data_8WGG
# 
_entry.id   8WGG 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_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   8WGG         pdb_00008wgg 10.2210/pdb8wgg/pdb 
WWPDB D_1300041205 ?            ?                   
# 
_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       2025-03-26 
_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                        8WGG 
_pdbx_database_status.recvd_initial_deposition_date   2023-09-21 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBJ 
_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_database_related.db_name        PDB 
_pdbx_database_related.details        'SeMet derivative of the same protein' 
_pdbx_database_related.db_id          8WG6 
_pdbx_database_related.content_type   unspecified 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              kvengadesan@rcb.res.in 
_pdbx_contact_author.name_first         Vengadesan 
_pdbx_contact_author.name_last          Krishnan 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-8083-0121 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Yadav, S.'    1 0000-0003-4345-7265 
'Parijat, P.'  2 ?                   
'Krishnan, V.' 3 0000-0002-8083-0121 
# 
_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                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To be published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'Crystal structure of basal pilin PilB from Streptococcus sanguinis' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Yadav, S.'    1 0000-0003-4345-7265 
primary 'Parijat, P.'  2 ?                   
primary 'Krishnan, V.' 3 0000-0002-8083-0121 
# 
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 'FimA fimbrial subunit-like protein, putative' 48619.457 1   ? ? ? ? 
2 non-polymer syn 'FORMIC ACID'                                  46.025    4   ? ? ? ? 
3 non-polymer syn 'ACETIC ACID'                                  60.052    2   ? ? ? ? 
4 non-polymer syn 1,2-ETHANEDIOL                                 62.068    4   ? ? ? ? 
5 non-polymer syn 'ACETATE ION'                                  59.044    1   ? ? ? ? 
6 non-polymer syn 'SODIUM ION'                                   22.990    1   ? ? ? ? 
7 water       nat water                                          18.015    230 ? ? ? ? 
# 
_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       
;MGSSHHHHHHSSGLVPRRGSHMSADTTTYTIQLTGTSSGHVYELYHIFSGDLDANNVLTNIEWGAGVAIGDRAKFGDASE
KAASLSGKQNDSSEVKAFAQELSNSLSAAGRTRVRSEQGTTTISGLKPGYYLIKDSNGSLDNVKGQAYTSIMLQVAKDTT
IAIKSDVPTLTKQVKASNSENYISATDYAIWDTVPFQITVTLPSNYGDFSKYHFSVKDSMTSGMINNGDIQVYLQQGGSE
VAITDSFSITTNNGLTVSIADLKTLPNVNENSKIVIRYTARLKDSATLGTTGNSNTASLTYSNNPNNNASTTAQTLDSRA
TVYTYRLRLTKVNERQERVAGAGFTLYKKINNQYSEVRKIEASSSSTFDFYGIKAGDYKLVESTTPAGYNTMKDIEFTIT
STIDSTGALTDMTSTSATATFETDVNRGYINLKVVNKQGALLPNTGGIGTT
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MGSSHHHHHHSSGLVPRRGSHMSADTTTYTIQLTGTSSGHVYELYHIFSGDLDANNVLTNIEWGAGVAIGDRAKFGDASE
KAASLSGKQNDSSEVKAFAQELSNSLSAAGRTRVRSEQGTTTISGLKPGYYLIKDSNGSLDNVKGQAYTSIMLQVAKDTT
IAIKSDVPTLTKQVKASNSENYISATDYAIWDTVPFQITVTLPSNYGDFSKYHFSVKDSMTSGMINNGDIQVYLQQGGSE
VAITDSFSITTNNGLTVSIADLKTLPNVNENSKIVIRYTARLKDSATLGTTGNSNTASLTYSNNPNNNASTTAQTLDSRA
TVYTYRLRLTKVNERQERVAGAGFTLYKKINNQYSEVRKIEASSSSTFDFYGIKAGDYKLVESTTPAGYNTMKDIEFTIT
STIDSTGALTDMTSTSATATFETDVNRGYINLKVVNKQGALLPNTGGIGTT
;
_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 
2 'FORMIC ACID'  FMT 
3 'ACETIC ACID'  ACY 
4 1,2-ETHANEDIOL EDO 
5 'ACETATE ION'  ACT 
6 'SODIUM ION'   NA  
7 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   GLY n 
1 3   SER n 
1 4   SER n 
1 5   HIS n 
1 6   HIS n 
1 7   HIS n 
1 8   HIS n 
1 9   HIS n 
1 10  HIS n 
1 11  SER n 
1 12  SER n 
1 13  GLY n 
1 14  LEU n 
1 15  VAL n 
1 16  PRO n 
1 17  ARG n 
1 18  ARG n 
1 19  GLY n 
1 20  SER n 
1 21  HIS n 
1 22  MET n 
1 23  SER n 
1 24  ALA n 
1 25  ASP n 
1 26  THR n 
1 27  THR n 
1 28  THR n 
1 29  TYR n 
1 30  THR n 
1 31  ILE n 
1 32  GLN n 
1 33  LEU n 
1 34  THR n 
1 35  GLY n 
1 36  THR n 
1 37  SER n 
1 38  SER n 
1 39  GLY n 
1 40  HIS n 
1 41  VAL n 
1 42  TYR n 
1 43  GLU n 
1 44  LEU n 
1 45  TYR n 
1 46  HIS n 
1 47  ILE n 
1 48  PHE n 
1 49  SER n 
1 50  GLY n 
1 51  ASP n 
1 52  LEU n 
1 53  ASP n 
1 54  ALA n 
1 55  ASN n 
1 56  ASN n 
1 57  VAL n 
1 58  LEU n 
1 59  THR n 
1 60  ASN n 
1 61  ILE n 
1 62  GLU n 
1 63  TRP n 
1 64  GLY n 
1 65  ALA n 
1 66  GLY n 
1 67  VAL n 
1 68  ALA n 
1 69  ILE n 
1 70  GLY n 
1 71  ASP n 
1 72  ARG n 
1 73  ALA n 
1 74  LYS n 
1 75  PHE n 
1 76  GLY n 
1 77  ASP n 
1 78  ALA n 
1 79  SER n 
1 80  GLU n 
1 81  LYS n 
1 82  ALA n 
1 83  ALA n 
1 84  SER n 
1 85  LEU n 
1 86  SER n 
1 87  GLY n 
1 88  LYS n 
1 89  GLN n 
1 90  ASN n 
1 91  ASP n 
1 92  SER n 
1 93  SER n 
1 94  GLU n 
1 95  VAL n 
1 96  LYS n 
1 97  ALA n 
1 98  PHE n 
1 99  ALA n 
1 100 GLN n 
1 101 GLU n 
1 102 LEU n 
1 103 SER n 
1 104 ASN n 
1 105 SER n 
1 106 LEU n 
1 107 SER n 
1 108 ALA n 
1 109 ALA n 
1 110 GLY n 
1 111 ARG n 
1 112 THR n 
1 113 ARG n 
1 114 VAL n 
1 115 ARG n 
1 116 SER n 
1 117 GLU n 
1 118 GLN n 
1 119 GLY n 
1 120 THR n 
1 121 THR n 
1 122 THR n 
1 123 ILE n 
1 124 SER n 
1 125 GLY n 
1 126 LEU n 
1 127 LYS n 
1 128 PRO n 
1 129 GLY n 
1 130 TYR n 
1 131 TYR n 
1 132 LEU n 
1 133 ILE n 
1 134 LYS n 
1 135 ASP n 
1 136 SER n 
1 137 ASN n 
1 138 GLY n 
1 139 SER n 
1 140 LEU n 
1 141 ASP n 
1 142 ASN n 
1 143 VAL n 
1 144 LYS n 
1 145 GLY n 
1 146 GLN n 
1 147 ALA n 
1 148 TYR n 
1 149 THR n 
1 150 SER n 
1 151 ILE n 
1 152 MET n 
1 153 LEU n 
1 154 GLN n 
1 155 VAL n 
1 156 ALA n 
1 157 LYS n 
1 158 ASP n 
1 159 THR n 
1 160 THR n 
1 161 ILE n 
1 162 ALA n 
1 163 ILE n 
1 164 LYS n 
1 165 SER n 
1 166 ASP n 
1 167 VAL n 
1 168 PRO n 
1 169 THR n 
1 170 LEU n 
1 171 THR n 
1 172 LYS n 
1 173 GLN n 
1 174 VAL n 
1 175 LYS n 
1 176 ALA n 
1 177 SER n 
1 178 ASN n 
1 179 SER n 
1 180 GLU n 
1 181 ASN n 
1 182 TYR n 
1 183 ILE n 
1 184 SER n 
1 185 ALA n 
1 186 THR n 
1 187 ASP n 
1 188 TYR n 
1 189 ALA n 
1 190 ILE n 
1 191 TRP n 
1 192 ASP n 
1 193 THR n 
1 194 VAL n 
1 195 PRO n 
1 196 PHE n 
1 197 GLN n 
1 198 ILE n 
1 199 THR n 
1 200 VAL n 
1 201 THR n 
1 202 LEU n 
1 203 PRO n 
1 204 SER n 
1 205 ASN n 
1 206 TYR n 
1 207 GLY n 
1 208 ASP n 
1 209 PHE n 
1 210 SER n 
1 211 LYS n 
1 212 TYR n 
1 213 HIS n 
1 214 PHE n 
1 215 SER n 
1 216 VAL n 
1 217 LYS n 
1 218 ASP n 
1 219 SER n 
1 220 MET n 
1 221 THR n 
1 222 SER n 
1 223 GLY n 
1 224 MET n 
1 225 ILE n 
1 226 ASN n 
1 227 ASN n 
1 228 GLY n 
1 229 ASP n 
1 230 ILE n 
1 231 GLN n 
1 232 VAL n 
1 233 TYR n 
1 234 LEU n 
1 235 GLN n 
1 236 GLN n 
1 237 GLY n 
1 238 GLY n 
1 239 SER n 
1 240 GLU n 
1 241 VAL n 
1 242 ALA n 
1 243 ILE n 
1 244 THR n 
1 245 ASP n 
1 246 SER n 
1 247 PHE n 
1 248 SER n 
1 249 ILE n 
1 250 THR n 
1 251 THR n 
1 252 ASN n 
1 253 ASN n 
1 254 GLY n 
1 255 LEU n 
1 256 THR n 
1 257 VAL n 
1 258 SER n 
1 259 ILE n 
1 260 ALA n 
1 261 ASP n 
1 262 LEU n 
1 263 LYS n 
1 264 THR n 
1 265 LEU n 
1 266 PRO n 
1 267 ASN n 
1 268 VAL n 
1 269 ASN n 
1 270 GLU n 
1 271 ASN n 
1 272 SER n 
1 273 LYS n 
1 274 ILE n 
1 275 VAL n 
1 276 ILE n 
1 277 ARG n 
1 278 TYR n 
1 279 THR n 
1 280 ALA n 
1 281 ARG n 
1 282 LEU n 
1 283 LYS n 
1 284 ASP n 
1 285 SER n 
1 286 ALA n 
1 287 THR n 
1 288 LEU n 
1 289 GLY n 
1 290 THR n 
1 291 THR n 
1 292 GLY n 
1 293 ASN n 
1 294 SER n 
1 295 ASN n 
1 296 THR n 
1 297 ALA n 
1 298 SER n 
1 299 LEU n 
1 300 THR n 
1 301 TYR n 
1 302 SER n 
1 303 ASN n 
1 304 ASN n 
1 305 PRO n 
1 306 ASN n 
1 307 ASN n 
1 308 ASN n 
1 309 ALA n 
1 310 SER n 
1 311 THR n 
1 312 THR n 
1 313 ALA n 
1 314 GLN n 
1 315 THR n 
1 316 LEU n 
1 317 ASP n 
1 318 SER n 
1 319 ARG n 
1 320 ALA n 
1 321 THR n 
1 322 VAL n 
1 323 TYR n 
1 324 THR n 
1 325 TYR n 
1 326 ARG n 
1 327 LEU n 
1 328 ARG n 
1 329 LEU n 
1 330 THR n 
1 331 LYS n 
1 332 VAL n 
1 333 ASN n 
1 334 GLU n 
1 335 ARG n 
1 336 GLN n 
1 337 GLU n 
1 338 ARG n 
1 339 VAL n 
1 340 ALA n 
1 341 GLY n 
1 342 ALA n 
1 343 GLY n 
1 344 PHE n 
1 345 THR n 
1 346 LEU n 
1 347 TYR n 
1 348 LYS n 
1 349 LYS n 
1 350 ILE n 
1 351 ASN n 
1 352 ASN n 
1 353 GLN n 
1 354 TYR n 
1 355 SER n 
1 356 GLU n 
1 357 VAL n 
1 358 ARG n 
1 359 LYS n 
1 360 ILE n 
1 361 GLU n 
1 362 ALA n 
1 363 SER n 
1 364 SER n 
1 365 SER n 
1 366 SER n 
1 367 THR n 
1 368 PHE n 
1 369 ASP n 
1 370 PHE n 
1 371 TYR n 
1 372 GLY n 
1 373 ILE n 
1 374 LYS n 
1 375 ALA n 
1 376 GLY n 
1 377 ASP n 
1 378 TYR n 
1 379 LYS n 
1 380 LEU n 
1 381 VAL n 
1 382 GLU n 
1 383 SER n 
1 384 THR n 
1 385 THR n 
1 386 PRO n 
1 387 ALA n 
1 388 GLY n 
1 389 TYR n 
1 390 ASN n 
1 391 THR n 
1 392 MET n 
1 393 LYS n 
1 394 ASP n 
1 395 ILE n 
1 396 GLU n 
1 397 PHE n 
1 398 THR n 
1 399 ILE n 
1 400 THR n 
1 401 SER n 
1 402 THR n 
1 403 ILE n 
1 404 ASP n 
1 405 SER n 
1 406 THR n 
1 407 GLY n 
1 408 ALA n 
1 409 LEU n 
1 410 THR n 
1 411 ASP n 
1 412 MET n 
1 413 THR n 
1 414 SER n 
1 415 THR n 
1 416 SER n 
1 417 ALA n 
1 418 THR n 
1 419 ALA n 
1 420 THR n 
1 421 PHE n 
1 422 GLU n 
1 423 THR n 
1 424 ASP n 
1 425 VAL n 
1 426 ASN n 
1 427 ARG n 
1 428 GLY n 
1 429 TYR n 
1 430 ILE n 
1 431 ASN n 
1 432 LEU n 
1 433 LYS n 
1 434 VAL n 
1 435 VAL n 
1 436 ASN n 
1 437 LYS n 
1 438 GLN n 
1 439 GLY n 
1 440 ALA n 
1 441 LEU n 
1 442 LEU n 
1 443 PRO n 
1 444 ASN n 
1 445 THR n 
1 446 GLY n 
1 447 GLY n 
1 448 ILE n 
1 449 GLY n 
1 450 THR n 
1 451 THR 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                   451 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 SSA_1633 
_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      'Streptococcus sanguinis SK36' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     388919 
_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 BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_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_
_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 
ACT non-polymer         . 'ACETATE ION'   ?                 'C2 H3 O2 -1'    59.044  
ACY non-polymer         . 'ACETIC ACID'   ?                 'C2 H4 O2'       60.052  
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 
EDO non-polymer         . 1,2-ETHANEDIOL  'ETHYLENE GLYCOL' 'C2 H6 O2'       62.068  
FMT non-polymer         . 'FORMIC ACID'   ?                 'C H2 O2'        46.025  
GLN 'L-peptide linking' y GLUTAMINE       ?                 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ?                 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE         ?                 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE       ?                 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER           ?                 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE      ?                 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE         ?                 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE          ?                 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE      ?                 'C5 H11 N O2 S'  149.211 
NA  non-polymer         . 'SODIUM ION'    ?                 'Na 1'           22.990  
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_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   3   ?   ?   ?   A . n 
A 1 2   GLY 2   4   ?   ?   ?   A . n 
A 1 3   SER 3   5   ?   ?   ?   A . n 
A 1 4   SER 4   6   ?   ?   ?   A . n 
A 1 5   HIS 5   7   ?   ?   ?   A . n 
A 1 6   HIS 6   8   ?   ?   ?   A . n 
A 1 7   HIS 7   9   ?   ?   ?   A . n 
A 1 8   HIS 8   10  ?   ?   ?   A . n 
A 1 9   HIS 9   11  ?   ?   ?   A . n 
A 1 10  HIS 10  12  ?   ?   ?   A . n 
A 1 11  SER 11  13  ?   ?   ?   A . n 
A 1 12  SER 12  14  ?   ?   ?   A . n 
A 1 13  GLY 13  15  ?   ?   ?   A . n 
A 1 14  LEU 14  16  ?   ?   ?   A . n 
A 1 15  VAL 15  17  ?   ?   ?   A . n 
A 1 16  PRO 16  18  ?   ?   ?   A . n 
A 1 17  ARG 17  19  ?   ?   ?   A . n 
A 1 18  ARG 18  20  ?   ?   ?   A . n 
A 1 19  GLY 19  21  ?   ?   ?   A . n 
A 1 20  SER 20  22  ?   ?   ?   A . n 
A 1 21  HIS 21  23  ?   ?   ?   A . n 
A 1 22  MET 22  24  ?   ?   ?   A . n 
A 1 23  SER 23  25  ?   ?   ?   A . n 
A 1 24  ALA 24  26  ?   ?   ?   A . n 
A 1 25  ASP 25  27  ?   ?   ?   A . n 
A 1 26  THR 26  28  28  THR THR A . n 
A 1 27  THR 27  29  29  THR THR A . n 
A 1 28  THR 28  30  30  THR THR A . n 
A 1 29  TYR 29  31  31  TYR TYR A . n 
A 1 30  THR 30  32  32  THR THR A . n 
A 1 31  ILE 31  33  33  ILE ILE A . n 
A 1 32  GLN 32  34  34  GLN GLN A . n 
A 1 33  LEU 33  35  35  LEU LEU A . n 
A 1 34  THR 34  36  36  THR THR A . n 
A 1 35  GLY 35  37  37  GLY GLY A . n 
A 1 36  THR 36  38  38  THR THR A . n 
A 1 37  SER 37  39  39  SER SER A . n 
A 1 38  SER 38  40  40  SER SER A . n 
A 1 39  GLY 39  41  41  GLY GLY A . n 
A 1 40  HIS 40  42  42  HIS HIS A . n 
A 1 41  VAL 41  43  43  VAL VAL A . n 
A 1 42  TYR 42  44  44  TYR TYR A . n 
A 1 43  GLU 43  45  45  GLU GLU A . n 
A 1 44  LEU 44  46  46  LEU LEU A . n 
A 1 45  TYR 45  47  47  TYR TYR A . n 
A 1 46  HIS 46  48  48  HIS HIS A . n 
A 1 47  ILE 47  49  49  ILE ILE A . n 
A 1 48  PHE 48  50  50  PHE PHE A . n 
A 1 49  SER 49  51  51  SER SER A . n 
A 1 50  GLY 50  52  52  GLY GLY A . n 
A 1 51  ASP 51  53  53  ASP ASP A . n 
A 1 52  LEU 52  54  54  LEU LEU A . n 
A 1 53  ASP 53  55  55  ASP ASP A . n 
A 1 54  ALA 54  56  56  ALA ALA A . n 
A 1 55  ASN 55  57  57  ASN ASN A . n 
A 1 56  ASN 56  58  58  ASN ASN A . n 
A 1 57  VAL 57  59  59  VAL VAL A . n 
A 1 58  LEU 58  60  60  LEU LEU A . n 
A 1 59  THR 59  61  61  THR THR A . n 
A 1 60  ASN 60  62  62  ASN ASN A . n 
A 1 61  ILE 61  63  63  ILE ILE A . n 
A 1 62  GLU 62  64  64  GLU GLU A . n 
A 1 63  TRP 63  65  65  TRP TRP A . n 
A 1 64  GLY 64  66  66  GLY GLY A . n 
A 1 65  ALA 65  67  67  ALA ALA A . n 
A 1 66  GLY 66  68  68  GLY GLY A . n 
A 1 67  VAL 67  69  69  VAL VAL A . n 
A 1 68  ALA 68  70  70  ALA ALA A . n 
A 1 69  ILE 69  71  71  ILE ILE A . n 
A 1 70  GLY 70  72  72  GLY GLY A . n 
A 1 71  ASP 71  73  73  ASP ASP A . n 
A 1 72  ARG 72  74  74  ARG ARG A . n 
A 1 73  ALA 73  75  75  ALA ALA A . n 
A 1 74  LYS 74  76  76  LYS LYS A . n 
A 1 75  PHE 75  77  77  PHE PHE A . n 
A 1 76  GLY 76  78  78  GLY GLY A . n 
A 1 77  ASP 77  79  79  ASP ASP A . n 
A 1 78  ALA 78  80  80  ALA ALA A . n 
A 1 79  SER 79  81  81  SER SER A . n 
A 1 80  GLU 80  82  82  GLU GLU A . n 
A 1 81  LYS 81  83  83  LYS LYS A . n 
A 1 82  ALA 82  84  84  ALA ALA A . n 
A 1 83  ALA 83  85  85  ALA ALA A . n 
A 1 84  SER 84  86  86  SER SER A . n 
A 1 85  LEU 85  87  87  LEU LEU A . n 
A 1 86  SER 86  88  88  SER SER A . n 
A 1 87  GLY 87  89  89  GLY GLY A . n 
A 1 88  LYS 88  90  90  LYS LYS A . n 
A 1 89  GLN 89  91  91  GLN GLN A . n 
A 1 90  ASN 90  92  92  ASN ASN A . n 
A 1 91  ASP 91  93  93  ASP ASP A . n 
A 1 92  SER 92  94  94  SER SER A . n 
A 1 93  SER 93  95  95  SER SER A . n 
A 1 94  GLU 94  96  96  GLU GLU A . n 
A 1 95  VAL 95  97  97  VAL VAL A . n 
A 1 96  LYS 96  98  98  LYS LYS A . n 
A 1 97  ALA 97  99  99  ALA ALA A . n 
A 1 98  PHE 98  100 100 PHE PHE A . n 
A 1 99  ALA 99  101 101 ALA ALA A . n 
A 1 100 GLN 100 102 102 GLN GLN A . n 
A 1 101 GLU 101 103 103 GLU GLU A . n 
A 1 102 LEU 102 104 104 LEU LEU A . n 
A 1 103 SER 103 105 105 SER SER A . n 
A 1 104 ASN 104 106 106 ASN ASN A . n 
A 1 105 SER 105 107 107 SER SER A . n 
A 1 106 LEU 106 108 108 LEU LEU A . n 
A 1 107 SER 107 109 109 SER SER A . n 
A 1 108 ALA 108 110 110 ALA ALA A . n 
A 1 109 ALA 109 111 111 ALA ALA A . n 
A 1 110 GLY 110 112 112 GLY GLY A . n 
A 1 111 ARG 111 113 113 ARG ARG A . n 
A 1 112 THR 112 114 114 THR THR A . n 
A 1 113 ARG 113 115 115 ARG ARG A . n 
A 1 114 VAL 114 116 116 VAL VAL A . n 
A 1 115 ARG 115 117 117 ARG ARG A . n 
A 1 116 SER 116 118 118 SER SER A . n 
A 1 117 GLU 117 119 119 GLU GLU A . n 
A 1 118 GLN 118 120 120 GLN GLN A . n 
A 1 119 GLY 119 121 121 GLY GLY A . n 
A 1 120 THR 120 122 122 THR THR A . n 
A 1 121 THR 121 123 123 THR THR A . n 
A 1 122 THR 122 124 124 THR THR A . n 
A 1 123 ILE 123 125 125 ILE ILE A . n 
A 1 124 SER 124 126 126 SER SER A . n 
A 1 125 GLY 125 127 127 GLY GLY A . n 
A 1 126 LEU 126 128 128 LEU LEU A . n 
A 1 127 LYS 127 129 129 LYS LYS A . n 
A 1 128 PRO 128 130 130 PRO PRO A . n 
A 1 129 GLY 129 131 131 GLY GLY A . n 
A 1 130 TYR 130 132 132 TYR TYR A . n 
A 1 131 TYR 131 133 133 TYR TYR A . n 
A 1 132 LEU 132 134 134 LEU LEU A . n 
A 1 133 ILE 133 135 135 ILE ILE A . n 
A 1 134 LYS 134 136 136 LYS LYS A . n 
A 1 135 ASP 135 137 137 ASP ASP A . n 
A 1 136 SER 136 138 138 SER SER A . n 
A 1 137 ASN 137 139 139 ASN ASN A . n 
A 1 138 GLY 138 140 140 GLY GLY A . n 
A 1 139 SER 139 141 141 SER SER A . n 
A 1 140 LEU 140 142 142 LEU LEU A . n 
A 1 141 ASP 141 143 143 ASP ASP A . n 
A 1 142 ASN 142 144 144 ASN ASN A . n 
A 1 143 VAL 143 145 145 VAL VAL A . n 
A 1 144 LYS 144 146 146 LYS LYS A . n 
A 1 145 GLY 145 147 147 GLY GLY A . n 
A 1 146 GLN 146 148 148 GLN GLN A . n 
A 1 147 ALA 147 149 149 ALA ALA A . n 
A 1 148 TYR 148 150 150 TYR TYR A . n 
A 1 149 THR 149 151 151 THR THR A . n 
A 1 150 SER 150 152 152 SER SER A . n 
A 1 151 ILE 151 153 153 ILE ILE A . n 
A 1 152 MET 152 154 154 MET MET A . n 
A 1 153 LEU 153 155 155 LEU LEU A . n 
A 1 154 GLN 154 156 156 GLN GLN A . n 
A 1 155 VAL 155 157 157 VAL VAL A . n 
A 1 156 ALA 156 158 158 ALA ALA A . n 
A 1 157 LYS 157 159 159 LYS LYS A . n 
A 1 158 ASP 158 160 160 ASP ASP A . n 
A 1 159 THR 159 161 161 THR THR A . n 
A 1 160 THR 160 162 162 THR THR A . n 
A 1 161 ILE 161 163 163 ILE ILE A . n 
A 1 162 ALA 162 164 164 ALA ALA A . n 
A 1 163 ILE 163 165 165 ILE ILE A . n 
A 1 164 LYS 164 166 166 LYS LYS A . n 
A 1 165 SER 165 167 167 SER SER A . n 
A 1 166 ASP 166 168 168 ASP ASP A . n 
A 1 167 VAL 167 169 169 VAL VAL A . n 
A 1 168 PRO 168 170 170 PRO PRO A . n 
A 1 169 THR 169 171 171 THR THR A . n 
A 1 170 LEU 170 172 172 LEU LEU A . n 
A 1 171 THR 171 173 173 THR THR A . n 
A 1 172 LYS 172 174 174 LYS LYS A . n 
A 1 173 GLN 173 175 175 GLN GLN A . n 
A 1 174 VAL 174 176 176 VAL VAL A . n 
A 1 175 LYS 175 177 177 LYS LYS A . n 
A 1 176 ALA 176 178 178 ALA ALA A . n 
A 1 177 SER 177 179 179 SER SER A . n 
A 1 178 ASN 178 180 180 ASN ASN A . n 
A 1 179 SER 179 181 181 SER SER A . n 
A 1 180 GLU 180 182 182 GLU GLU A . n 
A 1 181 ASN 181 183 183 ASN ASN A . n 
A 1 182 TYR 182 184 184 TYR TYR A . n 
A 1 183 ILE 183 185 185 ILE ILE A . n 
A 1 184 SER 184 186 186 SER SER A . n 
A 1 185 ALA 185 187 187 ALA ALA A . n 
A 1 186 THR 186 188 188 THR THR A . n 
A 1 187 ASP 187 189 189 ASP ASP A . n 
A 1 188 TYR 188 190 190 TYR TYR A . n 
A 1 189 ALA 189 191 191 ALA ALA A . n 
A 1 190 ILE 190 192 192 ILE ILE A . n 
A 1 191 TRP 191 193 193 TRP TRP A . n 
A 1 192 ASP 192 194 194 ASP ASP A . n 
A 1 193 THR 193 195 195 THR THR A . n 
A 1 194 VAL 194 196 196 VAL VAL A . n 
A 1 195 PRO 195 197 197 PRO PRO A . n 
A 1 196 PHE 196 198 198 PHE PHE A . n 
A 1 197 GLN 197 199 199 GLN GLN A . n 
A 1 198 ILE 198 200 200 ILE ILE A . n 
A 1 199 THR 199 201 201 THR THR A . n 
A 1 200 VAL 200 202 202 VAL VAL A . n 
A 1 201 THR 201 203 203 THR THR A . n 
A 1 202 LEU 202 204 204 LEU LEU A . n 
A 1 203 PRO 203 205 205 PRO PRO A . n 
A 1 204 SER 204 206 206 SER SER A . n 
A 1 205 ASN 205 207 207 ASN ASN A . n 
A 1 206 TYR 206 208 208 TYR TYR A . n 
A 1 207 GLY 207 209 209 GLY GLY A . n 
A 1 208 ASP 208 210 210 ASP ASP A . n 
A 1 209 PHE 209 211 211 PHE PHE A . n 
A 1 210 SER 210 212 212 SER SER A . n 
A 1 211 LYS 211 213 213 LYS LYS A . n 
A 1 212 TYR 212 214 214 TYR TYR A . n 
A 1 213 HIS 213 215 215 HIS HIS A . n 
A 1 214 PHE 214 216 216 PHE PHE A . n 
A 1 215 SER 215 217 217 SER SER A . n 
A 1 216 VAL 216 218 218 VAL VAL A . n 
A 1 217 LYS 217 219 219 LYS LYS A . n 
A 1 218 ASP 218 220 220 ASP ASP A . n 
A 1 219 SER 219 221 221 SER SER A . n 
A 1 220 MET 220 222 222 MET MET A . n 
A 1 221 THR 221 223 223 THR THR A . n 
A 1 222 SER 222 224 224 SER SER A . n 
A 1 223 GLY 223 225 225 GLY GLY A . n 
A 1 224 MET 224 226 226 MET MET A . n 
A 1 225 ILE 225 227 227 ILE ILE A . n 
A 1 226 ASN 226 228 228 ASN ASN A . n 
A 1 227 ASN 227 229 229 ASN ASN A . n 
A 1 228 GLY 228 230 230 GLY GLY A . n 
A 1 229 ASP 229 231 231 ASP ASP A . n 
A 1 230 ILE 230 232 232 ILE ILE A . n 
A 1 231 GLN 231 233 233 GLN GLN A . n 
A 1 232 VAL 232 234 234 VAL VAL A . n 
A 1 233 TYR 233 235 235 TYR TYR A . n 
A 1 234 LEU 234 236 236 LEU LEU A . n 
A 1 235 GLN 235 237 237 GLN GLN A . n 
A 1 236 GLN 236 238 238 GLN GLN A . n 
A 1 237 GLY 237 239 239 GLY GLY A . n 
A 1 238 GLY 238 240 240 GLY GLY A . n 
A 1 239 SER 239 241 241 SER SER A . n 
A 1 240 GLU 240 242 242 GLU GLU A . n 
A 1 241 VAL 241 243 243 VAL VAL A . n 
A 1 242 ALA 242 244 244 ALA ALA A . n 
A 1 243 ILE 243 245 245 ILE ILE A . n 
A 1 244 THR 244 246 246 THR THR A . n 
A 1 245 ASP 245 247 247 ASP ASP A . n 
A 1 246 SER 246 248 248 SER SER A . n 
A 1 247 PHE 247 249 249 PHE PHE A . n 
A 1 248 SER 248 250 250 SER SER A . n 
A 1 249 ILE 249 251 251 ILE ILE A . n 
A 1 250 THR 250 252 252 THR THR A . n 
A 1 251 THR 251 253 253 THR THR A . n 
A 1 252 ASN 252 254 254 ASN ASN A . n 
A 1 253 ASN 253 255 255 ASN ASN A . n 
A 1 254 GLY 254 256 256 GLY GLY A . n 
A 1 255 LEU 255 257 257 LEU LEU A . n 
A 1 256 THR 256 258 258 THR THR A . n 
A 1 257 VAL 257 259 259 VAL VAL A . n 
A 1 258 SER 258 260 260 SER SER A . n 
A 1 259 ILE 259 261 261 ILE ILE A . n 
A 1 260 ALA 260 262 262 ALA ALA A . n 
A 1 261 ASP 261 263 263 ASP ASP A . n 
A 1 262 LEU 262 264 264 LEU LEU A . n 
A 1 263 LYS 263 265 265 LYS LYS A . n 
A 1 264 THR 264 266 266 THR THR A . n 
A 1 265 LEU 265 267 267 LEU LEU A . n 
A 1 266 PRO 266 268 268 PRO PRO A . n 
A 1 267 ASN 267 269 269 ASN ASN A . n 
A 1 268 VAL 268 270 270 VAL VAL A . n 
A 1 269 ASN 269 271 271 ASN ASN A . n 
A 1 270 GLU 270 272 272 GLU GLU A . n 
A 1 271 ASN 271 273 273 ASN ASN A . n 
A 1 272 SER 272 274 274 SER SER A . n 
A 1 273 LYS 273 275 275 LYS LYS A . n 
A 1 274 ILE 274 276 276 ILE ILE A . n 
A 1 275 VAL 275 277 277 VAL VAL A . n 
A 1 276 ILE 276 278 278 ILE ILE A . n 
A 1 277 ARG 277 279 279 ARG ARG A . n 
A 1 278 TYR 278 280 280 TYR TYR A . n 
A 1 279 THR 279 281 281 THR THR A . n 
A 1 280 ALA 280 282 282 ALA ALA A . n 
A 1 281 ARG 281 283 283 ARG ARG A . n 
A 1 282 LEU 282 284 284 LEU LEU A . n 
A 1 283 LYS 283 285 285 LYS LYS A . n 
A 1 284 ASP 284 286 286 ASP ASP A . n 
A 1 285 SER 285 287 287 SER SER A . n 
A 1 286 ALA 286 288 288 ALA ALA A . n 
A 1 287 THR 287 289 289 THR THR A . n 
A 1 288 LEU 288 290 290 LEU LEU A . n 
A 1 289 GLY 289 291 291 GLY GLY A . n 
A 1 290 THR 290 292 292 THR THR A . n 
A 1 291 THR 291 293 293 THR THR A . n 
A 1 292 GLY 292 294 294 GLY GLY A . n 
A 1 293 ASN 293 295 295 ASN ASN A . n 
A 1 294 SER 294 296 296 SER SER A . n 
A 1 295 ASN 295 297 297 ASN ASN A . n 
A 1 296 THR 296 298 298 THR THR A . n 
A 1 297 ALA 297 299 299 ALA ALA A . n 
A 1 298 SER 298 300 300 SER SER A . n 
A 1 299 LEU 299 301 301 LEU LEU A . n 
A 1 300 THR 300 302 302 THR THR A . n 
A 1 301 TYR 301 303 303 TYR TYR A . n 
A 1 302 SER 302 304 304 SER SER A . n 
A 1 303 ASN 303 305 305 ASN ASN A . n 
A 1 304 ASN 304 306 306 ASN ASN A . n 
A 1 305 PRO 305 307 307 PRO PRO A . n 
A 1 306 ASN 306 308 308 ASN ASN A . n 
A 1 307 ASN 307 309 309 ASN ASN A . n 
A 1 308 ASN 308 310 310 ASN ASN A . n 
A 1 309 ALA 309 311 311 ALA ALA A . n 
A 1 310 SER 310 312 312 SER SER A . n 
A 1 311 THR 311 313 313 THR THR A . n 
A 1 312 THR 312 314 314 THR THR A . n 
A 1 313 ALA 313 315 315 ALA ALA A . n 
A 1 314 GLN 314 316 316 GLN GLN A . n 
A 1 315 THR 315 317 317 THR THR A . n 
A 1 316 LEU 316 318 318 LEU LEU A . n 
A 1 317 ASP 317 319 319 ASP ASP A . n 
A 1 318 SER 318 320 320 SER SER A . n 
A 1 319 ARG 319 321 321 ARG ARG A . n 
A 1 320 ALA 320 322 322 ALA ALA A . n 
A 1 321 THR 321 323 323 THR THR A . n 
A 1 322 VAL 322 324 324 VAL VAL A . n 
A 1 323 TYR 323 325 325 TYR TYR A . n 
A 1 324 THR 324 326 326 THR THR A . n 
A 1 325 TYR 325 327 327 TYR TYR A . n 
A 1 326 ARG 326 328 328 ARG ARG A . n 
A 1 327 LEU 327 329 329 LEU LEU A . n 
A 1 328 ARG 328 330 330 ARG ARG A . n 
A 1 329 LEU 329 331 331 LEU LEU A . n 
A 1 330 THR 330 332 332 THR THR A . n 
A 1 331 LYS 331 333 333 LYS LYS A . n 
A 1 332 VAL 332 334 334 VAL VAL A . n 
A 1 333 ASN 333 335 335 ASN ASN A . n 
A 1 334 GLU 334 336 336 GLU GLU A . n 
A 1 335 ARG 335 337 337 ARG ARG A . n 
A 1 336 GLN 336 338 338 GLN GLN A . n 
A 1 337 GLU 337 339 339 GLU GLU A . n 
A 1 338 ARG 338 340 340 ARG ARG A . n 
A 1 339 VAL 339 341 341 VAL VAL A . n 
A 1 340 ALA 340 342 342 ALA ALA A . n 
A 1 341 GLY 341 343 343 GLY GLY A . n 
A 1 342 ALA 342 344 344 ALA ALA A . n 
A 1 343 GLY 343 345 345 GLY GLY A . n 
A 1 344 PHE 344 346 346 PHE PHE A . n 
A 1 345 THR 345 347 347 THR THR A . n 
A 1 346 LEU 346 348 348 LEU LEU A . n 
A 1 347 TYR 347 349 349 TYR TYR A . n 
A 1 348 LYS 348 350 350 LYS LYS A . n 
A 1 349 LYS 349 351 351 LYS LYS A . n 
A 1 350 ILE 350 352 352 ILE ILE A . n 
A 1 351 ASN 351 353 353 ASN ASN A . n 
A 1 352 ASN 352 354 354 ASN ASN A . n 
A 1 353 GLN 353 355 355 GLN GLN A . n 
A 1 354 TYR 354 356 356 TYR TYR A . n 
A 1 355 SER 355 357 357 SER SER A . n 
A 1 356 GLU 356 358 358 GLU GLU A . n 
A 1 357 VAL 357 359 359 VAL VAL A . n 
A 1 358 ARG 358 360 360 ARG ARG A . n 
A 1 359 LYS 359 361 361 LYS LYS A . n 
A 1 360 ILE 360 362 362 ILE ILE A . n 
A 1 361 GLU 361 363 363 GLU GLU A . n 
A 1 362 ALA 362 364 364 ALA ALA A . n 
A 1 363 SER 363 365 365 SER SER A . n 
A 1 364 SER 364 366 366 SER SER A . n 
A 1 365 SER 365 367 367 SER SER A . n 
A 1 366 SER 366 368 368 SER SER A . n 
A 1 367 THR 367 369 369 THR THR A . n 
A 1 368 PHE 368 370 370 PHE PHE A . n 
A 1 369 ASP 369 371 371 ASP ASP A . n 
A 1 370 PHE 370 372 372 PHE PHE A . n 
A 1 371 TYR 371 373 373 TYR TYR A . n 
A 1 372 GLY 372 374 374 GLY GLY A . n 
A 1 373 ILE 373 375 375 ILE ILE A . n 
A 1 374 LYS 374 376 376 LYS LYS A . n 
A 1 375 ALA 375 377 377 ALA ALA A . n 
A 1 376 GLY 376 378 378 GLY GLY A . n 
A 1 377 ASP 377 379 379 ASP ASP A . n 
A 1 378 TYR 378 380 380 TYR TYR A . n 
A 1 379 LYS 379 381 381 LYS LYS A . n 
A 1 380 LEU 380 382 382 LEU LEU A . n 
A 1 381 VAL 381 383 383 VAL VAL A . n 
A 1 382 GLU 382 384 384 GLU GLU A . n 
A 1 383 SER 383 385 385 SER SER A . n 
A 1 384 THR 384 386 386 THR THR A . n 
A 1 385 THR 385 387 387 THR THR A . n 
A 1 386 PRO 386 388 388 PRO PRO A . n 
A 1 387 ALA 387 389 389 ALA ALA A . n 
A 1 388 GLY 388 390 390 GLY GLY A . n 
A 1 389 TYR 389 391 391 TYR TYR A . n 
A 1 390 ASN 390 392 392 ASN ASN A . n 
A 1 391 THR 391 393 393 THR THR A . n 
A 1 392 MET 392 394 394 MET MET A . n 
A 1 393 LYS 393 395 395 LYS LYS A . n 
A 1 394 ASP 394 396 396 ASP ASP A . n 
A 1 395 ILE 395 397 397 ILE ILE A . n 
A 1 396 GLU 396 398 398 GLU GLU A . n 
A 1 397 PHE 397 399 399 PHE PHE A . n 
A 1 398 THR 398 400 400 THR THR A . n 
A 1 399 ILE 399 401 401 ILE ILE A . n 
A 1 400 THR 400 402 402 THR THR A . n 
A 1 401 SER 401 403 403 SER SER A . n 
A 1 402 THR 402 404 404 THR THR A . n 
A 1 403 ILE 403 405 405 ILE ILE A . n 
A 1 404 ASP 404 406 406 ASP ASP A . n 
A 1 405 SER 405 407 407 SER SER A . n 
A 1 406 THR 406 408 408 THR THR A . n 
A 1 407 GLY 407 409 409 GLY GLY A . n 
A 1 408 ALA 408 410 410 ALA ALA A . n 
A 1 409 LEU 409 411 411 LEU LEU A . n 
A 1 410 THR 410 412 412 THR THR A . n 
A 1 411 ASP 411 413 413 ASP ASP A . n 
A 1 412 MET 412 414 414 MET MET A . n 
A 1 413 THR 413 415 415 THR THR A . n 
A 1 414 SER 414 416 416 SER SER A . n 
A 1 415 THR 415 417 417 THR THR A . n 
A 1 416 SER 416 418 418 SER SER A . n 
A 1 417 ALA 417 419 419 ALA ALA A . n 
A 1 418 THR 418 420 420 THR THR A . n 
A 1 419 ALA 419 421 421 ALA ALA A . n 
A 1 420 THR 420 422 422 THR THR A . n 
A 1 421 PHE 421 423 423 PHE PHE A . n 
A 1 422 GLU 422 424 424 GLU GLU A . n 
A 1 423 THR 423 425 425 THR THR A . n 
A 1 424 ASP 424 426 426 ASP ASP A . n 
A 1 425 VAL 425 427 427 VAL VAL A . n 
A 1 426 ASN 426 428 428 ASN ASN A . n 
A 1 427 ARG 427 429 429 ARG ARG A . n 
A 1 428 GLY 428 430 430 GLY GLY A . n 
A 1 429 TYR 429 431 431 TYR TYR A . n 
A 1 430 ILE 430 432 432 ILE ILE A . n 
A 1 431 ASN 431 433 433 ASN ASN A . n 
A 1 432 LEU 432 434 434 LEU LEU A . n 
A 1 433 LYS 433 435 435 LYS LYS A . n 
A 1 434 VAL 434 436 436 VAL VAL A . n 
A 1 435 VAL 435 437 437 VAL VAL A . n 
A 1 436 ASN 436 438 438 ASN ASN A . n 
A 1 437 LYS 437 439 439 LYS LYS A . n 
A 1 438 GLN 438 440 440 GLN GLN A . n 
A 1 439 GLY 439 441 441 GLY GLY A . n 
A 1 440 ALA 440 442 442 ALA ALA A . n 
A 1 441 LEU 441 443 443 LEU LEU A . n 
A 1 442 LEU 442 444 444 LEU LEU A . n 
A 1 443 PRO 443 445 445 PRO PRO A . n 
A 1 444 ASN 444 446 ?   ?   ?   A . n 
A 1 445 THR 445 447 ?   ?   ?   A . n 
A 1 446 GLY 446 448 ?   ?   ?   A . n 
A 1 447 GLY 447 449 ?   ?   ?   A . n 
A 1 448 ILE 448 450 ?   ?   ?   A . n 
A 1 449 GLY 449 451 ?   ?   ?   A . n 
A 1 450 THR 450 452 ?   ?   ?   A . n 
A 1 451 THR 451 453 ?   ?   ?   A . n 
# 
loop_
_pdbx_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 ACT ? ? ACT ? ? 'SUBJECT OF INVESTIGATION' ? 
