data_9JLV
# 
_entry.id   9JLV 
# 
_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   9JLV         pdb_00009jlv 10.2210/pdb9jlv/pdb 
WWPDB D_1300051235 ?            ?                   
# 
_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                        9JLV 
_pdbx_database_status.recvd_initial_deposition_date   2024-09-19 
_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                 4 
_pdbx_contact_author.email              yufeng@sari.ac.cn 
_pdbx_contact_author.name_first         Feng 
_pdbx_contact_author.name_last          Yu 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-9502-3277 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Zhu, Z.M.'   1 ? 
'Wang, W.W.'  2 ? 
'Li, M.J.'    3 ? 
'Xu, Q.'      4 ? 
'Zhou, H.'    5 ? 
'Huang, L.Q.' 6 ? 
'Wang, Q.S.'  7 ? 
'Yu, F.'      8 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            J.Struct.Biol. 
_citation.journal_id_ASTM           JSBIEM 
_citation.journal_id_CSD            0803 
_citation.journal_id_ISSN           1095-8657 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            217 
_citation.language                  ? 
_citation.page_first                108199 
_citation.page_last                 108199 
_citation.title                     
'Mechanistic insights into cyclodextrins as substrates and inhibitors of GH57 family amylopullulanase from Aquifex aeolicus.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1016/j.jsb.2025.108199 
_citation.pdbx_database_id_PubMed   40120836 
_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 ? 
primary 'Li, M.'    2 ? 
primary 'Xu, Q.'    3 ? 
primary 'Huang, L.' 4 ? 
primary 'Zhou, H.'  5 ? 
primary 'Wang, W.'  6 ? 
primary 'Wang, Q.'  7 ? 
primary 'Yu, F.'    8 ? 
# 
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 1   ? E256Q ? ? 
2 branched    syn 'alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose' 
666.578   1   ? ?     ? ? 
3 branched    syn 'Cyclohexakis-(1-4)-(alpha-D-glucopyranose)'                                                                
990.860   1   ? ?     ? ? 
4 non-polymer syn 'CITRATE ANION'                                                                                             
189.100   2   ? ?     ? ? 
5 non-polymer syn GLYCEROL                                                                                                    
92.094    2   ? ?     ? ? 
6 water       nat water                                                                                                       
18.015    340 ? ?     ? ? 
# 
_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 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
4 'CITRATE ANION' FLC 
5 GLYCEROL        GOL 
6 water           HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   LYS n 
1 3   LYS n 
1 4   LEU n 
1 5   PHE n 
1 6   LEU n 
1 7   VAL n 
1 8   PHE n 
1 9   TRP n 
1 10  TRP n 
1 11  HIS n 
1 12  MET n 
1 13  HIS n 
1 14  GLN n 
1 15  PRO n 
1 16  LEU n 
1 17  TYR n 
1 18  ARG n 
1 19  GLU n 
1 20  PRO n 
1 21  TYR n 
1 22  THR n 
1 23  GLY n 
1 24  GLU n 
1 25  TYR n 
1 26  LEU n 
1 27  LEU n 
1 28  PRO n 
1 29  TRP n 
1 30  THR n 
1 31  PHE n 
1 32  PHE n 
1 33  HIS n 
1 34  ALA n 
1 35  VAL n 
1 36  LYS n 
1 37  ASP n 
1 38  TYR n 
1 39  TYR n 
1 40  ASP n 
1 41  MET n 
1 42  PRO n 
1 43  ALA n 
1 44  TYR n 
1 45  LEU n 
1 46  LYS n 
1 47  ASP n 
1 48  PHE n 
1 49  GLU n 
1 50  ILE n 
1 51  LYS n 
1 52  LEU n 
1 53  ASN n 
1 54  PHE n 
1 55  ASN n 
1 56  LEU n 
1 57  THR n 
1 58  PRO n 
1 59  VAL n 
1 60  LEU n 
1 61  ILE n 
1 62  ASP n 
1 63  GLN n 
1 64  ILE n 
1 65  GLN n 
1 66  GLU n 
1 67  TYR n 
1 68  ALA n 
1 69  GLN n 
1 70  GLY n 
1 71  LYS n 
1 72  ALA n 
1 73  LYS n 
1 74  ASP n 
1 75  VAL n 
1 76  PHE n 
1 77  LEU n 
1 78  GLU n 
1 79  ALA n 
1 80  ILE n 
1 81  ARG n 
1 82  LYS n 
1 83  ASP n 
1 84  PRO n 
1 85  ASP n 
1 86  ASP n 
1 87  LEU n 
1 88  GLU n 
1 89  LYS n 
1 90  GLU n 
1 91  GLU n 
1 92  VAL n 
1 93  GLU n 
1 94  LYS n 
1 95  LEU n 
1 96  ILE n 
1 97  GLU n 
1 98  PHE n 
1 99  THR n 
1 100 LYS n 
1 101 LEU n 
1 102 ASN n 
1 103 TYR n 
1 104 GLU n 
1 105 LYS n 
1 106 PRO n 
1 107 ILE n 
1 108 TYR n 
1 109 ARG n 
1 110 PHE n 
1 111 GLU n 
1 112 ARG n 
1 113 ILE n 
1 114 ARG n 
1 115 GLU n 
1 116 LEU n 
1 117 MET n 
1 118 ASN n 
1 119 LYS n 
1 120 GLU n 
1 121 LYS n 
1 122 LEU n 
1 123 ASN n 
1 124 ARG n 
1 125 GLU n 
1 126 GLU n 
1 127 LEU n 
1 128 LEU n 
1 129 ASP n 
1 130 LEU n 
1 131 GLN n 
1 132 THR n 
1 133 LEU n 
1 134 ASN n 
1 135 LEU n 
1 136 LEU n 
1 137 ALA n 
1 138 TRP n 
1 139 CYS n 
1 140 GLY n 
1 141 ARG n 
1 142 THR n 
1 143 LEU n 
1 144 ARG n 
1 145 LYS n 
1 146 ASP n 
1 147 LEU n 
1 148 LYS n 
1 149 ASP n 
1 150 LEU n 
1 151 LEU n 
1 152 ASN n 
1 153 LYS n 
1 154 GLY n 
1 155 ARG n 
1 156 ASN n 
1 157 TYR n 
1 158 THR n 
1 159 GLN n 
1 160 GLU n 
1 161 GLU n 
1 162 LYS n 
1 163 GLU n 
1 164 TYR n 
1 165 VAL n 
1 166 LEU n 
1 167 ASN n 
1 168 LYS n 
1 169 TYR n 
1 170 PHE n 
1 171 GLU n 
1 172 ILE n 
1 173 ILE n 
1 174 LYS n 
1 175 LYS n 
1 176 THR n 
1 177 LEU n 
1 178 SER n 
1 179 ILE n 
1 180 TYR n 
1 181 ARG n 
1 182 GLU n 
1 183 ILE n 
1 184 LYS n 
1 185 GLU n 
1 186 GLU n 
1 187 GLY n 
1 188 LYS n 
1 189 GLY n 
1 190 SER n 
1 191 VAL n 
1 192 SER n 
1 193 THR n 
1 194 SER n 
1 195 PRO n 
1 196 TYR n 
1 197 TYR n 
1 198 HIS n 
1 199 PRO n 
1 200 LEU n 
1 201 ILE n 
1 202 PRO n 
1 203 ILE n 
1 204 LEU n 
1 205 LEU n 
1 206 ASN n 
1 207 PRO n 
1 208 ASN n 
1 209 CYS n 
1 210 VAL n 
1 211 TYR n 
1 212 GLU n 
1 213 THR n 
1 214 THR n 
1 215 PRO n 
1 216 ASN n 
1 217 VAL n 
1 218 LYS n 
1 219 ILE n 
1 220 PRO n 
1 221 ASP n 
1 222 PHE n 
1 223 ALA n 
1 224 VAL n 
1 225 SER n 
1 226 PHE n 
1 227 ARG n 
1 228 GLU n 
1 229 ASP n 
1 230 ALA n 
1 231 SER n 
1 232 LYS n 
1 233 HIS n 
1 234 VAL n 
1 235 GLU n 
1 236 LEU n 
1 237 ALA n 
1 238 LYS n 
1 239 GLU n 
1 240 LYS n 
1 241 TYR n 
1 242 PHE n 
1 243 GLU n 
1 244 ILE n 
1 245 PHE n 
1 246 GLY n 
1 247 GLU n 
1 248 HIS n 
1 249 PRO n 
1 250 VAL n 
1 251 TYR n 
1 252 MET n 
1 253 TRP n 
1 254 PRO n 
1 255 PRO n 
1 256 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-ROH                                            'Glycam Condensed Sequence' GMML       1.0   
2 2 'WURCS=2.0/1,4,3/[a2122h-1a_1-5]/1-1-1-1/a4-b1_b4-c1_c4-d1'                       WURCS                       PDB2Glycan 1.1.0 
3 2 '[][a-D-Glcp]{[(4+1)][a-D-Glcp]{[(4+1)][a-D-Glcp]{[(4+1)][a-D-Glcp]{}}}}'         LINUCS                      PDB-CARE   ?     
4 3 'WURCS=2.0/1,6,6/[a2122h-1a_1-5]/1-1-1-1-1-1/a1-f4_a4-b1_b4-c1_c4-d1_d4-e1_e4-f1' WURCS                       PDB2Glycan 1.1.0 
# 
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 3 1 GLC C1 O1 6 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 
FLC non-polymer                   . 'CITRATE ANION'       ?                                     'C6 H5 O7 -3'    189.100 
GLC 'D-saccharide, alpha linking' . alpha-D-glucopyranose 'alpha-D-glucose; D-glucose; glucose' 'C6 H12 O6'      180.156 
GLN 'L-peptide linking'           y GLUTAMINE             ?                                     'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking'           y 'GLUTAMIC ACID'       ?                                     'C5 H9 N O4'     147.129 
GLY 'peptide linking'             y GLYCINE               ?                                     'C2 H5 N O2'     75.067  
GOL non-polymer                   . GLYCEROL              'GLYCERIN; PROPANE-1,2,3-TRIOL'       'C3 H8 O3'       92.094  
HIS 'L-peptide linking'           y HISTIDINE             ?                                     'C6 H10 N3 O2 1' 156.162 
HOH non-polymer                   . WATER                 ?                                     'H2 O'           18.015  
ILE 'L-peptide linking'           y ISOLEUCINE            ?                                     'C6 H13 N O2'    131.173 
LEU 'L-peptide linking'           y LEUCINE               ?                                     'C6 H13 N O2'    131.173 
LYS 'L-peptide linking'           y LYSINE                ?                                     'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking'           y METHIONINE            ?                                     'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking'           y PHENYLALANINE         ?                                     'C9 H11 N O2'    165.189 
PRO 'L-peptide linking'           y PROLINE               ?                                     'C5 H9 N O2'     115.130 
SER 'L-peptide linking'           y SERINE                ?                                     'C3 H7 N O3'     105.093 
THR 'L-peptide linking'           y THREONINE             ?                                     'C4 H9 N O3'     119.119 
TRP 'L-peptide linking'           y TRYPTOPHAN            ?                                     'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking'           y TYROSINE              ?                                     'C9 H11 N O3'    181.189 
VAL 'L-peptide linking'           y VALINE                ?                                     'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_chem_comp_identifier.comp_id 
_pdbx_chem_comp_identifier.type 
_pdbx_chem_comp_identifier.program 
_pdbx_chem_comp_identifier.program_version 
_pdbx_chem_comp_identifier.identifier 
GLC 'CONDENSED IUPAC CARBOHYDRATE SYMBOL' GMML     1.0 DGlcpa            
GLC 'COMMON NAME'                         GMML     1.0 a-D-glucopyranose 
GLC 'IUPAC CARBOHYDRATE SYMBOL'           PDB-CARE 1.0 a-D-Glcp          
GLC 'SNFG CARBOHYDRATE SYMBOL'            GMML     1.0 Glc               
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   1   MET MET A . n 
A 1 2   LYS 2   2   2   LYS LYS A . n 
A 1 3   LYS 3   3   3   LYS LYS A . n 
A 1 4   LEU 4   4   4   LEU LEU A . n 
A 1 5   PHE 5   5   5   PHE PHE A . n 
A 1 6   LEU 6   6   6   LEU LEU A . n 
A 1 7   VAL 7   7   7   VAL VAL A . n 
A 1 8   PHE 8   8   8   PHE PHE A . n 
A 1 9   TRP 9   9   9   TRP TRP A . n 
A 1 10  TRP 10  10  10  TRP TRP A . n 
A 1 11  HIS 11  11  11  HIS HIS A . n 
A 1 12  MET 12  12  12  MET MET A . n 
A 1 13  HIS 13  13  13  HIS HIS A . n 
A 1 14  GLN 14  14  14  GLN GLN A . n 
A 1 15  PRO 15  15  15  PRO PRO A . n 
A 1 16  LEU 16  16  16  LEU LEU A . n 
A 1 17  TYR 17  17  17  TYR TYR A . n 
A 1 18  ARG 18  18  18  ARG ARG A . n 
A 1 19  GLU 19  19  19  GLU GLU A . n 
A 1 20  PRO 20  20  20  PRO PRO A . n 
A 1 21  TYR 21  21  21  TYR TYR A . n 
A 1 22  THR 22  22  22  THR THR A . n 
A 1 23  GLY 23  23  23  GLY GLY A . n 
A 1 24  GLU 24  24  24  GLU GLU A . n 
A 1 25  TYR 25  25  25  TYR TYR A . n 
A 1 26  LEU 26  26  26  LEU LEU A . n 
A 1 27  LEU 27  27  27  LEU LEU A . n 
A 1 28  PRO 28  28  28  PRO PRO A . n 
A 1 29  TRP 29  29  29  TRP TRP A . n 
A 1 30  THR 30  30  30  THR THR A . n 
A 1 31  PHE 31  31  31  PHE PHE A . n 
A 1 32  PHE 32  32  32  PHE PHE A . n 
A 1 33  HIS 33  33  33  HIS HIS A . n 
A 1 34  ALA 34  34  34  ALA ALA A . n 
A 1 35  VAL 35  35  35  VAL VAL A . n 
A 1 36  LYS 36  36  36  LYS LYS A . n 
A 1 37  ASP 37  37  37  ASP ASP A . n 
A 1 38  TYR 38  38  38  TYR TYR A . n 
A 1 39  TYR 39  39  39  TYR TYR A . n 
A 1 40  ASP 40  40  40  ASP ASP A . n 
A 1 41  MET 41  41  41  MET MET A . n 
A 1 42  PRO 42  42  42  PRO PRO A . n 
A 1 43  ALA 43  43  43  ALA ALA A . n 
A 1 44  TYR 44  44  44  TYR TYR A . n 
A 1 45  LEU 45  45  45  LEU LEU A . n 
A 1 46  LYS 46  46  46  LYS LYS A . n 
A 1 47  ASP 47  47  47  ASP ASP A . n 
A 1 48  PHE 48  48  48  PHE PHE A . n 
A 1 49  GLU 49  49  49  GLU GLU A . n 
A 1 50  ILE 50  50  50  ILE ILE A . n 
A 1 51  LYS 51  51  51  LYS LYS A . n 
A 1 52  LEU 52  52  52  LEU LEU A . n 
A 1 53  ASN 53  53  53  ASN ASN A . n 
A 1 54  PHE 54  54  54  PHE PHE A . n 
A 1 55  ASN 55  55  55  ASN ASN A . n 
A 1 56  LEU 56  56  56  LEU LEU A . n 
A 1 57  THR 57  57  57  THR THR A . n 
A 1 58  PRO 58  58  58  PRO PRO A . n 
A 1 59  VAL 59  59  59  VAL VAL A . n 
A 1 60  LEU 60  60  60  LEU LEU A . n 
A 1 61  ILE 61  61  61  ILE ILE A . n 
A 1 62  ASP 62  62  62  ASP ASP A . n 
A 1 63  GLN 63  63  63  GLN GLN A . n 
A 1 64  ILE 64  64  64  ILE ILE A . n 
A 1 65  GLN 65  65  65  GLN GLN A . n 
A 1 66  GLU 66  66  66  GLU GLU A . n 
A 1 67  TYR 67  67  67  TYR TYR A . n 
A 1 68  ALA 68  68  68  ALA ALA A . n 
A 1 69  GLN 69  69  69  GLN GLN A . n 
A 1 70  GLY 70  70  70  GLY GLY A . n 
A 1 71  LYS 71  71  71  LYS LYS A . n 
A 1 72  ALA 72  72  72  ALA ALA A . n 
A 1 73  LYS 73  73  73  LYS LYS A . n 
A 1 74  ASP 74  74  74  ASP ASP A . n 
A 1 75  VAL 75  75  75  VAL VAL A . n 
A 1 76  PHE 76  76  76  PHE PHE A . n 
A 1 77  LEU 77  77  77  LEU LEU A . n 
A 1 78  GLU 78  78  78  GLU GLU A . n 
A 1 79  ALA 79  79  79  ALA ALA A . n 
A 1 80  ILE 80  80  80  ILE ILE A . n 
A 1 81  ARG 81  81  81  ARG ARG A . n 
A 1 82  LYS 82  82  82  LYS LYS A . n 
A 1 83  ASP 83  83  83  ASP ASP A . n 
A 1 84  PRO 84  84  84  PRO PRO A . n 
A 1 85  ASP 85  85  85  ASP ASP A . n 
A 1 86  ASP 86  86  86  ASP ASP A . n 
A 1 87  LEU 87  87  87  LEU LEU A . n 
A 1 88  GLU 88  88  88  GLU GLU A . n 
A 1 89  LYS 89  89  89  LYS LYS A . n 
A 1 90  GLU 90  90  90  GLU GLU A . n 
A 1 91  GLU 91  91  91  GLU GLU A . n 
A 1 92  VAL 92  92  92  VAL VAL A . n 
A 1 93  GLU 93  93  93  GLU GLU A . n 
A 1 94  LYS 94  94  94  LYS LYS A . n 
A 1 95  LEU 95  95  95  LEU LEU A . n 
A 1 96  ILE 96  96  96  ILE ILE A . n 
A 1 97  GLU 97  97  97  GLU GLU A . n 
A 1 98  PHE 98  98  98  PHE PHE A . n 
A 1 99  THR 99  99  99  THR THR A . n 
A 1 100 LYS 100 100 100 LYS LYS A . n 
A 1 101 LEU 101 101 101 LEU LEU A . n 
A 1 102 ASN 102 102 102 ASN ASN A . n 
A 1 103 TYR 103 103 103 TYR TYR A . n 
A 1 104 GLU 104 104 104 GLU GLU A . n 
A 1 105 LYS 105 105 105 LYS LYS A . n 
A 1 106 PRO 106 106 106 PRO PRO A . n 
A 1 107 ILE 107 107 107 ILE ILE A . n 
A 1 108 TYR 108 108 108 TYR TYR A . n 
A 1 109 ARG 109 109 109 ARG ARG A . n 
A 1 110 PHE 110 110 110 PHE PHE A . n 
A 1 111 GLU 111 111 111 GLU GLU A . n 
A 1 112 ARG 112 112 112 ARG ARG A . n 
A 1 113 ILE 113 113 113 ILE ILE A . n 
A 1 114 ARG 114 114 114 ARG ARG A . n 
A 1 115 GLU 115 115 115 GLU GLU A . n 
A 1 116 LEU 116 116 116 LEU LEU A . n 
A 1 117 MET 117 117 117 MET MET A . n 
A 1 118 ASN 118 118 118 ASN ASN A . n 
A 1 119 LYS 119 119 119 LYS LYS A . n 
A 1 120 GLU 120 120 120 GLU GLU A . n 
A 1 121 LYS 121 121 121 LYS LYS A . n 
A 1 122 LEU 122 122 122 LEU LEU A . n 
A 1 123 ASN 123 123 123 ASN ASN A . n 
A 1 124 ARG 124 124 124 ARG ARG A . n 
A 1 125 GLU 125 125 125 GLU GLU A . n 
A 1 126 GLU 126 126 126 GLU GLU A . n 
A 1 127 LEU 127 127 127 LEU LEU A . n 
A 1 128 LEU 128 128 128 LEU LEU A . n 
A 1 129 ASP 129 129 129 ASP ASP A . n 
A 1 130 LEU 130 130 130 LEU LEU A . n 
A 1 131 GLN 131 131 131 GLN GLN A . n 
A 1 132 THR 132 132 132 THR THR A . n 
A 1 133 LEU 133 133 133 LEU LEU A . n 
A 1 134 ASN 134 134 134 ASN ASN A . n 
A 1 135 LEU 135 135 135 LEU LEU A . n 
A 1 136 LEU 136 136 136 LEU LEU A . n 
A 1 137 ALA 137 137 137 ALA ALA A . n 
A 1 138 TRP 138 138 138 TRP TRP A . n 
A 1 139 CYS 139 139 139 CYS CYS A . n 
A 1 140 GLY 140 140 140 GLY GLY A . n 
A 1 141 ARG 141 141 141 ARG ARG A . n 
A 1 142 THR 142 142 142 THR THR A . n 
A 1 143 LEU 143 143 143 LEU LEU A . n 
A 1 144 ARG 144 144 144 ARG ARG A . n 
A 1 145 LYS 145 145 145 LYS LYS A . n 
A 1 146 ASP 146 146 146 ASP ASP A . n 
A 1 147 LEU 147 147 147 LEU LEU A . n 
A 1 148 LYS 148 148 148 LYS LYS A . n 
A 1 149 ASP 149 149 149 ASP ASP A . n 
A 1 150 LEU 150 150 150 LEU LEU A . n 
A 1 151 LEU 151 151 151 LEU LEU A . n 
A 1 152 ASN 152 152 152 ASN ASN A . n 
A 1 153 LYS 153 153 153 LYS LYS A . n 
A 1 154 GLY 154 154 154 GLY GLY A . n 
A 1 155 ARG 155 155 155 ARG ARG A . n 
A 1 156 ASN 156 156 156 ASN ASN A . n 
A 1 157 TYR 157 157 157 TYR TYR A . n 
A 1 158 THR 158 158 158 THR THR A . n 
A 1 159 GLN 159 159 159 GLN GLN A . n 
A 1 160 GLU 160 160 160 GLU GLU A . n 
A 1 161 GLU 161 161 161 GLU GLU A . n 
A 1 162 LYS 162 162 162 LYS LYS A . n 
A 1 163 GLU 163 163 163 GLU GLU A . n 
A 1 164 TYR 164 164 164 TYR TYR A . n 
A 1 165 VAL 165 165 165 VAL VAL A . n 
A 1 166 LEU 166 166 166 LEU LEU A . n 
A 1 167 ASN 167 167 167 ASN ASN A . n 
A 1 168 LYS 168 168 168 LYS LYS A . n 
A 1 169 TYR 169 169 169 TYR TYR A . n 
A 1 170 PHE 170 170 170 PHE PHE A . n 
A 1 171 GLU 171 171 171 GLU GLU A . n 
A 1 172 ILE 172 172 172 ILE ILE A . n 
A 1 173 ILE 173 173 173 ILE ILE A . n 
A 1 174 LYS 174 174 174 LYS LYS A . n 
A 1 175 LYS 175 175 175 LYS LYS A . n 
A 1 176 THR 176 176 176 THR THR A . n 
A 1 177 LEU 177 177 177 LEU LEU A . n 
A 1 178 SER 178 178 178 SER SER A . n 
A 1 179 ILE 179 179 179 ILE ILE A . n 
A 1 180 TYR 180 180 180 TYR TYR A . n 
A 1 181 ARG 181 181 181 ARG ARG A . n 
A 1 182 GLU 182 182 182 GLU GLU A . n 
A 1 183 ILE 183 183 183 ILE ILE A . n 
A 1 184 LYS 184 184 184 LYS LYS A . n 
A 1 185 GLU 185 185 185 GLU GLU A . n 
A 1 186 GLU 186 186 186 GLU GLU A . n 
A 1 187 GLY 187 187 187 GLY GLY A . n 
A 1 188 LYS 188 188 188 LYS LYS A . n 
A 1 189 GLY 189 189 189 GLY GLY A . n 
A 1 190 SER 190 190 190 SER SER A . n 
A 1 191 VAL 191 191 191 VAL VAL A . n 
A 1 192 SER 192 192 192 SER SER A . n 
A 1 193 THR 193 193 193 THR THR A . n 
A 1 194 SER 194 194 194 SER SER A . n 
A 1 195 PRO 195 195 195 PRO PRO A . n 
A 1 196 TYR 196 196 196 TYR TYR A . n 
A 1 197 TYR 197 197 197 TYR TYR A . n 
A 1 198 HIS 198 198 198 HIS HIS A . n 
A 1 199 PRO 199 199 199 PRO PRO A . n 
A 1 200 LEU 200 200 200 LEU LEU A . n 
A 1 201 ILE 201 201 201 ILE ILE A . n 
A 1 202 PRO 202 202 202 PRO PRO A . n 
A 1 203 ILE 203 203 203 ILE ILE A . n 
A 1 204 LEU 204 204 204 LEU LEU A . n 
A 1 205 LEU 205 205 205 LEU LEU A . n 
A 1 206 ASN 206 206 206 ASN ASN A . n 
A 1 207 PRO 207 207 207 PRO PRO A . n 
A 1 208 ASN 208 208 208 ASN ASN A . n 
A 1 209 CYS 209 209 209 CYS CYS A . n 
A 1 210 VAL 210 210 210 VAL VAL A . n 
A 1 211 TYR 211 211 211 TYR TYR A . n 
A 1 212 GLU 212 212 212 GLU GLU A . n 
A 1 213 THR 213 213 213 THR THR A . n 
A 1 214 THR 214 214 214 THR THR A . n 
A 1 215 PRO 215 215 215 PRO PRO A . n 
A 1 216 ASN 216 216 216 ASN ASN A . n 
A 1 217 VAL 217 217 217 VAL VAL A . n 
A 1 218 LYS 218 218 218 LYS LYS A . n 
A 1 219 ILE 219 219 219 ILE ILE A . n 
A 1 220 PRO 220 220 220 PRO PRO A . n 
A 1 221 ASP 221 221 221 ASP ASP A . n 
A 1 222 PHE 222 222 222 PHE PHE A . n 
A 1 223 ALA 223 223 223 ALA ALA A . n 
A 1 224 VAL 224 224 224 VAL VAL A . n 
A 1 225 SER 225 225 225 SER SER A . n 
A 1 226 PHE 226 226 226 PHE PHE A . n 
A 1 227 ARG 227 227 227 ARG ARG A . n 
A 1 228 GLU 228 228 228 GLU GLU A . n 
A 1 229 ASP 229 229 229 ASP ASP A . n 
A 1 230 ALA 230 230 230 ALA ALA A . n 
A 1 231 SER 231 231 231 SER SER A . n 
A 1 232 LYS 232 232 232 LYS LYS A . n 
A 1 233 HIS 233 233 233 HIS HIS A . n 
A 1 234 VAL 234 234 234 VAL VAL A . n 
A 1 235 GLU 235 235 235 GLU GLU A . n 
A 1 236 LEU 236 236 236 LEU LEU A . n 
A 1 237 ALA 237 237 237 ALA ALA A . n 
A 1 238 LYS 238 238 238 LYS LYS A . n 
A 1 239 GLU 239 239 239 GLU GLU A . n 
A 1 240 LYS 240 240 240 LYS LYS A . n 
A 1 241 TYR 241 241 241 TYR TYR A . n 
A 1 242 PHE 242 242 242 PHE PHE A . n 
A 1 243 GLU 243 243 243 GLU GLU A . n 
A 1 244 ILE 244 244 244 ILE ILE A . n 
A 1 245 PHE 245 245 245 PHE PHE A . n 
A 1 246 GLY 246 246 246 GLY GLY A . n 
A 1 247 GLU 247 247 247 GLU GLU A . n 
A 1 248 HIS 248 248 248 HIS HIS A . n 
A 1 249 PRO 249 249 249 PRO PRO A . n 
A 1 250 VAL 250 250 250 VAL VAL A . n 
A 1 251 TYR 251 251 251 TYR TYR A . n 
A 1 252 MET 252 252 252 MET MET A . n 
A 1 253 TRP 253 253 253 TRP TRP A . n 
A 1 254 PRO 254 254 254 PRO PRO A . n 
A 1 255 PRO 255 255 255 PRO PRO A . n 
A 1 256 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 
# 
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 
B 2 GLC 1 B GLC 1 A GLC 491 n 
B 2 GLC 2 B GLC 2 A GLC 492 n 
B 2 GLC 3 B GLC 3 A GLC 493 n 
B 2 GLC 4 B GLC 4 A GLC 494 n 
C 3 GLC 1 C GLC 1 A GLC 495 n 
C 3 GLC 2 C GLC 2 A GLC 496 n 
C 3 GLC 3 C GLC 3 A GLC 497 n 
C 3 GLC 4 C GLC 4 A GLC 498 n 
C 3 GLC 5 C GLC 5 A GLC 499 n 
C 3 GLC 6 C GLC 6 A GLC 500 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 
D 4 FLC 1   501 511 FLC FLC A . 
E 4 FLC 1   502 513 FLC FLC A . 
F 5 GOL 1   503 516 GOL GOL A . 
G 5 GOL 1   504 517 GOL GOL A . 
H 6 HOH 1   601 106 HOH HOH A . 
H 6 HOH 2   602 263 HOH HOH A . 
H 6 HOH 3   603 298 HOH HOH A . 
H 6 HOH 4   604 168 HOH HOH A . 
H 6 HOH 5   605 129 HOH HOH A . 
H 6 HOH 6   606 107 HOH HOH A . 
H 6 HOH 7   607 258 HOH HOH A . 
H 6 HOH 8   608 215 HOH HOH A . 
H 6 HOH 9   609 163 HOH HOH A . 
H 6 HOH 10  610 216 HOH HOH A . 
H 6 HOH 11  611 279 HOH HOH A . 
H 6 HOH 12  612 98  HOH HOH A . 
H 6 HOH 13  613 281 HOH HOH A . 
H 6 HOH 14  614 287 HOH HOH A . 
H 6 HOH 15  615 172 HOH HOH A . 
H 6 HOH 16  616 261 HOH HOH A . 
H 6 HOH 17  617 328 HOH HOH A . 
H 6 HOH 18  618 228 HOH HOH A . 
H 6 HOH 19  619 79  HOH HOH A . 
H 6 HOH 20  620 293 HOH HOH A . 
H 6 HOH 21  621 135 HOH HOH A . 
H 6 HOH 22  622 142 HOH HOH A . 
H 6 HOH 23  623 55  HOH HOH A . 
H 6 HOH 24  624 40  HOH HOH A . 
H 6 HOH 25  625 115 HOH HOH A . 
H 6 HOH 26  626 88  HOH HOH A . 
H 6 HOH 27  627 304 HOH HOH A . 
H 6 HOH 28  628 255 HOH HOH A . 
H 6 HOH 29  629 222 HOH HOH A . 
H 6 HOH 30  630 210 HOH HOH A . 
H 6 HOH 31  631 138 HOH HOH A . 
H 6 HOH 32  632 148 HOH HOH A . 
H 6 HOH 33  633 120 HOH HOH A . 
H 6 HOH 34  634 221 HOH HOH A . 
H 6 HOH 35  635 250 HOH HOH A . 
H 6 HOH 36  636 183 HOH HOH A . 
H 6 HOH 37  637 230 HOH HOH A . 
H 6 HOH 38  638 111 HOH HOH A . 
H 6 HOH 39  639 41  HOH HOH A . 
H 6 HOH 40  640 2   HOH HOH A . 
H 6 HOH 41  641 178 HOH HOH A . 
H 6 HOH 42  642 39  HOH HOH A . 
H 6 HOH 43  643 234 HOH HOH A . 
H 6 HOH 44  644 154 HOH HOH A . 
H 6 HOH 45  645 150 HOH HOH A . 
H 6 HOH 46  646 283 HOH HOH A . 
H 6 HOH 47  647 202 HOH HOH A . 
H 6 HOH 48  648 19  HOH HOH A . 
H 6 HOH 49  649 174 HOH HOH A . 
H 6 HOH 50  650 158 HOH HOH A . 
H 6 HOH 51  651 217 HOH HOH A . 
H 6 HOH 52  652 85  HOH HOH A . 
H 6 HOH 53  653 155 HOH HOH A . 
H 6 HOH 54  654 307 HOH HOH A . 
H 6 HOH 55  655 147 HOH HOH A . 
H 6 HOH 56  656 25  HOH HOH A . 
H 6 HOH 57  657 51  HOH HOH A . 
H 6 HOH 58  658 64  HOH HOH A . 
H 6 HOH 59  659 43  HOH HOH A . 
H 6 HOH 60  660 78  HOH HOH A . 
H 6 HOH 61  661 3   HOH HOH A . 
H 6 HOH 62  662 121 HOH HOH A . 
H 6 HOH 63  663 128 HOH HOH A . 
H 6 HOH 64  664 32  HOH HOH A . 
H 6 HOH 65  665 71  HOH HOH A . 
H 6 HOH 66  666 49  HOH HOH A . 
H 6 HOH 67  667 65  HOH HOH A . 
H 6 HOH 68  668 68  HOH HOH A . 
H 6 HOH 69  669 315 HOH HOH A . 
H 6 HOH 70  670 94  HOH HOH A . 
H 6 HOH 71  671 206 HOH HOH A . 
H 6 HOH 72  672 45  HOH HOH A . 
H 6 HOH 73  673 173 HOH HOH A . 
H 6 HOH 74  674 271 HOH HOH A . 
H 6 HOH 75  675 290 HOH HOH A . 
H 6 HOH 76  676 103 HOH HOH A . 
H 6 HOH 77  677 336 HOH HOH A . 
H 6 HOH 78  678 7   HOH HOH A . 
H 6 HOH 79  679 62  HOH HOH A . 
H 6 HOH 80  680 162 HOH HOH A . 
H 6 HOH 81  681 30  HOH HOH A . 
H 6 HOH 82  682 20  HOH HOH A . 
H 6 HOH 83  683 187 HOH HOH A . 
H 6 HOH 84  684 57  HOH HOH A . 
H 6 HOH 85  685 190 HOH HOH A . 
H 6 HOH 86  686 37  HOH HOH A . 
H 6 HOH 87  687 143 HOH HOH A . 
H 6 HOH 88  688 244 HOH HOH A . 
H 6 HOH 89  689 292 HOH HOH A . 
H 6 HOH 90  690 15  HOH HOH A . 
H 6 HOH 91  691 58  HOH HOH A . 
H 6 HOH 92  692 186 HOH HOH A . 
H 6 HOH 93  693 8   HOH HOH A . 
H 6 HOH 94  694 140 HOH HOH A . 
H 6 HOH 95  695 266 HOH HOH A . 
H 6 HOH 96  696 44  HOH HOH A . 
H 6 HOH 97  697 63  HOH HOH A . 
H 6 HOH 98  698 50  HOH HOH A . 
H 6 HOH 99  699 218 HOH HOH A . 
H 6 HOH 100 700 54  HOH HOH A . 
H 6 HOH 101 701 5   HOH HOH A . 
H 6 HOH 102 702 9   HOH HOH A . 
H 6 HOH 103 703 122 HOH HOH A . 
H 6 HOH 104 704 109 HOH HOH A . 
H 6 HOH 105 705 116 HOH HOH A . 
H 6 HOH 106 706 166 HOH HOH A . 
H 6 HOH 107 707 46  HOH HOH A . 
H 6 HOH 108 708 319 HOH HOH A . 
H 6 HOH 109 709 159 HOH HOH A . 
H 6 HOH 110 710 28  HOH HOH A . 
H 6 HOH 111 711 99  HOH HOH A . 
H 6 HOH 112 712 42  HOH HOH A . 
H 6 HOH 113 713 47  HOH HOH A . 
H 6 HOH 114 714 10  HOH HOH A . 
H 6 HOH 115 715 139 HOH HOH A . 
H 6 HOH 116 716 102 HOH HOH A . 
H 6 HOH 117 717 160 HOH HOH A . 
H 6 HOH 118 718 75  HOH HOH A . 
H 6 HOH 119 719 212 HOH HOH A . 
H 6 HOH 120 720 38  HOH HOH A . 
H 6 HOH 121 721 26  HOH HOH A . 
H 6 HOH 122 722 73  HOH HOH A . 
H 6 HOH 123 723 248 HOH HOH A . 
H 6 HOH 124 724 104 HOH HOH A . 
H 6 HOH 125 725 291 HOH HOH A . 
H 6 HOH 126 726 31  HOH HOH A . 
H 6 HOH 127 727 61  HOH HOH A . 
H 6 HOH 128 728 81  HOH HOH A . 
H 6 HOH 129 729 153 HOH HOH A . 
H 6 HOH 130 730 14  HOH HOH A . 
H 6 HOH 131 731 243 HOH HOH A . 
H 6 HOH 132 732 24  HOH HOH A . 
H 6 HOH 133 733 83  HOH HOH A . 
H 6 HOH 134 734 286 HOH HOH A . 
H 6 HOH 135 735 95  HOH HOH A . 
H 6 HOH 136 736 136 HOH HOH A . 
H 6 HOH 137 737 76  HOH HOH A . 
H 6 HOH 138 738 29  HOH HOH A . 
H 6 HOH 139 739 59  HOH HOH A . 
H 6 HOH 140 740 23  HOH HOH A . 
H 6 HOH 141 741 134 HOH HOH A . 
H 6 HOH 142 742 305 HOH HOH A . 
H 6 HOH 143 743 311 HOH HOH A . 
H 6 HOH 144 744 97  HOH HOH A . 
H 6 HOH 145 745 132 HOH HOH A . 
H 6 HOH 146 746 198 HOH HOH A . 
H 6 HOH 147 747 1   HOH HOH A . 
H 6 HOH 148 748 226 HOH HOH A . 
H 6 HOH 149 749 48  HOH HOH A . 
H 6 HOH 150 750 91  HOH HOH A . 
H 6 HOH 151 751 185 HOH HOH A . 
H 6 HOH 152 752 333 HOH HOH A . 
H 6 HOH 153 753 149 HOH HOH A . 
H 6 HOH 154 754 213 HOH HOH A . 
H 6 HOH 155 755 114 HOH HOH A . 
H 6 HOH 156 756 141 HOH HOH A . 
H 6 HOH 157 757 339 HOH HOH A . 
H 6 HOH 158 758 34  HOH HOH A . 
H 6 HOH 159 759 12  HOH HOH A . 
H 6 HOH 160 760 209 HOH HOH A . 
H 6 HOH 161 761 314 HOH HOH A . 
H 6 HOH 162 762 13  HOH HOH A . 
H 6 HOH 163 763 52  HOH HOH A . 
H 6 HOH 164 764 211 HOH HOH A . 
H 6 HOH 165 765 16  HOH HOH A . 
H 6 HOH 166 766 133 HOH HOH A . 
H 6 HOH 167 767 93  HOH HOH A . 
H 6 HOH 168 768 17  HOH HOH A . 
H 6 HOH 169 769 191 HOH HOH A . 
H 6 HOH 170 770 204 HOH HOH A . 
H 6 HOH 171 771 33  HOH HOH A . 
H 6 HOH 172 772 137 HOH HOH A . 
H 6 HOH 173 773 179 HOH HOH A . 
H 6 HOH 174 774 80  HOH HOH A . 
H 6 HOH 175 775 268 HOH HOH A . 
H 6 HOH 176 776 297 HOH HOH A . 
H 6 HOH 177 777 67  HOH HOH A . 
H 6 HOH 178 778 11  HOH HOH A . 
H 6 HOH 179 779 101 HOH HOH A . 
H 6 HOH 180 780 171 HOH HOH A . 
H 6 HOH 181 781 207 HOH HOH A . 
H 6 HOH 182 782 123 HOH HOH A . 
H 6 HOH 183 783 113 HOH HOH A . 
H 6 HOH 184 784 36  HOH HOH A . 
H 6 HOH 185 785 284 HOH HOH A . 
H 6 HOH 186 786 252 HOH HOH A . 
H 6 HOH 187 787 84  HOH HOH A . 
H 6 HOH 188 788 188 HOH HOH A . 
H 6 HOH 189 789 119 HOH HOH A . 
H 6 HOH 190 790 224 HOH HOH A . 
H 6 HOH 191 791 60  HOH HOH A . 
H 6 HOH 192 792 192 HOH HOH A . 
H 6 HOH 193 793 169 HOH HOH A . 
H 6 HOH 194 794 86  HOH HOH A . 
H 6 HOH 195 795 6   HOH HOH A . 
H 6 HOH 196 796 125 HOH HOH A . 
H 6 HOH 197 797 53  HOH HOH A . 
H 6 HOH 198 798 177 HOH HOH A . 
H 6 HOH 199 799 152 HOH HOH A . 
H 6 HOH 200 800 144 HOH HOH A . 
H 6 HOH 201 801 240 HOH HOH A . 
H 6 HOH 202 802 18  HOH HOH A . 
H 6 HOH 203 803 35  HOH HOH A . 
H 6 HOH 204 804 87  HOH HOH A . 
H 6 HOH 205 805 74  HOH HOH A . 
H 6 HOH 206 806 165 HOH HOH A . 
H 6 HOH 207 807 201 HOH HOH A . 
H 6 HOH 208 808 89  HOH HOH A . 
H 6 HOH 209 809 70  HOH HOH A . 
H 6 HOH 210 810 316 HOH HOH A . 
H 6 HOH 211 811 77  HOH HOH A . 
H 6 HOH 212 812 313 HOH HOH A . 
H 6 HOH 213 813 318 HOH HOH A . 
H 6 HOH 214 814 338 HOH HOH A . 
H 6 HOH 215 815 124 HOH HOH A . 
H 6 HOH 216 816 82  HOH HOH A . 
H 6 HOH 217 817 194 HOH HOH A . 
H 6 HOH 218 818 100 HOH HOH A . 
H 6 HOH 219 819 110 HOH HOH A . 
H 6 HOH 220 820 69  HOH HOH A . 
H 6 HOH 221 821 21  HOH HOH A . 
H 6 HOH 222 822 280 HOH HOH A . 
H 6 HOH 223 823 164 HOH HOH A . 
H 6 HOH 224 824 251 HOH HOH A . 
H 6 HOH 225 825 327 HOH HOH A . 
H 6 HOH 226 826 278 HOH HOH A . 
H 6 HOH 227 827 117 HOH HOH A . 
H 6 HOH 228 828 235 HOH HOH A . 
H 6 HOH 229 829 288 HOH HOH A . 
H 6 HOH 230 830 208 HOH HOH A . 
H 6 HOH 231 831 199 HOH HOH A . 
H 6 HOH 232 832 167 HOH HOH A . 
H 6 HOH 233 833 203 HOH HOH A . 
H 6 HOH 234 834 145 HOH HOH A . 
H 6 HOH 235 835 196 HOH HOH A . 
H 6 HOH 236 836 96  HOH HOH A . 
H 6 HOH 237 837 189 HOH HOH A . 
H 6 HOH 238 838 309 HOH HOH A . 
H 6 HOH 239 839 112 HOH HOH A . 
H 6 HOH 240 840 126 HOH HOH A . 
H 6 HOH 241 841 220 HOH HOH A . 
H 6 HOH 242 842 285 HOH HOH A . 
H 6 HOH 243 843 219 HOH HOH A . 
H 6 HOH 244 844 242 HOH HOH A . 
H 6 HOH 245 845 275 HOH HOH A . 
H 6 HOH 246 846 56  HOH HOH A . 
H 6 HOH 247 847 4   HOH HOH A . 
H 6 HOH 248 848 223 HOH HOH A . 
H 6 HOH 249 849 176 HOH HOH A . 
H 6 HOH 250 850 296 HOH HOH A . 
H 6 HOH 251 851 22  HOH HOH A . 
H 6 HOH 252 852 303 HOH HOH A . 
H 6 HOH 253 853 326 HOH HOH A . 
H 6 HOH 254 854 27  HOH HOH A . 
H 6 HOH 255 855 227 HOH HOH A . 
H 6 HOH 256 856 322 HOH HOH A . 
H 6 HOH 257 857 306 HOH HOH A . 
H 6 HOH 258 858 282 HOH HOH A . 
H 6 HOH 259 859 127 HOH HOH A . 
H 6 HOH 260 860 231 HOH HOH A . 
H 6 HOH 261 861 229 HOH HOH A . 
H 6 HOH 262 862 92  HOH HOH A . 
H 6 HOH 263 863 276 HOH HOH A . 
H 6 HOH 264 864 294 HOH HOH A . 
H 6 HOH 265 865 90  HOH HOH A . 
H 6 HOH 266 866 105 HOH HOH A . 
H 6 HOH 267 867 233 HOH HOH A . 
H 6 HOH 268 868 182 HOH HOH A . 
H 6 HOH 269 869 272 HOH HOH A . 
H 6 HOH 270 870 181 HOH HOH A . 
H 6 HOH 271 871 108 HOH HOH A . 
H 6 HOH 272 872 262 HOH HOH A . 
H 6 HOH 273 873 151 HOH HOH A . 
H 6 HOH 274 874 329 HOH HOH A . 
H 6 HOH 275 875 340 HOH HOH A . 
H 6 HOH 276 876 260 HOH HOH A . 
H 6 HOH 277 877 310 HOH HOH A . 
H 6 HOH 278 878 225 HOH HOH A . 
H 6 HOH 279 879 273 HOH HOH A . 
H 6 HOH 280 880 300 HOH HOH A . 
H 6 HOH 281 881 180 HOH HOH A . 
H 6 HOH 282 882 331 HOH HOH A . 
H 6 HOH 283 883 200 HOH HOH A . 
H 6 HOH 284 884 118 HOH HOH A . 
H 6 HOH 285 885 161 HOH HOH A . 
H 6 HOH 286 886 264 HOH HOH A . 
H 6 HOH 287 887 197 HOH HOH A . 
H 6 HOH 288 888 245 HOH HOH A . 
H 6 HOH 289 889 131 HOH HOH A . 
H 6 HOH 290 890 274 HOH HOH A . 
H 6 HOH 291 891 253 HOH HOH A . 
H 6 HOH 292 892 170 HOH HOH A . 
H 6 HOH 293 893 66  HOH HOH A . 
H 6 HOH 294 894 130 HOH HOH A . 
H 6 HOH 295 895 146 HOH HOH A . 
H 6 HOH 296 896 232 HOH HOH A . 
H 6 HOH 297 897 256 HOH HOH A . 
H 6 HOH 298 898 195 HOH HOH A . 
H 6 HOH 299 899 324 HOH HOH A . 
H 6 HOH 300 900 321 HOH HOH A . 
H 6 HOH 301 901 239 HOH HOH A . 
H 6 HOH 302 902 295 HOH HOH A . 
H 6 HOH 303 903 156 HOH HOH A . 
H 6 HOH 304 904 332 HOH HOH A . 
H 6 HOH 305 905 335 HOH HOH A . 
H 6 HOH 306 906 267 HOH HOH A . 
H 6 HOH 307 907 265 HOH HOH A . 
H 6 HOH 308 908 323 HOH HOH A . 
H 6 HOH 309 909 334 HOH HOH A . 
H 6 HOH 310 910 317 HOH HOH A . 
H 6 HOH 311 911 257 HOH HOH A . 
H 6 HOH 312 912 302 HOH HOH A . 
H 6 HOH 313 913 241 HOH HOH A . 
H 6 HOH 314 914 184 HOH HOH A . 
H 6 HOH 315 915 175 HOH HOH A . 
H 6 HOH 316 916 205 HOH HOH A . 
H 6 HOH 317 917 157 HOH HOH A . 
H 6 HOH 318 918 259 HOH HOH A . 
H 6 HOH 319 919 301 HOH HOH A . 
H 6 HOH 320 920 193 HOH HOH A . 
H 6 HOH 321 921 337 HOH HOH A . 
H 6 HOH 322 922 289 HOH HOH A . 
H 6 HOH 323 923 246 HOH HOH A . 
H 6 HOH 324 924 330 HOH HOH A . 
H 6 HOH 325 925 320 HOH HOH A . 
H 6 HOH 326 926 247 HOH HOH A . 
H 6 HOH 327 927 325 HOH HOH A . 
H 6 HOH 328 928 237 HOH HOH A . 
H 6 HOH 329 929 236 HOH HOH A . 
H 6 HOH 330 930 270 HOH HOH A . 
H 6 HOH 331 931 214 HOH HOH A . 
H 6 HOH 332 932 254 HOH HOH A . 
H 6 HOH 333 933 299 HOH HOH A . 
H 6 HOH 334 934 72  HOH HOH A . 
H 6 HOH 335 935 249 HOH HOH A . 
H 6 HOH 336 936 238 HOH HOH A . 
H 6 HOH 337 937 308 HOH HOH A . 
H 6 HOH 338 938 269 HOH HOH A . 
H 6 HOH 339 939 277 HOH HOH A . 
H 6 HOH 340 940 312 HOH HOH A . 
# 
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'   ? ? ? ? ? ? ? ? ? ? ? xia2   ? ? ? .                  2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? xia2   ? ? ? .                  3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? .                  4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   102.82 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9JLV 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     199.970 
_cell.length_a_esd                 ? 
_cell.length_b                     40.570 
_cell.length_b_esd                 ? 
_cell.length_c                     62.620 
_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                         9JLV 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                5 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'C 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                   9JLV 
_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             2.16 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          43.14 
_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 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2024-05-05 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.97918 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'SSRF BEAMLINE BL10U2' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97918 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL10U2 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9JLV 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.51 
_reflns.d_resolution_low                               28.58 
_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                                     76826 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.2 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                5.9 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          15.8 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_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                                0.067 
_reflns.pdbx_Rpim_I_all                                0.027 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.999 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.062 
_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                                    1.51 
_reflns_shell.d_res_low                                     1.55 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             5334 
_reflns_shell.percent_possible_obs                          ? 
_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                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               0.925 
_reflns_shell.pdbx_Rpim_I_all                               0.483 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.515 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.781 
_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                                 9JLV 
_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                            1.510 
_refine.ls_d_res_low                             25.218 
_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                     76794 
_refine.ls_number_reflns_R_free                  3885 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.17 
_refine.ls_percent_reflns_R_free                 5.06 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1650 
_refine.ls_R_factor_R_free                       0.1840 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1640 
_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                 18.96 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.15 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        4052 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         149 
_refine_hist.number_atoms_solvent             340 
_refine_hist.number_atoms_total               4541 
_refine_hist.d_res_high                       1.510 
_refine_hist.d_res_low                        25.218 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.007 ? 4335 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.918 ? 5881 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 5.609 ? 3614 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.052 ? 639  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.006 ? 724  ? 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' 1.5100 1.5284 . . 110 2422 92.00  . . . . 0.2736 . . . . . . . . . . . 0.2736 
'X-RAY DIFFRACTION' 1.5284 1.5478 . . 114 2488 94.00  . . . . 0.2614 . . . . . . . . . . . 0.2713 
'X-RAY DIFFRACTION' 1.5478 1.5681 . . 130 2499 96.00  . . . . 0.2570 . . . . . . . . . . . 0.2768 
'X-RAY DIFFRACTION' 1.5681 1.5896 . . 137 2493 97.00  . . . . 0.2357 . . . . . . . . . . . 0.2838 
'X-RAY DIFFRACTION' 1.5896 1.6123 . . 122 2643 100.00 . . . . 0.2154 . . . . . . . . . . . 0.2866 
'X-RAY DIFFRACTION' 1.6123 1.6364 . . 137 2578 100.00 . . . . 0.2094 . . . . . . . . . . . 0.2184 
'X-RAY DIFFRACTION' 1.6364 1.6619 . . 139 2618 100.00 . . . . 0.2015 . . . . . . . . . . . 0.2405 
'X-RAY DIFFRACTION' 1.6619 1.6892 . . 150 2611 100.00 . . . . 0.1938 . . . . . . . . . . . 0.2256 
'X-RAY DIFFRACTION' 1.6892 1.7183 . . 123 2575 100.00 . . . . 0.1879 . . . . . . . . . . . 0.2303 
'X-RAY DIFFRACTION' 1.7183 1.7495 . . 146 2619 100.00 . . . . 0.1806 . . . . . . . . . . . 0.2008 
'X-RAY DIFFRACTION' 1.7495 1.7832 . . 159 2598 100.00 . . . . 0.1739 . . . . . . . . . . . 0.2293 
'X-RAY DIFFRACTION' 1.7832 1.8196 . . 114 2640 100.00 . . . . 0.1675 . . . . . . . . . . . 0.1842 
'X-RAY DIFFRACTION' 1.8196 1.8591 . . 139 2628 100.00 . . . . 0.1581 . . . . . . . . . . . 0.1967 
'X-RAY DIFFRACTION' 1.8591 1.9024 . . 135 2610 100.00 . . . . 0.1631 . . . . . . . . . . . 0.2015 
'X-RAY DIFFRACTION' 1.9024 1.9499 . . 126 2617 100.00 . . . . 0.1724 . . . . . . . . . . . 0.2050 
'X-RAY DIFFRACTION' 1.9499 2.0026 . . 161 2601 100.00 . . . . 0.1561 . . . . . . . . . . . 0.1767 
'X-RAY DIFFRACTION' 2.0026 2.0615 . . 160 2587 100.00 . . . . 0.1577 . . . . . . . . . . . 0.1778 
'X-RAY DIFFRACTION' 2.0615 2.1280 . . 134 2659 100.00 . . . . 0.1536 . . . . . . . . . . . 0.1590 
'X-RAY DIFFRACTION' 2.1280 2.2040 . . 151 2568 100.00 . . . . 0.1542 . . . . . . . . . . . 0.1932 
'X-RAY DIFFRACTION' 2.2040 2.2922 . . 119 2632 100.00 . . . . 0.1583 . . . . . . . . . . . 0.1762 
'X-RAY DIFFRACTION' 2.2922 2.3965 . . 147 2657 100.00 . . . . 0.1612 . . . . . . . . . . . 0.1659 
'X-RAY DIFFRACTION' 2.3965 2.5227 . . 147 2607 100.00 . . . . 0.1605 . . . . . . . . . . . 0.1908 
'X-RAY DIFFRACTION' 2.5227 2.6806 . . 137 2646 100.00 . . . . 0.1542 . . . . . . . . . . . 0.1578 
'X-RAY DIFFRACTION' 2.6806 2.8873 . . 156 2612 100.00 . . . . 0.1579 . . . . . . . . . . . 0.1998 
'X-RAY DIFFRACTION' 2.8873 3.1774 . . 124 2660 100.00 . . . . 0.1602 . . . . . . . . . . . 0.1645 
'X-RAY DIFFRACTION' 3.1774 3.6359 . . 158 2649 100.00 . . . . 0.1506 . . . . . . . . . . . 0.1705 
'X-RAY DIFFRACTION' 3.6359 4.5764 . . 153 2653 100.00 . . . . 0.1363 . . . . . . . . . . . 0.1666 
'X-RAY DIFFRACTION' 4.5764 25.218 . . 157 2739 99.00  . . . . 0.1632 . . . . . . . . . . . 0.1632 
# 
_struct.entry_id                     9JLV 
_struct.title                        
'Crystal structure of GH57 family amylopullulanase from Aquifex aeolicus mutant E256Q in complex with alpha-cyclodextrin' 
_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        9JLV 
_struct_keywords.text            'GH57 family, amylopullulanase, Aquifex aeolicus, alpha-cyclodextrin, 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 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 4 ? 
F N N 5 ? 
G N N 5 ? 
H N N 6 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    O66934_AQUAE 
_struct_ref.pdbx_db_accession          O66934 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MKKLFLVFWWHMHQPLYREPYTGEYLLPWTFFHAVKDYYDMPAYLKDFEIKLNFNLTPVLIDQIQEYAQGKAKDVFLEAI
RKDPDDLEKEEVEKLIEFTKLNYEKPIYRFERIRELMNKEKLNREELLDLQTLNLLAWCGRTLRKDLKDLLNKGRNYTQE
EKEYVLNKYFEIIKKTLSIYREIKEEGKGSVSTSPYYHPLIPILLNPNCVYETTPNVKIPDFAVSFREDASKHVELAKEK
YFEIFGEHPVYMWPPEASVSNEALELYYEKGINMLATDEVILKNSVERASPYLRYYFRELISVFFRDKTLSDLIGFSYHA
WNAEDAVRDFIGRLKKIHESVDFQPVVFVVLDGENCWEYYEENGIPFLEKLYSTLEKEEWIETLTLEEAMRKEDVKTEVI
ESVKAGTWFDGNFLKWIGNKEKNEYWKILIEAKKKAKNDYILVAEGSDWFWWQGEEKAPFVEVFDKLFRSFVRRAQE
;
_struct_ref.pdbx_align_begin           1 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9JLV 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 477 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             O66934 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  477 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       477 
# 
_struct_ref_seq_dif.align_id                     1 
_struct_ref_seq_dif.pdbx_pdb_id_code             9JLV 
_struct_ref_seq_dif.mon_id                       GLN 
_struct_ref_seq_dif.pdbx_pdb_strand_id           A 
_struct_ref_seq_dif.seq_num                      256 
_struct_ref_seq_dif.pdbx_pdb_ins_code            ? 
_struct_ref_seq_dif.pdbx_seq_db_name             UNP 
_struct_ref_seq_dif.pdbx_seq_db_accession_code   O66934 
_struct_ref_seq_dif.db_mon_id                    GLU 
_struct_ref_seq_dif.pdbx_seq_db_seq_num          256 
_struct_ref_seq_dif.details                      'engineered mutation' 
_struct_ref_seq_dif.pdbx_auth_seq_num            256 
_struct_ref_seq_dif.pdbx_ordinal                 1 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,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 ASP A 278 ? VAL A 286 ? ASP A 278 VAL A 286 1 ? 9  
HELX_P HELX_P21 AC3 ASP A 307 ? SER A 317 ? ASP A 307 SER A 317 1 ? 11 
HELX_P HELX_P22 AC4 TYR A 318 ? TRP A 321 ? TYR A 318 TRP A 321 5 ? 4  
HELX_P HELX_P23 AC5 ASN A 322 ? VAL A 341 ? ASN A 322 VAL A 341 1 ? 20 
HELX_P HELX_P24 AC6 CYS A 356 ? ASN A 363 ? CYS A 356 ASN A 363 5 ? 8  
HELX_P HELX_P25 AC7 GLY A 364 ? GLU A 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 
# 
_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 ? B GLC . O4 ? ? ? 1_555 B GLC . C1 ? ? B GLC 1 B GLC 2 1_555 ? ? ? ? ? ? ? 1.421 ? ? 
covale2 covale both ? B GLC . O4 ? ? ? 1_555 B GLC . C1 ? ? B GLC 2 B GLC 3 1_555 ? ? ? ? ? ? ? 1.434 ? ? 
covale3 covale both ? B GLC . O4 ? ? ? 1_555 B GLC . C1 ? ? B GLC 3 B GLC 4 1_555 ? ? ? ? ? ? ? 1.441 ? ? 
covale4 covale both ? C GLC . O4 ? ? ? 1_555 C GLC . C1 ? ? C GLC 1 C GLC 2 1_555 ? ? ? ? ? ? ? 1.413 ? ? 
covale5 covale both ? C GLC . C1 ? ? ? 1_555 C GLC . O4 ? ? C GLC 1 C GLC 6 1_555 ? ? ? ? ? ? ? 1.456 ? ? 
covale6 covale both ? C GLC . O4 ? ? ? 1_555 C GLC . C1 ? ? C GLC 2 C GLC 3 1_555 ? ? ? ? ? ? ? 1.436 ? ? 
covale7 covale both ? C GLC . O4 ? ? ? 1_555 C GLC . C1 ? ? C GLC 3 C GLC 4 1_555 ? ? ? ? ? ? ? 1.413 ? ? 
covale8 covale both ? C GLC . O4 ? ? ? 1_555 C GLC . C1 ? ? C GLC 4 C GLC 5 1_555 ? ? ? ? ? ? ? 1.418 ? ? 
covale9 covale both ? C GLC . O4 ? ? ? 1_555 C GLC . C1 ? ? C GLC 5 C GLC 6 1_555 ? ? ? ? ? ? ? 1.400 ? ? 
# 
_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 ? 
# 
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      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 VAL A 191 ? SER A 192 ? VAL A 191 SER A 192 
AA1 2 ASN A 53  ? LEU A 56  ? ASN A 53  LEU A 56  
AA1 3 LEU A 4   ? MET A 12  ? LEU A 4   MET A 12  
AA1 4 VAL A 346 ? ASP A 352 ? VAL A 346 ASP A 352 
AA2 1 VAL A 191 ? SER A 192 ? VAL A 191 SER A 192 
AA2 2 ASN A 53  ? LEU A 56  ? ASN A 53  LEU A 56  
AA2 3 LEU A 4   ? MET A 12  ? LEU A 4   MET A 12  
AA2 4 ILE A 381 ? THR A 383 ? ILE A 381 THR A 383 
AA3 1 GLU A 24  ? TYR A 25  ? GLU A 24  TYR A 25  
AA3 2 LYS A 73  ? ASP A 74  ? LYS A 73  ASP A 74  
AA4 1 TYR A 251 ? MET A 252 ? TYR A 251 MET A 252 
AA4 2 MET A 274 ? THR A 277 ? MET A 274 THR A 277 
AA4 3 ILE A 301 ? PHE A 305 ? ILE A 301 PHE A 305 
AA4 4 ARG A 294 ? PHE A 297 ? ARG A 294 PHE A 297 
AA4 5 THR A 397 ? ILE A 400 ? THR A 397 ILE A 400 
# 
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 PHE A 304 ? O PHE A 304 
AA4 3 4 O VAL A 303 ? O VAL A 303 N TYR A 295 ? N TYR A 295 
AA4 4 5 N TYR A 296 ? N TYR A 296 O GLU A 398 ? O GLU A 398 
# 
_pdbx_entry_details.entry_id                   9JLV 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1  1 O   A HOH 886 ? ? O A HOH 938 ? ? 1.82 
2  1 O   A HOH 669 ? ? O A HOH 838 ? ? 1.86 
3  1 O   A HOH 663 ? ? O A HOH 845 ? ? 1.92 
4  1 O   A HOH 882 ? ? O A HOH 909 ? ? 1.93 
5  1 O   A HOH 674 ? ? O A HOH 863 ? ? 1.99 
6  1 O   A HOH 891 ? ? O A HOH 914 ? ? 2.00 
7  1 OD1 A ASP 149 ? ? O A HOH 601 ? ? 2.00 
8  1 O   A HOH 742 ? ? O A HOH 823 ? ? 2.01 
9  1 NH1 A ARG 181 ? ? O A HOH 602 ? ? 2.02 
10 1 ND2 A ASN 167 ? B O A HOH 603 ? ? 2.03 
11 1 O   A HOH 907 ? ? O A HOH 925 ? ? 2.03 
12 1 O   A HOH 613 ? ? O A HOH 812 ? ? 2.06 
13 1 O   A HOH 680 ? ? O A HOH 754 ? ? 2.09 
14 1 NZ  A LYS 174 ? ? O A HOH 604 ? ? 2.09 
15 1 OD1 A ASP 325 ? ? O A HOH 605 ? ? 2.09 
16 1 NH2 A ARG 181 ? ? O A HOH 602 ? ? 2.12 
17 1 O   A HOH 923 ? ? O A HOH 933 ? ? 2.15 
18 1 O   A HOH 925 ? ? O A HOH 940 ? ? 2.17 
19 1 O   A PRO 459 ? ? O A HOH 606 ? ? 2.18 
20 1 OE2 A GLU 378 ? ? O A HOH 607 ? ? 2.19 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 NE A ARG 81 ? ? CZ A ARG 81 ? ? NH1 A ARG 81 ? ? 124.42 120.30 4.12  0.50 N 
2 1 NE A ARG 81 ? ? CZ A ARG 81 ? ? NH2 A ARG 81 ? ? 116.01 120.30 -4.29 0.50 N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ASN A 206 ? ? -163.35 95.87 
2 1 ALA A 289 ? ? -110.17 67.28 
3 1 ASP A 394 ? ? -88.56  47.32 
4 1 PHE A 460 ? ? 74.18   -3.59 
# 
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 -32.6140 15.4348 28.1985 0.0954 ? 0.0009  ? 0.0027  ? 0.0652 ? 0.0091  ? 0.0842 ? 1.2123 ? -0.1370 
? 0.0071  ? 0.7156 ? -0.0512 ? 1.4859 ? 0.0051  ? -0.0818 ? -0.0466 ? 0.0521  ? 0.0182  ? -0.0267 ? 0.0753  ? 0.0929  ? -0.0470 ? 
2 'X-RAY DIFFRACTION' ? refined -17.7843 28.8991 41.8885 0.1871 ? -0.0226 ? -0.0326 ? 0.2600 ? -0.0347 ? 0.1830 ? 2.9785 ? -0.7853 
? 0.8977  ? 1.5994 ? -0.2652 ? 2.7569 ? -0.1860 ? -0.2656 ? 0.2797  ? 0.0850  ? 0.1090  ? -0.1767 ? -0.2481 ? 0.3990  ? 0.0618  ? 
3 'X-RAY DIFFRACTION' ? refined -31.0169 18.0419 43.2768 0.1610 ? 0.0383  ? 0.0157  ? 0.1797 ? 0.0210  ? 0.1094 ? 1.5812 ? 0.2706  
? 0.9116  ? 0.7940 ? 0.4276  ? 2.2159 ? 0.0065  ? -0.2738 ? -0.0786 ? 0.1701  ? 0.0092  ? -0.0246 ? 0.0807  ? 0.0316  ? -0.0112 ? 
4 'X-RAY DIFFRACTION' ? refined -32.6484 13.0894 8.3079  0.1096 ? -0.0002 ? -0.0162 ? 0.0755 ? -0.0116 ? 0.1134 ? 1.2036 ? 0.0349  
? -0.2121 ? 0.7934 ? -0.2307 ? 1.5715 ? 0.0128  ? 0.1001  ? -0.0952 ? -0.0780 ? -0.0085 ? 0.0461  ? 0.0973  ? 0.0655  ? -0.0098 ? 
5 'X-RAY DIFFRACTION' ? refined -43.7725 27.5945 10.2370 0.1004 ? 0.0062  ? -0.0052 ? 0.0625 ? 0.0178  ? 0.1115 ? 1.1817 ? -0.0222 
? 0.3279  ? 1.7103 ? 0.8290  ? 2.4527 ? 0.0456  ? 0.0535  ? 0.0450  ? 0.0567  ? -0.0255 ? -0.0392 ? -0.0815 ? -0.1286 ? -0.0146 ? 
6 'X-RAY DIFFRACTION' ? refined -47.4721 31.0416 21.1422 0.1762 ? 0.0495  ? 0.0122  ? 0.1321 ? 0.0198  ? 0.1482 ? 1.9816 ? -0.0729 
? 1.1238  ? 0.6393 ? -0.1440 ? 2.2625 ? -0.0909 ? -0.1127 ? 0.1224  ? 0.0562  ? 0.1002  ? 0.0990  ? -0.3543 ? -0.3080 ? 0.0497  ? 
7 'X-RAY DIFFRACTION' ? refined -51.8598 23.4953 23.8466 0.1226 ? 0.0206  ? 0.0297  ? 0.1728 ? 0.0346  ? 0.1629 ? 2.1451 ? -0.3749 
? 0.9019  ? 0.7522 ? -0.2981 ? 2.5833 ? -0.0460 ? -0.2031 ? -0.0562 ? 0.0209  ? 0.0599  ? 0.1509  ? -0.0236 ? -0.5075 ? -0.0208 ? 
8 'X-RAY DIFFRACTION' ? refined -24.5670 22.2695 5.6213  0.1585 ? -0.0228 ? 0.0173  ? 0.1512 ? 0.0075  ? 0.0971 ? 2.4624 ? -0.1600 
? 0.5837  ? 1.0173 ? -0.0777 ? 1.5237 ? -0.0229 ? 0.1022  ? 0.1416  ? -0.0646 ? -0.0081 ? -0.0887 ? -0.1373 ? 0.3125  ? 0.0357  ? 
9 'X-RAY DIFFRACTION' ? refined -16.1016 16.6024 17.0055 0.1134 ? -0.0054 ? 0.0101  ? 0.2356 ? 0.0093  ? 0.1393 ? 2.9265 ? -0.2782 
? 0.4617  ? 2.0801 ? 0.1640  ? 2.8759 ? -0.0131 ? -0.0440 ? 0.0289  ? 0.0391  ? 0.0114  ? -0.1198 ? -0.0582 ? 0.3793  ? -0.0264 ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1 'X-RAY DIFFRACTION' 1 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 1 through 81 )
;
2 'X-RAY DIFFRACTION' 2 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 82 through 123 )
;
3 'X-RAY DIFFRACTION' 3 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 124 through 185 )
;
4 'X-RAY DIFFRACTION' 4 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 186 through 278 )
;
5 'X-RAY DIFFRACTION' 5 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 279 through 322 )
;
6 'X-RAY DIFFRACTION' 6 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 323 through 360 )
;
7 'X-RAY DIFFRACTION' 7 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 361 through 396 )
;
8 'X-RAY DIFFRACTION' 8 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 397 through 435 )
;
9 'X-RAY DIFFRACTION' 9 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 436 through 477 )
;
# 
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  
FLC CAC  C N N 88  
FLC CA   C N N 89  
FLC CB   C N N 90  
FLC CBC  C N N 91  
FLC CG   C N N 92  
FLC CGC  C N N 93  
FLC OA1  O N N 94  
FLC OA2  O N N 95  
FLC OB1  O N N 96  
FLC OB2  O N N 97  
FLC OG1  O N N 98  
FLC OG2  O N N 99  
FLC OHB  O N N 100 
FLC HA1  H N N 101 
FLC HA2  H N N 102 
FLC HG1  H N N 103 
FLC HG2  H N N 104 
FLC HOB  H N N 105 
GLC C1   C N S 106 
GLC C2   C N R 107 
GLC C3   C N S 108 
GLC C4   C N S 109 
GLC C5   C N R 110 
GLC C6   C N N 111 
GLC O1   O N N 112 
GLC O2   O N N 113 
GLC O3   O N N 114 
GLC O4   O N N 115 
GLC O5   O N N 116 
GLC O6   O N N 117 
GLC H1   H N N 118 
GLC H2   H N N 119 
GLC H3   H N N 120 
GLC H4   H N N 121 
GLC H5   H N N 122 
GLC H61  H N N 123 
GLC H62  H N N 124 
GLC HO1  H N N 125 
GLC HO2  H N N 126 
GLC HO3  H N N 127 
GLC HO4  H N N 128 
GLC HO6  H N N 129 
GLN N    N N N 130 
GLN CA   C N S 131 
GLN C    C N N 132 
GLN O    O N N 133 
GLN CB   C N N 134 
GLN CG   C N N 135 
GLN CD   C N N 136 
GLN OE1  O N N 137 
GLN NE2  N N N 138 
GLN OXT  O N N 139 
GLN H    H N N 140 
GLN H2   H N N 141 
GLN HA   H N N 142 
GLN HB2  H N N 143 
GLN HB3  H N N 144 
GLN HG2  H N N 145 
GLN HG3  H N N 146 
GLN HE21 H N N 147 
GLN HE22 H N N 148 
GLN HXT  H N N 149 
GLU N    N N N 150 
GLU CA   C N S 151 
GLU C    C N N 152 
GLU O    O N N 153 
GLU CB   C N N 154 
GLU CG   C N N 155 
GLU CD   C N N 156 
GLU OE1  O N N 157 
GLU OE2  O N N 158 
GLU OXT  O N N 159 
GLU H    H N N 160 
GLU H2   H N N 161 
GLU HA   H N N 162 
GLU HB2  H N N 163 
GLU HB3  H N N 164 
GLU HG2  H N N 165 
GLU HG3  H N N 166 
GLU HE2  H N N 167 
GLU HXT  H N N 168 
GLY N    N N N 169 
GLY CA   C N N 170 
GLY C    C N N 171 
GLY O    O N N 172 
GLY OXT  O N N 173 
GLY H    H N N 174 
GLY H2   H N N 175 
GLY HA2  H N N 176 
GLY HA3  H N N 177 
GLY HXT  H N N 178 
GOL C1   C N N 179 
GOL O1   O N N 180 
GOL C2   C N N 181 
GOL O2   O N N 182 
GOL C3   C N N 183 
GOL O3   O N N 184 
GOL H11  H N N 185 
GOL H12  H N N 186 
GOL HO1  H N N 187 
GOL H2   H N N 188 
GOL HO2  H N N 189 
GOL H31  H N N 190 
GOL H32  H N N 191 
GOL HO3  H N N 192 
HIS N    N N N 193 
HIS CA   C N S 194 
HIS C    C N N 195 
HIS O    O N N 196 
HIS CB   C N N 197 
HIS CG   C Y N 198 
HIS ND1  N Y N 199 
HIS CD2  C Y N 200 
HIS CE1  C Y N 201 
HIS NE2  N Y N 202 
HIS OXT  O N N 203 
HIS H    H N N 204 
HIS H2   H N N 205 
HIS HA   H N N 206 
HIS HB2  H N N 207 
HIS HB3  H N N 208 
HIS HD1  H N N 209 
HIS HD2  H N N 210 
HIS HE1  H N N 211 
HIS HE2  H N N 212 
HIS HXT  H N N 213 
HOH O    O N N 214 
HOH H1   H N N 215 
HOH H2   H N N 216 
ILE N    N N N 217 
ILE CA   C N S 218 
ILE C    C N N 219 
ILE O    O N N 220 
ILE CB   C N S 221 
ILE CG1  C N N 222 
ILE CG2  C N N 223 
ILE CD1  C N N 224 
ILE OXT  O N N 225 
ILE H    H N N 226 
ILE H2   H N N 227 
ILE HA   H N N 228 
ILE HB   H N N 229 
ILE HG12 H N N 230 
ILE HG13 H N N 231 
ILE HG21 H N N 232 
ILE HG22 H N N 233 
ILE HG23 H N N 234 
ILE HD11 H N N 235 
ILE HD12 H N N 236 
ILE HD13 H N N 237 
ILE HXT  H N N 238 
LEU N    N N N 239 
LEU CA   C N S 240 
LEU C    C N N 241 
LEU O    O N N 242 
LEU CB   C N N 243 
LEU CG   C N N 244 
LEU CD1  C N N 245 
LEU CD2  C N N 246 
LEU OXT  O N N 247 
LEU H    H N N 248 
LEU H2   H N N 249 
LEU HA   H N N 250 
LEU HB2  H N N 251 
LEU HB3  H N N 252 
LEU HG   H N N 253 
LEU HD11 H N N 254 
LEU HD12 H N N 255 
LEU HD13 H N N 256 
LEU HD21 H N N 257 
LEU HD22 H N N 258 
LEU HD23 H N N 259 
LEU HXT  H N N 260 
LYS N    N N N 261 
LYS CA   C N S 262 
LYS C    C N N 263 
LYS O    O N N 264 
LYS CB   C N N 265 
LYS CG   C N N 266 
LYS CD   C N N 267 
LYS CE   C N N 268 
LYS NZ   N N N 269 
LYS OXT  O N N 270 
LYS H    H N N 271 
LYS H2   H N N 272 
LYS HA   H N N 273 
LYS HB2  H N N 274 
LYS HB3  H N N 275 
LYS HG2  H N N 276 
LYS HG3  H N N 277 
LYS HD2  H N N 278 
LYS HD3  H N N 279 
LYS HE2  H N N 280 
LYS HE3  H N N 281 
LYS HZ1  H N N 282 
LYS HZ2  H N N 283 
LYS HZ3  H N N 284 
LYS HXT  H N N 285 
MET N    N N N 286 
MET CA   C N S 287 
MET C    C N N 288 
MET O    O N N 289 
MET CB   C N N 290 
MET CG   C N N 291 
MET SD   S N N 292 
MET CE   C N N 293 
MET OXT  O N N 294 
MET H    H N N 295 
MET H2   H N N 296 
MET HA   H N N 297 
MET HB2  H N N 298 
MET HB3  H N N 299 
MET HG2  H N N 300 
MET HG3  H N N 301 
MET HE1  H N N 302 
MET HE2  H N N 303 
MET HE3  H N N 304 
MET HXT  H N N 305 
PHE N    N N N 306 
PHE CA   C N S 307 
PHE C    C N N 308 
PHE O    O N N 309 
PHE CB   C N N 310 
PHE CG   C Y N 311 
PHE CD1  C Y N 312 
PHE CD2  C Y N 313 
PHE CE1  C Y N 314 
PHE CE2  C Y N 315 
PHE CZ   C Y N 316 
PHE OXT  O N N 317 
PHE H    H N N 318 
PHE H2   H N N 319 
PHE HA   H N N 320 
PHE HB2  H N N 321 
PHE HB3  H N N 322 
PHE HD1  H N N 323 
PHE HD2  H N N 324 
PHE HE1  H N N 325 
PHE HE2  H N N 326 
PHE HZ   H N N 327 
PHE HXT  H N N 328 
PRO N    N N N 329 
PRO CA   C N S 330 
PRO C    C N N 331 
PRO O    O N N 332 
PRO CB   C N N 333 
PRO CG   C N N 334 
PRO CD   C N N 335 
PRO OXT  O N N 336 
PRO H    H N N 337 
PRO HA   H N N 338 
PRO HB2  H N N 339 
PRO HB3  H N N 340 
PRO HG2  H N N 341 
PRO HG3  H N N 342 
PRO HD2  H N N 343 
PRO HD3  H N N 344 
PRO HXT  H N N 345 
SER N    N N N 346 
SER CA   C N S 347 
SER C    C N N 348 
SER O    O N N 349 
SER CB   C N N 350 
SER OG   O N N 351 
SER OXT  O N N 352 
SER H    H N N 353 
SER H2   H N N 354 
SER HA   H N N 355 
SER HB2  H N N 356 
SER HB3  H N N 357 
SER HG   H N N 358 
SER HXT  H N N 359 
THR N    N N N 360 
THR CA   C N S 361 
THR C    C N N 362 
THR O    O N N 363 
THR CB   C N R 364 
THR OG1  O N N 365 
THR CG2  C N N 366 
THR OXT  O N N 367 
THR H    H N N 368 
THR H2   H N N 369 
THR HA   H N N 370 
THR HB   H N N 371 
THR HG1  H N N 372 
THR HG21 H N N 373 
THR HG22 H N N 374 
THR HG23 H N N 375 
THR HXT  H N N 376 
TRP N    N N N 377 
TRP CA   C N S 378 
TRP C    C N N 379 
TRP O    O N N 380 
TRP CB   C N N 381 
TRP CG   C Y N 382 
TRP CD1  C Y N 383 
TRP CD2  C Y N 384 
TRP NE1  N Y N 385 
TRP CE2  C Y N 386 
TRP CE3  C Y N 387 
TRP CZ2  C Y N 388 
TRP CZ3  C Y N 389 
TRP CH2  C Y N 390 
TRP OXT  O N N 391 
TRP H    H N N 392 
TRP H2   H N N 393 
TRP HA   H N N 394 
TRP HB2  H N N 395 
TRP HB3  H N N 396 
TRP HD1  H N N 397 
TRP HE1  H N N 398 
TRP HE3  H N N 399 
TRP HZ2  H N N 400 
TRP HZ3  H N N 401 
TRP HH2  H N N 402 
TRP HXT  H N N 403 
TYR N    N N N 404 
TYR CA   C N S 405 
TYR C    C N N 406 
TYR O    O N N 407 
TYR CB   C N N 408 
TYR CG   C Y N 409 
TYR CD1  C Y N 410 
TYR CD2  C Y N 411 
TYR CE1  C Y N 412 
TYR CE2  C Y N 413 
TYR CZ   C Y N 414 
TYR OH   O N N 415 
TYR OXT  O N N 416 
TYR H    H N N 417 
TYR H2   H N N 418 
TYR HA   H N N 419 
TYR HB2  H N N 420 
TYR HB3  H N N 421 
TYR HD1  H N N 422 
TYR HD2  H N N 423 
TYR HE1  H N N 424 
TYR HE2  H N N 425 
TYR HH   H N N 426 
TYR HXT  H N N 427 
VAL N    N N N 428 
VAL CA   C N S 429 
VAL C    C N N 430 
VAL O    O N N 431 
VAL CB   C N N 432 
VAL CG1  C N N 433 
VAL CG2  C N N 434 
VAL OXT  O N N 435 
VAL H    H N N 436 
VAL H2   H N N 437 
VAL HA   H N N 438 
VAL HB   H N N 439 
VAL HG11 H N N 440 
VAL HG12 H N N 441 
VAL HG13 H N N 442 
VAL HG21 H N N 443 
VAL HG22 H N N 444 
VAL HG23 H N N 445 
VAL HXT  H N N 446 
# 
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  
FLC CAC CA   sing N N 83  
FLC CAC OA1  doub N N 84  
FLC CAC OA2  sing N N 85  
FLC CA  CB   sing N N 86  
FLC CA  HA1  sing N N 87  
FLC CA  HA2  sing N N 88  
FLC CB  CBC  sing N N 89  
FLC CB  CG   sing N N 90  
FLC CB  OHB  sing N N 91  
FLC CBC OB1  doub N N 92  
FLC CBC OB2  sing N N 93  
FLC CG  CGC  sing N N 94  
FLC CG  HG1  sing N N 95  
FLC CG  HG2  sing N N 96  
FLC CGC OG1  doub N N 97  
FLC CGC OG2  sing N N 98  
FLC OHB HOB  sing N N 99  
GLC C1  C2   sing N N 100 
GLC C1  O1   sing N N 101 
GLC C1  O5   sing N N 102 
GLC C1  H1   sing N N 103 
GLC C2  C3   sing N N 104 
GLC C2  O2   sing N N 105 
GLC C2  H2   sing N N 106 
GLC C3  C4   sing N N 107 
GLC C3  O3   sing N N 108 
GLC C3  H3   sing N N 109 
GLC C4  C5   sing N N 110 
GLC C4  O4   sing N N 111 
GLC C4  H4   sing N N 112 
GLC C5  C6   sing N N 113 
GLC C5  O5   sing N N 114 
GLC C5  H5   sing N N 115 
GLC C6  O6   sing N N 116 
GLC C6  H61  sing N N 117 
GLC C6  H62  sing N N 118 
GLC O1  HO1  sing N N 119 
GLC O2  HO2  sing N N 120 
GLC O3  HO3  sing N N 121 
GLC O4  HO4  sing N N 122 
GLC O6  HO6  sing N N 123 
GLN N   CA   sing N N 124 
GLN N   H    sing N N 125 
GLN N   H2   sing N N 126 
GLN CA  C    sing N N 127 
GLN CA  CB   sing N N 128 
GLN CA  HA   sing N N 129 
GLN C   O    doub N N 130 
GLN C   OXT  sing N N 131 
GLN CB  CG   sing N N 132 
GLN CB  HB2  sing N N 133 
GLN CB  HB3  sing N N 134 
GLN CG  CD   sing N N 135 
GLN CG  HG2  sing N N 136 
GLN CG  HG3  sing N N 137 
GLN CD  OE1  doub N N 138 
GLN CD  NE2  sing N N 139 
GLN NE2 HE21 sing N N 140 
GLN NE2 HE22 sing N N 141 
GLN OXT HXT  sing N N 142 
GLU N   CA   sing N N 143 
GLU N   H    sing N N 144 
GLU N   H2   sing N N 145 
GLU CA  C    sing N N 146 
GLU CA  CB   sing N N 147 
GLU CA  HA   sing N N 148 
GLU C   O    doub N N 149 
GLU C   OXT  sing N N 150 
GLU CB  CG   sing N N 151 
GLU CB  HB2  sing N N 152 
GLU CB  HB3  sing N N 153 
GLU CG  CD   sing N N 154 
GLU CG  HG2  sing N N 155 
GLU CG  HG3  sing N N 156 
GLU CD  OE1  doub N N 157 
GLU CD  OE2  sing N N 158 
GLU OE2 HE2  sing N N 159 
GLU OXT HXT  sing N N 160 
GLY N   CA   sing N N 161 
GLY N   H    sing N N 162 
GLY N   H2   sing N N 163 
GLY CA  C    sing N N 164 
GLY CA  HA2  sing N N 165 
GLY CA  HA3  sing N N 166 
GLY C   O    doub N N 167 
GLY C   OXT  sing N N 168 
GLY OXT HXT  sing N N 169 
GOL C1  O1   sing N N 170 
GOL C1  C2   sing N N 171 
GOL C1  H11  sing N N 172 
GOL C1  H12  sing N N 173 
GOL O1  HO1  sing N N 174 
GOL C2  O2   sing N N 175 
GOL C2  C3   sing N N 176 
GOL C2  H2   sing N N 177 
GOL O2  HO2  sing N N 178 
GOL C3  O3   sing N N 179 
GOL C3  H31  sing N N 180 
GOL C3  H32  sing N N 181 
GOL O3  HO3  sing N N 182 
HIS N   CA   sing N N 183 
HIS N   H    sing N N 184 
HIS N   H2   sing N N 185 
HIS CA  C    sing N N 186 
HIS CA  CB   sing N N 187 
HIS CA  HA   sing N N 188 
HIS C   O    doub N N 189 
HIS C   OXT  sing N N 190 
HIS CB  CG   sing N N 191 
HIS CB  HB2  sing N N 192 
HIS CB  HB3  sing N N 193 
HIS CG  ND1  sing Y N 194 
HIS CG  CD2  doub Y N 195 
HIS ND1 CE1  doub Y N 196 
HIS ND1 HD1  sing N N 197 
HIS CD2 NE2  sing Y N 198 
HIS CD2 HD2  sing N N 199 
HIS CE1 NE2  sing Y N 200 
HIS CE1 HE1  sing N N 201 
HIS NE2 HE2  sing N N 202 
HIS OXT HXT  sing N N 203 
HOH O   H1   sing N N 204 
HOH O   H2   sing N N 205 
ILE N   CA   sing N N 206 
ILE N   H    sing N N 207 
ILE N   H2   sing N N 208 
ILE CA  C    sing N N 209 
ILE CA  CB   sing N N 210 
ILE CA  HA   sing N N 211 
ILE C   O    doub N N 212 
ILE C   OXT  sing N N 213 
ILE CB  CG1  sing N N 214 
ILE CB  CG2  sing N N 215 
ILE CB  HB   sing N N 216 
ILE CG1 CD1  sing N N 217 
ILE CG1 HG12 sing N N 218 
ILE CG1 HG13 sing N N 219 
ILE CG2 HG21 sing N N 220 
ILE CG2 HG22 sing N N 221 
ILE CG2 HG23 sing N N 222 
ILE CD1 HD11 sing N N 223 
ILE CD1 HD12 sing N N 224 
ILE CD1 HD13 sing N N 225 
ILE OXT HXT  sing N N 226 
LEU N   CA   sing N N 227 
LEU N   H    sing N N 228 
LEU N   H2   sing N N 229 
LEU CA  C    sing N N 230 
LEU CA  CB   sing N N 231 
LEU CA  HA   sing N N 232 
LEU C   O    doub N N 233 
LEU C   OXT  sing N N 234 
LEU CB  CG   sing N N 235 
LEU CB  HB2  sing N N 236 
LEU CB  HB3  sing N N 237 
LEU CG  CD1  sing N N 238 
LEU CG  CD2  sing N N 239 
LEU CG  HG   sing N N 240 
LEU CD1 HD11 sing N N 241 
LEU CD1 HD12 sing N N 242 
LEU CD1 HD13 sing N N 243 
LEU CD2 HD21 sing N N 244 
LEU CD2 HD22 sing N N 245 
LEU CD2 HD23 sing N N 246 
LEU OXT HXT  sing N N 247 
LYS N   CA   sing N N 248 
LYS N   H    sing N N 249 
LYS N   H2   sing N N 250 
LYS CA  C    sing N N 251 
LYS CA  CB   sing N N 252 
LYS CA  HA   sing N N 253 
LYS C   O    doub N N 254 
LYS C   OXT  sing N N 255 
LYS CB  CG   sing N N 256 
LYS CB  HB2  sing N N 257 
LYS CB  HB3  sing N N 258 
LYS CG  CD   sing N N 259 
LYS CG  HG2  sing N N 260 
LYS CG  HG3  sing N N 261 
LYS CD  CE   sing N N 262 
LYS CD  HD2  sing N N 263 
LYS CD  HD3  sing N N 264 
LYS CE  NZ   sing N N 265 
LYS CE  HE2  sing N N 266 
LYS CE  HE3  sing N N 267 
LYS NZ  HZ1  sing N N 268 
LYS NZ  HZ2  sing N N 269 
LYS NZ  HZ3  sing N N 270 
LYS OXT HXT  sing N N 271 
MET N   CA   sing N N 272 
MET N   H    sing N N 273 
MET N   H2   sing N N 274 
MET CA  C    sing N N 275 
MET CA  CB   sing N N 276 
MET CA  HA   sing N N 277 
MET C   O    doub N N 278 
MET C   OXT  sing N N 279 
MET CB  CG   sing N N 280 
MET CB  HB2  sing N N 281 
MET CB  HB3  sing N N 282 
MET CG  SD   sing N N 283 
MET CG  HG2  sing N N 284 
MET CG  HG3  sing N N 285 
MET SD  CE   sing N N 286 
MET CE  HE1  sing N N 287 
MET CE  HE2  sing N N 288 
MET CE  HE3  sing N N 289 
MET OXT HXT  sing N N 290 
PHE N   CA   sing N N 291 
PHE N   H    sing N N 292 
PHE N   H2   sing N N 293 
PHE CA  C    sing N N 294 
PHE CA  CB   sing N N 295 
PHE CA  HA   sing N N 296 
PHE C   O    doub N N 297 
PHE C   OXT  sing N N 298 
PHE CB  CG   sing N N 299 
PHE CB  HB2  sing N N 300 
PHE CB  HB3  sing N N 301 
PHE CG  CD1  doub Y N 302 
PHE CG  CD2  sing Y N 303 
PHE CD1 CE1  sing Y N 304 
PHE CD1 HD1  sing N N 305 
PHE CD2 CE2  doub Y N 306 
PHE CD2 HD2  sing N N 307 
PHE CE1 CZ   doub Y N 308 
PHE CE1 HE1  sing N N 309 
PHE CE2 CZ   sing Y N 310 
PHE CE2 HE2  sing N N 311 
PHE CZ  HZ   sing N N 312 
PHE OXT HXT  sing N N 313 
PRO N   CA   sing N N 314 
PRO N   CD   sing N N 315 
PRO N   H    sing N N 316 
PRO CA  C    sing N N 317 
PRO CA  CB   sing N N 318 
PRO CA  HA   sing N N 319 
PRO C   O    doub N N 320 
PRO C   OXT  sing N N 321 
PRO CB  CG   sing N N 322 
PRO CB  HB2  sing N N 323 
PRO CB  HB3  sing N N 324 
PRO CG  CD   sing N N 325 
PRO CG  HG2  sing N N 326 
PRO CG  HG3  sing N N 327 
PRO CD  HD2  sing N N 328 
PRO CD  HD3  sing N N 329 
PRO OXT HXT  sing N N 330 
SER N   CA   sing N N 331 
SER N   H    sing N N 332 
SER N   H2   sing N N 333 
SER CA  C    sing N N 334 
SER CA  CB   sing N N 335 
SER CA  HA   sing N N 336 
SER C   O    doub N N 337 
SER C   OXT  sing N N 338 
SER CB  OG   sing N N 339 
SER CB  HB2  sing N N 340 
SER CB  HB3  sing N N 341 
SER OG  HG   sing N N 342 
SER OXT HXT  sing N N 343 
THR N   CA   sing N N 344 
THR N   H    sing N N 345 
THR N   H2   sing N N 346 
THR CA  C    sing N N 347 
THR CA  CB   sing N N 348 
THR CA  HA   sing N N 349 
THR C   O    doub N N 350 
THR C   OXT  sing N N 351 
THR CB  OG1  sing N N 352 
THR CB  CG2  sing N N 353 
THR CB  HB   sing N N 354 
THR OG1 HG1  sing N N 355 
THR CG2 HG21 sing N N 356 
THR CG2 HG22 sing N N 357 
THR CG2 HG23 sing N N 358 
THR OXT HXT  sing N N 359 
TRP N   CA   sing N N 360 
TRP N   H    sing N N 361 
TRP N   H2   sing N N 362 
TRP CA  C    sing N N 363 
TRP CA  CB   sing N N 364 
TRP CA  HA   sing N N 365 
TRP C   O    doub N N 366 
TRP C   OXT  sing N N 367 
TRP CB  CG   sing N N 368 
TRP CB  HB2  sing N N 369 
TRP CB  HB3  sing N N 370 
TRP CG  CD1  doub Y N 371 
TRP CG  CD2  sing Y N 372 
TRP CD1 NE1  sing Y N 373 
TRP CD1 HD1  sing N N 374 
TRP CD2 CE2  doub Y N 375 
TRP CD2 CE3  sing Y N 376 
TRP NE1 CE2  sing Y N 377 
TRP NE1 HE1  sing N N 378 
TRP CE2 CZ2  sing Y N 379 
TRP CE3 CZ3  doub Y N 380 
TRP CE3 HE3  sing N N 381 
TRP CZ2 CH2  doub Y N 382 
TRP CZ2 HZ2  sing N N 383 
TRP CZ3 CH2  sing Y N 384 
TRP CZ3 HZ3  sing N N 385 
TRP CH2 HH2  sing N N 386 
TRP OXT HXT  sing N N 387 
TYR N   CA   sing N N 388 
TYR N   H    sing N N 389 
TYR N   H2   sing N N 390 
TYR CA  C    sing N N 391 
TYR CA  CB   sing N N 392 
TYR CA  HA   sing N N 393 
TYR C   O    doub N N 394 
TYR C   OXT  sing N N 395 
TYR CB  CG   sing N N 396 
TYR CB  HB2  sing N N 397 
TYR CB  HB3  sing N N 398 
TYR CG  CD1  doub Y N 399 
TYR CG  CD2  sing Y N 400 
TYR CD1 CE1  sing Y N 401 
TYR CD1 HD1  sing N N 402 
TYR CD2 CE2  doub Y N 403 
TYR CD2 HD2  sing N N 404 
TYR CE1 CZ   doub Y N 405 
TYR CE1 HE1  sing N N 406 
TYR CE2 CZ   sing Y N 407 
TYR CE2 HE2  sing N N 408 
TYR CZ  OH   sing N N 409 
TYR OH  HH   sing N N 410 
TYR OXT HXT  sing N N 411 
VAL N   CA   sing N N 412 
VAL N   H    sing N N 413 
VAL N   H2   sing N N 414 
VAL CA  C    sing N N 415 
VAL CA  CB   sing N N 416 
VAL CA  HA   sing N N 417 
VAL C   O    doub N N 418 
VAL C   OXT  sing N N 419 
VAL CB  CG1  sing N N 420 
VAL CB  CG2  sing N N 421 
VAL CB  HB   sing N N 422 
VAL CG1 HG11 sing N N 423 
VAL CG1 HG12 sing N N 424 
VAL CG1 HG13 sing N N 425 
VAL CG2 HG21 sing N N 426 
VAL CG2 HG22 sing N N 427 
VAL CG2 HG23 sing N N 428 
VAL OXT HXT  sing N N 429 
# 
_pdbx_audit_support.funding_organization   'Other government' 
_pdbx_audit_support.country                China 
_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 
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                    9JLV 
_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]   0.005001 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.001138 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.024649 
_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]   0.016378 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . MET A 1 1   ? -67.861 24.450 16.414  1.00 47.81 ? 1   MET A N   1 
ATOM   2    C CA  . MET A 1 1   ? -67.079 25.643 16.708  1.00 42.78 ? 1   MET A CA  1 
ATOM   3    C C   . MET A 1 1   ? -65.741 25.615 15.981  1.00 37.50 ? 1   MET A C   1 
ATOM   4    O O   . MET A 1 1   ? -65.073 24.581 15.916  1.00 40.04 ? 1   MET A O   1 
ATOM   5    C CB  . MET A 1 1   ? -66.859 25.783 18.219  1.00 44.12 ? 1   MET A CB  1 
ATOM   6    C CG  . MET A 1 1   ? -65.499 26.343 18.612  1.00 47.71 ? 1   MET A CG  1 
ATOM   7    S SD  . MET A 1 1   ? -65.217 26.302 20.394  1.00 50.55 ? 1   MET A SD  1 
ATOM   8    C CE  . MET A 1 1   ? -65.457 24.548 20.694  1.00 54.39 ? 1   MET A CE  1 
ATOM   9    N N   . LYS A 1 2   ? -65.362 26.765 15.431  1.00 31.39 ? 2   LYS A N   1 
ATOM   10   C CA  . LYS A 1 2   ? -64.069 26.926 14.773  1.00 23.80 ? 2   LYS A CA  1 
ATOM   11   C C   . LYS A 1 2   ? -62.979 27.026 15.833  1.00 25.86 ? 2   LYS A C   1 
ATOM   12   O O   . LYS A 1 2   ? -62.911 28.011 16.574  1.00 26.42 ? 2   LYS A O   1 
ATOM   13   C CB  . LYS A 1 2   ? -64.084 28.162 13.883  1.00 26.66 ? 2   LYS A CB  1 
ATOM   14   C CG  . LYS A 1 2   ? -62.778 28.431 13.157  1.00 27.05 ? 2   LYS A CG  1 
ATOM   15   C CD  . LYS A 1 2   ? -62.823 29.797 12.480  1.00 28.10 ? 2   LYS A CD  1 
ATOM   16   C CE  . LYS A 1 2   ? -62.703 30.926 13.496  1.00 29.58 ? 2   LYS A CE  1 
ATOM   17   N NZ  . LYS A 1 2   ? -62.807 32.259 12.833  1.00 30.37 ? 2   LYS A NZ  1 
ATOM   18   N N   . LYS A 1 3   ? -62.124 26.014 15.899  1.00 19.80 ? 3   LYS A N   1 
ATOM   19   C CA  . LYS A 1 3   ? -61.029 25.988 16.849  1.00 18.60 ? 3   LYS A CA  1 
ATOM   20   C C   . LYS A 1 3   ? -59.721 26.375 16.177  1.00 19.74 ? 3   LYS A C   1 
ATOM   21   O O   . LYS A 1 3   ? -59.586 26.357 14.949  1.00 22.14 ? 3   LYS A O   1 
ATOM   22   C CB  . LYS A 1 3   ? -60.903 24.600 17.477  1.00 25.59 ? 3   LYS A CB  1 
ATOM   23   C CG  . LYS A 1 3   ? -62.034 24.276 18.454  1.00 32.45 ? 3   LYS A CG  1 
ATOM   24   C CD  . LYS A 1 3   ? -61.892 22.867 18.992  1.00 40.07 ? 3   LYS A CD  1 
ATOM   25   C CE  . LYS A 1 3   ? -62.923 22.574 20.073  1.00 46.47 ? 3   LYS A CE  1 
ATOM   26   N NZ  . LYS A 1 3   ? -62.682 23.357 21.314  1.00 51.64 ? 3   LYS A NZ  1 
ATOM   27   N N   . LEU A 1 4   ? -58.755 26.741 17.011  1.00 18.14 ? 4   LEU A N   1 
ATOM   28   C CA  . LEU A 1 4   ? -57.366 26.843 16.609  1.00 20.24 ? 4   LEU A CA  1 
ATOM   29   C C   . LEU A 1 4   ? -56.676 25.596 17.124  1.00 19.38 ? 4   LEU A C   1 
ATOM   30   O O   . LEU A 1 4   ? -56.822 25.253 18.299  1.00 19.15 ? 4   LEU A O   1 
ATOM   31   C CB  . LEU A 1 4   ? -56.710 28.096 17.190  1.00 20.99 ? 4   LEU A CB  1 
ATOM   32   C CG  . LEU A 1 4   ? -55.224 28.312 16.899  1.00 17.45 ? 4   LEU A CG  1 
ATOM   33   C CD1 . LEU A 1 4   ? -54.926 29.801 16.748  1.00 19.65 ? 4   LEU A CD1 1 
ATOM   34   C CD2 . LEU A 1 4   ? -54.361 27.700 18.000  1.00 15.95 ? 4   LEU A CD2 1 
ATOM   35   N N   . PHE A 1 5   ? -55.949 24.915 16.253  1.00 14.93 ? 5   PHE A N   1 
ATOM   36   C CA  . PHE A 1 5   ? -55.224 23.711 16.631  1.00 16.52 ? 5   PHE A CA  1 
ATOM   37   C C   . PHE A 1 5   ? -53.773 24.092 16.908  1.00 16.15 ? 5   PHE A C   1 
ATOM   38   O O   . PHE A 1 5   ? -53.074 24.597 16.018  1.00 19.39 ? 5   PHE A O   1 
ATOM   39   C CB  . PHE A 1 5   ? -55.326 22.649 15.540  1.00 14.86 ? 5   PHE A CB  1 
ATOM   40   C CG  . PHE A 1 5   ? -56.729 22.132 15.317  1.00 17.05 ? 5   PHE A CG  1 
ATOM   41   C CD1 . PHE A 1 5   ? -57.477 21.623 16.373  1.00 19.11 ? 5   PHE A CD1 1 
ATOM   42   C CD2 . PHE A 1 5   ? -57.301 22.157 14.052  1.00 19.09 ? 5   PHE A CD2 1 
ATOM   43   C CE1 . PHE A 1 5   ? -58.760 21.149 16.167  1.00 19.71 ? 5   PHE A CE1 1 
ATOM   44   C CE2 . PHE A 1 5   ? -58.588 21.683 13.832  1.00 20.46 ? 5   PHE A CE2 1 
ATOM   45   C CZ  . PHE A 1 5   ? -59.325 21.182 14.894  1.00 19.67 ? 5   PHE A CZ  1 
ATOM   46   N N   . LEU A 1 6   ? -53.337 23.857 18.140  1.00 14.84 ? 6   LEU A N   1 
ATOM   47   C CA  . LEU A 1 6   ? -52.030 24.261 18.631  1.00 13.98 ? 6   LEU A CA  1 
ATOM   48   C C   . LEU A 1 6   ? -51.201 23.016 18.895  1.00 12.46 ? 6   LEU A C   1 
ATOM   49   O O   . LEU A 1 6   ? -51.665 22.095 19.575  1.00 14.31 ? 6   LEU A O   1 
ATOM   50   C CB  . LEU A 1 6   ? -52.187 25.101 19.898  1.00 14.44 ? 6   LEU A CB  1 
ATOM   51   C CG  . LEU A 1 6   ? -50.907 25.691 20.502  1.00 16.90 ? 6   LEU A CG  1 
ATOM   52   C CD1 . LEU A 1 6   ? -50.205 26.605 19.485  1.00 15.40 ? 6   LEU A CD1 1 
ATOM   53   C CD2 . LEU A 1 6   ? -51.288 26.468 21.749  1.00 16.91 ? 6   LEU A CD2 1 
ATOM   54   N N   . VAL A 1 7   ? -49.989 22.975 18.344  1.00 11.99 ? 7   VAL A N   1 
ATOM   55   C CA  . VAL A 1 7   ? -49.144 21.782 18.414  1.00 13.83 ? 7   VAL A CA  1 
ATOM   56   C C   . VAL A 1 7   ? -47.772 22.200 18.926  1.00 12.32 ? 7   VAL A C   1 
ATOM   57   O O   . VAL A 1 7   ? -47.000 22.825 18.186  1.00 12.74 ? 7   VAL A O   1 
ATOM   58   C CB  . VAL A 1 7   ? -49.019 21.093 17.050  1.00 11.51 ? 7   VAL A CB  1 
ATOM   59   C CG1 . VAL A 1 7   ? -48.387 19.709 17.199  1.00 14.66 ? 7   VAL A CG1 1 
ATOM   60   C CG2 . VAL A 1 7   ? -50.382 20.996 16.362  1.00 14.96 ? 7   VAL A CG2 1 
ATOM   61   N N   . PHE A 1 8   ? -47.455 21.843 20.176  1.00 11.93 ? 8   PHE A N   1 
ATOM   62   C CA  . PHE A 1 8   ? -46.115 22.051 20.720  1.00 11.27 ? 8   PHE A CA  1 
ATOM   63   C C   . PHE A 1 8   ? -45.250 20.853 20.382  1.00 11.86 ? 8   PHE A C   1 
ATOM   64   O O   . PHE A 1 8   ? -45.671 19.715 20.575  1.00 12.98 ? 8   PHE A O   1 
ATOM   65   C CB  . PHE A 1 8   ? -46.124 22.220 22.242  1.00 12.40 ? 8   PHE A CB  1 
ATOM   66   C CG  . PHE A 1 8   ? -46.687 23.521 22.695  1.00 13.21 ? 8   PHE A CG  1 
ATOM   67   C CD1 . PHE A 1 8   ? -45.870 24.632 22.838  1.00 14.21 ? 8   PHE A CD1 1 
ATOM   68   C CD2 . PHE A 1 8   ? -48.040 23.640 22.966  1.00 12.38 ? 8   PHE A CD2 1 
ATOM   69   C CE1 . PHE A 1 8   ? -46.395 25.846 23.251  1.00 15.10 ? 8   PHE A CE1 1 
ATOM   70   C CE2 . PHE A 1 8   ? -48.578 24.849 23.383  1.00 16.41 ? 8   PHE A CE2 1 
ATOM   71   C CZ  . PHE A 1 8   ? -47.758 25.953 23.528  1.00 16.44 ? 8   PHE A CZ  1 
ATOM   72   N N   . TRP A 1 9   ? -44.038 21.106 19.893  1.00 12.28 ? 9   TRP A N   1 
ATOM   73   C CA  . TRP A 1 9   ? -43.083 20.032 19.632  1.00 11.88 ? 9   TRP A CA  1 
ATOM   74   C C   . TRP A 1 9   ? -41.750 20.475 20.230  1.00 11.69 ? 9   TRP A C   1 
ATOM   75   O O   . TRP A 1 9   ? -41.068 21.338 19.674  1.00 11.21 ? 9   TRP A O   1 
ATOM   76   C CB  . TRP A 1 9   ? -42.989 19.746 18.138  1.00 12.39 ? 9   TRP A CB  1 
ATOM   77   C CG  . TRP A 1 9   ? -42.379 18.432 17.733  1.00 9.22  ? 9   TRP A CG  1 
ATOM   78   C CD1 . TRP A 1 9   ? -41.697 17.530 18.520  1.00 13.98 ? 9   TRP A CD1 1 
ATOM   79   C CD2 . TRP A 1 9   ? -42.372 17.898 16.403  1.00 8.98  ? 9   TRP A CD2 1 
ATOM   80   N NE1 . TRP A 1 9   ? -41.280 16.458 17.738  1.00 11.82 ? 9   TRP A NE1 1 
ATOM   81   C CE2 . TRP A 1 9   ? -41.689 16.668 16.441  1.00 10.95 ? 9   TRP A CE2 1 
ATOM   82   C CE3 . TRP A 1 9   ? -42.910 18.341 15.175  1.00 11.60 ? 9   TRP A CE3 1 
ATOM   83   C CZ2 . TRP A 1 9   ? -41.514 15.877 15.296  1.00 12.07 ? 9   TRP A CZ2 1 
ATOM   84   C CZ3 . TRP A 1 9   ? -42.739 17.553 14.049  1.00 11.84 ? 9   TRP A CZ3 1 
ATOM   85   C CH2 . TRP A 1 9   ? -42.047 16.331 14.116  1.00 13.74 ? 9   TRP A CH2 1 
ATOM   86   N N   . TRP A 1 10  ? -41.412 19.906 21.385  1.00 11.57 ? 10  TRP A N   1 
ATOM   87   C CA  . TRP A 1 10  ? -40.233 20.296 22.150  1.00 13.29 ? 10  TRP A CA  1 
ATOM   88   C C   . TRP A 1 10  ? -39.091 19.347 21.806  1.00 12.59 ? 10  TRP A C   1 
ATOM   89   O O   . TRP A 1 10  ? -39.193 18.143 22.060  1.00 13.53 ? 10  TRP A O   1 
ATOM   90   C CB  . TRP A 1 10  ? -40.525 20.226 23.645  1.00 13.10 ? 10  TRP A CB  1 
ATOM   91   C CG  . TRP A 1 10  ? -41.603 21.130 24.176  1.00 10.38 ? 10  TRP A CG  1 
ATOM   92   C CD1 . TRP A 1 10  ? -42.784 20.748 24.721  1.00 11.01 ? 10  TRP A CD1 1 
ATOM   93   C CD2 . TRP A 1 10  ? -41.556 22.565 24.277  1.00 11.02 ? 10  TRP A CD2 1 
ATOM   94   N NE1 . TRP A 1 10  ? -43.497 21.857 25.147  1.00 11.36 ? 10  TRP A NE1 1 
ATOM   95   C CE2 . TRP A 1 10  ? -42.758 22.979 24.888  1.00 11.15 ? 10  TRP A CE2 1 
ATOM   96   C CE3 . TRP A 1 10  ? -40.613 23.532 23.909  1.00 11.25 ? 10  TRP A CE3 1 
ATOM   97   C CZ2 . TRP A 1 10  ? -43.047 24.318 25.143  1.00 12.32 ? 10  TRP A CZ2 1 
ATOM   98   C CZ3 . TRP A 1 10  ? -40.896 24.863 24.165  1.00 11.29 ? 10  TRP A CZ3 1 
ATOM   99   C CH2 . TRP A 1 10  ? -42.109 25.245 24.766  1.00 12.89 ? 10  TRP A CH2 1 
ATOM   100  N N   . HIS A 1 11  ? -38.018 19.881 21.229  1.00 9.94  ? 11  HIS A N   1 
ATOM   101  C CA  . HIS A 1 11  ? -36.932 19.066 20.688  1.00 10.30 ? 11  HIS A CA  1 
ATOM   102  C C   . HIS A 1 11  ? -35.777 18.947 21.685  1.00 10.14 ? 11  HIS A C   1 
ATOM   103  O O   . HIS A 1 11  ? -35.171 19.956 22.066  1.00 10.62 ? 11  HIS A O   1 
ATOM   104  C CB  . HIS A 1 11  ? -36.446 19.662 19.370  1.00 11.09 ? 11  HIS A CB  1 
ATOM   105  C CG  . HIS A 1 11  ? -35.045 19.282 19.019  1.00 11.78 ? 11  HIS A CG  1 
ATOM   106  N ND1 . HIS A 1 11  ? -34.675 17.985 18.719  1.00 10.75 ? 11  HIS A ND1 1 
ATOM   107  C CD2 . HIS A 1 11  ? -33.919 20.027 18.949  1.00 12.54 ? 11  HIS A CD2 1 
ATOM   108  C CE1 . HIS A 1 11  ? -33.373 17.958 18.473  1.00 11.66 ? 11  HIS A CE1 1 
ATOM   109  N NE2 . HIS A 1 11  ? -32.895 19.184 18.601  1.00 12.36 ? 11  HIS A NE2 1 
ATOM   110  N N   . MET A 1 12  ? -35.454 17.713 22.063  1.00 9.33  ? 12  MET A N   1 
ATOM   111  C CA  . MET A 1 12  ? -34.417 17.414 23.048  1.00 9.10  ? 12  MET A CA  1 
ATOM   112  C C   . MET A 1 12  ? -33.216 16.733 22.395  1.00 9.49  ? 12  MET A C   1 
ATOM   113  O O   . MET A 1 12  ? -33.369 15.701 21.729  1.00 11.33 ? 12  MET A O   1 
ATOM   114  C CB  . MET A 1 12  ? -34.968 16.506 24.148  1.00 9.78  ? 12  MET A CB  1 
ATOM   115  C CG  . MET A 1 12  ? -36.291 16.935 24.727  1.00 10.78 ? 12  MET A CG  1 
ATOM   116  S SD  . MET A 1 12  ? -36.221 18.575 25.470  1.00 11.21 ? 12  MET A SD  1 
ATOM   117  C CE  . MET A 1 12  ? -37.752 18.592 26.395  1.00 13.78 ? 12  MET A CE  1 
ATOM   118  N N   . HIS A 1 13  ? -32.013 17.259 22.654  1.00 10.92 ? 13  HIS A N   1 
ATOM   119  C CA  . HIS A 1 13  ? -30.817 16.710 22.022  1.00 10.67 ? 13  HIS A CA  1 
ATOM   120  C C   . HIS A 1 13  ? -29.566 17.070 22.805  1.00 9.96  ? 13  HIS A C   1 
ATOM   121  O O   . HIS A 1 13  ? -29.463 18.176 23.326  1.00 10.64 ? 13  HIS A O   1 
ATOM   122  C CB  . HIS A 1 13  ? -30.663 17.248 20.599  1.00 10.24 ? 13  HIS A CB  1 
ATOM   123  C CG  . HIS A 1 13  ? -29.352 16.912 19.963  1.00 9.22  ? 13  HIS A CG  1 
ATOM   124  N ND1 . HIS A 1 13  ? -28.888 15.618 19.830  1.00 10.71 ? 13  HIS A ND1 1 
ATOM   125  C CD2 . HIS A 1 13  ? -28.402 17.714 19.421  1.00 10.59 ? 13  HIS A CD2 1 
ATOM   126  C CE1 . HIS A 1 13  ? -27.705 15.641 19.237  1.00 11.82 ? 13  HIS A CE1 1 
ATOM   127  N NE2 . HIS A 1 13  ? -27.394 16.900 18.971  1.00 11.56 ? 13  HIS A NE2 1 
ATOM   128  N N   . GLN A 1 14  ? -28.598 16.144 22.843  1.00 8.85  ? 14  GLN A N   1 
ATOM   129  C CA  . GLN A 1 14  ? -27.213 16.463 23.249  1.00 9.24  ? 14  GLN A CA  1 
ATOM   130  C C   . GLN A 1 14  ? -26.277 15.659 22.355  1.00 10.64 ? 14  GLN A C   1 
ATOM   131  O O   . GLN A 1 14  ? -26.528 14.471 22.127  1.00 11.56 ? 14  GLN A O   1 
ATOM   132  C CB  . GLN A 1 14  ? -26.889 16.133 24.727  1.00 12.07 ? 14  GLN A CB  1 
ATOM   133  C CG  . GLN A 1 14  ? -27.655 16.923 25.786  1.00 13.14 ? 14  GLN A CG  1 
ATOM   134  C CD  . GLN A 1 14  ? -27.331 18.415 25.793  1.00 11.13 ? 14  GLN A CD  1 
ATOM   135  O OE1 . GLN A 1 14  ? -26.263 18.852 25.348  1.00 11.21 ? 14  GLN A OE1 1 
ATOM   136  N NE2 . GLN A 1 14  ? -28.275 19.207 26.281  1.00 12.05 ? 14  GLN A NE2 1 
ATOM   137  N N   . PRO A 1 15  ? -25.206 16.263 21.840  1.00 10.29 ? 15  PRO A N   1 
ATOM   138  C CA  . PRO A 1 15  ? -24.170 15.480 21.164  1.00 10.99 ? 15  PRO A CA  1 
ATOM   139  C C   . PRO A 1 15  ? -23.468 14.567 22.164  1.00 12.73 ? 15  PRO A C   1 
ATOM   140  O O   . PRO A 1 15  ? -23.597 14.711 23.379  1.00 13.30 ? 15  PRO A O   1 
ATOM   141  C CB  . PRO A 1 15  ? -23.226 16.554 20.612  1.00 13.75 ? 15  PRO A CB  1 
ATOM   142  C CG  . PRO A 1 15  ? -23.331 17.675 21.650  1.00 12.61 ? 15  PRO A CG  1 
ATOM   143  C CD  . PRO A 1 15  ? -24.796 17.665 22.064  1.00 12.04 ? 15  PRO A CD  1 
ATOM   144  N N   . LEU A 1 16  ? -22.712 13.606 21.645  1.00 13.13 ? 16  LEU A N   1 
ATOM   145  C CA  . LEU A 1 16  ? -22.065 12.624 22.518  1.00 10.95 ? 16  LEU A CA  1 
ATOM   146  C C   . LEU A 1 16  ? -20.874 13.257 23.229  1.00 14.36 ? 16  LEU A C   1 
ATOM   147  O O   . LEU A 1 16  ? -19.856 13.561 22.604  1.00 13.68 ? 16  LEU A O   1 
ATOM   148  C CB  . LEU A 1 16  ? -21.627 11.401 21.717  1.00 12.75 ? 16  LEU A CB  1 
ATOM   149  C CG  . LEU A 1 16  ? -21.070 10.240 22.555  1.00 11.88 ? 16  LEU A CG  1 
ATOM   150  C CD1 . LEU A 1 16  ? -22.077 9.810  23.637  1.00 16.50 ? 16  LEU A CD1 1 
ATOM   151  C CD2 . LEU A 1 16  ? -20.720 9.082  21.637  1.00 13.53 ? 16  LEU A CD2 1 
ATOM   152  N N   . TYR A 1 17  ? -20.990 13.427 24.545  1.00 12.60 ? 17  TYR A N   1 
ATOM   153  C CA  . TYR A 1 17  ? -19.907 13.995 25.338  1.00 14.60 ? 17  TYR A CA  1 
ATOM   154  C C   . TYR A 1 17  ? -18.917 12.945 25.806  1.00 16.43 ? 17  TYR A C   1 
ATOM   155  O O   . TYR A 1 17  ? -17.901 13.304 26.415  1.00 15.48 ? 17  TYR A O   1 
ATOM   156  C CB  . TYR A 1 17  ? -20.465 14.743 26.555  1.00 13.88 ? 17  TYR A CB  1 
ATOM   157  C CG  . TYR A 1 17  ? -21.299 15.947 26.176  1.00 12.37 ? 17  TYR A CG  1 
ATOM   158  C CD1 . TYR A 1 17  ? -20.746 16.990 25.439  1.00 17.88 ? 17  TYR A CD1 1 
ATOM   159  C CD2 . TYR A 1 17  ? -22.634 16.029 26.538  1.00 12.22 ? 17  TYR A CD2 1 
ATOM   160  C CE1 . TYR A 1 17  ? -21.509 18.089 25.074  1.00 13.29 ? 17  TYR A CE1 1 
ATOM   161  C CE2 . TYR A 1 17  ? -23.412 17.118 26.184  1.00 12.00 ? 17  TYR A CE2 1 
ATOM   162  C CZ  . TYR A 1 17  ? -22.840 18.151 25.462  1.00 14.25 ? 17  TYR A CZ  1 
ATOM   163  O OH  . TYR A 1 17  ? -23.614 19.244 25.107  1.00 14.07 ? 17  TYR A OH  1 
ATOM   164  N N   . ARG A 1 18  ? -19.179 11.671 25.520  1.00 15.89 ? 18  ARG A N   1 
ATOM   165  C CA  . ARG A 1 18  ? -18.353 10.572 26.015  1.00 16.10 ? 18  ARG A CA  1 
ATOM   166  C C   . ARG A 1 18  ? -17.158 10.377 25.090  1.00 16.98 ? 18  ARG A C   1 
ATOM   167  O O   . ARG A 1 18  ? -17.310 9.896  23.961  1.00 17.95 ? 18  ARG A O   1 
ATOM   168  C CB  . ARG A 1 18  ? -19.185 9.301  26.106  1.00 15.22 ? 18  ARG A CB  1 
ATOM   169  C CG  . ARG A 1 18  ? -18.492 8.143  26.795  1.00 19.56 ? 18  ARG A CG  1 
ATOM   170  C CD  . ARG A 1 18  ? -19.335 6.879  26.645  1.00 23.84 ? 18  ARG A CD  1 
ATOM   171  N NE  . ARG A 1 18  ? -18.792 5.756  27.401  1.00 24.66 ? 18  ARG A NE  1 
ATOM   172  C CZ  . ARG A 1 18  ? -17.809 4.974  26.977  1.00 25.97 ? 18  ARG A CZ  1 
ATOM   173  N NH1 . ARG A 1 18  ? -17.250 5.189  25.794  1.00 23.60 ? 18  ARG A NH1 1 
ATOM   174  N NH2 . ARG A 1 18  ? -17.376 3.972  27.737  1.00 35.69 ? 18  ARG A NH2 1 
ATOM   175  N N   . GLU A 1 19  ? -15.966 10.723 25.580  1.00 15.89 ? 19  GLU A N   1 
ATOM   176  C CA  . GLU A 1 19  ? -14.752 10.566 24.788  1.00 17.69 ? 19  GLU A CA  1 
ATOM   177  C C   . GLU A 1 19  ? -14.458 9.079  24.604  1.00 22.59 ? 19  GLU A C   1 
ATOM   178  O O   . GLU A 1 19  ? -14.485 8.322  25.581  1.00 23.70 ? 19  GLU A O   1 
ATOM   179  C CB  . GLU A 1 19  ? -13.578 11.264 25.489  1.00 20.56 ? 19  GLU A CB  1 
ATOM   180  C CG  . GLU A 1 19  ? -12.454 11.715 24.550  1.00 24.07 ? 19  GLU A CG  1 
ATOM   181  C CD  . GLU A 1 19  ? -11.337 10.701 24.461  1.00 30.25 ? 19  GLU A CD  1 
ATOM   182  O OE1 . GLU A 1 19  ? -11.430 9.650  25.126  1.00 31.49 ? 19  GLU A OE1 1 
ATOM   183  O OE2 . GLU A 1 19  ? -10.358 10.960 23.733  1.00 41.62 ? 19  GLU A OE2 1 
ATOM   184  N N   . PRO A 1 20  ? -14.174 8.622  23.381  1.00 22.44 ? 20  PRO A N   1 
ATOM   185  C CA  . PRO A 1 20  ? -14.152 7.174  23.125  1.00 27.65 ? 20  PRO A CA  1 
ATOM   186  C C   . PRO A 1 20  ? -12.944 6.436  23.674  1.00 31.37 ? 20  PRO A C   1 
ATOM   187  O O   . PRO A 1 20  ? -13.020 5.209  23.827  1.00 35.91 ? 20  PRO A O   1 
ATOM   188  C CB  . PRO A 1 20  ? -14.187 7.088  21.591  1.00 27.29 ? 20  PRO A CB  1 
ATOM   189  C CG  . PRO A 1 20  ? -13.628 8.394  21.127  1.00 20.45 ? 20  PRO A CG  1 
ATOM   190  C CD  . PRO A 1 20  ? -14.077 9.412  22.142  1.00 20.01 ? 20  PRO A CD  1 
ATOM   191  N N   . TYR A 1 21  ? -11.832 7.118  23.965  1.00 24.45 ? 21  TYR A N   1 
ATOM   192  C CA  . TYR A 1 21  ? -10.648 6.417  24.444  1.00 24.74 ? 21  TYR A CA  1 
ATOM   193  C C   . TYR A 1 21  ? -10.620 6.310  25.960  1.00 33.88 ? 21  TYR A C   1 
ATOM   194  O O   . TYR A 1 21  ? -10.186 5.289  26.500  1.00 37.33 ? 21  TYR A O   1 
ATOM   195  C CB  . TYR A 1 21  ? -9.385  7.113  23.930  1.00 22.61 ? 21  TYR A CB  1 
ATOM   196  C CG  . TYR A 1 21  ? -9.243  6.973  22.443  1.00 29.62 ? 21  TYR A CG  1 
ATOM   197  C CD1 . TYR A 1 21  ? -8.654  5.848  21.890  1.00 25.01 ? 21  TYR A CD1 1 
ATOM   198  C CD2 . TYR A 1 21  ? -9.747  7.940  21.582  1.00 32.01 ? 21  TYR A CD2 1 
ATOM   199  C CE1 . TYR A 1 21  ? -8.536  5.697  20.525  1.00 28.39 ? 21  TYR A CE1 1 
ATOM   200  C CE2 . TYR A 1 21  ? -9.635  7.794  20.207  1.00 24.54 ? 21  TYR A CE2 1 
ATOM   201  C CZ  . TYR A 1 21  ? -9.032  6.669  19.692  1.00 26.19 ? 21  TYR A CZ  1 
ATOM   202  O OH  . TYR A 1 21  ? -8.907  6.514  18.331  1.00 28.57 ? 21  TYR A OH  1 
ATOM   203  N N   . THR A 1 22  ? -11.102 7.335  26.659  1.00 28.06 ? 22  THR A N   1 
ATOM   204  C CA  . THR A 1 22  ? -11.150 7.311  28.115  1.00 30.06 ? 22  THR A CA  1 
ATOM   205  C C   . THR A 1 22  ? -12.512 6.911  28.661  1.00 28.10 ? 22  THR A C   1 
ATOM   206  O O   . THR A 1 22  ? -12.605 6.542  29.838  1.00 28.00 ? 22  THR A O   1 
ATOM   207  C CB  . THR A 1 22  ? -10.778 8.685  28.684  1.00 25.02 ? 22  THR A CB  1 
ATOM   208  O OG1 . THR A 1 22  ? -11.791 9.635  28.310  1.00 25.59 ? 22  THR A OG1 1 
ATOM   209  C CG2 . THR A 1 22  ? -9.417  9.139  28.158  1.00 29.92 ? 22  THR A CG2 1 
ATOM   210  N N   . GLY A 1 23  ? -13.564 6.971  27.846  1.00 24.29 ? 23  GLY A N   1 
ATOM   211  C CA  . GLY A 1 23  ? -14.904 6.716  28.321  1.00 24.88 ? 23  GLY A CA  1 
ATOM   212  C C   . GLY A 1 23  ? -15.492 7.826  29.157  1.00 26.32 ? 23  GLY A C   1 
ATOM   213  O O   . GLY A 1 23  ? -16.602 7.664  29.681  1.00 33.49 ? 23  GLY A O   1 
ATOM   214  N N   . GLU A 1 24  ? -14.806 8.955  29.277  1.00 20.97 ? 24  GLU A N   1 
ATOM   215  C CA  . GLU A 1 24  ? -15.240 10.016 30.173  1.00 20.69 ? 24  GLU A CA  1 
ATOM   216  C C   . GLU A 1 24  ? -16.153 11.009 29.465  1.00 18.63 ? 24  GLU A C   1 
ATOM   217  O O   . GLU A 1 24  ? -15.901 11.408 28.324  1.00 19.20 ? 24  GLU A O   1 
ATOM   218  C CB  . GLU A 1 24  ? -14.023 10.738 30.751  1.00 25.19 ? 24  GLU A CB  1 
ATOM   219  C CG  . GLU A 1 24  ? -13.294 9.900  31.779  1.00 30.88 ? 24  GLU A CG  1 
ATOM   220  C CD  . GLU A 1 24  ? -11.849 10.305 31.952  1.00 42.27 ? 24  GLU A CD  1 
ATOM   221  O OE1 . GLU A 1 24  ? -11.071 9.493  32.495  1.00 51.06 ? 24  GLU A OE1 1 
ATOM   222  O OE2 . GLU A 1 24  ? -11.487 11.425 31.537  1.00 38.96 ? 24  GLU A OE2 1 
ATOM   223  N N   . TYR A 1 25  ? -17.215 11.405 30.159  1.00 15.83 ? 25  TYR A N   1 
ATOM   224  C CA  . TYR A 1 25  ? -18.075 12.490 29.702  1.00 15.69 ? 25  TYR A CA  1 
ATOM   225  C C   . TYR A 1 25  ? -17.356 13.794 30.007  1.00 16.94 ? 25  TYR A C   1 
ATOM   226  O O   . TYR A 1 25  ? -17.158 14.145 31.178  1.00 16.85 ? 25  TYR A O   1 
ATOM   227  C CB  . TYR A 1 25  ? -19.436 12.418 30.385  1.00 16.82 ? 25  TYR A CB  1 
ATOM   228  C CG  . TYR A 1 25  ? -20.368 11.421 29.741  1.00 14.28 ? 25  TYR A CG  1 
ATOM   229  C CD1 . TYR A 1 25  ? -20.191 10.052 29.916  1.00 17.22 ? 25  TYR A CD1 1 
ATOM   230  C CD2 . TYR A 1 25  ? -21.425 11.852 28.949  1.00 14.71 ? 25  TYR A CD2 1 
ATOM   231  C CE1 . TYR A 1 25  ? -21.050 9.140  29.319  1.00 22.05 ? 25  TYR A CE1 1 
ATOM   232  C CE2 . TYR A 1 25  ? -22.288 10.954 28.353  1.00 20.08 ? 25  TYR A CE2 1 
ATOM   233  C CZ  . TYR A 1 25  ? -22.096 9.604  28.533  1.00 18.92 ? 25  TYR A CZ  1 
ATOM   234  O OH  . TYR A 1 25  ? -22.976 8.729  27.927  1.00 22.47 ? 25  TYR A OH  1 
ATOM   235  N N   . LEU A 1 26  ? -16.931 14.498 28.958  1.00 18.28 ? 26  LEU A N   1 
ATOM   236  C CA  . LEU A 1 26  ? -16.038 15.636 29.134  1.00 18.75 ? 26  LEU A CA  1 
ATOM   237  C C   . LEU A 1 26  ? -16.770 16.934 29.443  1.00 17.41 ? 26  LEU A C   1 
ATOM   238  O O   . LEU A 1 26  ? -16.128 17.897 29.868  1.00 19.58 ? 26  LEU A O   1 
ATOM   239  C CB  . LEU A 1 26  ? -15.160 15.811 27.887  1.00 17.97 ? 26  LEU A CB  1 
ATOM   240  C CG  . LEU A 1 26  ? -14.237 14.637 27.568  1.00 20.35 ? 26  LEU A CG  1 
ATOM   241  C CD1 . LEU A 1 26  ? -13.302 14.975 26.406  1.00 23.30 ? 26  LEU A CD1 1 
ATOM   242  C CD2 . LEU A 1 26  ? -13.436 14.217 28.794  1.00 21.01 ? 26  LEU A CD2 1 
ATOM   243  N N   . LEU A 1 27  ? -18.079 16.994 29.208  1.00 14.34 ? 27  LEU A N   1 
ATOM   244  C CA  . LEU A 1 27  ? -18.913 18.094 29.666  1.00 16.23 ? 27  LEU A CA  1 
ATOM   245  C C   . LEU A 1 27  ? -20.129 17.528 30.386  1.00 15.35 ? 27  LEU A C   1 
ATOM   246  O O   . LEU A 1 27  ? -20.566 16.411 30.086  1.00 14.83 ? 27  LEU A O   1 
ATOM   247  C CB  . LEU A 1 27  ? -19.371 18.980 28.497  1.00 16.60 ? 27  LEU A CB  1 
ATOM   248  C CG  . LEU A 1 27  ? -18.231 19.822 27.905  1.00 18.39 ? 27  LEU A CG  1 
ATOM   249  C CD1 . LEU A 1 27  ? -18.655 20.420 26.556  1.00 17.72 ? 27  LEU A CD1 1 
ATOM   250  C CD2 . LEU A 1 27  ? -17.783 20.907 28.870  1.00 24.69 ? 27  LEU A CD2 1 
ATOM   251  N N   . PRO A 1 28  ? -20.676 18.261 31.355  1.00 17.01 ? 28  PRO A N   1 
ATOM   252  C CA  . PRO A 1 28  ? -21.819 17.769 32.144  1.00 15.82 ? 28  PRO A CA  1 
ATOM   253  C C   . PRO A 1 28  ? -23.186 18.134 31.588  1.00 15.13 ? 28  PRO A C   1 
ATOM   254  O O   . PRO A 1 28  ? -24.182 17.983 32.301  1.00 13.89 ? 28  PRO A O   1 
ATOM   255  C CB  . PRO A 1 28  ? -21.608 18.480 33.485  1.00 15.52 ? 28  PRO A CB  1 
ATOM   256  C CG  . PRO A 1 28  ? -21.071 19.804 33.083  1.00 14.19 ? 28  PRO A CG  1 
ATOM   257  C CD  . PRO A 1 28  ? -20.156 19.534 31.891  1.00 15.80 ? 28  PRO A CD  1 
ATOM   258  N N   . TRP A 1 29  ? -23.258 18.643 30.363  1.00 12.28 ? 29  TRP A N   1 
ATOM   259  C CA  . TRP A 1 29  ? -24.503 19.243 29.902  1.00 12.37 ? 29  TRP A CA  1 
ATOM   260  C C   . TRP A 1 29  ? -25.650 18.239 29.785  1.00 12.02 ? 29  TRP A C   1 
ATOM   261  O O   . TRP A 1 29  ? -26.817 18.614 29.961  1.00 13.74 ? 29  TRP A O   1 
ATOM   262  C CB  . TRP A 1 29  ? -24.270 19.919 28.559  1.00 14.02 ? 29  TRP A CB  1 
ATOM   263  C CG  . TRP A 1 29  ? -23.323 21.122 28.543  1.00 12.29 ? 29  TRP A CG  1 
ATOM   264  C CD1 . TRP A 1 29  ? -22.275 21.307 27.688  1.00 11.89 ? 29  TRP A CD1 1 
ATOM   265  C CD2 . TRP A 1 29  ? -23.388 22.323 29.355  1.00 13.21 ? 29  TRP A CD2 1 
ATOM   266  N NE1 . TRP A 1 29  ? -21.684 22.525 27.912  1.00 14.10 ? 29  TRP A NE1 1 
ATOM   267  C CE2 . TRP A 1 29  ? -22.348 23.169 28.923  1.00 16.07 ? 29  TRP A CE2 1 
ATOM   268  C CE3 . TRP A 1 29  ? -24.244 22.770 30.369  1.00 13.63 ? 29  TRP A CE3 1 
ATOM   269  C CZ2 . TRP A 1 29  ? -22.124 24.431 29.483  1.00 18.12 ? 29  TRP A CZ2 1 
ATOM   270  C CZ3 . TRP A 1 29  ? -24.015 24.027 30.931  1.00 13.88 ? 29  TRP A CZ3 1 
ATOM   271  C CH2 . TRP A 1 29  ? -22.970 24.839 30.481  1.00 18.88 ? 29  TRP A CH2 1 
ATOM   272  N N   . THR A 1 30  ? -25.367 16.977 29.445  1.00 12.20 ? 30  THR A N   1 
ATOM   273  C CA  . THR A 1 30  ? -26.460 16.007 29.419  1.00 11.85 ? 30  THR A CA  1 
ATOM   274  C C   . THR A 1 30  ? -26.990 15.773 30.819  1.00 12.32 ? 30  THR A C   1 
ATOM   275  O O   . THR A 1 30  ? -28.204 15.695 31.036  1.00 14.23 ? 30  THR A O   1 
ATOM   276  C CB  . THR A 1 30  ? -26.006 14.695 28.792  1.00 17.07 ? 30  THR A CB  1 
ATOM   277  O OG1 . THR A 1 30  ? -25.661 14.944 27.424  1.00 14.55 ? 30  THR A OG1 1 
ATOM   278  C CG2 . THR A 1 30  ? -27.122 13.639 28.862  1.00 16.31 ? 30  THR A CG2 1 
ATOM   279  N N   . PHE A 1 31  ? -26.092 15.680 31.792  1.00 12.75 ? 31  PHE A N   1 
ATOM   280  C CA  . PHE A 1 31  ? -26.539 15.506 33.164  1.00 13.32 ? 31  PHE A CA  1 
ATOM   281  C C   . PHE A 1 31  ? -27.391 16.684 33.607  1.00 11.32 ? 31  PHE A C   1 
ATOM   282  O O   . PHE A 1 31  ? -28.473 16.505 34.179  1.00 12.08 ? 31  PHE A O   1 
ATOM   283  C CB  . PHE A 1 31  ? -25.336 15.344 34.088  1.00 14.59 ? 31  PHE A CB  1 
ATOM   284  C CG  . PHE A 1 31  ? -25.705 15.305 35.547  1.00 14.74 ? 31  PHE A CG  1 
ATOM   285  C CD1 . PHE A 1 31  ? -26.138 14.122 36.133  1.00 15.04 ? 31  PHE A CD1 1 
ATOM   286  C CD2 . PHE A 1 31  ? -25.634 16.453 36.328  1.00 13.99 ? 31  PHE A CD2 1 
ATOM   287  C CE1 . PHE A 1 31  ? -26.487 14.073 37.479  1.00 15.17 ? 31  PHE A CE1 1 
ATOM   288  C CE2 . PHE A 1 31  ? -25.972 16.418 37.674  1.00 16.67 ? 31  PHE A CE2 1 
ATOM   289  C CZ  . PHE A 1 31  ? -26.405 15.222 38.253  1.00 15.11 ? 31  PHE A CZ  1 
ATOM   290  N N   . PHE A 1 32  ? -26.920 17.907 33.355  1.00 12.73 ? 32  PHE A N   1 
ATOM   291  C CA  . PHE A 1 32  ? -27.644 19.053 33.893  1.00 12.41 ? 32  PHE A CA  1 
ATOM   292  C C   . PHE A 1 32  ? -28.970 19.259 33.180  1.00 12.87 ? 32  PHE A C   1 
ATOM   293  O O   . PHE A 1 32  ? -29.961 19.624 33.815  1.00 12.65 ? 32  PHE A O   1 
ATOM   294  C CB  . PHE A 1 32  ? -26.783 20.311 33.826  1.00 11.14 ? 32  PHE A CB  1 
ATOM   295  C CG  . PHE A 1 32  ? -25.750 20.384 34.913  1.00 13.97 ? 32  PHE A CG  1 
ATOM   296  C CD1 . PHE A 1 32  ? -26.119 20.216 36.238  1.00 12.21 ? 32  PHE A CD1 1 
ATOM   297  C CD2 . PHE A 1 32  ? -24.418 20.613 34.613  1.00 16.99 ? 32  PHE A CD2 1 
ATOM   298  C CE1 . PHE A 1 32  ? -25.166 20.272 37.255  1.00 15.35 ? 32  PHE A CE1 1 
ATOM   299  C CE2 . PHE A 1 32  ? -23.457 20.671 35.634  1.00 17.16 ? 32  PHE A CE2 1 
ATOM   300  C CZ  . PHE A 1 32  ? -23.837 20.504 36.940  1.00 15.25 ? 32  PHE A CZ  1 
ATOM   301  N N   . HIS A 1 33  ? -29.027 19.018 31.873  1.00 12.11 ? 33  HIS A N   1 
ATOM   302  C CA  . HIS A 1 33  ? -30.330 19.155 31.230  1.00 10.12 ? 33  HIS A CA  1 
ATOM   303  C C   . HIS A 1 33  ? -31.253 17.985 31.532  1.00 12.80 ? 33  HIS A C   1 
ATOM   304  O O   . HIS A 1 33  ? -32.475 18.160 31.485  1.00 12.12 ? 33  HIS A O   1 
ATOM   305  C CB  . HIS A 1 33  ? -30.172 19.373 29.723  1.00 11.40 ? 33  HIS A CB  1 
ATOM   306  C CG  . HIS A 1 33  ? -29.735 20.763 29.390  1.00 11.08 ? 33  HIS A CG  1 
ATOM   307  N ND1 . HIS A 1 33  ? -30.535 21.863 29.625  1.00 11.71 ? 33  HIS A ND1 1 
ATOM   308  C CD2 . HIS A 1 33  ? -28.553 21.245 28.929  1.00 11.86 ? 33  HIS A CD2 1 
ATOM   309  C CE1 . HIS A 1 33  ? -29.880 22.961 29.288  1.00 12.27 ? 33  HIS A CE1 1 
ATOM   310  N NE2 . HIS A 1 33  ? -28.672 22.615 28.867  1.00 13.96 ? 33  HIS A NE2 1 
ATOM   311  N N   . ALA A 1 34  ? -30.707 16.810 31.871  1.00 11.76 ? 34  ALA A N   1 
ATOM   312  C CA  . ALA A 1 34  ? -31.560 15.720 32.324  1.00 11.67 ? 34  ALA A CA  1 
ATOM   313  C C   . ALA A 1 34  ? -32.228 16.075 33.648  1.00 12.83 ? 34  ALA A C   1 
ATOM   314  O O   . ALA A 1 34  ? -33.442 15.917 33.803  1.00 13.19 ? 34  ALA A O   1 
ATOM   315  C CB  . ALA A 1 34  ? -30.751 14.422 32.448  1.00 14.26 ? 34  ALA A CB  1 
ATOM   316  N N   . VAL A 1 35  ? -31.452 16.578 34.617  1.00 12.92 ? 35  VAL A N   1 
ATOM   317  C CA  . VAL A 1 35  ? -32.054 16.842 35.919  1.00 12.07 ? 35  VAL A CA  1 
ATOM   318  C C   . VAL A 1 35  ? -32.962 18.060 35.864  1.00 12.64 ? 35  VAL A C   1 
ATOM   319  O O   . VAL A 1 35  ? -33.917 18.165 36.645  1.00 15.27 ? 35  VAL A O   1 
ATOM   320  C CB  . VAL A 1 35  ? -30.975 16.991 37.011  1.00 15.85 ? 35  VAL A CB  1 
ATOM   321  C CG1 . VAL A 1 35  ? -30.104 15.740 37.073  1.00 15.19 ? 35  VAL A CG1 1 
ATOM   322  C CG2 . VAL A 1 35  ? -30.113 18.263 36.816  1.00 14.94 ? 35  VAL A CG2 1 
ATOM   323  N N   . LYS A 1 36  ? -32.700 18.989 34.944  1.00 12.32 ? 36  LYS A N   1 
ATOM   324  C CA  . LYS A 1 36  ? -33.466 20.227 34.921  1.00 14.50 ? 36  LYS A CA  1 
ATOM   325  C C   . LYS A 1 36  ? -34.659 20.151 33.983  1.00 13.42 ? 36  LYS A C   1 
ATOM   326  O O   . LYS A 1 36  ? -35.739 20.639 34.328  1.00 12.79 ? 36  LYS A O   1 
ATOM   327  C CB  . LYS A 1 36  ? -32.569 21.404 34.527  1.00 12.81 ? 36  LYS A CB  1 
ATOM   328  C CG  . LYS A 1 36  ? -33.231 22.773 34.737  1.00 14.50 ? 36  LYS A CG  1 
ATOM   329  C CD  . LYS A 1 36  ? -32.264 23.948 34.543  1.00 13.21 ? 36  LYS A CD  1 
ATOM   330  C CE  . LYS A 1 36  ? -31.982 24.187 33.067  1.00 11.91 ? 36  LYS A CE  1 
ATOM   331  N NZ  . LYS A 1 36  ? -33.222 24.561 32.295  1.00 12.00 ? 36  LYS A NZ  1 
ATOM   332  N N   . ASP A 1 37  ? -34.489 19.532 32.817  1.00 11.05 ? 37  ASP A N   1 
ATOM   333  C CA  . ASP A 1 37  ? -35.470 19.647 31.735  1.00 10.64 ? 37  ASP A CA  1 
ATOM   334  C C   . ASP A 1 37  ? -36.019 18.329 31.211  1.00 11.21 ? 37  ASP A C   1 
ATOM   335  O O   . ASP A 1 37  ? -37.206 18.263 30.889  1.00 13.07 ? 37  ASP A O   1 
ATOM   336  C CB  . ASP A 1 37  ? -34.857 20.410 30.562  1.00 10.63 ? 37  ASP A CB  1 
ATOM   337  C CG  . ASP A 1 37  ? -34.213 21.696 31.003  1.00 13.32 ? 37  ASP A CG  1 
ATOM   338  O OD1 . ASP A 1 37  ? -34.957 22.555 31.533  1.00 13.23 ? 37  ASP A OD1 1 
ATOM   339  O OD2 . ASP A 1 37  ? -32.976 21.813 30.873  1.00 13.69 ? 37  ASP A OD2 1 
ATOM   340  N N   . TYR A 1 38  ? -35.208 17.280 31.054  1.00 11.89 ? 38  TYR A N   1 
ATOM   341  C CA  . TYR A 1 38  ? -35.700 16.177 30.224  1.00 11.80 ? 38  TYR A CA  1 
ATOM   342  C C   . TYR A 1 38  ? -36.790 15.364 30.916  1.00 13.30 ? 38  TYR A C   1 
ATOM   343  O O   . TYR A 1 38  ? -37.662 14.825 30.231  1.00 12.85 ? 38  TYR A O   1 
ATOM   344  C CB  . TYR A 1 38  ? -34.559 15.266 29.777  1.00 12.73 ? 38  TYR A CB  1 
ATOM   345  C CG  . TYR A 1 38  ? -33.581 15.947 28.845  1.00 12.71 ? 38  TYR A CG  1 
ATOM   346  C CD1 . TYR A 1 38  ? -34.011 16.874 27.914  1.00 10.91 ? 38  TYR A CD1 1 
ATOM   347  C CD2 . TYR A 1 38  ? -32.221 15.674 28.907  1.00 11.45 ? 38  TYR A CD2 1 
ATOM   348  C CE1 . TYR A 1 38  ? -33.115 17.518 27.073  1.00 11.20 ? 38  TYR A CE1 1 
ATOM   349  C CE2 . TYR A 1 38  ? -31.312 16.299 28.075  1.00 11.01 ? 38  TYR A CE2 1 
ATOM   350  C CZ  . TYR A 1 38  ? -31.757 17.235 27.162  1.00 10.50 ? 38  TYR A CZ  1 
ATOM   351  O OH  . TYR A 1 38  ? -30.855 17.856 26.327  1.00 11.35 ? 38  TYR A OH  1 
ATOM   352  N N   . TYR A 1 39  ? -36.767 15.259 32.248  1.00 13.26 ? 39  TYR A N   1 
ATOM   353  C CA  . TYR A 1 39  ? -37.897 14.672 32.965  1.00 12.74 ? 39  TYR A CA  1 
ATOM   354  C C   . TYR A 1 39  ? -39.019 15.686 33.141  1.00 13.66 ? 39  TYR A C   1 
ATOM   355  O O   . TYR A 1 39  ? -40.201 15.363 32.951  1.00 12.74 ? 39  TYR A O   1 
ATOM   356  C CB  . TYR A 1 39  ? -37.450 14.148 34.339  1.00 13.39 ? 39  TYR A CB  1 
ATOM   357  C CG  . TYR A 1 39  ? -38.597 13.645 35.181  1.00 11.81 ? 39  TYR A CG  1 
ATOM   358  C CD1 . TYR A 1 39  ? -39.056 12.341 35.046  1.00 13.81 ? 39  TYR A CD1 1 
ATOM   359  C CD2 . TYR A 1 39  ? -39.235 14.476 36.098  1.00 13.01 ? 39  TYR A CD2 1 
ATOM   360  C CE1 . TYR A 1 39  ? -40.116 11.883 35.799  1.00 17.29 ? 39  TYR A CE1 1 
ATOM   361  C CE2 . TYR A 1 39  ? -40.309 14.027 36.848  1.00 13.76 ? 39  TYR A CE2 1 
ATOM   362  C CZ  . TYR A 1 39  ? -40.741 12.724 36.696  1.00 19.01 ? 39  TYR A CZ  1 
ATOM   363  O OH  . TYR A 1 39  ? -41.796 12.240 37.448  1.00 21.36 ? 39  TYR A OH  1 
ATOM   364  N N   . ASP A 1 40  ? -38.656 16.919 33.476  1.00 12.27 ? 40  ASP A N   1 
ATOM   365  C CA  . ASP A 1 40  ? -39.657 17.876 33.919  1.00 9.32  ? 40  ASP A CA  1 
ATOM   366  C C   . ASP A 1 40  ? -40.525 18.394 32.775  1.00 13.33 ? 40  ASP A C   1 
ATOM   367  O O   . ASP A 1 40  ? -41.701 18.688 32.999  1.00 14.14 ? 40  ASP A O   1 
ATOM   368  C CB  . ASP A 1 40  ? -38.965 19.007 34.671  1.00 13.10 ? 40  ASP A CB  1 
ATOM   369  C CG  . ASP A 1 40  ? -38.733 18.631 36.101  1.00 13.82 ? 40  ASP A CG  1 
ATOM   370  O OD1 . ASP A 1 40  ? -39.733 18.549 36.824  1.00 15.29 ? 40  ASP A OD1 1 
ATOM   371  O OD2 . ASP A 1 40  ? -37.577 18.346 36.486  1.00 13.53 ? 40  ASP A OD2 1 
ATOM   372  N N   . MET A 1 41  ? -40.000 18.477 31.548  1.00 11.77 ? 41  MET A N   1 
ATOM   373  C CA  . MET A 1 41  ? -40.833 18.985 30.459  1.00 10.72 ? 41  MET A CA  1 
ATOM   374  C C   . MET A 1 41  ? -42.017 18.070 30.178  1.00 13.24 ? 41  MET A C   1 
ATOM   375  O O   . MET A 1 41  ? -43.158 18.561 30.186  1.00 12.76 ? 41  MET A O   1 
ATOM   376  C CB  . MET A 1 41  ? -39.968 19.248 29.215  1.00 13.33 ? 41  MET A CB  1 
ATOM   377  C CG  . MET A 1 41  ? -39.162 20.555 29.320  1.00 11.57 ? 41  MET A CG  1 
ATOM   378  S SD  . MET A 1 41  ? -40.190 22.062 29.311  1.00 11.90 ? 41  MET A SD  1 
ATOM   379  C CE  . MET A 1 41  ? -40.550 22.197 27.554  1.00 14.07 ? 41  MET A CE  1 
ATOM   380  N N   . PRO A 1 42  ? -41.850 16.755 29.964  1.00 12.21 ? 42  PRO A N   1 
ATOM   381  C CA  . PRO A 1 42  ? -43.049 15.909 29.855  1.00 12.66 ? 42  PRO A CA  1 
ATOM   382  C C   . PRO A 1 42  ? -43.831 15.808 31.163  1.00 10.63 ? 42  PRO A C   1 
ATOM   383  O O   . PRO A 1 42  ? -45.042 15.570 31.117  1.00 12.87 ? 42  PRO A O   1 
ATOM   384  C CB  . PRO A 1 42  ? -42.485 14.545 29.406  1.00 12.68 ? 42  PRO A CB  1 
ATOM   385  C CG  . PRO A 1 42  ? -41.040 14.559 29.881  1.00 12.15 ? 42  PRO A CG  1 
ATOM   386  C CD  . PRO A 1 42  ? -40.612 15.991 29.673  1.00 10.69 ? 42  PRO A CD  1 
ATOM   387  N N   . ALA A 1 43  ? -43.186 15.987 32.327  1.00 12.85 ? 43  ALA A N   1 
ATOM   388  C CA  . ALA A 1 43  ? -43.908 15.844 33.589  1.00 13.06 ? 43  ALA A CA  1 
ATOM   389  C C   . ALA A 1 43  ? -44.950 16.932 33.795  1.00 14.81 ? 43  ALA A C   1 
ATOM   390  O O   . ALA A 1 43  ? -45.874 16.735 34.589  1.00 15.64 ? 43  ALA A O   1 
ATOM   391  C CB  . ALA A 1 43  ? -42.940 15.812 34.784  1.00 15.09 ? 43  ALA A CB  1 
ATOM   392  N N   . TYR A 1 44  ? -44.874 18.051 33.068  1.00 13.58 ? 44  TYR A N   1 
ATOM   393  C CA  . TYR A 1 44  ? -45.980 19.006 33.125  1.00 14.64 ? 44  TYR A CA  1 
ATOM   394  C C   . TYR A 1 44  ? -47.314 18.352 32.753  1.00 13.94 ? 44  TYR A C   1 
ATOM   395  O O   . TYR A 1 44  ? -48.371 18.811 33.197  1.00 15.91 ? 44  TYR A O   1 
ATOM   396  C CB  . TYR A 1 44  ? -45.731 20.193 32.183  1.00 14.73 ? 44  TYR A CB  1 
ATOM   397  C CG  . TYR A 1 44  ? -44.799 21.270 32.720  1.00 12.79 ? 44  TYR A CG  1 
ATOM   398  C CD1 . TYR A 1 44  ? -45.284 22.341 33.467  1.00 14.27 ? 44  TYR A CD1 1 
ATOM   399  C CD2 . TYR A 1 44  ? -43.444 21.226 32.442  1.00 14.58 ? 44  TYR A CD2 1 
ATOM   400  C CE1 . TYR A 1 44  ? -44.437 23.329 33.937  1.00 12.67 ? 44  TYR A CE1 1 
ATOM   401  C CE2 . TYR A 1 44  ? -42.578 22.213 32.913  1.00 15.05 ? 44  TYR A CE2 1 
ATOM   402  C CZ  . TYR A 1 44  ? -43.085 23.268 33.650  1.00 13.59 ? 44  TYR A CZ  1 
ATOM   403  O OH  . TYR A 1 44  ? -42.236 24.248 34.124  1.00 16.11 ? 44  TYR A OH  1 
ATOM   404  N N   . LEU A 1 45  ? -47.295 17.289 31.942  1.00 14.47 ? 45  LEU A N   1 
ATOM   405  C CA  . LEU A 1 45  ? -48.543 16.669 31.510  1.00 14.58 ? 45  LEU A CA  1 
ATOM   406  C C   . LEU A 1 45  ? -49.269 15.965 32.655  1.00 15.64 ? 45  LEU A C   1 
ATOM   407  O O   . LEU A 1 45  ? -50.459 15.657 32.532  1.00 19.32 ? 45  LEU A O   1 
ATOM   408  C CB  . LEU A 1 45  ? -48.271 15.694 30.357  1.00 12.57 ? 45  LEU A CB  1 
