 401 ? -52.349 41.142 46.374  1.00 22.18 ? 401 GLU B N   1 
ATOM   7445 C CA  . GLU B 1 401 ? -53.470 40.334 45.910  1.00 27.46 ? 401 GLU B CA  1 
ATOM   7446 C C   . GLU B 1 401 ? -53.730 40.427 44.413  1.00 24.13 ? 401 GLU B C   1 
ATOM   7447 O O   . GLU B 1 401 ? -54.335 39.507 43.844  1.00 23.87 ? 401 GLU B O   1 
ATOM   7448 C CB  . GLU B 1 401 ? -54.740 40.732 46.667  1.00 27.74 ? 401 GLU B CB  1 
ATOM   7449 C CG  . GLU B 1 401 ? -54.731 40.272 48.115  1.00 40.15 ? 401 GLU B CG  1 
ATOM   7450 C CD  . GLU B 1 401 ? -54.697 38.750 48.252  1.00 52.68 ? 401 GLU B CD  1 
ATOM   7451 O OE1 . GLU B 1 401 ? -55.075 38.045 47.288  1.00 44.18 ? 401 GLU B OE1 1 
ATOM   7452 O OE2 . GLU B 1 401 ? -54.303 38.262 49.337  1.00 63.50 ? 401 GLU B OE2 1 
ATOM   7453 N N   . SER B 1 402 ? -53.277 41.489 43.759  1.00 22.80 ? 402 SER B N   1 
ATOM   7454 C CA  . SER B 1 402 ? -53.580 41.665 42.349  1.00 24.22 ? 402 SER B CA  1 
ATOM   7455 C C   . SER B 1 402 ? -52.532 42.587 41.742  1.00 24.06 ? 402 SER B C   1 
ATOM   7456 O O   . SER B 1 402 ? -51.990 43.463 42.426  1.00 22.97 ? 402 SER B O   1 
ATOM   7457 C CB  . SER B 1 402 ? -54.988 42.237 42.163  1.00 21.33 ? 402 SER B CB  1 
ATOM   7458 O OG  . SER B 1 402 ? -55.284 42.367 40.783  1.00 26.92 ? 402 SER B OG  1 
ATOM   7459 N N   . VAL B 1 403 ? -52.251 42.383 40.454  1.00 20.74 ? 403 VAL B N   1 
ATOM   7460 C CA  . VAL B 1 403 ? -51.411 43.303 39.693  1.00 17.75 ? 403 VAL B CA  1 
ATOM   7461 C C   . VAL B 1 403 ? -52.185 43.714 38.451  1.00 20.33 ? 403 VAL B C   1 
ATOM   7462 O O   . VAL B 1 403 ? -53.005 42.946 37.936  1.00 21.28 ? 403 VAL B O   1 
ATOM   7463 C CB  . VAL B 1 403 ? -50.035 42.699 39.299  1.00 16.69 ? 403 VAL B CB  1 
ATOM   7464 C CG1 . VAL B 1 403 ? -49.249 42.283 40.563  1.00 17.85 ? 403 VAL B CG1 1 
ATOM   7465 C CG2 . VAL B 1 403 ? -50.180 41.524 38.376  1.00 17.79 ? 403 VAL B CG2 1 
ATOM   7466 N N   . LYS B 1 404 ? -51.917 44.926 37.962  1.00 24.10 ? 404 LYS B N   1 
ATOM   7467 C CA  . LYS B 1 404 ? -52.430 45.362 36.665  1.00 20.61 ? 404 LYS B CA  1 
ATOM   7468 C C   . LYS B 1 404 ? -51.417 44.930 35.608  1.00 18.01 ? 404 LYS B C   1 
ATOM   7469 O O   . LYS B 1 404 ? -50.232 45.270 35.703  1.00 22.20 ? 404 LYS B O   1 
ATOM   7470 C CB  . LYS B 1 404 ? -52.639 46.875 36.617  1.00 28.18 ? 404 LYS B CB  1 
ATOM   7471 C CG  . LYS B 1 404 ? -53.816 47.397 37.448  1.00 41.05 ? 404 LYS B CG  1 
ATOM   7472 C CD  . LYS B 1 404 ? -54.490 48.582 36.738  1.00 44.46 ? 404 LYS B CD  1 
ATOM   7473 C CE  . LYS B 1 404 ? -55.760 49.041 37.451  1.00 47.88 ? 404 LYS B CE  1 
ATOM   7474 N NZ  . LYS B 1 404 ? -55.474 50.004 38.547  1.00 54.11 ? 404 LYS B NZ  1 
ATOM   7475 N N   . ALA B 1 405 ? -51.879 44.178 34.610  1.00 19.16 ? 405 ALA B N   1 
ATOM   7476 C CA  . ALA B 1 405 ? -50.966 43.569 33.647  1.00 18.82 ? 405 ALA B CA  1 
ATOM   7477 C C   . ALA B 1 405 ? -50.163 44.630 32.904  1.00 20.50 ? 405 ALA B C   1 
ATOM   7478 O O   . ALA B 1 405 ? -50.669 45.708 32.588  1.00 21.89 ? 405 ALA B O   1 
ATOM   7479 C CB  . ALA B 1 405 ? -51.745 42.720 32.642  1.00 16.87 ? 405 ALA B CB  1 
ATOM   7480 N N   . GLY B 1 406 ? -48.902 44.324 32.633  1.00 18.77 ? 406 GLY B N   1 
ATOM   7481 C CA  . GLY B 1 406 ? -48.077 45.247 31.875  1.00 17.57 ? 406 GLY B CA  1 
ATOM   7482 C C   . GLY B 1 406 ? -46.684 44.714 31.647  1.00 15.66 ? 406 GLY B C   1 
ATOM   7483 O O   . GLY B 1 406 ? -46.426 43.524 31.819  1.00 19.78 ? 406 GLY B O   1 
ATOM   7484 N N   . THR B 1 407 ? -45.787 45.623 31.259  1.00 16.74 ? 407 THR B N   1 
ATOM   7485 C CA  . THR B 1 407 ? -44.385 45.334 31.006  1.00 17.65 ? 407 THR B CA  1 
ATOM   7486 C C   . THR B 1 407 ? -43.547 46.471 31.568  1.00 19.61 ? 407 THR B C   1 
ATOM   7487 O O   . THR B 1 407 ? -44.073 47.507 31.982  1.00 18.35 ? 407 THR B O   1 
ATOM   7488 C CB  . THR B 1 407 ? -44.082 45.210 29.498  1.00 19.49 ? 407 THR B CB  1 
ATOM   7489 O OG1 . THR B 1 407 ? -43.965 46.525 28.930  1.00 19.36 ? 407 THR B OG1 1 
ATOM   7490 C CG2 . THR B 1 407 ? -45.166 44.425 28.766  1.00 18.59 ? 407 THR B CG2 1 
ATOM   7491 N N   . TRP B 1 408 ? -42.227 46.313 31.518  1.00 15.81 ? 408 TRP B N   1 
ATOM   7492 C CA  . TRP B 1 408 ? -41.362 47.407 31.952  1.00 16.15 ? 408 TRP B CA  1 
ATOM   7493 C C   . TRP B 1 408 ? -41.262 48.532 30.920  1.00 19.06 ? 408 TRP B C   1 
ATOM   7494 O O   . TRP B 1 408 ? -40.473 49.469 31.114  1.00 21.70 ? 408 TRP B O   1 
ATOM   7495 C CB  . TRP B 1 408 ? -39.975 46.881 32.344  1.00 16.23 ? 408 TRP B CB  1 
ATOM   7496 C CG  . TRP B 1 408 ? -39.144 46.213 31.246  1.00 18.76 ? 408 TRP B CG  1 
ATOM   7497 C CD1 . TRP B 1 408 ? -39.436 46.133 29.908  1.00 20.66 ? 408 TRP B CD1 1 
ATOM   7498 C CD2 . TRP B 1 408 ? -37.881 45.552 31.422  1.00 21.15 ? 408 TRP B CD2 1 
ATOM   7499 N NE1 . TRP B 1 408 ? -38.439 45.459 29.246  1.00 18.90 ? 408 TRP B NE1 1 
ATOM   7500 C CE2 . TRP B 1 408 ? -37.466 45.099 30.153  1.00 19.42 ? 408 TRP B CE2 1 
ATOM   7501 C CE3 . TRP B 1 408 ? -37.068 45.291 32.535  1.00 17.34 ? 408 TRP B CE3 1 
ATOM   7502 C CZ2 . TRP B 1 408 ? -36.279 44.402 29.971  1.00 17.56 ? 408 TRP B CZ2 1 
ATOM   7503 C CZ3 . TRP B 1 408 ? -35.892 44.604 32.355  1.00 15.94 ? 408 TRP B CZ3 1 
ATOM   7504 C CH2 . TRP B 1 408 ? -35.500 44.173 31.080  1.00 22.36 ? 408 TRP B CH2 1 
ATOM   7505 N N   . PHE B 1 409 ? -42.062 48.486 29.847  1.00 18.78 ? 409 PHE B N   1 
ATOM   7506 C CA  . PHE B 1 409 ? -42.125 49.569 28.868  1.00 20.01 ? 409 PHE B CA  1 
ATOM   7507 C C   . PHE B 1 409 ? -43.409 50.329 29.156  1.00 24.83 ? 409 PHE B C   1 
ATOM   7508 O O   . PHE B 1 409 ? -44.489 49.925 28.719  1.00 24.54 ? 409 PHE B O   1 
ATOM   7509 C CB  . PHE B 1 409 ? -42.089 49.039 27.437  1.00 21.97 ? 409 PHE B CB  1 
ATOM   7510 C CG  . PHE B 1 409 ? -42.119 50.127 26.392  1.00 38.15 ? 409 PHE B CG  1 
ATOM   7511 C CD1 . PHE B 1 409 ? -43.323 50.695 25.991  1.00 53.89 ? 409 PHE B CD1 1 
ATOM   7512 C CD2 . PHE B 1 409 ? -40.951 50.566 25.798  1.00 38.70 ? 409 PHE B CD2 1 
ATOM   7513 C CE1 . PHE B 1 409 ? -43.354 51.694 25.029  1.00 53.81 ? 409 PHE B CE1 1 
ATOM   7514 C CE2 . PHE B 1 409 ? -40.972 51.571 24.831  1.00 37.07 ? 409 PHE B CE2 1 
ATOM   7515 C CZ  . PHE B 1 409 ? -42.171 52.131 24.451  1.00 45.74 ? 409 PHE B CZ  1 
ATOM   7516 N N   . ASP B 1 410 ? -43.293 51.401 29.933  1.00 33.07 ? 410 ASP B N   1 
ATOM   7517 C CA  . ASP B 1 410 ? -44.409 52.257 30.324  1.00 38.86 ? 410 ASP B CA  1 
ATOM   7518 C C   . ASP B 1 410 ? -45.496 51.512 31.085  1.00 33.82 ? 410 ASP B C   1 
ATOM   7519 O O   . ASP B 1 410 ? -46.614 52.022 31.202  1.00 34.41 ? 410 ASP B O   1 
ATOM   7520 C CB  . ASP B 1 410 ? -45.034 52.953 29.106  1.00 37.26 ? 410 ASP B CB  1 
ATOM   7521 C CG  . ASP B 1 410 ? -44.104 53.956 28.468  1.00 45.15 ? 410 ASP B CG  1 
ATOM   7522 O OD1 . ASP B 1 410 ? -43.404 54.670 29.218  1.00 54.96 ? 410 ASP B OD1 1 
ATOM   7523 O OD2 . ASP B 1 410 ? -44.082 54.034 27.217  1.00 43.01 ? 410 ASP B OD2 1 
ATOM   7524 N N   . GLY B 1 411 ? -45.211 50.314 31.589  1.00 27.24 ? 411 GLY B N   1 
ATOM   7525 C CA  . GLY B 1 411 ? -46.241 49.528 32.230  1.00 28.33 ? 411 GLY B CA  1 
ATOM   7526 C C   . GLY B 1 411 ? -47.324 49.000 31.314  1.00 24.93 ? 411 GLY B C   1 
ATOM   7527 O O   . GLY B 1 411 ? -48.396 48.631 31.797  1.00 24.85 ? 411 GLY B O   1 
ATOM   7528 N N   . ASN B 1 412 ? -47.098 48.958 30.002  1.00 24.43 ? 412 ASN B N   1 
ATOM   7529 C CA  . ASN B 1 412 ? -48.157 48.538 29.099  1.00 22.95 ? 412 ASN B CA  1 
ATOM   7530 C C   . ASN B 1 412 ? -47.563 47.711 27.960  1.00 20.96 ? 412 ASN B C   1 
ATOM   7531 O O   . ASN B 1 412 ? -46.357 47.415 27.930  1.00 24.87 ? 412 ASN B O   1 
ATOM   7532 C CB  . ASN B 1 412 ? -48.991 49.739 28.618  1.00 24.54 ? 412 ASN B CB  1 
ATOM   7533 C CG  . ASN B 1 412 ? -48.210 50.739 27.772  1.00 33.08 ? 412 ASN B CG  1 
ATOM   7534 O OD1 . ASN B 1 412 ? -47.488 50.369 26.847  1.00 30.51 ? 412 ASN B OD1 1 
ATOM   7535 N ND2 . ASN B 1 412 ? -48.408 52.020 28.049  1.00 34.46 ? 412 ASN B ND2 1 
ATOM   7536 N N   . PHE B 1 413 ? -48.426 47.327 27.019  1.00 20.88 ? 413 PHE B N   1 
ATOM   7537 C CA  . PHE B 1 413 ? -48.048 46.416 25.944  1.00 21.37 ? 413 PHE B CA  1 
ATOM   7538 C C   . PHE B 1 413 ? -47.930 47.097 24.578  1.00 23.71 ? 413 PHE B C   1 
ATOM   7539 O O   . PHE B 1 413 ? -47.846 46.400 23.559  1.00 22.10 ? 413 PHE B O   1 
ATOM   7540 C CB  . PHE B 1 413 ? -49.052 45.268 25.869  1.00 18.03 ? 413 PHE B CB  1 
ATOM   7541 C CG  . PHE B 1 413 ? -49.046 44.368 27.074  1.00 17.41 ? 413 PHE B CG  1 
ATOM   7542 C CD1 . PHE B 1 413 ? -48.126 43.344 27.186  1.00 19.83 ? 413 PHE B CD1 1 
ATOM   7543 C CD2 . PHE B 1 413 ? -49.982 44.543 28.090  1.00 23.79 ? 413 PHE B CD2 1 
ATOM   7544 C CE1 . PHE B 1 413 ? -48.118 42.504 28.304  1.00 18.97 ? 413 PHE B CE1 1 
ATOM   7545 C CE2 . PHE B 1 413 ? -49.990 43.700 29.213  1.00 23.57 ? 413 PHE B CE2 1 
ATOM   7546 C CZ  . PHE B 1 413 ? -49.055 42.682 29.315  1.00 19.42 ? 413 PHE B CZ  1 
ATOM   7547 N N   . LEU B 1 414 ? -47.878 48.430 24.531  1.00 20.74 ? 414 LEU B N   1 
ATOM   7548 C CA  . LEU B 1 414 ? -47.961 49.143 23.252  1.00 22.98 ? 414 LEU B CA  1 
ATOM   7549 C C   . LEU B 1 414 ? -46.739 48.938 22.366  1.00 24.66 ? 414 LEU B C   1 
ATOM   7550 O O   . LEU B 1 414 ? -46.807 49.218 21.161  1.00 27.56 ? 414 LEU B O   1 
ATOM   7551 C CB  . LEU B 1 414 ? -48.161 50.641 23.486  1.00 28.59 ? 414 LEU B CB  1 
ATOM   7552 C CG  . LEU B 1 414 ? -49.527 51.015 24.077  1.00 36.64 ? 414 LEU B CG  1 
ATOM   7553 C CD1 . LEU B 1 414 ? -49.823 52.496 23.958  1.00 38.96 ? 414 LEU B CD1 1 
ATOM   7554 C CD2 . LEU B 1 414 ? -50.611 50.218 23.402  1.00 34.75 ? 414 LEU B CD2 1 
ATOM   7555 N N   . LYS B 1 415 ? -45.617 48.485 22.918  1.00 23.95 ? 415 LYS B N   1 
ATOM   7556 C CA  . LYS B 1 415 ? -44.465 48.225 22.065  1.00 22.42 ? 415 LYS B CA  1 
ATOM   7557 C C   . LYS B 1 415 ? -44.618 46.959 21.225  1.00 22.72 ? 415 LYS B C   1 
ATOM   7558 O O   . LYS B 1 415 ? -43.845 46.765 20.273  1.00 22.30 ? 415 LYS B O   1 
ATOM   7559 C CB  . LYS B 1 415 ? -43.203 48.157 22.924  1.00 26.93 ? 415 LYS B CB  1 
ATOM   7560 C CG  . LYS B 1 415 ? -41.904 48.092 22.144  1.00 35.23 ? 415 LYS B CG  1 
ATOM   7561 C CD  . LYS B 1 415 ? -41.820 49.075 20.984  1.00 40.99 ? 415 LYS B CD  1 
ATOM   7562 C CE  . LYS B 1 415 ? -41.572 50.504 21.448  1.00 47.38 ? 415 LYS B CE  1 
ATOM   7563 N NZ  . LYS B 1 415 ? -41.118 51.371 20.315  1.00 52.22 ? 415 LYS B NZ  1 
ATOM   7564 N N   . TRP B 1 416 ? -45.608 46.111 21.521  1.00 19.29 ? 416 TRP B N   1 
ATOM   7565 C CA  . TRP B 1 416 ? -45.783 44.850 20.813  1.00 19.31 ? 416 TRP B CA  1 
ATOM   7566 C C   . TRP B 1 416 ? -47.166 44.663 20.203  1.00 21.75 ? 416 TRP B C   1 
ATOM   7567 O O   . TRP B 1 416 ? -47.352 43.718 19.425  1.00 21.31 ? 416 TRP B O   1 
ATOM   7568 C CB  . TRP B 1 416 ? -45.490 43.666 21.756  1.00 17.13 ? 416 TRP B CB  1 
ATOM   7569 C CG  . TRP B 1 416 ? -44.167 43.762 22.402  1.00 18.86 ? 416 TRP B CG  1 
ATOM   7570 C CD1 . TRP B 1 416 ? -42.998 43.206 21.966  1.00 19.97 ? 416 TRP B CD1 1 
ATOM   7571 C CD2 . TRP B 1 416 ? -43.855 44.461 23.611  1.00 19.35 ? 416 TRP B CD2 1 
ATOM   7572 N NE1 . TRP B 1 416 ? -41.968 43.526 22.826  1.00 17.33 ? 416 TRP B NE1 1 
ATOM   7573 C CE2 . TRP B 1 416 ? -42.467 44.298 23.843  1.00 19.33 ? 416 TRP B CE2 1 
ATOM   7574 C CE3 . TRP B 1 416 ? -44.609 45.221 24.511  1.00 20.05 ? 416 TRP B CE3 1 
ATOM   7575 C CZ2 . TRP B 1 416 ? -41.818 44.859 24.940  1.00 19.25 ? 416 TRP B CZ2 1 
ATOM   7576 C CZ3 . TRP B 1 416 ? -43.959 45.779 25.606  1.00 19.62 ? 416 TRP B CZ3 1 
ATOM   7577 C CH2 . TRP B 1 416 ? -42.591 45.597 25.813  1.00 17.98 ? 416 TRP B CH2 1 
ATOM   7578 N N   . ILE B 1 417 ? -48.129 45.530 20.513  1.00 18.35 ? 417 ILE B N   1 
ATOM   7579 C CA  . ILE B 1 417 ? -49.488 45.376 20.006  1.00 22.66 ? 417 ILE B CA  1 
ATOM   7580 C C   . ILE B 1 417 ? -50.171 46.735 20.069  1.00 20.92 ? 417 ILE B C   1 
ATOM   7581 O O   . ILE B 1 417 ? -49.771 47.605 20.841  1.00 28.12 ? 417 ILE B O   1 
ATOM   7582 C CB  . ILE B 1 417 ? -50.244 44.294 20.818  1.00 24.56 ? 417 ILE B CB  1 
ATOM   7583 C CG1 . ILE B 1 417 ? -51.500 43.822 20.075  1.00 22.36 ? 417 ILE B CG1 1 
ATOM   7584 C CG2 . ILE B 1 417 ? -50.555 44.801 22.235  1.00 31.15 ? 417 ILE B CG2 1 
ATOM   7585 C CD1 . ILE B 1 417 ? -51.983 42.466 20.531  1.00 25.64 ? 417 ILE B CD1 1 
ATOM   7586 N N   . GLY B 1 418 ? -51.196 46.927 19.232  1.00 26.11 ? 418 GLY B N   1 
ATOM   7587 C CA  . GLY B 1 418 ? -52.043 48.103 19.336  1.00 33.31 ? 418 GLY B CA  1 
ATOM   7588 C C   . GLY B 1 418 ? -51.951 49.106 18.203  1.00 37.60 ? 418 GLY B C   1 
ATOM   7589 O O   . GLY B 1 418 ? -52.809 50.000 18.131  1.00 55.18 ? 418 GLY B O   1 
ATOM   7590 N N   . ASN B 1 419 ? -50.959 49.024 17.327  1.00 34.57 ? 419 ASN B N   1 
ATOM   7591 C CA  . ASN B 1 419 ? -50.990 49.830 16.114  1.00 40.35 ? 419 ASN B CA  1 
ATOM   7592 C C   . ASN B 1 419 ? -51.242 48.925 14.911  1.00 38.08 ? 419 ASN B C   1 
ATOM   7593 O O   . ASN B 1 419 ? -51.271 47.696 15.022  1.00 34.70 ? 419 ASN B O   1 
ATOM   7594 C CB  . ASN B 1 419 ? -49.709 50.682 15.969  1.00 46.62 ? 419 ASN B CB  1 
ATOM   7595 C CG  . ASN B 1 419 ? -48.478 49.897 15.486  1.00 47.34 ? 419 ASN B CG  1 
ATOM   7596 O OD1 . ASN B 1 419 ? -48.534 48.712 15.166  1.00 53.84 ? 419 ASN B OD1 1 
ATOM   7597 N ND2 . ASN B 1 419 ? -47.349 50.591 15.425  1.00 44.98 ? 419 ASN B ND2 1 
ATOM   7598 N N   . LYS B 1 420 ? -51.438 49.544 13.749  1.00 39.02 ? 420 LYS B N   1 
ATOM   7599 C CA  . LYS B 1 420 ? -51.848 48.769 12.585  1.00 36.06 ? 420 LYS B CA  1 
ATOM   7600 C C   . LYS B 1 420 ? -50.792 47.737 12.198  1.00 37.34 ? 420 LYS B C   1 
ATOM   7601 O O   . LYS B 1 420 ? -51.122 46.586 11.886  1.00 30.58 ? 420 LYS B O   1 
ATOM   7602 C CB  . LYS B 1 420 ? -52.155 49.698 11.406  1.00 40.67 ? 420 LYS B CB  1 
ATOM   7603 C CG  . LYS B 1 420 ? -52.730 48.965 10.208  1.00 46.31 ? 420 LYS B CG  1 
ATOM   7604 C CD  . LYS B 1 420 ? -52.993 49.897 9.039   1.00 61.29 ? 420 LYS B CD  1 
ATOM   7605 C CE  . LYS B 1 420 ? -53.662 49.152 7.891   1.00 67.50 ? 420 LYS B CE  1 
ATOM   7606 N NZ  . LYS B 1 420 ? -54.759 48.274 8.392   1.00 70.23 ? 420 LYS B NZ  1 
ATOM   7607 N N   . GLU B 1 421 ? -49.513 48.118 12.214  1.00 34.60 ? 421 GLU B N   1 
ATOM   7608 C CA  . GLU B 1 421 ? -48.497 47.188 11.730  1.00 34.01 ? 421 GLU B CA  1 
ATOM   7609 C C   . GLU B 1 421 ? -48.238 46.078 12.745  1.00 30.47 ? 421 GLU B C   1 
ATOM   7610 O O   . GLU B 1 421 ? -48.149 44.900 12.375  1.00 30.01 ? 421 GLU B O   1 
ATOM   7611 C CB  . GLU B 1 421 ? -47.205 47.932 11.396  1.00 41.21 ? 421 GLU B CB  1 
ATOM   7612 C CG  . GLU B 1 421 ? -47.249 48.710 10.087  1.00 45.79 ? 421 GLU B CG  1 
ATOM   7613 C CD  . GLU B 1 421 ? -47.797 50.118 10.275  1.00 55.17 ? 421 GLU B CD  1 
ATOM   7614 O OE1 . GLU B 1 421 ? -48.076 50.504 11.436  1.00 47.43 ? 421 GLU B OE1 1 
ATOM   7615 O OE2 . GLU B 1 421 ? -47.946 50.842 9.264   1.00 62.54 ? 421 GLU B OE2 1 
ATOM   7616 N N   . LYS B 1 422 ? -48.127 46.424 14.029  1.00 30.15 ? 422 LYS B N   1 
ATOM   7617 C CA  . LYS B 1 422 ? -47.933 45.387 15.039  1.00 30.93 ? 422 LYS B CA  1 
ATOM   7618 C C   . LYS B 1 422 ? -49.117 44.424 15.076  1.00 31.17 ? 422 LYS B C   1 
ATOM   7619 O O   . LYS B 1 422 ? -48.933 43.207 15.216  1.00 30.06 ? 422 LYS B O   1 
ATOM   7620 C CB  . LYS B 1 422 ? -47.694 46.026 16.410  1.00 29.94 ? 422 LYS B CB  1 
ATOM   7621 C CG  . LYS B 1 422 ? -46.351 46.760 16.471  1.00 37.25 ? 422 LYS B CG  1 
ATOM   7622 C CD  . LYS B 1 422 ? -46.088 47.478 17.789  1.00 34.26 ? 422 LYS B CD  1 
ATOM   7623 C CE  . LYS B 1 422 ? -44.829 48.343 17.690  1.00 26.45 ? 422 LYS B CE  1 
ATOM   7624 N NZ  . LYS B 1 422 ? -43.553 47.545 17.615  1.00 23.49 ? 422 LYS B NZ  1 
ATOM   7625 N N   . ASN B 1 423 ? -50.341 44.947 14.914  1.00 25.77 ? 423 ASN B N   1 
ATOM   7626 C CA  . ASN B 1 423 ? -51.516 44.081 14.898  1.00 25.93 ? 423 ASN B CA  1 
ATOM   7627 C C   . ASN B 1 423 ? -51.499 43.135 13.706  1.00 33.42 ? 423 ASN B C   1 
ATOM   7628 O O   . ASN B 1 423 ? -52.062 42.037 13.784  1.00 33.19 ? 423 ASN B O   1 
ATOM   7629 C CB  . ASN B 1 423 ? -52.804 44.914 14.895  1.00 29.96 ? 423 ASN B CB  1 
ATOM   7630 C CG  . ASN B 1 423 ? -53.102 45.533 16.258  1.00 34.93 ? 423 ASN B CG  1 
ATOM   7631 O OD1 . ASN B 1 423 ? -52.407 45.271 17.231  1.00 30.39 ? 423 ASN B OD1 1 
ATOM   7632 N ND2 . ASN B 1 423 ? -54.138 46.356 16.325  1.00 30.49 ? 423 ASN B ND2 1 
ATOM   7633 N N   . GLU B 1 424 ? -50.881 43.540 12.589  1.00 30.34 ? 424 GLU B N   1 
ATOM   7634 C CA  . GLU B 1 424 ? -50.835 42.646 11.440  1.00 31.50 ? 424 GLU B CA  1 
ATOM   7635 C C   . GLU B 1 424 ? -50.020 41.401 11.752  1.00 25.44 ? 424 GLU B C   1 
ATOM   7636 O O   . GLU B 1 424 ? -50.369 40.304 11.300  1.00 28.40 ? 424 GLU B O   1 
ATOM   7637 C CB  . GLU B 1 424 ? -50.293 43.369 10.201  1.00 37.85 ? 424 GLU B CB  1 
ATOM   7638 C CG  . GLU B 1 424 ? -50.101 42.465 8.968   1.00 48.38 ? 424 GLU B CG  1 
ATOM   7639 C CD  . GLU B 1 424 ? -51.411 41.977 8.337   1.00 62.16 ? 424 GLU B CD  1 
ATOM   7640 O OE1 . GLU B 1 424 ? -52.497 42.474 8.720   1.00 60.95 ? 424 GLU B OE1 1 
ATOM   7641 O OE2 . GLU B 1 424 ? -51.353 41.102 7.440   1.00 64.64 ? 424 GLU B OE2 1 
ATOM   7642 N N   . TYR B 1 425 ? -48.926 41.547 12.522  1.00 24.08 ? 425 TYR B N   1 
ATOM   7643 C CA  . TYR B 1 425 ? -48.174 40.372 12.954  1.00 27.67 ? 425 TYR B CA  1 
ATOM   7644 C C   . TYR B 1 425 ? -49.035 39.449 13.804  1.00 26.36 ? 425 TYR B C   1 
ATOM   7645 O O   . TYR B 1 425 ? -49.014 38.226 13.615  1.00 24.38 ? 425 TYR B O   1 
ATOM   7646 C CB  . TYR B 1 425 ? -46.911 40.778 13.731  1.00 23.50 ? 425 TYR B CB  1 
ATOM   7647 C CG  . TYR B 1 425 ? -45.645 40.857 12.891  1.00 23.52 ? 425 TYR B CG  1 
ATOM   7648 C CD1 . TYR B 1 425 ? -45.693 41.198 11.553  1.00 27.18 ? 425 TYR B CD1 1 
ATOM   7649 C CD2 . TYR B 1 425 ? -44.400 40.604 13.463  1.00 22.51 ? 425 TYR B CD2 1 
ATOM   7650 C CE1 . TYR B 1 425 ? -44.536 41.280 10.793  1.00 33.86 ? 425 TYR B CE1 1 
ATOM   7651 C CE2 . TYR B 1 425 ? -43.235 40.681 12.711  1.00 24.05 ? 425 TYR B CE2 1 
ATOM   7652 C CZ  . TYR B 1 425 ? -43.315 41.015 11.384  1.00 27.73 ? 425 TYR B CZ  1 
ATOM   7653 O OH  . TYR B 1 425 ? -42.173 41.090 10.650  1.00 28.93 ? 425 TYR B OH  1 
ATOM   7654 N N   . TRP B 1 426 ? -49.805 40.014 14.744  1.00 23.96 ? 426 TRP B N   1 
ATOM   7655 C CA  . TRP B 1 426 ? -50.682 39.177 15.558  1.00 26.30 ? 426 TRP B CA  1 
ATOM   7656 C C   . TRP B 1 426 ? -51.728 38.470 14.697  1.00 26.58 ? 426 TRP B C   1 
ATOM   7657 O O   . TRP B 1 426 ? -51.987 37.272 14.881  1.00 26.55 ? 426 TRP B O   1 
ATOM   7658 C CB  . TRP B 1 426 ? -51.338 40.012 16.667  1.00 21.71 ? 426 TRP B CB  1 
ATOM   7659 C CG  . TRP B 1 426 ? -50.334 40.374 17.777  1.00 19.15 ? 426 TRP B CG  1 
ATOM   7660 C CD1 . TRP B 1 426 ? -49.697 41.560 17.946  1.00 22.89 ? 426 TRP B CD1 1 
ATOM   7661 C CD2 . TRP B 1 426 ? -49.864 39.511 18.818  1.00 17.90 ? 426 TRP B CD2 1 
ATOM   7662 N NE1 . TRP B 1 426 ? -48.858 41.503 19.033  1.00 21.60 ? 426 TRP B NE1 1 
ATOM   7663 C CE2 . TRP B 1 426 ? -48.945 40.251 19.587  1.00 23.28 ? 426 TRP B CE2 1 
ATOM   7664 C CE3 . TRP B 1 426 ? -50.158 38.190 19.189  1.00 19.49 ? 426 TRP B CE3 1 
ATOM   7665 C CZ2 . TRP B 1 426 ? -48.293 39.714 20.703  1.00 27.64 ? 426 TRP B CZ2 1 
ATOM   7666 C CZ3 . TRP B 1 426 ? -49.501 37.651 20.298  1.00 25.53 ? 426 TRP B CZ3 1 
ATOM   7667 C CH2 . TRP B 1 426 ? -48.577 38.415 21.036  1.00 26.70 ? 426 TRP B CH2 1 
ATOM   7668 N N   . LYS B 1 427 ? -52.326 39.191 13.740  1.00 24.72 ? 427 LYS B N   1 
ATOM   7669 C CA  . LYS B 1 427 ? -53.284 38.581 12.822  1.00 25.60 ? 427 LYS B CA  1 
ATOM   7670 C C   . LYS B 1 427 ? -52.661 37.420 12.059  1.00 27.29 ? 427 LYS B C   1 
ATOM   7671 O O   . LYS B 1 427 ? -53.303 36.383 11.870  1.00 29.35 ? 427 LYS B O   1 
ATOM   7672 C CB  . LYS B 1 427 ? -53.815 39.618 11.826  1.00 28.12 ? 427 LYS B CB  1 
ATOM   7673 C CG  . LYS B 1 427 ? -54.686 40.693 12.446  1.00 43.19 ? 427 LYS B CG  1 
ATOM   7674 C CD  . LYS B 1 427 ? -55.217 41.640 11.384  1.00 52.11 ? 427 LYS B CD  1 
ATOM   7675 C CE  . LYS B 1 427 ? -54.513 42.985 11.462  1.00 59.39 ? 427 LYS B CE  1 
ATOM   7676 N NZ  . LYS B 1 427 ? -55.436 44.111 11.818  1.00 66.11 ? 427 LYS B NZ  1 
ATOM   7677 N N   . ILE B 1 428 ? -51.417 37.596 11.592  1.00 27.54 ? 428 ILE B N   1 
ATOM   7678 C CA  . ILE B 1 428 ? -50.694 36.536 10.894  1.00 28.47 ? 428 ILE B CA  1 
ATOM   7679 C C   . ILE B 1 428 ? -50.493 35.342 11.811  1.00 26.58 ? 428 ILE B C   1 
ATOM   7680 O O   . ILE B 1 428 ? -50.688 34.184 11.409  1.00 30.23 ? 428 ILE B O   1 
ATOM   7681 C CB  . ILE B 1 428 ? -49.352 37.083 10.368  1.00 31.88 ? 428 ILE B CB  1 
ATOM   7682 C CG1 . ILE B 1 428 ? -49.567 37.987 9.150   1.00 36.15 ? 428 ILE B CG1 1 
ATOM   7683 C CG2 . ILE B 1 428 ? -48.376 35.957 10.029  1.00 27.71 ? 428 ILE B CG2 1 
ATOM   7684 C CD1 . ILE B 1 428 ? -48.352 38.847 8.847   1.00 35.45 ? 428 ILE B CD1 1 
ATOM   7685 N N   . LEU B 1 429 ? -50.104 35.610 13.061  1.00 25.06 ? 429 LEU B N   1 
ATOM   7686 C CA  . LEU B 1 429 ? -49.889 34.549 14.034  1.00 25.30 ? 429 LEU B CA  1 
ATOM   7687 C C   . LEU B 1 429 ? -51.180 33.805 14.347  1.00 30.77 ? 429 LEU B C   1 
ATOM   7688 O O   . LEU B 1 429 ? -51.183 32.571 14.452  1.00 27.93 ? 429 LEU B O   1 
ATOM   7689 C CB  . LEU B 1 429 ? -49.309 35.147 15.315  1.00 26.30 ? 429 LEU B CB  1 
ATOM   7690 C CG  . LEU B 1 429 ? -49.059 34.149 16.442  1.00 26.78 ? 429 LEU B CG  1 
ATOM   7691 C CD1 . LEU B 1 429 ? -47.943 33.190 16.070  1.00 28.36 ? 429 LEU B CD1 1 
ATOM   7692 C CD2 . LEU B 1 429 ? -48.728 34.909 17.699  1.00 22.19 ? 429 LEU B CD2 1 
ATOM   7693 N N   . ILE B 1 430 ? -52.277 34.548 14.533  1.00 23.34 ? 430 ILE B N   1 
ATOM   7694 C CA  . ILE B 1 430 ? -53.571 33.943 14.842  1.00 25.79 ? 430 ILE B CA  1 
ATOM   7695 C C   . ILE B 1 430 ? -54.013 33.015 13.720  1.00 30.18 ? 430 ILE B C   1 
ATOM   7696 O O   . ILE B 1 430 ? -54.495 31.900 13.966  1.00 32.06 ? 430 ILE B O   1 
ATOM   7697 C CB  . ILE B 1 430 ? -54.621 35.041 15.093  1.00 26.10 ? 430 ILE B CB  1 
ATOM   7698 C CG1 . ILE B 1 430 ? -54.360 35.764 16.405  1.00 27.54 ? 430 ILE B CG1 1 
ATOM   7699 C CG2 . ILE B 1 430 ? -56.017 34.470 15.047  1.00 32.92 ? 430 ILE B CG2 1 
ATOM   7700 C CD1 . ILE B 1 430 ? -54.872 37.175 16.420  1.00 29.23 ? 430 ILE B CD1 1 
ATOM   7701 N N   . GLU B 1 431 ? -53.875 33.469 12.469  1.00 29.50 ? 431 GLU B N   1 
ATOM   7702 C CA  . GLU B 1 431 ? -54.275 32.646 11.330  1.00 40.09 ? 431 GLU B CA  1 
ATOM   7703 C C   . GLU B 1 431 ? -53.378 31.426 11.190  1.00 32.79 ? 431 GLU B C   1 
ATOM   7704 O O   . GLU B 1 431 ? -53.850 30.334 10.858  1.00 37.98 ? 431 GLU B O   1 
ATOM   7705 C CB  . GLU B 1 431 ? -54.249 33.477 10.048  1.00 44.90 ? 431 GLU B CB  1 
ATOM   7706 C CG  . GLU B 1 431 ? -55.452 34.380 9.888   1.00 54.12 ? 431 GLU B CG  1 
ATOM   7707 C CD  . GLU B 1 431 ? -56.752 33.597 9.792   1.00 65.49 ? 431 GLU B CD  1 
ATOM   7708 O OE1 . GLU B 1 431 ? -56.772 32.549 9.110   1.00 67.20 ? 431 GLU B OE1 1 
ATOM   7709 O OE2 . GLU B 1 431 ? -57.753 34.024 10.408  1.00 71.11 ? 431 GLU B OE2 1 
ATOM   7710 N N   . ALA B 1 432 ? -52.081 31.594 11.441  1.00 30.58 ? 432 ALA B N   1 
ATOM   7711 C CA  . ALA B 1 432 ? -51.166 30.461 11.364  1.00 33.74 ? 432 ALA B CA  1 
ATOM   7712 C C   . ALA B 1 432 ? -51.414 29.478 12.499  1.00 34.24 ? 432 ALA B C   1 
ATOM   7713 O O   . ALA B 1 432 ? -51.285 28.265 12.317  1.00 40.40 ? 432 ALA B O   1 
ATOM   7714 C CB  . ALA B 1 432 ? -49.722 30.955 11.394  1.00 31.16 ? 432 ALA B CB  1 
ATOM   7715 N N   . LYS B 1 433 ? -51.774 29.983 13.677  1.00 28.64 ? 433 LYS B N   1 
ATOM   7716 C CA  . LYS B 1 433 ? -52.027 29.094 14.805  1.00 30.10 ? 433 LYS B CA  1 
ATOM   7717 C C   . LYS B 1 433 ? -53.197 28.157 14.515  1.00 33.00 ? 433 LYS B C   1 
ATOM   7718 O O   . LYS B 1 433 ? -53.178 26.991 14.928  1.00 35.05 ? 433 LYS B O   1 
ATOM   7719 C CB  . LYS B 1 433 ? -52.259 29.924 16.070  1.00 25.30 ? 433 LYS B CB  1 
ATOM   7720 C CG  . LYS B 1 433 ? -52.627 29.119 17.319  1.00 30.92 ? 433 LYS B CG  1 
ATOM   7721 C CD  . LYS B 1 433 ? -51.510 28.190 17.795  1.00 29.88 ? 433 LYS B CD  1 
ATOM   7722 C CE  . LYS B 1 433 ? -51.996 27.358 18.978  1.00 32.70 ? 433 LYS B CE  1 
ATOM   7723 N NZ  . LYS B 1 433 ? -51.039 26.304 19.412  1.00 33.79 ? 433 LYS B NZ  1 
ATOM   7724 N N   . LYS B 1 434 ? -54.192 28.625 13.758  1.00 37.45 ? 434 LYS B N   1 
ATOM   7725 C CA  . LYS B 1 434 ? -55.306 27.761 13.382  1.00 41.51 ? 434 LYS B CA  1 
ATOM   7726 C C   . LYS B 1 434 ? -54.859 26.545 12.581  1.00 43.15 ? 434 LYS B C   1 
ATOM   7727 O O   . LYS B 1 434 ? -55.568 25.533 12.566  1.00 44.29 ? 434 LYS B O   1 
ATOM   7728 C CB  . LYS B 1 434 ? -56.341 28.548 12.571  1.00 42.56 ? 434 LYS B CB  1 
ATOM   7729 C CG  . LYS B 1 434 ? -56.959 29.722 13.301  1.00 40.42 ? 434 LYS B CG  1 
ATOM   7730 C CD  . LYS B 1 434 ? -58.380 29.981 12.803  1.00 53.13 ? 434 LYS B CD  1 
ATOM   7731 C CE  . LYS B 1 434 ? -58.857 31.368 13.205  1.00 60.06 ? 434 LYS B CE  1 
ATOM   7732 N NZ  . LYS B 1 434 ? -58.599 32.376 12.136  1.00 65.11 ? 434 LYS B NZ  1 
ATOM   7733 N N   . LYS B 1 435 ? -53.707 26.622 11.914  1.00 38.28 ? 435 LYS B N   1 
ATOM   7734 C CA  . LYS B 1 435 ? -53.230 25.554 11.043  1.00 41.42 ? 435 LYS B CA  1 
ATOM   7735 C C   . LYS B 1 435 ? -51.849 25.058 11.446  1.00 45.44 ? 435 LYS B C   1 
ATOM   7736 O O   . LYS B 1 435 ? -51.132 24.514 10.605  1.00 43.53 ? 435 LYS B O   1 
ATOM   7737 C CB  . LYS B 1 435 ? -53.192 26.015 9.582   1.00 46.31 ? 435 LYS B CB  1 
ATOM   7738 C CG  . LYS B 1 435 ? -54.335 26.917 9.138   1.00 52.18 ? 435 LYS B CG  1 
ATOM   7739 C CD  . LYS B 1 435 ? -53.986 27.568 7.798   1.00 52.11 ? 435 LYS B CD  1 
ATOM   7740 C CE  . LYS B 1 435 ? -55.219 28.071 7.068   1.00 54.60 ? 435 LYS B CE  1 
ATOM   7741 N NZ  . LYS B 1 435 ? -54.898 28.467 5.657   1.00 62.68 ? 435 LYS B NZ  1 
ATOM   7742 N N   . ALA B 1 436 ? -51.448 25.249 12.698  1.00 36.08 ? 436 ALA B N   1 
ATOM   7743 C CA  . ALA B 1 436 ? -50.088 24.922 13.105  1.00 34.53 ? 436 ALA B CA  1 
ATOM   7744 C C   . ALA B 1 436 ? -49.917 23.419 13.280  1.00 36.39 ? 436 ALA B C   1 
ATOM   7745 O O   . ALA B 1 436 ? -50.799 22.733 13.803  1.00 43.40 ? 436 ALA B O   1 
ATOM   7746 C CB  . ALA B 1 436 ? -49.718 25.653 14.406  1.00 30.04 ? 436 ALA B CB  1 
ATOM   7747 N N   . LYS B 1 437 ? -48.764 22.913 12.843  1.00 38.25 ? 437 LYS B N   1 
ATOM   7748 C CA  . LYS B 1 437 ? -48.451 21.495 12.915  1.00 37.55 ? 437 LYS B CA  1 
ATOM   7749 C C   . LYS B 1 437 ? -47.262 21.176 13.807  1.00 35.77 ? 437 LYS B C   1 
ATOM   7750 O O   . LYS B 1 437 ? -47.063 20.001 14.134  1.00 39.58 ? 437 LYS B O   1 
ATOM   7751 C CB  . LYS B 1 437 ? -48.166 20.930 11.511  1.00 37.62 ? 437 LYS B CB  1 
ATOM   7752 C CG  . LYS B 1 437 ? -49.405 20.695 10.653  1.00 48.53 ? 437 LYS B CG  1 
ATOM   7753 C CD  . LYS B 1 437 ? -49.809 21.966 9.948   1.00 54.15 ? 437 LYS B CD  1 
ATOM   7754 C CE  . LYS B 1 437 ? -50.898 21.740 8.897   1.00 52.76 ? 437 LYS B CE  1 
ATOM   7755 N NZ  . LYS B 1 437 ? -51.243 23.012 8.171   1.00 42.24 ? 437 LYS B NZ  1 
ATOM   7756 N N   . ASN B 1 438 ? -46.465 22.168 14.201  1.00 29.16 ? 438 ASN B N   1 
ATOM   7757 C CA  . ASN B 1 438 ? -45.230 21.915 14.928  1.00 28.67 ? 438 ASN B CA  1 
ATOM   7758 C C   . ASN B 1 438 ? -44.893 23.136 15.773  1.00 28.01 ? 438 ASN B C   1 
ATOM   7759 O O   . ASN B 1 438 ? -45.570 24.168 15.713  1.00 27.96 ? 438 ASN B O   1 
ATOM   7760 C CB  . ASN B 1 438 ? -44.085 21.579 13.971  1.00 28.79 ? 438 ASN B CB  1 
ATOM   7761 C CG  . ASN B 1 438 ? -43.813 22.689 12.976  1.00 33.59 ? 438 ASN B CG  1 
ATOM   7762 O OD1 . ASN B 1 438 ? -43.308 23.755 13.337  1.00 32.79 ? 438 ASN B OD1 1 
ATOM   7763 N ND2 . ASN B 1 438 ? -44.118 22.433 11.707  1.00 32.73 ? 438 ASN B ND2 1 
ATOM   7764 N N   . ASP B 1 439 ? -43.807 23.025 16.535  1.00 27.41 ? 439 ASP B N   1 
ATOM   7765 C CA  . ASP B 1 439 ? -43.447 24.026 17.532  1.00 25.84 ? 439 ASP B CA  1 
ATOM   7766 C C   . ASP B 1 439 ? -42.763 25.261 16.940  1.00 25.40 ? 439 ASP B C   1 
ATOM   7767 O O   . ASP B 1 439 ? -42.315 26.120 17.710  1.00 26.23 ? 439 ASP B O   1 
ATOM   7768 C CB  . ASP B 1 439 ? -42.550 23.398 18.607  1.00 30.69 ? 439 ASP B CB  1 
ATOM   7769 C CG  . ASP B 1 439 ? -43.316 22.489 19.557  1.00 33.68 ? 439 ASP B CG  1 
ATOM   7770 O OD1 . ASP B 1 439 ? -44.553 22.392 19.435  1.00 37.27 ? 439 ASP B OD1 1 
ATOM   7771 O OD2 . ASP B 1 439 ? -42.673 21.857 20.432  1.00 38.55 ? 439 ASP B OD2 1 
ATOM   7772 N N   . TYR B 1 440 ? -42.675 25.402 15.608  1.00 22.86 ? 440 TYR B N   1 
ATOM   7773 C CA  . TYR B 1 440 ? -42.242 26.693 15.088  1.00 22.23 ? 440 TYR B CA  1 
ATOM   7774 C C   . TYR B 1 440 ? -43.292 27.774 15.336  1.00 23.13 ? 440 TYR B C   1 
ATOM   7775 O O   . TYR B 1 440 ? -42.963 28.965 15.299  1.00 25.81 ? 440 TYR B O   1 
ATOM   7776 C CB  . TYR B 1 440 ? -41.891 26.582 13.595  1.00 22.05 ? 440 TYR B CB  1 
ATOM   7777 C CG  . TYR B 1 440 ? -40.449 26.165 13.352  1.00 26.22 ? 440 TYR B CG  1 
ATOM   7778 C CD1 . TYR B 1 440 ? -39.404 27.055 13.571  1.00 32.08 ? 440 TYR B CD1 1 
ATOM   7779 C CD2 . TYR B 1 440 ? -40.132 24.882 12.926  1.00 28.71 ? 440 TYR B CD2 1 
ATOM   7780 C CE1 . TYR B 1 440 ? -38.085 26.678 13.363  1.00 35.01 ? 440 TYR B CE1 1 
ATOM   7781 C CE2 . TYR B 1 440 ? -38.812 24.498 12.712  1.00 37.37 ? 440 TYR B CE2 1 
ATOM   7782 C CZ  . TYR B 1 440 ? -37.796 25.404 12.937  1.00 37.59 ? 440 TYR B CZ  1 
ATOM   7783 O OH  . TYR B 1 440 ? -36.484 25.045 12.728  1.00 40.65 ? 440 TYR B OH  1 
ATOM   7784 N N   . ILE B 1 441 ? -44.539 27.390 15.625  1.00 21.49 ? 441 ILE B N   1 
ATOM   7785 C CA  . ILE B 1 441 ? -45.514 28.383 16.071  1.00 26.63 ? 441 ILE B CA  1 
ATOM   7786 C C   . ILE B 1 441 ? -45.038 29.032 17.373  1.00 21.20 ? 441 ILE B C   1 
ATOM   7787 O O   . ILE B 1 441 ? -45.246 30.229 17.583  1.00 20.99 ? 441 ILE B O   1 
ATOM   7788 C CB  . ILE B 1 441 ? -46.928 27.756 16.199  1.00 28.31 ? 441 ILE B CB  1 
ATOM   7789 C CG1 . ILE B 1 441 ? -48.008 28.845 16.152  1.00 22.36 ? 441 ILE B CG1 1 
ATOM   7790 C CG2 . ILE B 1 441 ? -47.080 26.917 17.491  1.00 24.74 ? 441 ILE B CG2 1 
ATOM   7791 C CD1 . ILE B 1 441 ? -48.066 29.596 14.810  1.00 27.41 ? 441 ILE B CD1 1 
ATOM   7792 N N   . LEU B 1 442 ? -44.347 28.276 18.233  1.00 17.27 ? 442 LEU B N   1 
ATOM   7793 C CA  . LEU B 1 442 ? -43.818 28.847 19.475  1.00 19.10 ? 442 LEU B CA  1 
ATOM   7794 C C   . LEU B 1 442 ? -42.677 29.822 19.194  1.00 17.96 ? 442 LEU B C   1 
ATOM   7795 O O   . LEU B 1 442 ? -42.543 30.852 19.869  1.00 19.08 ? 442 LEU B O   1 
ATOM   7796 C CB  . LEU B 1 442 ? -43.342 27.732 20.400  1.00 18.14 ? 442 LEU B CB  1 
ATOM   7797 C CG  . LEU B 1 442 ? -44.343 26.632 20.756  1.00 21.93 ? 442 LEU B CG  1 
ATOM   7798 C CD1 . LEU B 1 442 ? -43.619 25.547 21.549  1.00 23.96 ? 442 LEU B CD1 1 
ATOM   7799 C CD2 . LEU B 1 442 ? -45.560 27.194 21.523  1.00 19.31 ? 442 LEU B CD2 1 
ATOM   7800 N N   . VAL B 1 443 ? -41.852 29.520 18.192  1.00 19.32 ? 443 VAL B N   1 
ATOM   7801 C CA  . VAL B 1 443 ? -40.792 30.445 17.801  1.00 22.58 ? 443 VAL B CA  1 
ATOM   7802 C C   . VAL B 1 443 ? -41.401 31.777 17.382  1.00 21.82 ? 443 VAL B C   1 
ATOM   7803 O O   . VAL B 1 443 ? -40.945 32.852 17.791  1.00 18.97 ? 443 VAL B O   1 
ATOM   7804 C CB  . VAL B 1 443 ? -39.936 29.844 16.667  1.00 19.16 ? 443 VAL B CB  1 
ATOM   7805 C CG1 . VAL B 1 443 ? -38.802 30.797 16.316  1.00 20.91 ? 443 VAL B CG1 1 
ATOM   7806 C CG2 . VAL B 1 443 ? -39.417 28.472 17.041  1.00 17.39 ? 443 VAL B CG2 1 
ATOM   7807 N N   . ALA B 1 444 ? -42.447 31.716 16.550  1.00 19.53 ? 444 ALA B N   1 
ATOM   7808 C CA  . ALA B 1 444 ? -43.116 32.911 16.045  1.00 18.13 ? 444 ALA B CA  1 
ATOM   7809 C C   . ALA B 1 444 ? -43.813 33.706 17.143  1.00 21.45 ? 444 ALA B C   1 
ATOM   7810 O O   . ALA B 1 444 ? -44.206 34.852 16.911  1.00 22.21 ? 444 ALA B O   1 
ATOM   7811 C CB  . ALA B 1 444 ? -44.131 32.508 14.963  1.00 18.81 ? 444 ALA B CB  1 
ATOM   7812 N N   . GLU B 1 445 ? -43.993 33.125 18.320  1.00 19.95 ? 445 GLU B N   1 
ATOM   7813 C CA  . GLU B 1 445 ? -44.619 33.815 19.435  1.00 21.34 ? 445 GLU B CA  1 
ATOM   7814 C C   . GLU B 1 445 ? -43.634 34.655 20.237  1.00 18.67 ? 445 GLU B C   1 
ATOM   7815 O O   . GLU B 1 445 ? -44.049 35.334 21.186  1.00 20.44 ? 445 GLU B O   1 
ATOM   7816 C CB  . GLU B 1 445 ? -45.320 32.792 20.339  1.00 25.08 ? 445 GLU B CB  1 
ATOM   7817 C CG  . GLU B 1 445 ? -46.592 32.260 19.678  1.00 18.13 ? 445 GLU B CG  1 
ATOM   7818 C CD  . GLU B 1 445 ? -47.124 30.956 20.272  1.00 24.32 ? 445 GLU B CD  1 
ATOM   7819 O OE1 . GLU B 1 445 ? -46.624 30.513 21.335  1.00 24.94 ? 445 GLU B OE1 1 
ATOM   7820 O OE2 . GLU B 1 445 ? -48.080 30.396 19.683  1.00 20.96 ? 445 GLU B OE2 1 
ATOM   7821 N N   . GLY B 1 446 ? -42.353 34.630 19.874  1.00 19.36 ? 446 GLY B N   1 
ATOM   7822 C CA  . GLY B 1 446 ? -41.367 35.406 20.601  1.00 17.98 ? 446 GLY B CA  1 
ATOM   7823 C C   . GLY B 1 446 ? -41.637 36.895 20.495  1.00 18.86 ? 446 GLY B C   1 
ATOM   7824 O O   . GLY B 1 446 ? -42.153 37.389 19.489  1.00 18.01 ? 446 GLY B O   1 
ATOM   7825 N N   . SER B 1 447 ? -41.275 37.625 21.555  1.00 19.84 ? 447 SER B N   1 
ATOM   7826 C CA  . SER B 1 447 ? -41.634 39.037 21.593  1.00 21.01 ? 447 SER B CA  1 
ATOM   7827 C C   . SER B 1 447 ? -40.841 39.855 20.582  1.00 17.23 ? 447 SER B C   1 
ATOM   7828 O O   . SER B 1 447 ? -41.334 40.891 20.123  1.00 18.59 ? 447 SER B O   1 
ATOM   7829 C CB  . SER B 1 447 ? -41.441 39.608 23.012  1.00 20.46 ? 447 SER B CB  1 
ATOM   7830 O OG  . SER B 1 447 ? -40.071 39.618 23.383  1.00 19.31 ? 447 SER B OG  1 
ATOM   7831 N N   . ASP B 1 448 ? -39.659 39.385 20.181  1.00 17.86 ? 448 ASP B N   1 
ATOM   7832 C CA  . ASP B 1 448 ? -38.764 40.215 19.378  1.00 15.41 ? 448 ASP B CA  1 
ATOM   7833 C C   . ASP B 1 448 ? -39.384 40.602 18.033  1.00 18.38 ? 448 ASP B C   1 
ATOM   7834 O O   . ASP B 1 448 ? -39.215 41.738 17.578  1.00 20.22 ? 448 ASP B O   1 
ATOM   7835 C CB  . ASP B 1 448 ? -37.444 39.487 19.157  1.00 17.17 ? 448 ASP B CB  1 
ATOM   7836 C CG  . ASP B 1 448 ? -36.807 39.091 20.446  1.00 17.18 ? 448 ASP B CG  1 
ATOM   7837 O OD1 . ASP B 1 448 ? -37.237 38.040 21.003  1.00 19.18 ? 448 ASP B OD1 1 
ATOM   7838 O OD2 . ASP B 1 448 ? -35.937 39.852 20.930  1.00 20.07 ? 448 ASP B OD2 1 
ATOM   7839 N N   . TRP B 1 449 ? -40.086 39.673 17.377  1.00 18.48 ? 449 TRP B N   1 
ATOM   7840 C CA  . TRP B 1 449 ? -40.665 39.980 16.062  1.00 14.41 ? 449 TRP B CA  1 
ATOM   7841 C C   . TRP B 1 449 ? -41.589 41.189 16.141  1.00 20.96 ? 449 TRP B C   1 
ATOM   7842 O O   . TRP B 1 449 ? -41.537 42.086 15.288  1.00 18.58 ? 449 TRP B O   1 
ATOM   7843 C CB  . TRP B 1 449 ? -41.408 38.757 15.522  1.00 21.68 ? 449 TRP B CB  1 
ATOM   7844 C CG  . TRP B 1 449 ? -40.684 37.469 15.842  1.00 17.37 ? 449 TRP B CG  1 
ATOM   7845 C CD1 . TRP B 1 449 ? -41.154 36.418 16.572  1.00 22.74 ? 449 TRP B CD1 1 
ATOM   7846 C CD2 . TRP B 1 449 ? -39.355 37.128 15.462  1.00 18.16 ? 449 TRP B CD2 1 
ATOM   7847 N NE1 . TRP B 1 449 ? -40.192 35.447 16.689  1.00 17.90 ? 449 TRP B NE1 1 
ATOM   7848 C CE2 . TRP B 1 449 ? -39.076 35.852 16.007  1.00 16.90 ? 449 TRP B CE2 1 
ATOM   7849 C CE3 . TRP B 1 449 ? -38.368 37.773 14.708  1.00 18.39 ? 449 TRP B CE3 1 
ATOM   7850 C CZ2 . TRP B 1 449 ? -37.851 35.209 15.824  1.00 13.90 ? 449 TRP B CZ2 1 
ATOM   7851 C CZ3 . TRP B 1 449 ? -37.138 37.137 14.537  1.00 19.85 ? 449 TRP B CZ3 1 
ATOM   7852 C CH2 . TRP B 1 449 ? -36.905 35.858 15.079  1.00 19.96 ? 449 TRP B CH2 1 
ATOM   7853 N N   . PHE B 1 450 ? -42.425 41.240 17.179  1.00 20.23 ? 450 PHE B N   1 
ATOM   7854 C CA  . PHE B 1 450 ? -43.396 42.317 17.353  1.00 24.45 ? 450 PHE B CA  1 
ATOM   7855 C C   . PHE B 1 450 ? -42.727 43.627 17.767  1.00 19.19 ? 450 PHE B C   1 
ATOM   7856 O O   . PHE B 1 450 ? -43.209 44.715 17.416  1.00 21.53 ? 450 PHE B O   1 
ATOM   7857 C CB  . PHE B 1 450 ? -44.447 41.874 18.388  1.00 23.34 ? 450 PHE B CB  1 
ATOM   7858 C CG  . PHE B 1 450 ? -45.076 40.550 18.064  1.00 19.13 ? 450 PHE B CG  1 
ATOM   7859 C CD1 . PHE B 1 450 ? -46.221 40.498 17.277  1.00 19.53 ? 450 PHE B CD1 1 
ATOM   7860 C CD2 . PHE B 1 450 ? -44.502 39.354 18.485  1.00 22.38 ? 450 PHE B CD2 1 
ATOM   7861 C CE1 . PHE B 1 450 ? -46.790 39.286 16.933  1.00 19.54 ? 450 PHE B CE1 1 
ATOM   7862 C CE2 . PHE B 1 450 ? -45.069 38.127 18.141  1.00 21.09 ? 450 PHE B CE2 1 
ATOM   7863 C CZ  . PHE B 1 450 ? -46.228 38.103 17.369  1.00 18.58 ? 450 PHE B CZ  1 
ATOM   7864 N N   . TRP B 1 451 ? -41.637 43.544 18.527  1.00 17.54 ? 451 TRP B N   1 
ATOM   7865 C CA  . TRP B 1 451 ? -40.888 44.733 18.912  1.00 17.30 ? 451 TRP B CA  1 
ATOM   7866 C C   . TRP B 1 451 ? -40.424 45.521 17.680  1.00 22.73 ? 451 TRP B C   1 
ATOM   7867 O O   . TRP B 1 451 ? -40.609 46.745 17.598  1.00 19.82 ? 451 TRP B O   1 
ATOM   7868 C CB  . TRP B 1 451 ? -39.701 44.308 19.795  1.00 18.59 ? 451 TRP B CB  1 
ATOM   7869 C CG  . TRP B 1 451 ? -38.693 45.387 20.065  1.00 20.64 ? 451 TRP B CG  1 
ATOM   7870 C CD1 . TRP B 1 451 ? -37.685 45.788 19.240  1.00 20.36 ? 451 TRP B CD1 1 
ATOM   7871 C CD2 . TRP B 1 451 ? -38.587 46.189 21.243  1.00 22.58 ? 451 TRP B CD2 1 
ATOM   7872 N NE1 . TRP B 1 451 ? -36.968 46.798 19.820  1.00 24.58 ? 451 TRP B NE1 1 
ATOM   7873 C CE2 . TRP B 1 451 ? -37.500 47.063 21.056  1.00 28.57 ? 451 TRP B CE2 1 
ATOM   7874 C CE3 . TRP B 1 451 ? -39.293 46.239 22.449  1.00 33.87 ? 451 TRP B CE3 1 
ATOM   7875 C CZ2 . TRP B 1 451 ? -37.113 47.995 22.019  1.00 29.28 ? 451 TRP B CZ2 1 
ATOM   7876 C CZ3 . TRP B 1 451 ? -38.909 47.173 23.411  1.00 37.90 ? 451 TRP B CZ3 1 
ATOM   7877 C CH2 . TRP B 1 451 ? -37.826 48.032 23.189  1.00 38.42 ? 451 TRP B CH2 1 
ATOM   7878 N N   . TRP B 1 452 ? -39.827 44.825 16.701  1.00 19.80 ? 452 TRP B N   1 
ATOM   7879 C CA  . TRP B 1 452 ? -39.266 45.475 15.521  1.00 21.22 ? 452 TRP B CA  1 
ATOM   7880 C C   . TRP B 1 452 ? -40.310 45.818 14.475  1.00 19.96 ? 452 TRP B C   1 
ATOM   7881 O O   . TRP B 1 452 ? -40.073 46.715 13.649  1.00 21.50 ? 452 TRP B O   1 
ATOM   7882 C CB  . TRP B 1 452 ? -38.201 44.568 14.882  1.00 21.30 ? 452 TRP B CB  1 
ATOM   7883 C CG  . TRP B 1 452 ? -37.078 44.307 15.815  1.00 19.39 ? 452 TRP B CG  1 
ATOM   7884 C CD1 . TRP B 1 452 ? -36.785 43.128 16.438  1.00 17.83 ? 452 TRP B CD1 1 
ATOM   7885 C CD2 . TRP B 1 452 ? -36.129 45.258 16.287  1.00 19.25 ? 452 TRP B CD2 1 
ATOM   7886 N NE1 . TRP B 1 452 ? -35.683 43.276 17.242  1.00 17.55 ? 452 TRP B NE1 1 
ATOM   7887 C CE2 . TRP B 1 452 ? -35.268 44.578 17.189  1.00 18.60 ? 452 TRP B CE2 1 
ATOM   7888 C CE3 . TRP B 1 452 ? -35.918 46.614 16.048  1.00 20.88 ? 452 TRP B CE3 1 
ATOM   7889 C CZ2 . TRP B 1 452 ? -34.210 45.209 17.832  1.00 21.11 ? 452 TRP B CZ2 1 
ATOM   7890 C CZ3 . TRP B 1 452 ? -34.867 47.244 16.689  1.00 22.21 ? 452 TRP B CZ3 1 
ATOM   7891 C CH2 . TRP B 1 452 ? -34.025 46.545 17.574  1.00 22.52 ? 452 TRP B CH2 1 
ATOM   7892 N N   . GLN B 1 453 ? -41.444 45.126 14.473  1.00 24.05 ? 453 GLN B N   1 
ATOM   7893 C CA  . GLN B 1 453 ? -42.455 45.378 13.453  1.00 25.69 ? 453 GLN B CA  1 
ATOM   7894 C C   . GLN B 1 453 ? -43.001 46.790 13.580  1.00 24.63 ? 453 GLN B C   1 
ATOM   7895 O O   . GLN B 1 453 ? -43.148 47.326 14.681  1.00 27.81 ? 453 GLN B O   1 
ATOM   7896 C CB  . GLN B 1 453 ? -43.590 44.356 13.565  1.00 23.22 ? 453 GLN B CB  1 
ATOM   7897 C CG  . GLN B 1 453 ? -44.897 44.720 12.856  1.00 32.10 ? 453 GLN B CG  1 
ATOM   7898 C CD  . GLN B 1 453 ? -44.771 44.728 11.338  1.00 39.51 ? 453 GLN B CD  1 
ATOM   7899 O OE1 . GLN B 1 453 ? -43.684 44.565 10.787  1.00 32.23 ? 453 GLN B OE1 1 
ATOM   7900 N NE2 . GLN B 1 453 ? -45.898 44.908 10.656  1.00 34.08 ? 453 GLN B NE2 1 
ATOM   7901 N N   . GLY B 1 454 ? -43.342 47.355 12.460  1.00 33.16 ? 454 GLY B N   1 
ATOM   7902 C CA  . GLY B 1 454 ? -43.990 48.624 12.433  1.00 42.93 ? 454 GLY B CA  1 
ATOM   7903 C C   . GLY B 1 454 ? -43.320 49.665 13.230  1.00 52.76 ? 454 GLY B C   1 
ATOM   7904 O O   . GLY B 1 454 ? -43.884 50.204 14.162  1.00 51.54 ? 454 GLY B O   1 
ATOM   7905 N N   . GLU B 1 455 ? -42.084 49.910 12.839  1.00 52.77 ? 455 GLU B N   1 
ATOM   7906 C CA  . GLU B 1 455 ? -41.277 50.929 13.429  1.00 56.19 ? 455 GLU B CA  1 
ATOM   7907 C C   . GLU B 1 455 ? -40.690 51.639 12.212  1.00 63.70 ? 455 GLU B C   1 
ATOM   7908 O O   . GLU B 1 455 ? -40.752 51.111 11.119  1.00 55.89 ? 455 GLU B O   1 
ATOM   7909 C CB  . GLU B 1 455 ? -40.188 50.306 14.289  1.00 49.22 ? 455 GLU B CB  1 
ATOM   7910 C CG  . GLU B 1 455 ? -40.682 49.563 15.529  1.00 41.56 ? 455 GLU B CG  1 
ATOM   7911 C CD  . GLU B 1 455 ? -41.076 50.473 16.683  1.00 47.20 ? 455 GLU B CD  1 
ATOM   7912 O OE1 . GLU B 1 455 ? -41.920 50.076 17.509  1.00 41.40 ? 455 GLU B OE1 1 
ATOM   7913 O OE2 . GLU B 1 455 ? -40.536 51.569 16.759  1.00 52.09 ? 455 GLU B OE2 1 
ATOM   7914 N N   . GLU B 1 456 ? -40.088 52.820 12.390  1.00 68.81 ? 456 GLU B N   1 
ATOM   7915 C CA  . GLU B 1 456 ? -39.396 53.537 11.313  1.00 66.92 ? 456 GLU B CA  1 
ATOM   7916 C C   . GLU B 1 456 ? -38.474 52.487 10.692  1.00 64.14 ? 456 GLU B C   1 
ATOM   7917 O O   . GLU B 1 456 ? -38.098 51.581 11.414  1.00 63.24 ? 456 GLU B O   1 
ATOM   7918 C CB  . GLU B 1 456 ? -38.467 54.578 11.905  1.00 73.39 ? 456 GLU B CB  1 
ATOM   7919 C CG  . GLU B 1 456 ? -39.053 55.890 12.412  1.00 78.32 ? 456 GLU B CG  1 
ATOM   7920 C CD  . GLU B 1 456 ? -38.018 57.028 12.512  1.00 79.78 ? 456 GLU B CD  1 
ATOM   7921 O OE1 . GLU B 1 456 ? -38.112 57.839 13.478  1.00 78.57 ? 456 GLU B OE1 1 
ATOM   7922 O OE2 . GLU B 1 456 ? -37.122 57.108 11.622  1.00 77.84 ? 456 GLU B OE2 1 
ATOM   7923 N N   . LYS B 1 457 ? -38.132 52.553 9.407   1.00 57.97 ? 457 LYS B N   1 
ATOM   7924 C CA  . LYS B 1 457 ? -37.250 51.538 8.856   1.00 57.07 ? 457 LYS B CA  1 
ATOM   7925 C C   . LYS B 1 457 ? -35.891 51.820 9.444   1.00 63.86 ? 457 LYS B C   1 
ATOM   7926 O O   . LYS B 1 457 ? -35.650 52.927 9.856   1.00 68.36 ? 457 LYS B O   1 
ATOM   7927 C CB  . LYS B 1 457 ? -37.242 51.490 7.316   1.00 50.87 ? 457 LYS B CB  1 
ATOM   7928 C CG  . LYS B 1 457 ? -36.060 52.197 6.646   1.00 57.76 ? 457 LYS B CG  1 
ATOM   7929 C CD  . LYS B 1 457 ? -35.974 51.974 5.147   1.00 58.95 ? 457 LYS B CD  1 
ATOM   7930 C CE  . LYS B 1 457 ? -35.720 53.283 4.430   1.00 60.75 ? 457 LYS B CE  1 
ATOM   7931 N NZ  . LYS B 1 457 ? -35.896 53.131 2.957   1.00 65.53 ? 457 LYS B NZ  1 
ATOM   7932 N N   . ALA B 1 458 ? -35.005 50.825 9.458   1.00 57.65 ? 458 ALA B N   1 
ATOM   7933 C CA  . ALA B 1 458 ? -33.650 50.961 9.974   1.00 49.65 ? 458 ALA B CA  1 
ATOM   7934 C C   . ALA B 1 458 ? -32.901 49.776 9.446   1.00 46.55 ? 458 ALA B C   1 
ATOM   7935 O O   . ALA B 1 458 ? -33.497 48.797 9.139   1.00 42.24 ? 458 ALA B O   1 
ATOM   7936 C CB  . ALA B 1 458 ? -33.644 50.958 11.467  1.00 46.94 ? 458 ALA B CB  1 
ATOM   7937 N N   . PRO B 1 459 ? -31.599 49.866 9.328   1.00 51.46 ? 459 PRO B N   1 
ATOM   7938 C CA  . PRO B 1 459 ? -30.848 48.735 8.749   1.00 48.95 ? 459 PRO B CA  1 
ATOM   7939 C C   . PRO B 1 459 ? -30.891 47.374 9.433   1.00 38.64 ? 459 PRO B C   1 
ATOM   7940 O O   . PRO B 1 459 ? -30.781 47.359 10.620  1.00 34.74 ? 459 PRO B O   1 
ATOM   7941 C CB  . PRO B 1 459 ? -29.409 49.242 8.711   1.00 53.57 ? 459 PRO B CB  1 
ATOM   7942 C CG  . PRO B 1 459 ? -29.323 50.275 9.715   1.00 56.08 ? 459 PRO B CG  1 
ATOM   7943 C CD  . PRO B 1 459 ? -30.596 50.979 9.643   1.00 57.46 ? 459 PRO B CD  1 
ATOM   7944 N N   . PHE B 1 460 ? -30.975 46.301 8.630   1.00 39.29 ? 460 PHE B N   1 
ATOM   7945 C CA  . PHE B 1 460 ? -31.099 44.895 9.005   1.00 36.74 ? 460 PHE B CA  1 
ATOM   7946 C C   . PHE B 1 460 ? -32.461 44.557 9.609   1.00 34.18 ? 460 PHE B C   1 
ATOM   7947 O O   . PHE B 1 460 ? -32.751 43.372 9.793   1.00 30.78 ? 460 PHE B O   1 
ATOM   7948 C CB  . PHE B 1 460 ? -29.994 44.425 9.974   1.00 31.31 ? 460 PHE B CB  1 
ATOM   7949 C CG  . PHE B 1 460 ? -28.605 44.542 9.404   1.00 40.70 ? 460 PHE B CG  1 
ATOM   7950 C CD1 . PHE B 1 460 ? -28.144 43.619 8.477   1.00 43.92 ? 460 PHE B CD1 1 
ATOM   7951 C CD2 . PHE B 1 460 ? -27.758 45.572 9.795   1.00 33.85 ? 460 PHE B CD2 1 
ATOM   7952 C CE1 . PHE B 1 460 ? -26.869 43.719 7.943   1.00 44.40 ? 460 PHE B CE1 1 
ATOM   7953 C CE2 . PHE B 1 460 ? -26.487 45.678 9.270   1.00 45.19 ? 460 PHE B CE2 1 
ATOM   7954 C CZ  . PHE B 1 460 ? -26.040 44.754 8.337   1.00 50.05 ? 460 PHE B CZ  1 
ATOM   7955 N N   . VAL B 1 461 ? -33.318 45.538 9.903   1.00 38.76 ? 461 VAL B N   1 
ATOM   7956 C CA  . VAL B 1 461 ? -34.590 45.234 10.561  1.00 44.78 ? 461 VAL B CA  1 
ATOM   7957 C C   . VAL B 1 461 ? -35.489 44.388 9.669   1.00 41.10 ? 461 VAL B C   1 
ATOM   7958 O O   . VAL B 1 461 ? -36.318 43.614 10.170  1.00 43.68 ? 461 VAL B O   1 
ATOM   7959 C CB  . VAL B 1 461 ? -35.289 46.534 10.998  1.00 55.38 ? 461 VAL B CB  1 
ATOM   7960 C CG1 . VAL B 1 461 ? -36.516 46.223 11.858  1.00 52.11 ? 461 VAL B CG1 1 
ATOM   7961 C CG2 . VAL B 1 461 ? -34.315 47.391 11.785  1.00 55.22 ? 461 VAL B CG2 1 
ATOM   7962 N N   . GLU B 1 462 ? -35.334 44.503 8.345   1.00 29.60 ? 462 GLU B N   1 
ATOM   7963 C CA  . GLU B 1 462 ? -36.039 43.641 7.404   1.00 35.89 ? 462 GLU B CA  1 
ATOM   7964 C C   . GLU B 1 462 ? -35.756 42.160 7.639   1.00 30.27 ? 462 GLU B C   1 
ATOM   7965 O O   . GLU B 1 462 ? -36.581 41.312 7.271   1.00 31.03 ? 462 GLU B O   1 
ATOM   7966 C CB  . GLU B 1 462 ? -35.650 44.024 5.965   1.00 44.11 ? 462 GLU B CB  1 
ATOM   7967 C CG  . GLU B 1 462 ? -34.131 44.085 5.706   1.00 63.37 ? 462 GLU B CG  1 
ATOM   7968 C CD  . GLU B 1 462 ? -33.521 45.485 5.867   1.00 71.00 ? 462 GLU B CD  1 
ATOM   7969 O OE1 . GLU B 1 462 ? -32.782 45.929 4.956   1.00 72.45 ? 462 GLU B OE1 1 
ATOM   7970 O OE2 . GLU B 1 462 ? -33.765 46.136 6.907   1.00 67.07 ? 462 GLU B OE2 1 
ATOM   7971 N N   . VAL B 1 463 ? -34.617 41.830 8.250   1.00 23.10 ? 463 VAL B N   1 
ATOM   7972 C CA  . VAL B 1 463 ? -34.277 40.431 8.460   1.00 22.20 ? 463 VAL B CA  1 
ATOM   7973 C C   . VAL B 1 463 ? -35.147 39.813 9.544   1.00 22.99 ? 463 VAL B C   1 
ATOM   7974 O O   . VAL B 1 463 ? -35.479 38.622 9.471   1.00 23.62 ? 463 VAL B O   1 
ATOM   7975 C CB  . VAL B 1 463 ? -32.772 40.302 8.777   1.00 24.51 ? 463 VAL B CB  1 
ATOM   7976 C CG1 . VAL B 1 463 ? -32.409 38.864 9.123   1.00 26.85 ? 463 VAL B CG1 1 
ATOM   7977 C CG2 . VAL B 1 463 ? -31.955 40.798 7.605   1.00 28.09 ? 463 VAL B CG2 1 
ATOM   7978 N N   . PHE B 1 464 ? -35.575 40.609 10.538  1.00 20.21 ? 464 PHE B N   1 
ATOM   7979 C CA  . PHE B 1 464 ? -36.475 40.083 11.562  1.00 17.72 ? 464 PHE B CA  1 
ATOM   7980 C C   . PHE B 1 464 ? -37.816 39.691 10.956  1.00 20.28 ? 464 PHE B C   1 
ATOM   7981 O O   . PHE B 1 464 ? -38.399 38.669 11.337  1.00 19.91 ? 464 PHE B O   1 
ATOM   7982 C CB  . PHE B 1 464 ? -36.663 41.104 12.689  1.00 17.40 ? 464 PHE B CB  1 
ATOM   7983 C CG  . PHE B 1 464 ? -35.429 41.316 13.531  1.00 18.38 ? 464 PHE B CG  1 
ATOM   7984 C CD1 . PHE B 1 464 ? -35.208 40.534 14.673  1.00 22.10 ? 464 PHE B CD1 1 
ATOM   7985 C CD2 . PHE B 1 464 ? -34.513 42.292 13.201  1.00 25.12 ? 464 PHE B CD2 1 
ATOM   7986 C CE1 . PHE B 1 464 ? -34.045 40.717 15.449  1.00 16.50 ? 464 PHE B CE1 1 
ATOM   7987 C CE2 . PHE B 1 464 ? -33.371 42.498 13.968  1.00 18.43 ? 464 PHE B CE2 1 
ATOM   7988 C CZ  . PHE B 1 464 ? -33.141 41.706 15.097  1.00 17.38 ? 464 PHE B CZ  1 
ATOM   7989 N N   . ASP B 1 465 ? -38.307 40.482 9.994   1.00 26.80 ? 465 ASP B N   1 
ATOM   7990 C CA  . ASP B 1 465 ? -39.547 40.144 9.304   1.00 19.24 ? 465 ASP B CA  1 
ATOM   7991 C C   . ASP B 1 465 ? -39.409 38.862 8.495   1.00 22.88 ? 465 ASP B C   1 
ATOM   7992 O O   . ASP B 1 465 ? -40.309 38.010 8.515   1.00 21.48 ? 465 ASP B O   1 
ATOM   7993 C CB  . ASP B 1 465 ? -39.969 41.305 8.396   1.00 20.92 ? 465 ASP B CB  1 
ATOM   7994 C CG  . ASP B 1 465 ? -41.192 40.981 7.564   1.00 26.62 ? 465 ASP B CG  1 
ATOM   7995 O OD1 . ASP B 1 465 ? -42.312 41.117 8.087   1.00 26.15 ? 465 ASP B OD1 1 
ATOM   7996 O OD2 . ASP B 1 465 ? -41.032 40.586 6.396   1.00 25.93 ? 465 ASP B OD2 1 
ATOM   7997 N N   . LYS B 1 466 ? -38.305 38.716 7.754   1.00 20.35 ? 466 LYS B N   1 
ATOM   7998 C CA  . LYS B 1 466 ? -38.081 37.484 7.005   1.00 28.21 ? 466 LYS B CA  1 
ATOM   7999 C C   . LYS B 1 466 ? -38.035 36.271 7.930   1.00 23.69 ? 466 LYS B C   1 
ATOM   8000 O O   . LYS B 1 466 ? -38.610 35.224 7.610   1.00 24.79 ? 466 LYS B O   1 
ATOM   8001 C CB  . LYS B 1 466 ? -36.795 37.598 6.187   1.00 23.54 ? 466 LYS B CB  1 
ATOM   8002 C CG  . LYS B 1 466 ? -36.336 36.310 5.554   1.00 29.65 ? 466 LYS B CG  1 
ATOM   8003 C CD  . LYS B 1 466 ? -35.508 36.618 4.322   1.00 44.02 ? 466 LYS B CD  1 
ATOM   8004 C CE  . LYS B 1 466 ? -35.045 35.356 3.621   1.00 58.93 ? 466 LYS B CE  1 
ATOM   8005 N NZ  . LYS B 1 466 ? -33.603 35.118 3.909   1.00 65.74 ? 466 LYS B NZ  1 
ATOM   8006 N N   . LEU B 1 467 ? -37.358 36.391 9.077   1.00 20.52 ? 467 LEU B N   1 
ATOM   8007 C CA  . LEU B 1 467 ? -37.327 35.297 10.053  1.00 18.51 ? 467 LEU B CA  1 
ATOM   8008 C C   . LEU B 1 467 ? -38.726 34.976 10.581  1.00 18.76 ? 467 LEU B C   1 
ATOM   8009 O O   . LEU B 1 467 ? -39.165 33.819 10.552  1.00 21.67 ? 467 LEU B O   1 
ATOM   8010 C CB  . LEU B 1 467 ? -36.394 35.658 11.221  1.00 16.63 ? 467 LEU B CB  1 
ATOM   8011 C CG  . LEU B 1 467 ? -34.904 35.528 10.876  1.00 18.94 ? 467 LEU B CG  1 
ATOM   8012 C CD1 . LEU B 1 467 ? -34.046 36.170 11.961  1.00 16.94 ? 467 LEU B CD1 1 
ATOM   8013 C CD2 . LEU B 1 467 ? -34.540 34.073 10.680  1.00 19.62 ? 467 LEU B CD2 1 
ATOM   8014 N N   . PHE B 1 468 ? -39.443 35.990 11.067  1.00 16.98 ? 468 PHE B N   1 
ATOM   8015 C CA  . PHE B 1 468 ? -40.791 35.771 11.598  1.00 20.80 ? 468 PHE B CA  1 
ATOM   8016 C C   . PHE B 1 468 ? -41.674 35.062 10.580  1.00 21.56 ? 468 PHE B C   1 
ATOM   8017 O O   . PHE B 1 468 ? -42.359 34.077 10.889  1.00 18.28 ? 468 PHE B O   1 
ATOM   8018 C CB  . PHE B 1 468 ? -41.416 37.112 11.989  1.00 19.95 ? 468 PHE B CB  1 
ATOM   8019 C CG  . PHE B 1 468 ? -42.885 37.027 12.347  1.00 23.95 ? 468 PHE B CG  1 
ATOM   8020 C CD1 . PHE B 1 468 ? -43.283 36.472 13.558  1.00 18.96 ? 468 PHE B CD1 1 
ATOM   8021 C CD2 . PHE B 1 468 ? -43.864 37.496 11.473  1.00 24.23 ? 468 PHE B CD2 1 
ATOM   8022 C CE1 . PHE B 1 468 ? -44.635 36.406 13.899  1.00 22.61 ? 468 PHE B CE1 1 
ATOM   8023 C CE2 . PHE B 1 468 ? -45.212 37.440 11.800  1.00 20.76 ? 468 PHE B CE2 1 
ATOM   8024 C CZ  . PHE B 1 468 ? -45.602 36.892 13.034  1.00 21.99 ? 468 PHE B CZ  1 
ATOM   8025 N N   . ARG B 1 469 ? -41.676 35.554 9.351   1.00 21.60 ? 469 ARG B N   1 
ATOM   8026 C CA  . ARG B 1 469 ? -42.555 34.947 8.364   1.00 23.57 ? 469 ARG B CA  1 
ATOM   8027 C C   . ARG B 1 469 ? -42.055 33.566 7.950   1.00 25.40 ? 469 ARG B C   1 
ATOM   8028 O O   . ARG B 1 469 ? -42.864 32.690 7.628   1.00 24.05 ? 469 ARG B O   1 
ATOM   8029 C CB  . ARG B 1 469 ? -42.693 35.883 7.168   1.00 25.54 ? 469 ARG B CB  1 
ATOM   8030 C CG  . ARG B 1 469 ? -43.447 37.160 7.503   1.00 32.58 ? 469 ARG B CG  1 
ATOM   8031 C CD  . ARG B 1 469 ? -43.574 38.039 6.280   1.00 34.96 ? 469 ARG B CD  1 
ATOM   8032 N NE  . ARG B 1 469 ? -44.219 39.315 6.580   1.00 29.69 ? 469 ARG B NE  1 
ATOM   8033 C CZ  . ARG B 1 469 ? -45.504 39.566 6.351   1.00 29.23 ? 469 ARG B CZ  1 
ATOM   8034 N NH1 . ARG B 1 469 ? -46.288 38.622 5.837   1.00 27.70 ? 469 ARG B NH1 1 
ATOM   8035 N NH2 . ARG B 1 469 ? -46.008 40.757 6.644   1.00 36.15 ? 469 ARG B NH2 1 
ATOM   8036 N N   . SER B 1 470 ? -40.741 33.341 7.986   1.00 23.46 ? 470 SER B N   1 
ATOM   8037 C CA  . SER B 1 470 ? -40.216 31.994 7.786   1.00 29.24 ? 470 SER B CA  1 
ATOM   8038 C C   . SER B 1 470 ? -40.740 31.038 8.851   1.00 19.45 ? 470 SER B C   1 
ATOM   8039 O O   . SER B 1 470 ? -41.166 29.919 8.548   1.00 29.96 ? 470 SER B O   1 
ATOM   8040 C CB  . SER B 1 470 ? -38.687 32.019 7.798   1.00 41.23 ? 470 SER B CB  1 
ATOM   8041 O OG  . SER B 1 470 ? -38.191 32.710 6.668   1.00 49.81 ? 470 SER B OG  1 
ATOM   8042 N N   . PHE B 1 471 ? -40.720 31.465 10.110  1.00 18.01 ? 471 PHE B N   1 
ATOM   8043 C CA  . PHE B 1 471 ? -41.198 30.599 11.184  1.00 20.97 ? 471 PHE B CA  1 
ATOM   8044 C C   . PHE B 1 471 ? -42.700 30.348 11.076  1.00 24.55 ? 471 PHE B C   1 
ATOM   8045 O O   . PHE B 1 471 ? -43.160 29.213 11.265  1.00 23.86 ? 471 PHE B O   1 
ATOM   8046 C CB  . PHE B 1 471 ? -40.839 31.218 12.532  1.00 18.43 ? 471 PHE B CB  1 
ATOM   8047 C CG  . PHE B 1 471 ? -39.339 31.332 12.756  1.00 21.55 ? 471 PHE B CG  1 
ATOM   8048 C CD1 . PHE B 1 471 ? -38.513 30.249 12.509  1.00 24.06 ? 471 PHE B CD1 1 
ATOM   8049 C CD2 . PHE B 1 471 ? -38.772 32.514 13.196  1.00 21.56 ? 471 PHE B CD2 1 
ATOM   8050 C CE1 . PHE B 1 471 ? -37.125 30.340 12.724  1.00 21.36 ? 471 PHE B CE1 1 
ATOM   8051 C CE2 . PHE B 1 471 ? -37.386 32.619 13.397  1.00 19.14 ? 471 PHE B CE2 1 
ATOM   8052 C CZ  . PHE B 1 471 ? -36.569 31.525 13.156  1.00 20.57 ? 471 PHE B CZ  1 
ATOM   8053 N N   . VAL B 1 472 ? -43.474 31.389 10.754  1.00 22.12 ? 472 VAL B N   1 
ATOM   8054 C CA  . VAL B 1 472 ? -44.910 31.222 10.566  1.00 24.41 ? 472 VAL B CA  1 
ATOM   8055 C C   . VAL B 1 472 ? -45.187 30.243 9.427   1.00 29.86 ? 472 VAL B C   1 
ATOM   8056 O O   . VAL B 1 472 ? -46.062 29.374 9.530   1.00 27.19 ? 472 VAL B O   1 
ATOM   8057 C CB  . VAL B 1 472 ? -45.574 32.591 10.325  1.00 24.54 ? 472 VAL B CB  1 
ATOM   8058 C CG1 . VAL B 1 472 ? -46.973 32.417 9.706   1.00 34.11 ? 472 VAL B CG1 1 
ATOM   8059 C CG2 . VAL B 1 472 ? -45.640 33.387 11.641  1.00 21.85 ? 472 VAL B CG2 1 
ATOM   8060 N N   . ARG B 1 473 ? -44.425 30.342 8.337   1.00 29.57 ? 473 ARG B N   1 
ATOM   8061 C CA  . ARG B 1 473 ? -44.645 29.419 7.231   1.00 23.47 ? 473 ARG B CA  1 
ATOM   8062 C C   . ARG B 1 473 ? -44.291 27.991 7.633   1.00 31.92 ? 473 ARG B C   1 
ATOM   8063 O O   . ARG B 1 473 ? -45.044 27.053 7.348   1.00 31.88 ? 473 ARG B O   1 
ATOM   8064 C CB  . ARG B 1 473 ? -43.841 29.857 6.014   1.00 28.80 ? 473 ARG B CB  1 
ATOM   8065 C CG  . ARG B 1 473 ? -43.902 28.869 4.858   1.00 40.70 ? 473 ARG B CG  1 
ATOM   8066 C CD  . ARG B 1 473 ? -43.504 29.534 3.558   1.00 52.07 ? 473 ARG B CD  1 
ATOM   8067 N NE  . ARG B 1 473 ? -42.793 28.623 2.661   1.00 65.19 ? 473 ARG B NE  1 
ATOM   8068 C CZ  . ARG B 1 473 ? -41.498 28.733 2.371   1.00 65.45 ? 473 ARG B CZ  1 
ATOM   8069 N NH1 . ARG B 1 473 ? -40.780 29.713 2.912   1.00 67.52 ? 473 ARG B NH1 1 
ATOM   8070 N NH2 . ARG B 1 473 ? -40.921 27.866 1.548   1.00 60.06 ? 473 ARG B NH2 1 
ATOM   8071 N N   . ARG B 1 474 ? -43.166 27.813 8.329   1.00 25.45 ? 474 ARG B N   1 
ATOM   8072 C CA  . ARG B 1 474 ? -42.713 26.472 8.683   1.00 28.08 ? 474 ARG B CA  1 
ATOM   8073 C C   . ARG B 1 474 ? -43.641 25.810 9.692   1.00 28.49 ? 474 ARG B C   1 
ATOM   8074 O O   . ARG B 1 474 ? -43.810 24.586 9.669   1.00 31.55 ? 474 ARG B O   1 
ATOM   8075 C CB  . ARG B 1 474 ? -41.287 26.548 9.247   1.00 31.04 ? 474 ARG B CB  1 
ATOM   8076 C CG  . ARG B 1 474 ? -40.658 25.202 9.585   1.00 34.91 ? 474 ARG B CG  1 
ATOM   8077 C CD  . ARG B 1 474 ? -40.087 24.491 8.366   1.00 40.98 ? 474 ARG B CD  1 
ATOM   8078 N NE  . ARG B 1 474 ? -39.302 23.322 8.756   1.00 48.30 ? 474 ARG B NE  1 
ATOM   8079 C CZ  . ARG B 1 474 ? -38.248 22.873 8.078   1.00 61.58 ? 474 ARG B CZ  1 
ATOM   8080 N NH1 . ARG B 1 474 ? -37.854 23.497 6.976   1.00 64.78 ? 474 ARG B NH1 1 
ATOM   8081 N NH2 . ARG B 1 474 ? -37.581 21.803 8.501   1.00 64.66 ? 474 ARG B NH2 1 
ATOM   8082 N N   . ALA B 1 475 ? -44.262 26.605 10.565  1.00 23.97 ? 475 ALA B N   1 
ATOM   8083 C CA  . ALA B 1 475 ? -45.170 26.068 11.569  1.00 26.28 ? 475 ALA B CA  1 
ATOM   8084 C C   . ALA B 1 475 ? -46.397 25.422 10.951  1.00 31.33 ? 475 ALA B C   1 
ATOM   8085 O O   . ALA B 1 475 ? -47.097 24.663 11.632  1.00 33.49 ? 475 ALA B O   1 
ATOM   8086 C CB  . ALA B 1 475 ? -45.612 27.172 12.530  1.00 27.29 ? 475 ALA B CB  1 
ATOM   8087 N N   . GLN B 1 476 ? -46.695 25.715 9.693   1.00 29.73 ? 476 GLN B N   1 
ATOM   8088 C CA  . GLN B 1 476 ? -47.868 25.143 9.054   1.00 31.98 ? 476 GLN B CA  1 
ATOM   8089 C C   . GLN B 1 476 ? -47.522 23.992 8.125   1.00 30.25 ? 476 GLN B C   1 
ATOM   8090 O O   . GLN B 1 476 ? -48.421 23.421 7.499   1.00 36.01 ? 476 GLN B O   1 
ATOM   8091 C CB  . GLN B 1 476 ? -48.632 26.235 8.300   1.00 29.77 ? 476 GLN B CB  1 
ATOM   8092 C CG  . GLN B 1 476 ? -49.172 27.318 9.228   1.00 33.72 ? 476 GLN B CG  1 
ATOM   8093 C CD  . GLN B 1 476 ? -49.492 28.616 8.506   1.00 40.23 ? 476 GLN B CD  1 
ATOM   8094 O OE1 . GLN B 1 476 ? -50.644 28.855 8.136   1.00 43.27 ? 476 GLN B OE1 1 
ATOM   8095 N NE2 . GLN B 1 476 ? -48.484 29.470 8.322   1.00 35.15 ? 476 GLN B NE2 1 
ATOM   8096 N N   . GLU B 1 477 ? -46.250 23.625 8.035   1.00 36.50 ? 477 GLU B N   1 
ATOM   8097 C CA  . GLU B 1 477 ? -45.822 22.618 7.071   1.00 44.34 ? 477 GLU B CA  1 
ATOM   8098 C C   . GLU B 1 477 ? -45.229 21.403 7.771   1.00 53.86 ? 477 GLU B C   1 
ATOM   8099 O O   . GLU B 1 477 ? -45.301 21.289 8.994   1.00 56.12 ? 477 GLU B O   1 
ATOM   8100 C CB  . GLU B 1 477 ? -44.807 23.215 6.089   1.00 50.07 ? 477 GLU B CB  1 
ATOM   8101 C CG  . GLU B 1 477 ? -45.361 24.377 5.260   1.00 64.35 ? 477 GLU B CG  1 
ATOM   8102 C CD  . GLU B 1 477 ? -44.319 24.999 4.341   1.00 66.87 ? 477 GLU B CD  1 
ATOM   8103 O OE1 . GLU B 1 477 ? -44.702 25.804 3.458   1.00 66.27 ? 477 GLU B OE1 1 
ATOM   8104 O OE2 . GLU B 1 477 ? -43.121 24.682 4.505   1.00 63.34 ? 477 GLU B OE2 1 
HETATM 8105 C C1  . GLC C 2 .   ? -0.615  23.730 73.559  1.00 20.17 ? 1   GLC C C1  1 
HETATM 8106 C C2  . GLC C 2 .   ? -1.055  22.374 73.052  1.00 13.11 ? 1   GLC C C2  1 
HETATM 8107 C C3  . GLC C 2 .   ? -2.429  21.999 73.617  1.00 14.40 ? 1   GLC C C3  1 
HETATM 8108 C C4  . GLC C 2 .   ? -2.439  22.111 75.148  1.00 13.93 ? 1   GLC C C4  1 
HETATM 8109 C C5  . GLC C 2 .   ? -1.669  23.359 75.660  1.00 13.74 ? 1   GLC C C5  1 
HETATM 8110 C C6  . GLC C 2 .   ? -1.286  23.292 77.139  1.00 10.73 ? 1   GLC C C6  1 
HETATM 8111 O O1  . GLC C 2 .   ? -1.394  24.779 73.070  1.00 18.54 ? 1   GLC C O1  1 
HETATM 8112 O O2  . GLC C 2 .   ? -0.999  22.357 71.653  1.00 13.23 ? 1   GLC C O2  1 
HETATM 8113 O O3  . GLC C 2 .   ? -2.793  20.699 73.233  1.00 14.14 ? 1   GLC C O3  1 
HETATM 8114 O O4  . GLC C 2 .   ? -3.756  22.184 75.578  1.00 13.59 ? 1   GLC C O4  1 
HETATM 8115 O O5  . GLC C 2 .   ? -0.519  23.657 74.950  1.00 15.95 ? 1   GLC C O5  1 
HETATM 8116 O O6  . GLC C 2 .   ? -0.428  22.231 77.333  1.00 16.26 ? 1   GLC C O6  1 
HETATM 8117 C C1  . GLC C 2 .   ? -4.320  21.017 76.054  1.00 13.23 ? 2   GLC C C1  1 
HETATM 8118 C C2  . GLC C 2 .   ? -5.800  21.106 75.751  1.00 12.49 ? 2   GLC C C2  1 
HETATM 8119 C C3  . GLC C 2 .   ? -6.432  22.238 76.548  1.00 10.34 ? 2   GLC C C3  1 
HETATM 8120 C C4  . GLC C 2 .   ? -6.201  22.006 78.034  1.00 10.11 ? 2   GLC C C4  1 
HETATM 8121 C C5  . GLC C 2 .   ? -4.689  21.848 78.259  1.00 16.07 ? 2   GLC C C5  1 
HETATM 8122 C C6  . GLC C 2 .   ? -4.371  21.423 79.685  1.00 11.52 ? 2   GLC C C6  1 
HETATM 8123 O O2  . GLC C 2 .   ? -5.990  21.341 74.365  1.00 13.39 ? 2   GLC C O2  1 
HETATM 8124 O O3  . GLC C 2 .   ? -7.811  22.275 76.261  1.00 12.68 ? 2   GLC C O3  1 
HETATM 8125 O O4  . GLC C 2 .   ? -6.663  23.157 78.710  1.00 12.12 ? 2   GLC C O4  1 
HETATM 8126 O O5  . GLC C 2 .   ? -4.125  20.842 77.455  1.00 13.97 ? 2   GLC C O5  1 
HETATM 8127 O O6  . GLC C 2 .   ? -2.962  21.313 79.803  1.00 14.10 ? 2   GLC C O6  1 
HETATM 8128 C C1  . GLC C 2 .   ? -7.591  22.860 79.799  1.00 12.72 ? 3   GLC C C1  1 
HETATM 8129 C C2  . GLC C 2 .   ? -8.911  23.550 79.501  1.00 14.23 ? 3   GLC C C2  1 
HETATM 8130 C C3  . GLC C 2 .   ? -8.723  25.066 79.476  1.00 17.13 ? 3   GLC C C3  1 
HETATM 8131 C C4  . GLC C 2 .   ? -8.206  25.515 80.845  1.00 14.17 ? 3   GLC C C4  1 
HETATM 8132 C C5  . GLC C 2 .   ? -6.940  24.735 81.164  1.00 11.91 ? 3   GLC C C5  1 
HETATM 8133 C C6  . GLC C 2 .   ? -6.477  25.011 82.614  1.00 14.68 ? 3   GLC C C6  1 
HETATM 8134 O O2  . GLC C 2 .   ? -9.387  23.066 78.255  1.00 15.90 ? 3   GLC C O2  1 
HETATM 8135 O O3  . GLC C 2 .   ? -9.921  25.754 79.180  1.00 15.99 ? 3   GLC C O3  1 
HETATM 8136 O O4  . GLC C 2 .   ? -7.924  26.901 80.794  1.00 15.17 ? 3   GLC C O4  1 
HETATM 8137 O O5  . GLC C 2 .   ? -7.136  23.333 81.055  1.00 13.31 ? 3   GLC C O5  1 
HETATM 8138 O O6  . GLC C 2 .   ? -7.511  24.573 83.498  1.00 15.87 ? 3   GLC C O6  1 
HETATM 8139 C C1  . GLC C 2 .   ? -8.673  27.607 81.805  1.00 17.50 ? 4   GLC C C1  1 
HETATM 8140 C C2  . GLC C 2 .   ? -9.419  28.759 81.134  1.00 20.79 ? 4   GLC C C2  1 
HETATM 8141 C C3  . GLC C 2 .   ? -8.425  29.747 80.525  1.00 23.28 ? 4   GLC C C3  1 
HETATM 8142 C C4  . GLC C 2 .   ? -7.423  30.210 81.592  1.00 26.41 ? 4   GLC C C4  1 
HETATM 8143 C C5  . GLC C 2 .   ? -6.820  29.001 82.291  1.00 17.43 ? 4   GLC C C5  1 
HETATM 8144 C C6  . GLC C 2 .   ? -5.885  29.437 83.423  1.00 23.61 ? 4   GLC C C6  1 
HETATM 8145 O O2  . GLC C 2 .   ? -10.313 28.242 80.157  1.00 23.14 ? 4   GLC C O2  1 
HETATM 8146 O O3  . GLC C 2 .   ? -9.115  30.840 79.958  1.00 26.24 ? 4   GLC C O3  1 
HETATM 8147 O O4  . GLC C 2 .   ? -6.325  30.891 81.027  1.00 34.41 ? 4   GLC C O4  1 
HETATM 8148 O O5  . GLC C 2 .   ? -7.823  28.140 82.804  1.00 20.89 ? 4   GLC C O5  1 
HETATM 8149 O O6  . GLC C 2 .   ? -6.647  29.885 84.523  1.00 28.55 ? 4   GLC C O6  1 
HETATM 8150 C C1  . GLC C 2 .   ? -6.361  32.298 80.966  1.00 49.35 ? 5   GLC C C1  1 
HETATM 8151 C C2  . GLC C 2 .   ? -5.539  32.863 79.820  1.00 54.25 ? 5   GLC C C2  1 
HETATM 8152 C C3  . GLC C 2 .   ? -4.050  32.754 80.013  1.00 54.95 ? 5   GLC C C3  1 
HETATM 8153 C C4  . GLC C 2 .   ? -3.582  33.229 81.354  1.00 52.37 ? 5   GLC C C4  1 
HETATM 8154 C C5  . GLC C 2 .   ? -4.429  32.485 82.408  1.00 56.94 ? 5   GLC C C5  1 
HETATM 8155 C C6  . GLC C 2 .   ? -4.215  32.816 83.887  1.00 57.99 ? 5   GLC C C6  1 
HETATM 8156 O O2  . GLC C 2 .   ? -5.617  31.926 78.801  1.00 64.42 ? 5   GLC C O2  1 
HETATM 8157 O O3  . GLC C 2 .   ? -3.285  33.259 78.893  1.00 60.72 ? 5   GLC C O3  1 
HETATM 8158 O O4  . GLC C 2 .   ? -2.200  32.907 81.391  1.00 52.52 ? 5   GLC C O4  1 
HETATM 8159 O O5  . GLC C 2 .   ? -5.779  32.780 82.158  1.00 58.12 ? 5   GLC C O5  1 
HETATM 8160 O O6  . GLC C 2 .   ? -2.946  33.397 84.049  1.00 63.09 ? 5   GLC C O6  1 
HETATM 8161 C C1  . GLC D 3 .   ? -2.035  38.050 70.596  1.00 28.77 ? 1   GLC D C1  1 
HETATM 8162 C C2  . GLC D 3 .   ? -0.967  38.267 69.513  1.00 31.24 ? 1   GLC D C2  1 
HETATM 8163 C C3  . GLC D 3 .   ? -0.219  37.000 69.111  1.00 32.96 ? 1   GLC D C3  1 
HETATM 8164 C C4  . GLC D 3 .   ? 0.164   36.189 70.317  1.00 28.29 ? 1   GLC D C4  1 
HETATM 8165 C C5  . GLC D 3 .   ? -1.071  35.900 71.121  1.00 25.44 ? 1   GLC D C5  1 
HETATM 8166 C C6  . GLC D 3 .   ? -0.715  35.037 72.315  1.00 26.09 ? 1   GLC D C6  1 
HETATM 8167 O O1  . GLC D 3 .   ? -3.224  37.562 70.006  1.00 33.46 ? 1   GLC D O1  1 
HETATM 8168 O O2  . GLC D 3 .   ? -1.576  38.827 68.346  1.00 25.53 ? 1   GLC D O2  1 
HETATM 8169 O O3  . GLC D 3 .   ? 0.983   37.342 68.431  1.00 29.26 ? 1   GLC D O3  1 
HETATM 8170 O O4  . GLC D 3 .   ? 0.706   34.976 69.834  1.00 28.10 ? 1   GLC D O4  1 
HETATM 8171 O O5  . GLC D 3 .   ? -1.625  37.120 71.592  1.00 27.02 ? 1   GLC D O5  1 
HETATM 8172 O O6  . GLC D 3 .   ? -0.158  35.884 73.306  1.00 28.66 ? 1   GLC D O6  1 
HETATM 8173 C C1  . GLC D 3 .   ? 2.111   34.750 70.121  1.00 22.08 ? 2   GLC D C1  1 
HETATM 8174 C C2  . GLC D 3 .   ? 2.745   34.166 68.882  1.00 27.54 ? 2   GLC D C2  1 
HETATM 8175 C C3  . GLC D 3 .   ? 1.980   32.881 68.555  1.00 23.20 ? 2   GLC D C3  1 
HETATM 8176 C C4  . GLC D 3 .   ? 2.067   31.890 69.709  1.00 23.05 ? 2   GLC D C4  1 
HETATM 8177 C C5  . GLC D 3 .   ? 1.672   32.586 71.015  1.00 22.79 ? 2   GLC D C5  1 
HETATM 8178 C C6  . GLC D 3 .   ? 2.041   31.718 72.210  1.00 24.09 ? 2   GLC D C6  1 
HETATM 8179 O O2  . GLC D 3 .   ? 2.565   35.085 67.832  1.00 29.63 ? 2   GLC D O2  1 
HETATM 8180 O O3  . GLC D 3 .   ? 2.399   32.299 67.335  1.00 24.03 ? 2   GLC D O3  1 
HETATM 8181 O O4  . GLC D 3 .   ? 1.096   30.897 69.463  1.00 27.01 ? 2   GLC D O4  1 
HETATM 8182 O O5  . GLC D 3 .   ? 2.295   33.851 71.187  1.00 27.34 ? 2   GLC D O5  1 
HETATM 8183 O O6  . GLC D 3 .   ? 1.357   32.177 73.357  1.00 26.34 ? 2   GLC D O6  1 
HETATM 8184 C C1  . GLC D 3 .   ? 1.623   29.564 69.333  1.00 26.79 ? 3   GLC D C1  1 
HETATM 8185 C C2  . GLC D 3 .   ? 0.725   28.860 68.334  1.00 24.42 ? 3   GLC D C2  1 
HETATM 8186 C C3  . GLC D 3 .   ? -0.704  28.811 68.879  1.00 20.49 ? 3   GLC D C3  1 
HETATM 8187 C C4  . GLC D 3 .   ? -0.761  28.185 70.280  1.00 26.77 ? 3   GLC D C4  1 
HETATM 8188 C C5  . GLC D 3 .   ? 0.321   28.793 71.176  1.00 23.16 ? 3   GLC D C5  1 
HETATM 8189 C C6  . GLC D 3 .   ? 0.457   28.085 72.530  1.00 21.96 ? 3   GLC D C6  1 
HETATM 8190 O O2  . GLC D 3 .   ? 0.784   29.554 67.092  1.00 23.55 ? 3   GLC D O2  1 
HETATM 8191 O O3  . GLC D 3 .   ? -1.569  28.101 68.001  1.00 18.40 ? 3   GLC D O3  1 
HETATM 8192 O O4  . GLC D 3 .   ? -2.036  28.532 70.787  1.00 20.25 ? 3   GLC D O4  1 
HETATM 8193 O O5  . GLC D 3 .   ? 1.603   28.836 70.552  1.00 28.71 ? 3   GLC D O5  1 
HETATM 8194 O O6  . GLC D 3 .   ? 0.689   26.705 72.317  1.00 24.48 ? 3   GLC D O6  1 
HETATM 8195 C C1  . GLC D 3 .   ? -2.764  27.493 71.465  1.00 19.19 ? 4   GLC D C1  1 
HETATM 8196 C C2  . GLC D 3 .   ? -4.138  27.350 70.817  1.00 14.05 ? 4   GLC D C2  1 
HETATM 8197 C C3  . GLC D 3 .   ? -4.976  28.623 71.005  1.00 20.86 ? 4   GLC D C3  1 
HETATM 8198 C C4  . GLC D 3 .   ? -4.999  29.036 72.479  1.00 20.05 ? 4   GLC D C4  1 
HETATM 8199 C C5  . GLC D 3 .   ? -3.576  29.064 73.054  1.00 19.35 ? 4   GLC D C5  1 
HETATM 8200 C C6  . GLC D 3 .   ? -3.603  29.314 74.561  1.00 18.36 ? 4   GLC D C6  1 
HETATM 8201 O O2  . GLC D 3 .   ? -3.967  27.054 69.435  1.00 15.56 ? 4   GLC D O2  1 
HETATM 8202 O O3  . GLC D 3 .   ? -6.299  28.450 70.536  1.00 19.41 ? 4   GLC D O3  1 
HETATM 8203 O O4  . GLC D 3 .   ? -5.545  30.334 72.583  1.00 18.89 ? 4   GLC D O4  1 
HETATM 8204 O O5  . GLC D 3 .   ? -2.916  27.828 72.832  1.00 19.40 ? 4   GLC D O5  1 
HETATM 8205 O O6  . GLC D 3 .   ? -2.284  29.338 75.096  1.00 21.78 ? 4   GLC D O6  1 
HETATM 8206 C C1  . GLC D 3 .   ? -6.807  30.369 73.255  1.00 16.60 ? 5   GLC D C1  1 
HETATM 8207 C C2  . GLC D 3 .   ? -7.767  31.190 72.398  1.00 17.32 ? 5   GLC D C2  1 
HETATM 8208 C C3  . GLC D 3 .   ? -7.347  32.655 72.353  1.00 17.06 ? 5   GLC D C3  1 
HETATM 8209 C C4  . GLC D 3 .   ? -7.185  33.228 73.756  1.00 21.64 ? 5   GLC D C4  1 
HETATM 8210 C C5  . GLC D 3 .   ? -6.280  32.310 74.583  1.00 19.66 ? 5   GLC D C5  1 
HETATM 8211 C C6  . GLC D 3 .   ? -6.280  32.728 76.048  1.00 19.39 ? 5   GLC D C6  1 
HETATM 8212 O O2  . GLC D 3 .   ? -7.738  30.686 71.067  1.00 17.27 ? 5   GLC D O2  1 
HETATM 8213 O O3  . GLC D 3 .   ? -8.302  33.435 71.668  1.00 19.33 ? 5   GLC D O3  1 
HETATM 8214 O O4  . GLC D 3 .   ? -6.555  34.495 73.617  1.00 21.48 ? 5   GLC D O4  1 
HETATM 8215 O O5  . GLC D 3 .   ? -6.652  30.929 74.564  1.00 20.48 ? 5   GLC D O5  1 
HETATM 8216 O O6  . GLC D 3 .   ? -4.971  32.442 76.504  1.00 27.89 ? 5   GLC D O6  1 
HETATM 8217 C C1  . GLC D 3 .   ? -7.465  35.611 73.711  1.00 21.40 ? 6   GLC D C1  1 
HETATM 8218 C C2  . GLC D 3 .   ? -7.156  36.570 72.563  1.00 24.15 ? 6   GLC D C2  1 
HETATM 8219 C C3  . GLC D 3 .   ? -5.781  37.199 72.719  1.00 20.20 ? 6   GLC D C3  1 
HETATM 8220 C C4  . GLC D 3 .   ? -5.615  37.837 74.087  1.00 24.96 ? 6   GLC D C4  1 
HETATM 8221 C C5  . GLC D 3 .   ? -5.988  36.794 75.147  1.00 24.91 ? 6   GLC D C5  1 
HETATM 8222 C C6  . GLC D 3 .   ? -5.869  37.345 76.574  1.00 35.04 ? 6   GLC D C6  1 
HETATM 8223 O O2  . GLC D 3 .   ? -7.137  35.888 71.332  1.00 23.80 ? 6   GLC D O2  1 
HETATM 8224 O O3  . GLC D 3 .   ? -5.596  38.154 71.680  1.00 22.55 ? 6   GLC D O3  1 
HETATM 8225 O O4  . GLC D 3 .   ? -4.275  38.276 74.216  1.00 28.11 ? 6   GLC D O4  1 
HETATM 8226 O O5  . GLC D 3 .   ? -7.309  36.306 74.933  1.00 26.67 ? 6   GLC D O5  1 
HETATM 8227 O O6  . GLC D 3 .   ? -4.910  36.570 77.268  1.00 50.10 ? 6   GLC D O6  1 
HETATM 8228 C C1  . GLC E 2 .   ? -35.827 43.667 25.578  1.00 23.64 ? 1   GLC E C1  1 
HETATM 8229 C C2  . GLC E 2 .   ? -35.229 42.336 26.039  1.00 15.41 ? 1   GLC E C2  1 
HETATM 8230 C C3  . GLC E 2 .   ? -34.036 41.949 25.195  1.00 11.89 ? 1   GLC E C3  1 
HETATM 8231 C C4  . GLC E 2 .   ? -34.308 42.050 23.693  1.00 12.72 ? 1   GLC E C4  1 
HETATM 8232 C C5  . GLC E 2 .   ? -35.072 43.341 23.367  1.00 14.13 ? 1   GLC E C5  1 
HETATM 8233 C C6  . GLC E 2 .   ? -35.642 43.369 21.953  1.00 14.36 ? 1   GLC E C6  1 
HETATM 8234 O O1  . GLC E 2 .   ? -35.020 44.727 25.943  1.00 22.24 ? 1   GLC E O1  1 
HETATM 8235 O O2  . GLC E 2 .   ? -35.070 42.270 27.439  1.00 19.04 ? 1   GLC E O2  1 
HETATM 8236 O O3  . GLC E 2 .   ? -33.538 40.717 25.544  1.00 15.88 ? 1   GLC E O3  1 
HETATM 8237 O O4  . GLC E 2 .   ? -33.091 42.152 23.011  1.00 13.20 ? 1   GLC E O4  1 
HETATM 8238 O O5  . GLC E 2 .   ? -36.114 43.613 24.228  1.00 20.53 ? 1   GLC E O5  1 
HETATM 8239 O O6  . GLC E 2 .   ? -36.609 42.401 21.787  1.00 18.48 ? 1   GLC E O6  1 
HETATM 8240 C C1  . GLC E 2 .   ? -32.592 40.973 22.473  1.00 14.74 ? 2   GLC E C1  1 
HETATM 8241 C C2  . GLC E 2 .   ? -31.063 40.988 22.520  1.00 14.15 ? 2   GLC E C2  1 
HETATM 8242 C C3  . GLC E 2 .   ? -30.463 42.114 21.684  1.00 12.85 ? 2   GLC E C3  1 
HETATM 8243 C C4  . GLC E 2 .   ? -30.973 41.944 20.261  1.00 13.97 ? 2   GLC E C4  1 
HETATM 8244 C C5  . GLC E 2 .   ? -32.499 41.854 20.266  1.00 14.17 ? 2   GLC E C5  1 
HETATM 8245 C C6  . GLC E 2 .   ? -33.026 41.569 18.863  1.00 15.70 ? 2   GLC E C6  1 
HETATM 8246 O O2  . GLC E 2 .   ? -30.611 41.138 23.855  1.00 15.48 ? 2   GLC E O2  1 
HETATM 8247 O O3  . GLC E 2 .   ? -29.047 42.056 21.727  1.00 15.76 ? 2   GLC E O3  1 
HETATM 8248 O O4  . GLC E 2 .   ? -30.563 43.090 19.535  1.00 15.53 ? 2   GLC E O4  1 
HETATM 8249 O O5  . GLC E 2 .   ? -33.012 40.828 21.126  1.00 15.64 ? 2   GLC E O5  1 
HETATM 8250 O O6  . GLC E 2 .   ? -34.398 41.318 18.997  1.00 16.19 ? 2   GLC E O6  1 
HETATM 8251 C C1  . GLC E 2 .   ? -29.827 42.775 18.336  1.00 11.98 ? 3   GLC E C1  1 
HETATM 8252 C C2  . GLC E 2 .   ? -28.466 43.443 18.425  1.00 16.16 ? 3   GLC E C2  1 
HETATM 8253 C C3  . GLC E 2 .   ? -28.635 44.955 18.483  1.00 20.09 ? 3   GLC E C3  1 
HETATM 8254 C C4  . GLC E 2 .   ? -29.366 45.397 17.214  1.00 14.23 ? 3   GLC E C4  1 
HETATM 8255 C C5  . GLC E 2 .   ? -30.696 44.648 17.125  1.00 15.69 ? 3   GLC E C5  1 
HETATM 8256 C C6  . GLC E 2 .   ? -31.445 44.957 15.817  1.00 17.48 ? 3   GLC E C6  1 
HETATM 8257 O O2  . GLC E 2 .   ? -27.777 42.934 19.549  1.00 16.49 ? 3   GLC E O2  1 
HETATM 8258 O O3  . GLC E 2 .   ? -27.377 45.595 18.598  1.00 18.70 ? 3   GLC E O3  1 
HETATM 8259 O O4  . GLC E 2 .   ? -29.559 46.796 17.303  1.00 17.21 ? 3   GLC E O4  1 
HETATM 8260 O O5  . GLC E 2 .   ? -30.496 43.254 17.173  1.00 17.39 ? 3   GLC E O5  1 
HETATM 8261 O O6  . GLC E 2 .   ? -30.650 44.567 14.716  1.00 17.33 ? 3   GLC E O6  1 
HETATM 8262 C C1  . GLC E 2 .   ? -28.952 47.450 16.166  1.00 23.28 ? 4   GLC E C1  1 
HETATM 8263 C C2  . GLC E 2 .   ? -28.067 48.572 16.657  1.00 23.35 ? 4   GLC E C2  1 
HETATM 8264 C C3  . GLC E 2 .   ? -28.899 49.558 17.457  1.00 25.24 ? 4   GLC E C3  1 
HETATM 8265 C C4  . GLC E 2 .   ? -30.086 50.067 16.627  1.00 28.29 ? 4   GLC E C4  1 
HETATM 8266 C C5  . GLC E 2 .   ? -30.832 48.863 16.047  1.00 24.68 ? 4   GLC E C5  1 
HETATM 8267 C C6  . GLC E 2 .   ? -31.979 49.221 15.100  1.00 30.73 ? 4   GLC E C6  1 
HETATM 8268 O O2  . GLC E 2 .   ? -27.057 48.027 17.461  1.00 25.15 ? 4   GLC E O2  1 
HETATM 8269 O O3  . GLC E 2 .   ? -28.037 50.599 17.823  1.00 31.06 ? 4   GLC E O3  1 
HETATM 8270 O O4  . GLC E 2 .   ? -30.937 50.886 17.414  1.00 37.36 ? 4   GLC E O4  1 
HETATM 8271 O O5  . GLC E 2 .   ? -29.930 48.028 15.335  1.00 24.09 ? 4   GLC E O5  1 
HETATM 8272 O O6  . GLC E 2 .   ? -31.499 50.097 14.101  1.00 36.20 ? 4   GLC E O6  1 
HETATM 8273 C C1  . GLC E 2 .   ? -31.272 52.113 16.703  1.00 57.95 ? 5   GLC E C1  1 
HETATM 8274 C C2  . GLC E 2 .   ? -30.750 53.270 17.521  1.00 60.45 ? 5   GLC E C2  1 
HETATM 8275 C C3  . GLC E 2 .   ? -31.396 53.197 18.892  1.00 61.29 ? 5   GLC E C3  1 
HETATM 8276 C C4  . GLC E 2 .   ? -32.910 53.268 18.782  1.00 60.73 ? 5   GLC E C4  1 
HETATM 8277 C C5  . GLC E 2 .   ? -33.450 52.315 17.718  1.00 61.44 ? 5   GLC E C5  1 
HETATM 8278 C C6  . GLC E 2 .   ? -34.905 52.677 17.412  1.00 61.57 ? 5   GLC E C6  1 
HETATM 8279 O O2  . GLC E 2 .   ? -29.356 53.135 17.633  1.00 69.31 ? 5   GLC E O2  1 
HETATM 8280 O O3  . GLC E 2 .   ? -30.951 54.263 19.697  1.00 67.17 ? 5   GLC E O3  1 
HETATM 8281 O O4  . GLC E 2 .   ? -33.447 52.936 20.044  1.00 53.64 ? 5   GLC E O4  1 
HETATM 8282 O O5  . GLC E 2 .   ? -32.670 52.328 16.527  1.00 60.13 ? 5   GLC E O5  1 
HETATM 8283 O O6  . GLC E 2 .   ? -35.339 52.015 16.243  1.00 68.60 ? 5   GLC E O6  1 
HETATM 8284 C C1  . GLC F 3 .   ? -33.762 57.676 28.122  1.00 39.02 ? 1   GLC F C1  1 
HETATM 8285 C C2  . GLC F 3 .   ? -34.797 58.060 29.169  1.00 35.13 ? 1   GLC F C2  1 
HETATM 8286 C C3  . GLC F 3 .   ? -35.486 56.839 29.750  1.00 37.84 ? 1   GLC F C3  1 
HETATM 8287 C C4  . GLC F 3 .   ? -36.021 55.957 28.643  1.00 35.32 ? 1   GLC F C4  1 
HETATM 8288 C C5  . GLC F 3 .   ? -34.897 55.628 27.680  1.00 39.59 ? 1   GLC F C5  1 
HETATM 8289 C C6  . GLC F 3 .   ? -35.413 54.799 26.520  1.00 44.31 ? 1   GLC F C6  1 
HETATM 8290 O O1  . GLC F 3 .   ? -32.727 56.952 28.753  1.00 39.74 ? 1   GLC F O1  1 
HETATM 8291 O O2  . GLC F 3 .   ? -34.166 58.748 30.241  1.00 37.47 ? 1   GLC F O2  1 
HETATM 8292 O O3  . GLC F 3 .   ? -36.552 57.255 30.604  1.00 40.31 ? 1   GLC F O3  1 
HETATM 8293 O O4  . GLC F 3 .   ? -36.479 54.776 29.267  1.00 31.60 ? 1   GLC F O4  1 
HETATM 8294 O O5  . GLC F 3 .   ? -34.342 56.824 27.148  1.00 43.24 ? 1   GLC F O5  1 
HETATM 8295 O O6  . GLC F 3 .   ? -36.313 55.617 25.773  1.00 46.92 ? 1   GLC F O6  1 
HETATM 8296 C C1  . GLC F 3 .   ? -37.912 54.524 29.265  1.00 36.87 ? 2   GLC F C1  1 
HETATM 8297 C C2  . GLC F 3 .   ? -38.322 53.946 30.597  1.00 32.59 ? 2   GLC F C2  1 
HETATM 8298 C C3  . GLC F 3 .   ? -37.467 52.698 30.811  1.00 30.15 ? 2   GLC F C3  1 
HETATM 8299 C C4  . GLC F 3 .   ? -37.656 51.691 29.682  1.00 29.99 ? 2   GLC F C4  1 
HETATM 8300 C C5  . GLC F 3 .   ? -37.578 52.387 28.320  1.00 35.37 ? 2   GLC F C5  1 
HETATM 8301 C C6  . GLC F 3 .   ? -38.105 51.472 27.224  1.00 40.16 ? 2   GLC F C6  1 
HETATM 8302 O O2  . GLC F 3 .   ? -38.090 54.893 31.616  1.00 36.28 ? 2   GLC F O2  1 
HETATM 8303 O O3  . GLC F 3 .   ? -37.734 52.082 32.049  1.00 34.51 ? 2   GLC F O3  1 
HETATM 8304 O O4  . GLC F 3 .   ? -36.602 50.754 29.753  1.00 29.23 ? 2   GLC F O4  1 
HETATM 8305 O O5  . GLC F 3 .   ? -38.306 53.607 28.273  1.00 42.66 ? 2   GLC F O5  1 
HETATM 8306 O O6  . GLC F 3 .   ? -37.790 52.041 25.974  1.00 34.28 ? 2   GLC F O6  1 
HETATM 8307 C C1  . GLC F 3 .   ? -37.075 49.421 30.020  1.00 29.64 ? 3   GLC F C1  1 
HETATM 8308 C C2  . GLC F 3 .   ? -36.014 48.704 30.836  1.00 25.79 ? 3   GLC F C2  1 
HETATM 8309 C C3  . GLC F 3 .   ? -34.723 48.652 30.047  1.00 21.57 ? 3   GLC F C3  1 
HETATM 8310 C C4  . GLC F 3 .   ? -34.911 48.058 28.655  1.00 23.59 ? 3   GLC F C4  1 
HETATM 8311 C C5  . GLC F 3 .   ? -36.138 48.688 27.976  1.00 25.45 ? 3   GLC F C5  1 
HETATM 8312 C C6  . GLC F 3 .   ? -36.535 48.034 26.650  1.00 22.86 ? 3   GLC F C6  1 
HETATM 8313 O O2  . GLC F 3 .   ? -35.750 49.426 32.018  1.00 31.28 ? 3   GLC F O2  1 
HETATM 8314 O O3  . GLC F 3 .   ? -33.773 47.908 30.783  1.00 24.52 ? 3   GLC F O3  1 
HETATM 8315 O O4  . GLC F 3 .   ? -33.727 48.405 27.948  1.00 25.17 ? 3   GLC F O4  1 
HETATM 8316 O O5  . GLC F 3 .   ? -37.276 48.699 28.825  1.00 32.03 ? 3   GLC F O5  1 
HETATM 8317 O O6  . GLC F 3 .   ? -36.570 46.635 26.816  1.00 23.53 ? 3   GLC F O6  1 
HETATM 8318 C C1  . GLC F 3 .   ? -33.105 47.335 27.227  1.00 23.54 ? 4   GLC F C1  1 
HETATM 8319 C C2  . GLC F 3 .   ? -31.666 47.197 27.734  1.00 29.41 ? 4   GLC F C2  1 
HETATM 8320 C C3  . GLC F 3 .   ? -30.860 48.443 27.388  1.00 21.17 ? 4   GLC F C3  1 
HETATM 8321 C C4  . GLC F 3 .   ? -31.081 48.847 25.924  1.00 20.47 ? 4   GLC F C4  1 
HETATM 8322 C C5  . GLC F 3 .   ? -32.566 48.887 25.556  1.00 26.62 ? 4   GLC F C5  1 
HETATM 8323 C C6  . GLC F 3 .   ? -32.781 49.212 24.076  1.00 29.16 ? 4   GLC F C6  1 
HETATM 8324 O O2  . GLC F 3 .   ? -31.651 46.941 29.145  1.00 25.76 ? 4   GLC F O2  1 
HETATM 8325 O O3  . GLC F 3 .   ? -29.482 48.218 27.607  1.00 22.08 ? 4   GLC F O3  1 
HETATM 8326 O O4  . GLC F 3 .   ? -30.564 50.139 25.732  1.00 22.98 ? 4   GLC F O4  1 
HETATM 8327 O O5  . GLC F 3 .   ? -33.143 47.631 25.834  1.00 23.25 ? 4   GLC F O5  1 
HETATM 8328 O O6  . GLC F 3 .   ? -34.173 49.154 23.807  1.00 26.15 ? 4   GLC F O6  1 
HETATM 8329 C C1  . GLC F 3 .   ? -29.417 50.126 24.881  1.00 24.80 ? 5   GLC F C1  1 
HETATM 8330 C C2  . GLC F 3 .   ? -28.328 50.943 25.562  1.00 22.63 ? 5   GLC F C2  1 
HETATM 8331 C C3  . GLC F 3 .   ? -28.733 52.418 25.645  1.00 29.44 ? 5   GLC F C3  1 
HETATM 8332 C C4  . GLC F 3 .   ? -29.216 52.969 24.303  1.00 29.62 ? 5   GLC F C4  1 
HETATM 8333 C C5  . GLC F 3 .   ? -30.261 52.014 23.726  1.00 25.45 ? 5   GLC F C5  1 
HETATM 8334 C C6  . GLC F 3 .   ? -30.699 52.429 22.326  1.00 27.37 ? 5   GLC F C6  1 
HETATM 8335 O O2  . GLC F 3 .   ? -28.155 50.436 26.866  1.00 21.19 ? 5   GLC F O2  1 
HETATM 8336 O O3  . GLC F 3 .   ? -27.656 53.201 26.125  1.00 20.72 ? 5   GLC F O3  1 
HETATM 8337 O O4  . GLC F 3 .   ? -29.799 54.246 24.482  1.00 26.03 ? 5   GLC F O4  1 
HETATM 8338 O O5  . GLC F 3 .   ? -29.738 50.706 23.628  1.00 26.77 ? 5   GLC F O5  1 
HETATM 8339 O O6  . GLC F 3 .   ? -29.595 52.273 21.461  1.00 40.29 ? 5   GLC F O6  1 
HETATM 8340 C C1  . GLC F 3 .   ? -28.908 55.364 24.266  1.00 32.78 ? 6   GLC F C1  1 
HETATM 8341 C C2  . GLC F 3 .   ? -29.030 56.342 25.436  1.00 35.65 ? 6   GLC F C2  1 
HETATM 8342 C C3  . GLC F 3 .   ? -30.453 56.879 25.541  1.00 32.79 ? 6   GLC F C3  1 
HETATM 8343 C C4  . GLC F 3 .   ? -30.889 57.492 24.210  1.00 40.70 ? 6   GLC F C4  1 
HETATM 8344 C C5  . GLC F 3 .   ? -30.566 56.543 23.059  1.00 40.58 ? 6   GLC F C5  1 
HETATM 8345 C C6  . GLC F 3 .   ? -30.802 57.238 21.728  1.00 46.37 ? 6   GLC F C6  1 
HETATM 8346 O O2  . GLC F 3 .   ? -28.674 55.680 26.622  1.00 34.81 ? 6   GLC F O2  1 
HETATM 8347 O O3  . GLC F 3 .   ? -30.546 57.849 26.560  1.00 35.92 ? 6   GLC F O3  1 
HETATM 8348 O O4  . GLC F 3 .   ? -32.280 57.759 24.221  1.00 39.03 ? 6   GLC F O4  1 
HETATM 8349 O O5  . GLC F 3 .   ? -29.228 56.081 23.090  1.00 36.06 ? 6   GLC F O5  1 
HETATM 8350 O O6  . GLC F 3 .   ? -30.124 56.492 20.741  1.00 56.06 ? 6   GLC F O6  1 
HETATM 8351 O O   . HOH G 4 .   ? 19.752  12.365 60.835  1.00 37.46 ? 501 HOH A O   1 
HETATM 8352 O O   . HOH G 4 .   ? -5.180  26.479 36.627  1.00 61.67 ? 502 HOH A O   1 
HETATM 8353 O O   . HOH G 4 .   ? -21.352 38.072 59.988  1.00 44.06 ? 503 HOH A O   1 
HETATM 8354 O O   . HOH G 4 .   ? -25.658 24.907 62.499  1.00 36.08 ? 504 HOH A O   1 
HETATM 8355 O O   . HOH G 4 .   ? -12.035 3.575  85.090  1.00 51.04 ? 505 HOH A O   1 
HETATM 8356 O O   . HOH G 4 .   ? -27.177 37.796 76.809  1.00 56.21 ? 506 HOH A O   1 
HETATM 8357 O O   . HOH G 4 .   ? 6.879   31.234 65.690  1.00 49.43 ? 507 HOH A O   1 
HETATM 8358 O O   . HOH G 4 .   ? 4.942   36.288 66.898  1.00 36.07 ? 508 HOH A O   1 
HETATM 8359 O O   . HOH G 4 .   ? 16.943  30.238 83.665  1.00 28.65 ? 509 HOH A O   1 
HETATM 8360 O O   . HOH G 4 .   ? -30.768 28.350 70.289  1.00 42.28 ? 510 HOH A O   1 
HETATM 8361 O O   . HOH G 4 .   ? -3.623  40.539 56.099  1.00 41.53 ? 511 HOH A O   1 
HETATM 8362 O O   . HOH G 4 .   ? -1.944  34.559 39.874  1.00 48.04 ? 512 HOH A O   1 
HETATM 8363 O O   . HOH G 4 .   ? -16.381 13.748 71.724  1.00 30.34 ? 513 HOH A O   1 
HETATM 8364 O O   . HOH G 4 .   ? 5.250   33.566 55.667  1.00 39.86 ? 514 HOH A O   1 
HETATM 8365 O O   . HOH G 4 .   ? -36.952 13.548 79.690  1.00 51.98 ? 515 HOH A O   1 
HETATM 8366 O O   . HOH G 4 .   ? 9.932   3.649  80.988  1.00 39.11 ? 516 HOH A O   1 
HETATM 8367 O O   . HOH G 4 .   ? 1.143   40.524 53.642  1.00 55.46 ? 517 HOH A O   1 
HETATM 8368 O O   . HOH G 4 .   ? -29.363 15.319 100.486 1.00 37.61 ? 518 HOH A O   1 
HETATM 8369 O O   . HOH G 4 .   ? -28.667 11.374 82.108  1.00 34.56 ? 519 HOH A O   1 
HETATM 8370 O O   . HOH G 4 .   ? 18.085  24.355 88.768  1.00 46.40 ? 520 HOH A O   1 
HETATM 8371 O O   . HOH G 4 .   ? 23.069  28.705 80.953  1.00 36.78 ? 521 HOH A O   1 
HETATM 8372 O O   . HOH G 4 .   ? -12.555 7.013  86.265  1.00 19.17 ? 522 HOH A O   1 
HETATM 8373 O O   . HOH G 4 .   ? -3.215  6.745  79.162  1.00 30.68 ? 523 HOH A O   1 
HETATM 8374 O O   . HOH G 4 .   ? 22.944  14.533 72.227  1.00 39.17 ? 524 HOH A O   1 
HETATM 8375 O O   . HOH G 4 .   ? 25.253  14.321 88.088  1.00 36.93 ? 525 HOH A O   1 
HETATM 8376 O O   . HOH G 4 .   ? -10.354 23.220 43.727  1.00 47.19 ? 526 HOH A O   1 
HETATM 8377 O O   . HOH G 4 .   ? -17.857 2.346  64.874  1.00 29.69 ? 527 HOH A O   1 
HETATM 8378 O O   . HOH G 4 .   ? 0.255   30.502 42.932  1.00 43.99 ? 528 HOH A O   1 
HETATM 8379 O O   . HOH G 4 .   ? 7.932   17.021 78.304  1.00 32.54 ? 529 HOH A O   1 
HETATM 8380 O O   . HOH G 4 .   ? -10.310 25.567 76.492  1.00 19.49 ? 530 HOH A O   1 
HETATM 8381 O O   . HOH G 4 .   ? 16.696  25.658 71.587  1.00 23.05 ? 531 HOH A O   1 
HETATM 8382 O O   . HOH G 4 .   ? -18.115 16.192 92.927  1.00 27.04 ? 532 HOH A O   1 
HETATM 8383 O O   . HOH G 4 .   ? 11.023  29.490 82.141  1.00 30.92 ? 533 HOH A O   1 
HETATM 8384 O O   . HOH G 4 .   ? 8.717   19.439 42.476  1.00 34.66 ? 534 HOH A O   1 
HETATM 8385 O O   . HOH G 4 .   ? 2.066   27.763 88.333  1.00 34.05 ? 535 HOH A O   1 
HETATM 8386 O O   . HOH G 4 .   ? -37.331 23.080 67.832  1.00 43.28 ? 536 HOH A O   1 
HETATM 8387 O O   . HOH G 4 .   ? 2.738   -3.290 64.812  1.00 35.09 ? 537 HOH A O   1 
HETATM 8388 O O   . HOH G 4 .   ? 1.241   35.685 64.219  1.00 32.11 ? 538 HOH A O   1 
HETATM 8389 O O   . HOH G 4 .   ? -37.782 20.002 72.281  1.00 27.79 ? 539 HOH A O   1 
HETATM 8390 O O   . HOH G 4 .   ? 2.294   33.525 84.446  1.00 41.89 ? 540 HOH A O   1 
HETATM 8391 O O   . HOH G 4 .   ? -31.564 33.056 96.085  1.00 37.62 ? 541 HOH A O   1 
HETATM 8392 O O   . HOH G 4 .   ? -13.011 41.594 56.236  1.00 32.50 ? 542 HOH A O   1 
HETATM 8393 O O   . HOH G 4 .   ? 2.259   21.930 77.099  1.00 18.71 ? 543 HOH A O   1 
HETATM 8394 O O   . HOH G 4 .   ? 20.435  11.260 54.658  1.00 47.95 ? 544 HOH A O   1 
HETATM 8395 O O   . HOH G 4 .   ? 15.612  7.259  71.506  1.00 31.87 ? 545 HOH A O   1 
HETATM 8396 O O   . HOH G 4 .   ? -13.790 16.583 87.149  1.00 17.62 ? 546 HOH A O   1 
HETATM 8397 O O   . HOH G 4 .   ? -21.742 22.581 51.776  1.00 33.02 ? 547 HOH A O   1 
HETATM 8398 O O   . HOH G 4 .   ? -23.973 14.246 63.162  1.00 37.92 ? 548 HOH A O   1 
HETATM 8399 O O   . HOH G 4 .   ? -34.089 14.820 91.525  1.00 42.02 ? 549 HOH A O   1 
HETATM 8400 O O   . HOH G 4 .   ? 16.124  4.519  55.276  1.00 32.28 ? 550 HOH A O   1 
HETATM 8401 O O   . HOH G 4 .   ? 1.323   34.089 54.890  1.00 44.75 ? 551 HOH A O   1 
HETATM 8402 O O   . HOH G 4 .   ? 6.588   24.494 54.324  1.00 16.95 ? 552 HOH A O   1 
HETATM 8403 O O   . HOH G 4 .   ? 10.764  31.675 89.293  1.00 51.88 ? 553 HOH A O   1 
HETATM 8404 O O   . HOH G 4 .   ? -7.898  9.783  54.447  1.00 22.26 ? 554 HOH A O   1 
HETATM 8405 O O   . HOH G 4 .   ? -0.021  38.924 45.860  1.00 37.89 ? 555 HOH A O   1 
HETATM 8406 O O   . HOH G 4 .   ? -28.878 13.589 93.452  1.00 36.04 ? 556 HOH A O   1 
HETATM 8407 O O   . HOH G 4 .   ? -11.259 22.315 48.724  1.00 22.48 ? 557 HOH A O   1 
HETATM 8408 O O   . HOH G 4 .   ? -1.959  7.664  58.444  1.00 46.64 ? 558 HOH A O   1 
HETATM 8409 O O   . HOH G 4 .   ? 2.779   26.382 54.908  1.00 23.79 ? 559 HOH A O   1 
HETATM 8410 O O   . HOH G 4 .   ? 6.054   31.643 81.885  1.00 36.54 ? 560 HOH A O   1 
HETATM 8411 O O   . HOH G 4 .   ? -21.938 13.794 54.007  1.00 42.66 ? 561 HOH A O   1 
HETATM 8412 O O   . HOH G 4 .   ? -12.999 26.236 72.751  1.00 17.71 ? 562 HOH A O   1 
HETATM 8413 O O   . HOH G 4 .   ? -8.573  3.752  59.312  1.00 32.86 ? 563 HOH A O   1 
HETATM 8414 O O   . HOH G 4 .   ? -32.869 11.068 78.315  1.00 50.02 ? 564 HOH A O   1 
HETATM 8415 O O   . HOH G 4 .   ? 18.135  12.168 77.956  1.00 21.53 ? 565 HOH A O   1 
HETATM 8416 O O   . HOH G 4 .   ? 11.144  2.416  93.022  1.00 35.74 ? 566 HOH A O   1 
HETATM 8417 O O   . HOH G 4 .   ? -6.080  11.537 50.619  1.00 23.71 ? 567 HOH A O   1 
HETATM 8418 O O   . HOH G 4 .   ? 4.716   38.350 45.120  1.00 46.22 ? 568 HOH A O   1 
HETATM 8419 O O   . HOH G 4 .   ? -5.065  7.117  86.082  1.00 26.91 ? 569 HOH A O   1 
HETATM 8420 O O   . HOH G 4 .   ? -22.721 18.659 72.315  1.00 21.29 ? 570 HOH A O   1 
HETATM 8421 O O   . HOH G 4 .   ? -5.656  3.282  89.065  1.00 40.26 ? 571 HOH A O   1 
HETATM 8422 O O   . HOH G 4 .   ? -10.770 32.407 81.879  1.00 41.05 ? 572 HOH A O   1 
HETATM 8423 O O   . HOH G 4 .   ? -20.742 25.849 73.003  1.00 15.94 ? 573 HOH A O   1 
HETATM 8424 O O   . HOH G 4 .   ? 4.567   30.767 66.690  1.00 25.78 ? 574 HOH A O   1 
HETATM 8425 O O   . HOH G 4 .   ? -16.988 35.983 67.374  1.00 26.14 ? 575 HOH A O   1 
HETATM 8426 O O   . HOH G 4 .   ? -33.700 11.023 82.784  1.00 41.97 ? 576 HOH A O   1 
HETATM 8427 O O   . HOH G 4 .   ? 14.489  4.283  80.315  1.00 26.99 ? 577 HOH A O   1 
HETATM 8428 O O   . HOH G 4 .   ? -4.577  10.444 48.456  1.00 39.76 ? 578 HOH A O   1 
HETATM 8429 O O   . HOH G 4 .   ? 5.011   4.714  61.934  1.00 40.07 ? 579 HOH A O   1 
HETATM 8430 O O   . HOH G 4 .   ? -7.570  26.250 69.467  1.00 15.01 ? 580 HOH A O   1 
HETATM 8431 O O   . HOH G 4 .   ? 17.269  8.683  52.690  1.00 33.22 ? 581 HOH A O   1 
HETATM 8432 O O   . HOH G 4 .   ? -13.848 2.995  67.733  1.00 42.74 ? 582 HOH A O   1 
HETATM 8433 O O   . HOH G 4 .   ? -8.644  12.080 49.777  1.00 24.79 ? 583 HOH A O   1 
HETATM 8434 O O   . HOH G 4 .   ? 8.750   16.373 69.104  1.00 16.95 ? 584 HOH A O   1 
HETATM 8435 O O   . HOH G 4 .   ? 0.179   15.129 78.674  1.00 17.42 ? 585 HOH A O   1 
HETATM 8436 O O   . HOH G 4 .   ? -15.314 35.629 63.559  1.00 21.69 ? 586 HOH A O   1 
HETATM 8437 O O   . HOH G 4 .   ? -23.634 17.020 62.711  1.00 35.19 ? 587 HOH A O   1 
HETATM 8438 O O   . HOH G 4 .   ? -4.927  20.822 71.471  1.00 13.41 ? 588 HOH A O   1 
HETATM 8439 O O   . HOH G 4 .   ? 5.288   12.906 94.081  1.00 40.97 ? 589 HOH A O   1 
HETATM 8440 O O   . HOH G 4 .   ? -19.213 11.729 55.939  1.00 30.76 ? 590 HOH A O   1 
HETATM 8441 O O   . HOH G 4 .   ? -6.039  42.022 57.674  1.00 36.30 ? 591 HOH A O   1 
HETATM 8442 O O   . HOH G 4 .   ? -23.249 25.618 50.611  1.00 45.52 ? 592 HOH A O   1 
HETATM 8443 O O   . HOH G 4 .   ? -7.891  26.618 85.051  1.00 38.72 ? 593 HOH A O   1 
HETATM 8444 O O   . HOH G 4 .   ? -34.883 25.623 87.783  1.00 24.39 ? 594 HOH A O   1 
HETATM 8445 O O   . HOH G 4 .   ? 19.988  24.571 58.040  1.00 40.30 ? 595 HOH A O   1 
HETATM 8446 O O   . HOH G 4 .   ? -22.299 17.708 60.435  1.00 29.01 ? 596 HOH A O   1 
HETATM 8447 O O   . HOH G 4 .   ? -21.695 10.369 63.269  1.00 30.94 ? 597 HOH A O   1 
HETATM 8448 O O   . HOH G 4 .   ? -15.806 23.121 67.860  1.00 18.93 ? 598 HOH A O   1 
HETATM 8449 O O   . HOH G 4 .   ? -21.607 16.207 49.491  1.00 38.58 ? 599 HOH A O   1 
HETATM 8450 O O   . HOH G 4 .   ? -16.922 5.778  68.312  1.00 19.52 ? 600 HOH A O   1 
HETATM 8451 O O   . HOH G 4 .   ? -34.990 21.730 70.102  1.00 29.25 ? 601 HOH A O   1 
HETATM 8452 O O   . HOH G 4 .   ? -19.398 16.499 52.571  1.00 32.13 ? 602 HOH A O   1 
HETATM 8453 O O   . HOH G 4 .   ? -11.891 24.659 47.606  1.00 43.57 ? 603 HOH A O   1 
HETATM 8454 O O   . HOH G 4 .   ? 25.550  32.762 77.314  1.00 46.13 ? 604 HOH A O   1 
HETATM 8455 O O   . HOH G 4 .   ? -14.245 34.191 81.181  1.00 27.83 ? 605 HOH A O   1 
HETATM 8456 O O   . HOH G 4 .   ? -13.593 21.508 61.724  1.00 15.05 ? 606 HOH A O   1 
HETATM 8457 O O   . HOH G 4 .   ? -12.088 15.357 81.881  1.00 17.04 ? 607 HOH A O   1 
HETATM 8458 O O   . HOH G 4 .   ? -30.270 32.994 80.093  1.00 22.29 ? 608 HOH A O   1 
HETATM 8459 O O   . HOH G 4 .   ? -20.346 35.657 78.332  1.00 28.48 ? 609 HOH A O   1 
HETATM 8460 O O   . HOH G 4 .   ? 17.072  16.969 70.807  1.00 15.76 ? 610 HOH A O   1 
HETATM 8461 O O   . HOH G 4 .   ? -18.207 17.682 69.744  1.00 15.52 ? 611 HOH A O   1 
HETATM 8462 O O   . HOH G 4 .   ? 21.984  24.934 84.294  1.00 40.48 ? 612 HOH A O   1 
HETATM 8463 O O   . HOH G 4 .   ? 20.291  6.995  82.699  1.00 32.28 ? 613 HOH A O   1 
HETATM 8464 O O   . HOH G 4 .   ? 18.539  20.861 66.413  1.00 16.92 ? 614 HOH A O   1 
HETATM 8465 O O   . HOH G 4 .   ? -16.115 37.705 70.785  1.00 46.14 ? 615 HOH A O   1 
HETATM 8466 O O   . HOH G 4 .   ? -24.119 7.343  70.307  1.00 33.75 ? 616 HOH A O   1 
HETATM 8467 O O   . HOH G 4 .   ? -2.559  29.837 66.300  1.00 19.01 ? 617 HOH A O   1 
HETATM 8468 O O   . HOH G 4 .   ? -20.437 24.733 47.429  1.00 38.63 ? 618 HOH A O   1 
HETATM 8469 O O   . HOH G 4 .   ? 7.403   32.090 48.534  1.00 31.22 ? 619 HOH A O   1 
HETATM 8470 O O   . HOH G 4 .   ? -20.181 19.742 63.624  1.00 18.45 ? 620 HOH A O   1 
HETATM 8471 O O   . HOH G 4 .   ? -15.825 7.451  70.900  1.00 21.75 ? 621 HOH A O   1 
HETATM 8472 O O   . HOH G 4 .   ? 21.927  18.465 80.256  1.00 25.15 ? 622 HOH A O   1 
HETATM 8473 O O   . HOH G 4 .   ? 18.910  13.460 80.209  1.00 25.95 ? 623 HOH A O   1 
HETATM 8474 O O   . HOH G 4 .   ? 7.548   17.583 71.346  1.00 21.70 ? 624 HOH A O   1 
HETATM 8475 O O   . HOH G 4 .   ? 20.903  15.083 52.590  1.00 39.65 ? 625 HOH A O   1 
HETATM 8476 O O   . HOH G 4 .   ? -5.016  9.548  55.124  1.00 25.82 ? 626 HOH A O   1 
HETATM 8477 O O   . HOH G 4 .   ? 17.662  10.694 67.643  1.00 27.67 ? 627 HOH A O   1 
HETATM 8478 O O   . HOH G 4 .   ? -18.507 34.292 52.019  1.00 40.89 ? 628 HOH A O   1 
HETATM 8479 O O   . HOH G 4 .   ? -8.696  -0.320 74.107  1.00 36.96 ? 629 HOH A O   1 
HETATM 8480 O O   . HOH G 4 .   ? 20.777  30.050 55.257  1.00 51.42 ? 630 HOH A O   1 
HETATM 8481 O O   . HOH G 4 .   ? 3.021   36.171 61.965  1.00 36.85 ? 631 HOH A O   1 
HETATM 8482 O O   . HOH G 4 .   ? -22.357 31.540 59.167  1.00 28.52 ? 632 HOH A O   1 
HETATM 8483 O O   . HOH G 4 .   ? -1.660  20.570 94.248  1.00 21.32 ? 633 HOH A O   1 
HETATM 8484 O O   . HOH G 4 .   ? -15.627 16.342 53.206  1.00 23.65 ? 634 HOH A O   1 
HETATM 8485 O O   . HOH G 4 .   ? 8.577   21.047 94.983  1.00 30.87 ? 635 HOH A O   1 
HETATM 8486 O O   . HOH G 4 .   ? 9.156   31.575 75.684  1.00 30.68 ? 636 HOH A O   1 
HETATM 8487 O O   . HOH G 4 .   ? -0.738  10.551 95.938  1.00 50.25 ? 637 HOH A O   1 
HETATM 8488 O O   . HOH G 4 .   ? -13.456 31.116 42.792  1.00 35.87 ? 638 HOH A O   1 
HETATM 8489 O O   . HOH G 4 .   ? -39.321 18.808 82.955  1.00 20.51 ? 639 HOH A O   1 
HETATM 8490 O O   . HOH G 4 .   ? -7.016  20.556 54.700  1.00 17.10 ? 640 HOH A O   1 
HETATM 8491 O O   . HOH G 4 .   ? -1.787  2.141  75.717  1.00 51.75 ? 641 HOH A O   1 
HETATM 8492 O O   . HOH G 4 .   ? -13.159 24.498 44.438  1.00 50.71 ? 642 HOH A O   1 
HETATM 8493 O O   . HOH G 4 .   ? 11.072  12.591 92.715  1.00 24.25 ? 643 HOH A O   1 
HETATM 8494 O O   . HOH G 4 .   ? 14.297  27.627 67.080  1.00 35.14 ? 644 HOH A O   1 
HETATM 8495 O O   . HOH G 4 .   ? -10.315 19.179 47.935  1.00 40.49 ? 645 HOH A O   1 
HETATM 8496 O O   . HOH G 4 .   ? -9.133  27.864 76.143  1.00 41.60 ? 646 HOH A O   1 
HETATM 8497 O O   . HOH G 4 .   ? -8.378  17.238 47.754  1.00 33.95 ? 647 HOH A O   1 
HETATM 8498 O O   . HOH G 4 .   ? -24.278 34.833 72.127  1.00 46.00 ? 648 HOH A O   1 
HETATM 8499 O O   . HOH G 4 .   ? 4.604   27.219 90.585  1.00 36.08 ? 649 HOH A O   1 
HETATM 8500 O O   . HOH G 4 .   ? -0.626  28.143 85.807  1.00 33.09 ? 650 HOH A O   1 
HETATM 8501 O O   . HOH G 4 .   ? 4.375   22.619 93.184  1.00 33.63 ? 651 HOH A O   1 
HETATM 8502 O O   . HOH G 4 .   ? -22.940 18.417 69.532  1.00 18.73 ? 652 HOH A O   1 
HETATM 8503 O O   . HOH G 4 .   ? 12.058  3.812  83.908  1.00 34.54 ? 653 HOH A O   1 
HETATM 8504 O O   . HOH G 4 .   ? -23.815 29.373 74.331  1.00 25.09 ? 654 HOH A O   1 
HETATM 8505 O O   . HOH G 4 .   ? -33.772 25.809 97.795  1.00 35.54 ? 655 HOH A O   1 
HETATM 8506 O O   . HOH G 4 .   ? 18.507  17.136 89.001  1.00 30.98 ? 656 HOH A O   1 
HETATM 8507 O O   . HOH G 4 .   ? -36.854 26.798 69.831  1.00 36.49 ? 657 HOH A O   1 
HETATM 8508 O O   . HOH G 4 .   ? -18.667 32.345 65.117  1.00 20.01 ? 658 HOH A O   1 
HETATM 8509 O O   . HOH G 4 .   ? 15.167  27.334 74.768  1.00 21.35 ? 659 HOH A O   1 
HETATM 8510 O O   . HOH G 4 .   ? -19.155 22.700 68.026  1.00 16.59 ? 660 HOH A O   1 
HETATM 8511 O O   . HOH G 4 .   ? 4.852   24.156 46.564  1.00 19.82 ? 661 HOH A O   1 
HETATM 8512 O O   . HOH G 4 .   ? -21.799 34.991 81.504  1.00 29.43 ? 662 HOH A O   1 
HETATM 8513 O O   . HOH G 4 .   ? 3.965   24.179 41.712  1.00 32.12 ? 663 HOH A O   1 
HETATM 8514 O O   . HOH G 4 .   ? -16.094 1.821  63.021  1.00 24.69 ? 664 HOH A O   1 
HETATM 8515 O O   . HOH G 4 .   ? 14.649  24.688 90.897  1.00 30.64 ? 665 HOH A O   1 
HETATM 8516 O O   . HOH G 4 .   ? -34.307 33.332 90.557  1.00 44.02 ? 666 HOH A O   1 
HETATM 8517 O O   . HOH G 4 .   ? -20.657 39.636 49.465  1.00 42.22 ? 667 HOH A O   1 
HETATM 8518 O O   . HOH G 4 .   ? -17.124 45.663 61.414  1.00 28.11 ? 668 HOH A O   1 
HETATM 8519 O O   . HOH G 4 .   ? 17.265  5.768  81.787  1.00 35.53 ? 669 HOH A O   1 
HETATM 8520 O O   . HOH G 4 .   ? -30.748 31.428 75.640  1.00 34.66 ? 670 HOH A O   1 
HETATM 8521 O O   . HOH G 4 .   ? -1.540  29.462 43.878  1.00 34.40 ? 671 HOH A O   1 
HETATM 8522 O O   . HOH G 4 .   ? -23.994 30.012 59.478  1.00 45.27 ? 672 HOH A O   1 
HETATM 8523 O O   . HOH G 4 .   ? -36.447 32.524 86.553  1.00 50.00 ? 673 HOH A O   1 
HETATM 8524 O O   . HOH G 4 .   ? 8.668   28.894 75.342  1.00 21.27 ? 674 HOH A O   1 
HETATM 8525 O O   . HOH G 4 .   ? -0.482  29.030 88.510  1.00 45.50 ? 675 HOH A O   1 
HETATM 8526 O O   . HOH G 4 .   ? 20.807  24.595 62.297  1.00 30.75 ? 676 HOH A O   1 
HETATM 8527 O O   . HOH G 4 .   ? -19.985 37.848 77.053  1.00 36.90 ? 677 HOH A O   1 
HETATM 8528 O O   . HOH G 4 .   ? -6.515  39.970 48.294  1.00 30.06 ? 678 HOH A O   1 
HETATM 8529 O O   . HOH G 4 .   ? 17.737  5.969  77.699  1.00 29.44 ? 679 HOH A O   1 
HETATM 8530 O O   . HOH G 4 .   ? -1.479  37.155 52.140  1.00 31.71 ? 680 HOH A O   1 
HETATM 8531 O O   . HOH G 4 .   ? 0.719   -0.026 58.719  1.00 43.47 ? 681 HOH A O   1 
HETATM 8532 O O   . HOH G 4 .   ? 0.909   20.696 70.477  1.00 11.59 ? 682 HOH A O   1 
HETATM 8533 O O   . HOH G 4 .   ? 3.176   33.776 58.406  1.00 26.39 ? 683 HOH A O   1 
HETATM 8534 O O   . HOH G 4 .   ? 19.218  32.973 76.836  1.00 34.69 ? 684 HOH A O   1 
HETATM 8535 O O   . HOH G 4 .   ? 8.405   31.012 81.132  1.00 57.21 ? 685 HOH A O   1 
HETATM 8536 O O   . HOH G 4 .   ? 16.909  15.344 90.621  1.00 31.28 ? 686 HOH A O   1 
HETATM 8537 O O   . HOH G 4 .   ? 20.194  23.144 55.064  1.00 44.62 ? 687 HOH A O   1 
HETATM 8538 O O   . HOH G 4 .   ? -19.233 7.427  62.057  1.00 32.92 ? 688 HOH A O   1 
HETATM 8539 O O   . HOH G 4 .   ? -4.677  9.253  57.882  1.00 18.44 ? 689 HOH A O   1 
HETATM 8540 O O   . HOH G 4 .   ? -10.519 18.397 91.563  1.00 29.41 ? 690 HOH A O   1 
HETATM 8541 O O   . HOH G 4 .   ? 13.382  7.843  54.490  1.00 35.60 ? 691 HOH A O   1 
HETATM 8542 O O   . HOH G 4 .   ? -26.472 25.184 102.568 1.00 42.63 ? 692 HOH A O   1 
HETATM 8543 O O   . HOH G 4 .   ? 19.550  19.592 89.490  1.00 29.51 ? 693 HOH A O   1 
HETATM 8544 O O   . HOH G 4 .   ? 10.746  6.711  57.989  1.00 29.64 ? 694 HOH A O   1 
HETATM 8545 O O   . HOH G 4 .   ? -29.580 35.281 77.433  1.00 35.15 ? 695 HOH A O   1 
HETATM 8546 O O   . HOH G 4 .   ? -14.157 36.646 73.311  1.00 32.47 ? 696 HOH A O   1 
HETATM 8547 O O   . HOH G 4 .   ? 14.708  6.675  79.211  1.00 23.02 ? 697 HOH A O   1 
HETATM 8548 O O   . HOH G 4 .   ? -9.500  34.021 67.681  1.00 16.20 ? 698 HOH A O   1 
HETATM 8549 O O   . HOH G 4 .   ? -22.585 33.150 71.915  1.00 24.37 ? 699 HOH A O   1 
HETATM 8550 O O   . HOH G 4 .   ? -24.709 22.820 99.782  1.00 36.68 ? 700 HOH A O   1 
HETATM 8551 O O   . HOH G 4 .   ? -17.453 24.645 66.357  1.00 25.20 ? 701 HOH A O   1 
HETATM 8552 O O   . HOH G 4 .   ? 1.468   21.712 87.008  1.00 16.28 ? 702 HOH A O   1 
HETATM 8553 O O   . HOH G 4 .   ? 0.038   1.719  73.099  1.00 32.27 ? 703 HOH A O   1 
HETATM 8554 O O   . HOH G 4 .   ? -26.572 27.646 68.956  1.00 30.49 ? 704 HOH A O   1 
HETATM 8555 O O   . HOH G 4 .   ? -10.181 43.002 57.250  1.00 39.02 ? 705 HOH A O   1 
HETATM 8556 O O   . HOH G 4 .   ? -26.099 8.217  76.140  1.00 53.73 ? 706 HOH A O   1 
HETATM 8557 O O   . HOH G 4 .   ? 0.364   23.643 88.435  1.00 33.36 ? 707 HOH A O   1 
HETATM 8558 O O   . HOH G 4 .   ? -12.441 31.074 89.030  1.00 32.33 ? 708 HOH A O   1 
HETATM 8559 O O   . HOH G 4 .   ? 10.960  33.883 75.151  1.00 41.99 ? 709 HOH A O   1 
HETATM 8560 O O   . HOH G 4 .   ? -35.655 30.605 89.946  1.00 47.77 ? 710 HOH A O   1 
HETATM 8561 O O   . HOH G 4 .   ? 2.796   35.598 49.900  1.00 42.35 ? 711 HOH A O   1 
HETATM 8562 O O   . HOH G 4 .   ? -8.280  29.235 77.183  1.00 34.01 ? 712 HOH A O   1 
HETATM 8563 O O   . HOH G 4 .   ? 13.752  32.184 68.308  1.00 53.67 ? 713 HOH A O   1 
HETATM 8564 O O   . HOH G 4 .   ? -12.517 37.905 50.259  1.00 26.84 ? 714 HOH A O   1 
HETATM 8565 O O   . HOH G 4 .   ? -10.204 32.537 69.817  1.00 16.63 ? 715 HOH A O   1 
HETATM 8566 O O   . HOH G 4 .   ? 11.928  10.409 94.071  1.00 37.78 ? 716 HOH A O   1 
HETATM 8567 O O   . HOH G 4 .   ? 25.141  16.716 79.006  1.00 27.29 ? 717 HOH A O   1 
HETATM 8568 O O   . HOH G 4 .   ? -27.710 18.421 63.923  1.00 39.12 ? 718 HOH A O   1 
HETATM 8569 O O   . HOH G 4 .   ? 23.845  28.950 71.239  1.00 42.76 ? 719 HOH A O   1 
HETATM 8570 O O   . HOH G 4 .   ? -7.554  40.363 53.633  1.00 38.34 ? 720 HOH A O   1 
HETATM 8571 O O   . HOH G 4 .   ? -24.851 30.583 72.391  1.00 34.29 ? 721 HOH A O   1 
HETATM 8572 O O   . HOH G 4 .   ? -3.797  21.840 39.907  1.00 47.18 ? 722 HOH A O   1 
HETATM 8573 O O   . HOH G 4 .   ? 21.458  13.805 80.287  1.00 32.52 ? 723 HOH A O   1 
HETATM 8574 O O   . HOH G 4 .   ? -36.446 19.538 88.847  1.00 18.06 ? 724 HOH A O   1 
HETATM 8575 O O   . HOH G 4 .   ? 22.517  15.193 76.438  1.00 28.05 ? 725 HOH A O   1 
HETATM 8576 O O   . HOH G 4 .   ? -19.585 12.300 51.000  1.00 30.70 ? 726 HOH A O   1 
HETATM 8577 O O   . HOH G 4 .   ? -31.360 15.086 68.928  1.00 47.35 ? 727 HOH A O   1 
HETATM 8578 O O   . HOH G 4 .   ? 20.686  12.424 76.617  1.00 33.07 ? 728 HOH A O   1 
HETATM 8579 O O   . HOH G 4 .   ? 6.993   3.960  57.199  1.00 35.58 ? 729 HOH A O   1 
HETATM 8580 O O   . HOH G 4 .   ? -19.866 8.623  64.258  1.00 26.58 ? 730 HOH A O   1 
HETATM 8581 O O   . HOH G 4 .   ? -14.252 36.652 75.848  1.00 37.10 ? 731 HOH A O   1 
HETATM 8582 O O   . HOH G 4 .   ? 16.801  26.372 88.870  1.00 32.87 ? 732 HOH A O   1 
HETATM 8583 O O   . HOH G 4 .   ? -34.494 12.813 80.943  1.00 37.90 ? 733 HOH A O   1 
HETATM 8584 O O   . HOH G 4 .   ? -12.556 20.641 47.952  1.00 37.21 ? 734 HOH A O   1 
HETATM 8585 O O   . HOH G 4 .   ? -6.274  11.306 46.847  1.00 54.11 ? 735 HOH A O   1 
HETATM 8586 O O   . HOH G 4 .   ? -1.621  29.407 79.681  1.00 41.47 ? 736 HOH A O   1 
HETATM 8587 O O   . HOH G 4 .   ? -8.860  3.621  77.825  1.00 41.04 ? 737 HOH A O   1 
HETATM 8588 O O   . HOH G 4 .   ? -6.636  26.052 37.974  1.00 61.27 ? 738 HOH A O   1 
HETATM 8589 O O   . HOH G 4 .   ? 5.688   15.217 94.864  1.00 36.17 ? 739 HOH A O   1 
HETATM 8590 O O   . HOH G 4 .   ? -13.242 19.730 89.155  1.00 43.83 ? 740 HOH A O   1 
HETATM 8591 O O   . HOH G 4 .   ? 3.470   0.096  83.124  1.00 37.86 ? 741 HOH A O   1 
HETATM 8592 O O   . HOH G 4 .   ? -20.039 36.619 64.407  1.00 24.80 ? 742 HOH A O   1 
HETATM 8593 O O   . HOH G 4 .   ? 21.769  9.959  77.271  1.00 37.83 ? 743 HOH A O   1 
HETATM 8594 O O   . HOH G 4 .   ? 19.444  18.015 68.060  1.00 23.69 ? 744 HOH A O   1 
HETATM 8595 O O   . HOH G 4 .   ? -16.413 31.600 47.595  1.00 40.35 ? 745 HOH A O   1 
HETATM 8596 O O   . HOH G 4 .   ? -0.598  13.212 80.361  1.00 17.17 ? 746 HOH A O   1 
HETATM 8597 O O   . HOH G 4 .   ? 13.739  10.597 95.657  1.00 47.29 ? 747 HOH A O   1 
HETATM 8598 O O   . HOH G 4 .   ? 11.099  21.678 43.298  1.00 35.65 ? 748 HOH A O   1 
HETATM 8599 O O   . HOH G 4 .   ? 1.074   37.246 50.408  1.00 42.39 ? 749 HOH A O   1 
HETATM 8600 O O   . HOH G 4 .   ? 21.251  23.469 65.457  1.00 45.04 ? 750 HOH A O   1 
HETATM 8601 O O   . HOH G 4 .   ? -25.142 29.521 97.488  1.00 40.57 ? 751 HOH A O   1 
HETATM 8602 O O   . HOH G 4 .   ? -26.279 19.590 59.973  1.00 38.36 ? 752 HOH A O   1 
HETATM 8603 O O   . HOH G 4 .   ? 5.669   3.874  55.127  1.00 41.83 ? 753 HOH A O   1 
HETATM 8604 O O   . HOH G 4 .   ? 8.162   24.497 93.038  1.00 44.14 ? 754 HOH A O   1 
HETATM 8605 O O   . HOH G 4 .   ? -20.596 31.219 51.160  1.00 45.31 ? 755 HOH A O   1 
HETATM 8606 O O   . HOH G 4 .   ? -0.164  29.926 80.933  1.00 44.98 ? 756 HOH A O   1 
HETATM 8607 O O   . HOH G 4 .   ? -31.420 11.913 75.791  1.00 38.45 ? 757 HOH A O   1 
HETATM 8608 O O   . HOH G 4 .   ? 0.093   3.469  77.654  1.00 40.18 ? 758 HOH A O   1 
HETATM 8609 O O   . HOH G 4 .   ? -12.084 35.046 85.800  1.00 44.96 ? 759 HOH A O   1 
HETATM 8610 O O   . HOH G 4 .   ? -34.380 20.783 72.867  1.00 41.81 ? 760 HOH A O   1 
HETATM 8611 O O   . HOH G 4 .   ? -16.657 38.488 72.512  1.00 49.15 ? 761 HOH A O   1 
HETATM 8612 O O   . HOH G 4 .   ? -4.056  0.376  73.702  1.00 53.13 ? 762 HOH A O   1 
HETATM 8613 O O   . HOH G 4 .   ? -23.964 31.917 95.793  1.00 45.35 ? 763 HOH A O   1 
HETATM 8614 O O   . HOH G 4 .   ? -19.464 11.125 86.613  1.00 45.01 ? 764 HOH A O   1 
HETATM 8615 O O   . HOH G 4 .   ? -7.281  0.501  75.879  1.00 37.98 ? 765 HOH A O   1 
HETATM 8616 O O   . HOH G 4 .   ? 8.676   1.197  82.604  1.00 49.71 ? 766 HOH A O   1 
HETATM 8617 O O   . HOH G 4 .   ? -21.578 11.193 86.312  1.00 50.68 ? 767 HOH A O   1 
HETATM 8618 O O   . HOH G 4 .   ? 21.653  19.377 67.155  1.00 32.39 ? 768 HOH A O   1 
HETATM 8619 O O   . HOH G 4 .   ? -17.666 34.911 64.783  1.00 22.31 ? 769 HOH A O   1 
HETATM 8620 O O   . HOH G 4 .   ? -7.829  1.953  89.987  1.00 51.83 ? 770 HOH A O   1 