2 ACY ? ? ACY ? ? 'SUBJECT OF INVESTIGATION' ? 
3 EDO ? ? EDO ? ? 'SUBJECT OF INVESTIGATION' ? 
4 FMT ? ? FMT ? ? 'SUBJECT OF INVESTIGATION' ? 
5 NA  ? ? NA  ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 FMT 1   801  801  FMT FMT A . 
C 2 FMT 1   802  2501 FMT FMT A . 
D 3 ACY 1   803  2601 ACY ACY A . 
E 4 EDO 1   804  2701 EDO EDO A . 
F 3 ACY 1   805  3401 ACY ACY A . 
G 4 EDO 1   806  3501 EDO EDO A . 
H 4 EDO 1   807  3901 EDO EDO A . 
I 4 EDO 1   808  4301 EDO EDO A . 
J 2 FMT 1   809  4501 FMT FMT A . 
K 5 ACT 1   810  4901 ACT ACT A . 
L 2 FMT 1   811  5001 FMT FMT A . 
M 6 NA  1   812  5201 NA  NA  A . 
N 7 HOH 1   901  488  HOH HOH A . 
N 7 HOH 2   902  449  HOH HOH A . 
N 7 HOH 3   903  36   HOH HOH A . 
N 7 HOH 4   904  485  HOH HOH A . 
N 7 HOH 5   905  448  HOH HOH A . 
N 7 HOH 6   906  141  HOH HOH A . 
N 7 HOH 7   907  462  HOH HOH A . 
N 7 HOH 8   908  57   HOH HOH A . 
N 7 HOH 9   909  121  HOH HOH A . 
N 7 HOH 10  910  215  HOH HOH A . 
N 7 HOH 11  911  229  HOH HOH A . 
N 7 HOH 12  912  102  HOH HOH A . 
N 7 HOH 13  913  307  HOH HOH A . 
N 7 HOH 14  914  418  HOH HOH A . 
N 7 HOH 15  915  458  HOH HOH A . 
N 7 HOH 16  916  81   HOH HOH A . 
N 7 HOH 17  917  239  HOH HOH A . 
N 7 HOH 18  918  486  HOH HOH A . 
N 7 HOH 19  919  445  HOH HOH A . 
N 7 HOH 20  920  206  HOH HOH A . 
N 7 HOH 21  921  63   HOH HOH A . 
N 7 HOH 22  922  75   HOH HOH A . 
N 7 HOH 23  923  31   HOH HOH A . 
N 7 HOH 24  924  34   HOH HOH A . 
N 7 HOH 25  925  108  HOH HOH A . 
N 7 HOH 26  926  178  HOH HOH A . 
N 7 HOH 27  927  358  HOH HOH A . 
N 7 HOH 28  928  69   HOH HOH A . 
N 7 HOH 29  929  74   HOH HOH A . 
N 7 HOH 30  930  131  HOH HOH A . 
N 7 HOH 31  931  469  HOH HOH A . 
N 7 HOH 32  932  125  HOH HOH A . 
N 7 HOH 33  933  140  HOH HOH A . 
N 7 HOH 34  934  129  HOH HOH A . 
N 7 HOH 35  935  37   HOH HOH A . 
N 7 HOH 36  936  92   HOH HOH A . 
N 7 HOH 37  937  19   HOH HOH A . 
N 7 HOH 38  938  481  HOH HOH A . 
N 7 HOH 39  939  54   HOH HOH A . 
N 7 HOH 40  940  113  HOH HOH A . 
N 7 HOH 41  941  245  HOH HOH A . 
N 7 HOH 42  942  68   HOH HOH A . 
N 7 HOH 43  943  14   HOH HOH A . 
N 7 HOH 44  944  158  HOH HOH A . 
N 7 HOH 45  945  91   HOH HOH A . 
N 7 HOH 46  946  167  HOH HOH A . 
N 7 HOH 47  947  487  HOH HOH A . 
N 7 HOH 48  948  450  HOH HOH A . 
N 7 HOH 49  949  106  HOH HOH A . 
N 7 HOH 50  950  130  HOH HOH A . 
N 7 HOH 51  951  484  HOH HOH A . 
N 7 HOH 52  952  66   HOH HOH A . 
N 7 HOH 53  953  336  HOH HOH A . 
N 7 HOH 54  954  149  HOH HOH A . 
N 7 HOH 55  955  55   HOH HOH A . 
N 7 HOH 56  956  96   HOH HOH A . 
N 7 HOH 57  957  43   HOH HOH A . 
N 7 HOH 58  958  111  HOH HOH A . 
N 7 HOH 59  959  3    HOH HOH A . 
N 7 HOH 60  960  95   HOH HOH A . 
N 7 HOH 61  961  123  HOH HOH A . 
N 7 HOH 62  962  35   HOH HOH A . 
N 7 HOH 63  963  2    HOH HOH A . 
N 7 HOH 64  964  48   HOH HOH A . 
N 7 HOH 65  965  397  HOH HOH A . 
N 7 HOH 66  966  8    HOH HOH A . 
N 7 HOH 67  967  38   HOH HOH A . 
N 7 HOH 68  968  4    HOH HOH A . 
N 7 HOH 69  969  172  HOH HOH A . 
N 7 HOH 70  970  170  HOH HOH A . 
N 7 HOH 71  971  137  HOH HOH A . 
N 7 HOH 72  972  184  HOH HOH A . 
N 7 HOH 73  973  118  HOH HOH A . 
N 7 HOH 74  974  180  HOH HOH A . 
N 7 HOH 75  975  136  HOH HOH A . 
N 7 HOH 76  976  444  HOH HOH A . 
N 7 HOH 77  977  1    HOH HOH A . 
N 7 HOH 78  978  122  HOH HOH A . 
N 7 HOH 79  979  478  HOH HOH A . 
N 7 HOH 80  980  104  HOH HOH A . 
N 7 HOH 81  981  405  HOH HOH A . 
N 7 HOH 82  982  153  HOH HOH A . 
N 7 HOH 83  983  472  HOH HOH A . 
N 7 HOH 84  984  27   HOH HOH A . 
N 7 HOH 85  985  379  HOH HOH A . 
N 7 HOH 86  986  103  HOH HOH A . 
N 7 HOH 87  987  446  HOH HOH A . 
N 7 HOH 88  988  228  HOH HOH A . 
N 7 HOH 89  989  10   HOH HOH A . 
N 7 HOH 90  990  316  HOH HOH A . 
N 7 HOH 91  991  53   HOH HOH A . 
N 7 HOH 92  992  452  HOH HOH A . 
N 7 HOH 93  993  225  HOH HOH A . 
N 7 HOH 94  994  93   HOH HOH A . 
N 7 HOH 95  995  114  HOH HOH A . 
N 7 HOH 96  996  475  HOH HOH A . 
N 7 HOH 97  997  124  HOH HOH A . 
N 7 HOH 98  998  322  HOH HOH A . 
N 7 HOH 99  999  127  HOH HOH A . 
N 7 HOH 100 1000 219  HOH HOH A . 
N 7 HOH 101 1001 105  HOH HOH A . 
N 7 HOH 102 1002 473  HOH HOH A . 
N 7 HOH 103 1003 39   HOH HOH A . 
N 7 HOH 104 1004 290  HOH HOH A . 
N 7 HOH 105 1005 280  HOH HOH A . 
N 7 HOH 106 1006 214  HOH HOH A . 
N 7 HOH 107 1007 465  HOH HOH A . 
N 7 HOH 108 1008 142  HOH HOH A . 
N 7 HOH 109 1009 156  HOH HOH A . 
N 7 HOH 110 1010 50   HOH HOH A . 
N 7 HOH 111 1011 70   HOH HOH A . 
N 7 HOH 112 1012 191  HOH HOH A . 
N 7 HOH 113 1013 210  HOH HOH A . 
N 7 HOH 114 1014 320  HOH HOH A . 
N 7 HOH 115 1015 51   HOH HOH A . 
N 7 HOH 116 1016 5    HOH HOH A . 
N 7 HOH 117 1017 459  HOH HOH A . 
N 7 HOH 118 1018 87   HOH HOH A . 
N 7 HOH 119 1019 30   HOH HOH A . 
N 7 HOH 120 1020 471  HOH HOH A . 
N 7 HOH 121 1021 200  HOH HOH A . 
N 7 HOH 122 1022 116  HOH HOH A . 
N 7 HOH 123 1023 89   HOH HOH A . 
N 7 HOH 124 1024 451  HOH HOH A . 
N 7 HOH 125 1025 464  HOH HOH A . 
N 7 HOH 126 1026 44   HOH HOH A . 
N 7 HOH 127 1027 62   HOH HOH A . 
N 7 HOH 128 1028 474  HOH HOH A . 
N 7 HOH 129 1029 457  HOH HOH A . 
N 7 HOH 130 1030 187  HOH HOH A . 
N 7 HOH 131 1031 483  HOH HOH A . 
N 7 HOH 132 1032 477  HOH HOH A . 
N 7 HOH 133 1033 90   HOH HOH A . 
N 7 HOH 134 1034 476  HOH HOH A . 
N 7 HOH 135 1035 143  HOH HOH A . 
N 7 HOH 136 1036 467  HOH HOH A . 
N 7 HOH 137 1037 58   HOH HOH A . 
N 7 HOH 138 1038 72   HOH HOH A . 
N 7 HOH 139 1039 271  HOH HOH A . 
N 7 HOH 140 1040 183  HOH HOH A . 
N 7 HOH 141 1041 207  HOH HOH A . 
N 7 HOH 142 1042 128  HOH HOH A . 
N 7 HOH 143 1043 24   HOH HOH A . 
N 7 HOH 144 1044 26   HOH HOH A . 
N 7 HOH 145 1045 436  HOH HOH A . 
N 7 HOH 146 1046 13   HOH HOH A . 
N 7 HOH 147 1047 120  HOH HOH A . 
N 7 HOH 148 1048 80   HOH HOH A . 
N 7 HOH 149 1049 145  HOH HOH A . 
N 7 HOH 150 1050 41   HOH HOH A . 
N 7 HOH 151 1051 182  HOH HOH A . 
N 7 HOH 152 1052 460  HOH HOH A . 
N 7 HOH 153 1053 21   HOH HOH A . 
N 7 HOH 154 1054 186  HOH HOH A . 
N 7 HOH 155 1055 16   HOH HOH A . 
N 7 HOH 156 1056 211  HOH HOH A . 
N 7 HOH 157 1057 199  HOH HOH A . 
N 7 HOH 158 1058 112  HOH HOH A . 
N 7 HOH 159 1059 133  HOH HOH A . 
N 7 HOH 160 1060 421  HOH HOH A . 
N 7 HOH 161 1061 67   HOH HOH A . 
N 7 HOH 162 1062 73   HOH HOH A . 
N 7 HOH 163 1063 117  HOH HOH A . 
N 7 HOH 164 1064 49   HOH HOH A . 
N 7 HOH 165 1065 138  HOH HOH A . 
N 7 HOH 166 1066 155  HOH HOH A . 
N 7 HOH 167 1067 85   HOH HOH A . 
N 7 HOH 168 1068 164  HOH HOH A . 
N 7 HOH 169 1069 29   HOH HOH A . 
N 7 HOH 170 1070 100  HOH HOH A . 
N 7 HOH 171 1071 482  HOH HOH A . 
N 7 HOH 172 1072 40   HOH HOH A . 
N 7 HOH 173 1073 15   HOH HOH A . 
N 7 HOH 174 1074 47   HOH HOH A . 
N 7 HOH 175 1075 165  HOH HOH A . 
N 7 HOH 176 1076 60   HOH HOH A . 
N 7 HOH 177 1077 52   HOH HOH A . 
N 7 HOH 178 1078 479  HOH HOH A . 
N 7 HOH 179 1079 324  HOH HOH A . 
N 7 HOH 180 1080 264  HOH HOH A . 
N 7 HOH 181 1081 99   HOH HOH A . 
N 7 HOH 182 1082 6    HOH HOH A . 
N 7 HOH 183 1083 204  HOH HOH A . 
N 7 HOH 184 1084 391  HOH HOH A . 
N 7 HOH 185 1085 293  HOH HOH A . 
N 7 HOH 186 1086 88   HOH HOH A . 
N 7 HOH 187 1087 205  HOH HOH A . 
N 7 HOH 188 1088 84   HOH HOH A . 
N 7 HOH 189 1089 177  HOH HOH A . 
N 7 HOH 190 1090 489  HOH HOH A . 
N 7 HOH 191 1091 284  HOH HOH A . 
N 7 HOH 192 1092 46   HOH HOH A . 
N 7 HOH 193 1093 268  HOH HOH A . 
N 7 HOH 194 1094 12   HOH HOH A . 
N 7 HOH 195 1095 64   HOH HOH A . 
N 7 HOH 196 1096 23   HOH HOH A . 
N 7 HOH 197 1097 78   HOH HOH A . 
N 7 HOH 198 1098 162  HOH HOH A . 
N 7 HOH 199 1099 9    HOH HOH A . 
N 7 HOH 200 1100 18   HOH HOH A . 
N 7 HOH 201 1101 298  HOH HOH A . 
N 7 HOH 202 1102 77   HOH HOH A . 
N 7 HOH 203 1103 261  HOH HOH A . 
N 7 HOH 204 1104 32   HOH HOH A . 
N 7 HOH 205 1105 399  HOH HOH A . 
N 7 HOH 206 1106 289  HOH HOH A . 
N 7 HOH 207 1107 166  HOH HOH A . 
N 7 HOH 208 1108 152  HOH HOH A . 
N 7 HOH 209 1109 174  HOH HOH A . 
N 7 HOH 210 1110 132  HOH HOH A . 
N 7 HOH 211 1111 209  HOH HOH A . 
N 7 HOH 212 1112 410  HOH HOH A . 
N 7 HOH 213 1113 337  HOH HOH A . 
N 7 HOH 214 1114 404  HOH HOH A . 
N 7 HOH 215 1115 76   HOH HOH A . 
N 7 HOH 216 1116 160  HOH HOH A . 
N 7 HOH 217 1117 408  HOH HOH A . 
N 7 HOH 218 1118 466  HOH HOH A . 
N 7 HOH 219 1119 440  HOH HOH A . 
N 7 HOH 220 1120 413  HOH HOH A . 
N 7 HOH 221 1121 248  HOH HOH A . 
N 7 HOH 222 1122 217  HOH HOH A . 
N 7 HOH 223 1123 250  HOH HOH A . 
N 7 HOH 224 1124 281  HOH HOH A . 
N 7 HOH 225 1125 407  HOH HOH A . 
N 7 HOH 226 1126 431  HOH HOH A . 
N 7 HOH 227 1127 416  HOH HOH A . 
N 7 HOH 228 1128 456  HOH HOH A . 
N 7 HOH 229 1129 415  HOH HOH A . 
N 7 HOH 230 1130 338  HOH HOH A . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1 1 Y 1 A ASN 297 ? ND2 ? A ASN 295 ND2 
2 1 Y 1 A ASN 438 ? ND2 ? A ASN 436 ND2 
# 
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 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? autoPROC ? ? ? .        1 
? phasing          ? ? ? ? ? ? ? ? ? ? ? MOLREP   ? ? ? 7.0.0.78 2 
? 'model building' ? ? ? ? ? ? ? ? ? ? ? Coot     ? ? ? 0.8.9.2  3 
? refinement       ? ? ? ? ? ? ? ? ? ? ? REFMAC   ? ? ? 7.0.078  4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8WGG 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     36.911 
_cell.length_a_esd                 ? 
_cell.length_b                     58.630 
_cell.length_b_esd                 ? 
_cell.length_c                     212.985 
_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                         8WGG 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_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                   8WGG 
_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             2.4 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          48 
_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, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              8.0 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.1 M Tris pH 8.5, 8% (w/v) PEG 4000 and 0.8 M Lithium Chloride' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            295 
# 
_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 PILATUS 2M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2022-02-16 
_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   0.8713128 
_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                        'ESRF BEAMLINE ID23-2' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.8713128 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   ID23-2 
_diffrn_source.pdbx_synchrotron_site       ESRF 
# 
_reflns.B_iso_Wilson_estimate                          21 
_reflns.entry_id                                       8WGG 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.878 
_reflns.d_resolution_low                               45.207 
_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                                     30356 
_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                           94.5 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                8.9 
_reflns.pdbx_netI_over_av_sigmaI                       9.3 
_reflns.pdbx_netI_over_sigmaI                          9.3 
_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                                ? 
_reflns.pdbx_Rpim_I_all                                0.055 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.995 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_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                                    1.878 
_reflns_shell.d_res_low                                     1.937 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           2.8 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             1518 
_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                               9.4 
_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                               ? 
_reflns_shell.pdbx_Rpim_I_all                               0.317 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.887 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          92.3 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_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]                            -0.09 
_refine.aniso_B[1][2]                            -0.00 
_refine.aniso_B[1][3]                            -0.00 
_refine.aniso_B[2][2]                            -0.47 
_refine.aniso_B[2][3]                            0.00 
_refine.aniso_B[3][3]                            0.56 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               18.3 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.936 
_refine.correlation_coeff_Fo_to_Fc_free          0.910 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_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                                 8WGG 
_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                            1.88 
_refine.ls_d_res_low                             45.20 
_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                     28866 
_refine.ls_number_reflns_R_free                  1490 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    77.97 
_refine.ls_percent_reflns_R_free                 4.9 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.19917 
_refine.ls_R_factor_R_free                       0.22900 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.19762 
_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                    MASK 
_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                          ? 
_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       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.198 
_refine.pdbx_overall_ESU_R_Free                  0.165 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_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                 ? 
_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                             7.431 
_refine.overall_SU_ML                            0.112 
_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                         1 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.88 
_refine_hist.d_res_low                        45.20 
_refine_hist.number_atoms_solvent             230 
_refine_hist.number_atoms_total               3446 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        3175 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         41 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.006  0.012  3273  ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.016  3055  ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 1.099  1.665  4431  ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 0.352  1.571  7040  ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 6.567  5.000  424   ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 5.186  5.000  13    ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 11.756 10.000 550   ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.044  0.200  523   ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.005  0.020  3855  ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.020  733   ? r_gen_planes_other           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbd_refined                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbd_other                  ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbtor_refined              ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbtor_other                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_xyhbond_nbd_refined        ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_xyhbond_nbd_other          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_metal_ion_refined          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_metal_ion_other            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_vdw_refined       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_vdw_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_hbond_refined     ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_hbond_other       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_metal_ion_refined ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_metal_ion_other   ? ? 
'X-RAY DIFFRACTION' ? 0.755  0.966  1678  ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 0.757  0.967  1679  ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 1.230  1.723  2094  ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 1.230  1.723  2095  ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 1.154  1.137  1595  ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 1.154  1.135  1594  ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 1.873  1.990  2334  ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 4.431  13.03  13621 ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 4.279  12.86  13484 ? r_long_range_B_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_rigid_bond_restr           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_sphericity_free            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_sphericity_bonded          ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.88 
_refine_ls_shell.d_res_low                        1.926 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             71 
_refine_ls_shell.number_reflns_R_work             1147 
_refine_ls_shell.percent_reflns_obs               42.95 
_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                  0.225 
_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                  0.263 
# 
_struct.entry_id                     8WGG 
_struct.title                        'Crystal structure of basal pilin PilB from Streptococcus sanguinis' 
_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        8WGG 
_struct_keywords.text            
'Basal Pilin, isopeptide bond, oral biofilm, dental plaque, sortase pili, Bacterial adhesion, Fimbrial subunit, CELL ADHESION' 
_struct_keywords.pdbx_keywords   'CELL ADHESION' 
# 
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 2 ? 
D N N 3 ? 
E N N 4 ? 
F N N 3 ? 
G N N 4 ? 
H N N 4 ? 
I N N 4 ? 
J N N 2 ? 
K N N 5 ? 
L N N 2 ? 
M N N 6 ? 
N N N 7 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    A3CPB6_STRSV 
_struct_ref.pdbx_db_accession          A3CPB6 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;SADTTTYTIQLTGTSSGHVYELYHIFSGDLDANNVLTNIEWGAGVAIGDRAKFGDASEKAASLSGKQNDSSEVKAFAQEL
SNSLSAAGRTRVRSEQGTTTISGLKPGYYLIKDSNGSLDNVKGQAYTSIMLQVAKDTTIAIKSDVPTLTKQVKASNSENY
ISATDYAIWDTVPFQITVTLPSNYGDFSKYHFSVKDSMTSGMINNGDIQVYLQQGGSEVAITDSFSITTNNGLTVSIADL
KTLPNVNENSKIVIRYTARLKDSATLGTTGNSNTASLTYSNNPNNNASTTAQTLDSRATVYTYRLRLTKVNERQERVAGA
GFTLYKKINNQYSEVRKIEASSSSTFDFYGIKAGDYKLVESTTPAGYNTMKDIEFTITSTIDSTGALTDMTSTSATATFE
TDVNRGYINLKVVNKQGALLPNTGGIGTT
;
_struct_ref.pdbx_align_begin           25 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              8WGG 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 23 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 451 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             A3CPB6 
_struct_ref_seq.db_align_beg                  25 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  453 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       25 
_struct_ref_seq.pdbx_auth_seq_align_end       453 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 8WGG MET A 1  ? UNP A3CPB6 ? ? 'initiating methionine' 3  1  
1 8WGG GLY A 2  ? UNP A3CPB6 ? ? 'expression tag'        4  2  
1 8WGG SER A 3  ? UNP A3CPB6 ? ? 'expression tag'        5  3  
1 8WGG SER A 4  ? UNP A3CPB6 ? ? 'expression tag'        6  4  
1 8WGG HIS A 5  ? UNP A3CPB6 ? ? 'expression tag'        7  5  
1 8WGG HIS A 6  ? UNP A3CPB6 ? ? 'expression tag'        8  6  
1 8WGG HIS A 7  ? UNP A3CPB6 ? ? 'expression tag'        9  7  
1 8WGG HIS A 8  ? UNP A3CPB6 ? ? 'expression tag'        10 8  
1 8WGG HIS A 9  ? UNP A3CPB6 ? ? 'expression tag'        11 9  
1 8WGG HIS A 10 ? UNP A3CPB6 ? ? 'expression tag'        12 10 
1 8WGG SER A 11 ? UNP A3CPB6 ? ? 'expression tag'        13 11 
1 8WGG SER A 12 ? UNP A3CPB6 ? ? 'expression tag'        14 12 
1 8WGG GLY A 13 ? UNP A3CPB6 ? ? 'expression tag'        15 13 
1 8WGG LEU A 14 ? UNP A3CPB6 ? ? 'expression tag'        16 14 
1 8WGG VAL A 15 ? UNP A3CPB6 ? ? 'expression tag'        17 15 
1 8WGG PRO A 16 ? UNP A3CPB6 ? ? 'expression tag'        18 16 
1 8WGG ARG A 17 ? UNP A3CPB6 ? ? 'expression tag'        19 17 
1 8WGG ARG A 18 ? UNP A3CPB6 ? ? 'expression tag'        20 18 
1 8WGG GLY A 19 ? UNP A3CPB6 ? ? 'expression tag'        21 19 
1 8WGG SER A 20 ? UNP A3CPB6 ? ? 'expression tag'        22 20 
1 8WGG HIS A 21 ? UNP A3CPB6 ? ? 'expression tag'        23 21 
1 8WGG MET A 22 ? UNP A3CPB6 ? ? 'expression tag'        24 22 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 150   ? 
1 MORE         -12   ? 
1 'SSA (A^2)'  20090 ? 
# 
_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,I,J,K,L,M,N 
# 
_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                Monomer 
# 
_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 ALA A 68  ? ALA A 73  ? ALA A 70  ALA A 75  1 ? 6  
HELX_P HELX_P2 AA2 ASP A 77  ? SER A 86  ? ASP A 79  SER A 88  1 ? 10 
HELX_P HELX_P3 AA3 SER A 92  ? SER A 103 ? SER A 94  SER A 105 1 ? 12 
HELX_P HELX_P4 AA4 SER A 107 ? ALA A 109 ? SER A 109 ALA A 111 5 ? 3  
HELX_P HELX_P5 AA5 ASN A 205 ? PHE A 209 ? ASN A 207 PHE A 211 5 ? 5  
HELX_P HELX_P6 AA6 THR A 244 ? PHE A 247 ? THR A 246 PHE A 249 5 ? 4  
HELX_P HELX_P7 AA7 ASP A 261 ? LEU A 265 ? ASP A 263 LEU A 267 5 ? 5  
HELX_P HELX_P8 AA8 PRO A 305 ? ALA A 309 ? PRO A 307 ALA A 311 5 ? 5  
# 
_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 
metalc1 metalc ? ? A TYR 42 OH ? ? ? 1_555 M NA  . NA ? ? A TYR 44  A NA  812  1_555 ? ? ? ? ? ? ? 2.465 ? ? 
metalc2 metalc ? ? M NA  .  NA ? ? ? 1_555 N HOH . O  ? ? A NA  812 A HOH 928  1_555 ? ? ? ? ? ? ? 2.724 ? ? 
metalc3 metalc ? ? M NA  .  NA ? ? ? 1_555 N HOH . O  ? ? A NA  812 A HOH 1070 1_555 ? ? ? ? ? ? ? 2.763 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1 OH ? A TYR 42 ? A TYR 44  ? 1_555 NA ? M NA . ? A NA 812 ? 1_555 O ? N HOH . ? A HOH 928  ? 1_555 116.0 ? 
2 OH ? A TYR 42 ? A TYR 44  ? 1_555 NA ? M NA . ? A NA 812 ? 1_555 O ? N HOH . ? A HOH 1070 ? 1_555 121.9 ? 
3 O  ? N HOH .  ? A HOH 928 ? 1_555 NA ? M NA . ? A NA 812 ? 1_555 O ? N HOH . ? A HOH 1070 ? 1_555 119.1 ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 3 ? 
AA2 ? 3 ? 
AA3 ? 4 ? 
AA4 ? 5 ? 
AA5 ? 6 ? 
AA6 ? 6 ? 
AA7 ? 4 ? 
AA8 ? 4 ? 