ATOM   409  C CG  . LEU A 1 45  ? -47.831 16.365 29.051  1.00 13.24 ? 45  LEU A CG  1 
ATOM   410  C CD1 . LEU A 1 45  ? -47.230 15.340 28.090  1.00 15.56 ? 45  LEU A CD1 1 
ATOM   411  C CD2 . LEU A 1 45  ? -49.052 17.059 28.419  1.00 15.93 ? 45  LEU A CD2 1 
ATOM   412  N N   . LYS A 1 46  ? -48.588 15.715 33.777  1.00 16.69 ? 46  LYS A N   1 
ATOM   413  C CA  . LYS A 1 46  ? -49.285 15.171 34.934  1.00 20.70 ? 46  LYS A CA  1 
ATOM   414  C C   . LYS A 1 46  ? -50.229 16.183 35.565  1.00 17.16 ? 46  LYS A C   1 
ATOM   415  O O   . LYS A 1 46  ? -51.183 15.783 36.239  1.00 19.59 ? 46  LYS A O   1 
ATOM   416  C CB  . LYS A 1 46  ? -48.270 14.695 35.976  1.00 21.83 ? 46  LYS A CB  1 
ATOM   417  C CG  . LYS A 1 46  ? -47.378 13.587 35.448  1.00 25.17 ? 46  LYS A CG  1 
ATOM   418  C CD  . LYS A 1 46  ? -46.107 13.454 36.264  1.00 34.83 ? 46  LYS A CD  1 
ATOM   419  C CE  . LYS A 1 46  ? -46.331 12.639 37.514  1.00 43.20 ? 46  LYS A CE  1 
ATOM   420  N NZ  . LYS A 1 46  ? -45.050 12.457 38.252  1.00 49.13 ? 46  LYS A NZ  1 
ATOM   421  N N   . ASP A 1 47  ? -49.992 17.482 35.350  1.00 17.13 ? 47  ASP A N   1 
ATOM   422  C CA  . ASP A 1 47  ? -50.715 18.535 36.040  1.00 16.55 ? 47  ASP A CA  1 
ATOM   423  C C   . ASP A 1 47  ? -51.577 19.403 35.138  1.00 19.97 ? 47  ASP A C   1 
ATOM   424  O O   . ASP A 1 47  ? -52.391 20.176 35.658  1.00 22.11 ? 47  ASP A O   1 
ATOM   425  C CB  . ASP A 1 47  ? -49.728 19.439 36.791  1.00 18.53 ? 47  ASP A CB  1 
ATOM   426  C CG  . ASP A 1 47  ? -48.917 18.674 37.818  1.00 24.23 ? 47  ASP A CG  1 
ATOM   427  O OD1 . ASP A 1 47  ? -49.485 17.764 38.449  1.00 22.35 ? 47  ASP A OD1 1 
ATOM   428  O OD2 . ASP A 1 47  ? -47.718 18.969 37.979  1.00 24.85 ? 47  ASP A OD2 1 
ATOM   429  N N   . PHE A 1 48  ? -51.427 19.309 33.823  1.00 17.97 ? 48  PHE A N   1 
ATOM   430  C CA  . PHE A 1 48  ? -52.165 20.149 32.892  1.00 19.39 ? 48  PHE A CA  1 
ATOM   431  C C   . PHE A 1 48  ? -52.795 19.266 31.831  1.00 21.12 ? 48  PHE A C   1 
ATOM   432  O O   . PHE A 1 48  ? -52.140 18.367 31.293  1.00 21.54 ? 48  PHE A O   1 
ATOM   433  C CB  . PHE A 1 48  ? -51.244 21.215 32.286  1.00 20.18 ? 48  PHE A CB  1 
ATOM   434  C CG  . PHE A 1 48  ? -50.670 22.134 33.318  1.00 17.39 ? 48  PHE A CG  1 
ATOM   435  C CD1 . PHE A 1 48  ? -51.406 23.219 33.781  1.00 20.76 ? 48  PHE A CD1 1 
ATOM   436  C CD2 . PHE A 1 48  ? -49.415 21.893 33.868  1.00 16.40 ? 48  PHE A CD2 1 
ATOM   437  C CE1 . PHE A 1 48  ? -50.895 24.059 34.752  1.00 22.20 ? 48  PHE A CE1 1 
ATOM   438  C CE2 . PHE A 1 48  ? -48.900 22.734 34.849  1.00 19.01 ? 48  PHE A CE2 1 
ATOM   439  C CZ  . PHE A 1 48  ? -49.639 23.811 35.289  1.00 20.77 ? 48  PHE A CZ  1 
ATOM   440  N N   . GLU A 1 49  ? -54.074 19.519 31.554  1.00 19.88 ? 49  GLU A N   1 
ATOM   441  C CA  . GLU A 1 49  ? -54.864 18.694 30.640  1.00 21.35 ? 49  GLU A CA  1 
ATOM   442  C C   . GLU A 1 49  ? -54.761 19.237 29.216  1.00 21.75 ? 49  GLU A C   1 
ATOM   443  O O   . GLU A 1 49  ? -55.727 19.706 28.616  1.00 24.73 ? 49  GLU A O   1 
ATOM   444  C CB  . GLU A 1 49  ? -56.312 18.625 31.112  1.00 27.99 ? 49  GLU A CB  1 
ATOM   445  C CG  . GLU A 1 49  ? -56.509 17.862 32.418  1.00 40.42 ? 49  GLU A CG  1 
ATOM   446  C CD  . GLU A 1 49  ? -55.988 18.614 33.627  1.00 48.89 ? 49  GLU A CD  1 
ATOM   447  O OE1 . GLU A 1 49  ? -55.142 18.057 34.361  1.00 49.86 ? 49  GLU A OE1 1 
ATOM   448  O OE2 . GLU A 1 49  ? -56.414 19.768 33.838  1.00 50.18 ? 49  GLU A OE2 1 
ATOM   449  N N   . ILE A 1 50  ? -53.538 19.178 28.694  1.00 18.68 ? 50  ILE A N   1 
ATOM   450  C CA  . ILE A 1 50  ? -53.217 19.582 27.336  1.00 20.98 ? 50  ILE A CA  1 
ATOM   451  C C   . ILE A 1 50  ? -52.393 18.469 26.707  1.00 17.43 ? 50  ILE A C   1 
ATOM   452  O O   . ILE A 1 50  ? -52.036 17.486 27.361  1.00 18.19 ? 50  ILE A O   1 
ATOM   453  C CB  . ILE A 1 50  ? -52.451 20.919 27.293  1.00 18.39 ? 50  ILE A CB  1 
ATOM   454  C CG1 . ILE A 1 50  ? -51.139 20.795 28.064  1.00 20.16 ? 50  ILE A CG1 1 
ATOM   455  C CG2 . ILE A 1 50  ? -53.306 22.026 27.900  1.00 18.61 ? 50  ILE A CG2 1 
ATOM   456  C CD1 . ILE A 1 50  ? -50.303 22.042 28.010  1.00 22.25 ? 50  ILE A CD1 1 
ATOM   457  N N   . LYS A 1 51  ? -52.115 18.622 25.414  1.00 15.82 ? 51  LYS A N   1 
ATOM   458  C CA  . LYS A 1 51  ? -51.227 17.723 24.682  1.00 15.36 ? 51  LYS A CA  1 
ATOM   459  C C   . LYS A 1 51  ? -49.904 18.431 24.445  1.00 13.23 ? 51  LYS A C   1 
ATOM   460  O O   . LYS A 1 51  ? -49.888 19.601 24.053  1.00 14.26 ? 51  LYS A O   1 
ATOM   461  C CB  . LYS A 1 51  ? -51.827 17.295 23.337  1.00 15.10 ? 51  LYS A CB  1 
ATOM   462  C CG  . LYS A 1 51  ? -53.258 16.783 23.397  1.00 17.82 ? 51  LYS A CG  1 
ATOM   463  C CD  . LYS A 1 51  ? -53.383 15.531 24.258  1.00 18.26 ? 51  LYS A CD  1 
ATOM   464  C CE  . LYS A 1 51  ? -54.805 14.967 24.141  1.00 28.14 ? 51  LYS A CE  1 
ATOM   465  N NZ  . LYS A 1 51  ? -54.981 13.628 24.780  1.00 33.23 ? 51  LYS A NZ  1 
ATOM   466  N N   . LEU A 1 52  ? -48.793 17.729 24.681  1.00 13.18 ? 52  LEU A N   1 
ATOM   467  C CA  . LEU A 1 52  ? -47.478 18.269 24.350  1.00 12.22 ? 52  LEU A CA  1 
ATOM   468  C C   . LEU A 1 52  ? -46.658 17.176 23.688  1.00 12.00 ? 52  LEU A C   1 
ATOM   469  O O   . LEU A 1 52  ? -46.726 16.016 24.112  1.00 14.60 ? 52  LEU A O   1 
ATOM   470  C CB  . LEU A 1 52  ? -46.737 18.779 25.596  1.00 13.51 ? 52  LEU A CB  1 
ATOM   471  C CG  . LEU A 1 52  ? -47.360 19.905 26.413  1.00 11.43 ? 52  LEU A CG  1 
ATOM   472  C CD1 . LEU A 1 52  ? -46.630 20.042 27.757  1.00 14.40 ? 52  LEU A CD1 1 
ATOM   473  C CD2 . LEU A 1 52  ? -47.303 21.202 25.638  1.00 12.45 ? 52  LEU A CD2 1 
ATOM   474  N N   . ASN A 1 53  ? -45.886 17.532 22.659  1.00 10.76 ? 53  ASN A N   1 
ATOM   475  C CA  . ASN A 1 53  ? -45.099 16.538 21.944  1.00 11.98 ? 53  ASN A CA  1 
ATOM   476  C C   . ASN A 1 53  ? -43.611 16.787 22.135  1.00 10.68 ? 53  ASN A C   1 
ATOM   477  O O   . ASN A 1 53  ? -43.179 17.896 22.451  1.00 11.54 ? 53  ASN A O   1 
ATOM   478  C CB  . ASN A 1 53  ? -45.459 16.531 20.459  1.00 13.11 ? 53  ASN A CB  1 
ATOM   479  C CG  . ASN A 1 53  ? -46.941 16.455 20.258  1.00 14.34 ? 53  ASN A CG  1 
ATOM   480  O OD1 . ASN A 1 53  ? -47.536 15.406 20.438  1.00 13.41 ? 53  ASN A OD1 1 
ATOM   481  N ND2 . ASN A 1 53  ? -47.556 17.580 19.947  1.00 13.14 ? 53  ASN A ND2 1 
ATOM   482  N N   . PHE A 1 54  ? -42.826 15.724 21.930  1.00 11.60 ? 54  PHE A N   1 
ATOM   483  C CA  . PHE A 1 54  ? -41.401 15.750 22.232  1.00 10.29 ? 54  PHE A CA  1 
ATOM   484  C C   . PHE A 1 54  ? -40.609 15.032 21.154  1.00 12.73 ? 54  PHE A C   1 
ATOM   485  O O   . PHE A 1 54  ? -41.063 14.024 20.612  1.00 13.67 ? 54  PHE A O   1 
ATOM   486  C CB  . PHE A 1 54  ? -41.136 15.109 23.596  1.00 11.11 ? 54  PHE A CB  1 
ATOM   487  C CG  . PHE A 1 54  ? -41.863 15.793 24.699  1.00 13.52 ? 54  PHE A CG  1 
ATOM   488  C CD1 . PHE A 1 54  ? -41.294 16.899 25.331  1.00 12.13 ? 54  PHE A CD1 1 
ATOM   489  C CD2 . PHE A 1 54  ? -43.141 15.390 25.057  1.00 12.65 ? 54  PHE A CD2 1 
ATOM   490  C CE1 . PHE A 1 54  ? -41.971 17.563 26.320  1.00 12.56 ? 54  PHE A CE1 1 
ATOM   491  C CE2 . PHE A 1 54  ? -43.831 16.063 26.060  1.00 13.96 ? 54  PHE A CE2 1 
ATOM   492  C CZ  . PHE A 1 54  ? -43.239 17.146 26.686  1.00 14.55 ? 54  PHE A CZ  1 
ATOM   493  N N   . ASN A 1 55  ? -39.419 15.551 20.859  1.00 9.83  ? 55  ASN A N   1 
ATOM   494  C CA  . ASN A 1 55  ? -38.426 14.829 20.083  1.00 10.62 ? 55  ASN A CA  1 
ATOM   495  C C   . ASN A 1 55  ? -37.278 14.454 21.000  1.00 9.99  ? 55  ASN A C   1 
ATOM   496  O O   . ASN A 1 55  ? -36.831 15.275 21.789  1.00 12.70 ? 55  ASN A O   1 
ATOM   497  C CB  . ASN A 1 55  ? -37.883 15.683 18.938  1.00 10.42 ? 55  ASN A CB  1 
ATOM   498  C CG  . ASN A 1 55  ? -36.975 14.902 18.028  1.00 11.02 ? 55  ASN A CG  1 
ATOM   499  O OD1 . ASN A 1 55  ? -37.406 13.940 17.407  1.00 12.28 ? 55  ASN A OD1 1 
ATOM   500  N ND2 . ASN A 1 55  ? -35.711 15.299 17.946  1.00 11.00 ? 55  ASN A ND2 1 
ATOM   501  N N   . LEU A 1 56  ? -36.798 13.217 20.878  1.00 10.60 ? 56  LEU A N   1 
ATOM   502  C CA  . LEU A 1 56  ? -35.608 12.763 21.594  1.00 8.59  ? 56  LEU A CA  1 
ATOM   503  C C   . LEU A 1 56  ? -34.631 12.221 20.562  1.00 9.90  ? 56  LEU A C   1 
ATOM   504  O O   . LEU A 1 56  ? -34.964 11.273 19.840  1.00 12.86 ? 56  LEU A O   1 
ATOM   505  C CB  . LEU A 1 56  ? -35.951 11.668 22.617  1.00 13.17 ? 56  LEU A CB  1 
ATOM   506  C CG  . LEU A 1 56  ? -36.863 12.009 23.796  1.00 15.18 ? 56  LEU A CG  1 
ATOM   507  C CD1 . LEU A 1 56  ? -37.254 10.729 24.543  1.00 16.30 ? 56  LEU A CD1 1 
ATOM   508  C CD2 . LEU A 1 56  ? -36.154 12.975 24.729  1.00 22.79 ? 56  LEU A CD2 1 
ATOM   509  N N   . THR A 1 57  ? -33.413 12.795 20.501  1.00 12.70 ? 57  THR A N   1 
ATOM   510  C CA  . THR A 1 57  ? -32.488 12.179 19.559  1.00 12.08 ? 57  THR A CA  1 
ATOM   511  C C   . THR A 1 57  ? -31.926 10.883 20.147  1.00 11.32 ? 57  THR A C   1 
ATOM   512  O O   . THR A 1 57  ? -31.817 10.743 21.376  1.00 11.27 ? 57  THR A O   1 
ATOM   513  C CB  . THR A 1 57  ? -31.339 13.126 19.207  1.00 11.81 ? 57  THR A CB  1 
ATOM   514  O OG1 . THR A 1 57  ? -30.549 13.384 20.382  1.00 11.39 ? 57  THR A OG1 1 
ATOM   515  C CG2 . THR A 1 57  ? -31.884 14.445 18.656  1.00 11.99 ? 57  THR A CG2 1 
ATOM   516  N N   . PRO A 1 58  ? -31.593 9.908  19.299  1.00 12.64 ? 58  PRO A N   1 
ATOM   517  C CA  . PRO A 1 58  ? -31.062 8.644  19.837  1.00 11.01 ? 58  PRO A CA  1 
ATOM   518  C C   . PRO A 1 58  ? -29.769 8.819  20.599  1.00 11.68 ? 58  PRO A C   1 
ATOM   519  O O   . PRO A 1 58  ? -29.567 8.135  21.609  1.00 12.19 ? 58  PRO A O   1 
ATOM   520  C CB  . PRO A 1 58  ? -30.875 7.773  18.583  1.00 11.73 ? 58  PRO A CB  1 
ATOM   521  C CG  . PRO A 1 58  ? -31.883 8.337  17.576  1.00 11.16 ? 58  PRO A CG  1 
ATOM   522  C CD  . PRO A 1 58  ? -31.840 9.830  17.844  1.00 11.52 ? 58  PRO A CD  1 
ATOM   523  N N   . VAL A 1 59  ? -28.886 9.716  20.148  1.00 10.31 ? 59  VAL A N   1 
ATOM   524  C CA  . VAL A 1 59  ? -27.637 9.920  20.884  1.00 11.02 ? 59  VAL A CA  1 
ATOM   525  C C   . VAL A 1 59  ? -27.910 10.497 22.274  1.00 12.47 ? 59  VAL A C   1 
ATOM   526  O O   . VAL A 1 59  ? -27.201 10.163 23.231  1.00 12.19 ? 59  VAL A O   1 
ATOM   527  C CB  . VAL A 1 59  ? -26.659 10.790 20.067  1.00 10.72 ? 59  VAL A CB  1 
ATOM   528  C CG1 . VAL A 1 59  ? -27.253 12.157 19.737  1.00 13.90 ? 59  VAL A CG1 1 
ATOM   529  C CG2 . VAL A 1 59  ? -25.305 10.950 20.809  1.00 11.47 ? 59  VAL A CG2 1 
ATOM   530  N N   . LEU A 1 60  ? -28.925 11.351 22.426  1.00 11.46 ? 60  LEU A N   1 
ATOM   531  C CA  . LEU A 1 60  ? -29.338 11.776 23.765  1.00 11.44 ? 60  LEU A CA  1 
ATOM   532  C C   . LEU A 1 60  ? -29.865 10.595 24.582  1.00 13.16 ? 60  LEU A C   1 
ATOM   533  O O   . LEU A 1 60  ? -29.487 10.411 25.750  1.00 12.72 ? 60  LEU A O   1 
ATOM   534  C CB  . LEU A 1 60  ? -30.391 12.885 23.672  1.00 12.22 ? 60  LEU A CB  1 
ATOM   535  C CG  . LEU A 1 60  ? -31.009 13.257 25.033  1.00 11.10 ? 60  LEU A CG  1 
ATOM   536  C CD1 . LEU A 1 60  ? -29.935 13.692 26.036  1.00 12.97 ? 60  LEU A CD1 1 
ATOM   537  C CD2 . LEU A 1 60  ? -32.076 14.336 24.917  1.00 12.89 ? 60  LEU A CD2 1 
ATOM   538  N N   . ILE A 1 61  ? -30.749 9.784  23.986  1.00 11.25 ? 61  ILE A N   1 
ATOM   539  C CA  . ILE A 1 61  ? -31.283 8.616  24.690  1.00 11.22 ? 61  ILE A CA  1 
ATOM   540  C C   . ILE A 1 61  ? -30.154 7.733  25.220  1.00 11.30 ? 61  ILE A C   1 
ATOM   541  O O   . ILE A 1 61  ? -30.202 7.282  26.367  1.00 13.74 ? 61  ILE A O   1 
ATOM   542  C CB  . ILE A 1 61  ? -32.238 7.817  23.783  1.00 12.58 ? 61  ILE A CB  1 
ATOM   543  C CG1 . ILE A 1 61  ? -33.477 8.643  23.425  1.00 12.16 ? 61  ILE A CG1 1 
ATOM   544  C CG2 . ILE A 1 61  ? -32.650 6.504  24.463  1.00 16.30 ? 61  ILE A CG2 1 
ATOM   545  C CD1 . ILE A 1 61  ? -34.361 7.950  22.393  1.00 13.93 ? 61  ILE A CD1 1 
ATOM   546  N N   . ASP A 1 62  ? -29.125 7.465  24.390  1.00 10.44 ? 62  ASP A N   1 
ATOM   547  C CA  . ASP A 1 62  ? -27.991 6.640  24.831  1.00 12.50 ? 62  ASP A CA  1 
ATOM   548  C C   . ASP A 1 62  ? -27.357 7.201  26.095  1.00 13.56 ? 62  ASP A C   1 
ATOM   549  O O   . ASP A 1 62  ? -27.026 6.456  27.027  1.00 15.16 ? 62  ASP A O   1 
ATOM   550  C CB  . ASP A 1 62  ? -26.909 6.551  23.747  1.00 15.97 ? 62  ASP A CB  1 
ATOM   551  C CG  . ASP A 1 62  ? -27.271 5.624  22.610  1.00 18.31 ? 62  ASP A CG  1 
ATOM   552  O OD1 . ASP A 1 62  ? -28.105 4.719  22.812  1.00 20.50 ? 62  ASP A OD1 1 
ATOM   553  O OD2 . ASP A 1 62  ? -26.677 5.776  21.513  1.00 17.78 ? 62  ASP A OD2 1 
ATOM   554  N N   . GLN A 1 63  ? -27.164 8.517  26.136  1.00 13.54 ? 63  GLN A N   1 
ATOM   555  C CA  . GLN A 1 63  ? -26.504 9.123  27.286  1.00 11.79 ? 63  GLN A CA  1 
ATOM   556  C C   . GLN A 1 63  ? -27.389 9.087  28.527  1.00 13.66 ? 63  GLN A C   1 
ATOM   557  O O   . GLN A 1 63  ? -26.899 8.821  29.629  1.00 15.00 ? 63  GLN A O   1 
ATOM   558  C CB  . GLN A 1 63  ? -26.096 10.558 26.963  1.00 11.50 ? 63  GLN A CB  1 
ATOM   559  C CG  . GLN A 1 63  ? -25.094 10.649 25.832  1.00 13.21 ? 63  GLN A CG  1 
ATOM   560  C CD  . GLN A 1 63  ? -24.837 12.092 25.465  1.00 12.96 ? 63  GLN A CD  1 
ATOM   561  O OE1 . GLN A 1 63  ? -24.188 12.812 26.223  1.00 15.33 ? 63  GLN A OE1 1 
ATOM   562  N NE2 . GLN A 1 63  ? -25.362 12.532 24.324  1.00 11.96 ? 63  GLN A NE2 1 
ATOM   563  N N   . ILE A 1 64  ? -28.683 9.366  28.371  1.00 11.75 ? 64  ILE A N   1 
ATOM   564  C CA  . ILE A 1 64  ? -29.609 9.253  29.497  1.00 11.51 ? 64  ILE A CA  1 
ATOM   565  C C   . ILE A 1 64  ? -29.558 7.848  30.069  1.00 16.23 ? 64  ILE A C   1 
ATOM   566  O O   . ILE A 1 64  ? -29.519 7.659  31.287  1.00 15.87 ? 64  ILE A O   1 
ATOM   567  C CB  . ILE A 1 64  ? -31.038 9.628  29.061  1.00 11.22 ? 64  ILE A CB  1 
ATOM   568  C CG1 . ILE A 1 64  ? -31.122 11.122 28.754  1.00 13.44 ? 64  ILE A CG1 1 
ATOM   569  C CG2 . ILE A 1 64  ? -32.039 9.295  30.157  1.00 12.47 ? 64  ILE A CG2 1 
ATOM   570  C CD1 . ILE A 1 64  ? -32.491 11.542 28.202  1.00 14.97 ? 64  ILE A CD1 1 
ATOM   571  N N   . GLN A 1 65  ? -29.548 6.841  29.197  1.00 14.94 ? 65  GLN A N   1 
ATOM   572  C CA  . GLN A 1 65  ? -29.434 5.468  29.674  1.00 15.08 ? 65  GLN A CA  1 
ATOM   573  C C   . GLN A 1 65  ? -28.154 5.256  30.471  1.00 16.75 ? 65  GLN A C   1 
ATOM   574  O O   . GLN A 1 65  ? -28.184 4.628  31.529  1.00 17.99 ? 65  GLN A O   1 
ATOM   575  C CB  . GLN A 1 65  ? -29.503 4.486  28.504  1.00 17.44 ? 65  GLN A CB  1 
ATOM   576  C CG  . GLN A 1 65  ? -30.893 4.367  27.859  1.00 16.18 ? 65  GLN A CG  1 
ATOM   577  C CD  . GLN A 1 65  ? -30.907 3.365  26.719  1.00 20.58 ? 65  GLN A CD  1 
ATOM   578  O OE1 . GLN A 1 65  ? -30.104 3.465  25.792  1.00 20.32 ? 65  GLN A OE1 1 
ATOM   579  N NE2 . GLN A 1 65  ? -31.819 2.397  26.778  1.00 24.04 ? 65  GLN A NE2 1 
ATOM   580  N N   . GLU A 1 66  ? -27.020 5.769  29.988  1.00 15.52 ? 66  GLU A N   1 
ATOM   581  C CA  . GLU A 1 66  ? -25.760 5.532  30.697  1.00 15.55 ? 66  GLU A CA  1 
ATOM   582  C C   . GLU A 1 66  ? -25.755 6.211  32.061  1.00 15.65 ? 66  GLU A C   1 
ATOM   583  O O   . GLU A 1 66  ? -25.285 5.627  33.047  1.00 17.78 ? 66  GLU A O   1 
ATOM   584  C CB  . GLU A 1 66  ? -24.577 6.006  29.848  1.00 18.67 ? 66  GLU A CB  1 
ATOM   585  C CG  . GLU A 1 66  ? -23.197 5.703  30.450  1.00 26.21 ? 66  GLU A CG  1 
ATOM   586  C CD  . GLU A 1 66  ? -22.066 5.771  29.419  1.00 23.83 ? 66  GLU A CD  1 
ATOM   587  O OE1 . GLU A 1 66  ? -22.331 6.160  28.266  1.00 25.22 ? 66  GLU A OE1 1 
ATOM   588  O OE2 . GLU A 1 66  ? -20.905 5.428  29.764  1.00 34.77 ? 66  GLU A OE2 1 
ATOM   589  N N   . TYR A 1 67  ? -26.253 7.448  32.140  1.00 13.76 ? 67  TYR A N   1 
ATOM   590  C CA  . TYR A 1 67  ? -26.344 8.104  33.445  1.00 14.05 ? 67  TYR A CA  1 
ATOM   591  C C   . TYR A 1 67  ? -27.279 7.342  34.375  1.00 15.63 ? 67  TYR A C   1 
ATOM   592  O O   . TYR A 1 67  ? -26.983 7.173  35.566  1.00 19.54 ? 67  TYR A O   1 
ATOM   593  C CB  . TYR A 1 67  ? -26.806 9.552  33.295  1.00 15.33 ? 67  TYR A CB  1 
ATOM   594  C CG  . TYR A 1 67  ? -25.693 10.530 32.956  1.00 14.07 ? 67  TYR A CG  1 
ATOM   595  C CD1 . TYR A 1 67  ? -24.892 11.078 33.962  1.00 15.53 ? 67  TYR A CD1 1 
ATOM   596  C CD2 . TYR A 1 67  ? -25.449 10.907 31.638  1.00 13.35 ? 67  TYR A CD2 1 
ATOM   597  C CE1 . TYR A 1 67  ? -23.882 11.979 33.653  1.00 14.48 ? 67  TYR A CE1 1 
ATOM   598  C CE2 . TYR A 1 67  ? -24.451 11.808 31.324  1.00 14.18 ? 67  TYR A CE2 1 
ATOM   599  C CZ  . TYR A 1 67  ? -23.672 12.342 32.339  1.00 15.82 ? 67  TYR A CZ  1 
ATOM   600  O OH  . TYR A 1 67  ? -22.676 13.228 32.023  1.00 14.91 ? 67  TYR A OH  1 
ATOM   601  N N   . ALA A 1 68  ? -28.406 6.859  33.846  1.00 16.86 ? 68  ALA A N   1 
ATOM   602  C CA  . ALA A 1 68  ? -29.379 6.170  34.686  1.00 16.99 ? 68  ALA A CA  1 
ATOM   603  C C   . ALA A 1 68  ? -28.842 4.853  35.229  1.00 20.08 ? 68  ALA A C   1 
ATOM   604  O O   . ALA A 1 68  ? -29.260 4.421  36.312  1.00 22.75 ? 68  ALA A O   1 
ATOM   605  C CB  . ALA A 1 68  ? -30.670 5.928  33.903  1.00 17.97 ? 68  ALA A CB  1 
ATOM   606  N N   . GLN A 1 69  ? -27.930 4.205  34.509  1.00 17.29 ? 69  GLN A N   1 
ATOM   607  C CA  . GLN A 1 69  ? -27.323 2.961  34.968  1.00 20.14 ? 69  GLN A CA  1 
ATOM   608  C C   . GLN A 1 69  ? -26.130 3.197  35.873  1.00 23.51 ? 69  GLN A C   1 
ATOM   609  O O   . GLN A 1 69  ? -25.535 2.225  36.346  1.00 27.88 ? 69  GLN A O   1 
ATOM   610  C CB  . GLN A 1 69  ? -26.879 2.094  33.783  1.00 28.16 ? 69  GLN A CB  1 
ATOM   611  C CG  . GLN A 1 69  ? -27.794 2.182  32.601  1.00 45.75 ? 69  GLN A CG  1 
ATOM   612  C CD  . GLN A 1 69  ? -28.169 0.870  31.968  1.00 56.59 ? 69  GLN A CD  1 
ATOM   613  O OE1 . GLN A 1 69  ? -27.615 -0.178 32.285  1.00 63.12 ? 69  GLN A OE1 1 
ATOM   614  N NE2 . GLN A 1 69  ? -29.116 0.930  31.030  1.00 55.85 ? 69  GLN A NE2 1 
ATOM   615  N N   . GLY A 1 70  ? -25.767 4.452  36.133  1.00 22.34 ? 70  GLY A N   1 
ATOM   616  C CA  . GLY A 1 70  ? -24.599 4.719  36.951  1.00 21.91 ? 70  GLY A CA  1 
ATOM   617  C C   . GLY A 1 70  ? -23.282 4.489  36.244  1.00 29.96 ? 70  GLY A C   1 
ATOM   618  O O   . GLY A 1 70  ? -22.241 4.409  36.904  1.00 34.34 ? 70  GLY A O   1 
ATOM   619  N N   . LYS A 1 71  ? -23.302 4.389  34.912  1.00 26.47 ? 71  LYS A N   1 
ATOM   620  C CA  . LYS A 1 71  ? -22.132 4.070  34.104  1.00 30.59 ? 71  LYS A CA  1 
ATOM   621  C C   . LYS A 1 71  ? -21.407 5.294  33.556  1.00 27.64 ? 71  LYS A C   1 
ATOM   622  O O   . LYS A 1 71  ? -20.294 5.149  33.039  1.00 31.98 ? 71  LYS A O   1 
ATOM   623  C CB  . LYS A 1 71  ? -22.531 3.174  32.923  1.00 28.12 ? 71  LYS A CB  1 
ATOM   624  C CG  . LYS A 1 71  ? -22.857 1.743  33.303  1.00 40.58 ? 71  LYS A CG  1 
ATOM   625  C CD  . LYS A 1 71  ? -23.030 0.867  32.066  1.00 48.98 ? 71  LYS A CD  1 
ATOM   626  C CE  . LYS A 1 71  ? -21.696 0.283  31.612  1.00 56.13 ? 71  LYS A CE  1 
ATOM   627  N NZ  . LYS A 1 71  ? -21.846 -0.645 30.452  1.00 59.72 ? 71  LYS A NZ  1 
ATOM   628  N N   . ALA A 1 72  ? -21.998 6.483  33.647  1.00 21.11 ? 72  ALA A N   1 
ATOM   629  C CA  . ALA A 1 72  ? -21.412 7.669  33.038  1.00 20.36 ? 72  ALA A CA  1 
ATOM   630  C C   . ALA A 1 72  ? -20.321 8.227  33.943  1.00 22.38 ? 72  ALA A C   1 
ATOM   631  O O   . ALA A 1 72  ? -20.581 8.573  35.101  1.00 27.88 ? 72  ALA A O   1 
ATOM   632  C CB  . ALA A 1 72  ? -22.488 8.719  32.768  1.00 23.93 ? 72  ALA A CB  1 
ATOM   633  N N   . LYS A 1 73  ? -19.100 8.310  33.417  1.00 19.80 ? 73  LYS A N   1 
ATOM   634  C CA  . LYS A 1 73  ? -17.975 8.885  34.154  1.00 18.17 ? 73  LYS A CA  1 
ATOM   635  C C   . LYS A 1 73  ? -17.865 10.356 33.770  1.00 21.31 ? 73  LYS A C   1 
ATOM   636  O O   . LYS A 1 73  ? -17.182 10.723 32.815  1.00 23.77 ? 73  LYS A O   1 
ATOM   637  C CB  . LYS A 1 73  ? -16.686 8.132  33.851  1.00 22.08 ? 73  LYS A CB  1 
ATOM   638  C CG  . LYS A 1 73  ? -16.573 6.786  34.523  1.00 31.11 ? 73  LYS A CG  1 
ATOM   639  C CD  . LYS A 1 73  ? -15.157 6.236  34.385  1.00 43.18 ? 73  LYS A CD  1 
ATOM   640  C CE  . LYS A 1 73  ? -14.107 7.306  34.686  1.00 51.10 ? 73  LYS A CE  1 
ATOM   641  N NZ  . LYS A 1 73  ? -14.117 7.748  36.112  1.00 56.67 ? 73  LYS A NZ  1 
ATOM   642  N N   . ASP A 1 74  ? -18.536 11.209 34.534  1.00 20.33 ? 74  ASP A N   1 
ATOM   643  C CA  . ASP A 1 74  ? -18.675 12.625 34.213  1.00 17.50 ? 74  ASP A CA  1 
ATOM   644  C C   . ASP A 1 74  ? -17.639 13.407 35.019  1.00 16.77 ? 74  ASP A C   1 
ATOM   645  O O   . ASP A 1 74  ? -17.749 13.523 36.247  1.00 17.52 ? 74  ASP A O   1 
ATOM   646  C CB  . ASP A 1 74  ? -20.111 13.072 34.498  1.00 15.84 ? 74  ASP A CB  1 
ATOM   647  C CG  . ASP A 1 74  ? -20.373 14.523 34.146  1.00 17.69 ? 74  ASP A CG  1 
ATOM   648  O OD1 . ASP A 1 74  ? -19.521 15.400 34.431  1.00 17.83 ? 74  ASP A OD1 1 
ATOM   649  O OD2 . ASP A 1 74  ? -21.482 14.785 33.632  1.00 17.25 ? 74  ASP A OD2 1 
ATOM   650  N N   . VAL A 1 75  ? -16.642 13.952 34.319  1.00 18.12 ? 75  VAL A N   1 
ATOM   651  C CA  . VAL A 1 75  ? -15.476 14.548 34.977  1.00 18.79 ? 75  VAL A CA  1 
ATOM   652  C C   . VAL A 1 75  ? -15.884 15.756 35.812  1.00 19.27 ? 75  VAL A C   1 
ATOM   653  O O   . VAL A 1 75  ? -15.410 15.936 36.941  1.00 21.32 ? 75  VAL A O   1 
ATOM   654  C CB  . VAL A 1 75  ? -14.411 14.916 33.923  1.00 25.08 ? 75  VAL A CB  1 
ATOM   655  C CG1 . VAL A 1 75  ? -13.258 15.675 34.551  1.00 32.51 ? 75  VAL A CG1 1 
ATOM   656  C CG2 . VAL A 1 75  ? -13.921 13.665 33.207  1.00 28.08 ? 75  VAL A CG2 1 
ATOM   657  N N   . PHE A 1 76  ? -16.750 16.611 35.270  1.00 21.09 ? 76  PHE A N   1 
ATOM   658  C CA  . PHE A 1 76  ? -17.183 17.789 36.012  1.00 20.38 ? 76  PHE A CA  1 
ATOM   659  C C   . PHE A 1 76  ? -18.014 17.394 37.226  1.00 20.45 ? 76  PHE A C   1 
ATOM   660  O O   . PHE A 1 76  ? -17.853 17.959 38.318  1.00 19.96 ? 76  PHE A O   1 
ATOM   661  C CB  . PHE A 1 76  ? -17.975 18.713 35.083  1.00 20.09 ? 76  PHE A CB  1 
ATOM   662  C CG  . PHE A 1 76  ? -18.299 20.026 35.694  1.00 21.72 ? 76  PHE A CG  1 
ATOM   663  C CD1 . PHE A 1 76  ? -17.390 21.072 35.636  1.00 27.43 ? 76  PHE A CD1 1 
ATOM   664  C CD2 . PHE A 1 76  ? -19.503 20.218 36.352  1.00 22.52 ? 76  PHE A CD2 1 
ATOM   665  C CE1 . PHE A 1 76  ? -17.679 22.290 36.218  1.00 29.90 ? 76  PHE A CE1 1 
ATOM   666  C CE2 . PHE A 1 76  ? -19.801 21.437 36.938  1.00 26.50 ? 76  PHE A CE2 1 
ATOM   667  C CZ  . PHE A 1 76  ? -18.887 22.472 36.872  1.00 28.20 ? 76  PHE A CZ  1 
ATOM   668  N N   . LEU A 1 77  ? -18.873 16.392 37.065  1.00 19.10 ? 77  LEU A N   1 
ATOM   669  C CA  . LEU A 1 77  ? -19.712 15.952 38.170  1.00 18.81 ? 77  LEU A CA  1 
ATOM   670  C C   . LEU A 1 77  ? -18.882 15.314 39.275  1.00 23.83 ? 77  LEU A C   1 
ATOM   671  O O   . LEU A 1 77  ? -19.232 15.430 40.456  1.00 24.38 ? 77  LEU A O   1 
ATOM   672  C CB  . LEU A 1 77  ? -20.782 14.996 37.632  1.00 22.66 ? 77  LEU A CB  1 
ATOM   673  C CG  . LEU A 1 77  ? -21.971 14.681 38.537  1.00 25.16 ? 77  LEU A CG  1 
ATOM   674  C CD1 . LEU A 1 77  ? -22.618 15.957 39.073  1.00 24.49 ? 77  LEU A CD1 1 
ATOM   675  C CD2 . LEU A 1 77  ? -22.976 13.829 37.785  1.00 21.08 ? 77  LEU A CD2 1 
ATOM   676  N N   . GLU A 1 78  ? -17.769 14.660 38.922  1.00 21.56 ? 78  GLU A N   1 
ATOM   677  C CA  . GLU A 1 78  ? -16.907 14.067 39.943  1.00 26.55 ? 78  GLU A CA  1 
ATOM   678  C C   . GLU A 1 78  ? -16.234 15.136 40.796  1.00 27.94 ? 78  GLU A C   1 
ATOM   679  O O   . GLU A 1 78  ? -16.002 14.920 41.992  1.00 28.64 ? 78  GLU A O   1 
ATOM   680  C CB  . GLU A 1 78  ? -15.866 13.156 39.289  1.00 29.48 ? 78  GLU A CB  1 
ATOM   681  C CG  . GLU A 1 78  ? -15.289 12.115 40.240  1.00 39.20 ? 78  GLU A CG  1 
ATOM   682  C CD  . GLU A 1 78  ? -16.302 11.625 41.272  1.00 47.28 ? 78  GLU A CD  1 
ATOM   683  O OE1 . GLU A 1 78  ? -16.095 11.886 42.479  1.00 49.14 ? 78  GLU A OE1 1 
ATOM   684  O OE2 . GLU A 1 78  ? -17.301 10.979 40.884  1.00 50.41 ? 78  GLU A OE2 1 
ATOM   685  N N   . ALA A 1 79  ? -15.924 16.291 40.209  1.00 22.49 ? 79  ALA A N   1 
ATOM   686  C CA  . ALA A 1 79  ? -15.397 17.400 40.992  1.00 29.87 ? 79  ALA A CA  1 
ATOM   687  C C   . ALA A 1 79  ? -16.454 17.981 41.924  1.00 22.54 ? 79  ALA A C   1 
ATOM   688  O O   . ALA A 1 79  ? -16.119 18.435 43.022  1.00 27.54 ? 79  ALA A O   1 
ATOM   689  C CB  . ALA A 1 79  ? -14.851 18.483 40.069  1.00 27.52 ? 79  ALA A CB  1 
ATOM   690  N N   . ILE A 1 80  ? -17.724 17.990 41.502  1.00 20.13 ? 80  ILE A N   1 
ATOM   691  C CA  . ILE A 1 80  ? -18.798 18.430 42.389  1.00 18.96 ? 80  ILE A CA  1 
ATOM   692  C C   . ILE A 1 80  ? -18.952 17.477 43.563  1.00 21.62 ? 80  ILE A C   1 
ATOM   693  O O   . ILE A 1 80  ? -19.108 17.902 44.713  1.00 23.19 ? 80  ILE A O   1 
ATOM   694  C CB  . ILE A 1 80  ? -20.114 18.551 41.605  1.00 19.22 ? 80  ILE A CB  1 
ATOM   695  C CG1 . ILE A 1 80  ? -20.034 19.715 40.628  1.00 23.61 ? 80  ILE A CG1 1 
ATOM   696  C CG2 . ILE A 1 80  ? -21.290 18.696 42.575  1.00 22.02 ? 80  ILE A CG2 1 
ATOM   697  C CD1 . ILE A 1 80  ? -20.000 21.052 41.269  1.00 30.76 ? 80  ILE A CD1 1 
ATOM   698  N N   . ARG A 1 81  ? -18.909 16.174 43.291  1.00 22.99 ? 81  ARG A N   1 
ATOM   699  C CA  . ARG A 1 81  ? -19.158 15.176 44.324  1.00 21.92 ? 81  ARG A CA  1 
ATOM   700  C C   . ARG A 1 81  ? -18.076 15.188 45.405  1.00 24.78 ? 81  ARG A C   1 
ATOM   701  O O   . ARG A 1 81  ? -18.379 15.021 46.596  1.00 29.52 ? 81  ARG A O   1 
ATOM   702  C CB  . ARG A 1 81  ? -19.277 13.805 43.647  1.00 24.38 ? 81  ARG A CB  1 
ATOM   703  C CG  . ARG A 1 81  ? -19.276 12.628 44.581  1.00 36.31 ? 81  ARG A CG  1 
ATOM   704  C CD  . ARG A 1 81  ? -19.370 11.356 43.835  1.00 41.48 ? 81  ARG A CD  1 
ATOM   705  N NE  . ARG A 1 81  ? -20.635 11.197 43.151  1.00 48.49 ? 81  ARG A NE  1 
ATOM   706  C CZ  . ARG A 1 81  ? -21.806 11.003 43.825  1.00 55.35 ? 81  ARG A CZ  1 
ATOM   707  N NH1 . ARG A 1 81  ? -21.914 10.960 45.166  1.00 53.51 ? 81  ARG A NH1 1 
ATOM   708  N NH2 . ARG A 1 81  ? -22.895 10.855 43.073  1.00 48.49 ? 81  ARG A NH2 1 
ATOM   709  N N   . LYS A 1 82  ? -16.814 15.388 45.007  1.00 23.35 ? 82  LYS A N   1 
ATOM   710  C CA  . LYS A 1 82  ? -15.662 15.279 45.900  1.00 27.22 ? 82  LYS A CA  1 
ATOM   711  C C   . LYS A 1 82  ? -15.804 16.170 47.127  1.00 20.99 ? 82  LYS A C   1 
ATOM   712  O O   . LYS A 1 82  ? -16.381 17.255 47.068  1.00 23.04 ? 82  LYS A O   1 
ATOM   713  C CB  . LYS A 1 82  ? -14.382 15.703 45.168  1.00 25.12 ? 82  LYS A CB  1 
ATOM   714  C CG  . LYS A 1 82  ? -13.615 14.637 44.435  1.00 32.92 ? 82  LYS A CG  1 
ATOM   715  C CD  . LYS A 1 82  ? -12.478 15.319 43.687  1.00 31.58 ? 82  LYS A CD  1 
ATOM   716  C CE  . LYS A 1 82  ? -11.614 14.347 42.925  1.00 43.37 ? 82  LYS A CE  1 
ATOM   717  N NZ  . LYS A 1 82  ? -10.353 15.022 42.528  1.00 38.87 ? 82  LYS A NZ  1 
ATOM   718  N N   . ASP A 1 83  ? -15.215 15.732 48.238  1.00 22.27 ? 83  ASP A N   1 
ATOM   719  C CA  . ASP A 1 83  ? -14.965 16.674 49.314  1.00 25.83 ? 83  ASP A CA  1 
ATOM   720  C C   . ASP A 1 83  ? -14.041 17.770 48.789  1.00 25.10 ? 83  ASP A C   1 
ATOM   721  O O   . ASP A 1 83  ? -13.088 17.471 48.057  1.00 22.31 ? 83  ASP A O   1 
ATOM   722  C CB  . ASP A 1 83  ? -14.333 15.973 50.519  1.00 30.83 ? 83  ASP A CB  1 
ATOM   723  C CG  . ASP A 1 83  ? -14.290 16.860 51.748  1.00 35.42 ? 83  ASP A CG  1 
ATOM   724  O OD1 . ASP A 1 83  ? -13.487 17.815 51.755  1.00 31.12 ? 83  ASP A OD1 1 
ATOM   725  O OD2 . ASP A 1 83  ? -15.062 16.603 52.702  1.00 41.79 ? 83  ASP A OD2 1 
ATOM   726  N N   . PRO A 1 84  ? -14.304 19.043 49.100  1.00 23.50 ? 84  PRO A N   1 
ATOM   727  C CA  . PRO A 1 84  ? -13.465 20.114 48.536  1.00 23.87 ? 84  PRO A CA  1 
ATOM   728  C C   . PRO A 1 84  ? -12.001 19.985 48.905  1.00 27.40 ? 84  PRO A C   1 
ATOM   729  O O   . PRO A 1 84  ? -11.140 20.483 48.170  1.00 27.35 ? 84  PRO A O   1 
ATOM   730  C CB  . PRO A 1 84  ? -14.082 21.390 49.124  1.00 28.18 ? 84  PRO A CB  1 
ATOM   731  C CG  . PRO A 1 84  ? -15.486 21.015 49.448  1.00 27.04 ? 84  PRO A CG  1 
ATOM   732  C CD  . PRO A 1 84  ? -15.435 19.579 49.877  1.00 27.95 ? 84  PRO A CD  1 
ATOM   733  N N   . ASP A 1 85  ? -11.694 19.332 50.028  1.00 26.63 ? 85  ASP A N   1 
ATOM   734  C CA  . ASP A 1 85  ? -10.302 19.107 50.403  1.00 25.37 ? 85  ASP A CA  1 
ATOM   735  C C   . ASP A 1 85  ? -9.553  18.273 49.375  1.00 28.49 ? 85  ASP A C   1 
ATOM   736  O O   . ASP A 1 85  ? -8.318  18.311 49.342  1.00 31.03 ? 85  ASP A O   1 
ATOM   737  C CB  . ASP A 1 85  ? -10.213 18.406 51.763  1.00 28.72 ? 85  ASP A CB  1 
ATOM   738  C CG  . ASP A 1 85  ? -10.473 19.345 52.928  1.00 35.73 ? 85  ASP A CG  1 
ATOM   739  O OD1 . ASP A 1 85  ? -10.465 20.577 52.716  1.00 40.98 ? 85  ASP A OD1 1 
ATOM   740  O OD2 . ASP A 1 85  ? -10.667 18.845 54.058  1.00 42.07 ? 85  ASP A OD2 1 
ATOM   741  N N   . ASP A 1 86  ? -10.268 17.513 48.550  1.00 26.73 ? 86  ASP A N   1 
ATOM   742  C CA  . ASP A 1 86  ? -9.656  16.661 47.546  1.00 30.63 ? 86  ASP A CA  1 
ATOM   743  C C   . ASP A 1 86  ? -9.667  17.282 46.158  1.00 29.00 ? 86  ASP A C   1 
ATOM   744  O O   . ASP A 1 86  ? -9.237  16.630 45.204  1.00 28.51 ? 86  ASP A O   1 
ATOM   745  C CB  . ASP A 1 86  ? -10.364 15.306 47.511  1.00 29.59 ? 86  ASP A CB  1 
ATOM   746  C CG  . ASP A 1 86  ? -10.327 14.599 48.851  1.00 39.32 ? 86  ASP A CG  1 
ATOM   747  O OD1 . ASP A 1 86  ? -9.347  14.794 49.603  1.00 41.09 ? 86  ASP A OD1 1 
ATOM   748  O OD2 . ASP A 1 86  ? -11.278 13.849 49.153  1.00 47.18 ? 86  ASP A OD2 1 
ATOM   749  N N   . LEU A 1 87  ? -10.139 18.520 46.024  1.00 22.91 ? 87  LEU A N   1 
ATOM   750  C CA  . LEU A 1 87  ? -10.196 19.162 44.717  1.00 22.10 ? 87  LEU A CA  1 
ATOM   751  C C   . LEU A 1 87  ? -8.805  19.567 44.248  1.00 23.32 ? 87  LEU A C   1 
ATOM   752  O O   . LEU A 1 87  ? -8.052  20.212 44.989  1.00 24.91 ? 87  LEU A O   1 
ATOM   753  C CB  . LEU A 1 87  ? -11.088 20.396 44.771  1.00 23.25 ? 87  LEU A CB  1 
ATOM   754  C CG  . LEU A 1 87  ? -12.593 20.145 44.781  1.00 20.84 ? 87  LEU A CG  1 
ATOM   755  C CD1 . LEU A 1 87  ? -13.327 21.430 45.124  1.00 24.81 ? 87  LEU A CD1 1 
ATOM   756  C CD2 . LEU A 1 87  ? -13.063 19.583 43.440  1.00 21.27 ? 87  LEU A CD2 1 
ATOM   757  N N   . GLU A 1 88  ? -8.465  19.190 43.018  1.00 23.25 ? 88  GLU A N   1 
ATOM   758  C CA  . GLU A 1 88  ? -7.273  19.725 42.379  1.00 24.28 ? 88  GLU A CA  1 
ATOM   759  C C   . GLU A 1 88  ? -7.496  21.184 42.010  1.00 23.74 ? 88  GLU A C   1 
ATOM   760  O O   . GLU A 1 88  ? -8.630  21.616 41.781  1.00 22.41 ? 88  GLU A O   1 
ATOM   761  C CB  . GLU A 1 88  ? -6.933  18.928 41.115  1.00 25.11 ? 88  GLU A CB  1 
ATOM   762  C CG  . GLU A 1 88  ? -6.706  17.454 41.369  1.00 31.87 ? 88  GLU A CG  1 
ATOM   763  C CD  . GLU A 1 88  ? -6.720  16.648 40.095  1.00 37.67 ? 88  GLU A CD  1 
ATOM   764  O OE1 . GLU A 1 88  ? -7.256  17.147 39.088  1.00 41.48 ? 88  GLU A OE1 1 
ATOM   765  O OE2 . GLU A 1 88  ? -6.198  15.518 40.106  1.00 48.73 ? 88  GLU A OE2 1 
ATOM   766  N N   . LYS A 1 89  ? -6.396  21.944 41.930  1.00 25.00 ? 89  LYS A N   1 
ATOM   767  C CA  . LYS A 1 89  ? -6.493  23.318 41.440  1.00 24.89 ? 89  LYS A CA  1 
ATOM   768  C C   . LYS A 1 89  ? -7.224  23.387 40.105  1.00 25.27 ? 89  LYS A C   1 
ATOM   769  O O   . LYS A 1 89  ? -8.060  24.271 39.899  1.00 23.92 ? 89  LYS A O   1 
ATOM   770  C CB  . LYS A 1 89  ? -5.108  23.942 41.289  1.00 26.78 ? 89  LYS A CB  1 
ATOM   771  C CG  . LYS A 1 89  ? -4.420  24.258 42.595  1.00 33.63 ? 89  LYS A CG  1 
ATOM   772  C CD  . LYS A 1 89  ? -3.060  24.883 42.330  1.00 36.32 ? 89  LYS A CD  1 
ATOM   773  C CE  . LYS A 1 89  ? -2.419  25.380 43.612  1.00 36.47 ? 89  LYS A CE  1 
ATOM   774  N NZ  . LYS A 1 89  ? -1.249  26.256 43.324  1.00 39.53 ? 89  LYS A NZ  1 
ATOM   775  N N   . GLU A 1 90  ? -6.903  22.469 39.184  1.00 24.27 ? 90  GLU A N   1 
ATOM   776  C CA  . GLU A 1 90  ? -7.584  22.414 37.889  1.00 23.57 ? 90  GLU A CA  1 
ATOM   777  C C   . GLU A 1 90  ? -9.091  22.269 38.061  1.00 23.59 ? 90  GLU A C   1 
ATOM   778  O O   . GLU A 1 90  ? -9.875  22.862 37.304  1.00 22.43 ? 90  GLU A O   1 
ATOM   779  C CB  . GLU A 1 90  ? -7.043  21.241 37.064  1.00 24.45 ? 90  GLU A CB  1 
ATOM   780  C CG  . GLU A 1 90  ? -5.674  21.444 36.466  1.00 51.15 ? 90  GLU A CG  1 
ATOM   781  C CD  . GLU A 1 90  ? -5.153  20.206 35.748  1.00 56.75 ? 90  GLU A CD  1 
ATOM   782  O OE1 . GLU A 1 90  ? -5.924  19.234 35.598  1.00 55.65 ? 90  GLU A OE1 1 
ATOM   783  O OE2 . GLU A 1 90  ? -3.969  20.204 35.337  1.00 58.35 ? 90  GLU A OE2 1 
ATOM   784  N N   . GLU A 1 91  ? -9.512  21.458 39.033  1.00 21.32 ? 91  GLU A N   1 
ATOM   785  C CA  . GLU A 1 91  ? -10.938 21.224 39.236  1.00 20.43 ? 91  GLU A CA  1 
ATOM   786  C C   . GLU A 1 91  ? -11.612 22.447 39.836  1.00 20.83 ? 91  GLU A C   1 
ATOM   787  O O   . GLU A 1 91  ? -12.743 22.790 39.462  1.00 22.08 ? 91  GLU A O   1 
ATOM   788  C CB  . GLU A 1 91  ? -11.154 20.000 40.126  1.00 19.99 ? 91  GLU A CB  1 
ATOM   789  C CG  . GLU A 1 91  ? -10.699 18.689 39.501  1.00 20.80 ? 91  GLU A CG  1 
ATOM   790  C CD  . GLU A 1 91  ? -10.886 17.509 40.440  1.00 29.36 ? 91  GLU A CD  1 
ATOM   791  O OE1 . GLU A 1 91  ? -10.293 17.523 41.545  1.00 23.93 ? 91  GLU A OE1 1 
ATOM   792  O OE2 . GLU A 1 91  ? -11.634 16.572 40.078  1.00 29.42 ? 91  GLU A OE2 1 
ATOM   793  N N   . VAL A 1 92  ? -10.937 23.122 40.766  1.00 20.80 ? 92  VAL A N   1 
ATOM   794  C CA  . VAL A 1 92  ? -11.485 24.364 41.295  1.00 19.63 ? 92  VAL A CA  1 
ATOM   795  C C   . VAL A 1 92  ? -11.620 25.388 40.178  1.00 20.68 ? 92  VAL A C   1 
ATOM   796  O O   . VAL A 1 92  ? -12.627 26.103 40.088  1.00 22.22 ? 92  VAL A O   1 
ATOM   797  C CB  . VAL A 1 92  ? -10.602 24.886 42.441  1.00 22.10 ? 92  VAL A CB  1 
ATOM   798  C CG1 . VAL A 1 92  ? -11.101 26.234 42.912  1.00 27.99 ? 92  VAL A CG1 1 
ATOM   799  C CG2 . VAL A 1 92  ? -10.580 23.882 43.581  1.00 24.29 ? 92  VAL A CG2 1 
ATOM   800  N N   . GLU A 1 93  ? -10.620 25.457 39.294  1.00 20.45 ? 93  GLU A N   1 
ATOM   801  C CA  . GLU A 1 93  ? -10.682 26.412 38.193  1.00 22.96 ? 93  GLU A CA  1 
ATOM   802  C C   . GLU A 1 93  ? -11.846 26.112 37.258  1.00 25.43 ? 93  GLU A C   1 
ATOM   803  O O   . GLU A 1 93  ? -12.520 27.035 36.786  1.00 25.20 ? 93  GLU A O   1 
ATOM   804  C CB  . GLU A 1 93  ? -9.360  26.419 37.430  1.00 24.66 ? 93  GLU A CB  1 
ATOM   805  C CG  . GLU A 1 93  ? -8.240  27.115 38.200  1.00 29.67 ? 93  GLU A CG  1 
ATOM   806  C CD  . GLU A 1 93  ? -6.874  26.872 37.590  1.00 43.89 ? 93  GLU A CD  1 
ATOM   807  O OE1 . GLU A 1 93  ? -5.878  27.382 38.144  1.00 46.44 ? 93  GLU A OE1 1 
ATOM   808  O OE2 . GLU A 1 93  ? -6.798  26.171 36.558  1.00 44.61 ? 93  GLU A OE2 1 
ATOM   809  N N   . LYS A 1 94  ? -12.101 24.829 36.975  1.00 20.46 ? 94  LYS A N   1 
ATOM   810  C CA  . LYS A 1 94  ? -13.214 24.487 36.097  1.00 18.85 ? 94  LYS A CA  1 
ATOM   811  C C   . LYS A 1 94  ? -14.551 24.804 36.755  1.00 17.26 ? 94  LYS A C   1 
ATOM   812  O O   . LYS A 1 94  ? -15.505 25.208 36.077  1.00 19.66 ? 94  LYS A O   1 
ATOM   813  C CB  . LYS A 1 94  ? -13.151 23.010 35.695  1.00 23.58 ? 94  LYS A CB  1 
ATOM   814  C CG  . LYS A 1 94  ? -12.029 22.660 34.718  1.00 33.45 ? 94  LYS A CG  1 
ATOM   815  C CD  . LYS A 1 94  ? -12.320 21.342 34.005  1.00 43.47 ? 94  LYS A CD  1 
ATOM   816  C CE  . LYS A 1 94  ? -11.051 20.549 33.720  1.00 48.04 ? 94  LYS A CE  1 
ATOM   817  N NZ  . LYS A 1 94  ? -10.100 21.278 32.841  1.00 43.07 ? 94  LYS A NZ  1 
ATOM   818  N N   . LEU A 1 95  ? -14.645 24.617 38.073  1.00 17.57 ? 95  LEU A N   1 
ATOM   819  C CA  . LEU A 1 95  ? -15.875 24.945 38.785  1.00 17.33 ? 95  LEU A CA  1 
ATOM   820  C C   . LEU A 1 95  ? -16.150 26.445 38.758  1.00 21.83 ? 95  LEU A C   1 
ATOM   821  O O   . LEU A 1 95  ? -17.297 26.871 38.559  1.00 18.41 ? 95  LEU A O   1 
ATOM   822  C CB  . LEU A 1 95  ? -15.786 24.437 40.221  1.00 19.66 ? 95  LEU A CB  1 
ATOM   823  C CG  . LEU A 1 95  ? -17.022 24.537 41.104  1.00 31.79 ? 95  LEU A CG  1 
ATOM   824  C CD1 . LEU A 1 95  ? -18.255 24.053 40.347  1.00 35.85 ? 95  LEU A CD1 1 
ATOM   825  C CD2 . LEU A 1 95  ? -16.802 23.730 42.373  1.00 40.56 ? 95  LEU A CD2 1 
ATOM   826  N N   . ILE A 1 96  ? -15.112 27.263 38.944  1.00 20.70 ? 96  ILE A N   1 
ATOM   827  C CA  . ILE A 1 96  ? -15.284 28.711 38.879  1.00 20.05 ? 96  ILE A CA  1 
ATOM   828  C C   . ILE A 1 96  ? -15.617 29.141 37.455  1.00 23.90 ? 96  ILE A C   1 
ATOM   829  O O   . ILE A 1 96  ? -16.500 29.981 37.238  1.00 23.66 ? 96  ILE A O   1 
ATOM   830  C CB  . ILE A 1 96  ? -14.025 29.416 39.420  1.00 22.13 ? 96  ILE A CB  1 
ATOM   831  C CG1 . ILE A 1 96  ? -13.879 29.154 40.924  1.00 21.84 ? 96  ILE A CG1 1 
ATOM   832  C CG2 . ILE A 1 96  ? -14.086 30.913 39.146  1.00 26.98 ? 96  ILE A CG2 1 
ATOM   833  C CD1 . ILE A 1 96  ? -12.523 29.550 41.498  1.00 25.68 ? 96  ILE A CD1 1 
ATOM   834  N N   . GLU A 1 97  ? -14.935 28.557 36.461  1.00 21.88 ? 97  GLU A N   1 
ATOM   835  C CA  . GLU A 1 97  ? -15.209 28.889 35.064  1.00 23.10 ? 97  GLU A CA  1 
ATOM   836  C C   . GLU A 1 97  ? -16.644 28.552 34.691  1.00 20.72 ? 97  GLU A C   1 
ATOM   837  O O   . GLU A 1 97  ? -17.317 29.332 34.009  1.00 21.08 ? 97  GLU A O   1 
ATOM   838  C CB  . GLU A 1 97  ? -14.232 28.150 34.153  1.00 26.69 ? 97  GLU A CB  1 
ATOM   839  C CG  . GLU A 1 97  ? -14.483 28.341 32.673  1.00 44.98 ? 97  GLU A CG  1 
ATOM   840  C CD  . GLU A 1 97  ? -13.613 27.432 31.815  1.00 60.45 ? 97  GLU A CD  1 
ATOM   841  O OE1 . GLU A 1 97  ? -13.553 27.655 30.587  1.00 64.16 ? 97  GLU A OE1 1 
ATOM   842  O OE2 . GLU A 1 97  ? -12.992 26.496 32.368  1.00 60.57 ? 97  GLU A OE2 1 
ATOM   843  N N   . PHE A 1 98  ? -17.129 27.389 35.133  1.00 17.38 ? 98  PHE A N   1 
ATOM   844  C CA  . PHE A 1 98  ? -18.507 26.996 34.859  1.00 16.91 ? 98  PHE A CA  1 
ATOM   845  C C   . PHE A 1 98  ? -19.492 27.946 35.530  1.00 18.61 ? 98  PHE A C   1 
ATOM   846  O O   . PHE A 1 98  ? -20.509 28.324 34.933  1.00 17.14 ? 98  PHE A O   1 
ATOM   847  C CB  . PHE A 1 98  ? -18.722 25.562 35.343  1.00 16.99 ? 98  PHE A CB  1 
ATOM   848  C CG  . PHE A 1 98  ? -20.022 24.942 34.906  1.00 16.74 ? 98  PHE A CG  1 
ATOM   849  C CD1 . PHE A 1 98  ? -20.154 24.396 33.647  1.00 17.29 ? 98  PHE A CD1 1 
ATOM   850  C CD2 . PHE A 1 98  ? -21.080 24.837 35.795  1.00 17.66 ? 98  PHE A CD2 1 
ATOM   851  C CE1 . PHE A 1 98  ? -21.352 23.801 33.255  1.00 15.76 ? 98  PHE A CE1 1 
ATOM   852  C CE2 . PHE A 1 98  ? -22.274 24.248 35.418  1.00 18.76 ? 98  PHE A CE2 1 
ATOM   853  C CZ  . PHE A 1 98  ? -22.406 23.726 34.152  1.00 17.32 ? 98  PHE A CZ  1 
ATOM   854  N N   . THR A 1 99  ? -19.196 28.357 36.768  1.00 18.34 ? 99  THR A N   1 
ATOM   855  C CA  . THR A 1 99  ? -20.047 29.322 37.461  1.00 17.91 ? 99  THR A CA  1 
ATOM   856  C C   . THR A 1 99  ? -20.103 30.645 36.701  1.00 18.36 ? 99  THR A C   1 
ATOM   857  O O   . THR A 1 99  ? -21.179 31.216 36.497  1.00 19.81 ? 99  THR A O   1 
ATOM   858  C CB  . THR A 1 99  ? -19.535 29.554 38.889  1.00 18.77 ? 99  THR A CB  1 
ATOM   859  O OG1 . THR A 1 99  ? -19.448 28.304 39.576  1.00 17.39 ? 99  THR A OG1 1 
ATOM   860  C CG2 . THR A 1 99  ? -20.500 30.429 39.652  1.00 16.89 ? 99  THR A CG2 1 
ATOM   861  N N   . LYS A 1 100 ? -18.945 31.142 36.265  1.00 17.65 ? 100 LYS A N   1 
ATOM   862  C CA  . LYS A 1 100 ? -18.906 32.423 35.568  1.00 17.50 ? 100 LYS A CA  1 
ATOM   863  C C   . LYS A 1 100 ? -19.635 32.365 34.226  1.00 19.05 ? 100 LYS A C   1 
ATOM   864  O O   . LYS A 1 100 ? -20.238 33.361 33.811  1.00 20.85 ? 100 LYS A O   1 
ATOM   865  C CB  . LYS A 1 100 ? -17.460 32.862 35.375  1.00 22.42 ? 100 LYS A CB  1 
ATOM   866  C CG  . LYS A 1 100 ? -16.892 33.588 36.592  1.00 31.17 ? 100 LYS A CG  1 
ATOM   867  C CD  . LYS A 1 100 ? -15.407 33.885 36.441  1.00 34.26 ? 100 LYS A CD  1 
ATOM   868  C CE  . LYS A 1 100 ? -14.813 34.360 37.765  1.00 42.12 ? 100 LYS A CE  1 
ATOM   869  N NZ  . LYS A 1 100 ? -13.326 34.475 37.716  1.00 39.07 ? 100 LYS A NZ  1 
ATOM   870  N N   . LEU A 1 101 ? -19.587 31.221 33.540  1.00 17.53 ? 101 LEU A N   1 
ATOM   871  C CA  . LEU A 1 101 ? -20.322 31.076 32.286  1.00 17.95 ? 101 LEU A CA  1 
ATOM   872  C C   . LEU A 1 101 ? -21.819 31.232 32.511  1.00 19.55 ? 101 LEU A C   1 
ATOM   873  O O   . LEU A 1 101 ? -22.529 31.789 31.667  1.00 20.48 ? 101 LEU A O   1 
ATOM   874  C CB  . LEU A 1 101 ? -20.016 29.715 31.659  1.00 19.17 ? 101 LEU A CB  1 
ATOM   875  C CG  . LEU A 1 101 ? -20.774 29.348 30.381  1.00 22.49 ? 101 LEU A CG  1 
ATOM   876  C CD1 . LEU A 1 101 ? -20.368 30.288 29.268  1.00 20.93 ? 101 LEU A CD1 1 
ATOM   877  C CD2 . LEU A 1 101 ? -20.488 27.895 29.987  1.00 24.79 ? 101 LEU A CD2 1 
ATOM   878  N N   . ASN A 1 102 ? -22.315 30.753 33.648  1.00 18.38 ? 102 ASN A N   1 
ATOM   879  C CA  . ASN A 1 102 ? -23.741 30.698 33.928  1.00 16.01 ? 102 ASN A CA  1 
ATOM   880  C C   . ASN A 1 102 ? -24.205 31.818 34.847  1.00 18.30 ? 102 ASN A C   1 
ATOM   881  O O   . ASN A 1 102 ? -25.406 31.907 35.135  1.00 17.77 ? 102 ASN A O   1 
ATOM   882  C CB  . ASN A 1 102 ? -24.095 29.337 34.546  1.00 14.00 ? 102 ASN A CB  1 
ATOM   883  C CG  . ASN A 1 102 ? -23.890 28.195 33.581  1.00 18.49 ? 102 ASN A CG  1 
ATOM   884  O OD1 . ASN A 1 102 ? -24.527 28.152 32.537  1.00 20.27 ? 102 ASN A OD1 1 
ATOM   885  N ND2 . ASN A 1 102 ? -23.012 27.255 33.925  1.00 19.10 ? 102 ASN A ND2 1 
ATOM   886  N N   . TYR A 1 103 ? -23.277 32.696 35.258  1.00 18.47 ? 103 TYR A N   1 
ATOM   887  C CA  . TYR A 1 103 ? -23.468 33.596 36.393  1.00 23.40 ? 103 TYR A CA  1 
ATOM   888  C C   . TYR A 1 103 ? -24.666 34.526 36.217  1.00 21.50 ? 103 TYR A C   1 
ATOM   889  O O   . TYR A 1 103 ? -25.345 34.859 37.197  1.00 21.44 ? 103 TYR A O   1 
ATOM   890  C CB  . TYR A 1 103 ? -22.177 34.400 36.595  1.00 21.82 ? 103 TYR A CB  1 
ATOM   891  C CG  . TYR A 1 103 ? -22.191 35.422 37.708  1.00 25.87 ? 103 TYR A CG  1 
ATOM   892  C CD1 . TYR A 1 103 ? -21.772 35.081 38.988  1.00 26.20 ? 103 TYR A CD1 1 
ATOM   893  C CD2 . TYR A 1 103 ? -22.581 36.734 37.474  1.00 28.30 ? 103 TYR A CD2 1 
ATOM   894  C CE1 . TYR A 1 103 ? -21.766 36.017 40.011  1.00 30.65 ? 103 TYR A CE1 1 
ATOM   895  C CE2 . TYR A 1 103 ? -22.581 37.677 38.493  1.00 32.86 ? 103 TYR A CE2 1 
ATOM   896  C CZ  . TYR A 1 103 ? -22.173 37.311 39.754  1.00 36.08 ? 103 TYR A CZ  1 
ATOM   897  O OH  . TYR A 1 103 ? -22.170 38.241 40.767  1.00 39.07 ? 103 TYR A OH  1 
ATOM   898  N N   . GLU A 1 104 ? -24.923 34.984 34.992  1.00 19.32 ? 104 GLU A N   1 
ATOM   899  C CA  . GLU A 1 104 ? -25.979 35.964 34.759  1.00 23.10 ? 104 GLU A CA  1 
ATOM   900  C C   . GLU A 1 104 ? -27.341 35.345 34.504  1.00 18.89 ? 104 GLU A C   1 
ATOM   901  O O   . GLU A 1 104 ? -28.317 36.091 34.345  1.00 23.73 ? 104 GLU A O   1 
ATOM   902  C CB  . GLU A 1 104 ? -25.631 36.855 33.567  1.00 23.15 ? 104 GLU A CB  1 
ATOM   903  C CG  . GLU A 1 104 ? -24.338 37.600 33.719  1.00 32.60 ? 104 GLU A CG  1 
ATOM   904  C CD  . GLU A 1 104 ? -24.426 38.735 34.721  1.00 44.50 ? 104 GLU A CD  1 
ATOM   905  O OE1 . GLU A 1 104 ? -25.553 39.099 35.125  1.00 46.60 ? 104 GLU A OE1 1 
ATOM   906  O OE2 . GLU A 1 104 ? -23.363 39.270 35.096  1.00 42.23 ? 104 GLU A OE2 1 
ATOM   907  N N   . LYS A 1 105 ? -27.427 34.018 34.422  1.00 17.93 ? 105 LYS A N   1 
ATOM   908  C CA  . LYS A 1 105 ? -28.708 33.371 34.179  1.00 16.56 ? 105 LYS A CA  1 
ATOM   909  C C   . LYS A 1 105 ? -29.549 33.400 35.455  1.00 15.88 ? 105 LYS A C   1 
ATOM   910  O O   . LYS A 1 105 ? -29.009 33.258 36.552  1.00 17.00 ? 105 LYS A O   1 
ATOM   911  C CB  . LYS A 1 105 ? -28.498 31.928 33.716  1.00 15.60 ? 105 LYS A CB  1 
ATOM   912  C CG  . LYS A 1 105 ? -27.660 31.825 32.435  1.00 16.06 ? 105 LYS A CG  1 
ATOM   913  C CD  . LYS A 1 105 ? -27.263 30.400 32.101  1.00 15.17 ? 105 LYS A CD  1 
ATOM   914  C CE  . LYS A 1 105 ? -26.411 30.355 30.838  1.00 17.69 ? 105 LYS A CE  1 
ATOM   915  N NZ  . LYS A 1 105 ? -26.057 28.962 30.412  1.00 18.74 ? 105 LYS A NZ  1 
ATOM   916  N N   . PRO A 1 106 ? -30.862 33.618 35.350  1.00 16.28 ? 106 PRO A N   1 
ATOM   917  C CA  . PRO A 1 106 ? -31.680 33.699 36.571  1.00 16.68 ? 106 PRO A CA  1 
ATOM   918  C C   . PRO A 1 106 ? -31.657 32.433 37.414  1.00 17.37 ? 106 PRO A C   1 
ATOM   919  O O   . PRO A 1 106 ? -31.882 32.509 38.628  1.00 18.69 ? 106 PRO A O   1 
ATOM   920  C CB  . PRO A 1 106 ? -33.084 34.012 36.025  1.00 17.32 ? 106 PRO A CB  1 
ATOM   921  C CG  . PRO A 1 106 ? -32.796 34.779 34.757  1.00 17.97 ? 106 PRO A CG  1 
ATOM   922  C CD  . PRO A 1 106 ? -31.612 34.050 34.157  1.00 16.77 ? 106 PRO A CD  1 
ATOM   923  N N   . ILE A 1 107 ? -31.387 31.262 36.832  1.00 15.12 ? 107 ILE A N   1 
ATOM   924  C CA  . ILE A 1 107 ? -31.314 30.067 37.664  1.00 14.70 ? 107 ILE A CA  1 
ATOM   925  C C   . ILE A 1 107 ? -30.089 30.056 38.563  1.00 16.11 ? 107 ILE A C   1 
ATOM   926  O O   . ILE A 1 107 ? -30.019 29.223 39.472  1.00 15.95 ? 107 ILE A O   1 
ATOM   927  C CB  . ILE A 1 107 ? -31.350 28.773 36.822  1.00 14.76 ? 107 ILE A CB  1 
ATOM   928  C CG1 . ILE A 1 107 ? -30.182 28.711 35.828  1.00 14.52 ? 107 ILE A CG1 1 
ATOM   929  C CG2 . ILE A 1 107 ? -32.704 28.614 36.123  1.00 14.98 ? 107 ILE A CG2 1 
ATOM   930  C CD1 . ILE A 1 107 ? -29.997 27.285 35.233  1.00 15.70 ? 107 ILE A CD1 1 
ATOM   931  N N   . TYR A 1 108 ? -29.133 30.962 38.341  1.00 15.06 ? 108 TYR A N   1 
ATOM   932  C CA  . TYR A 1 108 ? -27.978 31.127 39.220  1.00 15.89 ? 108 TYR A CA  1 
ATOM   933  C C   . TYR A 1 108 ? -28.129 32.296 40.188  1.00 19.46 ? 108 TYR A C   1 
ATOM   934  O O   . TYR A 1 108 ? -27.137 32.725 40.787  1.00 18.29 ? 108 TYR A O   1 
ATOM   935  C CB  . TYR A 1 108 ? -26.699 31.295 38.392  1.00 16.83 ? 108 TYR A CB  1 
ATOM   936  C CG  . TYR A 1 108 ? -26.019 29.973 38.105  1.00 14.97 ? 108 TYR A CG  1 
ATOM   937  C CD1 . TYR A 1 108 ? -26.549 29.086 37.176  1.00 16.91 ? 108 TYR A CD1 1 
ATOM   938  C CD2 . TYR A 1 108 ? -24.864 29.603 38.778  1.00 17.40 ? 108 TYR A CD2 1 
ATOM   939  C CE1 . TYR A 1 108 ? -25.947 27.868 36.918  1.00 16.72 ? 108 TYR A CE1 1 
ATOM   940  C CE2 . TYR A 1 108 ? -24.248 28.393 38.528  1.00 16.23 ? 108 TYR A CE2 1 
ATOM   941  C CZ  . TYR A 1 108 ? -24.791 27.527 37.594  1.00 14.49 ? 108 TYR A CZ  1 
ATOM   942  O OH  . TYR A 1 108 ? -24.195 26.318 37.334  1.00 16.55 ? 108 TYR A OH  1 
ATOM   943  N N   . ARG A 1 109 ? -29.349 32.804 40.375  1.00 18.54 ? 109 ARG A N   1 
ATOM   944  C CA  . ARG A 1 109 ? -29.587 33.980 41.219  1.00 17.78 ? 109 ARG A CA  1 
ATOM   945  C C   . ARG A 1 109 ? -29.638 33.547 42.682  1.00 19.56 ? 109 ARG A C   1 
ATOM   946  O O   . ARG A 1 109 ? -30.699 33.423 43.303  1.00 22.79 ? 109 ARG A O   1 
ATOM   947  C CB  . ARG A 1 109 ? -30.864 34.698 40.802  1.00 22.18 ? 109 ARG A CB  1 
ATOM   948  C CG  . ARG A 1 109 ? -31.021 36.078 41.423  1.00 32.04 ? 109 ARG A CG  1 
ATOM   949  C CD  . ARG A 1 109 ? -32.100 36.871 40.690  1.00 42.13 ? 109 ARG A CD  1 
ATOM   950  N NE  . ARG A 1 109 ? -31.671 37.243 39.343  1.00 45.45 ? 109 ARG A NE  1 
ATOM   951  C CZ  . ARG A 1 109 ? -32.452 37.215 38.267  1.00 45.74 ? 109 ARG A CZ  1 
ATOM   952  N NH1 . ARG A 1 109 ? -33.718 36.831 38.367  1.00 48.31 ? 109 ARG A NH1 1 
ATOM   953  N NH2 . ARG A 1 109 ? -31.965 37.580 37.089  1.00 47.54 ? 109 ARG A NH2 1 
ATOM   954  N N   . PHE A 1 110 ? -28.448 33.322 43.234  1.00 18.52 ? 110 PHE A N   1 
ATOM   955  C CA  . PHE A 1 110 ? -28.233 33.077 44.653  1.00 20.86 ? 110 PHE A CA  1 
ATOM   956  C C   . PHE A 1 110 ? -27.238 34.113 45.139  1.00 19.81 ? 110 PHE A C   1 
ATOM   957  O O   . PHE A 1 110 ? -26.160 34.249 44.556  1.00 22.07 ? 110 PHE A O   1 
ATOM   958  C CB  . PHE A 1 110 ? -27.645 31.685 44.929  1.00 18.86 ? 110 PHE A CB  1 
ATOM   959  C CG  . PHE A 1 110 ? -28.516 30.546 44.517  1.00 17.16 ? 110 PHE A CG  1 
ATOM   960  C CD1 . PHE A 1 110 ? -29.476 30.032 45.381  1.00 20.68 ? 110 PHE A CD1 1 
ATOM   961  C CD2 . PHE A 1 110 ? -28.340 29.957 43.291  1.00 19.45 ? 110 PHE A CD2 1 
ATOM   962  C CE1 . PHE A 1 110 ? -30.258 28.954 45.002  1.00 21.13 ? 110 PHE A CE1 1 
ATOM   963  C CE2 . PHE A 1 110 ? -29.121 28.881 42.904  1.00 21.00 ? 110 PHE A CE2 1 
ATOM   964  C CZ  . PHE A 1 110 ? -30.078 28.384 43.762  1.00 18.34 ? 110 PHE A CZ  1 
ATOM   965  N N   . GLU A 1 111 ? -27.585 34.818 46.213  1.00 21.30 ? 111 GLU A N   1 
ATOM   966  C CA  . GLU A 1 111 ? -26.666 35.811 46.751  1.00 23.25 ? 111 GLU A CA  1 
ATOM   967  C C   . GLU A 1 111 ? -25.320 35.189 47.120  1.00 23.23 ? 111 GLU A C   1 
ATOM   968  O O   . GLU A 1 111 ? -24.279 35.838 46.966  1.00 26.20 ? 111 GLU A O   1 
ATOM   969  C CB  . GLU A 1 111 ? -27.332 36.501 47.941  1.00 25.87 ? 111 GLU A CB  1 
ATOM   970  C CG  . GLU A 1 111 ? -26.536 37.600 48.561  1.00 51.47 ? 111 GLU A CG  1 
ATOM   971  C CD  . GLU A 1 111 ? -26.078 38.655 47.580  1.00 60.93 ? 111 GLU A CD  1 
ATOM   972  O OE1 . GLU A 1 111 ? -26.828 38.998 46.635  1.00 63.21 ? 111 GLU A OE1 1 
ATOM   973  O OE2 . GLU A 1 111 ? -24.940 39.130 47.755  1.00 63.89 ? 111 GLU A OE2 1 
ATOM   974  N N   . ARG A 1 112 ? -25.308 33.920 47.550  1.00 24.43 ? 112 ARG A N   1 
ATOM   975  C CA  . ARG A 1 112 ? -24.046 33.282 47.933  1.00 25.04 ? 112 ARG A CA  1 
ATOM   976  C C   . ARG A 1 112 ? -23.127 33.073 46.730  1.00 24.68 ? 112 ARG A C   1 
ATOM   977  O O   . ARG A 1 112 ? -21.903 33.097 46.874  1.00 24.20 ? 112 ARG A O   1 
ATOM   978  C CB  . ARG A 1 112 ? -24.328 31.948 48.635  1.00 22.71 ? 112 ARG A CB  1 
ATOM   979  C CG  . ARG A 1 112 ? -23.098 31.158 49.067  1.00 20.76 ? 112 ARG A CG  1 
ATOM   980  C CD  . ARG A 1 112 ? -22.300 31.904 50.118  1.00 22.39 ? 112 ARG A CD  1 
ATOM   981  N NE  . ARG A 1 112 ? -21.467 30.977 50.874  1.00 23.58 ? 112 ARG A NE  1 
ATOM   982  C CZ  . ARG A 1 112 ? -20.428 31.342 51.622  1.00 29.34 ? 112 ARG A CZ  1 
ATOM   983  N NH1 . ARG A 1 112 ? -20.088 32.623 51.713  1.00 29.20 ? 112 ARG A NH1 1 
ATOM   984  N NH2 . ARG A 1 112 ? -19.731 30.424 52.282  1.00 29.40 ? 112 ARG A NH2 1 
ATOM   985  N N   . ILE A 1 113 ? -23.688 32.863 45.537  1.00 20.41 ? 113 ILE A N   1 
ATOM   986  C CA  . ILE A 1 113 ? -22.835 32.743 44.356  1.00 18.34 ? 113 ILE A CA  1 
ATOM   987  C C   . ILE A 1 113 ? -22.113 34.060 44.090  1.00 22.42 ? 113 ILE A C   1 
ATOM   988  O O   . ILE A 1 113 ? -20.927 34.073 43.747  1.00 24.80 ? 113 ILE A O   1 
ATOM   989  C CB  . ILE A 1 113 ? -23.667 32.287 43.142  1.00 20.70 ? 113 ILE A CB  1 
ATOM   990  C CG1 . ILE A 1 113 ? -23.944 30.788 43.234  1.00 22.56 ? 113 ILE A CG1 1 
ATOM   991  C CG2 . ILE A 1 113 ? -22.951 32.622 41.825  1.00 22.73 ? 113 ILE A CG2 1 
ATOM   992  C CD1 . ILE A 1 113 ? -25.050 30.322 42.335  1.00 29.51 ? 113 ILE A CD1 1 
ATOM   993  N N   . ARG A 1 114 ? -22.808 35.189 44.262  1.00 23.45 ? 114 ARG A N   1 
ATOM   994  C CA  . ARG A 1 114 ? -22.159 36.481 44.060  1.00 24.63 ? 114 ARG A CA  1 
ATOM   995  C C   . ARG A 1 114 ? -21.041 36.696 45.073  1.00 30.72 ? 114 ARG A C   1 
ATOM   996  O O   . ARG A 1 114 ? -19.977 37.224 44.733  1.00 29.95 ? 114 ARG A O   1 
ATOM   997  C CB  . ARG A 1 114 ? -23.191 37.608 44.142  1.00 31.10 ? 114 ARG A CB  1 
ATOM   998  C CG  . ARG A 1 114 ? -24.380 37.408 43.211  1.00 38.21 ? 114 ARG A CG  1 
ATOM   999  C CD  . ARG A 1 114 ? -25.246 38.657 43.107  1.00 48.58 ? 114 ARG A CD  1 
ATOM   1000 N NE  . ARG A 1 114 ? -26.329 38.676 44.089  1.00 55.04 ? 114 ARG A NE  1 
ATOM   1001 C CZ  . ARG A 1 114 ? -27.481 38.025 43.947  1.00 57.64 ? 114 ARG A CZ  1 
ATOM   1002 N NH1 . ARG A 1 114 ? -27.704 37.288 42.866  1.00 53.88 ? 114 ARG A NH1 1 
ATOM   1003 N NH2 . ARG A 1 114 ? -28.409 38.105 44.894  1.00 60.47 ? 114 ARG A NH2 1 
ATOM   1004 N N   . GLU A 1 115 ? -21.261 36.274 46.320  1.00 29.01 ? 115 GLU A N   1 
ATOM   1005 C CA  . GLU A 1 115 ? -20.211 36.351 47.333  1.00 27.15 ? 115 GLU A CA  1 
ATOM   1006 C C   . GLU A 1 115 ? -19.009 35.499 46.955  1.00 30.06 ? 115 GLU A C   1 
ATOM   1007 O O   . GLU A 1 115 ? -17.858 35.935 47.081  1.00 35.15 ? 115 GLU A O   1 
ATOM   1008 C CB  . GLU A 1 115 ? -20.748 35.895 48.684  1.00 29.36 ? 115 GLU A CB  1 
ATOM   1009 C CG  . GLU A 1 115 ? -21.783 36.786 49.293  1.00 37.02 ? 115 GLU A CG  1 
ATOM   1010 C CD  . GLU A 1 115 ? -22.380 36.169 50.543  1.00 46.59 ? 115 GLU A CD  1 
ATOM   1011 O OE1 . GLU A 1 115 ? -21.716 35.302 51.155  1.00 41.52 ? 115 GLU A OE1 1 
ATOM   1012 O OE2 . GLU A 1 115 ? -23.511 36.545 50.915  1.00 57.44 ? 115 GLU A OE2 1 
ATOM   1013 N N   . LEU A 1 116 ? -19.257 34.256 46.541  1.00 27.02 ? 116 LEU A N   1 
ATOM   1014 C CA  . LEU A 1 116 ? -18.158 33.339 46.259  1.00 27.45 ? 116 LEU A CA  1 
ATOM   1015 C C   . LEU A 1 116 ? -17.326 33.817 45.077  1.00 29.98 ? 116 LEU A C   1 
ATOM   1016 O O   . LEU A 1 116 ? -16.102 33.649 45.067  1.00 33.94 ? 116 LEU A O   1 
ATOM   1017 C CB  . LEU A 1 116 ? -18.705 31.935 45.992  1.00 25.63 ? 116 LEU A CB  1 
ATOM   1018 C CG  . LEU A 1 116 ? -19.395 31.265 47.190  1.00 24.06 ? 116 LEU A CG  1 
ATOM   1019 C CD1 . LEU A 1 116 ? -20.047 29.943 46.766  1.00 23.96 ? 116 LEU A CD1 1 
ATOM   1020 C CD2 . LEU A 1 116 ? -18.434 31.049 48.341  1.00 28.50 ? 116 LEU A CD2 1 
ATOM   1021 N N   . MET A 1 117 ? -17.970 34.404 44.063  1.00 29.57 ? 117 MET A N   1 
ATOM   1022 C CA  . MET A 1 117 ? -17.226 34.845 42.890  1.00 25.25 ? 117 MET A CA  1 
ATOM   1023 C C   . MET A 1 117 ? -16.459 36.140 43.124  1.00 33.43 ? 117 MET A C   1 
ATOM   1024 O O   . MET A 1 117 ? -15.585 36.475 42.316  1.00 39.98 ? 117 MET A O   1 
ATOM   1025 C CB  . MET A 1 117 ? -18.170 34.973 41.687  1.00 26.35 ? 117 MET A CB  1 
ATOM   1026 C CG  . MET A 1 117 ? -18.807 33.643 41.318  1.00 26.50 ? 117 MET A CG  1 
ATOM   1027 S SD  . MET A 1 117 ? -17.611 32.651 40.395  1.00 32.06 ? 117 MET A SD  1 
ATOM   1028 C CE  . MET A 1 117 ? -17.089 31.421 41.567  1.00 42.12 ? 117 MET A CE  1 
ATOM   1029 N N   . ASN A 1 118 ? -16.728 36.850 44.218  1.00 29.63 ? 118 ASN A N   1 
ATOM   1030 C CA  . ASN A 1 118 ? -15.992 38.053 44.575  1.00 35.64 ? 118 ASN A CA  1 
ATOM   1031 C C   . ASN A 1 118 ? -14.867 37.784 45.568  1.00 39.30 ? 118 ASN A C   1 
ATOM   1032 O O   . ASN A 1 118 ? -14.284 38.736 46.097  1.00 44.75 ? 118 ASN A O   1 
ATOM   1033 C CB  . ASN A 1 118 ? -16.942 39.104 45.157  1.00 43.29 ? 118 ASN A CB  1 
ATOM   1034 C CG  . ASN A 1 118 ? -17.824 39.738 44.105  1.00 54.58 ? 118 ASN A CG  1 
ATOM   1035 O OD1 . ASN A 1 118 ? -17.454 39.818 42.933  1.00 61.09 ? 118 ASN A OD1 1 
ATOM   1036 N ND2 . ASN A 1 118 ? -18.998 40.197 44.517  1.00 61.12 ? 118 ASN A ND2 1 
ATOM   1037 N N   . LYS A 1 119 ? -14.554 36.521 45.833  1.00 33.61 ? 119 LYS A N   1 
ATOM   1038 C CA  . LYS A 1 119 ? -13.555 36.155 46.825  1.00 33.03 ? 119 LYS A CA  1 
ATOM   1039 C C   . LYS A 1 119 ? -12.244 35.762 46.156  1.00 43.82 ? 119 LYS A C   1 
ATOM   1040 O O   . LYS A 1 119 ? -12.224 35.012 45.175  1.00 48.28 ? 119 LYS A O   1 
ATOM   1041 C CB  . LYS A 1 119 ? -14.056 35.010 47.707  1.00 36.26 ? 119 LYS A CB  1 
ATOM   1042 C CG  . LYS A 1 119 ? -15.084 35.446 48.736  1.00 42.06 ? 119 LYS A CG  1 
ATOM   1043 C CD  . LYS A 1 119 ? -15.241 34.412 49.834  1.00 47.14 ? 119 LYS A CD  1 
ATOM   1044 C CE  . LYS A 1 119 ? -16.528 34.628 50.612  1.00 43.51 ? 119 LYS A CE  1 
ATOM   1045 N NZ  . LYS A 1 119 ? -16.441 35.797 51.531  1.00 47.57 ? 119 LYS A NZ  1 
ATOM   1046 N N   . GLU A 1 120 ? -11.148 36.277 46.716  1.00 53.74 ? 120 GLU A N   1 
ATOM   1047 C CA  . GLU A 1 120 ? -9.811  35.979 46.214  1.00 56.80 ? 120 GLU A CA  1 
ATOM   1048 C C   . GLU A 1 120 ? -9.497  34.490 46.316  1.00 49.71 ? 120 GLU A C   1 
ATOM   1049 O O   . GLU A 1 120 ? -9.022  33.876 45.354  1.00 48.80 ? 120 GLU A O   1 
ATOM   1050 C CB  . GLU A 1 120 ? -8.780  36.817 46.980  1.00 62.55 ? 120 GLU A CB  1 
ATOM   1051 C CG  . GLU A 1 120 ? -8.675  36.564 48.507  1.00 72.55 ? 120 GLU A CG  1 
ATOM   1052 C CD  . GLU A 1 120 ? -10.002 36.695 49.259  1.00 75.61 ? 120 GLU A CD  1 
ATOM   1053 O OE1 . GLU A 1 120 ? -10.703 37.715 49.072  1.00 76.09 ? 120 GLU A OE1 1 
ATOM   1054 O OE2 . GLU A 1 120 ? -10.349 35.770 50.026  1.00 74.39 ? 120 GLU A OE2 1 
ATOM   1055 N N   . LYS A 1 121 ? -9.758  33.894 47.478  1.00 47.79 ? 121 LYS A N   1 
ATOM   1056 C CA  . LYS A 1 121 ? -9.494  32.488 47.745  1.00 41.68 ? 121 LYS A CA  1 
ATOM   1057 C C   . LYS A 1 121 ? -10.722 31.886 48.411  1.00 39.16 ? 121 LYS A C   1 
ATOM   1058 O O   . LYS A 1 121 ? -11.463 32.577 49.114  1.00 43.13 ? 121 LYS A O   1 
ATOM   1059 C CB  . LYS A 1 121 ? -8.265  32.293 48.658  1.00 43.25 ? 121 LYS A CB  1 
ATOM   1060 C CG  . LYS A 1 121 ? -6.976  32.945 48.173  1.00 48.01 ? 121 LYS A CG  1 
ATOM   1061 C CD  . LYS A 1 121 ? -5.821  32.633 49.125  1.00 48.74 ? 121 LYS A CD  1 
ATOM   1062 C CE  . LYS A 1 121 ? -4.783  33.750 49.171  1.00 46.20 ? 121 LYS A CE  1 
ATOM   1063 N NZ  . LYS A 1 121 ? -3.627  33.399 50.053  1.00 50.83 ? 121 LYS A NZ  1 
ATOM   1064 N N   . LEU A 1 122 ? -10.929 30.590 48.190  1.00 33.42 ? 122 LEU A N   1 
ATOM   1065 C CA  . LEU A 1 122 ? -12.092 29.879 48.708  1.00 34.22 ? 122 LEU A CA  1 
ATOM   1066 C C   . LEU A 1 122 ? -11.637 28.776 49.651  1.00 35.40 ? 122 LEU A C   1 
ATOM   1067 O O   . LEU A 1 122 ? -10.743 27.993 49.311  1.00 33.55 ? 122 LEU A O   1 
ATOM   1068 C CB  . LEU A 1 122 ? -12.926 29.275 47.570  1.00 30.38 ? 122 LEU A CB  1 
ATOM   1069 C CG  . LEU A 1 122 ? -13.490 30.203 46.489  1.00 28.94 ? 122 LEU A CG  1 
ATOM   1070 C CD1 . LEU A 1 122 ? -14.273 29.403 45.461  1.00 34.44 ? 122 LEU A CD1 1 
ATOM   1071 C CD2 . LEU A 1 122 ? -14.365 31.270 47.107  1.00 30.76 ? 122 LEU A CD2 1 
ATOM   1072 N N   . ASN A 1 123 ? -12.252 28.709 50.830  1.00 25.57 ? 123 ASN A N   1 
ATOM   1073 C CA  . ASN A 1 123 ? -11.939 27.653 51.782  1.00 28.79 ? 123 ASN A CA  1 
ATOM   1074 C C   . ASN A 1 123 ? -12.885 26.471 51.563  1.00 26.31 ? 123 ASN A C   1 
ATOM   1075 O O   . ASN A 1 123 ? -13.680 26.449 50.617  1.00 27.11 ? 123 ASN A O   1 
ATOM   1076 C CB  . ASN A 1 123 ? -11.984 28.189 53.216  1.00 31.18 ? 123 ASN A CB  1 
ATOM   1077 C CG  . ASN A 1 123 ? -13.323 28.802 53.583  1.00 33.67 ? 123 ASN A CG  1 
ATOM   1078 O OD1 . ASN A 1 123 ? -14.357 28.464 53.008  1.00 30.55 ? 123 ASN A OD1 1 
ATOM   1079 N ND2 . ASN A 1 123 ? -13.311 29.701 54.565  1.00 36.20 ? 123 ASN A ND2 1 
ATOM   1080 N N   . ARG A 1 124 ? -12.811 25.472 52.445  1.00 25.37 ? 124 ARG A N   1 
ATOM   1081 C CA  . ARG A 1 124 ? -13.553 24.232 52.229  1.00 24.55 ? 124 ARG A CA  1 
ATOM   1082 C C   . ARG A 1 124 ? -15.055 24.473 52.254  1.00 25.96 ? 124 ARG A C   1 
ATOM   1083 O O   . ARG A 1 124 ? -15.797 23.961 51.402  1.00 25.32 ? 124 ARG A O   1 
ATOM   1084 C CB  . ARG A 1 124 ? -13.159 23.196 53.285  1.00 28.17 ? 124 ARG A CB  1 
ATOM   1085 C CG  . ARG A 1 124 ? -13.883 21.872 53.120  1.00 26.90 ? 124 ARG A CG  1 
ATOM   1086 C CD  . ARG A 1 124 ? -13.743 20.953 54.337  1.00 28.31 ? 124 ARG A CD  1 
ATOM   1087 N NE  . ARG A 1 124 ? -14.573 19.760 54.175  1.00 28.36 ? 124 ARG A NE  1 
ATOM   1088 C CZ  . ARG A 1 124 ? -15.856 19.693 54.526  1.00 37.26 ? 124 ARG A CZ  1 
ATOM   1089 N NH1 . ARG A 1 124 ? -16.448 20.747 55.079  1.00 38.37 ? 124 ARG A NH1 1 
ATOM   1090 N NH2 . ARG A 1 124 ? -16.548 18.574 54.329  1.00 33.29 ? 124 ARG A NH2 1 
ATOM   1091 N N   . GLU A 1 125 ? -15.522 25.255 53.227  1.00 27.52 ? 125 GLU A N   1 
ATOM   1092 C CA  . GLU A 1 125 ? -16.950 25.527 53.343  1.00 28.10 ? 125 GLU A CA  1 
ATOM   1093 C C   . GLU A 1 125 ? -17.451 26.323 52.145  1.00 21.78 ? 125 GLU A C   1 
ATOM   1094 O O   . GLU A 1 125 ? -18.554 26.076 51.636  1.00 20.30 ? 125 GLU A O   1 
ATOM   1095 C CB  . GLU A 1 125 ? -17.225 26.274 54.649  1.00 30.84 ? 125 GLU A CB  1 
ATOM   1096 C CG  . GLU A 1 125 ? -17.020 25.434 55.909  1.00 39.56 ? 125 GLU A CG  1 
ATOM   1097 C CD  . GLU A 1 125 ? -15.564 25.020 56.145  1.00 52.30 ? 125 GLU A CD  1 
ATOM   1098 O OE1 . GLU A 1 125 ? -15.339 23.859 56.564  1.00 50.39 ? 125 GLU A OE1 1 
ATOM   1099 O OE2 . GLU A 1 125 ? -14.646 25.846 55.912  1.00 49.17 ? 125 GLU A OE2 1 
ATOM   1100 N N   . GLU A 1 126 ? -16.639 27.263 51.661  1.00 25.72 ? 126 GLU A N   1 
ATOM   1101 C CA  . GLU A 1 126 ? -17.034 28.059 50.505  1.00 23.64 ? 126 GLU A CA  1 
ATOM   1102 C C   . GLU A 1 126 ? -17.060 27.213 49.237  1.00 19.45 ? 126 GLU A C   1 
ATOM   1103 O O   . GLU A 1 126 ? -17.960 27.364 48.404  1.00 18.67 ? 126 GLU A O   1 
ATOM   1104 C CB  . GLU A 1 126 ? -16.092 29.257 50.367  1.00 22.74 ? 126 GLU A CB  1 
ATOM   1105 C CG  . GLU A 1 126 ? -16.339 30.306 51.457  1.00 23.07 ? 126 GLU A CG  1 
ATOM   1106 C CD  . GLU A 1 126 ? -15.159 31.220 51.725  1.00 30.05 ? 126 GLU A CD  1 
ATOM   1107 O OE1 . GLU A 1 126 ? -14.038 30.938 51.249  1.00 30.30 ? 126 GLU A OE1 1 
ATOM   1108 O OE2 . GLU A 1 126 ? -15.359 32.223 52.440  1.00 32.55 ? 126 GLU A OE2 1 
ATOM   1109 N N   . LEU A 1 127 ? -16.087 26.312 49.075  1.00 24.01 ? 127 LEU A N   1 
ATOM   1110 C CA  . LEU A 1 127 ? -16.103 25.429 47.912  1.00 24.99 ? 127 LEU A CA  1 
ATOM   1111 C C   . LEU A 1 127 ? -17.272 24.452 47.980  1.00 24.68 ? 127 LEU A C   1 
ATOM   1112 O O   . LEU A 1 127 ? -17.850 24.089 46.946  1.00 19.37 ? 127 LEU A O   1 
ATOM   1113 C CB  . LEU A 1 127 ? -14.770 24.687 47.806  1.00 27.53 ? 127 LEU A CB  1 
ATOM   1114 C CG  . LEU A 1 127 ? -13.596 25.547 47.334  1.00 27.88 ? 127 LEU A CG  1 
ATOM   1115 C CD1 . LEU A 1 127 ? -12.272 24.912 47.733  1.00 31.66 ? 127 LEU A CD1 1 
ATOM   1116 C CD2 . LEU A 1 127 ? -13.676 25.764 45.834  1.00 30.05 ? 127 LEU A CD2 1 
ATOM   1117 N N   . LEU A 1 128 ? -17.631 24.006 49.190  1.00 22.04 ? 128 LEU A N   1 
ATOM   1118 C CA  . LEU A 1 128 ? -18.812 23.156 49.332  1.00 20.75 ? 128 LEU A CA  1 
ATOM   1119 C C   . LEU A 1 128 ? -20.064 23.885 48.879  1.00 19.18 ? 128 LEU A C   1 
ATOM   1120 O O   . LEU A 1 128 ? -20.935 23.301 48.216  1.00 17.55 ? 128 LEU A O   1 
ATOM   1121 C CB  . LEU A 1 128 ? -18.964 22.701 50.786  1.00 22.72 ? 128 LEU A CB  1 
ATOM   1122 C CG  . LEU A 1 128 ? -18.738 21.225 51.096  1.00 29.81 ? 128 LEU A CG  1 
ATOM   1123 C CD1 . LEU A 1 128 ? -18.744 21.005 52.606  1.00 25.39 ? 128 LEU A CD1 1 
ATOM   1124 C CD2 . LEU A 1 128 ? -19.813 20.400 50.417  1.00 29.77 ? 128 LEU A CD2 1 
ATOM   1125 N N   . ASP A 1 129 ? -20.178 25.167 49.232  1.00 21.07 ? 129 ASP A N   1 
ATOM   1126 C CA  . ASP A 1 129 ? -21.303 25.958 48.746  1.00 19.91 ? 129 ASP A CA  1 
ATOM   1127 C C   . ASP A 1 129 ? -21.243 26.124 47.235  1.00 17.98 ? 129 ASP A C   1 
ATOM   1128 O O   . ASP A 1 129 ? -22.273 26.043 46.556  1.00 18.94 ? 129 ASP A O   1 
ATOM   1129 C CB  . ASP A 1 129 ? -21.328 27.319 49.448  1.00 19.05 ? 129 ASP A CB  1 
ATOM   1130 C CG  . ASP A 1 129 ? -21.864 27.228 50.865  1.00 21.51 ? 129 ASP A CG  1 
ATOM   1131 O OD1 . ASP A 1 129 ? -22.179 26.098 51.303  1.00 24.05 ? 129 ASP A OD1 1 
ATOM   1132 O OD2 . ASP A 1 129 ? -21.977 28.280 51.542  1.00 23.39 ? 129 ASP A OD2 1 
ATOM   1133 N N   . LEU A 1 130 ? -20.042 26.332 46.682  1.00 19.31 ? 130 LEU A N   1 
ATOM   1134 C CA  . LEU A 1 130 ? -19.913 26.483 45.236  1.00 20.39 ? 130 LEU A CA  1 
ATOM   1135 C C   . LEU A 1 130 ? -20.347 25.214 44.509  1.00 16.22 ? 130 LEU A C   1 
ATOM   1136 O O   . LEU A 1 130 ? -21.093 25.271 43.521  1.00 18.49 ? 130 LEU A O   1 
ATOM   1137 C CB  . LEU A 1 130 ? -18.474 26.853 44.873  1.00 19.55 ? 130 LEU A CB  1 
ATOM   1138 C CG  . LEU A 1 130 ? -18.316 27.256 43.401  1.00 22.32 ? 130 LEU A CG  1 
ATOM   1139 C CD1 . LEU A 1 130 ? -19.210 28.441 43.044  1.00 26.59 ? 130 LEU A CD1 1 
ATOM   1140 C CD2 . LEU A 1 130 ? -16.862 27.561 43.096  1.00 25.33 ? 130 LEU A CD2 1 
ATOM   1141 N N   . GLN A 1 131 ? -19.901 24.055 44.992  1.00 16.83 ? 131 GLN A N   1 
ATOM   1142 C CA  . GLN A 1 131 ? -20.328 22.788 44.400  1.00 16.91 ? 131 GLN A CA  1 
ATOM   1143 C C   . GLN A 1 131 ? -21.839 22.623 44.495  1.00 16.50 ? 131 GLN A C   1 
ATOM   1144 O O   . GLN A 1 131 ? -22.514 22.306 43.508  1.00 16.01 ? 131 GLN A O   1 
ATOM   1145 C CB  . GLN A 1 131 ? -19.645 21.618 45.105  1.00 17.91 ? 131 GLN A CB  1 
ATOM   1146 C CG  . GLN A 1 131 ? -18.144 21.556 44.993  1.00 17.36 ? 131 GLN A CG  1 
ATOM   1147 C CD  . GLN A 1 131 ? -17.564 20.541 45.959  1.00 19.26 ? 131 GLN A CD  1 
ATOM   1148 O OE1 . GLN A 1 131 ? -17.981 20.451 47.125  1.00 19.37 ? 131 GLN A OE1 1 
ATOM   1149 N NE2 . GLN A 1 131 ? -16.611 19.753 45.479  1.00 20.21 ? 131 GLN A NE2 1 
ATOM   1150 N N   . THR A 1 132 ? -22.383 22.803 45.700  1.00 15.04 ? 132 THR A N   1 
ATOM   1151 C CA  . THR A 1 132 ? -23.787 22.488 45.926  1.00 16.49 ? 132 THR A CA  1 
ATOM   1152 C C   . THR A 1 132 ? -24.696 23.482 45.221  1.00 16.37 ? 132 THR A C   1 
ATOM   1153 O O   . THR A 1 132 ? -25.741 23.097 44.686  1.00 16.48 ? 132 THR A O   1 
ATOM   1154 C CB  . THR A 1 132 ? -24.072 22.458 47.426  1.00 16.64 ? 132 THR A CB  1 
ATOM   1155 O OG1 . THR A 1 132 ? -23.154 21.554 48.064  1.00 17.86 ? 132 THR A OG1 1 
ATOM   1156 C CG2 . THR A 1 132 ? -25.483 21.982 47.688  1.00 19.03 ? 132 THR A CG2 1 
ATOM   1157 N N   . LEU A 1 133 ? -24.320 24.763 45.201  1.00 17.45 ? 133 LEU A N   1 
ATOM   1158 C CA  . LEU A 1 133 ? -25.168 25.733 44.505  1.00 18.41 ? 133 LEU A CA  1 
ATOM   1159 C C   . LEU A 1 133 ? -25.144 25.529 43.002  1.00 21.05 ? 133 LEU A C   1 
ATOM   1160 O O   . LEU A 1 133 ? -26.139 25.814 42.326  1.00 17.10 ? 133 LEU A O   1 
ATOM   1161 C CB  . LEU A 1 133 ? -24.752 27.162 44.844  1.00 17.32 ? 133 LEU A CB  1 
ATOM   1162 C CG  . LEU A 1 133 ? -25.163 27.544 46.263  1.00 18.48 ? 133 LEU A CG  1 
ATOM   1163 C CD1 . LEU A 1 133 ? -24.350 28.754 46.725  1.00 22.52 ? 133 LEU A CD1 1 
ATOM   1164 C CD2 . LEU A 1 133 ? -26.667 27.822 46.335  1.00 20.21 ? 133 LEU A CD2 1 
ATOM   1165 N N   . ASN A 1 134 ? -24.029 25.048 42.456  1.00 18.34 ? 134 ASN A N   1 
ATOM   1166 C CA  . ASN A 1 134 ? -24.034 24.696 41.043  1.00 17.37 ? 134 ASN A CA  1 
ATOM   1167 C C   . ASN A 1 134 ? -25.006 23.552 40.774  1.00 19.98 ? 134 ASN A C   1 
ATOM   1168 O O   . ASN A 1 134 ? -25.751 23.590 39.789  1.00 17.21 ? 134 ASN A O   1 
ATOM   1169 C CB  . ASN A 1 134 ? -22.621 24.355 40.570  1.00 15.20 ? 134 ASN A CB  1 
ATOM   1170 C CG  . ASN A 1 134 ? -21.885 25.570 40.017  1.00 16.26 ? 134 ASN A CG  1 
ATOM   1171 O OD1 . ASN A 1 134 ? -22.054 25.928 38.850  1.00 19.19 ? 134 ASN A OD1 1 
ATOM   1172 N ND2 . ASN A 1 134 ? -21.090 26.221 40.857  1.00 17.19 ? 134 ASN A ND2 1 
ATOM   1173 N N   . LEU A 1 135 ? -25.050 22.544 41.651  1.00 15.99 ? 135 LEU A N   1 
ATOM   1174 C CA  . LEU A 1 135 ? -26.052 21.490 41.488  1.00 14.82 ? 135 LEU A CA  1 
ATOM   1175 C C   . LEU A 1 135 ? -27.457 22.065 41.574  1.00 16.08 ? 135 LEU A C   1 
ATOM   1176 O O   . LEU A 1 135 ? -28.307 21.810 40.710  1.00 15.20 ? 135 LEU A O   1 
ATOM   1177 C CB  . LEU A 1 135 ? -25.889 20.405 42.555  1.00 17.55 ? 135 LEU A CB  1 
ATOM   1178 C CG  . LEU A 1 135 ? -24.841 19.322 42.380  1.00 22.53 ? 135 LEU A CG  1 
ATOM   1179 C CD1 . LEU A 1 135 ? -24.925 18.376 43.572  1.00 19.91 ? 135 LEU A CD1 1 
ATOM   1180 C CD2 . LEU A 1 135 ? -25.035 18.570 41.073  1.00 16.68 ? 135 LEU A CD2 1 
ATOM   1181 N N   . LEU A 1 136 ? -27.709 22.869 42.609  1.00 15.41 ? 136 LEU A N   1 
ATOM   1182 C CA  . LEU A 1 136 ? -29.065 23.339 42.876  1.00 15.25 ? 136 LEU A CA  1 
ATOM   1183 C C   . LEU A 1 136 ? -29.554 24.302 41.805  1.00 16.30 ? 136 LEU A C   1 
ATOM   1184 O O   . LEU A 1 136 ? -30.767 24.396 41.575  1.00 16.00 ? 136 LEU A O   1 
ATOM   1185 C CB  . LEU A 1 136 ? -29.132 24.006 44.253  1.00 17.87 ? 136 LEU A CB  1 
ATOM   1186 C CG  . LEU A 1 136 ? -29.067 23.062 45.454  1.00 17.15 ? 136 LEU A CG  1 
ATOM   1187 C CD1 . LEU A 1 136 ? -28.892 23.846 46.753  1.00 19.37 ? 136 LEU A CD1 1 
ATOM   1188 C CD2 . LEU A 1 136 ? -30.310 22.184 45.520  1.00 20.20 ? 136 LEU A CD2 1 
ATOM   1189 N N   . ALA A 1 137 ? -28.644 25.043 41.158  1.00 15.46 ? 137 ALA A N   1 
ATOM   1190 C CA  . ALA A 1 137 ? -29.066 25.952 40.088  1.00 13.27 ? 137 ALA A CA  1 
ATOM   1191 C C   . ALA A 1 137 ? -29.770 25.212 38.955  1.00 14.67 ? 137 ALA A C   1 
ATOM   1192 O O   . ALA A 1 137 ? -30.618 25.797 38.262  1.00 15.70 ? 137 ALA A O   1 
ATOM   1193 C CB  . ALA A 1 137 ? -27.861 26.717 39.529  1.00 17.75 ? 137 ALA A CB  1 
ATOM   1194 N N   . TRP A 1 138 ? -29.442 23.935 38.742  1.00 14.40 ? 138 TRP A N   1 
ATOM   1195 C CA  . TRP A 1 138 ? -30.064 23.154 37.679  1.00 14.38 ? 138 TRP A CA  1 
ATOM   1196 C C   . TRP A 1 138 ? -31.236 22.313 38.184  1.00 13.18 ? 138 TRP A C   1 
ATOM   1197 O O   . TRP A 1 138 ? -31.675 21.388 37.485  1.00 15.13 ? 138 TRP A O   1 
ATOM   1198 C CB  . TRP A 1 138 ? -28.999 22.293 36.976  1.00 16.18 ? 138 TRP A CB  1 
ATOM   1199 C CG  . TRP A 1 138 ? -27.943 23.165 36.333  1.00 14.71 ? 138 TRP A CG  1 
ATOM   1200 C CD1 . TRP A 1 138 ? -26.823 23.694 36.934  1.00 16.98 ? 138 TRP A CD1 1 
ATOM   1201 C CD2 . TRP A 1 138 ? -27.940 23.655 34.987  1.00 13.98 ? 138 TRP A CD2 1 
ATOM   1202 N NE1 . TRP A 1 138 ? -26.135 24.471 36.034  1.00 17.05 ? 138 TRP A NE1 1 
ATOM   1203 C CE2 . TRP A 1 138 ? -26.800 24.464 34.834  1.00 15.14 ? 138 TRP A CE2 1 
ATOM   1204 C CE3 . TRP A 1 138 ? -28.789 23.474 33.889  1.00 16.14 ? 138 TRP A CE3 1 
ATOM   1205 C CZ2 . TRP A 1 138 ? -26.488 25.095 33.627  1.00 17.66 ? 138 TRP A CZ2 1 
ATOM   1206 C CZ3 . TRP A 1 138 ? -28.483 24.114 32.697  1.00 19.40 ? 138 TRP A CZ3 1 
ATOM   1207 C CH2 . TRP A 1 138 ? -27.342 24.906 32.574  1.00 20.58 ? 138 TRP A CH2 1 
ATOM   1208 N N   . CYS A 1 139 ? -31.782 22.637 39.358  1.00 13.05 ? 139 CYS A N   1 
ATOM   1209 C CA  . CYS A 1 139 ? -32.917 21.886 39.882  1.00 12.68 ? 139 CYS A CA  1 
ATOM   1210 C C   . CYS A 1 139 ? -34.141 22.065 38.990  1.00 12.80 ? 139 CYS A C   1 
ATOM   1211 O O   . CYS A 1 139 ? -34.512 23.189 38.642  1.00 14.19 ? 139 CYS A O   1 
ATOM   1212 C CB  . CYS A 1 139 ? -33.245 22.340 41.302  1.00 13.80 ? 139 CYS A CB  1 
ATOM   1213 S SG  . CYS A 1 139 ? -34.294 21.175 42.194  1.00 16.78 ? 139 CYS A SG  1 
ATOM   1214 N N   . GLY A 1 140 ? -34.779 20.950 38.650  1.00 13.37 ? 140 GLY A N   1 
ATOM   1215 C CA  . GLY A 1 140 ? -35.997 20.989 37.866  1.00 13.24 ? 140 GLY A CA  1 
ATOM   1216 C C   . GLY A 1 140 ? -37.231 21.252 38.705  1.00 15.74 ? 140 GLY A C   1 
ATOM   1217 O O   . GLY A 1 140 ? -37.211 21.261 39.938  1.00 14.06 ? 140 GLY A O   1 
ATOM   1218 N N   . ARG A 1 141 ? -38.349 21.435 38.000  1.00 14.07 ? 141 ARG A N   1 
ATOM   1219 C CA  . ARG A 1 141 ? -39.606 21.795 38.647  1.00 11.64 ? 141 ARG A CA  1 
ATOM   1220 C C   . ARG A 1 141 ? -40.007 20.790 39.719  1.00 13.08 ? 141 ARG A C   1 
ATOM   1221 O O   . ARG A 1 141 ? -40.430 21.180 40.808  1.00 14.74 ? 141 ARG A O   1 
ATOM   1222 C CB  . ARG A 1 141 ? -40.695 21.919 37.578  1.00 13.42 ? 141 ARG A CB  1 
ATOM   1223 C CG  . ARG A 1 141 ? -42.106 22.131 38.114  1.00 13.17 ? 141 ARG A CG  1 
ATOM   1224 C CD  . ARG A 1 141 ? -43.048 22.352 36.927  1.00 15.56 ? 141 ARG A CD  1 
ATOM   1225 N NE  . ARG A 1 141 ? -44.457 22.409 37.316  1.00 17.68 ? 141 ARG A NE  1 
ATOM   1226 C CZ  . ARG A 1 141 ? -45.287 21.373 37.257  1.00 16.14 ? 141 ARG A CZ  1 
ATOM   1227 N NH1 . ARG A 1 141 ? -44.862 20.192 36.821  1.00 17.33 ? 141 ARG A NH1 1 
ATOM   1228 N NH2 . ARG A 1 141 ? -46.539 21.520 37.630  1.00 19.41 ? 141 ARG A NH2 1 
ATOM   1229 N N   . THR A 1 142 ? -39.868 19.492 39.440  1.00 14.02 ? 142 THR A N   1 
ATOM   1230 C CA  . THR A 1 142 ? -40.326 18.492 40.399  1.00 14.06 ? 142 THR A CA  1 
ATOM   1231 C C   . THR A 1 142 ? -39.551 18.603 41.705  1.00 14.64 ? 142 THR A C   1 
ATOM   1232 O O   . THR A 1 142 ? -40.136 18.687 42.796  1.00 16.46 ? 142 THR A O   1 
ATOM   1233 C CB  . THR A 1 142 ? -40.173 17.087 39.812  1.00 16.12 ? 142 THR A CB  1 
ATOM   1234 O OG1 . THR A 1 142 ? -41.011 16.958 38.659  1.00 16.32 ? 142 THR A OG1 1 
ATOM   1235 C CG2 . THR A 1 142 ? -40.590 16.030 40.833  1.00 19.84 ? 142 THR A CG2 1 
ATOM   1236 N N   . LEU A 1 143 ? -38.230 18.631 41.607  1.00 17.06 ? 143 LEU A N   1 
ATOM   1237 C CA  . LEU A 1 143 ? -37.438 18.626 42.824  1.00 15.48 ? 143 LEU A CA  1 
ATOM   1238 C C   . LEU A 1 143 ? -37.347 19.997 43.469  1.00 19.69 ? 143 LEU A C   1 
ATOM   1239 O O   . LEU A 1 143 ? -36.931 20.085 44.624  1.00 20.66 ? 143 LEU A O   1 
ATOM   1240 C CB  . LEU A 1 143 ? -36.046 18.074 42.534  1.00 15.35 ? 143 LEU A CB  1 
ATOM   1241 C CG  . LEU A 1 143 ? -36.007 16.570 42.246  1.00 18.89 ? 143 LEU A CG  1 
ATOM   1242 C CD1 . LEU A 1 143 ? -34.571 16.117 42.031  1.00 19.99 ? 143 LEU A CD1 1 
ATOM   1243 C CD2 . LEU A 1 143 ? -36.622 15.798 43.404  1.00 18.48 ? 143 LEU A CD2 1 
ATOM   1244 N N   . ARG A 1 144 ? -37.746 21.063 42.773  1.00 15.71 ? 144 ARG A N   1 
ATOM   1245 C CA  . ARG A 1 144 ? -37.821 22.363 43.430  1.00 17.00 ? 144 ARG A CA  1 
ATOM   1246 C C   . ARG A 1 144 ? -38.837 22.346 44.567  1.00 22.31 ? 144 ARG A C   1 
ATOM   1247 O O   . ARG A 1 144 ? -38.760 23.183 45.476  1.00 24.50 ? 144 ARG A O   1 
ATOM   1248 C CB  . ARG A 1 144 ? -38.135 23.463 42.397  1.00 15.67 ? 144 ARG A CB  1 
ATOM   1249 C CG  . ARG A 1 144 ? -36.863 24.058 41.767  1.00 15.72 ? 144 ARG A CG  1 
ATOM   1250 C CD  . ARG A 1 144 ? -37.142 24.897 40.525  1.00 18.56 ? 144 ARG A CD  1 
ATOM   1251 N NE  . ARG A 1 144 ? -35.917 25.441 39.934  1.00 18.89 ? 144 ARG A NE  1 
ATOM   1252 C CZ  . ARG A 1 144 ? -35.401 26.626 40.248  1.00 25.37 ? 144 ARG A CZ  1 
ATOM   1253 N NH1 . ARG A 1 144 ? -36.006 27.397 41.145  1.00 25.74 ? 144 ARG A NH1 1 
ATOM   1254 N NH2 . ARG A 1 144 ? -34.284 27.046 39.662  1.00 24.27 ? 144 ARG A NH2 1 
ATOM   1255 N N   . LYS A 1 145 ? -39.762 21.381 44.561  1.00 24.59 ? 145 LYS A N   1 
ATOM   1256 C CA  . LYS A 1 145 ? -40.633 21.166 45.713  1.00 33.72 ? 145 LYS A CA  1 
ATOM   1257 C C   . LYS A 1 145 ? -39.956 20.306 46.782  1.00 32.98 ? 145 LYS A C   1 
ATOM   1258 O O   . LYS A 1 145 ? -39.870 20.711 47.946  1.00 35.08 ? 145 LYS A O   1 
ATOM   1259 C CB  . LYS A 1 145 ? -41.949 20.534 45.254  1.00 44.31 ? 145 LYS A CB  1 
ATOM   1260 C CG  . LYS A 1 145 ? -42.701 21.378 44.228  1.00 49.19 ? 145 LYS A CG  1 
ATOM   1261 C CD  . LYS A 1 145 ? -42.810 20.669 42.882  1.00 54.16 ? 145 LYS A CD  1 
ATOM   1262 C CE  . LYS A 1 145 ? -44.033 19.757 42.819  1.00 57.87 ? 145 LYS A CE  1 
ATOM   1263 N NZ  . LYS A 1 145 ? -44.301 19.265 41.433  1.00 56.14 ? 145 LYS A NZ  1 
ATOM   1264 N N   . ASP A 1 146 ? -39.464 19.119 46.404  1.00 29.28 ? 146 ASP A N   1 
ATOM   1265 C CA  . ASP A 1 146 ? -38.763 18.246 47.349  1.00 31.20 ? 146 ASP A CA  1 
ATOM   1266 C C   . ASP A 1 146 ? -37.601 18.958 48.032  1.00 30.40 ? 146 ASP A C   1 
ATOM   1267 O O   . ASP A 1 146 ? -37.391 18.804 49.241  1.00 38.20 ? 146 ASP A O   1 
ATOM   1268 C CB  . ASP A 1 146 ? -38.233 17.005 46.628  1.00 39.34 ? 146 ASP A CB  1 
ATOM   1269 C CG  . ASP A 1 146 ? -39.330 16.163 46.016  1.00 45.57 ? 146 ASP A CG  1 
ATOM   1270 O OD1 . ASP A 1 146 ? -40.183 16.719 45.296  1.00 39.88 ? 146 ASP A OD1 1 
ATOM   1271 O OD2 . ASP A 1 146 ? -39.323 14.934 46.246  1.00 48.75 ? 146 ASP A OD2 1 
ATOM   1272 N N   . LEU A 1 147 ? -36.813 19.714 47.271  1.00 22.72 ? 147 LEU A N   1 
ATOM   1273 C CA  . LEU A 1 147 ? -35.594 20.341 47.766  1.00 17.66 ? 147 LEU A CA  1 
ATOM   1274 C C   . LEU A 1 147 ? -35.800 21.820 48.107  1.00 22.28 ? 147 LEU A C   1 
ATOM   1275 O O   . LEU A 1 147 ? -34.821 22.568 48.202  1.00 21.73 ? 147 LEU A O   1 
ATOM   1276 C CB  . LEU A 1 147 ? -34.467 20.167 46.743  1.00 20.45 ? 147 LEU A CB  1 
ATOM   1277 C CG  . LEU A 1 147 ? -34.072 18.746 46.278  1.00 18.69 ? 147 LEU A CG  1 
ATOM   1278 C CD1 . LEU A 1 147 ? -33.091 18.783 45.119  1.00 20.39 ? 147 LEU A CD1 1 
ATOM   1279 C CD2 . LEU A 1 147 ? -33.491 17.908 47.407  1.00 23.41 ? 147 LEU A CD2 1 
ATOM   1280 N N   . LYS A 1 148 ? -37.053 22.245 48.310  1.00 21.22 ? 148 LYS A N   1 
ATOM   1281 C CA  . LYS A 1 148 ? -37.354 23.668 48.496  1.00 20.61 ? 148 LYS A CA  1 
ATOM   1282 C C   . LYS A 1 148 ? -36.589 24.269 49.675  1.00 23.72 ? 148 LYS A C   1 
ATOM   1283 O O   . LYS A 1 148 ? -36.172 25.432 49.617  1.00 20.34 ? 148 LYS A O   1 
ATOM   1284 C CB  . LYS A 1 148 ? -38.862 23.870 48.681  1.00 24.64 ? 148 LYS A CB  1 
ATOM   1285 C CG  . LYS A 1 148 ? -39.367 23.719 50.116  1.00 34.97 ? 148 LYS A CG  1 
ATOM   1286 C CD  . LYS A 1 148 ? -40.888 23.691 50.195  1.00 41.32 ? 148 LYS A CD  1 
ATOM   1287 C CE  . LYS A 1 148 ? -41.391 24.299 51.501  1.00 45.09 ? 148 LYS A CE  1 
ATOM   1288 N NZ  . LYS A 1 148 ? -40.580 23.868 52.679  1.00 48.42 ? 148 LYS A NZ  1 
ATOM   1289 N N   . ASP A 1 149 ? -36.388 23.492 50.748  1.00 25.89 ? 149 ASP A N   1 
ATOM   1290 C CA  . ASP A 1 149 ? -35.729 24.025 51.940  1.00 23.50 ? 149 ASP A CA  1 
ATOM   1291 C C   . ASP A 1 149 ? -34.231 24.183 51.732  1.00 22.41 ? 149 ASP A C   1 
ATOM   1292 O O   . ASP A 1 149 ? -33.634 25.154 52.216  1.00 23.07 ? 149 ASP A O   1 
ATOM   1293 C CB  . ASP A 1 149 ? -36.000 23.114 53.137  1.00 28.94 ? 149 ASP A CB  1 
ATOM   1294 C CG  . ASP A 1 149 ? -37.444 22.701 53.227  1.00 27.39 ? 149 ASP A CG  1 
ATOM   1295 O OD1 . ASP A 1 149 ? -38.306 23.559 53.521  1.00 26.55 ? 149 ASP A OD1 1 
ATOM   1296 O OD2 . ASP A 1 149 ? -37.722 21.509 52.963  1.00 31.48 ? 149 ASP A OD2 1 
ATOM   1297 N N   . LEU A 1 150 ? -33.597 23.221 51.055  1.00 21.97 ? 150 LEU A N   1 
ATOM   1298 C CA  . LEU A 1 150 ? -32.192 23.371 50.699  1.00 22.16 ? 150 LEU A CA  1 
ATOM   1299 C C   . LEU A 1 150 ? -31.990 24.553 49.774  1.00 19.72 ? 150 LEU A C   1 
ATOM   1300 O O   . LEU A 1 150 ? -31.002 25.282 49.899  1.00 21.61 ? 150 LEU A O   1 
ATOM   1301 C CB  . LEU A 1 150 ? -31.660 22.108 50.028  1.00 26.62 ? 150 LEU A CB  1 
ATOM   1302 C CG  . LEU A 1 150 ? -31.251 20.951 50.924  1.00 21.21 ? 150 LEU A CG  1 
ATOM   1303 C CD1 . LEU A 1 150 ? -30.543 19.903 50.092  1.00 23.39 ? 150 LEU A CD1 1 
ATOM   1304 C CD2 . LEU A 1 150 ? -30.387 21.414 52.097  1.00 18.95 ? 150 LEU A CD2 1 
ATOM   1305 N N   . LEU A 1 151 ? -32.913 24.746 48.820  1.00 17.47 ? 151 LEU A N   1 
ATOM   1306 C CA  . LEU A 1 151 ? -32.793 25.871 47.899  1.00 16.83 ? 151 LEU A CA  1 
ATOM   1307 C C   . LEU A 1 151 ? -32.881 27.194 48.643  1.00 19.92 ? 151 LEU A C   1 
ATOM   1308 O O   . LEU A 1 151 ? -32.129 28.134 48.354  1.00 23.63 ? 151 LEU A O   1 
ATOM   1309 C CB  . LEU A 1 151 ? -33.880 25.786 46.821  1.00 16.98 ? 151 LEU A CB  1 
ATOM   1310 C CG  . LEU A 1 151 ? -33.641 24.763 45.724  1.00 16.82 ? 151 LEU A CG  1 
ATOM   1311 C CD1 . LEU A 1 151 ? -34.959 24.450 45.004  1.00 20.85 ? 151 LEU A CD1 1 
ATOM   1312 C CD2 . LEU A 1 151 ? -32.610 25.286 44.735  1.00 21.55 ? 151 LEU A CD2 1 
ATOM   1313 N N   . ASN A 1 152 ? -33.786 27.280 49.621  1.00 18.46 ? 152 ASN A N   1 
ATOM   1314 C CA  . ASN A 1 152 ? -33.940 28.507 50.391  1.00 19.84 ? 152 ASN A CA  1 
ATOM   1315 C C   . ASN A 1 152 ? -32.775 28.733 51.344  1.00 25.28 ? 152 ASN A C   1 
ATOM   1316 O O   . ASN A 1 152 ? -32.474 29.885 51.677  1.00 26.61 ? 152 ASN A O   1 
ATOM   1317 C CB  . ASN A 1 152 ? -35.257 28.479 51.169  1.00 23.17 ? 152 ASN A CB  1 
ATOM   1318 C CG  . ASN A 1 152 ? -36.466 28.574 50.264  1.00 42.98 ? 152 ASN A CG  1 
ATOM   1319 O OD1 . ASN A 1 152 ? -36.400 29.161 49.183  1.00 46.90 ? 152 ASN A OD1 1 
ATOM   1320 N ND2 . ASN A 1 152 ? -37.581 27.994 50.699  1.00 45.63 ? 152 ASN A ND2 1 
ATOM   1321 N N   . LYS A 1 153 ? -32.140 27.653 51.821  1.00 20.24 ? 153 LYS A N   1 
ATOM   1322 C CA  . LYS A 1 153 ? -31.015 27.780 52.747  1.00 23.25 ? 153 LYS A CA  1 
ATOM   1323 C C   . LYS A 1 153 ? -29.950 28.699 52.168  1.00 26.24 ? 153 LYS A C   1 
ATOM   1324 O O   . LYS A 1 153 ? -29.490 29.639 52.827  1.00 27.59 ? 153 LYS A O   1 
ATOM   1325 C CB  . LYS A 1 153 ? -30.433 26.393 53.045  1.00 23.71 ? 153 LYS A CB  1 
ATOM   1326 C CG  . LYS A 1 153 ? -29.344 26.373 54.112  1.00 27.79 ? 153 LYS A CG  1 
ATOM   1327 C CD  . LYS A 1 153 ? -28.946 24.947 54.482  1.00 24.35 ? 153 LYS A CD  1 
ATOM   1328 C CE  . LYS A 1 153 ? -27.732 24.944 55.398  1.00 22.10 ? 153 LYS A CE  1 
ATOM   1329 N NZ  . LYS A 1 153 ? -27.409 23.576 55.922  1.00 29.23 ? 153 LYS A NZ  1 
ATOM   1330 N N   . GLY A 1 154 ? -29.552 28.435 50.927  1.00 23.32 ? 154 GLY A N   1 
ATOM   1331 C CA  . GLY A 1 154 ? -28.755 29.350 50.140  1.00 25.06 ? 154 GLY A CA  1 
ATOM   1332 C C   . GLY A 1 154 ? -27.273 29.325 50.413  1.00 25.50 ? 154 GLY A C   1 
ATOM   1333 O O   . GLY A 1 154 ? -26.510 29.882 49.611  1.00 24.25 ? 154 GLY A O   1 
ATOM   1334 N N   . ARG A 1 155 ? -26.833 28.689 51.497  1.00 24.07 ? 155 ARG A N   1 
ATOM   1335 C CA  . ARG A 1 155 ? -25.435 28.728 51.903  1.00 22.55 ? 155 ARG A CA  1 
ATOM   1336 C C   . ARG A 1 155 ? -25.218 27.721 53.025  1.00 27.11 ? 155 ARG A C   1 
ATOM   1337 O O   . ARG A 1 155 ? -26.169 27.160 53.576  1.00 28.43 ? 155 ARG A O   1 
ATOM   1338 C CB  . ARG A 1 155 ? -25.035 30.128 52.364  1.00 25.31 ? 155 ARG A CB  1 
ATOM   1339 C CG  . ARG A 1 155 ? -25.846 30.611 53.564  1.00 25.35 ? 155 ARG A CG  1 
ATOM   1340 C CD  . ARG A 1 155 ? -25.349 31.941 54.083  1.00 30.35 ? 155 ARG A CD  1 
ATOM   1341 N NE  . ARG A 1 155 ? -25.516 32.988 53.083  1.00 34.10 ? 155 ARG A NE  1 
ATOM   1342 C CZ  . ARG A 1 155 ? -24.532 33.772 52.660  1.00 36.29 ? 155 ARG A CZ  1 
ATOM   1343 N NH1 . ARG A 1 155 ? -24.775 34.699 51.745  1.00 41.73 ? 155 ARG A NH1 1 
ATOM   1344 N NH2 . ARG A 1 155 ? -23.308 33.632 53.159  1.00 38.67 ? 155 ARG A NH2 1 
ATOM   1345 N N   . ASN A 1 156 ? -23.943 27.522 53.370  1.00 22.08 ? 156 ASN A N   1 
ATOM   1346 C CA  . ASN A 1 156 ? -23.520 26.637 54.463  1.00 21.37 ? 156 ASN A CA  1 
ATOM   1347 C C   . ASN A 1 156 ? -24.040 25.210 54.268  1.00 24.38 ? 156 ASN A C   1 
ATOM   1348 O O   . ASN A 1 156 ? -24.621 24.600 55.171  1.00 27.18 ? 156 ASN A O   1 
ATOM   1349 C CB  . ASN A 1 156 ? -23.947 27.200 55.823  1.00 27.67 ? 156 ASN A CB  1 
ATOM   1350 C CG  . ASN A 1 156 ? -23.503 28.641 56.023  1.00 39.09 ? 156 ASN A CG  1 
ATOM   1351 O OD1 . ASN A 1 156 ? -22.469 29.060 55.502  1.00 40.75 ? 156 ASN A OD1 1 
ATOM   1352 N ND2 . ASN A 1 156 ? -24.287 29.406 56.775  1.00 38.77 ? 156 ASN A ND2 1 
ATOM   1353 N N   . TYR A 1 157 ? -23.806 24.671 53.076  1.00 18.07 ? 157 TYR A N   1 
ATOM   1354 C CA  . TYR A 1 157 ? -24.222 23.316 52.752  1.00 19.05 ? 157 TYR A CA  1 
ATOM   1355 C C   . TYR A 1 157 ? -23.192 22.317 53.262  1.00 23.07 ? 157 TYR A C   1 
ATOM   1356 O O   . TYR A 1 157 ? -22.005 22.629 53.386  1.00 23.57 ? 157 TYR A O   1 
ATOM   1357 C CB  . TYR A 1 157 ? -24.411 23.156 51.236  1.00 17.99 ? 157 TYR A CB  1 
ATOM   1358 C CG  . TYR A 1 157 ? -25.557 23.976 50.694  1.00 19.18 ? 157 TYR A CG  1 
ATOM   1359 C CD1 . TYR A 1 157 ? -26.865 23.573 50.894  1.00 16.64 ? 157 TYR A CD1 1 
ATOM   1360 C CD2 . TYR A 1 157 ? -25.325 25.162 50.007  1.00 19.80 ? 157 TYR A CD2 1 
ATOM   1361 C CE1 . TYR A 1 157 ? -27.922 24.327 50.408  1.00 15.68 ? 157 TYR A CE1 1 
ATOM   1362 C CE2 . TYR A 1 157 ? -26.364 25.912 49.514  1.00 21.13 ? 157 TYR A CE2 1 
ATOM   1363 C CZ  . TYR A 1 157 ? -27.658 25.495 49.726  1.00 19.22 ? 157 TYR A CZ  1 
ATOM   1364 O OH  . TYR A 1 157 ? -28.695 26.234 49.233  1.00 20.28 ? 157 TYR A OH  1 
ATOM   1365 N N   . THR A 1 158 ? -23.657 21.113 53.570  1.00 19.10 ? 158 THR A N   1 
ATOM   1366 C CA  . THR A 1 158 ? -22.790 20.031 54.017  1.00 18.80 ? 158 THR A CA  1 
ATOM   1367 C C   . THR A 1 158 ? -22.566 19.038 52.886  1.00 18.28 ? 158 THR A C   1 
ATOM   1368 O O   . THR A 1 158 ? -23.321 18.987 51.916  1.00 18.70 ? 158 THR A O   1 
ATOM   1369 C CB  . THR A 1 158 ? -23.395 19.283 55.200  1.00 22.68 ? 158 THR A CB  1 
ATOM   1370 O OG1 . THR A 1 158 ? -24.633 18.684 54.784  1.00 19.80 ? 158 THR A OG1 1 
ATOM   1371 C CG2 . THR A 1 158 ? -23.631 20.217 56.371  1.00 20.62 ? 158 THR A CG2 1 
ATOM   1372 N N   . GLN A 1 159 ? -21.538 18.205 53.053  1.00 18.92 ? 159 GLN A N   1 
ATOM   1373 C CA  . GLN A 1 159 ? -21.300 17.128 52.094  1.00 18.70 ? 159 GLN A CA  1 
ATOM   1374 C C   . GLN A 1 159 ? -22.505 16.195 52.008  1.00 20.56 ? 159 GLN A C   1 
ATOM   1375 O O   . GLN A 1 159 ? -22.875 15.739 50.917  1.00 18.65 ? 159 GLN A O   1 
ATOM   1376 C CB  . GLN A 1 159 ? -20.034 16.364 52.506  1.00 19.75 ? 159 GLN A CB  1 
ATOM   1377 C CG  . GLN A 1 159 ? -19.701 15.169 51.636  1.00 23.34 ? 159 GLN A CG  1 
ATOM   1378 C CD  . GLN A 1 159 ? -19.215 15.560 50.255  1.00 26.13 ? 159 GLN A CD  1 
ATOM   1379 O OE1 . GLN A 1 159 ? -18.620 16.621 50.068  1.00 23.73 ? 159 GLN A OE1 1 
ATOM   1380 N NE2 . GLN A 1 159 ? -19.483 14.703 49.271  1.00 24.13 ? 159 GLN A NE2 1 
ATOM   1381 N N   . GLU A 1 160 ? -23.156 15.932 53.145  1.00 22.57 ? 160 GLU A N   1 
ATOM   1382 C CA  . GLU A 1 160 ? -24.316 15.045 53.152  1.00 20.09 ? 160 GLU A CA  1 
ATOM   1383 C C   . GLU A 1 160 ? -25.501 15.654 52.412  1.00 19.18 ? 160 GLU A C   1 
ATOM   1384 O O   . GLU A 1 160 ? -26.223 14.939 51.710  1.00 19.20 ? 160 GLU A O   1 
ATOM   1385 C CB  . GLU A 1 160 ? -24.715 14.708 54.587  1.00 20.45 ? 160 GLU A CB  1 
ATOM   1386 C CG  . GLU A 1 160 ? -23.721 13.813 55.297  1.00 25.11 ? 160 GLU A CG  1 
ATOM   1387 C CD  . GLU A 1 160 ? -22.731 14.580 56.158  1.00 37.55 ? 160 GLU A CD  1 
ATOM   1388 O OE1 . GLU A 1 160 ? -22.279 14.009 57.174  1.00 44.16 ? 160 GLU A OE1 1 
ATOM   1389 O OE2 . GLU A 1 160 ? -22.401 15.743 55.838  1.00 36.37 ? 160 GLU A OE2 1 
ATOM   1390 N N   . GLU A 1 161 ? -25.733 16.964 52.566  1.00 17.79 ? 161 GLU A N   1 
ATOM   1391 C CA  . GLU A 1 161 ? -26.796 17.615 51.798  1.00 16.93 ? 161 GLU A CA  1 
ATOM   1392 C C   . GLU A 1 161 ? -26.509 17.561 50.299  1.00 16.45 ? 161 GLU A C   1 
ATOM   1393 O O   . GLU A 1 161 ? -27.409 17.279 49.492  1.00 16.39 ? 161 GLU A O   1 
ATOM   1394 C CB  . GLU A 1 161 ? -26.969 19.061 52.270  1.00 18.40 ? 161 GLU A CB  1 
ATOM   1395 C CG  . GLU A 1 161 ? -27.650 19.176 53.633  1.00 18.32 ? 161 GLU A CG  1 
ATOM   1396 C CD  . GLU A 1 161 ? -27.565 20.568 54.237  1.00 22.19 ? 161 GLU A CD  1 
ATOM   1397 O OE1 . GLU A 1 161 ? -26.713 21.360 53.791  1.00 20.55 ? 161 GLU A OE1 1 
ATOM   1398 O OE2 . GLU A 1 161 ? -28.356 20.868 55.158  1.00 22.91 ? 161 GLU A OE2 1 
ATOM   1399 N N   . LYS A 1 162 ? -25.262 17.842 49.905  1.00 16.09 ? 162 LYS A N   1 
ATOM   1400 C CA  . LYS A 1 162 ? -24.865 17.745 48.503  1.00 15.52 ? 162 LYS A CA  1 
ATOM   1401 C C   . LYS A 1 162 ? -25.108 16.342 47.957  1.00 17.51 ? 162 LYS A C   1 
ATOM   1402 O O   . LYS A 1 162 ? -25.609 16.180 46.836  1.00 17.56 ? 162 LYS A O   1 
ATOM   1403 C CB  . LYS A 1 162 ? -23.393 18.138 48.363  1.00 16.59 ? 162 LYS A CB  1 
ATOM   1404 C CG  . LYS A 1 162 ? -22.840 18.065 46.928  1.00 19.08 ? 162 LYS A CG  1 
ATOM   1405 C CD  . LYS A 1 162 ? -21.370 18.500 46.871  1.00 20.61 ? 162 LYS A CD  1 
ATOM   1406 C CE  . LYS A 1 162 ? -20.469 17.557 47.642  1.00 20.99 ? 162 LYS A CE  1 
ATOM   1407 N NZ  . LYS A 1 162 ? -19.019 17.885 47.470  1.00 20.49 ? 162 LYS A NZ  1 
ATOM   1408 N N   . GLU A 1 163 ? -24.755 15.317 48.738  1.00 17.90 ? 163 GLU A N   1 
ATOM   1409 C CA  . GLU A 1 163 ? -24.972 13.936 48.322  1.00 19.06 ? 163 GLU A CA  1 
ATOM   1410 C C   . GLU A 1 163 ? -26.462 13.615 48.222  1.00 18.67 ? 163 GLU A C   1 
ATOM   1411 O O   . GLU A 1 163 ? -26.881 12.852 47.345  1.00 17.05 ? 163 GLU A O   1 
ATOM   1412 C CB  . GLU A 1 163 ? -24.272 12.983 49.298  1.00 21.21 ? 163 GLU A CB  1 
ATOM   1413 C CG  . GLU A 1 163 ? -22.769 12.841 49.041  1.00 21.36 ? 163 GLU A CG  1 
ATOM   1414 C CD  . GLU A 1 163 ? -21.997 12.211 50.193  1.00 31.91 ? 163 GLU A CD  1 
ATOM   1415 O OE1 . GLU A 1 163 ? -22.619 11.775 51.188  1.00 33.97 ? 163 GLU A OE1 1 
ATOM   1416 O OE2 . GLU A 1 163 ? -20.756 12.143 50.093  1.00 31.87 ? 163 GLU A OE2 1 
ATOM   1417 N N   . TYR A 1 164 ? -27.274 14.169 49.124  1.00 19.10 ? 164 TYR A N   1 
ATOM   1418 C CA  . TYR A 1 164 ? -28.717 13.972 49.030  1.00 18.60 ? 164 TYR A CA  1 
ATOM   1419 C C   . TYR A 1 164 ? -29.248 14.526 47.717  1.00 17.65 ? 164 TYR A C   1 
ATOM   1420 O O   . TYR A 1 164 ? -30.025 13.860 47.023  1.00 18.00 ? 164 TYR A O   1 
ATOM   1421 C CB  . TYR A 1 164 ? -29.409 14.626 50.228  1.00 19.79 ? 164 TYR A CB  1 
ATOM   1422 C CG  . TYR A 1 164 ? -30.900 14.343 50.339  1.00 19.53 ? 164 TYR A CG  1 
ATOM   1423 C CD1 . TYR A 1 164 ? -31.826 15.021 49.551  1.00 25.66 ? 164 TYR A CD1 1 
ATOM   1424 C CD2 . TYR A 1 164 ? -31.376 13.429 51.261  1.00 23.63 ? 164 TYR A CD2 1 
ATOM   1425 C CE1 . TYR A 1 164 ? -33.185 14.774 49.674  1.00 23.56 ? 164 TYR A CE1 1 
ATOM   1426 C CE2 . TYR A 1 164 ? -32.729 13.171 51.389  1.00 27.15 ? 164 TYR A CE2 1 
ATOM   1427 C CZ  . TYR A 1 164 ? -33.626 13.840 50.595  1.00 29.35 ? 164 TYR A CZ  1 
ATOM   1428 O OH  . TYR A 1 164 ? -34.970 13.572 50.744  1.00 34.08 ? 164 TYR A OH  1 
ATOM   1429 N N   . VAL A 1 165 ? -28.818 15.733 47.347  1.00 17.35 ? 165 VAL A N   1 
ATOM   1430 C CA  . VAL A 1 165 ? -29.238 16.319 46.071  1.00 14.90 ? 165 VAL A CA  1 
ATOM   1431 C C   . VAL A 1 165 ? -28.812 15.428 44.908  1.00 15.77 ? 165 VAL A C   1 
ATOM   1432 O O   . VAL A 1 165 ? -29.603 15.139 44.001  1.00 16.04 ? 165 VAL A O   1 
ATOM   1433 C CB  . VAL A 1 165 ? -28.673 17.745 45.926  1.00 15.72 ? 165 VAL A CB  1 
ATOM   1434 C CG1 . VAL A 1 165 ? -28.996 18.310 44.538  1.00 17.24 ? 165 VAL A CG1 1 
ATOM   1435 C CG2 . VAL A 1 165 ? -29.249 18.644 47.011  1.00 17.79 ? 165 VAL A CG2 1 
ATOM   1436 N N   . LEU A 1 166 ? -27.553 14.977 44.918  1.00 17.46 ? 166 LEU A N   1 
ATOM   1437 C CA  . LEU A 1 166 ? -27.085 14.098 43.849  1.00 17.95 ? 166 LEU A CA  1 
ATOM   1438 C C   . LEU A 1 166 ? -27.964 12.863 43.730  1.00 19.48 ? 166 LEU A C   1 
ATOM   1439 O O   . LEU A 1 166 ? -28.348 12.470 42.624  1.00 16.77 ? 166 LEU A O   1 
ATOM   1440 C CB  . LEU A 1 166 ? -25.629 13.706 44.090  1.00 18.68 ? 166 LEU A CB  1 
ATOM   1441 C CG  . LEU A 1 166 ? -24.620 14.788 43.701  1.00 21.20 ? 166 LEU A CG  1 
ATOM   1442 C CD1 . LEU A 1 166 ? -23.245 14.532 44.327  1.00 22.63 ? 166 LEU A CD1 1 
ATOM   1443 C CD2 . LEU A 1 166 ? -24.519 14.905 42.184  1.00 21.96 ? 166 LEU A CD2 1 
ATOM   1444 N N   A ASN A 1 167 ? -28.312 12.250 44.864  0.37 17.87 ? 167 ASN A N   1 
ATOM   1445 N N   B ASN A 1 167 ? -28.317 12.250 44.859  0.63 17.40 ? 167 ASN A N   1 
ATOM   1446 C CA  A ASN A 1 167 ? -29.119 11.034 44.836  0.37 19.07 ? 167 ASN A CA  1 
ATOM   1447 C CA  B ASN A 1 167 ? -29.116 11.031 44.804  0.63 18.87 ? 167 ASN A CA  1 
ATOM   1448 C C   A ASN A 1 167 ? -30.497 11.292 44.242  0.37 16.81 ? 167 ASN A C   1 
ATOM   1449 C C   B ASN A 1 167 ? -30.494 11.301 44.217  0.63 16.79 ? 167 ASN A C   1 
ATOM   1450 O O   A ASN A 1 167 ? -30.976 10.513 43.409  0.37 17.38 ? 167 ASN A O   1 
ATOM   1451 O O   B ASN A 1 167 ? -30.973 10.545 43.362  0.63 18.07 ? 167 ASN A O   1 
ATOM   1452 C CB  A ASN A 1 167 ? -29.242 10.459 46.247  0.37 20.35 ? 167 ASN A CB  1 
ATOM   1453 C CB  B ASN A 1 167 ? -29.236 10.412 46.194  0.63 20.01 ? 167 ASN A CB  1 
ATOM   1454 C CG  A ASN A 1 167 ? -27.943 9.863  46.744  0.37 23.33 ? 167 ASN A CG  1 
ATOM   1455 C CG  B ASN A 1 167 ? -30.086 9.161  46.190  0.63 27.86 ? 167 ASN A CG  1 
ATOM   1456 O OD1 A ASN A 1 167 ? -27.134 9.372  45.959  0.37 24.86 ? 167 ASN A OD1 1 
ATOM   1457 O OD1 B ASN A 1 167 ? -29.708 8.141  45.611  0.63 33.42 ? 167 ASN A OD1 1 
ATOM   1458 N ND2 A ASN A 1 167 ? -27.735 9.906  48.055  0.37 27.46 ? 167 ASN A ND2 1 
ATOM   1459 N ND2 B ASN A 1 167 ? -31.250 9.239  46.816  0.63 43.54 ? 167 ASN A ND2 1 
ATOM   1460 N N   . LYS A 1 168 ? -31.148 12.384 44.655  1.00 15.11 ? 168 LYS A N   1 
ATOM   1461 C CA  . LYS A 1 168 ? -32.449 12.736 44.084  1.00 16.46 ? 168 LYS A CA  1 
ATOM   1462 C C   . LYS A 1 168 ? -32.341 13.035 42.593  1.00 17.12 ? 168 LYS A C   1 
ATOM   1463 O O   . LYS A 1 168 ? -33.241 12.691 41.815  1.00 15.62 ? 168 LYS A O   1 
ATOM   1464 C CB  . LYS A 1 168 ? -33.044 13.948 44.803  1.00 15.22 ? 168 LYS A CB  1 
ATOM   1465 C CG  . LYS A 1 168 ? -33.434 13.728 46.243  1.00 18.70 ? 168 LYS A CG  1 
ATOM   1466 C CD  . LYS A 1 168 ? -34.251 12.471 46.432  1.00 28.88 ? 168 LYS A CD  1 
ATOM   1467 C CE  . LYS A 1 168 ? -35.707 12.702 46.088  1.00 31.71 ? 168 LYS A CE  1 
ATOM   1468 N NZ  . LYS A 1 168 ? -36.566 11.680 46.754  1.00 39.27 ? 168 LYS A NZ  1 
ATOM   1469 N N   . TYR A 1 169 ? -31.256 13.695 42.181  1.00 16.18 ? 169 TYR A N   1 
ATOM   1470 C CA  . TYR A 1 169 ? -31.048 13.988 40.768  1.00 14.13 ? 169 TYR A CA  1 
ATOM   1471 C C   . TYR A 1 169 ? -30.944 12.707 39.954  1.00 17.36 ? 169 TYR A C   1 
ATOM   1472 O O   . TYR A 1 169 ? -31.550 12.591 38.886  1.00 15.47 ? 169 TYR A O   1 
ATOM   1473 C CB  . TYR A 1 169 ? -29.786 14.833 40.587  1.00 14.56 ? 169 TYR A CB  1 
ATOM   1474 C CG  . TYR A 1 169 ? -29.977 16.323 40.819  1.00 12.02 ? 169 TYR A CG  1 
ATOM   1475 C CD1 . TYR A 1 169 ? -31.104 16.820 41.476  1.00 13.50 ? 169 TYR A CD1 1 
ATOM   1476 C CD2 . TYR A 1 169 ? -29.032 17.236 40.365  1.00 15.94 ? 169 TYR A CD2 1 
ATOM   1477 C CE1 . TYR A 1 169 ? -31.269 18.189 41.684  1.00 13.99 ? 169 TYR A CE1 1 
ATOM   1478 C CE2 . TYR A 1 169 ? -29.190 18.599 40.572  1.00 11.38 ? 169 TYR A CE2 1 
ATOM   1479 C CZ  . TYR A 1 169 ? -30.308 19.067 41.230  1.00 12.42 ? 169 TYR A CZ  1 
ATOM   1480 O OH  . TYR A 1 169 ? -30.463 20.422 41.433  1.00 14.99 ? 169 TYR A OH  1 
ATOM   1481 N N   . PHE A 1 170 ? -30.197 11.723 40.447  1.00 16.78 ? 170 PHE A N   1 
ATOM   1482 C CA  . PHE A 1 170 ? -30.095 10.481 39.687  1.00 15.19 ? 170 PHE A CA  1 
ATOM   1483 C C   . PHE A 1 170 ? -31.414 9.719  39.693  1.00 17.30 ? 170 PHE A C   1 
ATOM   1484 O O   . PHE A 1 170 ? -31.717 9.011  38.727  1.00 17.40 ? 170 PHE A O   1 
ATOM   1485 C CB  . PHE A 1 170 ? -28.947 9.624  40.217  1.00 18.82 ? 170 PHE A CB  1 
ATOM   1486 C CG  . PHE A 1 170 ? -27.623 9.975  39.600  1.00 20.38 ? 170 PHE A CG  1 
ATOM   1487 C CD1 . PHE A 1 170 ? -27.279 9.484  38.347  1.00 20.45 ? 170 PHE A CD1 1 
ATOM   1488 C CD2 . PHE A 1 170 ? -26.746 10.842 40.241  1.00 21.87 ? 170 PHE A CD2 1 
ATOM   1489 C CE1 . PHE A 1 170 ? -26.078 9.832  37.754  1.00 20.05 ? 170 PHE A CE1 1 
ATOM   1490 C CE2 . PHE A 1 170 ? -25.531 11.184 39.655  1.00 22.85 ? 170 PHE A CE2 1 
ATOM   1491 C CZ  . PHE A 1 170 ? -25.200 10.687 38.414  1.00 19.31 ? 170 PHE A CZ  1 
ATOM   1492 N N   . GLU A 1 171 ? -32.218 9.862  40.755  1.00 17.22 ? 171 GLU A N   1 
ATOM   1493 C CA  . GLU A 1 171 ? -33.545 9.255  40.741  1.00 17.27 ? 171 GLU A CA  1 
ATOM   1494 C C   . GLU A 1 171 ? -34.395 9.833  39.613  1.00 17.73 ? 171 GLU A C   1 
ATOM   1495 O O   . GLU A 1 171 ? -35.116 9.096  38.936  1.00 20.82 ? 171 GLU A O   1 
ATOM   1496 C CB  . GLU A 1 171 ? -34.236 9.447  42.091  1.00 19.29 ? 171 GLU A CB  1 
ATOM   1497 C CG  . GLU A 1 171 ? -33.696 8.578  43.214  1.00 21.73 ? 171 GLU A CG  1 
ATOM   1498 C CD  . GLU A 1 171 ? -34.373 8.892  44.539  1.00 31.41 ? 171 GLU A CD  1 
ATOM   1499 O OE1 . GLU A 1 171 ? -35.265 9.775  44.552  1.00 33.98 ? 171 GLU A OE1 1 
ATOM   1500 O OE2 . GLU A 1 171 ? -34.021 8.256  45.555  1.00 51.21 ? 171 GLU A OE2 1 
ATOM   1501 N N   . ILE A 1 172 ? -34.298 11.147 39.379  1.00 14.59 ? 172 ILE A N   1 
ATOM   1502 C CA  . ILE A 1 172 ? -35.036 11.780 38.286  1.00 15.00 ? 172 ILE A CA  1 
ATOM   1503 C C   . ILE A 1 172 ? -34.562 11.236 36.939  1.00 16.84 ? 172 ILE A C   1 
ATOM   1504 O O   . ILE A 1 172 ? -35.375 10.926 36.059  1.00 15.32 ? 172 ILE A O   1 
ATOM   1505 C CB  . ILE A 1 172 ? -34.891 13.316 38.370  1.00 16.04 ? 172 ILE A CB  1 
ATOM   1506 C CG1 . ILE A 1 172 ? -35.714 13.867 39.540  1.00 18.98 ? 172 ILE A CG1 1 
ATOM   1507 C CG2 . ILE A 1 172 ? -35.294 13.982 37.057  1.00 20.47 ? 172 ILE A CG2 1 
ATOM   1508 C CD1 . ILE A 1 172 ? -37.215 13.806 39.320  1.00 22.90 ? 172 ILE A CD1 1 
ATOM   1509 N N   . ILE A 1 173 ? -33.246 11.083 36.766  1.00 14.22 ? 173 ILE A N   1 
ATOM   1510 C CA  . ILE A 1 173 ? -32.721 10.566 35.503  1.00 13.81 ? 173 ILE A CA  1 
ATOM   1511 C C   . ILE A 1 173 ? -33.225 9.150  35.263  1.00 15.45 ? 173 ILE A C   1 
ATOM   1512 O O   . ILE A 1 173 ? -33.603 8.797  34.137  1.00 16.95 ? 173 ILE A O   1 
ATOM   1513 C CB  . ILE A 1 173 ? -31.180 10.630 35.488  1.00 15.66 ? 173 ILE A CB  1 
ATOM   1514 C CG1 . ILE A 1 173 ? -30.703 12.085 35.529  1.00 13.94 ? 173 ILE A CG1 1 
ATOM   1515 C CG2 . ILE A 1 173 ? -30.618 9.924  34.256  1.00 21.36 ? 173 ILE A CG2 1 
ATOM   1516 C CD1 . ILE A 1 173 ? -29.187 12.229 35.623  1.00 18.34 ? 173 ILE A CD1 1 
ATOM   1517 N N   . LYS A 1 174 ? -33.276 8.328  36.320  1.00 14.47 ? 174 LYS A N   1 
ATOM   1518 C CA  . LYS A 1 174 ? -33.711 6.938  36.172  1.00 14.37 ? 174 LYS A CA  1 
ATOM   1519 C C   . LYS A 1 174 ? -35.166 6.823  35.749  1.00 17.26 ? 174 LYS A C   1 
ATOM   1520 O O   . LYS A 1 174 ? -35.555 5.782  35.204  1.00 20.59 ? 174 LYS A O   1 
ATOM   1521 C CB  . LYS A 1 174 ? -33.514 6.159  37.472  1.00 20.85 ? 174 LYS A CB  1 
ATOM   1522 C CG  . LYS A 1 174 ? -32.070 5.949  37.855  1.00 21.45 ? 174 LYS A CG  1 
ATOM   1523 C CD  . LYS A 1 174 ? -31.967 5.304  39.228  1.00 30.23 ? 174 LYS A CD  1 
ATOM   1524 C CE  . LYS A 1 174 ? -30.640 5.656  39.882  1.00 45.94 ? 174 LYS A CE  1 
ATOM   1525 N NZ  . LYS A 1 174 ? -29.517 5.600  38.910  1.00 50.31 ? 174 LYS A NZ  1 
ATOM   1526 N N   . LYS A 1 175 ? -35.981 7.847  35.994  1.00 14.96 ? 175 LYS A N   1 
ATOM   1527 C CA  . LYS A 1 175 ? -37.387 7.810  35.612  1.00 17.24 ? 175 LYS A CA  1 
ATOM   1528 C C   . LYS A 1 175 ? -37.674 8.568  34.328  1.00 15.64 ? 175 LYS A C   1 
ATOM   1529 O O   . LYS A 1 175 ? -38.841 8.677  33.938  1.00 15.89 ? 175 LYS A O   1 
ATOM   1530 C CB  . LYS A 1 175 ? -38.260 8.345  36.748  1.00 25.28 ? 175 LYS A CB  1 
ATOM   1531 C CG  . LYS A 1 175 ? -37.790 7.902  38.110  1.00 33.77 ? 175 LYS A CG  1 
ATOM   1532 C CD  . LYS A 1 175 ? -38.408 8.727  39.222  1.00 40.89 ? 175 LYS A CD  1 
ATOM   1533 C CE  . LYS A 1 175 ? -39.777 8.207  39.583  1.00 44.07 ? 175 LYS A CE  1 
ATOM   1534 N NZ  . LYS A 1 175 ? -39.998 8.259  41.055  1.00 46.95 ? 175 LYS A NZ  1 
ATOM   1535 N N   . THR A 1 176 ? -36.644 9.035  33.629  1.00 15.02 ? 176 THR A N   1 
ATOM   1536 C CA  . THR A 1 176 ? -36.870 9.977  32.540  1.00 15.70 ? 176 THR A CA  1 
ATOM   1537 C C   . THR A 1 176 ? -37.432 9.295  31.294  1.00 15.32 ? 176 THR A C   1 
ATOM   1538 O O   . THR A 1 176 ? -38.482 9.705  30.784  1.00 14.98 ? 176 THR A O   1 
ATOM   1539 C CB  . THR A 1 176 ? -35.583 10.737 32.232  1.00 17.84 ? 176 THR A CB  1 
ATOM   1540 O OG1 . THR A 1 176 ? -35.305 11.631 33.319  1.00 16.77 ? 176 THR A OG1 1 
ATOM   1541 C CG2 . THR A 1 176 ? -35.753 11.564 30.958  1.00 16.81 ? 176 THR A CG2 1 
ATOM   1542 N N   . LEU A 1 177 ? -36.790 8.235  30.799  1.00 14.75 ? 177 LEU A N   1 
ATOM   1543 C CA  . LEU A 1 177 ? -37.351 7.576  29.618  1.00 15.17 ? 177 LEU A CA  1 
ATOM   1544 C C   . LEU A 1 177 ? -38.735 6.999  29.907  1.00 17.36 ? 177 LEU A C   1 
ATOM   1545 O O   . LEU A 1 177 ? -39.602 6.984  29.018  1.00 18.14 ? 177 LEU A O   1 
ATOM   1546 C CB  . LEU A 1 177 ? -36.405 6.485  29.112  1.00 16.12 ? 177 LEU A CB  1 
ATOM   1547 C CG  . LEU A 1 177 ? -35.065 7.013  28.579  1.00 18.73 ? 177 LEU A CG  1 
ATOM   1548 C CD1 . LEU A 1 177 ? -34.147 5.885  28.126  1.00 16.63 ? 177 LEU A CD1 1 
ATOM   1549 C CD2 . LEU A 1 177 ? -35.256 8.005  27.442  1.00 20.10 ? 177 LEU A CD2 1 
ATOM   1550 N N   . SER A 1 178 ? -38.969 6.561  31.149  1.00 16.87 ? 178 SER A N   1 
ATOM   1551 C CA  . SER A 1 178 ? -40.273 6.017  31.513  1.00 16.90 ? 178 SER A CA  1 
ATOM   1552 C C   . SER A 1 178 ? -41.373 7.065  31.396  1.00 17.43 ? 178 SER A C   1 
ATOM   1553 O O   . SER A 1 178 ? -42.497 6.741  31.001  1.00 17.88 ? 178 SER A O   1 
ATOM   1554 C CB  . SER A 1 178 ? -40.229 5.448  32.925  1.00 19.44 ? 178 SER A CB  1 
ATOM   1555 O OG  . SER A 1 178 ? -39.563 4.201  32.912  1.00 26.41 ? 178 SER A OG  1 
ATOM   1556 N N   . ILE A 1 179 ? -41.081 8.329  31.718  1.00 15.43 ? 179 ILE A N   1 
ATOM   1557 C CA  . ILE A 1 179 ? -42.177 9.290  31.642  1.00 16.16 ? 179 ILE A CA  1 
ATOM   1558 C C   . ILE A 1 179 ? -42.513 9.623  30.192  1.00 13.63 ? 179 ILE A C   1 
ATOM   1559 O O   . ILE A 1 179 ? -43.676 9.896  29.871  1.00 14.72 ? 179 ILE A O   1 
ATOM   1560 C CB  . ILE A 1 179 ? -41.898 10.558 32.477  1.00 17.46 ? 179 ILE A CB  1 
ATOM   1561 C CG1 . ILE A 1 179 ? -43.227 11.293 32.731  1.00 20.73 ? 179 ILE A CG1 1 
ATOM   1562 C CG2 . ILE A 1 179 ? -40.899 11.490 31.799  1.00 17.60 ? 179 ILE A CG2 1 
ATOM   1563 C CD1 . ILE A 1 179 ? -43.164 12.354 33.789  1.00 24.79 ? 179 ILE A CD1 1 
ATOM   1564 N N   . TYR A 1 180 ? -41.534 9.586  29.278  1.00 16.62 ? 180 TYR A N   1 
ATOM   1565 C CA  . TYR A 1 180 ? -41.883 9.749  27.868  1.00 15.69 ? 180 TYR A CA  1 
ATOM   1566 C C   . TYR A 1 180 ? -42.751 8.593  27.392  1.00 16.66 ? 180 TYR A C   1 
ATOM   1567 O O   . TYR A 1 180 ? -43.723 8.789  26.654  1.00 16.20 ? 180 TYR A O   1 
ATOM   1568 C CB  . TYR A 1 180 ? -40.624 9.858  27.002  1.00 14.13 ? 180 TYR A CB  1 