HETATM 8621 O O   . HOH G 4 .   ? 17.103  8.189  69.101  1.00 45.69 ? 771 HOH A O   1 
HETATM 8622 O O   . HOH G 4 .   ? -14.581 15.779 50.464  1.00 40.79 ? 772 HOH A O   1 
HETATM 8623 O O   . HOH G 4 .   ? -8.664  35.187 77.608  1.00 40.48 ? 773 HOH A O   1 
HETATM 8624 O O   . HOH G 4 .   ? 22.396  13.611 75.099  1.00 52.54 ? 774 HOH A O   1 
HETATM 8625 O O   . HOH G 4 .   ? -12.065 33.388 87.645  1.00 41.99 ? 775 HOH A O   1 
HETATM 8626 O O   . HOH G 4 .   ? -1.717  -0.038 72.293  1.00 34.23 ? 776 HOH A O   1 
HETATM 8627 O O   . HOH G 4 .   ? -4.283  24.198 35.580  1.00 52.45 ? 777 HOH A O   1 
HETATM 8628 O O   . HOH G 4 .   ? 2.883   34.866 56.169  1.00 48.06 ? 778 HOH A O   1 
HETATM 8629 O O   . HOH G 4 .   ? 22.350  17.366 66.480  1.00 41.67 ? 779 HOH A O   1 
HETATM 8630 O O   . HOH G 4 .   ? -23.615 8.650  63.263  1.00 46.68 ? 780 HOH A O   1 
HETATM 8631 O O   . HOH G 4 .   ? -1.631  4.061  82.012  1.00 48.04 ? 781 HOH A O   1 
HETATM 8632 O O   . HOH G 4 .   ? 10.308  25.546 93.231  1.00 48.22 ? 782 HOH A O   1 
HETATM 8633 O O   . HOH G 4 .   ? 10.166  2.493  83.117  1.00 48.47 ? 783 HOH A O   1 
HETATM 8634 O O   . HOH G 4 .   ? 12.887  31.822 82.212  1.00 41.86 ? 784 HOH A O   1 
HETATM 8635 O O   . HOH G 4 .   ? 18.121  4.693  79.708  1.00 46.72 ? 785 HOH A O   1 
HETATM 8636 O O   . HOH G 4 .   ? 0.653   3.456  82.498  1.00 38.03 ? 786 HOH A O   1 
HETATM 8637 O O   . HOH G 4 .   ? -21.098 14.307 51.561  1.00 33.42 ? 787 HOH A O   1 
HETATM 8638 O O   . HOH G 4 .   ? -22.726 5.013  68.984  1.00 38.47 ? 788 HOH A O   1 
HETATM 8639 O O   . HOH G 4 .   ? 6.727   33.799 61.338  1.00 51.94 ? 789 HOH A O   1 
HETATM 8640 O O   . HOH G 4 .   ? 5.515   35.097 60.377  1.00 52.77 ? 790 HOH A O   1 
HETATM 8641 O O   . HOH G 4 .   ? 15.611  32.082 81.544  1.00 42.86 ? 791 HOH A O   1 
HETATM 8642 O O   . HOH G 4 .   ? 17.188  4.996  84.324  1.00 39.83 ? 792 HOH A O   1 
HETATM 8643 O O   . HOH G 4 .   ? -12.595 36.693 77.441  1.00 48.00 ? 793 HOH A O   1 
HETATM 8644 O O   . HOH G 4 .   ? -23.014 11.122 57.247  1.00 47.77 ? 794 HOH A O   1 
HETATM 8645 O O   . HOH G 4 .   ? -36.675 34.183 88.494  1.00 46.41 ? 795 HOH A O   1 
HETATM 8646 O O   . HOH G 4 .   ? 22.085  15.903 79.180  1.00 26.44 ? 796 HOH A O   1 
HETATM 8647 O O   . HOH G 4 .   ? 0.297   34.110 83.135  1.00 46.77 ? 797 HOH A O   1 
HETATM 8648 O O   . HOH G 4 .   ? -25.802 20.077 62.242  1.00 43.27 ? 798 HOH A O   1 
HETATM 8649 O O   . HOH G 4 .   ? -32.286 14.729 101.339 1.00 44.71 ? 799 HOH A O   1 
HETATM 8650 O O   . HOH G 4 .   ? -9.436  40.311 47.846  1.00 45.00 ? 800 HOH A O   1 
HETATM 8651 O O   . HOH G 4 .   ? 18.063  32.080 85.126  1.00 41.32 ? 801 HOH A O   1 
HETATM 8652 O O   . HOH G 4 .   ? -15.320 4.021  69.852  1.00 36.61 ? 802 HOH A O   1 
HETATM 8653 O O   . HOH G 4 .   ? -1.594  26.647 75.306  1.00 24.73 ? 803 HOH A O   1 
HETATM 8654 O O   . HOH G 4 .   ? -27.438 23.946 98.800  1.00 42.35 ? 804 HOH A O   1 
HETATM 8655 O O   . HOH G 4 .   ? -12.205 35.047 79.355  1.00 39.78 ? 805 HOH A O   1 
HETATM 8656 O O   . HOH G 4 .   ? -15.144 4.748  71.830  1.00 28.35 ? 806 HOH A O   1 
HETATM 8657 O O   . HOH G 4 .   ? -11.785 17.346 93.491  1.00 38.46 ? 807 HOH A O   1 
HETATM 8658 O O   . HOH G 4 .   ? -6.697  9.269  51.939  1.00 41.98 ? 808 HOH A O   1 
HETATM 8659 O O   . HOH G 4 .   ? -22.086 35.283 64.872  1.00 49.11 ? 809 HOH A O   1 
HETATM 8660 O O   . HOH G 4 .   ? -1.666  30.867 77.404  1.00 40.50 ? 810 HOH A O   1 
HETATM 8661 O O   . HOH G 4 .   ? 11.950  35.641 76.944  1.00 47.44 ? 811 HOH A O   1 
HETATM 8662 O O   . HOH G 4 .   ? -10.116 37.040 76.253  1.00 43.24 ? 812 HOH A O   1 
HETATM 8663 O O   . HOH G 4 .   ? 1.959   -6.143 74.493  1.00 34.23 ? 813 HOH A O   1 
HETATM 8664 O O   . HOH G 4 .   ? 1.766   34.384 77.198  1.00 39.55 ? 814 HOH A O   1 
HETATM 8665 O O   . HOH G 4 .   ? -0.806  34.037 80.717  1.00 49.91 ? 815 HOH A O   1 
HETATM 8666 O O   . HOH G 4 .   ? -2.776  33.521 75.071  1.00 31.01 ? 816 HOH A O   1 
HETATM 8667 O O   . HOH G 4 .   ? -1.181  31.538 73.954  1.00 35.81 ? 817 HOH A O   1 
HETATM 8668 O O   . HOH G 4 .   ? -2.077  36.959 74.985  1.00 45.59 ? 818 HOH A O   1 
HETATM 8669 O O   . HOH H 4 .   ? 2.311   39.021 20.295  1.00 42.46 ? 501 HOH B O   1 
HETATM 8670 O O   . HOH H 4 .   ? -28.255 30.117 49.482  1.00 43.64 ? 502 HOH B O   1 
HETATM 8671 O O   . HOH H 4 .   ? -17.195 31.770 45.365  1.00 37.64 ? 503 HOH B O   1 
HETATM 8672 O O   . HOH H 4 .   ? -21.369 34.334 -4.954  1.00 38.46 ? 504 HOH B O   1 
HETATM 8673 O O   . HOH H 4 .   ? -39.581 52.053 57.586  1.00 43.41 ? 505 HOH B O   1 
HETATM 8674 O O   . HOH H 4 .   ? -15.756 55.630 42.721  1.00 38.87 ? 506 HOH B O   1 
HETATM 8675 O O   . HOH H 4 .   ? -25.846 45.666 61.642  1.00 46.26 ? 507 HOH B O   1 
HETATM 8676 O O   . HOH H 4 .   ? -56.177 53.283 26.042  1.00 43.06 ? 508 HOH B O   1 
HETATM 8677 O O   . HOH H 4 .   ? -13.767 41.214 -3.220  1.00 45.62 ? 509 HOH B O   1 
HETATM 8678 O O   . HOH H 4 .   ? -54.330 32.729 41.510  1.00 30.83 ? 510 HOH B O   1 
HETATM 8679 O O   . HOH H 4 .   ? -54.719 51.243 18.957  1.00 39.36 ? 511 HOH B O   1 
HETATM 8680 O O   . HOH H 4 .   ? 0.065   37.156 9.794   1.00 43.52 ? 512 HOH B O   1 
HETATM 8681 O O   . HOH H 4 .   ? -10.878 42.041 43.225  1.00 26.57 ? 513 HOH B O   1 
HETATM 8682 O O   . HOH H 4 .   ? -26.792 26.859 10.864  1.00 24.23 ? 514 HOH B O   1 
HETATM 8683 O O   . HOH H 4 .   ? -38.345 53.886 43.971  1.00 52.36 ? 515 HOH B O   1 
HETATM 8684 O O   . HOH H 4 .   ? -12.328 35.305 -5.778  1.00 51.16 ? 516 HOH B O   1 
HETATM 8685 O O   . HOH H 4 .   ? -26.029 23.540 38.331  1.00 41.31 ? 517 HOH B O   1 
HETATM 8686 O O   . HOH H 4 .   ? -53.648 45.751 11.275  1.00 44.02 ? 518 HOH B O   1 
HETATM 8687 O O   . HOH H 4 .   ? -25.500 31.551 51.130  1.00 41.99 ? 519 HOH B O   1 
HETATM 8688 O O   . HOH H 4 .   ? -32.051 57.884 42.709  1.00 30.42 ? 520 HOH B O   1 
HETATM 8689 O O   . HOH H 4 .   ? -20.948 44.168 48.856  1.00 31.76 ? 521 HOH B O   1 
HETATM 8690 O O   . HOH H 4 .   ? -4.947  47.516 24.054  1.00 49.32 ? 522 HOH B O   1 
HETATM 8691 O O   . HOH H 4 .   ? -30.274 46.790 13.029  1.00 39.49 ? 523 HOH B O   1 
HETATM 8692 O O   . HOH H 4 .   ? -22.032 36.256 3.357   1.00 39.75 ? 524 HOH B O   1 
HETATM 8693 O O   . HOH H 4 .   ? -27.808 41.898 58.412  1.00 45.17 ? 525 HOH B O   1 
HETATM 8694 O O   . HOH H 4 .   ? -14.008 38.077 23.318  1.00 20.99 ? 526 HOH B O   1 
HETATM 8695 O O   . HOH H 4 .   ? -28.286 19.491 23.419  1.00 33.09 ? 527 HOH B O   1 
HETATM 8696 O O   . HOH H 4 .   ? -6.440  34.042 1.868   1.00 42.21 ? 528 HOH B O   1 
HETATM 8697 O O   . HOH H 4 .   ? -10.179 30.535 12.332  1.00 36.31 ? 529 HOH B O   1 
HETATM 8698 O O   . HOH H 4 .   ? -26.711 52.278 15.784  1.00 36.19 ? 530 HOH B O   1 
HETATM 8699 O O   . HOH H 4 .   ? -23.387 45.844 24.411  1.00 21.57 ? 531 HOH B O   1 
HETATM 8700 O O   . HOH H 4 .   ? -11.702 36.090 32.509  1.00 32.28 ? 532 HOH B O   1 
HETATM 8701 O O   . HOH H 4 .   ? -18.132 55.358 29.275  1.00 21.86 ? 533 HOH B O   1 
HETATM 8702 O O   . HOH H 4 .   ? -39.603 24.481 37.986  1.00 39.47 ? 534 HOH B O   1 
HETATM 8703 O O   . HOH H 4 .   ? -48.122 24.929 45.905  1.00 37.87 ? 535 HOH B O   1 
HETATM 8704 O O   . HOH H 4 .   ? -41.093 24.101 42.365  1.00 49.10 ? 536 HOH B O   1 
HETATM 8705 O O   . HOH H 4 .   ? -27.026 31.030 46.902  1.00 26.64 ? 537 HOH B O   1 
HETATM 8706 O O   . HOH H 4 .   ? -37.988 16.549 34.745  1.00 39.26 ? 538 HOH B O   1 
HETATM 8707 O O   . HOH H 4 .   ? -11.596 33.162 32.274  1.00 40.29 ? 539 HOH B O   1 
HETATM 8708 O O   . HOH H 4 .   ? -8.626  52.787 -1.392  1.00 44.11 ? 540 HOH B O   1 
HETATM 8709 O O   . HOH H 4 .   ? -55.319 32.856 24.322  1.00 31.67 ? 541 HOH B O   1 
HETATM 8710 O O   . HOH H 4 .   ? -20.026 29.291 12.814  1.00 49.74 ? 542 HOH B O   1 
HETATM 8711 O O   . HOH H 4 .   ? -25.406 36.412 9.958   1.00 24.31 ? 543 HOH B O   1 
HETATM 8712 O O   . HOH H 4 .   ? -16.468 30.634 11.008  1.00 47.11 ? 544 HOH B O   1 
HETATM 8713 O O   . HOH H 4 .   ? -44.398 36.655 31.457  1.00 18.80 ? 545 HOH B O   1 
HETATM 8714 O O   . HOH H 4 .   ? -48.487 52.459 32.998  1.00 43.25 ? 546 HOH B O   1 
HETATM 8715 O O   . HOH H 4 .   ? -52.526 46.081 30.473  1.00 26.25 ? 547 HOH B O   1 
HETATM 8716 O O   . HOH H 4 .   ? -12.775 29.572 13.810  1.00 36.49 ? 548 HOH B O   1 
HETATM 8717 O O   . HOH H 4 .   ? -12.255 36.899 34.880  1.00 39.62 ? 549 HOH B O   1 
HETATM 8718 O O   . HOH H 4 .   ? -19.653 22.334 31.654  1.00 45.99 ? 550 HOH B O   1 
HETATM 8719 O O   . HOH H 4 .   ? -15.521 52.209 50.637  1.00 27.71 ? 551 HOH B O   1 
HETATM 8720 O O   . HOH H 4 .   ? -26.354 40.032 43.024  1.00 14.31 ? 552 HOH B O   1 
HETATM 8721 O O   . HOH H 4 .   ? -24.985 56.511 55.669  1.00 42.07 ? 553 HOH B O   1 
HETATM 8722 O O   . HOH H 4 .   ? -60.045 46.625 20.915  1.00 43.16 ? 554 HOH B O   1 
HETATM 8723 O O   . HOH H 4 .   ? -25.673 19.464 29.967  1.00 30.23 ? 555 HOH B O   1 
HETATM 8724 O O   . HOH H 4 .   ? -25.737 51.127 8.479   1.00 37.14 ? 556 HOH B O   1 
HETATM 8725 O O   . HOH H 4 .   ? -53.388 41.351 35.850  1.00 20.36 ? 557 HOH B O   1 
HETATM 8726 O O   . HOH H 4 .   ? -45.079 37.487 22.354  1.00 31.27 ? 558 HOH B O   1 
HETATM 8727 O O   . HOH H 4 .   ? -15.429 45.221 23.007  1.00 22.00 ? 559 HOH B O   1 
HETATM 8728 O O   . HOH H 4 .   ? -34.545 26.799 19.373  1.00 26.20 ? 560 HOH B O   1 
HETATM 8729 O O   . HOH H 4 .   ? -11.994 50.717 36.729  1.00 31.84 ? 561 HOH B O   1 
HETATM 8730 O O   . HOH H 4 .   ? -35.187 44.042 57.812  1.00 43.34 ? 562 HOH B O   1 
HETATM 8731 O O   . HOH H 4 .   ? -13.269 37.659 25.967  1.00 23.42 ? 563 HOH B O   1 
HETATM 8732 O O   . HOH H 4 .   ? -33.922 54.159 44.146  1.00 31.50 ? 564 HOH B O   1 
HETATM 8733 O O   . HOH H 4 .   ? -36.805 44.318 52.988  1.00 22.31 ? 565 HOH B O   1 
HETATM 8734 O O   . HOH H 4 .   ? -13.545 29.422 31.825  1.00 37.91 ? 566 HOH B O   1 
HETATM 8735 O O   . HOH H 4 .   ? -48.690 50.038 19.426  1.00 37.47 ? 567 HOH B O   1 
HETATM 8736 O O   . HOH H 4 .   ? -21.119 41.117 35.142  1.00 19.12 ? 568 HOH B O   1 
HETATM 8737 O O   . HOH H 4 .   ? -28.803 23.923 19.350  1.00 43.22 ? 569 HOH B O   1 
HETATM 8738 O O   . HOH H 4 .   ? -39.483 42.067 22.430  1.00 25.07 ? 570 HOH B O   1 
HETATM 8739 O O   . HOH H 4 .   ? -60.467 50.059 22.938  1.00 43.54 ? 571 HOH B O   1 
HETATM 8740 O O   . HOH H 4 .   ? -26.424 45.281 21.067  1.00 21.23 ? 572 HOH B O   1 
HETATM 8741 O O   . HOH H 4 .   ? -19.705 42.510 28.715  1.00 23.89 ? 573 HOH B O   1 
HETATM 8742 O O   . HOH H 4 .   ? -37.618 35.268 20.668  1.00 17.78 ? 574 HOH B O   1 
HETATM 8743 O O   . HOH H 4 .   ? -40.013 50.778 33.562  1.00 30.58 ? 575 HOH B O   1 
HETATM 8744 O O   . HOH H 4 .   ? -26.092 35.103 15.489  1.00 20.80 ? 576 HOH B O   1 
HETATM 8745 O O   . HOH H 4 .   ? -22.989 54.030 16.016  1.00 32.37 ? 577 HOH B O   1 
HETATM 8746 O O   . HOH H 4 .   ? -21.251 41.569 48.398  1.00 22.79 ? 578 HOH B O   1 
HETATM 8747 O O   . HOH H 4 .   ? -31.086 35.078 2.912   1.00 49.04 ? 579 HOH B O   1 
HETATM 8748 O O   . HOH H 4 .   ? -36.638 53.526 41.255  1.00 37.57 ? 580 HOH B O   1 
HETATM 8749 O O   . HOH H 4 .   ? -9.865  42.749 36.623  1.00 51.14 ? 581 HOH B O   1 
HETATM 8750 O O   . HOH H 4 .   ? -9.438  44.102 32.406  1.00 43.69 ? 582 HOH B O   1 
HETATM 8751 O O   . HOH H 4 .   ? -39.527 51.638 51.531  1.00 33.35 ? 583 HOH B O   1 
HETATM 8752 O O   . HOH H 4 .   ? -29.230 38.359 6.332   1.00 32.27 ? 584 HOH B O   1 
HETATM 8753 O O   . HOH H 4 .   ? -6.158  45.369 25.657  1.00 48.83 ? 585 HOH B O   1 
HETATM 8754 O O   . HOH H 4 .   ? -4.405  44.434 5.698   1.00 39.83 ? 586 HOH B O   1 
HETATM 8755 O O   . HOH H 4 .   ? -32.216 58.918 52.658  1.00 43.81 ? 587 HOH B O   1 
HETATM 8756 O O   . HOH H 4 .   ? -4.102  31.875 12.362  1.00 41.17 ? 588 HOH B O   1 
HETATM 8757 O O   . HOH H 4 .   ? -16.979 43.029 -7.043  1.00 34.30 ? 589 HOH B O   1 
HETATM 8758 O O   . HOH H 4 .   ? -50.701 33.219 8.852   1.00 32.19 ? 590 HOH B O   1 
HETATM 8759 O O   . HOH H 4 .   ? -20.840 26.875 25.452  1.00 16.78 ? 591 HOH B O   1 
HETATM 8760 O O   . HOH H 4 .   ? -35.986 46.399 44.385  1.00 22.39 ? 592 HOH B O   1 
HETATM 8761 O O   . HOH H 4 .   ? -39.721 33.859 49.674  1.00 46.95 ? 593 HOH B O   1 
HETATM 8762 O O   . HOH H 4 .   ? -53.077 37.351 31.308  1.00 22.59 ? 594 HOH B O   1 
HETATM 8763 O O   . HOH H 4 .   ? -32.541 49.626 32.392  1.00 28.69 ? 595 HOH B O   1 
HETATM 8764 O O   . HOH H 4 .   ? -10.103 49.060 35.437  1.00 49.54 ? 596 HOH B O   1 
HETATM 8765 O O   . HOH H 4 .   ? -20.566 61.146 41.097  1.00 41.18 ? 597 HOH B O   1 
HETATM 8766 O O   . HOH H 4 .   ? -8.955  46.637 26.080  1.00 45.87 ? 598 HOH B O   1 
HETATM 8767 O O   . HOH H 4 .   ? -50.843 24.546 17.301  1.00 47.62 ? 599 HOH B O   1 
HETATM 8768 O O   . HOH H 4 .   ? -16.462 40.218 49.364  1.00 24.14 ? 600 HOH B O   1 
HETATM 8769 O O   . HOH H 4 .   ? -44.203 29.240 44.245  1.00 42.53 ? 601 HOH B O   1 
HETATM 8770 O O   . HOH H 4 .   ? -31.215 56.907 46.615  1.00 36.17 ? 602 HOH B O   1 
HETATM 8771 O O   . HOH H 4 .   ? -45.197 33.502 6.398   1.00 36.43 ? 603 HOH B O   1 
HETATM 8772 O O   . HOH H 4 .   ? -51.565 27.709 30.225  1.00 41.22 ? 604 HOH B O   1 
HETATM 8773 O O   . HOH H 4 .   ? -39.917 44.496 45.612  1.00 19.43 ? 605 HOH B O   1 
HETATM 8774 O O   . HOH H 4 .   ? -45.579 47.538 53.825  1.00 36.19 ? 606 HOH B O   1 
HETATM 8775 O O   . HOH H 4 .   ? -25.710 59.523 44.482  1.00 37.56 ? 607 HOH B O   1 
HETATM 8776 O O   . HOH H 4 .   ? -35.032 22.115 23.348  1.00 47.29 ? 608 HOH B O   1 
HETATM 8777 O O   . HOH H 4 .   ? -19.336 25.320 27.778  1.00 26.80 ? 609 HOH B O   1 
HETATM 8778 O O   . HOH H 4 .   ? -54.761 26.617 24.255  1.00 34.91 ? 610 HOH B O   1 
HETATM 8779 O O   . HOH H 4 .   ? -16.344 58.579 -7.735  1.00 50.24 ? 611 HOH B O   1 
HETATM 8780 O O   . HOH H 4 .   ? -16.580 42.044 28.037  1.00 18.26 ? 612 HOH B O   1 
HETATM 8781 O O   . HOH H 4 .   ? -29.893 30.958 51.443  1.00 43.41 ? 613 HOH B O   1 
HETATM 8782 O O   . HOH H 4 .   ? -12.764 26.485 24.683  1.00 32.65 ? 614 HOH B O   1 
HETATM 8783 O O   . HOH H 4 .   ? -41.060 49.566 59.387  1.00 41.36 ? 615 HOH B O   1 
HETATM 8784 O O   . HOH H 4 .   ? -19.297 55.132 33.291  1.00 23.94 ? 616 HOH B O   1 
HETATM 8785 O O   . HOH H 4 .   ? -28.057 46.066 28.519  1.00 17.54 ? 617 HOH B O   1 
HETATM 8786 O O   . HOH H 4 .   ? -19.267 40.271 6.911   1.00 36.82 ? 618 HOH B O   1 
HETATM 8787 O O   . HOH H 4 .   ? -6.873  51.696 14.378  1.00 34.48 ? 619 HOH B O   1 
HETATM 8788 O O   . HOH H 4 .   ? -26.258 39.221 8.207   1.00 44.23 ? 620 HOH B O   1 
HETATM 8789 O O   . HOH H 4 .   ? -36.879 40.626 28.817  1.00 13.67 ? 621 HOH B O   1 
HETATM 8790 O O   . HOH H 4 .   ? -51.137 47.826 27.486  1.00 28.47 ? 622 HOH B O   1 
HETATM 8791 O O   . HOH H 4 .   ? -53.059 30.899 34.570  1.00 44.32 ? 623 HOH B O   1 
HETATM 8792 O O   . HOH H 4 .   ? -48.123 24.443 19.729  1.00 38.51 ? 624 HOH B O   1 
HETATM 8793 O O   . HOH H 4 .   ? -2.201  35.213 6.325   1.00 36.86 ? 625 HOH B O   1 
HETATM 8794 O O   . HOH H 4 .   ? -24.035 36.815 49.698  1.00 27.57 ? 626 HOH B O   1 
HETATM 8795 O O   . HOH H 4 .   ? -55.639 26.592 20.291  1.00 40.06 ? 627 HOH B O   1 
HETATM 8796 O O   . HOH H 4 .   ? -38.625 41.019 5.012   1.00 25.33 ? 628 HOH B O   1 
HETATM 8797 O O   . HOH H 4 .   ? -29.059 29.213 43.082  1.00 24.61 ? 629 HOH B O   1 
HETATM 8798 O O   . HOH H 4 .   ? -48.608 41.714 6.152   1.00 39.88 ? 630 HOH B O   1 
HETATM 8799 O O   . HOH H 4 .   ? -58.534 27.722 20.199  1.00 38.59 ? 631 HOH B O   1 
HETATM 8800 O O   . HOH H 4 .   ? -40.224 42.045 12.796  1.00 23.67 ? 632 HOH B O   1 
HETATM 8801 O O   . HOH H 4 .   ? -12.663 48.665 21.236  1.00 27.00 ? 633 HOH B O   1 
HETATM 8802 O O   . HOH H 4 .   ? -14.879 38.936 32.208  1.00 19.67 ? 634 HOH B O   1 
HETATM 8803 O O   . HOH H 4 .   ? -61.668 49.267 27.446  1.00 41.75 ? 635 HOH B O   1 
HETATM 8804 O O   . HOH H 4 .   ? -49.188 47.891 34.674  1.00 24.27 ? 636 HOH B O   1 
HETATM 8805 O O   . HOH H 4 .   ? -36.060 55.635 35.113  1.00 32.84 ? 637 HOH B O   1 
HETATM 8806 O O   . HOH H 4 .   ? -17.890 35.631 43.192  1.00 30.51 ? 638 HOH B O   1 
HETATM 8807 O O   . HOH H 4 .   ? -14.150 35.102 43.116  1.00 45.74 ? 639 HOH B O   1 
HETATM 8808 O O   . HOH H 4 .   ? -33.186 25.381 40.723  1.00 41.29 ? 640 HOH B O   1 
HETATM 8809 O O   . HOH H 4 .   ? -9.623  58.004 4.404   1.00 53.94 ? 641 HOH B O   1 
HETATM 8810 O O   . HOH H 4 .   ? -18.077 37.177 26.357  1.00 15.35 ? 642 HOH B O   1 
HETATM 8811 O O   . HOH H 4 .   ? -20.571 57.389 47.094  1.00 27.09 ? 643 HOH B O   1 
HETATM 8812 O O   . HOH H 4 .   ? -24.409 31.346 47.658  1.00 28.19 ? 644 HOH B O   1 
HETATM 8813 O O   . HOH H 4 .   ? 0.892   45.950 18.594  1.00 34.84 ? 645 HOH B O   1 
HETATM 8814 O O   . HOH H 4 .   ? -44.655 26.875 42.800  1.00 31.00 ? 646 HOH B O   1 
HETATM 8815 O O   . HOH H 4 .   ? -55.517 46.607 13.217  1.00 48.15 ? 647 HOH B O   1 
HETATM 8816 O O   . HOH H 4 .   ? -19.444 61.624 27.731  1.00 34.57 ? 648 HOH B O   1 
HETATM 8817 O O   . HOH H 4 .   ? -43.629 37.757 29.198  1.00 23.54 ? 649 HOH B O   1 
HETATM 8818 O O   . HOH H 4 .   ? -13.457 52.422 24.026  1.00 29.54 ? 650 HOH B O   1 
HETATM 8819 O O   . HOH H 4 .   ? -56.490 34.147 22.537  1.00 35.18 ? 651 HOH B O   1 
HETATM 8820 O O   . HOH H 4 .   ? -16.392 55.142 17.872  1.00 29.75 ? 652 HOH B O   1 
HETATM 8821 O O   . HOH H 4 .   ? -24.769 61.280 53.922  1.00 36.57 ? 653 HOH B O   1 
HETATM 8822 O O   . HOH H 4 .   ? -31.317 40.606 26.923  1.00 14.00 ? 654 HOH B O   1 
HETATM 8823 O O   . HOH H 4 .   ? -49.243 42.148 53.785  1.00 39.63 ? 655 HOH B O   1 
HETATM 8824 O O   . HOH H 4 .   ? -25.735 53.844 30.055  1.00 17.95 ? 656 HOH B O   1 
HETATM 8825 O O   . HOH H 4 .   ? -12.168 32.420 40.924  1.00 32.08 ? 657 HOH B O   1 
HETATM 8826 O O   . HOH H 4 .   ? -34.230 27.083 12.505  1.00 30.32 ? 658 HOH B O   1 
HETATM 8827 O O   . HOH H 4 .   ? -12.842 56.801 36.121  1.00 43.85 ? 659 HOH B O   1 
HETATM 8828 O O   . HOH H 4 .   ? -52.239 24.691 21.489  1.00 33.69 ? 660 HOH B O   1 
HETATM 8829 O O   . HOH H 4 .   ? -16.455 51.734 31.242  1.00 19.27 ? 661 HOH B O   1 
HETATM 8830 O O   . HOH H 4 .   ? -29.652 28.917 40.205  1.00 19.86 ? 662 HOH B O   1 
HETATM 8831 O O   . HOH H 4 .   ? -39.265 19.534 33.360  1.00 41.12 ? 663 HOH B O   1 
HETATM 8832 O O   . HOH H 4 .   ? -18.020 44.167 30.144  1.00 26.50 ? 664 HOH B O   1 
HETATM 8833 O O   . HOH H 4 .   ? -6.997  54.196 17.229  1.00 30.55 ? 665 HOH B O   1 
HETATM 8834 O O   . HOH H 4 .   ? -20.624 27.432 14.284  1.00 33.13 ? 666 HOH B O   1 
HETATM 8835 O O   . HOH H 4 .   ? -16.255 52.438 1.308   1.00 50.46 ? 667 HOH B O   1 
HETATM 8836 O O   . HOH H 4 .   ? -19.843 44.011 59.264  1.00 46.60 ? 668 HOH B O   1 
HETATM 8837 O O   . HOH H 4 .   ? -21.767 56.290 23.811  1.00 36.40 ? 669 HOH B O   1 
HETATM 8838 O O   . HOH H 4 .   ? -45.376 48.725 50.166  1.00 43.66 ? 670 HOH B O   1 
HETATM 8839 O O   . HOH H 4 .   ? -41.116 16.585 30.790  1.00 46.33 ? 671 HOH B O   1 
HETATM 8840 O O   . HOH H 4 .   ? -16.668 42.978 -4.184  1.00 36.93 ? 672 HOH B O   1 
HETATM 8841 O O   . HOH H 4 .   ? -3.278  38.228 4.344   1.00 30.70 ? 673 HOH B O   1 
HETATM 8842 O O   . HOH H 4 .   ? -21.380 22.942 27.541  1.00 39.41 ? 674 HOH B O   1 
HETATM 8843 O O   . HOH H 4 .   ? -1.250  40.264 23.302  1.00 36.19 ? 675 HOH B O   1 
HETATM 8844 O O   . HOH H 4 .   ? -21.319 40.784 4.830   1.00 33.25 ? 676 HOH B O   1 
HETATM 8845 O O   . HOH H 4 .   ? -42.475 42.191 57.215  1.00 29.61 ? 677 HOH B O   1 
HETATM 8846 O O   . HOH H 4 .   ? -22.256 56.280 21.062  1.00 41.56 ? 678 HOH B O   1 
HETATM 8847 O O   . HOH H 4 .   ? -33.660 28.884 38.793  1.00 27.51 ? 679 HOH B O   1 
HETATM 8848 O O   . HOH H 4 .   ? -18.560 23.235 24.209  1.00 41.16 ? 680 HOH B O   1 
HETATM 8849 O O   . HOH H 4 .   ? -41.463 52.768 31.857  1.00 42.39 ? 681 HOH B O   1 
HETATM 8850 O O   . HOH H 4 .   ? -46.056 35.649 6.100   1.00 42.29 ? 682 HOH B O   1 
HETATM 8851 O O   . HOH H 4 .   ? -5.879  50.605 18.833  1.00 37.99 ? 683 HOH B O   1 
HETATM 8852 O O   . HOH H 4 .   ? -52.368 27.159 22.490  1.00 23.94 ? 684 HOH B O   1 
HETATM 8853 O O   . HOH H 4 .   ? -57.976 37.424 39.379  1.00 44.15 ? 685 HOH B O   1 
HETATM 8854 O O   . HOH H 4 .   ? -1.593  36.134 21.242  1.00 51.30 ? 686 HOH B O   1 
HETATM 8855 O O   . HOH H 4 .   ? -50.467 52.825 30.090  1.00 39.27 ? 687 HOH B O   1 
HETATM 8856 O O   . HOH H 4 .   ? -46.971 54.612 26.550  1.00 43.28 ? 688 HOH B O   1 
HETATM 8857 O O   . HOH H 4 .   ? -9.652  43.526 29.894  1.00 31.97 ? 689 HOH B O   1 
HETATM 8858 O O   . HOH H 4 .   ? -52.416 44.020 47.331  1.00 44.63 ? 690 HOH B O   1 
HETATM 8859 O O   . HOH H 4 .   ? -4.561  51.963 3.371   1.00 37.07 ? 691 HOH B O   1 
HETATM 8860 O O   . HOH H 4 .   ? -25.449 52.286 27.737  1.00 16.78 ? 692 HOH B O   1 
HETATM 8861 O O   . HOH H 4 .   ? -17.960 59.641 -6.783  1.00 51.76 ? 693 HOH B O   1 
HETATM 8862 O O   . HOH H 4 .   ? 1.664   42.900 9.107   1.00 44.47 ? 694 HOH B O   1 
HETATM 8863 O O   . HOH H 4 .   ? -30.096 22.370 20.999  1.00 44.07 ? 695 HOH B O   1 
HETATM 8864 O O   . HOH H 4 .   ? -4.404  31.619 6.371   1.00 40.21 ? 696 HOH B O   1 
HETATM 8865 O O   . HOH H 4 .   ? -43.599 55.343 24.486  1.00 58.27 ? 697 HOH B O   1 
HETATM 8866 O O   . HOH H 4 .   ? -36.626 21.573 25.980  1.00 32.38 ? 698 HOH B O   1 
HETATM 8867 O O   . HOH H 4 .   ? -32.885 21.715 22.446  1.00 38.31 ? 699 HOH B O   1 
HETATM 8868 O O   . HOH H 4 .   ? -39.871 44.974 59.009  1.00 37.52 ? 700 HOH B O   1 
HETATM 8869 O O   . HOH H 4 .   ? -24.533 46.025 60.413  1.00 49.08 ? 701 HOH B O   1 
HETATM 8870 O O   . HOH H 4 .   ? -53.190 44.805 44.931  1.00 39.68 ? 702 HOH B O   1 
HETATM 8871 O O   . HOH H 4 .   ? -54.876 38.409 34.633  1.00 31.45 ? 703 HOH B O   1 
HETATM 8872 O O   . HOH H 4 .   ? -35.536 49.481 19.279  1.00 41.57 ? 704 HOH B O   1 
HETATM 8873 O O   . HOH H 4 .   ? -20.301 30.596 9.601   1.00 44.97 ? 705 HOH B O   1 
HETATM 8874 O O   . HOH H 4 .   ? -60.675 42.613 16.573  1.00 39.37 ? 706 HOH B O   1 
HETATM 8875 O O   . HOH H 4 .   ? -51.197 52.611 13.399  1.00 48.02 ? 707 HOH B O   1 
HETATM 8876 O O   . HOH H 4 .   ? -22.748 32.542 50.242  1.00 47.12 ? 708 HOH B O   1 
HETATM 8877 O O   . HOH H 4 .   ? -42.605 20.180 16.903  1.00 39.77 ? 709 HOH B O   1 
HETATM 8878 O O   . HOH H 4 .   ? -6.657  45.145 -3.977  1.00 41.67 ? 710 HOH B O   1 
HETATM 8879 O O   . HOH H 4 .   ? -37.252 33.332 18.815  1.00 18.56 ? 711 HOH B O   1 
HETATM 8880 O O   . HOH H 4 .   ? -4.191  31.367 25.711  1.00 47.95 ? 712 HOH B O   1 
HETATM 8881 O O   . HOH H 4 .   ? -55.225 38.750 32.676  1.00 39.46 ? 713 HOH B O   1 
HETATM 8882 O O   . HOH H 4 .   ? -26.567 53.575 18.168  1.00 44.23 ? 714 HOH B O   1 
HETATM 8883 O O   . HOH H 4 .   ? -2.242  42.202 4.810   1.00 50.24 ? 715 HOH B O   1 
HETATM 8884 O O   . HOH H 4 .   ? -15.677 27.891 31.485  1.00 34.66 ? 716 HOH B O   1 
HETATM 8885 O O   . HOH H 4 .   ? -2.092  51.602 6.537   1.00 53.05 ? 717 HOH B O   1 
HETATM 8886 O O   . HOH H 4 .   ? -15.806 53.867 44.808  1.00 46.63 ? 718 HOH B O   1 
HETATM 8887 O O   . HOH H 4 .   ? -11.838 49.912 23.433  1.00 43.70 ? 719 HOH B O   1 
HETATM 8888 O O   . HOH H 4 .   ? -14.704 55.790 32.008  1.00 34.56 ? 720 HOH B O   1 
HETATM 8889 O O   . HOH H 4 .   ? -9.405  35.896 42.163  1.00 57.18 ? 721 HOH B O   1 
HETATM 8890 O O   . HOH H 4 .   ? -23.857 22.451 26.455  1.00 44.96 ? 722 HOH B O   1 
HETATM 8891 O O   . HOH H 4 .   ? -16.806 33.805 -3.951  1.00 50.42 ? 723 HOH B O   1 
HETATM 8892 O O   . HOH H 4 .   ? -14.940 65.722 43.651  1.00 51.16 ? 724 HOH B O   1 
HETATM 8893 O O   . HOH H 4 .   ? -37.672 23.456 21.078  1.00 47.67 ? 725 HOH B O   1 
HETATM 8894 O O   . HOH H 4 .   ? -2.622  49.044 28.432  1.00 47.50 ? 726 HOH B O   1 
HETATM 8895 O O   . HOH H 4 .   ? -38.913 23.626 39.968  1.00 48.02 ? 727 HOH B O   1 
HETATM 8896 O O   . HOH H 4 .   ? -24.814 53.863 54.888  1.00 56.44 ? 728 HOH B O   1 
HETATM 8897 O O   . HOH H 4 .   ? -44.688 42.399 57.608  1.00 43.41 ? 729 HOH B O   1 
HETATM 8898 O O   . HOH H 4 .   ? -24.744 57.260 23.037  1.00 53.37 ? 730 HOH B O   1 
HETATM 8899 O O   . HOH H 4 .   ? -36.204 55.071 43.123  1.00 42.30 ? 731 HOH B O   1 
HETATM 8900 O O   . HOH H 4 .   ? -37.828 15.337 37.382  1.00 39.82 ? 732 HOH B O   1 
HETATM 8901 O O   . HOH H 4 .   ? -21.631 53.135 55.402  1.00 44.52 ? 733 HOH B O   1 
HETATM 8902 O O   . HOH H 4 .   ? -33.513 57.009 48.438  1.00 45.95 ? 734 HOH B O   1 
HETATM 8903 O O   . HOH H 4 .   ? -31.608 37.975 4.975   1.00 37.34 ? 735 HOH B O   1 
HETATM 8904 O O   . HOH H 4 .   ? -10.904 48.874 39.528  1.00 41.30 ? 736 HOH B O   1 
HETATM 8905 O O   . HOH H 4 .   ? -37.244 17.916 32.673  1.00 40.65 ? 737 HOH B O   1 
HETATM 8906 O O   . HOH H 4 .   ? -17.245 54.169 31.775  1.00 23.36 ? 738 HOH B O   1 
HETATM 8907 O O   . HOH H 4 .   ? -11.384 50.494 21.486  1.00 44.39 ? 739 HOH B O   1 
HETATM 8908 O O   . HOH H 4 .   ? -13.765 39.907 49.829  1.00 36.33 ? 740 HOH B O   1 
HETATM 8909 O O   . HOH H 4 .   ? -34.472 19.947 26.312  1.00 39.53 ? 741 HOH B O   1 
HETATM 8910 O O   . HOH H 4 .   ? -53.046 25.139 29.341  1.00 50.93 ? 742 HOH B O   1 
HETATM 8911 O O   . HOH H 4 .   ? -32.197 27.822 40.922  1.00 33.80 ? 743 HOH B O   1 
HETATM 8912 O O   . HOH H 4 .   ? -36.777 21.585 23.146  1.00 49.97 ? 744 HOH B O   1 
HETATM 8913 O O   . HOH H 4 .   ? -39.367 23.266 44.342  1.00 43.38 ? 745 HOH B O   1 
HETATM 8914 O O   . HOH H 4 .   ? -27.119 22.573 17.724  1.00 41.86 ? 746 HOH B O   1 
HETATM 8915 O O   . HOH H 4 .   ? -37.738 53.332 19.154  1.00 54.39 ? 747 HOH B O   1 
HETATM 8916 O O   . HOH H 4 .   ? -22.717 46.748 58.669  1.00 34.73 ? 748 HOH B O   1 
HETATM 8917 O O   . HOH H 4 .   ? -14.373 25.797 30.667  1.00 46.72 ? 749 HOH B O   1 
HETATM 8918 O O   . HOH H 4 .   ? -6.126  51.788 16.917  1.00 44.20 ? 750 HOH B O   1 
HETATM 8919 O O   . HOH H 4 .   ? -9.472  46.430 28.783  1.00 49.21 ? 751 HOH B O   1 
HETATM 8920 O O   . HOH H 4 .   ? -31.532 46.130 21.492  1.00 35.91 ? 752 HOH B O   1 
HETATM 8921 O O   . HOH H 4 .   ? -27.419 29.007 45.299  1.00 40.99 ? 753 HOH B O   1 
HETATM 8922 O O   . HOH H 4 .   ? -34.324 44.682 60.653  1.00 40.24 ? 754 HOH B O   1 
HETATM 8923 O O   . HOH H 4 .   ? -24.549 54.772 18.168  1.00 33.99 ? 755 HOH B O   1 
HETATM 8924 O O   . HOH H 4 .   ? -34.723 46.586 23.664  1.00 32.77 ? 756 HOH B O   1 
HETATM 8925 O O   . HOH H 4 .   ? -9.556  46.678 39.490  1.00 49.44 ? 757 HOH B O   1 
HETATM 8926 O O   . HOH H 4 .   ? -9.160  47.069 31.009  1.00 51.56 ? 758 HOH B O   1 
HETATM 8927 O O   . HOH H 4 .   ? -49.593 52.665 20.143  1.00 46.43 ? 759 HOH B O   1 
HETATM 8928 O O   . HOH H 4 .   ? -24.445 16.076 20.123  1.00 36.69 ? 760 HOH B O   1 
HETATM 8929 O O   . HOH H 4 .   ? -21.816 24.165 24.506  1.00 30.53 ? 761 HOH B O   1 
HETATM 8930 O O   . HOH H 4 .   ? -12.052 55.217 32.903  1.00 54.83 ? 762 HOH B O   1 
HETATM 8931 O O   . HOH H 4 .   ? -37.177 55.037 17.766  1.00 54.63 ? 763 HOH B O   1 
HETATM 8932 O O   . HOH H 4 .   ? -26.962 56.437 21.650  1.00 58.49 ? 764 HOH B O   1 
HETATM 8933 O O   . HOH H 4 .   ? -41.725 17.575 8.036   1.00 47.16 ? 765 HOH B O   1 
HETATM 8934 O O   . HOH H 4 .   ? -31.738 48.154 20.502  1.00 38.94 ? 766 HOH B O   1 
HETATM 8935 O O   . HOH H 4 .   ? -35.156 51.421 24.815  1.00 33.59 ? 767 HOH B O   1 
HETATM 8936 O O   . HOH H 4 .   ? -33.584 53.110 23.587  1.00 41.26 ? 768 HOH B O   1 
HETATM 8937 O O   . HOH H 4 .   ? -33.523 56.085 23.457  1.00 46.61 ? 769 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   ? 0.4973 0.6568 0.3992 0.0076  0.0290  0.0633  2   LYS A N   
2    C CA  . LYS A 2   ? 0.3624 0.5004 0.2732 0.0046  0.0321  0.0620  2   LYS A CA  
3    C C   . LYS A 2   ? 0.3156 0.4409 0.2342 0.0052  0.0289  0.0604  2   LYS A C   
4    O O   . LYS A 2   ? 0.4063 0.5276 0.3257 0.0097  0.0287  0.0698  2   LYS A O   
5    C CB  . LYS A 2   ? 0.4781 0.6077 0.3886 0.0060  0.0383  0.0744  2   LYS A CB  
6    C CG  . LYS A 2   ? 0.5021 0.6117 0.4218 0.0020  0.0417  0.0722  2   LYS A CG  
7    C CD  . LYS A 2   ? 0.6358 0.7368 0.5559 0.0030  0.0481  0.0846  2   LYS A CD  
8    C CE  . LYS A 2   ? 0.6603 0.7549 0.5812 0.0085  0.0482  0.0963  2   LYS A CE  
9    N NZ  . LYS A 2   ? 0.6600 0.7407 0.5843 0.0084  0.0550  0.1070  2   LYS A NZ  
10   N N   . LYS A 3   ? 0.2360 0.3550 0.1603 0.0011  0.0266  0.0487  3   LYS A N   
11   C CA  . LYS A 3   ? 0.2357 0.3442 0.1670 0.0012  0.0234  0.0458  3   LYS A CA  
12   C C   . LYS A 3   ? 0.2588 0.3477 0.1980 -0.0010 0.0263  0.0460  3   LYS A C   
13   O O   . LYS A 3   ? 0.3040 0.3882 0.2445 -0.0039 0.0299  0.0446  3   LYS A O   
14   C CB  . LYS A 3   ? 0.3392 0.4537 0.2720 -0.0019 0.0189  0.0331  3   LYS A CB  
15   C CG  . LYS A 3   ? 0.4137 0.5491 0.3392 -0.0011 0.0159  0.0298  3   LYS A CG  
16   C CD  . LYS A 3   ? 0.4938 0.6362 0.4192 0.0022  0.0116  0.0327  3   LYS A CD  
17   C CE  . LYS A 3   ? 0.4515 0.6144 0.3719 0.0012  0.0077  0.0252  3   LYS A CE  
18   N NZ  . LYS A 3   ? 0.5191 0.6851 0.4435 0.0018  0.0031  0.0225  3   LYS A NZ  
19   N N   . LEU A 4   ? 0.2420 0.3207 0.1866 0.0004  0.0248  0.0477  4   LEU A N   
20   C CA  . LEU A 4   ? 0.2376 0.2996 0.1902 -0.0023 0.0259  0.0445  4   LEU A CA  
21   C C   . LEU A 4   ? 0.2377 0.2996 0.1938 -0.0049 0.0217  0.0339  4   LEU A C   
22   O O   . LEU A 4   ? 0.2227 0.2901 0.1784 -0.0032 0.0180  0.0325  4   LEU A O   
23   C CB  . LEU A 4   ? 0.2360 0.2868 0.1924 0.0009  0.0274  0.0526  4   LEU A CB  
24   C CG  . LEU A 4   ? 0.2065 0.2412 0.1710 -0.0020 0.0286  0.0490  4   LEU A CG  
25   C CD1 . LEU A 4   ? 0.2756 0.2984 0.2432 0.0000  0.0329  0.0578  4   LEU A CD1 
26   C CD2 . LEU A 4   ? 0.2242 0.2566 0.1927 -0.0024 0.0242  0.0424  4   LEU A CD2 
27   N N   . PHE A 5   ? 0.2118 0.2675 0.1718 -0.0088 0.0225  0.0267  5   PHE A N   
28   C CA  . PHE A 5   ? 0.1571 0.2114 0.1208 -0.0113 0.0192  0.0172  5   PHE A CA  
29   C C   . PHE A 5   ? 0.1735 0.2144 0.1439 -0.0117 0.0189  0.0174  5   PHE A C   
30   O O   . PHE A 5   ? 0.2896 0.3211 0.2637 -0.0131 0.0216  0.0183  5   PHE A O   
31   C CB  . PHE A 5   ? 0.2366 0.2923 0.2010 -0.0147 0.0204  0.0096  5   PHE A CB  
32   C CG  . PHE A 5   ? 0.2392 0.3093 0.1970 -0.0147 0.0205  0.0071  5   PHE A CG  
33   C CD1 . PHE A 5   ? 0.2471 0.3288 0.2007 -0.0135 0.0173  0.0057  5   PHE A CD1 
34   C CD2 . PHE A 5   ? 0.2126 0.2859 0.1688 -0.0161 0.0239  0.0056  5   PHE A CD2 
35   C CE1 . PHE A 5   ? 0.3115 0.4078 0.2587 -0.0138 0.0173  0.0025  5   PHE A CE1 
36   C CE2 . PHE A 5   ? 0.2561 0.3436 0.2058 -0.0162 0.0242  0.0027  5   PHE A CE2 
37   C CZ  . PHE A 5   ? 0.2467 0.3459 0.1918 -0.0151 0.0208  0.0009  5   PHE A CZ  
38   N N   . LEU A 6   ? 0.2381 0.2793 0.2100 -0.0105 0.0156  0.0163  6   LEU A N   
39   C CA  . LEU A 6   ? 0.2414 0.2718 0.2188 -0.0104 0.0151  0.0168  6   LEU A CA  
40   C C   . LEU A 6   ? 0.1897 0.2183 0.1705 -0.0131 0.0124  0.0086  6   LEU A C   
41   O O   . LEU A 6   ? 0.1984 0.2350 0.1777 -0.0136 0.0098  0.0046  6   LEU A O   
42   C CB  . LEU A 6   ? 0.1910 0.2234 0.1675 -0.0064 0.0139  0.0227  6   LEU A CB  
43   C CG  . LEU A 6   ? 0.1852 0.2075 0.1671 -0.0056 0.0137  0.0235  6   LEU A CG  
44   C CD1 . LEU A 6   ? 0.2388 0.2491 0.2239 -0.0066 0.0175  0.0258  6   LEU A CD1 
45   C CD2 . LEU A 6   ? 0.1876 0.2142 0.1685 -0.0009 0.0127  0.0294  6   LEU A CD2 
46   N N   . VAL A 7   ? 0.1321 0.1510 0.1178 -0.0150 0.0132  0.0062  7   VAL A N   
47   C CA  . VAL A 7   ? 0.1278 0.1443 0.1169 -0.0173 0.0112  -0.0005 7   VAL A CA  
48   C C   . VAL A 7   ? 0.1856 0.1937 0.1789 -0.0170 0.0106  0.0003  7   VAL A C   
49   O O   . VAL A 7   ? 0.2320 0.2332 0.2280 -0.0177 0.0125  0.0012  7   VAL A O   
50   C CB  . VAL A 7   ? 0.1963 0.2111 0.1869 -0.0195 0.0126  -0.0049 7   VAL A CB  
51   C CG1 . VAL A 7   ? 0.2683 0.2816 0.2620 -0.0212 0.0107  -0.0113 7   VAL A CG1 
52   C CG2 . VAL A 7   ? 0.2133 0.2362 0.1994 -0.0195 0.0142  -0.0049 7   VAL A CG2 
53   N N   . PHE A 8   ? 0.1767 0.1865 0.1707 -0.0164 0.0082  -0.0005 8   PHE A N   
54   C CA  . PHE A 8   ? 0.1403 0.1437 0.1381 -0.0165 0.0076  -0.0007 8   PHE A CA  
55   C C   . PHE A 8   ? 0.1725 0.1732 0.1731 -0.0190 0.0066  -0.0059 8   PHE A C   
56   O O   . PHE A 8   ? 0.1727 0.1774 0.1728 -0.0204 0.0054  -0.0096 8   PHE A O   
57   C CB  . PHE A 8   ? 0.1617 0.1689 0.1595 -0.0147 0.0057  0.0008  8   PHE A CB  
58   C CG  . PHE A 8   ? 0.2102 0.2184 0.2064 -0.0112 0.0068  0.0069  8   PHE A CG  
59   C CD1 . PHE A 8   ? 0.1868 0.1874 0.1856 -0.0096 0.0085  0.0097  8   PHE A CD1 
60   C CD2 . PHE A 8   ? 0.2386 0.2558 0.2310 -0.0092 0.0063  0.0097  8   PHE A CD2 
61   C CE1 . PHE A 8   ? 0.2084 0.2087 0.2064 -0.0059 0.0101  0.0157  8   PHE A CE1 
62   C CE2 . PHE A 8   ? 0.1887 0.2070 0.1799 -0.0051 0.0075  0.0163  8   PHE A CE2 
63   C CZ  . PHE A 8   ? 0.1911 0.2002 0.1854 -0.0033 0.0095  0.0195  8   PHE A CZ  
64   N N   . TRP A 9   ? 0.1384 0.1324 0.1420 -0.0196 0.0071  -0.0062 9   TRP A N   
65   C CA  . TRP A 9   ? 0.1340 0.1255 0.1404 -0.0212 0.0062  -0.0099 9   TRP A CA  
66   C C   . TRP A 9   ? 0.1750 0.1627 0.1835 -0.0209 0.0057  -0.0090 9   TRP A C   
67   O O   . TRP A 9   ? 0.1539 0.1380 0.1638 -0.0209 0.0068  -0.0082 9   TRP A O   
68   C CB  . TRP A 9   ? 0.1637 0.1536 0.1714 -0.0221 0.0076  -0.0116 9   TRP A CB  
69   C CG  . TRP A 9   ? 0.1841 0.1727 0.1944 -0.0230 0.0068  -0.0150 9   TRP A CG  
70   C CD1 . TRP A 9   ? 0.2062 0.1935 0.2180 -0.0234 0.0053  -0.0162 9   TRP A CD1 
71   C CD2 . TRP A 9   ? 0.1931 0.1814 0.2054 -0.0233 0.0078  -0.0171 9   TRP A CD2 
72   N NE1 . TRP A 9   ? 0.1773 0.1626 0.1918 -0.0237 0.0055  -0.0185 9   TRP A NE1 
73   C CE2 . TRP A 9   ? 0.1757 0.1619 0.1906 -0.0233 0.0069  -0.0192 9   TRP A CE2 
74   C CE3 . TRP A 9   ? 0.1878 0.1776 0.2001 -0.0234 0.0097  -0.0172 9   TRP A CE3 
75   C CZ2 . TRP A 9   ? 0.1933 0.1789 0.2112 -0.0229 0.0076  -0.0213 9   TRP A CZ2 
76   C CZ3 . TRP A 9   ? 0.2555 0.2457 0.2708 -0.0233 0.0103  -0.0198 9   TRP A CZ3 
77   C CH2 . TRP A 9   ? 0.2126 0.2005 0.2307 -0.0227 0.0092  -0.0218 9   TRP A CH2 
78   N N   . TRP A 10  ? 0.1627 0.1519 0.1716 -0.0210 0.0042  -0.0095 10  TRP A N   
79   C CA  . TRP A 10  ? 0.1617 0.1490 0.1721 -0.0206 0.0038  -0.0087 10  TRP A CA  
80   C C   . TRP A 10  ? 0.1415 0.1266 0.1539 -0.0219 0.0031  -0.0106 10  TRP A C   
81   O O   . TRP A 10  ? 0.1955 0.1814 0.2086 -0.0230 0.0024  -0.0120 10  TRP A O   
82   C CB  . TRP A 10  ? 0.1640 0.1554 0.1740 -0.0199 0.0027  -0.0080 10  TRP A CB  
83   C CG  . TRP A 10  ? 0.1553 0.1504 0.1634 -0.0177 0.0030  -0.0053 10  TRP A CG  
84   C CD1 . TRP A 10  ? 0.2029 0.2048 0.2094 -0.0175 0.0020  -0.0052 10  TRP A CD1 
85   C CD2 . TRP A 10  ? 0.1600 0.1526 0.1681 -0.0152 0.0044  -0.0021 10  TRP A CD2 
86   N NE1 . TRP A 10  ? 0.1456 0.1502 0.1506 -0.0144 0.0025  -0.0013 10  TRP A NE1 
87   C CE2 . TRP A 10  ? 0.1456 0.1436 0.1519 -0.0129 0.0042  0.0008  10  TRP A CE2 
88   C CE3 . TRP A 10  ? 0.1478 0.1344 0.1574 -0.0147 0.0060  -0.0017 10  TRP A CE3 
89   C CZ2 . TRP A 10  ? 0.1529 0.1492 0.1591 -0.0096 0.0059  0.0050  10  TRP A CZ2 
90   C CZ3 . TRP A 10  ? 0.1593 0.1435 0.1692 -0.0120 0.0079  0.0015  10  TRP A CZ3 
91   C CH2 . TRP A 10  ? 0.1422 0.1307 0.1505 -0.0092 0.0079  0.0053  10  TRP A CH2 
92   N N   . HIS A 11  ? 0.1376 0.1201 0.1511 -0.0218 0.0036  -0.0105 11  HIS A N   
93   C CA  . HIS A 11  ? 0.1214 0.1030 0.1365 -0.0224 0.0030  -0.0114 11  HIS A CA  
94   C C   . HIS A 11  ? 0.1519 0.1342 0.1671 -0.0223 0.0023  -0.0107 11  HIS A C   
95   O O   . HIS A 11  ? 0.1826 0.1652 0.1975 -0.0218 0.0027  -0.0105 11  HIS A O   
96   C CB  . HIS A 11  ? 0.1313 0.1121 0.1476 -0.0224 0.0036  -0.0121 11  HIS A CB  
97   C CG  . HIS A 11  ? 0.1344 0.1162 0.1520 -0.0224 0.0027  -0.0125 11  HIS A CG  
98   N ND1 . HIS A 11  ? 0.1700 0.1522 0.1888 -0.0220 0.0019  -0.0122 11  HIS A ND1 
99   C CD2 . HIS A 11  ? 0.1876 0.1708 0.2056 -0.0226 0.0026  -0.0131 11  HIS A CD2 
100  C CE1 . HIS A 11  ? 0.1553 0.1396 0.1748 -0.0215 0.0011  -0.0117 11  HIS A CE1 
101  N NE2 . HIS A 11  ? 0.1422 0.1278 0.1610 -0.0221 0.0014  -0.0127 11  HIS A NE2 
102  N N   . MET A 12  ? 0.1365 0.1190 0.1524 -0.0229 0.0016  -0.0104 12  MET A N   
103  C CA  . MET A 12  ? 0.1118 0.0957 0.1278 -0.0231 0.0013  -0.0091 12  MET A CA  
104  C C   . MET A 12  ? 0.2050 0.1886 0.2217 -0.0228 0.0010  -0.0081 12  MET A C   
105  O O   . MET A 12  ? 0.1579 0.1394 0.1761 -0.0227 0.0010  -0.0078 12  MET A O   
106  C CB  . MET A 12  ? 0.1050 0.0898 0.1217 -0.0244 0.0013  -0.0090 12  MET A CB  
107  C CG  . MET A 12  ? 0.1225 0.1094 0.1385 -0.0245 0.0012  -0.0100 12  MET A CG  
108  S SD  . MET A 12  ? 0.1582 0.1474 0.1730 -0.0225 0.0015  -0.0090 12  MET A SD  
109  C CE  . MET A 12  ? 0.1851 0.1793 0.1996 -0.0224 0.0010  -0.0090 12  MET A CE  
110  N N   . HIS A 13  ? 0.1562 0.1424 0.1720 -0.0223 0.0008  -0.0074 13  HIS A N   
111  C CA  . HIS A 13  ? 0.1558 0.1436 0.1717 -0.0216 0.0002  -0.0058 13  HIS A CA  
112  C C   . HIS A 13  ? 0.1270 0.1189 0.1411 -0.0215 0.0001  -0.0049 13  HIS A C   
113  O O   . HIS A 13  ? 0.1469 0.1404 0.1600 -0.0216 0.0005  -0.0068 13  HIS A O   
114  C CB  . HIS A 13  ? 0.1278 0.1168 0.1444 -0.0209 -0.0003 -0.0075 13  HIS A CB  
115  C CG  . HIS A 13  ? 0.1475 0.1409 0.1641 -0.0197 -0.0013 -0.0061 13  HIS A CG  
116  N ND1 . HIS A 13  ? 0.1502 0.1432 0.1676 -0.0184 -0.0016 -0.0026 13  HIS A ND1 
117  C CD2 . HIS A 13  ? 0.1801 0.1788 0.1960 -0.0196 -0.0021 -0.0077 13  HIS A CD2 
118  C CE1 . HIS A 13  ? 0.1489 0.1476 0.1657 -0.0170 -0.0027 -0.0013 13  HIS A CE1 
119  N NE2 . HIS A 13  ? 0.1740 0.1770 0.1899 -0.0179 -0.0032 -0.0049 13  HIS A NE2 
120  N N   . GLN A 14  ? 0.1133 0.1071 0.1269 -0.0209 -0.0001 -0.0018 14  GLN A N   
121  C CA  . GLN A 14  ? 0.1276 0.1275 0.1389 -0.0204 -0.0003 -0.0009 14  GLN A CA  
122  C C   . GLN A 14  ? 0.1486 0.1512 0.1598 -0.0187 -0.0013 0.0024  14  GLN A C   
123  O O   . GLN A 14  ? 0.1725 0.1711 0.1856 -0.0180 -0.0009 0.0056  14  GLN A O   
124  C CB  . GLN A 14  ? 0.1734 0.1747 0.1836 -0.0213 0.0008  0.0012  14  GLN A CB  
125  C CG  . GLN A 14  ? 0.1505 0.1510 0.1611 -0.0223 0.0017  -0.0015 14  GLN A CG  
126  C CD  . GLN A 14  ? 0.1933 0.1965 0.2027 -0.0217 0.0017  -0.0053 14  GLN A CD  
127  O OE1 . GLN A 14  ? 0.1643 0.1720 0.1720 -0.0212 0.0014  -0.0065 14  GLN A OE1 
128  N NE2 . GLN A 14  ? 0.1804 0.1810 0.1910 -0.0216 0.0023  -0.0075 14  GLN A NE2 
129  N N   . PRO A 15  ? 0.1656 0.1754 0.1749 -0.0179 -0.0023 0.0015  15  PRO A N   
130  C CA  . PRO A 15  ? 0.1573 0.1720 0.1660 -0.0157 -0.0034 0.0056  15  PRO A CA  
131  C C   . PRO A 15  ? 0.1160 0.1316 0.1228 -0.0153 -0.0023 0.0111  15  PRO A C   
132  O O   . PRO A 15  ? 0.1887 0.2031 0.1945 -0.0170 -0.0009 0.0108  15  PRO A O   
133  C CB  . PRO A 15  ? 0.1728 0.1968 0.1796 -0.0156 -0.0048 0.0021  15  PRO A CB  
134  C CG  . PRO A 15  ? 0.1433 0.1674 0.1485 -0.0177 -0.0038 -0.0024 15  PRO A CG  
135  C CD  . PRO A 15  ? 0.1505 0.1648 0.1583 -0.0188 -0.0025 -0.0034 15  PRO A CD  
136  N N   . LEU A 16  ? 0.1887 0.2068 0.1953 -0.0128 -0.0028 0.0166  16  LEU A N   
137  C CA  . LEU A 16  ? 0.1965 0.2144 0.2018 -0.0123 -0.0012 0.0231  16  LEU A CA  
138  C C   . LEU A 16  ? 0.2226 0.2505 0.2230 -0.0126 -0.0013 0.0233  16  LEU A C   
139  O O   . LEU A 16  ? 0.1799 0.2176 0.1775 -0.0107 -0.0030 0.0239  16  LEU A O   
140  C CB  . LEU A 16  ? 0.2036 0.2204 0.2106 -0.0089 -0.0013 0.0298  16  LEU A CB  
141  C CG  . LEU A 16  ? 0.1660 0.1806 0.1724 -0.0084 0.0010  0.0376  16  LEU A CG  
142  C CD1 . LEU A 16  ? 0.1529 0.1576 0.1619 -0.0121 0.0035  0.0362  16  LEU A CD1 
143  C CD2 . LEU A 16  ? 0.2148 0.2271 0.2235 -0.0042 0.0012  0.0449  16  LEU A CD2 
144  N N   . TYR A 17  ? 0.2068 0.2336 0.2062 -0.0150 0.0006  0.0228  17  TYR A N   
145  C CA  . TYR A 17  ? 0.1811 0.2176 0.1760 -0.0153 0.0010  0.0227  17  TYR A CA  
146  C C   . TYR A 17  ? 0.1721 0.2122 0.1645 -0.0142 0.0025  0.0310  17  TYR A C   
147  O O   . TYR A 17  ? 0.2122 0.2618 0.2002 -0.0143 0.0030  0.0315  17  TYR A O   
148  C CB  . TYR A 17  ? 0.2162 0.2509 0.2115 -0.0180 0.0026  0.0179  17  TYR A CB  
149  C CG  . TYR A 17  ? 0.1842 0.2160 0.1814 -0.0187 0.0016  0.0104  17  TYR A CG  
150  C CD1 . TYR A 17  ? 0.1886 0.2267 0.1840 -0.0181 0.0001  0.0055  17  TYR A CD1 
151  C CD2 . TYR A 17  ? 0.1460 0.1694 0.1468 -0.0201 0.0022  0.0083  17  TYR A CD2 
152  C CE1 . TYR A 17  ? 0.1918 0.2261 0.1893 -0.0190 -0.0002 -0.0009 17  TYR A CE1 
153  C CE2 . TYR A 17  ? 0.1208 0.1413 0.1230 -0.0204 0.0016  0.0026  17  TYR A CE2 
154  C CZ  . TYR A 17  ? 0.2168 0.2421 0.2175 -0.0199 0.0006  -0.0017 17  TYR A CZ  
155  O OH  . TYR A 17  ? 0.1700 0.1915 0.1726 -0.0204 0.0006  -0.0068 17  TYR A OH  
156  N N   . ARG A 18  ? 0.1796 0.2127 0.1749 -0.0131 0.0034  0.0374  18  ARG A N   
157  C CA  . ARG A 18  ? 0.1831 0.2174 0.1768 -0.0122 0.0056  0.0465  18  ARG A CA  
158  C C   . ARG A 18  ? 0.2343 0.2781 0.2244 -0.0079 0.0037  0.0515  18  ARG A C   
159  O O   . ARG A 18  ? 0.2064 0.2476 0.1990 -0.0049 0.0023  0.0537  18  ARG A O   
160  C CB  . ARG A 18  ? 0.1840 0.2051 0.1832 -0.0130 0.0080  0.0509  18  ARG A CB  
161  C CG  . ARG A 18  ? 0.2222 0.2423 0.2209 -0.0126 0.0111  0.0608  18  ARG A CG  
162  C CD  . ARG A 18  ? 0.2397 0.2452 0.2449 -0.0133 0.0137  0.0644  18  ARG A CD  
163  N NE  . ARG A 18  ? 0.2581 0.2608 0.2639 -0.0137 0.0175  0.0739  18  ARG A NE  
164  C CZ  . ARG A 18  ? 0.3628 0.3676 0.3668 -0.0095 0.0183  0.0834  18  ARG A CZ  
165  N NH1 . ARG A 18  ? 0.3439 0.3551 0.3455 -0.0043 0.0150  0.0846  18  ARG A NH1 
166  N NH2 . ARG A 18  ? 0.4288 0.4297 0.4337 -0.0103 0.0224  0.0923  18  ARG A NH2 
167  N N   . GLU A 19  ? 0.1963 0.2523 0.1807 -0.0075 0.0038  0.0534  19  GLU A N   
168  C CA  . GLU A 19  ? 0.2784 0.3464 0.2585 -0.0035 0.0019  0.0585  19  GLU A CA  
169  C C   . GLU A 19  ? 0.2881 0.3511 0.2695 -0.0005 0.0039  0.0704  19  GLU A C   
170  O O   . GLU A 19  ? 0.2864 0.3430 0.2687 -0.0024 0.0075  0.0755  19  GLU A O   
171  C CB  . GLU A 19  ? 0.2577 0.3404 0.2309 -0.0042 0.0020  0.0569  19  GLU A CB  
172  C CG  . GLU A 19  ? 0.3364 0.4352 0.3048 -0.0012 -0.0014 0.0559  19  GLU A CG  
173  C CD  . GLU A 19  ? 0.3989 0.5063 0.3632 0.0029  -0.0010 0.0676  19  GLU A CD  
174  O OE1 . GLU A 19  ? 0.3731 0.4719 0.3388 0.0032  0.0022  0.0766  19  GLU A OE1 
175  O OE2 . GLU A 19  ? 0.4199 0.5427 0.3798 0.0057  -0.0039 0.0679  19  GLU A OE2 
176  N N   . PRO A 20  ? 0.3023 0.3679 0.2845 0.0043  0.0019  0.0752  20  PRO A N   
177  C CA  . PRO A 20  ? 0.3035 0.3602 0.2890 0.0075  0.0043  0.0862  20  PRO A CA  
178  C C   . PRO A 20  ? 0.3751 0.4394 0.3557 0.0100  0.0063  0.0975  20  PRO A C   
179  O O   . PRO A 20  ? 0.4626 0.5167 0.4464 0.0114  0.0097  0.1070  20  PRO A O   
180  C CB  . PRO A 20  ? 0.3343 0.3929 0.3227 0.0123  0.0011  0.0863  20  PRO A CB  
181  C CG  . PRO A 20  ? 0.3657 0.4414 0.3493 0.0125  -0.0030 0.0793  20  PRO A CG  
182  C CD  . PRO A 20  ? 0.2860 0.3611 0.2677 0.0066  -0.0023 0.0699  20  PRO A CD  
183  N N   . TYR A 21  ? 0.2902 0.3719 0.2633 0.0105  0.0046  0.0969  21  TYR A N   
184  C CA  . TYR A 21  ? 0.3410 0.4313 0.3085 0.0128  0.0067  0.1081  21  TYR A CA  
185  C C   . TYR A 21  ? 0.3567 0.4437 0.3228 0.0078  0.0110  0.1087  21  TYR A C   
186  O O   . TYR A 21  ? 0.4886 0.5724 0.4542 0.0084  0.0149  0.1196  21  TYR A O   
187  C CB  . TYR A 21  ? 0.3249 0.4376 0.2847 0.0158  0.0029  0.1074  21  TYR A CB  
188  C CG  . TYR A 21  ? 0.3698 0.4877 0.3314 0.0213  -0.0010 0.1090  21  TYR A CG  
189  C CD1 . TYR A 21  ? 0.4231 0.5419 0.3851 0.0276  -0.0004 0.1223  21  TYR A CD1 
190  C CD2 . TYR A 21  ? 0.3308 0.4521 0.2947 0.0203  -0.0049 0.0975  21  TYR A CD2 
191  C CE1 . TYR A 21  ? 0.3783 0.5025 0.3426 0.0331  -0.0040 0.1240  21  TYR A CE1 
192  C CE2 . TYR A 21  ? 0.3522 0.4792 0.3185 0.0252  -0.0084 0.0989  21  TYR A CE2 
193  C CZ  . TYR A 21  ? 0.3648 0.4938 0.3314 0.0318  -0.0080 0.1120  21  TYR A CZ  
194  O OH  . TYR A 21  ? 0.3612 0.4969 0.3308 0.0372  -0.0114 0.1139  21  TYR A OH  
195  N N   . THR A 22  ? 0.3627 0.4501 0.3287 0.0029  0.0107  0.0975  22  THR A N   
196  C CA  . THR A 22  ? 0.3644 0.4498 0.3298 -0.0018 0.0146  0.0972  22  THR A CA  
197  C C   . THR A 22  ? 0.3733 0.4406 0.3467 -0.0059 0.0172  0.0945  22  THR A C   
198  O O   . THR A 22  ? 0.3442 0.4082 0.3187 -0.0097 0.0211  0.0966  22  THR A O   
199  C CB  . THR A 22  ? 0.3522 0.4499 0.3129 -0.0043 0.0132  0.0869  22  THR A CB  
200  O OG1 . THR A 22  ? 0.3275 0.4193 0.2922 -0.0059 0.0105  0.0754  22  THR A OG1 
201  C CG2 . THR A 22  ? 0.3638 0.4809 0.3162 -0.0009 0.0108  0.0883  22  THR A CG2 
202  N N   . GLY A 23  ? 0.3131 0.3700 0.2921 -0.0056 0.0151  0.0894  23  GLY A N   
203  C CA  . GLY A 23  ? 0.3686 0.4104 0.3547 -0.0096 0.0171  0.0854  23  GLY A CA  
204  C C   . GLY A 23  ? 0.3523 0.3958 0.3387 -0.0141 0.0170  0.0753  23  GLY A C   
205  O O   . GLY A 23  ? 0.3941 0.4274 0.3861 -0.0178 0.0187  0.0722  23  GLY A O   
206  N N   . GLU A 24  ? 0.2667 0.3232 0.2477 -0.0137 0.0150  0.0699  24  GLU A N   
207  C CA  . GLU A 24  ? 0.2402 0.2988 0.2215 -0.0171 0.0152  0.0608  24  GLU A CA  
208  C C   . GLU A 24  ? 0.2263 0.2814 0.2100 -0.0170 0.0119  0.0513  24  GLU A C   
209  O O   . GLU A 24  ? 0.2576 0.3165 0.2394 -0.0142 0.0089  0.0496  24  GLU A O   
210  C CB  . GLU A 24  ? 0.2560 0.3300 0.2305 -0.0168 0.0155  0.0595  24  GLU A CB  
211  C CG  . GLU A 24  ? 0.3802 0.4593 0.3517 -0.0171 0.0191  0.0693  24  GLU A CG  
212  C CD  . GLU A 24  ? 0.5277 0.6243 0.4913 -0.0158 0.0190  0.0688  24  GLU A CD  
213  O OE1 . GLU A 24  ? 0.7594 0.8616 0.7203 -0.0170 0.0225  0.0749  24  GLU A OE1 
214  O OE2 . GLU A 24  ? 0.6368 0.7417 0.5968 -0.0140 0.0157  0.0623  24  GLU A OE2 
215  N N   . TYR A 25  ? 0.1731 0.2217 0.1608 -0.0200 0.0126  0.0453  25  TYR A N   
216  C CA  . TYR A 25  ? 0.1430 0.1895 0.1322 -0.0200 0.0101  0.0363  25  TYR A CA  
217  C C   . TYR A 25  ? 0.1834 0.2411 0.1683 -0.0197 0.0095  0.0304  25  TYR A C   
218  O O   . TYR A 25  ? 0.2240 0.2859 0.2082 -0.0213 0.0116  0.0287  25  TYR A O   
219  C CB  . TYR A 25  ? 0.2239 0.2612 0.2186 -0.0228 0.0111  0.0326  25  TYR A CB  
220  C CG  . TYR A 25  ? 0.2547 0.2806 0.2542 -0.0231 0.0110  0.0351  25  TYR A CG  
221  C CD1 . TYR A 25  ? 0.2222 0.2430 0.2237 -0.0239 0.0134  0.0425  25  TYR A CD1 
222  C CD2 . TYR A 25  ? 0.1955 0.2154 0.1975 -0.0227 0.0089  0.0299  25  TYR A CD2 
223  C CE1 . TYR A 25  ? 0.2228 0.2326 0.2291 -0.0241 0.0137  0.0439  25  TYR A CE1 
224  C CE2 . TYR A 25  ? 0.1768 0.1869 0.1830 -0.0228 0.0090  0.0315  25  TYR A CE2 
225  C CZ  . TYR A 25  ? 0.2502 0.2552 0.2586 -0.0235 0.0114  0.0381  25  TYR A CZ  
226  O OH  . TYR A 25  ? 0.2425 0.2373 0.2556 -0.0236 0.0120  0.0388  25  TYR A OH  
227  N N   . LEU A 26  ? 0.2023 0.2652 0.1847 -0.0177 0.0068  0.0268  26  LEU A N   
228  C CA  . LEU A 26  ? 0.2141 0.2884 0.1921 -0.0175 0.0064  0.0210  26  LEU A CA  
229  C C   . LEU A 26  ? 0.2465 0.3175 0.2270 -0.0188 0.0065  0.0117  26  LEU A C   
230  O O   . LEU A 26  ? 0.2190 0.2979 0.1969 -0.0190 0.0072  0.0063  26  LEU A O   
231  C CB  . LEU A 26  ? 0.1611 0.2442 0.1355 -0.0153 0.0037  0.0206  26  LEU A CB  
232  C CG  . LEU A 26  ? 0.1977 0.2862 0.1689 -0.0130 0.0035  0.0306  26  LEU A CG  
233  C CD1 . LEU A 26  ? 0.2523 0.3517 0.2204 -0.0105 0.0002  0.0295  26  LEU A CD1 
234  C CD2 . LEU A 26  ? 0.2648 0.3615 0.2315 -0.0134 0.0064  0.0354  26  LEU A CD2 
235  N N   . LEU A 27  ? 0.1934 0.2533 0.1788 -0.0194 0.0059  0.0097  27  LEU A N   
236  C CA  . LEU A 27  ? 0.2149 0.2707 0.2032 -0.0203 0.0065  0.0028  27  LEU A CA  
237  C C   . LEU A 27  ? 0.1686 0.2158 0.1613 -0.0215 0.0077  0.0052  27  LEU A C   
238  O O   . LEU A 27  ? 0.1982 0.2401 0.1926 -0.0219 0.0074  0.0104  27  LEU A O   
239  C CB  . LEU A 27  ? 0.1630 0.2149 0.1530 -0.0199 0.0045  -0.0028 27  LEU A CB  
240  C CG  . LEU A 27  ? 0.2281 0.2894 0.2147 -0.0195 0.0035  -0.0076 27  LEU A CG  
241  C CD1 . LEU A 27  ? 0.2624 0.3203 0.2514 -0.0198 0.0016  -0.0120 27  LEU A CD1 
242  C CD2 . LEU A 27  ? 0.2528 0.3193 0.2381 -0.0199 0.0055  -0.0137 27  LEU A CD2 
243  N N   . PRO A 28  ? 0.2021 0.2482 0.1970 -0.0219 0.0089  0.0011  28  PRO A N   
244  C CA  . PRO A 28  ? 0.2236 0.2642 0.2227 -0.0232 0.0098  0.0029  28  PRO A CA  
245  C C   . PRO A 28  ? 0.2085 0.2408 0.2110 -0.0230 0.0085  0.0002  28  PRO A C   
246  O O   . PRO A 28  ? 0.1757 0.2055 0.1815 -0.0238 0.0090  0.0004  28  PRO A O   
247  C CB  . PRO A 28  ? 0.2190 0.2658 0.2184 -0.0230 0.0120  0.0002  28  PRO A CB  
248  C CG  . PRO A 28  ? 0.1952 0.2446 0.1927 -0.0213 0.0117  -0.0059 28  PRO A CG  
249  C CD  . PRO A 28  ? 0.1951 0.2469 0.1888 -0.0211 0.0100  -0.0049 28  PRO A CD  
250  N N   . TRP A 29  ? 0.1590 0.1883 0.1609 -0.0220 0.0068  -0.0022 29  TRP A N   
251  C CA  . TRP A 29  ? 0.1745 0.1970 0.1792 -0.0217 0.0061  -0.0051 29  TRP A CA  
252  C C   . TRP A 29  ? 0.1745 0.1911 0.1818 -0.0227 0.0055  -0.0023 29  TRP A C   
253  O O   . TRP A 29  ? 0.1780 0.1913 0.1876 -0.0226 0.0055  -0.0039 29  TRP A O   
254  C CB  . TRP A 29  ? 0.1607 0.1818 0.1645 -0.0210 0.0048  -0.0081 29  TRP A CB  
255  C CG  . TRP A 29  ? 0.1951 0.2214 0.1970 -0.0205 0.0054  -0.0129 29  TRP A CG  
256  C CD1 . TRP A 29  ? 0.1932 0.2251 0.1925 -0.0206 0.0045  -0.0144 29  TRP A CD1 
257  C CD2 . TRP A 29  ? 0.1949 0.2217 0.1978 -0.0197 0.0073  -0.0173 29  TRP A CD2 
258  N NE1 . TRP A 29  ? 0.2243 0.2600 0.2227 -0.0205 0.0057  -0.0202 29  TRP A NE1 
259  C CE2 . TRP A 29  ? 0.2327 0.2645 0.2336 -0.0198 0.0076  -0.0220 29  TRP A CE2 
260  C CE3 . TRP A 29  ? 0.2500 0.2738 0.2557 -0.0187 0.0086  -0.0178 29  TRP A CE3 
261  C CZ2 . TRP A 29  ? 0.2211 0.2536 0.2229 -0.0190 0.0097  -0.0276 29  TRP A CZ2 
262  C CZ3 . TRP A 29  ? 0.3108 0.3355 0.3174 -0.0173 0.0106  -0.0223 29  TRP A CZ3 
263  C CH2 . TRP A 29  ? 0.3187 0.3471 0.3236 -0.0176 0.0113  -0.0274 29  TRP A CH2 
264  N N   . THR A 30  ? 0.1367 0.1521 0.1438 -0.0236 0.0053  0.0019  30  THR A N   
265  C CA  . THR A 30  ? 0.1410 0.1506 0.1511 -0.0250 0.0052  0.0037  30  THR A CA  
266  C C   . THR A 30  ? 0.1736 0.1852 0.1860 -0.0267 0.0066  0.0037  30  THR A C   
267  O O   . THR A 30  ? 0.2052 0.2143 0.2202 -0.0275 0.0062  0.0021  30  THR A O   
268  C CB  . THR A 30  ? 0.2364 0.2436 0.2466 -0.0253 0.0054  0.0082  30  THR A CB  
269  O OG1 . THR A 30  ? 0.2092 0.2158 0.2180 -0.0234 0.0038  0.0079  30  THR A OG1 
270  C CG2 . THR A 30  ? 0.1959 0.1966 0.2098 -0.0273 0.0059  0.0091  30  THR A CG2 
271  N N   . PHE A 31  ? 0.1532 0.1706 0.1647 -0.0273 0.0081  0.0055  31  PHE A N   
272  C CA  . PHE A 31  ? 0.1653 0.1862 0.1795 -0.0291 0.0095  0.0054  31  PHE A CA  
273  C C   . PHE A 31  ? 0.1789 0.2015 0.1946 -0.0275 0.0088  0.0012  31  PHE A C   
274  O O   . PHE A 31  ? 0.1918 0.2147 0.2106 -0.0286 0.0086  0.0003  31  PHE A O   
275  C CB  . PHE A 31  ? 0.1548 0.1828 0.1675 -0.0297 0.0115  0.0077  31  PHE A CB  
276  C CG  . PHE A 31  ? 0.1792 0.2127 0.1954 -0.0314 0.0131  0.0071  31  PHE A CG  
277  C CD1 . PHE A 31  ? 0.1879 0.2200 0.2077 -0.0350 0.0142  0.0092  31  PHE A CD1 
278  C CD2 . PHE A 31  ? 0.2201 0.2599 0.2364 -0.0294 0.0136  0.0038  31  PHE A CD2 
279  C CE1 . PHE A 31  ? 0.1873 0.2260 0.2111 -0.0370 0.0155  0.0083  31  PHE A CE1 
280  C CE2 . PHE A 31  ? 0.1708 0.2170 0.1909 -0.0306 0.0149  0.0033  31  PHE A CE2 
281  C CZ  . PHE A 31  ? 0.1524 0.1988 0.1762 -0.0346 0.0158  0.0055  31  PHE A CZ  
282  N N   . PHE A 32  ? 0.1787 0.2027 0.1922 -0.0249 0.0087  -0.0013 32  PHE A N   
283  C CA  . PHE A 32  ? 0.1831 0.2086 0.1983 -0.0228 0.0088  -0.0044 32  PHE A CA  
284  C C   . PHE A 32  ? 0.1660 0.1858 0.1825 -0.0222 0.0072  -0.0053 32  PHE A C   
285  O O   . PHE A 32  ? 0.1824 0.2040 0.2012 -0.0213 0.0071  -0.0060 32  PHE A O   
286  C CB  . PHE A 32  ? 0.1289 0.1564 0.1421 -0.0204 0.0096  -0.0073 32  PHE A CB  
287  C CG  . PHE A 32  ? 0.1358 0.1713 0.1484 -0.0203 0.0116  -0.0075 32  PHE A CG  
288  C CD1 . PHE A 32  ? 0.1962 0.2372 0.2120 -0.0204 0.0128  -0.0070 32  PHE A CD1 
289  C CD2 . PHE A 32  ? 0.1944 0.2334 0.2034 -0.0201 0.0123  -0.0085 32  PHE A CD2 
290  C CE1 . PHE A 32  ? 0.1992 0.2483 0.2146 -0.0203 0.0150  -0.0073 32  PHE A CE1 
291  C CE2 . PHE A 32  ? 0.2666 0.3139 0.2746 -0.0200 0.0144  -0.0089 32  PHE A CE2 
292  C CZ  . PHE A 32  ? 0.2107 0.2628 0.2220 -0.0200 0.0159  -0.0082 32  PHE A CZ  
293  N N   . HIS A 33  ? 0.1761 0.1902 0.1910 -0.0225 0.0061  -0.0052 33  HIS A N   
294  C CA  . HIS A 33  ? 0.1591 0.1686 0.1750 -0.0222 0.0050  -0.0059 33  HIS A CA  
295  C C   . HIS A 33  ? 0.1605 0.1700 0.1785 -0.0245 0.0044  -0.0047 33  HIS A C   
296  O O   . HIS A 33  ? 0.1777 0.1867 0.1967 -0.0242 0.0037  -0.0056 33  HIS A O   
297  C CB  . HIS A 33  ? 0.1627 0.1670 0.1769 -0.0218 0.0042  -0.0065 33  HIS A CB  
298  C CG  . HIS A 33  ? 0.1856 0.1894 0.1990 -0.0199 0.0049  -0.0090 33  HIS A CG  
299  N ND1 . HIS A 33  ? 0.1439 0.1457 0.1584 -0.0180 0.0055  -0.0103 33  HIS A ND1 
300  C CD2 . HIS A 33  ? 0.1456 0.1507 0.1572 -0.0197 0.0052  -0.0107 33  HIS A CD2 
301  C CE1 . HIS A 33  ? 0.1704 0.1710 0.1846 -0.0170 0.0065  -0.0128 33  HIS A CE1 
302  N NE2 . HIS A 33  ? 0.1515 0.1546 0.1639 -0.0182 0.0062  -0.0136 33  HIS A NE2 
303  N N   . ALA A 34  ? 0.1563 0.1665 0.1749 -0.0270 0.0051  -0.0028 34  ALA A N   
304  C CA  . ALA A 34  ? 0.1562 0.1664 0.1776 -0.0299 0.0051  -0.0027 34  ALA A CA  
305  C C   . ALA A 34  ? 0.2073 0.2247 0.2312 -0.0301 0.0051  -0.0040 34  ALA A C   
306  O O   . ALA A 34  ? 0.1686 0.1874 0.1942 -0.0309 0.0042  -0.0056 34  ALA A O   
307  C CB  . ALA A 34  ? 0.1618 0.1704 0.1842 -0.0326 0.0065  -0.0001 34  ALA A CB  
308  N N   . VAL A 35  ? 0.1660 0.1891 0.1901 -0.0291 0.0062  -0.0035 35  VAL A N   
309  C CA  . VAL A 35  ? 0.1561 0.1875 0.1834 -0.0291 0.0064  -0.0044 35  VAL A CA  
310  C C   . VAL A 35  ? 0.1476 0.1804 0.1747 -0.0252 0.0052  -0.0057 35  VAL A C   
311  O O   . VAL A 35  ? 0.1600 0.1995 0.1897 -0.0248 0.0045  -0.0063 35  VAL A O   
312  C CB  . VAL A 35  ? 0.1899 0.2278 0.2181 -0.0292 0.0083  -0.0035 35  VAL A CB  
313  C CG1 . VAL A 35  ? 0.1463 0.1829 0.1746 -0.0331 0.0099  -0.0011 35  VAL A CG1 
314  C CG2 . VAL A 35  ? 0.1788 0.2162 0.2041 -0.0253 0.0090  -0.0041 35  VAL A CG2 
315  N N   . LYS A 36  ? 0.1318 0.1590 0.1561 -0.0223 0.0052  -0.0059 36  LYS A N   
316  C CA  . LYS A 36  ? 0.1320 0.1589 0.1562 -0.0183 0.0048  -0.0063 36  LYS A CA  
317  C C   . LYS A 36  ? 0.1479 0.1707 0.1710 -0.0183 0.0033  -0.0062 36  LYS A C   
318  O O   . LYS A 36  ? 0.1826 0.2086 0.2064 -0.0161 0.0026  -0.0056 36  LYS A O   
319  C CB  . LYS A 36  ? 0.1662 0.1890 0.1887 -0.0156 0.0061  -0.0071 36  LYS A CB  
320  C CG  . LYS A 36  ? 0.1509 0.1723 0.1743 -0.0112 0.0066  -0.0071 36  LYS A CG  
321  C CD  . LYS A 36  ? 0.1605 0.1786 0.1836 -0.0088 0.0087  -0.0089 36  LYS A CD  
322  C CE  . LYS A 36  ? 0.1497 0.1595 0.1705 -0.0097 0.0087  -0.0101 36  LYS A CE  
323  N NZ  . LYS A 36  ? 0.1284 0.1336 0.1492 -0.0085 0.0081  -0.0084 36  LYS A NZ  
324  N N   . ASP A 37  ? 0.1464 0.1629 0.1676 -0.0205 0.0029  -0.0064 37  ASP A N   
325  C CA  . ASP A 37  ? 0.1316 0.1439 0.1514 -0.0200 0.0020  -0.0066 37  ASP A CA  
326  C C   . ASP A 37  ? 0.1712 0.1820 0.1912 -0.0233 0.0012  -0.0075 37  ASP A C   
327  O O   . ASP A 37  ? 0.1401 0.1514 0.1594 -0.0233 0.0003  -0.0081 37  ASP A O   
328  C CB  . ASP A 37  ? 0.1574 0.1627 0.1752 -0.0187 0.0027  -0.0067 37  ASP A CB  
329  C CG  . ASP A 37  ? 0.1924 0.1979 0.2105 -0.0159 0.0041  -0.0069 37  ASP A CG  
330  O OD1 . ASP A 37  ? 0.1843 0.1910 0.2033 -0.0130 0.0045  -0.0061 37  ASP A OD1 
331  O OD2 . ASP A 37  ? 0.1932 0.1979 0.2107 -0.0163 0.0049  -0.0079 37  ASP A OD2 
332  N N   . TYR A 38  ? 0.1822 0.1905 0.2027 -0.0259 0.0017  -0.0074 38  TYR A N   
333  C CA  . TYR A 38  ? 0.1337 0.1381 0.1546 -0.0283 0.0014  -0.0085 38  TYR A CA  
334  C C   . TYR A 38  ? 0.1357 0.1445 0.1588 -0.0311 0.0009  -0.0105 38  TYR A C   
335  O O   . TYR A 38  ? 0.1701 0.1770 0.1931 -0.0322 0.0005  -0.0125 38  TYR A O   
336  C CB  . TYR A 38  ? 0.1939 0.1937 0.2151 -0.0297 0.0023  -0.0071 38  TYR A CB  
337  C CG  . TYR A 38  ? 0.1701 0.1667 0.1890 -0.0274 0.0023  -0.0059 38  TYR A CG  
338  C CD1 . TYR A 38  ? 0.1667 0.1615 0.1840 -0.0253 0.0018  -0.0069 38  TYR A CD1 
339  C CD2 . TYR A 38  ? 0.1709 0.1674 0.1892 -0.0275 0.0030  -0.0039 38  TYR A CD2 
340  C CE1 . TYR A 38  ? 0.1277 0.1204 0.1435 -0.0240 0.0019  -0.0067 38  TYR A CE1 
341  C CE2 . TYR A 38  ? 0.1766 0.1722 0.1928 -0.0256 0.0027  -0.0035 38  TYR A CE2 
342  C CZ  . TYR A 38  ? 0.1478 0.1416 0.1631 -0.0241 0.0022  -0.0053 38  TYR A CZ  
343  O OH  . TYR A 38  ? 0.1686 0.1623 0.1825 -0.0230 0.0020  -0.0058 38  TYR A OH  
344  N N   . TYR A 39  ? 0.1543 0.1698 0.1798 -0.0323 0.0011  -0.0106 39  TYR A N   
345  C CA  . TYR A 39  ? 0.1403 0.1623 0.1681 -0.0349 0.0004  -0.0133 39  TYR A CA  
346  C C   . TYR A 39  ? 0.1571 0.1857 0.1834 -0.0318 -0.0012 -0.0135 39  TYR A C   
347  O O   . TYR A 39  ? 0.1350 0.1667 0.1608 -0.0328 -0.0023 -0.0158 39  TYR A O   
348  C CB  . TYR A 39  ? 0.1154 0.1435 0.1469 -0.0377 0.0012  -0.0134 39  TYR A CB  
349  C CG  . TYR A 39  ? 0.2025 0.2397 0.2370 -0.0405 0.0002  -0.0168 39  TYR A CG  
350  C CD1 . TYR A 39  ? 0.1874 0.2228 0.2246 -0.0455 0.0008  -0.0203 39  TYR A CD1 
351  C CD2 . TYR A 39  ? 0.1690 0.2173 0.2041 -0.0381 -0.0012 -0.0167 39  TYR A CD2 
352  C CE1 . TYR A 39  ? 0.1861 0.2311 0.2261 -0.0487 -0.0002 -0.0245 39  TYR A CE1 
353  C CE2 . TYR A 39  ? 0.1984 0.2572 0.2362 -0.0407 -0.0025 -0.0201 39  TYR A CE2 
354  C CZ  . TYR A 39  ? 0.2146 0.2721 0.2548 -0.0463 -0.0021 -0.0243 39  TYR A CZ  
355  O OH  . TYR A 39  ? 0.1889 0.2580 0.2319 -0.0494 -0.0035 -0.0287 39  TYR A OH  
356  N N   . ASP A 40  ? 0.1419 0.1724 0.1672 -0.0278 -0.0012 -0.0110 40  ASP A N   
357  C CA  . ASP A 40  ? 0.1303 0.1679 0.1550 -0.0244 -0.0024 -0.0100 40  ASP A CA  
358  C C   . ASP A 40  ? 0.1708 0.2048 0.1920 -0.0223 -0.0029 -0.0094 40  ASP A C   
359  O O   . ASP A 40  ? 0.1573 0.1984 0.1777 -0.0207 -0.0042 -0.0091 40  ASP A O   
360  C CB  . ASP A 40  ? 0.1726 0.2120 0.1980 -0.0205 -0.0015 -0.0076 40  ASP A CB  
361  C CG  . ASP A 40  ? 0.1978 0.2468 0.2272 -0.0217 -0.0015 -0.0082 40  ASP A CG  
362  O OD1 . ASP A 40  ? 0.1755 0.2345 0.2066 -0.0217 -0.0030 -0.0090 40  ASP A OD1 
363  O OD2 . ASP A 40  ? 0.1895 0.2371 0.2202 -0.0230 -0.0001 -0.0081 40  ASP A OD2 
364  N N   . MET A 41  ? 0.1760 0.2002 0.1952 -0.0222 -0.0020 -0.0090 41  MET A N   
365  C CA  . MET A 41  ? 0.1355 0.1568 0.1518 -0.0204 -0.0020 -0.0082 41  MET A CA  
366  C C   . MET A 41  ? 0.1622 0.1873 0.1776 -0.0228 -0.0031 -0.0109 41  MET A C   
367  O O   . MET A 41  ? 0.1640 0.1944 0.1773 -0.0209 -0.0038 -0.0100 41  MET A O   
368  C CB  . MET A 41  ? 0.1258 0.1372 0.1409 -0.0201 -0.0007 -0.0077 41  MET A CB  
369  C CG  . MET A 41  ? 0.1627 0.1712 0.1779 -0.0170 0.0004  -0.0055 41  MET A CG  
370  S SD  . MET A 41  ? 0.1691 0.1783 0.1829 -0.0126 0.0011  -0.0022 41  MET A SD  
371  C CE  . MET A 41  ? 0.1808 0.1827 0.1924 -0.0135 0.0021  -0.0023 41  MET A CE  
372  N N   . PRO A 42  ? 0.1300 0.1531 0.1470 -0.0269 -0.0030 -0.0143 42  PRO A N   
373  C CA  . PRO A 42  ? 0.1545 0.1824 0.1712 -0.0294 -0.0037 -0.0181 42  PRO A CA  
374  C C   . PRO A 42  ? 0.1496 0.1896 0.1678 -0.0306 -0.0052 -0.0198 42  PRO A C   
375  O O   . PRO A 42  ? 0.1455 0.1927 0.1624 -0.0315 -0.0063 -0.0225 42  PRO A O   
376  C CB  . PRO A 42  ? 0.1436 0.1641 0.1626 -0.0332 -0.0026 -0.0212 42  PRO A CB  
377  C CG  . PRO A 42  ? 0.1550 0.1713 0.1762 -0.0333 -0.0017 -0.0187 42  PRO A CG  
378  C CD  . PRO A 42  ? 0.1699 0.1857 0.1889 -0.0290 -0.0018 -0.0148 42  PRO A CD  
379  N N   . ALA A 43  ? 0.1618 0.2058 0.1829 -0.0303 -0.0054 -0.0184 43  ALA A N   
380  C CA  . ALA A 43  ? 0.1347 0.1920 0.1580 -0.0314 -0.0069 -0.0200 43  ALA A CA  
381  C C   . ALA A 43  ? 0.1816 0.2483 0.2020 -0.0268 -0.0086 -0.0173 43  ALA A C   
382  O O   . ALA A 43  ? 0.1559 0.2359 0.1774 -0.0276 -0.0104 -0.0193 43  ALA A O   
383  C CB  . ALA A 43  ? 0.1503 0.2100 0.1775 -0.0318 -0.0063 -0.0188 43  ALA A CB  
384  N N   . TYR A 44  ? 0.1693 0.2303 0.1866 -0.0220 -0.0079 -0.0127 44  TYR A N   
385  C CA  . TYR A 44  ? 0.1656 0.2342 0.1799 -0.0174 -0.0090 -0.0093 44  TYR A CA  
386  C C   . TYR A 44  ? 0.1464 0.2231 0.1580 -0.0196 -0.0104 -0.0126 44  TYR A C   
387  O O   . TYR A 44  ? 0.1593 0.2479 0.1690 -0.0168 -0.0120 -0.0108 44  TYR A O   
388  C CB  . TYR A 44  ? 0.1088 0.1672 0.1203 -0.0132 -0.0072 -0.0044 44  TYR A CB  
389  C CG  . TYR A 44  ? 0.1341 0.1881 0.1476 -0.0093 -0.0059 -0.0004 44  TYR A CG  
390  C CD1 . TYR A 44  ? 0.2253 0.2862 0.2393 -0.0040 -0.0062 0.0040  44  TYR A CD1 
391  C CD2 . TYR A 44  ? 0.1429 0.1863 0.1579 -0.0106 -0.0042 -0.0013 44  TYR A CD2 
392  C CE1 . TYR A 44  ? 0.1989 0.2552 0.2153 -0.0002 -0.0046 0.0068  44  TYR A CE1 
393  C CE2 . TYR A 44  ? 0.1356 0.1753 0.1523 -0.0073 -0.0028 0.0012  44  TYR A CE2 
394  C CZ  . TYR A 44  ? 0.1909 0.2365 0.2085 -0.0022 -0.0028 0.0050  44  TYR A CZ  
395  O OH  . TYR A 44  ? 0.1910 0.2324 0.2110 0.0013  -0.0009 0.0068  44  TYR A OH  
396  N N   . LEU A 45  ? 0.1184 0.1889 0.1297 -0.0242 -0.0097 -0.0174 45  LEU A N   
397  C CA  . LEU A 45  ? 0.1604 0.2381 0.1691 -0.0263 -0.0106 -0.0216 45  LEU A CA  
398  C C   . LEU A 45  ? 0.2246 0.3170 0.2357 -0.0296 -0.0127 -0.0266 45  LEU A C   
399  O O   . LEU A 45  ? 0.2111 0.3135 0.2196 -0.0310 -0.0139 -0.0302 45  LEU A O   
400  C CB  . LEU A 45  ? 0.1581 0.2249 0.1667 -0.0299 -0.0088 -0.0258 45  LEU A CB  
401  C CG  . LEU A 45  ? 0.1710 0.2256 0.1771 -0.0272 -0.0070 -0.0219 45  LEU A CG  
402  C CD1 . LEU A 45  ? 0.1785 0.2227 0.1861 -0.0304 -0.0053 -0.0260 45  LEU A CD1 
403  C CD2 . LEU A 45  ? 0.1765 0.2363 0.1773 -0.0239 -0.0070 -0.0191 45  LEU A CD2 
404  N N   . LYS A 46  ? 0.2005 0.2957 0.2166 -0.0313 -0.0130 -0.0273 46  LYS A N   
405  C CA  . LYS A 46  ? 0.1702 0.2813 0.1893 -0.0345 -0.0151 -0.0318 46  LYS A CA  
406  C C   . LYS A 46  ? 0.1890 0.3162 0.2057 -0.0292 -0.0176 -0.0277 46  LYS A C   
407  O O   . LYS A 46  ? 0.2345 0.3782 0.2521 -0.0313 -0.0199 -0.0318 46  LYS A O   
408  C CB  . LYS A 46  ? 0.2246 0.3343 0.2501 -0.0379 -0.0143 -0.0333 46  LYS A CB  
409  C CG  . LYS A 46  ? 0.3076 0.4009 0.3351 -0.0420 -0.0115 -0.0355 46  LYS A CG  
410  C CD  . LYS A 46  ? 0.4943 0.5885 0.5282 -0.0475 -0.0105 -0.0389 46  LYS A CD  
411  C CE  . LYS A 46  ? 0.5839 0.6813 0.6203 -0.0446 -0.0104 -0.0340 46  LYS A CE  
412  N NZ  . LYS A 46  ? 0.7134 0.8203 0.7562 -0.0499 -0.0103 -0.0377 46  LYS A NZ  
413  N N   . ASP A 47  ? 0.2134 0.3367 0.2277 -0.0224 -0.0171 -0.0198 47  ASP A N   
414  C CA  . ASP A 47  ? 0.1684 0.3055 0.1814 -0.0164 -0.0191 -0.0144 47  ASP A CA  
415  C C   . ASP A 47  ? 0.2626 0.4000 0.2690 -0.0115 -0.0191 -0.0092 47  ASP A C   
416  O O   . ASP A 47  ? 0.2428 0.3939 0.2473 -0.0065 -0.0209 -0.0047 47  ASP A O   
417  C CB  . ASP A 47  ? 0.1617 0.2947 0.1782 -0.0117 -0.0181 -0.0088 47  ASP A CB  
418  C CG  . ASP A 47  ? 0.3451 0.4807 0.3680 -0.0161 -0.0180 -0.0130 47  ASP A CG  
419  O OD1 . ASP A 47  ? 0.3431 0.4905 0.3686 -0.0212 -0.0197 -0.0190 47  ASP A OD1 
420  O OD2 . ASP A 47  ? 0.4348 0.5612 0.4603 -0.0145 -0.0161 -0.0105 47  ASP A OD2 
421  N N   . PHE A 48  ? 0.1573 0.2807 0.1604 -0.0125 -0.0169 -0.0093 48  PHE A N   
422  C CA  . PHE A 48  ? 0.1661 0.2877 0.1633 -0.0083 -0.0160 -0.0038 48  PHE A CA  
423  C C   . PHE A 48  ? 0.2201 0.3403 0.2138 -0.0127 -0.0155 -0.0094 48  PHE A C   
424  O O   . PHE A 48  ? 0.2396 0.3490 0.2354 -0.0175 -0.0142 -0.0148 48  PHE A O   
425  C CB  . PHE A 48  ? 0.2161 0.3212 0.2136 -0.0045 -0.0131 0.0025  48  PHE A CB  
426  C CG  . PHE A 48  ? 0.2241 0.3302 0.2252 0.0004  -0.0131 0.0076  48  PHE A CG  
427  C CD1 . PHE A 48  ? 0.2044 0.3201 0.2038 0.0070  -0.0139 0.0146  48  PHE A CD1 
428  C CD2 . PHE A 48  ? 0.2271 0.3261 0.2332 -0.0013 -0.0123 0.0055  48  PHE A CD2 
429  C CE1 . PHE A 48  ? 0.2514 0.3686 0.2548 0.0120  -0.0136 0.0192  48  PHE A CE1 
430  C CE2 . PHE A 48  ? 0.2065 0.3075 0.2161 0.0033  -0.0121 0.0096  48  PHE A CE2 
431  C CZ  . PHE A 48  ? 0.2323 0.3420 0.2409 0.0101  -0.0127 0.0162  48  PHE A CZ  
432  N N   . GLU A 49  ? 0.2208 0.3526 0.2090 -0.0107 -0.0165 -0.0079 49  GLU A N   
433  C CA  . GLU A 49  ? 0.1804 0.3151 0.1648 -0.0146 -0.0163 -0.0140 49  GLU A CA  
434  C C   . GLU A 49  ? 0.2352 0.3572 0.2158 -0.0128 -0.0132 -0.0098 49  GLU A C   
435  O O   . GLU A 49  ? 0.2715 0.3999 0.2464 -0.0104 -0.0128 -0.0067 49  GLU A O   
436  C CB  . GLU A 49  ? 0.2364 0.3929 0.2166 -0.0137 -0.0191 -0.0151 49  GLU A CB  
437  C CG  . GLU A 49  ? 0.3557 0.5269 0.3403 -0.0170 -0.0222 -0.0213 49  GLU A CG  
438  C CD  . GLU A 49  ? 0.5196 0.6918 0.5092 -0.0134 -0.0232 -0.0159 49  GLU A CD  
439  O OE1 . GLU A 49  ? 0.4739 0.6446 0.4698 -0.0177 -0.0236 -0.0211 49  GLU A OE1 
440  O OE2 . GLU A 49  ? 0.5059 0.6800 0.4934 -0.0063 -0.0232 -0.0063 49  GLU A OE2 
441  N N   . ILE A 50  ? 0.1829 0.2876 0.1670 -0.0138 -0.0110 -0.0095 50  ILE A N   
442  C CA  . ILE A 50  ? 0.2372 0.3288 0.2194 -0.0131 -0.0080 -0.0069 50  ILE A CA  
443  C C   . ILE A 50  ? 0.1851 0.2659 0.1708 -0.0182 -0.0069 -0.0141 50  ILE A C   
444  O O   . ILE A 50  ? 0.2392 0.3209 0.2289 -0.0218 -0.0081 -0.0197 50  ILE A O   
445  C CB  . ILE A 50  ? 0.2442 0.3253 0.2276 -0.0086 -0.0063 0.0014  50  ILE A CB  
446  C CG1 . ILE A 50  ? 0.2754 0.3511 0.2646 -0.0092 -0.0069 0.0004  50  ILE A CG1 
447  C CG2 . ILE A 50  ? 0.2376 0.3282 0.2176 -0.0029 -0.0067 0.0095  50  ILE A CG2 
448  C CD1 . ILE A 50  ? 0.3202 0.3825 0.3117 -0.0067 -0.0047 0.0052  50  ILE A CD1 
449  N N   . LYS A 51  ? 0.2277 0.2988 0.2123 -0.0184 -0.0044 -0.0135 51  LYS A N   
450  C CA  . LYS A 51  ? 0.1647 0.2243 0.1529 -0.0218 -0.0031 -0.0184 51  LYS A CA  
451  C C   . LYS A 51  ? 0.1329 0.1799 0.1240 -0.0201 -0.0018 -0.0138 51  LYS A C   
452  O O   . LYS A 51  ? 0.2039 0.2482 0.1932 -0.0168 -0.0005 -0.0076 51  LYS A O   
453  C CB  . LYS A 51  ? 0.1678 0.2263 0.1533 -0.0229 -0.0011 -0.0213 51  LYS A CB  
454  C CG  . LYS A 51  ? 0.2308 0.3029 0.2124 -0.0244 -0.0020 -0.0262 51  LYS A CG  
455  C CD  . LYS A 51  ? 0.2510 0.3277 0.2358 -0.0284 -0.0037 -0.0342 51  LYS A CD  
456  C CE  . LYS A 51  ? 0.3270 0.4168 0.3083 -0.0307 -0.0042 -0.0410 51  LYS A CE  
457  N NZ  . LYS A 51  ? 0.4314 0.5365 0.4066 -0.0275 -0.0059 -0.0364 51  LYS A NZ  
458  N N   . LEU A 52  ? 0.1209 0.1603 0.1165 -0.0224 -0.0018 -0.0168 52  LEU A N   
459  C CA  . LEU A 52  ? 0.1314 0.1597 0.1296 -0.0214 -0.0006 -0.0138 52  LEU A CA  
460  C C   . LEU A 52  ? 0.1574 0.1782 0.1587 -0.0243 0.0000  -0.0183 52  LEU A C   
461  O O   . LEU A 52  ? 0.2005 0.2231 0.2038 -0.0271 -0.0007 -0.0229 52  LEU A O   
462  C CB  . LEU A 52  ? 0.1618 0.1899 0.1624 -0.0202 -0.0016 -0.0113 52  LEU A CB  
463  C CG  . LEU A 52  ? 0.2164 0.2516 0.2152 -0.0164 -0.0023 -0.0063 52  LEU A CG  
464  C CD1 . LEU A 52  ? 0.1627 0.1993 0.1649 -0.0158 -0.0034 -0.0056 52  LEU A CD1 
465  C CD2 . LEU A 52  ? 0.1948 0.2242 0.1917 -0.0132 -0.0002 -0.0008 52  LEU A CD2 
466  N N   . ASN A 53  ? 0.1460 0.1585 0.1483 -0.0237 0.0015  -0.0168 53  ASN A N   
467  C CA  . ASN A 53  ? 0.1265 0.1325 0.1319 -0.0255 0.0022  -0.0200 53  ASN A CA  
468  C C   . ASN A 53  ? 0.1392 0.1386 0.1473 -0.0250 0.0021  -0.0178 53  ASN A C   
469  O O   . ASN A 53  ? 0.1879 0.1864 0.1954 -0.0233 0.0022  -0.0142 53  ASN A O   
470  C CB  . ASN A 53  ? 0.1883 0.1925 0.1929 -0.0251 0.0039  -0.0209 53  ASN A CB  
471  C CG  . ASN A 53  ? 0.1599 0.1717 0.1609 -0.0253 0.0042  -0.0227 53  ASN A CG  
472  O OD1 . ASN A 53  ? 0.1869 0.2021 0.1880 -0.0272 0.0040  -0.0277 53  ASN A OD1 
473  N ND2 . ASN A 53  ? 0.1486 0.1632 0.1462 -0.0234 0.0051  -0.0186 53  ASN A ND2 
474  N N   . PHE A 54  ? 0.1580 0.1530 0.1692 -0.0265 0.0023  -0.0200 54  PHE A N   
475  C CA  . PHE A 54  ? 0.1673 0.1579 0.1806 -0.0262 0.0020  -0.0180 54  PHE A CA  
476  C C   . PHE A 54  ? 0.1720 0.1572 0.1876 -0.0261 0.0028  -0.0187 54  PHE A C   
477  O O   . PHE A 54  ? 0.1788 0.1627 0.1960 -0.0270 0.0034  -0.0215 54  PHE A O   
478  C CB  . PHE A 54  ? 0.1579 0.1503 0.1727 -0.0279 0.0012  -0.0186 54  PHE A CB  
479  C CG  . PHE A 54  ? 0.1577 0.1569 0.1708 -0.0274 0.0003  -0.0176 54  PHE A CG  
480  C CD1 . PHE A 54  ? 0.2190 0.2189 0.2317 -0.0254 0.0000  -0.0143 54  PHE A CD1 
481  C CD2 . PHE A 54  ? 0.1270 0.1327 0.1391 -0.0286 -0.0003 -0.0203 54  PHE A CD2 
482  C CE1 . PHE A 54  ? 0.2066 0.2130 0.2182 -0.0241 -0.0007 -0.0129 54  PHE A CE1 
483  C CE2 . PHE A 54  ? 0.2257 0.2393 0.2364 -0.0275 -0.0015 -0.0189 54  PHE A CE2 
484  C CZ  . PHE A 54  ? 0.1957 0.2094 0.2063 -0.0250 -0.0017 -0.0149 54  PHE A CZ  
485  N N   . ASN A 55  ? 0.1341 0.1170 0.1504 -0.0249 0.0027  -0.0163 55  ASN A N   
486  C CA  . ASN A 55  ? 0.1251 0.1045 0.1438 -0.0244 0.0029  -0.0160 55  ASN A CA  
487  C C   . ASN A 55  ? 0.1339 0.1122 0.1536 -0.0247 0.0024  -0.0140 55  ASN A C   
488  O O   . ASN A 55  ? 0.1772 0.1573 0.1955 -0.0246 0.0019  -0.0125 55  ASN A O   
489  C CB  . ASN A 55  ? 0.1481 0.1276 0.1668 -0.0231 0.0031  -0.0150 55  ASN A CB  
490  C CG  . ASN A 55  ? 0.1720 0.1500 0.1935 -0.0220 0.0031  -0.0147 55  ASN A CG  
491  O OD1 . ASN A 55  ? 0.1895 0.1662 0.2130 -0.0216 0.0038  -0.0163 55  ASN A OD1 
492  N ND2 . ASN A 55  ? 0.1534 0.1323 0.1753 -0.0213 0.0023  -0.0128 55  ASN A ND2 
493  N N   . LEU A 56  ? 0.1639 0.1390 0.1861 -0.0250 0.0028  -0.0139 56  LEU A N   
494  C CA  . LEU A 56  ? 0.1195 0.0934 0.1426 -0.0251 0.0027  -0.0111 56  LEU A CA  
495  C C   . LEU A 56  ? 0.1802 0.1519 0.2050 -0.0230 0.0029  -0.0090 56  LEU A C   
496  O O   . LEU A 56  ? 0.1915 0.1598 0.2190 -0.0224 0.0038  -0.0098 56  LEU A O   
497  C CB  . LEU A 56  ? 0.1226 0.0944 0.1477 -0.0275 0.0036  -0.0119 56  LEU A CB  
498  C CG  . LEU A 56  ? 0.2143 0.1902 0.2383 -0.0297 0.0032  -0.0140 56  LEU A CG  
499  C CD1 . LEU A 56  ? 0.2432 0.2171 0.2703 -0.0327 0.0044  -0.0158 56  LEU A CD1 
500  C CD2 . LEU A 56  ? 0.2059 0.1857 0.2280 -0.0293 0.0025  -0.0115 56  LEU A CD2 
501  N N   . THR A 57  ? 0.1906 0.1650 0.2142 -0.0217 0.0020  -0.0064 57  THR A N   
502  C CA  . THR A 57  ? 0.1646 0.1388 0.1897 -0.0194 0.0019  -0.0038 57  THR A CA  
503  C C   . THR A 57  ? 0.1600 0.1303 0.1869 -0.0193 0.0029  -0.0004 57  THR A C   
504  O O   . THR A 57  ? 0.1601 0.1299 0.1863 -0.0214 0.0035  0.0004  57  THR A O   
505  C CB  . THR A 57  ? 0.1617 0.1415 0.1849 -0.0182 0.0005  -0.0025 57  THR A CB  
506  O OG1 . THR A 57  ? 0.1359 0.1177 0.1569 -0.0191 0.0004  -0.0007 57  THR A OG1 
507  C CG2 . THR A 57  ? 0.1437 0.1261 0.1659 -0.0188 0.0001  -0.0058 57  THR A CG2 
508  N N   . PRO A 58  ? 0.1706 0.1381 0.2004 -0.0169 0.0036  0.0017  58  PRO A N   
509  C CA  . PRO A 58  ? 0.1827 0.1450 0.2148 -0.0167 0.0052  0.0056  58  PRO A CA  
510  C C   . PRO A 58  ? 0.1653 0.1313 0.1950 -0.0166 0.0048  0.0105  58  PRO A C   
511  O O   . PRO A 58  ? 0.1672 0.1296 0.1977 -0.0184 0.0065  0.0128  58  PRO A O   
512  C CB  . PRO A 58  ? 0.1558 0.1151 0.1916 -0.0130 0.0059  0.0074  58  PRO A CB  
513  C CG  . PRO A 58  ? 0.1707 0.1316 0.2070 -0.0128 0.0054  0.0020  58  PRO A CG  
514  C CD  . PRO A 58  ? 0.1918 0.1596 0.2239 -0.0144 0.0034  0.0002  58  PRO A CD  
515  N N   . VAL A 59  ? 0.1286 0.1019 0.1553 -0.0148 0.0029  0.0116  59  VAL A N   
516  C CA  . VAL A 59  ? 0.1648 0.1429 0.1885 -0.0147 0.0026  0.0157  59  VAL A CA  
517  C C   . VAL A 59  ? 0.1812 0.1603 0.2029 -0.0182 0.0031  0.0136  59  VAL A C   
518  O O   . VAL A 59  ? 0.1583 0.1385 0.1789 -0.0192 0.0042  0.0170  59  VAL A O   
519  C CB  . VAL A 59  ? 0.1784 0.1654 0.1996 -0.0122 0.0004  0.0163  59  VAL A CB  
520  C CG1 . VAL A 59  ? 0.1831 0.1734 0.2032 -0.0135 -0.0009 0.0103  59  VAL A CG1 
521  C CG2 . VAL A 59  ? 0.1480 0.1418 0.1654 -0.0120 0.0001  0.0201  59  VAL A CG2 
522  N N   . LEU A 60  ? 0.1575 0.1366 0.1788 -0.0200 0.0026  0.0084  60  LEU A N   
523  C CA  . LEU A 60  ? 0.1705 0.1505 0.1909 -0.0227 0.0031  0.0066  60  LEU A CA  
524  C C   . LEU A 60  ? 0.2056 0.1806 0.2290 -0.0252 0.0050  0.0075  60  LEU A C   
525  O O   . LEU A 60  ? 0.1675 0.1442 0.1907 -0.0271 0.0060  0.0091  60  LEU A O   
526  C CB  . LEU A 60  ? 0.1905 0.1716 0.2101 -0.0234 0.0023  0.0018  60  LEU A CB  
527  C CG  . LEU A 60  ? 0.2006 0.1834 0.2199 -0.0256 0.0027  0.0001  60  LEU A CG  
528  C CD1 . LEU A 60  ? 0.2570 0.2448 0.2744 -0.0256 0.0029  0.0019  60  LEU A CD1 
529  C CD2 . LEU A 60  ? 0.1793 0.1629 0.1978 -0.0255 0.0020  -0.0035 60  LEU A CD2 
530  N N   . ILE A 61  ? 0.1820 0.1511 0.2085 -0.0255 0.0057  0.0057  61  ILE A N   
531  C CA  . ILE A 61  ? 0.1246 0.0883 0.1547 -0.0284 0.0079  0.0055  61  ILE A CA  
532  C C   . ILE A 61  ? 0.1784 0.1400 0.2096 -0.0285 0.0098  0.0114  61  ILE A C   
533  O O   . ILE A 61  ? 0.1956 0.1563 0.2286 -0.0318 0.0115  0.0119  61  ILE A O   
534  C CB  . ILE A 61  ? 0.1635 0.1209 0.1970 -0.0281 0.0088  0.0025  61  ILE A CB  
535  C CG1 . ILE A 61  ? 0.2035 0.1639 0.2355 -0.0286 0.0073  -0.0032 61  ILE A CG1 
536  C CG2 . ILE A 61  ? 0.2091 0.1598 0.2471 -0.0315 0.0115  0.0019  61  ILE A CG2 
537  C CD1 . ILE A 61  ? 0.1696 0.1253 0.2044 -0.0280 0.0082  -0.0066 61  ILE A CD1 
538  N N   . ASP A 62  ? 0.1753 0.1369 0.2055 -0.0248 0.0095  0.0163  62  ASP A N   
539  C CA  . ASP A 62  ? 0.2006 0.1605 0.2313 -0.0242 0.0114  0.0232  62  ASP A CA  
540  C C   . ASP A 62  ? 0.1747 0.1410 0.2026 -0.0265 0.0117  0.0247  62  ASP A C   
541  O O   . ASP A 62  ? 0.1876 0.1515 0.2173 -0.0288 0.0143  0.0283  62  ASP A O   
542  C CB  . ASP A 62  ? 0.2136 0.1761 0.2427 -0.0192 0.0104  0.0283  62  ASP A CB  
543  C CG  . ASP A 62  ? 0.2858 0.2408 0.3192 -0.0164 0.0114  0.0295  62  ASP A CG  
544  O OD1 . ASP A 62  ? 0.3087 0.2547 0.3466 -0.0186 0.0139  0.0278  62  ASP A OD1 
545  O OD2 . ASP A 62  ? 0.2938 0.2523 0.3265 -0.0119 0.0098  0.0319  62  ASP A OD2 
546  N N   . GLN A 63  ? 0.1826 0.1569 0.2064 -0.0258 0.0094  0.0221  63  GLN A N   
547  C CA  . GLN A 63  ? 0.1551 0.1364 0.1762 -0.0272 0.0097  0.0230  63  GLN A CA  
548  C C   . GLN A 63  ? 0.1746 0.1555 0.1981 -0.0313 0.0109  0.0195  63  GLN A C   
549  O O   . GLN A 63  ? 0.2246 0.2084 0.2484 -0.0335 0.0127  0.0218  63  GLN A O   
550  C CB  . GLN A 63  ? 0.1440 0.1331 0.1607 -0.0251 0.0073  0.0204  63  GLN A CB  
551  C CG  . GLN A 63  ? 0.1882 0.1806 0.2025 -0.0215 0.0059  0.0232  63  GLN A CG  
552  C CD  . GLN A 63  ? 0.2125 0.2119 0.2235 -0.0204 0.0038  0.0189  63  GLN A CD  
553  O OE1 . GLN A 63  ? 0.2400 0.2460 0.2480 -0.0208 0.0039  0.0183  63  GLN A OE1 
554  N NE2 . GLN A 63  ? 0.1766 0.1744 0.1885 -0.0193 0.0022  0.0153  63  GLN A NE2 
555  N N   . ILE A 64  ? 0.1705 0.1494 0.1958 -0.0324 0.0098  0.0140  64  ILE A N   
556  C CA  . ILE A 64  ? 0.1461 0.1263 0.1740 -0.0362 0.0106  0.0107  64  ILE A CA  
557  C C   . ILE A 64  ? 0.1798 0.1548 0.2120 -0.0397 0.0136  0.0130  64  ILE A C   
558  O O   . ILE A 64  ? 0.1863 0.1649 0.2203 -0.0429 0.0151  0.0134  64  ILE A O   
559  C CB  . ILE A 64  ? 0.1374 0.1168 0.1661 -0.0364 0.0090  0.0049  64  ILE A CB  
560  C CG1 . ILE A 64  ? 0.1638 0.1482 0.1886 -0.0335 0.0068  0.0031  64  ILE A CG1 
561  C CG2 . ILE A 64  ? 0.1602 0.1419 0.1923 -0.0407 0.0097  0.0012  64  ILE A CG2 
562  C CD1 . ILE A 64  ? 0.2131 0.1971 0.2378 -0.0331 0.0053  -0.0014 64  ILE A CD1 
563  N N   . GLN A 65  ? 0.1994 0.1659 0.2339 -0.0389 0.0149  0.0150  65  GLN A N   
564  C CA  . GLN A 65  ? 0.1939 0.1536 0.2334 -0.0422 0.0184  0.0176  65  GLN A CA  
565  C C   . GLN A 65  ? 0.1973 0.1597 0.2357 -0.0428 0.0205  0.0244  65  GLN A C   
566  O O   . GLN A 65  ? 0.2028 0.1642 0.2450 -0.0473 0.0234  0.0252  65  GLN A O   
567  C CB  . GLN A 65  ? 0.2393 0.1888 0.2815 -0.0400 0.0196  0.0194  65  GLN A CB  
568  C CG  . GLN A 65  ? 0.2226 0.1680 0.2672 -0.0406 0.0189  0.0123  65  GLN A CG  
569  C CD  . GLN A 65  ? 0.3047 0.2403 0.3525 -0.0378 0.0205  0.0143  65  GLN A CD  
570  O OE1 . GLN A 65  ? 0.3614 0.2975 0.4068 -0.0328 0.0193  0.0185  65  GLN A OE1 
571  N NE2 . GLN A 65  ? 0.3333 0.2604 0.3869 -0.0410 0.0234  0.0112  65  GLN A NE2 
572  N N   . GLU A 66  ? 0.2029 0.1696 0.2364 -0.0386 0.0193  0.0292  66  GLU A N   
573  C CA  . GLU A 66  ? 0.2112 0.1818 0.2429 -0.0389 0.0214  0.0359  66  GLU A CA  
574  C C   . GLU A 66  ? 0.1726 0.1522 0.2035 -0.0420 0.0216  0.0334  66  GLU A C   
575  O O   . GLU A 66  ? 0.2412 0.2220 0.2741 -0.0452 0.0248  0.0369  66  GLU A O   
576  C CB  . GLU A 66  ? 0.2892 0.2645 0.3154 -0.0336 0.0197  0.0409  66  GLU A CB  
577  C CG  . GLU A 66  ? 0.5302 0.5091 0.5540 -0.0331 0.0223  0.0495  66  GLU A CG  
578  C CD  . GLU A 66  ? 0.4642 0.4469 0.4834 -0.0275 0.0208  0.0553  66  GLU A CD  
579  O OE1 . GLU A 66  ? 0.5247 0.5113 0.5412 -0.0265 0.0227  0.0631  66  GLU A OE1 
580  O OE2 . GLU A 66  ? 0.3146 0.2975 0.3328 -0.0242 0.0178  0.0524  66  GLU A OE2 
581  N N   . TYR A 67  ? 0.1699 0.1559 0.1985 -0.0410 0.0187  0.0275  67  TYR A N   
582  C CA  . TYR A 67  ? 0.2126 0.2072 0.2413 -0.0434 0.0190  0.0249  67  TYR A CA  
583  C C   . TYR A 67  ? 0.2411 0.2339 0.2760 -0.0487 0.0209  0.0222  67  TYR A C   
584  O O   . TYR A 67  ? 0.2519 0.2497 0.2889 -0.0520 0.0232  0.0235  67  TYR A O   
585  C CB  . TYR A 67  ? 0.1748 0.1751 0.2007 -0.0408 0.0158  0.0195  67  TYR A CB  
586  C CG  . TYR A 67  ? 0.1616 0.1680 0.1820 -0.0371 0.0148  0.0209  67  TYR A CG  
587  C CD1 . TYR A 67  ? 0.2035 0.2186 0.2220 -0.0373 0.0160  0.0217  67  TYR A CD1 
588  C CD2 . TYR A 67  ? 0.1592 0.1633 0.1764 -0.0336 0.0127  0.0210  67  TYR A CD2 
589  C CE1 . TYR A 67  ? 0.1761 0.1972 0.1894 -0.0342 0.0152  0.0220  67  TYR A CE1 
590  C CE2 . TYR A 67  ? 0.2039 0.2144 0.2164 -0.0307 0.0117  0.0213  67  TYR A CE2 
591  C CZ  . TYR A 67  ? 0.2080 0.2268 0.2184 -0.0311 0.0130  0.0216  67  TYR A CZ  
592  O OH  . TYR A 67  ? 0.2060 0.2315 0.2117 -0.0285 0.0121  0.0208  67  TYR A OH  
593  N N   . ALA A 68  ? 0.2387 0.2252 0.2768 -0.0500 0.0201  0.0179  68  ALA A N   
594  C CA  . ALA A 68  ? 0.2312 0.2169 0.2753 -0.0555 0.0217  0.0141  68  ALA A CA  
595  C C   . ALA A 68  ? 0.2547 0.2351 0.3033 -0.0596 0.0261  0.0186  68  ALA A C   
596  O O   . ALA A 68  ? 0.2910 0.2749 0.3444 -0.0650 0.0282  0.0166  68  ALA A O   
597  C CB  . ALA A 68  ? 0.2684 0.2483 0.3146 -0.0558 0.0203  0.0085  68  ALA A CB  
598  N N   . GLN A 69  ? 0.2529 0.2251 0.3004 -0.0573 0.0278  0.0248  69  GLN A N   
599  C CA  . GLN A 69  ? 0.3066 0.2716 0.3585 -0.0606 0.0324  0.0305  69  GLN A CA  
600  C C   . GLN A 69  ? 0.3356 0.3078 0.3851 -0.0611 0.0346  0.0369  69  GLN A C   
601  O O   . GLN A 69  ? 0.3029 0.2704 0.3559 -0.0644 0.0390  0.0424  69  GLN A O   
602  C CB  . GLN A 69  ? 0.3039 0.2571 0.3558 -0.0569 0.0334  0.0351  69  GLN A CB  
603  C CG  . GLN A 69  ? 0.4037 0.3478 0.4601 -0.0579 0.0330  0.0286  69  GLN A CG  
604  C CD  . GLN A 69  ? 0.5183 0.4545 0.5730 -0.0520 0.0321  0.0313  69  GLN A CD  
605  O OE1 . GLN A 69  ? 0.5524 0.4877 0.6042 -0.0478 0.0326  0.0393  69  GLN A OE1 
606  N NE2 . GLN A 69  ? 0.4388 0.3709 0.4954 -0.0516 0.0306  0.0245  69  GLN A NE2 
607  N N   . GLY A 70  ? 0.2951 0.2786 0.3390 -0.0582 0.0319  0.0361  70  GLY A N   
608  C CA  . GLY A 70  ? 0.3475 0.3393 0.3885 -0.0583 0.0339  0.0414  70  GLY A CA  
609  C C   . GLY A 70  ? 0.3485 0.3385 0.3848 -0.0543 0.0350  0.0503  70  GLY A C   
610  O O   . GLY A 70  ? 0.3761 0.3710 0.4110 -0.0554 0.0380  0.0563  70  GLY A O   
611  N N   . LYS A 71  ? 0.3198 0.3038 0.3535 -0.0496 0.0328  0.0515  71  LYS A N   
612  C CA  . LYS A 71  ? 0.4002 0.3843 0.4292 -0.0452 0.0334  0.0602  71  LYS A CA  
613  C C   . LYS A 71  ? 0.4077 0.4016 0.4292 -0.0400 0.0294  0.0589  71  LYS A C   
614  O O   . LYS A 71  ? 0.3788 0.3760 0.3957 -0.0363 0.0295  0.0656  71  LYS A O   
615  C CB  . LYS A 71  ? 0.4723 0.4433 0.5047 -0.0434 0.0345  0.0642  71  LYS A CB  
616  C CG  . LYS A 71  ? 0.5947 0.5579 0.6313 -0.0441 0.0327  0.0564  71  LYS A CG  
617  C CD  . LYS A 71  ? 0.6021 0.5510 0.6444 -0.0441 0.0357  0.0601  71  LYS A CD  
618  C CE  . LYS A 71  ? 0.7025 0.6495 0.7419 -0.0386 0.0367  0.0704  71  LYS A CE  
619  N NZ  . LYS A 71  ? 0.7920 0.7239 0.8379 -0.0380 0.0400  0.0739  71  LYS A NZ  
620  N N   . ALA A 72  ? 0.2943 0.2934 0.3146 -0.0397 0.0262  0.0507  72  ALA A N   
621  C CA  . ALA A 72  ? 0.2907 0.2985 0.3046 -0.0354 0.0229  0.0488  72  ALA A CA  
622  C C   . ALA A 72  ? 0.3168 0.3363 0.3265 -0.0357 0.0244  0.0508  72  ALA A C   
623  O O   . ALA A 72  ? 0.3433 0.3672 0.3550 -0.0389 0.0258  0.0478  72  ALA A O   
624  C CB  . ALA A 72  ? 0.2908 0.2989 0.3052 -0.0349 0.0196  0.0399  72  ALA A CB  
625  N N   . LYS A 73  ? 0.2224 0.2481 0.2262 -0.0324 0.0240  0.0559  73  LYS A N   
626  C CA  . LYS A 73  ? 0.1941 0.2327 0.1927 -0.0320 0.0251  0.0571  73  LYS A CA  
627  C C   . LYS A 73  ? 0.3008 0.3468 0.2955 -0.0294 0.0217  0.0492  73  LYS A C   
628  O O   . LYS A 73  ? 0.3254 0.3754 0.3157 -0.0260 0.0193  0.0496  73  LYS A O   
629  C CB  . LYS A 73  ? 0.2580 0.3004 0.2521 -0.0298 0.0268  0.0670  73  LYS A CB  
630  C CG  . LYS A 73  ? 0.4563 0.4893 0.4550 -0.0322 0.0308  0.0754  73  LYS A CG  
631  C CD  . LYS A 73  ? 0.6058 0.6396 0.6007 -0.0285 0.0318  0.0864  73  LYS A CD  
632  C CE  . LYS A 73  ? 0.6581 0.6813 0.6557 -0.0251 0.0298  0.0882  73  LYS A CE  
633  N NZ  . LYS A 73  ? 0.6574 0.6657 0.6634 -0.0285 0.0312  0.0850  73  LYS A NZ  
634  N N   . ASP A 74  ? 0.2497 0.2977 0.2465 -0.0311 0.0215  0.0421  74  ASP A N   
635  C CA  . ASP A 74  ? 0.2547 0.3070 0.2494 -0.0290 0.0188  0.0341  74  ASP A CA  
636  C C   . ASP A 74  ? 0.2627 0.3276 0.2529 -0.0284 0.0202  0.0324  74  ASP A C   
637  O O   . ASP A 74  ? 0.2528 0.3217 0.2450 -0.0305 0.0228  0.0319  74  ASP A O   
638  C CB  . ASP A 74  ? 0.2185 0.2649 0.2184 -0.0304 0.0180  0.0278  74  ASP A CB  
639  C CG  . ASP A 74  ? 0.2194 0.2674 0.2180 -0.0280 0.0156  0.0203  74  ASP A CG  
640  O OD1 . ASP A 74  ? 0.2338 0.2903 0.2289 -0.0266 0.0159  0.0174  74  ASP A OD1 
641  O OD2 . ASP A 74  ? 0.2475 0.2883 0.2488 -0.0277 0.0137  0.0171  74  ASP A OD2 
642  N N   . VAL A 75  ? 0.2474 0.3194 0.2320 -0.0257 0.0187  0.0311  75  VAL A N   
643  C CA  . VAL A 75  ? 0.3095 0.3947 0.2891 -0.0253 0.0204  0.0303  75  VAL A CA  
644  C C   . VAL A 75  ? 0.2121 0.3003 0.1934 -0.0254 0.0209  0.0215  75  VAL A C   
645  O O   . VAL A 75  ? 0.2552 0.3516 0.2358 -0.0261 0.0237  0.0208  75  VAL A O   
646  C CB  . VAL A 75  ? 0.3449 0.4386 0.3178 -0.0226 0.0185  0.0310  75  VAL A CB  
647  C CG1 . VAL A 75  ? 0.3309 0.4218 0.3026 -0.0216 0.0182  0.0409  75  VAL A CG1 
648  C CG2 . VAL A 75  ? 0.3138 0.4057 0.2868 -0.0211 0.0152  0.0229  75  VAL A CG2 
649  N N   . PHE A 76  ? 0.2479 0.3294 0.2322 -0.0245 0.0187  0.0151  76  PHE A N   
650  C CA  . PHE A 76  ? 0.2405 0.3231 0.2274 -0.0240 0.0194  0.0076  76  PHE A CA  
651  C C   . PHE A 76  ? 0.2550 0.3360 0.2471 -0.0258 0.0215  0.0091  76  PHE A C   
652  O O   . PHE A 76  ? 0.2144 0.3023 0.2076 -0.0256 0.0237  0.0061  76  PHE A O   
653  C CB  . PHE A 76  ? 0.2786 0.3532 0.2676 -0.0227 0.0169  0.0018  76  PHE A CB  
654  C CG  . PHE A 76  ? 0.3352 0.4113 0.3259 -0.0213 0.0178  -0.0057 76  PHE A CG  
655  C CD1 . PHE A 76  ? 0.3456 0.4280 0.3328 -0.0201 0.0181  -0.0115 76  PHE A CD1 
656  C CD2 . PHE A 76  ? 0.3209 0.3927 0.3171 -0.0211 0.0185  -0.0072 76  PHE A CD2 
657  C CE1 . PHE A 76  ? 0.4154 0.4980 0.4048 -0.0186 0.0196  -0.0188 76  PHE A CE1 
658  C CE2 . PHE A 76  ? 0.3390 0.4117 0.3372 -0.0190 0.0198  -0.0135 76  PHE A CE2 
659  C CZ  . PHE A 76  ? 0.4078 0.4851 0.4029 -0.0177 0.0205  -0.0193 76  PHE A CZ  
660  N N   . LEU A 77  ? 0.1801 0.2529 0.1760 -0.0277 0.0209  0.0133  77  LEU A N   
661  C CA  . LEU A 77  ? 0.2430 0.3154 0.2444 -0.0301 0.0227  0.0143  77  LEU A CA  
662  C C   . LEU A 77  ? 0.2658 0.3470 0.2664 -0.0323 0.0263  0.0188  77  LEU A C   
663  O O   . LEU A 77  ? 0.2312 0.3174 0.2359 -0.0336 0.0283  0.0174  77  LEU A O   
664  C CB  . LEU A 77  ? 0.3050 0.3669 0.3102 -0.0322 0.0214  0.0171  77  LEU A CB  
665  C CG  . LEU A 77  ? 0.3677 0.4276 0.3795 -0.0347 0.0219  0.0160  77  LEU A CG  
666  C CD1 . LEU A 77  ? 0.2201 0.2837 0.2342 -0.0325 0.0212  0.0097  77  LEU A CD1 
667  C CD2 . LEU A 77  ? 0.2791 0.3281 0.2930 -0.0359 0.0201  0.0172  77  LEU A CD2 
668  N N   . GLU A 78  ? 0.2453 0.3294 0.2411 -0.0325 0.0272  0.0245  78  GLU A N   
669  C CA  . GLU A 78  ? 0.2571 0.3503 0.2514 -0.0344 0.0310  0.0292  78  GLU A CA  
670  C C   . GLU A 78  ? 0.2639 0.3690 0.2563 -0.0328 0.0326  0.0237  78  GLU A C   
671  O O   . GLU A 78  ? 0.3294 0.4420 0.3239 -0.0346 0.0359  0.0247  78  GLU A O   
672  C CB  . GLU A 78  ? 0.3011 0.3959 0.2896 -0.0339 0.0316  0.0370  78  GLU A CB  
673  C CG  . GLU A 78  ? 0.5244 0.6079 0.5161 -0.0359 0.0317  0.0441  78  GLU A CG  
674  C CD  . GLU A 78  ? 0.6801 0.7640 0.6662 -0.0339 0.0315  0.0519  78  GLU A CD  
675  O OE1 . GLU A 78  ? 0.6981 0.7714 0.6867 -0.0342 0.0310  0.0568  78  GLU A OE1 
676  O OE2 . GLU A 78  ? 0.6046 0.6999 0.5839 -0.0319 0.0319  0.0531  78  GLU A OE2 
677  N N   . ALA A 79  ? 0.2483 0.3553 0.2372 -0.0295 0.0306  0.0174  79  ALA A N   
678  C CA  . ALA A 79  ? 0.2318 0.3488 0.2195 -0.0277 0.0324  0.0110  79  ALA A CA  
679  C C   . ALA A 79  ? 0.2298 0.3453 0.2246 -0.0273 0.0330  0.0062  79  ALA A C   
680  O O   . ALA A 79  ? 0.2055 0.3303 0.2015 -0.0266 0.0358  0.0031  79  ALA A O   
681  C CB  . ALA A 79  ? 0.2618 0.3802 0.2448 -0.0247 0.0303  0.0047  79  ALA A CB  
682  N N   . ILE A 80  ? 0.1518 0.2569 0.1515 -0.0275 0.0306  0.0055  80  ILE A N   
683  C CA  . ILE A 80  ? 0.1993 0.3044 0.2058 -0.0270 0.0310  0.0021  80  ILE A CA  
684  C C   . ILE A 80  ? 0.1847 0.2956 0.1953 -0.0306 0.0336  0.0064  80  ILE A C   
685  O O   . ILE A 80  ? 0.1941 0.3131 0.2089 -0.0300 0.0356  0.0038  80  ILE A O   
686  C CB  . ILE A 80  ? 0.1716 0.2650 0.1813 -0.0263 0.0276  0.0008  80  ILE A CB  
687  C CG1 . ILE A 80  ? 0.3289 0.4175 0.3359 -0.0228 0.0257  -0.0046 80  ILE A CG1 
688  C CG2 . ILE A 80  ? 0.1509 0.2453 0.1678 -0.0265 0.0277  -0.0006 80  ILE A CG2 
689  C CD1 . ILE A 80  ? 0.4691 0.5610 0.4787 -0.0194 0.0269  -0.0106 80  ILE A CD1 
690  N N   . ARG A 81  ? 0.1776 0.2846 0.1880 -0.0343 0.0339  0.0129  81  ARG A N   
691  C CA  . ARG A 81  ? 0.2394 0.3502 0.2549 -0.0387 0.0366  0.0168  81  ARG A CA  
692  C C   . ARG A 81  ? 0.2176 0.3417 0.2319 -0.0396 0.0409  0.0183  81  ARG A C   
693  O O   . ARG A 81  ? 0.2667 0.3980 0.2868 -0.0419 0.0432  0.0181  81  ARG A O   
694  C CB  . ARG A 81  ? 0.2081 0.3096 0.2238 -0.0425 0.0365  0.0234  81  ARG A CB  
695  C CG  . ARG A 81  ? 0.3135 0.4177 0.3351 -0.0480 0.0399  0.0275  81  ARG A CG  
696  C CD  . ARG A 81  ? 0.4500 0.5434 0.4722 -0.0516 0.0404  0.0339  81  ARG A CD  
697  N NE  . ARG A 81  ? 0.4317 0.5138 0.4572 -0.0518 0.0371  0.0311  81  ARG A NE  
698  C CZ  . ARG A 81  ? 0.4885 0.5700 0.5212 -0.0547 0.0366  0.0275  81  ARG A CZ  
699  N NH1 . ARG A 81  ? 0.6176 0.7093 0.6555 -0.0577 0.0390  0.0262  81  ARG A NH1 
700  N NH2 . ARG A 81  ? 0.3774 0.4494 0.4120 -0.0547 0.0336  0.0250  81  ARG A NH2 
701  N N   . LYS A 82  ? 0.1852 0.3140 0.1920 -0.0378 0.0419  0.0197  82  LYS A N   
702  C CA  . LYS A 82  ? 0.2336 0.3754 0.2378 -0.0389 0.0462  0.0223  82  LYS A CA  
703  C C   . LYS A 82  ? 0.1694 0.3222 0.1776 -0.0374 0.0483  0.0162  82  LYS A C   
704  O O   . LYS A 82  ? 0.2172 0.3689 0.2271 -0.0335 0.0464  0.0091  82  LYS A O   
705  C CB  . LYS A 82  ? 0.3056 0.4520 0.3003 -0.0363 0.0461  0.0229  82  LYS A CB  
706  C CG  . LYS A 82  ? 0.3555 0.4967 0.3452 -0.0375 0.0454  0.0310  82  LYS A CG  
707  C CD  . LYS A 82  ? 0.2924 0.4418 0.2730 -0.0342 0.0449  0.0295  82  LYS A CD  
708  C CE  . LYS A 82  ? 0.5821 0.7288 0.5568 -0.0343 0.0439  0.0380  82  LYS A CE  
709  N NZ  . LYS A 82  ? 0.6751 0.8358 0.6408 -0.0321 0.0449  0.0376  82  LYS A NZ  
710  N N   . ASP A 83  ? 0.1548 0.3188 0.1646 -0.0401 0.0527  0.0193  83  ASP A N   
711  C CA  . ASP A 83  ? 0.1944 0.3716 0.2063 -0.0378 0.0554  0.0137  83  ASP A CA  
712  C C   . ASP A 83  ? 0.2590 0.4402 0.2634 -0.0331 0.0551  0.0083  83  ASP A C   
713  O O   . ASP A 83  ? 0.2895 0.4711 0.2858 -0.0333 0.0550  0.0117  83  ASP A O   
714  C CB  . ASP A 83  ? 0.2330 0.4226 0.2463 -0.0419 0.0607  0.0187  83  ASP A CB  
715  C CG  . ASP A 83  ? 0.3320 0.5363 0.3490 -0.0397 0.0638  0.0129  83  ASP A CG  
716  O OD1 . ASP A 83  ? 0.2352 0.4456 0.2472 -0.0353 0.0645  0.0076  83  ASP A OD1 
717  O OD2 . ASP A 83  ? 0.3905 0.6009 0.4158 -0.0424 0.0658  0.0134  83  ASP A OD2 
718  N N   . PRO A 84  ? 0.2212 0.4053 0.2282 -0.0287 0.0549  -0.0001 84  PRO A N   
719  C CA  . PRO A 84  ? 0.2728 0.4593 0.2734 -0.0246 0.0546  -0.0065 84  PRO A CA  
720  C C   . PRO A 84  ? 0.2551 0.4554 0.2483 -0.0254 0.0583  -0.0051 84  PRO A C   
721  O O   . PRO A 84  ? 0.2568 0.4585 0.2424 -0.0237 0.0574  -0.0080 84  PRO A O   
722  C CB  . PRO A 84  ? 0.2704 0.4584 0.2772 -0.0201 0.0552  -0.0150 84  PRO A CB  
723  C CG  . PRO A 84  ? 0.2297 0.4112 0.2448 -0.0210 0.0533  -0.0128 84  PRO A CG  
724  C CD  . PRO A 84  ? 0.2252 0.4095 0.2414 -0.0268 0.0545  -0.0043 84  PRO A CD  
725  N N   . ASP A 85  ? 0.2166 0.4279 0.2119 -0.0282 0.0625  -0.0007 85  ASP A N   
726  C CA  . ASP A 85  ? 0.2311 0.4564 0.2189 -0.0292 0.0664  0.0019  85  ASP A CA  
727  C C   . ASP A 85  ? 0.2029 0.4248 0.1819 -0.0311 0.0647  0.0095  85  ASP A C   
728  O O   . ASP A 85  ? 0.1897 0.4193 0.1608 -0.0301 0.0654  0.0101  85  ASP A O   
729  C CB  . ASP A 85  ? 0.2866 0.5190 0.2791 -0.0322 0.0699  0.0067  85  ASP A CB  
730  C CG  . ASP A 85  ? 0.4111 0.6508 0.4107 -0.0294 0.0718  -0.0008 85  ASP A CG  
731  O OD1 . ASP A 85  ? 0.3851 0.6258 0.3843 -0.0246 0.0712  -0.0099 85  ASP A OD1 
732  O OD2 . ASP A 85  ? 0.4383 0.6823 0.4443 -0.0319 0.0739  0.0022  85  ASP A OD2 
733  N N   . ASP A 86  ? 0.1858 0.3935 0.1667 -0.0330 0.0614  0.0151  86  ASP A N   
734  C CA  . ASP A 86  ? 0.2805 0.4842 0.2543 -0.0342 0.0598  0.0231  86  ASP A CA  
735  C C   . ASP A 86  ? 0.2733 0.4691 0.2428 -0.0310 0.0549  0.0187  86  ASP A C   
736  O O   . ASP A 86  ? 0.3152 0.5073 0.2795 -0.0313 0.0529  0.0251  86  ASP A O   
737  C CB  . ASP A 86  ? 0.3013 0.4943 0.2802 -0.0384 0.0599  0.0326  86  ASP A CB  
738  C CG  . ASP A 86  ? 0.4412 0.6418 0.4251 -0.0426 0.0650  0.0374  86  ASP A CG  
739  O OD1 . ASP A 86  ? 0.4733 0.6852 0.4537 -0.0420 0.0679  0.0373  86  ASP A OD1 
740  O OD2 . ASP A 86  ? 0.4664 0.6586 0.4582 -0.0461 0.0651  0.0402  86  ASP A OD2 
741  N N   . LEU A 87  ? 0.2035 0.3963 0.1756 -0.0279 0.0529  0.0084  87  LEU A N   
742  C CA  . LEU A 87  ? 0.1723 0.3576 0.1411 -0.0255 0.0486  0.0037  87  LEU A CA  
743  C C   . LEU A 87  ? 0.1794 0.3766 0.1384 -0.0241 0.0488  0.0014  87  LEU A C   
744  O O   . LEU A 87  ? 0.2090 0.4193 0.1652 -0.0231 0.0520  -0.0037 87  LEU A O   
745  C CB  . LEU A 87  ? 0.1663 0.3450 0.1409 -0.0228 0.0473  -0.0065 87  LEU A CB  
746  C CG  . LEU A 87  ? 0.1774 0.3430 0.1605 -0.0236 0.0454  -0.0046 87  LEU A CG  
747  C CD1 . LEU A 87  ? 0.2364 0.3984 0.2254 -0.0203 0.0452  -0.0136 87  LEU A CD1 
748  C CD2 . LEU A 87  ? 0.1811 0.3341 0.1629 -0.0244 0.0412  -0.0007 87  LEU A CD2 
749  N N   . GLU A 88  ? 0.1836 0.3771 0.1376 -0.0238 0.0453  0.0046  88  GLU A N   
750  C CA  . GLU A 88  ? 0.1881 0.3925 0.1335 -0.0222 0.0443  0.0003  88  GLU A CA  
751  C C   . GLU A 88  ? 0.2548 0.4565 0.2022 -0.0202 0.0429  -0.0130 88  GLU A C   
752  O O   . GLU A 88  ? 0.2098 0.3978 0.1643 -0.0197 0.0412  -0.0165 88  GLU A O   
753  C CB  . GLU A 88  ? 0.2513 0.4527 0.1918 -0.0221 0.0406  0.0075  88  GLU A CB  
754  C CG  . GLU A 88  ? 0.3188 0.5206 0.2576 -0.0237 0.0420  0.0215  88  GLU A CG  
755  C CD  . GLU A 88  ? 0.4329 0.6261 0.3703 -0.0229 0.0381  0.0283  88  GLU A CD  
756  O OE1 . GLU A 88  ? 0.5525 0.7453 0.4882 -0.0236 0.0392  0.0401  88  GLU A OE1 
757  O OE2 . GLU A 88  ? 0.4200 0.6070 0.3586 -0.0216 0.0341  0.0219  88  GLU A OE2 
758  N N   . LYS A 89  ? 0.2236 0.4281 0.1560 -0.0486 0.0221  0.0223  89  LYS A N   
759  C CA  . LYS A 89  ? 0.2243 0.4259 0.1557 -0.0523 0.0202  0.0037  89  LYS A CA  
760  C C   . LYS A 89  ? 0.2514 0.4455 0.1946 -0.0511 0.0141  0.0067  89  LYS A C   
761  O O   . LYS A 89  ? 0.2627 0.4398 0.2120 -0.0520 0.0149  -0.0053 89  LYS A O   
762  C CB  . LYS A 89  ? 0.2433 0.4697 0.1565 -0.0606 0.0181  -0.0051 89  LYS A CB  
763  C CG  . LYS A 89  ? 0.2899 0.5233 0.1902 -0.0618 0.0262  -0.0131 89  LYS A CG  
764  C CD  . LYS A 89  ? 0.3115 0.5647 0.1911 -0.0712 0.0253  -0.0279 89  LYS A CD  
765  C CE  . LYS A 89  ? 0.4801 0.7502 0.3442 -0.0724 0.0328  -0.0304 89  LYS A CE  
766  N NZ  . LYS A 89  ? 0.5445 0.7987 0.4162 -0.0647 0.0436  -0.0371 89  LYS A NZ  
767  N N   . GLU A 90  ? 0.2401 0.4478 0.1867 -0.0483 0.0087  0.0236  90  GLU A N   
768  C CA  . GLU A 90  ? 0.2670 0.4727 0.2263 -0.0461 0.0039  0.0270  90  GLU A CA  
769  C C   . GLU A 90  ? 0.2452 0.4208 0.2176 -0.0400 0.0083  0.0266  90  GLU A C   
770  O O   . GLU A 90  ? 0.2037 0.3718 0.1846 -0.0410 0.0069  0.0205  90  GLU A O   
771  C CB  . GLU A 90  ? 0.3081 0.5346 0.2704 -0.0400 -0.0013 0.0477  90  GLU A CB  
772  C CG  . GLU A 90  ? 0.5686 0.8308 0.5185 -0.0472 -0.0078 0.0484  90  GLU A CG  
773  C CD  . GLU A 90  ? 0.7841 1.0702 0.7364 -0.0390 -0.0129 0.0719  90  GLU A CD  
774  O OE1 . GLU A 90  ? 0.7877 1.1022 0.7263 -0.0427 -0.0169 0.0785  90  GLU A OE1 
775  O OE2 . GLU A 90  ? 0.8572 1.1348 0.8242 -0.0280 -0.0127 0.0843  90  GLU A OE2 
776  N N   . GLU A 91  ? 0.2258 0.3858 0.1989 -0.0354 0.0137  0.0332  91  GLU A N   
777  C CA  . GLU A 91  ? 0.1820 0.3158 0.1651 -0.0316 0.0176  0.0317  91  GLU A CA  
778  C C   . GLU A 91  ? 0.1822 0.3049 0.1662 -0.0348 0.0200  0.0149  91  GLU A C   
779  O O   . GLU A 91  ? 0.1876 0.2944 0.1798 -0.0332 0.0204  0.0112  91  GLU A O   
780  C CB  . GLU A 91  ? 0.2238 0.3458 0.2056 -0.0293 0.0225  0.0422  91  GLU A CB  
781  C CG  . GLU A 91  ? 0.2607 0.3822 0.2423 -0.0238 0.0220  0.0603  91  GLU A CG  
782  C CD  . GLU A 91  ? 0.3484 0.4536 0.3258 -0.0245 0.0278  0.0701  91  GLU A CD  
783  O OE1 . GLU A 91  ? 0.3451 0.4586 0.3148 -0.0305 0.0303  0.0693  91  GLU A OE1 
784  O OE2 . GLU A 91  ? 0.3215 0.4053 0.3026 -0.0199 0.0307  0.0781  91  GLU A OE2 
785  N N   . VAL A 92  ? 0.2038 0.3343 0.1789 -0.0383 0.0221  0.0051  92  VAL A N   
786  C CA  . VAL A 92  ? 0.2067 0.3244 0.1822 -0.0385 0.0253  -0.0102 92  VAL A CA  
787  C C   . VAL A 92  ? 0.2402 0.3533 0.2160 -0.0430 0.0218  -0.0188 92  VAL A C   
788  O O   . VAL A 92  ? 0.2080 0.3024 0.1895 -0.0418 0.0231  -0.0245 92  VAL A O   
789  C CB  . VAL A 92  ? 0.2164 0.3431 0.1814 -0.0394 0.0302  -0.0197 92  VAL A CB  
790  C CG1 . VAL A 92  ? 0.2495 0.3592 0.2152 -0.0365 0.0347  -0.0348 92  VAL A CG1 
791  C CG2 . VAL A 92  ? 0.2281 0.3627 0.1940 -0.0371 0.0343  -0.0105 92  VAL A CG2 
792  N N   . GLU A 93  ? 0.2117 0.3437 0.1809 -0.0494 0.0170  -0.0190 93  GLU A N   
793  C CA  . GLU A 93  ? 0.1985 0.3300 0.1679 -0.0572 0.0133  -0.0271 93  GLU A CA  
794  C C   . GLU A 93  ? 0.2571 0.3800 0.2410 -0.0542 0.0114  -0.0192 93  GLU A C   
795  O O   . GLU A 93  ? 0.2628 0.3717 0.2494 -0.0586 0.0119  -0.0269 93  GLU A O   
796  C CB  . GLU A 93  ? 0.2406 0.4019 0.2014 -0.0659 0.0071  -0.0264 93  GLU A CB  
797  C CG  . GLU A 93  ? 0.3744 0.5440 0.3171 -0.0717 0.0095  -0.0384 93  GLU A CG  
798  C CD  . GLU A 93  ? 0.5966 0.8013 0.5291 -0.0811 0.0022  -0.0360 93  GLU A CD  
799  O OE1 . GLU A 93  ? 0.5961 0.8160 0.5138 -0.0833 0.0034  -0.0382 93  GLU A OE1 
800  O OE2 . GLU A 93  ? 0.6860 0.9064 0.6254 -0.0865 -0.0048 -0.0312 93  GLU A OE2 
801  N N   . LYS A 94  ? 0.2324 0.3617 0.2243 -0.0468 0.0102  -0.0038 94  LYS A N   
802  C CA  . LYS A 94  ? 0.2556 0.3771 0.2601 -0.0428 0.0100  0.0028  94  LYS A CA  
803  C C   . LYS A 94  ? 0.2825 0.3766 0.2903 -0.0401 0.0148  -0.0023 94  LYS A C   
804  O O   . LYS A 94  ? 0.2447 0.3298 0.2586 -0.0414 0.0151  -0.0040 94  LYS A O   
805  C CB  . LYS A 94  ? 0.2573 0.3862 0.2674 -0.0337 0.0098  0.0193  94  LYS A CB  
806  C CG  . LYS A 94  ? 0.3792 0.5392 0.3895 -0.0337 0.0042  0.0285  94  LYS A CG  
807  C CD  . LYS A 94  ? 0.4886 0.6498 0.5057 -0.0213 0.0056  0.0463  94  LYS A CD  
808  C CE  . LYS A 94  ? 0.4701 0.6664 0.4901 -0.0185 -0.0006 0.0581  94  LYS A CE  
809  N NZ  . LYS A 94  ? 0.5257 0.7428 0.5323 -0.0257 -0.0050 0.0569  94  LYS A NZ  
810  N N   . LEU A 95  ? 0.1924 0.2767 0.1965 -0.0364 0.0185  -0.0034 95  LEU A N   
811  C CA  . LEU A 95  ? 0.2080 0.2723 0.2153 -0.0335 0.0220  -0.0072 95  LEU A CA  
812  C C   . LEU A 95  ? 0.1955 0.2482 0.1999 -0.0368 0.0231  -0.0190 95  LEU A C   
813  O O   . LEU A 95  ? 0.1877 0.2250 0.1962 -0.0357 0.0242  -0.0197 95  LEU A O   
814  C CB  . LEU A 95  ? 0.2294 0.2939 0.2343 -0.0301 0.0253  -0.0054 95  LEU A CB  
815  C CG  . LEU A 95  ? 0.4388 0.4915 0.4478 -0.0267 0.0282  -0.0066 95  LEU A CG  
816  C CD1 . LEU A 95  ? 0.3573 0.3990 0.3719 -0.0261 0.0275  -0.0011 95  LEU A CD1 
817  C CD2 . LEU A 95  ? 0.5058 0.5677 0.5134 -0.0260 0.0309  -0.0034 95  LEU A CD2 
818  N N   . ILE A 96  ? 0.1964 0.2539 0.1918 -0.0410 0.0235  -0.0284 96  ILE A N   
819  C CA  . ILE A 96  ? 0.2461 0.2866 0.2360 -0.0451 0.0257  -0.0406 96  ILE A CA  
820  C C   . ILE A 96  ? 0.2757 0.3134 0.2690 -0.0535 0.0226  -0.0405 96  ILE A C   
821  O O   . ILE A 96  ? 0.2623 0.2790 0.2563 -0.0549 0.0248  -0.0438 96  ILE A O   
822  C CB  . ILE A 96  ? 0.3118 0.3577 0.2884 -0.0498 0.0275  -0.0526 96  ILE A CB  
823  C CG1 . ILE A 96  ? 0.4198 0.4709 0.3938 -0.0412 0.0321  -0.0530 96  ILE A CG1 
824  C CG2 . ILE A 96  ? 0.3175 0.3394 0.2861 -0.0554 0.0310  -0.0665 96  ILE A CG2 
825  C CD1 . ILE A 96  ? 0.5170 0.5486 0.4942 -0.0316 0.0380  -0.0565 96  ILE A CD1 
826  N N   . GLU A 97  ? 0.2375 0.2985 0.2331 -0.0592 0.0175  -0.0355 97  GLU A N   
827  C CA  . GLU A 97  ? 0.2091 0.2755 0.2095 -0.0684 0.0146  -0.0352 97  GLU A CA  
828  C C   . GLU A 97  ? 0.2149 0.2708 0.2261 -0.0630 0.0162  -0.0269 97  GLU A C   
829  O O   . GLU A 97  ? 0.2682 0.3147 0.2813 -0.0699 0.0170  -0.0292 97  GLU A O   
830  C CB  . GLU A 97  ? 0.2686 0.3694 0.2717 -0.0726 0.0085  -0.0290 97  GLU A CB  
831  C CG  . GLU A 97  ? 0.4568 0.5733 0.4683 -0.0815 0.0052  -0.0264 97  GLU A CG  
832  C CD  . GLU A 97  ? 0.5531 0.7097 0.5691 -0.0830 -0.0013 -0.0181 97  GLU A CD  
833  O OE1 . GLU A 97  ? 0.5917 0.7705 0.6164 -0.0906 -0.0047 -0.0153 97  GLU A OE1 
834  O OE2 . GLU A 97  ? 0.5971 0.7654 0.6084 -0.0766 -0.0029 -0.0132 97  GLU A OE2 
835  N N   . PHE A 98  ? 0.1887 0.2455 0.2052 -0.0521 0.0173  -0.0176 98  PHE A N   
836  C CA  . PHE A 98  ? 0.1719 0.2184 0.1957 -0.0471 0.0195  -0.0112 98  PHE A CA  
837  C C   . PHE A 98  ? 0.2140 0.2358 0.2343 -0.0467 0.0227  -0.0160 98  PHE A C   
838  O O   . PHE A 98  ? 0.2454 0.2583 0.2684 -0.0491 0.0240  -0.0142 98  PHE A O   
839  C CB  . PHE A 98  ? 0.2280 0.2770 0.2543 -0.0377 0.0206  -0.0027 98  PHE A CB  
840  C CG  . PHE A 98  ? 0.2958 0.3369 0.3274 -0.0334 0.0233  0.0030  98  PHE A CG  
841  C CD1 . PHE A 98  ? 0.2298 0.2826 0.2684 -0.0320 0.0237  0.0087  98  PHE A CD1 
842  C CD2 . PHE A 98  ? 0.2271 0.2520 0.2562 -0.0306 0.0258  0.0025  98  PHE A CD2 
843  C CE1 . PHE A 98  ? 0.2864 0.3313 0.3279 -0.0275 0.0277  0.0124  98  PHE A CE1 
844  C CE2 . PHE A 98  ? 0.3367 0.3548 0.3676 -0.0281 0.0285  0.0062  98  PHE A CE2 
845  C CZ  . PHE A 98  ? 0.2522 0.2785 0.2885 -0.0265 0.0301  0.0104  98  PHE A CZ  
846  N N   . THR A 99  ? 0.2452 0.2576 0.2597 -0.0428 0.0244  -0.0210 99  THR A N   
847  C CA  . THR A 99  ? 0.2151 0.2054 0.2268 -0.0397 0.0276  -0.0242 99  THR A CA  
848  C C   . THR A 99  ? 0.2513 0.2265 0.2584 -0.0486 0.0287  -0.0303 99  THR A C   
849  O O   . THR A 99  ? 0.2862 0.2452 0.2938 -0.0488 0.0305  -0.0273 99  THR A O   
850  C CB  . THR A 99  ? 0.2612 0.2487 0.2687 -0.0325 0.0301  -0.0289 99  THR A CB  
851  O OG1 . THR A 99  ? 0.2425 0.2456 0.2537 -0.0276 0.0292  -0.0230 99  THR A OG1 
852  C CG2 . THR A 99  ? 0.2393 0.2073 0.2465 -0.0251 0.0335  -0.0287 99  THR A CG2 
853  N N   . LYS A 100 ? 0.2287 0.2093 0.2299 -0.0578 0.0277  -0.0388 100 LYS A N   
854  C CA  . LYS A 100 ? 0.2389 0.2027 0.2336 -0.0699 0.0293  -0.0464 100 LYS A CA  
855  C C   . LYS A 100 ? 0.2655 0.2359 0.2675 -0.0783 0.0275  -0.0396 100 LYS A C   
856  O O   . LYS A 100 ? 0.3012 0.2510 0.2995 -0.0859 0.0303  -0.0412 100 LYS A O   
857  C CB  . LYS A 100 ? 0.2898 0.2627 0.2752 -0.0811 0.0278  -0.0580 100 LYS A CB  
858  C CG  . LYS A 100 ? 0.4174 0.3731 0.3911 -0.0753 0.0328  -0.0690 100 LYS A CG  
859  C CD  . LYS A 100 ? 0.5327 0.4978 0.4938 -0.0882 0.0317  -0.0822 100 LYS A CD  
860  C CE  . LYS A 100 ? 0.6182 0.5680 0.5670 -0.0805 0.0382  -0.0938 100 LYS A CE  
861  N NZ  . LYS A 100 ? 0.7203 0.6352 0.6530 -0.0896 0.0448  -0.1101 100 LYS A NZ  
862  N N   . LEU A 101 ? 0.2758 0.2740 0.2877 -0.0764 0.0240  -0.0315 101 LEU A N   
863  C CA  . LEU A 101 ? 0.2482 0.2572 0.2686 -0.0820 0.0237  -0.0247 101 LEU A CA  
864  C C   . LEU A 101 ? 0.2428 0.2308 0.2634 -0.0769 0.0276  -0.0191 101 LEU A C   
865  O O   . LEU A 101 ? 0.3195 0.3027 0.3410 -0.0857 0.0294  -0.0170 101 LEU A O   
866  C CB  . LEU A 101 ? 0.2904 0.3303 0.3212 -0.0756 0.0208  -0.0166 101 LEU A CB  
867  C CG  . LEU A 101 ? 0.3728 0.4315 0.4146 -0.0780 0.0215  -0.0091 101 LEU A CG  
868  C CD1 . LEU A 101 ? 0.3461 0.4183 0.3895 -0.0955 0.0198  -0.0131 101 LEU A CD1 
869  C CD2 . LEU A 101 ? 0.2946 0.3788 0.3455 -0.0671 0.0201  -0.0008 101 LEU A CD2 
870  N N   . ASN A 102 ? 0.2421 0.2198 0.2613 -0.0642 0.0287  -0.0162 102 ASN A N   
871  C CA  . ASN A 102 ? 0.2554 0.2210 0.2747 -0.0584 0.0310  -0.0093 102 ASN A CA  
872  C C   . ASN A 102 ? 0.2419 0.1804 0.2537 -0.0546 0.0334  -0.0104 102 ASN A C   
873  O O   . ASN A 102 ? 0.2085 0.1382 0.2192 -0.0496 0.0346  -0.0033 102 ASN A O   
874  C CB  . ASN A 102 ? 0.2118 0.1886 0.2348 -0.0481 0.0302  -0.0045 102 ASN A CB  
875  C CG  . ASN A 102 ? 0.2285 0.2262 0.2586 -0.0486 0.0298  -0.0011 102 ASN A CG  
876  O OD1 . ASN A 102 ? 0.2892 0.2929 0.3229 -0.0527 0.0317  0.0021  102 ASN A OD1 
877  N ND2 . ASN A 102 ? 0.2113 0.2203 0.2433 -0.0435 0.0283  -0.0007 102 ASN A ND2 
878  N N   . TYR A 103 ? 0.2753 0.2008 0.2810 -0.0567 0.0345  -0.0189 103 TYR A N   
879  C CA  . TYR A 103 ? 0.3502 0.2503 0.3492 -0.0483 0.0380  -0.0209 103 TYR A CA  