AA9 ? 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 ? anti-parallel 
AA1 2 3 ? parallel      
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA4 4 5 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA5 2 3 ? anti-parallel 
AA5 3 4 ? anti-parallel 
AA5 4 5 ? anti-parallel 
AA5 5 6 ? anti-parallel 
AA6 1 2 ? parallel      
AA6 2 3 ? anti-parallel 
AA6 3 4 ? anti-parallel 
AA6 4 5 ? anti-parallel 
AA6 5 6 ? anti-parallel 
AA7 1 2 ? parallel      
AA7 2 3 ? anti-parallel 
AA7 3 4 ? anti-parallel 
AA8 1 2 ? anti-parallel 
AA8 2 3 ? parallel      
AA8 3 4 ? anti-parallel 
AA9 1 2 ? anti-parallel 
AA9 2 3 ? anti-parallel 
AA9 3 4 ? anti-parallel 
AA9 4 5 ? anti-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 GLY A 119 ? LEU A 126 ? GLY A 121 LEU A 128 
AA1 2 TYR A 29  ? THR A 36  ? TYR A 31  THR A 38  
AA1 3 THR A 159 ? ALA A 162 ? THR A 161 ALA A 164 
AA2 1 LEU A 58  ? TRP A 63  ? LEU A 60  TRP A 65  
AA2 2 VAL A 41  ? LEU A 52  ? VAL A 43  LEU A 54  
AA2 3 ARG A 111 ? ARG A 115 ? ARG A 113 ARG A 117 
AA3 1 LEU A 58  ? TRP A 63  ? LEU A 60  TRP A 65  
AA3 2 VAL A 41  ? LEU A 52  ? VAL A 43  LEU A 54  
AA3 3 GLY A 129 ? ASP A 135 ? GLY A 131 ASP A 137 
AA3 4 MET A 152 ? VAL A 155 ? MET A 154 VAL A 157 
AA4 1 TYR A 182 ? ILE A 183 ? TYR A 184 ILE A 185 
AA4 2 THR A 169 ? LYS A 175 ? THR A 171 LYS A 177 
AA4 3 VAL A 194 ? THR A 201 ? VAL A 196 THR A 203 
AA4 4 LYS A 273 ? LEU A 282 ? LYS A 275 LEU A 284 
AA4 5 MET A 224 ? ASN A 226 ? MET A 226 ASN A 228 
AA5 1 TYR A 182 ? ILE A 183 ? TYR A 184 ILE A 185 
AA5 2 THR A 169 ? LYS A 175 ? THR A 171 LYS A 177 
AA5 3 VAL A 194 ? THR A 201 ? VAL A 196 THR A 203 
AA5 4 LYS A 273 ? LEU A 282 ? LYS A 275 LEU A 284 
AA5 5 GLN A 231 ? GLN A 236 ? GLN A 233 GLN A 238 
AA5 6 SER A 239 ? ALA A 242 ? SER A 241 ALA A 244 
AA6 1 ALA A 185 ? ASP A 187 ? ALA A 187 ASP A 189 
AA6 2 SER A 318 ? TYR A 323 ? SER A 320 TYR A 325 
AA6 3 ASN A 293 ? SER A 302 ? ASN A 295 SER A 304 
AA6 4 PHE A 214 ? ASP A 218 ? PHE A 216 ASP A 220 
AA6 5 LEU A 255 ? ILE A 259 ? LEU A 257 ILE A 261 
AA6 6 SER A 248 ? THR A 250 ? SER A 250 THR A 252 
AA7 1 ALA A 185 ? ASP A 187 ? ALA A 187 ASP A 189 
AA7 2 SER A 318 ? TYR A 323 ? SER A 320 TYR A 325 
AA7 3 ASN A 293 ? SER A 302 ? ASN A 295 SER A 304 
AA7 4 THR A 312 ? GLN A 314 ? THR A 314 GLN A 316 
AA8 1 THR A 367 ? ILE A 373 ? THR A 369 ILE A 375 
AA8 2 TYR A 325 ? ASN A 333 ? TYR A 327 ASN A 335 
AA8 3 TYR A 429 ? ASN A 436 ? TYR A 431 ASN A 438 
AA8 4 GLU A 422 ? ASP A 424 ? GLU A 424 ASP A 426 
AA9 1 GLN A 353 ? ILE A 360 ? GLN A 355 ILE A 362 
AA9 2 GLY A 343 ? ILE A 350 ? GLY A 345 ILE A 352 
AA9 3 GLY A 376 ? THR A 384 ? GLY A 378 THR A 386 
AA9 4 ILE A 395 ? ILE A 403 ? ILE A 397 ILE A 405 
AA9 5 LEU A 409 ? SER A 416 ? LEU A 411 SER A 418 
# 
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 THR A 121 ? O THR A 123 N LEU A 33  ? N LEU A 35  
AA1 2 3 N GLN A 32  ? N GLN A 34  O ILE A 161 ? O ILE A 163 
AA2 1 2 O THR A 59  ? O THR A 61  N ASP A 51  ? N ASP A 53  
AA2 2 3 N LEU A 44  ? N LEU A 46  O THR A 112 ? O THR A 114 
AA3 1 2 O THR A 59  ? O THR A 61  N ASP A 51  ? N ASP A 53  
AA3 2 3 N GLU A 43  ? N GLU A 45  O LYS A 134 ? O LYS A 136 
AA3 3 4 N TYR A 131 ? N TYR A 133 O GLN A 154 ? O GLN A 156 
AA4 1 2 O ILE A 183 ? O ILE A 185 N VAL A 174 ? N VAL A 176 
AA4 2 3 N THR A 171 ? N THR A 173 O THR A 199 ? O THR A 201 
AA4 3 4 N VAL A 194 ? N VAL A 196 O ALA A 280 ? O ALA A 282 
AA4 4 5 O ARG A 281 ? O ARG A 283 N ILE A 225 ? N ILE A 227 
AA5 1 2 O ILE A 183 ? O ILE A 185 N VAL A 174 ? N VAL A 176 
AA5 2 3 N THR A 171 ? N THR A 173 O THR A 199 ? O THR A 201 
AA5 3 4 N VAL A 194 ? N VAL A 196 O ALA A 280 ? O ALA A 282 
AA5 4 5 O LYS A 273 ? O LYS A 275 N GLN A 235 ? N GLN A 237 
AA5 5 6 N LEU A 234 ? N LEU A 236 O VAL A 241 ? O VAL A 243 
AA6 1 2 N THR A 186 ? N THR A 188 O TYR A 323 ? O TYR A 325 
AA6 2 3 O SER A 318 ? O SER A 320 N ALA A 297 ? N ALA A 299 
AA6 3 4 O THR A 300 ? O THR A 302 N SER A 215 ? N SER A 217 
AA6 4 5 N ASP A 218 ? N ASP A 220 O LEU A 255 ? O LEU A 257 
AA6 5 6 O SER A 258 ? O SER A 260 N SER A 248 ? N SER A 250 
AA7 1 2 N THR A 186 ? N THR A 188 O TYR A 323 ? O TYR A 325 
AA7 2 3 O SER A 318 ? O SER A 320 N ALA A 297 ? N ALA A 299 
AA7 3 4 N TYR A 301 ? N TYR A 303 O ALA A 313 ? O ALA A 315 
AA8 1 2 O PHE A 370 ? O PHE A 372 N LEU A 327 ? N LEU A 329 
AA8 2 3 N ARG A 328 ? N ARG A 330 O ILE A 430 ? O ILE A 432 
AA8 3 4 O ASN A 431 ? O ASN A 433 N GLU A 422 ? N GLU A 424 
AA9 1 2 O ARG A 358 ? O ARG A 360 N LEU A 346 ? N LEU A 348 
AA9 2 3 N LYS A 349 ? N LYS A 351 O ASP A 377 ? O ASP A 379 
AA9 3 4 N TYR A 378 ? N TYR A 380 O PHE A 397 ? O PHE A 399 
AA9 4 5 N THR A 402 ? N THR A 404 O THR A 410 ? O THR A 412 
# 
_pdbx_entry_details.entry_id                   8WGG 
_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 NZ A LYS 174 ? ? CG A ASN 297 ? ? 1.33 
2 1 NZ A LYS 333 ? ? CG A ASN 438 ? ? 1.34 
# 
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 LYS A 159 ? ? -142.54 32.36   
2 1 MET A 222 ? ? 63.62   -178.53 
3 1 ASN A 353 ? ? 70.07   -125.78 
# 
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 31.7052 24.2683 17.6710 0.0220 ? 0.0045  ? -0.0216 ? 0.0499 ? 0.0058  ? 0.0234 ? 1.0328 ? 0.0581 ? 
0.1072 ? 2.1648 ? -0.8819 ? 4.1701 ? 0.0728  ? 0.0322  ? -0.0634 ? -0.0850 ? 0.0687  ? 0.1012 ? 0.1208  ? -0.1462 ? -0.1415 ? 
2 'X-RAY DIFFRACTION' ? refined 22.0055 17.7226 51.9582 0.0758 ? -0.0247 ? -0.0424 ? 0.0144 ? 0.0071  ? 0.0336 ? 0.8168 ? 0.1074 ? 
0.6260 ? 0.6433 ? 0.0906  ? 3.3371 ? -0.0016 ? -0.0526 ? 0.0337  ? -0.0232 ? -0.0339 ? 0.0885 ? 0.0458  ? -0.1112 ? 0.0354  ? 
3 'X-RAY DIFFRACTION' ? refined 30.5302 22.4542 88.4669 0.0430 ? 0.0072  ? -0.0294 ? 0.0593 ? -0.0295 ? 0.0373 ? 0.6958 ? 0.1559 ? 
0.3170 ? 1.2112 ? -0.8295 ? 4.9055 ? -0.1049 ? -0.0671 ? 0.1112  ? -0.0653 ? 0.0538  ? 0.0860 ? -0.2857 ? -0.0385 ? 0.0511  ? 
# 
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 ? ? A 29  ? ? ? A 166 ? ? ? 
2 'X-RAY DIFFRACTION' 2 ? ? A 167 ? ? ? A 326 ? ? ? 
3 'X-RAY DIFFRACTION' 3 ? ? A 327 ? ? ? A 445 ? ? ? 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A MET 3   ? A MET 1   
2  1 Y 1 A GLY 4   ? A GLY 2   
3  1 Y 1 A SER 5   ? A SER 3   
4  1 Y 1 A SER 6   ? A SER 4   
5  1 Y 1 A HIS 7   ? A HIS 5   
6  1 Y 1 A HIS 8   ? A HIS 6   
7  1 Y 1 A HIS 9   ? A HIS 7   
8  1 Y 1 A HIS 10  ? A HIS 8   
9  1 Y 1 A HIS 11  ? A HIS 9   
10 1 Y 1 A HIS 12  ? A HIS 10  
11 1 Y 1 A SER 13  ? A SER 11  
12 1 Y 1 A SER 14  ? A SER 12  
13 1 Y 1 A GLY 15  ? A GLY 13  
14 1 Y 1 A LEU 16  ? A LEU 14  
15 1 Y 1 A VAL 17  ? A VAL 15  
16 1 Y 1 A PRO 18  ? A PRO 16  
17 1 Y 1 A ARG 19  ? A ARG 17  
18 1 Y 1 A ARG 20  ? A ARG 18  
19 1 Y 1 A GLY 21  ? A GLY 19  
20 1 Y 1 A SER 22  ? A SER 20  
21 1 Y 1 A HIS 23  ? A HIS 21  
22 1 Y 1 A MET 24  ? A MET 22  
23 1 Y 1 A SER 25  ? A SER 23  
24 1 Y 1 A ALA 26  ? A ALA 24  
25 1 Y 1 A ASP 27  ? A ASP 25  
26 1 Y 1 A ASN 446 ? A ASN 444 
27 1 Y 1 A THR 447 ? A THR 445 
28 1 Y 1 A GLY 448 ? A GLY 446 
29 1 Y 1 A GLY 449 ? A GLY 447 
30 1 Y 1 A ILE 450 ? A ILE 448 
31 1 Y 1 A GLY 451 ? A GLY 449 
32 1 Y 1 A THR 452 ? A THR 450 
33 1 Y 1 A THR 453 ? A THR 451 
# 
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 
ACT C    C  N N 1   
ACT O    O  N N 2   
ACT OXT  O  N N 3   
ACT CH3  C  N N 4   
ACT H1   H  N N 5   
ACT H2   H  N N 6   
ACT H3   H  N N 7   
ACY C    C  N N 8   
ACY O    O  N N 9   
ACY OXT  O  N N 10  
ACY CH3  C  N N 11  
ACY HXT  H  N N 12  
ACY H1   H  N N 13  
ACY H2   H  N N 14  
ACY H3   H  N N 15  
ALA N    N  N N 16  
ALA CA   C  N S 17  
ALA C    C  N N 18  
ALA O    O  N N 19  
ALA CB   C  N N 20  
ALA OXT  O  N N 21  
ALA H    H  N N 22  
ALA H2   H  N N 23  
ALA HA   H  N N 24  
ALA HB1  H  N N 25  
ALA HB2  H  N N 26  
ALA HB3  H  N N 27  
ALA HXT  H  N N 28  
ARG N    N  N N 29  
ARG CA   C  N S 30  
ARG C    C  N N 31  
ARG O    O  N N 32  
ARG CB   C  N N 33  
ARG CG   C  N N 34  
ARG CD   C  N N 35  
ARG NE   N  N N 36  
ARG CZ   C  N N 37  
ARG NH1  N  N N 38  
ARG NH2  N  N N 39  
ARG OXT  O  N N 40  
ARG H    H  N N 41  
ARG H2   H  N N 42  
ARG HA   H  N N 43  
ARG HB2  H  N N 44  
ARG HB3  H  N N 45  
ARG HG2  H  N N 46  
ARG HG3  H  N N 47  
ARG HD2  H  N N 48  
ARG HD3  H  N N 49  
ARG HE   H  N N 50  
ARG HH11 H  N N 51  
ARG HH12 H  N N 52  
ARG HH21 H  N N 53  
ARG HH22 H  N N 54  
ARG HXT  H  N N 55  
ASN N    N  N N 56  
ASN CA   C  N S 57  
ASN C    C  N N 58  
ASN O    O  N N 59  
ASN CB   C  N N 60  
ASN CG   C  N N 61  
ASN OD1  O  N N 62  
ASN ND2  N  N N 63  
ASN OXT  O  N N 64  
ASN H    H  N N 65  
ASN H2   H  N N 66  
ASN HA   H  N N 67  
ASN HB2  H  N N 68  
ASN HB3  H  N N 69  
ASN HD21 H  N N 70  
ASN HD22 H  N N 71  
ASN HXT  H  N N 72  
ASP N    N  N N 73  
ASP CA   C  N S 74  
ASP C    C  N N 75  
ASP O    O  N N 76  
ASP CB   C  N N 77  
ASP CG   C  N N 78  
ASP OD1  O  N N 79  
ASP OD2  O  N N 80  
ASP OXT  O  N N 81  
ASP H    H  N N 82  
ASP H2   H  N N 83  
ASP HA   H  N N 84  
ASP HB2  H  N N 85  
ASP HB3  H  N N 86  
ASP HD2  H  N N 87  
ASP HXT  H  N N 88  
EDO C1   C  N N 89  
EDO O1   O  N N 90  
EDO C2   C  N N 91  
EDO O2   O  N N 92  
EDO H11  H  N N 93  
EDO H12  H  N N 94  
EDO HO1  H  N N 95  
EDO H21  H  N N 96  
EDO H22  H  N N 97  
EDO HO2  H  N N 98  
FMT C    C  N N 99  
FMT O1   O  N N 100 
FMT O2   O  N N 101 
FMT H    H  N N 102 
FMT HO2  H  N N 103 
GLN N    N  N N 104 
GLN CA   C  N S 105 
GLN C    C  N N 106 
GLN O    O  N N 107 
GLN CB   C  N N 108 
GLN CG   C  N N 109 
GLN CD   C  N N 110 
GLN OE1  O  N N 111 
GLN NE2  N  N N 112 
GLN OXT  O  N N 113 
GLN H    H  N N 114 
GLN H2   H  N N 115 
GLN HA   H  N N 116 
GLN HB2  H  N N 117 
GLN HB3  H  N N 118 
GLN HG2  H  N N 119 
GLN HG3  H  N N 120 
GLN HE21 H  N N 121 
GLN HE22 H  N N 122 
GLN HXT  H  N N 123 
GLU N    N  N N 124 
GLU CA   C  N S 125 
GLU C    C  N N 126 
GLU O    O  N N 127 
GLU CB   C  N N 128 
GLU CG   C  N N 129 
GLU CD   C  N N 130 
GLU OE1  O  N N 131 
GLU OE2  O  N N 132 
GLU OXT  O  N N 133 
GLU H    H  N N 134 
GLU H2   H  N N 135 
GLU HA   H  N N 136 
GLU HB2  H  N N 137 
GLU HB3  H  N N 138 
GLU HG2  H  N N 139 
GLU HG3  H  N N 140 
GLU HE2  H  N N 141 
GLU HXT  H  N N 142 
GLY N    N  N N 143 
GLY CA   C  N N 144 
GLY C    C  N N 145 
GLY O    O  N N 146 
GLY OXT  O  N N 147 
GLY H    H  N N 148 
GLY H2   H  N N 149 
GLY HA2  H  N N 150 
GLY HA3  H  N N 151 
GLY HXT  H  N N 152 
HIS N    N  N N 153 
HIS CA   C  N S 154 
HIS C    C  N N 155 
HIS O    O  N N 156 
HIS CB   C  N N 157 
HIS CG   C  Y N 158 
HIS ND1  N  Y N 159 
HIS CD2  C  Y N 160 
HIS CE1  C  Y N 161 
HIS NE2  N  Y N 162 
HIS OXT  O  N N 163 
HIS H    H  N N 164 
HIS H2   H  N N 165 
HIS HA   H  N N 166 
HIS HB2  H  N N 167 
HIS HB3  H  N N 168 
HIS HD1  H  N N 169 
HIS HD2  H  N N 170 
HIS HE1  H  N N 171 
HIS HE2  H  N N 172 
HIS HXT  H  N N 173 
HOH O    O  N N 174 
HOH H1   H  N N 175 
HOH H2   H  N N 176 
ILE N    N  N N 177 
ILE CA   C  N S 178 
ILE C    C  N N 179 
ILE O    O  N N 180 
ILE CB   C  N S 181 
ILE CG1  C  N N 182 
ILE CG2  C  N N 183 
ILE CD1  C  N N 184 
ILE OXT  O  N N 185 
ILE H    H  N N 186 
ILE H2   H  N N 187 
ILE HA   H  N N 188 
ILE HB   H  N N 189 
ILE HG12 H  N N 190 
ILE HG13 H  N N 191 
ILE HG21 H  N N 192 
ILE HG22 H  N N 193 
ILE HG23 H  N N 194 
ILE HD11 H  N N 195 
ILE HD12 H  N N 196 
ILE HD13 H  N N 197 
ILE HXT  H  N N 198 
LEU N    N  N N 199 
LEU CA   C  N S 200 
LEU C    C  N N 201 
LEU O    O  N N 202 
LEU CB   C  N N 203 
LEU CG   C  N N 204 
LEU CD1  C  N N 205 
LEU CD2  C  N N 206 
LEU OXT  O  N N 207 
LEU H    H  N N 208 
LEU H2   H  N N 209 
LEU HA   H  N N 210 
LEU HB2  H  N N 211 
LEU HB3  H  N N 212 
LEU HG   H  N N 213 
LEU HD11 H  N N 214 
LEU HD12 H  N N 215 
LEU HD13 H  N N 216 
LEU HD21 H  N N 217 
LEU HD22 H  N N 218 
LEU HD23 H  N N 219 
LEU HXT  H  N N 220 
LYS N    N  N N 221 
LYS CA   C  N S 222 
LYS C    C  N N 223 
LYS O    O  N N 224 
LYS CB   C  N N 225 
LYS CG   C  N N 226 
LYS CD   C  N N 227 
LYS CE   C  N N 228 
LYS NZ   N  N N 229 
LYS OXT  O  N N 230 
LYS H    H  N N 231 
LYS H2   H  N N 232 
LYS HA   H  N N 233 
LYS HB2  H  N N 234 
LYS HB3  H  N N 235 
LYS HG2  H  N N 236 
LYS HG3  H  N N 237 
LYS HD2  H  N N 238 
LYS HD3  H  N N 239 
LYS HE2  H  N N 240 
LYS HE3  H  N N 241 
LYS HZ1  H  N N 242 
LYS HZ2  H  N N 243 
LYS HZ3  H  N N 244 
LYS HXT  H  N N 245 
MET N    N  N N 246 
MET CA   C  N S 247 
MET C    C  N N 248 
MET O    O  N N 249 
MET CB   C  N N 250 
MET CG   C  N N 251 
MET SD   S  N N 252 
MET CE   C  N N 253 
MET OXT  O  N N 254 
MET H    H  N N 255 
MET H2   H  N N 256 
MET HA   H  N N 257 
MET HB2  H  N N 258 
MET HB3  H  N N 259 
MET HG2  H  N N 260 
MET HG3  H  N N 261 
MET HE1  H  N N 262 
MET HE2  H  N N 263 
MET HE3  H  N N 264 
MET HXT  H  N N 265 
NA  NA   NA N N 266 
PHE N    N  N N 267 
PHE CA   C  N S 268 
PHE C    C  N N 269 
PHE O    O  N N 270 
PHE CB   C  N N 271 
PHE CG   C  Y N 272 
PHE CD1  C  Y N 273 
PHE CD2  C  Y N 274 
PHE CE1  C  Y N 275 
PHE CE2  C  Y N 276 
PHE CZ   C  Y N 277 
PHE OXT  O  N N 278 
PHE H    H  N N 279 
PHE H2   H  N N 280 
PHE HA   H  N N 281 
PHE HB2  H  N N 282 
PHE HB3  H  N N 283 
PHE HD1  H  N N 284 
PHE HD2  H  N N 285 
PHE HE1  H  N N 286 
PHE HE2  H  N N 287 
PHE HZ   H  N N 288 
PHE HXT  H  N N 289 
PRO N    N  N N 290 
PRO CA   C  N S 291 
PRO C    C  N N 292 
PRO O    O  N N 293 
PRO CB   C  N N 294 
PRO CG   C  N N 295 
PRO CD   C  N N 296 
PRO OXT  O  N N 297 
PRO H    H  N N 298 
PRO HA   H  N N 299 
PRO HB2  H  N N 300 
PRO HB3  H  N N 301 
PRO HG2  H  N N 302 
PRO HG3  H  N N 303 
PRO HD2  H  N N 304 
PRO HD3  H  N N 305 
PRO HXT  H  N N 306 
SER N    N  N N 307 
SER CA   C  N S 308 
SER C    C  N N 309 
SER O    O  N N 310 
SER CB   C  N N 311 
SER OG   O  N N 312 
SER OXT  O  N N 313 
SER H    H  N N 314 
SER H2   H  N N 315 
SER HA   H  N N 316 
SER HB2  H  N N 317 
SER HB3  H  N N 318 
SER HG   H  N N 319 
SER HXT  H  N N 320 
THR N    N  N N 321 
THR CA   C  N S 322 
THR C    C  N N 323 
THR O    O  N N 324 
THR CB   C  N R 325 
THR OG1  O  N N 326 
THR CG2  C  N N 327 
THR OXT  O  N N 328 
THR H    H  N N 329 
THR H2   H  N N 330 
THR HA   H  N N 331 
THR HB   H  N N 332 
THR HG1  H  N N 333 
THR HG21 H  N N 334 
THR HG22 H  N N 335 
THR HG23 H  N N 336 
THR HXT  H  N N 337 
TRP N    N  N N 338 
TRP CA   C  N S 339 
TRP C    C  N N 340 
TRP O    O  N N 341 
TRP CB   C  N N 342 
TRP CG   C  Y N 343 
TRP CD1  C  Y N 344 
TRP CD2  C  Y N 345 
TRP NE1  N  Y N 346 
TRP CE2  C  Y N 347 
TRP CE3  C  Y N 348 
TRP CZ2  C  Y N 349 
TRP CZ3  C  Y N 350 
TRP CH2  C  Y N 351 
TRP OXT  O  N N 352 
TRP H    H  N N 353 
TRP H2   H  N N 354 
TRP HA   H  N N 355 
TRP HB2  H  N N 356 
TRP HB3  H  N N 357 
TRP HD1  H  N N 358 
TRP HE1  H  N N 359 
TRP HE3  H  N N 360 
TRP HZ2  H  N N 361 
TRP HZ3  H  N N 362 
TRP HH2  H  N N 363 
TRP HXT  H  N N 364 
TYR N    N  N N 365 
TYR CA   C  N S 366 
TYR C    C  N N 367 
TYR O    O  N N 368 
TYR CB   C  N N 369 
TYR CG   C  Y N 370 
TYR CD1  C  Y N 371 
TYR CD2  C  Y N 372 
TYR CE1  C  Y N 373 
TYR CE2  C  Y N 374 
TYR CZ   C  Y N 375 
TYR OH   O  N N 376 
TYR OXT  O  N N 377 
TYR H    H  N N 378 
TYR H2   H  N N 379 
TYR HA   H  N N 380 
TYR HB2  H  N N 381 
TYR HB3  H  N N 382 
TYR HD1  H  N N 383 
TYR HD2  H  N N 384 
TYR HE1  H  N N 385 
TYR HE2  H  N N 386 
TYR HH   H  N N 387 
TYR HXT  H  N N 388 
VAL N    N  N N 389 
VAL CA   C  N S 390 
VAL C    C  N N 391 
VAL O    O  N N 392 
VAL CB   C  N N 393 
VAL CG1  C  N N 394 
VAL CG2  C  N N 395 
VAL OXT  O  N N 396 
VAL H    H  N N 397 
VAL H2   H  N N 398 
VAL HA   H  N N 399 
VAL HB   H  N N 400 
VAL HG11 H  N N 401 
VAL HG12 H  N N 402 
VAL HG13 H  N N 403 
VAL HG21 H  N N 404 
VAL HG22 H  N N 405 
VAL HG23 H  N N 406 
VAL HXT  H  N N 407 
# 
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 
ACT C   O    doub N N 1   
ACT C   OXT  sing N N 2   
ACT C   CH3  sing N N 3   
ACT CH3 H1   sing N N 4   
ACT CH3 H2   sing N N 5   
ACT CH3 H3   sing N N 6   
ACY C   O    doub N N 7   
ACY C   OXT  sing N N 8   
ACY C   CH3  sing N N 9   
ACY OXT HXT  sing N N 10  
ACY CH3 H1   sing N N 11  
ACY CH3 H2   sing N N 12  
ACY CH3 H3   sing N N 13  
ALA N   CA   sing N N 14  
ALA N   H    sing N N 15  
ALA N   H2   sing N N 16  
ALA CA  C    sing N N 17  
ALA CA  CB   sing N N 18  
ALA CA  HA   sing N N 19  
ALA C   O    doub N N 20  
ALA C   OXT  sing N N 21  
ALA CB  HB1  sing N N 22  
ALA CB  HB2  sing N N 23  
ALA CB  HB3  sing N N 24  
ALA OXT HXT  sing N N 25  
ARG N   CA   sing N N 26  
ARG N   H    sing N N 27  
ARG N   H2   sing N N 28  
ARG CA  C    sing N N 29  
ARG CA  CB   sing N N 30  
ARG CA  HA   sing N N 31  
ARG C   O    doub N N 32  
ARG C   OXT  sing N N 33  
ARG CB  CG   sing N N 34  
ARG CB  HB2  sing N N 35  
ARG CB  HB3  sing N N 36  
ARG CG  CD   sing N N 37  
ARG CG  HG2  sing N N 38  
ARG CG  HG3  sing N N 39  
ARG CD  NE   sing N N 40  
ARG CD  HD2  sing N N 41  
ARG CD  HD3  sing N N 42  
ARG NE  CZ   sing N N 43  
ARG NE  HE   sing N N 44  
ARG CZ  NH1  sing N N 45  
ARG CZ  NH2  doub N N 46  
ARG NH1 HH11 sing N N 47  
ARG NH1 HH12 sing N N 48  
ARG NH2 HH21 sing N N 49  
ARG NH2 HH22 sing N N 50  
ARG OXT HXT  sing N N 51  
ASN N   CA   sing N N 52  
ASN N   H    sing N N 53  
ASN N   H2   sing N N 54  
ASN CA  C    sing N N 55  
ASN CA  CB   sing N N 56  
ASN CA  HA   sing N N 57  
ASN C   O    doub N N 58  
ASN C   OXT  sing N N 59  
ASN CB  CG   sing N N 60  
ASN CB  HB2  sing N N 61  
ASN CB  HB3  sing N N 62  
ASN CG  OD1  doub N N 63  
ASN CG  ND2  sing N N 64  
ASN ND2 HD21 sing N N 65  
ASN ND2 HD22 sing N N 66  
ASN OXT HXT  sing N N 67  
ASP N   CA   sing N N 68  
ASP N   H    sing N N 69  
ASP N   H2   sing N N 70  
ASP CA  C    sing N N 71  
ASP CA  CB   sing N N 72  
ASP CA  HA   sing N N 73  
ASP C   O    doub N N 74  
ASP C   OXT  sing N N 75  
ASP CB  CG   sing N N 76  
ASP CB  HB2  sing N N 77  
ASP CB  HB3  sing N N 78  
ASP CG  OD1  doub N N 79  
ASP CG  OD2  sing N N 80  
ASP OD2 HD2  sing N N 81  
ASP OXT HXT  sing N N 82  
EDO C1  O1   sing N N 83  
EDO C1  C2   sing N N 84  
EDO C1  H11  sing N N 85  
EDO C1  H12  sing N N 86  
EDO O1  HO1  sing N N 87  
EDO C2  O2   sing N N 88  
EDO C2  H21  sing N N 89  
EDO C2  H22  sing N N 90  
EDO O2  HO2  sing N N 91  
FMT C   O1   doub N N 92  
FMT C   O2   sing N N 93  
FMT C   H    sing N N 94  
FMT O2  HO2  sing N N 95  
GLN N   CA   sing N N 96  
GLN N   H    sing N N 97  
GLN N   H2   sing N N 98  
GLN CA  C    sing N N 99  
GLN CA  CB   sing N N 100 
GLN CA  HA   sing N N 101 
GLN C   O    doub N N 102 
GLN C   OXT  sing N N 103 
GLN CB  CG   sing N N 104 
GLN CB  HB2  sing N N 105 
GLN CB  HB3  sing N N 106 
GLN CG  CD   sing N N 107 
GLN CG  HG2  sing N N 108 
GLN CG  HG3  sing N N 109 
GLN CD  OE1  doub N N 110 
GLN CD  NE2  sing N N 111 
GLN NE2 HE21 sing N N 112 
GLN NE2 HE22 sing N N 113 
GLN OXT HXT  sing N N 114 
GLU N   CA   sing N N 115 
GLU N   H    sing N N 116 
GLU N   H2   sing N N 117 
GLU CA  C    sing N N 118 
GLU CA  CB   sing N N 119 
GLU CA  HA   sing N N 120 
GLU C   O    doub N N 121 
GLU C   OXT  sing N N 122 
GLU CB  CG   sing N N 123 
GLU CB  HB2  sing N N 124 
GLU CB  HB3  sing N N 125 
GLU CG  CD   sing N N 126 
GLU CG  HG2  sing N N 127 
GLU CG  HG3  sing N N 128 
GLU CD  OE1  doub N N 129 
GLU CD  OE2  sing N N 130 
GLU OE2 HE2  sing N N 131 
GLU OXT HXT  sing N N 132 
GLY N   CA   sing N N 133 
GLY N   H    sing N N 134 
GLY N   H2   sing N N 135 
GLY CA  C    sing N N 136 
GLY CA  HA2  sing N N 137 
GLY CA  HA3  sing N N 138 
GLY C   O    doub N N 139 
GLY C   OXT  sing N N 140 
GLY OXT HXT  sing N N 141 
HIS N   CA   sing N N 142 
HIS N   H    sing N N 143 
HIS N   H2   sing N N 144 
HIS CA  C    sing N N 145 
HIS CA  CB   sing N N 146 
HIS CA  HA   sing N N 147 
HIS C   O    doub N N 148 
HIS C   OXT  sing N N 149 
HIS CB  CG   sing N N 150 
HIS CB  HB2  sing N N 151 
HIS CB  HB3  sing N N 152 
HIS CG  ND1  sing Y N 153 
HIS CG  CD2  doub Y N 154 
HIS ND1 CE1  doub Y N 155 
HIS ND1 HD1  sing N N 156 
HIS CD2 NE2  sing Y N 157 
HIS CD2 HD2  sing N N 158 
HIS CE1 NE2  sing Y N 159 
HIS CE1 HE1  sing N N 160 
HIS NE2 HE2  sing N N 161 
HIS OXT HXT  sing N N 162 
HOH O   H1   sing N N 163 
HOH O   H2   sing N N 164 
ILE N   CA   sing N N 165 
ILE N   H    sing N N 166 
ILE N   H2   sing N N 167 
ILE CA  C    sing N N 168 
ILE CA  CB   sing N N 169 
ILE CA  HA   sing N N 170 
ILE C   O    doub N N 171 
ILE C   OXT  sing N N 172 
ILE CB  CG1  sing N N 173 
ILE CB  CG2  sing N N 174 
ILE CB  HB   sing N N 175 
ILE CG1 CD1  sing N N 176 
ILE CG1 HG12 sing N N 177 
ILE CG1 HG13 sing N N 178 
ILE CG2 HG21 sing N N 179 
ILE CG2 HG22 sing N N 180 
ILE CG2 HG23 sing N N 181 
ILE CD1 HD11 sing N N 182 
ILE CD1 HD12 sing N N 183 
ILE CD1 HD13 sing N N 184 
ILE OXT HXT  sing N N 185 
LEU N   CA   sing N N 186 
LEU N   H    sing N N 187 
LEU N   H2   sing N N 188 
LEU CA  C    sing N N 189 
LEU CA  CB   sing N N 190 
LEU CA  HA   sing N N 191 
LEU C   O    doub N N 192 
LEU C   OXT  sing N N 193 
LEU CB  CG   sing N N 194 
LEU CB  HB2  sing N N 195 
LEU CB  HB3  sing N N 196 
LEU CG  CD1  sing N N 197 
LEU CG  CD2  sing N N 198 
LEU CG  HG   sing N N 199 
LEU CD1 HD11 sing N N 200 
LEU CD1 HD12 sing N N 201 
LEU CD1 HD13 sing N N 202 
LEU CD2 HD21 sing N N 203 
LEU CD2 HD22 sing N N 204 
LEU CD2 HD23 sing N N 205 
LEU OXT HXT  sing N N 206 
LYS N   CA   sing N N 207 
LYS N   H    sing N N 208 
LYS N   H2   sing N N 209 
LYS CA  C    sing N N 210 
LYS CA  CB   sing N N 211 
LYS CA  HA   sing N N 212 
LYS C   O    doub N N 213 
LYS C   OXT  sing N N 214 
LYS CB  CG   sing N N 215 
LYS CB  HB2  sing N N 216 
LYS CB  HB3  sing N N 217 
LYS CG  CD   sing N N 218 
LYS CG  HG2  sing N N 219 
LYS CG  HG3  sing N N 220 
LYS CD  CE   sing N N 221 
LYS CD  HD2  sing N N 222 
LYS CD  HD3  sing N N 223 
LYS CE  NZ   sing N N 224 
LYS CE  HE2  sing N N 225 
LYS CE  HE3  sing N N 226 
LYS NZ  HZ1  sing N N 227 
LYS NZ  HZ2  sing N N 228 
LYS NZ  HZ3  sing N N 229 
LYS OXT HXT  sing N N 230 
MET N   CA   sing N N 231 
MET N   H    sing N N 232 
MET N   H2   sing N N 233 
MET CA  C    sing N N 234 
MET CA  CB   sing N N 235 
MET CA  HA   sing N N 236 
MET C   O    doub N N 237 
MET C   OXT  sing N N 238 
MET CB  CG   sing N N 239 
MET CB  HB2  sing N N 240 
MET CB  HB3  sing N N 241 
MET CG  SD   sing N N 242 
MET CG  HG2  sing N N 243 
MET CG  HG3  sing N N 244 
MET SD  CE   sing N N 245 
MET CE  HE1  sing N N 246 
MET CE  HE2  sing N N 247 
MET CE  HE3  sing N N 248 
MET OXT HXT  sing N N 249 
PHE N   CA   sing N N 250 
PHE N   H    sing N N 251 
PHE N   H2   sing N N 252 
PHE CA  C    sing N N 253 
PHE CA  CB   sing N N 254 
PHE CA  HA   sing N N 255 
PHE C   O    doub N N 256 
PHE C   OXT  sing N N 257 
PHE CB  CG   sing N N 258 
PHE CB  HB2  sing N N 259 
PHE CB  HB3  sing N N 260 
PHE CG  CD1  doub Y N 261 
PHE CG  CD2  sing Y N 262 
PHE CD1 CE1  sing Y N 263 
PHE CD1 HD1  sing N N 264 
PHE CD2 CE2  doub Y N 265 
PHE CD2 HD2  sing N N 266 
PHE CE1 CZ   doub Y N 267 
PHE CE1 HE1  sing N N 268 
PHE CE2 CZ   sing Y N 269 
PHE CE2 HE2  sing N N 270 
PHE CZ  HZ   sing N N 271 
PHE OXT HXT  sing N N 272 
PRO N   CA   sing N N 273 
PRO N   CD   sing N N 274 
PRO N   H    sing N N 275 
PRO CA  C    sing N N 276 
PRO CA  CB   sing N N 277 
PRO CA  HA   sing N N 278 
PRO C   O    doub N N 279 