ATOM   1569 C CG  . TYR A 1 180 ? -39.931 11.181 27.140  1.00 12.36 ? 180 TYR A CG  1 
ATOM   1570 C CD1 . TYR A 1 180 ? -40.382 12.301 26.453  1.00 14.04 ? 180 TYR A CD1 1 
ATOM   1571 C CD2 . TYR A 1 180 ? -38.851 11.327 27.992  1.00 13.62 ? 180 TYR A CD2 1 
ATOM   1572 C CE1 . TYR A 1 180 ? -39.768 13.525 26.600  1.00 14.59 ? 180 TYR A CE1 1 
ATOM   1573 C CE2 . TYR A 1 180 ? -38.221 12.550 28.140  1.00 13.31 ? 180 TYR A CE2 1 
ATOM   1574 C CZ  . TYR A 1 180 ? -38.676 13.644 27.442  1.00 13.32 ? 180 TYR A CZ  1 
ATOM   1575 O OH  . TYR A 1 180 ? -38.070 14.877 27.591  1.00 13.25 ? 180 TYR A OH  1 
ATOM   1576 N N   . ARG A 1 181 ? -42.415 7.373  27.802  1.00 16.26 ? 181 ARG A N   1 
ATOM   1577 C CA  . ARG A 1 181 ? -43.243 6.238  27.413  1.00 15.64 ? 181 ARG A CA  1 
ATOM   1578 C C   . ARG A 1 181 ? -44.644 6.371  27.985  1.00 16.06 ? 181 ARG A C   1 
ATOM   1579 O O   . ARG A 1 181 ? -45.635 6.051  27.324  1.00 19.04 ? 181 ARG A O   1 
ATOM   1580 C CB  . ARG A 1 181 ? -42.595 4.946  27.895  1.00 18.74 ? 181 ARG A CB  1 
ATOM   1581 C CG  . ARG A 1 181 ? -43.394 3.721  27.581  1.00 23.16 ? 181 ARG A CG  1 
ATOM   1582 C CD  . ARG A 1 181 ? -42.615 2.495  28.018  1.00 27.18 ? 181 ARG A CD  1 
ATOM   1583 N NE  . ARG A 1 181 ? -41.260 2.541  27.483  1.00 20.96 ? 181 ARG A NE  1 
ATOM   1584 C CZ  . ARG A 1 181 ? -40.164 2.665  28.225  1.00 21.61 ? 181 ARG A CZ  1 
ATOM   1585 N NH1 . ARG A 1 181 ? -40.269 2.736  29.542  1.00 26.55 ? 181 ARG A NH1 1 
ATOM   1586 N NH2 . ARG A 1 181 ? -38.962 2.706  27.652  1.00 22.65 ? 181 ARG A NH2 1 
ATOM   1587 N N   . GLU A 1 182 ? -44.732 6.846  29.224  1.00 17.47 ? 182 GLU A N   1 
ATOM   1588 C CA  . GLU A 1 182 ? -46.006 6.985  29.906  1.00 19.73 ? 182 GLU A CA  1 
ATOM   1589 C C   . GLU A 1 182 ? -46.906 8.014  29.228  1.00 17.11 ? 182 GLU A C   1 
ATOM   1590 O O   . GLU A 1 182 ? -48.084 7.741  28.985  1.00 17.47 ? 182 GLU A O   1 
ATOM   1591 C CB  . GLU A 1 182 ? -45.748 7.351  31.358  1.00 25.49 ? 182 GLU A CB  1 
ATOM   1592 C CG  . GLU A 1 182 ? -46.893 8.015  31.969  1.00 36.19 ? 182 GLU A CG  1 
ATOM   1593 C CD  . GLU A 1 182 ? -46.452 8.737  33.245  1.00 50.55 ? 182 GLU A CD  1 
ATOM   1594 O OE1 . GLU A 1 182 ? -45.369 8.461  33.741  1.00 49.64 ? 182 GLU A OE1 1 
ATOM   1595 O OE2 . GLU A 1 182 ? -47.227 9.654  33.690  1.00 53.09 ? 182 GLU A OE2 1 
ATOM   1596 N N   . ILE A 1 183 ? -46.390 9.207  28.925  1.00 16.96 ? 183 ILE A N   1 
ATOM   1597 C CA  . ILE A 1 183 ? -47.276 10.196 28.308  1.00 19.13 ? 183 ILE A CA  1 
ATOM   1598 C C   . ILE A 1 183 ? -47.653 9.774  26.888  1.00 15.19 ? 183 ILE A C   1 
ATOM   1599 O O   . ILE A 1 183 ? -48.749 10.100 26.405  1.00 17.80 ? 183 ILE A O   1 
ATOM   1600 C CB  . ILE A 1 183 ? -46.658 11.614 28.363  1.00 18.36 ? 183 ILE A CB  1 
ATOM   1601 C CG1 . ILE A 1 183 ? -45.388 11.727 27.509  1.00 17.22 ? 183 ILE A CG1 1 
ATOM   1602 C CG2 . ILE A 1 183 ? -46.406 12.017 29.818  1.00 19.94 ? 183 ILE A CG2 1 
ATOM   1603 C CD1 . ILE A 1 183 ? -45.625 12.387 26.146  1.00 17.71 ? 183 ILE A CD1 1 
ATOM   1604 N N   . LYS A 1 184 ? -46.794 9.001  26.217  1.00 16.57 ? 184 LYS A N   1 
ATOM   1605 C CA  . LYS A 1 184 ? -47.129 8.498  24.891  1.00 15.88 ? 184 LYS A CA  1 
ATOM   1606 C C   . LYS A 1 184 ? -48.232 7.449  24.975  1.00 17.35 ? 184 LYS A C   1 
ATOM   1607 O O   . LYS A 1 184 ? -49.233 7.524  24.253  1.00 18.64 ? 184 LYS A O   1 
ATOM   1608 C CB  . LYS A 1 184 ? -45.881 7.928  24.213  1.00 17.80 ? 184 LYS A CB  1 
ATOM   1609 C CG  . LYS A 1 184 ? -46.123 7.375  22.809  1.00 21.35 ? 184 LYS A CG  1 
ATOM   1610 C CD  . LYS A 1 184 ? -44.871 6.682  22.268  1.00 21.92 ? 184 LYS A CD  1 
ATOM   1611 C CE  . LYS A 1 184 ? -45.161 5.954  20.965  1.00 27.21 ? 184 LYS A CE  1 
ATOM   1612 N NZ  . LYS A 1 184 ? -45.888 4.671  21.186  1.00 34.33 ? 184 LYS A NZ  1 
ATOM   1613 N N   . GLU A 1 185 ? -48.078 6.477  25.879  1.00 19.00 ? 185 GLU A N   1 
ATOM   1614 C CA  . GLU A 1 185 ? -49.078 5.423  26.011  1.00 21.90 ? 185 GLU A CA  1 
ATOM   1615 C C   . GLU A 1 185 ? -50.427 5.972  26.462  1.00 23.66 ? 185 GLU A C   1 
ATOM   1616 O O   . GLU A 1 185 ? -51.473 5.398  26.131  1.00 23.67 ? 185 GLU A O   1 
ATOM   1617 C CB  . GLU A 1 185 ? -48.579 4.359  26.989  1.00 20.64 ? 185 GLU A CB  1 
ATOM   1618 C CG  . GLU A 1 185 ? -48.577 4.836  28.422  1.00 42.07 ? 185 GLU A CG  1 
ATOM   1619 C CD  . GLU A 1 185 ? -48.041 3.814  29.387  1.00 55.39 ? 185 GLU A CD  1 
ATOM   1620 O OE1 . GLU A 1 185 ? -48.342 3.932  30.596  1.00 56.32 ? 185 GLU A OE1 1 
ATOM   1621 O OE2 . GLU A 1 185 ? -47.351 2.874  28.936  1.00 54.87 ? 185 GLU A OE2 1 
ATOM   1622 N N   . GLU A 1 186 ? -50.428 7.081  27.202  1.00 18.62 ? 186 GLU A N   1 
ATOM   1623 C CA  . GLU A 1 186 ? -51.649 7.715  27.685  1.00 19.87 ? 186 GLU A CA  1 
ATOM   1624 C C   . GLU A 1 186 ? -52.256 8.689  26.680  1.00 20.34 ? 186 GLU A C   1 
ATOM   1625 O O   . GLU A 1 186 ? -53.292 9.295  26.980  1.00 21.84 ? 186 GLU A O   1 
ATOM   1626 C CB  . GLU A 1 186 ? -51.379 8.442  29.005  1.00 21.24 ? 186 GLU A CB  1 
ATOM   1627 C CG  . GLU A 1 186 ? -50.965 7.497  30.139  1.00 22.36 ? 186 GLU A CG  1 
ATOM   1628 C CD  . GLU A 1 186 ? -50.515 8.223  31.395  1.00 29.36 ? 186 GLU A CD  1 
ATOM   1629 O OE1 . GLU A 1 186 ? -50.267 9.443  31.336  1.00 27.28 ? 186 GLU A OE1 1 
ATOM   1630 O OE2 . GLU A 1 186 ? -50.409 7.563  32.449  1.00 34.66 ? 186 GLU A OE2 1 
ATOM   1631 N N   . GLY A 1 187 ? -51.641 8.850  25.513  1.00 18.93 ? 187 GLY A N   1 
ATOM   1632 C CA  . GLY A 1 187 ? -52.150 9.763  24.505  1.00 16.85 ? 187 GLY A CA  1 
ATOM   1633 C C   . GLY A 1 187 ? -52.035 11.224 24.865  1.00 19.26 ? 187 GLY A C   1 
ATOM   1634 O O   . GLY A 1 187 ? -52.702 12.060 24.256  1.00 19.93 ? 187 GLY A O   1 
ATOM   1635 N N   . LYS A 1 188 ? -51.210 11.555 25.855  1.00 18.27 ? 188 LYS A N   1 
ATOM   1636 C CA  . LYS A 1 188 ? -51.020 12.948 26.234  1.00 16.56 ? 188 LYS A CA  1 
ATOM   1637 C C   . LYS A 1 188 ? -50.005 13.651 25.351  1.00 15.39 ? 188 LYS A C   1 
ATOM   1638 O O   . LYS A 1 188 ? -49.930 14.886 25.377  1.00 17.01 ? 188 LYS A O   1 
ATOM   1639 C CB  . LYS A 1 188 ? -50.605 13.028 27.709  1.00 17.77 ? 188 LYS A CB  1 
ATOM   1640 C CG  . LYS A 1 188 ? -51.693 12.524 28.649  1.00 24.05 ? 188 LYS A CG  1 
ATOM   1641 C CD  . LYS A 1 188 ? -51.241 12.515 30.096  1.00 29.70 ? 188 LYS A CD  1 
ATOM   1642 C CE  . LYS A 1 188 ? -52.387 12.128 31.025  1.00 38.26 ? 188 LYS A CE  1 
ATOM   1643 N NZ  . LYS A 1 188 ? -52.108 12.575 32.408  1.00 44.94 ? 188 LYS A NZ  1 
ATOM   1644 N N   . GLY A 1 189 ? -49.232 12.904 24.579  1.00 13.74 ? 189 GLY A N   1 
ATOM   1645 C CA  . GLY A 1 189 ? -48.320 13.494 23.623  1.00 13.00 ? 189 GLY A CA  1 
ATOM   1646 C C   . GLY A 1 189 ? -47.756 12.423 22.722  1.00 13.93 ? 189 GLY A C   1 
ATOM   1647 O O   . GLY A 1 189 ? -47.811 11.229 23.040  1.00 16.59 ? 189 GLY A O   1 
ATOM   1648 N N   . SER A 1 190 ? -47.240 12.861 21.580  1.00 12.97 ? 190 SER A N   1 
ATOM   1649 C CA  . SER A 1 190 ? -46.491 12.003 20.678  1.00 14.63 ? 190 SER A CA  1 
ATOM   1650 C C   . SER A 1 190 ? -45.009 12.225 20.923  1.00 14.99 ? 190 SER A C   1 
ATOM   1651 O O   . SER A 1 190 ? -44.593 13.304 21.351  1.00 12.83 ? 190 SER A O   1 
ATOM   1652 C CB  . SER A 1 190 ? -46.821 12.292 19.214  1.00 16.57 ? 190 SER A CB  1 
ATOM   1653 O OG  . SER A 1 190 ? -48.171 11.986 18.921  1.00 16.11 ? 190 SER A OG  1 
ATOM   1654 N N   . VAL A 1 191 ? -44.215 11.184 20.680  1.00 14.55 ? 191 VAL A N   1 
ATOM   1655 C CA  . VAL A 1 191 ? -42.765 11.273 20.762  1.00 11.93 ? 191 VAL A CA  1 
ATOM   1656 C C   . VAL A 1 191 ? -42.183 10.929 19.396  1.00 13.72 ? 191 VAL A C   1 
ATOM   1657 O O   . VAL A 1 191 ? -42.553 9.916  18.783  1.00 16.77 ? 191 VAL A O   1 
ATOM   1658 C CB  . VAL A 1 191 ? -42.186 10.348 21.847  1.00 12.79 ? 191 VAL A CB  1 
ATOM   1659 C CG1 . VAL A 1 191 ? -40.669 10.566 21.953  1.00 13.67 ? 191 VAL A CG1 1 
ATOM   1660 C CG2 . VAL A 1 191 ? -42.851 10.590 23.220  1.00 14.37 ? 191 VAL A CG2 1 
ATOM   1661 N N   . SER A 1 192 ? -41.277 11.767 18.927  1.00 13.26 ? 192 SER A N   1 
ATOM   1662 C CA  . SER A 1 192 ? -40.563 11.562 17.676  1.00 12.55 ? 192 SER A CA  1 
ATOM   1663 C C   . SER A 1 192 ? -39.089 11.305 17.965  1.00 12.15 ? 192 SER A C   1 
ATOM   1664 O O   . SER A 1 192 ? -38.621 11.408 19.102  1.00 13.29 ? 192 SER A O   1 
ATOM   1665 C CB  . SER A 1 192 ? -40.716 12.781 16.769  1.00 13.63 ? 192 SER A CB  1 
ATOM   1666 O OG  . SER A 1 192 ? -40.075 13.903 17.381  1.00 12.39 ? 192 SER A OG  1 
ATOM   1667 N N   . THR A 1 193 ? -38.340 10.986 16.909  1.00 12.63 ? 193 THR A N   1 
ATOM   1668 C CA  . THR A 1 193 ? -36.885 10.998 17.018  1.00 10.97 ? 193 THR A CA  1 
ATOM   1669 C C   . THR A 1 193 ? -36.312 11.677 15.776  1.00 12.87 ? 193 THR A C   1 
ATOM   1670 O O   . THR A 1 193 ? -37.047 12.173 14.922  1.00 13.21 ? 193 THR A O   1 
ATOM   1671 C CB  . THR A 1 193 ? -36.336 9.581  17.246  1.00 10.28 ? 193 THR A CB  1 
ATOM   1672 O OG1 . THR A 1 193 ? -34.977 9.659  17.700  1.00 12.35 ? 193 THR A OG1 1 
ATOM   1673 C CG2 . THR A 1 193 ? -36.421 8.698  15.985  1.00 11.74 ? 193 THR A CG2 1 
ATOM   1674 N N   . SER A 1 194 ? -34.993 11.743 15.703  1.00 10.66 ? 194 SER A N   1 
ATOM   1675 C CA  . SER A 1 194 ? -34.226 12.303 14.603  1.00 12.46 ? 194 SER A CA  1 
ATOM   1676 C C   . SER A 1 194 ? -33.219 11.268 14.132  1.00 10.13 ? 194 SER A C   1 
ATOM   1677 O O   . SER A 1 194 ? -32.865 10.349 14.881  1.00 12.37 ? 194 SER A O   1 
ATOM   1678 C CB  . SER A 1 194 ? -33.456 13.566 15.030  1.00 13.20 ? 194 SER A CB  1 
ATOM   1679 O OG  . SER A 1 194 ? -34.298 14.598 15.506  1.00 13.24 ? 194 SER A OG  1 
ATOM   1680 N N   . PRO A 1 195 ? -32.689 11.426 12.921  1.00 12.27 ? 195 PRO A N   1 
ATOM   1681 C CA  . PRO A 1 195 ? -31.505 10.657 12.532  1.00 11.32 ? 195 PRO A CA  1 
ATOM   1682 C C   . PRO A 1 195 ? -30.459 10.694 13.640  1.00 12.02 ? 195 PRO A C   1 
ATOM   1683 O O   . PRO A 1 195 ? -30.282 11.716 14.317  1.00 12.03 ? 195 PRO A O   1 
ATOM   1684 C CB  . PRO A 1 195 ? -31.024 11.364 11.262  1.00 14.04 ? 195 PRO A CB  1 
ATOM   1685 C CG  . PRO A 1 195 ? -32.262 12.014 10.697  1.00 27.31 ? 195 PRO A CG  1 
ATOM   1686 C CD  . PRO A 1 195 ? -33.133 12.364 11.873  1.00 14.99 ? 195 PRO A CD  1 
ATOM   1687 N N   . TYR A 1 196 ? -29.771 9.558  13.809  1.00 13.21 ? 196 TYR A N   1 
ATOM   1688 C CA  . TYR A 1 196 ? -29.218 9.133  15.100  1.00 11.91 ? 196 TYR A CA  1 
ATOM   1689 C C   . TYR A 1 196 ? -28.362 10.193 15.790  1.00 13.81 ? 196 TYR A C   1 
ATOM   1690 O O   . TYR A 1 196 ? -28.597 10.516 16.956  1.00 12.19 ? 196 TYR A O   1 
ATOM   1691 C CB  . TYR A 1 196 ? -28.395 7.860  14.908  1.00 11.29 ? 196 TYR A CB  1 
ATOM   1692 C CG  . TYR A 1 196 ? -28.276 7.030  16.174  1.00 11.52 ? 196 TYR A CG  1 
ATOM   1693 C CD1 . TYR A 1 196 ? -27.417 7.405  17.210  1.00 13.78 ? 196 TYR A CD1 1 
ATOM   1694 C CD2 . TYR A 1 196 ? -29.046 5.887  16.342  1.00 13.41 ? 196 TYR A CD2 1 
ATOM   1695 C CE1 . TYR A 1 196 ? -27.314 6.629  18.372  1.00 15.31 ? 196 TYR A CE1 1 
ATOM   1696 C CE2 . TYR A 1 196 ? -28.954 5.111  17.485  1.00 13.12 ? 196 TYR A CE2 1 
ATOM   1697 C CZ  . TYR A 1 196 ? -28.087 5.484  18.500  1.00 14.43 ? 196 TYR A CZ  1 
ATOM   1698 O OH  . TYR A 1 196 ? -28.007 4.709  19.635  1.00 16.68 ? 196 TYR A OH  1 
ATOM   1699 N N   . TYR A 1 197 ? -27.325 10.698 15.116  1.00 12.07 ? 197 TYR A N   1 
ATOM   1700 C CA  . TYR A 1 197 ? -26.438 11.673 15.742  1.00 11.87 ? 197 TYR A CA  1 
ATOM   1701 C C   . TYR A 1 197 ? -26.758 13.101 15.332  1.00 13.50 ? 197 TYR A C   1 
ATOM   1702 O O   . TYR A 1 197 ? -25.891 13.971 15.429  1.00 13.16 ? 197 TYR A O   1 
ATOM   1703 C CB  . TYR A 1 197 ? -24.971 11.318 15.463  1.00 13.57 ? 197 TYR A CB  1 
ATOM   1704 C CG  . TYR A 1 197 ? -24.617 10.004 16.103  1.00 13.40 ? 197 TYR A CG  1 
ATOM   1705 C CD1 . TYR A 1 197 ? -24.382 9.927  17.470  1.00 13.74 ? 197 TYR A CD1 1 
ATOM   1706 C CD2 . TYR A 1 197 ? -24.578 8.829  15.364  1.00 13.53 ? 197 TYR A CD2 1 
ATOM   1707 C CE1 . TYR A 1 197 ? -24.089 8.721  18.076  1.00 17.19 ? 197 TYR A CE1 1 
ATOM   1708 C CE2 . TYR A 1 197 ? -24.296 7.618  15.965  1.00 15.74 ? 197 TYR A CE2 1 
ATOM   1709 C CZ  . TYR A 1 197 ? -24.047 7.576  17.321  1.00 15.75 ? 197 TYR A CZ  1 
ATOM   1710 O OH  . TYR A 1 197 ? -23.764 6.377  17.944  1.00 20.41 ? 197 TYR A OH  1 
ATOM   1711 N N   . HIS A 1 198 ? -28.004 13.368 14.915  1.00 10.04 ? 198 HIS A N   1 
ATOM   1712 C CA  . HIS A 1 198 ? -28.433 14.742 14.621  1.00 11.56 ? 198 HIS A CA  1 
ATOM   1713 C C   . HIS A 1 198 ? -27.561 15.382 13.535  1.00 14.90 ? 198 HIS A C   1 
ATOM   1714 O O   . HIS A 1 198 ? -27.106 16.519 13.690  1.00 14.59 ? 198 HIS A O   1 
ATOM   1715 C CB  . HIS A 1 198 ? -28.427 15.546 15.935  1.00 11.19 ? 198 HIS A CB  1 
ATOM   1716 C CG  . HIS A 1 198 ? -29.199 16.832 15.905  1.00 12.77 ? 198 HIS A CG  1 
ATOM   1717 N ND1 . HIS A 1 198 ? -28.619 18.045 15.600  1.00 14.15 ? 198 HIS A ND1 1 
ATOM   1718 C CD2 . HIS A 1 198 ? -30.488 17.100 16.218  1.00 12.18 ? 198 HIS A CD2 1 
ATOM   1719 C CE1 . HIS A 1 198 ? -29.524 19.005 15.702  1.00 11.21 ? 198 HIS A CE1 1 
ATOM   1720 N NE2 . HIS A 1 198 ? -30.667 18.459 16.074  1.00 12.02 ? 198 HIS A NE2 1 
ATOM   1721 N N   . PRO A 1 199 ? -27.336 14.704 12.406  1.00 11.59 ? 199 PRO A N   1 
ATOM   1722 C CA  . PRO A 1 199 ? -26.576 15.306 11.303  1.00 12.05 ? 199 PRO A CA  1 
ATOM   1723 C C   . PRO A 1 199 ? -27.456 16.199 10.436  1.00 13.34 ? 199 PRO A C   1 
ATOM   1724 O O   . PRO A 1 199 ? -28.687 16.168 10.511  1.00 14.66 ? 199 PRO A O   1 
ATOM   1725 C CB  . PRO A 1 199 ? -26.136 14.086 10.498  1.00 15.53 ? 199 PRO A CB  1 
ATOM   1726 C CG  . PRO A 1 199 ? -27.368 13.215 10.565  1.00 16.04 ? 199 PRO A CG  1 
ATOM   1727 C CD  . PRO A 1 199 ? -27.900 13.403 12.006  1.00 11.56 ? 199 PRO A CD  1 
ATOM   1728 N N   . LEU A 1 200 ? -26.792 16.939 9.537   1.00 15.08 ? 200 LEU A N   1 
ATOM   1729 C CA  . LEU A 1 200 ? -27.461 17.692 8.472   1.00 14.59 ? 200 LEU A CA  1 
ATOM   1730 C C   . LEU A 1 200 ? -27.652 16.764 7.280   1.00 13.42 ? 200 LEU A C   1 
ATOM   1731 O O   . LEU A 1 200 ? -26.823 16.707 6.368   1.00 14.42 ? 200 LEU A O   1 
ATOM   1732 C CB  . LEU A 1 200 ? -26.659 18.930 8.090   1.00 16.21 ? 200 LEU A CB  1 
ATOM   1733 C CG  . LEU A 1 200 ? -26.583 20.033 9.145   1.00 17.75 ? 200 LEU A CG  1 
ATOM   1734 C CD1 . LEU A 1 200 ? -25.440 20.973 8.824   1.00 21.80 ? 200 LEU A CD1 1 
ATOM   1735 C CD2 . LEU A 1 200 ? -27.918 20.792 9.234   1.00 20.22 ? 200 LEU A CD2 1 
ATOM   1736 N N   . ILE A 1 201 ? -28.773 16.046 7.281   1.00 13.98 ? 201 ILE A N   1 
ATOM   1737 C CA  . ILE A 1 201 ? -29.096 15.050 6.253   1.00 13.85 ? 201 ILE A CA  1 
ATOM   1738 C C   . ILE A 1 201 ? -29.005 15.633 4.844   1.00 12.72 ? 201 ILE A C   1 
ATOM   1739 O O   . ILE A 1 201 ? -28.450 14.965 3.955   1.00 13.31 ? 201 ILE A O   1 
ATOM   1740 C CB  . ILE A 1 201 ? -30.482 14.426 6.509   1.00 13.26 ? 201 ILE A CB  1 
ATOM   1741 C CG1 . ILE A 1 201 ? -30.457 13.569 7.782   1.00 12.67 ? 201 ILE A CG1 1 
ATOM   1742 C CG2 . ILE A 1 201 ? -30.949 13.569 5.321   1.00 12.09 ? 201 ILE A CG2 1 
ATOM   1743 C CD1 . ILE A 1 201 ? -29.633 12.275 7.649   1.00 13.78 ? 201 ILE A CD1 1 
ATOM   1744 N N   . PRO A 1 202 ? -29.535 16.836 4.562   1.00 13.02 ? 202 PRO A N   1 
ATOM   1745 C CA  . PRO A 1 202 ? -29.427 17.342 3.185   1.00 12.68 ? 202 PRO A CA  1 
ATOM   1746 C C   . PRO A 1 202 ? -27.996 17.419 2.682   1.00 11.62 ? 202 PRO A C   1 
ATOM   1747 O O   . PRO A 1 202 ? -27.746 17.063 1.524   1.00 14.23 ? 202 PRO A O   1 
ATOM   1748 C CB  . PRO A 1 202 ? -30.102 18.718 3.266   1.00 12.43 ? 202 PRO A CB  1 
ATOM   1749 C CG  . PRO A 1 202 ? -31.123 18.540 4.358   1.00 12.25 ? 202 PRO A CG  1 
ATOM   1750 C CD  . PRO A 1 202 ? -30.375 17.728 5.389   1.00 12.50 ? 202 PRO A CD  1 
ATOM   1751 N N   . ILE A 1 203 ? -27.043 17.853 3.516   1.00 12.31 ? 203 ILE A N   1 
ATOM   1752 C CA  . ILE A 1 203 ? -25.652 17.926 3.068   1.00 13.34 ? 203 ILE A CA  1 
ATOM   1753 C C   . ILE A 1 203 ? -25.077 16.528 2.852   1.00 15.62 ? 203 ILE A C   1 
ATOM   1754 O O   . ILE A 1 203 ? -24.365 16.283 1.870   1.00 14.58 ? 203 ILE A O   1 
ATOM   1755 C CB  . ILE A 1 203 ? -24.816 18.745 4.070   1.00 15.06 ? 203 ILE A CB  1 
ATOM   1756 C CG1 . ILE A 1 203 ? -25.251 20.217 4.031   1.00 15.71 ? 203 ILE A CG1 1 
ATOM   1757 C CG2 . ILE A 1 203 ? -23.332 18.610 3.753   1.00 14.92 ? 203 ILE A CG2 1 
ATOM   1758 C CD1 . ILE A 1 203 ? -24.471 21.145 4.982   1.00 15.21 ? 203 ILE A CD1 1 
ATOM   1759 N N   . LEU A 1 204 ? -25.369 15.584 3.754   1.00 15.18 ? 204 LEU A N   1 
ATOM   1760 C CA  . LEU A 1 204 ? -24.860 14.228 3.561   1.00 15.15 ? 204 LEU A CA  1 
ATOM   1761 C C   . LEU A 1 204 ? -25.378 13.616 2.263   1.00 13.96 ? 204 LEU A C   1 
ATOM   1762 O O   . LEU A 1 204 ? -24.642 12.894 1.577   1.00 14.45 ? 204 LEU A O   1 
ATOM   1763 C CB  . LEU A 1 204 ? -25.236 13.346 4.749   1.00 12.79 ? 204 LEU A CB  1 
ATOM   1764 C CG  . LEU A 1 204 ? -24.717 13.773 6.132   1.00 13.92 ? 204 LEU A CG  1 
ATOM   1765 C CD1 . LEU A 1 204 ? -25.043 12.662 7.109   1.00 15.86 ? 204 LEU A CD1 1 
ATOM   1766 C CD2 . LEU A 1 204 ? -23.212 14.079 6.135   1.00 16.00 ? 204 LEU A CD2 1 
ATOM   1767 N N   . LEU A 1 205 ? -26.625 13.918 1.894   1.00 14.53 ? 205 LEU A N   1 
ATOM   1768 C CA  . LEU A 1 205 ? -27.183 13.379 0.659   1.00 13.08 ? 205 LEU A CA  1 
ATOM   1769 C C   . LEU A 1 205 ? -26.615 14.074 -0.574  1.00 15.50 ? 205 LEU A C   1 
ATOM   1770 O O   . LEU A 1 205 ? -26.361 13.421 -1.594  1.00 16.09 ? 205 LEU A O   1 
ATOM   1771 C CB  . LEU A 1 205 ? -28.703 13.508 0.672   1.00 16.60 ? 205 LEU A CB  1 
ATOM   1772 C CG  . LEU A 1 205 ? -29.406 12.511 1.591   1.00 14.09 ? 205 LEU A CG  1 
ATOM   1773 C CD1 . LEU A 1 205 ? -30.879 12.834 1.705   1.00 15.35 ? 205 LEU A CD1 1 
ATOM   1774 C CD2 . LEU A 1 205 ? -29.217 11.091 1.078   1.00 16.34 ? 205 LEU A CD2 1 
ATOM   1775 N N   . ASN A 1 206 ? -26.413 15.389 -0.498  1.00 12.39 ? 206 ASN A N   1 
ATOM   1776 C CA  . ASN A 1 206 ? -25.967 16.157 -1.654  1.00 11.79 ? 206 ASN A CA  1 
ATOM   1777 C C   . ASN A 1 206 ? -25.437 17.498 -1.182  1.00 15.68 ? 206 ASN A C   1 
ATOM   1778 O O   . ASN A 1 206 ? -26.223 18.431 -0.958  1.00 15.75 ? 206 ASN A O   1 
ATOM   1779 C CB  . ASN A 1 206 ? -27.111 16.373 -2.643  1.00 14.99 ? 206 ASN A CB  1 
ATOM   1780 C CG  . ASN A 1 206 ? -26.633 16.952 -3.963  1.00 22.97 ? 206 ASN A CG  1 
ATOM   1781 O OD1 . ASN A 1 206 ? -25.538 17.498 -4.058  1.00 17.64 ? 206 ASN A OD1 1 
ATOM   1782 N ND2 . ASN A 1 206 ? -27.446 16.802 -5.003  1.00 29.80 ? 206 ASN A ND2 1 
ATOM   1783 N N   . PRO A 1 207 ? -24.120 17.620 -0.994  1.00 14.50 ? 207 PRO A N   1 
ATOM   1784 C CA  . PRO A 1 207 ? -23.567 18.893 -0.499  1.00 14.07 ? 207 PRO A CA  1 
ATOM   1785 C C   . PRO A 1 207 ? -23.927 20.096 -1.358  1.00 15.63 ? 207 PRO A C   1 
ATOM   1786 O O   . PRO A 1 207 ? -23.902 21.226 -0.853  1.00 16.29 ? 207 PRO A O   1 
ATOM   1787 C CB  . PRO A 1 207 ? -22.052 18.637 -0.492  1.00 17.40 ? 207 PRO A CB  1 
ATOM   1788 C CG  . PRO A 1 207 ? -21.929 17.141 -0.350  1.00 19.45 ? 207 PRO A CG  1 
ATOM   1789 C CD  . PRO A 1 207 ? -23.106 16.556 -1.093  1.00 16.71 ? 207 PRO A CD  1 
ATOM   1790 N N   . ASN A 1 208 ? -24.287 19.898 -2.629  1.00 14.45 ? 208 ASN A N   1 
ATOM   1791 C CA  . ASN A 1 208 ? -24.630 21.028 -3.486  1.00 14.37 ? 208 ASN A CA  1 
ATOM   1792 C C   . ASN A 1 208 ? -25.940 21.694 -3.101  1.00 16.49 ? 208 ASN A C   1 
ATOM   1793 O O   . ASN A 1 208 ? -26.250 22.764 -3.642  1.00 16.64 ? 208 ASN A O   1 
ATOM   1794 C CB  . ASN A 1 208 ? -24.683 20.571 -4.937  1.00 18.24 ? 208 ASN A CB  1 
ATOM   1795 C CG  . ASN A 1 208 ? -23.337 20.133 -5.433  1.00 20.85 ? 208 ASN A CG  1 
ATOM   1796 O OD1 . ASN A 1 208 ? -22.345 20.841 -5.259  1.00 21.84 ? 208 ASN A OD1 1 
ATOM   1797 N ND2 . ASN A 1 208 ? -23.281 18.951 -6.037  1.00 30.39 ? 208 ASN A ND2 1 
ATOM   1798 N N   . CYS A 1 209 ? -26.699 21.107 -2.175  1.00 15.03 ? 209 CYS A N   1 
ATOM   1799 C CA  . CYS A 1 209 ? -27.915 21.757 -1.704  1.00 18.51 ? 209 CYS A CA  1 
ATOM   1800 C C   . CYS A 1 209 ? -27.623 23.093 -1.036  1.00 13.11 ? 209 CYS A C   1 
ATOM   1801 O O   . CYS A 1 209 ? -28.524 23.928 -0.942  1.00 17.23 ? 209 CYS A O   1 
ATOM   1802 C CB  . CYS A 1 209 ? -28.679 20.833 -0.748  1.00 18.71 ? 209 CYS A CB  1 
ATOM   1803 S SG  . CYS A 1 209 ? -27.940 20.598 0.879   1.00 21.21 ? 209 CYS A SG  1 
ATOM   1804 N N   . VAL A 1 210 ? -26.395 23.315 -0.563  1.00 15.59 ? 210 VAL A N   1 
ATOM   1805 C CA  . VAL A 1 210 ? -26.099 24.586 0.083   1.00 14.61 ? 210 VAL A CA  1 
ATOM   1806 C C   . VAL A 1 210 ? -26.196 25.737 -0.899  1.00 17.48 ? 210 VAL A C   1 
ATOM   1807 O O   . VAL A 1 210 ? -26.402 26.882 -0.486  1.00 17.29 ? 210 VAL A O   1 
ATOM   1808 C CB  . VAL A 1 210 ? -24.706 24.566 0.745   1.00 15.36 ? 210 VAL A CB  1 
ATOM   1809 C CG1 . VAL A 1 210 ? -24.607 23.417 1.732   1.00 18.65 ? 210 VAL A CG1 1 
ATOM   1810 C CG2 . VAL A 1 210 ? -23.602 24.472 -0.306  1.00 20.25 ? 210 VAL A CG2 1 
ATOM   1811 N N   . TYR A 1 211 ? -26.063 25.471 -2.197  1.00 18.19 ? 211 TYR A N   1 
ATOM   1812 C CA  . TYR A 1 211 ? -26.104 26.550 -3.167  1.00 18.25 ? 211 TYR A CA  1 
ATOM   1813 C C   . TYR A 1 211 ? -27.522 27.025 -3.454  1.00 15.53 ? 211 TYR A C   1 
ATOM   1814 O O   . TYR A 1 211 ? -27.687 28.056 -4.116  1.00 18.71 ? 211 TYR A O   1 
ATOM   1815 C CB  . TYR A 1 211 ? -25.435 26.100 -4.464  1.00 15.94 ? 211 TYR A CB  1 
ATOM   1816 C CG  . TYR A 1 211 ? -23.975 25.734 -4.306  1.00 18.41 ? 211 TYR A CG  1 
ATOM   1817 C CD1 . TYR A 1 211 ? -23.043 26.680 -3.891  1.00 23.12 ? 211 TYR A CD1 1 
ATOM   1818 C CD2 . TYR A 1 211 ? -23.526 24.447 -4.575  1.00 15.90 ? 211 TYR A CD2 1 
ATOM   1819 C CE1 . TYR A 1 211 ? -21.700 26.354 -3.748  1.00 20.52 ? 211 TYR A CE1 1 
ATOM   1820 C CE2 . TYR A 1 211 ? -22.184 24.113 -4.443  1.00 20.36 ? 211 TYR A CE2 1 
ATOM   1821 C CZ  . TYR A 1 211 ? -21.279 25.074 -4.028  1.00 22.02 ? 211 TYR A CZ  1 
ATOM   1822 O OH  . TYR A 1 211 ? -19.949 24.750 -3.897  1.00 23.74 ? 211 TYR A OH  1 
ATOM   1823 N N   . GLU A 1 212 ? -28.534 26.308 -2.962  1.00 16.30 ? 212 GLU A N   1 
ATOM   1824 C CA  . GLU A 1 212 ? -29.913 26.642 -3.306  1.00 15.46 ? 212 GLU A CA  1 
ATOM   1825 C C   . GLU A 1 212 ? -30.329 27.978 -2.699  1.00 18.69 ? 212 GLU A C   1 
ATOM   1826 O O   . GLU A 1 212 ? -31.055 28.747 -3.336  1.00 19.93 ? 212 GLU A O   1 
ATOM   1827 C CB  . GLU A 1 212 ? -30.848 25.501 -2.883  1.00 17.42 ? 212 GLU A CB  1 
ATOM   1828 C CG  . GLU A 1 212 ? -30.608 24.248 -3.734  1.00 20.77 ? 212 GLU A CG  1 
ATOM   1829 C CD  . GLU A 1 212 ? -31.498 23.069 -3.376  1.00 26.34 ? 212 GLU A CD  1 
ATOM   1830 O OE1 . GLU A 1 212 ? -31.131 21.923 -3.738  1.00 28.57 ? 212 GLU A OE1 1 
ATOM   1831 O OE2 . GLU A 1 212 ? -32.556 23.277 -2.753  1.00 23.06 ? 212 GLU A OE2 1 
ATOM   1832 N N   . THR A 1 213 ? -29.866 28.297 -1.482  1.00 17.97 ? 213 THR A N   1 
ATOM   1833 C CA  . THR A 1 213 ? -30.162 29.609 -0.920  1.00 18.03 ? 213 THR A CA  1 
ATOM   1834 C C   . THR A 1 213 ? -28.935 30.470 -0.631  1.00 20.77 ? 213 THR A C   1 
ATOM   1835 O O   . THR A 1 213 ? -29.100 31.669 -0.370  1.00 20.74 ? 213 THR A O   1 
ATOM   1836 C CB  . THR A 1 213 ? -31.019 29.480 0.357   1.00 22.45 ? 213 THR A CB  1 
ATOM   1837 O OG1 . THR A 1 213 ? -30.260 28.872 1.403   1.00 22.83 ? 213 THR A OG1 1 
ATOM   1838 C CG2 . THR A 1 213 ? -32.275 28.648 0.087   1.00 19.88 ? 213 THR A CG2 1 
ATOM   1839 N N   . THR A 1 214 ? -27.715 29.919 -0.694  1.00 18.37 ? 214 THR A N   1 
ATOM   1840 C CA  . THR A 1 214 ? -26.484 30.712 -0.621  1.00 16.93 ? 214 THR A CA  1 
ATOM   1841 C C   . THR A 1 214 ? -25.608 30.336 -1.811  1.00 23.07 ? 214 THR A C   1 
ATOM   1842 O O   . THR A 1 214 ? -24.605 29.620 -1.674  1.00 20.75 ? 214 THR A O   1 
ATOM   1843 C CB  . THR A 1 214 ? -25.758 30.521 0.713   1.00 20.25 ? 214 THR A CB  1 
ATOM   1844 O OG1 . THR A 1 214 ? -25.545 29.127 0.956   1.00 19.61 ? 214 THR A OG1 1 
ATOM   1845 C CG2 . THR A 1 214 ? -26.592 31.095 1.851   1.00 19.23 ? 214 THR A CG2 1 
ATOM   1846 N N   . PRO A 1 215 ? -25.945 30.827 -3.002  1.00 22.60 ? 215 PRO A N   1 
ATOM   1847 C CA  . PRO A 1 215 ? -25.210 30.398 -4.200  1.00 20.88 ? 215 PRO A CA  1 
ATOM   1848 C C   . PRO A 1 215 ? -23.749 30.811 -4.217  1.00 22.15 ? 215 PRO A C   1 
ATOM   1849 O O   . PRO A 1 215 ? -22.975 30.215 -4.975  1.00 23.63 ? 215 PRO A O   1 
ATOM   1850 C CB  . PRO A 1 215 ? -25.996 31.056 -5.341  1.00 23.51 ? 215 PRO A CB  1 
ATOM   1851 C CG  . PRO A 1 215 ? -26.636 32.255 -4.704  1.00 24.99 ? 215 PRO A CG  1 
ATOM   1852 C CD  . PRO A 1 215 ? -27.000 31.805 -3.314  1.00 21.91 ? 215 PRO A CD  1 
ATOM   1853 N N   . ASN A 1 216 ? -23.340 31.795 -3.408  1.00 22.25 ? 216 ASN A N   1 
ATOM   1854 C CA  . ASN A 1 216 ? -21.967 32.292 -3.411  1.00 28.85 ? 216 ASN A CA  1 
ATOM   1855 C C   . ASN A 1 216 ? -21.101 31.656 -2.331  1.00 26.99 ? 216 ASN A C   1 
ATOM   1856 O O   . ASN A 1 216 ? -19.946 32.067 -2.158  1.00 29.57 ? 216 ASN A O   1 
ATOM   1857 C CB  . ASN A 1 216 ? -21.947 33.813 -3.239  1.00 31.50 ? 216 ASN A CB  1 
ATOM   1858 C CG  . ASN A 1 216 ? -22.645 34.539 -4.368  1.00 36.84 ? 216 ASN A CG  1 
ATOM   1859 O OD1 . ASN A 1 216 ? -22.593 34.117 -5.522  1.00 37.10 ? 216 ASN A OD1 1 
ATOM   1860 N ND2 . ASN A 1 216 ? -23.309 35.641 -4.037  1.00 43.26 ? 216 ASN A ND2 1 
ATOM   1861 N N   . VAL A 1 217 ? -21.628 30.673 -1.602  1.00 22.30 ? 217 VAL A N   1 
ATOM   1862 C CA  . VAL A 1 217 ? -20.862 30.057 -0.522  1.00 23.31 ? 217 VAL A CA  1 
ATOM   1863 C C   . VAL A 1 217 ? -19.710 29.239 -1.102  1.00 24.05 ? 217 VAL A C   1 
ATOM   1864 O O   . VAL A 1 217 ? -19.809 28.653 -2.188  1.00 23.70 ? 217 VAL A O   1 
ATOM   1865 C CB  . VAL A 1 217 ? -21.773 29.193 0.370   1.00 20.37 ? 217 VAL A CB  1 
ATOM   1866 C CG1 . VAL A 1 217 ? -22.189 27.907 -0.347  1.00 19.71 ? 217 VAL A CG1 1 
ATOM   1867 C CG2 . VAL A 1 217 ? -21.067 28.857 1.677   1.00 24.39 ? 217 VAL A CG2 1 
ATOM   1868 N N   . LYS A 1 218 ? -18.593 29.223 -0.382  1.00 19.84 ? 218 LYS A N   1 
ATOM   1869 C CA  . LYS A 1 218 ? -17.441 28.403 -0.729  1.00 19.55 ? 218 LYS A CA  1 
ATOM   1870 C C   . LYS A 1 218 ? -17.401 27.218 0.225   1.00 22.28 ? 218 LYS A C   1 
ATOM   1871 O O   . LYS A 1 218 ? -17.516 27.395 1.440   1.00 21.51 ? 218 LYS A O   1 
ATOM   1872 C CB  . LYS A 1 218 ? -16.140 29.209 -0.650  1.00 23.60 ? 218 LYS A CB  1 
ATOM   1873 C CG  . LYS A 1 218 ? -16.156 30.529 -1.433  1.00 29.36 ? 218 LYS A CG  1 
ATOM   1874 C CD  . LYS A 1 218 ? -16.589 30.334 -2.882  1.00 37.64 ? 218 LYS A CD  1 
ATOM   1875 C CE  . LYS A 1 218 ? -15.701 31.125 -3.846  1.00 39.15 ? 218 LYS A CE  1 
ATOM   1876 N NZ  . LYS A 1 218 ? -15.744 30.594 -5.250  1.00 35.50 ? 218 LYS A NZ  1 
ATOM   1877 N N   . ILE A 1 219 ? -17.279 26.015 -0.324  1.00 23.18 ? 219 ILE A N   1 
ATOM   1878 C CA  . ILE A 1 219 ? -17.252 24.797 0.485   1.00 19.52 ? 219 ILE A CA  1 
ATOM   1879 C C   . ILE A 1 219 ? -16.118 23.915 -0.021  1.00 19.02 ? 219 ILE A C   1 
ATOM   1880 O O   . ILE A 1 219 ? -15.596 24.121 -1.130  1.00 21.70 ? 219 ILE A O   1 
ATOM   1881 C CB  . ILE A 1 219 ? -18.603 24.043 0.444   1.00 18.03 ? 219 ILE A CB  1 
ATOM   1882 C CG1 . ILE A 1 219 ? -18.898 23.518 -0.965  1.00 19.53 ? 219 ILE A CG1 1 
ATOM   1883 C CG2 . ILE A 1 219 ? -19.732 24.911 0.983   1.00 19.94 ? 219 ILE A CG2 1 
ATOM   1884 C CD1 . ILE A 1 219 ? -20.222 22.729 -1.067  1.00 21.83 ? 219 ILE A CD1 1 
ATOM   1885 N N   . PRO A 1 220 ? -15.677 22.943 0.791   1.00 20.92 ? 220 PRO A N   1 
ATOM   1886 C CA  . PRO A 1 220 ? -14.576 22.083 0.337   1.00 19.25 ? 220 PRO A CA  1 
ATOM   1887 C C   . PRO A 1 220 ? -15.026 21.069 -0.699  1.00 17.95 ? 220 PRO A C   1 
ATOM   1888 O O   . PRO A 1 220 ? -16.211 20.996 -1.044  1.00 18.12 ? 220 PRO A O   1 
ATOM   1889 C CB  . PRO A 1 220 ? -14.084 21.406 1.627   1.00 22.29 ? 220 PRO A CB  1 
ATOM   1890 C CG  . PRO A 1 220 ? -15.180 21.560 2.617   1.00 22.93 ? 220 PRO A CG  1 
ATOM   1891 C CD  . PRO A 1 220 ? -15.983 22.765 2.224   1.00 23.54 ? 220 PRO A CD  1 
ATOM   1892 N N   . ASP A 1 221 ? -14.067 20.326 -1.240  1.00 19.98 ? 221 ASP A N   1 
ATOM   1893 C CA  . ASP A 1 221 ? -14.331 19.300 -2.244  1.00 17.88 ? 221 ASP A CA  1 
ATOM   1894 C C   . ASP A 1 221 ? -14.860 18.058 -1.540  1.00 17.72 ? 221 ASP A C   1 
ATOM   1895 O O   . ASP A 1 221 ? -14.104 17.347 -0.870  1.00 18.50 ? 221 ASP A O   1 
ATOM   1896 C CB  . ASP A 1 221 ? -13.046 19.011 -3.009  1.00 18.66 ? 221 ASP A CB  1 
ATOM   1897 C CG  . ASP A 1 221 ? -13.164 17.842 -3.971  1.00 19.11 ? 221 ASP A CG  1 
ATOM   1898 O OD1 . ASP A 1 221 ? -14.290 17.429 -4.302  1.00 20.68 ? 221 ASP A OD1 1 
ATOM   1899 O OD2 . ASP A 1 221 ? -12.096 17.351 -4.409  1.00 23.52 ? 221 ASP A OD2 1 
ATOM   1900 N N   . PHE A 1 222 ? -16.155 17.783 -1.692  1.00 17.69 ? 222 PHE A N   1 
ATOM   1901 C CA  . PHE A 1 222 ? -16.736 16.572 -1.115  1.00 15.46 ? 222 PHE A CA  1 
ATOM   1902 C C   . PHE A 1 222 ? -16.425 15.394 -2.034  1.00 21.54 ? 222 PHE A C   1 
ATOM   1903 O O   . PHE A 1 222 ? -17.248 14.951 -2.840  1.00 22.03 ? 222 PHE A O   1 
ATOM   1904 C CB  . PHE A 1 222 ? -18.231 16.751 -0.902  1.00 18.36 ? 222 PHE A CB  1 
ATOM   1905 C CG  . PHE A 1 222 ? -18.575 17.516 0.343   1.00 16.05 ? 222 PHE A CG  1 
ATOM   1906 C CD1 . PHE A 1 222 ? -18.442 18.901 0.383   1.00 17.59 ? 222 PHE A CD1 1 
ATOM   1907 C CD2 . PHE A 1 222 ? -19.062 16.859 1.470   1.00 17.23 ? 222 PHE A CD2 1 
ATOM   1908 C CE1 . PHE A 1 222 ? -18.771 19.618 1.545   1.00 15.48 ? 222 PHE A CE1 1 
ATOM   1909 C CE2 . PHE A 1 222 ? -19.397 17.565 2.627   1.00 16.60 ? 222 PHE A CE2 1 
ATOM   1910 C CZ  . PHE A 1 222 ? -19.255 18.947 2.658   1.00 14.54 ? 222 PHE A CZ  1 
ATOM   1911 N N   . ALA A 1 223 ? -15.206 14.869 -1.893  1.00 19.86 ? 223 ALA A N   1 
ATOM   1912 C CA  . ALA A 1 223 ? -14.683 13.831 -2.777  1.00 20.02 ? 223 ALA A CA  1 
ATOM   1913 C C   . ALA A 1 223 ? -14.970 12.423 -2.267  1.00 20.51 ? 223 ALA A C   1 
ATOM   1914 O O   . ALA A 1 223 ? -14.220 11.482 -2.576  1.00 29.53 ? 223 ALA A O   1 
ATOM   1915 C CB  . ALA A 1 223 ? -13.180 14.024 -2.979  1.00 24.10 ? 223 ALA A CB  1 
ATOM   1916 N N   . VAL A 1 224 ? -16.034 12.265 -1.487  1.00 18.23 ? 224 VAL A N   1 
ATOM   1917 C CA  . VAL A 1 224 ? -16.476 10.979 -0.968  1.00 21.23 ? 224 VAL A CA  1 
ATOM   1918 C C   . VAL A 1 224 ? -17.982 11.088 -0.777  1.00 19.96 ? 224 VAL A C   1 
ATOM   1919 O O   . VAL A 1 224 ? -18.511 12.179 -0.561  1.00 22.18 ? 224 VAL A O   1 
ATOM   1920 C CB  . VAL A 1 224 ? -15.743 10.621 0.352   1.00 26.45 ? 224 VAL A CB  1 
ATOM   1921 C CG1 . VAL A 1 224 ? -16.170 11.562 1.486   1.00 22.35 ? 224 VAL A CG1 1 
ATOM   1922 C CG2 . VAL A 1 224 ? -15.981 9.167  0.736   1.00 31.72 ? 224 VAL A CG2 1 
ATOM   1923 N N   . SER A 1 225 ? -18.682 9.962  -0.882  1.00 19.26 ? 225 SER A N   1 
ATOM   1924 C CA  . SER A 1 225 ? -20.130 9.965  -0.705  1.00 17.67 ? 225 SER A CA  1 
ATOM   1925 C C   . SER A 1 225 ? -20.520 9.742  0.753   1.00 16.78 ? 225 SER A C   1 
ATOM   1926 O O   . SER A 1 225 ? -19.993 8.841  1.422   1.00 19.71 ? 225 SER A O   1 
ATOM   1927 C CB  . SER A 1 225 ? -20.781 8.895  -1.583  1.00 18.78 ? 225 SER A CB  1 
ATOM   1928 O OG  . SER A 1 225 ? -22.181 8.871  -1.354  1.00 19.62 ? 225 SER A OG  1 
ATOM   1929 N N   . PHE A 1 226 ? -21.453 10.563 1.238   1.00 14.87 ? 226 PHE A N   1 
ATOM   1930 C CA  . PHE A 1 226 ? -22.075 10.383 2.544   1.00 15.07 ? 226 PHE A CA  1 
ATOM   1931 C C   . PHE A 1 226 ? -23.506 9.872  2.440   1.00 16.42 ? 226 PHE A C   1 
ATOM   1932 O O   . PHE A 1 226 ? -24.235 9.893  3.442   1.00 15.20 ? 226 PHE A O   1 
ATOM   1933 C CB  . PHE A 1 226 ? -22.061 11.699 3.328   1.00 14.50 ? 226 PHE A CB  1 
ATOM   1934 C CG  . PHE A 1 226 ? -20.698 12.127 3.777   1.00 15.83 ? 226 PHE A CG  1 
ATOM   1935 C CD1 . PHE A 1 226 ? -20.123 11.571 4.913   1.00 17.11 ? 226 PHE A CD1 1 
ATOM   1936 C CD2 . PHE A 1 226 ? -19.989 13.086 3.070   1.00 17.11 ? 226 PHE A CD2 1 
ATOM   1937 C CE1 . PHE A 1 226 ? -18.865 11.973 5.345   1.00 17.58 ? 226 PHE A CE1 1 
ATOM   1938 C CE2 . PHE A 1 226 ? -18.723 13.491 3.486   1.00 18.57 ? 226 PHE A CE2 1 
ATOM   1939 C CZ  . PHE A 1 226 ? -18.157 12.931 4.626   1.00 17.63 ? 226 PHE A CZ  1 
ATOM   1940 N N   . ARG A 1 227 ? -23.931 9.409  1.260   1.00 17.15 ? 227 ARG A N   1 
ATOM   1941 C CA  . ARG A 1 227 ? -25.344 9.105  1.082   1.00 16.13 ? 227 ARG A CA  1 
ATOM   1942 C C   . ARG A 1 227 ? -25.761 7.885  1.892   1.00 14.96 ? 227 ARG A C   1 
ATOM   1943 O O   . ARG A 1 227 ? -26.823 7.891  2.522   1.00 17.99 ? 227 ARG A O   1 
ATOM   1944 C CB  . ARG A 1 227 ? -25.658 8.907  -0.399  1.00 14.78 ? 227 ARG A CB  1 
ATOM   1945 C CG  . ARG A 1 227 ? -25.617 10.208 -1.170  1.00 18.17 ? 227 ARG A CG  1 
ATOM   1946 C CD  . ARG A 1 227 ? -25.864 9.987  -2.655  1.00 18.29 ? 227 ARG A CD  1 
ATOM   1947 N NE  . ARG A 1 227 ? -27.196 9.467  -2.970  1.00 21.49 ? 227 ARG A NE  1 
ATOM   1948 C CZ  . ARG A 1 227 ? -28.296 10.209 -3.023  1.00 24.81 ? 227 ARG A CZ  1 
ATOM   1949 N NH1 . ARG A 1 227 ? -28.238 11.512 -2.762  1.00 21.32 ? 227 ARG A NH1 1 
ATOM   1950 N NH2 . ARG A 1 227 ? -29.460 9.646  -3.338  1.00 23.11 ? 227 ARG A NH2 1 
ATOM   1951 N N   . GLU A 1 228 ? -24.942 6.834  1.894   1.00 15.81 ? 228 GLU A N   1 
ATOM   1952 C CA  . GLU A 1 228 ? -25.265 5.671  2.710   1.00 17.57 ? 228 GLU A CA  1 
ATOM   1953 C C   . GLU A 1 228 ? -25.286 6.037  4.191   1.00 16.17 ? 228 GLU A C   1 
ATOM   1954 O O   . GLU A 1 228 ? -26.138 5.553  4.948   1.00 17.20 ? 228 GLU A O   1 
ATOM   1955 C CB  . GLU A 1 228 ? -24.269 4.545  2.427   1.00 25.48 ? 228 GLU A CB  1 
ATOM   1956 C CG  . GLU A 1 228 ? -24.510 3.258  3.210   1.00 38.97 ? 228 GLU A CG  1 
ATOM   1957 C CD  . GLU A 1 228 ? -23.622 2.110  2.749   1.00 57.83 ? 228 GLU A CD  1 
ATOM   1958 O OE1 . GLU A 1 228 ? -23.606 1.061  3.426   1.00 63.26 ? 228 GLU A OE1 1 
ATOM   1959 O OE2 . GLU A 1 228 ? -22.942 2.253  1.708   1.00 63.07 ? 228 GLU A OE2 1 
ATOM   1960 N N   . ASP A 1 229 ? -24.375 6.915  4.622   1.00 15.51 ? 229 ASP A N   1 
ATOM   1961 C CA  . ASP A 1 229 ? -24.386 7.315  6.026   1.00 15.69 ? 229 ASP A CA  1 
ATOM   1962 C C   . ASP A 1 229 ? -25.689 8.020  6.381   1.00 15.93 ? 229 ASP A C   1 
ATOM   1963 O O   . ASP A 1 229 ? -26.239 7.807  7.471   1.00 14.68 ? 229 ASP A O   1 
ATOM   1964 C CB  . ASP A 1 229 ? -23.196 8.219  6.347   1.00 14.79 ? 229 ASP A CB  1 
ATOM   1965 C CG  . ASP A 1 229 ? -21.908 7.449  6.527   1.00 17.28 ? 229 ASP A CG  1 
ATOM   1966 O OD1 . ASP A 1 229 ? -21.942 6.200  6.473   1.00 20.18 ? 229 ASP A OD1 1 
ATOM   1967 O OD2 . ASP A 1 229 ? -20.862 8.095  6.724   1.00 18.61 ? 229 ASP A OD2 1 
ATOM   1968 N N   . ALA A 1 230 ? -26.213 8.852  5.473   1.00 13.92 ? 230 ALA A N   1 
ATOM   1969 C CA  . ALA A 1 230 ? -27.496 9.498  5.736   1.00 17.31 ? 230 ALA A CA  1 
ATOM   1970 C C   . ALA A 1 230 ? -28.585 8.460  5.985   1.00 16.01 ? 230 ALA A C   1 
ATOM   1971 O O   . ALA A 1 230 ? -29.368 8.578  6.938   1.00 14.12 ? 230 ALA A O   1 
ATOM   1972 C CB  . ALA A 1 230 ? -27.871 10.413 4.570   1.00 14.47 ? 230 ALA A CB  1 
ATOM   1973 N N   . SER A 1 231 ? -28.636 7.426  5.144   1.00 14.60 ? 231 SER A N   1 
ATOM   1974 C CA  . SER A 1 231 ? -29.586 6.337  5.363   1.00 15.21 ? 231 SER A CA  1 
ATOM   1975 C C   . SER A 1 231 ? -29.357 5.656  6.704   1.00 13.33 ? 231 SER A C   1 
ATOM   1976 O O   . SER A 1 231 ? -30.314 5.376  7.433   1.00 16.34 ? 231 SER A O   1 
ATOM   1977 C CB  . SER A 1 231 ? -29.487 5.308  4.234   1.00 21.71 ? 231 SER A CB  1 
ATOM   1978 O OG  . SER A 1 231 ? -30.422 5.576  3.214   1.00 32.67 ? 231 SER A OG  1 
ATOM   1979 N N   . LYS A 1 232 ? -28.091 5.419  7.062   1.00 14.21 ? 232 LYS A N   1 
ATOM   1980 C CA  . LYS A 1 232 ? -27.780 4.732  8.313   1.00 13.92 ? 232 LYS A CA  1 
ATOM   1981 C C   . LYS A 1 232 ? -28.246 5.525  9.527   1.00 11.74 ? 232 LYS A C   1 
ATOM   1982 O O   . LYS A 1 232 ? -28.747 4.942  10.496  1.00 13.90 ? 232 LYS A O   1 
ATOM   1983 C CB  . LYS A 1 232 ? -26.279 4.459  8.405   1.00 18.21 ? 232 LYS A CB  1 
ATOM   1984 C CG  . LYS A 1 232 ? -25.799 3.298  7.570   1.00 26.35 ? 232 LYS A CG  1 
ATOM   1985 C CD  . LYS A 1 232 ? -24.388 2.885  7.975   1.00 34.52 ? 232 LYS A CD  1 
ATOM   1986 C CE  . LYS A 1 232 ? -24.339 2.363  9.405   1.00 37.16 ? 232 LYS A CE  1 
ATOM   1987 N NZ  . LYS A 1 232 ? -23.127 1.511  9.652   1.00 44.24 ? 232 LYS A NZ  1 
ATOM   1988 N N   . HIS A 1 233 ? -28.083 6.858  9.508   1.00 13.44 ? 233 HIS A N   1 
ATOM   1989 C CA  . HIS A 1 233 ? -28.566 7.654  10.634  1.00 11.10 ? 233 HIS A CA  1 
ATOM   1990 C C   . HIS A 1 233 ? -30.059 7.441  10.849  1.00 15.00 ? 233 HIS A C   1 
ATOM   1991 O O   . HIS A 1 233 ? -30.522 7.326  11.990  1.00 13.86 ? 233 HIS A O   1 
ATOM   1992 C CB  . HIS A 1 233 ? -28.297 9.151  10.421  1.00 11.03 ? 233 HIS A CB  1 
ATOM   1993 C CG  . HIS A 1 233 ? -26.873 9.588  10.660  1.00 12.09 ? 233 HIS A CG  1 
ATOM   1994 N ND1 . HIS A 1 233 ? -26.405 9.993  11.895  1.00 15.42 ? 233 HIS A ND1 1 
ATOM   1995 C CD2 . HIS A 1 233 ? -25.846 9.774  9.792   1.00 12.62 ? 233 HIS A CD2 1 
ATOM   1996 C CE1 . HIS A 1 233 ? -25.142 10.367 11.785  1.00 15.03 ? 233 HIS A CE1 1 
ATOM   1997 N NE2 . HIS A 1 233 ? -24.773 10.235 10.521  1.00 13.69 ? 233 HIS A NE2 1 
ATOM   1998 N N   . VAL A 1 234 ? -30.835 7.402  9.762   1.00 13.99 ? 234 VAL A N   1 
ATOM   1999 C CA  . VAL A 1 234 ? -32.280 7.227  9.887   1.00 15.47 ? 234 VAL A CA  1 
ATOM   2000 C C   . VAL A 1 234 ? -32.605 5.815  10.350  1.00 12.15 ? 234 VAL A C   1 
ATOM   2001 O O   . VAL A 1 234 ? -33.438 5.614  11.242  1.00 12.79 ? 234 VAL A O   1 
ATOM   2002 C CB  . VAL A 1 234 ? -32.986 7.549  8.558   1.00 14.50 ? 234 VAL A CB  1 
ATOM   2003 C CG1 . VAL A 1 234 ? -34.494 7.372  8.714   1.00 15.61 ? 234 VAL A CG1 1 
ATOM   2004 C CG2 . VAL A 1 234 ? -32.659 8.966  8.118   1.00 13.42 ? 234 VAL A CG2 1 
ATOM   2005 N N   . GLU A 1 235 ? -31.954 4.816  9.751   1.00 12.37 ? 235 GLU A N   1 
ATOM   2006 C CA  . GLU A 1 235 ? -32.273 3.433  10.083  1.00 14.75 ? 235 GLU A CA  1 
ATOM   2007 C C   . GLU A 1 235 ? -31.914 3.109  11.525  1.00 14.84 ? 235 GLU A C   1 
ATOM   2008 O O   . GLU A 1 235 ? -32.690 2.458  12.237  1.00 14.65 ? 235 GLU A O   1 
ATOM   2009 C CB  . GLU A 1 235 ? -31.553 2.477  9.132   1.00 19.84 ? 235 GLU A CB  1 
ATOM   2010 C CG  . GLU A 1 235 ? -32.108 1.063  9.167   1.00 33.08 ? 235 GLU A CG  1 
ATOM   2011 C CD  . GLU A 1 235 ? -33.609 1.024  8.920   1.00 41.15 ? 235 GLU A CD  1 
ATOM   2012 O OE1 . GLU A 1 235 ? -34.064 1.571  7.895   1.00 41.14 ? 235 GLU A OE1 1 
ATOM   2013 O OE2 . GLU A 1 235 ? -34.338 0.452  9.758   1.00 46.01 ? 235 GLU A OE2 1 
ATOM   2014 N N   . LEU A 1 236 ? -30.734 3.535  11.970  1.00 15.64 ? 236 LEU A N   1 
ATOM   2015 C CA  . LEU A 1 236 ? -30.344 3.277  13.351  1.00 13.40 ? 236 LEU A CA  1 
ATOM   2016 C C   . LEU A 1 236 ? -31.293 3.965  14.327  1.00 12.89 ? 236 LEU A C   1 
ATOM   2017 O O   . LEU A 1 236 ? -31.595 3.425  15.399  1.00 15.33 ? 236 LEU A O   1 
ATOM   2018 C CB  . LEU A 1 236 ? -28.913 3.745  13.580  1.00 15.42 ? 236 LEU A CB  1 
ATOM   2019 C CG  . LEU A 1 236 ? -27.870 2.883  12.868  1.00 18.00 ? 236 LEU A CG  1 
ATOM   2020 C CD1 . LEU A 1 236 ? -26.498 3.512  13.051  1.00 20.86 ? 236 LEU A CD1 1 
ATOM   2021 C CD2 . LEU A 1 236 ? -27.887 1.451  13.391  1.00 18.89 ? 236 LEU A CD2 1 
ATOM   2022 N N   . ALA A 1 237 ? -31.755 5.167  13.980  1.00 12.70 ? 237 ALA A N   1 
ATOM   2023 C CA  . ALA A 1 237 ? -32.702 5.877  14.839  1.00 11.05 ? 237 ALA A CA  1 
ATOM   2024 C C   . ALA A 1 237 ? -34.029 5.134  14.952  1.00 13.42 ? 237 ALA A C   1 
ATOM   2025 O O   . ALA A 1 237 ? -34.642 5.106  16.026  1.00 13.09 ? 237 ALA A O   1 
ATOM   2026 C CB  . ALA A 1 237 ? -32.933 7.288  14.303  1.00 12.14 ? 237 ALA A CB  1 
ATOM   2027 N N   . LYS A 1 238 ? -34.510 4.552  13.845  1.00 12.53 ? 238 LYS A N   1 
ATOM   2028 C CA  . LYS A 1 238 ? -35.720 3.729  13.905  1.00 14.54 ? 238 LYS A CA  1 
ATOM   2029 C C   . LYS A 1 238 ? -35.547 2.554  14.855  1.00 12.95 ? 238 LYS A C   1 
ATOM   2030 O O   . LYS A 1 238 ? -36.465 2.219  15.618  1.00 15.10 ? 238 LYS A O   1 
ATOM   2031 C CB  . LYS A 1 238 ? -36.087 3.215  12.511  1.00 15.24 ? 238 LYS A CB  1 
ATOM   2032 C CG  . LYS A 1 238 ? -36.478 4.308  11.538  1.00 13.95 ? 238 LYS A CG  1 
ATOM   2033 C CD  . LYS A 1 238 ? -36.660 3.792  10.112  1.00 17.95 ? 238 LYS A CD  1 
ATOM   2034 C CE  . LYS A 1 238 ? -37.652 2.641  10.034  1.00 21.28 ? 238 LYS A CE  1 
ATOM   2035 N NZ  . LYS A 1 238 ? -37.918 2.249  8.611   1.00 21.23 ? 238 LYS A NZ  1 
ATOM   2036 N N   . GLU A 1 239 ? -34.368 1.921  14.836  1.00 14.34 ? 239 GLU A N   1 
ATOM   2037 C CA  . GLU A 1 239 ? -34.098 0.804  15.736  1.00 16.72 ? 239 GLU A CA  1 
ATOM   2038 C C   . GLU A 1 239 ? -34.119 1.245  17.192  1.00 14.28 ? 239 GLU A C   1 
ATOM   2039 O O   . GLU A 1 239 ? -34.702 0.568  18.046  1.00 16.17 ? 239 GLU A O   1 
ATOM   2040 C CB  . GLU A 1 239 ? -32.748 0.179  15.389  1.00 16.30 ? 239 GLU A CB  1 
ATOM   2041 C CG  . GLU A 1 239 ? -32.735 -0.526 14.043  1.00 25.04 ? 239 GLU A CG  1 
ATOM   2042 C CD  . GLU A 1 239 ? -31.336 -0.947 13.617  1.00 31.38 ? 239 GLU A CD  1 
ATOM   2043 O OE1 . GLU A 1 239 ? -31.176 -1.396 12.465  1.00 38.73 ? 239 GLU A OE1 1 
ATOM   2044 O OE2 . GLU A 1 239 ? -30.394 -0.827 14.432  1.00 32.10 ? 239 GLU A OE2 1 
ATOM   2045 N N   . LYS A 1 240 ? -33.468 2.373  17.500  1.00 13.90 ? 240 LYS A N   1 
ATOM   2046 C CA  . LYS A 1 240 ? -33.413 2.825  18.888  1.00 14.68 ? 240 LYS A CA  1 
ATOM   2047 C C   . LYS A 1 240 ? -34.788 3.257  19.367  1.00 13.35 ? 240 LYS A C   1 
ATOM   2048 O O   . LYS A 1 240 ? -35.194 2.940  20.491  1.00 14.03 ? 240 LYS A O   1 
ATOM   2049 C CB  . LYS A 1 240 ? -32.402 3.966  19.038  1.00 16.80 ? 240 LYS A CB  1 
ATOM   2050 C CG  . LYS A 1 240 ? -32.110 4.321  20.500  1.00 16.92 ? 240 LYS A CG  1 
ATOM   2051 C CD  . LYS A 1 240 ? -31.390 3.188  21.206  1.00 21.74 ? 240 LYS A CD  1 
ATOM   2052 C CE  . LYS A 1 240 ? -30.995 3.576  22.628  1.00 22.07 ? 240 LYS A CE  1 
ATOM   2053 N NZ  . LYS A 1 240 ? -30.392 2.427  23.366  1.00 24.46 ? 240 LYS A NZ  1 
ATOM   2054 N N   . TYR A 1 241 ? -35.529 3.971  18.515  1.00 14.13 ? 241 TYR A N   1 
ATOM   2055 C CA  . TYR A 1 241 ? -36.894 4.342  18.863  1.00 16.66 ? 241 TYR A CA  1 
ATOM   2056 C C   . TYR A 1 241 ? -37.750 3.107  19.115  1.00 14.77 ? 241 TYR A C   1 
ATOM   2057 O O   . TYR A 1 241 ? -38.553 3.079  20.058  1.00 14.83 ? 241 TYR A O   1 
ATOM   2058 C CB  . TYR A 1 241 ? -37.497 5.205  17.755  1.00 14.63 ? 241 TYR A CB  1 
ATOM   2059 C CG  . TYR A 1 241 ? -38.851 5.770  18.097  1.00 13.01 ? 241 TYR A CG  1 
ATOM   2060 C CD1 . TYR A 1 241 ? -40.005 5.029  17.883  1.00 15.03 ? 241 TYR A CD1 1 
ATOM   2061 C CD2 . TYR A 1 241 ? -38.983 7.057  18.612  1.00 13.71 ? 241 TYR A CD2 1 
ATOM   2062 C CE1 . TYR A 1 241 ? -41.253 5.529  18.193  1.00 14.72 ? 241 TYR A CE1 1 
ATOM   2063 C CE2 . TYR A 1 241 ? -40.243 7.578  18.911  1.00 14.93 ? 241 TYR A CE2 1 
ATOM   2064 C CZ  . TYR A 1 241 ? -41.367 6.815  18.692  1.00 16.86 ? 241 TYR A CZ  1 
ATOM   2065 O OH  . TYR A 1 241 ? -42.609 7.310  19.001  1.00 17.71 ? 241 TYR A OH  1 
ATOM   2066 N N   . PHE A 1 242 ? -37.585 2.063  18.297  1.00 13.63 ? 242 PHE A N   1 
ATOM   2067 C CA  . PHE A 1 242 ? -38.368 0.853  18.523  1.00 14.97 ? 242 PHE A CA  1 
ATOM   2068 C C   . PHE A 1 242 ? -38.051 0.238  19.880  1.00 14.84 ? 242 PHE A C   1 
ATOM   2069 O O   . PHE A 1 242 ? -38.953 -0.232 20.583  1.00 15.16 ? 242 PHE A O   1 
ATOM   2070 C CB  . PHE A 1 242 ? -38.125 -0.165 17.411  1.00 14.69 ? 242 PHE A CB  1 
ATOM   2071 C CG  . PHE A 1 242 ? -38.971 -1.397 17.538  1.00 15.82 ? 242 PHE A CG  1 
ATOM   2072 C CD1 . PHE A 1 242 ? -38.578 -2.439 18.358  1.00 15.67 ? 242 PHE A CD1 1 
ATOM   2073 C CD2 . PHE A 1 242 ? -40.168 -1.513 16.848  1.00 18.26 ? 242 PHE A CD2 1 
ATOM   2074 C CE1 . PHE A 1 242 ? -39.347 -3.583 18.492  1.00 18.57 ? 242 PHE A CE1 1 
ATOM   2075 C CE2 . PHE A 1 242 ? -40.950 -2.665 16.967  1.00 19.32 ? 242 PHE A CE2 1 
ATOM   2076 C CZ  . PHE A 1 242 ? -40.545 -3.701 17.797  1.00 19.15 ? 242 PHE A CZ  1 
ATOM   2077 N N   . GLU A 1 243 ? -36.776 0.240  20.272  1.00 16.27 ? 243 GLU A N   1 
ATOM   2078 C CA  . GLU A 1 243 ? -36.411 -0.318 21.573  1.00 16.97 ? 243 GLU A CA  1 
ATOM   2079 C C   . GLU A 1 243 ? -37.127 0.405  22.703  1.00 14.23 ? 243 GLU A C   1 
ATOM   2080 O O   . GLU A 1 243 ? -37.679 -0.233 23.611  1.00 16.07 ? 243 GLU A O   1 
ATOM   2081 C CB  . GLU A 1 243 ? -34.902 -0.243 21.783  1.00 18.46 ? 243 GLU A CB  1 
ATOM   2082 C CG  . GLU A 1 243 ? -34.500 -0.840 23.108  1.00 22.60 ? 243 GLU A CG  1 
ATOM   2083 C CD  . GLU A 1 243 ? -33.158 -0.360 23.621  1.00 30.89 ? 243 GLU A CD  1 
ATOM   2084 O OE1 . GLU A 1 243 ? -32.763 -0.818 24.713  1.00 34.43 ? 243 GLU A OE1 1 
ATOM   2085 O OE2 . GLU A 1 243 ? -32.491 0.440  22.941  1.00 27.13 ? 243 GLU A OE2 1 
ATOM   2086 N N   . ILE A 1 244 ? -37.144 1.740  22.650  1.00 14.75 ? 244 ILE A N   1 
ATOM   2087 C CA  . ILE A 1 244 ? -37.665 2.528  23.763  1.00 17.52 ? 244 ILE A CA  1 
ATOM   2088 C C   . ILE A 1 244 ? -39.185 2.572  23.751  1.00 17.64 ? 244 ILE A C   1 
ATOM   2089 O O   . ILE A 1 244 ? -39.821 2.463  24.802  1.00 17.16 ? 244 ILE A O   1 
ATOM   2090 C CB  . ILE A 1 244 ? -37.075 3.951  23.744  1.00 15.93 ? 244 ILE A CB  1 
ATOM   2091 C CG1 . ILE A 1 244 ? -35.545 3.913  23.759  1.00 18.44 ? 244 ILE A CG1 1 
ATOM   2092 C CG2 . ILE A 1 244 ? -37.637 4.770  24.908  1.00 18.54 ? 244 ILE A CG2 1 
ATOM   2093 C CD1 . ILE A 1 244 ? -34.952 3.132  24.938  1.00 19.16 ? 244 ILE A CD1 1 
ATOM   2094 N N   . PHE A 1 245 ? -39.793 2.737  22.573  1.00 13.97 ? 245 PHE A N   1 
ATOM   2095 C CA  . PHE A 1 245 ? -41.215 3.029  22.480  1.00 17.09 ? 245 PHE A CA  1 
ATOM   2096 C C   . PHE A 1 245 ? -42.047 1.956  21.799  1.00 20.12 ? 245 PHE A C   1 
ATOM   2097 O O   . PHE A 1 245 ? -43.280 2.049  21.837  1.00 20.66 ? 245 PHE A O   1 
ATOM   2098 C CB  . PHE A 1 245 ? -41.420 4.368  21.760  1.00 14.38 ? 245 PHE A CB  1 
ATOM   2099 C CG  . PHE A 1 245 ? -40.813 5.506  22.499  1.00 16.33 ? 245 PHE A CG  1 
ATOM   2100 C CD1 . PHE A 1 245 ? -41.357 5.923  23.705  1.00 17.78 ? 245 PHE A CD1 1 
ATOM   2101 C CD2 . PHE A 1 245 ? -39.679 6.128  22.025  1.00 16.96 ? 245 PHE A CD2 1 
ATOM   2102 C CE1 . PHE A 1 245 ? -40.789 6.965  24.415  1.00 20.31 ? 245 PHE A CE1 1 
ATOM   2103 C CE2 . PHE A 1 245 ? -39.097 7.171  22.728  1.00 19.84 ? 245 PHE A CE2 1 
ATOM   2104 C CZ  . PHE A 1 245 ? -39.648 7.592  23.920  1.00 19.92 ? 245 PHE A CZ  1 
ATOM   2105 N N   . GLY A 1 246 ? -41.431 0.946  21.197  1.00 16.95 ? 246 GLY A N   1 
ATOM   2106 C CA  . GLY A 1 246 ? -42.193 -0.202 20.749  1.00 18.62 ? 246 GLY A CA  1 
ATOM   2107 C C   . GLY A 1 246 ? -42.876 -0.059 19.410  1.00 17.14 ? 246 GLY A C   1 
ATOM   2108 O O   . GLY A 1 246 ? -43.785 -0.839 19.106  1.00 20.77 ? 246 GLY A O   1 
ATOM   2109 N N   . GLU A 1 247 ? -42.476 0.913  18.599  1.00 17.35 ? 247 GLU A N   1 
ATOM   2110 C CA  . GLU A 1 247 ? -42.976 1.039  17.236  1.00 20.79 ? 247 GLU A CA  1 
ATOM   2111 C C   . GLU A 1 247 ? -41.866 1.646  16.396  1.00 16.32 ? 247 GLU A C   1 
ATOM   2112 O O   . GLU A 1 247 ? -40.918 2.233  16.921  1.00 17.11 ? 247 GLU A O   1 
ATOM   2113 C CB  . GLU A 1 247 ? -44.228 1.932  17.130  1.00 31.41 ? 247 GLU A CB  1 
ATOM   2114 C CG  . GLU A 1 247 ? -45.107 2.011  18.367  1.00 44.03 ? 247 GLU A CG  1 
ATOM   2115 C CD  . GLU A 1 247 ? -46.063 3.195  18.340  1.00 50.18 ? 247 GLU A CD  1 
ATOM   2116 O OE1 . GLU A 1 247 ? -45.640 4.302  17.942  1.00 43.07 ? 247 GLU A OE1 1 
ATOM   2117 O OE2 . GLU A 1 247 ? -47.243 3.013  18.713  1.00 55.07 ? 247 GLU A OE2 1 
ATOM   2118 N N   . HIS A 1 248 ? -41.981 1.496  15.086  1.00 18.21 ? 248 HIS A N   1 
ATOM   2119 C CA  . HIS A 1 248 ? -41.141 2.304  14.220  1.00 18.94 ? 248 HIS A CA  1 
ATOM   2120 C C   . HIS A 1 248 ? -41.687 3.727  14.212  1.00 20.62 ? 248 HIS A C   1 
ATOM   2121 O O   . HIS A 1 248 ? -42.908 3.917  14.154  1.00 20.79 ? 248 HIS A O   1 
ATOM   2122 C CB  . HIS A 1 248 ? -41.109 1.741  12.802  1.00 23.37 ? 248 HIS A CB  1 
ATOM   2123 C CG  . HIS A 1 248 ? -40.495 0.381  12.720  1.00 35.10 ? 248 HIS A CG  1 
ATOM   2124 N ND1 . HIS A 1 248 ? -39.138 0.175  12.833  1.00 39.00 ? 248 HIS A ND1 1 
ATOM   2125 C CD2 . HIS A 1 248 ? -41.053 -0.844 12.572  1.00 40.64 ? 248 HIS A CD2 1 
ATOM   2126 C CE1 . HIS A 1 248 ? -38.884 -1.117 12.737  1.00 41.18 ? 248 HIS A CE1 1 
ATOM   2127 N NE2 . HIS A 1 248 ? -40.028 -1.758 12.580  1.00 40.39 ? 248 HIS A NE2 1 
ATOM   2128 N N   . PRO A 1 249 ? -40.822 4.735  14.295  1.00 18.03 ? 249 PRO A N   1 
ATOM   2129 C CA  . PRO A 1 249 ? -41.314 6.117  14.365  1.00 16.08 ? 249 PRO A CA  1 
ATOM   2130 C C   . PRO A 1 249 ? -41.902 6.536  13.026  1.00 18.51 ? 249 PRO A C   1 
ATOM   2131 O O   . PRO A 1 249 ? -41.277 6.365  11.978  1.00 25.77 ? 249 PRO A O   1 
ATOM   2132 C CB  . PRO A 1 249 ? -40.060 6.929  14.716  1.00 16.66 ? 249 PRO A CB  1 
ATOM   2133 C CG  . PRO A 1 249 ? -38.921 6.109  14.158  1.00 18.51 ? 249 PRO A CG  1 
ATOM   2134 C CD  . PRO A 1 249 ? -39.349 4.661  14.287  1.00 16.62 ? 249 PRO A CD  1 
ATOM   2135 N N   . VAL A 1 250 ? -43.124 7.070  13.061  1.00 17.38 ? 250 VAL A N   1 
ATOM   2136 C CA  . VAL A 1 250 ? -43.717 7.630  11.853  1.00 19.46 ? 250 VAL A CA  1 
ATOM   2137 C C   . VAL A 1 250 ? -43.560 9.141  11.792  1.00 17.47 ? 250 VAL A C   1 
ATOM   2138 O O   . VAL A 1 250 ? -43.876 9.744  10.753  1.00 17.51 ? 250 VAL A O   1 
ATOM   2139 C CB  . VAL A 1 250 ? -45.205 7.236  11.710  1.00 22.56 ? 250 VAL A CB  1 
ATOM   2140 C CG1 . VAL A 1 250 ? -45.354 5.701  11.605  1.00 23.09 ? 250 VAL A CG1 1 
ATOM   2141 C CG2 . VAL A 1 250 ? -46.009 7.768  12.875  1.00 23.75 ? 250 VAL A CG2 1 
ATOM   2142 N N   . TYR A 1 251 ? -43.091 9.770  12.864  1.00 15.63 ? 251 TYR A N   1 
ATOM   2143 C CA  . TYR A 1 251 ? -42.754 11.189 12.891  1.00 15.70 ? 251 TYR A CA  1 
ATOM   2144 C C   . TYR A 1 251 ? -41.276 11.349 13.186  1.00 14.17 ? 251 TYR A C   1 
ATOM   2145 O O   . TYR A 1 251 ? -40.742 10.707 14.103  1.00 15.95 ? 251 TYR A O   1 
ATOM   2146 C CB  . TYR A 1 251 ? -43.519 11.945 13.977  1.00 21.37 ? 251 TYR A CB  1 
ATOM   2147 C CG  . TYR A 1 251 ? -44.893 11.447 14.148  1.00 22.91 ? 251 TYR A CG  1 
ATOM   2148 C CD1 . TYR A 1 251 ? -45.827 11.692 13.169  1.00 28.10 ? 251 TYR A CD1 1 
ATOM   2149 C CD2 . TYR A 1 251 ? -45.266 10.720 15.274  1.00 31.41 ? 251 TYR A CD2 1 
ATOM   2150 C CE1 . TYR A 1 251 ? -47.074 11.245 13.282  1.00 36.26 ? 251 TYR A CE1 1 
ATOM   2151 C CE2 . TYR A 1 251 ? -46.543 10.265 15.397  1.00 29.60 ? 251 TYR A CE2 1 
ATOM   2152 C CZ  . TYR A 1 251 ? -47.434 10.543 14.382  1.00 36.46 ? 251 TYR A CZ  1 
ATOM   2153 O OH  . TYR A 1 251 ? -48.715 10.132 14.393  1.00 41.98 ? 251 TYR A OH  1 
ATOM   2154 N N   . MET A 1 252 ? -40.613 12.239 12.450  1.00 12.15 ? 252 MET A N   1 
ATOM   2155 C CA  . MET A 1 252 ? -39.253 12.605 12.809  1.00 11.85 ? 252 MET A CA  1 
ATOM   2156 C C   . MET A 1 252 ? -39.101 14.111 12.775  1.00 11.46 ? 252 MET A C   1 
ATOM   2157 O O   . MET A 1 252 ? -39.736 14.802 11.970  1.00 13.50 ? 252 MET A O   1 
ATOM   2158 C CB  . MET A 1 252 ? -38.201 11.971 11.882  1.00 15.50 ? 252 MET A CB  1 
ATOM   2159 C CG  . MET A 1 252 ? -37.850 10.535 12.260  1.00 19.11 ? 252 MET A CG  1 
ATOM   2160 S SD  . MET A 1 252 ? -36.337 10.009 11.435  1.00 17.97 ? 252 MET A SD  1 
ATOM   2161 C CE  . MET A 1 252 ? -36.239 8.321  12.041  1.00 19.48 ? 252 MET A CE  1 
ATOM   2162 N N   . TRP A 1 253 ? -38.243 14.606 13.661  1.00 10.84 ? 253 TRP A N   1 
ATOM   2163 C CA  . TRP A 1 253 ? -37.808 15.992 13.599  1.00 12.52 ? 253 TRP A CA  1 
ATOM   2164 C C   . TRP A 1 253 ? -36.495 16.065 12.824  1.00 11.25 ? 253 TRP A C   1 
ATOM   2165 O O   . TRP A 1 253 ? -35.490 15.477 13.264  1.00 11.67 ? 253 TRP A O   1 
ATOM   2166 C CB  . TRP A 1 253 ? -37.623 16.566 15.001  1.00 12.02 ? 253 TRP A CB  1 
ATOM   2167 C CG  . TRP A 1 253 ? -36.953 17.914 14.970  1.00 10.51 ? 253 TRP A CG  1 
ATOM   2168 C CD1 . TRP A 1 253 ? -35.701 18.238 15.451  1.00 11.74 ? 253 TRP A CD1 1 
ATOM   2169 C CD2 . TRP A 1 253 ? -37.485 19.115 14.408  1.00 12.39 ? 253 TRP A CD2 1 
ATOM   2170 N NE1 . TRP A 1 253 ? -35.437 19.568 15.212  1.00 12.60 ? 253 TRP A NE1 1 
ATOM   2171 C CE2 . TRP A 1 253 ? -36.515 20.124 14.574  1.00 10.09 ? 253 TRP A CE2 1 
ATOM   2172 C CE3 . TRP A 1 253 ? -38.695 19.440 13.774  1.00 14.16 ? 253 TRP A CE3 1 
ATOM   2173 C CZ2 . TRP A 1 253 ? -36.711 21.424 14.131  1.00 12.75 ? 253 TRP A CZ2 1 
ATOM   2174 C CZ3 . TRP A 1 253 ? -38.887 20.727 13.337  1.00 11.04 ? 253 TRP A CZ3 1 
ATOM   2175 C CH2 . TRP A 1 253 ? -37.897 21.714 13.518  1.00 11.92 ? 253 TRP A CH2 1 
ATOM   2176 N N   . PRO A 1 254 ? -36.446 16.738 11.683  1.00 9.70  ? 254 PRO A N   1 
ATOM   2177 C CA  . PRO A 1 254 ? -35.174 16.858 10.968  1.00 11.56 ? 254 PRO A CA  1 
ATOM   2178 C C   . PRO A 1 254 ? -34.258 17.811 11.715  1.00 9.37  ? 254 PRO A C   1 
ATOM   2179 O O   . PRO A 1 254 ? -34.673 18.926 12.072  1.00 11.65 ? 254 PRO A O   1 
ATOM   2180 C CB  . PRO A 1 254 ? -35.584 17.414 9.595   1.00 13.19 ? 254 PRO A CB  1 
ATOM   2181 C CG  . PRO A 1 254 ? -36.851 18.178 9.864   1.00 16.11 ? 254 PRO A CG  1 
ATOM   2182 C CD  . PRO A 1 254 ? -37.543 17.470 11.024  1.00 13.83 ? 254 PRO A CD  1 
ATOM   2183 N N   . PRO A 1 255 ? -33.025 17.405 12.014  1.00 9.49  ? 255 PRO A N   1 
ATOM   2184 C CA  . PRO A 1 255 ? -32.135 18.278 12.788  1.00 10.67 ? 255 PRO A CA  1 
ATOM   2185 C C   . PRO A 1 255 ? -32.008 19.649 12.140  1.00 12.39 ? 255 PRO A C   1 
ATOM   2186 O O   . PRO A 1 255 ? -31.857 19.765 10.919  1.00 11.56 ? 255 PRO A O   1 
ATOM   2187 C CB  . PRO A 1 255 ? -30.802 17.525 12.770  1.00 10.56 ? 255 PRO A CB  1 
ATOM   2188 C CG  . PRO A 1 255 ? -31.215 16.088 12.697  1.00 9.93  ? 255 PRO A CG  1 
ATOM   2189 C CD  . PRO A 1 255 ? -32.436 16.077 11.777  1.00 10.02 ? 255 PRO A CD  1 
ATOM   2190 N N   . GLN A 1 256 ? -32.092 20.699 12.964  1.00 12.55 ? 256 GLN A N   1 
ATOM   2191 C CA  . GLN A 1 256 ? -32.018 22.088 12.513  1.00 12.41 ? 256 GLN A CA  1 
ATOM   2192 C C   . GLN A 1 256 ? -33.130 22.417 11.544  1.00 13.44 ? 256 GLN A C   1 
ATOM   2193 O O   . GLN A 1 256 ? -33.001 23.274 10.810  1.00 12.29 ? 256 GLN A O   1 
ATOM   2194 C CB  . GLN A 1 256 ? -30.637 22.403 11.908  1.00 13.06 ? 256 GLN A CB  1 
ATOM   2195 C CG  . GLN A 1 256 ? -29.463 22.014 12.777  1.00 19.77 ? 256 GLN A CG  1 
ATOM   2196 C CD  . GLN A 1 256 ? -29.467 22.718 14.113  1.00 21.91 ? 256 GLN A CD  1 
ATOM   2197 O OE1 . GLN A 1 256 ? -30.010 23.740 14.282  1.00 25.86 ? 256 GLN A OE1 1 
ATOM   2198 N NE2 . GLN A 1 256 ? -28.830 22.160 15.004  1.00 19.35 ? 256 GLN A NE2 1 
ATOM   2199 N N   . ALA A 1 257 ? -34.217 21.685 11.655  1.00 11.14 ? 257 ALA A N   1 
ATOM   2200 C CA  . ALA A 1 257 ? -35.345 21.809 10.733  1.00 11.69 ? 257 ALA A CA  1 
ATOM   2201 C C   . ALA A 1 257 ? -34.921 21.574 9.293   1.00 13.84 ? 257 ALA A C   1 
ATOM   2202 O O   . ALA A 1 257 ? -35.611 21.997 8.358   1.00 13.40 ? 257 ALA A O   1 
ATOM   2203 C CB  . ALA A 1 257 ? -36.027 23.181 10.864  1.00 11.77 ? 257 ALA A CB  1 
ATOM   2204 N N   . SER A 1 258 ? -33.811 20.877 9.077   1.00 12.38 ? 258 SER A N   1 
ATOM   2205 C CA  . SER A 1 258 ? -33.183 20.924 7.761   1.00 11.15 ? 258 SER A CA  1 
ATOM   2206 C C   . SER A 1 258 ? -33.875 19.983 6.784   1.00 12.16 ? 258 SER A C   1 
ATOM   2207 O O   . SER A 1 258 ? -34.024 18.783 7.045   1.00 12.64 ? 258 SER A O   1 
ATOM   2208 C CB  . SER A 1 258 ? -31.697 20.586 7.851   1.00 12.10 ? 258 SER A CB  1 
ATOM   2209 O OG  . SER A 1 258 ? -31.089 20.877 6.593   1.00 15.58 ? 258 SER A OG  1 
ATOM   2210 N N   . VAL A 1 259 ? -34.307 20.538 5.653   1.00 12.12 ? 259 VAL A N   1 
ATOM   2211 C CA  . VAL A 1 259 ? -34.921 19.734 4.603   1.00 11.54 ? 259 VAL A CA  1 
ATOM   2212 C C   . VAL A 1 259 ? -34.350 20.120 3.245   1.00 12.49 ? 259 VAL A C   1 
ATOM   2213 O O   . VAL A 1 259 ? -33.745 21.181 3.060   1.00 14.02 ? 259 VAL A O   1 
ATOM   2214 C CB  . VAL A 1 259 ? -36.467 19.850 4.591   1.00 14.44 ? 259 VAL A CB  1 
ATOM   2215 C CG1 . VAL A 1 259 ? -37.054 19.335 5.916   1.00 14.80 ? 259 VAL A CG1 1 
ATOM   2216 C CG2 . VAL A 1 259 ? -36.890 21.287 4.332   1.00 14.98 ? 259 VAL A CG2 1 
ATOM   2217 N N   . SER A 1 260 ? -34.537 19.201 2.300   1.00 12.09 ? 260 SER A N   1 
ATOM   2218 C CA  . SER A 1 260 ? -34.239 19.357 0.886   1.00 10.16 ? 260 SER A CA  1 
ATOM   2219 C C   . SER A 1 260 ? -35.139 18.358 0.194   1.00 11.92 ? 260 SER A C   1 
ATOM   2220 O O   . SER A 1 260 ? -35.709 17.473 0.843   1.00 13.67 ? 260 SER A O   1 
ATOM   2221 C CB  . SER A 1 260 ? -32.769 19.075 0.563   1.00 14.82 ? 260 SER A CB  1 
ATOM   2222 O OG  . SER A 1 260 ? -32.455 17.697 0.785   1.00 13.77 ? 260 SER A OG  1 
ATOM   2223 N N   . ASN A 1 261 ? -35.247 18.486 -1.126  1.00 11.85 ? 261 ASN A N   1 
ATOM   2224 C CA  . ASN A 1 261 ? -36.043 17.506 -1.851  1.00 11.20 ? 261 ASN A CA  1 
ATOM   2225 C C   . ASN A 1 261 ? -35.509 16.106 -1.598  1.00 14.89 ? 261 ASN A C   1 
ATOM   2226 O O   . ASN A 1 261 ? -36.284 15.187 -1.317  1.00 14.62 ? 261 ASN A O   1 
ATOM   2227 C CB  . ASN A 1 261 ? -36.055 17.826 -3.348  1.00 13.88 ? 261 ASN A CB  1 
ATOM   2228 C CG  . ASN A 1 261 ? -36.861 19.084 -3.671  1.00 15.68 ? 261 ASN A CG  1 
ATOM   2229 O OD1 . ASN A 1 261 ? -37.726 19.508 -2.895  1.00 15.85 ? 261 ASN A OD1 1 
ATOM   2230 N ND2 . ASN A 1 261 ? -36.575 19.683 -4.815  1.00 17.60 ? 261 ASN A ND2 1 
ATOM   2231 N N   . GLU A 1 262 ? -34.181 15.940 -1.626  1.00 12.71 ? 262 GLU A N   1 
ATOM   2232 C CA  . GLU A 1 262 ? -33.606 14.608 -1.451  1.00 13.70 ? 262 GLU A CA  1 
ATOM   2233 C C   . GLU A 1 262 ? -33.800 14.107 -0.029  1.00 13.75 ? 262 GLU A C   1 
ATOM   2234 O O   . GLU A 1 262 ? -34.026 12.906 0.182   1.00 15.34 ? 262 GLU A O   1 
ATOM   2235 C CB  . GLU A 1 262 ? -32.125 14.607 -1.836  1.00 14.38 ? 262 GLU A CB  1 
ATOM   2236 C CG  . GLU A 1 262 ? -31.919 14.791 -3.328  1.00 15.65 ? 262 GLU A CG  1 
ATOM   2237 C CD  . GLU A 1 262 ? -30.469 14.678 -3.747  1.00 23.13 ? 262 GLU A CD  1 
ATOM   2238 O OE1 . GLU A 1 262 ? -29.760 13.795 -3.222  1.00 29.69 ? 262 GLU A OE1 1 
ATOM   2239 O OE2 . GLU A 1 262 ? -30.038 15.482 -4.597  1.00 25.32 ? 262 GLU A OE2 1 
ATOM   2240 N N   . ALA A 1 263 ? -33.724 15.004 0.962   1.00 11.87 ? 263 ALA A N   1 
ATOM   2241 C CA  . ALA A 1 263 ? -33.926 14.566 2.344   1.00 12.64 ? 263 ALA A CA  1 
ATOM   2242 C C   . ALA A 1 263 ? -35.367 14.132 2.576   1.00 13.80 ? 263 ALA A C   1 
ATOM   2243 O O   . ALA A 1 263 ? -35.610 13.099 3.211   1.00 13.57 ? 263 ALA A O   1 
ATOM   2244 C CB  . ALA A 1 263 ? -33.523 15.664 3.330   1.00 13.22 ? 263 ALA A CB  1 
ATOM   2245 N N   . LEU A 1 264 ? -36.335 14.891 2.046   1.00 14.23 ? 264 LEU A N   1 
ATOM   2246 C CA  . LEU A 1 264 ? -37.739 14.489 2.163   1.00 12.21 ? 264 LEU A CA  1 
ATOM   2247 C C   . LEU A 1 264 ? -37.974 13.132 1.515   1.00 14.36 ? 264 LEU A C   1 
ATOM   2248 O O   . LEU A 1 264 ? -38.736 12.311 2.034   1.00 15.86 ? 264 LEU A O   1 
ATOM   2249 C CB  . LEU A 1 264 ? -38.641 15.548 1.531   1.00 12.63 ? 264 LEU A CB  1 
ATOM   2250 C CG  . LEU A 1 264 ? -38.694 16.867 2.305   1.00 13.74 ? 264 LEU A CG  1 
ATOM   2251 C CD1 . LEU A 1 264 ? -39.327 17.972 1.478   1.00 15.63 ? 264 LEU A CD1 1 
ATOM   2252 C CD2 . LEU A 1 264 ? -39.432 16.692 3.628   1.00 20.96 ? 264 LEU A CD2 1 
ATOM   2253 N N   . GLU A 1 265 ? -37.311 12.872 0.385   1.00 13.36 ? 265 GLU A N   1 
ATOM   2254 C CA  . GLU A 1 265 ? -37.425 11.568 -0.258  1.00 12.83 ? 265 GLU A CA  1 
ATOM   2255 C C   . GLU A 1 265 ? -36.864 10.458 0.623   1.00 16.21 ? 265 GLU A C   1 
ATOM   2256 O O   . GLU A 1 265 ? -37.434 9.356  0.688   1.00 18.28 ? 265 GLU A O   1 
ATOM   2257 C CB  . GLU A 1 265 ? -36.723 11.603 -1.618  1.00 13.27 ? 265 GLU A CB  1 
ATOM   2258 C CG  . GLU A 1 265 ? -37.402 12.535 -2.640  1.00 16.39 ? 265 GLU A CG  1 
ATOM   2259 C CD  . GLU A 1 265 ? -36.586 12.749 -3.910  1.00 24.07 ? 265 GLU A CD  1 
ATOM   2260 O OE1 . GLU A 1 265 ? -35.368 12.473 -3.906  1.00 27.92 ? 265 GLU A OE1 1 
ATOM   2261 O OE2 . GLU A 1 265 ? -37.163 13.211 -4.914  1.00 30.96 ? 265 GLU A OE2 1 
ATOM   2262 N N   . LEU A 1 266 ? -35.743 10.722 1.300   1.00 13.48 ? 266 LEU A N   1 
ATOM   2263 C CA  . LEU A 1 266 ? -35.155 9.712  2.179   1.00 14.09 ? 266 LEU A CA  1 
ATOM   2264 C C   . LEU A 1 266 ? -36.074 9.404  3.357   1.00 12.74 ? 266 LEU A C   1 
ATOM   2265 O O   . LEU A 1 266 ? -36.301 8.229  3.691   1.00 14.97 ? 266 LEU A O   1 
ATOM   2266 C CB  . LEU A 1 266 ? -33.778 10.179 2.670   1.00 12.46 ? 266 LEU A CB  1 
ATOM   2267 C CG  . LEU A 1 266 ? -33.122 9.235  3.687   1.00 11.84 ? 266 LEU A CG  1 
ATOM   2268 C CD1 . LEU A 1 266 ? -32.844 7.863  3.081   1.00 14.37 ? 266 LEU A CD1 1 
ATOM   2269 C CD2 . LEU A 1 266 ? -31.831 9.863  4.227   1.00 16.47 ? 266 LEU A CD2 1 
ATOM   2270 N N   . TYR A 1 267 ? -36.589 10.446 4.017   1.00 12.08 ? 267 TYR A N   1 
ATOM   2271 C CA  . TYR A 1 267 ? -37.499 10.227 5.136   1.00 12.17 ? 267 TYR A CA  1 
ATOM   2272 C C   . TYR A 1 267 ? -38.709 9.415  4.691   1.00 14.20 ? 267 TYR A C   1 
ATOM   2273 O O   . TYR A 1 267 ? -39.105 8.452  5.359   1.00 15.53 ? 267 TYR A O   1 
ATOM   2274 C CB  . TYR A 1 267 ? -37.939 11.566 5.732   1.00 13.61 ? 267 TYR A CB  1 
ATOM   2275 C CG  . TYR A 1 267 ? -36.870 12.263 6.559   1.00 14.25 ? 267 TYR A CG  1 
ATOM   2276 C CD1 . TYR A 1 267 ? -36.397 11.699 7.727   1.00 14.72 ? 267 TYR A CD1 1 
ATOM   2277 C CD2 . TYR A 1 267 ? -36.364 13.498 6.177   1.00 12.16 ? 267 TYR A CD2 1 
ATOM   2278 C CE1 . TYR A 1 267 ? -35.434 12.328 8.493   1.00 15.07 ? 267 TYR A CE1 1 
ATOM   2279 C CE2 . TYR A 1 267 ? -35.389 14.141 6.933   1.00 14.57 ? 267 TYR A CE2 1 
ATOM   2280 C CZ  . TYR A 1 267 ? -34.931 13.547 8.089   1.00 13.74 ? 267 TYR A CZ  1 
ATOM   2281 O OH  . TYR A 1 267 ? -33.965 14.181 8.839   1.00 13.51 ? 267 TYR A OH  1 
ATOM   2282 N N   . TYR A 1 268 ? -39.293 9.765  3.548   1.00 15.22 ? 268 TYR A N   1 
ATOM   2283 C CA  . TYR A 1 268 ? -40.437 8.991  3.075   1.00 13.64 ? 268 TYR A CA  1 
ATOM   2284 C C   . TYR A 1 268 ? -40.055 7.539  2.787   1.00 16.57 ? 268 TYR A C   1 
ATOM   2285 O O   . TYR A 1 268 ? -40.798 6.612  3.144   1.00 16.89 ? 268 TYR A O   1 
ATOM   2286 C CB  . TYR A 1 268 ? -41.044 9.641  1.835   1.00 17.78 ? 268 TYR A CB  1 
ATOM   2287 C CG  . TYR A 1 268 ? -42.127 8.790  1.220   1.00 23.49 ? 268 TYR A CG  1 
ATOM   2288 C CD1 . TYR A 1 268 ? -43.366 8.661  1.837   1.00 23.40 ? 268 TYR A CD1 1 
ATOM   2289 C CD2 . TYR A 1 268 ? -41.900 8.085  0.050   1.00 26.63 ? 268 TYR A CD2 1 
ATOM   2290 C CE1 . TYR A 1 268 ? -44.366 7.859  1.285   1.00 24.34 ? 268 TYR A CE1 1 
ATOM   2291 C CE2 . TYR A 1 268 ? -42.901 7.282  -0.513  1.00 29.31 ? 268 TYR A CE2 1 
ATOM   2292 C CZ  . TYR A 1 268 ? -44.128 7.179  0.115   1.00 28.05 ? 268 TYR A CZ  1 
ATOM   2293 O OH  . TYR A 1 268 ? -45.120 6.383  -0.434  1.00 34.50 ? 268 TYR A OH  1 
ATOM   2294 N N   . GLU A 1 269 ? -38.908 7.320  2.125   1.00 15.87 ? 269 GLU A N   1 
ATOM   2295 C CA  . GLU A 1 269 ? -38.492 5.958  1.798   1.00 15.28 ? 269 GLU A CA  1 
ATOM   2296 C C   . GLU A 1 269 ? -38.295 5.127  3.055   1.00 14.50 ? 269 GLU A C   1 
ATOM   2297 O O   . GLU A 1 269 ? -38.485 3.909  3.024   1.00 18.28 ? 269 GLU A O   1 
ATOM   2298 C CB  . GLU A 1 269 ? -37.194 5.980  0.979   1.00 24.79 ? 269 GLU A CB  1 
ATOM   2299 C CG  . GLU A 1 269 ? -37.367 6.384  -0.477  1.00 45.95 ? 269 GLU A CG  1 
ATOM   2300 C CD  . GLU A 1 269 ? -36.108 7.005  -1.069  1.00 59.99 ? 269 GLU A CD  1 
ATOM   2301 O OE1 . GLU A 1 269 ? -36.210 7.660  -2.129  1.00 59.64 ? 269 GLU A OE1 1 
ATOM   2302 O OE2 . GLU A 1 269 ? -35.020 6.840  -0.476  1.00 63.03 ? 269 GLU A OE2 1 
ATOM   2303 N N   . LYS A 1 270 ? -37.932 5.768  4.167   1.00 16.19 ? 270 LYS A N   1 
ATOM   2304 C CA  . LYS A 1 270 ? -37.703 5.075  5.427   1.00 15.66 ? 270 LYS A CA  1 
ATOM   2305 C C   . LYS A 1 270 ? -38.956 4.978  6.291   1.00 17.45 ? 270 LYS A C   1 
ATOM   2306 O O   . LYS A 1 270 ? -38.872 4.534  7.437   1.00 20.30 ? 270 LYS A O   1 
ATOM   2307 C CB  . LYS A 1 270 ? -36.567 5.761  6.190   1.00 16.68 ? 270 LYS A CB  1 
ATOM   2308 C CG  . LYS A 1 270 ? -35.251 5.708  5.413   1.00 19.83 ? 270 LYS A CG  1 
ATOM   2309 C CD  . LYS A 1 270 ? -34.834 4.285  5.138   1.00 29.73 ? 270 LYS A CD  1 
ATOM   2310 C CE  . LYS A 1 270 ? -33.580 4.227  4.269   1.00 35.50 ? 270 LYS A CE  1 
ATOM   2311 N NZ  . LYS A 1 270 ? -33.321 2.829  3.800   1.00 44.24 ? 270 LYS A NZ  1 
ATOM   2312 N N   . GLY A 1 271 ? -40.119 5.349  5.762   1.00 15.47 ? 271 GLY A N   1 
ATOM   2313 C CA  . GLY A 1 271 ? -41.354 5.126  6.481   1.00 18.21 ? 271 GLY A CA  1 
ATOM   2314 C C   . GLY A 1 271 ? -41.830 6.268  7.341   1.00 17.59 ? 271 GLY A C   1 
ATOM   2315 O O   . GLY A 1 271 ? -42.783 6.079  8.113   1.00 18.69 ? 271 GLY A O   1 
ATOM   2316 N N   . ILE A 1 272 ? -41.216 7.443  7.237   1.00 17.22 ? 272 ILE A N   1 
ATOM   2317 C CA  . ILE A 1 272 ? -41.673 8.606  7.991   1.00 14.51 ? 272 ILE A CA  1 
ATOM   2318 C C   . ILE A 1 272 ? -42.891 9.185  7.285   1.00 16.37 ? 272 ILE A C   1 
ATOM   2319 O O   . ILE A 1 272 ? -42.853 9.453  6.080   1.00 20.27 ? 272 ILE A O   1 
ATOM   2320 C CB  . ILE A 1 272 ? -40.553 9.655  8.125   1.00 18.21 ? 272 ILE A CB  1 
ATOM   2321 C CG1 . ILE A 1 272 ? -39.306 9.036  8.765   1.00 20.89 ? 272 ILE A CG1 1 
ATOM   2322 C CG2 . ILE A 1 272 ? -41.053 10.884 8.899   1.00 19.13 ? 272 ILE A CG2 1 
ATOM   2323 C CD1 . ILE A 1 272 ? -39.585 8.286  10.023  1.00 26.24 ? 272 ILE A CD1 1 
ATOM   2324 N N   . ASN A 1 273 ? -43.985 9.356  8.028   1.00 16.18 ? 273 ASN A N   1 
ATOM   2325 C CA  . ASN A 1 273 ? -45.212 9.878  7.439   1.00 20.15 ? 273 ASN A CA  1 
ATOM   2326 C C   . ASN A 1 273 ? -45.351 11.381 7.588   1.00 16.84 ? 273 ASN A C   1 
ATOM   2327 O O   . ASN A 1 273 ? -46.085 12.000 6.808   1.00 17.77 ? 273 ASN A O   1 
ATOM   2328 C CB  . ASN A 1 273 ? -46.427 9.200  8.075   1.00 22.71 ? 273 ASN A CB  1 
ATOM   2329 C CG  . ASN A 1 273 ? -46.553 7.744  7.674   1.00 32.01 ? 273 ASN A CG  1 
ATOM   2330 O OD1 . ASN A 1 273 ? -46.005 7.320  6.655   1.00 32.78 ? 273 ASN A OD1 1 
ATOM   2331 N ND2 . ASN A 1 273 ? -47.272 6.973  8.474   1.00 33.96 ? 273 ASN A ND2 1 
ATOM   2332 N N   . MET A 1 274 ? -44.682 11.973 8.569   1.00 18.59 ? 274 MET A N   1 
ATOM   2333 C CA  . MET A 1 274 ? -44.822 13.396 8.816   1.00 13.40 ? 274 MET A CA  1 
ATOM   2334 C C   . MET A 1 274 ? -43.545 13.921 9.440   1.00 13.51 ? 274 MET A C   1 
ATOM   2335 O O   . MET A 1 274 ? -42.931 13.259 10.289  1.00 14.85 ? 274 MET A O   1 
ATOM   2336 C CB  . MET A 1 274 ? -46.010 13.698 9.741   1.00 16.11 ? 274 MET A CB  1 
ATOM   2337 C CG  . MET A 1 274 ? -46.306 15.197 9.906   1.00 16.43 ? 274 MET A CG  1 
ATOM   2338 S SD  . MET A 1 274 ? -45.371 15.925 11.281  1.00 25.60 ? 274 MET A SD  1 
ATOM   2339 C CE  . MET A 1 274 ? -46.523 15.635 12.641  1.00 22.98 ? 274 MET A CE  1 
ATOM   2340 N N   . LEU A 1 275 ? -43.162 15.126 9.025   1.00 12.80 ? 275 LEU A N   1 
ATOM   2341 C CA  . LEU A 1 275 ? -42.138 15.884 9.717   1.00 11.61 ? 275 LEU A CA  1 
ATOM   2342 C C   . LEU A 1 275 ? -42.573 17.339 9.763   1.00 11.51 ? 275 LEU A C   1 
ATOM   2343 O O   . LEU A 1 275 ? -43.569 17.731 9.145   1.00 12.70 ? 275 LEU A O   1 
ATOM   2344 C CB  . LEU A 1 275 ? -40.762 15.738 9.051   1.00 16.64 ? 275 LEU A CB  1 
ATOM   2345 C CG  . LEU A 1 275 ? -40.624 15.969 7.548   1.00 20.16 ? 275 LEU A CG  1 
ATOM   2346 C CD1 . LEU A 1 275 ? -40.497 17.462 7.215   1.00 18.75 ? 275 LEU A CD1 1 
ATOM   2347 C CD2 . LEU A 1 275 ? -39.415 15.205 7.019   1.00 21.12 ? 275 LEU A CD2 1 
ATOM   2348 N N   . ALA A 1 276 ? -41.830 18.141 10.516  1.00 12.25 ? 276 ALA A N   1 
ATOM   2349 C CA  . ALA A 1 276 ? -42.004 19.586 10.487  1.00 13.93 ? 276 ALA A CA  1 
ATOM   2350 C C   . ALA A 1 276 ? -40.700 20.260 10.089  1.00 12.79 ? 276 ALA A C   1 
ATOM   2351 O O   . ALA A 1 276 ? -39.612 19.692 10.216  1.00 11.83 ? 276 ALA A O   1 
ATOM   2352 C CB  . ALA A 1 276 ? -42.483 20.138 11.839  1.00 13.69 ? 276 ALA A CB  1 
ATOM   2353 N N   . THR A 1 277 ? -40.819 21.488 9.605   1.00 12.82 ? 277 THR A N   1 
ATOM   2354 C CA  . THR A 1 277 ? -39.630 22.273 9.284   1.00 10.57 ? 277 THR A CA  1 
ATOM   2355 C C   . THR A 1 277 ? -39.971 23.738 9.529   1.00 13.01 ? 277 THR A C   1 
ATOM   2356 O O   . THR A 1 277 ? -40.930 24.049 10.242  1.00 13.69 ? 277 THR A O   1 
ATOM   2357 C CB  . THR A 1 277 ? -39.150 21.947 7.858   1.00 12.56 ? 277 THR A CB  1 
ATOM   2358 O OG1 . THR A 1 277 ? -37.998 22.726 7.535   1.00 13.24 ? 277 THR A OG1 1 
ATOM   2359 C CG2 . THR A 1 277 ? -40.253 22.243 6.839   1.00 15.05 ? 277 THR A CG2 1 
ATOM   2360 N N   . ASP A 1 278 ? -39.186 24.642 8.959   1.00 11.61 ? 278 ASP A N   1 
ATOM   2361 C CA  . ASP A 1 278 ? -39.249 26.050 9.331   1.00 12.78 ? 278 ASP A CA  1 
ATOM   2362 C C   . ASP A 1 278 ? -40.001 26.905 8.317   1.00 15.60 ? 278 ASP A C   1 
ATOM   2363 O O   . ASP A 1 278 ? -40.020 26.628 7.115   1.00 14.41 ? 278 ASP A O   1 
ATOM   2364 C CB  . ASP A 1 278 ? -37.838 26.615 9.520   1.00 14.90 ? 278 ASP A CB  1 
ATOM   2365 C CG  . ASP A 1 278 ? -37.853 28.056 9.980   1.00 16.93 ? 278 ASP A CG  1 
ATOM   2366 O OD1 . ASP A 1 278 ? -38.489 28.355 11.008  1.00 16.21 ? 278 ASP A OD1 1 
ATOM   2367 O OD2 . ASP A 1 278 ? -37.252 28.900 9.295   1.00 17.58 ? 278 ASP A OD2 1 
ATOM   2368 N N   . GLU A 1 279 ? -40.573 27.998 8.828   1.00 14.48 ? 279 GLU A N   1 
ATOM   2369 C CA  . GLU A 1 279 ? -41.371 28.902 8.014   1.00 14.70 ? 279 GLU A CA  1 
ATOM   2370 C C   . GLU A 1 279 ? -40.543 29.617 6.950   1.00 17.38 ? 279 GLU A C   1 
ATOM   2371 O O   . GLU A 1 279 ? -41.070 29.922 5.872   1.00 19.37 ? 279 GLU A O   1 
ATOM   2372 C CB  . GLU A 1 279 ? -42.064 29.924 8.916   1.00 18.88 ? 279 GLU A CB  1 
ATOM   2373 C CG  . GLU A 1 279 ? -43.135 30.695 8.186   1.00 20.48 ? 279 GLU A CG  1 
ATOM   2374 C CD  . GLU A 1 279 ? -44.040 31.480 9.114   1.00 17.72 ? 279 GLU A CD  1 
ATOM   2375 O OE1 . GLU A 1 279 ? -43.826 31.462 10.352  1.00 16.78 ? 279 GLU A OE1 1 
ATOM   2376 O OE2 . GLU A 1 279 ? -44.959 32.130 8.589   1.00 19.28 ? 279 GLU A OE2 1 
ATOM   2377 N N   . VAL A 1 280 ? -39.271 29.920 7.228   1.00 16.38 ? 280 VAL A N   1 
ATOM   2378 C CA  . VAL A 1 280 ? -38.442 30.571 6.215   1.00 15.29 ? 280 VAL A CA  1 
ATOM   2379 C C   . VAL A 1 280 ? -38.305 29.667 4.998   1.00 14.92 ? 280 VAL A C   1 
ATOM   2380 O O   . VAL A 1 280 ? -38.316 30.137 3.852   1.00 17.38 ? 280 VAL A O   1 
ATOM   2381 C CB  . VAL A 1 280 ? -37.062 30.967 6.781   1.00 14.70 ? 280 VAL A CB  1 
ATOM   2382 C CG1 . VAL A 1 280 ? -36.166 31.493 5.662   1.00 16.03 ? 280 VAL A CG1 1 
ATOM   2383 C CG2 . VAL A 1 280 ? -37.191 32.004 7.905   1.00 18.75 ? 280 VAL A CG2 1 
ATOM   2384 N N   . ILE A 1 281 ? -38.184 28.356 5.223   1.00 14.29 ? 281 ILE A N   1 
ATOM   2385 C CA  . ILE A 1 281 ? -38.097 27.430 4.099   1.00 13.44 ? 281 ILE A CA  1 
ATOM   2386 C C   . ILE A 1 281 ? -39.392 27.457 3.292   1.00 13.03 ? 281 ILE A C   1 
ATOM   2387 O O   . ILE A 1 281 ? -39.364 27.453 2.051   1.00 15.92 ? 281 ILE A O   1 
ATOM   2388 C CB  . ILE A 1 281 ? -37.745 26.018 4.599   1.00 16.48 ? 281 ILE A CB  1 
ATOM   2389 C CG1 . ILE A 1 281 ? -36.393 26.052 5.333   1.00 15.42 ? 281 ILE A CG1 1 
ATOM   2390 C CG2 . ILE A 1 281 ? -37.705 25.037 3.428   1.00 16.64 ? 281 ILE A CG2 1 
ATOM   2391 C CD1 . ILE A 1 281 ? -35.959 24.715 5.891   1.00 18.56 ? 281 ILE A CD1 1 
ATOM   2392 N N   . LEU A 1 282 ? -40.543 27.511 3.973   1.00 15.08 ? 282 LEU A N   1 
ATOM   2393 C CA  . LEU A 1 282 ? -41.814 27.630 3.261   1.00 15.83 ? 282 LEU A CA  1 
ATOM   2394 C C   . LEU A 1 282 ? -41.837 28.873 2.376   1.00 15.66 ? 282 LEU A C   1 
ATOM   2395 O O   . LEU A 1 282 ? -42.151 28.791 1.181   1.00 16.80 ? 282 LEU A O   1 
ATOM   2396 C CB  . LEU A 1 282 ? -42.983 27.657 4.246   1.00 14.14 ? 282 LEU A CB  1 
ATOM   2397 C CG  . LEU A 1 282 ? -44.373 27.801 3.612   1.00 17.58 ? 282 LEU A CG  1 
ATOM   2398 C CD1 . LEU A 1 282 ? -44.707 26.614 2.726   1.00 17.47 ? 282 LEU A CD1 1 
ATOM   2399 C CD2 . LEU A 1 282 ? -45.431 27.982 4.698   1.00 19.42 ? 282 LEU A CD2 1 
ATOM   2400 N N   . LYS A 1 283 ? -41.494 30.037 2.943   1.00 15.46 ? 283 LYS A N   1 
ATOM   2401 C CA  . LYS A 1 283 ? -41.542 31.281 2.174   1.00 17.52 ? 283 LYS A CA  1 
ATOM   2402 C C   . LYS A 1 283 ? -40.533 31.283 1.030   1.00 16.53 ? 283 LYS A C   1 
ATOM   2403 O O   . LYS A 1 283 ? -40.775 31.916 -0.008  1.00 18.02 ? 283 LYS A O   1 
ATOM   2404 C CB  . LYS A 1 283 ? -41.286 32.490 3.079   1.00 21.39 ? 283 LYS A CB  1 
ATOM   2405 C CG  . LYS A 1 283 ? -42.109 32.521 4.346   1.00 26.16 ? 283 LYS A CG  1 
ATOM   2406 C CD  . LYS A 1 283 ? -43.536 32.924 4.076   1.00 32.23 ? 283 LYS A CD  1 
ATOM   2407 C CE  . LYS A 1 283 ? -44.448 32.433 5.190   1.00 32.37 ? 283 LYS A CE  1 
ATOM   2408 N NZ  . LYS A 1 283 ? -45.503 33.403 5.531   1.00 37.41 ? 283 LYS A NZ  1 
ATOM   2409 N N   . ASN A 1 284 ? -39.387 30.614 1.208   1.00 15.63 ? 284 ASN A N   1 
ATOM   2410 C CA  . ASN A 1 284 ? -38.400 30.495 0.138   1.00 13.62 ? 284 ASN A CA  1 
ATOM   2411 C C   . ASN A 1 284 ? -38.872 29.600 -0.995  1.00 16.09 ? 284 ASN A C   1 
ATOM   2412 O O   . ASN A 1 284 ? -38.328 29.683 -2.104  1.00 17.16 ? 284 ASN A O   1 
ATOM   2413 C CB  . ASN A 1 284 ? -37.094 29.915 0.680   1.00 17.29 ? 284 ASN A CB  1 
ATOM   2414 C CG  . ASN A 1 284 ? -36.291 30.909 1.471   1.00 18.23 ? 284 ASN A CG  1 
ATOM   2415 O OD1 . ASN A 1 284 ? -36.541 32.117 1.434   1.00 18.82 ? 284 ASN A OD1 1 
ATOM   2416 N ND2 . ASN A 1 284 ? -35.283 30.407 2.170   1.00 16.57 ? 284 ASN A ND2 1 
ATOM   2417 N N   . SER A 1 285 ? -39.849 28.736 -0.727  1.00 16.77 ? 285 SER A N   1 
ATOM   2418 C CA  . SER A 1 285 ? -40.222 27.664 -1.635  1.00 15.61 ? 285 SER A CA  1 
ATOM   2419 C C   . SER A 1 285 ? -41.530 27.898 -2.363  1.00 17.16 ? 285 SER A C   1 
ATOM   2420 O O   . SER A 1 285 ? -41.673 27.426 -3.491  1.00 21.72 ? 285 SER A O   1 
ATOM   2421 C CB  . SER A 1 285 ? -40.327 26.336 -0.878  1.00 16.63 ? 285 SER A CB  1 
ATOM   2422 O OG  . SER A 1 285 ? -39.123 26.071 -0.159  1.00 15.95 ? 285 SER A OG  1 
ATOM   2423 N N   . VAL A 1 286 ? -42.504 28.573 -1.743  1.00 17.68 ? 286 VAL A N   1 
ATOM   2424 C CA  . VAL A 1 286 ? -43.811 28.729 -2.369  1.00 21.03 ? 286 VAL A CA  1 
ATOM   2425 C C   . VAL A 1 286 ? -44.257 30.181 -2.278  1.00 26.87 ? 286 VAL A C   1 
ATOM   2426 O O   . VAL A 1 286 ? -43.820 30.939 -1.412  1.00 27.58 ? 286 VAL A O   1 
ATOM   2427 C CB  . VAL A 1 286 ? -44.887 27.808 -1.750  1.00 24.46 ? 286 VAL A CB  1 
ATOM   2428 C CG1 . VAL A 1 286 ? -44.381 26.381 -1.630  1.00 30.05 ? 286 VAL A CG1 1 
ATOM   2429 C CG2 . VAL A 1 286 ? -45.328 28.328 -0.408  1.00 23.62 ? 286 VAL A CG2 1 
ATOM   2430 N N   . GLU A 1 287 ? -45.170 30.553 -3.179  1.00 28.10 ? 287 GLU A N   1 
ATOM   2431 C CA  . GLU A 1 287 ? -45.689 31.919 -3.179  1.00 27.71 ? 287 GLU A CA  1 
ATOM   2432 C C   . GLU A 1 287 ? -46.790 32.104 -2.141  1.00 27.58 ? 287 GLU A C   1 
ATOM   2433 O O   . GLU A 1 287 ? -46.735 33.033 -1.332  1.00 26.61 ? 287 GLU A O   1 
ATOM   2434 C CB  . GLU A 1 287 ? -46.193 32.291 -4.569  1.00 35.92 ? 287 GLU A CB  1 
ATOM   2435 C CG  . GLU A 1 287 ? -45.094 32.797 -5.470  1.00 46.94 ? 287 GLU A CG  1 
ATOM   2436 C CD  . GLU A 1 287 ? -45.410 32.581 -6.918  1.00 55.71 ? 287 GLU A CD  1 
ATOM   2437 O OE1 . GLU A 1 287 ? -46.610 32.468 -7.235  1.00 60.09 ? 287 GLU A OE1 1 
ATOM   2438 O OE2 . GLU A 1 287 ? -44.467 32.512 -7.733  1.00 61.43 ? 287 GLU A OE2 1 
ATOM   2439 N N   . ARG A 1 288 ? -47.800 31.235 -2.149  1.00 31.96 ? 288 ARG A N   1 
ATOM   2440 C CA  . ARG A 1 288 ? -48.919 31.337 -1.210  1.00 29.13 ? 288 ARG A CA  1 
ATOM   2441 C C   . ARG A 1 288 ? -48.541 30.519 0.017   1.00 29.49 ? 288 ARG A C   1 
ATOM   2442 O O   . ARG A 1 288 ? -48.844 29.329 0.121   1.00 36.39 ? 288 ARG A O   1 
ATOM   2443 C CB  . ARG A 1 288 ? -50.211 30.860 -1.862  1.00 39.31 ? 288 ARG A CB  1 
ATOM   2444 C CG  . ARG A 1 288 ? -50.497 31.559 -3.190  1.00 38.68 ? 288 ARG A CG  1 
ATOM   2445 C CD  . ARG A 1 288 ? -51.670 30.945 -3.950  1.00 38.93 ? 288 ARG A CD  1 
ATOM   2446 N NE  . ARG A 1 288 ? -51.374 29.608 -4.462  1.00 35.18 ? 288 ARG A NE  1 
ATOM   2447 C CZ  . ARG A 1 288 ? -51.754 28.478 -3.871  1.00 39.70 ? 288 ARG A CZ  1 
ATOM   2448 N NH1 . ARG A 1 288 ? -51.443 27.306 -4.407  1.00 43.85 ? 288 ARG A NH1 1 
ATOM   2449 N NH2 . ARG A 1 288 ? -52.442 28.518 -2.738  1.00 47.68 ? 288 ARG A NH2 1 
ATOM   2450 N N   . ALA A 1 289 ? -47.873 31.169 0.963   1.00 24.08 ? 289 ALA A N   1 
ATOM   2451 C CA  . ALA A 1 289 ? -47.109 30.470 1.986   1.00 20.44 ? 289 ALA A CA  1 
ATOM   2452 C C   . ALA A 1 289 ? -47.775 30.607 3.354   1.00 17.94 ? 289 ALA A C   1 
ATOM   2453 O O   . ALA A 1 289 ? -47.223 31.212 4.271   1.00 24.31 ? 289 ALA A O   1 
ATOM   2454 C CB  . ALA A 1 289 ? -45.675 31.008 2.007   1.00 29.41 ? 289 ALA A CB  1 
ATOM   2455 N N   . SER A 1 290 ? -48.958 29.994 3.506   1.00 16.21 ? 290 SER A N   1 
ATOM   2456 C CA  . SER A 1 290 ? -49.583 29.938 4.833   1.00 15.12 ? 290 SER A CA  1 
ATOM   2457 C C   . SER A 1 290 ? -48.999 28.786 5.642   1.00 12.44 ? 290 SER A C   1 
ATOM   2458 O O   . SER A 1 290 ? -48.998 27.645 5.173   1.00 15.61 ? 290 SER A O   1 
ATOM   2459 C CB  . SER A 1 290 ? -51.099 29.751 4.741   1.00 17.80 ? 290 SER A CB  1 
ATOM   2460 O OG  . SER A 1 290 ? -51.655 29.628 6.050   1.00 18.08 ? 290 SER A OG  1 
ATOM   2461 N N   . PRO A 1 291 ? -48.518 29.029 6.860   1.00 13.90 ? 291 PRO A N   1 
ATOM   2462 C CA  . PRO A 1 291 ? -48.032 27.927 7.695   1.00 12.71 ? 291 PRO A CA  1 
ATOM   2463 C C   . PRO A 1 291 ? -49.128 27.175 8.432   1.00 13.83 ? 291 PRO A C   1 
ATOM   2464 O O   . PRO A 1 291 ? -48.813 26.304 9.247   1.00 14.02 ? 291 PRO A O   1 
ATOM   2465 C CB  . PRO A 1 291 ? -47.103 28.644 8.684   1.00 14.61 ? 291 PRO A CB  1 
ATOM   2466 C CG  . PRO A 1 291 ? -47.770 29.948 8.896   1.00 14.13 ? 291 PRO A CG  1 
ATOM   2467 C CD  . PRO A 1 291 ? -48.380 30.329 7.549   1.00 14.73 ? 291 PRO A CD  1 
ATOM   2468 N N   . TYR A 1 292 ? -50.403 27.459 8.160   1.00 13.24 ? 292 TYR A N   1 
ATOM   2469 C CA  . TYR A 1 292 ? -51.491 26.907 8.952   1.00 13.29 ? 292 TYR A CA  1 
ATOM   2470 C C   . TYR A 1 292 ? -52.133 25.691 8.294   1.00 12.30 ? 292 TYR A C   1 
ATOM   2471 O O   . TYR A 1 292 ? -53.135 25.185 8.802   1.00 14.68 ? 292 TYR A O   1 
ATOM   2472 C CB  . TYR A 1 292 ? -52.527 27.998 9.227   1.00 14.27 ? 292 TYR A CB  1 
ATOM   2473 C CG  . TYR A 1 292 ? -51.907 29.164 9.977   1.00 16.60 ? 292 TYR A CG  1 
ATOM   2474 C CD1 . TYR A 1 292 ? -51.012 28.935 11.018  1.00 22.39 ? 292 TYR A CD1 1 
ATOM   2475 C CD2 . TYR A 1 292 ? -52.183 30.477 9.622   1.00 23.70 ? 292 TYR A CD2 1 
ATOM   2476 C CE1 . TYR A 1 292 ? -50.424 29.984 11.701  1.00 27.63 ? 292 TYR A CE1 1 
ATOM   2477 C CE2 . TYR A 1 292 ? -51.593 31.539 10.311  1.00 26.88 ? 292 TYR A CE2 1 
ATOM   2478 C CZ  . TYR A 1 292 ? -50.719 31.279 11.340  1.00 28.73 ? 292 TYR A CZ  1 
ATOM   2479 O OH  . TYR A 1 292 ? -50.130 32.327 12.020  1.00 41.36 ? 292 TYR A OH  1 
ATOM   2480 N N   . LEU A 1 293 ? -51.545 25.204 7.199   1.00 13.13 ? 293 LEU A N   1 
ATOM   2481 C CA  . LEU A 1 293 ? -52.041 24.072 6.434   1.00 14.13 ? 293 LEU A CA  1 
ATOM   2482 C C   . LEU A 1 293 ? -51.174 22.847 6.698   1.00 12.37 ? 293 LEU A C   1 
ATOM   2483 O O   . LEU A 1 293 ? -49.995 22.971 7.048   1.00 14.49 ? 293 LEU A O   1 
ATOM   2484 C CB  . LEU A 1 293 ? -52.007 24.374 4.936   1.00 15.74 ? 293 LEU A CB  1 
ATOM   2485 C CG  . LEU A 1 293 ? -53.067 25.243 4.259   1.00 21.99 ? 293 LEU A CG  1 
ATOM   2486 C CD1 . LEU A 1 293 ? -53.578 26.412 5.096   1.00 21.10 ? 293 LEU A CD1 1 
ATOM   2487 C CD2 . LEU A 1 293 ? -52.505 25.731 2.921   1.00 21.33 ? 293 LEU A CD2 1 
ATOM   2488 N N   . ARG A 1 294 ? -51.762 21.663 6.516   1.00 14.07 ? 294 ARG A N   1 
ATOM   2489 C CA  . ARG A 1 294 ? -50.974 20.435 6.399   1.00 14.48 ? 294 ARG A CA  1 
ATOM   2490 C C   . ARG A 1 294 ? -50.562 20.281 4.940   1.00 12.58 ? 294 ARG A C   1 
ATOM   2491 O O   . ARG A 1 294 ? -51.422 20.210 4.054   1.00 14.60 ? 294 ARG A O   1 
ATOM   2492 C CB  . ARG A 1 294 ? -51.763 19.211 6.875   1.00 15.74 ? 294 ARG A CB  1 
ATOM   2493 C CG  . ARG A 1 294 ? -50.963 17.889 6.820   1.00 17.56 ? 294 ARG A CG  1 
ATOM   2494 C CD  . ARG A 1 294 ? -51.683 16.761 7.578   1.00 16.39 ? 294 ARG A CD  1 
ATOM   2495 N NE  . ARG A 1 294 ? -52.967 16.425 6.970   1.00 20.37 ? 294 ARG A NE  1 
ATOM   2496 C CZ  . ARG A 1 294 ? -54.130 16.392 7.615   1.00 21.43 ? 294 ARG A CZ  1 
ATOM   2497 N NH1 . ARG A 1 294 ? -54.202 16.675 8.912   1.00 19.43 ? 294 ARG A NH1 1 
ATOM   2498 N NH2 . ARG A 1 294 ? -55.237 16.076 6.956   1.00 22.81 ? 294 ARG A NH2 1 
ATOM   2499 N N   . TYR A 1 295 ? -49.259 20.282 4.681   1.00 13.13 ? 295 TYR A N   1 
ATOM   2500 C CA  . TYR A 1 295 ? -48.755 20.132 3.329   1.00 12.42 ? 295 TYR A CA  1 
ATOM   2501 C C   . TYR A 1 295 ? -48.414 18.678 3.041   1.00 15.96 ? 295 TYR A C   1 
ATOM   2502 O O   . TYR A 1 295 ? -48.048 17.915 3.937   1.00 15.07 ? 295 TYR A O   1 
ATOM   2503 C CB  . TYR A 1 295 ? -47.520 21.006 3.110   1.00 13.73 ? 295 TYR A CB  1 
ATOM   2504 C CG  . TYR A 1 295 ? -47.843 22.474 3.036   1.00 14.02 ? 295 TYR A CG  1 
ATOM   2505 C CD1 . TYR A 1 295 ? -47.964 23.238 4.186   1.00 12.90 ? 295 TYR A CD1 1 
ATOM   2506 C CD2 . TYR A 1 295 ? -48.035 23.094 1.806   1.00 15.86 ? 295 TYR A CD2 1 
ATOM   2507 C CE1 . TYR A 1 295 ? -48.267 24.598 4.113   1.00 14.96 ? 295 TYR A CE1 1 
ATOM   2508 C CE2 . TYR A 1 295 ? -48.324 24.442 1.723   1.00 15.26 ? 295 TYR A CE2 1 
ATOM   2509 C CZ  . TYR A 1 295 ? -48.442 25.184 2.877   1.00 16.27 ? 295 TYR A CZ  1 
ATOM   2510 O OH  . TYR A 1 295 ? -48.741 26.529 2.779   1.00 15.32 ? 295 TYR A OH  1 
ATOM   2511 N N   . TYR A 1 296 ? -48.552 18.299 1.776   1.00 15.92 ? 296 TYR A N   1 
ATOM   2512 C CA  . TYR A 1 296 ? -48.131 16.984 1.299   1.00 14.14 ? 296 TYR A CA  1 
ATOM   2513 C C   . TYR A 1 296 ? -47.046 17.195 0.254   1.00 13.59 ? 296 TYR A C   1 
ATOM   2514 O O   . TYR A 1 296 ? -47.331 17.692 -0.840  1.00 16.03 ? 296 TYR A O   1 
ATOM   2515 C CB  . TYR A 1 296 ? -49.310 16.205 0.708   1.00 15.20 ? 296 TYR A CB  1 
ATOM   2516 C CG  . TYR A 1 296 ? -50.471 15.992 1.672   1.00 18.35 ? 296 TYR A CG  1 
ATOM   2517 C CD1 . TYR A 1 296 ? -50.315 15.244 2.835   1.00 23.59 ? 296 TYR A CD1 1 
ATOM   2518 C CD2 . TYR A 1 296 ? -51.741 16.486 1.380   1.00 29.61 ? 296 TYR A CD2 1 
ATOM   2519 C CE1 . TYR A 1 296 ? -51.400 15.030 3.707   1.00 19.62 ? 296 TYR A CE1 1 
ATOM   2520 C CE2 . TYR A 1 296 ? -52.818 16.277 2.242   1.00 27.63 ? 296 TYR A CE2 1 
ATOM   2521 C CZ  . TYR A 1 296 ? -52.632 15.554 3.405   1.00 29.43 ? 296 TYR A CZ  1 
ATOM   2522 O OH  . TYR A 1 296 ? -53.694 15.346 4.259   1.00 27.71 ? 296 TYR A OH  1 
ATOM   2523 N N   . PHE A 1 297 ? -45.811 16.816 0.584   1.00 14.15 ? 297 PHE A N   1 
ATOM   2524 C CA  . PHE A 1 297 ? -44.721 16.859 -0.389  1.00 11.21 ? 297 PHE A CA  1 
ATOM   2525 C C   . PHE A 1 297 ? -44.941 15.758 -1.414  1.00 12.90 ? 297 PHE A C   1 
ATOM   2526 O O   . PHE A 1 297 ? -44.823 14.573 -1.091  1.00 13.94 ? 297 PHE A O   1 
ATOM   2527 C CB  . PHE A 1 297 ? -43.374 16.700 0.308   1.00 11.65 ? 297 PHE A CB  1 
ATOM   2528 C CG  . PHE A 1 297 ? -42.196 16.694 -0.635  1.00 12.89 ? 297 PHE A CG  1 
ATOM   2529 C CD1 . PHE A 1 297 ? -41.740 17.884 -1.189  1.00 15.83 ? 297 PHE A CD1 1 
ATOM   2530 C CD2 . PHE A 1 297 ? -41.552 15.512 -0.965  1.00 13.16 ? 297 PHE A CD2 1 
ATOM   2531 C CE1 . PHE A 1 297 ? -40.654 17.886 -2.063  1.00 16.62 ? 297 PHE A CE1 1 
ATOM   2532 C CE2 . PHE A 1 297 ? -40.466 15.505 -1.845  1.00 16.28 ? 297 PHE A CE2 1 
ATOM   2533 C CZ  . PHE A 1 297 ? -40.018 16.697 -2.390  1.00 16.42 ? 297 PHE A CZ  1 
ATOM   2534 N N   . ARG A 1 298 ? -45.289 16.156 -2.642  1.00 14.26 ? 298 ARG A N   1 
ATOM   2535 C CA  . ARG A 1 298 ? -45.486 15.249 -3.783  1.00 14.34 ? 298 ARG A CA  1 
ATOM   2536 C C   . ARG A 1 298 ? -46.513 14.160 -3.487  1.00 13.08 ? 298 ARG A C   1 
ATOM   2537 O O   . ARG A 1 298 ? -46.430 13.056 -4.025  1.00 17.20 ? 298 ARG A O   1 
ATOM   2538 C CB  . ARG A 1 298 ? -44.154 14.648 -4.236  1.00 17.87 ? 298 ARG A CB  1 
ATOM   2539 C CG  . ARG A 1 298 ? -43.173 15.742 -4.608  1.00 16.48 ? 298 ARG A CG  1 
ATOM   2540 C CD  . ARG A 1 298 ? -41.868 15.203 -5.176  1.00 18.36 ? 298 ARG A CD  1 
ATOM   2541 N NE  . ARG A 1 298 ? -40.993 16.332 -5.480  1.00 17.99 ? 298 ARG A NE  1 
ATOM   2542 C CZ  . ARG A 1 298 ? -39.716 16.231 -5.817  1.00 18.66 ? 298 ARG A CZ  1 
ATOM   2543 N NH1 . ARG A 1 298 ? -39.129 15.036 -5.900  1.00 19.21 ? 298 ARG A NH1 1 
ATOM   2544 N NH2 . ARG A 1 298 ? -39.027 17.339 -6.073  1.00 18.68 ? 298 ARG A NH2 1 
ATOM   2545 N N   . GLU A 1 299 ? -47.468 14.482 -2.606  1.00 14.49 ? 299 GLU A N   1 
ATOM   2546 C CA  . GLU A 1 299 ? -48.532 13.574 -2.184  1.00 17.08 ? 299 GLU A CA  1 
ATOM   2547 C C   . GLU A 1 299 ? -47.991 12.344 -1.469  1.00 19.57 ? 299 GLU A C   1 
ATOM   2548 O O   . GLU A 1 299 ? -48.685 11.330 -1.375  1.00 20.64 ? 299 GLU A O   1 
ATOM   2549 C CB  . GLU A 1 299 ? -49.426 13.167 -3.370  1.00 15.97 ? 299 GLU A CB  1 
ATOM   2550 C CG  . GLU A 1 299 ? -50.080 14.362 -4.064  1.00 19.62 ? 299 GLU A CG  1 
ATOM   2551 C CD  . GLU A 1 299 ? -51.056 13.966 -5.156  1.00 27.17 ? 299 GLU A CD  1 
ATOM   2552 O OE1 . GLU A 1 299 ? -52.251 14.303 -5.028  1.00 40.12 ? 299 GLU A OE1 1 
ATOM   2553 O OE2 . GLU A 1 299 ? -50.627 13.327 -6.142  1.00 29.72 ? 299 GLU A OE2 1 
ATOM   2554 N N   . LEU A 1 300 ? -46.770 12.432 -0.918  1.00 14.56 ? 300 LEU A N   1 
ATOM   2555 C CA  . LEU A 1 300 ? -46.090 11.269 -0.348  1.00 16.56 ? 300 LEU A CA  1 
ATOM   2556 C C   . LEU A 1 300 ? -45.822 11.374 1.148   1.00 18.12 ? 300 LEU A C   1 
ATOM   2557 O O   . LEU A 1 300 ? -45.933 10.372 1.858   1.00 24.25 ? 300 LEU A O   1 
ATOM   2558 C CB  . LEU A 1 300 ? -44.753 11.033 -1.074  1.00 19.03 ? 300 LEU A CB  1 
ATOM   2559 C CG  . LEU A 1 300 ? -44.729 10.592 -2.542  1.00 31.16 ? 300 LEU A CG  1 
ATOM   2560 C CD1 . LEU A 1 300 ? -43.276 10.462 -2.995  1.00 36.92 ? 300 LEU A CD1 1 
ATOM   2561 C CD2 . LEU A 1 300 ? -45.475 9.292  -2.748  1.00 27.84 ? 300 LEU A CD2 1 
ATOM   2562 N N   . ILE A 1 301 ? -45.435 12.541 1.655   1.00 15.69 ? 301 ILE A N   1 
ATOM   2563 C CA  . ILE A 1 301 ? -45.115 12.701 3.073   1.00 14.92 ? 301 ILE A CA  1 
ATOM   2564 C C   . ILE A 1 301 ? -45.718 14.020 3.538   1.00 14.46 ? 301 ILE A C   1 
ATOM   2565 O O   . ILE A 1 301 ? -45.664 15.024 2.823   1.00 18.27 ? 301 ILE A O   1 
ATOM   2566 C CB  . ILE A 1 301 ? -43.586 12.637 3.332   1.00 19.63 ? 301 ILE A CB  1 
ATOM   2567 C CG1 . ILE A 1 301 ? -43.266 12.799 4.822   1.00 19.36 ? 301 ILE A CG1 1 
ATOM   2568 C CG2 . ILE A 1 301 ? -42.842 13.703 2.517   1.00 18.25 ? 301 ILE A CG2 1 
ATOM   2569 C CD1 . ILE A 1 301 ? -41.776 12.641 5.168   1.00 19.51 ? 301 ILE A CD1 1 
ATOM   2570 N N   . SER A 1 302 ? -46.310 14.012 4.729   1.00 13.53 ? 302 SER A N   1 
ATOM   2571 C CA  . SER A 1 302 ? -46.877 15.226 5.305   1.00 13.67 ? 302 SER A CA  1 
ATOM   2572 C C   . SER A 1 302 ? -45.803 16.114 5.916   1.00 13.28 ? 302 SER A C   1 
ATOM   2573 O O   . SER A 1 302 ? -44.857 15.636 6.547   1.00 13.77 ? 302 SER A O   1 
ATOM   2574 C CB  . SER A 1 302 ? -47.916 14.865 6.365   1.00 14.59 ? 302 SER A CB  1 
ATOM   2575 O OG  . SER A 1 302 ? -49.008 14.180 5.763   1.00 18.84 ? 302 SER A OG  1 
ATOM   2576 N N   . VAL A 1 303 ? -45.953 17.421 5.718   1.00 13.04 ? 303 VAL A N   1 
ATOM   2577 C CA  . VAL A 1 303 ? -44.995 18.405 6.200   1.00 11.15 ? 303 VAL A CA  1 
ATOM   2578 C C   . VAL A 1 303 ? -45.770 19.544 6.838   1.00 11.94 ? 303 VAL A C   1 
ATOM   2579 O O   . VAL A 1 303 ? -46.675 20.106 6.215   1.00 13.28 ? 303 VAL A O   1 
ATOM   2580 C CB  . VAL A 1 303 ? -44.103 18.950 5.064   1.00 12.68 ? 303 VAL A CB  1 
ATOM   2581 C CG1 . VAL A 1 303 ? -43.130 20.000 5.604   1.00 16.13 ? 303 VAL A CG1 1 
ATOM   2582 C CG2 . VAL A 1 303 ? -43.344 17.812 4.365   1.00 13.39 ? 303 VAL A CG2 1 
ATOM   2583 N N   . PHE A 1 304 ? -45.430 19.879 8.077   1.00 13.01 ? 304 PHE A N   1 
ATOM   2584 C CA  . PHE A 1 304 ? -45.914 21.101 8.694   1.00 12.06 ? 304 PHE A CA  1 
ATOM   2585 C C   . PHE A 1 304 ? -44.765 22.085 8.808   1.00 12.72 ? 304 PHE A C   1 
ATOM   2586 O O   . PHE A 1 304 ? -43.618 21.699 9.046   1.00 13.41 ? 304 PHE A O   1 
ATOM   2587 C CB  . PHE A 1 304 ? -46.505 20.855 10.079  1.00 13.35 ? 304 PHE A CB  1 
ATOM   2588 C CG  . PHE A 1 304 ? -47.881 20.255 10.061  1.00 13.87 ? 304 PHE A CG  1 
ATOM   2589 C CD1 . PHE A 1 304 ? -49.009 21.044 9.825   1.00 16.95 ? 304 PHE A CD1 1 
ATOM   2590 C CD2 . PHE A 1 304 ? -48.051 18.903 10.296  1.00 13.75 ? 304 PHE A CD2 1 
ATOM   2591 C CE1 . PHE A 1 304 ? -50.290 20.480 9.833   1.00 16.11 ? 304 PHE A CE1 1 
ATOM   2592 C CE2 . PHE A 1 304 ? -49.337 18.326 10.292  1.00 15.14 ? 304 PHE A CE2 1 
ATOM   2593 C CZ  . PHE A 1 304 ? -50.445 19.122 10.077  1.00 16.20 ? 304 PHE A CZ  1 
ATOM   2594 N N   . PHE A 1 305 ? -45.077 23.357 8.640   1.00 13.86 ? 305 PHE A N   1 
ATOM   2595 C CA  . PHE A 1 305 ? -44.106 24.424 8.801   1.00 14.09 ? 305 PHE A CA  1 
ATOM   2596 C C   . PHE A 1 305 ? -44.443 25.166 10.080  1.00 12.24 ? 305 PHE A C   1 
ATOM   2597 O O   . PHE A 1 305 ? -45.568 25.644 10.243  1.00 13.51 ? 305 PHE A O   1 
ATOM   2598 C CB  . PHE A 1 305 ? -44.132 25.352 7.592   1.00 12.12 ? 305 PHE A CB  1 
ATOM   2599 C CG  . PHE A 1 305 ? -43.789 24.652 6.311   1.00 12.04 ? 305 PHE A CG  1 
ATOM   2600 C CD1 . PHE A 1 305 ? -44.769 23.992 5.575   1.00 14.87 ? 305 PHE A CD1 1 
ATOM   2601 C CD2 . PHE A 1 305 ? -42.489 24.642 5.853   1.00 13.17 ? 305 PHE A CD2 1 
ATOM   2602 C CE1 . PHE A 1 305 ? -44.441 23.338 4.389   1.00 13.11 ? 305 PHE A CE1 1 
ATOM   2603 C CE2 . PHE A 1 305 ? -42.155 24.005 4.664   1.00 12.76 ? 305 PHE A CE2 1 
ATOM   2604 C CZ  . PHE A 1 305 ? -43.146 23.342 3.937   1.00 13.20 ? 305 PHE A CZ  1 
ATOM   2605 N N   . ARG A 1 306 ? -43.471 25.254 10.986  1.00 10.58 ? 306 ARG A N   1 
ATOM   2606 C CA  . ARG A 1 306 ? -43.738 25.889 12.268  1.00 9.85  ? 306 ARG A CA  1 
ATOM   2607 C C   . ARG A 1 306 ? -44.046 27.371 12.092  1.00 11.59 ? 306 ARG A C   1 
ATOM   2608 O O   . ARG A 1 306 ? -43.570 28.032 11.166  1.00 12.16 ? 306 ARG A O   1 
ATOM   2609 C CB  . ARG A 1 306 ? -42.539 25.717 13.216  1.00 11.05 ? 306 ARG A CB  1 
ATOM   2610 C CG  . ARG A 1 306 ? -41.350 26.607 12.885  1.00 13.51 ? 306 ARG A CG  1 
ATOM   2611 C CD  . ARG A 1 306 ? -40.231 26.508 13.928  1.00 14.38 ? 306 ARG A CD  1 
ATOM   2612 N NE  . ARG A 1 306 ? -39.163 27.429 13.555  1.00 11.59 ? 306 ARG A NE  1 
ATOM   2613 C CZ  . ARG A 1 306 ? -38.221 27.888 14.370  1.00 11.65 ? 306 ARG A CZ  1 
ATOM   2614 N NH1 . ARG A 1 306 ? -38.183 27.511 15.648  1.00 14.64 ? 306 ARG A NH1 1 
ATOM   2615 N NH2 . ARG A 1 306 ? -37.316 28.732 13.887  1.00 12.30 ? 306 ARG A NH2 1 
ATOM   2616 N N   . ASP A 1 307 ? -44.857 27.887 13.008  1.00 12.58 ? 307 ASP A N   1 
ATOM   2617 C CA  . ASP A 1 307 ? -45.017 29.322 13.150  1.00 9.50  ? 307 ASP A CA  1 
ATOM   2618 C C   . ASP A 1 307 ? -43.749 29.858 13.796  1.00 10.82 ? 307 ASP A C   1 
ATOM   2619 O O   . ASP A 1 307 ? -43.521 29.660 14.995  1.00 14.17 ? 307 ASP A O   1 
ATOM   2620 C CB  . ASP A 1 307 ? -46.254 29.618 13.992  1.00 12.79 ? 307 ASP A CB  1 
ATOM   2621 C CG  . ASP A 1 307 ? -46.595 31.076 14.005  1.00 15.24 ? 307 ASP A CG  1 
ATOM   2622 O OD1 . ASP A 1 307 ? -45.687 31.880 14.281  1.00 15.92 ? 307 ASP A OD1 1 
ATOM   2623 O OD2 . ASP A 1 307 ? -47.758 31.430 13.715  1.00 20.17 ? 307 ASP A OD2 1 
ATOM   2624 N N   . LYS A 1 308 ? -42.913 30.516 12.993  1.00 11.63 ? 308 LYS A N   1 
ATOM   2625 C CA  . LYS A 1 308 ? -41.615 30.940 13.498  1.00 11.59 ? 308 LYS A CA  1 
ATOM   2626 C C   . LYS A 1 308 ? -41.758 31.996 14.589  1.00 11.77 ? 308 LYS A C   1 
ATOM   2627 O O   . LYS A 1 308 ? -40.997 31.989 15.558  1.00 14.31 ? 308 LYS A O   1 
ATOM   2628 C CB  . LYS A 1 308 ? -40.766 31.462 12.345  1.00 15.17 ? 308 LYS A CB  1 
ATOM   2629 C CG  . LYS A 1 308 ? -39.419 32.036 12.737  1.00 16.36 ? 308 LYS A CG  1 
ATOM   2630 C CD  . LYS A 1 308 ? -38.660 32.449 11.474  1.00 17.87 ? 308 LYS A CD  1 
ATOM   2631 C CE  . LYS A 1 308 ? -37.487 33.353 11.802  1.00 20.03 ? 308 LYS A CE  1 
ATOM   2632 N NZ  . LYS A 1 308 ? -36.615 32.666 12.769  1.00 26.43 ? 308 LYS A NZ  1 
ATOM   2633 N N   . THR A 1 309 ? -42.694 32.932 14.429  1.00 12.68 ? 309 THR A N   1 
ATOM   2634 C CA  . THR A 1 309 ? -42.858 34.003 15.411  1.00 13.02 ? 309 THR A CA  1 
ATOM   2635 C C   . THR A 1 309 ? -43.196 33.446 16.788  1.00 14.84 ? 309 THR A C   1 
ATOM   2636 O O   . THR A 1 309 ? -42.548 33.790 17.789  1.00 13.28 ? 309 THR A O   1 
ATOM   2637 C CB  . THR A 1 309 ? -43.942 34.963 14.937  1.00 15.83 ? 309 THR A CB  1 
ATOM   2638 O OG1 . THR A 1 309 ? -43.443 35.658 13.793  1.00 20.63 ? 309 THR A OG1 1 
ATOM   2639 C CG2 . THR A 1 309 ? -44.306 35.965 16.030  1.00 18.69 ? 309 THR A CG2 1 
ATOM   2640 N N   . LEU A 1 310 ? -44.195 32.565 16.857  1.00 14.35 ? 310 LEU A N   1 
ATOM   2641 C CA  . LEU A 1 310 ? -44.576 31.985 18.139  1.00 12.30 ? 310 LEU A CA  1 
ATOM   2642 C C   . LEU A 1 310 ? -43.439 31.169 18.730  1.00 12.43 ? 310 LEU A C   1 
ATOM   2643 O O   . LEU A 1 310 ? -43.189 31.223 19.941  1.00 13.80 ? 310 LEU A O   1 
ATOM   2644 C CB  . LEU A 1 310 ? -45.823 31.117 17.969  1.00 12.54 ? 310 LEU A CB  1 
ATOM   2645 C CG  . LEU A 1 310 ? -47.083 31.914 17.633  1.00 14.17 ? 310 LEU A CG  1 
ATOM   2646 C CD1 . LEU A 1 310 ? -48.175 30.955 17.264  1.00 18.00 ? 310 LEU A CD1 1 
ATOM   2647 C CD2 . LEU A 1 310 ? -47.534 32.746 18.803  1.00 16.44 ? 310 LEU A CD2 1 
ATOM   2648 N N   . SER A 1 311 ? -42.740 30.405 17.886  1.00 12.00 ? 311 SER A N   1 
ATOM   2649 C CA  . SER A 1 311 ? -41.634 29.584 18.374  1.00 11.27 ? 311 SER A CA  1 
ATOM   2650 C C   . SER A 1 311 ? -40.523 30.463 18.930  1.00 12.31 ? 311 SER A C   1 
ATOM   2651 O O   . SER A 1 311 ? -39.961 30.172 19.994  1.00 14.72 ? 311 SER A O   1 
ATOM   2652 C CB  . SER A 1 311 ? -41.108 28.702 17.242  1.00 11.52 ? 311 SER A CB  1 
ATOM   2653 O OG  . SER A 1 311 ? -42.146 27.900 16.676  1.00 11.38 ? 311 SER A OG  1 
ATOM   2654 N N   . ASP A 1 312 ? -40.224 31.572 18.243  1.00 11.74 ? 312 ASP A N   1 
ATOM   2655 C CA  . ASP A 1 312 ? -39.126 32.427 18.677  1.00 13.82 ? 312 ASP A CA  1 
ATOM   2656 C C   . ASP A 1 312 ? -39.517 33.380 19.803  1.00 13.49 ? 312 ASP A C   1 
ATOM   2657 O O   . ASP A 1 312 ? -38.624 33.891 20.493  1.00 13.34 ? 312 ASP A O   1 
ATOM   2658 C CB  . ASP A 1 312 ? -38.563 33.218 17.491  1.00 13.22 ? 312 ASP A CB  1 
ATOM   2659 C CG  . ASP A 1 312 ? -37.616 32.389 16.614  1.00 13.91 ? 312 ASP A CG  1 
ATOM   2660 O OD1 . ASP A 1 312 ? -37.239 31.265 16.989  1.00 20.28 ? 312 ASP A OD1 1 
ATOM   2661 O OD2 . ASP A 1 312 ? -37.236 32.898 15.542  1.00 20.96 ? 312 ASP A OD2 1 
ATOM   2662 N N   . LEU A 1 313 ? -40.810 33.634 20.027  1.00 12.58 ? 313 LEU A N   1 
ATOM   2663 C CA  . LEU A 1 313 ? -41.202 34.358 21.237  1.00 12.84 ? 313 LEU A CA  1 
ATOM   2664 C C   . LEU A 1 313 ? -40.746 33.610 22.484  1.00 12.73 ? 313 LEU A C   1 
ATOM   2665 O O   . LEU A 1 313 ? -40.173 34.197 23.414  1.00 14.55 ? 313 LEU A O   1 
ATOM   2666 C CB  . LEU A 1 313 ? -42.719 34.555 21.268  1.00 14.29 ? 313 LEU A CB  1 
ATOM   2667 C CG  . LEU A 1 313 ? -43.241 35.656 20.348  1.00 14.30 ? 313 LEU A CG  1 
ATOM   2668 C CD1 . LEU A 1 313 ? -44.748 35.539 20.178  1.00 14.74 ? 313 LEU A CD1 1 
ATOM   2669 C CD2 . LEU A 1 313 ? -42.854 37.022 20.881  1.00 15.91 ? 313 LEU A CD2 1 
ATOM   2670 N N   . ILE A 1 314 ? -41.001 32.298 22.519  1.00 14.43 ? 314 ILE A N   1 
ATOM   2671 C CA  . ILE A 1 314 ? -40.600 31.493 23.665  1.00 13.04 ? 314 ILE A CA  1 
ATOM   2672 C C   . ILE A 1 314 ? -39.085 31.372 23.708  1.00 13.51 ? 314 ILE A C   1 
ATOM   2673 O O   . ILE A 1 314 ? -38.455 31.543 24.763  1.00 15.89 ? 314 ILE A O   1 
ATOM   2674 C CB  . ILE A 1 314 ? -41.283 30.112 23.589  1.00 12.49 ? 314 ILE A CB  1 
ATOM   2675 C CG1 . ILE A 1 314 ? -42.806 30.285 23.660  1.00 14.88 ? 314 ILE A CG1 1 
ATOM   2676 C CG2 . ILE A 1 314 ? -40.749 29.192 24.695  1.00 15.00 ? 314 ILE A CG2 1 
ATOM   2677 C CD1 . ILE A 1 314 ? -43.592 28.960 23.551  1.00 14.68 ? 314 ILE A CD1 1 
ATOM   2678 N N   . GLY A 1 315 ? -38.471 31.152 22.545  1.00 12.56 ? 315 GLY A N   1 
ATOM   2679 C CA  . GLY A 1 315 ? -37.040 30.898 22.522  1.00 13.23 ? 315 GLY A CA  1 
ATOM   2680 C C   . GLY A 1 315 ? -36.189 32.123 22.760  1.00 13.95 ? 315 GLY A C   1 
ATOM   2681 O O   . GLY A 1 315 ? -35.095 32.017 23.327  1.00 15.56 ? 315 GLY A O   1 
ATOM   2682 N N   . PHE A 1 316 ? -36.669 33.302 22.353  1.00 12.38 ? 316 PHE A N   1 
ATOM   2683 C CA  . PHE A 1 316 ? -35.804 34.479 22.351  1.00 14.03 ? 316 PHE A CA  1 
ATOM   2684 C C   . PHE A 1 316 ? -36.323 35.680 23.129  1.00 17.86 ? 316 PHE A C   1 
ATOM   2685 O O   . PHE A 1 316 ? -35.524 36.464 23.643  1.00 20.09 ? 316 PHE A O   1 
ATOM   2686 C CB  . PHE A 1 316 ? -35.518 34.922 20.907  1.00 15.31 ? 316 PHE A CB  1 
ATOM   2687 C CG  . PHE A 1 316 ? -34.622 33.970 20.157  1.00 14.87 ? 316 PHE A CG  1 
ATOM   2688 C CD1 . PHE A 1 316 ? -33.244 34.104 20.230  1.00 20.12 ? 316 PHE A CD1 1 
ATOM   2689 C CD2 . PHE A 1 316 ? -35.154 32.924 19.411  1.00 14.70 ? 316 PHE A CD2 1 
ATOM   2690 C CE1 . PHE A 1 316 ? -32.410 33.227 19.559  1.00 20.63 ? 316 PHE A CE1 1 
ATOM   2691 C CE2 . PHE A 1 316 ? -34.324 32.049 18.737  1.00 17.69 ? 316 PHE A CE2 1 
ATOM   2692 C CZ  . PHE A 1 316 ? -32.956 32.199 18.812  1.00 17.03 ? 316 PHE A CZ  1 
ATOM   2693 N N   A SER A 1 317 ? -37.640 35.846 23.230  0.40 14.53 ? 317 SER A N   1 
ATOM   2694 N N   B SER A 1 317 ? -37.642 35.851 23.219  0.60 14.07 ? 317 SER A N   1 
ATOM   2695 C CA  A SER A 1 317 ? -38.190 37.066 23.810  0.40 13.74 ? 317 SER A CA  1 
ATOM   2696 C CA  B SER A 1 317 ? -38.210 37.062 23.805  0.60 13.73 ? 317 SER A CA  1 
ATOM   2697 C C   A SER A 1 317 ? -38.599 36.919 25.271  0.40 16.04 ? 317 SER A C   1 
ATOM   2698 C C   B SER A 1 317 ? -38.570 36.896 25.278  0.60 16.36 ? 317 SER A C   1 
ATOM   2699 O O   A SER A 1 317 ? -38.180 37.717 26.112  0.40 17.12 ? 317 SER A O   1 
ATOM   2700 O O   B SER A 1 317 ? -38.097 37.654 26.127  0.60 16.72 ? 317 SER A O   1 
ATOM   2701 C CB  A SER A 1 317 ? -39.397 37.542 22.991  0.40 15.71 ? 317 SER A CB  1 
ATOM   2702 C CB  B SER A 1 317 ? -39.459 37.496 23.023  0.60 14.84 ? 317 SER A CB  1 
ATOM   2703 O OG  A SER A 1 317 ? -39.797 38.842 23.393  0.40 16.64 ? 317 SER A OG  1 
ATOM   2704 O OG  B SER A 1 317 ? -39.170 37.675 21.649  0.60 12.95 ? 317 SER A OG  1 
ATOM   2705 N N   . TYR A 1 318 ? -39.412 35.913 25.592  1.00 15.03 ? 318 TYR A N   1 
ATOM   2706 C CA  . TYR A 1 318 ? -40.124 35.917 26.865  1.00 14.66 ? 318 TYR A CA  1 
ATOM   2707 C C   . TYR A 1 318 ? -39.235 35.722 28.090  1.00 15.78 ? 318 TYR A C   1 
ATOM   2708 O O   . TYR A 1 318 ? -39.694 36.005 29.199  1.00 17.39 ? 318 TYR A O   1 
ATOM   2709 C CB  . TYR A 1 318 ? -41.208 34.838 26.849  1.00 14.85 ? 318 TYR A CB  1 
ATOM   2710 C CG  . TYR A 1 318 ? -42.400 35.114 25.944  1.00 14.93 ? 318 TYR A CG  1 
ATOM   2711 C CD1 . TYR A 1 318 ? -42.736 36.404 25.549  1.00 14.06 ? 318 TYR A CD1 1 
ATOM   2712 C CD2 . TYR A 1 318 ? -43.192 34.071 25.508  1.00 16.57 ? 318 TYR A CD2 1 
ATOM   2713 C CE1 . TYR A 1 318 ? -43.848 36.635 24.747  1.00 14.65 ? 318 TYR A CE1 1 
ATOM   2714 C CE2 . TYR A 1 318 ? -44.288 34.281 24.703  1.00 13.63 ? 318 TYR A CE2 1 
ATOM   2715 C CZ  . TYR A 1 318 ? -44.613 35.563 24.329  1.00 16.29 ? 318 TYR A CZ  1 
ATOM   2716 O OH  . TYR A 1 318 ? -45.718 35.735 23.537  1.00 16.89 ? 318 TYR A OH  1 
ATOM   2717 N N   . HIS A 1 319 ? -37.988 35.262 27.937  1.00 16.90 ? 319 HIS A N   1 
ATOM   2718 C CA  . HIS A 1 319 ? -37.130 35.134 29.117  1.00 16.47 ? 319 HIS A CA  1 
ATOM   2719 C C   . HIS A 1 319 ? -36.972 36.463 29.847  1.00 21.78 ? 319 HIS A C   1 
ATOM   2720 O O   . HIS A 1 319 ? -36.767 36.481 31.061  1.00 23.19 ? 319 HIS A O   1 
ATOM   2721 C CB  . HIS A 1 319 ? -35.749 34.604 28.736  1.00 17.91 ? 319 HIS A CB  1 
ATOM   2722 C CG  . HIS A 1 319 ? -34.905 35.591 27.986  1.00 22.34 ? 319 HIS A CG  1 
ATOM   2723 N ND1 . HIS A 1 319 ? -35.013 35.784 26.625  1.00 23.50 ? 319 HIS A ND1 1 
ATOM   2724 C CD2 . HIS A 1 319 ? -33.943 36.447 28.414  1.00 23.88 ? 319 HIS A CD2 1 
ATOM   2725 C CE1 . HIS A 1 319 ? -34.155 36.718 26.248  1.00 24.34 ? 319 HIS A CE1 1 
ATOM   2726 N NE2 . HIS A 1 319 ? -33.488 37.130 27.311  1.00 26.58 ? 319 HIS A NE2 1 
ATOM   2727 N N   . ALA A 1 320 ? -37.063 37.575 29.122  1.00 19.57 ? 320 ALA A N   1 
ATOM   2728 C CA  . ALA A 1 320 ? -36.875 38.911 29.676  1.00 25.43 ? 320 ALA A CA  1 