880  C C   . TYR A 103 ? 0.3126 0.1882 0.3076 -0.0481 0.0411  -0.0136 103 TYR A C   
881  O O   . TYR A 103 ? 0.3197 0.1827 0.3132 -0.0354 0.0428  -0.0081 103 TYR A O   
882  C CB  . TYR A 103 ? 0.3084 0.1966 0.2991 -0.0540 0.0403  -0.0339 103 TYR A CB  
883  C CG  . TYR A 103 ? 0.4078 0.2674 0.3908 -0.0437 0.0460  -0.0383 103 TYR A CG  
884  C CD1 . TYR A 103 ? 0.4143 0.2379 0.3890 -0.0459 0.0512  -0.0382 103 TYR A CD1 
885  C CD2 . TYR A 103 ? 0.4495 0.3175 0.4333 -0.0311 0.0472  -0.0421 103 TYR A CD2 
886  C CE1 . TYR A 103 ? 0.5065 0.3012 0.4741 -0.0331 0.0578  -0.0416 103 TYR A CE1 
887  C CE2 . TYR A 103 ? 0.5324 0.3769 0.5104 -0.0190 0.0537  -0.0462 103 TYR A CE2 
888  C CZ  . TYR A 103 ? 0.5839 0.3908 0.5540 -0.0187 0.0592  -0.0459 103 TYR A CZ  
889  O OH  . TYR A 103 ? 0.5638 0.3451 0.5284 -0.0032 0.0669  -0.0491 103 TYR A OH  
890  N N   . GLU A 104 ? 0.3157 0.1857 0.3089 -0.0620 0.0420  -0.0125 104 GLU A N   
891  C CA  . GLU A 104 ? 0.3521 0.1954 0.3391 -0.0638 0.0458  -0.0049 104 GLU A CA  
892  C C   . GLU A 104 ? 0.2879 0.1443 0.2788 -0.0605 0.0444  0.0078  104 GLU A C   
893  O O   . GLU A 104 ? 0.3272 0.1644 0.3122 -0.0604 0.0471  0.0169  104 GLU A O   
894  C CB  . GLU A 104 ? 0.3785 0.2071 0.3596 -0.0837 0.0486  -0.0100 104 GLU A CB  
895  C CG  . GLU A 104 ? 0.4363 0.2479 0.4092 -0.0904 0.0507  -0.0247 104 GLU A CG  
896  C CD  . GLU A 104 ? 0.6624 0.4308 0.6240 -0.0803 0.0571  -0.0263 104 GLU A CD  
897  O OE1 . GLU A 104 ? 0.7892 0.5381 0.7487 -0.0720 0.0598  -0.0140 104 GLU A OE1 
898  O OE2 . GLU A 104 ? 0.7459 0.4997 0.6998 -0.0801 0.0600  -0.0395 104 GLU A OE2 
899  N N   . LYS A 105 ? 0.2565 0.1426 0.2552 -0.0578 0.0409  0.0088  105 LYS A N   
900  C CA  . LYS A 105 ? 0.2405 0.1376 0.2401 -0.0555 0.0406  0.0185  105 LYS A CA  
901  C C   . LYS A 105 ? 0.2931 0.1847 0.2895 -0.0418 0.0393  0.0255  105 LYS A C   
902  O O   . LYS A 105 ? 0.2524 0.1461 0.2511 -0.0322 0.0376  0.0221  105 LYS A O   
903  C CB  . LYS A 105 ? 0.2143 0.1402 0.2215 -0.0560 0.0387  0.0163  105 LYS A CB  
904  C CG  . LYS A 105 ? 0.2548 0.1942 0.2678 -0.0674 0.0394  0.0117  105 LYS A CG  
905  C CD  . LYS A 105 ? 0.2834 0.2484 0.3045 -0.0631 0.0379  0.0098  105 LYS A CD  
906  C CE  . LYS A 105 ? 0.2481 0.2329 0.2771 -0.0726 0.0378  0.0071  105 LYS A CE  
907  N NZ  . LYS A 105 ? 0.2451 0.2533 0.2822 -0.0655 0.0370  0.0078  105 LYS A NZ  
908  N N   . PRO A 106 ? 0.2905 0.1788 0.2818 -0.0410 0.0399  0.0361  106 PRO A N   
909  C CA  . PRO A 106 ? 0.2561 0.1448 0.2447 -0.0281 0.0375  0.0444  106 PRO A CA  
910  C C   . PRO A 106 ? 0.2326 0.1462 0.2265 -0.0222 0.0334  0.0411  106 PRO A C   
911  O O   . PRO A 106 ? 0.2689 0.1871 0.2639 -0.0115 0.0309  0.0451  106 PRO A O   
912  C CB  . PRO A 106 ? 0.2684 0.1556 0.2492 -0.0320 0.0386  0.0564  106 PRO A CB  
913  C CG  . PRO A 106 ? 0.3356 0.2064 0.3138 -0.0452 0.0434  0.0554  106 PRO A CG  
914  C CD  . PRO A 106 ? 0.2637 0.1475 0.2504 -0.0522 0.0432  0.0421  106 PRO A CD  
915  N N   . ILE A 107 ? 0.2132 0.1431 0.2104 -0.0285 0.0330  0.0345  107 ILE A N   
916  C CA  . ILE A 107 ? 0.1966 0.1448 0.1968 -0.0247 0.0299  0.0313  107 ILE A CA  
917  C C   . ILE A 107 ? 0.2328 0.1822 0.2392 -0.0190 0.0289  0.0253  107 ILE A C   
918  O O   . ILE A 107 ? 0.2076 0.1715 0.2166 -0.0158 0.0265  0.0241  107 ILE A O   
919  C CB  . ILE A 107 ? 0.2533 0.2132 0.2538 -0.0314 0.0313  0.0265  107 ILE A CB  
920  C CG1 . ILE A 107 ? 0.2033 0.1625 0.2099 -0.0353 0.0335  0.0203  107 ILE A CG1 
921  C CG2 . ILE A 107 ? 0.2060 0.1681 0.1987 -0.0362 0.0334  0.0315  107 ILE A CG2 
922  C CD1 . ILE A 107 ? 0.2078 0.1785 0.2165 -0.0371 0.0354  0.0168  107 ILE A CD1 
923  N N   . TYR A 108 ? 0.2432 0.1782 0.2506 -0.0191 0.0311  0.0210  108 TYR A N   
924  C CA  . TYR A 108 ? 0.2249 0.1594 0.2355 -0.0134 0.0314  0.0146  108 TYR A CA  
925  C C   . TYR A 108 ? 0.2846 0.2046 0.2937 -0.0023 0.0332  0.0180  108 TYR A C   
926  O O   . TYR A 108 ? 0.2897 0.2053 0.3000 0.0034  0.0354  0.0117  108 TYR A O   
927  C CB  . TYR A 108 ? 0.2160 0.1458 0.2267 -0.0213 0.0330  0.0057  108 TYR A CB  
928  C CG  . TYR A 108 ? 0.1931 0.1428 0.2081 -0.0252 0.0310  0.0023  108 TYR A CG  
929  C CD1 . TYR A 108 ? 0.1911 0.1497 0.2075 -0.0302 0.0307  0.0053  108 TYR A CD1 
930  C CD2 . TYR A 108 ? 0.1951 0.1537 0.2119 -0.0227 0.0305  -0.0032 108 TYR A CD2 
931  C CE1 . TYR A 108 ? 0.2102 0.1830 0.2301 -0.0312 0.0301  0.0037  108 TYR A CE1 
932  C CE2 . TYR A 108 ? 0.2345 0.2087 0.2541 -0.0253 0.0291  -0.0038 108 TYR A CE2 
933  C CZ  . TYR A 108 ? 0.2106 0.1901 0.2319 -0.0288 0.0290  0.0000  108 TYR A CZ  
934  O OH  . TYR A 108 ? 0.2028 0.1936 0.2263 -0.0291 0.0288  0.0007  108 TYR A OH  
935  N N   . ARG A 109 ? 0.2707 0.1840 0.2767 0.0022  0.0329  0.0286  109 ARG A N   
936  C CA  . ARG A 109 ? 0.3368 0.2341 0.3415 0.0158  0.0354  0.0347  109 ARG A CA  
937  C C   . ARG A 109 ? 0.3114 0.2327 0.3240 0.0287  0.0330  0.0372  109 ARG A C   
938  O O   . ARG A 109 ? 0.3083 0.2456 0.3229 0.0356  0.0294  0.0481  109 ARG A O   
939  C CB  . ARG A 109 ? 0.3432 0.2268 0.3413 0.0167  0.0356  0.0479  109 ARG A CB  
940  C CG  . ARG A 109 ? 0.5241 0.3765 0.5180 0.0286  0.0408  0.0534  109 ARG A CG  
941  C CD  . ARG A 109 ? 0.6907 0.5249 0.6758 0.0268  0.0418  0.0677  109 ARG A CD  
942  N NE  . ARG A 109 ? 0.7498 0.5633 0.7279 0.0088  0.0452  0.0628  109 ARG A NE  
943  C CZ  . ARG A 109 ? 0.7155 0.5291 0.6875 -0.0017 0.0448  0.0713  109 ARG A CZ  
944  N NH1 . ARG A 109 ? 0.7552 0.5863 0.7252 0.0039  0.0409  0.0849  109 ARG A NH1 
945  N NH2 . ARG A 109 ? 0.6933 0.4924 0.6610 -0.0186 0.0484  0.0664  109 ARG A NH2 
946  N N   . PHE A 110 ? 0.3072 0.2351 0.3242 0.0307  0.0348  0.0271  110 PHE A N   
947  C CA  . PHE A 110 ? 0.2666 0.2167 0.2920 0.0431  0.0346  0.0282  110 PHE A CA  
948  C C   . PHE A 110 ? 0.2569 0.1871 0.2813 0.0545  0.0418  0.0216  110 PHE A C   
949  O O   . PHE A 110 ? 0.3246 0.2399 0.3436 0.0468  0.0451  0.0097  110 PHE A O   
950  C CB  . PHE A 110 ? 0.2857 0.2630 0.3158 0.0345  0.0317  0.0219  110 PHE A CB  
951  C CG  . PHE A 110 ? 0.2282 0.2225 0.2577 0.0234  0.0261  0.0261  110 PHE A CG  
952  C CD1 . PHE A 110 ? 0.2350 0.2553 0.2689 0.0260  0.0218  0.0337  110 PHE A CD1 
953  C CD2 . PHE A 110 ? 0.2338 0.2201 0.2581 0.0103  0.0256  0.0215  110 PHE A CD2 
954  C CE1 . PHE A 110 ? 0.2044 0.2375 0.2346 0.0139  0.0175  0.0350  110 PHE A CE1 
955  C CE2 . PHE A 110 ? 0.2961 0.2940 0.3180 0.0014  0.0224  0.0237  110 PHE A CE2 
956  C CZ  . PHE A 110 ? 0.2514 0.2704 0.2748 0.0023  0.0186  0.0295  110 PHE A CZ  
957  N N   . GLU A 111 ? 0.2891 0.2208 0.3184 0.0734  0.0446  0.0290  111 GLU A N   
958  C CA  . GLU A 111 ? 0.2995 0.2108 0.3271 0.0868  0.0535  0.0215  111 GLU A CA  
959  C C   . GLU A 111 ? 0.3407 0.2686 0.3703 0.0824  0.0557  0.0076  111 GLU A C   
960  O O   . GLU A 111 ? 0.3440 0.2490 0.3657 0.0829  0.0628  -0.0049 111 GLU A O   
961  C CB  . GLU A 111 ? 0.3181 0.2371 0.3539 0.1113  0.0562  0.0338  111 GLU A CB  
962  C CG  . GLU A 111 ? 0.5863 0.4969 0.6241 0.1291  0.0663  0.0257  111 GLU A CG  
963  C CD  . GLU A 111 ? 0.7606 0.6157 0.7835 0.1313  0.0760  0.0168  111 GLU A CD  
964  O OE1 . GLU A 111 ? 0.8535 0.6783 0.8664 0.1203  0.0744  0.0204  111 GLU A OE1 
965  O OE2 . GLU A 111 ? 0.8131 0.6549 0.8332 0.1426  0.0858  0.0055  111 GLU A OE2 
966  N N   . ARG A 112 ? 0.2559 0.2223 0.2940 0.0764  0.0501  0.0093  112 ARG A N   
967  C CA  . ARG A 112 ? 0.3312 0.3150 0.3705 0.0719  0.0524  -0.0014 112 ARG A CA  
968  C C   . ARG A 112 ? 0.3041 0.2706 0.3326 0.0550  0.0521  -0.0124 112 ARG A C   
969  O O   . ARG A 112 ? 0.2851 0.2519 0.3091 0.0534  0.0565  -0.0234 112 ARG A O   
970  C CB  . ARG A 112 ? 0.2176 0.2434 0.2673 0.0669  0.0466  0.0047  112 ARG A CB  
971  C CG  . ARG A 112 ? 0.2046 0.2512 0.2552 0.0596  0.0483  -0.0032 112 ARG A CG  
972  C CD  . ARG A 112 ? 0.2832 0.3329 0.3351 0.0737  0.0574  -0.0106 112 ARG A CD  
973  N NE  . ARG A 112 ? 0.3078 0.3905 0.3643 0.0688  0.0586  -0.0131 112 ARG A NE  
974  C CZ  . ARG A 112 ? 0.3364 0.4305 0.3941 0.0786  0.0669  -0.0199 112 ARG A CZ  
975  N NH1 . ARG A 112 ? 0.2589 0.3306 0.3127 0.0948  0.0752  -0.0263 112 ARG A NH1 
976  N NH2 . ARG A 112 ? 0.2738 0.3999 0.3352 0.0721  0.0680  -0.0205 112 ARG A NH2 
977  N N   . ILE A 113 ? 0.3035 0.2576 0.3276 0.0426  0.0474  -0.0095 113 ILE A N   
978  C CA  . ILE A 113 ? 0.2497 0.1921 0.2655 0.0277  0.0469  -0.0187 113 ILE A CA  
979  C C   . ILE A 113 ? 0.2633 0.1747 0.2688 0.0291  0.0536  -0.0292 113 ILE A C   
980  O O   . ILE A 113 ? 0.3567 0.2671 0.3552 0.0211  0.0553  -0.0407 113 ILE A O   
981  C CB  . ILE A 113 ? 0.3608 0.2998 0.3758 0.0157  0.0416  -0.0128 113 ILE A CB  
982  C CG1 . ILE A 113 ? 0.3586 0.3246 0.3797 0.0107  0.0365  -0.0076 113 ILE A CG1 
983  C CG2 . ILE A 113 ? 0.3279 0.2531 0.3355 0.0025  0.0420  -0.0211 113 ILE A CG2 
984  C CD1 . ILE A 113 ? 0.5096 0.4730 0.5296 0.0013  0.0330  -0.0027 113 ILE A CD1 
985  N N   . ARG A 114 ? 0.2886 0.1738 0.2918 0.0392  0.0578  -0.0253 114 ARG A N   
986  C CA  . ARG A 114 ? 0.3365 0.1853 0.3276 0.0407  0.0659  -0.0362 114 ARG A CA  
987  C C   . ARG A 114 ? 0.3958 0.2510 0.3847 0.0500  0.0727  -0.0479 114 ARG A C   
988  O O   . ARG A 114 ? 0.4255 0.2640 0.4018 0.0420  0.0773  -0.0629 114 ARG A O   
989  C CB  . ARG A 114 ? 0.3958 0.2129 0.3848 0.0530  0.0703  -0.0271 114 ARG A CB  
990  C CG  . ARG A 114 ? 0.6083 0.4197 0.5975 0.0429  0.0645  -0.0151 114 ARG A CG  
991  C CD  . ARG A 114 ? 0.8380 0.6094 0.8203 0.0515  0.0701  -0.0067 114 ARG A CD  
992  N NE  . ARG A 114 ? 0.8929 0.6785 0.8840 0.0681  0.0672  0.0115  114 ARG A NE  
993  C CZ  . ARG A 114 ? 0.8737 0.6846 0.8705 0.0622  0.0590  0.0233  114 ARG A CZ  
994  N NH1 . ARG A 114 ? 0.8259 0.6490 0.8217 0.0422  0.0539  0.0191  114 ARG A NH1 
995  N NH2 . ARG A 114 ? 0.8412 0.6670 0.8443 0.0767  0.0561  0.0393  114 ARG A NH2 
996  N N   . GLU A 115 ? 0.4692 0.3517 0.4696 0.0657  0.0734  -0.0414 115 GLU A N   
997  C CA  . GLU A 115 ? 0.4781 0.3724 0.4778 0.0756  0.0808  -0.0515 115 GLU A CA  
998  C C   . GLU A 115 ? 0.4138 0.3279 0.4079 0.0592  0.0780  -0.0615 115 GLU A C   
999  O O   . GLU A 115 ? 0.4887 0.3948 0.4714 0.0580  0.0847  -0.0762 115 GLU A O   
1000 C CB  . GLU A 115 ? 0.4977 0.4265 0.5139 0.0932  0.0810  -0.0405 115 GLU A CB  
1001 C CG  . GLU A 115 ? 0.5806 0.4998 0.6045 0.1111  0.0819  -0.0268 115 GLU A CG  
1002 C CD  . GLU A 115 ? 0.6056 0.5687 0.6474 0.1265  0.0807  -0.0154 115 GLU A CD  
1003 O OE1 . GLU A 115 ? 0.6002 0.5645 0.6502 0.1422  0.0801  -0.0018 115 GLU A OE1 
1004 O OE2 . GLU A 115 ? 0.5592 0.5577 0.6070 0.1220  0.0801  -0.0192 115 GLU A OE2 
1005 N N   . LEU A 116 ? 0.3168 0.2561 0.3174 0.0467  0.0686  -0.0537 116 LEU A N   
1006 C CA  . LEU A 116 ? 0.3297 0.2903 0.3261 0.0338  0.0658  -0.0594 116 LEU A CA  
1007 C C   . LEU A 116 ? 0.4318 0.3727 0.4137 0.0191  0.0655  -0.0709 116 LEU A C   
1008 O O   . LEU A 116 ? 0.4608 0.4112 0.4334 0.0128  0.0673  -0.0810 116 LEU A O   
1009 C CB  . LEU A 116 ? 0.3135 0.2995 0.3194 0.0257  0.0572  -0.0474 116 LEU A CB  
1010 C CG  . LEU A 116 ? 0.3019 0.3134 0.3211 0.0343  0.0560  -0.0367 116 LEU A CG  
1011 C CD1 . LEU A 116 ? 0.2408 0.2670 0.2650 0.0230  0.0482  -0.0273 116 LEU A CD1 
1012 C CD2 . LEU A 116 ? 0.2821 0.3178 0.3036 0.0410  0.0617  -0.0406 116 LEU A CD2 
1013 N N   . MET A 117 ? 0.3502 0.2666 0.3294 0.0119  0.0630  -0.0693 117 MET A N   
1014 C CA  . MET A 117 ? 0.4203 0.3222 0.3867 -0.0047 0.0622  -0.0802 117 MET A CA  
1015 C C   . MET A 117 ? 0.4779 0.3506 0.4284 -0.0032 0.0717  -0.0970 117 MET A C   
1016 O O   . MET A 117 ? 0.5703 0.4350 0.5077 -0.0194 0.0714  -0.1090 117 MET A O   
1017 C CB  . MET A 117 ? 0.4220 0.3092 0.3908 -0.0146 0.0576  -0.0733 117 MET A CB  
1018 C CG  . MET A 117 ? 0.3883 0.3026 0.3696 -0.0184 0.0492  -0.0597 117 MET A CG  
1019 S SD  . MET A 117 ? 0.4349 0.3844 0.4167 -0.0292 0.0430  -0.0605 117 MET A SD  
1020 C CE  . MET A 117 ? 0.3957 0.3689 0.3848 -0.0165 0.0438  -0.0541 117 MET A CE  
1021 N N   . ASN A 118 ? 0.4805 0.3382 0.4315 0.0156  0.0806  -0.0985 118 ASN A N   
1022 C CA  . ASN A 118 ? 0.5176 0.3444 0.4524 0.0201  0.0920  -0.1157 118 ASN A CA  
1023 C C   . ASN A 118 ? 0.5488 0.3991 0.4805 0.0287  0.0979  -0.1247 118 ASN A C   
1024 O O   . ASN A 118 ? 0.6914 0.5188 0.6116 0.0388  0.1098  -0.1383 118 ASN A O   
1025 C CB  . ASN A 118 ? 0.6172 0.4060 0.5530 0.0381  0.1003  -0.1115 118 ASN A CB  
1026 C CG  . ASN A 118 ? 0.7580 0.5160 0.6911 0.0271  0.0970  -0.1053 118 ASN A CG  
1027 O OD1 . ASN A 118 ? 0.8899 0.6507 0.8179 0.0047  0.0903  -0.1085 118 ASN A OD1 
1028 N ND2 . ASN A 118 ? 0.8540 0.5851 0.7909 0.0433  0.1017  -0.0950 118 ASN A ND2 
1029 N N   . LYS A 119 ? 0.5214 0.4152 0.4620 0.0250  0.0910  -0.1175 119 LYS A N   
1030 C CA  . LYS A 119 ? 0.5397 0.4609 0.4774 0.0307  0.0962  -0.1239 119 LYS A CA  
1031 C C   . LYS A 119 ? 0.5650 0.4989 0.4867 0.0110  0.0928  -0.1348 119 LYS A C   
1032 O O   . LYS A 119 ? 0.5037 0.4516 0.4280 -0.0042 0.0821  -0.1276 119 LYS A O   
1033 C CB  . LYS A 119 ? 0.4761 0.4374 0.4329 0.0381  0.0915  -0.1073 119 LYS A CB  
1034 C CG  . LYS A 119 ? 0.4867 0.4465 0.4597 0.0576  0.0943  -0.0963 119 LYS A CG  
1035 C CD  . LYS A 119 ? 0.5840 0.5504 0.5577 0.0770  0.1068  -0.1031 119 LYS A CD  
1036 C CE  . LYS A 119 ? 0.6325 0.6112 0.6263 0.0968  0.1076  -0.0883 119 LYS A CE  
1037 N NZ  . LYS A 119 ? 0.5412 0.5510 0.5495 0.0873  0.0955  -0.0718 119 LYS A NZ  
1038 N N   . GLU A 120 ? 0.6114 0.5433 0.5168 0.0125  0.1022  -0.1518 120 GLU A N   
1039 C CA  . GLU A 120 ? 0.6767 0.6274 0.5653 -0.0060 0.0987  -0.1616 120 GLU A CA  
1040 C C   . GLU A 120 ? 0.6075 0.6047 0.5061 -0.0093 0.0906  -0.1465 120 GLU A C   
1041 O O   . GLU A 120 ? 0.5420 0.5571 0.4363 -0.0254 0.0810  -0.1426 120 GLU A O   
1042 C CB  . GLU A 120 ? 0.7515 0.6905 0.6185 -0.0027 0.1119  -0.1838 120 GLU A CB  
1043 C CG  . GLU A 120 ? 0.7964 0.6851 0.6561 0.0057  0.1188  -0.1926 120 GLU A CG  
1044 C CD  . GLU A 120 ? 0.9885 0.8646 0.8264 0.0050  0.1249  -0.2092 120 GLU A CD  
1045 O OE1 . GLU A 120 ? 1.0086 0.8842 0.8463 0.0253  0.1351  -0.2127 120 GLU A OE1 
1046 O OE2 . GLU A 120 ? 1.0650 0.9342 0.8865 -0.0161 0.1196  -0.2189 120 GLU A OE2 
1047 N N   . LYS A 121 ? 0.5405 0.5577 0.4531 0.0058  0.0943  -0.1366 121 LYS A N   
1048 C CA  . LYS A 121 ? 0.4700 0.5271 0.3905 0.0027  0.0892  -0.1227 121 LYS A CA  
1049 C C   . LYS A 121 ? 0.4267 0.4932 0.3702 0.0136  0.0870  -0.1057 121 LYS A C   
1050 O O   . LYS A 121 ? 0.5347 0.5912 0.4870 0.0293  0.0938  -0.1067 121 LYS A O   
1051 C CB  . LYS A 121 ? 0.4927 0.5729 0.4018 0.0060  0.0985  -0.1316 121 LYS A CB  
1052 C CG  . LYS A 121 ? 0.5768 0.6914 0.4798 -0.0066 0.0927  -0.1233 121 LYS A CG  
1053 C CD  . LYS A 121 ? 0.6432 0.7772 0.5297 -0.0052 0.1030  -0.1354 121 LYS A CD  
1054 C CE  . LYS A 121 ? 0.7503 0.8607 0.6143 -0.0117 0.1055  -0.1550 121 LYS A CE  
1055 N NZ  . LYS A 121 ? 0.8011 0.9239 0.6510 -0.0094 0.1124  -0.1616 121 LYS A NZ  
1056 N N   . LEU A 122 ? 0.3818 0.4681 0.3342 0.0057  0.0781  -0.0900 122 LEU A N   
1057 C CA  . LEU A 122 ? 0.2911 0.3868 0.2627 0.0116  0.0751  -0.0749 122 LEU A CA  
1058 C C   . LEU A 122 ? 0.3320 0.4620 0.3080 0.0106  0.0773  -0.0667 122 LEU A C   
1059 O O   . LEU A 122 ? 0.3568 0.5014 0.3242 -0.0002 0.0745  -0.0629 122 LEU A O   
1060 C CB  . LEU A 122 ? 0.2932 0.3796 0.2709 0.0027  0.0646  -0.0639 122 LEU A CB  
1061 C CG  . LEU A 122 ? 0.3902 0.4460 0.3665 0.0019  0.0619  -0.0685 122 LEU A CG  
1062 C CD1 . LEU A 122 ? 0.4259 0.4798 0.4113 -0.0043 0.0532  -0.0558 122 LEU A CD1 
1063 C CD2 . LEU A 122 ? 0.3253 0.3637 0.3069 0.0165  0.0685  -0.0726 122 LEU A CD2 
1064 N N   . ASN A 123 ? 0.2595 0.4040 0.2490 0.0213  0.0823  -0.0626 123 ASN A N   
1065 C CA  . ASN A 123 ? 0.2343 0.4132 0.2300 0.0179  0.0844  -0.0536 123 ASN A CA  
1066 C C   . ASN A 123 ? 0.2012 0.3836 0.2077 0.0087  0.0759  -0.0382 123 ASN A C   
1067 O O   . ASN A 123 ? 0.2195 0.3796 0.2272 0.0053  0.0686  -0.0350 123 ASN A O   
1068 C CB  . ASN A 123 ? 0.2588 0.4590 0.2644 0.0329  0.0946  -0.0571 123 ASN A CB  
1069 C CG  . ASN A 123 ? 0.2519 0.4451 0.2741 0.0462  0.0936  -0.0531 123 ASN A CG  
1070 O OD1 . ASN A 123 ? 0.2263 0.4140 0.2572 0.0408  0.0850  -0.0430 123 ASN A OD1 
1071 N ND2 . ASN A 123 ? 0.2978 0.4918 0.3237 0.0649  0.1033  -0.0609 123 ASN A ND2 
1072 N N   . ARG A 124 ? 0.1825 0.3261 0.2445 -0.0330 0.0582  -0.0409 124 ARG A N   
1073 C CA  . ARG A 124 ? 0.1724 0.3109 0.2322 -0.0361 0.0542  -0.0322 124 ARG A CA  
1074 C C   . ARG A 124 ? 0.1789 0.3129 0.2492 -0.0324 0.0513  -0.0305 124 ARG A C   
1075 O O   . ARG A 124 ? 0.1721 0.2967 0.2406 -0.0330 0.0466  -0.0258 124 ARG A O   
1076 C CB  . ARG A 124 ? 0.2619 0.4092 0.3188 -0.0418 0.0580  -0.0287 124 ARG A CB  
1077 C CG  . ARG A 124 ? 0.2962 0.4367 0.3513 -0.0465 0.0559  -0.0212 124 ARG A CG  
1078 C CD  . ARG A 124 ? 0.2877 0.4340 0.3388 -0.0543 0.0621  -0.0185 124 ARG A CD  
1079 N NE  . ARG A 124 ? 0.2794 0.4158 0.3273 -0.0600 0.0620  -0.0124 124 ARG A NE  
1080 C CZ  . ARG A 124 ? 0.3359 0.4758 0.3949 -0.0623 0.0604  -0.0136 124 ARG A CZ  
1081 N NH1 . ARG A 124 ? 0.4064 0.5599 0.4793 -0.0574 0.0583  -0.0193 124 ARG A NH1 
1082 N NH2 . ARG A 124 ? 0.4152 0.5452 0.4708 -0.0687 0.0613  -0.0095 124 ARG A NH2 
1083 N N   . GLU A 125 ? 0.2215 0.3629 0.3021 -0.0273 0.0541  -0.0340 125 GLU A N   
1084 C CA  . GLU A 125 ? 0.2277 0.3672 0.3166 -0.0218 0.0513  -0.0315 125 GLU A CA  
1085 C C   . GLU A 125 ? 0.1922 0.3153 0.2799 -0.0171 0.0495  -0.0316 125 GLU A C   
1086 O O   . GLU A 125 ? 0.1942 0.3113 0.2837 -0.0149 0.0456  -0.0273 125 GLU A O   
1087 C CB  . GLU A 125 ? 0.2234 0.3772 0.3227 -0.0150 0.0548  -0.0346 125 GLU A CB  
1088 C CG  . GLU A 125 ? 0.4241 0.5976 0.5278 -0.0205 0.0562  -0.0348 125 GLU A CG  
1089 C CD  . GLU A 125 ? 0.6573 0.8343 0.7535 -0.0291 0.0604  -0.0364 125 GLU A CD  
1090 O OE1 . GLU A 125 ? 0.6979 0.8736 0.7909 -0.0270 0.0640  -0.0408 125 GLU A OE1 
1091 O OE2 . GLU A 125 ? 0.7205 0.9010 0.8134 -0.0380 0.0609  -0.0335 125 GLU A OE2 
1092 N N   . GLU A 126 ? 0.1861 0.3027 0.2709 -0.0164 0.0530  -0.0374 126 GLU A N   
1093 C CA  . GLU A 126 ? 0.1875 0.2882 0.2712 -0.0143 0.0530  -0.0392 126 GLU A CA  
1094 C C   . GLU A 126 ? 0.2093 0.3045 0.2863 -0.0199 0.0472  -0.0359 126 GLU A C   
1095 O O   . GLU A 126 ? 0.1636 0.2480 0.2413 -0.0185 0.0450  -0.0338 126 GLU A O   
1096 C CB  . GLU A 126 ? 0.2015 0.2986 0.2845 -0.0141 0.0597  -0.0487 126 GLU A CB  
1097 C CG  . GLU A 126 ? 0.2447 0.3401 0.3346 -0.0056 0.0667  -0.0514 126 GLU A CG  
1098 C CD  . GLU A 126 ? 0.3101 0.4076 0.3996 -0.0065 0.0742  -0.0616 126 GLU A CD  
1099 O OE1 . GLU A 126 ? 0.3374 0.4393 0.4212 -0.0141 0.0737  -0.0675 126 GLU A OE1 
1100 O OE2 . GLU A 126 ? 0.2829 0.3787 0.3777 0.0014  0.0808  -0.0640 126 GLU A OE2 
1101 N N   . LEU A 127 ? 0.1848 0.2873 0.2545 -0.0255 0.0451  -0.0351 127 LEU A N   
1102 C CA  . LEU A 127 ? 0.1847 0.2827 0.2474 -0.0286 0.0397  -0.0310 127 LEU A CA  
1103 C C   . LEU A 127 ? 0.1736 0.2670 0.2382 -0.0286 0.0358  -0.0232 127 LEU A C   
1104 O O   . LEU A 127 ? 0.2266 0.3117 0.2897 -0.0285 0.0320  -0.0207 127 LEU A O   
1105 C CB  . LEU A 127 ? 0.1982 0.3043 0.2506 -0.0321 0.0394  -0.0300 127 LEU A CB  
1106 C CG  . LEU A 127 ? 0.1983 0.3108 0.2467 -0.0326 0.0412  -0.0387 127 LEU A CG  
1107 C CD1 . LEU A 127 ? 0.2000 0.3235 0.2373 -0.0342 0.0421  -0.0370 127 LEU A CD1 
1108 C CD2 . LEU A 127 ? 0.2485 0.3570 0.2954 -0.0326 0.0375  -0.0418 127 LEU A CD2 
1109 N N   . LEU A 128 ? 0.1542 0.2548 0.2227 -0.0293 0.0370  -0.0205 128 LEU A N   
1110 C CA  . LEU A 128 ? 0.1650 0.2641 0.2365 -0.0302 0.0339  -0.0154 128 LEU A CA  
1111 C C   . LEU A 128 ? 0.1562 0.2487 0.2333 -0.0245 0.0318  -0.0151 128 LEU A C   
1112 O O   . LEU A 128 ? 0.1479 0.2345 0.2242 -0.0252 0.0280  -0.0115 128 LEU A O   
1113 C CB  . LEU A 128 ? 0.1873 0.3000 0.2645 -0.0324 0.0364  -0.0154 128 LEU A CB  
1114 C CG  . LEU A 128 ? 0.2783 0.3925 0.3502 -0.0408 0.0378  -0.0122 128 LEU A CG  
1115 C CD1 . LEU A 128 ? 0.2703 0.4013 0.3503 -0.0439 0.0415  -0.0150 128 LEU A CD1 
1116 C CD2 . LEU A 128 ? 0.2699 0.3735 0.3388 -0.0435 0.0341  -0.0079 128 LEU A CD2 
1117 N N   . ASP A 129 ? 0.1557 0.2483 0.2378 -0.0182 0.0353  -0.0187 129 ASP A N   
1118 C CA  . ASP A 129 ? 0.1722 0.2553 0.2572 -0.0117 0.0351  -0.0173 129 ASP A CA  
1119 C C   . ASP A 129 ? 0.1700 0.2393 0.2503 -0.0143 0.0340  -0.0182 129 ASP A C   
1120 O O   . ASP A 129 ? 0.1711 0.2325 0.2512 -0.0126 0.0317  -0.0149 129 ASP A O   
1121 C CB  . ASP A 129 ? 0.2035 0.2858 0.2930 -0.0035 0.0412  -0.0203 129 ASP A CB  
1122 C CG  . ASP A 129 ? 0.2491 0.3471 0.3451 0.0026  0.0413  -0.0184 129 ASP A CG  
1123 O OD1 . ASP A 129 ? 0.2482 0.3591 0.3460 -0.0017 0.0369  -0.0162 129 ASP A OD1 
1124 O OD2 . ASP A 129 ? 0.2710 0.3693 0.3705 0.0118  0.0463  -0.0199 129 ASP A OD2 
1125 N N   . LEU A 130 ? 0.1642 0.2328 0.2407 -0.0183 0.0358  -0.0234 130 LEU A N   
1126 C CA  . LEU A 130 ? 0.2213 0.2818 0.2944 -0.0212 0.0346  -0.0261 130 LEU A CA  
1127 C C   . LEU A 130 ? 0.1681 0.2279 0.2375 -0.0236 0.0282  -0.0203 130 LEU A C   
1128 O O   . LEU A 130 ? 0.1811 0.2329 0.2508 -0.0232 0.0266  -0.0194 130 LEU A O   
1129 C CB  . LEU A 130 ? 0.2104 0.2766 0.2801 -0.0251 0.0367  -0.0338 130 LEU A CB  
1130 C CG  . LEU A 130 ? 0.2195 0.2810 0.2884 -0.0280 0.0369  -0.0397 130 LEU A CG  
1131 C CD1 . LEU A 130 ? 0.2214 0.2683 0.2954 -0.0262 0.0432  -0.0427 130 LEU A CD1 
1132 C CD2 . LEU A 130 ? 0.3091 0.3819 0.3747 -0.0318 0.0384  -0.0487 130 LEU A CD2 
1133 N N   . GLN A 131 ? 0.1751 0.2417 0.2405 -0.0262 0.0256  -0.0164 131 GLN A N   
1134 C CA  . GLN A 131 ? 0.1427 0.2059 0.2039 -0.0281 0.0210  -0.0109 131 GLN A CA  
1135 C C   . GLN A 131 ? 0.1954 0.2542 0.2613 -0.0265 0.0192  -0.0074 131 GLN A C   
1136 O O   . GLN A 131 ? 0.1867 0.2389 0.2511 -0.0265 0.0162  -0.0055 131 GLN A O   
1137 C CB  . GLN A 131 ? 0.1510 0.2189 0.2067 -0.0314 0.0214  -0.0071 131 GLN A CB  
1138 C CG  . GLN A 131 ? 0.1851 0.2581 0.2329 -0.0321 0.0228  -0.0086 131 GLN A CG  
1139 C CD  . GLN A 131 ? 0.1695 0.2450 0.2115 -0.0354 0.0256  -0.0041 131 GLN A CD  
1140 O OE1 . GLN A 131 ? 0.1881 0.2682 0.2358 -0.0379 0.0285  -0.0043 131 GLN A OE1 
1141 N NE2 . GLN A 131 ? 0.1919 0.2651 0.2222 -0.0350 0.0254  0.0000  131 GLN A NE2 
1142 N N   . THR A 132 ? 0.1175 0.1827 0.1889 -0.0247 0.0207  -0.0068 132 THR A N   
1143 C CA  . THR A 132 ? 0.1302 0.1963 0.2052 -0.0230 0.0183  -0.0038 132 THR A CA  
1144 C C   . THR A 132 ? 0.1691 0.2270 0.2456 -0.0172 0.0186  -0.0035 132 THR A C   
1145 O O   . THR A 132 ? 0.1502 0.2048 0.2264 -0.0165 0.0157  -0.0008 132 THR A O   
1146 C CB  . THR A 132 ? 0.1099 0.1904 0.1909 -0.0219 0.0197  -0.0044 132 THR A CB  
1147 O OG1 . THR A 132 ? 0.1690 0.2557 0.2480 -0.0285 0.0214  -0.0052 132 THR A OG1 
1148 C CG2 . THR A 132 ? 0.1491 0.2363 0.2337 -0.0208 0.0164  -0.0026 132 THR A CG2 
1149 N N   . LEU A 133 ? 0.1920 0.2454 0.2698 -0.0133 0.0231  -0.0064 133 LEU A N   
1150 C CA  . LEU A 133 ? 0.2031 0.2447 0.2809 -0.0082 0.0257  -0.0056 133 LEU A CA  
1151 C C   . LEU A 133 ? 0.1633 0.1955 0.2378 -0.0128 0.0244  -0.0070 133 LEU A C   
1152 O O   . LEU A 133 ? 0.1942 0.2180 0.2679 -0.0105 0.0248  -0.0047 133 LEU A O   
1153 C CB  . LEU A 133 ? 0.1870 0.2228 0.2665 -0.0033 0.0331  -0.0089 133 LEU A CB  
1154 C CG  . LEU A 133 ? 0.2255 0.2700 0.3086 0.0052  0.0350  -0.0064 133 LEU A CG  
1155 C CD1 . LEU A 133 ? 0.2231 0.2627 0.3077 0.0088  0.0429  -0.0111 133 LEU A CD1 
1156 C CD2 . LEU A 133 ? 0.2616 0.3035 0.3440 0.0143  0.0346  -0.0001 133 LEU A CD2 
1157 N N   . ASN A 134 ? 0.1455 0.1806 0.2177 -0.0184 0.0229  -0.0106 134 ASN A N   
1158 C CA  . ASN A 134 ? 0.1667 0.1975 0.2365 -0.0217 0.0205  -0.0119 134 ASN A CA  
1159 C C   . ASN A 134 ? 0.1849 0.2149 0.2531 -0.0216 0.0154  -0.0063 134 ASN A C   
1160 O O   . ASN A 134 ? 0.2292 0.2529 0.2971 -0.0214 0.0149  -0.0059 134 ASN A O   
1161 C CB  . ASN A 134 ? 0.1692 0.2073 0.2358 -0.0254 0.0192  -0.0163 134 ASN A CB  
1162 C CG  . ASN A 134 ? 0.1643 0.2020 0.2329 -0.0275 0.0241  -0.0251 134 ASN A CG  
1163 O OD1 . ASN A 134 ? 0.1592 0.1946 0.2288 -0.0299 0.0248  -0.0294 134 ASN A OD1 
1164 N ND2 . ASN A 134 ? 0.1503 0.1905 0.2202 -0.0273 0.0285  -0.0290 134 ASN A ND2 
1165 N N   . LEU A 135 ? 0.1620 0.1981 0.2293 -0.0225 0.0127  -0.0029 135 LEU A N   
1166 C CA  . LEU A 135 ? 0.2055 0.2407 0.2718 -0.0235 0.0091  0.0009  135 LEU A CA  
1167 C C   . LEU A 135 ? 0.2281 0.2616 0.2971 -0.0193 0.0093  0.0027  135 LEU A C   
1168 O O   . LEU A 135 ? 0.1874 0.2157 0.2549 -0.0192 0.0076  0.0039  135 LEU A O   
1169 C CB  . LEU A 135 ? 0.2289 0.2712 0.2951 -0.0267 0.0085  0.0025  135 LEU A CB  
1170 C CG  . LEU A 135 ? 0.2828 0.3229 0.3431 -0.0310 0.0084  0.0038  135 LEU A CG  
1171 C CD1 . LEU A 135 ? 0.2304 0.2759 0.2920 -0.0356 0.0099  0.0046  135 LEU A CD1 
1172 C CD2 . LEU A 135 ? 0.2067 0.2380 0.2622 -0.0310 0.0060  0.0056  135 LEU A CD2 
1173 N N   . LEU A 136 ? 0.1409 0.1799 0.2131 -0.0149 0.0115  0.0033  136 LEU A N   
1174 C CA  . LEU A 136 ? 0.1563 0.1967 0.2294 -0.0085 0.0115  0.0063  136 LEU A CA  
1175 C C   . LEU A 136 ? 0.2327 0.2591 0.3031 -0.0048 0.0153  0.0073  136 LEU A C   
1176 O O   . LEU A 136 ? 0.1909 0.2154 0.2592 -0.0003 0.0149  0.0109  136 LEU A O   
1177 C CB  . LEU A 136 ? 0.1338 0.1850 0.2105 -0.0025 0.0133  0.0068  136 LEU A CB  
1178 C CG  . LEU A 136 ? 0.1917 0.2610 0.2724 -0.0059 0.0102  0.0055  136 LEU A CG  
1179 C CD1 . LEU A 136 ? 0.1555 0.2378 0.2408 0.0010  0.0124  0.0051  136 LEU A CD1 
1180 C CD2 . LEU A 136 ? 0.1444 0.2209 0.2249 -0.0068 0.0059  0.0064  136 LEU A CD2 
1181 N N   . ALA A 137 ? 0.1518 0.1691 0.2221 -0.0069 0.0198  0.0037  137 ALA A N   
1182 C CA  . ALA A 137 ? 0.2039 0.2070 0.2720 -0.0061 0.0249  0.0030  137 ALA A CA  
1183 C C   . ALA A 137 ? 0.2032 0.2042 0.2693 -0.0092 0.0214  0.0040  137 ALA A C   
1184 O O   . ALA A 137 ? 0.2224 0.2136 0.2859 -0.0069 0.0252  0.0059  137 ALA A O   
1185 C CB  . ALA A 137 ? 0.1811 0.1787 0.2507 -0.0111 0.0300  -0.0042 137 ALA A CB  
1186 N N   . TRP A 138 ? 0.1617 0.1703 0.2280 -0.0139 0.0152  0.0031  138 TRP A N   
1187 C CA  . TRP A 138 ? 0.1767 0.1835 0.2413 -0.0164 0.0120  0.0034  138 TRP A CA  
1188 C C   . TRP A 138 ? 0.1843 0.1962 0.2476 -0.0144 0.0079  0.0074  138 TRP A C   
1189 O O   . TRP A 138 ? 0.1736 0.1850 0.2354 -0.0169 0.0049  0.0072  138 TRP A O   
1190 C CB  . TRP A 138 ? 0.1884 0.1989 0.2528 -0.0211 0.0087  0.0001  138 TRP A CB  
1191 C CG  . TRP A 138 ? 0.1739 0.1835 0.2399 -0.0233 0.0123  -0.0057 138 TRP A CG  
1192 C CD1 . TRP A 138 ? 0.1775 0.1904 0.2448 -0.0240 0.0148  -0.0089 138 TRP A CD1 
1193 C CD2 . TRP A 138 ? 0.1791 0.1866 0.2465 -0.0259 0.0146  -0.0106 138 TRP A CD2 
1194 N NE1 . TRP A 138 ? 0.1995 0.2127 0.2687 -0.0273 0.0184  -0.0162 138 TRP A NE1 
1195 C CE2 . TRP A 138 ? 0.1822 0.1927 0.2519 -0.0288 0.0185  -0.0176 138 TRP A CE2 
1196 C CE3 . TRP A 138 ? 0.2092 0.2141 0.2764 -0.0267 0.0142  -0.0109 138 TRP A CE3 
1197 C CZ2 . TRP A 138 ? 0.2465 0.2591 0.3192 -0.0333 0.0220  -0.0257 138 TRP A CZ2 
1198 C CZ3 . TRP A 138 ? 0.2769 0.2833 0.3471 -0.0306 0.0178  -0.0181 138 TRP A CZ3 
1199 C CH2 . TRP A 138 ? 0.2687 0.2797 0.3420 -0.0343 0.0216  -0.0258 138 TRP A CH2 
1200 N N   . CYS A 139 ? 0.1605 0.1788 0.2244 -0.0098 0.0080  0.0101  139 CYS A N   
1201 C CA  . CYS A 139 ? 0.0965 0.1246 0.1599 -0.0087 0.0040  0.0119  139 CYS A CA  
1202 C C   . CYS A 139 ? 0.1001 0.1234 0.1595 -0.0059 0.0043  0.0142  139 CYS A C   
1203 O O   . CYS A 139 ? 0.1776 0.1921 0.2341 -0.0006 0.0090  0.0170  139 CYS A O   
1204 C CB  . CYS A 139 ? 0.1712 0.2122 0.2370 -0.0030 0.0039  0.0134  139 CYS A CB  
1205 S SG  . CYS A 139 ? 0.1983 0.2594 0.2660 -0.0045 -0.0014 0.0118  139 CYS A SG  
1206 N N   . GLY A 140 ? 0.1540 0.1814 0.2126 -0.0096 0.0004  0.0127  140 GLY A N   
1207 C CA  . GLY A 140 ? 0.1921 0.2175 0.2465 -0.0070 0.0003  0.0144  140 GLY A CA  
1208 C C   . GLY A 140 ? 0.1420 0.1800 0.1939 0.0001  -0.0010 0.0174  140 GLY A C   
1209 O O   . GLY A 140 ? 0.2191 0.2703 0.2736 0.0031  -0.0025 0.0175  140 GLY A O   
1210 N N   . ARG A 141 ? 0.1109 0.1463 0.1571 0.0035  -0.0002 0.0199  141 ARG A N   
1211 C CA  . ARG A 141 ? 0.1181 0.1665 0.1595 0.0124  -0.0014 0.0237  141 ARG A CA  
1212 C C   . ARG A 141 ? 0.1274 0.1993 0.1729 0.0100  -0.0075 0.0187  141 ARG A C   
1213 O O   . ARG A 141 ? 0.1264 0.2156 0.1720 0.0177  -0.0091 0.0204  141 ARG A O   
1214 C CB  . ARG A 141 ? 0.1551 0.1967 0.1890 0.0144  0.0005  0.0262  141 ARG A CB  
1215 C CG  . ARG A 141 ? 0.1699 0.2265 0.1965 0.0240  -0.0012 0.0302  141 ARG A CG  
1216 C CD  . ARG A 141 ? 0.1589 0.2062 0.1773 0.0249  0.0018  0.0327  141 ARG A CD  
1217 N NE  . ARG A 141 ? 0.1871 0.2512 0.1971 0.0346  -0.0004 0.0364  141 ARG A NE  
1218 C CZ  . ARG A 141 ? 0.2159 0.2980 0.2254 0.0312  -0.0060 0.0308  141 ARG A CZ  
1219 N NH1 . ARG A 141 ? 0.2006 0.2817 0.2171 0.0185  -0.0088 0.0218  141 ARG A NH1 
1220 N NH2 . ARG A 141 ? 0.2137 0.3146 0.2148 0.0414  -0.0082 0.0341  141 ARG A NH2 
1221 N N   . THR A 142 ? 0.1455 0.2190 0.1944 -0.0005 -0.0103 0.0120  142 THR A N   
1222 C CA  . THR A 142 ? 0.1326 0.2274 0.1856 -0.0054 -0.0143 0.0052  142 THR A CA  
1223 C C   . THR A 142 ? 0.1411 0.2479 0.2008 -0.0062 -0.0148 0.0033  142 THR A C   
1224 O O   . THR A 142 ? 0.1662 0.2974 0.2285 -0.0029 -0.0174 0.0007  142 THR A O   
1225 C CB  . THR A 142 ? 0.1695 0.2567 0.2241 -0.0171 -0.0146 -0.0015 142 THR A CB  
1226 O OG1 . THR A 142 ? 0.1997 0.2791 0.2487 -0.0159 -0.0143 -0.0008 142 THR A OG1 
1227 C CG2 . THR A 142 ? 0.1908 0.2973 0.2503 -0.0249 -0.0166 -0.0105 142 THR A CG2 
1228 N N   . LEU A 143 ? 0.1729 0.2654 0.2355 -0.0104 -0.0122 0.0040  143 LEU A N   
1229 C CA  . LEU A 143 ? 0.1668 0.2700 0.2355 -0.0116 -0.0118 0.0021  143 LEU A CA  
1230 C C   . LEU A 143 ? 0.2268 0.3345 0.2950 0.0004  -0.0105 0.0078  143 LEU A C   
1231 O O   . LEU A 143 ? 0.2135 0.3363 0.2871 0.0015  -0.0107 0.0058  143 LEU A O   
1232 C CB  . LEU A 143 ? 0.1418 0.2292 0.2123 -0.0200 -0.0092 0.0009  143 LEU A CB  
1233 C CG  . LEU A 143 ? 0.0937 0.1771 0.1646 -0.0312 -0.0089 -0.0047 143 LEU A CG  
1234 C CD1 . LEU A 143 ? 0.1032 0.1708 0.1735 -0.0363 -0.0058 -0.0036 143 LEU A CD1 
1235 C CD2 . LEU A 143 ? 0.1337 0.2388 0.2098 -0.0376 -0.0097 -0.0123 143 LEU A CD2 
1236 N N   . ARG A 144 ? 0.1892 0.2826 0.2511 0.0090  -0.0079 0.0145  144 ARG A N   
1237 C CA  . ARG A 144 ? 0.2545 0.3501 0.3145 0.0218  -0.0051 0.0204  144 ARG A CA  
1238 C C   . ARG A 144 ? 0.2656 0.3892 0.3258 0.0309  -0.0089 0.0206  144 ARG A C   
1239 O O   . ARG A 144 ? 0.2846 0.4198 0.3470 0.0401  -0.0081 0.0226  144 ARG A O   
1240 C CB  . ARG A 144 ? 0.2240 0.2969 0.2758 0.0287  0.0004  0.0273  144 ARG A CB  
1241 C CG  . ARG A 144 ? 0.3345 0.3848 0.3879 0.0228  0.0055  0.0264  144 ARG A CG  
1242 C CD  . ARG A 144 ? 0.2952 0.3238 0.3416 0.0274  0.0126  0.0313  144 ARG A CD  
1243 N NE  . ARG A 144 ? 0.3496 0.3608 0.3984 0.0213  0.0179  0.0283  144 ARG A NE  
1244 C CZ  . ARG A 144 ? 0.2826 0.2812 0.3302 0.0263  0.0256  0.0301  144 ARG A CZ  
1245 N NH1 . ARG A 144 ? 0.3415 0.3410 0.3848 0.0391  0.0290  0.0364  144 ARG A NH1 
1246 N NH2 . ARG A 144 ? 0.3092 0.2953 0.3597 0.0189  0.0301  0.0251  144 ARG A NH2 
1247 N N   . LYS A 145 ? 0.3197 0.4571 0.3780 0.0288  -0.0132 0.0176  145 LYS A N   
1248 C CA  . LYS A 145 ? 0.2744 0.4455 0.3345 0.0359  -0.0178 0.0151  145 LYS A CA  
1249 C C   . LYS A 145 ? 0.2200 0.4127 0.2916 0.0263  -0.0202 0.0055  145 LYS A C   
1250 O O   . LYS A 145 ? 0.3040 0.5217 0.3800 0.0341  -0.0218 0.0044  145 LYS A O   
1251 C CB  . LYS A 145 ? 0.4774 0.6609 0.5327 0.0348  -0.0217 0.0122  145 LYS A CB  
1252 C CG  . LYS A 145 ? 0.6377 0.8282 0.6820 0.0523  -0.0219 0.0211  145 LYS A CG  
1253 C CD  . LYS A 145 ? 0.6796 0.8359 0.7156 0.0596  -0.0147 0.0320  145 LYS A CD  
1254 C CE  . LYS A 145 ? 0.6927 0.8255 0.7258 0.0487  -0.0127 0.0307  145 LYS A CE  
1255 N NZ  . LYS A 145 ? 0.7455 0.8449 0.7737 0.0506  -0.0047 0.0379  145 LYS A NZ  
1256 N N   . ASP A 146 ? 0.2840 0.4675 0.3601 0.0098  -0.0196 -0.0016 146 ASP A N   
1257 C CA  . ASP A 146 ? 0.2265 0.4286 0.3125 -0.0017 -0.0201 -0.0115 146 ASP A CA  
1258 C C   . ASP A 146 ? 0.3420 0.5424 0.4334 -0.0008 -0.0171 -0.0102 146 ASP A C   
1259 O O   . ASP A 146 ? 0.4272 0.6527 0.5270 -0.0042 -0.0176 -0.0169 146 ASP A O   
1260 C CB  . ASP A 146 ? 0.2942 0.4812 0.3809 -0.0183 -0.0183 -0.0178 146 ASP A CB  
1261 C CG  . ASP A 146 ? 0.4135 0.6036 0.4959 -0.0205 -0.0208 -0.0212 146 ASP A CG  
1262 O OD1 . ASP A 146 ? 0.5060 0.7158 0.5853 -0.0104 -0.0246 -0.0200 146 ASP A OD1 
1263 O OD2 . ASP A 146 ? 0.4265 0.5991 0.5076 -0.0316 -0.0186 -0.0248 146 ASP A OD2 
1264 N N   . LEU A 147 ? 0.2308 0.4038 0.3179 0.0026  -0.0136 -0.0029 147 LEU A N   
1265 C CA  . LEU A 147 ? 0.2021 0.3713 0.2933 0.0030  -0.0102 -0.0020 147 LEU A CA  
1266 C C   . LEU A 147 ? 0.2437 0.4163 0.3331 0.0198  -0.0089 0.0046  147 LEU A C   
1267 O O   . LEU A 147 ? 0.1877 0.3504 0.2785 0.0219  -0.0050 0.0065  147 LEU A O   
1268 C CB  . LEU A 147 ? 0.1708 0.3101 0.2586 -0.0046 -0.0067 0.0000  147 LEU A CB  
1269 C CG  . LEU A 147 ? 0.2425 0.3723 0.3299 -0.0189 -0.0064 -0.0045 147 LEU A CG  
1270 C CD1 . LEU A 147 ? 0.2621 0.3654 0.3447 -0.0219 -0.0037 -0.0010 147 LEU A CD1 
1271 C CD2 . LEU A 147 ? 0.3927 0.5392 0.4871 -0.0289 -0.0051 -0.0118 147 LEU A CD2 
1272 N N   . LYS A 148 ? 0.1883 0.3743 0.2738 0.0324  -0.0114 0.0083  148 LYS A N   
1273 C CA  . LYS A 148 ? 0.2605 0.4461 0.3418 0.0509  -0.0088 0.0164  148 LYS A CA  
1274 C C   . LYS A 148 ? 0.2433 0.4423 0.3323 0.0548  -0.0068 0.0142  148 LYS A C   
1275 O O   . LYS A 148 ? 0.2547 0.4374 0.3407 0.0643  -0.0014 0.0198  148 LYS A O   
1276 C CB  . LYS A 148 ? 0.2943 0.5032 0.3709 0.0643  -0.0129 0.0193  148 LYS A CB  
1277 C CG  . LYS A 148 ? 0.4934 0.6835 0.5574 0.0817  -0.0086 0.0314  148 LYS A CG  
1278 C CD  . LYS A 148 ? 0.5540 0.7721 0.6124 0.0964  -0.0133 0.0346  148 LYS A CD  
1279 C CE  . LYS A 148 ? 0.6222 0.8607 0.6802 0.1130  -0.0130 0.0372  148 LYS A CE  
1280 N NZ  . LYS A 148 ? 0.6386 0.8921 0.6833 0.1250  -0.0153 0.0404  148 LYS A NZ  
1281 N N   . ASP A 149 ? 0.2215 0.4505 0.3205 0.0473  -0.0103 0.0053  149 ASP A N   
1282 C CA  . ASP A 149 ? 0.2251 0.4707 0.3324 0.0504  -0.0084 0.0021  149 ASP A CA  
1283 C C   . ASP A 149 ? 0.2159 0.4333 0.3230 0.0434  -0.0026 0.0031  149 ASP A C   
1284 O O   . ASP A 149 ? 0.2702 0.4826 0.3774 0.0534  0.0017  0.0063  149 ASP A O   
1285 C CB  . ASP A 149 ? 0.3051 0.5856 0.4240 0.0385  -0.0117 -0.0097 149 ASP A CB  
1286 C CG  . ASP A 149 ? 0.3565 0.6597 0.4702 0.0448  -0.0166 -0.0126 149 ASP A CG  
1287 O OD1 . ASP A 149 ? 0.2932 0.5953 0.3981 0.0615  -0.0181 -0.0045 149 ASP A OD1 
1288 O OD2 . ASP A 149 ? 0.3363 0.6574 0.4534 0.0329  -0.0180 -0.0232 149 ASP A OD2 
1289 N N   . LEU A 150 ? 0.1332 0.3326 0.2392 0.0271  -0.0020 0.0002  150 LEU A N   
1290 C CA  . LEU A 150 ? 0.1998 0.3765 0.3047 0.0206  0.0028  0.0005  150 LEU A CA  
1291 C C   . LEU A 150 ? 0.2384 0.3866 0.3353 0.0290  0.0067  0.0075  150 LEU A C   
1292 O O   . LEU A 150 ? 0.2110 0.3471 0.3079 0.0301  0.0115  0.0076  150 LEU A O   
1293 C CB  . LEU A 150 ? 0.2377 0.4037 0.3418 0.0034  0.0024  -0.0034 150 LEU A CB  
1294 C CG  . LEU A 150 ? 0.2547 0.4406 0.3663 -0.0088 0.0026  -0.0112 150 LEU A CG  
1295 C CD1 . LEU A 150 ? 0.2044 0.3702 0.3115 -0.0232 0.0043  -0.0123 150 LEU A CD1 
1296 C CD2 . LEU A 150 ? 0.1164 0.3146 0.2339 -0.0069 0.0062  -0.0136 150 LEU A CD2 
1297 N N   . LEU A 151 ? 0.2129 0.3506 0.3031 0.0342  0.0055  0.0123  151 LEU A N   
1298 C CA  . LEU A 151 ? 0.1792 0.2886 0.2619 0.0400  0.0109  0.0179  151 LEU A CA  
1299 C C   . LEU A 151 ? 0.3059 0.4135 0.3872 0.0558  0.0165  0.0223  151 LEU A C   
1300 O O   . LEU A 151 ? 0.2895 0.3749 0.3681 0.0572  0.0235  0.0233  151 LEU A O   
1301 C CB  . LEU A 151 ? 0.2097 0.3096 0.2853 0.0416  0.0093  0.0220  151 LEU A CB  
1302 C CG  . LEU A 151 ? 0.2134 0.2984 0.2872 0.0282  0.0078  0.0194  151 LEU A CG  
1303 C CD1 . LEU A 151 ? 0.3344 0.4170 0.4021 0.0315  0.0059  0.0231  151 LEU A CD1 
1304 C CD2 . LEU A 151 ? 0.2309 0.2918 0.3027 0.0245  0.0136  0.0190  151 LEU A CD2 
1305 N N   . ASN A 152 ? 0.3051 0.4364 0.3879 0.0684  0.0139  0.0246  152 ASN A N   
1306 C CA  . ASN A 152 ? 0.3027 0.4332 0.3832 0.0866  0.0195  0.0300  152 ASN A CA  
1307 C C   . ASN A 152 ? 0.2810 0.4185 0.3693 0.0860  0.0226  0.0251  152 ASN A C   
1308 O O   . ASN A 152 ? 0.3885 0.5156 0.4743 0.0990  0.0296  0.0287  152 ASN A O   
1309 C CB  . ASN A 152 ? 0.2817 0.4402 0.3608 0.1026  0.0149  0.0342  152 ASN A CB  
1310 C CG  . ASN A 152 ? 0.4229 0.5724 0.4915 0.1076  0.0137  0.0410  152 ASN A CG  
1311 O OD1 . ASN A 152 ? 0.6304 0.7480 0.6916 0.1034  0.0188  0.0445  152 ASN A OD1 
1312 N ND2 . ASN A 152 ? 0.5369 0.7167 0.6048 0.1168  0.0072  0.0422  152 ASN A ND2 
1313 N N   . LYS A 153 ? 0.3203 0.4741 0.4171 0.0715  0.0184  0.0170  153 LYS A N   
1314 C CA  . LYS A 153 ? 0.2726 0.4332 0.3762 0.0694  0.0218  0.0120  153 LYS A CA  
1315 C C   . LYS A 153 ? 0.3289 0.4577 0.4279 0.0681  0.0298  0.0125  153 LYS A C   
1316 O O   . LYS A 153 ? 0.2849 0.4102 0.3849 0.0773  0.0361  0.0124  153 LYS A O   
1317 C CB  . LYS A 153 ? 0.2377 0.4160 0.3488 0.0519  0.0174  0.0041  153 LYS A CB  
1318 C CG  . LYS A 153 ? 0.3179 0.5024 0.4349 0.0465  0.0210  -0.0014 153 LYS A CG  
1319 C CD  . LYS A 153 ? 0.2214 0.4127 0.3417 0.0276  0.0188  -0.0074 153 LYS A CD  
1320 C CE  . LYS A 153 ? 0.2246 0.4326 0.3521 0.0246  0.0222  -0.0130 153 LYS A CE  
1321 N NZ  . LYS A 153 ? 0.5139 0.7341 0.6453 0.0078  0.0216  -0.0188 153 LYS A NZ  
1322 N N   . GLY A 154 ? 0.3275 0.4338 0.4214 0.0571  0.0301  0.0123  154 GLY A N   
1323 C CA  . GLY A 154 ? 0.3117 0.3894 0.4009 0.0546  0.0376  0.0114  154 GLY A CA  
1324 C C   . GLY A 154 ? 0.2127 0.2903 0.3058 0.0461  0.0406  0.0043  154 GLY A C   
1325 O O   . GLY A 154 ? 0.2391 0.2963 0.3290 0.0424  0.0466  0.0014  154 GLY A O   
1326 N N   . ARG A 155 ? 0.1914 0.2922 0.2910 0.0423  0.0372  0.0007  155 ARG A N   
1327 C CA  . ARG A 155 ? 0.2269 0.3295 0.3292 0.0364  0.0409  -0.0054 155 ARG A CA  
1328 C C   . ARG A 155 ? 0.2056 0.3356 0.3146 0.0309  0.0367  -0.0084 155 ARG A C   
1329 O O   . ARG A 155 ? 0.2692 0.4166 0.3816 0.0323  0.0316  -0.0068 155 ARG A O   
1330 C CB  . ARG A 155 ? 0.2952 0.3896 0.3978 0.0480  0.0494  -0.0064 155 ARG A CB  
1331 C CG  . ARG A 155 ? 0.2703 0.3855 0.3783 0.0626  0.0492  -0.0037 155 ARG A CG  
1332 C CD  . ARG A 155 ? 0.3688 0.4724 0.4759 0.0761  0.0588  -0.0038 155 ARG A CD  
1333 N NE  . ARG A 155 ? 0.4891 0.5615 0.5879 0.0823  0.0655  0.0007  155 ARG A NE  
1334 C CZ  . ARG A 155 ? 0.4863 0.5334 0.5816 0.0802  0.0752  -0.0035 155 ARG A CZ  
1335 N NH1 . ARG A 155 ? 0.5821 0.6002 0.6700 0.0843  0.0826  0.0000  155 ARG A NH1 
1336 N NH2 . ARG A 155 ? 0.3959 0.4473 0.4952 0.0731  0.0782  -0.0120 155 ARG A NH2 
1337 N N   . ASN A 156 ? 0.2173 0.3513 0.3279 0.0237  0.0394  -0.0135 156 ASN A N   
1338 C CA  . ASN A 156 ? 0.2372 0.3956 0.3539 0.0176  0.0382  -0.0171 156 ASN A CA  
1339 C C   . ASN A 156 ? 0.2209 0.3861 0.3374 0.0062  0.0328  -0.0165 156 ASN A C   
1340 O O   . ASN A 156 ? 0.2785 0.4663 0.4017 0.0042  0.0308  -0.0186 156 ASN A O   
1341 C CB  . ASN A 156 ? 0.2650 0.4468 0.3903 0.0299  0.0391  -0.0180 156 ASN A CB  
1342 C CG  . ASN A 156 ? 0.3193 0.4927 0.4446 0.0422  0.0459  -0.0187 156 ASN A CG  
1343 O OD1 . ASN A 156 ? 0.3181 0.4790 0.4405 0.0374  0.0508  -0.0223 156 ASN A OD1 
1344 N ND2 . ASN A 156 ? 0.2847 0.4646 0.4124 0.0589  0.0468  -0.0152 156 ASN A ND2 
1345 N N   . TYR A 157 ? 0.1691 0.3154 0.2780 -0.0016 0.0310  -0.0144 157 TYR A N   
1346 C CA  . TYR A 157 ? 0.1599 0.3082 0.2672 -0.0119 0.0273  -0.0136 157 TYR A CA  
1347 C C   . TYR A 157 ? 0.1854 0.3394 0.2918 -0.0234 0.0304  -0.0164 157 TYR A C   
1348 O O   . TYR A 157 ? 0.1937 0.3436 0.2968 -0.0246 0.0342  -0.0177 157 TYR A O   
1349 C CB  . TYR A 157 ? 0.1004 0.2269 0.1998 -0.0143 0.0247  -0.0100 157 TYR A CB  
1350 C CG  . TYR A 157 ? 0.1189 0.2395 0.2184 -0.0046 0.0226  -0.0069 157 TYR A CG  
1351 C CD1 . TYR A 157 ? 0.0986 0.2299 0.2009 -0.0027 0.0185  -0.0055 157 TYR A CD1 
1352 C CD2 . TYR A 157 ? 0.1597 0.2642 0.2560 0.0023  0.0256  -0.0058 157 TYR A CD2 
1353 C CE1 . TYR A 157 ? 0.1426 0.2685 0.2430 0.0073  0.0171  -0.0016 157 TYR A CE1 
1354 C CE2 . TYR A 157 ? 0.1547 0.2511 0.2495 0.0112  0.0255  -0.0020 157 TYR A CE2 
1355 C CZ  . TYR A 157 ? 0.1870 0.2941 0.2832 0.0143  0.0210  0.0009  157 TYR A CZ  
1356 O OH  . TYR A 157 ? 0.1424 0.2416 0.2352 0.0241  0.0212  0.0057  157 TYR A OH  
1357 N N   . THR A 158 ? 0.1286 0.2919 0.2373 -0.0320 0.0297  -0.0177 158 THR A N   
1358 C CA  . THR A 158 ? 0.1185 0.2836 0.2247 -0.0441 0.0344  -0.0195 158 THR A CA  
1359 C C   . THR A 158 ? 0.1795 0.3234 0.2754 -0.0515 0.0340  -0.0154 158 THR A C   
1360 O O   . THR A 158 ? 0.1452 0.2782 0.2386 -0.0489 0.0295  -0.0126 158 THR A O   
1361 C CB  . THR A 158 ? 0.1066 0.2964 0.2228 -0.0505 0.0364  -0.0254 158 THR A CB  
1362 O OG1 . THR A 158 ? 0.1044 0.2959 0.2225 -0.0539 0.0327  -0.0262 158 THR A OG1 
1363 C CG2 . THR A 158 ? 0.1261 0.3408 0.2533 -0.0404 0.0359  -0.0294 158 THR A CG2 
1364 N N   . GLN A 159 ? 0.1755 0.3131 0.2645 -0.0601 0.0395  -0.0144 159 GLN A N   
1365 C CA  . GLN A 159 ? 0.1438 0.2605 0.2217 -0.0657 0.0405  -0.0096 159 GLN A CA  
1366 C C   . GLN A 159 ? 0.1720 0.2890 0.2537 -0.0720 0.0398  -0.0115 159 GLN A C   
1367 O O   . GLN A 159 ? 0.1739 0.2744 0.2494 -0.0718 0.0374  -0.0079 159 GLN A O   
1368 C CB  . GLN A 159 ? 0.2153 0.3255 0.2837 -0.0728 0.0482  -0.0073 159 GLN A CB  
1369 C CG  . GLN A 159 ? 0.2392 0.3262 0.2939 -0.0771 0.0512  -0.0010 159 GLN A CG  
1370 C CD  . GLN A 159 ? 0.3179 0.3909 0.3622 -0.0681 0.0463  0.0048  159 GLN A CD  
1371 O OE1 . GLN A 159 ? 0.2346 0.3142 0.2797 -0.0613 0.0432  0.0035  159 GLN A OE1 
1372 N NE2 . GLN A 159 ? 0.2617 0.3165 0.2966 -0.0681 0.0463  0.0101  159 GLN A NE2 
1373 N N   . GLU A 160 ? 0.1347 0.2728 0.2273 -0.0776 0.0418  -0.0182 160 GLU A N   
1374 C CA  . GLU A 160 ? 0.1510 0.2927 0.2480 -0.0848 0.0414  -0.0223 160 GLU A CA  
1375 C C   . GLU A 160 ? 0.1365 0.2783 0.2357 -0.0755 0.0329  -0.0210 160 GLU A C   
1376 O O   . GLU A 160 ? 0.1245 0.2560 0.2208 -0.0791 0.0316  -0.0209 160 GLU A O   
1377 C CB  . GLU A 160 ? 0.2321 0.3936 0.3363 -0.0880 0.0427  -0.0302 160 GLU A CB  
1378 C CG  . GLU A 160 ? 0.2951 0.4583 0.4006 -0.0933 0.0413  -0.0355 160 GLU A CG  
1379 C CD  . GLU A 160 ? 0.5933 0.7358 0.6899 -0.1053 0.0494  -0.0362 160 GLU A CD  
1380 O OE1 . GLU A 160 ? 0.7207 0.8652 0.8184 -0.1113 0.0503  -0.0427 160 GLU A OE1 
1381 O OE2 . GLU A 160 ? 0.6471 0.7714 0.7349 -0.1083 0.0556  -0.0305 160 GLU A OE2 
1382 N N   . GLU A 161 ? 0.1460 0.2981 0.2497 -0.0634 0.0279  -0.0201 161 GLU A N   
1383 C CA  . GLU A 161 ? 0.1408 0.2914 0.2451 -0.0540 0.0212  -0.0179 161 GLU A CA  
1384 C C   . GLU A 161 ? 0.1776 0.3012 0.2715 -0.0520 0.0195  -0.0117 161 GLU A C   
1385 O O   . GLU A 161 ? 0.1180 0.2347 0.2100 -0.0512 0.0161  -0.0106 161 GLU A O   
1386 C CB  . GLU A 161 ? 0.1245 0.2886 0.2344 -0.0408 0.0187  -0.0173 161 GLU A CB  
1387 C CG  . GLU A 161 ? 0.1174 0.3137 0.2387 -0.0398 0.0188  -0.0237 161 GLU A CG  
1388 C CD  . GLU A 161 ? 0.1448 0.3530 0.2705 -0.0258 0.0184  -0.0227 161 GLU A CD  
1389 O OE1 . GLU A 161 ? 0.1577 0.3478 0.2779 -0.0200 0.0200  -0.0184 161 GLU A OE1 
1390 O OE2 . GLU A 161 ? 0.1577 0.3948 0.2926 -0.0206 0.0171  -0.0270 161 GLU A OE2 
1391 N N   . LYS A 162 ? 0.1350 0.2457 0.2224 -0.0507 0.0217  -0.0084 162 LYS A N   
1392 C CA  . LYS A 162 ? 0.1564 0.2461 0.2345 -0.0487 0.0201  -0.0037 162 LYS A CA  
1393 C C   . LYS A 162 ? 0.1431 0.2205 0.2156 -0.0561 0.0212  -0.0023 162 LYS A C   
1394 O O   . LYS A 162 ? 0.1739 0.2406 0.2432 -0.0536 0.0179  -0.0003 162 LYS A O   
1395 C CB  . LYS A 162 ? 0.1224 0.2063 0.1946 -0.0474 0.0227  -0.0019 162 LYS A CB  
1396 C CG  . LYS A 162 ? 0.1141 0.1814 0.1771 -0.0448 0.0207  0.0018  162 LYS A CG  
1397 C CD  . LYS A 162 ? 0.1934 0.2601 0.2504 -0.0432 0.0229  0.0021  162 LYS A CD  
1398 C CE  . LYS A 162 ? 0.1911 0.2581 0.2421 -0.0490 0.0283  0.0039  162 LYS A CE  
1399 N NZ  . LYS A 162 ? 0.1785 0.2474 0.2225 -0.0466 0.0302  0.0042  162 LYS A NZ  
1400 N N   . GLU A 163 ? 0.1278 0.2055 0.1989 -0.0654 0.0271  -0.0038 163 GLU A N   
1401 C CA  . GLU A 163 ? 0.1770 0.2393 0.2417 -0.0728 0.0307  -0.0028 163 GLU A CA  
1402 C C   . GLU A 163 ? 0.2184 0.2867 0.2895 -0.0756 0.0278  -0.0075 163 GLU A C   
1403 O O   . GLU A 163 ? 0.2145 0.2674 0.2803 -0.0772 0.0280  -0.0061 163 GLU A O   
1404 C CB  . GLU A 163 ? 0.2995 0.3594 0.3611 -0.0832 0.0400  -0.0039 163 GLU A CB  
1405 C CG  . GLU A 163 ? 0.2487 0.2984 0.2996 -0.0804 0.0437  0.0023  163 GLU A CG  
1406 C CD  . GLU A 163 ? 0.3777 0.4249 0.4248 -0.0908 0.0543  0.0017  163 GLU A CD  
1407 O OE1 . GLU A 163 ? 0.3793 0.4199 0.4165 -0.0886 0.0581  0.0070  163 GLU A OE1 
1408 O OE2 . GLU A 163 ? 0.4374 0.4901 0.4910 -0.1017 0.0595  -0.0045 163 GLU A OE2 
1409 N N   . TYR A 164 ? 0.1725 0.2647 0.2548 -0.0752 0.0252  -0.0133 164 TYR A N   
1410 C CA  . TYR A 164 ? 0.1723 0.2750 0.2602 -0.0765 0.0217  -0.0182 164 TYR A CA  
1411 C C   . TYR A 164 ? 0.2016 0.2939 0.2855 -0.0670 0.0154  -0.0135 164 TYR A C   
1412 O O   . TYR A 164 ? 0.1694 0.2548 0.2512 -0.0695 0.0144  -0.0148 164 TYR A O   
1413 C CB  . TYR A 164 ? 0.1711 0.3054 0.2707 -0.0748 0.0194  -0.0245 164 TYR A CB  
1414 C CG  . TYR A 164 ? 0.2148 0.3669 0.3203 -0.0745 0.0150  -0.0302 164 TYR A CG  
1415 C CD1 . TYR A 164 ? 0.2472 0.4010 0.3516 -0.0831 0.0177  -0.0374 164 TYR A CD1 
1416 C CD2 . TYR A 164 ? 0.2257 0.3847 0.3315 -0.0615 0.0081  -0.0268 164 TYR A CD2 
1417 C CE1 . TYR A 164 ? 0.3277 0.4971 0.4345 -0.0816 0.0134  -0.0431 164 TYR A CE1 
1418 C CE2 . TYR A 164 ? 0.2798 0.4569 0.3892 -0.0602 0.0039  -0.0315 164 TYR A CE2 
1419 C CZ  . TYR A 164 ? 0.3193 0.5022 0.4291 -0.0705 0.0062  -0.0401 164 TYR A CZ  
1420 O OH  . TYR A 164 ? 0.3140 0.5133 0.4245 -0.0683 0.0021  -0.0453 164 TYR A OH  
1421 N N   . VAL A 165 ? 0.1322 0.2228 0.2150 -0.0567 0.0122  -0.0088 165 VAL A N   
1422 C CA  . VAL A 165 ? 0.1254 0.2047 0.2043 -0.0488 0.0080  -0.0047 165 VAL A CA  
1423 C C   . VAL A 165 ? 0.1872 0.2450 0.2576 -0.0517 0.0091  -0.0018 165 VAL A C   
1424 O O   . VAL A 165 ? 0.1546 0.2055 0.2230 -0.0506 0.0068  -0.0014 165 VAL A O   
1425 C CB  . VAL A 165 ? 0.1798 0.2588 0.2589 -0.0396 0.0071  -0.0016 165 VAL A CB  
1426 C CG1 . VAL A 165 ? 0.1811 0.2460 0.2557 -0.0342 0.0047  0.0017  165 VAL A CG1 
1427 C CG2 . VAL A 165 ? 0.1497 0.2482 0.2360 -0.0333 0.0060  -0.0033 165 VAL A CG2 
1428 N N   . LEU A 166 ? 0.1631 0.2111 0.2280 -0.0545 0.0130  0.0006  166 LEU A N   
1429 C CA  . LEU A 166 ? 0.1554 0.1842 0.2110 -0.0548 0.0144  0.0045  166 LEU A CA  
1430 C C   . LEU A 166 ? 0.1522 0.1733 0.2064 -0.0612 0.0168  0.0022  166 LEU A C   
1431 O O   . LEU A 166 ? 0.1854 0.1942 0.2351 -0.0584 0.0154  0.0041  166 LEU A O   
1432 C CB  . LEU A 166 ? 0.1745 0.1959 0.2227 -0.0561 0.0192  0.0080  166 LEU A CB  
1433 C CG  . LEU A 166 ? 0.2879 0.3111 0.3334 -0.0487 0.0166  0.0105  166 LEU A CG  
1434 C CD1 . LEU A 166 ? 0.2651 0.2858 0.3033 -0.0504 0.0216  0.0133  166 LEU A CD1 
1435 C CD2 . LEU A 166 ? 0.3115 0.3256 0.3522 -0.0425 0.0129  0.0129  166 LEU A CD2 
1436 N N   . ASN A 167 ? 0.1547 0.1838 0.2134 -0.0703 0.0210  -0.0029 167 ASN A N   
1437 C CA  . ASN A 167 ? 0.2582 0.2800 0.3162 -0.0784 0.0248  -0.0072 167 ASN A CA  
1438 C C   . ASN A 167 ? 0.2247 0.2540 0.2869 -0.0753 0.0188  -0.0105 167 ASN A C   
1439 O O   . ASN A 167 ? 0.2010 0.2169 0.2591 -0.0767 0.0199  -0.0111 167 ASN A O   
1440 C CB  . ASN A 167 ? 0.2498 0.2824 0.3133 -0.0907 0.0313  -0.0145 167 ASN A CB  
1441 C CG  . ASN A 167 ? 0.4945 0.5134 0.5510 -0.0957 0.0400  -0.0110 167 ASN A CG  
1442 O OD1 . ASN A 167 ? 0.5653 0.5625 0.6103 -0.0906 0.0421  -0.0030 167 ASN A OD1 
1443 N ND2 . ASN A 167 ? 0.5687 0.6008 0.6297 -0.1015 0.0437  -0.0159 167 ASN A ND2 
1444 N N   . LYS A 168 ? 0.1648 0.2151 0.2345 -0.0704 0.0131  -0.0123 168 LYS A N   
1445 C CA  . LYS A 168 ? 0.1873 0.2447 0.2590 -0.0663 0.0078  -0.0142 168 LYS A CA  
1446 C C   . LYS A 168 ? 0.2184 0.2586 0.2837 -0.0589 0.0053  -0.0084 168 LYS A C   
1447 O O   . LYS A 168 ? 0.1558 0.1914 0.2193 -0.0589 0.0039  -0.0100 168 LYS A O   
1448 C CB  . LYS A 168 ? 0.1881 0.2694 0.2666 -0.0598 0.0032  -0.0152 168 LYS A CB  
1449 C CG  . LYS A 168 ? 0.2325 0.3385 0.3192 -0.0663 0.0045  -0.0230 168 LYS A CG  
1450 C CD  . LYS A 168 ? 0.4068 0.5238 0.4960 -0.0729 0.0039  -0.0313 168 LYS A CD  
1451 C CE  . LYS A 168 ? 0.4772 0.6056 0.5706 -0.0840 0.0088  -0.0404 168 LYS A CE  
1452 N NZ  . LYS A 168 ? 0.5087 0.6357 0.5994 -0.0900 0.0102  -0.0480 168 LYS A NZ  
1453 N N   . TYR A 169 ? 0.1816 0.2138 0.2438 -0.0532 0.0049  -0.0028 169 TYR A N   
1454 C CA  . TYR A 169 ? 0.1945 0.2144 0.2520 -0.0469 0.0027  0.0012  169 TYR A CA  
1455 C C   . TYR A 169 ? 0.1977 0.2011 0.2489 -0.0493 0.0052  0.0017  169 TYR A C   
1456 O O   . TYR A 169 ? 0.1910 0.1889 0.2405 -0.0460 0.0032  0.0019  169 TYR A O   
1457 C CB  . TYR A 169 ? 0.1357 0.1536 0.1916 -0.0420 0.0026  0.0048  169 TYR A CB  
1458 C CG  . TYR A 169 ? 0.1310 0.1590 0.1917 -0.0368 0.0006  0.0048  169 TYR A CG  
1459 C CD1 . TYR A 169 ? 0.1026 0.1426 0.1680 -0.0354 -0.0008 0.0032  169 TYR A CD1 
1460 C CD2 . TYR A 169 ? 0.1902 0.2156 0.2500 -0.0327 0.0008  0.0062  169 TYR A CD2 
1461 C CE1 . TYR A 169 ? 0.1264 0.1721 0.1943 -0.0287 -0.0011 0.0046  169 TYR A CE1 
1462 C CE2 . TYR A 169 ? 0.2084 0.2387 0.2717 -0.0283 0.0011  0.0059  169 TYR A CE2 
1463 C CZ  . TYR A 169 ? 0.1605 0.1991 0.2273 -0.0256 0.0005  0.0059  169 TYR A CZ  
1464 O OH  . TYR A 169 ? 0.1856 0.2256 0.2542 -0.0195 0.0022  0.0069  169 TYR A OH  
1465 N N   . PHE A 170 ? 0.1693 0.1633 0.2163 -0.0546 0.0107  0.0023  170 PHE A N   
1466 C CA  . PHE A 170 ? 0.2157 0.1906 0.2552 -0.0551 0.0146  0.0038  170 PHE A CA  
1467 C C   . PHE A 170 ? 0.2157 0.1896 0.2576 -0.0612 0.0161  -0.0025 170 PHE A C   
1468 O O   . PHE A 170 ? 0.2271 0.1874 0.2643 -0.0590 0.0173  -0.0020 170 PHE A O   
1469 C CB  . PHE A 170 ? 0.2497 0.2109 0.2815 -0.0578 0.0218  0.0076  170 PHE A CB  
1470 C CG  . PHE A 170 ? 0.2752 0.2324 0.3001 -0.0486 0.0202  0.0148  170 PHE A CG  
1471 C CD1 . PHE A 170 ? 0.2941 0.2393 0.3113 -0.0402 0.0196  0.0192  170 PHE A CD1 
1472 C CD2 . PHE A 170 ? 0.3162 0.2846 0.3428 -0.0476 0.0189  0.0160  170 PHE A CD2 
1473 C CE1 . PHE A 170 ? 0.3760 0.3230 0.3871 -0.0311 0.0173  0.0245  170 PHE A CE1 
1474 C CE2 . PHE A 170 ? 0.2945 0.2625 0.3148 -0.0397 0.0173  0.0210  170 PHE A CE2 
1475 C CZ  . PHE A 170 ? 0.2967 0.2555 0.3094 -0.0314 0.0162  0.0250  170 PHE A CZ  
1476 N N   . GLU A 171 ? 0.2131 0.2036 0.2624 -0.0681 0.0156  -0.0090 171 GLU A N   
1477 C CA  . GLU A 171 ? 0.2426 0.2374 0.2948 -0.0739 0.0161  -0.0166 171 GLU A CA  
1478 C C   . GLU A 171 ? 0.1973 0.1950 0.2493 -0.0662 0.0100  -0.0155 171 GLU A C   
1479 O O   . GLU A 171 ? 0.2160 0.2057 0.2657 -0.0678 0.0114  -0.0188 171 GLU A O   
1480 C CB  . GLU A 171 ? 0.2102 0.2292 0.2709 -0.0814 0.0157  -0.0245 171 GLU A CB  
1481 C CG  . GLU A 171 ? 0.3690 0.3858 0.4306 -0.0927 0.0238  -0.0293 171 GLU A CG  
1482 C CD  . GLU A 171 ? 0.5434 0.5891 0.6133 -0.0961 0.0217  -0.0368 171 GLU A CD  
1483 O OE1 . GLU A 171 ? 0.5460 0.6146 0.6220 -0.0918 0.0147  -0.0391 171 GLU A OE1 
1484 O OE2 . GLU A 171 ? 0.6689 0.7148 0.7385 -0.1024 0.0275  -0.0403 171 GLU A OE2 
1485 N N   . ILE A 172 ? 0.1500 0.1574 0.2041 -0.0581 0.0044  -0.0110 172 ILE A N   
1486 C CA  . ILE A 172 ? 0.1967 0.2054 0.2501 -0.0511 0.0002  -0.0093 172 ILE A CA  
1487 C C   . ILE A 172 ? 0.1827 0.1734 0.2307 -0.0476 0.0015  -0.0065 172 ILE A C   
1488 O O   . ILE A 172 ? 0.2276 0.2147 0.2742 -0.0464 0.0010  -0.0085 172 ILE A O   
1489 C CB  . ILE A 172 ? 0.1740 0.1923 0.2299 -0.0441 -0.0034 -0.0051 172 ILE A CB  
1490 C CG1 . ILE A 172 ? 0.2367 0.2749 0.2972 -0.0441 -0.0053 -0.0074 172 ILE A CG1 
1491 C CG2 . ILE A 172 ? 0.2268 0.2405 0.2808 -0.0376 -0.0054 -0.0024 172 ILE A CG2 
1492 C CD1 . ILE A 172 ? 0.2346 0.2839 0.2951 -0.0438 -0.0076 -0.0112 172 ILE A CD1 
1493 N N   . ILE A 173 ? 0.1905 0.1716 0.2351 -0.0450 0.0032  -0.0019 173 ILE A N   
1494 C CA  . ILE A 173 ? 0.1571 0.1245 0.1962 -0.0395 0.0041  0.0011  173 ILE A CA  
1495 C C   . ILE A 173 ? 0.1463 0.0996 0.1812 -0.0429 0.0088  -0.0017 173 ILE A C   
1496 O O   . ILE A 173 ? 0.2236 0.1706 0.2564 -0.0385 0.0084  -0.0021 173 ILE A O   
1497 C CB  . ILE A 173 ? 0.2221 0.1845 0.2567 -0.0354 0.0052  0.0065  173 ILE A CB  
1498 C CG1 . ILE A 173 ? 0.1825 0.1585 0.2217 -0.0321 0.0010  0.0075  173 ILE A CG1 
1499 C CG2 . ILE A 173 ? 0.2561 0.2066 0.2840 -0.0279 0.0062  0.0099  173 ILE A CG2 
1500 C CD1 . ILE A 173 ? 0.2007 0.1762 0.2360 -0.0287 0.0017  0.0114  173 ILE A CD1 
1501 N N   . LYS A 174 ? 0.1984 0.1461 0.2323 -0.0512 0.0143  -0.0045 174 LYS A N   
1502 C CA  . LYS A 174 ? 0.2011 0.1321 0.2308 -0.0559 0.0210  -0.0083 174 LYS A CA  
1503 C C   . LYS A 174 ? 0.2122 0.1503 0.2456 -0.0582 0.0189  -0.0154 174 LYS A C   
1504 O O   . LYS A 174 ? 0.2454 0.1684 0.2747 -0.0591 0.0237  -0.0184 174 LYS A O   
1505 C CB  . LYS A 174 ? 0.2101 0.1361 0.2396 -0.0673 0.0286  -0.0122 174 LYS A CB  
1506 C CG  . LYS A 174 ? 0.2142 0.1263 0.2365 -0.0655 0.0339  -0.0048 174 LYS A CG  
1507 C CD  . LYS A 174 ? 0.3985 0.3007 0.4195 -0.0785 0.0445  -0.0096 174 LYS A CD  
1508 C CE  . LYS A 174 ? 0.5757 0.4774 0.5938 -0.0793 0.0475  -0.0040 174 LYS A CE  
1509 N NZ  . LYS A 174 ? 0.6965 0.5820 0.7031 -0.0668 0.0482  0.0076  174 LYS A NZ  
1510 N N   . LYS A 175 ? 0.2130 0.1725 0.2527 -0.0586 0.0126  -0.0180 175 LYS A N   
1511 C CA  . LYS A 175 ? 0.2431 0.2123 0.2851 -0.0601 0.0102  -0.0243 175 LYS A CA  
1512 C C   . LYS A 175 ? 0.2413 0.2111 0.2822 -0.0510 0.0059  -0.0206 175 LYS A C   
1513 O O   . LYS A 175 ? 0.2108 0.1888 0.2525 -0.0512 0.0040  -0.0248 175 LYS A O   
1514 C CB  . LYS A 175 ? 0.2164 0.2101 0.2642 -0.0642 0.0064  -0.0285 175 LYS A CB  
1515 C CG  . LYS A 175 ? 0.4326 0.4316 0.4835 -0.0759 0.0111  -0.0367 175 LYS A CG  
1516 C CD  . LYS A 175 ? 0.5328 0.5578 0.5900 -0.0770 0.0070  -0.0382 175 LYS A CD  
1517 C CE  . LYS A 175 ? 0.5774 0.6222 0.6356 -0.0696 0.0000  -0.0374 175 LYS A CE  
1518 N NZ  . LYS A 175 ? 0.7336 0.8070 0.7975 -0.0712 -0.0031 -0.0418 175 LYS A NZ  
1519 N N   . THR A 176 ? 0.1870 0.1502 0.2262 -0.0434 0.0047  -0.0138 176 THR A N   
1520 C CA  . THR A 176 ? 0.2046 0.1740 0.2450 -0.0365 0.0007  -0.0116 176 THR A CA  
1521 C C   . THR A 176 ? 0.2391 0.2010 0.2773 -0.0334 0.0021  -0.0141 176 THR A C   
1522 O O   . THR A 176 ? 0.2376 0.2075 0.2771 -0.0327 0.0003  -0.0165 176 THR A O   
1523 C CB  . THR A 176 ? 0.2432 0.2129 0.2841 -0.0309 -0.0010 -0.0059 176 THR A CB  
1524 O OG1 . THR A 176 ? 0.2115 0.1905 0.2553 -0.0332 -0.0024 -0.0043 176 THR A OG1 
1525 C CG2 . THR A 176 ? 0.1342 0.1092 0.1769 -0.0254 -0.0033 -0.0054 176 THR A CG2 
1526 N N   . LEU A 177 ? 0.2266 0.1729 0.2606 -0.0305 0.0058  -0.0131 177 LEU A N   
1527 C CA  . LEU A 177 ? 0.1890 0.1288 0.2210 -0.0264 0.0075  -0.0158 177 LEU A CA  
1528 C C   . LEU A 177 ? 0.1925 0.1330 0.2248 -0.0335 0.0096  -0.0236 177 LEU A C   
1529 O O   . LEU A 177 ? 0.2171 0.1612 0.2498 -0.0315 0.0091  -0.0270 177 LEU A O   
1530 C CB  . LEU A 177 ? 0.2212 0.1426 0.2472 -0.0198 0.0120  -0.0124 177 LEU A CB  
1531 C CG  . LEU A 177 ? 0.2606 0.1869 0.2862 -0.0107 0.0087  -0.0057 177 LEU A CG  
1532 C CD1 . LEU A 177 ? 0.3177 0.2268 0.3349 -0.0014 0.0132  -0.0005 177 LEU A CD1 
1533 C CD2 . LEU A 177 ? 0.2664 0.2092 0.2976 -0.0060 0.0038  -0.0072 177 LEU A CD2 
1534 N N   . SER A 178 ? 0.2026 0.1432 0.2351 -0.0425 0.0120  -0.0274 178 SER A N   
1535 C CA  . SER A 178 ? 0.2316 0.1766 0.2646 -0.0504 0.0142  -0.0368 178 SER A CA  
1536 C C   . SER A 178 ? 0.2824 0.2490 0.3181 -0.0498 0.0083  -0.0385 178 SER A C   
1537 O O   . SER A 178 ? 0.2409 0.2119 0.2755 -0.0517 0.0090  -0.0449 178 SER A O   
1538 C CB  . SER A 178 ? 0.2541 0.1989 0.2881 -0.0613 0.0182  -0.0421 178 SER A CB  
1539 O OG  . SER A 178 ? 0.3227 0.2428 0.3522 -0.0632 0.0265  -0.0418 178 SER A OG  
1540 N N   . ILE A 179 ? 0.2219 0.2013 0.2600 -0.0468 0.0035  -0.0327 179 ILE A N   
1541 C CA  . ILE A 179 ? 0.1975 0.1943 0.2357 -0.0450 -0.0005 -0.0329 179 ILE A CA  
1542 C C   . ILE A 179 ? 0.1796 0.1734 0.2162 -0.0391 -0.0005 -0.0313 179 ILE A C   
1543 O O   . ILE A 179 ? 0.1747 0.1779 0.2090 -0.0389 -0.0012 -0.0341 179 ILE A O   
1544 C CB  . ILE A 179 ? 0.2207 0.2292 0.2609 -0.0424 -0.0040 -0.0268 179 ILE A CB  
1545 C CG1 . ILE A 179 ? 0.2276 0.2540 0.2657 -0.0404 -0.0067 -0.0274 179 ILE A CG1 
1546 C CG2 . ILE A 179 ? 0.1911 0.1924 0.2322 -0.0362 -0.0046 -0.0194 179 ILE A CG2 
1547 C CD1 . ILE A 179 ? 0.3998 0.4391 0.4389 -0.0375 -0.0093 -0.0229 179 ILE A CD1 
1548 N N   . TYR A 180 ? 0.1784 0.1612 0.2157 -0.0342 0.0004  -0.0274 180 TYR A N   
1549 C CA  . TYR A 180 ? 0.1643 0.1467 0.2014 -0.0295 0.0010  -0.0278 180 TYR A CA  
1550 C C   . TYR A 180 ? 0.1488 0.1262 0.1836 -0.0311 0.0040  -0.0349 180 TYR A C   
1551 O O   . TYR A 180 ? 0.1895 0.1730 0.2232 -0.0300 0.0043  -0.0376 180 TYR A O   
1552 C CB  . TYR A 180 ? 0.1778 0.1540 0.2171 -0.0235 0.0010  -0.0239 180 TYR A CB  
1553 C CG  . TYR A 180 ? 0.1430 0.1262 0.1852 -0.0221 -0.0011 -0.0188 180 TYR A CG  
1554 C CD1 . TYR A 180 ? 0.1403 0.1313 0.1838 -0.0214 -0.0008 -0.0182 180 TYR A CD1 
1555 C CD2 . TYR A 180 ? 0.1796 0.1602 0.2226 -0.0221 -0.0022 -0.0151 180 TYR A CD2 
1556 C CE1 . TYR A 180 ? 0.1779 0.1726 0.2239 -0.0210 -0.0009 -0.0147 180 TYR A CE1 
1557 C CE2 . TYR A 180 ? 0.1708 0.1573 0.2165 -0.0213 -0.0034 -0.0117 180 TYR A CE2 
1558 C CZ  . TYR A 180 ? 0.1687 0.1615 0.2160 -0.0209 -0.0024 -0.0119 180 TYR A CZ  
1559 O OH  . TYR A 180 ? 0.1536 0.1498 0.2034 -0.0210 -0.0017 -0.0096 180 TYR A OH  
1560 N N   . ARG A 181 ? 0.1564 0.1208 0.1898 -0.0338 0.0073  -0.0380 181 ARG A N   
1561 C CA  . ARG A 181 ? 0.1759 0.1332 0.2068 -0.0362 0.0116  -0.0460 181 ARG A CA  
1562 C C   . ARG A 181 ? 0.2123 0.1848 0.2424 -0.0432 0.0105  -0.0530 181 ARG A C   
1563 O O   . ARG A 181 ? 0.2095 0.1856 0.2377 -0.0433 0.0119  -0.0587 181 ARG A O   
1564 C CB  . ARG A 181 ? 0.1853 0.1225 0.2140 -0.0387 0.0175  -0.0480 181 ARG A CB  
1565 C CG  . ARG A 181 ? 0.2950 0.2202 0.3207 -0.0415 0.0240  -0.0568 181 ARG A CG  
1566 C CD  . ARG A 181 ? 0.2813 0.1819 0.3033 -0.0443 0.0322  -0.0578 181 ARG A CD  
1567 N NE  . ARG A 181 ? 0.2485 0.1358 0.2680 -0.0336 0.0326  -0.0475 181 ARG A NE  
1568 C CZ  . ARG A 181 ? 0.2711 0.1524 0.2893 -0.0339 0.0330  -0.0409 181 ARG A CZ  
1569 N NH1 . ARG A 181 ? 0.3173 0.2042 0.3374 -0.0450 0.0334  -0.0439 181 ARG A NH1 
1570 N NH2 . ARG A 181 ? 0.2406 0.1125 0.2553 -0.0227 0.0331  -0.0317 181 ARG A NH2 
1571 N N   . GLU A 182 ? 0.1931 0.1770 0.2243 -0.0484 0.0080  -0.0529 182 GLU A N   
1572 C CA  . GLU A 182 ? 0.1901 0.1933 0.2201 -0.0535 0.0061  -0.0597 182 GLU A CA  
1573 C C   . GLU A 182 ? 0.1838 0.2000 0.2107 -0.0475 0.0029  -0.0560 182 GLU A C   
1574 O O   . GLU A 182 ? 0.1712 0.1957 0.1947 -0.0489 0.0037  -0.0624 182 GLU A O   
1575 C CB  . GLU A 182 ? 0.2513 0.2684 0.2837 -0.0581 0.0034  -0.0598 182 GLU A CB  
1576 C CG  . GLU A 182 ? 0.2545 0.2976 0.2851 -0.0614 0.0004  -0.0668 182 GLU A CG  
1577 C CD  . GLU A 182 ? 0.3346 0.3970 0.3686 -0.0653 -0.0025 -0.0687 182 GLU A CD  
1578 O OE1 . GLU A 182 ? 0.2768 0.3644 0.3097 -0.0676 -0.0052 -0.0758 182 GLU A OE1 
1579 O OE2 . GLU A 182 ? 0.2943 0.3496 0.3320 -0.0657 -0.0023 -0.0638 182 GLU A OE2 
1580 N N   . ILE A 183 ? 0.1629 0.1807 0.1903 -0.0413 0.0004  -0.0461 183 ILE A N   
1581 C CA  . ILE A 183 ? 0.2185 0.2463 0.2416 -0.0365 -0.0005 -0.0425 183 ILE A CA  
1582 C C   . ILE A 183 ? 0.2143 0.2356 0.2362 -0.0349 0.0027  -0.0457 183 ILE A C   
1583 O O   . ILE A 183 ? 0.2096 0.2400 0.2265 -0.0335 0.0034  -0.0469 183 ILE A O   
1584 C CB  . ILE A 183 ? 0.1822 0.2100 0.2056 -0.0312 -0.0017 -0.0322 183 ILE A CB  
1585 C CG1 . ILE A 183 ? 0.2279 0.2417 0.2564 -0.0292 -0.0001 -0.0289 183 ILE A CG1 
1586 C CG2 . ILE A 183 ? 0.1786 0.2148 0.2030 -0.0317 -0.0047 -0.0294 183 ILE A CG2 
1587 C CD1 . ILE A 183 ? 0.2168 0.2287 0.2449 -0.0259 0.0028  -0.0274 183 ILE A CD1 
1588 N N   . LYS A 184 ? 0.1875 0.1940 0.2134 -0.0340 0.0050  -0.0471 184 LYS A N   
1589 C CA  . LYS A 184 ? 0.2087 0.2107 0.2344 -0.0317 0.0082  -0.0514 184 LYS A CA  
1590 C C   . LYS A 184 ? 0.1681 0.1726 0.1902 -0.0363 0.0104  -0.0615 184 LYS A C   
1591 O O   . LYS A 184 ? 0.1939 0.2061 0.2127 -0.0356 0.0118  -0.0650 184 LYS A O   
1592 C CB  . LYS A 184 ? 0.2310 0.2184 0.2609 -0.0274 0.0098  -0.0501 184 LYS A CB  
1593 C CG  . LYS A 184 ? 0.2113 0.1946 0.2417 -0.0235 0.0133  -0.0551 184 LYS A CG  
1594 C CD  . LYS A 184 ? 0.2522 0.2252 0.2862 -0.0161 0.0143  -0.0523 184 LYS A CD  
1595 C CE  . LYS A 184 ? 0.3281 0.2985 0.3628 -0.0106 0.0179  -0.0578 184 LYS A CE  
1596 N NZ  . LYS A 184 ? 0.3786 0.3377 0.4091 -0.0136 0.0225  -0.0655 184 LYS A NZ  
1597 N N   . GLU A 185 ? 0.2219 0.2203 0.2446 -0.0420 0.0117  -0.0672 185 GLU A N   
1598 C CA  . GLU A 185 ? 0.2270 0.2274 0.2471 -0.0483 0.0150  -0.0792 185 GLU A CA  
1599 C C   . GLU A 185 ? 0.2190 0.2434 0.2346 -0.0507 0.0118  -0.0824 185 GLU A C   
1600 O O   . GLU A 185 ? 0.2348 0.2659 0.2469 -0.0531 0.0139  -0.0911 185 GLU A O   
1601 C CB  . GLU A 185 ? 0.2441 0.2334 0.2660 -0.0560 0.0185  -0.0855 185 GLU A CB  
1602 C CG  . GLU A 185 ? 0.4403 0.4289 0.4603 -0.0646 0.0240  -0.1005 185 GLU A CG  
1603 C CD  . GLU A 185 ? 0.6224 0.6387 0.6404 -0.0712 0.0205  -0.1084 185 GLU A CD  
1604 O OE1 . GLU A 185 ? 0.5372 0.5576 0.5537 -0.0785 0.0245  -0.1222 185 GLU A OE1 
1605 O OE2 . GLU A 185 ? 0.6707 0.7050 0.6887 -0.0686 0.0140  -0.1013 185 GLU A OE2 
1606 N N   . GLU A 186 ? 0.1771 0.1734 0.1975 -0.0334 -0.0277 -0.0669 186 GLU A N   
1607 C CA  . GLU A 186 ? 0.1797 0.1874 0.1977 -0.0324 -0.0323 -0.0679 186 GLU A CA  
1608 C C   . GLU A 186 ? 0.2293 0.2391 0.2385 -0.0268 -0.0318 -0.0648 186 GLU A C   
1609 O O   . GLU A 186 ? 0.2675 0.2866 0.2731 -0.0258 -0.0358 -0.0644 186 GLU A O   
1610 C CB  . GLU A 186 ? 0.2066 0.2255 0.2345 -0.0335 -0.0344 -0.0645 186 GLU A CB  
1611 C CG  . GLU A 186 ? 0.2360 0.2561 0.2731 -0.0403 -0.0349 -0.0670 186 GLU A CG  
1612 C CD  . GLU A 186 ? 0.2654 0.3001 0.3133 -0.0411 -0.0369 -0.0647 186 GLU A CD  
1613 O OE1 . GLU A 186 ? 0.2351 0.2759 0.2855 -0.0356 -0.0366 -0.0603 186 GLU A OE1 
1614 O OE2 . GLU A 186 ? 0.2649 0.3052 0.3198 -0.0474 -0.0390 -0.0675 186 GLU A OE2 
1615 N N   . GLY A 187 ? 0.2066 0.2091 0.2124 -0.0235 -0.0272 -0.0619 187 GLY A N   
1616 C CA  . GLY A 187 ? 0.2457 0.2510 0.2437 -0.0192 -0.0264 -0.0581 187 GLY A CA  
1617 C C   . GLY A 187 ? 0.2277 0.2383 0.2293 -0.0167 -0.0275 -0.0504 187 GLY A C   
1618 O O   . GLY A 187 ? 0.2263 0.2408 0.2219 -0.0142 -0.0286 -0.0461 187 GLY A O   
1619 N N   . LYS A 188 ? 0.2075 0.2189 0.2191 -0.0173 -0.0276 -0.0486 188 LYS A N   
1620 C CA  . LYS A 188 ? 0.1847 0.1998 0.2012 -0.0140 -0.0288 -0.0425 188 LYS A CA  
1621 C C   . LYS A 188 ? 0.1699 0.1778 0.1862 -0.0115 -0.0244 -0.0383 188 LYS A C   
1622 O O   . LYS A 188 ? 0.2000 0.2086 0.2179 -0.0084 -0.0257 -0.0331 188 LYS A O   
1623 C CB  . LYS A 188 ? 0.1764 0.1977 0.2043 -0.0152 -0.0304 -0.0436 188 LYS A CB  
1624 C CG  . LYS A 188 ? 0.2021 0.2334 0.2321 -0.0175 -0.0359 -0.0469 188 LYS A CG  
1625 C CD  . LYS A 188 ? 0.1981 0.2377 0.2408 -0.0188 -0.0368 -0.0480 188 LYS A CD  
1626 C CE  . LYS A 188 ? 0.2658 0.3175 0.3116 -0.0201 -0.0430 -0.0500 188 LYS A CE  
1627 N NZ  . LYS A 188 ? 0.2274 0.2778 0.2672 -0.0255 -0.0444 -0.0556 188 LYS A NZ  
1628 N N   . GLY A 189 ? 0.1619 0.1624 0.1764 -0.0127 -0.0199 -0.0403 189 GLY A N   
1629 C CA  . GLY A 189 ? 0.1994 0.1940 0.2130 -0.0107 -0.0161 -0.0365 189 GLY A CA  
1630 C C   . GLY A 189 ? 0.2203 0.2080 0.2306 -0.0118 -0.0122 -0.0393 189 GLY A C   
1631 O O   . GLY A 189 ? 0.2526 0.2383 0.2630 -0.0143 -0.0124 -0.0441 189 GLY A O   
1632 N N   . SER A 190 ? 0.1749 0.1588 0.1826 -0.0099 -0.0091 -0.0362 190 SER A N   
1633 C CA  . SER A 190 ? 0.2125 0.1901 0.2188 -0.0100 -0.0054 -0.0380 190 SER A CA  
1634 C C   . SER A 190 ? 0.1971 0.1717 0.2096 -0.0106 -0.0032 -0.0358 190 SER A C   
1635 O O   . SER A 190 ? 0.2047 0.1820 0.2211 -0.0098 -0.0037 -0.0329 190 SER A O   
1636 C CB  . SER A 190 ? 0.2460 0.2236 0.2460 -0.0077 -0.0033 -0.0364 190 SER A CB  
1637 O OG  . SER A 190 ? 0.2401 0.2224 0.2333 -0.0072 -0.0048 -0.0389 190 SER A OG  
1638 N N   . VAL A 191 ? 0.1918 0.1608 0.2052 -0.0118 -0.0010 -0.0373 191 VAL A N   
1639 C CA  . VAL A 191 ? 0.1704 0.1376 0.1882 -0.0127 0.0013  -0.0348 191 VAL A CA  
1640 C C   . VAL A 191 ? 0.1802 0.1426 0.1951 -0.0108 0.0039  -0.0334 191 VAL A C   
1641 O O   . VAL A 191 ? 0.2044 0.1623 0.2167 -0.0102 0.0041  -0.0358 191 VAL A O   
1642 C CB  . VAL A 191 ? 0.1973 0.1637 0.2198 -0.0167 0.0011  -0.0362 191 VAL A CB  
1643 C CG1 . VAL A 191 ? 0.1511 0.1181 0.1771 -0.0178 0.0036  -0.0331 191 VAL A CG1 
1644 C CG2 . VAL A 191 ? 0.2466 0.2199 0.2729 -0.0185 -0.0017 -0.0380 191 VAL A CG2 
1645 N N   . SER A 192 ? 0.1862 0.1497 0.2022 -0.0098 0.0056  -0.0300 192 SER A N   
1646 C CA  . SER A 192 ? 0.2143 0.1752 0.2288 -0.0083 0.0078  -0.0282 192 SER A CA  
1647 C C   . SER A 192 ? 0.1811 0.1407 0.1988 -0.0101 0.0091  -0.0264 192 SER A C   
1648 O O   . SER A 192 ? 0.1674 0.1292 0.1884 -0.0126 0.0088  -0.0266 192 SER A O   
1649 C CB  . SER A 192 ? 0.1935 0.1576 0.2063 -0.0065 0.0083  -0.0255 192 SER A CB  
1650 O OG  . SER A 192 ? 0.1924 0.1585 0.2087 -0.0073 0.0078  -0.0239 192 SER A OG  
1651 N N   . THR A 193 ? 0.1778 0.1353 0.1945 -0.0088 0.0106  -0.0244 193 THR A N   
1652 C CA  . THR A 193 ? 0.1542 0.1122 0.1729 -0.0105 0.0118  -0.0218 193 THR A CA  
1653 C C   . THR A 193 ? 0.1985 0.1586 0.2162 -0.0085 0.0129  -0.0196 193 THR A C   
1654 O O   . THR A 193 ? 0.1841 0.1454 0.2002 -0.0064 0.0130  -0.0198 193 THR A O   
1655 C CB  . THR A 193 ? 0.2117 0.1642 0.2310 -0.0123 0.0115  -0.0208 193 THR A CB  
1656 O OG1 . THR A 193 ? 0.2167 0.1721 0.2375 -0.0152 0.0124  -0.0177 193 THR A OG1 
1657 C CG2 . THR A 193 ? 0.1888 0.1360 0.2066 -0.0090 0.0114  -0.0204 193 THR A CG2 
1658 N N   . SER A 194 ? 0.1704 0.1322 0.1890 -0.0098 0.0137  -0.0173 194 SER A N   
1659 C CA  . SER A 194 ? 0.1766 0.1412 0.1947 -0.0087 0.0143  -0.0152 194 SER A CA  
1660 C C   . SER A 194 ? 0.2084 0.1714 0.2263 -0.0087 0.0144  -0.0122 194 SER A C   
1661 O O   . SER A 194 ? 0.1760 0.1361 0.1941 -0.0109 0.0141  -0.0111 194 SER A O   
1662 C CB  . SER A 194 ? 0.1757 0.1452 0.1949 -0.0102 0.0145  -0.0157 194 SER A CB  
1663 O OG  . SER A 194 ? 0.1791 0.1491 0.1994 -0.0097 0.0137  -0.0178 194 SER A OG  
1664 N N   . PRO A 195 ? 0.2051 0.1704 0.2228 -0.0069 0.0145  -0.0103 195 PRO A N   
1665 C CA  . PRO A 195 ? 0.1835 0.1486 0.2012 -0.0069 0.0140  -0.0065 195 PRO A CA  
1666 C C   . PRO A 195 ? 0.1728 0.1404 0.1896 -0.0111 0.0142  -0.0048 195 PRO A C   
1667 O O   . PRO A 195 ? 0.1901 0.1629 0.2069 -0.0129 0.0150  -0.0071 195 PRO A O   
1668 C CB  . PRO A 195 ? 0.1914 0.1626 0.2095 -0.0053 0.0140  -0.0053 195 PRO A CB  
1669 C CG  . PRO A 195 ? 0.3817 0.3541 0.4002 -0.0038 0.0147  -0.0079 195 PRO A CG  
1670 C CD  . PRO A 195 ? 0.2225 0.1917 0.2403 -0.0052 0.0149  -0.0108 195 PRO A CD  
1671 N N   . TYR A 196 ? 0.1528 0.1173 0.1692 -0.0124 0.0132  -0.0008 196 TYR A N   
1672 C CA  . TYR A 196 ? 0.1778 0.1432 0.1936 -0.0171 0.0136  0.0011  196 TYR A CA  
1673 C C   . TYR A 196 ? 0.1648 0.1406 0.1794 -0.0201 0.0152  -0.0004 196 TYR A C   
1674 O O   . TYR A 196 ? 0.1627 0.1416 0.1786 -0.0223 0.0163  -0.0033 196 TYR A O   
1675 C CB  . TYR A 196 ? 0.1704 0.1316 0.1855 -0.0185 0.0118  0.0076  196 TYR A CB  
1676 C CG  . TYR A 196 ? 0.1905 0.1489 0.2059 -0.0238 0.0116  0.0100  196 TYR A CG  
1677 C CD1 . TYR A 196 ? 0.1690 0.1372 0.1829 -0.0290 0.0134  0.0114  196 TYR A CD1 
1678 C CD2 . TYR A 196 ? 0.1801 0.1270 0.1975 -0.0238 0.0097  0.0105  196 TYR A CD2 
1679 C CE1 . TYR A 196 ? 0.1678 0.1355 0.1826 -0.0348 0.0134  0.0141  196 TYR A CE1 
1680 C CE2 . TYR A 196 ? 0.1755 0.1198 0.1938 -0.0296 0.0092  0.0130  196 TYR A CE2 
1681 C CZ  . TYR A 196 ? 0.1957 0.1511 0.2128 -0.0354 0.0112  0.0153  196 TYR A CZ  
1682 O OH  . TYR A 196 ? 0.2485 0.2032 0.2672 -0.0422 0.0109  0.0183  196 TYR A OH  
1683 N N   . TYR A 197 ? 0.1719 0.1541 0.1846 -0.0200 0.0152  0.0011  197 TYR A N   
1684 C CA  . TYR A 197 ? 0.1560 0.1485 0.1673 -0.0226 0.0166  -0.0015 197 TYR A CA  
1685 C C   . TYR A 197 ? 0.2116 0.2065 0.2242 -0.0203 0.0168  -0.0072 197 TYR A C   
1686 O O   . TYR A 197 ? 0.1733 0.1759 0.1848 -0.0213 0.0172  -0.0099 197 TYR A O   
1687 C CB  . TYR A 197 ? 0.1672 0.1666 0.1748 -0.0250 0.0162  0.0035  197 TYR A CB  
1688 C CG  . TYR A 197 ? 0.1865 0.1836 0.1929 -0.0286 0.0159  0.0099  197 TYR A CG  
1689 C CD1 . TYR A 197 ? 0.1753 0.1784 0.1815 -0.0331 0.0178  0.0094  197 TYR A CD1 
1690 C CD2 . TYR A 197 ? 0.2277 0.2164 0.2340 -0.0274 0.0133  0.0163  197 TYR A CD2 
1691 C CE1 . TYR A 197 ? 0.2179 0.2185 0.2234 -0.0377 0.0173  0.0161  197 TYR A CE1 
1692 C CE2 . TYR A 197 ? 0.2092 0.1935 0.2150 -0.0312 0.0123  0.0228  197 TYR A CE2 
1693 C CZ  . TYR A 197 ? 0.2278 0.2179 0.2331 -0.0368 0.0142  0.0231  197 TYR A CZ  
1694 O OH  . TYR A 197 ? 0.2716 0.2570 0.2767 -0.0416 0.0129  0.0304  197 TYR A OH  
1695 N N   . HIS A 198 ? 0.1621 0.1505 0.1771 -0.0174 0.0163  -0.0093 198 HIS A N   
1696 C CA  . HIS A 198 ? 0.1626 0.1515 0.1792 -0.0160 0.0159  -0.0134 198 HIS A CA  
1697 C C   . HIS A 198 ? 0.1633 0.1563 0.1790 -0.0160 0.0150  -0.0129 198 HIS A C   
1698 O O   . HIS A 198 ? 0.1595 0.1561 0.1756 -0.0169 0.0146  -0.0169 198 HIS A O   
1699 C CB  . HIS A 198 ? 0.1634 0.1560 0.1817 -0.0168 0.0166  -0.0184 198 HIS A CB  
1700 C CG  . HIS A 198 ? 0.2039 0.1935 0.2251 -0.0149 0.0154  -0.0224 198 HIS A CG  
1701 N ND1 . HIS A 198 ? 0.2301 0.2215 0.2521 -0.0149 0.0144  -0.0257 198 HIS A ND1 
1702 C CD2 . HIS A 198 ? 0.1919 0.1765 0.2153 -0.0133 0.0146  -0.0233 198 HIS A CD2 
1703 C CE1 . HIS A 198 ? 0.2357 0.2220 0.2607 -0.0134 0.0128  -0.0278 198 HIS A CE1 
1704 N NE2 . HIS A 198 ? 0.2113 0.1942 0.2370 -0.0123 0.0130  -0.0262 198 HIS A NE2 
1705 N N   . PRO A 199 ? 0.1525 0.1453 0.1674 -0.0151 0.0142  -0.0086 199 PRO A N   
1706 C CA  . PRO A 199 ? 0.1608 0.1589 0.1755 -0.0154 0.0130  -0.0081 199 PRO A CA  
1707 C C   . PRO A 199 ? 0.3019 0.2983 0.3195 -0.0145 0.0124  -0.0097 199 PRO A C   
1708 O O   . PRO A 199 ? 0.2714 0.2626 0.2903 -0.0132 0.0129  -0.0103 199 PRO A O   
1709 C CB  . PRO A 199 ? 0.1732 0.1719 0.1873 -0.0138 0.0121  -0.0025 199 PRO A CB  
1710 C CG  . PRO A 199 ? 0.2155 0.2063 0.2311 -0.0112 0.0127  -0.0016 199 PRO A CG  
1711 C CD  . PRO A 199 ? 0.1879 0.1755 0.2030 -0.0130 0.0140  -0.0047 199 PRO A CD  
1712 N N   . LEU A 200 ? 0.2525 0.2541 0.2707 -0.0157 0.0111  -0.0097 200 LEU A N   
1713 C CA  . LEU A 200 ? 0.2373 0.2392 0.2585 -0.0160 0.0104  -0.0095 200 LEU A CA  
1714 C C   . LEU A 200 ? 0.2102 0.2155 0.2327 -0.0135 0.0106  -0.0053 200 LEU A C   
1715 O O   . LEU A 200 ? 0.1946 0.2069 0.2180 -0.0138 0.0093  -0.0034 200 LEU A O   
1716 C CB  . LEU A 200 ? 0.2600 0.2659 0.2822 -0.0193 0.0085  -0.0121 200 LEU A CB  
1717 C CG  . LEU A 200 ? 0.2966 0.2986 0.3187 -0.0209 0.0078  -0.0177 200 LEU A CG  
1718 C CD1 . LEU A 200 ? 0.3339 0.3405 0.3565 -0.0241 0.0056  -0.0211 200 LEU A CD1 
1719 C CD2 . LEU A 200 ? 0.2991 0.2934 0.3239 -0.0206 0.0076  -0.0182 200 LEU A CD2 
1720 N N   . ILE A 201 ? 0.1862 0.1874 0.2092 -0.0106 0.0119  -0.0043 201 ILE A N   
1721 C CA  . ILE A 201 ? 0.1861 0.1903 0.2110 -0.0069 0.0123  -0.0017 201 ILE A CA  
1722 C C   . ILE A 201 ? 0.1737 0.1871 0.2020 -0.0076 0.0117  -0.0004 201 ILE A C   
1723 O O   . ILE A 201 ? 0.1957 0.2152 0.2261 -0.0052 0.0109  0.0019  201 ILE A O   
1724 C CB  . ILE A 201 ? 0.1898 0.1885 0.2144 -0.0040 0.0138  -0.0027 201 ILE A CB  
1725 C CG1 . ILE A 201 ? 0.2059 0.1964 0.2280 -0.0034 0.0139  -0.0034 201 ILE A CG1 
1726 C CG2 . ILE A 201 ? 0.1352 0.1387 0.1626 0.0004  0.0144  -0.0017 201 ILE A CG2 
1727 C CD1 . ILE A 201 ? 0.2129 0.2022 0.2351 -0.0015 0.0127  -0.0005 201 ILE A CD1 
1728 N N   . PRO A 202 ? 0.1655 0.1807 0.1950 -0.0111 0.0118  -0.0013 202 PRO A N   
1729 C CA  . PRO A 202 ? 0.1978 0.2232 0.2313 -0.0128 0.0112  0.0005  202 PRO A CA  
1730 C C   . PRO A 202 ? 0.1857 0.2181 0.2204 -0.0142 0.0089  0.0012  202 PRO A C   
1731 O O   . PRO A 202 ? 0.1980 0.2402 0.2364 -0.0127 0.0084  0.0034  202 PRO A O   
1732 C CB  . PRO A 202 ? 0.2422 0.2655 0.2763 -0.0178 0.0109  -0.0001 202 PRO A CB  
1733 C CG  . PRO A 202 ? 0.1322 0.1459 0.1631 -0.0163 0.0120  -0.0014 202 PRO A CG  
1734 C CD  . PRO A 202 ? 0.1741 0.1824 0.2022 -0.0136 0.0121  -0.0032 202 PRO A CD  
1735 N N   . ILE A 203 ? 0.1353 0.1641 0.1670 -0.0167 0.0074  -0.0009 203 ILE A N   
1736 C CA  . ILE A 203 ? 0.1334 0.1699 0.1650 -0.0183 0.0050  -0.0004 203 ILE A CA  
1737 C C   . ILE A 203 ? 0.1573 0.1970 0.1883 -0.0138 0.0045  0.0032  203 ILE A C   
1738 O O   . ILE A 203 ? 0.1750 0.2244 0.2085 -0.0131 0.0026  0.0057  203 ILE A O   
1739 C CB  . ILE A 203 ? 0.1723 0.2054 0.2002 -0.0220 0.0038  -0.0046 203 ILE A CB  
1740 C CG1 . ILE A 203 ? 0.2241 0.2536 0.2542 -0.0263 0.0029  -0.0081 203 ILE A CG1 
1741 C CG2 . ILE A 203 ? 0.1716 0.2140 0.1979 -0.0235 0.0012  -0.0043 203 ILE A CG2 
1742 C CD1 . ILE A 203 ? 0.2417 0.2671 0.2691 -0.0289 0.0016  -0.0140 203 ILE A CD1 
1743 N N   . LEU A 204 ? 0.1655 0.1970 0.1937 -0.0106 0.0059  0.0040  204 LEU A N   
1744 C CA  . LEU A 204 ? 0.1815 0.2136 0.2096 -0.0065 0.0048  0.0081  204 LEU A CA  
1745 C C   . LEU A 204 ? 0.2059 0.2434 0.2397 -0.0016 0.0046  0.0102  204 LEU A C   
1746 O O   . LEU A 204 ? 0.1714 0.2147 0.2073 0.0014  0.0022  0.0138  204 LEU A O   
1747 C CB  . LEU A 204 ? 0.1874 0.2083 0.2123 -0.0049 0.0061  0.0084  204 LEU A CB  
1748 C CG  . LEU A 204 ? 0.2098 0.2267 0.2297 -0.0089 0.0068  0.0065  204 LEU A CG  
1749 C CD1 . LEU A 204 ? 0.1986 0.2070 0.2167 -0.0073 0.0074  0.0087  204 LEU A CD1 
1750 C CD2 . LEU A 204 ? 0.1905 0.2158 0.2073 -0.0122 0.0049  0.0073  204 LEU A CD2 
1751 N N   . LEU A 205 ? 0.2039 0.2409 0.2404 -0.0005 0.0070  0.0080  205 LEU A N   
1752 C CA  . LEU A 205 ? 0.1156 0.1606 0.1579 0.0042  0.0075  0.0088  205 LEU A CA  
1753 C C   . LEU A 205 ? 0.2015 0.2609 0.2482 0.0019  0.0059  0.0101  205 LEU A C   
1754 O O   . LEU A 205 ? 0.1956 0.2641 0.2475 0.0063  0.0046  0.0122  205 LEU A O   
1755 C CB  . LEU A 205 ? 0.1217 0.1646 0.1645 0.0049  0.0107  0.0059  205 LEU A CB  
1756 C CG  . LEU A 205 ? 0.1965 0.2271 0.2362 0.0087  0.0118  0.0043  205 LEU A CG  
1757 C CD1 . LEU A 205 ? 0.1374 0.1664 0.1760 0.0086  0.0147  0.0012  205 LEU A CD1 
1758 C CD2 . LEU A 205 ? 0.2425 0.2732 0.2858 0.0160  0.0106  0.0054  205 LEU A CD2 
1759 N N   . ASN A 206 ? 0.1928 0.2544 0.2385 -0.0049 0.0057  0.0087  206 ASN A N   
1760 C CA  . ASN A 206 ? 0.1389 0.2142 0.1896 -0.0084 0.0043  0.0095  206 ASN A CA  
1761 C C   . ASN A 206 ? 0.1504 0.2231 0.1983 -0.0162 0.0026  0.0073  206 ASN A C   
1762 O O   . ASN A 206 ? 0.1629 0.2311 0.2106 -0.0205 0.0038  0.0057  206 ASN A O   
1763 C CB  . ASN A 206 ? 0.1716 0.2549 0.2275 -0.0082 0.0069  0.0096  206 ASN A CB  
1764 C CG  . ASN A 206 ? 0.1795 0.2771 0.2410 -0.0138 0.0055  0.0107  206 ASN A CG  
1765 O OD1 . ASN A 206 ? 0.1663 0.2707 0.2292 -0.0157 0.0022  0.0114  206 ASN A OD1 
1766 N ND2 . ASN A 206 ? 0.1974 0.3003 0.2617 -0.0172 0.0078  0.0111  206 ASN A ND2 
1767 N N   . PRO A 207 ? 0.1951 0.2701 0.2406 -0.0179 -0.0004 0.0071  207 PRO A N   
1768 C CA  . PRO A 207 ? 0.2012 0.2739 0.2441 -0.0247 -0.0022 0.0034  207 PRO A CA  
1769 C C   . PRO A 207 ? 0.1803 0.2595 0.2285 -0.0306 -0.0032 0.0027  207 PRO A C   
1770 O O   . PRO A 207 ? 0.2133 0.2864 0.2604 -0.0361 -0.0044 -0.0009 207 PRO A O   
1771 C CB  . PRO A 207 ? 0.2021 0.2811 0.2419 -0.0249 -0.0053 0.0038  207 PRO A CB  
1772 C CG  . PRO A 207 ? 0.2304 0.3087 0.2691 -0.0182 -0.0048 0.0082  207 PRO A CG  
1773 C CD  . PRO A 207 ? 0.2192 0.2991 0.2639 -0.0137 -0.0026 0.0103  207 PRO A CD  
1774 N N   . ASN A 208 ? 0.1864 0.2781 0.2411 -0.0297 -0.0030 0.0059  208 ASN A N   
1775 C CA  . ASN A 208 ? 0.1569 0.2558 0.2170 -0.0366 -0.0040 0.0060  208 ASN A CA  
1776 C C   . ASN A 208 ? 0.1853 0.2753 0.2454 -0.0396 -0.0016 0.0061  208 ASN A C   
1777 O O   . ASN A 208 ? 0.1626 0.2553 0.2264 -0.0468 -0.0028 0.0067  208 ASN A O   
1778 C CB  . ASN A 208 ? 0.1833 0.3009 0.2512 -0.0349 -0.0041 0.0096  208 ASN A CB  
1779 C CG  . ASN A 208 ? 0.2084 0.3364 0.2773 -0.0330 -0.0078 0.0102  208 ASN A CG  
1780 O OD1 . ASN A 208 ? 0.2553 0.3798 0.3196 -0.0363 -0.0109 0.0076  208 ASN A OD1 
1781 N ND2 . ASN A 208 ? 0.2548 0.3961 0.3295 -0.0273 -0.0077 0.0134  208 ASN A ND2 
1782 N N   . CYS A 209 ? 0.1688 0.2480 0.2246 -0.0349 0.0014  0.0059  209 CYS A N   
1783 C CA  . CYS A 209 ? 0.1674 0.2392 0.2227 -0.0378 0.0032  0.0067  209 CYS A CA  
1784 C C   . CYS A 209 ? 0.2190 0.2793 0.2728 -0.0441 0.0004  0.0040  209 CYS A C   
1785 O O   . CYS A 209 ? 0.1973 0.2528 0.2523 -0.0485 0.0005  0.0059  209 CYS A O   
1786 C CB  . CYS A 209 ? 0.2348 0.2980 0.2858 -0.0314 0.0065  0.0065  209 CYS A CB  
1787 S SG  . CYS A 209 ? 0.2805 0.3275 0.3246 -0.0287 0.0058  0.0026  209 CYS A SG  
1788 N N   . VAL A 210 ? 0.2265 0.2823 0.2776 -0.0446 -0.0022 -0.0003 210 VAL A N   
1789 C CA  . VAL A 210 ? 0.2422 0.2869 0.2926 -0.0497 -0.0051 -0.0045 210 VAL A CA  
1790 C C   . VAL A 210 ? 0.2250 0.2734 0.2811 -0.0579 -0.0079 -0.0030 210 VAL A C   
1791 O O   . VAL A 210 ? 0.2474 0.2845 0.3045 -0.0626 -0.0103 -0.0046 210 VAL A O   
1792 C CB  . VAL A 210 ? 0.2177 0.2605 0.2642 -0.0486 -0.0071 -0.0104 210 VAL A CB  
1793 C CG1 . VAL A 210 ? 0.1585 0.1984 0.1996 -0.0417 -0.0043 -0.0108 210 VAL A CG1 
1794 C CG2 . VAL A 210 ? 0.1995 0.2558 0.2478 -0.0512 -0.0097 -0.0108 210 VAL A CG2 
1795 N N   . TYR A 211 ? 0.1657 0.2297 0.2264 -0.0599 -0.0080 0.0003  211 TYR A N   
1796 C CA  . TYR A 211 ? 0.1904 0.2600 0.2573 -0.0688 -0.0109 0.0021  211 TYR A CA  
1797 C C   . TYR A 211 ? 0.1853 0.2526 0.2548 -0.0728 -0.0092 0.0078  211 TYR A C   
1798 O O   . TYR A 211 ? 0.2291 0.2970 0.3034 -0.0816 -0.0120 0.0100  211 TYR A O   
1799 C CB  . TYR A 211 ? 0.1848 0.2743 0.2565 -0.0695 -0.0115 0.0039  211 TYR A CB  
1800 C CG  . TYR A 211 ? 0.2198 0.3122 0.2884 -0.0668 -0.0140 -0.0009 211 TYR A CG  
1801 C CD1 . TYR A 211 ? 0.2763 0.3601 0.3424 -0.0710 -0.0180 -0.0072 211 TYR A CD1 
1802 C CD2 . TYR A 211 ? 0.1570 0.2606 0.2248 -0.0599 -0.0126 0.0009  211 TYR A CD2 
1803 C CE1 . TYR A 211 ? 0.2632 0.3517 0.3253 -0.0688 -0.0201 -0.0115 211 TYR A CE1 
1804 C CE2 . TYR A 211 ? 0.2393 0.3464 0.3036 -0.0578 -0.0152 -0.0021 211 TYR A CE2 
1805 C CZ  . TYR A 211 ? 0.3817 0.4822 0.4426 -0.0625 -0.0186 -0.0082 211 TYR A CZ  
1806 O OH  . TYR A 211 ? 0.5707 0.6769 0.6270 -0.0608 -0.0210 -0.0111 211 TYR A OH  
1807 N N   . GLU A 212 ? 0.2197 0.2843 0.2859 -0.0671 -0.0051 0.0105  212 GLU A N   
1808 C CA  . GLU A 212 ? 0.2884 0.3517 0.3557 -0.0710 -0.0036 0.0162  212 GLU A CA  
1809 C C   . GLU A 212 ? 0.3130 0.3576 0.3794 -0.0762 -0.0072 0.0159  212 GLU A C   
1810 O O   . GLU A 212 ? 0.3693 0.4128 0.4379 -0.0828 -0.0079 0.0218  212 GLU A O   
1811 C CB  . GLU A 212 ? 0.2729 0.3382 0.3360 -0.0632 0.0014  0.0180  212 GLU A CB  
1812 C CG  . GLU A 212 ? 0.3048 0.3876 0.3701 -0.0575 0.0046  0.0182  212 GLU A CG  
1813 C CD  . GLU A 212 ? 0.4082 0.4907 0.4693 -0.0490 0.0088  0.0179  212 GLU A CD  
1814 O OE1 . GLU A 212 ? 0.4440 0.5356 0.5063 -0.0422 0.0106  0.0164  212 GLU A OE1 
1815 O OE2 . GLU A 212 ? 0.3524 0.4254 0.4093 -0.0491 0.0099  0.0191  212 GLU A OE2 
1816 N N   . THR A 213 ? 0.2320 0.2627 0.2955 -0.0736 -0.0097 0.0094  213 THR A N   
1817 C CA  . THR A 213 ? 0.2195 0.2318 0.2832 -0.0771 -0.0138 0.0077  213 THR A CA  
1818 C C   . THR A 213 ? 0.2969 0.3030 0.3632 -0.0812 -0.0188 0.0008  213 THR A C   
1819 O O   . THR A 213 ? 0.3660 0.3592 0.4354 -0.0869 -0.0233 0.0006  213 THR A O   
1820 C CB  . THR A 213 ? 0.2648 0.2647 0.3233 -0.0695 -0.0124 0.0048  213 THR A CB  
1821 O OG1 . THR A 213 ? 0.2758 0.2790 0.3307 -0.0628 -0.0106 -0.0013 213 THR A OG1 
1822 C CG2 . THR A 213 ? 0.2850 0.2879 0.3408 -0.0668 -0.0085 0.0114  213 THR A CG2 
1823 N N   . THR A 214 ? 0.2671 0.2814 0.3319 -0.0784 -0.0188 -0.0050 214 THR A N   
1824 C CA  . THR A 214 ? 0.3237 0.3346 0.3902 -0.0823 -0.0236 -0.0126 214 THR A CA  
1825 C C   . THR A 214 ? 0.3082 0.3372 0.3773 -0.0857 -0.0243 -0.0123 214 THR A C   
1826 O O   . THR A 214 ? 0.2454 0.2827 0.3110 -0.0813 -0.0236 -0.0165 214 THR A O   
1827 C CB  . THR A 214 ? 0.2657 0.2686 0.3269 -0.0757 -0.0236 -0.0214 214 THR A CB  
1828 O OG1 . THR A 214 ? 0.2589 0.2730 0.3153 -0.0688 -0.0194 -0.0209 214 THR A OG1 
1829 C CG2 . THR A 214 ? 0.2596 0.2457 0.3198 -0.0723 -0.0235 -0.0220 214 THR A CG2 
1830 N N   . PRO A 215 ? 0.2878 0.3242 0.3631 -0.0939 -0.0260 -0.0070 215 PRO A N   
1831 C CA  . PRO A 215 ? 0.2780 0.3344 0.3569 -0.0967 -0.0265 -0.0061 215 PRO A CA  
1832 C C   . PRO A 215 ? 0.3016 0.3598 0.3796 -0.0985 -0.0310 -0.0147 215 PRO A C   
1833 O O   . PRO A 215 ? 0.3073 0.3826 0.3859 -0.0976 -0.0311 -0.0147 215 PRO A O   
1834 C CB  . PRO A 215 ? 0.3918 0.4540 0.4785 -0.1068 -0.0280 0.0009  215 PRO A CB  
1835 C CG  . PRO A 215 ? 0.2753 0.3166 0.3622 -0.1111 -0.0303 0.0018  215 PRO A CG  
1836 C CD  . PRO A 215 ? 0.2539 0.2824 0.3337 -0.1012 -0.0274 -0.0007 215 PRO A CD  
1837 N N   . ASN A 216 ? 0.2693 0.3110 0.3456 -0.1003 -0.0347 -0.0224 216 ASN A N   
1838 C CA  . ASN A 216 ? 0.3713 0.4152 0.4465 -0.1029 -0.0393 -0.0317 216 ASN A CA  
1839 C C   . ASN A 216 ? 0.3643 0.4105 0.4312 -0.0943 -0.0374 -0.0380 216 ASN A C   
1840 O O   . ASN A 216 ? 0.3598 0.4110 0.4244 -0.0958 -0.0407 -0.0458 216 ASN A O   
1841 C CB  . ASN A 216 ? 0.4567 0.4819 0.5349 -0.1093 -0.0449 -0.0384 216 ASN A CB  
1842 C CG  . ASN A 216 ? 0.5275 0.5511 0.6143 -0.1200 -0.0481 -0.0320 216 ASN A CG  
1843 O OD1 . ASN A 216 ? 0.4603 0.5016 0.5514 -0.1245 -0.0474 -0.0256 216 ASN A OD1 
1844 N ND2 . ASN A 216 ? 0.6212 0.6244 0.7110 -0.1230 -0.0511 -0.0332 216 ASN A ND2 
1845 N N   . VAL A 217 ? 0.3675 0.4113 0.4299 -0.0861 -0.0322 -0.0346 217 VAL A N   
1846 C CA  . VAL A 217 ? 0.2999 0.3440 0.3546 -0.0788 -0.0302 -0.0399 217 VAL A CA  
1847 C C   . VAL A 217 ? 0.3289 0.3917 0.3806 -0.0773 -0.0303 -0.0390 217 VAL A C   
1848 O O   . VAL A 217 ? 0.2704 0.3460 0.3257 -0.0780 -0.0297 -0.0318 217 VAL A O   
1849 C CB  . VAL A 217 ? 0.2430 0.2795 0.2946 -0.0714 -0.0251 -0.0356 217 VAL A CB  
1850 C CG1 . VAL A 217 ? 0.3149 0.3634 0.3667 -0.0677 -0.0212 -0.0266 217 VAL A CG1 
1851 C CG2 . VAL A 217 ? 0.3163 0.3481 0.3612 -0.0656 -0.0236 -0.0424 217 VAL A CG2 
1852 N N   . LYS A 218 ? 0.2062 0.2717 0.2514 -0.0753 -0.0313 -0.0462 218 LYS A N   
1853 C CA  . LYS A 218 ? 0.1956 0.2780 0.2362 -0.0730 -0.0314 -0.0445 218 LYS A CA  
1854 C C   . LYS A 218 ? 0.2205 0.3023 0.2552 -0.0649 -0.0266 -0.0403 218 LYS A C   
1855 O O   . LYS A 218 ? 0.2572 0.3284 0.2879 -0.0619 -0.0244 -0.0446 218 LYS A O   
1856 C CB  . LYS A 218 ? 0.2405 0.3284 0.2765 -0.0762 -0.0355 -0.0544 218 LYS A CB  
1857 C CG  . LYS A 218 ? 0.3054 0.3965 0.3471 -0.0849 -0.0412 -0.0587 218 LYS A CG  
1858 C CD  . LYS A 218 ? 0.4078 0.5069 0.4437 -0.0875 -0.0453 -0.0691 218 LYS A CD  
1859 C CE  . LYS A 218 ? 0.4854 0.6031 0.5142 -0.0839 -0.0447 -0.0650 218 LYS A CE  
1860 N NZ  . LYS A 218 ? 0.6071 0.7373 0.6307 -0.0881 -0.0496 -0.0738 218 LYS A NZ  
1861 N N   . ILE A 219 ? 0.2220 0.3149 0.2566 -0.0615 -0.0252 -0.0321 219 ILE A N   
1862 C CA  . ILE A 219 ? 0.2206 0.3128 0.2497 -0.0545 -0.0215 -0.0278 219 ILE A CA  
1863 C C   . ILE A 219 ? 0.2451 0.3526 0.2704 -0.0531 -0.0236 -0.0242 219 ILE A C   
1864 O O   . ILE A 219 ? 0.2686 0.3885 0.2972 -0.0563 -0.0273 -0.0230 219 ILE A O   
1865 C CB  . ILE A 219 ? 0.2126 0.2991 0.2458 -0.0501 -0.0177 -0.0204 219 ILE A CB  
1866 C CG1 . ILE A 219 ? 0.2368 0.3356 0.2763 -0.0497 -0.0187 -0.0136 219 ILE A CG1 
1867 C CG2 . ILE A 219 ? 0.1747 0.2463 0.2109 -0.0515 -0.0160 -0.0229 219 ILE A CG2 
1868 C CD1 . ILE A 219 ? 0.3250 0.4202 0.3675 -0.0440 -0.0147 -0.0073 219 ILE A CD1 
1869 N N   . PRO A 220 ? 0.2421 0.3499 0.2603 -0.0489 -0.0216 -0.0220 220 PRO A N   
1870 C CA  . PRO A 220 ? 0.2228 0.3445 0.2368 -0.0476 -0.0240 -0.0170 220 PRO A CA  
1871 C C   . PRO A 220 ? 0.1930 0.3204 0.2133 -0.0436 -0.0245 -0.0076 220 PRO A C   
1872 O O   . PRO A 220 ? 0.2151 0.3364 0.2421 -0.0415 -0.0223 -0.0052 220 PRO A O   
1873 C CB  . PRO A 220 ? 0.2608 0.3790 0.2663 -0.0447 -0.0212 -0.0161 220 PRO A CB  
1874 C CG  . PRO A 220 ? 0.2924 0.3951 0.2996 -0.0430 -0.0169 -0.0189 220 PRO A CG  
1875 C CD  . PRO A 220 ? 0.2811 0.3776 0.2946 -0.0464 -0.0178 -0.0250 220 PRO A CD  
1876 N N   . ASP A 221 ? 0.2163 0.3567 0.2342 -0.0425 -0.0279 -0.0026 221 ASP A N   
1877 C CA  . ASP A 221 ? 0.1744 0.3220 0.1982 -0.0374 -0.0293 0.0062  221 ASP A CA  
1878 C C   . ASP A 221 ? 0.1930 0.3299 0.2150 -0.0309 -0.0261 0.0123  221 ASP A C   
1879 O O   . ASP A 221 ? 0.2277 0.3641 0.2422 -0.0297 -0.0265 0.0157  221 ASP A O   
1880 C CB  . ASP A 221 ? 0.1754 0.3401 0.1968 -0.0384 -0.0349 0.0096  221 ASP A CB  
1881 C CG  . ASP A 221 ? 0.2452 0.4182 0.2737 -0.0325 -0.0372 0.0185  221 ASP A CG  
1882 O OD1 . ASP A 221 ? 0.2213 0.3927 0.2592 -0.0297 -0.0353 0.0194  221 ASP A OD1 
1883 O OD2 . ASP A 221 ? 0.2815 0.4632 0.3062 -0.0302 -0.0410 0.0246  221 ASP A OD2 
1884 N N   . PHE A 222 ? 0.1465 0.2749 0.1750 -0.0271 -0.0228 0.0136  222 PHE A N   
1885 C CA  . PHE A 222 ? 0.1667 0.2838 0.1942 -0.0211 -0.0200 0.0183  222 PHE A CA  
1886 C C   . PHE A 222 ? 0.1778 0.3015 0.2093 -0.0148 -0.0231 0.0264  222 PHE A C   
1887 O O   . PHE A 222 ? 0.1983 0.3215 0.2376 -0.0095 -0.0222 0.0285  222 PHE A O   
1888 C CB  . PHE A 222 ? 0.2223 0.3282 0.2542 -0.0197 -0.0156 0.0154  222 PHE A CB  
1889 C CG  . PHE A 222 ? 0.2059 0.3004 0.2328 -0.0233 -0.0126 0.0095  222 PHE A CG  
1890 C CD1 . PHE A 222 ? 0.2399 0.3353 0.2668 -0.0292 -0.0130 0.0029  222 PHE A CD1 
1891 C CD2 . PHE A 222 ? 0.1793 0.2622 0.2021 -0.0206 -0.0097 0.0105  222 PHE A CD2 
1892 C CE1 . PHE A 222 ? 0.2023 0.2871 0.2256 -0.0314 -0.0107 -0.0027 222 PHE A CE1 
1893 C CE2 . PHE A 222 ? 0.1661 0.2401 0.1854 -0.0233 -0.0071 0.0051  222 PHE A CE2 
1894 C CZ  . PHE A 222 ? 0.2217 0.2965 0.2412 -0.0282 -0.0076 -0.0016 222 PHE A CZ  
1895 N N   . ALA A 223 ? 0.1920 0.3227 0.2180 -0.0152 -0.0269 0.0310  223 ALA A N   
1896 C CA  . ALA A 223 ? 0.2332 0.3708 0.2624 -0.0095 -0.0312 0.0397  223 ALA A CA  
1897 C C   . ALA A 223 ? 0.2655 0.3895 0.2955 -0.0027 -0.0301 0.0456  223 ALA A C   
1898 O O   . ALA A 223 ? 0.3254 0.4523 0.3586 0.0029  -0.0342 0.0531  223 ALA A O   
1899 C CB  . ALA A 223 ? 0.2166 0.3658 0.2381 -0.0131 -0.0360 0.0433  223 ALA A CB  
1900 N N   . VAL A 224 ? 0.1957 0.3045 0.2234 -0.0030 -0.0253 0.0424  224 VAL A N   
1901 C CA  . VAL A 224 ? 0.2525 0.3472 0.2812 0.0026  -0.0244 0.0469  224 VAL A CA  
1902 C C   . VAL A 224 ? 0.1950 0.2796 0.2279 0.0043  -0.0193 0.0407  224 VAL A C   
1903 O O   . VAL A 224 ? 0.2829 0.3676 0.3143 -0.0005 -0.0161 0.0340  224 VAL A O   
1904 C CB  . VAL A 224 ? 0.2414 0.3279 0.2606 -0.0008 -0.0241 0.0507  224 VAL A CB  
1905 C CG1 . VAL A 224 ? 0.4487 0.5457 0.4626 -0.0027 -0.0291 0.0579  224 VAL A CG1 
1906 C CG2 . VAL A 224 ? 0.2670 0.3503 0.2803 -0.0073 -0.0195 0.0429  224 VAL A CG2 
1907 N N   . SER A 225 ? 0.2696 0.3450 0.3074 0.0112  -0.0190 0.0428  225 SER A N   
1908 C CA  . SER A 225 ? 0.2237 0.2906 0.2650 0.0134  -0.0144 0.0371  225 SER A CA  
1909 C C   . SER A 225 ? 0.1590 0.2111 0.1939 0.0105  -0.0116 0.0358  225 SER A C   
1910 O O   . SER A 225 ? 0.2411 0.2854 0.2725 0.0110  -0.0135 0.0411  225 SER A O   
1911 C CB  . SER A 225 ? 0.2327 0.2978 0.2826 0.0226  -0.0153 0.0383  225 SER A CB  
1912 O OG  . SER A 225 ? 0.2554 0.3125 0.3069 0.0244  -0.0109 0.0326  225 SER A OG  
1913 N N   . PHE A 226 ? 0.1726 0.2212 0.2062 0.0072  -0.0075 0.0294  226 PHE A N   
1914 C CA  . PHE A 226 ? 0.1535 0.1892 0.1826 0.0052  -0.0047 0.0274  226 PHE A CA  
1915 C C   . PHE A 226 ? 0.1621 0.1891 0.1952 0.0098  -0.0022 0.0241  226 PHE A C   
1916 O O   . PHE A 226 ? 0.2018 0.2191 0.2319 0.0080  0.0002  0.0214  226 PHE A O   
1917 C CB  . PHE A 226 ? 0.1943 0.2316 0.2186 -0.0015 -0.0024 0.0224  226 PHE A CB  
1918 C CG  . PHE A 226 ? 0.2190 0.2631 0.2375 -0.0064 -0.0042 0.0241  226 PHE A CG  
1919 C CD1 . PHE A 226 ? 0.2568 0.2963 0.2696 -0.0086 -0.0040 0.0270  226 PHE A CD1 
1920 C CD2 . PHE A 226 ? 0.2331 0.2892 0.2516 -0.0093 -0.0059 0.0223  226 PHE A CD2 
1921 C CE1 . PHE A 226 ? 0.2573 0.3053 0.2638 -0.0132 -0.0052 0.0282  226 PHE A CE1 
1922 C CE2 . PHE A 226 ? 0.1987 0.2622 0.2110 -0.0137 -0.0076 0.0228  226 PHE A CE2 
1923 C CZ  . PHE A 226 ? 0.2005 0.2606 0.2066 -0.0154 -0.0070 0.0257  226 PHE A CZ  
1924 N N   . ARG A 227 ? 0.1621 0.1937 0.2019 0.0158  -0.0028 0.0240  227 ARG A N   
1925 C CA  . ARG A 227 ? 0.1639 0.1904 0.2071 0.0202  -0.0001 0.0196  227 ARG A CA  
1926 C C   . ARG A 227 ? 0.2287 0.2398 0.2705 0.0231  -0.0006 0.0201  227 ARG A C   
1927 O O   . ARG A 227 ? 0.2289 0.2323 0.2689 0.0224  0.0021  0.0158  227 ARG A O   
1928 C CB  . ARG A 227 ? 0.2724 0.3098 0.3236 0.0265  -0.0005 0.0188  227 ARG A CB  
1929 C CG  . ARG A 227 ? 0.2378 0.2910 0.2915 0.0227  0.0003  0.0178  227 ARG A CG  
1930 C CD  . ARG A 227 ? 0.3294 0.3960 0.3921 0.0289  0.0003  0.0171  227 ARG A CD  
1931 N NE  . ARG A 227 ? 0.3202 0.3842 0.3852 0.0338  0.0037  0.0123  227 ARG A NE  
1932 C CZ  . ARG A 227 ? 0.3527 0.4205 0.4167 0.0303  0.0076  0.0086  227 ARG A CZ  
1933 N NH1 . ARG A 227 ? 0.3583 0.4307 0.4196 0.0221  0.0084  0.0092  227 ARG A NH1 
1934 N NH2 . ARG A 227 ? 0.3716 0.4384 0.4370 0.0351  0.0105  0.0042  227 ARG A NH2 
1935 N N   . GLU A 228 ? 0.1904 0.1966 0.2329 0.0258  -0.0044 0.0259  228 GLU A N   
1936 C CA  . GLU A 228 ? 0.2401 0.2302 0.2816 0.0275  -0.0055 0.0270  228 GLU A CA  
1937 C C   . GLU A 228 ? 0.2674 0.2507 0.3020 0.0198  -0.0037 0.0270  228 GLU A C   
1938 O O   . GLU A 228 ? 0.2295 0.2013 0.2633 0.0196  -0.0027 0.0246  228 GLU A O   
1939 C CB  . GLU A 228 ? 0.3132 0.2988 0.3575 0.0317  -0.0108 0.0344  228 GLU A CB  
1940 C CG  . GLU A 228 ? 0.5361 0.5039 0.5788 0.0312  -0.0129 0.0375  228 GLU A CG  
1941 C CD  . GLU A 228 ? 0.7340 0.6900 0.7822 0.0384  -0.0131 0.0321  228 GLU A CD  
1942 O OE1 . GLU A 228 ? 0.7636 0.7249 0.8142 0.0416  -0.0096 0.0241  228 GLU A OE1 
1943 O OE2 . GLU A 228 ? 0.8287 0.7700 0.8786 0.0405  -0.0169 0.0359  228 GLU A OE2 
1944 N N   . ASP A 229 ? 0.2075 0.1987 0.2373 0.0135  -0.0032 0.0289  229 ASP A N   
1945 C CA  . ASP A 229 ? 0.1978 0.1848 0.2219 0.0070  -0.0011 0.0278  229 ASP A CA  
1946 C C   . ASP A 229 ? 0.2153 0.2003 0.2396 0.0063  0.0027  0.0203  229 ASP A C   
1947 O O   . ASP A 229 ? 0.2260 0.2031 0.2482 0.0038  0.0040  0.0185  229 ASP A O   
1948 C CB  . ASP A 229 ? 0.2224 0.2197 0.2416 0.0012  -0.0012 0.0298  229 ASP A CB  
1949 C CG  . ASP A 229 ? 0.2889 0.2861 0.3050 -0.0006 -0.0045 0.0382  229 ASP A CG  
1950 O OD1 . ASP A 229 ? 0.2766 0.2640 0.2951 0.0027  -0.0071 0.0430  229 ASP A OD1 
1951 O OD2 . ASP A 229 ? 0.3020 0.3088 0.3130 -0.0054 -0.0046 0.0399  229 ASP A OD2 
1952 N N   . ALA A 230 ? 0.1898 0.1824 0.2166 0.0080  0.0041  0.0165  230 ALA A N   
1953 C CA  . ALA A 230 ? 0.1457 0.1367 0.1725 0.0073  0.0071  0.0106  230 ALA A CA  
1954 C C   . ALA A 230 ? 0.1779 0.1589 0.2061 0.0112  0.0075  0.0083  230 ALA A C   
1955 O O   . ALA A 230 ? 0.1653 0.1407 0.1913 0.0091  0.0091  0.0051  230 ALA A O   
1956 C CB  . ALA A 230 ? 0.1871 0.1885 0.2169 0.0082  0.0082  0.0084  230 ALA A CB  
1957 N N   . SER A 231 ? 0.1885 0.1673 0.2207 0.0172  0.0057  0.0095  231 SER A N   
1958 C CA  . SER A 231 ? 0.1966 0.1649 0.2304 0.0213  0.0056  0.0062  231 SER A CA  
1959 C C   . SER A 231 ? 0.2213 0.1774 0.2521 0.0175  0.0043  0.0082  231 SER A C   
1960 O O   . SER A 231 ? 0.2204 0.1692 0.2502 0.0168  0.0053  0.0040  231 SER A O   
1961 C CB  . SER A 231 ? 0.2484 0.2159 0.2879 0.0292  0.0032  0.0070  231 SER A CB  
1962 O OG  . SER A 231 ? 0.4231 0.4015 0.4661 0.0336  0.0053  0.0027  231 SER A OG  
1963 N N   . LYS A 232 ? 0.2040 0.1590 0.2333 0.0144  0.0021  0.0148  232 LYS A N   
1964 C CA  . LYS A 232 ? 0.2015 0.1470 0.2282 0.0095  0.0009  0.0181  232 LYS A CA  
1965 C C   . LYS A 232 ? 0.2308 0.1785 0.2539 0.0035  0.0040  0.0147  232 LYS A C   
1966 O O   . LYS A 232 ? 0.2234 0.1630 0.2459 0.0007  0.0039  0.0138  232 LYS A O   
1967 C CB  . LYS A 232 ? 0.2504 0.1981 0.2753 0.0066  -0.0017 0.0268  232 LYS A CB  
1968 C CG  . LYS A 232 ? 0.3794 0.3203 0.4082 0.0119  -0.0062 0.0322  232 LYS A CG  
1969 C CD  . LYS A 232 ? 0.5038 0.4441 0.5295 0.0072  -0.0093 0.0422  232 LYS A CD  
1970 C CE  . LYS A 232 ? 0.7092 0.6509 0.7382 0.0128  -0.0138 0.0485  232 LYS A CE  
1971 N NZ  . LYS A 232 ? 0.8022 0.7593 0.8272 0.0097  -0.0141 0.0531  232 LYS A NZ  
1972 N N   . HIS A 233 ? 0.1823 0.1409 0.2035 0.0014  0.0062  0.0128  233 HIS A N   
1973 C CA  . HIS A 233 ? 0.2166 0.1769 0.2356 -0.0029 0.0086  0.0089  233 HIS A CA  
1974 C C   . HIS A 233 ? 0.2788 0.2328 0.2990 -0.0009 0.0095  0.0035  233 HIS A C   
1975 O O   . HIS A 233 ? 0.2119 0.1619 0.2313 -0.0040 0.0099  0.0018  233 HIS A O   
1976 C CB  . HIS A 233 ? 0.1823 0.1530 0.2002 -0.0044 0.0103  0.0066  233 HIS A CB  
1977 C CG  . HIS A 233 ? 0.2165 0.1946 0.2318 -0.0082 0.0099  0.0097  233 HIS A CG  
1978 N ND1 . HIS A 233 ? 0.1624 0.1431 0.1752 -0.0129 0.0111  0.0090  233 HIS A ND1 
1979 C CD2 . HIS A 233 ? 0.2084 0.1934 0.2231 -0.0078 0.0085  0.0130  233 HIS A CD2 
1980 C CE1 . HIS A 233 ? 0.1999 0.1888 0.2100 -0.0153 0.0107  0.0113  233 HIS A CE1 
1981 N NE2 . HIS A 233 ? 0.1754 0.1669 0.1864 -0.0125 0.0089  0.0139  233 HIS A NE2 
1982 N N   . VAL A 234 ? 0.1926 0.1472 0.2148 0.0043  0.0097  0.0007  234 VAL A N   
1983 C CA  . VAL A 234 ? 0.2059 0.1565 0.2282 0.0062  0.0106  -0.0048 234 VAL A CA  
1984 C C   . VAL A 234 ? 0.2029 0.1416 0.2263 0.0072  0.0086  -0.0056 234 VAL A C   
1985 O O   . VAL A 234 ? 0.2108 0.1449 0.2332 0.0050  0.0087  -0.0090 234 VAL A O   
1986 C CB  . VAL A 234 ? 0.1566 0.1138 0.1804 0.0110  0.0119  -0.0077 234 VAL A CB  
1987 C CG1 . VAL A 234 ? 0.1827 0.1374 0.2054 0.0129  0.0129  -0.0136 234 VAL A CG1 
1988 C CG2 . VAL A 234 ? 0.2069 0.1743 0.2299 0.0085  0.0133  -0.0066 234 VAL A CG2 
1989 N N   . GLU A 235 ? 0.1697 0.1029 0.1957 0.0104  0.0062  -0.0023 235 GLU A N   
1990 C CA  . GLU A 235 ? 0.2102 0.1298 0.2380 0.0116  0.0035  -0.0033 235 GLU A CA  
1991 C C   . GLU A 235 ? 0.2609 0.1743 0.2872 0.0042  0.0025  0.0001  235 GLU A C   
1992 O O   . GLU A 235 ? 0.2655 0.1705 0.2921 0.0025  0.0016  -0.0034 235 GLU A O   
1993 C CB  . GLU A 235 ? 0.2390 0.1533 0.2707 0.0171  0.0004  0.0002  235 GLU A CB  
1994 C CG  . GLU A 235 ? 0.5643 0.4642 0.5993 0.0214  -0.0024 -0.0038 235 GLU A CG  
1995 C CD  . GLU A 235 ? 0.6419 0.5455 0.6790 0.0294  -0.0010 -0.0124 235 GLU A CD  
1996 O OE1 . GLU A 235 ? 0.5714 0.4779 0.6059 0.0285  0.0013  -0.0190 235 GLU A OE1 
1997 O OE2 . GLU A 235 ? 0.7360 0.6410 0.7775 0.0367  -0.0024 -0.0123 235 GLU A OE2 
1998 N N   . LEU A 236 ? 0.1946 0.1134 0.2191 -0.0006 0.0028  0.0065  236 LEU A N   
1999 C CA  . LEU A 236 ? 0.2285 0.1451 0.2517 -0.0081 0.0026  0.0097  236 LEU A CA  
2000 C C   . LEU A 236 ? 0.2132 0.1343 0.2353 -0.0112 0.0050  0.0039  236 LEU A C   
2001 O O   . LEU A 236 ? 0.2112 0.1278 0.2339 -0.0160 0.0043  0.0037  236 LEU A O   
2002 C CB  . LEU A 236 ? 0.2148 0.1398 0.2355 -0.0122 0.0029  0.0169  236 LEU A CB  
2003 C CG  . LEU A 236 ? 0.2910 0.2107 0.3127 -0.0103 -0.0005 0.0245  236 LEU A CG  
2004 C CD1 . LEU A 236 ? 0.3225 0.2534 0.3405 -0.0144 0.0000  0.0311  236 LEU A CD1 
2005 C CD2 . LEU A 236 ? 0.3303 0.2346 0.3543 -0.0126 -0.0041 0.0280  236 LEU A CD2 
2006 N N   . ALA A 237 ? 0.2101 0.1401 0.2310 -0.0087 0.0074  -0.0003 237 ALA A N   
2007 C CA  . ALA A 237 ? 0.2179 0.1516 0.2382 -0.0107 0.0090  -0.0053 237 ALA A CA  
2008 C C   . ALA A 237 ? 0.2431 0.1687 0.2643 -0.0091 0.0077  -0.0104 237 ALA A C   
2009 O O   . ALA A 237 ? 0.1899 0.1148 0.2114 -0.0128 0.0074  -0.0128 237 ALA A O   
2010 C CB  . ALA A 237 ? 0.1760 0.1189 0.1951 -0.0082 0.0110  -0.0078 237 ALA A CB  
2011 N N   . LYS A 238 ? 0.1951 0.1159 0.2169 -0.0034 0.0068  -0.0129 238 LYS A N   
2012 C CA  . LYS A 238 ? 0.1910 0.1038 0.2132 -0.0015 0.0053  -0.0189 238 LYS A CA  
2013 C C   . LYS A 238 ? 0.2043 0.1061 0.2285 -0.0061 0.0024  -0.0174 238 LYS A C   
2014 O O   . LYS A 238 ? 0.2224 0.1206 0.2466 -0.0087 0.0013  -0.0219 238 LYS A O   
2015 C CB  . LYS A 238 ? 0.2661 0.1760 0.2893 0.0060  0.0048  -0.0220 238 LYS A CB  
2016 C CG  . LYS A 238 ? 0.2469 0.1687 0.2685 0.0100  0.0077  -0.0242 238 LYS A CG  
2017 C CD  . LYS A 238 ? 0.2958 0.2176 0.3197 0.0176  0.0075  -0.0265 238 LYS A CD  
2018 C CE  . LYS A 238 ? 0.3287 0.2411 0.3535 0.0214  0.0057  -0.0339 238 LYS A CE  
2019 N NZ  . LYS A 238 ? 0.3814 0.2977 0.4087 0.0298  0.0063  -0.0380 238 LYS A NZ  
2020 N N   . GLU A 239 ? 0.2139 0.1103 0.2397 -0.0078 0.0008  -0.0106 239 GLU A N   
2021 C CA  . GLU A 239 ? 0.2325 0.1176 0.2605 -0.0131 -0.0023 -0.0076 239 GLU A CA  
2022 C C   . GLU A 239 ? 0.2461 0.1374 0.2737 -0.0214 -0.0011 -0.0064 239 GLU A C   
2023 O O   . GLU A 239 ? 0.2188 0.1035 0.2483 -0.0259 -0.0032 -0.0084 239 GLU A O   
2024 C CB  . GLU A 239 ? 0.2562 0.1358 0.2855 -0.0135 -0.0044 0.0012  239 GLU A CB  
2025 C CG  . GLU A 239 ? 0.3377 0.2079 0.3695 -0.0053 -0.0069 -0.0002 239 GLU A CG  
2026 C CD  . GLU A 239 ? 0.5674 0.4327 0.6006 -0.0055 -0.0097 0.0096  239 GLU A CD  
2027 O OE1 . GLU A 239 ? 0.6804 0.5429 0.7158 0.0021  -0.0113 0.0098  239 GLU A OE1 
2028 O OE2 . GLU A 239 ? 0.5249 0.3904 0.5569 -0.0134 -0.0103 0.0174  239 GLU A OE2 
2029 N N   . LYS A 240 ? 0.1982 0.1028 0.2241 -0.0236 0.0019  -0.0034 240 LYS A N   
2030 C CA  . LYS A 240 ? 0.2530 0.1658 0.2795 -0.0303 0.0033  -0.0030 240 LYS A CA  
2031 C C   . LYS A 240 ? 0.1842 0.0995 0.2111 -0.0295 0.0035  -0.0107 240 LYS A C   
2032 O O   . LYS A 240 ? 0.2082 0.1242 0.2374 -0.0349 0.0026  -0.0119 240 LYS A O   
2033 C CB  . LYS A 240 ? 0.2474 0.1741 0.2721 -0.0313 0.0065  0.0001  240 LYS A CB  
2034 C CG  . LYS A 240 ? 0.2336 0.1706 0.2598 -0.0376 0.0081  0.0003  240 LYS A CG  
2035 C CD  . LYS A 240 ? 0.2298 0.1638 0.2575 -0.0452 0.0068  0.0068  240 LYS A CD  
2036 C CE  . LYS A 240 ? 0.3071 0.2544 0.3370 -0.0517 0.0090  0.0069  240 LYS A CE  
2037 N NZ  . LYS A 240 ? 0.2937 0.2392 0.3246 -0.0603 0.0079  0.0148  240 LYS A NZ  
2038 N N   . TYR A 241 ? 0.2127 0.1309 0.2376 -0.0233 0.0045  -0.0154 241 TYR A N   
2039 C CA  . TYR A 241 ? 0.2140 0.1350 0.2384 -0.0223 0.0043  -0.0219 241 TYR A CA  
2040 C C   . TYR A 241 ? 0.2342 0.1447 0.2597 -0.0236 0.0011  -0.0261 241 TYR A C   
2041 O O   . TYR A 241 ? 0.2354 0.1481 0.2618 -0.0270 -0.0001 -0.0296 241 TYR A O   
2042 C CB  . TYR A 241 ? 0.1807 0.1060 0.2021 -0.0159 0.0057  -0.0248 241 TYR A CB  
2043 C CG  . TYR A 241 ? 0.1758 0.1057 0.1956 -0.0150 0.0054  -0.0302 241 TYR A CG  
2044 C CD1 . TYR A 241 ? 0.1752 0.0998 0.1935 -0.0131 0.0035  -0.0358 241 TYR A CD1 
2045 C CD2 . TYR A 241 ? 0.2518 0.1914 0.2716 -0.0156 0.0064  -0.0297 241 TYR A CD2 
2046 C CE1 . TYR A 241 ? 0.2045 0.1345 0.2204 -0.0126 0.0029  -0.0403 241 TYR A CE1 
2047 C CE2 . TYR A 241 ? 0.2069 0.1506 0.2250 -0.0147 0.0054  -0.0335 241 TYR A CE2 
2048 C CZ  . TYR A 241 ? 0.2366 0.1761 0.2523 -0.0135 0.0036  -0.0385 241 TYR A CZ  
2049 O OH  . TYR A 241 ? 0.2168 0.1615 0.2301 -0.0128 0.0023  -0.0419 241 TYR A OH  
2050 N N   . PHE A 242 ? 0.2102 0.1091 0.2359 -0.0206 -0.0006 -0.0262 242 PHE A N   
2051 C CA  . PHE A 242 ? 0.2012 0.0879 0.2285 -0.0217 -0.0042 -0.0310 242 PHE A CA  
2052 C C   . PHE A 242 ? 0.2276 0.1109 0.2583 -0.0307 -0.0062 -0.0279 242 PHE A C   
2053 O O   . PHE A 242 ? 0.2512 0.1312 0.2831 -0.0339 -0.0087 -0.0331 242 PHE A O   
2054 C CB  . PHE A 242 ? 0.2188 0.0927 0.2471 -0.0164 -0.0061 -0.0310 242 PHE A CB  
2055 C CG  . PHE A 242 ? 0.2581 0.1175 0.2884 -0.0166 -0.0102 -0.0371 242 PHE A CG  
2056 C CD1 . PHE A 242 ? 0.3111 0.1699 0.3393 -0.0108 -0.0106 -0.0471 242 PHE A CD1 
2057 C CD2 . PHE A 242 ? 0.2459 0.0924 0.2801 -0.0228 -0.0139 -0.0330 242 PHE A CD2 
2058 C CE1 . PHE A 242 ? 0.2950 0.1402 0.3249 -0.0106 -0.0147 -0.0542 242 PHE A CE1 
2059 C CE2 . PHE A 242 ? 0.2530 0.0858 0.2883 -0.0230 -0.0179 -0.0388 242 PHE A CE2 
2060 C CZ  . PHE A 242 ? 0.2960 0.1295 0.3280 -0.0166 -0.0178 -0.0493 242 PHE A CZ  
2061 N N   . GLU A 243 ? 0.2260 0.1109 0.2582 -0.0353 -0.0055 -0.0194 243 GLU A N   
2062 C CA  . GLU A 243 ? 0.2087 0.0928 0.2444 -0.0448 -0.0069 -0.0154 243 GLU A CA  
2063 C C   . GLU A 243 ? 0.2088 0.1055 0.2457 -0.0485 -0.0059 -0.0196 243 GLU A C   
2064 O O   . GLU A 243 ? 0.2283 0.1219 0.2682 -0.0545 -0.0085 -0.0218 243 GLU A O   
2065 C CB  . GLU A 243 ? 0.2112 0.1003 0.2471 -0.0492 -0.0052 -0.0053 243 GLU A CB  
2066 C CG  . GLU A 243 ? 0.2833 0.1755 0.3229 -0.0601 -0.0061 -0.0008 243 GLU A CG  
2067 C CD  . GLU A 243 ? 0.2953 0.1997 0.3343 -0.0651 -0.0031 0.0079  243 GLU A CD  
2068 O OE1 . GLU A 243 ? 0.3597 0.2664 0.4016 -0.0745 -0.0038 0.0130  243 GLU A OE1 
2069 O OE2 . GLU A 243 ? 0.3041 0.2164 0.3398 -0.0603 -0.0002 0.0095  243 GLU A OE2 
2070 N N   . ILE A 244 ? 0.2217 0.1321 0.2566 -0.0448 -0.0026 -0.0209 244 ILE A N   
2071 C CA  . ILE A 244 ? 0.2405 0.1643 0.2776 -0.0479 -0.0017 -0.0234 244 ILE A CA  
2072 C C   . ILE A 244 ? 0.2486 0.1716 0.2846 -0.0451 -0.0039 -0.0314 244 ILE A C   
2073 O O   . ILE A 244 ? 0.2246 0.1530 0.2637 -0.0497 -0.0056 -0.0341 244 ILE A O   
2074 C CB  . ILE A 244 ? 0.2165 0.1540 0.2526 -0.0450 0.0021  -0.0214 244 ILE A CB  
2075 C CG1 . ILE A 244 ? 0.2634 0.2041 0.2999 -0.0484 0.0042  -0.0140 244 ILE A CG1 
2076 C CG2 . ILE A 244 ? 0.2638 0.2147 0.3031 -0.0465 0.0024  -0.0248 244 ILE A CG2 
2077 C CD1 . ILE A 244 ? 0.2027 0.1460 0.2433 -0.0578 0.0036  -0.0099 244 ILE A CD1 
2078 N N   . PHE A 245 ? 0.2114 0.1291 0.2429 -0.0380 -0.0039 -0.0351 245 PHE A N   
2079 C CA  . PHE A 245 ? 0.2250 0.1452 0.2539 -0.0347 -0.0054 -0.0423 245 PHE A CA  
2080 C C   . PHE A 245 ? 0.2942 0.2022 0.3207 -0.0321 -0.0080 -0.0484 245 PHE A C   
2081 O O   . PHE A 245 ? 0.2946 0.2053 0.3185 -0.0306 -0.0096 -0.0550 245 PHE A O   
2082 C CB  . PHE A 245 ? 0.2276 0.1568 0.2528 -0.0286 -0.0028 -0.0421 245 PHE A CB  
2083 C CG  . PHE A 245 ? 0.2233 0.1640 0.2511 -0.0301 -0.0009 -0.0382 245 PHE A CG  