PRO C   OXT  sing N N 280 
PRO CB  CG   sing N N 281 
PRO CB  HB2  sing N N 282 
PRO CB  HB3  sing N N 283 
PRO CG  CD   sing N N 284 
PRO CG  HG2  sing N N 285 
PRO CG  HG3  sing N N 286 
PRO CD  HD2  sing N N 287 
PRO CD  HD3  sing N N 288 
PRO OXT HXT  sing N N 289 
SER N   CA   sing N N 290 
SER N   H    sing N N 291 
SER N   H2   sing N N 292 
SER CA  C    sing N N 293 
SER CA  CB   sing N N 294 
SER CA  HA   sing N N 295 
SER C   O    doub N N 296 
SER C   OXT  sing N N 297 
SER CB  OG   sing N N 298 
SER CB  HB2  sing N N 299 
SER CB  HB3  sing N N 300 
SER OG  HG   sing N N 301 
SER OXT HXT  sing N N 302 
THR N   CA   sing N N 303 
THR N   H    sing N N 304 
THR N   H2   sing N N 305 
THR CA  C    sing N N 306 
THR CA  CB   sing N N 307 
THR CA  HA   sing N N 308 
THR C   O    doub N N 309 
THR C   OXT  sing N N 310 
THR CB  OG1  sing N N 311 
THR CB  CG2  sing N N 312 
THR CB  HB   sing N N 313 
THR OG1 HG1  sing N N 314 
THR CG2 HG21 sing N N 315 
THR CG2 HG22 sing N N 316 
THR CG2 HG23 sing N N 317 
THR OXT HXT  sing N N 318 
TRP N   CA   sing N N 319 
TRP N   H    sing N N 320 
TRP N   H2   sing N N 321 
TRP CA  C    sing N N 322 
TRP CA  CB   sing N N 323 
TRP CA  HA   sing N N 324 
TRP C   O    doub N N 325 
TRP C   OXT  sing N N 326 
TRP CB  CG   sing N N 327 
TRP CB  HB2  sing N N 328 
TRP CB  HB3  sing N N 329 
TRP CG  CD1  doub Y N 330 
TRP CG  CD2  sing Y N 331 
TRP CD1 NE1  sing Y N 332 
TRP CD1 HD1  sing N N 333 
TRP CD2 CE2  doub Y N 334 
TRP CD2 CE3  sing Y N 335 
TRP NE1 CE2  sing Y N 336 
TRP NE1 HE1  sing N N 337 
TRP CE2 CZ2  sing Y N 338 
TRP CE3 CZ3  doub Y N 339 
TRP CE3 HE3  sing N N 340 
TRP CZ2 CH2  doub Y N 341 
TRP CZ2 HZ2  sing N N 342 
TRP CZ3 CH2  sing Y N 343 
TRP CZ3 HZ3  sing N N 344 
TRP CH2 HH2  sing N N 345 
TRP OXT HXT  sing N N 346 
TYR N   CA   sing N N 347 
TYR N   H    sing N N 348 
TYR N   H2   sing N N 349 
TYR CA  C    sing N N 350 
TYR CA  CB   sing N N 351 
TYR CA  HA   sing N N 352 
TYR C   O    doub N N 353 
TYR C   OXT  sing N N 354 
TYR CB  CG   sing N N 355 
TYR CB  HB2  sing N N 356 
TYR CB  HB3  sing N N 357 
TYR CG  CD1  doub Y N 358 
TYR CG  CD2  sing Y N 359 
TYR CD1 CE1  sing Y N 360 
TYR CD1 HD1  sing N N 361 
TYR CD2 CE2  doub Y N 362 
TYR CD2 HD2  sing N N 363 
TYR CE1 CZ   doub Y N 364 
TYR CE1 HE1  sing N N 365 
TYR CE2 CZ   sing Y N 366 
TYR CE2 HE2  sing N N 367 
TYR CZ  OH   sing N N 368 
TYR OH  HH   sing N N 369 
TYR OXT HXT  sing N N 370 
VAL N   CA   sing N N 371 
VAL N   H    sing N N 372 
VAL N   H2   sing N N 373 
VAL CA  C    sing N N 374 
VAL CA  CB   sing N N 375 
VAL CA  HA   sing N N 376 
VAL C   O    doub N N 377 
VAL C   OXT  sing N N 378 
VAL CB  CG1  sing N N 379 
VAL CB  CG2  sing N N 380 
VAL CB  HB   sing N N 381 
VAL CG1 HG11 sing N N 382 
VAL CG1 HG12 sing N N 383 
VAL CG1 HG13 sing N N 384 
VAL CG2 HG21 sing N N 385 
VAL CG2 HG22 sing N N 386 
VAL CG2 HG23 sing N N 387 
VAL OXT HXT  sing N N 388 
# 
_pdbx_audit_support.funding_organization   'Science and Engineering Research Board (SERB)' 
_pdbx_audit_support.country                India 
_pdbx_audit_support.grant_number           CRG/2019/000432 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   8WG6 
_pdbx_initial_refinement_model.details          'SeMet derivative of same protein' 
# 
_atom_sites.entry_id                    8WGG 
_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]   0.027092 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   -0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.017056 
_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]   0.004695 
_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  
NA 
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   . THR A 1 26  ? 45.263 34.274 4.450   1.00 30.00 ? 28   THR A N   1 
ATOM   2    C  CA  . THR A 1 26  ? 43.845 34.081 4.804   1.00 30.00 ? 28   THR A CA  1 
ATOM   3    C  C   . THR A 1 26  ? 43.572 34.728 6.172   1.00 30.00 ? 28   THR A C   1 
ATOM   4    O  O   . THR A 1 26  ? 44.473 35.311 6.745   1.00 30.00 ? 28   THR A O   1 
ATOM   5    C  CB  . THR A 1 26  ? 43.542 32.591 4.962   1.00 30.00 ? 28   THR A CB  1 
ATOM   6    O  OG1 . THR A 1 26  ? 44.616 32.069 5.743   1.00 30.00 ? 28   THR A OG1 1 
ATOM   7    C  CG2 . THR A 1 26  ? 43.372 31.852 3.656   1.00 30.00 ? 28   THR A CG2 1 
ATOM   8    N  N   . THR A 1 27  ? 42.343 34.668 6.620   1.00 18.59 ? 29   THR A N   1 
ATOM   9    C  CA  . THR A 1 27  ? 41.990 35.258 7.934   1.00 18.00 ? 29   THR A CA  1 
ATOM   10   C  C   . THR A 1 27  ? 41.749 34.108 8.913   1.00 16.57 ? 29   THR A C   1 
ATOM   11   O  O   . THR A 1 27  ? 41.282 33.093 8.474   1.00 15.93 ? 29   THR A O   1 
ATOM   12   C  CB  . THR A 1 27  ? 40.720 36.109 7.839   1.00 17.67 ? 29   THR A CB  1 
ATOM   13   O  OG1 . THR A 1 27  ? 40.836 36.951 6.708   1.00 19.22 ? 29   THR A OG1 1 
ATOM   14   C  CG2 . THR A 1 27  ? 40.506 36.990 9.047   1.00 17.65 ? 29   THR A CG2 1 
ATOM   15   N  N   . THR A 1 28  ? 42.092 34.321 10.177  1.00 15.98 ? 30   THR A N   1 
ATOM   16   C  CA  . THR A 1 28  ? 41.881 33.341 11.263  1.00 14.69 ? 30   THR A CA  1 
ATOM   17   C  C   . THR A 1 28  ? 41.153 34.071 12.393  1.00 14.12 ? 30   THR A C   1 
ATOM   18   O  O   . THR A 1 28  ? 41.169 35.267 12.434  1.00 14.60 ? 30   THR A O   1 
ATOM   19   C  CB  . THR A 1 28  ? 43.176 32.656 11.711  1.00 15.33 ? 30   THR A CB  1 
ATOM   20   O  OG1 . THR A 1 28  ? 44.086 33.562 12.321  1.00 15.89 ? 30   THR A OG1 1 
ATOM   21   C  CG2 . THR A 1 28  ? 43.846 31.876 10.598  1.00 16.41 ? 30   THR A CG2 1 
ATOM   22   N  N   . TYR A 1 29  ? 40.492 33.319 13.240  1.00 13.33 ? 31   TYR A N   1 
ATOM   23   C  CA  . TYR A 1 29  ? 39.681 33.881 14.307  1.00 13.29 ? 31   TYR A CA  1 
ATOM   24   C  C   . TYR A 1 29  ? 39.971 33.183 15.623  1.00 13.12 ? 31   TYR A C   1 
ATOM   25   O  O   . TYR A 1 29  ? 40.619 32.131 15.671  1.00 12.72 ? 31   TYR A O   1 
ATOM   26   C  CB  . TYR A 1 29  ? 38.211 33.741 13.919  1.00 12.74 ? 31   TYR A CB  1 
ATOM   27   C  CG  . TYR A 1 29  ? 37.848 34.667 12.772  1.00 13.29 ? 31   TYR A CG  1 
ATOM   28   C  CD1 . TYR A 1 29  ? 37.616 36.020 12.998  1.00 14.07 ? 31   TYR A CD1 1 
ATOM   29   C  CD2 . TYR A 1 29  ? 37.820 34.211 11.461  1.00 13.60 ? 31   TYR A CD2 1 
ATOM   30   C  CE1 . TYR A 1 29  ? 37.320 36.875 11.952  1.00 15.00 ? 31   TYR A CE1 1 
ATOM   31   C  CE2 . TYR A 1 29  ? 37.543 35.059 10.410  1.00 14.28 ? 31   TYR A CE2 1 
ATOM   32   C  CZ  . TYR A 1 29  ? 37.288 36.392 10.658  1.00 15.10 ? 31   TYR A CZ  1 
ATOM   33   O  OH  . TYR A 1 29  ? 36.992 37.185 9.595   1.00 16.21 ? 31   TYR A OH  1 
ATOM   34   N  N   . THR A 1 30  ? 39.487 33.828 16.686  1.00 13.50 ? 32   THR A N   1 
ATOM   35   C  CA  . THR A 1 30  ? 39.691 33.385 18.050  1.00 13.87 ? 32   THR A CA  1 
ATOM   36   C  C   . THR A 1 30  ? 38.335 33.115 18.688  1.00 13.33 ? 32   THR A C   1 
ATOM   37   O  O   . THR A 1 30  ? 37.402 33.893 18.516  1.00 13.43 ? 32   THR A O   1 
ATOM   38   C  CB  . THR A 1 30  ? 40.498 34.440 18.827  1.00 15.26 ? 32   THR A CB  1 
ATOM   39   O  OG1 . THR A 1 30  ? 41.800 34.551 18.246  1.00 16.27 ? 32   THR A OG1 1 
ATOM   40   C  CG2 . THR A 1 30  ? 40.671 34.113 20.288  1.00 15.58 ? 32   THR A CG2 1 
ATOM   41   N  N   . ILE A 1 31  ? 38.250 32.022 19.445  1.00 13.05 ? 33   ILE A N   1 
ATOM   42   C  CA  . ILE A 1 31  ? 37.173 31.840 20.405  1.00 12.94 ? 33   ILE A CA  1 
ATOM   43   C  C   . ILE A 1 31  ? 37.802 31.803 21.793  1.00 13.72 ? 33   ILE A C   1 
ATOM   44   O  O   . ILE A 1 31  ? 38.727 31.036 22.029  1.00 14.20 ? 33   ILE A O   1 
ATOM   45   C  CB  . ILE A 1 31  ? 36.351 30.561 20.122  1.00 12.40 ? 33   ILE A CB  1 
ATOM   46   C  CG1 . ILE A 1 31  ? 35.670 30.603 18.754  1.00 12.12 ? 33   ILE A CG1 1 
ATOM   47   C  CG2 . ILE A 1 31  ? 35.343 30.309 21.255  1.00 12.11 ? 33   ILE A CG2 1 
ATOM   48   C  CD1 . ILE A 1 31  ? 35.125 29.279 18.300  1.00 12.14 ? 33   ILE A CD1 1 
ATOM   49   N  N   . GLN A 1 32  ? 37.312 32.657 22.687  1.00 14.57 ? 34   GLN A N   1 
ATOM   50   C  CA  . GLN A 1 32  ? 37.731 32.646 24.074  1.00 15.86 ? 34   GLN A CA  1 
ATOM   51   C  C   . GLN A 1 32  ? 36.565 32.148 24.919  1.00 14.82 ? 34   GLN A C   1 
ATOM   52   O  O   . GLN A 1 32  ? 35.477 32.707 24.888  1.00 14.30 ? 34   GLN A O   1 
ATOM   53   C  CB  . GLN A 1 32  ? 38.190 34.036 24.512  1.00 18.32 ? 34   GLN A CB  1 
ATOM   54   C  CG  . GLN A 1 32  ? 38.657 34.051 25.953  1.00 21.38 ? 34   GLN A CG  1 
ATOM   55   C  CD  . GLN A 1 32  ? 39.210 35.378 26.393  1.00 25.34 ? 34   GLN A CD  1 
ATOM   56   O  OE1 . GLN A 1 32  ? 38.601 36.064 27.203  1.00 29.82 ? 34   GLN A OE1 1 
ATOM   57   N  NE2 . GLN A 1 32  ? 40.379 35.734 25.883  1.00 27.60 ? 34   GLN A NE2 1 
ATOM   58   N  N   . LEU A 1 33  ? 36.809 31.087 25.692  1.00 14.49 ? 35   LEU A N   1 
ATOM   59   C  CA  . LEU A 1 33  ? 35.785 30.499 26.535  1.00 14.49 ? 35   LEU A CA  1 
ATOM   60   C  C   . LEU A 1 33  ? 36.018 30.909 27.982  1.00 14.49 ? 35   LEU A C   1 
ATOM   61   O  O   . LEU A 1 33  ? 37.094 30.677 28.503  1.00 14.75 ? 35   LEU A O   1 
ATOM   62   C  CB  . LEU A 1 33  ? 35.882 28.981 26.394  1.00 14.76 ? 35   LEU A CB  1 
ATOM   63   C  CG  . LEU A 1 33  ? 35.500 28.424 25.027  1.00 14.84 ? 35   LEU A CG  1 
ATOM   64   C  CD1 . LEU A 1 33  ? 35.979 26.989 24.851  1.00 15.36 ? 35   LEU A CD1 1 
ATOM   65   C  CD2 . LEU A 1 33  ? 34.002 28.506 24.857  1.00 15.28 ? 35   LEU A CD2 1 
ATOM   66   N  N   . THR A 1 34  ? 35.015 31.516 28.612  1.00 14.86 ? 36   THR A N   1 
ATOM   67   C  CA  . THR A 1 34  ? 35.126 31.940 29.996  1.00 16.21 ? 36   THR A CA  1 
ATOM   68   C  C   . THR A 1 34  ? 34.367 30.959 30.876  1.00 15.54 ? 36   THR A C   1 
ATOM   69   O  O   . THR A 1 34  ? 33.521 30.224 30.381  1.00 14.24 ? 36   THR A O   1 
ATOM   70   C  CB  . THR A 1 34  ? 34.556 33.349 30.205  1.00 18.43 ? 36   THR A CB  1 
ATOM   71   O  OG1 . THR A 1 34  ? 33.173 33.331 29.832  1.00 18.82 ? 36   THR A OG1 1 
ATOM   72   C  CG2 . THR A 1 34  ? 35.305 34.373 29.389  1.00 19.53 ? 36   THR A CG2 1 
ATOM   73   N  N   . GLY A 1 35  ? 34.696 30.956 32.170  1.00 15.83 ? 37   GLY A N   1 
ATOM   74   C  CA  . GLY A 1 35  ? 34.121 30.040 33.139  1.00 16.23 ? 37   GLY A CA  1 
ATOM   75   C  C   . GLY A 1 35  ? 34.645 28.607 32.983  1.00 15.38 ? 37   GLY A C   1 
ATOM   76   O  O   . GLY A 1 35  ? 33.942 27.661 33.336  1.00 15.09 ? 37   GLY A O   1 
ATOM   77   N  N   . THR A 1 36  ? 35.851 28.452 32.414  1.00 14.91 ? 38   THR A N   1 
ATOM   78   C  CA  . THR A 1 36  ? 36.437 27.141 32.163  1.00 14.47 ? 38   THR A CA  1 
ATOM   79   C  C   . THR A 1 36  ? 37.217 26.685 33.390  1.00 15.71 ? 38   THR A C   1 
ATOM   80   O  O   . THR A 1 36  ? 37.543 27.480 34.270  1.00 16.26 ? 38   THR A O   1 
ATOM   81   C  CB  . THR A 1 36  ? 37.354 27.164 30.936  1.00 14.01 ? 38   THR A CB  1 
ATOM   82   O  OG1 . THR A 1 36  ? 38.363 28.155 31.121  1.00 14.75 ? 38   THR A OG1 1 
ATOM   83   C  CG2 . THR A 1 36  ? 36.604 27.480 29.660  1.00 13.28 ? 38   THR A CG2 1 
ATOM   84   N  N   . SER A 1 37  ? 37.484 25.383 33.426  1.00 16.23 ? 39   SER A N   1 
ATOM   85   C  CA  . SER A 1 37  ? 38.187 24.757 34.527  1.00 17.72 ? 39   SER A CA  1 
ATOM   86   C  C   . SER A 1 37  ? 39.405 24.047 33.963  1.00 17.38 ? 39   SER A C   1 
ATOM   87   O  O   . SER A 1 37  ? 39.350 23.524 32.851  1.00 16.55 ? 39   SER A O   1 
ATOM   88   C  CB  . SER A 1 37  ? 37.290 23.779 35.257  1.00 18.95 ? 39   SER A CB  1 
ATOM   89   O  OG  . SER A 1 37  ? 36.097 24.401 35.690  1.00 20.52 ? 39   SER A OG  1 
ATOM   90   N  N   . SER A 1 38  ? 40.478 23.998 34.761  1.00 18.29 ? 40   SER A N   1 
ATOM   91   C  CA  . SER A 1 38  ? 41.651 23.207 34.427  1.00 18.65 ? 40   SER A CA  1 
ATOM   92   C  C   . SER A 1 38  ? 41.265 21.733 34.370  1.00 18.02 ? 40   SER A C   1 
ATOM   93   O  O   . SER A 1 38  ? 40.347 21.295 35.058  1.00 18.00 ? 40   SER A O   1 
ATOM   94   C  CB  . SER A 1 38  ? 42.759 23.446 35.423  1.00 20.31 ? 40   SER A CB  1 
ATOM   95   O  OG  . SER A 1 38  ? 42.365 23.004 36.718  1.00 21.82 ? 40   SER A OG  1 
ATOM   96   N  N   . GLY A 1 39  ? 42.002 20.949 33.584  1.00 17.84 ? 41   GLY A N   1 
ATOM   97   C  CA  . GLY A 1 39  ? 41.841 19.504 33.617  1.00 17.99 ? 41   GLY A CA  1 
ATOM   98   C  C   . GLY A 1 39  ? 40.844 19.020 32.568  1.00 17.03 ? 41   GLY A C   1 
ATOM   99   O  O   . GLY A 1 39  ? 40.380 17.888 32.618  1.00 17.13 ? 41   GLY A O   1 
ATOM   100  N  N   . HIS A 1 40  ? 40.520 19.888 31.606  1.00 15.98 ? 42   HIS A N   1 
ATOM   101  C  CA  . HIS A 1 40  ? 39.625 19.523 30.531  1.00 15.13 ? 42   HIS A CA  1 
ATOM   102  C  C   . HIS A 1 40  ? 40.397 19.574 29.221  1.00 14.96 ? 42   HIS A C   1 
ATOM   103  O  O   . HIS A 1 40  ? 41.408 20.267 29.108  1.00 15.01 ? 42   HIS A O   1 
ATOM   104  C  CB  . HIS A 1 40  ? 38.439 20.487 30.456  1.00 14.56 ? 42   HIS A CB  1 
ATOM   105  C  CG  . HIS A 1 40  ? 37.490 20.374 31.587  1.00 15.00 ? 42   HIS A CG  1 
ATOM   106  N  ND1 . HIS A 1 40  ? 36.175 20.008 31.423  1.00 14.65 ? 42   HIS A ND1 1 
ATOM   107  C  CD2 . HIS A 1 40  ? 37.654 20.599 32.878  1.00 15.95 ? 42   HIS A CD2 1 
ATOM   108  C  CE1 . HIS A 1 40  ? 35.574 20.019 32.590  1.00 15.48 ? 42   HIS A CE1 1 
ATOM   109  N  NE2 . HIS A 1 40  ? 36.463 20.361 33.500  1.00 16.35 ? 42   HIS A NE2 1 
ATOM   110  N  N   . VAL A 1 41  ? 39.891 18.825 28.247  1.00 14.74 ? 43   VAL A N   1 
ATOM   111  C  CA  . VAL A 1 41  ? 40.384 18.911 26.890  1.00 15.53 ? 43   VAL A CA  1 
ATOM   112  C  C   . VAL A 1 41  ? 39.185 19.239 26.020  1.00 14.72 ? 43   VAL A C   1 
ATOM   113  O  O   . VAL A 1 41  ? 38.292 18.414 25.867  1.00 14.92 ? 43   VAL A O   1 
ATOM   114  C  CB  . VAL A 1 41  ? 41.079 17.624 26.417  1.00 16.68 ? 43   VAL A CB  1 
ATOM   115  C  CG1 . VAL A 1 41  ? 41.426 17.695 24.946  1.00 16.65 ? 43   VAL A CG1 1 
ATOM   116  C  CG2 . VAL A 1 41  ? 42.311 17.313 27.261  1.00 18.25 ? 43   VAL A CG2 1 
ATOM   117  N  N   . TYR A 1 42  ? 39.156 20.466 25.518  1.00 14.75 ? 44   TYR A N   1 
ATOM   118  C  CA  . TYR A 1 42  ? 38.052 20.901 24.678  1.00 14.75 ? 44   TYR A CA  1 
ATOM   119  C  C   . TYR A 1 42  ? 38.377 20.588 23.223  1.00 14.66 ? 44   TYR A C   1 
ATOM   120  O  O   . TYR A 1 42  ? 39.509 20.768 22.788  1.00 14.80 ? 44   TYR A O   1 
ATOM   121  C  CB  . TYR A 1 42  ? 37.786 22.393 24.844  1.00 14.79 ? 44   TYR A CB  1 
ATOM   122  C  CG  . TYR A 1 42  ? 37.460 22.805 26.270  1.00 15.95 ? 44   TYR A CG  1 
ATOM   123  C  CD1 . TYR A 1 42  ? 36.424 22.204 26.980  1.00 17.12 ? 44   TYR A CD1 1 
ATOM   124  C  CD2 . TYR A 1 42  ? 38.182 23.813 26.897  1.00 17.09 ? 44   TYR A CD2 1 
ATOM   125  C  CE1 . TYR A 1 42  ? 36.124 22.597 28.276  1.00 17.17 ? 44   TYR A CE1 1 
ATOM   126  C  CE2 . TYR A 1 42  ? 37.882 24.215 28.185  1.00 17.63 ? 44   TYR A CE2 1 
ATOM   127  C  CZ  . TYR A 1 42  ? 36.850 23.605 28.876  1.00 17.82 ? 44   TYR A CZ  1 
ATOM   128  O  OH  . TYR A 1 42  ? 36.573 24.024 30.154  1.00 19.73 ? 44   TYR A OH  1 
ATOM   129  N  N   . GLU A 1 43  ? 37.350 20.178 22.480  1.00 14.75 ? 45   GLU A N   1 
ATOM   130  C  CA  . GLU A 1 43  ? 37.471 19.886 21.057  1.00 15.04 ? 45   GLU A CA  1 
ATOM   131  C  C   . GLU A 1 43  ? 36.558 20.817 20.261  1.00 14.09 ? 45   GLU A C   1 
ATOM   132  O  O   . GLU A 1 43  ? 35.369 20.952 20.561  1.00 13.35 ? 45   GLU A O   1 
ATOM   133  C  CB  . GLU A 1 43  ? 37.108 18.428 20.792  1.00 16.22 ? 45   GLU A CB  1 
ATOM   134  C  CG  . GLU A 1 43  ? 37.903 17.472 21.657  1.00 17.59 ? 45   GLU A CG  1 
ATOM   135  C  CD  . GLU A 1 43  ? 37.764 16.016 21.267  1.00 18.90 ? 45   GLU A CD  1 
ATOM   136  O  OE1 . GLU A 1 43  ? 36.626 15.590 21.011  1.00 19.05 ? 45   GLU A OE1 1 
ATOM   137  O  OE2 . GLU A 1 43  ? 38.796 15.327 21.228  1.00 20.64 ? 45   GLU A OE2 1 
ATOM   138  N  N   . LEU A 1 44  ? 37.150 21.428 19.227  1.00 13.35 ? 46   LEU A N   1 
ATOM   139  C  CA  . LEU A 1 44  ? 36.426 22.289 18.312  1.00 12.68 ? 46   LEU A CA  1 
ATOM   140  C  C   . LEU A 1 44  ? 36.409 21.613 16.946  1.00 12.21 ? 46   LEU A C   1 
ATOM   141  O  O   . LEU A 1 44  ? 37.465 21.302 16.413  1.00 12.35 ? 46   LEU A O   1 
ATOM   142  C  CB  . LEU A 1 44  ? 37.130 23.649 18.226  1.00 13.03 ? 46   LEU A CB  1 
ATOM   143  C  CG  . LEU A 1 44  ? 37.082 24.526 19.481  1.00 14.02 ? 46   LEU A CG  1 
ATOM   144  C  CD1 . LEU A 1 44  ? 38.105 24.074 20.513  1.00 14.76 ? 46   LEU A CD1 1 
ATOM   145  C  CD2 . LEU A 1 44  ? 37.314 25.992 19.126  1.00 14.26 ? 46   LEU A CD2 1 
ATOM   146  N  N   . TYR A 1 45  ? 35.201 21.371 16.418  1.00 11.55 ? 47   TYR A N   1 
ATOM   147  C  CA  . TYR A 1 45  ? 35.031 20.747 15.111  1.00 11.81 ? 47   TYR A CA  1 
ATOM   148  C  C   . TYR A 1 45  ? 34.522 21.785 14.112  1.00 11.42 ? 47   TYR A C   1 
ATOM   149  O  O   . TYR A 1 45  ? 33.517 22.443 14.332  1.00 10.91 ? 47   TYR A O   1 
ATOM   150  C  CB  . TYR A 1 45  ? 34.085 19.538 15.197  1.00 12.54 ? 47   TYR A CB  1 
ATOM   151  C  CG  . TYR A 1 45  ? 34.620 18.395 16.052  1.00 12.90 ? 47   TYR A CG  1 
ATOM   152  C  CD1 . TYR A 1 45  ? 34.519 18.407 17.439  1.00 12.34 ? 47   TYR A CD1 1 
ATOM   153  C  CD2 . TYR A 1 45  ? 35.285 17.335 15.458  1.00 14.18 ? 47   TYR A CD2 1 
ATOM   154  C  CE1 . TYR A 1 45  ? 35.051 17.375 18.206  1.00 13.06 ? 47   TYR A CE1 1 
ATOM   155  C  CE2 . TYR A 1 45  ? 35.805 16.294 16.202  1.00 14.46 ? 47   TYR A CE2 1 
ATOM   156  C  CZ  . TYR A 1 45  ? 35.691 16.321 17.581  1.00 14.08 ? 47   TYR A CZ  1 
ATOM   157  O  OH  . TYR A 1 45  ? 36.245 15.276 18.250  1.00 14.74 ? 47   TYR A OH  1 
ATOM   158  N  N   . HIS A 1 46  ? 35.204 21.886 12.974  1.00 11.84 ? 48   HIS A N   1 
ATOM   159  C  CA  . HIS A 1 46  ? 34.861 22.854 11.942  1.00 11.49 ? 48   HIS A CA  1 
ATOM   160  C  C   . HIS A 1 46  ? 33.639 22.356 11.171  1.00 11.55 ? 48   HIS A C   1 
ATOM   161  O  O   . HIS A 1 46  ? 33.726 21.417 10.396  1.00 12.51 ? 48   HIS A O   1 
ATOM   162  C  CB  . HIS A 1 46  ? 36.075 23.095 11.035  1.00 11.91 ? 48   HIS A CB  1 
ATOM   163  C  CG  . HIS A 1 46  ? 36.001 24.337 10.228  1.00 11.57 ? 48   HIS A CG  1 
ATOM   164  N  ND1 . HIS A 1 46  ? 36.763 24.518 9.086   1.00 12.49 ? 48   HIS A ND1 1 
ATOM   165  C  CD2 . HIS A 1 46  ? 35.224 25.419 10.339  1.00 10.97 ? 48   HIS A CD2 1 
ATOM   166  C  CE1 . HIS A 1 46  ? 36.486 25.711 8.574   1.00 12.17 ? 48   HIS A CE1 1 
ATOM   167  N  NE2 . HIS A 1 46  ? 35.553 26.274 9.319   1.00 11.41 ? 48   HIS A NE2 1 
ATOM   168  N  N   . ILE A 1 47  ? 32.481 22.969 11.402  1.00 11.07 ? 49   ILE A N   1 
ATOM   169  C  CA  . ILE A 1 47  ? 31.242 22.522 10.789  1.00 11.68 ? 49   ILE A CA  1 
ATOM   170  C  C   . ILE A 1 47  ? 31.081 23.194 9.429   1.00 12.31 ? 49   ILE A C   1 
ATOM   171  O  O   . ILE A 1 47  ? 30.874 22.504 8.430   1.00 13.43 ? 49   ILE A O   1 
ATOM   172  C  CB  . ILE A 1 47  ? 30.053 22.826 11.719  1.00 11.70 ? 49   ILE A CB  1 
ATOM   173  C  CG1 . ILE A 1 47  ? 30.265 22.239 13.120  1.00 11.23 ? 49   ILE A CG1 1 
ATOM   174  C  CG2 . ILE A 1 47  ? 28.752 22.347 11.108  1.00 12.80 ? 49   ILE A CG2 1 
ATOM   175  C  CD1 . ILE A 1 47  ? 30.594 20.765 13.123  1.00 11.76 ? 49   ILE A CD1 1 
ATOM   176  N  N   . PHE A 1 48  ? 31.117 24.532 9.409   1.00 11.86 ? 50   PHE A N   1 
ATOM   177  C  CA  . PHE A 1 48  ? 30.989 25.287 8.169   1.00 12.49 ? 50   PHE A CA  1 
ATOM   178  C  C   . PHE A 1 48  ? 32.239 26.134 7.941   1.00 12.64 ? 50   PHE A C   1 
ATOM   179  O  O   . PHE A 1 48  ? 32.721 26.812 8.846   1.00 11.71 ? 50   PHE A O   1 
ATOM   180  C  CB  . PHE A 1 48  ? 29.811 26.258 8.214   1.00 12.55 ? 50   PHE A CB  1 
ATOM   181  C  CG  . PHE A 1 48  ? 28.431 25.672 8.330   1.00 13.20 ? 50   PHE A CG  1 
ATOM   182  C  CD1 . PHE A 1 48  ? 28.041 24.614 7.538   1.00 14.24 ? 50   PHE A CD1 1 
ATOM   183  C  CD2 . PHE A 1 48  ? 27.495 26.250 9.169   1.00 13.30 ? 50   PHE A CD2 1 
ATOM   184  C  CE1 . PHE A 1 48  ? 26.753 24.110 7.620   1.00 15.37 ? 50   PHE A CE1 1 
ATOM   185  C  CE2 . PHE A 1 48  ? 26.205 25.749 9.248   1.00 14.38 ? 50   PHE A CE2 1 
ATOM   186  C  CZ  . PHE A 1 48  ? 25.835 24.679 8.474   1.00 15.39 ? 50   PHE A CZ  1 
ATOM   187  N  N   . SER A 1 49  ? 32.736 26.126 6.700   1.00 14.06 ? 51   SER A N   1 
ATOM   188  C  CA  . SER A 1 49  ? 33.700 27.127 6.278   1.00 14.62 ? 51   SER A CA  1 
ATOM   189  C  C   . SER A 1 49  ? 32.941 28.272 5.623   1.00 15.62 ? 51   SER A C   1 
ATOM   190  O  O   . SER A 1 49  ? 31.791 28.113 5.211   1.00 15.99 ? 51   SER A O   1 
ATOM   191  C  CB  . SER A 1 49  ? 34.715 26.533 5.341   1.00 15.57 ? 51   SER A CB  1 
ATOM   192  O  OG  . SER A 1 49  ? 34.066 26.078 4.165   1.00 16.43 ? 51   SER A OG  1 
ATOM   193  N  N   . GLY A 1 50  ? 33.606 29.422 5.513   1.00 15.98 ? 52   GLY A N   1 
ATOM   194  C  CA  . GLY A 1 50  ? 33.037 30.559 4.824   1.00 17.05 ? 52   GLY A CA  1 
ATOM   195  C  C   . GLY A 1 50  ? 33.838 31.824 5.101   1.00 17.57 ? 52   GLY A C   1 
ATOM   196  O  O   . GLY A 1 50  ? 34.947 31.768 5.622   1.00 17.85 ? 52   GLY A O   1 
ATOM   197  N  N   . ASP A 1 51  ? 33.258 32.965 4.724   1.00 18.51 ? 53   ASP A N   1 
ATOM   198  C  CA  . ASP A 1 51  ? 33.877 34.255 4.951   1.00 19.04 ? 53   ASP A CA  1 
ATOM   199  C  C   . ASP A 1 51  ? 33.003 35.041 5.920   1.00 18.16 ? 53   ASP A C   1 
ATOM   200  O  O   . ASP A 1 51  ? 31.806 35.168 5.690   1.00 18.55 ? 53   ASP A O   1 
ATOM   201  C  CB  . ASP A 1 51  ? 34.026 35.040 3.644   1.00 20.81 ? 53   ASP A CB  1 
ATOM   202  C  CG  . ASP A 1 51  ? 34.787 34.278 2.578   1.00 22.52 ? 53   ASP A CG  1 
ATOM   203  O  OD1 . ASP A 1 51  ? 35.923 33.831 2.875   1.00 23.20 ? 53   ASP A OD1 1 
ATOM   204  O  OD2 . ASP A 1 51  ? 34.233 34.138 1.447   1.00 24.51 ? 53   ASP A OD2 1 
ATOM   205  N  N   . LEU A 1 52  ? 33.630 35.599 6.957   1.00 17.81 ? 54   LEU A N   1 
ATOM   206  C  CA  . LEU A 1 52  ? 32.906 36.353 7.969   1.00 18.01 ? 54   LEU A CA  1 
ATOM   207  C  C   . LEU A 1 52  ? 33.086 37.842 7.717   1.00 19.11 ? 54   LEU A C   1 
ATOM   208  O  O   . LEU A 1 52  ? 34.217 38.302 7.593   1.00 19.52 ? 54   LEU A O   1 
ATOM   209  C  CB  . LEU A 1 52  ? 33.432 35.992 9.358   1.00 17.05 ? 54   LEU A CB  1 
ATOM   210  C  CG  . LEU A 1 52  ? 32.565 36.458 10.525  1.00 17.57 ? 54   LEU A CG  1 
ATOM   211  C  CD1 . LEU A 1 52  ? 31.400 35.497 10.735  1.00 17.54 ? 54   LEU A CD1 1 
ATOM   212  C  CD2 . LEU A 1 52  ? 33.398 36.564 11.804  1.00 17.30 ? 54   LEU A CD2 1 
ATOM   213  N  N   . ASP A 1 53  ? 31.972 38.582 7.701   1.00 19.98 ? 55   ASP A N   1 
ATOM   214  C  CA  . ASP A 1 53  ? 32.008 40.024 7.499   1.00 21.78 ? 55   ASP A CA  1 
ATOM   215  C  C   . ASP A 1 53  ? 31.988 40.725 8.857   1.00 21.63 ? 55   ASP A C   1 
ATOM   216  O  O   . ASP A 1 53  ? 32.052 40.068 9.892   1.00 20.59 ? 55   ASP A O   1 
ATOM   217  C  CB  . ASP A 1 53  ? 30.881 40.480 6.561   1.00 23.56 ? 55   ASP A CB  1 
ATOM   218  C  CG  . ASP A 1 53  ? 29.476 40.485 7.142   1.00 23.98 ? 55   ASP A CG  1 
ATOM   219  O  OD1 . ASP A 1 53  ? 29.291 39.943 8.236   1.00 23.80 ? 55   ASP A OD1 1 
ATOM   220  O  OD2 . ASP A 1 53  ? 28.575 41.053 6.460   1.00 25.33 ? 55   ASP A OD2 1 
ATOM   221  N  N   . ALA A 1 54  ? 31.884 42.055 8.837   1.00 23.21 ? 56   ALA A N   1 
ATOM   222  C  CA  . ALA A 1 54  ? 31.967 42.884 10.033  1.00 23.84 ? 56   ALA A CA  1 
ATOM   223  C  C   . ALA A 1 54  ? 30.702 42.774 10.881  1.00 23.96 ? 56   ALA A C   1 