ATOM   2729 C C   . ALA A 1 320 ? -38.176 39.555 30.140  1.00 29.03 ? 320 ALA A C   1 
ATOM   2730 O O   . ALA A 1 320 ? -38.152 40.692 30.625  1.00 31.41 ? 320 ALA A O   1 
ATOM   2731 C CB  . ALA A 1 320 ? -36.202 39.809 28.636  1.00 26.76 ? 320 ALA A CB  1 
ATOM   2732 N N   . TRP A 1 321 ? -39.302 38.871 29.990  1.00 19.05 ? 321 TRP A N   1 
ATOM   2733 C CA  . TRP A 1 321 ? -40.606 39.373 30.385  1.00 23.95 ? 321 TRP A CA  1 
ATOM   2734 C C   . TRP A 1 321 ? -41.033 38.728 31.688  1.00 23.87 ? 321 TRP A C   1 
ATOM   2735 O O   . TRP A 1 321 ? -40.521 37.674 32.072  1.00 29.82 ? 321 TRP A O   1 
ATOM   2736 C CB  . TRP A 1 321 ? -41.666 39.063 29.329  1.00 20.17 ? 321 TRP A CB  1 
ATOM   2737 C CG  . TRP A 1 321 ? -41.390 39.506 27.930  1.00 22.08 ? 321 TRP A CG  1 
ATOM   2738 C CD1 . TRP A 1 321 ? -40.176 39.646 27.315  1.00 23.07 ? 321 TRP A CD1 1 
ATOM   2739 C CD2 . TRP A 1 321 ? -42.373 39.847 26.961  1.00 22.85 ? 321 TRP A CD2 1 
ATOM   2740 N NE1 . TRP A 1 321 ? -40.351 40.070 26.015  1.00 26.08 ? 321 TRP A NE1 1 
ATOM   2741 C CE2 . TRP A 1 321 ? -41.693 40.191 25.772  1.00 20.85 ? 321 TRP A CE2 1 
ATOM   2742 C CE3 . TRP A 1 321 ? -43.770 39.900 26.983  1.00 20.74 ? 321 TRP A CE3 1 
ATOM   2743 C CZ2 . TRP A 1 321 ? -42.365 40.588 24.613  1.00 24.60 ? 321 TRP A CZ2 1 
ATOM   2744 C CZ3 . TRP A 1 321 ? -44.437 40.295 25.826  1.00 23.97 ? 321 TRP A CZ3 1 
ATOM   2745 C CH2 . TRP A 1 321 ? -43.730 40.631 24.661  1.00 21.83 ? 321 TRP A CH2 1 
ATOM   2746 N N   . ASN A 1 322 ? -42.010 39.345 32.352  1.00 25.22 ? 322 ASN A N   1 
ATOM   2747 C CA  . ASN A 1 322 ? -42.626 38.607 33.443  1.00 30.29 ? 322 ASN A CA  1 
ATOM   2748 C C   . ASN A 1 322 ? -43.676 37.652 32.879  1.00 28.95 ? 322 ASN A C   1 
ATOM   2749 O O   . ASN A 1 322 ? -44.130 37.786 31.736  1.00 30.25 ? 322 ASN A O   1 
ATOM   2750 C CB  . ASN A 1 322 ? -43.187 39.554 34.518  1.00 41.31 ? 322 ASN A CB  1 
ATOM   2751 C CG  . ASN A 1 322 ? -44.473 40.272 34.114  1.00 47.92 ? 322 ASN A CG  1 
ATOM   2752 O OD1 . ASN A 1 322 ? -45.365 39.713 33.473  1.00 52.47 ? 322 ASN A OD1 1 
ATOM   2753 N ND2 . ASN A 1 322 ? -44.572 41.537 34.519  1.00 55.19 ? 322 ASN A ND2 1 
ATOM   2754 N N   . ALA A 1 323 ? -44.024 36.647 33.678  1.00 20.95 ? 323 ALA A N   1 
ATOM   2755 C CA  . ALA A 1 323 ? -44.770 35.520 33.133  1.00 22.69 ? 323 ALA A CA  1 
ATOM   2756 C C   . ALA A 1 323 ? -46.151 35.939 32.650  1.00 18.95 ? 323 ALA A C   1 
ATOM   2757 O O   . ALA A 1 323 ? -46.617 35.456 31.611  1.00 21.77 ? 323 ALA A O   1 
ATOM   2758 C CB  . ALA A 1 323 ? -44.875 34.407 34.174  1.00 23.78 ? 323 ALA A CB  1 
ATOM   2759 N N   . GLU A 1 324 ? -46.821 36.840 33.378  1.00 22.88 ? 324 GLU A N   1 
ATOM   2760 C CA  . GLU A 1 324 ? -48.163 37.247 32.967  1.00 32.56 ? 324 GLU A CA  1 
ATOM   2761 C C   . GLU A 1 324 ? -48.135 38.073 31.682  1.00 29.56 ? 324 GLU A C   1 
ATOM   2762 O O   . GLU A 1 324 ? -48.979 37.873 30.801  1.00 31.40 ? 324 GLU A O   1 
ATOM   2763 C CB  . GLU A 1 324 ? -48.863 38.011 34.096  1.00 42.71 ? 324 GLU A CB  1 
ATOM   2764 C CG  . GLU A 1 324 ? -50.161 38.724 33.690  1.00 54.88 ? 324 GLU A CG  1 
ATOM   2765 C CD  . GLU A 1 324 ? -51.373 37.807 33.579  1.00 65.67 ? 324 GLU A CD  1 
ATOM   2766 O OE1 . GLU A 1 324 ? -51.205 36.570 33.570  1.00 67.92 ? 324 GLU A OE1 1 
ATOM   2767 O OE2 . GLU A 1 324 ? -52.505 38.336 33.497  1.00 70.41 ? 324 GLU A OE2 1 
ATOM   2768 N N   . ASP A 1 325 ? -47.178 39.001 31.553  1.00 28.60 ? 325 ASP A N   1 
ATOM   2769 C CA  . ASP A 1 325 ? -47.028 39.741 30.299  1.00 31.42 ? 325 ASP A CA  1 
ATOM   2770 C C   . ASP A 1 325 ? -46.855 38.782 29.127  1.00 27.11 ? 325 ASP A C   1 
ATOM   2771 O O   . ASP A 1 325 ? -47.500 38.929 28.081  1.00 26.14 ? 325 ASP A O   1 
ATOM   2772 C CB  . ASP A 1 325 ? -45.824 40.691 30.363  1.00 34.54 ? 325 ASP A CB  1 
ATOM   2773 C CG  . ASP A 1 325 ? -46.073 41.935 31.212  1.00 40.60 ? 325 ASP A CG  1 
ATOM   2774 O OD1 . ASP A 1 325 ? -47.174 42.101 31.767  1.00 35.73 ? 325 ASP A OD1 1 
ATOM   2775 O OD2 . ASP A 1 325 ? -45.146 42.771 31.299  1.00 38.64 ? 325 ASP A OD2 1 
ATOM   2776 N N   . ALA A 1 326 ? -45.983 37.784 29.295  1.00 19.77 ? 326 ALA A N   1 
ATOM   2777 C CA  . ALA A 1 326 ? -45.647 36.873 28.203  1.00 18.11 ? 326 ALA A CA  1 
ATOM   2778 C C   . ALA A 1 326 ? -46.842 36.009 27.803  1.00 22.37 ? 326 ALA A C   1 
ATOM   2779 O O   . ALA A 1 326 ? -47.139 35.854 26.608  1.00 19.43 ? 326 ALA A O   1 
ATOM   2780 C CB  . ALA A 1 326 ? -44.458 35.995 28.607  1.00 17.63 ? 326 ALA A CB  1 
ATOM   2781 N N   . VAL A 1 327 ? -47.532 35.423 28.788  1.00 19.90 ? 327 VAL A N   1 
ATOM   2782 C CA  . VAL A 1 327 ? -48.657 34.549 28.467  1.00 20.99 ? 327 VAL A CA  1 
ATOM   2783 C C   . VAL A 1 327 ? -49.785 35.346 27.818  1.00 19.86 ? 327 VAL A C   1 
ATOM   2784 O O   . VAL A 1 327 ? -50.387 34.898 26.838  1.00 21.62 ? 327 VAL A O   1 
ATOM   2785 C CB  . VAL A 1 327 ? -49.137 33.791 29.717  1.00 22.69 ? 327 VAL A CB  1 
ATOM   2786 C CG1 . VAL A 1 327 ? -50.404 33.008 29.407  1.00 21.76 ? 327 VAL A CG1 1 
ATOM   2787 C CG2 . VAL A 1 327 ? -48.037 32.851 30.221  1.00 19.86 ? 327 VAL A CG2 1 
ATOM   2788 N N   . ARG A 1 328 ? -50.090 36.532 28.353  1.00 19.21 ? 328 ARG A N   1 
ATOM   2789 C CA  . ARG A 1 328 ? -51.084 37.398 27.729  1.00 23.11 ? 328 ARG A CA  1 
ATOM   2790 C C   . ARG A 1 328 ? -50.712 37.713 26.286  1.00 23.48 ? 328 ARG A C   1 
ATOM   2791 O O   . ARG A 1 328 ? -51.572 37.696 25.393  1.00 22.72 ? 328 ARG A O   1 
ATOM   2792 C CB  . ARG A 1 328 ? -51.219 38.682 28.529  1.00 32.06 ? 328 ARG A CB  1 
ATOM   2793 C CG  . ARG A 1 328 ? -52.348 38.639 29.512  1.00 41.30 ? 328 ARG A CG  1 
ATOM   2794 C CD  . ARG A 1 328 ? -52.613 40.030 30.042  1.00 48.66 ? 328 ARG A CD  1 
ATOM   2795 N NE  . ARG A 1 328 ? -51.380 40.749 30.346  1.00 57.71 ? 328 ARG A NE  1 
ATOM   2796 C CZ  . ARG A 1 328 ? -51.108 41.989 29.952  1.00 56.21 ? 328 ARG A CZ  1 
ATOM   2797 N NH1 . ARG A 1 328 ? -51.973 42.682 29.223  1.00 59.95 ? 328 ARG A NH1 1 
ATOM   2798 N NH2 . ARG A 1 328 ? -49.959 42.535 30.299  1.00 55.90 ? 328 ARG A NH2 1 
ATOM   2799 N N   . ASP A 1 329 ? -49.434 38.012 26.047  1.00 21.69 ? 329 ASP A N   1 
ATOM   2800 C CA  . ASP A 1 329 ? -48.960 38.283 24.695  1.00 20.99 ? 329 ASP A CA  1 
ATOM   2801 C C   . ASP A 1 329 ? -49.174 37.077 23.790  1.00 20.33 ? 329 ASP A C   1 
ATOM   2802 O O   . ASP A 1 329 ? -49.695 37.205 22.671  1.00 22.92 ? 329 ASP A O   1 
ATOM   2803 C CB  . ASP A 1 329 ? -47.483 38.677 24.748  1.00 21.98 ? 329 ASP A CB  1 
ATOM   2804 C CG  . ASP A 1 329 ? -46.924 39.053 23.392  1.00 19.48 ? 329 ASP A CG  1 
ATOM   2805 O OD1 . ASP A 1 329 ? -47.031 40.240 23.022  1.00 22.75 ? 329 ASP A OD1 1 
ATOM   2806 O OD2 . ASP A 1 329 ? -46.360 38.178 22.701  1.00 21.14 ? 329 ASP A OD2 1 
ATOM   2807 N N   . PHE A 1 330 ? -48.810 35.889 24.277  1.00 17.89 ? 330 PHE A N   1 
ATOM   2808 C CA  . PHE A 1 330 ? -48.902 34.681 23.462  1.00 18.84 ? 330 PHE A CA  1 
ATOM   2809 C C   . PHE A 1 330 ? -50.353 34.380 23.107  1.00 18.52 ? 330 PHE A C   1 
ATOM   2810 O O   . PHE A 1 330 ? -50.681 34.103 21.946  1.00 19.26 ? 330 PHE A O   1 
ATOM   2811 C CB  . PHE A 1 330 ? -48.264 33.518 24.229  1.00 15.25 ? 330 PHE A CB  1 
ATOM   2812 C CG  . PHE A 1 330 ? -47.937 32.306 23.385  1.00 17.47 ? 330 PHE A CG  1 
ATOM   2813 C CD1 . PHE A 1 330 ? -46.777 32.261 22.623  1.00 19.65 ? 330 PHE A CD1 1 
ATOM   2814 C CD2 . PHE A 1 330 ? -48.758 31.185 23.408  1.00 15.33 ? 330 PHE A CD2 1 
ATOM   2815 C CE1 . PHE A 1 330 ? -46.458 31.135 21.867  1.00 19.08 ? 330 PHE A CE1 1 
ATOM   2816 C CE2 . PHE A 1 330 ? -48.445 30.054 22.650  1.00 15.01 ? 330 PHE A CE2 1 
ATOM   2817 C CZ  . PHE A 1 330 ? -47.292 30.031 21.882  1.00 16.81 ? 330 PHE A CZ  1 
ATOM   2818 N N   . ILE A 1 331 ? -51.241 34.436 24.104  1.00 19.66 ? 331 ILE A N   1 
ATOM   2819 C CA  . ILE A 1 331 ? -52.655 34.182 23.850  1.00 18.81 ? 331 ILE A CA  1 
ATOM   2820 C C   . ILE A 1 331 ? -53.206 35.212 22.875  1.00 18.98 ? 331 ILE A C   1 
ATOM   2821 O O   . ILE A 1 331 ? -53.994 34.882 21.983  1.00 20.58 ? 331 ILE A O   1 
ATOM   2822 C CB  . ILE A 1 331 ? -53.449 34.178 25.168  1.00 20.95 ? 331 ILE A CB  1 
ATOM   2823 C CG1 . ILE A 1 331 ? -52.968 33.048 26.078  1.00 24.25 ? 331 ILE A CG1 1 
ATOM   2824 C CG2 . ILE A 1 331 ? -54.951 34.061 24.897  1.00 25.79 ? 331 ILE A CG2 1 
ATOM   2825 C CD1 . ILE A 1 331 ? -53.269 31.666 25.535  1.00 26.46 ? 331 ILE A CD1 1 
ATOM   2826 N N   . GLY A 1 332 ? -52.804 36.477 23.036  1.00 22.15 ? 332 GLY A N   1 
ATOM   2827 C CA  . GLY A 1 332 ? -53.298 37.520 22.149  1.00 22.36 ? 332 GLY A CA  1 
ATOM   2828 C C   . GLY A 1 332 ? -52.923 37.290 20.698  1.00 21.41 ? 332 GLY A C   1 
ATOM   2829 O O   . GLY A 1 332 ? -53.702 37.601 19.789  1.00 22.79 ? 332 GLY A O   1 
ATOM   2830 N N   . ARG A 1 333 ? -51.720 36.766 20.459  1.00 20.03 ? 333 ARG A N   1 
ATOM   2831 C CA  . ARG A 1 333 ? -51.326 36.439 19.097  1.00 18.35 ? 333 ARG A CA  1 
ATOM   2832 C C   . ARG A 1 333 ? -52.110 35.237 18.579  1.00 16.83 ? 333 ARG A C   1 
ATOM   2833 O O   . ARG A 1 333 ? -52.523 35.214 17.411  1.00 20.24 ? 333 ARG A O   1 
ATOM   2834 C CB  . ARG A 1 333 ? -49.817 36.196 19.034  1.00 20.45 ? 333 ARG A CB  1 
ATOM   2835 C CG  . ARG A 1 333 ? -49.257 36.326 17.619  1.00 32.70 ? 333 ARG A CG  1 
ATOM   2836 C CD  . ARG A 1 333 ? -47.741 36.197 17.577  1.00 34.26 ? 333 ARG A CD  1 
ATOM   2837 N NE  . ARG A 1 333 ? -47.048 37.478 17.721  1.00 30.90 ? 333 ARG A NE  1 
ATOM   2838 C CZ  . ARG A 1 333 ? -46.871 38.353 16.735  1.00 35.42 ? 333 ARG A CZ  1 
ATOM   2839 N NH1 . ARG A 1 333 ? -47.346 38.102 15.520  1.00 30.11 ? 333 ARG A NH1 1 
ATOM   2840 N NH2 . ARG A 1 333 ? -46.216 39.486 16.961  1.00 37.29 ? 333 ARG A NH2 1 
ATOM   2841 N N   . LEU A 1 334 ? -52.361 34.246 19.442  1.00 17.00 ? 334 LEU A N   1 
ATOM   2842 C CA  . LEU A 1 334 ? -53.205 33.125 19.044  1.00 17.59 ? 334 LEU A CA  1 
ATOM   2843 C C   . LEU A 1 334 ? -54.614 33.587 18.693  1.00 18.86 ? 334 LEU A C   1 
ATOM   2844 O O   . LEU A 1 334 ? -55.223 33.071 17.752  1.00 18.35 ? 334 LEU A O   1 
ATOM   2845 C CB  . LEU A 1 334 ? -53.260 32.079 20.152  1.00 15.20 ? 334 LEU A CB  1 
ATOM   2846 C CG  . LEU A 1 334 ? -51.970 31.296 20.380  1.00 14.11 ? 334 LEU A CG  1 
ATOM   2847 C CD1 . LEU A 1 334 ? -52.178 30.305 21.512  1.00 19.42 ? 334 LEU A CD1 1 
ATOM   2848 C CD2 . LEU A 1 334 ? -51.510 30.577 19.105  1.00 17.92 ? 334 LEU A CD2 1 
ATOM   2849 N N   . LYS A 1 335 ? -55.158 34.551 19.443  1.00 17.73 ? 335 LYS A N   1 
ATOM   2850 C CA  . LYS A 1 335 ? -56.483 35.068 19.109  1.00 20.13 ? 335 LYS A CA  1 
ATOM   2851 C C   . LYS A 1 335 ? -56.483 35.710 17.731  1.00 19.13 ? 335 LYS A C   1 
ATOM   2852 O O   . LYS A 1 335 ? -57.431 35.535 16.949  1.00 22.41 ? 335 LYS A O   1 
ATOM   2853 C CB  . LYS A 1 335 ? -56.943 36.076 20.160  1.00 26.97 ? 335 LYS A CB  1 
ATOM   2854 C CG  . LYS A 1 335 ? -57.003 35.529 21.569  1.00 40.79 ? 335 LYS A CG  1 
ATOM   2855 C CD  . LYS A 1 335 ? -57.837 36.416 22.479  1.00 52.15 ? 335 LYS A CD  1 
ATOM   2856 C CE  . LYS A 1 335 ? -57.108 37.712 22.799  1.00 56.89 ? 335 LYS A CE  1 
ATOM   2857 N NZ  . LYS A 1 335 ? -56.391 37.643 24.108  1.00 56.17 ? 335 LYS A NZ  1 
ATOM   2858 N N   . LYS A 1 336 ? -55.429 36.466 17.418  1.00 24.44 ? 336 LYS A N   1 
ATOM   2859 C CA  . LYS A 1 336 ? -55.348 37.114 16.112  1.00 27.21 ? 336 LYS A CA  1 
ATOM   2860 C C   . LYS A 1 336 ? -55.344 36.084 14.991  1.00 22.53 ? 336 LYS A C   1 
ATOM   2861 O O   . LYS A 1 336 ? -56.029 36.263 13.973  1.00 23.34 ? 336 LYS A O   1 
ATOM   2862 C CB  . LYS A 1 336 ? -54.101 37.996 16.041  1.00 29.07 ? 336 LYS A CB  1 
ATOM   2863 C CG  . LYS A 1 336 ? -53.837 38.608 14.672  1.00 39.94 ? 336 LYS A CG  1 
ATOM   2864 C CD  . LYS A 1 336 ? -52.360 38.949 14.504  1.00 50.94 ? 336 LYS A CD  1 
ATOM   2865 C CE  . LYS A 1 336 ? -51.986 39.114 13.038  1.00 57.01 ? 336 LYS A CE  1 
ATOM   2866 N NZ  . LYS A 1 336 ? -51.829 40.551 12.667  1.00 59.07 ? 336 LYS A NZ  1 
ATOM   2867 N N   . ILE A 1 337 ? -54.582 34.997 15.159  1.00 20.64 ? 337 ILE A N   1 
ATOM   2868 C CA  . ILE A 1 337 ? -54.577 33.939 14.151  1.00 19.65 ? 337 ILE A CA  1 
ATOM   2869 C C   . ILE A 1 337 ? -55.970 33.337 14.014  1.00 21.10 ? 337 ILE A C   1 
ATOM   2870 O O   . ILE A 1 337 ? -56.508 33.200 12.907  1.00 22.45 ? 337 ILE A O   1 
ATOM   2871 C CB  . ILE A 1 337 ? -53.528 32.866 14.497  1.00 19.11 ? 337 ILE A CB  1 
ATOM   2872 C CG1 . ILE A 1 337 ? -52.122 33.479 14.529  1.00 16.78 ? 337 ILE A CG1 1 
ATOM   2873 C CG2 . ILE A 1 337 ? -53.615 31.723 13.510  1.00 20.61 ? 337 ILE A CG2 1 
ATOM   2874 C CD1 . ILE A 1 337 ? -51.059 32.587 15.223  1.00 17.14 ? 337 ILE A CD1 1 
ATOM   2875 N N   . HIS A 1 338 ? -56.580 32.988 15.150  1.00 19.81 ? 338 HIS A N   1 
ATOM   2876 C CA  . HIS A 1 338 ? -57.920 32.408 15.167  1.00 20.45 ? 338 HIS A CA  1 
ATOM   2877 C C   . HIS A 1 338 ? -58.927 33.289 14.440  1.00 23.93 ? 338 HIS A C   1 
ATOM   2878 O O   . HIS A 1 338 ? -59.753 32.801 13.659  1.00 24.24 ? 338 HIS A O   1 
ATOM   2879 C CB  . HIS A 1 338 ? -58.342 32.199 16.624  1.00 20.95 ? 338 HIS A CB  1 
ATOM   2880 C CG  . HIS A 1 338 ? -59.686 31.563 16.794  1.00 24.14 ? 338 HIS A CG  1 
ATOM   2881 N ND1 . HIS A 1 338 ? -60.706 32.165 17.499  1.00 28.13 ? 338 HIS A ND1 1 
ATOM   2882 C CD2 . HIS A 1 338 ? -60.162 30.358 16.399  1.00 21.84 ? 338 HIS A CD2 1 
ATOM   2883 C CE1 . HIS A 1 338 ? -61.763 31.370 17.505  1.00 29.27 ? 338 HIS A CE1 1 
ATOM   2884 N NE2 . HIS A 1 338 ? -61.455 30.264 16.850  1.00 26.02 ? 338 HIS A NE2 1 
ATOM   2885 N N   . GLU A 1 339 ? -58.890 34.593 14.707  1.00 22.67 ? 339 GLU A N   1 
ATOM   2886 C CA  . GLU A 1 339 ? -59.836 35.510 14.092  1.00 21.65 ? 339 GLU A CA  1 
ATOM   2887 C C   . GLU A 1 339 ? -59.503 35.821 12.642  1.00 21.82 ? 339 GLU A C   1 
ATOM   2888 O O   . GLU A 1 339 ? -60.365 36.349 11.928  1.00 24.52 ? 339 GLU A O   1 
ATOM   2889 C CB  . GLU A 1 339 ? -59.889 36.818 14.882  1.00 25.96 ? 339 GLU A CB  1 
ATOM   2890 C CG  . GLU A 1 339 ? -60.372 36.687 16.315  1.00 31.56 ? 339 GLU A CG  1 
ATOM   2891 C CD  . GLU A 1 339 ? -59.903 37.846 17.176  1.00 44.57 ? 339 GLU A CD  1 
ATOM   2892 O OE1 . GLU A 1 339 ? -60.218 37.868 18.382  1.00 45.26 ? 339 GLU A OE1 1 
ATOM   2893 O OE2 . GLU A 1 339 ? -59.217 38.745 16.645  1.00 49.61 ? 339 GLU A OE2 1 
ATOM   2894 N N   . SER A 1 340 ? -58.295 35.495 12.180  1.00 25.62 ? 340 SER A N   1 
ATOM   2895 C CA  . SER A 1 340 ? -57.859 35.945 10.861  1.00 25.38 ? 340 SER A CA  1 
ATOM   2896 C C   . SER A 1 340 ? -58.354 35.064 9.718   1.00 25.32 ? 340 SER A C   1 
ATOM   2897 O O   . SER A 1 340 ? -58.355 35.516 8.563   1.00 24.20 ? 340 SER A O   1 
ATOM   2898 C CB  . SER A 1 340 ? -56.333 36.021 10.813  1.00 24.00 ? 340 SER A CB  1 
ATOM   2899 O OG  . SER A 1 340 ? -55.770 34.725 10.767  1.00 26.71 ? 340 SER A OG  1 
ATOM   2900 N N   . VAL A 1 341 ? -58.772 33.827 9.992   1.00 23.98 ? 341 VAL A N   1 
ATOM   2901 C CA  . VAL A 1 341 ? -59.215 32.919 8.942   1.00 23.68 ? 341 VAL A CA  1 
ATOM   2902 C C   . VAL A 1 341 ? -60.519 32.244 9.353   1.00 21.91 ? 341 VAL A C   1 
ATOM   2903 O O   . VAL A 1 341 ? -60.850 32.143 10.537  1.00 22.73 ? 341 VAL A O   1 
ATOM   2904 C CB  . VAL A 1 341 ? -58.148 31.863 8.603   1.00 21.75 ? 341 VAL A CB  1 
ATOM   2905 C CG1 . VAL A 1 341 ? -56.894 32.533 8.047   1.00 27.99 ? 341 VAL A CG1 1 
ATOM   2906 C CG2 . VAL A 1 341 ? -57.809 31.032 9.830   1.00 20.79 ? 341 VAL A CG2 1 
ATOM   2907 N N   . ASP A 1 342 ? -61.270 31.792 8.348   1.00 21.09 ? 342 ASP A N   1 
ATOM   2908 C CA  . ASP A 1 342 ? -62.551 31.127 8.561   1.00 23.03 ? 342 ASP A CA  1 
ATOM   2909 C C   . ASP A 1 342 ? -62.430 29.615 8.692   1.00 24.51 ? 342 ASP A C   1 
ATOM   2910 O O   . ASP A 1 342 ? -63.431 28.952 8.976   1.00 28.14 ? 342 ASP A O   1 
ATOM   2911 C CB  . ASP A 1 342 ? -63.528 31.471 7.426   1.00 25.53 ? 342 ASP A CB  1 
ATOM   2912 C CG  . ASP A 1 342 ? -63.423 30.515 6.230   1.00 39.46 ? 342 ASP A CG  1 
ATOM   2913 O OD1 . ASP A 1 342 ? -62.304 30.103 5.855   1.00 48.09 ? 342 ASP A OD1 1 
ATOM   2914 O OD2 . ASP A 1 342 ? -64.483 30.189 5.649   1.00 50.46 ? 342 ASP A OD2 1 
ATOM   2915 N N   . PHE A 1 343 ? -61.237 29.058 8.499   1.00 22.49 ? 343 PHE A N   1 
ATOM   2916 C CA  . PHE A 1 343 ? -60.990 27.639 8.710   1.00 18.67 ? 343 PHE A CA  1 
ATOM   2917 C C   . PHE A 1 343 ? -60.239 27.452 10.021  1.00 20.95 ? 343 PHE A C   1 
ATOM   2918 O O   . PHE A 1 343 ? -59.938 28.411 10.732  1.00 21.92 ? 343 PHE A O   1 
ATOM   2919 C CB  . PHE A 1 343 ? -60.231 27.025 7.522   1.00 19.69 ? 343 PHE A CB  1 
ATOM   2920 C CG  . PHE A 1 343 ? -58.844 27.587 7.300   1.00 20.15 ? 343 PHE A CG  1 
ATOM   2921 C CD1 . PHE A 1 343 ? -58.658 28.726 6.525   1.00 24.22 ? 343 PHE A CD1 1 
ATOM   2922 C CD2 . PHE A 1 343 ? -57.727 26.959 7.829   1.00 19.97 ? 343 PHE A CD2 1 
ATOM   2923 C CE1 . PHE A 1 343 ? -57.391 29.235 6.308   1.00 19.46 ? 343 PHE A CE1 1 
ATOM   2924 C CE2 . PHE A 1 343 ? -56.460 27.464 7.617   1.00 21.12 ? 343 PHE A CE2 1 
ATOM   2925 C CZ  . PHE A 1 343 ? -56.283 28.601 6.858   1.00 21.16 ? 343 PHE A CZ  1 
ATOM   2926 N N   . GLN A 1 344 ? -59.968 26.193 10.356  1.00 19.71 ? 344 GLN A N   1 
ATOM   2927 C CA  . GLN A 1 344 ? -59.275 25.878 11.596  1.00 18.09 ? 344 GLN A CA  1 
ATOM   2928 C C   . GLN A 1 344 ? -57.787 25.756 11.306  1.00 18.18 ? 344 GLN A C   1 
ATOM   2929 O O   . GLN A 1 344 ? -57.370 24.774 10.670  1.00 19.03 ? 344 GLN A O   1 
ATOM   2930 C CB  . GLN A 1 344 ? -59.818 24.594 12.205  1.00 20.77 ? 344 GLN A CB  1 
ATOM   2931 C CG  . GLN A 1 344 ? -61.303 24.709 12.540  1.00 21.38 ? 344 GLN A CG  1 
ATOM   2932 C CD  . GLN A 1 344 ? -61.882 23.494 13.253  1.00 23.60 ? 344 GLN A CD  1 
ATOM   2933 O OE1 . GLN A 1 344 ? -62.456 23.615 14.338  1.00 25.61 ? 344 GLN A OE1 1 
ATOM   2934 N NE2 . GLN A 1 344 ? -61.771 22.326 12.631  1.00 22.79 ? 344 GLN A NE2 1 
ATOM   2935 N N   . PRO A 1 345 ? -56.959 26.706 11.737  1.00 15.93 ? 345 PRO A N   1 
ATOM   2936 C CA  . PRO A 1 345 ? -55.526 26.643 11.438  1.00 15.80 ? 345 PRO A CA  1 
ATOM   2937 C C   . PRO A 1 345 ? -54.812 25.654 12.339  1.00 15.86 ? 345 PRO A C   1 
ATOM   2938 O O   . PRO A 1 345 ? -55.216 25.420 13.480  1.00 15.36 ? 345 PRO A O   1 
ATOM   2939 C CB  . PRO A 1 345 ? -55.039 28.068 11.730  1.00 18.12 ? 345 PRO A CB  1 
ATOM   2940 C CG  . PRO A 1 345 ? -55.977 28.551 12.808  1.00 15.59 ? 345 PRO A CG  1 
ATOM   2941 C CD  . PRO A 1 345 ? -57.330 27.937 12.455  1.00 18.79 ? 345 PRO A CD  1 
ATOM   2942 N N   . VAL A 1 346 ? -53.739 25.078 11.804  1.00 13.75 ? 346 VAL A N   1 
ATOM   2943 C CA  . VAL A 1 346 ? -52.834 24.238 12.580  1.00 12.85 ? 346 VAL A CA  1 
ATOM   2944 C C   . VAL A 1 346 ? -51.571 25.042 12.833  1.00 12.23 ? 346 VAL A C   1 
ATOM   2945 O O   . VAL A 1 346 ? -50.880 25.452 11.892  1.00 14.85 ? 346 VAL A O   1 
ATOM   2946 C CB  . VAL A 1 346 ? -52.514 22.916 11.863  1.00 15.29 ? 346 VAL A CB  1 
ATOM   2947 C CG1 . VAL A 1 346 ? -51.700 22.018 12.789  1.00 15.59 ? 346 VAL A CG1 1 
ATOM   2948 C CG2 . VAL A 1 346 ? -53.823 22.230 11.391  1.00 17.35 ? 346 VAL A CG2 1 
ATOM   2949 N N   . VAL A 1 347 ? -51.255 25.235 14.106  1.00 14.04 ? 347 VAL A N   1 
ATOM   2950 C CA  . VAL A 1 347 ? -50.229 26.175 14.532  1.00 11.55 ? 347 VAL A CA  1 
ATOM   2951 C C   . VAL A 1 347 ? -49.154 25.374 15.259  1.00 11.69 ? 347 VAL A C   1 
ATOM   2952 O O   . VAL A 1 347 ? -49.347 24.977 16.418  1.00 12.70 ? 347 VAL A O   1 
ATOM   2953 C CB  . VAL A 1 347 ? -50.822 27.267 15.429  1.00 13.61 ? 347 VAL A CB  1 
ATOM   2954 C CG1 . VAL A 1 347 ? -49.754 28.233 15.878  1.00 17.55 ? 347 VAL A CG1 1 
ATOM   2955 C CG2 . VAL A 1 347 ? -51.968 27.992 14.695  1.00 15.81 ? 347 VAL A CG2 1 
ATOM   2956 N N   . PHE A 1 348 ? -48.033 25.109 14.573  1.00 12.72 ? 348 PHE A N   1 
ATOM   2957 C CA  . PHE A 1 348 ? -46.911 24.366 15.144  1.00 11.08 ? 348 PHE A CA  1 
ATOM   2958 C C   . PHE A 1 348 ? -45.939 25.311 15.842  1.00 12.71 ? 348 PHE A C   1 
ATOM   2959 O O   . PHE A 1 348 ? -45.440 26.270 15.243  1.00 13.78 ? 348 PHE A O   1 
ATOM   2960 C CB  . PHE A 1 348 ? -46.175 23.569 14.058  1.00 10.63 ? 348 PHE A CB  1 
ATOM   2961 C CG  . PHE A 1 348 ? -46.658 22.153 13.911  1.00 12.28 ? 348 PHE A CG  1 
ATOM   2962 C CD1 . PHE A 1 348 ? -47.920 21.892 13.395  1.00 12.26 ? 348 PHE A CD1 1 
ATOM   2963 C CD2 . PHE A 1 348 ? -45.850 21.083 14.276  1.00 14.42 ? 348 PHE A CD2 1 
ATOM   2964 C CE1 . PHE A 1 348 ? -48.377 20.589 13.259  1.00 13.04 ? 348 PHE A CE1 1 
ATOM   2965 C CE2 . PHE A 1 348 ? -46.303 19.769 14.129  1.00 14.80 ? 348 PHE A CE2 1 
ATOM   2966 C CZ  . PHE A 1 348 ? -47.579 19.530 13.618  1.00 12.89 ? 348 PHE A CZ  1 
ATOM   2967 N N   . VAL A 1 349 ? -45.666 25.024 17.107  1.00 10.60 ? 349 VAL A N   1 
ATOM   2968 C CA  . VAL A 1 349 ? -44.706 25.762 17.911  1.00 10.14 ? 349 VAL A CA  1 
ATOM   2969 C C   . VAL A 1 349 ? -43.580 24.775 18.197  1.00 10.60 ? 349 VAL A C   1 
ATOM   2970 O O   . VAL A 1 349 ? -43.757 23.821 18.969  1.00 12.34 ? 349 VAL A O   1 
ATOM   2971 C CB  . VAL A 1 349 ? -45.350 26.291 19.200  1.00 10.40 ? 349 VAL A CB  1 
ATOM   2972 C CG1 . VAL A 1 349 ? -44.323 27.028 20.029  1.00 11.98 ? 349 VAL A CG1 1 
ATOM   2973 C CG2 . VAL A 1 349 ? -46.517 27.218 18.875  1.00 15.25 ? 349 VAL A CG2 1 
ATOM   2974 N N   . VAL A 1 350 ? -42.446 24.957 17.520  1.00 10.40 ? 350 VAL A N   1 
ATOM   2975 C CA  . VAL A 1 350 ? -41.362 23.974 17.511  1.00 12.37 ? 350 VAL A CA  1 
ATOM   2976 C C   . VAL A 1 350 ? -40.057 24.687 17.833  1.00 11.25 ? 350 VAL A C   1 
ATOM   2977 O O   . VAL A 1 350 ? -39.687 25.638 17.140  1.00 12.34 ? 350 VAL A O   1 
ATOM   2978 C CB  . VAL A 1 350 ? -41.243 23.268 16.151  1.00 11.28 ? 350 VAL A CB  1 
ATOM   2979 C CG1 . VAL A 1 350 ? -40.277 22.095 16.261  1.00 10.99 ? 350 VAL A CG1 1 
ATOM   2980 C CG2 . VAL A 1 350 ? -42.621 22.780 15.659  1.00 12.07 ? 350 VAL A CG2 1 
ATOM   2981 N N   . LEU A 1 351 ? -39.351 24.217 18.859  1.00 10.91 ? 351 LEU A N   1 
ATOM   2982 C CA  . LEU A 1 351 ? -38.072 24.803 19.240  1.00 9.78  ? 351 LEU A CA  1 
ATOM   2983 C C   . LEU A 1 351 ? -37.366 23.811 20.148  1.00 10.45 ? 351 LEU A C   1 
ATOM   2984 O O   . LEU A 1 351 ? -37.929 22.778 20.524  1.00 11.15 ? 351 LEU A O   1 
ATOM   2985 C CB  . LEU A 1 351 ? -38.241 26.169 19.928  1.00 11.91 ? 351 LEU A CB  1 
ATOM   2986 C CG  . LEU A 1 351 ? -39.077 26.264 21.212  1.00 12.24 ? 351 LEU A CG  1 
ATOM   2987 C CD1 . LEU A 1 351 ? -38.544 27.390 22.116  1.00 14.63 ? 351 LEU A CD1 1 
ATOM   2988 C CD2 . LEU A 1 351 ? -40.584 26.446 20.897  1.00 10.55 ? 351 LEU A CD2 1 
ATOM   2989 N N   . ASP A 1 352 ? -36.119 24.131 20.488  1.00 11.53 ? 352 ASP A N   1 
ATOM   2990 C CA  . ASP A 1 352 ? -35.419 23.321 21.479  1.00 11.69 ? 352 ASP A CA  1 
ATOM   2991 C C   . ASP A 1 352 ? -36.248 23.251 22.757  1.00 11.63 ? 352 ASP A C   1 
ATOM   2992 O O   . ASP A 1 352 ? -36.852 24.241 23.180  1.00 12.98 ? 352 ASP A O   1 
ATOM   2993 C CB  . ASP A 1 352 ? -34.053 23.914 21.817  1.00 11.64 ? 352 ASP A CB  1 
ATOM   2994 C CG  . ASP A 1 352 ? -33.065 23.882 20.660  1.00 10.97 ? 352 ASP A CG  1 
ATOM   2995 O OD1 . ASP A 1 352 ? -33.385 23.368 19.564  1.00 13.98 ? 352 ASP A OD1 1 
ATOM   2996 O OD2 . ASP A 1 352 ? -31.948 24.404 20.885  1.00 11.89 ? 352 ASP A OD2 1 
ATOM   2997 N N   . GLY A 1 353 ? -36.259 22.080 23.394  1.00 11.01 ? 353 GLY A N   1 
ATOM   2998 C CA  . GLY A 1 353 ? -37.089 21.928 24.574  1.00 9.55  ? 353 GLY A CA  1 
ATOM   2999 C C   . GLY A 1 353 ? -36.374 22.137 25.899  1.00 12.06 ? 353 GLY A C   1 
ATOM   3000 O O   . GLY A 1 353 ? -37.018 22.113 26.957  1.00 11.59 ? 353 GLY A O   1 
ATOM   3001 N N   . GLU A 1 354 ? -35.056 22.333 25.864  1.00 11.41 ? 354 GLU A N   1 
ATOM   3002 C CA  . GLU A 1 354 ? -34.289 22.407 27.111  1.00 11.82 ? 354 GLU A CA  1 
ATOM   3003 C C   . GLU A 1 354 ? -33.372 23.607 27.242  1.00 12.68 ? 354 GLU A C   1 
ATOM   3004 O O   . GLU A 1 354 ? -32.733 23.750 28.293  1.00 16.98 ? 354 GLU A O   1 
ATOM   3005 C CB  . GLU A 1 354 ? -33.428 21.143 27.305  1.00 12.44 ? 354 GLU A CB  1 
ATOM   3006 C CG  . GLU A 1 354 ? -32.132 21.080 26.475  1.00 12.76 ? 354 GLU A CG  1 
ATOM   3007 C CD  . GLU A 1 354 ? -32.377 20.647 25.041  1.00 11.07 ? 354 GLU A CD  1 
ATOM   3008 O OE1 . GLU A 1 354 ? -31.963 19.522 24.657  1.00 12.80 ? 354 GLU A OE1 1 
ATOM   3009 O OE2 . GLU A 1 354 ? -32.973 21.451 24.310  1.00 12.03 ? 354 GLU A OE2 1 
ATOM   3010 N N   . ASN A 1 355 ? -33.244 24.449 26.225  1.00 11.76 ? 355 ASN A N   1 
ATOM   3011 C CA  . ASN A 1 355 ? -32.212 25.470 26.254  1.00 10.61 ? 355 ASN A CA  1 
ATOM   3012 C C   . ASN A 1 355 ? -32.709 26.864 26.610  1.00 11.94 ? 355 ASN A C   1 
ATOM   3013 O O   . ASN A 1 355 ? -31.900 27.700 27.016  1.00 13.30 ? 355 ASN A O   1 
ATOM   3014 C CB  . ASN A 1 355 ? -31.494 25.494 24.904  1.00 11.73 ? 355 ASN A CB  1 
ATOM   3015 C CG  . ASN A 1 355 ? -30.713 24.229 24.669  1.00 14.37 ? 355 ASN A CG  1 
ATOM   3016 O OD1 . ASN A 1 355 ? -30.037 23.741 25.580  1.00 13.06 ? 355 ASN A OD1 1 
ATOM   3017 N ND2 . ASN A 1 355 ? -30.784 23.688 23.456  1.00 13.17 ? 355 ASN A ND2 1 
ATOM   3018 N N   . CYS A 1 356 ? -34.004 27.149 26.482  1.00 12.99 ? 356 CYS A N   1 
ATOM   3019 C CA  . CYS A 1 356 ? -34.428 28.513 26.755  1.00 13.92 ? 356 CYS A CA  1 
ATOM   3020 C C   . CYS A 1 356 ? -34.707 28.786 28.230  1.00 11.76 ? 356 CYS A C   1 
ATOM   3021 O O   . CYS A 1 356 ? -34.603 29.942 28.656  1.00 13.36 ? 356 CYS A O   1 
ATOM   3022 C CB  . CYS A 1 356 ? -35.667 28.859 25.923  1.00 15.05 ? 356 CYS A CB  1 
ATOM   3023 S SG  . CYS A 1 356 ? -37.059 27.781 26.130  1.00 15.26 ? 356 CYS A SG  1 
ATOM   3024 N N   . TRP A 1 357 ? -34.985 27.750 29.030  1.00 12.07 ? 357 TRP A N   1 
ATOM   3025 C CA  . TRP A 1 357 ? -35.570 27.971 30.353  1.00 13.36 ? 357 TRP A CA  1 
ATOM   3026 C C   . TRP A 1 357 ? -34.568 28.547 31.342  1.00 11.93 ? 357 TRP A C   1 
ATOM   3027 O O   . TRP A 1 357 ? -34.970 29.262 32.263  1.00 13.69 ? 357 TRP A O   1 
ATOM   3028 C CB  . TRP A 1 357 ? -36.167 26.665 30.897  1.00 13.27 ? 357 TRP A CB  1 
ATOM   3029 C CG  . TRP A 1 357 ? -37.014 26.017 29.851  1.00 10.73 ? 357 TRP A CG  1 
ATOM   3030 C CD1 . TRP A 1 357 ? -36.816 24.789 29.265  1.00 12.97 ? 357 TRP A CD1 1 
ATOM   3031 C CD2 . TRP A 1 357 ? -38.172 26.578 29.222  1.00 12.66 ? 357 TRP A CD2 1 
ATOM   3032 N NE1 . TRP A 1 357 ? -37.785 24.556 28.314  1.00 12.06 ? 357 TRP A NE1 1 
ATOM   3033 C CE2 . TRP A 1 357 ? -38.617 25.644 28.261  1.00 11.98 ? 357 TRP A CE2 1 
ATOM   3034 C CE3 . TRP A 1 357 ? -38.864 27.797 29.357  1.00 13.65 ? 357 TRP A CE3 1 
ATOM   3035 C CZ2 . TRP A 1 357 ? -39.730 25.868 27.472  1.00 11.75 ? 357 TRP A CZ2 1 
ATOM   3036 C CZ3 . TRP A 1 357 ? -39.973 28.022 28.551  1.00 13.95 ? 357 TRP A CZ3 1 
ATOM   3037 C CH2 . TRP A 1 357 ? -40.390 27.064 27.624  1.00 12.55 ? 357 TRP A CH2 1 
ATOM   3038 N N   . GLU A 1 358 ? -33.278 28.250 31.167  1.00 14.24 ? 358 GLU A N   1 
ATOM   3039 C CA  . GLU A 1 358 ? -32.267 28.736 32.105  1.00 12.85 ? 358 GLU A CA  1 
ATOM   3040 C C   . GLU A 1 358 ? -32.172 30.258 32.115  1.00 13.25 ? 358 GLU A C   1 
ATOM   3041 O O   . GLU A 1 358 ? -31.629 30.840 33.069  1.00 15.26 ? 358 GLU A O   1 
ATOM   3042 C CB  . GLU A 1 358 ? -30.911 28.105 31.761  1.00 14.51 ? 358 GLU A CB  1 
ATOM   3043 C CG  . GLU A 1 358 ? -30.394 28.457 30.376  1.00 15.03 ? 358 GLU A CG  1 
ATOM   3044 C CD  . GLU A 1 358 ? -29.421 27.415 29.831  1.00 15.67 ? 358 GLU A CD  1 
ATOM   3045 O OE1 . GLU A 1 358 ? -28.221 27.732 29.699  1.00 19.93 ? 358 GLU A OE1 1 
ATOM   3046 O OE2 . GLU A 1 358 ? -29.853 26.277 29.560  1.00 15.25 ? 358 GLU A OE2 1 
ATOM   3047 N N   . TYR A 1 359 ? -32.693 30.916 31.076  1.00 14.59 ? 359 TYR A N   1 
ATOM   3048 C CA  . TYR A 1 359 ? -32.689 32.368 30.983  1.00 13.41 ? 359 TYR A CA  1 
ATOM   3049 C C   . TYR A 1 359 ? -33.953 33.007 31.547  1.00 14.51 ? 359 TYR A C   1 
ATOM   3050 O O   . TYR A 1 359 ? -34.008 34.236 31.656  1.00 15.71 ? 359 TYR A O   1 
ATOM   3051 C CB  . TYR A 1 359 ? -32.511 32.799 29.525  1.00 16.64 ? 359 TYR A CB  1 
ATOM   3052 C CG  . TYR A 1 359 ? -31.274 32.221 28.865  1.00 15.77 ? 359 TYR A CG  1 
ATOM   3053 C CD1 . TYR A 1 359 ? -30.030 32.839 29.010  1.00 21.12 ? 359 TYR A CD1 1 
ATOM   3054 C CD2 . TYR A 1 359 ? -31.344 31.052 28.119  1.00 15.85 ? 359 TYR A CD2 1 
ATOM   3055 C CE1 . TYR A 1 359 ? -28.892 32.306 28.404  1.00 20.10 ? 359 TYR A CE1 1 
ATOM   3056 C CE2 . TYR A 1 359 ? -30.214 30.516 27.521  1.00 21.92 ? 359 TYR A CE2 1 
ATOM   3057 C CZ  . TYR A 1 359 ? -28.996 31.144 27.675  1.00 21.92 ? 359 TYR A CZ  1 
ATOM   3058 O OH  . TYR A 1 359 ? -27.881 30.609 27.074  1.00 27.50 ? 359 TYR A OH  1 
ATOM   3059 N N   . TYR A 1 360 ? -34.950 32.209 31.910  1.00 15.49 ? 360 TYR A N   1 
ATOM   3060 C CA  . TYR A 1 360 ? -36.172 32.705 32.531  1.00 13.82 ? 360 TYR A CA  1 
ATOM   3061 C C   . TYR A 1 360 ? -36.028 32.726 34.046  1.00 18.72 ? 360 TYR A C   1 
ATOM   3062 O O   . TYR A 1 360 ? -35.319 31.905 34.636  1.00 17.82 ? 360 TYR A O   1 
ATOM   3063 C CB  . TYR A 1 360 ? -37.370 31.811 32.204  1.00 14.86 ? 360 TYR A CB  1 
ATOM   3064 C CG  . TYR A 1 360 ? -37.990 31.864 30.819  1.00 13.58 ? 360 TYR A CG  1 
ATOM   3065 C CD1 . TYR A 1 360 ? -37.291 31.444 29.690  1.00 12.53 ? 360 TYR A CD1 1 
ATOM   3066 C CD2 . TYR A 1 360 ? -39.311 32.261 30.656  1.00 14.97 ? 360 TYR A CD2 1 
ATOM   3067 C CE1 . TYR A 1 360 ? -37.880 31.464 28.429  1.00 14.09 ? 360 TYR A CE1 1 
ATOM   3068 C CE2 . TYR A 1 360 ? -39.900 32.282 29.405  1.00 14.28 ? 360 TYR A CE2 1 
ATOM   3069 C CZ  . TYR A 1 360 ? -39.182 31.880 28.299  1.00 14.96 ? 360 TYR A CZ  1 
ATOM   3070 O OH  . TYR A 1 360 ? -39.773 31.876 27.047  1.00 14.69 ? 360 TYR A OH  1 
ATOM   3071 N N   . GLU A 1 361 ? -36.738 33.661 34.674  1.00 19.13 ? 361 GLU A N   1 
ATOM   3072 C CA  . GLU A 1 361 ? -36.956 33.613 36.113  1.00 21.43 ? 361 GLU A CA  1 
ATOM   3073 C C   . GLU A 1 361 ? -37.438 32.230 36.538  1.00 18.16 ? 361 GLU A C   1 
ATOM   3074 O O   . GLU A 1 361 ? -38.350 31.661 35.929  1.00 17.02 ? 361 GLU A O   1 
ATOM   3075 C CB  . GLU A 1 361 ? -37.985 34.681 36.502  1.00 25.78 ? 361 GLU A CB  1 
ATOM   3076 C CG  . GLU A 1 361 ? -38.295 34.771 37.975  1.00 40.80 ? 361 GLU A CG  1 
ATOM   3077 C CD  . GLU A 1 361 ? -37.270 35.590 38.725  1.00 55.74 ? 361 GLU A CD  1 
ATOM   3078 O OE1 . GLU A 1 361 ? -36.350 36.132 38.073  1.00 53.86 ? 361 GLU A OE1 1 
ATOM   3079 O OE2 . GLU A 1 361 ? -37.389 35.699 39.965  1.00 66.61 ? 361 GLU A OE2 1 
ATOM   3080 N N   . GLU A 1 362 ? -36.790 31.672 37.558  1.00 17.64 ? 362 GLU A N   1 
ATOM   3081 C CA  . GLU A 1 362 ? -37.216 30.406 38.161  1.00 16.95 ? 362 GLU A CA  1 
ATOM   3082 C C   . GLU A 1 362 ? -37.339 29.301 37.109  1.00 18.51 ? 362 GLU A C   1 
ATOM   3083 O O   . GLU A 1 362 ? -38.256 28.473 37.139  1.00 15.91 ? 362 GLU A O   1 
ATOM   3084 C CB  . GLU A 1 362 ? -38.528 30.590 38.930  1.00 20.43 ? 362 GLU A CB  1 
ATOM   3085 C CG  . GLU A 1 362 ? -38.857 29.491 39.924  1.00 30.77 ? 362 GLU A CG  1 
ATOM   3086 C CD  . GLU A 1 362 ? -40.164 29.753 40.654  1.00 46.31 ? 362 GLU A CD  1 
ATOM   3087 O OE1 . GLU A 1 362 ? -40.326 30.871 41.191  1.00 39.09 ? 362 GLU A OE1 1 
ATOM   3088 O OE2 . GLU A 1 362 ? -41.033 28.847 40.673  1.00 48.13 ? 362 GLU A OE2 1 
ATOM   3089 N N   . ASN A 1 363 ? -36.402 29.295 36.155  1.00 14.38 ? 363 ASN A N   1 
ATOM   3090 C CA  . ASN A 1 363 ? -36.272 28.209 35.178  1.00 13.29 ? 363 ASN A CA  1 
ATOM   3091 C C   . ASN A 1 363 ? -37.514 28.076 34.299  1.00 15.97 ? 363 ASN A C   1 
ATOM   3092 O O   . ASN A 1 363 ? -37.849 26.984 33.827  1.00 15.26 ? 363 ASN A O   1 
ATOM   3093 C CB  . ASN A 1 363 ? -35.963 26.879 35.867  1.00 14.55 ? 363 ASN A CB  1 
ATOM   3094 C CG  . ASN A 1 363 ? -35.489 25.844 34.896  1.00 16.20 ? 363 ASN A CG  1 
ATOM   3095 O OD1 . ASN A 1 363 ? -34.737 26.159 33.966  1.00 13.94 ? 363 ASN A OD1 1 
ATOM   3096 N ND2 . ASN A 1 363 ? -35.920 24.604 35.089  1.00 21.14 ? 363 ASN A ND2 1 
ATOM   3097 N N   . GLY A 1 364 ? -38.208 29.192 34.098  1.00 13.80 ? 364 GLY A N   1 
ATOM   3098 C CA  . GLY A 1 364 ? -39.386 29.228 33.246  1.00 14.75 ? 364 GLY A CA  1 
ATOM   3099 C C   . GLY A 1 364 ? -40.613 28.563 33.815  1.00 17.50 ? 364 GLY A C   1 
ATOM   3100 O O   . GLY A 1 364 ? -41.606 28.411 33.096  1.00 14.78 ? 364 GLY A O   1 
ATOM   3101 N N   . ILE A 1 365 ? -40.588 28.190 35.088  1.00 14.93 ? 365 ILE A N   1 
ATOM   3102 C CA  . ILE A 1 365 ? -41.685 27.456 35.712  1.00 13.58 ? 365 ILE A CA  1 
ATOM   3103 C C   . ILE A 1 365 ? -42.889 28.382 35.884  1.00 17.75 ? 365 ILE A C   1 
ATOM   3104 O O   . ILE A 1 365 ? -44.005 27.996 35.507  1.00 17.37 ? 365 ILE A O   1 
ATOM   3105 C CB  . ILE A 1 365 ? -41.221 26.812 37.030  1.00 14.43 ? 365 ILE A CB  1 
ATOM   3106 C CG1 . ILE A 1 365 ? -40.172 25.745 36.707  1.00 15.19 ? 365 ILE A CG1 1 
ATOM   3107 C CG2 . ILE A 1 365 ? -42.390 26.200 37.781  1.00 20.13 ? 365 ILE A CG2 1 
ATOM   3108 C CD1 . ILE A 1 365 ? -39.426 25.267 37.941  1.00 15.44 ? 365 ILE A CD1 1 
ATOM   3109 N N   . PRO A 1 366 ? -42.740 29.612 36.396  1.00 15.29 ? 366 PRO A N   1 
ATOM   3110 C CA  . PRO A 1 366 ? -43.911 30.503 36.395  1.00 18.41 ? 366 PRO A CA  1 
ATOM   3111 C C   . PRO A 1 366 ? -44.485 30.714 35.003  1.00 17.39 ? 366 PRO A C   1 
ATOM   3112 O O   . PRO A 1 366 ? -45.712 30.730 34.842  1.00 18.25 ? 366 PRO A O   1 
ATOM   3113 C CB  . PRO A 1 366 ? -43.369 31.799 37.014  1.00 19.49 ? 366 PRO A CB  1 
ATOM   3114 C CG  . PRO A 1 366 ? -42.246 31.324 37.912  1.00 18.94 ? 366 PRO A CG  1 
ATOM   3115 C CD  . PRO A 1 366 ? -41.605 30.206 37.139  1.00 16.06 ? 366 PRO A CD  1 
ATOM   3116 N N   . PHE A 1 367 ? -43.633 30.838 33.978  1.00 16.25 ? 367 PHE A N   1 
ATOM   3117 C CA  . PHE A 1 367 ? -44.150 31.042 32.630  1.00 16.72 ? 367 PHE A CA  1 
ATOM   3118 C C   . PHE A 1 367 ? -44.914 29.815 32.140  1.00 15.88 ? 367 PHE A C   1 
ATOM   3119 O O   . PHE A 1 367 ? -46.055 29.930 31.674  1.00 16.09 ? 367 PHE A O   1 
ATOM   3120 C CB  . PHE A 1 367 ? -43.015 31.376 31.662  1.00 14.58 ? 367 PHE A CB  1 
ATOM   3121 C CG  . PHE A 1 367 ? -43.437 31.344 30.218  1.00 14.62 ? 367 PHE A CG  1 
ATOM   3122 C CD1 . PHE A 1 367 ? -44.211 32.375 29.689  1.00 17.79 ? 367 PHE A CD1 1 
ATOM   3123 C CD2 . PHE A 1 367 ? -43.084 30.277 29.403  1.00 14.34 ? 367 PHE A CD2 1 
ATOM   3124 C CE1 . PHE A 1 367 ? -44.615 32.354 28.358  1.00 13.75 ? 367 PHE A CE1 1 
ATOM   3125 C CE2 . PHE A 1 367 ? -43.491 30.239 28.071  1.00 14.58 ? 367 PHE A CE2 1 
ATOM   3126 C CZ  . PHE A 1 367 ? -44.256 31.280 27.548  1.00 14.13 ? 367 PHE A CZ  1 
ATOM   3127 N N   . LEU A 1 368 ? -44.309 28.633 32.226  1.00 13.31 ? 368 LEU A N   1 
ATOM   3128 C CA  . LEU A 1 368 ? -44.957 27.456 31.647  1.00 12.19 ? 368 LEU A CA  1 
ATOM   3129 C C   . LEU A 1 368 ? -46.202 27.068 32.432  1.00 14.75 ? 368 LEU A C   1 
ATOM   3130 O O   . LEU A 1 368 ? -47.208 26.667 31.839  1.00 17.19 ? 368 LEU A O   1 
ATOM   3131 C CB  . LEU A 1 368 ? -43.982 26.279 31.583  1.00 13.89 ? 368 LEU A CB  1 
ATOM   3132 C CG  . LEU A 1 368 ? -42.990 26.343 30.417  1.00 12.74 ? 368 LEU A CG  1 
ATOM   3133 C CD1 . LEU A 1 368 ? -42.060 25.135 30.433  1.00 16.60 ? 368 LEU A CD1 1 
ATOM   3134 C CD2 . LEU A 1 368 ? -43.724 26.438 29.068  1.00 12.61 ? 368 LEU A CD2 1 
ATOM   3135 N N   . GLU A 1 369 ? -46.155 27.149 33.766  1.00 15.86 ? 369 GLU A N   1 
ATOM   3136 C CA  . GLU A 1 369 ? -47.358 26.855 34.541  1.00 17.46 ? 369 GLU A CA  1 
ATOM   3137 C C   . GLU A 1 369 ? -48.490 27.797 34.160  1.00 20.37 ? 369 GLU A C   1 
ATOM   3138 O O   . GLU A 1 369 ? -49.632 27.363 33.951  1.00 18.97 ? 369 GLU A O   1 
ATOM   3139 C CB  . GLU A 1 369 ? -47.063 26.925 36.039  1.00 16.45 ? 369 GLU A CB  1 
ATOM   3140 C CG  . GLU A 1 369 ? -46.171 25.777 36.499  1.00 16.14 ? 369 GLU A CG  1 
ATOM   3141 C CD  . GLU A 1 369 ? -45.950 25.719 37.993  1.00 21.64 ? 369 GLU A CD  1 
ATOM   3142 O OE1 . GLU A 1 369 ? -46.275 26.693 38.714  1.00 22.71 ? 369 GLU A OE1 1 
ATOM   3143 O OE2 . GLU A 1 369 ? -45.434 24.671 38.453  1.00 21.75 ? 369 GLU A OE2 1 
ATOM   3144 N N   . LYS A 1 370 ? -48.190 29.092 34.032  1.00 17.64 ? 370 LYS A N   1 
ATOM   3145 C CA  . LYS A 1 370 ? -49.231 30.033 33.642  1.00 17.57 ? 370 LYS A CA  1 
ATOM   3146 C C   . LYS A 1 370 ? -49.670 29.794 32.200  1.00 16.78 ? 370 LYS A C   1 
ATOM   3147 O O   . LYS A 1 370 ? -50.867 29.835 31.897  1.00 17.07 ? 370 LYS A O   1 
ATOM   3148 C CB  . LYS A 1 370 ? -48.747 31.464 33.836  1.00 20.07 ? 370 LYS A CB  1 
ATOM   3149 C CG  . LYS A 1 370 ? -49.823 32.507 33.557  1.00 32.67 ? 370 LYS A CG  1 
ATOM   3150 C CD  . LYS A 1 370 ? -49.285 33.917 33.714  1.00 42.61 ? 370 LYS A CD  1 
ATOM   3151 C CE  . LYS A 1 370 ? -49.209 34.337 35.178  1.00 49.55 ? 370 LYS A CE  1 
ATOM   3152 N NZ  . LYS A 1 370 ? -50.354 33.819 35.975  1.00 50.57 ? 370 LYS A NZ  1 
ATOM   3153 N N   . LEU A 1 371 ? -48.723 29.503 31.302  1.00 15.34 ? 371 LEU A N   1 
ATOM   3154 C CA  . LEU A 1 371 ? -49.098 29.275 29.909  1.00 14.48 ? 371 LEU A CA  1 
ATOM   3155 C C   . LEU A 1 371 ? -50.007 28.061 29.782  1.00 14.76 ? 371 LEU A C   1 
ATOM   3156 O O   . LEU A 1 371 ? -51.081 28.136 29.173  1.00 15.97 ? 371 LEU A O   1 
ATOM   3157 C CB  . LEU A 1 371 ? -47.847 29.097 29.052  1.00 16.71 ? 371 LEU A CB  1 
ATOM   3158 C CG  . LEU A 1 371 ? -48.124 28.736 27.586  1.00 17.77 ? 371 LEU A CG  1 
ATOM   3159 C CD1 . LEU A 1 371 ? -48.752 29.917 26.853  1.00 18.66 ? 371 LEU A CD1 1 
ATOM   3160 C CD2 . LEU A 1 371 ? -46.839 28.307 26.890  1.00 16.14 ? 371 LEU A CD2 1 
ATOM   3161 N N   . TYR A 1 372 ? -49.609 26.939 30.387  1.00 15.57 ? 372 TYR A N   1 
ATOM   3162 C CA  . TYR A 1 372 ? -50.382 25.710 30.251  1.00 16.33 ? 372 TYR A CA  1 
ATOM   3163 C C   . TYR A 1 372 ? -51.724 25.829 30.963  1.00 17.53 ? 372 TYR A C   1 
ATOM   3164 O O   . TYR A 1 372 ? -52.750 25.354 30.455  1.00 19.80 ? 372 TYR A O   1 
ATOM   3165 C CB  . TYR A 1 372 ? -49.578 24.532 30.797  1.00 13.42 ? 372 TYR A CB  1 
ATOM   3166 C CG  . TYR A 1 372 ? -48.346 24.158 29.985  1.00 14.48 ? 372 TYR A CG  1 
ATOM   3167 C CD1 . TYR A 1 372 ? -48.178 24.592 28.680  1.00 12.41 ? 372 TYR A CD1 1 
ATOM   3168 C CD2 . TYR A 1 372 ? -47.339 23.366 30.551  1.00 12.82 ? 372 TYR A CD2 1 
ATOM   3169 C CE1 . TYR A 1 372 ? -47.049 24.225 27.926  1.00 10.82 ? 372 TYR A CE1 1 
ATOM   3170 C CE2 . TYR A 1 372 ? -46.205 23.000 29.820  1.00 13.20 ? 372 TYR A CE2 1 
ATOM   3171 C CZ  . TYR A 1 372 ? -46.065 23.428 28.517  1.00 11.32 ? 372 TYR A CZ  1 
ATOM   3172 O OH  . TYR A 1 372 ? -44.952 23.050 27.811  1.00 14.17 ? 372 TYR A OH  1 
ATOM   3173 N N   . SER A 1 373 ? -51.742 26.484 32.123  1.00 15.64 ? 373 SER A N   1 
ATOM   3174 C CA  . SER A 1 373 ? -53.011 26.712 32.812  1.00 19.95 ? 373 SER A CA  1 
ATOM   3175 C C   . SER A 1 373 ? -53.942 27.567 31.961  1.00 19.89 ? 373 SER A C   1 
ATOM   3176 O O   . SER A 1 373 ? -55.143 27.285 31.856  1.00 22.07 ? 373 SER A O   1 
ATOM   3177 C CB  . SER A 1 373 ? -52.771 27.380 34.161  1.00 22.71 ? 373 SER A CB  1 
ATOM   3178 O OG  . SER A 1 373 ? -54.001 27.634 34.823  1.00 24.84 ? 373 SER A OG  1 
ATOM   3179 N N   . THR A 1 374 ? -53.399 28.610 31.331  1.00 19.70 ? 374 THR A N   1 
ATOM   3180 C CA  . THR A 1 374 ? -54.238 29.491 30.530  1.00 20.34 ? 374 THR A CA  1 
ATOM   3181 C C   . THR A 1 374 ? -54.721 28.794 29.264  1.00 20.57 ? 374 THR A C   1 
ATOM   3182 O O   . THR A 1 374 ? -55.886 28.945 28.880  1.00 20.68 ? 374 THR A O   1 
ATOM   3183 C CB  . THR A 1 374 ? -53.478 30.774 30.194  1.00 20.76 ? 374 THR A CB  1 
ATOM   3184 O OG1 . THR A 1 374 ? -53.067 31.411 31.412  1.00 21.32 ? 374 THR A OG1 1 
ATOM   3185 C CG2 . THR A 1 374 ? -54.366 31.732 29.372  1.00 21.21 ? 374 THR A CG2 1 
ATOM   3186 N N   . LEU A 1 375 ? -53.853 28.008 28.615  1.00 18.89 ? 375 LEU A N   1 
ATOM   3187 C CA  . LEU A 1 375 ? -54.261 27.333 27.383  1.00 17.71 ? 375 LEU A CA  1 
ATOM   3188 C C   . LEU A 1 375 ? -55.397 26.352 27.633  1.00 22.05 ? 375 LEU A C   1 
ATOM   3189 O O   . LEU A 1 375 ? -56.349 26.279 26.844  1.00 21.28 ? 375 LEU A O   1 
ATOM   3190 C CB  . LEU A 1 375 ? -53.074 26.600 26.760  1.00 19.48 ? 375 LEU A CB  1 
ATOM   3191 C CG  . LEU A 1 375 ? -51.994 27.451 26.106  1.00 19.82 ? 375 LEU A CG  1 
ATOM   3192 C CD1 . LEU A 1 375 ? -50.844 26.561 25.678  1.00 19.46 ? 375 LEU A CD1 1 
ATOM   3193 C CD2 . LEU A 1 375 ? -52.560 28.194 24.918  1.00 19.24 ? 375 LEU A CD2 1 
ATOM   3194 N N   . GLU A 1 376 ? -55.314 25.582 28.719  1.00 21.12 ? 376 GLU A N   1 
ATOM   3195 C CA  . GLU A 1 376 ? -56.333 24.579 28.988  1.00 23.48 ? 376 GLU A CA  1 
ATOM   3196 C C   . GLU A 1 376 ? -57.682 25.186 29.363  1.00 25.76 ? 376 GLU A C   1 
ATOM   3197 O O   . GLU A 1 376 ? -58.660 24.441 29.475  1.00 31.64 ? 376 GLU A O   1 
ATOM   3198 C CB  . GLU A 1 376 ? -55.845 23.631 30.089  1.00 21.22 ? 376 GLU A CB  1 
ATOM   3199 C CG  . GLU A 1 376 ? -55.927 24.218 31.495  1.00 25.30 ? 376 GLU A CG  1 
ATOM   3200 C CD  . GLU A 1 376 ? -55.243 23.350 32.549  1.00 31.06 ? 376 GLU A CD  1 
ATOM   3201 O OE1 . GLU A 1 376 ? -54.816 22.220 32.224  1.00 32.98 ? 376 GLU A OE1 1 
ATOM   3202 O OE2 . GLU A 1 376 ? -55.120 23.811 33.701  1.00 26.22 ? 376 GLU A OE2 1 
ATOM   3203 N N   . LYS A 1 377 ? -57.765 26.509 29.540  1.00 20.71 ? 377 LYS A N   1 
ATOM   3204 C CA  . LYS A 1 377 ? -58.997 27.203 29.904  1.00 24.13 ? 377 LYS A CA  1 
ATOM   3205 C C   . LYS A 1 377 ? -59.541 28.046 28.759  1.00 24.92 ? 377 LYS A C   1 
ATOM   3206 O O   . LYS A 1 377 ? -60.450 28.861 28.976  1.00 29.26 ? 377 LYS A O   1 
ATOM   3207 C CB  . LYS A 1 377 ? -58.767 28.080 31.138  1.00 25.21 ? 377 LYS A CB  1 
ATOM   3208 C CG  . LYS A 1 377 ? -58.372 27.300 32.400  1.00 25.53 ? 377 LYS A CG  1 
ATOM   3209 C CD  . LYS A 1 377 ? -57.790 28.196 33.491  1.00 30.31 ? 377 LYS A CD  1 
ATOM   3210 C CE  . LYS A 1 377 ? -57.566 27.422 34.790  1.00 29.98 ? 377 LYS A CE  1 
ATOM   3211 N NZ  . LYS A 1 377 ? -56.615 26.278 34.607  1.00 30.19 ? 377 LYS A NZ  1 
ATOM   3212 N N   . GLU A 1 378 ? -58.985 27.894 27.553  1.00 21.75 ? 378 GLU A N   1 
ATOM   3213 C CA  . GLU A 1 378 ? -59.495 28.557 26.353  1.00 23.75 ? 378 GLU A CA  1 
ATOM   3214 C C   . GLU A 1 378 ? -60.224 27.516 25.515  1.00 22.09 ? 378 GLU A C   1 
ATOM   3215 O O   . GLU A 1 378 ? -59.589 26.620 24.939  1.00 23.37 ? 378 GLU A O   1 
ATOM   3216 C CB  . GLU A 1 378 ? -58.384 29.217 25.541  1.00 26.09 ? 378 GLU A CB  1 
ATOM   3217 C CG  . GLU A 1 378 ? -57.620 30.288 26.293  1.00 26.69 ? 378 GLU A CG  1 
ATOM   3218 C CD  . GLU A 1 378 ? -58.465 31.503 26.608  1.00 44.66 ? 378 GLU A CD  1 
ATOM   3219 O OE1 . GLU A 1 378 ? -59.437 31.767 25.870  1.00 52.70 ? 378 GLU A OE1 1 
ATOM   3220 O OE2 . GLU A 1 378 ? -58.155 32.200 27.597  1.00 55.15 ? 378 GLU A OE2 1 
ATOM   3221 N N   . GLU A 1 379 ? -61.559 27.670 25.420  1.00 25.84 ? 379 GLU A N   1 
ATOM   3222 C CA  . GLU A 1 379 ? -62.376 26.687 24.696  1.00 32.21 ? 379 GLU A CA  1 
ATOM   3223 C C   . GLU A 1 379 ? -62.012 26.603 23.241  1.00 29.10 ? 379 GLU A C   1 
ATOM   3224 O O   . GLU A 1 379 ? -62.243 25.566 22.615  1.00 30.86 ? 379 GLU A O   1 
ATOM   3225 C CB  . GLU A 1 379 ? -63.851 27.018 24.726  1.00 37.62 ? 379 GLU A CB  1 
ATOM   3226 C CG  . GLU A 1 379 ? -64.012 28.483 24.803  1.00 52.16 ? 379 GLU A CG  1 
ATOM   3227 C CD  . GLU A 1 379 ? -65.424 28.648 25.074  1.00 70.80 ? 379 GLU A CD  1 
ATOM   3228 O OE1 . GLU A 1 379 ? -65.754 28.174 26.153  1.00 74.54 ? 379 GLU A OE1 1 
ATOM   3229 O OE2 . GLU A 1 379 ? -66.154 29.349 24.318  1.00 71.45 ? 379 GLU A OE2 1 
ATOM   3230 N N   . TRP A 1 380 ? -61.593 27.712 22.655  1.00 24.48 ? 380 TRP A N   1 
ATOM   3231 C CA  . TRP A 1 380 ? -61.376 27.771 21.225  1.00 22.06 ? 380 TRP A CA  1 
ATOM   3232 C C   . TRP A 1 380 ? -59.995 27.270 20.835  1.00 22.10 ? 380 TRP A C   1 
ATOM   3233 O O   . TRP A 1 380 ? -59.704 27.197 19.638  1.00 22.87 ? 380 TRP A O   1 
ATOM   3234 C CB  . TRP A 1 380 ? -61.592 29.208 20.732  1.00 24.38 ? 380 TRP A CB  1 
ATOM   3235 C CG  . TRP A 1 380 ? -60.793 30.198 21.511  1.00 24.32 ? 380 TRP A CG  1 
ATOM   3236 C CD1 . TRP A 1 380 ? -61.137 30.786 22.699  1.00 27.89 ? 380 TRP A CD1 1 
ATOM   3237 C CD2 . TRP A 1 380 ? -59.503 30.706 21.169  1.00 21.97 ? 380 TRP A CD2 1 
ATOM   3238 N NE1 . TRP A 1 380 ? -60.133 31.630 23.114  1.00 28.75 ? 380 TRP A NE1 1 
ATOM   3239 C CE2 . TRP A 1 380 ? -59.121 31.602 22.189  1.00 22.46 ? 380 TRP A CE2 1 
ATOM   3240 C CE3 . TRP A 1 380 ? -58.641 30.509 20.086  1.00 18.26 ? 380 TRP A CE3 1 
ATOM   3241 C CZ2 . TRP A 1 380 ? -57.907 32.282 22.170  1.00 22.25 ? 380 TRP A CZ2 1 
ATOM   3242 C CZ3 . TRP A 1 380 ? -57.423 31.182 20.073  1.00 22.34 ? 380 TRP A CZ3 1 
ATOM   3243 C CH2 . TRP A 1 380 ? -57.071 32.059 21.104  1.00 24.03 ? 380 TRP A CH2 1 
ATOM   3244 N N   . ILE A 1 381 ? -59.130 26.935 21.802  1.00 18.55 ? 381 ILE A N   1 
ATOM   3245 C CA  . ILE A 1 381 ? -57.841 26.313 21.514  1.00 17.36 ? 381 ILE A CA  1 
ATOM   3246 C C   . ILE A 1 381 ? -57.945 24.826 21.805  1.00 16.81 ? 381 ILE A C   1 
ATOM   3247 O O   . ILE A 1 381 ? -58.401 24.427 22.882  1.00 20.67 ? 381 ILE A O   1 
ATOM   3248 C CB  . ILE A 1 381 ? -56.697 26.936 22.336  1.00 18.52 ? 381 ILE A CB  1 
ATOM   3249 C CG1 . ILE A 1 381 ? -56.533 28.418 22.003  1.00 22.18 ? 381 ILE A CG1 1 
ATOM   3250 C CG2 . ILE A 1 381 ? -55.380 26.174 22.056  1.00 17.17 ? 381 ILE A CG2 1 
ATOM   3251 C CD1 . ILE A 1 381 ? -55.502 29.131 22.865  1.00 18.67 ? 381 ILE A CD1 1 
ATOM   3252 N N   . GLU A 1 382 ? -57.495 24.006 20.864  1.00 17.36 ? 382 GLU A N   1 
ATOM   3253 C CA  . GLU A 1 382 ? -57.342 22.576 21.102  1.00 15.67 ? 382 GLU A CA  1 
ATOM   3254 C C   . GLU A 1 382 ? -55.899 22.216 20.791  1.00 14.50 ? 382 GLU A C   1 
ATOM   3255 O O   . GLU A 1 382 ? -55.467 22.315 19.636  1.00 17.30 ? 382 GLU A O   1 
ATOM   3256 C CB  . GLU A 1 382 ? -58.313 21.750 20.254  1.00 20.21 ? 382 GLU A CB  1 
ATOM   3257 C CG  . GLU A 1 382 ? -58.163 20.240 20.476  1.00 26.85 ? 382 GLU A CG  1 
ATOM   3258 C CD  . GLU A 1 382 ? -59.110 19.401 19.636  1.00 32.67 ? 382 GLU A CD  1 
ATOM   3259 O OE1 . GLU A 1 382 ? -60.086 19.956 19.095  1.00 32.24 ? 382 GLU A OE1 1 
ATOM   3260 O OE2 . GLU A 1 382 ? -58.879 18.177 19.526  1.00 37.69 ? 382 GLU A OE2 1 
ATOM   3261 N N   . THR A 1 383 ? -55.145 21.826 21.820  1.00 17.02 ? 383 THR A N   1 
ATOM   3262 C CA  . THR A 1 383 ? -53.797 21.320 21.598  1.00 15.35 ? 383 THR A CA  1 
ATOM   3263 C C   . THR A 1 383 ? -53.865 19.884 21.095  1.00 14.70 ? 383 THR A C   1 
ATOM   3264 O O   . THR A 1 383 ? -54.760 19.119 21.464  1.00 17.90 ? 383 THR A O   1 
ATOM   3265 C CB  . THR A 1 383 ? -52.945 21.382 22.873  1.00 14.59 ? 383 THR A CB  1 
ATOM   3266 O OG1 . THR A 1 383 ? -53.566 20.638 23.930  1.00 15.51 ? 383 THR A OG1 1 
ATOM   3267 C CG2 . THR A 1 383 ? -52.746 22.821 23.323  1.00 14.69 ? 383 THR A CG2 1 
ATOM   3268 N N   . LEU A 1 384 ? -52.906 19.525 20.235  1.00 13.57 ? 384 LEU A N   1 
ATOM   3269 C CA  . LEU A 1 384 ? -52.945 18.246 19.541  1.00 13.77 ? 384 LEU A CA  1 
ATOM   3270 C C   . LEU A 1 384 ? -51.654 17.469 19.747  1.00 13.16 ? 384 LEU A C   1 
ATOM   3271 O O   . LEU A 1 384 ? -50.574 18.047 19.867  1.00 14.38 ? 384 LEU A O   1 
ATOM   3272 C CB  . LEU A 1 384 ? -53.156 18.438 18.023  1.00 16.01 ? 384 LEU A CB  1 
ATOM   3273 C CG  . LEU A 1 384 ? -54.433 19.125 17.522  1.00 16.02 ? 384 LEU A CG  1 
ATOM   3274 C CD1 . LEU A 1 384 ? -54.417 19.066 16.000  1.00 17.23 ? 384 LEU A CD1 1 
ATOM   3275 C CD2 . LEU A 1 384 ? -55.683 18.446 18.088  1.00 17.22 ? 384 LEU A CD2 1 
ATOM   3276 N N   . THR A 1 385 ? -51.774 16.143 19.765  1.00 15.11 ? 385 THR A N   1 
ATOM   3277 C CA  . THR A 1 385 ? -50.597 15.312 19.570  1.00 14.13 ? 385 THR A CA  1 
ATOM   3278 C C   . THR A 1 385 ? -50.165 15.385 18.109  1.00 17.48 ? 385 THR A C   1 
ATOM   3279 O O   . THR A 1 385 ? -50.925 15.826 17.235  1.00 14.57 ? 385 THR A O   1 
ATOM   3280 C CB  . THR A 1 385 ? -50.871 13.855 19.941  1.00 15.03 ? 385 THR A CB  1 
ATOM   3281 O OG1 . THR A 1 385 ? -51.806 13.280 19.003  1.00 16.07 ? 385 THR A OG1 1 
ATOM   3282 C CG2 . THR A 1 385 ? -51.458 13.733 21.362  1.00 17.98 ? 385 THR A CG2 1 
ATOM   3283 N N   . LEU A 1 386 ? -48.936 14.932 17.839  1.00 14.10 ? 386 LEU A N   1 
ATOM   3284 C CA  . LEU A 1 386 ? -48.494 14.844 16.448  1.00 13.66 ? 386 LEU A CA  1 
ATOM   3285 C C   . LEU A 1 386 ? -49.385 13.899 15.656  1.00 14.90 ? 386 LEU A C   1 
ATOM   3286 O O   . LEU A 1 386 ? -49.710 14.175 14.495  1.00 16.68 ? 386 LEU A O   1 
ATOM   3287 C CB  . LEU A 1 386 ? -47.041 14.380 16.374  1.00 13.53 ? 386 LEU A CB  1 
ATOM   3288 C CG  . LEU A 1 386 ? -46.004 15.243 17.089  1.00 14.88 ? 386 LEU A CG  1 
ATOM   3289 C CD1 . LEU A 1 386 ? -44.623 14.627 16.889  1.00 14.58 ? 386 LEU A CD1 1 
ATOM   3290 C CD2 . LEU A 1 386 ? -46.064 16.667 16.558  1.00 14.18 ? 386 LEU A CD2 1 
ATOM   3291 N N   . GLU A 1 387 ? -49.786 12.779 16.273  1.00 15.85 ? 387 GLU A N   1 
ATOM   3292 C CA  . GLU A 1 387 ? -50.724 11.855 15.644  1.00 17.28 ? 387 GLU A CA  1 
ATOM   3293 C C   . GLU A 1 387 ? -52.013 12.564 15.264  1.00 17.50 ? 387 GLU A C   1 
ATOM   3294 O O   . GLU A 1 387 ? -52.501 12.429 14.134  1.00 18.78 ? 387 GLU A O   1 
ATOM   3295 C CB  . GLU A 1 387 ? -51.006 10.686 16.594  1.00 18.43 ? 387 GLU A CB  1 
ATOM   3296 C CG  . GLU A 1 387 ? -51.568 9.413  15.923  1.00 53.30 ? 387 GLU A CG  1 
ATOM   3297 C CD  . GLU A 1 387 ? -50.479 8.486  15.395  1.00 66.15 ? 387 GLU A CD  1 
ATOM   3298 O OE1 . GLU A 1 387 ? -49.533 8.168  16.153  1.00 69.85 ? 387 GLU A OE1 1 
ATOM   3299 O OE2 . GLU A 1 387 ? -50.535 8.121  14.201  1.00 71.83 ? 387 GLU A OE2 1 
ATOM   3300 N N   . GLU A 1 388 ? -52.571 13.344 16.193  1.00 16.84 ? 388 GLU A N   1 
ATOM   3301 C CA  . GLU A 1 388 ? -53.822 14.031 15.893  1.00 19.22 ? 388 GLU A CA  1 
ATOM   3302 C C   . GLU A 1 388 ? -53.628 15.061 14.791  1.00 16.43 ? 388 GLU A C   1 
ATOM   3303 O O   . GLU A 1 388 ? -54.490 15.208 13.918  1.00 19.81 ? 388 GLU A O   1 
ATOM   3304 C CB  . GLU A 1 388 ? -54.387 14.684 17.152  1.00 19.94 ? 388 GLU A CB  1 
ATOM   3305 C CG  . GLU A 1 388 ? -54.899 13.682 18.170  1.00 20.94 ? 388 GLU A CG  1 
ATOM   3306 C CD  . GLU A 1 388 ? -55.257 14.312 19.497  1.00 26.69 ? 388 GLU A CD  1 
ATOM   3307 O OE1 . GLU A 1 388 ? -54.573 15.265 19.924  1.00 19.09 ? 388 GLU A OE1 1 
ATOM   3308 O OE2 . GLU A 1 388 ? -56.219 13.834 20.130  1.00 31.04 ? 388 GLU A OE2 1 
ATOM   3309 N N   . ALA A 1 389 ? -52.502 15.784 14.810  1.00 16.04 ? 389 ALA A N   1 
ATOM   3310 C CA  . ALA A 1 389 ? -52.247 16.776 13.768  1.00 16.49 ? 389 ALA A CA  1 
ATOM   3311 C C   . ALA A 1 389 ? -52.096 16.117 12.402  1.00 20.31 ? 389 ALA A C   1 
ATOM   3312 O O   . ALA A 1 389 ? -52.579 16.641 11.390  1.00 18.65 ? 389 ALA A O   1 
ATOM   3313 C CB  . ALA A 1 389 ? -50.997 17.588 14.113  1.00 17.00 ? 389 ALA A CB  1 
ATOM   3314 N N   . MET A 1 390 ? -51.436 14.959 12.357  1.00 19.10 ? 390 MET A N   1 
ATOM   3315 C CA  . MET A 1 390 ? -51.261 14.253 11.093  1.00 21.62 ? 390 MET A CA  1 
ATOM   3316 C C   . MET A 1 390 ? -52.590 13.795 10.503  1.00 24.21 ? 390 MET A C   1 
ATOM   3317 O O   . MET A 1 390 ? -52.754 13.808 9.276   1.00 26.09 ? 390 MET A O   1 
ATOM   3318 C CB  . MET A 1 390 ? -50.333 13.056 11.303  1.00 23.76 ? 390 MET A CB  1 
ATOM   3319 C CG  . MET A 1 390 ? -49.938 12.324 10.027  1.00 26.00 ? 390 MET A CG  1 
ATOM   3320 S SD  . MET A 1 390 ? -48.886 10.894 10.370  1.00 36.82 ? 390 MET A SD  1 
ATOM   3321 C CE  . MET A 1 390 ? -50.055 9.800  11.185  1.00 33.22 ? 390 MET A CE  1 
ATOM   3322 N N   . ARG A 1 391 ? -53.549 13.392 11.343  1.00 18.79 ? 391 ARG A N   1 
ATOM   3323 C CA  . ARG A 1 391 ? -54.762 12.735 10.872  1.00 21.00 ? 391 ARG A CA  1 
ATOM   3324 C C   . ARG A 1 391 ? -55.993 13.627 10.907  1.00 20.31 ? 391 ARG A C   1 
ATOM   3325 O O   . ARG A 1 391 ? -57.060 13.194 10.455  1.00 25.43 ? 391 ARG A O   1 
ATOM   3326 C CB  . ARG A 1 391 ? -55.034 11.470 11.692  1.00 26.15 ? 391 ARG A CB  1 
ATOM   3327 C CG  . ARG A 1 391 ? -53.886 10.486 11.717  1.00 26.68 ? 391 ARG A CG  1 
ATOM   3328 C CD  . ARG A 1 391 ? -54.317 9.164  12.319  1.00 36.47 ? 391 ARG A CD  1 
ATOM   3329 N NE  . ARG A 1 391 ? -53.281 8.149  12.154  1.00 50.27 ? 391 ARG A NE  1 
ATOM   3330 C CZ  . ARG A 1 391 ? -53.039 7.502  11.017  1.00 57.12 ? 391 ARG A CZ  1 
ATOM   3331 N NH1 . ARG A 1 391 ? -53.763 7.755  9.935   1.00 58.70 ? 391 ARG A NH1 1 
ATOM   3332 N NH2 . ARG A 1 391 ? -52.071 6.597  10.963  1.00 59.35 ? 391 ARG A NH2 1 
ATOM   3333 N N   . LYS A 1 392 ? -55.872 14.848 11.426  1.00 23.39 ? 392 LYS A N   1 
ATOM   3334 C CA  . LYS A 1 392 ? -57.020 15.738 11.561  1.00 26.04 ? 392 LYS A CA  1 
ATOM   3335 C C   . LYS A 1 392 ? -57.686 15.962 10.210  1.00 25.41 ? 392 LYS A C   1 
ATOM   3336 O O   . LYS A 1 392 ? -57.021 16.296 9.226   1.00 23.22 ? 392 LYS A O   1 
ATOM   3337 C CB  . LYS A 1 392 ? -56.575 17.074 12.153  1.00 23.75 ? 392 LYS A CB  1 
ATOM   3338 C CG  . LYS A 1 392 ? -57.581 17.695 13.106  1.00 27.10 ? 392 LYS A CG  1 
ATOM   3339 C CD  . LYS A 1 392 ? -57.692 16.879 14.388  1.00 29.66 ? 392 LYS A CD  1 
ATOM   3340 C CE  . LYS A 1 392 ? -58.665 17.510 15.360  1.00 31.19 ? 392 LYS A CE  1 
ATOM   3341 N NZ  . LYS A 1 392 ? -60.042 17.569 14.784  1.00 37.60 ? 392 LYS A NZ  1 
ATOM   3342 N N   . GLU A 1 393 ? -59.001 15.772 10.158  1.00 26.06 ? 393 GLU A N   1 
ATOM   3343 C CA  . GLU A 1 393 ? -59.686 15.883 8.878   1.00 26.82 ? 393 GLU A CA  1 
ATOM   3344 C C   . GLU A 1 393 ? -60.227 17.281 8.620   1.00 24.41 ? 393 GLU A C   1 
ATOM   3345 O O   . GLU A 1 393 ? -60.303 17.699 7.459   1.00 31.65 ? 393 GLU A O   1 
ATOM   3346 C CB  . GLU A 1 393 ? -60.823 14.857 8.797   1.00 34.00 ? 393 GLU A CB  1 
ATOM   3347 C CG  . GLU A 1 393 ? -60.327 13.418 8.693   1.00 44.96 ? 393 GLU A CG  1 
ATOM   3348 C CD  . GLU A 1 393 ? -61.443 12.387 8.763   1.00 61.00 ? 393 GLU A CD  1 
ATOM   3349 O OE1 . GLU A 1 393 ? -62.599 12.761 9.060   1.00 64.41 ? 393 GLU A OE1 1 
ATOM   3350 O OE2 . GLU A 1 393 ? -61.157 11.194 8.524   1.00 65.93 ? 393 GLU A OE2 1 
ATOM   3351 N N   . ASP A 1 394 ? -60.599 18.012 9.666   1.00 23.42 ? 394 ASP A N   1 
ATOM   3352 C CA  . ASP A 1 394 ? -61.236 19.321 9.520   1.00 27.40 ? 394 ASP A CA  1 
ATOM   3353 C C   . ASP A 1 394 ? -60.206 20.450 9.446   1.00 26.83 ? 394 ASP A C   1 
ATOM   3354 O O   . ASP A 1 394 ? -60.327 21.475 10.115  1.00 26.89 ? 394 ASP A O   1 
ATOM   3355 C CB  . ASP A 1 394 ? -62.211 19.552 10.669  1.00 31.54 ? 394 ASP A CB  1 
ATOM   3356 C CG  . ASP A 1 394 ? -61.601 19.232 12.027  1.00 37.27 ? 394 ASP A CG  1 
ATOM   3357 O OD1 . ASP A 1 394 ? -60.450 18.740 12.065  1.00 38.21 ? 394 ASP A OD1 1 
ATOM   3358 O OD2 . ASP A 1 394 ? -62.265 19.486 13.057  1.00 40.69 ? 394 ASP A OD2 1 
ATOM   3359 N N   . VAL A 1 395 ? -59.179 20.266 8.616   1.00 21.18 ? 395 VAL A N   1 
ATOM   3360 C CA  . VAL A 1 395 ? -58.121 21.252 8.426   1.00 20.64 ? 395 VAL A CA  1 
ATOM   3361 C C   . VAL A 1 395 ? -57.881 21.404 6.930   1.00 21.27 ? 395 VAL A C   1 
ATOM   3362 O O   . VAL A 1 395 ? -58.370 20.619 6.118   1.00 25.35 ? 395 VAL A O   1 
ATOM   3363 C CB  . VAL A 1 395 ? -56.807 20.867 9.138   1.00 18.96 ? 395 VAL A CB  1 
ATOM   3364 C CG1 . VAL A 1 395 ? -57.034 20.703 10.636  1.00 21.95 ? 395 VAL A CG1 1 
ATOM   3365 C CG2 . VAL A 1 395 ? -56.230 19.600 8.525   1.00 20.62 ? 395 VAL A CG2 1 
ATOM   3366 N N   . LYS A 1 396 ? -57.124 22.431 6.569   1.00 18.24 ? 396 LYS A N   1 
ATOM   3367 C CA  . LYS A 1 396 ? -56.827 22.686 5.168   1.00 18.98 ? 396 LYS A CA  1 
ATOM   3368 C C   . LYS A 1 396 ? -55.498 22.050 4.790   1.00 18.41 ? 396 LYS A C   1 
ATOM   3369 O O   . LYS A 1 396 ? -54.560 22.010 5.592   1.00 17.44 ? 396 LYS A O   1 
ATOM   3370 C CB  . LYS A 1 396 ? -56.796 24.187 4.874   1.00 22.47 ? 396 LYS A CB  1 
ATOM   3371 C CG  . LYS A 1 396 ? -58.180 24.825 4.875   1.00 28.94 ? 396 LYS A CG  1 
ATOM   3372 C CD  . LYS A 1 396 ? -58.281 26.051 3.972   1.00 36.64 ? 396 LYS A CD  1 
ATOM   3373 C CE  . LYS A 1 396 ? -59.517 25.990 3.056   1.00 45.52 ? 396 LYS A CE  1 
ATOM   3374 N NZ  . LYS A 1 396 ? -60.806 25.700 3.753   1.00 49.38 ? 396 LYS A NZ  1 
ATOM   3375 N N   . THR A 1 397 ? -55.432 21.540 3.563   1.00 18.47 ? 397 THR A N   1 
ATOM   3376 C CA  . THR A 1 397 ? -54.245 20.872 3.060   1.00 17.39 ? 397 THR A CA  1 
ATOM   3377 C C   . THR A 1 397 ? -53.843 21.454 1.715   1.00 17.21 ? 397 THR A C   1 
ATOM   3378 O O   . THR A 1 397 ? -54.641 22.097 1.019   1.00 18.02 ? 397 THR A O   1 
ATOM   3379 C CB  . THR A 1 397 ? -54.465 19.363 2.891   1.00 17.85 ? 397 THR A CB  1 
ATOM   3380 O OG1 . THR A 1 397 ? -55.412 19.149 1.835   1.00 18.69 ? 397 THR A OG1 1 
ATOM   3381 C CG2 . THR A 1 397 ? -55.012 18.757 4.163   1.00 18.01 ? 397 THR A CG2 1 
ATOM   3382 N N   . GLU A 1 398 ? -52.599 21.169 1.335   1.00 16.60 ? 398 GLU A N   1 
ATOM   3383 C CA  . GLU A 1 398 ? -52.016 21.665 0.095   1.00 16.21 ? 398 GLU A CA  1 
ATOM   3384 C C   . GLU A 1 398 ? -50.873 20.743 -0.312  1.00 18.43 ? 398 GLU A C   1 
ATOM   3385 O O   . GLU A 1 398 ? -50.153 20.219 0.538   1.00 18.13 ? 398 GLU A O   1 
ATOM   3386 C CB  . GLU A 1 398 ? -51.517 23.105 0.274   1.00 16.30 ? 398 GLU A CB  1 
ATOM   3387 C CG  . GLU A 1 398 ? -50.942 23.737 -0.971  1.00 24.02 ? 398 GLU A CG  1 
ATOM   3388 C CD  . GLU A 1 398 ? -51.970 23.819 -2.082  1.00 35.45 ? 398 GLU A CD  1 
ATOM   3389 O OE1 . GLU A 1 398 ? -52.004 22.900 -2.931  1.00 43.19 ? 398 GLU A OE1 1 
ATOM   3390 O OE2 . GLU A 1 398 ? -52.760 24.787 -2.091  1.00 37.67 ? 398 GLU A OE2 1 
ATOM   3391 N N   . VAL A 1 399 ? -50.693 20.571 -1.614  1.00 17.26 ? 399 VAL A N   1 
ATOM   3392 C CA  . VAL A 1 399 ? -49.571 19.796 -2.139  1.00 15.33 ? 399 VAL A CA  1 
ATOM   3393 C C   . VAL A 1 399 ? -48.420 20.739 -2.460  1.00 19.01 ? 399 VAL A C   1 
ATOM   3394 O O   . VAL A 1 399 ? -48.632 21.829 -3.002  1.00 23.16 ? 399 VAL A O   1 
ATOM   3395 C CB  . VAL A 1 399 ? -50.006 18.988 -3.380  1.00 20.59 ? 399 VAL A CB  1 
ATOM   3396 C CG1 . VAL A 1 399 ? -48.817 18.253 -3.999  1.00 21.08 ? 399 VAL A CG1 1 
ATOM   3397 C CG2 . VAL A 1 399 ? -51.106 18.021 -3.015  1.00 20.56 ? 399 VAL A CG2 1 
ATOM   3398 N N   . ILE A 1 400 ? -47.197 20.341 -2.094  1.00 17.50 ? 400 ILE A N   1 
ATOM   3399 C CA  . ILE A 1 400 ? -45.988 21.099 -2.411  1.00 17.21 ? 400 ILE A CA  1 
ATOM   3400 C C   . ILE A 1 400 ? -45.066 20.197 -3.231  1.00 17.10 ? 400 ILE A C   1 
ATOM   3401 O O   . ILE A 1 400 ? -44.892 19.016 -2.905  1.00 18.97 ? 400 ILE A O   1 
ATOM   3402 C CB  . ILE A 1 400 ? -45.303 21.640 -1.134  1.00 19.80 ? 400 ILE A CB  1 
ATOM   3403 C CG1 . ILE A 1 400 ? -44.069 22.485 -1.469  1.00 21.06 ? 400 ILE A CG1 1 
ATOM   3404 C CG2 . ILE A 1 400 ? -44.961 20.534 -0.146  1.00 23.20 ? 400 ILE A CG2 1 
ATOM   3405 C CD1 . ILE A 1 400 ? -43.483 23.186 -0.247  1.00 25.99 ? 400 ILE A CD1 1 
ATOM   3406 N N   . GLU A 1 401 ? -44.490 20.746 -4.301  1.00 16.99 ? 401 GLU A N   1 
ATOM   3407 C CA  . GLU A 1 401 ? -43.679 19.961 -5.228  1.00 14.92 ? 401 GLU A CA  1 
ATOM   3408 C C   . GLU A 1 401 ? -42.181 20.036 -4.942  1.00 15.29 ? 401 GLU A C   1 
ATOM   3409 O O   . GLU A 1 401 ? -41.450 19.082 -5.234  1.00 18.11 ? 401 GLU A O   1 
ATOM   3410 C CB  . GLU A 1 401 ? -43.957 20.410 -6.674  1.00 18.73 ? 401 GLU A CB  1 
ATOM   3411 C CG  . GLU A 1 401 ? -42.939 19.937 -7.714  1.00 26.54 ? 401 GLU A CG  1 
ATOM   3412 C CD  . GLU A 1 401 ? -42.929 18.425 -7.908  1.00 29.18 ? 401 GLU A CD  1 
ATOM   3413 O OE1 . GLU A 1 401 ? -43.948 17.761 -7.610  1.00 29.04 ? 401 GLU A OE1 1 
ATOM   3414 O OE2 . GLU A 1 401 ? -41.885 17.901 -8.353  1.00 27.09 ? 401 GLU A OE2 1 
ATOM   3415 N N   . SER A 1 402 ? -41.705 21.136 -4.370  1.00 14.07 ? 402 SER A N   1 
ATOM   3416 C CA  . SER A 1 402 ? -40.266 21.330 -4.242  1.00 14.70 ? 402 SER A CA  1 
ATOM   3417 C C   . SER A 1 402 ? -40.002 22.306 -3.108  1.00 14.68 ? 402 SER A C   1 
ATOM   3418 O O   . SER A 1 402 ? -40.779 23.241 -2.913  1.00 19.02 ? 402 SER A O   1 
ATOM   3419 C CB  . SER A 1 402 ? -39.690 21.869 -5.559  1.00 18.59 ? 402 SER A CB  1 
ATOM   3420 O OG  . SER A 1 402 ? -38.274 21.970 -5.514  1.00 21.65 ? 402 SER A OG  1 
ATOM   3421 N N   . VAL A 1 403 ? -38.918 22.077 -2.357  1.00 13.69 ? 403 VAL A N   1 
ATOM   3422 C CA  . VAL A 1 403 ? -38.464 23.023 -1.339  1.00 16.61 ? 403 VAL A CA  1 
ATOM   3423 C C   . VAL A 1 403 ? -37.080 23.526 -1.717  1.00 18.39 ? 403 VAL A C   1 
ATOM   3424 O O   . VAL A 1 403 ? -36.321 22.848 -2.413  1.00 17.46 ? 403 VAL A O   1 
ATOM   3425 C CB  . VAL A 1 403 ? -38.443 22.425 0.086   1.00 16.57 ? 403 VAL A CB  1 
ATOM   3426 C CG1 . VAL A 1 403 ? -39.863 22.058 0.532   1.00 19.67 ? 403 VAL A CG1 1 
ATOM   3427 C CG2 . VAL A 1 403 ? -37.500 21.234 0.168   1.00 15.74 ? 403 VAL A CG2 1 
ATOM   3428 N N   . LYS A 1 404 ? -36.778 24.757 -1.304  1.00 16.83 ? 404 LYS A N   1 
ATOM   3429 C CA  . LYS A 1 404 ? -35.407 25.258 -1.334  1.00 13.89 ? 404 LYS A CA  1 
ATOM   3430 C C   . LYS A 1 404 ? -34.697 24.811 -0.062  1.00 15.34 ? 404 LYS A C   1 
ATOM   3431 O O   . LYS A 1 404 ? -35.153 25.107 1.048   1.00 15.09 ? 404 LYS A O   1 
ATOM   3432 C CB  . LYS A 1 404 ? -35.382 26.778 -1.468  1.00 18.08 ? 404 LYS A CB  1 
ATOM   3433 C CG  . LYS A 1 404 ? -35.833 27.278 -2.834  1.00 22.11 ? 404 LYS A CG  1 
ATOM   3434 C CD  . LYS A 1 404 ? -35.406 28.727 -3.080  1.00 35.51 ? 404 LYS A CD  1 
ATOM   3435 C CE  . LYS A 1 404 ? -35.404 29.071 -4.563  1.00 44.50 ? 404 LYS A CE  1 
ATOM   3436 N NZ  . LYS A 1 404 ? -34.880 30.446 -4.814  1.00 51.34 ? 404 LYS A NZ  1 
ATOM   3437 N N   . ALA A 1 405 ? -33.603 24.068 -0.224  1.00 12.50 ? 405 ALA A N   1 
ATOM   3438 C CA  . ALA A 1 405 ? -32.938 23.441 0.916   1.00 13.38 ? 405 ALA A CA  1 
ATOM   3439 C C   . ALA A 1 405 ? -32.460 24.470 1.928   1.00 13.53 ? 405 ALA A C   1 
ATOM   3440 O O   . ALA A 1 405 ? -31.980 25.551 1.570   1.00 14.60 ? 405 ALA A O   1 
ATOM   3441 C CB  . ALA A 1 405 ? -31.747 22.614 0.434   1.00 13.47 ? 405 ALA A CB  1 
ATOM   3442 N N   . GLY A 1 406 ? -32.548 24.112 3.199   1.00 12.06 ? 406 GLY A N   1 
ATOM   3443 C CA  . GLY A 1 406 ? -32.054 25.004 4.229   1.00 13.68 ? 406 GLY A CA  1 
ATOM   3444 C C   . GLY A 1 406 ? -32.317 24.453 5.609   1.00 13.35 ? 406 GLY A C   1 
ATOM   3445 O O   . GLY A 1 406 ? -32.591 23.262 5.779   1.00 12.06 ? 406 GLY A O   1 
ATOM   3446 N N   . THR A 1 407 ? -32.206 25.347 6.595   1.00 14.04 ? 407 THR A N   1 
ATOM   3447 C CA  . THR A 1 407 ? -32.376 25.057 8.015   1.00 11.52 ? 407 THR A CA  1 
ATOM   3448 C C   . THR A 1 407 ? -33.186 26.191 8.621   1.00 10.56 ? 407 THR A C   1 
ATOM   3449 O O   . THR A 1 407 ? -33.478 27.193 7.955   1.00 13.08 ? 407 THR A O   1 
ATOM   3450 C CB  . THR A 1 407 ? -31.042 24.982 8.780   1.00 11.05 ? 407 THR A CB  1 
ATOM   3451 O OG1 . THR A 1 407 ? -30.537 26.315 8.951   1.00 14.14 ? 407 THR A OG1 1 
ATOM   3452 C CG2 . THR A 1 407 ? -30.022 24.126 8.052   1.00 12.04 ? 407 THR A CG2 1 
ATOM   3453 N N   . TRP A 1 408 ? -33.506 26.074 9.909   1.00 11.21 ? 408 TRP A N   1 
ATOM   3454 C CA  . TRP A 1 408 ? -34.172 27.181 10.583  1.00 12.29 ? 408 TRP A CA  1 
ATOM   3455 C C   . TRP A 1 408 ? -33.233 28.336 10.942  1.00 13.82 ? 408 TRP A C   1 
ATOM   3456 O O   . TRP A 1 408 ? -33.694 29.323 11.524  1.00 15.93 ? 408 TRP A O   1 
ATOM   3457 C CB  . TRP A 1 408 ? -34.928 26.692 11.827  1.00 12.99 ? 408 TRP A CB  1 
ATOM   3458 C CG  . TRP A 1 408 ? -34.134 25.994 12.920  1.00 14.42 ? 408 TRP A CG  1 
ATOM   3459 C CD1 . TRP A 1 408 ? -32.783 25.864 13.019  1.00 13.66 ? 408 TRP A CD1 1 
ATOM   3460 C CD2 . TRP A 1 408 ? -34.693 25.343 14.061  1.00 13.65 ? 408 TRP A CD2 1 
ATOM   3461 N NE1 . TRP A 1 408 ? -32.460 25.173 14.173  1.00 15.04 ? 408 TRP A NE1 1 
ATOM   3462 C CE2 . TRP A 1 408 ? -33.618 24.837 14.824  1.00 11.71 ? 408 TRP A CE2 1 
ATOM   3463 C CE3 . TRP A 1 408 ? -36.000 25.143 14.511  1.00 12.97 ? 408 TRP A CE3 1 
ATOM   3464 C CZ2 . TRP A 1 408 ? -33.812 24.140 16.018  1.00 14.98 ? 408 TRP A CZ2 1 
ATOM   3465 C CZ3 . TRP A 1 408 ? -36.200 24.446 15.700  1.00 13.98 ? 408 TRP A CZ3 1 
ATOM   3466 C CH2 . TRP A 1 408 ? -35.099 23.956 16.441  1.00 14.91 ? 408 TRP A CH2 1 
ATOM   3467 N N   . PHE A 1 409 ? -31.935 28.250 10.630  1.00 14.09 ? 409 PHE A N   1 
ATOM   3468 C CA  . PHE A 1 409 ? -31.109 29.460 10.630  1.00 14.02 ? 409 PHE A CA  1 
ATOM   3469 C C   . PHE A 1 409 ? -31.307 30.135 9.276   1.00 17.19 ? 409 PHE A C   1 
ATOM   3470 O O   . PHE A 1 409 ? -30.619 29.835 8.297   1.00 17.90 ? 409 PHE A O   1 
ATOM   3471 C CB  . PHE A 1 409 ? -29.639 29.143 10.886  1.00 16.81 ? 409 PHE A CB  1 
ATOM   3472 C CG  . PHE A 1 409 ? -28.743 30.345 10.756  1.00 19.06 ? 409 PHE A CG  1 
ATOM   3473 C CD1 . PHE A 1 409 ? -28.746 31.319 11.731  1.00 23.32 ? 409 PHE A CD1 1 
ATOM   3474 C CD2 . PHE A 1 409 ? -27.932 30.510 9.644   1.00 22.45 ? 409 PHE A CD2 1 
ATOM   3475 C CE1 . PHE A 1 409 ? -27.940 32.440 11.612  1.00 27.44 ? 409 PHE A CE1 1 
ATOM   3476 C CE2 . PHE A 1 409 ? -27.122 31.623 9.519   1.00 22.22 ? 409 PHE A CE2 1 
ATOM   3477 C CZ  . PHE A 1 409 ? -27.122 32.587 10.503  1.00 29.25 ? 409 PHE A CZ  1 
ATOM   3478 N N   . ASP A 1 410 ? -32.291 31.039 9.217   1.00 20.36 ? 410 ASP A N   1 
ATOM   3479 C CA  . ASP A 1 410 ? -32.503 31.913 8.053   1.00 21.05 ? 410 ASP A CA  1 
ATOM   3480 C C   . ASP A 1 410 ? -32.621 31.144 6.735   1.00 17.83 ? 410 ASP A C   1 
ATOM   3481 O O   . ASP A 1 410 ? -32.288 31.671 5.669   1.00 20.16 ? 410 ASP A O   1 
ATOM   3482 C CB  . ASP A 1 410 ? -31.393 32.960 7.953   1.00 28.91 ? 410 ASP A CB  1 
ATOM   3483 C CG  . ASP A 1 410 ? -31.250 33.781 9.223   1.00 40.82 ? 410 ASP A CG  1 
ATOM   3484 O OD1 . ASP A 1 410 ? -32.216 33.824 10.019  1.00 44.42 ? 410 ASP A OD1 1 
ATOM   3485 O OD2 . ASP A 1 410 ? -30.170 34.374 9.426   1.00 43.04 ? 410 ASP A OD2 1 
ATOM   3486 N N   . GLY A 1 411 ? -33.110 29.902 6.777   1.00 15.10 ? 411 GLY A N   1 
ATOM   3487 C CA  . GLY A 1 411 ? -33.277 29.130 5.560   1.00 14.94 ? 411 GLY A CA  1 
ATOM   3488 C C   . GLY A 1 411 ? -32.007 28.693 4.869   1.00 13.37 ? 411 GLY A C   1 
ATOM   3489 O O   . GLY A 1 411 ? -32.049 28.366 3.680   1.00 17.44 ? 411 GLY A O   1 
ATOM   3490 N N   . ASN A 1 412 ? -30.863 28.661 5.572   1.00 15.00 ? 412 ASN A N   1 
ATOM   3491 C CA  . ASN A 1 412 ? -29.601 28.335 4.907   1.00 14.83 ? 412 ASN A CA  1 
ATOM   3492 C C   . ASN A 1 412 ? -28.698 27.546 5.855   1.00 14.98 ? 412 ASN A C   1 
ATOM   3493 O O   . ASN A 1 412 ? -29.068 27.242 6.990   1.00 14.83 ? 412 ASN A O   1 
ATOM   3494 C CB  . ASN A 1 412 ? -28.911 29.598 4.353   1.00 15.66 ? 412 ASN A CB  1 
ATOM   3495 C CG  . ASN A 1 412 ? -28.370 30.524 5.442   1.00 20.53 ? 412 ASN A CG  1 
ATOM   3496 O OD1 . ASN A 1 412 ? -27.619 30.105 6.334   1.00 17.51 ? 412 ASN A OD1 1 
ATOM   3497 N ND2 . ASN A 1 412 ? -28.707 31.809 5.340   1.00 25.67 ? 412 ASN A ND2 1 
ATOM   3498 N N   . PHE A 1 413 ? -27.511 27.184 5.358   1.00 14.48 ? 413 PHE A N   1 
ATOM   3499 C CA  . PHE A 1 413 ? -26.614 26.277 6.064   1.00 13.59 ? 413 PHE A CA  1 
ATOM   3500 C C   . PHE A 1 413 ? -25.394 26.974 6.637   1.00 16.40 ? 413 PHE A C   1 
ATOM   3501 O O   . PHE A 1 413 ? -24.450 26.292 7.041   1.00 16.58 ? 413 PHE A O   1 
ATOM   3502 C CB  . PHE A 1 413 ? -26.163 25.151 5.136   1.00 12.76 ? 413 PHE A CB  1 
ATOM   3503 C CG  . PHE A 1 413 ? -27.275 24.216 4.739   1.00 13.16 ? 413 PHE A CG  1 
ATOM   3504 C CD1 . PHE A 1 413 ? -27.633 23.175 5.576   1.00 14.95 ? 413 PHE A CD1 1 
ATOM   3505 C CD2 . PHE A 1 413 ? -27.957 24.379 3.535   1.00 16.87 ? 413 PHE A CD2 1 
ATOM   3506 C CE1 . PHE A 1 413 ? -28.659 22.312 5.230   1.00 12.51 ? 413 PHE A CE1 1 
ATOM   3507 C CE2 . PHE A 1 413 ? -28.979 23.510 3.179   1.00 16.23 ? 413 PHE A CE2 1 
ATOM   3508 C CZ  . PHE A 1 413 ? -29.333 22.474 4.032   1.00 12.73 ? 413 PHE A CZ  1 
ATOM   3509 N N   . LEU A 1 414 ? -25.392 28.305 6.705   1.00 14.77 ? 414 LEU A N   1 
ATOM   3510 C CA  . LEU A 1 414 ? -24.160 29.021 7.024   1.00 16.04 ? 414 LEU A CA  1 
ATOM   3511 C C   . LEU A 1 414 ? -23.713 28.857 8.474   1.00 16.23 ? 414 LEU A C   1 
ATOM   3512 O O   . LEU A 1 414 ? -22.574 29.215 8.784   1.00 18.45 ? 414 LEU A O   1 
ATOM   3513 C CB  . LEU A 1 414 ? -24.327 30.503 6.691   1.00 15.87 ? 414 LEU A CB  1 
ATOM   3514 C CG  . LEU A 1 414 ? -24.502 30.772 5.190   1.00 18.22 ? 414 LEU A CG  1 
ATOM   3515 C CD1 . LEU A 1 414 ? -24.552 32.258 4.925   1.00 20.09 ? 414 LEU A CD1 1 
ATOM   3516 C CD2 . LEU A 1 414 ? -23.386 30.129 4.368   1.00 20.13 ? 414 LEU A CD2 1 
ATOM   3517 N N   . LYS A 1 415 ? -24.551 28.328 9.374   1.00 15.70 ? 415 LYS A N   1 
ATOM   3518 C CA  . LYS A 1 415 ? -24.043 28.088 10.724  1.00 14.74 ? 415 LYS A CA  1 
ATOM   3519 C C   . LYS A 1 415 ? -23.172 26.839 10.825  1.00 14.69 ? 415 LYS A C   1 
ATOM   3520 O O   . LYS A 1 415 ? -22.579 26.603 11.887  1.00 16.10 ? 415 LYS A O   1 
ATOM   3521 C CB  . LYS A 1 415 ? -25.205 27.985 11.726  1.00 15.16 ? 415 LYS A CB  1 
ATOM   3522 C CG  . LYS A 1 415 ? -25.730 29.339 12.209  1.00 24.43 ? 415 LYS A CG  1 
ATOM   3523 C CD  . LYS A 1 415 ? -24.711 30.060 13.083  1.00 35.75 ? 415 LYS A CD  1 
ATOM   3524 C CE  . LYS A 1 415 ? -25.300 31.337 13.663  1.00 43.64 ? 415 LYS A CE  1 
ATOM   3525 N NZ  . LYS A 1 415 ? -24.311 32.134 14.444  1.00 47.94 ? 415 LYS A NZ  1 
ATOM   3526 N N   . TRP A 1 416 ? -23.074 26.042 9.759   1.00 14.41 ? 416 TRP A N   1 
ATOM   3527 C CA  . TRP A 1 416 ? -22.363 24.770 9.806   1.00 12.67 ? 416 TRP A CA  1 
ATOM   3528 C C   . TRP A 1 416 ? -21.341 24.602 8.695   1.00 15.75 ? 416 TRP A C   1 
ATOM   3529 O O   . TRP A 1 416 ? -20.583 23.621 8.718   1.00 15.65 ? 416 TRP A O   1 
ATOM   3530 C CB  . TRP A 1 416 ? -23.358 23.595 9.755   1.00 14.15 ? 416 TRP A CB  1 
ATOM   3531 C CG  . TRP A 1 416 ? -24.401 23.670 10.827  1.00 12.80 ? 416 TRP A CG  1 
ATOM   3532 C CD1 . TRP A 1 416 ? -24.339 23.137 12.093  1.00 14.42 ? 416 TRP A CD1 1 
ATOM   3533 C CD2 . TRP A 1 416 ? -25.637 24.377 10.751  1.00 11.03 ? 416 TRP A CD2 1 
ATOM   3534 N NE1 . TRP A 1 416 ? -25.479 23.450 12.799  1.00 12.59 ? 416 TRP A NE1 1 
ATOM   3535 C CE2 . TRP A 1 416 ? -26.291 24.219 12.002  1.00 11.09 ? 416 TRP A CE2 1 
ATOM   3536 C CE3 . TRP A 1 416 ? -26.264 25.131 9.741   1.00 13.63 ? 416 TRP A CE3 1 
ATOM   3537 C CZ2 . TRP A 1 416 ? -27.529 24.791 12.275  1.00 16.12 ? 416 TRP A CZ2 1 
ATOM   3538 C CZ3 . TRP A 1 416 ? -27.501 25.690 10.008  1.00 15.22 ? 416 TRP A CZ3 1 
ATOM   3539 C CH2 . TRP A 1 416 ? -28.127 25.512 11.264  1.00 13.87 ? 416 TRP A CH2 1 
ATOM   3540 N N   . ILE A 1 417 ? -21.301 25.509 7.721   1.00 14.12 ? 417 ILE A N   1 
ATOM   3541 C CA  . ILE A 1 417 ? -20.404 25.372 6.582   1.00 14.51 ? 417 ILE A CA  1 
ATOM   3542 C C   . ILE A 1 417 ? -20.246 26.754 5.974   1.00 18.42 ? 417 ILE A C   1 
ATOM   3543 O O   . ILE A 1 417 ? -21.083 27.634 6.177   1.00 18.84 ? 417 ILE A O   1 
ATOM   3544 C CB  . ILE A 1 417 ? -20.972 24.348 5.562   1.00 16.37 ? 417 ILE A CB  1 
ATOM   3545 C CG1 . ILE A 1 417 ? -19.879 23.852 4.617   1.00 16.60 ? 417 ILE A CG1 1 
ATOM   3546 C CG2 . ILE A 1 417 ? -22.159 24.945 4.790   1.00 16.10 ? 417 ILE A CG2 1 
ATOM   3547 C CD1 . ILE A 1 417 ? -20.237 22.553 3.894   1.00 18.94 ? 417 ILE A CD1 1 
ATOM   3548 N N   . GLY A 1 418 ? -19.148 26.967 5.260   1.00 18.01 ? 418 GLY A N   1 
ATOM   3549 C CA  . GLY A 1 418 ? -18.998 28.167 4.462   1.00 20.14 ? 418 GLY A CA  1 
ATOM   3550 C C   . GLY A 1 418 ? -18.006 29.186 4.970   1.00 25.01 ? 418 GLY A C   1 
ATOM   3551 O O   . GLY A 1 418 ? -17.757 30.170 4.266   1.00 31.00 ? 418 GLY A O   1 
ATOM   3552 N N   . ASN A 1 419 ? -17.443 29.024 6.161   1.00 21.44 ? 419 ASN A N   1 
ATOM   3553 C CA  . ASN A 1 419 ? -16.255 29.795 6.483   1.00 25.38 ? 419 ASN A CA  1 
ATOM   3554 C C   . ASN A 1 419 ? -15.066 28.858 6.645   1.00 25.53 ? 419 ASN A C   1 
ATOM   3555 O O   . ASN A 1 419 ? -15.193 27.632 6.623   1.00 21.23 ? 419 ASN A O   1 
ATOM   3556 C CB  . ASN A 1 419 ? -16.462 30.707 7.711   1.00 27.45 ? 419 ASN A CB  1 
ATOM   3557 C CG  . ASN A 1 419 ? -16.551 29.960 9.045   1.00 28.72 ? 419 ASN A CG  1 
ATOM   3558 O OD1 . ASN A 1 419 ? -16.121 28.822 9.193   1.00 27.71 ? 419 ASN A OD1 1 
ATOM   3559 N ND2 . ASN A 1 419 ? -17.102 30.640 10.039  1.00 27.97 ? 419 ASN A ND2 1 
ATOM   3560 N N   . LYS A 1 420 ? -13.899 29.470 6.812   1.00 30.19 ? 420 LYS A N   1 
ATOM   3561 C CA  . LYS A 1 420 ? -12.645 28.730 6.766   1.00 25.49 ? 420 LYS A CA  1 
ATOM   3562 C C   . LYS A 1 420 ? -12.615 27.641 7.833   1.00 23.92 ? 420 LYS A C   1 
ATOM   3563 O O   . LYS A 1 420 ? -12.271 26.486 7.552   1.00 22.46 ? 420 LYS A O   1 
ATOM   3564 C CB  . LYS A 1 420 ? -11.457 29.692 6.933   1.00 32.00 ? 420 LYS A CB  1 
ATOM   3565 C CG  . LYS A 1 420 ? -11.312 30.844 5.893   1.00 48.88 ? 420 LYS A CG  1 
ATOM   3566 C CD  . LYS A 1 420 ? -12.527 31.792 5.762   1.00 55.39 ? 420 LYS A CD  1 
ATOM   3567 C CE  . LYS A 1 420 ? -12.969 32.369 7.109   1.00 57.03 ? 420 LYS A CE  1 
ATOM   3568 N NZ  . LYS A 1 420 ? -14.171 33.234 6.973   1.00 58.09 ? 420 LYS A NZ  1 
ATOM   3569 N N   . GLU A 1 421 ? -12.998 27.989 9.063   1.00 24.81 ? 421 GLU A N   1 
ATOM   3570 C CA  . GLU A 1 421 ? -12.888 27.045 10.171  1.00 24.89 ? 421 GLU A CA  1 
ATOM   3571 C C   . GLU A 1 421 ? -13.919 25.929 10.050  1.00 21.82 ? 421 GLU A C   1 
ATOM   3572 O O   . GLU A 1 421 ? -13.593 24.751 10.237  1.00 22.24 ? 421 GLU A O   1 
ATOM   3573 C CB  . GLU A 1 421 ? -13.041 27.776 11.508  1.00 24.13 ? 421 GLU A CB  1 
ATOM   3574 C CG  . GLU A 1 421 ? -11.891 28.714 11.879  1.00 29.29 ? 421 GLU A CG  1 
ATOM   3575 C CD  . GLU A 1 421 ? -11.838 29.962 11.013  1.00 44.17 ? 421 GLU A CD  1 
ATOM   3576 O OE1 . GLU A 1 421 ? -10.715 30.409 10.699  1.00 50.88 ? 421 GLU A OE1 1 
ATOM   3577 O OE2 . GLU A 1 421 ? -12.910 30.489 10.632  1.00 43.95 ? 421 GLU A OE2 1 
ATOM   3578 N N   . LYS A 1 422 ? -15.179 26.279 9.752   1.00 19.65 ? 422 LYS A N   1 
ATOM   3579 C CA  . LYS A 1 422 ? -16.203 25.253 9.569   1.00 17.93 ? 422 LYS A CA  1 
ATOM   3580 C C   . LYS A 1 422 ? -15.865 24.355 8.391   1.00 19.39 ? 422 LYS A C   1 
ATOM   3581 O O   . LYS A 1 422 ? -16.056 23.136 8.453   1.00 16.96 ? 422 LYS A O   1 
ATOM   3582 C CB  . LYS A 1 422 ? -17.582 25.895 9.372   1.00 17.51 ? 422 LYS A CB  1 
ATOM   3583 C CG  . LYS A 1 422 ? -18.126 26.584 10.625  1.00 19.16 ? 422 LYS A CG  1 
ATOM   3584 C CD  . LYS A 1 422 ? -19.452 27.290 10.374  1.00 17.49 ? 422 LYS A CD  1 
ATOM   3585 C CE  . LYS A 1 422 ? -19.779 28.259 11.516  1.00 18.31 ? 422 LYS A CE  1 
ATOM   3586 N NZ  . LYS A 1 422 ? -20.052 27.581 12.827  1.00 16.36 ? 422 LYS A NZ  1 
ATOM   3587 N N   . ASN A 1 423 ? -15.350 24.936 7.309   1.00 18.40 ? 423 ASN A N   1 
ATOM   3588 C CA  . ASN A 1 423 ? -14.949 24.120 6.170   1.00 21.78 ? 423 ASN A CA  1 
ATOM   3589 C C   . ASN A 1 423 ? -13.813 23.169 6.522   1.00 20.03 ? 423 ASN A C   1 
ATOM   3590 O O   . ASN A 1 423 ? -13.741 22.063 5.968   1.00 20.04 ? 423 ASN A O   1 
ATOM   3591 C CB  . ASN A 1 423 ? -14.548 25.016 5.005   1.00 21.27 ? 423 ASN A CB  1 
ATOM   3592 C CG  . ASN A 1 423 ? -15.741 25.636 4.322   1.00 19.86 ? 423 ASN A CG  1 
ATOM   3593 O OD1 . ASN A 1 423 ? -16.886 25.343 4.666   1.00 19.05 ? 423 ASN A OD1 1 
ATOM   3594 N ND2 . ASN A 1 423 ? -15.480 26.513 3.363   1.00 20.25 ? 423 ASN A ND2 1 
ATOM   3595 N N   . GLU A 1 424 ? -12.920 23.571 7.435   1.00 21.84 ? 424 GLU A N   1 
ATOM   3596 C CA  . GLU A 1 424 ? -11.830 22.683 7.824   1.00 20.84 ? 424 GLU A CA  1 
ATOM   3597 C C   . GLU A 1 424 ? -12.370 21.424 8.484   1.00 19.79 ? 424 GLU A C   1 
ATOM   3598 O O   . GLU A 1 424 ? -11.839 20.328 8.273   1.00 18.62 ? 424 GLU A O   1 
ATOM   3599 C CB  . GLU A 1 424 ? -10.859 23.412 8.757   1.00 21.81 ? 424 GLU A CB  1 
ATOM   3600 C CG  . GLU A 1 424 ? -9.676  22.575 9.266   1.00 29.98 ? 424 GLU A CG  1 
ATOM   3601 C CD  . GLU A 1 424 ? -8.804  22.007 8.152   1.00 42.79 ? 424 GLU A CD  1 
ATOM   3602 O OE1 . GLU A 1 424 ? -8.150  20.963 8.381   1.00 46.21 ? 424 GLU A OE1 1 
ATOM   3603 O OE2 . GLU A 1 424 ? -8.763  22.599 7.051   1.00 46.77 ? 424 GLU A OE2 1 
ATOM   3604 N N   . TYR A 1 425 ? -13.426 21.563 9.295   1.00 18.26 ? 425 TYR A N   1 
ATOM   3605 C CA  . TYR A 1 425 ? -14.061 20.388 9.881   1.00 15.83 ? 425 TYR A CA  1 
ATOM   3606 C C   . TYR A 1 425 ? -14.609 19.458 8.801   1.00 16.64 ? 425 TYR A C   1 
ATOM   3607 O O   . TYR A 1 425 ? -14.423 18.239 8.876   1.00 16.00 ? 425 TYR A O   1 
ATOM   3608 C CB  . TYR A 1 425 ? -15.172 20.810 10.842  1.00 16.73 ? 425 TYR A CB  1 
ATOM   3609 C CG  . TYR A 1 425 ? -14.764 20.857 12.300  1.00 16.59 ? 425 TYR A CG  1 
ATOM   3610 C CD1 . TYR A 1 425 ? -13.472 21.196 12.685  1.00 17.87 ? 425 TYR A CD1 1 
ATOM   3611 C CD2 . TYR A 1 425 ? -15.689 20.573 13.294  1.00 18.90 ? 425 TYR A CD2 1 
ATOM   3612 C CE1 . TYR A 1 425 ? -13.109 21.243 14.031  1.00 19.30 ? 425 TYR A CE1 1 
ATOM   3613 C CE2 . TYR A 1 425 ? -15.342 20.610 14.623  1.00 21.72 ? 425 TYR A CE2 1 
ATOM   3614 C CZ  . TYR A 1 425 ? -14.058 20.946 14.991  1.00 17.63 ? 425 TYR A CZ  1 
ATOM   3615 O OH  . TYR A 1 425 ? -13.740 20.979 16.324  1.00 18.20 ? 425 TYR A OH  1 
ATOM   3616 N N   . TRP A 1 426 ? -15.286 20.013 7.783   1.00 16.19 ? 426 TRP A N   1 
ATOM   3617 C CA  . TRP A 1 426 ? -15.777 19.163 6.703   1.00 15.71 ? 426 TRP A CA  1 
ATOM   3618 C C   . TRP A 1 426 ? -14.624 18.499 5.961   1.00 16.71 ? 426 TRP A C   1 
ATOM   3619 O O   . TRP A 1 426 ? -14.707 17.315 5.610   1.00 17.25 ? 426 TRP A O   1 
ATOM   3620 C CB  . TRP A 1 426 ? -16.661 19.966 5.735   1.00 15.66 ? 426 TRP A CB  1 
ATOM   3621 C CG  . TRP A 1 426 ? -18.004 20.283 6.329   1.00 15.18 ? 426 TRP A CG  1 
ATOM   3622 C CD1 . TRP A 1 426 ? -18.393 21.475 6.854   1.00 15.14 ? 426 TRP A CD1 1 
ATOM   3623 C CD2 . TRP A 1 426 ? -19.122 19.388 6.485   1.00 15.89 ? 426 TRP A CD2 1 
ATOM   3624 N NE1 . TRP A 1 426 ? -19.685 21.389 7.317   1.00 16.11 ? 426 TRP A NE1 1 
ATOM   3625 C CE2 . TRP A 1 426 ? -20.157 20.120 7.100   1.00 16.90 ? 426 TRP A CE2 1 
ATOM   3626 C CE3 . TRP A 1 426 ? -19.349 18.047 6.153   1.00 16.30 ? 426 TRP A CE3 1 
ATOM   3627 C CZ2 . TRP A 1 426 ? -21.404 19.552 7.404   1.00 15.15 ? 426 TRP A CZ2 1 
ATOM   3628 C CZ3 . TRP A 1 426 ? -20.596 17.486 6.444   1.00 15.60 ? 426 TRP A CZ3 1 
ATOM   3629 C CH2 . TRP A 1 426 ? -21.601 18.241 7.068   1.00 15.57 ? 426 TRP A CH2 1 
ATOM   3630 N N   . LYS A 1 427 ? -13.530 19.234 5.732   1.00 18.80 ? 427 LYS A N   1 
ATOM   3631 C CA  . LYS A 1 427 ? -12.352 18.621 5.121   1.00 21.08 ? 427 LYS A CA  1 
ATOM   3632 C C   . LYS A 1 427 ? -11.834 17.463 5.968   1.00 17.97 ? 427 LYS A C   1 
ATOM   3633 O O   . LYS A 1 427 ? -11.489 16.396 5.441   1.00 21.32 ? 427 LYS A O   1 
ATOM   3634 C CB  . LYS A 1 427 ? -11.251 19.661 4.928   1.00 19.49 ? 427 LYS A CB  1 
ATOM   3635 C CG  . LYS A 1 427 ? -11.443 20.591 3.762   1.00 30.37 ? 427 LYS A CG  1 
ATOM   3636 C CD  . LYS A 1 427 ? -10.488 21.778 3.839   1.00 40.74 ? 427 LYS A CD  1 
ATOM   3637 C CE  . LYS A 1 427 ? -9.040  21.328 3.908   1.00 51.42 ? 427 LYS A CE  1 
ATOM   3638 N NZ  . LYS A 1 427 ? -8.603  20.626 2.671   1.00 58.05 ? 427 LYS A NZ  1 
ATOM   3639 N N   . ILE A 1 428 ? -11.744 17.664 7.282   1.00 17.74 ? 428 ILE A N   1 
ATOM   3640 C CA  . ILE A 1 428 ? -11.313 16.580 8.159   1.00 19.81 ? 428 ILE A CA  1 
ATOM   3641 C C   . ILE A 1 428 ? -12.260 15.390 8.058   1.00 20.96 ? 428 ILE A C   1 
ATOM   3642 O O   . ILE A 1 428 ? -11.823 14.239 7.960   1.00 18.19 ? 428 ILE A O   1 
ATOM   3643 C CB  . ILE A 1 428 ? -11.198 17.089 9.604   1.00 17.94 ? 428 ILE A CB  1 
ATOM   3644 C CG1 . ILE A 1 428 ? -10.036 18.075 9.711   1.00 19.26 ? 428 ILE A CG1 1 
ATOM   3645 C CG2 . ILE A 1 428 ? -11.048 15.915 10.569  1.00 20.77 ? 428 ILE A CG2 1 
ATOM   3646 C CD1 . ILE A 1 428 ? -10.052 18.911 10.990  1.00 20.26 ? 428 ILE A CD1 1 
ATOM   3647 N N   . LEU A 1 429 ? -13.567 15.652 8.057   1.00 17.67 ? 429 LEU A N   1 
ATOM   3648 C CA  . LEU A 1 429 ? -14.549 14.573 7.975   1.00 17.87 ? 429 LEU A CA  1 
ATOM   3649 C C   . LEU A 1 429 ? -14.463 13.843 6.642   1.00 18.45 ? 429 LEU A C   1 
ATOM   3650 O O   . LEU A 1 429 ? -14.544 12.608 6.596   1.00 18.48 ? 429 LEU A O   1 
ATOM   3651 C CB  . LEU A 1 429 ? -15.953 15.133 8.188   1.00 17.32 ? 429 LEU A CB  1 
ATOM   3652 C CG  . LEU A 1 429 ? -17.087 14.116 8.214   1.00 19.06 ? 429 LEU A CG  1 
ATOM   3653 C CD1 . LEU A 1 429 ? -17.105 13.408 9.553   1.00 18.51 ? 429 LEU A CD1 1 
ATOM   3654 C CD2 . LEU A 1 429 ? -18.408 14.809 7.938   1.00 18.56 ? 429 LEU A CD2 1 
ATOM   3655 N N   . ILE A 1 430 ? -14.295 14.593 5.549   1.00 16.38 ? 430 ILE A N   1 
ATOM   3656 C CA  . ILE A 1 430 ? -14.209 13.991 4.218   1.00 20.78 ? 430 ILE A CA  1 
ATOM   3657 C C   . ILE A 1 430 ? -13.021 13.040 4.132   1.00 20.23 ? 430 ILE A C   1 
ATOM   3658 O O   . ILE A 1 430 ? -13.142 11.915 3.634   1.00 22.21 ? 430 ILE A O   1 
ATOM   3659 C CB  . ILE A 1 430 ? -14.136 15.092 3.148   1.00 18.03 ? 430 ILE A CB  1 
ATOM   3660 C CG1 . ILE A 1 430 ? -15.497 15.779 3.019   1.00 19.36 ? 430 ILE A CG1 1 
ATOM   3661 C CG2 . ILE A 1 430 ? -13.644 14.528 1.813   1.00 20.80 ? 430 ILE A CG2 1 
ATOM   3662 C CD1 . ILE A 1 430 ? -15.397 17.212 2.488   1.00 19.50 ? 430 ILE A CD1 1 
ATOM   3663 N N   . GLU A 1 431 ? -11.845 13.481 4.601   1.00 20.39 ? 431 GLU A N   1 
ATOM   3664 C CA  . GLU A 1 431 ? -10.669 12.620 4.554   1.00 23.62 ? 431 GLU A CA  1 
ATOM   3665 C C   . GLU A 1 431 ? -10.845 11.404 5.454   1.00 23.67 ? 431 GLU A C   1 
ATOM   3666 O O   . GLU A 1 431 ? -10.473 10.288 5.075   1.00 24.31 ? 431 GLU A O   1 
ATOM   3667 C CB  . GLU A 1 431 ? -9.415  13.402 4.955   1.00 29.59 ? 431 GLU A CB  1 
ATOM   3668 C CG  . GLU A 1 431 ? -8.903  14.351 3.892   1.00 44.70 ? 431 GLU A CG  1 
ATOM   3669 C CD  . GLU A 1 431 ? -8.806  13.705 2.517   1.00 47.24 ? 431 GLU A CD  1 
ATOM   3670 O OE1 . GLU A 1 431 ? -9.560  14.124 1.607   1.00 49.28 ? 431 GLU A OE1 1 
ATOM   3671 O OE2 . GLU A 1 431 ? -7.980  12.779 2.346   1.00 41.63 ? 431 GLU A OE2 1 
ATOM   3672 N N   . ALA A 1 432 ? -11.430 11.599 6.640   1.00 21.49 ? 432 ALA A N   1 
ATOM   3673 C CA  . ALA A 1 432 ? -11.650 10.486 7.556   1.00 22.58 ? 432 ALA A CA  1 
ATOM   3674 C C   . ALA A 1 432 ? -12.620 9.474  6.967   1.00 21.70 ? 432 ALA A C   1 
ATOM   3675 O O   . ALA A 1 432 ? -12.434 8.259  7.120   1.00 24.39 ? 432 ALA A O   1 
ATOM   3676 C CB  . ALA A 1 432 ? -12.180 11.008 8.893   1.00 19.44 ? 432 ALA A CB  1 
ATOM   3677 N N   . LYS A 1 433 ? -13.652 9.961  6.278   1.00 18.33 ? 433 LYS A N   1 
ATOM   3678 C CA  . LYS A 1 433 ? -14.648 9.070  5.695   1.00 20.90 ? 433 LYS A CA  1 
ATOM   3679 C C   . LYS A 1 433 ? -14.014 8.110  4.694   1.00 21.73 ? 433 LYS A C   1 
ATOM   3680 O O   . LYS A 1 433 ? -14.375 6.930  4.643   1.00 23.69 ? 433 LYS A O   1 
ATOM   3681 C CB  . LYS A 1 433 ? -15.752 9.903  5.042   1.00 19.39 ? 433 LYS A CB  1 
ATOM   3682 C CG  . LYS A 1 433 ? -16.815 9.101  4.292   1.00 22.22 ? 433 LYS A CG  1 
ATOM   3683 C CD  . LYS A 1 433 ? -17.591 8.197  5.226   1.00 20.80 ? 433 LYS A CD  1 
ATOM   3684 C CE  . LYS A 1 433 ? -18.559 7.307  4.450   1.00 23.32 ? 433 LYS A CE  1 
ATOM   3685 N NZ  . LYS A 1 433 ? -19.084 6.198  5.297   1.00 21.26 ? 433 LYS A NZ  1 
ATOM   3686 N N   . LYS A 1 434 ? -13.046 8.592  3.905   1.00 21.95 ? 434 LYS A N   1 
ATOM   3687 C CA  . LYS A 1 434 ? -12.365 7.714  2.958   1.00 24.59 ? 434 LYS A CA  1 
ATOM   3688 C C   . LYS A 1 434 ? -11.690 6.542  3.663   1.00 28.00 ? 434 LYS A C   1 
ATOM   3689 O O   . LYS A 1 434 ? -11.514 5.477  3.065   1.00 32.74 ? 434 LYS A O   1 
ATOM   3690 C CB  . LYS A 1 434 ? -11.323 8.499  2.163   1.00 26.65 ? 434 LYS A CB  1 
ATOM   3691 C CG  . LYS A 1 434 ? -11.887 9.633  1.323   1.00 30.50 ? 434 LYS A CG  1 
ATOM   3692 C CD  . LYS A 1 434 ? -10.766 10.311 0.546   1.00 34.99 ? 434 LYS A CD  1 
ATOM   3693 C CE  . LYS A 1 434 ? -11.232 11.592 -0.134  1.00 41.81 ? 434 LYS A CE  1 
ATOM   3694 N NZ  . LYS A 1 434 ? -10.070 12.366 -0.668  1.00 42.80 ? 434 LYS A NZ  1 
ATOM   3695 N N   . LYS A 1 435 ? -11.315 6.721  4.930   1.00 26.57 ? 435 LYS A N   1 
ATOM   3696 C CA  . LYS A 1 435 ? -10.571 5.729  5.695   1.00 29.71 ? 435 LYS A CA  1 
ATOM   3697 C C   . LYS A 1 435 ? -11.389 5.106  6.822   1.00 26.47 ? 435 LYS A C   1 
ATOM   3698 O O   . LYS A 1 435 ? -10.830 4.360  7.635   1.00 27.81 ? 435 LYS A O   1 
ATOM   3699 C CB  . LYS A 1 435 ? -9.302  6.354  6.283   1.00 33.59 ? 435 LYS A CB  1 
ATOM   3700 C CG  . LYS A 1 435 ? -8.245  6.788  5.263   1.00 41.31 ? 435 LYS A CG  1 
ATOM   3701 C CD  . LYS A 1 435 ? -8.102  8.307  5.239   1.00 49.83 ? 435 LYS A CD  1 
ATOM   3702 C CE  . LYS A 1 435 ? -7.964  8.838  3.811   1.00 49.45 ? 435 LYS A CE  1 
ATOM   3703 N NZ  . LYS A 1 435 ? -8.279  10.298 3.698   1.00 51.62 ? 435 LYS A NZ  1 
ATOM   3704 N N   . ALA A 1 436 ? -12.691 5.379  6.880   1.00 24.74 ? 436 ALA A N   1 
ATOM   3705 C CA  . ALA A 1 436 ? -13.493 5.007  8.039   1.00 23.67 ? 436 ALA A CA  1 
ATOM   3706 C C   . ALA A 1 436 ? -13.720 3.504  8.086   1.00 25.73 ? 436 ALA A C   1 
ATOM   3707 O O   . ALA A 1 436 ? -13.918 2.851  7.055   1.00 27.15 ? 436 ALA A O   1 
ATOM   3708 C CB  . ALA A 1 436 ? -14.841 5.736  8.013   1.00 22.85 ? 436 ALA A CB  1 
ATOM   3709 N N   . LYS A 1 437 ? -13.699 2.957  9.301   1.00 28.14 ? 437 LYS A N   1 
ATOM   3710 C CA  . LYS A 1 437 ? -13.899 1.533  9.503   1.00 28.36 ? 437 LYS A CA  1 
ATOM   3711 C C   . LYS A 1 437 ? -15.007 1.203  10.497  1.00 30.19 ? 437 LYS A C   1 
ATOM   3712 O O   . LYS A 1 437 ? -15.280 0.019  10.714  1.00 36.19 ? 437 LYS A O   1 
ATOM   3713 C CB  . LYS A 1 437 ? -12.588 0.873  9.957   1.00 28.23 ? 437 LYS A CB  1 
ATOM   3714 C CG  . LYS A 1 437 ? -11.417 1.090  8.995   1.00 36.24 ? 437 LYS A CG  1 
ATOM   3715 C CD  . LYS A 1 437 ? -11.650 0.382  7.664   1.00 48.93 ? 437 LYS A CD  1 
ATOM   3716 C CE  . LYS A 1 437 ? -10.353 0.148  6.893   1.00 55.97 ? 437 LYS A CE  1 
ATOM   3717 N NZ  . LYS A 1 437 ? -9.875  1.378  6.197   1.00 58.44 ? 437 LYS A NZ  1 
ATOM   3718 N N   . ASN A 1 438 ? -15.655 2.197  11.101  1.00 26.03 ? 438 ASN A N   1 
ATOM   3719 C CA  . ASN A 1 438 ? -16.706 1.914  12.073  1.00 25.17 ? 438 ASN A CA  1 
ATOM   3720 C C   . ASN A 1 438 ? -17.656 3.102  12.166  1.00 26.24 ? 438 ASN A C   1 
ATOM   3721 O O   . ASN A 1 438 ? -17.435 4.158  11.564  1.00 25.79 ? 438 ASN A O   1 
ATOM   3722 C CB  . ASN A 1 438 ? -16.119 1.573  13.446  1.00 24.32 ? 438 ASN A CB  1 
ATOM   3723 C CG  . ASN A 1 438 ? -15.283 2.693  14.017  1.00 21.13 ? 438 ASN A CG  1 
ATOM   3724 O OD1 . ASN A 1 438 ? -15.799 3.767  14.320  1.00 22.58 ? 438 ASN A OD1 1 
ATOM   3725 N ND2 . ASN A 1 438 ? -13.990 2.438  14.208  1.00 24.19 ? 438 ASN A ND2 1 
ATOM   3726 N N   . ASP A 1 439 ? -18.705 2.929  12.971  1.00 24.42 ? 439 ASP A N   1 
ATOM   3727 C CA  . ASP A 1 439 ? -19.781 3.908  13.070  1.00 25.44 ? 439 ASP A CA  1 
ATOM   3728 C C   . ASP A 1 439 ? -19.402 5.150  13.861  1.00 20.28 ? 439 ASP A C   1 
ATOM   3729 O O   . ASP A 1 439 ? -20.242 6.044  14.001  1.00 19.95 ? 439 ASP A O   1 
ATOM   3730 C CB  . ASP A 1 439 ? -21.024 3.259  13.687  1.00 26.47 ? 439 ASP A CB  1 
ATOM   3731 C CG  . ASP A 1 439 ? -21.825 2.450  12.676  1.00 31.10 ? 439 ASP A CG  1 
ATOM   3732 O OD1 . ASP A 1 439 ? -21.497 2.503  11.470  1.00 32.37 ? 439 ASP A OD1 1 
ATOM   3733 O OD2 . ASP A 1 439 ? -22.793 1.765  13.087  1.00 34.12 ? 439 ASP A OD2 1 
ATOM   3734 N N   . TYR A 1 440 ? -18.174 5.263  14.380  1.00 19.69 ? 440 TYR A N   1 
ATOM   3735 C CA  . TYR A 1 440 ? -17.809 6.542  14.977  1.00 16.75 ? 440 TYR A CA  1 
ATOM   3736 C C   . TYR A 1 440 ? -17.783 7.656  13.935  1.00 15.57 ? 440 TYR A C   1 
ATOM   3737 O O   . TYR A 1 440 ? -17.897 8.834  14.296  1.00 17.28 ? 440 TYR A O   1 
ATOM   3738 C CB  . TYR A 1 440 ? -16.474 6.438  15.724  1.00 18.86 ? 440 TYR A CB  1 
ATOM   3739 C CG  . TYR A 1 440 ? -16.673 6.076  17.184  1.00 19.88 ? 440 TYR A CG  1 
ATOM   3740 C CD1 . TYR A 1 440 ? -17.236 6.989  18.064  1.00 26.35 ? 440 TYR A CD1 1 
ATOM   3741 C CD2 . TYR A 1 440 ? -16.353 4.812  17.663  1.00 27.78 ? 440 TYR A CD2 1 
ATOM   3742 C CE1 . TYR A 1 440 ? -17.455 6.670  19.387  1.00 25.64 ? 440 TYR A CE1 1 
ATOM   3743 C CE2 . TYR A 1 440 ? -16.557 4.482  18.999  1.00 26.24 ? 440 TYR A CE2 1 
ATOM   3744 C CZ  . TYR A 1 440 ? -17.117 5.421  19.850  1.00 25.14 ? 440 TYR A CZ  1 
ATOM   3745 O OH  . TYR A 1 440 ? -17.333 5.129  21.183  1.00 33.93 ? 440 TYR A OH  1 
ATOM   3746 N N   . ILE A 1 441 ? -17.678 7.317  12.645  1.00 16.58 ? 441 ILE A N   1 
ATOM   3747 C CA  . ILE A 1 441 ? -17.773 8.359  11.627  1.00 17.03 ? 441 ILE A CA  1 
ATOM   3748 C C   . ILE A 1 441 ? -19.171 8.970  11.632  1.00 16.72 ? 441 ILE A C   1 
ATOM   3749 O O   . ILE A 1 441 ? -19.335 10.161 11.340  1.00 17.24 ? 441 ILE A O   1 
ATOM   3750 C CB  . ILE A 1 441 ? -17.368 7.811  10.234  1.00 17.21 ? 441 ILE A CB  1 
ATOM   3751 C CG1 . ILE A 1 441 ? -17.069 8.961  9.262   1.00 18.75 ? 441 ILE A CG1 1 
ATOM   3752 C CG2 . ILE A 1 441 ? -18.439 6.877  9.654   1.00 17.07 ? 441 ILE A CG2 1 
ATOM   3753 C CD1 . ILE A 1 441 ? -15.744 9.674  9.556   1.00 19.53 ? 441 ILE A CD1 1 
ATOM   3754 N N   . LEU A 1 442 ? -20.189 8.194  12.015  1.00 14.93 ? 442 LEU A N   1 
ATOM   3755 C CA  . LEU A 1 442 ? -21.531 8.754  12.143  1.00 14.77 ? 442 LEU A CA  1 
ATOM   3756 C C   . LEU A 1 442 ? -21.603 9.761  13.287  1.00 15.50 ? 442 LEU A C   1 
ATOM   3757 O O   . LEU A 1 442 ? -22.273 10.794 13.169  1.00 13.94 ? 442 LEU A O   1 
ATOM   3758 C CB  . LEU A 1 442 ? -22.558 7.637  12.341  1.00 15.40 ? 442 LEU A CB  1 
ATOM   3759 C CG  . LEU A 1 442 ? -22.637 6.520  11.296  1.00 17.44 ? 442 LEU A CG  1 
ATOM   3760 C CD1 . LEU A 1 442 ? -23.702 5.515  11.704  1.00 17.14 ? 442 LEU A CD1 1 
ATOM   3761 C CD2 . LEU A 1 442 ? -22.951 7.106  9.904   1.00 16.25 ? 442 LEU A CD2 1 
ATOM   3762 N N   . VAL A 1 443 ? -20.918 9.480  14.403  1.00 13.44 ? 443 VAL A N   1 
ATOM   3763 C CA  . VAL A 1 443 ? -20.899 10.415 15.525  1.00 12.88 ? 443 VAL A CA  1 
ATOM   3764 C C   . VAL A 1 443 ? -20.327 11.756 15.094  1.00 15.11 ? 443 VAL A C   1 
ATOM   3765 O O   . VAL A 1 443 ? -20.832 12.819 15.485  1.00 14.88 ? 443 VAL A O   1 
ATOM   3766 C CB  . VAL A 1 443 ? -20.090 9.831  16.700  1.00 13.55 ? 443 VAL A CB  1 
ATOM   3767 C CG1 . VAL A 1 443 ? -20.194 10.758 17.920  1.00 13.58 ? 443 VAL A CG1 1 
ATOM   3768 C CG2 . VAL A 1 443 ? -20.548 8.410  17.027  1.00 15.38 ? 443 VAL A CG2 1 
ATOM   3769 N N   . ALA A 1 444 ? -19.240 11.727 14.322  1.00 13.79 ? 444 ALA A N   1 
ATOM   3770 C CA  . ALA A 1 444 ? -18.559 12.930 13.862  1.00 16.57 ? 444 ALA A CA  1 
ATOM   3771 C C   . ALA A 1 444 ? -19.374 13.706 12.838  1.00 14.64 ? 444 ALA A C   1 
ATOM   3772 O O   . ALA A 1 444 ? -19.042 14.864 12.563  1.00 14.43 ? 444 ALA A O   1 
ATOM   3773 C CB  . ALA A 1 444 ? -17.189 12.574 13.266  1.00 15.70 ? 444 ALA A CB  1 
ATOM   3774 N N   . GLU A 1 445 ? -20.417 13.101 12.261  1.00 12.98 ? 445 GLU A N   1 
ATOM   3775 C CA  . GLU A 1 445 ? -21.297 13.802 11.338  1.00 13.34 ? 445 GLU A CA  1 
ATOM   3776 C C   . GLU A 1 445 ? -22.375 14.604 12.053  1.00 13.47 ? 445 GLU A C   1 
ATOM   3777 O O   . GLU A 1 445 ? -23.184 15.261 11.386  1.00 13.86 ? 445 GLU A O   1 
ATOM   3778 C CB  . GLU A 1 445 ? -21.932 12.800 10.358  1.00 13.35 ? 445 GLU A CB  1 
ATOM   3779 C CG  . GLU A 1 445 ? -20.915 12.214 9.366   1.00 14.98 ? 445 GLU A CG  1 
ATOM   3780 C CD  . GLU A 1 445 ? -21.334 10.899 8.714   1.00 15.41 ? 445 GLU A CD  1 
ATOM   3781 O OE1 . GLU A 1 445 ? -22.471 10.421 8.924   1.00 16.28 ? 445 GLU A OE1 1 
ATOM   3782 O OE2 . GLU A 1 445 ? -20.509 10.354 7.941   1.00 15.80 ? 445 GLU A OE2 1 
ATOM   3783 N N   . GLY A 1 446 ? -22.416 14.563 13.386  1.00 14.11 ? 446 GLY A N   1 
ATOM   3784 C CA  . GLY A 1 446 ? -23.383 15.369 14.107  1.00 13.00 ? 446 GLY A CA  1 
ATOM   3785 C C   . GLY A 1 446 ? -23.213 16.849 13.812  1.00 13.16 ? 446 GLY A C   1 
ATOM   3786 O O   . GLY A 1 446 ? -22.099 17.348 13.650  1.00 15.09 ? 446 GLY A O   1 
ATOM   3787 N N   . SER A 1 447 ? -24.340 17.566 13.747  1.00 12.73 ? 447 SER A N   1 
ATOM   3788 C CA  . SER A 1 447 ? -24.277 18.983 13.395  1.00 13.44 ? 447 SER A CA  1 
ATOM   3789 C C   . SER A 1 447 ? -23.574 19.815 14.462  1.00 15.21 ? 447 SER A C   1 
ATOM   3790 O O   . SER A 1 447 ? -22.996 20.858 14.136  1.00 13.02 ? 447 SER A O   1 
ATOM   3791 C CB  . SER A 1 447 ? -25.694 19.526 13.152  1.00 13.99 ? 447 SER A CB  1 
ATOM   3792 O OG  . SER A 1 447 ? -26.444 19.564 14.362  1.00 14.06 ? 447 SER A OG  1 
ATOM   3793 N N   . ASP A 1 448 ? -23.591 19.358 15.710  1.00 12.64 ? 448 ASP A N   1 
ATOM   3794 C CA  . ASP A 1 448 ? -23.076 20.167 16.812  1.00 14.18 ? 448 ASP A CA  1 
ATOM   3795 C C   . ASP A 1 448 ? -21.621 20.564 16.605  1.00 14.58 ? 448 ASP A C   1 
ATOM   3796 O O   . ASP A 1 448 ? -21.232 21.699 16.910  1.00 13.68 ? 448 ASP A O   1 
ATOM   3797 C CB  . ASP A 1 448 ? -23.221 19.403 18.126  1.00 14.98 ? 448 ASP A CB  1 
ATOM   3798 C CG  . ASP A 1 448 ? -24.639 18.969 18.383  1.00 13.34 ? 448 ASP A CG  1 
ATOM   3799 O OD1 . ASP A 1 448 ? -25.039 17.930 17.822  1.00 12.73 ? 448 ASP A OD1 1 
ATOM   3800 O OD2 . ASP A 1 448 ? -25.355 19.673 19.118  1.00 13.77 ? 448 ASP A OD2 1 
ATOM   3801 N N   . TRP A 1 449 ? -20.793 19.637 16.125  1.00 12.28 ? 449 TRP A N   1 
ATOM   3802 C CA  . TRP A 1 449 ? -19.360 19.922 16.026  1.00 14.31 ? 449 TRP A CA  1 
ATOM   3803 C C   . TRP A 1 449 ? -19.113 21.105 15.109  1.00 13.05 ? 449 TRP A C   1 
ATOM   3804 O O   . TRP A 1 449 ? -18.305 21.985 15.417  1.00 13.74 ? 449 TRP A O   1 
ATOM   3805 C CB  . TRP A 1 449 ? -18.605 18.693 15.528  1.00 16.65 ? 449 TRP A CB  1 
ATOM   3806 C CG  . TRP A 1 449 ? -19.087 17.426 16.151  1.00 12.96 ? 449 TRP A CG  1 
ATOM   3807 C CD1 . TRP A 1 449 ? -19.646 16.367 15.503  1.00 15.36 ? 449 TRP A CD1 1 
ATOM   3808 C CD2 . TRP A 1 449 ? -19.088 17.095 17.547  1.00 14.07 ? 449 TRP A CD2 1 
ATOM   3809 N NE1 . TRP A 1 449 ? -19.980 15.392 16.397  1.00 13.47 ? 449 TRP A NE1 1 
ATOM   3810 C CE2 . TRP A 1 449 ? -19.646 15.808 17.662  1.00 14.01 ? 449 TRP A CE2 1 
ATOM   3811 C CE3 . TRP A 1 449 ? -18.649 17.752 18.711  1.00 15.50 ? 449 TRP A CE3 1 
ATOM   3812 C CZ2 . TRP A 1 449 ? -19.805 15.165 18.889  1.00 12.99 ? 449 TRP A CZ2 1 
ATOM   3813 C CZ3 . TRP A 1 449 ? -18.808 17.111 19.935  1.00 15.92 ? 449 TRP A CZ3 1 
ATOM   3814 C CH2 . TRP A 1 449 ? -19.376 15.832 20.017  1.00 13.27 ? 449 TRP A CH2 1 
ATOM   3815 N N   . PHE A 1 450 ? -19.871 21.184 14.015  1.00 14.57 ? 450 PHE A N   1 
ATOM   3816 C CA  . PHE A 1 450 ? -19.698 22.260 13.049  1.00 14.13 ? 450 PHE A CA  1 
ATOM   3817 C C   . PHE A 1 450 ? -20.304 23.564 13.539  1.00 15.43 ? 450 PHE A C   1 
ATOM   3818 O O   . PHE A 1 450 ? -19.834 24.643 13.167  1.00 18.62 ? 450 PHE A O   1 
ATOM   3819 C CB  . PHE A 1 450 ? -20.320 21.846 11.708  1.00 13.85 ? 450 PHE A CB  1 
ATOM   3820 C CG  . PHE A 1 450 ? -19.846 20.498 11.224  1.00 13.44 ? 450 PHE A CG  1 
ATOM   3821 C CD1 . PHE A 1 450 ? -20.460 19.326 11.665  1.00 15.05 ? 450 PHE A CD1 1 
ATOM   3822 C CD2 . PHE A 1 450 ? -18.776 20.400 10.343  1.00 14.92 ? 450 PHE A CD2 1 
ATOM   3823 C CE1 . PHE A 1 450 ? -20.013 18.089 11.240  1.00 15.11 ? 450 PHE A CE1 1 
ATOM   3824 C CE2 . PHE A 1 450 ? -18.315 19.158 9.920   1.00 16.36 ? 450 PHE A CE2 1 
ATOM   3825 C CZ  . PHE A 1 450 ? -18.940 18.007 10.358  1.00 15.23 ? 450 PHE A CZ  1 
ATOM   3826 N N   . TRP A 1 451 ? -21.339 23.472 14.373  1.00 14.75 ? 451 TRP A N   1 
ATOM   3827 C CA  . TRP A 1 451 ? -21.980 24.655 14.936  1.00 14.95 ? 451 TRP A CA  1 
ATOM   3828 C C   . TRP A 1 451 ? -20.991 25.477 15.753  1.00 15.69 ? 451 TRP A C   1 
ATOM   3829 O O   . TRP A 1 451 ? -20.922 26.706 15.619  1.00 19.06 ? 451 TRP A O   1 
ATOM   3830 C CB  . TRP A 1 451 ? -23.158 24.201 15.798  1.00 16.27 ? 451 TRP A CB  1 
ATOM   3831 C CG  . TRP A 1 451 ? -23.815 25.243 16.629  1.00 17.53 ? 451 TRP A CG  1 
ATOM   3832 C CD1 . TRP A 1 451 ? -23.526 25.566 17.923  1.00 18.01 ? 451 TRP A CD1 1 
ATOM   3833 C CD2 . TRP A 1 451 ? -24.912 26.073 16.241  1.00 21.03 ? 451 TRP A CD2 1 
ATOM   3834 N NE1 . TRP A 1 451 ? -24.365 26.564 18.360  1.00 20.78 ? 451 TRP A NE1 1 
ATOM   3835 C CE2 . TRP A 1 451 ? -25.228 26.892 17.343  1.00 23.72 ? 451 TRP A CE2 1 
ATOM   3836 C CE3 . TRP A 1 451 ? -25.655 26.210 15.062  1.00 23.42 ? 451 TRP A CE3 1 
ATOM   3837 C CZ2 . TRP A 1 451 ? -26.253 27.836 17.303  1.00 24.83 ? 451 TRP A CZ2 1 
ATOM   3838 C CZ3 . TRP A 1 451 ? -26.669 27.153 15.022  1.00 26.16 ? 451 TRP A CZ3 1 
ATOM   3839 C CH2 . TRP A 1 451 ? -26.958 27.954 16.134  1.00 26.14 ? 451 TRP A CH2 1 
ATOM   3840 N N   . TRP A 1 452 ? -20.209 24.805 16.603  1.00 16.63 ? 452 TRP A N   1 
ATOM   3841 C CA  . TRP A 1 452 ? -19.304 25.487 17.521  1.00 16.10 ? 452 TRP A CA  1 
ATOM   3842 C C   . TRP A 1 452 ? -18.002 25.903 16.867  1.00 18.06 ? 452 TRP A C   1 
ATOM   3843 O O   . TRP A 1 452 ? -17.333 26.815 17.375  1.00 18.85 ? 452 TRP A O   1 
ATOM   3844 C CB  . TRP A 1 452 ? -19.002 24.588 18.725  1.00 15.61 ? 452 TRP A CB  1 
ATOM   3845 C CG  . TRP A 1 452 ? -20.231 24.297 19.506  1.00 15.33 ? 452 TRP A CG  1 
ATOM   3846 C CD1 . TRP A 1 452 ? -20.837 23.080 19.657  1.00 16.12 ? 452 TRP A CD1 1 
ATOM   3847 C CD2 . TRP A 1 452 ? -21.060 25.245 20.188  1.00 16.23 ? 452 TRP A CD2 1 
ATOM   3848 N NE1 . TRP A 1 452 ? -21.976 23.213 20.403  1.00 15.07 ? 452 TRP A NE1 1 
ATOM   3849 C CE2 . TRP A 1 452 ? -22.137 24.530 20.747  1.00 15.81 ? 452 TRP A CE2 1 
ATOM   3850 C CE3 . TRP A 1 452 ? -20.992 26.626 20.388  1.00 17.57 ? 452 TRP A CE3 1 
ATOM   3851 C CZ2 . TRP A 1 452 ? -23.141 25.148 21.487  1.00 17.21 ? 452 TRP A CZ2 1 
ATOM   3852 C CZ3 . TRP A 1 452 ? -21.994 27.243 21.132  1.00 18.43 ? 452 TRP A CZ3 1 
ATOM   3853 C CH2 . TRP A 1 452 ? -23.049 26.502 21.677  1.00 20.68 ? 452 TRP A CH2 1 
ATOM   3854 N N   . GLN A 1 453 ? -17.634 25.265 15.762  1.00 18.27 ? 453 GLN A N   1 
ATOM   3855 C CA  . GLN A 1 453 ? -16.392 25.590 15.078  1.00 19.99 ? 453 GLN A CA  1 
ATOM   3856 C C   . GLN A 1 453 ? -16.516 26.935 14.370  1.00 20.43 ? 453 GLN A C   1 
ATOM   3857 O O   . GLN A 1 453 ? -17.576 27.287 13.843  1.00 24.13 ? 453 GLN A O   1 
ATOM   3858 C CB  . GLN A 1 453 ? -16.048 24.470 14.086  1.00 19.77 ? 453 GLN A CB  1 
ATOM   3859 C CG  . GLN A 1 453 ? -14.913 24.772 13.133  1.00 21.33 ? 453 GLN A CG  1 
ATOM   3860 C CD  . GLN A 1 453 ? -13.539 24.619 13.778  1.00 23.96 ? 453 GLN A CD  1 
ATOM   3861 O OE1 . GLN A 1 453 ? -13.415 24.645 14.999  1.00 25.50 ? 453 GLN A OE1 1 
ATOM   3862 N NE2 . GLN A 1 453 ? -12.503 24.468 12.955  1.00 26.46 ? 453 GLN A NE2 1 
ATOM   3863 N N   . GLY A 1 454 ? -15.437 27.709 14.390  1.00 26.81 ? 454 GLY A N   1 
ATOM   3864 C CA  . GLY A 1 454 ? -15.427 28.959 13.651  1.00 24.73 ? 454 GLY A CA  1 
ATOM   3865 C C   . GLY A 1 454 ? -16.337 30.026 14.214  1.00 32.38 ? 454 GLY A C   1 
ATOM   3866 O O   . GLY A 1 454 ? -16.979 30.760 13.446  1.00 30.57 ? 454 GLY A O   1 
ATOM   3867 N N   . GLU A 1 455 ? -16.411 30.124 15.539  1.00 28.19 ? 455 GLU A N   1 
ATOM   3868 C CA  . GLU A 1 455 ? -17.219 31.112 16.236  1.00 31.99 ? 455 GLU A CA  1 
ATOM   3869 C C   . GLU A 1 455 ? -16.331 31.843 17.233  1.00 35.59 ? 455 GLU A C   1 
ATOM   3870 O O   . GLU A 1 455 ? -15.304 31.312 17.667  1.00 37.12 ? 455 GLU A O   1 
ATOM   3871 C CB  . GLU A 1 455 ? -18.407 30.454 16.966  1.00 29.13 ? 455 GLU A CB  1 
ATOM   3872 C CG  . GLU A 1 455 ? -19.320 29.633 16.072  1.00 28.96 ? 455 GLU A CG  1 
ATOM   3873 C CD  . GLU A 1 455 ? -20.150 30.499 15.145  1.00 30.99 ? 455 GLU A CD  1 
ATOM   3874 O OE1 . GLU A 1 455 ? -20.270 31.719 15.410  1.00 33.91 ? 455 GLU A OE1 1 
ATOM   3875 O OE2 . GLU A 1 455 ? -20.679 29.966 14.147  1.00 29.09 ? 455 GLU A OE2 1 
ATOM   3876 N N   . GLU A 1 456 ? -16.729 33.067 17.588  1.00 38.53 ? 456 GLU A N   1 
ATOM   3877 C CA  . GLU A 1 456 ? -15.932 33.872 18.509  1.00 51.91 ? 456 GLU A CA  1 
ATOM   3878 C C   . GLU A 1 456 ? -15.705 33.115 19.815  1.00 58.29 ? 456 GLU A C   1 
ATOM   3879 O O   . GLU A 1 456 ? -16.644 32.562 20.395  1.00 57.54 ? 456 GLU A O   1 
ATOM   3880 C CB  . GLU A 1 456 ? -16.606 35.222 18.773  1.00 56.04 ? 456 GLU A CB  1 
ATOM   3881 C CG  . GLU A 1 456 ? -18.124 35.224 18.672  1.00 60.62 ? 456 GLU A CG  1 
ATOM   3882 C CD  . GLU A 1 456 ? -18.706 36.629 18.602  1.00 69.34 ? 456 GLU A CD  1 
ATOM   3883 O OE1 . GLU A 1 456 ? -19.605 36.945 19.411  1.00 71.38 ? 456 GLU A OE1 1 
ATOM   3884 O OE2 . GLU A 1 456 ? -18.266 37.419 17.737  1.00 72.88 ? 456 GLU A OE2 1 
ATOM   3885 N N   . LYS A 1 457 ? -14.443 33.098 20.259  1.00 58.69 ? 457 LYS A N   1 
ATOM   3886 C CA  . LYS A 1 457 ? -13.971 32.259 21.359  1.00 58.34 ? 457 LYS A CA  1 
ATOM   3887 C C   . LYS A 1 457 ? -14.950 32.221 22.525  1.00 58.75 ? 457 LYS A C   1 
ATOM   3888 O O   . LYS A 1 457 ? -15.550 33.235 22.890  1.00 60.24 ? 457 LYS A O   1 