2084 C CD1 . PHE A 245 ? 0.2549 0.2044 0.2858 -0.0332 -0.0023 -0.0399 245 PHE A CD1 
2085 C CD2 . PHE A 245 ? 0.2521 0.1954 0.2798 -0.0283 0.0020  -0.0334 245 PHE A CD2 
2086 C CE1 . PHE A 245 ? 0.2156 0.1760 0.2499 -0.0337 -0.0006 -0.0373 245 PHE A CE1 
2087 C CE2 . PHE A 245 ? 0.2276 0.1814 0.2580 -0.0293 0.0037  -0.0312 245 PHE A CE2 
2088 C CZ  . PHE A 245 ? 0.2919 0.2541 0.3259 -0.0316 0.0024  -0.0334 245 PHE A CZ  
2089 N N   . GLY A 246 ? 0.2008 0.0960 0.2283 -0.0313 -0.0088 -0.0469 246 GLY A N   
2090 C CA  . GLY A 246 ? 0.2284 0.1107 0.2555 -0.0296 -0.0122 -0.0539 246 GLY A CA  
2091 C C   . GLY A 246 ? 0.2718 0.1534 0.2944 -0.0206 -0.0111 -0.0598 246 GLY A C   
2092 O O   . GLY A 246 ? 0.2944 0.1680 0.3160 -0.0183 -0.0137 -0.0680 246 GLY A O   
2093 N N   . GLU A 247 ? 0.2701 0.1605 0.2902 -0.0157 -0.0074 -0.0563 247 GLU A N   
2094 C CA  . GLU A 247 ? 0.3085 0.2003 0.3250 -0.0077 -0.0058 -0.0607 247 GLU A CA  
2095 C C   . GLU A 247 ? 0.2683 0.1649 0.2854 -0.0047 -0.0026 -0.0534 247 GLU A C   
2096 O O   . GLU A 247 ? 0.2603 0.1614 0.2789 -0.0087 -0.0014 -0.0464 247 GLU A O   
2097 C CB  . GLU A 247 ? 0.3412 0.2448 0.3523 -0.0057 -0.0049 -0.0662 247 GLU A CB  
2098 C CG  . GLU A 247 ? 0.3614 0.2781 0.3711 -0.0076 -0.0026 -0.0604 247 GLU A CG  
2099 C CD  . GLU A 247 ? 0.4683 0.3953 0.4731 -0.0074 -0.0032 -0.0645 247 GLU A CD  
2100 O OE1 . GLU A 247 ? 0.5706 0.5074 0.5721 -0.0050 -0.0009 -0.0616 247 GLU A OE1 
2101 O OE2 . GLU A 247 ? 0.5712 0.4964 0.5753 -0.0100 -0.0062 -0.0702 247 GLU A OE2 
2102 N N   . HIS A 248 ? 0.2874 0.1839 0.3035 0.0023  -0.0013 -0.0556 248 HIS A N   
2103 C CA  . HIS A 248 ? 0.2717 0.1755 0.2879 0.0049  0.0017  -0.0494 248 HIS A CA  
2104 C C   . HIS A 248 ? 0.2442 0.1623 0.2566 0.0044  0.0044  -0.0486 248 HIS A C   
2105 O O   . HIS A 248 ? 0.2985 0.2216 0.3070 0.0058  0.0045  -0.0541 248 HIS A O   
2106 C CB  . HIS A 248 ? 0.3448 0.2460 0.3623 0.0125  0.0022  -0.0518 248 HIS A CB  
2107 C CG  . HIS A 248 ? 0.5788 0.4653 0.6011 0.0133  -0.0010 -0.0500 248 HIS A CG  
2108 N ND1 . HIS A 248 ? 0.6066 0.4900 0.6316 0.0103  -0.0015 -0.0409 248 HIS A ND1 
2109 C CD2 . HIS A 248 ? 0.6530 0.5264 0.6780 0.0165  -0.0042 -0.0559 248 HIS A CD2 
2110 C CE1 . HIS A 248 ? 0.6685 0.5375 0.6975 0.0114  -0.0050 -0.0400 248 HIS A CE1 
2111 N NE2 . HIS A 248 ? 0.6864 0.5480 0.7159 0.0154  -0.0069 -0.0493 248 HIS A NE2 
2112 N N   . PRO A 249 ? 0.2192 0.1434 0.2322 0.0023  0.0061  -0.0419 249 PRO A N   
2113 C CA  . PRO A 249 ? 0.2568 0.1921 0.2669 0.0015  0.0078  -0.0407 249 PRO A CA  
2114 C C   . PRO A 249 ? 0.2432 0.1858 0.2504 0.0064  0.0099  -0.0424 249 PRO A C   
2115 O O   . PRO A 249 ? 0.3589 0.3020 0.3679 0.0098  0.0112  -0.0409 249 PRO A O   
2116 C CB  . PRO A 249 ? 0.2318 0.1699 0.2443 -0.0013 0.0089  -0.0340 249 PRO A CB  
2117 C CG  . PRO A 249 ? 0.2295 0.1614 0.2447 -0.0001 0.0088  -0.0311 249 PRO A CG  
2118 C CD  . PRO A 249 ? 0.2425 0.1637 0.2587 0.0007  0.0064  -0.0352 249 PRO A CD  
2119 N N   . VAL A 250 ? 0.1973 0.1468 0.2003 0.0064  0.0100  -0.0452 250 VAL A N   
2120 C CA  . VAL A 250 ? 0.2756 0.2350 0.2754 0.0097  0.0124  -0.0456 250 VAL A CA  
2121 C C   . VAL A 250 ? 0.2393 0.2064 0.2382 0.0071  0.0134  -0.0392 250 VAL A C   
2122 O O   . VAL A 250 ? 0.2416 0.2172 0.2388 0.0086  0.0155  -0.0376 250 VAL A O   
2123 C CB  . VAL A 250 ? 0.3988 0.3628 0.3934 0.0116  0.0121  -0.0525 250 VAL A CB  
2124 C CG1 . VAL A 250 ? 0.4728 0.4284 0.4689 0.0153  0.0111  -0.0601 250 VAL A CG1 
2125 C CG2 . VAL A 250 ? 0.3075 0.2728 0.2991 0.0075  0.0097  -0.0527 250 VAL A CG2 
2126 N N   . TYR A 251 ? 0.2009 0.1655 0.2017 0.0033  0.0120  -0.0356 251 TYR A N   
2127 C CA  . TYR A 251 ? 0.1985 0.1677 0.1999 0.0014  0.0124  -0.0301 251 TYR A CA  
2128 C C   . TYR A 251 ? 0.1645 0.1296 0.1706 -0.0001 0.0125  -0.0270 251 TYR A C   
2129 O O   . TYR A 251 ? 0.2004 0.1600 0.2088 -0.0013 0.0116  -0.0281 251 TYR A O   
2130 C CB  . TYR A 251 ? 0.2681 0.2395 0.2679 -0.0010 0.0101  -0.0292 251 TYR A CB  
2131 C CG  . TYR A 251 ? 0.3359 0.3102 0.3309 -0.0003 0.0089  -0.0334 251 TYR A CG  
2132 C CD1 . TYR A 251 ? 0.3834 0.3651 0.3733 0.0013  0.0103  -0.0340 251 TYR A CD1 
2133 C CD2 . TYR A 251 ? 0.4220 0.3929 0.4174 -0.0017 0.0065  -0.0373 251 TYR A CD2 
2134 C CE1 . TYR A 251 ? 0.3990 0.3849 0.3837 0.0020  0.0094  -0.0385 251 TYR A CE1 
2135 C CE2 . TYR A 251 ? 0.3187 0.2928 0.3092 -0.0012 0.0051  -0.0419 251 TYR A CE2 
2136 C CZ  . TYR A 251 ? 0.4078 0.3895 0.3925 0.0008  0.0066  -0.0428 251 TYR A CZ  
2137 O OH  . TYR A 251 ? 0.4926 0.4793 0.4714 0.0014  0.0055  -0.0481 251 TYR A OH  
2138 N N   . MET A 252 ? 0.1719 0.1405 0.1791 -0.0003 0.0136  -0.0231 252 MET A N   
2139 C CA  . MET A 252 ? 0.2145 0.1811 0.2252 -0.0019 0.0137  -0.0206 252 MET A CA  
2140 C C   . MET A 252 ? 0.2388 0.2086 0.2502 -0.0037 0.0133  -0.0176 252 MET A C   
2141 O O   . MET A 252 ? 0.1994 0.1734 0.2093 -0.0036 0.0136  -0.0157 252 MET A O   
2142 C CB  . MET A 252 ? 0.2864 0.2527 0.2986 -0.0002 0.0149  -0.0196 252 MET A CB  
2143 C CG  . MET A 252 ? 0.3094 0.2691 0.3226 0.0007  0.0144  -0.0212 252 MET A CG  
2144 S SD  . MET A 252 ? 0.2692 0.2283 0.2850 0.0020  0.0147  -0.0178 252 MET A SD  
2145 C CE  . MET A 252 ? 0.2947 0.2435 0.3115 0.0021  0.0130  -0.0190 252 MET A CE  
2146 N N   . TRP A 253 ? 0.1735 0.1416 0.1877 -0.0054 0.0125  -0.0173 253 TRP A N   
2147 C CA  . TRP A 253 ? 0.1137 0.0830 0.1297 -0.0067 0.0117  -0.0155 253 TRP A CA  
2148 C C   . TRP A 253 ? 0.1661 0.1370 0.1834 -0.0072 0.0128  -0.0143 253 TRP A C   
2149 O O   . TRP A 253 ? 0.1841 0.1544 0.2023 -0.0075 0.0133  -0.0152 253 TRP A O   
2150 C CB  . TRP A 253 ? 0.1129 0.0808 0.1316 -0.0073 0.0100  -0.0172 253 TRP A CB  
2151 C CG  . TRP A 253 ? 0.1635 0.1311 0.1850 -0.0081 0.0089  -0.0167 253 TRP A CG  
2152 C CD1 . TRP A 253 ? 0.1641 0.1327 0.1882 -0.0086 0.0093  -0.0189 253 TRP A CD1 
2153 C CD2 . TRP A 253 ? 0.1765 0.1427 0.1983 -0.0087 0.0071  -0.0142 253 TRP A CD2 
2154 N NE1 . TRP A 253 ? 0.1860 0.1530 0.2123 -0.0090 0.0076  -0.0190 253 TRP A NE1 
2155 C CE2 . TRP A 253 ? 0.1969 0.1615 0.2222 -0.0093 0.0059  -0.0157 253 TRP A CE2 
2156 C CE3 . TRP A 253 ? 0.1806 0.1471 0.1999 -0.0092 0.0061  -0.0106 253 TRP A CE3 
2157 C CZ2 . TRP A 253 ? 0.2137 0.1749 0.2408 -0.0105 0.0034  -0.0137 253 TRP A CZ2 
2158 C CZ3 . TRP A 253 ? 0.1649 0.1291 0.1856 -0.0109 0.0038  -0.0074 253 TRP A CZ3 
2159 C CH2 . TRP A 253 ? 0.1893 0.1497 0.2142 -0.0115 0.0022  -0.0089 253 TRP A CH2 
2160 N N   . PRO A 254 ? 0.1660 0.1398 0.1834 -0.0078 0.0130  -0.0120 254 PRO A N   
2161 C CA  . PRO A 254 ? 0.2149 0.1912 0.2338 -0.0086 0.0135  -0.0112 254 PRO A CA  
2162 C C   . PRO A 254 ? 0.1576 0.1326 0.1785 -0.0104 0.0122  -0.0127 254 PRO A C   
2163 O O   . PRO A 254 ? 0.1664 0.1391 0.1887 -0.0114 0.0105  -0.0129 254 PRO A O   
2164 C CB  . PRO A 254 ? 0.1892 0.1703 0.2083 -0.0094 0.0138  -0.0084 254 PRO A CB  
2165 C CG  . PRO A 254 ? 0.2626 0.2422 0.2804 -0.0104 0.0127  -0.0072 254 PRO A CG  
2166 C CD  . PRO A 254 ? 0.1916 0.1676 0.2076 -0.0084 0.0126  -0.0096 254 PRO A CD  
2167 N N   . PRO A 255 ? 0.1568 0.1333 0.1780 -0.0107 0.0127  -0.0139 255 PRO A N   
2168 C CA  . PRO A 255 ? 0.1834 0.1603 0.2062 -0.0121 0.0118  -0.0168 255 PRO A CA  
2169 C C   . PRO A 255 ? 0.1795 0.1557 0.2042 -0.0137 0.0100  -0.0171 255 PRO A C   
2170 O O   . PRO A 255 ? 0.1828 0.1616 0.2075 -0.0150 0.0099  -0.0147 255 PRO A O   
2171 C CB  . PRO A 255 ? 0.1570 0.1382 0.1784 -0.0127 0.0129  -0.0167 255 PRO A CB  
2172 C CG  . PRO A 255 ? 0.1161 0.0959 0.1360 -0.0114 0.0140  -0.0142 255 PRO A CG  
2173 C CD  . PRO A 255 ? 0.1524 0.1301 0.1722 -0.0098 0.0139  -0.0127 255 PRO A CD  
2174 N N   . GLN A 256 ? 0.1780 0.1506 0.2050 -0.0136 0.0082  -0.0201 256 GLN A N   
2175 C CA  . GLN A 256 ? 0.2037 0.1728 0.2334 -0.0153 0.0055  -0.0208 256 GLN A CA  
2176 C C   . GLN A 256 ? 0.1808 0.1478 0.2103 -0.0169 0.0046  -0.0155 256 GLN A C   
2177 O O   . GLN A 256 ? 0.1714 0.1370 0.2028 -0.0198 0.0027  -0.0140 256 GLN A O   
2178 C CB  . GLN A 256 ? 0.1808 0.1537 0.2107 -0.0174 0.0052  -0.0231 256 GLN A CB  
2179 C CG  . GLN A 256 ? 0.2110 0.1892 0.2395 -0.0165 0.0068  -0.0275 256 GLN A CG  
2180 C CD  . GLN A 256 ? 0.2828 0.2590 0.3142 -0.0146 0.0058  -0.0336 256 GLN A CD  
2181 O OE1 . GLN A 256 ? 0.2906 0.2599 0.3255 -0.0138 0.0032  -0.0350 256 GLN A OE1 
2182 N NE2 . GLN A 256 ? 0.2173 0.2000 0.2474 -0.0139 0.0078  -0.0371 256 GLN A NE2 
2183 N N   . ALA A 257 ? 0.1407 0.1084 0.1680 -0.0155 0.0058  -0.0126 257 ALA A N   
2184 C CA  . ALA A 257 ? 0.1654 0.1342 0.1913 -0.0170 0.0058  -0.0076 257 ALA A CA  
2185 C C   . ALA A 257 ? 0.1973 0.1728 0.2230 -0.0189 0.0073  -0.0052 257 ALA A C   
2186 O O   . ALA A 257 ? 0.1917 0.1702 0.2173 -0.0213 0.0073  -0.0011 257 ALA A O   
2187 C CB  . ALA A 257 ? 0.1555 0.1182 0.1834 -0.0191 0.0023  -0.0050 257 ALA A CB  
2188 N N   . SER A 258 ? 0.1671 0.1462 0.1929 -0.0180 0.0086  -0.0074 258 SER A N   
2189 C CA  . SER A 258 ? 0.1480 0.1340 0.1751 -0.0199 0.0091  -0.0057 258 SER A CA  
2190 C C   . SER A 258 ? 0.1847 0.1775 0.2106 -0.0179 0.0116  -0.0030 258 SER A C   
2191 O O   . SER A 258 ? 0.1932 0.1860 0.2174 -0.0141 0.0132  -0.0043 258 SER A O   
2192 C CB  . SER A 258 ? 0.2077 0.1960 0.2350 -0.0195 0.0090  -0.0085 258 SER A CB  
2193 O OG  . SER A 258 ? 0.2508 0.2457 0.2800 -0.0220 0.0084  -0.0069 258 SER A OG  
2194 N N   . VAL A 259 ? 0.1831 0.1821 0.2105 -0.0205 0.0118  0.0003  259 VAL A N   
2195 C CA  . VAL A 259 ? 0.1598 0.1680 0.1870 -0.0184 0.0144  0.0021  259 VAL A CA  
2196 C C   . VAL A 259 ? 0.1883 0.2066 0.2194 -0.0212 0.0143  0.0044  259 VAL A C   
2197 O O   . VAL A 259 ? 0.2000 0.2171 0.2335 -0.0258 0.0120  0.0051  259 VAL A O   
2198 C CB  . VAL A 259 ? 0.2381 0.2473 0.2627 -0.0188 0.0154  0.0043  259 VAL A CB  
2199 C CG1 . VAL A 259 ? 0.2145 0.2163 0.2355 -0.0152 0.0155  0.0014  259 VAL A CG1 
2200 C CG2 . VAL A 259 ? 0.3120 0.3182 0.3374 -0.0246 0.0130  0.0081  259 VAL A CG2 
2201 N N   . SER A 260 ? 0.1942 0.2229 0.2265 -0.0182 0.0168  0.0051  260 SER A N   
2202 C CA  . SER A 260 ? 0.1548 0.1969 0.1917 -0.0200 0.0174  0.0073  260 SER A CA  
2203 C C   . SER A 260 ? 0.1481 0.2001 0.1852 -0.0150 0.0207  0.0068  260 SER A C   
2204 O O   . SER A 260 ? 0.1437 0.1903 0.1774 -0.0101 0.0219  0.0040  260 SER A O   
2205 C CB  . SER A 260 ? 0.2125 0.2571 0.2525 -0.0191 0.0156  0.0063  260 SER A CB  
2206 O OG  . SER A 260 ? 0.1892 0.2326 0.2283 -0.0122 0.0166  0.0041  260 SER A OG  
2207 N N   . ASN A 261 ? 0.1642 0.2316 0.2056 -0.0163 0.0222  0.0089  261 ASN A N   
2208 C CA  . ASN A 261 ? 0.1459 0.2248 0.1882 -0.0106 0.0256  0.0071  261 ASN A CA  
2209 C C   . ASN A 261 ? 0.1548 0.2289 0.1978 -0.0021 0.0254  0.0028  261 ASN A C   
2210 O O   . ASN A 261 ? 0.1791 0.2511 0.2197 0.0036  0.0271  -0.0008 261 ASN A O   
2211 C CB  . ASN A 261 ? 0.1499 0.2486 0.1985 -0.0129 0.0272  0.0097  261 ASN A CB  
2212 C CG  . ASN A 261 ? 0.2064 0.3111 0.2541 -0.0216 0.0279  0.0148  261 ASN A CG  
2213 O OD1 . ASN A 261 ? 0.2128 0.3105 0.2548 -0.0236 0.0283  0.0160  261 ASN A OD1 
2214 N ND2 . ASN A 261 ? 0.2386 0.3563 0.2921 -0.0271 0.0276  0.0184  261 ASN A ND2 
2215 N N   . GLU A 262 ? 0.1591 0.2311 0.2052 -0.0015 0.0229  0.0033  262 GLU A N   
2216 C CA  . GLU A 262 ? 0.1840 0.2511 0.2310 0.0060  0.0220  0.0008  262 GLU A CA  
2217 C C   . GLU A 262 ? 0.2408 0.2909 0.2820 0.0074  0.0213  -0.0014 262 GLU A C   
2218 O O   . GLU A 262 ? 0.2129 0.2582 0.2536 0.0135  0.0218  -0.0043 262 GLU A O   
2219 C CB  . GLU A 262 ? 0.1614 0.2315 0.2123 0.0057  0.0190  0.0030  262 GLU A CB  
2220 C CG  . GLU A 262 ? 0.2223 0.3110 0.2802 0.0050  0.0193  0.0048  262 GLU A CG  
2221 C CD  . GLU A 262 ? 0.3201 0.4130 0.3820 0.0063  0.0160  0.0066  262 GLU A CD  
2222 O OE1 . GLU A 262 ? 0.3716 0.4538 0.4309 0.0095  0.0138  0.0066  262 GLU A OE1 
2223 O OE2 . GLU A 262 ? 0.3108 0.4184 0.3783 0.0036  0.0153  0.0085  262 GLU A OE2 
2224 N N   . ALA A 263 ? 0.1529 0.1939 0.1902 0.0017  0.0201  -0.0004 263 ALA A N   
2225 C CA  . ALA A 263 ? 0.1829 0.2101 0.2156 0.0026  0.0196  -0.0024 263 ALA A CA  
2226 C C   . ALA A 263 ? 0.1583 0.1841 0.1880 0.0050  0.0216  -0.0050 263 ALA A C   
2227 O O   . ALA A 263 ? 0.1830 0.2008 0.2109 0.0087  0.0215  -0.0079 263 ALA A O   
2228 C CB  . ALA A 263 ? 0.1666 0.1865 0.1968 -0.0032 0.0179  -0.0015 263 ALA A CB  
2229 N N   . LEU A 264 ? 0.1497 0.1837 0.1787 0.0024  0.0233  -0.0039 264 LEU A N   
2230 C CA  . LEU A 264 ? 0.1835 0.2187 0.2089 0.0045  0.0253  -0.0066 264 LEU A CA  
2231 C C   . LEU A 264 ? 0.1974 0.2373 0.2248 0.0120  0.0269  -0.0110 264 LEU A C   
2232 O O   . LEU A 264 ? 0.2321 0.2664 0.2564 0.0156  0.0273  -0.0154 264 LEU A O   
2233 C CB  . LEU A 264 ? 0.1745 0.2198 0.1986 -0.0003 0.0267  -0.0033 264 LEU A CB  
2234 C CG  . LEU A 264 ? 0.2173 0.2547 0.2392 -0.0070 0.0244  0.0007  264 LEU A CG  
2235 C CD1 . LEU A 264 ? 0.2162 0.2634 0.2382 -0.0130 0.0250  0.0059  264 LEU A CD1 
2236 C CD2 . LEU A 264 ? 0.2895 0.3161 0.3064 -0.0061 0.0233  -0.0014 264 LEU A CD2 
2237 N N   . GLU A 265 ? 0.1808 0.2306 0.2139 0.0148  0.0274  -0.0104 265 GLU A N   
2238 C CA  . GLU A 265 ? 0.2324 0.2854 0.2688 0.0231  0.0282  -0.0150 265 GLU A CA  
2239 C C   . GLU A 265 ? 0.1899 0.2265 0.2258 0.0270  0.0255  -0.0171 265 GLU A C   
2240 O O   . GLU A 265 ? 0.1907 0.2226 0.2262 0.0326  0.0257  -0.0224 265 GLU A O   
2241 C CB  . GLU A 265 ? 0.2494 0.3169 0.2932 0.0255  0.0286  -0.0134 265 GLU A CB  
2242 C CG  . GLU A 265 ? 0.4106 0.4805 0.4597 0.0354  0.0285  -0.0180 265 GLU A CG  
2243 C CD  . GLU A 265 ? 0.5556 0.6378 0.6051 0.0405  0.0322  -0.0240 265 GLU A CD  
2244 O OE1 . GLU A 265 ? 0.5847 0.6623 0.6360 0.0488  0.0319  -0.0302 265 GLU A OE1 
2245 O OE2 . GLU A 265 ? 0.6364 0.7329 0.6843 0.0360  0.0354  -0.0226 265 GLU A OE2 
2246 N N   . LEU A 266 ? 0.1889 0.2170 0.2248 0.0236  0.0228  -0.0132 266 LEU A N   
2247 C CA  . LEU A 266 ? 0.1663 0.1799 0.2015 0.0258  0.0203  -0.0138 266 LEU A CA  
2248 C C   . LEU A 266 ? 0.1939 0.1967 0.2240 0.0247  0.0205  -0.0172 266 LEU A C   
2249 O O   . LEU A 266 ? 0.1993 0.1935 0.2296 0.0288  0.0194  -0.0207 266 LEU A O   
2250 C CB  . LEU A 266 ? 0.1857 0.1951 0.2207 0.0214  0.0180  -0.0088 266 LEU A CB  
2251 C CG  . LEU A 266 ? 0.1802 0.1758 0.2137 0.0217  0.0155  -0.0078 266 LEU A CG  
2252 C CD1 . LEU A 266 ? 0.2249 0.2170 0.2627 0.0287  0.0136  -0.0081 266 LEU A CD1 
2253 C CD2 . LEU A 266 ? 0.1710 0.1660 0.2030 0.0163  0.0140  -0.0033 266 LEU A CD2 
2254 N N   . TYR A 267 ? 0.1642 0.1674 0.1903 0.0190  0.0213  -0.0162 267 TYR A N   
2255 C CA  . TYR A 267 ? 0.1522 0.1474 0.1737 0.0178  0.0211  -0.0193 267 TYR A CA  
2256 C C   . TYR A 267 ? 0.2245 0.2225 0.2451 0.0229  0.0225  -0.0252 267 TYR A C   
2257 O O   . TYR A 267 ? 0.2033 0.1919 0.2224 0.0248  0.0213  -0.0294 267 TYR A O   
2258 C CB  . TYR A 267 ? 0.1370 0.1345 0.1552 0.0120  0.0215  -0.0170 267 TYR A CB  
2259 C CG  . TYR A 267 ? 0.1787 0.1705 0.1973 0.0076  0.0198  -0.0137 267 TYR A CG  
2260 C CD1 . TYR A 267 ? 0.2094 0.1914 0.2274 0.0070  0.0182  -0.0144 267 TYR A CD1 
2261 C CD2 . TYR A 267 ? 0.1588 0.1558 0.1785 0.0038  0.0196  -0.0102 267 TYR A CD2 
2262 C CE1 . TYR A 267 ? 0.2361 0.2154 0.2544 0.0032  0.0171  -0.0121 267 TYR A CE1 
2263 C CE2 . TYR A 267 ? 0.1722 0.1647 0.1923 0.0003  0.0181  -0.0086 267 TYR A CE2 
2264 C CZ  . TYR A 267 ? 0.2752 0.2598 0.2945 0.0003  0.0171  -0.0098 267 TYR A CZ  
2265 O OH  . TYR A 267 ? 0.2659 0.2484 0.2854 -0.0028 0.0160  -0.0090 267 TYR A OH  
2266 N N   . TYR A 268 ? 0.2012 0.2128 0.2229 0.0250  0.0250  -0.0261 268 TYR A N   
2267 C CA  . TYR A 268 ? 0.2001 0.2171 0.2208 0.0304  0.0268  -0.0328 268 TYR A CA  
2268 C C   . TYR A 268 ? 0.2164 0.2256 0.2414 0.0378  0.0252  -0.0375 268 TYR A C   
2269 O O   . TYR A 268 ? 0.2463 0.2485 0.2695 0.0411  0.0245  -0.0441 268 TYR A O   
2270 C CB  . TYR A 268 ? 0.1816 0.2177 0.2033 0.0309  0.0302  -0.0323 268 TYR A CB  
2271 C CG  . TYR A 268 ? 0.2749 0.3194 0.2993 0.0392  0.0321  -0.0396 268 TYR A CG  
2272 C CD1 . TYR A 268 ? 0.2999 0.3461 0.3193 0.0418  0.0335  -0.0469 268 TYR A CD1 
2273 C CD2 . TYR A 268 ? 0.1999 0.2510 0.2319 0.0448  0.0324  -0.0400 268 TYR A CD2 
2274 C CE1 . TYR A 268 ? 0.3458 0.4000 0.3679 0.0501  0.0353  -0.0553 268 TYR A CE1 
2275 C CE2 . TYR A 268 ? 0.2387 0.2976 0.2742 0.0535  0.0340  -0.0477 268 TYR A CE2 
2276 C CZ  . TYR A 268 ? 0.3077 0.3680 0.3383 0.0563  0.0356  -0.0558 268 TYR A CZ  
2277 O OH  . TYR A 268 ? 0.3389 0.4078 0.3733 0.0657  0.0373  -0.0649 268 TYR A OH  
2278 N N   . GLU A 269 ? 0.1863 0.1965 0.2174 0.0404  0.0241  -0.0343 269 GLU A N   
2279 C CA  . GLU A 269 ? 0.2517 0.2534 0.2878 0.0477  0.0217  -0.0374 269 GLU A CA  
2280 C C   . GLU A 269 ? 0.2392 0.2213 0.2732 0.0460  0.0184  -0.0377 269 GLU A C   
2281 O O   . GLU A 269 ? 0.2828 0.2550 0.3196 0.0516  0.0162  -0.0423 269 GLU A O   
2282 C CB  . GLU A 269 ? 0.2411 0.2470 0.2835 0.0496  0.0203  -0.0318 269 GLU A CB  
2283 C CG  . GLU A 269 ? 0.2117 0.2374 0.2586 0.0528  0.0230  -0.0324 269 GLU A CG  
2284 C CD  . GLU A 269 ? 0.4338 0.4657 0.4856 0.0515  0.0214  -0.0254 269 GLU A CD  
2285 O OE1 . GLU A 269 ? 0.4616 0.4823 0.5125 0.0483  0.0183  -0.0204 269 GLU A OE1 
2286 O OE2 . GLU A 269 ? 0.4518 0.5011 0.5083 0.0532  0.0234  -0.0251 269 GLU A OE2 
2287 N N   . LYS A 270 ? 0.2101 0.1865 0.2400 0.0384  0.0177  -0.0332 270 LYS A N   
2288 C CA  . LYS A 270 ? 0.2571 0.2176 0.2856 0.0357  0.0149  -0.0329 270 LYS A CA  
2289 C C   . LYS A 270 ? 0.2300 0.1868 0.2537 0.0338  0.0153  -0.0386 270 LYS A C   
2290 O O   . LYS A 270 ? 0.2593 0.2049 0.2816 0.0300  0.0131  -0.0384 270 LYS A O   
2291 C CB  . LYS A 270 ? 0.2070 0.1649 0.2344 0.0289  0.0139  -0.0253 270 LYS A CB  
2292 C CG  . LYS A 270 ? 0.2223 0.1827 0.2538 0.0304  0.0126  -0.0194 270 LYS A CG  
2293 C CD  . LYS A 270 ? 0.3247 0.2766 0.3609 0.0370  0.0097  -0.0203 270 LYS A CD  
2294 C CE  . LYS A 270 ? 0.3203 0.2736 0.3600 0.0377  0.0074  -0.0131 270 LYS A CE  
2295 N NZ  . LYS A 270 ? 0.5039 0.4503 0.5494 0.0455  0.0041  -0.0134 270 LYS A NZ  
2296 N N   . GLY A 271 ? 0.2595 0.2269 0.2807 0.0360  0.0178  -0.0437 271 GLY A N   
2297 C CA  . GLY A 271 ? 0.2383 0.2037 0.2546 0.0350  0.0178  -0.0499 271 GLY A CA  
2298 C C   . GLY A 271 ? 0.2343 0.2032 0.2454 0.0280  0.0184  -0.0466 271 GLY A C   
2299 O O   . GLY A 271 ? 0.3265 0.2924 0.3337 0.0263  0.0174  -0.0509 271 GLY A O   
2300 N N   . ILE A 272 ? 0.2166 0.1912 0.2279 0.0240  0.0194  -0.0396 272 ILE A N   
2301 C CA  . ILE A 272 ? 0.1767 0.1541 0.1841 0.0183  0.0193  -0.0366 272 ILE A CA  
2302 C C   . ILE A 272 ? 0.2228 0.2128 0.2260 0.0188  0.0215  -0.0382 272 ILE A C   
2303 O O   . ILE A 272 ? 0.2749 0.2754 0.2794 0.0209  0.0239  -0.0373 272 ILE A O   
2304 C CB  . ILE A 272 ? 0.1721 0.1504 0.1816 0.0142  0.0192  -0.0295 272 ILE A CB  
2305 C CG1 . ILE A 272 ? 0.2577 0.2262 0.2705 0.0133  0.0174  -0.0273 272 ILE A CG1 
2306 C CG2 . ILE A 272 ? 0.2289 0.2098 0.2351 0.0093  0.0188  -0.0268 272 ILE A CG2 
2307 C CD1 . ILE A 272 ? 0.3252 0.2835 0.3374 0.0120  0.0154  -0.0300 272 ILE A CD1 
2308 N N   . ASN A 273 ? 0.2205 0.2109 0.2186 0.0165  0.0207  -0.0402 273 ASN A N   
2309 C CA  . ASN A 273 ? 0.2169 0.2201 0.2097 0.0165  0.0226  -0.0412 273 ASN A CA  
2310 C C   . ASN A 273 ? 0.1837 0.1925 0.1744 0.0111  0.0224  -0.0335 273 ASN A C   
2311 O O   . ASN A 273 ? 0.2157 0.2368 0.2028 0.0102  0.0243  -0.0316 273 ASN A O   
2312 C CB  . ASN A 273 ? 0.2914 0.2936 0.2789 0.0174  0.0213  -0.0482 273 ASN A CB  
2313 C CG  . ASN A 273 ? 0.5109 0.5086 0.5002 0.0234  0.0214  -0.0572 273 ASN A CG  
2314 O OD1 . ASN A 273 ? 0.5408 0.5423 0.5338 0.0281  0.0235  -0.0590 273 ASN A OD1 
2315 N ND2 . ASN A 273 ? 0.5741 0.5634 0.5614 0.0232  0.0187  -0.0632 273 ASN A ND2 
2316 N N   A MET A 274 ? 0.2293 0.2297 0.2222 0.0075  0.0201  -0.0291 274 MET A N   
2317 N N   B MET A 274 ? 0.2259 0.2263 0.2188 0.0075  0.0201  -0.0290 274 MET A N   
2318 C CA  A MET A 274 ? 0.2142 0.2172 0.2060 0.0029  0.0190  -0.0223 274 MET A CA  
2319 C CA  B MET A 274 ? 0.2144 0.2175 0.2062 0.0029  0.0190  -0.0223 274 MET A CA  
2320 C C   A MET A 274 ? 0.2418 0.2363 0.2387 0.0008  0.0173  -0.0189 274 MET A C   
2321 C C   B MET A 274 ? 0.2388 0.2332 0.2355 0.0007  0.0173  -0.0189 274 MET A C   
2322 O O   A MET A 274 ? 0.2261 0.2123 0.2254 0.0015  0.0163  -0.0215 274 MET A O   
2323 O O   B MET A 274 ? 0.2302 0.2165 0.2294 0.0014  0.0161  -0.0215 274 MET A O   
2324 C CB  A MET A 274 ? 0.2392 0.2426 0.2258 0.0010  0.0166  -0.0224 274 MET A CB  
2325 C CB  B MET A 274 ? 0.2422 0.2460 0.2287 0.0011  0.0167  -0.0226 274 MET A CB  
2326 C CG  A MET A 274 ? 0.2581 0.2641 0.2437 -0.0032 0.0149  -0.0147 274 MET A CG  
2327 C CG  B MET A 274 ? 0.2663 0.2732 0.2514 -0.0030 0.0151  -0.0149 274 MET A CG  
2328 S SD  A MET A 274 ? 0.2810 0.2756 0.2720 -0.0052 0.0112  -0.0116 274 MET A SD  
2329 S SD  B MET A 274 ? 0.2804 0.2881 0.2600 -0.0047 0.0113  -0.0140 274 MET A SD  
2330 C CE  A MET A 274 ? 0.2746 0.2681 0.2620 -0.0051 0.0078  -0.0143 274 MET A CE  
2331 C CE  B MET A 274 ? 0.2638 0.2592 0.2493 -0.0045 0.0081  -0.0159 274 MET A CE  
2332 N N   . LEU A 275 ? 0.2243 0.2212 0.2226 -0.0023 0.0171  -0.0132 275 LEU A N   
2333 C CA  . LEU A 275 ? 0.1919 0.1817 0.1943 -0.0045 0.0152  -0.0107 275 LEU A CA  
2334 C C   . LEU A 275 ? 0.2185 0.2093 0.2204 -0.0081 0.0132  -0.0052 275 LEU A C   
2335 O O   . LEU A 275 ? 0.2089 0.2064 0.2072 -0.0096 0.0136  -0.0021 275 LEU A O   
2336 C CB  . LEU A 275 ? 0.2340 0.2238 0.2407 -0.0039 0.0166  -0.0105 275 LEU A CB  
2337 C CG  . LEU A 275 ? 0.2981 0.2971 0.3056 -0.0043 0.0186  -0.0078 275 LEU A CG  
2338 C CD1 . LEU A 275 ? 0.2471 0.2467 0.2560 -0.0090 0.0172  -0.0026 275 LEU A CD1 
2339 C CD2 . LEU A 275 ? 0.3737 0.3733 0.3849 -0.0018 0.0198  -0.0093 275 LEU A CD2 
2340 N N   . ALA A 276 ? 0.1641 0.1482 0.1698 -0.0096 0.0110  -0.0039 276 ALA A N   
2341 C CA  . ALA A 276 ? 0.2068 0.1894 0.2135 -0.0129 0.0085  0.0014  276 ALA A CA  
2342 C C   . ALA A 276 ? 0.1891 0.1690 0.2006 -0.0146 0.0083  0.0021  276 ALA A C   
2343 O O   . ALA A 276 ? 0.2145 0.1931 0.2283 -0.0131 0.0095  -0.0015 276 ALA A O   
2344 C CB  . ALA A 276 ? 0.2032 0.1796 0.2106 -0.0125 0.0047  0.0016  276 ALA A CB  
2345 N N   . THR A 277 ? 0.1929 0.1723 0.2056 -0.0184 0.0064  0.0072  277 THR A N   
2346 C CA  . THR A 277 ? 0.1779 0.1537 0.1953 -0.0206 0.0053  0.0072  277 THR A CA  
2347 C C   . THR A 277 ? 0.2080 0.1772 0.2274 -0.0240 0.0011  0.0118  277 THR A C   
2348 O O   . THR A 277 ? 0.2252 0.1919 0.2427 -0.0237 -0.0011 0.0147  277 THR A O   
2349 C CB  . THR A 277 ? 0.1836 0.1678 0.2018 -0.0222 0.0081  0.0081  277 THR A CB  
2350 O OG1 . THR A 277 ? 0.1911 0.1722 0.2137 -0.0248 0.0065  0.0077  277 THR A OG1 
2351 C CG2 . THR A 277 ? 0.2190 0.2120 0.2347 -0.0255 0.0093  0.0140  277 THR A CG2 
2352 N N   . ASP A 278 ? 0.2080 0.1738 0.2315 -0.0273 -0.0005 0.0126  278 ASP A N   
2353 C CA  . ASP A 278 ? 0.2636 0.2193 0.2904 -0.0298 -0.0055 0.0156  278 ASP A CA  
2354 C C   . ASP A 278 ? 0.2864 0.2442 0.3124 -0.0360 -0.0069 0.0243  278 ASP A C   
2355 O O   . ASP A 278 ? 0.2259 0.1935 0.2510 -0.0394 -0.0040 0.0268  278 ASP A O   
2356 C CB  . ASP A 278 ? 0.2796 0.2284 0.3118 -0.0300 -0.0075 0.0104  278 ASP A CB  
2357 C CG  . ASP A 278 ? 0.3716 0.3075 0.4083 -0.0308 -0.0133 0.0113  278 ASP A CG  
2358 O OD1 . ASP A 278 ? 0.3608 0.2918 0.3971 -0.0287 -0.0159 0.0139  278 ASP A OD1 
2359 O OD2 . ASP A 278 ? 0.4449 0.3751 0.4859 -0.0335 -0.0157 0.0094  278 ASP A OD2 
2360 N N   . GLU A 279 ? 0.3221 0.3279 0.3844 -0.0475 -0.0068 0.0008  279 GLU A N   
2361 C CA  . GLU A 279 ? 0.4183 0.4317 0.4967 -0.0525 -0.0049 0.0068  279 GLU A CA  
2362 C C   . GLU A 279 ? 0.3564 0.3724 0.4493 -0.0576 -0.0113 0.0041  279 GLU A C   
2363 O O   . GLU A 279 ? 0.3573 0.3851 0.4669 -0.0612 -0.0096 0.0090  279 GLU A O   
2364 C CB  . GLU A 279 ? 0.4537 0.4585 0.5317 -0.0542 -0.0013 0.0107  279 GLU A CB  
2365 C CG  . GLU A 279 ? 0.4573 0.4697 0.5485 -0.0571 0.0041  0.0196  279 GLU A CG  
2366 C CD  . GLU A 279 ? 0.4951 0.4999 0.5826 -0.0562 0.0088  0.0247  279 GLU A CD  
2367 O OE1 . GLU A 279 ? 0.3356 0.3319 0.4101 -0.0527 0.0082  0.0212  279 GLU A OE1 
2368 O OE2 . GLU A 279 ? 0.4724 0.4804 0.5710 -0.0584 0.0137  0.0329  279 GLU A OE2 
2369 N N   . VAL A 280 ? 0.3169 0.3232 0.4045 -0.0575 -0.0188 -0.0039 280 VAL A N   
2370 C CA  . VAL A 280 ? 0.3037 0.3128 0.4056 -0.0622 -0.0270 -0.0085 280 VAL A CA  
2371 C C   . VAL A 280 ? 0.2547 0.2808 0.3652 -0.0609 -0.0291 -0.0083 280 VAL A C   
2372 O O   . VAL A 280 ? 0.3049 0.3410 0.4360 -0.0663 -0.0328 -0.0082 280 VAL A O   
2373 C CB  . VAL A 280 ? 0.3368 0.3320 0.4272 -0.0601 -0.0355 -0.0184 280 VAL A CB  
2374 C CG1 . VAL A 280 ? 0.4400 0.4354 0.5123 -0.0515 -0.0377 -0.0227 280 VAL A CG1 
2375 C CG2 . VAL A 280 ? 0.3924 0.3893 0.5000 -0.0662 -0.0452 -0.0246 280 VAL A CG2 
2376 N N   . ILE A 281 ? 0.2903 0.3199 0.3867 -0.0536 -0.0268 -0.0084 281 ILE A N   
2377 C CA  . ILE A 281 ? 0.2529 0.2980 0.3560 -0.0509 -0.0283 -0.0078 281 ILE A CA  
2378 C C   . ILE A 281 ? 0.2558 0.3152 0.3749 -0.0539 -0.0209 0.0010  281 ILE A C   
2379 O O   . ILE A 281 ? 0.2333 0.3076 0.3703 -0.0560 -0.0226 0.0027  281 ILE A O   
2380 C CB  . ILE A 281 ? 0.3554 0.3976 0.4387 -0.0419 -0.0265 -0.0098 281 ILE A CB  
2381 C CG1 . ILE A 281 ? 0.5102 0.5389 0.5777 -0.0377 -0.0329 -0.0173 281 ILE A CG1 
2382 C CG2 . ILE A 281 ? 0.3325 0.3902 0.4215 -0.0378 -0.0266 -0.0082 281 ILE A CG2 
2383 C CD1 . ILE A 281 ? 0.6331 0.6506 0.6800 -0.0310 -0.0273 -0.0171 281 ILE A CD1 
2384 N N   . LEU A 282 ? 0.3033 0.3589 0.4163 -0.0534 -0.0125 0.0069  282 LEU A N   
2385 C CA  . LEU A 282 ? 0.3468 0.4144 0.4722 -0.0549 -0.0046 0.0160  282 LEU A CA  
2386 C C   . LEU A 282 ? 0.2828 0.3549 0.4324 -0.0632 -0.0056 0.0195  282 LEU A C   
2387 O O   . LEU A 282 ? 0.3096 0.3971 0.4775 -0.0650 -0.0032 0.0245  282 LEU A O   
2388 C CB  . LEU A 282 ? 0.2955 0.3567 0.4082 -0.0521 0.0028  0.0206  282 LEU A CB  
2389 C CG  . LEU A 282 ? 0.3504 0.4234 0.4713 -0.0510 0.0117  0.0305  282 LEU A CG  
2390 C CD1 . LEU A 282 ? 0.3304 0.4183 0.4530 -0.0459 0.0141  0.0320  282 LEU A CD1 
2391 C CD2 . LEU A 282 ? 0.3260 0.3931 0.4333 -0.0473 0.0175  0.0342  282 LEU A CD2 
2392 N N   . LYS A 283 ? 0.3625 0.4209 0.5137 -0.0684 -0.0086 0.0171  283 LYS A N   
2393 C CA  . LYS A 283 ? 0.3104 0.3699 0.4861 -0.0772 -0.0097 0.0195  283 LYS A CA  
2394 C C   . LYS A 283 ? 0.3190 0.3889 0.5125 -0.0810 -0.0189 0.0132  283 LYS A C   
2395 O O   . LYS A 283 ? 0.3707 0.4510 0.5910 -0.0878 -0.0178 0.0174  283 LYS A O   
2396 C CB  . LYS A 283 ? 0.4221 0.4621 0.5932 -0.0809 -0.0123 0.0159  283 LYS A CB  
2397 C CG  . LYS A 283 ? 0.5473 0.5772 0.7013 -0.0767 -0.0043 0.0215  283 LYS A CG  
2398 C CD  . LYS A 283 ? 0.5818 0.6227 0.7418 -0.0749 0.0069  0.0340  283 LYS A CD  
2399 C CE  . LYS A 283 ? 0.5171 0.5484 0.6626 -0.0709 0.0134  0.0392  283 LYS A CE  
2400 N NZ  . LYS A 283 ? 0.6571 0.6705 0.8028 -0.0749 0.0100  0.0357  283 LYS A NZ  
2401 N N   . ASN A 284 ? 0.2292 0.2972 0.4091 -0.0763 -0.0279 0.0035  284 ASN A N   
2402 C CA  . ASN A 284 ? 0.2949 0.3740 0.4895 -0.0781 -0.0382 -0.0034 284 ASN A CA  
2403 C C   . ASN A 284 ? 0.2107 0.3117 0.4180 -0.0755 -0.0344 0.0024  284 ASN A C   
2404 O O   . ASN A 284 ? 0.3041 0.4192 0.5322 -0.0785 -0.0413 -0.0008 284 ASN A O   
2405 C CB  . ASN A 284 ? 0.4447 0.5150 0.6171 -0.0712 -0.0479 -0.0143 284 ASN A CB  
2406 C CG  . ASN A 284 ? 0.5037 0.5572 0.6724 -0.0746 -0.0566 -0.0235 284 ASN A CG  
2407 O OD1 . ASN A 284 ? 0.4109 0.4579 0.5942 -0.0828 -0.0557 -0.0223 284 ASN A OD1 
2408 N ND2 . ASN A 284 ? 0.4071 0.4524 0.5548 -0.0673 -0.0644 -0.0325 284 ASN A ND2 
2409 N N   . SER A 285 ? 0.2155 0.3202 0.4107 -0.0694 -0.0241 0.0101  285 SER A N   
2410 C CA  . SER A 285 ? 0.2460 0.3691 0.4464 -0.0640 -0.0208 0.0140  285 SER A CA  
2411 C C   . SER A 285 ? 0.2637 0.4003 0.4815 -0.0659 -0.0093 0.0261  285 SER A C   
2412 O O   . SER A 285 ? 0.2401 0.3953 0.4721 -0.0637 -0.0074 0.0296  285 SER A O   
2413 C CB  . SER A 285 ? 0.2232 0.3407 0.3953 -0.0536 -0.0183 0.0123  285 SER A CB  
2414 O OG  . SER A 285 ? 0.2220 0.3258 0.3765 -0.0508 -0.0268 0.0028  285 SER A OG  
2415 N N   . VAL A 286 ? 0.3172 0.4453 0.5339 -0.0690 -0.0012 0.0329  286 VAL A N   
2416 C CA  . VAL A 286 ? 0.3916 0.5304 0.6196 -0.0685 0.0114  0.0456  286 VAL A CA  
2417 C C   . VAL A 286 ? 0.3846 0.5139 0.6243 -0.0762 0.0159  0.0515  286 VAL A C   
2418 O O   . VAL A 286 ? 0.3691 0.4806 0.5928 -0.0766 0.0144  0.0485  286 VAL A O   
2419 C CB  . VAL A 286 ? 0.3450 0.4828 0.5477 -0.0581 0.0195  0.0494  286 VAL A CB  
2420 C CG1 . VAL A 286 ? 0.3100 0.4530 0.5174 -0.0565 0.0325  0.0623  286 VAL A CG1 
2421 C CG2 . VAL A 286 ? 0.3734 0.5238 0.5714 -0.0505 0.0183  0.0468  286 VAL A CG2 
2422 N N   . GLU A 287 ? 0.3380 0.4792 0.6066 -0.0819 0.0222  0.0606  287 GLU A N   
2423 C CA  . GLU A 287 ? 0.4724 0.6009 0.7489 -0.0879 0.0264  0.0649  287 GLU A CA  
2424 C C   . GLU A 287 ? 0.4987 0.6173 0.7568 -0.0827 0.0366  0.0737  287 GLU A C   
2425 O O   . GLU A 287 ? 0.4770 0.5782 0.7261 -0.0851 0.0345  0.0713  287 GLU A O   
2426 C CB  . GLU A 287 ? 0.5069 0.6459 0.8061 -0.0909 0.0322  0.0711  287 GLU A CB  
2427 C CG  . GLU A 287 ? 0.5854 0.7110 0.8973 -0.0989 0.0319  0.0709  287 GLU A CG  
2428 C CD  . GLU A 287 ? 0.6292 0.7665 0.9689 -0.1048 0.0311  0.0711  287 GLU A CD  
2429 O OE1 . GLU A 287 ? 0.6971 0.8531 1.0456 -0.1025 0.0297  0.0706  287 GLU A OE1 
2430 O OE2 . GLU A 287 ? 0.6456 0.7736 0.9989 -0.1115 0.0321  0.0721  287 GLU A OE2 
2431 N N   . ARG A 288 ? 0.5214 0.6511 0.7726 -0.0744 0.0476  0.0837  288 ARG A N   
2432 C CA  . ARG A 288 ? 0.5936 0.7168 0.8261 -0.0675 0.0572  0.0924  288 ARG A CA  
2433 C C   . ARG A 288 ? 0.5541 0.6756 0.7562 -0.0580 0.0536  0.0851  288 ARG A C   
2434 O O   . ARG A 288 ? 0.5503 0.6843 0.7461 -0.0509 0.0560  0.0856  288 ARG A O   
2435 C CB  . ARG A 288 ? 0.6175 0.7497 0.8534 -0.0613 0.0701  0.1050  288 ARG A CB  
2436 C CG  . ARG A 288 ? 0.5454 0.6771 0.7578 -0.0499 0.0795  0.1133  288 ARG A CG  
2437 C CD  . ARG A 288 ? 0.5180 0.6603 0.7328 -0.0422 0.0912  0.1247  288 ARG A CD  
2438 N NE  . ARG A 288 ? 0.5718 0.7294 0.7765 -0.0329 0.0939  0.1247  288 ARG A NE  
2439 C CZ  . ARG A 288 ? 0.5318 0.7015 0.7430 -0.0273 0.1016  0.1319  288 ARG A CZ  
2440 N NH1 . ARG A 288 ? 0.3536 0.5226 0.5831 -0.0308 0.1074  0.1399  288 ARG A NH1 
2441 N NH2 . ARG A 288 ? 0.5352 0.7170 0.7349 -0.0179 0.1038  0.1309  288 ARG A NH2 
2442 N N   . ALA A 289 ? 0.4340 0.5392 0.6173 -0.0576 0.0479  0.0781  289 ALA A N   
2443 C CA  . ALA A 289 ? 0.3922 0.4939 0.5495 -0.0502 0.0431  0.0693  289 ALA A CA  
2444 C C   . ALA A 289 ? 0.3294 0.4162 0.4688 -0.0481 0.0424  0.0675  289 ALA A C   
2445 O O   . ALA A 289 ? 0.4061 0.4797 0.5475 -0.0540 0.0369  0.0629  289 ALA A O   
2446 C CB  . ALA A 289 ? 0.3913 0.4918 0.5489 -0.0531 0.0324  0.0575  289 ALA A CB  
2447 N N   . SER A 290 ? 0.3046 0.3938 0.4265 -0.0392 0.0474  0.0707  290 SER A N   
2448 C CA  . SER A 290 ? 0.2021 0.2800 0.3068 -0.0360 0.0457  0.0679  290 SER A CA  
2449 C C   . SER A 290 ? 0.2323 0.3048 0.3228 -0.0346 0.0374  0.0552  290 SER A C   
2450 O O   . SER A 290 ? 0.2352 0.3148 0.3210 -0.0311 0.0363  0.0510  290 SER A O   
2451 C CB  . SER A 290 ? 0.1941 0.2782 0.2859 -0.0260 0.0534  0.0756  290 SER A CB  
2452 O OG  . SER A 290 ? 0.2617 0.3383 0.3359 -0.0216 0.0497  0.0703  290 SER A OG  
2453 N N   . PRO A 291 ? 0.2458 0.3052 0.3298 -0.0370 0.0324  0.0495  291 PRO A N   
2454 C CA  . PRO A 291 ? 0.2259 0.2800 0.2974 -0.0353 0.0265  0.0390  291 PRO A CA  
2455 C C   . PRO A 291 ? 0.2308 0.2874 0.2871 -0.0278 0.0276  0.0368  291 PRO A C   
2456 O O   . PRO A 291 ? 0.1713 0.2230 0.2194 -0.0269 0.0236  0.0286  291 PRO A O   
2457 C CB  . PRO A 291 ? 0.2801 0.3199 0.3524 -0.0403 0.0220  0.0351  291 PRO A CB  
2458 C CG  . PRO A 291 ? 0.2424 0.2791 0.3196 -0.0411 0.0265  0.0435  291 PRO A CG  
2459 C CD  . PRO A 291 ? 0.2534 0.3017 0.3420 -0.0410 0.0329  0.0529  291 PRO A CD  
2460 N N   . TYR A 292 ? 0.2070 0.2713 0.2595 -0.0220 0.0331  0.0439  292 TYR A N   
2461 C CA  . TYR A 292 ? 0.2046 0.2718 0.2425 -0.0143 0.0327  0.0409  292 TYR A CA  
2462 C C   . TYR A 292 ? 0.1770 0.2542 0.2077 -0.0079 0.0339  0.0381  292 TYR A C   
2463 O O   . TYR A 292 ? 0.1867 0.2677 0.2052 -0.0006 0.0331  0.0349  292 TYR A O   
2464 C CB  . TYR A 292 ? 0.1742 0.2433 0.2086 -0.0095 0.0372  0.0498  292 TYR A CB  
2465 C CG  . TYR A 292 ? 0.2258 0.2840 0.2664 -0.0145 0.0369  0.0531  292 TYR A CG  
2466 C CD1 . TYR A 292 ? 0.2508 0.2984 0.2920 -0.0196 0.0311  0.0453  292 TYR A CD1 
2467 C CD2 . TYR A 292 ? 0.3659 0.4236 0.4115 -0.0135 0.0434  0.0649  292 TYR A CD2 
2468 C CE1 . TYR A 292 ? 0.2426 0.2793 0.2883 -0.0233 0.0310  0.0479  292 TYR A CE1 
2469 C CE2 . TYR A 292 ? 0.3576 0.4035 0.4087 -0.0177 0.0434  0.0677  292 TYR A CE2 
2470 C CZ  . TYR A 292 ? 0.2985 0.3340 0.3491 -0.0224 0.0369  0.0587  292 TYR A CZ  
2471 O OH  . TYR A 292 ? 0.4149 0.4379 0.4699 -0.0256 0.0370  0.0611  292 TYR A OH  
2472 N N   . LEU A 293 ? 0.1570 0.2383 0.1947 -0.0099 0.0350  0.0382  293 LEU A N   
2473 C CA  . LEU A 293 ? 0.1694 0.2594 0.2014 -0.0035 0.0369  0.0361  293 LEU A CA  
2474 C C   . LEU A 293 ? 0.2753 0.3595 0.3049 -0.0053 0.0316  0.0256  293 LEU A C   
2475 O O   . LEU A 293 ? 0.2085 0.2842 0.2437 -0.0119 0.0278  0.0223  293 LEU A O   
2476 C CB  . LEU A 293 ? 0.1777 0.2779 0.2216 -0.0037 0.0430  0.0453  293 LEU A CB  
2477 C CG  . LEU A 293 ? 0.3738 0.4836 0.4199 0.0014  0.0519  0.0578  293 LEU A CG  
2478 C CD1 . LEU A 293 ? 0.2869 0.3915 0.3298 0.0017  0.0535  0.0634  293 LEU A CD1 
2479 C CD2 . LEU A 293 ? 0.3689 0.4863 0.4354 -0.0037 0.0567  0.0661  293 LEU A CD2 
2480 N N   . ARG A 294 ? 0.2123 0.3004 0.2328 0.0013  0.0321  0.0207  294 ARG A N   
2481 C CA  . ARG A 294 ? 0.1834 0.2670 0.2032 0.0008  0.0294  0.0130  294 ARG A CA  
2482 C C   . ARG A 294 ? 0.1532 0.2450 0.1816 0.0013  0.0326  0.0181  294 ARG A C   
2483 O O   . ARG A 294 ? 0.2012 0.3037 0.2285 0.0074  0.0378  0.0232  294 ARG A O   
2484 C CB  . ARG A 294 ? 0.1606 0.2431 0.1680 0.0077  0.0283  0.0045  294 ARG A CB  
2485 C CG  . ARG A 294 ? 0.1593 0.2335 0.1659 0.0070  0.0262  -0.0036 294 ARG A CG  
2486 C CD  . ARG A 294 ? 0.3119 0.3817 0.3086 0.0116  0.0240  -0.0136 294 ARG A CD  
2487 N NE  . ARG A 294 ? 0.3479 0.4268 0.3352 0.0207  0.0262  -0.0137 294 ARG A NE  
2488 C CZ  . ARG A 294 ? 0.3186 0.3994 0.2966 0.0257  0.0236  -0.0192 294 ARG A CZ  
2489 N NH1 . ARG A 294 ? 0.2755 0.3509 0.2549 0.0215  0.0185  -0.0249 294 ARG A NH1 
2490 N NH2 . ARG A 294 ? 0.3388 0.4279 0.3059 0.0357  0.0259  -0.0192 294 ARG A NH2 
2491 N N   . TYR A 295 ? 0.1732 0.2608 0.2099 -0.0041 0.0296  0.0168  295 TYR A N   
2492 C CA  . TYR A 295 ? 0.1597 0.2564 0.2065 -0.0037 0.0311  0.0205  295 TYR A CA  
2493 C C   . TYR A 295 ? 0.1732 0.2676 0.2131 0.0016  0.0304  0.0144  295 TYR A C   
2494 O O   . TYR A 295 ? 0.2122 0.2946 0.2434 0.0018  0.0276  0.0069  295 TYR A O   
2495 C CB  . TYR A 295 ? 0.1414 0.2362 0.2016 -0.0117 0.0270  0.0222  295 TYR A CB  
2496 C CG  . TYR A 295 ? 0.1467 0.2446 0.2174 -0.0170 0.0288  0.0296  295 TYR A CG  
2497 C CD1 . TYR A 295 ? 0.1486 0.2371 0.2140 -0.0197 0.0280  0.0292  295 TYR A CD1 
2498 C CD2 . TYR A 295 ? 0.1949 0.3052 0.2825 -0.0191 0.0322  0.0374  295 TYR A CD2 
2499 C CE1 . TYR A 295 ? 0.1573 0.2468 0.2319 -0.0238 0.0305  0.0365  295 TYR A CE1 
2500 C CE2 . TYR A 295 ? 0.2262 0.3377 0.3252 -0.0242 0.0351  0.0449  295 TYR A CE2 
2501 C CZ  . TYR A 295 ? 0.1825 0.2826 0.2741 -0.0263 0.0342  0.0444  295 TYR A CZ  
2502 O OH  . TYR A 295 ? 0.2174 0.3173 0.3204 -0.0307 0.0379  0.0526  295 TYR A OH  
2503 N N   . TYR A 296 ? 0.1722 0.2781 0.2171 0.0063  0.0338  0.0181  296 TYR A N   
2504 C CA  . TYR A 296 ? 0.1537 0.2584 0.1939 0.0122  0.0338  0.0137  296 TYR A CA  
2505 C C   . TYR A 296 ? 0.1906 0.3040 0.2448 0.0104  0.0319  0.0173  296 TYR A C   
2506 O O   . TYR A 296 ? 0.2213 0.3494 0.2890 0.0098  0.0347  0.0246  296 TYR A O   
2507 C CB  . TYR A 296 ? 0.1863 0.2978 0.2184 0.0218  0.0395  0.0141  296 TYR A CB  
2508 C CG  . TYR A 296 ? 0.2506 0.3542 0.2682 0.0246  0.0396  0.0084  296 TYR A CG  
2509 C CD1 . TYR A 296 ? 0.3812 0.4718 0.3882 0.0269  0.0372  -0.0014 296 TYR A CD1 
2510 C CD2 . TYR A 296 ? 0.5204 0.6295 0.5359 0.0250  0.0418  0.0127  296 TYR A CD2 
2511 C CE1 . TYR A 296 ? 0.4119 0.4965 0.4081 0.0289  0.0358  -0.0080 296 TYR A CE1 
2512 C CE2 . TYR A 296 ? 0.5447 0.6482 0.5468 0.0285  0.0404  0.0066  296 TYR A CE2 
2513 C CZ  . TYR A 296 ? 0.4601 0.5520 0.4535 0.0300  0.0368  -0.0043 296 TYR A CZ  
2514 O OH  . TYR A 296 ? 0.5901 0.6782 0.5727 0.0331  0.0342  -0.0114 296 TYR A OH  
2515 N N   . PHE A 297 ? 0.2036 0.3082 0.2553 0.0098  0.0272  0.0125  297 PHE A N   
2516 C CA  . PHE A 297 ? 0.1614 0.2742 0.2250 0.0089  0.0234  0.0144  297 PHE A CA  
2517 C C   . PHE A 297 ? 0.1698 0.2908 0.2326 0.0181  0.0267  0.0152  297 PHE A C   
2518 O O   . PHE A 297 ? 0.2234 0.3338 0.2735 0.0240  0.0273  0.0105  297 PHE A O   
2519 C CB  . PHE A 297 ? 0.1894 0.2892 0.2482 0.0061  0.0170  0.0093  297 PHE A CB  
2520 C CG  . PHE A 297 ? 0.1483 0.2565 0.2166 0.0071  0.0116  0.0097  297 PHE A CG  
2521 C CD1 . PHE A 297 ? 0.1466 0.2657 0.2322 0.0005  0.0070  0.0122  297 PHE A CD1 
2522 C CD2 . PHE A 297 ? 0.1539 0.2593 0.2146 0.0150  0.0108  0.0074  297 PHE A CD2 
2523 C CE1 . PHE A 297 ? 0.1467 0.2752 0.2423 0.0016  0.0004  0.0112  297 PHE A CE1 
2524 C CE2 . PHE A 297 ? 0.1904 0.3052 0.2590 0.0174  0.0048  0.0075  297 PHE A CE2 
2525 C CZ  . PHE A 297 ? 0.1788 0.3063 0.2655 0.0106  -0.0011 0.0089  297 PHE A CZ  
2526 N N   . ARG A 298 ? 0.1730 0.3126 0.2502 0.0196  0.0296  0.0216  298 ARG A N   
2527 C CA  . ARG A 298 ? 0.1566 0.3070 0.2352 0.0291  0.0333  0.0235  298 ARG A CA  
2528 C C   . ARG A 298 ? 0.1845 0.3256 0.2446 0.0376  0.0391  0.0200  298 ARG A C   
2529 O O   . ARG A 298 ? 0.2015 0.3428 0.2563 0.0465  0.0412  0.0186  298 ARG A O   
2530 C CB  . ARG A 298 ? 0.1991 0.3501 0.2805 0.0318  0.0273  0.0209  298 ARG A CB  
2531 C CG  . ARG A 298 ? 0.2167 0.3777 0.3167 0.0241  0.0197  0.0224  298 ARG A CG  
2532 C CD  . ARG A 298 ? 0.2338 0.4002 0.3371 0.0294  0.0132  0.0202  298 ARG A CD  
2533 N NE  . ARG A 298 ? 0.1990 0.3748 0.3200 0.0216  0.0044  0.0196  298 ARG A NE  
2534 C CZ  . ARG A 298 ? 0.2497 0.4255 0.3706 0.0237  -0.0047 0.0152  298 ARG A CZ  
2535 N NH1 . ARG A 298 ? 0.2309 0.3975 0.3344 0.0336  -0.0051 0.0127  298 ARG A NH1 
2536 N NH2 . ARG A 298 ? 0.2760 0.4605 0.4138 0.0162  -0.0136 0.0134  298 ARG A NH2 
2537 N N   . GLU A 299 ? 0.2337 0.3664 0.2840 0.0354  0.0411  0.0181  299 GLU A N   
2538 C CA  . GLU A 299 ? 0.1945 0.3169 0.2271 0.0426  0.0447  0.0123  299 GLU A CA  
2539 C C   . GLU A 299 ? 0.2504 0.3563 0.2728 0.0456  0.0424  0.0048  299 GLU A C   
2540 O O   . GLU A 299 ? 0.2304 0.3299 0.2421 0.0536  0.0457  0.0003  299 GLU A O   
2541 C CB  . GLU A 299 ? 0.3250 0.4607 0.3563 0.0525  0.0520  0.0165  299 GLU A CB  
2542 C CG  . GLU A 299 ? 0.3757 0.5279 0.4188 0.0500  0.0561  0.0260  299 GLU A CG  
2543 C CD  . GLU A 299 ? 0.6173 0.7809 0.6553 0.0608  0.0647  0.0304  299 GLU A CD  
2544 O OE1 . GLU A 299 ? 0.6704 0.8369 0.7033 0.0618  0.0685  0.0339  299 GLU A OE1 
2545 O OE2 . GLU A 299 ? 0.6318 0.8015 0.6700 0.0693  0.0681  0.0309  299 GLU A OE2 
2546 N N   . LEU A 300 ? 0.1744 0.2725 0.1999 0.0400  0.0372  0.0035  300 LEU A N   
2547 C CA  . LEU A 300 ? 0.2195 0.3004 0.2357 0.0425  0.0362  -0.0019 300 LEU A CA  
2548 C C   . LEU A 300 ? 0.2475 0.3115 0.2572 0.0361  0.0343  -0.0073 300 LEU A C   
2549 O O   . LEU A 300 ? 0.2635 0.3117 0.2647 0.0386  0.0360  -0.0128 300 LEU A O   
2550 C CB  . LEU A 300 ? 0.2590 0.3426 0.2809 0.0432  0.0323  0.0008  300 LEU A CB  
2551 C CG  . LEU A 300 ? 0.2369 0.3393 0.2694 0.0487  0.0322  0.0062  300 LEU A CG  
2552 C CD1 . LEU A 300 ? 0.3130 0.4177 0.3511 0.0475  0.0255  0.0072  300 LEU A CD1 
2553 C CD2 . LEU A 300 ? 0.2504 0.3510 0.2753 0.0602  0.0377  0.0053  300 LEU A CD2 
2554 N N   . ILE A 301 ? 0.2121 0.2786 0.2271 0.0278  0.0310  -0.0056 301 ILE A N   
2555 C CA  . ILE A 301 ? 0.2198 0.2722 0.2311 0.0216  0.0289  -0.0096 301 ILE A CA  
2556 C C   . ILE A 301 ? 0.2804 0.3394 0.2967 0.0149  0.0271  -0.0072 301 ILE A C   
2557 O O   . ILE A 301 ? 0.2300 0.3021 0.2552 0.0129  0.0264  -0.0015 301 ILE A O   
2558 C CB  . ILE A 301 ? 0.2447 0.2885 0.2557 0.0204  0.0262  -0.0091 301 ILE A CB  
2559 C CG1 . ILE A 301 ? 0.2505 0.2791 0.2573 0.0152  0.0257  -0.0125 301 ILE A CG1 
2560 C CG2 . ILE A 301 ? 0.1857 0.2419 0.2061 0.0176  0.0216  -0.0043 301 ILE A CG2 
2561 C CD1 . ILE A 301 ? 0.2484 0.2663 0.2512 0.0168  0.0248  -0.0118 301 ILE A CD1 
2562 N N   . SER A 302 ? 0.1823 0.2326 0.1939 0.0117  0.0267  -0.0115 302 SER A N   
2563 C CA  . SER A 302 ? 0.2125 0.2677 0.2273 0.0066  0.0253  -0.0092 302 SER A CA  
2564 C C   . SER A 302 ? 0.1836 0.2331 0.2029 -0.0002 0.0219  -0.0077 302 SER A C   
2565 O O   . SER A 302 ? 0.1705 0.2087 0.1869 -0.0008 0.0210  -0.0105 302 SER A O   
2566 C CB  . SER A 302 ? 0.1864 0.2368 0.1945 0.0073  0.0255  -0.0151 302 SER A CB  
2567 O OG  . SER A 302 ? 0.2505 0.3065 0.2528 0.0145  0.0280  -0.0172 302 SER A OG  
2568 N N   . VAL A 303 ? 0.1991 0.2556 0.2250 -0.0045 0.0207  -0.0028 303 VAL A N   
2569 C CA  . VAL A 303 ? 0.1746 0.2256 0.2045 -0.0106 0.0172  -0.0017 303 VAL A CA  
2570 C C   . VAL A 303 ? 0.1526 0.2050 0.1845 -0.0143 0.0175  0.0008  303 VAL A C   
2571 O O   . VAL A 303 ? 0.2260 0.2886 0.2612 -0.0132 0.0200  0.0055  303 VAL A O   
2572 C CB  . VAL A 303 ? 0.2080 0.2660 0.2472 -0.0123 0.0145  0.0018  303 VAL A CB  
2573 C CG1 . VAL A 303 ? 0.1909 0.2413 0.2327 -0.0180 0.0100  0.0012  303 VAL A CG1 
2574 C CG2 . VAL A 303 ? 0.1957 0.2544 0.2326 -0.0068 0.0139  0.0000  303 VAL A CG2 
2575 N N   . PHE A 304 ? 0.1573 0.1996 0.1866 -0.0177 0.0157  -0.0017 304 PHE A N   
2576 C CA  . PHE A 304 ? 0.1616 0.2040 0.1935 -0.0211 0.0155  0.0014  304 PHE A CA  
2577 C C   . PHE A 304 ? 0.1968 0.2331 0.2335 -0.0260 0.0124  0.0026  304 PHE A C   
2578 O O   . PHE A 304 ? 0.2139 0.2420 0.2474 -0.0260 0.0102  -0.0010 304 PHE A O   
2579 C CB  . PHE A 304 ? 0.1825 0.2190 0.2085 -0.0204 0.0156  -0.0027 304 PHE A CB  
2580 C CG  . PHE A 304 ? 0.1940 0.2379 0.2156 -0.0157 0.0171  -0.0043 304 PHE A CG  
2581 C CD1 . PHE A 304 ? 0.2269 0.2796 0.2485 -0.0138 0.0186  0.0010  304 PHE A CD1 
2582 C CD2 . PHE A 304 ? 0.2100 0.2511 0.2270 -0.0126 0.0172  -0.0111 304 PHE A CD2 
2583 C CE1 . PHE A 304 ? 0.2463 0.3059 0.2609 -0.0077 0.0194  -0.0011 304 PHE A CE1 
2584 C CE2 . PHE A 304 ? 0.2910 0.3383 0.3029 -0.0077 0.0173  -0.0143 304 PHE A CE2 
2585 C CZ  . PHE A 304 ? 0.2439 0.3009 0.2535 -0.0047 0.0180  -0.0096 304 PHE A CZ  
2586 N N   . PHE A 305 ? 0.1950 0.2341 0.2385 -0.0293 0.0126  0.0076  305 PHE A N   
2587 C CA  . PHE A 305 ? 0.1927 0.2246 0.2409 -0.0342 0.0092  0.0078  305 PHE A CA  
2588 C C   . PHE A 305 ? 0.1954 0.2189 0.2396 -0.0352 0.0099  0.0079  305 PHE A C   
2589 O O   . PHE A 305 ? 0.2204 0.2483 0.2650 -0.0341 0.0128  0.0120  305 PHE A O   
2590 C CB  . PHE A 305 ? 0.2226 0.2623 0.2845 -0.0380 0.0091  0.0132  305 PHE A CB  
2591 C CG  . PHE A 305 ? 0.2204 0.2703 0.2885 -0.0368 0.0080  0.0131  305 PHE A CG  
2592 C CD1 . PHE A 305 ? 0.1852 0.2325 0.2553 -0.0378 0.0022  0.0085  305 PHE A CD1 
2593 C CD2 . PHE A 305 ? 0.2288 0.2911 0.2993 -0.0331 0.0128  0.0174  305 PHE A CD2 
2594 C CE1 . PHE A 305 ? 0.1697 0.2274 0.2457 -0.0357 0.0007  0.0084  305 PHE A CE1 
2595 C CE2 . PHE A 305 ? 0.2028 0.2750 0.2794 -0.0312 0.0122  0.0175  305 PHE A CE2 
2596 C CZ  . PHE A 305 ? 0.1808 0.2513 0.2611 -0.0326 0.0060  0.0132  305 PHE A CZ  
2597 N N   . ARG A 306 ? 0.1650 0.1770 0.2045 -0.0359 0.0075  0.0038  306 ARG A N   
2598 C CA  . ARG A 306 ? 0.1908 0.1956 0.2266 -0.0359 0.0085  0.0037  306 ARG A CA  
2599 C C   . ARG A 306 ? 0.2240 0.2269 0.2660 -0.0390 0.0086  0.0085  306 ARG A C   
2600 O O   . ARG A 306 ? 0.2005 0.2035 0.2504 -0.0427 0.0066  0.0100  306 ARG A O   
2601 C CB  . ARG A 306 ? 0.1609 0.1539 0.1899 -0.0349 0.0073  -0.0012 306 ARG A CB  
2602 C CG  . ARG A 306 ? 0.2554 0.2407 0.2847 -0.0368 0.0034  -0.0026 306 ARG A CG  
2603 C CD  . ARG A 306 ? 0.3162 0.2889 0.3363 -0.0342 0.0033  -0.0063 306 ARG A CD  
2604 N NE  . ARG A 306 ? 0.2672 0.2326 0.2868 -0.0355 -0.0016 -0.0085 306 ARG A NE  
2605 C CZ  . ARG A 306 ? 0.2317 0.1848 0.2440 -0.0336 -0.0026 -0.0113 306 ARG A CZ  
2606 N NH1 . ARG A 306 ? 0.2372 0.1842 0.2426 -0.0300 0.0021  -0.0111 306 ARG A NH1 
2607 N NH2 . ARG A 306 ? 0.2386 0.1859 0.2512 -0.0350 -0.0084 -0.0147 306 ARG A NH2 
2608 N N   . ASP A 307 ? 0.1575 0.1587 0.1974 -0.0376 0.0108  0.0107  307 ASP A N   
2609 C CA  . ASP A 307 ? 0.1638 0.1598 0.2079 -0.0394 0.0117  0.0155  307 ASP A CA  
2610 C C   . ASP A 307 ? 0.2135 0.1954 0.2546 -0.0409 0.0089  0.0111  307 ASP A C   
2611 O O   . ASP A 307 ? 0.2066 0.1828 0.2411 -0.0381 0.0095  0.0085  307 ASP A O   
2612 C CB  . ASP A 307 ? 0.1801 0.1802 0.2210 -0.0354 0.0148  0.0193  307 ASP A CB  
2613 C CG  . ASP A 307 ? 0.2961 0.2917 0.3413 -0.0360 0.0172  0.0263  307 ASP A CG  
2614 O OD1 . ASP A 307 ? 0.2553 0.2387 0.3023 -0.0388 0.0158  0.0251  307 ASP A OD1 
2615 O OD2 . ASP A 307 ? 0.2804 0.2837 0.3260 -0.0329 0.0209  0.0331  307 ASP A OD2 
2616 N N   . LYS A 308 ? 0.1965 0.1735 0.2430 -0.0449 0.0055  0.0097  308 LYS A N   
2617 C CA  . LYS A 308 ? 0.2431 0.2065 0.2849 -0.0451 0.0018  0.0042  308 LYS A CA  
2618 C C   . LYS A 308 ? 0.2409 0.1937 0.2801 -0.0440 0.0039  0.0060  308 LYS A C   
2619 O O   . LYS A 308 ? 0.2350 0.1787 0.2652 -0.0406 0.0038  0.0022  308 LYS A O   
2620 C CB  . LYS A 308 ? 0.2330 0.1949 0.2832 -0.0498 -0.0036 0.0015  308 LYS A CB  
2621 C CG  . LYS A 308 ? 0.2909 0.2380 0.3353 -0.0496 -0.0088 -0.0054 308 LYS A CG  
2622 C CD  . LYS A 308 ? 0.3383 0.2860 0.3933 -0.0545 -0.0157 -0.0094 308 LYS A CD  
2623 C CE  . LYS A 308 ? 0.4010 0.3324 0.4506 -0.0542 -0.0214 -0.0168 308 LYS A CE  
2624 N NZ  . LYS A 308 ? 0.5410 0.4718 0.6063 -0.0610 -0.0282 -0.0204 308 LYS A NZ  
2625 N N   . THR A 309 ? 0.1962 0.1503 0.2429 -0.0456 0.0069  0.0126  309 THR A N   
2626 C CA  . THR A 309 ? 0.2516 0.1951 0.2963 -0.0439 0.0091  0.0151  309 THR A CA  
2627 C C   . THR A 309 ? 0.1901 0.1352 0.2258 -0.0379 0.0117  0.0147  309 THR A C   
2628 O O   . THR A 309 ? 0.1933 0.1278 0.2230 -0.0351 0.0117  0.0119  309 THR A O   
2629 C CB  . THR A 309 ? 0.2705 0.2162 0.3248 -0.0456 0.0132  0.0241  309 THR A CB  
2630 O OG1 . THR A 309 ? 0.2765 0.2178 0.3426 -0.0522 0.0108  0.0237  309 THR A OG1 
2631 C CG2 . THR A 309 ? 0.3335 0.2693 0.3847 -0.0420 0.0165  0.0279  309 THR A CG2 
2632 N N   . LEU A 310 ? 0.1740 0.1328 0.2094 -0.0355 0.0137  0.0170  310 LEU A N   
2633 C CA  . LEU A 310 ? 0.1712 0.1334 0.2016 -0.0306 0.0152  0.0157  310 LEU A CA  
2634 C C   . LEU A 310 ? 0.1756 0.1325 0.2008 -0.0299 0.0143  0.0091  310 LEU A C   
2635 O O   . LEU A 310 ? 0.2073 0.1605 0.2299 -0.0265 0.0161  0.0079  310 LEU A O   
2636 C CB  . LEU A 310 ? 0.1628 0.1406 0.1942 -0.0285 0.0160  0.0173  310 LEU A CB  
2637 C CG  . LEU A 310 ? 0.2279 0.2123 0.2618 -0.0266 0.0183  0.0252  310 LEU A CG  
2638 C CD1 . LEU A 310 ? 0.2469 0.2463 0.2788 -0.0233 0.0182  0.0251  310 LEU A CD1 
2639 C CD2 . LEU A 310 ? 0.2226 0.2023 0.2554 -0.0226 0.0203  0.0298  310 LEU A CD2 
2640 N N   . SER A 311 ? 0.1663 0.1236 0.1904 -0.0322 0.0121  0.0054  311 SER A N   
2641 C CA  . SER A 311 ? 0.1976 0.1492 0.2154 -0.0302 0.0123  0.0004  311 SER A CA  
2642 C C   . SER A 311 ? 0.1820 0.1188 0.1936 -0.0283 0.0118  -0.0017 311 SER A C   
2643 O O   . SER A 311 ? 0.2216 0.1528 0.2274 -0.0243 0.0146  -0.0035 311 SER A O   
2644 C CB  . SER A 311 ? 0.1698 0.1247 0.1866 -0.0317 0.0101  -0.0024 311 SER A CB  
2645 O OG  . SER A 311 ? 0.1784 0.1463 0.2003 -0.0329 0.0106  -0.0006 311 SER A OG  
2646 N N   . ASP A 312 ? 0.1855 0.1156 0.1987 -0.0309 0.0087  -0.0015 312 ASP A N   
2647 C CA  . ASP A 312 ? 0.1988 0.1134 0.2051 -0.0288 0.0071  -0.0050 312 ASP A CA  
2648 C C   . ASP A 312 ? 0.2271 0.1357 0.2325 -0.0255 0.0110  -0.0019 312 ASP A C   
2649 O O   . ASP A 312 ? 0.2279 0.1243 0.2250 -0.0212 0.0117  -0.0048 312 ASP A O   
2650 C CB  . ASP A 312 ? 0.2315 0.1404 0.2422 -0.0335 0.0014  -0.0074 312 ASP A CB  
2651 C CG  . ASP A 312 ? 0.2656 0.1776 0.2744 -0.0347 -0.0039 -0.0125 312 ASP A CG  
2652 O OD1 . ASP A 312 ? 0.2818 0.1956 0.2820 -0.0305 -0.0027 -0.0145 312 ASP A OD1 
2653 O OD2 . ASP A 312 ? 0.2991 0.2118 0.3163 -0.0398 -0.0090 -0.0141 312 ASP A OD2 
2654 N N   . LEU A 313 ? 0.1978 0.1147 0.2106 -0.0261 0.0135  0.0040  313 LEU A N   
2655 C CA  . LEU A 313 ? 0.2059 0.1195 0.2179 -0.0215 0.0173  0.0073  313 LEU A CA  
2656 C C   . LEU A 313 ? 0.2136 0.1287 0.2211 -0.0165 0.0206  0.0051  313 LEU A C   
2657 O O   . LEU A 313 ? 0.2084 0.1140 0.2110 -0.0117 0.0232  0.0046  313 LEU A O   
2658 C CB  . LEU A 313 ? 0.2354 0.1611 0.2545 -0.0213 0.0191  0.0138  313 LEU A CB  
2659 C CG  . LEU A 313 ? 0.2617 0.1836 0.2858 -0.0239 0.0192  0.0193  313 LEU A CG  
2660 C CD1 . LEU A 313 ? 0.2113 0.1475 0.2394 -0.0216 0.0214  0.0261  313 LEU A CD1 
2661 C CD2 . LEU A 313 ? 0.2376 0.1423 0.2594 -0.0217 0.0204  0.0200  313 LEU A CD2 
2662 N N   . ILE A 314 ? 0.2498 0.1765 0.2601 -0.0174 0.0213  0.0040  314 ILE A N   
2663 C CA  . ILE A 314 ? 0.1983 0.1268 0.2079 -0.0137 0.0254  0.0026  314 ILE A CA  
2664 C C   . ILE A 314 ? 0.2292 0.1448 0.2283 -0.0110 0.0264  -0.0010 314 ILE A C   
2665 O O   . ILE A 314 ? 0.2073 0.1167 0.2023 -0.0056 0.0311  -0.0008 314 ILE A O   
2666 C CB  . ILE A 314 ? 0.1898 0.1326 0.2067 -0.0161 0.0256  0.0018  314 ILE A CB  
2667 C CG1 . ILE A 314 ? 0.1956 0.1514 0.2204 -0.0166 0.0240  0.0046  314 ILE A CG1 
2668 C CG2 . ILE A 314 ? 0.1743 0.1180 0.1936 -0.0133 0.0308  0.0005  314 ILE A CG2 
2669 C CD1 . ILE A 314 ? 0.2256 0.1949 0.2568 -0.0186 0.0230  0.0023  314 ILE A CD1 
2670 N N   . GLY A 315 ? 0.2209 0.1329 0.2150 -0.0136 0.0222  -0.0040 315 GLY A N   
2671 C CA  . GLY A 315 ? 0.2170 0.1178 0.1989 -0.0095 0.0224  -0.0078 315 GLY A CA  
2672 C C   . GLY A 315 ? 0.2346 0.1199 0.2065 -0.0050 0.0215  -0.0101 315 GLY A C   
2673 O O   . GLY A 315 ? 0.2369 0.1129 0.1969 0.0017  0.0242  -0.0122 315 GLY A O   
2674 N N   . PHE A 316 ? 0.2291 0.1103 0.2049 -0.0080 0.0180  -0.0098 316 PHE A N   
2675 C CA  . PHE A 316 ? 0.2656 0.1298 0.2321 -0.0048 0.0153  -0.0140 316 PHE A CA  
2676 C C   . PHE A 316 ? 0.2911 0.1491 0.2607 -0.0030 0.0180  -0.0108 316 PHE A C   
2677 O O   . PHE A 316 ? 0.2703 0.1133 0.2300 0.0027  0.0186  -0.0139 316 PHE A O   
2678 C CB  . PHE A 316 ? 0.2676 0.1278 0.2354 -0.0103 0.0066  -0.0191 316 PHE A CB  
2679 C CG  . PHE A 316 ? 0.2809 0.1444 0.2422 -0.0095 0.0030  -0.0233 316 PHE A CG  
2680 C CD1 . PHE A 316 ? 0.2875 0.1406 0.2318 -0.0014 0.0028  -0.0282 316 PHE A CD1 
2681 C CD2 . PHE A 316 ? 0.3024 0.1793 0.2729 -0.0153 0.0007  -0.0218 316 PHE A CD2 
2682 C CE1 . PHE A 316 ? 0.2923 0.1486 0.2293 0.0009  -0.0001 -0.0312 316 PHE A CE1 
2683 C CE2 . PHE A 316 ? 0.3064 0.1865 0.2707 -0.0135 -0.0023 -0.0251 316 PHE A CE2 
2684 C CZ  . PHE A 316 ? 0.3190 0.1888 0.2665 -0.0053 -0.0027 -0.0297 316 PHE A CZ  
2685 N N   . SER A 317 ? 0.2460 0.1144 0.2278 -0.0066 0.0197  -0.0047 317 SER A N   
2686 C CA  . SER A 317 ? 0.2490 0.1113 0.2337 -0.0043 0.0221  -0.0008 317 SER A CA  
2687 C C   . SER A 317 ? 0.2544 0.1226 0.2398 0.0025  0.0287  0.0033  317 SER A C   
2688 O O   . SER A 317 ? 0.2669 0.1240 0.2463 0.0090  0.0318  0.0033  317 SER A O   
2689 C CB  . SER A 317 ? 0.3070 0.1765 0.3033 -0.0103 0.0206  0.0045  317 SER A CB  
2690 O OG  . SER A 317 ? 0.3044 0.1697 0.3035 -0.0170 0.0151  0.0012  317 SER A OG  
2691 N N   . TYR A 318 ? 0.2303 0.1164 0.2241 0.0012  0.0306  0.0065  318 TYR A N   
2692 C CA  . TYR A 318 ? 0.2263 0.1220 0.2265 0.0062  0.0352  0.0109  318 TYR A CA  
2693 C C   . TYR A 318 ? 0.2382 0.1295 0.2340 0.0133  0.0410  0.0099  318 TYR A C   
2694 O O   . TYR A 318 ? 0.2526 0.1495 0.2540 0.0185  0.0450  0.0135  318 TYR A O   
2695 C CB  . TYR A 318 ? 0.2129 0.1289 0.2239 0.0028  0.0343  0.0125  318 TYR A CB  
2696 C CG  . TYR A 318 ? 0.2048 0.1282 0.2205 -0.0010 0.0306  0.0158  318 TYR A CG  
2697 C CD1 . TYR A 318 ? 0.2171 0.1312 0.2310 -0.0003 0.0302  0.0196  318 TYR A CD1 
2698 C CD2 . TYR A 318 ? 0.1922 0.1314 0.2141 -0.0045 0.0284  0.0154  318 TYR A CD2 
2699 C CE1 . TYR A 318 ? 0.2117 0.1328 0.2298 -0.0028 0.0285  0.0243  318 TYR A CE1 
2700 C CE2 . TYR A 318 ? 0.2489 0.1951 0.2733 -0.0064 0.0260  0.0190  318 TYR A CE2 
2701 C CZ  . TYR A 318 ? 0.2547 0.1923 0.2773 -0.0053 0.0266  0.0241  318 TYR A CZ  
2702 O OH  . TYR A 318 ? 0.2867 0.2316 0.3117 -0.0063 0.0258  0.0291  318 TYR A OH  
2703 N N   . HIS A 319 ? 0.2390 0.1214 0.2250 0.0146  0.0421  0.0057  319 HIS A N   
2704 C CA  . HIS A 319 ? 0.2486 0.1253 0.2287 0.0229  0.0492  0.0060  319 HIS A CA  
2705 C C   . HIS A 319 ? 0.3060 0.1706 0.2804 0.0299  0.0513  0.0072  319 HIS A C   
2706 O O   . HIS A 319 ? 0.3108 0.1763 0.2860 0.0374  0.0583  0.0099  319 HIS A O   
2707 C CB  . HIS A 319 ? 0.2586 0.1238 0.2241 0.0255  0.0496  0.0014  319 HIS A CB  
2708 C CG  . HIS A 319 ? 0.2937 0.1404 0.2446 0.0268  0.0439  -0.0040 319 HIS A CG  
2709 N ND1 . HIS A 319 ? 0.3952 0.2254 0.3316 0.0358  0.0465  -0.0066 319 HIS A ND1 
2710 C CD2 . HIS A 319 ? 0.2758 0.1181 0.2259 0.0201  0.0354  -0.0079 319 HIS A CD2 
2711 C CE1 . HIS A 319 ? 0.3086 0.1244 0.2358 0.0343  0.0389  -0.0129 319 HIS A CE1 
2712 N NE2 . HIS A 319 ? 0.4041 0.2274 0.3408 0.0243  0.0322  -0.0136 319 HIS A NE2 
2713 N N   . ALA A 320 ? 0.2723 0.1247 0.2418 0.0278  0.0460  0.0053  320 ALA A N   
2714 C CA  . ALA A 320 ? 0.3376 0.1749 0.3006 0.0345  0.0479  0.0058  320 ALA A CA  
2715 C C   . ALA A 320 ? 0.3182 0.1642 0.2927 0.0357  0.0497  0.0126  320 ALA A C   
2716 O O   . ALA A 320 ? 0.3397 0.1733 0.3099 0.0418  0.0519  0.0141  320 ALA A O   
2717 C CB  . ALA A 320 ? 0.3047 0.1225 0.2584 0.0315  0.0414  -0.0002 320 ALA A CB  
2718 N N   . TRP A 321 ? 0.2677 0.1338 0.2553 0.0310  0.0486  0.0165  321 TRP A N   
2719 C CA  . TRP A 321 ? 0.2943 0.1704 0.2913 0.0330  0.0490  0.0229  321 TRP A CA  
2720 C C   . TRP A 321 ? 0.3247 0.2189 0.3319 0.0382  0.0532  0.0258  321 TRP A C   
2721 O O   . TRP A 321 ? 0.3400 0.2425 0.3511 0.0373  0.0555  0.0235  321 TRP A O   
2722 C CB  . TRP A 321 ? 0.2508 0.1382 0.2550 0.0254  0.0439  0.0249  321 TRP A CB  
2723 C CG  . TRP A 321 ? 0.2848 0.1594 0.2844 0.0185  0.0397  0.0229  321 TRP A CG  
2724 C CD1 . TRP A 321 ? 0.3629 0.2213 0.3540 0.0157  0.0374  0.0166  321 TRP A CD1 
2725 C CD2 . TRP A 321 ? 0.2871 0.1656 0.2921 0.0140  0.0373  0.0274  321 TRP A CD2 
2726 N NE1 . TRP A 321 ? 0.3392 0.1921 0.3328 0.0086  0.0332  0.0165  321 TRP A NE1 
2727 C CE2 . TRP A 321 ? 0.2941 0.1589 0.2964 0.0075  0.0340  0.0238  321 TRP A CE2 
2728 C CE3 . TRP A 321 ? 0.2739 0.1668 0.2856 0.0158  0.0377  0.0344  321 TRP A CE3 
2729 C CZ2 . TRP A 321 ? 0.3419 0.2070 0.3502 0.0018  0.0324  0.0278  321 TRP A CZ2 
2730 C CZ3 . TRP A 321 ? 0.3751 0.2674 0.3894 0.0115  0.0365  0.0388  321 TRP A CZ3 
2731 C CH2 . TRP A 321 ? 0.2827 0.1612 0.2964 0.0041  0.0345  0.0359  321 TRP A CH2 
2732 N N   . ASN A 322 ? 0.3015 0.2027 0.3147 0.0437  0.0542  0.0313  322 ASN A N   
2733 C CA  . ASN A 322 ? 0.3212 0.2451 0.3486 0.0472  0.0556  0.0338  322 ASN A CA  
2734 C C   . ASN A 322 ? 0.2992 0.2420 0.3360 0.0397  0.0501  0.0322  322 ASN A C   
2735 O O   . ASN A 322 ? 0.3068 0.2471 0.3394 0.0344  0.0456  0.0323  322 ASN A O   
2736 C CB  . ASN A 322 ? 0.4793 0.4056 0.5090 0.0561  0.0570  0.0400  322 ASN A CB  
2737 C CG  . ASN A 322 ? 0.6511 0.6038 0.6958 0.0584  0.0544  0.0424  322 ASN A CG  
2738 O OD1 . ASN A 322 ? 0.6620 0.6243 0.7084 0.0561  0.0490  0.0439  322 ASN A OD1 
2739 N ND2 . ASN A 322 ? 0.6612 0.6267 0.7173 0.0637  0.0580  0.0425  322 ASN A ND2 
2740 N N   . ALA A 323 ? 0.2585 0.1985 0.2879 0.0984  0.0463  0.0617  323 ALA A N   
2741 C CA  . ALA A 323 ? 0.2259 0.1873 0.2572 0.0844  0.0348  0.0617  323 ALA A CA  
2742 C C   . ALA A 323 ? 0.2348 0.1937 0.2607 0.0874  0.0326  0.0732  323 ALA A C   
2743 O O   . ALA A 323 ? 0.3027 0.2580 0.3233 0.0742  0.0280  0.0702  323 ALA A O   
2744 C CB  . ALA A 323 ? 0.2504 0.2530 0.2940 0.0833  0.0269  0.0626  323 ALA A CB  
2745 N N   . GLU A 324 ? 0.3154 0.2777 0.3424 0.1056  0.0360  0.0871  324 GLU A N   
2746 C CA  . GLU A 324 ? 0.4377 0.4007 0.4581 0.1082  0.0333  0.0993  324 GLU A CA  
2747 C C   . GLU A 324 ? 0.4036 0.3233 0.4111 0.1045  0.0420  0.0996  324 GLU A C   
2748 O O   . GLU A 324 ? 0.3970 0.3151 0.3974 0.0961  0.0389  0.1030  324 GLU A O   
2749 C CB  . GLU A 324 ? 0.5691 0.5558 0.5943 0.1277  0.0325  0.1152  324 GLU A CB  
2750 C CG  . GLU A 324 ? 0.6494 0.6123 0.6708 0.1407  0.0436  0.1183  324 GLU A CG  
2751 C CD  . GLU A 324 ? 0.8286 0.7734 0.8387 0.1436  0.0470  0.1284  324 GLU A CD  
2752 O OE1 . GLU A 324 ? 0.8738 0.8157 0.8769 0.1331  0.0428  0.1299  324 GLU A OE1 
2753 O OE2 . GLU A 324 ? 0.7185 0.6529 0.7266 0.1569  0.0541  0.1354  324 GLU A OE2 
2754 N N   . ASP A 325 ? 0.4285 0.3150 0.4323 0.1076  0.0528  0.0939  325 ASP A N   
2755 C CA  . ASP A 325 ? 0.4160 0.2654 0.4086 0.0960  0.0596  0.0882  325 ASP A CA  
2756 C C   . ASP A 325 ? 0.3862 0.2348 0.3773 0.0769  0.0549  0.0796  325 ASP A C   
2757 O O   . ASP A 325 ? 0.3429 0.1796 0.3271 0.0681  0.0559  0.0824  325 ASP A O   
2758 C CB  . ASP A 325 ? 0.5086 0.3297 0.4979 0.0960  0.0692  0.0770  325 ASP A CB  
2759 C CG  . ASP A 325 ? 0.6165 0.4312 0.6049 0.1133  0.0760  0.0848  325 ASP A CG  
2760 O OD1 . ASP A 325 ? 0.6164 0.4542 0.6090 0.1265  0.0724  0.0986  325 ASP A OD1 
2761 O OD2 . ASP A 325 ? 0.6215 0.4092 0.6047 0.1135  0.0848  0.0766  325 ASP A OD2 
2762 N N   . ALA A 326 ? 0.2950 0.1622 0.2930 0.0681  0.0488  0.0669  326 ALA A N   
2763 C CA  . ALA A 326 ? 0.2983 0.1693 0.2959 0.0490  0.0435  0.0557  326 ALA A CA  
2764 C C   . ALA A 326 ? 0.3080 0.2021 0.3059 0.0441  0.0350  0.0611  326 ALA A C   
2765 O O   . ALA A 326 ? 0.3004 0.1874 0.2937 0.0328  0.0349  0.0588  326 ALA A O   
2766 C CB  . ALA A 326 ? 0.2447 0.1303 0.2488 0.0434  0.0394  0.0435  326 ALA A CB  
2767 N N   . VAL A 327 ? 0.2514 0.1748 0.2545 0.0517  0.0281  0.0676  327 VAL A N   
2768 C CA  . VAL A 327 ? 0.2368 0.1826 0.2384 0.0462  0.0200  0.0707  327 VAL A CA  
2769 C C   . VAL A 327 ? 0.2840 0.2186 0.2756 0.0498  0.0238  0.0823  327 VAL A C   
2770 O O   . VAL A 327 ? 0.2583 0.1966 0.2445 0.0404  0.0214  0.0809  327 VAL A O   
2771 C CB  . VAL A 327 ? 0.2887 0.2696 0.2976 0.0519  0.0117  0.0742  327 VAL A CB  
2772 C CG1 . VAL A 327 ? 0.2963 0.2990 0.3008 0.0459  0.0038  0.0764  327 VAL A CG1 
2773 C CG2 . VAL A 327 ? 0.2366 0.2286 0.2546 0.0451  0.0083  0.0629  327 VAL A CG2 
2774 N N   . ARG A 328 ? 0.3213 0.2426 0.3097 0.0645  0.0303  0.0949  328 ARG A N   
2775 C CA  . ARG A 328 ? 0.3685 0.2764 0.3461 0.0681  0.0351  0.1081  328 ARG A CA  
2776 C C   . ARG A 328 ? 0.4173 0.2968 0.3888 0.0536  0.0417  0.1015  328 ARG A C   
2777 O O   . ARG A 328 ? 0.3374 0.2169 0.3012 0.0479  0.0424  0.1069  328 ARG A O   
2778 C CB  . ARG A 328 ? 0.4629 0.3560 0.4385 0.0862  0.0424  0.1212  328 ARG A CB  
2779 C CG  . ARG A 328 ? 0.5722 0.4992 0.5512 0.1008  0.0358  0.1327  328 ARG A CG  
2780 C CD  . ARG A 328 ? 0.5844 0.4959 0.5605 0.1142  0.0436  0.1416  328 ARG A CD  
2781 N NE  . ARG A 328 ? 0.7377 0.6827 0.7188 0.1288  0.0383  0.1522  328 ARG A NE  
2782 C CZ  . ARG A 328 ? 0.8041 0.7429 0.7846 0.1434  0.0442  0.1618  328 ARG A CZ  
2783 N NH1 . ARG A 328 ? 0.7604 0.6586 0.7346 0.1449  0.0556  0.1615  328 ARG A NH1 
2784 N NH2 . ARG A 328 ? 0.8266 0.8004 0.8126 0.1559  0.0389  0.1713  328 ARG A NH2 
2785 N N   . ASP A 329 ? 0.3631 0.2208 0.3379 0.0470  0.0468  0.0898  329 ASP A N   
2786 C CA  . ASP A 329 ? 0.3807 0.2154 0.3517 0.0316  0.0527  0.0821  329 ASP A CA  
2787 C C   . ASP A 329 ? 0.3339 0.1908 0.3076 0.0175  0.0454  0.0737  329 ASP A C   
2788 O O   . ASP A 329 ? 0.3611 0.2128 0.3302 0.0084  0.0485  0.0754  329 ASP A O   
2789 C CB  . ASP A 329 ? 0.3614 0.1748 0.3353 0.0276  0.0578  0.0696  329 ASP A CB  
2790 C CG  . ASP A 329 ? 0.3395 0.1391 0.3116 0.0096  0.0609  0.0585  329 ASP A CG  
2791 O OD1 . ASP A 329 ? 0.3173 0.1277 0.2939 -0.0023 0.0570  0.0488  329 ASP A OD1 
2792 O OD2 . ASP A 329 ? 0.4073 0.1872 0.3742 0.0075  0.0670  0.0598  329 ASP A OD2 
2793 N N   . PHE A 330 ? 0.2766 0.1580 0.2579 0.0162  0.0365  0.0651  330 PHE A N   
2794 C CA  . PHE A 330 ? 0.2753 0.1756 0.2592 0.0051  0.0302  0.0568  330 PHE A CA  
2795 C C   . PHE A 330 ? 0.3152 0.2303 0.2925 0.0062  0.0277  0.0648  330 PHE A C   
2796 O O   . PHE A 330 ? 0.2970 0.2139 0.2716 -0.0027 0.0291  0.0622  330 PHE A O   
2797 C CB  . PHE A 330 ? 0.2128 0.1320 0.2048 0.0052  0.0224  0.0481  330 PHE A CB  
2798 C CG  . PHE A 330 ? 0.2487 0.1792 0.2445 -0.0056 0.0179  0.0377  330 PHE A CG  
2799 C CD1 . PHE A 330 ? 0.2774 0.1994 0.2770 -0.0140 0.0199  0.0288  330 PHE A CD1 
2800 C CD2 . PHE A 330 ? 0.2538 0.2038 0.2490 -0.0068 0.0117  0.0366  330 PHE A CD2 
2801 C CE1 . PHE A 330 ? 0.2752 0.2089 0.2790 -0.0212 0.0161  0.0211  330 PHE A CE1 
2802 C CE2 . PHE A 330 ? 0.2385 0.1956 0.2369 -0.0145 0.0089  0.0275  330 PHE A CE2 
2803 C CZ  . PHE A 330 ? 0.2649 0.2144 0.2682 -0.0206 0.0111  0.0207  330 PHE A CZ  
2804 N N   . ILE A 331 ? 0.3261 0.2550 0.3005 0.0173  0.0240  0.0744  331 ILE A N   
2805 C CA  . ILE A 331 ? 0.2923 0.2377 0.2580 0.0185  0.0212  0.0821  331 ILE A CA  
2806 C C   . ILE A 331 ? 0.3473 0.2738 0.3034 0.0171  0.0302  0.0918  331 ILE A C   
2807 O O   . ILE A 331 ? 0.3130 0.2475 0.2626 0.0105  0.0307  0.0920  331 ILE A O   
2808 C CB  . ILE A 331 ? 0.3323 0.2989 0.2969 0.0309  0.0152  0.0918  331 ILE A CB  
2809 C CG1 . ILE A 331 ? 0.3483 0.3371 0.3225 0.0287  0.0064  0.0815  331 ILE A CG1 
2810 C CG2 . ILE A 331 ? 0.3800 0.3626 0.3323 0.0332  0.0132  0.1021  331 ILE A CG2 
2811 C CD1 . ILE A 331 ? 0.2667 0.2708 0.2395 0.0167  0.0004  0.0696  331 ILE A CD1 
2812 N N   . GLY A 332 ? 0.3225 0.2225 0.2774 0.0228  0.0383  0.0997  332 GLY A N   
2813 C CA  . GLY A 332 ? 0.3787 0.2561 0.3247 0.0198  0.0483  0.1095  332 GLY A CA  
2814 C C   . GLY A 332 ? 0.3200 0.1926 0.2679 0.0027  0.0519  0.0992  332 GLY A C   
2815 O O   . GLY A 332 ? 0.3704 0.2440 0.3109 -0.0026 0.0562  0.1055  332 GLY A O   
2816 N N   . ARG A 333 ? 0.2821 0.1525 0.2400 -0.0056 0.0501  0.0841  333 ARG A N   
2817 C CA  . ARG A 333 ? 0.3154 0.1877 0.2776 -0.0209 0.0522  0.0742  333 ARG A CA  
2818 C C   . ARG A 333 ? 0.2919 0.1920 0.2532 -0.0235 0.0470  0.0713  333 ARG A C   
2819 O O   . ARG A 333 ? 0.3126 0.2164 0.2722 -0.0320 0.0517  0.0715  333 ARG A O   
2820 C CB  . ARG A 333 ? 0.3225 0.1918 0.2951 -0.0270 0.0497  0.0596  333 ARG A CB  
2821 C CG  . ARG A 333 ? 0.4697 0.3095 0.4410 -0.0254 0.0562  0.0602  333 ARG A CG  
2822 C CD  . ARG A 333 ? 0.6100 0.4461 0.5889 -0.0352 0.0553  0.0452  333 ARG A CD  
2823 N NE  . ARG A 333 ? 0.5652 0.3975 0.5459 -0.0493 0.0586  0.0395  333 ARG A NE  
2824 C CZ  . ARG A 333 ? 0.6769 0.5253 0.6616 -0.0596 0.0584  0.0375  333 ARG A CZ  
2825 N NH1 . ARG A 333 ? 0.7528 0.6227 0.7393 -0.0570 0.0543  0.0388  333 ARG A NH1 
2826 N NH2 . ARG A 333 ? 0.5786 0.4263 0.5665 -0.0714 0.0609  0.0331  333 ARG A NH2 
2827 N N   . LEU A 334 ? 0.2648 0.1846 0.2271 -0.0168 0.0380  0.0679  334 LEU A N   
2828 C CA  . LEU A 334 ? 0.2351 0.1777 0.1943 -0.0189 0.0338  0.0637  334 LEU A CA  
2829 C C   . LEU A 334 ? 0.3057 0.2531 0.2516 -0.0166 0.0377  0.0756  334 LEU A C   
2830 O O   . LEU A 334 ? 0.2676 0.2270 0.2094 -0.0218 0.0397  0.0727  334 LEU A O   
2831 C CB  . LEU A 334 ? 0.2535 0.2128 0.2149 -0.0136 0.0240  0.0580  334 LEU A CB  
2832 C CG  . LEU A 334 ? 0.2446 0.2034 0.2178 -0.0166 0.0199  0.0460  334 LEU A CG  
2833 C CD1 . LEU A 334 ? 0.2703 0.2452 0.2445 -0.0127 0.0113  0.0422  334 LEU A CD1 
2834 C CD2 . LEU A 334 ? 0.2415 0.2027 0.2202 -0.0252 0.0218  0.0361  334 LEU A CD2 
2835 N N   . LYS A 335 ? 0.3016 0.2410 0.2402 -0.0077 0.0393  0.0897  335 LYS A N   
2836 C CA  . LYS A 335 ? 0.2877 0.2318 0.2119 -0.0046 0.0433  0.1035  335 LYS A CA  
2837 C C   . LYS A 335 ? 0.3093 0.2382 0.2314 -0.0143 0.0544  0.1073  335 LYS A C   
2838 O O   . LYS A 335 ? 0.3108 0.2514 0.2237 -0.0178 0.0579  0.1113  335 LYS A O   
2839 C CB  . LYS A 335 ? 0.3070 0.2452 0.2247 0.0091  0.0430  0.1201  335 LYS A CB  
2840 C CG  . LYS A 335 ? 0.4162 0.3644 0.3175 0.0144  0.0452  0.1362  335 LYS A CG  
2841 C CD  . LYS A 335 ? 0.4785 0.4266 0.3747 0.0308  0.0432  0.1533  335 LYS A CD  
2842 C CE  . LYS A 335 ? 0.6551 0.6109 0.5371 0.0351  0.0444  0.1660  335 LYS A CE  
2843 N NZ  . LYS A 335 ? 0.7428 0.6677 0.6239 0.0368  0.0535  0.1751  335 LYS A NZ  
2844 N N   . LYS A 336 ? 0.3075 0.2118 0.2378 -0.0201 0.0603  0.1051  336 LYS A N   
2845 C CA  . LYS A 336 ? 0.3228 0.2138 0.2528 -0.0323 0.0710  0.1076  336 LYS A CA  
2846 C C   . LYS A 336 ? 0.3310 0.2444 0.2673 -0.0427 0.0703  0.0955  336 LYS A C   
2847 O O   . LYS A 336 ? 0.3921 0.3105 0.3240 -0.0499 0.0778  0.1004  336 LYS A O   
2848 C CB  . LYS A 336 ? 0.5435 0.4055 0.4813 -0.0384 0.0760  0.1039  336 LYS A CB  
2849 C CG  . LYS A 336 ? 0.6271 0.4859 0.5712 -0.0546 0.0815  0.0985  336 LYS A CG  
2850 C CD  . LYS A 336 ? 0.7493 0.5836 0.6990 -0.0593 0.0830  0.0937  336 LYS A CD  
2851 C CE  . LYS A 336 ? 0.8394 0.6722 0.7940 -0.0750 0.0886  0.0919  336 LYS A CE  
2852 N NZ  . LYS A 336 ? 0.8580 0.7051 0.8269 -0.0874 0.0860  0.0763  336 LYS A NZ  
2853 N N   . ILE A 337 ? 0.3000 0.2272 0.2466 -0.0427 0.0621  0.0806  337 ILE A N   
2854 C CA  . ILE A 337 ? 0.2689 0.2181 0.2213 -0.0487 0.0614  0.0699  337 ILE A CA  
2855 C C   . ILE A 337 ? 0.2662 0.2343 0.2058 -0.0440 0.0612  0.0736  337 ILE A C   
2856 O O   . ILE A 337 ? 0.3210 0.3007 0.2586 -0.0495 0.0677  0.0737  337 ILE A O   
2857 C CB  . ILE A 337 ? 0.3603 0.3177 0.3244 -0.0473 0.0528  0.0553  337 ILE A CB  
2858 C CG1 . ILE A 337 ? 0.3081 0.2508 0.2836 -0.0534 0.0533  0.0503  337 ILE A CG1 
2859 C CG2 . ILE A 337 ? 0.2584 0.2376 0.2266 -0.0494 0.0524  0.0458  337 ILE A CG2 
2860 C CD1 . ILE A 337 ? 0.2965 0.2452 0.2813 -0.0501 0.0444  0.0388  337 ILE A CD1 
2861 N N   . HIS A 338 ? 0.2891 0.2627 0.2196 -0.0342 0.0540  0.0763  338 HIS A N   
2862 C CA  . HIS A 338 ? 0.3173 0.3103 0.2333 -0.0303 0.0525  0.0784  338 HIS A CA  
2863 C C   . HIS A 338 ? 0.3531 0.3455 0.2566 -0.0325 0.0623  0.0926  338 HIS A C   
2864 O O   . HIS A 338 ? 0.3715 0.3809 0.2663 -0.0345 0.0659  0.0908  338 HIS A O   
2865 C CB  . HIS A 338 ? 0.3050 0.3043 0.2137 -0.0208 0.0430  0.0815  338 HIS A CB  
2866 C CG  . HIS A 338 ? 0.3522 0.3730 0.2436 -0.0175 0.0403  0.0838  338 HIS A CG  
2867 N ND1 . HIS A 338 ? 0.3856 0.4113 0.2628 -0.0106 0.0398  0.1000  338 HIS A ND1 
2868 C CD2 . HIS A 338 ? 0.2803 0.3189 0.1653 -0.0199 0.0379  0.0714  338 HIS A CD2 
2869 C CE1 . HIS A 338 ? 0.3834 0.4320 0.2455 -0.0100 0.0364  0.0972  338 HIS A CE1 
2870 N NE2 . HIS A 338 ? 0.3551 0.4102 0.2213 -0.0161 0.0357  0.0789  338 HIS A NE2 
2871 N N   . GLU A 339 ? 0.3496 0.3212 0.2515 -0.0321 0.0677  0.1069  339 GLU A N   
2872 C CA  . GLU A 339 ? 0.3589 0.3263 0.2479 -0.0341 0.0778  0.1230  339 GLU A CA  
2873 C C   . GLU A 339 ? 0.4050 0.3670 0.3019 -0.0479 0.0888  0.1214  339 GLU A C   
2874 O O   . GLU A 339 ? 0.4374 0.3989 0.3244 -0.0520 0.0981  0.1333  339 GLU A O   
2875 C CB  . GLU A 339 ? 0.3844 0.3287 0.2666 -0.0262 0.0798  0.1411  339 GLU A CB  
2876 C CG  . GLU A 339 ? 0.4906 0.4473 0.3650 -0.0119 0.0693  0.1457  339 GLU A CG  
2877 C CD  . GLU A 339 ? 0.6070 0.5426 0.4799 -0.0022 0.0687  0.1581  339 GLU A CD  
2878 O OE1 . GLU A 339 ? 0.7165 0.6241 0.5983 -0.0065 0.0740  0.1574  339 GLU A OE1 
2879 O OE2 . GLU A 339 ? 0.7107 0.6597 0.5744 0.0094  0.0622  0.1665  339 GLU A OE2 
2880 N N   . SER A 340 ? 0.4243 0.3853 0.3389 -0.0555 0.0876  0.1070  340 SER A N   
2881 C CA  . SER A 340 ? 0.3811 0.3401 0.3057 -0.0698 0.0972  0.1053  340 SER A CA  
2882 C C   . SER A 340 ? 0.4376 0.4263 0.3658 -0.0740 0.1002  0.0969  340 SER A C   
2883 O O   . SER A 340 ? 0.5125 0.5065 0.4479 -0.0858 0.1095  0.0981  340 SER A O   
2884 C CB  . SER A 340 ? 0.3574 0.3032 0.2993 -0.0765 0.0944  0.0946  340 SER A CB  
2885 O OG  . SER A 340 ? 0.3910 0.3560 0.3436 -0.0734 0.0858  0.0789  340 SER A OG  
2886 N N   . VAL A 341 ? 0.3742 0.3824 0.2981 -0.0650 0.0934  0.0878  341 VAL A N   
2887 C CA  . VAL A 341 ? 0.3813 0.4155 0.3069 -0.0664 0.0975  0.0793  341 VAL A CA  
2888 C C   . VAL A 341 ? 0.4034 0.4513 0.3087 -0.0576 0.0959  0.0805  341 VAL A C   
2889 O O   . VAL A 341 ? 0.3653 0.4073 0.2593 -0.0499 0.0880  0.0836  341 VAL A O   
2890 C CB  . VAL A 341 ? 0.3371 0.3813 0.2803 -0.0652 0.0918  0.0621  341 VAL A CB  
2891 C CG1 . VAL A 341 ? 0.3710 0.4076 0.3334 -0.0753 0.0931  0.0603  341 VAL A CG1 
2892 C CG2 . VAL A 341 ? 0.3965 0.4349 0.3366 -0.0555 0.0799  0.0544  341 VAL A CG2 
2893 N N   . ASP A 342 ? 0.4013 0.4704 0.3024 -0.0590 0.1037  0.0771  342 ASP A N   
2894 C CA  . ASP A 342 ? 0.3505 0.4348 0.2304 -0.0522 0.1037  0.0761  342 ASP A CA  
2895 C C   . ASP A 342 ? 0.4545 0.5499 0.3353 -0.0457 0.0980  0.0566  342 ASP A C   
2896 O O   . ASP A 342 ? 0.6023 0.7076 0.4642 -0.0406 0.0959  0.0523  342 ASP A O   
2897 C CB  . ASP A 342 ? 0.3968 0.4969 0.2673 -0.0571 0.1174  0.0847  342 ASP A CB  
2898 C CG  . ASP A 342 ? 0.5556 0.6377 0.4161 -0.0593 0.1209  0.1039  342 ASP A CG  
2899 O OD1 . ASP A 342 ? 0.6392 0.7039 0.4948 -0.0559 0.1140  0.1127  342 ASP A OD1 
2900 O OD2 . ASP A 342 ? 0.6013 0.6852 0.4593 -0.0638 0.1309  0.1099  342 ASP A OD2 
2901 N N   . PHE A 343 ? 0.2964 0.3897 0.1973 -0.0458 0.0954  0.0448  343 PHE A N   
2902 C CA  . PHE A 343 ? 0.2862 0.3835 0.1885 -0.0390 0.0903  0.0275  343 PHE A CA  
2903 C C   . PHE A 343 ? 0.2904 0.3710 0.1960 -0.0364 0.0775  0.0243  343 PHE A C   
2904 O O   . PHE A 343 ? 0.2984 0.3670 0.2042 -0.0384 0.0730  0.0350  343 PHE A O   
2905 C CB  . PHE A 343 ? 0.3496 0.4569 0.2714 -0.0385 0.0960  0.0182  343 PHE A CB  
2906 C CG  . PHE A 343 ? 0.3345 0.4345 0.2789 -0.0435 0.0931  0.0209  343 PHE A CG  
2907 C CD1 . PHE A 343 ? 0.2782 0.3671 0.2333 -0.0398 0.0836  0.0130  343 PHE A CD1 
2908 C CD2 . PHE A 343 ? 0.3053 0.4101 0.2596 -0.0531 0.1001  0.0309  343 PHE A CD2 
2909 C CE1 . PHE A 343 ? 0.2836 0.3678 0.2575 -0.0446 0.0807  0.0148  343 PHE A CE1 
2910 C CE2 . PHE A 343 ? 0.3901 0.4890 0.3637 -0.0594 0.0970  0.0315  343 PHE A CE2 
2911 C CZ  . PHE A 343 ? 0.3342 0.4238 0.3172 -0.0547 0.0870  0.0232  343 PHE A CZ  
2912 N N   . GLN A 344 ? 0.2647 0.3438 0.1723 -0.0317 0.0724  0.0096  344 GLN A N   
2913 C CA  . GLN A 344 ? 0.2554 0.3206 0.1675 -0.0304 0.0610  0.0063  344 GLN A CA  
2914 C C   . GLN A 344 ? 0.2899 0.3477 0.2244 -0.0308 0.0595  0.0032  344 GLN A C   
2915 O O   . GLN A 344 ? 0.2415 0.3026 0.1839 -0.0273 0.0618  -0.0071 344 GLN A O   
2916 C CB  . GLN A 344 ? 0.2776 0.3431 0.1775 -0.0271 0.0561  -0.0072 344 GLN A CB  
2917 C CG  . GLN A 344 ? 0.3198 0.3962 0.1957 -0.0278 0.0556  -0.0039 344 GLN A CG  
2918 C CD  . GLN A 344 ? 0.3802 0.4581 0.2419 -0.0275 0.0503  -0.0186 344 GLN A CD  
2919 O OE1 . GLN A 344 ? 0.3981 0.4810 0.2478 -0.0293 0.0423  -0.0160 344 GLN A OE1 
2920 N NE2 . GLN A 344 ? 0.4035 0.4775 0.2662 -0.0253 0.0550  -0.0341 344 GLN A NE2 
2921 N N   . PRO A 345 ? 0.2234 0.2712 0.1673 -0.0344 0.0561  0.0117  345 PRO A N   
2922 C CA  . PRO A 345 ? 0.2261 0.2694 0.1895 -0.0359 0.0544  0.0087  345 PRO A CA  
2923 C C   . PRO A 345 ? 0.2487 0.2834 0.2163 -0.0317 0.0458  0.0004  345 PRO A C   
2924 O O   . PRO A 345 ? 0.2287 0.2572 0.1870 -0.0302 0.0395  0.0000  345 PRO A O   
2925 C CB  . PRO A 345 ? 0.2076 0.2403 0.1745 -0.0418 0.0544  0.0199  345 PRO A CB  
2926 C CG  . PRO A 345 ? 0.2243 0.2506 0.1754 -0.0391 0.0511  0.0273  345 PRO A CG  
2927 C CD  . PRO A 345 ? 0.2939 0.3337 0.2297 -0.0363 0.0542  0.0246  345 PRO A CD  
2928 N N   . VAL A 346 ? 0.1854 0.2216 0.1676 -0.0301 0.0455  -0.0052 346 VAL A N   
2929 C CA  . VAL A 346 ? 0.1739 0.2005 0.1619 -0.0271 0.0382  -0.0106 346 VAL A CA  
2930 C C   . VAL A 346 ? 0.1829 0.2048 0.1824 -0.0311 0.0348  -0.0056 346 VAL A C   
2931 O O   . VAL A 346 ? 0.2342 0.2643 0.2448 -0.0344 0.0382  -0.0040 346 VAL A O   
2932 C CB  . VAL A 346 ? 0.1734 0.2036 0.1679 -0.0206 0.0404  -0.0193 346 VAL A CB  
2933 C CG1 . VAL A 346 ? 0.2582 0.2755 0.2561 -0.0180 0.0333  -0.0232 346 VAL A CG1 
2934 C CG2 . VAL A 346 ? 0.1897 0.2233 0.1711 -0.0166 0.0460  -0.0262 346 VAL A CG2 
2935 N N   . VAL A 347 ? 0.2308 0.2414 0.2279 -0.0314 0.0283  -0.0039 347 VAL A N   
2936 C CA  . VAL A 347 ? 0.2382 0.2418 0.2425 -0.0350 0.0259  0.0003  347 VAL A CA  
2937 C C   . VAL A 347 ? 0.1604 0.1595 0.1708 -0.0323 0.0197  -0.0042 347 VAL A C   
2938 O O   . VAL A 347 ? 0.1908 0.1842 0.1960 -0.0301 0.0151  -0.0051 347 VAL A O   
2939 C CB  . VAL A 347 ? 0.1935 0.1879 0.1893 -0.0362 0.0254  0.0081  347 VAL A CB  
2940 C CG1 . VAL A 347 ? 0.2256 0.2095 0.2280 -0.0395 0.0246  0.0108  347 VAL A CG1 
2941 C CG2 . VAL A 347 ? 0.1811 0.1794 0.1682 -0.0382 0.0321  0.0144  347 VAL A CG2 
2942 N N   . PHE A 348 ? 0.1779 0.1822 0.1995 -0.0328 0.0194  -0.0065 348 PHE A N   
2943 C CA  . PHE A 348 ? 0.1897 0.1907 0.2162 -0.0298 0.0142  -0.0092 348 PHE A CA  
2944 C C   . PHE A 348 ? 0.1684 0.1634 0.1971 -0.0337 0.0113  -0.0067 348 PHE A C   
2945 O O   . PHE A 348 ? 0.1898 0.1876 0.2226 -0.0391 0.0134  -0.0057 348 PHE A O   
2946 C CB  . PHE A 348 ? 0.1411 0.1533 0.1776 -0.0262 0.0152  -0.0117 348 PHE A CB  
2947 C CG  . PHE A 348 ? 0.1820 0.1916 0.2159 -0.0186 0.0165  -0.0157 348 PHE A CG  
2948 C CD1 . PHE A 348 ? 0.1843 0.1957 0.2116 -0.0167 0.0215  -0.0184 348 PHE A CD1 
2949 C CD2 . PHE A 348 ? 0.1709 0.1746 0.2078 -0.0134 0.0135  -0.0167 348 PHE A CD2 
2950 C CE1 . PHE A 348 ? 0.1795 0.1848 0.2025 -0.0100 0.0238  -0.0241 348 PHE A CE1 
2951 C CE2 . PHE A 348 ? 0.1958 0.1915 0.2292 -0.0068 0.0160  -0.0208 348 PHE A CE2 
2952 C CZ  . PHE A 348 ? 0.1715 0.1673 0.1979 -0.0051 0.0213  -0.0254 348 PHE A CZ  
2953 N N   . VAL A 349 ? 0.1437 0.1309 0.1694 -0.0317 0.0070  -0.0066 349 VAL A N   
2954 C CA  . VAL A 349 ? 0.1325 0.1143 0.1598 -0.0336 0.0048  -0.0053 349 VAL A CA  
2955 C C   . VAL A 349 ? 0.1428 0.1274 0.1747 -0.0314 0.0011  -0.0074 349 VAL A C   
2956 O O   . VAL A 349 ? 0.1791 0.1606 0.2091 -0.0285 -0.0012 -0.0078 349 VAL A O   
2957 C CB  . VAL A 349 ? 0.1700 0.1442 0.1911 -0.0319 0.0038  -0.0020 349 VAL A CB  
2958 C CG1 . VAL A 349 ? 0.1479 0.1163 0.1704 -0.0323 0.0031  -0.0014 349 VAL A CG1 
2959 C CG2 . VAL A 349 ? 0.2124 0.1839 0.2274 -0.0325 0.0077  0.0024  349 VAL A CG2 
2960 N N   . VAL A 350 ? 0.1255 0.1167 0.1630 -0.0334 0.0005  -0.0084 350 VAL A N   
2961 C CA  . VAL A 350 ? 0.1039 0.1002 0.1452 -0.0302 -0.0028 -0.0085 350 VAL A CA  
2962 C C   . VAL A 350 ? 0.1033 0.1020 0.1448 -0.0338 -0.0047 -0.0093 350 VAL A C   
2963 O O   . VAL A 350 ? 0.1522 0.1565 0.1956 -0.0395 -0.0036 -0.0116 350 VAL A O   
2964 C CB  . VAL A 350 ? 0.1995 0.2081 0.2474 -0.0266 -0.0021 -0.0085 350 VAL A CB  
2965 C CG1 . VAL A 350 ? 0.2051 0.2163 0.2555 -0.0209 -0.0051 -0.0061 350 VAL A CG1 
2966 C CG2 . VAL A 350 ? 0.1704 0.1762 0.2164 -0.0231 0.0016  -0.0096 350 VAL A CG2 
2967 N N   . LEU A 351 ? 0.1615 0.1566 0.2006 -0.0317 -0.0071 -0.0079 351 LEU A N   
2968 C CA  . LEU A 351 ? 0.1462 0.1446 0.1835 -0.0343 -0.0086 -0.0093 351 LEU A CA  
2969 C C   . LEU A 351 ? 0.1759 0.1742 0.2118 -0.0302 -0.0109 -0.0057 351 LEU A C   
2970 O O   . LEU A 351 ? 0.1555 0.1487 0.1920 -0.0268 -0.0110 -0.0028 351 LEU A O   
2971 C CB  . LEU A 351 ? 0.1733 0.1617 0.2059 -0.0380 -0.0057 -0.0121 351 LEU A CB  
2972 C CG  . LEU A 351 ? 0.2001 0.1783 0.2296 -0.0343 -0.0043 -0.0095 351 LEU A CG  
2973 C CD1 . LEU A 351 ? 0.2104 0.1816 0.2355 -0.0342 -0.0017 -0.0113 351 LEU A CD1 
2974 C CD2 . LEU A 351 ? 0.1948 0.1676 0.2238 -0.0338 -0.0021 -0.0077 351 LEU A CD2 
2975 N N   . ASP A 352 ? 0.1554 0.1588 0.1883 -0.0316 -0.0121 -0.0063 352 ASP A N   
2976 C CA  . ASP A 352 ? 0.1463 0.1496 0.1769 -0.0287 -0.0131 -0.0018 352 ASP A CA  
2977 C C   . ASP A 352 ? 0.1503 0.1438 0.1800 -0.0284 -0.0111 -0.0010 352 ASP A C   
2978 O O   . ASP A 352 ? 0.2102 0.1992 0.2387 -0.0296 -0.0090 -0.0039 352 ASP A O   
2979 C CB  . ASP A 352 ? 0.1585 0.1702 0.1838 -0.0307 -0.0140 -0.0032 352 ASP A CB  
2980 C CG  . ASP A 352 ? 0.1657 0.1929 0.1916 -0.0317 -0.0173 -0.0037 352 ASP A CG  
2981 O OD1 . ASP A 352 ? 0.1977 0.2308 0.2298 -0.0293 -0.0189 -0.0014 352 ASP A OD1 
2982 O OD2 . ASP A 352 ? 0.2030 0.2390 0.2228 -0.0348 -0.0184 -0.0066 352 ASP A OD2 
2983 N N   . GLY A 353 ? 0.1358 0.1266 0.1662 -0.0270 -0.0115 0.0035  353 GLY A N   
2984 C CA  . GLY A 353 ? 0.1445 0.1310 0.1755 -0.0283 -0.0104 0.0041  353 GLY A CA  
2985 C C   . GLY A 353 ? 0.1852 0.1768 0.2149 -0.0290 -0.0090 0.0059  353 GLY A C   
2986 O O   . GLY A 353 ? 0.1719 0.1649 0.2039 -0.0300 -0.0082 0.0068  353 GLY A O   
2987 N N   . GLU A 354 ? 0.1726 0.1698 0.1986 -0.0284 -0.0086 0.0064  354 GLU A N   
2988 C CA  . GLU A 354 ? 0.1705 0.1739 0.1947 -0.0287 -0.0062 0.0085  354 GLU A CA  
2989 C C   . GLU A 354 ? 0.1755 0.1833 0.1939 -0.0275 -0.0039 0.0036  354 GLU A C   
2990 O O   . GLU A 354 ? 0.1686 0.1824 0.1847 -0.0266 -0.0007 0.0044  354 GLU A O   
2991 C CB  . GLU A 354 ? 0.1631 0.1689 0.1858 -0.0298 -0.0064 0.0158  354 GLU A CB  
2992 C CG  . GLU A 354 ? 0.1559 0.1678 0.1725 -0.0280 -0.0080 0.0179  354 GLU A CG  
2993 C CD  . GLU A 354 ? 0.1606 0.1696 0.1793 -0.0256 -0.0114 0.0186  354 GLU A CD  
2994 O OE1 . GLU A 354 ? 0.1587 0.1659 0.1770 -0.0230 -0.0122 0.0262  354 GLU A OE1 
2995 O OE2 . GLU A 354 ? 0.1715 0.1799 0.1924 -0.0259 -0.0125 0.0124  354 GLU A OE2 
2996 N N   . ASN A 355 ? 0.1292 0.1340 0.1449 -0.0282 -0.0047 -0.0022 355 ASN A N   
2997 C CA  . ASN A 355 ? 0.1595 0.1668 0.1675 -0.0292 -0.0025 -0.0086 355 ASN A CA  
2998 C C   . ASN A 355 ? 0.2014 0.1980 0.2077 -0.0279 0.0024  -0.0152 355 ASN A C   
2999 O O   . ASN A 355 ? 0.1833 0.1788 0.1819 -0.0280 0.0061  -0.0215 355 ASN A O   
3000 C CB  . ASN A 355 ? 0.1971 0.2107 0.2020 -0.0330 -0.0064 -0.0115 355 ASN A CB  
3001 C CG  . ASN A 355 ? 0.1879 0.2135 0.1919 -0.0316 -0.0101 -0.0038 355 ASN A CG  
3002 O OD1 . ASN A 355 ? 0.1953 0.2257 0.1951 -0.0302 -0.0085 0.0005  355 ASN A OD1 
3003 N ND2 . ASN A 355 ? 0.1651 0.1958 0.1731 -0.0313 -0.0143 -0.0010 355 ASN A ND2 
3004 N N   . CYS A 356 ? 0.2132 0.2011 0.2251 -0.0260 0.0030  -0.0137 356 CYS A N   
3005 C CA  . CYS A 356 ? 0.1836 0.1586 0.1931 -0.0233 0.0082  -0.0179 356 CYS A CA  
3006 C C   . CYS A 356 ? 0.1532 0.1297 0.1654 -0.0154 0.0124  -0.0145 356 CYS A C   
3007 O O   . CYS A 356 ? 0.1533 0.1195 0.1616 -0.0106 0.0185  -0.0181 356 CYS A O   
3008 C CB  . CYS A 356 ? 0.1746 0.1403 0.1873 -0.0248 0.0073  -0.0169 356 CYS A CB  
3009 S SG  . CYS A 356 ? 0.1999 0.1724 0.2207 -0.0227 0.0029  -0.0086 356 CYS A SG  
3010 N N   . TRP A 357 ? 0.1569 0.1462 0.1756 -0.0141 0.0098  -0.0077 357 TRP A N   
3011 C CA  . TRP A 357 ? 0.1849 0.1816 0.2092 -0.0073 0.0127  -0.0033 357 TRP A CA  
3012 C C   . TRP A 357 ? 0.1474 0.1486 0.1686 -0.0021 0.0191  -0.0059 357 TRP A C   
3013 O O   . TRP A 357 ? 0.1882 0.1907 0.2124 0.0067  0.0240  -0.0044 357 TRP A O   
3014 C CB  . TRP A 357 ? 0.1511 0.1619 0.1833 -0.0107 0.0081  0.0031  357 TRP A CB  
3015 C CG  . TRP A 357 ? 0.1423 0.1470 0.1752 -0.0157 0.0029  0.0038  357 TRP A CG  
3016 C CD1 . TRP A 357 ? 0.1872 0.1923 0.2202 -0.0217 -0.0008 0.0048  357 TRP A CD1 
3017 C CD2 . TRP A 357 ? 0.1354 0.1319 0.1682 -0.0142 0.0019  0.0036  357 TRP A CD2 
3018 N NE1 . TRP A 357 ? 0.1415 0.1396 0.1748 -0.0235 -0.0038 0.0041  357 TRP A NE1 
3019 C CE2 . TRP A 357 ? 0.1501 0.1441 0.1830 -0.0197 -0.0024 0.0034  357 TRP A CE2 
3020 C CE3 . TRP A 357 ? 0.1195 0.1094 0.1514 -0.0079 0.0049  0.0044  357 TRP A CE3 
3021 C CZ2 . TRP A 357 ? 0.1555 0.1433 0.1874 -0.0200 -0.0036 0.0031  357 TRP A CZ2 
3022 C CZ3 . TRP A 357 ? 0.1969 0.1799 0.2275 -0.0086 0.0034  0.0056  357 TRP A CZ3 
3023 C CH2 . TRP A 357 ? 0.1669 0.1502 0.1975 -0.0151 -0.0010 0.0045  357 TRP A CH2 
3024 N N   . GLU A 358 ? 0.1431 0.1482 0.1576 -0.0062 0.0196  -0.0094 358 GLU A N   
3025 C CA  . GLU A 358 ? 0.1552 0.1651 0.1642 -0.0015 0.0266  -0.0132 358 GLU A CA  
3026 C C   . GLU A 358 ? 0.1965 0.1889 0.1989 0.0050  0.0338  -0.0212 358 GLU A C   
3027 O O   . GLU A 358 ? 0.1856 0.1804 0.1855 0.0127  0.0415  -0.0239 358 GLU A O   
3028 C CB  . GLU A 358 ? 0.1901 0.2068 0.1899 -0.0079 0.0252  -0.0158 358 GLU A CB  
3029 C CG  . GLU A 358 ? 0.1849 0.1908 0.1757 -0.0143 0.0220  -0.0234 358 GLU A CG  
3030 C CD  . GLU A 358 ? 0.2401 0.2587 0.2258 -0.0205 0.0168  -0.0207 358 GLU A CD  
3031 O OE1 . GLU A 358 ? 0.2991 0.3211 0.2731 -0.0234 0.0177  -0.0277 358 GLU A OE1 
3032 O OE2 . GLU A 358 ? 0.2457 0.2706 0.2383 -0.0221 0.0122  -0.0116 358 GLU A OE2 
3033 N N   . TYR A 359 ? 0.1883 0.1620 0.1877 0.0020  0.0325  -0.0250 359 TYR A N   
3034 C CA  . TYR A 359 ? 0.2293 0.1803 0.2215 0.0066  0.0402  -0.0324 359 TYR A CA  
3035 C C   . TYR A 359 ? 0.2208 0.1642 0.2202 0.0176  0.0437  -0.0254 359 TYR A C   
3036 O O   . TYR A 359 ? 0.2375 0.1596 0.2313 0.0244  0.0519  -0.0294 359 TYR A O   
3037 C CB  . TYR A 359 ? 0.2232 0.1578 0.2083 -0.0039 0.0380  -0.0399 359 TYR A CB  
3038 C CG  . TYR A 359 ? 0.2515 0.1946 0.2278 -0.0136 0.0351  -0.0479 359 TYR A CG  
3039 C CD1 . TYR A 359 ? 0.3233 0.2585 0.2868 -0.0146 0.0416  -0.0596 359 TYR A CD1 
3040 C CD2 . TYR A 359 ? 0.2607 0.2208 0.2407 -0.0208 0.0262  -0.0434 359 TYR A CD2 
3041 C CE1 . TYR A 359 ? 0.3346 0.2817 0.2887 -0.0237 0.0381  -0.0667 359 TYR A CE1 
3042 C CE2 . TYR A 359 ? 0.2641 0.2357 0.2360 -0.0281 0.0230  -0.0488 359 TYR A CE2 
3043 C CZ  . TYR A 359 ? 0.3704 0.3371 0.3291 -0.0299 0.0284  -0.0603 359 TYR A CZ  
3044 O OH  . TYR A 359 ? 0.3373 0.3190 0.2862 -0.0375 0.0246  -0.0657 359 TYR A OH  
3045 N N   . TYR A 360 ? 0.2188 0.1782 0.2294 0.0194  0.0380  -0.0151 360 TYR A N   
3046 C CA  . TYR A 360 ? 0.2463 0.2055 0.2639 0.0303  0.0398  -0.0067 360 TYR A CA  
3047 C C   . TYR A 360 ? 0.1894 0.1679 0.2144 0.0418  0.0441  -0.0021 360 TYR A C   
3048 O O   . TYR A 360 ? 0.2098 0.2085 0.2381 0.0383  0.0428  -0.0022 360 TYR A O   
3049 C CB  . TYR A 360 ? 0.2038 0.1747 0.2290 0.0255  0.0310  0.0012  360 TYR A CB  
3050 C CG  . TYR A 360 ? 0.2151 0.1708 0.2361 0.0176  0.0274  -0.0001 360 TYR A CG  
3051 C CD1 . TYR A 360 ? 0.2228 0.1733 0.2388 0.0062  0.0245  -0.0070 360 TYR A CD1 
3052 C CD2 . TYR A 360 ? 0.2370 0.1883 0.2598 0.0218  0.0265  0.0070  360 TYR A CD2 
3053 C CE1 . TYR A 360 ? 0.1742 0.1153 0.1883 -0.0008 0.0216  -0.0076 360 TYR A CE1 
3054 C CE2 . TYR A 360 ? 0.1850 0.1256 0.2044 0.0145  0.0239  0.0066  360 TYR A CE2 
3055 C CZ  . TYR A 360 ? 0.2000 0.1358 0.2159 0.0032  0.0217  -0.0009 360 TYR A CZ  
3056 O OH  . TYR A 360 ? 0.1880 0.1167 0.2022 -0.0033 0.0199  -0.0006 360 TYR A OH  
3057 N N   . GLU A 361 ? 0.2031 0.1765 0.2312 0.0561  0.0498  0.0032  361 GLU A N   
3058 C CA  . GLU A 361 ? 0.2555 0.2539 0.2946 0.0688  0.0529  0.0103  361 GLU A CA  
3059 C C   . GLU A 361 ? 0.1958 0.2275 0.2470 0.0610  0.0434  0.0172  361 GLU A C   
3060 O O   . GLU A 361 ? 0.2173 0.2513 0.2707 0.0539  0.0352  0.0212  361 GLU A O   
3061 C CB  . GLU A 361 ? 0.3222 0.3124 0.3643 0.0857  0.0577  0.0186  361 GLU A CB  
3062 C CG  . GLU A 361 ? 0.4898 0.5120 0.5461 0.1006  0.0597  0.0282  361 GLU A CG  
3063 C CD  . GLU A 361 ? 0.7277 0.7538 0.7837 0.1106  0.0705  0.0228  361 GLU A CD  
3064 O OE1 . GLU A 361 ? 0.7338 0.7315 0.7760 0.1084  0.0778  0.0113  361 GLU A OE1 
3065 O OE2 . GLU A 361 ? 0.8477 0.9074 0.9173 0.1201  0.0720  0.0297  361 GLU A OE2 
3066 N N   . GLU A 362 ? 0.1943 0.2507 0.2522 0.0612  0.0452  0.0177  362 GLU A N   
3067 C CA  . GLU A 362 ? 0.1855 0.2735 0.2554 0.0527  0.0380  0.0239  362 GLU A CA  
3068 C C   . GLU A 362 ? 0.2166 0.2968 0.2822 0.0357  0.0291  0.0215  362 GLU A C   
3069 O O   . GLU A 362 ? 0.1727 0.2656 0.2450 0.0288  0.0216  0.0260  362 GLU A O   
3070 C CB  . GLU A 362 ? 0.2310 0.3422 0.3139 0.0616  0.0350  0.0338  362 GLU A CB  
3071 C CG  . GLU A 362 ? 0.3799 0.5156 0.4734 0.0770  0.0427  0.0386  362 GLU A CG  
3072 C CD  . GLU A 362 ? 0.4847 0.6488 0.5921 0.0869  0.0388  0.0497  362 GLU A CD  
3073 O OE1 . GLU A 362 ? 0.5481 0.7356 0.6662 0.1020  0.0451  0.0551  362 GLU A OE1 
3074 O OE2 . GLU A 362 ? 0.5007 0.6661 0.6081 0.0801  0.0297  0.0531  362 GLU A OE2 
3075 N N   . ASN A 363 ? 0.1621 0.2216 0.2160 0.0292  0.0302  0.0141  363 ASN A N   
3076 C CA  . ASN A 363 ? 0.1324 0.1856 0.1826 0.0152  0.0231  0.0124  363 ASN A CA  
3077 C C   . ASN A 363 ? 0.1269 0.1710 0.1775 0.0122  0.0168  0.0141  363 ASN A C   
3078 O O   . ASN A 363 ? 0.2108 0.2570 0.2626 0.0025  0.0106  0.0149  363 ASN A O   
3079 C CB  . ASN A 363 ? 0.1913 0.2654 0.2483 0.0063  0.0203  0.0164  363 ASN A CB  
3080 C CG  . ASN A 363 ? 0.2272 0.2907 0.2779 -0.0049 0.0159  0.0146  363 ASN A CG  
3081 O OD1 . ASN A 363 ? 0.1631 0.2113 0.2038 -0.0055 0.0169  0.0095  363 ASN A OD1 
3082 N ND2 . ASN A 363 ? 0.2441 0.3154 0.3004 -0.0141 0.0111  0.0185  363 ASN A ND2 
3083 N N   . GLY A 364 ? 0.1357 0.1683 0.1843 0.0211  0.0193  0.0150  364 GLY A N   
3084 C CA  . GLY A 364 ? 0.1853 0.2096 0.2326 0.0191  0.0145  0.0173  364 GLY A CA  
3085 C C   . GLY A 364 ? 0.2076 0.2531 0.2630 0.0179  0.0084  0.0238  364 GLY A C   
3086 O O   . GLY A 364 ? 0.1623 0.2030 0.2150 0.0148  0.0041  0.0250  364 GLY A O   
3087 N N   . ILE A 365 ? 0.1802 0.2512 0.2454 0.0197  0.0082  0.0276  365 ILE A N   
3088 C CA  . ILE A 365 ? 0.1243 0.2198 0.1976 0.0151  0.0014  0.0322  365 ILE A CA  
3089 C C   . ILE A 365 ? 0.1793 0.2806 0.2536 0.0262  0.0003  0.0389  365 ILE A C   
3090 O O   . ILE A 365 ? 0.1839 0.2906 0.2565 0.0210  -0.0061 0.0403  365 ILE A O   
3091 C CB  . ILE A 365 ? 0.1481 0.2720 0.2328 0.0119  0.0019  0.0343  365 ILE A CB  
3092 C CG1 . ILE A 365 ? 0.1715 0.2867 0.2528 -0.0011 0.0020  0.0293  365 ILE A CG1 
3093 C CG2 . ILE A 365 ? 0.1086 0.2629 0.2031 0.0076  -0.0050 0.0389  365 ILE A CG2 
3094 C CD1 . ILE A 365 ? 0.1691 0.3030 0.2576 -0.0022 0.0067  0.0311  365 ILE A CD1 
3095 N N   . PRO A 366 ? 0.1343 0.2326 0.2095 0.0420  0.0070  0.0435  366 PRO A N   
3096 C CA  . PRO A 366 ? 0.1686 0.2676 0.2426 0.0539  0.0065  0.0520  366 PRO A CA  
3097 C C   . PRO A 366 ? 0.1642 0.2366 0.2260 0.0492  0.0050  0.0503  366 PRO A C   
3098 O O   . PRO A 366 ? 0.2237 0.3043 0.2836 0.0506  0.0003  0.0564  366 PRO A O   
3099 C CB  . PRO A 366 ? 0.1611 0.2512 0.2361 0.0720  0.0166  0.0555  366 PRO A CB  
3100 C CG  . PRO A 366 ? 0.2545 0.3603 0.3372 0.0704  0.0199  0.0513  366 PRO A CG  
3101 C CD  . PRO A 366 ? 0.1534 0.2515 0.2315 0.0512  0.0156  0.0422  366 PRO A CD  
3102 N N   . PHE A 367 ? 0.1604 0.2040 0.2140 0.0433  0.0089  0.0424  367 PHE A N   
3103 C CA  . PHE A 367 ? 0.2076 0.2290 0.2514 0.0379  0.0082  0.0407  367 PHE A CA  
3104 C C   . PHE A 367 ? 0.1945 0.2277 0.2378 0.0256  -0.0002 0.0386  367 PHE A C   
3105 O O   . PHE A 367 ? 0.1734 0.2077 0.2121 0.0258  -0.0030 0.0428  367 PHE A O   
3106 C CB  . PHE A 367 ? 0.2260 0.2199 0.2628 0.0325  0.0134  0.0320  367 PHE A CB  
3107 C CG  . PHE A 367 ? 0.2147 0.1921 0.2442 0.0242  0.0121  0.0294  367 PHE A CG  
3108 C CD1 . PHE A 367 ? 0.2751 0.2368 0.2986 0.0292  0.0159  0.0351  367 PHE A CD1 
3109 C CD2 . PHE A 367 ? 0.1909 0.1696 0.2198 0.0120  0.0077  0.0226  367 PHE A CD2 
3110 C CE1 . PHE A 367 ? 0.2350 0.1849 0.2525 0.0208  0.0154  0.0332  367 PHE A CE1 
3111 C CE2 . PHE A 367 ? 0.2068 0.1745 0.2306 0.0054  0.0071  0.0206  367 PHE A CE2 
3112 C CZ  . PHE A 367 ? 0.1727 0.1273 0.1911 0.0091  0.0109  0.0255  367 PHE A CZ  
3113 N N   . LEU A 368 ? 0.1649 0.2058 0.2118 0.0151  -0.0035 0.0322  368 LEU A N   
3114 C CA  . LEU A 368 ? 0.1324 0.1782 0.1773 0.0036  -0.0099 0.0286  368 LEU A CA  
3115 C C   . LEU A 368 ? 0.1710 0.2426 0.2193 0.0032  -0.0159 0.0330  368 LEU A C   
3116 O O   . LEU A 368 ? 0.1968 0.2694 0.2392 -0.0023 -0.0200 0.0315  368 LEU A O   
3117 C CB  . LEU A 368 ? 0.1114 0.1558 0.1587 -0.0064 -0.0109 0.0220  368 LEU A CB  
3118 C CG  . LEU A 368 ? 0.1363 0.1589 0.1784 -0.0089 -0.0075 0.0168  368 LEU A CG  
3119 C CD1 . LEU A 368 ? 0.2104 0.2349 0.2547 -0.0172 -0.0090 0.0133  368 LEU A CD1 
3120 C CD2 . LEU A 368 ? 0.1866 0.1960 0.2219 -0.0113 -0.0083 0.0150  368 LEU A CD2 
3121 N N   . GLU A 369 ? 0.1207 0.2158 0.1782 0.0084  -0.0166 0.0380  369 GLU A N   
3122 C CA  . GLU A 369 ? 0.1223 0.2476 0.1839 0.0072  -0.0234 0.0423  369 GLU A CA  
3123 C C   . GLU A 369 ? 0.1968 0.3217 0.2511 0.0168  -0.0242 0.0499  369 GLU A C   
3124 O O   . GLU A 369 ? 0.1680 0.3057 0.2172 0.0112  -0.0304 0.0497  369 GLU A O   
3125 C CB  . GLU A 369 ? 0.2047 0.3602 0.2799 0.0122  -0.0235 0.0474  369 GLU A CB  
3126 C CG  . GLU A 369 ? 0.1758 0.3417 0.2581 -0.0023 -0.0251 0.0409  369 GLU A CG  
3127 C CD  . GLU A 369 ? 0.2098 0.4081 0.3068 0.0016  -0.0242 0.0460  369 GLU A CD  
3128 O OE1 . GLU A 369 ? 0.2033 0.4160 0.3058 0.0180  -0.0219 0.0546  369 GLU A OE1 
3129 O OE2 . GLU A 369 ? 0.1975 0.4074 0.3012 -0.0115 -0.0252 0.0421  369 GLU A OE2 
3130 N N   . LYS A 370 ? 0.1573 0.2649 0.2091 0.0306  -0.0174 0.0562  370 LYS A N   
3131 C CA  . LYS A 370 ? 0.1766 0.2801 0.2205 0.0404  -0.0167 0.0656  370 LYS A CA  
3132 C C   . LYS A 370 ? 0.2321 0.3134 0.2636 0.0317  -0.0166 0.0608  370 LYS A C   
3133 O O   . LYS A 370 ? 0.2133 0.3022 0.2370 0.0322  -0.0198 0.0657  370 LYS A O   
3134 C CB  . LYS A 370 ? 0.2482 0.3349 0.2927 0.0575  -0.0078 0.0738  370 LYS A CB  
3135 C CG  . LYS A 370 ? 0.3477 0.4304 0.3846 0.0702  -0.0060 0.0870  370 LYS A CG  
3136 C CD  . LYS A 370 ? 0.5069 0.5635 0.5430 0.0862  0.0049  0.0935  370 LYS A CD  
3137 C CE  . LYS A 370 ? 0.5490 0.6246 0.5980 0.0986  0.0073  0.0965  370 LYS A CE  
3138 N NZ  . LYS A 370 ? 0.5589 0.6749 0.6153 0.1095  0.0009  0.1093  370 LYS A NZ  
3139 N N   . LEU A 371 ? 0.1602 0.2171 0.1897 0.0239  -0.0127 0.0516  371 LEU A N   
3140 C CA  . LEU A 371 ? 0.1721 0.2120 0.1922 0.0159  -0.0121 0.0468  371 LEU A CA  
3141 C C   . LEU A 371 ? 0.1854 0.2421 0.2023 0.0060  -0.0193 0.0419  371 LEU A C   
3142 O O   . LEU A 371 ? 0.2176 0.2759 0.2252 0.0052  -0.0205 0.0441  371 LEU A O   
3143 C CB  . LEU A 371 ? 0.1790 0.1973 0.2001 0.0093  -0.0081 0.0378  371 LEU A CB  
3144 C CG  . LEU A 371 ? 0.1841 0.1902 0.1985 0.0009  -0.0076 0.0323  371 LEU A CG  
3145 C CD1 . LEU A 371 ? 0.2918 0.2857 0.2984 0.0056  -0.0029 0.0393  371 LEU A CD1 
3146 C CD2 . LEU A 371 ? 0.1779 0.1702 0.1951 -0.0053 -0.0053 0.0239  371 LEU A CD2 
3147 N N   . TYR A 372 ? 0.2147 0.2831 0.2380 -0.0022 -0.0234 0.0349  372 TYR A N   
3148 C CA  . TYR A 372 ? 0.1746 0.2538 0.1939 -0.0135 -0.0291 0.0276  372 TYR A CA  
3149 C C   . TYR A 372 ? 0.2266 0.3333 0.2427 -0.0117 -0.0352 0.0330  372 TYR A C   
3150 O O   . TYR A 372 ? 0.1856 0.2965 0.1915 -0.0177 -0.0382 0.0290  372 TYR A O   
3151 C CB  . TYR A 372 ? 0.1401 0.2224 0.1671 -0.0232 -0.0309 0.0201  372 TYR A CB  
3152 C CG  . TYR A 372 ? 0.1885 0.2461 0.2164 -0.0260 -0.0261 0.0146  372 TYR A CG  
3153 C CD1 . TYR A 372 ? 0.1628 0.2001 0.1848 -0.0235 -0.0220 0.0134  372 TYR A CD1 
3154 C CD2 . TYR A 372 ? 0.1255 0.1834 0.1605 -0.0314 -0.0259 0.0115  372 TYR A CD2 
3155 C CE1 . TYR A 372 ? 0.1694 0.1899 0.1930 -0.0259 -0.0187 0.0089  372 TYR A CE1 
3156 C CE2 . TYR A 372 ? 0.1230 0.1614 0.1580 -0.0331 -0.0222 0.0080  372 TYR A CE2 
3157 C CZ  . TYR A 372 ? 0.1511 0.1725 0.1807 -0.0300 -0.0192 0.0066  372 TYR A CZ  
3158 O OH  . TYR A 372 ? 0.1679 0.1754 0.1981 -0.0312 -0.0165 0.0038  372 TYR A OH  
3159 N N   . SER A 373 ? 0.1963 0.3237 0.2204 -0.0028 -0.0368 0.0423  373 SER A N   
3160 C CA  . SER A 373 ? 0.1545 0.3129 0.1761 0.0007  -0.0432 0.0495  373 SER A CA  
3161 C C   . SER A 373 ? 0.1668 0.3169 0.1751 0.0086  -0.0413 0.0573  373 SER A C   
3162 O O   . SER A 373 ? 0.2225 0.3924 0.2218 0.0058  -0.0470 0.0586  373 SER A O   
3163 C CB  . SER A 373 ? 0.1696 0.3527 0.2042 0.0124  -0.0441 0.0600  373 SER A CB  
3164 O OG  . SER A 373 ? 0.2710 0.4866 0.3034 0.0181  -0.0506 0.0692  373 SER A OG  
3165 N N   . THR A 374 ? 0.2254 0.3475 0.2317 0.0177  -0.0330 0.0629  374 THR A N   
3166 C CA  . THR A 374 ? 0.2341 0.3460 0.2279 0.0246  -0.0296 0.0720  374 THR A CA  
3167 C C   . THR A 374 ? 0.2293 0.3288 0.2117 0.0131  -0.0289 0.0625  374 THR A C   
3168 O O   . THR A 374 ? 0.2498 0.3578 0.2198 0.0134  -0.0304 0.0668  374 THR A O   
3169 C CB  . THR A 374 ? 0.2934 0.3765 0.2886 0.0359  -0.0200 0.0800  374 THR A CB  
3170 O OG1 . THR A 374 ? 0.2668 0.3589 0.2728 0.0479  -0.0190 0.0873  374 THR A OG1 
3171 C CG2 . THR A 374 ? 0.3122 0.3853 0.2950 0.0433  -0.0157 0.0923  374 THR A CG2 
3172 N N   . LEU A 375 ? 0.2282 0.3096 0.2143 0.0038  -0.0264 0.0502  375 LEU A N   
3173 C CA  . LEU A 375 ? 0.2177 0.2886 0.1949 -0.0054 -0.0249 0.0409  375 LEU A CA  
3174 C C   . LEU A 375 ? 0.2995 0.3923 0.2682 -0.0129 -0.0318 0.0347  375 LEU A C   
3175 O O   . LEU A 375 ? 0.3011 0.3957 0.2567 -0.0145 -0.0309 0.0342  375 LEU A O   
3176 C CB  . LEU A 375 ? 0.1811 0.2342 0.1657 -0.0124 -0.0223 0.0297  375 LEU A CB  
3177 C CG  . LEU A 375 ? 0.2485 0.2786 0.2373 -0.0086 -0.0151 0.0323  375 LEU A CG  
3178 C CD1 . LEU A 375 ? 0.2735 0.2936 0.2691 -0.0154 -0.0146 0.0218  375 LEU A CD1 
3179 C CD2 . LEU A 375 ? 0.3052 0.3251 0.2849 -0.0079 -0.0097 0.0360  375 LEU A CD2 
3180 N N   . GLU A 376 ? 0.2434 0.3541 0.2187 -0.0185 -0.0383 0.0296  376 GLU A N   
3181 C CA  . GLU A 376 ? 0.2842 0.4132 0.2509 -0.0292 -0.0447 0.0203  376 GLU A CA  
3182 C C   . GLU A 376 ? 0.2886 0.4438 0.2439 -0.0247 -0.0495 0.0288  376 GLU A C   
3183 O O   . GLU A 376 ? 0.3129 0.4835 0.2572 -0.0341 -0.0544 0.0202  376 GLU A O   
3184 C CB  . GLU A 376 ? 0.2613 0.4045 0.2387 -0.0384 -0.0503 0.0133  376 GLU A CB  
3185 C CG  . GLU A 376 ? 0.2883 0.4641 0.2746 -0.0328 -0.0564 0.0238  376 GLU A CG  
3186 C CD  . GLU A 376 ? 0.3478 0.5370 0.3475 -0.0427 -0.0602 0.0176  376 GLU A CD  
3187 O OE1 . GLU A 376 ? 0.3157 0.5317 0.3267 -0.0370 -0.0637 0.0264  376 GLU A OE1 
3188 O OE2 . GLU A 376 ? 0.4256 0.5986 0.4248 -0.0556 -0.0589 0.0047  376 GLU A OE2 
3189 N N   . LYS A 377 ? 0.3031 0.4623 0.2593 -0.0106 -0.0476 0.0455  377 LYS A N   
3190 C CA  . LYS A 377 ? 0.3283 0.5143 0.2741 -0.0037 -0.0523 0.0573  377 LYS A CA  
3191 C C   . LYS A 377 ? 0.3141 0.4849 0.2456 0.0031  -0.0456 0.0663  377 LYS A C   
3192 O O   . LYS A 377 ? 0.3616 0.5522 0.2825 0.0105  -0.0483 0.0788  377 LYS A O   
3193 C CB  . LYS A 377 ? 0.3232 0.5296 0.2810 0.0095  -0.0554 0.0724  377 LYS A CB  
3194 C CG  . LYS A 377 ? 0.3572 0.5905 0.3287 0.0021  -0.0632 0.0656  377 LYS A CG  
3195 C CD  . LYS A 377 ? 0.3927 0.6412 0.3798 0.0176  -0.0631 0.0802  377 LYS A CD  
3196 C CE  . LYS A 377 ? 0.2920 0.5653 0.2941 0.0090  -0.0677 0.0723  377 LYS A CE  
3197 N NZ  . LYS A 377 ? 0.2669 0.5262 0.2762 -0.0048 -0.0676 0.0586  377 LYS A NZ  
3198 N N   . GLU A 378 ? 0.2867 0.4253 0.2178 0.0007  -0.0368 0.0613  378 GLU A N   
3199 C CA  . GLU A 378 ? 0.3166 0.4413 0.2352 0.0045  -0.0293 0.0689  378 GLU A CA  
3200 C C   . GLU A 378 ? 0.3203 0.4498 0.2247 -0.0061 -0.0295 0.0560  378 GLU A C   
3201 O O   . GLU A 378 ? 0.3282 0.4451 0.2365 -0.0151 -0.0279 0.0404  378 GLU A O   
3202 C CB  . GLU A 378 ? 0.2909 0.3818 0.2179 0.0065  -0.0195 0.0702  378 GLU A CB  
3203 C CG  . GLU A 378 ? 0.3180 0.3992 0.2572 0.0163  -0.0176 0.0801  378 GLU A CG  
3204 C CD  . GLU A 378 ? 0.4025 0.4831 0.3348 0.0295  -0.0141 0.1001  378 GLU A CD  
3205 O OE1 . GLU A 378 ? 0.4837 0.5781 0.4014 0.0311  -0.0152 0.1077  378 GLU A OE1 
3206 O OE2 . GLU A 378 ? 0.5085 0.5728 0.4488 0.0387  -0.0094 0.1083  378 GLU A OE2 
3207 N N   . GLU A 379 ? 0.3779 0.5252 0.2650 -0.0042 -0.0309 0.0627  379 GLU A N   
3208 C CA  . GLU A 379 ? 0.3366 0.4909 0.2084 -0.0142 -0.0311 0.0485  379 GLU A CA  
3209 C C   . GLU A 379 ? 0.3604 0.4891 0.2300 -0.0163 -0.0198 0.0437  379 GLU A C   
3210 O O   . GLU A 379 ? 0.3559 0.4829 0.2177 -0.0241 -0.0177 0.0284  379 GLU A O   
3211 C CB  . GLU A 379 ? 0.4398 0.6242 0.2917 -0.0117 -0.0360 0.0569  379 GLU A CB  
3212 C CG  . GLU A 379 ? 0.5661 0.7453 0.4149 0.0024  -0.0302 0.0819  379 GLU A CG  
3213 C CD  . GLU A 379 ? 0.8379 1.0317 0.6697 0.0055  -0.0294 0.0896  379 GLU A CD  
3214 O OE1 . GLU A 379 ? 0.8625 1.0420 0.6858 0.0092  -0.0200 0.0998  379 GLU A OE1 
3215 O OE2 . GLU A 379 ? 0.8205 1.0380 0.6500 0.0038  -0.0375 0.0853  379 GLU A OE2 
3216 N N   . TRP A 380 ? 0.3481 0.4575 0.2245 -0.0098 -0.0120 0.0562  380 TRP A N   
3217 C CA  . TRP A 380 ? 0.3084 0.3991 0.1845 -0.0129 -0.0015 0.0528  380 TRP A CA  
3218 C C   . TRP A 380 ? 0.2987 0.3697 0.1923 -0.0171 0.0009  0.0409  380 TRP A C   
3219 O O   . TRP A 380 ? 0.2925 0.3510 0.1891 -0.0195 0.0090  0.0379  380 TRP A O   
3220 C CB  . TRP A 380 ? 0.3516 0.4314 0.2250 -0.0066 0.0066  0.0716  380 TRP A CB  
3221 C CG  . TRP A 380 ? 0.3005 0.3694 0.1849 0.0012  0.0054  0.0843  380 TRP A CG  
3222 C CD1 . TRP A 380 ? 0.3468 0.4288 0.2280 0.0106  -0.0002 0.0978  380 TRP A CD1 
3223 C CD2 . TRP A 380 ? 0.3301 0.3742 0.2306 0.0010  0.0102  0.0837  380 TRP A CD2 
3224 N NE1 . TRP A 380 ? 0.3005 0.3645 0.1948 0.0175  0.0020  0.1057  380 TRP A NE1 
3225 C CE2 . TRP A 380 ? 0.3096 0.3493 0.2147 0.0108  0.0085  0.0965  380 TRP A CE2 
3226 C CE3 . TRP A 380 ? 0.2693 0.2959 0.1800 -0.0061 0.0160  0.0739  380 TRP A CE3 
3227 C CZ2 . TRP A 380 ? 0.3150 0.3308 0.2331 0.0129  0.0128  0.0978  380 TRP A CZ2 
3228 C CZ3 . TRP A 380 ? 0.3412 0.3471 0.2650 -0.0051 0.0190  0.0757  380 TRP A CZ3 
3229 C CH2 . TRP A 380 ? 0.2944 0.2937 0.2208 0.0039  0.0178  0.0867  380 TRP A CH2 
3230 N N   . ILE A 381 ? 0.2331 0.3035 0.1383 -0.0180 -0.0057 0.0350  381 ILE A N   
3231 C CA  . ILE A 381 ? 0.2160 0.2702 0.1360 -0.0217 -0.0044 0.0243  381 ILE A CA  
3232 C C   . ILE A 381 ? 0.3003 0.3603 0.2180 -0.0284 -0.0093 0.0085  381 ILE A C   
3233 O O   . ILE A 381 ? 0.3100 0.3859 0.2236 -0.0308 -0.0169 0.0068  381 ILE A O   
3234 C CB  . ILE A 381 ? 0.2358 0.2817 0.1704 -0.0178 -0.0065 0.0305  381 ILE A CB  
3235 C CG1 . ILE A 381 ? 0.2967 0.3296 0.2331 -0.0122 0.0001  0.0440  381 ILE A CG1 
3236 C CG2 . ILE A 381 ? 0.2053 0.2384 0.1532 -0.0220 -0.0064 0.0194  381 ILE A CG2 
3237 C CD1 . ILE A 381 ? 0.2793 0.3058 0.2259 -0.0058 -0.0015 0.0517  381 ILE A CD1 
3238 N N   . GLU A 382 ? 0.2211 0.2685 0.1420 -0.0317 -0.0046 -0.0029 382 GLU A N   
3239 C CA  . GLU A 382 ? 0.2560 0.3003 0.1766 -0.0377 -0.0074 -0.0179 382 GLU A CA  
3240 C C   . GLU A 382 ? 0.2654 0.2921 0.2020 -0.0370 -0.0051 -0.0209 382 GLU A C   
3241 O O   . GLU A 382 ? 0.2470 0.2647 0.1883 -0.0340 0.0015  -0.0211 382 GLU A O   
3242 C CB  . GLU A 382 ? 0.2691 0.3145 0.1748 -0.0404 -0.0030 -0.0294 382 GLU A CB  
3243 C CG  . GLU A 382 ? 0.2657 0.2995 0.1717 -0.0459 -0.0036 -0.0453 382 GLU A CG  
3244 C CD  . GLU A 382 ? 0.4346 0.4675 0.3238 -0.0487 0.0010  -0.0591 382 GLU A CD  
3245 O OE1 . GLU A 382 ? 0.4845 0.5291 0.3609 -0.0465 0.0045  -0.0566 382 GLU A OE1 
3246 O OE2 . GLU A 382 ? 0.4827 0.5012 0.3707 -0.0531 0.0019  -0.0728 382 GLU A OE2 
3247 N N   . THR A 383 ? 0.1960 0.2210 0.1414 -0.0396 -0.0106 -0.0220 383 THR A N   
3248 C CA  . THR A 383 ? 0.1797 0.1894 0.1378 -0.0392 -0.0087 -0.0249 383 THR A CA  
3249 C C   . THR A 383 ? 0.1899 0.1881 0.1438 -0.0422 -0.0057 -0.0379 383 THR A C   
3250 O O   . THR A 383 ? 0.2425 0.2434 0.1854 -0.0479 -0.0075 -0.0468 383 THR A O   
3251 C CB  . THR A 383 ? 0.1856 0.1972 0.1537 -0.0409 -0.0142 -0.0214 383 THR A CB  
3252 O OG1 . THR A 383 ? 0.1986 0.2207 0.1617 -0.0481 -0.0201 -0.0267 383 THR A OG1 
3253 C CG2 . THR A 383 ? 0.2237 0.2416 0.1970 -0.0351 -0.0149 -0.0088 383 THR A CG2 
3254 N N   . LEU A 384 ? 0.1905 0.1758 0.1528 -0.0382 -0.0009 -0.0391 384 LEU A N   
3255 C CA  . LEU A 384 ? 0.2309 0.2029 0.1897 -0.0375 0.0040  -0.0497 384 LEU A CA  
3256 C C   . LEU A 384 ? 0.2168 0.1741 0.1863 -0.0364 0.0039  -0.0499 384 LEU A C   
3257 O O   . LEU A 384 ? 0.2033 0.1625 0.1841 -0.0338 0.0023  -0.0416 384 LEU A O   
3258 C CB  . LEU A 384 ? 0.2670 0.2403 0.2256 -0.0304 0.0116  -0.0499 384 LEU A CB  
3259 C CG  . LEU A 384 ? 0.2587 0.2452 0.2054 -0.0305 0.0143  -0.0493 384 LEU A CG  
3260 C CD1 . LEU A 384 ? 0.2565 0.2447 0.2059 -0.0237 0.0234  -0.0503 384 LEU A CD1 
3261 C CD2 . LEU A 384 ? 0.2598 0.2474 0.1898 -0.0363 0.0125  -0.0595 384 LEU A CD2 
3262 N N   . THR A 385 ? 0.2378 0.1789 0.2021 -0.0386 0.0064  -0.0596 385 THR A N   
3263 C CA  . THR A 385 ? 0.2130 0.1372 0.1858 -0.0344 0.0092  -0.0587 385 THR A CA  
3264 C C   . THR A 385 ? 0.2221 0.1463 0.2009 -0.0228 0.0155  -0.0561 385 THR A C   
3265 O O   . THR A 385 ? 0.2316 0.1651 0.2062 -0.0192 0.0194  -0.0582 385 THR A O   
3266 C CB  . THR A 385 ? 0.2385 0.1406 0.2032 -0.0395 0.0118  -0.0694 385 THR A CB  
3267 O OG1 . THR A 385 ? 0.2590 0.1533 0.2128 -0.0357 0.0187  -0.0797 385 THR A OG1 
3268 C CG2 . THR A 385 ? 0.2631 0.1697 0.2219 -0.0536 0.0054  -0.0736 385 THR A CG2 
3269 N N   . LEU A 386 ? 0.2067 0.1233 0.1957 -0.0168 0.0165  -0.0508 386 LEU A N   
3270 C CA  . LEU A 386 ? 0.2243 0.1436 0.2203 -0.0049 0.0223  -0.0485 386 LEU A CA  
3271 C C   . LEU A 386 ? 0.2316 0.1392 0.2187 0.0005  0.0304  -0.0586 386 LEU A C   
3272 O O   . LEU A 386 ? 0.2902 0.2094 0.2795 0.0082  0.0358  -0.0591 386 LEU A O   
3273 C CB  . LEU A 386 ? 0.2355 0.1482 0.2418 0.0013  0.0217  -0.0410 386 LEU A CB  
3274 C CG  . LEU A 386 ? 0.1845 0.1075 0.1983 -0.0034 0.0147  -0.0320 386 LEU A CG  
3275 C CD1 . LEU A 386 ? 0.1853 0.1044 0.2073 0.0039  0.0147  -0.0242 386 LEU A CD1 
3276 C CD2 . LEU A 386 ? 0.1876 0.1329 0.2062 -0.0052 0.0124  -0.0284 386 LEU A CD2 
3277 N N   . GLU A 387 ? 0.2811 0.1658 0.2578 -0.0040 0.0322  -0.0675 387 GLU A N   
3278 C CA  . GLU A 387 ? 0.2867 0.1564 0.2522 0.0006  0.0408  -0.0796 387 GLU A CA  
3279 C C   . GLU A 387 ? 0.2822 0.1695 0.2379 -0.0023 0.0421  -0.0857 387 GLU A C   
3280 O O   . GLU A 387 ? 0.3117 0.2020 0.2647 0.0069  0.0504  -0.0902 387 GLU A O   
3281 C CB  . GLU A 387 ? 0.3094 0.1500 0.2637 -0.0081 0.0418  -0.0896 387 GLU A CB  
3282 C CG  . GLU A 387 ? 0.4305 0.2523 0.3691 -0.0063 0.0509  -0.1055 387 GLU A CG  
3283 C CD  . GLU A 387 ? 0.7418 0.5369 0.6828 0.0065  0.0591  -0.1055 387 GLU A CD  
3284 O OE1 . GLU A 387 ? 0.7551 0.5524 0.7099 0.0201  0.0622  -0.0948 387 GLU A OE1 
3285 O OE2 . GLU A 387 ? 0.9247 0.7013 0.8553 0.0037  0.0610  -0.1141 387 GLU A OE2 
3286 N N   . GLU A 388 ? 0.2997 0.2006 0.2501 -0.0140 0.0346  -0.0846 388 GLU A N   
3287 C CA  . GLU A 388 ? 0.3211 0.2398 0.2609 -0.0165 0.0355  -0.0879 388 GLU A CA  