ATOM   224  O  O   . ALA A 1 54  ? 30.733 43.143 12.047  1.00 23.93 ? 56   ALA A O   1 
ATOM   225  C  CB  . ALA A 1 54  ? 32.231 44.309 9.648   1.00 25.64 ? 56   ALA A CB  1 
ATOM   226  N  N   . ASN A 1 55  ? 29.606 42.258 10.302  1.00 24.11 ? 57   ASN A N   1 
ATOM   227  C  CA  . ASN A 1 55  ? 28.355 42.042 11.018  1.00 24.44 ? 57   ASN A CA  1 
ATOM   228  C  C   . ASN A 1 55  ? 28.201 40.588 11.444  1.00 22.15 ? 57   ASN A C   1 
ATOM   229  O  O   . ASN A 1 55  ? 27.118 40.188 11.841  1.00 22.81 ? 57   ASN A O   1 
ATOM   230  C  CB  . ASN A 1 55  ? 27.154 42.467 10.167  1.00 26.15 ? 57   ASN A CB  1 
ATOM   231  C  CG  . ASN A 1 55  ? 27.213 43.933 9.834   1.00 28.75 ? 57   ASN A CG  1 
ATOM   232  O  OD1 . ASN A 1 55  ? 27.224 44.314 8.669   1.00 30.53 ? 57   ASN A OD1 1 
ATOM   233  N  ND2 . ASN A 1 55  ? 27.233 44.761 10.860  1.00 30.30 ? 57   ASN A ND2 1 
ATOM   234  N  N   . ASN A 1 56  ? 29.286 39.812 11.356  1.00 20.81 ? 58   ASN A N   1 
ATOM   235  C  CA  . ASN A 1 56  ? 29.320 38.395 11.700  1.00 19.06 ? 58   ASN A CA  1 
ATOM   236  C  C   . ASN A 1 56  ? 28.336 37.578 10.870  1.00 19.57 ? 58   ASN A C   1 
ATOM   237  O  O   . ASN A 1 56  ? 27.763 36.611 11.368  1.00 18.74 ? 58   ASN A O   1 
ATOM   238  C  CB  . ASN A 1 56  ? 29.074 38.146 13.184  1.00 18.84 ? 58   ASN A CB  1 
ATOM   239  C  CG  . ASN A 1 56  ? 29.981 38.990 14.040  1.00 19.13 ? 58   ASN A CG  1 
ATOM   240  O  OD1 . ASN A 1 56  ? 29.494 39.697 14.925  1.00 21.64 ? 58   ASN A OD1 1 
ATOM   241  N  ND2 . ASN A 1 56  ? 31.281 38.919 13.800  1.00 18.03 ? 58   ASN A ND2 1 
ATOM   242  N  N   . VAL A 1 57  ? 28.204 37.948 9.598   1.00 20.19 ? 59   VAL A N   1 
ATOM   243  C  CA  . VAL A 1 57  ? 27.417 37.187 8.647   1.00 20.50 ? 59   VAL A CA  1 
ATOM   244  C  C   . VAL A 1 57  ? 28.375 36.305 7.863   1.00 19.59 ? 59   VAL A C   1 
ATOM   245  O  O   . VAL A 1 57  ? 29.440 36.772 7.463   1.00 20.11 ? 59   VAL A O   1 
ATOM   246  C  CB  . VAL A 1 57  ? 26.614 38.109 7.722   1.00 22.00 ? 59   VAL A CB  1 
ATOM   247  C  CG1 . VAL A 1 57  ? 25.854 37.312 6.666   1.00 22.52 ? 59   VAL A CG1 1 
ATOM   248  C  CG2 . VAL A 1 57  ? 25.670 39.003 8.520   1.00 23.45 ? 59   VAL A CG2 1 
ATOM   249  N  N   . LEU A 1 58  ? 27.966 35.054 7.622   1.00 18.98 ? 60   LEU A N   1 
ATOM   250  C  CA  . LEU A 1 58  ? 28.823 34.080 6.972   1.00 18.50 ? 60   LEU A CA  1 
ATOM   251  C  C   . LEU A 1 58  ? 28.361 33.816 5.541   1.00 18.56 ? 60   LEU A C   1 
ATOM   252  O  O   . LEU A 1 58  ? 27.231 33.384 5.318   1.00 18.00 ? 60   LEU A O   1 
ATOM   253  C  CB  . LEU A 1 58  ? 28.794 32.795 7.795   1.00 18.87 ? 60   LEU A CB  1 
ATOM   254  C  CG  . LEU A 1 58  ? 30.049 31.931 7.690   1.00 19.09 ? 60   LEU A CG  1 
ATOM   255  C  CD1 . LEU A 1 58  ? 31.190 32.566 8.472   1.00 18.91 ? 60   LEU A CD1 1 
ATOM   256  C  CD2 . LEU A 1 58  ? 29.766 30.541 8.215   1.00 19.22 ? 60   LEU A CD2 1 
ATOM   257  N  N   . THR A 1 59  ? 29.281 34.030 4.588   1.00 18.41 ? 61   THR A N   1 
ATOM   258  C  CA  . THR A 1 59  ? 29.004 33.815 3.177   1.00 19.26 ? 61   THR A CA  1 
ATOM   259  C  C   . THR A 1 59  ? 29.914 32.716 2.631   1.00 18.93 ? 61   THR A C   1 
ATOM   260  O  O   . THR A 1 59  ? 30.957 32.401 3.222   1.00 17.62 ? 61   THR A O   1 
ATOM   261  C  CB  . THR A 1 59  ? 29.187 35.121 2.381   1.00 20.37 ? 61   THR A CB  1 
ATOM   262  O  OG1 . THR A 1 59  ? 30.431 35.722 2.757   1.00 20.19 ? 61   THR A OG1 1 
ATOM   263  C  CG2 . THR A 1 59  ? 28.055 36.104 2.574   1.00 21.24 ? 61   THR A CG2 1 
ATOM   264  N  N   . ASN A 1 60  ? 29.493 32.158 1.485   1.00 20.27 ? 62   ASN A N   1 
ATOM   265  C  CA  . ASN A 1 60  ? 30.289 31.253 0.676   1.00 21.11 ? 62   ASN A CA  1 
ATOM   266  C  C   . ASN A 1 60  ? 30.567 29.977 1.457   1.00 20.26 ? 62   ASN A C   1 
ATOM   267  O  O   . ASN A 1 60  ? 31.722 29.552 1.547   1.00 19.77 ? 62   ASN A O   1 
ATOM   268  C  CB  . ASN A 1 60  ? 31.556 31.945 0.172   1.00 21.92 ? 62   ASN A CB  1 
ATOM   269  C  CG  . ASN A 1 60  ? 31.222 33.202 -0.604  1.00 23.30 ? 62   ASN A CG  1 
ATOM   270  O  OD1 . ASN A 1 60  ? 30.378 33.183 -1.504  1.00 25.12 ? 62   ASN A OD1 1 
ATOM   271  N  ND2 . ASN A 1 60  ? 31.904 34.285 -0.273  1.00 23.30 ? 62   ASN A ND2 1 
ATOM   272  N  N   . ILE A 1 61  ? 29.471 29.390 1.974   1.00 20.99 ? 63   ILE A N   1 
ATOM   273  C  CA  . ILE A 1 61  ? 29.504 28.355 3.002   1.00 19.65 ? 63   ILE A CA  1 
ATOM   274  C  C   . ILE A 1 61  ? 29.682 26.995 2.337   1.00 20.30 ? 63   ILE A C   1 
ATOM   275  O  O   . ILE A 1 61  ? 28.998 26.688 1.367   1.00 21.12 ? 63   ILE A O   1 
ATOM   276  C  CB  . ILE A 1 61  ? 28.230 28.406 3.880   1.00 19.76 ? 63   ILE A CB  1 
ATOM   277  C  CG1 . ILE A 1 61  ? 28.260 29.614 4.817   1.00 19.34 ? 63   ILE A CG1 1 
ATOM   278  C  CG2 . ILE A 1 61  ? 28.012 27.129 4.686   1.00 19.25 ? 63   ILE A CG2 1 
ATOM   279  C  CD1 . ILE A 1 61  ? 26.926 29.920 5.469   1.00 19.99 ? 63   ILE A CD1 1 
ATOM   280  N  N   . GLU A 1 62  ? 30.585 26.186 2.915   1.00 19.71 ? 64   GLU A N   1 
ATOM   281  C  CA  . GLU A 1 62  ? 30.749 24.788 2.558   1.00 20.35 ? 64   GLU A CA  1 
ATOM   282  C  C   . GLU A 1 62  ? 30.830 23.995 3.858   1.00 18.42 ? 64   GLU A C   1 
ATOM   283  O  O   . GLU A 1 62  ? 30.962 24.581 4.927   1.00 16.59 ? 64   GLU A O   1 
ATOM   284  C  CB  . GLU A 1 62  ? 32.034 24.558 1.750   1.00 22.35 ? 64   GLU A CB  1 
ATOM   285  C  CG  . GLU A 1 62  ? 32.198 25.418 0.504   1.00 25.09 ? 64   GLU A CG  1 
ATOM   286  C  CD  . GLU A 1 62  ? 31.248 25.113 -0.638  1.00 28.13 ? 64   GLU A CD  1 
ATOM   287  O  OE1 . GLU A 1 62  ? 30.422 24.158 -0.517  1.00 29.89 ? 64   GLU A OE1 1 
ATOM   288  O  OE2 . GLU A 1 62  ? 31.327 25.839 -1.641  1.00 31.75 ? 64   GLU A OE2 1 
ATOM   289  N  N   . TRP A 1 63  ? 30.790 22.667 3.744   1.00 18.42 ? 65   TRP A N   1 
ATOM   290  C  CA  . TRP A 1 63  ? 31.018 21.786 4.877   1.00 17.63 ? 65   TRP A CA  1 
ATOM   291  C  C   . TRP A 1 63  ? 32.493 21.829 5.265   1.00 17.28 ? 65   TRP A C   1 
ATOM   292  O  O   . TRP A 1 63  ? 33.381 21.677 4.432   1.00 17.64 ? 65   TRP A O   1 
ATOM   293  C  CB  . TRP A 1 63  ? 30.577 20.351 4.550   1.00 18.54 ? 65   TRP A CB  1 
ATOM   294  C  CG  . TRP A 1 63  ? 29.086 20.175 4.488   1.00 18.73 ? 65   TRP A CG  1 
ATOM   295  C  CD1 . TRP A 1 63  ? 28.326 19.875 3.401   1.00 20.08 ? 65   TRP A CD1 1 
ATOM   296  C  CD2 . TRP A 1 63  ? 28.173 20.291 5.597   1.00 17.99 ? 65   TRP A CD2 1 
ATOM   297  N  NE1 . TRP A 1 63  ? 27.004 19.801 3.746   1.00 20.66 ? 65   TRP A NE1 1 
ATOM   298  C  CE2 . TRP A 1 63  ? 26.880 20.064 5.088   1.00 19.17 ? 65   TRP A CE2 1 
ATOM   299  C  CE3 . TRP A 1 63  ? 28.324 20.579 6.962   1.00 16.52 ? 65   TRP A CE3 1 
ATOM   300  C  CZ2 . TRP A 1 63  ? 25.749 20.115 5.895   1.00 19.25 ? 65   TRP A CZ2 1 
ATOM   301  C  CZ3 . TRP A 1 63  ? 27.205 20.607 7.761   1.00 16.55 ? 65   TRP A CZ3 1 
ATOM   302  C  CH2 . TRP A 1 63  ? 25.934 20.386 7.234   1.00 18.15 ? 65   TRP A CH2 1 
ATOM   303  N  N   . GLY A 1 64  ? 32.751 22.034 6.556   1.00 16.25 ? 66   GLY A N   1 
ATOM   304  C  CA  . GLY A 1 64  ? 34.105 21.924 7.065   1.00 16.28 ? 66   GLY A CA  1 
ATOM   305  C  C   . GLY A 1 64  ? 34.496 20.468 7.268   1.00 16.77 ? 66   GLY A C   1 
ATOM   306  O  O   . GLY A 1 64  ? 33.663 19.574 7.167   1.00 17.72 ? 66   GLY A O   1 
ATOM   307  N  N   . ALA A 1 65  ? 35.781 20.251 7.528   1.00 17.14 ? 67   ALA A N   1 
ATOM   308  C  CA  . ALA A 1 65  ? 36.339 18.917 7.671   1.00 18.40 ? 67   ALA A CA  1 
ATOM   309  C  C   . ALA A 1 65  ? 35.863 18.244 8.962   1.00 18.25 ? 67   ALA A C   1 
ATOM   310  O  O   . ALA A 1 65  ? 36.051 17.049 9.144   1.00 19.26 ? 67   ALA A O   1 
ATOM   311  C  CB  . ALA A 1 65  ? 37.848 19.024 7.620   1.00 19.06 ? 67   ALA A CB  1 
ATOM   312  N  N   . GLY A 1 66  ? 35.254 19.016 9.864   1.00 16.87 ? 68   GLY A N   1 
ATOM   313  C  CA  . GLY A 1 66  ? 34.768 18.493 11.123  1.00 16.99 ? 68   GLY A CA  1 
ATOM   314  C  C   . GLY A 1 66  ? 33.560 17.587 10.953  1.00 17.94 ? 68   GLY A C   1 
ATOM   315  O  O   . GLY A 1 66  ? 33.296 16.786 11.839  1.00 19.21 ? 68   GLY A O   1 
ATOM   316  N  N   . VAL A 1 67  ? 32.838 17.699 9.837   1.00 18.02 ? 69   VAL A N   1 
ATOM   317  C  CA  . VAL A 1 67  ? 31.713 16.820 9.570   1.00 19.53 ? 69   VAL A CA  1 
ATOM   318  C  C   . VAL A 1 67  ? 32.191 15.713 8.625   1.00 21.82 ? 69   VAL A C   1 
ATOM   319  O  O   . VAL A 1 67  ? 32.738 15.991 7.559   1.00 22.53 ? 69   VAL A O   1 
ATOM   320  C  CB  . VAL A 1 67  ? 30.526 17.595 8.970   1.00 19.36 ? 69   VAL A CB  1 
ATOM   321  C  CG1 . VAL A 1 67  ? 29.284 16.725 8.830   1.00 20.68 ? 69   VAL A CG1 1 
ATOM   322  C  CG2 . VAL A 1 67  ? 30.221 18.855 9.775   1.00 17.73 ? 69   VAL A CG2 1 
ATOM   323  N  N   . ALA A 1 68  ? 32.001 14.461 9.042   1.00 23.24 ? 70   ALA A N   1 
ATOM   324  C  CA  . ALA A 1 68  ? 32.383 13.300 8.249   1.00 26.46 ? 70   ALA A CA  1 
ATOM   325  C  C   . ALA A 1 68  ? 31.675 13.354 6.894   1.00 28.26 ? 70   ALA A C   1 
ATOM   326  O  O   . ALA A 1 68  ? 30.481 13.627 6.829   1.00 28.33 ? 70   ALA A O   1 
ATOM   327  C  CB  . ALA A 1 68  ? 32.053 12.020 9.000   1.00 26.88 ? 70   ALA A CB  1 
ATOM   328  N  N   . ILE A 1 69  ? 32.416 13.044 5.829   1.00 31.02 ? 71   ILE A N   1 
ATOM   329  C  CA  . ILE A 1 69  ? 31.924 13.196 4.467   1.00 33.64 ? 71   ILE A CA  1 
ATOM   330  C  C   . ILE A 1 69  ? 30.682 12.333 4.247   1.00 34.93 ? 71   ILE A C   1 
ATOM   331  O  O   . ILE A 1 69  ? 29.761 12.749 3.552   1.00 35.99 ? 71   ILE A O   1 
ATOM   332  C  CB  . ILE A 1 69  ? 33.037 12.875 3.449   1.00 36.15 ? 71   ILE A CB  1 
ATOM   333  C  CG1 . ILE A 1 69  ? 34.248 13.795 3.638   1.00 35.98 ? 71   ILE A CG1 1 
ATOM   334  C  CG2 . ILE A 1 69  ? 32.508 12.958 2.023   1.00 37.05 ? 71   ILE A CG2 1 
ATOM   335  C  CD1 . ILE A 1 69  ? 35.559 13.179 3.214   1.00 37.54 ? 71   ILE A CD1 1 
ATOM   336  N  N   . GLY A 1 70  ? 30.671 11.140 4.839   1.00 36.08 ? 72   GLY A N   1 
ATOM   337  C  CA  . GLY A 1 70  ? 29.550 10.228 4.733   1.00 38.34 ? 72   GLY A CA  1 
ATOM   338  C  C   . GLY A 1 70  ? 28.251 10.814 5.281   1.00 38.40 ? 72   GLY A C   1 
ATOM   339  O  O   . GLY A 1 70  ? 27.175 10.501 4.783   1.00 38.73 ? 72   GLY A O   1 
ATOM   340  N  N   . ASP A 1 71  ? 28.349 11.669 6.309   1.00 36.93 ? 73   ASP A N   1 
ATOM   341  C  CA  . ASP A 1 71  ? 27.173 12.133 7.034   1.00 38.44 ? 73   ASP A CA  1 
ATOM   342  C  C   . ASP A 1 71  ? 26.650 13.464 6.502   1.00 37.66 ? 73   ASP A C   1 
ATOM   343  O  O   . ASP A 1 71  ? 25.581 13.902 6.930   1.00 38.96 ? 73   ASP A O   1 
ATOM   344  C  CB  . ASP A 1 71  ? 27.462 12.291 8.530   1.00 38.93 ? 73   ASP A CB  1 
ATOM   345  C  CG  . ASP A 1 71  ? 27.670 10.955 9.213   1.00 41.98 ? 73   ASP A CG  1 
ATOM   346  O  OD1 . ASP A 1 71  ? 26.748 10.113 9.103   1.00 45.55 ? 73   ASP A OD1 1 
ATOM   347  O  OD2 . ASP A 1 71  ? 28.767 10.747 9.788   1.00 41.35 ? 73   ASP A OD2 1 
ATOM   348  N  N   . ARG A 1 72  ? 27.403 14.090 5.585   1.00 35.93 ? 74   ARG A N   1 
ATOM   349  C  CA  . ARG A 1 72  ? 27.091 15.422 5.091   1.00 34.14 ? 74   ARG A CA  1 
ATOM   350  C  C   . ARG A 1 72  ? 25.794 15.390 4.303   1.00 36.33 ? 74   ARG A C   1 
ATOM   351  O  O   . ARG A 1 72  ? 24.948 16.257 4.477   1.00 35.16 ? 74   ARG A O   1 
ATOM   352  C  CB  . ARG A 1 72  ? 28.225 15.959 4.215   1.00 32.75 ? 74   ARG A CB  1 
ATOM   353  C  CG  . ARG A 1 72  ? 29.463 16.370 4.997   1.00 29.86 ? 74   ARG A CG  1 
ATOM   354  C  CD  . ARG A 1 72  ? 30.603 16.778 4.089   1.00 29.63 ? 74   ARG A CD  1 
ATOM   355  N  NE  . ARG A 1 72  ? 31.815 17.013 4.864   1.00 28.41 ? 74   ARG A NE  1 
ATOM   356  C  CZ  . ARG A 1 72  ? 32.963 17.418 4.342   1.00 28.47 ? 74   ARG A CZ  1 
ATOM   357  N  NH1 . ARG A 1 72  ? 33.041 17.612 3.038   1.00 29.89 ? 74   ARG A NH1 1 
ATOM   358  N  NH2 . ARG A 1 72  ? 34.028 17.603 5.104   1.00 27.81 ? 74   ARG A NH2 1 
ATOM   359  N  N   . ALA A 1 73  ? 25.647 14.365 3.457   1.00 39.80 ? 75   ALA A N   1 
ATOM   360  C  CA  . ALA A 1 73  ? 24.508 14.261 2.564   1.00 42.37 ? 75   ALA A CA  1 
ATOM   361  C  C   . ALA A 1 73  ? 23.193 14.155 3.344   1.00 42.50 ? 75   ALA A C   1 
ATOM   362  O  O   . ALA A 1 73  ? 22.139 14.506 2.821   1.00 43.58 ? 75   ALA A O   1 
ATOM   363  C  CB  . ALA A 1 73  ? 24.716 13.083 1.647   1.00 44.97 ? 75   ALA A CB  1 
ATOM   364  N  N   . LYS A 1 74  ? 23.241 13.692 4.597   1.00 42.15 ? 76   LYS A N   1 
ATOM   365  C  CA  . LYS A 1 74  ? 22.030 13.564 5.394   1.00 43.13 ? 76   LYS A CA  1 
ATOM   366  C  C   . LYS A 1 74  ? 21.568 14.941 5.898   1.00 41.29 ? 76   LYS A C   1 
ATOM   367  O  O   . LYS A 1 74  ? 20.399 15.100 6.245   1.00 43.79 ? 76   LYS A O   1 
ATOM   368  C  CB  . LYS A 1 74  ? 22.246 12.560 6.531   1.00 43.04 ? 76   LYS A CB  1 
ATOM   369  C  CG  . LYS A 1 74  ? 22.560 13.151 7.895   1.00 41.05 ? 76   LYS A CG  1 
ATOM   370  C  CD  . LYS A 1 74  ? 23.015 12.119 8.907   1.00 41.37 ? 76   LYS A CD  1 
ATOM   371  C  CE  . LYS A 1 74  ? 23.193 12.706 10.295  1.00 40.53 ? 76   LYS A CE  1 
ATOM   372  N  NZ  . LYS A 1 74  ? 23.888 11.786 11.240  1.00 40.38 ? 76   LYS A NZ  1 
ATOM   373  N  N   . PHE A 1 75  ? 22.465 15.943 5.914   1.00 36.36 ? 77   PHE A N   1 
ATOM   374  C  CA  . PHE A 1 75  ? 22.083 17.320 6.210   1.00 33.22 ? 77   PHE A CA  1 
ATOM   375  C  C   . PHE A 1 75  ? 21.764 18.123 4.949   1.00 33.50 ? 77   PHE A C   1 
ATOM   376  O  O   . PHE A 1 75  ? 21.027 19.105 5.038   1.00 33.09 ? 77   PHE A O   1 
ATOM   377  C  CB  . PHE A 1 75  ? 23.191 18.051 6.967   1.00 30.28 ? 77   PHE A CB  1 
ATOM   378  C  CG  . PHE A 1 75  ? 23.483 17.482 8.327   1.00 28.53 ? 77   PHE A CG  1 
ATOM   379  C  CD1 . PHE A 1 75  ? 22.549 17.579 9.345   1.00 28.77 ? 77   PHE A CD1 1 
ATOM   380  C  CD2 . PHE A 1 75  ? 24.676 16.818 8.569   1.00 27.51 ? 77   PHE A CD2 1 
ATOM   381  C  CE1 . PHE A 1 75  ? 22.808 17.027 10.589  1.00 28.24 ? 77   PHE A CE1 1 
ATOM   382  C  CE2 . PHE A 1 75  ? 24.939 16.275 9.816   1.00 26.98 ? 77   PHE A CE2 1 
ATOM   383  C  CZ  . PHE A 1 75  ? 24.002 16.378 10.821  1.00 27.65 ? 77   PHE A CZ  1 
ATOM   384  N  N   . GLY A 1 76  ? 22.354 17.727 3.808   1.00 32.79 ? 78   GLY A N   1 
ATOM   385  C  CA  . GLY A 1 76  ? 22.149 18.389 2.530   1.00 33.41 ? 78   GLY A CA  1 
ATOM   386  C  C   . GLY A 1 76  ? 23.211 19.452 2.264   1.00 31.51 ? 78   GLY A C   1 
ATOM   387  O  O   . GLY A 1 76  ? 24.293 19.427 2.854   1.00 30.11 ? 78   GLY A O   1 
ATOM   388  N  N   . ASP A 1 77  ? 22.855 20.413 1.409   1.00 31.96 ? 79   ASP A N   1 
ATOM   389  C  CA  . ASP A 1 77  ? 23.712 21.537 1.068   1.00 31.05 ? 79   ASP A CA  1 
ATOM   390  C  C   . ASP A 1 77  ? 24.003 22.359 2.328   1.00 27.78 ? 79   ASP A C   1 
ATOM   391  O  O   . ASP A 1 77  ? 23.082 22.707 3.075   1.00 27.27 ? 79   ASP A O   1 
ATOM   392  C  CB  . ASP A 1 77  ? 23.060 22.394 -0.028  1.00 34.05 ? 79   ASP A CB  1 
ATOM   393  C  CG  . ASP A 1 77  ? 23.914 23.567 -0.486  1.00 35.89 ? 79   ASP A CG  1 
ATOM   394  O  OD1 . ASP A 1 77  ? 25.037 23.335 -0.958  1.00 37.25 ? 79   ASP A OD1 1 
ATOM   395  O  OD2 . ASP A 1 77  ? 23.453 24.708 -0.373  1.00 37.58 ? 79   ASP A OD2 1 
ATOM   396  N  N   . ALA A 1 78  ? 25.290 22.678 2.538   1.00 25.09 ? 80   ALA A N   1 
ATOM   397  C  CA  . ALA A 1 78  ? 25.731 23.378 3.741   1.00 22.66 ? 80   ALA A CA  1 
ATOM   398  C  C   . ALA A 1 78  ? 25.143 24.789 3.773   1.00 22.39 ? 80   ALA A C   1 
ATOM   399  O  O   . ALA A 1 78  ? 24.654 25.268 4.796   1.00 21.84 ? 80   ALA A O   1 
ATOM   400  C  CB  . ALA A 1 78  ? 27.244 23.429 3.795   1.00 20.98 ? 80   ALA A CB  1 
ATOM   401  N  N   . SER A 1 79  ? 25.229 25.466 2.631   1.00 22.45 ? 81   SER A N   1 
ATOM   402  C  CA  . SER A 1 79  ? 24.742 26.822 2.502   1.00 22.72 ? 81   SER A CA  1 
ATOM   403  C  C   . SER A 1 79  ? 23.260 26.941 2.864   1.00 23.79 ? 81   SER A C   1 
ATOM   404  O  O   . SER A 1 79  ? 22.865 27.872 3.565   1.00 23.72 ? 81   SER A O   1 
ATOM   405  C  CB  . SER A 1 79  ? 25.003 27.308 1.108   1.00 23.49 ? 81   SER A CB  1 
ATOM   406  O  OG  . SER A 1 79  ? 24.879 28.704 1.086   1.00 24.07 ? 81   SER A OG  1 
ATOM   407  N  N   . GLU A 1 80  ? 22.439 26.006 2.384   1.00 25.31 ? 82   GLU A N   1 
ATOM   408  C  CA  . GLU A 1 80  ? 21.005 26.043 2.631   1.00 27.46 ? 82   GLU A CA  1 
ATOM   409  C  C   . GLU A 1 80  ? 20.692 25.596 4.055   1.00 26.04 ? 82   GLU A C   1 
ATOM   410  O  O   . GLU A 1 80  ? 19.724 26.063 4.647   1.00 26.47 ? 82   GLU A O   1 
ATOM   411  C  CB  . GLU A 1 80  ? 20.263 25.149 1.639   1.00 31.21 ? 82   GLU A CB  1 
ATOM   412  C  CG  . GLU A 1 80  ? 20.014 25.792 0.290   1.00 34.35 ? 82   GLU A CG  1 
ATOM   413  C  CD  . GLU A 1 80  ? 19.494 24.790 -0.727  1.00 38.83 ? 82   GLU A CD  1 
ATOM   414  O  OE1 . GLU A 1 80  ? 19.318 23.612 -0.335  1.00 41.47 ? 82   GLU A OE1 1 
ATOM   415  O  OE2 . GLU A 1 80  ? 19.258 25.174 -1.900  1.00 42.34 ? 82   GLU A OE2 1 
ATOM   416  N  N   . LYS A 1 81  ? 21.503 24.680 4.598   1.00 24.43 ? 83   LYS A N   1 
ATOM   417  C  CA  . LYS A 1 81  ? 21.356 24.297 5.992   1.00 23.57 ? 83   LYS A CA  1 
ATOM   418  C  C   . LYS A 1 81  ? 21.650 25.499 6.885   1.00 21.79 ? 83   LYS A C   1 
ATOM   419  O  O   . LYS A 1 81  ? 20.962 25.727 7.879   1.00 21.97 ? 83   LYS A O   1 
ATOM   420  C  CB  . LYS A 1 81  ? 22.287 23.130 6.338   1.00 23.18 ? 83   LYS A CB  1 
ATOM   421  C  CG  . LYS A 1 81  ? 22.101 22.543 7.736   1.00 23.18 ? 83   LYS A CG  1 
ATOM   422  C  CD  . LYS A 1 81  ? 20.709 21.944 7.936   1.00 25.40 ? 83   LYS A CD  1 
ATOM   423  C  CE  . LYS A 1 81  ? 20.497 21.390 9.325   1.00 25.23 ? 83   LYS A CE  1 
ATOM   424  N  NZ  . LYS A 1 81  ? 19.054 21.286 9.631   1.00 27.31 ? 83   LYS A NZ  1 
ATOM   425  N  N   . ALA A 1 82  ? 22.722 26.222 6.554   1.00 20.38 ? 84   ALA A N   1 
ATOM   426  C  CA  . ALA A 1 82  ? 23.091 27.432 7.264   1.00 19.63 ? 84   ALA A CA  1 
ATOM   427  C  C   . ALA A 1 82  ? 21.978 28.468 7.156   1.00 20.65 ? 84   ALA A C   1 
ATOM   428  O  O   . ALA A 1 82  ? 21.628 29.108 8.140   1.00 20.51 ? 84   ALA A O   1 
ATOM   429  C  CB  . ALA A 1 82  ? 24.384 27.965 6.701   1.00 18.94 ? 84   ALA A CB  1 
ATOM   430  N  N   . ALA A 1 83  ? 21.423 28.610 5.954   1.00 21.99 ? 85   ALA A N   1 
ATOM   431  C  CA  . ALA A 1 83  ? 20.378 29.586 5.699   1.00 23.55 ? 85   ALA A CA  1 
ATOM   432  C  C   . ALA A 1 83  ? 19.135 29.274 6.528   1.00 24.71 ? 85   ALA A C   1 
ATOM   433  O  O   . ALA A 1 83  ? 18.451 30.190 6.973   1.00 25.57 ? 85   ALA A O   1 
ATOM   434  C  CB  . ALA A 1 83  ? 20.051 29.619 4.227   1.00 24.80 ? 85   ALA A CB  1 
ATOM   435  N  N   . SER A 1 84  ? 18.834 27.984 6.692   1.00 24.98 ? 86   SER A N   1 
ATOM   436  C  CA  . SER A 1 84  ? 17.667 27.545 7.431   1.00 26.41 ? 86   SER A CA  1 
ATOM   437  C  C   . SER A 1 84  ? 17.790 27.921 8.909   1.00 25.47 ? 86   SER A C   1 
ATOM   438  O  O   . SER A 1 84  ? 16.788 28.056 9.599   1.00 27.07 ? 86   SER A O   1 
ATOM   439  C  CB  . SER A 1 84  ? 17.472 26.056 7.250   1.00 27.11 ? 86   SER A CB  1 
ATOM   440  O  OG  . SER A 1 84  ? 18.525 25.321 7.866   1.00 24.91 ? 86   SER A OG  1 
ATOM   441  N  N   . LEU A 1 85  ? 19.029 28.037 9.404   1.00 23.31 ? 87   LEU A N   1 
ATOM   442  C  CA  . LEU A 1 85  ? 19.290 28.342 10.802  1.00 22.38 ? 87   LEU A CA  1 
ATOM   443  C  C   . LEU A 1 85  ? 19.502 29.832 11.015  1.00 22.13 ? 87   LEU A C   1 
ATOM   444  O  O   . LEU A 1 85  ? 19.581 30.253 12.160  1.00 21.58 ? 87   LEU A O   1 
ATOM   445  C  CB  . LEU A 1 85  ? 20.541 27.597 11.261  1.00 20.55 ? 87   LEU A CB  1 
ATOM   446  C  CG  . LEU A 1 85  ? 20.394 26.083 11.343  1.00 21.06 ? 87   LEU A CG  1 
ATOM   447  C  CD1 . LEU A 1 85  ? 21.697 25.444 11.784  1.00 19.47 ? 87   LEU A CD1 1 
ATOM   448  C  CD2 . LEU A 1 85  ? 19.257 25.692 12.276  1.00 22.53 ? 87   LEU A CD2 1 
ATOM   449  N  N   . SER A 1 86  ? 19.602 30.605 9.927   1.00 22.48 ? 88   SER A N   1 
ATOM   450  C  CA  . SER A 1 86  ? 19.975 32.009 9.989   1.00 22.67 ? 88   SER A CA  1 
ATOM   451  C  C   . SER A 1 86  ? 18.912 32.797 10.755  1.00 24.67 ? 88   SER A C   1 
ATOM   452  O  O   . SER A 1 86  ? 17.737 32.768 10.420  1.00 26.72 ? 88   SER A O   1 
ATOM   453  C  CB  . SER A 1 86  ? 20.193 32.550 8.576   1.00 23.23 ? 88   SER A CB  1 
ATOM   454  O  OG  . SER A 1 86  ? 20.628 33.896 8.577   1.00 23.36 ? 88   SER A OG  1 
ATOM   455  N  N   . GLY A 1 87  ? 19.336 33.497 11.800  1.00 25.08 ? 89   GLY A N   1 
ATOM   456  C  CA  . GLY A 1 87  ? 18.442 34.339 12.572  1.00 28.21 ? 89   GLY A CA  1 
ATOM   457  C  C   . GLY A 1 87  ? 17.860 33.646 13.805  1.00 30.59 ? 89   GLY A C   1 
ATOM   458  O  O   . GLY A 1 87  ? 17.191 34.291 14.595  1.00 33.08 ? 89   GLY A O   1 
ATOM   459  N  N   . LYS A 1 88  ? 18.118 32.348 13.989  1.00 31.69 ? 90   LYS A N   1 
ATOM   460  C  CA  . LYS A 1 88  ? 17.518 31.598 15.085  1.00 34.38 ? 90   LYS A CA  1 
ATOM   461  C  C   . LYS A 1 88  ? 18.399 31.699 16.324  1.00 34.85 ? 90   LYS A C   1 
ATOM   462  O  O   . LYS A 1 88  ? 19.604 31.909 16.212  1.00 32.10 ? 90   LYS A O   1 
ATOM   463  C  CB  . LYS A 1 88  ? 17.297 30.134 14.692  1.00 34.46 ? 90   LYS A CB  1 
ATOM   464  C  CG  . LYS A 1 88  ? 16.251 29.928 13.606  1.00 37.36 ? 90   LYS A CG  1 
ATOM   465  C  CD  . LYS A 1 88  ? 15.881 28.487 13.390  1.00 38.73 ? 90   LYS A CD  1 
ATOM   466  C  CE  . LYS A 1 88  ? 14.945 28.294 12.218  1.00 41.73 ? 90   LYS A CE  1 
ATOM   467  N  NZ  . LYS A 1 88  ? 13.787 29.219 12.282  1.00 44.33 ? 90   LYS A NZ  1 
ATOM   468  N  N   . GLN A 1 89  ? 17.763 31.545 17.493  1.00 39.71 ? 91   GLN A N   1 
ATOM   469  C  CA  . GLN A 1 89  ? 18.431 31.667 18.782  1.00 41.91 ? 91   GLN A CA  1 
ATOM   470  C  C   . GLN A 1 89  ? 19.457 30.546 18.895  1.00 40.47 ? 91   GLN A C   1 
ATOM   471  O  O   . GLN A 1 89  ? 19.271 29.474 18.319  1.00 39.04 ? 91   GLN A O   1 
ATOM   472  C  CB  . GLN A 1 89  ? 17.474 31.513 19.975  1.00 46.81 ? 91   GLN A CB  1 
ATOM   473  C  CG  . GLN A 1 89  ? 16.155 32.268 19.880  1.00 52.06 ? 91   GLN A CG  1 
ATOM   474  C  CD  . GLN A 1 89  ? 16.402 33.753 19.854  1.00 55.34 ? 91   GLN A CD  1 
ATOM   475  O  OE1 . GLN A 1 89  ? 17.208 34.270 20.625  1.00 55.48 ? 91   GLN A OE1 1 
ATOM   476  N  NE2 . GLN A 1 89  ? 15.736 34.442 18.939  1.00 57.83 ? 91   GLN A NE2 1 
ATOM   477  N  N   . ASN A 1 90  ? 20.517 30.790 19.671  1.00 41.62 ? 92   ASN A N   1 
ATOM   478  C  CA  . ASN A 1 90  ? 21.559 29.799 19.892  1.00 42.02 ? 92   ASN A CA  1 
ATOM   479  C  C   . ASN A 1 90  ? 20.970 28.645 20.711  1.00 42.67 ? 92   ASN A C   1 
ATOM   480  O  O   . ASN A 1 90  ? 21.458 27.521 20.630  1.00 41.80 ? 92   ASN A O   1 
ATOM   481  C  CB  . ASN A 1 90  ? 22.793 30.445 20.541  1.00 41.51 ? 92   ASN A CB  1 
ATOM   482  C  CG  . ASN A 1 90  ? 24.026 29.567 20.528  1.00 38.73 ? 92   ASN A CG  1 
ATOM   483  O  OD1 . ASN A 1 90  ? 24.417 29.018 21.554  1.00 36.75 ? 92   ASN A OD1 1 
ATOM   484  N  ND2 . ASN A 1 90  ? 24.635 29.411 19.369  1.00 39.16 ? 92   ASN A ND2 1 
ATOM   485  N  N   . ASP A 1 91  ? 19.919 28.935 21.493  1.00 44.39 ? 93   ASP A N   1 
ATOM   486  C  CA  . ASP A 1 91  ? 19.294 27.953 22.370  1.00 46.72 ? 93   ASP A CA  1 
ATOM   487  C  C   . ASP A 1 91  ? 17.898 27.580 21.859  1.00 46.29 ? 93   ASP A C   1 
ATOM   488  O  O   . ASP A 1 91  ? 17.083 27.063 22.617  1.00 46.00 ? 93   ASP A O   1 