ATOM   3889 C CB  . LYS A 1 457 ? -12.612 32.774 21.847  1.00 62.70 ? 457 LYS A CB  1 
ATOM   3890 C CG  . LYS A 1 457 ? -12.475 34.292 21.765  1.00 68.56 ? 457 LYS A CG  1 
ATOM   3891 C CD  . LYS A 1 457 ? -11.094 34.770 22.200  1.00 71.58 ? 457 LYS A CD  1 
ATOM   3892 C CE  . LYS A 1 457 ? -11.042 35.056 23.694  1.00 70.83 ? 457 LYS A CE  1 
ATOM   3893 N NZ  . LYS A 1 457 ? -9.667  34.893 24.241  1.00 71.32 ? 457 LYS A NZ  1 
ATOM   3894 N N   . ALA A 1 458 ? -15.093 31.039 23.114  1.00 57.15 ? 458 ALA A N   1 
ATOM   3895 C CA  . ALA A 1 458 ? -15.968 30.827 24.257  1.00 59.08 ? 458 ALA A CA  1 
ATOM   3896 C C   . ALA A 1 458 ? -15.382 29.710 25.104  1.00 56.64 ? 458 ALA A C   1 
ATOM   3897 O O   . ALA A 1 458 ? -14.605 28.888 24.601  1.00 57.75 ? 458 ALA A O   1 
ATOM   3898 C CB  . ALA A 1 458 ? -17.394 30.474 23.813  1.00 56.96 ? 458 ALA A CB  1 
ATOM   3899 N N   . PRO A 1 459 ? -15.712 29.662 26.396  1.00 48.84 ? 459 PRO A N   1 
ATOM   3900 C CA  . PRO A 1 459 ? -15.281 28.518 27.209  1.00 43.23 ? 459 PRO A CA  1 
ATOM   3901 C C   . PRO A 1 459 ? -15.864 27.212 26.681  1.00 45.02 ? 459 PRO A C   1 
ATOM   3902 O O   . PRO A 1 459 ? -16.979 27.169 26.153  1.00 41.12 ? 459 PRO A O   1 
ATOM   3903 C CB  . PRO A 1 459 ? -15.805 28.854 28.614  1.00 45.07 ? 459 PRO A CB  1 
ATOM   3904 C CG  . PRO A 1 459 ? -16.717 30.040 28.453  1.00 46.99 ? 459 PRO A CG  1 
ATOM   3905 C CD  . PRO A 1 459 ? -16.270 30.751 27.216  1.00 50.67 ? 459 PRO A CD  1 
ATOM   3906 N N   . PHE A 1 460 ? -15.068 26.150 26.787  1.00 47.00 ? 460 PHE A N   1 
ATOM   3907 C CA  . PHE A 1 460 ? -15.377 24.752 26.460  1.00 38.66 ? 460 PHE A CA  1 
ATOM   3908 C C   . PHE A 1 460 ? -15.434 24.431 24.964  1.00 30.61 ? 460 PHE A C   1 
ATOM   3909 O O   . PHE A 1 460 ? -15.586 23.251 24.638  1.00 29.42 ? 460 PHE A O   1 
ATOM   3910 C CB  . PHE A 1 460 ? -16.688 24.272 27.106  1.00 33.74 ? 460 PHE A CB  1 
ATOM   3911 C CG  . PHE A 1 460 ? -16.778 24.565 28.575  1.00 35.46 ? 460 PHE A CG  1 
ATOM   3912 C CD1 . PHE A 1 460 ? -15.666 24.428 29.395  1.00 36.90 ? 460 PHE A CD1 1 
ATOM   3913 C CD2 . PHE A 1 460 ? -17.965 25.002 29.138  1.00 42.62 ? 460 PHE A CD2 1 
ATOM   3914 C CE1 . PHE A 1 460 ? -15.736 24.708 30.745  1.00 43.54 ? 460 PHE A CE1 1 
ATOM   3915 C CE2 . PHE A 1 460 ? -18.040 25.284 30.494  1.00 42.93 ? 460 PHE A CE2 1 
ATOM   3916 C CZ  . PHE A 1 460 ? -16.922 25.138 31.296  1.00 43.63 ? 460 PHE A CZ  1 
ATOM   3917 N N   . VAL A 1 461 ? -15.283 25.397 24.047  1.00 29.04 ? 461 VAL A N   1 
ATOM   3918 C CA  . VAL A 1 461 ? -15.206 25.046 22.627  1.00 26.28 ? 461 VAL A CA  1 
ATOM   3919 C C   . VAL A 1 461 ? -14.075 24.057 22.385  1.00 28.66 ? 461 VAL A C   1 
ATOM   3920 O O   . VAL A 1 461 ? -14.183 23.153 21.545  1.00 26.02 ? 461 VAL A O   1 
ATOM   3921 C CB  . VAL A 1 461 ? -15.044 26.298 21.740  1.00 28.25 ? 461 VAL A CB  1 
ATOM   3922 C CG1 . VAL A 1 461 ? -13.747 27.040 22.045  1.00 37.30 ? 461 VAL A CG1 1 
ATOM   3923 C CG2 . VAL A 1 461 ? -15.065 25.896 20.275  1.00 30.48 ? 461 VAL A CG2 1 
ATOM   3924 N N   . GLU A 1 462 ? -12.979 24.199 23.128  1.00 23.12 ? 462 GLU A N   1 
ATOM   3925 C CA  . GLU A 1 462 ? -11.886 23.248 23.011  1.00 24.46 ? 462 GLU A CA  1 
ATOM   3926 C C   . GLU A 1 462 ? -12.343 21.833 23.329  1.00 24.63 ? 462 GLU A C   1 
ATOM   3927 O O   . GLU A 1 462 ? -11.768 20.868 22.815  1.00 23.17 ? 462 GLU A O   1 
ATOM   3928 C CB  . GLU A 1 462 ? -10.739 23.655 23.934  1.00 27.97 ? 462 GLU A CB  1 
ATOM   3929 C CG  . GLU A 1 462 ? -10.144 25.030 23.656  1.00 39.94 ? 462 GLU A CG  1 
ATOM   3930 C CD  . GLU A 1 462 ? -10.909 26.165 24.329  1.00 42.39 ? 462 GLU A CD  1 
ATOM   3931 O OE1 . GLU A 1 462 ? -11.921 25.900 25.025  1.00 30.03 ? 462 GLU A OE1 1 
ATOM   3932 O OE2 . GLU A 1 462 ? -10.493 27.329 24.154  1.00 43.87 ? 462 GLU A OE2 1 
ATOM   3933 N N   . VAL A 1 463 ? -13.366 21.682 24.178  1.00 19.53 ? 463 VAL A N   1 
ATOM   3934 C CA  . VAL A 1 463 ? -13.838 20.340 24.505  1.00 17.96 ? 463 VAL A CA  1 
ATOM   3935 C C   . VAL A 1 463 ? -14.629 19.750 23.340  1.00 18.10 ? 463 VAL A C   1 
ATOM   3936 O O   . VAL A 1 463 ? -14.472 18.572 23.003  1.00 17.94 ? 463 VAL A O   1 
ATOM   3937 C CB  . VAL A 1 463 ? -14.668 20.352 25.799  1.00 19.94 ? 463 VAL A CB  1 
ATOM   3938 C CG1 . VAL A 1 463 ? -15.048 18.934 26.168  1.00 24.98 ? 463 VAL A CG1 1 
ATOM   3939 C CG2 . VAL A 1 463 ? -13.882 21.004 26.928  1.00 20.45 ? 463 VAL A CG2 1 
ATOM   3940 N N   . PHE A 1 464 ? -15.488 20.548 22.705  1.00 15.85 ? 464 PHE A N   1 
ATOM   3941 C CA  . PHE A 1 464 ? -16.199 20.051 21.531  1.00 14.77 ? 464 PHE A CA  1 
ATOM   3942 C C   . PHE A 1 464 ? -15.212 19.656 20.442  1.00 14.67 ? 464 PHE A C   1 
ATOM   3943 O O   . PHE A 1 464 ? -15.394 18.642 19.760  1.00 16.66 ? 464 PHE A O   1 
ATOM   3944 C CB  . PHE A 1 464 ? -17.177 21.110 21.009  1.00 15.19 ? 464 PHE A CB  1 
ATOM   3945 C CG  . PHE A 1 464 ? -18.378 21.303 21.883  1.00 14.72 ? 464 PHE A CG  1 
ATOM   3946 C CD1 . PHE A 1 464 ? -19.514 20.535 21.683  1.00 14.30 ? 464 PHE A CD1 1 
ATOM   3947 C CD2 . PHE A 1 464 ? -18.378 22.248 22.898  1.00 15.75 ? 464 PHE A CD2 1 
ATOM   3948 C CE1 . PHE A 1 464 ? -20.619 20.695 22.489  1.00 14.37 ? 464 PHE A CE1 1 
ATOM   3949 C CE2 . PHE A 1 464 ? -19.495 22.411 23.717  1.00 16.09 ? 464 PHE A CE2 1 
ATOM   3950 C CZ  . PHE A 1 464 ? -20.618 21.639 23.496  1.00 15.39 ? 464 PHE A CZ  1 
ATOM   3951 N N   . ASP A 1 465 ? -14.128 20.425 20.297  1.00 15.83 ? 465 ASP A N   1 
ATOM   3952 C CA  . ASP A 1 465 ? -13.138 20.108 19.273  1.00 15.77 ? 465 ASP A CA  1 
ATOM   3953 C C   . ASP A 1 465 ? -12.374 18.833 19.625  1.00 15.95 ? 465 ASP A C   1 
ATOM   3954 O O   . ASP A 1 465 ? -12.099 18.004 18.747  1.00 19.04 ? 465 ASP A O   1 
ATOM   3955 C CB  . ASP A 1 465 ? -12.183 21.289 19.094  1.00 17.10 ? 465 ASP A CB  1 
ATOM   3956 C CG  . ASP A 1 465 ? -11.009 20.957 18.200  1.00 21.86 ? 465 ASP A CG  1 
ATOM   3957 O OD1 . ASP A 1 465 ? -11.155 21.011 16.960  1.00 21.24 ? 465 ASP A OD1 1 
ATOM   3958 O OD2 . ASP A 1 465 ? -9.940  20.626 18.744  1.00 18.53 ? 465 ASP A OD2 1 
ATOM   3959 N N   . LYS A 1 466 ? -12.016 18.660 20.903  1.00 16.56 ? 466 LYS A N   1 
ATOM   3960 C CA  . LYS A 1 466 ? -11.387 17.414 21.332  1.00 17.63 ? 466 LYS A CA  1 
ATOM   3961 C C   . LYS A 1 466 ? -12.282 16.219 21.044  1.00 17.52 ? 466 LYS A C   1 
ATOM   3962 O O   . LYS A 1 466 ? -11.813 15.185 20.554  1.00 20.44 ? 466 LYS A O   1 
ATOM   3963 C CB  . LYS A 1 466 ? -11.053 17.472 22.820  1.00 19.03 ? 466 LYS A CB  1 
ATOM   3964 C CG  . LYS A 1 466 ? -10.522 16.158 23.389  1.00 21.50 ? 466 LYS A CG  1 
ATOM   3965 C CD  . LYS A 1 466 ? -9.888  16.354 24.762  1.00 24.54 ? 466 LYS A CD  1 
ATOM   3966 C CE  . LYS A 1 466 ? -9.074  15.129 25.148  1.00 37.49 ? 466 LYS A CE  1 
ATOM   3967 N NZ  . LYS A 1 466 ? -7.767  15.504 25.756  1.00 49.48 ? 466 LYS A NZ  1 
ATOM   3968 N N   . LEU A 1 467 ? -13.579 16.341 21.336  1.00 16.35 ? 467 LEU A N   1 
ATOM   3969 C CA  . LEU A 1 467 ? -14.500 15.241 21.074  1.00 17.05 ? 467 LEU A CA  1 
ATOM   3970 C C   . LEU A 1 467 ? -14.590 14.935 19.580  1.00 17.69 ? 467 LEU A C   1 
ATOM   3971 O O   . LEU A 1 467 ? -14.436 13.778 19.161  1.00 16.47 ? 467 LEU A O   1 
ATOM   3972 C CB  . LEU A 1 467 ? -15.883 15.567 21.647  1.00 16.67 ? 467 LEU A CB  1 
ATOM   3973 C CG  . LEU A 1 467 ? -15.993 15.469 23.172  1.00 18.90 ? 467 LEU A CG  1 
ATOM   3974 C CD1 . LEU A 1 467 ? -17.234 16.195 23.700  1.00 14.73 ? 467 LEU A CD1 1 
ATOM   3975 C CD2 . LEU A 1 467 ? -16.000 14.010 23.621  1.00 17.95 ? 467 LEU A CD2 1 
ATOM   3976 N N   . PHE A 1 468 ? -14.841 15.962 18.763  1.00 15.47 ? 468 PHE A N   1 
ATOM   3977 C CA  . PHE A 1 468 ? -14.962 15.757 17.320  1.00 16.03 ? 468 PHE A CA  1 
ATOM   3978 C C   . PHE A 1 468 ? -13.729 15.049 16.775  1.00 17.21 ? 468 PHE A C   1 
ATOM   3979 O O   . PHE A 1 468 ? -13.834 14.046 16.055  1.00 17.25 ? 468 PHE A O   1 
ATOM   3980 C CB  . PHE A 1 468 ? -15.172 17.098 16.605  1.00 15.06 ? 468 PHE A CB  1 
ATOM   3981 C CG  . PHE A 1 468 ? -15.061 17.013 15.104  1.00 13.43 ? 468 PHE A CG  1 
ATOM   3982 C CD1 . PHE A 1 468 ? -16.124 16.526 14.352  1.00 14.06 ? 468 PHE A CD1 1 
ATOM   3983 C CD2 . PHE A 1 468 ? -13.921 17.429 14.446  1.00 15.97 ? 468 PHE A CD2 1 
ATOM   3984 C CE1 . PHE A 1 468 ? -16.041 16.438 12.992  1.00 14.83 ? 468 PHE A CE1 1 
ATOM   3985 C CE2 . PHE A 1 468 ? -13.823 17.358 13.060  1.00 16.18 ? 468 PHE A CE2 1 
ATOM   3986 C CZ  . PHE A 1 468 ? -14.903 16.857 12.326  1.00 14.60 ? 468 PHE A CZ  1 
ATOM   3987 N N   . ARG A 1 469 ? -12.546 15.532 17.153  1.00 15.38 ? 469 ARG A N   1 
ATOM   3988 C CA  . ARG A 1 469 ? -11.332 14.959 16.599  1.00 15.89 ? 469 ARG A CA  1 
ATOM   3989 C C   . ARG A 1 469 ? -11.089 13.559 17.142  1.00 17.22 ? 469 ARG A C   1 
ATOM   3990 O O   . ARG A 1 469 ? -10.545 12.708 16.430  1.00 20.10 ? 469 ARG A O   1 
ATOM   3991 C CB  . ARG A 1 469 ? -10.152 15.890 16.881  1.00 17.30 ? 469 ARG A CB  1 
ATOM   3992 C CG  . ARG A 1 469 ? -10.232 17.166 16.024  1.00 21.43 ? 469 ARG A CG  1 
ATOM   3993 C CD  . ARG A 1 469 ? -9.175  18.183 16.432  1.00 22.07 ? 469 ARG A CD  1 
ATOM   3994 N NE  . ARG A 1 469 ? -9.189  19.399 15.610  1.00 22.67 ? 469 ARG A NE  1 
ATOM   3995 C CZ  . ARG A 1 469 ? -8.555  19.534 14.446  1.00 25.45 ? 469 ARG A CZ  1 
ATOM   3996 N NH1 . ARG A 1 469 ? -7.858  18.526 13.936  1.00 24.20 ? 469 ARG A NH1 1 
ATOM   3997 N NH2 . ARG A 1 469 ? -8.613  20.685 13.786  1.00 27.61 ? 469 ARG A NH2 1 
ATOM   3998 N N   . SER A 1 470 ? -11.522 13.288 18.377  1.00 17.81 ? 470 SER A N   1 
ATOM   3999 C CA  . SER A 1 470 ? -11.388 11.942 18.922  1.00 18.42 ? 470 SER A CA  1 
ATOM   4000 C C   . SER A 1 470 ? -12.297 10.955 18.198  1.00 20.69 ? 470 SER A C   1 
ATOM   4001 O O   . SER A 1 470 ? -11.896 9.808  17.943  1.00 20.14 ? 470 SER A O   1 
ATOM   4002 C CB  . SER A 1 470 ? -11.685 11.947 20.420  1.00 24.09 ? 470 SER A CB  1 
ATOM   4003 O OG  . SER A 1 470 ? -10.667 12.628 21.125  1.00 35.56 ? 470 SER A OG  1 
ATOM   4004 N N   . PHE A 1 471 ? -13.524 11.374 17.867  1.00 19.25 ? 471 PHE A N   1 
ATOM   4005 C CA  . PHE A 1 471 ? -14.421 10.492 17.127  1.00 15.63 ? 471 PHE A CA  1 
ATOM   4006 C C   . PHE A 1 471 ? -13.894 10.245 15.722  1.00 18.49 ? 471 PHE A C   1 
ATOM   4007 O O   . PHE A 1 471 ? -13.962 9.119  15.213  1.00 18.62 ? 471 PHE A O   1 
ATOM   4008 C CB  . PHE A 1 471 ? -15.828 11.085 17.068  1.00 15.47 ? 471 PHE A CB  1 
ATOM   4009 C CG  . PHE A 1 471 ? -16.504 11.187 18.412  1.00 16.58 ? 471 PHE A CG  1 
ATOM   4010 C CD1 . PHE A 1 471 ? -16.501 10.119 19.297  1.00 17.83 ? 471 PHE A CD1 1 
ATOM   4011 C CD2 . PHE A 1 471 ? -17.129 12.362 18.789  1.00 15.06 ? 471 PHE A CD2 1 
ATOM   4012 C CE1 . PHE A 1 471 ? -17.131 10.223 20.547  1.00 18.36 ? 471 PHE A CE1 1 
ATOM   4013 C CE2 . PHE A 1 471 ? -17.757 12.476 20.021  1.00 16.53 ? 471 PHE A CE2 1 
ATOM   4014 C CZ  . PHE A 1 471 ? -17.760 11.406 20.902  1.00 18.41 ? 471 PHE A CZ  1 
ATOM   4015 N N   . VAL A 1 472 ? -13.355 11.287 15.088  1.00 16.88 ? 472 VAL A N   1 
ATOM   4016 C CA  . VAL A 1 472 ? -12.759 11.135 13.763  1.00 18.88 ? 472 VAL A CA  1 
ATOM   4017 C C   . VAL A 1 472 ? -11.594 10.152 13.800  1.00 20.17 ? 472 VAL A C   1 
ATOM   4018 O O   . VAL A 1 472 ? -11.448 9.301  12.910  1.00 20.22 ? 472 VAL A O   1 
ATOM   4019 C CB  . VAL A 1 472 ? -12.336 12.514 13.223  1.00 19.87 ? 472 VAL A CB  1 
ATOM   4020 C CG1 . VAL A 1 472 ? -11.384 12.366 12.050  1.00 24.10 ? 472 VAL A CG1 1 
ATOM   4021 C CG2 . VAL A 1 472 ? -13.571 13.321 12.820  1.00 19.60 ? 472 VAL A CG2 1 
ATOM   4022 N N   . ARG A 1 473 ? -10.744 10.244 14.825  1.00 18.31 ? 473 ARG A N   1 
ATOM   4023 C CA  . ARG A 1 473 ? -9.626  9.311  14.923  1.00 20.06 ? 473 ARG A CA  1 
ATOM   4024 C C   . ARG A 1 473 ? -10.126 7.892  15.167  1.00 22.14 ? 473 ARG A C   1 
ATOM   4025 O O   . ARG A 1 473 ? -9.693  6.940  14.505  1.00 21.19 ? 473 ARG A O   1 
ATOM   4026 C CB  . ARG A 1 473 ? -8.685  9.750  16.044  1.00 21.21 ? 473 ARG A CB  1 
ATOM   4027 C CG  . ARG A 1 473 ? -7.568  8.768  16.333  1.00 29.48 ? 473 ARG A CG  1 
ATOM   4028 C CD  . ARG A 1 473 ? -6.350  9.483  16.890  1.00 45.35 ? 473 ARG A CD  1 
ATOM   4029 N NE  . ARG A 1 473 ? -6.474  9.780  18.316  1.00 49.52 ? 473 ARG A NE  1 
ATOM   4030 C CZ  . ARG A 1 473 ? -6.232  8.908  19.292  1.00 59.25 ? 473 ARG A CZ  1 
ATOM   4031 N NH1 . ARG A 1 473 ? -5.849  7.670  19.003  1.00 59.75 ? 473 ARG A NH1 1 
ATOM   4032 N NH2 . ARG A 1 473 ? -6.368  9.274  20.561  1.00 56.97 ? 473 ARG A NH2 1 
ATOM   4033 N N   . ARG A 1 474 ? -11.047 7.741  16.122  1.00 21.52 ? 474 ARG A N   1 
ATOM   4034 C CA  . ARG A 1 474 ? -11.565 6.424  16.473  1.00 23.02 ? 474 ARG A CA  1 
ATOM   4035 C C   . ARG A 1 474 ? -12.265 5.769  15.292  1.00 20.90 ? 474 ARG A C   1 
ATOM   4036 O O   . ARG A 1 474 ? -12.217 4.541  15.144  1.00 23.78 ? 474 ARG A O   1 
ATOM   4037 C CB  . ARG A 1 474 ? -12.519 6.558  17.663  1.00 22.11 ? 474 ARG A CB  1 
ATOM   4038 C CG  . ARG A 1 474 ? -13.056 5.244  18.183  1.00 28.83 ? 474 ARG A CG  1 
ATOM   4039 C CD  . ARG A 1 474 ? -12.048 4.535  19.071  1.00 35.19 ? 474 ARG A CD  1 
ATOM   4040 N NE  . ARG A 1 474 ? -12.609 3.307  19.629  1.00 40.86 ? 474 ARG A NE  1 
ATOM   4041 C CZ  . ARG A 1 474 ? -12.848 2.200  18.930  1.00 53.46 ? 474 ARG A CZ  1 
ATOM   4042 N NH1 . ARG A 1 474 ? -12.556 2.146  17.638  1.00 54.27 ? 474 ARG A NH1 1 
ATOM   4043 N NH2 . ARG A 1 474 ? -13.373 1.138  19.529  1.00 62.50 ? 474 ARG A NH2 1 
ATOM   4044 N N   . ALA A 1 475 ? -12.890 6.577  14.430  1.00 19.64 ? 475 ALA A N   1 
ATOM   4045 C CA  . ALA A 1 475 ? -13.588 6.060  13.258  1.00 18.71 ? 475 ALA A CA  1 
ATOM   4046 C C   . ALA A 1 475 ? -12.660 5.350  12.290  1.00 22.22 ? 475 ALA A C   1 
ATOM   4047 O O   . ALA A 1 475 ? -13.126 4.541  11.480  1.00 25.34 ? 475 ALA A O   1 
ATOM   4048 C CB  . ALA A 1 475 ? -14.289 7.198  12.526  1.00 17.92 ? 475 ALA A CB  1 
ATOM   4049 N N   . GLN A 1 476 ? -11.367 5.650  12.338  1.00 22.13 ? 476 GLN A N   1 
ATOM   4050 C CA  . GLN A 1 476 ? -10.408 5.121  11.384  1.00 23.51 ? 476 GLN A CA  1 
ATOM   4051 C C   . GLN A 1 476 ? -9.635  3.933  11.930  1.00 25.55 ? 476 GLN A C   1 
ATOM   4052 O O   . GLN A 1 476 ? -8.767  3.400  11.232  1.00 30.61 ? 476 GLN A O   1 
ATOM   4053 C CB  . GLN A 1 476 ? -9.442  6.232  10.959  1.00 23.29 ? 476 GLN A CB  1 
ATOM   4054 C CG  . GLN A 1 476 ? -10.126 7.312  10.110  1.00 24.82 ? 476 GLN A CG  1 
ATOM   4055 C CD  . GLN A 1 476 ? -9.265  8.549  9.927   1.00 25.91 ? 476 GLN A CD  1 
ATOM   4056 O OE1 . GLN A 1 476 ? -8.469  8.627  8.994   1.00 28.31 ? 476 GLN A OE1 1 
ATOM   4057 N NE2 . GLN A 1 476 ? -9.435  9.529  10.808  1.00 24.36 ? 476 GLN A NE2 1 
ATOM   4058 N N   . GLU A 1 477 ? -9.949  3.488  13.139  1.00 28.59 ? 477 GLU A N   1 
ATOM   4059 C CA  . GLU A 1 477 ? -9.170  2.447  13.798  1.00 34.21 ? 477 GLU A CA  1 
ATOM   4060 C C   . GLU A 1 477 ? -9.983  1.175  13.980  1.00 41.00 ? 477 GLU A C   1 
ATOM   4061 O O   . GLU A 1 477 ? -11.203 1.187  13.838  1.00 44.11 ? 477 GLU A O   1 
ATOM   4062 C CB  . GLU A 1 477 ? -8.664  2.956  15.149  1.00 40.44 ? 477 GLU A CB  1 
ATOM   4063 C CG  . GLU A 1 477 ? -7.650  4.083  15.023  1.00 46.73 ? 477 GLU A CG  1 
ATOM   4064 C CD  . GLU A 1 477 ? -7.185  4.615  16.363  1.00 53.01 ? 477 GLU A CD  1 
ATOM   4065 O OE1 . GLU A 1 477 ? -6.221  5.410  16.380  1.00 53.35 ? 477 GLU A OE1 1 
ATOM   4066 O OE2 . GLU A 1 477 ? -7.787  4.248  17.395  1.00 53.75 ? 477 GLU A OE2 1 
HETATM 4067 C C1  . GLC B 2 .   ? -29.730 23.437 17.625  1.00 17.18 ? 1   GLC B C1  1 
HETATM 4068 C C2  . GLC B 2 .   ? -30.268 22.098 18.095  1.00 13.52 ? 1   GLC B C2  1 
HETATM 4069 C C3  . GLC B 2 .   ? -29.917 21.822 19.545  1.00 13.18 ? 1   GLC B C3  1 
HETATM 4070 C C4  . GLC B 2 .   ? -28.416 21.947 19.755  1.00 13.88 ? 1   GLC B C4  1 
HETATM 4071 C C5  . GLC B 2 .   ? -27.839 23.206 19.087  1.00 14.59 ? 1   GLC B C5  1 
HETATM 4072 C C6  . GLC B 2 .   ? -26.343 23.223 18.936  1.00 13.94 ? 1   GLC B C6  1 
HETATM 4073 O O1  . GLC B 2 .   ? -30.352 24.354 18.441  1.00 30.59 ? 1   GLC B O1  1 
HETATM 4074 O O2  . GLC B 2 .   ? -31.644 22.101 17.878  1.00 11.77 ? 1   GLC B O2  1 
HETATM 4075 O O3  . GLC B 2 .   ? -30.410 20.572 19.964  1.00 11.52 ? 1   GLC B O3  1 
HETATM 4076 O O4  . GLC B 2 .   ? -28.175 22.054 21.118  1.00 12.21 ? 1   GLC B O4  1 
HETATM 4077 O O5  . GLC B 2 .   ? -28.345 23.417 17.794  1.00 19.09 ? 1   GLC B O5  1 
HETATM 4078 O O6  . GLC B 2 .   ? -25.852 22.200 18.130  1.00 15.45 ? 1   GLC B O6  1 
HETATM 4079 C C1  . GLC B 2 .   ? -27.780 20.865 21.789  1.00 12.13 ? 2   GLC B C1  1 
HETATM 4080 C C2  . GLC B 2 .   ? -28.287 20.920 23.231  1.00 10.01 ? 2   GLC B C2  1 
HETATM 4081 C C3  . GLC B 2 .   ? -27.609 22.044 24.006  1.00 10.24 ? 2   GLC B C3  1 
HETATM 4082 C C4  . GLC B 2 .   ? -26.093 21.869 23.938  1.00 11.11 ? 2   GLC B C4  1 
HETATM 4083 C C5  . GLC B 2 .   ? -25.657 21.739 22.470  1.00 10.87 ? 2   GLC B C5  1 
HETATM 4084 C C6  . GLC B 2 .   ? -24.184 21.364 22.331  1.00 12.59 ? 2   GLC B C6  1 
HETATM 4085 O O2  . GLC B 2 .   ? -29.700 21.075 23.256  1.00 11.91 ? 2   GLC B O2  1 
HETATM 4086 O O3  . GLC B 2 .   ? -28.088 22.070 25.348  1.00 12.17 ? 2   GLC B O3  1 
HETATM 4087 O O4  . GLC B 2 .   ? -25.528 23.042 24.516  1.00 11.59 ? 2   GLC B O4  1 
HETATM 4088 O O5  . GLC B 2 .   ? -26.371 20.724 21.781  1.00 12.75 ? 2   GLC B O5  1 
HETATM 4089 O O6  . GLC B 2 .   ? -23.814 21.273 20.965  1.00 12.61 ? 2   GLC B O6  1 
HETATM 4090 C C1  . GLC B 2 .   ? -24.595 22.811 25.580  1.00 13.24 ? 3   GLC B C1  1 
HETATM 4091 C C2  . GLC B 2 .   ? -25.109 23.509 26.837  1.00 11.51 ? 3   GLC B C2  1 
HETATM 4092 C C3  . GLC B 2 .   ? -25.175 25.008 26.601  1.00 13.53 ? 3   GLC B C3  1 
HETATM 4093 C C4  . GLC B 2 .   ? -23.791 25.526 26.213  1.00 12.93 ? 3   GLC B C4  1 
HETATM 4094 C C5  . GLC B 2 .   ? -23.237 24.740 25.017  1.00 14.48 ? 3   GLC B C5  1 
HETATM 4095 C C6  . GLC B 2 .   ? -21.767 25.061 24.725  1.00 13.58 ? 3   GLC B C6  1 
HETATM 4096 O O2  . GLC B 2 .   ? -26.378 23.006 27.185  1.00 14.69 ? 3   GLC B O2  1 
HETATM 4097 O O3  . GLC B 2 .   ? -25.686 25.681 27.742  1.00 15.42 ? 3   GLC B O3  1 
HETATM 4098 O O4  . GLC B 2 .   ? -23.896 26.907 25.910  1.00 16.21 ? 3   GLC B O4  1 
HETATM 4099 O O5  . GLC B 2 .   ? -23.321 23.330 25.224  1.00 13.27 ? 3   GLC B O5  1 
HETATM 4100 O O6  . GLC B 2 .   ? -20.979 24.776 25.864  1.00 16.53 ? 3   GLC B O6  1 
HETATM 4101 C C1  . GLC B 2 .   ? -22.948 27.632 26.718  1.00 25.30 ? 4   GLC B C1  1 
HETATM 4102 C C2  . GLC B 2 .   ? -23.686 28.622 27.610  1.00 19.15 ? 4   GLC B C2  1 
HETATM 4103 C C3  . GLC B 2 .   ? -24.513 29.556 26.755  1.00 29.47 ? 4   GLC B C3  1 
HETATM 4104 C C4  . GLC B 2 .   ? -23.611 30.246 25.735  1.00 33.41 ? 4   GLC B C4  1 
HETATM 4105 C C5  . GLC B 2 .   ? -22.739 29.226 24.986  1.00 25.40 ? 4   GLC B C5  1 
HETATM 4106 C C6  . GLC B 2 .   ? -21.693 29.944 24.141  1.00 43.96 ? 4   GLC B C6  1 
HETATM 4107 O O2  . GLC B 2 .   ? -24.522 27.953 28.529  1.00 20.47 ? 4   GLC B O2  1 
HETATM 4108 O O3  . GLC B 2 .   ? -25.159 30.484 27.603  1.00 32.05 ? 4   GLC B O3  1 
HETATM 4109 O O4  . GLC B 2 .   ? -24.404 30.988 24.832  1.00 43.79 ? 4   GLC B O4  1 
HETATM 4110 O O5  . GLC B 2 .   ? -22.071 28.349 25.876  1.00 27.04 ? 4   GLC B O5  1 
HETATM 4111 O O6  . GLC B 2 .   ? -20.422 29.777 24.727  1.00 50.08 ? 4   GLC B O6  1 
HETATM 4112 C C1  . GLC C 3 .   ? -33.406 28.049 16.636  1.00 17.31 ? 1   GLC C C1  1 
HETATM 4113 C C2  . GLC C 3 .   ? -34.482 27.528 17.546  1.00 19.50 ? 1   GLC C C2  1 
HETATM 4114 C C3  . GLC C 3 .   ? -34.162 28.069 18.925  1.00 17.87 ? 1   GLC C C3  1 
HETATM 4115 C C4  . GLC C 3 .   ? -32.778 27.735 19.409  1.00 15.51 ? 1   GLC C C4  1 
HETATM 4116 C C5  . GLC C 3 .   ? -31.784 28.013 18.308  1.00 19.94 ? 1   GLC C C5  1 
HETATM 4117 C C6  . GLC C 3 .   ? -30.504 27.316 18.697  1.00 25.76 ? 1   GLC C C6  1 
HETATM 4118 O O2  . GLC C 3 .   ? -35.666 28.088 17.095  1.00 21.31 ? 1   GLC C O2  1 
HETATM 4119 O O3  . GLC C 3 .   ? -35.104 27.588 19.852  1.00 20.01 ? 1   GLC C O3  1 
HETATM 4120 O O4  . GLC C 3 .   ? -32.506 28.557 20.506  1.00 18.20 ? 1   GLC C O4  1 
HETATM 4121 O O5  . GLC C 3 .   ? -32.253 27.461 17.109  1.00 18.61 ? 1   GLC C O5  1 
HETATM 4122 O O6  . GLC C 3 .   ? -29.669 27.448 17.604  1.00 38.66 ? 1   GLC C O6  1 
HETATM 4123 C C1  . GLC C 3 .   ? -31.906 27.984 21.650  1.00 19.68 ? 2   GLC C C1  1 
HETATM 4124 C C2  . GLC C 3 .   ? -32.793 28.333 22.832  1.00 16.39 ? 2   GLC C C2  1 
HETATM 4125 C C3  . GLC C 3 .   ? -32.728 29.840 23.060  1.00 14.21 ? 2   GLC C C3  1 
HETATM 4126 C C4  . GLC C 3 .   ? -31.316 30.373 23.265  1.00 17.86 ? 2   GLC C C4  1 
HETATM 4127 C C5  . GLC C 3 .   ? -30.502 29.871 22.107  1.00 22.26 ? 2   GLC C C5  1 
HETATM 4128 C C6  . GLC C 3 .   ? -29.045 30.256 22.366  1.00 25.13 ? 2   GLC C C6  1 
HETATM 4129 O O2  . GLC C 3 .   ? -34.122 27.972 22.561  1.00 17.99 ? 2   GLC C O2  1 
HETATM 4130 O O3  . GLC C 3 .   ? -33.484 30.111 24.206  1.00 14.59 ? 2   GLC C O3  1 
HETATM 4131 O O4  . GLC C 3 .   ? -31.335 31.804 23.256  1.00 19.10 ? 2   GLC C O4  1 
HETATM 4132 O O5  . GLC C 3 .   ? -30.615 28.481 21.932  1.00 23.31 ? 2   GLC C O5  1 
HETATM 4133 O O6  . GLC C 3 .   ? -28.296 29.873 21.253  1.00 30.09 ? 2   GLC C O6  1 
HETATM 4134 C C1  . GLC C 3 .   ? -30.865 32.540 24.396  1.00 26.36 ? 3   GLC C C1  1 
HETATM 4135 C C2  . GLC C 3 .   ? -31.744 33.744 24.656  1.00 24.40 ? 3   GLC C C2  1 
HETATM 4136 C C3  . GLC C 3 .   ? -31.655 34.685 23.477  1.00 26.74 ? 3   GLC C C3  1 
HETATM 4137 C C4  . GLC C 3 .   ? -30.222 34.995 23.083  1.00 24.15 ? 3   GLC C C4  1 
HETATM 4138 C C5  . GLC C 3 .   ? -29.420 33.689 23.003  1.00 25.63 ? 3   GLC C C5  1 
HETATM 4139 C C6  . GLC C 3 .   ? -27.913 33.829 22.853  1.00 38.45 ? 3   GLC C C6  1 
HETATM 4140 O O2  . GLC C 3 .   ? -33.091 33.366 24.900  1.00 22.58 ? 3   GLC C O2  1 
HETATM 4141 O O3  . GLC C 3 .   ? -32.435 35.843 23.735  1.00 24.41 ? 3   GLC C O3  1 
HETATM 4142 O O4  . GLC C 3 .   ? -30.301 35.539 21.805  1.00 25.42 ? 3   GLC C O4  1 
HETATM 4143 O O5  . GLC C 3 .   ? -29.574 32.970 24.175  1.00 28.30 ? 3   GLC C O5  1 
HETATM 4144 O O6  . GLC C 3 .   ? -27.556 34.575 24.004  1.00 42.80 ? 3   GLC C O6  1 
HETATM 4145 C C1  . GLC C 3 .   ? -29.573 36.730 21.585  1.00 29.32 ? 4   GLC C C1  1 
HETATM 4146 C C2  . GLC C 3 .   ? -30.486 37.731 20.915  1.00 32.93 ? 4   GLC C C2  1 
HETATM 4147 C C3  . GLC C 3 .   ? -30.942 37.183 19.590  1.00 24.05 ? 4   GLC C C3  1 
HETATM 4148 C C4  . GLC C 3 .   ? -29.804 36.713 18.724  1.00 27.09 ? 4   GLC C C4  1 
HETATM 4149 C C5  . GLC C 3 .   ? -28.881 35.824 19.534  1.00 25.92 ? 4   GLC C C5  1 
HETATM 4150 C C6  . GLC C 3 .   ? -27.573 35.471 18.875  1.00 30.95 ? 4   GLC C C6  1 
HETATM 4151 O O2  . GLC C 3 .   ? -31.673 38.018 21.629  1.00 35.75 ? 4   GLC C O2  1 
HETATM 4152 O O3  . GLC C 3 .   ? -31.738 38.114 18.909  1.00 30.28 ? 4   GLC C O3  1 
HETATM 4153 O O4  . GLC C 3 .   ? -30.429 35.977 17.685  1.00 27.57 ? 4   GLC C O4  1 
HETATM 4154 O O5  . GLC C 3 .   ? -28.527 36.448 20.724  1.00 27.01 ? 4   GLC C O5  1 
HETATM 4155 O O6  . GLC C 3 .   ? -26.967 36.707 18.499  1.00 39.72 ? 4   GLC C O6  1 
HETATM 4156 C C1  . GLC C 3 .   ? -29.933 36.266 16.388  1.00 28.38 ? 5   GLC C C1  1 
HETATM 4157 C C2  . GLC C 3 .   ? -31.101 36.521 15.525  1.00 33.36 ? 5   GLC C C2  1 
HETATM 4158 C C3  . GLC C 3 .   ? -31.920 35.257 15.506  1.00 26.42 ? 5   GLC C C3  1 
HETATM 4159 C C4  . GLC C 3 .   ? -31.120 34.103 14.949  1.00 25.65 ? 5   GLC C C4  1 
HETATM 4160 C C5  . GLC C 3 .   ? -29.872 33.973 15.784  1.00 30.96 ? 5   GLC C C5  1 
HETATM 4161 C C6  . GLC C 3 .   ? -28.862 33.004 15.180  1.00 36.41 ? 5   GLC C C6  1 
HETATM 4162 O O2  . GLC C 3 .   ? -31.911 37.465 16.147  1.00 34.61 ? 5   GLC C O2  1 
HETATM 4163 O O3  . GLC C 3 .   ? -33.056 35.458 14.736  1.00 29.89 ? 5   GLC C O3  1 
HETATM 4164 O O4  . GLC C 3 .   ? -31.929 32.932 15.113  1.00 20.81 ? 5   GLC C O4  1 
HETATM 4165 O O5  . GLC C 3 .   ? -29.218 35.215 15.846  1.00 33.86 ? 5   GLC C O5  1 
HETATM 4166 O O6  . GLC C 3 .   ? -28.157 32.336 16.221  1.00 41.66 ? 5   GLC C O6  1 
HETATM 4167 C C1  . GLC C 3 .   ? -32.196 32.263 13.912  1.00 20.71 ? 6   GLC C C1  1 
HETATM 4168 C C2  . GLC C 3 .   ? -33.662 31.952 13.822  1.00 16.46 ? 6   GLC C C2  1 
HETATM 4169 C C3  . GLC C 3 .   ? -34.064 31.079 14.993  1.00 18.26 ? 6   GLC C C3  1 
HETATM 4170 C C4  . GLC C 3 .   ? -33.196 29.861 15.064  1.00 19.99 ? 6   GLC C C4  1 
HETATM 4171 C C5  . GLC C 3 .   ? -31.741 30.143 14.865  1.00 21.02 ? 6   GLC C C5  1 
HETATM 4172 C C6  . GLC C 3 .   ? -31.094 28.843 14.377  1.00 23.94 ? 6   GLC C C6  1 
HETATM 4173 O O2  . GLC C 3 .   ? -34.338 33.165 13.836  1.00 21.14 ? 6   GLC C O2  1 
HETATM 4174 O O3  . GLC C 3 .   ? -35.375 30.584 14.912  1.00 18.15 ? 6   GLC C O3  1 
HETATM 4175 O O4  . GLC C 3 .   ? -33.407 29.478 16.358  1.00 19.83 ? 6   GLC C O4  1 
HETATM 4176 O O5  . GLC C 3 .   ? -31.526 31.037 13.826  1.00 21.05 ? 6   GLC C O5  1 
HETATM 4177 O O6  . GLC C 3 .   ? -29.744 29.016 14.584  1.00 30.56 ? 6   GLC C O6  1 
HETATM 4178 C CAC . FLC D 4 .   ? -60.911 34.964 19.959  1.00 37.30 ? 501 FLC A CAC 1 
HETATM 4179 C CA  . FLC D 4 .   ? -61.670 34.072 20.909  1.00 38.15 ? 501 FLC A CA  1 
HETATM 4180 C CB  . FLC D 4 .   ? -63.147 34.066 20.540  1.00 40.40 ? 501 FLC A CB  1 
HETATM 4181 C CBC . FLC D 4 .   ? -63.767 32.862 21.180  1.00 36.90 ? 501 FLC A CBC 1 
HETATM 4182 C CG  . FLC D 4 .   ? -63.828 35.331 21.057  1.00 41.04 ? 501 FLC A CG  1 
HETATM 4183 C CGC . FLC D 4 .   ? -65.335 35.310 20.911  1.00 49.69 ? 501 FLC A CGC 1 
HETATM 4184 O OA1 . FLC D 4 .   ? -60.790 36.161 20.290  1.00 37.15 ? 501 FLC A OA1 1 
HETATM 4185 O OA2 . FLC D 4 .   ? -60.446 34.488 18.897  1.00 29.24 ? 501 FLC A OA2 1 
HETATM 4186 O OB1 . FLC D 4 .   ? -64.090 31.903 20.446  1.00 37.09 ? 501 FLC A OB1 1 
HETATM 4187 O OB2 . FLC D 4 .   ? -63.936 32.886 22.418  1.00 34.84 ? 501 FLC A OB2 1 
HETATM 4188 O OG1 . FLC D 4 .   ? -65.996 36.136 21.577  1.00 47.23 ? 501 FLC A OG1 1 
HETATM 4189 O OG2 . FLC D 4 .   ? -65.877 34.497 20.132  1.00 50.71 ? 501 FLC A OG2 1 
HETATM 4190 O OHB . FLC D 4 .   ? -63.289 33.961 19.121  1.00 40.12 ? 501 FLC A OHB 1 
HETATM 4191 C CAC . FLC E 4 .   ? -21.290 19.592 -9.431  1.00 29.93 ? 502 FLC A CAC 1 
HETATM 4192 C CA  . FLC E 4 .   ? -20.339 18.465 -9.763  1.00 29.76 ? 502 FLC A CA  1 
HETATM 4193 C CB  . FLC E 4 .   ? -19.614 17.956 -8.517  1.00 30.36 ? 502 FLC A CB  1 
HETATM 4194 C CBC . FLC E 4 .   ? -20.588 17.152 -7.693  1.00 34.37 ? 502 FLC A CBC 1 
HETATM 4195 C CG  . FLC E 4 .   ? -18.421 17.097 -8.933  1.00 31.15 ? 502 FLC A CG  1 
HETATM 4196 C CGC . FLC E 4 .   ? -17.568 16.611 -7.779  1.00 32.77 ? 502 FLC A CGC 1 
HETATM 4197 O OA1 . FLC E 4 .   ? -22.124 19.435 -8.516  1.00 31.08 ? 502 FLC A OA1 1 
HETATM 4198 O OA2 . FLC E 4 .   ? -21.220 20.651 -10.089 1.00 26.01 ? 502 FLC A OA2 1 
HETATM 4199 O OB1 . FLC E 4 .   ? -20.829 17.524 -6.524  1.00 30.86 ? 502 FLC A OB1 1 
HETATM 4200 O OB2 . FLC E 4 .   ? -21.109 16.140 -8.207  1.00 29.94 ? 502 FLC A OB2 1 
HETATM 4201 O OG1 . FLC E 4 .   ? -18.107 16.252 -6.711  1.00 30.84 ? 502 FLC A OG1 1 
HETATM 4202 O OG2 . FLC E 4 .   ? -16.333 16.565 -7.955  1.00 30.04 ? 502 FLC A OG2 1 
HETATM 4203 O OHB . FLC E 4 .   ? -19.128 19.065 -7.754  1.00 28.72 ? 502 FLC A OHB 1 
HETATM 4204 C C1  . GOL F 5 .   ? -21.018 5.542  20.002  1.00 37.80 ? 503 GOL A C1  1 
HETATM 4205 O O1  . GOL F 5 .   ? -20.364 5.551  21.229  1.00 52.30 ? 503 GOL A O1  1 
HETATM 4206 C C2  . GOL F 5 .   ? -20.790 4.153  19.379  1.00 42.08 ? 503 GOL A C2  1 
HETATM 4207 O O2  . GOL F 5 .   ? -21.868 3.308  19.588  1.00 51.58 ? 503 GOL A O2  1 
HETATM 4208 C C3  . GOL F 5 .   ? -20.531 4.430  17.887  1.00 38.99 ? 503 GOL A C3  1 
HETATM 4209 O O3  . GOL F 5 .   ? -20.632 3.208  17.228  1.00 45.67 ? 503 GOL A O3  1 
HETATM 4210 C C1  . GOL G 5 .   ? -39.269 24.102 32.352  1.00 30.22 ? 504 GOL A C1  1 
HETATM 4211 O O1  . GOL G 5 .   ? -39.688 25.027 33.281  1.00 28.02 ? 504 GOL A O1  1 
HETATM 4212 C C2  . GOL G 5 .   ? -38.135 23.279 32.966  1.00 31.37 ? 504 GOL A C2  1 
HETATM 4213 O O2  . GOL G 5 .   ? -37.628 22.409 31.976  1.00 19.18 ? 504 GOL A O2  1 
HETATM 4214 C C3  . GOL G 5 .   ? -38.805 22.570 34.224  1.00 29.07 ? 504 GOL A C3  1 
HETATM 4215 O O3  . GOL G 5 .   ? -37.809 22.231 35.180  1.00 14.15 ? 504 GOL A O3  1 
HETATM 4216 O O   . HOH H 6 .   ? -38.277 25.535 53.219  1.00 28.26 ? 601 HOH A O   1 
HETATM 4217 O O   . HOH H 6 .   ? -38.293 3.146  29.620  1.00 48.65 ? 602 HOH A O   1 
HETATM 4218 O O   . HOH H 6 .   ? -32.376 7.555  46.903  1.00 53.24 ? 603 HOH A O   1 
HETATM 4219 O O   . HOH H 6 .   ? -27.593 6.363  38.611  1.00 36.14 ? 604 HOH A O   1 
HETATM 4220 O O   . HOH H 6 .   ? -48.948 41.194 32.408  1.00 33.94 ? 605 HOH A O   1 
HETATM 4221 O O   . HOH H 6 .   ? -18.512 26.074 25.049  1.00 29.96 ? 606 HOH A O   1 
HETATM 4222 O O   . HOH H 6 .   ? -57.842 31.330 29.580  1.00 38.13 ? 607 HOH A O   1 
HETATM 4223 O O   . HOH H 6 .   ? -43.316 13.568 39.089  1.00 41.54 ? 608 HOH A O   1 
HETATM 4224 O O   . HOH H 6 .   ? -8.109  16.317 13.597  1.00 35.24 ? 609 HOH A O   1 
HETATM 4225 O O   . HOH H 6 .   ? -24.432 10.986 52.367  1.00 40.06 ? 610 HOH A O   1 
HETATM 4226 O O   . HOH H 6 .   ? -11.606 3.381  21.710  1.00 51.40 ? 611 HOH A O   1 
HETATM 4227 O O   . HOH H 6 .   ? -46.077 17.829 -6.641  1.00 36.75 ? 612 HOH A O   1 
HETATM 4228 O O   . HOH H 6 .   ? -43.166 33.074 -0.680  1.00 40.39 ? 613 HOH A O   1 
HETATM 4229 O O   . HOH H 6 .   ? -18.976 28.446 26.207  1.00 50.07 ? 614 HOH A O   1 
HETATM 4230 O O   . HOH H 6 .   ? -33.702 13.292 32.758  1.00 29.83 ? 615 HOH A O   1 
HETATM 4231 O O   . HOH H 6 .   ? -41.222 23.133 54.858  1.00 34.67 ? 616 HOH A O   1 
HETATM 4232 O O   . HOH H 6 .   ? -21.394 38.431 34.013  1.00 49.96 ? 617 HOH A O   1 
HETATM 4233 O O   . HOH H 6 .   ? -19.701 3.353  30.201  1.00 46.05 ? 618 HOH A O   1 
HETATM 4234 O O   . HOH H 6 .   ? -52.631 26.887 -0.855  1.00 31.59 ? 619 HOH A O   1 
HETATM 4235 O O   . HOH H 6 .   ? -60.919 22.926 22.961  1.00 39.38 ? 620 HOH A O   1 
HETATM 4236 O O   . HOH H 6 .   ? -37.094 27.387 47.597  1.00 32.08 ? 621 HOH A O   1 
HETATM 4237 O O   . HOH H 6 .   ? -48.866 33.508 -7.057  1.00 37.26 ? 622 HOH A O   1 
HETATM 4238 O O   . HOH H 6 .   ? -14.708 15.694 -6.254  1.00 25.36 ? 623 HOH A O   1 
HETATM 4239 O O   . HOH H 6 .   ? -18.649 6.975  30.959  1.00 22.93 ? 624 HOH A O   1 
HETATM 4240 O O   . HOH H 6 .   ? -10.112 16.675 -3.011  1.00 37.75 ? 625 HOH A O   1 
HETATM 4241 O O   . HOH H 6 .   ? -61.630 37.938 21.882  1.00 33.70 ? 626 HOH A O   1 
HETATM 4242 O O   . HOH H 6 .   ? -56.413 18.604 23.308  1.00 43.84 ? 627 HOH A O   1 
HETATM 4243 O O   . HOH H 6 .   ? -46.724 19.094 40.714  1.00 40.84 ? 628 HOH A O   1 
HETATM 4244 O O   . HOH H 6 .   ? -46.611 43.031 34.324  1.00 39.00 ? 629 HOH A O   1 
HETATM 4245 O O   . HOH H 6 .   ? -31.911 32.184 50.768  1.00 50.08 ? 630 HOH A O   1 
HETATM 4246 O O   . HOH H 6 .   ? -17.471 4.510  6.295   1.00 36.17 ? 631 HOH A O   1 
HETATM 4247 O O   . HOH H 6 .   ? -20.684 10.569 47.354  1.00 37.65 ? 632 HOH A O   1 
HETATM 4248 O O   . HOH H 6 .   ? -38.508 25.718 45.379  1.00 30.05 ? 633 HOH A O   1 
HETATM 4249 O O   . HOH H 6 .   ? -30.208 7.794  43.133  1.00 39.56 ? 634 HOH A O   1 
HETATM 4250 O O   . HOH H 6 .   ? -13.687 13.416 48.383  1.00 39.92 ? 635 HOH A O   1 
HETATM 4251 O O   . HOH H 6 .   ? -40.402 26.498 41.514  1.00 36.42 ? 636 HOH A O   1 
HETATM 4252 O O   . HOH H 6 .   ? -29.272 20.182 -4.142  1.00 42.85 ? 637 HOH A O   1 
HETATM 4253 O O   . HOH H 6 .   ? -16.143 18.902 -5.347  1.00 29.01 ? 638 HOH A O   1 
HETATM 4254 O O   . HOH H 6 .   ? -26.272 22.013 15.381  1.00 17.07 ? 639 HOH A O   1 
HETATM 4255 O O   . HOH H 6 .   ? -32.380 25.811 29.884  1.00 12.80 ? 640 HOH A O   1 
HETATM 4256 O O   . HOH H 6 .   ? -25.901 9.734  43.698  1.00 35.34 ? 641 HOH A O   1 
HETATM 4257 O O   . HOH H 6 .   ? -18.260 31.071 1.873   1.00 24.58 ? 642 HOH A O   1 
HETATM 4258 O O   . HOH H 6 .   ? -34.458 9.254  -3.219  1.00 35.71 ? 643 HOH A O   1 
HETATM 4259 O O   . HOH H 6 .   ? -32.110 30.682 47.752  1.00 34.16 ? 644 HOH A O   1 
HETATM 4260 O O   . HOH H 6 .   ? -40.868 2.103  33.785  1.00 35.12 ? 645 HOH A O   1 
HETATM 4261 O O   . HOH H 6 .   ? -35.245 33.932 2.813   1.00 40.93 ? 646 HOH A O   1 
HETATM 4262 O O   . HOH H 6 .   ? -57.496 17.567 2.019   1.00 38.75 ? 647 HOH A O   1 
HETATM 4263 O O   . HOH H 6 .   ? -18.100 16.554 32.552  1.00 17.02 ? 648 HOH A O   1 
HETATM 4264 O O   . HOH H 6 .   ? -19.109 16.997 -4.398  1.00 37.37 ? 649 HOH A O   1 
HETATM 4265 O O   . HOH H 6 .   ? -23.374 41.123 36.962  1.00 43.85 ? 650 HOH A O   1 
HETATM 4266 O O   . HOH H 6 .   ? -39.933 20.108 52.667  1.00 38.63 ? 651 HOH A O   1 
HETATM 4267 O O   . HOH H 6 .   ? -12.742 16.322 37.701  1.00 27.30 ? 652 HOH A O   1 
HETATM 4268 O O   . HOH H 6 .   ? -29.056 28.905 -6.204  1.00 34.73 ? 653 HOH A O   1 
HETATM 4269 O O   . HOH H 6 .   ? -49.246 11.351 32.852  1.00 43.35 ? 654 HOH A O   1 
HETATM 4270 O O   . HOH H 6 .   ? -16.407 14.356 53.056  1.00 39.05 ? 655 HOH A O   1 
HETATM 4271 O O   . HOH H 6 .   ? -30.069 17.165 -0.219  1.00 15.31 ? 656 HOH A O   1 
HETATM 4272 O O   . HOH H 6 .   ? -43.580 16.326 38.708  1.00 25.83 ? 657 HOH A O   1 
HETATM 4273 O O   . HOH H 6 .   ? -54.274 11.588 22.180  1.00 24.55 ? 658 HOH A O   1 
HETATM 4274 O O   . HOH H 6 .   ? -24.343 6.871  20.914  1.00 23.84 ? 659 HOH A O   1 
HETATM 4275 O O   . HOH H 6 .   ? -33.115 32.238 3.219   1.00 26.99 ? 660 HOH A O   1 
HETATM 4276 O O   . HOH H 6 .   ? -32.861 16.412 7.930   1.00 13.27 ? 661 HOH A O   1 
HETATM 4277 O O   . HOH H 6 .   ? -54.350 21.950 35.463  1.00 32.07 ? 662 HOH A O   1 
HETATM 4278 O O   . HOH H 6 .   ? -56.143 15.310 3.234   1.00 36.91 ? 663 HOH A O   1 
HETATM 4279 O O   . HOH H 6 .   ? -28.481 25.418 27.453  1.00 20.12 ? 664 HOH A O   1 
HETATM 4280 O O   . HOH H 6 .   ? -23.867 17.342 9.881   1.00 24.87 ? 665 HOH A O   1 
HETATM 4281 O O   . HOH H 6 .   ? -40.273 4.569  10.294  1.00 27.79 ? 666 HOH A O   1 
HETATM 4282 O O   . HOH H 6 .   ? -36.114 30.402 11.281  1.00 23.78 ? 667 HOH A O   1 
HETATM 4283 O O   . HOH H 6 .   ? -15.827 23.362 -3.670  1.00 24.65 ? 668 HOH A O   1 
HETATM 4284 O O   . HOH H 6 .   ? -62.440 18.472 15.513  1.00 53.22 ? 669 HOH A O   1 
HETATM 4285 O O   . HOH H 6 .   ? -57.088 24.165 25.186  1.00 31.07 ? 670 HOH A O   1 
HETATM 4286 O O   . HOH H 6 .   ? -50.522 27.273 0.413   1.00 34.62 ? 671 HOH A O   1 
HETATM 4287 O O   . HOH H 6 .   ? -46.344 38.834 20.113  1.00 19.38 ? 672 HOH A O   1 
HETATM 4288 O O   . HOH H 6 .   ? -43.942 4.141  -1.283  1.00 34.51 ? 673 HOH A O   1 
HETATM 4289 O O   . HOH H 6 .   ? -18.364 22.784 -4.768  1.00 42.48 ? 674 HOH A O   1 
HETATM 4290 O O   . HOH H 6 .   ? -10.022 14.920 -1.452  1.00 45.50 ? 675 HOH A O   1 
HETATM 4291 O O   . HOH H 6 .   ? -37.595 24.497 -4.960  1.00 31.73 ? 676 HOH A O   1 
HETATM 4292 O O   . HOH H 6 .   ? -16.181 11.065 45.025  1.00 47.78 ? 677 HOH A O   1 
HETATM 4293 O O   . HOH H 6 .   ? -49.367 20.091 21.472  1.00 15.36 ? 678 HOH A O   1 
HETATM 4294 O O   . HOH H 6 .   ? -38.235 35.473 33.066  1.00 25.19 ? 679 HOH A O   1 
HETATM 4295 O O   . HOH H 6 .   ? -42.630 9.744  36.920  1.00 33.95 ? 680 HOH A O   1 
HETATM 4296 O O   . HOH H 6 .   ? -33.972 18.235 39.328  1.00 16.23 ? 681 HOH A O   1 
HETATM 4297 O O   . HOH H 6 .   ? -22.994 15.263 30.084  1.00 16.43 ? 682 HOH A O   1 
HETATM 4298 O O   . HOH H 6 .   ? -8.698  21.417 47.528  1.00 38.91 ? 683 HOH A O   1 
HETATM 4299 O O   . HOH H 6 .   ? -29.480 26.093 15.481  1.00 28.08 ? 684 HOH A O   1 
HETATM 4300 O O   . HOH H 6 .   ? -1.111  27.610 45.656  1.00 32.06 ? 685 HOH A O   1 
HETATM 4301 O O   . HOH H 6 .   ? -9.397  20.918 21.524  1.00 18.86 ? 686 HOH A O   1 
HETATM 4302 O O   . HOH H 6 .   ? -64.829 32.567 11.070  1.00 37.43 ? 687 HOH A O   1 
HETATM 4303 O O   . HOH H 6 .   ? -12.120 32.741 51.870  1.00 44.91 ? 688 HOH A O   1 
HETATM 4304 O O   . HOH H 6 .   ? -15.096 3.731  24.737  1.00 40.69 ? 689 HOH A O   1 
HETATM 4305 O O   . HOH H 6 .   ? -34.960 25.896 24.184  1.00 15.00 ? 690 HOH A O   1 
HETATM 4306 O O   . HOH H 6 .   ? -53.111 11.089 19.912  1.00 24.81 ? 691 HOH A O   1 
HETATM 4307 O O   . HOH H 6 .   ? -57.098 38.574 13.047  1.00 36.44 ? 692 HOH A O   1 
HETATM 4308 O O   . HOH H 6 .   ? -43.378 21.155 28.940  1.00 14.66 ? 693 HOH A O   1 
HETATM 4309 O O   . HOH H 6 .   ? -44.367 3.879  8.094   1.00 32.45 ? 694 HOH A O   1 
HETATM 4310 O O   . HOH H 6 .   ? -30.167 -0.350 25.353  1.00 39.40 ? 695 HOH A O   1 
HETATM 4311 O O   . HOH H 6 .   ? -20.502 14.014 -0.792  1.00 21.50 ? 696 HOH A O   1 
HETATM 4312 O O   . HOH H 6 .   ? -48.261 33.860 0.994   1.00 34.52 ? 697 HOH A O   1 
HETATM 4313 O O   . HOH H 6 .   ? -44.281 33.604 11.965  1.00 22.47 ? 698 HOH A O   1 
HETATM 4314 O O   . HOH H 6 .   ? -55.789 25.657 37.124  1.00 42.03 ? 699 HOH A O   1 
HETATM 4315 O O   . HOH H 6 .   ? -49.484 9.287  22.120  1.00 26.84 ? 700 HOH A O   1 
HETATM 4316 O O   . HOH H 6 .   ? -32.455 20.816 21.709  1.00 13.06 ? 701 HOH A O   1 
HETATM 4317 O O   . HOH H 6 .   ? -47.670 24.128 7.882   1.00 16.29 ? 702 HOH A O   1 
HETATM 4318 O O   . HOH H 6 .   ? -31.618 11.446 48.379  1.00 28.34 ? 703 HOH A O   1 
HETATM 4319 O O   . HOH H 6 .   ? -23.510 15.786 -4.707  1.00 33.47 ? 704 HOH A O   1 
HETATM 4320 O O   . HOH H 6 .   ? -44.166 24.155 40.818  1.00 31.36 ? 705 HOH A O   1 
HETATM 4321 O O   . HOH H 6 .   ? -55.388 39.723 20.146  1.00 37.19 ? 706 HOH A O   1 
HETATM 4322 O O   . HOH H 6 .   ? -20.453 24.860 53.683  1.00 22.21 ? 707 HOH A O   1 
HETATM 4323 O O   . HOH H 6 .   ? -20.048 16.656 56.892  1.00 48.80 ? 708 HOH A O   1 
HETATM 4324 O O   . HOH H 6 .   ? -8.630  13.437 14.616  1.00 37.51 ? 709 HOH A O   1 
HETATM 4325 O O   . HOH H 6 .   ? -55.805 24.121 8.521   1.00 17.63 ? 710 HOH A O   1 
HETATM 4326 O O   . HOH H 6 .   ? -48.490 9.321  19.462  1.00 26.61 ? 711 HOH A O   1 
HETATM 4327 O O   . HOH H 6 .   ? -32.339 28.796 40.871  1.00 21.22 ? 712 HOH A O   1 
HETATM 4328 O O   . HOH H 6 .   ? -22.798 12.541 -0.429  1.00 19.28 ? 713 HOH A O   1 
HETATM 4329 O O   . HOH H 6 .   ? -33.262 25.421 37.602  1.00 16.14 ? 714 HOH A O   1 
HETATM 4330 O O   . HOH H 6 .   ? -54.974 11.457 26.721  1.00 29.52 ? 715 HOH A O   1 
HETATM 4331 O O   . HOH H 6 .   ? -22.735 6.532  -0.013  1.00 30.71 ? 716 HOH A O   1 
HETATM 4332 O O   . HOH H 6 .   ? -7.277  21.636 11.573  1.00 37.10 ? 717 HOH A O   1 
HETATM 4333 O O   . HOH H 6 .   ? -59.591 30.148 12.936  1.00 31.05 ? 718 HOH A O   1 
HETATM 4334 O O   . HOH H 6 .   ? -52.460 13.390 35.758  1.00 45.75 ? 719 HOH A O   1 
HETATM 4335 O O   . HOH H 6 .   ? -41.755 35.273 30.874  1.00 20.14 ? 720 HOH A O   1 
HETATM 4336 O O   . HOH H 6 .   ? -27.230 27.519 2.434   1.00 18.97 ? 721 HOH A O   1 
HETATM 4337 O O   . HOH H 6 .   ? -18.674 6.494  0.816   1.00 30.44 ? 722 HOH A O   1 
HETATM 4338 O O   . HOH H 6 .   ? -65.861 29.740 10.021  1.00 38.07 ? 723 HOH A O   1 
HETATM 4339 O O   . HOH H 6 .   ? -20.377 30.167 7.409   1.00 27.72 ? 724 HOH A O   1 
HETATM 4340 O O   . HOH H 6 .   ? -45.206 2.552  13.458  1.00 35.81 ? 725 HOH A O   1 
HETATM 4341 O O   . HOH H 6 .   ? -36.938 5.373  32.847  1.00 19.48 ? 726 HOH A O   1 
HETATM 4342 O O   . HOH H 6 .   ? -55.953 21.792 24.713  1.00 24.67 ? 727 HOH A O   1 
HETATM 4343 O O   . HOH H 6 .   ? -48.738 41.286 27.335  1.00 31.39 ? 728 HOH A O   1 
HETATM 4344 O O   . HOH H 6 .   ? -52.225 15.980 29.888  1.00 34.11 ? 729 HOH A O   1 
HETATM 4345 O O   . HOH H 6 .   ? -34.305 20.926 -2.051  1.00 14.54 ? 730 HOH A O   1 
HETATM 4346 O O   . HOH H 6 .   ? -16.942 20.507 38.933  1.00 30.16 ? 731 HOH A O   1 
HETATM 4347 O O   . HOH H 6 .   ? -24.571 15.193 17.542  1.00 15.01 ? 732 HOH A O   1 
HETATM 4348 O O   . HOH H 6 .   ? -26.939 12.334 52.355  1.00 27.66 ? 733 HOH A O   1 
HETATM 4349 O O   . HOH H 6 .   ? -63.570 21.494 15.752  1.00 48.48 ? 734 HOH A O   1 
HETATM 4350 O O   . HOH H 6 .   ? -28.023 35.292 38.177  1.00 26.95 ? 735 HOH A O   1 
HETATM 4351 O O   . HOH H 6 .   ? -10.709 16.468 2.579   1.00 28.30 ? 736 HOH A O   1 
HETATM 4352 O O   . HOH H 6 .   ? -45.656 17.200 37.327  1.00 25.82 ? 737 HOH A O   1 
HETATM 4353 O O   . HOH H 6 .   ? -36.874 17.966 39.157  1.00 17.89 ? 738 HOH A O   1 
HETATM 4354 O O   . HOH H 6 .   ? -24.209 33.908 32.347  1.00 26.98 ? 739 HOH A O   1 
HETATM 4355 O O   . HOH H 6 .   ? -29.333 26.156 0.528   1.00 16.75 ? 740 HOH A O   1 
HETATM 4356 O O   . HOH H 6 .   ? -9.218  13.504 8.636   1.00 25.95 ? 741 HOH A O   1 
HETATM 4357 O O   . HOH H 6 .   ? -48.445 36.199 13.794  1.00 40.80 ? 742 HOH A O   1 
HETATM 4358 O O   . HOH H 6 .   ? -54.651 37.610 26.298  1.00 48.21 ? 743 HOH A O   1 
HETATM 4359 O O   . HOH H 6 .   ? -32.947 10.741 -1.223  1.00 25.17 ? 744 HOH A O   1 
HETATM 4360 O O   . HOH H 6 .   ? -34.277 27.042 54.178  1.00 31.84 ? 745 HOH A O   1 
HETATM 4361 O O   . HOH H 6 .   ? -46.481 29.485 38.857  1.00 36.94 ? 746 HOH A O   1 
HETATM 4362 O O   . HOH H 6 .   ? -32.616 20.443 15.712  1.00 12.12 ? 747 HOH A O   1 
HETATM 4363 O O   . HOH H 6 .   ? -40.004 2.847  0.919   1.00 39.47 ? 748 HOH A O   1 
HETATM 4364 O O   . HOH H 6 .   ? -17.741 7.168  23.465  1.00 23.21 ? 749 HOH A O   1 
HETATM 4365 O O   . HOH H 6 .   ? -15.060 28.459 17.475  1.00 28.25 ? 750 HOH A O   1 
HETATM 4366 O O   . HOH H 6 .   ? -29.231 37.499 37.733  1.00 44.10 ? 751 HOH A O   1 
HETATM 4367 O O   . HOH H 6 .   ? -32.497 28.380 -5.720  1.00 39.45 ? 752 HOH A O   1 
HETATM 4368 O O   . HOH H 6 .   ? -32.058 36.213 31.216  1.00 31.53 ? 753 HOH A O   1 
HETATM 4369 O O   . HOH H 6 .   ? -44.509 9.035  36.357  1.00 40.71 ? 754 HOH A O   1 
HETATM 4370 O O   . HOH H 6 .   ? -13.385 18.531 29.977  1.00 31.92 ? 755 HOH A O   1 
HETATM 4371 O O   . HOH H 6 .   ? -12.074 18.121 0.924   1.00 27.93 ? 756 HOH A O   1 
HETATM 4372 O O   . HOH H 6 .   ? -13.711 8.727  -2.270  1.00 44.31 ? 757 HOH A O   1 
HETATM 4373 O O   . HOH H 6 .   ? -37.214 29.611 19.277  1.00 19.20 ? 758 HOH A O   1 
HETATM 4374 O O   . HOH H 6 .   ? -47.781 26.161 11.965  1.00 15.78 ? 759 HOH A O   1 
HETATM 4375 O O   . HOH H 6 .   ? -31.732 11.315 -3.498  1.00 30.96 ? 760 HOH A O   1 
HETATM 4376 O O   . HOH H 6 .   ? -19.000 34.263 -0.653  1.00 50.70 ? 761 HOH A O   1 
HETATM 4377 O O   . HOH H 6 .   ? -35.923 17.272 34.462  1.00 14.64 ? 762 HOH A O   1 
HETATM 4378 O O   . HOH H 6 .   ? -27.555 32.220 48.414  1.00 22.51 ? 763 HOH A O   1 
HETATM 4379 O O   . HOH H 6 .   ? -23.307 32.272 28.991  1.00 35.16 ? 764 HOH A O   1 
HETATM 4380 O O   . HOH H 6 .   ? -42.323 19.214 35.708  1.00 16.00 ? 765 HOH A O   1 
HETATM 4381 O O   . HOH H 6 .   ? -41.332 8.202  35.195  1.00 31.86 ? 766 HOH A O   1 
HETATM 4382 O O   . HOH H 6 .   ? -60.764 23.928 8.768   1.00 26.86 ? 767 HOH A O   1 
HETATM 4383 O O   . HOH H 6 .   ? -30.845 17.591 9.353   1.00 14.29 ? 768 HOH A O   1 
HETATM 4384 O O   . HOH H 6 .   ? -17.236 38.137 48.754  1.00 38.73 ? 769 HOH A O   1 
HETATM 4385 O O   . HOH H 6 .   ? -46.000 1.602  21.170  1.00 38.52 ? 770 HOH A O   1 
HETATM 4386 O O   . HOH H 6 .   ? -34.407 7.029  32.070  1.00 16.59 ? 771 HOH A O   1 
HETATM 4387 O O   . HOH H 6 .   ? -29.329 7.496  1.253   1.00 30.99 ? 772 HOH A O   1 
HETATM 4388 O O   . HOH H 6 .   ? -56.587 16.960 21.741  1.00 39.23 ? 773 HOH A O   1 
HETATM 4389 O O   . HOH H 6 .   ? -34.664 32.797 39.180  1.00 24.34 ? 774 HOH A O   1 
HETATM 4390 O O   . HOH H 6 .   ? -25.192 34.698 40.110  1.00 34.02 ? 775 HOH A O   1 
HETATM 4391 O O   . HOH H 6 .   ? -27.478 33.674 51.130  1.00 41.21 ? 776 HOH A O   1 
HETATM 4392 O O   . HOH H 6 .   ? -30.232 34.642 47.269  1.00 28.21 ? 777 HOH A O   1 
HETATM 4393 O O   . HOH H 6 .   ? -36.817 33.661 25.757  1.00 14.33 ? 778 HOH A O   1 
HETATM 4394 O O   . HOH H 6 .   ? -28.224 28.003 25.954  1.00 31.14 ? 779 HOH A O   1 
HETATM 4395 O O   . HOH H 6 .   ? -44.597 38.076 12.798  1.00 38.05 ? 780 HOH A O   1 
HETATM 4396 O O   . HOH H 6 .   ? -14.289 20.802 38.107  1.00 31.41 ? 781 HOH A O   1 
HETATM 4397 O O   . HOH H 6 .   ? -41.497 23.798 41.259  1.00 29.65 ? 782 HOH A O   1 
HETATM 4398 O O   . HOH H 6 .   ? -54.388 18.661 -0.794  1.00 34.72 ? 783 HOH A O   1 
HETATM 4399 O O   . HOH H 6 .   ? -34.626 27.596 2.371   1.00 17.42 ? 784 HOH A O   1 
HETATM 4400 O O   . HOH H 6 .   ? -44.887 7.092  17.272  1.00 48.42 ? 785 HOH A O   1 
HETATM 4401 O O   . HOH H 6 .   ? -7.982  3.960  8.524   1.00 45.92 ? 786 HOH A O   1 
HETATM 4402 O O   . HOH H 6 .   ? -47.095 42.622 24.630  1.00 28.74 ? 787 HOH A O   1 
HETATM 4403 O O   . HOH H 6 .   ? -27.685 34.128 6.709   1.00 35.11 ? 788 HOH A O   1 
HETATM 4404 O O   . HOH H 6 .   ? -44.689 3.691  23.739  1.00 32.21 ? 789 HOH A O   1 
HETATM 4405 O O   . HOH H 6 .   ? -30.778 35.957 11.756  1.00 48.06 ? 790 HOH A O   1 
HETATM 4406 O O   . HOH H 6 .   ? -24.676 33.275 -1.322  1.00 29.29 ? 791 HOH A O   1 
HETATM 4407 O O   . HOH H 6 .   ? -11.756 5.324  0.191   1.00 39.91 ? 792 HOH A O   1 
HETATM 4408 O O   . HOH H 6 .   ? -16.247 31.133 32.015  1.00 35.35 ? 793 HOH A O   1 
HETATM 4409 O O   . HOH H 6 .   ? -43.377 6.581  4.456   1.00 31.45 ? 794 HOH A O   1 
HETATM 4410 O O   . HOH H 6 .   ? -34.764 32.094 26.717  1.00 15.67 ? 795 HOH A O   1 
HETATM 4411 O O   . HOH H 6 .   ? -40.654 35.722 12.988  1.00 30.14 ? 796 HOH A O   1 
HETATM 4412 O O   . HOH H 6 .   ? -19.684 18.536 55.264  1.00 22.72 ? 797 HOH A O   1 
HETATM 4413 O O   . HOH H 6 .   ? -10.962 25.343 5.224   1.00 33.41 ? 798 HOH A O   1 
HETATM 4414 O O   . HOH H 6 .   ? -36.715 31.951 -2.939  1.00 44.72 ? 799 HOH A O   1 
HETATM 4415 O O   . HOH H 6 .   ? -38.673 35.254 14.627  1.00 32.43 ? 800 HOH A O   1 
HETATM 4416 O O   . HOH H 6 .   ? -49.063 40.130 13.459  1.00 47.16 ? 801 HOH A O   1 
HETATM 4417 O O   . HOH H 6 .   ? -21.897 7.024  3.104   1.00 18.27 ? 802 HOH A O   1 
HETATM 4418 O O   . HOH H 6 .   ? -40.745 31.937 34.300  1.00 18.50 ? 803 HOH A O   1 
HETATM 4419 O O   . HOH H 6 .   ? -7.815  11.106 7.608   1.00 32.17 ? 804 HOH A O   1 
HETATM 4420 O O   . HOH H 6 .   ? -17.841 19.230 -3.580  1.00 28.23 ? 805 HOH A O   1 
HETATM 4421 O O   . HOH H 6 .   ? -60.546 14.609 12.341  1.00 39.73 ? 806 HOH A O   1 
HETATM 4422 O O   . HOH H 6 .   ? -25.335 13.668 -4.314  1.00 41.16 ? 807 HOH A O   1 
HETATM 4423 O O   . HOH H 6 .   ? -44.349 0.021  14.222  1.00 31.83 ? 808 HOH A O   1 
HETATM 4424 O O   . HOH H 6 .   ? -20.799 4.559  3.593   1.00 26.59 ? 809 HOH A O   1 
HETATM 4425 O O   . HOH H 6 .   ? -13.469 32.932 43.543  1.00 51.82 ? 810 HOH A O   1 
HETATM 4426 O O   . HOH H 6 .   ? -38.131 27.007 43.113  1.00 29.43 ? 811 HOH A O   1 
HETATM 4427 O O   . HOH H 6 .   ? -42.140 34.462 0.450   1.00 42.68 ? 812 HOH A O   1 
HETATM 4428 O O   . HOH H 6 .   ? -47.491 24.499 -2.602  1.00 41.16 ? 813 HOH A O   1 
HETATM 4429 O O   . HOH H 6 .   ? -27.534 1.972  21.948  1.00 48.53 ? 814 HOH A O   1 
HETATM 4430 O O   . HOH H 6 .   ? -58.560 24.173 33.955  1.00 34.32 ? 815 HOH A O   1 
HETATM 4431 O O   . HOH H 6 .   ? -42.245 1.667  31.443  1.00 27.44 ? 816 HOH A O   1 
HETATM 4432 O O   . HOH H 6 .   ? -20.341 4.143  7.863   1.00 36.00 ? 817 HOH A O   1 
HETATM 4433 O O   . HOH H 6 .   ? -42.963 24.191 -4.664  1.00 32.05 ? 818 HOH A O   1 
HETATM 4434 O O   . HOH H 6 .   ? -50.340 39.892 21.621  1.00 33.90 ? 819 HOH A O   1 
HETATM 4435 O O   . HOH H 6 .   ? -16.329 22.077 17.616  1.00 21.42 ? 820 HOH A O   1 
HETATM 4436 O O   . HOH H 6 .   ? -45.756 8.945  19.507  1.00 18.25 ? 821 HOH A O   1 
HETATM 4437 O O   . HOH H 6 .   ? -31.568 39.316 27.872  1.00 43.24 ? 822 HOH A O   1 
HETATM 4438 O O   . HOH H 6 .   ? -47.903 34.335 14.297  1.00 34.58 ? 823 HOH A O   1 
HETATM 4439 O O   . HOH H 6 .   ? -33.806 3.508  34.447  1.00 41.59 ? 824 HOH A O   1 
HETATM 4440 O O   . HOH H 6 .   ? -13.640 28.521 -4.941  1.00 47.08 ? 825 HOH A O   1 
HETATM 4441 O O   . HOH H 6 .   ? -66.813 32.026 5.860   1.00 38.29 ? 826 HOH A O   1 
HETATM 4442 O O   . HOH H 6 .   ? -34.660 -2.338 18.686  1.00 28.64 ? 827 HOH A O   1 
HETATM 4443 O O   . HOH H 6 .   ? -39.849 -0.002 8.339   1.00 53.03 ? 828 HOH A O   1 
HETATM 4444 O O   . HOH H 6 .   ? -65.109 20.292 12.668  1.00 43.08 ? 829 HOH A O   1 
HETATM 4445 O O   . HOH H 6 .   ? -34.041 13.739 -6.259  1.00 38.19 ? 830 HOH A O   1 
HETATM 4446 O O   . HOH H 6 .   ? -47.994 28.770 -3.819  1.00 34.39 ? 831 HOH A O   1 
HETATM 4447 O O   . HOH H 6 .   ? -19.413 0.137  13.750  1.00 36.92 ? 832 HOH A O   1 
HETATM 4448 O O   . HOH H 6 .   ? -16.528 26.051 -3.215  1.00 37.35 ? 833 HOH A O   1 
HETATM 4449 O O   . HOH H 6 .   ? -17.625 7.528  -2.263  1.00 31.96 ? 834 HOH A O   1 
HETATM 4450 O O   . HOH H 6 .   ? -25.345 23.293 58.071  1.00 34.27 ? 835 HOH A O   1 
HETATM 4451 O O   . HOH H 6 .   ? -45.197 23.554 -5.091  1.00 31.59 ? 836 HOH A O   1 
HETATM 4452 O O   . HOH H 6 .   ? -18.277 27.181 -4.454  1.00 37.55 ? 837 HOH A O   1 
HETATM 4453 O O   . HOH H 6 .   ? -62.313 19.134 17.250  1.00 53.14 ? 838 HOH A O   1 
HETATM 4454 O O   . HOH H 6 .   ? -33.002 19.855 -4.864  1.00 34.89 ? 839 HOH A O   1 
HETATM 4455 O O   . HOH H 6 .   ? -58.049 21.385 2.080   1.00 30.21 ? 840 HOH A O   1 
HETATM 4456 O O   . HOH H 6 .   ? -19.457 10.692 37.356  1.00 38.14 ? 841 HOH A O   1 
HETATM 4457 O O   . HOH H 6 .   ? -27.725 13.688 -5.456  1.00 40.07 ? 842 HOH A O   1 
HETATM 4458 O O   . HOH H 6 .   ? -33.626 33.968 43.838  1.00 47.84 ? 843 HOH A O   1 
HETATM 4459 O O   . HOH H 6 .   ? -18.482 31.037 -6.465  1.00 42.83 ? 844 HOH A O   1 
HETATM 4460 O O   . HOH H 6 .   ? -57.231 15.305 4.810   1.00 38.42 ? 845 HOH A O   1 
HETATM 4461 O O   . HOH H 6 .   ? -41.854 35.990 35.692  1.00 26.21 ? 846 HOH A O   1 
HETATM 4462 O O   . HOH H 6 .   ? -39.900 12.052 -5.527  1.00 13.97 ? 847 HOH A O   1 
HETATM 4463 O O   . HOH H 6 .   ? -34.918 23.355 -5.064  1.00 33.48 ? 848 HOH A O   1 
HETATM 4464 O O   . HOH H 6 .   ? -9.585  23.119 15.416  1.00 32.78 ? 849 HOH A O   1 
HETATM 4465 O O   . HOH H 6 .   ? -24.403 28.562 -7.126  1.00 43.93 ? 850 HOH A O   1 
HETATM 4466 O O   . HOH H 6 .   ? -22.900 13.231 18.606  1.00 14.26 ? 851 HOH A O   1 
HETATM 4467 O O   . HOH H 6 .   ? -15.479 29.399 20.073  1.00 42.57 ? 852 HOH A O   1 
HETATM 4468 O O   . HOH H 6 .   ? -57.813 13.323 23.608  1.00 48.56 ? 853 HOH A O   1 
HETATM 4469 O O   . HOH H 6 .   ? -32.614 18.184 -3.039  1.00 20.11 ? 854 HOH A O   1 
HETATM 4470 O O   . HOH H 6 .   ? -35.226 2.557  1.373   1.00 50.80 ? 855 HOH A O   1 
HETATM 4471 O O   . HOH H 6 .   ? -14.872 32.953 -7.079  1.00 46.05 ? 856 HOH A O   1 
HETATM 4472 O O   . HOH H 6 .   ? -38.763 1.635  5.679   1.00 51.65 ? 857 HOH A O   1 
HETATM 4473 O O   . HOH H 6 .   ? -29.462 35.810 31.460  1.00 38.70 ? 858 HOH A O   1 
HETATM 4474 O O   . HOH H 6 .   ? -11.136 20.821 -0.301  1.00 32.66 ? 859 HOH A O   1 
HETATM 4475 O O   . HOH H 6 .   ? -23.034 10.045 -4.125  1.00 48.75 ? 860 HOH A O   1 
HETATM 4476 O O   . HOH H 6 .   ? -18.330 29.798 55.011  1.00 43.25 ? 861 HOH A O   1 
HETATM 4477 O O   . HOH H 6 .   ? -23.773 7.627  35.970  1.00 26.76 ? 862 HOH A O   1 
HETATM 4478 O O   . HOH H 6 .   ? -17.000 21.537 -4.042  1.00 44.37 ? 863 HOH A O   1 
HETATM 4479 O O   . HOH H 6 .   ? -52.788 20.581 38.755  1.00 48.00 ? 864 HOH A O   1 
HETATM 4480 O O   . HOH H 6 .   ? -30.137 18.044 -2.756  1.00 25.45 ? 865 HOH A O   1 
HETATM 4481 O O   . HOH H 6 .   ? -10.480 23.169 50.901  1.00 41.26 ? 866 HOH A O   1 
HETATM 4482 O O   . HOH H 6 .   ? -42.970 8.651  15.903  1.00 36.31 ? 867 HOH A O   1 
HETATM 4483 O O   . HOH H 6 .   ? -25.824 17.819 -7.562  1.00 35.19 ? 868 HOH A O   1 
HETATM 4484 O O   . HOH H 6 .   ? -30.110 10.322 50.124  1.00 40.08 ? 869 HOH A O   1 
HETATM 4485 O O   . HOH H 6 .   ? -29.661 1.376  16.902  1.00 35.92 ? 870 HOH A O   1 
HETATM 4486 O O   . HOH H 6 .   ? -34.389 17.802 -6.193  1.00 33.29 ? 871 HOH A O   1 
HETATM 4487 O O   . HOH H 6 .   ? -34.581 30.230 41.564  1.00 35.67 ? 872 HOH A O   1 
HETATM 4488 O O   . HOH H 6 .   ? -30.071 32.739 2.593   1.00 41.21 ? 873 HOH A O   1 
HETATM 4489 O O   . HOH H 6 .   ? -38.181 4.244  36.219  1.00 49.31 ? 874 HOH A O   1 
HETATM 4490 O O   . HOH H 6 .   ? -22.712 5.877  23.423  1.00 43.39 ? 875 HOH A O   1 
HETATM 4491 O O   . HOH H 6 .   ? -2.509  18.189 33.256  1.00 37.23 ? 876 HOH A O   1 
HETATM 4492 O O   . HOH H 6 .   ? -6.445  6.086  8.860   1.00 55.24 ? 877 HOH A O   1 
HETATM 4493 O O   . HOH H 6 .   ? -57.088 13.403 14.736  1.00 32.33 ? 878 HOH A O   1 
HETATM 4494 O O   . HOH H 6 .   ? -6.929  23.285 45.005  1.00 36.24 ? 879 HOH A O   1 
HETATM 4495 O O   . HOH H 6 .   ? -19.363 20.991 56.566  1.00 46.23 ? 880 HOH A O   1 
HETATM 4496 O O   . HOH H 6 .   ? -28.972 25.724 21.345  1.00 40.96 ? 881 HOH A O   1 
HETATM 4497 O O   . HOH H 6 .   ? -52.872 25.881 37.367  1.00 46.47 ? 882 HOH A O   1 
HETATM 4498 O O   . HOH H 6 .   ? -30.629 2.002  5.584   1.00 50.37 ? 883 HOH A O   1 
HETATM 4499 O O   . HOH H 6 .   ? -20.562 14.941 -3.305  1.00 35.75 ? 884 HOH A O   1 
HETATM 4500 O O   . HOH H 6 .   ? -48.778 26.728 -1.991  1.00 32.97 ? 885 HOH A O   1 
HETATM 4501 O O   . HOH H 6 .   ? -47.578 34.506 12.112  1.00 40.90 ? 886 HOH A O   1 
HETATM 4502 O O   . HOH H 6 .   ? -7.691  11.654 12.744  1.00 36.62 ? 887 HOH A O   1 
HETATM 4503 O O   . HOH H 6 .   ? -17.813 27.996 20.497  1.00 39.41 ? 888 HOH A O   1 
HETATM 4504 O O   . HOH H 6 .   ? -33.790 2.151  29.521  1.00 36.48 ? 889 HOH A O   1 
HETATM 4505 O O   . HOH H 6 .   ? -9.626  16.385 28.613  1.00 42.05 ? 890 HOH A O   1 
HETATM 4506 O O   . HOH H 6 .   ? -48.192 15.852 -6.474  1.00 42.18 ? 891 HOH A O   1 
HETATM 4507 O O   . HOH H 6 .   ? -31.847 18.221 -5.881  1.00 41.73 ? 892 HOH A O   1 
HETATM 4508 O O   . HOH H 6 .   ? -41.003 34.452 33.432  1.00 22.87 ? 893 HOH A O   1 
HETATM 4509 O O   . HOH H 6 .   ? -23.272 12.485 -3.071  1.00 40.59 ? 894 HOH A O   1 
HETATM 4510 O O   . HOH H 6 .   ? -18.303 25.651 22.182  1.00 26.21 ? 895 HOH A O   1 
HETATM 4511 O O   . HOH H 6 .   ? -34.232 32.291 -1.326  1.00 47.04 ? 896 HOH A O   1 
HETATM 4512 O O   . HOH H 6 .   ? -20.243 32.273 5.826   1.00 44.28 ? 897 HOH A O   1 
HETATM 4513 O O   . HOH H 6 .   ? -31.041 0.260  19.175  1.00 34.93 ? 898 HOH A O   1 
HETATM 4514 O O   . HOH H 6 .   ? -19.738 13.177 -5.684  1.00 46.82 ? 899 HOH A O   1 
HETATM 4515 O O   . HOH H 6 .   ? -50.860 41.580 25.944  1.00 42.89 ? 900 HOH A O   1 
HETATM 4516 O O   . HOH H 6 .   ? -20.780 4.582  -0.063  1.00 41.67 ? 901 HOH A O   1 
HETATM 4517 O O   . HOH H 6 .   ? -31.803 8.560  -0.311  1.00 47.99 ? 902 HOH A O   1 
HETATM 4518 O O   . HOH H 6 .   ? -28.218 20.089 -6.510  1.00 32.01 ? 903 HOH A O   1 
HETATM 4519 O O   . HOH H 6 .   ? -5.893  11.355 6.330   1.00 52.02 ? 904 HOH A O   1 
HETATM 4520 O O   . HOH H 6 .   ? -26.328 35.434 -1.891  1.00 50.72 ? 905 HOH A O   1 
HETATM 4521 O O   . HOH H 6 .   ? -58.616 24.568 0.872   1.00 42.81 ? 906 HOH A O   1 
HETATM 4522 O O   . HOH H 6 .   ? -28.745 26.945 23.593  1.00 40.23 ? 907 HOH A O   1 
HETATM 4523 O O   . HOH H 6 .   ? -21.081 24.765 56.673  1.00 45.55 ? 908 HOH A O   1 
HETATM 4524 O O   . HOH H 6 .   ? -51.175 26.789 37.442  1.00 44.72 ? 909 HOH A O   1 
HETATM 4525 O O   . HOH H 6 .   ? -24.059 8.672  48.412  1.00 55.59 ? 910 HOH A O   1 
HETATM 4526 O O   . HOH H 6 .   ? -41.764 2.291  9.314   1.00 46.06 ? 911 HOH A O   1 
HETATM 4527 O O   . HOH H 6 .   ? -51.035 40.335 18.743  1.00 49.17 ? 912 HOH A O   1 
HETATM 4528 O O   . HOH H 6 .   ? -23.248 7.663  38.966  1.00 41.72 ? 913 HOH A O   1 
HETATM 4529 O O   . HOH H 6 .   ? -46.920 14.793 -7.592  1.00 45.67 ? 914 HOH A O   1 
HETATM 4530 O O   . HOH H 6 .   ? -35.731 43.827 31.183  1.00 34.74 ? 915 HOH A O   1 
HETATM 4531 O O   . HOH H 6 .   ? -28.128 -3.991 12.322  1.00 51.41 ? 916 HOH A O   1 
HETATM 4532 O O   . HOH H 6 .   ? -20.509 32.682 2.761   1.00 47.59 ? 917 HOH A O   1 
HETATM 4533 O O   . HOH H 6 .   ? -26.782 28.930 -7.939  1.00 46.74 ? 918 HOH A O   1 
HETATM 4534 O O   . HOH H 6 .   ? -17.180 12.371 -5.944  1.00 52.79 ? 919 HOH A O   1 
HETATM 4535 O O   . HOH H 6 .   ? -28.395 12.952 54.523  1.00 37.30 ? 920 HOH A O   1 
HETATM 4536 O O   . HOH H 6 .   ? -49.501 36.218 10.948  1.00 52.78 ? 921 HOH A O   1 
HETATM 4537 O O   . HOH H 6 .   ? -33.010 0.041  29.919  1.00 46.24 ? 922 HOH A O   1 
HETATM 4538 O O   . HOH H 6 .   ? -56.104 10.948 15.654  1.00 43.93 ? 923 HOH A O   1 
HETATM 4539 O O   . HOH H 6 .   ? -5.805  10.163 12.849  1.00 48.92 ? 924 HOH A O   1 
HETATM 4540 O O   . HOH H 6 .   ? -27.225 25.868 22.782  1.00 41.82 ? 925 HOH A O   1 
HETATM 4541 O O   . HOH H 6 .   ? -63.520 24.706 8.516   1.00 45.26 ? 926 HOH A O   1 
HETATM 4542 O O   . HOH H 6 .   ? -51.455 41.484 23.413  1.00 53.71 ? 927 HOH A O   1 
HETATM 4543 O O   . HOH H 6 .   ? -30.420 32.198 48.656  1.00 40.84 ? 928 HOH A O   1 
HETATM 4544 O O   . HOH H 6 .   ? -22.995 33.479 1.414   1.00 45.76 ? 929 HOH A O   1 
HETATM 4545 O O   . HOH H 6 .   ? -26.002 34.396 30.322  1.00 35.17 ? 930 HOH A O   1 
HETATM 4546 O O   . HOH H 6 .   ? -36.916 4.256  39.059  1.00 45.74 ? 931 HOH A O   1 
HETATM 4547 O O   . HOH H 6 .   ? -54.901 10.123 18.048  1.00 42.58 ? 932 HOH A O   1 
HETATM 4548 O O   . HOH H 6 .   ? -57.822 11.316 14.422  1.00 43.35 ? 933 HOH A O   1 
HETATM 4549 O O   . HOH H 6 .   ? -33.203 4.566  31.560  1.00 27.11 ? 934 HOH A O   1 
HETATM 4550 O O   . HOH H 6 .   ? -13.590 31.611 32.781  1.00 52.72 ? 935 HOH A O   1 
HETATM 4551 O O   . HOH H 6 .   ? -41.266 5.897  36.778  1.00 40.47 ? 936 HOH A O   1 
HETATM 4552 O O   . HOH H 6 .   ? -40.306 38.291 36.688  1.00 42.91 ? 937 HOH A O   1 
HETATM 4553 O O   . HOH H 6 .   ? -47.175 35.827 10.929  1.00 41.48 ? 938 HOH A O   1 
HETATM 4554 O O   . HOH H 6 .   ? -54.868 35.637 28.196  1.00 38.62 ? 939 HOH A O   1 
HETATM 4555 O O   . HOH H 6 .   ? -26.214 27.446 23.880  1.00 41.98 ? 940 HOH A O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . MET A 1   ? 0.4362 0.7815 0.5987 0.0666  -0.0301 0.0441  1   MET A N   
2    C CA  . MET A 1   ? 0.3833 0.7065 0.5358 0.0794  -0.0263 0.0461  1   MET A CA  
3    C C   . MET A 1   ? 0.3280 0.6290 0.4677 0.0774  -0.0292 0.0465  1   MET A C   
4    O O   . MET A 1   ? 0.3622 0.6591 0.5001 0.0653  -0.0306 0.0441  1   MET A O   
5    C CB  . MET A 1   ? 0.4019 0.7184 0.5559 0.0808  -0.0177 0.0445  1   MET A CB  
6    C CG  . MET A 1   ? 0.4610 0.7489 0.6029 0.0853  -0.0141 0.0444  1   MET A CG  
7    S SD  . MET A 1   ? 0.4988 0.7803 0.6417 0.0848  -0.0045 0.0415  1   MET A SD  
8    C CE  . MET A 1   ? 0.5388 0.8370 0.6906 0.0658  -0.0050 0.0397  1   MET A CE  
9    N N   . LYS A 2   ? 0.2587 0.5448 0.3892 0.0891  -0.0300 0.0499  2   LYS A N   
10   C CA  . LYS A 2   ? 0.1745 0.4380 0.2917 0.0888  -0.0320 0.0511  2   LYS A CA  
11   C C   . LYS A 2   ? 0.2091 0.4520 0.3213 0.0883  -0.0256 0.0496  2   LYS A C   
12   O O   . LYS A 2   ? 0.2209 0.4520 0.3309 0.0980  -0.0204 0.0503  2   LYS A O   
13   C CB  . LYS A 2   ? 0.2168 0.4705 0.3258 0.1010  -0.0343 0.0559  2   LYS A CB  
14   C CG  . LYS A 2   ? 0.2343 0.4644 0.3290 0.1010  -0.0358 0.0582  2   LYS A CG  
15   C CD  . LYS A 2   ? 0.2543 0.4722 0.3411 0.1134  -0.0366 0.0636  2   LYS A CD  
16   C CE  . LYS A 2   ? 0.2791 0.4800 0.3648 0.1233  -0.0300 0.0642  2   LYS A CE  
17   N NZ  . LYS A 2   ? 0.2957 0.4839 0.3743 0.1348  -0.0310 0.0695  2   LYS A NZ  
18   N N   . LYS A 3   ? 0.1348 0.3728 0.2448 0.0772  -0.0262 0.0473  3   LYS A N   
19   C CA  . LYS A 3   ? 0.1272 0.3469 0.2326 0.0758  -0.0207 0.0459  3   LYS A CA  
20   C C   . LYS A 3   ? 0.1537 0.3503 0.2459 0.0778  -0.0223 0.0480  3   LYS A C   
21   O O   . LYS A 3   ? 0.1862 0.3824 0.2725 0.0771  -0.0278 0.0500  3   LYS A O   
22   C CB  . LYS A 3   ? 0.2104 0.4393 0.3225 0.0620  -0.0197 0.0424  3   LYS A CB  
23   C CG  . LYS A 3   ? 0.2872 0.5346 0.4111 0.0597  -0.0158 0.0407  3   LYS A CG  
24   C CD  . LYS A 3   ? 0.3799 0.6336 0.5091 0.0445  -0.0149 0.0380  3   LYS A CD  
25   C CE  . LYS A 3   ? 0.4522 0.7219 0.5916 0.0419  -0.0098 0.0372  3   LYS A CE  
26   N NZ  . LYS A 3   ? 0.5216 0.7821 0.6583 0.0506  -0.0020 0.0371  3   LYS A NZ  
27   N N   . LEU A 4   ? 0.1421 0.3184 0.2286 0.0798  -0.0169 0.0473  4   LEU A N   
28   C CA  . LEU A 4   ? 0.1826 0.3318 0.2548 0.0758  -0.0167 0.0471  4   LEU A CA  
29   C C   . LEU A 4   ? 0.1741 0.3175 0.2448 0.0616  -0.0151 0.0420  4   LEU A C   
30   O O   . LEU A 4   ? 0.1688 0.3142 0.2445 0.0586  -0.0105 0.0391  4   LEU A O   
31   C CB  . LEU A 4   ? 0.2024 0.3278 0.2672 0.0849  -0.0116 0.0483  4   LEU A CB  
32   C CG  . LEU A 4   ? 0.1713 0.2691 0.2225 0.0805  -0.0106 0.0483  4   LEU A CG  
33   C CD1 . LEU A 4   ? 0.2076 0.2868 0.2520 0.0918  -0.0089 0.0526  4   LEU A CD1 
34   C CD2 . LEU A 4   ? 0.1572 0.2429 0.2061 0.0714  -0.0060 0.0428  4   LEU A CD2 
35   N N   . PHE A 5   ? 0.1224 0.2589 0.1859 0.0536  -0.0186 0.0410  5   PHE A N   
36   C CA  . PHE A 5   ? 0.1459 0.2747 0.2069 0.0411  -0.0175 0.0363  5   PHE A CA  
37   C C   . PHE A 5   ? 0.1539 0.2562 0.2035 0.0407  -0.0138 0.0356  5   PHE A C   
38   O O   . PHE A 5   ? 0.2016 0.2929 0.2424 0.0432  -0.0154 0.0379  5   PHE A O   
39   C CB  . PHE A 5   ? 0.1222 0.2601 0.1825 0.0326  -0.0236 0.0344  5   PHE A CB  
40   C CG  . PHE A 5   ? 0.1367 0.3020 0.2093 0.0303  -0.0278 0.0342  5   PHE A CG  
41   C CD1 . PHE A 5   ? 0.1548 0.3327 0.2386 0.0262  -0.0249 0.0327  5   PHE A CD1 
42   C CD2 . PHE A 5   ? 0.1575 0.3374 0.2303 0.0321  -0.0346 0.0356  5   PHE A CD2 
43   C CE1 . PHE A 5   ? 0.1492 0.3542 0.2457 0.0231  -0.0286 0.0327  5   PHE A CE1 
44   C CE2 . PHE A 5   ? 0.1617 0.3689 0.2467 0.0294  -0.0391 0.0351  5   PHE A CE2 
45   C CZ  . PHE A 5   ? 0.1432 0.3634 0.2409 0.0246  -0.0359 0.0337  5   PHE A CZ  
46   N N   . LEU A 6   ? 0.1400 0.2337 0.1900 0.0374  -0.0090 0.0328  6   LEU A N   
47   C CA  . LEU A 6   ? 0.1397 0.2109 0.1807 0.0371  -0.0053 0.0317  6   LEU A CA  
48   C C   . LEU A 6   ? 0.1235 0.1883 0.1616 0.0265  -0.0050 0.0281  6   LEU A C   
49   O O   . LEU A 6   ? 0.1423 0.2155 0.1861 0.0209  -0.0042 0.0261  6   LEU A O   
50   C CB  . LEU A 6   ? 0.1464 0.2129 0.1892 0.0434  -0.0002 0.0312  6   LEU A CB  
51   C CG  . LEU A 6   ? 0.1880 0.2322 0.2221 0.0434  0.0033  0.0296  6   LEU A CG  
52   C CD1 . LEU A 6   ? 0.1760 0.2066 0.2026 0.0471  0.0017  0.0328  6   LEU A CD1 
53   C CD2 . LEU A 6   ? 0.1880 0.2303 0.2240 0.0499  0.0078  0.0279  6   LEU A CD2 
54   N N   . VAL A 7   ? 0.1253 0.1756 0.1547 0.0241  -0.0055 0.0276  7   VAL A N   
55   C CA  . VAL A 7   ? 0.1518 0.1958 0.1779 0.0154  -0.0057 0.0243  7   VAL A CA  
56   C C   . VAL A 7   ? 0.1407 0.1672 0.1600 0.0155  -0.0024 0.0236  7   VAL A C   
57   O O   . VAL A 7   ? 0.1509 0.1690 0.1641 0.0176  -0.0027 0.0252  7   VAL A O   
58   C CB  . VAL A 7   ? 0.1224 0.1697 0.1451 0.0118  -0.0103 0.0235  7   VAL A CB  
59   C CG1 . VAL A 7   ? 0.1648 0.2067 0.1854 0.0034  -0.0106 0.0194  7   VAL A CG1 
60   C CG2 . VAL A 7   ? 0.1579 0.2237 0.1868 0.0129  -0.0145 0.0247  7   VAL A CG2 
61   N N   . PHE A 8   ? 0.1369 0.1591 0.1571 0.0129  0.0007  0.0214  8   PHE A N   
62   C CA  . PHE A 8   ? 0.1353 0.1433 0.1497 0.0118  0.0031  0.0201  8   PHE A CA  
63   C C   . PHE A 8   ? 0.1450 0.1492 0.1564 0.0056  0.0017  0.0180  8   PHE A C   
64   O O   . PHE A 8   ? 0.1567 0.1658 0.1708 0.0011  0.0007  0.0167  8   PHE A O   
65   C CB  . PHE A 8   ? 0.1499 0.1557 0.1656 0.0124  0.0066  0.0186  8   PHE A CB  
66   C CG  . PHE A 8   ? 0.1598 0.1653 0.1767 0.0195  0.0086  0.0193  8   PHE A CG  
67   C CD1 . PHE A 8   ? 0.1787 0.1710 0.1905 0.0225  0.0101  0.0189  8   PHE A CD1 
68   C CD2 . PHE A 8   ? 0.1429 0.1613 0.1662 0.0232  0.0092  0.0202  8   PHE A CD2 
69   C CE1 . PHE A 8   ? 0.1908 0.1801 0.2029 0.0295  0.0119  0.0190  8   PHE A CE1 
70   C CE2 . PHE A 8   ? 0.1938 0.2115 0.2180 0.0312  0.0114  0.0205  8   PHE A CE2 
71   C CZ  . PHE A 8   ? 0.2016 0.2034 0.2196 0.0346  0.0127  0.0197  8   PHE A CZ  
72   N N   . TRP A 9   ? 0.1552 0.1503 0.1610 0.0054  0.0020  0.0179  9   TRP A N   
73   C CA  . TRP A 9   ? 0.1525 0.1436 0.1551 0.0010  0.0012  0.0156  9   TRP A CA  
74   C C   . TRP A 9   ? 0.1542 0.1362 0.1537 0.0011  0.0036  0.0150  9   TRP A C   
75   O O   . TRP A 9   ? 0.1504 0.1284 0.1471 0.0026  0.0043  0.0165  9   TRP A O   
76   C CB  . TRP A 9   ? 0.1593 0.1529 0.1586 0.0007  -0.0014 0.0155  9   TRP A CB  
77   C CG  . TRP A 9   ? 0.1208 0.1122 0.1173 -0.0031 -0.0026 0.0121  9   TRP A CG  
78   C CD1 . TRP A 9   ? 0.1830 0.1687 0.1794 -0.0056 -0.0016 0.0099  9   TRP A CD1 
79   C CD2 . TRP A 9   ? 0.1182 0.1125 0.1107 -0.0038 -0.0053 0.0104  9   TRP A CD2 
80   N NE1 . TRP A 9   ? 0.1575 0.1412 0.1504 -0.0075 -0.0033 0.0067  9   TRP A NE1 
81   C CE2 . TRP A 9   ? 0.1455 0.1345 0.1358 -0.0066 -0.0055 0.0065  9   TRP A CE2 
82   C CE3 . TRP A 9   ? 0.1499 0.1509 0.1399 -0.0019 -0.0077 0.0118  9   TRP A CE3 
83   C CZ2 . TRP A 9   ? 0.1613 0.1507 0.1466 -0.0076 -0.0077 0.0030  9   TRP A CZ2 
84   C CZ3 . TRP A 9   ? 0.1541 0.1570 0.1389 -0.0034 -0.0101 0.0086  9   TRP A CZ3 
85   C CH2 . TRP A 9   ? 0.1810 0.1778 0.1634 -0.0062 -0.0101 0.0037  9   TRP A CH2 
86   N N   . TRP A 10  ? 0.1531 0.1329 0.1534 -0.0008 0.0048  0.0134  10  TRP A N   
87   C CA  . TRP A 10  ? 0.1778 0.1513 0.1759 -0.0009 0.0065  0.0125  10  TRP A CA  
88   C C   . TRP A 10  ? 0.1704 0.1417 0.1664 -0.0030 0.0058  0.0111  10  TRP A C   
89   O O   . TRP A 10  ? 0.1821 0.1537 0.1783 -0.0046 0.0050  0.0101  10  TRP A O   
90   C CB  . TRP A 10  ? 0.1750 0.1487 0.1743 -0.0009 0.0079  0.0117  10  TRP A CB  
91   C CG  . TRP A 10  ? 0.1389 0.1153 0.1402 0.0021  0.0093  0.0123  10  TRP A CG  
92   C CD1 . TRP A 10  ? 0.1434 0.1270 0.1481 0.0024  0.0100  0.0129  10  TRP A CD1 
93   C CD2 . TRP A 10  ? 0.1490 0.1207 0.1491 0.0055  0.0106  0.0122  10  TRP A CD2 
94   N NE1 . TRP A 10  ? 0.1468 0.1320 0.1527 0.0069  0.0117  0.0129  10  TRP A NE1 
95   C CE2 . TRP A 10  ? 0.1481 0.1246 0.1508 0.0091  0.0120  0.0123  10  TRP A CE2 
96   C CE3 . TRP A 10  ? 0.1554 0.1192 0.1529 0.0057  0.0108  0.0121  10  TRP A CE3 
97   C CZ2 . TRP A 10  ? 0.1648 0.1367 0.1666 0.0138  0.0134  0.0117  10  TRP A CZ2 
98   C CZ3 . TRP A 10  ? 0.1582 0.1161 0.1547 0.0092  0.0121  0.0119  10  TRP A CZ3 
99   C CH2 . TRP A 10  ? 0.1767 0.1379 0.1751 0.0138  0.0133  0.0115  10  TRP A CH2 
100  N N   . HIS A 11  ? 0.1382 0.1074 0.1322 -0.0028 0.0064  0.0113  11  HIS A N   
101  C CA  . HIS A 11  ? 0.1432 0.1125 0.1355 -0.0035 0.0062  0.0099  11  HIS A CA  
102  C C   . HIS A 11  ? 0.1414 0.1095 0.1344 -0.0041 0.0069  0.0088  11  HIS A C   
103  O O   . HIS A 11  ? 0.1476 0.1149 0.1411 -0.0047 0.0080  0.0092  11  HIS A O   
104  C CB  . HIS A 11  ? 0.1536 0.1243 0.1437 -0.0031 0.0068  0.0112  11  HIS A CB  
105  C CG  . HIS A 11  ? 0.1621 0.1344 0.1512 -0.0034 0.0078  0.0101  11  HIS A CG  
106  N ND1 . HIS A 11  ? 0.1491 0.1224 0.1369 -0.0024 0.0070  0.0074  11  HIS A ND1 
107  C CD2 . HIS A 11  ? 0.1710 0.1446 0.1609 -0.0044 0.0096  0.0112  11  HIS A CD2 
108  C CE1 . HIS A 11  ? 0.1596 0.1359 0.1475 -0.0018 0.0086  0.0069  11  HIS A CE1 
109  N NE2 . HIS A 11  ? 0.1674 0.1450 0.1570 -0.0036 0.0101  0.0093  11  HIS A NE2 
110  N N   . MET A 12  ? 0.1314 0.0990 0.1240 -0.0038 0.0061  0.0075  12  MET A N   
111  C CA  . MET A 12  ? 0.1282 0.0961 0.1214 -0.0034 0.0061  0.0068  12  MET A CA  
112  C C   . MET A 12  ? 0.1326 0.1026 0.1255 -0.0017 0.0061  0.0056  12  MET A C   
113  O O   . MET A 12  ? 0.1571 0.1251 0.1483 -0.0003 0.0055  0.0044  12  MET A O   
114  C CB  . MET A 12  ? 0.1379 0.1033 0.1305 -0.0032 0.0054  0.0073  12  MET A CB  
115  C CG  . MET A 12  ? 0.1504 0.1157 0.1435 -0.0044 0.0059  0.0084  12  MET A CG  
116  S SD  . MET A 12  ? 0.1554 0.1218 0.1487 -0.0043 0.0071  0.0079  12  MET A SD  
117  C CE  . MET A 12  ? 0.1874 0.1551 0.1810 -0.0041 0.0082  0.0089  12  MET A CE  
118  N N   . HIS A 13  ? 0.1486 0.1231 0.1434 -0.0018 0.0067  0.0054  13  HIS A N   
119  C CA  . HIS A 13  ? 0.1434 0.1228 0.1391 0.0004  0.0072  0.0044  13  HIS A CA  
120  C C   . HIS A 13  ? 0.1310 0.1172 0.1303 0.0002  0.0071  0.0043  13  HIS A C   
121  O O   . HIS A 13  ? 0.1387 0.1261 0.1396 -0.0033 0.0072  0.0047  13  HIS A O   
122  C CB  . HIS A 13  ? 0.1371 0.1197 0.1322 -0.0003 0.0091  0.0047  13  HIS A CB  
123  C CG  . HIS A 13  ? 0.1212 0.1116 0.1177 0.0019  0.0105  0.0037  13  HIS A CG  
124  N ND1 . HIS A 13  ? 0.1402 0.1310 0.1358 0.0066  0.0101  0.0014  13  HIS A ND1 
125  C CD2 . HIS A 13  ? 0.1349 0.1334 0.1340 0.0001  0.0128  0.0049  13  HIS A CD2 
126  C CE1 . HIS A 13  ? 0.1503 0.1506 0.1481 0.0085  0.0121  0.0009  13  HIS A CE1 
127  N NE2 . HIS A 13  ? 0.1444 0.1503 0.1446 0.0040  0.0139  0.0032  13  HIS A NE2 
128  N N   . GLN A 14  ? 0.1150 0.1058 0.1156 0.0040  0.0067  0.0034  14  GLN A N   
129  C CA  . GLN A 14  ? 0.1147 0.1164 0.1202 0.0041  0.0065  0.0032  14  GLN A CA  
130  C C   . GLN A 14  ? 0.1296 0.1381 0.1367 0.0088  0.0078  0.0021  14  GLN A C   
131  O O   . GLN A 14  ? 0.1442 0.1468 0.1481 0.0138  0.0074  0.0011  14  GLN A O   
132  C CB  . GLN A 14  ? 0.1497 0.1530 0.1559 0.0054  0.0038  0.0034  14  GLN A CB  
133  C CG  . GLN A 14  ? 0.1656 0.1641 0.1696 0.0015  0.0026  0.0036  14  GLN A CG  
134  C CD  . GLN A 14  ? 0.1381 0.1402 0.1448 -0.0043 0.0033  0.0027  14  GLN A CD  
135  O OE1 . GLN A 14  ? 0.1344 0.1455 0.1459 -0.0062 0.0039  0.0023  14  GLN A OE1 
136  N NE2 . GLN A 14  ? 0.1530 0.1478 0.1569 -0.0071 0.0033  0.0024  14  GLN A NE2 
137  N N   . PRO A 15  ? 0.1195 0.1400 0.1315 0.0074  0.0097  0.0022  15  PRO A N   
138  C CA  . PRO A 15  ? 0.1243 0.1545 0.1387 0.0131  0.0112  0.0009  15  PRO A CA  
139  C C   . PRO A 15  ? 0.1442 0.1783 0.1611 0.0189  0.0087  0.0005  15  PRO A C   
140  O O   . PRO A 15  ? 0.1519 0.1842 0.1692 0.0174  0.0058  0.0015  15  PRO A O   
141  C CB  . PRO A 15  ? 0.1527 0.1967 0.1730 0.0084  0.0139  0.0020  15  PRO A CB  
142  C CG  . PRO A 15  ? 0.1377 0.1808 0.1606 0.0012  0.0119  0.0032  15  PRO A CG  
143  C CD  . PRO A 15  ? 0.1383 0.1647 0.1544 0.0005  0.0103  0.0033  15  PRO A CD  
144  N N   . LEU A 16  ? 0.1471 0.1868 0.1652 0.0263  0.0097  -0.0010 16  LEU A N   
145  C CA  . LEU A 16  ? 0.1180 0.1603 0.1379 0.0337  0.0072  -0.0009 16  LEU A CA  
146  C C   . LEU A 16  ? 0.1521 0.2131 0.1806 0.0322  0.0059  0.0002  16  LEU A C   
147  O O   . LEU A 16  ? 0.1358 0.2132 0.1709 0.0326  0.0082  -0.0004 16  LEU A O   
148  C CB  . LEU A 16  ? 0.1417 0.1830 0.1599 0.0433  0.0088  -0.0033 16  LEU A CB  
149  C CG  . LEU A 16  ? 0.1309 0.1710 0.1495 0.0527  0.0061  -0.0026 16  LEU A CG  
150  C CD1 . LEU A 16  ? 0.1971 0.2201 0.2098 0.0513  0.0027  -0.0001 16  LEU A CD1 
151  C CD2 . LEU A 16  ? 0.1539 0.1902 0.1700 0.0626  0.0081  -0.0059 16  LEU A CD2 
152  N N   . TYR A 17  ? 0.1302 0.1900 0.1586 0.0303  0.0021  0.0017  17  TYR A N   
153  C CA  . TYR A 17  ? 0.1469 0.2247 0.1830 0.0284  -0.0002 0.0021  17  TYR A CA  
154  C C   . TYR A 17  ? 0.1655 0.2537 0.2051 0.0385  -0.0025 0.0028  17  TYR A C   
155  O O   . TYR A 17  ? 0.1449 0.2514 0.1920 0.0380  -0.0049 0.0030  17  TYR A O   
156  C CB  . TYR A 17  ? 0.1404 0.2132 0.1737 0.0218  -0.0035 0.0026  17  TYR A CB  
157  C CG  . TYR A 17  ? 0.1248 0.1892 0.1559 0.0123  -0.0015 0.0019  17  TYR A CG  
158  C CD1 . TYR A 17  ? 0.1896 0.2632 0.2266 0.0058  0.0009  0.0012  17  TYR A CD1 
159  C CD2 . TYR A 17  ? 0.1311 0.1786 0.1545 0.0103  -0.0018 0.0023  17  TYR A CD2 
160  C CE1 . TYR A 17  ? 0.1355 0.1996 0.1699 -0.0020 0.0028  0.0012  17  TYR A CE1 
161  C CE2 . TYR A 17  ? 0.1315 0.1714 0.1530 0.0032  0.0000  0.0018  17  TYR A CE2 
162  C CZ  . TYR A 17  ? 0.1558 0.2031 0.1825 -0.0026 0.0021  0.0013  17  TYR A CZ  
163  O OH  . TYR A 17  ? 0.1575 0.1954 0.1818 -0.0089 0.0038  0.0015  17  TYR A OH  
164  N N   . ARG A 18  ? 0.1641 0.2411 0.1987 0.0478  -0.0020 0.0030  18  ARG A N   
165  C CA  . ARG A 18  ? 0.1641 0.2470 0.2006 0.0591  -0.0043 0.0043  18  ARG A CA  
166  C C   . ARG A 18  ? 0.1664 0.2676 0.2111 0.0652  -0.0015 0.0023  18  ARG A C   
167  O O   . ARG A 18  ? 0.1817 0.2766 0.2237 0.0691  0.0024  0.0000  18  ARG A O   
168  C CB  . ARG A 18  ? 0.1637 0.2238 0.1907 0.0659  -0.0048 0.0055  18  ARG A CB  
169  C CG  . ARG A 18  ? 0.2183 0.2796 0.2453 0.0779  -0.0078 0.0081  18  ARG A CG  
170  C CD  . ARG A 18  ? 0.2843 0.3198 0.3017 0.0837  -0.0074 0.0089  18  ARG A CD  
171  N NE  . ARG A 18  ? 0.2962 0.3286 0.3120 0.0953  -0.0104 0.0125  18  ARG A NE  
172  C CZ  . ARG A 18  ? 0.3095 0.3482 0.3289 0.1075  -0.0098 0.0114  18  ARG A CZ  
173  N NH1 . ARG A 18  ? 0.2740 0.3239 0.2989 0.1092  -0.0060 0.0064  18  ARG A NH1 
174  N NH2 . ARG A 18  ? 0.4350 0.4688 0.4522 0.1171  -0.0128 0.0154  18  ARG A NH2 
175  N N   . GLU A 19  ? 0.1414 0.2664 0.1960 0.0663  -0.0034 0.0030  19  GLU A N   
176  C CA  . GLU A 19  ? 0.1538 0.3005 0.2179 0.0723  -0.0005 0.0015  19  GLU A CA  
177  C C   . GLU A 19  ? 0.2188 0.3596 0.2801 0.0880  -0.0003 0.0013  19  GLU A C   
178  O O   . GLU A 19  ? 0.2362 0.3700 0.2942 0.0950  -0.0047 0.0039  19  GLU A O   
179  C CB  . GLU A 19  ? 0.1767 0.3516 0.2530 0.0691  -0.0035 0.0025  19  GLU A CB  
180  C CG  . GLU A 19  ? 0.2083 0.4096 0.2967 0.0682  0.0008  0.0011  19  GLU A CG  
181  C CD  . GLU A 19  ? 0.2805 0.4951 0.3737 0.0813  0.0008  0.0010  19  GLU A CD  
182  O OE1 . GLU A 19  ? 0.3022 0.5048 0.3895 0.0913  -0.0027 0.0023  19  GLU A OE1 
183  O OE2 . GLU A 19  ? 0.4163 0.6483 0.5168 0.0798  0.0044  0.0000  19  GLU A OE2 
184  N N   . PRO A 20  ? 0.2162 0.3587 0.2779 0.0943  0.0046  -0.0019 20  PRO A N   
185  C CA  . PRO A 20  ? 0.2889 0.4172 0.3445 0.1083  0.0050  -0.0032 20  PRO A CA  
186  C C   . PRO A 20  ? 0.3311 0.4698 0.3910 0.1166  0.0026  -0.0016 20  PRO A C   
187  O O   . PRO A 20  ? 0.3967 0.5178 0.4497 0.1255  0.0014  -0.0013 20  PRO A O   
188  C CB  . PRO A 20  ? 0.2858 0.4124 0.3388 0.1090  0.0112  -0.0079 20  PRO A CB  
189  C CG  . PRO A 20  ? 0.1873 0.3394 0.2501 0.0999  0.0143  -0.0078 20  PRO A CG  
190  C CD  . PRO A 20  ? 0.1813 0.3332 0.2458 0.0875  0.0102  -0.0043 20  PRO A CD  
191  N N   . TYR A 21  ? 0.2307 0.3967 0.3017 0.1135  0.0017  -0.0005 21  TYR A N   
192  C CA  . TYR A 21  ? 0.2290 0.4065 0.3044 0.1220  -0.0005 0.0009  21  TYR A CA  
193  C C   . TYR A 21  ? 0.3450 0.5223 0.4199 0.1226  -0.0071 0.0054  21  TYR A C   
194  O O   . TYR A 21  ? 0.3914 0.5634 0.4636 0.1322  -0.0096 0.0075  21  TYR A O   
195  C CB  . TYR A 21  ? 0.1880 0.3956 0.2755 0.1187  0.0021  -0.0003 21  TYR A CB  
196  C CG  . TYR A 21  ? 0.2770 0.4850 0.3635 0.1207  0.0088  -0.0041 21  TYR A CG  
197  C CD1 . TYR A 21  ? 0.2204 0.4252 0.3045 0.1325  0.0108  -0.0062 21  TYR A CD1 
198  C CD2 . TYR A 21  ? 0.3062 0.5167 0.3932 0.1108  0.0130  -0.0057 21  TYR A CD2 
199  C CE1 . TYR A 21  ? 0.2638 0.4691 0.3458 0.1346  0.0168  -0.0101 21  TYR A CE1 
200  C CE2 . TYR A 21  ? 0.2124 0.4232 0.2968 0.1127  0.0191  -0.0090 21  TYR A CE2 
201  C CZ  . TYR A 21  ? 0.2349 0.4434 0.3167 0.1246  0.0209  -0.0114 21  TYR A CZ  
202  O OH  . TYR A 21  ? 0.2659 0.4753 0.3444 0.1266  0.0267  -0.0151 21  TYR A OH  
203  N N   . THR A 22  ? 0.2691 0.4513 0.3456 0.1125  -0.0100 0.0069  22  THR A N   
204  C CA  . THR A 22  ? 0.2952 0.4773 0.3696 0.1122  -0.0165 0.0108  22  THR A CA  
205  C C   . THR A 22  ? 0.2835 0.4383 0.3457 0.1125  -0.0183 0.0133  22  THR A C   
206  O O   . THR A 22  ? 0.2857 0.4354 0.3429 0.1147  -0.0231 0.0173  22  THR A O   
207  C CB  . THR A 22  ? 0.2210 0.4257 0.3039 0.1003  -0.0193 0.0104  22  THR A CB  
208  O OG1 . THR A 22  ? 0.2307 0.4292 0.3123 0.0901  -0.0174 0.0088  22  THR A OG1 
209  C CG2 . THR A 22  ? 0.2699 0.5016 0.3652 0.0981  -0.0173 0.0084  22  THR A CG2 
210  N N   . GLY A 23  ? 0.2428 0.3803 0.2996 0.1100  -0.0146 0.0113  23  GLY A N   
211  C CA  . GLY A 23  ? 0.2626 0.3747 0.3082 0.1081  -0.0160 0.0137  23  GLY A CA  
212  C C   . GLY A 23  ? 0.2811 0.3943 0.3248 0.0946  -0.0185 0.0146  23  GLY A C   
213  O O   . GLY A 23  ? 0.3822 0.4744 0.4159 0.0908  -0.0193 0.0168  23  GLY A O   
214  N N   . GLU A 24  ? 0.2025 0.3390 0.2555 0.0870  -0.0194 0.0128  24  GLU A N   
215  C CA  . GLU A 24  ? 0.1990 0.3371 0.2500 0.0751  -0.0224 0.0129  24  GLU A CA  
216  C C   . GLU A 24  ? 0.1774 0.3044 0.2260 0.0627  -0.0183 0.0098  24  GLU A C   
217  O O   . GLU A 24  ? 0.1809 0.3136 0.2350 0.0598  -0.0140 0.0071  24  GLU A O   
218  C CB  . GLU A 24  ? 0.2423 0.4104 0.3043 0.0725  -0.0263 0.0120  24  GLU A CB  
219  C CG  . GLU A 24  ? 0.3106 0.4897 0.3732 0.0838  -0.0320 0.0159  24  GLU A CG  
220  C CD  . GLU A 24  ? 0.4415 0.6488 0.5158 0.0825  -0.0340 0.0143  24  GLU A CD  
221  O OE1 . GLU A 24  ? 0.5514 0.7634 0.6254 0.0910  -0.0364 0.0168  24  GLU A OE1 
222  O OE2 . GLU A 24  ? 0.3913 0.6143 0.4746 0.0720  -0.0328 0.0107  24  GLU A OE2 
223  N N   . TYR A 25  ? 0.1498 0.2617 0.1900 0.0558  -0.0196 0.0105  25  TYR A N   
224  C CA  . TYR A 25  ? 0.1516 0.2546 0.1898 0.0442  -0.0167 0.0079  25  TYR A CA  
225  C C   . TYR A 25  ? 0.1587 0.2802 0.2046 0.0350  -0.0184 0.0054  25  TYR A C   
226  O O   . TYR A 25  ? 0.1556 0.2839 0.2006 0.0326  -0.0230 0.0053  25  TYR A O   
227  C CB  . TYR A 25  ? 0.1765 0.2588 0.2036 0.0413  -0.0172 0.0095  25  TYR A CB  
228  C CG  . TYR A 25  ? 0.1535 0.2152 0.1739 0.0458  -0.0143 0.0109  25  TYR A CG  
229  C CD1 . TYR A 25  ? 0.1939 0.2491 0.2112 0.0563  -0.0154 0.0140  25  TYR A CD1 
230  C CD2 . TYR A 25  ? 0.1644 0.2129 0.1816 0.0396  -0.0108 0.0092  25  TYR A CD2 
231  C CE1 . TYR A 25  ? 0.2640 0.2989 0.2750 0.0593  -0.0130 0.0146  25  TYR A CE1 
232  C CE2 . TYR A 25  ? 0.2401 0.2711 0.2516 0.0426  -0.0087 0.0099  25  TYR A CE2 
233  C CZ  . TYR A 25  ? 0.2289 0.2526 0.2373 0.0519  -0.0098 0.0122  25  TYR A CZ  
234  O OH  . TYR A 25  ? 0.2820 0.2869 0.2847 0.0536  -0.0079 0.0122  25  TYR A OH  
235  N N   . LEU A 26  ? 0.1704 0.3004 0.2238 0.0296  -0.0148 0.0032  26  LEU A N   
236  C CA  . LEU A 26  ? 0.1667 0.3162 0.2295 0.0208  -0.0162 0.0011  26  LEU A CA  
237  C C   . LEU A 26  ? 0.1545 0.2937 0.2135 0.0085  -0.0163 -0.0011 26  LEU A C   
238  O O   . LEU A 26  ? 0.1756 0.3276 0.2407 0.0002  -0.0187 -0.0034 26  LEU A O   
239  C CB  . LEU A 26  ? 0.1482 0.3132 0.2212 0.0202  -0.0118 0.0007  26  LEU A CB  
240  C CG  . LEU A 26  ? 0.1717 0.3511 0.2503 0.0330  -0.0114 0.0019  26  LEU A CG  
241  C CD1 . LEU A 26  ? 0.1990 0.3977 0.2885 0.0313  -0.0067 0.0012  26  LEU A CD1 
242  C CD2 . LEU A 26  ? 0.1734 0.3687 0.2559 0.0386  -0.0178 0.0029  26  LEU A CD2 
243  N N   . LEU A 27  ? 0.1261 0.2428 0.1757 0.0072  -0.0139 -0.0007 27  LEU A N   
244  C CA  . LEU A 27  ? 0.1559 0.2606 0.2003 -0.0018 -0.0143 -0.0027 27  LEU A CA  
245  C C   . LEU A 27  ? 0.1543 0.2415 0.1876 0.0023  -0.0152 -0.0015 27  LEU A C   
246  O O   . LEU A 27  ? 0.1517 0.2308 0.1811 0.0100  -0.0139 0.0012  27  LEU A O   
247  C CB  . LEU A 27  ? 0.1632 0.2593 0.2084 -0.0087 -0.0094 -0.0030 27  LEU A CB  
248  C CG  . LEU A 27  ? 0.1767 0.2894 0.2327 -0.0159 -0.0082 -0.0038 27  LEU A CG  
249  C CD1 . LEU A 27  ? 0.1711 0.2753 0.2268 -0.0203 -0.0026 -0.0023 27  LEU A CD1 
250  C CD2 . LEU A 27  ? 0.2534 0.3723 0.3124 -0.0252 -0.0121 -0.0071 27  LEU A CD2 
251  N N   . PRO A 28  ? 0.1791 0.2603 0.2069 -0.0027 -0.0174 -0.0036 28  PRO A N   
252  C CA  . PRO A 28  ? 0.1721 0.2394 0.1896 0.0008  -0.0179 -0.0022 28  PRO A CA  
253  C C   . PRO A 28  ? 0.1711 0.2204 0.1834 -0.0019 -0.0139 -0.0021 28  PRO A C   
254  O O   . PRO A 28  ? 0.1612 0.2007 0.1658 -0.0008 -0.0140 -0.0015 28  PRO A O   
255  C CB  . PRO A 28  ? 0.1674 0.2405 0.1818 -0.0033 -0.0222 -0.0053 28  PRO A CB  
256  C CG  . PRO A 28  ? 0.1467 0.2249 0.1676 -0.0126 -0.0220 -0.0096 28  PRO A CG  
257  C CD  . PRO A 28  ? 0.1601 0.2490 0.1913 -0.0118 -0.0199 -0.0078 28  PRO A CD  
258  N N   . TRP A 29  ? 0.1346 0.1809 0.1510 -0.0052 -0.0105 -0.0025 29  TRP A N   
259  C CA  . TRP A 29  ? 0.1422 0.1736 0.1543 -0.0083 -0.0074 -0.0027 29  TRP A CA  
260  C C   . TRP A 29  ? 0.1435 0.1636 0.1497 -0.0031 -0.0059 0.0000  29  TRP A C   
261  O O   . TRP A 29  ? 0.1703 0.1801 0.1718 -0.0046 -0.0046 -0.0001 29  TRP A O   
262  C CB  . TRP A 29  ? 0.1614 0.1928 0.1784 -0.0123 -0.0042 -0.0026 29  TRP A CB  
263  C CG  . TRP A 29  ? 0.1347 0.1744 0.1577 -0.0200 -0.0048 -0.0049 29  TRP A CG  
264  C CD1 . TRP A 29  ? 0.1232 0.1744 0.1540 -0.0226 -0.0033 -0.0041 29  TRP A CD1 
265  C CD2 . TRP A 29  ? 0.1481 0.1841 0.1697 -0.0268 -0.0066 -0.0084 29  TRP A CD2 
266  N NE1 . TRP A 29  ? 0.1485 0.2036 0.1836 -0.0314 -0.0042 -0.0063 29  TRP A NE1 
267  C CE2 . TRP A 29  ? 0.1788 0.2236 0.2080 -0.0341 -0.0064 -0.0094 29  TRP A CE2 
268  C CE3 . TRP A 29  ? 0.1591 0.1851 0.1736 -0.0274 -0.0080 -0.0111 29  TRP A CE3 
269  C CZ2 . TRP A 29  ? 0.2057 0.2476 0.2354 -0.0425 -0.0081 -0.0132 29  TRP A CZ2 
270  C CZ3 . TRP A 29  ? 0.1631 0.1866 0.1774 -0.0346 -0.0096 -0.0155 29  TRP A CZ3 
271  C CH2 . TRP A 29  ? 0.2217 0.2521 0.2435 -0.0423 -0.0098 -0.0167 29  TRP A CH2 
272  N N   . THR A 30  ? 0.1451 0.1667 0.1518 0.0030  -0.0060 0.0024  30  THR A N   
273  C CA  . THR A 30  ? 0.1464 0.1562 0.1476 0.0066  -0.0049 0.0048  30  THR A CA  
274  C C   . THR A 30  ? 0.1553 0.1622 0.1505 0.0075  -0.0068 0.0062  30  THR A C   
275  O O   . THR A 30  ? 0.1842 0.1819 0.1748 0.0065  -0.0053 0.0074  30  THR A O   
276  C CB  . THR A 30  ? 0.2123 0.2218 0.2145 0.0130  -0.0048 0.0065  30  THR A CB  
277  O OG1 . THR A 30  ? 0.1781 0.1903 0.1845 0.0123  -0.0023 0.0050  30  THR A OG1 
278  C CG2 . THR A 30  ? 0.2091 0.2050 0.2055 0.0156  -0.0041 0.0090  30  THR A CG2 
279  N N   . PHE A 31  ? 0.1576 0.1740 0.1528 0.0093  -0.0100 0.0063  31  PHE A N   
280  C CA  . PHE A 31  ? 0.1675 0.1827 0.1558 0.0102  -0.0117 0.0078  31  PHE A CA  
281  C C   . PHE A 31  ? 0.1445 0.1560 0.1295 0.0048  -0.0105 0.0047  31  PHE A C   
282  O O   . PHE A 31  ? 0.1585 0.1631 0.1374 0.0050  -0.0091 0.0063  31  PHE A O   
283  C CB  . PHE A 31  ? 0.1791 0.2074 0.1679 0.0130  -0.0161 0.0080  31  PHE A CB  
284  C CG  . PHE A 31  ? 0.1835 0.2126 0.1639 0.0137  -0.0181 0.0092  31  PHE A CG  
285  C CD1 . PHE A 31  ? 0.1913 0.2148 0.1654 0.0190  -0.0182 0.0151  31  PHE A CD1 
286  C CD2 . PHE A 31  ? 0.1730 0.2076 0.1510 0.0089  -0.0198 0.0045  31  PHE A CD2 
287  C CE1 . PHE A 31  ? 0.1954 0.2205 0.1607 0.0197  -0.0197 0.0170  31  PHE A CE1 
288  C CE2 . PHE A 31  ? 0.2093 0.2456 0.1783 0.0100  -0.0215 0.0052  31  PHE A CE2 
289  C CZ  . PHE A 31  ? 0.1931 0.2255 0.1556 0.0155  -0.0213 0.0119  31  PHE A CZ  
290  N N   . PHE A 32  ? 0.1598 0.1754 0.1486 -0.0002 -0.0109 0.0002  32  PHE A N   
291  C CA  . PHE A 32  ? 0.1586 0.1694 0.1434 -0.0044 -0.0101 -0.0034 32  PHE A CA  
292  C C   . PHE A 32  ? 0.1685 0.1679 0.1524 -0.0049 -0.0061 -0.0025 32  PHE A C   
293  O O   . PHE A 32  ? 0.1691 0.1636 0.1478 -0.0051 -0.0047 -0.0034 32  PHE A O   
294  C CB  . PHE A 32  ? 0.1395 0.1553 0.1285 -0.0101 -0.0117 -0.0084 32  PHE A CB  
295  C CG  . PHE A 32  ? 0.1715 0.1994 0.1597 -0.0108 -0.0163 -0.0109 32  PHE A CG  
296  C CD1 . PHE A 32  ? 0.1517 0.1806 0.1314 -0.0086 -0.0182 -0.0115 32  PHE A CD1 
297  C CD2 . PHE A 32  ? 0.2032 0.2432 0.1992 -0.0135 -0.0188 -0.0123 32  PHE A CD2 
298  C CE1 . PHE A 32  ? 0.1880 0.2293 0.1660 -0.0090 -0.0231 -0.0139 32  PHE A CE1 
299  C CE2 . PHE A 32  ? 0.2009 0.2543 0.1968 -0.0143 -0.0238 -0.0148 32  PHE A CE2 
300  C CZ  . PHE A 32  ? 0.1797 0.2335 0.1662 -0.0119 -0.0262 -0.0157 32  PHE A CZ  
301  N N   . HIS A 33  ? 0.1584 0.1547 0.1469 -0.0048 -0.0042 -0.0008 33  HIS A N   
302  C CA  . HIS A 33  ? 0.1366 0.1239 0.1241 -0.0050 -0.0011 0.0002  33  HIS A CA  
303  C C   . HIS A 33  ? 0.1729 0.1566 0.1569 -0.0019 -0.0003 0.0039  33  HIS A C   
304  O O   . HIS A 33  ? 0.1664 0.1453 0.1489 -0.0023 0.0018  0.0045  33  HIS A O   
305  C CB  . HIS A 33  ? 0.1517 0.1373 0.1442 -0.0063 0.0004  0.0007  33  HIS A CB  
306  C CG  . HIS A 33  ? 0.1469 0.1322 0.1418 -0.0107 0.0008  -0.0019 33  HIS A CG  
307  N ND1 . HIS A 33  ? 0.1581 0.1363 0.1506 -0.0125 0.0020  -0.0038 33  HIS A ND1 
308  C CD2 . HIS A 33  ? 0.1533 0.1445 0.1530 -0.0138 0.0002  -0.0029 33  HIS A CD2 
309  C CE1 . HIS A 33  ? 0.1646 0.1419 0.1596 -0.0168 0.0020  -0.0057 33  HIS A CE1 
310  N NE2 . HIS A 33  ? 0.1816 0.1674 0.1814 -0.0183 0.0010  -0.0050 33  HIS A NE2 
311  N N   . ALA A 34  ? 0.1592 0.1453 0.1423 0.0012  -0.0019 0.0066  34  ALA A N   
312  C CA  . ALA A 34  ? 0.1610 0.1423 0.1402 0.0032  -0.0011 0.0107  34  ALA A CA  
313  C C   . ALA A 34  ? 0.1772 0.1599 0.1506 0.0027  -0.0005 0.0110  34  ALA A C   
314  O O   . ALA A 34  ? 0.1834 0.1626 0.1550 0.0018  0.0019  0.0128  34  ALA A O   
315  C CB  . ALA A 34  ? 0.1939 0.1755 0.1725 0.0074  -0.0030 0.0140  34  ALA A CB  
316  N N   . VAL A 35  ? 0.1771 0.1664 0.1476 0.0030  -0.0028 0.0089  35  VAL A N   
317  C CA  . VAL A 35  ? 0.1679 0.1592 0.1313 0.0032  -0.0022 0.0088  35  VAL A CA  
318  C C   . VAL A 35  ? 0.1761 0.1649 0.1392 0.0009  0.0004  0.0045  35  VAL A C   
319  O O   . VAL A 35  ? 0.2110 0.2001 0.1692 0.0015  0.0027  0.0050  35  VAL A O   
320  C CB  . VAL A 35  ? 0.2145 0.2143 0.1737 0.0044  -0.0059 0.0072  35  VAL A CB  
321  C CG1 . VAL A 35  ? 0.2050 0.2075 0.1645 0.0083  -0.0086 0.0122  35  VAL A CG1 
322  C CG2 . VAL A 35  ? 0.2004 0.2043 0.1631 0.0011  -0.0081 0.0005  35  VAL A CG2 
323  N N   . LYS A 36  ? 0.1712 0.1575 0.1395 -0.0014 0.0004  0.0007  36  LYS A N   
324  C CA  . LYS A 36  ? 0.2002 0.1827 0.1679 -0.0026 0.0026  -0.0033 36  LYS A CA  
325  C C   . LYS A 36  ? 0.1870 0.1647 0.1583 -0.0021 0.0057  -0.0010 36  LYS A C   
326  O O   . LYS A 36  ? 0.1800 0.1567 0.1493 -0.0010 0.0083  -0.0019 36  LYS A O   
327  C CB  . LYS A 36  ? 0.1784 0.1594 0.1489 -0.0057 0.0009  -0.0083 36  LYS A CB  
328  C CG  . LYS A 36  ? 0.2027 0.1774 0.1708 -0.0064 0.0026  -0.0132 36  LYS A CG  
329  C CD  . LYS A 36  ? 0.1868 0.1584 0.1568 -0.0106 0.0007  -0.0182 36  LYS A CD  
330  C CE  . LYS A 36  ? 0.1693 0.1370 0.1463 -0.0129 0.0014  -0.0157 36  LYS A CE  
331  N NZ  . LYS A 36  ? 0.1727 0.1327 0.1505 -0.0105 0.0047  -0.0139 36  LYS A NZ  
332  N N   . ASP A 37  ? 0.1558 0.1318 0.1321 -0.0026 0.0054  0.0018  37  ASP A N   
333  C CA  . ASP A 37  ? 0.1506 0.1230 0.1307 -0.0028 0.0074  0.0031  37  ASP A CA  
334  C C   . ASP A 37  ? 0.1574 0.1295 0.1392 -0.0026 0.0078  0.0073  37  ASP A C   
335  O O   . ASP A 37  ? 0.1804 0.1524 0.1639 -0.0028 0.0095  0.0086  37  ASP A O   
336  C CB  . ASP A 37  ? 0.1501 0.1198 0.1341 -0.0042 0.0068  0.0015  37  ASP A CB  
337  C CG  . ASP A 37  ? 0.1851 0.1532 0.1678 -0.0058 0.0062  -0.0027 37  ASP A CG  
338  O OD1 . ASP A 37  ? 0.1859 0.1509 0.1661 -0.0048 0.0076  -0.0050 37  ASP A OD1 
339  O OD2 . ASP A 37  ? 0.1884 0.1589 0.1728 -0.0080 0.0043  -0.0038 37  ASP A OD2 
340  N N   . TYR A 38  ? 0.1660 0.1379 0.1480 -0.0023 0.0061  0.0091  38  TYR A N   
341  C CA  . TYR A 38  ? 0.1653 0.1338 0.1492 -0.0026 0.0062  0.0118  38  TYR A CA  
342  C C   . TYR A 38  ? 0.1851 0.1531 0.1672 -0.0035 0.0076  0.0153  38  TYR A C   
343  O O   . TYR A 38  ? 0.1792 0.1453 0.1639 -0.0054 0.0082  0.0166  38  TYR A O   
344  C CB  . TYR A 38  ? 0.1775 0.1444 0.1619 -0.0011 0.0043  0.0123  38  TYR A CB  
345  C CG  . TYR A 38  ? 0.1755 0.1446 0.1629 -0.0008 0.0036  0.0095  38  TYR A CG  
346  C CD1 . TYR A 38  ? 0.1521 0.1209 0.1417 -0.0025 0.0047  0.0080  38  TYR A CD1 
347  C CD2 . TYR A 38  ? 0.1581 0.1308 0.1462 0.0011  0.0020  0.0090  38  TYR A CD2 
348  C CE1 . TYR A 38  ? 0.1542 0.1252 0.1462 -0.0029 0.0046  0.0064  38  TYR A CE1 
349  C CE2 . TYR A 38  ? 0.1501 0.1267 0.1416 0.0006  0.0020  0.0069  38  TYR A CE2 
350  C CZ  . TYR A 38  ? 0.1434 0.1188 0.1366 -0.0018 0.0035  0.0058  38  TYR A CZ  
351  O OH  . TYR A 38  ? 0.1519 0.1313 0.1481 -0.0029 0.0040  0.0047  38  TYR A OH  
352  N N   . TYR A 39  ? 0.1852 0.1557 0.1629 -0.0028 0.0081  0.0169  39  TYR A N   
353  C CA  . TYR A 39  ? 0.1788 0.1505 0.1548 -0.0042 0.0104  0.0207  39  TYR A CA  
354  C C   . TYR A 39  ? 0.1881 0.1653 0.1657 -0.0046 0.0132  0.0189  39  TYR A C   
355  O O   . TYR A 39  ? 0.1746 0.1542 0.1553 -0.0066 0.0152  0.0211  39  TYR A O   
356  C CB  . TYR A 39  ? 0.1888 0.1619 0.1582 -0.0028 0.0103  0.0240  39  TYR A CB  
357  C CG  . TYR A 39  ? 0.1687 0.1444 0.1356 -0.0047 0.0134  0.0286  39  TYR A CG  
358  C CD1 . TYR A 39  ? 0.1955 0.1659 0.1632 -0.0074 0.0140  0.0341  39  TYR A CD1 
359  C CD2 . TYR A 39  ? 0.1823 0.1657 0.1463 -0.0039 0.0161  0.0274  39  TYR A CD2 
360  C CE1 . TYR A 39  ? 0.2390 0.2126 0.2052 -0.0103 0.0173  0.0391  39  TYR A CE1 
361  C CE2 . TYR A 39  ? 0.1908 0.1789 0.1531 -0.0058 0.0198  0.0320  39  TYR A CE2 
362  C CZ  . TYR A 39  ? 0.2582 0.2419 0.2220 -0.0094 0.0204  0.0383  39  TYR A CZ  
363  O OH  . TYR A 39  ? 0.2866 0.2757 0.2492 -0.0124 0.0244  0.0437  39  TYR A OH  
364  N N   . ASP A 40  ? 0.1704 0.1496 0.1462 -0.0025 0.0132  0.0147  40  ASP A N   
365  C CA  . ASP A 40  ? 0.1315 0.1154 0.1072 -0.0012 0.0161  0.0126  40  ASP A CA  
366  C C   . ASP A 40  ? 0.1802 0.1642 0.1623 -0.0012 0.0169  0.0118  40  ASP A C   
367  O O   . ASP A 40  ? 0.1879 0.1776 0.1719 -0.0002 0.0196  0.0122  40  ASP A O   
368  C CB  . ASP A 40  ? 0.1811 0.1648 0.1519 0.0009  0.0155  0.0076  40  ASP A CB  
369  C CG  . ASP A 40  ? 0.1913 0.1791 0.1546 0.0017  0.0159  0.0086  40  ASP A CG  
370  O OD1 . ASP A 40  ? 0.2089 0.2021 0.1699 0.0026  0.0192  0.0102  40  ASP A OD1 
371  O OD2 . ASP A 40  ? 0.1890 0.1762 0.1488 0.0016  0.0129  0.0085  40  ASP A OD2 
372  N N   . MET A 41  ? 0.1608 0.1402 0.1462 -0.0020 0.0146  0.0109  41  MET A N   
373  C CA  . MET A 41  ? 0.1455 0.1259 0.1360 -0.0015 0.0150  0.0106  41  MET A CA  
374  C C   . MET A 41  ? 0.1742 0.1600 0.1690 -0.0036 0.0158  0.0140  41  MET A C   
375  O O   . MET A 41  ? 0.1648 0.1571 0.1629 -0.0022 0.0177  0.0141  41  MET A O   
376  C CB  . MET A 41  ? 0.1799 0.1550 0.1718 -0.0019 0.0126  0.0095  41  MET A CB  
377  C CG  . MET A 41  ? 0.1597 0.1305 0.1495 -0.0004 0.0124  0.0062  41  MET A CG  
378  S SD  . MET A 41  ? 0.1639 0.1338 0.1544 0.0033  0.0145  0.0045  41  MET A SD  
379  C CE  . MET A 41  ? 0.1902 0.1594 0.1851 0.0035  0.0133  0.0069  41  MET A CE  
380  N N   . PRO A 42  ? 0.1619 0.1454 0.1569 -0.0071 0.0145  0.0165  42  PRO A N   
381  C CA  . PRO A 42  ? 0.1644 0.1530 0.1636 -0.0106 0.0154  0.0195  42  PRO A CA  
382  C C   . PRO A 42  ? 0.1365 0.1323 0.1350 -0.0110 0.0189  0.0221  42  PRO A C   
383  O O   . PRO A 42  ? 0.1604 0.1646 0.1641 -0.0133 0.0206  0.0241  42  PRO A O   
384  C CB  . PRO A 42  ? 0.1676 0.1484 0.1658 -0.0141 0.0131  0.0210  42  PRO A CB  
385  C CG  . PRO A 42  ? 0.1649 0.1392 0.1575 -0.0114 0.0121  0.0201  42  PRO A CG  
386  C CD  . PRO A 42  ? 0.1459 0.1220 0.1382 -0.0079 0.0121  0.0165  42  PRO A CD  
387  N N   . ALA A 43  ? 0.1672 0.1617 0.1594 -0.0089 0.0201  0.0221  43  ALA A N   
388  C CA  . ALA A 43  ? 0.1680 0.1702 0.1579 -0.0092 0.0239  0.0248  43  ALA A CA  
389  C C   . ALA A 43  ? 0.1858 0.1981 0.1789 -0.0057 0.0270  0.0226  43  ALA A C   
390  O O   . ALA A 43  ? 0.1928 0.2148 0.1865 -0.0064 0.0308  0.0252  43  ALA A O   
391  C CB  . ALA A 43  ? 0.1978 0.1970 0.1788 -0.0072 0.0239  0.0250  43  ALA A CB  
392  N N   . TYR A 44  ? 0.1701 0.1805 0.1652 -0.0019 0.0258  0.0183  44  TYR A N   
393  C CA  . TYR A 44  ? 0.1793 0.1988 0.1783 0.0023  0.0286  0.0166  44  TYR A CA  
394  C C   . TYR A 44  ? 0.1634 0.1950 0.1711 -0.0008 0.0300  0.0205  44  TYR A C   
395  O O   . TYR A 44  ? 0.1833 0.2269 0.1945 0.0022  0.0336  0.0206  44  TYR A O   
396  C CB  . TYR A 44  ? 0.1819 0.1955 0.1824 0.0066  0.0266  0.0128  44  TYR A CB  
397  C CG  . TYR A 44  ? 0.1626 0.1672 0.1560 0.0104  0.0265  0.0080  44  TYR A CG  
398  C CD1 . TYR A 44  ? 0.1815 0.1883 0.1724 0.0161  0.0294  0.0044  44  TYR A CD1 
399  C CD2 . TYR A 44  ? 0.1899 0.1844 0.1796 0.0081  0.0233  0.0067  44  TYR A CD2 
400  C CE1 . TYR A 44  ? 0.1666 0.1638 0.1508 0.0186  0.0289  -0.0008 44  TYR A CE1 
401  C CE2 . TYR A 44  ? 0.2003 0.1872 0.1844 0.0102  0.0227  0.0021  44  TYR A CE2 
402  C CZ  . TYR A 44  ? 0.1826 0.1700 0.1637 0.0150  0.0253  -0.0019 44  TYR A CZ  
403  O OH  . TYR A 44  ? 0.2194 0.1981 0.1947 0.0161  0.0244  -0.0073 44  TYR A OH  
404  N N   . LEU A 45  ? 0.1697 0.1989 0.1811 -0.0068 0.0273  0.0232  45  LEU A N   
405  C CA  . LEU A 45  ? 0.1643 0.2051 0.1846 -0.0111 0.0278  0.0262  45  LEU A CA  
406  C C   . LEU A 45  ? 0.1743 0.2248 0.1953 -0.0149 0.0322  0.0306  45  LEU A C   
407  O O   . LEU A 45  ? 0.2134 0.2778 0.2430 -0.0182 0.0338  0.0331  45  LEU A O   
408  C CB  . LEU A 45  ? 0.1404 0.1741 0.1630 -0.0171 0.0234  0.0269  45  LEU A CB  
409  C CG  . LEU A 45  ? 0.1505 0.1789 0.1736 -0.0138 0.0196  0.0233  45  LEU A CG  
410  C CD1 . LEU A 45  ? 0.1835 0.2023 0.2055 -0.0189 0.0156  0.0230  45  LEU A CD1 
411  C CD2 . LEU A 45  ? 0.1773 0.2195 0.2085 -0.0112 0.0195  0.0231  45  LEU A CD2 
412  N N   . LYS A 46  ? 0.1921 0.2372 0.2046 -0.0146 0.0341  0.0319  46  LYS A N   
413  C CA  . LYS A 46  ? 0.2398 0.2950 0.2517 -0.0174 0.0390  0.0367  46  LYS A CA  
414  C C   . LYS A 46  ? 0.1888 0.2600 0.2031 -0.0115 0.0439  0.0350  46  LYS A C   
415  O O   . LYS A 46  ? 0.2138 0.2990 0.2315 -0.0143 0.0485  0.0392  46  LYS A O   
416  C CB  . LYS A 46  ? 0.2609 0.3067 0.2616 -0.0176 0.0395  0.0389  46  LYS A CB  
417  C CG  . LYS A 46  ? 0.3090 0.3396 0.3076 -0.0224 0.0352  0.0412  46  LYS A CG  
418  C CD  . LYS A 46  ? 0.4384 0.4591 0.4259 -0.0195 0.0341  0.0416  46  LYS A CD  
419  C CE  . LYS A 46  ? 0.5453 0.5691 0.5271 -0.0223 0.0377  0.0486  46  LYS A CE  
420  N NZ  . LYS A 46  ? 0.6270 0.6419 0.5980 -0.0190 0.0357  0.0493  46  LYS A NZ  
421  N N   . ASP A 47  ? 0.1898 0.2587 0.2024 -0.0034 0.0432  0.0290  47  ASP A N   
422  C CA  . ASP A 47  ? 0.1786 0.2591 0.1912 0.0041  0.0478  0.0261  47  ASP A CA  
423  C C   . ASP A 47  ? 0.2161 0.3047 0.2381 0.0093  0.0473  0.0236  47  ASP A C   
424  O O   . ASP A 47  ? 0.2385 0.3392 0.2624 0.0160  0.0516  0.0217  47  ASP A O   
425  C CB  . ASP A 47  ? 0.2111 0.2809 0.2120 0.0103  0.0478  0.0206  47  ASP A CB  
426  C CG  . ASP A 47  ? 0.2883 0.3530 0.2792 0.0067  0.0483  0.0232  47  ASP A CG  
427  O OD1 . ASP A 47  ? 0.2612 0.3354 0.2527 0.0022  0.0517  0.0291  47  ASP A OD1 
428  O OD2 . ASP A 47  ? 0.3031 0.3550 0.2859 0.0081  0.0451  0.0198  47  ASP A OD2 
429  N N   . PHE A 48  ? 0.1909 0.2738 0.2181 0.0072  0.0423  0.0235  48  PHE A N   
430  C CA  . PHE A 48  ? 0.2039 0.2937 0.2390 0.0127  0.0410  0.0218  48  PHE A CA  
431  C C   . PHE A 48  ? 0.2198 0.3177 0.2649 0.0057  0.0378  0.0253  48  PHE A C   
432  O O   . PHE A 48  ? 0.2293 0.3168 0.2725 -0.0016 0.0341  0.0266  48  PHE A O   
433  C CB  . PHE A 48  ? 0.2215 0.2945 0.2508 0.0186  0.0378  0.0173  48  PHE A CB  
434  C CG  . PHE A 48  ? 0.1920 0.2568 0.2119 0.0248  0.0405  0.0128  48  PHE A CG  
435  C CD1 . PHE A 48  ? 0.2323 0.3037 0.2528 0.0341  0.0442  0.0097  48  PHE A CD1 
436  C CD2 . PHE A 48  ? 0.1872 0.2385 0.1974 0.0216  0.0393  0.0113  48  PHE A CD2 
437  C CE1 . PHE A 48  ? 0.2565 0.3194 0.2674 0.0395  0.0465  0.0044  48  PHE A CE1 
438  C CE2 . PHE A 48  ? 0.2255 0.2702 0.2266 0.0266  0.0413  0.0064  48  PHE A CE2 
439  C CZ  . PHE A 48  ? 0.2461 0.2959 0.2472 0.0352  0.0449  0.0026  48  PHE A CZ  
440  N N   . GLU A 49  ? 0.1943 0.3112 0.2499 0.0081  0.0391  0.0265  49  GLU A N   
441  C CA  . GLU A 49  ? 0.2052 0.3342 0.2716 0.0008  0.0360  0.0295  49  GLU A CA  
442  C C   . GLU A 49  ? 0.2110 0.3358 0.2795 0.0043  0.0302  0.0276  49  GLU A C   
443  O O   . GLU A 49  ? 0.2407 0.3809 0.3182 0.0085  0.0291  0.0280  49  GLU A O   
444  C CB  . GLU A 49  ? 0.2768 0.4321 0.3545 0.0009  0.0402  0.0322  49  GLU A CB  
445  C CG  . GLU A 49  ? 0.4326 0.5943 0.5089 -0.0049 0.0461  0.0356  49  GLU A CG  
446  C CD  . GLU A 49  ? 0.5457 0.7009 0.6111 0.0031  0.0510  0.0332  49  GLU A CD  
447  O OE1 . GLU A 49  ? 0.5654 0.7080 0.6210 -0.0011 0.0521  0.0343  49  GLU A OE1 
448  O OE2 . GLU A 49  ? 0.5593 0.7217 0.6256 0.0140  0.0536  0.0300  49  GLU A OE2 
449  N N   . ILE A 50  ? 0.1819 0.2861 0.2417 0.0030  0.0267  0.0257  50  ILE A N   
450  C CA  . ILE A 50  ? 0.2134 0.3109 0.2727 0.0053  0.0214  0.0244  50  ILE A CA  
451  C C   . ILE A 50  ? 0.1738 0.2593 0.2292 -0.0036 0.0175  0.0243  50  ILE A C   
452  O O   . ILE A 50  ? 0.1860 0.2663 0.2387 -0.0104 0.0189  0.0253  50  ILE A O   
453  C CB  . ILE A 50  ? 0.1878 0.2715 0.2395 0.0147  0.0218  0.0219  50  ILE A CB  
454  C CG1 . ILE A 50  ? 0.2196 0.2857 0.2609 0.0127  0.0232  0.0201  50  ILE A CG1 
455  C CG2 . ILE A 50  ? 0.1860 0.2800 0.2411 0.0245  0.0256  0.0213  50  ILE A CG2 
456  C CD1 . ILE A 50  ? 0.2532 0.3048 0.2874 0.0197  0.0232  0.0173  50  ILE A CD1 
457  N N   . LYS A 51  ? 0.1553 0.2362 0.2097 -0.0030 0.0127  0.0232  51  LYS A N   
458  C CA  . LYS A 51  ? 0.1554 0.2236 0.2047 -0.0094 0.0091  0.0220  51  LYS A CA  
459  C C   . LYS A 51  ? 0.1371 0.1883 0.1770 -0.0046 0.0087  0.0203  51  LYS A C   
460  O O   . LYS A 51  ? 0.1508 0.2014 0.1897 0.0026  0.0086  0.0202  51  LYS A O   
461  C CB  . LYS A 51  ? 0.1478 0.2242 0.2018 -0.0128 0.0039  0.0216  51  LYS A CB  
462  C CG  . LYS A 51  ? 0.1717 0.2685 0.2370 -0.0176 0.0034  0.0231  51  LYS A CG  
463  C CD  . LYS A 51  ? 0.1769 0.2728 0.2441 -0.0272 0.0056  0.0243  51  LYS A CD  
464  C CE  . LYS A 51  ? 0.2907 0.4081 0.3704 -0.0339 0.0046  0.0258  51  LYS A CE  
465  N NZ  . LYS A 51  ? 0.3551 0.4704 0.4369 -0.0454 0.0061  0.0275  51  LYS A NZ  
466  N N   . LEU A 52  ? 0.1432 0.1809 0.1767 -0.0085 0.0086  0.0193  52  LEU A N   
467  C CA  . LEU A 52  ? 0.1382 0.1620 0.1641 -0.0054 0.0080  0.0177  52  LEU A CA  
468  C C   . LEU A 52  ? 0.1395 0.1546 0.1617 -0.0105 0.0053  0.0164  52  LEU A C   
469  O O   . LEU A 52  ? 0.1728 0.1865 0.1956 -0.0161 0.0053  0.0167  52  LEU A O   
470  C CB  . LEU A 52  ? 0.1585 0.1750 0.1797 -0.0027 0.0114  0.0171  52  LEU A CB  
471  C CG  . LEU A 52  ? 0.1300 0.1519 0.1526 0.0034  0.0147  0.0171  52  LEU A CG  
472  C CD1 . LEU A 52  ? 0.1716 0.1871 0.1885 0.0040  0.0176  0.0158  52  LEU A CD1 
473  C CD2 . LEU A 52  ? 0.1442 0.1628 0.1660 0.0096  0.0137  0.0165  52  LEU A CD2 
474  N N   . ASN A 53  ? 0.1273 0.1363 0.1453 -0.0086 0.0032  0.0151  53  ASN A N   
475  C CA  . ASN A 53  ? 0.1465 0.1481 0.1606 -0.0121 0.0010  0.0132  53  ASN A CA  
476  C C   . ASN A 53  ? 0.1355 0.1265 0.1437 -0.0100 0.0022  0.0123  53  ASN A C   
477  O O   . ASN A 53  ? 0.1475 0.1365 0.1543 -0.0062 0.0039  0.0130  53  ASN A O   
478  C CB  . ASN A 53  ? 0.1594 0.1655 0.1734 -0.0123 -0.0026 0.0121  53  ASN A CB  
479  C CG  . ASN A 53  ? 0.1682 0.1878 0.1891 -0.0140 -0.0043 0.0130  53  ASN A CG  
480  O OD1 . ASN A 53  ? 0.1542 0.1769 0.1786 -0.0200 -0.0054 0.0122  53  ASN A OD1 
481  N ND2 . ASN A 53  ? 0.1493 0.1771 0.1727 -0.0088 -0.0045 0.0150  53  ASN A ND2 
482  N N   . PHE A 54  ? 0.1506 0.1345 0.1556 -0.0125 0.0012  0.0106  54  PHE A N   
483  C CA  . PHE A 54  ? 0.1380 0.1141 0.1387 -0.0107 0.0023  0.0099  54  PHE A CA  
484  C C   . PHE A 54  ? 0.1717 0.1433 0.1688 -0.0109 0.0006  0.0074  54  PHE A C   
485  O O   . PHE A 54  ? 0.1841 0.1545 0.1810 -0.0137 -0.0014 0.0056  54  PHE A O   
486  C CB  . PHE A 54  ? 0.1498 0.1223 0.1502 -0.0119 0.0037  0.0110  54  PHE A CB  
487  C CG  . PHE A 54  ? 0.1778 0.1554 0.1805 -0.0112 0.0059  0.0129  54  PHE A CG  
488  C CD1 . PHE A 54  ? 0.1610 0.1380 0.1620 -0.0079 0.0076  0.0126  54  PHE A CD1 
489  C CD2 . PHE A 54  ? 0.1634 0.1472 0.1701 -0.0139 0.0064  0.0145  54  PHE A CD2 
490  C CE1 . PHE A 54  ? 0.1646 0.1459 0.1667 -0.0064 0.0097  0.0134  54  PHE A CE1 
491  C CE2 . PHE A 54  ? 0.1771 0.1674 0.1859 -0.0124 0.0091  0.0160  54  PHE A CE2 
492  C CZ  . PHE A 54  ? 0.1862 0.1746 0.1920 -0.0082 0.0108  0.0151  54  PHE A CZ  
493  N N   . ASN A 55  ? 0.1366 0.1060 0.1309 -0.0081 0.0015  0.0069  55  ASN A N   
494  C CA  . ASN A 55  ? 0.1490 0.1147 0.1397 -0.0072 0.0009  0.0043  55  ASN A CA  
495  C C   . ASN A 55  ? 0.1426 0.1042 0.1327 -0.0058 0.0021  0.0044  55  ASN A C   
496  O O   . ASN A 55  ? 0.1760 0.1392 0.1674 -0.0049 0.0035  0.0059  55  ASN A O   
497  C CB  . ASN A 55  ? 0.1461 0.1153 0.1345 -0.0052 0.0014  0.0043  55  ASN A CB  
498  C CG  . ASN A 55  ? 0.1557 0.1232 0.1400 -0.0038 0.0012  0.0012  55  ASN A CG  
499  O OD1 . ASN A 55  ? 0.1729 0.1384 0.1550 -0.0047 -0.0008 -0.0018 55  ASN A OD1 
500  N ND2 . ASN A 55  ? 0.1552 0.1241 0.1388 -0.0016 0.0032  0.0015  55  ASN A ND2 
501  N N   . LEU A 56  ? 0.1529 0.1089 0.1409 -0.0051 0.0013  0.0024  56  LEU A N   
502  C CA  . LEU A 56  ? 0.1286 0.0817 0.1160 -0.0023 0.0019  0.0025  56  LEU A CA  
503  C C   . LEU A 56  ? 0.1464 0.0985 0.1311 0.0010  0.0020  -0.0007 56  LEU A C   
504  O O   . LEU A 56  ? 0.1866 0.1333 0.1686 0.0009  0.0007  -0.0036 56  LEU A O   
505  C CB  . LEU A 56  ? 0.1892 0.1352 0.1762 -0.0033 0.0013  0.0040  56  LEU A CB  