3288 C C   . GLU A 388 ? 0.2666 0.2056 0.2162 -0.0084 0.0386  -0.0785 388 GLU A C   
3289 O O   . GLU A 388 ? 0.3427 0.2911 0.2854 -0.0046 0.0452  -0.0823 388 GLU A O   
3290 C CB  . GLU A 388 ? 0.2888 0.2193 0.2220 -0.0289 0.0262  -0.0862 388 GLU A CB  
3291 C CG  . GLU A 388 ? 0.3642 0.2805 0.2850 -0.0399 0.0236  -0.0986 388 GLU A CG  
3292 C CD  . GLU A 388 ? 0.4808 0.4113 0.4013 -0.0516 0.0129  -0.0945 388 GLU A CD  
3293 O OE1 . GLU A 388 ? 0.3268 0.2726 0.2582 -0.0499 0.0078  -0.0814 388 GLU A OE1 
3294 O OE2 . GLU A 388 ? 0.5537 0.4807 0.4630 -0.0629 0.0101  -0.1053 388 GLU A OE2 
3295 N N   . ALA A 389 ? 0.2493 0.1962 0.2146 -0.0068 0.0346  -0.0667 389 ALA A N   
3296 C CA  . ALA A 389 ? 0.2903 0.2567 0.2655 -0.0020 0.0375  -0.0586 389 ALA A CA  
3297 C C   . ALA A 389 ? 0.3730 0.3407 0.3542 0.0098  0.0466  -0.0616 389 ALA A C   
3298 O O   . ALA A 389 ? 0.3098 0.2950 0.2931 0.0131  0.0523  -0.0601 389 ALA A O   
3299 C CB  . ALA A 389 ? 0.2371 0.2100 0.2262 -0.0042 0.0312  -0.0477 389 ALA A CB  
3300 N N   . MET A 390 ? 0.3183 0.2675 0.3017 0.0168  0.0488  -0.0655 390 MET A N   
3301 C CA  . MET A 390 ? 0.3519 0.3017 0.3420 0.0311  0.0580  -0.0673 390 MET A CA  
3302 C C   . MET A 390 ? 0.3287 0.2754 0.3045 0.0347  0.0674  -0.0792 390 MET A C   
3303 O O   . MET A 390 ? 0.3849 0.3465 0.3663 0.0448  0.0758  -0.0792 390 MET A O   
3304 C CB  . MET A 390 ? 0.3421 0.2690 0.3368 0.0388  0.0584  -0.0667 390 MET A CB  
3305 C CG  . MET A 390 ? 0.5332 0.4644 0.5390 0.0569  0.0668  -0.0642 390 MET A CG  
3306 S SD  . MET A 390 ? 0.5996 0.4970 0.6064 0.0685  0.0701  -0.0632 390 MET A SD  
3307 C CE  . MET A 390 ? 0.5854 0.4456 0.5684 0.0628  0.0769  -0.0815 390 MET A CE  
3308 N N   . ARG A 391 ? 0.3153 0.2453 0.2726 0.0259  0.0663  -0.0897 391 ARG A N   
3309 C CA  . ARG A 391 ? 0.3595 0.2812 0.2997 0.0288  0.0755  -0.1040 391 ARG A CA  
3310 C C   . ARG A 391 ? 0.4265 0.3692 0.3538 0.0210  0.0755  -0.1060 391 ARG A C   
3311 O O   . ARG A 391 ? 0.4061 0.3495 0.3201 0.0251  0.0847  -0.1165 391 ARG A O   
3312 C CB  . ARG A 391 ? 0.4866 0.3755 0.4120 0.0226  0.0750  -0.1168 391 ARG A CB  
3313 C CG  . ARG A 391 ? 0.5729 0.4331 0.5051 0.0333  0.0802  -0.1179 391 ARG A CG  
3314 C CD  . ARG A 391 ? 0.7291 0.5567 0.6479 0.0224  0.0779  -0.1283 391 ARG A CD  
3315 N NE  . ARG A 391 ? 0.9033 0.7322 0.8020 0.0114  0.0762  -0.1411 391 ARG A NE  
3316 C CZ  . ARG A 391 ? 0.9158 0.7527 0.8060 -0.0059 0.0666  -0.1435 391 ARG A CZ  
3317 N NH1 . ARG A 391 ? 0.8087 0.6520 0.7084 -0.0141 0.0583  -0.1345 391 ARG A NH1 
3318 N NH2 . ARG A 391 ? 0.8923 0.7334 0.7646 -0.0143 0.0650  -0.1543 391 ARG A NH2 
3319 N N   . LYS A 392 ? 0.3840 0.3428 0.3139 0.0110  0.0663  -0.0958 392 LYS A N   
3320 C CA  . LYS A 392 ? 0.4072 0.3840 0.3234 0.0035  0.0654  -0.0951 392 LYS A CA  
3321 C C   . LYS A 392 ? 0.4137 0.4083 0.3285 0.0111  0.0766  -0.0955 392 LYS A C   
3322 O O   . LYS A 392 ? 0.3797 0.3873 0.3121 0.0179  0.0805  -0.0870 392 LYS A O   
3323 C CB  . LYS A 392 ? 0.4300 0.4200 0.3546 -0.0040 0.0560  -0.0804 392 LYS A CB  
3324 C CG  . LYS A 392 ? 0.5257 0.5239 0.4341 -0.0139 0.0498  -0.0793 392 LYS A CG  
3325 C CD  . LYS A 392 ? 0.5811 0.5648 0.4799 -0.0211 0.0427  -0.0888 392 LYS A CD  
3326 C CE  . LYS A 392 ? 0.6171 0.6138 0.5092 -0.0300 0.0329  -0.0818 392 LYS A CE  
3327 N NZ  . LYS A 392 ? 0.7047 0.7024 0.5761 -0.0380 0.0299  -0.0943 392 LYS A NZ  
3328 N N   . GLU A 393 ? 0.4195 0.4174 0.3130 0.0090  0.0817  -0.1054 393 GLU A N   
3329 C CA  . GLU A 393 ? 0.4060 0.4220 0.2963 0.0161  0.0936  -0.1065 393 GLU A CA  
3330 C C   . GLU A 393 ? 0.4168 0.4586 0.3070 0.0099  0.0926  -0.0926 393 GLU A C   
3331 O O   . GLU A 393 ? 0.4408 0.5014 0.3407 0.0149  0.1012  -0.0864 393 GLU A O   
3332 C CB  . GLU A 393 ? 0.4858 0.4932 0.3511 0.0174  0.1013  -0.1247 393 GLU A CB  
3333 C CG  . GLU A 393 ? 0.6407 0.6179 0.5053 0.0247  0.1057  -0.1393 393 GLU A CG  
3334 C CD  . GLU A 393 ? 0.7736 0.7394 0.6152 0.0273  0.1123  -0.1555 393 GLU A CD  
3335 O OE1 . GLU A 393 ? 0.8753 0.8575 0.6992 0.0221  0.1125  -0.1567 393 GLU A OE1 
3336 O OE2 . GLU A 393 ? 0.8819 0.8216 0.7241 0.0352  0.1150  -0.1640 393 GLU A OE2 
3337 N N   . ASP A 394 ? 0.3481 0.3919 0.2287 -0.0006 0.0829  -0.0865 394 ASP A N   
3338 C CA  . ASP A 394 ? 0.3669 0.4310 0.2435 -0.0057 0.0832  -0.0726 394 ASP A CA  
3339 C C   . ASP A 394 ? 0.4498 0.5177 0.3485 -0.0079 0.0794  -0.0567 394 ASP A C   
3340 O O   . ASP A 394 ? 0.4502 0.5215 0.3468 -0.0143 0.0737  -0.0447 394 ASP A O   
3341 C CB  . ASP A 394 ? 0.5081 0.5743 0.3630 -0.0138 0.0753  -0.0723 394 ASP A CB  
3342 C CG  . ASP A 394 ? 0.6442 0.6949 0.5017 -0.0186 0.0628  -0.0752 394 ASP A CG  
3343 O OD1 . ASP A 394 ? 0.7171 0.7518 0.5896 -0.0156 0.0616  -0.0797 394 ASP A OD1 
3344 O OD2 . ASP A 394 ? 0.6292 0.6857 0.4742 -0.0251 0.0544  -0.0721 394 ASP A OD2 
3345 N N   . VAL A 395 ? 0.3455 0.4129 0.2648 -0.0021 0.0828  -0.0567 395 VAL A N   
3346 C CA  . VAL A 395 ? 0.3933 0.4645 0.3342 -0.0045 0.0794  -0.0450 395 VAL A CA  
3347 C C   . VAL A 395 ? 0.4168 0.5088 0.3710 -0.0008 0.0900  -0.0418 395 VAL A C   
3348 O O   . VAL A 395 ? 0.4395 0.5393 0.3900 0.0071  0.0994  -0.0501 395 VAL A O   
3349 C CB  . VAL A 395 ? 0.4044 0.4588 0.3577 -0.0016 0.0717  -0.0485 395 VAL A CB  
3350 C CG1 . VAL A 395 ? 0.5599 0.6221 0.5364 -0.0009 0.0708  -0.0406 395 VAL A CG1 
3351 C CG2 . VAL A 395 ? 0.3457 0.3857 0.2902 -0.0083 0.0609  -0.0472 395 VAL A CG2 
3352 N N   . LYS A 396 ? 0.2466 0.3488 0.2159 -0.0072 0.0893  -0.0304 396 LYS A N   
3353 C CA  . LYS A 396 ? 0.3045 0.4308 0.2890 -0.0063 0.0986  -0.0268 396 LYS A CA  
3354 C C   . LYS A 396 ? 0.2621 0.3931 0.2695 -0.0003 0.0959  -0.0285 396 LYS A C   
3355 O O   . LYS A 396 ? 0.2362 0.3520 0.2489 -0.0012 0.0862  -0.0281 396 LYS A O   
3356 C CB  . LYS A 396 ? 0.2648 0.4009 0.2520 -0.0189 0.1007  -0.0139 396 LYS A CB  
3357 C CG  . LYS A 396 ? 0.2768 0.4104 0.2409 -0.0235 0.1041  -0.0090 396 LYS A CG  
3358 C CD  . LYS A 396 ? 0.3744 0.5216 0.3249 -0.0165 0.1143  -0.0165 396 LYS A CD  
3359 C CE  . LYS A 396 ? 0.4356 0.5811 0.3599 -0.0207 0.1159  -0.0116 396 LYS A CE  
3360 N NZ  . LYS A 396 ? 0.4866 0.6460 0.3949 -0.0145 0.1262  -0.0202 396 LYS A NZ  
3361 N N   . THR A 397 ? 0.2785 0.3911 0.2019 0.0088  0.0093  0.0625  397 THR A N   
3362 C CA  . THR A 397 ? 0.2644 0.3799 0.2044 0.0060  0.0137  0.0534  397 THR A CA  
3363 C C   . THR A 397 ? 0.2690 0.3848 0.2121 -0.0019 0.0216  0.0611  397 THR A C   
3364 O O   . THR A 397 ? 0.2894 0.4087 0.2202 -0.0058 0.0255  0.0713  397 THR A O   
3365 C CB  . THR A 397 ? 0.4571 0.5873 0.3950 0.0099  0.0151  0.0404  397 THR A CB  
3366 O OG1 . THR A 397 ? 0.4043 0.5324 0.3461 0.0143  0.0075  0.0310  397 THR A OG1 
3367 C CG2 . THR A 397 ? 0.6375 0.7735 0.5857 0.0080  0.0220  0.0341  397 THR A CG2 
3368 N N   . GLU A 398 ? 0.2307 0.3440 0.1902 -0.0048 0.0238  0.0568  398 GLU A N   
3369 C CA  . GLU A 398 ? 0.2852 0.4016 0.2501 -0.0131 0.0305  0.0631  398 GLU A CA  
3370 C C   . GLU A 398 ? 0.2621 0.3845 0.2440 -0.0128 0.0331  0.0538  398 GLU A C   
3371 O O   . GLU A 398 ? 0.2339 0.3492 0.2243 -0.0086 0.0287  0.0457  398 GLU A O   
3372 C CB  . GLU A 398 ? 0.3086 0.4064 0.2725 -0.0196 0.0283  0.0745  398 GLU A CB  
3373 C CG  . GLU A 398 ? 0.4576 0.5598 0.4246 -0.0308 0.0350  0.0823  398 GLU A CG  
3374 C CD  . GLU A 398 ? 0.6348 0.7567 0.5915 -0.0340 0.0423  0.0873  398 GLU A CD  
3375 O OE1 . GLU A 398 ? 0.7103 0.8261 0.6514 -0.0380 0.0427  0.0988  398 GLU A OE1 
3376 O OE2 . GLU A 398 ? 0.6151 0.7583 0.5783 -0.0317 0.0477  0.0798  398 GLU A OE2 
3377 N N   . VAL A 399 ? 0.2393 0.3761 0.2259 -0.0173 0.0403  0.0555  399 VAL A N   
3378 C CA  . VAL A 399 ? 0.2862 0.4303 0.2885 -0.0164 0.0427  0.0482  399 VAL A CA  
3379 C C   . VAL A 399 ? 0.2817 0.4190 0.2939 -0.0253 0.0425  0.0546  399 VAL A C   
3380 O O   . VAL A 399 ? 0.3242 0.4614 0.3318 -0.0343 0.0449  0.0649  399 VAL A O   
3381 C CB  . VAL A 399 ? 0.3179 0.4858 0.3204 -0.0136 0.0504  0.0445  399 VAL A CB  
3382 C CG1 . VAL A 399 ? 0.3312 0.5066 0.3497 -0.0106 0.0522  0.0374  399 VAL A CG1 
3383 C CG2 . VAL A 399 ? 0.3638 0.5361 0.3539 -0.0049 0.0502  0.0371  399 VAL A CG2 
3384 N N   . ILE A 400 ? 0.2471 0.3781 0.2719 -0.0237 0.0396  0.0487  400 ILE A N   
3385 C CA  . ILE A 400 ? 0.2095 0.3371 0.2442 -0.0319 0.0395  0.0526  400 ILE A CA  
3386 C C   . ILE A 400 ? 0.1784 0.3201 0.2266 -0.0287 0.0417  0.0456  400 ILE A C   
3387 O O   . ILE A 400 ? 0.2004 0.3421 0.2509 -0.0196 0.0405  0.0370  400 ILE A O   
3388 C CB  . ILE A 400 ? 0.2618 0.3658 0.2970 -0.0331 0.0328  0.0533  400 ILE A CB  
3389 C CG1 . ILE A 400 ? 0.2926 0.3901 0.3304 -0.0237 0.0284  0.0441  400 ILE A CG1 
3390 C CG2 . ILE A 400 ? 0.3970 0.4864 0.4188 -0.0368 0.0308  0.0626  400 ILE A CG2 
3391 C CD1 . ILE A 400 ? 0.3734 0.4522 0.4130 -0.0237 0.0226  0.0439  400 ILE A CD1 
3392 N N   . GLU A 401 ? 0.1546 0.3079 0.2114 -0.0365 0.0447  0.0496  401 GLU A N   
3393 C CA  . GLU A 401 ? 0.1550 0.3259 0.2245 -0.0326 0.0469  0.0442  401 GLU A CA  
3394 C C   . GLU A 401 ? 0.1644 0.3285 0.2445 -0.0362 0.0428  0.0430  401 GLU A C   
3395 O O   . GLU A 401 ? 0.1661 0.3415 0.2559 -0.0307 0.0431  0.0381  401 GLU A O   
3396 C CB  . GLU A 401 ? 0.2797 0.4788 0.3529 -0.0369 0.0540  0.0482  401 GLU A CB  
3397 C CG  . GLU A 401 ? 0.3326 0.5422 0.3943 -0.0332 0.0592  0.0493  401 GLU A CG  
3398 C CD  . GLU A 401 ? 0.4192 0.6324 0.4783 -0.0183 0.0600  0.0389  401 GLU A CD  
3399 O OE1 . GLU A 401 ? 0.4217 0.6324 0.4891 -0.0107 0.0577  0.0317  401 GLU A OE1 
3400 O OE2 . GLU A 401 ? 0.4585 0.6760 0.5058 -0.0144 0.0630  0.0381  401 GLU A OE2 
3401 N N   . SER A 402 ? 0.2225 0.3679 0.3000 -0.0442 0.0387  0.0471  402 SER A N   
3402 C CA  . SER A 402 ? 0.2282 0.3677 0.3143 -0.0478 0.0348  0.0453  402 SER A CA  
3403 C C   . SER A 402 ? 0.2156 0.3282 0.2947 -0.0514 0.0298  0.0470  402 SER A C   
3404 O O   . SER A 402 ? 0.1836 0.2854 0.2531 -0.0563 0.0299  0.0530  402 SER A O   
3405 C CB  . SER A 402 ? 0.1629 0.3211 0.2578 -0.0583 0.0372  0.0493  402 SER A CB  
3406 O OG  . SER A 402 ? 0.1876 0.3419 0.2902 -0.0615 0.0329  0.0467  402 SER A OG  
3407 N N   . VAL A 403 ? 0.1923 0.2942 0.2754 -0.0482 0.0255  0.0419  403 VAL A N   
3408 C CA  . VAL A 403 ? 0.1586 0.2372 0.2362 -0.0505 0.0210  0.0424  403 VAL A CA  
3409 C C   . VAL A 403 ? 0.2332 0.3103 0.3172 -0.0570 0.0186  0.0407  403 VAL A C   
3410 O O   . VAL A 403 ? 0.2298 0.3231 0.3231 -0.0564 0.0193  0.0379  403 VAL A O   
3411 C CB  . VAL A 403 ? 0.1992 0.2664 0.2739 -0.0404 0.0180  0.0372  403 VAL A CB  
3412 C CG1 . VAL A 403 ? 0.1798 0.2498 0.2476 -0.0345 0.0195  0.0379  403 VAL A CG1 
3413 C CG2 . VAL A 403 ? 0.2164 0.2895 0.2994 -0.0352 0.0171  0.0306  403 VAL A CG2 
3414 N N   . LYS A 404 ? 0.2041 0.2612 0.2821 -0.0626 0.0155  0.0423  404 LYS A N   
3415 C CA  . LYS A 404 ? 0.2052 0.2575 0.2869 -0.0682 0.0123  0.0391  404 LYS A CA  
3416 C C   . LYS A 404 ? 0.2074 0.2498 0.2889 -0.0588 0.0093  0.0326  404 LYS A C   
3417 O O   . LYS A 404 ? 0.2820 0.3089 0.3567 -0.0531 0.0078  0.0321  404 LYS A O   
3418 C CB  . LYS A 404 ? 0.2751 0.3084 0.3491 -0.0793 0.0104  0.0429  404 LYS A CB  
3419 C CG  . LYS A 404 ? 0.5460 0.5922 0.6237 -0.0936 0.0124  0.0476  404 LYS A CG  
3420 C CD  . LYS A 404 ? 0.6114 0.6360 0.6825 -0.1057 0.0088  0.0481  404 LYS A CD  
3421 C CE  . LYS A 404 ? 0.6485 0.6877 0.7241 -0.1226 0.0106  0.0528  404 LYS A CE  
3422 N NZ  . LYS A 404 ? 0.7124 0.7539 0.7823 -0.1267 0.0153  0.0613  404 LYS A NZ  
3423 N N   . ALA A 405 ? 0.1617 0.2147 0.2506 -0.0572 0.0084  0.0281  405 ALA A N   
3424 C CA  . ALA A 405 ? 0.1697 0.2169 0.2588 -0.0494 0.0065  0.0226  405 ALA A CA  
3425 C C   . ALA A 405 ? 0.1642 0.1905 0.2460 -0.0499 0.0034  0.0203  405 ALA A C   
3426 O O   . ALA A 405 ? 0.1767 0.1933 0.2549 -0.0579 0.0016  0.0209  405 ALA A O   
3427 C CB  . ALA A 405 ? 0.1645 0.2250 0.2607 -0.0495 0.0056  0.0197  405 ALA A CB  
3428 N N   . GLY A 406 ? 0.1966 0.2161 0.2761 -0.0413 0.0028  0.0173  406 GLY A N   
3429 C CA  . GLY A 406 ? 0.1897 0.1914 0.2627 -0.0391 0.0002  0.0142  406 GLY A CA  
3430 C C   . GLY A 406 ? 0.2119 0.2138 0.2852 -0.0291 0.0001  0.0108  406 GLY A C   
3431 O O   . GLY A 406 ? 0.1425 0.1572 0.2210 -0.0256 0.0017  0.0101  406 GLY A O   
3432 N N   . THR A 407 ? 0.1760 0.1635 0.2435 -0.0246 -0.0019 0.0082  407 THR A N   
3433 C CA  . THR A 407 ? 0.1825 0.1722 0.2507 -0.0149 -0.0022 0.0046  407 THR A CA  
3434 C C   . THR A 407 ? 0.1841 0.1579 0.2446 -0.0090 -0.0045 0.0062  407 THR A C   
3435 O O   . THR A 407 ? 0.2174 0.1752 0.2706 -0.0132 -0.0058 0.0100  407 THR A O   
3436 C CB  . THR A 407 ? 0.1584 0.1506 0.2281 -0.0124 -0.0022 -0.0020 407 THR A CB  
3437 O OG1 . THR A 407 ? 0.1962 0.1706 0.2581 -0.0117 -0.0044 -0.0049 407 THR A OG1 
3438 C CG2 . THR A 407 ? 0.1592 0.1633 0.2339 -0.0185 -0.0008 -0.0028 407 THR A CG2 
3439 N N   . TRP A 408 ? 0.1601 0.1383 0.2218 0.0007  -0.0053 0.0036  408 TRP A N   
3440 C CA  . TRP A 408 ? 0.1754 0.1389 0.2295 0.0089  -0.0081 0.0050  408 TRP A CA  
3441 C C   . TRP A 408 ? 0.1955 0.1414 0.2432 0.0128  -0.0097 0.0001  408 TRP A C   
3442 O O   . TRP A 408 ? 0.2422 0.1730 0.2825 0.0216  -0.0124 0.0006  408 TRP A O   
3443 C CB  . TRP A 408 ? 0.2044 0.1822 0.2628 0.0186  -0.0090 0.0040  408 TRP A CB  
3444 C CG  . TRP A 408 ? 0.1754 0.1702 0.2421 0.0237  -0.0078 -0.0030 408 TRP A CG  
3445 C CD1 . TRP A 408 ? 0.1919 0.1892 0.2610 0.0220  -0.0059 -0.0086 408 TRP A CD1 
3446 C CD2 . TRP A 408 ? 0.1494 0.1627 0.2225 0.0303  -0.0084 -0.0048 408 TRP A CD2 
3447 N NE1 . TRP A 408 ? 0.1559 0.1723 0.2325 0.0272  -0.0046 -0.0132 408 TRP A NE1 
3448 C CE2 . TRP A 408 ? 0.1523 0.1791 0.2322 0.0317  -0.0063 -0.0111 408 TRP A CE2 
3449 C CE3 . TRP A 408 ? 0.1595 0.1808 0.2331 0.0346  -0.0108 -0.0017 408 TRP A CE3 
3450 C CZ2 . TRP A 408 ? 0.1778 0.2263 0.2659 0.0361  -0.0061 -0.0142 408 TRP A CZ2 
3451 C CZ3 . TRP A 408 ? 0.1916 0.2341 0.2732 0.0393  -0.0113 -0.0054 408 TRP A CZ3 
3452 C CH2 . TRP A 408 ? 0.1602 0.2166 0.2496 0.0396  -0.0089 -0.0116 408 TRP A CH2 
3453 N N   . PHE A 409 ? 0.2177 0.1645 0.2669 0.0075  -0.0085 -0.0049 409 PHE A N   
3454 C CA  . PHE A 409 ? 0.2089 0.1375 0.2502 0.0102  -0.0101 -0.0107 409 PHE A CA  
3455 C C   . PHE A 409 ? 0.3036 0.2137 0.3378 -0.0019 -0.0114 -0.0079 409 PHE A C   
3456 O O   . PHE A 409 ? 0.3031 0.2219 0.3412 -0.0120 -0.0104 -0.0087 409 PHE A O   
3457 C CB  . PHE A 409 ? 0.2131 0.1564 0.2594 0.0118  -0.0081 -0.0185 409 PHE A CB  
3458 C CG  . PHE A 409 ? 0.3037 0.2326 0.3419 0.0195  -0.0093 -0.0265 409 PHE A CG  
3459 C CD1 . PHE A 409 ? 0.3813 0.2842 0.4083 0.0148  -0.0118 -0.0286 409 PHE A CD1 
3460 C CD2 . PHE A 409 ? 0.3373 0.2793 0.3789 0.0311  -0.0077 -0.0325 409 PHE A CD2 
3461 C CE1 . PHE A 409 ? 0.4754 0.3626 0.4932 0.0227  -0.0130 -0.0371 409 PHE A CE1 
3462 C CE2 . PHE A 409 ? 0.3844 0.3141 0.4179 0.0398  -0.0083 -0.0408 409 PHE A CE2 
3463 C CZ  . PHE A 409 ? 0.3418 0.2427 0.3627 0.0362  -0.0111 -0.0435 409 PHE A CZ  
3464 N N   . ASP A 410 ? 0.2952 0.1803 0.3188 -0.0011 -0.0139 -0.0039 410 ASP A N   
3465 C CA  . ASP A 410 ? 0.4192 0.2841 0.4347 -0.0142 -0.0153 -0.0003 410 ASP A CA  
3466 C C   . ASP A 410 ? 0.3779 0.2598 0.4008 -0.0275 -0.0131 0.0064  410 ASP A C   
3467 O O   . ASP A 410 ? 0.3678 0.2418 0.3878 -0.0408 -0.0136 0.0083  410 ASP A O   
3468 C CB  . ASP A 410 ? 0.4500 0.3024 0.4603 -0.0192 -0.0168 -0.0088 410 ASP A CB  
3469 C CG  . ASP A 410 ? 0.6134 0.4432 0.6131 -0.0063 -0.0191 -0.0160 410 ASP A CG  
3470 O OD1 . ASP A 410 ? 0.6194 0.4342 0.6127 0.0040  -0.0206 -0.0124 410 ASP A OD1 
3471 O OD2 . ASP A 410 ? 0.5678 0.3956 0.5650 -0.0057 -0.0195 -0.0254 410 ASP A OD2 
3472 N N   . GLY A 411 ? 0.2653 0.1707 0.2976 -0.0243 -0.0106 0.0096  411 GLY A N   
3473 C CA  . GLY A 411 ? 0.2584 0.1818 0.2979 -0.0342 -0.0080 0.0147  411 GLY A CA  
3474 C C   . GLY A 411 ? 0.3194 0.2586 0.3668 -0.0418 -0.0071 0.0108  411 GLY A C   
3475 O O   . GLY A 411 ? 0.2825 0.2360 0.3356 -0.0500 -0.0053 0.0149  411 GLY A O   
3476 N N   . ASN A 412 ? 0.2403 0.1790 0.2879 -0.0387 -0.0082 0.0031  412 ASN A N   
3477 C CA  . ASN A 412 ? 0.2074 0.1590 0.2602 -0.0463 -0.0083 -0.0001 412 ASN A CA  
3478 C C   . ASN A 412 ? 0.2166 0.1805 0.2734 -0.0384 -0.0075 -0.0061 412 ASN A C   
3479 O O   . ASN A 412 ? 0.2274 0.1915 0.2842 -0.0283 -0.0065 -0.0078 412 ASN A O   
3480 C CB  . ASN A 412 ? 0.2276 0.1622 0.2728 -0.0564 -0.0113 -0.0028 412 ASN A CB  
3481 C CG  . ASN A 412 ? 0.2297 0.1417 0.2643 -0.0501 -0.0137 -0.0103 412 ASN A CG  
3482 O OD1 . ASN A 412 ? 0.2728 0.1912 0.3085 -0.0408 -0.0131 -0.0162 412 ASN A OD1 
3483 N ND2 . ASN A 412 ? 0.3393 0.2240 0.3628 -0.0556 -0.0163 -0.0101 412 ASN A ND2 
3484 N N   . PHE A 413 ? 0.1683 0.1436 0.2282 -0.0435 -0.0080 -0.0089 413 PHE A N   
3485 C CA  . PHE A 413 ? 0.1623 0.1508 0.2253 -0.0377 -0.0067 -0.0127 413 PHE A CA  
3486 C C   . PHE A 413 ? 0.2084 0.1894 0.2639 -0.0368 -0.0084 -0.0206 413 PHE A C   
3487 O O   . PHE A 413 ? 0.1911 0.1843 0.2479 -0.0340 -0.0073 -0.0233 413 PHE A O   
3488 C CB  . PHE A 413 ? 0.1577 0.1662 0.2284 -0.0416 -0.0059 -0.0093 413 PHE A CB  
3489 C CG  . PHE A 413 ? 0.1639 0.1813 0.2413 -0.0400 -0.0036 -0.0033 413 PHE A CG  
3490 C CD1 . PHE A 413 ? 0.1408 0.1650 0.2214 -0.0329 -0.0012 -0.0028 413 PHE A CD1 
3491 C CD2 . PHE A 413 ? 0.2241 0.2439 0.3040 -0.0462 -0.0035 0.0015  413 PHE A CD2 
3492 C CE1 . PHE A 413 ? 0.1648 0.1958 0.2501 -0.0314 0.0007  0.0016  413 PHE A CE1 
3493 C CE2 . PHE A 413 ? 0.1618 0.1905 0.2466 -0.0438 -0.0010 0.0062  413 PHE A CE2 
3494 C CZ  . PHE A 413 ? 0.1731 0.2063 0.2600 -0.0360 0.0009  0.0057  413 PHE A CZ  
3495 N N   . LEU A 414 ? 0.2045 0.1647 0.2511 -0.0389 -0.0109 -0.0243 414 LEU A N   
3496 C CA  . LEU A 414 ? 0.2524 0.2046 0.2904 -0.0392 -0.0129 -0.0330 414 LEU A CA  
3497 C C   . LEU A 414 ? 0.2103 0.1662 0.2461 -0.0273 -0.0106 -0.0387 414 LEU A C   
3498 O O   . LEU A 414 ? 0.2274 0.1844 0.2571 -0.0267 -0.0111 -0.0459 414 LEU A O   
3499 C CB  . LEU A 414 ? 0.2804 0.2047 0.3076 -0.0439 -0.0163 -0.0361 414 LEU A CB  
3500 C CG  . LEU A 414 ? 0.3489 0.2701 0.3768 -0.0591 -0.0189 -0.0319 414 LEU A CG  
3501 C CD1 . LEU A 414 ? 0.3737 0.2627 0.3886 -0.0645 -0.0222 -0.0354 414 LEU A CD1 
3502 C CD2 . LEU A 414 ? 0.2878 0.2294 0.3202 -0.0676 -0.0205 -0.0338 414 LEU A CD2 
3503 N N   . LYS A 415 ? 0.2118 0.1719 0.2524 -0.0181 -0.0079 -0.0361 415 LYS A N   
3504 C CA  . LYS A 415 ? 0.1923 0.1613 0.2327 -0.0077 -0.0052 -0.0414 415 LYS A CA  
3505 C C   . LYS A 415 ? 0.1772 0.1693 0.2232 -0.0098 -0.0024 -0.0403 415 LYS A C   
3506 O O   . LYS A 415 ? 0.2100 0.2118 0.2550 -0.0036 0.0003  -0.0447 415 LYS A O   
3507 C CB  . LYS A 415 ? 0.2054 0.1760 0.2504 0.0021  -0.0036 -0.0390 415 LYS A CB  
3508 C CG  . LYS A 415 ? 0.3526 0.3011 0.3892 0.0106  -0.0057 -0.0427 415 LYS A CG  
3509 C CD  . LYS A 415 ? 0.4087 0.3537 0.4377 0.0188  -0.0050 -0.0532 415 LYS A CD  
3510 C CE  . LYS A 415 ? 0.4386 0.4095 0.4751 0.0269  -0.0007 -0.0555 415 LYS A CE  
3511 N NZ  . LYS A 415 ? 0.4762 0.4468 0.5057 0.0371  0.0009  -0.0659 415 LYS A NZ  
3512 N N   . TRP A 416 ? 0.1648 0.1661 0.2162 -0.0176 -0.0029 -0.0341 416 TRP A N   
3513 C CA  . TRP A 416 ? 0.1523 0.1720 0.2075 -0.0191 -0.0007 -0.0317 416 TRP A CA  
3514 C C   . TRP A 416 ? 0.1501 0.1746 0.2026 -0.0265 -0.0032 -0.0311 416 TRP A C   
3515 O O   . TRP A 416 ? 0.1568 0.1945 0.2099 -0.0269 -0.0019 -0.0289 416 TRP A O   
3516 C CB  . TRP A 416 ? 0.1395 0.1682 0.2040 -0.0189 0.0013  -0.0244 416 TRP A CB  
3517 C CG  . TRP A 416 ? 0.1598 0.1874 0.2273 -0.0120 0.0031  -0.0251 416 TRP A CG  
3518 C CD1 . TRP A 416 ? 0.1266 0.1652 0.1967 -0.0073 0.0062  -0.0268 416 TRP A CD1 
3519 C CD2 . TRP A 416 ? 0.1348 0.1515 0.2029 -0.0095 0.0016  -0.0236 416 TRP A CD2 
3520 N NE1 . TRP A 416 ? 0.1405 0.1776 0.2138 -0.0012 0.0062  -0.0272 416 TRP A NE1 
3521 C CE2 . TRP A 416 ? 0.1325 0.1550 0.2038 -0.0019 0.0033  -0.0250 416 TRP A CE2 
3522 C CE3 . TRP A 416 ? 0.2034 0.2069 0.2692 -0.0134 -0.0010 -0.0209 416 TRP A CE3 
3523 C CZ2 . TRP A 416 ? 0.1877 0.2029 0.2594 0.0032  0.0018  -0.0235 416 TRP A CZ2 
3524 C CZ3 . TRP A 416 ? 0.2421 0.2364 0.3072 -0.0091 -0.0018 -0.0188 416 TRP A CZ3 
3525 C CH2 . TRP A 416 ? 0.1956 0.1955 0.2633 -0.0002 -0.0007 -0.0201 416 TRP A CH2 
3526 N N   . ILE A 417 ? 0.1806 0.1954 0.2301 -0.0328 -0.0070 -0.0325 417 ILE A N   
3527 C CA  . ILE A 417 ? 0.1892 0.2122 0.2379 -0.0404 -0.0103 -0.0318 417 ILE A CA  
3528 C C   . ILE A 417 ? 0.2084 0.2167 0.2506 -0.0474 -0.0144 -0.0370 417 ILE A C   
3529 O O   . ILE A 417 ? 0.2912 0.2820 0.3312 -0.0471 -0.0146 -0.0381 417 ILE A O   
3530 C CB  . ILE A 417 ? 0.1457 0.1818 0.2043 -0.0432 -0.0102 -0.0232 417 ILE A CB  
3531 C CG1 . ILE A 417 ? 0.1645 0.2149 0.2228 -0.0476 -0.0133 -0.0220 417 ILE A CG1 
3532 C CG2 . ILE A 417 ? 0.1729 0.2024 0.2364 -0.0475 -0.0109 -0.0197 417 ILE A CG2 
3533 C CD1 . ILE A 417 ? 0.1484 0.2130 0.2157 -0.0465 -0.0126 -0.0140 417 ILE A CD1 
3534 N N   . GLY A 418 ? 0.2092 0.2233 0.2470 -0.0539 -0.0181 -0.0404 418 GLY A N   
3535 C CA  . GLY A 418 ? 0.2862 0.2883 0.3186 -0.0639 -0.0228 -0.0449 418 GLY A CA  
3536 C C   . GLY A 418 ? 0.3546 0.3451 0.3733 -0.0647 -0.0255 -0.0559 418 GLY A C   
3537 O O   . GLY A 418 ? 0.5232 0.5072 0.5370 -0.0752 -0.0303 -0.0602 418 GLY A O   
3538 N N   . ASN A 419 ? 0.3361 0.3244 0.3480 -0.0548 -0.0226 -0.0613 419 ASN A N   
3539 C CA  . ASN A 419 ? 0.3398 0.3201 0.3376 -0.0553 -0.0250 -0.0726 419 ASN A CA  
3540 C C   . ASN A 419 ? 0.3316 0.3348 0.3271 -0.0533 -0.0244 -0.0728 419 ASN A C   
3541 O O   . ASN A 419 ? 0.2825 0.3039 0.2866 -0.0505 -0.0217 -0.0641 419 ASN A O   
3542 C CB  . ASN A 419 ? 0.2966 0.2554 0.2854 -0.0452 -0.0226 -0.0806 419 ASN A CB  
3543 C CG  . ASN A 419 ? 0.3856 0.3573 0.3768 -0.0322 -0.0164 -0.0800 419 ASN A CG  
3544 O OD1 . ASN A 419 ? 0.3511 0.3453 0.3476 -0.0315 -0.0139 -0.0747 419 ASN A OD1 
3545 N ND2 . ASN A 419 ? 0.4019 0.3592 0.3891 -0.0218 -0.0140 -0.0853 419 ASN A ND2 
3546 N N   . LYS A 420 ? 0.3121 0.3126 0.2941 -0.0548 -0.0272 -0.0829 420 LYS A N   
3547 C CA  . LYS A 420 ? 0.2730 0.2955 0.2507 -0.0546 -0.0276 -0.0823 420 LYS A CA  
3548 C C   . LYS A 420 ? 0.3276 0.3634 0.3083 -0.0445 -0.0207 -0.0769 420 LYS A C   
3549 O O   . LYS A 420 ? 0.2971 0.3514 0.2824 -0.0449 -0.0200 -0.0682 420 LYS A O   
3550 C CB  . LYS A 420 ? 0.2868 0.3038 0.2471 -0.0567 -0.0311 -0.0953 420 LYS A CB  
3551 C CG  . LYS A 420 ? 0.4627 0.5039 0.4179 -0.0582 -0.0329 -0.0933 420 LYS A CG  
3552 C CD  . LYS A 420 ? 0.5953 0.6336 0.5324 -0.0621 -0.0378 -0.1065 420 LYS A CD  
3553 C CE  . LYS A 420 ? 0.6181 0.6824 0.5500 -0.0637 -0.0403 -0.1026 420 LYS A CE  
3554 N NZ  . LYS A 420 ? 0.6310 0.6953 0.5428 -0.0644 -0.0432 -0.1158 420 LYS A NZ  
3555 N N   . GLU A 421 ? 0.3055 0.3318 0.2839 -0.0353 -0.0156 -0.0815 421 GLU A N   
3556 C CA  . GLU A 421 ? 0.3362 0.3774 0.3167 -0.0272 -0.0088 -0.0778 421 GLU A CA  
3557 C C   . GLU A 421 ? 0.2391 0.2878 0.2347 -0.0269 -0.0061 -0.0655 421 GLU A C   
3558 O O   . GLU A 421 ? 0.2281 0.2925 0.2261 -0.0261 -0.0029 -0.0584 421 GLU A O   
3559 C CB  . GLU A 421 ? 0.3447 0.3776 0.3198 -0.0170 -0.0044 -0.0870 421 GLU A CB  
3560 C CG  . GLU A 421 ? 0.3718 0.3997 0.3298 -0.0147 -0.0055 -0.1003 421 GLU A CG  
3561 C CD  . GLU A 421 ? 0.6089 0.6101 0.5595 -0.0183 -0.0115 -0.1094 421 GLU A CD  
3562 O OE1 . GLU A 421 ? 0.5854 0.5716 0.5443 -0.0210 -0.0136 -0.1050 421 GLU A OE1 
3563 O OE2 . GLU A 421 ? 0.6274 0.6219 0.5628 -0.0192 -0.0142 -0.1208 421 GLU A OE2 
3564 N N   . LYS A 422 ? 0.2142 0.2506 0.2185 -0.0276 -0.0071 -0.0629 422 LYS A N   
3565 C CA  . LYS A 422 ? 0.2295 0.2727 0.2469 -0.0275 -0.0049 -0.0523 422 LYS A CA  
3566 C C   . LYS A 422 ? 0.1968 0.2512 0.2182 -0.0339 -0.0080 -0.0443 422 LYS A C   
3567 O O   . LYS A 422 ? 0.1661 0.2305 0.1934 -0.0326 -0.0055 -0.0362 422 LYS A O   
3568 C CB  . LYS A 422 ? 0.2459 0.2739 0.2699 -0.0267 -0.0056 -0.0514 422 LYS A CB  
3569 C CG  . LYS A 422 ? 0.2220 0.2396 0.2431 -0.0177 -0.0029 -0.0579 422 LYS A CG  
3570 C CD  . LYS A 422 ? 0.2480 0.2485 0.2735 -0.0170 -0.0045 -0.0559 422 LYS A CD  
3571 C CE  . LYS A 422 ? 0.2752 0.2613 0.2949 -0.0070 -0.0035 -0.0634 422 LYS A CE  
3572 N NZ  . LYS A 422 ? 0.2166 0.2178 0.2433 0.0025  0.0015  -0.0619 422 LYS A NZ  
3573 N N   . ASN A 423 ? 0.2068 0.2597 0.2247 -0.0407 -0.0136 -0.0469 423 ASN A N   
3574 C CA  . ASN A 423 ? 0.1905 0.2575 0.2123 -0.0454 -0.0171 -0.0400 423 ASN A CA  
3575 C C   . ASN A 423 ? 0.1868 0.2680 0.2020 -0.0426 -0.0160 -0.0369 423 ASN A C   
3576 O O   . ASN A 423 ? 0.2385 0.3300 0.2583 -0.0419 -0.0163 -0.0280 423 ASN A O   
3577 C CB  . ASN A 423 ? 0.2042 0.2700 0.2236 -0.0542 -0.0237 -0.0444 423 ASN A CB  
3578 C CG  . ASN A 423 ? 0.2460 0.3019 0.2742 -0.0592 -0.0249 -0.0429 423 ASN A CG  
3579 O OD1 . ASN A 423 ? 0.2539 0.3044 0.2896 -0.0552 -0.0210 -0.0382 423 ASN A OD1 
3580 N ND2 . ASN A 423 ? 0.2614 0.3160 0.2885 -0.0690 -0.0303 -0.0464 423 ASN A ND2 
3581 N N   . GLU A 424 ? 0.1941 0.2752 0.1973 -0.0405 -0.0145 -0.0440 424 GLU A N   
3582 C CA  . GLU A 424 ? 0.1968 0.2914 0.1922 -0.0382 -0.0125 -0.0401 424 GLU A CA  
3583 C C   . GLU A 424 ? 0.1863 0.2842 0.1881 -0.0343 -0.0065 -0.0310 424 GLU A C   
3584 O O   . GLU A 424 ? 0.2070 0.3137 0.2064 -0.0341 -0.0062 -0.0225 424 GLU A O   
3585 C CB  . GLU A 424 ? 0.2693 0.3644 0.2502 -0.0362 -0.0109 -0.0502 424 GLU A CB  
3586 C CG  . GLU A 424 ? 0.3001 0.4096 0.2712 -0.0340 -0.0073 -0.0458 424 GLU A CG  
3587 C CD  . GLU A 424 ? 0.4558 0.5769 0.4199 -0.0374 -0.0131 -0.0403 424 GLU A CD  
3588 O OE1 . GLU A 424 ? 0.5139 0.6457 0.4679 -0.0359 -0.0106 -0.0357 424 GLU A OE1 
3589 O OE2 . GLU A 424 ? 0.4181 0.5393 0.3868 -0.0416 -0.0200 -0.0402 424 GLU A OE2 
3590 N N   . TYR A 425 ? 0.1764 0.2667 0.1856 -0.0313 -0.0022 -0.0324 425 TYR A N   
3591 C CA  . TYR A 425 ? 0.1783 0.2718 0.1942 -0.0294 0.0028  -0.0243 425 TYR A CA  
3592 C C   . TYR A 425 ? 0.1893 0.2821 0.2130 -0.0310 0.0001  -0.0150 425 TYR A C   
3593 O O   . TYR A 425 ? 0.1824 0.2789 0.2056 -0.0307 0.0020  -0.0068 425 TYR A O   
3594 C CB  . TYR A 425 ? 0.1944 0.2820 0.2177 -0.0259 0.0068  -0.0281 425 TYR A CB  
3595 C CG  . TYR A 425 ? 0.1856 0.2805 0.2046 -0.0223 0.0125  -0.0326 425 TYR A CG  
3596 C CD1 . TYR A 425 ? 0.1789 0.2812 0.1854 -0.0215 0.0136  -0.0377 425 TYR A CD1 
3597 C CD2 . TYR A 425 ? 0.1727 0.2693 0.2002 -0.0192 0.0168  -0.0324 425 TYR A CD2 
3598 C CE1 . TYR A 425 ? 0.1975 0.3098 0.2009 -0.0175 0.0198  -0.0423 425 TYR A CE1 
3599 C CE2 . TYR A 425 ? 0.1750 0.2826 0.2005 -0.0155 0.0224  -0.0368 425 TYR A CE2 
3600 C CZ  . TYR A 425 ? 0.1775 0.2932 0.1913 -0.0145 0.0242  -0.0417 425 TYR A CZ  
3601 O OH  . TYR A 425 ? 0.1806 0.3102 0.1933 -0.0103 0.0304  -0.0462 425 TYR A OH  
3602 N N   . TRP A 426 ? 0.1510 0.2390 0.1816 -0.0327 -0.0041 -0.0162 426 TRP A N   
3603 C CA  . TRP A 426 ? 0.1681 0.2582 0.2062 -0.0330 -0.0064 -0.0082 426 TRP A CA  
3604 C C   . TRP A 426 ? 0.2183 0.3184 0.2503 -0.0329 -0.0099 -0.0030 426 TRP A C   
3605 O O   . TRP A 426 ? 0.1804 0.2821 0.2147 -0.0302 -0.0097 0.0053  426 TRP A O   
3606 C CB  . TRP A 426 ? 0.2349 0.3213 0.2810 -0.0357 -0.0096 -0.0105 426 TRP A CB  
3607 C CG  . TRP A 426 ? 0.2066 0.2827 0.2592 -0.0343 -0.0063 -0.0121 426 TRP A CG  
3608 C CD1 . TRP A 426 ? 0.1532 0.2195 0.2045 -0.0347 -0.0059 -0.0189 426 TRP A CD1 
3609 C CD2 . TRP A 426 ? 0.2116 0.2857 0.2718 -0.0315 -0.0033 -0.0068 426 TRP A CD2 
3610 N NE1 . TRP A 426 ? 0.1417 0.2019 0.1995 -0.0321 -0.0031 -0.0173 426 TRP A NE1 
3611 C CE2 . TRP A 426 ? 0.1450 0.2105 0.2083 -0.0306 -0.0015 -0.0104 426 TRP A CE2 
3612 C CE3 . TRP A 426 ? 0.1935 0.2709 0.2567 -0.0293 -0.0024 0.0004  426 TRP A CE3 
3613 C CZ2 . TRP A 426 ? 0.1856 0.2482 0.2554 -0.0283 0.0011  -0.0074 426 TRP A CZ2 
3614 C CZ3 . TRP A 426 ? 0.2005 0.2728 0.2699 -0.0273 0.0004  0.0026  426 TRP A CZ3 
3615 C CH2 . TRP A 426 ? 0.2089 0.2752 0.2816 -0.0273 0.0020  -0.0014 426 TRP A CH2 
3616 N N   . LYS A 427 ? 0.1845 0.2906 0.2076 -0.0354 -0.0134 -0.0080 427 LYS A N   
3617 C CA  . LYS A 427 ? 0.1942 0.3117 0.2100 -0.0348 -0.0175 -0.0029 427 LYS A CA  
3618 C C   . LYS A 427 ? 0.2060 0.3237 0.2139 -0.0316 -0.0134 0.0045  427 LYS A C   
3619 O O   . LYS A 427 ? 0.1946 0.3158 0.2002 -0.0287 -0.0154 0.0136  427 LYS A O   
3620 C CB  . LYS A 427 ? 0.1810 0.3049 0.1869 -0.0386 -0.0220 -0.0110 427 LYS A CB  
3621 C CG  . LYS A 427 ? 0.4505 0.5770 0.4622 -0.0441 -0.0281 -0.0165 427 LYS A CG  
3622 C CD  . LYS A 427 ? 0.4848 0.6177 0.4844 -0.0486 -0.0333 -0.0247 427 LYS A CD  
3623 C CE  . LYS A 427 ? 0.6209 0.7442 0.6219 -0.0557 -0.0358 -0.0354 427 LYS A CE  
3624 N NZ  . LYS A 427 ? 0.6917 0.8147 0.7076 -0.0597 -0.0377 -0.0322 427 LYS A NZ  
3625 N N   . ILE A 428 ? 0.2081 0.3224 0.2108 -0.0320 -0.0076 0.0008  428 ILE A N   
3626 C CA  . ILE A 428 ? 0.1928 0.3078 0.1882 -0.0313 -0.0026 0.0081  428 ILE A CA  
3627 C C   . ILE A 428 ? 0.2123 0.3189 0.2157 -0.0299 -0.0006 0.0169  428 ILE A C   
3628 O O   . ILE A 428 ? 0.2177 0.3223 0.2149 -0.0290 -0.0001 0.0265  428 ILE A O   
3629 C CB  . ILE A 428 ? 0.2392 0.3559 0.2307 -0.0322 0.0038  0.0015  428 ILE A CB  
3630 C CG1 . ILE A 428 ? 0.2241 0.3484 0.2037 -0.0326 0.0020  -0.0070 428 ILE A CG1 
3631 C CG2 . ILE A 428 ? 0.1885 0.3061 0.1760 -0.0336 0.0100  0.0097  428 ILE A CG2 
3632 C CD1 . ILE A 428 ? 0.2641 0.3891 0.2420 -0.0312 0.0071  -0.0176 428 ILE A CD1 
3633 N N   . LEU A 429 ? 0.1994 0.2995 0.2153 -0.0296 0.0004  0.0136  429 LEU A N   
3634 C CA  . LEU A 429 ? 0.1974 0.2887 0.2203 -0.0283 0.0022  0.0201  429 LEU A CA  
3635 C C   . LEU A 429 ? 0.2073 0.2978 0.2313 -0.0244 -0.0028 0.0269  429 LEU A C   
3636 O O   . LEU A 429 ? 0.2034 0.2860 0.2252 -0.0222 -0.0019 0.0348  429 LEU A O   
3637 C CB  . LEU A 429 ? 0.1609 0.2473 0.1955 -0.0286 0.0039  0.0143  429 LEU A CB  
3638 C CG  . LEU A 429 ? 0.1861 0.2636 0.2276 -0.0276 0.0059  0.0189  429 LEU A CG  
3639 C CD1 . LEU A 429 ? 0.2194 0.2941 0.2571 -0.0309 0.0111  0.0219  429 LEU A CD1 
3640 C CD2 . LEU A 429 ? 0.1673 0.2419 0.2195 -0.0269 0.0056  0.0137  429 LEU A CD2 
3641 N N   . ILE A 430 ? 0.1728 0.2715 0.2002 -0.0234 -0.0082 0.0237  430 ILE A N   
3642 C CA  . ILE A 430 ? 0.1570 0.2602 0.1870 -0.0186 -0.0131 0.0296  430 ILE A CA  
3643 C C   . ILE A 430 ? 0.1725 0.2773 0.1902 -0.0153 -0.0151 0.0380  430 ILE A C   
3644 O O   . ILE A 430 ? 0.2548 0.3541 0.2716 -0.0093 -0.0163 0.0460  430 ILE A O   
3645 C CB  . ILE A 430 ? 0.1556 0.2715 0.1920 -0.0203 -0.0185 0.0241  430 ILE A CB  
3646 C CG1 . ILE A 430 ? 0.1506 0.2625 0.1991 -0.0227 -0.0167 0.0190  430 ILE A CG1 
3647 C CG2 . ILE A 430 ? 0.2025 0.3303 0.2402 -0.0149 -0.0244 0.0301  430 ILE A CG2 
3648 C CD1 . ILE A 430 ? 0.1759 0.2959 0.2277 -0.0286 -0.0205 0.0116  430 ILE A CD1 
3649 N N   . GLU A 431 ? 0.1815 0.2930 0.1880 -0.0184 -0.0156 0.0362  431 GLU A N   
3650 C CA  . GLU A 431 ? 0.2473 0.3608 0.2399 -0.0156 -0.0176 0.0450  431 GLU A CA  
3651 C C   . GLU A 431 ? 0.2406 0.3387 0.2267 -0.0158 -0.0118 0.0532  431 GLU A C   
3652 O O   . GLU A 431 ? 0.2848 0.3760 0.2631 -0.0111 -0.0136 0.0636  431 GLU A O   
3653 C CB  . GLU A 431 ? 0.3456 0.4708 0.3267 -0.0194 -0.0189 0.0401  431 GLU A CB  
3654 C CG  . GLU A 431 ? 0.6190 0.7499 0.5841 -0.0164 -0.0223 0.0491  431 GLU A CG  
3655 C CD  . GLU A 431 ? 0.6707 0.8057 0.6383 -0.0085 -0.0295 0.0569  431 GLU A CD  
3656 O OE1 . GLU A 431 ? 0.5630 0.7094 0.5419 -0.0074 -0.0348 0.0516  431 GLU A OE1 
3657 O OE2 . GLU A 431 ? 0.7344 0.8616 0.6923 -0.0033 -0.0299 0.0686  431 GLU A OE2 
3658 N N   . ALA A 432 ? 0.2005 0.2929 0.1897 -0.0214 -0.0052 0.0487  432 ALA A N   
3659 C CA  . ALA A 432 ? 0.2349 0.3141 0.2193 -0.0243 0.0005  0.0556  432 ALA A CA  
3660 C C   . ALA A 432 ? 0.2965 0.3603 0.2867 -0.0200 -0.0005 0.0610  432 ALA A C   
3661 O O   . ALA A 432 ? 0.2599 0.3095 0.2413 -0.0197 0.0008  0.0704  432 ALA A O   
3662 C CB  . ALA A 432 ? 0.2321 0.3133 0.2217 -0.0307 0.0071  0.0484  432 ALA A CB  
3663 N N   . LYS A 433 ? 0.2434 0.3087 0.2472 -0.0168 -0.0025 0.0551  433 LYS A N   
3664 C CA  . LYS A 433 ? 0.2320 0.2840 0.2415 -0.0119 -0.0030 0.0582  433 LYS A CA  
3665 C C   . LYS A 433 ? 0.2875 0.3344 0.2896 -0.0031 -0.0078 0.0675  433 LYS A C   
3666 O O   . LYS A 433 ? 0.3342 0.3630 0.3331 0.0007  -0.0071 0.0732  433 LYS A O   
3667 C CB  . LYS A 433 ? 0.2179 0.2766 0.2424 -0.0101 -0.0043 0.0502  433 LYS A CB  
3668 C CG  . LYS A 433 ? 0.2706 0.3196 0.3006 -0.0030 -0.0053 0.0526  433 LYS A CG  
3669 C CD  . LYS A 433 ? 0.2859 0.3166 0.3151 -0.0063 -0.0006 0.0530  433 LYS A CD  
3670 C CE  . LYS A 433 ? 0.2616 0.2819 0.2949 0.0016  -0.0017 0.0537  433 LYS A CE  
3671 N NZ  . LYS A 433 ? 0.2513 0.2498 0.2796 -0.0014 0.0016  0.0554  433 LYS A NZ  
3672 N N   . LYS A 434 ? 0.2719 0.3338 0.2705 0.0007  -0.0131 0.0689  434 LYS A N   
3673 C CA  . LYS A 434 ? 0.3430 0.4023 0.3343 0.0107  -0.0184 0.0782  434 LYS A CA  
3674 C C   . LYS A 434 ? 0.3862 0.4261 0.3605 0.0102  -0.0163 0.0890  434 LYS A C   
3675 O O   . LYS A 434 ? 0.3988 0.4261 0.3661 0.0194  -0.0194 0.0978  434 LYS A O   
3676 C CB  . LYS A 434 ? 0.3414 0.4234 0.3311 0.0136  -0.0249 0.0775  434 LYS A CB  
3677 C CG  . LYS A 434 ? 0.3130 0.4143 0.3156 0.0089  -0.0264 0.0664  434 LYS A CG  
3678 C CD  . LYS A 434 ? 0.4483 0.5717 0.4490 0.0118  -0.0341 0.0665  434 LYS A CD  
3679 C CE  . LYS A 434 ? 0.4672 0.6078 0.4797 0.0053  -0.0361 0.0554  434 LYS A CE  
3680 N NZ  . LYS A 434 ? 0.5478 0.7106 0.5568 0.0055  -0.0440 0.0545  434 LYS A NZ  
3681 N N   . LYS A 435 ? 0.3723 0.4095 0.3392 -0.0003 -0.0109 0.0889  435 LYS A N   
3682 C CA  . LYS A 435 ? 0.4241 0.4448 0.3737 -0.0034 -0.0083 0.1001  435 LYS A CA  
3683 C C   . LYS A 435 ? 0.3910 0.3943 0.3415 -0.0130 -0.0011 0.0998  435 LYS A C   
3684 O O   . LYS A 435 ? 0.3781 0.3696 0.3151 -0.0196 0.0026  0.1081  435 LYS A O   
3685 C CB  . LYS A 435 ? 0.4319 0.4677 0.3691 -0.0083 -0.0080 0.1021  435 LYS A CB  
3686 C CG  . LYS A 435 ? 0.5354 0.5916 0.4721 -0.0009 -0.0157 0.1004  435 LYS A CG  
3687 C CD  . LYS A 435 ? 0.6824 0.7492 0.6017 -0.0039 -0.0163 0.1051  435 LYS A CD  
3688 C CE  . LYS A 435 ? 0.7177 0.8028 0.6404 -0.0121 -0.0129 0.0931  435 LYS A CE  
3689 N NZ  . LYS A 435 ? 0.7838 0.8810 0.6881 -0.0142 -0.0137 0.0966  435 LYS A NZ  
3690 N N   . ALA A 436 ? 0.2526 0.3569 0.3679 0.0538  -0.0007 0.0883  436 ALA A N   
3691 C CA  . ALA A 436 ? 0.2014 0.2771 0.3043 0.0449  0.0066  0.0812  436 ALA A CA  
3692 C C   . ALA A 436 ? 0.2740 0.3205 0.3840 0.0529  0.0140  0.0870  436 ALA A C   
3693 O O   . ALA A 436 ? 0.3067 0.3497 0.4316 0.0657  0.0180  0.0883  436 ALA A O   
3694 C CB  . ALA A 436 ? 0.2631 0.3369 0.3636 0.0367  0.0111  0.0639  436 ALA A CB  
3695 N N   . LYS A 437 ? 0.2898 0.3147 0.3918 0.0454  0.0162  0.0903  437 LYS A N   
3696 C CA  . LYS A 437 ? 0.3127 0.3054 0.4237 0.0500  0.0225  0.0961  437 LYS A CA  
3697 C C   . LYS A 437 ? 0.3142 0.2800 0.4231 0.0385  0.0265  0.0804  437 LYS A C   
3698 O O   . LYS A 437 ? 0.3606 0.2954 0.4788 0.0412  0.0310  0.0798  437 LYS A O   
3699 C CB  . LYS A 437 ? 0.2757 0.2647 0.3855 0.0518  0.0219  0.1190  437 LYS A CB  
3700 C CG  . LYS A 437 ? 0.4043 0.4184 0.5144 0.0660  0.0158  0.1358  437 LYS A CG  
3701 C CD  . LYS A 437 ? 0.5337 0.5449 0.6623 0.0826  0.0172  0.1366  437 LYS A CD  
3702 C CE  . LYS A 437 ? 0.6212 0.6631 0.7536 0.0970  0.0081  0.1533  437 LYS A CE  
3703 N NZ  . LYS A 437 ? 0.6719 0.7085 0.8268 0.1165  0.0109  0.1606  437 LYS A NZ  
3704 N N   . ASN A 438 ? 0.3000 0.2756 0.3977 0.0262  0.0239  0.0674  438 ASN A N   
3705 C CA  . ASN A 438 ? 0.2432 0.1979 0.3385 0.0149  0.0245  0.0531  438 ASN A CA  
3706 C C   . ASN A 438 ? 0.2646 0.2349 0.3467 0.0090  0.0218  0.0375  438 ASN A C   
3707 O O   . ASN A 438 ? 0.2813 0.2755 0.3588 0.0122  0.0206  0.0386  438 ASN A O   
3708 C CB  . ASN A 438 ? 0.2352 0.1836 0.3351 0.0034  0.0240  0.0635  438 ASN A CB  
3709 C CG  . ASN A 438 ? 0.2910 0.2684 0.3814 -0.0004 0.0217  0.0728  438 ASN A CG  
3710 O OD1 . ASN A 438 ? 0.2081 0.2008 0.2889 -0.0058 0.0184  0.0620  438 ASN A OD1 
3711 N ND2 . ASN A 438 ? 0.3034 0.2872 0.3946 0.0038  0.0237  0.0930  438 ASN A ND2 
3712 N N   . ASP A 439 ? 0.3337 0.2900 0.4111 -0.0001 0.0199  0.0235  439 ASP A N   
3713 C CA  . ASP A 439 ? 0.3098 0.2760 0.3728 -0.0044 0.0173  0.0094  439 ASP A CA  
3714 C C   . ASP A 439 ? 0.2286 0.2172 0.2866 -0.0124 0.0132  0.0143  439 ASP A C   
3715 O O   . ASP A 439 ? 0.2238 0.2201 0.2706 -0.0153 0.0109  0.0054  439 ASP A O   
3716 C CB  . ASP A 439 ? 0.3203 0.2646 0.3786 -0.0106 0.0138  -0.0071 439 ASP A CB  
3717 C CG  . ASP A 439 ? 0.4416 0.3649 0.4949 -0.0002 0.0184  -0.0196 439 ASP A CG  
3718 O OD1 . ASP A 439 ? 0.3606 0.2894 0.4171 0.0125  0.0257  -0.0138 439 ASP A OD1 
3719 O OD2 . ASP A 439 ? 0.5145 0.4166 0.5611 -0.0039 0.0144  -0.0362 439 ASP A OD2 
3720 N N   . TYR A 440 ? 0.2000 0.1986 0.2640 -0.0144 0.0129  0.0282  440 TYR A N   
3721 C CA  . TYR A 440 ? 0.1824 0.2015 0.2392 -0.0187 0.0102  0.0301  440 TYR A CA  
3722 C C   . TYR A 440 ? 0.1799 0.2144 0.2297 -0.0136 0.0096  0.0281  440 TYR A C   
3723 O O   . TYR A 440 ? 0.2048 0.2509 0.2477 -0.0172 0.0072  0.0253  440 TYR A O   
3724 C CB  . TYR A 440 ? 0.1712 0.1982 0.2317 -0.0200 0.0117  0.0448  440 TYR A CB  
3725 C CG  . TYR A 440 ? 0.2326 0.2549 0.3020 -0.0296 0.0124  0.0462  440 TYR A CG  
3726 C CD1 . TYR A 440 ? 0.2713 0.3047 0.3382 -0.0354 0.0097  0.0393  440 TYR A CD1 
3727 C CD2 . TYR A 440 ? 0.2670 0.2743 0.3510 -0.0329 0.0159  0.0552  440 TYR A CD2 
3728 C CE1 . TYR A 440 ? 0.2918 0.3263 0.3723 -0.0441 0.0098  0.0410  440 TYR A CE1 
3729 C CE2 . TYR A 440 ? 0.3059 0.3120 0.4047 -0.0438 0.0165  0.0570  440 TYR A CE2 
3730 C CZ  . TYR A 440 ? 0.3036 0.3258 0.4013 -0.0493 0.0131  0.0497  440 TYR A CZ  
3731 O OH  . TYR A 440 ? 0.3221 0.3486 0.4395 -0.0600 0.0132  0.0522  440 TYR A OH  
3732 N N   . ILE A 441 ? 0.1482 0.1831 0.2029 -0.0054 0.0120  0.0295  441 ILE A N   
3733 C CA  . ILE A 441 ? 0.1817 0.2328 0.2360 -0.0028 0.0119  0.0272  441 ILE A CA  
3734 C C   . ILE A 441 ? 0.2010 0.2486 0.2464 -0.0063 0.0142  0.0165  441 ILE A C   
3735 O O   . ILE A 441 ? 0.1884 0.2477 0.2313 -0.0093 0.0135  0.0155  441 ILE A O   
3736 C CB  . ILE A 441 ? 0.1703 0.2266 0.2373 0.0077  0.0148  0.0322  441 ILE A CB  
3737 C CG1 . ILE A 441 ? 0.1432 0.2235 0.2177 0.0083  0.0126  0.0335  441 ILE A CG1 
3738 C CG2 . ILE A 441 ? 0.1774 0.2168 0.2459 0.0143  0.0222  0.0249  441 ILE A CG2 
3739 C CD1 . ILE A 441 ? 0.1891 0.2852 0.2622 0.0050  0.0034  0.0392  441 ILE A CD1 
3740 N N   . LEU A 442 ? 0.2139 0.2443 0.2533 -0.0063 0.0160  0.0085  442 LEU A N   
3741 C CA  . LEU A 442 ? 0.1805 0.2082 0.2060 -0.0080 0.0171  -0.0008 442 LEU A CA  
3742 C C   . LEU A 442 ? 0.2007 0.2339 0.2200 -0.0160 0.0111  -0.0007 442 LEU A C   
3743 O O   . LEU A 442 ? 0.1903 0.2293 0.2009 -0.0168 0.0118  -0.0019 442 LEU A O   
3744 C CB  . LEU A 442 ? 0.1783 0.1859 0.1957 -0.0055 0.0179  -0.0120 442 LEU A CB  
3745 C CG  . LEU A 442 ? 0.2285 0.2244 0.2516 0.0047  0.0247  -0.0145 442 LEU A CG  
3746 C CD1 . LEU A 442 ? 0.2319 0.2031 0.2439 0.0053  0.0229  -0.0298 442 LEU A CD1 
3747 C CD2 . LEU A 442 ? 0.1901 0.2000 0.2136 0.0138  0.0342  -0.0126 442 LEU A CD2 
3748 N N   . VAL A 443 ? 0.1524 0.1840 0.1775 -0.0211 0.0065  0.0022  443 VAL A N   
3749 C CA  . VAL A 443 ? 0.1464 0.1860 0.1692 -0.0264 0.0021  0.0031  443 VAL A CA  
3750 C C   . VAL A 443 ? 0.2328 0.2843 0.2539 -0.0253 0.0031  0.0071  443 VAL A C   
3751 O O   . VAL A 443 ? 0.1750 0.2292 0.1900 -0.0266 0.0016  0.0055  443 VAL A O   
3752 C CB  . VAL A 443 ? 0.1356 0.1757 0.1691 -0.0309 0.0003  0.0081  443 VAL A CB  
3753 C CG1 . VAL A 443 ? 0.1682 0.2192 0.2021 -0.0342 -0.0026 0.0088  443 VAL A CG1 
3754 C CG2 . VAL A 443 ? 0.1406 0.1658 0.1811 -0.0344 -0.0014 0.0037  443 VAL A CG2 
3755 N N   . ALA A 444 ? 0.1655 0.2233 0.1926 -0.0228 0.0044  0.0123  444 ALA A N   
3756 C CA  . ALA A 444 ? 0.1629 0.2312 0.1904 -0.0234 0.0028  0.0136  444 ALA A CA  
3757 C C   . ALA A 444 ? 0.1770 0.2467 0.2050 -0.0239 0.0055  0.0115  444 ALA A C   
3758 O O   . ALA A 444 ? 0.1682 0.2427 0.1984 -0.0269 0.0037  0.0113  444 ALA A O   
3759 C CB  . ALA A 444 ? 0.1370 0.2143 0.1707 -0.0202 0.0009  0.0190  444 ALA A CB  
3760 N N   . GLU A 445 ? 0.1696 0.2345 0.1958 -0.0209 0.0107  0.0100  445 GLU A N   
3761 C CA  . GLU A 445 ? 0.1625 0.2307 0.1886 -0.0206 0.0165  0.0108  445 GLU A CA  
3762 C C   . GLU A 445 ? 0.1756 0.2367 0.1876 -0.0225 0.0167  0.0097  445 GLU A C   
3763 O O   . GLU A 445 ? 0.1561 0.2186 0.1656 -0.0222 0.0229  0.0132  445 GLU A O   
3764 C CB  . GLU A 445 ? 0.1797 0.2476 0.2073 -0.0137 0.0244  0.0098  445 GLU A CB  
3765 C CG  . GLU A 445 ? 0.1412 0.2213 0.1884 -0.0099 0.0255  0.0142  445 GLU A CG  
3766 C CD  . GLU A 445 ? 0.2500 0.3246 0.2989 0.0000  0.0321  0.0121  445 GLU A CD  
3767 O OE1 . GLU A 445 ? 0.2156 0.2773 0.2490 0.0035  0.0372  0.0053  445 GLU A OE1 
3768 O OE2 . GLU A 445 ? 0.2033 0.2862 0.2685 0.0054  0.0319  0.0167  445 GLU A OE2 
3769 N N   . GLY A 446 ? 0.1884 0.2437 0.1928 -0.0237 0.0105  0.0069  446 GLY A N   
3770 C CA  . GLY A 446 ? 0.1479 0.1990 0.1407 -0.0237 0.0087  0.0074  446 GLY A CA  
3771 C C   . GLY A 446 ? 0.2077 0.2592 0.2045 -0.0260 0.0105  0.0128  446 GLY A C   
3772 O O   . GLY A 446 ? 0.2191 0.2737 0.2275 -0.0292 0.0089  0.0129  446 GLY A O   
3773 N N   . SER A 447 ? 0.1993 0.2461 0.1854 -0.0240 0.0132  0.0175  447 SER A N   
3774 C CA  . SER A 447 ? 0.1906 0.2332 0.1830 -0.0269 0.0163  0.0244  447 SER A CA  
3775 C C   . SER A 447 ? 0.2136 0.2509 0.2107 -0.0276 0.0097  0.0222  447 SER A C   
3776 O O   . SER A 447 ? 0.1849 0.2165 0.1922 -0.0315 0.0102  0.0232  447 SER A O   
3777 C CB  . SER A 447 ? 0.1924 0.2301 0.1703 -0.0232 0.0223  0.0334  447 SER A CB  
3778 O OG  . SER A 447 ? 0.2164 0.2502 0.1791 -0.0177 0.0154  0.0334  447 SER A OG  
3779 N N   . ASP A 448 ? 0.2031 0.2423 0.1946 -0.0238 0.0036  0.0185  448 ASP A N   
3780 C CA  . ASP A 448 ? 0.1926 0.2286 0.1878 -0.0213 -0.0005 0.0172  448 ASP A CA  
3781 C C   . ASP A 448 ? 0.1647 0.2002 0.1692 -0.0243 -0.0008 0.0116  448 ASP A C   
3782 O O   . ASP A 448 ? 0.1623 0.1886 0.1695 -0.0229 -0.0014 0.0101  448 ASP A O   
3783 C CB  . ASP A 448 ? 0.1805 0.2253 0.1746 -0.0177 -0.0059 0.0146  448 ASP A CB  
3784 C CG  . ASP A 448 ? 0.1709 0.2173 0.1535 -0.0149 -0.0093 0.0172  448 ASP A CG  
3785 O OD1 . ASP A 448 ? 0.2301 0.2782 0.2064 -0.0171 -0.0089 0.0139  448 ASP A OD1 
3786 O OD2 . ASP A 448 ? 0.2119 0.2569 0.1901 -0.0094 -0.0127 0.0223  448 ASP A OD2 
3787 N N   . TRP A 449 ? 0.1531 0.1972 0.1611 -0.0273 -0.0011 0.0080  449 TRP A N   
3788 C CA  . TRP A 449 ? 0.1414 0.1876 0.1533 -0.0288 -0.0034 0.0023  449 TRP A CA  
3789 C C   . TRP A 449 ? 0.1296 0.1674 0.1482 -0.0337 -0.0041 0.0003  449 TRP A C   
3790 O O   . TRP A 449 ? 0.1649 0.1961 0.1832 -0.0336 -0.0074 -0.0069 449 TRP A O   
3791 C CB  . TRP A 449 ? 0.1464 0.2040 0.1603 -0.0300 -0.0042 0.0020  449 TRP A CB  
3792 C CG  . TRP A 449 ? 0.1189 0.1805 0.1309 -0.0279 -0.0027 0.0050  449 TRP A CG  
3793 C CD1 . TRP A 449 ? 0.1324 0.1950 0.1459 -0.0285 -0.0008 0.0070  449 TRP A CD1 
3794 C CD2 . TRP A 449 ? 0.1358 0.2002 0.1468 -0.0254 -0.0031 0.0054  449 TRP A CD2 
3795 N NE1 . TRP A 449 ? 0.1976 0.2601 0.2102 -0.0277 -0.0015 0.0072  449 TRP A NE1 
3796 C CE2 . TRP A 449 ? 0.1616 0.2272 0.1748 -0.0267 -0.0031 0.0071  449 TRP A CE2 
3797 C CE3 . TRP A 449 ? 0.1824 0.2491 0.1932 -0.0216 -0.0030 0.0041  449 TRP A CE3 
3798 C CZ2 . TRP A 449 ? 0.1626 0.2327 0.1811 -0.0272 -0.0043 0.0080  449 TRP A CZ2 
3799 C CZ3 . TRP A 449 ? 0.1626 0.2372 0.1790 -0.0204 -0.0025 0.0066  449 TRP A CZ3 
3800 C CH2 . TRP A 449 ? 0.1122 0.1890 0.1340 -0.0244 -0.0039 0.0088  449 TRP A CH2 
3801 N N   . PHE A 450 ? 0.1495 0.1868 0.1747 -0.0382 -0.0004 0.0063  450 PHE A N   
3802 C CA  . PHE A 450 ? 0.1417 0.1728 0.1802 -0.0457 -0.0004 0.0064  450 PHE A CA  
3803 C C   . PHE A 450 ? 0.1648 0.1762 0.2026 -0.0452 0.0015  0.0093  450 PHE A C   
3804 O O   . PHE A 450 ? 0.1959 0.1953 0.2444 -0.0512 -0.0011 0.0050  450 PHE A O   
3805 C CB  . PHE A 450 ? 0.1582 0.1994 0.2075 -0.0500 0.0059  0.0144  450 PHE A CB  
3806 C CG  . PHE A 450 ? 0.1370 0.1956 0.1893 -0.0483 0.0045  0.0124  450 PHE A CG  
3807 C CD1 . PHE A 450 ? 0.1274 0.1895 0.1678 -0.0415 0.0076  0.0141  450 PHE A CD1 
3808 C CD2 . PHE A 450 ? 0.1235 0.1943 0.1916 -0.0533 -0.0011 0.0087  450 PHE A CD2 
3809 C CE1 . PHE A 450 ? 0.1492 0.2230 0.1937 -0.0388 0.0069  0.0132  450 PHE A CE1 
3810 C CE2 . PHE A 450 ? 0.1374 0.2239 0.2088 -0.0495 -0.0028 0.0090  450 PHE A CE2 
3811 C CZ  . PHE A 450 ? 0.1879 0.2741 0.2476 -0.0418 0.0021  0.0119  450 PHE A CZ  
3812 N N   . TRP A 451 ? 0.1607 0.1678 0.1869 -0.0380 0.0049  0.0165  451 TRP A N   
3813 C CA  . TRP A 451 ? 0.1792 0.1677 0.2038 -0.0343 0.0064  0.0220  451 TRP A CA  
3814 C C   . TRP A 451 ? 0.1880 0.1647 0.2142 -0.0311 0.0015  0.0110  451 TRP A C   
3815 O O   . TRP A 451 ? 0.2086 0.1648 0.2426 -0.0335 0.0017  0.0102  451 TRP A O   
3816 C CB  . TRP A 451 ? 0.1794 0.1717 0.1895 -0.0250 0.0074  0.0304  451 TRP A CB  
3817 C CG  . TRP A 451 ? 0.2448 0.2217 0.2519 -0.0170 0.0071  0.0373  451 TRP A CG  
3818 C CD1 . TRP A 451 ? 0.2574 0.2298 0.2656 -0.0088 0.0031  0.0318  451 TRP A CD1 
3819 C CD2 . TRP A 451 ? 0.2628 0.2278 0.2652 -0.0144 0.0120  0.0530  451 TRP A CD2 
3820 N NE1 . TRP A 451 ? 0.2619 0.2196 0.2685 -0.0008 0.0041  0.0425  451 TRP A NE1 
3821 C CE2 . TRP A 451 ? 0.2971 0.2490 0.2992 -0.0043 0.0092  0.0564  451 TRP A CE2 
3822 C CE3 . TRP A 451 ? 0.3922 0.3568 0.3908 -0.0185 0.0200  0.0658  451 TRP A CE3 
3823 C CZ2 . TRP A 451 ? 0.3930 0.3301 0.3902 0.0020  0.0126  0.0735  451 TRP A CZ2 
3824 C CZ3 . TRP A 451 ? 0.5515 0.5023 0.5430 -0.0129 0.0247  0.0832  451 TRP A CZ3 
3825 C CH2 . TRP A 451 ? 0.5478 0.4841 0.5384 -0.0028 0.0202  0.0875  451 TRP A CH2 
3826 N N   . TRP A 452 ? 0.1827 0.1710 0.2019 -0.0255 -0.0019 0.0025  452 TRP A N   
3827 C CA  . TRP A 452 ? 0.1880 0.1677 0.2045 -0.0189 -0.0041 -0.0081 452 TRP A CA  
3828 C C   . TRP A 452 ? 0.2337 0.2086 0.2522 -0.0252 -0.0087 -0.0219 452 TRP A C   
3829 O O   . TRP A 452 ? 0.2205 0.1795 0.2363 -0.0210 -0.0104 -0.0329 452 TRP A O   
3830 C CB  . TRP A 452 ? 0.1747 0.1722 0.1843 -0.0104 -0.0036 -0.0096 452 TRP A CB  
3831 C CG  . TRP A 452 ? 0.1799 0.1831 0.1899 -0.0044 -0.0026 0.0011  452 TRP A CG  
3832 C CD1 . TRP A 452 ? 0.2064 0.2259 0.2147 -0.0060 -0.0036 0.0068  452 TRP A CD1 
3833 C CD2 . TRP A 452 ? 0.1852 0.1771 0.1973 0.0046  -0.0020 0.0069  452 TRP A CD2 
3834 N NE1 . TRP A 452 ? 0.1935 0.2150 0.2016 0.0007  -0.0054 0.0144  452 TRP A NE1 
3835 C CE2 . TRP A 452 ? 0.1771 0.1831 0.1876 0.0079  -0.0043 0.0162  452 TRP A CE2 
3836 C CE3 . TRP A 452 ? 0.2337 0.2035 0.2489 0.0108  -0.0005 0.0049  452 TRP A CE3 
3837 C CZ2 . TRP A 452 ? 0.1967 0.1996 0.2086 0.0181  -0.0061 0.0250  452 TRP A CZ2 
3838 C CZ3 . TRP A 452 ? 0.2590 0.2228 0.2768 0.0216  -0.0004 0.0148  452 TRP A CZ3 
3839 C CH2 . TRP A 452 ? 0.2337 0.2159 0.2496 0.0255  -0.0037 0.0256  452 TRP A CH2 
3840 N N   . GLN A 453 ? 0.1866 0.1746 0.2097 -0.0343 -0.0116 -0.0223 453 GLN A N   
3841 C CA  . GLN A 453 ? 0.1971 0.1856 0.2217 -0.0402 -0.0194 -0.0357 453 GLN A CA  
3842 C C   . GLN A 453 ? 0.2209 0.1873 0.2599 -0.0494 -0.0226 -0.0408 453 GLN A C   
3843 O O   . GLN A 453 ? 0.2647 0.2226 0.3176 -0.0552 -0.0175 -0.0291 453 GLN A O   
3844 C CB  . GLN A 453 ? 0.1998 0.2113 0.2292 -0.0460 -0.0223 -0.0322 453 GLN A CB  
3845 C CG  . GLN A 453 ? 0.2378 0.2548 0.2743 -0.0541 -0.0330 -0.0433 453 GLN A CG  
3846 C CD  . GLN A 453 ? 0.2986 0.3186 0.3146 -0.0471 -0.0397 -0.0571 453 GLN A CD  
3847 O OE1 . GLN A 453 ? 0.3122 0.3268 0.3118 -0.0365 -0.0344 -0.0590 453 GLN A OE1 
3848 N NE2 . GLN A 453 ? 0.2481 0.2790 0.2650 -0.0521 -0.0515 -0.0664 453 GLN A NE2 
3849 N N   . GLY A 454 ? 0.2434 0.1996 0.2785 -0.0508 -0.0309 -0.0586 454 GLY A N   
3850 C CA  . GLY A 454 ? 0.3214 0.2563 0.3743 -0.0628 -0.0364 -0.0660 454 GLY A CA  
3851 C C   . GLY A 454 ? 0.4028 0.3066 0.4625 -0.0604 -0.0294 -0.0602 454 GLY A C   
3852 O O   . GLY A 454 ? 0.4347 0.3240 0.5165 -0.0723 -0.0281 -0.0530 454 GLY A O   
3853 N N   . GLU A 455 ? 0.4714 0.3663 0.5148 -0.0447 -0.0240 -0.0607 455 GLU A N   
3854 C CA  . GLU A 455 ? 0.5181 0.3816 0.5657 -0.0381 -0.0187 -0.0569 455 GLU A CA  
3855 C C   . GLU A 455 ? 0.6120 0.4558 0.6466 -0.0279 -0.0222 -0.0792 455 GLU A C   
3856 O O   . GLU A 455 ? 0.5349 0.3915 0.5546 -0.0265 -0.0284 -0.0961 455 GLU A O   
3857 C CB  . GLU A 455 ? 0.4490 0.3219 0.4913 -0.0262 -0.0097 -0.0372 455 GLU A CB  
3858 C CG  . GLU A 455 ? 0.4515 0.3455 0.4993 -0.0340 -0.0060 -0.0185 455 GLU A CG  
3859 C CD  . GLU A 455 ? 0.5160 0.3925 0.5819 -0.0452 -0.0019 -0.0049 455 GLU A CD  
3860 O OE1 . GLU A 455 ? 0.5206 0.3652 0.5959 -0.0458 -0.0013 -0.0063 455 GLU A OE1 
3861 O OE2 . GLU A 455 ? 0.3907 0.2846 0.4622 -0.0528 0.0021  0.0078  455 GLU A OE2 
3862 N N   . GLU A 456 ? 0.6663 0.4780 0.7051 -0.0194 -0.0178 -0.0789 456 GLU A N   
3863 C CA  . GLU A 456 ? 0.7202 0.5124 0.7448 -0.0053 -0.0183 -0.1001 456 GLU A CA  
3864 C C   . GLU A 456 ? 0.7211 0.5418 0.7278 0.0128  -0.0116 -0.0978 456 GLU A C   
3865 O O   . GLU A 456 ? 0.6732 0.5146 0.6839 0.0174  -0.0058 -0.0775 456 GLU A O   
3866 C CB  . GLU A 456 ? 0.7935 0.5422 0.8300 0.0013  -0.0141 -0.0987 456 GLU A CB  
3867 C CG  . GLU A 456 ? 0.9279 0.6392 0.9605 0.0015  -0.0205 -0.1280 456 GLU A CG  
3868 C CD  . GLU A 456 ? 1.0345 0.6957 1.0856 0.0030  -0.0174 -0.1250 456 GLU A CD  
3869 O OE1 . GLU A 456 ? 1.0257 0.6813 1.0827 0.0165  -0.0077 -0.1037 456 GLU A OE1 
3870 O OE2 . GLU A 456 ? 1.0843 0.7171 1.1397 -0.0095 -0.0242 -0.1401 456 GLU A OE2 
3871 N N   . LYS A 457 ? 0.6606 0.4837 0.6474 0.0224  -0.0125 -0.1187 457 LYS A N   
3872 C CA  . LYS A 457 ? 0.5990 0.4528 0.5711 0.0378  -0.0045 -0.1157 457 LYS A CA  
3873 C C   . LYS A 457 ? 0.6059 0.4601 0.5890 0.0536  0.0054  -0.1004 457 LYS A C   
3874 O O   . LYS A 457 ? 0.5631 0.3861 0.5553 0.0612  0.0076  -0.1013 457 LYS A O   
3875 C CB  . LYS A 457 ? 0.7274 0.5784 0.6741 0.0490  -0.0042 -0.1407 457 LYS A CB  
3876 C CG  . LYS A 457 ? 0.7778 0.6673 0.7082 0.0597  0.0039  -0.1362 457 LYS A CG  
3877 C CD  . LYS A 457 ? 0.8388 0.7352 0.7728 0.0811  0.0183  -0.1303 457 LYS A CD  
3878 C CE  . LYS A 457 ? 0.8857 0.8202 0.8064 0.0906  0.0282  -0.1258 457 LYS A CE  
3879 N NZ  . LYS A 457 ? 0.8528 0.8193 0.7918 0.0826  0.0298  -0.1010 457 LYS A NZ  
3880 N N   . ALA A 458 ? 0.5132 0.4031 0.4976 0.0582  0.0105  -0.0857 458 ALA A N   
3881 C CA  . ALA A 458 ? 0.4870 0.3874 0.4848 0.0716  0.0170  -0.0698 458 ALA A CA  
3882 C C   . ALA A 458 ? 0.4633 0.4033 0.4581 0.0785  0.0233  -0.0658 458 ALA A C   
3883 O O   . ALA A 458 ? 0.4321 0.3910 0.4170 0.0685  0.0215  -0.0673 458 ALA A O   
3884 C CB  . ALA A 458 ? 0.4241 0.3254 0.4358 0.0618  0.0127  -0.0487 458 ALA A CB  
3885 N N   . PRO A 459 ? 0.4052 0.3593 0.4112 0.0953  0.0309  -0.0591 459 PRO A N   
3886 C CA  . PRO A 459 ? 0.5005 0.4939 0.5090 0.1003  0.0384  -0.0541 459 PRO A CA  
3887 C C   . PRO A 459 ? 0.4733 0.4921 0.4881 0.0838  0.0327  -0.0400 459 PRO A C   
3888 O O   . PRO A 459 ? 0.3784 0.3919 0.4007 0.0742  0.0245  -0.0298 459 PRO A O   
3889 C CB  . PRO A 459 ? 0.5183 0.5231 0.5472 0.1197  0.0454  -0.0463 459 PRO A CB  
3890 C CG  . PRO A 459 ? 0.4901 0.4615 0.5258 0.1241  0.0398  -0.0436 459 PRO A CG  
3891 C CD  . PRO A 459 ? 0.4396 0.3740 0.4576 0.1122  0.0343  -0.0572 459 PRO A CD  
3892 N N   . PHE A 460 ? 0.4043 0.4483 0.4134 0.0811  0.0380  -0.0398 460 PHE A N   
3893 C CA  . PHE A 460 ? 0.3505 0.4191 0.3674 0.0679  0.0350  -0.0273 460 PHE A CA  
3894 C C   . PHE A 460 ? 0.2838 0.3405 0.2909 0.0508  0.0254  -0.0274 460 PHE A C   
3895 O O   . PHE A 460 ? 0.2777 0.3508 0.2881 0.0410  0.0238  -0.0195 460 PHE A O   
3896 C CB  . PHE A 460 ? 0.3624 0.4491 0.4049 0.0690  0.0323  -0.0132 460 PHE A CB  
3897 C CG  . PHE A 460 ? 0.4075 0.5179 0.4680 0.0842  0.0421  -0.0097 460 PHE A CG  
3898 C CD1 . PHE A 460 ? 0.4816 0.6190 0.5464 0.0853  0.0530  -0.0069 460 PHE A CD1 
3899 C CD2 . PHE A 460 ? 0.3962 0.5030 0.4710 0.0987  0.0419  -0.0076 460 PHE A CD2 
3900 C CE1 . PHE A 460 ? 0.4441 0.6074 0.5294 0.0997  0.0644  -0.0024 460 PHE A CE1 
3901 C CE2 . PHE A 460 ? 0.3516 0.4837 0.4469 0.1144  0.0518  -0.0040 460 PHE A CE2 
3902 C CZ  . PHE A 460 ? 0.3445 0.5065 0.4463 0.1146  0.0637  -0.0016 460 PHE A CZ  
3903 N N   . VAL A 461 ? 0.3897 0.4187 0.3878 0.0470  0.0195  -0.0357 461 VAL A N   
3904 C CA  . VAL A 461 ? 0.4398 0.4631 0.4340 0.0314  0.0117  -0.0340 461 VAL A CA  
3905 C C   . VAL A 461 ? 0.3808 0.4145 0.3611 0.0264  0.0114  -0.0394 461 VAL A C   
3906 O O   . VAL A 461 ? 0.4093 0.4481 0.3903 0.0154  0.0065  -0.0346 461 VAL A O   
3907 C CB  . VAL A 461 ? 0.5919 0.5858 0.5858 0.0264  0.0062  -0.0394 461 VAL A CB  
3908 C CG1 . VAL A 461 ? 0.5108 0.4944 0.5168 0.0313  0.0064  -0.0290 461 VAL A CG1 
3909 C CG2 . VAL A 461 ? 0.6690 0.6441 0.6508 0.0315  0.0061  -0.0575 461 VAL A CG2 
3910 N N   . GLU A 462 ? 0.2641 0.3024 0.2304 0.0362  0.0170  -0.0484 462 GLU A N   
3911 C CA  . GLU A 462 ? 0.3494 0.4024 0.3003 0.0338  0.0175  -0.0491 462 GLU A CA  
3912 C C   . GLU A 462 ? 0.2997 0.3756 0.2624 0.0286  0.0211  -0.0321 462 GLU A C   
3913 O O   . GLU A 462 ? 0.2810 0.3650 0.2365 0.0229  0.0188  -0.0279 462 GLU A O   
3914 C CB  . GLU A 462 ? 0.4619 0.5185 0.3920 0.0479  0.0254  -0.0599 462 GLU A CB  
3915 C CG  . GLU A 462 ? 0.6439 0.7175 0.5837 0.0607  0.0397  -0.0525 462 GLU A CG  
3916 C CD  . GLU A 462 ? 0.7948 0.8525 0.7446 0.0714  0.0422  -0.0595 462 GLU A CD  
3917 O OE1 . GLU A 462 ? 0.8819 0.9556 0.8433 0.0838  0.0537  -0.0541 462 GLU A OE1 
3918 O OE2 . GLU A 462 ? 0.8183 0.8483 0.7674 0.0676  0.0333  -0.0689 462 GLU A OE2 
3919 N N   . VAL A 463 ? 0.2041 0.2897 0.1864 0.0304  0.0256  -0.0225 463 VAL A N   
3920 C CA  . VAL A 463 ? 0.2286 0.3327 0.2249 0.0235  0.0274  -0.0087 463 VAL A CA  
3921 C C   . VAL A 463 ? 0.1978 0.2934 0.1975 0.0111  0.0180  -0.0055 463 VAL A C   
3922 O O   . VAL A 463 ? 0.1632 0.2659 0.1642 0.0048  0.0179  0.0014  463 VAL A O   
3923 C CB  . VAL A 463 ? 0.2316 0.3508 0.2509 0.0277  0.0319  -0.0011 463 VAL A CB  
3924 C CG1 . VAL A 463 ? 0.2704 0.4069 0.3068 0.0184  0.0327  0.0111  463 VAL A CG1 
3925 C CG2 . VAL A 463 ? 0.2255 0.3552 0.2430 0.0423  0.0437  -0.0041 463 VAL A CG2 
3926 N N   . PHE A 464 ? 0.1574 0.2369 0.1585 0.0084  0.0115  -0.0095 464 PHE A N   
3927 C CA  . PHE A 464 ? 0.1851 0.2580 0.1878 -0.0015 0.0052  -0.0069 464 PHE A CA  
3928 C C   . PHE A 464 ? 0.1786 0.2512 0.1713 -0.0056 0.0029  -0.0098 464 PHE A C   
3929 O O   . PHE A 464 ? 0.1591 0.2357 0.1552 -0.0114 0.0011  -0.0044 464 PHE A O   
3930 C CB  . PHE A 464 ? 0.1377 0.1940 0.1419 -0.0026 0.0013  -0.0088 464 PHE A CB  
3931 C CG  . PHE A 464 ? 0.1751 0.2337 0.1882 0.0014  0.0009  -0.0028 464 PHE A CG  
3932 C CD1 . PHE A 464 ? 0.1256 0.1890 0.1425 -0.0036 -0.0027 0.0034  464 PHE A CD1 
3933 C CD2 . PHE A 464 ? 0.1470 0.2041 0.1640 0.0117  0.0034  -0.0041 464 PHE A CD2 
3934 C CE1 . PHE A 464 ? 0.1333 0.2012 0.1561 0.0005  -0.0060 0.0083  464 PHE A CE1 
3935 C CE2 . PHE A 464 ? 0.1466 0.2093 0.1734 0.0168  0.0010  0.0028  464 PHE A CE2 
3936 C CZ  . PHE A 464 ? 0.1369 0.2059 0.1658 0.0105  -0.0048 0.0090  464 PHE A CZ  
3937 N N   . ASP A 465 ? 0.1730 0.2413 0.1532 -0.0015 0.0021  -0.0191 465 ASP A N   
3938 C CA  . ASP A 465 ? 0.1905 0.2619 0.1607 -0.0045 -0.0031 -0.0225 465 ASP A CA  
3939 C C   . ASP A 465 ? 0.1987 0.2865 0.1635 -0.0018 0.0013  -0.0131 465 ASP A C   
3940 O O   . ASP A 465 ? 0.1948 0.2877 0.1601 -0.0056 -0.0025 -0.0078 465 ASP A O   
3941 C CB  . ASP A 465 ? 0.2213 0.2832 0.1771 -0.0005 -0.0071 -0.0376 465 ASP A CB  
3942 C CG  . ASP A 465 ? 0.2823 0.3514 0.2250 -0.0021 -0.0149 -0.0426 465 ASP A CG  
3943 O OD1 . ASP A 465 ? 0.2148 0.2825 0.1671 -0.0108 -0.0237 -0.0438 465 ASP A OD1 
3944 O OD2 . ASP A 465 ? 0.2829 0.3618 0.2062 0.0062  -0.0120 -0.0438 465 ASP A OD2 
3945 N N   . LYS A 466 ? 0.2050 0.3018 0.1675 0.0052  0.0106  -0.0090 466 LYS A N   
3946 C CA  . LYS A 466 ? 0.1682 0.2796 0.1283 0.0069  0.0171  0.0034  466 LYS A CA  
3947 C C   . LYS A 466 ? 0.1962 0.3081 0.1752 -0.0015 0.0164  0.0146  466 LYS A C   
3948 O O   . LYS A 466 ? 0.2199 0.3350 0.1973 -0.0030 0.0162  0.0234  466 LYS A O   
3949 C CB  . LYS A 466 ? 0.2134 0.3369 0.1716 0.0156  0.0294  0.0069  466 LYS A CB  
3950 C CG  . LYS A 466 ? 0.2442 0.3828 0.2081 0.0148  0.0388  0.0243  466 LYS A CG  
3951 C CD  . LYS A 466 ? 0.4071 0.5621 0.3731 0.0232  0.0536  0.0301  466 LYS A CD  
3952 C CE  . LYS A 466 ? 0.5209 0.6891 0.4716 0.0281  0.0639  0.0439  466 LYS A CE  
3953 N NZ  . LYS A 466 ? 0.5577 0.7424 0.5023 0.0400  0.0800  0.0457  466 LYS A NZ  
3954 N N   . LEU A 467 ? 0.1971 0.3041 0.1923 -0.0059 0.0152  0.0137  467 LEU A N   
3955 C CA  . LEU A 467 ? 0.1778 0.2821 0.1876 -0.0134 0.0130  0.0200  467 LEU A CA  
3956 C C   . LEU A 467 ? 0.1792 0.2753 0.1850 -0.0166 0.0070  0.0187  467 LEU A C   
3957 O O   . LEU A 467 ? 0.1596 0.2555 0.1697 -0.0185 0.0078  0.0260  467 LEU A O   
3958 C CB  . LEU A 467 ? 0.1506 0.2519 0.1725 -0.0161 0.0102  0.0169  467 LEU A CB  
3959 C CG  . LEU A 467 ? 0.1151 0.2301 0.1511 -0.0141 0.0152  0.0212  467 LEU A CG  
3960 C CD1 . LEU A 467 ? 0.1058 0.2203 0.1502 -0.0130 0.0100  0.0172  467 LEU A CD1 
3961 C CD2 . LEU A 467 ? 0.1172 0.2399 0.1694 -0.0208 0.0185  0.0310  467 LEU A CD2 
3962 N N   . PHE A 468 ? 0.1718 0.2612 0.1727 -0.0171 0.0019  0.0103  468 PHE A N   
3963 C CA  . PHE A 468 ? 0.1896 0.2759 0.1923 -0.0201 -0.0027 0.0097  468 PHE A CA  
3964 C C   . PHE A 468 ? 0.2089 0.3033 0.2061 -0.0172 -0.0043 0.0147  468 PHE A C   
3965 O O   . PHE A 468 ? 0.1944 0.2894 0.1983 -0.0175 -0.0050 0.0206  468 PHE A O   
3966 C CB  . PHE A 468 ? 0.2032 0.2835 0.2048 -0.0222 -0.0071 0.0013  468 PHE A CB  
3967 C CG  . PHE A 468 ? 0.2039 0.2871 0.2119 -0.0255 -0.0114 0.0012  468 PHE A CG  
3968 C CD1 . PHE A 468 ? 0.1611 0.2424 0.1790 -0.0280 -0.0089 0.0050  468 PHE A CD1 
3969 C CD2 . PHE A 468 ? 0.2207 0.3105 0.2252 -0.0256 -0.0184 -0.0035 468 PHE A CD2 
3970 C CE1 . PHE A 468 ? 0.1157 0.2039 0.1440 -0.0300 -0.0112 0.0059  468 PHE A CE1 
3971 C CE2 . PHE A 468 ? 0.2114 0.3089 0.2278 -0.0290 -0.0235 -0.0029 468 PHE A CE2 
3972 C CZ  . PHE A 468 ? 0.1671 0.2648 0.1974 -0.0309 -0.0188 0.0027  468 PHE A CZ  
3973 N N   . ARG A 469 ? 0.1621 0.2629 0.1453 -0.0125 -0.0049 0.0125  469 ARG A N   
3974 C CA  . ARG A 469 ? 0.1436 0.2538 0.1170 -0.0082 -0.0085 0.0176  469 ARG A CA  
3975 C C   . ARG A 469 ? 0.1772 0.2905 0.1529 -0.0055 -0.0013 0.0331  469 ARG A C   
3976 O O   . ARG A 469 ? 0.1957 0.3134 0.1705 -0.0023 -0.0040 0.0420  469 ARG A O   
3977 C CB  . ARG A 469 ? 0.2140 0.3293 0.1660 -0.0030 -0.0120 0.0087  469 ARG A CB  
3978 C CG  . ARG A 469 ? 0.2181 0.3277 0.1715 -0.0075 -0.0222 -0.0068 469 ARG A CG  
3979 C CD  . ARG A 469 ? 0.2046 0.3149 0.1347 -0.0021 -0.0266 -0.0198 469 ARG A CD  
3980 N NE  . ARG A 469 ? 0.2225 0.3233 0.1570 -0.0083 -0.0370 -0.0359 469 ARG A NE  
3981 C CZ  . ARG A 469 ? 0.2497 0.3574 0.1852 -0.0124 -0.0509 -0.0428 469 ARG A CZ  
3982 N NH1 . ARG A 469 ? 0.2204 0.3457 0.1504 -0.0087 -0.0567 -0.0342 469 ARG A NH1 
3983 N NH2 . ARG A 469 ? 0.2608 0.3579 0.2052 -0.0204 -0.0597 -0.0576 469 ARG A NH2 
3984 N N   . SER A 470 ? 0.2129 0.3242 0.1951 -0.0071 0.0074  0.0374  470 SER A N   
3985 C CA  . SER A 470 ? 0.2379 0.3495 0.2289 -0.0076 0.0148  0.0525  470 SER A CA  
3986 C C   . SER A 470 ? 0.2019 0.3015 0.2096 -0.0124 0.0124  0.0547  470 SER A C   
3987 O O   . SER A 470 ? 0.2210 0.3168 0.2337 -0.0108 0.0148  0.0667  470 SER A O   
3988 C CB  . SER A 470 ? 0.2307 0.3464 0.2310 -0.0100 0.0239  0.0555  470 SER A CB  
3989 O OG  . SER A 470 ? 0.3910 0.5188 0.3750 -0.0027 0.0298  0.0556  470 SER A OG  
3990 N N   . PHE A 471 ? 0.1316 0.2238 0.1468 -0.0171 0.0086  0.0437  471 PHE A N   
3991 C CA  . PHE A 471 ? 0.1829 0.2635 0.2095 -0.0195 0.0073  0.0434  471 PHE A CA  
3992 C C   . PHE A 471 ? 0.2033 0.2859 0.2284 -0.0140 0.0039  0.0464  471 PHE A C   
3993 O O   . PHE A 471 ? 0.1818 0.2566 0.2153 -0.0115 0.0056  0.0531  471 PHE A O   
3994 C CB  . PHE A 471 ? 0.1595 0.2342 0.1886 -0.0236 0.0048  0.0318  471 PHE A CB  
3995 C CG  . PHE A 471 ? 0.1441 0.2187 0.1785 -0.0282 0.0058  0.0295  471 PHE A CG  
3996 C CD1 . PHE A 471 ? 0.1801 0.2523 0.2269 -0.0323 0.0087  0.0356  471 PHE A CD1 
3997 C CD2 . PHE A 471 ? 0.1390 0.2165 0.1692 -0.0284 0.0034  0.0223  471 PHE A CD2 
3998 C CE1 . PHE A 471 ? 0.2367 0.3137 0.2941 -0.0375 0.0079  0.0336  471 PHE A CE1 
3999 C CE2 . PHE A 471 ? 0.1328 0.2141 0.1706 -0.0311 0.0029  0.0211  471 PHE A CE2 
4000 C CZ  . PHE A 471 ? 0.1543 0.2376 0.2069 -0.0360 0.0046  0.0263  471 PHE A CZ  
4001 N N   . VAL A 472 ? 0.1861 0.2794 0.2030 -0.0119 -0.0016 0.0415  472 VAL A N   
4002 C CA  . VAL A 472 ? 0.1793 0.2808 0.1989 -0.0071 -0.0071 0.0443  472 VAL A CA  
4003 C C   . VAL A 472 ? 0.2065 0.3121 0.2215 0.0002  -0.0068 0.0589  472 VAL A C   
4004 O O   . VAL A 472 ? 0.2171 0.3227 0.2414 0.0058  -0.0080 0.0665  472 VAL A O   
4005 C CB  . VAL A 472 ? 0.2015 0.3142 0.2153 -0.0088 -0.0152 0.0347  472 VAL A CB  
4006 C CG1 . VAL A 472 ? 0.2565 0.3843 0.2724 -0.0036 -0.0239 0.0388  472 VAL A CG1 
4007 C CG2 . VAL A 472 ? 0.1601 0.2671 0.1835 -0.0153 -0.0143 0.0249  472 VAL A CG2 
4008 N N   . ARG A 473 ? 0.1790 0.2890 0.1794 0.0018  -0.0040 0.0644  473 ARG A N   
4009 C CA  . ARG A 473 ? 0.1907 0.3044 0.1839 0.0094  -0.0018 0.0818  473 ARG A CA  
4010 C C   . ARG A 473 ? 0.2318 0.3287 0.2417 0.0084  0.0065  0.0939  473 ARG A C   
4011 O O   . ARG A 473 ? 0.2221 0.3158 0.2366 0.0155  0.0062  0.1072  473 ARG A O   
4012 C CB  . ARG A 473 ? 0.3034 0.4264 0.2753 0.0120  0.0025  0.0854  473 ARG A CB  
4013 C CG  . ARG A 473 ? 0.3767 0.5051 0.3364 0.0208  0.0067  0.1063  473 ARG A CG  
4014 C CD  . ARG A 473 ? 0.4613 0.6039 0.3921 0.0264  0.0090  0.1059  473 ARG A CD  
4015 N NE  . ARG A 473 ? 0.6467 0.7877 0.5801 0.0231  0.0241  0.1116  473 ARG A NE  
4016 C CZ  . ARG A 473 ? 0.7301 0.8709 0.6655 0.0251  0.0369  0.1337  473 ARG A CZ  
4017 N NH1 . ARG A 473 ? 0.6389 0.7749 0.5743 0.0310  0.0353  0.1490  473 ARG A NH1 
4018 N NH2 . ARG A 473 ? 0.7255 0.8670 0.6708 0.0207  0.0496  0.1354  473 ARG A NH2 
4019 N N   . ARG A 474 ? 0.2369 0.3224 0.2572 -0.0003 0.0128  0.0892  474 ARG A N   
4020 C CA  . ARG A 474 ? 0.2393 0.3061 0.2772 -0.0038 0.0192  0.0976  474 ARG A CA  
4021 C C   . ARG A 474 ? 0.1976 0.2505 0.2471 -0.0006 0.0161  0.0933  474 ARG A C   
4022 O O   . ARG A 474 ? 0.2345 0.2705 0.2956 0.0019  0.0199  0.1034  474 ARG A O   
4023 C CB  . ARG A 474 ? 0.2368 0.2985 0.2849 -0.0148 0.0228  0.0896  474 ARG A CB  
4024 C CG  . ARG A 474 ? 0.2807 0.3222 0.3498 -0.0218 0.0270  0.0946  474 ARG A CG  
4025 C CD  . ARG A 474 ? 0.3698 0.4100 0.4445 -0.0211 0.0360  0.1173  474 ARG A CD  
4026 N NE  . ARG A 474 ? 0.4362 0.4545 0.5360 -0.0306 0.0398  0.1217  474 ARG A NE  
4027 C CZ  . ARG A 474 ? 0.6148 0.6079 0.7250 -0.0285 0.0389  0.1234  474 ARG A CZ  
4028 N NH1 . ARG A 474 ? 0.4842 0.4745 0.5836 -0.0160 0.0353  0.1229  474 ARG A NH1 
4029 N NH2 . ARG A 474 ? 0.7191 0.6896 0.8531 -0.0389 0.0415  0.1250  474 ARG A NH2 
4030 N N   . ALA A 475 ? 0.1955 0.2547 0.2431 0.0002  0.0105  0.0791  475 ALA A N   
4031 C CA  . ALA A 475 ? 0.1782 0.2293 0.2360 0.0052  0.0096  0.0741  475 ALA A CA  
4032 C C   . ALA A 475 ? 0.2471 0.3021 0.3099 0.0172  0.0081  0.0879  475 ALA A C   
4033 O O   . ALA A 475 ? 0.2379 0.2812 0.3131 0.0239  0.0105  0.0879  475 ALA A O   
4034 C CB  . ALA A 475 ? 0.1485 0.2119 0.2037 0.0036  0.0057  0.0602  475 ALA A CB  
4035 N N   . GLN A 476 ? 0.2455 0.3174 0.2974 0.0217  0.0039  0.0992  476 GLN A N   
4036 C CA  . GLN A 476 ? 0.2208 0.3014 0.2753 0.0346  -0.0003 0.1138  476 GLN A CA  
4037 C C   . GLN A 476 ? 0.2622 0.3293 0.3153 0.0398  0.0057  0.1353  476 GLN A C   
4038 O O   . GLN A 476 ? 0.3195 0.3919 0.3736 0.0524  0.0025  0.1513  476 GLN A O   
4039 C CB  . GLN A 476 ? 0.2470 0.3565 0.2881 0.0373  -0.0116 0.1121  476 GLN A CB  
4040 C CG  . GLN A 476 ? 0.2156 0.3369 0.2640 0.0311  -0.0170 0.0932  476 GLN A CG  
4041 C CD  . GLN A 476 ? 0.2674 0.4125 0.3032 0.0295  -0.0292 0.0871  476 GLN A CD  
4042 O OE1 . GLN A 476 ? 0.2753 0.4399 0.3148 0.0367  -0.0397 0.0920  476 GLN A OE1 
4043 N NE2 . GLN A 476 ? 0.2741 0.4172 0.2959 0.0205  -0.0286 0.0755  476 GLN A NE2 
4044 N N   . GLU A 477 ? 0.2898 0.3405 0.3434 0.0305  0.0144  0.1377  477 GLU A N   
4045 C CA  . GLU A 477 ? 0.4177 0.4544 0.4739 0.0336  0.0221  0.1608  477 GLU A CA  
4046 C C   . GLU A 477 ? 0.5210 0.5241 0.6005 0.0309  0.0286  0.1617  477 GLU A C   
4047 O O   . GLU A 477 ? 0.4187 0.4089 0.5076 0.0208  0.0294  0.1432  477 GLU A O   
4048 C CB  . GLU A 477 ? 0.5114 0.5551 0.5567 0.0250  0.0289  0.1668  477 GLU A CB  
4049 C CG  . GLU A 477 ? 0.6607 0.7334 0.6792 0.0292  0.0236  0.1645  477 GLU A CG  
4050 C CD  . GLU A 477 ? 0.6449 0.7249 0.6543 0.0221  0.0328  0.1672  477 GLU A CD  
4051 O OE1 . GLU A 477 ? 0.6707 0.7361 0.6981 0.0134  0.0431  0.1750  477 GLU A OE1 
4052 O OE2 . GLU A 477 ? 0.6588 0.7593 0.6449 0.0252  0.0297  0.1610  477 GLU A OE2 
4053 N N   . LYS B 2   ? 0.3715 0.5555 0.1977 -0.0609 0.0142  -0.0941 2   LYS B N   
4054 C CA  . LYS B 2   ? 0.3728 0.5473 0.2107 -0.0587 0.0211  -0.0975 2   LYS B CA  
4055 C C   . LYS B 2   ? 0.3800 0.5361 0.2304 -0.0561 0.0173  -0.0962 2   LYS B C   
4056 O O   . LYS B 2   ? 0.4094 0.5591 0.2713 -0.0541 0.0152  -0.1078 2   LYS B O   
4057 C CB  . LYS B 2   ? 0.4816 0.6605 0.3297 -0.0564 0.0278  -0.1150 2   LYS B CB  
4058 C CG  . LYS B 2   ? 0.5830 0.7566 0.4420 -0.0540 0.0358  -0.1166 2   LYS B CG  
4059 C CD  . LYS B 2   ? 0.6719 0.8347 0.5498 -0.0495 0.0378  -0.1321 2   LYS B CD  
4060 C CE  . LYS B 2   ? 0.7030 0.8751 0.5865 -0.0476 0.0427  -0.1469 2   LYS B CE  
4061 N NZ  . LYS B 2   ? 0.6303 0.7903 0.5324 -0.0434 0.0425  -0.1614 2   LYS B NZ  
4062 N N   . LYS B 3   ? 0.3242 0.4689 0.1770 -0.0554 0.0162  -0.0797 3   LYS B N   
4063 C CA  . LYS B 3   ? 0.3343 0.4592 0.2022 -0.0517 0.0125  -0.0743 3   LYS B CA  
4064 C C   . LYS B 3   ? 0.3266 0.4406 0.2099 -0.0485 0.0187  -0.0765 3   LYS B C   
4065 O O   . LYS B 3   ? 0.3343 0.4551 0.2161 -0.0492 0.0255  -0.0780 3   LYS B O   
4066 C CB  . LYS B 3   ? 0.3532 0.4713 0.2153 -0.0522 0.0069  -0.0556 3   LYS B CB  
4067 C CG  . LYS B 3   ? 0.4122 0.5421 0.2582 -0.0551 0.0001  -0.0504 3   LYS B CG  
4068 C CD  . LYS B 3   ? 0.5342 0.6536 0.3859 -0.0526 -0.0081 -0.0431 3   LYS B CD  
4069 C CE  . LYS B 3   ? 0.5947 0.7253 0.4315 -0.0547 -0.0156 -0.0349 3   LYS B CE  
4070 N NZ  . LYS B 3   ? 0.6699 0.7879 0.5121 -0.0516 -0.0222 -0.0216 3   LYS B NZ  
4071 N N   . LEU B 4   ? 0.2574 0.3555 0.1557 -0.0450 0.0163  -0.0763 4   LEU B N   
4072 C CA  . LEU B 4   ? 0.2450 0.3307 0.1567 -0.0419 0.0200  -0.0730 4   LEU B CA  
4073 C C   . LEU B 4   ? 0.2372 0.3125 0.1477 -0.0416 0.0161  -0.0568 4   LEU B C   
4074 O O   . LEU B 4   ? 0.3062 0.3765 0.2158 -0.0411 0.0098  -0.0519 4   LEU B O   
4075 C CB  . LEU B 4   ? 0.2935 0.3687 0.2228 -0.0383 0.0203  -0.0828 4   LEU B CB  
4076 C CG  . LEU B 4   ? 0.2255 0.2882 0.1693 -0.0346 0.0233  -0.0791 4   LEU B CG  
4077 C CD1 . LEU B 4   ? 0.2677 0.3262 0.2269 -0.0315 0.0264  -0.0922 4   LEU B CD1 
4078 C CD2 . LEU B 4   ? 0.2148 0.2640 0.1632 -0.0332 0.0184  -0.0675 4   LEU B CD2 
4079 N N   . PHE B 5   ? 0.2327 0.3049 0.1445 -0.0416 0.0197  -0.0493 5   PHE B N   
4080 C CA  . PHE B 5   ? 0.2263 0.2875 0.1381 -0.0413 0.0165  -0.0353 5   PHE B CA  
4081 C C   . PHE B 5   ? 0.2325 0.2803 0.1598 -0.0373 0.0172  -0.0356 5   PHE B C   
4082 O O   . PHE B 5   ? 0.2747 0.3229 0.2104 -0.0360 0.0222  -0.0405 5   PHE B O   
4083 C CB  . PHE B 5   ? 0.2317 0.2983 0.1346 -0.0450 0.0194  -0.0263 5   PHE B CB  
4084 C CG  . PHE B 5   ? 0.2994 0.3795 0.1856 -0.0493 0.0183  -0.0233 5   PHE B CG  
4085 C CD1 . PHE B 5   ? 0.3654 0.4446 0.2437 -0.0496 0.0114  -0.0178 5   PHE B CD1 
4086 C CD2 . PHE B 5   ? 0.2552 0.3501 0.1340 -0.0529 0.0242  -0.0259 5   PHE B CD2 
4087 C CE1 . PHE B 5   ? 0.3464 0.4390 0.2087 -0.0535 0.0098  -0.0141 5   PHE B CE1 
4088 C CE2 . PHE B 5   ? 0.3115 0.4205 0.1737 -0.0573 0.0235  -0.0225 5   PHE B CE2 
4089 C CZ  . PHE B 5   ? 0.2987 0.4065 0.1521 -0.0576 0.0159  -0.0162 5   PHE B CZ  
4090 N N   . LEU B 6   ? 0.2069 0.2440 0.1378 -0.0353 0.0122  -0.0299 6   LEU B N   
4091 C CA  . LEU B 6   ? 0.2087 0.2340 0.1530 -0.0316 0.0122  -0.0297 6   LEU B CA  
4092 C C   . LEU B 6   ? 0.2940 0.3105 0.2370 -0.0311 0.0099  -0.0182 6   LEU B C   
4093 O O   . LEU B 6   ? 0.2256 0.2404 0.1614 -0.0317 0.0054  -0.0114 6   LEU B O   
4094 C CB  . LEU B 6   ? 0.1953 0.2172 0.1463 -0.0297 0.0088  -0.0347 6   LEU B CB  
4095 C CG  . LEU B 6   ? 0.1884 0.1995 0.1532 -0.0263 0.0089  -0.0345 6   LEU B CG  
4096 C CD1 . LEU B 6   ? 0.2468 0.2570 0.2212 -0.0249 0.0141  -0.0404 6   LEU B CD1 
4097 C CD2 . LEU B 6   ? 0.1985 0.2086 0.1688 -0.0258 0.0055  -0.0388 6   LEU B CD2 
4098 N N   . VAL B 7   ? 0.1989 0.2098 0.1491 -0.0298 0.0126  -0.0163 7   VAL B N   
4099 C CA  . VAL B 7   ? 0.1813 0.1841 0.1306 -0.0297 0.0108  -0.0070 7   VAL B CA  
4100 C C   . VAL B 7   ? 0.1894 0.1837 0.1499 -0.0260 0.0107  -0.0076 7   VAL B C   
4101 O O   . VAL B 7   ? 0.1998 0.1952 0.1681 -0.0250 0.0142  -0.0112 7   VAL B O   
4102 C CB  . VAL B 7   ? 0.1849 0.1916 0.1302 -0.0332 0.0140  -0.0031 7   VAL B CB  
4103 C CG1 . VAL B 7   ? 0.2293 0.2270 0.1725 -0.0340 0.0112  0.0063  7   VAL B CG1 
4104 C CG2 . VAL B 7   ? 0.2182 0.2361 0.1525 -0.0372 0.0152  -0.0032 7   VAL B CG2 
4105 N N   . PHE B 8   ? 0.2356 0.2226 0.1972 -0.0237 0.0068  -0.0039 8   PHE B N   
4106 C CA  . PHE B 8   ? 0.2063 0.1863 0.1765 -0.0206 0.0067  -0.0029 8   PHE B CA  
4107 C C   . PHE B 8   ? 0.2050 0.1794 0.1726 -0.0210 0.0059  0.0034  8   PHE B C   
4108 O O   . PHE B 8   ? 0.2016 0.1732 0.1622 -0.0223 0.0032  0.0085  8   PHE B O   
4109 C CB  . PHE B 8   ? 0.1963 0.1729 0.1698 -0.0180 0.0036  -0.0028 8   PHE B CB  
4110 C CG  . PHE B 8   ? 0.2046 0.1853 0.1835 -0.0178 0.0041  -0.0095 8   PHE B CG  
4111 C CD1 . PHE B 8   ? 0.2301 0.2088 0.2194 -0.0163 0.0063  -0.0128 8   PHE B CD1 
4112 C CD2 . PHE B 8   ? 0.2297 0.2162 0.2033 -0.0195 0.0019  -0.0122 8   PHE B CD2 
4113 C CE1 . PHE B 8   ? 0.2341 0.2150 0.2296 -0.0167 0.0065  -0.0192 8   PHE B CE1 
4114 C CE2 . PHE B 8   ? 0.2512 0.2413 0.2303 -0.0200 0.0020  -0.0194 8   PHE B CE2 
4115 C CZ  . PHE B 8   ? 0.2571 0.2437 0.2477 -0.0187 0.0044  -0.0231 8   PHE B CZ  
4116 N N   . TRP B 9   ? 0.1636 0.1362 0.1373 -0.0200 0.0078  0.0033  9   TRP B N   
4117 C CA  . TRP B 9   ? 0.1893 0.1568 0.1616 -0.0207 0.0067  0.0080  9   TRP B CA  
4118 C C   . TRP B 9   ? 0.2206 0.1846 0.1998 -0.0173 0.0065  0.0076  9   TRP B C   
4119 O O   . TRP B 9   ? 0.2055 0.1726 0.1911 -0.0165 0.0088  0.0057  9   TRP B O   
4120 C CB  . TRP B 9   ? 0.2080 0.1802 0.1794 -0.0243 0.0093  0.0086  9   TRP B CB  
4121 C CG  . TRP B 9   ? 0.2173 0.1849 0.1858 -0.0270 0.0078  0.0135  9   TRP B CG  
4122 C CD1 . TRP B 9   ? 0.2830 0.2416 0.2502 -0.0258 0.0044  0.0165  9   TRP B CD1 
4123 C CD2 . TRP B 9   ? 0.2040 0.1762 0.1715 -0.0316 0.0098  0.0154  9   TRP B CD2 
4124 N NE1 . TRP B 9   ? 0.1905 0.1466 0.1561 -0.0296 0.0038  0.0197  9   TRP B NE1 
4125 C CE2 . TRP B 9   ? 0.2169 0.1814 0.1827 -0.0336 0.0070  0.0196  9   TRP B CE2 
4126 C CE3 . TRP B 9   ? 0.2552 0.2379 0.2235 -0.0344 0.0138  0.0134  9   TRP B CE3 
4127 C CZ2 . TRP B 9   ? 0.2157 0.1824 0.1814 -0.0389 0.0079  0.0225  9   TRP B CZ2 
4128 C CZ3 . TRP B 9   ? 0.2471 0.2333 0.2149 -0.0395 0.0151  0.0166  9   TRP B CZ3 
4129 C CH2 . TRP B 9   ? 0.2618 0.2398 0.2284 -0.0420 0.0121  0.0214  9   TRP B CH2 
4130 N N   . TRP B 10  ? 0.1857 0.1441 0.1636 -0.0150 0.0038  0.0097  10  TRP B N   
4131 C CA  . TRP B 10  ? 0.1948 0.1514 0.1778 -0.0118 0.0038  0.0096  10  TRP B CA  
4132 C C   . TRP B 10  ? 0.2457 0.1989 0.2269 -0.0122 0.0027  0.0116  10  TRP B C   
4133 O O   . TRP B 10  ? 0.2064 0.1544 0.1827 -0.0128 0.0004  0.0134  10  TRP B O   
4134 C CB  . TRP B 10  ? 0.2004 0.1551 0.1835 -0.0091 0.0019  0.0098  10  TRP B CB  
4135 C CG  . TRP B 10  ? 0.1954 0.1538 0.1811 -0.0090 0.0022  0.0073  10  TRP B CG  
4136 C CD1 . TRP B 10  ? 0.1903 0.1495 0.1723 -0.0092 -0.0002 0.0074  10  TRP B CD1 
4137 C CD2 . TRP B 10  ? 0.2125 0.1743 0.2058 -0.0088 0.0043  0.0044  10  TRP B CD2 
4138 N NE1 . TRP B 10  ? 0.1739 0.1377 0.1602 -0.0096 0.0004  0.0039  10  TRP B NE1 
4139 C CE2 . TRP B 10  ? 0.1944 0.1589 0.1880 -0.0094 0.0032  0.0018  10  TRP B CE2 
4140 C CE3 . TRP B 10  ? 0.2074 0.1698 0.2076 -0.0081 0.0067  0.0040  10  TRP B CE3 
4141 C CZ2 . TRP B 10  ? 0.1923 0.1593 0.1933 -0.0099 0.0046  -0.0020 10  TRP B CZ2 
4142 C CZ3 . TRP B 10  ? 0.2092 0.1732 0.2171 -0.0081 0.0081  0.0011  10  TRP B CZ3 
4143 C CH2 . TRP B 10  ? 0.2070 0.1728 0.2154 -0.0092 0.0071  -0.0023 10  TRP B CH2 
4144 N N   . HIS B 11  ? 0.1531 0.1093 0.1387 -0.0119 0.0040  0.0113  11  HIS B N   
4145 C CA  . HIS B 11  ? 0.1936 0.1484 0.1778 -0.0130 0.0028  0.0124  11  HIS B CA  
4146 C C   . HIS B 11  ? 0.1491 0.1024 0.1333 -0.0098 0.0015  0.0125  11  HIS B C   
4147 O O   . HIS B 11  ? 0.1910 0.1478 0.1794 -0.0074 0.0027  0.0128  11  HIS B O   
4148 C CB  . HIS B 11  ? 0.1760 0.1371 0.1651 -0.0146 0.0045  0.0121  11  HIS B CB  
4149 C CG  . HIS B 11  ? 0.1624 0.1249 0.1524 -0.0148 0.0029  0.0128  11  HIS B CG  
4150 N ND1 . HIS B 11  ? 0.1773 0.1362 0.1631 -0.0178 0.0007  0.0129  11  HIS B ND1 
4151 C CD2 . HIS B 11  ? 0.1796 0.1468 0.1742 -0.0126 0.0029  0.0135  11  HIS B CD2 
4152 C CE1 . HIS B 11  ? 0.2087 0.1709 0.1962 -0.0175 -0.0007 0.0126  11  HIS B CE1 
4153 N NE2 . HIS B 11  ? 0.1851 0.1528 0.1774 -0.0143 0.0005  0.0135  11  HIS B NE2 
4154 N N   . MET B 12  ? 0.1913 0.1390 0.1707 -0.0099 -0.0008 0.0121  12  MET B N   
4155 C CA  . MET B 12  ? 0.1639 0.1108 0.1421 -0.0067 -0.0018 0.0110  12  MET B CA  
4156 C C   . MET B 12  ? 0.2274 0.1744 0.2038 -0.0084 -0.0034 0.0097  12  MET B C   
4157 O O   . MET B 12  ? 0.2107 0.1527 0.1849 -0.0116 -0.0051 0.0091  12  MET B O   
4158 C CB  . MET B 12  ? 0.2183 0.1588 0.1934 -0.0045 -0.0033 0.0100  12  MET B CB  
4159 C CG  . MET B 12  ? 0.2129 0.1537 0.1893 -0.0035 -0.0028 0.0112  12  MET B CG  
4160 S SD  . MET B 12  ? 0.2193 0.1680 0.2017 -0.0014 0.0001  0.0115  12  MET B SD  
4161 C CE  . MET B 12  ? 0.2334 0.1817 0.2167 -0.0002 -0.0008 0.0114  12  MET B CE  
4162 N N   . HIS B 13  ? 0.1992 0.1521 0.1765 -0.0066 -0.0031 0.0096  13  HIS B N   
4163 C CA  . HIS B 13  ? 0.1998 0.1549 0.1753 -0.0084 -0.0052 0.0079  13  HIS B CA  
4164 C C   . HIS B 13  ? 0.2098 0.1710 0.1833 -0.0053 -0.0052 0.0074  13  HIS B C   
4165 O O   . HIS B 13  ? 0.1900 0.1562 0.1662 -0.0028 -0.0031 0.0105  13  HIS B O   
4166 C CB  . HIS B 13  ? 0.2078 0.1685 0.1878 -0.0115 -0.0050 0.0099  13  HIS B CB  
4167 C CG  . HIS B 13  ? 0.1804 0.1465 0.1600 -0.0132 -0.0074 0.0087  13  HIS B CG  
4168 N ND1 . HIS B 13  ? 0.1716 0.1332 0.1471 -0.0159 -0.0102 0.0049  13  HIS B ND1 
4169 C CD2 . HIS B 13  ? 0.1856 0.1613 0.1686 -0.0125 -0.0079 0.0108  13  HIS B CD2 
4170 C CE1 . HIS B 13  ? 0.2077 0.1770 0.1838 -0.0172 -0.0124 0.0041  13  HIS B CE1 
4171 N NE2 . HIS B 13  ? 0.1721 0.1504 0.1526 -0.0150 -0.0112 0.0080  13  HIS B NE2 
4172 N N   . GLN B 14  ? 0.1699 0.1309 0.1388 -0.0058 -0.0075 0.0035  14  GLN B N   
4173 C CA  . GLN B 14  ? 0.1802 0.1502 0.1460 -0.0041 -0.0081 0.0030  14  GLN B CA  
4174 C C   . GLN B 14  ? 0.2227 0.1943 0.1861 -0.0075 -0.0116 -0.0007 14  GLN B C   
4175 O O   . GLN B 14  ? 0.1881 0.1514 0.1497 -0.0098 -0.0136 -0.0054 14  GLN B O   
4176 C CB  . GLN B 14  ? 0.2153 0.1856 0.1763 -0.0001 -0.0069 -0.0003 14  GLN B CB  
4177 C CG  . GLN B 14  ? 0.1987 0.1694 0.1625 0.0031  -0.0035 0.0030  14  GLN B CG  
4178 C CD  . GLN B 14  ? 0.1976 0.1766 0.1654 0.0036  -0.0015 0.0096  14  GLN B CD  
4179 O OE1 . GLN B 14  ? 0.2173 0.2040 0.1840 0.0031  -0.0024 0.0121  14  GLN B OE1 
4180 N NE2 . GLN B 14  ? 0.1825 0.1599 0.1555 0.0045  0.0009  0.0127  14  GLN B NE2 
4181 N N   . PRO B 15  ? 0.2060 0.1882 0.1699 -0.0080 -0.0130 0.0016  15  PRO B N   
4182 C CA  . PRO B 15  ? 0.2167 0.2026 0.1776 -0.0111 -0.0169 -0.0029 15  PRO B CA  
4183 C C   . PRO B 15  ? 0.2183 0.2027 0.1712 -0.0095 -0.0179 -0.0100 15  PRO B C   
4184 O O   . PRO B 15  ? 0.2188 0.2029 0.1684 -0.0053 -0.0152 -0.0103 15  PRO B O   
4185 C CB  . PRO B 15  ? 0.2120 0.2116 0.1749 -0.0105 -0.0181 0.0023  15  PRO B CB  
4186 C CG  . PRO B 15  ? 0.1956 0.1979 0.1589 -0.0060 -0.0145 0.0080  15  PRO B CG  
4187 C CD  . PRO B 15  ? 0.1840 0.1754 0.1508 -0.0054 -0.0113 0.0082  15  PRO B CD  
4188 N N   . LEU B 16  ? 0.2059 0.1902 0.1559 -0.0129 -0.0218 -0.0163 16  LEU B N   
4189 C CA  . LEU B 16  ? 0.2078 0.1898 0.1505 -0.0114 -0.0229 -0.0253 16  LEU B CA  
4190 C C   . LEU B 16  ? 0.2478 0.2443 0.1836 -0.0082 -0.0224 -0.0251 16  LEU B C   
4191 O O   . LEU B 16  ? 0.2671 0.2751 0.2009 -0.0102 -0.0254 -0.0242 16  LEU B O   
4192 C CB  . LEU B 16  ? 0.2177 0.1946 0.1603 -0.0168 -0.0275 -0.0327 16  LEU B CB  
4193 C CG  . LEU B 16  ? 0.2891 0.2605 0.2256 -0.0156 -0.0291 -0.0441 16  LEU B CG  
4194 C CD1 . LEU B 16  ? 0.2607 0.2187 0.1980 -0.0112 -0.0260 -0.0458 16  LEU B CD1 
4195 C CD2 . LEU B 16  ? 0.2749 0.2402 0.2130 -0.0220 -0.0340 -0.0512 16  LEU B CD2 
4196 N N   . TYR B 17  ? 0.2930 0.2903 0.2251 -0.0033 -0.0188 -0.0257 17  TYR B N   
4197 C CA  . TYR B 17  ? 0.2445 0.2564 0.1693 -0.0004 -0.0174 -0.0249 17  TYR B CA  
4198 C C   . TYR B 17  ? 0.2593 0.2745 0.1752 0.0001  -0.0192 -0.0365 17  TYR B C   
4199 O O   . TYR B 17  ? 0.2534 0.2825 0.1615 0.0023  -0.0181 -0.0369 17  TYR B O   
4200 C CB  . TYR B 17  ? 0.3269 0.3402 0.2529 0.0041  -0.0121 -0.0198 17  TYR B CB  
4201 C CG  . TYR B 17  ? 0.2927 0.3045 0.2270 0.0037  -0.0103 -0.0090 17  TYR B CG  
4202 C CD1 . TYR B 17  ? 0.2779 0.2986 0.2144 0.0023  -0.0116 -0.0009 17  TYR B CD1 
4203 C CD2 . TYR B 17  ? 0.2189 0.2206 0.1593 0.0051  -0.0075 -0.0074 17  TYR B CD2 
4204 C CE1 . TYR B 17  ? 0.2985 0.3169 0.2436 0.0024  -0.0099 0.0077  17  TYR B CE1 
4205 C CE2 . TYR B 17  ? 0.2273 0.2278 0.1753 0.0046  -0.0059 0.0011  17  TYR B CE2 
4206 C CZ  . TYR B 17  ? 0.2704 0.2786 0.2210 0.0033  -0.0070 0.0081  17  TYR B CZ  
4207 O OH  . TYR B 17  ? 0.2671 0.2731 0.2260 0.0032  -0.0054 0.0152  17  TYR B OH  
4208 N N   . ARG B 18  ? 0.3155 0.3186 0.2325 -0.0020 -0.0219 -0.0458 18  ARG B N   
4209 C CA  . ARG B 18  ? 0.3209 0.3241 0.2307 -0.0012 -0.0235 -0.0589 18  ARG B CA  
4210 C C   . ARG B 18  ? 0.3482 0.3606 0.2534 -0.0060 -0.0289 -0.0632 18  ARG B C   
4211 O O   . ARG B 18  ? 0.2976 0.3030 0.2081 -0.0113 -0.0330 -0.0644 18  ARG B O   
4212 C CB  . ARG B 18  ? 0.2973 0.2809 0.2120 -0.0009 -0.0241 -0.0665 18  ARG B CB  
4213 C CG  . ARG B 18  ? 0.3132 0.2939 0.2226 0.0000  -0.0261 -0.0813 18  ARG B CG  
4214 C CD  . ARG B 18  ? 0.3612 0.3204 0.2776 -0.0010 -0.0280 -0.0871 18  ARG B CD  
4215 N NE  . ARG B 18  ? 0.4743 0.4285 0.3872 0.0028  -0.0282 -0.1016 18  ARG B NE  
4216 C CZ  . ARG B 18  ? 0.4898 0.4434 0.3990 -0.0004 -0.0324 -0.1137 18  ARG B CZ  
4217 N NH1 . ARG B 18  ? 0.4537 0.4124 0.3621 -0.0077 -0.0370 -0.1125 18  ARG B NH1 
4218 N NH2 . ARG B 18  ? 0.5212 0.4697 0.4279 0.0038  -0.0321 -0.1278 18  ARG B NH2 
4219 N N   . GLU B 19  ? 0.2798 0.3092 0.1753 -0.0043 -0.0290 -0.0653 19  GLU B N   
4220 C CA  . GLU B 19  ? 0.3359 0.3771 0.2259 -0.0086 -0.0346 -0.0695 19  GLU B CA  
4221 C C   . GLU B 19  ? 0.3907 0.4217 0.2794 -0.0115 -0.0383 -0.0853 19  GLU B C   
4222 O O   . GLU B 19  ? 0.4003 0.4253 0.2854 -0.0077 -0.0360 -0.0954 19  GLU B O   
4223 C CB  . GLU B 19  ? 0.3366 0.3989 0.2148 -0.0059 -0.0335 -0.0681 19  GLU B CB  
4224 C CG  . GLU B 19  ? 0.4041 0.4831 0.2784 -0.0097 -0.0391 -0.0643 19  GLU B CG  
4225 C CD  . GLU B 19  ? 0.4718 0.5575 0.3372 -0.0127 -0.0442 -0.0792 19  GLU B CD  
4226 O OE1 . GLU B 19  ? 0.4829 0.5594 0.3454 -0.0115 -0.0431 -0.0929 19  GLU B OE1 
4227 O OE2 . GLU B 19  ? 0.5345 0.6351 0.3961 -0.0160 -0.0497 -0.0773 19  GLU B OE2 
4228 N N   . PRO B 20  ? 0.3541 0.3831 0.2466 -0.0180 -0.0442 -0.0881 20  PRO B N   
4229 C CA  . PRO B 20  ? 0.4308 0.4456 0.3253 -0.0217 -0.0478 -0.1022 20  PRO B CA  
4230 C C   . PRO B 20  ? 0.4915 0.5148 0.3751 -0.0211 -0.0501 -0.1176 20  PRO B C   
4231 O O   . PRO B 20  ? 0.5331 0.5423 0.4179 -0.0218 -0.0516 -0.1310 20  PRO B O   
4232 C CB  . PRO B 20  ? 0.4032 0.4161 0.3063 -0.0297 -0.0530 -0.0986 20  PRO B CB  
4233 C CG  . PRO B 20  ? 0.4126 0.4451 0.3144 -0.0296 -0.0536 -0.0867 20  PRO B CG  
4234 C CD  . PRO B 20  ? 0.3604 0.3980 0.2584 -0.0224 -0.0475 -0.0777 20  PRO B CD  
4235 N N   . TYR B 21  ? 0.4053 0.4507 0.2781 -0.0197 -0.0507 -0.1164 21  TYR B N   
4236 C CA  . TYR B 21  ? 0.4552 0.5103 0.3163 -0.0192 -0.0527 -0.1320 21  TYR B CA  
4237 C C   . TYR B 21  ? 0.6337 0.6900 0.4876 -0.0114 -0.0462 -0.1378 21  TYR B C   
4238 O O   . TYR B 21  ? 0.7229 0.7732 0.5733 -0.0098 -0.0463 -0.1543 21  TYR B O   
4239 C CB  . TYR B 21  ? 0.3680 0.4483 0.2198 -0.0219 -0.0571 -0.1286 21  TYR B CB  
4240 C CG  . TYR B 21  ? 0.3592 0.4397 0.2186 -0.0298 -0.0643 -0.1263 21  TYR B CG  
4241 C CD1 . TYR B 21  ? 0.4206 0.4991 0.2794 -0.0359 -0.0708 -0.1414 21  TYR B CD1 
4242 C CD2 . TYR B 21  ? 0.4637 0.5463 0.3323 -0.0312 -0.0645 -0.1099 21  TYR B CD2 
4243 C CE1 . TYR B 21  ? 0.5066 0.5865 0.3739 -0.0437 -0.0773 -0.1393 21  TYR B CE1 
4244 C CE2 . TYR B 21  ? 0.4821 0.5663 0.3591 -0.0383 -0.0707 -0.1080 21  TYR B CE2 
4245 C CZ  . TYR B 21  ? 0.5251 0.6085 0.4016 -0.0447 -0.0771 -0.1224 21  TYR B CZ  
4246 O OH  . TYR B 21  ? 0.5513 0.6379 0.4371 -0.0522 -0.0832 -0.1206 21  TYR B OH  
4247 N N   . THR B 22  ? 0.5649 0.6286 0.4178 -0.0064 -0.0402 -0.1249 22  THR B N   
4248 C CA  . THR B 22  ? 0.4610 0.5277 0.3087 0.0008  -0.0335 -0.1292 22  THR B CA  
4249 C C   . THR B 22  ? 0.5074 0.5527 0.3664 0.0047  -0.0295 -0.1289 22  THR B C   
4250 O O   . THR B 22  ? 0.4558 0.5002 0.3128 0.0108  -0.0247 -0.1364 22  THR B O   
4251 C CB  . THR B 22  ? 0.4937 0.5809 0.3346 0.0037  -0.0290 -0.1154 22  THR B CB  
4252 O OG1 . THR B 22  ? 0.4311 0.5114 0.2824 0.0034  -0.0273 -0.0985 22  THR B OG1 
4253 C CG2 . THR B 22  ? 0.4380 0.5474 0.2675 0.0001  -0.0336 -0.1138 22  THR B CG2 
4254 N N   . GLY B 23  ? 0.4425 0.4718 0.3132 0.0014  -0.0313 -0.1204 23  GLY B N   
4255 C CA  . GLY B 23  ? 0.4142 0.4260 0.2945 0.0053  -0.0275 -0.1175 23  GLY B CA  
4256 C C   . GLY B 23  ? 0.4316 0.4512 0.3127 0.0101  -0.0213 -0.1052 23  GLY B C   
4257 O O   . GLY B 23  ? 0.4604 0.4680 0.3493 0.0138  -0.0181 -0.1027 23  GLY B O   
4258 N N   . GLU B 24  ? 0.3571 0.3965 0.2313 0.0100  -0.0197 -0.0965 24  GLU B N   
4259 C CA  . GLU B 24  ? 0.3138 0.3614 0.1890 0.0140  -0.0135 -0.0854 24  GLU B CA  
4260 C C   . GLU B 24  ? 0.3073 0.3486 0.1920 0.0116  -0.0137 -0.0701 24  GLU B C   
4261 O O   . GLU B 24  ? 0.3615 0.4051 0.2474 0.0070  -0.0178 -0.0641 24  GLU B O   
4262 C CB  . GLU B 24  ? 0.4238 0.4955 0.2871 0.0150  -0.0114 -0.0825 24  GLU B CB  
4263 C CG  . GLU B 24  ? 0.4796 0.5605 0.3324 0.0179  -0.0103 -0.0983 24  GLU B CG  
4264 C CD  . GLU B 24  ? 0.6529 0.7591 0.4916 0.0171  -0.0099 -0.0961 24  GLU B CD  
4265 O OE1 . GLU B 24  ? 0.7035 0.8185 0.5408 0.0135  -0.0126 -0.0834 24  GLU B OE1 
4266 O OE2 . GLU B 24  ? 0.7555 0.8733 0.5846 0.0204  -0.0069 -0.1072 24  GLU B OE2 
4267 N N   . TYR B 25  ? 0.3105 0.3451 0.2023 0.0150  -0.0092 -0.0645 25  TYR B N   
4268 C CA  . TYR B 25  ? 0.2618 0.2934 0.1617 0.0135  -0.0082 -0.0503 25  TYR B CA  
4269 C C   . TYR B 25  ? 0.3709 0.4207 0.2662 0.0137  -0.0058 -0.0399 25  TYR B C   
4270 O O   . TYR B 25  ? 0.3187 0.3785 0.2108 0.0172  -0.0009 -0.0389 25  TYR B O   
4271 C CB  . TYR B 25  ? 0.2696 0.2896 0.1779 0.0169  -0.0046 -0.0486 25  TYR B CB  
4272 C CG  . TYR B 25  ? 0.3243 0.3247 0.2392 0.0155  -0.0079 -0.0533 25  TYR B CG  
4273 C CD1 . TYR B 25  ? 0.3402 0.3318 0.2534 0.0168  -0.0098 -0.0661 25  TYR B CD1 
4274 C CD2 . TYR B 25  ? 0.3131 0.3038 0.2359 0.0126  -0.0089 -0.0449 25  TYR B CD2 
4275 C CE1 . TYR B 25  ? 0.3807 0.3536 0.3003 0.0151  -0.0129 -0.0690 25  TYR B CE1 
4276 C CE2 . TYR B 25  ? 0.3595 0.3335 0.2876 0.0108  -0.0117 -0.0479 25  TYR B CE2 
4277 C CZ  . TYR B 25  ? 0.3957 0.3604 0.3223 0.0119  -0.0138 -0.0592 25  TYR B CZ  
4278 O OH  . TYR B 25  ? 0.3699 0.3170 0.3021 0.0097  -0.0168 -0.0610 25  TYR B OH  
4279 N N   . LEU B 26  ? 0.3118 0.3665 0.2076 0.0100  -0.0092 -0.0319 26  LEU B N   
4280 C CA  . LEU B 26  ? 0.3480 0.4201 0.2387 0.0099  -0.0083 -0.0219 26  LEU B CA  
4281 C C   . LEU B 26  ? 0.3074 0.3790 0.2062 0.0108  -0.0045 -0.0083 26  LEU B C   
4282 O O   . LEU B 26  ? 0.3397 0.4247 0.2353 0.0112  -0.0028 0.0011  26  LEU B O   
4283 C CB  . LEU B 26  ? 0.3598 0.4389 0.2481 0.0062  -0.0144 -0.0194 26  LEU B CB  
4284 C CG  . LEU B 26  ? 0.3882 0.4711 0.2678 0.0042  -0.0191 -0.0325 26  LEU B CG  
4285 C CD1 . LEU B 26  ? 0.3585 0.4522 0.2363 0.0005  -0.0253 -0.0279 26  LEU B CD1 
4286 C CD2 . LEU B 26  ? 0.3416 0.4362 0.2090 0.0071  -0.0162 -0.0413 26  LEU B CD2 
4287 N N   . LEU B 27  ? 0.2478 0.3044 0.1570 0.0109  -0.0035 -0.0068 27  LEU B N   
4288 C CA  . LEU B 27  ? 0.3006 0.3552 0.2180 0.0118  0.0004  0.0033  27  LEU B CA  
4289 C C   . LEU B 27  ? 0.2729 0.3157 0.1958 0.0139  0.0031  -0.0021 27  LEU B C   
4290 O O   . LEU B 27  ? 0.2744 0.3063 0.1978 0.0138  0.0008  -0.0108 27  LEU B O   
4291 C CB  . LEU B 27  ? 0.2409 0.2903 0.1671 0.0094  -0.0020 0.0122  27  LEU B CB  
4292 C CG  . LEU B 27  ? 0.2752 0.3368 0.1987 0.0082  -0.0048 0.0204  27  LEU B CG  
4293 C CD1 . LEU B 27  ? 0.2825 0.3373 0.2157 0.0064  -0.0078 0.0255  27  LEU B CD1 
4294 C CD2 . LEU B 27  ? 0.2947 0.3671 0.2171 0.0095  -0.0011 0.0308  27  LEU B CD2 
4295 N N   . PRO B 28  ? 0.2512 0.2960 0.1788 0.0156  0.0077  0.0033  28  PRO B N   
4296 C CA  . PRO B 28  ? 0.2097 0.2459 0.1425 0.0181  0.0100  -0.0018 28  PRO B CA  
4297 C C   . PRO B 28  ? 0.2327 0.2563 0.1755 0.0167  0.0092  0.0023  28  PRO B C   
4298 O O   . PRO B 28  ? 0.2654 0.2838 0.2134 0.0186  0.0110  0.0006  28  PRO B O   
4299 C CB  . PRO B 28  ? 0.2606 0.3095 0.1931 0.0202  0.0155  0.0016  28  PRO B CB  
4300 C CG  . PRO B 28  ? 0.2801 0.3366 0.2138 0.0174  0.0159  0.0141  28  PRO B CG  
4301 C CD  . PRO B 28  ? 0.2534 0.3101 0.1817 0.0153  0.0109  0.0142  28  PRO B CD  
4302 N N   . TRP B 29  ? 0.3002 0.3197 0.2460 0.0136  0.0064  0.0073  29  TRP B N   
4303 C CA  . TRP B 29  ? 0.2578 0.2680 0.2128 0.0122  0.0064  0.0117  29  TRP B CA  
4304 C C   . TRP B 29  ? 0.2624 0.2604 0.2196 0.0128  0.0052  0.0054  29  TRP B C   
4305 O O   . TRP B 29  ? 0.2448 0.2377 0.2083 0.0129  0.0064  0.0076  29  TRP B O   
4306 C CB  . TRP B 29  ? 0.2663 0.2755 0.2243 0.0094  0.0038  0.0169  29  TRP B CB  
4307 C CG  . TRP B 29  ? 0.2560 0.2760 0.2139 0.0093  0.0046  0.0254  29  TRP B CG  
4308 C CD1 . TRP B 29  ? 0.2434 0.2703 0.1977 0.0083  0.0017  0.0278  29  TRP B CD1 
4309 C CD2 . TRP B 29  ? 0.2725 0.2976 0.2349 0.0098  0.0081  0.0333  29  TRP B CD2 
4310 N NE1 . TRP B 29  ? 0.2499 0.2855 0.2057 0.0087  0.0030  0.0374  29  TRP B NE1 
4311 C CE2 . TRP B 29  ? 0.2922 0.3263 0.2532 0.0093  0.0071  0.0411  29  TRP B CE2 
4312 C CE3 . TRP B 29  ? 0.3035 0.3265 0.2717 0.0103  0.0116  0.0349  29  TRP B CE3 
4313 C CZ2 . TRP B 29  ? 0.2756 0.3153 0.2408 0.0091  0.0097  0.0511  29  TRP B CZ2 
4314 C CZ3 . TRP B 29  ? 0.3289 0.3582 0.3017 0.0097  0.0144  0.0439  29  TRP B CZ3 
4315 C CH2 . TRP B 29  ? 0.3637 0.4006 0.3350 0.0090  0.0135  0.0523  29  TRP B CH2 
4316 N N   . THR B 30  ? 0.2520 0.2448 0.2042 0.0128  0.0025  -0.0022 30  THR B N   
4317 C CA  . THR B 30  ? 0.2315 0.2121 0.1862 0.0134  0.0012  -0.0068 30  THR B CA  
4318 C C   . THR B 30  ? 0.2420 0.2233 0.1988 0.0177  0.0039  -0.0090 30  THR B C   
4319 O O   . THR B 30  ? 0.2620 0.2364 0.2239 0.0184  0.0037  -0.0079 30  THR B O   
4320 C CB  . THR B 30  ? 0.2875 0.2612 0.2377 0.0123  -0.0023 -0.0143 30  THR B CB  
4321 O OG1 . THR B 30  ? 0.2572 0.2309 0.2072 0.0079  -0.0050 -0.0118 30  THR B OG1 
4322 C CG2 . THR B 30  ? 0.2717 0.2316 0.2249 0.0131  -0.0039 -0.0176 30  THR B CG2 
4323 N N   . PHE B 31  ? 0.2426 0.2337 0.1955 0.0208  0.0063  -0.0122 31  PHE B N   
4324 C CA  . PHE B 31  ? 0.2445 0.2392 0.2007 0.0251  0.0094  -0.0144 31  PHE B CA  
4325 C C   . PHE B 31  ? 0.2443 0.2426 0.2080 0.0242  0.0118  -0.0065 31  PHE B C   
4326 O O   . PHE B 31  ? 0.2073 0.2017 0.1769 0.0261  0.0119  -0.0069 31  PHE B O   
4327 C CB  . PHE B 31  ? 0.2314 0.2391 0.1818 0.0281  0.0125  -0.0187 31  PHE B CB  
4328 C CG  . PHE B 31  ? 0.2549 0.2699 0.2097 0.0326  0.0165  -0.0206 31  PHE B CG  
4329 C CD1 . PHE B 31  ? 0.2520 0.2613 0.2088 0.0375  0.0159  -0.0292 31  PHE B CD1 
4330 C CD2 . PHE B 31  ? 0.2130 0.2407 0.1711 0.0320  0.0208  -0.0135 31  PHE B CD2 
4331 C CE1 . PHE B 31  ? 0.2909 0.3084 0.2531 0.0423  0.0196  -0.0312 31  PHE B CE1 
4332 C CE2 . PHE B 31  ? 0.2579 0.2939 0.2213 0.0357  0.0246  -0.0152 31  PHE B CE2 
4333 C CZ  . PHE B 31  ? 0.2483 0.2800 0.2138 0.0412  0.0241  -0.0243 31  PHE B CZ  
4334 N N   . PHE B 32  ? 0.2162 0.2218 0.1802 0.0213  0.0133  0.0008  32  PHE B N   
4335 C CA  . PHE B 32  ? 0.2056 0.2149 0.1774 0.0201  0.0158  0.0077  32  PHE B CA  
4336 C C   . PHE B 32  ? 0.2486 0.2470 0.2264 0.0182  0.0135  0.0093  32  PHE B C   
4337 O O   . PHE B 32  ? 0.2088 0.2073 0.1933 0.0187  0.0145  0.0103  32  PHE B O   
4338 C CB  . PHE B 32  ? 0.1711 0.1892 0.1423 0.0175  0.0177  0.0156  32  PHE B CB  
4339 C CG  . PHE B 32  ? 0.3114 0.3438 0.2787 0.0192  0.0215  0.0163  32  PHE B CG  
4340 C CD1 . PHE B 32  ? 0.2379 0.2766 0.2097 0.0213  0.0251  0.0151  32  PHE B CD1 
4341 C CD2 . PHE B 32  ? 0.3115 0.3522 0.2702 0.0188  0.0215  0.0175  32  PHE B CD2 
4342 C CE1 . PHE B 32  ? 0.3286 0.3825 0.2969 0.0228  0.0294  0.0155  32  PHE B CE1 
4343 C CE2 . PHE B 32  ? 0.3502 0.4058 0.3041 0.0202  0.0254  0.0180  32  PHE B CE2 
4344 C CZ  . PHE B 32  ? 0.2689 0.3313 0.2276 0.0221  0.0298  0.0169  32  PHE B CZ  
4345 N N   . HIS B 33  ? 0.2055 0.1959 0.1812 0.0159  0.0104  0.0091  33  HIS B N   
4346 C CA  . HIS B 33  ? 0.2039 0.1856 0.1842 0.0140  0.0087  0.0101  33  HIS B CA  
4347 C C   . HIS B 33  ? 0.2176 0.1919 0.1975 0.0161  0.0067  0.0053  33  HIS B C   
4348 O O   . HIS B 33  ? 0.2043 0.1744 0.1882 0.0153  0.0057  0.0065  33  HIS B O   
4349 C CB  . HIS B 33  ? 0.2242 0.2016 0.2031 0.0108  0.0066  0.0117  33  HIS B CB  
4350 C CG  . HIS B 33  ? 0.2203 0.2030 0.2031 0.0091  0.0080  0.0178  33  HIS B CG  
4351 N ND1 . HIS B 33  ? 0.2306 0.2133 0.2210 0.0080  0.0096  0.0214  33  HIS B ND1 
4352 C CD2 . HIS B 33  ? 0.1684 0.1563 0.1492 0.0083  0.0077  0.0208  33  HIS B CD2 
4353 C CE1 . HIS B 33  ? 0.2250 0.2113 0.2185 0.0069  0.0103  0.0267  33  HIS B CE1 
4354 N NE2 . HIS B 33  ? 0.2007 0.1906 0.1883 0.0073  0.0091  0.0270  33  HIS B NE2 
4355 N N   . ALA B 34  ? 0.2340 0.2067 0.2094 0.0189  0.0058  -0.0001 34  ALA B N   
4356 C CA  . ALA B 34  ? 0.2299 0.1951 0.2064 0.0218  0.0038  -0.0040 34  ALA B CA  
4357 C C   . ALA B 34  ? 0.2573 0.2287 0.2399 0.0251  0.0057  -0.0034 34  ALA B C   
4358 O O   . ALA B 34  ? 0.2425 0.2093 0.2289 0.0257  0.0038  -0.0024 34  ALA B O   
4359 C CB  . ALA B 34  ? 0.2287 0.1899 0.2003 0.0245  0.0025  -0.0108 34  ALA B CB  
4360 N N   . VAL B 35  ? 0.2163 0.1993 0.2001 0.0269  0.0094  -0.0035 35  VAL B N   
4361 C CA  . VAL B 35  ? 0.1936 0.1841 0.1845 0.0298  0.0113  -0.0031 35  VAL B CA  
4362 C C   . VAL B 35  ? 0.2346 0.2274 0.2319 0.0260  0.0117  0.0028  35  VAL B C   
4363 O O   . VAL B 35  ? 0.2166 0.2125 0.2205 0.0273  0.0114  0.0030  35  VAL B O   
4364 C CB  . VAL B 35  ? 0.2270 0.2310 0.2178 0.0326  0.0158  -0.0050 35  VAL B CB  
4365 C CG1 . VAL B 35  ? 0.3179 0.3196 0.3021 0.0365  0.0153  -0.0127 35  VAL B CG1 
4366 C CG2 . VAL B 35  ? 0.2202 0.2329 0.2094 0.0285  0.0189  0.0010  35  VAL B CG2 
4367 N N   . LYS B 36  ? 0.2121 0.2034 0.2082 0.0214  0.0120  0.0070  36  LYS B N   
4368 C CA  . LYS B 36  ? 0.1738 0.1668 0.1765 0.0179  0.0126  0.0115  36  LYS B CA  
4369 C C   . LYS B 36  ? 0.2160 0.1998 0.2188 0.0156  0.0092  0.0113  36  LYS B C   
4370 O O   . LYS B 36  ? 0.2489 0.2338 0.2574 0.0145  0.0085  0.0119  36  LYS B O   
4371 C CB  . LYS B 36  ? 0.2067 0.2039 0.2099 0.0147  0.0151  0.0165  36  LYS B CB  
4372 C CG  . LYS B 36  ? 0.2317 0.2303 0.2437 0.0112  0.0161  0.0207  36  LYS B CG  
4373 C CD  . LYS B 36  ? 0.1998 0.2020 0.2140 0.0085  0.0185  0.0269  36  LYS B CD  
4374 C CE  . LYS B 36  ? 0.2570 0.2521 0.2686 0.0070  0.0167  0.0283  36  LYS B CE  
4375 N NZ  . LYS B 36  ? 0.2100 0.1973 0.2260 0.0049  0.0148  0.0266  36  LYS B NZ  
4376 N N   . ASP B 37  ? 0.2328 0.2086 0.2295 0.0147  0.0072  0.0102  37  ASP B N   
4377 C CA  . ASP B 37  ? 0.1630 0.1319 0.1591 0.0118  0.0049  0.0107  37  ASP B CA  
4378 C C   . ASP B 37  ? 0.2120 0.1725 0.2029 0.0126  0.0016  0.0086  37  ASP B C   
4379 O O   . ASP B 37  ? 0.2343 0.1916 0.2254 0.0113  -0.0004 0.0091  37  ASP B O   
4380 C CB  . ASP B 37  ? 0.2213 0.1895 0.2168 0.0087  0.0059  0.0129  37  ASP B CB  
4381 C CG  . ASP B 37  ? 0.2761 0.2510 0.2768 0.0080  0.0088  0.0163  37  ASP B CG  
4382 O OD1 . ASP B 37  ? 0.2210 0.1985 0.2285 0.0069  0.0097  0.0173  37  ASP B OD1 
4383 O OD2 . ASP B 37  ? 0.2156 0.1937 0.2139 0.0083  0.0099  0.0182  37  ASP B OD2 
4384 N N   . TYR B 38  ? 0.2183 0.1750 0.2044 0.0142  0.0008  0.0063  38  TYR B N   
4385 C CA  . TYR B 38  ? 0.1721 0.1191 0.1540 0.0133  -0.0024 0.0054  38  TYR B CA  
4386 C C   . TYR B 38  ? 0.1860 0.1290 0.1692 0.0163  -0.0049 0.0052  38  TYR B C   
4387 O O   . TYR B 38  ? 0.2308 0.1669 0.2117 0.0145  -0.0077 0.0070  38  TYR B O   
4388 C CB  . TYR B 38  ? 0.1682 0.1111 0.1456 0.0137  -0.0031 0.0024  38  TYR B CB  
4389 C CG  . TYR B 38  ? 0.2320 0.1787 0.2077 0.0104  -0.0017 0.0034  38  TYR B CG  
4390 C CD1 . TYR B 38  ? 0.2062 0.1546 0.1839 0.0069  -0.0010 0.0068  38  TYR B CD1 
4391 C CD2 . TYR B 38  ? 0.1941 0.1439 0.1666 0.0113  -0.0013 0.0007  38  TYR B CD2 
4392 C CE1 . TYR B 38  ? 0.2423 0.1948 0.2200 0.0047  -0.0001 0.0081  38  TYR B CE1 
4393 C CE2 . TYR B 38  ? 0.2156 0.1702 0.1870 0.0087  -0.0007 0.0024  38  TYR B CE2 
4394 C CZ  . TYR B 38  ? 0.2459 0.2015 0.2205 0.0056  -0.0002 0.0064  38  TYR B CZ  
4395 O OH  . TYR B 38  ? 0.2350 0.1958 0.2099 0.0038  0.0000  0.0084  38  TYR B OH  
4396 N N   . TYR B 39  ? 0.1985 0.1466 0.1858 0.0208  -0.0043 0.0035  39  TYR B N   
4397 C CA  . TYR B 39  ? 0.1970 0.1430 0.1871 0.0241  -0.0071 0.0039  39  TYR B CA  
4398 C C   . TYR B 39  ? 0.2460 0.1983 0.2398 0.0221  -0.0075 0.0068  39  TYR B C   
4399 O O   . TYR B 39  ? 0.2229 0.1720 0.2160 0.0217  -0.0108 0.0090  39  TYR B O   
4400 C CB  . TYR B 39  ? 0.2195 0.1696 0.2138 0.0304  -0.0063 0.0003  39  TYR B CB  
4401 C CG  . TYR B 39  ? 0.2560 0.2066 0.2556 0.0346  -0.0094 0.0011  39  TYR B CG  
4402 C CD1 . TYR B 39  ? 0.2758 0.2157 0.2744 0.0378  -0.0134 0.0010  39  TYR B CD1 
4403 C CD2 . TYR B 39  ? 0.2193 0.1810 0.2254 0.0352  -0.0088 0.0025  39  TYR B CD2 
4404 C CE1 . TYR B 39  ? 0.2728 0.2133 0.2767 0.0423  -0.0169 0.0027  39  TYR B CE1 
4405 C CE2 . TYR B 39  ? 0.1947 0.1582 0.2061 0.0392  -0.0123 0.0035  39  TYR B CE2 
4406 C CZ  . TYR B 39  ? 0.2374 0.1905 0.2475 0.0430  -0.0164 0.0039  39  TYR B CZ  
4407 O OH  . TYR B 39  ? 0.2903 0.2452 0.3059 0.0476  -0.0205 0.0058  39  TYR B OH  
4408 N N   . ASP B 40  ? 0.2067 0.1679 0.2046 0.0204  -0.0042 0.0069  40  ASP B N   
4409 C CA  . ASP B 40  ? 0.2121 0.1800 0.2153 0.0188  -0.0046 0.0082  40  ASP B CA  
4410 C C   . ASP B 40  ? 0.2526 0.2173 0.2527 0.0139  -0.0059 0.0096  40  ASP B C   
4411 O O   . ASP B 40  ? 0.2116 0.1796 0.2136 0.0128  -0.0080 0.0100  40  ASP B O   
4412 C CB  . ASP B 40  ? 0.2179 0.1953 0.2275 0.0181  -0.0007 0.0082  40  ASP B CB  
4413 C CG  . ASP B 40  ? 0.2656 0.2510 0.2809 0.0227  0.0002  0.0068  40  ASP B CG  
4414 O OD1 . ASP B 40  ? 0.2409 0.2303 0.2611 0.0244  -0.0023 0.0067  40  ASP B OD1 
4415 O OD2 . ASP B 40  ? 0.2556 0.2441 0.2702 0.0250  0.0032  0.0056  40  ASP B OD2 
4416 N N   . MET B 41  ? 0.1902 0.1499 0.1856 0.0110  -0.0046 0.0100  41  MET B N   
4417 C CA  . MET B 41  ? 0.1925 0.1511 0.1857 0.0067  -0.0050 0.0105  41  MET B CA  
4418 C C   . MET B 41  ? 0.1824 0.1372 0.1704 0.0064  -0.0088 0.0120  41  MET B C   
4419 O O   . MET B 41  ? 0.1912 0.1500 0.1794 0.0045  -0.0101 0.0118  41  MET B O   
4420 C CB  . MET B 41  ? 0.1825 0.1384 0.1734 0.0041  -0.0027 0.0106  41  MET B CB  
4421 C CG  . MET B 41  ? 0.1807 0.1413 0.1775 0.0034  0.0006  0.0105  41  MET B CG  
4422 S SD  . MET B 41  ? 0.2074 0.1720 0.2104 0.0003  0.0015  0.0090  41  MET B SD  
4423 C CE  . MET B 41  ? 0.1796 0.1409 0.1781 -0.0027 0.0018  0.0081  41  MET B CE  
4424 N N   . PRO B 42  ? 0.2612 0.2085 0.2447 0.0080  -0.0108 0.0135  42  PRO B N   
4425 C CA  . PRO B 42  ? 0.2409 0.1848 0.2204 0.0080  -0.0148 0.0166  42  PRO B CA  
4426 C C   . PRO B 42  ? 0.2400 0.1886 0.2237 0.0120  -0.0178 0.0171  42  PRO B C   
4427 O O   . PRO B 42  ? 0.2440 0.1939 0.2249 0.0112  -0.0212 0.0198  42  PRO B O   
4428 C CB  . PRO B 42  ? 0.2626 0.1959 0.2384 0.0089  -0.0162 0.0181  42  PRO B CB  
4429 C CG  . PRO B 42  ? 0.2221 0.1553 0.2010 0.0114  -0.0136 0.0144  42  PRO B CG  
4430 C CD  . PRO B 42  ? 0.1955 0.1367 0.1770 0.0089  -0.0099 0.0128  42  PRO B CD  
4431 N N   . ALA B 43  ? 0.2177 0.1703 0.2080 0.0161  -0.0166 0.0147  43  ALA B N   
4432 C CA  . ALA B 43  ? 0.1766 0.1354 0.1726 0.0201  -0.0195 0.0150  43  ALA B CA  
4433 C C   . ALA B 43  ? 0.2128 0.1813 0.2113 0.0171  -0.0204 0.0147  43  ALA B C   
4434 O O   . ALA B 43  ? 0.1687 0.1429 0.1707 0.0195  -0.0242 0.0157  43  ALA B O   
4435 C CB  . ALA B 43  ? 0.1980 0.1613 0.2012 0.0248  -0.0170 0.0120  43  ALA B CB  
4436 N N   . TYR B 44  ? 0.1941 0.1649 0.1919 0.0121  -0.0175 0.0128  44  TYR B N   
4437 C CA  . TYR B 44  ? 0.1862 0.1648 0.1857 0.0087  -0.0187 0.0112  44  TYR B CA  
4438 C C   . TYR B 44  ? 0.1805 0.1591 0.1729 0.0079  -0.0234 0.0138  44  TYR B C   
4439 O O   . TYR B 44  ? 0.2168 0.2038 0.2109 0.0067  -0.0264 0.0129  44  TYR B O   
4440 C CB  . TYR B 44  ? 0.1644 0.1431 0.1639 0.0038  -0.0149 0.0083  44  TYR B CB  
4441 C CG  . TYR B 44  ? 0.1701 0.1519 0.1783 0.0032  -0.0109 0.0063  44  TYR B CG  
4442 C CD1 . TYR B 44  ? 0.2339 0.2234 0.2503 0.0013  -0.0111 0.0038  44  TYR B CD1 
4443 C CD2 . TYR B 44  ? 0.2234 0.2005 0.2314 0.0039  -0.0073 0.0071  44  TYR B CD2 
4444 C CE1 . TYR B 44  ? 0.2192 0.2109 0.2439 0.0001  -0.0074 0.0032  44  TYR B CE1 
4445 C CE2 . TYR B 44  ? 0.2349 0.2152 0.2503 0.0031  -0.0038 0.0068  44  TYR B CE2 
4446 C CZ  . TYR B 44  ? 0.2357 0.2228 0.2595 0.0011  -0.0037 0.0053  44  TYR B CZ  
4447 O OH  . TYR B 44  ? 0.2097 0.1992 0.2411 -0.0003 -0.0002 0.0062  44  TYR B OH  
4448 N N   . LEU B 45  ? 0.2028 0.1728 0.1873 0.0078  -0.0243 0.0175  45  LEU B N   
4449 C CA  . LEU B 45  ? 0.2170 0.1871 0.1938 0.0065  -0.0285 0.0216  45  LEU B CA  
4450 C C   . LEU B 45  ? 0.2715 0.2446 0.2512 0.0112  -0.0341 0.0250  45  LEU B C   
4451 O O   . LEU B 45  ? 0.2796 0.2564 0.2539 0.0102  -0.0385 0.0287  45  LEU B O   
4452 C CB  . LEU B 45  ? 0.2388 0.1985 0.2078 0.0048  -0.0279 0.0257  45  LEU B CB  
4453 C CG  . LEU B 45  ? 0.2363 0.1950 0.2017 -0.0002 -0.0231 0.0231  45  LEU B CG  
4454 C CD1 . LEU B 45  ? 0.2494 0.1979 0.2104 -0.0013 -0.0223 0.0267  45  LEU B CD1 
4455 C CD2 . LEU B 45  ? 0.2699 0.2367 0.2296 -0.0048 -0.0232 0.0220  45  LEU B CD2 
4456 N N   . LYS B 46  ? 0.2304 0.2035 0.2187 0.0166  -0.0341 0.0239  46  LYS B N   
4457 C CA  . LYS B 46  ? 0.2565 0.2341 0.2498 0.0220  -0.0394 0.0266  46  LYS B CA  
4458 C C   . LYS B 46  ? 0.2486 0.2408 0.2468 0.0205  -0.0416 0.0242  46  LYS B C   
4459 O O   . LYS B 46  ? 0.2549 0.2532 0.2545 0.0233  -0.0474 0.0274  46  LYS B O   
4460 C CB  . LYS B 46  ? 0.2694 0.2441 0.2713 0.0285  -0.0379 0.0250  46  LYS B CB  
4461 C CG  . LYS B 46  ? 0.2917 0.2519 0.2894 0.0299  -0.0361 0.0260  46  LYS B CG  
4462 C CD  . LYS B 46  ? 0.5599 0.5106 0.5522 0.0314  -0.0414 0.0327  46  LYS B CD  
4463 C CE  . LYS B 46  ? 0.6822 0.6182 0.6684 0.0293  -0.0396 0.0339  46  LYS B CE  
4464 N NZ  . LYS B 46  ? 0.7528 0.6768 0.7424 0.0354  -0.0426 0.0359  46  LYS B NZ  
4465 N N   . ASP B 47  ? 0.2792 0.2771 0.2805 0.0160  -0.0375 0.0187  47  ASP B N   
4466 C CA  . ASP B 47  ? 0.2306 0.2418 0.2383 0.0138  -0.0394 0.0152  47  ASP B CA  
4467 C C   . ASP B 47  ? 0.2508 0.2659 0.2515 0.0074  -0.0400 0.0124  47  ASP B C   
4468 O O   . ASP B 47  ? 0.2697 0.2961 0.2740 0.0053  -0.0433 0.0095  47  ASP B O   
4469 C CB  . ASP B 47  ? 0.2320 0.2476 0.2509 0.0134  -0.0347 0.0107  47  ASP B CB  
4470 C CG  . ASP B 47  ? 0.3706 0.3861 0.3970 0.0200  -0.0337 0.0121  47  ASP B CG  
4471 O OD1 . ASP B 47  ? 0.3214 0.3394 0.3498 0.0252  -0.0384 0.0151  47  ASP B OD1 
4472 O OD2 . ASP B 47  ? 0.3546 0.3682 0.3850 0.0201  -0.0283 0.0103  47  ASP B OD2 
4473 N N   . PHE B 48  ? 0.2359 0.2432 0.2275 0.0041  -0.0370 0.0125  48  PHE B N   
4474 C CA  . PHE B 48  ? 0.2509 0.2622 0.2364 -0.0018 -0.0362 0.0083  48  PHE B CA  
4475 C C   . PHE B 48  ? 0.2107 0.2186 0.1829 -0.0032 -0.0378 0.0130  48  PHE B C   
4476 O O   . PHE B 48  ? 0.2695 0.2672 0.2376 -0.0020 -0.0358 0.0173  48  PHE B O   
4477 C CB  . PHE B 48  ? 0.1778 0.1849 0.1674 -0.0047 -0.0298 0.0030  48  PHE B CB  
4478 C CG  . PHE B 48  ? 0.2326 0.2440 0.2352 -0.0046 -0.0283 -0.0008 48  PHE B CG  
4479 C CD1 . PHE B 48  ? 0.2179 0.2392 0.2260 -0.0078 -0.0305 -0.0060 48  PHE B CD1 
4480 C CD2 . PHE B 48  ? 0.1923 0.1991 0.2015 -0.0017 -0.0249 0.0009  48  PHE B CD2 
4481 C CE1 . PHE B 48  ? 0.2506 0.2762 0.2717 -0.0086 -0.0291 -0.0087 48  PHE B CE1 
4482 C CE2 . PHE B 48  ? 0.2067 0.2186 0.2276 -0.0022 -0.0231 -0.0014 48  PHE B CE2 
4483 C CZ  . PHE B 48  ? 0.2766 0.2976 0.3040 -0.0058 -0.0252 -0.0059 48  PHE B CZ  
4484 N N   . GLU B 49  ? 0.2058 0.2228 0.1710 -0.0062 -0.0413 0.0121  49  GLU B N   
4485 C CA  . GLU B 49  ? 0.2228 0.2394 0.1747 -0.0078 -0.0435 0.0181  49  GLU B CA  
4486 C C   . GLU B 49  ? 0.2742 0.2899 0.2189 -0.0129 -0.0381 0.0140  49  GLU B C   
4487 O O   . GLU B 49  ? 0.2903 0.3151 0.2272 -0.0169 -0.0386 0.0107  49  GLU B O   
4488 C CB  . GLU B 49  ? 0.2985 0.3276 0.2458 -0.0082 -0.0505 0.0199  49  GLU B CB  
4489 C CG  . GLU B 49  ? 0.4957 0.5237 0.4308 -0.0081 -0.0544 0.0299  49  GLU B CG  
4490 C CD  . GLU B 49  ? 0.6690 0.6884 0.6085 -0.0018 -0.0583 0.0391  49  GLU B CD  
4491 O OE1 . GLU B 49  ? 0.5974 0.6169 0.5489 0.0029  -0.0596 0.0372  49  GLU B OE1 
4492 O OE2 . GLU B 49  ? 0.7783 0.7909 0.7096 -0.0017 -0.0599 0.0482  49  GLU B OE2 