ATOM   489  C  CB  . ASP A 1 91  ? 19.242 28.471 23.817  1.00 50.39 ? 93   ASP A CB  1 
ATOM   490  C  CG  . ASP A 1 91  ? 18.560 29.825 23.983  1.00 54.46 ? 93   ASP A CG  1 
ATOM   491  O  OD1 . ASP A 1 91  ? 18.113 30.397 22.949  1.00 56.06 ? 93   ASP A OD1 1 
ATOM   492  O  OD2 . ASP A 1 91  ? 18.478 30.310 25.146  1.00 52.23 ? 93   ASP A OD2 1 
ATOM   493  N  N   . SER A 1 92  ? 17.612 27.852 20.577  1.00 43.37 ? 94   SER A N   1 
ATOM   494  C  CA  . SER A 1 92  ? 16.350 27.450 19.970  1.00 43.25 ? 94   SER A CA  1 
ATOM   495  C  C   . SER A 1 92  ? 16.393 25.951 19.686  1.00 42.18 ? 94   SER A C   1 
ATOM   496  O  O   . SER A 1 92  ? 17.465 25.354 19.639  1.00 38.54 ? 94   SER A O   1 
ATOM   497  C  CB  . SER A 1 92  ? 16.050 28.260 18.711  1.00 43.67 ? 94   SER A CB  1 
ATOM   498  O  OG  . SER A 1 92  ? 17.085 28.140 17.739  1.00 39.69 ? 94   SER A OG  1 
ATOM   499  N  N   . SER A 1 93  ? 15.224 25.352 19.450  1.00 45.89 ? 95   SER A N   1 
ATOM   500  C  CA  . SER A 1 93  ? 15.107 23.903 19.350  1.00 46.99 ? 95   SER A CA  1 
ATOM   501  C  C   . SER A 1 93  ? 15.824 23.374 18.106  1.00 45.42 ? 95   SER A C   1 
ATOM   502  O  O   . SER A 1 93  ? 16.435 22.307 18.163  1.00 45.16 ? 95   SER A O   1 
ATOM   503  C  CB  . SER A 1 93  ? 13.657 23.468 19.372  1.00 50.32 ? 95   SER A CB  1 
ATOM   504  O  OG  . SER A 1 93  ? 12.966 23.927 18.211  1.00 52.57 ? 95   SER A OG  1 
ATOM   505  N  N   . GLU A 1 94  ? 15.743 24.116 16.989  1.00 44.83 ? 96   GLU A N   1 
ATOM   506  C  CA  . GLU A 1 94  ? 16.301 23.672 15.716  1.00 42.50 ? 96   GLU A CA  1 
ATOM   507  C  C   . GLU A 1 94  ? 17.824 23.644 15.803  1.00 36.24 ? 96   GLU A C   1 
ATOM   508  O  O   . GLU A 1 94  ? 18.470 22.793 15.200  1.00 34.52 ? 96   GLU A O   1 
ATOM   509  C  CB  . GLU A 1 94  ? 15.896 24.582 14.550  1.00 45.21 ? 96   GLU A CB  1 
ATOM   510  C  CG  . GLU A 1 94  ? 14.398 24.703 14.320  1.00 49.69 ? 96   GLU A CG  1 
ATOM   511  C  CD  . GLU A 1 94  ? 13.661 25.713 15.191  1.00 53.06 ? 96   GLU A CD  1 
ATOM   512  O  OE1 . GLU A 1 94  ? 14.289 26.319 16.100  1.00 51.81 ? 96   GLU A OE1 1 
ATOM   513  O  OE2 . GLU A 1 94  ? 12.450 25.902 14.956  1.00 56.41 ? 96   GLU A OE2 1 
ATOM   514  N  N   . VAL A 1 95  ? 18.388 24.592 16.551  1.00 33.23 ? 97   VAL A N   1 
ATOM   515  C  CA  . VAL A 1 95  ? 19.832 24.689 16.693  1.00 29.97 ? 97   VAL A CA  1 
ATOM   516  C  C   . VAL A 1 95  ? 20.328 23.619 17.663  1.00 30.18 ? 97   VAL A C   1 
ATOM   517  O  O   . VAL A 1 95  ? 21.378 23.021 17.428  1.00 27.68 ? 97   VAL A O   1 
ATOM   518  C  CB  . VAL A 1 95  ? 20.262 26.097 17.135  1.00 28.05 ? 97   VAL A CB  1 
ATOM   519  C  CG1 . VAL A 1 95  ? 21.774 26.185 17.304  1.00 25.52 ? 97   VAL A CG1 1 
ATOM   520  C  CG2 . VAL A 1 95  ? 19.766 27.153 16.152  1.00 28.99 ? 97   VAL A CG2 1 
ATOM   521  N  N   . LYS A 1 96  ? 19.573 23.390 18.752  1.00 32.32 ? 98   LYS A N   1 
ATOM   522  C  CA  . LYS A 1 96  ? 19.922 22.340 19.702  1.00 33.39 ? 98   LYS A CA  1 
ATOM   523  C  C   . LYS A 1 96  ? 19.905 21.001 18.976  1.00 31.49 ? 98   LYS A C   1 
ATOM   524  O  O   . LYS A 1 96  ? 20.785 20.179 19.212  1.00 30.96 ? 98   LYS A O   1 
ATOM   525  C  CB  . LYS A 1 96  ? 18.996 22.309 20.923  1.00 37.53 ? 98   LYS A CB  1 
ATOM   526  C  CG  . LYS A 1 96  ? 19.139 23.491 21.883  1.00 39.51 ? 98   LYS A CG  1 
ATOM   527  C  CD  . LYS A 1 96  ? 18.774 23.230 23.351  1.00 41.82 ? 98   LYS A CD  1 
ATOM   528  C  CE  . LYS A 1 96  ? 17.612 22.276 23.588  1.00 46.47 ? 98   LYS A CE  1 
ATOM   529  N  NZ  . LYS A 1 96  ? 16.336 22.707 22.953  1.00 49.09 ? 98   LYS A NZ  1 
ATOM   530  N  N   . ALA A 1 97  ? 18.921 20.819 18.085  1.00 31.01 ? 99   ALA A N   1 
ATOM   531  C  CA  . ALA A 1 97  ? 18.764 19.582 17.336  1.00 30.75 ? 99   ALA A CA  1 
ATOM   532  C  C   . ALA A 1 97  ? 19.969 19.372 16.421  1.00 29.45 ? 99   ALA A C   1 
ATOM   533  O  O   . ALA A 1 97  ? 20.497 18.261 16.339  1.00 29.84 ? 99   ALA A O   1 
ATOM   534  C  CB  . ALA A 1 97  ? 17.481 19.619 16.551  1.00 32.25 ? 99   ALA A CB  1 
ATOM   535  N  N   . PHE A 1 98  ? 20.398 20.455 15.746  1.00 26.16 ? 100  PHE A N   1 
ATOM   536  C  CA  . PHE A 1 98  ? 21.506 20.395 14.813  1.00 23.93 ? 100  PHE A CA  1 
ATOM   537  C  C   . PHE A 1 98  ? 22.799 20.064 15.551  1.00 21.93 ? 100  PHE A C   1 
ATOM   538  O  O   . PHE A 1 98  ? 23.635 19.316 15.042  1.00 20.99 ? 100  PHE A O   1 
ATOM   539  C  CB  . PHE A 1 98  ? 21.597 21.704 14.021  1.00 23.12 ? 100  PHE A CB  1 
ATOM   540  C  CG  . PHE A 1 98  ? 22.614 21.733 12.913  1.00 21.98 ? 100  PHE A CG  1 
ATOM   541  C  CD1 . PHE A 1 98  ? 22.725 20.686 12.017  1.00 22.40 ? 100  PHE A CD1 1 
ATOM   542  C  CD2 . PHE A 1 98  ? 23.441 22.837 12.737  1.00 20.96 ? 100  PHE A CD2 1 
ATOM   543  C  CE1 . PHE A 1 98  ? 23.659 20.727 10.994  1.00 22.04 ? 100  PHE A CE1 1 
ATOM   544  C  CE2 . PHE A 1 98  ? 24.372 22.881 11.705  1.00 20.22 ? 100  PHE A CE2 1 
ATOM   545  C  CZ  . PHE A 1 98  ? 24.484 21.823 10.836  1.00 20.71 ? 100  PHE A CZ  1 
ATOM   546  N  N   . ALA A 1 99  ? 22.961 20.619 16.757  1.00 20.93 ? 101  ALA A N   1 
ATOM   547  C  CA  . ALA A 1 99  ? 24.149 20.362 17.556  1.00 20.01 ? 101  ALA A CA  1 
ATOM   548  C  C   . ALA A 1 99  ? 24.267 18.869 17.907  1.00 20.94 ? 101  ALA A C   1 
ATOM   549  O  O   . ALA A 1 99  ? 25.335 18.283 17.787  1.00 18.86 ? 101  ALA A O   1 
ATOM   550  C  CB  . ALA A 1 99  ? 24.108 21.218 18.795  1.00 19.55 ? 101  ALA A CB  1 
ATOM   551  N  N   . GLN A 1 100 ? 23.155 18.260 18.322  1.00 24.00 ? 102  GLN A N   1 
ATOM   552  C  CA  . GLN A 1 100 ? 23.141 16.883 18.805  1.00 26.83 ? 102  GLN A CA  1 
ATOM   553  C  C   . GLN A 1 100 ? 23.323 15.921 17.632  1.00 27.59 ? 102  GLN A C   1 
ATOM   554  O  O   . GLN A 1 100 ? 23.920 14.875 17.790  1.00 28.22 ? 102  GLN A O   1 
ATOM   555  C  CB  . GLN A 1 100 ? 21.840 16.591 19.569  1.00 29.45 ? 102  GLN A CB  1 
ATOM   556  C  CG  . GLN A 1 100 ? 21.689 17.403 20.861  1.00 29.91 ? 102  GLN A CG  1 
ATOM   557  C  CD  . GLN A 1 100 ? 22.733 17.087 21.916  1.00 28.68 ? 102  GLN A CD  1 
ATOM   558  O  OE1 . GLN A 1 100 ? 22.881 15.944 22.338  1.00 28.36 ? 102  GLN A OE1 1 
ATOM   559  N  NE2 . GLN A 1 100 ? 23.490 18.088 22.338  1.00 26.75 ? 102  GLN A NE2 1 
ATOM   560  N  N   . GLU A 1 101 ? 22.812 16.273 16.454  1.00 28.25 ? 103  GLU A N   1 
ATOM   561  C  CA  . GLU A 1 101 ? 22.980 15.432 15.282  1.00 29.94 ? 103  GLU A CA  1 
ATOM   562  C  C   . GLU A 1 101 ? 24.411 15.512 14.755  1.00 26.42 ? 103  GLU A C   1 
ATOM   563  O  O   . GLU A 1 101 ? 24.960 14.509 14.301  1.00 26.34 ? 103  GLU A O   1 
ATOM   564  C  CB  . GLU A 1 101 ? 21.973 15.835 14.207  1.00 33.75 ? 103  GLU A CB  1 
ATOM   565  C  CG  . GLU A 1 101 ? 20.602 15.265 14.476  1.00 39.30 ? 103  GLU A CG  1 
ATOM   566  C  CD  . GLU A 1 101 ? 19.484 16.136 13.942  1.00 44.54 ? 103  GLU A CD  1 
ATOM   567  O  OE1 . GLU A 1 101 ? 19.547 16.501 12.745  1.00 46.63 ? 103  GLU A OE1 1 
ATOM   568  O  OE2 . GLU A 1 101 ? 18.583 16.477 14.739  1.00 49.02 ? 103  GLU A OE2 1 
ATOM   569  N  N   . LEU A 1 102 ? 24.990 16.712 14.784  1.00 23.23 ? 104  LEU A N   1 
ATOM   570  C  CA  . LEU A 1 102 ? 26.376 16.896 14.394  1.00 21.70 ? 104  LEU A CA  1 
ATOM   571  C  C   . LEU A 1 102 ? 27.312 16.093 15.296  1.00 21.45 ? 104  LEU A C   1 
ATOM   572  O  O   . LEU A 1 102 ? 28.347 15.610 14.844  1.00 20.68 ? 104  LEU A O   1 
ATOM   573  C  CB  . LEU A 1 102 ? 26.727 18.382 14.476  1.00 19.83 ? 104  LEU A CB  1 
ATOM   574  C  CG  . LEU A 1 102 ? 26.242 19.277 13.327  1.00 19.79 ? 104  LEU A CG  1 
ATOM   575  C  CD1 . LEU A 1 102 ? 26.464 20.745 13.668  1.00 18.33 ? 104  LEU A CD1 1 
ATOM   576  C  CD2 . LEU A 1 102 ? 26.940 18.928 12.015  1.00 19.83 ? 104  LEU A CD2 1 
ATOM   577  N  N   . SER A 1 103 ? 26.961 15.983 16.583  1.00 22.25 ? 105  SER A N   1 
ATOM   578  C  CA  . SER A 1 103 ? 27.810 15.312 17.551  1.00 22.28 ? 105  SER A CA  1 
ATOM   579  C  C   . SER A 1 103 ? 28.009 13.845 17.180  1.00 23.88 ? 105  SER A C   1 
ATOM   580  O  O   . SER A 1 103 ? 28.975 13.238 17.622  1.00 23.63 ? 105  SER A O   1 
ATOM   581  C  CB  . SER A 1 103 ? 27.246 15.447 18.939  1.00 22.65 ? 105  SER A CB  1 
ATOM   582  O  OG  . SER A 1 103 ? 26.103 14.633 19.075  1.00 23.84 ? 105  SER A OG  1 
ATOM   583  N  N   . ASN A 1 104 ? 27.107 13.289 16.361  1.00 25.91 ? 106  ASN A N   1 
ATOM   584  C  CA  . ASN A 1 104 ? 27.185 11.911 15.901  1.00 27.77 ? 106  ASN A CA  1 
ATOM   585  C  C   . ASN A 1 104 ? 27.664 11.838 14.459  1.00 27.22 ? 106  ASN A C   1 
ATOM   586  O  O   . ASN A 1 104 ? 27.514 10.800 13.836  1.00 28.48 ? 106  ASN A O   1 
ATOM   587  C  CB  . ASN A 1 104 ? 25.820 11.220 15.994  1.00 30.93 ? 106  ASN A CB  1 
ATOM   588  C  CG  . ASN A 1 104 ? 25.291 11.235 17.411  1.00 32.08 ? 106  ASN A CG  1 
ATOM   589  O  OD1 . ASN A 1 104 ? 24.269 11.852 17.696  1.00 33.70 ? 106  ASN A OD1 1 
ATOM   590  N  ND2 . ASN A 1 104 ? 26.012 10.602 18.316  1.00 32.34 ? 106  ASN A ND2 1 
ATOM   591  N  N   . SER A 1 105 ? 28.258 12.925 13.958  1.00 24.83 ? 107  SER A N   1 
ATOM   592  C  CA  . SER A 1 105 ? 28.666 13.034 12.568  1.00 24.12 ? 107  SER A CA  1 
ATOM   593  C  C   . SER A 1 105 ? 30.045 13.678 12.456  1.00 21.82 ? 107  SER A C   1 
ATOM   594  O  O   . SER A 1 105 ? 30.365 14.258 11.429  1.00 21.17 ? 107  SER A O   1 
ATOM   595  C  CB  . SER A 1 105 ? 27.634 13.827 11.794  1.00 24.59 ? 107  SER A CB  1 
ATOM   596  O  OG  . SER A 1 105 ? 26.352 13.227 11.886  1.00 27.46 ? 107  SER A OG  1 
ATOM   597  N  N   . LEU A 1 106 ? 30.855 13.590 13.509  1.00 20.91 ? 108  LEU A N   1 
ATOM   598  C  CA  . LEU A 1 106 ? 32.067 14.381 13.592  1.00 19.83 ? 108  LEU A CA  1 
ATOM   599  C  C   . LEU A 1 106 ? 33.212 13.645 12.917  1.00 21.36 ? 108  LEU A C   1 
ATOM   600  O  O   . LEU A 1 106 ? 33.173 12.430 12.799  1.00 22.67 ? 108  LEU A O   1 
ATOM   601  C  CB  . LEU A 1 106 ? 32.408 14.652 15.062  1.00 18.82 ? 108  LEU A CB  1 
ATOM   602  C  CG  . LEU A 1 106 ? 31.393 15.505 15.826  1.00 18.16 ? 108  LEU A CG  1 
ATOM   603  C  CD1 . LEU A 1 106 ? 31.843 15.719 17.265  1.00 17.45 ? 108  LEU A CD1 1 
ATOM   604  C  CD2 . LEU A 1 106 ? 31.170 16.832 15.127  1.00 17.37 ? 108  LEU A CD2 1 
ATOM   605  N  N   . SER A 1 107 ? 34.240 14.402 12.519  1.00 21.27 ? 109  SER A N   1 
ATOM   606  C  CA  . SER A 1 107 ? 35.468 13.831 11.989  1.00 23.10 ? 109  SER A CA  1 
ATOM   607  C  C   . SER A 1 107 ? 36.680 14.509 12.624  1.00 22.46 ? 109  SER A C   1 
ATOM   608  O  O   . SER A 1 107 ? 36.657 15.712 12.866  1.00 20.82 ? 109  SER A O   1 
ATOM   609  C  CB  . SER A 1 107 ? 35.494 13.976 10.498  1.00 24.59 ? 109  SER A CB  1 
ATOM   610  O  OG  . SER A 1 107 ? 36.723 13.537 9.946   1.00 26.03 ? 109  SER A OG  1 
ATOM   611  N  N   . ALA A 1 108 ? 37.740 13.723 12.865  1.00 23.24 ? 110  ALA A N   1 
ATOM   612  C  CA  . ALA A 1 108 ? 38.989 14.227 13.423  1.00 22.85 ? 110  ALA A CA  1 
ATOM   613  C  C   . ALA A 1 108 ? 39.733 15.103 12.420  1.00 22.10 ? 110  ALA A C   1 
ATOM   614  O  O   . ALA A 1 108 ? 40.635 15.845 12.786  1.00 20.71 ? 110  ALA A O   1 
ATOM   615  C  CB  . ALA A 1 108 ? 39.856 13.064 13.838  1.00 24.70 ? 110  ALA A CB  1 
ATOM   616  N  N   . ALA A 1 109 ? 39.368 14.981 11.142  1.00 22.79 ? 111  ALA A N   1 
ATOM   617  C  CA  . ALA A 1 109 ? 39.944 15.791 10.084  1.00 23.18 ? 111  ALA A CA  1 
ATOM   618  C  C   . ALA A 1 109 ? 39.843 17.284 10.388  1.00 21.18 ? 111  ALA A C   1 
ATOM   619  O  O   . ALA A 1 109 ? 40.767 18.021 10.074  1.00 21.66 ? 111  ALA A O   1 
ATOM   620  C  CB  . ALA A 1 109 ? 39.269 15.469 8.765   1.00 24.46 ? 111  ALA A CB  1 
ATOM   621  N  N   . GLY A 1 110 ? 38.709 17.737 10.932  1.00 19.80 ? 112  GLY A N   1 
ATOM   622  C  CA  . GLY A 1 110 ? 38.486 19.148 11.227  1.00 18.23 ? 112  GLY A CA  1 
ATOM   623  C  C   . GLY A 1 110 ? 38.435 19.437 12.726  1.00 17.23 ? 112  GLY A C   1 
ATOM   624  O  O   . GLY A 1 110 ? 37.665 20.301 13.149  1.00 15.79 ? 112  GLY A O   1 
ATOM   625  N  N   . ARG A 1 111 ? 39.247 18.705 13.507  1.00 18.18 ? 113  ARG A N   1 
ATOM   626  C  CA  . ARG A 1 111 ? 39.232 18.793 14.970  1.00 18.33 ? 113  ARG A CA  1 
ATOM   627  C  C   . ARG A 1 111 ? 40.429 19.601 15.471  1.00 18.31 ? 113  ARG A C   1 
ATOM   628  O  O   . ARG A 1 111 ? 41.539 19.472 14.970  1.00 19.46 ? 113  ARG A O   1 
ATOM   629  C  CB  . ARG A 1 111 ? 39.266 17.399 15.602  1.00 19.67 ? 113  ARG A CB  1 
ATOM   630  C  CG  . ARG A 1 111 ? 39.255 17.394 17.131  1.00 19.90 ? 113  ARG A CG  1 
ATOM   631  C  CD  . ARG A 1 111 ? 39.430 15.992 17.688  1.00 21.00 ? 113  ARG A CD  1 
ATOM   632  N  NE  . ARG A 1 111 ? 40.719 15.433 17.320  1.00 22.84 ? 113  ARG A NE  1 
ATOM   633  C  CZ  . ARG A 1 111 ? 40.973 14.131 17.215  1.00 24.69 ? 113  ARG A CZ  1 
ATOM   634  N  NH1 . ARG A 1 111 ? 40.050 13.249 17.550  1.00 24.83 ? 113  ARG A NH1 1 
ATOM   635  N  NH2 . ARG A 1 111 ? 42.130 13.712 16.732  1.00 25.98 ? 113  ARG A NH2 1 
ATOM   636  N  N   . THR A 1 112 ? 40.181 20.459 16.461  1.00 17.79 ? 114  THR A N   1 
ATOM   637  C  CA  . THR A 1 112 ? 41.230 21.140 17.202  1.00 18.08 ? 114  THR A CA  1 
ATOM   638  C  C   . THR A 1 112 ? 41.021 20.828 18.681  1.00 18.04 ? 114  THR A C   1 
ATOM   639  O  O   . THR A 1 112 ? 39.944 21.068 19.221  1.00 17.07 ? 114  THR A O   1 
ATOM   640  C  CB  . THR A 1 112 ? 41.202 22.655 16.982  1.00 18.03 ? 114  THR A CB  1 
ATOM   641  O  OG1 . THR A 1 112 ? 41.218 22.922 15.583  1.00 17.66 ? 114  THR A OG1 1 
ATOM   642  C  CG2 . THR A 1 112 ? 42.343 23.394 17.659  1.00 18.75 ? 114  THR A CG2 1 
ATOM   643  N  N   . ARG A 1 113 ? 42.056 20.274 19.311  1.00 19.54 ? 115  ARG A N   1 
ATOM   644  C  CA  . ARG A 1 113 ? 42.003 19.954 20.729  1.00 20.68 ? 115  ARG A CA  1 
ATOM   645  C  C   . ARG A 1 113 ? 42.822 20.991 21.485  1.00 20.26 ? 115  ARG A C   1 
ATOM   646  O  O   . ARG A 1 113 ? 43.919 21.339 21.060  1.00 20.68 ? 115  ARG A O   1 
ATOM   647  C  CB  . ARG A 1 113 ? 42.549 18.548 20.985  1.00 23.28 ? 115  ARG A CB  1 
ATOM   648  C  CG  . ARG A 1 113 ? 41.784 17.473 20.234  1.00 25.46 ? 115  ARG A CG  1 
ATOM   649  C  CD  . ARG A 1 113 ? 42.369 16.099 20.450  1.00 28.96 ? 115  ARG A CD  1 
ATOM   650  N  NE  . ARG A 1 113 ? 42.294 15.732 21.853  1.00 31.56 ? 115  ARG A NE  1 
ATOM   651  C  CZ  . ARG A 1 113 ? 41.750 14.608 22.308  1.00 35.61 ? 115  ARG A CZ  1 
ATOM   652  N  NH1 . ARG A 1 113 ? 41.203 13.739 21.462  1.00 38.17 ? 115  ARG A NH1 1 
ATOM   653  N  NH2 . ARG A 1 113 ? 41.776 14.352 23.607  1.00 35.03 ? 115  ARG A NH2 1 
ATOM   654  N  N   . VAL A 1 114 ? 42.278 21.453 22.616  1.00 19.33 ? 116  VAL A N   1 
ATOM   655  C  CA  . VAL A 1 114 ? 42.904 22.471 23.444  1.00 20.06 ? 116  VAL A CA  1 
ATOM   656  C  C   . VAL A 1 114 ? 42.793 22.034 24.901  1.00 19.84 ? 116  VAL A C   1 
ATOM   657  O  O   . VAL A 1 114 ? 41.707 21.688 25.349  1.00 17.28 ? 116  VAL A O   1 
ATOM   658  C  CB  . VAL A 1 114 ? 42.204 23.818 23.184  1.00 20.17 ? 116  VAL A CB  1 
ATOM   659  C  CG1 . VAL A 1 114 ? 42.555 24.876 24.202  1.00 21.96 ? 116  VAL A CG1 1 
ATOM   660  C  CG2 . VAL A 1 114 ? 42.503 24.301 21.770  1.00 21.15 ? 116  VAL A CG2 1 
ATOM   661  N  N   . ARG A 1 115 ? 43.920 22.034 25.625  1.00 22.17 ? 117  ARG A N   1 
ATOM   662  C  CA  . ARG A 1 115 ? 43.867 21.797 27.061  1.00 24.37 ? 117  ARG A CA  1 
ATOM   663  C  C   . ARG A 1 115 ? 43.322 23.065 27.708  1.00 22.07 ? 117  ARG A C   1 
ATOM   664  O  O   . ARG A 1 115 ? 43.666 24.164 27.314  1.00 22.69 ? 117  ARG A O   1 
ATOM   665  C  CB  . ARG A 1 115 ? 45.219 21.368 27.646  1.00 29.70 ? 117  ARG A CB  1 
ATOM   666  C  CG  . ARG A 1 115 ? 46.367 22.342 27.419  1.00 35.09 ? 117  ARG A CG  1 
ATOM   667  C  CD  . ARG A 1 115 ? 47.600 22.022 28.266  1.00 41.30 ? 117  ARG A CD  1 
ATOM   668  N  NE  . ARG A 1 115 ? 47.415 22.242 29.707  1.00 45.86 ? 117  ARG A NE  1 
ATOM   669  C  CZ  . ARG A 1 115 ? 47.248 23.427 30.310  1.00 47.87 ? 117  ARG A CZ  1 
ATOM   670  N  NH1 . ARG A 1 115 ? 47.304 24.555 29.622  1.00 49.25 ? 117  ARG A NH1 1 
ATOM   671  N  NH2 . ARG A 1 115 ? 47.028 23.485 31.614  1.00 47.15 ? 117  ARG A NH2 1 
ATOM   672  N  N   . SER A 1 116 ? 42.454 22.906 28.698  1.00 20.48 ? 118  SER A N   1 
ATOM   673  C  CA  . SER A 1 116 ? 41.805 24.033 29.346  1.00 19.09 ? 118  SER A CA  1 
ATOM   674  C  C   . SER A 1 116 ? 42.761 24.723 30.319  1.00 20.85 ? 118  SER A C   1 
ATOM   675  O  O   . SER A 1 116 ? 43.680 24.110 30.864  1.00 21.37 ? 118  SER A O   1 
ATOM   676  C  CB  . SER A 1 116 ? 40.553 23.553 30.055  1.00 18.25 ? 118  SER A CB  1 
ATOM   677  O  OG  . SER A 1 116 ? 40.865 22.653 31.128  1.00 17.38 ? 118  SER A OG  1 
ATOM   678  N  N   . GLU A 1 117 ? 42.499 26.006 30.550  1.00 21.73 ? 119  GLU A N   1 
ATOM   679  C  CA  . GLU A 1 117 ? 43.029 26.723 31.689  1.00 23.75 ? 119  GLU A CA  1 
ATOM   680  C  C   . GLU A 1 117 ? 41.889 27.011 32.649  1.00 23.15 ? 119  GLU A C   1 
ATOM   681  O  O   . GLU A 1 117 ? 40.725 26.917 32.280  1.00 21.67 ? 119  GLU A O   1 
ATOM   682  C  CB  . GLU A 1 117 ? 43.643 28.042 31.256  1.00 26.80 ? 119  GLU A CB  1 
ATOM   683  C  CG  . GLU A 1 117 ? 44.791 27.905 30.277  1.00 29.32 ? 119  GLU A CG  1 
ATOM   684  C  CD  . GLU A 1 117 ? 45.447 29.257 30.052  1.00 32.18 ? 119  GLU A CD  1 
ATOM   685  O  OE1 . GLU A 1 117 ? 45.791 29.891 31.062  1.00 35.53 ? 119  GLU A OE1 1 
ATOM   686  O  OE2 . GLU A 1 117 ? 45.548 29.701 28.885  1.00 33.35 ? 119  GLU A OE2 1 
ATOM   687  N  N   . GLN A 1 118 ? 42.242 27.362 33.881  1.00 24.02 ? 120  GLN A N   1 
ATOM   688  C  CA  . GLN A 1 118 ? 41.273 27.824 34.855  1.00 24.85 ? 120  GLN A CA  1 
ATOM   689  C  C   . GLN A 1 118 ? 40.860 29.254 34.518  1.00 24.68 ? 120  GLN A C   1 
ATOM   690  O  O   . GLN A 1 118 ? 41.712 30.114 34.282  1.00 26.06 ? 120  GLN A O   1 
ATOM   691  C  CB  . GLN A 1 118 ? 41.870 27.773 36.261  1.00 26.72 ? 120  GLN A CB  1 
ATOM   692  C  CG  . GLN A 1 118 ? 40.845 27.988 37.360  1.00 27.62 ? 120  GLN A CG  1 
ATOM   693  C  CD  . GLN A 1 118 ? 39.908 26.809 37.481  1.00 27.39 ? 120  GLN A CD  1 
ATOM   694  O  OE1 . GLN A 1 118 ? 40.314 25.652 37.544  1.00 26.66 ? 120  GLN A OE1 1 
ATOM   695  N  NE2 . GLN A 1 118 ? 38.619 27.098 37.512  1.00 28.38 ? 120  GLN A NE2 1 
ATOM   696  N  N   . GLY A 1 119 ? 39.542 29.479 34.467  1.00 23.56 ? 121  GLY A N   1 
ATOM   697  C  CA  . GLY A 1 119 ? 38.999 30.812 34.258  1.00 23.86 ? 121  GLY A CA  1 
ATOM   698  C  C   . GLY A 1 119 ? 38.648 31.033 32.792  1.00 21.71 ? 121  GLY A C   1 
ATOM   699  O  O   . GLY A 1 119 ? 37.486 31.124 32.445  1.00 21.05 ? 121  GLY A O   1 
ATOM   700  N  N   . THR A 1 120 ? 39.677 31.103 31.945  1.00 22.05 ? 122  THR A N   1 
ATOM   701  C  CA  . THR A 1 120 ? 39.525 31.474 30.545  1.00 21.30 ? 122  THR A CA  1 
ATOM   702  C  C   . THR A 1 120 ? 40.403 30.594 29.665  1.00 19.68 ? 122  THR A C   1 
ATOM   703  O  O   . THR A 1 120 ? 41.583 30.428 29.929  1.00 21.30 ? 122  THR A O   1 
ATOM   704  C  CB  . THR A 1 120 ? 39.896 32.945 30.348  1.00 23.28 ? 122  THR A CB  1 
ATOM   705  O  OG1 . THR A 1 120 ? 38.906 33.709 31.032  1.00 25.79 ? 122  THR A OG1 1 
ATOM   706  C  CG2 . THR A 1 120 ? 39.934 33.373 28.908  1.00 22.79 ? 122  THR A CG2 1 
ATOM   707  N  N   . THR A 1 121 ? 39.813 30.018 28.617  1.00 17.45 ? 123  THR A N   1 
ATOM   708  C  CA  . THR A 1 121 ? 40.562 29.214 27.671  1.00 16.27 ? 123  THR A CA  1 
ATOM   709  C  C   . THR A 1 121 ? 40.428 29.860 26.295  1.00 15.72 ? 123  THR A C   1 
ATOM   710  O  O   . THR A 1 121 ? 39.320 30.111 25.840  1.00 15.69 ? 123  THR A O   1 
ATOM   711  C  CB  . THR A 1 121 ? 40.071 27.760 27.670  1.00 15.25 ? 123  THR A CB  1 
ATOM   712  O  OG1 . THR A 1 121 ? 40.205 27.229 28.995  1.00 15.31 ? 123  THR A OG1 1 
ATOM   713  C  CG2 . THR A 1 121 ? 40.834 26.897 26.695  1.00 14.83 ? 123  THR A CG2 1 
ATOM   714  N  N   . THR A 1 122 ? 41.556 30.103 25.629  1.00 16.24 ? 124  THR A N   1 
ATOM   715  C  CA  . THR A 1 122 ? 41.565 30.837 24.373  1.00 15.97 ? 124  THR A CA  1 
ATOM   716  C  C   . THR A 1 122 ? 42.069 29.943 23.249  1.00 16.07 ? 124  THR A C   1 
ATOM   717  O  O   . THR A 1 122 ? 43.105 29.304 23.399  1.00 17.20 ? 124  THR A O   1 
ATOM   718  C  CB  . THR A 1 122 ? 42.480 32.061 24.469  1.00 17.06 ? 124  THR A CB  1 
ATOM   719  O  OG1 . THR A 1 122 ? 42.114 32.766 25.650  1.00 17.46 ? 124  THR A OG1 1 
ATOM   720  C  CG2 . THR A 1 122 ? 42.380 32.983 23.277  1.00 17.01 ? 124  THR A CG2 1 
ATOM   721  N  N   . ILE A 1 123 ? 41.329 29.913 22.133  1.00 15.27 ? 125  ILE A N   1 
ATOM   722  C  CA  . ILE A 1 123 ? 41.714 29.166 20.951  1.00 15.09 ? 125  ILE A CA  1 
ATOM   723  C  C   . ILE A 1 123 ? 41.825 30.170 19.809  1.00 15.45 ? 125  ILE A C   1 
ATOM   724  O  O   . ILE A 1 123 ? 40.826 30.771 19.408  1.00 14.33 ? 125  ILE A O   1 
ATOM   725  C  CB  . ILE A 1 123 ? 40.681 28.069 20.631  1.00 14.74 ? 125  ILE A CB  1 
ATOM   726  C  CG1 . ILE A 1 123 ? 40.353 27.191 21.846  1.00 15.09 ? 125  ILE A CG1 1 
ATOM   727  C  CG2 . ILE A 1 123 ? 41.138 27.248 19.443  1.00 15.33 ? 125  ILE A CG2 1 
ATOM   728  C  CD1 . ILE A 1 123 ? 39.200 27.669 22.675  1.00 14.51 ? 125  ILE A CD1 1 
ATOM   729  N  N   . SER A 1 124 ? 43.049 30.354 19.304  1.00 16.68 ? 126  SER A N   1 
ATOM   730  C  CA  . SER A 1 124 ? 43.292 31.274 18.203  1.00 17.94 ? 126  SER A CA  1 
ATOM   731  C  C   . SER A 1 124 ? 43.694 30.504 16.947  1.00 17.64 ? 126  SER A C   1 
ATOM   732  O  O   . SER A 1 124 ? 44.033 29.333 17.018  1.00 17.90 ? 126  SER A O   1 
ATOM   733  C  CB  . SER A 1 124 ? 44.327 32.293 18.558  1.00 20.10 ? 126  SER A CB  1 
ATOM   734  O  OG  . SER A 1 124 ? 45.498 31.649 19.000  1.00 22.75 ? 126  SER A OG  1 
ATOM   735  N  N   . GLY A 1 125 ? 43.639 31.188 15.805  1.00 17.53 ? 127  GLY A N   1 
ATOM   736  C  CA  . GLY A 1 125 ? 44.127 30.645 14.551  1.00 17.83 ? 127  GLY A CA  1 
ATOM   737  C  C   . GLY A 1 125 ? 43.126 29.689 13.915  1.00 16.95 ? 127  GLY A C   1 
ATOM   738  O  O   . GLY A 1 125 ? 43.520 28.847 13.118  1.00 17.99 ? 127  GLY A O   1 
ATOM   739  N  N   . LEU A 1 126 ? 41.840 29.859 14.243  1.00 15.91 ? 128  LEU A N   1 
ATOM   740  C  CA  . LEU A 1 126 ? 40.776 29.045 13.689  1.00 15.37 ? 128  LEU A CA  1 
ATOM   741  C  C   . LEU A 1 126 ? 40.452 29.558 12.301  1.00 15.44 ? 128  LEU A C   1 
ATOM   742  O  O   . LEU A 1 126 ? 40.391 30.765 12.085  1.00 15.08 ? 128  LEU A O   1 
ATOM   743  C  CB  . LEU A 1 126 ? 39.536 29.142 14.578  1.00 14.66 ? 128  LEU A CB  1 
ATOM   744  C  CG  . LEU A 1 126 ? 39.696 28.532 15.962  1.00 14.23 ? 128  LEU A CG  1 
ATOM   745  C  CD1 . LEU A 1 126 ? 38.535 28.914 16.859  1.00 13.27 ? 128  LEU A CD1 1 
ATOM   746  C  CD2 . LEU A 1 126 ? 39.830 27.026 15.816  1.00 15.14 ? 128  LEU A CD2 1 
ATOM   747  N  N   . LYS A 1 127 ? 40.265 28.615 11.373  1.00 15.79 ? 129  LYS A N   1 
ATOM   748  C  CA  . LYS A 1 127 ? 39.710 28.942 10.071  1.00 15.70 ? 129  LYS A CA  1 
ATOM   749  C  C   . LYS A 1 127 ? 38.331 29.551 10.286  1.00 13.95 ? 129  LYS A C   1 
ATOM   750  O  O   . LYS A 1 127 ? 37.626 29.172 11.221  1.00 12.21 ? 129  LYS A O   1 
ATOM   751  C  CB  . LYS A 1 127 ? 39.620 27.699 9.186   1.00 17.48 ? 129  LYS A CB  1 
ATOM   752  C  CG  . LYS A 1 127 ? 40.965 27.065 8.861   1.00 20.46 ? 129  LYS A CG  1 
ATOM   753  C  CD  . LYS A 1 127 ? 40.842 25.858 7.951   1.00 22.70 ? 129  LYS A CD  1 
ATOM   754  C  CE  . LYS A 1 127 ? 42.140 25.100 7.796   1.00 25.49 ? 129  LYS A CE  1 