506  C CG  . LEU A 56  ? 0.2133 0.1611 0.2023 -0.0062 0.0019  0.0075  56  LEU A CG  
507  C CD1 . LEU A 56  ? 0.2307 0.1705 0.2184 -0.0080 0.0014  0.0095  56  LEU A CD1 
508  C CD2 . LEU A 56  ? 0.3080 0.2607 0.2974 -0.0042 0.0031  0.0089  56  LEU A CD2 
509  N N   . THR A 57  ? 0.1797 0.1375 0.1654 0.0038  0.0034  -0.0006 57  THR A N   
510  C CA  . THR A 57  ? 0.1724 0.1308 0.1558 0.0077  0.0040  -0.0037 57  THR A CA  
511  C C   . THR A 57  ? 0.1654 0.1167 0.1478 0.0116  0.0032  -0.0047 57  THR A C   
512  O O   . THR A 57  ? 0.1648 0.1143 0.1490 0.0117  0.0026  -0.0019 57  THR A O   
513  C CB  . THR A 57  ? 0.1649 0.1335 0.1504 0.0091  0.0062  -0.0030 57  THR A CB  
514  O OG1 . THR A 57  ? 0.1572 0.1291 0.1465 0.0098  0.0063  -0.0010 57  THR A OG1 
515  C CG2 . THR A 57  ? 0.1656 0.1386 0.1513 0.0055  0.0071  -0.0010 57  THR A CG2 
516  N N   . PRO A 58  ? 0.1849 0.1315 0.1638 0.0152  0.0031  -0.0088 58  PRO A N   
517  C CA  . PRO A 58  ? 0.1677 0.1052 0.1453 0.0200  0.0023  -0.0095 58  PRO A CA  
518  C C   . PRO A 58  ? 0.1725 0.1175 0.1536 0.0249  0.0031  -0.0073 58  PRO A C   
519  O O   . PRO A 58  ? 0.1811 0.1200 0.1622 0.0275  0.0019  -0.0049 58  PRO A O   
520  C CB  . PRO A 58  ? 0.1804 0.1123 0.1529 0.0237  0.0024  -0.0155 58  PRO A CB  
521  C CG  . PRO A 58  ? 0.1729 0.1077 0.1432 0.0182  0.0019  -0.0175 58  PRO A CG  
522  C CD  . PRO A 58  ? 0.1719 0.1193 0.1467 0.0153  0.0033  -0.0130 58  PRO A CD  
523  N N   . VAL A 59  ? 0.1496 0.1082 0.1338 0.0261  0.0051  -0.0076 59  VAL A N   
524  C CA  . VAL A 59  ? 0.1538 0.1222 0.1428 0.0300  0.0054  -0.0056 59  VAL A CA  
525  C C   . VAL A 59  ? 0.1709 0.1404 0.1623 0.0262  0.0039  -0.0014 59  VAL A C   
526  O O   . VAL A 59  ? 0.1659 0.1381 0.1591 0.0298  0.0026  0.0005  59  VAL A O   
527  C CB  . VAL A 59  ? 0.1436 0.1274 0.1362 0.0305  0.0081  -0.0066 59  VAL A CB  
528  C CG1 . VAL A 59  ? 0.1822 0.1704 0.1756 0.0230  0.0091  -0.0049 59  VAL A CG1 
529  C CG2 . VAL A 59  ? 0.1467 0.1434 0.1456 0.0341  0.0081  -0.0050 59  VAL A CG2 
530  N N   . LEU A 60  ? 0.1587 0.1268 0.1497 0.0196  0.0038  -0.0001 60  LEU A N   
531  C CA  . LEU A 60  ? 0.1584 0.1261 0.1502 0.0166  0.0026  0.0031  60  LEU A CA  
532  C C   . LEU A 60  ? 0.1850 0.1416 0.1733 0.0182  0.0010  0.0051  60  LEU A C   
533  O O   . LEU A 60  ? 0.1790 0.1369 0.1673 0.0201  -0.0002 0.0079  60  LEU A O   
534  C CB  . LEU A 60  ? 0.1682 0.1360 0.1601 0.0105  0.0033  0.0037  60  LEU A CB  
535  C CG  . LEU A 60  ? 0.1546 0.1210 0.1460 0.0079  0.0025  0.0062  60  LEU A CG  
536  C CD1 . LEU A 60  ? 0.1751 0.1493 0.1684 0.0091  0.0015  0.0068  60  LEU A CD1 
537  C CD2 . LEU A 60  ? 0.1772 0.1436 0.1689 0.0033  0.0034  0.0064  60  LEU A CD2 
538  N N   . ILE A 61  ? 0.1654 0.1112 0.1507 0.0172  0.0009  0.0040  61  ILE A N   
539  C CA  . ILE A 61  ? 0.1703 0.1038 0.1523 0.0176  -0.0002 0.0064  61  ILE A CA  
540  C C   . ILE A 61  ? 0.1724 0.1035 0.1534 0.0250  -0.0012 0.0078  61  ILE A C   
541  O O   . ILE A 61  ? 0.2053 0.1322 0.1844 0.0260  -0.0022 0.0122  61  ILE A O   
542  C CB  . ILE A 61  ? 0.1922 0.1144 0.1714 0.0149  -0.0005 0.0038  61  ILE A CB  
543  C CG1 . ILE A 61  ? 0.1851 0.1112 0.1659 0.0079  -0.0001 0.0034  61  ILE A CG1 
544  C CG2 . ILE A 61  ? 0.2454 0.1528 0.2214 0.0149  -0.0016 0.0065  61  ILE A CG2 
545  C CD1 . ILE A 61  ? 0.2108 0.1290 0.1895 0.0048  -0.0011 -0.0001 61  ILE A CD1 
546  N N   . ASP A 62  ? 0.1601 0.0944 0.1421 0.0309  -0.0008 0.0043  62  ASP A N   
547  C CA  . ASP A 62  ? 0.1865 0.1202 0.1684 0.0396  -0.0017 0.0055  62  ASP A CA  
548  C C   . ASP A 62  ? 0.1952 0.1403 0.1798 0.0406  -0.0030 0.0097  62  ASP A C   
549  O O   . ASP A 62  ? 0.2176 0.1584 0.2001 0.0454  -0.0047 0.0137  62  ASP A O   
550  C CB  . ASP A 62  ? 0.2272 0.1685 0.2113 0.0460  -0.0004 0.0009  62  ASP A CB  
551  C CG  . ASP A 62  ? 0.2627 0.1908 0.2422 0.0481  0.0004  -0.0040 62  ASP A CG  
552  O OD1 . ASP A 62  ? 0.2978 0.2084 0.2726 0.0465  -0.0009 -0.0033 62  ASP A OD1 
553  O OD2 . ASP A 62  ? 0.2533 0.1887 0.2336 0.0514  0.0022  -0.0086 62  ASP A OD2 
554  N N   . GLN A 63  ? 0.1888 0.1481 0.1775 0.0362  -0.0024 0.0089  63  GLN A N   
555  C CA  . GLN A 63  ? 0.1619 0.1329 0.1531 0.0365  -0.0041 0.0115  63  GLN A CA  
556  C C   . GLN A 63  ? 0.1893 0.1540 0.1760 0.0331  -0.0053 0.0157  63  GLN A C   
557  O O   . GLN A 63  ? 0.2055 0.1736 0.1907 0.0365  -0.0074 0.0191  63  GLN A O   
558  C CB  . GLN A 63  ? 0.1517 0.1372 0.1481 0.0316  -0.0032 0.0090  63  GLN A CB  
559  C CG  . GLN A 63  ? 0.1685 0.1636 0.1698 0.0348  -0.0015 0.0059  63  GLN A CG  
560  C CD  . GLN A 63  ? 0.1600 0.1667 0.1659 0.0283  -0.0002 0.0044  63  GLN A CD  
561  O OE1 . GLN A 63  ? 0.1850 0.2028 0.1948 0.0262  -0.0016 0.0050  63  GLN A OE1 
562  N NE2 . GLN A 63  ? 0.1484 0.1522 0.1536 0.0248  0.0024  0.0026  63  GLN A NE2 
563  N N   . ILE A 64  ? 0.1682 0.1255 0.1527 0.0267  -0.0038 0.0156  64  ILE A N   
564  C CA  . ILE A 64  ? 0.1684 0.1204 0.1486 0.0235  -0.0041 0.0197  64  ILE A CA  
565  C C   . ILE A 64  ? 0.2334 0.1743 0.2091 0.0281  -0.0052 0.0243  64  ILE A C   
566  O O   . ILE A 64  ? 0.2297 0.1715 0.2017 0.0293  -0.0063 0.0290  64  ILE A O   
567  C CB  . ILE A 64  ? 0.1665 0.1133 0.1465 0.0167  -0.0021 0.0188  64  ILE A CB  
568  C CG1 . ILE A 64  ? 0.1902 0.1469 0.1736 0.0128  -0.0011 0.0155  64  ILE A CG1 
569  C CG2 . ILE A 64  ? 0.1855 0.1271 0.1613 0.0137  -0.0016 0.0234  64  ILE A CG2 
570  C CD1 . ILE A 64  ? 0.2106 0.1638 0.1944 0.0075  0.0006  0.0146  64  ILE A CD1 
571  N N   . GLN A 65  ? 0.2211 0.1506 0.1961 0.0309  -0.0049 0.0231  65  GLN A N   
572  C CA  . GLN A 65  ? 0.2289 0.1448 0.1994 0.0359  -0.0060 0.0275  65  GLN A CA  
573  C C   . GLN A 65  ? 0.2476 0.1711 0.2178 0.0443  -0.0083 0.0306  65  GLN A C   
574  O O   . GLN A 65  ? 0.2667 0.1848 0.2321 0.0468  -0.0095 0.0369  65  GLN A O   
575  C CB  . GLN A 65  ? 0.2637 0.1655 0.2333 0.0382  -0.0055 0.0240  65  GLN A CB  
576  C CG  . GLN A 65  ? 0.2514 0.1432 0.2201 0.0296  -0.0042 0.0220  65  GLN A CG  
577  C CD  . GLN A 65  ? 0.3126 0.1899 0.2794 0.0318  -0.0044 0.0174  65  GLN A CD  
578  O OE1 . GLN A 65  ? 0.3072 0.1893 0.2756 0.0370  -0.0042 0.0121  65  GLN A OE1 
579  N NE2 . GLN A 65  ? 0.3635 0.2233 0.3267 0.0275  -0.0046 0.0192  65  GLN A NE2 
580  N N   . GLU A 66  ? 0.2256 0.1629 0.2011 0.0487  -0.0089 0.0266  66  GLU A N   
581  C CA  . GLU A 66  ? 0.2224 0.1696 0.1990 0.0571  -0.0115 0.0293  66  GLU A CA  
582  C C   . GLU A 66  ? 0.2206 0.1785 0.1954 0.0545  -0.0134 0.0331  66  GLU A C   
583  O O   . GLU A 66  ? 0.2487 0.2072 0.2198 0.0604  -0.0160 0.0385  66  GLU A O   
584  C CB  . GLU A 66  ? 0.2542 0.2169 0.2383 0.0612  -0.0113 0.0241  66  GLU A CB  
585  C CG  . GLU A 66  ? 0.3443 0.3201 0.3314 0.0708  -0.0143 0.0264  66  GLU A CG  
586  C CD  . GLU A 66  ? 0.3074 0.2960 0.3022 0.0766  -0.0132 0.0216  66  GLU A CD  
587  O OE1 . GLU A 66  ? 0.3244 0.3123 0.3214 0.0726  -0.0101 0.0166  66  GLU A OE1 
588  O OE2 . GLU A 66  ? 0.4406 0.4413 0.4393 0.0856  -0.0154 0.0231  66  GLU A OE2 
589  N N   . TYR A 67  ? 0.1933 0.1596 0.1698 0.0462  -0.0124 0.0302  67  TYR A N   
590  C CA  . TYR A 67  ? 0.1952 0.1702 0.1685 0.0435  -0.0141 0.0326  67  TYR A CA  
591  C C   . TYR A 67  ? 0.2221 0.1848 0.1870 0.0429  -0.0137 0.0392  67  TYR A C   
592  O O   . TYR A 67  ? 0.2717 0.2391 0.2316 0.0459  -0.0159 0.0439  67  TYR A O   
593  C CB  . TYR A 67  ? 0.2078 0.1907 0.1839 0.0352  -0.0127 0.0277  67  TYR A CB  
594  C CG  . TYR A 67  ? 0.1840 0.1832 0.1672 0.0347  -0.0140 0.0229  67  TYR A CG  
595  C CD1 . TYR A 67  ? 0.1977 0.2111 0.1811 0.0353  -0.0174 0.0227  67  TYR A CD1 
596  C CD2 . TYR A 67  ? 0.1723 0.1732 0.1617 0.0332  -0.0120 0.0186  67  TYR A CD2 
597  C CE1 . TYR A 67  ? 0.1768 0.2056 0.1677 0.0333  -0.0187 0.0182  67  TYR A CE1 
598  C CE2 . TYR A 67  ? 0.1755 0.1915 0.1718 0.0316  -0.0127 0.0150  67  TYR A CE2 
599  C CZ  . TYR A 67  ? 0.1913 0.2210 0.1889 0.0312  -0.0161 0.0148  67  TYR A CZ  
600  O OH  . TYR A 67  ? 0.1720 0.2171 0.1774 0.0283  -0.0169 0.0112  67  TYR A OH  
601  N N   . ALA A 68  ? 0.2432 0.1910 0.2064 0.0388  -0.0108 0.0400  68  ALA A N   
602  C CA  . ALA A 68  ? 0.2509 0.1876 0.2070 0.0365  -0.0097 0.0467  68  ALA A CA  
603  C C   . ALA A 68  ? 0.2950 0.2221 0.2460 0.0441  -0.0116 0.0537  68  ALA A C   
604  O O   . ALA A 68  ? 0.3325 0.2555 0.2764 0.0438  -0.0115 0.0610  68  ALA A O   
605  C CB  . ALA A 68  ? 0.2671 0.1916 0.2242 0.0296  -0.0065 0.0455  68  ALA A CB  
606  N N   . GLN A 69  ? 0.2600 0.1830 0.2139 0.0515  -0.0131 0.0520  69  GLN A N   
607  C CA  . GLN A 69  ? 0.3010 0.2139 0.2503 0.0606  -0.0151 0.0586  69  GLN A CA  
608  C C   . GLN A 69  ? 0.3383 0.2679 0.2872 0.0684  -0.0189 0.0612  69  GLN A C   
609  O O   . GLN A 69  ? 0.3956 0.3210 0.3426 0.0751  -0.0210 0.0658  69  GLN A O   
610  C CB  . GLN A 69  ? 0.4056 0.3063 0.3580 0.0664  -0.0148 0.0549  69  GLN A CB  
611  C CG  . GLN A 69  ? 0.6309 0.5218 0.5857 0.0589  -0.0119 0.0490  69  GLN A CG  
612  C CD  . GLN A 69  ? 0.7748 0.6460 0.7291 0.0585  -0.0112 0.0482  69  GLN A CD  
613  O OE1 . GLN A 69  ? 0.8599 0.7247 0.8137 0.0642  -0.0126 0.0512  69  GLN A OE1 
614  N NE2 . GLN A 69  ? 0.7679 0.6308 0.7233 0.0511  -0.0091 0.0435  69  GLN A NE2 
615  N N   . GLY A 70  ? 0.3154 0.2655 0.2681 0.0651  -0.0200 0.0568  70  GLY A N   
616  C CA  . GLY A 70  ? 0.3037 0.2718 0.2569 0.0715  -0.0243 0.0582  70  GLY A CA  
617  C C   . GLY A 70  ? 0.4000 0.3771 0.3611 0.0803  -0.0264 0.0550  70  GLY A C   
618  O O   . GLY A 70  ? 0.4505 0.4418 0.4124 0.0877  -0.0305 0.0575  70  GLY A O   
619  N N   . LYS A 71  ? 0.3560 0.3269 0.3229 0.0798  -0.0236 0.0495  71  LYS A N   
620  C CA  . LYS A 71  ? 0.4032 0.3817 0.3775 0.0887  -0.0244 0.0462  71  LYS A CA  
621  C C   . LYS A 71  ? 0.3550 0.3562 0.3392 0.0848  -0.0243 0.0391  71  LYS A C   
622  O O   . LYS A 71  ? 0.4034 0.4169 0.3948 0.0921  -0.0251 0.0368  71  LYS A O   
623  C CB  . LYS A 71  ? 0.3788 0.3370 0.3525 0.0911  -0.0212 0.0439  71  LYS A CB  
624  C CG  . LYS A 71  ? 0.5457 0.4829 0.5132 0.0941  -0.0212 0.0491  71  LYS A CG  
625  C CD  . LYS A 71  ? 0.6574 0.5778 0.6260 0.0956  -0.0185 0.0444  71  LYS A CD  
626  C CE  . LYS A 71  ? 0.7434 0.6716 0.7175 0.1062  -0.0193 0.0416  71  LYS A CE  
627  N NZ  . LYS A 71  ? 0.7946 0.7060 0.7685 0.1081  -0.0167 0.0366  71  LYS A NZ  
628  N N   . ALA A 72  ? 0.2700 0.2770 0.2550 0.0738  -0.0232 0.0358  72  ALA A N   
629  C CA  . ALA A 72  ? 0.2516 0.2764 0.2455 0.0687  -0.0227 0.0294  72  ALA A CA  
630  C C   . ALA A 72  ? 0.2682 0.3159 0.2662 0.0703  -0.0272 0.0297  72  ALA A C   
631  O O   . ALA A 72  ? 0.3388 0.3894 0.3313 0.0673  -0.0299 0.0319  72  ALA A O   
632  C CB  . ALA A 72  ? 0.2990 0.3187 0.2916 0.0570  -0.0199 0.0259  72  ALA A CB  
633  N N   . LYS A 73  ? 0.2265 0.2916 0.2342 0.0749  -0.0280 0.0271  73  LYS A N   
634  C CA  . LYS A 73  ? 0.1955 0.2856 0.2093 0.0755  -0.0327 0.0266  73  LYS A CA  
635  C C   . LYS A 73  ? 0.2290 0.3312 0.2496 0.0636  -0.0315 0.0204  73  LYS A C   
636  O O   . LYS A 73  ? 0.2531 0.3667 0.2833 0.0625  -0.0294 0.0170  73  LYS A O   
637  C CB  . LYS A 73  ? 0.2376 0.3422 0.2592 0.0874  -0.0343 0.0278  73  LYS A CB  
638  C CG  . LYS A 73  ? 0.3572 0.4528 0.3721 0.1002  -0.0370 0.0346  73  LYS A CG  
639  C CD  . LYS A 73  ? 0.5021 0.6131 0.5253 0.1082  -0.0380 0.0341  73  LYS A CD  
640  C CE  . LYS A 73  ? 0.5888 0.7303 0.6225 0.1031  -0.0411 0.0306  73  LYS A CE  
641  N NZ  . LYS A 73  ? 0.6585 0.8076 0.6870 0.0990  -0.0465 0.0328  73  LYS A NZ  
642  N N   . ASP A 74  ? 0.2194 0.3185 0.2345 0.0548  -0.0326 0.0192  74  ASP A N   
643  C CA  . ASP A 74  ? 0.1806 0.2845 0.1998 0.0430  -0.0312 0.0136  74  ASP A CA  
644  C C   . ASP A 74  ? 0.1619 0.2887 0.1866 0.0394  -0.0364 0.0110  74  ASP A C   
645  O O   . ASP A 74  ? 0.1728 0.3023 0.1908 0.0390  -0.0406 0.0117  74  ASP A O   
646  C CB  . ASP A 74  ? 0.1690 0.2541 0.1786 0.0363  -0.0289 0.0131  74  ASP A CB  
647  C CG  . ASP A 74  ? 0.1911 0.2771 0.2038 0.0252  -0.0272 0.0076  74  ASP A CG  
648  O OD1 . ASP A 74  ? 0.1857 0.2875 0.2043 0.0201  -0.0299 0.0041  74  ASP A OD1 
649  O OD2 . ASP A 74  ? 0.1922 0.2623 0.2009 0.0213  -0.0233 0.0071  74  ASP A OD2 
650  N N   . VAL A 75  ? 0.1692 0.3133 0.2059 0.0364  -0.0360 0.0078  75  VAL A N   
651  C CA  . VAL A 75  ? 0.1667 0.3361 0.2112 0.0333  -0.0414 0.0054  75  VAL A CA  
652  C C   . VAL A 75  ? 0.1749 0.3426 0.2146 0.0221  -0.0439 0.0009  75  VAL A C   
653  O O   . VAL A 75  ? 0.1972 0.3778 0.2351 0.0216  -0.0499 -0.0002 75  VAL A O   
654  C CB  . VAL A 75  ? 0.2352 0.4231 0.2945 0.0309  -0.0393 0.0032  75  VAL A CB  
655  C CG1 . VAL A 75  ? 0.3171 0.5321 0.3859 0.0250  -0.0447 0.0000  75  VAL A CG1 
656  C CG2 . VAL A 75  ? 0.2706 0.4621 0.3340 0.0440  -0.0371 0.0069  75  VAL A CG2 
657  N N   . PHE A 76  ? 0.2041 0.3559 0.2412 0.0133  -0.0396 -0.0021 76  PHE A N   
658  C CA  . PHE A 76  ? 0.1983 0.3459 0.2303 0.0034  -0.0415 -0.0071 76  PHE A CA  
659  C C   . PHE A 76  ? 0.2070 0.3447 0.2253 0.0074  -0.0438 -0.0056 76  PHE A C   
660  O O   . PHE A 76  ? 0.2000 0.3447 0.2138 0.0036  -0.0485 -0.0092 76  PHE A O   
661  C CB  . PHE A 76  ? 0.2000 0.3312 0.2320 -0.0049 -0.0359 -0.0097 76  PHE A CB  
662  C CG  . PHE A 76  ? 0.2235 0.3498 0.2518 -0.0151 -0.0375 -0.0156 76  PHE A CG  
663  C CD1 . PHE A 76  ? 0.2889 0.4277 0.3257 -0.0248 -0.0397 -0.0203 76  PHE A CD1 
664  C CD2 . PHE A 76  ? 0.2434 0.3526 0.2595 -0.0150 -0.0367 -0.0167 76  PHE A CD2 
665  C CE1 . PHE A 76  ? 0.3239 0.4557 0.3565 -0.0342 -0.0414 -0.0266 76  PHE A CE1 
666  C CE2 . PHE A 76  ? 0.2971 0.4008 0.3089 -0.0233 -0.0380 -0.0230 76  PHE A CE2 
667  C CZ  . PHE A 76  ? 0.3126 0.4263 0.3323 -0.0328 -0.0405 -0.0282 76  PHE A CZ  
668  N N   . LEU A 77  ? 0.1974 0.3197 0.2087 0.0148  -0.0406 -0.0003 77  LEU A N   
669  C CA  . LEU A 77  ? 0.2012 0.3142 0.1995 0.0184  -0.0418 0.0024  77  LEU A CA  
670  C C   . LEU A 77  ? 0.2602 0.3891 0.2559 0.0251  -0.0481 0.0054  77  LEU A C   
671  O O   . LEU A 77  ? 0.2707 0.3997 0.2560 0.0250  -0.0510 0.0053  77  LEU A O   
672  C CB  . LEU A 77  ? 0.2582 0.3515 0.2513 0.0236  -0.0368 0.0079  77  LEU A CB  
673  C CG  . LEU A 77  ? 0.2986 0.3787 0.2788 0.0248  -0.0358 0.0109  77  LEU A CG  
674  C CD1 . LEU A 77  ? 0.2927 0.3700 0.2679 0.0165  -0.0353 0.0049  77  LEU A CD1 
675  C CD2 . LEU A 77  ? 0.2537 0.3154 0.2317 0.0277  -0.0306 0.0154  77  LEU A CD2 
676  N N   . GLU A 78  ? 0.2236 0.3672 0.2283 0.0316  -0.0504 0.0080  78  GLU A N   
677  C CA  . GLU A 78  ? 0.2817 0.4424 0.2847 0.0390  -0.0570 0.0112  78  GLU A CA  
678  C C   . GLU A 78  ? 0.2924 0.4723 0.2969 0.0314  -0.0630 0.0048  78  GLU A C   
679  O O   . GLU A 78  ? 0.3007 0.4901 0.2976 0.0349  -0.0686 0.0063  78  GLU A O   
680  C CB  . GLU A 78  ? 0.3112 0.4841 0.3248 0.0486  -0.0577 0.0151  78  GLU A CB  
681  C CG  . GLU A 78  ? 0.4332 0.6139 0.4422 0.0598  -0.0625 0.0214  78  GLU A CG  
682  C CD  . GLU A 78  ? 0.5464 0.7110 0.5389 0.0625  -0.0628 0.0265  78  GLU A CD  
683  O OE1 . GLU A 78  ? 0.5699 0.7415 0.5558 0.0606  -0.0668 0.0258  78  GLU A OE1 
684  O OE2 . GLU A 78  ? 0.5953 0.7387 0.5814 0.0656  -0.0584 0.0309  78  GLU A OE2 
685  N N   . ALA A 79  ? 0.2187 0.4038 0.2322 0.0206  -0.0621 -0.0023 79  ALA A N   
686  C CA  . ALA A 79  ? 0.3070 0.5066 0.3213 0.0114  -0.0676 -0.0096 79  ALA A CA  
687  C C   . ALA A 79  ? 0.2240 0.4090 0.2232 0.0070  -0.0676 -0.0131 79  ALA A C   
688  O O   . ALA A 79  ? 0.2858 0.4810 0.2795 0.0041  -0.0733 -0.0173 79  ALA A O   
689  C CB  . ALA A 79  ? 0.2709 0.4765 0.2984 0.0001  -0.0659 -0.0156 79  ALA A CB  
690  N N   . ILE A 80  ? 0.2038 0.3647 0.1963 0.0065  -0.0610 -0.0118 80  ILE A N   
691  C CA  . ILE A 80  ? 0.1981 0.3460 0.1761 0.0041  -0.0602 -0.0145 80  ILE A CA  
692  C C   . ILE A 80  ? 0.2346 0.3865 0.2005 0.0130  -0.0634 -0.0086 80  ILE A C   
693  O O   . ILE A 80  ? 0.2566 0.4127 0.2118 0.0113  -0.0670 -0.0122 80  ILE A O   
694  C CB  . ILE A 80  ? 0.2104 0.3344 0.1857 0.0027  -0.0523 -0.0134 80  ILE A CB  
695  C CG1 . ILE A 80  ? 0.2645 0.3837 0.2489 -0.0070 -0.0496 -0.0196 80  ILE A CG1 
696  C CG2 . ILE A 80  ? 0.2547 0.3671 0.2148 0.0032  -0.0508 -0.0141 80  ILE A CG2 
697  C CD1 . ILE A 80  ? 0.3561 0.4757 0.3370 -0.0160 -0.0523 -0.0288 80  ILE A CD1 
698  N N   . ARG A 81  ? 0.2523 0.4022 0.2190 0.0229  -0.0622 0.0006  81  ARG A N   
699  C CA  . ARG A 81  ? 0.2428 0.3928 0.1973 0.0317  -0.0643 0.0081  81  ARG A CA  
700  C C   . ARG A 81  ? 0.2730 0.4422 0.2264 0.0335  -0.0713 0.0072  81  ARG A C   
701  O O   . ARG A 81  ? 0.3377 0.5052 0.2788 0.0353  -0.0725 0.0090  81  ARG A O   
702  C CB  . ARG A 81  ? 0.2764 0.4166 0.2335 0.0411  -0.0610 0.0177  81  ARG A CB  
703  C CG  . ARG A 81  ? 0.4309 0.5707 0.3779 0.0510  -0.0633 0.0271  81  ARG A CG  
704  C CD  . ARG A 81  ? 0.4994 0.6271 0.4494 0.0595  -0.0601 0.0354  81  ARG A CD  
705  N NE  . ARG A 81  ? 0.5967 0.7016 0.5441 0.0563  -0.0530 0.0367  81  ARG A NE  
706  C CZ  . ARG A 81  ? 0.6922 0.7840 0.6270 0.0549  -0.0499 0.0405  81  ARG A CZ  
707  N NH1 . ARG A 81  ? 0.6708 0.7691 0.5932 0.0568  -0.0529 0.0437  81  ARG A NH1 
708  N NH2 . ARG A 81  ? 0.6113 0.6843 0.5467 0.0514  -0.0434 0.0412  81  ARG A NH2 
709  N N   . LYS A 82  ? 0.2737 0.3535 0.2600 0.0849  -0.0218 0.0461  82  LYS A N   
710  C CA  . LYS A 82  ? 0.3153 0.4199 0.2992 0.0962  -0.0250 0.0476  82  LYS A CA  
711  C C   . LYS A 82  ? 0.2311 0.3587 0.2078 0.0931  -0.0246 0.0490  82  LYS A C   
712  O O   . LYS A 82  ? 0.2565 0.3872 0.2318 0.0822  -0.0220 0.0418  82  LYS A O   
713  C CB  . LYS A 82  ? 0.2801 0.4042 0.2703 0.0990  -0.0262 0.0338  82  LYS A CB  
714  C CG  . LYS A 82  ? 0.3797 0.4968 0.3745 0.1125  -0.0284 0.0322  82  LYS A CG  
715  C CD  . LYS A 82  ? 0.3510 0.4956 0.3534 0.1121  -0.0271 0.0189  82  LYS A CD  
716  C CE  . LYS A 82  ? 0.4988 0.6436 0.5054 0.1284  -0.0283 0.0149  82  LYS A CE  
717  N NZ  . LYS A 82  ? 0.4254 0.6096 0.4418 0.1291  -0.0264 0.0055  82  LYS A NZ  
718  N N   . ASP A 83  ? 0.2437 0.3878 0.2147 0.1046  -0.0281 0.0571  83  ASP A N   
719  C CA  . ASP A 83  ? 0.2820 0.4543 0.2450 0.1042  -0.0301 0.0527  83  ASP A CA  
720  C C   . ASP A 83  ? 0.2640 0.4549 0.2347 0.0975  -0.0330 0.0343  83  ASP A C   
721  O O   . ASP A 83  ? 0.2235 0.4200 0.2042 0.1010  -0.0347 0.0296  83  ASP A O   
722  C CB  . ASP A 83  ? 0.3422 0.5322 0.2970 0.1193  -0.0349 0.0640  83  ASP A CB  
723  C CG  . ASP A 83  ? 0.3953 0.6129 0.3377 0.1202  -0.0375 0.0599  83  ASP A CG  
724  O OD1 . ASP A 83  ? 0.3327 0.5713 0.2783 0.1168  -0.0427 0.0436  83  ASP A OD1 
725  O OD2 . ASP A 83  ? 0.4798 0.6990 0.4092 0.1243  -0.0347 0.0730  83  ASP A OD2 
726  N N   . PRO A 84  ? 0.2418 0.4421 0.2091 0.0879  -0.0337 0.0239  84  PRO A N   
727  C CA  . PRO A 84  ? 0.2386 0.4527 0.2158 0.0783  -0.0372 0.0084  84  PRO A CA  
728  C C   . PRO A 84  ? 0.2708 0.5156 0.2548 0.0853  -0.0442 0.0047  84  PRO A C   
729  O O   . PRO A 84  ? 0.2612 0.5190 0.2591 0.0782  -0.0457 -0.0039 84  PRO A O   
730  C CB  . PRO A 84  ? 0.2953 0.5106 0.2647 0.0698  -0.0391 -0.0009 84  PRO A CB  
731  C CG  . PRO A 84  ? 0.2905 0.4877 0.2494 0.0725  -0.0328 0.0090  84  PRO A CG  
732  C CD  . PRO A 84  ? 0.3032 0.5001 0.2586 0.0851  -0.0312 0.0257  84  PRO A CD  
733  N N   . ASP A 85  ? 0.2589 0.5184 0.2344 0.0991  -0.0486 0.0123  85  ASP A N   
734  C CA  . ASP A 85  ? 0.2300 0.5211 0.2128 0.1080  -0.0564 0.0098  85  ASP A CA  
735  C C   . ASP A 85  ? 0.2647 0.5562 0.2618 0.1145  -0.0539 0.0124  85  ASP A C   
736  O O   . ASP A 85  ? 0.2825 0.6045 0.2919 0.1187  -0.0590 0.0072  85  ASP A O   
737  C CB  . ASP A 85  ? 0.2741 0.5746 0.2426 0.1229  -0.0601 0.0200  85  ASP A CB  
738  C CG  . ASP A 85  ? 0.3638 0.6743 0.3193 0.1183  -0.0634 0.0122  85  ASP A CG  
739  O OD1 . ASP A 85  ? 0.4271 0.7429 0.3869 0.1055  -0.0670 -0.0030 85  ASP A OD1 
740  O OD2 . ASP A 85  ? 0.4484 0.7606 0.3896 0.1279  -0.0627 0.0210  85  ASP A OD2 
741  N N   . ASP A 86  ? 0.2531 0.5133 0.2490 0.1162  -0.0468 0.0193  86  ASP A N   
742  C CA  . ASP A 86  ? 0.3003 0.5572 0.3064 0.1251  -0.0446 0.0198  86  ASP A CA  
743  C C   . ASP A 86  ? 0.2781 0.5302 0.2938 0.1124  -0.0387 0.0100  86  ASP A C   
744  O O   . ASP A 86  ? 0.2705 0.5202 0.2926 0.1202  -0.0359 0.0085  86  ASP A O   
745  C CB  . ASP A 86  ? 0.3010 0.5242 0.2990 0.1369  -0.0429 0.0329  86  ASP A CB  
746  C CG  . ASP A 86  ? 0.4262 0.6537 0.4140 0.1503  -0.0482 0.0466  86  ASP A CG  
747  O OD1 . ASP A 86  ? 0.4378 0.6965 0.4268 0.1567  -0.0538 0.0441  86  ASP A OD1 
748  O OD2 . ASP A 86  ? 0.5383 0.7372 0.5172 0.1526  -0.0464 0.0604  86  ASP A OD2 
749  N N   . LEU A 87  ? 0.2014 0.4521 0.2171 0.0943  -0.0372 0.0033  87  LEU A N   
750  C CA  . LEU A 87  ? 0.1903 0.4358 0.2135 0.0817  -0.0317 -0.0034 87  LEU A CA  
751  C C   . LEU A 87  ? 0.1879 0.4704 0.2278 0.0797  -0.0324 -0.0095 87  LEU A C   
752  O O   . LEU A 87  ? 0.1958 0.5071 0.2435 0.0752  -0.0387 -0.0133 87  LEU A O   
753  C CB  . LEU A 87  ? 0.2110 0.4428 0.2297 0.0640  -0.0311 -0.0075 87  LEU A CB  
754  C CG  . LEU A 87  ? 0.1962 0.3930 0.2024 0.0628  -0.0275 -0.0021 87  LEU A CG  
755  C CD1 . LEU A 87  ? 0.2502 0.4405 0.2521 0.0495  -0.0287 -0.0074 87  LEU A CD1 
756  C CD2 . LEU A 87  ? 0.2089 0.3832 0.2159 0.0628  -0.0219 -0.0006 87  LEU A CD2 
757  N N   . GLU A 88  ? 0.1844 0.4686 0.2303 0.0830  -0.0263 -0.0108 88  GLU A N   
758  C CA  . GLU A 88  ? 0.1792 0.5011 0.2424 0.0777  -0.0242 -0.0151 88  GLU A CA  
759  C C   . GLU A 88  ? 0.1705 0.4926 0.2388 0.0535  -0.0230 -0.0179 88  GLU A C   
760  O O   . GLU A 88  ? 0.1684 0.4574 0.2255 0.0442  -0.0212 -0.0175 88  GLU A O   
761  C CB  . GLU A 88  ? 0.1882 0.5126 0.2531 0.0897  -0.0167 -0.0159 88  GLU A CB  
762  C CG  . GLU A 88  ? 0.2775 0.5959 0.3375 0.1151  -0.0190 -0.0141 88  GLU A CG  
763  C CD  . GLU A 88  ? 0.3561 0.6632 0.4118 0.1278  -0.0129 -0.0177 88  GLU A CD  
764  O OE1 . GLU A 88  ? 0.4100 0.7048 0.4612 0.1164  -0.0069 -0.0202 88  GLU A OE1 
765  O OE2 . GLU A 88  ? 0.4952 0.8052 0.5510 0.1504  -0.0149 -0.0187 88  GLU A OE2 
766  N N   . LYS A 89  ? 0.1676 0.5276 0.2546 0.0432  -0.0246 -0.0201 89  LYS A N   
767  C CA  . LYS A 89  ? 0.1641 0.5231 0.2584 0.0192  -0.0239 -0.0210 89  LYS A CA  
768  C C   . LYS A 89  ? 0.1799 0.5145 0.2656 0.0148  -0.0142 -0.0177 89  LYS A C   
769  O O   . LYS A 89  ? 0.1739 0.4819 0.2532 0.0001  -0.0146 -0.0174 89  LYS A O   
770  C CB  . LYS A 89  ? 0.1637 0.5704 0.2833 0.0083  -0.0254 -0.0210 89  LYS A CB  
771  C CG  . LYS A 89  ? 0.2388 0.6700 0.3690 0.0061  -0.0379 -0.0260 89  LYS A CG  
772  C CD  . LYS A 89  ? 0.2504 0.7233 0.4064 -0.0072 -0.0388 -0.0248 89  LYS A CD  
773  C CE  . LYS A 89  ? 0.2474 0.7293 0.4089 -0.0127 -0.0519 -0.0308 89  LYS A CE  
774  N NZ  . LYS A 89  ? 0.2692 0.7778 0.4549 -0.0316 -0.0533 -0.0288 89  LYS A NZ  
775  N N   . GLU A 90  ? 0.1645 0.5086 0.2491 0.0288  -0.0063 -0.0161 90  GLU A N   
776  C CA  . GLU A 90  ? 0.1664 0.4892 0.2398 0.0276  0.0019  -0.0143 90  GLU A CA  
777  C C   . GLU A 90  ? 0.1893 0.4633 0.2438 0.0278  -0.0004 -0.0149 90  GLU A C   
778  O O   . GLU A 90  ? 0.1842 0.4368 0.2313 0.0173  0.0025  -0.0132 90  GLU A O   
779  C CB  . GLU A 90  ? 0.1730 0.5112 0.2446 0.0484  0.0086  -0.0160 90  GLU A CB  
780  C CG  . GLU A 90  ? 0.4879 0.8781 0.5776 0.0482  0.0148  -0.0143 90  GLU A CG  
781  C CD  . GLU A 90  ? 0.5550 0.9606 0.6408 0.0738  0.0208  -0.0185 90  GLU A CD  
782  O OE1 . GLU A 90  ? 0.5590 0.9285 0.6270 0.0894  0.0191  -0.0231 90  GLU A OE1 
783  O OE2 . GLU A 90  ? 0.5537 1.0081 0.6552 0.0785  0.0266  -0.0176 90  GLU A OE2 
784  N N   . GLU A 91  ? 0.1681 0.4265 0.2155 0.0401  -0.0056 -0.0159 91  GLU A N   
785  C CA  . GLU A 91  ? 0.1754 0.3929 0.2079 0.0404  -0.0072 -0.0147 91  GLU A CA  
786  C C   . GLU A 91  ? 0.1850 0.3904 0.2161 0.0242  -0.0109 -0.0151 91  GLU A C   
787  O O   . GLU A 91  ? 0.2130 0.3905 0.2354 0.0180  -0.0098 -0.0143 91  GLU A O   
788  C CB  . GLU A 91  ? 0.1754 0.3821 0.2021 0.0572  -0.0111 -0.0126 91  GLU A CB  
789  C CG  . GLU A 91  ? 0.1859 0.3931 0.2115 0.0757  -0.0091 -0.0135 91  GLU A CG  
790  C CD  . GLU A 91  ? 0.3005 0.4937 0.3214 0.0912  -0.0142 -0.0089 91  GLU A CD  
791  O OE1 . GLU A 91  ? 0.2237 0.4366 0.2489 0.0953  -0.0186 -0.0062 91  GLU A OE1 
792  O OE2 . GLU A 91  ? 0.3144 0.4763 0.3273 0.0988  -0.0148 -0.0075 91  GLU A OE2 
793  N N   . VAL A 92  ? 0.1748 0.4010 0.2144 0.0182  -0.0165 -0.0174 92  VAL A N   
794  C CA  . VAL A 92  ? 0.1646 0.3785 0.2026 0.0038  -0.0214 -0.0205 92  VAL A CA  
795  C C   . VAL A 92  ? 0.1794 0.3853 0.2211 -0.0122 -0.0182 -0.0193 92  VAL A C   
796  O O   . VAL A 92  ? 0.2104 0.3893 0.2446 -0.0197 -0.0195 -0.0200 92  VAL A O   
797  C CB  . VAL A 92  ? 0.1846 0.4238 0.2314 0.0005  -0.0300 -0.0255 92  VAL A CB  
798  C CG1 . VAL A 92  ? 0.2649 0.4891 0.3097 -0.0138 -0.0366 -0.0315 92  VAL A CG1 
799  C CG2 . VAL A 92  ? 0.2126 0.4583 0.2521 0.0176  -0.0333 -0.0247 92  VAL A CG2 
800  N N   . GLU A 93  ? 0.1643 0.3951 0.2176 -0.0167 -0.0137 -0.0164 93  GLU A N   
801  C CA  . GLU A 93  ? 0.1968 0.4226 0.2531 -0.0323 -0.0100 -0.0120 93  GLU A CA  
802  C C   . GLU A 93  ? 0.2434 0.4390 0.2839 -0.0279 -0.0048 -0.0093 93  GLU A C   
803  O O   . GLU A 93  ? 0.2488 0.4234 0.2851 -0.0394 -0.0054 -0.0068 93  GLU A O   
804  C CB  . GLU A 93  ? 0.2000 0.4652 0.2719 -0.0364 -0.0043 -0.0072 93  GLU A CB  
805  C CG  . GLU A 93  ? 0.2463 0.5420 0.3388 -0.0482 -0.0111 -0.0086 93  GLU A CG  
806  C CD  . GLU A 93  ? 0.4042 0.7480 0.5152 -0.0486 -0.0048 -0.0036 93  GLU A CD  
807  O OE1 . GLU A 93  ? 0.4194 0.7941 0.5510 -0.0591 -0.0105 -0.0040 93  GLU A OE1 
808  O OE2 . GLU A 93  ? 0.4123 0.7650 0.5176 -0.0379 0.0055  0.0002  93  GLU A OE2 
809  N N   . LYS A 94  ? 0.1846 0.3763 0.2165 -0.0112 -0.0010 -0.0102 94  LYS A N   
810  C CA  . LYS A 94  ? 0.1781 0.3420 0.1959 -0.0074 0.0019  -0.0092 94  LYS A CA  
811  C C   . LYS A 94  ? 0.1710 0.3035 0.1813 -0.0100 -0.0032 -0.0104 94  LYS A C   
812  O O   . LYS A 94  ? 0.2112 0.3220 0.2138 -0.0146 -0.0028 -0.0087 94  LYS A O   
813  C CB  . LYS A 94  ? 0.2400 0.4042 0.2516 0.0109  0.0047  -0.0118 94  LYS A CB  
814  C CG  . LYS A 94  ? 0.3539 0.5479 0.3691 0.0171  0.0113  -0.0119 94  LYS A CG  
815  C CD  . LYS A 94  ? 0.4888 0.6707 0.4922 0.0351  0.0128  -0.0169 94  LYS A CD  
816  C CE  . LYS A 94  ? 0.5341 0.7482 0.5429 0.0507  0.0169  -0.0204 94  LYS A CE  
817  N NZ  . LYS A 94  ? 0.4567 0.7077 0.4722 0.0439  0.0252  -0.0167 94  LYS A NZ  
818  N N   . LEU A 95  ? 0.1744 0.3069 0.1861 -0.0058 -0.0078 -0.0129 95  LEU A N   
819  C CA  . LEU A 95  ? 0.1813 0.2907 0.1864 -0.0068 -0.0114 -0.0138 95  LEU A CA  
820  C C   . LEU A 95  ? 0.2411 0.3411 0.2474 -0.0204 -0.0147 -0.0156 95  LEU A C   
821  O O   . LEU A 95  ? 0.2074 0.2848 0.2074 -0.0222 -0.0156 -0.0154 95  LEU A O   
822  C CB  . LEU A 95  ? 0.2083 0.3256 0.2131 0.0017  -0.0148 -0.0151 95  LEU A CB  
823  C CG  . LEU A 95  ? 0.3700 0.4708 0.3672 0.0044  -0.0167 -0.0149 95  LEU A CG  
824  C CD1 . LEU A 95  ? 0.4303 0.5087 0.4230 0.0059  -0.0136 -0.0108 95  LEU A CD1 
825  C CD2 . LEU A 95  ? 0.4777 0.5907 0.4727 0.0153  -0.0183 -0.0129 95  LEU A CD2 
826  N N   . ILE A 96  ? 0.2180 0.3346 0.2339 -0.0302 -0.0176 -0.0174 96  ILE A N   
827  C CA  . ILE A 96  ? 0.2134 0.3168 0.2318 -0.0442 -0.0226 -0.0189 96  ILE A CA  
828  C C   . ILE A 96  ? 0.2672 0.3578 0.2830 -0.0517 -0.0183 -0.0116 96  ILE A C   
829  O O   . ILE A 96  ? 0.2742 0.3399 0.2849 -0.0565 -0.0214 -0.0113 96  ILE A O   
830  C CB  . ILE A 96  ? 0.2280 0.3527 0.2601 -0.0549 -0.0283 -0.0221 96  ILE A CB  
831  C CG1 . ILE A 96  ? 0.2216 0.3558 0.2522 -0.0466 -0.0347 -0.0308 96  ILE A CG1 
832  C CG2 . ILE A 96  ? 0.2936 0.4009 0.3304 -0.0719 -0.0343 -0.0222 96  ILE A CG2 
833  C CD1 . ILE A 96  ? 0.2561 0.4182 0.3014 -0.0546 -0.0415 -0.0349 96  ILE A CD1 
834  N N   . GLU A 97  ? 0.2349 0.3435 0.2530 -0.0508 -0.0113 -0.0058 97  GLU A N   
835  C CA  . GLU A 97  ? 0.2548 0.3554 0.2674 -0.0562 -0.0067 0.0019  97  GLU A CA  
836  C C   . GLU A 97  ? 0.2384 0.3116 0.2371 -0.0481 -0.0071 0.0011  97  GLU A C   
837  O O   . GLU A 97  ? 0.2511 0.3057 0.2443 -0.0541 -0.0084 0.0055  97  GLU A O   
838  C CB  . GLU A 97  ? 0.2900 0.4194 0.3048 -0.0522 0.0015  0.0061  97  GLU A CB  
839  C CG  . GLU A 97  ? 0.5260 0.6520 0.5312 -0.0547 0.0072  0.0140  97  GLU A CG  
840  C CD  . GLU A 97  ? 0.7123 0.8685 0.7161 -0.0454 0.0159  0.0153  97  GLU A CD  
841  O OE1 . GLU A 97  ? 0.7597 0.9223 0.7557 -0.0477 0.0217  0.0225  97  GLU A OE1 
842  O OE2 . GLU A 97  ? 0.7060 0.8802 0.7153 -0.0343 0.0168  0.0091  97  GLU A OE2 
843  N N   . PHE A 98  ? 0.1984 0.2693 0.1928 -0.0348 -0.0066 -0.0036 98  PHE A N   
844  C CA  . PHE A 98  ? 0.2031 0.2513 0.1883 -0.0285 -0.0078 -0.0041 98  PHE A CA  
845  C C   . PHE A 98  ? 0.2310 0.2601 0.2158 -0.0322 -0.0132 -0.0057 98  PHE A C   
846  O O   . PHE A 98  ? 0.2202 0.2316 0.1995 -0.0327 -0.0148 -0.0037 98  PHE A O   
847  C CB  . PHE A 98  ? 0.2038 0.2537 0.1879 -0.0159 -0.0072 -0.0072 98  PHE A CB  
848  C CG  . PHE A 98  ? 0.2091 0.2396 0.1871 -0.0107 -0.0088 -0.0070 98  PHE A CG  
849  C CD1 . PHE A 98  ? 0.2199 0.2464 0.1908 -0.0075 -0.0077 -0.0073 98  PHE A CD1 
850  C CD2 . PHE A 98  ? 0.2238 0.2434 0.2037 -0.0086 -0.0115 -0.0071 98  PHE A CD2 
851  C CE1 . PHE A 98  ? 0.2075 0.2166 0.1746 -0.0040 -0.0113 -0.0083 98  PHE A CE1 
852  C CE2 . PHE A 98  ? 0.2430 0.2484 0.2213 -0.0057 -0.0135 -0.0060 98  PHE A CE2 
853  C CZ  . PHE A 98  ? 0.2287 0.2278 0.2014 -0.0041 -0.0143 -0.0070 98  PHE A CZ  
854  N N   . THR A 99  ? 0.2244 0.2581 0.2143 -0.0332 -0.0165 -0.0103 99  THR A N   
855  C CA  . THR A 99  ? 0.2251 0.2421 0.2135 -0.0343 -0.0219 -0.0144 99  THR A CA  
856  C C   . THR A 99  ? 0.2361 0.2371 0.2243 -0.0450 -0.0253 -0.0115 99  THR A C   
857  O O   . THR A 99  ? 0.2627 0.2436 0.2463 -0.0431 -0.0283 -0.0115 99  THR A O   
858  C CB  . THR A 99  ? 0.2314 0.2588 0.2231 -0.0328 -0.0258 -0.0217 99  THR A CB  
859  O OG1 . THR A 99  ? 0.2092 0.2515 0.2001 -0.0226 -0.0226 -0.0214 99  THR A OG1 
860  C CG2 . THR A 99  ? 0.2144 0.2257 0.2018 -0.0297 -0.0311 -0.0283 99  THR A CG2 
861  N N   . LYS A 100 ? 0.2220 0.2325 0.2163 -0.0563 -0.0251 -0.0078 100 LYS A N   
862  C CA  . LYS A 100 ? 0.2252 0.2192 0.2205 -0.0686 -0.0288 -0.0021 100 LYS A CA  
863  C C   . LYS A 100 ? 0.2516 0.2344 0.2378 -0.0671 -0.0254 0.0069  100 LYS A C   
864  O O   . LYS A 100 ? 0.2832 0.2431 0.2660 -0.0712 -0.0301 0.0108  100 LYS A O   
865  C CB  . LYS A 100 ? 0.2776 0.2897 0.2845 -0.0829 -0.0283 0.0028  100 LYS A CB  
866  C CG  . LYS A 100 ? 0.3853 0.3972 0.4018 -0.0896 -0.0372 -0.0062 100 LYS A CG  
867  C CD  . LYS A 100 ? 0.4111 0.4474 0.4434 -0.1049 -0.0371 -0.0011 100 LYS A CD  
868  C CE  . LYS A 100 ? 0.5059 0.5467 0.5478 -0.1094 -0.0474 -0.0131 100 LYS A CE  
869  N NZ  . LYS A 100 ? 0.4504 0.5226 0.5113 -0.1238 -0.0478 -0.0087 100 LYS A NZ  
870  N N   . LEU A 101 ? 0.2291 0.2265 0.2103 -0.0602 -0.0186 0.0094  101 LEU A N   
871  C CA  . LEU A 101 ? 0.2411 0.2295 0.2115 -0.0572 -0.0169 0.0156  101 LEU A CA  
872  C C   . LEU A 101 ? 0.2702 0.2365 0.2361 -0.0497 -0.0223 0.0120  101 LEU A C   
873  O O   . LEU A 101 ? 0.2893 0.2407 0.2483 -0.0503 -0.0250 0.0177  101 LEU A O   
874  C CB  . LEU A 101 ? 0.2521 0.2588 0.2174 -0.0488 -0.0106 0.0147  101 LEU A CB  
875  C CG  . LEU A 101 ? 0.3009 0.3007 0.2531 -0.0434 -0.0102 0.0178  101 LEU A CG  
876  C CD1 . LEU A 101 ? 0.2827 0.2839 0.2286 -0.0523 -0.0081 0.0295  101 LEU A CD1 
877  C CD2 . LEU A 101 ? 0.3267 0.3409 0.2742 -0.0329 -0.0063 0.0123  101 LEU A CD2 
878  N N   . ASN A 102 ? 0.2539 0.2206 0.2240 -0.0422 -0.0237 0.0037  102 ASN A N   
879  C CA  . ASN A 102 ? 0.2285 0.1828 0.1972 -0.0339 -0.0271 0.0007  102 ASN A CA  
880  C C   . ASN A 102 ? 0.2611 0.2018 0.2324 -0.0330 -0.0326 -0.0043 102 ASN A C   
881  O O   . ASN A 102 ? 0.2567 0.1903 0.2280 -0.0248 -0.0351 -0.0069 102 ASN A O   
882  C CB  . ASN A 102 ? 0.1981 0.1641 0.1697 -0.0255 -0.0242 -0.0031 102 ASN A CB  
883  C CG  . ASN A 102 ? 0.2539 0.2267 0.2217 -0.0236 -0.0212 -0.0008 102 ASN A CG  
884  O OD1 . ASN A 102 ? 0.2809 0.2463 0.2430 -0.0228 -0.0232 0.0018  102 ASN A OD1 
885  N ND2 . ASN A 102 ? 0.2563 0.2429 0.2264 -0.0213 -0.0175 -0.0026 102 ASN A ND2 
886  N N   . TYR A 103 ? 0.2633 0.2009 0.2376 -0.0412 -0.0354 -0.0060 103 TYR A N   
887  C CA  . TYR A 103 ? 0.3287 0.2555 0.3050 -0.0389 -0.0416 -0.0153 103 TYR A CA  
888  C C   . TYR A 103 ? 0.3137 0.2168 0.2864 -0.0328 -0.0476 -0.0164 103 TYR A C   
889  O O   . TYR A 103 ? 0.3144 0.2134 0.2867 -0.0229 -0.0509 -0.0261 103 TYR A O   
890  C CB  . TYR A 103 ? 0.3074 0.2326 0.2889 -0.0520 -0.0456 -0.0161 103 TYR A CB  
891  C CG  . TYR A 103 ? 0.3631 0.2740 0.3459 -0.0510 -0.0548 -0.0281 103 TYR A CG  
892  C CD1 . TYR A 103 ? 0.3615 0.2884 0.3456 -0.0464 -0.0559 -0.0390 103 TYR A CD1 
893  C CD2 . TYR A 103 ? 0.4044 0.2848 0.3860 -0.0540 -0.0636 -0.0289 103 TYR A CD2 
894  C CE1 . TYR A 103 ? 0.4224 0.3367 0.4053 -0.0442 -0.0655 -0.0525 103 TYR A CE1 
895  C CE2 . TYR A 103 ? 0.4677 0.3317 0.4493 -0.0518 -0.0737 -0.0427 103 TYR A CE2 
896  C CZ  . TYR A 103 ? 0.5024 0.3843 0.4841 -0.0467 -0.0747 -0.0554 103 TYR A CZ  
897  O OH  . TYR A 103 ? 0.5464 0.4126 0.5257 -0.0430 -0.0859 -0.0714 103 TYR A OH  
898  N N   . GLU A 104 ? 0.2920 0.1808 0.2612 -0.0371 -0.0492 -0.0068 104 GLU A N   
899  C CA  . GLU A 104 ? 0.3490 0.2137 0.3151 -0.0307 -0.0562 -0.0068 104 GLU A CA  
900  C C   . GLU A 104 ? 0.2938 0.1651 0.2588 -0.0180 -0.0546 -0.0064 104 GLU A C   
901  O O   . GLU A 104 ? 0.3608 0.2162 0.3245 -0.0099 -0.0604 -0.0069 104 GLU A O   
902  C CB  . GLU A 104 ? 0.3574 0.2023 0.3198 -0.0412 -0.0600 0.0057  104 GLU A CB  
903  C CG  . GLU A 104 ? 0.4780 0.3155 0.4451 -0.0567 -0.0627 0.0080  104 GLU A CG  
904  C CD  . GLU A 104 ? 0.6360 0.4488 0.6062 -0.0552 -0.0732 -0.0034 104 GLU A CD  
905  O OE1 . GLU A 104 ? 0.6684 0.4671 0.6351 -0.0404 -0.0781 -0.0114 104 GLU A OE1 
906  O OE2 . GLU A 104 ? 0.6065 0.4149 0.5833 -0.0683 -0.0773 -0.0050 104 GLU A OE2 
907  N N   . LYS A 105 ? 0.2737 0.1672 0.2404 -0.0164 -0.0478 -0.0052 105 LYS A N   
908  C CA  . LYS A 105 ? 0.2530 0.1543 0.2221 -0.0071 -0.0474 -0.0043 105 LYS A CA  
909  C C   . LYS A 105 ? 0.2395 0.1489 0.2149 0.0042  -0.0471 -0.0128 105 LYS A C   
910  O O   . LYS A 105 ? 0.2505 0.1685 0.2270 0.0049  -0.0443 -0.0191 105 LYS A O   
911  C CB  . LYS A 105 ? 0.2346 0.1534 0.2046 -0.0100 -0.0420 -0.0010 105 LYS A CB  
912  C CG  . LYS A 105 ? 0.2442 0.1603 0.2057 -0.0183 -0.0411 0.0061  105 LYS A CG  
913  C CD  . LYS A 105 ? 0.2279 0.1596 0.1889 -0.0190 -0.0363 0.0059  105 LYS A CD  
914  C CE  . LYS A 105 ? 0.2629 0.1958 0.2135 -0.0246 -0.0345 0.0116  105 LYS A CE  
915  N NZ  . LYS A 105 ? 0.2727 0.2185 0.2207 -0.0222 -0.0312 0.0089  105 LYS A NZ  
916  N N   . PRO A 106 ? 0.2431 0.1529 0.2225 0.0142  -0.0500 -0.0129 106 PRO A N   
917  C CA  . PRO A 106 ? 0.2419 0.1646 0.2273 0.0266  -0.0484 -0.0204 106 PRO A CA  
918  C C   . PRO A 106 ? 0.2399 0.1889 0.2314 0.0265  -0.0403 -0.0199 106 PRO A C   
919  O O   . PRO A 106 ? 0.2519 0.2138 0.2446 0.0349  -0.0372 -0.0259 106 PRO A O   
920  C CB  . PRO A 106 ? 0.2478 0.1713 0.2389 0.0364  -0.0526 -0.0180 106 PRO A CB  
921  C CG  . PRO A 106 ? 0.2673 0.1651 0.2502 0.0309  -0.0597 -0.0123 106 PRO A CG  
922  C CD  . PRO A 106 ? 0.2537 0.1521 0.2312 0.0162  -0.0559 -0.0066 106 PRO A CD  
923  N N   . ILE A 107 ? 0.2078 0.1646 0.2020 0.0181  -0.0372 -0.0129 107 ILE A N   
924  C CA  . ILE A 107 ? 0.1937 0.1711 0.1939 0.0177  -0.0306 -0.0107 107 ILE A CA  
925  C C   . ILE A 107 ? 0.2130 0.1925 0.2065 0.0158  -0.0276 -0.0150 107 ILE A C   
926  O O   . ILE A 107 ? 0.2044 0.2008 0.2007 0.0178  -0.0224 -0.0130 107 ILE A O   
927  C CB  . ILE A 107 ? 0.1917 0.1724 0.1967 0.0103  -0.0300 -0.0035 107 ILE A CB  
928  C CG1 . ILE A 107 ? 0.1966 0.1634 0.1917 0.0023  -0.0317 -0.0033 107 ILE A CG1 
929  C CG2 . ILE A 107 ? 0.1899 0.1746 0.2046 0.0122  -0.0340 0.0001  107 ILE A CG2 
930  C CD1 . ILE A 107 ? 0.2096 0.1799 0.2071 -0.0023 -0.0310 0.0003  107 ILE A CD1 
931  N N   . TYR A 108 ? 0.2077 0.1713 0.1933 0.0114  -0.0314 -0.0196 108 TYR A N   
932  C CA  . TYR A 108 ? 0.2186 0.1856 0.1996 0.0093  -0.0308 -0.0253 108 TYR A CA  
933  C C   . TYR A 108 ? 0.2672 0.2286 0.2437 0.0170  -0.0351 -0.0363 108 TYR A C   
934  O O   . TYR A 108 ? 0.2544 0.2137 0.2267 0.0140  -0.0380 -0.0432 108 TYR A O   
935  C CB  . TYR A 108 ? 0.2346 0.1919 0.2129 -0.0026 -0.0326 -0.0231 108 TYR A CB  
936  C CG  . TYR A 108 ? 0.2060 0.1767 0.1861 -0.0066 -0.0274 -0.0174 108 TYR A CG  
937  C CD1 . TYR A 108 ? 0.2299 0.2007 0.2119 -0.0071 -0.0257 -0.0110 108 TYR A CD1 
938  C CD2 . TYR A 108 ? 0.2328 0.2155 0.2128 -0.0087 -0.0256 -0.0195 108 TYR A CD2 
939  C CE1 . TYR A 108 ? 0.2244 0.2036 0.2073 -0.0087 -0.0223 -0.0078 108 TYR A CE1 
940  C CE2 . TYR A 108 ? 0.2138 0.2074 0.1955 -0.0097 -0.0216 -0.0149 108 TYR A CE2 
941  C CZ  . TYR A 108 ? 0.1926 0.1827 0.1752 -0.0093 -0.0200 -0.0095 108 TYR A CZ  
942  O OH  . TYR A 108 ? 0.2162 0.2132 0.1996 -0.0084 -0.0173 -0.0068 108 TYR A OH  
943  N N   . ARG A 109 ? 0.2555 0.2158 0.2333 0.0280  -0.0363 -0.0394 109 ARG A N   
944  C CA  . ARG A 109 ? 0.2505 0.2025 0.2225 0.0386  -0.0415 -0.0524 109 ARG A CA  
945  C C   . ARG A 109 ? 0.2659 0.2431 0.2342 0.0487  -0.0365 -0.0584 109 ARG A C   
946  O O   . ARG A 109 ? 0.3003 0.2957 0.2700 0.0619  -0.0320 -0.0594 109 ARG A O   
947  C CB  . ARG A 109 ? 0.3084 0.2512 0.2831 0.0492  -0.0449 -0.0536 109 ARG A CB  
948  C CG  . ARG A 109 ? 0.4419 0.3664 0.4093 0.0608  -0.0531 -0.0686 109 ARG A CG  
949  C CD  . ARG A 109 ? 0.5740 0.4825 0.5444 0.0699  -0.0584 -0.0679 109 ARG A CD  
950  N NE  . ARG A 109 ? 0.6249 0.5064 0.5955 0.0565  -0.0642 -0.0585 109 ARG A NE  
951  C CZ  . ARG A 109 ? 0.6284 0.5061 0.6034 0.0574  -0.0655 -0.0488 109 ARG A CZ  
952  N NH1 . ARG A 109 ? 0.6510 0.5505 0.6339 0.0700  -0.0621 -0.0476 109 ARG A NH1 
953  N NH2 . ARG A 109 ? 0.6599 0.5146 0.6319 0.0457  -0.0704 -0.0395 109 ARG A NH2 
954  N N   . PHE A 110 ? 0.2530 0.2343 0.2164 0.0426  -0.0372 -0.0615 110 PHE A N   
955  C CA  . PHE A 110 ? 0.2780 0.2808 0.2338 0.0518  -0.0347 -0.0685 110 PHE A CA  
956  C C   . PHE A 110 ? 0.2726 0.2599 0.2203 0.0498  -0.0450 -0.0838 110 PHE A C   
957  O O   . PHE A 110 ? 0.3043 0.2788 0.2555 0.0352  -0.0496 -0.0821 110 PHE A O   
958  C CB  . PHE A 110 ? 0.2446 0.2692 0.2027 0.0464  -0.0274 -0.0572 110 PHE A CB  
959  C CG  . PHE A 110 ? 0.2155 0.2533 0.1830 0.0459  -0.0189 -0.0419 110 PHE A CG  
960  C CD1 . PHE A 110 ? 0.2515 0.3143 0.2200 0.0566  -0.0115 -0.0369 110 PHE A CD1 
961  C CD2 . PHE A 110 ? 0.2455 0.2724 0.2212 0.0344  -0.0186 -0.0325 110 PHE A CD2 
962  C CE1 . PHE A 110 ? 0.2494 0.3236 0.2299 0.0532  -0.0050 -0.0217 110 PHE A CE1 
963  C CE2 . PHE A 110 ? 0.2588 0.2950 0.2440 0.0329  -0.0132 -0.0201 110 PHE A CE2 
964  C CZ  . PHE A 110 ? 0.2163 0.2751 0.2054 0.0410  -0.0069 -0.0143 110 PHE A CZ  
965  N N   . GLU A 111 ? 0.2939 0.2844 0.2312 0.0645  -0.0489 -0.0990 111 GLU A N   
966  C CA  . GLU A 111 ? 0.3265 0.3007 0.2562 0.0627  -0.0612 -0.1161 111 GLU A CA  
967  C C   . GLU A 111 ? 0.3213 0.3100 0.2512 0.0517  -0.0620 -0.1140 111 GLU A C   
968  O O   . GLU A 111 ? 0.3636 0.3361 0.2960 0.0397  -0.0723 -0.1211 111 GLU A O   
969  C CB  . GLU A 111 ? 0.3625 0.3423 0.2783 0.0840  -0.0647 -0.1346 111 GLU A CB  
970  C CG  . GLU A 111 ? 0.6964 0.6561 0.6031 0.0843  -0.0801 -0.1561 111 GLU A CG  
971  C CD  . GLU A 111 ? 0.8276 0.7446 0.7427 0.0694  -0.0924 -0.1588 111 GLU A CD  
972  O OE1 . GLU A 111 ? 0.8609 0.7585 0.7824 0.0694  -0.0912 -0.1513 111 GLU A OE1 
973  O OE2 . GLU A 111 ? 0.8690 0.7734 0.7852 0.0569  -0.1036 -0.1671 111 GLU A OE2 
974  N N   . ARG A 112 ? 0.3267 0.3455 0.2560 0.0548  -0.0518 -0.1028 112 ARG A N   
975  C CA  . ARG A 112 ? 0.3292 0.3636 0.2586 0.0472  -0.0530 -0.1004 112 ARG A CA  
976  C C   . ARG A 112 ? 0.3239 0.3468 0.2669 0.0284  -0.0539 -0.0907 112 ARG A C   
977  O O   . ARG A 112 ? 0.3150 0.3433 0.2611 0.0195  -0.0595 -0.0937 112 ARG A O   
978  C CB  . ARG A 112 ? 0.2906 0.3565 0.2159 0.0561  -0.0420 -0.0883 112 ARG A CB  
979  C CG  . ARG A 112 ? 0.2600 0.3439 0.1850 0.0516  -0.0429 -0.0839 112 ARG A CG  
980  C CD  . ARG A 112 ? 0.2821 0.3723 0.1962 0.0558  -0.0542 -0.1019 112 ARG A CD  
981  N NE  . ARG A 112 ? 0.2897 0.4067 0.1994 0.0587  -0.0532 -0.0962 112 ARG A NE  
982  C CZ  . ARG A 112 ? 0.3612 0.4884 0.2654 0.0586  -0.0641 -0.1087 112 ARG A CZ  
983  N NH1 . ARG A 112 ? 0.3654 0.4757 0.2685 0.0542  -0.0774 -0.1284 112 ARG A NH1 
984  N NH2 . ARG A 112 ? 0.3545 0.5077 0.2547 0.0631  -0.0630 -0.1015 112 ARG A NH2 
985  N N   . ILE A 113 ? 0.2713 0.2818 0.2224 0.0227  -0.0486 -0.0792 113 ILE A N   
986  C CA  . ILE A 113 ? 0.2446 0.2463 0.2060 0.0066  -0.0490 -0.0707 113 ILE A CA  
987  C C   . ILE A 113 ? 0.3023 0.2829 0.2667 -0.0046 -0.0602 -0.0796 113 ILE A C   
988  O O   . ILE A 113 ? 0.3283 0.3133 0.3007 -0.0178 -0.0628 -0.0770 113 ILE A O   
989  C CB  . ILE A 113 ? 0.2757 0.2687 0.2421 0.0046  -0.0422 -0.0580 113 ILE A CB  
990  C CG1 . ILE A 113 ? 0.2921 0.3051 0.2600 0.0094  -0.0328 -0.0471 113 ILE A CG1 
991  C CG2 . ILE A 113 ? 0.3039 0.2828 0.2770 -0.0104 -0.0441 -0.0518 113 ILE A CG2 
992  C CD1 . ILE A 113 ? 0.3809 0.3874 0.3530 0.0104  -0.0280 -0.0378 113 ILE A CD1 
993  N N   . ARG A 114 ? 0.3245 0.2824 0.2841 0.0005  -0.0673 -0.0900 114 ARG A N   
994  C CA  . ARG A 114 ? 0.3468 0.2790 0.3100 -0.0110 -0.0799 -0.0982 114 ARG A CA  
995  C C   . ARG A 114 ? 0.4200 0.3639 0.3832 -0.0150 -0.0888 -0.1107 114 ARG A C   
996  O O   . ARG A 114 ? 0.4090 0.3460 0.3827 -0.0322 -0.0964 -0.1106 114 ARG A O   
997  C CB  . ARG A 114 ? 0.4407 0.3435 0.3974 -0.0011 -0.0872 -0.1085 114 ARG A CB  
998  C CG  . ARG A 114 ? 0.5332 0.4283 0.4905 0.0049  -0.0796 -0.0969 114 ARG A CG  
999  C CD  . ARG A 114 ? 0.6767 0.5393 0.6299 0.0136  -0.0886 -0.1058 114 ARG A CD  
1000 N NE  . ARG A 114 ? 0.7582 0.6311 0.7019 0.0364  -0.0869 -0.1180 114 ARG A NE  
1001 C CZ  . ARG A 114 ? 0.7851 0.6756 0.7292 0.0485  -0.0768 -0.1106 114 ARG A CZ  
1002 N NH1 . ARG A 114 ? 0.7329 0.6291 0.6851 0.0401  -0.0691 -0.0928 114 ARG A NH1 
1003 N NH2 . ARG A 114 ? 0.8188 0.7233 0.7555 0.0692  -0.0746 -0.1212 114 ARG A NH2 
1004 N N   . GLU A 115 ? 0.3953 0.3597 0.3473 0.0004  -0.0880 -0.1206 115 GLU A N   
1005 C CA  . GLU A 115 ? 0.3671 0.3474 0.3172 -0.0015 -0.0969 -0.1326 115 GLU A CA  
1006 C C   . GLU A 115 ? 0.3919 0.3960 0.3544 -0.0146 -0.0929 -0.1203 115 GLU A C   
1007 O O   . GLU A 115 ? 0.4519 0.4596 0.4239 -0.0276 -0.1028 -0.1259 115 GLU A O   
1008 C CB  . GLU A 115 ? 0.3934 0.3962 0.3261 0.0196  -0.0945 -0.1420 115 GLU A CB  
1009 C CG  . GLU A 115 ? 0.5004 0.4869 0.4192 0.0359  -0.0997 -0.1585 115 GLU A CG  
1010 C CD  . GLU A 115 ? 0.6174 0.6343 0.5186 0.0576  -0.0932 -0.1631 115 GLU A CD  
1011 O OE1 . GLU A 115 ? 0.5444 0.5905 0.4425 0.0584  -0.0903 -0.1582 115 GLU A OE1 
1012 O OE2 . GLU A 115 ? 0.7595 0.7731 0.6499 0.0748  -0.0908 -0.1706 115 GLU A OE2 
1013 N N   . LEU A 116 ? 0.3471 0.3689 0.3107 -0.0104 -0.0791 -0.1044 116 LEU A N   
1014 C CA  . LEU A 116 ? 0.3411 0.3872 0.3148 -0.0180 -0.0750 -0.0941 116 LEU A CA  
1015 C C   . LEU A 116 ? 0.3705 0.4081 0.3605 -0.0377 -0.0769 -0.0873 116 LEU A C   
1016 O O   . LEU A 116 ? 0.4102 0.4677 0.4117 -0.0472 -0.0797 -0.0858 116 LEU A O   
1017 C CB  . LEU A 116 ? 0.3144 0.3742 0.2854 -0.0085 -0.0612 -0.0794 116 LEU A CB  
1018 C CG  . LEU A 116 ? 0.2939 0.3692 0.2509 0.0093  -0.0574 -0.0809 116 LEU A CG  
1019 C CD1 . LEU A 116 ? 0.2903 0.3719 0.2480 0.0150  -0.0450 -0.0643 116 LEU A CD1 
1020 C CD2 . LEU A 116 ? 0.3436 0.4434 0.2960 0.0138  -0.0638 -0.0878 116 LEU A CD2 
1021 N N   . MET A 117 ? 0.3735 0.3847 0.3653 -0.0436 -0.0751 -0.0818 117 MET A N   
1022 C CA  . MET A 117 ? 0.3162 0.3214 0.3218 -0.0622 -0.0754 -0.0721 117 MET A CA  
1023 C C   . MET A 117 ? 0.4209 0.4131 0.4362 -0.0777 -0.0896 -0.0808 117 MET A C   
1024 O O   . MET A 117 ? 0.4978 0.4933 0.5280 -0.0958 -0.0902 -0.0714 117 MET A O   
1025 C CB  . MET A 117 ? 0.3385 0.3215 0.3410 -0.0626 -0.0689 -0.0612 117 MET A CB  
1026 C CG  . MET A 117 ? 0.3380 0.3342 0.3346 -0.0507 -0.0564 -0.0523 117 MET A CG  
1027 S SD  . MET A 117 ? 0.3960 0.4196 0.4027 -0.0587 -0.0479 -0.0396 117 MET A SD  
1028 C CE  . MET A 117 ? 0.5136 0.5677 0.5192 -0.0464 -0.0457 -0.0439 117 MET A CE  
1029 N N   . ASN A 118 ? 0.3797 0.3590 0.3873 -0.0714 -0.1014 -0.0986 118 ASN A N   
1030 C CA  . ASN A 118 ? 0.4577 0.4220 0.4745 -0.0860 -0.1180 -0.1100 118 ASN A CA  
1031 C C   . ASN A 118 ? 0.4918 0.4869 0.5146 -0.0886 -0.1257 -0.1200 118 ASN A C   
1032 O O   . ASN A 118 ? 0.5622 0.5470 0.5913 -0.0989 -0.1414 -0.1328 118 ASN A O   
1033 C CB  . ASN A 118 ? 0.5711 0.4987 0.5748 -0.0762 -0.1292 -0.1270 118 ASN A CB  
1034 C CG  . ASN A 118 ? 0.7264 0.6184 0.7290 -0.0784 -0.1269 -0.1177 118 ASN A CG  
1035 O OD1 . ASN A 118 ? 0.8063 0.6942 0.8207 -0.0943 -0.1222 -0.1001 118 ASN A OD1 
1036 N ND2 . ASN A 118 ? 0.8219 0.6905 0.8097 -0.0609 -0.1301 -0.1291 118 ASN A ND2 
1037 N N   . LYS A 119 ? 0.4083 0.4397 0.4292 -0.0791 -0.1158 -0.1139 119 LYS A N   
1038 C CA  . LYS A 119 ? 0.3888 0.4528 0.4135 -0.0778 -0.1230 -0.1225 119 LYS A CA  
1039 C C   . LYS A 119 ? 0.5079 0.6016 0.5556 -0.0939 -0.1199 -0.1098 119 LYS A C   
1040 O O   . LYS A 119 ? 0.5593 0.6632 0.6118 -0.0942 -0.1057 -0.0930 119 LYS A O   
1041 C CB  . LYS A 119 ? 0.4287 0.5142 0.4350 -0.0544 -0.1152 -0.1236 119 LYS A CB  
1042 C CG  . LYS A 119 ? 0.5148 0.5842 0.4991 -0.0375 -0.1206 -0.1397 119 LYS A CG  
1043 C CD  . LYS A 119 ? 0.5747 0.6736 0.5429 -0.0174 -0.1159 -0.1407 119 LYS A CD  
1044 C CE  . LYS A 119 ? 0.5402 0.6276 0.4856 0.0020  -0.1145 -0.1505 119 LYS A CE  
1045 N NZ  . LYS A 119 ? 0.5993 0.6711 0.5370 0.0041  -0.1264 -0.1677 119 LYS A NZ  
1046 N N   . GLU A 120 ? 0.6233 0.7329 0.6855 -0.1062 -0.1341 -0.1192 120 GLU A N   
1047 C CA  . GLU A 120 ? 0.6418 0.7870 0.7292 -0.1215 -0.1326 -0.1086 120 GLU A CA  
1048 C C   . GLU A 120 ? 0.5403 0.7237 0.6246 -0.1050 -0.1203 -0.0999 120 GLU A C   
1049 O O   . GLU A 120 ? 0.5182 0.7212 0.6147 -0.1088 -0.1083 -0.0844 120 GLU A O   
1050 C CB  . GLU A 120 ? 0.7094 0.8582 0.8092 -0.1335 -0.1503 -0.1172 120 GLU A CB  
1051 C CG  . GLU A 120 ? 0.8387 0.9975 0.9202 -0.1162 -0.1587 -0.1313 120 GLU A CG  
1052 C CD  . GLU A 120 ? 0.8973 1.0279 0.9478 -0.0967 -0.1582 -0.1439 120 GLU A CD  
1053 O OE1 . GLU A 120 ? 0.9185 1.0105 0.9622 -0.1020 -0.1621 -0.1499 120 GLU A OE1 
1054 O OE2 . GLU A 120 ? 0.8815 1.0301 0.9150 -0.0752 -0.1526 -0.1462 120 GLU A OE2 
1055 N N   . LYS A 121 ? 0.5183 0.7122 0.5852 -0.0855 -0.1232 -0.1096 121 LYS A N   
1056 C CA  . LYS A 121 ? 0.4320 0.6575 0.4942 -0.0683 -0.1140 -0.1016 121 LYS A CA  
1057 C C   . LYS A 121 ? 0.4143 0.6247 0.4489 -0.0463 -0.1081 -0.1033 121 LYS A C   
1058 O O   . LYS A 121 ? 0.4766 0.6661 0.4959 -0.0418 -0.1153 -0.1161 121 LYS A O   
1059 C CB  . LYS A 121 ? 0.4376 0.6970 0.5087 -0.0665 -0.1238 -0.1064 121 LYS A CB  
1060 C CG  . LYS A 121 ? 0.4831 0.7576 0.5833 -0.0877 -0.1298 -0.1030 121 LYS A CG  
1061 C CD  . LYS A 121 ? 0.4799 0.7851 0.5869 -0.0822 -0.1379 -0.1060 121 LYS A CD  
1062 C CE  . LYS A 121 ? 0.4391 0.7465 0.5698 -0.1039 -0.1520 -0.1098 121 LYS A CE  
1063 N NZ  . LYS A 121 ? 0.4839 0.8246 0.6228 -0.0986 -0.1602 -0.1125 121 LYS A NZ  
1064 N N   . LEU A 122 ? 0.3397 0.5615 0.3686 -0.0324 -0.0952 -0.0902 122 LEU A N   
1065 C CA  . LEU A 122 ? 0.3610 0.5713 0.3677 -0.0138 -0.0878 -0.0870 122 LEU A CA  
1066 C C   . LEU A 122 ? 0.3687 0.6083 0.3682 0.0026  -0.0880 -0.0832 122 LEU A C   
1067 O O   . LEU A 122 ? 0.3337 0.5958 0.3454 0.0039  -0.0853 -0.0749 122 LEU A O   
1068 C CB  . LEU A 122 ? 0.3192 0.5102 0.3250 -0.0124 -0.0732 -0.0731 122 LEU A CB  
1069 C CG  . LEU A 122 ? 0.3090 0.4706 0.3198 -0.0262 -0.0711 -0.0728 122 LEU A CG  
1070 C CD1 . LEU A 122 ? 0.3842 0.5324 0.3921 -0.0218 -0.0578 -0.0596 122 LEU A CD1 
1071 C CD2 . LEU A 122 ? 0.3440 0.4817 0.3429 -0.0254 -0.0784 -0.0855 122 LEU A CD2 
1072 N N   . ASN A 123 ? 0.2507 0.4911 0.2298 0.0164  -0.0911 -0.0887 123 ASN A N   
1073 C CA  . ASN A 123 ? 0.2863 0.5526 0.2551 0.0332  -0.0911 -0.0824 123 ASN A CA  
1074 C C   . ASN A 123 ? 0.2616 0.5172 0.2210 0.0451  -0.0766 -0.0648 123 ASN A C   
1075 O O   . ASN A 123 ? 0.2787 0.5099 0.2414 0.0396  -0.0675 -0.0588 123 ASN A O   
1076 C CB  . ASN A 123 ? 0.3208 0.5903 0.2737 0.0412  -0.0986 -0.0937 123 ASN A CB  
1077 C CG  . ASN A 123 ? 0.3656 0.6134 0.3003 0.0465  -0.0961 -0.1007 123 ASN A CG  
1078 O OD1 . ASN A 123 ? 0.3319 0.5677 0.2612 0.0492  -0.0871 -0.0930 123 ASN A OD1 
1079 N ND2 . ASN A 123 ? 0.4021 0.6460 0.3273 0.0490  -0.1042 -0.1155 123 ASN A ND2 
1080 N N   . ARG A 124 ? 0.2616 0.4862 0.2163 0.0027  -0.0719 -0.0345 124 ARG A N   
1081 C CA  . ARG A 124 ? 0.2547 0.4693 0.2089 0.0161  -0.0674 -0.0274 124 ARG A CA  
1082 C C   . ARG A 124 ? 0.2863 0.4721 0.2278 0.0164  -0.0610 -0.0251 124 ARG A C   
1083 O O   . ARG A 124 ? 0.2812 0.4552 0.2258 0.0201  -0.0546 -0.0209 124 ARG A O   
1084 C CB  . ARG A 124 ? 0.2983 0.5230 0.2490 0.0283  -0.0740 -0.0238 124 ARG A CB  
1085 C CG  . ARG A 124 ? 0.2872 0.4989 0.2359 0.0410  -0.0711 -0.0156 124 ARG A CG  
1086 C CD  . ARG A 124 ? 0.3078 0.5211 0.2466 0.0514  -0.0785 -0.0100 124 ARG A CD  
1087 N NE  . ARG A 124 ? 0.3159 0.5114 0.2501 0.0607  -0.0761 -0.0011 124 ARG A NE  
1088 C CZ  . ARG A 124 ? 0.4404 0.6150 0.3603 0.0593  -0.0707 0.0040  124 ARG A CZ  
1089 N NH1 . ARG A 124 ? 0.4598 0.6294 0.3688 0.0511  -0.0674 0.0000  124 ARG A NH1 
1090 N NH2 . ARG A 124 ? 0.3964 0.5557 0.3129 0.0661  -0.0690 0.0125  124 ARG A NH2 
1091 N N   . GLU A 125 ? 0.3141 0.4900 0.2415 0.0130  -0.0630 -0.0287 125 GLU A N   
1092 C CA  . GLU A 125 ? 0.3330 0.4858 0.2490 0.0144  -0.0574 -0.0283 125 GLU A CA  
1093 C C   . GLU A 125 ? 0.2562 0.3944 0.1770 0.0070  -0.0526 -0.0306 125 GLU A C   
1094 O O   . GLU A 125 ? 0.2430 0.3660 0.1622 0.0107  -0.0463 -0.0276 125 GLU A O   
1095 C CB  . GLU A 125 ? 0.3740 0.5233 0.2746 0.0129  -0.0612 -0.0342 125 GLU A CB  
1096 C CG  . GLU A 125 ? 0.4837 0.6442 0.3752 0.0205  -0.0652 -0.0303 125 GLU A CG  
1097 C CD  . GLU A 125 ? 0.6349 0.8179 0.5345 0.0212  -0.0732 -0.0295 125 GLU A CD  
1098 O OE1 . GLU A 125 ? 0.6085 0.7989 0.5072 0.0303  -0.0758 -0.0222 125 GLU A OE1 
1099 O OE2 . GLU A 125 ? 0.5893 0.7826 0.4963 0.0126  -0.0775 -0.0360 125 GLU A OE2 
1100 N N   . GLU A 126 ? 0.3026 0.4457 0.2290 -0.0042 -0.0561 -0.0353 126 GLU A N   
1101 C CA  . GLU A 126 ? 0.2803 0.4084 0.2096 -0.0127 -0.0531 -0.0362 126 GLU A CA  
1102 C C   . GLU A 126 ? 0.2217 0.3545 0.1627 -0.0101 -0.0470 -0.0301 126 GLU A C   
1103 O O   . GLU A 126 ? 0.2178 0.3337 0.1580 -0.0105 -0.0422 -0.0281 126 GLU A O   
1104 C CB  . GLU A 126 ? 0.2672 0.3991 0.1976 -0.0278 -0.0595 -0.0415 126 GLU A CB  
1105 C CG  . GLU A 126 ? 0.2805 0.3990 0.1971 -0.0309 -0.0657 -0.0493 126 GLU A CG  
1106 C CD  . GLU A 126 ? 0.3654 0.4936 0.2828 -0.0448 -0.0741 -0.0546 126 GLU A CD  
1107 O OE1 . GLU A 126 ? 0.3567 0.5085 0.2861 -0.0514 -0.0750 -0.0522 126 GLU A OE1 
1108 O OE2 . GLU A 126 ? 0.4060 0.5191 0.3118 -0.0490 -0.0801 -0.0621 126 GLU A OE2 
1109 N N   . LEU A 127 ? 0.2680 0.4243 0.2201 -0.0065 -0.0478 -0.0278 127 LEU A N   
1110 C CA  . LEU A 127 ? 0.2749 0.4366 0.2379 -0.0022 -0.0424 -0.0236 127 LEU A CA  
1111 C C   . LEU A 127 ? 0.2778 0.4238 0.2362 0.0099  -0.0377 -0.0185 127 LEU A C   
1112 O O   . LEU A 127 ? 0.2118 0.3499 0.1744 0.0113  -0.0323 -0.0158 127 LEU A O   
1113 C CB  . LEU A 127 ? 0.2926 0.4846 0.2689 0.0011  -0.0454 -0.0245 127 LEU A CB  
1114 C CG  . LEU A 127 ? 0.2872 0.5004 0.2719 -0.0130 -0.0480 -0.0290 127 LEU A CG  
1115 C CD1 . LEU A 127 ? 0.3200 0.5666 0.3164 -0.0080 -0.0532 -0.0318 127 LEU A CD1 
1116 C CD2 . LEU A 127 ? 0.3122 0.5259 0.3036 -0.0211 -0.0421 -0.0278 127 LEU A CD2 
1117 N N   . LEU A 128 ? 0.2487 0.3909 0.1979 0.0175  -0.0400 -0.0169 128 LEU A N   
1118 C CA  . LEU A 128 ? 0.2394 0.3666 0.1825 0.0261  -0.0356 -0.0114 128 LEU A CA  
1119 C C   . LEU A 128 ? 0.2279 0.3353 0.1656 0.0221  -0.0302 -0.0126 128 LEU A C   
1120 O O   . LEU A 128 ? 0.2100 0.3075 0.1495 0.0258  -0.0250 -0.0087 128 LEU A O   
1121 C CB  . LEU A 128 ? 0.2679 0.3960 0.1995 0.0320  -0.0392 -0.0090 128 LEU A CB  
1122 C CG  . LEU A 128 ? 0.3560 0.4883 0.2884 0.0422  -0.0418 -0.0017 128 LEU A CG  
1123 C CD1 . LEU A 128 ? 0.3038 0.4385 0.2225 0.0453  -0.0467 0.0009  128 LEU A CD1 
1124 C CD2 . LEU A 128 ? 0.3605 0.4772 0.2933 0.0462  -0.0358 0.0041  128 LEU A CD2 
1125 N N   . ASP A 129 ? 0.2561 0.3571 0.1873 0.0151  -0.0324 -0.0186 129 ASP A N   
1126 C CA  . ASP A 129 ? 0.2492 0.3311 0.1761 0.0125  -0.0291 -0.0210 129 ASP A CA  
1127 C C   . ASP A 129 ? 0.2232 0.3008 0.1591 0.0071  -0.0264 -0.0192 129 ASP A C   
1128 O O   . ASP A 129 ? 0.2397 0.3043 0.1755 0.0093  -0.0220 -0.0174 129 ASP A O   
1129 C CB  . ASP A 129 ? 0.2440 0.3180 0.1617 0.0070  -0.0340 -0.0290 129 ASP A CB  
1130 C CG  . ASP A 129 ? 0.2786 0.3538 0.1848 0.0134  -0.0347 -0.0319 129 ASP A CG  
1131 O OD1 . ASP A 129 ? 0.3090 0.3910 0.2138 0.0205  -0.0314 -0.0261 129 ASP A OD1 
1132 O OD2 . ASP A 129 ? 0.3074 0.3762 0.2050 0.0109  -0.0389 -0.0401 129 ASP A OD2 
1133 N N   . LEU A 130 ? 0.2331 0.3239 0.1767 -0.0003 -0.0291 -0.0197 130 LEU A N   
1134 C CA  . LEU A 130 ? 0.2446 0.3347 0.1955 -0.0068 -0.0263 -0.0177 130 LEU A CA  
1135 C C   . LEU A 130 ? 0.1887 0.2813 0.1463 0.0018  -0.0205 -0.0130 130 LEU A C   
1136 O O   . LEU A 130 ? 0.2210 0.3023 0.1793 0.0007  -0.0167 -0.0111 130 LEU A O   
1137 C CB  . LEU A 130 ? 0.2248 0.3349 0.1830 -0.0171 -0.0296 -0.0193 130 LEU A CB  
1138 C CG  . LEU A 130 ? 0.2583 0.3685 0.2211 -0.0273 -0.0271 -0.0174 130 LEU A CG  
1139 C CD1 . LEU A 130 ? 0.3252 0.4074 0.2778 -0.0347 -0.0288 -0.0173 130 LEU A CD1 
1140 C CD2 . LEU A 130 ? 0.2855 0.4210 0.2561 -0.0388 -0.0297 -0.0190 130 LEU A CD2 
1141 N N   . GLN A 131 ? 0.1905 0.2964 0.1525 0.0107  -0.0208 -0.0112 131 GLN A N   
1142 C CA  . GLN A 131 ? 0.1901 0.2950 0.1573 0.0195  -0.0168 -0.0072 131 GLN A CA  
1143 C C   . GLN A 131 ? 0.1943 0.2787 0.1541 0.0233  -0.0129 -0.0043 131 GLN A C   
1144 O O   . GLN A 131 ? 0.1896 0.2663 0.1524 0.0240  -0.0087 -0.0025 131 GLN A O   
1145 C CB  . GLN A 131 ? 0.1975 0.3151 0.1681 0.0293  -0.0202 -0.0055 131 GLN A CB  
1146 C CG  . GLN A 131 ? 0.1788 0.3214 0.1594 0.0284  -0.0243 -0.0092 131 GLN A CG  
1147 C CD  . GLN A 131 ? 0.1997 0.3514 0.1809 0.0393  -0.0299 -0.0076 131 GLN A CD  
1148 O OE1 . GLN A 131 ? 0.2076 0.3503 0.1782 0.0422  -0.0326 -0.0047 131 GLN A OE1 
1149 N NE2 . GLN A 131 ? 0.2015 0.3715 0.1947 0.0459  -0.0323 -0.0098 131 GLN A NE2 
1150 N N   . THR A 132 ? 0.1810 0.2593 0.1312 0.0257  -0.0142 -0.0043 132 THR A N   
1151 C CA  . THR A 132 ? 0.2059 0.2708 0.1500 0.0297  -0.0101 -0.0018 132 THR A CA  
1152 C C   . THR A 132 ? 0.2091 0.2610 0.1519 0.0253  -0.0076 -0.0049 132 THR A C   
1153 O O   . THR A 132 ? 0.2129 0.2565 0.1566 0.0278  -0.0034 -0.0026 132 THR A O   
1154 C CB  . THR A 132 ? 0.2109 0.2770 0.1444 0.0326  -0.0119 -0.0017 132 THR A CB  
1155 O OG1 . THR A 132 ? 0.2225 0.2995 0.1564 0.0367  -0.0159 0.0019  132 THR A OG1 
1156 C CG2 . THR A 132 ? 0.2458 0.3036 0.1737 0.0358  -0.0070 0.0015  132 THR A CG2 
1157 N N   . LEU A 133 ? 0.2246 0.2735 0.1650 0.0187  -0.0111 -0.0099 133 LEU A N   
1158 C CA  . LEU A 133 ? 0.2426 0.2759 0.1808 0.0154  -0.0107 -0.0126 133 LEU A CA  
1159 C C   . LEU A 133 ? 0.2744 0.3056 0.2197 0.0120  -0.0083 -0.0092 133 LEU A C   
1160 O O   . LEU A 133 ? 0.2289 0.2476 0.1733 0.0125  -0.0067 -0.0090 133 LEU A O   
1161 C CB  . LEU A 133 ? 0.2332 0.2594 0.1654 0.0087  -0.0169 -0.0185 133 LEU A CB  
1162 C CG  . LEU A 133 ? 0.2514 0.2762 0.1747 0.0133  -0.0190 -0.0241 133 LEU A CG  
1163 C CD1 . LEU A 133 ? 0.3055 0.3265 0.2235 0.0060  -0.0265 -0.0302 133 LEU A CD1 
1164 C CD2 . LEU A 133 ? 0.2785 0.2915 0.1978 0.0198  -0.0165 -0.0274 133 LEU A CD2 
1165 N N   . ASN A 134 ? 0.2333 0.2781 0.1856 0.0088  -0.0083 -0.0071 134 ASN A N   
1166 C CA  . ASN A 134 ? 0.2184 0.2645 0.1770 0.0064  -0.0052 -0.0045 134 ASN A CA  
1167 C C   . ASN A 134 ? 0.2521 0.2941 0.2132 0.0150  -0.0005 -0.0015 134 ASN A C   
1168 O O   . ASN A 134 ? 0.2194 0.2530 0.1814 0.0140  0.0018  -0.0003 134 ASN A O   
1169 C CB  . ASN A 134 ? 0.1814 0.2480 0.1479 0.0024  -0.0057 -0.0047 134 ASN A CB  
1170 C CG  . ASN A 134 ? 0.1946 0.2635 0.1596 -0.0111 -0.0087 -0.0059 134 ASN A CG  
1171 O OD1 . ASN A 134 ? 0.2332 0.2980 0.1981 -0.0178 -0.0073 -0.0040 134 ASN A OD1 
1172 N ND2 . ASN A 134 ? 0.2052 0.2801 0.1680 -0.0162 -0.0134 -0.0085 134 ASN A ND2 
1173 N N   . LEU A 135 ? 0.1999 0.2465 0.1612 0.0225  0.0001  0.0002  135 LEU A N   
1174 C CA  . LEU A 135 ? 0.1869 0.2271 0.1489 0.0286  0.0036  0.0037  135 LEU A CA  
1175 C C   . LEU A 135 ? 0.2088 0.2365 0.1657 0.0284  0.0057  0.0030  135 LEU A C   
1176 O O   . LEU A 135 ? 0.1989 0.2203 0.1584 0.0289  0.0085  0.0042  135 LEU A O   
1177 C CB  . LEU A 135 ? 0.2210 0.2651 0.1809 0.0350  0.0025  0.0069  135 LEU A CB  
1178 C CG  . LEU A 135 ? 0.2788 0.3323 0.2450 0.0398  0.0001  0.0083  135 LEU A CG  
1179 C CD1 . LEU A 135 ? 0.2482 0.2997 0.2087 0.0456  -0.0026 0.0130  135 LEU A CD1 
1180 C CD2 . LEU A 135 ? 0.2032 0.2542 0.1764 0.0418  0.0025  0.0085  135 LEU A CD2 
1181 N N   . LEU A 136 ? 0.2032 0.2289 0.1533 0.0283  0.0039  -0.0001 136 LEU A N   
1182 C CA  . LEU A 136 ? 0.2051 0.2230 0.1512 0.0304  0.0057  -0.0024 136 LEU A CA  
1183 C C   . LEU A 136 ? 0.2217 0.2287 0.1690 0.0277  0.0045  -0.0051 136 LEU A C   
1184 O O   . LEU A 136 ? 0.2196 0.2212 0.1672 0.0307  0.0064  -0.0062 136 LEU A O   
1185 C CB  . LEU A 136 ? 0.2402 0.2605 0.1783 0.0319  0.0036  -0.0070 136 LEU A CB  
1186 C CG  . LEU A 136 ? 0.2293 0.2593 0.1629 0.0350  0.0051  -0.0036 136 LEU A CG  
1187 C CD1 . LEU A 136 ? 0.2589 0.2933 0.1838 0.0355  0.0023  -0.0092 136 LEU A CD1 
1188 C CD2 . LEU A 136 ? 0.2677 0.2986 0.2012 0.0375  0.0103  0.0003  136 LEU A CD2 
1189 N N   . ALA A 137 ? 0.2118 0.2160 0.1596 0.0213  0.0008  -0.0058 137 ALA A N   
1190 C CA  . ALA A 137 ? 0.1887 0.1800 0.1356 0.0175  -0.0016 -0.0066 137 ALA A CA  
1191 C C   . ALA A 137 ? 0.2050 0.1954 0.1570 0.0190  0.0023  -0.0030 137 ALA A C   
1192 O O   . ALA A 137 ? 0.2221 0.2015 0.1728 0.0192  0.0007  -0.0037 137 ALA A O   
1193 C CB  . ALA A 137 ? 0.2462 0.2367 0.1916 0.0076  -0.0058 -0.0060 137 ALA A CB  
1194 N N   . TRP A 138 ? 0.1962 0.1970 0.1537 0.0208  0.0064  0.0004  138 TRP A N   
1195 C CA  . TRP A 138 ? 0.1947 0.1947 0.1569 0.0221  0.0096  0.0030  138 TRP A CA  
1196 C C   . TRP A 138 ? 0.1791 0.1789 0.1426 0.0280  0.0130  0.0040  138 TRP A C   
1197 O O   . TRP A 138 ? 0.2023 0.2024 0.1699 0.0291  0.0155  0.0063  138 TRP A O   
1198 C CB  . TRP A 138 ? 0.2123 0.2226 0.1797 0.0204  0.0110  0.0048  138 TRP A CB  
1199 C CG  . TRP A 138 ? 0.1928 0.2070 0.1591 0.0122  0.0085  0.0041  138 TRP A CG  
1200 C CD1 . TRP A 138 ? 0.2194 0.2412 0.1846 0.0081  0.0059  0.0028  138 TRP A CD1 
1201 C CD2 . TRP A 138 ? 0.1848 0.1964 0.1501 0.0056  0.0081  0.0053  138 TRP A CD2 
1202 N NE1 . TRP A 138 ? 0.2199 0.2442 0.1838 -0.0017 0.0041  0.0033  138 TRP A NE1 
1203 C CE2 . TRP A 138 ? 0.1981 0.2160 0.1612 -0.0035 0.0055  0.0052  138 TRP A CE2 
1204 C CE3 . TRP A 138 ? 0.2141 0.2195 0.1795 0.0057  0.0095  0.0067  138 TRP A CE3 
1205 C CZ2 . TRP A 138 ? 0.2311 0.2490 0.1910 -0.0135 0.0044  0.0074  138 TRP A CZ2 
1206 C CZ3 . TRP A 138 ? 0.2569 0.2617 0.2188 -0.0029 0.0080  0.0085  138 TRP A CZ3 
1207 C CH2 . TRP A 138 ? 0.2708 0.2817 0.2296 -0.0128 0.0057  0.0093  138 TRP A CH2 
1208 N N   . CYS A 139 ? 0.1787 0.1788 0.1382 0.0310  0.0129  0.0018  139 CYS A N   
1209 C CA  . CYS A 139 ? 0.1727 0.1761 0.1329 0.0346  0.0166  0.0031  139 CYS A CA  
1210 C C   . CYS A 139 ? 0.1744 0.1737 0.1382 0.0354  0.0176  0.0019  139 CYS A C   
1211 O O   . CYS A 139 ? 0.1945 0.1874 0.1572 0.0362  0.0145  -0.0022 139 CYS A O   
1212 C CB  . CYS A 139 ? 0.1871 0.1955 0.1417 0.0371  0.0167  -0.0002 139 CYS A CB  
1213 S SG  . CYS A 139 ? 0.2220 0.2400 0.1754 0.0383  0.0219  0.0036  139 CYS A SG  
1214 N N   . GLY A 140 ? 0.1795 0.1813 0.1472 0.0354  0.0209  0.0054  140 GLY A N   
1215 C CA  . GLY A 140 ? 0.1768 0.1776 0.1488 0.0360  0.0218  0.0042  140 GLY A CA  
1216 C C   . GLY A 140 ? 0.2056 0.2145 0.1778 0.0390  0.0238  0.0009  140 GLY A C   
1217 O O   . GLY A 140 ? 0.1833 0.1994 0.1515 0.0399  0.0254  0.0000  140 GLY A O   
1218 N N   . ARG A 141 ? 0.1824 0.1925 0.1595 0.0404  0.0238  -0.0014 141 ARG A N   
1219 C CA  . ARG A 141 ? 0.1470 0.1689 0.1265 0.0443  0.0255  -0.0065 141 ARG A CA  
1220 C C   . ARG A 141 ? 0.1608 0.1967 0.1394 0.0411  0.0311  -0.0032 141 ARG A C   
1221 O O   . ARG A 141 ? 0.1787 0.2267 0.1548 0.0435  0.0331  -0.0074 141 ARG A O   
1222 C CB  . ARG A 141 ? 0.1668 0.1897 0.1533 0.0460  0.0242  -0.0086 141 ARG A CB  
1223 C CG  . ARG A 141 ? 0.1561 0.1962 0.1479 0.0502  0.0263  -0.0146 141 ARG A CG  
1224 C CD  . ARG A 141 ? 0.1840 0.2239 0.1832 0.0527  0.0232  -0.0169 141 ARG A CD  
1225 N NE  . ARG A 141 ? 0.2013 0.2623 0.2082 0.0566  0.0254  -0.0229 141 ARG A NE  
1226 C CZ  . ARG A 141 ? 0.1746 0.2510 0.1877 0.0508  0.0302  -0.0200 141 ARG A CZ  
1227 N NH1 . ARG A 141 ? 0.1926 0.2617 0.2042 0.0418  0.0325  -0.0113 141 ARG A NH1 
1228 N NH2 . ARG A 141 ? 0.2058 0.3051 0.2266 0.0541  0.0324  -0.0264 141 ARG A NH2 
1229 N N   . THR A 142 ? 0.1732 0.2070 0.1525 0.0352  0.0333  0.0043  142 THR A N   
1230 C CA  . THR A 142 ? 0.1710 0.2154 0.1478 0.0301  0.0376  0.0093  142 THR A CA  
1231 C C   . THR A 142 ? 0.1804 0.2275 0.1484 0.0305  0.0379  0.0105  142 THR A C   
1232 O O   . THR A 142 ? 0.1996 0.2618 0.1639 0.0295  0.0413  0.0092  142 THR A O   
1233 C CB  . THR A 142 ? 0.1998 0.2353 0.1775 0.0240  0.0375  0.0173  142 THR A CB  
1234 O OG1 . THR A 142 ? 0.1998 0.2352 0.1852 0.0230  0.0373  0.0155  142 THR A OG1 
1235 C CG2 . THR A 142 ? 0.2463 0.2888 0.2189 0.0168  0.0405  0.0243  142 THR A CG2 
1236 N N   . LEU A 143 ? 0.2162 0.2512 0.1807 0.0317  0.0344  0.0125  143 LEU A N   
1237 C CA  . LEU A 143 ? 0.1982 0.2358 0.1542 0.0318  0.0339  0.0143  143 LEU A CA  
1238 C C   . LEU A 143 ? 0.2506 0.2938 0.2037 0.0366  0.0328  0.0057  143 LEU A C   
1239 O O   . LEU A 143 ? 0.2635 0.3127 0.2088 0.0367  0.0329  0.0057  143 LEU A O   
1240 C CB  . LEU A 143 ? 0.2010 0.2267 0.1555 0.0317  0.0300  0.0190  143 LEU A CB  
1241 C CG  . LEU A 143 ? 0.2482 0.2667 0.2028 0.0281  0.0296  0.0272  143 LEU A CG  
1242 C CD1 . LEU A 143 ? 0.2654 0.2748 0.2194 0.0308  0.0250  0.0295  143 LEU A CD1 
1243 C CD2 . LEU A 143 ? 0.2434 0.2683 0.1906 0.0230  0.0318  0.0338  143 LEU A CD2 
1244 N N   . ARG A 144 ? 0.1996 0.2398 0.1575 0.0409  0.0309  -0.0018 144 ARG A N   
1245 C CA  . ARG A 144 ? 0.2161 0.2594 0.1706 0.0463  0.0288  -0.0111 144 ARG A CA  
1246 C C   . ARG A 144 ? 0.2775 0.3406 0.2296 0.0478  0.0334  -0.0153 144 ARG A C   
1247 O O   . ARG A 144 ? 0.3051 0.3739 0.2519 0.0521  0.0323  -0.0229 144 ARG A O   
1248 C CB  . ARG A 144 ? 0.2010 0.2338 0.1604 0.0507  0.0242  -0.0176 144 ARG A CB  
1249 C CG  . ARG A 144 ? 0.2082 0.2239 0.1651 0.0489  0.0185  -0.0164 144 ARG A CG  
1250 C CD  . ARG A 144 ? 0.2475 0.2500 0.2077 0.0505  0.0136  -0.0190 144 ARG A CD  
1251 N NE  . ARG A 144 ? 0.2576 0.2461 0.2142 0.0460  0.0086  -0.0168 144 ARG A NE  
1252 C CZ  . ARG A 144 ? 0.3449 0.3233 0.2957 0.0464  0.0026  -0.0216 144 ARG A CZ  
1253 N NH1 . ARG A 144 ? 0.3502 0.3298 0.2981 0.0530  0.0005  -0.0302 144 ARG A NH1 
1254 N NH2 . ARG A 144 ? 0.3354 0.3034 0.2833 0.0399  -0.0014 -0.0185 144 ARG A NH2 
1255 N N   . LYS A 145 ? 0.3013 0.3763 0.2567 0.0435  0.0386  -0.0105 145 LYS A N   
1256 C CA  . LYS A 145 ? 0.4105 0.5085 0.3624 0.0420  0.0441  -0.0124 145 LYS A CA  
1257 C C   . LYS A 145 ? 0.4038 0.5047 0.3447 0.0354  0.0458  -0.0036 145 LYS A C   
1258 O O   . LYS A 145 ? 0.4290 0.5419 0.3617 0.0368  0.0470  -0.0077 145 LYS A O   
1259 C CB  . LYS A 145 ? 0.5374 0.6489 0.4973 0.0383  0.0486  -0.0108 145 LYS A CB  
1260 C CG  . LYS A 145 ? 0.5959 0.7064 0.5667 0.0457  0.0461  -0.0197 145 LYS A CG  
1261 C CD  . LYS A 145 ? 0.6606 0.7587 0.6385 0.0415  0.0447  -0.0129 145 LYS A CD  
1262 C CE  . LYS A 145 ? 0.6994 0.8159 0.6833 0.0346  0.0500  -0.0096 145 LYS A CE  
1263 N NZ  . LYS A 145 ? 0.6786 0.7842 0.6703 0.0321  0.0478  -0.0060 145 LYS A NZ  
1264 N N   . ASP A 146 ? 0.3612 0.4503 0.3009 0.0288  0.0450  0.0081  146 ASP A N   
1265 C CA  . ASP A 146 ? 0.3897 0.4774 0.3182 0.0233  0.0445  0.0177  146 ASP A CA  
1266 C C   . ASP A 146 ? 0.3832 0.4671 0.3047 0.0281  0.0405  0.0140  146 ASP A C   
1267 O O   . ASP A 146 ? 0.4825 0.5758 0.3931 0.0259  0.0411  0.0163  146 ASP A O   
1268 C CB  . ASP A 146 ? 0.4984 0.5681 0.4282 0.0188  0.0415  0.0286  146 ASP A CB  
1269 C CG  . ASP A 146 ? 0.5749 0.6464 0.5100 0.0122  0.0446  0.0332  146 ASP A CG  
1270 O OD1 . ASP A 146 ? 0.4974 0.5757 0.4422 0.0146  0.0469  0.0262  146 ASP A OD1 
1271 O OD2 . ASP A 146 ? 0.6193 0.6843 0.5487 0.0046  0.0438  0.0441  146 ASP A OD2 
1272 N N   . LEU A 147 ? 0.2886 0.3593 0.2155 0.0335  0.0360  0.0088  147 LEU A N   
1273 C CA  . LEU A 147 ? 0.2278 0.2937 0.1494 0.0365  0.0313  0.0058  147 LEU A CA  
1274 C C   . LEU A 147 ? 0.2851 0.3556 0.2058 0.0421  0.0301  -0.0071 147 LEU A C   
1275 O O   . LEU A 147 ? 0.2813 0.3444 0.1998 0.0441  0.0251  -0.0112 147 LEU A O   
1276 C CB  . LEU A 147 ? 0.2666 0.3165 0.1938 0.0369  0.0266  0.0089  147 LEU A CB  
1277 C CG  . LEU A 147 ? 0.2464 0.2884 0.1753 0.0339  0.0257  0.0194  147 LEU A CG  
1278 C CD1 . LEU A 147 ? 0.2690 0.3001 0.2055 0.0357  0.0221  0.0189  147 LEU A CD1 
1279 C CD2 . LEU A 147 ? 0.3087 0.3531 0.2276 0.0320  0.0237  0.0271  147 LEU A CD2 
1280 N N   . LYS A 148 ? 0.2668 0.3501 0.1894 0.0447  0.0340  -0.0141 148 LYS A N   
1281 C CA  . LYS A 148 ? 0.2584 0.3432 0.1813 0.0522  0.0315  -0.0280 148 LYS A CA  
1282 C C   . LYS A 148 ? 0.3003 0.3884 0.2126 0.0538  0.0285  -0.0334 148 LYS A C   
1283 O O   . LYS A 148 ? 0.2612 0.3391 0.1727 0.0584  0.0228  -0.0427 148 LYS A O   
1284 C CB  . LYS A 148 ? 0.3020 0.4054 0.2290 0.0560  0.0364  -0.0355 148 LYS A CB  
1285 C CG  . LYS A 148 ? 0.4273 0.5559 0.3456 0.0552  0.0417  -0.0388 148 LYS A CG  
1286 C CD  . LYS A 148 ? 0.4978 0.6488 0.4232 0.0567  0.0472  -0.0444 148 LYS A CD  
1287 C CE  . LYS A 148 ? 0.5408 0.7091 0.4634 0.0586  0.0475  -0.0536 148 LYS A CE  
1288 N NZ  . LYS A 148 ? 0.5862 0.7583 0.4952 0.0525  0.0483  -0.0478 148 LYS A NZ  
1289 N N   . ASP A 149 ? 0.3267 0.4276 0.2297 0.0493  0.0316  -0.0273 149 ASP A N   
1290 C CA  . ASP A 149 ? 0.2982 0.4049 0.1900 0.0507  0.0288  -0.0328 149 ASP A CA  
1291 C C   . ASP A 149 ? 0.2902 0.3806 0.1808 0.0491  0.0218  -0.0295 149 ASP A C   
1292 O O   . ASP A 149 ? 0.3011 0.3885 0.1869 0.0517  0.0168  -0.0382 149 ASP A O   
1293 C CB  . ASP A 149 ? 0.3642 0.4904 0.2448 0.0455  0.0338  -0.0260 149 ASP A CB  
1294 C CG  . ASP A 149 ? 0.3374 0.4827 0.2205 0.0437  0.0417  -0.0261 149 ASP A CG  
1295 O OD1 . ASP A 149 ? 0.3217 0.4769 0.2101 0.0485  0.0426  -0.0384 149 ASP A OD1 
1296 O OD2 . ASP A 149 ? 0.3889 0.5346 0.2727 0.0363  0.0449  -0.0133 149 ASP A OD2 
1297 N N   . LEU A 150 ? 0.2862 0.3674 0.1811 0.0448  0.0210  -0.0176 150 LEU A N   
1298 C CA  . LEU A 150 ? 0.2920 0.3614 0.1886 0.0436  0.0148  -0.0155 150 LEU A CA  
1299 C C   . LEU A 150 ? 0.2632 0.3194 0.1666 0.0454  0.0108  -0.0236 150 LEU A C   
1300 O O   . LEU A 150 ? 0.2897 0.3404 0.1910 0.0443  0.0050  -0.0276 150 LEU A O   
1301 C CB  . LEU A 150 ? 0.3488 0.4123 0.2503 0.0406  0.0147  -0.0033 150 LEU A CB  
1302 C CG  . LEU A 150 ? 0.2810 0.3505 0.1742 0.0383  0.0141  0.0066  150 LEU A CG  
1303 C CD1 . LEU A 150 ? 0.3098 0.3694 0.2095 0.0378  0.0115  0.0156  150 LEU A CD1 
1304 C CD2 . LEU A 150 ? 0.2533 0.3301 0.1366 0.0389  0.0096  0.0033  150 LEU A CD2 
1305 N N   . LEU A 151 ? 0.2341 0.2847 0.1450 0.0472  0.0130  -0.0254 151 LEU A N   
1306 C CA  . LEU A 151 ? 0.2295 0.2649 0.1450 0.0483  0.0082  -0.0317 151 LEU A CA  
1307 C C   . LEU A 151 ? 0.2717 0.3047 0.1806 0.0524  0.0035  -0.0443 151 LEU A C   
1308 O O   . LEU A 151 ? 0.3237 0.3427 0.2313 0.0504  -0.0034 -0.0482 151 LEU A O   
1309 C CB  . LEU A 151 ? 0.2301 0.2612 0.1537 0.0504  0.0109  -0.0312 151 LEU A CB  
1310 C CG  . LEU A 151 ? 0.2271 0.2542 0.1579 0.0462  0.0131  -0.0209 151 LEU A CG  
1311 C CD1 . LEU A 151 ? 0.2753 0.3042 0.2127 0.0483  0.0170  -0.0205 151 LEU A CD1 
1312 C CD2 . LEU A 151 ? 0.2906 0.3041 0.2241 0.0424  0.0080  -0.0198 151 LEU A CD2 
1313 N N   . ASN A 152 ? 0.2501 0.2970 0.1542 0.0576  0.0068  -0.0511 152 ASN A N   
1314 C CA  . ASN A 152 ? 0.2702 0.3158 0.1677 0.0632  0.0022  -0.0652 152 ASN A CA  
1315 C C   . ASN A 152 ? 0.3418 0.3888 0.2300 0.0598  -0.0020 -0.0666 152 ASN A C   
1316 O O   . ASN A 152 ? 0.3635 0.4007 0.2467 0.0620  -0.0090 -0.0775 152 ASN A O   
1317 C CB  . ASN A 152 ? 0.3064 0.3720 0.2021 0.0702  0.0078  -0.0733 152 ASN A CB  
1318 C CG  . ASN A 152 ? 0.5542 0.6191 0.4598 0.0754  0.0100  -0.0758 152 ASN A CG  
1319 O OD1 . ASN A 152 ? 0.6087 0.6535 0.5199 0.0765  0.0044  -0.0764 152 ASN A OD1 
1320 N ND2 . ASN A 152 ? 0.5794 0.6675 0.4868 0.0777  0.0177  -0.0769 152 ASN A ND2 
1321 N N   . LYS A 153 ? 0.2752 0.3334 0.1605 0.0547  0.0011  -0.0563 153 LYS A N   
1322 C CA  . LYS A 153 ? 0.3148 0.3768 0.1917 0.0516  -0.0033 -0.0570 153 LYS A CA  
1323 C C   . LYS A 153 ? 0.3578 0.4023 0.2371 0.0477  -0.0117 -0.0601 153 LYS A C   
1324 O O   . LYS A 153 ? 0.3784 0.4194 0.2506 0.0477  -0.0179 -0.0696 153 LYS A O   
1325 C CB  . LYS A 153 ? 0.3177 0.3901 0.1932 0.0472  -0.0004 -0.0433 153 LYS A CB  
1326 C CG  . LYS A 153 ? 0.3700 0.4499 0.2362 0.0449  -0.0051 -0.0432 153 LYS A CG  
1327 C CD  . LYS A 153 ? 0.3243 0.4134 0.1877 0.0425  -0.0032 -0.0295 153 LYS A CD  
1328 C CE  . LYS A 153 ? 0.2961 0.3918 0.1517 0.0407  -0.0096 -0.0290 153 LYS A CE  
1329 N NZ  . LYS A 153 ? 0.3856 0.4890 0.2359 0.0397  -0.0095 -0.0158 153 LYS A NZ  
1330 N N   . GLY A 154 ? 0.3210 0.3554 0.2097 0.0435  -0.0121 -0.0523 154 GLY A N   
1331 C CA  . GLY A 154 ? 0.3476 0.3655 0.2391 0.0380  -0.0191 -0.0543 154 GLY A CA  
1332 C C   . GLY A 154 ? 0.3520 0.3743 0.2425 0.0308  -0.0238 -0.0515 154 GLY A C   
1333 O O   . GLY A 154 ? 0.3382 0.3506 0.2326 0.0237  -0.0285 -0.0505 154 GLY A O   
1334 N N   . ARG A 155 ? 0.3303 0.3686 0.2157 0.0319  -0.0229 -0.0497 155 ARG A N   
1335 C CA  . ARG A 155 ? 0.3091 0.3543 0.1935 0.0262  -0.0284 -0.0486 155 ARG A CA  
1336 C C   . ARG A 155 ? 0.3628 0.4259 0.2414 0.0295  -0.0265 -0.0440 155 ARG A C   
1337 O O   . ARG A 155 ? 0.3794 0.4484 0.2526 0.0346  -0.0212 -0.0425 155 ARG A O   
1338 C CB  . ARG A 155 ? 0.3493 0.3853 0.2269 0.0225  -0.0365 -0.0599 155 ARG A CB  
1339 C CG  . ARG A 155 ? 0.3531 0.3911 0.2191 0.0294  -0.0368 -0.0706 155 ARG A CG  
1340 C CD  . ARG A 155 ? 0.4224 0.4500 0.2808 0.0260  -0.0462 -0.0827 155 ARG A CD  
1341 N NE  . ARG A 155 ? 0.4770 0.4803 0.3384 0.0226  -0.0513 -0.0867 155 ARG A NE  
1342 C CZ  . ARG A 155 ? 0.5085 0.4998 0.3706 0.0120  -0.0595 -0.0874 155 ARG A CZ  
1343 N NH1 . ARG A 155 ? 0.5854 0.5522 0.4481 0.0083  -0.0647 -0.0895 155 ARG A NH1 
1344 N NH2 . ARG A 155 ? 0.5345 0.5387 0.3960 0.0046  -0.0629 -0.0856 155 ARG A NH2 
1345 N N   . ASN A 156 ? 0.2957 0.3683 0.1749 0.0257  -0.0315 -0.0417 156 ASN A N   
1346 C CA  . ASN A 156 ? 0.2837 0.3720 0.1562 0.0285  -0.0325 -0.0368 156 ASN A CA  
1347 C C   . ASN A 156 ? 0.3201 0.4116 0.1946 0.0329  -0.0267 -0.0253 156 ASN A C   
1348 O O   . ASN A 156 ? 0.3568 0.4547 0.2213 0.0359  -0.0243 -0.0218 156 ASN A O   
1349 C CB  . ASN A 156 ? 0.3667 0.4600 0.2244 0.0306  -0.0340 -0.0452 156 ASN A CB  
1350 C CG  . ASN A 156 ? 0.5148 0.6011 0.3695 0.0265  -0.0408 -0.0579 156 ASN A CG  
1351 O OD1 . ASN A 156 ? 0.5344 0.6181 0.3960 0.0200  -0.0463 -0.0583 156 ASN A OD1 
1352 N ND2 . ASN A 156 ? 0.5152 0.5988 0.3593 0.0300  -0.0409 -0.0688 156 ASN A ND2 
1353 N N   . TYR A 157 ? 0.2376 0.3246 0.1244 0.0323  -0.0250 -0.0194 157 TYR A N   
1354 C CA  . TYR A 157 ? 0.2492 0.3358 0.1388 0.0361  -0.0210 -0.0090 157 TYR A CA  
1355 C C   . TYR A 157 ? 0.2971 0.3933 0.1860 0.0387  -0.0262 -0.0020 157 TYR A C   
1356 O O   . TYR A 157 ? 0.2994 0.4042 0.1920 0.0374  -0.0323 -0.0049 157 TYR A O   
1357 C CB  . TYR A 157 ? 0.2345 0.3121 0.1369 0.0353  -0.0176 -0.0070 157 TYR A CB  
1358 C CG  . TYR A 157 ? 0.2531 0.3199 0.1558 0.0342  -0.0131 -0.0123 157 TYR A CG  
1359 C CD1 . TYR A 157 ? 0.2229 0.2877 0.1215 0.0370  -0.0074 -0.0104 157 TYR A CD1 
1360 C CD2 . TYR A 157 ? 0.2622 0.3213 0.1689 0.0299  -0.0154 -0.0192 157 TYR A CD2 
1361 C CE1 . TYR A 157 ? 0.2129 0.2700 0.1129 0.0376  -0.0042 -0.0163 157 TYR A CE1 
1362 C CE2 . TYR A 157 ? 0.2829 0.3303 0.1894 0.0303  -0.0131 -0.0240 157 TYR A CE2 
1363 C CZ  . TYR A 157 ? 0.2597 0.3071 0.1636 0.0351  -0.0076 -0.0232 157 TYR A CZ  
1364 O OH  . TYR A 157 ? 0.2759 0.3137 0.1808 0.0369  -0.0060 -0.0288 157 TYR A OH  
1365 N N   . THR A 158 ? 0.2491 0.3436 0.1331 0.0421  -0.0248 0.0074  158 THR A N   
1366 C CA  . THR A 158 ? 0.2442 0.3436 0.1266 0.0462  -0.0311 0.0153  158 THR A CA  
1367 C C   . THR A 158 ? 0.2358 0.3285 0.1303 0.0501  -0.0311 0.0208  158 THR A C   
1368 O O   . THR A 158 ? 0.2421 0.3257 0.1428 0.0489  -0.0252 0.0208  158 THR A O   
1369 C CB  . THR A 158 ? 0.2988 0.3982 0.1646 0.0468  -0.0315 0.0235  158 THR A CB  
1370 O OG1 . THR A 158 ? 0.2661 0.3555 0.1307 0.0454  -0.0247 0.0292  158 THR A OG1 
1371 C CG2 . THR A 158 ? 0.2740 0.3828 0.1267 0.0437  -0.0313 0.0169  158 THR A CG2 
1372 N N   . GLN A 159 ? 0.2413 0.3388 0.1386 0.0556  -0.0386 0.0251  159 GLN A N   
1373 C CA  . GLN A 159 ? 0.2374 0.3283 0.1449 0.0614  -0.0401 0.0294  159 GLN A CA  
1374 C C   . GLN A 159 ? 0.2689 0.3428 0.1694 0.0613  -0.0363 0.0382  159 GLN A C   
1375 O O   . GLN A 159 ? 0.2449 0.3098 0.1541 0.0625  -0.0330 0.0387  159 GLN A O   
1376 C CB  . GLN A 159 ? 0.2471 0.3462 0.1570 0.0695  -0.0505 0.0318  159 GLN A CB  
1377 C CG  . GLN A 159 ? 0.2916 0.3838 0.2114 0.0781  -0.0540 0.0349  159 GLN A CG  
1378 C CD  . GLN A 159 ? 0.3179 0.4192 0.2559 0.0783  -0.0502 0.0261  159 GLN A CD  
1379 O OE1 . GLN A 159 ? 0.2799 0.3970 0.2245 0.0733  -0.0486 0.0184  159 GLN A OE1 
1380 N NE2 . GLN A 159 ? 0.2936 0.3846 0.2385 0.0832  -0.0489 0.0274  159 GLN A NE2 
1381 N N   . GLU A 160 ? 0.3009 0.3716 0.1851 0.0585  -0.0366 0.0449  160 GLU A N   
1382 C CA  . GLU A 160 ? 0.2768 0.3334 0.1532 0.0558  -0.0331 0.0542  160 GLU A CA  
1383 C C   . GLU A 160 ? 0.2644 0.3186 0.1457 0.0504  -0.0228 0.0495  160 GLU A C   
1384 O O   . GLU A 160 ? 0.2675 0.3101 0.1518 0.0494  -0.0199 0.0541  160 GLU A O   
1385 C CB  . GLU A 160 ? 0.2876 0.3454 0.1441 0.0520  -0.0353 0.0627  160 GLU A CB  
1386 C CG  . GLU A 160 ? 0.3500 0.4049 0.1993 0.0577  -0.0471 0.0707  160 GLU A CG  
1387 C CD  . GLU A 160 ? 0.5029 0.5748 0.3489 0.0597  -0.0523 0.0649  160 GLU A CD  
1388 O OE1 . GLU A 160 ? 0.5909 0.6630 0.4238 0.0616  -0.0609 0.0728  160 GLU A OE1 
1389 O OE2 . GLU A 160 ? 0.4808 0.5648 0.3364 0.0588  -0.0488 0.0531  160 GLU A OE2 
1390 N N   . GLU A 161 ? 0.2435 0.3075 0.1251 0.0471  -0.0181 0.0402  161 GLU A N   
1391 C CA  . GLU A 161 ? 0.2314 0.2928 0.1189 0.0438  -0.0099 0.0347  161 GLU A CA  
1392 C C   . GLU A 161 ? 0.2224 0.2771 0.1254 0.0459  -0.0091 0.0319  161 GLU A C   
1393 O O   . GLU A 161 ? 0.2228 0.2698 0.1302 0.0444  -0.0043 0.0332  161 GLU A O   
1394 C CB  . GLU A 161 ? 0.2480 0.3185 0.1324 0.0417  -0.0076 0.0243  161 GLU A CB  
1395 C CG  . GLU A 161 ? 0.2493 0.3286 0.1181 0.0393  -0.0056 0.0251  161 GLU A CG  
1396 C CD  . GLU A 161 ? 0.2967 0.3848 0.1615 0.0391  -0.0058 0.0131  161 GLU A CD  
1397 O OE1 . GLU A 161 ? 0.2740 0.3604 0.1463 0.0399  -0.0096 0.0061  161 GLU A OE1 
1398 O OE2 . GLU A 161 ? 0.3065 0.4036 0.1604 0.0378  -0.0023 0.0102  161 GLU A OE2 
1399 N N   . LYS A 162 ? 0.2135 0.2733 0.1247 0.0486  -0.0138 0.0277  162 LYS A N   
1400 C CA  . LYS A 162 ? 0.2024 0.2598 0.1274 0.0501  -0.0131 0.0248  162 LYS A CA  
1401 C C   . LYS A 162 ? 0.2302 0.2770 0.1579 0.0542  -0.0140 0.0317  162 LYS A C   
1402 O O   . LYS A 162 ? 0.2306 0.2710 0.1657 0.0536  -0.0101 0.0306  162 LYS A O   
1403 C CB  . LYS A 162 ? 0.2093 0.2792 0.1419 0.0518  -0.0183 0.0198  162 LYS A CB  
1404 C CG  . LYS A 162 ? 0.2352 0.3080 0.1818 0.0527  -0.0173 0.0161  162 LYS A CG  
1405 C CD  . LYS A 162 ? 0.2461 0.3367 0.2004 0.0528  -0.0220 0.0107  162 LYS A CD  
1406 C CE  . LYS A 162 ? 0.2484 0.3466 0.2025 0.0609  -0.0297 0.0136  162 LYS A CE  
1407 N NZ  . LYS A 162 ? 0.2313 0.3513 0.1958 0.0617  -0.0342 0.0074  162 LYS A NZ  
1408 N N   . GLU A 163 ? 0.2386 0.2821 0.1595 0.0583  -0.0201 0.0389  163 GLU A N   
1409 C CA  . GLU A 163 ? 0.2579 0.2871 0.1793 0.0622  -0.0230 0.0457  163 GLU A CA  
1410 C C   . GLU A 163 ? 0.2587 0.2764 0.1743 0.0559  -0.0170 0.0510  163 GLU A C   
1411 O O   . GLU A 163 ? 0.2406 0.2465 0.1609 0.0567  -0.0164 0.0529  163 GLU A O   
1412 C CB  . GLU A 163 ? 0.2892 0.3146 0.2022 0.0678  -0.0327 0.0531  163 GLU A CB  
1413 C CG  . GLU A 163 ? 0.2843 0.3198 0.2076 0.0772  -0.0403 0.0477  163 GLU A CG  
1414 C CD  . GLU A 163 ? 0.4209 0.4565 0.3352 0.0831  -0.0510 0.0537  163 GLU A CD  
1415 O OE1 . GLU A 163 ? 0.4557 0.4810 0.3539 0.0792  -0.0530 0.0637  163 GLU A OE1 
1416 O OE2 . GLU A 163 ? 0.4134 0.4609 0.3367 0.0913  -0.0577 0.0486  163 GLU A OE2 
1417 N N   . TYR A 164 ? 0.2659 0.2885 0.1712 0.0495  -0.0126 0.0527  164 TYR A N   
1418 C CA  . TYR A 164 ? 0.2625 0.2800 0.1640 0.0429  -0.0061 0.0564  164 TYR A CA  
1419 C C   . TYR A 164 ? 0.2467 0.2636 0.1605 0.0422  -0.0002 0.0491  164 TYR A C   
1420 O O   . TYR A 164 ? 0.2532 0.2609 0.1699 0.0400  0.0020  0.0522  164 TYR A O   
1421 C CB  . TYR A 164 ? 0.2778 0.3069 0.1674 0.0374  -0.0020 0.0566  164 TYR A CB  
1422 C CG  . TYR A 164 ? 0.2760 0.3054 0.1608 0.0299  0.0047  0.0608  164 TYR A CG  
1423 C CD1 . TYR A 164 ? 0.3492 0.3828 0.2429 0.0283  0.0117  0.0537  164 TYR A CD1 
1424 C CD2 . TYR A 164 ? 0.3332 0.3604 0.2041 0.0238  0.0035  0.0721  164 TYR A CD2 
1425 C CE1 . TYR A 164 ? 0.3220 0.3604 0.2129 0.0216  0.0177  0.0566  164 TYR A CE1 
1426 C CE2 . TYR A 164 ? 0.3776 0.4093 0.2446 0.0151  0.0100  0.0759  164 TYR A CE2 
1427 C CZ  . TYR A 164 ? 0.3995 0.4381 0.2774 0.0145  0.0173  0.0676  164 TYR A CZ  
1428 O OH  . TYR A 164 ? 0.4576 0.5045 0.3328 0.0059  0.0237  0.0708  164 TYR A OH  
1429 N N   . VAL A 165 ? 0.2377 0.2633 0.1582 0.0435  0.0015  0.0398  165 VAL A N   
1430 C CA  . VAL A 165 ? 0.2038 0.2278 0.1346 0.0426  0.0057  0.0337  165 VAL A CA  
1431 C C   . VAL A 165 ? 0.2146 0.2305 0.1540 0.0459  0.0036  0.0348  165 VAL A C   
1432 O O   . VAL A 165 ? 0.2188 0.2282 0.1627 0.0442  0.0068  0.0349  165 VAL A O   
1433 C CB  . VAL A 165 ? 0.2105 0.2422 0.1446 0.0424  0.0058  0.0250  165 VAL A CB  
1434 C CG1 . VAL A 165 ? 0.2279 0.2560 0.1712 0.0410  0.0087  0.0202  165 VAL A CG1 
1435 C CG2 . VAL A 165 ? 0.2375 0.2755 0.1630 0.0403  0.0077  0.0218  165 VAL A CG2 
1436 N N   . LEU A 166 ? 0.2345 0.2523 0.1767 0.0513  -0.0022 0.0347  166 LEU A N   
1437 C CA  . LEU A 166 ? 0.2397 0.2519 0.1904 0.0562  -0.0048 0.0338  166 LEU A CA  
1438 C C   . LEU A 166 ? 0.2658 0.2618 0.2127 0.0557  -0.0056 0.0406  166 LEU A C   
1439 O O   . LEU A 166 ? 0.2315 0.2210 0.1846 0.0559  -0.0039 0.0386  166 LEU A O   
1440 C CB  . LEU A 166 ? 0.2455 0.2646 0.1995 0.0637  -0.0119 0.0322  166 LEU A CB  
1441 C CG  . LEU A 166 ? 0.2690 0.3058 0.2310 0.0632  -0.0111 0.0241  166 LEU A CG  
1442 C CD1 . LEU A 166 ? 0.2825 0.3309 0.2465 0.0696  -0.0184 0.0228  166 LEU A CD1 
1443 C CD2 . LEU A 166 ? 0.2740 0.3141 0.2465 0.0628  -0.0077 0.0182  166 LEU A CD2 
1444 N N   A ASN A 167 ? 0.2513 0.2406 0.1870 0.0538  -0.0084 0.0491  167 ASN A N   
1445 N N   B ASN A 167 ? 0.2454 0.2346 0.1811 0.0538  -0.0084 0.0491  167 ASN A N   
1446 C CA  A ASN A 167 ? 0.2740 0.2461 0.2044 0.0511  -0.0103 0.0571  167 ASN A CA  
1447 C CA  B ASN A 167 ? 0.2715 0.2435 0.2021 0.0512  -0.0103 0.0570  167 ASN A CA  
1448 C C   A ASN A 167 ? 0.2449 0.2163 0.1774 0.0434  -0.0026 0.0565  167 ASN A C   
1449 C C   B ASN A 167 ? 0.2445 0.2160 0.1773 0.0434  -0.0026 0.0563  167 ASN A C   
1450 O O   A ASN A 167 ? 0.2549 0.2145 0.1908 0.0425  -0.0032 0.0575  167 ASN A O   
1451 O O   B ASN A 167 ? 0.2634 0.2233 0.1998 0.0426  -0.0031 0.0571  167 ASN A O   
1452 C CB  A ASN A 167 ? 0.2970 0.2637 0.2126 0.0479  -0.0146 0.0676  167 ASN A CB  
1453 C CB  B ASN A 167 ? 0.2928 0.2588 0.2087 0.0481  -0.0148 0.0676  167 ASN A CB  
1454 C CG  A ASN A 167 ? 0.3371 0.2995 0.2501 0.0568  -0.0248 0.0698  167 ASN A CG  
1455 C CG  B ASN A 167 ? 0.4011 0.3475 0.3099 0.0427  -0.0175 0.0773  167 ASN A CG  
1456 O OD1 A ASN A 167 ? 0.3550 0.3127 0.2770 0.0657  -0.0300 0.0651  167 ASN A OD1 
1457 O OD1 B ASN A 167 ? 0.4764 0.4057 0.3876 0.0480  -0.0246 0.0785  167 ASN A OD1 
1458 N ND2 A ASN A 167 ? 0.3922 0.3581 0.2930 0.0550  -0.0281 0.0762  167 ASN A ND2 
1459 N ND2 B ASN A 167 ? 0.6015 0.5511 0.5016 0.0318  -0.0121 0.0835  167 ASN A ND2 
1460 N N   . LYS A 168 ? 0.2196 0.2042 0.1505 0.0385  0.0039  0.0539  168 LYS A N   
1461 C CA  . LYS A 168 ? 0.2346 0.2217 0.1690 0.0327  0.0107  0.0519  168 LYS A CA  
1462 C C   . LYS A 168 ? 0.2396 0.2251 0.1858 0.0357  0.0120  0.0446  168 LYS A C   
1463 O O   . LYS A 168 ? 0.2210 0.2016 0.1709 0.0325  0.0143  0.0446  168 LYS A O   
1464 C CB  . LYS A 168 ? 0.2148 0.2173 0.1462 0.0299  0.0162  0.0480  168 LYS A CB  
1465 C CG  . LYS A 168 ? 0.2609 0.2697 0.1799 0.0252  0.0168  0.0544  168 LYS A CG  
1466 C CD  . LYS A 168 ? 0.3946 0.3951 0.3077 0.0178  0.0166  0.0646  168 LYS A CD  
1467 C CE  . LYS A 168 ? 0.4260 0.4356 0.3431 0.0114  0.0237  0.0626  168 LYS A CE  
1468 N NZ  . LYS A 168 ? 0.5253 0.5339 0.4329 0.0007  0.0244  0.0734  168 LYS A NZ  
1469 N N   . TYR A 169 ? 0.2241 0.2150 0.1756 0.0409  0.0104  0.0383  169 TYR A N   
1470 C CA  . TYR A 169 ? 0.1949 0.1861 0.1558 0.0426  0.0116  0.0320  169 TYR A CA  
1471 C C   . TYR A 169 ? 0.2385 0.2184 0.2028 0.0455  0.0084  0.0332  169 TYR A C   
1472 O O   . TYR A 169 ? 0.2141 0.1907 0.1831 0.0438  0.0106  0.0306  169 TYR A O   
1473 C CB  . TYR A 169 ? 0.1958 0.1970 0.1605 0.0457  0.0101  0.0263  169 TYR A CB  
1474 C CG  . TYR A 169 ? 0.1615 0.1703 0.1249 0.0422  0.0129  0.0225  169 TYR A CG  
1475 C CD1 . TYR A 169 ? 0.1819 0.1908 0.1403 0.0391  0.0160  0.0233  169 TYR A CD1 
1476 C CD2 . TYR A 169 ? 0.2075 0.2237 0.1745 0.0417  0.0120  0.0174  169 TYR A CD2 
1477 C CE1 . TYR A 169 ? 0.1870 0.2005 0.1440 0.0376  0.0171  0.0183  169 TYR A CE1 
1478 C CE2 . TYR A 169 ? 0.1497 0.1684 0.1142 0.0381  0.0128  0.0140  169 TYR A CE2 
1479 C CZ  . TYR A 169 ? 0.1655 0.1814 0.1249 0.0371  0.0149  0.0140  169 TYR A CZ  
1480 O OH  . TYR A 169 ? 0.1989 0.2149 0.1557 0.0352  0.0143  0.0092  169 TYR A OH  
1481 N N   . PHE A 170 ? 0.2344 0.2074 0.1959 0.0503  0.0023  0.0366  170 PHE A N   
1482 C CA  . PHE A 170 ? 0.2179 0.1773 0.1821 0.0544  -0.0022 0.0364  170 PHE A CA  
1483 C C   . PHE A 170 ? 0.2509 0.1962 0.2104 0.0474  -0.0015 0.0426  170 PHE A C   
1484 O O   . PHE A 170 ? 0.2543 0.1895 0.2174 0.0480  -0.0030 0.0403  170 PHE A O   
1485 C CB  . PHE A 170 ? 0.2663 0.2200 0.2286 0.0631  -0.0107 0.0378  170 PHE A CB  
1486 C CG  . PHE A 170 ? 0.2782 0.2464 0.2499 0.0714  -0.0121 0.0286  170 PHE A CG  
1487 C CD1 . PHE A 170 ? 0.2764 0.2444 0.2563 0.0770  -0.0132 0.0209  170 PHE A CD1 
1488 C CD2 . PHE A 170 ? 0.2913 0.2759 0.2638 0.0725  -0.0119 0.0268  170 PHE A CD2 
1489 C CE1 . PHE A 170 ? 0.2623 0.2486 0.2511 0.0834  -0.0134 0.0119  170 PHE A CE1 
1490 C CE2 . PHE A 170 ? 0.2949 0.2965 0.2767 0.0783  -0.0128 0.0184  170 PHE A CE2 
1491 C CZ  . PHE A 170 ? 0.2466 0.2505 0.2367 0.0835  -0.0131 0.0111  170 PHE A CZ  
1492 N N   . GLU A 171 ? 0.2523 0.1985 0.2036 0.0400  0.0009  0.0500  171 GLU A N   
1493 C CA  . GLU A 171 ? 0.2567 0.1947 0.2046 0.0310  0.0026  0.0557  171 GLU A CA  
1494 C C   . GLU A 171 ? 0.2574 0.2024 0.2138 0.0281  0.0085  0.0494  171 GLU A C   
1495 O O   . GLU A 171 ? 0.2991 0.2345 0.2572 0.0241  0.0077  0.0503  171 GLU A O   
1496 C CB  . GLU A 171 ? 0.2834 0.2281 0.2214 0.0230  0.0055  0.0635  171 GLU A CB  
1497 C CG  . GLU A 171 ? 0.3221 0.2555 0.2483 0.0228  -0.0015 0.0731  171 GLU A CG  
1498 C CD  . GLU A 171 ? 0.4445 0.3891 0.3599 0.0141  0.0024  0.0801  171 GLU A CD  
1499 O OE1 . GLU A 171 ? 0.4700 0.4321 0.3888 0.0095  0.0106  0.0761  171 GLU A OE1 
1500 O OE2 . GLU A 171 ? 0.7018 0.6386 0.6051 0.0122  -0.0031 0.0893  171 GLU A OE2 
1501 N N   . ILE A 172 ? 0.2109 0.1712 0.1721 0.0299  0.0133  0.0430  172 ILE A N   
1502 C CA  . ILE A 172 ? 0.2119 0.1779 0.1803 0.0281  0.0175  0.0373  172 ILE A CA  
1503 C C   . ILE A 172 ? 0.2358 0.1941 0.2099 0.0321  0.0147  0.0325  172 ILE A C   
1504 O O   . ILE A 172 ? 0.2167 0.1715 0.1941 0.0289  0.0156  0.0309  172 ILE A O   
1505 C CB  . ILE A 172 ? 0.2198 0.1995 0.1902 0.0298  0.0210  0.0320  172 ILE A CB  
1506 C CG1 . ILE A 172 ? 0.2554 0.2445 0.2211 0.0261  0.0244  0.0343  172 ILE A CG1 
1507 C CG2 . ILE A 172 ? 0.2728 0.2552 0.2498 0.0298  0.0228  0.0262  172 ILE A CG2 
1508 C CD1 . ILE A 172 ? 0.3027 0.2966 0.2710 0.0206  0.0281  0.0347  172 ILE A CD1 
1509 N N   . ILE A 173 ? 0.2025 0.1601 0.1779 0.0392  0.0112  0.0293  173 ILE A N   
1510 C CA  . ILE A 173 ? 0.1966 0.1508 0.1775 0.0440  0.0089  0.0230  173 ILE A CA  
1511 C C   . ILE A 173 ? 0.2238 0.1602 0.2029 0.0433  0.0045  0.0254  173 ILE A C   
1512 O O   . ILE A 173 ? 0.2430 0.1755 0.2257 0.0429  0.0044  0.0207  173 ILE A O   
1513 C CB  . ILE A 173 ? 0.2167 0.1780 0.2002 0.0522  0.0060  0.0184  173 ILE A CB  
1514 C CG1 . ILE A 173 ? 0.1887 0.1669 0.1739 0.0505  0.0101  0.0157  173 ILE A CG1 
1515 C CG2 . ILE A 173 ? 0.2875 0.2474 0.2765 0.0583  0.0034  0.0107  173 ILE A CG2 
1516 C CD1 . ILE A 173 ? 0.2397 0.2292 0.2281 0.0566  0.0076  0.0115  173 ILE A CD1 
1517 N N   . LYS A 174 ? 0.2178 0.1417 0.1901 0.0422  0.0001  0.0330  174 LYS A N   
1518 C CA  . LYS A 174 ? 0.2250 0.1275 0.1937 0.0404  -0.0060 0.0364  174 LYS A CA  
1519 C C   . LYS A 174 ? 0.2622 0.1624 0.2313 0.0297  -0.0026 0.0386  174 LYS A C   
1520 O O   . LYS A 174 ? 0.3101 0.1936 0.2784 0.0276  -0.0073 0.0386  174 LYS A O   
1521 C CB  . LYS A 174 ? 0.3150 0.2034 0.2740 0.0393  -0.0122 0.0463  174 LYS A CB  
1522 C CG  . LYS A 174 ? 0.3231 0.2100 0.2818 0.0512  -0.0184 0.0440  174 LYS A CG  
1523 C CD  . LYS A 174 ? 0.4427 0.3162 0.3897 0.0491  -0.0248 0.0554  174 LYS A CD  
1524 C CE  . LYS A 174 ? 0.6384 0.5214 0.5857 0.0592  -0.0282 0.0536  174 LYS A CE  
1525 N NZ  . LYS A 174 ? 0.6882 0.5771 0.6461 0.0724  -0.0310 0.0416  174 LYS A NZ  
1526 N N   . LYS A 175 ? 0.2270 0.1436 0.1976 0.0234  0.0047  0.0399  175 LYS A N   
1527 C CA  . LYS A 175 ? 0.2543 0.1736 0.2270 0.0139  0.0080  0.0412  175 LYS A CA  
1528 C C   . LYS A 175 ? 0.2279 0.1577 0.2087 0.0159  0.0115  0.0327  175 LYS A C   
1529 O O   . LYS A 175 ? 0.2282 0.1634 0.2121 0.0092  0.0140  0.0326  175 LYS A O   
1530 C CB  . LYS A 175 ? 0.3530 0.2852 0.3223 0.0060  0.0131  0.0476  175 LYS A CB  
1531 C CG  . LYS A 175 ? 0.4658 0.3919 0.4253 0.0047  0.0104  0.0560  175 LYS A CG  
1532 C CD  . LYS A 175 ? 0.5507 0.4958 0.5071 -0.0006 0.0165  0.0594  175 LYS A CD  
1533 C CE  . LYS A 175 ? 0.5904 0.5397 0.5443 -0.0137 0.0190  0.0658  175 LYS A CE  
1534 N NZ  . LYS A 175 ? 0.6269 0.5858 0.5711 -0.0201 0.0214  0.0736  175 LYS A NZ  
1535 N N   . THR A 176 ? 0.2177 0.1514 0.2016 0.0242  0.0112  0.0258  176 THR A N   
1536 C CA  . THR A 176 ? 0.2207 0.1659 0.2098 0.0249  0.0146  0.0194  176 THR A CA  
1537 C C   . THR A 176 ? 0.2171 0.1560 0.2090 0.0230  0.0126  0.0152  176 THR A C   
1538 O O   . THR A 176 ? 0.2097 0.1550 0.2044 0.0180  0.0148  0.0145  176 THR A O   
1539 C CB  . THR A 176 ? 0.2447 0.1981 0.2349 0.0318  0.0152  0.0145  176 THR A CB  
1540 O OG1 . THR A 176 ? 0.2293 0.1905 0.2172 0.0319  0.0173  0.0178  176 THR A OG1 
1541 C CG2 . THR A 176 ? 0.2278 0.1900 0.2211 0.0312  0.0174  0.0090  176 THR A CG2 
1542 N N   . LEU A 177 ? 0.2142 0.1406 0.2054 0.0273  0.0077  0.0116  177 LEU A N   
1543 C CA  . LEU A 177 ? 0.2211 0.1411 0.2141 0.0254  0.0054  0.0064  177 LEU A CA  
1544 C C   . LEU A 177 ? 0.2515 0.1642 0.2438 0.0151  0.0045  0.0120  177 LEU A C   
1545 O O   . LEU A 177 ? 0.2594 0.1750 0.2547 0.0106  0.0048  0.0089  177 LEU A O   
1546 C CB  . LEU A 177 ? 0.2378 0.1446 0.2299 0.0333  -0.0006 0.0000  177 LEU A CB  
1547 C CG  . LEU A 177 ? 0.2658 0.1857 0.2602 0.0428  0.0008  -0.0077 177 LEU A CG  
1548 C CD1 . LEU A 177 ? 0.2424 0.1522 0.2371 0.0526  -0.0056 -0.0159 177 LEU A CD1 
1549 C CD2 . LEU A 177 ? 0.2768 0.2136 0.2734 0.0406  0.0056  -0.0125 177 LEU A CD2 
1550 N N   . SER A 178 ? 0.2491 0.1545 0.2373 0.0104  0.0035  0.0206  178 SER A N   
1551 C CA  . SER A 178 ? 0.2510 0.1529 0.2382 -0.0017 0.0033  0.0269  178 SER A CA  
1552 C C   . SER A 178 ? 0.2485 0.1725 0.2415 -0.0069 0.0096  0.0265  178 SER A C   
1553 O O   . SER A 178 ? 0.2523 0.1789 0.2483 -0.0153 0.0095  0.0268  178 SER A O   
1554 C CB  . SER A 178 ? 0.2888 0.1814 0.2686 -0.0067 0.0014  0.0372  178 SER A CB  
1555 O OG  . SER A 178 ? 0.3875 0.2542 0.3616 -0.0039 -0.0072 0.0381  178 SER A OG  
1556 N N   . ILE A 179 ? 0.2172 0.1570 0.2119 -0.0017 0.0144  0.0254  179 ILE A N   
1557 C CA  . ILE A 179 ? 0.2183 0.1772 0.2185 -0.0050 0.0189  0.0242  179 ILE A CA  
1558 C C   . ILE A 179 ? 0.1834 0.1460 0.1886 -0.0031 0.0178  0.0172  179 ILE A C   
1559 O O   . ILE A 179 ? 0.1916 0.1656 0.2021 -0.0076 0.0189  0.0161  179 ILE A O   
1560 C CB  . ILE A 179 ? 0.2304 0.2028 0.2302 -0.0002 0.0230  0.0246  179 ILE A CB  
1561 C CG1 . ILE A 179 ? 0.2635 0.2552 0.2688 -0.0039 0.0267  0.0238  179 ILE A CG1 
1562 C CG2 . ILE A 179 ? 0.2319 0.2049 0.2318 0.0086  0.0227  0.0192  179 ILE A CG2 
1563 C CD1 . ILE A 179 ? 0.3111 0.3155 0.3153 -0.0002 0.0302  0.0239  179 ILE A CD1 
1564 N N   . TYR A 180 ? 0.2242 0.1794 0.2278 0.0034  0.0155  0.0121  180 TYR A N   
1565 C CA  . TYR A 180 ? 0.2106 0.1688 0.2168 0.0038  0.0141  0.0061  180 TYR A CA  
1566 C C   . TYR A 180 ? 0.2249 0.1754 0.2327 -0.0034 0.0106  0.0053  180 TYR A C   
1567 O O   . TYR A 180 ? 0.2150 0.1737 0.2269 -0.0072 0.0101  0.0028  180 TYR A O   
1568 C CB  . TYR A 180 ? 0.1930 0.1477 0.1962 0.0110  0.0129  0.0005  180 TYR A CB  
1569 C CG  . TYR A 180 ? 0.1678 0.1322 0.1697 0.0155  0.0157  0.0006  180 TYR A CG  
1570 C CD1 . TYR A 180 ? 0.1858 0.1596 0.1883 0.0152  0.0162  -0.0006 180 TYR A CD1 
1571 C CD2 . TYR A 180 ? 0.1849 0.1481 0.1845 0.0196  0.0168  0.0025  180 TYR A CD2 
1572 C CE1 . TYR A 180 ? 0.1918 0.1710 0.1918 0.0180  0.0175  0.0002  180 TYR A CE1 
1573 C CE2 . TYR A 180 ? 0.1788 0.1501 0.1770 0.0222  0.0187  0.0027  180 TYR A CE2 
1574 C CZ  . TYR A 180 ? 0.1767 0.1548 0.1746 0.0209  0.0190  0.0018  180 TYR A CZ  
1575 O OH  . TYR A 180 ? 0.1753 0.1579 0.1704 0.0222  0.0196  0.0026  180 TYR A OH  
1576 N N   . ARG A 181 ? 0.2268 0.1602 0.2309 -0.0056 0.0072  0.0075  181 ARG A N   
1577 C CA  . ARG A 181 ? 0.2223 0.1452 0.2269 -0.0140 0.0029  0.0073  181 ARG A CA  
1578 C C   . ARG A 181 ? 0.2219 0.1576 0.2308 -0.0251 0.0054  0.0129  181 ARG A C   
1579 O O   . ARG A 181 ? 0.2570 0.1966 0.2699 -0.0322 0.0036  0.0107  181 ARG A O   
1580 C CB  . ARG A 181 ? 0.2717 0.1702 0.2700 -0.0142 -0.0027 0.0098  181 ARG A CB  
1581 C CG  . ARG A 181 ? 0.3334 0.2161 0.3305 -0.0242 -0.0087 0.0102  181 ARG A CG  
1582 C CD  . ARG A 181 ? 0.3964 0.2504 0.3859 -0.0221 -0.0162 0.0122  181 ARG A CD  
1583 N NE  . ARG A 181 ? 0.3197 0.1687 0.3081 -0.0070 -0.0181 0.0037  181 ARG A NE  
1584 C CZ  . ARG A 181 ? 0.3299 0.1757 0.3154 0.0018  -0.0182 0.0058  181 ARG A CZ  
1585 N NH1 . ARG A 181 ? 0.3939 0.2387 0.3760 -0.0031 -0.0169 0.0167  181 ARG A NH1 
1586 N NH2 . ARG A 181 ? 0.3427 0.1888 0.3290 0.0152  -0.0196 -0.0033 181 ARG A NH2 
1587 N N   . GLU A 182 ? 0.2369 0.1818 0.2453 -0.0266 0.0097  0.0194  182 GLU A N   
1588 C CA  . GLU A 182 ? 0.2583 0.2202 0.2711 -0.0368 0.0130  0.0240  182 GLU A CA  
1589 C C   . GLU A 182 ? 0.2145 0.1992 0.2363 -0.0348 0.0155  0.0184  182 GLU A C   
1590 O O   . GLU A 182 ? 0.2134 0.2094 0.2411 -0.0436 0.0151  0.0181  182 GLU A O   
1591 C CB  . GLU A 182 ? 0.3304 0.2987 0.3394 -0.0368 0.0172  0.0307  182 GLU A CB  
1592 C CG  . GLU A 182 ? 0.4550 0.4498 0.4701 -0.0422 0.0226  0.0318  182 GLU A CG  
1593 C CD  . GLU A 182 ? 0.6352 0.6392 0.6464 -0.0379 0.0271  0.0350  182 GLU A CD  
1594 O OE1 . GLU A 182 ? 0.6316 0.6197 0.6348 -0.0342 0.0256  0.0385  182 GLU A OE1 
1595 O OE2 . GLU A 182 ? 0.6570 0.6861 0.6740 -0.0371 0.0319  0.0325  182 GLU A OE2 
1596 N N   . ILE A 183 ? 0.2100 0.2017 0.2327 -0.0238 0.0172  0.0142  183 ILE A N   
1597 C CA  . ILE A 183 ? 0.2287 0.2393 0.2588 -0.0212 0.0177  0.0095  183 ILE A CA  
1598 C C   . ILE A 183 ? 0.1794 0.1862 0.2116 -0.0232 0.0131  0.0046  183 ILE A C   
1599 O O   . ILE A 183 ? 0.2048 0.2272 0.2443 -0.0254 0.0120  0.0017  183 ILE A O   
1600 C CB  . ILE A 183 ? 0.2178 0.2332 0.2466 -0.0101 0.0192  0.0071  183 ILE A CB  
1601 C CG1 . ILE A 183 ? 0.2105 0.2108 0.2328 -0.0038 0.0168  0.0048  183 ILE A CG1 
1602 C CG2 . ILE A 183 ? 0.2366 0.2575 0.2635 -0.0087 0.0234  0.0109  183 ILE A CG2 
1603 C CD1 . ILE A 183 ? 0.2153 0.2191 0.2385 -0.0004 0.0136  -0.0001 183 ILE A CD1 
1604 N N   . LYS A 184 ? 0.2053 0.1927 0.2314 -0.0221 0.0099  0.0027  184 LYS A N   
1605 C CA  . LYS A 184 ? 0.1977 0.1812 0.2245 -0.0243 0.0053  -0.0029 184 LYS A CA  
1606 C C   . LYS A 184 ? 0.2148 0.1986 0.2457 -0.0368 0.0029  -0.0014 184 LYS A C   
1607 O O   . LYS A 184 ? 0.2251 0.2211 0.2619 -0.0409 0.0008  -0.0048 184 LYS A O   
1608 C CB  . LYS A 184 ? 0.2307 0.1956 0.2499 -0.0189 0.0026  -0.0069 184 LYS A CB  
1609 C CG  . LYS A 184 ? 0.2774 0.2382 0.2957 -0.0204 -0.0022 -0.0142 184 LYS A CG  
1610 C CD  . LYS A 184 ? 0.2924 0.2367 0.3038 -0.0143 -0.0046 -0.0198 184 LYS A CD  
1611 C CE  . LYS A 184 ? 0.3616 0.3008 0.3713 -0.0164 -0.0098 -0.0282 184 LYS A CE  
1612 N NZ  . LYS A 184 ? 0.4562 0.3810 0.4671 -0.0259 -0.0147 -0.0278 184 LYS A NZ  
1613 N N   . GLU A 185 ? 0.2412 0.2119 0.2686 -0.0437 0.0027  0.0042  185 GLU A N   
1614 C CA  . GLU A 185 ? 0.2779 0.2465 0.3076 -0.0583 -0.0001 0.0070  185 GLU A CA  
1615 C C   . GLU A 185 ? 0.2871 0.2850 0.3266 -0.0657 0.0037  0.0091  185 GLU A C   
1616 O O   . GLU A 185 ? 0.2832 0.2884 0.3279 -0.0773 0.0012  0.0086  185 GLU A O   
1617 C CB  . GLU A 185 ? 0.2720 0.2185 0.2937 -0.0646 -0.0020 0.0144  185 GLU A CB  
1618 C CG  . GLU A 185 ? 0.5398 0.4978 0.5607 -0.0661 0.0040  0.0226  185 GLU A CG  
1619 C CD  . GLU A 185 ? 0.7195 0.6545 0.7305 -0.0722 0.0011  0.0311  185 GLU A CD  
1620 O OE1 . GLU A 185 ? 0.7284 0.6738 0.7377 -0.0789 0.0053  0.0392  185 GLU A OE1 
1621 O OE2 . GLU A 185 ? 0.7246 0.6313 0.7291 -0.0703 -0.0059 0.0294  185 GLU A OE2 
1622 N N   . GLU A 186 ? 0.1943 0.2358 0.2775 -0.0545 0.0478  0.0613  186 GLU A N   
1623 C CA  . GLU A 186 ? 0.2001 0.2624 0.2926 -0.0538 0.0545  0.0628  186 GLU A CA  
1624 C C   . GLU A 186 ? 0.1984 0.2722 0.3022 -0.0496 0.0520  0.0570  186 GLU A C   
1625 O O   . GLU A 186 ? 0.2081 0.3004 0.3212 -0.0474 0.0574  0.0580  186 GLU A O   
1626 C CB  . GLU A 186 ? 0.2202 0.2861 0.3007 -0.0471 0.0615  0.0634  186 GLU A CB  
1627 C CG  . GLU A 186 ? 0.2402 0.2992 0.3100 -0.0511 0.0649  0.0710  186 GLU A CG  
1628 C CD  . GLU A 186 ? 0.3331 0.3945 0.3879 -0.0446 0.0705  0.0705  186 GLU A CD  
1629 O OE1 . GLU A 186 ? 0.3075 0.3710 0.3580 -0.0369 0.0708  0.0631  186 GLU A OE1 
1630 O OE2 . GLU A 186 ? 0.4033 0.4639 0.4497 -0.0474 0.0747  0.0777  186 GLU A OE2 
1631 N N   . GLY A 187 ? 0.1840 0.2480 0.2871 -0.0480 0.0442  0.0516  187 GLY A N   
1632 C CA  . GLY A 187 ? 0.1513 0.2252 0.2639 -0.0437 0.0412  0.0470  187 GLY A CA  
1633 C C   . GLY A 187 ? 0.1820 0.2599 0.2898 -0.0328 0.0451  0.0432  187 GLY A C   
1634 O O   . GLY A 187 ? 0.1838 0.2729 0.3007 -0.0280 0.0447  0.0411  187 GLY A O   
1635 N N   . LYS A 188 ? 0.1774 0.2462 0.2706 -0.0287 0.0488  0.0422  188 LYS A N   
1636 C CA  . LYS A 188 ? 0.1579 0.2271 0.2443 -0.0192 0.0525  0.0375  188 LYS A CA  
1637 C C   . LYS A 188 ? 0.1498 0.2056 0.2295 -0.0149 0.0463  0.0315  188 LYS A C   
1638 O O   . LYS A 188 ? 0.1718 0.2266 0.2479 -0.0074 0.0485  0.0272  188 LYS A O   
1639 C CB  . LYS A 188 ? 0.1787 0.2450 0.2514 -0.0178 0.0590  0.0385  188 LYS A CB  
1640 C CG  . LYS A 188 ? 0.2512 0.3327 0.3300 -0.0210 0.0668  0.0447  188 LYS A CG  
1641 C CD  . LYS A 188 ? 0.3288 0.4076 0.3922 -0.0201 0.0729  0.0461  188 LYS A CD  
1642 C CE  . LYS A 188 ? 0.4295 0.5252 0.4989 -0.0227 0.0818  0.0524  188 LYS A CE  
1643 N NZ  . LYS A 188 ? 0.5194 0.6154 0.5728 -0.0188 0.0891  0.0516  188 LYS A NZ  
1644 N N   . GLY A 189 ? 0.1331 0.1782 0.2108 -0.0193 0.0392  0.0312  189 GLY A N   
1645 C CA  . GLY A 189 ? 0.1289 0.1635 0.2016 -0.0159 0.0334  0.0262  189 GLY A CA  
1646 C C   . GLY A 189 ? 0.1432 0.1695 0.2167 -0.0215 0.0265  0.0266  189 GLY A C   
1647 O O   . GLY A 189 ? 0.1774 0.2015 0.2516 -0.0276 0.0264  0.0305  189 GLY A O   
1648 N N   . SER A 190 ? 0.1331 0.1540 0.2058 -0.0193 0.0211  0.0227  190 SER A N   
1649 C CA  . SER A 190 ? 0.1581 0.1692 0.2286 -0.0229 0.0148  0.0216  190 SER A CA  
1650 C C   . SER A 190 ? 0.1709 0.1700 0.2286 -0.0200 0.0137  0.0193  190 SER A C   
1651 O O   . SER A 190 ? 0.1458 0.1442 0.1975 -0.0153 0.0159  0.0170  190 SER A O   
1652 C CB  . SER A 190 ? 0.1793 0.1937 0.2563 -0.0226 0.0095  0.0190  190 SER A CB  
1653 O OG  . SER A 190 ? 0.1648 0.1926 0.2546 -0.0263 0.0094  0.0213  190 SER A OG  
1654 N N   . VAL A 191 ? 0.1698 0.1595 0.2236 -0.0228 0.0104  0.0198  191 VAL A N   
1655 C CA  . VAL A 191 ? 0.1430 0.1237 0.1866 -0.0200 0.0086  0.0181  191 VAL A CA  
1656 C C   . VAL A 191 ? 0.1676 0.1423 0.2115 -0.0202 0.0032  0.0150  191 VAL A C   
1657 O O   . VAL A 191 ? 0.2058 0.1774 0.2539 -0.0240 0.0009  0.0155  191 VAL A O   
1658 C CB  . VAL A 191 ? 0.1576 0.1334 0.1950 -0.0212 0.0103  0.0223  191 VAL A CB  
1659 C CG1 . VAL A 191 ? 0.1737 0.1439 0.2016 -0.0177 0.0082  0.0207  191 VAL A CG1 
1660 C CG2 . VAL A 191 ? 0.1757 0.1586 0.2118 -0.0216 0.0161  0.0257  191 VAL A CG2 
1661 N N   . SER A 192 ? 0.1642 0.1367 0.2030 -0.0166 0.0015  0.0117  192 SER A N   
1662 C CA  . SER A 192 ? 0.1573 0.1250 0.1947 -0.0159 -0.0028 0.0088  192 SER A CA  
1663 C C   . SER A 192 ? 0.1566 0.1187 0.1863 -0.0137 -0.0035 0.0087  192 SER A C   
1664 O O   . SER A 192 ? 0.1724 0.1351 0.1976 -0.0127 -0.0013 0.0108  192 SER A O   
1665 C CB  . SER A 192 ? 0.1692 0.1408 0.2078 -0.0136 -0.0042 0.0059  192 SER A CB  
1666 O OG  . SER A 192 ? 0.1554 0.1268 0.1885 -0.0108 -0.0020 0.0052  192 SER A OG  
1667 N N   . THR A 193 ? 0.1646 0.1226 0.1926 -0.0125 -0.0066 0.0062  193 THR A N   
1668 C CA  . THR A 193 ? 0.1461 0.1023 0.1682 -0.0095 -0.0072 0.0059  193 THR A CA  
1669 C C   . THR A 193 ? 0.1702 0.1276 0.1911 -0.0080 -0.0094 0.0022  193 THR A C   
1670 O O   . THR A 193 ? 0.1730 0.1321 0.1967 -0.0090 -0.0104 0.0005  193 THR A O   
1671 C CB  . THR A 193 ? 0.1402 0.0897 0.1608 -0.0084 -0.0076 0.0081  193 THR A CB  
1672 O OG1 . THR A 193 ? 0.1672 0.1187 0.1832 -0.0048 -0.0077 0.0093  193 THR A OG1 
1673 C CG2 . THR A 193 ? 0.1606 0.1031 0.1825 -0.0087 -0.0098 0.0052  193 THR A CG2 
1674 N N   . SER A 194 ? 0.1434 0.1015 0.1603 -0.0056 -0.0099 0.0018  194 SER A N   
1675 C CA  . SER A 194 ? 0.1660 0.1261 0.1811 -0.0043 -0.0112 -0.0008 194 SER A CA  
1676 C C   . SER A 194 ? 0.1378 0.0956 0.1513 -0.0012 -0.0120 -0.0014 194 SER A C   
1677 O O   . SER A 194 ? 0.1672 0.1225 0.1803 0.0007  -0.0114 0.0011  194 SER A O   
1678 C CB  . SER A 194 ? 0.1747 0.1399 0.1869 -0.0047 -0.0104 -0.0008 194 SER A CB  
1679 O OG  . SER A 194 ? 0.1750 0.1404 0.1877 -0.0066 -0.0089 -0.0009 194 SER A OG  
1680 N N   . PRO A 195 ? 0.1651 0.1241 0.1771 0.0002  -0.0129 -0.0041 195 PRO A N   
1681 C CA  . PRO A 195 ? 0.1536 0.1127 0.1637 0.0045  -0.0127 -0.0047 195 PRO A CA  
1682 C C   . PRO A 195 ? 0.1605 0.1256 0.1707 0.0065  -0.0119 -0.0013 195 PRO A C   
1683 O O   . PRO A 195 ? 0.1586 0.1299 0.1685 0.0039  -0.0117 -0.0001 195 PRO A O   
1684 C CB  . PRO A 195 ? 0.1872 0.1510 0.1953 0.0047  -0.0130 -0.0073 195 PRO A CB  
1685 C CG  . PRO A 195 ? 0.3557 0.3177 0.3642 0.0011  -0.0142 -0.0085 195 PRO A CG  
1686 C CD  . PRO A 195 ? 0.1990 0.1602 0.2105 -0.0015 -0.0138 -0.0061 195 PRO A CD  
1687 N N   . TYR A 196 ? 0.1763 0.1391 0.1864 0.0114  -0.0114 0.0001  196 TYR A N   
1688 C CA  . TYR A 196 ? 0.1588 0.1246 0.1693 0.0138  -0.0112 0.0048  196 TYR A CA  
1689 C C   . TYR A 196 ? 0.1784 0.1575 0.1888 0.0121  -0.0118 0.0065  196 TYR A C   
1690 O O   . TYR A 196 ? 0.1576 0.1390 0.1667 0.0096  -0.0121 0.0089  196 TYR A O   
1691 C CB  . TYR A 196 ? 0.1519 0.1143 0.1626 0.0210  -0.0105 0.0062  196 TYR A CB  
1692 C CG  . TYR A 196 ? 0.1557 0.1155 0.1663 0.0240  -0.0103 0.0121  196 TYR A CG  