4493 N N   . ILE B 50  ? 0.2293 0.2348 0.1770 -0.0125 -0.0329 0.0140  50  ILE B N   
4494 C CA  . ILE B 50  ? 0.2689 0.2727 0.2122 -0.0163 -0.0273 0.0107  50  ILE B CA  
4495 C C   . ILE B 50  ? 0.2946 0.2876 0.2349 -0.0156 -0.0256 0.0178  50  ILE B C   
4496 O O   . ILE B 50  ? 0.2764 0.2624 0.2187 -0.0120 -0.0285 0.0237  50  ILE B O   
4497 C CB  . ILE B 50  ? 0.2447 0.2479 0.1980 -0.0169 -0.0226 0.0020  50  ILE B CB  
4498 C CG1 . ILE B 50  ? 0.2270 0.2222 0.1902 -0.0130 -0.0217 0.0039  50  ILE B CG1 
4499 C CG2 . ILE B 50  ? 0.2700 0.2830 0.2271 -0.0186 -0.0244 -0.0057 50  ILE B CG2 
4500 C CD1 . ILE B 50  ? 0.2277 0.2199 0.1994 -0.0135 -0.0167 -0.0014 50  ILE B CD1 
4501 N N   . LYS B 51  ? 0.2462 0.2382 0.1825 -0.0190 -0.0209 0.0165  51  LYS B N   
4502 C CA  . LYS B 51  ? 0.2302 0.2126 0.1655 -0.0193 -0.0188 0.0217  51  LYS B CA  
4503 C C   . LYS B 51  ? 0.2248 0.2030 0.1687 -0.0184 -0.0141 0.0164  51  LYS B C   
4504 O O   . LYS B 51  ? 0.2162 0.1998 0.1634 -0.0198 -0.0108 0.0094  51  LYS B O   
4505 C CB  . LYS B 51  ? 0.2062 0.1919 0.1314 -0.0242 -0.0168 0.0252  51  LYS B CB  
4506 C CG  . LYS B 51  ? 0.2798 0.2721 0.1943 -0.0261 -0.0210 0.0311  51  LYS B CG  
4507 C CD  . LYS B 51  ? 0.2815 0.2652 0.1956 -0.0231 -0.0266 0.0407  51  LYS B CD  
4508 C CE  . LYS B 51  ? 0.4235 0.4128 0.3257 -0.0258 -0.0304 0.0491  51  LYS B CE  
4509 N NZ  . LYS B 51  ? 0.6130 0.5985 0.5167 -0.0212 -0.0375 0.0558  51  LYS B NZ  
4510 N N   . LEU B 52  ? 0.2166 0.1854 0.1644 -0.0161 -0.0140 0.0196  52  LEU B N   
4511 C CA  . LEU B 52  ? 0.2172 0.1826 0.1717 -0.0155 -0.0100 0.0160  52  LEU B CA  
4512 C C   . LEU B 52  ? 0.2181 0.1754 0.1704 -0.0163 -0.0096 0.0207  52  LEU B C   
4513 O O   . LEU B 52  ? 0.2325 0.1830 0.1826 -0.0148 -0.0130 0.0256  52  LEU B O   
4514 C CB  . LEU B 52  ? 0.1896 0.1532 0.1528 -0.0113 -0.0103 0.0134  52  LEU B CB  
4515 C CG  . LEU B 52  ? 0.1715 0.1425 0.1396 -0.0110 -0.0106 0.0085  52  LEU B CG  
4516 C CD1 . LEU B 52  ? 0.1942 0.1640 0.1708 -0.0073 -0.0111 0.0079  52  LEU B CD1 
4517 C CD2 . LEU B 52  ? 0.1841 0.1590 0.1552 -0.0136 -0.0065 0.0027  52  LEU B CD2 
4518 N N   . ASN B 53  ? 0.2053 0.1631 0.1592 -0.0186 -0.0058 0.0188  53  ASN B N   
4519 C CA  . ASN B 53  ? 0.1896 0.1411 0.1424 -0.0203 -0.0055 0.0223  53  ASN B CA  
4520 C C   . ASN B 53  ? 0.2026 0.1504 0.1621 -0.0179 -0.0042 0.0197  53  ASN B C   
4521 O O   . ASN B 53  ? 0.2272 0.1787 0.1923 -0.0158 -0.0024 0.0156  53  ASN B O   
4522 C CB  . ASN B 53  ? 0.1907 0.1478 0.1402 -0.0255 -0.0023 0.0229  53  ASN B CB  
4523 C CG  . ASN B 53  ? 0.2306 0.1938 0.1720 -0.0283 -0.0030 0.0253  53  ASN B CG  
4524 O OD1 . ASN B 53  ? 0.2518 0.2110 0.1873 -0.0297 -0.0061 0.0319  53  ASN B OD1 
4525 N ND2 . ASN B 53  ? 0.2324 0.2056 0.1737 -0.0290 -0.0003 0.0197  53  ASN B ND2 
4526 N N   . PHE B 54  ? 0.1925 0.1330 0.1513 -0.0185 -0.0055 0.0223  54  PHE B N   
4527 C CA  . PHE B 54  ? 0.2256 0.1630 0.1890 -0.0162 -0.0050 0.0199  54  PHE B CA  
4528 C C   . PHE B 54  ? 0.1707 0.1052 0.1337 -0.0198 -0.0047 0.0211  54  PHE B C   
4529 O O   . PHE B 54  ? 0.2275 0.1574 0.1866 -0.0233 -0.0062 0.0248  54  PHE B O   
4530 C CB  . PHE B 54  ? 0.2211 0.1521 0.1851 -0.0116 -0.0080 0.0200  54  PHE B CB  
4531 C CG  . PHE B 54  ? 0.1866 0.1219 0.1526 -0.0082 -0.0084 0.0188  54  PHE B CG  
4532 C CD1 . PHE B 54  ? 0.2528 0.1929 0.2243 -0.0057 -0.0063 0.0156  54  PHE B CD1 
4533 C CD2 . PHE B 54  ? 0.2113 0.1470 0.1743 -0.0081 -0.0109 0.0214  54  PHE B CD2 
4534 C CE1 . PHE B 54  ? 0.2538 0.1986 0.2285 -0.0035 -0.0066 0.0144  54  PHE B CE1 
4535 C CE2 . PHE B 54  ? 0.2635 0.2048 0.2292 -0.0055 -0.0115 0.0197  54  PHE B CE2 
4536 C CZ  . PHE B 54  ? 0.2453 0.1910 0.2174 -0.0034 -0.0093 0.0160  54  PHE B CZ  
4537 N N   . ASN B 55  ? 0.2208 0.1582 0.1881 -0.0192 -0.0032 0.0183  55  ASN B N   
4538 C CA  . ASN B 55  ? 0.2063 0.1412 0.1742 -0.0221 -0.0038 0.0184  55  ASN B CA  
4539 C C   . ASN B 55  ? 0.2095 0.1394 0.1781 -0.0185 -0.0058 0.0160  55  ASN B C   
4540 O O   . ASN B 55  ? 0.2126 0.1463 0.1836 -0.0145 -0.0048 0.0140  55  ASN B O   
4541 C CB  . ASN B 55  ? 0.2166 0.1605 0.1890 -0.0240 -0.0010 0.0170  55  ASN B CB  
4542 C CG  . ASN B 55  ? 0.2260 0.1692 0.1994 -0.0279 -0.0021 0.0173  55  ASN B CG  
4543 O OD1 . ASN B 55  ? 0.2245 0.1648 0.1958 -0.0328 -0.0027 0.0199  55  ASN B OD1 
4544 N ND2 . ASN B 55  ? 0.2185 0.1652 0.1956 -0.0262 -0.0024 0.0149  55  ASN B ND2 
4545 N N   . LEU B 56  ? 0.2154 0.1372 0.1822 -0.0202 -0.0084 0.0160  56  LEU B N   
4546 C CA  . LEU B 56  ? 0.2453 0.1633 0.2123 -0.0173 -0.0101 0.0122  56  LEU B CA  
4547 C C   . LEU B 56  ? 0.2580 0.1760 0.2259 -0.0218 -0.0111 0.0107  56  LEU B C   
4548 O O   . LEU B 56  ? 0.2146 0.1266 0.1819 -0.0267 -0.0126 0.0126  56  LEU B O   
4549 C CB  . LEU B 56  ? 0.2650 0.1722 0.2301 -0.0144 -0.0128 0.0118  56  LEU B CB  
4550 C CG  . LEU B 56  ? 0.2988 0.2061 0.2638 -0.0097 -0.0128 0.0132  56  LEU B CG  
4551 C CD1 . LEU B 56  ? 0.2537 0.1495 0.2182 -0.0067 -0.0162 0.0131  56  LEU B CD1 
4552 C CD2 . LEU B 56  ? 0.3188 0.2346 0.2861 -0.0053 -0.0106 0.0105  56  LEU B CD2 
4553 N N   . THR B 57  ? 0.2471 0.1724 0.2166 -0.0207 -0.0106 0.0079  57  THR B N   
4554 C CA  . THR B 57  ? 0.1885 0.1146 0.1591 -0.0249 -0.0124 0.0058  57  THR B CA  
4555 C C   . THR B 57  ? 0.2354 0.1512 0.2034 -0.0245 -0.0157 0.0014  57  THR B C   
4556 O O   . THR B 57  ? 0.2298 0.1423 0.1957 -0.0191 -0.0159 -0.0013 57  THR B O   
4557 C CB  . THR B 57  ? 0.1944 0.1324 0.1674 -0.0239 -0.0117 0.0046  57  THR B CB  
4558 O OG1 . THR B 57  ? 0.2278 0.1672 0.1983 -0.0189 -0.0120 0.0017  57  THR B OG1 
4559 C CG2 . THR B 57  ? 0.2173 0.1636 0.1941 -0.0233 -0.0084 0.0082  57  THR B CG2 
4560 N N   . PRO B 58  ? 0.2397 0.1508 0.2087 -0.0301 -0.0181 0.0002  58  PRO B N   
4561 C CA  . PRO B 58  ? 0.2134 0.1128 0.1809 -0.0298 -0.0215 -0.0050 58  PRO B CA  
4562 C C   . PRO B 58  ? 0.2224 0.1266 0.1875 -0.0256 -0.0222 -0.0120 58  PRO B C   
4563 O O   . PRO B 58  ? 0.2334 0.1294 0.1966 -0.0218 -0.0236 -0.0170 58  PRO B O   
4564 C CB  . PRO B 58  ? 0.2371 0.1324 0.2075 -0.0382 -0.0237 -0.0044 58  PRO B CB  
4565 C CG  . PRO B 58  ? 0.2464 0.1488 0.2190 -0.0422 -0.0208 0.0031  58  PRO B CG  
4566 C CD  . PRO B 58  ? 0.2857 0.2008 0.2581 -0.0372 -0.0178 0.0036  58  PRO B CD  
4567 N N   . VAL B 59  ? 0.2475 0.1653 0.2127 -0.0258 -0.0214 -0.0123 59  VAL B N   
4568 C CA  . VAL B 59  ? 0.3009 0.2253 0.2625 -0.0219 -0.0220 -0.0180 59  VAL B CA  
4569 C C   . VAL B 59  ? 0.2329 0.1586 0.1921 -0.0147 -0.0192 -0.0175 59  VAL B C   
4570 O O   . VAL B 59  ? 0.2216 0.1471 0.1773 -0.0108 -0.0195 -0.0233 59  VAL B O   
4571 C CB  . VAL B 59  ? 0.2019 0.1411 0.1644 -0.0239 -0.0223 -0.0168 59  VAL B CB  
4572 C CG1 . VAL B 59  ? 0.2326 0.1796 0.1989 -0.0229 -0.0191 -0.0094 59  VAL B CG1 
4573 C CG2 . VAL B 59  ? 0.2046 0.1524 0.1619 -0.0201 -0.0230 -0.0215 59  VAL B CG2 
4574 N N   . LEU B 60  ? 0.2384 0.1660 0.1999 -0.0131 -0.0163 -0.0113 60  LEU B N   
4575 C CA  . LEU B 60  ? 0.2240 0.1519 0.1847 -0.0070 -0.0140 -0.0109 60  LEU B CA  
4576 C C   . LEU B 60  ? 0.2524 0.1681 0.2125 -0.0045 -0.0155 -0.0145 60  LEU B C   
4577 O O   . LEU B 60  ? 0.2628 0.1793 0.2214 0.0008  -0.0147 -0.0187 60  LEU B O   
4578 C CB  . LEU B 60  ? 0.2174 0.1487 0.1813 -0.0065 -0.0114 -0.0045 60  LEU B CB  
4579 C CG  . LEU B 60  ? 0.2138 0.1456 0.1782 -0.0011 -0.0093 -0.0039 60  LEU B CG  
4580 C CD1 . LEU B 60  ? 0.2557 0.1964 0.2183 0.0027  -0.0076 -0.0062 60  LEU B CD1 
4581 C CD2 . LEU B 60  ? 0.2186 0.1534 0.1863 -0.0014 -0.0072 0.0013  60  LEU B CD2 
4582 N N   . ILE B 61  ? 0.2289 0.1337 0.1906 -0.0079 -0.0175 -0.0125 61  ILE B N   
4583 C CA  . ILE B 61  ? 0.2456 0.1372 0.2078 -0.0052 -0.0195 -0.0149 61  ILE B CA  
4584 C C   . ILE B 61  ? 0.3331 0.2212 0.2937 -0.0028 -0.0212 -0.0241 61  ILE B C   
4585 O O   . ILE B 61  ? 0.2450 0.1294 0.2061 0.0033  -0.0210 -0.0283 61  ILE B O   
4586 C CB  . ILE B 61  ? 0.2702 0.1506 0.2342 -0.0106 -0.0218 -0.0103 61  ILE B CB  
4587 C CG1 . ILE B 61  ? 0.2713 0.1559 0.2358 -0.0117 -0.0199 -0.0022 61  ILE B CG1 
4588 C CG2 . ILE B 61  ? 0.2874 0.1522 0.2530 -0.0078 -0.0248 -0.0127 61  ILE B CG2 
4589 C CD1 . ILE B 61  ? 0.2750 0.1516 0.2400 -0.0177 -0.0215 0.0037  61  ILE B CD1 
4590 N N   . ASP B 62  ? 0.2630 0.1533 0.2221 -0.0074 -0.0228 -0.0280 62  ASP B N   
4591 C CA  . ASP B 62  ? 0.2699 0.1573 0.2269 -0.0059 -0.0248 -0.0382 62  ASP B CA  
4592 C C   . ASP B 62  ? 0.2523 0.1501 0.2058 0.0011  -0.0220 -0.0426 62  ASP B C   
4593 O O   . ASP B 62  ? 0.2770 0.1704 0.2297 0.0058  -0.0224 -0.0509 62  ASP B O   
4594 C CB  . ASP B 62  ? 0.3142 0.2068 0.2697 -0.0124 -0.0270 -0.0411 62  ASP B CB  
4595 C CG  . ASP B 62  ? 0.4111 0.2915 0.3706 -0.0196 -0.0305 -0.0404 62  ASP B CG  
4596 O OD1 . ASP B 62  ? 0.4343 0.2988 0.3966 -0.0190 -0.0320 -0.0406 62  ASP B OD1 
4597 O OD2 . ASP B 62  ? 0.3504 0.2372 0.3106 -0.0260 -0.0318 -0.0396 62  ASP B OD2 
4598 N N   . GLN B 63  ? 0.2709 0.1829 0.2229 0.0019  -0.0189 -0.0373 63  GLN B N   
4599 C CA  . GLN B 63  ? 0.2277 0.1517 0.1763 0.0074  -0.0159 -0.0401 63  GLN B CA  
4600 C C   . GLN B 63  ? 0.2637 0.1850 0.2153 0.0136  -0.0135 -0.0395 63  GLN B C   
4601 O O   . GLN B 63  ? 0.2957 0.2213 0.2457 0.0190  -0.0118 -0.0458 63  GLN B O   
4602 C CB  . GLN B 63  ? 0.2226 0.1613 0.1699 0.0057  -0.0137 -0.0333 63  GLN B CB  
4603 C CG  . GLN B 63  ? 0.2695 0.2141 0.2141 0.0006  -0.0163 -0.0343 63  GLN B CG  
4604 C CD  . GLN B 63  ? 0.2889 0.2464 0.2342 -0.0005 -0.0146 -0.0263 63  GLN B CD  
4605 O OE1 . GLN B 63  ? 0.3526 0.3215 0.2946 0.0024  -0.0125 -0.0251 63  GLN B OE1 
4606 N NE2 . GLN B 63  ? 0.2462 0.2018 0.1963 -0.0045 -0.0153 -0.0203 63  GLN B NE2 
4607 N N   . ILE B 64  ? 0.2460 0.1619 0.2021 0.0131  -0.0134 -0.0323 64  ILE B N   
4608 C CA  . ILE B 64  ? 0.2537 0.1671 0.2136 0.0189  -0.0122 -0.0317 64  ILE B CA  
4609 C C   . ILE B 64  ? 0.2843 0.1862 0.2457 0.0229  -0.0144 -0.0395 64  ILE B C   
4610 O O   . ILE B 64  ? 0.2849 0.1899 0.2481 0.0295  -0.0127 -0.0440 64  ILE B O   
4611 C CB  . ILE B 64  ? 0.2389 0.1481 0.2025 0.0169  -0.0126 -0.0230 64  ILE B CB  
4612 C CG1 . ILE B 64  ? 0.2307 0.1518 0.1942 0.0142  -0.0099 -0.0168 64  ILE B CG1 
4613 C CG2 . ILE B 64  ? 0.2926 0.1985 0.2606 0.0228  -0.0127 -0.0226 64  ILE B CG2 
4614 C CD1 . ILE B 64  ? 0.2476 0.1659 0.2139 0.0117  -0.0102 -0.0096 64  ILE B CD1 
4615 N N   . GLN B 65  ? 0.2836 0.1717 0.2453 0.0190  -0.0182 -0.0413 65  GLN B N   
4616 C CA  . GLN B 65  ? 0.3084 0.1832 0.2727 0.0228  -0.0208 -0.0491 65  GLN B CA  
4617 C C   . GLN B 65  ? 0.3190 0.2009 0.2801 0.0272  -0.0192 -0.0607 65  GLN B C   
4618 O O   . GLN B 65  ? 0.2948 0.1722 0.2592 0.0341  -0.0190 -0.0676 65  GLN B O   
4619 C CB  . GLN B 65  ? 0.3484 0.2078 0.3137 0.0163  -0.0252 -0.0491 65  GLN B CB  
4620 C CG  . GLN B 65  ? 0.3385 0.1887 0.3071 0.0129  -0.0269 -0.0383 65  GLN B CG  
4621 C CD  . GLN B 65  ? 0.3811 0.2170 0.3512 0.0057  -0.0308 -0.0375 65  GLN B CD  
4622 O OE1 . GLN B 65  ? 0.3562 0.1958 0.3239 -0.0006 -0.0313 -0.0397 65  GLN B OE1 
4623 N NE2 . GLN B 65  ? 0.4139 0.2336 0.3886 0.0065  -0.0338 -0.0339 65  GLN B NE2 
4624 N N   . GLU B 66  ? 0.2795 0.1733 0.2344 0.0235  -0.0181 -0.0630 66  GLU B N   
4625 C CA  . GLU B 66  ? 0.3058 0.2081 0.2559 0.0270  -0.0167 -0.0742 66  GLU B CA  
4626 C C   . GLU B 66  ? 0.2877 0.2039 0.2376 0.0341  -0.0116 -0.0745 66  GLU B C   
4627 O O   . GLU B 66  ? 0.3210 0.2388 0.2710 0.0403  -0.0102 -0.0844 66  GLU B O   
4628 C CB  . GLU B 66  ? 0.3569 0.2698 0.2999 0.0210  -0.0174 -0.0752 66  GLU B CB  
4629 C CG  . GLU B 66  ? 0.4534 0.3759 0.3895 0.0236  -0.0167 -0.0876 66  GLU B CG  
4630 C CD  . GLU B 66  ? 0.5002 0.4290 0.4300 0.0168  -0.0197 -0.0903 66  GLU B CD  
4631 O OE1 . GLU B 66  ? 0.4243 0.3508 0.3562 0.0104  -0.0221 -0.0824 66  GLU B OE1 
4632 O OE2 . GLU B 66  ? 0.5178 0.4554 0.4408 0.0180  -0.0198 -0.1007 66  GLU B OE2 
4633 N N   . TYR B 67  ? 0.2498 0.1767 0.2004 0.0333  -0.0088 -0.0643 67  TYR B N   
4634 C CA  . TYR B 67  ? 0.2549 0.1948 0.2070 0.0391  -0.0040 -0.0634 67  TYR B CA  
4635 C C   . TYR B 67  ? 0.3199 0.2512 0.2800 0.0457  -0.0043 -0.0660 67  TYR B C   
4636 O O   . TYR B 67  ? 0.3419 0.2810 0.3035 0.0523  -0.0012 -0.0724 67  TYR B O   
4637 C CB  . TYR B 67  ? 0.2386 0.1884 0.1918 0.0361  -0.0016 -0.0516 67  TYR B CB  
4638 C CG  . TYR B 67  ? 0.2533 0.2173 0.1997 0.0324  0.0003  -0.0487 67  TYR B CG  
4639 C CD1 . TYR B 67  ? 0.2587 0.2393 0.2016 0.0353  0.0047  -0.0503 67  TYR B CD1 
4640 C CD2 . TYR B 67  ? 0.3306 0.2926 0.2748 0.0260  -0.0024 -0.0439 67  TYR B CD2 
4641 C CE1 . TYR B 67  ? 0.2806 0.2745 0.2172 0.0319  0.0060  -0.0461 67  TYR B CE1 
4642 C CE2 . TYR B 67  ? 0.3406 0.3157 0.2795 0.0232  -0.0013 -0.0405 67  TYR B CE2 
4643 C CZ  . TYR B 67  ? 0.3259 0.3164 0.2608 0.0262  0.0027  -0.0411 67  TYR B CZ  
4644 O OH  . TYR B 67  ? 0.2971 0.3005 0.2268 0.0235  0.0033  -0.0361 67  TYR B OH  
4645 N N   . ALA B 68  ? 0.3167 0.2328 0.2818 0.0442  -0.0080 -0.0609 68  ALA B N   
4646 C CA  . ALA B 68  ? 0.2946 0.2024 0.2679 0.0507  -0.0092 -0.0616 68  ALA B CA  
4647 C C   . ALA B 68  ? 0.3097 0.2091 0.2850 0.0567  -0.0103 -0.0740 68  ALA B C   
4648 O O   . ALA B 68  ? 0.4224 0.3220 0.4046 0.0646  -0.0094 -0.0774 68  ALA B O   
4649 C CB  . ALA B 68  ? 0.3110 0.2044 0.2878 0.0472  -0.0134 -0.0528 68  ALA B CB  
4650 N N   . GLN B 69  ? 0.3752 0.2398 0.3207 0.0266  -0.0510 -0.0335 69  GLN B N   
4651 C CA  . GLN B 69  ? 0.4067 0.2462 0.3377 0.0363  -0.0480 -0.0409 69  GLN B CA  
4652 C C   . GLN B 69  ? 0.4850 0.3377 0.4159 0.0434  -0.0427 -0.0482 69  GLN B C   
4653 O O   . GLN B 69  ? 0.5585 0.3915 0.4771 0.0515  -0.0391 -0.0558 69  GLN B O   
4654 C CB  . GLN B 69  ? 0.4670 0.2756 0.3799 0.0242  -0.0497 -0.0467 69  GLN B CB  
4655 C CG  . GLN B 69  ? 0.6313 0.4201 0.5401 0.0190  -0.0542 -0.0404 69  GLN B CG  
4656 C CD  . GLN B 69  ? 0.8201 0.5866 0.7133 0.0019  -0.0565 -0.0454 69  GLN B CD  
4657 O OE1 . GLN B 69  ? 0.9259 0.6796 0.8054 -0.0026 -0.0540 -0.0548 69  GLN B OE1 
4658 N NE2 . GLN B 69  ? 0.8511 0.6145 0.7459 -0.0088 -0.0612 -0.0393 69  GLN B NE2 
4659 N N   . GLY B 70  ? 0.4223 0.3063 0.3655 0.0402  -0.0419 -0.0463 70  GLY B N   
4660 C CA  . GLY B 70  ? 0.4695 0.3673 0.4118 0.0444  -0.0373 -0.0529 70  GLY B CA  
4661 C C   . GLY B 70  ? 0.4831 0.3705 0.4123 0.0340  -0.0368 -0.0615 70  GLY B C   
4662 O O   . GLY B 70  ? 0.5952 0.4884 0.5198 0.0377  -0.0326 -0.0685 70  GLY B O   
4663 N N   . LYS B 71  ? 0.4537 0.3283 0.3767 0.0203  -0.0408 -0.0612 71  LYS B N   
4664 C CA  . LYS B 71  ? 0.5129 0.3788 0.4225 0.0090  -0.0407 -0.0692 71  LYS B CA  
4665 C C   . LYS B 71  ? 0.5166 0.4098 0.4333 -0.0001 -0.0419 -0.0675 71  LYS B C   
4666 O O   . LYS B 71  ? 0.5297 0.4236 0.4368 -0.0070 -0.0411 -0.0742 71  LYS B O   
4667 C CB  . LYS B 71  ? 0.5212 0.3616 0.4193 -0.0024 -0.0444 -0.0702 71  LYS B CB  
4668 C CG  . LYS B 71  ? 0.6574 0.4653 0.5453 0.0051  -0.0437 -0.0711 71  LYS B CG  
4669 C CD  . LYS B 71  ? 0.7558 0.5443 0.6289 0.0139  -0.0380 -0.0810 71  LYS B CD  
4670 C CE  . LYS B 71  ? 0.8308 0.6008 0.6842 -0.0003 -0.0372 -0.0910 71  LYS B CE  
4671 N NZ  . LYS B 71  ? 0.9217 0.6738 0.7601 0.0075  -0.0306 -0.1018 71  LYS B NZ  
4672 N N   . ALA B 72  ? 0.4367 0.3516 0.3689 -0.0006 -0.0437 -0.0587 72  ALA B N   
4673 C CA  . ALA B 72  ? 0.3803 0.3167 0.3181 -0.0092 -0.0451 -0.0558 72  ALA B CA  
4674 C C   . ALA B 72  ? 0.3442 0.2982 0.2822 -0.0045 -0.0413 -0.0586 72  ALA B C   
4675 O O   . ALA B 72  ? 0.4336 0.3985 0.3787 0.0050  -0.0382 -0.0565 72  ALA B O   
4676 C CB  . ALA B 72  ? 0.3630 0.3131 0.3153 -0.0113 -0.0472 -0.0460 72  ALA B CB  
4677 N N   . LYS B 73  ? 0.3316 0.2898 0.2613 -0.0117 -0.0415 -0.0634 73  LYS B N   
4678 C CA  . LYS B 73  ? 0.3284 0.3050 0.2574 -0.0096 -0.0386 -0.0653 73  LYS B CA  
4679 C C   . LYS B 73  ? 0.3443 0.3423 0.2830 -0.0142 -0.0405 -0.0566 73  LYS B C   
4680 O O   . LYS B 73  ? 0.3889 0.3926 0.3252 -0.0227 -0.0435 -0.0556 73  LYS B O   
4681 C CB  . LYS B 73  ? 0.3951 0.3653 0.3088 -0.0153 -0.0378 -0.0749 73  LYS B CB  
4682 C CG  . LYS B 73  ? 0.5488 0.5298 0.4582 -0.0099 -0.0330 -0.0801 73  LYS B CG  
4683 C CD  . LYS B 73  ? 0.6842 0.6608 0.5777 -0.0177 -0.0322 -0.0897 73  LYS B CD  
4684 C CE  . LYS B 73  ? 0.6821 0.6841 0.5755 -0.0209 -0.0317 -0.0884 73  LYS B CE  
4685 N NZ  . LYS B 73  ? 0.6737 0.6880 0.5724 -0.0109 -0.0270 -0.0879 73  LYS B NZ  
4686 N N   . ASP B 74  ? 0.3279 0.3382 0.2771 -0.0086 -0.0386 -0.0502 74  ASP B N   
4687 C CA  . ASP B 74  ? 0.3488 0.3744 0.3067 -0.0123 -0.0395 -0.0413 74  ASP B CA  
4688 C C   . ASP B 74  ? 0.3599 0.4028 0.3160 -0.0108 -0.0365 -0.0404 74  ASP B C   
4689 O O   . ASP B 74  ? 0.3106 0.3604 0.2686 -0.0047 -0.0327 -0.0410 74  ASP B O   
4690 C CB  . ASP B 74  ? 0.2700 0.2960 0.2388 -0.0094 -0.0389 -0.0348 74  ASP B CB  
4691 C CG  . ASP B 74  ? 0.2928 0.3305 0.2689 -0.0137 -0.0389 -0.0262 74  ASP B CG  
4692 O OD1 . ASP B 74  ? 0.3135 0.3635 0.2878 -0.0143 -0.0371 -0.0239 74  ASP B OD1 
4693 O OD2 . ASP B 74  ? 0.2497 0.2834 0.2327 -0.0164 -0.0402 -0.0215 74  ASP B OD2 
4694 N N   . VAL B 75  ? 0.2895 0.3408 0.2416 -0.0163 -0.0384 -0.0387 75  VAL B N   
4695 C CA  . VAL B 75  ? 0.2710 0.3369 0.2182 -0.0156 -0.0359 -0.0389 75  VAL B CA  
4696 C C   . VAL B 75  ? 0.3619 0.4387 0.3154 -0.0129 -0.0326 -0.0315 75  VAL B C   
4697 O O   . VAL B 75  ? 0.3300 0.4163 0.2806 -0.0100 -0.0289 -0.0334 75  VAL B O   
4698 C CB  . VAL B 75  ? 0.3200 0.3940 0.2612 -0.0218 -0.0391 -0.0374 75  VAL B CB  
4699 C CG1 . VAL B 75  ? 0.4099 0.4742 0.3431 -0.0265 -0.0418 -0.0457 75  VAL B CG1 
4700 C CG2 . VAL B 75  ? 0.3911 0.4697 0.3394 -0.0242 -0.0416 -0.0276 75  VAL B CG2 
4701 N N   . PHE B 76  ? 0.3265 0.4022 0.2876 -0.0148 -0.0335 -0.0237 76  PHE B N   
4702 C CA  . PHE B 76  ? 0.2982 0.3822 0.2634 -0.0142 -0.0299 -0.0170 76  PHE B CA  
4703 C C   . PHE B 76  ? 0.3350 0.4207 0.3042 -0.0097 -0.0265 -0.0198 76  PHE B C   
4704 O O   . PHE B 76  ? 0.2821 0.3795 0.2503 -0.0086 -0.0225 -0.0187 76  PHE B O   
4705 C CB  . PHE B 76  ? 0.3140 0.3937 0.2852 -0.0177 -0.0309 -0.0089 76  PHE B CB  
4706 C CG  . PHE B 76  ? 0.3331 0.4187 0.3053 -0.0191 -0.0267 -0.0019 76  PHE B CG  
4707 C CD1 . PHE B 76  ? 0.3578 0.4481 0.3240 -0.0207 -0.0257 0.0037  76  PHE B CD1 
4708 C CD2 . PHE B 76  ? 0.3522 0.4384 0.3298 -0.0194 -0.0236 -0.0006 76  PHE B CD2 
4709 C CE1 . PHE B 76  ? 0.3902 0.4825 0.3546 -0.0230 -0.0212 0.0101  76  PHE B CE1 
4710 C CE2 . PHE B 76  ? 0.3852 0.4762 0.3617 -0.0227 -0.0192 0.0053  76  PHE B CE2 
4711 C CZ  . PHE B 76  ? 0.3813 0.4737 0.3504 -0.0248 -0.0177 0.0104  76  PHE B CZ  
4712 N N   . LEU B 77  ? 0.2966 0.3720 0.2701 -0.0069 -0.0282 -0.0230 77  LEU B N   
4713 C CA  . LEU B 77  ? 0.2957 0.3743 0.2736 -0.0008 -0.0255 -0.0253 77  LEU B CA  
4714 C C   . LEU B 77  ? 0.3895 0.4756 0.3617 0.0048  -0.0223 -0.0324 77  LEU B C   
4715 O O   . LEU B 77  ? 0.2917 0.3910 0.2669 0.0088  -0.0185 -0.0325 77  LEU B O   
4716 C CB  . LEU B 77  ? 0.2938 0.3573 0.2752 0.0018  -0.0284 -0.0272 77  LEU B CB  
4717 C CG  . LEU B 77  ? 0.3463 0.4139 0.3351 0.0076  -0.0268 -0.0258 77  LEU B CG  
4718 C CD1 . LEU B 77  ? 0.3707 0.4538 0.3659 0.0034  -0.0241 -0.0184 77  LEU B CD1 
4719 C CD2 . LEU B 77  ? 0.3244 0.3752 0.3156 0.0082  -0.0306 -0.0254 77  LEU B CD2 
4720 N N   . GLU B 78  ? 0.3377 0.4173 0.3011 0.0045  -0.0236 -0.0388 78  GLU B N   
4721 C CA  . GLU B 78  ? 0.4347 0.5208 0.3915 0.0092  -0.0200 -0.0467 78  GLU B CA  
4722 C C   . GLU B 78  ? 0.3890 0.4951 0.3445 0.0070  -0.0165 -0.0436 78  GLU B C   
4723 O O   . GLU B 78  ? 0.4298 0.5475 0.3847 0.0121  -0.0122 -0.0480 78  GLU B O   
4724 C CB  . GLU B 78  ? 0.5028 0.5786 0.4489 0.0062  -0.0219 -0.0538 78  GLU B CB  
4725 C CG  . GLU B 78  ? 0.5946 0.6492 0.5378 0.0096  -0.0233 -0.0603 78  GLU B CG  
4726 C CD  . GLU B 78  ? 0.7639 0.8074 0.6953 0.0032  -0.0255 -0.0668 78  GLU B CD  
4727 O OE1 . GLU B 78  ? 0.7797 0.8344 0.7063 -0.0035 -0.0266 -0.0657 78  GLU B OE1 
4728 O OE2 . GLU B 78  ? 0.8540 0.8775 0.7798 0.0046  -0.0260 -0.0728 78  GLU B OE2 
4729 N N   . ALA B 79  ? 0.2964 0.4068 0.2509 -0.0002 -0.0180 -0.0360 79  ALA B N   
4730 C CA  . ALA B 79  ? 0.2974 0.4240 0.2490 -0.0033 -0.0145 -0.0320 79  ALA B CA  
4731 C C   . ALA B 79  ? 0.3343 0.4704 0.2930 -0.0022 -0.0109 -0.0282 79  ALA B C   
4732 O O   . ALA B 79  ? 0.3916 0.5434 0.3478 -0.0027 -0.0067 -0.0288 79  ALA B O   
4733 C CB  . ALA B 79  ? 0.2937 0.4193 0.2413 -0.0101 -0.0169 -0.0239 79  ALA B CB  
4734 N N   . ILE B 80  ? 0.2466 0.3751 0.2137 -0.0017 -0.0125 -0.0246 80  ILE B N   
4735 C CA  . ILE B 80  ? 0.2402 0.3799 0.2141 -0.0013 -0.0092 -0.0217 80  ILE B CA  
4736 C C   . ILE B 80  ? 0.3551 0.5057 0.3318 0.0077  -0.0066 -0.0289 80  ILE B C   
4737 O O   . ILE B 80  ? 0.2846 0.4544 0.2631 0.0079  -0.0023 -0.0287 80  ILE B O   
4738 C CB  . ILE B 80  ? 0.2310 0.3604 0.2129 -0.0030 -0.0117 -0.0167 80  ILE B CB  
4739 C CG1 . ILE B 80  ? 0.4173 0.5396 0.3972 -0.0116 -0.0125 -0.0090 80  ILE B CG1 
4740 C CG2 . ILE B 80  ? 0.2747 0.4177 0.2642 -0.0011 -0.0089 -0.0154 80  ILE B CG2 
4741 C CD1 . ILE B 80  ? 0.4317 0.5650 0.4091 -0.0182 -0.0077 -0.0034 80  ILE B CD1 
4742 N N   . ARG B 81  ? 0.3190 0.4575 0.2958 0.0153  -0.0087 -0.0354 81  ARG B N   
4743 C CA  . ARG B 81  ? 0.2871 0.4328 0.2672 0.0262  -0.0060 -0.0418 81  ARG B CA  
4744 C C   . ARG B 81  ? 0.3200 0.4822 0.2944 0.0285  -0.0012 -0.0480 81  ARG B C   
4745 O O   . ARG B 81  ? 0.3329 0.5141 0.3117 0.0343  0.0028  -0.0500 81  ARG B O   
4746 C CB  . ARG B 81  ? 0.3290 0.4527 0.3077 0.0334  -0.0088 -0.0472 81  ARG B CB  
4747 C CG  . ARG B 81  ? 0.3621 0.4887 0.3432 0.0470  -0.0059 -0.0536 81  ARG B CG  
4748 C CD  . ARG B 81  ? 0.4636 0.5630 0.4402 0.0532  -0.0083 -0.0587 81  ARG B CD  
4749 N NE  . ARG B 81  ? 0.5406 0.6268 0.5229 0.0522  -0.0128 -0.0522 81  ARG B NE  
4750 C CZ  . ARG B 81  ? 0.5720 0.6644 0.5634 0.0598  -0.0129 -0.0481 81  ARG B CZ  
4751 N NH1 . ARG B 81  ? 0.4850 0.5980 0.4814 0.0696  -0.0087 -0.0498 81  ARG B NH1 
4752 N NH2 . ARG B 81  ? 0.5812 0.6611 0.5765 0.0574  -0.0172 -0.0422 81  ARG B NH2 
4753 N N   . LYS B 82  ? 0.3333 0.4908 0.2978 0.0236  -0.0017 -0.0509 82  LYS B N   
4754 C CA  . LYS B 82  ? 0.3290 0.5000 0.2863 0.0251  0.0026  -0.0580 82  LYS B CA  
4755 C C   . LYS B 82  ? 0.3679 0.5648 0.3271 0.0218  0.0071  -0.0548 82  LYS B C   
4756 O O   . LYS B 82  ? 0.2920 0.4939 0.2535 0.0139  0.0066  -0.0460 82  LYS B O   
4757 C CB  . LYS B 82  ? 0.3664 0.5306 0.3127 0.0174  0.0006  -0.0591 82  LYS B CB  
4758 C CG  . LYS B 82  ? 0.4964 0.6402 0.4370 0.0198  -0.0020 -0.0662 82  LYS B CG  
4759 C CD  . LYS B 82  ? 0.4939 0.6315 0.4264 0.0102  -0.0060 -0.0634 82  LYS B CD  
4760 C CE  . LYS B 82  ? 0.5286 0.6832 0.4531 0.0042  -0.0040 -0.0625 82  LYS B CE  
4761 N NZ  . LYS B 82  ? 0.6134 0.7630 0.5278 -0.0024 -0.0073 -0.0640 82  LYS B NZ  
4762 N N   . ASP B 83  ? 0.4134 0.6267 0.3706 0.0273  0.0119  -0.0626 83  ASP B N   
4763 C CA  . ASP B 83  ? 0.3273 0.5667 0.2829 0.0218  0.0165  -0.0610 83  ASP B CA  
4764 C C   . ASP B 83  ? 0.3452 0.5824 0.2904 0.0088  0.0152  -0.0552 83  ASP B C   
4765 O O   . ASP B 83  ? 0.3425 0.5682 0.2794 0.0071  0.0130  -0.0581 83  ASP B O   
4766 C CB  . ASP B 83  ? 0.3448 0.6012 0.2982 0.0294  0.0220  -0.0717 83  ASP B CB  
4767 C CG  . ASP B 83  ? 0.4800 0.7673 0.4331 0.0239  0.0271  -0.0705 83  ASP B CG  
4768 O OD1 . ASP B 83  ? 0.3947 0.6871 0.3386 0.0117  0.0275  -0.0662 83  ASP B OD1 
4769 O OD2 . ASP B 83  ? 0.4758 0.7828 0.4375 0.0318  0.0306  -0.0733 83  ASP B OD2 
4770 N N   . PRO B 84  ? 0.3226 0.5699 0.2667 -0.0007 0.0166  -0.0468 84  PRO B N   
4771 C CA  . PRO B 84  ? 0.3318 0.5741 0.2647 -0.0118 0.0154  -0.0400 84  PRO B CA  
4772 C C   . PRO B 84  ? 0.2938 0.5447 0.2157 -0.0139 0.0172  -0.0454 84  PRO B C   
4773 O O   . PRO B 84  ? 0.3342 0.5772 0.2467 -0.0204 0.0146  -0.0405 84  PRO B O   
4774 C CB  . PRO B 84  ? 0.3543 0.6083 0.2864 -0.0209 0.0187  -0.0322 84  PRO B CB  
4775 C CG  . PRO B 84  ? 0.2683 0.5251 0.2130 -0.0158 0.0189  -0.0321 84  PRO B CG  
4776 C CD  . PRO B 84  ? 0.2717 0.5330 0.2237 -0.0023 0.0190  -0.0423 84  PRO B CD  
4777 N N   . ASP B 85  ? 0.3006 0.5688 0.2231 -0.0084 0.0216  -0.0552 85  ASP B N   
4778 C CA  . ASP B 85  ? 0.3128 0.5893 0.2243 -0.0109 0.0235  -0.0616 85  ASP B CA  
4779 C C   . ASP B 85  ? 0.3800 0.6376 0.2869 -0.0085 0.0193  -0.0657 85  ASP B C   
4780 O O   . ASP B 85  ? 0.3734 0.6350 0.2693 -0.0135 0.0195  -0.0685 85  ASP B O   
4781 C CB  . ASP B 85  ? 0.3972 0.6955 0.3112 -0.0040 0.0297  -0.0727 85  ASP B CB  
4782 C CG  . ASP B 85  ? 0.5036 0.8277 0.4183 -0.0099 0.0345  -0.0696 85  ASP B CG  
4783 O OD1 . ASP B 85  ? 0.5561 0.8796 0.4649 -0.0216 0.0336  -0.0595 85  ASP B OD1 
4784 O OD2 . ASP B 85  ? 0.4531 0.7981 0.3735 -0.0028 0.0394  -0.0775 85  ASP B OD2 
4785 N N   . ASP B 86  ? 0.3633 0.6017 0.2775 -0.0019 0.0157  -0.0663 86  ASP B N   
4786 C CA  . ASP B 86  ? 0.4012 0.6215 0.3106 -0.0009 0.0118  -0.0706 86  ASP B CA  
4787 C C   . ASP B 86  ? 0.3876 0.5937 0.2956 -0.0074 0.0056  -0.0605 86  ASP B C   
4788 O O   . ASP B 86  ? 0.3750 0.5682 0.2791 -0.0080 0.0019  -0.0633 86  ASP B O   
4789 C CB  . ASP B 86  ? 0.5137 0.7200 0.4298 0.0102  0.0120  -0.0787 86  ASP B CB  
4790 C CG  . ASP B 86  ? 0.6067 0.8253 0.5238 0.0193  0.0184  -0.0897 86  ASP B CG  
4791 O OD1 . ASP B 86  ? 0.6651 0.9001 0.5746 0.0161  0.0225  -0.0948 86  ASP B OD1 
4792 O OD2 . ASP B 86  ? 0.6521 0.8641 0.5774 0.0302  0.0195  -0.0932 86  ASP B OD2 
4793 N N   . LEU B 87  ? 0.3186 0.5268 0.2291 -0.0124 0.0048  -0.0493 87  LEU B N   
4794 C CA  . LEU B 87  ? 0.2990 0.4938 0.2089 -0.0169 -0.0005 -0.0397 87  LEU B CA  
4795 C C   . LEU B 87  ? 0.3072 0.5056 0.2052 -0.0231 -0.0028 -0.0367 87  LEU B C   
4796 O O   . LEU B 87  ? 0.3290 0.5409 0.2187 -0.0281 0.0000  -0.0346 87  LEU B O   
4797 C CB  . LEU B 87  ? 0.2896 0.4839 0.2036 -0.0204 0.0004  -0.0290 87  LEU B CB  
4798 C CG  . LEU B 87  ? 0.2794 0.4682 0.2058 -0.0158 0.0008  -0.0290 87  LEU B CG  
4799 C CD1 . LEU B 87  ? 0.2918 0.4824 0.2194 -0.0218 0.0030  -0.0195 87  LEU B CD1 
4800 C CD2 . LEU B 87  ? 0.2920 0.4624 0.2237 -0.0124 -0.0044 -0.0294 87  LEU B CD2 
4801 N N   . GLU B 88  ? 0.3080 0.4960 0.2048 -0.0236 -0.0079 -0.0361 88  GLU B N   
4802 C CA  . GLU B 88  ? 0.3139 0.5063 0.2009 -0.0293 -0.0113 -0.0299 88  GLU B CA  
4803 C C   . GLU B 88  ? 0.3228 0.5126 0.2097 -0.0319 -0.0122 -0.0157 88  GLU B C   
4804 O O   . GLU B 88  ? 0.2995 0.4796 0.1948 -0.0300 -0.0118 -0.0111 88  GLU B O   
4805 C CB  . GLU B 88  ? 0.3208 0.5052 0.2076 -0.0294 -0.0167 -0.0324 88  GLU B CB  
4806 C CG  . GLU B 88  ? 0.4393 0.6192 0.3253 -0.0271 -0.0156 -0.0462 88  GLU B CG  
4807 C CD  . GLU B 88  ? 0.5413 0.7098 0.4283 -0.0283 -0.0207 -0.0480 88  GLU B CD  
4808 O OE1 . GLU B 88  ? 0.6619 0.8248 0.5441 -0.0287 -0.0201 -0.0592 88  GLU B OE1 
4809 O OE2 . GLU B 88  ? 0.6434 0.8080 0.5351 -0.0291 -0.0249 -0.0386 88  GLU B OE2 
4810 N N   . LYS B 89  ? 0.3173 0.5147 0.1935 -0.0366 -0.0133 -0.0086 89  LYS B N   
4811 C CA  . LYS B 89  ? 0.3171 0.5082 0.1908 -0.0381 -0.0143 0.0055  89  LYS B CA  
4812 C C   . LYS B 89  ? 0.4715 0.6485 0.3544 -0.0341 -0.0184 0.0103  89  LYS B C   
4813 O O   . LYS B 89  ? 0.3660 0.5324 0.2524 -0.0334 -0.0170 0.0180  89  LYS B O   
4814 C CB  . LYS B 89  ? 0.3296 0.5297 0.1902 -0.0420 -0.0164 0.0128  89  LYS B CB  
4815 C CG  . LYS B 89  ? 0.4208 0.6348 0.2704 -0.0475 -0.0123 0.0102  89  LYS B CG  
4816 C CD  . LYS B 89  ? 0.4014 0.6229 0.2376 -0.0513 -0.0153 0.0196  89  LYS B CD  
4817 C CE  . LYS B 89  ? 0.4677 0.7060 0.2923 -0.0578 -0.0120 0.0147  89  LYS B CE  
4818 N NZ  . LYS B 89  ? 0.5284 0.7679 0.3539 -0.0603 -0.0053 0.0114  89  LYS B NZ  
4819 N N   . GLU B 90  ? 0.3067 0.4839 0.1925 -0.0324 -0.0231 0.0053  90  GLU B N   
4820 C CA  . GLU B 90  ? 0.4266 0.5932 0.3211 -0.0293 -0.0270 0.0089  90  GLU B CA  
4821 C C   . GLU B 90  ? 0.4204 0.5747 0.3259 -0.0268 -0.0246 0.0062  90  GLU B C   
4822 O O   . GLU B 90  ? 0.3488 0.4930 0.2606 -0.0252 -0.0256 0.0127  90  GLU B O   
4823 C CB  . GLU B 90  ? 0.4223 0.5931 0.3167 -0.0300 -0.0319 0.0019  90  GLU B CB  
4824 C CG  . GLU B 90  ? 0.6518 0.8131 0.5557 -0.0279 -0.0357 0.0025  90  GLU B CG  
4825 C CD  . GLU B 90  ? 0.8008 0.9513 0.7115 -0.0270 -0.0346 -0.0083 90  GLU B CD  
4826 O OE1 . GLU B 90  ? 0.6694 0.8092 0.5891 -0.0252 -0.0358 -0.0065 90  GLU B OE1 
4827 O OE2 . GLU B 90  ? 0.8931 1.0455 0.7997 -0.0277 -0.0322 -0.0183 90  GLU B OE2 
4828 N N   . GLU B 91  ? 0.2863 0.4422 0.1942 -0.0261 -0.0214 -0.0033 91  GLU B N   
4829 C CA  . GLU B 91  ? 0.2768 0.4237 0.1949 -0.0235 -0.0194 -0.0056 91  GLU B CA  
4830 C C   . GLU B 91  ? 0.2737 0.4198 0.1925 -0.0256 -0.0151 0.0022  91  GLU B C   
4831 O O   . GLU B 91  ? 0.2847 0.4212 0.2109 -0.0252 -0.0147 0.0058  91  GLU B O   
4832 C CB  . GLU B 91  ? 0.2944 0.4444 0.2145 -0.0205 -0.0171 -0.0174 91  GLU B CB  
4833 C CG  . GLU B 91  ? 0.3560 0.5005 0.2752 -0.0191 -0.0205 -0.0260 91  GLU B CG  
4834 C CD  . GLU B 91  ? 0.4214 0.5655 0.3409 -0.0148 -0.0174 -0.0377 91  GLU B CD  
4835 O OE1 . GLU B 91  ? 0.3330 0.4889 0.2468 -0.0146 -0.0135 -0.0422 91  GLU B OE1 
4836 O OE2 . GLU B 91  ? 0.4178 0.5494 0.3429 -0.0111 -0.0185 -0.0421 91  GLU B OE2 
4837 N N   . VAL B 92  ? 0.2816 0.4374 0.1912 -0.0291 -0.0116 0.0047  92  VAL B N   
4838 C CA  . VAL B 92  ? 0.3258 0.4796 0.2329 -0.0332 -0.0071 0.0123  92  VAL B CA  
4839 C C   . VAL B 92  ? 0.2830 0.4227 0.1886 -0.0338 -0.0087 0.0232  92  VAL B C   
4840 O O   . VAL B 92  ? 0.3254 0.4554 0.2340 -0.0358 -0.0059 0.0279  92  VAL B O   
4841 C CB  . VAL B 92  ? 0.3312 0.4980 0.2266 -0.0382 -0.0032 0.0129  92  VAL B CB  
4842 C CG1 . VAL B 92  ? 0.2966 0.4594 0.1867 -0.0445 0.0018  0.0208  92  VAL B CG1 
4843 C CG2 . VAL B 92  ? 0.3234 0.5049 0.2215 -0.0365 -0.0008 0.0014  92  VAL B CG2 
4844 N N   . GLU B 93  ? 0.3325 0.4718 0.2335 -0.0319 -0.0130 0.0273  93  GLU B N   
4845 C CA  . GLU B 93  ? 0.3314 0.4587 0.2314 -0.0302 -0.0145 0.0379  93  GLU B CA  
4846 C C   . GLU B 93  ? 0.3605 0.4769 0.2730 -0.0274 -0.0160 0.0366  93  GLU B C   
4847 O O   . GLU B 93  ? 0.4351 0.5389 0.3485 -0.0279 -0.0133 0.0431  93  GLU B O   
4848 C CB  . GLU B 93  ? 0.4636 0.5975 0.3581 -0.0275 -0.0197 0.0417  93  GLU B CB  
4849 C CG  . GLU B 93  ? 0.5944 0.7325 0.4745 -0.0298 -0.0183 0.0499  93  GLU B CG  
4850 C CD  . GLU B 93  ? 0.6477 0.7997 0.5225 -0.0285 -0.0236 0.0503  93  GLU B CD  
4851 O OE1 . GLU B 93  ? 0.6604 0.8165 0.5427 -0.0255 -0.0286 0.0466  93  GLU B OE1 
4852 O OE2 . GLU B 93  ? 0.6950 0.8549 0.5576 -0.0316 -0.0229 0.0544  93  GLU B OE2 
4853 N N   . LYS B 94  ? 0.3329 0.4528 0.2537 -0.0251 -0.0197 0.0280  94  LYS B N   
4854 C CA  . LYS B 94  ? 0.3044 0.4146 0.2364 -0.0234 -0.0214 0.0264  94  LYS B CA  
4855 C C   . LYS B 94  ? 0.3106 0.4146 0.2475 -0.0259 -0.0166 0.0260  94  LYS B C   
4856 O O   . LYS B 94  ? 0.3092 0.4028 0.2519 -0.0263 -0.0161 0.0293  94  LYS B O   
4857 C CB  . LYS B 94  ? 0.3660 0.4796 0.3034 -0.0218 -0.0257 0.0168  94  LYS B CB  
4858 C CG  . LYS B 94  ? 0.5029 0.6246 0.4354 -0.0213 -0.0305 0.0160  94  LYS B CG  
4859 C CD  . LYS B 94  ? 0.5598 0.6800 0.4932 -0.0194 -0.0334 0.0252  94  LYS B CD  
4860 C CE  . LYS B 94  ? 0.6133 0.7470 0.5408 -0.0193 -0.0382 0.0255  94  LYS B CE  
4861 N NZ  . LYS B 94  ? 0.6935 0.8371 0.6095 -0.0205 -0.0369 0.0281  94  LYS B NZ  
4862 N N   . LEU B 95  ? 0.2935 0.4057 0.2282 -0.0279 -0.0131 0.0215  95  LEU B N   
4863 C CA  . LEU B 95  ? 0.2795 0.3904 0.2186 -0.0311 -0.0087 0.0212  95  LEU B CA  
4864 C C   . LEU B 95  ? 0.3147 0.4169 0.2473 -0.0363 -0.0042 0.0303  95  LEU B C   
4865 O O   . LEU B 95  ? 0.3167 0.4110 0.2538 -0.0393 -0.0018 0.0322  95  LEU B O   
4866 C CB  . LEU B 95  ? 0.2779 0.4036 0.2160 -0.0314 -0.0060 0.0144  95  LEU B CB  
4867 C CG  . LEU B 95  ? 0.4248 0.5558 0.3678 -0.0345 -0.0016 0.0134  95  LEU B CG  
4868 C CD1 . LEU B 95  ? 0.4300 0.5543 0.3848 -0.0314 -0.0042 0.0110  95  LEU B CD1 
4869 C CD2 . LEU B 95  ? 0.4551 0.6046 0.3965 -0.0335 0.0012  0.0070  95  LEU B CD2 
4870 N N   . ILE B 96  ? 0.2679 0.3705 0.1886 -0.0381 -0.0026 0.0359  96  ILE B N   
4871 C CA  . ILE B 96  ? 0.3267 0.4167 0.2381 -0.0429 0.0022  0.0450  96  ILE B CA  
4872 C C   . ILE B 96  ? 0.3602 0.4341 0.2752 -0.0391 0.0005  0.0506  96  ILE B C   
4873 O O   . ILE B 96  ? 0.3062 0.3666 0.2201 -0.0427 0.0049  0.0547  96  ILE B O   
4874 C CB  . ILE B 96  ? 0.3614 0.4545 0.2578 -0.0449 0.0037  0.0503  96  ILE B CB  
4875 C CG1 . ILE B 96  ? 0.3626 0.4725 0.2551 -0.0502 0.0067  0.0445  96  ILE B CG1 
4876 C CG2 . ILE B 96  ? 0.3282 0.4029 0.2126 -0.0486 0.0083  0.0609  96  ILE B CG2 
4877 C CD1 . ILE B 96  ? 0.3950 0.5077 0.2710 -0.0547 0.0091  0.0500  96  ILE B CD1 
4878 N N   . GLU B 97  ? 0.3028 0.3793 0.2223 -0.0323 -0.0056 0.0502  97  GLU B N   
4879 C CA  . GLU B 97  ? 0.3039 0.3698 0.2285 -0.0276 -0.0077 0.0547  97  GLU B CA  
4880 C C   . GLU B 97  ? 0.2884 0.3477 0.2241 -0.0295 -0.0068 0.0507  97  GLU B C   
4881 O O   . GLU B 97  ? 0.2760 0.3220 0.2127 -0.0296 -0.0042 0.0553  97  GLU B O   
4882 C CB  . GLU B 97  ? 0.4550 0.5312 0.3831 -0.0217 -0.0148 0.0529  97  GLU B CB  
4883 C CG  . GLU B 97  ? 0.5397 0.6107 0.4700 -0.0157 -0.0173 0.0594  97  GLU B CG  
4884 C CD  . GLU B 97  ? 0.7800 0.8655 0.7080 -0.0116 -0.0234 0.0602  97  GLU B CD  
4885 O OE1 . GLU B 97  ? 0.7981 0.8947 0.7315 -0.0126 -0.0278 0.0518  97  GLU B OE1 
4886 O OE2 . GLU B 97  ? 0.9008 0.9865 0.8205 -0.0076 -0.0235 0.0693  97  GLU B OE2 
4887 N N   . PHE B 98  ? 0.2570 0.3253 0.2009 -0.0306 -0.0090 0.0421  98  PHE B N   
4888 C CA  . PHE B 98  ? 0.2526 0.3163 0.2066 -0.0328 -0.0087 0.0386  98  PHE B CA  
4889 C C   . PHE B 98  ? 0.2558 0.3131 0.2065 -0.0398 -0.0019 0.0414  98  PHE B C   
4890 O O   . PHE B 98  ? 0.2738 0.3217 0.2290 -0.0425 0.0001  0.0426  98  PHE B O   
4891 C CB  . PHE B 98  ? 0.3055 0.3796 0.2664 -0.0314 -0.0122 0.0298  98  PHE B CB  
4892 C CG  . PHE B 98  ? 0.2318 0.3020 0.2031 -0.0325 -0.0135 0.0263  98  PHE B CG  
4893 C CD1 . PHE B 98  ? 0.3378 0.4039 0.3153 -0.0301 -0.0185 0.0242  98  PHE B CD1 
4894 C CD2 . PHE B 98  ? 0.2154 0.2883 0.1897 -0.0365 -0.0101 0.0249  98  PHE B CD2 
4895 C CE1 . PHE B 98  ? 0.2821 0.3442 0.2680 -0.0319 -0.0199 0.0212  98  PHE B CE1 
4896 C CE2 . PHE B 98  ? 0.2437 0.3140 0.2272 -0.0376 -0.0118 0.0223  98  PHE B CE2 
4897 C CZ  . PHE B 98  ? 0.2577 0.3216 0.2466 -0.0353 -0.0166 0.0206  98  PHE B CZ  
4898 N N   . THR B 99  ? 0.2699 0.3335 0.2122 -0.0439 0.0021  0.0420  99  THR B N   
4899 C CA  . THR B 99  ? 0.3115 0.3703 0.2482 -0.0527 0.0091  0.0446  99  THR B CA  
4900 C C   . THR B 99  ? 0.3019 0.3406 0.2300 -0.0546 0.0133  0.0524  99  THR B C   
4901 O O   . THR B 99  ? 0.3221 0.3506 0.2503 -0.0606 0.0179  0.0536  99  THR B O   
4902 C CB  . THR B 99  ? 0.2957 0.3669 0.2236 -0.0575 0.0125  0.0437  99  THR B CB  
4903 O OG1 . THR B 99  ? 0.2936 0.3832 0.2295 -0.0536 0.0089  0.0360  99  THR B OG1 
4904 C CG2 . THR B 99  ? 0.2775 0.3469 0.1999 -0.0686 0.0197  0.0453  99  THR B CG2 
4905 N N   . LYS B 100 ? 0.3162 0.3489 0.2366 -0.0492 0.0121  0.0580  100 LYS B N   
4906 C CA  . LYS B 100 ? 0.3014 0.3133 0.2121 -0.0488 0.0165  0.0663  100 LYS B CA  
4907 C C   . LYS B 100 ? 0.3306 0.3324 0.2510 -0.0451 0.0157  0.0662  100 LYS B C   
4908 O O   . LYS B 100 ? 0.3262 0.3098 0.2412 -0.0483 0.0218  0.0700  100 LYS B O   
4909 C CB  . LYS B 100 ? 0.3444 0.3549 0.2461 -0.0417 0.0141  0.0729  100 LYS B CB  
4910 C CG  . LYS B 100 ? 0.5319 0.5491 0.4205 -0.0463 0.0160  0.0747  100 LYS B CG  
4911 C CD  . LYS B 100 ? 0.6356 0.6412 0.5103 -0.0413 0.0166  0.0851  100 LYS B CD  
4912 C CE  . LYS B 100 ? 0.6976 0.6997 0.5541 -0.0496 0.0218  0.0893  100 LYS B CE  
4913 N NZ  . LYS B 100 ? 0.8231 0.8466 0.6826 -0.0570 0.0215  0.0807  100 LYS B NZ  
4914 N N   . LEU B 101 ? 0.2716 0.2846 0.2053 -0.0391 0.0086  0.0615  101 LEU B N   
4915 C CA  . LEU B 101 ? 0.3130 0.3200 0.2568 -0.0360 0.0071  0.0606  101 LEU B CA  
4916 C C   . LEU B 101 ? 0.2990 0.3000 0.2471 -0.0445 0.0114  0.0572  101 LEU B C   
4917 O O   . LEU B 101 ? 0.3113 0.3005 0.2619 -0.0446 0.0140  0.0585  101 LEU B O   
4918 C CB  . LEU B 101 ? 0.3665 0.3882 0.3216 -0.0305 -0.0014 0.0554  101 LEU B CB  
4919 C CG  . LEU B 101 ? 0.3710 0.3910 0.3374 -0.0284 -0.0042 0.0530  101 LEU B CG  
4920 C CD1 . LEU B 101 ? 0.4451 0.4568 0.4095 -0.0215 -0.0030 0.0597  101 LEU B CD1 
4921 C CD2 . LEU B 101 ? 0.3737 0.4081 0.3484 -0.0262 -0.0120 0.0466  101 LEU B CD2 
4922 N N   . ASN B 102 ? 0.2737 0.2845 0.2228 -0.0515 0.0123  0.0528  102 ASN B N   
4923 C CA  . ASN B 102 ? 0.2527 0.2627 0.2064 -0.0601 0.0156  0.0496  102 ASN B CA  
4924 C C   . ASN B 102 ? 0.2714 0.2747 0.2131 -0.0707 0.0241  0.0521  102 ASN B C   
4925 O O   . ASN B 102 ? 0.3012 0.3056 0.2451 -0.0796 0.0275  0.0498  102 ASN B O   
4926 C CB  . ASN B 102 ? 0.3087 0.3367 0.2729 -0.0601 0.0104  0.0431  102 ASN B CB  
4927 C CG  . ASN B 102 ? 0.3266 0.3586 0.3012 -0.0523 0.0027  0.0397  102 ASN B CG  
4928 O OD1 . ASN B 102 ? 0.3570 0.3816 0.3371 -0.0515 0.0015  0.0399  102 ASN B OD1 
4929 N ND2 . ASN B 102 ? 0.3699 0.4135 0.3464 -0.0474 -0.0022 0.0360  102 ASN B ND2 
4930 N N   . TYR B 103 ? 0.3168 0.2433 0.2740 -0.0173 0.0200  0.0577  103 TYR B N   
4931 C CA  . TYR B 103 ? 0.3933 0.3099 0.3465 -0.0290 0.0265  0.0597  103 TYR B CA  
4932 C C   . TYR B 103 ? 0.3681 0.2566 0.3197 -0.0352 0.0318  0.0564  103 TYR B C   
4933 O O   . TYR B 103 ? 0.3256 0.2114 0.2776 -0.0483 0.0348  0.0508  103 TYR B O   
4934 C CB  . TYR B 103 ? 0.4512 0.3652 0.3956 -0.0269 0.0310  0.0744  103 TYR B CB  
4935 C CG  . TYR B 103 ? 0.4891 0.3915 0.4278 -0.0395 0.0389  0.0791  103 TYR B CG  
4936 C CD1 . TYR B 103 ? 0.5920 0.4611 0.5243 -0.0431 0.0468  0.0847  103 TYR B CD1 
4937 C CD2 . TYR B 103 ? 0.5455 0.4695 0.4847 -0.0479 0.0393  0.0780  103 TYR B CD2 
4938 C CE1 . TYR B 103 ? 0.6209 0.4779 0.5474 -0.0566 0.0545  0.0889  103 TYR B CE1 
4939 C CE2 . TYR B 103 ? 0.5430 0.4585 0.4774 -0.0607 0.0468  0.0827  103 TYR B CE2 
4940 C CZ  . TYR B 103 ? 0.6260 0.5076 0.5540 -0.0659 0.0543  0.0882  103 TYR B CZ  
4941 O OH  . TYR B 103 ? 0.8110 0.6827 0.7337 -0.0806 0.0624  0.0927  103 TYR B OH  
4942 N N   . GLU B 104 ? 0.3640 0.2327 0.3136 -0.0263 0.0333  0.0594  104 GLU B N   
4943 C CA  . GLU B 104 ? 0.4918 0.3310 0.4377 -0.0318 0.0394  0.0556  104 GLU B CA  
4944 C C   . GLU B 104 ? 0.4296 0.2733 0.3818 -0.0358 0.0353  0.0412  104 GLU B C   
4945 O O   . GLU B 104 ? 0.4724 0.2946 0.4211 -0.0427 0.0399  0.0355  104 GLU B O   
4946 C CB  . GLU B 104 ? 0.5113 0.3259 0.4517 -0.0191 0.0442  0.0651  104 GLU B CB  
4947 C CG  . GLU B 104 ? 0.5641 0.3751 0.4979 -0.0124 0.0479  0.0815  104 GLU B CG  
4948 C CD  . GLU B 104 ? 0.6975 0.4809 0.6215 -0.0228 0.0578  0.0874  104 GLU B CD  
4949 O OE1 . GLU B 104 ? 0.6739 0.4354 0.5955 -0.0335 0.0626  0.0786  104 GLU B OE1 
4950 O OE2 . GLU B 104 ? 0.8164 0.6000 0.7344 -0.0211 0.0610  0.1008  104 GLU B OE2 
4951 N N   . LYS B 105 ? 0.3263 0.1956 0.2864 -0.0320 0.0273  0.0352  105 LYS B N   
4952 C CA  . LYS B 105 ? 0.3175 0.1902 0.2826 -0.0344 0.0236  0.0233  105 LYS B CA  
4953 C C   . LYS B 105 ? 0.3754 0.2563 0.3425 -0.0491 0.0237  0.0152  105 LYS B C   
4954 O O   . LYS B 105 ? 0.3260 0.2238 0.2951 -0.0545 0.0232  0.0168  105 LYS B O   
4955 C CB  . LYS B 105 ? 0.3475 0.2424 0.3198 -0.0253 0.0157  0.0204  105 LYS B CB  
4956 C CG  . LYS B 105 ? 0.3519 0.2459 0.3236 -0.0120 0.0147  0.0285  105 LYS B CG  
4957 C CD  . LYS B 105 ? 0.3000 0.2177 0.2778 -0.0063 0.0072  0.0257  105 LYS B CD  
4958 C CE  . LYS B 105 ? 0.3302 0.2504 0.3081 0.0055  0.0059  0.0334  105 LYS B CE  
4959 N NZ  . LYS B 105 ? 0.3203 0.2621 0.3034 0.0086  -0.0012 0.0293  105 LYS B NZ  
4960 N N   . PRO B 106 ? 0.3298 0.2019 0.2964 -0.0558 0.0244  0.0063  106 PRO B N   
4961 C CA  . PRO B 106 ? 0.2976 0.1812 0.2665 -0.0707 0.0242  -0.0012 106 PRO B CA  
4962 C C   . PRO B 106 ? 0.2816 0.1988 0.2597 -0.0699 0.0176  -0.0041 106 PRO B C   
4963 O O   . PRO B 106 ? 0.3565 0.2883 0.3373 -0.0808 0.0183  -0.0065 106 PRO B O   
4964 C CB  . PRO B 106 ? 0.3267 0.1988 0.2933 -0.0747 0.0242  -0.0107 106 PRO B CB  
4965 C CG  . PRO B 106 ? 0.3613 0.2039 0.3207 -0.0659 0.0292  -0.0065 106 PRO B CG  
4966 C CD  . PRO B 106 ? 0.2970 0.1475 0.2597 -0.0511 0.0266  0.0033  106 PRO B CD  
4967 N N   . ILE B 107 ? 0.2440 0.1737 0.2268 -0.0578 0.0118  -0.0043 107 ILE B N   
4968 C CA  . ILE B 107 ? 0.2254 0.1831 0.2158 -0.0560 0.0069  -0.0072 107 ILE B CA  
4969 C C   . ILE B 107 ? 0.2660 0.2355 0.2563 -0.0569 0.0089  -0.0014 107 ILE B C   
4970 O O   . ILE B 107 ? 0.2469 0.2395 0.2428 -0.0567 0.0066  -0.0041 107 ILE B O   
4971 C CB  . ILE B 107 ? 0.2426 0.2078 0.2368 -0.0439 0.0010  -0.0093 107 ILE B CB  
4972 C CG1 . ILE B 107 ? 0.2817 0.2389 0.2728 -0.0343 0.0010  -0.0028 107 ILE B CG1 
4973 C CG2 . ILE B 107 ? 0.2192 0.1784 0.2141 -0.0438 -0.0013 -0.0154 107 ILE B CG2 
4974 C CD1 . ILE B 107 ? 0.2422 0.2113 0.2373 -0.0252 -0.0045 -0.0052 107 ILE B CD1 
4975 N N   . TYR B 108 ? 0.2731 0.2277 0.2567 -0.0571 0.0137  0.0069  108 TYR B N   
4976 C CA  . TYR B 108 ? 0.2781 0.2428 0.2596 -0.0594 0.0165  0.0134  108 TYR B CA  
4977 C C   . TYR B 108 ? 0.3080 0.2665 0.2863 -0.0738 0.0231  0.0157  108 TYR B C   
4978 O O   . TYR B 108 ? 0.3420 0.3042 0.3167 -0.0768 0.0270  0.0230  108 TYR B O   
4979 C CB  . TYR B 108 ? 0.2799 0.2357 0.2554 -0.0496 0.0172  0.0229  108 TYR B CB  
4980 C CG  . TYR B 108 ? 0.2730 0.2474 0.2515 -0.0393 0.0114  0.0211  108 TYR B CG  
4981 C CD1 . TYR B 108 ? 0.2301 0.2046 0.2126 -0.0321 0.0062  0.0154  108 TYR B CD1 
4982 C CD2 . TYR B 108 ? 0.2572 0.2486 0.2337 -0.0380 0.0116  0.0244  108 TYR B CD2 
4983 C CE1 . TYR B 108 ? 0.2572 0.2462 0.2416 -0.0247 0.0015  0.0129  108 TYR B CE1 
4984 C CE2 . TYR B 108 ? 0.2199 0.2262 0.1976 -0.0302 0.0068  0.0211  108 TYR B CE2 
4985 C CZ  . TYR B 108 ? 0.2479 0.2521 0.2296 -0.0240 0.0018  0.0151  108 TYR B CZ  
4986 O OH  . TYR B 108 ? 0.2283 0.2450 0.2102 -0.0180 -0.0023 0.0111  108 TYR B OH  
4987 N N   . ARG B 109 ? 0.2728 0.2226 0.2516 -0.0841 0.0245  0.0095  109 ARG B N   
4988 C CA  . ARG B 109 ? 0.3599 0.3012 0.3348 -0.1003 0.0313  0.0110  109 ARG B CA  
4989 C C   . ARG B 109 ? 0.3840 0.3579 0.3665 -0.1090 0.0306  0.0082  109 ARG B C   
4990 O O   . ARG B 109 ? 0.3469 0.3360 0.3354 -0.1181 0.0287  0.0002  109 ARG B O   
4991 C CB  . ARG B 109 ? 0.3946 0.3148 0.3659 -0.1097 0.0335  0.0042  109 ARG B CB  
4992 C CG  . ARG B 109 ? 0.5125 0.4011 0.4731 -0.1204 0.0428  0.0095  109 ARG B CG  
4993 C CD  . ARG B 109 ? 0.6788 0.5502 0.6353 -0.1350 0.0459  0.0001  109 ARG B CD  
4994 N NE  . ARG B 109 ? 0.7724 0.6335 0.7283 -0.1264 0.0422  -0.0070 109 ARG B NE  
4995 C CZ  . ARG B 109 ? 0.7765 0.6074 0.7250 -0.1160 0.0456  -0.0036 109 ARG B CZ  
4996 N NH1 . ARG B 109 ? 0.8790 0.6861 0.8201 -0.1116 0.0523  0.0075  109 ARG B NH1 
4997 N NH2 . ARG B 109 ? 0.6284 0.4537 0.5769 -0.1094 0.0425  -0.0107 109 ARG B NH2 
4998 N N   . PHE B 110 ? 0.3601 0.3474 0.3423 -0.1055 0.0321  0.0150  110 PHE B N   
4999 C CA  . PHE B 110 ? 0.3125 0.3296 0.3006 -0.1134 0.0336  0.0144  110 PHE B CA  
5000 C C   . PHE B 110 ? 0.3576 0.3648 0.3377 -0.1221 0.0416  0.0246  110 PHE B C   
5001 O O   . PHE B 110 ? 0.3808 0.3728 0.3529 -0.1135 0.0433  0.0335  110 PHE B O   
5002 C CB  . PHE B 110 ? 0.2805 0.3251 0.2747 -0.1003 0.0290  0.0126  110 PHE B CB  
5003 C CG  . PHE B 110 ? 0.2386 0.2935 0.2404 -0.0911 0.0218  0.0038  110 PHE B CG  
5004 C CD1 . PHE B 110 ? 0.2961 0.3775 0.3078 -0.0947 0.0196  -0.0029 110 PHE B CD1 
5005 C CD2 . PHE B 110 ? 0.3108 0.3511 0.3101 -0.0783 0.0174  0.0031  110 PHE B CD2 
5006 C CE1 . PHE B 110 ? 0.3040 0.3941 0.3219 -0.0852 0.0134  -0.0094 110 PHE B CE1 
5007 C CE2 . PHE B 110 ? 0.3513 0.3997 0.3568 -0.0704 0.0115  -0.0041 110 PHE B CE2 
5008 C CZ  . PHE B 110 ? 0.3407 0.4129 0.3550 -0.0734 0.0096  -0.0099 110 PHE B CZ  
5009 N N   . GLU B 111 ? 0.3562 0.3732 0.3382 -0.1393 0.0464  0.0240  111 GLU B N   
5010 C CA  . GLU B 111 ? 0.3904 0.3984 0.3644 -0.1491 0.0548  0.0345  111 GLU B CA  
5011 C C   . GLU B 111 ? 0.3972 0.4238 0.3698 -0.1384 0.0548  0.0417  111 GLU B C   
5012 O O   . GLU B 111 ? 0.3902 0.4005 0.3524 -0.1365 0.0596  0.0532  111 GLU B O   
5013 C CB  . GLU B 111 ? 0.5133 0.5360 0.4916 -0.1707 0.0596  0.0313  111 GLU B CB  
5014 C CG  . GLU B 111 ? 0.6644 0.6886 0.6368 -0.1822 0.0683  0.0418  111 GLU B CG  
5015 C CD  . GLU B 111 ? 0.7515 0.7314 0.7088 -0.1850 0.0755  0.0528  111 GLU B CD  
5016 O OE1 . GLU B 111 ? 0.8273 0.7745 0.7793 -0.1817 0.0748  0.0504  111 GLU B OE1 
5017 O OE2 . GLU B 111 ? 0.8507 0.8285 0.8009 -0.1897 0.0824  0.0642  111 GLU B OE2 
5018 N N   . ARG B 112 ? 0.3670 0.4267 0.3489 -0.1302 0.0498  0.0352  112 ARG B N   
5019 C CA  . ARG B 112 ? 0.3530 0.4323 0.3328 -0.1213 0.0504  0.0400  112 ARG B CA  
5020 C C   . ARG B 112 ? 0.3312 0.3917 0.3018 -0.1068 0.0478  0.0460  112 ARG B C   
5021 O O   . ARG B 112 ? 0.3334 0.3984 0.2963 -0.1035 0.0507  0.0545  112 ARG B O   
5022 C CB  . ARG B 112 ? 0.2941 0.4085 0.2851 -0.1141 0.0461  0.0304  112 ARG B CB  
5023 C CG  . ARG B 112 ? 0.2799 0.4149 0.2679 -0.1048 0.0473  0.0328  112 ARG B CG  
5024 C CD  . ARG B 112 ? 0.2903 0.4345 0.2726 -0.1156 0.0555  0.0421  112 ARG B CD  
5025 N NE  . ARG B 112 ? 0.2832 0.4574 0.2660 -0.1081 0.0568  0.0403  112 ARG B NE  
5026 C CZ  . ARG B 112 ? 0.4404 0.6259 0.4157 -0.1121 0.0631  0.0483  112 ARG B CZ  
5027 N NH1 . ARG B 112 ? 0.5226 0.6907 0.4891 -0.1236 0.0688  0.0602  112 ARG B NH1 
5028 N NH2 . ARG B 112 ? 0.4275 0.6408 0.4031 -0.1043 0.0643  0.0445  112 ARG B NH2 
5029 N N   . ILE B 113 ? 0.3189 0.3607 0.2900 -0.0984 0.0425  0.0420  113 ILE B N   
5030 C CA  . ILE B 113 ? 0.3616 0.3873 0.3250 -0.0856 0.0400  0.0482  113 ILE B CA  
5031 C C   . ILE B 113 ? 0.4162 0.4167 0.3685 -0.0896 0.0465  0.0618  113 ILE B C   
5032 O O   . ILE B 113 ? 0.4341 0.4337 0.3785 -0.0816 0.0470  0.0714  113 ILE B O   
5033 C CB  . ILE B 113 ? 0.3512 0.3639 0.3186 -0.0769 0.0337  0.0412  113 ILE B CB  
5034 C CG1 . ILE B 113 ? 0.3696 0.4056 0.3457 -0.0697 0.0274  0.0303  113 ILE B CG1 
5035 C CG2 . ILE B 113 ? 0.3414 0.3364 0.3014 -0.0655 0.0321  0.0489  113 ILE B CG2 
5036 C CD1 . ILE B 113 ? 0.4750 0.4992 0.4547 -0.0623 0.0217  0.0241  113 ILE B CD1 
5037 N N   . ARG B 114 ? 0.4093 0.3885 0.3599 -0.1020 0.0520  0.0630  114 ARG B N   
5038 C CA  . ARG B 114 ? 0.4347 0.3858 0.3737 -0.1061 0.0597  0.0765  114 ARG B CA  
5039 C C   . ARG B 114 ? 0.3797 0.3461 0.3129 -0.1106 0.0648  0.0868  114 ARG B C   
5040 O O   . ARG B 114 ? 0.4756 0.4296 0.3983 -0.1045 0.0680  0.1005  114 ARG B O   
5041 C CB  . ARG B 114 ? 0.4433 0.3682 0.3808 -0.1214 0.0656  0.0738  114 ARG B CB  
5042 C CG  . ARG B 114 ? 0.6723 0.5732 0.6107 -0.1156 0.0626  0.0669  114 ARG B CG  
5043 C CD  . ARG B 114 ? 0.7862 0.6549 0.7192 -0.1308 0.0699  0.0647  114 ARG B CD  
5044 N NE  . ARG B 114 ? 0.8445 0.7277 0.7861 -0.1441 0.0672  0.0502  114 ARG B NE  
5045 C CZ  . ARG B 114 ? 0.7743 0.6696 0.7241 -0.1379 0.0595  0.0387  114 ARG B CZ  
5046 N NH1 . ARG B 114 ? 0.6916 0.5855 0.6426 -0.1196 0.0537  0.0390  114 ARG B NH1 
5047 N NH2 . ARG B 114 ? 0.7240 0.6343 0.6806 -0.1508 0.0575  0.0273  114 ARG B NH2 
5048 N N   . GLU B 115 ? 0.3770 0.3724 0.3168 -0.1205 0.0658  0.0810  115 GLU B N   
5049 C CA  . GLU B 115 ? 0.4001 0.4138 0.3347 -0.1252 0.0711  0.0900  115 GLU B CA  
5050 C C   . GLU B 115 ? 0.4281 0.4587 0.3581 -0.1094 0.0668  0.0939  115 GLU B C   
5051 O O   . GLU B 115 ? 0.4152 0.4457 0.3345 -0.1082 0.0710  0.1068  115 GLU B O   
5052 C CB  . GLU B 115 ? 0.4769 0.5229 0.4215 -0.1374 0.0728  0.0817  115 GLU B CB  
5053 C CG  . GLU B 115 ? 0.5843 0.6208 0.5330 -0.1566 0.0776  0.0782  115 GLU B CG  
5054 C CD  . GLU B 115 ? 0.6464 0.7220 0.6082 -0.1656 0.0770  0.0684  115 GLU B CD  
5055 O OE1 . GLU B 115 ? 0.5586 0.6663 0.5240 -0.1579 0.0757  0.0672  115 GLU B OE1 
5056 O OE2 . GLU B 115 ? 0.6983 0.7738 0.6666 -0.1800 0.0780  0.0618  115 GLU B OE2 
5057 N N   . LEU B 116 ? 0.4554 0.5013 0.3928 -0.0981 0.0586  0.0826  116 LEU B N   
5058 C CA  . LEU B 116 ? 0.4566 0.5210 0.3896 -0.0853 0.0543  0.0832  116 LEU B CA  
5059 C C   . LEU B 116 ? 0.4645 0.5098 0.3869 -0.0756 0.0530  0.0952  116 LEU B C   
5060 O O   . LEU B 116 ? 0.4331 0.4910 0.3465 -0.0705 0.0533  0.1033  116 LEU B O   
5061 C CB  . LEU B 116 ? 0.3625 0.4418 0.3051 -0.0765 0.0465  0.0681  116 LEU B CB  
5062 C CG  . LEU B 116 ? 0.3715 0.4771 0.3242 -0.0819 0.0476  0.0574  116 LEU B CG  
5063 C CD1 . LEU B 116 ? 0.4379 0.5514 0.3998 -0.0724 0.0405  0.0437  116 LEU B CD1 
5064 C CD2 . LEU B 116 ? 0.4266 0.5580 0.3741 -0.0833 0.0522  0.0607  116 LEU B CD2 
5065 N N   . MET B 117 ? 0.4128 0.4297 0.3360 -0.0725 0.0518  0.0968  117 MET B N   
5066 C CA  . MET B 117 ? 0.4871 0.4875 0.4023 -0.0613 0.0504  0.1083  117 MET B CA  
5067 C C   . MET B 117 ? 0.6290 0.6122 0.5321 -0.0648 0.0586  0.1264  117 MET B C   
5068 O O   . MET B 117 ? 0.6131 0.5857 0.5087 -0.0539 0.0581  0.1386  117 MET B O   
5069 C CB  . MET B 117 ? 0.4503 0.4265 0.3706 -0.0558 0.0473  0.1036  117 MET B CB  
5070 C CG  . MET B 117 ? 0.4361 0.4269 0.3667 -0.0501 0.0388  0.0881  117 MET B CG  
5071 S SD  . MET B 117 ? 0.4811 0.4970 0.4087 -0.0369 0.0312  0.0883  117 MET B SD  
5072 C CE  . MET B 117 ? 0.5100 0.5577 0.4407 -0.0427 0.0307  0.0770  117 MET B CE  
5073 N N   . ASN B 118 ? 0.6041 0.5857 0.5053 -0.0794 0.0664  0.1292  118 ASN B N   
5074 C CA  . ASN B 118 ? 0.6665 0.6292 0.5555 -0.0845 0.0754  0.1470  118 ASN B CA  
5075 C C   . ASN B 118 ? 0.6263 0.6154 0.5073 -0.0863 0.0781  0.1560  118 ASN B C   
5076 O O   . ASN B 118 ? 0.6994 0.6748 0.5693 -0.0911 0.0862  0.1722  118 ASN B O   
5077 C CB  . ASN B 118 ? 0.7274 0.6667 0.6177 -0.1021 0.0837  0.1456  118 ASN B CB  
5078 C CG  . ASN B 118 ? 0.7862 0.6863 0.6761 -0.0998 0.0850  0.1448  118 ASN B CG  
5079 O OD1 . ASN B 118 ? 0.9089 0.7976 0.7968 -0.0839 0.0811  0.1488  118 ASN B OD1 
5080 N ND2 . ASN B 118 ? 0.7990 0.6798 0.6909 -0.1159 0.0907  0.1390  118 ASN B ND2 
5081 N N   . LYS B 119 ? 0.6434 0.6684 0.5283 -0.0826 0.0725  0.1465  119 LYS B N   
5082 C CA  . LYS B 119 ? 0.6923 0.7441 0.5689 -0.0850 0.0757  0.1533  119 LYS B CA  
5083 C C   . LYS B 119 ? 0.6735 0.7447 0.5430 -0.0704 0.0689  0.1559  119 LYS B C   
5084 O O   . LYS B 119 ? 0.6369 0.7135 0.5125 -0.0608 0.0604  0.1450  119 LYS B O   
5085 C CB  . LYS B 119 ? 0.6597 0.7403 0.5451 -0.0951 0.0773  0.1399  119 LYS B CB  
5086 C CG  . LYS B 119 ? 0.6768 0.7678 0.5763 -0.0912 0.0701  0.1204  119 LYS B CG  
5087 C CD  . LYS B 119 ? 0.6564 0.7725 0.5654 -0.1016 0.0734  0.1099  119 LYS B CD  
5088 C CE  . LYS B 119 ? 0.7117 0.8132 0.6243 -0.1185 0.0808  0.1138  119 LYS B CE  
5089 N NZ  . LYS B 119 ? 0.6478 0.7802 0.5699 -0.1289 0.0844  0.1055  119 LYS B NZ  
5090 N N   . GLU B 120 ? 0.7734 0.8565 0.6294 -0.0699 0.0727  0.1703  120 GLU B N   
5091 C CA  . GLU B 120 ? 0.8164 0.9173 0.6632 -0.0569 0.0664  0.1754  120 GLU B CA  
5092 C C   . GLU B 120 ? 0.6758 0.8101 0.5262 -0.0543 0.0601  0.1576  120 GLU B C   
5093 O O   . GLU B 120 ? 0.7116 0.8548 0.5617 -0.0442 0.0517  0.1520  120 GLU B O   
5094 C CB  . GLU B 120 ? 0.9170 1.0228 0.7472 -0.0574 0.0724  0.1965  120 GLU B CB  
5095 C CG  . GLU B 120 ? 0.9982 1.0656 0.8231 -0.0572 0.0788  0.2144  120 GLU B CG  
5096 C CD  . GLU B 120 ? 1.1551 1.2217 0.9660 -0.0519 0.0810  0.2289  120 GLU B CD  
5097 O OE1 . GLU B 120 ? 1.1711 1.2632 0.9765 -0.0563 0.0825  0.2273  120 GLU B OE1 
5098 O OE2 . GLU B 120 ? 1.2244 1.2653 1.0299 -0.0429 0.0811  0.2416  120 GLU B OE2 
5099 N N   . LYS B 121 ? 0.5840 0.7371 0.4375 -0.0634 0.0646  0.1484  121 LYS B N   
5100 C CA  . LYS B 121 ? 0.5832 0.7655 0.4391 -0.0604 0.0605  0.1312  121 LYS B CA  
5101 C C   . LYS B 121 ? 0.5772 0.7616 0.4486 -0.0662 0.0618  0.1148  121 LYS B C   
5102 O O   . LYS B 121 ? 0.6129 0.7911 0.4899 -0.0767 0.0685  0.1179  121 LYS B O   
5103 C CB  . LYS B 121 ? 0.5010 0.7125 0.3434 -0.0626 0.0650  0.1358  121 LYS B CB  
5104 C CG  . LYS B 121 ? 0.7233 0.9351 0.5492 -0.0583 0.0650  0.1555  121 LYS B CG  
5105 C CD  . LYS B 121 ? 0.8001 1.0207 0.6209 -0.0466 0.0549  0.1520  121 LYS B CD  
5106 C CE  . LYS B 121 ? 0.8093 1.0234 0.6204 -0.0398 0.0528  0.1692  121 LYS B CE  
5107 N NZ  . LYS B 121 ? 0.7888 1.0297 0.5899 -0.0381 0.0511  0.1666  121 LYS B NZ  
5108 N N   . LEU B 122 ? 0.4964 0.6909 0.3742 -0.0595 0.0556  0.0977  122 LEU B N   
5109 C CA  . LEU B 122 ? 0.4441 0.6422 0.3367 -0.0616 0.0556  0.0821  122 LEU B CA  
5110 C C   . LEU B 122 ? 0.4176 0.6456 0.3085 -0.0596 0.0579  0.0703  122 LEU B C   
5111 O O   . LEU B 122 ? 0.4864 0.7252 0.3684 -0.0525 0.0543  0.0647  122 LEU B O   
5112 C CB  . LEU B 122 ? 0.3743 0.5556 0.2758 -0.0543 0.0474  0.0723  122 LEU B CB  
5113 C CG  . LEU B 122 ? 0.4643 0.6157 0.3678 -0.0538 0.0448  0.0815  122 LEU B CG  
5114 C CD1 . LEU B 122 ? 0.5058 0.6458 0.4183 -0.0470 0.0373  0.0702  122 LEU B CD1 
5115 C CD2 . LEU B 122 ? 0.5256 0.6626 0.4342 -0.0648 0.0513  0.0879  122 LEU B CD2 
5116 N N   . ASN B 123 ? 0.3760 0.6181 0.2752 -0.0660 0.0642  0.0660  123 ASN B N   
5117 C CA  . ASN B 123 ? 0.3421 0.6125 0.2413 -0.0627 0.0677  0.0540  123 ASN B CA  
5118 C C   . ASN B 123 ? 0.3640 0.6323 0.2750 -0.0543 0.0628  0.0369  123 ASN B C   
5119 O O   . ASN B 123 ? 0.3618 0.6081 0.2794 -0.0517 0.0563  0.0349  123 ASN B O   
5120 C CB  . ASN B 123 ? 0.3661 0.6571 0.2690 -0.0726 0.0773  0.0586  123 ASN B CB  
5121 C CG  . ASN B 123 ? 0.3977 0.6839 0.3181 -0.0799 0.0786  0.0566  123 ASN B CG  
5122 O OD1 . ASN B 123 ? 0.3650 0.6394 0.2961 -0.0751 0.0728  0.0477  123 ASN B OD1 
5123 N ND2 . ASN B 123 ? 0.4179 0.7154 0.3408 -0.0926 0.0865  0.0650  123 ASN B ND2 
5124 N N   . ARG B 124 ? 0.4360 0.7265 0.3491 -0.0495 0.0665  0.0249  124 ARG B N   
5125 C CA  . ARG B 124 ? 0.4193 0.7060 0.3409 -0.0397 0.0626  0.0093  124 ARG B CA  
5126 C C   . ARG B 124 ? 0.3318 0.6089 0.2708 -0.0418 0.0605  0.0085  124 ARG B C   
5127 O O   . ARG B 124 ? 0.3079 0.5668 0.2523 -0.0362 0.0540  0.0025  124 ARG B O   
5128 C CB  . ARG B 124 ? 0.3794 0.6911 0.2997 -0.0330 0.0688  -0.0026 124 ARG B CB  
5129 C CG  . ARG B 124 ? 0.4415 0.7480 0.3715 -0.0222 0.0665  -0.0174 124 ARG B CG  
5130 C CD  . ARG B 124 ? 0.3958 0.7234 0.3231 -0.0133 0.0736  -0.0297 124 ARG B CD  
5131 N NE  . ARG B 124 ? 0.3736 0.6914 0.3087 -0.0016 0.0716  -0.0427 124 ARG B NE  
5132 C CZ  . ARG B 124 ? 0.3616 0.6834 0.3139 0.0022  0.0720  -0.0439 124 ARG B CZ  
5133 N NH1 . ARG B 124 ? 0.3779 0.7141 0.3414 -0.0065 0.0738  -0.0342 124 ARG B NH1 
5134 N NH2 . ARG B 124 ? 0.4485 0.7599 0.4061 0.0140  0.0704  -0.0544 124 ARG B NH2 
5135 N N   . GLU B 125 ? 0.3071 0.5972 0.2545 -0.0508 0.0660  0.0144  125 GLU B N   
5136 C CA  . GLU B 125 ? 0.3030 0.5889 0.2666 -0.0542 0.0641  0.0128  125 GLU B CA  
5137 C C   . GLU B 125 ? 0.2937 0.5486 0.2569 -0.0593 0.0582  0.0198  125 GLU B C   
5138 O O   . GLU B 125 ? 0.2945 0.5371 0.2672 -0.0572 0.0532  0.0149  125 GLU B O   
5139 C CB  . GLU B 125 ? 0.3693 0.6802 0.3412 -0.0650 0.0716  0.0174  125 GLU B CB  
5140 C CG  . GLU B 125 ? 0.4537 0.7991 0.4289 -0.0586 0.0782  0.0099  125 GLU B CG  
5141 C CD  . GLU B 125 ? 0.6221 0.9754 0.5807 -0.0535 0.0821  0.0093  125 GLU B CD  
5142 O OE1 . GLU B 125 ? 0.6487 1.0051 0.6038 -0.0404 0.0814  -0.0023 125 GLU B OE1 
5143 O OE2 . GLU B 125 ? 0.5248 0.8804 0.4728 -0.0628 0.0860  0.0205  125 GLU B OE2 
5144 N N   . GLU B 126 ? 0.2795 0.5213 0.2309 -0.0649 0.0591  0.0315  126 GLU B N   
5145 C CA  . GLU B 126 ? 0.3103 0.5215 0.2603 -0.0675 0.0544  0.0383  126 GLU B CA  
5146 C C   . GLU B 126 ? 0.3125 0.5090 0.2613 -0.0559 0.0463  0.0310  126 GLU B C   
5147 O O   . GLU B 126 ? 0.3157 0.4925 0.2706 -0.0552 0.0416  0.0296  126 GLU B O   
5148 C CB  . GLU B 126 ? 0.3128 0.5141 0.2499 -0.0738 0.0580  0.0538  126 GLU B CB  
5149 C CG  . GLU B 126 ? 0.3951 0.5973 0.3347 -0.0888 0.0656  0.0627  126 GLU B CG  
5150 C CD  . GLU B 126 ? 0.4475 0.6553 0.3739 -0.0947 0.0723  0.0765  126 GLU B CD  
5151 O OE1 . GLU B 126 ? 0.4556 0.6667 0.3698 -0.0866 0.0707  0.0802  126 GLU B OE1 
5152 O OE2 . GLU B 126 ? 0.5152 0.7250 0.4429 -0.1083 0.0795  0.0840  126 GLU B OE2 
5153 N N   . LEU B 127 ? 0.2863 0.4930 0.2271 -0.0476 0.0450  0.0255  127 LEU B N   
5154 C CA  . LEU B 127 ? 0.3141 0.5078 0.2533 -0.0385 0.0377  0.0183  127 LEU B CA  
5155 C C   . LEU B 127 ? 0.3093 0.5011 0.2608 -0.0332 0.0350  0.0060  127 LEU B C   
5156 O O   . LEU B 127 ? 0.3142 0.4881 0.2691 -0.0295 0.0291  0.0031  127 LEU B O   
5157 C CB  . LEU B 127 ? 0.2899 0.4955 0.2160 -0.0332 0.0373  0.0143  127 LEU B CB  
5158 C CG  . LEU B 127 ? 0.3435 0.5486 0.2560 -0.0358 0.0370  0.0271  127 LEU B CG  
5159 C CD1 . LEU B 127 ? 0.3362 0.5588 0.2354 -0.0320 0.0372  0.0214  127 LEU B CD1 
5160 C CD2 . LEU B 127 ? 0.3496 0.5325 0.2623 -0.0337 0.0304  0.0333  127 LEU B CD2 
5161 N N   . LEU B 128 ? 0.2937 0.5053 0.2520 -0.0322 0.0397  -0.0004 128 LEU B N   
5162 C CA  . LEU B 128 ? 0.2857 0.4978 0.2564 -0.0264 0.0378  -0.0098 128 LEU B CA  
5163 C C   . LEU B 128 ? 0.2716 0.4696 0.2518 -0.0322 0.0344  -0.0055 128 LEU B C   
5164 O O   . LEU B 128 ? 0.2780 0.4642 0.2641 -0.0269 0.0295  -0.0109 128 LEU B O   
5165 C CB  . LEU B 128 ? 0.3302 0.5699 0.3077 -0.0243 0.0443  -0.0147 128 LEU B CB  
5166 C CG  . LEU B 128 ? 0.3567 0.6042 0.3314 -0.0116 0.0460  -0.0268 128 LEU B CG  
5167 C CD1 . LEU B 128 ? 0.3182 0.5957 0.2997 -0.0091 0.0537  -0.0298 128 LEU B CD1 
5168 C CD2 . LEU B 128 ? 0.3751 0.6050 0.3553 -0.0025 0.0405  -0.0346 128 LEU B CD2 
5169 N N   . ASP B 129 ? 0.2686 0.4670 0.2497 -0.0437 0.0376  0.0039  129 ASP B N   
5170 C CA  . ASP B 129 ? 0.2890 0.4716 0.2769 -0.0506 0.0349  0.0069  129 ASP B CA  
5171 C C   . ASP B 129 ? 0.2869 0.4412 0.2690 -0.0474 0.0295  0.0095  129 ASP B C   
5172 O O   . ASP B 129 ? 0.2680 0.4087 0.2559 -0.0465 0.0253  0.0065  129 ASP B O   
5173 C CB  . ASP B 129 ? 0.2392 0.4252 0.2273 -0.0652 0.0406  0.0158  129 ASP B CB  
5174 C CG  . ASP B 129 ? 0.3785 0.5945 0.3767 -0.0703 0.0452  0.0126  129 ASP B CG  
5175 O OD1 . ASP B 129 ? 0.3752 0.6092 0.3805 -0.0606 0.0441  0.0039  129 ASP B OD1 
5176 O OD2 . ASP B 129 ? 0.3557 0.5778 0.3547 -0.0840 0.0504  0.0192  129 ASP B OD2 
5177 N N   . LEU B 130 ? 0.2643 0.4121 0.2350 -0.0453 0.0294  0.0153  130 LEU B N   
5178 C CA  . LEU B 130 ? 0.3090 0.4344 0.2750 -0.0411 0.0243  0.0183  130 LEU B CA  
5179 C C   . LEU B 130 ? 0.3225 0.4444 0.2922 -0.0318 0.0184  0.0079  130 LEU B C   
5180 O O   . LEU B 130 ? 0.2717 0.3764 0.2445 -0.0300 0.0142  0.0074  130 LEU B O   
5181 C CB  . LEU B 130 ? 0.3024 0.4277 0.2557 -0.0397 0.0250  0.0271  130 LEU B CB  
5182 C CG  . LEU B 130 ? 0.3381 0.4429 0.2872 -0.0358 0.0207  0.0334  130 LEU B CG  
5183 C CD1 . LEU B 130 ? 0.3207 0.4044 0.2742 -0.0413 0.0223  0.0391  130 LEU B CD1 
5184 C CD2 . LEU B 130 ? 0.3383 0.4474 0.2751 -0.0340 0.0213  0.0439  130 LEU B CD2 
5185 N N   . GLN B 131 ? 0.2361 0.3730 0.2049 -0.0260 0.0188  -0.0006 131 GLN B N   
5186 C CA  . GLN B 131 ? 0.2662 0.3968 0.2376 -0.0180 0.0143  -0.0104 131 GLN B CA  
5187 C C   . GLN B 131 ? 0.2896 0.4158 0.2726 -0.0172 0.0127  -0.0143 131 GLN B C   
5188 O O   . GLN B 131 ? 0.2804 0.3917 0.2660 -0.0139 0.0081  -0.0168 131 GLN B O   
5189 C CB  . GLN B 131 ? 0.2939 0.4386 0.2608 -0.0120 0.0166  -0.0195 131 GLN B CB  
5190 C CG  . GLN B 131 ? 0.2793 0.4301 0.2328 -0.0123 0.0172  -0.0183 131 GLN B CG  
5191 C CD  . GLN B 131 ? 0.2952 0.4619 0.2441 -0.0078 0.0217  -0.0279 131 GLN B CD  
5192 O OE1 . GLN B 131 ? 0.2372 0.4172 0.1926 -0.0065 0.0267  -0.0303 131 GLN B OE1 
5193 N NE2 . GLN B 131 ? 0.2522 0.4187 0.1897 -0.0055 0.0203  -0.0339 131 GLN B NE2 
5194 N N   . THR B 132 ? 0.1992 0.3409 0.1894 -0.0204 0.0166  -0.0146 132 THR B N   
5195 C CA  . THR B 132 ? 0.2331 0.3772 0.2345 -0.0188 0.0149  -0.0187 132 THR B CA  
5196 C C   . THR B 132 ? 0.2865 0.4147 0.2907 -0.0258 0.0120  -0.0141 132 THR B C   
5197 O O   . THR B 132 ? 0.2721 0.3919 0.2812 -0.0225 0.0080  -0.0176 132 THR B O   
5198 C CB  . THR B 132 ? 0.2213 0.3917 0.2301 -0.0206 0.0198  -0.0198 132 THR B CB  
5199 O OG1 . THR B 132 ? 0.2370 0.4210 0.2415 -0.0135 0.0236  -0.0243 132 THR B OG1 
5200 C CG2 . THR B 132 ? 0.2054 0.3836 0.2259 -0.0167 0.0176  -0.0241 132 THR B CG2 
5201 N N   . LEU B 133 ? 0.2239 0.3463 0.2241 -0.0353 0.0146  -0.0063 133 LEU B N   
5202 C CA  . LEU B 133 ? 0.2338 0.3383 0.2353 -0.0421 0.0132  -0.0030 133 LEU B CA  
5203 C C   . LEU B 133 ? 0.2556 0.3381 0.2528 -0.0361 0.0087  -0.0026 133 LEU B C   
5204 O O   . LEU B 133 ? 0.2529 0.3225 0.2530 -0.0372 0.0062  -0.0039 133 LEU B O   
5205 C CB  . LEU B 133 ? 0.2219 0.3222 0.2190 -0.0537 0.0184  0.0054  133 LEU B CB  
5206 C CG  . LEU B 133 ? 0.3370 0.4591 0.3406 -0.0633 0.0228  0.0048  133 LEU B CG  
5207 C CD1 . LEU B 133 ? 0.4024 0.5220 0.3993 -0.0740 0.0292  0.0139  133 LEU B CD1 
5208 C CD2 . LEU B 133 ? 0.2472 0.3696 0.2592 -0.0699 0.0207  0.0002  133 LEU B CD2 
5209 N N   . ASN B 134 ? 0.2559 0.3361 0.2461 -0.0301 0.0077  -0.0010 134 ASN B N   
5210 C CA  . ASN B 134 ? 0.2554 0.3205 0.2433 -0.0241 0.0030  -0.0017 134 ASN B CA  
5211 C C   . ASN B 134 ? 0.2666 0.3311 0.2608 -0.0187 -0.0008 -0.0102 134 ASN B C   
5212 O O   . ASN B 134 ? 0.2924 0.3433 0.2885 -0.0175 -0.0038 -0.0106 134 ASN B O   
5213 C CB  . ASN B 134 ? 0.2433 0.3120 0.2230 -0.0198 0.0021  0.0003  134 ASN B CB  
5214 C CG  . ASN B 134 ? 0.2754 0.3344 0.2485 -0.0216 0.0032  0.0112  134 ASN B CG  
5215 O OD1 . ASN B 134 ? 0.2506 0.2956 0.2237 -0.0188 0.0006  0.0141  134 ASN B OD1 
5216 N ND2 . ASN B 134 ? 0.3139 0.3805 0.2814 -0.0257 0.0076  0.0180  134 ASN B ND2 
5217 N N   . LEU B 135 ? 0.2236 0.3025 0.2209 -0.0148 -0.0001 -0.0165 135 LEU B N   
5218 C CA  . LEU B 135 ? 0.2523 0.3300 0.2555 -0.0089 -0.0028 -0.0229 135 LEU B CA  
5219 C C   . LEU B 135 ? 0.1906 0.2677 0.2008 -0.0133 -0.0037 -0.0220 135 LEU B C   
5220 O O   . LEU B 135 ? 0.2436 0.3097 0.2556 -0.0113 -0.0072 -0.0234 135 LEU B O   
5221 C CB  . LEU B 135 ? 0.2758 0.3691 0.2810 -0.0026 -0.0005 -0.0289 135 LEU B CB  
5222 C CG  . LEU B 135 ? 0.2635 0.3559 0.2611 0.0031  0.0003  -0.0337 135 LEU B CG  
5223 C CD1 . LEU B 135 ? 0.2567 0.3643 0.2574 0.0101  0.0043  -0.0397 135 LEU B CD1 
5224 C CD2 . LEU B 135 ? 0.2179 0.2927 0.2128 0.0068  -0.0038 -0.0369 135 LEU B CD2 
5225 N N   . LEU B 136 ? 0.1812 0.2717 0.1951 -0.0204 -0.0006 -0.0200 136 LEU B N   
5226 C CA  . LEU B 136 ? 0.1778 0.2722 0.1982 -0.0260 -0.0016 -0.0207 136 LEU B CA  
5227 C C   . LEU B 136 ? 0.2366 0.3096 0.2534 -0.0317 -0.0030 -0.0182 136 LEU B C   
5228 O O   . LEU B 136 ? 0.1783 0.2493 0.1985 -0.0338 -0.0054 -0.0206 136 LEU B O   
5229 C CB  . LEU B 136 ? 0.2234 0.3384 0.2483 -0.0346 0.0025  -0.0193 136 LEU B CB  
5230 C CG  . LEU B 136 ? 0.2170 0.3576 0.2483 -0.0274 0.0039  -0.0227 136 LEU B CG  
5231 C CD1 . LEU B 136 ? 0.1738 0.3387 0.2101 -0.0365 0.0085  -0.0208 136 LEU B CD1 
5232 C CD2 . LEU B 136 ? 0.2403 0.3870 0.2787 -0.0197 -0.0001 -0.0267 136 LEU B CD2 
5233 N N   . ALA B 137 ? 0.2196 0.2771 0.2292 -0.0332 -0.0014 -0.0132 137 ALA B N   
5234 C CA  . ALA B 137 ? 0.2878 0.3237 0.2936 -0.0368 -0.0015 -0.0105 137 ALA B CA  
5235 C C   . ALA B 137 ? 0.2111 0.2378 0.2182 -0.0300 -0.0060 -0.0141 137 ALA B C   
5236 O O   . ALA B 137 ? 0.2225 0.2365 0.2288 -0.0331 -0.0064 -0.0147 137 ALA B O   
5237 C CB  . ALA B 137 ? 0.2676 0.2907 0.2658 -0.0364 0.0010  -0.0031 137 ALA B CB  
5238 N N   . TRP B 138 ? 0.2333 0.2656 0.2416 -0.0214 -0.0089 -0.0169 138 TRP B N   
5239 C CA  . TRP B 138 ? 0.2335 0.2574 0.2426 -0.0153 -0.0127 -0.0196 138 TRP B CA  
5240 C C   . TRP B 138 ? 0.2256 0.2594 0.2403 -0.0126 -0.0148 -0.0242 138 TRP B C   
5241 O O   . TRP B 138 ? 0.2134 0.2423 0.2285 -0.0065 -0.0175 -0.0263 138 TRP B O   
5242 C CB  . TRP B 138 ? 0.2082 0.2293 0.2138 -0.0089 -0.0141 -0.0198 138 TRP B CB  
5243 C CG  . TRP B 138 ? 0.2375 0.2510 0.2379 -0.0101 -0.0130 -0.0140 138 TRP B CG  
5244 C CD1 . TRP B 138 ? 0.2066 0.2253 0.2031 -0.0124 -0.0102 -0.0096 138 TRP B CD1 
5245 C CD2 . TRP B 138 ? 0.2442 0.2453 0.2429 -0.0081 -0.0143 -0.0109 138 TRP B CD2 
5246 N NE1 . TRP B 138 ? 0.2371 0.2469 0.2293 -0.0114 -0.0100 -0.0032 138 TRP B NE1 
5247 C CE2 . TRP B 138 ? 0.2517 0.2514 0.2457 -0.0083 -0.0125 -0.0041 138 TRP B CE2 
5248 C CE3 . TRP B 138 ? 0.2781 0.2707 0.2787 -0.0056 -0.0166 -0.0126 138 TRP B CE3 
5249 C CZ2 . TRP B 138 ? 0.2438 0.2350 0.2360 -0.0050 -0.0129 0.0010  138 TRP B CZ2 
5250 C CZ3 . TRP B 138 ? 0.3287 0.3130 0.3275 -0.0033 -0.0166 -0.0083 138 TRP B CZ3 
5251 C CH2 . TRP B 138 ? 0.3167 0.3007 0.3118 -0.0025 -0.0149 -0.0014 138 TRP B CH2 
5252 N N   . CYS B 139 ? 0.1943 0.2431 0.2134 -0.0171 -0.0136 -0.0251 139 CYS B N   
5253 C CA  . CYS B 139 ? 0.1522 0.2142 0.1772 -0.0135 -0.0159 -0.0280 139 CYS B CA  
5254 C C   . CYS B 139 ? 0.2137 0.2658 0.2378 -0.0147 -0.0189 -0.0288 139 CYS B C   
5255 O O   . CYS B 139 ? 0.2160 0.2592 0.2373 -0.0229 -0.0181 -0.0284 139 CYS B O   
5256 C CB  . CYS B 139 ? 0.1771 0.2613 0.2078 -0.0194 -0.0142 -0.0284 139 CYS B CB  
5257 S SG  . CYS B 139 ? 0.2619 0.3695 0.3012 -0.0115 -0.0168 -0.0304 139 CYS B SG  
5258 N N   . GLY B 140 ? 0.1889 0.2413 0.2145 -0.0065 -0.0217 -0.0298 140 GLY B N   
5259 C CA  . GLY B 140 ? 0.1475 0.1939 0.1718 -0.0074 -0.0244 -0.0302 140 GLY B CA  
5260 C C   . GLY B 140 ? 0.2190 0.2845 0.2476 -0.0111 -0.0263 -0.0313 140 GLY B C   
5261 O O   . GLY B 140 ? 0.2003 0.2860 0.2344 -0.0124 -0.0256 -0.0315 140 GLY B O   
5262 N N   . ARG B 141 ? 0.1582 0.2194 0.1841 -0.0133 -0.0286 -0.0321 141 ARG B N   
5263 C CA  . ARG B 141 ? 0.1520 0.2321 0.1804 -0.0188 -0.0311 -0.0336 141 ARG B CA  
5264 C C   . ARG B 141 ? 0.1489 0.2539 0.1848 -0.0103 -0.0333 -0.0316 141 ARG B C   
5265 O O   . ARG B 141 ? 0.1508 0.2801 0.1920 -0.0156 -0.0341 -0.0324 141 ARG B O   
5266 C CB  . ARG B 141 ? 0.1549 0.2254 0.1775 -0.0204 -0.0332 -0.0348 141 ARG B CB  
5267 C CG  . ARG B 141 ? 0.1776 0.2688 0.2010 -0.0254 -0.0367 -0.0365 141 ARG B CG  
5268 C CD  . ARG B 141 ? 0.1691 0.2476 0.1844 -0.0282 -0.0377 -0.0385 141 ARG B CD  
5269 N NE  . ARG B 141 ? 0.1764 0.2770 0.1912 -0.0318 -0.0418 -0.0398 141 ARG B NE  
5270 C CZ  . ARG B 141 ? 0.2047 0.3168 0.2203 -0.0221 -0.0456 -0.0354 141 ARG B CZ  
5271 N NH1 . ARG B 141 ? 0.1924 0.2927 0.2088 -0.0093 -0.0451 -0.0301 141 ARG B NH1 
5272 N NH2 . ARG B 141 ? 0.3070 0.4421 0.3217 -0.0259 -0.0496 -0.0361 141 ARG B NH2 
5273 N N   . THR B 142 ? 0.1765 0.2757 0.2126 0.0028  -0.0339 -0.0288 142 THR B N   
5274 C CA  . THR B 142 ? 0.1751 0.2951 0.2175 0.0136  -0.0354 -0.0259 142 THR B CA  
5275 C C   . THR B 142 ? 0.2265 0.3652 0.2759 0.0148  -0.0327 -0.0264 142 THR B C   
5276 O O   . THR B 142 ? 0.2261 0.3935 0.2830 0.0168  -0.0340 -0.0250 142 THR B O   
5277 C CB  . THR B 142 ? 0.2408 0.3441 0.2803 0.0270  -0.0351 -0.0229 142 THR B CB  
5278 O OG1 . THR B 142 ? 0.2340 0.3246 0.2676 0.0259  -0.0375 -0.0215 142 THR B OG1 
5279 C CG2 . THR B 142 ? 0.2879 0.4088 0.3333 0.0407  -0.0352 -0.0192 142 THR B CG2 
5280 N N   . LEU B 143 ? 0.2365 0.3619 0.2838 0.0139  -0.0289 -0.0281 143 LEU B N   
5281 C CA  . LEU B 143 ? 0.2473 0.3903 0.3003 0.0158  -0.0256 -0.0286 143 LEU B CA  
5282 C C   . LEU B 143 ? 0.2197 0.3782 0.2756 0.0011  -0.0245 -0.0299 143 LEU B C   
5283 O O   . LEU B 143 ? 0.2504 0.4296 0.3122 0.0011  -0.0217 -0.0298 143 LEU B O   
5284 C CB  . LEU B 143 ? 0.2372 0.3618 0.2854 0.0208  -0.0219 -0.0300 143 LEU B CB  
5285 C CG  . LEU B 143 ? 0.1595 0.2736 0.2060 0.0358  -0.0210 -0.0299 143 LEU B CG  
5286 C CD1 . LEU B 143 ? 0.1849 0.2837 0.2256 0.0370  -0.0172 -0.0331 143 LEU B CD1 
5287 C CD2 . LEU B 143 ? 0.2896 0.4267 0.3437 0.0474  -0.0202 -0.0281 143 LEU B CD2 
5288 N N   . ARG B 144 ? 0.2445 0.3937 0.2961 -0.0115 -0.0259 -0.0311 144 ARG B N   
5289 C CA  . ARG B 144 ? 0.3472 0.5071 0.4002 -0.0270 -0.0240 -0.0326 144 ARG B CA  
5290 C C   . ARG B 144 ? 0.4207 0.6175 0.4831 -0.0304 -0.0258 -0.0328 144 ARG B C   
5291 O O   . ARG B 144 ? 0.4095 0.6221 0.4756 -0.0419 -0.0231 -0.0337 144 ARG B O   
5292 C CB  . ARG B 144 ? 0.3472 0.4850 0.3921 -0.0390 -0.0243 -0.0348 144 ARG B CB  
5293 C CG  . ARG B 144 ? 0.3959 0.5077 0.4340 -0.0428 -0.0199 -0.0338 144 ARG B CG  
5294 C CD  . ARG B 144 ? 0.4703 0.5554 0.4999 -0.0484 -0.0197 -0.0351 144 ARG B CD  
5295 N NE  . ARG B 144 ? 0.4738 0.5348 0.4973 -0.0479 -0.0161 -0.0324 144 ARG B NE  
5296 C CZ  . ARG B 144 ? 0.4748 0.5241 0.4939 -0.0582 -0.0116 -0.0314 144 ARG B CZ  
5297 N NH1 . ARG B 144 ? 0.5228 0.5807 0.5425 -0.0717 -0.0100 -0.0340 144 ARG B NH1 
5298 N NH2 . ARG B 144 ? 0.4616 0.4906 0.4752 -0.0553 -0.0087 -0.0275 144 ARG B NH2 
5299 N N   . LYS B 145 ? 0.4255 0.6386 0.4924 -0.0205 -0.0299 -0.0313 145 LYS B N   
5300 C CA  . LYS B 145 ? 0.4156 0.6694 0.4932 -0.0208 -0.0316 -0.0302 145 LYS B CA  
5301 C C   . LYS B 145 ? 0.4243 0.6958 0.5100 -0.0066 -0.0284 -0.0275 145 LYS B C   
5302 O O   . LYS B 145 ? 0.3454 0.6471 0.4398 -0.0114 -0.0264 -0.0274 145 LYS B O   
5303 C CB  . LYS B 145 ? 0.6356 0.9039 0.7144 -0.0166 -0.0377 -0.0287 145 LYS B CB  
5304 C CG  . LYS B 145 ? 0.7871 1.0352 0.8559 -0.0287 -0.0403 -0.0323 145 LYS B CG  
5305 C CD  . LYS B 145 ? 0.6778 0.8971 0.7388 -0.0169 -0.0416 -0.0301 145 LYS B CD  
5306 C CE  . LYS B 145 ? 0.6656 0.8836 0.7200 -0.0238 -0.0459 -0.0320 145 LYS B CE  
5307 N NZ  . LYS B 145 ? 0.6381 0.8241 0.6835 -0.0168 -0.0460 -0.0308 145 LYS B NZ  
5308 N N   . ASP B 146 ? 0.3840 0.6364 0.4666 0.0101  -0.0271 -0.0258 146 ASP B N   
5309 C CA  . ASP B 146 ? 0.3658 0.6306 0.4542 0.0244  -0.0229 -0.0246 146 ASP B CA  
5310 C C   . ASP B 146 ? 0.4232 0.6908 0.5118 0.0160  -0.0174 -0.0269 146 ASP B C   
5311 O O   . ASP B 146 ? 0.4155 0.7092 0.5120 0.0215  -0.0138 -0.0263 146 ASP B O   
5312 C CB  . ASP B 146 ? 0.4640 0.6999 0.5458 0.0405  -0.0216 -0.0240 146 ASP B CB  
5313 C CG  . ASP B 146 ? 0.5941 0.8438 0.6814 0.0592  -0.0224 -0.0197 146 ASP B CG  
5314 O OD1 . ASP B 146 ? 0.5988 0.8806 0.6945 0.0598  -0.0258 -0.0164 146 ASP B OD1 
5315 O OD2 . ASP B 146 ? 0.6181 0.8463 0.7007 0.0733  -0.0195 -0.0196 146 ASP B OD2 
5316 N N   . LEU B 147 ? 0.3125 0.5543 0.3923 0.0037  -0.0164 -0.0288 147 LEU B N   
5317 C CA  . LEU B 147 ? 0.2160 0.4562 0.2937 -0.0036 -0.0111 -0.0296 147 LEU B CA  
5318 C C   . LEU B 147 ? 0.2020 0.4538 0.2813 -0.0236 -0.0103 -0.0296 147 LEU B C   
5319 O O   . LEU B 147 ? 0.3203 0.5634 0.3951 -0.0324 -0.0060 -0.0291 147 LEU B O   
5320 C CB  . LEU B 147 ? 0.2668 0.4706 0.3329 -0.0020 -0.0098 -0.0305 147 LEU B CB  
5321 C CG  . LEU B 147 ? 0.2528 0.4406 0.3153 0.0147  -0.0099 -0.0317 147 LEU B CG  
5322 C CD1 . LEU B 147 ? 0.2662 0.4223 0.3179 0.0130  -0.0094 -0.0327 147 LEU B CD1 
5323 C CD2 . LEU B 147 ? 0.4232 0.6299 0.4905 0.0263  -0.0053 -0.0328 147 LEU B CD2 
5324 N N   . LYS B 148 ? 0.2439 0.5156 0.3289 -0.0315 -0.0140 -0.0300 148 LYS B N   
5325 C CA  . LYS B 148 ? 0.2634 0.5416 0.3482 -0.0529 -0.0129 -0.0312 148 LYS B CA  
5326 C C   . LYS B 148 ? 0.2539 0.5554 0.3445 -0.0597 -0.0072 -0.0299 148 LYS B C   
5327 O O   . LYS B 148 ? 0.1980 0.4893 0.2837 -0.0757 -0.0034 -0.0297 148 LYS B O   
5328 C CB  . LYS B 148 ? 0.1850 0.4852 0.2748 -0.0607 -0.0182 -0.0331 148 LYS B CB  
5329 C CG  . LYS B 148 ? 0.1867 0.5016 0.2780 -0.0844 -0.0166 -0.0356 148 LYS B CG  
5330 C CD  . LYS B 148 ? 0.2949 0.6346 0.3904 -0.0922 -0.0227 -0.0385 148 LYS B CD  
5331 C CE  . LYS B 148 ? 0.4579 0.7807 0.5444 -0.1160 -0.0219 -0.0437 148 LYS B CE  
5332 N NZ  . LYS B 148 ? 0.5627 0.8675 0.6446 -0.1305 -0.0146 -0.0436 148 LYS B NZ  
5333 N N   . ASP B 149 ? 0.2341 0.5660 0.3346 -0.0471 -0.0058 -0.0286 149 ASP B N   
5334 C CA  . ASP B 149 ? 0.2771 0.6330 0.3831 -0.0524 0.0004  -0.0273 149 ASP B CA  
5335 C C   . ASP B 149 ? 0.2803 0.6072 0.3753 -0.0542 0.0057  -0.0262 149 ASP B C   
5336 O O   . ASP B 149 ? 0.3278 0.6562 0.4205 -0.0696 0.0103  -0.0245 149 ASP B O   
5337 C CB  . ASP B 149 ? 0.3276 0.7179 0.4450 -0.0345 0.0019  -0.0263 149 ASP B CB  
5338 C CG  . ASP B 149 ? 0.6094 1.0385 0.7397 -0.0339 -0.0029 -0.0256 149 ASP B CG  
5339 O OD1 . ASP B 149 ? 0.7474 1.1833 0.8776 -0.0527 -0.0056 -0.0266 149 ASP B OD1 
5340 O OD2 . ASP B 149 ? 0.6514 1.0995 0.7890 -0.0144 -0.0034 -0.0239 149 ASP B OD2 
5341 N N   . LEU B 150 ? 0.2088 0.5096 0.2963 -0.0391 0.0052  -0.0268 150 LEU B N   
5342 C CA  . LEU B 150 ? 0.1673 0.4435 0.2440 -0.0401 0.0094  -0.0255 150 LEU B CA  
5343 C C   . LEU B 150 ? 0.1927 0.4403 0.2601 -0.0555 0.0089  -0.0236 150 LEU B C   
5344 O O   . LEU B 150 ? 0.2393 0.4799 0.3009 -0.0648 0.0136  -0.0204 150 LEU B O   
5345 C CB  . LEU B 150 ? 0.2381 0.4945 0.3089 -0.0223 0.0083  -0.0276 150 LEU B CB  
5346 C CG  . LEU B 150 ? 0.3092 0.5895 0.3862 -0.0074 0.0120  -0.0295 150 LEU B CG  
5347 C CD1 . LEU B 150 ? 0.2352 0.4936 0.3056 0.0095  0.0114  -0.0328 150 LEU B CD1 
5348 C CD2 . LEU B 150 ? 0.2937 0.5911 0.3701 -0.0134 0.0189  -0.0282 150 LEU B CD2 
5349 N N   . LEU B 151 ? 0.2056 0.4366 0.2710 -0.0579 0.0039  -0.0252 151 LEU B N   
5350 C CA  . LEU B 151 ? 0.2545 0.4560 0.3107 -0.0705 0.0042  -0.0239 151 LEU B CA  
5351 C C   . LEU B 151 ? 0.3512 0.5625 0.4083 -0.0901 0.0086  -0.0224 151 LEU B C   
5352 O O   . LEU B 151 ? 0.3861 0.5754 0.4345 -0.0990 0.0128  -0.0188 151 LEU B O   
5353 C CB  . LEU B 151 ? 0.2635 0.4509 0.3183 -0.0699 -0.0014 -0.0270 151 LEU B CB  
5354 C CG  . LEU B 151 ? 0.2953 0.4602 0.3450 -0.0547 -0.0046 -0.0273 151 LEU B CG  
5355 C CD1 . LEU B 151 ? 0.3185 0.4803 0.3693 -0.0523 -0.0101 -0.0301 151 LEU B CD1 
5356 C CD2 . LEU B 151 ? 0.2203 0.3533 0.2594 -0.0564 -0.0023 -0.0245 151 LEU B CD2 
5357 N N   . ASN B 152 ? 0.2727 0.5173 0.3402 -0.0973 0.0077  -0.0247 152 ASN B N   
5358 C CA  . ASN B 152 ? 0.2337 0.4901 0.3027 -0.1184 0.0120  -0.0240 152 ASN B CA  
5359 C C   . ASN B 152 ? 0.2788 0.5513 0.3495 -0.1209 0.0187  -0.0195 152 ASN B C   
5360 O O   . ASN B 152 ? 0.3400 0.6117 0.4082 -0.1391 0.0239  -0.0171 152 ASN B O   
5361 C CB  . ASN B 152 ? 0.3138 0.6063 0.3941 -0.1268 0.0084  -0.0280 152 ASN B CB  
5362 C CG  . ASN B 152 ? 0.4291 0.7077 0.5060 -0.1297 0.0025  -0.0327 152 ASN B CG  
5363 O OD1 . ASN B 152 ? 0.4932 0.7335 0.5592 -0.1275 0.0019  -0.0331 152 ASN B OD1 
5364 N ND2 . ASN B 152 ? 0.4493 0.7616 0.5355 -0.1343 -0.0019 -0.0360 152 ASN B ND2 
5365 N N   . LYS B 153 ? 0.3256 0.6135 0.4003 -0.1038 0.0193  -0.0187 153 LYS B N   
5366 C CA  . LYS B 153 ? 0.2882 0.5905 0.3628 -0.1053 0.0262  -0.0147 153 LYS B CA  
5367 C C   . LYS B 153 ? 0.3353 0.6040 0.3959 -0.1138 0.0306  -0.0093 153 LYS B C   
5368 O O   . LYS B 153 ? 0.3676 0.6434 0.4264 -0.1274 0.0369  -0.0048 153 LYS B O   
5369 C CB  . LYS B 153 ? 0.2479 0.5628 0.3251 -0.0838 0.0264  -0.0161 153 LYS B CB  
5370 C CG  . LYS B 153 ? 0.2318 0.5675 0.3093 -0.0840 0.0339  -0.0132 153 LYS B CG  
5371 C CD  . LYS B 153 ? 0.3234 0.6681 0.4018 -0.0624 0.0347  -0.0164 153 LYS B CD  
5372 C CE  . LYS B 153 ? 0.3392 0.7115 0.4193 -0.0624 0.0427  -0.0147 153 LYS B CE  
5373 N NZ  . LYS B 153 ? 0.4437 0.8280 0.5254 -0.0413 0.0445  -0.0195 153 LYS B NZ  
5374 N N   . GLY B 154 ? 0.2792 0.5122 0.3299 -0.1057 0.0276  -0.0089 154 GLY B N   
5375 C CA  . GLY B 154 ? 0.3241 0.5236 0.3619 -0.1124 0.0309  -0.0030 154 GLY B CA  
5376 C C   . GLY B 154 ? 0.3583 0.5567 0.3886 -0.1075 0.0356  0.0031  154 GLY B C   
5377 O O   . GLY B 154 ? 0.3477 0.5175 0.3666 -0.1079 0.0371  0.0089  154 GLY B O   
5378 N N   . ARG B 155 ? 0.3150 0.5444 0.3508 -0.1021 0.0383  0.0022  155 ARG B N   
5379 C CA  . ARG B 155 ? 0.2742 0.5061 0.3018 -0.0997 0.0436  0.0077  155 ARG B CA  
5380 C C   . ARG B 155 ? 0.3323 0.6009 0.3675 -0.0911 0.0461  0.0037  155 ARG B C   
5381 O O   . ARG B 155 ? 0.3461 0.6389 0.3938 -0.0876 0.0443  -0.0019 155 ARG B O   
5382 C CB  . ARG B 155 ? 0.3924 0.6174 0.4138 -0.1176 0.0503  0.0165  155 ARG B CB  
5383 C CG  . ARG B 155 ? 0.4541 0.7110 0.4857 -0.1321 0.0550  0.0160  155 ARG B CG  
5384 C CD  . ARG B 155 ? 0.5776 0.8239 0.6015 -0.1511 0.0626  0.0253  155 ARG B CD  
5385 N NE  . ARG B 155 ? 0.6139 0.8202 0.6297 -0.1597 0.0616  0.0279  155 ARG B NE  
5386 C CZ  . ARG B 155 ? 0.5361 0.7129 0.5389 -0.1669 0.0669  0.0377  155 ARG B CZ  
5387 N NH1 . ARG B 155 ? 0.5507 0.6902 0.5466 -0.1728 0.0665  0.0390  155 ARG B NH1 
5388 N NH2 . ARG B 155 ? 0.4980 0.6824 0.4938 -0.1675 0.0729  0.0465  155 ARG B NH2 
5389 N N   . ASN B 156 ? 0.2831 0.5572 0.3102 -0.0875 0.0509  0.0072  156 ASN B N   
5390 C CA  . ASN B 156 ? 0.3024 0.6095 0.3339 -0.0788 0.0552  0.0034  156 ASN B CA  
5391 C C   . ASN B 156 ? 0.2984 0.6112 0.3365 -0.0608 0.0507  -0.0061 156 ASN B C   
5392 O O   . ASN B 156 ? 0.3215 0.6641 0.3710 -0.0549 0.0526  -0.0104 156 ASN B O   
5393 C CB  . ASN B 156 ? 0.4129 0.7550 0.4551 -0.0911 0.0612  0.0055  156 ASN B CB  
5394 C CG  . ASN B 156 ? 0.4869 0.8197 0.5230 -0.1115 0.0660  0.0150  156 ASN B CG  
5395 O OD1 . ASN B 156 ? 0.7188 1.0546 0.7617 -0.1265 0.0661  0.0161  156 ASN B OD1 
5396 N ND2 . ASN B 156 ? 0.4725 0.7935 0.4948 -0.1125 0.0702  0.0220  156 ASN B ND2 
5397 N N   . TYR B 157 ? 0.2215 0.5053 0.2522 -0.0517 0.0452  -0.0086 157 TYR B N   
5398 C CA  . TYR B 157 ? 0.2386 0.5209 0.2726 -0.0350 0.0415  -0.0169 157 TYR B CA  
5399 C C   . TYR B 157 ? 0.2569 0.5513 0.2854 -0.0233 0.0463  -0.0218 157 TYR B C   
5400 O O   . TYR B 157 ? 0.2801 0.5751 0.2981 -0.0272 0.0503  -0.0187 157 TYR B O   
5401 C CB  . TYR B 157 ? 0.1995 0.4470 0.2267 -0.0315 0.0346  -0.0178 157 TYR B CB  
5402 C CG  . TYR B 157 ? 0.1954 0.4306 0.2277 -0.0410 0.0303  -0.0149 157 TYR B CG  
5403 C CD1 . TYR B 157 ? 0.1872 0.4317 0.2305 -0.0377 0.0267  -0.0188 157 TYR B CD1 
5404 C CD2 . TYR B 157 ? 0.3267 0.5411 0.3518 -0.0528 0.0302  -0.0083 157 TYR B CD2 
5405 C CE1 . TYR B 157 ? 0.2227 0.4570 0.2692 -0.0473 0.0228  -0.0173 157 TYR B CE1 
5406 C CE2 . TYR B 157 ? 0.3404 0.5415 0.3686 -0.0617 0.0271  -0.0070 157 TYR B CE2 
5407 C CZ  . TYR B 157 ? 0.2647 0.4765 0.3033 -0.0595 0.0234  -0.0121 157 TYR B CZ  
5408 O OH  . TYR B 157 ? 0.2354 0.4347 0.2756 -0.0692 0.0205  -0.0119 157 TYR B OH  
5409 N N   . THR B 158 ? 0.2328 0.5368 0.2676 -0.0088 0.0463  -0.0293 158 THR B N   
5410 C CA  . THR B 158 ? 0.2423 0.5539 0.2711 0.0040  0.0515  -0.0361 158 THR B CA  
5411 C C   . THR B 158 ? 0.3148 0.5969 0.3345 0.0147  0.0473  -0.0428 158 THR B C   
5412 O O   . THR B 158 ? 0.2068 0.4677 0.2283 0.0150  0.0407  -0.0423 158 THR B O   
5413 C CB  . THR B 158 ? 0.2766 0.6195 0.3181 0.0148  0.0564  -0.0401 158 THR B CB  
5414 O OG1 . THR B 158 ? 0.2801 0.6156 0.3304 0.0245  0.0513  -0.0427 158 THR B OG1 
5415 C CG2 . THR B 158 ? 0.2735 0.6504 0.3260 0.0029  0.0603  -0.0338 158 THR B CG2 
5416 N N   . GLN B 159 ? 0.3240 0.6053 0.3331 0.0228  0.0518  -0.0495 159 GLN B N   
5417 C CA  . GLN B 159 ? 0.2664 0.5208 0.2662 0.0317  0.0489  -0.0574 159 GLN B CA  
5418 C C   . GLN B 159 ? 0.2491 0.4970 0.2586 0.0440  0.0470  -0.0616 159 GLN B C   
5419 O O   . GLN B 159 ? 0.2637 0.4855 0.2706 0.0459  0.0414  -0.0631 159 GLN B O   
5420 C CB  . GLN B 159 ? 0.3031 0.5606 0.2896 0.0377  0.0552  -0.0658 159 GLN B CB  
5421 C CG  . GLN B 159 ? 0.3297 0.5596 0.3058 0.0460  0.0533  -0.0760 159 GLN B CG  
5422 C CD  . GLN B 159 ? 0.4020 0.6095 0.3677 0.0365  0.0462  -0.0737 159 GLN B CD  
5423 O OE1 . GLN B 159 ? 0.3185 0.5318 0.2801 0.0256  0.0444  -0.0657 159 GLN B OE1 
5424 N NE2 . GLN B 159 ? 0.3739 0.5561 0.3354 0.0407  0.0424  -0.0801 159 GLN B NE2 
5425 N N   . GLU B 160 ? 0.2614 0.5341 0.2824 0.0527  0.0518  -0.0624 160 GLU B N   
5426 C CA  . GLU B 160 ? 0.2864 0.5551 0.3167 0.0659  0.0502  -0.0644 160 GLU B CA  
5427 C C   . GLU B 160 ? 0.2947 0.5549 0.3330 0.0585  0.0417  -0.0576 160 GLU B C   
5428 O O   . GLU B 160 ? 0.2966 0.5366 0.3352 0.0658  0.0377  -0.0591 160 GLU B O   
5429 C CB  . GLU B 160 ? 0.3458 0.6486 0.3885 0.0771  0.0569  -0.0649 160 GLU B CB  
5430 C CG  . GLU B 160 ? 0.4635 0.7635 0.5157 0.0927  0.0552  -0.0652 160 GLU B CG  
5431 C CD  . GLU B 160 ? 0.5401 0.8748 0.6050 0.1073  0.0621  -0.0653 160 GLU B CD  
5432 O OE1 . GLU B 160 ? 0.5704 0.9365 0.6397 0.1024  0.0674  -0.0640 160 GLU B OE1 
5433 O OE2 . GLU B 160 ? 0.4820 0.8132 0.5526 0.1241  0.0624  -0.0658 160 GLU B OE2 
5434 N N   . GLU B 161 ? 0.2017 0.4760 0.2455 0.0436  0.0395  -0.0504 161 GLU B N   
5435 C CA  . GLU B 161 ? 0.1906 0.4555 0.2402 0.0358  0.0320  -0.0453 161 GLU B CA  
5436 C C   . GLU B 161 ? 0.2219 0.4506 0.2604 0.0321  0.0267  -0.0458 161 GLU B C   
5437 O O   . GLU B 161 ? 0.2003 0.4137 0.2412 0.0341  0.0212  -0.0452 161 GLU B O   
5438 C CB  . GLU B 161 ? 0.2291 0.5133 0.2849 0.0192  0.0319  -0.0386 161 GLU B CB  
5439 C CG  . GLU B 161 ? 0.2463 0.5696 0.3169 0.0208  0.0351  -0.0372 161 GLU B CG  
5440 C CD  . GLU B 161 ? 0.3012 0.6450 0.3763 0.0023  0.0370  -0.0317 161 GLU B CD  
5441 O OE1 . GLU B 161 ? 0.2309 0.5600 0.2961 -0.0097 0.0382  -0.0286 161 GLU B OE1 
5442 O OE2 . GLU B 161 ? 0.4142 0.7902 0.5028 -0.0003 0.0376  -0.0300 161 GLU B OE2 
5443 N N   . LYS B 162 ? 0.2757 0.4931 0.3022 0.0268  0.0281  -0.0465 162 LYS B N   
5444 C CA  . LYS B 162 ? 0.2581 0.4456 0.2746 0.0243  0.0233  -0.0471 162 LYS B CA  
5445 C C   . LYS B 162 ? 0.2949 0.4643 0.3084 0.0365  0.0221  -0.0541 162 LYS B C   
5446 O O   . LYS B 162 ? 0.2422 0.3908 0.2547 0.0359  0.0168  -0.0535 162 LYS B O   
5447 C CB  . LYS B 162 ? 0.2700 0.4550 0.2742 0.0180  0.0255  -0.0464 162 LYS B CB  
5448 C CG  . LYS B 162 ? 0.2928 0.4526 0.2874 0.0147  0.0203  -0.0459 162 LYS B CG  
5449 C CD  . LYS B 162 ? 0.2833 0.4458 0.2658 0.0093  0.0222  -0.0441 162 LYS B CD  
5450 C CE  . LYS B 162 ? 0.3107 0.4837 0.2859 0.0161  0.0277  -0.0527 162 LYS B CE  
5451 N NZ  . LYS B 162 ? 0.2636 0.4382 0.2248 0.0109  0.0283  -0.0517 162 LYS B NZ  
5452 N N   . GLU B 163 ? 0.2679 0.4442 0.2798 0.0478  0.0278  -0.0608 163 GLU B N   
5453 C CA  . GLU B 163 ? 0.3009 0.4568 0.3091 0.0596  0.0280  -0.0675 163 GLU B CA  
5454 C C   . GLU B 163 ? 0.2945 0.4494 0.3137 0.0663  0.0248  -0.0639 163 GLU B C   
5455 O O   . GLU B 163 ? 0.2649 0.3965 0.2810 0.0715  0.0224  -0.0659 163 GLU B O   
5456 C CB  . GLU B 163 ? 0.2485 0.4109 0.2520 0.0711  0.0362  -0.0758 163 GLU B CB  
5457 C CG  . GLU B 163 ? 0.2745 0.4311 0.2630 0.0655  0.0388  -0.0818 163 GLU B CG  
5458 C CD  . GLU B 163 ? 0.4532 0.6225 0.4369 0.0751  0.0481  -0.0899 163 GLU B CD  
5459 O OE1 . GLU B 163 ? 0.5612 0.7404 0.5532 0.0883  0.0529  -0.0913 163 GLU B OE1 
5460 O OE2 . GLU B 163 ? 0.5374 0.7079 0.5085 0.0699  0.0508  -0.0947 163 GLU B OE2 
5461 N N   . TYR B 164 ? 0.3071 0.4884 0.3388 0.0657  0.0249  -0.0585 164 TYR B N   
5462 C CA  . TYR B 164 ? 0.3015 0.4865 0.3434 0.0712  0.0211  -0.0544 164 TYR B CA  
5463 C C   . TYR B 164 ? 0.2387 0.4042 0.2787 0.0614  0.0136  -0.0506 164 TYR B C   
5464 O O   . TYR B 164 ? 0.2189 0.3689 0.2591 0.0675  0.0105  -0.0500 164 TYR B O   
5465 C CB  . TYR B 164 ? 0.1940 0.4163 0.2495 0.0699  0.0223  -0.0497 164 TYR B CB  
5466 C CG  . TYR B 164 ? 0.2957 0.5276 0.3617 0.0743  0.0176  -0.0450 164 TYR B CG  
5467 C CD1 . TYR B 164 ? 0.3520 0.5857 0.4222 0.0925  0.0193  -0.0452 164 TYR B CD1 
5468 C CD2 . TYR B 164 ? 0.3602 0.5987 0.4310 0.0606  0.0118  -0.0402 164 TYR B CD2 
5469 C CE1 . TYR B 164 ? 0.4288 0.6738 0.5079 0.0972  0.0146  -0.0397 164 TYR B CE1 
5470 C CE2 . TYR B 164 ? 0.4773 0.7270 0.5565 0.0639  0.0072  -0.0363 164 TYR B CE2 
5471 C CZ  . TYR B 164 ? 0.4800 0.7344 0.5635 0.0823  0.0082  -0.0356 164 TYR B CZ  
5472 O OH  . TYR B 164 ? 0.5822 0.8504 0.6736 0.0860  0.0033  -0.0306 164 TYR B OH  
5473 N N   . VAL B 165 ? 0.2534 0.4189 0.2911 0.0466  0.0114  -0.0476 165 VAL B N   
5474 C CA  . VAL B 165 ? 0.2693 0.4152 0.3041 0.0378  0.0054  -0.0445 165 VAL B CA  
5475 C C   . VAL B 165 ? 0.2444 0.3619 0.2702 0.0425  0.0038  -0.0482 165 VAL B C   
5476 O O   . VAL B 165 ? 0.2467 0.3496 0.2729 0.0438  -0.0002 -0.0468 165 VAL B O   
5477 C CB  . VAL B 165 ? 0.2123 0.3593 0.2440 0.0233  0.0051  -0.0407 165 VAL B CB  
5478 C CG1 . VAL B 165 ? 0.2207 0.3454 0.2486 0.0165  0.0000  -0.0381 165 VAL B CG1 
5479 C CG2 . VAL B 165 ? 0.1670 0.3398 0.2075 0.0158  0.0067  -0.0371 165 VAL B CG2 
5480 N N   . LEU B 166 ? 0.2425 0.3529 0.2594 0.0444  0.0072  -0.0533 166 LEU B N   
5481 C CA  . LEU B 166 ? 0.2073 0.2921 0.2148 0.0462  0.0059  -0.0578 166 LEU B CA  
5482 C C   . LEU B 166 ? 0.2509 0.3233 0.2600 0.0577  0.0065  -0.0602 166 LEU B C   
5483 O O   . LEU B 166 ? 0.3093 0.3611 0.3151 0.0568  0.0033  -0.0601 166 LEU B O   
5484 C CB  . LEU B 166 ? 0.2277 0.3108 0.2247 0.0456  0.0098  -0.0641 166 LEU B CB  
5485 C CG  . LEU B 166 ? 0.2535 0.3408 0.2446 0.0343  0.0082  -0.0612 166 LEU B CG  
5486 C CD1 . LEU B 166 ? 0.3264 0.4204 0.3077 0.0352  0.0131  -0.0676 166 LEU B CD1 
5487 C CD2 . LEU B 166 ? 0.3229 0.3922 0.3097 0.0278  0.0027  -0.0593 166 LEU B CD2 
5488 N N   . ASN B 167 ? 0.2268 0.3114 0.2405 0.0692  0.0112  -0.0618 167 ASN B N   
5489 C CA  . ASN B 167 ? 0.2597 0.3323 0.2748 0.0823  0.0126  -0.0624 167 ASN B CA  
5490 C C   . ASN B 167 ? 0.2682 0.3405 0.2903 0.0811  0.0067  -0.0550 167 ASN B C   
5491 O O   . ASN B 167 ? 0.2876 0.3389 0.3065 0.0856  0.0054  -0.0544 167 ASN B O   
5492 C CB  . ASN B 167 ? 0.3496 0.4404 0.3702 0.0964  0.0189  -0.0638 167 ASN B CB  
5493 C CG  . ASN B 167 ? 0.5477 0.6307 0.5585 0.1014  0.0262  -0.0731 167 ASN B CG  
5494 O OD1 . ASN B 167 ? 0.6328 0.6946 0.6318 0.0946  0.0261  -0.0790 167 ASN B OD1 
5495 N ND2 . ASN B 167 ? 0.4906 0.5928 0.5061 0.1133  0.0327  -0.0748 167 ASN B ND2 
5496 N N   . LYS B 168 ? 0.2807 0.3757 0.3115 0.0745  0.0035  -0.0497 168 LYS B N   
5497 C CA  . LYS B 168 ? 0.2742 0.3696 0.3101 0.0725  -0.0020 -0.0437 168 LYS B CA  
5498 C C   . LYS B 168 ? 0.2582 0.3302 0.2873 0.0628  -0.0062 -0.0434 168 LYS B C   
5499 O O   . LYS B 168 ? 0.1997 0.2605 0.2286 0.0647  -0.0093 -0.0404 168 LYS B O   
5500 C CB  . LYS B 168 ? 0.2085 0.3340 0.2544 0.0660  -0.0041 -0.0395 168 LYS B CB  
5501 C CG  . LYS B 168 ? 0.2724 0.4272 0.3275 0.0761  -0.0004 -0.0388 168 LYS B CG  
5502 C CD  . LYS B 168 ? 0.4045 0.5769 0.4686 0.0838  -0.0035 -0.0333 168 LYS B CD  
5503 C CE  . LYS B 168 ? 0.4734 0.6215 0.5326 0.0938  -0.0052 -0.0312 168 LYS B CE  
5504 N NZ  . LYS B 168 ? 0.5010 0.6673 0.5680 0.1089  -0.0056 -0.0254 168 LYS B NZ  
5505 N N   . TYR B 169 ? 0.2247 0.2908 0.2483 0.0529  -0.0062 -0.0458 169 TYR B N   
5506 C CA  . TYR B 169 ? 0.2491 0.2956 0.2670 0.0451  -0.0097 -0.0452 169 TYR B CA  
5507 C C   . TYR B 169 ? 0.2502 0.2737 0.2616 0.0506  -0.0090 -0.0485 169 TYR B C   
5508 O O   . TYR B 169 ? 0.2310 0.2407 0.2409 0.0481  -0.0120 -0.0463 169 TYR B O   
5509 C CB  . TYR B 169 ? 0.2661 0.3132 0.2793 0.0358  -0.0093 -0.0461 169 TYR B CB  
5510 C CG  . TYR B 169 ? 0.2209 0.2810 0.2384 0.0270  -0.0106 -0.0414 169 TYR B CG  
5511 C CD1 . TYR B 169 ? 0.2071 0.2817 0.2325 0.0266  -0.0115 -0.0386 169 TYR B CD1 
5512 C CD2 . TYR B 169 ? 0.1991 0.2568 0.2122 0.0188  -0.0107 -0.0397 169 TYR B CD2 
5513 C CE1 . TYR B 169 ? 0.2154 0.2991 0.2435 0.0165  -0.0120 -0.0353 169 TYR B CE1 
5514 C CE2 . TYR B 169 ? 0.2652 0.3302 0.2809 0.0106  -0.0107 -0.0351 169 TYR B CE2 
5515 C CZ  . TYR B 169 ? 0.2411 0.3179 0.2640 0.0087  -0.0111 -0.0336 169 TYR B CZ  
5516 O OH  . TYR B 169 ? 0.1787 0.2601 0.2029 -0.0014 -0.0105 -0.0302 169 TYR B OH  
5517 N N   . PHE B 170 ? 0.2068 0.2251 0.2135 0.0573  -0.0043 -0.0541 170 PHE B N   
5518 C CA  . PHE B 170 ? 0.2486 0.2418 0.2478 0.0608  -0.0028 -0.0580 170 PHE B CA  
5519 C C   . PHE B 170 ? 0.2763 0.2622 0.2789 0.0708  -0.0027 -0.0536 170 PHE B C   
5520 O O   . PHE B 170 ? 0.2740 0.2383 0.2717 0.0704  -0.0033 -0.0534 170 PHE B O   
5521 C CB  . PHE B 170 ? 0.2695 0.2565 0.2608 0.0645  0.0028  -0.0666 170 PHE B CB  
5522 C CG  . PHE B 170 ? 0.3260 0.3104 0.3096 0.0531  0.0017  -0.0713 170 PHE B CG  
5523 C CD1 . PHE B 170 ? 0.3517 0.3174 0.3288 0.0460  -0.0005 -0.0737 170 PHE B CD1 
5524 C CD2 . PHE B 170 ? 0.3416 0.3449 0.3249 0.0490  0.0025  -0.0721 170 PHE B CD2 
5525 C CE1 . PHE B 170 ? 0.4427 0.4104 0.4133 0.0359  -0.0023 -0.0773 170 PHE B CE1 
5526 C CE2 . PHE B 170 ? 0.4167 0.4201 0.3926 0.0395  0.0009  -0.0749 170 PHE B CE2 
5527 C CZ  . PHE B 170 ? 0.4416 0.4284 0.4114 0.0332  -0.0018 -0.0776 170 PHE B CZ  
5528 N N   . GLU B 171 ? 0.2587 0.2640 0.2696 0.0791  -0.0023 -0.0493 171 GLU B N   
5529 C CA  . GLU B 171 ? 0.2807 0.2835 0.2952 0.0884  -0.0034 -0.0431 171 GLU B CA  
5530 C C   . GLU B 171 ? 0.2585 0.2564 0.2734 0.0796  -0.0092 -0.0381 171 GLU B C   
5531 O O   . GLU B 171 ? 0.3041 0.2860 0.3159 0.0837  -0.0097 -0.0346 171 GLU B O   
5532 C CB  . GLU B 171 ? 0.2469 0.2787 0.2716 0.0974  -0.0030 -0.0389 171 GLU B CB  
5533 C CG  . GLU B 171 ? 0.4067 0.4421 0.4316 0.1110  0.0039  -0.0425 171 GLU B CG  
5534 C CD  . GLU B 171 ? 0.5523 0.6226 0.5892 0.1196  0.0042  -0.0378 171 GLU B CD  
5535 O OE1 . GLU B 171 ? 0.5260 0.6134 0.5699 0.1175  -0.0011 -0.0310 171 GLU B OE1 
5536 O OE2 . GLU B 171 ? 0.6394 0.7215 0.6784 0.1282  0.0100  -0.0413 171 GLU B OE2 
5537 N N   . ILE B 172 ? 0.2471 0.2575 0.2648 0.0680  -0.0129 -0.0376 172 ILE B N   
5538 C CA  . ILE B 172 ? 0.2806 0.2867 0.2981 0.0599  -0.0175 -0.0338 172 ILE B CA  
5539 C C   . ILE B 172 ? 0.2696 0.2509 0.2796 0.0554  -0.0175 -0.0357 172 ILE B C   
5540 O O   . ILE B 172 ? 0.2585 0.2297 0.2668 0.0545  -0.0194 -0.0321 172 ILE B O   
5541 C CB  . ILE B 172 ? 0.3086 0.3302 0.3297 0.0491  -0.0200 -0.0335 172 ILE B CB  
5542 C CG1 . ILE B 172 ? 0.2986 0.3460 0.3276 0.0509  -0.0209 -0.0310 172 ILE B CG1 
5543 C CG2 . ILE B 172 ? 0.2781 0.2905 0.2970 0.0406  -0.0234 -0.0314 172 ILE B CG2 
5544 C CD1 . ILE B 172 ? 0.2732 0.3274 0.3049 0.0518  -0.0247 -0.0262 172 ILE B CD1 
5545 N N   . ILE B 173 ? 0.2396 0.2130 0.2447 0.0517  -0.0153 -0.0414 173 ILE B N   
5546 C CA  . ILE B 173 ? 0.2020 0.1556 0.2005 0.0459  -0.0154 -0.0439 173 ILE B CA  
5547 C C   . ILE B 173 ? 0.2197 0.1529 0.2136 0.0528  -0.0126 -0.0437 173 ILE B C   
5548 O O   . ILE B 173 ? 0.2966 0.2156 0.2874 0.0485  -0.0137 -0.0418 173 ILE B O   
5549 C CB  . ILE B 173 ? 0.2494 0.2024 0.2430 0.0402  -0.0139 -0.0505 173 ILE B CB  
5550 C CG1 . ILE B 173 ? 0.2167 0.1852 0.2135 0.0324  -0.0169 -0.0483 173 ILE B CG1 
5551 C CG2 . ILE B 173 ? 0.3359 0.2694 0.3220 0.0348  -0.0133 -0.0546 173 ILE B CG2 
5552 C CD1 . ILE B 173 ? 0.2911 0.2658 0.2837 0.0285  -0.0155 -0.0529 173 ILE B CD1 
5553 N N   . LYS B 174 ? 0.2611 0.1920 0.2543 0.0638  -0.0084 -0.0453 174 LYS B N   
5554 C CA  . LYS B 174 ? 0.2542 0.1624 0.2421 0.0721  -0.0045 -0.0444 174 LYS B CA  
5555 C C   . LYS B 174 ? 0.3254 0.2329 0.3161 0.0764  -0.0070 -0.0350 174 LYS B C   
5556 O O   . LYS B 174 ? 0.3307 0.2158 0.3157 0.0799  -0.0043 -0.0325 174 LYS B O   
5557 C CB  . LYS B 174 ? 0.2695 0.1775 0.2568 0.0856  0.0013  -0.0473 174 LYS B CB  
5558 C CG  . LYS B 174 ? 0.3391 0.2359 0.3186 0.0826  0.0059  -0.0580 174 LYS B CG  
5559 C CD  . LYS B 174 ? 0.5277 0.4208 0.5055 0.0979  0.0130  -0.0611 174 LYS B CD  
5560 C CE  . LYS B 174 ? 0.6266 0.5512 0.6123 0.1017  0.0129  -0.0617 174 LYS B CE  
5561 N NZ  . LYS B 174 ? 0.6944 0.6165 0.6731 0.1015  0.0184  -0.0724 174 LYS B NZ  
5562 N N   . LYS B 175 ? 0.2610 0.1920 0.2594 0.0757  -0.0116 -0.0298 175 LYS B N   
5563 C CA  . LYS B 175 ? 0.2558 0.1904 0.2560 0.0786  -0.0145 -0.0212 175 LYS B CA  
5564 C C   . LYS B 175 ? 0.3004 0.2330 0.2994 0.0664  -0.0183 -0.0199 175 LYS B C   
5565 O O   . LYS B 175 ? 0.2700 0.2066 0.2694 0.0673  -0.0208 -0.0135 175 LYS B O   
5566 C CB  . LYS B 175 ? 0.2707 0.2347 0.2794 0.0846  -0.0172 -0.0171 175 LYS B CB  
5567 C CG  . LYS B 175 ? 0.3973 0.3667 0.4085 0.1009  -0.0140 -0.0137 175 LYS B CG  
5568 C CD  . LYS B 175 ? 0.5830 0.5848 0.6035 0.1037  -0.0151 -0.0144 175 LYS B CD  
5569 C CE  . LYS B 175 ? 0.6260 0.6538 0.6526 0.0968  -0.0212 -0.0104 175 LYS B CE  
5570 N NZ  . LYS B 175 ? 0.7452 0.8067 0.7815 0.1022  -0.0219 -0.0090 175 LYS B NZ  
5571 N N   . THR B 176 ? 0.2450 0.1732 0.2423 0.0557  -0.0187 -0.0255 176 THR B N   
5572 C CA  . THR B 176 ? 0.2182 0.1504 0.2164 0.0457  -0.0221 -0.0241 176 THR B CA  
5573 C C   . THR B 176 ? 0.2787 0.1945 0.2721 0.0434  -0.0216 -0.0204 176 THR B C   
5574 O O   . THR B 176 ? 0.2508 0.1722 0.2450 0.0420  -0.0238 -0.0155 176 THR B O   
5575 C CB  . THR B 176 ? 0.2740 0.2091 0.2724 0.0369  -0.0225 -0.0296 176 THR B CB  
5576 O OG1 . THR B 176 ? 0.2420 0.1947 0.2450 0.0375  -0.0233 -0.0309 176 THR B OG1 
5577 C CG2 . THR B 176 ? 0.2508 0.1865 0.2495 0.0284  -0.0248 -0.0278 176 THR B CG2 
5578 N N   . LEU B 177 ? 0.2633 0.1589 0.2512 0.0422  -0.0183 -0.0229 177 LEU B N   
5579 C CA  . LEU B 177 ? 0.3055 0.1861 0.2890 0.0381  -0.0174 -0.0189 177 LEU B CA  
5580 C C   . LEU B 177 ? 0.2978 0.1745 0.2795 0.0476  -0.0167 -0.0104 177 LEU B C   
5581 O O   . LEU B 177 ? 0.3023 0.1781 0.2824 0.0447  -0.0176 -0.0048 177 LEU B O   
5582 C CB  . LEU B 177 ? 0.3146 0.1735 0.2918 0.0324  -0.0136 -0.0242 177 LEU B CB  
5583 C CG  . LEU B 177 ? 0.2857 0.1524 0.2643 0.0212  -0.0153 -0.0311 177 LEU B CG  
5584 C CD1 . LEU B 177 ? 0.3893 0.2372 0.3609 0.0145  -0.0119 -0.0380 177 LEU B CD1 
5585 C CD2 . LEU B 177 ? 0.3131 0.1909 0.2954 0.0133  -0.0184 -0.0279 177 LEU B CD2 
5586 N N   . SER B 178 ? 0.2768 0.1544 0.2591 0.0596  -0.0151 -0.0089 178 SER B N   
5587 C CA  . SER B 178 ? 0.2642 0.1433 0.2456 0.0706  -0.0151 0.0006  178 SER B CA  
5588 C C   . SER B 178 ? 0.2475 0.1501 0.2328 0.0684  -0.0203 0.0052  178 SER B C   
5589 O O   . SER B 178 ? 0.2545 0.1569 0.2367 0.0718  -0.0211 0.0134  178 SER B O   
5590 C CB  . SER B 178 ? 0.2731 0.1565 0.2568 0.0850  -0.0129 0.0014  178 SER B CB  
5591 O OG  . SER B 178 ? 0.3693 0.2253 0.3466 0.0893  -0.0067 -0.0019 178 SER B OG  
5592 N N   . ILE B 179 ? 0.2278 0.1504 0.2190 0.0626  -0.0237 0.0002  179 ILE B N   
5593 C CA  . ILE B 179 ? 0.2703 0.2132 0.2637 0.0605  -0.0279 0.0035  179 ILE B CA  
5594 C C   . ILE B 179 ? 0.2138 0.1503 0.2033 0.0514  -0.0284 0.0047  179 ILE B C   
5595 O O   . ILE B 179 ? 0.2292 0.1746 0.2165 0.0515  -0.0304 0.0095  179 ILE B O   
5596 C CB  . ILE B 179 ? 0.2750 0.2398 0.2750 0.0568  -0.0306 -0.0017 179 ILE B CB  
5597 C CG1 . ILE B 179 ? 0.3708 0.3569 0.3720 0.0562  -0.0345 0.0017  179 ILE B CG1 
5598 C CG2 . ILE B 179 ? 0.2957 0.2569 0.2964 0.0458  -0.0304 -0.0082 179 ILE B CG2 
5599 C CD1 . ILE B 179 ? 0.4492 0.4591 0.4569 0.0558  -0.0367 -0.0012 179 ILE B CD1 
5600 N N   . TYR B 180 ? 0.2390 0.1617 0.2272 0.0437  -0.0264 0.0004  180 TYR B N   
5601 C CA  . TYR B 180 ? 0.2866 0.2043 0.2717 0.0361  -0.0260 0.0022  180 TYR B CA  
5602 C C   . TYR B 180 ? 0.3079 0.2121 0.2867 0.0398  -0.0238 0.0101  180 TYR B C   
5603 O O   . TYR B 180 ? 0.2797 0.1879 0.2554 0.0374  -0.0243 0.0148  180 TYR B O   
5604 C CB  . TYR B 180 ? 0.2210 0.1309 0.2073 0.0274  -0.0245 -0.0034 180 TYR B CB  
5605 C CG  . TYR B 180 ? 0.2256 0.1493 0.2170 0.0232  -0.0265 -0.0089 180 TYR B CG  
5606 C CD1 . TYR B 180 ? 0.2471 0.1804 0.2395 0.0191  -0.0276 -0.0087 180 TYR B CD1 
5607 C CD2 . TYR B 180 ? 0.2269 0.1527 0.2211 0.0239  -0.0266 -0.0139 180 TYR B CD2 
5608 C CE1 . TYR B 180 ? 0.2279 0.1701 0.2240 0.0161  -0.0285 -0.0128 180 TYR B CE1 
5609 C CE2 . TYR B 180 ? 0.1770 0.1140 0.1750 0.0202  -0.0280 -0.0174 180 TYR B CE2 
5610 C CZ  . TYR B 180 ? 0.1851 0.1288 0.1839 0.0166  -0.0288 -0.0166 180 TYR B CZ  
5611 O OH  . TYR B 180 ? 0.2077 0.1588 0.2092 0.0136  -0.0291 -0.0192 180 TYR B OH  
5612 N N   . ARG B 181 ? 0.3055 0.1921 0.2813 0.0456  -0.0206 0.0117  181 ARG B N   
5613 C CA  . ARG B 181 ? 0.3076 0.1785 0.2765 0.0506  -0.0177 0.0207  181 ARG B CA  
5614 C C   . ARG B 181 ? 0.3322 0.2197 0.3003 0.0591  -0.0207 0.0291  181 ARG B C   
5615 O O   . ARG B 181 ? 0.3309 0.2168 0.2935 0.0584  -0.0203 0.0367  181 ARG B O   
5616 C CB  . ARG B 181 ? 0.3512 0.1994 0.3166 0.0579  -0.0132 0.0207  181 ARG B CB  
5617 C CG  . ARG B 181 ? 0.4208 0.2458 0.3827 0.0481  -0.0090 0.0141  181 ARG B CG  
5618 C CD  . ARG B 181 ? 0.3938 0.1909 0.3493 0.0560  -0.0031 0.0145  181 ARG B CD  
5619 N NE  . ARG B 181 ? 0.4375 0.2177 0.3903 0.0456  0.0000  0.0043  181 ARG B NE  
5620 C CZ  . ARG B 181 ? 0.4708 0.2548 0.4260 0.0459  0.0000  -0.0054 181 ARG B CZ  
5621 N NH1 . ARG B 181 ? 0.4629 0.2659 0.4240 0.0563  -0.0025 -0.0058 181 ARG B NH1 
5622 N NH2 . ARG B 181 ? 0.6091 0.3794 0.5605 0.0350  0.0024  -0.0147 181 ARG B NH2 
5623 N N   . GLU B 182 ? 0.2591 0.1652 0.2324 0.0663  -0.0237 0.0277  182 GLU B N   
5624 C CA  . GLU B 182 ? 0.2737 0.1995 0.2466 0.0744  -0.0271 0.0354  182 GLU B CA  
5625 C C   . GLU B 182 ? 0.2789 0.2214 0.2501 0.0659  -0.0306 0.0352  182 GLU B C   
5626 O O   . GLU B 182 ? 0.2634 0.2121 0.2291 0.0691  -0.0317 0.0435  182 GLU B O   
5627 C CB  . GLU B 182 ? 0.3651 0.3107 0.3454 0.0820  -0.0296 0.0328  182 GLU B CB  
5628 C CG  . GLU B 182 ? 0.5795 0.5124 0.5599 0.0957  -0.0258 0.0364  182 GLU B CG  
5629 C CD  . GLU B 182 ? 0.7227 0.6666 0.7109 0.0986  -0.0257 0.0289  182 GLU B CD  
5630 O OE1 . GLU B 182 ? 0.6854 0.6525 0.6795 0.0917  -0.0297 0.0234  182 GLU B OE1 
5631 O OE2 . GLU B 182 ? 0.7426 0.6710 0.7303 0.1076  -0.0211 0.0283  182 GLU B OE2 
5632 N N   . ILE B 183 ? 0.2657 0.2158 0.2409 0.0558  -0.0319 0.0260  183 ILE B N   
5633 C CA  . ILE B 183 ? 0.2631 0.2281 0.2358 0.0490  -0.0344 0.0250  183 ILE B CA  
5634 C C   . ILE B 183 ? 0.3335 0.2861 0.2996 0.0444  -0.0315 0.0292  183 ILE B C   
5635 O O   . ILE B 183 ? 0.2618 0.2248 0.2224 0.0427  -0.0326 0.0325  183 ILE B O   
5636 C CB  . ILE B 183 ? 0.2538 0.2280 0.2315 0.0404  -0.0356 0.0148  183 ILE B CB  
5637 C CG1 . ILE B 183 ? 0.2907 0.2491 0.2706 0.0340  -0.0325 0.0096  183 ILE B CG1 
5638 C CG2 . ILE B 183 ? 0.2441 0.2339 0.2277 0.0436  -0.0383 0.0117  183 ILE B CG2 
5639 C CD1 . ILE B 183 ? 0.3420 0.3000 0.3189 0.0263  -0.0311 0.0079  183 ILE B CD1 
5640 N N   . LYS B 184 ? 0.2650 0.1964 0.2308 0.0419  -0.0276 0.0292  184 LYS B N   
5641 C CA  . LYS B 184 ? 0.3432 0.2633 0.3031 0.0372  -0.0243 0.0343  184 LYS B CA  
5642 C C   . LYS B 184 ? 0.3324 0.2475 0.2846 0.0451  -0.0234 0.0462  184 LYS B C   
5643 O O   . LYS B 184 ? 0.3403 0.2615 0.2862 0.0433  -0.0231 0.0521  184 LYS B O   
5644 C CB  . LYS B 184 ? 0.2995 0.1999 0.2613 0.0310  -0.0205 0.0308  184 LYS B CB  
5645 C CG  . LYS B 184 ? 0.3894 0.2791 0.3463 0.0238  -0.0165 0.0355  184 LYS B CG  
5646 C CD  . LYS B 184 ? 0.3413 0.2132 0.3000 0.0166  -0.0132 0.0315  184 LYS B CD  
5647 C CE  . LYS B 184 ? 0.4218 0.2840 0.3758 0.0082  -0.0089 0.0369  184 LYS B CE  
5648 N NZ  . LYS B 184 ? 0.5508 0.4050 0.4962 0.0147  -0.0071 0.0483  184 LYS B NZ  
5649 N N   . GLU B 185 ? 0.2865 0.1908 0.2387 0.0548  -0.0225 0.0505  185 GLU B N   
5650 C CA  . GLU B 185 ? 0.3534 0.2507 0.2979 0.0643  -0.0210 0.0636  185 GLU B CA  
5651 C C   . GLU B 185 ? 0.4364 0.3612 0.3785 0.0695  -0.0259 0.0690  185 GLU B C   
5652 O O   . GLU B 185 ? 0.3965 0.3215 0.3305 0.0738  -0.0253 0.0804  185 GLU B O   
5653 C CB  . GLU B 185 ? 0.3864 0.2670 0.3316 0.0759  -0.0185 0.0667  185 GLU B CB  
5654 C CG  . GLU B 185 ? 0.5717 0.4196 0.5146 0.0704  -0.0123 0.0634  185 GLU B CG  
5655 C CD  . GLU B 185 ? 0.7835 0.6115 0.7172 0.0650  -0.0076 0.0721  185 GLU B CD  
5656 O OE1 . GLU B 185 ? 0.7971 0.6153 0.7234 0.0747  -0.0053 0.0848  185 GLU B OE1 
5657 O OE2 . GLU B 185 ? 0.8297 0.6530 0.7637 0.0510  -0.0059 0.0668  185 GLU B OE2 
5658 N N   . GLU B 186 ? 0.2797 0.2282 0.2281 0.0681  -0.0308 0.0612  186 GLU B N   
5659 C CA  . GLU B 186 ? 0.3143 0.2914 0.2603 0.0708  -0.0359 0.0644  186 GLU B CA  
5660 C C   . GLU B 186 ? 0.3437 0.3318 0.2850 0.0594  -0.0368 0.0595  186 GLU B C   
5661 O O   . GLU B 186 ? 0.3144 0.3268 0.2527 0.0588  -0.0410 0.0593  186 GLU B O   
5662 C CB  . GLU B 186 ? 0.3124 0.3104 0.2670 0.0742  -0.0403 0.0583  186 GLU B CB  
5663 C CG  . GLU B 186 ? 0.4090 0.4026 0.3674 0.0885  -0.0394 0.0648  186 GLU B CG  
5664 C CD  . GLU B 186 ? 0.4733 0.4795 0.4421 0.0894  -0.0413 0.0562  186 GLU B CD  
5665 O OE1 . GLU B 186 ? 0.4399 0.4634 0.4123 0.0796  -0.0445 0.0471  186 GLU B OE1 
5666 O OE2 . GLU B 186 ? 0.5051 0.5032 0.4779 0.1002  -0.0390 0.0587  186 GLU B OE2 
5667 N N   . GLY B 187 ? 0.2928 0.2652 0.2335 0.0504  -0.0327 0.0552  187 GLY B N   
5668 C CA  . GLY B 187 ? 0.2792 0.2620 0.2153 0.0414  -0.0325 0.0507  187 GLY B CA  
5669 C C   . GLY B 187 ? 0.3279 0.3273 0.2680 0.0359  -0.0356 0.0389  187 GLY B C   
5670 O O   . GLY B 187 ? 0.3010 0.3110 0.2356 0.0298  -0.0355 0.0347  187 GLY B O   
5671 N N   . LYS B 188 ? 0.2621 0.2625 0.2107 0.0373  -0.0375 0.0332  188 LYS B N   
5672 C CA  . LYS B 188 ? 0.2262 0.2382 0.1785 0.0308  -0.0394 0.0221  188 LYS B CA  
5673 C C   . LYS B 188 ? 0.2419 0.2409 0.1972 0.0234  -0.0356 0.0143  188 LYS B C   
5674 O O   . LYS B 188 ? 0.2403 0.2452 0.1957 0.0173  -0.0356 0.0058  188 LYS B O   
5675 C CB  . LYS B 188 ? 0.2158 0.2356 0.1762 0.0348  -0.0425 0.0199  188 LYS B CB  
5676 C CG  . LYS B 188 ? 0.3278 0.3684 0.2870 0.0426  -0.0469 0.0271  188 LYS B CG  
5677 C CD  . LYS B 188 ? 0.3794 0.4309 0.3480 0.0468  -0.0493 0.0248  188 LYS B CD  
5678 C CE  . LYS B 188 ? 0.4491 0.5237 0.4178 0.0566  -0.0535 0.0334  188 LYS B CE  
5679 N NZ  . LYS B 188 ? 0.5599 0.6612 0.5229 0.0506  -0.0581 0.0321  188 LYS B NZ  
5680 N N   . GLY B 189 ? 0.2205 0.2022 0.1779 0.0237  -0.0321 0.0171  189 GLY B N   
5681 C CA  . GLY B 189 ? 0.2296 0.2030 0.1901 0.0176  -0.0287 0.0113  189 GLY B CA  
5682 C C   . GLY B 189 ? 0.2670 0.2262 0.2276 0.0169  -0.0252 0.0166  189 GLY B C   
5683 O O   . GLY B 189 ? 0.2986 0.2490 0.2576 0.0211  -0.0251 0.0234  189 GLY B O   
5684 N N   . SER B 190 ? 0.2507 0.2079 0.2129 0.0115  -0.0219 0.0135  190 SER B N   
5685 C CA  . SER B 190 ? 0.2230 0.1689 0.1876 0.0083  -0.0188 0.0166  190 SER B CA  
5686 C C   . SER B 190 ? 0.2406 0.1815 0.2133 0.0067  -0.0193 0.0110  190 SER B C   
5687 O O   . SER B 190 ? 0.2007 0.1476 0.1772 0.0071  -0.0208 0.0050  190 SER B O   
5688 C CB  . SER B 190 ? 0.2623 0.2130 0.2252 0.0034  -0.0147 0.0175  190 SER B CB  
5689 O OG  . SER B 190 ? 0.2611 0.2166 0.2150 0.0045  -0.0138 0.0233  190 SER B OG  
5690 N N   . VAL B 191 ? 0.2276 0.1570 0.2020 0.0041  -0.0179 0.0129  191 VAL B N   
5691 C CA  . VAL B 191 ? 0.2235 0.1500 0.2044 0.0012  -0.0183 0.0074  191 VAL B CA  
5692 C C   . VAL B 191 ? 0.2504 0.1768 0.2339 -0.0065 -0.0154 0.0079  191 VAL B C   
5693 O O   . VAL B 191 ? 0.2572 0.1754 0.2370 -0.0104 -0.0129 0.0128  191 VAL B O   
5694 C CB  . VAL B 191 ? 0.2300 0.1443 0.2105 0.0044  -0.0194 0.0068  191 VAL B CB  
5695 C CG1 . VAL B 191 ? 0.2486 0.1633 0.2347 0.0010  -0.0202 0.0003  191 VAL B CG1 
5696 C CG2 . VAL B 191 ? 0.2663 0.1852 0.2454 0.0124  -0.0221 0.0074  191 VAL B CG2 