ATOM   755  N  NZ  . LYS A 1 127 ? 41.871 23.788 7.177   1.00 28.29 ? 129  LYS A NZ  1 
ATOM   756  N  N   . PRO A 1 128 ? 37.899 30.512 9.442   1.00 13.46 ? 130  PRO A N   1 
ATOM   757  C  CA  . PRO A 1 128 ? 36.608 31.150 9.644   1.00 13.03 ? 130  PRO A CA  1 
ATOM   758  C  C   . PRO A 1 128 ? 35.461 30.157 9.502   1.00 12.28 ? 130  PRO A C   1 
ATOM   759  O  O   . PRO A 1 128 ? 35.527 29.219 8.704   1.00 12.64 ? 130  PRO A O   1 
ATOM   760  C  CB  . PRO A 1 128 ? 36.511 32.208 8.543   1.00 14.09 ? 130  PRO A CB  1 
ATOM   761  C  CG  . PRO A 1 128 ? 37.917 32.327 7.989   1.00 15.07 ? 130  PRO A CG  1 
ATOM   762  C  CD  . PRO A 1 128 ? 38.589 30.997 8.246   1.00 14.75 ? 130  PRO A CD  1 
ATOM   763  N  N   . GLY A 1 129 ? 34.402 30.395 10.267  1.00 11.44 ? 131  GLY A N   1 
ATOM   764  C  CA  . GLY A 1 129 ? 33.176 29.641 10.110  1.00 11.42 ? 131  GLY A CA  1 
ATOM   765  C  C   . GLY A 1 129 ? 32.591 29.220 11.451  1.00 10.85 ? 131  GLY A C   1 
ATOM   766  O  O   . GLY A 1 129 ? 32.816 29.885 12.457  1.00 10.75 ? 131  GLY A O   1 
ATOM   767  N  N   . TYR A 1 130 ? 31.828 28.124 11.420  1.00 10.76 ? 132  TYR A N   1 
ATOM   768  C  CA  . TYR A 1 130 ? 31.014 27.651 12.522  1.00 10.41 ? 132  TYR A CA  1 
ATOM   769  C  C   . TYR A 1 130 ? 31.686 26.418 13.106  1.00 10.13 ? 132  TYR A C   1 
ATOM   770  O  O   . TYR A 1 130 ? 32.126 25.537 12.351  1.00 10.44 ? 132  TYR A O   1 
ATOM   771  C  CB  . TYR A 1 130 ? 29.652 27.292 11.930  1.00 11.31 ? 132  TYR A CB  1 
ATOM   772  C  CG  . TYR A 1 130 ? 28.422 27.269 12.823  1.00 11.64 ? 132  TYR A CG  1 
ATOM   773  C  CD1 . TYR A 1 130 ? 28.179 28.249 13.772  1.00 11.68 ? 132  TYR A CD1 1 
ATOM   774  C  CD2 . TYR A 1 130 ? 27.444 26.311 12.623  1.00 12.46 ? 132  TYR A CD2 1 
ATOM   775  C  CE1 . TYR A 1 130 ? 27.017 28.253 14.526  1.00 12.12 ? 132  TYR A CE1 1 
ATOM   776  C  CE2 . TYR A 1 130 ? 26.264 26.328 13.337  1.00 13.01 ? 132  TYR A CE2 1 
ATOM   777  C  CZ  . TYR A 1 130 ? 26.040 27.308 14.275  1.00 13.13 ? 132  TYR A CZ  1 
ATOM   778  O  OH  . TYR A 1 130 ? 24.854 27.217 14.943  1.00 14.51 ? 132  TYR A OH  1 
ATOM   779  N  N   . TYR A 1 131 ? 31.716 26.357 14.438  1.00 9.40  ? 133  TYR A N   1 
ATOM   780  C  CA  . TYR A 1 131 ? 32.409 25.300 15.151  1.00 9.37  ? 133  TYR A CA  1 
ATOM   781  C  C   . TYR A 1 131 ? 31.474 24.646 16.163  1.00 9.34  ? 133  TYR A C   1 
ATOM   782  O  O   . TYR A 1 131 ? 30.672 25.325 16.794  1.00 9.59  ? 133  TYR A O   1 
ATOM   783  C  CB  . TYR A 1 131 ? 33.640 25.869 15.860  1.00 9.05  ? 133  TYR A CB  1 
ATOM   784  C  CG  . TYR A 1 131 ? 34.798 26.122 14.912  1.00 9.29  ? 133  TYR A CG  1 
ATOM   785  C  CD1 . TYR A 1 131 ? 34.888 27.312 14.193  1.00 9.49  ? 133  TYR A CD1 1 
ATOM   786  C  CD2 . TYR A 1 131 ? 35.806 25.172 14.733  1.00 9.64  ? 133  TYR A CD2 1 
ATOM   787  C  CE1 . TYR A 1 131 ? 35.931 27.530 13.301  1.00 10.04 ? 133  TYR A CE1 1 
ATOM   788  C  CE2 . TYR A 1 131 ? 36.871 25.403 13.870  1.00 10.12 ? 133  TYR A CE2 1 
ATOM   789  C  CZ  . TYR A 1 131 ? 36.935 26.578 13.153  1.00 10.17 ? 133  TYR A CZ  1 
ATOM   790  O  OH  . TYR A 1 131 ? 37.987 26.759 12.297  1.00 11.08 ? 133  TYR A OH  1 
ATOM   791  N  N   . LEU A 1 132 ? 31.635 23.333 16.332  1.00 9.93  ? 134  LEU A N   1 
ATOM   792  C  CA  . LEU A 1 132 ? 31.007 22.594 17.413  1.00 10.46 ? 134  LEU A CA  1 
ATOM   793  C  C   . LEU A 1 132 ? 32.043 22.399 18.518  1.00 10.45 ? 134  LEU A C   1 
ATOM   794  O  O   . LEU A 1 132 ? 33.147 21.947 18.236  1.00 10.99 ? 134  LEU A O   1 
ATOM   795  C  CB  . LEU A 1 132 ? 30.456 21.252 16.901  1.00 11.48 ? 134  LEU A CB  1 
ATOM   796  C  CG  . LEU A 1 132 ? 29.863 20.319 17.960  1.00 12.00 ? 134  LEU A CG  1 
ATOM   797  C  CD1 . LEU A 1 132 ? 28.796 19.408 17.361  1.00 13.42 ? 134  LEU A CD1 1 
ATOM   798  C  CD2 . LEU A 1 132 ? 30.950 19.459 18.626  1.00 12.08 ? 134  LEU A CD2 1 
ATOM   799  N  N   . ILE A 1 133 ? 31.660 22.736 19.758  1.00 10.17 ? 135  ILE A N   1 
ATOM   800  C  CA  . ILE A 1 133 ? 32.542 22.642 20.915  1.00 10.11 ? 135  ILE A CA  1 
ATOM   801  C  C   . ILE A 1 133 ? 31.993 21.609 21.901  1.00 10.76 ? 135  ILE A C   1 
ATOM   802  O  O   . ILE A 1 133 ? 30.801 21.614 22.219  1.00 11.25 ? 135  ILE A O   1 
ATOM   803  C  CB  . ILE A 1 133 ? 32.714 24.019 21.573  1.00 10.01 ? 135  ILE A CB  1 
ATOM   804  C  CG1 . ILE A 1 133 ? 33.118 25.074 20.536  1.00 10.07 ? 135  ILE A CG1 1 
ATOM   805  C  CG2 . ILE A 1 133 ? 33.690 23.953 22.733  1.00 9.90  ? 135  ILE A CG2 1 
ATOM   806  C  CD1 . ILE A 1 133 ? 33.215 26.463 21.104  1.00 10.24 ? 135  ILE A CD1 1 
ATOM   807  N  N   . LYS A 1 134 ? 32.867 20.690 22.327  1.00 10.99 ? 136  LYS A N   1 
ATOM   808  C  CA  . LYS A 1 134 ? 32.514 19.686 23.317  1.00 12.00 ? 136  LYS A CA  1 
ATOM   809  C  C   . LYS A 1 134 ? 33.749 19.350 24.141  1.00 12.03 ? 136  LYS A C   1 
ATOM   810  O  O   . LYS A 1 134 ? 34.861 19.687 23.747  1.00 11.25 ? 136  LYS A O   1 
ATOM   811  C  CB  . LYS A 1 134 ? 32.039 18.394 22.658  1.00 13.18 ? 136  LYS A CB  1 
ATOM   812  C  CG  . LYS A 1 134 ? 33.061 17.772 21.706  1.00 14.40 ? 136  LYS A CG  1 
ATOM   813  C  CD  . LYS A 1 134 ? 32.610 16.531 20.984  1.00 16.71 ? 136  LYS A CD  1 
ATOM   814  C  CE  . LYS A 1 134 ? 32.303 15.387 21.915  1.00 18.73 ? 136  LYS A CE  1 
ATOM   815  N  NZ  . LYS A 1 134 ? 32.349 14.103 21.173  1.00 21.45 ? 136  LYS A NZ  1 
ATOM   816  N  N   . ASP A 1 135 ? 33.527 18.671 25.273  1.00 12.61 ? 137  ASP A N   1 
ATOM   817  C  CA  . ASP A 1 135 ? 34.604 18.027 26.009  1.00 13.70 ? 137  ASP A CA  1 
ATOM   818  C  C   . ASP A 1 135 ? 34.974 16.715 25.310  1.00 14.63 ? 137  ASP A C   1 
ATOM   819  O  O   . ASP A 1 135 ? 34.111 15.971 24.828  1.00 15.20 ? 137  ASP A O   1 
ATOM   820  C  CB  . ASP A 1 135 ? 34.188 17.797 27.464  1.00 14.46 ? 137  ASP A CB  1 
ATOM   821  C  CG  . ASP A 1 135 ? 34.346 19.017 28.360  1.00 14.80 ? 137  ASP A CG  1 
ATOM   822  O  OD1 . ASP A 1 135 ? 35.505 19.332 28.680  1.00 15.52 ? 137  ASP A OD1 1 
ATOM   823  O  OD2 . ASP A 1 135 ? 33.321 19.668 28.692  1.00 15.12 ? 137  ASP A OD2 1 
ATOM   824  N  N   . SER A 1 136 ? 36.274 16.424 25.262  1.00 15.01 ? 138  SER A N   1 
ATOM   825  C  CA  . SER A 1 136 ? 36.755 15.183 24.678  1.00 16.15 ? 138  SER A CA  1 
ATOM   826  C  C   . SER A 1 136 ? 36.130 13.973 25.381  1.00 17.00 ? 138  SER A C   1 
ATOM   827  O  O   . SER A 1 136 ? 36.023 13.949 26.610  1.00 16.90 ? 138  SER A O   1 
ATOM   828  C  CB  . SER A 1 136 ? 38.255 15.156 24.741  1.00 17.05 ? 138  SER A CB  1 
ATOM   829  O  OG  . SER A 1 136 ? 38.761 13.951 24.190  1.00 19.02 ? 138  SER A OG  1 
ATOM   830  N  N   . ASN A 1 137 ? 35.726 12.964 24.607  1.00 17.74 ? 139  ASN A N   1 
ATOM   831  C  CA  . ASN A 1 137 ? 34.997 11.806 25.142  1.00 19.63 ? 139  ASN A CA  1 
ATOM   832  C  C   . ASN A 1 137 ? 35.797 11.071 26.211  1.00 20.55 ? 139  ASN A C   1 
ATOM   833  O  O   . ASN A 1 137 ? 36.945 10.709 25.987  1.00 21.84 ? 139  ASN A O   1 
ATOM   834  C  CB  . ASN A 1 137 ? 34.630 10.798 24.042  1.00 20.98 ? 139  ASN A CB  1 
ATOM   835  C  CG  . ASN A 1 137 ? 33.615 11.360 23.063  1.00 20.63 ? 139  ASN A CG  1 
ATOM   836  O  OD1 . ASN A 1 137 ? 32.959 12.359 23.335  1.00 20.21 ? 139  ASN A OD1 1 
ATOM   837  N  ND2 . ASN A 1 137 ? 33.453 10.714 21.929  1.00 21.95 ? 139  ASN A ND2 1 
ATOM   838  N  N   . GLY A 1 138 ? 35.174 10.847 27.368  1.00 21.02 ? 140  GLY A N   1 
ATOM   839  C  CA  . GLY A 1 138 ? 35.760 10.052 28.438  1.00 22.47 ? 140  GLY A CA  1 
ATOM   840  C  C   . GLY A 1 138 ? 36.837 10.791 29.243  1.00 22.14 ? 140  GLY A C   1 
ATOM   841  O  O   . GLY A 1 138 ? 37.464 10.205 30.116  1.00 23.90 ? 140  GLY A O   1 
ATOM   842  N  N   . SER A 1 139 ? 37.033 12.086 28.976  1.00 20.23 ? 141  SER A N   1 
ATOM   843  C  CA  . SER A 1 139 ? 38.140 12.847 29.540  1.00 20.15 ? 141  SER A CA  1 
ATOM   844  C  C   . SER A 1 139 ? 37.874 13.235 30.998  1.00 20.61 ? 141  SER A C   1 
ATOM   845  O  O   . SER A 1 139 ? 38.813 13.522 31.723  1.00 21.24 ? 141  SER A O   1 
ATOM   846  C  CB  . SER A 1 139 ? 38.437 14.074 28.681  1.00 18.37 ? 141  SER A CB  1 
ATOM   847  O  OG  . SER A 1 139 ? 37.334 14.976 28.675  1.00 16.77 ? 141  SER A OG  1 
ATOM   848  N  N   . LEU A 1 140 ? 36.606 13.197 31.430  1.00 21.21 ? 142  LEU A N   1 
ATOM   849  C  CA  . LEU A 1 140 ? 36.208 13.606 32.779  1.00 21.74 ? 142  LEU A CA  1 
ATOM   850  C  C   . LEU A 1 140 ? 35.607 12.445 33.582  1.00 23.43 ? 142  LEU A C   1 
ATOM   851  O  O   . LEU A 1 140 ? 34.940 12.662 34.601  1.00 23.17 ? 142  LEU A O   1 
ATOM   852  C  CB  . LEU A 1 140 ? 35.174 14.732 32.652  1.00 20.38 ? 142  LEU A CB  1 
ATOM   853  C  CG  . LEU A 1 140 ? 35.609 15.951 31.834  1.00 19.40 ? 142  LEU A CG  1 
ATOM   854  C  CD1 . LEU A 1 140 ? 34.447 16.923 31.662  1.00 18.54 ? 142  LEU A CD1 1 
ATOM   855  C  CD2 . LEU A 1 140 ? 36.809 16.661 32.470  1.00 19.39 ? 142  LEU A CD2 1 
ATOM   856  N  N   . ASP A 1 141 ? 35.823 11.201 33.144  1.00 24.65 ? 143  ASP A N   1 
ATOM   857  C  CA  . ASP A 1 141 ? 35.178 10.072 33.793  1.00 26.71 ? 143  ASP A CA  1 
ATOM   858  C  C   . ASP A 1 141 ? 35.786 9.925  35.181  1.00 28.06 ? 143  ASP A C   1 
ATOM   859  O  O   . ASP A 1 141 ? 37.009 9.876  35.326  1.00 28.88 ? 143  ASP A O   1 
ATOM   860  C  CB  . ASP A 1 141 ? 35.270 8.792  32.958  1.00 28.28 ? 143  ASP A CB  1 
ATOM   861  C  CG  . ASP A 1 141 ? 34.357 8.814  31.736  1.00 28.41 ? 143  ASP A CG  1 
ATOM   862  O  OD1 . ASP A 1 141 ? 33.595 9.802  31.571  1.00 27.06 ? 143  ASP A OD1 1 
ATOM   863  O  OD2 . ASP A 1 141 ? 34.401 7.850  30.947  1.00 30.78 ? 143  ASP A OD2 1 
ATOM   864  N  N   . ASN A 1 142 ? 34.903 9.884  36.191  1.00 29.08 ? 144  ASN A N   1 
ATOM   865  C  CA  . ASN A 1 142 ? 35.283 9.675  37.579  1.00 30.46 ? 144  ASN A CA  1 
ATOM   866  C  C   . ASN A 1 142 ? 36.158 10.815 38.094  1.00 28.72 ? 144  ASN A C   1 
ATOM   867  O  O   . ASN A 1 142 ? 36.969 10.610 38.991  1.00 29.31 ? 144  ASN A O   1 
ATOM   868  C  CB  . ASN A 1 142 ? 35.969 8.323  37.776  1.00 33.73 ? 144  ASN A CB  1 
ATOM   869  C  CG  . ASN A 1 142 ? 35.097 7.178  37.307  1.00 36.32 ? 144  ASN A CG  1 
ATOM   870  O  OD1 . ASN A 1 142 ? 35.500 6.384  36.457  1.00 38.48 ? 144  ASN A OD1 1 
ATOM   871  N  ND2 . ASN A 1 142 ? 33.887 7.106  37.838  1.00 37.65 ? 144  ASN A ND2 1 
ATOM   872  N  N   . VAL A 1 143 ? 35.963 12.023 37.557  1.00 25.93 ? 145  VAL A N   1 
ATOM   873  C  CA  . VAL A 1 143 ? 36.615 13.207 38.084  1.00 24.88 ? 145  VAL A CA  1 
ATOM   874  C  C   . VAL A 1 143 ? 35.563 14.013 38.846  1.00 23.60 ? 145  VAL A C   1 
ATOM   875  O  O   . VAL A 1 143 ? 34.547 14.421 38.278  1.00 22.14 ? 145  VAL A O   1 
ATOM   876  C  CB  . VAL A 1 143 ? 37.303 14.036 36.981  1.00 24.30 ? 145  VAL A CB  1 
ATOM   877  C  CG1 . VAL A 1 143 ? 38.076 15.215 37.569  1.00 24.89 ? 145  VAL A CG1 1 
ATOM   878  C  CG2 . VAL A 1 143 ? 38.227 13.175 36.134  1.00 24.95 ? 145  VAL A CG2 1 
ATOM   879  N  N   . LYS A 1 144 ? 35.836 14.231 40.144  1.00 23.47 ? 146  LYS A N   1 
ATOM   880  C  CA  . LYS A 1 144 ? 34.881 14.861 41.037  1.00 23.16 ? 146  LYS A CA  1 
ATOM   881  C  C   . LYS A 1 144 ? 34.758 16.342 40.709  1.00 21.41 ? 146  LYS A C   1 
ATOM   882  O  O   . LYS A 1 144 ? 35.723 16.974 40.315  1.00 20.73 ? 146  LYS A O   1 
ATOM   883  C  CB  . LYS A 1 144 ? 35.315 14.665 42.489  1.00 24.62 ? 146  LYS A CB  1 
ATOM   884  C  CG  . LYS A 1 144 ? 35.187 13.248 43.015  1.00 26.16 ? 146  LYS A CG  1 
ATOM   885  C  CD  . LYS A 1 144 ? 35.501 13.177 44.481  1.00 27.84 ? 146  LYS A CD  1 
ATOM   886  C  CE  . LYS A 1 144 ? 35.387 11.770 45.006  1.00 29.66 ? 146  LYS A CE  1 
ATOM   887  N  NZ  . LYS A 1 144 ? 35.421 11.771 46.481  1.00 31.72 ? 146  LYS A NZ  1 
ATOM   888  N  N   . GLY A 1 145 ? 33.539 16.868 40.833  1.00 21.07 ? 147  GLY A N   1 
ATOM   889  C  CA  . GLY A 1 145 ? 33.266 18.287 40.700  1.00 20.29 ? 147  GLY A CA  1 
ATOM   890  C  C   . GLY A 1 145 ? 33.443 18.814 39.281  1.00 18.99 ? 147  GLY A C   1 
ATOM   891  O  O   . GLY A 1 145 ? 33.689 19.993 39.110  1.00 18.56 ? 147  GLY A O   1 
ATOM   892  N  N   . GLN A 1 146 ? 33.312 17.949 38.287  1.00 18.45 ? 148  GLN A N   1 
ATOM   893  C  CA  . GLN A 1 146 ? 33.415 18.361 36.898  1.00 18.10 ? 148  GLN A CA  1 
ATOM   894  C  C   . GLN A 1 146 ? 32.210 17.820 36.137  1.00 16.82 ? 148  GLN A C   1 
ATOM   895  O  O   . GLN A 1 146 ? 31.494 16.961 36.628  1.00 17.08 ? 148  GLN A O   1 
ATOM   896  C  CB  . GLN A 1 146 ? 34.720 17.881 36.258  1.00 19.37 ? 148  GLN A CB  1 
ATOM   897  C  CG  . GLN A 1 146 ? 35.990 18.400 36.918  1.00 21.36 ? 148  GLN A CG  1 
ATOM   898  C  CD  . GLN A 1 146 ? 36.098 19.902 36.981  1.00 22.49 ? 148  GLN A CD  1 
ATOM   899  O  OE1 . GLN A 1 146 ? 35.975 20.619 35.991  1.00 23.86 ? 148  GLN A OE1 1 
ATOM   900  N  NE2 . GLN A 1 146 ? 36.337 20.402 38.179  1.00 25.33 ? 148  GLN A NE2 1 
ATOM   901  N  N   . ALA A 1 147 ? 31.992 18.389 34.950  1.00 15.37 ? 149  ALA A N   1 
ATOM   902  C  CA  . ALA A 1 147 ? 30.902 17.989 34.085  1.00 14.97 ? 149  ALA A CA  1 
ATOM   903  C  C   . ALA A 1 147 ? 31.268 18.286 32.640  1.00 13.38 ? 149  ALA A C   1 
ATOM   904  O  O   . ALA A 1 147 ? 32.035 19.209 32.358  1.00 12.42 ? 149  ALA A O   1 
ATOM   905  C  CB  . ALA A 1 147 ? 29.636 18.702 34.481  1.00 15.39 ? 149  ALA A CB  1 
ATOM   906  N  N   . TYR A 1 148 ? 30.714 17.466 31.735  1.00 13.18 ? 150  TYR A N   1 
ATOM   907  C  CA  . TYR A 1 148 ? 30.863 17.693 30.306  1.00 12.19 ? 150  TYR A CA  1 
ATOM   908  C  C   . TYR A 1 148 ? 30.029 18.899 29.894  1.00 11.53 ? 150  TYR A C   1 
ATOM   909  O  O   . TYR A 1 148 ? 28.906 19.065 30.334  1.00 12.03 ? 150  TYR A O   1 
ATOM   910  C  CB  . TYR A 1 148 ? 30.446 16.436 29.527  1.00 12.68 ? 150  TYR A CB  1 
ATOM   911  C  CG  . TYR A 1 148 ? 31.423 15.274 29.680  1.00 13.37 ? 150  TYR A CG  1 
ATOM   912  C  CD1 . TYR A 1 148 ? 31.323 14.405 30.753  1.00 14.47 ? 150  TYR A CD1 1 
ATOM   913  C  CD2 . TYR A 1 148 ? 32.425 15.042 28.748  1.00 12.98 ? 150  TYR A CD2 1 
ATOM   914  C  CE1 . TYR A 1 148 ? 32.179 13.335 30.907  1.00 15.31 ? 150  TYR A CE1 1 
ATOM   915  C  CE2 . TYR A 1 148 ? 33.297 13.978 28.884  1.00 13.98 ? 150  TYR A CE2 1 
ATOM   916  C  CZ  . TYR A 1 148 ? 33.173 13.130 29.970  1.00 15.15 ? 150  TYR A CZ  1 
ATOM   917  O  OH  . TYR A 1 148 ? 34.016 12.086 30.112  1.00 16.43 ? 150  TYR A OH  1 
ATOM   918  N  N   . THR A 1 149 ? 30.589 19.745 29.041  1.00 10.64 ? 151  THR A N   1 
ATOM   919  C  CA  . THR A 1 149 ? 29.868 20.904 28.553  1.00 10.76 ? 151  THR A CA  1 
ATOM   920  C  C   . THR A 1 149 ? 28.695 20.474 27.688  1.00 11.13 ? 151  THR A C   1 
ATOM   921  O  O   . THR A 1 149 ? 28.796 19.479 26.954  1.00 11.33 ? 151  THR A O   1 
ATOM   922  C  CB  . THR A 1 149 ? 30.788 21.863 27.782  1.00 9.96  ? 151  THR A CB  1 
ATOM   923  O  OG1 . THR A 1 149 ? 30.030 23.046 27.490  1.00 9.88  ? 151  THR A OG1 1 
ATOM   924  C  CG2 . THR A 1 149 ? 31.354 21.255 26.510  1.00 9.69  ? 151  THR A CG2 1 
ATOM   925  N  N   . SER A 1 150 ? 27.603 21.251 27.764  1.00 11.77 ? 152  SER A N   1 
ATOM   926  C  CA  . SER A 1 150 ? 26.580 21.210 26.724  1.00 12.46 ? 152  SER A CA  1 
ATOM   927  C  C   . SER A 1 150 ? 27.268 21.519 25.405  1.00 11.80 ? 152  SER A C   1 
ATOM   928  O  O   . SER A 1 150 ? 28.041 22.471 25.323  1.00 11.20 ? 152  SER A O   1 
ATOM   929  C  CB  . SER A 1 150 ? 25.442 22.173 26.979  1.00 13.21 ? 152  SER A CB  1 
ATOM   930  O  OG  . SER A 1 150 ? 24.772 21.862 28.174  1.00 13.97 ? 152  SER A OG  1 
ATOM   931  N  N   . ILE A 1 151 ? 27.012 20.693 24.385  1.00 12.27 ? 153  ILE A N   1 
ATOM   932  C  CA  . ILE A 1 151 ? 27.631 20.887 23.097  1.00 12.17 ? 153  ILE A CA  1 
ATOM   933  C  C   . ILE A 1 151 ? 27.171 22.253 22.592  1.00 11.60 ? 153  ILE A C   1 
ATOM   934  O  O   . ILE A 1 151 ? 25.983 22.566 22.659  1.00 12.29 ? 153  ILE A O   1 
ATOM   935  C  CB  . ILE A 1 151 ? 27.267 19.716 22.150  1.00 13.63 ? 153  ILE A CB  1 
ATOM   936  C  CG1 . ILE A 1 151 ? 28.034 18.448 22.540  1.00 13.81 ? 153  ILE A CG1 1 
ATOM   937  C  CG2 . ILE A 1 151 ? 27.507 20.076 20.692  1.00 13.37 ? 153  ILE A CG2 1 
ATOM   938  C  CD1 . ILE A 1 151 ? 27.585 17.244 21.805  1.00 15.17 ? 153  ILE A CD1 1 
ATOM   939  N  N   . MET A 1 152 ? 28.153 23.028 22.127  1.00 10.41 ? 154  MET A N   1 
ATOM   940  C  CA  . MET A 1 152 ? 27.950 24.393 21.712  1.00 10.66 ? 154  MET A CA  1 
ATOM   941  C  C   . MET A 1 152 ? 28.219 24.508 20.209  1.00 10.22 ? 154  MET A C   1 
ATOM   942  O  O   . MET A 1 152 ? 29.102 23.855 19.668  1.00 9.57  ? 154  MET A O   1 
ATOM   943  C  CB  . MET A 1 152 ? 28.930 25.323 22.436  1.00 10.49 ? 154  MET A CB  1 
ATOM   944  C  CG  . MET A 1 152 ? 28.760 25.342 23.916  1.00 11.49 ? 154  MET A CG  1 
ATOM   945  S  SD  . MET A 1 152 ? 30.148 26.145 24.751  1.00 12.34 ? 154  MET A SD  1 
ATOM   946  C  CE  . MET A 1 152 ? 29.742 27.848 24.386  1.00 13.06 ? 154  MET A CE  1 
ATOM   947  N  N   . LEU A 1 153 ? 27.439 25.357 19.542  1.00 10.74 ? 155  LEU A N   1 
ATOM   948  C  CA  . LEU A 1 153 ? 27.735 25.787 18.178  1.00 11.06 ? 155  LEU A CA  1 
ATOM   949  C  C   . LEU A 1 153 ? 28.075 27.271 18.213  1.00 11.60 ? 155  LEU A C   1 
ATOM   950  O  O   . LEU A 1 153 ? 27.295 28.050 18.774  1.00 11.87 ? 155  LEU A O   1 
ATOM   951  C  CB  . LEU A 1 153 ? 26.527 25.505 17.280  1.00 12.04 ? 155  LEU A CB  1 
ATOM   952  C  CG  . LEU A 1 153 ? 26.240 24.027 17.050  1.00 12.69 ? 155  LEU A CG  1 
ATOM   953  C  CD1 . LEU A 1 153 ? 24.898 23.835 16.361  1.00 14.18 ? 155  LEU A CD1 1 
ATOM   954  C  CD2 . LEU A 1 153 ? 27.362 23.390 16.255  1.00 12.06 ? 155  LEU A CD2 1 
ATOM   955  N  N   . GLN A 1 154 ? 29.256 27.622 17.671  1.00 11.92 ? 156  GLN A N   1 
ATOM   956  C  CA  . GLN A 1 154 ? 29.776 28.981 17.759  1.00 12.90 ? 156  GLN A CA  1 
ATOM   957  C  C   . GLN A 1 154 ? 30.460 29.393 16.454  1.00 12.34 ? 156  GLN A C   1 
ATOM   958  O  O   . GLN A 1 154 ? 31.214 28.617 15.853  1.00 11.46 ? 156  GLN A O   1 
ATOM   959  C  CB  . GLN A 1 154 ? 30.806 29.116 18.878  1.00 14.39 ? 156  GLN A CB  1 
ATOM   960  C  CG  . GLN A 1 154 ? 30.245 28.841 20.268  1.00 17.15 ? 156  GLN A CG  1 
ATOM   961  C  CD  . GLN A 1 154 ? 29.217 29.886 20.647  1.00 20.46 ? 156  GLN A CD  1 
ATOM   962  O  OE1 . GLN A 1 154 ? 29.458 31.089 20.481  1.00 20.31 ? 156  GLN A OE1 1 
ATOM   963  N  NE2 . GLN A 1 154 ? 28.053 29.415 21.098  1.00 21.54 ? 156  GLN A NE2 1 
ATOM   964  N  N   . VAL A 1 155 ? 30.209 30.649 16.053  1.00 12.35 ? 157  VAL A N   1 
ATOM   965  C  CA  . VAL A 1 155 ? 30.969 31.277 14.991  1.00 12.24 ? 157  VAL A CA  1 
ATOM   966  C  C   . VAL A 1 155 ? 32.259 31.802 15.607  1.00 12.33 ? 157  VAL A C   1 
ATOM   967  O  O   . VAL A 1 155 ? 32.225 32.443 16.656  1.00 12.56 ? 157  VAL A O   1 
ATOM   968  C  CB  . VAL A 1 155 ? 30.160 32.407 14.333  1.00 12.85 ? 157  VAL A CB  1 
ATOM   969  C  CG1 . VAL A 1 155 ? 30.979 33.180 13.313  1.00 13.33 ? 157  VAL A CG1 1 
ATOM   970  C  CG2 . VAL A 1 155 ? 28.893 31.873 13.690  1.00 13.32 ? 157  VAL A CG2 1 
ATOM   971  N  N   . ALA A 1 156 ? 33.393 31.486 14.983  1.00 12.31 ? 158  ALA A N   1 
ATOM   972  C  CA  . ALA A 1 156 ? 34.666 32.013 15.451  1.00 13.16 ? 158  ALA A CA  1 
ATOM   973  C  C   . ALA A 1 156 ? 34.783 33.474 15.002  1.00 13.52 ? 158  ALA A C   1 
ATOM   974  O  O   . ALA A 1 156 ? 34.985 33.744 13.816  1.00 13.68 ? 158  ALA A O   1 
ATOM   975  C  CB  . ALA A 1 156 ? 35.806 31.149 14.927  1.00 13.06 ? 158  ALA A CB  1 
ATOM   976  N  N   . LYS A 1 157 ? 34.635 34.419 15.946  1.00 13.67 ? 159  LYS A N   1 
ATOM   977  C  CA  . LYS A 1 157 ? 34.552 35.828 15.566  1.00 14.90 ? 159  LYS A CA  1 
ATOM   978  C  C   . LYS A 1 157 ? 35.263 36.760 16.550  1.00 14.75 ? 159  LYS A C   1 
ATOM   979  O  O   . LYS A 1 157 ? 34.835 37.892 16.731  1.00 15.58 ? 159  LYS A O   1 
ATOM   980  C  CB  . LYS A 1 157 ? 33.083 36.220 15.400  1.00 15.91 ? 159  LYS A CB  1 
ATOM   981  C  CG  . LYS A 1 157 ? 32.200 35.948 16.603  1.00 16.50 ? 159  LYS A CG  1 
ATOM   982  C  CD  . LYS A 1 157 ? 30.907 36.713 16.484  1.00 19.34 ? 159  LYS A CD  1 
ATOM   983  C  CE  . LYS A 1 157 ? 29.942 36.491 17.628  1.00 20.65 ? 159  LYS A CE  1 
ATOM   984  N  NZ  . LYS A 1 157 ? 29.130 35.295 17.332  1.00 21.50 ? 159  LYS A NZ  1 
ATOM   985  N  N   . ASP A 1 158 ? 36.343 36.278 17.164  1.00 14.34 ? 160  ASP A N   1 
ATOM   986  C  CA  . ASP A 1 158 ? 37.199 37.060 18.043  1.00 15.59 ? 160  ASP A CA  1 
ATOM   987  C  C   . ASP A 1 158 ? 36.383 37.609 19.215  1.00 16.52 ? 160  ASP A C   1 
ATOM   988  O  O   . ASP A 1 158 ? 36.419 38.797 19.504  1.00 18.03 ? 160  ASP A O   1 
ATOM   989  C  CB  . ASP A 1 158 ? 37.899 38.173 17.257  1.00 16.52 ? 160  ASP A CB  1 
ATOM   990  C  CG  . ASP A 1 158 ? 38.787 37.667 16.129  1.00 16.34 ? 160  ASP A CG  1 
ATOM   991  O  OD1 . ASP A 1 158 ? 39.133 36.470 16.150  1.00 15.44 ? 160  ASP A OD1 1 
ATOM   992  O  OD2 . ASP A 1 158 ? 39.103 38.468 15.232  1.00 16.99 ? 160  ASP A OD2 1 
ATOM   993  N  N   . THR A 1 159 ? 35.570 36.755 19.831  1.00 16.24 ? 161  THR A N   1 
ATOM   994  C  CA  . THR A 1 159 ? 34.784 37.174 20.971  1.00 17.52 ? 161  THR A CA  1 
ATOM   995  C  C   . THR A 1 159 ? 34.906 36.118 22.058  1.00 17.31 ? 161  THR A C   1 
ATOM   996  O  O   . THR A 1 159 ? 35.340 35.001 21.821  1.00 16.18 ? 161  THR A O   1 
ATOM   997  C  CB  . THR A 1 159 ? 33.312 37.427 20.621  1.00 18.62 ? 161  THR A CB  1 
ATOM   998  O  OG1 . THR A 1 159 ? 32.782 36.205 20.092  1.00 19.13 ? 161  THR A OG1 1 
ATOM   999  C  CG2 . THR A 1 159 ? 33.112 38.571 19.644  1.00 20.12 ? 161  THR A CG2 1 
ATOM   1000 N  N   . THR A 1 160 ? 34.536 36.522 23.261  1.00 18.89 ? 162  THR A N   1 
ATOM   1001 C  CA  . THR A 1 160 ? 34.500 35.648 24.413  1.00 20.04 ? 162  THR A CA  1 
ATOM   1002 C  C   . THR A 1 160 ? 33.067 35.155 24.599  1.00 21.07 ? 162  THR A C   1 
ATOM   1003 O  O   . THR A 1 160 ? 32.120 35.933 24.473  1.00 24.25 ? 162  THR A O   1 
ATOM   1004 C  CB  . THR A 1 160 ? 34.987 36.404 25.655  1.00 22.67 ? 162  THR A CB  1 
ATOM   1005 O  OG1 . THR A 1 160 ? 33.956 37.348 25.917  1.00 24.98 ? 162  THR A OG1 1 
ATOM   1006 C  CG2 . THR A 1 160 ? 36.303 37.131 25.452  1.00 23.15 ? 162  THR A CG2 1 
ATOM   1007 N  N   . ILE A 1 161 ? 32.912 33.869 24.927  1.00 19.06 ? 163  ILE A N   1 
ATOM   1008 C  CA  . ILE A 1 161 ? 31.613 33.321 25.282  1.00 18.75 ? 163  ILE A CA  1 
ATOM   1009 C  C   . ILE A 1 161 ? 31.777 32.459 26.529  1.00 17.17 ? 163  ILE A C   1 
ATOM   1010 O  O   . ILE A 1 161 ? 32.874 31.987 26.805  1.00 17.02 ? 163  ILE A O   1 
ATOM   1011 C  CB  . ILE A 1 161 ? 31.046 32.496 24.120  1.00 19.17 ? 163  ILE A CB  1 
ATOM   1012 C  CG1 . ILE A 1 161 ? 31.881 31.239 23.933  1.00 18.93 ? 163  ILE A CG1 1 
ATOM   1013 C  CG2 . ILE A 1 161 ? 31.008 33.332 22.859  1.00 21.16 ? 163  ILE A CG2 1 
ATOM   1014 C  CD1 . ILE A 1 161 ? 31.513 30.447 22.756  1.00 20.04 ? 163  ILE A CD1 1 
ATOM   1015 N  N   . ALA A 1 162 ? 30.695 32.326 27.302  1.00 16.47 ? 164  ALA A N   1 
ATOM   1016 C  CA  . ALA A 1 162 ? 30.695 31.457 28.456  1.00 15.87 ? 164  ALA A CA  1 
ATOM   1017 C  C   . ALA A 1 162 ? 30.527 30.008 27.996  1.00 14.15 ? 164  ALA A C   1 
ATOM   1018 O  O   . ALA A 1 162 ? 29.644 29.684 27.214  1.00 13.47 ? 164  ALA A O   1 
ATOM   1019 C  CB  . ALA A 1 162 ? 29.619 31.920 29.414  1.00 17.33 ? 164  ALA A CB  1 