1693 C CD1 . TYR A 196 ? 0.1801 0.1525 0.1909 0.0253  -0.0112 0.0165  196 TYR A CD1 
1694 C CD2 . TYR A 196 ? 0.1849 0.1298 0.1947 0.0246  -0.0094 0.0135  196 TYR A CD2 
1695 C CE1 . TYR A 196 ? 0.2004 0.1712 0.2102 0.0284  -0.0113 0.0229  196 TYR A CE1 
1696 C CE2 . TYR A 196 ? 0.1826 0.1241 0.1916 0.0274  -0.0090 0.0200  196 TYR A CE2 
1697 C CZ  . TYR A 196 ? 0.1949 0.1497 0.2036 0.0297  -0.0100 0.0250  196 TYR A CZ  
1698 O OH  . TYR A 196 ? 0.2248 0.1770 0.2319 0.0328  -0.0097 0.0323  196 TYR A OH  
1699 N N   . TYR A 197 ? 0.1530 0.1413 0.1642 0.0132  -0.0119 0.0051  197 TYR A N   
1700 C CA  . TYR A 197 ? 0.1461 0.1475 0.1574 0.0103  -0.0127 0.0064  197 TYR A CA  
1701 C C   . TYR A 197 ? 0.1669 0.1691 0.1769 0.0037  -0.0126 0.0034  197 TYR A C   
1702 O O   . TYR A 197 ? 0.1593 0.1714 0.1694 0.0005  -0.0130 0.0033  197 TYR A O   
1703 C CB  . TYR A 197 ? 0.1624 0.1764 0.1768 0.0152  -0.0128 0.0080  197 TYR A CB  
1704 C CG  . TYR A 197 ? 0.1601 0.1733 0.1757 0.0225  -0.0130 0.0122  197 TYR A CG  
1705 C CD1 . TYR A 197 ? 0.1626 0.1819 0.1776 0.0223  -0.0147 0.0166  197 TYR A CD1 
1706 C CD2 . TYR A 197 ? 0.1643 0.1691 0.1807 0.0297  -0.0113 0.0117  197 TYR A CD2 
1707 C CE1 . TYR A 197 ? 0.2066 0.2244 0.2222 0.0295  -0.0148 0.0217  197 TYR A CE1 
1708 C CE2 . TYR A 197 ? 0.1933 0.1944 0.2103 0.0369  -0.0111 0.0161  197 TYR A CE2 
1709 C CZ  . TYR A 197 ? 0.1912 0.1991 0.2081 0.0370  -0.0129 0.0217  197 TYR A CZ  
1710 O OH  . TYR A 197 ? 0.2515 0.2555 0.2687 0.0447  -0.0126 0.0274  197 TYR A OH  
1711 N N   . HIS A 198 ? 0.1270 0.1189 0.1358 0.0016  -0.0120 0.0013  198 HIS A N   
1712 C CA  . HIS A 198 ? 0.1472 0.1377 0.1544 -0.0035 -0.0115 -0.0007 198 HIS A CA  
1713 C C   . HIS A 198 ? 0.1875 0.1839 0.1947 -0.0046 -0.0112 -0.0016 198 HIS A C   
1714 O O   . HIS A 198 ? 0.1828 0.1828 0.1887 -0.0094 -0.0109 -0.0018 198 HIS A O   
1715 C CB  . HIS A 198 ? 0.1426 0.1351 0.1473 -0.0077 -0.0115 -0.0003 198 HIS A CB  
1716 C CG  . HIS A 198 ? 0.1655 0.1518 0.1679 -0.0119 -0.0103 -0.0023 198 HIS A CG  
1717 N ND1 . HIS A 198 ? 0.1831 0.1709 0.1835 -0.0162 -0.0099 -0.0036 198 HIS A ND1 
1718 C CD2 . HIS A 198 ? 0.1608 0.1393 0.1626 -0.0121 -0.0091 -0.0030 198 HIS A CD2 
1719 C CE1 . HIS A 198 ? 0.1496 0.1287 0.1477 -0.0182 -0.0084 -0.0051 198 HIS A CE1 
1720 N NE2 . HIS A 198 ? 0.1610 0.1355 0.1603 -0.0153 -0.0078 -0.0047 198 HIS A NE2 
1721 N N   . PRO A 199 ? 0.1453 0.1420 0.1532 -0.0008 -0.0108 -0.0023 199 PRO A N   
1722 C CA  . PRO A 199 ? 0.1491 0.1520 0.1565 -0.0017 -0.0098 -0.0028 199 PRO A CA  
1723 C C   . PRO A 199 ? 0.1687 0.1648 0.1733 -0.0047 -0.0096 -0.0037 199 PRO A C   
1724 O O   . PRO A 199 ? 0.1884 0.1759 0.1925 -0.0047 -0.0104 -0.0044 199 PRO A O   
1725 C CB  . PRO A 199 ? 0.1925 0.1970 0.2005 0.0046  -0.0091 -0.0038 199 PRO A CB  
1726 C CG  . PRO A 199 ? 0.2034 0.1956 0.2104 0.0066  -0.0101 -0.0053 199 PRO A CG  
1727 C CD  . PRO A 199 ? 0.1471 0.1367 0.1553 0.0040  -0.0110 -0.0033 199 PRO A CD  
1728 N N   . LEU A 200 ? 0.1896 0.1908 0.1927 -0.0067 -0.0084 -0.0031 200 LEU A N   
1729 C CA  . LEU A 200 ? 0.1862 0.1822 0.1860 -0.0082 -0.0082 -0.0028 200 LEU A CA  
1730 C C   . LEU A 200 ? 0.1721 0.1682 0.1697 -0.0037 -0.0084 -0.0046 200 LEU A C   
1731 O O   . LEU A 200 ? 0.1830 0.1861 0.1788 -0.0026 -0.0068 -0.0046 200 LEU A O   
1732 C CB  . LEU A 200 ? 0.2057 0.2062 0.2040 -0.0132 -0.0065 -0.0006 200 LEU A CB  
1733 C CG  . LEU A 200 ? 0.2262 0.2234 0.2247 -0.0190 -0.0062 0.0002  200 LEU A CG  
1734 C CD1 . LEU A 200 ? 0.2755 0.2794 0.2735 -0.0249 -0.0045 0.0021  200 LEU A CD1 
1735 C CD2 . LEU A 200 ? 0.2626 0.2468 0.2587 -0.0195 -0.0065 0.0004  200 LEU A CD2 
1736 N N   . ILE A 201 ? 0.1816 0.1703 0.1792 -0.0016 -0.0102 -0.0065 201 ILE A N   
1737 C CA  . ILE A 201 ? 0.1816 0.1683 0.1763 0.0018  -0.0110 -0.0095 201 ILE A CA  
1738 C C   . ILE A 201 ? 0.1680 0.1580 0.1574 0.0013  -0.0106 -0.0092 201 ILE A C   
1739 O O   . ILE A 201 ? 0.1756 0.1688 0.1613 0.0043  -0.0095 -0.0117 201 ILE A O   
1740 C CB  . ILE A 201 ? 0.1765 0.1550 0.1725 0.0017  -0.0135 -0.0111 201 ILE A CB  
1741 C CG1 . ILE A 201 ? 0.1688 0.1439 0.1688 0.0028  -0.0133 -0.0111 201 ILE A CG1 
1742 C CG2 . ILE A 201 ? 0.1640 0.1397 0.1557 0.0033  -0.0150 -0.0150 201 ILE A CG2 
1743 C CD1 . ILE A 201 ? 0.1833 0.1577 0.1825 0.0074  -0.0122 -0.0133 201 ILE A CD1 
1744 N N   . PRO A 202 ? 0.1726 0.1614 0.1606 -0.0018 -0.0111 -0.0061 202 PRO A N   
1745 C CA  . PRO A 202 ? 0.1692 0.1614 0.1511 -0.0019 -0.0107 -0.0048 202 PRO A CA  
1746 C C   . PRO A 202 ? 0.1535 0.1546 0.1334 -0.0017 -0.0073 -0.0042 202 PRO A C   
1747 O O   . PRO A 202 ? 0.1872 0.1923 0.1613 0.0004  -0.0064 -0.0056 202 PRO A O   
1748 C CB  . PRO A 202 ? 0.1673 0.1555 0.1493 -0.0048 -0.0113 -0.0002 202 PRO A CB  
1749 C CG  . PRO A 202 ? 0.1653 0.1474 0.1526 -0.0047 -0.0131 -0.0011 202 PRO A CG  
1750 C CD  . PRO A 202 ? 0.1668 0.1502 0.1578 -0.0043 -0.0120 -0.0036 202 PRO A CD  
1751 N N   . ILE A 203 ? 0.1594 0.1648 0.1436 -0.0040 -0.0052 -0.0023 203 ILE A N   
1752 C CA  . ILE A 203 ? 0.1686 0.1855 0.1527 -0.0041 -0.0018 -0.0012 203 ILE A CA  
1753 C C   . ILE A 203 ? 0.1956 0.2176 0.1801 0.0021  -0.0006 -0.0053 203 ILE A C   
1754 O O   . ILE A 203 ? 0.1810 0.2109 0.1620 0.0046  0.0023  -0.0060 203 ILE A O   
1755 C CB  . ILE A 203 ? 0.1870 0.2088 0.1765 -0.0093 -0.0006 0.0017  203 ILE A CB  
1756 C CG1 . ILE A 203 ? 0.1983 0.2130 0.1854 -0.0154 -0.0006 0.0056  203 ILE A CG1 
1757 C CG2 . ILE A 203 ? 0.1793 0.2165 0.1712 -0.0092 0.0028  0.0027  203 ILE A CG2 
1758 C CD1 . ILE A 203 ? 0.1899 0.2071 0.1807 -0.0223 0.0005  0.0075  203 ILE A CD1 
1759 N N   . LEU A 204 ? 0.1906 0.2075 0.1788 0.0052  -0.0022 -0.0079 204 LEU A N   
1760 C CA  . LEU A 204 ? 0.1897 0.2082 0.1778 0.0120  -0.0008 -0.0116 204 LEU A CA  
1761 C C   . LEU A 204 ? 0.1790 0.1925 0.1590 0.0149  -0.0007 -0.0160 204 LEU A C   
1762 O O   . LEU A 204 ? 0.1847 0.2027 0.1617 0.0201  0.0023  -0.0190 204 LEU A O   
1763 C CB  . LEU A 204 ? 0.1607 0.1718 0.1533 0.0143  -0.0027 -0.0127 204 LEU A CB  
1764 C CG  . LEU A 204 ? 0.1710 0.1875 0.1703 0.0120  -0.0032 -0.0090 204 LEU A CG  
1765 C CD1 . LEU A 204 ? 0.1971 0.2065 0.1991 0.0158  -0.0045 -0.0098 204 LEU A CD1 
1766 C CD2 . LEU A 204 ? 0.1906 0.2236 0.1938 0.0126  -0.0005 -0.0066 204 LEU A CD2 
1767 N N   . LEU A 205 ? 0.1901 0.1956 0.1663 0.0117  -0.0040 -0.0166 205 LEU A N   
1768 C CA  . LEU A 205 ? 0.1759 0.1777 0.1435 0.0133  -0.0049 -0.0210 205 LEU A CA  
1769 C C   . LEU A 205 ? 0.2057 0.2168 0.1664 0.0129  -0.0024 -0.0194 205 LEU A C   
1770 O O   . LEU A 205 ? 0.2152 0.2278 0.1682 0.0164  -0.0007 -0.0238 205 LEU A O   
1771 C CB  . LEU A 205 ? 0.2234 0.2169 0.1902 0.0098  -0.0097 -0.0214 205 LEU A CB  
1772 C CG  . LEU A 205 ? 0.1935 0.1772 0.1649 0.0102  -0.0119 -0.0243 205 LEU A CG  
1773 C CD1 . LEU A 205 ? 0.2103 0.1897 0.1833 0.0061  -0.0163 -0.0234 205 LEU A CD1 
1774 C CD2 . LEU A 205 ? 0.2257 0.2033 0.1921 0.0142  -0.0111 -0.0311 205 LEU A CD2 
1775 N N   . ASN A 206 ? 0.1639 0.1803 0.1265 0.0086  -0.0018 -0.0131 206 ASN A N   
1776 C CA  . ASN A 206 ? 0.1560 0.1803 0.1118 0.0072  0.0007  -0.0100 206 ASN A CA  
1777 C C   . ASN A 206 ? 0.2022 0.2309 0.1628 0.0019  0.0024  -0.0029 206 ASN A C   
1778 O O   . ASN A 206 ? 0.2051 0.2272 0.1661 -0.0019 -0.0001 0.0010  206 ASN A O   
1779 C CB  . ASN A 206 ? 0.2008 0.2208 0.1481 0.0062  -0.0028 -0.0101 206 ASN A CB  
1780 C CG  . ASN A 206 ? 0.3022 0.3306 0.2401 0.0057  -0.0001 -0.0072 206 ASN A CG  
1781 O OD1 . ASN A 206 ? 0.2313 0.2684 0.1705 0.0046  0.0045  -0.0033 206 ASN A OD1 
1782 N ND2 . ASN A 206 ? 0.3922 0.4195 0.3205 0.0063  -0.0030 -0.0088 206 ASN A ND2 
1783 N N   . PRO A 207 ? 0.1822 0.2217 0.1468 0.0015  0.0066  -0.0013 207 PRO A N   
1784 C CA  . PRO A 207 ? 0.1741 0.2172 0.1432 -0.0052 0.0080  0.0049  207 PRO A CA  
1785 C C   . PRO A 207 ? 0.1970 0.2374 0.1595 -0.0097 0.0085  0.0106  207 PRO A C   
1786 O O   . PRO A 207 ? 0.2059 0.2421 0.1711 -0.0157 0.0086  0.0153  207 PRO A O   
1787 C CB  . PRO A 207 ? 0.2093 0.2686 0.1831 -0.0045 0.0126  0.0053  207 PRO A CB  
1788 C CG  . PRO A 207 ? 0.2345 0.2948 0.2096 0.0038  0.0127  -0.0010 207 PRO A CG  
1789 C CD  . PRO A 207 ? 0.2066 0.2553 0.1730 0.0072  0.0100  -0.0052 207 PRO A CD  
1790 N N   . ASN A 208 ? 0.1848 0.2263 0.1379 -0.0070 0.0087  0.0103  208 ASN A N   
1791 C CA  . ASN A 208 ? 0.1869 0.2262 0.1330 -0.0105 0.0090  0.0170  208 ASN A CA  
1792 C C   . ASN A 208 ? 0.2182 0.2438 0.1645 -0.0116 0.0045  0.0196  208 ASN A C   
1793 O O   . ASN A 208 ? 0.2230 0.2447 0.1646 -0.0142 0.0047  0.0264  208 ASN A O   
1794 C CB  . ASN A 208 ? 0.2376 0.2832 0.1724 -0.0068 0.0101  0.0159  208 ASN A CB  
1795 C CG  . ASN A 208 ? 0.2660 0.3262 0.2000 -0.0054 0.0160  0.0146  208 ASN A CG  
1796 O OD1 . ASN A 208 ? 0.2744 0.3425 0.2128 -0.0100 0.0201  0.0195  208 ASN A OD1 
1797 N ND2 . ASN A 208 ? 0.3873 0.4514 0.3158 0.0008  0.0167  0.0075  208 ASN A ND2 
1798 N N   . CYS A 209 ? 0.2002 0.2188 0.1521 -0.0095 0.0008  0.0150  209 CYS A N   
1799 C CA  . CYS A 209 ? 0.2475 0.2548 0.2012 -0.0101 -0.0028 0.0175  209 CYS A CA  
1800 C C   . CYS A 209 ? 0.1802 0.1810 0.1371 -0.0152 -0.0006 0.0230  209 CYS A C   
1801 O O   . CYS A 209 ? 0.2357 0.2268 0.1920 -0.0152 -0.0022 0.0269  209 CYS A O   
1802 C CB  . CYS A 209 ? 0.2494 0.2520 0.2093 -0.0074 -0.0062 0.0116  209 CYS A CB  
1803 S SG  . CYS A 209 ? 0.2783 0.2801 0.2477 -0.0094 -0.0045 0.0089  209 CYS A SG  
1804 N N   . VAL A 210 ? 0.2087 0.2146 0.1691 -0.0196 0.0029  0.0233  210 VAL A N   
1805 C CA  . VAL A 210 ? 0.1980 0.1963 0.1606 -0.0260 0.0047  0.0276  210 VAL A CA  
1806 C C   . VAL A 210 ? 0.2383 0.2317 0.1940 -0.0285 0.0066  0.0354  210 VAL A C   
1807 O O   . VAL A 210 ? 0.2401 0.2212 0.1956 -0.0324 0.0075  0.0394  210 VAL A O   
1808 C CB  . VAL A 210 ? 0.2025 0.2102 0.1708 -0.0314 0.0076  0.0262  210 VAL A CB  
1809 C CG1 . VAL A 210 ? 0.2404 0.2529 0.2152 -0.0280 0.0056  0.0196  210 VAL A CG1 
1810 C CG2 . VAL A 210 ? 0.2606 0.2827 0.2262 -0.0329 0.0115  0.0289  210 VAL A CG2 
1811 N N   . TYR A 211 ? 0.2469 0.2486 0.1957 -0.0262 0.0075  0.0378  211 TYR A N   
1812 C CA  . TYR A 211 ? 0.2515 0.2492 0.1926 -0.0285 0.0095  0.0465  211 TYR A CA  
1813 C C   . TYR A 211 ? 0.2222 0.2084 0.1595 -0.0238 0.0058  0.0503  211 TYR A C   
1814 O O   . TYR A 211 ? 0.2667 0.2464 0.1979 -0.0251 0.0071  0.0587  211 TYR A O   
1815 C CB  . TYR A 211 ? 0.2198 0.2320 0.1538 -0.0275 0.0120  0.0480  211 TYR A CB  
1816 C CG  . TYR A 211 ? 0.2450 0.2711 0.1834 -0.0314 0.0166  0.0457  211 TYR A CG  
1817 C CD1 . TYR A 211 ? 0.3034 0.3294 0.2457 -0.0400 0.0204  0.0502  211 TYR A CD1 
1818 C CD2 . TYR A 211 ? 0.2086 0.2481 0.1474 -0.0265 0.0171  0.0391  211 TYR A CD2 
1819 C CE1 . TYR A 211 ? 0.2633 0.3054 0.2112 -0.0437 0.0243  0.0486  211 TYR A CE1 
1820 C CE2 . TYR A 211 ? 0.2584 0.3127 0.2024 -0.0287 0.0215  0.0376  211 TYR A CE2 
1821 C CZ  . TYR A 211 ? 0.2769 0.3339 0.2260 -0.0374 0.0249  0.0427  211 TYR A CZ  
1822 O OH  . TYR A 211 ? 0.2906 0.3653 0.2462 -0.0398 0.0290  0.0417  211 TYR A OH  
1823 N N   . GLU A 212 ? 0.2314 0.2156 0.1725 -0.0186 0.0013  0.0449  212 GLU A N   
1824 C CA  . GLU A 212 ? 0.2237 0.2014 0.1625 -0.0135 -0.0026 0.0485  212 GLU A CA  
1825 C C   . GLU A 212 ? 0.2692 0.2309 0.2099 -0.0146 -0.0012 0.0543  212 GLU A C   
1826 O O   . GLU A 212 ? 0.2884 0.2442 0.2246 -0.0113 -0.0021 0.0617  212 GLU A O   
1827 C CB  . GLU A 212 ? 0.2456 0.2269 0.1893 -0.0088 -0.0073 0.0411  212 GLU A CB  
1828 C CG  . GLU A 212 ? 0.2853 0.2794 0.2244 -0.0070 -0.0089 0.0359  212 GLU A CG  
1829 C CD  . GLU A 212 ? 0.3538 0.3499 0.2970 -0.0037 -0.0135 0.0285  212 GLU A CD  
1830 O OE1 . GLU A 212 ? 0.3805 0.3837 0.3212 -0.0030 -0.0138 0.0221  212 GLU A OE1 
1831 O OE2 . GLU A 212 ? 0.3122 0.3028 0.2611 -0.0019 -0.0163 0.0291  212 GLU A OE2 
1832 N N   . THR A 213 ? 0.2608 0.2147 0.2074 -0.0189 0.0012  0.0510  213 THR A N   
1833 C CA  . THR A 213 ? 0.2673 0.2036 0.2141 -0.0205 0.0033  0.0555  213 THR A CA  
1834 C C   . THR A 213 ? 0.3046 0.2345 0.2501 -0.0298 0.0081  0.0576  213 THR A C   
1835 O O   . THR A 213 ? 0.3106 0.2234 0.2539 -0.0319 0.0105  0.0621  213 THR A O   
1836 C CB  . THR A 213 ? 0.3234 0.2521 0.2772 -0.0173 0.0017  0.0501  213 THR A CB  
1837 O OG1 . THR A 213 ? 0.3253 0.2582 0.2841 -0.0219 0.0024  0.0424  213 THR A OG1 
1838 C CG2 . THR A 213 ? 0.2876 0.2238 0.2440 -0.0093 -0.0031 0.0484  213 THR A CG2 
1839 N N   . THR A 214 ? 0.2694 0.2125 0.2161 -0.0354 0.0098  0.0546  214 THR A N   
1840 C CA  . THR A 214 ? 0.2521 0.1933 0.1979 -0.0453 0.0143  0.0576  214 THR A CA  
1841 C C   . THR A 214 ? 0.3255 0.2834 0.2676 -0.0471 0.0164  0.0611  214 THR A C   
1842 O O   . THR A 214 ? 0.2895 0.2631 0.2358 -0.0501 0.0176  0.0569  214 THR A O   
1843 C CB  . THR A 214 ? 0.2911 0.2342 0.2440 -0.0514 0.0147  0.0503  214 THR A CB  
1844 O OG1 . THR A 214 ? 0.2757 0.2356 0.2337 -0.0475 0.0123  0.0436  214 THR A OG1 
1845 C CG2 . THR A 214 ? 0.2838 0.2086 0.2381 -0.0504 0.0137  0.0473  214 THR A CG2 
1846 N N   . PRO A 215 ? 0.3230 0.2785 0.2570 -0.0448 0.0172  0.0693  215 PRO A N   
1847 C CA  . PRO A 215 ? 0.2974 0.2698 0.2262 -0.0454 0.0195  0.0724  215 PRO A CA  
1848 C C   . PRO A 215 ? 0.3103 0.2905 0.2409 -0.0556 0.0249  0.0748  215 PRO A C   
1849 O O   . PRO A 215 ? 0.3236 0.3219 0.2525 -0.0558 0.0273  0.0749  215 PRO A O   
1850 C CB  . PRO A 215 ? 0.3364 0.3018 0.2552 -0.0413 0.0190  0.0819  215 PRO A CB  
1851 C CG  . PRO A 215 ? 0.3625 0.3050 0.2820 -0.0424 0.0191  0.0864  215 PRO A CG  
1852 C CD  . PRO A 215 ? 0.3219 0.2599 0.2506 -0.0410 0.0164  0.0767  215 PRO A CD  
1853 N N   . ASN A 216 ? 0.3146 0.2822 0.2486 -0.0644 0.0270  0.0763  216 ASN A N   
1854 C CA  . ASN A 216 ? 0.3948 0.3701 0.3313 -0.0759 0.0319  0.0792  216 ASN A CA  
1855 C C   . ASN A 216 ? 0.3633 0.3518 0.3104 -0.0802 0.0312  0.0707  216 ASN A C   
1856 O O   . ASN A 216 ? 0.3918 0.3886 0.3430 -0.0908 0.0346  0.0723  216 ASN A O   
1857 C CB  . ASN A 216 ? 0.4369 0.3902 0.3699 -0.0848 0.0347  0.0864  216 ASN A CB  
1858 C CG  . ASN A 216 ? 0.5122 0.4532 0.4344 -0.0809 0.0360  0.0971  216 ASN A CG  
1859 O OD1 . ASN A 216 ? 0.5128 0.4673 0.4294 -0.0767 0.0368  0.1015  216 ASN A OD1 
1860 N ND2 . ASN A 216 ? 0.6031 0.5183 0.5222 -0.0815 0.0362  0.1011  216 ASN A ND2 
1861 N N   . VAL A 217 ? 0.3015 0.2928 0.2532 -0.0727 0.0269  0.0622  217 VAL A N   
1862 C CA  . VAL A 217 ? 0.3069 0.3103 0.2683 -0.0758 0.0259  0.0549  217 VAL A CA  
1863 C C   . VAL A 217 ? 0.3063 0.3359 0.2716 -0.0757 0.0286  0.0546  217 VAL A C   
1864 O O   . VAL A 217 ? 0.3005 0.3390 0.2610 -0.0690 0.0299  0.0562  217 VAL A O   
1865 C CB  . VAL A 217 ? 0.2702 0.2690 0.2347 -0.0673 0.0209  0.0471  217 VAL A CB  
1866 C CG1 . VAL A 217 ? 0.2587 0.2685 0.2217 -0.0564 0.0193  0.0444  217 VAL A CG1 
1867 C CG2 . VAL A 217 ? 0.3157 0.3223 0.2888 -0.0718 0.0196  0.0409  217 VAL A CG2 
1868 N N   . LYS A 218 ? 0.2456 0.2886 0.2196 -0.0832 0.0296  0.0525  218 LYS A N   
1869 C CA  . LYS A 218 ? 0.2308 0.3009 0.2111 -0.0822 0.0323  0.0518  218 LYS A CA  
1870 C C   . LYS A 218 ? 0.2599 0.3390 0.2477 -0.0752 0.0285  0.0438  218 LYS A C   
1871 O O   . LYS A 218 ? 0.2509 0.3233 0.2430 -0.0787 0.0252  0.0401  218 LYS A O   
1872 C CB  . LYS A 218 ? 0.2760 0.3586 0.2621 -0.0957 0.0361  0.0562  218 LYS A CB  
1873 C CG  . LYS A 218 ? 0.3557 0.4257 0.3343 -0.1049 0.0400  0.0650  218 LYS A CG  
1874 C CD  . LYS A 218 ? 0.4636 0.5341 0.4324 -0.0972 0.0429  0.0702  218 LYS A CD  
1875 C CE  . LYS A 218 ? 0.4808 0.5592 0.4477 -0.1050 0.0488  0.0784  218 LYS A CE  
1876 N NZ  . LYS A 218 ? 0.4333 0.5233 0.3922 -0.0973 0.0524  0.0822  218 LYS A NZ  
1877 N N   . ILE A 219 ? 0.2666 0.3592 0.2549 -0.0650 0.0293  0.0411  219 ILE A N   
1878 C CA  . ILE A 219 ? 0.2157 0.3155 0.2106 -0.0570 0.0262  0.0343  219 ILE A CA  
1879 C C   . ILE A 219 ? 0.1990 0.3242 0.1994 -0.0523 0.0301  0.0339  219 ILE A C   
1880 O O   . ILE A 219 ? 0.2306 0.3662 0.2279 -0.0533 0.0351  0.0380  219 ILE A O   
1881 C CB  . ILE A 219 ? 0.2041 0.2880 0.1928 -0.0469 0.0225  0.0299  219 ILE A CB  
1882 C CG1 . ILE A 219 ? 0.2251 0.3114 0.2056 -0.0396 0.0249  0.0304  219 ILE A CG1 
1883 C CG2 . ILE A 219 ? 0.2373 0.2982 0.2219 -0.0504 0.0192  0.0305  219 ILE A CG2 
1884 C CD1 . ILE A 219 ? 0.2607 0.3331 0.2356 -0.0308 0.0208  0.0256  219 ILE A CD1 
1885 N N   . PRO A 220 ? 0.2166 0.3530 0.2253 -0.0467 0.0283  0.0296  220 PRO A N   
1886 C CA  . PRO A 220 ? 0.1852 0.3462 0.2000 -0.0405 0.0325  0.0294  220 PRO A CA  
1887 C C   . PRO A 220 ? 0.1723 0.3305 0.1793 -0.0284 0.0347  0.0261  220 PRO A C   
1888 O O   . PRO A 220 ? 0.1842 0.3227 0.1815 -0.0254 0.0322  0.0240  220 PRO A O   
1889 C CB  . PRO A 220 ? 0.2167 0.3878 0.2424 -0.0377 0.0291  0.0265  220 PRO A CB  
1890 C CG  . PRO A 220 ? 0.2333 0.3821 0.2557 -0.0391 0.0232  0.0236  220 PRO A CG  
1891 C CD  . PRO A 220 ? 0.2504 0.3800 0.2641 -0.0473 0.0230  0.0260  220 PRO A CD  
1892 N N   . ASP A 221 ? 0.1899 0.3686 0.2007 -0.0217 0.0396  0.0256  221 ASP A N   
1893 C CA  . ASP A 221 ? 0.1665 0.3438 0.1692 -0.0101 0.0426  0.0213  221 ASP A CA  
1894 C C   . ASP A 221 ? 0.1674 0.3345 0.1714 0.0002  0.0387  0.0147  221 ASP A C   
1895 O O   . ASP A 221 ? 0.1697 0.3495 0.1836 0.0057  0.0392  0.0136  221 ASP A O   
1896 C CB  . ASP A 221 ? 0.1662 0.3697 0.1731 -0.0064 0.0501  0.0231  221 ASP A CB  
1897 C CG  . ASP A 221 ? 0.1749 0.3780 0.1733 0.0067  0.0540  0.0173  221 ASP A CG  
1898 O OD1 . ASP A 221 ? 0.2054 0.3878 0.1926 0.0107  0.0509  0.0125  221 ASP A OD1 
1899 O OD2 . ASP A 221 ? 0.2219 0.4467 0.2251 0.0128  0.0604  0.0174  221 ASP A OD2 
1900 N N   . PHE A 222 ? 0.1776 0.3224 0.1721 0.0027  0.0349  0.0108  222 PHE A N   
1901 C CA  . PHE A 222 ? 0.1532 0.2863 0.1478 0.0116  0.0317  0.0047  222 PHE A CA  
1902 C C   . PHE A 222 ? 0.2305 0.3679 0.2200 0.0229  0.0362  -0.0005 222 PHE A C   
1903 O O   . PHE A 222 ? 0.2449 0.3691 0.2229 0.0264  0.0358  -0.0051 222 PHE A O   
1904 C CB  . PHE A 222 ? 0.2001 0.3098 0.1878 0.0089  0.0260  0.0027  222 PHE A CB  
1905 C CG  . PHE A 222 ? 0.1709 0.2741 0.1647 0.0013  0.0214  0.0056  222 PHE A CG  
1906 C CD1 . PHE A 222 ? 0.1899 0.2944 0.1842 -0.0090 0.0216  0.0110  222 PHE A CD1 
1907 C CD2 . PHE A 222 ? 0.1875 0.2816 0.1854 0.0043  0.0174  0.0028  222 PHE A CD2 
1908 C CE1 . PHE A 222 ? 0.1644 0.2610 0.1629 -0.0159 0.0178  0.0125  222 PHE A CE1 
1909 C CE2 . PHE A 222 ? 0.1802 0.2684 0.1823 -0.0025 0.0136  0.0048  222 PHE A CE2 
1910 C CZ  . PHE A 222 ? 0.1537 0.2428 0.1558 -0.0124 0.0138  0.0091  222 PHE A CZ  
1911 N N   . ALA A 223 ? 0.2000 0.3565 0.1981 0.0289  0.0407  0.0000  223 ALA A N   
1912 C CA  . ALA A 223 ? 0.2012 0.3643 0.1951 0.0405  0.0467  -0.0047 223 ALA A CA  
1913 C C   . ALA A 223 ? 0.2116 0.3621 0.2058 0.0517  0.0452  -0.0109 223 ALA A C   
1914 O O   . ALA A 223 ? 0.3226 0.4813 0.3183 0.0629  0.0505  -0.0139 223 ALA A O   
1915 C CB  . ALA A 223 ? 0.2399 0.4322 0.2435 0.0421  0.0532  -0.0003 223 ALA A CB  
1916 N N   . VAL A 224 ? 0.1898 0.3201 0.1828 0.0491  0.0387  -0.0125 224 VAL A N   
1917 C CA  . VAL A 224 ? 0.2333 0.3479 0.2256 0.0579  0.0368  -0.0177 224 VAL A CA  
1918 C C   . VAL A 224 ? 0.2274 0.3187 0.2124 0.0518  0.0305  -0.0202 224 VAL A C   
1919 O O   . VAL A 224 ? 0.2559 0.3457 0.2411 0.0418  0.0270  -0.0163 224 VAL A O   
1920 C CB  . VAL A 224 ? 0.2917 0.4157 0.2977 0.0618  0.0357  -0.0137 224 VAL A CB  
1921 C CG1 . VAL A 224 ? 0.2383 0.3607 0.2501 0.0509  0.0295  -0.0087 224 VAL A CG1 
1922 C CG2 . VAL A 224 ? 0.3638 0.4727 0.3687 0.0731  0.0356  -0.0183 224 VAL A CG2 
1923 N N   . SER A 225 ? 0.2267 0.2997 0.2053 0.0577  0.0295  -0.0267 225 SER A N   
1924 C CA  . SER A 225 ? 0.2152 0.2681 0.1882 0.0520  0.0236  -0.0291 225 SER A CA  
1925 C C   . SER A 225 ? 0.2038 0.2487 0.1851 0.0507  0.0192  -0.0264 225 SER A C   
1926 O O   . SER A 225 ? 0.2393 0.2836 0.2260 0.0582  0.0205  -0.0264 225 SER A O   
1927 C CB  . SER A 225 ? 0.2386 0.2753 0.1998 0.0568  0.0242  -0.0378 225 SER A CB  
1928 O OG  . SER A 225 ? 0.2560 0.2759 0.2135 0.0507  0.0181  -0.0397 225 SER A OG  
1929 N N   . PHE A 226 ? 0.1814 0.2203 0.1634 0.0418  0.0143  -0.0237 226 PHE A N   
1930 C CA  . PHE A 226 ? 0.1851 0.2146 0.1727 0.0397  0.0101  -0.0218 226 PHE A CA  
1931 C C   . PHE A 226 ? 0.2106 0.2209 0.1922 0.0375  0.0064  -0.0260 226 PHE A C   
1932 O O   . PHE A 226 ? 0.1965 0.1991 0.1820 0.0341  0.0030  -0.0241 226 PHE A O   
1933 C CB  . PHE A 226 ? 0.1734 0.2108 0.1668 0.0313  0.0077  -0.0158 226 PHE A CB  
1934 C CG  . PHE A 226 ? 0.1813 0.2377 0.1826 0.0317  0.0101  -0.0113 226 PHE A CG  
1935 C CD1 . PHE A 226 ? 0.1933 0.2546 0.2022 0.0357  0.0095  -0.0091 226 PHE A CD1 
1936 C CD2 . PHE A 226 ? 0.1927 0.2632 0.1940 0.0277  0.0128  -0.0088 226 PHE A CD2 
1937 C CE1 . PHE A 226 ? 0.1897 0.2714 0.2067 0.0356  0.0109  -0.0047 226 PHE A CE1 
1938 C CE2 . PHE A 226 ? 0.2019 0.2920 0.2116 0.0267  0.0148  -0.0046 226 PHE A CE2 
1939 C CZ  . PHE A 226 ? 0.1851 0.2818 0.2031 0.0307  0.0136  -0.0028 226 PHE A CZ  
1940 N N   . ARG A 227 ? 0.2253 0.2287 0.1976 0.0389  0.0071  -0.0318 227 ARG A N   
1941 C CA  . ARG A 227 ? 0.2191 0.2074 0.1863 0.0347  0.0028  -0.0355 227 ARG A CA  
1942 C C   . ARG A 227 ? 0.2085 0.1819 0.1779 0.0375  0.0017  -0.0379 227 ARG A C   
1943 O O   . ARG A 227 ? 0.2489 0.2139 0.2207 0.0324  -0.0022 -0.0369 227 ARG A O   
1944 C CB  . ARG A 227 ? 0.2066 0.1926 0.1622 0.0348  0.0033  -0.0415 227 ARG A CB  
1945 C CG  . ARG A 227 ? 0.2467 0.2447 0.1991 0.0303  0.0032  -0.0378 227 ARG A CG  
1946 C CD  . ARG A 227 ? 0.2527 0.2501 0.1922 0.0308  0.0037  -0.0434 227 ARG A CD  
1947 N NE  . ARG A 227 ? 0.2993 0.2843 0.2331 0.0272  -0.0014 -0.0485 227 ARG A NE  
1948 C CZ  . ARG A 227 ? 0.3411 0.3262 0.2752 0.0207  -0.0066 -0.0455 227 ARG A CZ  
1949 N NH1 . ARG A 227 ? 0.2924 0.2863 0.2314 0.0176  -0.0070 -0.0375 227 ARG A NH1 
1950 N NH2 . ARG A 227 ? 0.3241 0.3003 0.2538 0.0174  -0.0113 -0.0504 227 ARG A NH2 
1951 N N   . GLU A 228 ? 0.2205 0.1906 0.1895 0.0460  0.0055  -0.0406 228 GLU A N   
1952 C CA  . GLU A 228 ? 0.2474 0.2019 0.2183 0.0490  0.0049  -0.0416 228 GLU A CA  
1953 C C   . GLU A 228 ? 0.2252 0.1835 0.2059 0.0469  0.0029  -0.0340 228 GLU A C   
1954 O O   . GLU A 228 ? 0.2418 0.1878 0.2241 0.0440  0.0004  -0.0332 228 GLU A O   
1955 C CB  . GLU A 228 ? 0.3498 0.3000 0.3184 0.0601  0.0101  -0.0451 228 GLU A CB  
1956 C CG  . GLU A 228 ? 0.5265 0.4579 0.4962 0.0645  0.0103  -0.0456 228 GLU A CG  
1957 C CD  . GLU A 228 ? 0.7693 0.6930 0.7349 0.0765  0.0159  -0.0501 228 GLU A CD  
1958 O OE1 . GLU A 228 ? 0.8428 0.7512 0.8097 0.0819  0.0169  -0.0493 228 GLU A OE1 
1959 O OE2 . GLU A 228 ? 0.8344 0.7668 0.7951 0.0809  0.0197  -0.0543 228 GLU A OE2 
1960 N N   . ASP A 229 ? 0.2089 0.1847 0.1958 0.0473  0.0039  -0.0285 229 ASP A N   
1961 C CA  . ASP A 229 ? 0.2072 0.1873 0.2017 0.0446  0.0017  -0.0220 229 ASP A CA  
1962 C C   . ASP A 229 ? 0.2121 0.1865 0.2065 0.0353  -0.0023 -0.0212 229 ASP A C   
1963 O O   . ASP A 229 ? 0.1973 0.1657 0.1949 0.0334  -0.0042 -0.0184 229 ASP A O   
1964 C CB  . ASP A 229 ? 0.1869 0.1876 0.1875 0.0449  0.0030  -0.0171 229 ASP A CB  
1965 C CG  . ASP A 229 ? 0.2142 0.2234 0.2189 0.0548  0.0063  -0.0155 229 ASP A CG  
1966 O OD1 . ASP A 229 ? 0.2558 0.2525 0.2583 0.0624  0.0080  -0.0179 229 ASP A OD1 
1967 O OD2 . ASP A 229 ? 0.2227 0.2512 0.2332 0.0551  0.0074  -0.0116 229 ASP A OD2 
1968 N N   . ALA A 230 ? 0.1873 0.1639 0.1777 0.0301  -0.0034 -0.0232 230 ALA A N   
1969 C CA  . ALA A 230 ? 0.2317 0.2036 0.2224 0.0228  -0.0069 -0.0222 230 ALA A CA  
1970 C C   . ALA A 230 ? 0.2205 0.1774 0.2103 0.0218  -0.0088 -0.0249 230 ALA A C   
1971 O O   . ALA A 230 ? 0.1965 0.1499 0.1903 0.0181  -0.0107 -0.0221 230 ALA A O   
1972 C CB  . ALA A 230 ? 0.1958 0.1720 0.1818 0.0190  -0.0077 -0.0236 230 ALA A CB  
1973 N N   . SER A 231 ? 0.2075 0.1553 0.1917 0.0248  -0.0081 -0.0306 231 SER A N   
1974 C CA  . SER A 231 ? 0.2209 0.1530 0.2040 0.0230  -0.0096 -0.0335 231 SER A CA  
1975 C C   . SER A 231 ? 0.1973 0.1235 0.1856 0.0258  -0.0086 -0.0291 231 SER A C   
1976 O O   . SER A 231 ? 0.2370 0.1558 0.2281 0.0213  -0.0104 -0.0273 231 SER A O   
1977 C CB  . SER A 231 ? 0.3095 0.2312 0.2843 0.0261  -0.0084 -0.0412 231 SER A CB  
1978 O OG  . SER A 231 ? 0.4502 0.3715 0.4197 0.0202  -0.0116 -0.0458 231 SER A OG  
1979 N N   . LYS A 232 ? 0.2062 0.1374 0.1962 0.0333  -0.0056 -0.0266 232 LYS A N   
1980 C CA  . LYS A 232 ? 0.2027 0.1294 0.1969 0.0371  -0.0047 -0.0215 232 LYS A CA  
1981 C C   . LYS A 232 ? 0.1710 0.1045 0.1705 0.0317  -0.0069 -0.0155 232 LYS A C   
1982 O O   . LYS A 232 ? 0.2006 0.1258 0.2018 0.0307  -0.0073 -0.0122 232 LYS A O   
1983 C CB  . LYS A 232 ? 0.2536 0.1887 0.2496 0.0468  -0.0015 -0.0193 232 LYS A CB  
1984 C CG  . LYS A 232 ? 0.3622 0.2861 0.3531 0.0549  0.0018  -0.0245 232 LYS A CG  
1985 C CD  . LYS A 232 ? 0.4614 0.3939 0.4564 0.0660  0.0051  -0.0204 232 LYS A CD  
1986 C CE  . LYS A 232 ? 0.4945 0.4231 0.4942 0.0686  0.0041  -0.0129 232 LYS A CE  
1987 N NZ  . LYS A 232 ? 0.5827 0.5134 0.5850 0.0816  0.0075  -0.0096 232 LYS A NZ  
1988 N N   . HIS A 233 ? 0.1873 0.1349 0.1886 0.0280  -0.0078 -0.0141 233 HIS A N   
1989 C CA  . HIS A 233 ? 0.1548 0.1074 0.1597 0.0228  -0.0094 -0.0096 233 HIS A CA  
1990 C C   . HIS A 233 ? 0.2076 0.1499 0.2126 0.0171  -0.0110 -0.0103 233 HIS A C   
1991 O O   . HIS A 233 ? 0.1930 0.1334 0.2004 0.0152  -0.0112 -0.0064 233 HIS A O   
1992 C CB  . HIS A 233 ? 0.1493 0.1148 0.1549 0.0190  -0.0099 -0.0091 233 HIS A CB  
1993 C CG  . HIS A 233 ? 0.1575 0.1366 0.1651 0.0220  -0.0087 -0.0066 233 HIS A CG  
1994 N ND1 . HIS A 233 ? 0.1961 0.1831 0.2066 0.0209  -0.0093 -0.0023 233 HIS A ND1 
1995 C CD2 . HIS A 233 ? 0.1613 0.1495 0.1685 0.0250  -0.0070 -0.0078 233 HIS A CD2 
1996 C CE1 . HIS A 233 ? 0.1858 0.1866 0.1985 0.0228  -0.0085 -0.0010 233 HIS A CE1 
1997 N NE2 . HIS A 233 ? 0.1690 0.1711 0.1802 0.0255  -0.0067 -0.0040 233 HIS A NE2 
1998 N N   . VAL A 234 ? 0.1972 0.1347 0.1997 0.0141  -0.0122 -0.0150 234 VAL A N   
1999 C CA  . VAL A 234 ? 0.2176 0.1486 0.2216 0.0081  -0.0141 -0.0157 234 VAL A CA  
2000 C C   . VAL A 234 ? 0.1802 0.0973 0.1842 0.0085  -0.0134 -0.0155 234 VAL A C   
2001 O O   . VAL A 234 ? 0.1883 0.1022 0.1956 0.0046  -0.0136 -0.0122 234 VAL A O   
2002 C CB  . VAL A 234 ? 0.2060 0.1377 0.2074 0.0047  -0.0163 -0.0205 234 VAL A CB  
2003 C CG1 . VAL A 234 ? 0.2200 0.1482 0.2247 -0.0018 -0.0186 -0.0207 234 VAL A CG1 
2004 C CG2 . VAL A 234 ? 0.1884 0.1322 0.1894 0.0045  -0.0165 -0.0194 234 VAL A CG2 
2005 N N   . GLU A 235 ? 0.1875 0.0953 0.1873 0.0134  -0.0121 -0.0188 235 GLU A N   
2006 C CA  . GLU A 235 ? 0.2235 0.1145 0.2222 0.0136  -0.0112 -0.0190 235 GLU A CA  
2007 C C   . GLU A 235 ? 0.2241 0.1140 0.2259 0.0166  -0.0096 -0.0113 235 GLU A C   
2008 O O   . GLU A 235 ? 0.2243 0.1047 0.2276 0.0128  -0.0094 -0.0084 235 GLU A O   
2009 C CB  . GLU A 235 ? 0.2939 0.1737 0.2864 0.0196  -0.0094 -0.0247 235 GLU A CB  
2010 C CG  . GLU A 235 ? 0.4697 0.3279 0.4594 0.0179  -0.0088 -0.0269 235 GLU A CG  
2011 C CD  . GLU A 235 ? 0.5729 0.4270 0.5637 0.0067  -0.0120 -0.0297 235 GLU A CD  
2012 O OE1 . GLU A 235 ? 0.5712 0.4320 0.5599 0.0026  -0.0146 -0.0352 235 GLU A OE1 
2013 O OE2 . GLU A 235 ? 0.6363 0.4818 0.6303 0.0020  -0.0119 -0.0259 235 GLU A OE2 
2014 N N   . LEU A 236 ? 0.2304 0.1310 0.2331 0.0230  -0.0084 -0.0077 236 LEU A N   
2015 C CA  . LEU A 236 ? 0.2007 0.1028 0.2056 0.0260  -0.0075 -0.0001 236 LEU A CA  
2016 C C   . LEU A 236 ? 0.1915 0.0992 0.1992 0.0188  -0.0086 0.0037  236 LEU A C   
2017 O O   . LEU A 236 ? 0.2238 0.1265 0.2320 0.0183  -0.0077 0.0093  236 LEU A O   
2018 C CB  . LEU A 236 ? 0.2211 0.1376 0.2271 0.0331  -0.0069 0.0026  236 LEU A CB  
2019 C CG  . LEU A 236 ? 0.2560 0.1677 0.2602 0.0425  -0.0047 0.0005  236 LEU A CG  
2020 C CD1 . LEU A 236 ? 0.2848 0.2158 0.2920 0.0483  -0.0043 0.0034  236 LEU A CD1 
2021 C CD2 . LEU A 236 ? 0.2737 0.1677 0.2764 0.0477  -0.0029 0.0040  236 LEU A CD2 
2022 N N   . ALA A 237 ? 0.1851 0.1031 0.1942 0.0139  -0.0099 0.0011  237 ALA A N   
2023 C CA  . ALA A 237 ? 0.1616 0.0849 0.1733 0.0080  -0.0103 0.0039  237 ALA A CA  
2024 C C   . ALA A 237 ? 0.1944 0.1075 0.2079 0.0025  -0.0101 0.0041  237 ALA A C   
2025 O O   . ALA A 237 ? 0.1894 0.1032 0.2046 -0.0005 -0.0090 0.0088  237 ALA A O   
2026 C CB  . ALA A 237 ? 0.1715 0.1056 0.1841 0.0050  -0.0114 0.0008  237 ALA A CB  
2027 N N   . LYS A 238 ? 0.1863 0.0907 0.1992 0.0002  -0.0113 -0.0010 238 LYS A N   
2028 C CA  . LYS A 238 ? 0.2143 0.1088 0.2293 -0.0063 -0.0114 -0.0011 238 LYS A CA  
2029 C C   . LYS A 238 ? 0.1988 0.0808 0.2126 -0.0048 -0.0092 0.0043  238 LYS A C   
2030 O O   . LYS A 238 ? 0.2259 0.1053 0.2427 -0.0103 -0.0081 0.0084  238 LYS A O   
2031 C CB  . LYS A 238 ? 0.2266 0.1131 0.2394 -0.0090 -0.0135 -0.0084 238 LYS A CB  
2032 C CG  . LYS A 238 ? 0.2059 0.1046 0.2197 -0.0113 -0.0161 -0.0127 238 LYS A CG  
2033 C CD  . LYS A 238 ? 0.2601 0.1521 0.2697 -0.0133 -0.0185 -0.0204 238 LYS A CD  
2034 C CE  . LYS A 238 ? 0.3063 0.1856 0.3167 -0.0206 -0.0195 -0.0225 238 LYS A CE  
2035 N NZ  . LYS A 238 ? 0.3091 0.1833 0.3142 -0.0239 -0.0224 -0.0310 238 LYS A NZ  
2036 N N   . GLU A 239 ? 0.2200 0.0949 0.2299 0.0031  -0.0080 0.0052  239 GLU A N   
2037 C CA  . GLU A 239 ? 0.2549 0.1172 0.2631 0.0062  -0.0057 0.0115  239 GLU A CA  
2038 C C   . GLU A 239 ? 0.2201 0.0925 0.2298 0.0061  -0.0047 0.0198  239 GLU A C   
2039 O O   . GLU A 239 ? 0.2467 0.1113 0.2566 0.0030  -0.0030 0.0257  239 GLU A O   
2040 C CB  . GLU A 239 ? 0.2531 0.1087 0.2574 0.0166  -0.0046 0.0110  239 GLU A CB  
2041 C CG  . GLU A 239 ? 0.3697 0.2111 0.3706 0.0173  -0.0046 0.0027  239 GLU A CG  
2042 C CD  . GLU A 239 ? 0.4520 0.2906 0.4495 0.0290  -0.0028 0.0015  239 GLU A CD  
2043 O OE1 . GLU A 239 ? 0.5497 0.3786 0.5432 0.0308  -0.0022 -0.0062 239 GLU A OE1 
2044 O OE2 . GLU A 239 ? 0.4578 0.3051 0.4568 0.0364  -0.0019 0.0082  239 GLU A OE2 
2045 N N   . LYS A 240 ? 0.2096 0.0990 0.2195 0.0091  -0.0055 0.0204  240 LYS A N   
2046 C CA  . LYS A 240 ? 0.2164 0.1156 0.2259 0.0090  -0.0047 0.0272  240 LYS A CA  
2047 C C   . LYS A 240 ? 0.1975 0.1001 0.2097 0.0006  -0.0038 0.0280  240 LYS A C   
2048 O O   . LYS A 240 ? 0.2066 0.1086 0.2179 -0.0012 -0.0019 0.0345  240 LYS A O   
2049 C CB  . LYS A 240 ? 0.2379 0.1538 0.2465 0.0127  -0.0061 0.0264  240 LYS A CB  
2050 C CG  . LYS A 240 ? 0.2370 0.1628 0.2432 0.0134  -0.0057 0.0330  240 LYS A CG  
2051 C CD  . LYS A 240 ? 0.3009 0.2208 0.3045 0.0198  -0.0051 0.0405  240 LYS A CD  
2052 C CE  . LYS A 240 ? 0.3021 0.2343 0.3020 0.0207  -0.0055 0.0471  240 LYS A CE  
2053 N NZ  . LYS A 240 ? 0.3352 0.2618 0.3324 0.0273  -0.0051 0.0561  240 LYS A NZ  
2054 N N   . TYR A 241 ? 0.2047 0.1117 0.2204 -0.0040 -0.0050 0.0219  241 TYR A N   
2055 C CA  . TYR A 241 ? 0.2339 0.1455 0.2538 -0.0111 -0.0039 0.0226  241 TYR A CA  
2056 C C   . TYR A 241 ? 0.2133 0.1127 0.2350 -0.0162 -0.0024 0.0260  241 TYR A C   
2057 O O   . TYR A 241 ? 0.2123 0.1152 0.2360 -0.0204 0.0001  0.0310  241 TYR A O   
2058 C CB  . TYR A 241 ? 0.2048 0.1228 0.2284 -0.0141 -0.0060 0.0159  241 TYR A CB  
2059 C CG  . TYR A 241 ? 0.1796 0.1059 0.2087 -0.0198 -0.0048 0.0168  241 TYR A CG  
2060 C CD1 . TYR A 241 ? 0.2048 0.1272 0.2392 -0.0264 -0.0047 0.0172  241 TYR A CD1 
2061 C CD2 . TYR A 241 ? 0.1844 0.1228 0.2139 -0.0187 -0.0036 0.0169  241 TYR A CD2 
2062 C CE1 . TYR A 241 ? 0.1951 0.1279 0.2362 -0.0312 -0.0033 0.0185  241 TYR A CE1 
2063 C CE2 . TYR A 241 ? 0.1952 0.1418 0.2304 -0.0225 -0.0018 0.0177  241 TYR A CE2 
2064 C CZ  . TYR A 241 ? 0.2180 0.1632 0.2596 -0.0284 -0.0017 0.0188  241 TYR A CZ  
2065 O OH  . TYR A 241 ? 0.2228 0.1788 0.2714 -0.0317 0.0003  0.0201  241 TYR A OH  
2066 N N   . PHE A 242 ? 0.2043 0.0888 0.2249 -0.0162 -0.0034 0.0234  242 PHE A N   
2067 C CA  . PHE A 242 ? 0.2254 0.0959 0.2474 -0.0221 -0.0019 0.0265  242 PHE A CA  
2068 C C   . PHE A 242 ? 0.2265 0.0920 0.2453 -0.0196 0.0012  0.0362  242 PHE A C   
2069 O O   . PHE A 242 ? 0.2308 0.0935 0.2517 -0.0260 0.0036  0.0415  242 PHE A O   
2070 C CB  . PHE A 242 ? 0.2287 0.0812 0.2481 -0.0220 -0.0033 0.0211  242 PHE A CB  
2071 C CG  . PHE A 242 ? 0.2482 0.0851 0.2678 -0.0296 -0.0016 0.0229  242 PHE A CG  
2072 C CD1 . PHE A 242 ? 0.2528 0.0761 0.2665 -0.0265 0.0015  0.0296  242 PHE A CD1 
2073 C CD2 . PHE A 242 ? 0.2773 0.1161 0.3003 -0.0394 -0.0028 0.0177  242 PHE A CD2 
2074 C CE1 . PHE A 242 ? 0.2953 0.1048 0.3055 -0.0337 0.0036  0.0308  242 PHE A CE1 
2075 C CE2 . PHE A 242 ? 0.2953 0.1223 0.3165 -0.0470 -0.0004 0.0186  242 PHE A CE2 
2076 C CZ  . PHE A 242 ? 0.3007 0.1119 0.3150 -0.0444 0.0031  0.0251  242 PHE A CZ  
2077 N N   . GLU A 243 ? 0.2462 0.1121 0.2598 -0.0104 0.0012  0.0391  243 GLU A N   
2078 C CA  . GLU A 243 ? 0.2574 0.1202 0.2671 -0.0072 0.0036  0.0491  243 GLU A CA  
2079 C C   . GLU A 243 ? 0.2177 0.0950 0.2282 -0.0117 0.0055  0.0538  243 GLU A C   
2080 O O   . GLU A 243 ? 0.2428 0.1154 0.2523 -0.0152 0.0085  0.0615  243 GLU A O   
2081 C CB  . GLU A 243 ? 0.2765 0.1430 0.2818 0.0037  0.0024  0.0513  243 GLU A CB  
2082 C CG  . GLU A 243 ? 0.3311 0.1957 0.3318 0.0077  0.0042  0.0624  243 GLU A CG  
2083 C CD  . GLU A 243 ? 0.4327 0.3108 0.4300 0.0167  0.0023  0.0653  243 GLU A CD  
2084 O OE1 . GLU A 243 ? 0.4789 0.3576 0.4719 0.0207  0.0031  0.0749  243 GLU A OE1 
2085 O OE2 . GLU A 243 ? 0.3812 0.2697 0.3800 0.0196  0.0000  0.0586  243 GLU A OE2 
2086 N N   . ILE A 244 ? 0.2181 0.1124 0.2299 -0.0117 0.0044  0.0492  244 ILE A N   
2087 C CA  . ILE A 244 ? 0.2489 0.1570 0.2598 -0.0143 0.0067  0.0526  244 ILE A CA  
2088 C C   . ILE A 244 ? 0.2474 0.1579 0.2647 -0.0228 0.0092  0.0522  244 ILE A C   
2089 O O   . ILE A 244 ? 0.2403 0.1549 0.2568 -0.0261 0.0128  0.0584  244 ILE A O   
2090 C CB  . ILE A 244 ? 0.2244 0.1475 0.2335 -0.0110 0.0050  0.0475  244 ILE A CB  
2091 C CG1 . ILE A 244 ? 0.2575 0.1815 0.2617 -0.0033 0.0024  0.0482  244 ILE A CG1 
2092 C CG2 . ILE A 244 ? 0.2541 0.1895 0.2607 -0.0133 0.0080  0.0499  244 ILE A CG2 
2093 C CD1 . ILE A 244 ? 0.2692 0.1912 0.2674 0.0006  0.0034  0.0576  244 ILE A CD1 
2094 N N   . PHE A 245 ? 0.1991 0.1087 0.2229 -0.0266 0.0072  0.0453  245 PHE A N   
2095 C CA  . PHE A 245 ? 0.2334 0.1508 0.2650 -0.0341 0.0088  0.0443  245 PHE A CA  
2096 C C   . PHE A 245 ? 0.2735 0.1802 0.3107 -0.0418 0.0082  0.0438  245 PHE A C   
2097 O O   . PHE A 245 ? 0.2751 0.1899 0.3200 -0.0490 0.0097  0.0444  245 PHE A O   
2098 C CB  . PHE A 245 ? 0.1936 0.1238 0.2288 -0.0328 0.0069  0.0371  245 PHE A CB  
2099 C CG  . PHE A 245 ? 0.2168 0.1571 0.2466 -0.0273 0.0081  0.0370  245 PHE A CG  
2100 C CD1 . PHE A 245 ? 0.2325 0.1819 0.2612 -0.0283 0.0124  0.0411  245 PHE A CD1 
2101 C CD2 . PHE A 245 ? 0.2261 0.1667 0.2515 -0.0217 0.0052  0.0328  245 PHE A CD2 
2102 C CE1 . PHE A 245 ? 0.2641 0.2213 0.2863 -0.0240 0.0134  0.0400  245 PHE A CE1 
2103 C CE2 . PHE A 245 ? 0.2615 0.2106 0.2816 -0.0181 0.0060  0.0323  245 PHE A CE2 
2104 C CZ  . PHE A 245 ? 0.2607 0.2174 0.2788 -0.0194 0.0099  0.0355  245 PHE A CZ  
2105 N N   . GLY A 246 ? 0.2403 0.1295 0.2742 -0.0407 0.0063  0.0426  246 GLY A N   
2106 C CA  . GLY A 246 ? 0.2648 0.1405 0.3022 -0.0492 0.0063  0.0427  246 GLY A CA  
2107 C C   . GLY A 246 ? 0.2433 0.1212 0.2866 -0.0549 0.0025  0.0341  246 GLY A C   
2108 O O   . GLY A 246 ? 0.2901 0.1638 0.3353 -0.0632 0.0028  0.0325  246 GLY A O   
2109 N N   . GLU A 247 ? 0.2430 0.1302 0.2860 -0.0500 -0.0007 0.0274  247 GLU A N   
2110 C CA  . GLU A 247 ? 0.2847 0.1740 0.3313 -0.0542 -0.0049 0.0193  247 GLU A CA  
2111 C C   . GLU A 247 ? 0.2300 0.1194 0.2707 -0.0457 -0.0076 0.0134  247 GLU A C   
2112 O O   . GLU A 247 ? 0.2402 0.1333 0.2766 -0.0377 -0.0062 0.0156  247 GLU A O   
2113 C CB  . GLU A 247 ? 0.4091 0.3189 0.4656 -0.0595 -0.0056 0.0188  247 GLU A CB  
2114 C CG  . GLU A 247 ? 0.5636 0.4834 0.6261 -0.0635 -0.0010 0.0263  247 GLU A CG  
2115 C CD  . GLU A 247 ? 0.6310 0.5733 0.7023 -0.0641 -0.0009 0.0258  247 GLU A CD  
2116 O OE1 . GLU A 247 ? 0.5390 0.4891 0.6085 -0.0571 -0.0024 0.0223  247 GLU A OE1 
2117 O OE2 . GLU A 247 ? 0.6865 0.6388 0.7669 -0.0714 0.0011  0.0293  247 GLU A OE2 
2118 N N   . HIS A 248 ? 0.2552 0.1412 0.2953 -0.0480 -0.0114 0.0060  248 HIS A N   
2119 C CA  . HIS A 248 ? 0.2643 0.1553 0.3001 -0.0410 -0.0137 0.0007  248 HIS A CA  
2120 C C   . HIS A 248 ? 0.2770 0.1883 0.3183 -0.0406 -0.0145 0.0011  248 HIS A C   
2121 O O   . HIS A 248 ? 0.2733 0.1944 0.3222 -0.0470 -0.0155 0.0016  248 HIS A O   
2122 C CB  . HIS A 248 ? 0.3246 0.2066 0.3566 -0.0434 -0.0173 -0.0075 248 HIS A CB  
2123 C CG  . HIS A 248 ? 0.4829 0.3429 0.5080 -0.0423 -0.0157 -0.0090 248 HIS A CG  
2124 N ND1 . HIS A 248 ? 0.5374 0.3885 0.5560 -0.0326 -0.0139 -0.0085 248 HIS A ND1 
2125 C CD2 . HIS A 248 ? 0.5579 0.4057 0.5805 -0.0486 -0.0140 -0.0107 248 HIS A CD2 
2126 C CE1 . HIS A 248 ? 0.5729 0.4064 0.5855 -0.0321 -0.0111 -0.0097 248 HIS A CE1 
2127 N NE2 . HIS A 248 ? 0.5632 0.3935 0.5778 -0.0421 -0.0109 -0.0113 248 HIS A NE2 
2128 N N   . PRO A 249 ? 0.2430 0.1610 0.2809 -0.0331 -0.0140 0.0012  249 PRO A N   
2129 C CA  . PRO A 249 ? 0.2115 0.1457 0.2537 -0.0321 -0.0141 0.0019  249 PRO A CA  
2130 C C   . PRO A 249 ? 0.2392 0.1800 0.2839 -0.0343 -0.0182 -0.0029 249 PRO A C   
2131 O O   . PRO A 249 ? 0.3348 0.2705 0.3740 -0.0326 -0.0208 -0.0077 249 PRO A O   
2132 C CB  . PRO A 249 ? 0.2203 0.1561 0.2567 -0.0245 -0.0127 0.0026  249 PRO A CB  
2133 C CG  . PRO A 249 ? 0.2497 0.1739 0.2796 -0.0211 -0.0136 0.0000  249 PRO A CG  
2134 C CD  . PRO A 249 ? 0.2299 0.1412 0.2603 -0.0255 -0.0133 0.0006  249 PRO A CD  
2135 N N   . VAL A 250 ? 0.2180 0.1715 0.2709 -0.0379 -0.0188 -0.0014 250 VAL A N   
2136 C CA  . VAL A 250 ? 0.2402 0.2032 0.2958 -0.0391 -0.0231 -0.0047 250 VAL A CA  
2137 C C   . VAL A 250 ? 0.2117 0.1847 0.2674 -0.0327 -0.0224 -0.0033 250 VAL A C   
2138 O O   . VAL A 250 ? 0.2095 0.1899 0.2660 -0.0319 -0.0259 -0.0051 250 VAL A O   
2139 C CB  . VAL A 250 ? 0.2730 0.2456 0.3386 -0.0471 -0.0252 -0.0039 250 VAL A CB  
2140 C CG1 . VAL A 250 ? 0.2844 0.2442 0.3488 -0.0550 -0.0263 -0.0062 250 VAL A CG1 
2141 C CG2 . VAL A 250 ? 0.2814 0.2653 0.3556 -0.0469 -0.0210 0.0019  250 VAL A CG2 
2142 N N   . TYR A 251 ? 0.1889 0.1617 0.2432 -0.0283 -0.0181 -0.0002 251 TYR A N   
2143 C CA  . TYR A 251 ? 0.1888 0.1667 0.2412 -0.0224 -0.0169 0.0006  251 TYR A CA  
2144 C C   . TYR A 251 ? 0.1751 0.1446 0.2188 -0.0186 -0.0153 -0.0003 251 TYR A C   
2145 O O   . TYR A 251 ? 0.2004 0.1640 0.2415 -0.0187 -0.0131 0.0012  251 TYR A O   
2146 C CB  . TYR A 251 ? 0.2561 0.2419 0.3141 -0.0210 -0.0128 0.0042  251 TYR A CB  
2147 C CG  . TYR A 251 ? 0.2693 0.2640 0.3372 -0.0256 -0.0127 0.0063  251 TYR A CG  
2148 C CD1 . TYR A 251 ? 0.3292 0.3344 0.4040 -0.0269 -0.0164 0.0059  251 TYR A CD1 
2149 C CD2 . TYR A 251 ? 0.3761 0.3704 0.4469 -0.0290 -0.0092 0.0093  251 TYR A CD2 
2150 C CE1 . TYR A 251 ? 0.4255 0.4415 0.5106 -0.0318 -0.0168 0.0079  251 TYR A CE1 
2151 C CE2 . TYR A 251 ? 0.3466 0.3507 0.4275 -0.0343 -0.0089 0.0115  251 TYR A CE2 
2152 C CZ  . TYR A 251 ? 0.4270 0.4426 0.5156 -0.0357 -0.0129 0.0106  251 TYR A CZ  
2153 O OH  . TYR A 251 ? 0.4889 0.5173 0.5889 -0.0414 -0.0134 0.0128  251 TYR A OH  
2154 N N   . MET A 252 ? 0.1507 0.1208 0.1901 -0.0151 -0.0165 -0.0018 252 MET A N   
2155 C CA  . MET A 252 ? 0.1507 0.1162 0.1833 -0.0120 -0.0148 -0.0021 252 MET A CA  
2156 C C   . MET A 252 ? 0.1452 0.1140 0.1763 -0.0093 -0.0136 -0.0015 252 MET A C   
2157 O O   . MET A 252 ? 0.1689 0.1418 0.2022 -0.0084 -0.0150 -0.0013 252 MET A O   
2158 C CB  . MET A 252 ? 0.2004 0.1609 0.2275 -0.0111 -0.0168 -0.0050 252 MET A CB  
2159 C CG  . MET A 252 ? 0.2491 0.2020 0.2751 -0.0120 -0.0165 -0.0054 252 MET A CG  
2160 S SD  . MET A 252 ? 0.2387 0.1864 0.2577 -0.0082 -0.0171 -0.0084 252 MET A SD  
2161 C CE  . MET A 252 ? 0.2616 0.1981 0.2804 -0.0084 -0.0162 -0.0078 252 MET A CE  
2162 N N   . TRP A 253 ? 0.1394 0.1061 0.1664 -0.0080 -0.0110 -0.0010 253 TRP A N   
2163 C CA  . TRP A 253 ? 0.1618 0.1283 0.1855 -0.0064 -0.0098 -0.0012 253 TRP A CA  
2164 C C   . TRP A 253 ? 0.1479 0.1130 0.1665 -0.0062 -0.0112 -0.0025 253 TRP A C   
2165 O O   . TRP A 253 ? 0.1544 0.1188 0.1703 -0.0063 -0.0110 -0.0029 253 TRP A O   
2166 C CB  . TRP A 253 ? 0.1567 0.1221 0.1780 -0.0064 -0.0063 -0.0008 253 TRP A CB  
2167 C CG  . TRP A 253 ? 0.1401 0.1026 0.1565 -0.0060 -0.0051 -0.0019 253 TRP A CG  
2168 C CD1 . TRP A 253 ? 0.1581 0.1192 0.1688 -0.0077 -0.0046 -0.0030 253 TRP A CD1 
2169 C CD2 . TRP A 253 ? 0.1647 0.1248 0.1814 -0.0043 -0.0042 -0.0016 253 TRP A CD2 
2170 N NE1 . TRP A 253 ? 0.1714 0.1285 0.1788 -0.0083 -0.0034 -0.0039 253 TRP A NE1 
2171 C CE2 . TRP A 253 ? 0.1392 0.0944 0.1498 -0.0056 -0.0029 -0.0028 253 TRP A CE2 
2172 C CE3 . TRP A 253 ? 0.1846 0.1469 0.2066 -0.0016 -0.0045 0.0001  253 TRP A CE3 
2173 C CZ2 . TRP A 253 ? 0.1754 0.1248 0.1841 -0.0044 -0.0015 -0.0024 253 TRP A CZ2 
2174 C CZ3 . TRP A 253 ? 0.1470 0.1051 0.1675 0.0009  -0.0033 0.0010  253 TRP A CZ3 
2175 C CH2 . TRP A 253 ? 0.1631 0.1134 0.1766 -0.0005 -0.0015 -0.0002 253 TRP A CH2 
2176 N N   . PRO A 254 ? 0.1286 0.0942 0.1458 -0.0054 -0.0125 -0.0027 254 PRO A N   
2177 C CA  . PRO A 254 ? 0.1537 0.1195 0.1662 -0.0054 -0.0131 -0.0035 254 PRO A CA  
2178 C C   . PRO A 254 ? 0.1273 0.0920 0.1366 -0.0067 -0.0108 -0.0031 254 PRO A C   
2179 O O   . PRO A 254 ? 0.1574 0.1190 0.1661 -0.0070 -0.0091 -0.0024 254 PRO A O   
2180 C CB  . PRO A 254 ? 0.1742 0.1412 0.1856 -0.0046 -0.0148 -0.0028 254 PRO A CB  
2181 C CG  . PRO A 254 ? 0.2099 0.1768 0.2253 -0.0035 -0.0143 -0.0008 254 PRO A CG  
2182 C CD  . PRO A 254 ? 0.1793 0.1467 0.1994 -0.0041 -0.0133 -0.0012 254 PRO A CD  
2183 N N   . PRO A 255 ? 0.1286 0.0960 0.1359 -0.0074 -0.0106 -0.0037 255 PRO A N   
2184 C CA  . PRO A 255 ? 0.1443 0.1123 0.1488 -0.0100 -0.0091 -0.0037 255 PRO A CA  
2185 C C   . PRO A 255 ? 0.1680 0.1330 0.1699 -0.0120 -0.0082 -0.0032 255 PRO A C   
2186 O O   . PRO A 255 ? 0.1574 0.1234 0.1585 -0.0113 -0.0089 -0.0022 255 PRO A O   
2187 C CB  . PRO A 255 ? 0.1408 0.1156 0.1450 -0.0097 -0.0099 -0.0038 255 PRO A CB  
2188 C CG  . PRO A 255 ? 0.1322 0.1063 0.1388 -0.0063 -0.0110 -0.0039 255 PRO A CG  
2189 C CD  . PRO A 255 ? 0.1343 0.1041 0.1421 -0.0057 -0.0118 -0.0044 255 PRO A CD  
2190 N N   . GLN A 256 ? 0.1724 0.1324 0.1718 -0.0144 -0.0063 -0.0038 256 GLN A N   
2191 C CA  . GLN A 256 ? 0.1739 0.1274 0.1701 -0.0166 -0.0047 -0.0031 256 GLN A CA  
2192 C C   . GLN A 256 ? 0.1878 0.1372 0.1855 -0.0127 -0.0048 -0.0008 256 GLN A C   
2193 O O   . GLN A 256 ? 0.1756 0.1206 0.1708 -0.0133 -0.0042 0.0014  256 GLN A O   
2194 C CB  . GLN A 256 ? 0.1815 0.1392 0.1756 -0.0206 -0.0049 -0.0024 256 GLN A CB  
2195 C CG  . GLN A 256 ? 0.2637 0.2295 0.2578 -0.0240 -0.0055 -0.0039 256 GLN A CG  
2196 C CD  . GLN A 256 ? 0.2934 0.2547 0.2842 -0.0279 -0.0045 -0.0065 256 GLN A CD  
2197 O OE1 . GLN A 256 ? 0.3411 0.3094 0.3318 -0.0293 -0.0056 -0.0077 256 GLN A OE1 
2198 N NE2 . GLN A 256 ? 0.2663 0.2157 0.2534 -0.0296 -0.0023 -0.0073 256 GLN A NE2 
2199 N N   . ALA A 257 ? 0.1567 0.1081 0.1586 -0.0090 -0.0058 -0.0007 257 ALA A N   
2200 C CA  . ALA A 257 ? 0.1626 0.1141 0.1673 -0.0053 -0.0070 0.0017  257 ALA A CA  
2201 C C   . ALA A 257 ? 0.1892 0.1447 0.1922 -0.0052 -0.0094 0.0032  257 ALA A C   
2202 O O   . ALA A 257 ? 0.1834 0.1390 0.1866 -0.0028 -0.0105 0.0060  257 ALA A O   
2203 C CB  . ALA A 257 ? 0.1667 0.1101 0.1706 -0.0032 -0.0044 0.0035  257 ALA A CB  
2204 N N   . SER A 258 ? 0.1697 0.1296 0.1709 -0.0073 -0.0100 0.0017  258 SER A N   
2205 C CA  . SER A 258 ? 0.1543 0.1175 0.1519 -0.0076 -0.0109 0.0030  258 SER A CA  
2206 C C   . SER A 258 ? 0.1653 0.1331 0.1637 -0.0050 -0.0140 0.0023  258 SER A C   
2207 O O   . SER A 258 ? 0.1698 0.1398 0.1705 -0.0045 -0.0153 -0.0006 258 SER A O   
2208 C CB  . SER A 258 ? 0.1653 0.1332 0.1611 -0.0101 -0.0099 0.0017  258 SER A CB  
2209 O OG  . SER A 258 ? 0.2096 0.1809 0.2015 -0.0106 -0.0096 0.0035  258 SER A OG  
2210 N N   . VAL A 259 ? 0.1655 0.1340 0.1611 -0.0037 -0.0152 0.0052  259 VAL A N   
2211 C CA  . VAL A 259 ? 0.1566 0.1304 0.1513 -0.0021 -0.0187 0.0041  259 VAL A CA  
2212 C C   . VAL A 259 ? 0.1701 0.1470 0.1576 -0.0020 -0.0190 0.0063  259 VAL A C   
2213 O O   . VAL A 259 ? 0.1913 0.1657 0.1757 -0.0030 -0.0165 0.0100  259 VAL A O   
2214 C CB  . VAL A 259 ? 0.1913 0.1666 0.1909 -0.0001 -0.0213 0.0058  259 VAL A CB  
2215 C CG1 . VAL A 259 ? 0.1940 0.1678 0.2005 -0.0005 -0.0205 0.0037  259 VAL A CG1 
2216 C CG2 . VAL A 259 ? 0.1993 0.1717 0.1981 0.0022  -0.0204 0.0114  259 VAL A CG2 
2217 N N   . SER A 260 ? 0.1643 0.1463 0.1486 -0.0014 -0.0217 0.0035  260 SER A N   
2218 C CA  . SER A 260 ? 0.1410 0.1277 0.1173 -0.0009 -0.0226 0.0049  260 SER A CA  
2219 C C   . SER A 260 ? 0.1623 0.1533 0.1373 -0.0005 -0.0272 0.0011  260 SER A C   
2220 O O   . SER A 260 ? 0.1832 0.1726 0.1635 -0.0012 -0.0288 -0.0028 260 SER A O   
2221 C CB  . SER A 260 ? 0.2009 0.1899 0.1723 -0.0017 -0.0192 0.0030  260 SER A CB  
2222 O OG  . SER A 260 ? 0.1872 0.1767 0.1594 -0.0010 -0.0194 -0.0034 260 SER A OG  
2223 N N   . ASN A 261 ? 0.1622 0.1586 0.1293 0.0001  -0.0294 0.0023  261 ASN A N   
2224 C CA  . ASN A 261 ? 0.1534 0.1543 0.1177 -0.0006 -0.0342 -0.0024 261 ASN A CA  
2225 C C   . ASN A 261 ? 0.2017 0.1988 0.1651 -0.0017 -0.0332 -0.0106 261 ASN A C   
2226 O O   . ASN A 261 ? 0.1978 0.1931 0.1647 -0.0036 -0.0362 -0.0150 261 ASN A O   
2227 C CB  . ASN A 261 ? 0.1887 0.1966 0.1422 0.0000  -0.0364 -0.0004 261 ASN A CB  
2228 C CG  . ASN A 261 ? 0.2097 0.2215 0.1644 0.0020  -0.0387 0.0084  261 ASN A CG  
2229 O OD1 . ASN A 261 ? 0.2091 0.2197 0.1732 0.0030  -0.0398 0.0115  261 ASN A OD1 
2230 N ND2 . ASN A 261 ? 0.2358 0.2522 0.1807 0.0031  -0.0389 0.0128  261 ASN A ND2 
2231 N N   . GLU A 262 ? 0.1760 0.1714 0.1354 -0.0005 -0.0286 -0.0122 262 GLU A N   
2232 C CA  . GLU A 262 ? 0.1905 0.1815 0.1485 0.0001  -0.0271 -0.0195 262 GLU A CA  
2233 C C   . GLU A 262 ? 0.1901 0.1746 0.1578 -0.0005 -0.0265 -0.0204 262 GLU A C   
2234 O O   . GLU A 262 ? 0.2119 0.1908 0.1801 -0.0010 -0.0274 -0.0258 262 GLU A O   
2235 C CB  . GLU A 262 ? 0.2001 0.1936 0.1527 0.0027  -0.0220 -0.0202 262 GLU A CB  
2236 C CG  . GLU A 262 ? 0.2179 0.2178 0.1589 0.0033  -0.0222 -0.0208 262 GLU A CG  
2237 C CD  . GLU A 262 ? 0.3129 0.3171 0.2489 0.0061  -0.0164 -0.0218 262 GLU A CD  
2238 O OE1 . GLU A 262 ? 0.3961 0.3971 0.3349 0.0087  -0.0135 -0.0262 262 GLU A OE1 
2239 O OE2 . GLU A 262 ? 0.3404 0.3517 0.2700 0.0059  -0.0146 -0.0176 262 GLU A OE2 
2240 N N   . ALA A 263 ? 0.1640 0.1482 0.1386 -0.0007 -0.0247 -0.0151 263 ALA A N   
2241 C CA  . ALA A 263 ? 0.1729 0.1520 0.1555 -0.0012 -0.0240 -0.0155 263 ALA A CA  
2242 C C   . ALA A 263 ? 0.1865 0.1642 0.1738 -0.0035 -0.0278 -0.0165 263 ALA A C   
2243 O O   . ALA A 263 ? 0.1841 0.1567 0.1747 -0.0046 -0.0280 -0.0195 263 ALA A O   
2244 C CB  . ALA A 263 ? 0.1786 0.1578 0.1658 -0.0014 -0.0213 -0.0105 263 ALA A CB  
2245 N N   . LEU A 264 ? 0.1899 0.1728 0.1779 -0.0043 -0.0308 -0.0134 264 LEU A N   
2246 C CA  . LEU A 264 ? 0.1616 0.1469 0.1553 -0.0067 -0.0347 -0.0140 264 LEU A CA  
2247 C C   . LEU A 264 ? 0.1909 0.1741 0.1805 -0.0096 -0.0377 -0.0207 264 LEU A C   
2248 O O   . LEU A 264 ? 0.2089 0.1897 0.2040 -0.0130 -0.0393 -0.0229 264 LEU A O   
2249 C CB  . LEU A 264 ? 0.1639 0.1574 0.1587 -0.0058 -0.0377 -0.0090 264 LEU A CB  
2250 C CG  . LEU A 264 ? 0.1765 0.1692 0.1763 -0.0030 -0.0346 -0.0027 264 LEU A CG  
2251 C CD1 . LEU A 264 ? 0.1988 0.1977 0.1974 -0.0005 -0.0369 0.0030  264 LEU A CD1 
2252 C CD2 . LEU A 264 ? 0.2651 0.2565 0.2747 -0.0037 -0.0335 -0.0023 264 LEU A CD2 
2253 N N   . GLU A 265 ? 0.1816 0.1650 0.1611 -0.0087 -0.0380 -0.0243 265 GLU A N   
2254 C CA  . GLU A 265 ? 0.1784 0.1573 0.1520 -0.0113 -0.0402 -0.0321 265 GLU A CA  
2255 C C   . GLU A 265 ? 0.2243 0.1916 0.2000 -0.0110 -0.0369 -0.0358 265 GLU A C   
2256 O O   . GLU A 265 ? 0.2527 0.2132 0.2288 -0.0148 -0.0389 -0.0407 265 GLU A O   
2257 C CB  . GLU A 265 ? 0.1871 0.1688 0.1482 -0.0094 -0.0401 -0.0352 265 GLU A CB  
2258 C CG  . GLU A 265 ? 0.2241 0.2173 0.1813 -0.0101 -0.0444 -0.0314 265 GLU A CG  
2259 C CD  . GLU A 265 ? 0.3245 0.3214 0.2685 -0.0078 -0.0432 -0.0328 265 GLU A CD  
2260 O OE1 . GLU A 265 ? 0.3763 0.3686 0.3158 -0.0047 -0.0380 -0.0352 265 GLU A OE1 
2261 O OE2 . GLU A 265 ? 0.4108 0.4166 0.3488 -0.0087 -0.0474 -0.0310 265 GLU A OE2 
2262 N N   . LEU A 266 ? 0.1901 0.1549 0.1671 -0.0067 -0.0320 -0.0333 266 LEU A N   
2263 C CA  . LEU A 266 ? 0.2005 0.1553 0.1795 -0.0051 -0.0289 -0.0354 266 LEU A CA  
2264 C C   . LEU A 266 ? 0.1816 0.1328 0.1698 -0.0086 -0.0299 -0.0330 266 LEU A C   
2265 O O   . LEU A 266 ? 0.2129 0.1544 0.2016 -0.0104 -0.0299 -0.0363 266 LEU A O   
2266 C CB  . LEU A 266 ? 0.1790 0.1359 0.1585 -0.0001 -0.0242 -0.0322 266 LEU A CB  
2267 C CG  . LEU A 266 ? 0.1729 0.1217 0.1554 0.0028  -0.0212 -0.0327 266 LEU A CG  
2268 C CD1 . LEU A 266 ? 0.2106 0.1490 0.1866 0.0048  -0.0205 -0.0395 266 LEU A CD1 
2269 C CD2 . LEU A 266 ? 0.2288 0.1840 0.2132 0.0069  -0.0176 -0.0286 266 LEU A CD2 
2270 N N   . TYR A 267 ? 0.1685 0.1268 0.1635 -0.0093 -0.0301 -0.0272 267 TYR A N   
2271 C CA  . TYR A 267 ? 0.1673 0.1243 0.1709 -0.0124 -0.0303 -0.0246 267 TYR A CA  
2272 C C   . TYR A 267 ? 0.1927 0.1488 0.1980 -0.0181 -0.0343 -0.0280 267 TYR A C   
2273 O O   . TYR A 267 ? 0.2107 0.1597 0.2196 -0.0214 -0.0339 -0.0289 267 TYR A O   
2274 C CB  . TYR A 267 ? 0.1810 0.1460 0.1904 -0.0116 -0.0296 -0.0188 267 TYR A CB  
2275 C CG  . TYR A 267 ? 0.1893 0.1535 0.1984 -0.0080 -0.0256 -0.0157 267 TYR A CG  
2276 C CD1 . TYR A 267 ? 0.1964 0.1555 0.2074 -0.0074 -0.0230 -0.0149 267 TYR A CD1 
2277 C CD2 . TYR A 267 ? 0.1623 0.1311 0.1687 -0.0060 -0.0247 -0.0132 267 TYR A CD2 
2278 C CE1 . TYR A 267 ? 0.2006 0.1609 0.2112 -0.0051 -0.0201 -0.0124 267 TYR A CE1 
2279 C CE2 . TYR A 267 ? 0.1931 0.1614 0.1992 -0.0043 -0.0214 -0.0110 267 TYR A CE2 
2280 C CZ  . TYR A 267 ? 0.1829 0.1479 0.1911 -0.0040 -0.0194 -0.0109 267 TYR A CZ  
2281 O OH  . TYR A 267 ? 0.1798 0.1462 0.1874 -0.0031 -0.0169 -0.0089 267 TYR A OH  
2282 N N   . TYR A 268 ? 0.2041 0.1678 0.2067 -0.0199 -0.0384 -0.0296 268 TYR A N   
2283 C CA  . TYR A 268 ? 0.1830 0.1479 0.1873 -0.0266 -0.0430 -0.0333 268 TYR A CA  
2284 C C   . TYR A 268 ? 0.2271 0.1779 0.2247 -0.0292 -0.0429 -0.0406 268 TYR A C   
2285 O O   . TYR A 268 ? 0.2316 0.1768 0.2332 -0.0353 -0.0442 -0.0427 268 TYR A O   
2286 C CB  . TYR A 268 ? 0.2324 0.2096 0.2337 -0.0276 -0.0481 -0.0335 268 TYR A CB  
2287 C CG  . TYR A 268 ? 0.3035 0.2835 0.3054 -0.0354 -0.0537 -0.0384 268 TYR A CG  
2288 C CD1 . TYR A 268 ? 0.2961 0.2833 0.3097 -0.0408 -0.0559 -0.0357 268 TYR A CD1 
2289 C CD2 . TYR A 268 ? 0.3486 0.3244 0.3391 -0.0380 -0.0566 -0.0461 268 TYR A CD2 
2290 C CE1 . TYR A 268 ? 0.3062 0.2973 0.3212 -0.0495 -0.0614 -0.0402 268 TYR A CE1 
2291 C CE2 . TYR A 268 ? 0.3818 0.3598 0.3721 -0.0466 -0.0623 -0.0515 268 TYR A CE2 
2292 C CZ  . TYR A 268 ? 0.3588 0.3449 0.3619 -0.0528 -0.0649 -0.0483 268 TYR A CZ  
2293 O OH  . TYR A 268 ? 0.4391 0.4289 0.4428 -0.0627 -0.0709 -0.0536 268 TYR A OH  
2294 N N   . GLU A 269 ? 0.2237 0.1682 0.2111 -0.0246 -0.0408 -0.0447 269 GLU A N   
2295 C CA  . GLU A 269 ? 0.2238 0.1529 0.2037 -0.0256 -0.0399 -0.0522 269 GLU A CA  
2296 C C   . GLU A 269 ? 0.2164 0.1328 0.2016 -0.0253 -0.0363 -0.0504 269 GLU A C   
2297 O O   . GLU A 269 ? 0.2701 0.1722 0.2523 -0.0289 -0.0364 -0.0554 269 GLU A O   
2298 C CB  . GLU A 269 ? 0.3487 0.2752 0.3178 -0.0188 -0.0369 -0.0559 269 GLU A CB  
2299 C CG  . GLU A 269 ? 0.6170 0.5521 0.5768 -0.0199 -0.0404 -0.0599 269 GLU A CG  
2300 C CD  . GLU A 269 ? 0.7957 0.7355 0.7482 -0.0126 -0.0366 -0.0592 269 GLU A CD  
2301 O OE1 . GLU A 269 ? 0.7901 0.7399 0.7359 -0.0128 -0.0389 -0.0594 269 GLU A OE1 
2302 O OE2 . GLU A 269 ? 0.8355 0.7703 0.7891 -0.0067 -0.0314 -0.0578 269 GLU A OE2 
2303 N N   . LYS A 270 ? 0.2341 0.1548 0.2262 -0.0214 -0.0331 -0.0431 270 LYS A N   
2304 C CA  . LYS A 270 ? 0.2293 0.1399 0.2257 -0.0205 -0.0298 -0.0399 270 LYS A CA  
2305 C C   . LYS A 270 ? 0.2481 0.1611 0.2539 -0.0273 -0.0311 -0.0360 270 LYS A C   
2306 O O   . LYS A 270 ? 0.2850 0.1916 0.2947 -0.0270 -0.0282 -0.0319 270 LYS A O   
2307 C CB  . LYS A 270 ? 0.2404 0.1553 0.2381 -0.0130 -0.0258 -0.0346 270 LYS A CB  
2308 C CG  . LYS A 270 ? 0.2834 0.1968 0.2731 -0.0063 -0.0237 -0.0380 270 LYS A CG  
2309 C CD  . LYS A 270 ? 0.4163 0.3133 0.4001 -0.0042 -0.0221 -0.0435 270 LYS A CD  
2310 C CE  . LYS A 270 ? 0.4919 0.3890 0.4678 0.0032  -0.0194 -0.0474 270 LYS A CE  
2311 N NZ  . LYS A 270 ? 0.6110 0.4903 0.5797 0.0054  -0.0177 -0.0544 270 LYS A NZ  
2312 N N   . GLY A 271 ? 0.2183 0.1415 0.2279 -0.0334 -0.0353 -0.0368 271 GLY A N   
2313 C CA  . GLY A 271 ? 0.2487 0.1755 0.2679 -0.0404 -0.0364 -0.0335 271 GLY A CA  
2314 C C   . GLY A 271 ? 0.2330 0.1740 0.2612 -0.0386 -0.0350 -0.0263 271 GLY A C   
2315 O O   . GLY A 271 ? 0.2429 0.1877 0.2796 -0.0435 -0.0345 -0.0228 271 GLY A O   
2316 N N   . ILE A 272 ? 0.2265 0.1749 0.2528 -0.0321 -0.0339 -0.0240 272 ILE A N   
2317 C CA  . ILE A 272 ? 0.1859 0.1458 0.2194 -0.0299 -0.0323 -0.0180 272 ILE A CA  
2318 C C   . ILE A 272 ? 0.2030 0.1769 0.2422 -0.0329 -0.0365 -0.0175 272 ILE A C   
2319 O O   . ILE A 272 ? 0.2526 0.2306 0.2871 -0.0324 -0.0402 -0.0202 272 ILE A O   
2320 C CB  . ILE A 272 ? 0.2340 0.1948 0.2630 -0.0227 -0.0296 -0.0161 272 ILE A CB  
2321 C CG1 . ILE A 272 ? 0.2733 0.2232 0.2973 -0.0196 -0.0262 -0.0164 272 ILE A CG1 
2322 C CG2 . ILE A 272 ? 0.2407 0.2105 0.2757 -0.0206 -0.0276 -0.0109 272 ILE A CG2 
2323 C CD1 . ILE A 272 ? 0.3415 0.2860 0.3696 -0.0217 -0.0238 -0.0135 272 ILE A CD1 
2324 N N   . ASN A 273 ? 0.1941 0.1769 0.2436 -0.0356 -0.0358 -0.0135 273 ASN A N   
2325 C CA  . ASN A 273 ? 0.2367 0.2354 0.2937 -0.0378 -0.0398 -0.0120 273 ASN A CA  
2326 C C   . ASN A 273 ? 0.1904 0.1990 0.2505 -0.0306 -0.0381 -0.0072 273 ASN A C   
2327 O O   . ASN A 273 ? 0.1968 0.2180 0.2605 -0.0297 -0.0419 -0.0057 273 ASN A O   
2328 C CB  . ASN A 273 ? 0.2632 0.2686 0.3312 -0.0450 -0.0399 -0.0102 273 ASN A CB  
2329 C CG  . ASN A 273 ? 0.3849 0.3810 0.4504 -0.0538 -0.0427 -0.0154 273 ASN A CG  
2330 O OD1 . ASN A 273 ? 0.4003 0.3887 0.4565 -0.0547 -0.0459 -0.0211 273 ASN A OD1 
2331 N ND2 . ASN A 273 ? 0.4071 0.4030 0.4802 -0.0606 -0.0411 -0.0135 273 ASN A ND2 
2332 N N   . MET A 274 ? 0.2150 0.2179 0.2735 -0.0256 -0.0328 -0.0046 274 MET A N   
2333 C CA  . MET A 274 ? 0.1465 0.1555 0.2072 -0.0192 -0.0305 -0.0006 274 MET A CA  
2334 C C   . MET A 274 ? 0.1541 0.1521 0.2070 -0.0149 -0.0262 -0.0006 274 MET A C   
2335 O O   . MET A 274 ? 0.1746 0.1645 0.2250 -0.0163 -0.0235 -0.0016 274 MET A O   
2336 C CB  . MET A 274 ? 0.1736 0.1930 0.2456 -0.0189 -0.0278 0.0034  274 MET A CB  
2337 C CG  . MET A 274 ? 0.1750 0.1999 0.2495 -0.0113 -0.0253 0.0072  274 MET A CG  
2338 S SD  . MET A 274 ? 0.2972 0.3101 0.3655 -0.0068 -0.0180 0.0075  274 MET A SD  
2339 C CE  . MET A 274 ? 0.2577 0.2793 0.3363 -0.0080 -0.0133 0.0101  274 MET A CE  
2340 N N   . LEU A 275 ? 0.1463 0.1444 0.1956 -0.0099 -0.0257 0.0009  275 LEU A N   
2341 C CA  . LEU A 275 ? 0.1358 0.1258 0.1794 -0.0066 -0.0215 0.0014  275 LEU A CA  
2342 C C   . LEU A 275 ? 0.1330 0.1257 0.1784 -0.0016 -0.0196 0.0047  275 LEU A C   
2343 O O   . LEU A 275 ? 0.1435 0.1448 0.1943 0.0003  -0.0218 0.0072  275 LEU A O   
2344 C CB  . LEU A 275 ? 0.2050 0.1880 0.2393 -0.0067 -0.0224 -0.0011 275 LEU A CB  
2345 C CG  . LEU A 275 ? 0.2501 0.2358 0.2800 -0.0060 -0.0262 -0.0016 275 LEU A CG  
2346 C CD1 . LEU A 275 ? 0.2329 0.2189 0.2606 -0.0020 -0.0250 0.0020  275 LEU A CD1 
2347 C CD2 . LEU A 275 ? 0.2667 0.2468 0.2889 -0.0072 -0.0267 -0.0053 275 LEU A CD2 
2348 N N   . ALA A 276 ? 0.1465 0.1315 0.1873 0.0005  -0.0155 0.0048  276 ALA A N   
2349 C CA  . ALA A 276 ? 0.1689 0.1515 0.2088 0.0053  -0.0132 0.0073  276 ALA A CA  
2350 C C   . ALA A 276 ? 0.1604 0.1342 0.1912 0.0051  -0.0126 0.0067  276 ALA A C   
2351 O O   . ALA A 276 ? 0.1511 0.1215 0.1771 0.0019  -0.0128 0.0042  276 ALA A O   
2352 C CB  . ALA A 276 ? 0.1656 0.1464 0.2082 0.0077  -0.0079 0.0076  276 ALA A CB  
2353 N N   . THR A 277 ? 0.1626 0.1330 0.1916 0.0088  -0.0117 0.0096  277 THR A N   
2354 C CA  . THR A 277 ? 0.1399 0.1013 0.1605 0.0077  -0.0105 0.0097  277 THR A CA  
2355 C C   . THR A 277 ? 0.1739 0.1269 0.1934 0.0119  -0.0069 0.0124  277 THR A C   
2356 O O   . THR A 277 ? 0.1807 0.1343 0.2052 0.0157  -0.0045 0.0129  277 THR A O   
2357 C CB  . THR A 277 ? 0.1650 0.1302 0.1819 0.0065  -0.0144 0.0108  277 THR A CB  
2358 O OG1 . THR A 277 ? 0.1785 0.1365 0.1881 0.0049  -0.0127 0.0117  277 THR A OG1 
2359 C CG2 . THR A 277 ? 0.1932 0.1651 0.2134 0.0104  -0.0176 0.0150  277 THR A CG2 
2360 N N   . ASP A 278 ? 0.1612 0.1060 0.1740 0.0113  -0.0061 0.0143  278 ASP A N   
2361 C CA  . ASP A 278 ? 0.1814 0.1133 0.1910 0.0140  -0.0019 0.0159  278 ASP A CA  
2362 C C   . ASP A 278 ? 0.2172 0.1478 0.2278 0.0202  -0.0026 0.0223  278 ASP A C   
2363 O O   . ASP A 278 ? 0.1999 0.1377 0.2100 0.0205  -0.0066 0.0258  278 ASP A O   
2364 C CB  . ASP A 278 ? 0.2144 0.1359 0.2157 0.0081  0.0002  0.0140  278 ASP A CB  
2365 C CG  . ASP A 278 ? 0.2471 0.1521 0.2439 0.0095  0.0048  0.0146  278 ASP A CG  
2366 O OD1 . ASP A 278 ? 0.2391 0.1393 0.2373 0.0125  0.0081  0.0120  278 ASP A OD1 
2367 O OD2 . ASP A 278 ? 0.2602 0.1564 0.2515 0.0077  0.0055  0.0177  278 ASP A OD2 
2368 N N   . GLU A 279 ? 0.1896 0.1493 0.2112 0.0022  -0.0043 0.0173  279 GLU A N   
2369 C CA  . GLU A 279 ? 0.1950 0.1529 0.2104 0.0045  -0.0011 0.0209  279 GLU A CA  
2370 C C   . GLU A 279 ? 0.2300 0.1862 0.2443 0.0021  0.0030  0.0230  279 GLU A C   
2371 O O   . GLU A 279 ? 0.2577 0.2133 0.2648 0.0044  0.0051  0.0262  279 GLU A O   
2372 C CB  . GLU A 279 ? 0.2526 0.2022 0.2626 0.0068  -0.0016 0.0219  279 GLU A CB  
2373 C CG  . GLU A 279 ? 0.2757 0.2234 0.2788 0.0124  -0.0006 0.0247  279 GLU A CG  
2374 C CD  . GLU A 279 ? 0.2438 0.1866 0.2430 0.0171  -0.0016 0.0237  279 GLU A CD  
2375 O OE1 . GLU A 279 ? 0.2325 0.1723 0.2327 0.0150  -0.0023 0.0211  279 GLU A OE1 
2376 O OE2 . GLU A 279 ? 0.2655 0.2073 0.2599 0.0239  -0.0021 0.0250  279 GLU A OE2 
2377 N N   . VAL A 280 ? 0.2154 0.1710 0.2360 -0.0031 0.0043  0.0213  280 VAL A N   
2378 C CA  . VAL A 280 ? 0.2020 0.1573 0.2216 -0.0081 0.0101  0.0231  280 VAL A CA  
2379 C C   . VAL A 280 ? 0.1932 0.1599 0.2138 -0.0070 0.0128  0.0220  280 VAL A C   
2380 O O   . VAL A 280 ? 0.2281 0.1926 0.2398 -0.0085 0.0178  0.0256  280 VAL A O   
2381 C CB  . VAL A 280 ? 0.1903 0.1479 0.2203 -0.0153 0.0112  0.0195  280 VAL A CB  
2382 C CG1 . VAL A 280 ? 0.2060 0.1668 0.2363 -0.0228 0.0191  0.0207  280 VAL A CG1 
2383 C CG2 . VAL A 280 ? 0.2474 0.1911 0.2738 -0.0169 0.0084  0.0201  280 VAL A CG2 
2384 N N   . ILE A 281 ? 0.1792 0.1558 0.2080 -0.0043 0.0092  0.0171  281 ILE A N   
2385 C CA  . ILE A 281 ? 0.1652 0.1513 0.1940 -0.0024 0.0111  0.0146  281 ILE A CA  
2386 C C   . ILE A 281 ? 0.1654 0.1480 0.1817 0.0015  0.0108  0.0185  281 ILE A C   
2387 O O   . ILE A 281 ? 0.2034 0.1890 0.2126 0.0017  0.0145  0.0193  281 ILE A O   
2388 C CB  . ILE A 281 ? 0.1985 0.1911 0.2367 0.0007  0.0059  0.0082  281 ILE A CB  
2389 C CG1 . ILE A 281 ? 0.1788 0.1770 0.2302 -0.0014 0.0048  0.0035  281 ILE A CG1 
2390 C CG2 . ILE A 281 ? 0.1982 0.1987 0.2354 0.0035  0.0074  0.0045  281 ILE A CG2 
2391 C CD1 . ILE A 281 ? 0.2150 0.2163 0.2738 0.0036  -0.0022 -0.0027 281 ILE A CD1 
2392 N N   . LEU A 282 ? 0.1940 0.1717 0.2072 0.0046  0.0063  0.0202  282 LEU A N   
2393 C CA  . LEU A 282 ? 0.2066 0.1842 0.2106 0.0089  0.0048  0.0227  282 LEU A CA  
2394 C C   . LEU A 282 ? 0.2112 0.1808 0.2029 0.0098  0.0082  0.0284  282 LEU A C   
2395 O O   . LEU A 282 ? 0.2282 0.1995 0.2105 0.0121  0.0089  0.0297  282 LEU A O   
2396 C CB  . LEU A 282 ? 0.1851 0.1619 0.1904 0.0116  0.0007  0.0226  282 LEU A CB  
2397 C CG  . LEU A 282 ? 0.2290 0.2103 0.2287 0.0170  -0.0019 0.0235  282 LEU A CG  
2398 C CD1 . LEU A 282 ? 0.2241 0.2152 0.2245 0.0168  -0.0038 0.0199  282 LEU A CD1 
2399 C CD2 . LEU A 282 ? 0.2502 0.2339 0.2537 0.0191  -0.0042 0.0223  282 LEU A CD2 
2400 N N   . LYS A 283 ? 0.2133 0.1714 0.2026 0.0077  0.0100  0.0318  283 LYS A N   
2401 C CA  . LYS A 283 ? 0.2492 0.1934 0.2231 0.0081  0.0127  0.0381  283 LYS A CA  
2402 C C   . LYS A 283 ? 0.2383 0.1836 0.2064 0.0020  0.0196  0.0397  283 LYS A C   
2403 O O   . LYS A 283 ? 0.2663 0.2016 0.2168 0.0032  0.0215  0.0453  283 LYS A O   
2404 C CB  . LYS A 283 ? 0.3040 0.2328 0.2761 0.0058  0.0131  0.0406  283 LYS A CB  
2405 C CG  . LYS A 283 ? 0.3624 0.2912 0.3405 0.0109  0.0078  0.0378  283 LYS A CG  
2406 C CD  . LYS A 283 ? 0.4431 0.3690 0.4125 0.0211  0.0034  0.0396  283 LYS A CD  
2407 C CE  . LYS A 283 ? 0.4380 0.3745 0.4175 0.0253  -0.0003 0.0345  283 LYS A CE  
2408 N NZ  . LYS A 283 ? 0.5062 0.4356 0.4798 0.0345  -0.0035 0.0348  283 LYS A NZ  
2409 N N   . ASN A 284 ? 0.2184 0.1755 0.1999 -0.0041 0.0234  0.0346  284 ASN A N   
2410 C CA  . ASN A 284 ? 0.1918 0.1553 0.1706 -0.0100 0.0313  0.0341  284 ASN A CA  
2411 C C   . ASN A 284 ? 0.2227 0.1945 0.1942 -0.0050 0.0309  0.0323  284 ASN A C   
2412 O O   . ASN A 284 ? 0.2388 0.2127 0.2006 -0.0086 0.0379  0.0333  284 ASN A O   
2413 C CB  . ASN A 284 ? 0.2267 0.2050 0.2254 -0.0155 0.0342  0.0268  284 ASN A CB  
2414 C CG  . ASN A 284 ? 0.2384 0.2108 0.2433 -0.0236 0.0367  0.0277  284 ASN A CG  
2415 O OD1 . ASN A 284 ? 0.2562 0.2107 0.2481 -0.0270 0.0385  0.0344  284 ASN A OD1 
2416 N ND2 . ASN A 284 ? 0.2061 0.1928 0.2306 -0.0265 0.0362  0.0203  284 ASN A ND2 
2417 N N   . SER A 285 ? 0.2283 0.2051 0.2036 0.0021  0.0233  0.0292  285 SER A N   
2418 C CA  . SER A 285 ? 0.2116 0.1979 0.1836 0.0061  0.0215  0.0249  285 SER A CA  
2419 C C   . SER A 285 ? 0.2380 0.2194 0.1946 0.0124  0.0165  0.0285  285 SER A C   
2420 O O   . SER A 285 ? 0.2976 0.2834 0.2442 0.0143  0.0169  0.0268  285 SER A O   
2421 C CB  . SER A 285 ? 0.2163 0.2117 0.2039 0.0081  0.0162  0.0174  285 SER A CB  
2422 O OG  . SER A 285 ? 0.2013 0.2015 0.2032 0.0045  0.0186  0.0134  285 SER A OG  
2423 N N   . VAL A 286 ? 0.2475 0.2217 0.2026 0.0165  0.0111  0.0323  286 VAL A N   
2424 C CA  . VAL A 286 ? 0.2938 0.2674 0.2378 0.0242  0.0045  0.0339  286 VAL A CA  
2425 C C   . VAL A 286 ? 0.3773 0.3347 0.3087 0.0285  0.0029  0.0414  286 VAL A C   
2426 O O   . VAL A 286 ? 0.3884 0.3360 0.3235 0.0255  0.0055  0.0441  286 VAL A O   
2427 C CB  . VAL A 286 ? 0.3285 0.3148 0.2859 0.0274  -0.0026 0.0278  286 VAL A CB  
2428 C CG1 . VAL A 286 ? 0.3923 0.3885 0.3611 0.0227  -0.0017 0.0207  286 VAL A CG1 
2429 C CG2 . VAL A 286 ? 0.3155 0.2993 0.2826 0.0283  -0.0044 0.0287  286 VAL A CG2 
2430 N N   . GLU A 287 ? 0.3995 0.3531 0.3151 0.0365  -0.0026 0.0442  287 GLU A N   
2431 C CA  . GLU A 287 ? 0.4056 0.3409 0.3065 0.0434  -0.0061 0.0511  287 GLU A CA  
2432 C C   . GLU A 287 ? 0.3973 0.3390 0.3116 0.0510  -0.0131 0.0476  287 GLU A C   
2433 O O   . GLU A 287 ? 0.3893 0.3180 0.3037 0.0523  -0.0125 0.0503  287 GLU A O   
2434 C CB  . GLU A 287 ? 0.5207 0.4475 0.3967 0.0506  -0.0105 0.0557  287 GLU A CB  
2435 C CG  . GLU A 287 ? 0.6732 0.5827 0.5274 0.0431  -0.0018 0.0630  287 GLU A CG  
2436 C CD  . GLU A 287 ? 0.7922 0.7007 0.6238 0.0476  -0.0047 0.0649  287 GLU A CD  
2437 O OE1 . GLU A 287 ? 0.8468 0.7611 0.6751 0.0593  -0.0159 0.0627  287 GLU A OE1 
2438 O OE2 . GLU A 287 ? 0.8710 0.7745 0.6884 0.0396  0.0043  0.0677  287 GLU A OE2 
2439 N N   . ARG A 288 ? 0.4421 0.4043 0.3679 0.0555  -0.0192 0.0409  288 ARG A N   
2440 C CA  . ARG A 288 ? 0.3978 0.3711 0.3379 0.0620  -0.0246 0.0362  288 ARG A CA  
2441 C C   . ARG A 288 ? 0.3925 0.3759 0.3523 0.0527  -0.0197 0.0314  288 ARG A C   
2442 O O   . ARG A 288 ? 0.4703 0.4704 0.4421 0.0483  -0.0204 0.0255  288 ARG A O   
2443 C CB  . ARG A 288 ? 0.5195 0.5116 0.4625 0.0701  -0.0335 0.0309  288 ARG A CB  
2444 C CG  . ARG A 288 ? 0.5231 0.5038 0.4428 0.0799  -0.0398 0.0359  288 ARG A CG  
2445 C CD  . ARG A 288 ? 0.5181 0.5200 0.4410 0.0872  -0.0496 0.0293  288 ARG A CD  
2446 N NE  . ARG A 288 ? 0.4646 0.4797 0.3926 0.0779  -0.0476 0.0243  288 ARG A NE  
2447 C CZ  . ARG A 288 ? 0.5076 0.5434 0.4573 0.0708  -0.0470 0.0159  288 ARG A CZ  
2448 N NH1 . ARG A 288 ? 0.5575 0.6002 0.5085 0.0632  -0.0459 0.0114  288 ARG A NH1 
2449 N NH2 . ARG A 288 ? 0.5983 0.6464 0.5669 0.0710  -0.0473 0.0118  288 ARG A NH2 
2450 N N   . ALA A 289 ? 0.3277 0.2984 0.2890 0.0494  -0.0152 0.0340  289 ALA A N   
2451 C CA  . ALA A 289 ? 0.2760 0.2503 0.2502 0.0398  -0.0104 0.0312  289 ALA A CA  
2452 C C   . ALA A 289 ? 0.2392 0.2186 0.2240 0.0414  -0.0112 0.0277  289 ALA A C   
2453 O O   . ALA A 289 ? 0.3233 0.2919 0.3083 0.0392  -0.0086 0.0289  289 ALA A O   
2454 C CB  . ALA A 289 ? 0.3969 0.3552 0.3651 0.0332  -0.0045 0.0357  289 ALA A CB  
2455 N N   . SER A 290 ? 0.2080 0.2058 0.2021 0.0441  -0.0145 0.0224  290 SER A N   
2456 C CA  . SER A 290 ? 0.1880 0.1940 0.1924 0.0435  -0.0133 0.0181  290 SER A CA  
2457 C C   . SER A 290 ? 0.1511 0.1592 0.1624 0.0323  -0.0097 0.0163  290 SER A C   
2458 O O   . SER A 290 ? 0.1877 0.2034 0.2022 0.0271  -0.0103 0.0143  290 SER A O   
2459 C CB  . SER A 290 ? 0.2117 0.2394 0.2251 0.0493  -0.0170 0.0123  290 SER A CB  
2460 O OG  . SER A 290 ? 0.2088 0.2462 0.2319 0.0468  -0.0138 0.0078  290 SER A OG  
2461 N N   . PRO A 291 ? 0.1720 0.1721 0.1839 0.0291  -0.0068 0.0166  291 PRO A N   
2462 C CA  . PRO A 291 ? 0.1560 0.1558 0.1714 0.0199  -0.0048 0.0152  291 PRO A CA  
2463 C C   . PRO A 291 ? 0.1635 0.1769 0.1849 0.0160  -0.0036 0.0110  291 PRO A C   
2464 O O   . PRO A 291 ? 0.1677 0.1770 0.1882 0.0082  -0.0021 0.0106  291 PRO A O   
2465 C CB  . PRO A 291 ? 0.1862 0.1714 0.1976 0.0190  -0.0033 0.0171  291 PRO A CB  
2466 C CG  . PRO A 291 ? 0.1816 0.1649 0.1904 0.0269  -0.0033 0.0168  291 PRO A CG  
2467 C CD  . PRO A 291 ? 0.1882 0.1764 0.1953 0.0341  -0.0060 0.0180  291 PRO A CD  
2468 N N   . TYR A 292 ? 0.1488 0.1785 0.1759 0.0208  -0.0043 0.0075  292 TYR A N   
2469 C CA  . TYR A 292 ? 0.1416 0.1875 0.1760 0.0159  -0.0013 0.0025  292 TYR A CA  
2470 C C   . TYR A 292 ? 0.1221 0.1821 0.1631 0.0088  -0.0026 -0.0007 292 TYR A C   
2471 O O   . TYR A 292 ? 0.1443 0.2206 0.1928 0.0028  0.0004  -0.0054 292 TYR A O   
2472 C CB  . TYR A 292 ? 0.1479 0.2069 0.1875 0.0257  -0.0009 -0.0015 292 TYR A CB  
2473 C CG  . TYR A 292 ? 0.1858 0.2278 0.2173 0.0316  0.0003  0.0009  292 TYR A CG  
2474 C CD1 . TYR A 292 ? 0.2663 0.2934 0.2909 0.0245  0.0033  0.0032  292 TYR A CD1 
2475 C CD2 . TYR A 292 ? 0.2775 0.3161 0.3068 0.0446  -0.0028 0.0005  292 TYR A CD2 
2476 C CE1 . TYR A 292 ? 0.3403 0.3519 0.3576 0.0290  0.0036  0.0043  292 TYR A CE1 
2477 C CE2 . TYR A 292 ? 0.3269 0.3468 0.3476 0.0490  -0.0020 0.0021  292 TYR A CE2 
2478 C CZ  . TYR A 292 ? 0.3561 0.3639 0.3717 0.0406  0.0013  0.0036  292 TYR A CZ  
2479 O OH  . TYR A 292 ? 0.5248 0.5145 0.5321 0.0441  0.0013  0.0040  292 TYR A OH  
2480 N N   . LEU A 293 ? 0.1358 0.1896 0.1737 0.0085  -0.0064 0.0010  293 LEU A N   
2481 C CA  . LEU A 293 ? 0.1437 0.2074 0.1858 0.0024  -0.0088 -0.0027 293 LEU A CA  
2482 C C   . LEU A 293 ? 0.1286 0.1763 0.1649 -0.0074 -0.0080 -0.0011 293 LEU A C   
2483 O O   . LEU A 293 ? 0.1637 0.1939 0.1929 -0.0063 -0.0074 0.0030  293 LEU A O   
2484 C CB  . LEU A 293 ? 0.1637 0.2305 0.2037 0.0104  -0.0143 -0.0027 293 LEU A CB  
2485 C CG  . LEU A 293 ? 0.2355 0.3196 0.2803 0.0209  -0.0187 -0.0056 293 LEU A CG  
2486 C CD1 . LEU A 293 ? 0.2216 0.3103 0.2699 0.0287  -0.0168 -0.0058 293 LEU A CD1 
2487 C CD2 . LEU A 293 ? 0.2341 0.3087 0.2677 0.0292  -0.0233 -0.0020 293 LEU A CD2 
2488 N N   . ARG A 294 ? 0.1472 0.2007 0.1865 -0.0167 -0.0087 -0.0051 294 ARG A N   
2489 C CA  . ARG A 294 ? 0.1608 0.1967 0.1928 -0.0236 -0.0103 -0.0046 294 ARG A CA  
2490 C C   . ARG A 294 ? 0.1372 0.1732 0.1677 -0.0179 -0.0150 -0.0064 294 ARG A C   
2491 O O   . ARG A 294 ? 0.1558 0.2074 0.1913 -0.0173 -0.0180 -0.0109 294 ARG A O   
2492 C CB  . ARG A 294 ? 0.1761 0.2130 0.2089 -0.0374 -0.0089 -0.0079 294 ARG A CB  
2493 C CG  . ARG A 294 ? 0.2106 0.2238 0.2330 -0.0437 -0.0117 -0.0075 294 ARG A CG  
2494 C CD  . ARG A 294 ? 0.1992 0.2060 0.2176 -0.0594 -0.0092 -0.0087 294 ARG A CD  
2495 N NE  . ARG A 294 ? 0.2388 0.2672 0.2680 -0.0672 -0.0091 -0.0154 294 ARG A NE  
2496 C CZ  . ARG A 294 ? 0.2442 0.2894 0.2807 -0.0778 -0.0036 -0.0178 294 ARG A CZ  
2497 N NH1 . ARG A 294 ? 0.2217 0.2632 0.2535 -0.0820 0.0031  -0.0137 294 ARG A NH1 
2498 N NH2 . ARG A 294 ? 0.2500 0.3178 0.2989 -0.0846 -0.0046 -0.0253 294 ARG A NH2 
2499 N N   . TYR A 295 ? 0.1514 0.1722 0.1752 -0.0135 -0.0157 -0.0036 295 TYR A N   
2500 C CA  . TYR A 295 ? 0.1436 0.1642 0.1640 -0.0085 -0.0185 -0.0056 295 TYR A CA  
2501 C C   . TYR A 295 ? 0.1932 0.2032 0.2099 -0.0140 -0.0212 -0.0100 295 TYR A C   
2502 O O   . TYR A 295 ? 0.1876 0.1833 0.2015 -0.0194 -0.0211 -0.0093 295 TYR A O   
2503 C CB  . TYR A 295 ? 0.1640 0.1773 0.1805 -0.0011 -0.0165 -0.0013 295 TYR A CB  
2504 C CG  . TYR A 295 ? 0.1654 0.1852 0.1820 0.0053  -0.0150 0.0027  295 TYR A CG  
2505 C CD1 . TYR A 295 ? 0.1510 0.1688 0.1701 0.0055  -0.0126 0.0058  295 TYR A CD1 
2506 C CD2 . TYR A 295 ? 0.1885 0.2139 0.2001 0.0116  -0.0165 0.0032  295 TYR A CD2 
2507 C CE1 . TYR A 295 ? 0.1768 0.1972 0.1946 0.0124  -0.0119 0.0088  295 TYR A CE1 
2508 C CE2 . TYR A 295 ? 0.1816 0.2080 0.1902 0.0184  -0.0162 0.0074  295 TYR A CE2 
2509 C CZ  . TYR A 295 ? 0.1942 0.2177 0.2065 0.0190  -0.0140 0.0099  295 TYR A CZ  
2510 O OH  . TYR A 295 ? 0.1843 0.2056 0.1922 0.0267  -0.0145 0.0134  295 TYR A OH  
2511 N N   . TYR A 296 ? 0.1917 0.2068 0.2063 -0.0120 -0.0243 -0.0146 296 TYR A N   
2512 C CA  . TYR A 296 ? 0.1747 0.1783 0.1843 -0.0150 -0.0274 -0.0201 296 TYR A CA  
2513 C C   . TYR A 296 ? 0.1701 0.1719 0.1744 -0.0062 -0.0270 -0.0213 296 TYR A C   
2514 O O   . TYR A 296 ? 0.1983 0.2111 0.1996 -0.0018 -0.0276 -0.0225 296 TYR A O   
2515 C CB  . TYR A 296 ? 0.1850 0.1966 0.1960 -0.0220 -0.0315 -0.0267 296 TYR A CB  
2516 C CG  . TYR A 296 ? 0.2205 0.2385 0.2384 -0.0328 -0.0304 -0.0267 296 TYR A CG  
2517 C CD1 . TYR A 296 ? 0.2937 0.2945 0.3082 -0.0417 -0.0285 -0.0245 296 TYR A CD1 
2518 C CD2 . TYR A 296 ? 0.3520 0.3937 0.3792 -0.0344 -0.0314 -0.0295 296 TYR A CD2 
2519 C CE1 . TYR A 296 ? 0.2396 0.2469 0.2589 -0.0536 -0.0256 -0.0245 296 TYR A CE1 
2520 C CE2 . TYR A 296 ? 0.3206 0.3726 0.3564 -0.0452 -0.0290 -0.0308 296 TYR A CE2 
2521 C CZ  . TYR A 296 ? 0.3508 0.3854 0.3820 -0.0556 -0.0252 -0.0281 296 TYR A CZ  
2522 O OH  . TYR A 296 ? 0.3232 0.3684 0.3613 -0.0680 -0.0210 -0.0294 296 TYR A OH  
2523 N N   . PHE A 297 ? 0.1821 0.1710 0.1847 -0.0035 -0.0259 -0.0213 297 PHE A N   
2524 C CA  . PHE A 297 ? 0.1456 0.1354 0.1449 0.0037  -0.0242 -0.0243 297 PHE A CA  
2525 C C   . PHE A 297 ? 0.1699 0.1571 0.1631 0.0035  -0.0282 -0.0329 297 PHE A C   
2526 O O   . PHE A 297 ? 0.1884 0.1614 0.1798 0.0009  -0.0320 -0.0377 297 PHE A O   
2527 C CB  . PHE A 297 ? 0.1533 0.1337 0.1558 0.0072  -0.0229 -0.0239 297 PHE A CB  
2528 C CG  . PHE A 297 ? 0.1676 0.1527 0.1696 0.0141  -0.0199 -0.0286 297 PHE A CG  
2529 C CD1 . PHE A 297 ? 0.2008 0.1977 0.2031 0.0165  -0.0136 -0.0249 297 PHE A CD1 
2530 C CD2 . PHE A 297 ? 0.1741 0.1514 0.1745 0.0179  -0.0229 -0.0370 297 PHE A CD2 
2531 C CE1 . PHE A 297 ? 0.2087 0.2122 0.2104 0.0211  -0.0089 -0.0295 297 PHE A CE1 
2532 C CE2 . PHE A 297 ? 0.2107 0.1960 0.2119 0.0247  -0.0189 -0.0428 297 PHE A CE2 
2533 C CZ  . PHE A 297 ? 0.2072 0.2071 0.2095 0.0255  -0.0112 -0.0390 297 PHE A CZ  
2534 N N   . ARG A 298 ? 0.1850 0.1837 0.1729 0.0065  -0.0278 -0.0349 298 ARG A N   
2535 C CA  . ARG A 298 ? 0.1889 0.1870 0.1690 0.0072  -0.0316 -0.0440 298 ARG A CA  
2536 C C   . ARG A 298 ? 0.1749 0.1663 0.1560 -0.0014 -0.0381 -0.0491 298 ARG A C   
2537 O O   . ARG A 298 ? 0.2321 0.2141 0.2075 -0.0022 -0.0420 -0.0577 298 ARG A O   
2538 C CB  . ARG A 298 ? 0.2372 0.2281 0.2136 0.0135  -0.0294 -0.0500 298 ARG A CB  
2539 C CG  . ARG A 298 ? 0.2164 0.2171 0.1925 0.0193  -0.0216 -0.0457 298 ARG A CG  
2540 C CD  . ARG A 298 ? 0.2409 0.2410 0.2157 0.0257  -0.0180 -0.0533 298 ARG A CD  
2541 N NE  . ARG A 298 ? 0.2321 0.2436 0.2077 0.0282  -0.0091 -0.0486 298 ARG A NE  
2542 C CZ  . ARG A 298 ? 0.2376 0.2550 0.2163 0.0328  -0.0031 -0.0538 298 ARG A CZ  
2543 N NH1 . ARG A 298 ? 0.2452 0.2579 0.2266 0.0381  -0.0059 -0.0646 298 ARG A NH1 
2544 N NH2 . ARG A 298 ? 0.2341 0.2622 0.2133 0.0320  0.0059  -0.0488 298 ARG A NH2 
2545 N N   . GLU A 299 ? 0.1887 0.1848 0.1772 -0.0083 -0.0386 -0.0443 299 GLU A N   
2546 C CA  . GLU A 299 ? 0.2218 0.2143 0.2130 -0.0196 -0.0428 -0.0481 299 GLU A CA  
2547 C C   . GLU A 299 ? 0.2632 0.2304 0.2500 -0.0243 -0.0444 -0.0503 299 GLU A C   
2548 O O   . GLU A 299 ? 0.2808 0.2385 0.2652 -0.0344 -0.0483 -0.0552 299 GLU A O   
2549 C CB  . GLU A 299 ? 0.2050 0.2082 0.1935 -0.0219 -0.0484 -0.0566 299 GLU A CB  
2550 C CG  . GLU A 299 ? 0.2428 0.2694 0.2335 -0.0161 -0.0490 -0.0544 299 GLU A CG  
2551 C CD  . GLU A 299 ? 0.3350 0.3740 0.3235 -0.0182 -0.0564 -0.0633 299 GLU A CD  
2552 O OE1 . GLU A 299 ? 0.4896 0.5470 0.4878 -0.0223 -0.0596 -0.0642 299 GLU A OE1 
2553 O OE2 . GLU A 299 ? 0.3733 0.4051 0.3508 -0.0153 -0.0593 -0.0703 299 GLU A OE2 
2554 N N   . LEU A 300 ? 0.2043 0.1595 0.1895 -0.0175 -0.0420 -0.0467 300 LEU A N   
2555 C CA  . LEU A 300 ? 0.2405 0.1694 0.2192 -0.0181 -0.0454 -0.0493 300 LEU A CA  
2556 C C   . LEU A 300 ? 0.2643 0.1807 0.2434 -0.0209 -0.0441 -0.0414 300 LEU A C   
2557 O O   . LEU A 300 ? 0.3525 0.2454 0.3236 -0.0273 -0.0477 -0.0415 300 LEU A O   
2558 C CB  . LEU A 300 ? 0.2742 0.1989 0.2499 -0.0053 -0.0458 -0.0550 300 LEU A CB  
2559 C CG  . LEU A 300 ? 0.4280 0.3576 0.3982 -0.0010 -0.0476 -0.0651 300 LEU A CG  
2560 C CD1 . LEU A 300 ? 0.5018 0.4298 0.4712 0.0120  -0.0458 -0.0703 300 LEU A CD1 
2561 C CD2 . LEU A 300 ? 0.3945 0.3066 0.3567 -0.0092 -0.0543 -0.0726 300 LEU A CD2 
2562 N N   . ILE A 301 ? 0.2271 0.1558 0.2130 -0.0163 -0.0396 -0.0345 301 ILE A N   
2563 C CA  . ILE A 301 ? 0.2215 0.1388 0.2064 -0.0179 -0.0389 -0.0276 301 ILE A CA  
2564 C C   . ILE A 301 ? 0.2068 0.1432 0.1993 -0.0202 -0.0334 -0.0210 301 ILE A C   
2565 O O   . ILE A 301 ? 0.2469 0.2017 0.2455 -0.0147 -0.0304 -0.0205 301 ILE A O   
2566 C CB  . ILE A 301 ? 0.2844 0.1924 0.2692 -0.0067 -0.0409 -0.0282 301 ILE A CB  
2567 C CG1 . ILE A 301 ? 0.2861 0.1817 0.2679 -0.0079 -0.0418 -0.0214 301 ILE A CG1 
2568 C CG2 . ILE A 301 ? 0.2566 0.1862 0.2506 0.0022  -0.0363 -0.0291 301 ILE A CG2 
2569 C CD1 . ILE A 301 ? 0.2904 0.1776 0.2733 0.0036  -0.0460 -0.0232 301 ILE A CD1 
2570 N N   . SER A 302 ? 0.1979 0.1282 0.1880 -0.0284 -0.0320 -0.0160 302 SER A N   
2571 C CA  . SER A 302 ? 0.1920 0.1389 0.1888 -0.0296 -0.0269 -0.0108 302 SER A CA  
2572 C C   . SER A 302 ? 0.1869 0.1323 0.1852 -0.0214 -0.0256 -0.0064 302 SER A C   
2573 O O   . SER A 302 ? 0.2007 0.1291 0.1934 -0.0187 -0.0287 -0.0055 302 SER A O   
2574 C CB  . SER A 302 ? 0.2060 0.1488 0.1993 -0.0420 -0.0246 -0.0084 302 SER A CB  
2575 O OG  . SER A 302 ? 0.2570 0.2064 0.2523 -0.0513 -0.0252 -0.0134 302 SER A OG  
2576 N N   . VAL A 303 ? 0.1760 0.1383 0.1812 -0.0173 -0.0218 -0.0040 303 VAL A N   
2577 C CA  . VAL A 303 ? 0.1513 0.1136 0.1588 -0.0110 -0.0202 -0.0004 303 VAL A CA  
2578 C C   . VAL A 303 ? 0.1570 0.1292 0.1673 -0.0123 -0.0162 0.0035  303 VAL A C   
2579 O O   . VAL A 303 ? 0.1679 0.1544 0.1823 -0.0117 -0.0145 0.0028  303 VAL A O   
2580 C CB  . VAL A 303 ? 0.1666 0.1369 0.1783 -0.0034 -0.0192 -0.0021 303 VAL A CB  
2581 C CG1 . VAL A 303 ? 0.2090 0.1797 0.2242 0.0005  -0.0170 0.0012  303 VAL A CG1 
2582 C CG2 . VAL A 303 ? 0.1786 0.1418 0.1884 -0.0006 -0.0225 -0.0078 303 VAL A CG2 
2583 N N   . PHE A 304 ? 0.1742 0.1384 0.1816 -0.0130 -0.0156 0.0067  304 PHE A N   
2584 C CA  . PHE A 304 ? 0.1589 0.1309 0.1684 -0.0120 -0.0119 0.0093  304 PHE A CA  
2585 C C   . PHE A 304 ? 0.1676 0.1367 0.1789 -0.0059 -0.0120 0.0111  304 PHE A C   
2586 O O   . PHE A 304 ? 0.1797 0.1398 0.1901 -0.0044 -0.0149 0.0106  304 PHE A O   
2587 C CB  . PHE A 304 ? 0.1792 0.1454 0.1825 -0.0184 -0.0102 0.0109  304 PHE A CB  
2588 C CG  . PHE A 304 ? 0.1826 0.1575 0.1867 -0.0264 -0.0076 0.0090  304 PHE A CG  
2589 C CD1 . PHE A 304 ? 0.2122 0.2072 0.2246 -0.0254 -0.0040 0.0070  304 PHE A CD1 
2590 C CD2 . PHE A 304 ? 0.1876 0.1504 0.1843 -0.0352 -0.0090 0.0085  304 PHE A CD2 
2591 C CE1 . PHE A 304 ? 0.1959 0.2038 0.2124 -0.0337 -0.0014 0.0037  304 PHE A CE1 
2592 C CE2 . PHE A 304 ? 0.2016 0.1735 0.2000 -0.0454 -0.0057 0.0061  304 PHE A CE2 
2593 C CZ  . PHE A 304 ? 0.2030 0.1998 0.2128 -0.0450 -0.0016 0.0033  304 PHE A CZ  
2594 N N   . PHE A 305 ? 0.1787 0.1553 0.1927 -0.0024 -0.0092 0.0126  305 PHE A N   
2595 C CA  . PHE A 305 ? 0.1827 0.1552 0.1976 0.0011  -0.0085 0.0144  305 PHE A CA  
2596 C C   . PHE A 305 ? 0.1616 0.1302 0.1733 0.0007  -0.0074 0.0155  305 PHE A C   
2597 O O   . PHE A 305 ? 0.1756 0.1507 0.1869 0.0017  -0.0051 0.0153  305 PHE A O   
2598 C CB  . PHE A 305 ? 0.1553 0.1336 0.1715 0.0052  -0.0064 0.0156  305 PHE A CB  
2599 C CG  . PHE A 305 ? 0.1527 0.1351 0.1697 0.0057  -0.0068 0.0140  305 PHE A CG  
2600 C CD1 . PHE A 305 ? 0.1864 0.1762 0.2026 0.0056  -0.0081 0.0120  305 PHE A CD1 
2601 C CD2 . PHE A 305 ? 0.1667 0.1476 0.1859 0.0060  -0.0058 0.0132  305 PHE A CD2 
2602 C CE1 . PHE A 305 ? 0.1635 0.1562 0.1786 0.0064  -0.0087 0.0095  305 PHE A CE1 
2603 C CE2 . PHE A 305 ? 0.1600 0.1457 0.1791 0.0070  -0.0053 0.0106  305 PHE A CE2 
2604 C CZ  . PHE A 305 ? 0.1651 0.1554 0.1810 0.0075  -0.0070 0.0088  305 PHE A CZ  
2605 N N   . ARG A 306 ? 0.1444 0.1038 0.1541 0.0000  -0.0095 0.0156  306 ARG A N   
2606 C CA  . ARG A 306 ? 0.1386 0.0929 0.1428 -0.0005 -0.0089 0.0158  306 ARG A CA  
2607 C C   . ARG A 306 ? 0.1597 0.1158 0.1650 0.0036  -0.0062 0.0162  306 ARG A C   
2608 O O   . ARG A 306 ? 0.1657 0.1219 0.1743 0.0058  -0.0056 0.0173  306 ARG A O   
2609 C CB  . ARG A 306 ? 0.1582 0.1021 0.1594 -0.0013 -0.0134 0.0152  306 ARG A CB  
2610 C CG  . ARG A 306 ? 0.1872 0.1309 0.1953 0.0004  -0.0146 0.0142  306 ARG A CG  
2611 C CD  . ARG A 306 ? 0.2009 0.1376 0.2078 0.0000  -0.0203 0.0120  306 ARG A CD  
2612 N NE  . ARG A 306 ? 0.1615 0.1013 0.1775 -0.0004 -0.0204 0.0101  306 ARG A NE  
2613 C CZ  . ARG A 306 ? 0.1627 0.0993 0.1806 -0.0014 -0.0247 0.0071  306 ARG A CZ  
2614 N NH1 . ARG A 306 ? 0.2063 0.1350 0.2152 -0.0005 -0.0304 0.0060  306 ARG A NH1 
2615 N NH2 . ARG A 306 ? 0.1662 0.1074 0.1939 -0.0040 -0.0233 0.0051  306 ARG A NH2 
2616 N N   . ASP A 307 ? 0.1738 0.1297 0.1744 0.0046  -0.0042 0.0152  307 ASP A N   
2617 C CA  . ASP A 307 ? 0.1365 0.0888 0.1356 0.0095  -0.0029 0.0146  307 ASP A CA  
2618 C C   . ASP A 307 ? 0.1581 0.0981 0.1548 0.0077  -0.0056 0.0142  307 ASP A C   
2619 O O   . ASP A 307 ? 0.2043 0.1390 0.1952 0.0056  -0.0073 0.0125  307 ASP A O   
2620 C CB  . ASP A 307 ? 0.1775 0.1354 0.1731 0.0119  0.0002  0.0118  307 ASP A CB  
2621 C CG  . ASP A 307 ? 0.2105 0.1641 0.2043 0.0194  0.0008  0.0102  307 ASP A CG  
2622 O OD1 . ASP A 307 ? 0.2252 0.1648 0.2151 0.0195  -0.0011 0.0105  307 ASP A OD1 
2623 O OD2 . ASP A 307 ? 0.2686 0.2327 0.2652 0.0255  0.0026  0.0080  307 ASP A OD2 
2624 N N   . LYS A 308 ? 0.1687 0.1045 0.1689 0.0077  -0.0061 0.0156  308 LYS A N   
2625 C CA  . LYS A 308 ? 0.1704 0.0982 0.1719 0.0041  -0.0087 0.0141  308 LYS A CA  
2626 C C   . LYS A 308 ? 0.1787 0.0958 0.1728 0.0054  -0.0095 0.0116  308 LYS A C   
2627 O O   . LYS A 308 ? 0.2131 0.1253 0.2055 0.0027  -0.0132 0.0087  308 LYS A O   
2628 C CB  . LYS A 308 ? 0.2141 0.1412 0.2210 0.0017  -0.0071 0.0159  308 LYS A CB  
2629 C CG  . LYS A 308 ? 0.2294 0.1515 0.2406 -0.0037 -0.0089 0.0134  308 LYS A CG  
2630 C CD  . LYS A 308 ? 0.2462 0.1702 0.2627 -0.0081 -0.0049 0.0155  308 LYS A CD  
2631 C CE  . LYS A 308 ? 0.2740 0.1923 0.2947 -0.0154 -0.0052 0.0128  308 LYS A CE  
2632 N NZ  . LYS A 308 ? 0.3493 0.2759 0.3790 -0.0170 -0.0111 0.0071  308 LYS A NZ  
2633 N N   . THR A 309 ? 0.1931 0.1062 0.1823 0.0106  -0.0069 0.0118  309 THR A N   
2634 C CA  . THR A 309 ? 0.2041 0.1053 0.1854 0.0132  -0.0076 0.0082  309 THR A CA  
2635 C C   . THR A 309 ? 0.2282 0.1321 0.2035 0.0129  -0.0083 0.0046  309 THR A C   
2636 O O   . THR A 309 ? 0.2133 0.1082 0.1831 0.0107  -0.0115 0.0012  309 THR A O   
2637 C CB  . THR A 309 ? 0.2424 0.1397 0.2195 0.0215  -0.0053 0.0084  309 THR A CB  
2638 O OG1 . THR A 309 ? 0.3065 0.1941 0.2834 0.0207  -0.0053 0.0125  309 THR A OG1 
2639 C CG2 . THR A 309 ? 0.2854 0.1712 0.2535 0.0262  -0.0059 0.0031  309 THR A CG2 
2640 N N   . LEU A 310 ? 0.2180 0.1341 0.1933 0.0142  -0.0054 0.0051  310 LEU A N   
2641 C CA  . LEU A 310 ? 0.1944 0.1120 0.1609 0.0123  -0.0045 0.0026  310 LEU A CA  
2642 C C   . LEU A 310 ? 0.1993 0.1107 0.1623 0.0066  -0.0099 0.0036  310 LEU A C   
2643 O O   . LEU A 310 ? 0.2229 0.1266 0.1748 0.0055  -0.0122 0.0010  310 LEU A O   
2644 C CB  . LEU A 310 ? 0.1918 0.1244 0.1601 0.0119  0.0006  0.0033  310 LEU A CB  
2645 C CG  . LEU A 310 ? 0.2078 0.1504 0.1801 0.0195  0.0051  0.0002  310 LEU A CG  
2646 C CD1 . LEU A 310 ? 0.2481 0.2094 0.2266 0.0172  0.0093  0.0003  310 LEU A CD1 
2647 C CD2 . LEU A 310 ? 0.2408 0.1798 0.2041 0.0237  0.0075  -0.0057 310 LEU A CD2 
2648 N N   . SER A 311 ? 0.1899 0.1046 0.1615 0.0039  -0.0125 0.0067  311 SER A N   
2649 C CA  . SER A 311 ? 0.1828 0.0927 0.1527 0.0008  -0.0191 0.0068  311 SER A CA  
2650 C C   . SER A 311 ? 0.1984 0.1007 0.1687 0.0004  -0.0244 0.0030  311 SER A C   
2651 O O   . SER A 311 ? 0.2338 0.1297 0.1957 -0.0003 -0.0304 0.0009  311 SER A O   
2652 C CB  . SER A 311 ? 0.1800 0.0966 0.1610 -0.0002 -0.0205 0.0092  311 SER A CB  
2653 O OG  . SER A 311 ? 0.1761 0.0993 0.1569 -0.0007 -0.0162 0.0118  311 SER A OG  
2654 N N   . ASP A 312 ? 0.1887 0.0903 0.1670 0.0004  -0.0226 0.0021  312 ASP A N   
2655 C CA  . ASP A 312 ? 0.2166 0.1115 0.1971 -0.0024 -0.0274 -0.0021 312 ASP A CA  
2656 C C   . ASP A 312 ? 0.2205 0.1038 0.1882 -0.0007 -0.0280 -0.0062 312 ASP A C   
2657 O O   . ASP A 312 ? 0.2213 0.0981 0.1877 -0.0034 -0.0338 -0.0110 312 ASP A O   
2658 C CB  . ASP A 312 ? 0.2048 0.1007 0.1969 -0.0055 -0.0246 -0.0010 312 ASP A CB  
2659 C CG  . ASP A 312 ? 0.2047 0.1131 0.2109 -0.0085 -0.0256 -0.0001 312 ASP A CG  
2660 O OD1 . ASP A 312 ? 0.2827 0.1972 0.2908 -0.0072 -0.0305 -0.0011 312 ASP A OD1 
2661 O OD2 . ASP A 312 ? 0.2905 0.2013 0.3046 -0.0119 -0.0215 0.0015  312 ASP A OD2 
2662 N N   . LEU A 313 ? 0.2125 0.0943 0.1711 0.0039  -0.0225 -0.0059 313 LEU A N   
2663 C CA  . LEU A 313 ? 0.2237 0.0958 0.1683 0.0065  -0.0229 -0.0112 313 LEU A CA  
2664 C C   . LEU A 313 ? 0.2270 0.0966 0.1603 0.0043  -0.0285 -0.0132 313 LEU A C   
2665 O O   . LEU A 313 ? 0.2559 0.1159 0.1810 0.0036  -0.0338 -0.0186 313 LEU A O   
2666 C CB  . LEU A 313 ? 0.2424 0.1189 0.1815 0.0126  -0.0154 -0.0115 313 LEU A CB  
2667 C CG  . LEU A 313 ? 0.2420 0.1150 0.1864 0.0180  -0.0121 -0.0116 313 LEU A CG  
2668 C CD1 . LEU A 313 ? 0.2437 0.1286 0.1879 0.0250  -0.0056 -0.0121 313 LEU A CD1 
2669 C CD2 . LEU A 313 ? 0.2709 0.1257 0.2079 0.0196  -0.0150 -0.0172 313 LEU A CD2 
2670 N N   . ILE A 314 ? 0.2471 0.1233 0.1778 0.0032  -0.0280 -0.0089 314 ILE A N   
2671 C CA  . ILE A 314 ? 0.2366 0.1066 0.1524 0.0017  -0.0340 -0.0093 314 ILE A CA  
2672 C C   . ILE A 314 ? 0.2406 0.1086 0.1639 0.0003  -0.0449 -0.0114 314 ILE A C   
2673 O O   . ILE A 314 ? 0.2771 0.1372 0.1896 0.0004  -0.0528 -0.0156 314 ILE A O   
2674 C CB  . ILE A 314 ? 0.2303 0.1041 0.1401 0.0000  -0.0305 -0.0034 314 ILE A CB  
2675 C CG1 . ILE A 314 ? 0.2602 0.1405 0.1646 0.0004  -0.0193 -0.0032 314 ILE A CG1 
2676 C CG2 . ILE A 314 ? 0.2721 0.1346 0.1632 -0.0013 -0.0382 -0.0022 314 ILE A CG2 
2677 C CD1 . ILE A 314 ? 0.2578 0.1427 0.1571 -0.0041 -0.0144 0.0021  314 ILE A CD1 
2678 N N   . GLY A 315 ? 0.2192 0.0962 0.1618 -0.0008 -0.0456 -0.0095 315 GLY A N   
2679 C CA  . GLY A 315 ? 0.2229 0.1034 0.1762 -0.0019 -0.0553 -0.0125 315 GLY A CA  
2680 C C   . GLY A 315 ? 0.2302 0.1092 0.1905 -0.0049 -0.0593 -0.0193 315 GLY A C   
2681 O O   . GLY A 315 ? 0.2490 0.1297 0.2125 -0.0055 -0.0695 -0.0243 315 GLY A O   
2682 N N   . PHE A 316 ? 0.2111 0.0859 0.1733 -0.0068 -0.0523 -0.0199 316 PHE A N   
2683 C CA  . PHE A 316 ? 0.2305 0.1018 0.2008 -0.0120 -0.0552 -0.0258 316 PHE A CA  
2684 C C   . PHE A 316 ? 0.2891 0.1444 0.2450 -0.0115 -0.0542 -0.0303 316 PHE A C   
2685 O O   . PHE A 316 ? 0.3191 0.1683 0.2760 -0.0159 -0.0602 -0.0371 316 PHE A O   
2686 C CB  . PHE A 316 ? 0.2389 0.1163 0.2265 -0.0167 -0.0488 -0.0229 316 PHE A CB  
2687 C CG  . PHE A 316 ? 0.2217 0.1164 0.2268 -0.0185 -0.0508 -0.0219 316 PHE A CG  
2688 C CD1 . PHE A 316 ? 0.2798 0.1845 0.3003 -0.0240 -0.0572 -0.0283 316 PHE A CD1 
2689 C CD2 . PHE A 316 ? 0.2163 0.1188 0.2234 -0.0144 -0.0466 -0.0159 316 PHE A CD2 
2690 C CE1 . PHE A 316 ? 0.2742 0.1974 0.3122 -0.0241 -0.0589 -0.0290 316 PHE A CE1 
2691 C CE2 . PHE A 316 ? 0.2441 0.1616 0.2664 -0.0147 -0.0487 -0.0164 316 PHE A CE2 
2692 C CZ  . PHE A 316 ? 0.2268 0.1553 0.2648 -0.0188 -0.0546 -0.0231 316 PHE A CZ  
2693 N N   A SER A 317 ? 0.2532 0.1024 0.1964 -0.0060 -0.0469 -0.0277 317 SER A N   
2694 N N   B SER A 317 ? 0.2473 0.0966 0.1907 -0.0060 -0.0469 -0.0277 317 SER A N   
2695 C CA  A SER A 317 ? 0.2524 0.0865 0.1832 -0.0036 -0.0451 -0.0329 317 SER A CA  
2696 C CA  B SER A 317 ? 0.2523 0.0865 0.1830 -0.0035 -0.0450 -0.0328 317 SER A CA  
2697 C C   A SER A 317 ? 0.2902 0.1185 0.2006 0.0002  -0.0479 -0.0378 317 SER A C   
2698 C C   B SER A 317 ? 0.2942 0.1227 0.2048 0.0001  -0.0481 -0.0377 317 SER A C   
2699 O O   A SER A 317 ? 0.3108 0.1274 0.2123 -0.0009 -0.0533 -0.0454 317 SER A O   
2700 O O   B SER A 317 ? 0.3053 0.1226 0.2074 -0.0012 -0.0539 -0.0453 317 SER A O   
2701 C CB  A SER A 317 ? 0.2781 0.1102 0.2087 0.0018  -0.0357 -0.0291 317 SER A CB  
2702 C CB  B SER A 317 ? 0.2671 0.0996 0.1971 0.0022  -0.0354 -0.0290 317 SER A CB  
2703 O OG  A SER A 317 ? 0.2989 0.1141 0.2193 0.0052  -0.0348 -0.0348 317 SER A OG  
2704 O OG  B SER A 317 ? 0.2374 0.0727 0.1818 -0.0009 -0.0326 -0.0238 317 SER A OG  
2705 N N   . TYR A 318 ? 0.2781 0.1135 0.1794 0.0038  -0.0440 -0.0337 318 TYR A N   
2706 C CA  . TYR A 318 ? 0.2830 0.1124 0.1618 0.0074  -0.0424 -0.0377 318 TYR A CA  
2707 C C   . TYR A 318 ? 0.3046 0.1262 0.1690 0.0054  -0.0530 -0.0425 318 TYR A C   
2708 O O   . TYR A 318 ? 0.3346 0.1482 0.1779 0.0080  -0.0523 -0.0476 318 TYR A O   
2709 C CB  . TYR A 318 ? 0.2840 0.1235 0.1567 0.0090  -0.0343 -0.0317 318 TYR A CB  
2710 C CG  . TYR A 318 ? 0.2786 0.1274 0.1612 0.0128  -0.0237 -0.0295 318 TYR A CG  
2711 C CD1 . TYR A 318 ? 0.2678 0.1112 0.1553 0.0177  -0.0212 -0.0339 318 TYR A CD1 
2712 C CD2 . TYR A 318 ? 0.2940 0.1558 0.1798 0.0119  -0.0173 -0.0235 318 TYR A CD2 
2713 C CE1 . TYR A 318 ? 0.2697 0.1219 0.1652 0.0234  -0.0133 -0.0324 318 TYR A CE1 
2714 C CE2 . TYR A 318 ? 0.2497 0.1227 0.1454 0.0158  -0.0090 -0.0226 318 TYR A CE2 
2715 C CZ  . TYR A 318 ? 0.2830 0.1521 0.1838 0.0224  -0.0075 -0.0271 318 TYR A CZ  
2716 O OH  . TYR A 318 ? 0.2834 0.1645 0.1937 0.0281  -0.0009 -0.0266 318 TYR A OH  
2717 N N   . HIS A 319 ? 0.3142 0.1390 0.1889 0.0016  -0.0632 -0.0420 319 HIS A N   
2718 C CA  . HIS A 319 ? 0.3156 0.1336 0.1765 0.0011  -0.0754 -0.0476 319 HIS A CA  
2719 C C   . HIS A 319 ? 0.3899 0.1957 0.2420 0.0007  -0.0784 -0.0579 319 HIS A C   
2720 O O   . HIS A 319 ? 0.4154 0.2160 0.2496 0.0022  -0.0842 -0.0620 319 HIS A O   
2721 C CB  . HIS A 319 ? 0.3249 0.1519 0.2038 -0.0017 -0.0867 -0.0478 319 HIS A CB  
2722 C CG  . HIS A 319 ? 0.3715 0.2031 0.2740 -0.0074 -0.0884 -0.0528 319 HIS A CG  
2723 N ND1 . HIS A 319 ? 0.3769 0.2163 0.2998 -0.0103 -0.0800 -0.0481 319 HIS A ND1 
2724 C CD2 . HIS A 319 ? 0.3875 0.2218 0.2980 -0.0114 -0.0942 -0.0598 319 HIS A CD2 
2725 C CE1 . HIS A 319 ? 0.3811 0.2235 0.3203 -0.0169 -0.0814 -0.0527 319 HIS A CE1 
2726 N NE2 . HIS A 319 ? 0.4118 0.2528 0.3453 -0.0180 -0.0894 -0.0597 319 HIS A NE2 
2727 N N   . ALA A 320 ? 0.3576 0.1620 0.2241 -0.0011 -0.0730 -0.0598 320 ALA A N   
2728 C CA  . ALA A 320 ? 0.4351 0.2319 0.2993 -0.0020 -0.0735 -0.0672 320 ALA A CA  
2729 C C   . ALA A 320 ? 0.4900 0.2764 0.3364 0.0049  -0.0649 -0.0704 320 ALA A C   
2730 O O   . ALA A 320 ? 0.5242 0.3023 0.3669 0.0054  -0.0650 -0.0770 320 ALA A O   
2731 C CB  . ALA A 320 ? 0.4434 0.2423 0.3310 -0.0085 -0.0720 -0.0669 320 ALA A CB  
2732 N N   . TRP A 321 ? 0.3667 0.1543 0.2028 0.0101  -0.0572 -0.0669 321 TRP A N   
2733 C CA  . TRP A 321 ? 0.4351 0.2183 0.2567 0.0178  -0.0477 -0.0711 321 TRP A CA  
2734 C C   . TRP A 321 ? 0.4428 0.2260 0.2381 0.0197  -0.0467 -0.0736 321 TRP A C   
2735 O O   . TRP A 321 ? 0.5192 0.3060 0.3079 0.0158  -0.0521 -0.0687 321 TRP A O   
2736 C CB  . TRP A 321 ? 0.3791 0.1744 0.2129 0.0217  -0.0367 -0.0641 321 TRP A CB  
2737 C CG  . TRP A 321 ? 0.3959 0.1911 0.2517 0.0202  -0.0364 -0.0595 321 TRP A CG  
2738 C CD1 . TRP A 321 ? 0.4050 0.1967 0.2749 0.0126  -0.0436 -0.0575 321 TRP A CD1 
2739 C CD2 . TRP A 321 ? 0.4012 0.2008 0.2663 0.0264  -0.0282 -0.0565 321 TRP A CD2 
2740 N NE1 . TRP A 321 ? 0.4377 0.2303 0.3230 0.0128  -0.0391 -0.0522 321 TRP A NE1 
2741 C CE2 . TRP A 321 ? 0.3719 0.1671 0.2532 0.0220  -0.0308 -0.0516 321 TRP A CE2 
2742 C CE3 . TRP A 321 ? 0.3727 0.1810 0.2342 0.0355  -0.0191 -0.0580 321 TRP A CE3 
2743 C CZ2 . TRP A 321 ? 0.4162 0.2119 0.3066 0.0270  -0.0256 -0.0473 321 TRP A CZ2 
2744 C CZ3 . TRP A 321 ? 0.4083 0.2199 0.2824 0.0414  -0.0148 -0.0548 321 TRP A CZ3 
2745 C CH2 . TRP A 321 ? 0.3797 0.1833 0.2664 0.0374  -0.0186 -0.0490 321 TRP A CH2 
2746 N N   . ASN A 322 ? 0.4649 0.2465 0.2466 0.0260  -0.0388 -0.0801 322 ASN A N   
2747 C CA  . ASN A 322 ? 0.5363 0.3214 0.2930 0.0268  -0.0338 -0.0807 322 ASN A CA  
2748 C C   . ASN A 322 ? 0.5118 0.3140 0.2740 0.0266  -0.0218 -0.0725 322 ASN A C   
2749 O O   . ASN A 322 ? 0.5176 0.3297 0.3022 0.0287  -0.0166 -0.0688 322 ASN A O   
2750 C CB  . ASN A 322 ? 0.6812 0.4641 0.4243 0.0321  -0.0294 -0.0905 322 ASN A CB  
2751 C CG  . ASN A 322 ? 0.7604 0.5503 0.5102 0.0409  -0.0172 -0.0957 322 ASN A CG  
2752 O OD1 . ASN A 322 ? 0.8124 0.6142 0.5670 0.0433  -0.0077 -0.0922 322 ASN A OD1 
2753 N ND2 . ASN A 322 ? 0.8545 0.6377 0.6050 0.0462  -0.0179 -0.1047 322 ASN A ND2 
2754 N N   . ALA A 323 ? 0.3509 0.2402 0.2048 0.1124  0.0009  -0.0608 323 ALA A N   
2755 C CA  . ALA A 323 ? 0.3577 0.2760 0.2282 0.1087  0.0090  -0.0485 323 ALA A CA  
2756 C C   . ALA A 323 ? 0.3066 0.2339 0.1797 0.1231  0.0111  -0.0490 323 ALA A C   
2757 O O   . ALA A 323 ? 0.3355 0.2700 0.2216 0.1181  0.0135  -0.0397 323 ALA A O   
2758 C CB  . ALA A 323 ? 0.3594 0.3108 0.2335 0.1063  0.0155  -0.0436 323 ALA A CB  
2759 N N   . GLU A 324 ? 0.3600 0.2882 0.2211 0.1418  0.0096  -0.0605 324 GLU A N   
2760 C CA  . GLU A 324 ? 0.4759 0.4180 0.3431 0.1534  0.0104  -0.0595 324 GLU A CA  
2761 C C   . GLU A 324 ? 0.4481 0.3588 0.3164 0.1517  0.0031  -0.0584 324 GLU A C   
2762 O O   . GLU A 324 ? 0.4645 0.3860 0.3426 0.1546  0.0056  -0.0519 324 GLU A O   
2763 C CB  . GLU A 324 ? 0.6026 0.5581 0.4620 0.1676  0.0084  -0.0689 324 GLU A CB  
2764 C CG  . GLU A 324 ? 0.7531 0.7163 0.6156 0.1812  0.0065  -0.0705 324 GLU A CG  
2765 C CD  . GLU A 324 ? 0.8708 0.8778 0.7466 0.1846  0.0157  -0.0615 324 GLU A CD  
2766 O OE1 . GLU A 324 ? 0.8893 0.9174 0.7740 0.1746  0.0234  -0.0519 324 GLU A OE1 
2767 O OE2 . GLU A 324 ? 0.9257 0.9463 0.8033 0.1968  0.0146  -0.0637 324 GLU A OE2 
2768 N N   . ASP A 325 ? 0.4511 0.3252 0.3102 0.1457  -0.0064 -0.0633 325 ASP A N   
2769 C CA  . ASP A 325 ? 0.4961 0.3416 0.3563 0.1405  -0.0136 -0.0596 325 ASP A CA  
2770 C C   . ASP A 325 ? 0.4366 0.2858 0.3078 0.1299  -0.0088 -0.0481 325 ASP A C   
2771 O O   . ASP A 325 ? 0.4222 0.2710 0.2999 0.1316  -0.0095 -0.0423 325 ASP A O   
2772 C CB  . ASP A 325 ? 0.5508 0.3604 0.4011 0.1307  -0.0239 -0.0637 325 ASP A CB  
2773 C CG  . ASP A 325 ? 0.6353 0.4329 0.4744 0.1419  -0.0318 -0.0748 325 ASP A CG  
2774 O OD1 . ASP A 325 ? 0.5674 0.3844 0.4057 0.1582  -0.0294 -0.0802 325 ASP A OD1 
2775 O OD2 . ASP A 325 ? 0.6225 0.3915 0.4540 0.1341  -0.0411 -0.0779 325 ASP A OD2 
2776 N N   . ALA A 326 ? 0.3396 0.1964 0.2151 0.1165  -0.0044 -0.0437 326 ALA A N   
2777 C CA  . ALA A 326 ? 0.3112 0.1761 0.2007 0.1004  -0.0013 -0.0316 326 ALA A CA  
2778 C C   . ALA A 326 ? 0.3502 0.2467 0.2533 0.1045  0.0059  -0.0244 326 ALA A C   
2779 O O   . ALA A 326 ? 0.3102 0.2066 0.2214 0.1000  0.0055  -0.0174 326 ALA A O   
2780 C CB  . ALA A 326 ? 0.3020 0.1725 0.1951 0.0850  0.0008  -0.0290 326 ALA A CB  
2781 N N   . VAL A 327 ? 0.3083 0.2338 0.2140 0.1119  0.0120  -0.0254 327 VAL A N   
2782 C CA  . VAL A 327 ? 0.3067 0.2646 0.2264 0.1133  0.0181  -0.0172 327 VAL A CA  
2783 C C   . VAL A 327 ? 0.2923 0.2502 0.2122 0.1275  0.0163  -0.0187 327 VAL A C   
2784 O O   . VAL A 327 ? 0.3070 0.2762 0.2384 0.1239  0.0175  -0.0108 327 VAL A O   
2785 C CB  . VAL A 327 ? 0.3162 0.3075 0.2382 0.1166  0.0246  -0.0161 327 VAL A CB  
2786 C CG1 . VAL A 327 ? 0.2882 0.3140 0.2246 0.1179  0.0298  -0.0070 327 VAL A CG1 
2787 C CG2 . VAL A 327 ? 0.2798 0.2711 0.2036 0.1014  0.0254  -0.0122 327 VAL A CG2 
2788 N N   . ARG A 328 ? 0.2926 0.2377 0.1996 0.1447  0.0125  -0.0295 328 ARG A N   
2789 C CA  . ARG A 328 ? 0.3432 0.2849 0.2501 0.1572  0.0086  -0.0312 328 ARG A CA  
2790 C C   . ARG A 328 ? 0.3561 0.2711 0.2648 0.1492  0.0029  -0.0252 328 ARG A C   
2791 O O   . ARG A 328 ? 0.3405 0.2654 0.2573 0.1525  0.0028  -0.0196 328 ARG A O   
2792 C CB  . ARG A 328 ? 0.4657 0.3932 0.3594 0.1679  0.0019  -0.0428 328 ARG A CB  
2793 C CG  . ARG A 328 ? 0.5706 0.5332 0.4654 0.1814  0.0064  -0.0470 328 ARG A CG  
2794 C CD  . ARG A 328 ? 0.6737 0.6193 0.5559 0.1943  -0.0018 -0.0586 328 ARG A CD  
2795 N NE  . ARG A 328 ? 0.8049 0.7131 0.6748 0.1884  -0.0095 -0.0652 328 ARG A NE  
2796 C CZ  . ARG A 328 ? 0.8005 0.6734 0.6619 0.1901  -0.0202 -0.0698 328 ARG A CZ  
2797 N NH1 . ARG A 328 ? 0.8489 0.7170 0.7119 0.1987  -0.0246 -0.0693 328 ARG A NH1 
2798 N NH2 . ARG A 328 ? 0.8098 0.6529 0.6613 0.1824  -0.0270 -0.0745 328 ARG A NH2 
2799 N N   . ASP A 329 ? 0.3466 0.2297 0.2476 0.1375  -0.0023 -0.0256 329 ASP A N   
2800 C CA  . ASP A 329 ? 0.3446 0.2059 0.2470 0.1262  -0.0076 -0.0182 329 ASP A CA  
2801 C C   . ASP A 329 ? 0.3227 0.2090 0.2408 0.1142  -0.0017 -0.0074 329 ASP A C   
2802 O O   . ASP A 329 ? 0.3539 0.2402 0.2766 0.1143  -0.0037 -0.0015 329 ASP A O   
2803 C CB  . ASP A 329 ? 0.3702 0.2017 0.2634 0.1124  -0.0130 -0.0196 329 ASP A CB  
2804 C CG  . ASP A 329 ? 0.3453 0.1563 0.2384 0.0999  -0.0187 -0.0112 329 ASP A CG  
2805 O OD1 . ASP A 329 ? 0.3957 0.1860 0.2825 0.1018  -0.0269 -0.0118 329 ASP A OD1 
2806 O OD2 . ASP A 329 ? 0.3593 0.1827 0.2614 0.0845  -0.0148 -0.0037 329 ASP A OD2 
2807 N N   . PHE A 330 ? 0.2822 0.1894 0.2083 0.1043  0.0047  -0.0051 330 PHE A N   
2808 C CA  . PHE A 330 ? 0.2829 0.2098 0.2231 0.0924  0.0086  0.0037  330 PHE A CA  
2809 C C   . PHE A 330 ? 0.2671 0.2195 0.2171 0.1010  0.0112  0.0078  330 PHE A C   
2810 O O   . PHE A 330 ? 0.2727 0.2293 0.2299 0.0962  0.0100  0.0138  330 PHE A O   
2811 C CB  . PHE A 330 ? 0.2309 0.1719 0.1765 0.0823  0.0131  0.0046  330 PHE A CB  
2812 C CG  . PHE A 330 ? 0.2516 0.2029 0.2092 0.0682  0.0143  0.0115  330 PHE A CG  
2813 C CD1 . PHE A 330 ? 0.2849 0.2205 0.2411 0.0567  0.0115  0.0121  330 PHE A CD1 
2814 C CD2 . PHE A 330 ? 0.2116 0.1893 0.1817 0.0662  0.0177  0.0170  330 PHE A CD2 
2815 C CE1 . PHE A 330 ? 0.2710 0.2167 0.2374 0.0461  0.0122  0.0161  330 PHE A CE1 
2816 C CE2 . PHE A 330 ? 0.2022 0.1858 0.1824 0.0542  0.0171  0.0217  330 PHE A CE2 
2817 C CZ  . PHE A 330 ? 0.2310 0.1985 0.2090 0.0453  0.0144  0.0202  330 PHE A CZ  
2818 N N   . ILE A 331 ? 0.2747 0.2472 0.2251 0.1138  0.0147  0.0044  331 ILE A N   
2819 C CA  . ILE A 331 ? 0.2507 0.2525 0.2114 0.1223  0.0173  0.0085  331 ILE A CA  
2820 C C   . ILE A 331 ? 0.2587 0.2462 0.2160 0.1326  0.0117  0.0079  331 ILE A C   
2821 O O   . ILE A 331 ? 0.2705 0.2736 0.2378 0.1319  0.0116  0.0143  331 ILE A O   
2822 C CB  . ILE A 331 ? 0.2687 0.2979 0.2292 0.1354  0.0224  0.0045  331 ILE A CB  
2823 C CG1 . ILE A 331 ? 0.3037 0.3494 0.2683 0.1234  0.0274  0.0080  331 ILE A CG1 
2824 C CG2 . ILE A 331 ? 0.3153 0.3779 0.2867 0.1455  0.0248  0.0086  331 ILE A CG2 
2825 C CD1 . ILE A 331 ? 0.3192 0.3864 0.2999 0.1083  0.0295  0.0194  331 ILE A CD1 
2826 N N   . GLY A 332 ? 0.3141 0.2706 0.2570 0.1420  0.0058  0.0006  332 GLY A N   
2827 C CA  . GLY A 332 ? 0.3240 0.2631 0.2625 0.1514  -0.0013 0.0008  332 GLY A CA  
2828 C C   . GLY A 332 ? 0.3142 0.2429 0.2565 0.1377  -0.0044 0.0101  332 GLY A C   
2829 O O   . GLY A 332 ? 0.3295 0.2615 0.2751 0.1435  -0.0078 0.0145  332 GLY A O   
2830 N N   . ARG A 333 ? 0.3005 0.2184 0.2421 0.1195  -0.0036 0.0129  333 ARG A N   
2831 C CA  . ARG A 333 ? 0.2793 0.1934 0.2246 0.1058  -0.0056 0.0209  333 ARG A CA  
2832 C C   . ARG A 333 ? 0.2440 0.1910 0.2046 0.1015  -0.0009 0.0264  333 ARG A C   
2833 O O   . ARG A 333 ? 0.2845 0.2356 0.2487 0.0994  -0.0036 0.0321  333 ARG A O   
2834 C CB  . ARG A 333 ? 0.3127 0.2108 0.2536 0.0891  -0.0058 0.0212  333 ARG A CB  
2835 C CG  . ARG A 333 ? 0.4716 0.3598 0.4110 0.0773  -0.0096 0.0283  333 ARG A CG  
2836 C CD  . ARG A 333 ? 0.4970 0.3729 0.4320 0.0619  -0.0099 0.0284  333 ARG A CD  
2837 N NE  . ARG A 333 ? 0.4695 0.3138 0.3909 0.0610  -0.0168 0.0279  333 ARG A NE  
2838 C CZ  . ARG A 333 ? 0.5351 0.3614 0.4492 0.0569  -0.0237 0.0347  333 ARG A CZ  
2839 N NH1 . ARG A 333 ? 0.4623 0.3010 0.3808 0.0544  -0.0238 0.0419  333 ARG A NH1 
2840 N NH2 . ARG A 333 ? 0.5731 0.3687 0.4750 0.0544  -0.0314 0.0348  333 ARG A NH2 
2841 N N   . LEU A 334 ? 0.2353 0.2062 0.2046 0.0999  0.0051  0.0252  334 LEU A N   
2842 C CA  . LEU A 334 ? 0.2276 0.2289 0.2117 0.0954  0.0080  0.0308  334 LEU A CA  
2843 C C   . LEU A 334 ? 0.2366 0.2547 0.2254 0.1089  0.0066  0.0330  334 LEU A C   
2844 O O   . LEU A 334 ? 0.2220 0.2553 0.2200 0.1046  0.0053  0.0387  334 LEU A O   
2845 C CB  . LEU A 334 ? 0.1879 0.2102 0.1795 0.0911  0.0135  0.0308  334 LEU A CB  
2846 C CG  . LEU A 334 ? 0.1780 0.1894 0.1687 0.0767  0.0143  0.0300  334 LEU A CG  
2847 C CD1 . LEU A 334 ? 0.2358 0.2683 0.2337 0.0734  0.0185  0.0318  334 LEU A CD1 
2848 C CD2 . LEU A 334 ? 0.2255 0.2337 0.2216 0.0639  0.0115  0.0334  334 LEU A CD2 
2849 N N   . LYS A 335 ? 0.2248 0.2416 0.2075 0.1262  0.0063  0.0279  335 LYS A N   
2850 C CA  . LYS A 335 ? 0.2479 0.2816 0.2352 0.1415  0.0044  0.0291  335 LYS A CA  
2851 C C   . LYS A 335 ? 0.2431 0.2575 0.2264 0.1414  -0.0028 0.0332  335 LYS A C   
2852 O O   . LYS A 335 ? 0.2752 0.3091 0.2673 0.1442  -0.0044 0.0384  335 LYS A O   
2853 C CB  . LYS A 335 ? 0.3380 0.3699 0.3171 0.1602  0.0043  0.0202  335 LYS A CB  
2854 C CG  . LYS A 335 ? 0.5047 0.5591 0.4859 0.1619  0.0115  0.0163  335 LYS A CG  
2855 C CD  . LYS A 335 ? 0.6479 0.7110 0.6225 0.1768  0.0114  0.0075  335 LYS A CD  
2856 C CE  . LYS A 335 ? 0.7273 0.7500 0.6843 0.1833  0.0049  -0.0024 335 LYS A CE  
2857 N NZ  . LYS A 335 ? 0.7221 0.7413 0.6708 0.1832  0.0080  -0.0093 335 LYS A NZ  
2858 N N   . LYS A 336 ? 0.3270 0.3046 0.2969 0.1373  -0.0077 0.0318  336 LYS A N   
2859 C CA  . LYS A 336 ? 0.3701 0.3290 0.3346 0.1354  -0.0150 0.0375  336 LYS A CA  
2860 C C   . LYS A 336 ? 0.3019 0.2782 0.2759 0.1202  -0.0136 0.0448  336 LYS A C   
2861 O O   . LYS A 336 ? 0.3090 0.2922 0.2856 0.1230  -0.0177 0.0503  336 LYS A O   
2862 C CB  . LYS A 336 ? 0.4122 0.3309 0.3613 0.1296  -0.0204 0.0365  336 LYS A CB  
2863 C CG  . LYS A 336 ? 0.5585 0.4582 0.5009 0.1235  -0.0280 0.0448  336 LYS A CG  
2864 C CD  . LYS A 336 ? 0.7109 0.5823 0.6424 0.1083  -0.0306 0.0465  336 LYS A CD  
2865 C CE  . LYS A 336 ? 0.7910 0.6563 0.7189 0.0963  -0.0353 0.0569  336 LYS A CE  
2866 N NZ  . LYS A 336 ? 0.8315 0.6651 0.7477 0.0984  -0.0455 0.0612  336 LYS A NZ  
2867 N N   . ILE A 337 ? 0.2741 0.2574 0.2528 0.1050  -0.0087 0.0443  337 ILE A N   
2868 C CA  . ILE A 337 ? 0.2533 0.2527 0.2405 0.0918  -0.0083 0.0489  337 ILE A CA  
2869 C C   . ILE A 337 ? 0.2563 0.2881 0.2574 0.0969  -0.0074 0.0517  337 ILE A C   
2870 O O   . ILE A 337 ? 0.2689 0.3105 0.2738 0.0951  -0.0111 0.0564  337 ILE A O   
2871 C CB  . ILE A 337 ? 0.2453 0.2453 0.2353 0.0772  -0.0042 0.0462  337 ILE A CB  
2872 C CG1 . ILE A 337 ? 0.2294 0.2012 0.2068 0.0712  -0.0053 0.0441  337 ILE A CG1 
2873 C CG2 . ILE A 337 ? 0.2560 0.2724 0.2549 0.0660  -0.0049 0.0488  337 ILE A CG2 
2874 C CD1 . ILE A 337 ? 0.2334 0.2050 0.2130 0.0608  -0.0012 0.0399  337 ILE A CD1 
2875 N N   . HIS A 338 ? 0.2311 0.2820 0.2397 0.1029  -0.0029 0.0495  338 HIS A N   
2876 C CA  . HIS A 338 ? 0.2227 0.3088 0.2457 0.1066  -0.0018 0.0532  338 HIS A CA  
2877 C C   . HIS A 338 ? 0.2646 0.3568 0.2877 0.1202  -0.0066 0.0559  338 HIS A C   
2878 O O   . HIS A 338 ? 0.2578 0.3722 0.2911 0.1175  -0.0089 0.0609  338 HIS A O   
2879 C CB  . HIS A 338 ? 0.2209 0.3262 0.2488 0.1130  0.0040  0.0509  338 HIS A CB  