5697 N N   . SER B 192 ? 0.2061 0.1426 0.1960 -0.0089 -0.0157 0.0035  192 SER B N   
5698 C CA  . SER B 192 ? 0.2397 0.1824 0.2341 -0.0160 -0.0135 0.0037  192 SER B CA  
5699 C C   . SER B 192 ? 0.2044 0.1457 0.2031 -0.0196 -0.0154 -0.0006 192 SER B C   
5700 O O   . SER B 192 ? 0.2246 0.1601 0.2225 -0.0159 -0.0178 -0.0038 192 SER B O   
5701 C CB  . SER B 192 ? 0.2630 0.2215 0.2615 -0.0142 -0.0120 0.0030  192 SER B CB  
5702 O OG  . SER B 192 ? 0.2354 0.1979 0.2375 -0.0095 -0.0140 -0.0013 192 SER B OG  
5703 N N   . THR B 193 ? 0.1953 0.1446 0.1984 -0.0274 -0.0143 -0.0009 193 THR B N   
5704 C CA  . THR B 193 ? 0.1921 0.1463 0.1995 -0.0311 -0.0166 -0.0055 193 THR B CA  
5705 C C   . THR B 193 ? 0.2424 0.2187 0.2580 -0.0343 -0.0163 -0.0048 193 THR B C   
5706 O O   . THR B 193 ? 0.2191 0.2054 0.2372 -0.0324 -0.0137 -0.0013 193 THR B O   
5707 C CB  . THR B 193 ? 0.2068 0.1456 0.2097 -0.0389 -0.0163 -0.0080 193 THR B CB  
5708 O OG1 . THR B 193 ? 0.2380 0.1819 0.2431 -0.0415 -0.0190 -0.0137 193 THR B OG1 
5709 C CG2 . THR B 193 ? 0.2469 0.1850 0.2493 -0.0502 -0.0132 -0.0055 193 THR B CG2 
5710 N N   . SER B 194 ? 0.2087 0.1943 0.2284 -0.0377 -0.0188 -0.0080 194 SER B N   
5711 C CA  . SER B 194 ? 0.1764 0.1864 0.2047 -0.0398 -0.0193 -0.0068 194 SER B CA  
5712 C C   . SER B 194 ? 0.1851 0.2015 0.2147 -0.0531 -0.0205 -0.0096 194 SER B C   
5713 O O   . SER B 194 ? 0.1951 0.1945 0.2181 -0.0588 -0.0213 -0.0141 194 SER B O   
5714 C CB  . SER B 194 ? 0.1806 0.1999 0.2122 -0.0312 -0.0218 -0.0074 194 SER B CB  
5715 O OG  . SER B 194 ? 0.1966 0.2109 0.2272 -0.0208 -0.0199 -0.0054 194 SER B OG  
5716 N N   . PRO B 195 ? 0.2467 0.1901 0.2305 -0.0378 -0.0114 0.0012  195 PRO B N   
5717 C CA  . PRO B 195 ? 0.2504 0.1938 0.2337 -0.0404 -0.0138 -0.0036 195 PRO B CA  
5718 C C   . PRO B 195 ? 0.2465 0.1878 0.2253 -0.0343 -0.0145 -0.0067 195 PRO B C   
5719 O O   . PRO B 195 ? 0.2373 0.1828 0.2153 -0.0285 -0.0126 -0.0045 195 PRO B O   
5720 C CB  . PRO B 195 ? 0.2662 0.2237 0.2540 -0.0425 -0.0143 -0.0046 195 PRO B CB  
5721 C CG  . PRO B 195 ? 0.4477 0.4093 0.4383 -0.0429 -0.0114 -0.0001 195 PRO B CG  
5722 C CD  . PRO B 195 ? 0.3628 0.3175 0.3503 -0.0380 -0.0101 0.0026  195 PRO B CD  
5723 N N   . TYR B 196 ? 0.2500 0.1843 0.2257 -0.0359 -0.0167 -0.0120 196 TYR B N   
5724 C CA  . TYR B 196 ? 0.2612 0.1883 0.2313 -0.0300 -0.0164 -0.0149 196 TYR B CA  
5725 C C   . TYR B 196 ? 0.3000 0.2359 0.2665 -0.0226 -0.0147 -0.0142 196 TYR B C   
5726 O O   . TYR B 196 ? 0.2335 0.1666 0.1989 -0.0170 -0.0115 -0.0118 196 TYR B O   
5727 C CB  . TYR B 196 ? 0.2329 0.1527 0.2000 -0.0331 -0.0194 -0.0229 196 TYR B CB  
5728 C CG  . TYR B 196 ? 0.2530 0.1600 0.2152 -0.0279 -0.0182 -0.0257 196 TYR B CG  
5729 C CD1 . TYR B 196 ? 0.2332 0.1440 0.1894 -0.0198 -0.0166 -0.0277 196 TYR B CD1 
5730 C CD2 . TYR B 196 ? 0.2662 0.1574 0.2298 -0.0304 -0.0181 -0.0257 196 TYR B CD2 
5731 C CE1 . TYR B 196 ? 0.2712 0.1717 0.2235 -0.0141 -0.0147 -0.0308 196 TYR B CE1 
5732 C CE2 . TYR B 196 ? 0.2491 0.1284 0.2089 -0.0242 -0.0168 -0.0286 196 TYR B CE2 
5733 C CZ  . TYR B 196 ? 0.2472 0.1321 0.2019 -0.0162 -0.0151 -0.0315 196 TYR B CZ  
5734 O OH  . TYR B 196 ? 0.3178 0.1923 0.2695 -0.0096 -0.0132 -0.0347 196 TYR B OH  
5735 N N   . TYR B 197 ? 0.2261 0.1730 0.1907 -0.0219 -0.0166 -0.0161 197 TYR B N   
5736 C CA  . TYR B 197 ? 0.1928 0.1469 0.1518 -0.0142 -0.0146 -0.0144 197 TYR B CA  
5737 C C   . TYR B 197 ? 0.1912 0.1534 0.1548 -0.0123 -0.0120 -0.0076 197 TYR B C   
5738 O O   . TYR B 197 ? 0.2049 0.1742 0.1642 -0.0065 -0.0109 -0.0052 197 TYR B O   
5739 C CB  . TYR B 197 ? 0.2110 0.1716 0.1622 -0.0123 -0.0188 -0.0210 197 TYR B CB  
5740 C CG  . TYR B 197 ? 0.2275 0.1779 0.1730 -0.0124 -0.0201 -0.0286 197 TYR B CG  
5741 C CD1 . TYR B 197 ? 0.2263 0.1711 0.1658 -0.0056 -0.0158 -0.0281 197 TYR B CD1 
5742 C CD2 . TYR B 197 ? 0.2196 0.1650 0.1675 -0.0198 -0.0248 -0.0361 197 TYR B CD2 
5743 C CE1 . TYR B 197 ? 0.2633 0.1977 0.1978 -0.0047 -0.0164 -0.0355 197 TYR B CE1 
5744 C CE2 . TYR B 197 ? 0.3009 0.2340 0.2441 -0.0197 -0.0255 -0.0436 197 TYR B CE2 
5745 C CZ  . TYR B 197 ? 0.2845 0.2120 0.2206 -0.0116 -0.0215 -0.0434 197 TYR B CZ  
5746 O OH  . TYR B 197 ? 0.3434 0.2583 0.2748 -0.0103 -0.0217 -0.0513 197 TYR B OH  
5747 N N   . HIS B 198 ? 0.2071 0.1676 0.1783 -0.0164 -0.0110 -0.0043 198 HIS B N   
5748 C CA  . HIS B 198 ? 0.2090 0.1748 0.1850 -0.0149 -0.0082 0.0009  198 HIS B CA  
5749 C C   . HIS B 198 ? 0.2794 0.2564 0.2555 -0.0133 -0.0102 0.0010  198 HIS B C   
5750 O O   . HIS B 198 ? 0.2511 0.2319 0.2262 -0.0075 -0.0077 0.0051  198 HIS B O   
5751 C CB  . HIS B 198 ? 0.1863 0.1495 0.1619 -0.0092 -0.0033 0.0051  198 HIS B CB  
5752 C CG  . HIS B 198 ? 0.1979 0.1620 0.1804 -0.0088 0.0002  0.0096  198 HIS B CG  
5753 N ND1 . HIS B 198 ? 0.2506 0.2193 0.2336 -0.0048 0.0025  0.0133  198 HIS B ND1 
5754 C CD2 . HIS B 198 ? 0.2206 0.1811 0.2097 -0.0116 0.0016  0.0105  198 HIS B CD2 
5755 C CE1 . HIS B 198 ? 0.2360 0.2023 0.2263 -0.0057 0.0056  0.0157  198 HIS B CE1 
5756 N NE2 . HIS B 198 ? 0.2189 0.1811 0.2129 -0.0100 0.0048  0.0135  198 HIS B NE2 
5757 N N   . PRO B 199 ? 0.2373 0.2200 0.2155 -0.0181 -0.0145 -0.0032 199 PRO B N   
5758 C CA  . PRO B 199 ? 0.1967 0.1929 0.1772 -0.0162 -0.0170 -0.0035 199 PRO B CA  
5759 C C   . PRO B 199 ? 0.3250 0.3261 0.3138 -0.0173 -0.0146 -0.0001 199 PRO B C   
5760 O O   . PRO B 199 ? 0.3095 0.3039 0.3016 -0.0210 -0.0118 0.0014  199 PRO B O   
5761 C CB  . PRO B 199 ? 0.2695 0.2701 0.2516 -0.0227 -0.0224 -0.0106 199 PRO B CB  
5762 C CG  . PRO B 199 ? 0.2108 0.1995 0.1961 -0.0303 -0.0205 -0.0109 199 PRO B CG  
5763 C CD  . PRO B 199 ? 0.2521 0.2293 0.2328 -0.0261 -0.0166 -0.0071 199 PRO B CD  
5764 N N   . LEU B 200 ? 0.3019 0.3157 0.2938 -0.0136 -0.0163 0.0005  200 LEU B N   
5765 C CA  . LEU B 200 ? 0.2937 0.3144 0.2943 -0.0141 -0.0143 0.0022  200 LEU B CA  
5766 C C   . LEU B 200 ? 0.2969 0.3266 0.3046 -0.0222 -0.0170 -0.0023 200 LEU B C   
5767 O O   . LEU B 200 ? 0.2546 0.2989 0.2672 -0.0219 -0.0209 -0.0050 200 LEU B O   
5768 C CB  . LEU B 200 ? 0.3280 0.3578 0.3295 -0.0050 -0.0142 0.0058  200 LEU B CB  
5769 C CG  . LEU B 200 ? 0.2629 0.2827 0.2592 0.0026  -0.0097 0.0118  200 LEU B CG  
5770 C CD1 . LEU B 200 ? 0.3022 0.3305 0.2993 0.0122  -0.0098 0.0162  200 LEU B CD1 
5771 C CD2 . LEU B 200 ? 0.3179 0.3264 0.3180 0.0000  -0.0043 0.0134  200 LEU B CD2 
5772 N N   . ILE B 201 ? 0.2309 0.2523 0.2399 -0.0295 -0.0147 -0.0028 201 ILE B N   
5773 C CA  . ILE B 201 ? 0.2615 0.2886 0.2772 -0.0385 -0.0157 -0.0059 201 ILE B CA  
5774 C C   . ILE B 201 ? 0.2422 0.2873 0.2684 -0.0384 -0.0151 -0.0063 201 ILE B C   
5775 O O   . ILE B 201 ? 0.2284 0.2856 0.2622 -0.0432 -0.0185 -0.0103 201 ILE B O   
5776 C CB  . ILE B 201 ? 0.2162 0.2305 0.2298 -0.0445 -0.0121 -0.0039 201 ILE B CB  
5777 C CG1 . ILE B 201 ? 0.2518 0.2507 0.2576 -0.0453 -0.0137 -0.0047 201 ILE B CG1 
5778 C CG2 . ILE B 201 ? 0.2185 0.2391 0.2398 -0.0536 -0.0108 -0.0050 201 ILE B CG2 
5779 C CD1 . ILE B 201 ? 0.2473 0.2454 0.2541 -0.0509 -0.0176 -0.0100 201 ILE B CD1 
5780 N N   . PRO B 202 ? 0.2377 0.2861 0.2660 -0.0328 -0.0112 -0.0031 202 PRO B N   
5781 C CA  . PRO B 202 ? 0.1699 0.2366 0.2093 -0.0317 -0.0102 -0.0038 202 PRO B CA  
5782 C C   . PRO B 202 ? 0.2143 0.2981 0.2596 -0.0279 -0.0161 -0.0064 202 PRO B C   
5783 O O   . PRO B 202 ? 0.2106 0.3116 0.2676 -0.0318 -0.0172 -0.0093 202 PRO B O   
5784 C CB  . PRO B 202 ? 0.2243 0.2875 0.2624 -0.0238 -0.0055 -0.0006 202 PRO B CB  
5785 C CG  . PRO B 202 ? 0.1956 0.2402 0.2247 -0.0260 -0.0028 0.0010  202 PRO B CG  
5786 C CD  . PRO B 202 ? 0.2538 0.2896 0.2762 -0.0283 -0.0070 0.0005  202 PRO B CD  
5787 N N   . ILE B 203 ? 0.1972 0.2779 0.2346 -0.0203 -0.0198 -0.0054 203 ILE B N   
5788 C CA  . ILE B 203 ? 0.1873 0.2847 0.2275 -0.0154 -0.0265 -0.0078 203 ILE B CA  
5789 C C   . ILE B 203 ? 0.1786 0.2820 0.2216 -0.0247 -0.0324 -0.0149 203 ILE B C   
5790 O O   . ILE B 203 ? 0.2281 0.3515 0.2816 -0.0264 -0.0373 -0.0193 203 ILE B O   
5791 C CB  . ILE B 203 ? 0.2529 0.3437 0.2811 -0.0043 -0.0278 -0.0035 203 ILE B CB  
5792 C CG1 . ILE B 203 ? 0.2617 0.3482 0.2906 0.0048  -0.0221 0.0031  203 ILE B CG1 
5793 C CG2 . ILE B 203 ? 0.2197 0.3273 0.2468 0.0009  -0.0361 -0.0064 203 ILE B CG2 
5794 C CD1 . ILE B 203 ? 0.2755 0.3516 0.2932 0.0150  -0.0210 0.0092  203 ILE B CD1 
5795 N N   . LEU B 204 ? 0.1999 0.2863 0.2348 -0.0308 -0.0320 -0.0166 204 LEU B N   
5796 C CA  . LEU B 204 ? 0.1791 0.2673 0.2168 -0.0401 -0.0370 -0.0242 204 LEU B CA  
5797 C C   . LEU B 204 ? 0.2708 0.3702 0.3246 -0.0508 -0.0356 -0.0269 204 LEU B C   
5798 O O   . LEU B 204 ? 0.1990 0.3119 0.2623 -0.0571 -0.0411 -0.0339 204 LEU B O   
5799 C CB  . LEU B 204 ? 0.1904 0.2556 0.2174 -0.0440 -0.0351 -0.0245 204 LEU B CB  
5800 C CG  . LEU B 204 ? 0.2377 0.2922 0.2498 -0.0351 -0.0358 -0.0228 204 LEU B CG  
5801 C CD1 . LEU B 204 ? 0.2468 0.2820 0.2519 -0.0400 -0.0347 -0.0252 204 LEU B CD1 
5802 C CD2 . LEU B 204 ? 0.2243 0.2926 0.2320 -0.0286 -0.0430 -0.0270 204 LEU B CD2 
5803 N N   . LEU B 205 ? 0.2415 0.3363 0.2987 -0.0532 -0.0281 -0.0217 205 LEU B N   
5804 C CA  . LEU B 205 ? 0.2376 0.3433 0.3095 -0.0631 -0.0248 -0.0228 205 LEU B CA  
5805 C C   . LEU B 205 ? 0.2332 0.3660 0.3193 -0.0592 -0.0267 -0.0244 205 LEU B C   
5806 O O   . LEU B 205 ? 0.1990 0.3484 0.3005 -0.0675 -0.0282 -0.0289 205 LEU B O   
5807 C CB  . LEU B 205 ? 0.1923 0.2859 0.2610 -0.0655 -0.0160 -0.0166 205 LEU B CB  
5808 C CG  . LEU B 205 ? 0.2386 0.3088 0.2976 -0.0719 -0.0139 -0.0150 205 LEU B CG  
5809 C CD1 . LEU B 205 ? 0.2433 0.3032 0.2955 -0.0701 -0.0067 -0.0084 205 LEU B CD1 
5810 C CD2 . LEU B 205 ? 0.2115 0.2818 0.2797 -0.0851 -0.0142 -0.0185 205 LEU B CD2 
5811 N N   . ASN B 206 ? 0.2364 0.3740 0.3188 -0.0466 -0.0265 -0.0207 206 ASN B N   
5812 C CA  . ASN B 206 ? 0.1976 0.3599 0.2936 -0.0408 -0.0272 -0.0210 206 ASN B CA  
5813 C C   . ASN B 206 ? 0.2144 0.3764 0.3024 -0.0253 -0.0289 -0.0168 206 ASN B C   
5814 O O   . ASN B 206 ? 0.1975 0.3491 0.2804 -0.0190 -0.0226 -0.0117 206 ASN B O   
5815 C CB  . ASN B 206 ? 0.2033 0.3708 0.3090 -0.0447 -0.0182 -0.0185 206 ASN B CB  
5816 C CG  . ASN B 206 ? 0.3153 0.5076 0.4351 -0.0369 -0.0177 -0.0185 206 ASN B CG  
5817 O OD1 . ASN B 206 ? 0.2740 0.4857 0.4020 -0.0323 -0.0252 -0.0217 206 ASN B OD1 
5818 N ND2 . ASN B 206 ? 0.3403 0.5330 0.4627 -0.0343 -0.0091 -0.0154 206 ASN B ND2 
5819 N N   . PRO B 207 ? 0.2723 0.4449 0.3583 -0.0187 -0.0372 -0.0189 207 PRO B N   
5820 C CA  . PRO B 207 ? 0.2896 0.4599 0.3664 -0.0034 -0.0381 -0.0132 207 PRO B CA  
5821 C C   . PRO B 207 ? 0.1970 0.3793 0.2840 0.0058  -0.0341 -0.0093 207 PRO B C   
5822 O O   . PRO B 207 ? 0.2630 0.4350 0.3422 0.0172  -0.0311 -0.0031 207 PRO B O   
5823 C CB  . PRO B 207 ? 0.2905 0.4744 0.3639 0.0010  -0.0486 -0.0169 207 PRO B CB  
5824 C CG  . PRO B 207 ? 0.2859 0.4659 0.3593 -0.0128 -0.0520 -0.0247 207 PRO B CG  
5825 C CD  . PRO B 207 ? 0.2939 0.4763 0.3822 -0.0251 -0.0461 -0.0265 207 PRO B CD  
5826 N N   . ASN B 208 ? 0.2078 0.4106 0.3125 0.0011  -0.0331 -0.0129 208 ASN B N   
5827 C CA  . ASN B 208 ? 0.2309 0.4464 0.3465 0.0102  -0.0285 -0.0102 208 ASN B CA  
5828 C C   . ASN B 208 ? 0.1816 0.3760 0.2904 0.0119  -0.0183 -0.0061 208 ASN B C   
5829 O O   . ASN B 208 ? 0.2449 0.4440 0.3591 0.0218  -0.0140 -0.0037 208 ASN B O   
5830 C CB  . ASN B 208 ? 0.2423 0.4855 0.3798 0.0031  -0.0284 -0.0154 208 ASN B CB  
5831 C CG  . ASN B 208 ? 0.4234 0.6966 0.5736 0.0093  -0.0383 -0.0186 208 ASN B CG  
5832 O OD1 . ASN B 208 ? 0.3510 0.6248 0.4922 0.0138  -0.0473 -0.0192 208 ASN B OD1 
5833 N ND2 . ASN B 208 ? 0.4692 0.7693 0.6407 0.0098  -0.0366 -0.0210 208 ASN B ND2 
5834 N N   . CYS B 209 ? 0.2253 0.3973 0.3227 0.0032  -0.0148 -0.0058 209 CYS B N   
5835 C CA  . CYS B 209 ? 0.2801 0.4331 0.3703 0.0048  -0.0065 -0.0030 209 CYS B CA  
5836 C C   . CYS B 209 ? 0.2358 0.3754 0.3177 0.0177  -0.0056 0.0018  209 CYS B C   
5837 O O   . CYS B 209 ? 0.2729 0.4015 0.3531 0.0214  0.0010  0.0028  209 CYS B O   
5838 C CB  . CYS B 209 ? 0.2052 0.3387 0.2850 -0.0064 -0.0043 -0.0035 209 CYS B CB  
5839 S SG  . CYS B 209 ? 0.2827 0.3950 0.3462 -0.0061 -0.0089 -0.0014 209 CYS B SG  
5840 N N   . VAL B 210 ? 0.2284 0.3688 0.3050 0.0248  -0.0117 0.0046  210 VAL B N   
5841 C CA  . VAL B 210 ? 0.1965 0.3238 0.2658 0.0373  -0.0098 0.0108  210 VAL B CA  
5842 C C   . VAL B 210 ? 0.2513 0.3877 0.3307 0.0486  -0.0063 0.0123  210 VAL B C   
5843 O O   . VAL B 210 ? 0.2808 0.4015 0.3563 0.0572  -0.0016 0.0166  210 VAL B O   
5844 C CB  . VAL B 210 ? 0.2216 0.3505 0.2820 0.0433  -0.0168 0.0143  210 VAL B CB  
5845 C CG1 . VAL B 210 ? 0.2729 0.3918 0.3232 0.0329  -0.0195 0.0117  210 VAL B CG1 
5846 C CG2 . VAL B 210 ? 0.3314 0.4879 0.4010 0.0489  -0.0244 0.0126  210 VAL B CG2 
5847 N N   . TYR B 211 ? 0.2090 0.3706 0.3027 0.0488  -0.0084 0.0088  211 TYR B N   
5848 C CA  . TYR B 211 ? 0.2551 0.4278 0.3600 0.0604  -0.0049 0.0097  211 TYR B CA  
5849 C C   . TYR B 211 ? 0.2236 0.3849 0.3302 0.0583  0.0048  0.0070  211 TYR B C   
5850 O O   . TYR B 211 ? 0.2422 0.4058 0.3554 0.0693  0.0092  0.0077  211 TYR B O   
5851 C CB  . TYR B 211 ? 0.2874 0.4936 0.4094 0.0607  -0.0098 0.0060  211 TYR B CB  
5852 C CG  . TYR B 211 ? 0.3147 0.5361 0.4359 0.0640  -0.0208 0.0071  211 TYR B CG  
5853 C CD1 . TYR B 211 ? 0.3390 0.5541 0.4507 0.0781  -0.0245 0.0140  211 TYR B CD1 
5854 C CD2 . TYR B 211 ? 0.2889 0.5304 0.4183 0.0530  -0.0272 0.0010  211 TYR B CD2 
5855 C CE1 . TYR B 211 ? 0.3340 0.5640 0.4424 0.0819  -0.0350 0.0147  211 TYR B CE1 
5856 C CE2 . TYR B 211 ? 0.3565 0.6126 0.4842 0.0559  -0.0382 0.0001  211 TYR B CE2 
5857 C CZ  . TYR B 211 ? 0.2943 0.5455 0.4107 0.0709  -0.0423 0.0069  211 TYR B CZ  
5858 O OH  . TYR B 211 ? 0.3230 0.5896 0.4353 0.0749  -0.0535 0.0060  211 TYR B OH  
5859 N N   . GLU B 212 ? 0.2246 0.3739 0.3247 0.0455  0.0081  0.0039  212 GLU B N   
5860 C CA  . GLU B 212 ? 0.2245 0.3653 0.3245 0.0436  0.0166  0.0005  212 GLU B CA  
5861 C C   . GLU B 212 ? 0.3061 0.4239 0.3992 0.0527  0.0209  0.0025  212 GLU B C   
5862 O O   . GLU B 212 ? 0.3217 0.4375 0.4185 0.0578  0.0273  -0.0008 212 GLU B O   
5863 C CB  . GLU B 212 ? 0.2493 0.3826 0.3421 0.0287  0.0181  -0.0022 212 GLU B CB  
5864 C CG  . GLU B 212 ? 0.2952 0.4512 0.3985 0.0196  0.0176  -0.0049 212 GLU B CG  
5865 C CD  . GLU B 212 ? 0.3433 0.4906 0.4389 0.0053  0.0178  -0.0056 212 GLU B CD  
5866 O OE1 . GLU B 212 ? 0.3837 0.5438 0.4859 -0.0033 0.0146  -0.0065 212 GLU B OE1 
5867 O OE2 . GLU B 212 ? 0.2926 0.4203 0.3763 0.0027  0.0209  -0.0055 212 GLU B OE2 
5868 N N   . THR B 213 ? 0.3096 0.4099 0.3931 0.0547  0.0180  0.0073  213 THR B N   
5869 C CA  . THR B 213 ? 0.3746 0.4517 0.4531 0.0618  0.0224  0.0096  213 THR B CA  
5870 C C   . THR B 213 ? 0.4468 0.5214 0.5261 0.0755  0.0207  0.0172  213 THR B C   
5871 O O   . THR B 213 ? 0.4878 0.5456 0.5672 0.0837  0.0257  0.0192  213 THR B O   
5872 C CB  . THR B 213 ? 0.3794 0.4351 0.4466 0.0528  0.0226  0.0100  213 THR B CB  
5873 O OG1 . THR B 213 ? 0.4489 0.5076 0.5105 0.0496  0.0165  0.0143  213 THR B OG1 
5874 C CG2 . THR B 213 ? 0.3621 0.4170 0.4268 0.0414  0.0248  0.0033  213 THR B CG2 
5875 N N   . THR B 214 ? 0.3887 0.4782 0.4677 0.0782  0.0137  0.0215  214 THR B N   
5876 C CA  . THR B 214 ? 0.3151 0.4050 0.3931 0.0926  0.0112  0.0298  214 THR B CA  
5877 C C   . THR B 214 ? 0.3845 0.5056 0.4724 0.0978  0.0046  0.0290  214 THR B C   
5878 O O   . THR B 214 ? 0.3009 0.4351 0.3853 0.0956  -0.0032 0.0301  214 THR B O   
5879 C CB  . THR B 214 ? 0.3023 0.3782 0.3666 0.0914  0.0086  0.0364  214 THR B CB  
5880 O OG1 . THR B 214 ? 0.3183 0.4079 0.3789 0.0819  0.0017  0.0334  214 THR B OG1 
5881 C CG2 . THR B 214 ? 0.2538 0.3016 0.3116 0.0848  0.0153  0.0364  214 THR B CG2 
5882 N N   . PRO B 215 ? 0.4060 0.5409 0.5072 0.1049  0.0074  0.0262  215 PRO B N   
5883 C CA  . PRO B 215 ? 0.3944 0.5629 0.5088 0.1085  0.0011  0.0241  215 PRO B CA  
5884 C C   . PRO B 215 ? 0.3603 0.5401 0.4736 0.1226  -0.0065 0.0315  215 PRO B C   
5885 O O   . PRO B 215 ? 0.4122 0.6214 0.5348 0.1233  -0.0143 0.0291  215 PRO B O   
5886 C CB  . PRO B 215 ? 0.4162 0.5935 0.5448 0.1143  0.0080  0.0197  215 PRO B CB  
5887 C CG  . PRO B 215 ? 0.4292 0.5754 0.5504 0.1204  0.0162  0.0220  215 PRO B CG  
5888 C CD  . PRO B 215 ? 0.4421 0.5640 0.5480 0.1088  0.0165  0.0231  215 PRO B CD  
5889 N N   . ASN B 216 ? 0.3441 0.5027 0.4467 0.1339  -0.0046 0.0406  216 ASN B N   
5890 C CA  . ASN B 216 ? 0.3862 0.5547 0.4851 0.1492  -0.0114 0.0494  216 ASN B CA  
5891 C C   . ASN B 216 ? 0.3621 0.5251 0.4440 0.1451  -0.0175 0.0536  216 ASN B C   
5892 O O   . ASN B 216 ? 0.4109 0.5762 0.4841 0.1563  -0.0222 0.0615  216 ASN B O   
5893 C CB  . ASN B 216 ? 0.4769 0.6235 0.5731 0.1637  -0.0049 0.0576  216 ASN B CB  
5894 C CG  . ASN B 216 ? 0.5989 0.7488 0.7104 0.1679  0.0011  0.0521  216 ASN B CG  
5895 O OD1 . ASN B 216 ? 0.5307 0.7083 0.6565 0.1656  -0.0017 0.0449  216 ASN B OD1 
5896 N ND2 . ASN B 216 ? 0.7084 0.8299 0.8174 0.1731  0.0099  0.0547  216 ASN B ND2 
5897 N N   . VAL B 217 ? 0.3825 0.5367 0.4578 0.1283  -0.0169 0.0480  217 VAL B N   
5898 C CA  . VAL B 217 ? 0.3806 0.5292 0.4397 0.1243  -0.0217 0.0508  217 VAL B CA  
5899 C C   . VAL B 217 ? 0.3848 0.5643 0.4458 0.1259  -0.0338 0.0475  217 VAL B C   
5900 O O   . VAL B 217 ? 0.4138 0.6187 0.4909 0.1226  -0.0381 0.0400  217 VAL B O   
5901 C CB  . VAL B 217 ? 0.3729 0.5053 0.4267 0.1065  -0.0180 0.0448  217 VAL B CB  
5902 C CG1 . VAL B 217 ? 0.4239 0.5751 0.4891 0.0930  -0.0213 0.0338  217 VAL B CG1 
5903 C CG2 . VAL B 217 ? 0.3734 0.4957 0.4098 0.1040  -0.0207 0.0485  217 VAL B CG2 
5904 N N   . LYS B 218 ? 0.3189 0.4974 0.3639 0.1313  -0.0393 0.0528  218 LYS B N   
5905 C CA  . LYS B 218 ? 0.3336 0.5391 0.3770 0.1308  -0.0516 0.0478  218 LYS B CA  
5906 C C   . LYS B 218 ? 0.3876 0.5836 0.4193 0.1162  -0.0531 0.0418  218 LYS B C   
5907 O O   . LYS B 218 ? 0.4439 0.6158 0.4599 0.1160  -0.0475 0.0477  218 LYS B O   
5908 C CB  . LYS B 218 ? 0.3690 0.5755 0.3994 0.1440  -0.0555 0.0553  218 LYS B CB  
5909 C CG  . LYS B 218 ? 0.4700 0.6927 0.5131 0.1532  -0.0579 0.0557  218 LYS B CG  
5910 C CD  . LYS B 218 ? 0.5393 0.7763 0.5724 0.1601  -0.0670 0.0567  218 LYS B CD  
5911 C CE  . LYS B 218 ? 0.6265 0.8647 0.6628 0.1749  -0.0656 0.0644  218 LYS B CE  
5912 N NZ  . LYS B 218 ? 0.6358 0.8693 0.6900 0.1762  -0.0580 0.0644  218 LYS B NZ  
5913 N N   . ILE B 219 ? 0.4449 0.6594 0.4856 0.1038  -0.0598 0.0302  219 ILE B N   
5914 C CA  . ILE B 219 ? 0.4275 0.6324 0.4587 0.0899  -0.0611 0.0235  219 ILE B CA  
5915 C C   . ILE B 219 ? 0.3390 0.5696 0.3702 0.0878  -0.0741 0.0148  219 ILE B C   
5916 O O   . ILE B 219 ? 0.3695 0.6279 0.4133 0.0935  -0.0818 0.0121  219 ILE B O   
5917 C CB  . ILE B 219 ? 0.4227 0.6171 0.4646 0.0732  -0.0544 0.0168  219 ILE B CB  
5918 C CG1 . ILE B 219 ? 0.3187 0.5377 0.3827 0.0676  -0.0572 0.0094  219 ILE B CG1 
5919 C CG2 . ILE B 219 ? 0.4491 0.6168 0.4882 0.0746  -0.0426 0.0238  219 ILE B CG2 
5920 C CD1 . ILE B 219 ? 0.3232 0.5347 0.3953 0.0504  -0.0521 0.0027  219 ILE B CD1 
5921 N N   . PRO B 220 ? 0.3604 0.5831 0.3783 0.0801  -0.0770 0.0096  220 PRO B N   
5922 C CA  . PRO B 220 ? 0.4304 0.6761 0.4474 0.0774  -0.0898 -0.0006 220 PRO B CA  
5923 C C   . PRO B 220 ? 0.4085 0.6737 0.4490 0.0635  -0.0940 -0.0125 220 PRO B C   
5924 O O   . PRO B 220 ? 0.3904 0.6498 0.4457 0.0548  -0.0863 -0.0129 220 PRO B O   
5925 C CB  . PRO B 220 ? 0.4277 0.6540 0.4251 0.0714  -0.0889 -0.0036 220 PRO B CB  
5926 C CG  . PRO B 220 ? 0.4475 0.6445 0.4428 0.0660  -0.0761 0.0023  220 PRO B CG  
5927 C CD  . PRO B 220 ? 0.4140 0.6073 0.4154 0.0762  -0.0693 0.0133  220 PRO B CD  
5928 N N   . ASP B 221 ? 0.3641 0.6432 0.4061 0.0593  -0.1027 -0.0217 221 ASP B N   
5929 C CA  . ASP B 221 ? 0.3392 0.6337 0.4023 0.0445  -0.1064 -0.0334 221 ASP B CA  
5930 C C   . ASP B 221 ? 0.3240 0.6044 0.3841 0.0284  -0.1058 -0.0422 221 ASP B C   
5931 O O   . ASP B 221 ? 0.3854 0.6583 0.4303 0.0270  -0.1106 -0.0475 221 ASP B O   
5932 C CB  . ASP B 221 ? 0.3643 0.6781 0.4295 0.0478  -0.1161 -0.0389 221 ASP B CB  
5933 C CG  . ASP B 221 ? 0.4341 0.7656 0.5239 0.0341  -0.1194 -0.0492 221 ASP B CG  
5934 O OD1 . ASP B 221 ? 0.4341 0.7664 0.5416 0.0251  -0.1128 -0.0494 221 ASP B OD1 
5935 O OD2 . ASP B 221 ? 0.4225 0.7674 0.5141 0.0323  -0.1282 -0.0569 221 ASP B OD2 
5936 N N   . PHE B 222 ? 0.2465 0.5224 0.3208 0.0165  -0.0993 -0.0437 222 PHE B N   
5937 C CA  . PHE B 222 ? 0.2829 0.5418 0.3554 0.0006  -0.0972 -0.0510 222 PHE B CA  
5938 C C   . PHE B 222 ? 0.3366 0.6054 0.4254 -0.0134 -0.1015 -0.0620 222 PHE B C   
5939 O O   . PHE B 222 ? 0.3374 0.6077 0.4443 -0.0258 -0.0965 -0.0641 222 PHE B O   
5940 C CB  . PHE B 222 ? 0.2758 0.5112 0.3506 -0.0055 -0.0839 -0.0440 222 PHE B CB  
5941 C CG  . PHE B 222 ? 0.2618 0.4724 0.3172 0.0043  -0.0767 -0.0336 222 PHE B CG  
5942 C CD1 . PHE B 222 ? 0.2998 0.5129 0.3521 0.0190  -0.0738 -0.0237 222 PHE B CD1 
5943 C CD2 . PHE B 222 ? 0.1725 0.3567 0.2139 -0.0012 -0.0723 -0.0336 222 PHE B CD2 
5944 C CE1 . PHE B 222 ? 0.2737 0.4631 0.3100 0.0267  -0.0665 -0.0142 222 PHE B CE1 
5945 C CE2 . PHE B 222 ? 0.2458 0.4092 0.2719 0.0070  -0.0655 -0.0245 222 PHE B CE2 
5946 C CZ  . PHE B 222 ? 0.2881 0.4539 0.3121 0.0201  -0.0625 -0.0149 222 PHE B CZ  
5947 N N   . ALA B 223 ? 0.3477 0.6218 0.4288 -0.0112 -0.1102 -0.0684 223 ALA B N   
5948 C CA  . ALA B 223 ? 0.3958 0.6790 0.4909 -0.0231 -0.1156 -0.0789 223 ALA B CA  
5949 C C   . ALA B 223 ? 0.3880 0.6500 0.4815 -0.0385 -0.1136 -0.0865 223 ALA B C   
5950 O O   . ALA B 223 ? 0.4221 0.6865 0.5210 -0.0471 -0.1192 -0.0960 223 ALA B O   
5951 C CB  . ALA B 223 ? 0.4024 0.7000 0.4892 -0.0142 -0.1262 -0.0832 223 ALA B CB  
5952 N N   . VAL B 224 ? 0.3197 0.5607 0.4058 -0.0418 -0.1059 -0.0825 224 VAL B N   
5953 C CA  . VAL B 224 ? 0.3408 0.5587 0.4250 -0.0553 -0.1027 -0.0881 224 VAL B CA  
5954 C C   . VAL B 224 ? 0.2638 0.4677 0.3512 -0.0601 -0.0921 -0.0809 224 VAL B C   
5955 O O   . VAL B 224 ? 0.3066 0.5142 0.3895 -0.0509 -0.0885 -0.0728 224 VAL B O   
5956 C CB  . VAL B 224 ? 0.4676 0.6699 0.5286 -0.0508 -0.1069 -0.0932 224 VAL B CB  
5957 C CG1 . VAL B 224 ? 0.3981 0.5909 0.4405 -0.0390 -0.1030 -0.0852 224 VAL B CG1 
5958 C CG2 . VAL B 224 ? 0.4615 0.6412 0.5231 -0.0645 -0.1049 -0.1005 224 VAL B CG2 
5959 N N   . SER B 225 ? 0.2828 0.4703 0.3779 -0.0743 -0.0869 -0.0832 225 SER B N   
5960 C CA  . SER B 225 ? 0.2418 0.4156 0.3400 -0.0800 -0.0764 -0.0759 225 SER B CA  
5961 C C   . SER B 225 ? 0.2347 0.3804 0.3131 -0.0780 -0.0729 -0.0739 225 SER B C   
5962 O O   . SER B 225 ? 0.3047 0.4373 0.3753 -0.0819 -0.0767 -0.0817 225 SER B O   
5963 C CB  . SER B 225 ? 0.2896 0.4573 0.4046 -0.0945 -0.0708 -0.0762 225 SER B CB  
5964 O OG  . SER B 225 ? 0.3156 0.4625 0.4272 -0.0999 -0.0609 -0.0694 225 SER B OG  
5965 N N   . PHE B 226 ? 0.2346 0.3681 0.3042 -0.0704 -0.0648 -0.0623 226 PHE B N   
5966 C CA  . PHE B 226 ? 0.2175 0.3228 0.2704 -0.0678 -0.0595 -0.0577 226 PHE B CA  
5967 C C   . PHE B 226 ? 0.2276 0.3163 0.2854 -0.0767 -0.0505 -0.0521 226 PHE B C   
5968 O O   . PHE B 226 ? 0.2915 0.3592 0.3373 -0.0735 -0.0454 -0.0465 226 PHE B O   
5969 C CB  . PHE B 226 ? 0.2673 0.3701 0.3063 -0.0529 -0.0573 -0.0492 226 PHE B CB  
5970 C CG  . PHE B 226 ? 0.2854 0.3972 0.3127 -0.0427 -0.0649 -0.0530 226 PHE B CG  
5971 C CD1 . PHE B 226 ? 0.2901 0.3880 0.3026 -0.0413 -0.0672 -0.0579 226 PHE B CD1 
5972 C CD2 . PHE B 226 ? 0.3095 0.4437 0.3398 -0.0337 -0.0694 -0.0513 226 PHE B CD2 
5973 C CE1 . PHE B 226 ? 0.3403 0.4470 0.3397 -0.0313 -0.0735 -0.0610 226 PHE B CE1 
5974 C CE2 . PHE B 226 ? 0.3055 0.4482 0.3228 -0.0234 -0.0764 -0.0536 226 PHE B CE2 
5975 C CZ  . PHE B 226 ? 0.3017 0.4308 0.3029 -0.0225 -0.0783 -0.0585 226 PHE B CZ  
5976 N N   . ARG B 227 ? 0.2587 0.3571 0.3338 -0.0875 -0.0481 -0.0531 227 ARG B N   
5977 C CA  . ARG B 227 ? 0.2482 0.3323 0.3255 -0.0941 -0.0387 -0.0457 227 ARG B CA  
5978 C C   . ARG B 227 ? 0.2410 0.2984 0.3107 -0.1007 -0.0370 -0.0469 227 ARG B C   
5979 O O   . ARG B 227 ? 0.2597 0.2987 0.3206 -0.0991 -0.0307 -0.0392 227 ARG B O   
5980 C CB  . ARG B 227 ? 0.3699 0.4720 0.4676 -0.1039 -0.0354 -0.0458 227 ARG B CB  
5981 C CG  . ARG B 227 ? 0.3279 0.4570 0.4344 -0.0961 -0.0363 -0.0441 227 ARG B CG  
5982 C CD  . ARG B 227 ? 0.3790 0.5279 0.5072 -0.1057 -0.0318 -0.0442 227 ARG B CD  
5983 N NE  . ARG B 227 ? 0.4199 0.5548 0.5470 -0.1119 -0.0209 -0.0362 227 ARG B NE  
5984 C CZ  . ARG B 227 ? 0.4042 0.5386 0.5260 -0.1049 -0.0137 -0.0283 227 ARG B CZ  
5985 N NH1 . ARG B 227 ? 0.4067 0.5518 0.5250 -0.0918 -0.0157 -0.0270 227 ARG B NH1 
5986 N NH2 . ARG B 227 ? 0.5289 0.6513 0.6480 -0.1106 -0.0045 -0.0217 227 ARG B NH2 
5987 N N   . GLU B 228 ? 0.2915 0.3463 0.3644 -0.1075 -0.0428 -0.0570 228 GLU B N   
5988 C CA  . GLU B 228 ? 0.3759 0.4033 0.4416 -0.1119 -0.0411 -0.0582 228 GLU B CA  
5989 C C   . GLU B 228 ? 0.3311 0.3425 0.3775 -0.1008 -0.0410 -0.0557 228 GLU B C   
5990 O O   . GLU B 228 ? 0.2662 0.2556 0.3054 -0.1008 -0.0360 -0.0504 228 GLU B O   
5991 C CB  . GLU B 228 ? 0.4037 0.4294 0.4757 -0.1165 -0.0476 -0.0681 228 GLU B CB  
5992 C CG  . GLU B 228 ? 0.6276 0.6554 0.7174 -0.1270 -0.0450 -0.0665 228 GLU B CG  
5993 C CD  . GLU B 228 ? 0.7819 0.7947 0.8740 -0.1333 -0.0494 -0.0739 228 GLU B CD  
5994 O OE1 . GLU B 228 ? 0.8175 0.8259 0.8988 -0.1292 -0.0563 -0.0828 228 GLU B OE1 
5995 O OE2 . GLU B 228 ? 0.8493 0.8547 0.9530 -0.1425 -0.0456 -0.0706 228 GLU B OE2 
5996 N N   . ASP B 229 ? 0.2581 0.2808 0.2962 -0.0900 -0.0461 -0.0582 229 ASP B N   
5997 C CA  . ASP B 229 ? 0.2539 0.2630 0.2750 -0.0789 -0.0446 -0.0545 229 ASP B CA  
5998 C C   . ASP B 229 ? 0.1980 0.1995 0.2161 -0.0748 -0.0371 -0.0426 229 ASP B C   
5999 O O   . ASP B 229 ? 0.2662 0.2502 0.2749 -0.0708 -0.0340 -0.0389 229 ASP B O   
6000 C CB  . ASP B 229 ? 0.2248 0.2485 0.2375 -0.0681 -0.0501 -0.0573 229 ASP B CB  
6001 C CG  . ASP B 229 ? 0.3419 0.3680 0.3507 -0.0694 -0.0578 -0.0699 229 ASP B CG  
6002 O OD1 . ASP B 229 ? 0.3842 0.3985 0.3974 -0.0790 -0.0588 -0.0773 229 ASP B OD1 
6003 O OD2 . ASP B 229 ? 0.3108 0.3501 0.3113 -0.0604 -0.0629 -0.0725 229 ASP B OD2 
6004 N N   . ALA B 230 ? 0.2593 0.2748 0.2857 -0.0753 -0.0344 -0.0372 230 ALA B N   
6005 C CA  . ALA B 230 ? 0.2085 0.2175 0.2315 -0.0715 -0.0279 -0.0277 230 ALA B CA  
6006 C C   . ALA B 230 ? 0.2669 0.2567 0.2886 -0.0781 -0.0234 -0.0242 230 ALA B C   
6007 O O   . ALA B 230 ? 0.2266 0.2031 0.2396 -0.0732 -0.0206 -0.0191 230 ALA B O   
6008 C CB  . ALA B 230 ? 0.2396 0.2667 0.2721 -0.0713 -0.0254 -0.0240 230 ALA B CB  
6009 N N   . SER B 231 ? 0.2821 0.2703 0.3128 -0.0892 -0.0229 -0.0269 231 SER B N   
6010 C CA  . SER B 231 ? 0.2960 0.2641 0.3249 -0.0953 -0.0185 -0.0228 231 SER B CA  
6011 C C   . SER B 231 ? 0.2781 0.2260 0.2968 -0.0914 -0.0207 -0.0256 231 SER B C   
6012 O O   . SER B 231 ? 0.3260 0.2574 0.3376 -0.0888 -0.0173 -0.0194 231 SER B O   
6013 C CB  . SER B 231 ? 0.3287 0.2991 0.3709 -0.1086 -0.0171 -0.0254 231 SER B CB  
6014 O OG  . SER B 231 ? 0.5481 0.4990 0.5889 -0.1110 -0.0120 -0.0194 231 SER B OG  
6015 N N   . LYS B 232 ? 0.2429 0.1933 0.2602 -0.0898 -0.0265 -0.0351 232 LYS B N   
6016 C CA  . LYS B 232 ? 0.2629 0.1955 0.2705 -0.0853 -0.0282 -0.0392 232 LYS B CA  
6017 C C   . LYS B 232 ? 0.3010 0.2295 0.2979 -0.0736 -0.0261 -0.0332 232 LYS B C   
6018 O O   . LYS B 232 ? 0.3060 0.2171 0.2968 -0.0703 -0.0243 -0.0312 232 LYS B O   
6019 C CB  . LYS B 232 ? 0.3148 0.2543 0.3214 -0.0850 -0.0349 -0.0514 232 LYS B CB  
6020 C CG  . LYS B 232 ? 0.4311 0.3643 0.4465 -0.0967 -0.0376 -0.0607 232 LYS B CG  
6021 C CD  . LYS B 232 ? 0.4682 0.4006 0.4773 -0.0941 -0.0443 -0.0741 232 LYS B CD  
6022 C CE  . LYS B 232 ? 0.5693 0.4763 0.5678 -0.0893 -0.0422 -0.0759 232 LYS B CE  
6023 N NZ  . LYS B 232 ? 0.6849 0.5876 0.6789 -0.0883 -0.0481 -0.0902 232 LYS B NZ  
6024 N N   . HIS B 233 ? 0.2370 0.1815 0.2324 -0.0670 -0.0264 -0.0304 233 HIS B N   
6025 C CA  . HIS B 233 ? 0.2456 0.1867 0.2335 -0.0575 -0.0238 -0.0246 233 HIS B CA  
6026 C C   . HIS B 233 ? 0.2783 0.2079 0.2661 -0.0587 -0.0195 -0.0168 233 HIS B C   
6027 O O   . HIS B 233 ? 0.2464 0.1661 0.2288 -0.0529 -0.0182 -0.0141 233 HIS B O   
6028 C CB  . HIS B 233 ? 0.2640 0.2218 0.2524 -0.0518 -0.0235 -0.0214 233 HIS B CB  
6029 C CG  . HIS B 233 ? 0.2733 0.2413 0.2575 -0.0463 -0.0272 -0.0264 233 HIS B CG  
6030 N ND1 . HIS B 233 ? 0.2377 0.2024 0.2128 -0.0376 -0.0264 -0.0259 233 HIS B ND1 
6031 C CD2 . HIS B 233 ? 0.1924 0.1756 0.1799 -0.0475 -0.0317 -0.0312 233 HIS B CD2 
6032 C CE1 . HIS B 233 ? 0.2542 0.2303 0.2252 -0.0334 -0.0299 -0.0298 233 HIS B CE1 
6033 N NE2 . HIS B 233 ? 0.2681 0.2559 0.2464 -0.0390 -0.0338 -0.0333 233 HIS B NE2 
6034 N N   . VAL B 234 ? 0.2549 0.1874 0.2485 -0.0656 -0.0174 -0.0130 234 VAL B N   
6035 C CA  . VAL B 234 ? 0.2475 0.1712 0.2389 -0.0658 -0.0136 -0.0051 234 VAL B CA  
6036 C C   . VAL B 234 ? 0.2749 0.1784 0.2634 -0.0683 -0.0130 -0.0042 234 VAL B C   
6037 O O   . VAL B 234 ? 0.3110 0.2042 0.2939 -0.0629 -0.0121 0.0004  234 VAL B O   
6038 C CB  . VAL B 234 ? 0.2277 0.1617 0.2245 -0.0715 -0.0104 -0.0009 234 VAL B CB  
6039 C CG1 . VAL B 234 ? 0.2277 0.1526 0.2193 -0.0713 -0.0067 0.0074  234 VAL B CG1 
6040 C CG2 . VAL B 234 ? 0.2008 0.1526 0.1999 -0.0669 -0.0106 -0.0014 234 VAL B CG2 
6041 N N   . GLU B 235 ? 0.2273 0.1250 0.2205 -0.0762 -0.0139 -0.0090 235 GLU B N   
6042 C CA  . GLU B 235 ? 0.3182 0.1938 0.3096 -0.0790 -0.0127 -0.0081 235 GLU B CA  
6043 C C   . GLU B 235 ? 0.3138 0.1780 0.2985 -0.0704 -0.0149 -0.0121 235 GLU B C   
6044 O O   . GLU B 235 ? 0.3660 0.2141 0.3464 -0.0664 -0.0134 -0.0073 235 GLU B O   
6045 C CB  . GLU B 235 ? 0.3223 0.1980 0.3243 -0.0879 -0.0124 -0.0137 235 GLU B CB  
6046 C CG  . GLU B 235 ? 0.5293 0.3860 0.5341 -0.0888 -0.0091 -0.0107 235 GLU B CG  
6047 C CD  . GLU B 235 ? 0.7064 0.5557 0.7061 -0.0855 -0.0042 0.0020  235 GLU B CD  
6048 O OE1 . GLU B 235 ? 0.7005 0.5607 0.7013 -0.0887 -0.0012 0.0084  235 GLU B OE1 
6049 O OE2 . GLU B 235 ? 0.6536 0.4868 0.6474 -0.0792 -0.0036 0.0054  235 GLU B OE2 
6050 N N   . LEU B 236 ? 0.2783 0.1517 0.2616 -0.0662 -0.0182 -0.0201 236 LEU B N   
6051 C CA  . LEU B 236 ? 0.3526 0.2174 0.3292 -0.0572 -0.0192 -0.0238 236 LEU B CA  
6052 C C   . LEU B 236 ? 0.2624 0.1291 0.2355 -0.0483 -0.0171 -0.0161 236 LEU B C   
6053 O O   . LEU B 236 ? 0.3093 0.1642 0.2792 -0.0419 -0.0164 -0.0153 236 LEU B O   
6054 C CB  . LEU B 236 ? 0.3147 0.1909 0.2888 -0.0545 -0.0225 -0.0333 236 LEU B CB  
6055 C CG  . LEU B 236 ? 0.3622 0.2345 0.3391 -0.0623 -0.0260 -0.0438 236 LEU B CG  
6056 C CD1 . LEU B 236 ? 0.3462 0.2345 0.3192 -0.0588 -0.0302 -0.0523 236 LEU B CD1 
6057 C CD2 . LEU B 236 ? 0.3686 0.2171 0.3430 -0.0622 -0.0254 -0.0484 236 LEU B CD2 
6058 N N   . ALA B 237 ? 0.2391 0.1209 0.2138 -0.0476 -0.0163 -0.0111 237 ALA B N   
6059 C CA  . ALA B 237 ? 0.2951 0.1797 0.2684 -0.0409 -0.0148 -0.0048 237 ALA B CA  
6060 C C   . ALA B 237 ? 0.2597 0.1314 0.2316 -0.0408 -0.0139 0.0019  237 ALA B C   
6061 O O   . ALA B 237 ? 0.2644 0.1321 0.2347 -0.0335 -0.0139 0.0046  237 ALA B O   
6062 C CB  . ALA B 237 ? 0.1953 0.0962 0.1712 -0.0416 -0.0141 -0.0017 237 ALA B CB  
6063 N N   . LYS B 238 ? 0.3017 0.1678 0.2745 -0.0484 -0.0127 0.0051  238 LYS B N   
6064 C CA  . LYS B 238 ? 0.2950 0.1478 0.2644 -0.0477 -0.0114 0.0129  238 LYS B CA  
6065 C C   . LYS B 238 ? 0.3416 0.1757 0.3090 -0.0430 -0.0120 0.0114  238 LYS B C   
6066 O O   . LYS B 238 ? 0.3168 0.1438 0.2810 -0.0360 -0.0123 0.0171  238 LYS B O   
6067 C CB  . LYS B 238 ? 0.2879 0.1375 0.2585 -0.0574 -0.0086 0.0173  238 LYS B CB  
6068 C CG  . LYS B 238 ? 0.2969 0.1648 0.2688 -0.0603 -0.0071 0.0199  238 LYS B CG  
6069 C CD  . LYS B 238 ? 0.3692 0.2364 0.3441 -0.0704 -0.0032 0.0234  238 LYS B CD  
6070 C CE  . LYS B 238 ? 0.4770 0.3296 0.4485 -0.0696 0.0001  0.0315  238 LYS B CE  
6071 N NZ  . LYS B 238 ? 0.4513 0.3078 0.4279 -0.0777 0.0055  0.0354  238 LYS B NZ  
6072 N N   . GLU B 239 ? 0.2794 0.1061 0.2486 -0.0460 -0.0126 0.0031  239 GLU B N   
6073 C CA  . GLU B 239 ? 0.2981 0.1058 0.2654 -0.0410 -0.0127 0.0001  239 GLU B CA  
6074 C C   . GLU B 239 ? 0.3350 0.1476 0.3005 -0.0293 -0.0136 -0.0015 239 GLU B C   
6075 O O   . GLU B 239 ? 0.3328 0.1332 0.2970 -0.0219 -0.0133 0.0015  239 GLU B O   
6076 C CB  . GLU B 239 ? 0.3347 0.1379 0.3059 -0.0467 -0.0129 -0.0104 239 GLU B CB  
6077 C CG  . GLU B 239 ? 0.5162 0.3208 0.4953 -0.0572 -0.0106 -0.0086 239 GLU B CG  
6078 C CD  . GLU B 239 ? 0.6926 0.4983 0.6779 -0.0643 -0.0123 -0.0202 239 GLU B CD  
6079 O OE1 . GLU B 239 ? 0.8016 0.6147 0.7953 -0.0736 -0.0114 -0.0200 239 GLU B OE1 
6080 O OE2 . GLU B 239 ? 0.7054 0.5055 0.6875 -0.0605 -0.0147 -0.0299 239 GLU B OE2 
6081 N N   . LYS B 240 ? 0.2973 0.1279 0.2636 -0.0271 -0.0142 -0.0055 240 LYS B N   
6082 C CA  . LYS B 240 ? 0.3650 0.2021 0.3314 -0.0169 -0.0138 -0.0064 240 LYS B CA  
6083 C C   . LYS B 240 ? 0.3706 0.2123 0.3390 -0.0121 -0.0141 0.0024  240 LYS B C   
6084 O O   . LYS B 240 ? 0.2955 0.1349 0.2655 -0.0034 -0.0140 0.0035  240 LYS B O   
6085 C CB  . LYS B 240 ? 0.3124 0.1669 0.2790 -0.0163 -0.0135 -0.0109 240 LYS B CB  
6086 C CG  . LYS B 240 ? 0.3525 0.2132 0.3198 -0.0065 -0.0115 -0.0123 240 LYS B CG  
6087 C CD  . LYS B 240 ? 0.3681 0.2172 0.3313 -0.0017 -0.0106 -0.0202 240 LYS B CD  
6088 C CE  . LYS B 240 ? 0.4122 0.2669 0.3772 0.0088  -0.0075 -0.0206 240 LYS B CE  
6089 N NZ  . LYS B 240 ? 0.3891 0.2325 0.3492 0.0147  -0.0059 -0.0292 240 LYS B NZ  
6090 N N   . TYR B 241 ? 0.2886 0.1389 0.2574 -0.0172 -0.0146 0.0078  241 TYR B N   
6091 C CA  . TYR B 241 ? 0.3115 0.1668 0.2809 -0.0131 -0.0158 0.0150  241 TYR B CA  
6092 C C   . TYR B 241 ? 0.2827 0.1216 0.2490 -0.0088 -0.0167 0.0205  241 TYR B C   
6093 O O   . TYR B 241 ? 0.2941 0.1354 0.2620 -0.0006 -0.0185 0.0239  241 TYR B O   
6094 C CB  . TYR B 241 ? 0.2551 0.1203 0.2233 -0.0196 -0.0159 0.0188  241 TYR B CB  
6095 C CG  . TYR B 241 ? 0.2346 0.1079 0.2023 -0.0157 -0.0179 0.0244  241 TYR B CG  
6096 C CD1 . TYR B 241 ? 0.2847 0.1493 0.2467 -0.0140 -0.0191 0.0317  241 TYR B CD1 
6097 C CD2 . TYR B 241 ? 0.2627 0.1520 0.2354 -0.0138 -0.0186 0.0222  241 TYR B CD2 
6098 C CE1 . TYR B 241 ? 0.2948 0.1682 0.2550 -0.0099 -0.0220 0.0359  241 TYR B CE1 
6099 C CE2 . TYR B 241 ? 0.2554 0.1528 0.2282 -0.0107 -0.0214 0.0254  241 TYR B CE2 
6100 C CZ  . TYR B 241 ? 0.2740 0.1644 0.2401 -0.0085 -0.0236 0.0319  241 TYR B CZ  
6101 O OH  . TYR B 241 ? 0.2908 0.1909 0.2557 -0.0050 -0.0273 0.0343  241 TYR B OH  
6102 N N   . PHE B 242 ? 0.2560 0.0781 0.2189 -0.0141 -0.0153 0.0216  242 PHE B N   
6103 C CA  . PHE B 242 ? 0.2769 0.0803 0.2364 -0.0094 -0.0154 0.0280  242 PHE B CA  
6104 C C   . PHE B 242 ? 0.3038 0.0995 0.2658 0.0007  -0.0159 0.0239  242 PHE B C   
6105 O O   . PHE B 242 ? 0.3186 0.1086 0.2801 0.0098  -0.0173 0.0296  242 PHE B O   
6106 C CB  . PHE B 242 ? 0.2958 0.0834 0.2540 -0.0180 -0.0123 0.0293  242 PHE B CB  
6107 C CG  . PHE B 242 ? 0.3147 0.0872 0.2722 -0.0127 -0.0104 0.0366  242 PHE B CG  
6108 C CD1 . PHE B 242 ? 0.3369 0.0960 0.2980 -0.0068 -0.0095 0.0323  242 PHE B CD1 
6109 C CD2 . PHE B 242 ? 0.3589 0.1307 0.3117 -0.0131 -0.0095 0.0479  242 PHE B CD2 
6110 C CE1 . PHE B 242 ? 0.3501 0.0950 0.3119 -0.0013 -0.0079 0.0396  242 PHE B CE1 
6111 C CE2 . PHE B 242 ? 0.3945 0.1524 0.3466 -0.0075 -0.0078 0.0559  242 PHE B CE2 
6112 C CZ  . PHE B 242 ? 0.3827 0.1269 0.3400 -0.0016 -0.0071 0.0520  242 PHE B CZ  
6113 N N   . GLU B 243 ? 0.3242 0.1198 0.2885 0.0001  -0.0146 0.0138  243 GLU B N   
6114 C CA  . GLU B 243 ? 0.3285 0.1186 0.2949 0.0105  -0.0141 0.0090  243 GLU B CA  
6115 C C   . GLU B 243 ? 0.3461 0.1516 0.3174 0.0202  -0.0156 0.0131  243 GLU B C   
6116 O O   . GLU B 243 ? 0.3795 0.1779 0.3527 0.0302  -0.0163 0.0160  243 GLU B O   
6117 C CB  . GLU B 243 ? 0.2926 0.0871 0.2590 0.0090  -0.0125 -0.0025 243 GLU B CB  
6118 C CG  . GLU B 243 ? 0.4442 0.2370 0.4126 0.0208  -0.0108 -0.0079 243 GLU B CG  
6119 C CD  . GLU B 243 ? 0.5492 0.3516 0.5158 0.0212  -0.0087 -0.0181 243 GLU B CD  
6120 O OE1 . GLU B 243 ? 0.6521 0.4580 0.6203 0.0310  -0.0061 -0.0219 243 GLU B OE1 
6121 O OE2 . GLU B 243 ? 0.4965 0.3041 0.4598 0.0126  -0.0094 -0.0221 243 GLU B OE2 
6122 N N   . ILE B 244 ? 0.3219 0.1485 0.2963 0.0175  -0.0163 0.0135  244 ILE B N   
6123 C CA  . ILE B 244 ? 0.3141 0.1574 0.2959 0.0252  -0.0176 0.0153  244 ILE B CA  
6124 C C   . ILE B 244 ? 0.3031 0.1478 0.2844 0.0284  -0.0217 0.0242  244 ILE B C   
6125 O O   . ILE B 244 ? 0.2843 0.1318 0.2705 0.0382  -0.0238 0.0267  244 ILE B O   
6126 C CB  . ILE B 244 ? 0.3459 0.2092 0.3320 0.0207  -0.0163 0.0120  244 ILE B CB  
6127 C CG1 . ILE B 244 ? 0.3202 0.1827 0.3046 0.0192  -0.0124 0.0041  244 ILE B CG1 
6128 C CG2 . ILE B 244 ? 0.2637 0.1445 0.2599 0.0268  -0.0174 0.0136  244 ILE B CG2 
6129 C CD1 . ILE B 244 ? 0.3353 0.1904 0.3209 0.0285  -0.0100 -0.0006 244 ILE B CD1 
6130 N N   . PHE B 245 ? 0.2836 0.1274 0.2586 0.0209  -0.0229 0.0290  245 PHE B N   
6131 C CA  . PHE B 245 ? 0.2857 0.1358 0.2584 0.0237  -0.0271 0.0368  245 PHE B CA  
6132 C C   . PHE B 245 ? 0.3502 0.1814 0.3133 0.0249  -0.0277 0.0456  245 PHE B C   
6133 O O   . PHE B 245 ? 0.3402 0.1757 0.2990 0.0295  -0.0315 0.0530  245 PHE B O   
6134 C CB  . PHE B 245 ? 0.2473 0.1133 0.2193 0.0158  -0.0277 0.0361  245 PHE B CB  
6135 C CG  . PHE B 245 ? 0.2555 0.1391 0.2373 0.0152  -0.0269 0.0292  245 PHE B CG  
6136 C CD1 . PHE B 245 ? 0.3137 0.2115 0.3048 0.0219  -0.0298 0.0284  245 PHE B CD1 
6137 C CD2 . PHE B 245 ? 0.2517 0.1379 0.2343 0.0082  -0.0232 0.0239  245 PHE B CD2 
6138 C CE1 . PHE B 245 ? 0.2746 0.1875 0.2761 0.0205  -0.0278 0.0228  245 PHE B CE1 
6139 C CE2 . PHE B 245 ? 0.2371 0.1375 0.2279 0.0082  -0.0216 0.0192  245 PHE B CE2 
6140 C CZ  . PHE B 245 ? 0.2443 0.1573 0.2448 0.0138  -0.0233 0.0188  245 PHE B CZ  
6141 N N   . GLY B 246 ? 0.3031 0.1136 0.2625 0.0211  -0.0241 0.0451  246 GLY B N   
6142 C CA  . GLY B 246 ? 0.3374 0.1272 0.2884 0.0220  -0.0234 0.0545  246 GLY B CA  
6143 C C   . GLY B 246 ? 0.4000 0.1907 0.3425 0.0138  -0.0224 0.0621  246 GLY B C   
6144 O O   . GLY B 246 ? 0.4237 0.2047 0.3596 0.0164  -0.0214 0.0719  246 GLY B O   
6145 N N   . GLU B 247 ? 0.3814 0.1873 0.3253 0.0047  -0.0213 0.0574  247 GLU B N   
6146 C CA  . GLU B 247 ? 0.4396 0.2481 0.3763 -0.0036 -0.0191 0.0629  247 GLU B CA  
6147 C C   . GLU B 247 ? 0.3451 0.1601 0.2870 -0.0148 -0.0158 0.0550  247 GLU B C   
6148 O O   . GLU B 247 ? 0.3593 0.1833 0.3085 -0.0147 -0.0167 0.0459  247 GLU B O   
6149 C CB  . GLU B 247 ? 0.5525 0.3804 0.4849 -0.0002 -0.0228 0.0661  247 GLU B CB  
6150 C CG  . GLU B 247 ? 0.6780 0.5053 0.6044 0.0112  -0.0277 0.0740  247 GLU B CG  
6151 C CD  . GLU B 247 ? 0.6688 0.5178 0.5918 0.0134  -0.0323 0.0739  247 GLU B CD  
6152 O OE1 . GLU B 247 ? 0.5631 0.4267 0.4907 0.0070  -0.0316 0.0664  247 GLU B OE1 
6153 O OE2 . GLU B 247 ? 0.7411 0.5922 0.6562 0.0217  -0.0369 0.0812  247 GLU B OE2 
6154 N N   . HIS B 248 ? 0.3535 0.1657 0.2916 -0.0239 -0.0119 0.0590  248 HIS B N   
6155 C CA  . HIS B 248 ? 0.3641 0.1888 0.3076 -0.0332 -0.0098 0.0522  248 HIS B CA  
6156 C C   . HIS B 248 ? 0.3707 0.2173 0.3138 -0.0311 -0.0119 0.0504  248 HIS B C   
6157 O O   . HIS B 248 ? 0.3916 0.2426 0.3273 -0.0270 -0.0134 0.0566  248 HIS B O   
6158 C CB  . HIS B 248 ? 0.4037 0.2239 0.3470 -0.0431 -0.0041 0.0560  248 HIS B CB  
6159 C CG  . HIS B 248 ? 0.6192 0.4258 0.5700 -0.0456 -0.0007 0.0541  248 HIS B CG  
6160 N ND1 . HIS B 248 ? 0.6986 0.4924 0.6479 -0.0450 0.0032  0.0629  248 HIS B ND1 
6161 C CD2 . HIS B 248 ? 0.6796 0.4830 0.6392 -0.0489 -0.0009 0.0444  248 HIS B CD2 
6162 C CE1 . HIS B 248 ? 0.6799 0.4625 0.6386 -0.0484 0.0053  0.0584  248 HIS B CE1 
6163 N NE2 . HIS B 248 ? 0.6842 0.4726 0.6485 -0.0507 0.0026  0.0466  248 HIS B NE2 
6164 N N   . PRO B 249 ? 0.3011 0.1610 0.2513 -0.0332 -0.0124 0.0419  249 PRO B N   
6165 C CA  . PRO B 249 ? 0.3195 0.1976 0.2704 -0.0313 -0.0141 0.0398  249 PRO B CA  
6166 C C   . PRO B 249 ? 0.3333 0.2182 0.2798 -0.0374 -0.0109 0.0428  249 PRO B C   
6167 O O   . PRO B 249 ? 0.4129 0.2960 0.3618 -0.0449 -0.0071 0.0424  249 PRO B O   
6168 C CB  . PRO B 249 ? 0.2962 0.1826 0.2557 -0.0318 -0.0143 0.0312  249 PRO B CB  
6169 C CG  . PRO B 249 ? 0.3690 0.2462 0.3306 -0.0379 -0.0120 0.0285  249 PRO B CG  
6170 C CD  . PRO B 249 ? 0.3166 0.1751 0.2737 -0.0376 -0.0114 0.0341  249 PRO B CD  
6171 N N   . VAL B 250 ? 0.3034 0.1972 0.2439 -0.0341 -0.0124 0.0454  250 VAL B N   
6172 C CA  . VAL B 250 ? 0.3419 0.2440 0.2775 -0.0387 -0.0087 0.0472  250 VAL B CA  
6173 C C   . VAL B 250 ? 0.2860 0.2040 0.2260 -0.0383 -0.0095 0.0399  250 VAL B C   
6174 O O   . VAL B 250 ? 0.2718 0.1981 0.2090 -0.0414 -0.0061 0.0397  250 VAL B O   
6175 C CB  . VAL B 250 ? 0.3522 0.2512 0.2742 -0.0358 -0.0086 0.0560  250 VAL B CB  
6176 C CG1 . VAL B 250 ? 0.4533 0.3343 0.3710 -0.0379 -0.0054 0.0648  250 VAL B CG1 
6177 C CG2 . VAL B 250 ? 0.3560 0.2598 0.2744 -0.0268 -0.0154 0.0554  250 VAL B CG2 
6178 N N   . TYR B 251 ? 0.2381 0.1602 0.1855 -0.0344 -0.0131 0.0341  251 TYR B N   
6179 C CA  . TYR B 251 ? 0.2133 0.1474 0.1670 -0.0345 -0.0130 0.0273  251 TYR B CA  
6180 C C   . TYR B 251 ? 0.2142 0.1475 0.1772 -0.0356 -0.0121 0.0232  251 TYR B C   
6181 O O   . TYR B 251 ? 0.2504 0.1763 0.2157 -0.0336 -0.0135 0.0234  251 TYR B O   
6182 C CB  . TYR B 251 ? 0.2574 0.1981 0.2121 -0.0292 -0.0175 0.0242  251 TYR B CB  
6183 C CG  . TYR B 251 ? 0.3194 0.2599 0.2630 -0.0262 -0.0203 0.0288  251 TYR B CG  
6184 C CD1 . TYR B 251 ? 0.4007 0.3453 0.3345 -0.0282 -0.0179 0.0305  251 TYR B CD1 
6185 C CD2 . TYR B 251 ? 0.3414 0.2780 0.2835 -0.0207 -0.0251 0.0320  251 TYR B CD2 
6186 C CE1 . TYR B 251 ? 0.3486 0.2933 0.2696 -0.0248 -0.0202 0.0356  251 TYR B CE1 
6187 C CE2 . TYR B 251 ? 0.3246 0.2616 0.2549 -0.0168 -0.0282 0.0372  251 TYR B CE2 
6188 C CZ  . TYR B 251 ? 0.3633 0.3041 0.2821 -0.0190 -0.0258 0.0391  251 TYR B CZ  
6189 O OH  . TYR B 251 ? 0.4602 0.4019 0.3647 -0.0146 -0.0285 0.0450  251 TYR B OH  
6190 N N   . MET B 252 ? 0.2322 0.1733 0.1998 -0.0382 -0.0095 0.0196  252 MET B N   
6191 C CA  . MET B 252 ? 0.2137 0.1562 0.1886 -0.0377 -0.0092 0.0159  252 MET B CA  
6192 C C   . MET B 252 ? 0.2453 0.1967 0.2252 -0.0360 -0.0080 0.0122  252 MET B C   
6193 O O   . MET B 252 ? 0.2394 0.1968 0.2181 -0.0370 -0.0064 0.0113  252 MET B O   
6194 C CB  . MET B 252 ? 0.3243 0.2654 0.3009 -0.0423 -0.0075 0.0156  252 MET B CB  
6195 C CG  . MET B 252 ? 0.3773 0.3065 0.3519 -0.0434 -0.0087 0.0171  252 MET B CG  
6196 S SD  . MET B 252 ? 0.3659 0.2952 0.3447 -0.0495 -0.0079 0.0138  252 MET B SD  
6197 C CE  . MET B 252 ? 0.6346 0.5731 0.6175 -0.0453 -0.0090 0.0090  252 MET B CE  
6198 N N   . TRP B 253 ? 0.2104 0.1620 0.1958 -0.0331 -0.0082 0.0101  253 TRP B N   
6199 C CA  . TRP B 253 ? 0.2205 0.1778 0.2114 -0.0313 -0.0062 0.0077  253 TRP B CA  
6200 C C   . TRP B 253 ? 0.2277 0.1881 0.2201 -0.0317 -0.0047 0.0074  253 TRP B C   
6201 O O   . TRP B 253 ? 0.2261 0.1839 0.2180 -0.0308 -0.0054 0.0075  253 TRP B O   
6202 C CB  . TRP B 253 ? 0.2239 0.1799 0.2202 -0.0279 -0.0063 0.0068  253 TRP B CB  
6203 C CG  . TRP B 253 ? 0.2018 0.1607 0.2037 -0.0262 -0.0032 0.0057  253 TRP B CG  
6204 C CD1 . TRP B 253 ? 0.2281 0.1865 0.2321 -0.0235 -0.0010 0.0071  253 TRP B CD1 
6205 C CD2 . TRP B 253 ? 0.2362 0.1979 0.2412 -0.0263 -0.0015 0.0035  253 TRP B CD2 
6206 N NE1 . TRP B 253 ? 0.2079 0.1679 0.2164 -0.0218 0.0021  0.0071  253 TRP B NE1 
6207 C CE2 . TRP B 253 ? 0.1879 0.1493 0.1979 -0.0236 0.0019  0.0044  253 TRP B CE2 
6208 C CE3 . TRP B 253 ? 0.2559 0.2200 0.2590 -0.0279 -0.0022 0.0007  253 TRP B CE3 
6209 C CZ2 . TRP B 253 ? 0.1518 0.1133 0.1662 -0.0225 0.0046  0.0028  253 TRP B CZ2 
6210 C CZ3 . TRP B 253 ? 0.2520 0.2173 0.2593 -0.0270 0.0003  -0.0024 253 TRP B CZ3 
6211 C CH2 . TRP B 253 ? 0.2089 0.1721 0.2225 -0.0243 0.0037  -0.0013 253 TRP B CH2 
6212 N N   . PRO B 254 ? 0.1683 0.1352 0.1623 -0.0324 -0.0028 0.0066  254 PRO B N   
6213 C CA  . PRO B 254 ? 0.1513 0.1239 0.1478 -0.0318 -0.0023 0.0063  254 PRO B CA  
6214 C C   . PRO B 254 ? 0.2063 0.1787 0.2054 -0.0266 -0.0013 0.0066  254 PRO B C   
6215 O O   . PRO B 254 ? 0.2112 0.1823 0.2134 -0.0242 0.0008  0.0065  254 PRO B O   
6216 C CB  . PRO B 254 ? 0.2307 0.2115 0.2295 -0.0330 -0.0001 0.0055  254 PRO B CB  
6217 C CG  . PRO B 254 ? 0.2805 0.2588 0.2777 -0.0322 0.0011  0.0045  254 PRO B CG  
6218 C CD  . PRO B 254 ? 0.2272 0.1977 0.2205 -0.0331 -0.0013 0.0054  254 PRO B CD  
6219 N N   . PRO B 255 ? 0.2241 0.1971 0.2217 -0.0247 -0.0025 0.0069  255 PRO B N   
6220 C CA  . PRO B 255 ? 0.1946 0.1667 0.1927 -0.0191 -0.0006 0.0088  255 PRO B CA  
6221 C C   . PRO B 255 ? 0.2027 0.1790 0.2048 -0.0154 0.0020  0.0103  255 PRO B C   
6222 O O   . PRO B 255 ? 0.2232 0.2071 0.2270 -0.0154 0.0012  0.0094  255 PRO B O   
6223 C CB  . PRO B 255 ? 0.2076 0.1822 0.2009 -0.0177 -0.0031 0.0080  255 PRO B CB  
6224 C CG  . PRO B 255 ? 0.2133 0.1845 0.2045 -0.0233 -0.0060 0.0053  255 PRO B CG  
6225 C CD  . PRO B 255 ? 0.2088 0.1819 0.2034 -0.0279 -0.0054 0.0054  255 PRO B CD  
6226 N N   . GLN B 256 ? 0.2077 0.1787 0.2125 -0.0122 0.0055  0.0124  256 GLN B N   
6227 C CA  . GLN B 256 ? 0.2447 0.2155 0.2541 -0.0084 0.0089  0.0140  256 GLN B CA  
6228 C C   . GLN B 256 ? 0.2283 0.2015 0.2409 -0.0108 0.0089  0.0103  256 GLN B C   
6229 O O   . GLN B 256 ? 0.1928 0.1681 0.2087 -0.0071 0.0110  0.0105  256 GLN B O   
6230 C CB  . GLN B 256 ? 0.2589 0.2351 0.2660 -0.0022 0.0089  0.0175  256 GLN B CB  
6231 C CG  . GLN B 256 ? 0.2301 0.2061 0.2305 0.0006  0.0082  0.0203  256 GLN B CG  
6232 C CD  . GLN B 256 ? 0.3335 0.3009 0.3350 0.0032  0.0136  0.0247  256 GLN B CD  
6233 O OE1 . GLN B 256 ? 0.3379 0.2992 0.3464 0.0027  0.0174  0.0255  256 GLN B OE1 
6234 N NE2 . GLN B 256 ? 0.3370 0.3041 0.3322 0.0057  0.0143  0.0271  256 GLN B NE2 
6235 N N   . ALA B 257 ? 0.1624 0.1352 0.1734 -0.0162 0.0069  0.0072  257 ALA B N   
6236 C CA  . ALA B 257 ? 0.1873 0.1634 0.1985 -0.0185 0.0071  0.0037  257 ALA B CA  
6237 C C   . ALA B 257 ? 0.1986 0.1846 0.2102 -0.0180 0.0071  0.0038  257 ALA B C   
6238 O O   . ALA B 257 ? 0.1993 0.1899 0.2123 -0.0180 0.0091  0.0014  257 ALA B O   
6239 C CB  . ALA B 257 ? 0.2661 0.2376 0.2818 -0.0165 0.0101  0.0010  257 ALA B CB  
6240 N N   . SER B 258 ? 0.1915 0.1822 0.2023 -0.0176 0.0050  0.0058  258 SER B N   
6241 C CA  . SER B 258 ? 0.1984 0.2011 0.2128 -0.0162 0.0046  0.0056  258 SER B CA  
6242 C C   . SER B 258 ? 0.1820 0.1911 0.1966 -0.0228 0.0044  0.0037  258 SER B C   
6243 O O   . SER B 258 ? 0.2278 0.2336 0.2390 -0.0283 0.0023  0.0039  258 SER B O   
6244 C CB  . SER B 258 ? 0.2490 0.2564 0.2626 -0.0137 0.0014  0.0072  258 SER B CB  
6245 O OG  . SER B 258 ? 0.3526 0.3738 0.3717 -0.0113 0.0005  0.0066  258 SER B OG  
6246 N N   . VAL B 259 ? 0.2132 0.2308 0.2320 -0.0220 0.0073  0.0023  259 VAL B N   
6247 C CA  . VAL B 259 ? 0.1980 0.2235 0.2179 -0.0281 0.0087  0.0015  259 VAL B CA  
6248 C C   . VAL B 259 ? 0.1752 0.2171 0.2043 -0.0257 0.0104  0.0004  259 VAL B C   
6249 O O   . VAL B 259 ? 0.2239 0.2698 0.2574 -0.0181 0.0106  0.0003  259 VAL B O   
6250 C CB  . VAL B 259 ? 0.2296 0.2499 0.2436 -0.0302 0.0120  0.0005  259 VAL B CB  
6251 C CG1 . VAL B 259 ? 0.2165 0.2232 0.2229 -0.0319 0.0094  0.0014  259 VAL B CG1 
6252 C CG2 . VAL B 259 ? 0.2187 0.2411 0.2349 -0.0241 0.0155  -0.0024 259 VAL B CG2 
6253 N N   . SER B 260 ? 0.1573 0.2087 0.1900 -0.0321 0.0120  0.0002  260 SER B N   
6254 C CA  . SER B 260 ? 0.1732 0.2433 0.2168 -0.0319 0.0145  -0.0010 260 SER B CA  
6255 C C   . SER B 260 ? 0.1992 0.2725 0.2424 -0.0409 0.0185  0.0000  260 SER B C   
6256 O O   . SER B 260 ? 0.2320 0.2926 0.2668 -0.0466 0.0178  0.0020  260 SER B O   
6257 C CB  . SER B 260 ? 0.1927 0.2749 0.2452 -0.0313 0.0093  -0.0018 260 SER B CB  
6258 O OG  . SER B 260 ? 0.2221 0.3014 0.2738 -0.0404 0.0061  -0.0020 260 SER B OG  
6259 N N   . ASN B 261 ? 0.1783 0.2683 0.2305 -0.0415 0.0234  -0.0009 261 ASN B N   
6260 C CA  . ASN B 261 ? 0.1818 0.2758 0.2343 -0.0505 0.0288  0.0013  261 ASN B CA  
6261 C C   . ASN B 261 ? 0.2519 0.3413 0.3064 -0.0603 0.0253  0.0030  261 ASN B C   
6262 O O   . ASN B 261 ? 0.2342 0.3122 0.2808 -0.0669 0.0275  0.0066  261 ASN B O   
6263 C CB  . ASN B 261 ? 0.2081 0.3243 0.2736 -0.0500 0.0347  -0.0001 261 ASN B CB  
6264 C CG  . ASN B 261 ? 0.2057 0.3241 0.2675 -0.0405 0.0397  -0.0023 261 ASN B CG  
6265 O OD1 . ASN B 261 ? 0.2161 0.3190 0.2639 -0.0375 0.0401  -0.0026 261 ASN B OD1 
6266 N ND2 . ASN B 261 ? 0.2039 0.3416 0.2787 -0.0352 0.0429  -0.0048 261 ASN B ND2 
6267 N N   . GLU B 262 ? 0.1951 0.2920 0.2592 -0.0606 0.0193  0.0003  262 GLU B N   
6268 C CA  . GLU B 262 ? 0.2146 0.3074 0.2818 -0.0702 0.0157  -0.0001 262 GLU B CA  
6269 C C   . GLU B 262 ? 0.2531 0.3226 0.3063 -0.0704 0.0119  0.0014  262 GLU B C   
6270 O O   . GLU B 262 ? 0.1819 0.2407 0.2326 -0.0786 0.0125  0.0032  262 GLU B O   
6271 C CB  . GLU B 262 ? 0.1873 0.2964 0.2677 -0.0697 0.0093  -0.0050 262 GLU B CB  
6272 C CG  . GLU B 262 ? 0.2699 0.4046 0.3681 -0.0720 0.0127  -0.0067 262 GLU B CG  
6273 C CD  . GLU B 262 ? 0.4251 0.5775 0.5364 -0.0715 0.0048  -0.0121 262 GLU B CD  
6274 O OE1 . GLU B 262 ? 0.3397 0.4843 0.4485 -0.0761 -0.0018 -0.0151 262 GLU B OE1 
6275 O OE2 . GLU B 262 ? 0.5493 0.7238 0.6730 -0.0658 0.0049  -0.0138 262 GLU B OE2 
6276 N N   . ALA B 263 ? 0.2091 0.2703 0.2539 -0.0614 0.0087  0.0009  263 ALA B N   
6277 C CA  . ALA B 263 ? 0.2138 0.2552 0.2468 -0.0608 0.0059  0.0023  263 ALA B CA  
6278 C C   . ALA B 263 ? 0.2358 0.2653 0.2594 -0.0635 0.0102  0.0065  263 ALA B C   
6279 O O   . ALA B 263 ? 0.2492 0.2648 0.2667 -0.0673 0.0089  0.0086  263 ALA B O   
6280 C CB  . ALA B 263 ? 0.1686 0.2056 0.1968 -0.0511 0.0029  0.0014  263 ALA B CB  
6281 N N   . LEU B 264 ? 0.1859 0.2209 0.2076 -0.0607 0.0152  0.0076  264 LEU B N   
6282 C CA  . LEU B 264 ? 0.2757 0.3017 0.2867 -0.0626 0.0188  0.0115  264 LEU B CA  
6283 C C   . LEU B 264 ? 0.2946 0.3187 0.3065 -0.0720 0.0222  0.0159  264 LEU B C   
6284 O O   . LEU B 264 ? 0.2776 0.2876 0.2796 -0.0741 0.0224  0.0204  264 LEU B O   
6285 C CB  . LEU B 264 ? 0.2268 0.2608 0.2350 -0.0577 0.0236  0.0105  264 LEU B CB  
6286 C CG  . LEU B 264 ? 0.2325 0.2625 0.2381 -0.0491 0.0207  0.0066  264 LEU B CG  
6287 C CD1 . LEU B 264 ? 0.2495 0.2886 0.2555 -0.0441 0.0254  0.0035  264 LEU B CD1 
6288 C CD2 . LEU B 264 ? 0.4103 0.4251 0.4048 -0.0481 0.0174  0.0078  264 LEU B CD2 
6289 N N   . GLU B 265 ? 0.2017 0.2397 0.2264 -0.0777 0.0250  0.0149  265 GLU B N   
6290 C CA  . GLU B 265 ? 0.2724 0.3079 0.3008 -0.0882 0.0289  0.0190  265 GLU B CA  
6291 C C   . GLU B 265 ? 0.2472 0.2665 0.2745 -0.0925 0.0236  0.0188  265 GLU B C   
6292 O O   . GLU B 265 ? 0.2558 0.2616 0.2783 -0.0984 0.0264  0.0241  265 GLU B O   
6293 C CB  . GLU B 265 ? 0.3657 0.4222 0.4117 -0.0940 0.0325  0.0167  265 GLU B CB  
6294 C CG  . GLU B 265 ? 0.4930 0.5472 0.5474 -0.1068 0.0361  0.0197  265 GLU B CG  
6295 C CD  . GLU B 265 ? 0.5421 0.5937 0.5902 -0.1113 0.0462  0.0281  265 GLU B CD  
6296 O OE1 . GLU B 265 ? 0.4669 0.5256 0.5072 -0.1048 0.0507  0.0297  265 GLU B OE1 
6297 O OE2 . GLU B 265 ? 0.5349 0.5761 0.5852 -0.1191 0.0493  0.0328  265 GLU B OE2 
6298 N N   . LEU B 266 ? 0.2956 0.3152 0.3266 -0.0890 0.0164  0.0128  266 LEU B N   
6299 C CA  . LEU B 266 ? 0.1761 0.1800 0.2045 -0.0916 0.0115  0.0113  266 LEU B CA  
6300 C C   . LEU B 266 ? 0.1956 0.1799 0.2094 -0.0873 0.0111  0.0160  266 LEU B C   
6301 O O   . LEU B 266 ? 0.2522 0.2209 0.2625 -0.0918 0.0116  0.0191  266 LEU B O   
6302 C CB  . LEU B 266 ? 0.1818 0.1913 0.2141 -0.0869 0.0043  0.0042  266 LEU B CB  
6303 C CG  . LEU B 266 ? 0.2225 0.2166 0.2503 -0.0873 -0.0010 0.0010  266 LEU B CG  
6304 C CD1 . LEU B 266 ? 0.2657 0.2521 0.2998 -0.0984 -0.0003 -0.0002 266 LEU B CD1 
6305 C CD2 . LEU B 266 ? 0.2235 0.2255 0.2525 -0.0812 -0.0073 -0.0054 266 LEU B CD2 
6306 N N   . TYR B 267 ? 0.2173 0.2021 0.2233 -0.0785 0.0101  0.0163  267 TYR B N   
6307 C CA  . TYR B 267 ? 0.2172 0.1868 0.2111 -0.0741 0.0089  0.0201  267 TYR B CA  
6308 C C   . TYR B 267 ? 0.2614 0.2236 0.2484 -0.0783 0.0138  0.0276  267 TYR B C   
6309 O O   . TYR B 267 ? 0.2650 0.2113 0.2455 -0.0787 0.0129  0.0317  267 TYR B O   
6310 C CB  . TYR B 267 ? 0.2295 0.2035 0.2188 -0.0655 0.0075  0.0184  267 TYR B CB  
6311 C CG  . TYR B 267 ? 0.2012 0.1769 0.1943 -0.0602 0.0030  0.0134  267 TYR B CG  
6312 C CD1 . TYR B 267 ? 0.2807 0.2455 0.2715 -0.0586 -0.0008 0.0124  267 TYR B CD1 
6313 C CD2 . TYR B 267 ? 0.2485 0.2363 0.2468 -0.0562 0.0034  0.0102  267 TYR B CD2 
6314 C CE1 . TYR B 267 ? 0.2887 0.2557 0.2816 -0.0534 -0.0037 0.0087  267 TYR B CE1 
6315 C CE2 . TYR B 267 ? 0.1916 0.1801 0.1919 -0.0509 0.0002  0.0073  267 TYR B CE2 
6316 C CZ  . TYR B 267 ? 0.2914 0.2700 0.2887 -0.0498 -0.0031 0.0068  267 TYR B CZ  
6317 O OH  . TYR B 267 ? 0.2400 0.2198 0.2380 -0.0443 -0.0051 0.0048  267 TYR B OH  
6318 N N   . TYR B 268 ? 0.2532 0.2268 0.2412 -0.0808 0.0197  0.0300  268 TYR B N   
6319 C CA  . TYR B 268 ? 0.2724 0.2400 0.2527 -0.0848 0.0256  0.0383  268 TYR B CA  
6320 C C   . TYR B 268 ? 0.2565 0.2121 0.2418 -0.0938 0.0274  0.0419  268 TYR B C   
6321 O O   . TYR B 268 ? 0.2985 0.2379 0.2746 -0.0943 0.0288  0.0492  268 TYR B O   
6322 C CB  . TYR B 268 ? 0.2630 0.2471 0.2449 -0.0863 0.0327  0.0393  268 TYR B CB  
6323 C CG  . TYR B 268 ? 0.3564 0.3376 0.3357 -0.0938 0.0410  0.0481  268 TYR B CG  
6324 C CD1 . TYR B 268 ? 0.3422 0.3119 0.3047 -0.0912 0.0434  0.0566  268 TYR B CD1 
6325 C CD2 . TYR B 268 ? 0.3574 0.3480 0.3512 -0.1033 0.0464  0.0482  268 TYR B CD2 
6326 C CE1 . TYR B 268 ? 0.3211 0.2869 0.2798 -0.0976 0.0519  0.0662  268 TYR B CE1 
6327 C CE2 . TYR B 268 ? 0.4759 0.4637 0.4692 -0.1092 0.0548  0.0566  268 TYR B CE2 
6328 C CZ  . TYR B 268 ? 0.4354 0.4101 0.4109 -0.1056 0.0577  0.0658  268 TYR B CZ  
6329 O OH  . TYR B 268 ? 0.4555 0.4270 0.4307 -0.1085 0.0661  0.0747  268 TYR B OH  
6330 N N   . GLU B 269 ? 0.2526 0.2158 0.2530 -0.1006 0.0271  0.0365  269 GLU B N   
6331 C CA  . GLU B 269 ? 0.2991 0.2522 0.3075 -0.1079 0.0285  0.0377  269 GLU B CA  
6332 C C   . GLU B 269 ? 0.2875 0.2198 0.2903 -0.1043 0.0232  0.0370  269 GLU B C   
6333 O O   . GLU B 269 ? 0.3450 0.2635 0.3495 -0.1065 0.0254  0.0407  269 GLU B O   
6334 C CB  . GLU B 269 ? 0.3274 0.2955 0.3542 -0.1139 0.0271  0.0297  269 GLU B CB  
6335 C CG  . GLU B 269 ? 0.4256 0.4124 0.4622 -0.1187 0.0344  0.0319  269 GLU B CG  
6336 C CD  . GLU B 269 ? 0.6482 0.6531 0.7040 -0.1236 0.0317  0.0236  269 GLU B CD  
6337 O OE1 . GLU B 269 ? 0.6879 0.6891 0.7479 -0.1237 0.0241  0.0163  269 GLU B OE1 
6338 O OE2 . GLU B 269 ? 0.6628 0.6865 0.7293 -0.1267 0.0370  0.0242  269 GLU B OE2 
6339 N N   . LYS B 270 ? 0.2936 0.2234 0.2906 -0.0984 0.0168  0.0325  270 LYS B N   
6340 C CA  . LYS B 270 ? 0.3181 0.2302 0.3100 -0.0936 0.0121  0.0313  270 LYS B CA  
6341 C C   . LYS B 270 ? 0.3231 0.2230 0.3003 -0.0868 0.0121  0.0392  270 LYS B C   
6342 O O   . LYS B 270 ? 0.3343 0.2219 0.3071 -0.0811 0.0079  0.0382  270 LYS B O   
6343 C CB  . LYS B 270 ? 0.3255 0.2431 0.3198 -0.0895 0.0056  0.0224  270 LYS B CB  
6344 C CG  . LYS B 270 ? 0.3511 0.2783 0.3577 -0.0959 0.0035  0.0141  270 LYS B CG  
6345 C CD  . LYS B 270 ? 0.5629 0.4799 0.5770 -0.1016 0.0049  0.0128  270 LYS B CD  
6346 C CE  . LYS B 270 ? 0.6136 0.5436 0.6413 -0.1078 0.0019  0.0036  270 LYS B CE  
6347 N NZ  . LYS B 270 ? 0.7134 0.6441 0.7542 -0.1163 0.0058  0.0045  270 LYS B NZ  
6348 N N   . GLY B 271 ? 0.3127 0.2172 0.2825 -0.0865 0.0166  0.0465  271 GLY B N   
6349 C CA  . GLY B 271 ? 0.3125 0.2069 0.2683 -0.0796 0.0162  0.0542  271 GLY B CA  
6350 C C   . GLY B 271 ? 0.3344 0.2378 0.2841 -0.0698 0.0114  0.0513  271 GLY B C   
6351 O O   . GLY B 271 ? 0.3327 0.2289 0.2720 -0.0633 0.0091  0.0563  271 GLY B O   
6352 N N   . ILE B 272 ? 0.2855 0.2041 0.2418 -0.0685 0.0097  0.0435  272 ILE B N   
6353 C CA  . ILE B 272 ? 0.2739 0.2005 0.2263 -0.0607 0.0060  0.0402  272 ILE B CA  
6354 C C   . ILE B 272 ? 0.2912 0.2266 0.2350 -0.0597 0.0095  0.0434  272 ILE B C   
6355 O O   . ILE B 272 ? 0.3276 0.2722 0.2743 -0.0644 0.0149  0.0437  272 ILE B O   
6356 C CB  . ILE B 272 ? 0.2671 0.2043 0.2294 -0.0595 0.0039  0.0316  272 ILE B CB  
6357 C CG1 . ILE B 272 ? 0.3088 0.2386 0.2777 -0.0604 0.0009  0.0280  272 ILE B CG1 
6358 C CG2 . ILE B 272 ? 0.2742 0.2184 0.2342 -0.0525 0.0010  0.0282  272 ILE B CG2 
6359 C CD1 . ILE B 272 ? 0.3311 0.2465 0.2954 -0.0562 -0.0024 0.0300  272 ILE B CD1 
6360 N N   . ASN B 273 ? 0.2707 0.2043 0.2041 -0.0533 0.0063  0.0456  273 ASN B N   
6361 C CA  . ASN B 273 ? 0.3085 0.2500 0.2308 -0.0510 0.0085  0.0479  273 ASN B CA  
6362 C C   . ASN B 273 ? 0.2987 0.2528 0.2230 -0.0471 0.0062  0.0391  273 ASN B C   
6363 O O   . ASN B 273 ? 0.3099 0.2733 0.2281 -0.0467 0.0098  0.0380  273 ASN B O   
6364 C CB  . ASN B 273 ? 0.3504 0.2834 0.2585 -0.0458 0.0055  0.0552  273 ASN B CB  
6365 C CG  . ASN B 273 ? 0.5873 0.5060 0.4906 -0.0494 0.0097  0.0660  273 ASN B CG  
6366 O OD1 . ASN B 273 ? 0.5815 0.4998 0.4883 -0.0569 0.0168  0.0691  273 ASN B OD1 
6367 N ND2 . ASN B 273 ? 0.7406 0.6473 0.6368 -0.0440 0.0055  0.0719  273 ASN B ND2 
6368 N N   A MET B 274 ? 0.3094 0.2636 0.2420 -0.0441 0.0011  0.0328  274 MET B N   
6369 N N   B MET B 274 ? 0.3150 0.2693 0.2482 -0.0443 0.0013  0.0327  274 MET B N   
6370 C CA  A MET B 274 ? 0.2912 0.2550 0.2277 -0.0411 -0.0004 0.0246  274 MET B CA  
6371 C CA  B MET B 274 ? 0.2949 0.2584 0.2313 -0.0410 -0.0006 0.0247  274 MET B CA  
6372 C C   A MET B 274 ? 0.2990 0.2621 0.2487 -0.0408 -0.0023 0.0197  274 MET B C   
6373 C C   B MET B 274 ? 0.2963 0.2594 0.2459 -0.0407 -0.0025 0.0196  274 MET B C   
6374 O O   A MET B 274 ? 0.2768 0.2324 0.2301 -0.0405 -0.0049 0.0214  274 MET B O   
6375 O O   B MET B 274 ? 0.2898 0.2454 0.2429 -0.0401 -0.0053 0.0211  274 MET B O   
6376 C CB  A MET B 274 ? 0.2723 0.2380 0.2010 -0.0358 -0.0056 0.0224  274 MET B CB  
6377 C CB  B MET B 274 ? 0.2759 0.2404 0.2040 -0.0357 -0.0060 0.0234  274 MET B CB  
6378 C CG  A MET B 274 ? 0.2626 0.2366 0.1961 -0.0338 -0.0068 0.0128  274 MET B CG  
6379 C CG  B MET B 274 ? 0.2864 0.2601 0.2151 -0.0335 -0.0070 0.0147  274 MET B CG  
6380 S SD  A MET B 274 ? 0.3215 0.2933 0.2695 -0.0320 -0.0116 0.0073  274 MET B SD  
6381 S SD  B MET B 274 ? 0.3050 0.2808 0.2297 -0.0283 -0.0156 0.0110  274 MET B SD  
6382 C CE  A MET B 274 ? 0.3316 0.3037 0.2733 -0.0278 -0.0192 0.0080  274 MET B CE  
6383 C CE  B MET B 274 ? 0.3241 0.2964 0.2666 -0.0282 -0.0186 0.0074  274 MET B CE  
6384 N N   . LEU B 275 ? 0.2578 0.2284 0.2138 -0.0403 -0.0005 0.0139  275 LEU B N   
6385 C CA  . LEU B 275 ? 0.1870 0.1575 0.1536 -0.0386 -0.0019 0.0098  275 LEU B CA  
6386 C C   . LEU B 275 ? 0.2179 0.1936 0.1869 -0.0358 -0.0015 0.0035  275 LEU B C   
6387 O O   . LEU B 275 ? 0.2190 0.1992 0.1815 -0.0353 -0.0002 0.0013  275 LEU B O   
6388 C CB  . LEU B 275 ? 0.2095 0.1820 0.1831 -0.0412 0.0007  0.0105  275 LEU B CB  
6389 C CG  . LEU B 275 ? 0.3065 0.2883 0.2823 -0.0433 0.0054  0.0099  275 LEU B CG  
6390 C CD1 . LEU B 275 ? 0.2719 0.2599 0.2529 -0.0393 0.0069  0.0047  275 LEU B CD1 
6391 C CD2 . LEU B 275 ? 0.3198 0.3030 0.3020 -0.0471 0.0060  0.0115  275 LEU B CD2 
6392 N N   . ALA B 276 ? 0.2044 0.1789 0.1825 -0.0339 -0.0022 0.0004  276 ALA B N   
6393 C CA  . ALA B 276 ? 0.2105 0.1875 0.1931 -0.0318 -0.0007 -0.0055 276 ALA B CA  
6394 C C   . ALA B 276 ? 0.2003 0.1784 0.1910 -0.0303 0.0026  -0.0053 276 ALA B C   
6395 O O   . ALA B 276 ? 0.2144 0.1914 0.2078 -0.0307 0.0023  -0.0016 276 ALA B O   
6396 C CB  . ALA B 276 ? 0.2564 0.2303 0.2435 -0.0306 -0.0041 -0.0094 276 ALA B CB  
6397 N N   . THR B 277 ? 0.2198 0.2000 0.2138 -0.0280 0.0055  -0.0096 277 THR B N   
6398 C CA  . THR B 277 ? 0.1986 0.1791 0.2005 -0.0248 0.0083  -0.0089 277 THR B CA  
6399 C C   . THR B 277 ? 0.2295 0.2054 0.2365 -0.0219 0.0102  -0.0143 277 THR B C   
6400 O O   . THR B 277 ? 0.2290 0.2012 0.2354 -0.0234 0.0082  -0.0186 277 THR B O   
6401 C CB  . THR B 277 ? 0.2381 0.2276 0.2404 -0.0243 0.0110  -0.0072 277 THR B CB  
6402 O OG1 . THR B 277 ? 0.2161 0.2068 0.2258 -0.0198 0.0127  -0.0061 277 THR B OG1 
6403 C CG2 . THR B 277 ? 0.2010 0.1962 0.1995 -0.0240 0.0141  -0.0110 277 THR B CG2 
6404 N N   . ASP B 278 ? 0.2102 0.1860 0.2230 -0.0176 0.0138  -0.0142 278 ASP B N   
6405 C CA  . ASP B 278 ? 0.1999 0.1675 0.2194 -0.0148 0.0162  -0.0180 278 ASP B CA  
6406 C C   . ASP B 278 ? 0.2195 0.1883 0.2384 -0.0122 0.0192  -0.0249 278 ASP B C   
6407 O O   . ASP B 278 ? 0.2440 0.2217 0.2599 -0.0103 0.0211  -0.0248 278 ASP B O   
6408 C CB  . ASP B 278 ? 0.2188 0.1824 0.2447 -0.0102 0.0187  -0.0125 278 ASP B CB  
6409 C CG  . ASP B 278 ? 0.3019 0.2536 0.3354 -0.0081 0.0221  -0.0149 278 ASP B CG  
6410 O OD1 . ASP B 278 ? 0.2890 0.2348 0.3252 -0.0123 0.0209  -0.0188 278 ASP B OD1 
6411 O OD2 . ASP B 278 ? 0.3265 0.2748 0.3643 -0.0021 0.0259  -0.0130 278 ASP B OD2 
6412 N N   . GLU B 279 ? 0.2981 0.2660 0.3282 0.0076  -0.0167 -0.0071 279 GLU B N   
6413 C CA  . GLU B 279 ? 0.3253 0.2969 0.3654 0.0103  -0.0141 -0.0152 279 GLU B CA  
6414 C C   . GLU B 279 ? 0.2923 0.2653 0.3482 0.0156  -0.0165 -0.0155 279 GLU B C   
6415 O O   . GLU B 279 ? 0.2383 0.2189 0.3053 0.0179  -0.0125 -0.0227 279 GLU B O   
6416 C CB  . GLU B 279 ? 0.2904 0.2541 0.3294 0.0096  -0.0133 -0.0185 279 GLU B CB  
6417 C CG  . GLU B 279 ? 0.3331 0.3008 0.3790 0.0095  -0.0080 -0.0297 279 GLU B CG  
6418 C CD  . GLU B 279 ? 0.4537 0.4158 0.4952 0.0057  -0.0064 -0.0345 279 GLU B CD  
6419 O OE1 . GLU B 279 ? 0.3201 0.2775 0.3531 0.0033  -0.0095 -0.0282 279 GLU B OE1 
6420 O OE2 . GLU B 279 ? 0.5420 0.5051 0.5891 0.0044  -0.0011 -0.0455 279 GLU B OE2 
6421 N N   . VAL B 280 ? 0.2555 0.2230 0.3137 0.0172  -0.0227 -0.0073 280 VAL B N   
6422 C CA  . VAL B 280 ? 0.2636 0.2351 0.3394 0.0227  -0.0263 -0.0051 280 VAL B CA  
6423 C C   . VAL B 280 ? 0.2690 0.2557 0.3495 0.0220  -0.0254 -0.0067 280 VAL B C   
6424 O O   . VAL B 280 ? 0.3130 0.3082 0.4119 0.0269  -0.0245 -0.0100 280 VAL B O   
6425 C CB  . VAL B 280 ? 0.2727 0.2371 0.3482 0.0231  -0.0346 0.0062  280 VAL B CB  
6426 C CG1 . VAL B 280 ? 0.2633 0.2357 0.3588 0.0287  -0.0403 0.0116  280 VAL B CG1 
6427 C CG2 . VAL B 280 ? 0.3053 0.2544 0.3798 0.0240  -0.0346 0.0072  280 VAL B CG2 
6428 N N   . ILE B 281 ? 0.2910 0.2812 0.3568 0.0158  -0.0246 -0.0049 281 ILE B N   
6429 C CA  . ILE B 281 ? 0.2919 0.2958 0.3608 0.0135  -0.0225 -0.0073 281 ILE B CA  
6430 C C   . ILE B 281 ? 0.2827 0.2942 0.3588 0.0150  -0.0150 -0.0169 281 ILE B C   
6431 O O   . ILE B 281 ? 0.2432 0.2673 0.3333 0.0167  -0.0132 -0.0207 281 ILE B O   
6432 C CB  . ILE B 281 ? 0.3550 0.3575 0.4067 0.0060  -0.0210 -0.0046 281 ILE B CB  
6433 C CG1 . ILE B 281 ? 0.3933 0.3878 0.4357 0.0027  -0.0263 0.0026  281 ILE B CG1 
6434 C CG2 . ILE B 281 ? 0.2834 0.2990 0.3388 0.0024  -0.0186 -0.0069 281 ILE B CG2 
6435 C CD1 . ILE B 281 ? 0.3911 0.3934 0.4411 0.0023  -0.0335 0.0075  281 ILE B CD1 
6436 N N   . LEU B 282 ? 0.2683 0.2743 0.3346 0.0131  -0.0104 -0.0212 282 LEU B N   
6437 C CA  . LEU B 282 ? 0.3271 0.3413 0.3966 0.0121  -0.0028 -0.0310 282 LEU B CA  
6438 C C   . LEU B 282 ? 0.2480 0.2648 0.3387 0.0185  -0.0005 -0.0384 282 LEU B C   
6439 O O   . LEU B 282 ? 0.2701 0.2992 0.3725 0.0190  0.0049  -0.0455 282 LEU B O   
6440 C CB  . LEU B 282 ? 0.2714 0.2807 0.3263 0.0079  0.0000  -0.0333 282 LEU B CB  
6441 C CG  . LEU B 282 ? 0.2737 0.2931 0.3276 0.0040  0.0078  -0.0437 282 LEU B CG  
6442 C CD1 . LEU B 282 ? 0.2833 0.3155 0.3342 -0.0003 0.0114  -0.0435 282 LEU B CD1 
6443 C CD2 . LEU B 282 ? 0.2630 0.2801 0.3015 -0.0015 0.0086  -0.0440 282 LEU B CD2 
6444 N N   . LYS B 283 ? 0.2260 0.2307 0.3236 0.0232  -0.0037 -0.0368 283 LYS B N   
6445 C CA  . LYS B 283 ? 0.2561 0.2597 0.3772 0.0304  -0.0008 -0.0430 283 LYS B CA  
6446 C C   . LYS B 283 ? 0.3027 0.3181 0.4448 0.0360  -0.0038 -0.0393 283 LYS B C   
6447 O O   . LYS B 283 ? 0.2579 0.2807 0.4219 0.0410  0.0022  -0.0474 283 LYS B O   
6448 C CB  . LYS B 283 ? 0.3699 0.3562 0.4946 0.0342  -0.0051 -0.0384 283 LYS B CB  
6449 C CG  . LYS B 283 ? 0.4885 0.4645 0.5969 0.0287  -0.0018 -0.0434 283 LYS B CG  
6450 C CD  . LYS B 283 ? 0.6293 0.6138 0.7326 0.0233  0.0080  -0.0574 283 LYS B CD  
6451 C CE  . LYS B 283 ? 0.5947 0.5739 0.6791 0.0157  0.0093  -0.0603 283 LYS B CE  
6452 N NZ  . LYS B 283 ? 0.6709 0.6334 0.7568 0.0177  0.0050  -0.0555 283 LYS B NZ  
6453 N N   . ASN B 284 ? 0.1885 0.2069 0.3252 0.0348  -0.0126 -0.0275 284 ASN B N   
6454 C CA  . ASN B 284 ? 0.2689 0.3017 0.4244 0.0384  -0.0173 -0.0225 284 ASN B CA  
6455 C C   . ASN B 284 ? 0.2807 0.3312 0.4391 0.0347  -0.0107 -0.0302 284 ASN B C   
6456 O O   . ASN B 284 ? 0.2316 0.2973 0.4112 0.0383  -0.0121 -0.0293 284 ASN B O   
6457 C CB  . ASN B 284 ? 0.2564 0.2889 0.4009 0.0348  -0.0282 -0.0089 284 ASN B CB  
6458 C CG  . ASN B 284 ? 0.3329 0.3528 0.4812 0.0391  -0.0363 0.0013  284 ASN B CG  
6459 O OD1 . ASN B 284 ? 0.2753 0.2876 0.4411 0.0468  -0.0349 0.0001  284 ASN B OD1 
6460 N ND2 . ASN B 284 ? 0.3090 0.3264 0.4408 0.0332  -0.0442 0.0114  284 ASN B ND2 
6461 N N   . SER B 285 ? 0.2898 0.3397 0.4281 0.0272  -0.0040 -0.0363 285 SER B N   
6462 C CA  . SER B 285 ? 0.2892 0.3546 0.4260 0.0216  0.0015  -0.0411 285 SER B CA  
6463 C C   . SER B 285 ? 0.2663 0.3387 0.4076 0.0203  0.0132  -0.0546 285 SER B C   
6464 O O   . SER B 285 ? 0.2610 0.3496 0.4122 0.0183  0.0187  -0.0600 285 SER B O   
6465 C CB  . SER B 285 ? 0.2815 0.3428 0.3925 0.0126  0.0003  -0.0356 285 SER B CB  
6466 O OG  . SER B 285 ? 0.2461 0.2997 0.3509 0.0124  -0.0088 -0.0254 285 SER B OG  
6467 N N   . VAL B 286 ? 0.2099 0.2716 0.3437 0.0201  0.0175  -0.0608 286 VAL B N   
6468 C CA  . VAL B 286 ? 0.3365 0.4044 0.4697 0.0162  0.0292  -0.0749 286 VAL B CA  
6469 C C   . VAL B 286 ? 0.3466 0.4040 0.4932 0.0221  0.0327  -0.0830 286 VAL B C   
6470 O O   . VAL B 286 ? 0.4689 0.5106 0.6088 0.0241  0.0270  -0.0775 286 VAL B O   
6471 C CB  . VAL B 286 ? 0.3456 0.4127 0.4494 0.0055  0.0314  -0.0743 286 VAL B CB  
6472 C CG1 . VAL B 286 ? 0.4392 0.5175 0.5399 -0.0014 0.0434  -0.0884 286 VAL B CG1 
6473 C CG2 . VAL B 286 ? 0.2950 0.3662 0.3861 0.0006  0.0270  -0.0636 286 VAL B CG2 
6474 N N   . GLU B 287 ? 0.3736 0.4390 0.5400 0.0243  0.0433  -0.0968 287 GLU B N   
6475 C CA  . GLU B 287 ? 0.5033 0.5570 0.6857 0.0298  0.0490  -0.1065 287 GLU B CA  
6476 C C   . GLU B 287 ? 0.4738 0.5165 0.6319 0.0213  0.0518  -0.1124 287 GLU B C   
6477 O O   . GLU B 287 ? 0.3831 0.4348 0.5238 0.0107  0.0595  -0.1220 287 GLU B O   
6478 C CB  . GLU B 287 ? 0.5681 0.6333 0.7770 0.0327  0.0626  -0.1227 287 GLU B CB  
6479 C CG  . GLU B 287 ? 0.6442 0.7279 0.8407 0.0218  0.0729  -0.1336 287 GLU B CG  
6480 C CD  . GLU B 287 ? 0.7352 0.8331 0.9632 0.0261  0.0860  -0.1481 287 GLU B CD  
6481 O OE1 . GLU B 287 ? 0.7114 0.8135 0.9696 0.0376  0.0816  -0.1414 287 GLU B OE1 
6482 O OE2 . GLU B 287 ? 0.7670 0.8710 0.9863 0.0165  0.0985  -0.1631 287 GLU B OE2 
6483 N N   . ARG B 288 ? 0.5617 0.5865 0.7184 0.0251  0.0452  -0.1059 288 ARG B N   
6484 C CA  . ARG B 288 ? 0.5754 0.5893 0.7104 0.0176  0.0448  -0.1082 288 ARG B CA  
6485 C C   . ARG B 288 ? 0.6470 0.6726 0.7531 0.0050  0.0463  -0.1097 288 ARG B C   
6486 O O   . ARG B 288 ? 0.6889 0.7205 0.7866 -0.0039 0.0557  -0.1236 288 ARG B O   
6487 C CB  . ARG B 288 ? 0.6120 0.6153 0.7605 0.0181  0.0549  -0.1240 288 ARG B CB  
6488 C CG  . ARG B 288 ? 0.6930 0.6759 0.8561 0.0270  0.0488  -0.1159 288 ARG B CG  
6489 C CD  . ARG B 288 ? 0.6910 0.6598 0.8677 0.0268  0.0595  -0.1315 288 ARG B CD  
6490 N NE  . ARG B 288 ? 0.7912 0.7508 0.9983 0.0389  0.0585  -0.1251 288 ARG B NE  
6491 C CZ  . ARG B 288 ? 0.8039 0.7476 1.0207 0.0402  0.0613  -0.1259 288 ARG B CZ  
6492 N NH1 . ARG B 288 ? 0.8217 0.7565 1.0224 0.0304  0.0660  -0.1349 288 ARG B NH1 
6493 N NH2 . ARG B 288 ? 0.8198 0.7579 1.0629 0.0509  0.0593  -0.1171 288 ARG B NH2 
6494 N N   . ALA B 289 ? 0.5759 0.6046 0.6671 0.0036  0.0374  -0.0951 289 ALA B N   
6495 C CA  . ALA B 289 ? 0.5611 0.5985 0.6268 -0.0067 0.0364  -0.0913 289 ALA B CA  
6496 C C   . ALA B 289 ? 0.4290 0.4564 0.4799 -0.0093 0.0296  -0.0839 289 ALA B C   
6497 O O   . ALA B 289 ? 0.5185 0.5317 0.5767 -0.0032 0.0246  -0.0795 289 ALA B O   
6498 C CB  . ALA B 289 ? 0.4825 0.5280 0.5438 -0.0066 0.0323  -0.0800 289 ALA B CB  
6499 N N   . SER B 290 ? 0.3472 0.3830 0.3780 -0.0185 0.0290  -0.0812 290 SER B N   
6500 C CA  . SER B 290 ? 0.3234 0.3547 0.3410 -0.0226 0.0235  -0.0756 290 SER B CA  
6501 C C   . SER B 290 ? 0.2726 0.3017 0.2829 -0.0202 0.0151  -0.0583 290 SER B C   
6502 O O   . SER B 290 ? 0.3304 0.3674 0.3354 -0.0219 0.0151  -0.0518 290 SER B O   
6503 C CB  . SER B 290 ? 0.3133 0.3586 0.3144 -0.0353 0.0275  -0.0825 290 SER B CB  
6504 O OG  . SER B 290 ? 0.3908 0.4389 0.3781 -0.0397 0.0200  -0.0712 290 SER B OG  
6505 N N   . PRO B 291 ? 0.3059 0.3238 0.3162 -0.0168 0.0091  -0.0510 291 PRO B N   
6506 C CA  . PRO B 291 ? 0.2719 0.2876 0.2764 -0.0151 0.0032  -0.0364 291 PRO B CA  
6507 C C   . PRO B 291 ? 0.1866 0.2126 0.1782 -0.0219 0.0011  -0.0294 291 PRO B C   
6508 O O   . PRO B 291 ? 0.2824 0.3056 0.2722 -0.0200 -0.0028 -0.0176 291 PRO B O   
6509 C CB  . PRO B 291 ? 0.2495 0.2503 0.2599 -0.0099 -0.0010 -0.0331 291 PRO B CB  
6510 C CG  . PRO B 291 ? 0.3380 0.3363 0.3507 -0.0127 0.0015  -0.0438 291 PRO B CG  
6511 C CD  . PRO B 291 ? 0.3704 0.3770 0.3861 -0.0155 0.0086  -0.0564 291 PRO B CD  
6512 N N   . TYR B 292 ? 0.1934 0.2322 0.1767 -0.0304 0.0039  -0.0362 292 TYR B N   
6513 C CA  . TYR B 292 ? 0.2543 0.3055 0.2259 -0.0377 0.0001  -0.0281 292 TYR B CA  
6514 C C   . TYR B 292 ? 0.1825 0.2468 0.1455 -0.0425 0.0008  -0.0204 292 TYR B C   
6515 O O   . TYR B 292 ? 0.2160 0.2935 0.1693 -0.0493 -0.0030 -0.0118 292 TYR B O   
6516 C CB  . TYR B 292 ? 0.2837 0.3429 0.2487 -0.0468 0.0016  -0.0394 292 TYR B CB  
6517 C CG  . TYR B 292 ? 0.2256 0.2704 0.1995 -0.0431 0.0015  -0.0466 292 TYR B CG  
6518 C CD1 . TYR B 292 ? 0.2492 0.2828 0.2293 -0.0361 -0.0037 -0.0368 292 TYR B CD1 
6519 C CD2 . TYR B 292 ? 0.3516 0.3932 0.3278 -0.0471 0.0077  -0.0636 292 TYR B CD2 
6520 C CE1 . TYR B 292 ? 0.3290 0.3491 0.3161 -0.0337 -0.0036 -0.0423 292 TYR B CE1 
6521 C CE2 . TYR B 292 ? 0.3283 0.3547 0.3134 -0.0439 0.0080  -0.0691 292 TYR B CE2 
6522 C CZ  . TYR B 292 ? 0.4080 0.4240 0.3977 -0.0375 0.0019  -0.0577 292 TYR B CZ  
6523 O OH  . TYR B 292 ? 0.4750 0.4758 0.4725 -0.0355 0.0024  -0.0624 292 TYR B OH  
6524 N N   . LEU B 293 ? 0.2464 0.3080 0.2134 -0.0394 0.0049  -0.0218 293 LEU B N   
6525 C CA  . LEU B 293 ? 0.3106 0.3825 0.2703 -0.0442 0.0067  -0.0148 293 LEU B CA  
6526 C C   . LEU B 293 ? 0.2212 0.2833 0.1860 -0.0378 0.0041  -0.0005 293 LEU B C   
6527 O O   . LEU B 293 ? 0.2431 0.2912 0.2175 -0.0299 0.0027  0.0001  293 LEU B O   
6528 C CB  . LEU B 293 ? 0.3166 0.3932 0.2785 -0.0465 0.0147  -0.0279 293 LEU B CB  
6529 C CG  . LEU B 293 ? 0.3288 0.4171 0.2852 -0.0551 0.0214  -0.0442 293 LEU B CG  
6530 C CD1 . LEU B 293 ? 0.4641 0.5460 0.4249 -0.0540 0.0214  -0.0554 293 LEU B CD1 
6531 C CD2 . LEU B 293 ? 0.2946 0.3856 0.2596 -0.0541 0.0299  -0.0552 293 LEU B CD2 
6532 N N   . ARG B 294 ? 0.2591 0.3286 0.2173 -0.0424 0.0042  0.0107  294 ARG B N   
6533 C CA  . ARG B 294 ? 0.2108 0.2700 0.1747 -0.0379 0.0050  0.0209  294 ARG B CA  
6534 C C   . ARG B 294 ? 0.2195 0.2801 0.1847 -0.0398 0.0112  0.0130  294 ARG B C   
6535 O O   . ARG B 294 ? 0.2586 0.3323 0.2154 -0.0478 0.0148  0.0109  294 ARG B O   
6536 C CB  . ARG B 294 ? 0.2648 0.3286 0.2240 -0.0410 0.0023  0.0389  294 ARG B CB  
6537 C CG  . ARG B 294 ? 0.2579 0.3081 0.2244 -0.0369 0.0051  0.0481  294 ARG B CG  
6538 C CD  . ARG B 294 ? 0.2741 0.3246 0.2417 -0.0373 0.0026  0.0677  294 ARG B CD  
6539 N NE  . ARG B 294 ? 0.3296 0.3958 0.2854 -0.0467 0.0021  0.0759  294 ARG B NE  
6540 C CZ  . ARG B 294 ? 0.3575 0.4377 0.3078 -0.0508 -0.0041 0.0884  294 ARG B CZ  
6541 N NH1 . ARG B 294 ? 0.3215 0.4023 0.2790 -0.0456 -0.0100 0.0934  294 ARG B NH1 
6542 N NH2 . ARG B 294 ? 0.4261 0.5216 0.3634 -0.0610 -0.0047 0.0964  294 ARG B NH2 
6543 N N   . TYR B 295 ? 0.2253 0.2745 0.2008 -0.0335 0.0124  0.0086  295 TYR B N   
6544 C CA  . TYR B 295 ? 0.2145 0.2673 0.1944 -0.0351 0.0176  0.0010  295 TYR B CA  
6545 C C   . TYR B 295 ? 0.2934 0.3414 0.2728 -0.0374 0.0198  0.0105  295 TYR B C   
6546 O O   . TYR B 295 ? 0.2568 0.2931 0.2373 -0.0347 0.0178  0.0208  295 TYR B O   
6547 C CB  . TYR B 295 ? 0.2083 0.2548 0.2008 -0.0281 0.0168  -0.0087 295 TYR B CB  
6548 C CG  . TYR B 295 ? 0.2580 0.3088 0.2542 -0.0264 0.0171  -0.0204 295 TYR B CG  
6549 C CD1 . TYR B 295 ? 0.2145 0.2584 0.2097 -0.0233 0.0128  -0.0201 295 TYR B CD1 
6550 C CD2 . TYR B 295 ? 0.2379 0.2993 0.2401 -0.0283 0.0229  -0.0325 295 TYR B CD2 
6551 C CE1 . TYR B 295 ? 0.1867 0.2323 0.1859 -0.0226 0.0143  -0.0314 295 TYR B CE1 
6552 C CE2 . TYR B 295 ? 0.2189 0.2820 0.2267 -0.0267 0.0251  -0.0443 295 TYR B CE2 
6553 C CZ  . TYR B 295 ? 0.2404 0.2947 0.2463 -0.0241 0.0207  -0.0437 295 TYR B CZ  
6554 O OH  . TYR B 295 ? 0.3032 0.3571 0.3154 -0.0233 0.0240  -0.0563 295 TYR B OH  
6555 N N   . TYR B 296 ? 0.2845 0.3415 0.2634 -0.0430 0.0252  0.0064  296 TYR B N   
6556 C CA  . TYR B 296 ? 0.2531 0.3059 0.2322 -0.0468 0.0287  0.0132  296 TYR B CA  
6557 C C   . TYR B 296 ? 0.2169 0.2721 0.2066 -0.0460 0.0314  0.0027  296 TYR B C   
6558 O O   . TYR B 296 ? 0.2952 0.3644 0.2882 -0.0488 0.0352  -0.0070 296 TYR B O   
6559 C CB  . TYR B 296 ? 0.2687 0.3323 0.2369 -0.0564 0.0327  0.0196  296 TYR B CB  
6560 C CG  . TYR B 296 ? 0.3294 0.3937 0.2876 -0.0582 0.0287  0.0333  296 TYR B CG  
6561 C CD1 . TYR B 296 ? 0.4213 0.4715 0.3836 -0.0526 0.0247  0.0456  296 TYR B CD1 
6562 C CD2 . TYR B 296 ? 0.5060 0.5870 0.4517 -0.0663 0.0290  0.0338  296 TYR B CD2 
6563 C CE1 . TYR B 296 ? 0.3992 0.4526 0.3561 -0.0535 0.0201  0.0598  296 TYR B CE1 
6564 C CE2 . TYR B 296 ? 0.5709 0.6560 0.5078 -0.0689 0.0236  0.0479  296 TYR B CE2 
6565 C CZ  . TYR B 296 ? 0.5569 0.6284 0.5009 -0.0617 0.0186  0.0617  296 TYR B CZ  
6566 O OH  . TYR B 296 ? 0.5326 0.6104 0.4717 -0.0633 0.0124  0.0775  296 TYR B OH  
6567 N N   . PHE B 297 ? 0.2089 0.2521 0.2047 -0.0428 0.0297  0.0044  297 PHE B N   
6568 C CA  . PHE B 297 ? 0.1664 0.2141 0.1725 -0.0427 0.0303  -0.0037 297 PHE B CA  
6569 C C   . PHE B 297 ? 0.1894 0.2421 0.1943 -0.0515 0.0365  -0.0023 297 PHE B C   
6570 O O   . PHE B 297 ? 0.2066 0.2474 0.2074 -0.0554 0.0388  0.0054  297 PHE B O   
6571 C CB  . PHE B 297 ? 0.1696 0.2046 0.1796 -0.0386 0.0259  -0.0027 297 PHE B CB  
6572 C CG  . PHE B 297 ? 0.1921 0.2342 0.2119 -0.0401 0.0251  -0.0091 297 PHE B CG  
6573 C CD1 . PHE B 297 ? 0.2072 0.2610 0.2384 -0.0352 0.0216  -0.0162 297 PHE B CD1 
6574 C CD2 . PHE B 297 ? 0.1782 0.2160 0.1971 -0.0470 0.0278  -0.0075 297 PHE B CD2 
6575 C CE1 . PHE B 297 ? 0.1807 0.2445 0.2234 -0.0365 0.0194  -0.0201 297 PHE B CE1 
6576 C CE2 . PHE B 297 ? 0.2364 0.2839 0.2638 -0.0500 0.0260  -0.0130 297 PHE B CE2 
6577 C CZ  . PHE B 297 ? 0.2231 0.2851 0.2630 -0.0444 0.0210  -0.0184 297 PHE B CZ  
6578 N N   . ARG B 298 ? 0.1758 0.2457 0.1854 -0.0550 0.0404  -0.0102 298 ARG B N   
6579 C CA  . ARG B 298 ? 0.1839 0.2619 0.1934 -0.0644 0.0471  -0.0105 298 ARG B CA  
6580 C C   . ARG B 298 ? 0.2210 0.2917 0.2166 -0.0716 0.0509  0.0014  298 ARG B C   
6581 O O   . ARG B 298 ? 0.3029 0.3717 0.2973 -0.0795 0.0559  0.0051  298 ARG B O   
6582 C CB  . ARG B 298 ? 0.2421 0.3175 0.2606 -0.0663 0.0463  -0.0126 298 ARG B CB  
6583 C CG  . ARG B 298 ? 0.2600 0.3456 0.2937 -0.0595 0.0410  -0.0215 298 ARG B CG  
6584 C CD  . ARG B 298 ? 0.2556 0.3432 0.2972 -0.0634 0.0388  -0.0232 298 ARG B CD  
6585 N NE  . ARG B 298 ? 0.2427 0.3453 0.3013 -0.0572 0.0333  -0.0296 298 ARG B NE  
6586 C CZ  . ARG B 298 ? 0.2745 0.3848 0.3428 -0.0593 0.0285  -0.0310 298 ARG B CZ  
6587 N NH1 . ARG B 298 ? 0.2559 0.3601 0.3172 -0.0688 0.0296  -0.0289 298 ARG B NH1 
6588 N NH2 . ARG B 298 ? 0.2716 0.3966 0.3576 -0.0523 0.0227  -0.0343 298 ARG B NH2 
6589 N N   . GLU B 299 ? 0.2471 0.3144 0.2332 -0.0693 0.0483  0.0083  299 GLU B N   
6590 C CA  . GLU B 299 ? 0.2344 0.2952 0.2089 -0.0746 0.0497  0.0232  299 GLU B CA  
6591 C C   . GLU B 299 ? 0.3080 0.3482 0.2853 -0.0742 0.0506  0.0331  299 GLU B C   
6592 O O   . GLU B 299 ? 0.3160 0.3500 0.2882 -0.0802 0.0542  0.0451  299 GLU B O   
6593 C CB  . GLU B 299 ? 0.2916 0.3667 0.2580 -0.0860 0.0563  0.0243  299 GLU B CB  
6594 C CG  . GLU B 299 ? 0.3166 0.4122 0.2786 -0.0885 0.0580  0.0137  299 GLU B CG  
6595 C CD  . GLU B 299 ? 0.6348 0.7334 0.5827 -0.0899 0.0540  0.0222  299 GLU B CD  
6596 O OE1 . GLU B 299 ? 0.5759 0.6622 0.5193 -0.0884 0.0496  0.0386  299 GLU B OE1 
6597 O OE2 . GLU B 299 ? 0.7697 0.8841 0.7118 -0.0936 0.0559  0.0127  299 GLU B OE2 
6598 N N   . LEU B 300 ? 0.2240 0.2530 0.2094 -0.0680 0.0479  0.0282  300 LEU B N   
6599 C CA  . LEU B 300 ? 0.2534 0.2621 0.2421 -0.0682 0.0505  0.0342  300 LEU B CA  
6600 C C   . LEU B 300 ? 0.3170 0.3115 0.3074 -0.0597 0.0465  0.0403  300 LEU B C   
6601 O O   . LEU B 300 ? 0.3410 0.3194 0.3336 -0.0594 0.0498  0.0504  300 LEU B O   
6602 C CB  . LEU B 300 ? 0.2653 0.2731 0.2609 -0.0709 0.0519  0.0229  300 LEU B CB  
6603 C CG  . LEU B 300 ? 0.2888 0.3122 0.2867 -0.0794 0.0559  0.0157  300 LEU B CG  
6604 C CD1 . LEU B 300 ? 0.3449 0.3712 0.3508 -0.0813 0.0545  0.0052  300 LEU B CD1 
6605 C CD2 . LEU B 300 ? 0.2289 0.2454 0.2222 -0.0891 0.0637  0.0244  300 LEU B CD2 
6606 N N   . ILE B 301 ? 0.2631 0.2628 0.2547 -0.0526 0.0404  0.0341  301 ILE B N   
6607 C CA  . ILE B 301 ? 0.2676 0.2551 0.2619 -0.0452 0.0372  0.0376  301 ILE B CA  
6608 C C   . ILE B 301 ? 0.2425 0.2410 0.2342 -0.0398 0.0306  0.0356  301 ILE B C   
6609 O O   . ILE B 301 ? 0.2853 0.2968 0.2764 -0.0402 0.0287  0.0262  301 ILE B O   
6610 C CB  . ILE B 301 ? 0.2873 0.2644 0.2862 -0.0446 0.0381  0.0294  301 ILE B CB  
6611 C CG1 . ILE B 301 ? 0.2604 0.2249 0.2619 -0.0381 0.0365  0.0324  301 ILE B CG1 
6612 C CG2 . ILE B 301 ? 0.2979 0.2885 0.2983 -0.0447 0.0339  0.0174  301 ILE B CG2 
6613 C CD1 . ILE B 301 ? 0.3131 0.2674 0.3163 -0.0398 0.0385  0.0244  301 ILE B CD1 
6614 N N   . SER B 302 ? 0.2389 0.2326 0.2308 -0.0351 0.0276  0.0442  302 SER B N   
6615 C CA  . SER B 302 ? 0.1784 0.1820 0.1674 -0.0315 0.0217  0.0420  302 SER B CA  
6616 C C   . SER B 302 ? 0.1805 0.1783 0.1740 -0.0259 0.0187  0.0333  302 SER B C   
6617 O O   . SER B 302 ? 0.2367 0.2213 0.2346 -0.0239 0.0204  0.0337  302 SER B O   
6618 C CB  . SER B 302 ? 0.3477 0.3523 0.3359 -0.0299 0.0189  0.0558  302 SER B CB  
6619 O OG  . SER B 302 ? 0.3518 0.3645 0.3339 -0.0361 0.0202  0.0656  302 SER B OG  
6620 N N   . VAL B 303 ? 0.1777 0.1849 0.1700 -0.0244 0.0151  0.0250  303 VAL B N   
6621 C CA  . VAL B 303 ? 0.1846 0.1868 0.1811 -0.0195 0.0117  0.0180  303 VAL B CA  
6622 C C   . VAL B 303 ? 0.1796 0.1872 0.1740 -0.0172 0.0076  0.0165  303 VAL B C   
6623 O O   . VAL B 303 ? 0.2329 0.2523 0.2237 -0.0201 0.0079  0.0127  303 VAL B O   
6624 C CB  . VAL B 303 ? 0.2434 0.2503 0.2445 -0.0198 0.0117  0.0081  303 VAL B CB  
6625 C CG1 . VAL B 303 ? 0.1873 0.1891 0.1928 -0.0150 0.0072  0.0037  303 VAL B CG1 
6626 C CG2 . VAL B 303 ? 0.2211 0.2248 0.2235 -0.0241 0.0155  0.0088  303 VAL B CG2 
6627 N N   . PHE B 304 ? 0.2011 0.2006 0.1977 -0.0133 0.0048  0.0183  304 PHE B N   
6628 C CA  . PHE B 304 ? 0.2082 0.2112 0.2040 -0.0118 0.0011  0.0152  304 PHE B CA  
6629 C C   . PHE B 304 ? 0.2097 0.2053 0.2099 -0.0083 -0.0009 0.0082  304 PHE B C   
6630 O O   . PHE B 304 ? 0.2480 0.2346 0.2502 -0.0069 -0.0008 0.0096  304 PHE B O   
6631 C CB  . PHE B 304 ? 0.2722 0.2739 0.2681 -0.0108 -0.0009 0.0243  304 PHE B CB  
6632 C CG  . PHE B 304 ? 0.2071 0.2204 0.1988 -0.0145 -0.0016 0.0326  304 PHE B CG  
6633 C CD1 . PHE B 304 ? 0.2228 0.2497 0.2080 -0.0190 -0.0040 0.0291  304 PHE B CD1 
6634 C CD2 . PHE B 304 ? 0.2259 0.2365 0.2203 -0.0143 0.0004  0.0445  304 PHE B CD2 
6635 C CE1 . PHE B 304 ? 0.2202 0.2605 0.1994 -0.0243 -0.0057 0.0383  304 PHE B CE1 
6636 C CE2 . PHE B 304 ? 0.1888 0.2109 0.1799 -0.0178 -0.0015 0.0553  304 PHE B CE2 
6637 C CZ  . PHE B 304 ? 0.2291 0.2675 0.2114 -0.0233 -0.0052 0.0527  304 PHE B CZ  
6638 N N   . PHE B 305 ? 0.2326 0.2323 0.2342 -0.0077 -0.0023 0.0006  305 PHE B N   
6639 C CA  . PHE B 305 ? 0.2151 0.2074 0.2224 -0.0041 -0.0048 -0.0041 305 PHE B CA  
6640 C C   . PHE B 305 ? 0.1990 0.1865 0.2045 -0.0037 -0.0072 -0.0029 305 PHE B C   
6641 O O   . PHE B 305 ? 0.2219 0.2161 0.2247 -0.0064 -0.0070 -0.0055 305 PHE B O   
6642 C CB  . PHE B 305 ? 0.2093 0.2073 0.2235 -0.0029 -0.0035 -0.0133 305 PHE B CB  
6643 C CG  . PHE B 305 ? 0.2267 0.2311 0.2448 -0.0034 -0.0012 -0.0146 305 PHE B CG  
6644 C CD1 . PHE B 305 ? 0.2318 0.2469 0.2458 -0.0079 0.0032  -0.0161 305 PHE B CD1 
6645 C CD2 . PHE B 305 ? 0.2109 0.2123 0.2358 -0.0009 -0.0037 -0.0133 305 PHE B CD2 
6646 C CE1 . PHE B 305 ? 0.2453 0.2671 0.2634 -0.0094 0.0059  -0.0175 305 PHE B CE1 
6647 C CE2 . PHE B 305 ? 0.2159 0.2256 0.2454 -0.0025 -0.0018 -0.0146 305 PHE B CE2 
6648 C CZ  . PHE B 305 ? 0.2335 0.2528 0.2600 -0.0066 0.0034  -0.0171 305 PHE B CZ  
6649 N N   . ARG B 306 ? 0.2099 0.1873 0.2161 -0.0019 -0.0092 0.0008  306 ARG B N   
6650 C CA  . ARG B 306 ? 0.2159 0.1896 0.2210 -0.0023 -0.0108 0.0025  306 ARG B CA  
6651 C C   . ARG B 306 ? 0.1946 0.1670 0.2025 -0.0023 -0.0121 -0.0045 306 ARG B C   
6652 O O   . ARG B 306 ? 0.2282 0.1982 0.2416 -0.0001 -0.0121 -0.0095 306 ARG B O   
6653 C CB  . ARG B 306 ? 0.2743 0.2379 0.2789 -0.0016 -0.0112 0.0070  306 ARG B CB  
6654 C CG  . ARG B 306 ? 0.2799 0.2359 0.2863 -0.0004 -0.0139 0.0047  306 ARG B CG  
6655 C CD  . ARG B 306 ? 0.2687 0.2160 0.2715 -0.0021 -0.0143 0.0088  306 ARG B CD  
6656 N NE  . ARG B 306 ? 0.3051 0.2472 0.3093 -0.0015 -0.0184 0.0089  306 ARG B NE  
6657 C CZ  . ARG B 306 ? 0.2874 0.2218 0.2884 -0.0035 -0.0204 0.0121  306 ARG B CZ  
6658 N NH1 . ARG B 306 ? 0.2366 0.1676 0.2330 -0.0066 -0.0175 0.0137  306 ARG B NH1 
6659 N NH2 . ARG B 306 ? 0.2479 0.1788 0.2517 -0.0025 -0.0252 0.0144  306 ARG B NH2 
6660 N N   . ASP B 307 ? 0.2097 0.1842 0.2156 -0.0051 -0.0127 -0.0051 307 ASP B N   
6661 C CA  . ASP B 307 ? 0.2046 0.1746 0.2132 -0.0064 -0.0130 -0.0122 307 ASP B CA  
6662 C C   . ASP B 307 ? 0.2697 0.2259 0.2811 -0.0040 -0.0150 -0.0090 307 ASP B C   
6663 O O   . ASP B 307 ? 0.2313 0.1846 0.2401 -0.0057 -0.0159 -0.0042 307 ASP B O   
6664 C CB  . ASP B 307 ? 0.2348 0.2131 0.2393 -0.0122 -0.0133 -0.0138 307 ASP B CB  
6665 C CG  . ASP B 307 ? 0.3169 0.2903 0.3237 -0.0153 -0.0120 -0.0236 307 ASP B CG  
6666 O OD1 . ASP B 307 ? 0.2969 0.2564 0.3089 -0.0127 -0.0124 -0.0241 307 ASP B OD1 
6667 O OD2 . ASP B 307 ? 0.3405 0.3236 0.3435 -0.0214 -0.0102 -0.0309 307 ASP B OD2 
6668 N N   . LYS B 308 ? 0.2186 0.1676 0.2363 -0.0004 -0.0157 -0.0111 308 LYS B N   
6669 C CA  . LYS B 308 ? 0.2492 0.1867 0.2682 0.0011  -0.0188 -0.0054 308 LYS B CA  
6670 C C   . LYS B 308 ? 0.3402 0.2689 0.3590 -0.0017 -0.0191 -0.0059 308 LYS B C   
6671 O O   . LYS B 308 ? 0.2172 0.1400 0.2315 -0.0038 -0.0206 0.0002  308 LYS B O   
6672 C CB  . LYS B 308 ? 0.2146 0.1488 0.2429 0.0059  -0.0208 -0.0054 308 LYS B CB  
6673 C CG  . LYS B 308 ? 0.2996 0.2227 0.3303 0.0069  -0.0253 0.0017  308 LYS B CG  
6674 C CD  . LYS B 308 ? 0.3794 0.3028 0.4235 0.0126  -0.0279 0.0027  308 LYS B CD  
6675 C CE  . LYS B 308 ? 0.5232 0.4351 0.5731 0.0143  -0.0329 0.0108  308 LYS B CE  
6676 N NZ  . LYS B 308 ? 0.4666 0.3766 0.5031 0.0091  -0.0369 0.0203  308 LYS B NZ  
6677 N N   . THR B 309 ? 0.2795 0.2069 0.3028 -0.0031 -0.0169 -0.0139 309 THR B N   
6678 C CA  . THR B 309 ? 0.2769 0.1941 0.3009 -0.0067 -0.0168 -0.0146 309 THR B CA  
6679 C C   . THR B 309 ? 0.1905 0.1143 0.2067 -0.0123 -0.0168 -0.0120 309 THR B C   
6680 O O   . THR B 309 ? 0.2662 0.1827 0.2807 -0.0150 -0.0176 -0.0078 309 THR B O   
6681 C CB  . THR B 309 ? 0.4190 0.3316 0.4501 -0.0083 -0.0130 -0.0256 309 THR B CB  
6682 O OG1 . THR B 309 ? 0.6115 0.5378 0.6369 -0.0140 -0.0103 -0.0332 309 THR B OG1 
6683 C CG2 . THR B 309 ? 0.3550 0.2632 0.3983 -0.0017 -0.0116 -0.0290 309 THR B CG2 
6684 N N   . LEU B 310 ? 0.1968 0.1355 0.2093 -0.0140 -0.0161 -0.0132 310 LEU B N   
6685 C CA  . LEU B 310 ? 0.2187 0.1660 0.2280 -0.0180 -0.0165 -0.0091 310 LEU B CA  
6686 C C   . LEU B 310 ? 0.2027 0.1464 0.2108 -0.0157 -0.0166 -0.0005 310 LEU B C   
6687 O O   . LEU B 310 ? 0.2584 0.2017 0.2667 -0.0187 -0.0160 0.0026  310 LEU B O   
6688 C CB  . LEU B 310 ? 0.2327 0.1978 0.2399 -0.0198 -0.0167 -0.0094 310 LEU B CB  
6689 C CG  . LEU B 310 ? 0.3184 0.2910 0.3237 -0.0257 -0.0159 -0.0191 310 LEU B CG  
6690 C CD1 . LEU B 310 ? 0.2239 0.2160 0.2248 -0.0284 -0.0173 -0.0161 310 LEU B CD1 
6691 C CD2 . LEU B 310 ? 0.4033 0.3742 0.4093 -0.0327 -0.0159 -0.0233 310 LEU B CD2 
6692 N N   . SER B 311 ? 0.1994 0.1411 0.2064 -0.0113 -0.0166 0.0024  311 SER B N   
6693 C CA  . SER B 311 ? 0.2267 0.1641 0.2311 -0.0108 -0.0154 0.0084  311 SER B CA  
6694 C C   . SER B 311 ? 0.2490 0.1743 0.2508 -0.0133 -0.0164 0.0103  311 SER B C   
6695 O O   . SER B 311 ? 0.2383 0.1616 0.2373 -0.0165 -0.0142 0.0135  311 SER B O   
6696 C CB  . SER B 311 ? 0.2315 0.1699 0.2345 -0.0075 -0.0151 0.0096  311 SER B CB  
6697 O OG  . SER B 311 ? 0.1944 0.1435 0.1992 -0.0061 -0.0141 0.0089  311 SER B OG  
6698 N N   . ASP B 312 ? 0.2164 0.1336 0.2202 -0.0120 -0.0192 0.0088  312 ASP B N   
6699 C CA  . ASP B 312 ? 0.1963 0.1015 0.1979 -0.0146 -0.0211 0.0132  312 ASP B CA  
6700 C C   . ASP B 312 ? 0.2735 0.1747 0.2753 -0.0198 -0.0195 0.0120  312 ASP B C   
6701 O O   . ASP B 312 ? 0.2344 0.1274 0.2319 -0.0240 -0.0196 0.0168  312 ASP B O   
6702 C CB  . ASP B 312 ? 0.2143 0.1119 0.2219 -0.0105 -0.0248 0.0140  312 ASP B CB  
6703 C CG  . ASP B 312 ? 0.3264 0.2278 0.3327 -0.0074 -0.0276 0.0181  312 ASP B CG  
6704 O OD1 . ASP B 312 ? 0.2695 0.1757 0.2678 -0.0101 -0.0262 0.0202  312 ASP B OD1 
6705 O OD2 . ASP B 312 ? 0.2835 0.1835 0.2984 -0.0027 -0.0307 0.0186  312 ASP B OD2 
6706 N N   . LEU B 313 ? 0.2179 0.1256 0.2239 -0.0211 -0.0180 0.0056  313 LEU B N   
6707 C CA  . LEU B 313 ? 0.2731 0.1798 0.2795 -0.0276 -0.0163 0.0040  313 LEU B CA  
6708 C C   . LEU B 313 ? 0.2277 0.1398 0.2309 -0.0308 -0.0140 0.0089  313 LEU B C   
6709 O O   . LEU B 313 ? 0.2603 0.1653 0.2609 -0.0360 -0.0127 0.0116  313 LEU B O   
6710 C CB  . LEU B 313 ? 0.2889 0.2070 0.2987 -0.0302 -0.0156 -0.0036 313 LEU B CB  
6711 C CG  . LEU B 313 ? 0.3671 0.2786 0.3806 -0.0311 -0.0150 -0.0122 313 LEU B CG  
6712 C CD1 . LEU B 313 ? 0.3496 0.2775 0.3626 -0.0359 -0.0143 -0.0194 313 LEU B CD1 
6713 C CD2 . LEU B 313 ? 0.2976 0.1929 0.3132 -0.0356 -0.0139 -0.0129 313 LEU B CD2 
6714 N N   . ILE B 314 ? 0.1998 0.1241 0.2043 -0.0279 -0.0125 0.0100  314 ILE B N   
6715 C CA  . ILE B 314 ? 0.2370 0.1664 0.2422 -0.0298 -0.0084 0.0135  314 ILE B CA  
6716 C C   . ILE B 314 ? 0.2948 0.2133 0.2918 -0.0318 -0.0066 0.0169  314 ILE B C   
6717 O O   . ILE B 314 ? 0.2783 0.1948 0.2730 -0.0373 -0.0029 0.0184  314 ILE B O   
6718 C CB  . ILE B 314 ? 0.2503 0.1927 0.2613 -0.0251 -0.0068 0.0148  314 ILE B CB  
6719 C CG1 . ILE B 314 ? 0.2220 0.1787 0.2395 -0.0256 -0.0095 0.0132  314 ILE B CG1 
6720 C CG2 . ILE B 314 ? 0.2016 0.1468 0.2163 -0.0256 -0.0006 0.0175  314 ILE B CG2 
6721 C CD1 . ILE B 314 ? 0.2368 0.2070 0.2607 -0.0210 -0.0093 0.0172  314 ILE B CD1 
6722 N N   . GLY B 315 ? 0.2393 0.1520 0.2315 -0.0285 -0.0094 0.0182  315 GLY B N   
6723 C CA  . GLY B 315 ? 0.2141 0.1200 0.1969 -0.0318 -0.0085 0.0218  315 GLY B CA  
6724 C C   . GLY B 315 ? 0.2613 0.1563 0.2376 -0.0372 -0.0114 0.0263  315 GLY B C   
6725 O O   . GLY B 315 ? 0.2703 0.1622 0.2369 -0.0435 -0.0093 0.0297  315 GLY B O   
6726 N N   . PHE B 316 ? 0.2479 0.1364 0.2291 -0.0355 -0.0156 0.0265  316 PHE B N   
6727 C CA  . PHE B 316 ? 0.2680 0.1437 0.2447 -0.0398 -0.0189 0.0331  316 PHE B CA  
6728 C C   . PHE B 316 ? 0.2543 0.1230 0.2356 -0.0437 -0.0177 0.0316  316 PHE B C   
6729 O O   . PHE B 316 ? 0.3368 0.1957 0.3126 -0.0501 -0.0181 0.0378  316 PHE B O   
6730 C CB  . PHE B 316 ? 0.2808 0.1506 0.2610 -0.0340 -0.0257 0.0375  316 PHE B CB  
6731 C CG  . PHE B 316 ? 0.2962 0.1728 0.2708 -0.0324 -0.0277 0.0400  316 PHE B CG  
6732 C CD1 . PHE B 316 ? 0.2856 0.1622 0.2471 -0.0398 -0.0282 0.0462  316 PHE B CD1 
6733 C CD2 . PHE B 316 ? 0.2870 0.1711 0.2682 -0.0254 -0.0285 0.0354  316 PHE B CD2 
6734 C CE1 . PHE B 316 ? 0.3309 0.2146 0.2861 -0.0405 -0.0297 0.0471  316 PHE B CE1 
6735 C CE2 . PHE B 316 ? 0.3374 0.2281 0.3135 -0.0253 -0.0300 0.0371  316 PHE B CE2 
6736 C CZ  . PHE B 316 ? 0.3644 0.2549 0.3276 -0.0331 -0.0306 0.0426  316 PHE B CZ  
6737 N N   . SER B 317 ? 0.2424 0.1161 0.2325 -0.0415 -0.0162 0.0238  317 SER B N   
6738 C CA  . SER B 317 ? 0.2362 0.1021 0.2306 -0.0465 -0.0151 0.0212  317 SER B CA  
6739 C C   . SER B 317 ? 0.2617 0.1373 0.2563 -0.0538 -0.0105 0.0179  317 SER B C   
6740 O O   . SER B 317 ? 0.2798 0.1480 0.2722 -0.0615 -0.0086 0.0201  317 SER B O   
6741 C CB  . SER B 317 ? 0.2423 0.1066 0.2460 -0.0422 -0.0160 0.0133  317 SER B CB  
6742 O OG  . SER B 317 ? 0.3435 0.1964 0.3513 -0.0480 -0.0142 0.0100  317 SER B OG  
6743 N N   . TYR B 318 ? 0.2215 0.1145 0.2199 -0.0516 -0.0088 0.0138  318 TYR B N   
6744 C CA  . TYR B 318 ? 0.2320 0.1378 0.2359 -0.0574 -0.0057 0.0104  318 TYR B CA  
6745 C C   . TYR B 318 ? 0.2140 0.1211 0.2153 -0.0638 -0.0008 0.0143  318 TYR B C   
6746 O O   . TYR B 318 ? 0.2680 0.1844 0.2752 -0.0700 0.0019  0.0120  318 TYR B O   
6747 C CB  . TYR B 318 ? 0.2186 0.1441 0.2292 -0.0526 -0.0060 0.0081  318 TYR B CB  
6748 C CG  . TYR B 318 ? 0.1953 0.1264 0.2088 -0.0509 -0.0094 0.0023  318 TYR B CG  
6749 C CD1 . TYR B 318 ? 0.2035 0.1241 0.2164 -0.0551 -0.0102 -0.0035 318 TYR B CD1 
6750 C CD2 . TYR B 318 ? 0.1815 0.1283 0.1984 -0.0460 -0.0110 0.0024  318 TYR B CD2 
6751 C CE1 . TYR B 318 ? 0.2259 0.1524 0.2404 -0.0553 -0.0117 -0.0111 318 TYR B CE1 
6752 C CE2 . TYR B 318 ? 0.2487 0.2025 0.2659 -0.0464 -0.0137 -0.0032 318 TYR B CE2 
6753 C CZ  . TYR B 318 ? 0.2339 0.1781 0.2493 -0.0514 -0.0136 -0.0109 318 TYR B CZ  
6754 O OH  . TYR B 318 ? 0.2775 0.2293 0.2920 -0.0534 -0.0147 -0.0186 318 TYR B OH  
6755 N N   . HIS B 319 ? 0.2176 0.1177 0.2103 -0.0636 0.0007  0.0194  319 HIS B N   
6756 C CA  . HIS B 319 ? 0.2630 0.1649 0.2517 -0.0713 0.0070  0.0216  319 HIS B CA  
6757 C C   . HIS B 319 ? 0.2458 0.1398 0.2329 -0.0810 0.0080  0.0226  319 HIS B C   
6758 O O   . HIS B 319 ? 0.2860 0.1872 0.2750 -0.0885 0.0140  0.0218  319 HIS B O   
6759 C CB  . HIS B 319 ? 0.3197 0.2138 0.2953 -0.0725 0.0081  0.0264  319 HIS B CB  
6760 C CG  . HIS B 319 ? 0.3252 0.2022 0.2904 -0.0753 0.0024  0.0334  319 HIS B CG  
6761 N ND1 . HIS B 319 ? 0.2977 0.1675 0.2636 -0.0678 -0.0048 0.0356  319 HIS B ND1 
6762 C CD2 . HIS B 319 ? 0.3667 0.2329 0.3223 -0.0845 0.0026  0.0398  319 HIS B CD2 
6763 C CE1 . HIS B 319 ? 0.3653 0.2209 0.3246 -0.0712 -0.0091 0.0438  319 HIS B CE1 
6764 N NE2 . HIS B 319 ? 0.3690 0.2224 0.3213 -0.0812 -0.0050 0.0470  319 HIS B NE2 
6765 N N   . ALA B 320 ? 0.2797 0.1586 0.2650 -0.0813 0.0030  0.0240  320 ALA B N   
6766 C CA  . ALA B 320 ? 0.3231 0.1903 0.3070 -0.0908 0.0042  0.0256  320 ALA B CA  
6767 C C   . ALA B 320 ? 0.2901 0.1631 0.2846 -0.0940 0.0047  0.0174  320 ALA B C   
6768 O O   . ALA B 320 ? 0.3368 0.1989 0.3314 -0.1026 0.0061  0.0172  320 ALA B O   
6769 C CB  . ALA B 320 ? 0.3565 0.2028 0.3348 -0.0890 -0.0005 0.0331  320 ALA B CB  
6770 N N   . TRP B 321 ? 0.2482 0.1387 0.2510 -0.0888 0.0035  0.0110  321 TRP B N   
6771 C CA  . TRP B 321 ? 0.2996 0.1999 0.3108 -0.0935 0.0031  0.0030  321 TRP B CA  
6772 C C   . TRP B 321 ? 0.2942 0.2181 0.3137 -0.0986 0.0062  0.0016  321 TRP B C   
6773 O O   . TRP B 321 ? 0.3587 0.2947 0.3810 -0.0942 0.0085  0.0052  321 TRP B O   
6774 C CB  . TRP B 321 ? 0.2437 0.1517 0.2584 -0.0861 -0.0010 -0.0026 321 TRP B CB  
6775 C CG  . TRP B 321 ? 0.2815 0.1713 0.2931 -0.0799 -0.0035 -0.0037 321 TRP B CG  
6776 C CD1 . TRP B 321 ? 0.2826 0.1548 0.2890 -0.0747 -0.0048 0.0034  321 TRP B CD1 
6777 C CD2 . TRP B 321 ? 0.2808 0.1709 0.2955 -0.0784 -0.0049 -0.0125 321 TRP B CD2 
6778 N NE1 . TRP B 321 ? 0.3399 0.2015 0.3492 -0.0688 -0.0069 0.0000  321 TRP B NE1 
6779 C CE2 . TRP B 321 ? 0.3325 0.2041 0.3465 -0.0711 -0.0061 -0.0107 321 TRP B CE2 
6780 C CE3 . TRP B 321 ? 0.3098 0.2157 0.3278 -0.0837 -0.0051 -0.0219 321 TRP B CE3 
6781 C CZ2 . TRP B 321 ? 0.3396 0.2068 0.3577 -0.0680 -0.0059 -0.0193 321 TRP B CZ2 
6782 C CZ3 . TRP B 321 ? 0.3638 0.2652 0.3823 -0.0822 -0.0050 -0.0308 321 TRP B CZ3 
6783 C CH2 . TRP B 321 ? 0.3683 0.2498 0.3876 -0.0740 -0.0046 -0.0301 321 TRP B CH2 
6784 N N   . ASN B 322 ? 0.3195 0.2510 0.3448 -0.1079 0.0065  -0.0041 322 ASN B N   
6785 C CA  . ASN B 322 ? 0.3238 0.2836 0.3609 -0.1117 0.0071  -0.0058 322 ASN B CA  
6786 C C   . ASN B 322 ? 0.2989 0.2777 0.3421 -0.1017 0.0028  -0.0048 322 ASN B C   
6787 O O   . ASN B 322 ? 0.3914 0.3663 0.4302 -0.0977 -0.0015 -0.0081 322 ASN B O   
6788 C CB  . ASN B 322 ? 0.3610 0.3259 0.4017 -0.1244 0.0066  -0.0133 322 ASN B CB  
6789 C CG  . ASN B 322 ? 0.3904 0.3887 0.4445 -0.1284 0.0047  -0.0146 322 ASN B CG  
6790 O OD1 . ASN B 322 ? 0.4928 0.5073 0.5499 -0.1269 -0.0008 -0.0174 322 ASN B OD1 
6791 N ND2 . ASN B 322 ? 0.4352 0.4460 0.4984 -0.1340 0.0091  -0.0118 322 ASN B ND2 
6792 N N   . ALA B 323 ? 0.2501 0.1992 0.3161 -0.0616 0.0004  0.0039  323 ALA B N   
6793 C CA  . ALA B 323 ? 0.2629 0.2257 0.3263 -0.0521 -0.0042 0.0010  323 ALA B CA  
6794 C C   . ALA B 323 ? 0.2823 0.2482 0.3437 -0.0571 -0.0114 -0.0084 323 ALA B C   
6795 O O   . ALA B 323 ? 0.2390 0.2014 0.2912 -0.0495 -0.0143 -0.0123 323 ALA B O   
6796 C CB  . ALA B 323 ? 0.3115 0.3004 0.3851 -0.0482 -0.0031 0.0068  323 ALA B CB  
6797 N N   . GLU B 324 ? 0.2375 0.2122 0.3073 -0.0707 -0.0145 -0.0121 324 GLU B N   
6798 C CA  . GLU B 324 ? 0.2638 0.2422 0.3297 -0.0769 -0.0219 -0.0223 324 GLU B CA  
6799 C C   . GLU B 324 ? 0.2688 0.2167 0.3189 -0.0754 -0.0211 -0.0302 324 GLU B C   
6800 O O   . GLU B 324 ? 0.3174 0.2658 0.3579 -0.0703 -0.0250 -0.0366 324 GLU B O   
6801 C CB  . GLU B 324 ? 0.3364 0.3299 0.4142 -0.0946 -0.0255 -0.0255 324 GLU B CB  
6802 C CG  . GLU B 324 ? 0.4751 0.4760 0.5478 -0.1026 -0.0343 -0.0369 324 GLU B CG  
6803 C CD  . GLU B 324 ? 0.7363 0.7695 0.8126 -0.0941 -0.0407 -0.0342 324 GLU B CD  
6804 O OE1 . GLU B 324 ? 0.8239 0.8761 0.9109 -0.0854 -0.0382 -0.0239 324 GLU B OE1 
6805 O OE2 . GLU B 324 ? 0.7460 0.7845 0.8131 -0.0952 -0.0476 -0.0421 324 GLU B OE2 
6806 N N   . ASP B 325 ? 0.2683 0.1896 0.3152 -0.0787 -0.0152 -0.0293 325 ASP B N   
6807 C CA  . ASP B 325 ? 0.3771 0.2683 0.4095 -0.0748 -0.0132 -0.0362 325 ASP B CA  
6808 C C   . ASP B 325 ? 0.3754 0.2657 0.3996 -0.0577 -0.0119 -0.0336 325 ASP B C   
6809 O O   . ASP B 325 ? 0.3327 0.2125 0.3459 -0.0525 -0.0126 -0.0411 325 ASP B O   
6810 C CB  . ASP B 325 ? 0.3626 0.2245 0.3934 -0.0789 -0.0063 -0.0328 325 ASP B CB  
6811 C CG  . ASP B 325 ? 0.4653 0.3238 0.5034 -0.0985 -0.0068 -0.0360 325 ASP B CG  
6812 O OD1 . ASP B 325 ? 0.4808 0.3534 0.5212 -0.1098 -0.0134 -0.0453 325 ASP B OD1 
6813 O OD2 . ASP B 325 ? 0.5550 0.3968 0.5958 -0.1034 -0.0005 -0.0288 325 ASP B OD2 
6814 N N   . ALA B 326 ? 0.2514 0.1525 0.2804 -0.0493 -0.0094 -0.0234 326 ALA B N   
6815 C CA  . ALA B 326 ? 0.2800 0.1813 0.3019 -0.0357 -0.0084 -0.0210 326 ALA B CA  
6816 C C   . ALA B 326 ? 0.2610 0.1790 0.2800 -0.0326 -0.0135 -0.0254 326 ALA B C   
6817 O O   . ALA B 326 ? 0.2608 0.1746 0.2711 -0.0253 -0.0134 -0.0284 326 ALA B O   
6818 C CB  . ALA B 326 ? 0.2312 0.1397 0.2571 -0.0295 -0.0050 -0.0106 326 ALA B CB  
6819 N N   . VAL B 327 ? 0.2210 0.1598 0.2474 -0.0374 -0.0176 -0.0246 327 VAL B N   
6820 C CA  . VAL B 327 ? 0.2141 0.1686 0.2370 -0.0338 -0.0225 -0.0269 327 VAL B CA  
6821 C C   . VAL B 327 ? 0.2519 0.2004 0.2651 -0.0381 -0.0260 -0.0377 327 VAL B C   
6822 O O   . VAL B 327 ? 0.2821 0.2328 0.2859 -0.0319 -0.0271 -0.0401 327 VAL B O   
6823 C CB  . VAL B 327 ? 0.2052 0.1845 0.2388 -0.0362 -0.0261 -0.0223 327 VAL B CB  
6824 C CG1 . VAL B 327 ? 0.2328 0.2280 0.2617 -0.0331 -0.0319 -0.0241 327 VAL B CG1 
6825 C CG2 . VAL B 327 ? 0.1960 0.1793 0.2357 -0.0289 -0.0213 -0.0127 327 VAL B CG2 
6826 N N   . ARG B 328 ? 0.2477 0.1875 0.2617 -0.0494 -0.0272 -0.0447 328 ARG B N   
6827 C CA  . ARG B 328 ? 0.2678 0.1980 0.2696 -0.0537 -0.0297 -0.0571 328 ARG B CA  
6828 C C   . ARG B 328 ? 0.3702 0.2780 0.3601 -0.0436 -0.0240 -0.0601 328 ARG B C   
6829 O O   . ARG B 328 ? 0.3414 0.2491 0.3195 -0.0398 -0.0250 -0.0672 328 ARG B O   
6830 C CB  . ARG B 328 ? 0.3193 0.2397 0.3234 -0.0696 -0.0314 -0.0649 328 ARG B CB  
6831 C CG  . ARG B 328 ? 0.4998 0.4068 0.4888 -0.0755 -0.0337 -0.0801 328 ARG B CG  
6832 C CD  . ARG B 328 ? 0.6976 0.6039 0.6899 -0.0951 -0.0382 -0.0887 328 ARG B CD  
6833 N NE  . ARG B 328 ? 0.8309 0.7047 0.8237 -0.1019 -0.0317 -0.0901 328 ARG B NE  
6834 C CZ  . ARG B 328 ? 0.9102 0.7679 0.8997 -0.1193 -0.0330 -0.1009 328 ARG B CZ  
6835 N NH1 . ARG B 328 ? 0.8793 0.7537 0.8649 -0.1323 -0.0415 -0.1123 328 ARG B NH1 
6836 N NH2 . ARG B 328 ? 0.9719 0.7965 0.9613 -0.1244 -0.0258 -0.1001 328 ARG B NH2 
6837 N N   . ASP B 329 ? 0.3120 0.2029 0.3049 -0.0385 -0.0178 -0.0541 329 ASP B N   
6838 C CA  . ASP B 329 ? 0.3492 0.2234 0.3334 -0.0270 -0.0123 -0.0548 329 ASP B CA  
6839 C C   . ASP B 329 ? 0.2891 0.1806 0.2704 -0.0168 -0.0128 -0.0513 329 ASP B C   
6840 O O   . ASP B 329 ? 0.3345 0.2224 0.3061 -0.0102 -0.0109 -0.0567 329 ASP B O   
6841 C CB  . ASP B 329 ? 0.2974 0.1570 0.2869 -0.0226 -0.0067 -0.0459 329 ASP B CB  
6842 C CG  . ASP B 329 ? 0.3070 0.1526 0.2895 -0.0092 -0.0012 -0.0451 329 ASP B CG  
6843 O OD1 . ASP B 329 ? 0.4067 0.2287 0.3814 -0.0078 0.0024  -0.0522 329 ASP B OD1 
6844 O OD2 . ASP B 329 ? 0.3443 0.2028 0.3292 -0.0001 -0.0003 -0.0377 329 ASP B OD2 
6845 N N   . PHE B 330 ? 0.2570 0.1665 0.2461 -0.0157 -0.0147 -0.0423 330 PHE B N   
6846 C CA  . PHE B 330 ? 0.2269 0.1499 0.2137 -0.0079 -0.0146 -0.0377 330 PHE B CA  
6847 C C   . PHE B 330 ? 0.2570 0.1911 0.2354 -0.0087 -0.0182 -0.0434 330 PHE B C   
6848 O O   . PHE B 330 ? 0.2665 0.2029 0.2374 -0.0023 -0.0159 -0.0445 330 PHE B O   
6849 C CB  . PHE B 330 ? 0.2606 0.1955 0.2560 -0.0080 -0.0155 -0.0283 330 PHE B CB  
6850 C CG  . PHE B 330 ? 0.2433 0.1866 0.2366 -0.0016 -0.0144 -0.0228 330 PHE B CG  
6851 C CD1 . PHE B 330 ? 0.3037 0.2426 0.2969 0.0035  -0.0107 -0.0191 330 PHE B CD1 
6852 C CD2 . PHE B 330 ? 0.2715 0.2276 0.2627 -0.0015 -0.0172 -0.0207 330 PHE B CD2 
6853 C CE1 . PHE B 330 ? 0.3506 0.2976 0.3422 0.0066  -0.0099 -0.0146 330 PHE B CE1 
6854 C CE2 . PHE B 330 ? 0.3168 0.2772 0.3055 0.0026  -0.0155 -0.0154 330 PHE B CE2 
6855 C CZ  . PHE B 330 ? 0.3285 0.2844 0.3175 0.0055  -0.0119 -0.0130 330 PHE B CZ  
6856 N N   . ILE B 331 ? 0.2741 0.2178 0.2537 -0.0164 -0.0237 -0.0465 331 ILE B N   
6857 C CA  . ILE B 331 ? 0.2823 0.2384 0.2523 -0.0174 -0.0279 -0.0515 331 ILE B CA  
6858 C C   . ILE B 331 ? 0.3202 0.2629 0.2770 -0.0168 -0.0256 -0.0632 331 ILE B C   
6859 O O   . ILE B 331 ? 0.2731 0.2227 0.2186 -0.0126 -0.0253 -0.0662 331 ILE B O   
6860 C CB  . ILE B 331 ? 0.2884 0.2604 0.2634 -0.0262 -0.0353 -0.0524 331 ILE B CB  
6861 C CG1 . ILE B 331 ? 0.2847 0.2706 0.2727 -0.0240 -0.0363 -0.0406 331 ILE B CG1 
6862 C CG2 . ILE B 331 ? 0.3357 0.3220 0.2986 -0.0276 -0.0406 -0.0579 331 ILE B CG2 
6863 C CD1 . ILE B 331 ? 0.2967 0.2914 0.2815 -0.0149 -0.0353 -0.0318 331 ILE B CD1 
6864 N N   . GLY B 332 ? 0.3027 0.2249 0.2595 -0.0210 -0.0233 -0.0701 332 GLY B N   
6865 C CA  . GLY B 332 ? 0.3253 0.2297 0.2685 -0.0192 -0.0198 -0.0822 332 GLY B CA  
6866 C C   . GLY B 332 ? 0.3084 0.2097 0.2471 -0.0056 -0.0128 -0.0795 332 GLY B C   
6867 O O   . GLY B 332 ? 0.3698 0.2685 0.2953 -0.0010 -0.0100 -0.0879 332 GLY B O   
6868 N N   . ARG B 333 ? 0.2812 0.1850 0.2304 0.0007  -0.0098 -0.0681 333 ARG B N   
6869 C CA  . ARG B 333 ? 0.3811 0.2889 0.3285 0.0125  -0.0041 -0.0643 333 ARG B CA  
6870 C C   . ARG B 333 ? 0.3549 0.2845 0.2973 0.0142  -0.0054 -0.0618 333 ARG B C   
6871 O O   . ARG B 333 ? 0.3374 0.2711 0.2724 0.0215  -0.0007 -0.0645 333 ARG B O   
6872 C CB  . ARG B 333 ? 0.3333 0.2413 0.2926 0.0168  -0.0020 -0.0530 333 ARG B CB  
6873 C CG  . ARG B 333 ? 0.4667 0.3520 0.4285 0.0178  0.0010  -0.0542 333 ARG B CG  
6874 C CD  . ARG B 333 ? 0.5573 0.4453 0.5293 0.0211  0.0021  -0.0426 333 ARG B CD  
6875 N NE  . ARG B 333 ? 0.5802 0.4467 0.5545 0.0201  0.0044  -0.0414 333 ARG B NE  
6876 C CZ  . ARG B 333 ? 0.6280 0.4792 0.6003 0.0299  0.0098  -0.0402 333 ARG B CZ  
6877 N NH1 . ARG B 333 ? 0.6834 0.5418 0.6530 0.0416  0.0134  -0.0407 333 ARG B NH1 
6878 N NH2 . ARG B 333 ? 0.6102 0.4400 0.5839 0.0285  0.0121  -0.0375 333 ARG B NH2 
6879 N N   . LEU B 334 ? 0.3273 0.2709 0.2735 0.0083  -0.0110 -0.0558 334 LEU B N   
6880 C CA  . LEU B 334 ? 0.3085 0.2701 0.2483 0.0094  -0.0122 -0.0524 334 LEU B CA  
6881 C C   . LEU B 334 ? 0.2810 0.2448 0.2054 0.0084  -0.0131 -0.0630 334 LEU B C   
6882 O O   . LEU B 334 ? 0.3003 0.2748 0.2155 0.0128  -0.0102 -0.0625 334 LEU B O   
6883 C CB  . LEU B 334 ? 0.2452 0.2179 0.1914 0.0048  -0.0177 -0.0438 334 LEU B CB  
6884 C CG  . LEU B 334 ? 0.2364 0.2066 0.1948 0.0061  -0.0159 -0.0342 334 LEU B CG  
6885 C CD1 . LEU B 334 ? 0.3042 0.2824 0.2681 0.0033  -0.0201 -0.0267 334 LEU B CD1 
6886 C CD2 . LEU B 334 ? 0.2658 0.2394 0.2243 0.0113  -0.0107 -0.0288 334 LEU B CD2 
6887 N N   . LYS B 335 ? 0.2996 0.2547 0.2202 0.0015  -0.0172 -0.0730 335 LYS B N   
6888 C CA  . LYS B 335 ? 0.3506 0.3062 0.2539 -0.0006 -0.0183 -0.0855 335 LYS B CA  
6889 C C   . LYS B 335 ? 0.3658 0.3101 0.2592 0.0087  -0.0095 -0.0928 335 LYS B C   
6890 O O   . LYS B 335 ? 0.3490 0.3022 0.2277 0.0120  -0.0074 -0.0979 335 LYS B O   
6891 C CB  . LYS B 335 ? 0.3543 0.2999 0.2558 -0.0119 -0.0241 -0.0962 335 LYS B CB  
6892 C CG  . LYS B 335 ? 0.3713 0.3135 0.2522 -0.0155 -0.0252 -0.1124 335 LYS B CG  
6893 C CD  . LYS B 335 ? 0.5516 0.4808 0.4306 -0.0293 -0.0306 -0.1249 335 LYS B CD  
6894 C CE  . LYS B 335 ? 0.5328 0.4308 0.4191 -0.0294 -0.0246 -0.1278 335 LYS B CE  
6895 N NZ  . LYS B 335 ? 0.5476 0.4258 0.4252 -0.0431 -0.0273 -0.1439 335 LYS B NZ  
6896 N N   . LYS B 336 ? 0.4039 0.3298 0.3048 0.0140  -0.0038 -0.0928 336 LYS B N   
6897 C CA  . LYS B 336 ? 0.4832 0.3994 0.3761 0.0254  0.0053  -0.0991 336 LYS B CA  
6898 C C   . LYS B 336 ? 0.3665 0.3050 0.2606 0.0339  0.0099  -0.0901 336 LYS B C   
6899 O O   . LYS B 336 ? 0.4010 0.3444 0.2828 0.0408  0.0157  -0.0964 336 LYS B O   
6900 C CB  . LYS B 336 ? 0.5463 0.4392 0.4478 0.0308  0.0101  -0.0985 336 LYS B CB  
6901 C CG  . LYS B 336 ? 0.5744 0.4402 0.4720 0.0219  0.0078  -0.1087 336 LYS B CG  
6902 C CD  . LYS B 336 ? 0.7384 0.5838 0.6167 0.0247  0.0128  -0.1260 336 LYS B CD  
6903 C CE  . LYS B 336 ? 0.7039 0.5337 0.5735 0.0085  0.0065  -0.1390 336 LYS B CE  
6904 N NZ  . LYS B 336 ? 0.7980 0.6240 0.6447 0.0067  0.0072  -0.1564 336 LYS B NZ  
6905 N N   . ILE B 337 ? 0.3383 0.2907 0.2464 0.0327  0.0078  -0.0760 337 ILE B N   
6906 C CA  . ILE B 337 ? 0.3187 0.2929 0.2285 0.0370  0.0114  -0.0668 337 ILE B CA  
6907 C C   . ILE B 337 ? 0.3609 0.3492 0.2558 0.0341  0.0099  -0.0691 337 ILE B C   
6908 O O   . ILE B 337 ? 0.3807 0.3808 0.2672 0.0400  0.0163  -0.0701 337 ILE B O   
6909 C CB  . ILE B 337 ? 0.3598 0.3421 0.2845 0.0329  0.0082  -0.0529 337 ILE B CB  
6910 C CG1 . ILE B 337 ? 0.3646 0.3372 0.3026 0.0367  0.0100  -0.0494 337 ILE B CG1 
6911 C CG2 . ILE B 337 ? 0.3811 0.3843 0.3061 0.0337  0.0113  -0.0437 337 ILE B CG2 
6912 C CD1 . ILE B 337 ? 0.3267 0.3027 0.2766 0.0308  0.0057  -0.0388 337 ILE B CD1 
6913 N N   . HIS B 338 ? 0.3032 0.2927 0.1946 0.0253  0.0017  -0.0693 338 HIS B N   
6914 C CA  . HIS B 338 ? 0.3108 0.3156 0.1875 0.0226  -0.0012 -0.0696 338 HIS B CA  
6915 C C   . HIS B 338 ? 0.3501 0.3532 0.2076 0.0264  0.0031  -0.0837 338 HIS B C   
6916 O O   . HIS B 338 ? 0.3916 0.4103 0.2369 0.0296  0.0069  -0.0820 338 HIS B O   
6917 C CB  . HIS B 338 ? 0.3803 0.3872 0.2582 0.0138  -0.0115 -0.0684 338 HIS B CB  
6918 C CG  . HIS B 338 ? 0.4864 0.5114 0.3499 0.0115  -0.0160 -0.0664 338 HIS B CG  
6919 N ND1 . HIS B 338 ? 0.5682 0.5960 0.4138 0.0086  -0.0191 -0.0793 338 HIS B ND1 
6920 C CD2 . HIS B 338 ? 0.4649 0.5053 0.3279 0.0119  -0.0179 -0.0525 338 HIS B CD2 
6921 C CE1 . HIS B 338 ? 0.5955 0.6428 0.4304 0.0077  -0.0233 -0.0727 338 HIS B CE1 
6922 N NE2 . HIS B 338 ? 0.5281 0.5822 0.3735 0.0102  -0.0223 -0.0558 338 HIS B NE2 
6923 N N   . GLU B 339 ? 0.4386 0.4213 0.2919 0.0260  0.0035  -0.0978 339 GLU B N   
6924 C CA  . GLU B 339 ? 0.4778 0.4538 0.3109 0.0302  0.0087  -0.1135 339 GLU B CA  
6925 C C   . GLU B 339 ? 0.5789 0.5567 0.4119 0.0438  0.0209  -0.1130 339 GLU B C   
6926 O O   . GLU B 339 ? 0.6516 0.6310 0.4667 0.0497  0.0272  -0.1234 339 GLU B O   
6927 C CB  . GLU B 339 ? 0.5461 0.4944 0.3743 0.0254  0.0067  -0.1293 339 GLU B CB  
6928 C CG  . GLU B 339 ? 0.6002 0.5491 0.4286 0.0106  -0.0052 -0.1323 339 GLU B CG  
6929 C CD  . GLU B 339 ? 0.7816 0.7013 0.6130 0.0039  -0.0064 -0.1433 339 GLU B CD  
6930 O OE1 . GLU B 339 ? 0.7846 0.7042 0.6136 -0.0097 -0.0154 -0.1497 339 GLU B OE1 
6931 O OE2 . GLU B 339 ? 0.8300 0.7278 0.6665 0.0122  0.0018  -0.1446 339 GLU B OE2 
6932 N N   . SER B 340 ? 0.6087 0.5885 0.4609 0.0492  0.0245  -0.1014 340 SER B N   
6933 C CA  . SER B 340 ? 0.4894 0.4716 0.3447 0.0628  0.0357  -0.1014 340 SER B CA  
6934 C C   . SER B 340 ? 0.5702 0.5814 0.4228 0.0669  0.0416  -0.0934 340 SER B C   
6935 O O   . SER B 340 ? 0.6233 0.6418 0.4753 0.0788  0.0519  -0.0953 340 SER B O   
6936 C CB  . SER B 340 ? 0.4797 0.4554 0.3565 0.0666  0.0364  -0.0922 340 SER B CB  
6937 O OG  . SER B 340 ? 0.4980 0.4949 0.3891 0.0625  0.0340  -0.0764 340 SER B OG  
6938 N N   . VAL B 341 ? 0.4790 0.5071 0.3299 0.0580  0.0363  -0.0838 341 VAL B N   
6939 C CA  . VAL B 341 ? 0.4774 0.5319 0.3265 0.0596  0.0421  -0.0737 341 VAL B CA  
6940 C C   . VAL B 341 ? 0.5027 0.5669 0.3325 0.0533  0.0380  -0.0740 341 VAL B C   
6941 O O   . VAL B 341 ? 0.5398 0.5954 0.3645 0.0456  0.0282  -0.0767 341 VAL B O   
6942 C CB  . VAL B 341 ? 0.4666 0.5324 0.3363 0.0550  0.0407  -0.0565 341 VAL B CB  
6943 C CG1 . VAL B 341 ? 0.4956 0.5585 0.3830 0.0623  0.0450  -0.0554 341 VAL B CG1 
6944 C CG2 . VAL B 341 ? 0.4515 0.5077 0.3262 0.0444  0.0298  -0.0504 341 VAL B CG2 
6945 N N   . ASP B 342 ? 0.4870 0.5721 0.3063 0.0569  0.0458  -0.0703 342 ASP B N   
6946 C CA  . ASP B 342 ? 0.5307 0.6281 0.3297 0.0522  0.0429  -0.0686 342 ASP B CA  
6947 C C   . ASP B 342 ? 0.5717 0.6814 0.3774 0.0443  0.0390  -0.0490 342 ASP B C   
6948 O O   . ASP B 342 ? 0.6224 0.7408 0.4125 0.0405  0.0349  -0.0446 342 ASP B O   
6949 C CB  . ASP B 342 ? 0.6102 0.7234 0.3908 0.0603  0.0543  -0.0747 342 ASP B CB  
6950 C CG  . ASP B 342 ? 0.7971 0.9294 0.5914 0.0657  0.0658  -0.0638 342 ASP B CG  
6951 O OD1 . ASP B 342 ? 0.9030 1.0305 0.7197 0.0675  0.0666  -0.0599 342 ASP B OD1 
6952 O OD2 . ASP B 342 ? 0.9610 1.1154 0.7437 0.0679  0.0740  -0.0591 342 ASP B OD2 
6953 N N   . PHE B 343 ? 0.4835 0.5931 0.3108 0.0421  0.0402  -0.0373 343 PHE B N   
6954 C CA  . PHE B 343 ? 0.4114 0.5259 0.2454 0.0343  0.0371  -0.0198 343 PHE B CA  
6955 C C   . PHE B 343 ? 0.3311 0.4275 0.1779 0.0294  0.0270  -0.0180 343 PHE B C   
6956 O O   . PHE B 343 ? 0.3570 0.4394 0.2078 0.0310  0.0226  -0.0293 343 PHE B O   
6957 C CB  . PHE B 343 ? 0.3704 0.4981 0.2183 0.0331  0.0459  -0.0088 343 PHE B CB  
6958 C CG  . PHE B 343 ? 0.3388 0.4608 0.2071 0.0358  0.0471  -0.0126 343 PHE B CG  
6959 C CD1 . PHE B 343 ? 0.3531 0.4794 0.2229 0.0459  0.0538  -0.0233 343 PHE B CD1 
6960 C CD2 . PHE B 343 ? 0.2888 0.4006 0.1735 0.0293  0.0418  -0.0052 343 PHE B CD2 
6961 C CE1 . PHE B 343 ? 0.3110 0.4334 0.1995 0.0498  0.0547  -0.0249 343 PHE B CE1 
6962 C CE2 . PHE B 343 ? 0.3214 0.4300 0.2234 0.0318  0.0423  -0.0079 343 PHE B CE2 
6963 C CZ  . PHE B 343 ? 0.3070 0.4218 0.2114 0.0423  0.0484  -0.0169 343 PHE B CZ  
6964 N N   . GLN B 344 ? 0.3074 0.4030 0.1602 0.0234  0.0242  -0.0033 344 GLN B N   
6965 C CA  . GLN B 344 ? 0.2931 0.3730 0.1573 0.0198  0.0159  -0.0007 344 GLN B CA  
6966 C C   . GLN B 344 ? 0.3189 0.3918 0.2025 0.0180  0.0184  0.0016  344 GLN B C   
6967 O O   . GLN B 344 ? 0.3145 0.3926 0.2035 0.0138  0.0230  0.0122  344 GLN B O   
6968 C CB  . GLN B 344 ? 0.3140 0.3939 0.1729 0.0163  0.0119  0.0132  344 GLN B CB  
6969 C CG  . GLN B 344 ? 0.3217 0.4111 0.1613 0.0186  0.0073  0.0112  344 GLN B CG  
6970 C CD  . GLN B 344 ? 0.4171 0.5074 0.2513 0.0177  0.0029  0.0264  344 GLN B CD  
6971 O OE1 . GLN B 344 ? 0.4022 0.4940 0.2325 0.0190  -0.0060 0.0253  344 GLN B OE1 
6972 N NE2 . GLN B 344 ? 0.3407 0.4304 0.1747 0.0154  0.0091  0.0413  344 GLN B NE2 
6973 N N   . PRO B 345 ? 0.2659 0.3280 0.1593 0.0202  0.0156  -0.0076 345 PRO B N   
6974 C CA  . PRO B 345 ? 0.3019 0.3605 0.2119 0.0193  0.0179  -0.0054 345 PRO B CA  
6975 C C   . PRO B 345 ? 0.2547 0.3021 0.1733 0.0133  0.0130  0.0027  345 PRO B C   
6976 O O   . PRO B 345 ? 0.2946 0.3340 0.2096 0.0122  0.0071  0.0038  345 PRO B O   
6977 C CB  . PRO B 345 ? 0.2660 0.3153 0.1798 0.0251  0.0169  -0.0178 345 PRO B CB  
6978 C CG  . PRO B 345 ? 0.2958 0.3367 0.1986 0.0245  0.0108  -0.0254 345 PRO B CG  
6979 C CD  . PRO B 345 ? 0.2759 0.3292 0.1637 0.0230  0.0109  -0.0207 345 PRO B CD  
6980 N N   . VAL B 346 ? 0.2839 0.3328 0.2135 0.0094  0.0158  0.0083  346 VAL B N   
6981 C CA  . VAL B 346 ? 0.2827 0.3189 0.2197 0.0039  0.0123  0.0139  346 VAL B CA  
6982 C C   . VAL B 346 ? 0.2275 0.2591 0.1762 0.0057  0.0107  0.0081  346 VAL B C   
6983 O O   . VAL B 346 ? 0.2264 0.2687 0.1817 0.0072  0.0143  0.0067  346 VAL B O   
6984 C CB  . VAL B 346 ? 0.2952 0.3345 0.2334 -0.0043 0.0163  0.0242  346 VAL B CB  
6985 C CG1 . VAL B 346 ? 0.3181 0.3396 0.2607 -0.0095 0.0131  0.0282  346 VAL B CG1 
6986 C CG2 . VAL B 346 ? 0.2942 0.3391 0.2196 -0.0053 0.0192  0.0314  346 VAL B CG2 
6987 N N   . VAL B 347 ? 0.2365 0.2541 0.1879 0.0062  0.0056  0.0057  347 VAL B N   
6988 C CA  . VAL B 347 ? 0.2240 0.2356 0.1842 0.0084  0.0040  0.0008  347 VAL B CA  
6989 C C   . VAL B 347 ? 0.1922 0.1947 0.1579 0.0033  0.0020  0.0055  347 VAL B C   
6990 O O   . VAL B 347 ? 0.2370 0.2293 0.2010 0.0025  -0.0010 0.0068  347 VAL B O   
6991 C CB  . VAL B 347 ? 0.1992 0.2024 0.1573 0.0125  0.0008  -0.0069 347 VAL B CB  
6992 C CG1 . VAL B 347 ? 0.2081 0.2037 0.1746 0.0147  0.0002  -0.0102 347 VAL B CG1 
6993 C CG2 . VAL B 347 ? 0.2802 0.2899 0.2293 0.0169  0.0030  -0.0134 347 VAL B CG2 
6994 N N   . PHE B 348 ? 0.1860 0.1938 0.1579 -0.0001 0.0037  0.0077  348 PHE B N   
6995 C CA  . PHE B 348 ? 0.1829 0.1820 0.1579 -0.0056 0.0022  0.0102  348 PHE B CA  
6996 C C   . PHE B 348 ? 0.2275 0.2215 0.2078 -0.0017 -0.0003 0.0063  348 PHE B C   
6997 O O   . PHE B 348 ? 0.2394 0.2417 0.2245 0.0025  0.0004  0.0043  348 PHE B O   
6998 C CB  . PHE B 348 ? 0.2388 0.2479 0.2167 -0.0135 0.0044  0.0138  348 PHE B CB  
6999 C CG  . PHE B 348 ? 0.2458 0.2488 0.2174 -0.0216 0.0066  0.0195  348 PHE B CG  
7000 C CD1 . PHE B 348 ? 0.2023 0.2107 0.1683 -0.0209 0.0094  0.0231  348 PHE B CD1 
7001 C CD2 . PHE B 348 ? 0.2523 0.2418 0.2218 -0.0296 0.0063  0.0211  348 PHE B CD2 
7002 C CE1 . PHE B 348 ? 0.2153 0.2151 0.1743 -0.0278 0.0120  0.0300  348 PHE B CE1 
7003 C CE2 . PHE B 348 ? 0.2484 0.2268 0.2108 -0.0368 0.0091  0.0266  348 PHE B CE2 
7004 C CZ  . PHE B 348 ? 0.2229 0.2061 0.1804 -0.0358 0.0120  0.0320  348 PHE B CZ  
7005 N N   . VAL B 349 ? 0.1984 0.1793 0.1779 -0.0023 -0.0023 0.0062  349 VAL B N   
7006 C CA  . VAL B 349 ? 0.1792 0.1551 0.1630 -0.0002 -0.0039 0.0042  349 VAL B CA  
7007 C C   . VAL B 349 ? 0.2340 0.2052 0.2167 -0.0058 -0.0038 0.0061  349 VAL B C   
7008 O O   . VAL B 349 ? 0.2054 0.1658 0.1840 -0.0079 -0.0033 0.0074  349 VAL B O   
7009 C CB  . VAL B 349 ? 0.1707 0.1380 0.1549 0.0030  -0.0056 0.0021  349 VAL B CB  
7010 C CG1 . VAL B 349 ? 0.2227 0.1853 0.2111 0.0041  -0.0060 0.0013  349 VAL B CG1 
7011 C CG2 . VAL B 349 ? 0.2085 0.1793 0.1912 0.0064  -0.0060 -0.0016 349 VAL B CG2 
7012 N N   . VAL B 350 ? 0.1914 0.1708 0.1767 -0.0077 -0.0043 0.0063  350 VAL B N   
7013 C CA  . VAL B 350 ? 0.2099 0.1869 0.1920 -0.0150 -0.0046 0.0066  350 VAL B CA  
7014 C C   . VAL B 350 ? 0.1725 0.1529 0.1564 -0.0129 -0.0064 0.0060  350 VAL B C   
7015 O O   . VAL B 350 ? 0.2082 0.2017 0.1974 -0.0087 -0.0074 0.0074  350 VAL B O   
7016 C CB  . VAL B 350 ? 0.2382 0.2274 0.2207 -0.0231 -0.0042 0.0081  350 VAL B CB  
7017 C CG1 . VAL B 350 ? 0.2255 0.2075 0.2021 -0.0333 -0.0046 0.0067  350 VAL B CG1 
7018 C CG2 . VAL B 350 ? 0.2280 0.2171 0.2089 -0.0240 -0.0016 0.0104  350 VAL B CG2 
7019 N N   . LEU B 351 ? 0.1768 0.1459 0.1555 -0.0149 -0.0063 0.0046  351 LEU B N   
7020 C CA  . LEU B 351 ? 0.1772 0.1504 0.1551 -0.0138 -0.0077 0.0049  351 LEU B CA  
7021 C C   . LEU B 351 ? 0.1866 0.1473 0.1555 -0.0185 -0.0065 0.0019  351 LEU B C   
7022 O O   . LEU B 351 ? 0.2430 0.1907 0.2075 -0.0213 -0.0042 0.0002  351 LEU B O   
7023 C CB  . LEU B 351 ? 0.2718 0.2432 0.2544 -0.0052 -0.0073 0.0068  351 LEU B CB  
7024 C CG  . LEU B 351 ? 0.2506 0.2090 0.2339 -0.0024 -0.0053 0.0059  351 LEU B CG  
7025 C CD1 . LEU B 351 ? 0.2712 0.2269 0.2564 0.0015  -0.0045 0.0080  351 LEU B CD1 
7026 C CD2 . LEU B 351 ? 0.2254 0.1832 0.2127 0.0001  -0.0053 0.0051  351 LEU B CD2 
7027 N N   . ASP B 352 ? 0.1918 0.1556 0.1566 -0.0185 -0.0074 0.0017  352 ASP B N   
7028 C CA  . ASP B 352 ? 0.2425 0.1936 0.1970 -0.0215 -0.0051 -0.0021 352 ASP B CA  
7029 C C   . ASP B 352 ? 0.2363 0.1740 0.1928 -0.0150 -0.0010 -0.0018 352 ASP B C   
7030 O O   . ASP B 352 ? 0.2709 0.2120 0.2356 -0.0090 -0.0009 0.0016  352 ASP B O   
7031 C CB  . ASP B 352 ? 0.2198 0.1786 0.1688 -0.0211 -0.0064 -0.0016 352 ASP B CB  
7032 C CG  . ASP B 352 ? 0.2698 0.2462 0.2165 -0.0277 -0.0114 -0.0018 352 ASP B CG  
7033 O OD1 . ASP B 352 ? 0.2450 0.2276 0.1946 -0.0342 -0.0134 -0.0030 352 ASP B OD1 
7034 O OD2 . ASP B 352 ? 0.2735 0.2601 0.2159 -0.0262 -0.0135 0.0004  352 ASP B OD2 
7035 N N   . GLY B 353 ? 0.2411 0.1636 0.1900 -0.0163 0.0026  -0.0053 353 GLY B N   
7036 C CA  . GLY B 353 ? 0.2239 0.1378 0.1761 -0.0091 0.0064  -0.0040 353 GLY B CA  
7037 C C   . GLY B 353 ? 0.2867 0.1991 0.2364 -0.0044 0.0102  -0.0045 353 GLY B C   
7038 O O   . GLY B 353 ? 0.2353 0.1456 0.1903 0.0020  0.0135  -0.0026 353 GLY B O   
7039 N N   . GLU B 354 ? 0.2783 0.1946 0.2202 -0.0074 0.0100  -0.0063 354 GLU B N   
7040 C CA  . GLU B 354 ? 0.2280 0.1431 0.1648 -0.0033 0.0149  -0.0069 354 GLU B CA  
7041 C C   . GLU B 354 ? 0.2238 0.1519 0.1612 -0.0032 0.0135  -0.0027 354 GLU B C   
7042 O O   . GLU B 354 ? 0.2709 0.1998 0.2037 -0.0002 0.0181  -0.0020 354 GLU B O   
7043 C CB  . GLU B 354 ? 0.2499 0.1511 0.1699 -0.0062 0.0187  -0.0146 354 GLU B CB  
7044 C CG  . GLU B 354 ? 0.2601 0.1663 0.1672 -0.0151 0.0147  -0.0189 354 GLU B CG  
7045 C CD  . GLU B 354 ? 0.2590 0.1665 0.1671 -0.0240 0.0090  -0.0205 354 GLU B CD  
7046 O OE1 . GLU B 354 ? 0.2776 0.1733 0.1733 -0.0322 0.0093  -0.0279 354 GLU B OE1 
7047 O OE2 . GLU B 354 ? 0.2415 0.1615 0.1626 -0.0231 0.0048  -0.0146 354 GLU B OE2 
7048 N N   . ASN B 355 ? 0.2149 0.1531 0.1574 -0.0051 0.0081  0.0011  355 ASN B N   
7049 C CA  . ASN B 355 ? 0.2457 0.1942 0.1856 -0.0042 0.0069  0.0061  355 ASN B CA  
7050 C C   . ASN B 355 ? 0.2074 0.1589 0.1591 0.0005  0.0075  0.0136  355 ASN B C   
7051 O O   . ASN B 355 ? 0.2404 0.1965 0.1894 0.0023  0.0086  0.0193  355 ASN B O   
7052 C CB  . ASN B 355 ? 0.2500 0.2094 0.1857 -0.0085 0.0007  0.0061  355 ASN B CB  
7053 C CG  . ASN B 355 ? 0.2328 0.1900 0.1543 -0.0158 -0.0002 -0.0017 355 ASN B CG  
7054 O OD1 . ASN B 355 ? 0.2556 0.2067 0.1653 -0.0161 0.0038  -0.0054 355 ASN B OD1 
7055 N ND2 . ASN B 355 ? 0.2648 0.2269 0.1867 -0.0226 -0.0048 -0.0047 355 ASN B ND2 
7056 N N   . CYS B 356 ? 0.2412 0.1890 0.2042 0.0018  0.0071  0.0137  356 CYS B N   
7057 C CA  . CYS B 356 ? 0.2300 0.1775 0.2027 0.0042  0.0077  0.0190  356 CYS B CA  
7058 C C   . CYS B 356 ? 0.2086 0.1543 0.1869 0.0045  0.0126  0.0206  356 CYS B C   
7059 O O   . CYS B 356 ? 0.2227 0.1678 0.2058 0.0043  0.0143  0.0259  356 CYS B O   
7060 C CB  . CYS B 356 ? 0.2063 0.1524 0.1873 0.0047  0.0043  0.0173  356 CYS B CB  
7061 S SG  . CYS B 356 ? 0.2521 0.1951 0.2365 0.0035  0.0041  0.0118  356 CYS B SG  
7062 N N   . TRP B 357 ? 0.2485 0.1934 0.2264 0.0051  0.0153  0.0167  357 TRP B N   
7063 C CA  . TRP B 357 ? 0.2266 0.1751 0.2139 0.0060  0.0194  0.0185  357 TRP B CA  
7064 C C   . TRP B 357 ? 0.2304 0.1833 0.2159 0.0057  0.0249  0.0236  357 TRP B C   
7065 O O   . TRP B 357 ? 0.1995 0.1575 0.1955 0.0039  0.0276  0.0275  357 TRP B O   
7066 C CB  . TRP B 357 ? 0.1937 0.1413 0.1809 0.0094  0.0216  0.0144  357 TRP B CB  
7067 C CG  . TRP B 357 ? 0.1897 0.1318 0.1757 0.0091  0.0170  0.0109  357 TRP B CG  
7068 C CD1 . TRP B 357 ? 0.2110 0.1447 0.1868 0.0093  0.0169  0.0066  357 TRP B CD1 
7069 C CD2 . TRP B 357 ? 0.2388 0.1825 0.2326 0.0075  0.0120  0.0111  357 TRP B CD2 
7070 N NE1 . TRP B 357 ? 0.2045 0.1359 0.1826 0.0078  0.0125  0.0057  357 TRP B NE1 
7071 C CE2 . TRP B 357 ? 0.2210 0.1594 0.2096 0.0074  0.0096  0.0082  357 TRP B CE2 
7072 C CE3 . TRP B 357 ? 0.2393 0.1874 0.2429 0.0053  0.0099  0.0130  357 TRP B CE3 
7073 C CZ2 . TRP B 357 ? 0.2188 0.1584 0.2113 0.0064  0.0053  0.0077  357 TRP B CZ2 
7074 C CZ3 . TRP B 357 ? 0.2295 0.1771 0.2359 0.0043  0.0054  0.0109  357 TRP B CZ3 
7075 C CH2 . TRP B 357 ? 0.2198 0.1644 0.2206 0.0054  0.0033  0.0086  357 TRP B CH2 
7076 N N   . GLU B 358 ? 0.2226 0.1751 0.1947 0.0065  0.0265  0.0240  358 GLU B N   
7077 C CA  . GLU B 358 ? 0.2506 0.2084 0.2186 0.0066  0.0324  0.0296  358 GLU B CA  
7078 C C   . GLU B 358 ? 0.2616 0.2191 0.2363 0.0039  0.0322  0.0382  358 GLU B C   
7079 O O   . GLU B 358 ? 0.2672 0.2291 0.2429 0.0026  0.0381  0.0446  358 GLU B O   
7080 C CB  . GLU B 358 ? 0.2615 0.2196 0.2110 0.0075  0.0330  0.0278  358 GLU B CB  
7081 C CG  . GLU B 358 ? 0.2311 0.1889 0.1748 0.0061  0.0259  0.0294  358 GLU B CG  
7082 C CD  . GLU B 358 ? 0.3813 0.3408 0.3080 0.0048  0.0236  0.0233  358 GLU B CD  
7083 O OE1 . GLU B 358 ? 0.3608 0.3275 0.2778 0.0045  0.0212  0.0277  358 GLU B OE1 
7084 O OE2 . GLU B 358 ? 0.2987 0.2521 0.2213 0.0037  0.0240  0.0144  358 GLU B OE2 
7085 N N   . TYR B 359 ? 0.2293 0.1804 0.2079 0.0031  0.0265  0.0388  359 TYR B N   
7086 C CA  . TYR B 359 ? 0.2213 0.1663 0.2049 0.0013  0.0269  0.0463  359 TYR B CA  
7087 C C   . TYR B 359 ? 0.2277 0.1699 0.2259 -0.0036 0.0275  0.0452  359 TYR B C   
7088 O O   . TYR B 359 ? 0.2552 0.1892 0.2575 -0.0071 0.0289  0.0506  359 TYR B O   
7089 C CB  . TYR B 359 ? 0.2220 0.1612 0.2019 0.0047  0.0213  0.0474  359 TYR B CB  
7090 C CG  . TYR B 359 ? 0.2749 0.2210 0.2412 0.0083  0.0198  0.0501  359 TYR B CG  
7091 C CD1 . TYR B 359 ? 0.3783 0.3252 0.3372 0.0102  0.0225  0.0602  359 TYR B CD1 
7092 C CD2 . TYR B 359 ? 0.2663 0.2189 0.2266 0.0088  0.0156  0.0431  359 TYR B CD2 
7093 C CE1 . TYR B 359 ? 0.3518 0.3086 0.2974 0.0131  0.0202  0.0629  359 TYR B CE1 
7094 C CE2 . TYR B 359 ? 0.2999 0.2615 0.2474 0.0100  0.0132  0.0447  359 TYR B CE2 
7095 C CZ  . TYR B 359 ? 0.3907 0.3556 0.3308 0.0125  0.0151  0.0545  359 TYR B CZ  
7096 O OH  . TYR B 359 ? 0.4245 0.4015 0.3508 0.0136  0.0119  0.0565  359 TYR B OH  
7097 N N   . TYR B 360 ? 0.2360 0.1841 0.2411 -0.0043 0.0261  0.0385  360 TYR B N   
7098 C CA  . TYR B 360 ? 0.2555 0.2059 0.2743 -0.0096 0.0254  0.0368  360 TYR B CA  
7099 C C   . TYR B 360 ? 0.2814 0.2445 0.3084 -0.0131 0.0315  0.0406  360 TYR B C   
7100 O O   . TYR B 360 ? 0.2385 0.2100 0.2609 -0.0088 0.0362  0.0416  360 TYR B O   
7101 C CB  . TYR B 360 ? 0.1930 0.1472 0.2153 -0.0076 0.0206  0.0293  360 TYR B CB  
7102 C CG  . TYR B 360 ? 0.2081 0.1535 0.2268 -0.0061 0.0148  0.0248  360 TYR B CG  
7103 C CD1 . TYR B 360 ? 0.1893 0.1300 0.1977 -0.0016 0.0132  0.0246  360 TYR B CD1 
7104 C CD2 . TYR B 360 ? 0.2008 0.1459 0.2263 -0.0093 0.0108  0.0204  360 TYR B CD2 
7105 C CE1 . TYR B 360 ? 0.1861 0.1224 0.1927 0.0001  0.0087  0.0209  360 TYR B CE1 
7106 C CE2 . TYR B 360 ? 0.1966 0.1354 0.2180 -0.0071 0.0065  0.0160  360 TYR B CE2 
7107 C CZ  . TYR B 360 ? 0.2463 0.1812 0.2590 -0.0022 0.0059  0.0166  360 TYR B CZ  
7108 O OH  . TYR B 360 ? 0.2337 0.1655 0.2437 0.0001  0.0027  0.0129  360 TYR B OH  
7109 N N   . GLU B 361 ? 0.2552 0.1950 0.2912 -0.0229 0.0424  0.0431  361 GLU B N   
7110 C CA  . GLU B 361 ? 0.2975 0.2616 0.3472 -0.0355 0.0476  0.0446  361 GLU B CA  
7111 C C   . GLU B 361 ? 0.2626 0.2612 0.3274 -0.0302 0.0399  0.0360  361 GLU B C   
7112 O O   . GLU B 361 ? 0.2337 0.2333 0.3033 -0.0280 0.0306  0.0272  361 GLU B O   
7113 C CB  . GLU B 361 ? 0.4159 0.3680 0.4728 -0.0560 0.0503  0.0425  361 GLU B CB  
7114 C CG  . GLU B 361 ? 0.6005 0.5844 0.6771 -0.0708 0.0536  0.0402  361 GLU B CG  
7115 C CD  . GLU B 361 ? 0.7873 0.7569 0.8661 -0.0919 0.0638  0.0460  361 GLU B CD  
7116 O OE1 . GLU B 361 ? 0.8073 0.7380 0.8702 -0.0938 0.0678  0.0519  361 GLU B OE1 
7117 O OE2 . GLU B 361 ? 0.8730 0.8699 0.9696 -0.1067 0.0679  0.0442  361 GLU B OE2 
7118 N N   . GLU B 362 ? 0.2186 0.2443 0.2890 -0.0266 0.0441  0.0387  362 GLU B N   
7119 C CA  . GLU B 362 ? 0.2228 0.2806 0.3068 -0.0196 0.0371  0.0307  362 GLU B CA  
7120 C C   . GLU B 362 ? 0.1644 0.2160 0.2443 -0.0050 0.0260  0.0239  362 GLU B C   
7121 O O   . GLU B 362 ? 0.1609 0.2239 0.2503 -0.0035 0.0173  0.0161  362 GLU B O   
7122 C CB  . GLU B 362 ? 0.2454 0.3236 0.3483 -0.0338 0.0351  0.0243  362 GLU B CB  
7123 C CG  . GLU B 362 ? 0.4336 0.5249 0.5446 -0.0498 0.0470  0.0302  362 GLU B CG  
7124 C CD  . GLU B 362 ? 0.6433 0.7518 0.7735 -0.0667 0.0447  0.0229  362 GLU B CD  
7125 O OE1 . GLU B 362 ? 0.7246 0.8712 0.8717 -0.0681 0.0455  0.0192  362 GLU B OE1 
7126 O OE2 . GLU B 362 ? 0.6361 0.7224 0.7649 -0.0778 0.0420  0.0199  362 GLU B OE2 
7127 N N   . ASN B 363 ? 0.1872 0.2210 0.2525 0.0057  0.0262  0.0273  363 ASN B N   
7128 C CA  . ASN B 363 ? 0.1705 0.2010 0.2327 0.0190  0.0171  0.0213  363 ASN B CA  
7129 C C   . ASN B 363 ? 0.2203 0.2392 0.2857 0.0144  0.0096  0.0154  363 ASN B C   
7130 O O   . ASN B 363 ? 0.1909 0.2138 0.2592 0.0212  0.0017  0.0097  363 ASN B O   
7131 C CB  . ASN B 363 ? 0.1560 0.2116 0.2256 0.0295  0.0127  0.0162  363 ASN B CB  
7132 C CG  . ASN B 363 ? 0.2163 0.2658 0.2808 0.0428  0.0050  0.0111  363 ASN B CG  
7133 O OD1 . ASN B 363 ? 0.2259 0.2607 0.2799 0.0480  0.0058  0.0132  363 ASN B OD1 
7134 N ND2 . ASN B 363 ? 0.2567 0.3170 0.3293 0.0484  -0.0028 0.0040  363 ASN B ND2 
7135 N N   . GLY B 364 ? 0.1513 0.1542 0.2147 0.0029  0.0124  0.0168  364 GLY B N   
7136 C CA  . GLY B 364 ? 0.1437 0.1360 0.2073 -0.0008 0.0062  0.0111  364 GLY B CA  
7137 C C   . GLY B 364 ? 0.2125 0.2219 0.2876 -0.0062 0.0000  0.0053  364 GLY B C   
7138 O O   . GLY B 364 ? 0.2202 0.2225 0.2938 -0.0085 -0.0054 0.0008  364 GLY B O   
7139 N N   . ILE B 365 ? 0.1562 0.1898 0.2423 -0.0071 0.0005  0.0050  365 ILE B N   
7140 C CA  . ILE B 365 ? 0.2050 0.2576 0.3020 -0.0093 -0.0068 -0.0010 365 ILE B CA  
7141 C C   . ILE B 365 ? 0.1949 0.2441 0.2954 -0.0237 -0.0075 -0.0045 365 ILE B C   
7142 O O   . ILE B 365 ? 0.2030 0.2519 0.3027 -0.0234 -0.0155 -0.0095 365 ILE B O   
7143 C CB  . ILE B 365 ? 0.1404 0.2228 0.2493 -0.0052 -0.0059 -0.0016 365 ILE B CB  
7144 C CG1 . ILE B 365 ? 0.1705 0.2540 0.2744 0.0108  -0.0074 -0.0008 365 ILE B CG1 
7145 C CG2 . ILE B 365 ? 0.1445 0.2479 0.2650 -0.0060 -0.0143 -0.0081 365 ILE B CG2 
7146 C CD1 . ILE B 365 ? 0.2326 0.3434 0.3446 0.0165  -0.0036 -0.0008 365 ILE B CD1 
7147 N N   . PRO B 366 ? 0.1409 0.1858 0.2439 -0.0368 0.0002  -0.0023 366 PRO B N   
7148 C CA  . PRO B 366 ? 0.1515 0.1896 0.2569 -0.0508 -0.0017 -0.0078 366 PRO B CA  
7149 C C   . PRO B 366 ? 0.2277 0.2404 0.3196 -0.0478 -0.0059 -0.0108 366 PRO B C   
7150 O O   . PRO B 366 ? 0.2228 0.2385 0.3157 -0.0522 -0.0127 -0.0179 366 PRO B O   
7151 C CB  . PRO B 366 ? 0.2567 0.2858 0.3640 -0.0647 0.0090  -0.0032 366 PRO B CB  
7152 C CG  . PRO B 366 ? 0.2388 0.2880 0.3518 -0.0599 0.0153  0.0034  366 PRO B CG  
7153 C CD  . PRO B 366 ? 0.1500 0.1977 0.2542 -0.0406 0.0108  0.0049  366 PRO B CD  
7154 N N   . PHE B 367 ? 0.1698 0.1607 0.2490 -0.0396 -0.0024 -0.0060 367 PHE B N   
7155 C CA  . PHE B 367 ? 0.2298 0.2002 0.2972 -0.0360 -0.0053 -0.0091 367 PHE B CA  
7156 C C   . PHE B 367 ? 0.2267 0.2078 0.2935 -0.0284 -0.0138 -0.0126 367 PHE B C   
7157 O O   . PHE B 367 ? 0.1909 0.1685 0.2534 -0.0314 -0.0184 -0.0181 367 PHE B O   
7158 C CB  . PHE B 367 ? 0.2198 0.1698 0.2759 -0.0272 -0.0001 -0.0037 367 PHE B CB  
7159 C CG  . PHE B 367 ? 0.2007 0.1356 0.2466 -0.0215 -0.0028 -0.0075 367 PHE B CG  
7160 C CD1 . PHE B 367 ? 0.2358 0.1520 0.2750 -0.0275 -0.0018 -0.0122 367 PHE B CD1 
7161 C CD2 . PHE B 367 ? 0.1926 0.1332 0.2364 -0.0108 -0.0063 -0.0073 367 PHE B CD2 
7162 C CE1 . PHE B 367 ? 0.2921 0.1983 0.3223 -0.0214 -0.0036 -0.0167 367 PHE B CE1 
7163 C CE2 . PHE B 367 ? 0.2548 0.1856 0.2908 -0.0068 -0.0075 -0.0108 367 PHE B CE2 
7164 C CZ  . PHE B 367 ? 0.2375 0.1525 0.2665 -0.0114 -0.0060 -0.0155 367 PHE B CZ  
7165 N N   . LEU B 368 ? 0.1683 0.1613 0.2380 -0.0184 -0.0160 -0.0095 368 LEU B N   
7166 C CA  . LEU B 368 ? 0.1454 0.1425 0.2124 -0.0114 -0.0233 -0.0112 368 LEU B CA  
7167 C C   . LEU B 368 ? 0.1555 0.1695 0.2284 -0.0149 -0.0305 -0.0152 368 LEU B C   
7168 O O   . LEU B 368 ? 0.1752 0.1870 0.2415 -0.0135 -0.0361 -0.0172 368 LEU B O   
7169 C CB  . LEU B 368 ? 0.1856 0.1872 0.2540 -0.0002 -0.0242 -0.0078 368 LEU B CB  
7170 C CG  . LEU B 368 ? 0.2057 0.1923 0.2668 0.0054  -0.0200 -0.0056 368 LEU B CG  
7171 C CD1 . LEU B 368 ? 0.2000 0.1930 0.2638 0.0156  -0.0220 -0.0044 368 LEU B CD1 
7172 C CD2 . LEU B 368 ? 0.2194 0.1926 0.2719 0.0044  -0.0210 -0.0075 368 LEU B CD2 
7173 N N   . GLU B 369 ? 0.1516 0.1850 0.2368 -0.0188 -0.0303 -0.0164 369 GLU B N   
7174 C CA  . GLU B 369 ? 0.1855 0.2387 0.2776 -0.0213 -0.0381 -0.0215 369 GLU B CA  
7175 C C   . GLU B 369 ? 0.2466 0.2927 0.3338 -0.0316 -0.0401 -0.0273 369 GLU B C   
7176 O O   . GLU B 369 ? 0.2044 0.2573 0.2876 -0.0297 -0.0482 -0.0310 369 GLU B O   
7177 C CB  . GLU B 369 ? 0.2090 0.2884 0.3177 -0.0247 -0.0365 -0.0228 369 GLU B CB  
7178 C CG  . GLU B 369 ? 0.1825 0.2737 0.2953 -0.0112 -0.0375 -0.0196 369 GLU B CG  
7179 C CD  . GLU B 369 ? 0.2243 0.3473 0.3541 -0.0124 -0.0365 -0.0220 369 GLU B CD  
7180 O OE1 . GLU B 369 ? 0.2214 0.3554 0.3609 -0.0264 -0.0322 -0.0245 369 GLU B OE1 
7181 O OE2 . GLU B 369 ? 0.2263 0.3636 0.3604 0.0004  -0.0396 -0.0219 369 GLU B OE2 
7182 N N   . LYS B 370 ? 0.1649 0.1947 0.2499 -0.0412 -0.0330 -0.0281 370 LYS B N   
7183 C CA  . LYS B 370 ? 0.2079 0.2280 0.2873 -0.0505 -0.0349 -0.0355 370 LYS B CA  
7184 C C   . LYS B 370 ? 0.1823 0.1870 0.2453 -0.0433 -0.0375 -0.0359 370 LYS B C   
7185 O O   . LYS B 370 ? 0.2106 0.2194 0.2676 -0.0448 -0.0439 -0.0419 370 LYS B O   
7186 C CB  . LYS B 370 ? 0.2076 0.2092 0.2875 -0.0615 -0.0264 -0.0359 370 LYS B CB  
7187 C CG  . LYS B 370 ? 0.2795 0.2697 0.3545 -0.0718 -0.0288 -0.0457 370 LYS B CG  
7188 C CD  . LYS B 370 ? 0.4543 0.4705 0.5419 -0.0815 -0.0362 -0.0546 370 LYS B CD  
7189 C CE  . LYS B 370 ? 0.5248 0.5346 0.6033 -0.0860 -0.0426 -0.0660 370 LYS B CE  
7190 N NZ  . LYS B 370 ? 0.4802 0.5150 0.5719 -0.0974 -0.0499 -0.0767 370 LYS B NZ  
7191 N N   . LEU B 371 ? 0.1945 0.1829 0.2499 -0.0358 -0.0323 -0.0301 371 LEU B N   
7192 C CA  . LEU B 371 ? 0.1807 0.1576 0.2224 -0.0297 -0.0332 -0.0301 371 LEU B CA  
7193 C C   . LEU B 371 ? 0.1537 0.1431 0.1918 -0.0240 -0.0408 -0.0287 371 LEU B C   
7194 O O   . LEU B 371 ? 0.1802 0.1681 0.2074 -0.0241 -0.0441 -0.0319 371 LEU B O   
7195 C CB  . LEU B 371 ? 0.1684 0.1328 0.2070 -0.0222 -0.0272 -0.0243 371 LEU B CB  
7196 C CG  . LEU B 371 ? 0.1969 0.1535 0.2246 -0.0164 -0.0266 -0.0240 371 LEU B CG  
7197 C CD1 . LEU B 371 ? 0.2119 0.1569 0.2304 -0.0203 -0.0247 -0.0310 371 LEU B CD1 
7198 C CD2 . LEU B 371 ? 0.1761 0.1265 0.2049 -0.0093 -0.0219 -0.0194 371 LEU B CD2 
7199 N N   . TYR B 372 ? 0.1465 0.1471 0.1919 -0.0179 -0.0435 -0.0238 372 TYR B N   
7200 C CA  . TYR B 372 ? 0.2059 0.2132 0.2461 -0.0108 -0.0507 -0.0209 372 TYR B CA  
7201 C C   . TYR B 372 ? 0.1692 0.1928 0.2098 -0.0132 -0.0589 -0.0259 372 TYR B C   
7202 O O   . TYR B 372 ? 0.1990 0.2233 0.2280 -0.0089 -0.0648 -0.0246 372 TYR B O   
7203 C CB  . TYR B 372 ? 0.2154 0.2276 0.2632 -0.0024 -0.0518 -0.0156 372 TYR B CB  
7204 C CG  . TYR B 372 ? 0.1890 0.1876 0.2357 0.0016  -0.0458 -0.0114 372 TYR B CG  
7205 C CD1 . TYR B 372 ? 0.1664 0.1506 0.2045 -0.0005 -0.0407 -0.0111 372 TYR B CD1 
7206 C CD2 . TYR B 372 ? 0.1575 0.1605 0.2122 0.0084  -0.0458 -0.0090 372 TYR B CD2 
7207 C CE1 . TYR B 372 ? 0.1622 0.1381 0.2010 0.0034  -0.0362 -0.0086 372 TYR B CE1 
7208 C CE2 . TYR B 372 ? 0.1651 0.1578 0.2189 0.0122  -0.0416 -0.0068 372 TYR B CE2 
7209 C CZ  . TYR B 372 ? 0.1774 0.1575 0.2240 0.0094  -0.0371 -0.0066 372 TYR B CZ  
7210 O OH  . TYR B 372 ? 0.1675 0.1415 0.2151 0.0135  -0.0339 -0.0056 372 TYR B OH  
7211 N N   . SER B 373 ? 0.1765 0.2144 0.2302 -0.0202 -0.0595 -0.0316 373 SER B N   
7212 C CA  . SER B 373 ? 0.1940 0.2507 0.2503 -0.0240 -0.0678 -0.0389 373 SER B CA  
7213 C C   . SER B 373 ? 0.2440 0.2911 0.2859 -0.0289 -0.0693 -0.0448 373 SER B C   
7214 O O   . SER B 373 ? 0.2550 0.3123 0.2884 -0.0258 -0.0778 -0.0478 373 SER B O   
7215 C CB  . SER B 373 ? 0.2681 0.3419 0.3435 -0.0342 -0.0661 -0.0447 373 SER B CB  
7216 O OG  . SER B 373 ? 0.5488 0.6434 0.6288 -0.0391 -0.0746 -0.0538 373 SER B OG  
7217 N N   . THR B 374 ? 0.1864 0.2141 0.2243 -0.0352 -0.0614 -0.0468 374 THR B N   
7218 C CA  . THR B 374 ? 0.2321 0.2500 0.2559 -0.0387 -0.0620 -0.0539 374 THR B CA  
7219 C C   . THR B 374 ? 0.2293 0.2412 0.2351 -0.0293 -0.0630 -0.0483 374 THR B C   
7220 O O   . THR B 374 ? 0.2492 0.2674 0.2423 -0.0279 -0.0689 -0.0521 374 THR B O   
7221 C CB  . THR B 374 ? 0.2615 0.2583 0.2852 -0.0453 -0.0533 -0.0573 374 THR B CB  
7222 O OG1 . THR B 374 ? 0.2601 0.2605 0.2995 -0.0557 -0.0515 -0.0610 374 THR B OG1 
7223 C CG2 . THR B 374 ? 0.2557 0.2427 0.2651 -0.0478 -0.0542 -0.0670 374 THR B CG2 
7224 N N   . LEU B 375 ? 0.2194 0.2203 0.2237 -0.0234 -0.0571 -0.0391 375 LEU B N   
7225 C CA  . LEU B 375 ? 0.2490 0.2435 0.2377 -0.0171 -0.0562 -0.0330 375 LEU B CA  
7226 C C   . LEU B 375 ? 0.2589 0.2644 0.2393 -0.0113 -0.0650 -0.0286 375 LEU B C   
7227 O O   . LEU B 375 ? 0.2610 0.2653 0.2239 -0.0091 -0.0665 -0.0274 375 LEU B O   
7228 C CB  . LEU B 375 ? 0.2695 0.2532 0.2622 -0.0131 -0.0493 -0.0249 375 LEU B CB  
7229 C CG  . LEU B 375 ? 0.2602 0.2316 0.2550 -0.0156 -0.0406 -0.0281 375 LEU B CG  
7230 C CD1 . LEU B 375 ? 0.2238 0.1893 0.2239 -0.0110 -0.0356 -0.0213 375 LEU B CD1 
7231 C CD2 . LEU B 375 ? 0.2618 0.2278 0.2424 -0.0167 -0.0376 -0.0338 375 LEU B CD2 
7232 N N   . GLU B 376 ? 0.2249 0.2417 0.2163 -0.0076 -0.0710 -0.0260 376 GLU B N   
7233 C CA  . GLU B 376 ? 0.2799 0.3048 0.2621 0.0008  -0.0802 -0.0209 376 GLU B CA  
7234 C C   . GLU B 376 ? 0.3137 0.3517 0.2850 -0.0002 -0.0879 -0.0281 376 GLU B C   
7235 O O   . GLU B 376 ? 0.3023 0.3431 0.2581 0.0076  -0.0946 -0.0228 376 GLU B O   
7236 C CB  . GLU B 376 ? 0.2659 0.3028 0.2634 0.0069  -0.0857 -0.0188 376 GLU B CB  
7237 C CG  . GLU B 376 ? 0.3138 0.3738 0.3282 0.0024  -0.0904 -0.0286 376 GLU B CG  
7238 C CD  . GLU B 376 ? 0.3672 0.4428 0.3957 0.0108  -0.0957 -0.0265 376 GLU B CD  
7239 O OE1 . GLU B 376 ? 0.3207 0.3869 0.3429 0.0218  -0.0979 -0.0179 376 GLU B OE1 
7240 O OE2 . GLU B 376 ? 0.3703 0.4678 0.4165 0.0063  -0.0975 -0.0340 376 GLU B OE2 
7241 N N   . LYS B 377 ? 0.2478 0.2926 0.2258 -0.0094 -0.0876 -0.0402 377 LYS B N   
7242 C CA  . LYS B 377 ? 0.2559 0.3138 0.2239 -0.0112 -0.0954 -0.0498 377 LYS B CA  
7243 C C   . LYS B 377 ? 0.3205 0.3661 0.2683 -0.0129 -0.0908 -0.0527 377 LYS B C   
7244 O O   . LYS B 377 ? 0.3081 0.3636 0.2414 -0.0113 -0.0976 -0.0588 377 LYS B O   
7245 C CB  . LYS B 377 ? 0.2941 0.3666 0.2810 -0.0217 -0.0983 -0.0634 377 LYS B CB  
7246 C CG  . LYS B 377 ? 0.4057 0.4994 0.4131 -0.0200 -0.1040 -0.0628 377 LYS B CG  
7247 C CD  . LYS B 377 ? 0.4903 0.5914 0.5205 -0.0337 -0.1004 -0.0721 377 LYS B CD  
7248 C CE  . LYS B 377 ? 0.5389 0.6612 0.5906 -0.0312 -0.1024 -0.0693 377 LYS B CE  
7249 N NZ  . LYS B 377 ? 0.3737 0.4845 0.4234 -0.0198 -0.0980 -0.0558 377 LYS B NZ  
7250 N N   . GLU B 378 ? 0.2884 0.3155 0.2348 -0.0154 -0.0797 -0.0499 378 GLU B N   
7251 C CA  . GLU B 378 ? 0.2802 0.2997 0.2085 -0.0162 -0.0752 -0.0548 378 GLU B CA  
7252 C C   . GLU B 378 ? 0.3639 0.3827 0.2704 -0.0085 -0.0748 -0.0439 378 GLU B C   
7253 O O   . GLU B 378 ? 0.4388 0.4504 0.3459 -0.0045 -0.0715 -0.0306 378 GLU B O   
7254 C CB  . GLU B 378 ? 0.2787 0.2812 0.2128 -0.0198 -0.0638 -0.0564 378 GLU B CB  
7255 C CG  . GLU B 378 ? 0.2687 0.2660 0.2217 -0.0274 -0.0622 -0.0640 378 GLU B CG  
7256 C CD  . GLU B 378 ? 0.4867 0.4898 0.4405 -0.0348 -0.0684 -0.0793 378 GLU B CD  
7257 O OE1 . GLU B 378 ? 0.4289 0.4367 0.3662 -0.0332 -0.0722 -0.0869 378 GLU B OE1 
7258 O OE2 . GLU B 378 ? 0.5266 0.5303 0.4977 -0.0428 -0.0693 -0.0841 378 GLU B OE2 
7259 N N   . GLU B 379 ? 0.3567 0.3821 0.2430 -0.0068 -0.0778 -0.0497 379 GLU B N   
7260 C CA  . GLU B 379 ? 0.4117 0.4362 0.2741 -0.0005 -0.0758 -0.0388 379 GLU B CA  
7261 C C   . GLU B 379 ? 0.4084 0.4238 0.2613 -0.0023 -0.0632 -0.0385 379 GLU B C   
7262 O O   . GLU B 379 ? 0.4427 0.4546 0.2814 0.0005  -0.0574 -0.0259 379 GLU B O   
7263 C CB  . GLU B 379 ? 0.4785 0.5183 0.3207 0.0042  -0.0862 -0.0440 379 GLU B CB  
7264 C CG  . GLU B 379 ? 0.5689 0.6228 0.4188 0.0084  -0.1000 -0.0440 379 GLU B CG  
7265 C CD  . GLU B 379 ? 0.6102 0.6818 0.4393 0.0140  -0.1113 -0.0508 379 GLU B CD  
7266 O OE1 . GLU B 379 ? 0.8399 0.9108 0.6463 0.0150  -0.1074 -0.0535 379 GLU B OE1 
7267 O OE2 . GLU B 379 ? 0.5697 0.6581 0.4048 0.0181  -0.1240 -0.0541 379 GLU B OE2 
7268 N N   . TRP B 380 ? 0.3382 0.3501 0.1987 -0.0067 -0.0586 -0.0519 380 TRP B N   
7269 C CA  . TRP B 380 ? 0.3332 0.3398 0.1856 -0.0063 -0.0472 -0.0538 380 TRP B CA  
7270 C C   . TRP B 380 ? 0.3508 0.3470 0.2194 -0.0077 -0.0378 -0.0456 380 TRP B C   
7271 O O   . TRP B 380 ? 0.3570 0.3527 0.2206 -0.0067 -0.0280 -0.0445 380 TRP B O   
7272 C CB  . TRP B 380 ? 0.3415 0.3469 0.1924 -0.0080 -0.0472 -0.0729 380 TRP B CB  
7273 C CG  . TRP B 380 ? 0.3333 0.3281 0.2065 -0.0134 -0.0487 -0.0807 380 TRP B CG  
7274 C CD1 . TRP B 380 ? 0.3299 0.3275 0.2154 -0.0185 -0.0579 -0.0864 380 TRP B CD1 
7275 C CD2 . TRP B 380 ? 0.3071 0.2877 0.1929 -0.0141 -0.0403 -0.0826 380 TRP B CD2 
7276 N NE1 . TRP B 380 ? 0.3604 0.3445 0.2643 -0.0237 -0.0547 -0.0907 380 TRP B NE1 
7277 C CE2 . TRP B 380 ? 0.3065 0.2789 0.2099 -0.0201 -0.0444 -0.0881 380 TRP B CE2 
7278 C CE3 . TRP B 380 ? 0.3381 0.3140 0.2222 -0.0099 -0.0298 -0.0803 380 TRP B CE3 
7279 C CZ2 . TRP B 380 ? 0.2826 0.2386 0.1985 -0.0212 -0.0383 -0.0900 380 TRP B CZ2 
7280 C CZ3 . TRP B 380 ? 0.3110 0.2730 0.2091 -0.0097 -0.0250 -0.0835 380 TRP B CZ3 
7281 C CH2 . TRP B 380 ? 0.3496 0.3001 0.2619 -0.0149 -0.0293 -0.0877 380 TRP B CH2 
7282 N N   . ILE B 381 ? 0.2906 0.2815 0.1786 -0.0096 -0.0409 -0.0411 381 ILE B N   
7283 C CA  . ILE B 381 ? 0.2600 0.2432 0.1620 -0.0099 -0.0343 -0.0319 381 ILE B CA  
7284 C C   . ILE B 381 ? 0.3366 0.3197 0.2364 -0.0080 -0.0378 -0.0176 381 ILE B C   
7285 O O   . ILE B 381 ? 0.3277 0.3146 0.2282 -0.0061 -0.0473 -0.0161 381 ILE B O   
7286 C CB  . ILE B 381 ? 0.2377 0.2141 0.1609 -0.0121 -0.0350 -0.0368 381 ILE B CB  
7287 C CG1 . ILE B 381 ? 0.2773 0.2477 0.2015 -0.0133 -0.0312 -0.0499 381 ILE B CG1 
7288 C CG2 . ILE B 381 ? 0.2438 0.2147 0.1802 -0.0111 -0.0300 -0.0274 381 ILE B CG2 
7289 C CD1 . ILE B 381 ? 0.3160 0.2786 0.2572 -0.0170 -0.0333 -0.0545 381 ILE B CD1 
7290 N N   . GLU B 382 ? 0.2782 0.2569 0.1761 -0.0084 -0.0304 -0.0075 382 GLU B N   
7291 C CA  . GLU B 382 ? 0.2755 0.2478 0.1729 -0.0072 -0.0330 0.0062  382 GLU B CA  
7292 C C   . GLU B 382 ? 0.2625 0.2277 0.1792 -0.0092 -0.0280 0.0089  382 GLU B C   
7293 O O   . GLU B 382 ? 0.2827 0.2484 0.2019 -0.0122 -0.0188 0.0089  382 GLU B O   
7294 C CB  . GLU B 382 ? 0.3353 0.3067 0.2109 -0.0076 -0.0289 0.0168  382 GLU B CB  
7295 C CG  . GLU B 382 ? 0.4551 0.4144 0.3280 -0.0068 -0.0312 0.0319  382 GLU B CG  
7296 C CD  . GLU B 382 ? 0.6831 0.6395 0.5290 -0.0056 -0.0306 0.0437  382 GLU B CD  
7297 O OE1 . GLU B 382 ? 0.6579 0.6251 0.4870 -0.0056 -0.0274 0.0399  382 GLU B OE1 
7298 O OE2 . GLU B 382 ? 0.8266 0.7689 0.6669 -0.0041 -0.0333 0.0570  382 GLU B OE2 
7299 N N   . THR B 383 ? 0.2449 0.2062 0.1756 -0.0069 -0.0340 0.0101  383 THR B N   
7300 C CA  . THR B 383 ? 0.2299 0.1847 0.1762 -0.0077 -0.0303 0.0130  383 THR B CA  
7301 C C   . THR B 383 ? 0.3033 0.2484 0.2432 -0.0090 -0.0289 0.0250  383 THR B C   
7302 O O   . THR B 383 ? 0.2679 0.2078 0.1947 -0.0062 -0.0346 0.0326  383 THR B O   
7303 C CB  . THR B 383 ? 0.2192 0.1741 0.1813 -0.0042 -0.0365 0.0102  383 THR B CB  
7304 O OG1 . THR B 383 ? 0.2317 0.1867 0.1890 0.0004  -0.0457 0.0147  383 THR B OG1 
7305 C CG2 . THR B 383 ? 0.2654 0.2268 0.2348 -0.0052 -0.0361 -0.0003 383 THR B CG2 
7306 N N   . LEU B 384 ? 0.2187 0.1609 0.1677 -0.0133 -0.0218 0.0264  384 LEU B N   
7307 C CA  . LEU B 384 ? 0.2340 0.1657 0.1781 -0.0179 -0.0185 0.0370  384 LEU B CA  
7308 C C   . LEU B 384 ? 0.2366 0.1600 0.1977 -0.0181 -0.0200 0.0372  384 LEU B C   
7309 O O   . LEU B 384 ? 0.2598 0.1900 0.2368 -0.0163 -0.0196 0.0287  384 LEU B O   
7310 C CB  . LEU B 384 ? 0.2416 0.1809 0.1814 -0.0256 -0.0070 0.0381  384 LEU B CB  
7311 C CG  . LEU B 384 ? 0.2985 0.2473 0.2192 -0.0255 -0.0036 0.0375  384 LEU B CG  
7312 C CD1 . LEU B 384 ? 0.3440 0.3033 0.2633 -0.0327 0.0088  0.0380  384 LEU B CD1 
7313 C CD2 . LEU B 384 ? 0.3037 0.2431 0.2029 -0.0230 -0.0094 0.0482  384 LEU B CD2 
7314 N N   . THR B 385 ? 0.2417 0.1490 0.1977 -0.0201 -0.0218 0.0470  385 THR B N   
7315 C CA  . THR B 385 ? 0.3189 0.2174 0.2898 -0.0235 -0.0211 0.0465  385 THR B CA  
7316 C C   . THR B 385 ? 0.2848 0.1921 0.2630 -0.0340 -0.0104 0.0449  385 THR B C   
7317 O O   . THR B 385 ? 0.2611 0.1777 0.2297 -0.0389 -0.0029 0.0470  385 THR B O   
7318 C CB  . THR B 385 ? 0.2629 0.1374 0.2256 -0.0231 -0.0262 0.0570  385 THR B CB  
7319 O OG1 . THR B 385 ? 0.2903 0.1558 0.2357 -0.0312 -0.0199 0.0688  385 THR B OG1 
7320 C CG2 . THR B 385 ? 0.2659 0.1349 0.2215 -0.0102 -0.0377 0.0582  385 THR B CG2 
7321 N N   . LEU B 386 ? 0.2617 0.1685 0.2575 -0.0370 -0.0099 0.0399  386 LEU B N   
7322 C CA  . LEU B 386 ? 0.2558 0.1733 0.2614 -0.0477 -0.0005 0.0378  386 LEU B CA  
7323 C C   . LEU B 386 ? 0.2728 0.1800 0.2659 -0.0592 0.0061  0.0501  386 LEU B C   
7324 O O   . LEU B 386 ? 0.2831 0.2054 0.2753 -0.0674 0.0163  0.0508  386 LEU B O   
7325 C CB  . LEU B 386 ? 0.2560 0.1731 0.2819 -0.0493 -0.0031 0.0304  386 LEU B CB  
7326 C CG  . LEU B 386 ? 0.2096 0.1372 0.2469 -0.0380 -0.0087 0.0193  386 LEU B CG  
7327 C CD1 . LEU B 386 ? 0.1877 0.1180 0.2441 -0.0397 -0.0110 0.0110  386 LEU B CD1 
7328 C CD2 . LEU B 386 ? 0.2274 0.1757 0.2649 -0.0342 -0.0036 0.0132  386 LEU B CD2 
7329 N N   . GLU B 387 ? 0.2801 0.1614 0.2624 -0.0592 0.0007  0.0602  387 GLU B N   
7330 C CA  . GLU B 387 ? 0.3140 0.1794 0.2804 -0.0695 0.0067  0.0748  387 GLU B CA  
7331 C C   . GLU B 387 ? 0.3236 0.1995 0.2687 -0.0684 0.0119  0.0811  387 GLU B C   
7332 O O   . GLU B 387 ? 0.3456 0.2261 0.2827 -0.0795 0.0228  0.0888  387 GLU B O   
7333 C CB  . GLU B 387 ? 0.3939 0.2262 0.3504 -0.0653 -0.0024 0.0839  387 GLU B CB  
7334 C CG  . GLU B 387 ? 0.4898 0.2971 0.4325 -0.0774 0.0033  0.0997  387 GLU B CG  
7335 C CD  . GLU B 387 ? 0.8127 0.6089 0.7253 -0.0723 0.0027  0.1144  387 GLU B CD  
7336 O OE1 . GLU B 387 ? 0.9667 0.7829 0.8706 -0.0635 0.0013  0.1109  387 GLU B OE1 
7337 O OE2 . GLU B 387 ? 0.8826 0.6524 0.7816 -0.0749 0.0035  0.1275  387 GLU B OE2 
7338 N N   . GLU B 388 ? 0.3129 0.1941 0.2489 -0.0555 0.0046  0.0777  388 GLU B N   
7339 C CA  . GLU B 388 ? 0.3951 0.2877 0.3108 -0.0537 0.0085  0.0811  388 GLU B CA  
7340 C C   . GLU B 388 ? 0.3635 0.2832 0.2874 -0.0585 0.0190  0.0718  388 GLU B C   
7341 O O   . GLU B 388 ? 0.3977 0.3271 0.3070 -0.0634 0.0278  0.0767  388 GLU B O   
7342 C CB  . GLU B 388 ? 0.3144 0.2085 0.2217 -0.0400 -0.0027 0.0769  388 GLU B CB  
7343 C CG  . GLU B 388 ? 0.3966 0.2675 0.2900 -0.0330 -0.0127 0.0876  388 GLU B CG  
7344 C CD  . GLU B 388 ? 0.4663 0.3432 0.3598 -0.0196 -0.0249 0.0805  388 GLU B CD  
7345 O OE1 . GLU B 388 ? 0.3290 0.2227 0.2380 -0.0172 -0.0259 0.0673  388 GLU B OE1 
7346 O OE2 . GLU B 388 ? 0.5741 0.4394 0.4518 -0.0115 -0.0333 0.0886  388 GLU B OE2 
7347 N N   . ALA B 389 ? 0.3393 0.2721 0.2853 -0.0559 0.0181  0.0583  389 ALA B N   
7348 C CA  . ALA B 389 ? 0.3208 0.2787 0.2754 -0.0578 0.0271  0.0485  389 ALA B CA  
7349 C C   . ALA B 389 ? 0.3227 0.2892 0.2822 -0.0715 0.0391  0.0536  389 ALA B C   
7350 O O   . ALA B 389 ? 0.3619 0.3494 0.3179 -0.0743 0.0490  0.0509  389 ALA B O   
7351 C CB  . ALA B 389 ? 0.2622 0.2289 0.2384 -0.0512 0.0229  0.0350  389 ALA B CB  
7352 N N   . MET B 390 ? 0.3083 0.2595 0.2761 -0.0805 0.0387  0.0602  390 MET B N   
7353 C CA  . MET B 390 ? 0.3185 0.2784 0.2946 -0.0962 0.0503  0.0643  390 MET B CA  
7354 C C   . MET B 390 ? 0.4349 0.3895 0.3869 -0.1046 0.0593  0.0797  390 MET B C   
7355 O O   . MET B 390 ? 0.4379 0.4121 0.3924 -0.1158 0.0725  0.0815  390 MET B O   
7356 C CB  . MET B 390 ? 0.3444 0.2866 0.3368 -0.1045 0.0465  0.0657  390 MET B CB  
7357 C CG  . MET B 390 ? 0.5004 0.4476 0.5014 -0.1242 0.0583  0.0714  390 MET B CG  
7358 S SD  . MET B 390 ? 0.7603 0.6924 0.7866 -0.1337 0.0527  0.0662  390 MET B SD  
7359 C CE  . MET B 390 ? 0.7312 0.6134 0.7350 -0.1370 0.0472  0.0847  390 MET B CE  
7360 N N   . ARG B 391 ? 0.4704 0.4010 0.3984 -0.0988 0.0527  0.0911  391 ARG B N   
7361 C CA  . ARG B 391 ? 0.4966 0.4177 0.3985 -0.1062 0.0606  0.1083  391 ARG B CA  
7362 C C   . ARG B 391 ? 0.4576 0.3932 0.3354 -0.0969 0.0621  0.1084  391 ARG B C   
7363 O O   . ARG B 391 ? 0.4750 0.4081 0.3289 -0.1024 0.0701  0.1221  391 ARG B O   
7364 C CB  . ARG B 391 ? 0.5924 0.4742 0.4795 -0.1059 0.0525  0.1234  391 ARG B CB  
7365 C CG  . ARG B 391 ? 0.6810 0.5432 0.5887 -0.1158 0.0508  0.1237  391 ARG B CG  
7366 C CD  . ARG B 391 ? 0.8081 0.6358 0.7082 -0.1054 0.0364  0.1288  391 ARG B CD  
7367 N NE  . ARG B 391 ? 0.9223 0.7203 0.8134 -0.1104 0.0384  0.1431  391 ARG B NE  
7368 C CZ  . ARG B 391 ? 0.9471 0.7206 0.8192 -0.0976 0.0302  0.1528  391 ARG B CZ  
7369 N NH1 . ARG B 391 ? 0.9494 0.7235 0.8076 -0.0817 0.0185  0.1509  391 ARG B NH1 
7370 N NH2 . ARG B 391 ? 0.9418 0.6915 0.8102 -0.1002 0.0332  0.1639  391 ARG B NH2 
7371 N N   . LYS B 392 ? 0.4467 0.3967 0.3292 -0.0837 0.0551  0.0936  392 LYS B N   
7372 C CA  . LYS B 392 ? 0.5004 0.4624 0.3604 -0.0746 0.0546  0.0913  392 LYS B CA  
7373 C C   . LYS B 392 ? 0.4447 0.4308 0.2958 -0.0819 0.0702  0.0925  392 LYS B C   
7374 O O   . LYS B 392 ? 0.4305 0.4389 0.3016 -0.0867 0.0788  0.0828  392 LYS B O   
7375 C CB  . LYS B 392 ? 0.5745 0.5476 0.4459 -0.0621 0.0459  0.0732  392 LYS B CB  
7376 C CG  . LYS B 392 ? 0.7152 0.6859 0.5650 -0.0509 0.0367  0.0715  392 LYS B CG  
7377 C CD  . LYS B 392 ? 0.7196 0.6659 0.5627 -0.0464 0.0244  0.0811  392 LYS B CD  
7378 C CE  . LYS B 392 ? 0.7189 0.6669 0.5452 -0.0349 0.0135  0.0771  392 LYS B CE  
7379 N NZ  . LYS B 392 ? 0.8060 0.7390 0.6408 -0.0278 -0.0002 0.0771  392 LYS B NZ  
7380 N N   . GLU B 393 ? 0.4987 0.4827 0.3191 -0.0814 0.0738  0.1041  393 GLU B N   
7381 C CA  . GLU B 393 ? 0.6122 0.6202 0.4218 -0.0888 0.0901  0.1069  393 GLU B CA  
7382 C C   . GLU B 393 ? 0.5990 0.6340 0.4018 -0.0776 0.0913  0.0906  393 GLU B C   
7383 O O   . GLU B 393 ? 0.5877 0.6499 0.3933 -0.0818 0.1048  0.0855  393 GLU B O   
7384 C CB  . GLU B 393 ? 0.7090 0.7018 0.4864 -0.0949 0.0957  0.1293  393 GLU B CB  
7385 C CG  . GLU B 393 ? 0.7977 0.7582 0.5795 -0.1059 0.0946  0.1461  393 GLU B CG  
7386 C CD  . GLU B 393 ? 0.9585 0.9158 0.7318 -0.1170 0.1092  0.1624  393 GLU B CD  
7387 O OE1 . GLU B 393 ? 1.0222 0.9815 0.7673 -0.1107 0.1132  0.1712  393 GLU B OE1 
7388 O OE2 . GLU B 393 ? 0.9915 0.9443 0.7888 -0.1301 0.1159  0.1648  393 GLU B OE2 
7389 N N   . ASP B 394 ? 0.4730 0.5021 0.2688 -0.0638 0.0776  0.0809  394 ASP B N   
7390 C CA  . ASP B 394 ? 0.5129 0.5630 0.2984 -0.0535 0.0778  0.0653  394 ASP B CA  
7391 C C   . ASP B 394 ? 0.4873 0.5487 0.3001 -0.0480 0.0757  0.0450  394 ASP B C   
7392 O O   . ASP B 394 ? 0.5718 0.6329 0.3833 -0.0375 0.0667  0.0311  394 ASP B O   
7393 C CB  . ASP B 394 ? 0.6290 0.6679 0.3905 -0.0429 0.0645  0.0652  394 ASP B CB  
7394 C CG  . ASP B 394 ? 0.7351 0.7492 0.5070 -0.0398 0.0492  0.0684  394 ASP B CG  
7395 O OD1 . ASP B 394 ? 0.7022 0.7021 0.4908 -0.0471 0.0501  0.0770  394 ASP B OD1 
7396 O OD2 . ASP B 394 ? 0.7253 0.7356 0.4893 -0.0302 0.0364  0.0614  394 ASP B OD2 
7397 N N   . VAL B 395 ? 0.4560 0.5277 0.2937 -0.0553 0.0841  0.0431  395 VAL B N   
7398 C CA  . VAL B 395 ? 0.3676 0.4493 0.2308 -0.0493 0.0823  0.0258  395 VAL B CA  
7399 C C   . VAL B 395 ? 0.4622 0.5747 0.3352 -0.0530 0.0975  0.0203  395 VAL B C   
7400 O O   . VAL B 395 ? 0.4515 0.5750 0.3190 -0.0643 0.1095  0.0317  395 VAL B O   
7401 C CB  . VAL B 395 ? 0.4554 0.5202 0.3434 -0.0520 0.0743  0.0272  395 VAL B CB  
7402 C CG1 . VAL B 395 ? 0.4658 0.5040 0.3456 -0.0473 0.0597  0.0317  395 VAL B CG1 
7403 C CG2 . VAL B 395 ? 0.5350 0.6001 0.4341 -0.0665 0.0824  0.0396  395 VAL B CG2 
7404 N N   . LYS B 396 ? 0.3295 0.4564 0.2169 -0.0430 0.0972  0.0026  396 LYS B N   
7405 C CA  . LYS B 396 ? 0.3563 0.5160 0.2559 -0.0437 0.1105  -0.0052 396 LYS B CA  
7406 C C   . LYS B 396 ? 0.3345 0.5006 0.2646 -0.0524 0.1128  -0.0033 396 LYS B C   
7407 O O   . LYS B 396 ? 0.2925 0.4399 0.2373 -0.0505 0.1021  -0.0045 396 LYS B O   
7408 C CB  . LYS B 396 ? 0.4462 0.6177 0.3471 -0.0270 0.1087  -0.0255 396 LYS B CB  
7409 C CG  . LYS B 396 ? 0.4836 0.6934 0.3920 -0.0245 0.1229  -0.0348 396 LYS B CG  
7410 C CD  . LYS B 396 ? 0.4452 0.6630 0.3570 -0.0058 0.1200  -0.0559 396 LYS B CD  
7411 C CE  . LYS B 396 ? 0.4775 0.6880 0.3606 0.0041  0.1171  -0.0637 396 LYS B CE  
7412 N NZ  . LYS B 396 ? 0.5464 0.7788 0.4127 0.0029  0.1282  -0.0617 396 LYS B NZ  
7413 N N   . THR B 397 ? 0.3878 0.4191 0.2260 -0.0958 0.0094  -0.0466 397 THR B N   
7414 C CA  . THR B 397 ? 0.3504 0.3790 0.2069 -0.0912 0.0169  -0.0371 397 THR B CA  
7415 C C   . THR B 397 ? 0.4064 0.4365 0.2663 -0.0887 0.0320  -0.0477 397 THR B C   
7416 O O   . THR B 397 ? 0.3956 0.4290 0.2396 -0.0900 0.0381  -0.0609 397 THR B O   
7417 C CB  . THR B 397 ? 0.3850 0.4157 0.2302 -0.0931 0.0156  -0.0193 397 THR B CB  
7418 O OG1 . THR B 397 ? 0.4010 0.4386 0.2182 -0.0987 0.0219  -0.0204 397 THR B OG1 
7419 C CG2 . THR B 397 ? 0.4400 0.4694 0.2836 -0.0919 0.0003  -0.0078 397 THR B CG2 
7420 N N   . GLU B 398 ? 0.3257 0.3554 0.2065 -0.0844 0.0379  -0.0423 398 GLU B N   
7421 C CA  . GLU B 398 ? 0.4042 0.4401 0.2930 -0.0803 0.0514  -0.0511 398 GLU B CA  
7422 C C   . GLU B 398 ? 0.3794 0.4195 0.2864 -0.0792 0.0551  -0.0397 398 GLU B C   
7423 O O   . GLU B 398 ? 0.3404 0.3727 0.2600 -0.0781 0.0471  -0.0305 398 GLU B O   
7424 C CB  . GLU B 398 ? 0.4128 0.4395 0.3144 -0.0730 0.0524  -0.0661 398 GLU B CB  
7425 C CG  . GLU B 398 ? 0.4930 0.5263 0.4068 -0.0647 0.0651  -0.0753 398 GLU B CG  
7426 C CD  . GLU B 398 ? 0.6021 0.6204 0.5228 -0.0564 0.0654  -0.0902 398 GLU B CD  
7427 O OE1 . GLU B 398 ? 0.7105 0.7153 0.6191 -0.0603 0.0586  -0.0975 398 GLU B OE1 
7428 O OE2 . GLU B 398 ? 0.6108 0.6300 0.5486 -0.0463 0.0717  -0.0945 398 GLU B OE2 
7429 N N   . VAL B 399 ? 0.2996 0.3538 0.2067 -0.0806 0.0672  -0.0409 399 VAL B N   
7430 C CA  . VAL B 399 ? 0.2773 0.3382 0.2029 -0.0811 0.0712  -0.0327 399 VAL B CA  
7431 C C   . VAL B 399 ? 0.3664 0.4301 0.3168 -0.0704 0.0742  -0.0422 399 VAL B C   
7432 O O   . VAL B 399 ? 0.3508 0.4183 0.3016 -0.0634 0.0801  -0.0559 399 VAL B O   
7433 C CB  . VAL B 399 ? 0.3079 0.3864 0.2235 -0.0898 0.0829  -0.0288 399 VAL B CB  
7434 C CG1 . VAL B 399 ? 0.3089 0.3984 0.2465 -0.0918 0.0879  -0.0235 399 VAL B CG1 
7435 C CG2 . VAL B 399 ? 0.3371 0.4087 0.2259 -0.1003 0.0790  -0.0162 399 VAL B CG2 
7436 N N   . ILE B 400 ? 0.3347 0.3949 0.3043 -0.0681 0.0696  -0.0352 400 ILE B N   
7437 C CA  . ILE B 400 ? 0.3155 0.3800 0.3077 -0.0579 0.0718  -0.0415 400 ILE B CA  
7438 C C   . ILE B 400 ? 0.3276 0.4084 0.3347 -0.0611 0.0759  -0.0352 400 ILE B C   
7439 O O   . ILE B 400 ? 0.3082 0.3845 0.3129 -0.0697 0.0718  -0.0242 400 ILE B O   
7440 C CB  . ILE B 400 ? 0.2747 0.3205 0.2756 -0.0521 0.0617  -0.0402 400 ILE B CB  
7441 C CG1 . ILE B 400 ? 0.2821 0.3306 0.3038 -0.0412 0.0632  -0.0442 400 ILE B CG1 
7442 C CG2 . ILE B 400 ? 0.3050 0.3429 0.3055 -0.0578 0.0532  -0.0277 400 ILE B CG2 
7443 C CD1 . ILE B 400 ? 0.3276 0.3570 0.3546 -0.0360 0.0551  -0.0436 400 ILE B CD1 
7444 N N   . GLU B 401 ? 0.2402 0.3401 0.2625 -0.0543 0.0838  -0.0430 401 GLU B N   
7445 C CA  . GLU B 401 ? 0.2948 0.4167 0.3319 -0.0594 0.0884  -0.0388 401 GLU B CA  
7446 C C   . GLU B 401 ? 0.2446 0.3682 0.3039 -0.0522 0.0823  -0.0371 401 GLU B C   
7447 O O   . GLU B 401 ? 0.2338 0.3697 0.3034 -0.0596 0.0820  -0.0315 401 GLU B O   
7448 C CB  . GLU B 401 ? 0.2869 0.4383 0.3289 -0.0574 0.1017  -0.0480 401 GLU B CB  
7449 C CG  . GLU B 401 ? 0.4502 0.6066 0.4689 -0.0689 0.1096  -0.0471 401 GLU B CG  
7450 C CD  . GLU B 401 ? 0.6123 0.7671 0.6222 -0.0871 0.1087  -0.0326 401 GLU B CD  
7451 O OE1 . GLU B 401 ? 0.4981 0.6567 0.5239 -0.0916 0.1053  -0.0264 401 GLU B OE1 
7452 O OE2 . GLU B 401 ? 0.7596 0.9079 0.7450 -0.0968 0.1110  -0.0276 401 GLU B OE2 
7453 N N   . SER B 402 ? 0.2302 0.3406 0.2954 -0.0392 0.0771  -0.0413 402 SER B N   
7454 C CA  . SER B 402 ? 0.2411 0.3544 0.3249 -0.0314 0.0715  -0.0393 402 SER B CA  
7455 C C   . SER B 402 ? 0.2487 0.3362 0.3294 -0.0225 0.0640  -0.0393 402 SER B C   
7456 O O   . SER B 402 ? 0.2432 0.3163 0.3133 -0.0189 0.0652  -0.0451 402 SER B O   
7457 C CB  . SER B 402 ? 0.1889 0.3301 0.2914 -0.0213 0.0778  -0.0467 402 SER B CB  
7458 O OG  . SER B 402 ? 0.2529 0.3981 0.3717 -0.0137 0.0709  -0.0436 402 SER B OG  
7459 N N   . VAL B 403 ? 0.2057 0.2875 0.2947 -0.0204 0.0566  -0.0329 403 VAL B N   
7460 C CA  . VAL B 403 ? 0.1750 0.2359 0.2634 -0.0124 0.0505  -0.0317 403 VAL B CA  
7461 C C   . VAL B 403 ? 0.1995 0.2695 0.3034 -0.0016 0.0478  -0.0304 403 VAL B C   
7462 O O   . VAL B 403 ? 0.2011 0.2917 0.3156 -0.0038 0.0473  -0.0284 403 VAL B O   
7463 C CB  . VAL B 403 ? 0.1701 0.2141 0.2499 -0.0201 0.0436  -0.0239 403 VAL B CB  
7464 C CG1 . VAL B 403 ? 0.1924 0.2293 0.2567 -0.0295 0.0446  -0.0244 403 VAL B CG1 
7465 C CG2 . VAL B 403 ? 0.1795 0.2312 0.2651 -0.0247 0.0398  -0.0173 403 VAL B CG2 
7466 N N   . LYS B 404 ? 0.2525 0.3065 0.3568 0.0094  0.0453  -0.0312 404 LYS B N   
7467 C CA  . LYS B 404 ? 0.2034 0.2612 0.3186 0.0204  0.0406  -0.0272 404 LYS B CA  
7468 C C   . LYS B 404 ? 0.1762 0.2216 0.2865 0.0147  0.0337  -0.0180 404 LYS B C   
7469 O O   . LYS B 404 ? 0.2399 0.2639 0.3399 0.0104  0.0322  -0.0157 404 LYS B O   
7470 C CB  . LYS B 404 ? 0.3042 0.3465 0.4198 0.0357  0.0412  -0.0309 404 LYS B CB  
7471 C CG  . LYS B 404 ? 0.4595 0.5175 0.5828 0.0466  0.0482  -0.0413 404 LYS B CG  
7472 C CD  . LYS B 404 ? 0.5017 0.5544 0.6332 0.0670  0.0457  -0.0417 404 LYS B CD  
7473 C CE  . LYS B 404 ? 0.5340 0.6084 0.6769 0.0810  0.0527  -0.0527 404 LYS B CE  
7474 N NZ  . LYS B 404 ? 0.6247 0.6756 0.7557 0.0861  0.0589  -0.0635 404 LYS B NZ  
7475 N N   . ALA B 405 ? 0.1831 0.2441 0.3008 0.0141  0.0296  -0.0137 405 ALA B N   
7476 C CA  . ALA B 405 ? 0.1834 0.2363 0.2954 0.0082  0.0242  -0.0067 405 ALA B CA  
7477 C C   . ALA B 405 ? 0.2135 0.2458 0.3195 0.0143  0.0213  -0.0012 405 ALA B C   
7478 O O   . ALA B 405 ? 0.2319 0.2593 0.3407 0.0257  0.0206  -0.0006 405 ALA B O   
7479 C CB  . ALA B 405 ? 0.1493 0.2224 0.2693 0.0077  0.0201  -0.0050 405 ALA B CB  
7480 N N   . GLY B 406 ? 0.1983 0.2186 0.2961 0.0068  0.0197  0.0031  406 GLY B N   
7481 C CA  . GLY B 406 ? 0.1909 0.1938 0.2828 0.0093  0.0178  0.0094  406 GLY B CA  
7482 C C   . GLY B 406 ? 0.1705 0.1683 0.2563 -0.0001 0.0171  0.0131  406 GLY B C   
7483 O O   . GLY B 406 ? 0.2195 0.2267 0.3054 -0.0058 0.0167  0.0116  406 GLY B O   
7484 N N   . THR B 407 ? 0.1909 0.1735 0.2715 -0.0015 0.0171  0.0181  407 THR B N   
7485 C CA  . THR B 407 ? 0.2043 0.1853 0.2812 -0.0100 0.0172  0.0217  407 THR B CA  
7486 C C   . THR B 407 ? 0.2361 0.1994 0.3094 -0.0157 0.0188  0.0220  407 THR B C   
7487 O O   . THR B 407 ? 0.2260 0.1739 0.2974 -0.0119 0.0196  0.0197  407 THR B O   
7488 C CB  . THR B 407 ? 0.2269 0.2126 0.3009 -0.0082 0.0158  0.0296  407 THR B CB  
7489 O OG1 . THR B 407 ? 0.2322 0.2020 0.3013 -0.0063 0.0163  0.0365  407 THR B OG1 
7490 C CG2 . THR B 407 ? 0.2100 0.2100 0.2861 -0.0014 0.0130  0.0288  407 THR B CG2 
7491 N N   . TRP B 408 ? 0.1876 0.1532 0.2601 -0.0248 0.0191  0.0244  408 TRP B N   
7492 C CA  . TRP B 408 ? 0.1978 0.1481 0.2676 -0.0333 0.0200  0.0246  408 TRP B CA  
7493 C C   . TRP B 408 ? 0.2419 0.1757 0.3067 -0.0334 0.0211  0.0333  408 TRP B C   
7494 O O   . TRP B 408 ? 0.2813 0.2002 0.3431 -0.0430 0.0221  0.0349  408 TRP B O   
7495 C CB  . TRP B 408 ? 0.1935 0.1566 0.2665 -0.0436 0.0195  0.0238  408 TRP B CB  
7496 C CG  . TRP B 408 ? 0.2187 0.1989 0.2950 -0.0450 0.0203  0.0303  408 TRP B CG  
7497 C CD1 . TRP B 408 ? 0.2427 0.2257 0.3165 -0.0398 0.0217  0.0370  408 TRP B CD1 
7498 C CD2 . TRP B 408 ? 0.2409 0.2394 0.3231 -0.0509 0.0198  0.0297  408 TRP B CD2 
7499 N NE1 . TRP B 408 ? 0.2133 0.2147 0.2902 -0.0424 0.0232  0.0397  408 TRP B NE1 
7500 C CE2 . TRP B 408 ? 0.2142 0.2259 0.2977 -0.0485 0.0221  0.0354  408 TRP B CE2 
7501 C CE3 . TRP B 408 ? 0.1885 0.1954 0.2749 -0.0569 0.0172  0.0248  408 TRP B CE3 
7502 C CZ2 . TRP B 408 ? 0.1811 0.2144 0.2715 -0.0508 0.0228  0.0355  408 TRP B CZ2 
7503 C CZ3 . TRP B 408 ? 0.1610 0.1898 0.2549 -0.0590 0.0166  0.0260  408 TRP B CZ3 
7504 C CH2 . TRP B 408 ? 0.2369 0.2790 0.3336 -0.0555 0.0199  0.0310  408 TRP B CH2 
7505 N N   . PHE B 409 ? 0.2385 0.1739 0.3013 -0.0238 0.0204  0.0394  409 PHE B N   
7506 C CA  . PHE B 409 ? 0.2626 0.1798 0.3177 -0.0219 0.0207  0.0494  409 PHE B CA  
7507 C C   . PHE B 409 ? 0.3300 0.2302 0.3835 -0.0094 0.0189  0.0471  409 PHE B C   
7508 O O   . PHE B 409 ? 0.3215 0.2332 0.3777 0.0026  0.0165  0.0473  409 PHE B O   
7509 C CB  . PHE B 409 ? 0.2837 0.2157 0.3354 -0.0188 0.0203  0.0583  409 PHE B CB  
7510 C CG  . PHE B 409 ? 0.4985 0.4119 0.5393 -0.0174 0.0205  0.0710  409 PHE B CG  
7511 C CD1 . PHE B 409 ? 0.7033 0.6047 0.7395 -0.0036 0.0168  0.0748  409 PHE B CD1 
7512 C CD2 . PHE B 409 ? 0.5087 0.4180 0.5436 -0.0296 0.0243  0.0798  409 PHE B CD2 
7513 C CE1 . PHE B 409 ? 0.7131 0.5944 0.7368 -0.0011 0.0161  0.0883  409 PHE B CE1 
7514 C CE2 . PHE B 409 ? 0.4990 0.3885 0.5209 -0.0297 0.0248  0.0934  409 PHE B CE2 
7515 C CZ  . PHE B 409 ? 0.6164 0.4899 0.6316 -0.0150 0.0203  0.0982  409 PHE B CZ  
7516 N N   . ASP B 410 ? 0.4441 0.3185 0.4940 -0.0120 0.0199  0.0435  410 ASP B N   
7517 C CA  . ASP B 410 ? 0.5244 0.3793 0.5726 0.0013  0.0190  0.0396  410 ASP B CA  
7518 C C   . ASP B 410 ? 0.4506 0.3263 0.5080 0.0112  0.0190  0.0289  410 ASP B C   
7519 O O   . ASP B 410 ? 0.4594 0.3293 0.5188 0.0257  0.0184  0.0259  410 ASP B O   
7520 C CB  . ASP B 410 ? 0.5108 0.3522 0.5527 0.0131  0.0164  0.0517  410 ASP B CB  
7521 C CG  . ASP B 410 ? 0.6243 0.4370 0.6541 0.0032  0.0173  0.0632  410 ASP B CG  
7522 O OD1 . ASP B 410 ? 0.7575 0.5471 0.7835 -0.0079 0.0195  0.0589  410 ASP B OD1 
7523 O OD2 . ASP B 410 ? 0.5994 0.4127 0.6222 0.0055  0.0159  0.0767  410 ASP B OD2 
7524 N N   . GLY B 411 ? 0.3571 0.2575 0.4203 0.0041  0.0198  0.0235  411 GLY B N   
7525 C CA  . GLY B 411 ? 0.3616 0.2825 0.4325 0.0109  0.0205  0.0152  411 GLY B CA  
7526 C C   . GLY B 411 ? 0.3100 0.2500 0.3873 0.0218  0.0178  0.0190  411 GLY B C   
7527 O O   . GLY B 411 ? 0.3011 0.2570 0.3862 0.0286  0.0186  0.0124  411 GLY B O   
7528 N N   . ASN B 412 ? 0.3043 0.2457 0.3784 0.0228  0.0147  0.0292  412 ASN B N   
7529 C CA  . ASN B 412 ? 0.2776 0.2378 0.3565 0.0331  0.0108  0.0322  412 ASN B CA  
7530 C C   . ASN B 412 ? 0.2499 0.2222 0.3245 0.0271  0.0085  0.0389  412 ASN B C   
7531 O O   . ASN B 412 ? 0.3022 0.2707 0.3720 0.0162  0.0109  0.0408  412 ASN B O   
7532 C CB  . ASN B 412 ? 0.3027 0.2494 0.3802 0.0486  0.0079  0.0372  412 ASN B CB  
7533 C CG  . ASN B 412 ? 0.4245 0.3438 0.4886 0.0474  0.0068  0.0494  412 ASN B CG  
7534 O OD1 . ASN B 412 ? 0.3928 0.3164 0.4501 0.0400  0.0060  0.0575  412 ASN B OD1 
7535 N ND2 . ASN B 412 ? 0.4532 0.3436 0.5126 0.0553  0.0070  0.0509  412 ASN B ND2 
7536 N N   . PHE B 413 ? 0.2426 0.2318 0.3191 0.0348  0.0039  0.0416  413 PHE B N   
7537 C CA  . PHE B 413 ? 0.2458 0.2491 0.3172 0.0303  0.0016  0.0451  413 PHE B CA  
7538 C C   . PHE B 413 ? 0.2814 0.2784 0.3411 0.0357  -0.0018 0.0571  413 PHE B C   
7539 O O   . PHE B 413 ? 0.2582 0.2695 0.3120 0.0344  -0.0044 0.0593  413 PHE B O   
7540 C CB  . PHE B 413 ? 0.1919 0.2210 0.2720 0.0315  -0.0018 0.0378  413 PHE B CB  
7541 C CG  . PHE B 413 ? 0.1794 0.2146 0.2674 0.0234  0.0018  0.0281  413 PHE B CG  
7542 C CD1 . PHE B 413 ? 0.2112 0.2467 0.2955 0.0134  0.0038  0.0256  413 PHE B CD1 
7543 C CD2 . PHE B 413 ? 0.2547 0.2960 0.3530 0.0267  0.0035  0.0218  413 PHE B CD2 
7544 C CE1 . PHE B 413 ? 0.1978 0.2361 0.2868 0.0064  0.0064  0.0186  413 PHE B CE1 
7545 C CE2 . PHE B 413 ? 0.2487 0.2954 0.3515 0.0182  0.0073  0.0143  413 PHE B CE2 
7546 C CZ  . PHE B 413 ? 0.1991 0.2426 0.2963 0.0079  0.0083  0.0136  413 PHE B CZ  
7547 N N   . LEU B 414 ? 0.2535 0.2272 0.3073 0.0412  -0.0016 0.0650  414 LEU B N   
7548 C CA  . LEU B 414 ? 0.2889 0.2547 0.3296 0.0479  -0.0056 0.0784  414 LEU B CA  
7549 C C   . LEU B 414 ? 0.3150 0.2795 0.3424 0.0369  -0.0023 0.0863  414 LEU B C   
7550 O O   . LEU B 414 ? 0.3560 0.3210 0.3702 0.0410  -0.0054 0.0972  414 LEU B O   
7551 C CB  . LEU B 414 ? 0.3719 0.3065 0.4077 0.0562  -0.0059 0.0856  414 LEU B CB  
7552 C CG  . LEU B 414 ? 0.4689 0.4069 0.5166 0.0726  -0.0098 0.0794  414 LEU B CG  
7553 C CD1 . LEU B 414 ? 0.5118 0.4172 0.5515 0.0853  -0.0119 0.0884  414 LEU B CD1 
7554 C CD2 . LEU B 414 ? 0.4311 0.4033 0.4860 0.0814  -0.0167 0.0775  414 LEU B CD2 
7555 N N   . LYS B 415 ? 0.3050 0.2697 0.3351 0.0238  0.0039  0.0815  415 LYS B N   
7556 C CA  . LYS B 415 ? 0.2873 0.2571 0.3073 0.0143  0.0080  0.0877  415 LYS B CA  
7557 C C   . LYS B 415 ? 0.2831 0.2795 0.3007 0.0159  0.0059  0.0833  415 LYS B C   
7558 O O   . LYS B 415 ? 0.2790 0.2826 0.2856 0.0113  0.0090  0.0887  415 LYS B O   
7559 C CB  . LYS B 415 ? 0.3438 0.3094 0.3698 0.0011  0.0146  0.0835  415 LYS B CB  
7560 C CG  . LYS B 415 ? 0.4493 0.4217 0.4677 -0.0093 0.0203  0.0903  415 LYS B CG  
7561 C CD  . LYS B 415 ? 0.5320 0.4918 0.5335 -0.0093 0.0210  0.1062  415 LYS B CD  
7562 C CE  . LYS B 415 ? 0.6249 0.5524 0.6229 -0.0149 0.0226  0.1143  415 LYS B CE  
7563 N NZ  . LYS B 415 ? 0.6965 0.6112 0.6764 -0.0200 0.0254  0.1316  415 LYS B NZ  
7564 N N   . TRP B 416 ? 0.2318 0.2429 0.2584 0.0215  0.0011  0.0733  416 TRP B N   
7565 C CA  . TRP B 416 ? 0.2256 0.2584 0.2497 0.0214  -0.0014 0.0668  416 TRP B CA  
7566 C C   . TRP B 416 ? 0.2520 0.2986 0.2758 0.0306  -0.0100 0.0656  416 TRP B C   
7567 O O   . TRP B 416 ? 0.2428 0.3060 0.2610 0.0300  -0.0132 0.0606  416 TRP B O   
7568 C CB  . TRP B 416 ? 0.1920 0.2316 0.2273 0.0152  0.0011  0.0540  416 TRP B CB  
7569 C CG  . TRP B 416 ? 0.2158 0.2471 0.2535 0.0072  0.0080  0.0543  416 TRP B CG  
7570 C CD1 . TRP B 416 ? 0.2291 0.2675 0.2624 0.0024  0.0126  0.0536  416 TRP B CD1 
7571 C CD2 . TRP B 416 ? 0.2242 0.2413 0.2698 0.0035  0.0108  0.0543  416 TRP B CD2 
7572 N NE1 . TRP B 416 ? 0.1955 0.2276 0.2354 -0.0045 0.0175  0.0541  416 TRP B NE1 
7573 C CE2 . TRP B 416 ? 0.2235 0.2414 0.2698 -0.0047 0.0161  0.0543  416 TRP B CE2 
7574 C CE3 . TRP B 416 ? 0.2350 0.2402 0.2868 0.0067  0.0093  0.0534  416 TRP B CE3 
7575 C CZ2 . TRP B 416 ? 0.2237 0.2312 0.2764 -0.0113 0.0188  0.0536  416 TRP B CZ2 
7576 C CZ3 . TRP B 416 ? 0.2325 0.2244 0.2885 0.0006  0.0128  0.0519  416 TRP B CZ3 
7577 C CH2 . TRP B 416 ? 0.2113 0.2043 0.2674 -0.0089 0.0169  0.0521  416 TRP B CH2 
7578 N N   . ILE B 417 ? 0.2088 0.2501 0.2384 0.0396  -0.0143 0.0693  417 ILE B N   
7579 C CA  . ILE B 417 ? 0.2561 0.3159 0.2891 0.0491  -0.0234 0.0678  417 ILE B CA  
7580 C C   . ILE B 417 ? 0.2378 0.2854 0.2719 0.0621  -0.0270 0.0772  417 ILE B C   
7581 O O   . ILE B 417 ? 0.3361 0.3603 0.3722 0.0623  -0.0220 0.0803  417 ILE B O   
7582 C CB  . ILE B 417 ? 0.2684 0.3462 0.3185 0.0454  -0.0246 0.0533  417 ILE B CB  
7583 C CG1 . ILE B 417 ? 0.2306 0.3350 0.2840 0.0508  -0.0343 0.0498  417 ILE B CG1 
7584 C CG2 . ILE B 417 ? 0.3500 0.4187 0.4151 0.0471  -0.0206 0.0497  417 ILE B CG2 
7585 C CD1 . ILE B 417 ? 0.2625 0.3844 0.3272 0.0415  -0.0350 0.0359  417 ILE B CD1 
7586 N N   . GLY B 418 ? 0.2991 0.3620 0.3310 0.0736  -0.0364 0.0815  418 GLY B N   
7587 C CA  . GLY B 418 ? 0.3917 0.4463 0.4275 0.0896  -0.0414 0.0890  418 GLY B CA  
7588 C C   . GLY B 418 ? 0.4578 0.4974 0.4733 0.0992  -0.0466 0.1066  418 GLY B C   
7589 O O   . GLY B 418 ? 0.6811 0.7162 0.6992 0.1159  -0.0531 0.1133  418 GLY B O   
7590 N N   . ASN B 419 ? 0.4289 0.4607 0.4240 0.0903  -0.0436 0.1150  419 ASN B N   
7591 C CA  . ASN B 419 ? 0.5127 0.5350 0.4855 0.0986  -0.0494 0.1328  419 ASN B CA  
7592 C C   . ASN B 419 ? 0.4775 0.5305 0.4387 0.0974  -0.0562 0.1314  419 ASN B C   
7593 O O   . ASN B 419 ? 0.4240 0.5006 0.3937 0.0887  -0.0554 0.1164  419 ASN B O   
7594 C CB  . ASN B 419 ? 0.6096 0.5972 0.5645 0.0895  -0.0405 0.1463  419 ASN B CB  
7595 C CG  . ASN B 419 ? 0.6195 0.6158 0.5635 0.0722  -0.0321 0.1444  419 ASN B CG  
7596 O OD1 . ASN B 419 ? 0.6917 0.7159 0.6380 0.0680  -0.0331 0.1332  419 ASN B OD1 
7597 N ND2 . ASN B 419 ? 0.6018 0.5734 0.5338 0.0622  -0.0234 0.1551  419 ASN B ND2 
7598 N N   . LYS B 420 ? 0.4975 0.5480 0.4370 0.1061  -0.0633 0.1472  420 LYS B N   
7599 C CA  . LYS B 420 ? 0.4539 0.5354 0.3809 0.1069  -0.0719 0.1453  420 LYS B CA  
7600 C C   . LYS B 420 ? 0.4709 0.5607 0.3870 0.0900  -0.0632 0.1370  420 LYS B C   
7601 O O   . LYS B 420 ? 0.3754 0.4925 0.2942 0.0858  -0.0672 0.1228  420 LYS B O   
7602 C CB  . LYS B 420 ? 0.5229 0.5980 0.4245 0.1195  -0.0810 0.1660  420 LYS B CB  
7603 C CG  . LYS B 420 ? 0.5877 0.6950 0.4768 0.1201  -0.0913 0.1611  420 LYS B CG  
7604 C CD  . LYS B 420 ? 0.7898 0.8840 0.6550 0.1269  -0.0985 0.1761  420 LYS B CD  
7605 C CE  . LYS B 420 ? 0.8611 0.9884 0.7154 0.1274  -0.1096 0.1694  420 LYS B CE  
7606 N NZ  . LYS B 420 ? 0.8749 1.0364 0.7569 0.1303  -0.1179 0.1510  420 LYS B NZ  
7607 N N   . GLU B 421 ? 0.4476 0.5149 0.3522 0.0800  -0.0513 0.1447  421 GLU B N   
7608 C CA  . GLU B 421 ? 0.4400 0.5186 0.3337 0.0669  -0.0430 0.1375  421 GLU B CA  
7609 C C   . GLU B 421 ? 0.3849 0.4716 0.3012 0.0582  -0.0374 0.1171  421 GLU B C   
7610 O O   . GLU B 421 ? 0.3735 0.4795 0.2874 0.0533  -0.0375 0.1037  421 GLU B O   
7611 C CB  . GLU B 421 ? 0.5440 0.6017 0.4200 0.0583  -0.0316 0.1523  421 GLU B CB  
7612 C CG  . GLU B 421 ? 0.6136 0.6672 0.4589 0.0632  -0.0356 0.1725  421 GLU B CG  
7613 C CD  . GLU B 421 ? 0.7430 0.7676 0.5855 0.0738  -0.0413 0.1907  421 GLU B CD  
7614 O OE1 . GLU B 421 ? 0.6430 0.6512 0.5080 0.0769  -0.0410 0.1861  421 GLU B OE1 
7615 O OE2 . GLU B 421 ? 0.8476 0.8624 0.6664 0.0779  -0.0459 0.2055  421 GLU B OE2 
7616 N N   . LYS B 422 ? 0.3796 0.4499 0.3162 0.0564  -0.0327 0.1143  422 LYS B N   
7617 C CA  . LYS B 422 ? 0.3807 0.4575 0.3369 0.0489  -0.0283 0.0968  422 LYS B CA  
7618 C C   . LYS B 422 ? 0.3723 0.4723 0.3396 0.0522  -0.0375 0.0832  422 LYS B C   
7619 O O   . LYS B 422 ? 0.3532 0.4639 0.3248 0.0448  -0.0357 0.0690  422 LYS B O   
7620 C CB  . LYS B 422 ? 0.3695 0.4253 0.3428 0.0470  -0.0227 0.0971  422 LYS B CB  
7621 C CG  . LYS B 422 ? 0.4718 0.5070 0.4367 0.0387  -0.0127 0.1071  422 LYS B CG  
7622 C CD  . LYS B 422 ? 0.4366 0.4496 0.4157 0.0358  -0.0082 0.1068  422 LYS B CD  
7623 C CE  . LYS B 422 ? 0.3475 0.3407 0.3168 0.0260  0.0002  0.1183  422 LYS B CE  
7624 N NZ  . LYS B 422 ? 0.3054 0.3120 0.2749 0.0138  0.0088  0.1128  422 LYS B NZ  
7625 N N   . ASN B 423 ? 0.2997 0.4081 0.2714 0.0633  -0.0477 0.0875  423 ASN B N   
7626 C CA  . ASN B 423 ? 0.2888 0.4240 0.2726 0.0648  -0.0570 0.0749  423 ASN B CA  
7627 C C   . ASN B 423 ? 0.3829 0.5372 0.3496 0.0604  -0.0620 0.0686  423 ASN B C   
7628 O O   . ASN B 423 ? 0.3713 0.5433 0.3465 0.0545  -0.0663 0.0536  423 ASN B O   
7629 C CB  . ASN B 423 ? 0.3333 0.4784 0.3265 0.0794  -0.0674 0.0815  423 ASN B CB  
7630 C CG  . ASN B 423 ? 0.3932 0.5258 0.4083 0.0838  -0.0629 0.0805  423 ASN B CG  
7631 O OD1 . ASN B 423 ? 0.3379 0.4560 0.3608 0.0745  -0.0531 0.0744  423 ASN B OD1 
7632 N ND2 . ASN B 423 ? 0.3317 0.4708 0.3560 0.0990  -0.0705 0.0860  423 ASN B ND2 
7633 N N   . GLU B 424 ? 0.3538 0.5041 0.2948 0.0623  -0.0613 0.0795  424 GLU B N   
7634 C CA  . GLU B 424 ? 0.3688 0.5372 0.2907 0.0585  -0.0655 0.0720  424 GLU B CA  
7635 C C   . GLU B 424 ? 0.2922 0.4582 0.2163 0.0468  -0.0568 0.0556  424 GLU B C   
7636 O O   . GLU B 424 ? 0.3261 0.5071 0.2460 0.0422  -0.0618 0.0410  424 GLU B O   
7637 C CB  . GLU B 424 ? 0.4604 0.6257 0.3521 0.0626  -0.0651 0.0879  424 GLU B CB  
7638 C CG  . GLU B 424 ? 0.5957 0.7794 0.4632 0.0586  -0.0677 0.0793  424 GLU B CG  
7639 C CD  . GLU B 424 ? 0.7618 0.9726 0.6274 0.0626  -0.0841 0.0713  424 GLU B CD  
7640 O OE1 . GLU B 424 ? 0.7382 0.9571 0.6207 0.0705  -0.0941 0.0755  424 GLU B OE1 
7641 O OE2 . GLU B 424 ? 0.7943 1.0201 0.6416 0.0580  -0.0872 0.0600  424 GLU B OE2 
7642 N N   . TYR B 425 ? 0.2793 0.4260 0.2098 0.0421  -0.0443 0.0575  425 TYR B N   
7643 C CA  . TYR B 425 ? 0.3242 0.4677 0.2594 0.0336  -0.0368 0.0425  425 TYR B CA  
7644 C C   . TYR B 425 ? 0.2995 0.4474 0.2546 0.0294  -0.0418 0.0279  425 TYR B C   
7645 O O   . TYR B 425 ? 0.2742 0.4261 0.2261 0.0238  -0.0427 0.0130  425 TYR B O   
7646 C CB  . TYR B 425 ? 0.2752 0.4008 0.2169 0.0301  -0.0241 0.0480  425 TYR B CB  
7647 C CG  . TYR B 425 ? 0.2816 0.4078 0.2043 0.0282  -0.0150 0.0528  425 TYR B CG  
7648 C CD1 . TYR B 425 ? 0.3327 0.4689 0.2310 0.0314  -0.0174 0.0604  425 TYR B CD1 
7649 C CD2 . TYR B 425 ? 0.2686 0.3882 0.1983 0.0233  -0.0038 0.0499  425 TYR B CD2 
7650 C CE1 . TYR B 425 ? 0.4219 0.5618 0.3027 0.0287  -0.0074 0.0650  425 TYR B CE1 
7651 C CE2 . TYR B 425 ? 0.2910 0.4165 0.2061 0.0214  0.0056  0.0538  425 TYR B CE2 
7652 C CZ  . TYR B 425 ? 0.3424 0.4781 0.2330 0.0236  0.0045  0.0611  425 TYR B CZ  
7653 O OH  . TYR B 425 ? 0.3596 0.5040 0.2357 0.0209  0.0152  0.0650  425 TYR B OH  
7654 N N   . TRP B 426 ? 0.2631 0.4094 0.2378 0.0319  -0.0446 0.0317  426 TRP B N   
7655 C CA  . TRP B 426 ? 0.2840 0.4376 0.2776 0.0263  -0.0485 0.0192  426 TRP B CA  
7656 C C   . TRP B 426 ? 0.2815 0.4579 0.2706 0.0244  -0.0601 0.0099  426 TRP B C   
7657 O O   . TRP B 426 ? 0.2789 0.4580 0.2720 0.0149  -0.0616 -0.0046 426 TRP B O   
7658 C CB  . TRP B 426 ? 0.2196 0.3712 0.2340 0.0305  -0.0484 0.0250  426 TRP B CB  
7659 C CG  . TRP B 426 ? 0.1927 0.3213 0.2137 0.0282  -0.0374 0.0286  426 TRP B CG  
7660 C CD1 . TRP B 426 ? 0.2463 0.3595 0.2640 0.0332  -0.0324 0.0411  426 TRP B CD1 
7661 C CD2 . TRP B 426 ? 0.1769 0.2959 0.2072 0.0195  -0.0311 0.0196  426 TRP B CD2 
7662 N NE1 . TRP B 426 ? 0.2326 0.3300 0.2582 0.0276  -0.0237 0.0392  426 TRP B NE1 
7663 C CE2 . TRP B 426 ? 0.2501 0.3513 0.2831 0.0202  -0.0231 0.0266  426 TRP B CE2 
7664 C CE3 . TRP B 426 ? 0.1943 0.3164 0.2300 0.0108  -0.0321 0.0067  426 TRP B CE3 
7665 C CZ2 . TRP B 426 ? 0.3066 0.3964 0.3473 0.0137  -0.0167 0.0214  426 TRP B CZ2 
7666 C CZ3 . TRP B 426 ? 0.2737 0.3805 0.3158 0.0048  -0.0252 0.0028  426 TRP B CZ3 
7667 C CH2 . TRP B 426 ? 0.2924 0.3850 0.3371 0.0070  -0.0179 0.0102  426 TRP B CH2 
7668 N N   . LYS B 427 ? 0.2559 0.4478 0.2353 0.0329  -0.0689 0.0184  427 LYS B N   
7669 C CA  . LYS B 427 ? 0.2606 0.4779 0.2340 0.0310  -0.0814 0.0097  427 LYS B CA  
7670 C C   . LYS B 427 ? 0.2898 0.5039 0.2433 0.0227  -0.0800 -0.0036 427 LYS B C   
7671 O O   . LYS B 427 ? 0.3114 0.5370 0.2666 0.0139  -0.0868 -0.0187 427 LYS B O   
7672 C CB  . LYS B 427 ? 0.2915 0.5240 0.2528 0.0435  -0.0911 0.0234  427 LYS B CB  
7673 C CG  . LYS B 427 ? 0.4735 0.7126 0.4548 0.0546  -0.0955 0.0342  427 LYS B CG  
7674 C CD  . LYS B 427 ? 0.5868 0.8394 0.5538 0.0687  -0.1068 0.0483  427 LYS B CD  
7675 C CE  . LYS B 427 ? 0.6912 0.9168 0.6486 0.0792  -0.1001 0.0682  427 LYS B CE  
7676 N NZ  . LYS B 427 ? 0.7701 0.9995 0.7422 0.0952  -0.1070 0.0794  427 LYS B NZ  
7677 N N   . ILE B 428 ? 0.3043 0.5036 0.2385 0.0251  -0.0709 0.0014  428 ILE B N   
7678 C CA  . ILE B 428 ? 0.3239 0.5192 0.2387 0.0198  -0.0674 -0.0119 428 ILE B CA  
7679 C C   . ILE B 428 ? 0.3004 0.4809 0.2286 0.0105  -0.0628 -0.0274 428 ILE B C   
7680 O O   . ILE B 428 ? 0.3493 0.5302 0.2693 0.0036  -0.0666 -0.0441 428 ILE B O   
7681 C CB  . ILE B 428 ? 0.3766 0.5621 0.2726 0.0249  -0.0564 -0.0019 428 ILE B CB  
7682 C CG1 . ILE B 428 ? 0.4334 0.6331 0.3071 0.0321  -0.0621 0.0115  428 ILE B CG1 
7683 C CG2 . ILE B 428 ? 0.3307 0.5086 0.2135 0.0212  -0.0486 -0.0170 428 ILE B CG2 
7684 C CD1 . ILE B 428 ? 0.4326 0.6222 0.2923 0.0356  -0.0502 0.0269  428 ILE B CD1 
7685 N N   . LEU B 429 ? 0.2799 0.4451 0.2270 0.0100  -0.0548 -0.0219 429 LEU B N   
7686 C CA  . LEU B 429 ? 0.2845 0.4335 0.2434 0.0021  -0.0505 -0.0335 429 LEU B CA  
7687 C C   . LEU B 429 ? 0.3468 0.5046 0.3178 -0.0076 -0.0597 -0.0441 429 LEU B C   
7688 O O   . LEU B 429 ? 0.3154 0.4620 0.2836 -0.0165 -0.0602 -0.0585 429 LEU B O   
7689 C CB  . LEU B 429 ? 0.2963 0.4310 0.2720 0.0038  -0.0416 -0.0237 429 LEU B CB  
7690 C CG  . LEU B 429 ? 0.3045 0.4214 0.2914 -0.0034 -0.0373 -0.0325 429 LEU B CG  
7691 C CD1 . LEU B 429 ? 0.3341 0.4365 0.3069 -0.0026 -0.0318 -0.0419 429 LEU B CD1 
7692 C CD2 . LEU B 429 ? 0.2439 0.3522 0.2469 -0.0017 -0.0309 -0.0220 429 LEU B CD2 
7693 N N   . ILE B 430 ? 0.2415 0.4189 0.2266 -0.0061 -0.0667 -0.0371 430 ILE B N   
7694 C CA  . ILE B 430 ? 0.2621 0.4553 0.2623 -0.0163 -0.0751 -0.0463 430 ILE B CA  
7695 C C   . ILE B 430 ? 0.3194 0.5234 0.3041 -0.0237 -0.0847 -0.0607 430 ILE B C   
7696 O O   . ILE B 430 ? 0.3429 0.5434 0.3320 -0.0376 -0.0877 -0.0745 430 ILE B O   
7697 C CB  . ILE B 430 ? 0.2518 0.4699 0.2701 -0.0095 -0.0809 -0.0357 430 ILE B CB  
7698 C CG1 . ILE B 430 ? 0.2684 0.4741 0.3039 -0.0052 -0.0715 -0.0260 430 ILE B CG1 
7699 C CG2 . ILE B 430 ? 0.3243 0.5698 0.3566 -0.0194 -0.0915 -0.0456 430 ILE B CG2 
7700 C CD1 . ILE B 430 ? 0.2823 0.5019 0.3264 0.0085  -0.0744 -0.0125 430 ILE B CD1 
7701 N N   . GLU B 431 ? 0.3133 0.5296 0.2779 -0.0156 -0.0898 -0.0576 431 GLU B N   
7702 C CA  . GLU B 431 ? 0.4496 0.6775 0.3960 -0.0221 -0.0997 -0.0722 431 GLU B CA  
7703 C C   . GLU B 431 ? 0.3719 0.5722 0.3019 -0.0286 -0.0932 -0.0876 431 GLU B C   
7704 O O   . GLU B 431 ? 0.4402 0.6391 0.3640 -0.0405 -0.0998 -0.1049 431 GLU B O   
7705 C CB  . GLU B 431 ? 0.5113 0.7580 0.4366 -0.0107 -0.1059 -0.0635 431 GLU B CB  
7706 C CG  . GLU B 431 ? 0.6132 0.8918 0.5515 -0.0050 -0.1180 -0.0533 431 GLU B CG  
7707 C CD  . GLU B 431 ? 0.7446 1.0487 0.6951 -0.0177 -0.1313 -0.0679 431 GLU B CD  
7708 O OE1 . GLU B 431 ? 0.7736 1.0710 0.7086 -0.0281 -0.1342 -0.0835 431 GLU B OE1 
7709 O OE2 . GLU B 431 ? 0.8012 1.1221 0.7784 -0.0172 -0.1349 -0.0622 431 GLU B OE2 
7710 N N   . ALA B 432 ? 0.3536 0.5317 0.2768 -0.0207 -0.0805 -0.0820 432 ALA B N   
7711 C CA  . ALA B 432 ? 0.4068 0.5589 0.3163 -0.0232 -0.0738 -0.0963 432 ALA B CA  
7712 C C   . ALA B 432 ? 0.4150 0.5454 0.3405 -0.0347 -0.0724 -0.1048 432 ALA B C   
7713 O O   . ALA B 432 ? 0.5032 0.6141 0.4177 -0.0417 -0.0733 -0.1215 432 ALA B O   
7714 C CB  . ALA B 432 ? 0.3806 0.5207 0.2827 -0.0112 -0.0607 -0.0872 432 ALA B CB  
7715 N N   . LYS B 433 ? 0.3356 0.4673 0.2852 -0.0367 -0.0700 -0.0936 433 LYS B N   
7716 C CA  . LYS B 433 ? 0.3562 0.4679 0.3194 -0.0485 -0.0680 -0.0993 433 LYS B CA  
7717 C C   . LYS B 433 ? 0.3906 0.5087 0.3543 -0.0653 -0.0785 -0.1139 433 LYS B C   
7718 O O   . LYS B 433 ? 0.4261 0.5182 0.3873 -0.0766 -0.0777 -0.1249 433 LYS B O   
7719 C CB  . LYS B 433 ? 0.2858 0.4026 0.2728 -0.0473 -0.0633 -0.0845 433 LYS B CB  
7720 C CG  . LYS B 433 ? 0.3580 0.4580 0.3589 -0.0603 -0.0609 -0.0877 433 LYS B CG  
7721 C CD  . LYS B 433 ? 0.3607 0.4232 0.3515 -0.0595 -0.0536 -0.0923 433 LYS B CD  
7722 C CE  . LYS B 433 ? 0.3989 0.4436 0.4001 -0.0740 -0.0524 -0.0940 433 LYS B CE  
7723 N NZ  . LYS B 433 ? 0.4297 0.4348 0.4194 -0.0734 -0.0475 -0.0988 433 LYS B NZ  
7724 N N   . LYS B 434 ? 0.4353 0.5869 0.4008 -0.0673 -0.0891 -0.1143 434 LYS B N   
7725 C CA  . LYS B 434 ? 0.4826 0.6455 0.4490 -0.0848 -0.1003 -0.1292 434 LYS B CA  
7726 C C   . LYS B 434 ? 0.5204 0.6582 0.4608 -0.0909 -0.1024 -0.1486 434 LYS B C   
7727 O O   . LYS B 434 ? 0.5379 0.6663 0.4788 -0.1075 -0.1080 -0.1604 434 LYS B O   
7728 C CB  . LYS B 434 ? 0.4795 0.6870 0.4506 -0.0826 -0.1125 -0.1260 434 LYS B CB  
7729 C CG  . LYS B 434 ? 0.4349 0.6687 0.4323 -0.0755 -0.1120 -0.1091 434 LYS B CG  
7730 C CD  . LYS B 434 ? 0.5794 0.8497 0.5895 -0.0787 -0.1235 -0.1082 434 LYS B CD  
7731 C CE  . LYS B 434 ? 0.6512 0.9492 0.6814 -0.0645 -0.1240 -0.0915 434 LYS B CE  
7732 N NZ  . LYS B 434 ? 0.7161 1.0279 0.7300 -0.0465 -0.1296 -0.0818 434 LYS B NZ  
7733 N N   . LYS B 435 ? 0.4708 0.5944 0.3891 -0.0766 -0.0965 -0.1498 435 LYS B N   
7734 C CA  . LYS B 435 ? 0.5269 0.6286 0.4182 -0.0787 -0.0978 -0.1694 435 LYS B CA  
7735 C C   . LYS B 435 ? 0.5934 0.6573 0.4757 -0.0683 -0.0850 -0.1711 435 LYS B C   
7736 O O   . LYS B 435 ? 0.5820 0.6321 0.4401 -0.0615 -0.0828 -0.1842 435 LYS B O   
7737 C CB  . LYS B 435 ? 0.5881 0.7151 0.4565 -0.0703 -0.1038 -0.1731 435 LYS B CB  
7738 C CG  . LYS B 435 ? 0.6456 0.8128 0.5244 -0.0712 -0.1145 -0.1617 435 LYS B CG  
7739 C CD  . LYS B 435 ? 0.6468 0.8322 0.5011 -0.0580 -0.1165 -0.1578 435 LYS B CD  
7740 C CE  . LYS B 435 ? 0.6662 0.8836 0.5247 -0.0602 -0.1293 -0.1514 435 LYS B CE  
7741 N NZ  . LYS B 435 ? 0.7743 1.0030 0.6041 -0.0499 -0.1316 -0.1496 435 LYS B NZ  
7742 N N   . ALA B 436 ? 0.3913 0.5328 0.4467 -0.0871 -0.0882 -0.1103 436 ALA B N   
7743 C CA  . ALA B 436 ? 0.3889 0.4913 0.4318 -0.0781 -0.0797 -0.1080 436 ALA B CA  
7744 C C   . ALA B 436 ? 0.4227 0.4896 0.4703 -0.0916 -0.0772 -0.1183 436 ALA B C   
7745 O O   . ALA B 436 ? 0.5064 0.5720 0.5705 -0.1088 -0.0772 -0.1175 436 ALA B O   
7746 C CB  . ALA B 436 ? 0.3327 0.4304 0.3785 -0.0677 -0.0712 -0.0882 436 ALA B CB  
7747 N N   . LYS B 437 ? 0.4605 0.4981 0.4947 -0.0836 -0.0744 -0.1277 437 LYS B N   
7748 C CA  . LYS B 437 ? 0.4639 0.4611 0.5019 -0.0922 -0.0720 -0.1387 437 LYS B CA  
7749 C C   . LYS B 437 ? 0.4533 0.4155 0.4903 -0.0794 -0.0638 -0.1271 437 LYS B C   
7750 O O   . LYS B 437 ? 0.5119 0.4364 0.5555 -0.0853 -0.0615 -0.1305 437 LYS B O   
7751 C CB  . LYS B 437 ? 0.4710 0.4620 0.4963 -0.0936 -0.0762 -0.1654 437 LYS B CB  
7752 C CG  . LYS B 437 ? 0.6007 0.6155 0.6277 -0.1115 -0.0857 -0.1788 437 LYS B CG  
7753 C CD  . LYS B 437 ? 0.6603 0.7205 0.6767 -0.1030 -0.0914 -0.1711 437 LYS B CD  
7754 C CE  . LYS B 437 ? 0.6367 0.7180 0.6499 -0.1139 -0.1006 -0.1784 437 LYS B CE  
7755 N NZ  . LYS B 437 ? 0.4935 0.6147 0.4966 -0.1031 -0.1064 -0.1682 437 LYS B NZ  
7756 N N   . ASN B 438 ? 0.3684 0.3414 0.3982 -0.0624 -0.0602 -0.1135 438 ASN B N   
7757 C CA  . ASN B 438 ? 0.3714 0.3178 0.4003 -0.0489 -0.0544 -0.1039 438 ASN B CA  
7758 C C   . ASN B 438 ? 0.3575 0.3236 0.3833 -0.0388 -0.0519 -0.0844 438 ASN B C   
7759 O O   . ASN B 438 ? 0.3474 0.3434 0.3715 -0.0405 -0.0538 -0.0799 438 ASN B O   
7760 C CB  . ASN B 438 ? 0.3797 0.3139 0.4002 -0.0360 -0.0525 -0.1202 438 ASN B CB  
7761 C CG  . ASN B 438 ? 0.4342 0.4014 0.4406 -0.0281 -0.0533 -0.1260 438 ASN B CG  
7762 O OD1 . ASN B 438 ? 0.4199 0.4038 0.4223 -0.0184 -0.0512 -0.1121 438 ASN B OD1 
7763 N ND2 . ASN B 438 ? 0.4237 0.3992 0.4207 -0.0332 -0.0564 -0.1466 438 ASN B ND2 
7764 N N   . ASP B 439 ? 0.3556 0.3048 0.3812 -0.0275 -0.0483 -0.0738 439 ASP B N   
7765 C CA  . ASP B 439 ? 0.3320 0.2952 0.3547 -0.0205 -0.0464 -0.0562 439 ASP B CA  
7766 C C   . ASP B 439 ? 0.3219 0.3077 0.3356 -0.0093 -0.0460 -0.0582 439 ASP B C   
7767 O O   . ASP B 439 ? 0.3303 0.3249 0.3412 -0.0036 -0.0446 -0.0462 439 ASP B O   
7768 C CB  . ASP B 439 ? 0.4003 0.3396 0.4261 -0.0139 -0.0448 -0.0432 439 ASP B CB  
7769 C CG  . ASP B 439 ? 0.4427 0.3626 0.4745 -0.0267 -0.0443 -0.0322 439 ASP B CG  
7770 O OD1 . ASP B 439 ? 0.4840 0.4121 0.5199 -0.0418 -0.0443 -0.0353 439 ASP B OD1 
7771 O OD2 . ASP B 439 ? 0.5113 0.4092 0.5444 -0.0220 -0.0442 -0.0190 439 ASP B OD2 
7772 N N   . TYR B 440 ? 0.2886 0.2840 0.2960 -0.0073 -0.0471 -0.0727 440 TYR B N   
7773 C CA  . TYR B 440 ? 0.2763 0.2943 0.2742 0.0000  -0.0465 -0.0705 440 TYR B CA  
7774 C C   . TYR B 440 ? 0.2812 0.3194 0.2782 -0.0044 -0.0492 -0.0621 440 TYR B C   
7775 O O   . TYR B 440 ? 0.3130 0.3637 0.3040 0.0015  -0.0484 -0.0552 440 TYR B O   
7776 C CB  . TYR B 440 ? 0.2748 0.3004 0.2627 0.0026  -0.0463 -0.0863 440 TYR B CB  
7777 C CG  . TYR B 440 ? 0.3304 0.3473 0.3184 0.0135  -0.0406 -0.0920 440 TYR B CG  
7778 C CD1 . TYR B 440 ? 0.4012 0.4297 0.3878 0.0218  -0.0369 -0.0826 440 TYR B CD1 
7779 C CD2 . TYR B 440 ? 0.3672 0.3647 0.3591 0.0155  -0.0387 -0.1075 440 TYR B CD2 
7780 C CE1 . TYR B 440 ? 0.4375 0.4645 0.4284 0.0320  -0.0313 -0.0877 440 TYR B CE1 
7781 C CE2 . TYR B 440 ? 0.4773 0.4699 0.4728 0.0282  -0.0327 -0.1136 440 TYR B CE2 
7782 C CZ  . TYR B 440 ? 0.4739 0.4843 0.4700 0.0365  -0.0290 -0.1030 440 TYR B CZ  
7783 O OH  . TYR B 440 ? 0.5094 0.5219 0.5132 0.0493  -0.0227 -0.1089 440 TYR B OH  
7784 N N   . ILE B 441 ? 0.2566 0.2980 0.2618 -0.0147 -0.0518 -0.0623 441 ILE B N   
7785 C CA  . ILE B 441 ? 0.3137 0.3755 0.3227 -0.0162 -0.0529 -0.0538 441 ILE B CA  
7786 C C   . ILE B 441 ? 0.2465 0.3039 0.2551 -0.0109 -0.0481 -0.0409 441 ILE B C   
7787 O O   . ILE B 441 ? 0.2402 0.3105 0.2468 -0.0057 -0.0475 -0.0354 441 ILE B O   
7788 C CB  . ILE B 441 ? 0.3275 0.3987 0.3494 -0.0293 -0.0555 -0.0570 441 ILE B CB  
7789 C CG1 . ILE B 441 ? 0.2401 0.3414 0.2681 -0.0276 -0.0581 -0.0527 441 ILE B CG1 
7790 C CG2 . ILE B 441 ? 0.2850 0.3397 0.3152 -0.0374 -0.0506 -0.0494 441 ILE B CG2 
7791 C CD1 . ILE B 441 ? 0.3011 0.4197 0.3205 -0.0210 -0.0650 -0.0572 441 ILE B CD1 
7792 N N   . LEU B 442 ? 0.2029 0.2411 0.2124 -0.0113 -0.0452 -0.0363 442 LEU B N   
7793 C CA  . LEU B 442 ? 0.2278 0.2641 0.2338 -0.0073 -0.0420 -0.0250 442 LEU B CA  
7794 C C   . LEU B 442 ? 0.2148 0.2543 0.2132 0.0024  -0.0420 -0.0244 442 LEU B C   
7795 O O   . LEU B 442 ? 0.2283 0.2740 0.2227 0.0050  -0.0405 -0.0189 442 LEU B O   
7796 C CB  . LEU B 442 ? 0.2216 0.2381 0.2294 -0.0098 -0.0409 -0.0180 442 LEU B CB  
7797 C CG  . LEU B 442 ? 0.2701 0.2778 0.2855 -0.0222 -0.0400 -0.0160 442 LEU B CG  
7798 C CD1 . LEU B 442 ? 0.3044 0.2864 0.3195 -0.0219 -0.0400 -0.0063 442 LEU B CD1 
7799 C CD2 . LEU B 442 ? 0.2294 0.2569 0.2473 -0.0299 -0.0363 -0.0104 442 LEU B CD2 
7800 N N   . VAL B 443 ? 0.2338 0.2697 0.2304 0.0068  -0.0428 -0.0313 443 VAL B N   
7801 C CA  . VAL B 443 ? 0.2748 0.3174 0.2657 0.0134  -0.0417 -0.0304 443 VAL B CA  
7802 C C   . VAL B 443 ? 0.2628 0.3179 0.2482 0.0135  -0.0423 -0.0284 443 VAL B C   
7803 O O   . VAL B 443 ? 0.2273 0.2843 0.2093 0.0156  -0.0410 -0.0228 443 VAL B O   
7804 C CB  . VAL B 443 ? 0.2322 0.2738 0.2222 0.0177  -0.0405 -0.0396 443 VAL B CB  
7805 C CG1 . VAL B 443 ? 0.2521 0.3044 0.2381 0.0223  -0.0378 -0.0370 443 VAL B CG1 
7806 C CG2 . VAL B 443 ? 0.2125 0.2376 0.2108 0.0203  -0.0401 -0.0423 443 VAL B CG2 
7807 N N   . ALA B 444 ? 0.2312 0.2945 0.2164 0.0111  -0.0451 -0.0330 444 ALA B N   
7808 C CA  . ALA B 444 ? 0.2107 0.2859 0.1922 0.0135  -0.0473 -0.0294 444 ALA B CA  
7809 C C   . ALA B 444 ? 0.2504 0.3271 0.2374 0.0147  -0.0460 -0.0233 444 ALA B C   
7810 O O   . ALA B 444 ? 0.2589 0.3407 0.2445 0.0196  -0.0471 -0.0192 444 ALA B O   
7811 C CB  . ALA B 444 ? 0.2149 0.3030 0.1967 0.0106  -0.0527 -0.0357 444 ALA B CB  
7812 N N   . GLU B 445 ? 0.2311 0.3032 0.2236 0.0110  -0.0432 -0.0224 445 GLU B N   
7813 C CA  . GLU B 445 ? 0.2464 0.3222 0.2421 0.0120  -0.0400 -0.0188 445 GLU B CA  
7814 C C   . GLU B 445 ? 0.2184 0.2847 0.2062 0.0148  -0.0373 -0.0158 445 GLU B C   
7815 O O   . GLU B 445 ? 0.2404 0.3082 0.2278 0.0160  -0.0339 -0.0155 445 GLU B O   
7816 C CB  . GLU B 445 ? 0.2907 0.3690 0.2932 0.0044  -0.0373 -0.0183 445 GLU B CB  
7817 C CG  . GLU B 445 ? 0.1939 0.2869 0.2079 -0.0004 -0.0398 -0.0222 445 GLU B CG  
7818 C CD  . GLU B 445 ? 0.2704 0.3617 0.2918 -0.0121 -0.0376 -0.0215 445 GLU B CD  
7819 O OE1 . GLU B 445 ? 0.2840 0.3631 0.3003 -0.0151 -0.0337 -0.0155 445 GLU B OE1 
7820 O OE2 . GLU B 445 ? 0.2204 0.3234 0.2525 -0.0192 -0.0404 -0.0261 445 GLU B OE2 
7821 N N   . GLY B 446 ? 0.2315 0.2904 0.2138 0.0153  -0.0384 -0.0151 446 GLY B N   
7822 C CA  . GLY B 446 ? 0.2178 0.2708 0.1946 0.0154  -0.0372 -0.0131 446 GLY B CA  
7823 C C   . GLY B 446 ? 0.2310 0.2807 0.2049 0.0185  -0.0361 -0.0130 446 GLY B C   
7824 O O   . GLY B 446 ? 0.2193 0.2706 0.1943 0.0223  -0.0375 -0.0117 446 GLY B O   
7825 N N   . SER B 447 ? 0.2469 0.2906 0.2164 0.0170  -0.0343 -0.0144 447 SER B N   
7826 C CA  . SER B 447 ? 0.2652 0.2999 0.2330 0.0205  -0.0326 -0.0162 447 SER B CA  
7827 C C   . SER B 447 ? 0.2212 0.2469 0.1866 0.0197  -0.0342 -0.0119 447 SER B C   
7828 O O   . SER B 447 ? 0.2417 0.2576 0.2072 0.0245  -0.0340 -0.0097 447 SER B O   
7829 C CB  . SER B 447 ? 0.2621 0.2913 0.2237 0.0177  -0.0298 -0.0222 447 SER B CB  
7830 O OG  . SER B 447 ? 0.2502 0.2771 0.2065 0.0103  -0.0323 -0.0221 447 SER B OG  
7831 N N   . ASP B 448 ? 0.2282 0.2579 0.1925 0.0143  -0.0353 -0.0096 448 ASP B N   
7832 C CA  . ASP B 448 ? 0.2001 0.2238 0.1618 0.0104  -0.0349 -0.0050 448 ASP B CA  
7833 C C   . ASP B 448 ? 0.2390 0.2612 0.1980 0.0152  -0.0355 0.0017  448 ASP B C   
7834 O O   . ASP B 448 ? 0.2679 0.2772 0.2232 0.0140  -0.0350 0.0079  448 ASP B O   
7835 C CB  . ASP B 448 ? 0.2173 0.2534 0.1818 0.0051  -0.0347 -0.0046 448 ASP B CB  
7836 C CG  . ASP B 448 ? 0.2150 0.2556 0.1822 0.0015  -0.0365 -0.0087 448 ASP B CG  
7837 O OD1 . ASP B 448 ? 0.2381 0.2839 0.2067 0.0052  -0.0379 -0.0103 448 ASP B OD1 
7838 O OD2 . ASP B 448 ? 0.2522 0.2909 0.2194 -0.0059 -0.0370 -0.0097 448 ASP B OD2 
7839 N N   . TRP B 449 ? 0.2358 0.2706 0.1959 0.0197  -0.0375 0.0012  449 TRP B N   
7840 C CA  . TRP B 449 ? 0.1846 0.2230 0.1398 0.0238  -0.0400 0.0077  449 TRP B CA  
7841 C C   . TRP B 449 ? 0.2712 0.2973 0.2277 0.0309  -0.0419 0.0132  449 TRP B C   
7842 O O   . TRP B 449 ? 0.2460 0.2639 0.1960 0.0326  -0.0433 0.0234  449 TRP B O   
7843 C CB  . TRP B 449 ? 0.2706 0.3254 0.2277 0.0260  -0.0431 0.0029  449 TRP B CB  
7844 C CG  . TRP B 449 ? 0.2133 0.2735 0.1733 0.0217  -0.0409 -0.0047 449 TRP B CG  
7845 C CD1 . TRP B 449 ? 0.2781 0.3406 0.2455 0.0212  -0.0414 -0.0108 449 TRP B CD1 
7846 C CD2 . TRP B 449 ? 0.2230 0.2865 0.1805 0.0181  -0.0375 -0.0058 449 TRP B CD2 
7847 N NE1 . TRP B 449 ? 0.2161 0.2789 0.1852 0.0189  -0.0396 -0.0148 449 TRP B NE1 
7848 C CE2 . TRP B 449 ? 0.2040 0.2696 0.1684 0.0180  -0.0371 -0.0129 449 TRP B CE2 
7849 C CE3 . TRP B 449 ? 0.2272 0.2932 0.1783 0.0149  -0.0342 -0.0007 449 TRP B CE3 
7850 C CZ2 . TRP B 449 ? 0.1632 0.2342 0.1307 0.0177  -0.0340 -0.0162 449 TRP B CZ2 
7851 C CZ3 . TRP B 449 ? 0.2414 0.3171 0.1957 0.0126  -0.0299 -0.0048 449 TRP B CZ3 
7852 C CH2 . TRP B 449 ? 0.2388 0.3173 0.2022 0.0155  -0.0302 -0.0130 449 TRP B CH2 
7853 N N   . PHE B 450 ? 0.2599 0.2842 0.2246 0.0357  -0.0413 0.0070  450 PHE B N   
7854 C CA  . PHE B 450 ? 0.3149 0.3293 0.2849 0.0458  -0.0421 0.0094  450 PHE B CA  
7855 C C   . PHE B 450 ? 0.2588 0.2457 0.2248 0.0441  -0.0392 0.0111  450 PHE B C   
7856 O O   . PHE B 450 ? 0.2934 0.2640 0.2607 0.0525  -0.0406 0.0178  450 PHE B O   
7857 C CB  . PHE B 450 ? 0.2933 0.3193 0.2743 0.0506  -0.0400 0.0001  450 PHE B CB  
7858 C CG  . PHE B 450 ? 0.2300 0.2804 0.2164 0.0486  -0.0426 -0.0021 450 PHE B CG  
7859 C CD1 . PHE B 450 ? 0.2267 0.2940 0.2215 0.0558  -0.0480 0.0012  450 PHE B CD1 
7860 C CD2 . PHE B 450 ? 0.2701 0.3262 0.2542 0.0391  -0.0408 -0.0069 450 PHE B CD2 
7861 C CE1 . PHE B 450 ? 0.2177 0.3068 0.2180 0.0511  -0.0511 -0.0024 450 PHE B CE1 
7862 C CE2 . PHE B 450 ? 0.2464 0.3192 0.2357 0.0358  -0.0432 -0.0094 450 PHE B CE2 
7863 C CZ  . PHE B 450 ? 0.2064 0.2958 0.2038 0.0405  -0.0481 -0.0082 450 PHE B CZ  
7864 N N   . TRP B 451 ? 0.2412 0.2220 0.2033 0.0334  -0.0358 0.0051  451 TRP B N   
7865 C CA  . TRP B 451 ? 0.2480 0.2032 0.2063 0.0277  -0.0335 0.0048  451 TRP B CA  
7866 C C   . TRP B 451 ? 0.3229 0.2646 0.2759 0.0249  -0.0348 0.0194  451 TRP B C   
7867 O O   . TRP B 451 ? 0.2954 0.2098 0.2479 0.0280  -0.0346 0.0243  451 TRP B O   
7868 C CB  . TRP B 451 ? 0.2633 0.2238 0.2193 0.0147  -0.0319 -0.0033 451 TRP B CB  
7869 C CG  . TRP B 451 ? 0.2972 0.2367 0.2501 0.0036  -0.0306 -0.0042 451 TRP B CG  
7870 C CD1 . TRP B 451 ? 0.2956 0.2311 0.2469 -0.0068 -0.0302 0.0051  451 TRP B CD1 
7871 C CD2 . TRP B 451 ? 0.3285 0.2497 0.2796 -0.0004 -0.0292 -0.0164 451 TRP B CD2 
7872 N NE1 . TRP B 451 ? 0.3562 0.2709 0.3069 -0.0182 -0.0292 0.0005  451 TRP B NE1 
7873 C CE2 . TRP B 451 ? 0.4104 0.3148 0.3602 -0.0144 -0.0291 -0.0139 451 TRP B CE2 
7874 C CE3 . TRP B 451 ? 0.4727 0.3919 0.4224 0.0053  -0.0273 -0.0302 451 TRP B CE3 
7875 C CZ2 . TRP B 451 ? 0.4274 0.3102 0.3747 -0.0233 -0.0284 -0.0262 451 TRP B CZ2 
7876 C CZ3 . TRP B 451 ? 0.5322 0.4309 0.4769 -0.0019 -0.0259 -0.0431 451 TRP B CZ3 
7877 C CH2 . TRP B 451 ? 0.5455 0.4252 0.4892 -0.0164 -0.0272 -0.0418 451 TRP B CH2 
7878 N N   . TRP B 452 ? 0.2815 0.2410 0.2296 0.0193  -0.0355 0.0266  452 TRP B N   
7879 C CA  . TRP B 452 ? 0.3049 0.2567 0.2447 0.0140  -0.0351 0.0416  452 TRP B CA  
7880 C C   . TRP B 452 ? 0.2910 0.2414 0.2261 0.0258  -0.0400 0.0545  452 TRP B C   
7881 O O   . TRP B 452 ? 0.3184 0.2532 0.2452 0.0235  -0.0404 0.0702  452 TRP B O   
7882 C CB  . TRP B 452 ? 0.2991 0.2754 0.2348 0.0041  -0.0323 0.0423  452 TRP B CB  
7883 C CG  . TRP B 452 ? 0.2711 0.2520 0.2135 -0.0067 -0.0291 0.0326  452 TRP B CG  
7884 C CD1 . TRP B 452 ? 0.2427 0.2436 0.1913 -0.0064 -0.0293 0.0217  452 TRP B CD1 
7885 C CD2 . TRP B 452 ? 0.2738 0.2392 0.2185 -0.0194 -0.0265 0.0332  452 TRP B CD2 
7886 N NE1 . TRP B 452 ? 0.2365 0.2391 0.1910 -0.0168 -0.0279 0.0166  452 TRP B NE1 
7887 C CE2 . TRP B 452 ? 0.2573 0.2396 0.2099 -0.0261 -0.0262 0.0221  452 TRP B CE2 
7888 C CE3 . TRP B 452 ? 0.3049 0.2424 0.2462 -0.0267 -0.0250 0.0424  452 TRP B CE3 
7889 C CZ2 . TRP B 452 ? 0.2889 0.2666 0.2466 -0.0404 -0.0253 0.0186  452 TRP B CZ2 
7890 C CZ3 . TRP B 452 ? 0.3231 0.2515 0.2694 -0.0425 -0.0229 0.0381  452 TRP B CZ3 
7891 C CH2 . TRP B 452 ? 0.3166 0.2675 0.2713 -0.0497 -0.0235 0.0256  452 TRP B CH2 
7892 N N   . GLN B 453 ? 0.3351 0.3031 0.2756 0.0373  -0.0444 0.0497  453 GLN B N   
7893 C CA  . GLN B 453 ? 0.3550 0.3288 0.2925 0.0487  -0.0513 0.0619  453 GLN B CA  
7894 C C   . GLN B 453 ? 0.3501 0.2940 0.2918 0.0591  -0.0532 0.0716  453 GLN B C   
7895 O O   . GLN B 453 ? 0.3936 0.3180 0.3451 0.0624  -0.0497 0.0619  453 GLN B O   
7896 C CB  . GLN B 453 ? 0.3113 0.3126 0.2582 0.0570  -0.0558 0.0526  453 GLN B CB  
7897 C CG  . GLN B 453 ? 0.4192 0.4302 0.3704 0.0716  -0.0648 0.0623  453 GLN B CG  
7898 C CD  . GLN B 453 ? 0.5150 0.5372 0.4490 0.0700  -0.0711 0.0775  453 GLN B CD  
7899 O OE1 . GLN B 453 ? 0.4284 0.4493 0.3468 0.0581  -0.0668 0.0811  453 GLN B OE1 
7900 N NE2 . GLN B 453 ? 0.4402 0.4775 0.3770 0.0823  -0.0813 0.0865  453 GLN B NE2 
7901 N N   . GLY B 454 ? 0.4628 0.4017 0.3956 0.0646  -0.0589 0.0909  454 GLY B N   
7902 C CA  . GLY B 454 ? 0.5938 0.5047 0.5327 0.0791  -0.0628 0.1025  454 GLY B CA  
7903 C C   . GLY B 454 ? 0.7318 0.6002 0.6726 0.0727  -0.0559 0.1003  454 GLY B C   
7904 O O   . GLY B 454 ? 0.7193 0.5658 0.6732 0.0839  -0.0546 0.0917  454 GLY B O   
7905 N N   . GLU B 455 ? 0.7392 0.5982 0.6678 0.0536  -0.0508 0.1055  455 GLU B N   
7906 C CA  . GLU B 455 ? 0.7962 0.6143 0.7244 0.0428  -0.0454 0.1070  455 GLU B CA  
7907 C C   . GLU B 455 ? 0.9018 0.7034 0.8150 0.0341  -0.0458 0.1335  455 GLU B C   
7908 O O   . GLU B 455 ? 0.7993 0.6240 0.7004 0.0373  -0.0502 0.1491  455 GLU B O   
7909 C CB  . GLU B 455 ? 0.7043 0.5306 0.6350 0.0246  -0.0384 0.0882  455 GLU B CB  
7910 C CG  . GLU B 455 ? 0.5973 0.4429 0.5388 0.0313  -0.0377 0.0647  455 GLU B CG  
7911 C CD  . GLU B 455 ? 0.6759 0.4910 0.6265 0.0395  -0.0359 0.0513  455 GLU B CD  
7912 O OE1 . GLU B 455 ? 0.5947 0.4246 0.5538 0.0517  -0.0357 0.0372  455 GLU B OE1 
7913 O OE2 . GLU B 455 ? 0.7513 0.5273 0.7005 0.0330  -0.0339 0.0542  455 GLU B OE2 
7914 N N   . GLU B 456 ? 0.9802 0.7412 0.8929 0.0218  -0.0413 0.1387  456 GLU B N   
7915 C CA  . GLU B 456 ? 0.9657 0.7133 0.8635 0.0063  -0.0388 0.1635  456 GLU B CA  
7916 C C   . GLU B 456 ? 0.9186 0.7120 0.8064 -0.0092 -0.0340 0.1630  456 GLU B C   
7917 O O   . GLU B 456 ? 0.8956 0.7160 0.7914 -0.0153 -0.0305 0.1415  456 GLU B O   
7918 C CB  . GLU B 456 ? 1.0618 0.7628 0.9639 -0.0109 -0.0330 0.1631  456 GLU B CB  
7919 C CG  . GLU B 456 ? 1.1435 0.7900 1.0424 -0.0043 -0.0360 0.1859  456 GLU B CG  
7920 C CD  . GLU B 456 ? 1.1765 0.7772 1.0774 -0.0279 -0.0294 0.1875  456 GLU B CD  
7921 O OE1 . GLU B 456 ? 1.1672 0.7374 1.0809 -0.0274 -0.0282 0.1657  456 GLU B OE1 
7922 O OE2 . GLU B 456 ? 1.1572 0.7536 1.0465 -0.0481 -0.0251 0.2098  456 GLU B OE2 
7923 N N   . LYS B 457 ? 0.8433 0.6463 0.7130 -0.0145 -0.0337 0.1869  457 LYS B N   
7924 C CA  . LYS B 457 ? 0.8208 0.6671 0.6805 -0.0287 -0.0272 0.1853  457 LYS B CA  
7925 C C   . LYS B 457 ? 0.9063 0.7473 0.7729 -0.0536 -0.0167 0.1807  457 LYS B C   
7926 O O   . LYS B 457 ? 0.9758 0.7785 0.8429 -0.0658 -0.0139 0.1935  457 LYS B O   
7927 C CB  . LYS B 457 ? 0.7455 0.6067 0.5805 -0.0283 -0.0288 0.2112  457 LYS B CB  
7928 C CG  . LYS B 457 ? 0.8420 0.6893 0.6632 -0.0499 -0.0200 0.2350  457 LYS B CG  
7929 C CD  . LYS B 457 ? 0.8556 0.7342 0.6500 -0.0508 -0.0185 0.2522  457 LYS B CD  
7930 C CE  . LYS B 457 ? 0.8891 0.7472 0.6718 -0.0658 -0.0090 0.2727  457 LYS B CE  
7931 N NZ  . LYS B 457 ? 0.9522 0.8296 0.7081 -0.0595 -0.0095 0.2861  457 LYS B NZ  
7932 N N   . ALA B 458 ? 0.8124 0.6912 0.6869 -0.0607 -0.0116 0.1617  458 ALA B N   
7933 C CA  . ALA B 458 ? 0.7050 0.5914 0.5902 -0.0831 -0.0028 0.1550  458 ALA B CA  
7934 C C   . ALA B 458 ? 0.6491 0.5878 0.5317 -0.0881 0.0042  0.1497  458 ALA B C   
7935 O O   . ALA B 458 ? 0.5886 0.5524 0.4640 -0.0731 0.0010  0.1435  458 ALA B O   
7936 C CB  . ALA B 458 ? 0.6678 0.5430 0.5728 -0.0834 -0.0056 0.1311  458 ALA B CB  
7937 N N   . PRO B 459 ? 0.7031 0.6597 0.5925 -0.1090 0.0141  0.1511  459 PRO B N   
7938 C CA  . PRO B 459 ? 0.6543 0.6624 0.5432 -0.1118 0.0225  0.1452  459 PRO B CA  
7939 C C   . PRO B 459 ? 0.5109 0.5441 0.4130 -0.0969 0.0184  0.1199  459 PRO B C   
7940 O O   . PRO B 459 ? 0.4592 0.4826 0.3784 -0.0954 0.0132  0.1053  459 PRO B O   
7941 C CB  . PRO B 459 ? 0.7041 0.7251 0.6064 -0.1374 0.0332  0.1492  459 PRO B CB  
7942 C CG  . PRO B 459 ? 0.7467 0.7236 0.6603 -0.1475 0.0278  0.1491  459 PRO B CG  
7943 C CD  . PRO B 459 ? 0.7844 0.7163 0.6825 -0.1320 0.0188  0.1594  459 PRO B CD  
7944 N N   . PHE B 460 ? 0.5119 0.5766 0.4042 -0.0865 0.0208  0.1151  460 PHE B N   
7945 C CA  . PHE B 460 ? 0.4682 0.5578 0.3700 -0.0726 0.0185  0.0935  460 PHE B CA  
7946 C C   . PHE B 460 ? 0.4430 0.5119 0.3436 -0.0554 0.0064  0.0855  460 PHE B C   
7947 O O   . PHE B 460 ? 0.3930 0.4783 0.2981 -0.0441 0.0040  0.0701  460 PHE B O   
7948 C CB  . PHE B 460 ? 0.3843 0.4933 0.3121 -0.0785 0.0216  0.0786  460 PHE B CB  
7949 C CG  . PHE B 460 ? 0.4900 0.6310 0.4254 -0.0942 0.0344  0.0831  460 PHE B CG  
7950 C CD1 . PHE B 460 ? 0.5193 0.6984 0.4510 -0.0896 0.0438  0.0775  460 PHE B CD1 
7951 C CD2 . PHE B 460 ? 0.4015 0.5360 0.3487 -0.1143 0.0377  0.0912  460 PHE B CD2 
7952 C CE1 . PHE B 460 ? 0.5108 0.7248 0.4514 -0.1033 0.0575  0.0808  460 PHE B CE1 
7953 C CE2 . PHE B 460 ? 0.5302 0.6993 0.4875 -0.1304 0.0503  0.0957  460 PHE B CE2 
7954 C CZ  . PHE B 460 ? 0.5787 0.7897 0.5332 -0.1243 0.0609  0.0909  460 PHE B CZ  
7955 N N   . VAL B 461 ? 0.5143 0.5480 0.4102 -0.0526 -0.0006 0.0953  461 VAL B N   
7956 C CA  . VAL B 461 ? 0.5943 0.6138 0.4933 -0.0365 -0.0105 0.0866  461 VAL B CA  
7957 C C   . VAL B 461 ? 0.5460 0.5834 0.4321 -0.0242 -0.0146 0.0855  461 VAL B C   
7958 O O   . VAL B 461 ? 0.5754 0.6162 0.4680 -0.0130 -0.0207 0.0728  461 VAL B O   
7959 C CB  . VAL B 461 ? 0.7420 0.7214 0.6407 -0.0344 -0.0158 0.0967  461 VAL B CB  
7960 C CG1 . VAL B 461 ? 0.7011 0.6711 0.6076 -0.0183 -0.0238 0.0850  461 VAL B CG1 
7961 C CG2 . VAL B 461 ? 0.7426 0.7034 0.6520 -0.0501 -0.0115 0.0960  461 VAL B CG2 
7962 N N   . GLU B 462 ? 0.4022 0.4531 0.2692 -0.0278 -0.0113 0.0982  462 GLU B N   
7963 C CA  . GLU B 462 ? 0.4796 0.5527 0.3316 -0.0190 -0.0151 0.0945  462 GLU B CA  
7964 C C   . GLU B 462 ? 0.3972 0.4946 0.2584 -0.0155 -0.0123 0.0712  462 GLU B C   
7965 O O   . GLU B 462 ? 0.4049 0.5136 0.2604 -0.0071 -0.0181 0.0618  462 GLU B O   
7966 C CB  . GLU B 462 ? 0.5873 0.6748 0.4139 -0.0265 -0.0098 0.1114  462 GLU B CB  
7967 C CG  . GLU B 462 ? 0.8252 0.9294 0.6530 -0.0419 0.0049  0.1126  462 GLU B CG  
7968 C CD  . GLU B 462 ? 0.9294 1.0094 0.7590 -0.0560 0.0093  0.1332  462 GLU B CD  
7969 O OE1 . GLU B 462 ? 0.9485 1.0407 0.7635 -0.0691 0.0190  0.1485  462 GLU B OE1 
7970 O OE2 . GLU B 462 ? 0.8847 0.9335 0.7300 -0.0552 0.0039  0.1334  462 GLU B OE2 
7971 N N   . VAL B 463 ? 0.2985 0.4037 0.1753 -0.0217 -0.0044 0.0620  463 VAL B N   
7972 C CA  . VAL B 463 ? 0.2771 0.4021 0.1642 -0.0165 -0.0017 0.0418  463 VAL B CA  
7973 C C   . VAL B 463 ? 0.2872 0.3986 0.1877 -0.0072 -0.0106 0.0305  463 VAL B C   
7974 O O   . VAL B 463 ? 0.2914 0.4121 0.1939 -0.0005 -0.0123 0.0164  463 VAL B O   
7975 C CB  . VAL B 463 ? 0.2959 0.4371 0.1984 -0.0242 0.0085  0.0374  463 VAL B CB  
7976 C CG1 . VAL B 463 ? 0.3154 0.4726 0.2322 -0.0156 0.0102  0.0176  463 VAL B CG1 
7977 C CG2 . VAL B 463 ? 0.3392 0.4999 0.2281 -0.0345 0.0195  0.0480  463 VAL B CG2 
7978 N N   . PHE B 464 ? 0.2569 0.3453 0.1656 -0.0072 -0.0158 0.0361  464 PHE B N   
7979 C CA  . PHE B 464 ? 0.2251 0.3035 0.1445 0.0007  -0.0227 0.0268  464 PHE B CA  
7980 C C   . PHE B 464 ? 0.2594 0.3409 0.1703 0.0086  -0.0297 0.0256  464 PHE B C   
7981 O O   . PHE B 464 ? 0.2510 0.3367 0.1689 0.0132  -0.0330 0.0140  464 PHE B O   
7982 C CB  . PHE B 464 ? 0.2261 0.2815 0.1534 -0.0008 -0.0253 0.0313  464 PHE B CB  
7983 C CG  . PHE B 464 ? 0.2349 0.2901 0.1732 -0.0096 -0.0211 0.0284  464 PHE B CG  
7984 C CD1 . PHE B 464 ? 0.2766 0.3360 0.2272 -0.0075 -0.0228 0.0174  464 PHE B CD1 
7985 C CD2 . PHE B 464 ? 0.3219 0.3740 0.2584 -0.0208 -0.0162 0.0378  464 PHE B CD2 
7986 C CE1 . PHE B 464 ? 0.2005 0.2648 0.1615 -0.0156 -0.0210 0.0150  464 PHE B CE1 
7987 C CE2 . PHE B 464 ? 0.2317 0.2882 0.1805 -0.0308 -0.0135 0.0343  464 PHE B CE2 
7988 C CZ  . PHE B 464 ? 0.2116 0.2759 0.1729 -0.0275 -0.0167 0.0224  464 PHE B CZ  
7989 N N   . ASP B 465 ? 0.3472 0.4278 0.2433 0.0093  -0.0326 0.0387  465 ASP B N   
7990 C CA  . ASP B 465 ? 0.2510 0.3409 0.1392 0.0161  -0.0410 0.0383  465 ASP B CA  
7991 C C   . ASP B 465 ? 0.2924 0.4046 0.1723 0.0148  -0.0397 0.0247  465 ASP B C   
7992 O O   . ASP B 465 ? 0.2711 0.3902 0.1549 0.0183  -0.0459 0.0138  465 ASP B O   
7993 C CB  . ASP B 465 ? 0.2789 0.3646 0.1515 0.0178  -0.0454 0.0582  465 ASP B CB  
7994 C CG  . ASP B 465 ? 0.3486 0.4507 0.2121 0.0247  -0.0560 0.0591  465 ASP B CG  
7995 O OD1 . ASP B 465 ? 0.3395 0.4381 0.2159 0.0331  -0.0640 0.0588  465 ASP B OD1 
7996 O OD2 . ASP B 465 ? 0.3398 0.4617 0.1837 0.0213  -0.0563 0.0592  465 ASP B OD2 
7997 N N   . LYS B 466 ? 0.2600 0.3841 0.1289 0.0091  -0.0310 0.0239  466 LYS B N   
7998 C CA  . LYS B 466 ? 0.3557 0.4992 0.2169 0.0089  -0.0279 0.0073  466 LYS B CA  
7999 C C   . LYS B 466 ? 0.2937 0.4318 0.1747 0.0121  -0.0274 -0.0109 466 LYS B C   
8000 O O   . LYS B 466 ? 0.3065 0.4499 0.1857 0.0139  -0.0310 -0.0254 466 LYS B O   
8001 C CB  . LYS B 466 ? 0.2952 0.4546 0.1445 0.0031  -0.0158 0.0089  466 LYS B CB  
8002 C CG  . LYS B 466 ? 0.3680 0.5459 0.2128 0.0047  -0.0094 -0.0122 466 LYS B CG  
8003 C CD  . LYS B 466 ? 0.5496 0.7505 0.3725 -0.0009 0.0012  -0.0079 466 LYS B CD  
8004 C CE  . LYS B 466 ? 0.7340 0.9521 0.5531 0.0020  0.0092  -0.0318 466 LYS B CE  
8005 N NZ  . LYS B 466 ? 0.8108 1.0422 0.6450 0.0026  0.0237  -0.0381 466 LYS B NZ  
8006 N N   . LEU B 467 ? 0.2512 0.3780 0.1503 0.0121  -0.0236 -0.0097 467 LEU B N   
8007 C CA  . LEU B 467 ? 0.2224 0.3418 0.1392 0.0156  -0.0243 -0.0225 467 LEU B CA  
8008 C C   . LEU B 467 ? 0.2271 0.3368 0.1488 0.0176  -0.0334 -0.0248 467 LEU B C   
8009 O O   . LEU B 467 ? 0.2628 0.3722 0.1884 0.0184  -0.0355 -0.0375 467 LEU B O   
8010 C CB  . LEU B 467 ? 0.1957 0.3079 0.1282 0.0145  -0.0208 -0.0178 467 LEU B CB  
8011 C CG  . LEU B 467 ? 0.2184 0.3461 0.1550 0.0131  -0.0114 -0.0203 467 LEU B CG  
8012 C CD1 . LEU B 467 ? 0.1893 0.3140 0.1405 0.0093  -0.0103 -0.0132 467 LEU B CD1 
8013 C CD2 . LEU B 467 ? 0.2224 0.3568 0.1662 0.0199  -0.0082 -0.0366 467 LEU B CD2 
8014 N N   . PHE B 468 ? 0.2066 0.3085 0.1299 0.0181  -0.0381 -0.0132 468 PHE B N   
8015 C CA  . PHE B 468 ? 0.2535 0.3522 0.1847 0.0202  -0.0453 -0.0150 468 PHE B CA  
8016 C C   . PHE B 468 ? 0.2609 0.3734 0.1847 0.0194  -0.0512 -0.0229 468 PHE B C   
8017 O O   . PHE B 468 ? 0.2162 0.3291 0.1491 0.0175  -0.0543 -0.0331 468 PHE B O   
8018 C CB  . PHE B 468 ? 0.2446 0.3362 0.1774 0.0235  -0.0485 -0.0020 468 PHE B CB  
8019 C CG  . PHE B 468 ? 0.2906 0.3865 0.2330 0.0272  -0.0552 -0.0032 468 PHE B CG  
8020 C CD1 . PHE B 468 ? 0.2242 0.3155 0.1808 0.0264  -0.0538 -0.0092 468 PHE B CD1 
8021 C CD2 . PHE B 468 ? 0.2916 0.3997 0.2292 0.0313  -0.0629 0.0028  468 PHE B CD2 
8022 C CE1 . PHE B 468 ? 0.2636 0.3640 0.2314 0.0287  -0.0582 -0.0103 468 PHE B CE1 
8023 C CE2 . PHE B 468 ? 0.2399 0.3582 0.1908 0.0352  -0.0690 0.0016  468 PHE B CE2 
8024 C CZ  . PHE B 468 ? 0.2510 0.3662 0.2181 0.0334  -0.0656 -0.0057 468 PHE B CZ  
8025 N N   . ARG B 469 ? 0.2631 0.3879 0.1696 0.0193  -0.0532 -0.0180 469 ARG B N   
8026 C CA  . ARG B 469 ? 0.2857 0.4271 0.1829 0.0176  -0.0608 -0.0261 469 ARG B CA  
8027 C C   . ARG B 469 ? 0.3091 0.4529 0.2030 0.0136  -0.0567 -0.0461 469 ARG B C   
8028 O O   . ARG B 469 ? 0.2897 0.4394 0.1847 0.0097  -0.0626 -0.0589 469 ARG B O   
8029 C CB  . ARG B 469 ? 0.3133 0.4667 0.1906 0.0186  -0.0645 -0.0132 469 ARG B CB  
8030 C CG  . ARG B 469 ? 0.4021 0.5510 0.2848 0.0250  -0.0710 0.0055  469 ARG B CG  
8031 C CD  . ARG B 469 ? 0.4368 0.5904 0.3013 0.0258  -0.0743 0.0206  469 ARG B CD  
8032 N NE  . ARG B 469 ? 0.3709 0.5158 0.2413 0.0342  -0.0806 0.0393  469 ARG B NE  
8033 C CZ  . ARG B 469 ? 0.3599 0.5121 0.2387 0.0399  -0.0908 0.0436  469 ARG B CZ  
8034 N NH1 . ARG B 469 ? 0.3338 0.5033 0.2154 0.0358  -0.0962 0.0308  469 ARG B NH1 
8035 N NH2 . ARG B 469 ? 0.4485 0.5907 0.3344 0.0501  -0.0955 0.0602  469 ARG B NH2 
8036 N N   . SER B 470 ? 0.2867 0.4252 0.1793 0.0144  -0.0463 -0.0499 470 SER B N   
8037 C CA  . SER B 470 ? 0.3602 0.4960 0.2549 0.0139  -0.0412 -0.0698 470 SER B CA  
8038 C C   . SER B 470 ? 0.2353 0.3535 0.1501 0.0131  -0.0442 -0.0772 470 SER B C   
8039 O O   . SER B 470 ? 0.3694 0.4837 0.2852 0.0097  -0.0466 -0.0936 470 SER B O   
8040 C CB  . SER B 470 ? 0.5114 0.6479 0.4074 0.0174  -0.0293 -0.0704 470 SER B CB  
8041 O OG  . SER B 470 ? 0.6207 0.7759 0.4961 0.0157  -0.0247 -0.0655 470 SER B OG  
8042 N N   . PHE B 471 ? 0.2159 0.3225 0.1457 0.0148  -0.0439 -0.0654 471 PHE B N   
8043 C CA  . PHE B 471 ? 0.2530 0.3441 0.1996 0.0130  -0.0458 -0.0690 471 PHE B CA  
8044 C C   . PHE B 471 ? 0.2955 0.3923 0.2450 0.0065  -0.0542 -0.0721 471 PHE B C   
8045 O O   . PHE B 471 ? 0.2872 0.3746 0.2448 0.0009  -0.0558 -0.0827 471 PHE B O   
8046 C CB  . PHE B 471 ? 0.2204 0.3023 0.1777 0.0156  -0.0436 -0.0556 471 PHE B CB  
8047 C CG  . PHE B 471 ? 0.2601 0.3397 0.2192 0.0205  -0.0368 -0.0535 471 PHE B CG  
8048 C CD1 . PHE B 471 ? 0.2918 0.3671 0.2552 0.0242  -0.0325 -0.0646 471 PHE B CD1 
8049 C CD2 . PHE B 471 ? 0.2592 0.3420 0.2178 0.0212  -0.0348 -0.0414 471 PHE B CD2 
8050 C CE1 . PHE B 471 ? 0.2542 0.3336 0.2239 0.0298  -0.0266 -0.0626 471 PHE B CE1 
8051 C CE2 . PHE B 471 ? 0.2260 0.3120 0.1893 0.0237  -0.0293 -0.0399 471 PHE B CE2 
8052 C CZ  . PHE B 471 ? 0.2414 0.3287 0.2114 0.0285  -0.0253 -0.0501 471 PHE B CZ  
8053 N N   . VAL B 472 ? 0.2611 0.3735 0.2058 0.0071  -0.0597 -0.0625 472 VAL B N   
8054 C CA  . VAL B 472 ? 0.2836 0.4097 0.2343 0.0018  -0.0686 -0.0652 472 VAL B CA  
8055 C C   . VAL B 472 ? 0.3530 0.4873 0.2943 -0.0052 -0.0732 -0.0827 472 VAL B C   
8056 O O   . VAL B 472 ? 0.3152 0.4508 0.2669 -0.0141 -0.0780 -0.0927 472 VAL B O   
8057 C CB  . VAL B 472 ? 0.2807 0.4232 0.2287 0.0075  -0.0742 -0.0507 472 VAL B CB  
8058 C CG1 . VAL B 472 ? 0.3929 0.5574 0.3457 0.0032  -0.0846 -0.0539 472 VAL B CG1 
8059 C CG2 . VAL B 472 ? 0.2454 0.3779 0.2069 0.0127  -0.0701 -0.0385 472 VAL B CG2 
8060 N N   . ARG B 473 ? 0.3540 0.4942 0.2752 -0.0028 -0.0710 -0.0878 473 ARG B N   
8061 C CA  . ARG B 473 ? 0.2792 0.4216 0.1910 -0.0094 -0.0722 -0.1037 473 ARG B CA  
8062 C C   . ARG B 473 ? 0.3901 0.5122 0.3104 -0.0137 -0.0687 -0.1238 473 ARG B C   
8063 O O   . ARG B 473 ? 0.3897 0.5074 0.3143 -0.0232 -0.0729 -0.1364 473 ARG B O   
8064 C CB  . ARG B 473 ? 0.3513 0.5025 0.2404 -0.0057 -0.0673 -0.1025 473 ARG B CB  
8065 C CG  . ARG B 473 ? 0.5057 0.6585 0.3823 -0.0116 -0.0670 -0.1212 473 ARG B CG  
8066 C CD  . ARG B 473 ? 0.6522 0.8212 0.5049 -0.0097 -0.0647 -0.1155 473 ARG B CD  
8067 N NE  . ARG B 473 ? 0.8235 0.9907 0.6628 -0.0110 -0.0572 -0.1353 473 ARG B NE  
8068 C CZ  . ARG B 473 ? 0.8291 0.9980 0.6596 -0.0053 -0.0451 -0.1376 473 ARG B CZ  
8069 N NH1 . ARG B 473 ? 0.8533 1.0255 0.6866 0.0004  -0.0400 -0.1207 473 ARG B NH1 
8070 N NH2 . ARG B 473 ? 0.7645 0.9328 0.5847 -0.0054 -0.0377 -0.1571 473 ARG B NH2 
8071 N N   . ARG B 474 ? 0.3122 0.4163 0.2384 -0.0065 -0.0597 -0.1227 474 ARG B N   
8072 C CA  . ARG B 474 ? 0.3509 0.4287 0.2873 -0.0072 -0.0548 -0.1375 474 ARG B CA  
8073 C C   . ARG B 474 ? 0.3551 0.4166 0.3107 -0.0159 -0.0591 -0.1350 474 ARG B C   
8074 O O   . ARG B 474 ? 0.3986 0.4396 0.3605 -0.0223 -0.0593 -0.1500 474 ARG B O   
8075 C CB  . ARG B 474 ? 0.3905 0.4562 0.3325 0.0047  -0.0447 -0.1312 474 ARG B CB  
8076 C CG  . ARG B 474 ? 0.4449 0.4826 0.3988 0.0086  -0.0396 -0.1444 474 ARG B CG  
8077 C CD  . ARG B 474 ? 0.5256 0.5638 0.4676 0.0120  -0.0344 -0.1687 474 ARG B CD  
8078 N NE  . ARG B 474 ? 0.6230 0.6324 0.5796 0.0206  -0.0284 -0.1794 474 ARG B NE  
8079 C CZ  . ARG B 474 ? 0.7921 0.8019 0.7459 0.0318  -0.0192 -0.1957 474 ARG B CZ  
8080 N NH1 . ARG B 474 ? 0.8291 0.8686 0.7636 0.0334  -0.0141 -0.2028 474 ARG B NH1 
8081 N NH2 . ARG B 474 ? 0.8349 0.8164 0.8056 0.0422  -0.0146 -0.2042 474 ARG B NH2 
8082 N N   . ALA B 475 ? 0.2919 0.3618 0.2569 -0.0168 -0.0618 -0.1166 475 ALA B N   
8083 C CA  . ALA B 475 ? 0.3186 0.3786 0.3013 -0.0261 -0.0641 -0.1122 475 ALA B CA  
8084 C C   . ALA B 475 ? 0.3781 0.4480 0.3644 -0.0408 -0.0721 -0.1256 475 ALA B C   
8085 O O   . ALA B 475 ? 0.4041 0.4628 0.4058 -0.0522 -0.0729 -0.1259 475 ALA B O   
8086 C CB  . ALA B 475 ? 0.3245 0.3976 0.3146 -0.0231 -0.0640 -0.0924 475 ALA B CB  
8087 N N   . GLN B 476 ? 0.3549 0.4477 0.3271 -0.0423 -0.0785 -0.1358 476 GLN B N   
8088 C CA  . GLN B 476 ? 0.3783 0.4830 0.3537 -0.0565 -0.0868 -0.1465 476 GLN B CA  
8089 C C   . GLN B 476 ? 0.3667 0.4518 0.3309 -0.0617 -0.0851 -0.1671 476 GLN B C   
8090 O O   . GLN B 476 ? 0.4378 0.5281 0.4022 -0.0737 -0.0913 -0.1756 476 GLN B O   
8091 C CB  . GLN B 476 ? 0.3417 0.4795 0.3100 -0.0529 -0.0935 -0.1343 476 GLN B CB  
8092 C CG  . GLN B 476 ? 0.3810 0.5362 0.3638 -0.0472 -0.0949 -0.1152 476 GLN B CG  
8093 C CD  . GLN B 476 ? 0.4589 0.6372 0.4323 -0.0370 -0.0993 -0.1008 476 GLN B CD  
8094 O OE1 . GLN B 476 ? 0.4876 0.6876 0.4689 -0.0400 -0.1071 -0.0970 476 GLN B OE1 
8095 N NE2 . GLN B 476 ? 0.4015 0.5748 0.3595 -0.0251 -0.0946 -0.0921 476 GLN B NE2 
8096 N N   . GLU B 477 ? 0.4559 0.5194 0.4117 -0.0523 -0.0768 -0.1760 477 GLU B N   
8097 C CA  . GLU B 477 ? 0.5649 0.6110 0.5088 -0.0538 -0.0733 -0.1963 477 GLU B CA  
8098 C C   . GLU B 477 ? 0.6951 0.6991 0.6521 -0.0536 -0.0672 -0.2078 477 GLU B C   
8099 O O   . GLU B 477 ? 0.7226 0.7113 0.6983 -0.0553 -0.0673 -0.1993 477 GLU B O   
8100 C CB  . GLU B 477 ? 0.6401 0.7001 0.5622 -0.0408 -0.0671 -0.1976 477 GLU B CB  
8101 C CG  . GLU B 477 ? 0.8141 0.9097 0.7213 -0.0408 -0.0733 -0.1844 477 GLU B CG  
8102 C CD  . GLU B 477 ? 0.8488 0.9572 0.7347 -0.0303 -0.0659 -0.1830 477 GLU B CD  
8103 O OE1 . GLU B 477 ? 0.8382 0.9708 0.7088 -0.0309 -0.0706 -0.1738 477 GLU B OE1 
8104 O OE2 . GLU B 477 ? 0.8087 0.9035 0.6946 -0.0215 -0.0554 -0.1902 477 GLU B OE2 
# 