2880 C CG  . HIS A 338 ? 0.2423 0.3888 0.2861 0.1150  0.0058  0.0559  338 HIS A CG  
2881 N ND1 . HIS A 338 ? 0.2840 0.4538 0.3309 0.1322  0.0082  0.0546  338 HIS A ND1 
2882 C CD2 . HIS A 338 ? 0.2008 0.3706 0.2585 0.1014  0.0051  0.0622  338 HIS A CD2 
2883 C CE1 . HIS A 338 ? 0.2818 0.4875 0.3430 0.1263  0.0096  0.0603  338 HIS A CE1 
2884 N NE2 . HIS A 338 ? 0.2370 0.4449 0.3067 0.1089  0.0071  0.0661  338 HIS A NE2 
2885 N N   . GLU A 339 ? 0.2593 0.3311 0.2711 0.1355  -0.0091 0.0523  339 GLU A N   
2886 C CA  . GLU A 339 ? 0.2462 0.3196 0.2569 0.1481  -0.0146 0.0535  339 GLU A CA  
2887 C C   . GLU A 339 ? 0.2561 0.3121 0.2608 0.1427  -0.0216 0.0599  339 GLU A C   
2888 O O   . GLU A 339 ? 0.2881 0.3493 0.2943 0.1486  -0.0264 0.0621  339 GLU A O   
2889 C CB  . GLU A 339 ? 0.3117 0.3637 0.3111 0.1619  -0.0162 0.0452  339 GLU A CB  
2890 C CG  . GLU A 339 ? 0.3748 0.4469 0.3775 0.1697  -0.0096 0.0382  339 GLU A CG  
2891 C CD  . GLU A 339 ? 0.5541 0.5973 0.5422 0.1796  -0.0117 0.0287  339 GLU A CD  
2892 O OE1 . GLU A 339 ? 0.5583 0.6156 0.5457 0.1869  -0.0070 0.0219  339 GLU A OE1 
2893 O OE2 . GLU A 339 ? 0.6338 0.6406 0.6105 0.1790  -0.0187 0.0284  339 GLU A OE2 
2894 N N   . SER A 340 ? 0.3130 0.3496 0.3108 0.1275  -0.0217 0.0614  340 SER A N   
2895 C CA  . SER A 340 ? 0.3188 0.3378 0.3077 0.1213  -0.0281 0.0673  340 SER A CA  
2896 C C   . SER A 340 ? 0.3069 0.3503 0.3047 0.1122  -0.0294 0.0722  340 SER A C   
2897 O O   . SER A 340 ? 0.2971 0.3337 0.2885 0.1107  -0.0354 0.0781  340 SER A O   
2898 C CB  . SER A 340 ? 0.3142 0.3060 0.2917 0.1077  -0.0273 0.0663  340 SER A CB  
2899 O OG  . SER A 340 ? 0.3416 0.3473 0.3261 0.0926  -0.0221 0.0643  340 SER A OG  
2900 N N   . VAL A 341 ? 0.2762 0.3471 0.2879 0.1054  -0.0251 0.0705  341 VAL A N   
2901 C CA  . VAL A 341 ? 0.2625 0.3548 0.2824 0.0959  -0.0277 0.0737  341 VAL A CA  
2902 C C   . VAL A 341 ? 0.2227 0.3499 0.2597 0.0996  -0.0265 0.0748  341 VAL A C   
2903 O O   . VAL A 341 ? 0.2276 0.3652 0.2709 0.1052  -0.0217 0.0725  341 VAL A O   
2904 C CB  . VAL A 341 ? 0.2400 0.3274 0.2588 0.0782  -0.0259 0.0706  341 VAL A CB  
2905 C CG1 . VAL A 341 ? 0.3335 0.3935 0.3365 0.0735  -0.0271 0.0709  341 VAL A CG1 
2906 C CG2 . VAL A 341 ? 0.2244 0.3152 0.2503 0.0733  -0.0200 0.0658  341 VAL A CG2 
2907 N N   . ASP A 342 ? 0.2032 0.3507 0.2474 0.0959  -0.0314 0.0787  342 ASP A N   
2908 C CA  . ASP A 342 ? 0.2099 0.3937 0.2715 0.0969  -0.0318 0.0813  342 ASP A CA  
2909 C C   . ASP A 342 ? 0.2207 0.4177 0.2930 0.0794  -0.0309 0.0800  342 ASP A C   
2910 O O   . ASP A 342 ? 0.2514 0.4787 0.3390 0.0768  -0.0315 0.0833  342 ASP A O   
2911 C CB  . ASP A 342 ? 0.2363 0.4338 0.2999 0.1010  -0.0382 0.0852  342 ASP A CB  
2912 C CG  . ASP A 342 ? 0.4086 0.6157 0.4751 0.0869  -0.0441 0.0871  342 ASP A CG  
2913 O OD1 . ASP A 342 ? 0.5276 0.7145 0.5851 0.0757  -0.0437 0.0833  342 ASP A OD1 
2914 O OD2 . ASP A 342 ? 0.5378 0.7665 0.6129 0.0845  -0.0478 0.0887  342 ASP A OD2 
2915 N N   . PHE A 343 ? 0.2047 0.3801 0.2696 0.0674  -0.0303 0.0756  343 PHE A N   
2916 C CA  . PHE A 343 ? 0.1515 0.3327 0.2250 0.0521  -0.0308 0.0733  343 PHE A CA  
2917 C C   . PHE A 343 ? 0.1850 0.3540 0.2571 0.0506  -0.0244 0.0706  343 PHE A C   
2918 O O   . PHE A 343 ? 0.2036 0.3610 0.2680 0.0612  -0.0195 0.0696  343 PHE A O   
2919 C CB  . PHE A 343 ? 0.1707 0.3398 0.2377 0.0412  -0.0359 0.0689  343 PHE A CB  
2920 C CG  . PHE A 343 ? 0.1913 0.3322 0.2421 0.0417  -0.0332 0.0646  343 PHE A CG  
2921 C CD1 . PHE A 343 ? 0.2503 0.3813 0.2888 0.0487  -0.0344 0.0672  343 PHE A CD1 
2922 C CD2 . PHE A 343 ? 0.1950 0.3207 0.2432 0.0342  -0.0303 0.0589  343 PHE A CD2 
2923 C CE1 . PHE A 343 ? 0.2022 0.3104 0.2267 0.0469  -0.0323 0.0650  343 PHE A CE1 
2924 C CE2 . PHE A 343 ? 0.2212 0.3255 0.2559 0.0338  -0.0278 0.0555  343 PHE A CE2 
2925 C CZ  . PHE A 343 ? 0.2282 0.3245 0.2512 0.0393  -0.0286 0.0588  343 PHE A CZ  
2926 N N   . GLN A 344 ? 0.1661 0.3372 0.2456 0.0375  -0.0254 0.0692  344 GLN A N   
2927 C CA  . GLN A 344 ? 0.1490 0.3103 0.2278 0.0348  -0.0202 0.0676  344 GLN A CA  
2928 C C   . GLN A 344 ? 0.1638 0.2962 0.2308 0.0299  -0.0200 0.0606  344 GLN A C   
2929 O O   . GLN A 344 ? 0.1755 0.3033 0.2443 0.0197  -0.0251 0.0570  344 GLN A O   
2930 C CB  . GLN A 344 ? 0.1722 0.3514 0.2656 0.0231  -0.0224 0.0718  344 GLN A CB  
2931 C CG  . GLN A 344 ? 0.1638 0.3781 0.2703 0.0270  -0.0220 0.0799  344 GLN A CG  
2932 C CD  . GLN A 344 ? 0.1801 0.4150 0.3015 0.0135  -0.0243 0.0869  344 GLN A CD  
2933 O OE1 . GLN A 344 ? 0.1962 0.4531 0.3239 0.0167  -0.0190 0.0927  344 GLN A OE1 
2934 N NE2 . GLN A 344 ? 0.1701 0.3991 0.2969 -0.0016 -0.0329 0.0866  344 GLN A NE2 
2935 N N   . PRO A 345 ? 0.1455 0.2591 0.2008 0.0371  -0.0151 0.0579  345 PRO A N   
2936 C CA  . PRO A 345 ? 0.1550 0.2454 0.1999 0.0321  -0.0148 0.0520  345 PRO A CA  
2937 C C   . PRO A 345 ? 0.1565 0.2410 0.2052 0.0244  -0.0135 0.0490  345 PRO A C   
2938 O O   . PRO A 345 ? 0.1453 0.2380 0.2003 0.0250  -0.0107 0.0522  345 PRO A O   
2939 C CB  . PRO A 345 ? 0.1941 0.2680 0.2265 0.0418  -0.0109 0.0519  345 PRO A CB  
2940 C CG  . PRO A 345 ? 0.1567 0.2421 0.1938 0.0518  -0.0076 0.0550  345 PRO A CG  
2941 C CD  . PRO A 345 ? 0.1833 0.2967 0.2339 0.0508  -0.0106 0.0598  345 PRO A CD  
2942 N N   . VAL A 346 ? 0.1353 0.2072 0.1799 0.0177  -0.0157 0.0430  346 VAL A N   
2943 C CA  . VAL A 346 ? 0.1265 0.1887 0.1728 0.0119  -0.0153 0.0393  346 VAL A CA  
2944 C C   . VAL A 346 ? 0.1283 0.1734 0.1628 0.0150  -0.0107 0.0355  346 VAL A C   
2945 O O   . VAL A 346 ? 0.1664 0.2052 0.1928 0.0147  -0.0113 0.0322  346 VAL A O   
2946 C CB  . VAL A 346 ? 0.1563 0.2172 0.2074 0.0035  -0.0225 0.0338  346 VAL A CB  
2947 C CG1 . VAL A 346 ? 0.1627 0.2131 0.2167 -0.0012 -0.0233 0.0310  346 VAL A CG1 
2948 C CG2 . VAL A 346 ? 0.1734 0.2506 0.2354 -0.0009 -0.0289 0.0377  346 VAL A CG2 
2949 N N   . VAL A 347 ? 0.1535 0.1931 0.1870 0.0170  -0.0066 0.0363  347 VAL A N   
2950 C CA  . VAL A 347 ? 0.1307 0.1549 0.1533 0.0202  -0.0026 0.0338  347 VAL A CA  
2951 C C   . VAL A 347 ? 0.1346 0.1513 0.1583 0.0150  -0.0023 0.0297  347 VAL A C   
2952 O O   . VAL A 347 ? 0.1450 0.1644 0.1730 0.0148  -0.0009 0.0319  347 VAL A O   
2953 C CB  . VAL A 347 ? 0.1583 0.1820 0.1770 0.0294  0.0013  0.0372  347 VAL A CB  
2954 C CG1 . VAL A 347 ? 0.2184 0.2232 0.2253 0.0317  0.0037  0.0341  347 VAL A CG1 
2955 C CG2 . VAL A 347 ? 0.1832 0.2154 0.2020 0.0363  -0.0001 0.0412  347 VAL A CG2 
2956 N N   . PHE A 348 ? 0.1510 0.1611 0.1713 0.0110  -0.0039 0.0241  348 PHE A N   
2957 C CA  . PHE A 348 ? 0.1320 0.1356 0.1534 0.0073  -0.0045 0.0193  348 PHE A CA  
2958 C C   . PHE A 348 ? 0.1591 0.1523 0.1717 0.0089  -0.0003 0.0184  348 PHE A C   
2959 O O   . PHE A 348 ? 0.1769 0.1655 0.1812 0.0092  0.0011  0.0180  348 PHE A O   
2960 C CB  . PHE A 348 ? 0.1253 0.1306 0.1479 0.0040  -0.0087 0.0121  348 PHE A CB  
2961 C CG  . PHE A 348 ? 0.1419 0.1505 0.1744 0.0009  -0.0154 0.0100  348 PHE A CG  
2962 C CD1 . PHE A 348 ? 0.1369 0.1539 0.1749 -0.0002 -0.0188 0.0137  348 PHE A CD1 
2963 C CD2 . PHE A 348 ? 0.1695 0.1720 0.2061 -0.0009 -0.0197 0.0045  348 PHE A CD2 
2964 C CE1 . PHE A 348 ? 0.1435 0.1615 0.1906 -0.0047 -0.0267 0.0123  348 PHE A CE1 
2965 C CE2 . PHE A 348 ? 0.1720 0.1731 0.2172 -0.0042 -0.0281 0.0027  348 PHE A CE2 
2966 C CZ  . PHE A 348 ? 0.1437 0.1520 0.1941 -0.0068 -0.0318 0.0068  348 PHE A CZ  
2967 N N   . VAL A 349 ? 0.1329 0.1227 0.1470 0.0090  0.0010  0.0187  349 VAL A N   
2968 C CA  . VAL A 349 ? 0.1329 0.1129 0.1393 0.0097  0.0039  0.0170  349 VAL A CA  
2969 C C   . VAL A 349 ? 0.1378 0.1167 0.1481 0.0057  0.0017  0.0124  349 VAL A C   
2970 O O   . VAL A 349 ? 0.1572 0.1379 0.1738 0.0048  -0.0004 0.0137  349 VAL A O   
2971 C CB  . VAL A 349 ? 0.1374 0.1165 0.1413 0.0147  0.0068  0.0205  349 VAL A CB  
2972 C CG1 . VAL A 349 ? 0.1640 0.1318 0.1592 0.0151  0.0085  0.0175  349 VAL A CG1 
2973 C CG2 . VAL A 349 ? 0.1988 0.1807 0.1999 0.0211  0.0082  0.0239  349 VAL A CG2 
2974 N N   . VAL A 350 ? 0.1369 0.1147 0.1438 0.0033  0.0014  0.0076  350 VAL A N   
2975 C CA  . VAL A 350 ? 0.1595 0.1396 0.1710 0.0014  -0.0015 0.0016  350 VAL A CA  
2976 C C   . VAL A 350 ? 0.1480 0.1258 0.1535 -0.0006 0.0008  -0.0007 350 VAL A C   
2977 O O   . VAL A 350 ? 0.1636 0.1424 0.1627 -0.0029 0.0028  0.0000  350 VAL A O   
2978 C CB  . VAL A 350 ? 0.1417 0.1301 0.1569 0.0011  -0.0048 -0.0038 350 VAL A CB  
2979 C CG1 . VAL A 350 ? 0.1355 0.1256 0.1565 0.0020  -0.0093 -0.0113 350 VAL A CG1 
2980 C CG2 . VAL A 350 ? 0.1492 0.1400 0.1692 0.0017  -0.0077 -0.0010 350 VAL A CG2 
2981 N N   . LEU A 351 ? 0.1438 0.1191 0.1515 -0.0006 -0.0002 -0.0025 351 LEU A N   
2982 C CA  . LEU A 351 ? 0.1311 0.1061 0.1344 -0.0032 0.0010  -0.0048 351 LEU A CA  
2983 C C   . LEU A 351 ? 0.1375 0.1133 0.1464 -0.0019 -0.0020 -0.0078 351 LEU A C   
2984 O O   . LEU A 351 ? 0.1450 0.1187 0.1600 0.0003  -0.0053 -0.0068 351 LEU A O   
2985 C CB  . LEU A 351 ? 0.1647 0.1294 0.1584 -0.0043 0.0039  -0.0007 351 LEU A CB  
2986 C CG  . LEU A 351 ? 0.1720 0.1294 0.1636 -0.0004 0.0047  0.0025  351 LEU A CG  
2987 C CD1 . LEU A 351 ? 0.2089 0.1564 0.1908 -0.0012 0.0056  0.0021  351 LEU A CD1 
2988 C CD2 . LEU A 351 ? 0.1505 0.1079 0.1423 0.0036  0.0060  0.0068  351 LEU A CD2 
2989 N N   . ASP A 352 ? 0.1508 0.1296 0.1578 -0.0041 -0.0018 -0.0107 352 ASP A N   
2990 C CA  . ASP A 352 ? 0.1512 0.1302 0.1627 -0.0024 -0.0051 -0.0128 352 ASP A CA  
2991 C C   . ASP A 352 ? 0.1544 0.1239 0.1636 -0.0012 -0.0051 -0.0070 352 ASP A C   
2992 O O   . ASP A 352 ? 0.1759 0.1397 0.1774 -0.0018 -0.0016 -0.0034 352 ASP A O   
2993 C CB  . ASP A 352 ? 0.1497 0.1343 0.1585 -0.0057 -0.0045 -0.0154 352 ASP A CB  
2994 C CG  . ASP A 352 ? 0.1345 0.1354 0.1468 -0.0071 -0.0043 -0.0208 352 ASP A CG  
2995 O OD1 . ASP A 352 ? 0.1692 0.1768 0.1850 -0.0045 -0.0048 -0.0238 352 ASP A OD1 
2996 O OD2 . ASP A 352 ? 0.1439 0.1529 0.1549 -0.0113 -0.0038 -0.0219 352 ASP A OD2 
2997 N N   . GLY A 353 ? 0.1448 0.1134 0.1602 0.0008  -0.0097 -0.0061 353 GLY A N   
2998 C CA  . GLY A 353 ? 0.1285 0.0925 0.1418 0.0009  -0.0096 0.0010  353 GLY A CA  
2999 C C   . GLY A 353 ? 0.1622 0.1254 0.1707 0.0006  -0.0099 0.0019  353 GLY A C   
3000 O O   . GLY A 353 ? 0.1577 0.1202 0.1627 0.0009  -0.0092 0.0078  353 GLY A O   
3001 N N   . GLU A 354 ? 0.1531 0.1191 0.1614 0.0000  -0.0111 -0.0036 354 GLU A N   
3002 C CA  . GLU A 354 ? 0.1594 0.1258 0.1640 -0.0004 -0.0128 -0.0032 354 GLU A CA  
3003 C C   . GLU A 354 ? 0.1723 0.1398 0.1699 -0.0036 -0.0106 -0.0073 354 GLU A C   
3004 O O   . GLU A 354 ? 0.2278 0.1959 0.2214 -0.0043 -0.0124 -0.0074 354 GLU A O   
3005 C CB  . GLU A 354 ? 0.1632 0.1328 0.1766 0.0020  -0.0198 -0.0048 354 GLU A CB  
3006 C CG  . GLU A 354 ? 0.1624 0.1412 0.1812 0.0030  -0.0215 -0.0131 354 GLU A CG  
3007 C CD  . GLU A 354 ? 0.1379 0.1198 0.1630 0.0053  -0.0217 -0.0175 354 GLU A CD  
3008 O OE1 . GLU A 354 ? 0.1562 0.1404 0.1897 0.0105  -0.0278 -0.0221 354 GLU A OE1 
3009 O OE2 . GLU A 354 ? 0.1515 0.1332 0.1724 0.0025  -0.0165 -0.0169 354 GLU A OE2 
3010 N N   . ASN A 355 ? 0.1610 0.1290 0.1567 -0.0064 -0.0077 -0.0099 355 ASN A N   
3011 C CA  . ASN A 355 ? 0.1476 0.1174 0.1383 -0.0118 -0.0075 -0.0128 355 ASN A CA  
3012 C C   . ASN A 355 ? 0.1728 0.1296 0.1513 -0.0142 -0.0054 -0.0114 355 ASN A C   
3013 O O   . ASN A 355 ? 0.1929 0.1469 0.1655 -0.0193 -0.0071 -0.0133 355 ASN A O   
3014 C CB  . ASN A 355 ? 0.1559 0.1373 0.1525 -0.0150 -0.0070 -0.0158 355 ASN A CB  
3015 C CG  . ASN A 355 ? 0.1810 0.1762 0.1886 -0.0109 -0.0103 -0.0199 355 ASN A CG  
3016 O OD1 . ASN A 355 ? 0.1627 0.1609 0.1728 -0.0091 -0.0138 -0.0210 355 ASN A OD1 
3017 N ND2 . ASN A 355 ? 0.1608 0.1648 0.1748 -0.0084 -0.0100 -0.0230 355 ASN A ND2 
3018 N N   . CYS A 356 ? 0.1901 0.1388 0.1646 -0.0104 -0.0027 -0.0087 356 CYS A N   
3019 C CA  . CYS A 356 ? 0.2104 0.1453 0.1730 -0.0107 -0.0020 -0.0090 356 CYS A CA  
3020 C C   . CYS A 356 ? 0.1878 0.1172 0.1417 -0.0064 -0.0026 -0.0104 356 CYS A C   
3021 O O   . CYS A 356 ? 0.2159 0.1328 0.1589 -0.0070 -0.0043 -0.0134 356 CYS A O   
3022 C CB  . CYS A 356 ? 0.2268 0.1566 0.1884 -0.0071 0.0007  -0.0064 356 CYS A CB  
3023 S SG  . CYS A 356 ? 0.2248 0.1623 0.1927 0.0003  0.0033  -0.0026 356 CYS A SG  
3024 N N   . TRP A 357 ? 0.1875 0.1257 0.1453 -0.0026 -0.0022 -0.0082 357 TRP A N   
3025 C CA  . TRP A 357 ? 0.2071 0.1445 0.1559 0.0027  -0.0015 -0.0083 357 TRP A CA  
3026 C C   . TRP A 357 ? 0.1933 0.1266 0.1334 0.0003  -0.0051 -0.0130 357 TRP A C   
3027 O O   . TRP A 357 ? 0.2213 0.1494 0.1495 0.0049  -0.0051 -0.0163 357 TRP A O   
3028 C CB  . TRP A 357 ? 0.1997 0.1494 0.1552 0.0053  -0.0007 -0.0021 357 TRP A CB  
3029 C CG  . TRP A 357 ? 0.1630 0.1163 0.1283 0.0058  0.0010  0.0023  357 TRP A CG  
3030 C CD1 . TRP A 357 ? 0.1858 0.1440 0.1631 0.0033  -0.0015 0.0053  357 TRP A CD1 
3031 C CD2 . TRP A 357 ? 0.1886 0.1399 0.1525 0.0093  0.0046  0.0032  357 TRP A CD2 
3032 N NE1 . TRP A 357 ? 0.1719 0.1313 0.1548 0.0041  0.0002  0.0078  357 TRP A NE1 
3033 C CE2 . TRP A 357 ? 0.1745 0.1309 0.1498 0.0076  0.0042  0.0071  357 TRP A CE2 
3034 C CE3 . TRP A 357 ? 0.2066 0.1516 0.1605 0.0147  0.0070  0.0004  357 TRP A CE3 
3035 C CZ2 . TRP A 357 ? 0.1705 0.1282 0.1479 0.0100  0.0067  0.0092  357 TRP A CZ2 
3036 C CZ3 . TRP A 357 ? 0.2091 0.1552 0.1656 0.0183  0.0095  0.0025  357 TRP A CZ3 
3037 C CH2 . TRP A 357 ? 0.1850 0.1385 0.1533 0.0154  0.0096  0.0073  357 TRP A CH2 
3038 N N   . GLU A 358 ? 0.2194 0.1566 0.1650 -0.0061 -0.0085 -0.0143 358 GLU A N   
3039 C CA  . GLU A 358 ? 0.2047 0.1402 0.1432 -0.0095 -0.0127 -0.0185 358 GLU A CA  
3040 C C   . GLU A 358 ? 0.2194 0.1382 0.1457 -0.0121 -0.0149 -0.0237 358 GLU A C   
3041 O O   . GLU A 358 ? 0.2498 0.1633 0.1665 -0.0135 -0.0191 -0.0284 358 GLU A O   
3042 C CB  . GLU A 358 ? 0.2186 0.1652 0.1676 -0.0157 -0.0159 -0.0185 358 GLU A CB  
3043 C CG  . GLU A 358 ? 0.2225 0.1704 0.1781 -0.0220 -0.0155 -0.0189 358 GLU A CG  
3044 C CD  . GLU A 358 ? 0.2202 0.1857 0.1896 -0.0235 -0.0168 -0.0187 358 GLU A CD  
3045 O OE1 . GLU A 358 ? 0.2703 0.2445 0.2424 -0.0302 -0.0196 -0.0209 358 GLU A OE1 
3046 O OE2 . GLU A 358 ? 0.2102 0.1814 0.1879 -0.0178 -0.0158 -0.0167 358 GLU A OE2 
3047 N N   . TYR A 359 ? 0.2399 0.1486 0.1658 -0.0128 -0.0135 -0.0230 359 TYR A N   
3048 C CA  . TYR A 359 ? 0.2357 0.1239 0.1498 -0.0153 -0.0173 -0.0269 359 TYR A CA  
3049 C C   . TYR A 359 ? 0.2576 0.1338 0.1601 -0.0039 -0.0162 -0.0305 359 TYR A C   
3050 O O   . TYR A 359 ? 0.2835 0.1392 0.1744 -0.0034 -0.0211 -0.0354 359 TYR A O   
3051 C CB  . TYR A 359 ? 0.2765 0.1601 0.1957 -0.0226 -0.0175 -0.0230 359 TYR A CB  
3052 C CG  . TYR A 359 ? 0.2560 0.1563 0.1868 -0.0328 -0.0179 -0.0202 359 TYR A CG  
3053 C CD1 . TYR A 359 ? 0.3248 0.2241 0.2536 -0.0439 -0.0234 -0.0214 359 TYR A CD1 
3054 C CD2 . TYR A 359 ? 0.2468 0.1651 0.1905 -0.0309 -0.0135 -0.0170 359 TYR A CD2 
3055 C CE1 . TYR A 359 ? 0.3010 0.2211 0.2414 -0.0522 -0.0233 -0.0191 359 TYR A CE1 
3056 C CE2 . TYR A 359 ? 0.3142 0.2503 0.2683 -0.0376 -0.0140 -0.0162 359 TYR A CE2 
3057 C CZ  . TYR A 359 ? 0.3137 0.2527 0.2665 -0.0479 -0.0184 -0.0171 359 TYR A CZ  
3058 O OH  . TYR A 359 ? 0.3731 0.3349 0.3370 -0.0536 -0.0184 -0.0166 359 TYR A OH  
3059 N N   . TYR A 360 ? 0.2646 0.1538 0.1701 0.0051  -0.0108 -0.0281 360 TYR A N   
3060 C CA  . TYR A 360 ? 0.2479 0.1336 0.1436 0.0173  -0.0088 -0.0317 360 TYR A CA  
3061 C C   . TYR A 360 ? 0.3117 0.2026 0.1970 0.0222  -0.0102 -0.0370 360 TYR A C   
3062 O O   . TYR A 360 ? 0.2947 0.1983 0.1839 0.0176  -0.0106 -0.0346 360 TYR A O   
3063 C CB  . TYR A 360 ? 0.2525 0.1548 0.1572 0.0234  -0.0022 -0.0251 360 TYR A CB  
3064 C CG  . TYR A 360 ? 0.2348 0.1340 0.1473 0.0229  -0.0002 -0.0209 360 TYR A CG  
3065 C CD1 . TYR A 360 ? 0.2180 0.1176 0.1406 0.0134  -0.0009 -0.0168 360 TYR A CD1 
3066 C CD2 . TYR A 360 ? 0.2531 0.1527 0.1630 0.0330  0.0026  -0.0209 360 TYR A CD2 
3067 C CE1 . TYR A 360 ? 0.2360 0.1348 0.1646 0.0131  0.0009  -0.0129 360 TYR A CE1 
3068 C CE2 . TYR A 360 ? 0.2426 0.1407 0.1595 0.0327  0.0039  -0.0166 360 TYR A CE2 
3069 C CZ  . TYR A 360 ? 0.2485 0.1457 0.1742 0.0224  0.0030  -0.0125 360 TYR A CZ  
3070 O OH  . TYR A 360 ? 0.2430 0.1406 0.1747 0.0221  0.0042  -0.0084 360 TYR A OH  
3071 N N   . GLU A 361 ? 0.2981 0.1794 0.2495 0.0322  -0.0454 -0.0379 361 GLU A N   
3072 C CA  . GLU A 361 ? 0.3280 0.2190 0.2673 0.0427  -0.0469 -0.0488 361 GLU A CA  
3073 C C   . GLU A 361 ? 0.2768 0.1964 0.2167 0.0486  -0.0340 -0.0423 361 GLU A C   
3074 O O   . GLU A 361 ? 0.2586 0.1852 0.2030 0.0518  -0.0249 -0.0361 361 GLU A O   
3075 C CB  . GLU A 361 ? 0.3926 0.2671 0.3199 0.0564  -0.0531 -0.0629 361 GLU A CB  
3076 C CG  . GLU A 361 ? 0.5839 0.4696 0.4965 0.0698  -0.0552 -0.0762 361 GLU A CG  
3077 C CD  . GLU A 361 ? 0.7807 0.6516 0.6858 0.0653  -0.0697 -0.0870 361 GLU A CD  
3078 O OE1 . GLU A 361 ? 0.7608 0.6121 0.6734 0.0506  -0.0783 -0.0832 361 GLU A OE1 
3079 O OE2 . GLU A 361 ? 0.9196 0.7999 0.8111 0.0761  -0.0728 -0.0991 361 GLU A OE2 
3080 N N   . GLU A 362 ? 0.2662 0.2019 0.2021 0.0487  -0.0339 -0.0427 362 GLU A N   
3081 C CA  . GLU A 362 ? 0.2495 0.2107 0.1840 0.0541  -0.0234 -0.0360 362 GLU A CA  
3082 C C   . GLU A 362 ? 0.2632 0.2300 0.2100 0.0479  -0.0137 -0.0217 362 GLU A C   
3083 O O   . GLU A 362 ? 0.2260 0.2054 0.1731 0.0523  -0.0049 -0.0160 362 GLU A O   
3084 C CB  . GLU A 362 ? 0.2939 0.2650 0.2173 0.0685  -0.0201 -0.0437 362 GLU A CB  
3085 C CG  . GLU A 362 ? 0.4172 0.4164 0.3356 0.0737  -0.0119 -0.0377 362 GLU A CG  
3086 C CD  . GLU A 362 ? 0.6124 0.6268 0.5204 0.0880  -0.0082 -0.0448 362 GLU A CD  
3087 O OE1 . GLU A 362 ? 0.5272 0.5338 0.4241 0.0976  -0.0160 -0.0604 362 GLU A OE1 
3088 O OE2 . GLU A 362 ? 0.6277 0.6622 0.5388 0.0895  0.0020  -0.0349 362 GLU A OE2 
3089 N N   . ASN A 363 ? 0.2105 0.1687 0.1673 0.0374  -0.0159 -0.0158 363 ASN A N   
3090 C CA  . ASN A 363 ? 0.1913 0.1551 0.1585 0.0323  -0.0081 -0.0039 363 ASN A CA  
3091 C C   . ASN A 363 ? 0.2258 0.1853 0.1957 0.0349  -0.0021 -0.0015 363 ASN A C   
3092 O O   . ASN A 363 ? 0.2127 0.1794 0.1876 0.0339  0.0052  0.0065  363 ASN A O   
3093 C CB  . ASN A 363 ? 0.2018 0.1829 0.1683 0.0342  -0.0028 0.0033  363 ASN A CB  
3094 C CG  . ASN A 363 ? 0.2189 0.2017 0.1951 0.0294  0.0021  0.0133  363 ASN A CG  
3095 O OD1 . ASN A 363 ? 0.1895 0.1671 0.1731 0.0233  -0.0002 0.0148  363 ASN A OD1 
3096 N ND2 . ASN A 363 ? 0.2790 0.2694 0.2549 0.0323  0.0085  0.0205  363 ASN A ND2 
3097 N N   . GLY A 364 ? 0.2035 0.1507 0.1700 0.0385  -0.0061 -0.0090 364 GLY A N   
3098 C CA  . GLY A 364 ? 0.2157 0.1599 0.1850 0.0416  -0.0018 -0.0074 364 GLY A CA  
3099 C C   . GLY A 364 ? 0.2458 0.2068 0.2121 0.0494  0.0054  -0.0067 364 GLY A C   
3100 O O   . GLY A 364 ? 0.2094 0.1724 0.1798 0.0510  0.0095  -0.0041 364 GLY A O   
3101 N N   . ILE A 365 ? 0.2108 0.1861 0.1702 0.0541  0.0067  -0.0084 365 ILE A N   
3102 C CA  . ILE A 365 ? 0.1876 0.1838 0.1447 0.0597  0.0141  -0.0049 365 ILE A CA  
3103 C C   . ILE A 365 ? 0.2408 0.2407 0.1928 0.0708  0.0134  -0.0139 365 ILE A C   
3104 O O   . ILE A 365 ? 0.2304 0.2424 0.1871 0.0726  0.0193  -0.0095 365 ILE A O   
3105 C CB  . ILE A 365 ? 0.1954 0.2075 0.1456 0.0613  0.0154  -0.0025 365 ILE A CB  
3106 C CG1 . ILE A 365 ? 0.2038 0.2128 0.1604 0.0519  0.0166  0.0078  365 ILE A CG1 
3107 C CG2 . ILE A 365 ? 0.2604 0.2972 0.2072 0.0668  0.0226  0.0020  365 ILE A CG2 
3108 C CD1 . ILE A 365 ? 0.2054 0.2262 0.1549 0.0535  0.0155  0.0099  365 ILE A CD1 
3109 N N   . PRO A 366 ? 0.2162 0.2057 0.1591 0.0790  0.0057  -0.0269 366 PRO A N   
3110 C CA  . PRO A 366 ? 0.2568 0.2474 0.1952 0.0918  0.0045  -0.0360 366 PRO A CA  
3111 C C   . PRO A 366 ? 0.2446 0.2240 0.1923 0.0891  0.0052  -0.0320 366 PRO A C   
3112 O O   . PRO A 366 ? 0.2501 0.2437 0.1996 0.0970  0.0094  -0.0322 366 PRO A O   
3113 C CB  . PRO A 366 ? 0.2807 0.2522 0.2074 0.0992  -0.0068 -0.0511 366 PRO A CB  
3114 C CG  . PRO A 366 ? 0.2733 0.2504 0.1958 0.0933  -0.0083 -0.0500 366 PRO A CG  
3115 C CD  . PRO A 366 ? 0.2321 0.2109 0.1671 0.0785  -0.0028 -0.0347 366 PRO A CD  
3116 N N   . PHE A 367 ? 0.2350 0.1930 0.1892 0.0780  0.0014  -0.0275 367 PHE A N   
3117 C CA  . PHE A 367 ? 0.2415 0.1903 0.2034 0.0756  0.0018  -0.0231 367 PHE A CA  
3118 C C   . PHE A 367 ? 0.2212 0.1905 0.1917 0.0715  0.0114  -0.0130 367 PHE A C   
3119 O O   . PHE A 367 ? 0.2200 0.1977 0.1936 0.0770  0.0137  -0.0128 367 PHE A O   
3120 C CB  . PHE A 367 ? 0.2204 0.1466 0.1868 0.0639  -0.0036 -0.0189 367 PHE A CB  
3121 C CG  . PHE A 367 ? 0.2201 0.1412 0.1943 0.0599  -0.0019 -0.0120 367 PHE A CG  
3122 C CD1 . PHE A 367 ? 0.2648 0.1739 0.2370 0.0675  -0.0066 -0.0160 367 PHE A CD1 
3123 C CD2 . PHE A 367 ? 0.2114 0.1398 0.1937 0.0499  0.0039  -0.0021 367 PHE A CD2 
3124 C CE1 . PHE A 367 ? 0.2125 0.1188 0.1910 0.0642  -0.0054 -0.0091 367 PHE A CE1 
3125 C CE2 . PHE A 367 ? 0.2135 0.1391 0.2015 0.0469  0.0051  0.0033  367 PHE A CE2 
3126 C CZ  . PHE A 367 ? 0.2117 0.1273 0.1979 0.0536  0.0006  0.0003  367 PHE A CZ  
3127 N N   . LEU A 368 ? 0.1847 0.1616 0.1593 0.0620  0.0160  -0.0046 368 LEU A N   
3128 C CA  . LEU A 368 ? 0.1634 0.1535 0.1461 0.0562  0.0229  0.0048  368 LEU A CA  
3129 C C   . LEU A 368 ? 0.1875 0.2033 0.1696 0.0623  0.0283  0.0060  368 LEU A C   
3130 O O   . LEU A 368 ? 0.2123 0.2395 0.2012 0.0608  0.0318  0.0104  368 LEU A O   
3131 C CB  . LEU A 368 ? 0.1845 0.1728 0.1705 0.0462  0.0251  0.0128  368 LEU A CB  
3132 C CG  . LEU A 368 ? 0.1743 0.1453 0.1646 0.0392  0.0222  0.0148  368 LEU A CG  
3133 C CD1 . LEU A 368 ? 0.2222 0.1938 0.2149 0.0326  0.0244  0.0214  368 LEU A CD1 
3134 C CD2 . LEU A 368 ? 0.1719 0.1395 0.1677 0.0376  0.0228  0.0165  368 LEU A CD2 
3135 N N   . GLU A 369 ? 0.2000 0.2284 0.1741 0.0686  0.0291  0.0026  369 GLU A N   
3136 C CA  . GLU A 369 ? 0.2106 0.2690 0.1839 0.0749  0.0348  0.0044  369 GLU A CA  
3137 C C   . GLU A 369 ? 0.2450 0.3100 0.2191 0.0861  0.0338  -0.0028 369 GLU A C   
3138 O O   . GLU A 369 ? 0.2174 0.3052 0.1984 0.0861  0.0389  0.0027  369 GLU A O   
3139 C CB  . GLU A 369 ? 0.1968 0.2689 0.1591 0.0817  0.0353  0.0009  369 GLU A CB  
3140 C CG  . GLU A 369 ? 0.1928 0.2653 0.1553 0.0713  0.0373  0.0110  369 GLU A CG  
3141 C CD  . GLU A 369 ? 0.2601 0.3506 0.2115 0.0775  0.0383  0.0097  369 GLU A CD  
3142 O OE1 . GLU A 369 ? 0.2740 0.3732 0.2157 0.0908  0.0362  -0.0021 369 GLU A OE1 
3143 O OE2 . GLU A 369 ? 0.2597 0.3553 0.2112 0.0699  0.0407  0.0204  369 GLU A OE2 
3144 N N   . LYS A 370 ? 0.2194 0.2639 0.1869 0.0954  0.0266  -0.0146 370 LYS A N   
3145 C CA  . LYS A 370 ? 0.2177 0.2650 0.1850 0.1082  0.0244  -0.0218 370 LYS A CA  
3146 C C   . LYS A 370 ? 0.2057 0.2476 0.1842 0.1008  0.0251  -0.0146 370 LYS A C   
3147 O O   . LYS A 370 ? 0.2011 0.2627 0.1848 0.1069  0.0278  -0.0137 370 LYS A O   
3148 C CB  . LYS A 370 ? 0.2618 0.2823 0.2183 0.1192  0.0145  -0.0357 370 LYS A CB  
3149 C CG  . LYS A 370 ? 0.4220 0.4431 0.3763 0.1358  0.0110  -0.0443 370 LYS A CG  
3150 C CD  . LYS A 370 ? 0.5624 0.5503 0.5062 0.1408  -0.0013 -0.0558 370 LYS A CD  
3151 C CE  . LYS A 370 ? 0.6518 0.6478 0.5830 0.1499  -0.0043 -0.0664 370 LYS A CE  
3152 N NZ  . LYS A 370 ? 0.6509 0.6884 0.5820 0.1575  0.0036  -0.0648 370 LYS A NZ  
3153 N N   . LEU A 371 ? 0.1938 0.2129 0.1763 0.0880  0.0228  -0.0093 371 LEU A N   
3154 C CA  . LEU A 371 ? 0.1813 0.1961 0.1727 0.0816  0.0230  -0.0032 371 LEU A CA  
3155 C C   . LEU A 371 ? 0.1729 0.2146 0.1733 0.0750  0.0300  0.0056  371 LEU A C   
3156 O O   . LEU A 371 ? 0.1817 0.2370 0.1882 0.0780  0.0309  0.0068  371 LEU A O   
3157 C CB  . LEU A 371 ? 0.2172 0.2075 0.2101 0.0697  0.0201  0.0009  371 LEU A CB  
3158 C CG  . LEU A 371 ? 0.2290 0.2166 0.2296 0.0627  0.0205  0.0072  371 LEU A CG  
3159 C CD1 . LEU A 371 ? 0.2433 0.2227 0.2429 0.0715  0.0154  0.0035  371 LEU A CD1 
3160 C CD2 . LEU A 371 ? 0.2135 0.1847 0.2151 0.0514  0.0195  0.0117  371 LEU A CD2 
3161 N N   . TYR A 372 ? 0.1801 0.2299 0.1817 0.0659  0.0343  0.0121  372 TYR A N   
3162 C CA  . TYR A 372 ? 0.1799 0.2504 0.1902 0.0566  0.0394  0.0219  372 TYR A CA  
3163 C C   . TYR A 372 ? 0.1829 0.2877 0.1955 0.0643  0.0435  0.0223  372 TYR A C   
3164 O O   . TYR A 372 ? 0.2021 0.3260 0.2242 0.0598  0.0456  0.0279  372 TYR A O   
3165 C CB  . TYR A 372 ? 0.1445 0.2114 0.1540 0.0458  0.0417  0.0294  372 TYR A CB  
3166 C CG  . TYR A 372 ? 0.1672 0.2065 0.1766 0.0380  0.0385  0.0304  372 TYR A CG  
3167 C CD1 . TYR A 372 ? 0.1453 0.1691 0.1572 0.0370  0.0351  0.0276  372 TYR A CD1 
3168 C CD2 . TYR A 372 ? 0.1497 0.1813 0.1561 0.0326  0.0390  0.0346  372 TYR A CD2 
3169 C CE1 . TYR A 372 ? 0.1319 0.1358 0.1435 0.0308  0.0330  0.0287  372 TYR A CE1 
3170 C CE2 . TYR A 372 ? 0.1615 0.1720 0.1680 0.0273  0.0365  0.0352  372 TYR A CE2 
3171 C CZ  . TYR A 372 ? 0.1409 0.1392 0.1502 0.0265  0.0338  0.0320  372 TYR A CZ  
3172 O OH  . TYR A 372 ? 0.1822 0.1650 0.1914 0.0223  0.0321  0.0327  372 TYR A OH  
3173 N N   . SER A 373 ? 0.1583 0.2736 0.1623 0.0765  0.0443  0.0158  373 SER A N   
3174 C CA  . SER A 373 ? 0.2001 0.3525 0.2054 0.0870  0.0485  0.0149  373 SER A CA  
3175 C C   . SER A 373 ? 0.1963 0.3533 0.2061 0.0973  0.0459  0.0092  373 SER A C   
3176 O O   . SER A 373 ? 0.2101 0.3996 0.2288 0.0981  0.0497  0.0140  373 SER A O   
3177 C CB  . SER A 373 ? 0.2367 0.3973 0.2291 0.1012  0.0488  0.0061  373 SER A CB  
3178 O OG  . SER A 373 ? 0.2529 0.4462 0.2449 0.1099  0.0505  0.0049  373 SER A OG  
3179 N N   . THR A 374 ? 0.2063 0.3316 0.2105 0.1045  0.0390  0.0002  374 THR A N   
3180 C CA  . THR A 374 ? 0.2131 0.3396 0.2201 0.1158  0.0353  -0.0048 374 THR A CA  
3181 C C   . THR A 374 ? 0.2104 0.3415 0.2298 0.1032  0.0360  0.0044  374 THR A C   
3182 O O   . THR A 374 ? 0.2012 0.3566 0.2278 0.1093  0.0368  0.0053  374 THR A O   
3183 C CB  . THR A 374 ? 0.2345 0.3226 0.2317 0.1249  0.0266  -0.0149 374 THR A CB  
3184 O OG1 . THR A 374 ? 0.2478 0.3298 0.2325 0.1340  0.0239  -0.0244 374 THR A OG1 
3185 C CG2 . THR A 374 ? 0.2410 0.3256 0.2392 0.1347  0.0211  -0.0186 374 THR A CG2 
3186 N N   . LEU A 375 ? 0.1952 0.3055 0.2170 0.0866  0.0355  0.0108  375 LEU A N   
3187 C CA  . LEU A 375 ? 0.1762 0.2888 0.2078 0.0752  0.0350  0.0177  375 LEU A CA  
3188 C C   . LEU A 375 ? 0.2153 0.3648 0.2577 0.0681  0.0399  0.0256  375 LEU A C   
3189 O O   . LEU A 375 ? 0.1972 0.3632 0.2484 0.0670  0.0389  0.0280  375 LEU A O   
3190 C CB  . LEU A 375 ? 0.2081 0.2933 0.2386 0.0607  0.0336  0.0216  375 LEU A CB  
3191 C CG  . LEU A 375 ? 0.2259 0.2780 0.2492 0.0633  0.0283  0.0171  375 LEU A CG  
3192 C CD1 . LEU A 375 ? 0.2275 0.2616 0.2504 0.0500  0.0286  0.0213  375 LEU A CD1 
3193 C CD2 . LEU A 375 ? 0.2190 0.2676 0.2444 0.0686  0.0240  0.0159  375 LEU A CD2 
3194 N N   . GLU A 376 ? 0.1987 0.3629 0.2411 0.0622  0.0448  0.0308  376 GLU A N   
3195 C CA  . GLU A 376 ? 0.2133 0.4123 0.2667 0.0519  0.0491  0.0411  376 GLU A CA  
3196 C C   . GLU A 376 ? 0.2265 0.4669 0.2852 0.0648  0.0519  0.0395  376 GLU A C   
3197 O O   . GLU A 376 ? 0.2890 0.5567 0.3564 0.0545  0.0531  0.0480  376 GLU A O   
3198 C CB  . GLU A 376 ? 0.1842 0.3872 0.2350 0.0423  0.0532  0.0490  376 GLU A CB  
3199 C CG  . GLU A 376 ? 0.2315 0.4554 0.2743 0.0561  0.0576  0.0455  376 GLU A CG  
3200 C CD  . GLU A 376 ? 0.3064 0.5296 0.3442 0.0473  0.0608  0.0534  376 GLU A CD  
3201 O OE1 . GLU A 376 ? 0.3345 0.5423 0.3763 0.0303  0.0597  0.0628  376 GLU A OE1 
3202 O OE2 . GLU A 376 ? 0.2454 0.4777 0.2733 0.0576  0.0620  0.0490  376 GLU A OE2 
3203 N N   . LYS A 377 ? 0.1675 0.4021 0.2172 0.0845  0.0491  0.0279  377 LYS A N   
3204 C CA  . LYS A 377 ? 0.2036 0.4619 0.2512 0.0961  0.0474  0.0237  377 LYS A CA  
3205 C C   . LYS A 377 ? 0.2148 0.4670 0.2649 0.1054  0.0422  0.0184  377 LYS A C   
3206 O O   . LYS A 377 ? 0.2669 0.5324 0.3126 0.1185  0.0398  0.0130  377 LYS A O   
3207 C CB  . LYS A 377 ? 0.2237 0.4781 0.2561 0.1113  0.0465  0.0142  377 LYS A CB  
3208 C CG  . LYS A 377 ? 0.2252 0.4912 0.2538 0.1040  0.0512  0.0199  377 LYS A CG  
3209 C CD  . LYS A 377 ? 0.2950 0.5494 0.3074 0.1187  0.0490  0.0088  377 LYS A CD  
3210 C CE  . LYS A 377 ? 0.2861 0.5583 0.2948 0.1125  0.0533  0.0154  377 LYS A CE  
3211 N NZ  . LYS A 377 ? 0.2914 0.5506 0.3053 0.0952  0.0568  0.0256  377 LYS A NZ  
3212 N N   . GLU A 378 ? 0.1794 0.4116 0.2353 0.0998  0.0400  0.0200  378 GLU A N   
3213 C CA  . GLU A 378 ? 0.2054 0.4327 0.2644 0.1065  0.0345  0.0174  378 GLU A CA  
3214 C C   . GLU A 378 ? 0.1710 0.4230 0.2455 0.0913  0.0354  0.0269  378 GLU A C   
3215 O O   . GLU A 378 ? 0.1917 0.4271 0.2692 0.0743  0.0348  0.0321  378 GLU A O   
3216 C CB  . GLU A 378 ? 0.2515 0.4366 0.3034 0.1104  0.0292  0.0130  378 GLU A CB  
3217 C CG  . GLU A 378 ? 0.2732 0.4307 0.3104 0.1235  0.0263  0.0034  378 GLU A CG  
3218 C CD  . GLU A 378 ? 0.5027 0.6623 0.5318 0.1393  0.0217  -0.0047 378 GLU A CD  
3219 O OE1 . GLU A 378 ? 0.5984 0.7715 0.6324 0.1433  0.0194  -0.0034 378 GLU A OE1 
3220 O OE2 . GLU A 378 ? 0.6433 0.7913 0.6607 0.1480  0.0200  -0.0127 378 GLU A OE2 
3221 N N   . GLU A 379 ? 0.2074 0.4881 0.2864 0.0943  0.0342  0.0279  379 GLU A N   
3222 C CA  . GLU A 379 ? 0.2749 0.5806 0.3683 0.0785  0.0336  0.0365  379 GLU A CA  
3223 C C   . GLU A 379 ? 0.2385 0.5294 0.3377 0.0741  0.0287  0.0370  379 GLU A C   
3224 O O   . GLU A 379 ? 0.2543 0.5545 0.3638 0.0561  0.0273  0.0436  379 GLU A O   
3225 C CB  . GLU A 379 ? 0.3316 0.6698 0.4279 0.0847  0.0323  0.0368  379 GLU A CB  
3226 C CG  . GLU A 379 ? 0.5233 0.8506 0.6079 0.1078  0.0295  0.0267  379 GLU A CG  
3227 C CD  . GLU A 379 ? 0.7466 1.1101 0.8336 0.1132  0.0298  0.0280  379 GLU A CD  
3228 O OE1 . GLU A 379 ? 0.7866 1.1720 0.8735 0.1091  0.0343  0.0317  379 GLU A OE1 
3229 O OE2 . GLU A 379 ? 0.7527 1.1220 0.8401 0.1235  0.0257  0.0250  379 GLU A OE2 
3230 N N   . TRP A 380 ? 0.1909 0.4576 0.2818 0.0895  0.0245  0.0303  380 TRP A N   
3231 C CA  . TRP A 380 ? 0.1672 0.4140 0.2571 0.0850  0.0182  0.0307  380 TRP A CA  
3232 C C   . TRP A 380 ? 0.1844 0.3898 0.2655 0.0716  0.0172  0.0310  380 TRP A C   
3233 O O   . TRP A 380 ? 0.2003 0.3896 0.2792 0.0664  0.0125  0.0315  380 TRP A O   
3234 C CB  . TRP A 380 ? 0.2017 0.4394 0.2853 0.1066  0.0131  0.0254  380 TRP A CB  
3235 C CG  . TRP A 380 ? 0.2157 0.4229 0.2853 0.1196  0.0131  0.0186  380 TRP A CG  
3236 C CD1 . TRP A 380 ? 0.2620 0.4735 0.3241 0.1296  0.0152  0.0127  380 TRP A CD1 
3237 C CD2 . TRP A 380 ? 0.2045 0.3676 0.2627 0.1196  0.0097  0.0167  380 TRP A CD2 
3238 N NE1 . TRP A 380 ? 0.2895 0.4644 0.3386 0.1374  0.0127  0.0065  380 TRP A NE1 
3239 C CE2 . TRP A 380 ? 0.2198 0.3660 0.2675 0.1321  0.0094  0.0095  380 TRP A CE2 
3240 C CE3 . TRP A 380 ? 0.1683 0.3033 0.2222 0.1080  0.0064  0.0203  380 TRP A CE3 
3241 C CZ2 . TRP A 380 ? 0.2346 0.3397 0.2711 0.1341  0.0056  0.0068  380 TRP A CZ2 
3242 C CZ3 . TRP A 380 ? 0.2368 0.3329 0.2792 0.1093  0.0037  0.0185  380 TRP A CZ3 
3243 C CH2 . TRP A 380 ? 0.2656 0.3470 0.3003 0.1217  0.0030  0.0122  380 TRP A CH2 
3244 N N   . ILE A 381 ? 0.1462 0.3366 0.2219 0.0671  0.0215  0.0306  381 ILE A N   
3245 C CA  . ILE A 381 ? 0.1447 0.3015 0.2136 0.0545  0.0211  0.0314  381 ILE A CA  
3246 C C   . ILE A 381 ? 0.1318 0.2990 0.2079 0.0361  0.0236  0.0373  381 ILE A C   
3247 O O   . ILE A 381 ? 0.1716 0.3609 0.2527 0.0338  0.0280  0.0409  381 ILE A O   
3248 C CB  . ILE A 381 ? 0.1718 0.3023 0.2295 0.0615  0.0228  0.0273  381 ILE A CB  
3249 C CG1 . ILE A 381 ? 0.2264 0.3401 0.2763 0.0779  0.0183  0.0220  381 ILE A CG1 
3250 C CG2 . ILE A 381 ? 0.1660 0.2679 0.2185 0.0483  0.0228  0.0289  381 ILE A CG2 
3251 C CD1 . ILE A 381 ? 0.1937 0.2825 0.2331 0.0846  0.0183  0.0172  381 ILE A CD1 
3252 N N   . GLU A 382 ? 0.1445 0.2948 0.2201 0.0232  0.0202  0.0383  382 GLU A N   
3253 C CA  . GLU A 382 ? 0.1226 0.2708 0.2021 0.0058  0.0206  0.0430  382 GLU A CA  
3254 C C   . GLU A 382 ? 0.1234 0.2349 0.1926 0.0022  0.0197  0.0403  382 GLU A C   
3255 O O   . GLU A 382 ? 0.1657 0.2615 0.2302 0.0025  0.0158  0.0367  382 GLU A O   
3256 C CB  . GLU A 382 ? 0.1711 0.3362 0.2605 -0.0067 0.0157  0.0457  382 GLU A CB  
3257 C CG  . GLU A 382 ? 0.2567 0.4139 0.3495 -0.0257 0.0141  0.0506  382 GLU A CG  
3258 C CD  . GLU A 382 ? 0.3226 0.4936 0.4249 -0.0399 0.0073  0.0525  382 GLU A CD  
3259 O OE1 . GLU A 382 ? 0.3062 0.5033 0.4154 -0.0354 0.0053  0.0518  382 GLU A OE1 
3260 O OE2 . GLU A 382 ? 0.3913 0.5464 0.4942 -0.0553 0.0032  0.0546  382 GLU A OE2 
3261 N N   . THR A 383 ? 0.1601 0.2608 0.2257 -0.0001 0.0234  0.0423  383 THR A N   
3262 C CA  . THR A 383 ? 0.1520 0.2221 0.2093 -0.0039 0.0225  0.0404  383 THR A CA  
3263 C C   . THR A 383 ? 0.1453 0.2079 0.2055 -0.0183 0.0186  0.0426  383 THR A C   
3264 O O   . THR A 383 ? 0.1777 0.2560 0.2463 -0.0285 0.0178  0.0482  383 THR A O   
3265 C CB  . THR A 383 ? 0.1468 0.2087 0.1990 -0.0007 0.0268  0.0418  383 THR A CB  
3266 O OG1 . THR A 383 ? 0.1507 0.2300 0.2086 -0.0078 0.0296  0.0488  383 THR A OG1 
3267 C CG2 . THR A 383 ? 0.1492 0.2124 0.1965 0.0136  0.0287  0.0376  383 THR A CG2 
3268 N N   . LEU A 384 ? 0.1414 0.1798 0.1944 -0.0190 0.0156  0.0380  384 LEU A N   
3269 C CA  . LEU A 384 ? 0.1476 0.1745 0.2010 -0.0300 0.0100  0.0368  384 LEU A CA  
3270 C C   . LEU A 384 ? 0.1515 0.1516 0.1971 -0.0307 0.0097  0.0353  384 LEU A C   
3271 O O   . LEU A 384 ? 0.1724 0.1626 0.2113 -0.0218 0.0130  0.0330  384 LEU A O   
3272 C CB  . LEU A 384 ? 0.1770 0.2035 0.2278 -0.0283 0.0050  0.0304  384 LEU A CB  
3273 C CG  . LEU A 384 ? 0.1661 0.2185 0.2241 -0.0269 0.0033  0.0310  384 LEU A CG  
3274 C CD1 . LEU A 384 ? 0.1847 0.2325 0.2375 -0.0263 -0.0025 0.0246  384 LEU A CD1 
3275 C CD2 . LEU A 384 ? 0.1702 0.2438 0.2404 -0.0386 0.0017  0.0369  384 LEU A CD2 
3276 N N   . THR A 385 ? 0.1798 0.1679 0.2264 -0.0415 0.0049  0.0368  385 THR A N   
3277 C CA  . THR A 385 ? 0.1795 0.1399 0.2176 -0.0400 0.0024  0.0329  385 THR A CA  
3278 C C   . THR A 385 ? 0.2272 0.1790 0.2581 -0.0343 -0.0014 0.0228  385 THR A C   
3279 O O   . THR A 385 ? 0.1852 0.1503 0.2182 -0.0348 -0.0036 0.0198  385 THR A O   
3280 C CB  . THR A 385 ? 0.1952 0.1405 0.2353 -0.0525 -0.0036 0.0370  385 THR A CB  
3281 O OG1 . THR A 385 ? 0.2071 0.1530 0.2507 -0.0622 -0.0115 0.0336  385 THR A OG1 
3282 C CG2 . THR A 385 ? 0.2254 0.1846 0.2731 -0.0601 0.0001  0.0495  385 THR A CG2 
3283 N N   . LEU A 386 ? 0.1939 0.1259 0.2159 -0.0280 -0.0021 0.0176  386 LEU A N   
3284 C CA  . LEU A 386 ? 0.1931 0.1191 0.2069 -0.0221 -0.0057 0.0078  386 LEU A CA  
3285 C C   . LEU A 386 ? 0.2108 0.1307 0.2248 -0.0308 -0.0148 0.0024  386 LEU A C   
3286 O O   . LEU A 386 ? 0.2317 0.1597 0.2425 -0.0286 -0.0179 -0.0040 386 LEU A O   
3287 C CB  . LEU A 386 ? 0.2001 0.1090 0.2049 -0.0130 -0.0050 0.0031  386 LEU A CB  
3288 C CG  . LEU A 386 ? 0.2153 0.1301 0.2198 -0.0053 0.0028  0.0076  386 LEU A CG  
3289 C CD1 . LEU A 386 ? 0.2187 0.1201 0.2151 0.0037  0.0024  0.0025  386 LEU A CD1 
3290 C CD2 . LEU A 386 ? 0.2001 0.1334 0.2054 -0.0011 0.0070  0.0087  386 LEU A CD2 
3291 N N   . GLU A 387 ? 0.2265 0.1319 0.2439 -0.0414 -0.0202 0.0056  387 GLU A N   
3292 C CA  . GLU A 387 ? 0.2464 0.1447 0.2655 -0.0530 -0.0306 0.0015  387 GLU A CA  
3293 C C   . GLU A 387 ? 0.2366 0.1635 0.2649 -0.0593 -0.0307 0.0042  387 GLU A C   
3294 O O   . GLU A 387 ? 0.2526 0.1826 0.2784 -0.0610 -0.0374 -0.0038 387 GLU A O   
3295 C CB  . GLU A 387 ? 0.2656 0.1455 0.2892 -0.0660 -0.0358 0.0089  387 GLU A CB  
3296 C CG  . GLU A 387 ? 0.7152 0.5732 0.7369 -0.0777 -0.0497 0.0026  387 GLU A CG  
3297 C CD  . GLU A 387 ? 0.8946 0.7169 0.9018 -0.0682 -0.0565 -0.0093 387 GLU A CD  
3298 O OE1 . GLU A 387 ? 0.9484 0.7541 0.9515 -0.0615 -0.0535 -0.0059 387 GLU A OE1 
3299 O OE2 . GLU A 387 ? 0.9723 0.7854 0.9714 -0.0654 -0.0647 -0.0229 387 GLU A OE2 
3300 N N   . GLU A 388 ? 0.2172 0.1669 0.2556 -0.0613 -0.0236 0.0147  388 GLU A N   
3301 C CA  . GLU A 388 ? 0.2344 0.2138 0.2822 -0.0653 -0.0237 0.0174  388 GLU A CA  
3302 C C   . GLU A 388 ? 0.1976 0.1872 0.2393 -0.0530 -0.0220 0.0106  388 GLU A C   
3303 O O   . GLU A 388 ? 0.2347 0.2391 0.2790 -0.0558 -0.0270 0.0075  388 GLU A O   
3304 C CB  . GLU A 388 ? 0.2323 0.2350 0.2905 -0.0666 -0.0160 0.0288  388 GLU A CB  
3305 C CG  . GLU A 388 ? 0.2425 0.2442 0.3089 -0.0816 -0.0181 0.0384  388 GLU A CG  
3306 C CD  . GLU A 388 ? 0.3049 0.3306 0.3787 -0.0802 -0.0093 0.0491  388 GLU A CD  
3307 O OE1 . GLU A 388 ? 0.2097 0.2372 0.2784 -0.0664 -0.0018 0.0479  388 GLU A OE1 
3308 O OE2 . GLU A 388 ? 0.3504 0.3941 0.4351 -0.0933 -0.0103 0.0588  388 GLU A OE2 
3309 N N   . ALA A 389 ? 0.1977 0.1806 0.2314 -0.0401 -0.0156 0.0091  389 ALA A N   
3310 C CA  . ALA A 389 ? 0.2024 0.1942 0.2298 -0.0296 -0.0142 0.0051  389 ALA A CA  
3311 C C   . ALA A 389 ? 0.2565 0.2402 0.2748 -0.0293 -0.0216 -0.0051 389 ALA A C   
3312 O O   . ALA A 389 ? 0.2314 0.2297 0.2476 -0.0264 -0.0241 -0.0078 389 ALA A O   
3313 C CB  . ALA A 389 ? 0.2129 0.1984 0.2344 -0.0187 -0.0067 0.0070  389 ALA A CB  
3314 N N   . MET A 390 ? 0.2512 0.2117 0.2629 -0.0311 -0.0257 -0.0114 390 MET A N   
3315 C CA  . MET A 390 ? 0.2898 0.2409 0.2908 -0.0291 -0.0336 -0.0235 390 MET A CA  
3316 C C   . MET A 390 ? 0.3183 0.2777 0.3241 -0.0403 -0.0432 -0.0268 390 MET A C   
3317 O O   . MET A 390 ? 0.3425 0.3081 0.3405 -0.0368 -0.0486 -0.0354 390 MET A O   
3318 C CB  . MET A 390 ? 0.3294 0.2511 0.3224 -0.0275 -0.0371 -0.0302 390 MET A CB  
3319 C CG  . MET A 390 ? 0.3664 0.2763 0.3453 -0.0212 -0.0450 -0.0452 390 MET A CG  
3320 S SD  . MET A 390 ? 0.5191 0.3916 0.4884 -0.0167 -0.0502 -0.0536 390 MET A SD  
3321 C CE  . MET A 390 ? 0.4764 0.3295 0.4564 -0.0374 -0.0605 -0.0488 390 MET A CE  
3322 N N   . ARG A 391 ? 0.2442 0.2069 0.2628 -0.0541 -0.0458 -0.0196 391 ARG A N   
3323 C CA  . ARG A 391 ? 0.2681 0.2370 0.2928 -0.0679 -0.0566 -0.0224 391 ARG A CA  
3324 C C   . ARG A 391 ? 0.2432 0.2478 0.2808 -0.0718 -0.0546 -0.0145 391 ARG A C   
3325 O O   . ARG A 391 ? 0.3019 0.3182 0.3462 -0.0834 -0.0636 -0.0162 391 ARG A O   
3326 C CB  . ARG A 391 ? 0.3383 0.2864 0.3690 -0.0836 -0.0631 -0.0191 391 ARG A CB  
3327 C CG  . ARG A 391 ? 0.3619 0.2720 0.3799 -0.0791 -0.0667 -0.0268 391 ARG A CG  
3328 C CD  . ARG A 391 ? 0.4921 0.3784 0.5153 -0.0964 -0.0767 -0.0237 391 ARG A CD  
3329 N NE  . ARG A 391 ? 0.6848 0.5311 0.6939 -0.0901 -0.0829 -0.0336 391 ARG A NE  
3330 C CZ  . ARG A 391 ? 0.7825 0.6094 0.7785 -0.0854 -0.0936 -0.0502 391 ARG A CZ  
3331 N NH1 . ARG A 391 ? 0.7972 0.6413 0.7920 -0.0875 -0.0993 -0.0583 391 ARG A NH1 
3332 N NH2 . ARG A 391 ? 0.8271 0.6178 0.8101 -0.0771 -0.0989 -0.0594 391 ARG A NH2 
3333 N N   . LYS A 392 ? 0.2752 0.2970 0.3165 -0.0620 -0.0441 -0.0066 392 LYS A N   
3334 C CA  . LYS A 392 ? 0.2935 0.3490 0.3469 -0.0626 -0.0420 0.0006  392 LYS A CA  
3335 C C   . LYS A 392 ? 0.2810 0.3526 0.3319 -0.0613 -0.0493 -0.0056 392 LYS A C   
3336 O O   . LYS A 392 ? 0.2598 0.3247 0.2976 -0.0509 -0.0498 -0.0123 392 LYS A O   
3337 C CB  . LYS A 392 ? 0.2619 0.3257 0.3150 -0.0486 -0.0310 0.0070  392 LYS A CB  
3338 C CG  . LYS A 392 ? 0.2903 0.3816 0.3576 -0.0497 -0.0267 0.0164  392 LYS A CG  
3339 C CD  . LYS A 392 ? 0.3214 0.4089 0.3967 -0.0611 -0.0247 0.0228  392 LYS A CD  
3340 C CE  . LYS A 392 ? 0.3257 0.4453 0.4141 -0.0605 -0.0194 0.0319  392 LYS A CE  
3341 N NZ  . LYS A 392 ? 0.3924 0.5443 0.4921 -0.0661 -0.0250 0.0331  392 LYS A NZ  
3342 N N   . GLU A 393 ? 0.2768 0.3727 0.3404 -0.0720 -0.0553 -0.0027 393 GLU A N   
3343 C CA  . GLU A 393 ? 0.2816 0.3942 0.3431 -0.0719 -0.0638 -0.0089 393 GLU A CA  
3344 C C   . GLU A 393 ? 0.2398 0.3825 0.3051 -0.0592 -0.0592 -0.0032 393 GLU A C   
3345 O O   . GLU A 393 ? 0.3315 0.4822 0.3886 -0.0519 -0.0633 -0.0080 393 GLU A O   
3346 C CB  . GLU A 393 ? 0.3651 0.4885 0.4383 -0.0917 -0.0751 -0.0097 393 GLU A CB  
3347 C CG  . GLU A 393 ? 0.5181 0.6060 0.5841 -0.1038 -0.0839 -0.0181 393 GLU A CG  
3348 C CD  . GLU A 393 ? 0.7145 0.8096 0.7936 -0.1266 -0.0961 -0.0168 393 GLU A CD  
3349 O OE1 . GLU A 393 ? 0.7397 0.8718 0.8357 -0.1340 -0.0959 -0.0077 393 GLU A OE1 
3350 O OE2 . GLU A 393 ? 0.7897 0.8534 0.8621 -0.1372 -0.1065 -0.0250 393 GLU A OE2 
3351 N N   . ASP A 394 ? 0.2183 0.3772 0.2945 -0.0553 -0.0512 0.0066  394 ASP A N   
3352 C CA  . ASP A 394 ? 0.2580 0.4446 0.3386 -0.0422 -0.0482 0.0118  394 ASP A CA  
3353 C C   . ASP A 394 ? 0.2601 0.4307 0.3285 -0.0248 -0.0408 0.0130  394 ASP A C   
3354 O O   . ASP A 394 ? 0.2569 0.4359 0.3291 -0.0141 -0.0347 0.0191  394 ASP A O   
3355 C CB  . ASP A 394 ? 0.2953 0.5097 0.3933 -0.0449 -0.0441 0.0205  394 ASP A CB  
3356 C CG  . ASP A 394 ? 0.3727 0.5711 0.4725 -0.0484 -0.0363 0.0247  394 ASP A CG  
3357 O OD1 . ASP A 394 ? 0.3994 0.5643 0.4881 -0.0499 -0.0350 0.0208  394 ASP A OD1 
3358 O OD2 . ASP A 394 ? 0.4041 0.6258 0.5159 -0.0485 -0.0315 0.0319  394 ASP A OD2 
3359 N N   . VAL A 395 ? 0.2012 0.3491 0.2544 -0.0219 -0.0421 0.0071  395 VAL A N   
3360 C CA  . VAL A 395 ? 0.2031 0.3366 0.2447 -0.0084 -0.0361 0.0093  395 VAL A CA  
3361 C C   . VAL A 395 ? 0.2148 0.3500 0.2436 -0.0035 -0.0412 0.0052  395 VAL A C   
3362 O O   . VAL A 395 ? 0.2645 0.4072 0.2916 -0.0103 -0.0492 -0.0017 395 VAL A O   
3363 C CB  . VAL A 395 ? 0.1933 0.2985 0.2288 -0.0094 -0.0299 0.0081  395 VAL A CB  
3364 C CG1 . VAL A 395 ? 0.2274 0.3324 0.2741 -0.0140 -0.0249 0.0127  395 VAL A CG1 
3365 C CG2 . VAL A 395 ? 0.2227 0.3112 0.2496 -0.0167 -0.0347 -0.0012 395 VAL A CG2 
3366 N N   . LYS A 396 ? 0.1817 0.3105 0.2010 0.0078  -0.0370 0.0099  396 LYS A N   
3367 C CA  . LYS A 396 ? 0.1939 0.3272 0.2000 0.0133  -0.0407 0.0085  396 LYS A CA  
3368 C C   . LYS A 396 ? 0.1973 0.3118 0.1905 0.0126  -0.0384 0.0025  396 LYS A C   
3369 O O   . LYS A 396 ? 0.1910 0.2877 0.1840 0.0127  -0.0319 0.0039  396 LYS A O   
3370 C CB  . LYS A 396 ? 0.2373 0.3763 0.2402 0.0253  -0.0386 0.0191  396 LYS A CB  
3371 C CG  . LYS A 396 ? 0.3082 0.4702 0.3211 0.0298  -0.0430 0.0236  396 LYS A CG  
3372 C CD  . LYS A 396 ? 0.4058 0.5754 0.4109 0.0416  -0.0454 0.0322  396 LYS A CD  
3373 C CE  . LYS A 396 ? 0.5080 0.7062 0.5155 0.0431  -0.0541 0.0311  396 LYS A CE  
3374 N NZ  . LYS A 396 ? 0.5442 0.7632 0.5690 0.0398  -0.0568 0.0289  396 LYS A NZ  
3375 N N   . THR A 397 ? 0.1612 0.2446 0.2958 0.0431  -0.0340 0.0126  397 THR A N   
3376 C CA  . THR A 397 ? 0.1607 0.2233 0.2768 0.0352  -0.0359 0.0129  397 THR A CA  
3377 C C   . THR A 397 ? 0.1686 0.2143 0.2709 0.0383  -0.0452 0.0123  397 THR A C   
3378 O O   . THR A 397 ? 0.1746 0.2260 0.2840 0.0445  -0.0524 0.0130  397 THR A O   
3379 C CB  . THR A 397 ? 0.1616 0.2305 0.2863 0.0235  -0.0387 0.0153  397 THR A CB  
3380 O OG1 . THR A 397 ? 0.1655 0.2430 0.3017 0.0225  -0.0494 0.0153  397 THR A OG1 
3381 C CG2 . THR A 397 ? 0.1516 0.2403 0.2925 0.0192  -0.0302 0.0190  397 THR A CG2 
3382 N N   . GLU A 398 ? 0.1736 0.2007 0.2566 0.0338  -0.0450 0.0117  398 GLU A N   
3383 C CA  . GLU A 398 ? 0.1789 0.1912 0.2457 0.0356  -0.0521 0.0122  398 GLU A CA  
3384 C C   . GLU A 398 ? 0.2161 0.2166 0.2674 0.0280  -0.0519 0.0106  398 GLU A C   
3385 O O   . GLU A 398 ? 0.2146 0.2113 0.2630 0.0240  -0.0445 0.0096  398 GLU A O   
3386 C CB  . GLU A 398 ? 0.1871 0.1872 0.2449 0.0435  -0.0496 0.0133  398 GLU A CB  
3387 C CG  . GLU A 398 ? 0.2949 0.2811 0.3367 0.0449  -0.0565 0.0168  398 GLU A CG  
3388 C CD  . GLU A 398 ? 0.4344 0.4299 0.4826 0.0479  -0.0674 0.0195  398 GLU A CD  
3389 O OE1 . GLU A 398 ? 0.5325 0.5323 0.5764 0.0424  -0.0731 0.0184  398 GLU A OE1 
3390 O OE2 . GLU A 398 ? 0.4580 0.4570 0.5161 0.0563  -0.0708 0.0220  398 GLU A OE2 
3391 N N   . VAL A 399 ? 0.2062 0.2022 0.2472 0.0268  -0.0601 0.0101  399 VAL A N   
3392 C CA  . VAL A 399 ? 0.1904 0.1763 0.2157 0.0216  -0.0602 0.0071  399 VAL A CA  
3393 C C   . VAL A 399 ? 0.2477 0.2208 0.2538 0.0245  -0.0572 0.0097  399 VAL A C   
3394 O O   . VAL A 399 ? 0.3022 0.2733 0.3042 0.0295  -0.0608 0.0142  399 VAL A O   
3395 C CB  . VAL A 399 ? 0.2557 0.2467 0.2801 0.0187  -0.0706 0.0034  399 VAL A CB  
3396 C CG1 . VAL A 399 ? 0.2707 0.2522 0.2779 0.0154  -0.0707 -0.0016 399 VAL A CG1 
3397 C CG2 . VAL A 399 ? 0.2441 0.2471 0.2901 0.0141  -0.0739 0.0012  399 VAL A CG2 
3398 N N   . ILE A 400 ? 0.2349 0.1995 0.2307 0.0211  -0.0510 0.0079  400 ILE A N   
3399 C CA  . ILE A 400 ? 0.2403 0.1946 0.2190 0.0219  -0.0479 0.0105  400 ILE A CA  
3400 C C   . ILE A 400 ? 0.2438 0.1966 0.2092 0.0184  -0.0490 0.0066  400 ILE A C   
3401 O O   . ILE A 400 ? 0.2658 0.2194 0.2355 0.0151  -0.0478 0.0012  400 ILE A O   
3402 C CB  . ILE A 400 ? 0.2750 0.2228 0.2544 0.0222  -0.0390 0.0114  400 ILE A CB  
3403 C CG1 . ILE A 400 ? 0.2993 0.2371 0.2636 0.0218  -0.0366 0.0148  400 ILE A CG1 
3404 C CG2 . ILE A 400 ? 0.3155 0.2657 0.3002 0.0182  -0.0334 0.0076  400 ILE A CG2 
3405 C CD1 . ILE A 400 ? 0.3633 0.2946 0.3294 0.0221  -0.0297 0.0147  400 ILE A CD1 
3406 N N   . GLU A 401 ? 0.2482 0.1994 0.1980 0.0194  -0.0515 0.0095  401 GLU A N   
3407 C CA  . GLU A 401 ? 0.2258 0.1793 0.1618 0.0176  -0.0527 0.0048  401 GLU A CA  
3408 C C   . GLU A 401 ? 0.2355 0.1842 0.1612 0.0158  -0.0447 0.0052  401 GLU A C   
3409 O O   . GLU A 401 ? 0.2726 0.2233 0.1923 0.0148  -0.0435 -0.0015 401 GLU A O   
3410 C CB  . GLU A 401 ? 0.2760 0.2358 0.1997 0.0197  -0.0602 0.0079  401 GLU A CB  
3411 C CG  . GLU A 401 ? 0.3795 0.3443 0.2846 0.0190  -0.0600 0.0041  401 GLU A CG  
3412 C CD  . GLU A 401 ? 0.4112 0.3792 0.3183 0.0182  -0.0626 -0.0090 401 GLU A CD  
3413 O OE1 . GLU A 401 ? 0.4044 0.3727 0.3262 0.0173  -0.0679 -0.0139 401 GLU A OE1 
3414 O OE2 . GLU A 401 ? 0.3879 0.3583 0.2831 0.0184  -0.0596 -0.0146 401 GLU A OE2 
3415 N N   . SER A 402 ? 0.2225 0.1650 0.1472 0.0157  -0.0398 0.0120  402 SER A N   
3416 C CA  . SER A 402 ? 0.2343 0.1746 0.1495 0.0132  -0.0332 0.0134  402 SER A CA  
3417 C C   . SER A 402 ? 0.2348 0.1667 0.1562 0.0124  -0.0283 0.0178  402 SER A C   
3418 O O   . SER A 402 ? 0.2894 0.2166 0.2167 0.0146  -0.0309 0.0222  402 SER A O   
3419 C CB  . SER A 402 ? 0.2874 0.2325 0.1865 0.0128  -0.0348 0.0190  402 SER A CB  
3420 O OG  . SER A 402 ? 0.3284 0.2749 0.2195 0.0099  -0.0282 0.0204  402 SER A OG  
3421 N N   . VAL A 403 ? 0.2230 0.1534 0.1435 0.0099  -0.0219 0.0157  403 VAL A N   
3422 C CA  . VAL A 403 ? 0.2612 0.1844 0.1855 0.0086  -0.0178 0.0185  403 VAL A CA  
3423 C C   . VAL A 403 ? 0.2869 0.2102 0.2017 0.0045  -0.0145 0.0227  403 VAL A C   
3424 O O   . VAL A 403 ? 0.2751 0.2064 0.1818 0.0033  -0.0130 0.0213  403 VAL A O   
3425 C CB  . VAL A 403 ? 0.2577 0.1811 0.1909 0.0087  -0.0136 0.0131  403 VAL A CB  
3426 C CG1 . VAL A 403 ? 0.2923 0.2181 0.2368 0.0118  -0.0161 0.0108  403 VAL A CG1 
3427 C CG2 . VAL A 403 ? 0.2464 0.1750 0.1765 0.0070  -0.0105 0.0090  403 VAL A CG2 
3428 N N   . LYS A 404 ? 0.2693 0.1842 0.1859 0.0024  -0.0138 0.0276  404 LYS A N   
3429 C CA  . LYS A 404 ? 0.2337 0.1488 0.1454 -0.0030 -0.0101 0.0316  404 LYS A CA  
3430 C C   . LYS A 404 ? 0.2499 0.1664 0.1666 -0.0043 -0.0054 0.0250  404 LYS A C   
3431 O O   . LYS A 404 ? 0.2462 0.1567 0.1704 -0.0026 -0.0053 0.0213  404 LYS A O   
3432 C CB  . LYS A 404 ? 0.2900 0.1937 0.2031 -0.0058 -0.0128 0.0400  404 LYS A CB  
3433 C CG  . LYS A 404 ? 0.3434 0.2471 0.2497 -0.0054 -0.0176 0.0497  404 LYS A CG  
3434 C CD  . LYS A 404 ? 0.5165 0.4091 0.4236 -0.0104 -0.0197 0.0610  404 LYS A CD  
3435 C CE  . LYS A 404 ? 0.6320 0.5300 0.5287 -0.0123 -0.0228 0.0737  404 LYS A CE  
3436 N NZ  . LYS A 404 ? 0.7218 0.6085 0.6204 -0.0187 -0.0249 0.0871  404 LYS A NZ  
3437 N N   . ALA A 405 ? 0.2121 0.1385 0.1244 -0.0064 -0.0015 0.0233  405 ALA A N   
3438 C CA  . ALA A 405 ? 0.2205 0.1504 0.1374 -0.0067 0.0021  0.0176  405 ALA A CA  
3439 C C   . ALA A 405 ? 0.2230 0.1466 0.1444 -0.0103 0.0030  0.0182  405 ALA A C   
3440 O O   . ALA A 405 ? 0.2384 0.1576 0.1588 -0.0150 0.0022  0.0238  405 ALA A O   
3441 C CB  . ALA A 405 ? 0.2191 0.1612 0.1314 -0.0076 0.0055  0.0163  405 ALA A CB  
3442 N N   . GLY A 406 ? 0.2026 0.1265 0.1290 -0.0085 0.0043  0.0126  406 GLY A N   
3443 C CA  . GLY A 406 ? 0.2234 0.1431 0.1533 -0.0115 0.0046  0.0107  406 GLY A CA  
3444 C C   . GLY A 406 ? 0.2169 0.1403 0.1502 -0.0083 0.0061  0.0046  406 GLY A C   
3445 O O   . GLY A 406 ? 0.1982 0.1283 0.1319 -0.0052 0.0075  0.0034  406 GLY A O   
3446 N N   . THR A 407 ? 0.2263 0.1453 0.1620 -0.0094 0.0054  0.0007  407 THR A N   
3447 C CA  . THR A 407 ? 0.1919 0.1165 0.1292 -0.0067 0.0068  -0.0053 407 THR A CA  
3448 C C   . THR A 407 ? 0.1817 0.0976 0.1218 -0.0040 0.0048  -0.0106 407 THR A C   
3449 O O   . THR A 407 ? 0.2170 0.1208 0.1592 -0.0046 0.0017  -0.0091 407 THR A O   
3450 C CB  . THR A 407 ? 0.1838 0.1161 0.1199 -0.0106 0.0076  -0.0075 407 THR A CB  
3451 O OG1 . THR A 407 ? 0.2251 0.1492 0.1627 -0.0151 0.0048  -0.0102 407 THR A OG1 
3452 C CG2 . THR A 407 ? 0.1941 0.1346 0.1288 -0.0132 0.0092  -0.0028 407 THR A CG2 
3453 N N   . TRP A 408 ? 0.1876 0.1103 0.1279 -0.0006 0.0064  -0.0169 408 TRP A N   
3454 C CA  . TRP A 408 ? 0.2026 0.1188 0.1456 0.0032  0.0046  -0.0247 408 TRP A CA  
3455 C C   . TRP A 408 ? 0.2249 0.1322 0.1681 -0.0012 0.0010  -0.0303 408 TRP A C   
3456 O O   . TRP A 408 ? 0.2532 0.1529 0.1990 0.0024  -0.0014 -0.0388 408 TRP A O   
3457 C CB  . TRP A 408 ? 0.2072 0.1368 0.1496 0.0090  0.0081  -0.0301 408 TRP A CB  
3458 C CG  . TRP A 408 ? 0.2222 0.1662 0.1594 0.0073  0.0104  -0.0316 408 TRP A CG  
3459 C CD1 . TRP A 408 ? 0.2130 0.1589 0.1470 0.0017  0.0092  -0.0306 408 TRP A CD1 
3460 C CD2 . TRP A 408 ? 0.2079 0.1680 0.1428 0.0114  0.0142  -0.0332 408 TRP A CD2 
3461 N NE1 . TRP A 408 ? 0.2268 0.1883 0.1564 0.0027  0.0112  -0.0318 408 TRP A NE1 
3462 C CE2 . TRP A 408 ? 0.1817 0.1521 0.1112 0.0083  0.0145  -0.0327 408 TRP A CE2 
3463 C CE3 . TRP A 408 ? 0.1953 0.1644 0.1330 0.0172  0.0175  -0.0341 408 TRP A CE3 
3464 C CZ2 . TRP A 408 ? 0.2187 0.2068 0.1438 0.0108  0.0177  -0.0321 408 TRP A CZ2 
3465 C CZ3 . TRP A 408 ? 0.2029 0.1911 0.1370 0.0192  0.0216  -0.0335 408 TRP A CZ3 
3466 C CH2 . TRP A 408 ? 0.2142 0.2111 0.1413 0.0159  0.0215  -0.0321 408 TRP A CH2 
3467 N N   . PHE A 409 ? 0.2284 0.1369 0.1700 -0.0086 0.0003  -0.0265 409 PHE A N   
3468 C CA  . PHE A 409 ? 0.2303 0.1275 0.1751 -0.0148 -0.0042 -0.0293 409 PHE A CA  
3469 C C   . PHE A 409 ? 0.2742 0.1565 0.2225 -0.0177 -0.0068 -0.0208 409 PHE A C   
3470 O O   . PHE A 409 ? 0.2826 0.1679 0.2298 -0.0233 -0.0058 -0.0114 409 PHE A O   
3471 C CB  . PHE A 409 ? 0.2625 0.1701 0.2062 -0.0222 -0.0041 -0.0282 409 PHE A CB  
3472 C CG  . PHE A 409 ? 0.2927 0.1895 0.2419 -0.0307 -0.0091 -0.0293 409 PHE A CG  
3473 C CD1 . PHE A 409 ? 0.3484 0.2372 0.3003 -0.0308 -0.0138 -0.0409 409 PHE A CD1 
3474 C CD2 . PHE A 409 ? 0.3352 0.2305 0.2874 -0.0388 -0.0093 -0.0189 409 PHE A CD2 
3475 C CE1 . PHE A 409 ? 0.4023 0.2790 0.3613 -0.0397 -0.0196 -0.0420 409 PHE A CE1 
3476 C CE2 . PHE A 409 ? 0.3331 0.2189 0.2923 -0.0482 -0.0140 -0.0182 409 PHE A CE2 
3477 C CZ  . PHE A 409 ? 0.4243 0.2994 0.3877 -0.0491 -0.0197 -0.0296 409 PHE A CZ  
3478 N N   . ASP A 410 ? 0.3178 0.1856 0.2704 -0.0129 -0.0102 -0.0240 410 ASP A N   
3479 C CA  . ASP A 410 ? 0.3306 0.1818 0.2873 -0.0154 -0.0143 -0.0155 410 ASP A CA  
3480 C C   . ASP A 410 ? 0.2891 0.1468 0.2415 -0.0164 -0.0118 -0.0031 410 ASP A C   
3481 O O   . ASP A 410 ? 0.3209 0.1710 0.2739 -0.0218 -0.0142 0.0071  410 ASP A O   
3482 C CB  . ASP A 410 ? 0.4325 0.2720 0.3941 -0.0252 -0.0189 -0.0137 410 ASP A CB  
3483 C CG  . ASP A 410 ? 0.5844 0.4159 0.5505 -0.0244 -0.0229 -0.0280 410 ASP A CG  
3484 O OD1 . ASP A 410 ? 0.6301 0.4615 0.5960 -0.0146 -0.0227 -0.0388 410 ASP A OD1 
3485 O OD2 . ASP A 410 ? 0.6128 0.4397 0.5829 -0.0336 -0.0263 -0.0290 410 ASP A OD2 
3486 N N   . GLY A 411 ? 0.2512 0.1232 0.1993 -0.0116 -0.0074 -0.0036 411 GLY A N   
3487 C CA  . GLY A 411 ? 0.2485 0.1267 0.1923 -0.0117 -0.0059 0.0054  411 GLY A CA  
3488 C C   . GLY A 411 ? 0.2273 0.1141 0.1665 -0.0190 -0.0036 0.0119  411 GLY A C   
3489 O O   . GLY A 411 ? 0.2792 0.1694 0.2141 -0.0198 -0.0033 0.0194  411 GLY A O   
3490 N N   . ASN A 412 ? 0.2456 0.1385 0.1857 -0.0240 -0.0021 0.0087  412 ASN A N   
3491 C CA  . ASN A 412 ? 0.2407 0.1442 0.1785 -0.0307 0.0003  0.0149  412 ASN A CA  
3492 C C   . ASN A 412 ? 0.2378 0.1552 0.1760 -0.0313 0.0032  0.0092  412 ASN A C   
3493 O O   . ASN A 412 ? 0.2353 0.1539 0.1741 -0.0270 0.0032  0.0016  412 ASN A O   
3494 C CB  . ASN A 412 ? 0.2528 0.1478 0.1944 -0.0397 -0.0025 0.0222  412 ASN A CB  
3495 C CG  . ASN A 412 ? 0.3148 0.2016 0.2635 -0.0445 -0.0059 0.0159  412 ASN A CG  
3496 O OD1 . ASN A 412 ? 0.2726 0.1702 0.2223 -0.0459 -0.0045 0.0095  412 ASN A OD1 
3497 N ND2 . ASN A 412 ? 0.3844 0.2521 0.3387 -0.0472 -0.0113 0.0177  412 ASN A ND2 
3498 N N   . PHE A 413 ? 0.2274 0.1575 0.1654 -0.0362 0.0057  0.0135  413 PHE A N   
3499 C CA  . PHE A 413 ? 0.2107 0.1561 0.1496 -0.0355 0.0081  0.0095  413 PHE A CA  
3500 C C   . PHE A 413 ? 0.2427 0.1931 0.1874 -0.0435 0.0066  0.0086  413 PHE A C   
3501 O O   . PHE A 413 ? 0.2391 0.2050 0.1857 -0.0438 0.0083  0.0070  413 PHE A O   
3502 C CB  . PHE A 413 ? 0.1965 0.1559 0.1323 -0.0330 0.0120  0.0130  413 PHE A CB  
3503 C CG  . PHE A 413 ? 0.2042 0.1605 0.1355 -0.0251 0.0126  0.0117  413 PHE A CG  
3504 C CD1 . PHE A 413 ? 0.2257 0.1846 0.1578 -0.0192 0.0130  0.0069  413 PHE A CD1 
3505 C CD2 . PHE A 413 ? 0.2543 0.2055 0.1811 -0.0242 0.0122  0.0160  413 PHE A CD2 
3506 C CE1 . PHE A 413 ? 0.1964 0.1521 0.1267 -0.0133 0.0128  0.0060  413 PHE A CE1 
3507 C CE2 . PHE A 413 ? 0.2479 0.1970 0.1718 -0.0176 0.0116  0.0140  413 PHE A CE2 
3508 C CZ  . PHE A 413 ? 0.2021 0.1529 0.1286 -0.0126 0.0119  0.0088  413 PHE A CZ  
3509 N N   . LEU A 414 ? 0.2250 0.1624 0.1740 -0.0499 0.0027  0.0093  414 LEU A N   
3510 C CA  . LEU A 414 ? 0.2370 0.1791 0.1934 -0.0598 0.0005  0.0097  414 LEU A CA  
3511 C C   . LEU A 414 ? 0.2365 0.1853 0.1950 -0.0590 -0.0018 -0.0004 414 LEU A C   
3512 O O   . LEU A 414 ? 0.2594 0.2170 0.2247 -0.0669 -0.0038 -0.0008 414 LEU A O   
3513 C CB  . LEU A 414 ? 0.2393 0.1624 0.2012 -0.0673 -0.0044 0.0134  414 LEU A CB  
3514 C CG  . LEU A 414 ? 0.2708 0.1908 0.2308 -0.0704 -0.0026 0.0266  414 LEU A CG  
3515 C CD1 . LEU A 414 ? 0.2986 0.1988 0.2660 -0.0788 -0.0084 0.0323  414 LEU A CD1 
3516 C CD2 . LEU A 414 ? 0.2873 0.2306 0.2469 -0.0748 0.0030  0.0346  414 LEU A CD2 
3517 N N   . LYS A 415 ? 0.2321 0.1791 0.1853 -0.0503 -0.0018 -0.0080 415 LYS A N   
3518 C CA  . LYS A 415 ? 0.2165 0.1739 0.1697 -0.0494 -0.0038 -0.0162 415 LYS A CA  
3519 C C   . LYS A 415 ? 0.2088 0.1875 0.1619 -0.0473 -0.0007 -0.0133 415 LYS A C   
3520 O O   . LYS A 415 ? 0.2227 0.2128 0.1763 -0.0472 -0.0029 -0.0183 415 LYS A O   
3521 C CB  . LYS A 415 ? 0.2257 0.1773 0.1730 -0.0411 -0.0044 -0.0245 415 LYS A CB  
3522 C CG  . LYS A 415 ? 0.3481 0.2827 0.2974 -0.0425 -0.0094 -0.0330 415 LYS A CG  
3523 C CD  . LYS A 415 ? 0.4890 0.4270 0.4424 -0.0495 -0.0150 -0.0409 415 LYS A CD  
3524 C CE  . LYS A 415 ? 0.5943 0.5143 0.5498 -0.0491 -0.0206 -0.0523 415 LYS A CE  
3525 N NZ  . LYS A 415 ? 0.6466 0.5675 0.6073 -0.0569 -0.0276 -0.0615 415 LYS A NZ  
3526 N N   . TRP A 416 ? 0.2035 0.1880 0.1559 -0.0451 0.0037  -0.0060 416 TRP A N   
3527 C CA  . TRP A 416 ? 0.1751 0.1778 0.1284 -0.0407 0.0064  -0.0041 416 TRP A CA  
3528 C C   . TRP A 416 ? 0.2083 0.2236 0.1664 -0.0445 0.0095  0.0020  416 TRP A C   
3529 O O   . TRP A 416 ? 0.2006 0.2324 0.1616 -0.0405 0.0113  0.0025  416 TRP A O   
3530 C CB  . TRP A 416 ? 0.1968 0.1964 0.1443 -0.0309 0.0089  -0.0036 416 TRP A CB  
3531 C CG  . TRP A 416 ? 0.1840 0.1754 0.1270 -0.0270 0.0072  -0.0082 416 TRP A CG  
3532 C CD1 . TRP A 416 ? 0.2023 0.2022 0.1434 -0.0235 0.0059  -0.0111 416 TRP A CD1 
3533 C CD2 . TRP A 416 ? 0.1677 0.1435 0.1077 -0.0261 0.0067  -0.0104 416 TRP A CD2 
3534 N NE1 . TRP A 416 ? 0.1832 0.1753 0.1196 -0.0206 0.0055  -0.0150 416 TRP A NE1 
3535 C CE2 . TRP A 416 ? 0.1692 0.1463 0.1057 -0.0217 0.0059  -0.0153 416 TRP A CE2 
3536 C CE3 . TRP A 416 ? 0.2052 0.1672 0.1453 -0.0280 0.0066  -0.0080 416 TRP A CE3 
3537 C CZ2 . TRP A 416 ? 0.2373 0.2037 0.1715 -0.0187 0.0057  -0.0192 416 TRP A CZ2 
3538 C CZ3 . TRP A 416 ? 0.2302 0.1797 0.1686 -0.0248 0.0054  -0.0115 416 TRP A CZ3 
3539 C CH2 . TRP A 416 ? 0.2129 0.1652 0.1489 -0.0199 0.0053  -0.0176 416 TRP A CH2 
3540 N N   . ILE A 417 ? 0.1891 0.1985 0.1488 -0.0514 0.0102  0.0070  417 ILE A N   
3541 C CA  . ILE A 417 ? 0.1879 0.2124 0.1511 -0.0550 0.0142  0.0138  417 ILE A CA  
3542 C C   . ILE A 417 ? 0.2387 0.2554 0.2055 -0.0663 0.0129  0.0202  417 ILE A C   
3543 O O   . ILE A 417 ? 0.2516 0.2476 0.2167 -0.0685 0.0091  0.0193  417 ILE A O   
3544 C CB  . ILE A 417 ? 0.2133 0.2395 0.1693 -0.0463 0.0187  0.0155  417 ILE A CB  
3545 C CG1 . ILE A 417 ? 0.2075 0.2564 0.1667 -0.0465 0.0236  0.0192  417 ILE A CG1 
3546 C CG2 . ILE A 417 ? 0.2184 0.2261 0.1674 -0.0467 0.0181  0.0190  417 ILE A CG2 
3547 C CD1 . ILE A 417 ? 0.2376 0.2912 0.1909 -0.0355 0.0269  0.0166  417 ILE A CD1 
3548 N N   . GLY A 418 ? 0.2256 0.2597 0.1989 -0.0736 0.0158  0.0270  418 GLY A N   
3549 C CA  . GLY A 418 ? 0.2534 0.2817 0.2303 -0.0849 0.0152  0.0367  418 GLY A CA  
3550 C C   . GLY A 418 ? 0.3095 0.3412 0.2996 -0.0982 0.0112  0.0386  418 GLY A C   
3551 O O   . GLY A 418 ? 0.3848 0.4129 0.3801 -0.1092 0.0107  0.0487  418 GLY A O   
3552 N N   . ASN A 419 ? 0.2600 0.2984 0.2562 -0.0984 0.0076  0.0299  419 ASN A N   
3553 C CA  . ASN A 419 ? 0.3014 0.3509 0.3121 -0.1116 0.0042  0.0320  419 ASN A CA  
3554 C C   . ASN A 419 ? 0.2903 0.3722 0.3075 -0.1093 0.0077  0.0309  419 ASN A C   
3555 O O   . ASN A 419 ? 0.2346 0.3269 0.2451 -0.0968 0.0119  0.0275  419 ASN A O   
3556 C CB  . ASN A 419 ? 0.3325 0.3630 0.3474 -0.1165 -0.0051 0.0226  419 ASN A CB  
3557 C CG  . ASN A 419 ? 0.3485 0.3839 0.3589 -0.1071 -0.0079 0.0096  419 ASN A CG  
3558 O OD1 . ASN A 419 ? 0.3296 0.3853 0.3381 -0.0995 -0.0042 0.0086  419 ASN A OD1 
3559 N ND2 . ASN A 419 ? 0.3458 0.3626 0.3544 -0.1075 -0.0149 -0.0003 419 ASN A ND2 
3560 N N   . LYS A 420 ? 0.3391 0.4366 0.3713 -0.1217 0.0054  0.0340  420 LYS A N   
3561 C CA  . LYS A 420 ? 0.2648 0.3971 0.3067 -0.1210 0.0091  0.0352  420 LYS A CA  
3562 C C   . LYS A 420 ? 0.2438 0.3833 0.2819 -0.1083 0.0069  0.0243  420 LYS A C   
3563 O O   . LYS A 420 ? 0.2191 0.3780 0.2563 -0.0978 0.0121  0.0241  420 LYS A O   
3564 C CB  . LYS A 420 ? 0.3361 0.4830 0.3969 -0.1382 0.0052  0.0396  420 LYS A CB  
3565 C CG  . LYS A 420 ? 0.5491 0.6911 0.6171 -0.1537 0.0068  0.0536  420 LYS A CG  
3566 C CD  . LYS A 420 ? 0.6473 0.7502 0.7070 -0.1566 0.0023  0.0551  420 LYS A CD  
3567 C CE  . LYS A 420 ? 0.6762 0.7543 0.7365 -0.1573 -0.0084 0.0416  420 LYS A CE  
3568 N NZ  . LYS A 420 ? 0.7042 0.7455 0.7575 -0.1577 -0.0125 0.0418  420 LYS A NZ  
3569 N N   . GLU A 421 ? 0.2610 0.3851 0.2967 -0.1084 -0.0010 0.0153  421 GLU A N   
3570 C CA  . GLU A 421 ? 0.2600 0.3932 0.2926 -0.0980 -0.0039 0.0070  421 GLU A CA  
3571 C C   . GLU A 421 ? 0.2292 0.3523 0.2473 -0.0825 0.0004  0.0055  421 GLU A C   
3572 O O   . GLU A 421 ? 0.2296 0.3679 0.2476 -0.0722 0.0023  0.0046  421 GLU A O   
3573 C CB  . GLU A 421 ? 0.2543 0.3759 0.2865 -0.1026 -0.0134 -0.0026 421 GLU A CB  
3574 C CG  . GLU A 421 ? 0.3100 0.4444 0.3586 -0.1175 -0.0200 -0.0036 421 GLU A CG  
3575 C CD  . GLU A 421 ? 0.4998 0.6217 0.5569 -0.1322 -0.0200 0.0033  421 GLU A CD  
3576 O OE1 . GLU A 421 ? 0.5728 0.7137 0.6465 -0.1445 -0.0208 0.0090  421 GLU A OE1 
3577 O OE2 . GLU A 421 ? 0.5092 0.6032 0.5575 -0.1316 -0.0194 0.0042  421 GLU A OE2 
3578 N N   . LYS A 422 ? 0.2142 0.3111 0.2214 -0.0807 0.0012  0.0053  422 LYS A N   
3579 C CA  . LYS A 422 ? 0.1995 0.2869 0.1947 -0.0676 0.0049  0.0044  422 LYS A CA  
3580 C C   . LYS A 422 ? 0.2130 0.3147 0.2090 -0.0619 0.0120  0.0098  422 LYS A C   
3581 O O   . LYS A 422 ? 0.1821 0.2879 0.1744 -0.0504 0.0139  0.0078  422 LYS A O   
3582 C CB  . LYS A 422 ? 0.2067 0.2662 0.1924 -0.0676 0.0043  0.0036  422 LYS A CB  
3583 C CG  . LYS A 422 ? 0.2335 0.2784 0.2161 -0.0691 -0.0022 -0.0046 422 LYS A CG  
3584 C CD  . LYS A 422 ? 0.2233 0.2422 0.1990 -0.0684 -0.0027 -0.0057 422 LYS A CD  
3585 C CE  . LYS A 422 ? 0.2381 0.2442 0.2135 -0.0715 -0.0095 -0.0154 422 LYS A CE  
3586 N NZ  . LYS A 422 ? 0.2133 0.2263 0.1818 -0.0633 -0.0112 -0.0233 422 LYS A NZ  
3587 N N   . ASN A 423 ? 0.1960 0.3059 0.1971 -0.0699 0.0157  0.0166  423 ASN A N   
3588 C CA  . ASN A 423 ? 0.2329 0.3605 0.2341 -0.0640 0.0229  0.0203  423 ASN A CA  
3589 C C   . ASN A 423 ? 0.1985 0.3532 0.2093 -0.0578 0.0238  0.0176  423 ASN A C   
3590 O O   . ASN A 423 ? 0.1959 0.3604 0.2049 -0.0466 0.0281  0.0159  423 ASN A O   
3591 C CB  . ASN A 423 ? 0.2227 0.3580 0.2273 -0.0749 0.0270  0.0296  423 ASN A CB  
3592 C CG  . ASN A 423 ? 0.2169 0.3274 0.2104 -0.0769 0.0272  0.0337  423 ASN A CG  
3593 O OD1 . ASN A 423 ? 0.2169 0.3062 0.2008 -0.0695 0.0248  0.0287  423 ASN A OD1 
3594 N ND2 . ASN A 423 ? 0.2197 0.3342 0.2154 -0.0872 0.0298  0.0438  423 ASN A ND2 
3595 N N   . GLU A 424 ? 0.2135 0.3807 0.2354 -0.0643 0.0191  0.0164  424 GLU A N   
3596 C CA  . GLU A 424 ? 0.1884 0.3826 0.2209 -0.0577 0.0190  0.0142  424 GLU A CA  
3597 C C   . GLU A 424 ? 0.1801 0.3662 0.2057 -0.0428 0.0169  0.0090  424 GLU A C   
3598 O O   . GLU A 424 ? 0.1582 0.3604 0.1889 -0.0320 0.0191  0.0078  424 GLU A O   
3599 C CB  . GLU A 424 ? 0.1918 0.4000 0.2371 -0.0683 0.0128  0.0136  424 GLU A CB  
3600 C CG  . GLU A 424 ? 0.2809 0.5192 0.3389 -0.0618 0.0112  0.0117  424 GLU A CG  
3601 C CD  . GLU A 424 ? 0.4305 0.6971 0.4982 -0.0573 0.0192  0.0152  424 GLU A CD  
3602 O OE1 . GLU A 424 ? 0.4648 0.7510 0.5401 -0.0457 0.0192  0.0126  424 GLU A OE1 
3603 O OE2 . GLU A 424 ? 0.4794 0.7499 0.5476 -0.0649 0.0255  0.0207  424 GLU A OE2 
3604 N N   . TYR A 425 ? 0.1723 0.3341 0.1874 -0.0418 0.0124  0.0062  425 TYR A N   
3605 C CA  . TYR A 425 ? 0.1467 0.2996 0.1553 -0.0291 0.0107  0.0037  425 TYR A CA  
3606 C C   . TYR A 425 ? 0.1606 0.3073 0.1644 -0.0194 0.0162  0.0039  425 TYR A C   
3607 O O   . TYR A 425 ? 0.1497 0.3019 0.1564 -0.0079 0.0160  0.0026  425 TYR A O   
3608 C CB  . TYR A 425 ? 0.1692 0.2995 0.1670 -0.0309 0.0064  0.0014  425 TYR A CB  
3609 C CG  . TYR A 425 ? 0.1642 0.3023 0.1637 -0.0315 -0.0005 -0.0012 425 TYR A CG  
3610 C CD1 . TYR A 425 ? 0.1691 0.3299 0.1801 -0.0370 -0.0039 -0.0017 425 TYR A CD1 
3611 C CD2 . TYR A 425 ? 0.2012 0.3265 0.1906 -0.0269 -0.0035 -0.0028 425 TYR A CD2 
3612 C CE1 . TYR A 425 ? 0.1842 0.3535 0.1955 -0.0374 -0.0111 -0.0045 425 TYR A CE1 
3613 C CE2 . TYR A 425 ? 0.2341 0.3687 0.2226 -0.0271 -0.0098 -0.0050 425 TYR A CE2 
3614 C CZ  . TYR A 425 ? 0.1717 0.3278 0.1705 -0.0322 -0.0139 -0.0062 425 TYR A CZ  
3615 O OH  . TYR A 425 ? 0.1761 0.3426 0.1728 -0.0321 -0.0210 -0.0089 425 TYR A OH  
3616 N N   . TRP A 426 ? 0.1612 0.2960 0.1580 -0.0236 0.0202  0.0054  426 TRP A N   
3617 C CA  . TRP A 426 ? 0.1582 0.2889 0.1498 -0.0148 0.0247  0.0043  426 TRP A CA  
3618 C C   . TRP A 426 ? 0.1591 0.3161 0.1598 -0.0089 0.0290  0.0032  426 TRP A C   
3619 O O   . TRP A 426 ? 0.1656 0.3234 0.1664 0.0032  0.0300  -0.0010 426 TRP A O   
3620 C CB  . TRP A 426 ? 0.1655 0.2817 0.1477 -0.0208 0.0275  0.0069  426 TRP A CB  
3621 C CG  . TRP A 426 ? 0.1712 0.2609 0.1446 -0.0218 0.0238  0.0062  426 TRP A CG  
3622 C CD1 . TRP A 426 ? 0.1753 0.2530 0.1468 -0.0310 0.0208  0.0076  426 TRP A CD1 
3623 C CD2 . TRP A 426 ? 0.1878 0.2613 0.1547 -0.0132 0.0224  0.0035  426 TRP A CD2 
3624 N NE1 . TRP A 426 ? 0.1970 0.2542 0.1609 -0.0276 0.0185  0.0056  426 TRP A NE1 
3625 C CE2 . TRP A 426 ? 0.2086 0.2635 0.1698 -0.0175 0.0196  0.0038  426 TRP A CE2 
3626 C CE3 . TRP A 426 ? 0.1932 0.2661 0.1600 -0.0024 0.0230  0.0005  426 TRP A CE3 
3627 C CZ2 . TRP A 426 ? 0.1937 0.2325 0.1494 -0.0120 0.0181  0.0024  426 TRP A CZ2 
3628 C CZ3 . TRP A 426 ? 0.1924 0.2463 0.1540 0.0020  0.0206  -0.0006 426 TRP A CZ3 
3629 C CH2 . TRP A 426 ? 0.1988 0.2376 0.1551 -0.0031 0.0186  0.0010  426 TRP A CH2 
3630 N N   . LYS A 427 ? 0.1750 0.3544 0.1848 -0.0172 0.0313  0.0064  427 LYS A N   
3631 C CA  . LYS A 427 ? 0.1905 0.3999 0.2108 -0.0112 0.0358  0.0051  427 LYS A CA  
3632 C C   . LYS A 427 ? 0.1455 0.3628 0.1745 0.0010  0.0317  0.0007  427 LYS A C   
3633 O O   . LYS A 427 ? 0.1830 0.4110 0.2162 0.0137  0.0343  -0.0039 427 LYS A O   
3634 C CB  . LYS A 427 ? 0.1584 0.3924 0.1896 -0.0240 0.0383  0.0107  427 LYS A CB  
3635 C CG  . LYS A 427 ? 0.2977 0.5328 0.3233 -0.0341 0.0440  0.0170  427 LYS A CG  
3636 C CD  . LYS A 427 ? 0.4190 0.6722 0.4569 -0.0502 0.0443  0.0246  427 LYS A CD  
3637 C CE  . LYS A 427 ? 0.5358 0.8269 0.5911 -0.0475 0.0468  0.0238  427 LYS A CE  
3638 N NZ  . LYS A 427 ? 0.6114 0.9275 0.6669 -0.0383 0.0560  0.0227  427 LYS A NZ  
3639 N N   . ILE A 428 ? 0.1430 0.3560 0.1752 -0.0023 0.0250  0.0020  428 ILE A N   
3640 C CA  . ILE A 428 ? 0.1645 0.3839 0.2041 0.0091  0.0200  0.0000  428 ILE A CA  
3641 C C   . ILE A 428 ? 0.1887 0.3866 0.2211 0.0217  0.0190  -0.0028 428 ILE A C   
3642 O O   . ILE A 428 ? 0.1486 0.3539 0.1887 0.0348  0.0183  -0.0057 428 ILE A O   
3643 C CB  . ILE A 428 ? 0.1410 0.3588 0.1817 0.0024  0.0125  0.0023  428 ILE A CB  
3644 C CG1 . ILE A 428 ? 0.1455 0.3884 0.1979 -0.0091 0.0121  0.0039  428 ILE A CG1 
3645 C CG2 . ILE A 428 ? 0.1754 0.3941 0.2198 0.0146  0.0066  0.0025  428 ILE A CG2 
3646 C CD1 . ILE A 428 ? 0.1601 0.3987 0.2110 -0.0189 0.0044  0.0042  428 ILE A CD1 
3647 N N   . LEU A 429 ? 0.1604 0.3314 0.1795 0.0181  0.0186  -0.0021 429 LEU A N   
3648 C CA  . LEU A 429 ? 0.1719 0.3217 0.1854 0.0280  0.0171  -0.0041 429 LEU A CA  
3649 C C   . LEU A 429 ? 0.1776 0.3312 0.1922 0.0370  0.0217  -0.0100 429 LEU A C   
3650 O O   . LEU A 429 ? 0.1784 0.3263 0.1974 0.0492  0.0194  -0.0136 429 LEU A O   
3651 C CB  . LEU A 429 ? 0.1778 0.3021 0.1782 0.0212  0.0162  -0.0022 429 LEU A CB  
3652 C CG  . LEU A 429 ? 0.2087 0.3109 0.2044 0.0288  0.0141  -0.0030 429 LEU A CG  
3653 C CD1 . LEU A 429 ? 0.2016 0.3005 0.2010 0.0332  0.0082  0.0013  429 LEU A CD1 
3654 C CD2 . LEU A 429 ? 0.2128 0.2954 0.1970 0.0219  0.0153  -0.0024 429 LEU A CD2 
3655 N N   . ILE A 430 ? 0.1492 0.3128 0.1602 0.0311  0.0279  -0.0109 430 ILE A N   
3656 C CA  . ILE A 430 ? 0.2031 0.3739 0.2127 0.0394  0.0328  -0.0175 430 ILE A CA  
3657 C C   . ILE A 430 ? 0.1838 0.3775 0.2073 0.0519  0.0334  -0.0227 430 ILE A C   
3658 O O   . ILE A 430 ? 0.2098 0.3991 0.2351 0.0651  0.0328  -0.0306 430 ILE A O   
3659 C CB  . ILE A 430 ? 0.1668 0.3486 0.1695 0.0295  0.0394  -0.0149 430 ILE A CB  
3660 C CG1 . ILE A 430 ? 0.1971 0.3526 0.1859 0.0214  0.0381  -0.0115 430 ILE A CG1 
3661 C CG2 . ILE A 430 ? 0.1954 0.3968 0.1981 0.0384  0.0456  -0.0218 430 ILE A CG2 
3662 C CD1 . ILE A 430 ? 0.1982 0.3603 0.1825 0.0075  0.0420  -0.0043 430 ILE A CD1 
3663 N N   . GLU A 431 ? 0.1735 0.3925 0.2085 0.0482  0.0340  -0.0192 431 GLU A N   
3664 C CA  . GLU A 431 ? 0.2011 0.4448 0.2514 0.0607  0.0345  -0.0239 431 GLU A CA  
3665 C C   . GLU A 431 ? 0.2049 0.4330 0.2615 0.0731  0.0265  -0.0254 431 GLU A C   
3666 O O   . GLU A 431 ? 0.2086 0.4414 0.2736 0.0883  0.0259  -0.0328 431 GLU A O   
3667 C CB  . GLU A 431 ? 0.2622 0.5372 0.3250 0.0527  0.0358  -0.0188 431 GLU A CB  
3668 C CG  . GLU A 431 ? 0.4458 0.7447 0.5081 0.0432  0.0447  -0.0169 431 GLU A CG  
3669 C CD  . GLU A 431 ? 0.4746 0.7861 0.5343 0.0543  0.0520  -0.0251 431 GLU A CD  
3670 O OE1 . GLU A 431 ? 0.5086 0.8101 0.5537 0.0494  0.0563  -0.0249 431 GLU A OE1 
3671 O OE2 . GLU A 431 ? 0.3956 0.7209 0.4655 0.0673  0.0515  -0.0315 431 GLU A OE2 
3672 N N   . ALA A 432 ? 0.1848 0.3942 0.2374 0.0670  0.0201  -0.0185 432 ALA A N   
3673 C CA  . ALA A 432 ? 0.2019 0.3964 0.2597 0.0772  0.0123  -0.0168 432 ALA A CA  
3674 C C   . ALA A 432 ? 0.2008 0.3696 0.2539 0.0863  0.0111  -0.0222 432 ALA A C   
3675 O O   . ALA A 432 ? 0.2336 0.3966 0.2965 0.0997  0.0064  -0.0248 432 ALA A O   
3676 C CB  . ALA A 432 ? 0.1684 0.3504 0.2198 0.0675  0.0068  -0.0078 432 ALA A CB  
3677 N N   . LYS A 433 ? 0.1681 0.3210 0.2075 0.0791  0.0146  -0.0240 433 LYS A N   
3678 C CA  . LYS A 433 ? 0.2101 0.3388 0.2452 0.0860  0.0128  -0.0297 433 LYS A CA  
3679 C C   . LYS A 433 ? 0.2145 0.3533 0.2580 0.1008  0.0143  -0.0416 433 LYS A C   
3680 O O   . LYS A 433 ? 0.2434 0.3644 0.2924 0.1117  0.0090  -0.0466 433 LYS A O   
3681 C CB  . LYS A 433 ? 0.2005 0.3162 0.2200 0.0754  0.0164  -0.0298 433 LYS A CB  
3682 C CG  . LYS A 433 ? 0.2455 0.3387 0.2600 0.0809  0.0145  -0.0368 433 LYS A CG  
3683 C CD  . LYS A 433 ? 0.2343 0.3025 0.2533 0.0837  0.0068  -0.0322 433 LYS A CD  
3684 C CE  . LYS A 433 ? 0.2739 0.3206 0.2915 0.0892  0.0037  -0.0402 433 LYS A CE  
3685 N NZ  . LYS A 433 ? 0.2522 0.2767 0.2790 0.0935  -0.0044 -0.0354 433 LYS A NZ  
3686 N N   . LYS A 434 ? 0.2067 0.3750 0.2523 0.1017  0.0213  -0.0464 434 LYS A N   
3687 C CA  . LYS A 434 ? 0.2326 0.4154 0.2862 0.1171  0.0236  -0.0591 434 LYS A CA  
3688 C C   . LYS A 434 ? 0.2699 0.4525 0.3414 0.1319  0.0168  -0.0609 434 LYS A C   
3689 O O   . LYS A 434 ? 0.3295 0.5074 0.4073 0.1457  0.0149  -0.0720 434 LYS A O   
3690 C CB  . LYS A 434 ? 0.2458 0.4663 0.3004 0.1144  0.0331  -0.0613 434 LYS A CB  
3691 C CG  . LYS A 434 ? 0.2994 0.5222 0.3373 0.1008  0.0398  -0.0586 434 LYS A CG  
3692 C CD  . LYS A 434 ? 0.3441 0.6013 0.3839 0.0962  0.0478  -0.0576 434 LYS A CD  
3693 C CE  . LYS A 434 ? 0.4345 0.6944 0.4597 0.0806  0.0535  -0.0505 434 LYS A CE  
3694 N NZ  . LYS A 434 ? 0.4357 0.7253 0.4650 0.0725  0.0592  -0.0449 434 LYS A NZ  
3695 N N   . LYS A 435 ? 0.2487 0.4337 0.3273 0.1278  0.0122  -0.0496 435 LYS A N   
3696 C CA  . LYS A 435 ? 0.2815 0.4697 0.3775 0.1411  0.0051  -0.0483 435 LYS A CA  
3697 C C   . LYS A 435 ? 0.2509 0.4079 0.3470 0.1405  -0.0044 -0.0386 435 LYS A C   
3698 O O   . LYS A 435 ? 0.2629 0.4211 0.3726 0.1498  -0.0115 -0.0337 435 LYS A O   
3699 C CB  . LYS A 435 ? 0.3159 0.5383 0.4222 0.1383  0.0066  -0.0424 435 LYS A CB  
3700 C CG  . LYS A 435 ? 0.4009 0.6572 0.5114 0.1389  0.0155  -0.0500 435 LYS A CG  
3701 C CD  . LYS A 435 ? 0.5042 0.7814 0.6079 0.1216  0.0221  -0.0434 435 LYS A CD  
3702 C CE  . LYS A 435 ? 0.4980 0.7883 0.5927 0.1166  0.0320  -0.0496 435 LYS A CE  
3703 N NZ  . LYS A 435 ? 0.5259 0.8245 0.6107 0.0985  0.0377  -0.0422 435 LYS A NZ  
3704 N N   . ALA A 436 ? 0.2632 0.3989 0.2778 0.1176  0.0245  -0.0819 436 ALA A N   
3705 C CA  . ALA A 436 ? 0.2577 0.3623 0.2793 0.1117  0.0157  -0.0730 436 ALA A CA  
3706 C C   . ALA A 436 ? 0.2942 0.3658 0.3178 0.1245  0.0084  -0.0835 436 ALA A C   
3707 O O   . ALA A 436 ? 0.3187 0.3798 0.3331 0.1320  0.0071  -0.1001 436 ALA A O   
3708 C CB  . ALA A 436 ? 0.2544 0.3456 0.2680 0.0935  0.0125  -0.0662 436 ALA A CB  
3709 N N   . LYS A 437 ? 0.3272 0.3806 0.3615 0.1268  0.0031  -0.0738 437 LYS A N   
3710 C CA  . LYS A 437 ? 0.3412 0.3577 0.3786 0.1379  -0.0045 -0.0800 437 LYS A CA  
3711 C C   . LYS A 437 ? 0.3748 0.3579 0.4146 0.1248  -0.0112 -0.0669 437 LYS A C   
3712 O O   . LYS A 437 ? 0.4617 0.4091 0.5043 0.1306  -0.0179 -0.0694 437 LYS A O   
3713 C CB  . LYS A 437 ? 0.3334 0.3577 0.3815 0.1592  -0.0047 -0.0807 437 LYS A CB  
3714 C CG  . LYS A 437 ? 0.4218 0.4841 0.4711 0.1738  0.0035  -0.0944 437 LYS A CG  
3715 C CD  . LYS A 437 ? 0.5909 0.6395 0.6289 0.1834  0.0037  -0.1169 437 LYS A CD  
3716 C CE  . LYS A 437 ? 0.6701 0.7472 0.7094 0.1953  0.0109  -0.1258 437 LYS A CE  
3717 N NZ  . LYS A 437 ? 0.6878 0.8106 0.7221 0.1859  0.0221  -0.1233 437 LYS A NZ  
3718 N N   . ASN A 438 ? 0.3189 0.3119 0.3581 0.1074  -0.0092 -0.0532 438 ASN A N   
3719 C CA  . ASN A 438 ? 0.3158 0.2829 0.3578 0.0950  -0.0133 -0.0404 438 ASN A CA  
3720 C C   . ASN A 438 ? 0.3255 0.3066 0.3648 0.0767  -0.0101 -0.0337 438 ASN A C   
3721 O O   . ASN A 438 ? 0.3126 0.3197 0.3474 0.0739  -0.0057 -0.0369 438 ASN A O   
3722 C CB  . ASN A 438 ? 0.3049 0.2675 0.3518 0.1010  -0.0149 -0.0250 438 ASN A CB  
3723 C CG  . ASN A 438 ? 0.2521 0.2511 0.2996 0.1011  -0.0104 -0.0171 438 ASN A CG  
3724 O OD1 . ASN A 438 ? 0.2667 0.2798 0.3115 0.0870  -0.0069 -0.0107 438 ASN A OD1 
3725 N ND2 . ASN A 438 ? 0.2840 0.2983 0.3369 0.1172  -0.0111 -0.0180 438 ASN A ND2 
3726 N N   . ASP A 439 ? 0.3071 0.2709 0.3500 0.0645  -0.0120 -0.0231 439 ASP A N   
3727 C CA  . ASP A 439 ? 0.3165 0.2907 0.3595 0.0489  -0.0096 -0.0182 439 ASP A CA  
3728 C C   . ASP A 439 ? 0.2436 0.2426 0.2843 0.0458  -0.0043 -0.0079 439 ASP A C   
3729 O O   . ASP A 439 ? 0.2364 0.2441 0.2773 0.0350  -0.0021 -0.0044 439 ASP A O   
3730 C CB  . ASP A 439 ? 0.3347 0.2862 0.3849 0.0370  -0.0120 -0.0108 439 ASP A CB  
3731 C CG  . ASP A 439 ? 0.3986 0.3302 0.4527 0.0328  -0.0183 -0.0236 439 ASP A CG  
3732 O OD1 . ASP A 439 ? 0.4149 0.3520 0.4630 0.0395  -0.0207 -0.0390 439 ASP A OD1 
3733 O OD2 . ASP A 439 ? 0.4405 0.3523 0.5036 0.0218  -0.0208 -0.0185 439 ASP A OD2 
3734 N N   . TYR A 440 ? 0.2323 0.2439 0.2719 0.0551  -0.0029 -0.0042 440 TYR A N   
3735 C CA  . TYR A 440 ? 0.1878 0.2235 0.2253 0.0504  0.0008  0.0021  440 TYR A CA  
3736 C C   . TYR A 440 ? 0.1678 0.2215 0.2024 0.0460  0.0039  -0.0049 440 TYR A C   
3737 O O   . TYR A 440 ? 0.1858 0.2521 0.2186 0.0383  0.0063  -0.0004 440 TYR A O   
3738 C CB  . TYR A 440 ? 0.2095 0.2584 0.2486 0.0604  -0.0001 0.0067  440 TYR A CB  
3739 C CG  . TYR A 440 ? 0.2266 0.2657 0.2633 0.0594  -0.0022 0.0199  440 TYR A CG  
3740 C CD1 . TYR A 440 ? 0.3075 0.3542 0.3394 0.0489  0.0003  0.0270  440 TYR A CD1 
3741 C CD2 . TYR A 440 ? 0.3324 0.3530 0.3701 0.0696  -0.0067 0.0254  440 TYR A CD2 
3742 C CE1 . TYR A 440 ? 0.3026 0.3427 0.3288 0.0480  -0.0005 0.0391  440 TYR A CE1 
3743 C CE2 . TYR A 440 ? 0.3178 0.3293 0.3498 0.0682  -0.0084 0.0401  440 TYR A CE2 
3744 C CZ  . TYR A 440 ? 0.3023 0.3254 0.3277 0.0570  -0.0047 0.0468  440 TYR A CZ  
3745 O OH  . TYR A 440 ? 0.4187 0.4357 0.4350 0.0557  -0.0053 0.0613  440 TYR A OH  
3746 N N   . ILE A 441 ? 0.1815 0.2346 0.2136 0.0507  0.0035  -0.0158 441 ILE A N   
3747 C CA  . ILE A 441 ? 0.1844 0.2525 0.2103 0.0457  0.0063  -0.0198 441 ILE A CA  
3748 C C   . ILE A 441 ? 0.1834 0.2436 0.2082 0.0345  0.0045  -0.0167 441 ILE A C   
3749 O O   . ILE A 441 ? 0.1877 0.2588 0.2085 0.0287  0.0063  -0.0140 441 ILE A O   
3750 C CB  . ILE A 441 ? 0.1876 0.2588 0.2074 0.0541  0.0066  -0.0326 441 ILE A CB  
3751 C CG1 . ILE A 441 ? 0.2030 0.2955 0.2139 0.0502  0.0113  -0.0331 441 ILE A CG1 
3752 C CG2 . ILE A 441 ? 0.1943 0.2422 0.2121 0.0538  0.0005  -0.0414 441 ILE A CG2 
3753 C CD1 . ILE A 441 ? 0.2030 0.3210 0.2180 0.0509  0.0177  -0.0278 441 ILE A CD1 
3754 N N   . LEU A 442 ? 0.1651 0.2069 0.1952 0.0312  0.0008  -0.0162 442 LEU A N   
3755 C CA  . LEU A 442 ? 0.1626 0.2024 0.1961 0.0214  -0.0005 -0.0130 442 LEU A CA  
3756 C C   . LEU A 442 ? 0.1685 0.2170 0.2035 0.0167  0.0036  -0.0033 442 LEU A C   
3757 O O   . LEU A 442 ? 0.1467 0.2015 0.1816 0.0119  0.0040  -0.0020 442 LEU A O   
3758 C CB  . LEU A 442 ? 0.1738 0.1954 0.2161 0.0171  -0.0045 -0.0141 442 LEU A CB  
3759 C CG  . LEU A 442 ? 0.2046 0.2118 0.2462 0.0206  -0.0104 -0.0263 442 LEU A CG  
3760 C CD1 . LEU A 442 ? 0.2033 0.1912 0.2568 0.0123  -0.0144 -0.0251 442 LEU A CD1 
3761 C CD2 . LEU A 442 ? 0.1887 0.2064 0.2222 0.0206  -0.0139 -0.0361 442 LEU A CD2 
3762 N N   . VAL A 443 ? 0.1423 0.1907 0.1777 0.0193  0.0057  0.0030  443 VAL A N   
3763 C CA  . VAL A 443 ? 0.1328 0.1899 0.1667 0.0157  0.0089  0.0099  443 VAL A CA  
3764 C C   . VAL A 443 ? 0.1581 0.2285 0.1876 0.0143  0.0100  0.0078  443 VAL A C   
3765 O O   . VAL A 443 ? 0.1545 0.2277 0.1831 0.0095  0.0113  0.0095  443 VAL A O   
3766 C CB  . VAL A 443 ? 0.1420 0.1988 0.1741 0.0201  0.0092  0.0164  443 VAL A CB  
3767 C CG1 . VAL A 443 ? 0.1409 0.2064 0.1685 0.0160  0.0117  0.0216  443 VAL A CG1 
3768 C CG2 . VAL A 443 ? 0.1701 0.2086 0.2055 0.0214  0.0077  0.0207  443 VAL A CG2 
3769 N N   . ALA A 444 ? 0.1393 0.2180 0.1667 0.0184  0.0101  0.0042  444 ALA A N   
3770 C CA  . ALA A 444 ? 0.1713 0.2628 0.1954 0.0150  0.0120  0.0042  444 ALA A CA  
3771 C C   . ALA A 444 ? 0.1496 0.2375 0.1692 0.0109  0.0114  0.0031  444 ALA A C   
3772 O O   . ALA A 444 ? 0.1463 0.2395 0.1624 0.0061  0.0127  0.0057  444 ALA A O   
3773 C CB  . ALA A 444 ? 0.1551 0.2612 0.1801 0.0205  0.0138  0.0013  444 ALA A CB  
3774 N N   . GLU A 445 ? 0.1315 0.2101 0.1514 0.0122  0.0085  -0.0002 445 GLU A N   
3775 C CA  . GLU A 445 ? 0.1382 0.2147 0.1539 0.0097  0.0058  -0.0007 445 GLU A CA  
3776 C C   . GLU A 445 ? 0.1397 0.2116 0.1607 0.0061  0.0048  0.0028  445 GLU A C   
3777 O O   . GLU A 445 ? 0.1456 0.2158 0.1650 0.0057  0.0014  0.0031  445 GLU A O   
3778 C CB  . GLU A 445 ? 0.1403 0.2120 0.1548 0.0127  0.0013  -0.0078 445 GLU A CB  
3779 C CG  . GLU A 445 ? 0.1620 0.2396 0.1676 0.0183  0.0027  -0.0138 445 GLU A CG  
3780 C CD  . GLU A 445 ? 0.1705 0.2393 0.1757 0.0227  -0.0021 -0.0242 445 GLU A CD  
3781 O OE1 . GLU A 445 ? 0.1823 0.2407 0.1954 0.0192  -0.0073 -0.0262 445 GLU A OE1 
3782 O OE2 . GLU A 445 ? 0.1765 0.2499 0.1739 0.0294  -0.0006 -0.0315 445 GLU A OE2 
3783 N N   . GLY A 446 ? 0.1462 0.2173 0.1727 0.0050  0.0074  0.0051  446 GLY A N   
3784 C CA  . GLY A 446 ? 0.1312 0.2007 0.1620 0.0033  0.0080  0.0066  446 GLY A CA  
3785 C C   . GLY A 446 ? 0.1358 0.2031 0.1612 0.0023  0.0071  0.0079  446 GLY A C   
3786 O O   . GLY A 446 ? 0.1618 0.2305 0.1811 -0.0001 0.0082  0.0095  446 GLY A O   
3787 N N   . SER A 447 ? 0.1300 0.1941 0.1595 0.0040  0.0050  0.0076  447 SER A N   
3788 C CA  . SER A 447 ? 0.1434 0.1997 0.1676 0.0040  0.0028  0.0098  447 SER A CA  
3789 C C   . SER A 447 ? 0.1684 0.2200 0.1897 0.0012  0.0057  0.0089  447 SER A C   
3790 O O   . SER A 447 ? 0.1454 0.1882 0.1610 -0.0021 0.0042  0.0114  447 SER A O   
3791 C CB  . SER A 447 ? 0.1489 0.2028 0.1800 0.0095  -0.0011 0.0090  447 SER A CB  
3792 O OG  . SER A 447 ? 0.1452 0.2033 0.1859 0.0121  0.0025  0.0051  447 SER A OG  
3793 N N   . ASP A 448 ? 0.1330 0.1900 0.1572 0.0016  0.0092  0.0058  448 ASP A N   
3794 C CA  . ASP A 448 ? 0.1551 0.2087 0.1751 -0.0002 0.0105  0.0024  448 ASP A CA  
3795 C C   . ASP A 448 ? 0.1620 0.2152 0.1769 -0.0071 0.0091  0.0040  448 ASP A C   
3796 O O   . ASP A 448 ? 0.1546 0.1986 0.1665 -0.0111 0.0072  0.0017  448 ASP A O   
3797 C CB  . ASP A 448 ? 0.1620 0.2249 0.1821 0.0014  0.0146  0.0003  448 ASP A CB  
3798 C CG  . ASP A 448 ? 0.1372 0.2048 0.1650 0.0059  0.0178  -0.0002 448 ASP A CG  
3799 O OD1 . ASP A 448 ? 0.1257 0.1978 0.1601 0.0055  0.0178  0.0034  448 ASP A OD1 
3800 O OD2 . ASP A 448 ? 0.1423 0.2101 0.1708 0.0098  0.0203  -0.0049 448 ASP A OD2 
3801 N N   . TRP A 449 ? 0.1292 0.1929 0.1445 -0.0087 0.0099  0.0072  449 TRP A N   
3802 C CA  . TRP A 449 ? 0.1529 0.2237 0.1672 -0.0152 0.0097  0.0084  449 TRP A CA  
3803 C C   . TRP A 449 ? 0.1409 0.2024 0.1528 -0.0217 0.0085  0.0121  449 TRP A C   
3804 O O   . TRP A 449 ? 0.1500 0.2095 0.1624 -0.0299 0.0074  0.0118  449 TRP A O   
3805 C CB  . TRP A 449 ? 0.1769 0.2623 0.1936 -0.0128 0.0114  0.0103  449 TRP A CB  
3806 C CG  . TRP A 449 ? 0.1289 0.2163 0.1473 -0.0059 0.0119  0.0092  449 TRP A CG  
3807 C CD1 . TRP A 449 ? 0.1593 0.2448 0.1794 -0.0011 0.0123  0.0096  449 TRP A CD1 
3808 C CD2 . TRP A 449 ? 0.1425 0.2323 0.1598 -0.0041 0.0118  0.0084  449 TRP A CD2 
3809 N NE1 . TRP A 449 ? 0.1351 0.2197 0.1570 0.0025  0.0128  0.0103  449 TRP A NE1 
3810 C CE2 . TRP A 449 ? 0.1418 0.2299 0.1608 0.0011  0.0129  0.0106  449 TRP A CE2 
3811 C CE3 . TRP A 449 ? 0.1607 0.2538 0.1744 -0.0068 0.0102  0.0059  449 TRP A CE3 
3812 C CZ2 . TRP A 449 ? 0.1293 0.2185 0.1457 0.0036  0.0137  0.0132  449 TRP A CZ2 
3813 C CZ3 . TRP A 449 ? 0.1664 0.2630 0.1755 -0.0030 0.0105  0.0067  449 TRP A CZ3 
3814 C CH2 . TRP A 449 ? 0.1332 0.2278 0.1433 0.0021  0.0127  0.0117  449 TRP A CH2 
3815 N N   . PHE A 450 ? 0.1635 0.2177 0.1723 -0.0186 0.0079  0.0161  450 PHE A N   
3816 C CA  . PHE A 450 ? 0.1633 0.2068 0.1668 -0.0242 0.0067  0.0228  450 PHE A CA  
3817 C C   . PHE A 450 ? 0.1874 0.2088 0.1902 -0.0247 0.0029  0.0217  450 PHE A C   
3818 O O   . PHE A 450 ? 0.2333 0.2413 0.2329 -0.0325 0.0015  0.0271  450 PHE A O   
3819 C CB  . PHE A 450 ? 0.1615 0.2059 0.1590 -0.0191 0.0059  0.0275  450 PHE A CB  
3820 C CG  . PHE A 450 ? 0.1502 0.2131 0.1475 -0.0163 0.0090  0.0254  450 PHE A CG  
3821 C CD1 . PHE A 450 ? 0.1672 0.2347 0.1700 -0.0093 0.0084  0.0190  450 PHE A CD1 
3822 C CD2 . PHE A 450 ? 0.1664 0.2418 0.1587 -0.0207 0.0132  0.0295  450 PHE A CD2 
3823 C CE1 . PHE A 450 ? 0.1641 0.2433 0.1667 -0.0059 0.0103  0.0159  450 PHE A CE1 
3824 C CE2 . PHE A 450 ? 0.1792 0.2709 0.1714 -0.0156 0.0161  0.0251  450 PHE A CE2 
3825 C CZ  . PHE A 450 ? 0.1635 0.2546 0.1607 -0.0078 0.0139  0.0178  450 PHE A CZ  
3826 N N   . TRP A 451 ? 0.1789 0.1961 0.1853 -0.0164 0.0017  0.0148  451 TRP A N   
3827 C CA  . TRP A 451 ? 0.1882 0.1853 0.1945 -0.0135 -0.0015 0.0106  451 TRP A CA  
3828 C C   . TRP A 451 ? 0.2009 0.1896 0.2058 -0.0228 -0.0025 0.0061  451 TRP A C   
3829 O O   . TRP A 451 ? 0.2519 0.2176 0.2546 -0.0268 -0.0062 0.0070  451 TRP A O   
3830 C CB  . TRP A 451 ? 0.2011 0.2043 0.2129 -0.0028 0.0000  0.0027  451 TRP A CB  
3831 C CG  . TRP A 451 ? 0.2219 0.2099 0.2343 0.0032  -0.0015 -0.0055 451 TRP A CG  
3832 C CD1 . TRP A 451 ? 0.2294 0.2161 0.2390 0.0024  -0.0001 -0.0156 451 TRP A CD1 
3833 C CD2 . TRP A 451 ? 0.2700 0.2431 0.2857 0.0130  -0.0052 -0.0058 451 TRP A CD2 
3834 N NE1 . TRP A 451 ? 0.2695 0.2401 0.2798 0.0112  -0.0018 -0.0237 451 TRP A NE1 
3835 C CE2 . TRP A 451 ? 0.3079 0.2699 0.3234 0.0185  -0.0050 -0.0174 451 TRP A CE2 
3836 C CE3 . TRP A 451 ? 0.3010 0.2698 0.3192 0.0189  -0.0096 0.0021  451 TRP A CE3 
3837 C CZ2 . TRP A 451 ? 0.3259 0.2718 0.3456 0.0309  -0.0084 -0.0217 451 TRP A CZ2 
3838 C CZ3 . TRP A 451 ? 0.3392 0.2930 0.3618 0.0308  -0.0140 -0.0004 451 TRP A CZ3 
3839 C CH2 . TRP A 451 ? 0.3422 0.2844 0.3666 0.0372  -0.0131 -0.0123 451 TRP A CH2 
3840 N N   . TRP A 452 ? 0.2065 0.2126 0.2129 -0.0265 -0.0003 0.0011  452 TRP A N   
3841 C CA  . TRP A 452 ? 0.2010 0.2037 0.2069 -0.0352 -0.0030 -0.0057 452 TRP A CA  
3842 C C   . TRP A 452 ? 0.2239 0.2292 0.2330 -0.0498 -0.0039 0.0010  452 TRP A C   
3843 O O   . TRP A 452 ? 0.2367 0.2324 0.2472 -0.0600 -0.0078 -0.0037 452 TRP A O   
3844 C CB  . TRP A 452 ? 0.1884 0.2113 0.1935 -0.0323 -0.0017 -0.0127 452 TRP A CB  
3845 C CG  . TRP A 452 ? 0.1864 0.2082 0.1880 -0.0205 0.0007  -0.0188 452 TRP A CG  
3846 C CD1 . TRP A 452 ? 0.1910 0.2278 0.1938 -0.0131 0.0052  -0.0159 452 TRP A CD1 
3847 C CD2 . TRP A 452 ? 0.2044 0.2098 0.2022 -0.0147 -0.0004 -0.0285 452 TRP A CD2 
3848 N NE1 . TRP A 452 ? 0.1792 0.2135 0.1799 -0.0046 0.0079  -0.0220 452 TRP A NE1 
3849 C CE2 . TRP A 452 ? 0.1956 0.2122 0.1930 -0.0040 0.0049  -0.0307 452 TRP A CE2 
3850 C CE3 . TRP A 452 ? 0.2303 0.2119 0.2254 -0.0175 -0.0052 -0.0362 452 TRP A CE3 
3851 C CZ2 . TRP A 452 ? 0.2164 0.2261 0.2114 0.0053  0.0068  -0.0407 452 TRP A CZ2 
3852 C CZ3 . TRP A 452 ? 0.2463 0.2164 0.2377 -0.0067 -0.0047 -0.0476 452 TRP A CZ3 
3853 C CH2 . TRP A 452 ? 0.2692 0.2559 0.2608 0.0051  0.0019  -0.0500 452 TRP A CH2 
3854 N N   . GLN A 453 ? 0.2214 0.2406 0.2321 -0.0514 0.0000  0.0110  453 GLN A N   
3855 C CA  . GLN A 453 ? 0.2389 0.2670 0.2537 -0.0652 0.0016  0.0185  453 GLN A CA  
3856 C C   . GLN A 453 ? 0.2548 0.2554 0.2659 -0.0739 -0.0004 0.0264  453 GLN A C   
3857 O O   . GLN A 453 ? 0.3110 0.2912 0.3148 -0.0659 -0.0020 0.0304  453 GLN A O   
3858 C CB  . GLN A 453 ? 0.2279 0.2800 0.2433 -0.0617 0.0075  0.0253  453 GLN A CB  
3859 C CG  . GLN A 453 ? 0.2421 0.3075 0.2607 -0.0743 0.0119  0.0347  453 GLN A CG  
3860 C CD  . GLN A 453 ? 0.2623 0.3534 0.2945 -0.0836 0.0124  0.0307  453 GLN A CD  
3861 O OE1 . GLN A 453 ? 0.2802 0.3719 0.3169 -0.0833 0.0071  0.0212  453 GLN A OE1 
3862 N NE2 . GLN A 453 ? 0.2837 0.3992 0.3225 -0.0915 0.0187  0.0377  453 GLN A NE2 
3863 N N   . GLY A 454 ? 0.3340 0.3337 0.3511 -0.0908 -0.0012 0.0291  454 GLY A N   
3864 C CA  . GLY A 454 ? 0.3182 0.2897 0.3316 -0.1016 -0.0027 0.0397  454 GLY A CA  
3865 C C   . GLY A 454 ? 0.4301 0.3617 0.4386 -0.0970 -0.0101 0.0334  454 GLY A C   
3866 O O   . GLY A 454 ? 0.4189 0.3226 0.4199 -0.0947 -0.0121 0.0433  454 GLY A O   
3867 N N   . GLU A 455 ? 0.3770 0.3057 0.3885 -0.0941 -0.0147 0.0168  455 GLU A N   
3868 C CA  . GLU A 455 ? 0.4384 0.3316 0.4456 -0.0879 -0.0213 0.0063  455 GLU A CA  
3869 C C   . GLU A 455 ? 0.4849 0.3700 0.4972 -0.1024 -0.0273 -0.0060 455 GLU A C   
3870 O O   . GLU A 455 ? 0.4919 0.4068 0.5116 -0.1121 -0.0267 -0.0095 455 GLU A O   
3871 C CB  . GLU A 455 ? 0.4013 0.3013 0.4043 -0.0669 -0.0205 -0.0052 455 GLU A CB  
3872 C CG  . GLU A 455 ? 0.3961 0.3075 0.3968 -0.0535 -0.0160 0.0045  455 GLU A CG  
3873 C CD  . GLU A 455 ? 0.4333 0.3147 0.4296 -0.0478 -0.0194 0.0139  455 GLU A CD  
3874 O OE1 . GLU A 455 ? 0.4820 0.3294 0.4770 -0.0496 -0.0251 0.0104  455 GLU A OE1 
3875 O OE2 . GLU A 455 ? 0.4070 0.2974 0.4006 -0.0409 -0.0175 0.0246  455 GLU A OE2 
3876 N N   . GLU A 456 ? 0.5368 0.3813 0.5458 -0.1031 -0.0342 -0.0135 456 GLU A N   
3877 C CA  . GLU A 456 ? 0.7093 0.5408 0.7224 -0.1180 -0.0418 -0.0275 456 GLU A CA  
3878 C C   . GLU A 456 ? 0.7804 0.6423 0.7922 -0.1124 -0.0430 -0.0454 456 GLU A C   
3879 O O   . GLU A 456 ? 0.7712 0.6403 0.7746 -0.0930 -0.0405 -0.0539 456 GLU A O   
3880 C CB  . GLU A 456 ? 0.7810 0.5598 0.7885 -0.1143 -0.0496 -0.0364 456 GLU A CB  
3881 C CG  . GLU A 456 ? 0.8472 0.6097 0.8462 -0.0885 -0.0480 -0.0384 456 GLU A CG  
3882 C CD  . GLU A 456 ? 0.9773 0.6842 0.9729 -0.0845 -0.0558 -0.0422 456 GLU A CD  
3883 O OE1 . GLU A 456 ? 1.0099 0.7018 1.0003 -0.0661 -0.0584 -0.0605 456 GLU A OE1 
3884 O OE2 . GLU A 456 ? 1.0311 0.7091 1.0288 -0.0991 -0.0589 -0.0267 456 GLU A OE2 
3885 N N   . LYS A 457 ? 0.7758 0.6576 0.7965 -0.1301 -0.0470 -0.0499 457 LYS A N   
3886 C CA  . LYS A 457 ? 0.7597 0.6773 0.7796 -0.1269 -0.0490 -0.0623 457 LYS A CA  
3887 C C   . LYS A 457 ? 0.7731 0.6819 0.7773 -0.1083 -0.0511 -0.0806 457 LYS A C   
3888 O O   . LYS A 457 ? 0.8065 0.6790 0.8035 -0.1047 -0.0557 -0.0928 457 LYS A O   
3889 C CB  . LYS A 457 ? 0.8079 0.7350 0.8395 -0.1495 -0.0579 -0.0700 457 LYS A CB  
3890 C CG  . LYS A 457 ? 0.8962 0.7781 0.9308 -0.1657 -0.0658 -0.0754 457 LYS A CG  
3891 C CD  . LYS A 457 ? 0.9251 0.8195 0.9750 -0.1914 -0.0753 -0.0829 457 LYS A CD  
3892 C CE  . LYS A 457 ? 0.9199 0.8112 0.9602 -0.1888 -0.0873 -0.1101 457 LYS A CE  
3893 N NZ  . LYS A 457 ? 0.9087 0.8370 0.9643 -0.2076 -0.0961 -0.1169 457 LYS A NZ  
3894 N N   . ALA A 458 ? 0.7436 0.6858 0.7420 -0.0963 -0.0471 -0.0822 458 ALA A N   
3895 C CA  . ALA A 458 ? 0.7733 0.7159 0.7557 -0.0792 -0.0466 -0.0971 458 ALA A CA  
3896 C C   . ALA A 458 ? 0.7306 0.7129 0.7087 -0.0769 -0.0471 -0.0988 458 ALA A C   
3897 O O   . ALA A 458 ? 0.7321 0.7412 0.7209 -0.0825 -0.0454 -0.0859 458 ALA A O   
3898 C CB  . ALA A 458 ? 0.7504 0.6852 0.7285 -0.0605 -0.0373 -0.0906 458 ALA A CB  
3899 N N   . PRO A 459 ? 0.6357 0.6229 0.5970 -0.0678 -0.0497 -0.1144 459 PRO A N   
3900 C CA  . PRO A 459 ? 0.5551 0.5785 0.5087 -0.0630 -0.0500 -0.1129 459 PRO A CA  
3901 C C   . PRO A 459 ? 0.5713 0.6119 0.5272 -0.0514 -0.0389 -0.0951 459 PRO A C   
3902 O O   . PRO A 459 ? 0.5264 0.5534 0.4826 -0.0421 -0.0305 -0.0901 459 PRO A O   
3903 C CB  . PRO A 459 ? 0.5874 0.6072 0.5179 -0.0534 -0.0527 -0.1326 459 PRO A CB  
3904 C CG  . PRO A 459 ? 0.6251 0.6071 0.5530 -0.0492 -0.0513 -0.1444 459 PRO A CG  
3905 C CD  . PRO A 459 ? 0.6727 0.6321 0.6205 -0.0634 -0.0543 -0.1356 459 PRO A CD  
3906 N N   . PHE A 460 ? 0.5853 0.6557 0.5448 -0.0524 -0.0402 -0.0859 460 PHE A N   
3907 C CA  . PHE A 460 ? 0.4733 0.5612 0.4344 -0.0424 -0.0322 -0.0703 460 PHE A CA  
3908 C C   . PHE A 460 ? 0.3670 0.4512 0.3450 -0.0447 -0.0261 -0.0561 460 PHE A C   
3909 O O   . PHE A 460 ? 0.3467 0.4440 0.3271 -0.0374 -0.0208 -0.0448 460 PHE A O   
3910 C CB  . PHE A 460 ? 0.4172 0.5023 0.3625 -0.0281 -0.0239 -0.0708 460 PHE A CB  
3911 C CG  . PHE A 460 ? 0.4445 0.5343 0.3684 -0.0238 -0.0278 -0.0848 460 PHE A CG  
3912 C CD1 . PHE A 460 ? 0.4589 0.5673 0.3757 -0.0284 -0.0382 -0.0894 460 PHE A CD1 
3913 C CD2 . PHE A 460 ? 0.5435 0.6217 0.4540 -0.0145 -0.0212 -0.0942 460 PHE A CD2 
3914 C CE1 . PHE A 460 ? 0.5490 0.6629 0.4425 -0.0242 -0.0427 -0.1032 460 PHE A CE1 
3915 C CE2 . PHE A 460 ? 0.5530 0.6375 0.4406 -0.0098 -0.0239 -0.1086 460 PHE A CE2 
3916 C CZ  . PHE A 460 ? 0.5597 0.6610 0.4370 -0.0149 -0.0350 -0.1131 460 PHE A CZ  
3917 N N   . VAL A 461 ? 0.3495 0.4160 0.3378 -0.0545 -0.0269 -0.0558 461 VAL A N   
3918 C CA  . VAL A 461 ? 0.3100 0.3775 0.3109 -0.0568 -0.0213 -0.0419 461 VAL A CA  
3919 C C   . VAL A 461 ? 0.3266 0.4247 0.3376 -0.0591 -0.0218 -0.0342 461 VAL A C   
3920 O O   . VAL A 461 ? 0.2887 0.3953 0.3048 -0.0534 -0.0159 -0.0240 461 VAL A O   
3921 C CB  . VAL A 461 ? 0.3400 0.3849 0.3482 -0.0690 -0.0228 -0.0406 461 VAL A CB  
3922 C CG1 . VAL A 461 ? 0.4498 0.5007 0.4665 -0.0861 -0.0308 -0.0463 461 VAL A CG1 
3923 C CG2 . VAL A 461 ? 0.3648 0.4125 0.3809 -0.0697 -0.0163 -0.0257 461 VAL A CG2 
3924 N N   . GLU A 462 ? 0.2492 0.3653 0.2640 -0.0663 -0.0298 -0.0404 462 GLU A N   
3925 C CA  . GLU A 462 ? 0.2515 0.4000 0.2778 -0.0657 -0.0313 -0.0342 462 GLU A CA  
3926 C C   . GLU A 462 ? 0.2532 0.4110 0.2715 -0.0491 -0.0278 -0.0280 462 GLU A C   
3927 O O   . GLU A 462 ? 0.2252 0.4017 0.2533 -0.0441 -0.0258 -0.0202 462 GLU A O   
3928 C CB  . GLU A 462 ? 0.2875 0.4560 0.3190 -0.0749 -0.0427 -0.0433 462 GLU A CB  
3929 C CG  . GLU A 462 ? 0.4383 0.5981 0.4811 -0.0948 -0.0474 -0.0495 462 GLU A CG  
3930 C CD  . GLU A 462 ? 0.4855 0.6120 0.5133 -0.0980 -0.0517 -0.0626 462 GLU A CD  
3931 O OE1 . GLU A 462 ? 0.3394 0.4536 0.3480 -0.0842 -0.0497 -0.0673 462 GLU A OE1 
3932 O OE2 . GLU A 462 ? 0.5063 0.6185 0.5421 -0.1146 -0.0566 -0.0683 462 GLU A OE2 
3933 N N   . VAL A 463 ? 0.1988 0.3435 0.1997 -0.0404 -0.0266 -0.0312 463 VAL A N   
3934 C CA  . VAL A 463 ? 0.1795 0.3301 0.1728 -0.0271 -0.0228 -0.0232 463 VAL A CA  
3935 C C   . VAL A 463 ? 0.1831 0.3224 0.1822 -0.0224 -0.0137 -0.0146 463 VAL A C   
3936 O O   . VAL A 463 ? 0.1770 0.3245 0.1802 -0.0151 -0.0117 -0.0065 463 VAL A O   
3937 C CB  . VAL A 463 ? 0.2135 0.3578 0.1863 -0.0208 -0.0227 -0.0280 463 VAL A CB  
3938 C CG1 . VAL A 463 ? 0.2778 0.4280 0.2433 -0.0095 -0.0190 -0.0168 463 VAL A CG1 
3939 C CG2 . VAL A 463 ? 0.2192 0.3745 0.1834 -0.0255 -0.0332 -0.0391 463 VAL A CG2 
3940 N N   . PHE A 464 ? 0.1612 0.2808 0.1604 -0.0257 -0.0095 -0.0167 464 PHE A N   
3941 C CA  . PHE A 464 ? 0.1484 0.2597 0.1529 -0.0220 -0.0029 -0.0095 464 PHE A CA  
3942 C C   . PHE A 464 ? 0.1389 0.2630 0.1554 -0.0248 -0.0025 -0.0042 464 PHE A C   
3943 O O   . PHE A 464 ? 0.1624 0.2890 0.1817 -0.0182 0.0011  0.0013  464 PHE A O   
3944 C CB  . PHE A 464 ? 0.1614 0.2513 0.1646 -0.0245 -0.0006 -0.0124 464 PHE A CB  
3945 C CG  . PHE A 464 ? 0.1618 0.2418 0.1557 -0.0180 0.0017  -0.0176 464 PHE A CG  
3946 C CD1 . PHE A 464 ? 0.1568 0.2353 0.1513 -0.0106 0.0073  -0.0130 464 PHE A CD1 
3947 C CD2 . PHE A 464 ? 0.1795 0.2538 0.1650 -0.0197 -0.0016 -0.0282 464 PHE A CD2 
3948 C CE1 . PHE A 464 ? 0.1607 0.2359 0.1493 -0.0049 0.0112  -0.0174 464 PHE A CE1 
3949 C CE2 . PHE A 464 ? 0.1886 0.2576 0.1650 -0.0121 0.0023  -0.0341 464 PHE A CE2 
3950 C CZ  . PHE A 464 ? 0.1782 0.2495 0.1572 -0.0047 0.0094  -0.0279 464 PHE A CZ  
3951 N N   . ASP A 465 ? 0.1478 0.2818 0.1719 -0.0349 -0.0060 -0.0065 465 ASP A N   
3952 C CA  . ASP A 465 ? 0.1369 0.2887 0.1735 -0.0378 -0.0037 -0.0016 465 ASP A CA  
3953 C C   . ASP A 465 ? 0.1297 0.3045 0.1718 -0.0282 -0.0055 0.0001  465 ASP A C   
3954 O O   . ASP A 465 ? 0.1637 0.3477 0.2120 -0.0219 -0.0013 0.0039  465 ASP A O   
3955 C CB  . ASP A 465 ? 0.1482 0.3071 0.1942 -0.0534 -0.0064 -0.0036 465 ASP A CB  
3956 C CG  . ASP A 465 ? 0.1943 0.3806 0.2555 -0.0571 -0.0029 0.0012  465 ASP A CG  
3957 O OD1 . ASP A 465 ? 0.1875 0.3706 0.2491 -0.0588 0.0042  0.0072  465 ASP A OD1 
3958 O OD2 . ASP A 465 ? 0.1394 0.3528 0.2118 -0.0575 -0.0072 -0.0012 465 ASP A OD2 
3959 N N   . LYS A 466 ? 0.1355 0.3194 0.1742 -0.0256 -0.0123 -0.0031 466 LYS A N   
3960 C CA  . LYS A 466 ? 0.1419 0.3439 0.1840 -0.0139 -0.0155 0.0003  466 LYS A CA  
3961 C C   . LYS A 466 ? 0.1479 0.3345 0.1832 -0.0018 -0.0106 0.0061  466 LYS A C   
3962 O O   . LYS A 466 ? 0.1796 0.3749 0.2222 0.0076  -0.0097 0.0093  466 LYS A O   
3963 C CB  . LYS A 466 ? 0.1593 0.3702 0.1935 -0.0126 -0.0247 -0.0028 466 LYS A CB  
3964 C CG  . LYS A 466 ? 0.1858 0.4111 0.2199 0.0016  -0.0294 0.0031  466 LYS A CG  
3965 C CD  . LYS A 466 ? 0.2211 0.4629 0.2485 0.0019  -0.0408 0.0001  466 LYS A CD  
3966 C CE  . LYS A 466 ? 0.3772 0.6380 0.4092 0.0166  -0.0474 0.0071  466 LYS A CE  
3967 N NZ  . LYS A 466 ? 0.5143 0.8086 0.5572 0.0140  -0.0596 0.0020  466 LYS A NZ  
3968 N N   . LEU A 467 ? 0.1448 0.3089 0.1675 -0.0018 -0.0075 0.0066  467 LEU A N   
3969 C CA  . LEU A 467 ? 0.1599 0.3093 0.1786 0.0066  -0.0032 0.0120  467 LEU A CA  
3970 C C   . LEU A 467 ? 0.1665 0.3123 0.1933 0.0076  0.0015  0.0121  467 LEU A C   
3971 O O   . LEU A 467 ? 0.1500 0.2954 0.1803 0.0164  0.0021  0.0145  467 LEU A O   
3972 C CB  . LEU A 467 ? 0.1648 0.2966 0.1721 0.0046  0.0001  0.0119  467 LEU A CB  
3973 C CG  . LEU A 467 ? 0.1963 0.3311 0.1906 0.0070  -0.0026 0.0132  467 LEU A CG  
3974 C CD1 . LEU A 467 ? 0.1505 0.2741 0.1352 0.0040  0.0020  0.0095  467 LEU A CD1 
3975 C CD2 . LEU A 467 ? 0.1860 0.3194 0.1765 0.0161  -0.0031 0.0232  467 LEU A CD2 
3976 N N   . PHE A 468 ? 0.1394 0.2810 0.1676 -0.0007 0.0043  0.0093  468 PHE A N   
3977 C CA  . PHE A 468 ? 0.1459 0.2854 0.1776 0.0000  0.0085  0.0096  468 PHE A CA  
3978 C C   . PHE A 468 ? 0.1511 0.3109 0.1918 0.0056  0.0092  0.0092  468 PHE A C   
3979 O O   . PHE A 468 ? 0.1523 0.3094 0.1936 0.0142  0.0111  0.0083  468 PHE A O   
3980 C CB  . PHE A 468 ? 0.1359 0.2700 0.1662 -0.0102 0.0104  0.0092  468 PHE A CB  
3981 C CG  . PHE A 468 ? 0.1142 0.2512 0.1450 -0.0102 0.0146  0.0107  468 PHE A CG  
3982 C CD1 . PHE A 468 ? 0.1286 0.2520 0.1537 -0.0054 0.0156  0.0105  468 PHE A CD1 
3983 C CD2 . PHE A 468 ? 0.1382 0.2937 0.1748 -0.0158 0.0174  0.0120  468 PHE A CD2 
3984 C CE1 . PHE A 468 ? 0.1383 0.2652 0.1599 -0.0046 0.0186  0.0109  468 PHE A CE1 
3985 C CE2 . PHE A 468 ? 0.1403 0.3007 0.1737 -0.0154 0.0225  0.0138  468 PHE A CE2 
3986 C CZ  . PHE A 468 ? 0.1286 0.2736 0.1526 -0.0091 0.0227  0.0128  468 PHE A CZ  
3987 N N   . ARG A 469 ? 0.1180 0.2994 0.1670 0.0015  0.0070  0.0084  469 ARG A N   
3988 C CA  . ARG A 469 ? 0.1119 0.3188 0.1731 0.0074  0.0085  0.0073  469 ARG A CA  
3989 C C   . ARG A 469 ? 0.1276 0.3360 0.1908 0.0231  0.0047  0.0077  469 ARG A C   
3990 O O   . ARG A 469 ? 0.1583 0.3769 0.2284 0.0337  0.0071  0.0054  469 ARG A O   
3991 C CB  . ARG A 469 ? 0.1169 0.3501 0.1903 -0.0031 0.0067  0.0066  469 ARG A CB  
3992 C CG  . ARG A 469 ? 0.1703 0.4006 0.2432 -0.0187 0.0118  0.0081  469 ARG A CG  
3993 C CD  . ARG A 469 ? 0.1670 0.4185 0.2530 -0.0330 0.0089  0.0075  469 ARG A CD  
3994 N NE  . ARG A 469 ? 0.1767 0.4223 0.2625 -0.0493 0.0139  0.0114  469 ARG A NE  
3995 C CZ  . ARG A 469 ? 0.2032 0.4677 0.2962 -0.0544 0.0223  0.0157  469 ARG A CZ  
3996 N NH1 . ARG A 469 ? 0.1752 0.4673 0.2770 -0.0430 0.0272  0.0143  469 ARG A NH1 
3997 N NH2 . ARG A 469 ? 0.2345 0.4897 0.3250 -0.0703 0.0262  0.0218  469 ARG A NH2 
3998 N N   . SER A 470 ? 0.1414 0.3382 0.1972 0.0256  -0.0009 0.0108  470 SER A N   
3999 C CA  . SER A 470 ? 0.1507 0.3431 0.2059 0.0403  -0.0050 0.0141  470 SER A CA  
4000 C C   . SER A 470 ? 0.1895 0.3569 0.2398 0.0469  -0.0014 0.0143  470 SER A C   
4001 O O   . SER A 470 ? 0.1816 0.3470 0.2366 0.0601  -0.0028 0.0138  470 SER A O   
4002 C CB  . SER A 470 ? 0.2282 0.4142 0.2729 0.0399  -0.0111 0.0195  470 SER A CB  
4003 O OG  . SER A 470 ? 0.3632 0.5746 0.4132 0.0364  -0.0173 0.0176  470 SER A OG  
4004 N N   . PHE A 471 ? 0.1803 0.3284 0.2226 0.0383  0.0023  0.0141  471 PHE A N   
4005 C CA  . PHE A 471 ? 0.1427 0.2692 0.1822 0.0423  0.0044  0.0127  471 PHE A CA  
4006 C C   . PHE A 471 ? 0.1744 0.3094 0.2188 0.0474  0.0076  0.0052  471 PHE A C   
4007 O O   . PHE A 471 ? 0.1796 0.3032 0.2248 0.0572  0.0069  0.0015  471 PHE A O   
4008 C CB  . PHE A 471 ? 0.1482 0.2586 0.1810 0.0322  0.0069  0.0136  471 PHE A CB  
4009 C CG  . PHE A 471 ? 0.1669 0.2694 0.1936 0.0286  0.0058  0.0200  471 PHE A CG  
4010 C CD1 . PHE A 471 ? 0.1865 0.2804 0.2106 0.0350  0.0033  0.0269  471 PHE A CD1 
4011 C CD2 . PHE A 471 ? 0.1489 0.2521 0.1712 0.0198  0.0077  0.0193  471 PHE A CD2 
4012 C CE1 . PHE A 471 ? 0.1976 0.2870 0.2130 0.0314  0.0039  0.0339  471 PHE A CE1 
4013 C CE2 . PHE A 471 ? 0.1712 0.2703 0.1864 0.0177  0.0082  0.0236  471 PHE A CE2 
4014 C CZ  . PHE A 471 ? 0.1983 0.2922 0.2092 0.0229  0.0069  0.0313  471 PHE A CZ  
4015 N N   . VAL A 472 ? 0.1467 0.3011 0.1936 0.0405  0.0114  0.0028  472 VAL A N   
4016 C CA  . VAL A 472 ? 0.1666 0.3348 0.2161 0.0449  0.0163  -0.0034 472 VAL A CA  
4017 C C   . VAL A 472 ? 0.1739 0.3585 0.2338 0.0599  0.0155  -0.0072 472 VAL A C   
4018 O O   . VAL A 472 ? 0.1753 0.3582 0.2349 0.0709  0.0177  -0.0147 472 VAL A O   
4019 C CB  . VAL A 472 ? 0.1727 0.3595 0.2228 0.0324  0.0211  -0.0017 472 VAL A CB  
4020 C CG1 . VAL A 472 ? 0.2168 0.4280 0.2710 0.0371  0.0278  -0.0064 472 VAL A CG1 
4021 C CG2 . VAL A 472 ? 0.1799 0.3465 0.2185 0.0221  0.0216  0.0007  472 VAL A CG2 
4022 N N   . ARG A 473 ? 0.1418 0.3431 0.2110 0.0619  0.0115  -0.0032 473 ARG A N   
4023 C CA  . ARG A 473 ? 0.1540 0.3729 0.2354 0.0786  0.0093  -0.0062 473 ARG A CA  
4024 C C   . ARG A 473 ? 0.1919 0.3809 0.2686 0.0930  0.0045  -0.0065 473 ARG A C   
4025 O O   . ARG A 473 ? 0.1782 0.3672 0.2596 0.1084  0.0053  -0.0140 473 ARG A O   
4026 C CB  . ARG A 473 ? 0.1565 0.4006 0.2487 0.0772  0.0036  -0.0013 473 ARG A CB  
4027 C CG  . ARG A 473 ? 0.2502 0.5134 0.3566 0.0966  -0.0011 -0.0030 473 ARG A CG  
4028 C CD  . ARG A 473 ? 0.4326 0.7356 0.5550 0.0921  -0.0044 -0.0019 473 ARG A CD  
4029 N NE  . ARG A 473 ? 0.4879 0.7881 0.6056 0.0876  -0.0145 0.0053  473 ARG A NE  
4030 C CZ  . ARG A 473 ? 0.6130 0.9086 0.7296 0.1021  -0.0243 0.0107  473 ARG A CZ  
4031 N NH1 . ARG A 473 ? 0.6211 0.9075 0.7416 0.1209  -0.0255 0.0093  473 ARG A NH1 
4032 N NH2 . ARG A 473 ? 0.5879 0.8813 0.6952 0.0964  -0.0329 0.0171  473 ARG A NH2 
4033 N N   . ARG A 474 ? 0.1958 0.3586 0.2632 0.0880  -0.0003 0.0016  474 ARG A N   
4034 C CA  . ARG A 474 ? 0.2267 0.3581 0.2899 0.0983  -0.0050 0.0045  474 ARG A CA  
4035 C C   . ARG A 474 ? 0.2085 0.3177 0.2679 0.1007  -0.0021 -0.0047 474 ARG A C   
4036 O O   . ARG A 474 ? 0.2513 0.3401 0.3122 0.1139  -0.0057 -0.0079 474 ARG A O   
4037 C CB  . ARG A 474 ? 0.2252 0.3370 0.2781 0.0885  -0.0080 0.0161  474 ARG A CB  
4038 C CG  . ARG A 474 ? 0.3227 0.4016 0.3711 0.0960  -0.0125 0.0232  474 ARG A CG  
4039 C CD  . ARG A 474 ? 0.4006 0.4844 0.4521 0.1114  -0.0200 0.0307  474 ARG A CD  
4040 N NE  . ARG A 474 ? 0.4866 0.5340 0.5318 0.1170  -0.0243 0.0408  474 ARG A NE  
4041 C CZ  . ARG A 474 ? 0.6546 0.6734 0.7030 0.1253  -0.0255 0.0359  474 ARG A CZ  
4042 N NH1 . ARG A 474 ? 0.6604 0.6855 0.7163 0.1308  -0.0225 0.0196  474 ARG A NH1 
4043 N NH2 . ARG A 474 ? 0.7829 0.7659 0.8259 0.1277  -0.0298 0.0474  474 ARG A NH2 
4044 N N   . ALA A 475 ? 0.1933 0.3055 0.2473 0.0886  0.0032  -0.0096 475 ALA A N   
4045 C CA  . ALA A 475 ? 0.1892 0.2838 0.2378 0.0898  0.0046  -0.0196 475 ALA A CA  
4046 C C   . ALA A 475 ? 0.2290 0.3339 0.2813 0.1061  0.0066  -0.0322 475 ALA A C   
4047 O O   . ALA A 475 ? 0.2770 0.3616 0.3243 0.1117  0.0053  -0.0426 475 ALA A O   
4048 C CB  . ALA A 475 ? 0.1794 0.2809 0.2206 0.0753  0.0090  -0.0209 475 ALA A CB  
4049 N N   . GLN A 476 ? 0.2138 0.3516 0.2756 0.1137  0.0097  -0.0328 476 GLN A N   
4050 C CA  . GLN A 476 ? 0.2232 0.3797 0.2902 0.1299  0.0140  -0.0456 476 GLN A CA  
4051 C C   . GLN A 476 ? 0.2473 0.3983 0.3253 0.1511  0.0083  -0.0476 476 GLN A C   
4052 O O   . GLN A 476 ? 0.3035 0.4712 0.3882 0.1684  0.0116  -0.0595 476 GLN A O   
4053 C CB  . GLN A 476 ? 0.2031 0.4051 0.2768 0.1243  0.0225  -0.0452 476 GLN A CB  
4054 C CG  . GLN A 476 ? 0.2259 0.4308 0.2865 0.1067  0.0286  -0.0443 476 GLN A CG  
4055 C CD  . GLN A 476 ? 0.2243 0.4685 0.2918 0.0960  0.0363  -0.0389 476 GLN A CD  
4056 O OE1 . GLN A 476 ? 0.2462 0.5149 0.3147 0.0991  0.0440  -0.0442 476 GLN A OE1 
4057 N NE2 . GLN A 476 ? 0.2035 0.4483 0.2739 0.0807  0.0334  -0.0277 476 GLN A NE2 
4058 N N   . GLU A 477 ? 0.2933 0.4210 0.3721 0.1514  -0.0001 -0.0361 477 GLU A N   
4059 C CA  . GLU A 477 ? 0.3630 0.4852 0.4516 0.1720  -0.0071 -0.0341 477 GLU A CA  
4060 C C   . GLU A 477 ? 0.4686 0.5391 0.5502 0.1784  -0.0142 -0.0335 477 GLU A C   
4061 O O   . GLU A 477 ? 0.5208 0.5633 0.5918 0.1634  -0.0141 -0.0321 477 GLU A O   
4062 C CB  . GLU A 477 ? 0.4338 0.5745 0.5283 0.1687  -0.0122 -0.0189 477 GLU A CB  
4063 C CG  . GLU A 477 ? 0.4921 0.6848 0.5986 0.1638  -0.0071 -0.0206 477 GLU A CG  
4064 C CD  . GLU A 477 ? 0.5641 0.7748 0.6753 0.1591  -0.0141 -0.0080 477 GLU A CD  
4065 O OE1 . GLU A 477 ? 0.5531 0.7997 0.6744 0.1515  -0.0119 -0.0093 477 GLU A OE1 
4066 O OE2 . GLU A 477 ? 0.5862 0.7691 0.6871 0.1576  -0.0214 0.0033  477 GLU A OE2 
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