ATOM   1020 N  N   . ILE A 1 163 ? 31.401 29.110 28.478  1.00 13.58 ? 165  ILE A N   1 
ATOM   1021 C  CA  . ILE A 1 163 ? 31.208 27.690 28.255  1.00 12.76 ? 165  ILE A CA  1 
ATOM   1022 C  C   . ILE A 1 163 ? 29.870 27.282 28.874  1.00 13.27 ? 165  ILE A C   1 
ATOM   1023 O  O   . ILE A 1 163 ? 29.558 27.695 29.995  1.00 13.17 ? 165  ILE A O   1 
ATOM   1024 C  CB  . ILE A 1 163 ? 32.398 26.871 28.791  1.00 12.94 ? 165  ILE A CB  1 
ATOM   1025 C  CG1 . ILE A 1 163 ? 32.342 25.423 28.313  1.00 13.31 ? 165  ILE A CG1 1 
ATOM   1026 C  CG2 . ILE A 1 163 ? 32.507 26.951 30.311  1.00 13.41 ? 165  ILE A CG2 1 
ATOM   1027 C  CD1 . ILE A 1 163 ? 33.692 24.848 27.982  1.00 13.60 ? 165  ILE A CD1 1 
ATOM   1028 N  N   . LYS A 1 164 ? 29.067 26.501 28.123  1.00 13.16 ? 166  LYS A N   1 
ATOM   1029 C  CA  . LYS A 1 164 ? 27.779 26.011 28.607  1.00 15.23 ? 166  LYS A CA  1 
ATOM   1030 C  C   . LYS A 1 164 ? 28.023 24.757 29.445  1.00 14.16 ? 166  LYS A C   1 
ATOM   1031 O  O   . LYS A 1 164 ? 27.652 23.640 29.085  1.00 14.21 ? 166  LYS A O   1 
ATOM   1032 C  CB  . LYS A 1 164 ? 26.793 25.730 27.462  1.00 17.34 ? 166  LYS A CB  1 
ATOM   1033 C  CG  . LYS A 1 164 ? 25.983 26.939 27.027  1.00 21.11 ? 166  LYS A CG  1 
ATOM   1034 C  CD  . LYS A 1 164 ? 25.115 26.716 25.789  1.00 24.85 ? 166  LYS A CD  1 
ATOM   1035 C  CE  . LYS A 1 164 ? 24.042 25.659 25.990  1.00 28.63 ? 166  LYS A CE  1 
ATOM   1036 N  NZ  . LYS A 1 164 ? 23.277 25.893 27.241  1.00 31.94 ? 166  LYS A NZ  1 
ATOM   1037 N  N   . SER A 1 165 ? 28.725 24.968 30.548  1.00 18.28 ? 167  SER A N   1 
ATOM   1038 C  CA  . SER A 1 165 ? 29.107 23.893 31.434  1.00 17.09 ? 167  SER A CA  1 
ATOM   1039 C  C   . SER A 1 165 ? 29.060 24.423 32.855  1.00 16.33 ? 167  SER A C   1 
ATOM   1040 O  O   . SER A 1 165 ? 29.515 25.533 33.115  1.00 16.55 ? 167  SER A O   1 
ATOM   1041 C  CB  . SER A 1 165 ? 30.489 23.432 31.092  1.00 17.89 ? 167  SER A CB  1 
ATOM   1042 O  OG  . SER A 1 165 ? 30.858 22.289 31.828  1.00 17.12 ? 167  SER A OG  1 
ATOM   1043 N  N   . ASP A 1 166 ? 28.526 23.600 33.749  1.00 15.30 ? 168  ASP A N   1 
ATOM   1044 C  CA  . ASP A 1 166 ? 28.478 23.950 35.144  1.00 15.15 ? 168  ASP A CA  1 
ATOM   1045 C  C   . ASP A 1 166 ? 28.294 22.658 35.928  1.00 14.22 ? 168  ASP A C   1 
ATOM   1046 O  O   . ASP A 1 166 ? 27.927 21.619 35.373  1.00 13.68 ? 168  ASP A O   1 
ATOM   1047 C  CB  . ASP A 1 166 ? 27.355 24.956 35.384  1.00 15.36 ? 168  ASP A CB  1 
ATOM   1048 C  CG  . ASP A 1 166 ? 27.402 25.680 36.708  1.00 15.56 ? 168  ASP A CG  1 
ATOM   1049 O  OD1 . ASP A 1 166 ? 28.469 25.640 37.361  1.00 15.98 ? 168  ASP A OD1 1 
ATOM   1050 O  OD2 . ASP A 1 166 ? 26.371 26.270 37.057  1.00 15.84 ? 168  ASP A OD2 1 
ATOM   1051 N  N   . VAL A 1 167 ? 28.549 22.756 37.228  1.00 13.77 ? 169  VAL A N   1 
ATOM   1052 C  CA  . VAL A 1 167 ? 28.339 21.655 38.137  1.00 13.22 ? 169  VAL A CA  1 
ATOM   1053 C  C   . VAL A 1 167 ? 27.412 22.109 39.257  1.00 12.67 ? 169  VAL A C   1 
ATOM   1054 O  O   . VAL A 1 167 ? 27.385 23.282 39.626  1.00 13.05 ? 169  VAL A O   1 
ATOM   1055 C  CB  . VAL A 1 167 ? 29.673 21.157 38.702  1.00 13.67 ? 169  VAL A CB  1 
ATOM   1056 C  CG1 . VAL A 1 167 ? 30.530 20.541 37.597  1.00 14.26 ? 169  VAL A CG1 1 
ATOM   1057 C  CG2 . VAL A 1 167 ? 30.402 22.273 39.425  1.00 14.37 ? 169  VAL A CG2 1 
ATOM   1058 N  N   . PRO A 1 168 ? 26.590 21.199 39.819  1.00 12.03 ? 170  PRO A N   1 
ATOM   1059 C  CA  . PRO A 1 168 ? 25.854 21.509 41.040  1.00 11.65 ? 170  PRO A CA  1 
ATOM   1060 C  C   . PRO A 1 168 ? 26.846 21.655 42.186  1.00 11.61 ? 170  PRO A C   1 
ATOM   1061 O  O   . PRO A 1 168 ? 27.921 21.081 42.123  1.00 11.76 ? 170  PRO A O   1 
ATOM   1062 C  CB  . PRO A 1 168 ? 24.960 20.273 41.250  1.00 11.03 ? 170  PRO A CB  1 
ATOM   1063 C  CG  . PRO A 1 168 ? 25.719 19.150 40.556  1.00 11.11 ? 170  PRO A CG  1 
ATOM   1064 C  CD  . PRO A 1 168 ? 26.363 19.817 39.365  1.00 11.93 ? 170  PRO A CD  1 
ATOM   1065 N  N   . THR A 1 169 ? 26.419 22.324 43.262  1.00 11.70 ? 171  THR A N   1 
ATOM   1066 C  CA  . THR A 1 169 ? 27.223 22.466 44.460  1.00 12.04 ? 171  THR A CA  1 
ATOM   1067 C  C   . THR A 1 169 ? 26.426 21.924 45.640  1.00 11.51 ? 171  THR A C   1 
ATOM   1068 O  O   . THR A 1 169 ? 25.191 21.964 45.637  1.00 11.23 ? 171  THR A O   1 
ATOM   1069 C  CB  . THR A 1 169 ? 27.661 23.910 44.741  1.00 12.75 ? 171  THR A CB  1 
ATOM   1070 O  OG1 . THR A 1 169 ? 26.513 24.655 45.162  1.00 13.06 ? 171  THR A OG1 1 
ATOM   1071 C  CG2 . THR A 1 169 ? 28.304 24.578 43.540  1.00 13.57 ? 171  THR A CG2 1 
ATOM   1072 N  N   . LEU A 1 170 ? 27.140 21.383 46.630  1.00 11.32 ? 172  LEU A N   1 
ATOM   1073 C  CA  . LEU A 1 170 ? 26.482 20.974 47.857  1.00 11.12 ? 172  LEU A CA  1 
ATOM   1074 C  C   . LEU A 1 170 ? 27.221 21.561 49.051  1.00 11.40 ? 172  LEU A C   1 
ATOM   1075 O  O   . LEU A 1 170 ? 28.443 21.514 49.111  1.00 12.04 ? 172  LEU A O   1 
ATOM   1076 C  CB  . LEU A 1 170 ? 26.429 19.447 47.915  1.00 11.06 ? 172  LEU A CB  1 
ATOM   1077 C  CG  . LEU A 1 170 ? 25.720 18.839 49.133  1.00 10.79 ? 172  LEU A CG  1 
ATOM   1078 C  CD1 . LEU A 1 170 ? 25.191 17.452 48.805  1.00 10.78 ? 172  LEU A CD1 1 
ATOM   1079 C  CD2 . LEU A 1 170 ? 26.630 18.742 50.353  1.00 10.99 ? 172  LEU A CD2 1 
ATOM   1080 N  N   . THR A 1 171 ? 26.460 22.102 50.006  1.00 11.76 ? 173  THR A N   1 
ATOM   1081 C  CA  . THR A 1 171 ? 27.017 22.643 51.241  1.00 11.64 ? 173  THR A CA  1 
ATOM   1082 C  C   . THR A 1 171 ? 26.262 22.048 52.425  1.00 11.43 ? 173  THR A C   1 
ATOM   1083 O  O   . THR A 1 171 ? 25.057 22.233 52.529  1.00 11.85 ? 173  THR A O   1 
ATOM   1084 C  CB  . THR A 1 171 ? 26.904 24.168 51.297  1.00 12.05 ? 173  THR A CB  1 
ATOM   1085 O  OG1 . THR A 1 171 ? 27.301 24.720 50.041  1.00 12.85 ? 173  THR A OG1 1 
ATOM   1086 C  CG2 . THR A 1 171 ? 27.742 24.744 52.411  1.00 11.94 ? 173  THR A CG2 1 
ATOM   1087 N  N   . LYS A 1 172 ? 26.976 21.341 53.309  1.00 11.11 ? 174  LYS A N   1 
ATOM   1088 C  CA  . LYS A 1 172 ? 26.401 20.849 54.549  1.00 10.42 ? 174  LYS A CA  1 
ATOM   1089 C  C   . LYS A 1 172 ? 26.704 21.862 55.643  1.00 10.74 ? 174  LYS A C   1 
ATOM   1090 O  O   . LYS A 1 172 ? 27.841 22.305 55.774  1.00 11.18 ? 174  LYS A O   1 
ATOM   1091 C  CB  . LYS A 1 172 ? 26.991 19.488 54.911  1.00 10.09 ? 174  LYS A CB  1 
ATOM   1092 C  CG  . LYS A 1 172 ? 26.407 18.892 56.166  1.00 9.89  ? 174  LYS A CG  1 
ATOM   1093 C  CD  . LYS A 1 172 ? 26.987 17.597 56.563  1.00 9.84  ? 174  LYS A CD  1 
ATOM   1094 C  CE  . LYS A 1 172 ? 26.205 17.030 57.733  1.00 9.67  ? 174  LYS A CE  1 
ATOM   1095 N  NZ  . LYS A 1 172 ? 26.849 15.802 58.190  1.00 9.92  ? 174  LYS A NZ  1 
ATOM   1096 N  N   . GLN A 1 173 ? 25.679 22.230 56.417  1.00 10.74 ? 175  GLN A N   1 
ATOM   1097 C  CA  . GLN A 1 173 ? 25.835 23.196 57.491  1.00 10.98 ? 175  GLN A CA  1 
ATOM   1098 C  C   . GLN A 1 173 ? 25.046 22.729 58.712  1.00 10.72 ? 175  GLN A C   1 
ATOM   1099 O  O   . GLN A 1 173 ? 24.155 21.886 58.609  1.00 10.42 ? 175  GLN A O   1 
ATOM   1100 C  CB  . GLN A 1 173 ? 25.355 24.584 57.059  1.00 11.66 ? 175  GLN A CB  1 
ATOM   1101 C  CG  . GLN A 1 173 ? 26.160 25.198 55.913  1.00 12.16 ? 175  GLN A CG  1 
ATOM   1102 C  CD  . GLN A 1 173 ? 25.582 26.497 55.433  1.00 12.74 ? 175  GLN A CD  1 
ATOM   1103 O  OE1 . GLN A 1 173 ? 24.443 26.557 54.997  1.00 12.37 ? 175  GLN A OE1 1 
ATOM   1104 N  NE2 . GLN A 1 173 ? 26.365 27.555 55.518  1.00 13.97 ? 175  GLN A NE2 1 
ATOM   1105 N  N   . VAL A 1 174 ? 25.385 23.320 59.846  1.00 10.80 ? 176  VAL A N   1 
ATOM   1106 C  CA  . VAL A 1 174 ? 24.705 23.086 61.101  1.00 11.18 ? 176  VAL A CA  1 
ATOM   1107 C  C   . VAL A 1 174 ? 24.257 24.440 61.645  1.00 11.83 ? 176  VAL A C   1 
ATOM   1108 O  O   . VAL A 1 174 ? 24.966 25.437 61.488  1.00 12.13 ? 176  VAL A O   1 
ATOM   1109 C  CB  . VAL A 1 174 ? 25.621 22.334 62.090  1.00 11.24 ? 176  VAL A CB  1 
ATOM   1110 C  CG1 . VAL A 1 174 ? 26.873 23.118 62.461  1.00 11.50 ? 176  VAL A CG1 1 
ATOM   1111 C  CG2 . VAL A 1 174 ? 24.873 21.934 63.356  1.00 11.84 ? 176  VAL A CG2 1 
ATOM   1112 N  N   . LYS A 1 175 ? 23.072 24.478 62.270  1.00 12.39 ? 177  LYS A N   1 
ATOM   1113 C  CA  . LYS A 1 175 ? 22.554 25.690 62.874  1.00 13.58 ? 177  LYS A CA  1 
ATOM   1114 C  C   . LYS A 1 175 ? 23.451 26.103 64.032  1.00 13.97 ? 177  LYS A C   1 
ATOM   1115 O  O   . LYS A 1 175 ? 23.718 25.291 64.914  1.00 13.50 ? 177  LYS A O   1 
ATOM   1116 C  CB  . LYS A 1 175 ? 21.126 25.504 63.396  1.00 14.54 ? 177  LYS A CB  1 
ATOM   1117 C  CG  . LYS A 1 175 ? 20.388 26.797 63.723  1.00 16.14 ? 177  LYS A CG  1 
ATOM   1118 C  CD  . LYS A 1 175 ? 19.106 26.578 64.496  1.00 17.48 ? 177  LYS A CD  1 
ATOM   1119 C  CE  . LYS A 1 175 ? 19.305 26.288 65.975  1.00 18.33 ? 177  LYS A CE  1 
ATOM   1120 N  NZ  . LYS A 1 175 ? 19.688 27.496 66.744  1.00 19.39 ? 177  LYS A NZ  1 
ATOM   1121 N  N   . ALA A 1 176 ? 23.906 27.360 64.015  1.00 14.54 ? 178  ALA A N   1 
ATOM   1122 C  CA  . ALA A 1 176 ? 24.699 27.914 65.097  1.00 15.94 ? 178  ALA A CA  1 
ATOM   1123 C  C   . ALA A 1 176 ? 23.940 27.741 66.409  1.00 16.38 ? 178  ALA A C   1 
ATOM   1124 O  O   . ALA A 1 176 ? 22.722 27.871 66.451  1.00 16.26 ? 178  ALA A O   1 
ATOM   1125 C  CB  . ALA A 1 176 ? 25.015 29.369 64.837  1.00 17.22 ? 178  ALA A CB  1 
ATOM   1126 N  N   . SER A 1 177 ? 24.684 27.418 67.464  1.00 17.34 ? 179  SER A N   1 
ATOM   1127 C  CA  . SER A 1 177 ? 24.131 27.251 68.798  1.00 18.50 ? 179  SER A CA  1 
ATOM   1128 C  C   . SER A 1 177 ? 23.379 28.498 69.252  1.00 20.41 ? 179  SER A C   1 
ATOM   1129 O  O   . SER A 1 177 ? 22.323 28.381 69.857  1.00 21.37 ? 179  SER A O   1 
ATOM   1130 C  CB  . SER A 1 177 ? 25.226 26.899 69.768  1.00 18.55 ? 179  SER A CB  1 
ATOM   1131 O  OG  . SER A 1 177 ? 24.693 26.734 71.064  1.00 20.31 ? 179  SER A OG  1 
ATOM   1132 N  N   . ASN A 1 178 ? 23.937 29.686 68.968  1.00 22.30 ? 180  ASN A N   1 
ATOM   1133 C  CA  . ASN A 1 178 ? 23.494 30.927 69.579  1.00 24.95 ? 180  ASN A CA  1 
ATOM   1134 C  C   . ASN A 1 178 ? 22.765 31.832 68.581  1.00 26.02 ? 180  ASN A C   1 
ATOM   1135 O  O   . ASN A 1 178 ? 22.583 33.005 68.867  1.00 27.35 ? 180  ASN A O   1 
ATOM   1136 C  CB  . ASN A 1 178 ? 24.692 31.625 70.229  1.00 26.24 ? 180  ASN A CB  1 
ATOM   1137 C  CG  . ASN A 1 178 ? 25.356 30.722 71.253  1.00 27.03 ? 180  ASN A CG  1 
ATOM   1138 O  OD1 . ASN A 1 178 ? 26.533 30.375 71.150  1.00 27.93 ? 180  ASN A OD1 1 
ATOM   1139 N  ND2 . ASN A 1 178 ? 24.579 30.296 72.232  1.00 27.15 ? 180  ASN A ND2 1 
ATOM   1140 N  N   . SER A 1 179 ? 22.312 31.290 67.444  1.00 25.56 ? 181  SER A N   1 
ATOM   1141 C  CA  . SER A 1 179 ? 21.604 32.085 66.453  1.00 27.41 ? 181  SER A CA  1 
ATOM   1142 C  C   . SER A 1 179 ? 20.891 31.168 65.461  1.00 26.06 ? 181  SER A C   1 
ATOM   1143 O  O   . SER A 1 179 ? 20.995 29.948 65.548  1.00 24.29 ? 181  SER A O   1 
ATOM   1144 C  CB  . SER A 1 179 ? 22.552 33.037 65.739  1.00 28.61 ? 181  SER A CB  1 
ATOM   1145 O  OG  . SER A 1 179 ? 23.605 32.333 65.101  1.00 29.21 ? 181  SER A OG  1 
ATOM   1146 N  N   . GLU A 1 180 ? 20.186 31.767 64.498  1.00 28.04 ? 182  GLU A N   1 
ATOM   1147 C  CA  . GLU A 1 180 ? 19.347 31.016 63.572  1.00 28.09 ? 182  GLU A CA  1 
ATOM   1148 C  C   . GLU A 1 180 ? 20.086 30.661 62.283  1.00 26.17 ? 182  GLU A C   1 
ATOM   1149 O  O   . GLU A 1 180 ? 19.583 29.889 61.465  1.00 23.55 ? 182  GLU A O   1 
ATOM   1150 C  CB  . GLU A 1 180 ? 18.091 31.822 63.243  1.00 31.50 ? 182  GLU A CB  1 
ATOM   1151 C  CG  . GLU A 1 180 ? 17.166 32.004 64.429  1.00 34.99 ? 182  GLU A CG  1 
ATOM   1152 C  CD  . GLU A 1 180 ? 16.526 30.737 64.973  1.00 37.57 ? 182  GLU A CD  1 
ATOM   1153 O  OE1 . GLU A 1 180 ? 16.615 29.688 64.300  1.00 37.74 ? 182  GLU A OE1 1 
ATOM   1154 O  OE2 . GLU A 1 180 ? 15.966 30.792 66.094  1.00 42.63 ? 182  GLU A OE2 1 
ATOM   1155 N  N   . ASN A 1 181 ? 21.282 31.202 62.086  1.00 25.30 ? 183  ASN A N   1 
ATOM   1156 C  CA  . ASN A 1 181 ? 21.952 30.988 60.819  1.00 25.65 ? 183  ASN A CA  1 
ATOM   1157 C  C   . ASN A 1 181 ? 22.752 29.693 60.849  1.00 22.00 ? 183  ASN A C   1 
ATOM   1158 O  O   . ASN A 1 181 ? 23.135 29.200 61.908  1.00 21.26 ? 183  ASN A O   1 
ATOM   1159 C  CB  . ASN A 1 181 ? 22.827 32.174 60.414  1.00 31.11 ? 183  ASN A CB  1 
ATOM   1160 C  CG  . ASN A 1 181 ? 23.872 32.510 61.450  1.00 34.08 ? 183  ASN A CG  1 
ATOM   1161 O  OD1 . ASN A 1 181 ? 23.527 32.897 62.571  1.00 39.21 ? 183  ASN A OD1 1 
ATOM   1162 N  ND2 . ASN A 1 181 ? 25.136 32.387 61.067  1.00 34.50 ? 183  ASN A ND2 1 
ATOM   1163 N  N   . TYR A 1 182 ? 22.999 29.170 59.652  1.00 18.64 ? 184  TYR A N   1 
ATOM   1164 C  CA  . TYR A 1 182 ? 23.664 27.899 59.433  1.00 16.45 ? 184  TYR A CA  1 
ATOM   1165 C  C   . TYR A 1 182 ? 25.125 28.170 59.097  1.00 16.01 ? 184  TYR A C   1 
ATOM   1166 O  O   . TYR A 1 182 ? 25.421 29.033 58.274  1.00 17.41 ? 184  TYR A O   1 
ATOM   1167 C  CB  . TYR A 1 182 ? 22.896 27.163 58.330  1.00 15.52 ? 184  TYR A CB  1 
ATOM   1168 C  CG  . TYR A 1 182 ? 21.687 26.419 58.879  1.00 14.95 ? 184  TYR A CG  1 
ATOM   1169 C  CD1 . TYR A 1 182 ? 21.806 25.128 59.380  1.00 13.87 ? 184  TYR A CD1 1 
ATOM   1170 C  CD2 . TYR A 1 182 ? 20.455 27.051 58.979  1.00 15.64 ? 184  TYR A CD2 1 
ATOM   1171 C  CE1 . TYR A 1 182 ? 20.710 24.462 59.893  1.00 13.97 ? 184  TYR A CE1 1 
ATOM   1172 C  CE2 . TYR A 1 182 ? 19.356 26.407 59.507  1.00 15.64 ? 184  TYR A CE2 1 
ATOM   1173 C  CZ  . TYR A 1 182 ? 19.497 25.119 59.985  1.00 14.95 ? 184  TYR A CZ  1 
ATOM   1174 O  OH  . TYR A 1 182 ? 18.429 24.451 60.476  1.00 15.81 ? 184  TYR A OH  1 
ATOM   1175 N  N   . ILE A 1 183 ? 26.020 27.415 59.736  1.00 14.52 ? 185  ILE A N   1 
ATOM   1176 C  CA  . ILE A 1 183 ? 27.454 27.605 59.615  1.00 14.01 ? 185  ILE A CA  1 
ATOM   1177 C  C   . ILE A 1 183 ? 28.096 26.228 59.528  1.00 12.39 ? 185  ILE A C   1 
ATOM   1178 O  O   . ILE A 1 183 ? 27.413 25.215 59.596  1.00 11.94 ? 185  ILE A O   1 
ATOM   1179 C  CB  . ILE A 1 183 ? 27.999 28.451 60.792  1.00 14.79 ? 185  ILE A CB  1 
ATOM   1180 C  CG1 . ILE A 1 183 ? 27.577 27.904 62.162  1.00 14.36 ? 185  ILE A CG1 1 
ATOM   1181 C  CG2 . ILE A 1 183 ? 27.593 29.906 60.628  1.00 15.96 ? 185  ILE A CG2 1 
ATOM   1182 C  CD1 . ILE A 1 183 ? 28.185 28.671 63.356  1.00 15.15 ? 185  ILE A CD1 1 
ATOM   1183 N  N   . SER A 1 184 ? 29.422 26.183 59.400  1.00 12.03 ? 186  SER A N   1 
ATOM   1184 C  CA  A SER A 1 184 ? 30.101 24.909 59.221  0.50 11.25 ? 186  SER A CA  1 
ATOM   1185 C  CA  B SER A 1 184 ? 30.136 24.925 59.226  0.50 11.29 ? 186  SER A CA  1 
ATOM   1186 C  C   . SER A 1 184 ? 30.319 24.195 60.555  1.00 11.13 ? 186  SER A C   1 
ATOM   1187 O  O   . SER A 1 184 ? 30.381 22.974 60.571  1.00 10.87 ? 186  SER A O   1 
ATOM   1188 C  CB  A SER A 1 184 ? 31.388 25.093 58.483  0.50 11.63 ? 186  SER A CB  1 
ATOM   1189 C  CB  B SER A 1 184 ? 31.476 25.155 58.601  0.50 11.74 ? 186  SER A CB  1 
ATOM   1190 O  OG  A SER A 1 184 ? 31.118 25.425 57.126  0.50 11.38 ? 186  SER A OG  1 
ATOM   1191 O  OG  B SER A 1 184 ? 32.275 25.992 59.417  0.50 12.35 ? 186  SER A OG  1 
ATOM   1192 N  N   . ALA A 1 185 ? 30.449 24.948 61.651  1.00 11.31 ? 187  ALA A N   1 
ATOM   1193 C  CA  . ALA A 1 185 ? 30.806 24.356 62.936  1.00 11.38 ? 187  ALA A CA  1 
ATOM   1194 C  C   . ALA A 1 185 ? 30.231 25.160 64.085  1.00 11.78 ? 187  ALA A C   1 
ATOM   1195 O  O   . ALA A 1 185 ? 30.208 26.395 64.061  1.00 12.39 ? 187  ALA A O   1 
ATOM   1196 C  CB  . ALA A 1 185 ? 32.307 24.230 63.065  1.00 11.84 ? 187  ALA A CB  1 
ATOM   1197 N  N   . THR A 1 186 ? 29.866 24.449 65.160  1.00 11.55 ? 188  THR A N   1 
ATOM   1198 C  CA  . THR A 1 186 ? 29.403 25.106 66.361  1.00 12.01 ? 188  THR A CA  1 
ATOM   1199 C  C   . THR A 1 186 ? 29.588 24.133 67.520  1.00 12.13 ? 188  THR A C   1 
ATOM   1200 O  O   . THR A 1 186 ? 30.143 23.042 67.341  1.00 11.51 ? 188  THR A O   1 
ATOM   1201 C  CB  . THR A 1 186 ? 27.963 25.603 66.187  1.00 12.09 ? 188  THR A CB  1 
ATOM   1202 O  OG1 . THR A 1 186 ? 27.606 26.444 67.287  1.00 12.86 ? 188  THR A OG1 1 
ATOM   1203 C  CG2 . THR A 1 186 ? 26.959 24.489 66.039  1.00 11.66 ? 188  THR A CG2 1 
ATOM   1204 N  N   . ASP A 1 187 ? 29.094 24.532 68.685  1.00 12.75 ? 189  ASP A N   1 
ATOM   1205 C  CA  . ASP A 1 187 ? 29.104 23.643 69.833  1.00 13.06 ? 189  ASP A CA  1 
ATOM   1206 C  C   . ASP A 1 187 ? 27.666 23.401 70.265  1.00 13.02 ? 189  ASP A C   1 
ATOM   1207 O  O   . ASP A 1 187 ? 26.822 24.282 70.106  1.00 13.84 ? 189  ASP A O   1 
ATOM   1208 C  CB  . ASP A 1 187 ? 29.992 24.190 70.951  1.00 14.04 ? 189  ASP A CB  1 
ATOM   1209 C  CG  . ASP A 1 187 ? 29.657 25.573 71.495  1.00 15.39 ? 189  ASP A CG  1 
ATOM   1210 O  OD1 . ASP A 1 187 ? 28.857 26.289 70.883  1.00 16.50 ? 189  ASP A OD1 1 
ATOM   1211 O  OD2 . ASP A 1 187 ? 30.227 25.933 72.553  1.00 16.29 ? 189  ASP A OD2 1 
ATOM   1212 N  N   . TYR A 1 188 ? 27.408 22.222 70.848  1.00 12.63 ? 190  TYR A N   1 
ATOM   1213 C  CA  . TYR A 1 188 ? 26.079 21.857 71.303  1.00 12.45 ? 190  TYR A CA  1 
ATOM   1214 C  C   . TYR A 1 188 ? 26.198 21.064 72.603  1.00 12.67 ? 190  TYR A C   1 
ATOM   1215 O  O   . TYR A 1 188 ? 27.267 20.570 72.952  1.00 12.23 ? 190  TYR A O   1 
ATOM   1216 C  CB  . TYR A 1 188 ? 25.301 21.103 70.223  1.00 11.95 ? 190  TYR A CB  1 
ATOM   1217 C  CG  . TYR A 1 188 ? 24.481 21.972 69.276  1.00 11.91 ? 190  TYR A CG  1 
ATOM   1218 C  CD1 . TYR A 1 188 ? 23.362 22.664 69.731  1.00 12.81 ? 190  TYR A CD1 1 
ATOM   1219 C  CD2 . TYR A 1 188 ? 24.819 22.117 67.937  1.00 11.50 ? 190  TYR A CD2 1 
ATOM   1220 C  CE1 . TYR A 1 188 ? 22.594 23.463 68.893  1.00 13.06 ? 190  TYR A CE1 1 
ATOM   1221 C  CE2 . TYR A 1 188 ? 24.084 22.946 67.096  1.00 11.63 ? 190  TYR A CE2 1 
ATOM   1222 C  CZ  . TYR A 1 188 ? 22.958 23.602 67.572  1.00 12.52 ? 190  TYR A CZ  1 
ATOM   1223 O  OH  . TYR A 1 188 ? 22.192 24.439 66.797  1.00 13.00 ? 190  TYR A OH  1 
ATOM   1224 N  N   . ALA A 1 189 ? 25.077 20.995 73.314  1.00 13.15 ? 191  ALA A N   1 
ATOM   1225 C  CA  . ALA A 1 189 ? 25.009 20.269 74.569  1.00 13.84 ? 191  ALA A CA  1 
ATOM   1226 C  C   . ALA A 1 189 ? 24.137 19.028 74.382  1.00 14.04 ? 191  ALA A C   1 
ATOM   1227 O  O   . ALA A 1 189 ? 23.474 18.871 73.366  1.00 13.77 ? 191  ALA A O   1 
ATOM   1228 C  CB  . ALA A 1 189 ? 24.493 21.193 75.652  1.00 14.72 ? 191  ALA A CB  1 
ATOM   1229 N  N   . ILE A 1 190 ? 24.169 18.143 75.379  1.00 14.86 ? 192  ILE A N   1 
ATOM   1230 C  CA  . ILE A 1 190 ? 23.443 16.884 75.361  1.00 15.41 ? 192  ILE A CA  1 
ATOM   1231 C  C   . ILE A 1 190 ? 21.934 17.126 75.371  1.00 15.86 ? 192  ILE A C   1 
ATOM   1232 O  O   . ILE A 1 190 ? 21.197 16.282 74.881  1.00 15.89 ? 192  ILE A O   1 
ATOM   1233 C  CB  . ILE A 1 190 ? 23.898 16.001 76.555  1.00 16.38 ? 192  ILE A CB  1 
ATOM   1234 C  CG1 . ILE A 1 190 ? 23.475 14.535 76.411  1.00 17.01 ? 192  ILE A CG1 1 
ATOM   1235 C  CG2 . ILE A 1 190 ? 23.431 16.572 77.882  1.00 17.34 ? 192  ILE A CG2 1 
ATOM   1236 C  CD1 . ILE A 1 190 ? 24.244 13.768 75.359  1.00 16.54 ? 192  ILE A CD1 1 
ATOM   1237 N  N   . TRP A 1 191 ? 21.472 18.253 75.935  1.00 16.30 ? 193  TRP A N   1 
ATOM   1238 C  CA  . TRP A 1 191 ? 20.050 18.549 76.013  1.00 17.32 ? 193  TRP A CA  1 
ATOM   1239 C  C   . TRP A 1 191 ? 19.533 19.206 74.734  1.00 17.20 ? 193  TRP A C   1 
ATOM   1240 O  O   . TRP A 1 191 ? 18.342 19.420 74.612  1.00 18.27 ? 193  TRP A O   1 
ATOM   1241 C  CB  . TRP A 1 191 ? 19.736 19.406 77.251  1.00 18.46 ? 193  TRP A CB  1 
ATOM   1242 C  CG  . TRP A 1 191 ? 20.561 20.655 77.334  1.00 18.47 ? 193  TRP A CG  1 
ATOM   1243 C  CD1 . TRP A 1 191 ? 20.354 21.821 76.665  1.00 18.57 ? 193  TRP A CD1 1 
ATOM   1244 C  CD2 . TRP A 1 191 ? 21.784 20.835 78.080  1.00 18.84 ? 193  TRP A CD2 1 
ATOM   1245 N  NE1 . TRP A 1 191 ? 21.344 22.718 76.959  1.00 18.63 ? 193  TRP A NE1 1 
ATOM   1246 C  CE2 . TRP A 1 191 ? 22.233 22.143 77.824  1.00 18.83 ? 193  TRP A CE2 1 
ATOM   1247 C  CE3 . TRP A 1 191 ? 22.535 20.029 78.943  1.00 19.40 ? 193  TRP A CE3 1 
ATOM   1248 C  CZ2 . TRP A 1 191 ? 23.398 22.659 78.393  1.00 19.29 ? 193  TRP A CZ2 1 
ATOM   1249 C  CZ3 . TRP A 1 191 ? 23.687 20.541 79.510  1.00 19.48 ? 193  TRP A CZ3 1 
ATOM   1250 C  CH2 . TRP A 1 191 ? 24.110 21.841 79.237  1.00 19.34 ? 193  TRP A CH2 1 
ATOM   1251 N  N   . ASP A 1 192 ? 20.412 19.516 73.773  1.00 16.27 ? 194  ASP A N   1 
ATOM   1252 C  CA  . ASP A 1 192 ? 20.042 20.250 72.565  1.00 15.86 ? 194  ASP A CA  1 
ATOM   1253 C  C   . ASP A 1 192 ? 19.677 19.300 71.428  1.00 15.22 ? 194  ASP A C   1 
ATOM   1254 O  O   . ASP A 1 192 ? 20.139 18.166 71.383  1.00 14.92 ? 194  ASP A O   1 
ATOM   1255 C  CB  . ASP A 1 192 ? 21.176 21.153 72.082  1.00 15.03 ? 194  ASP A CB  1 
ATOM   1256 C  CG  . ASP A 1 192 ? 21.473 22.322 72.994  1.00 15.87 ? 194  ASP A CG  1 
ATOM   1257 O  OD1 . ASP A 1 192 ? 20.525 22.976 73.436  1.00 17.02 ? 194  ASP A OD1 1 
ATOM   1258 O  OD2 . ASP A 1 192 ? 22.652 22.553 73.258  1.00 15.82 ? 194  ASP A OD2 1 
ATOM   1259 N  N   . THR A 1 193 ? 18.804 19.794 70.543  1.00 15.26 ? 195  THR A N   1 
ATOM   1260 C  CA  . THR A 1 193 ? 18.587 19.241 69.221  1.00 14.72 ? 195  THR A CA  1 
ATOM   1261 C  C   . THR A 1 193 ? 19.524 19.926 68.232  1.00 13.71 ? 195  THR A C   1 
ATOM   1262 O  O   . THR A 1 193 ? 19.615 21.148 68.220  1.00 14.21 ? 195  THR A O   1 
ATOM   1263 C  CB  . THR A 1 193 ? 17.124 19.396 68.819  1.00 15.52 ? 195  THR A CB  1 
ATOM   1264 O  OG1 . THR A 1 193 ? 16.380 18.705 69.814  1.00 16.71 ? 195  THR A OG1 1 
ATOM   1265 C  CG2 . THR A 1 193 ? 16.802 18.768 67.484  1.00 15.21 ? 195  THR A CG2 1 
ATOM   1266 N  N   . VAL A 1 194 ? 20.268 19.131 67.457  1.00 12.73 ? 196  VAL A N   1 
ATOM   1267 C  CA  . VAL A 1 194 ? 21.256 19.642 66.521  1.00 12.03 ? 196  VAL A CA  1 
ATOM   1268 C  C   . VAL A 1 194 ? 20.650 19.674 65.112  1.00 11.75 ? 196  VAL A C   1 
ATOM   1269 O  O   . VAL A 1 194 ? 20.567 18.649 64.459  1.00 11.30 ? 196  VAL A O   1 
ATOM   1270 C  CB  . VAL A 1 194 ? 22.526 18.775 66.548  1.00 11.54 ? 196  VAL A CB  1 
ATOM   1271 C  CG1 . VAL A 1 194 ? 23.617 19.354 65.673  1.00 11.07 ? 196  VAL A CG1 1 
ATOM   1272 C  CG2 . VAL A 1 194 ? 23.039 18.601 67.966  1.00 11.99 ? 196  VAL A CG2 1 
ATOM   1273 N  N   . PRO A 1 195 ? 20.213 20.838 64.586  1.00 12.04 ? 197  PRO A N   1 
ATOM   1274 C  CA  . PRO A 1 195 ? 19.676 20.920 63.218  1.00 11.75 ? 197  PRO A CA  1 
ATOM   1275 C  C   . PRO A 1 195 ? 20.754 21.004 62.147  1.00 10.96 ? 197  PRO A C   1 
ATOM   1276 O  O   . PRO A 1 195 ? 21.678 21.816 62.237  1.00 10.52 ? 197  PRO A O   1 
ATOM   1277 C  CB  . PRO A 1 195 ? 18.868 22.231 63.221  1.00 12.51 ? 197  PRO A CB  1 
ATOM   1278 C  CG  . PRO A 1 195 ? 18.861 22.673 64.679  1.00 13.21 ? 197  PRO A CG  1 
ATOM   1279 C  CD  . PRO A 1 195 ? 20.140 22.127 65.275  1.00 12.55 ? 197  PRO A CD  1 
ATOM   1280 N  N   . PHE A 1 196 ? 20.599 20.178 61.111  1.00 10.53 ? 198  PHE A N   1 
ATOM   1281 C  CA  . PHE A 1 196 ? 21.515 20.174 59.995  1.00 10.40 ? 198  PHE A CA  1 
ATOM   1282 C  C   . PHE A 1 196 ? 20.742 20.593 58.746  1.00 10.59 ? 198  PHE A C   1 
ATOM   1283 O  O   . PHE A 1 196 ? 19.545 20.410 58.678  1.00 10.44 ? 198  PHE A O   1 
ATOM   1284 C  CB  . PHE A 1 196 ? 22.111 18.779 59.783  1.00 10.52 ? 198  PHE A CB  1 
ATOM   1285 C  CG  . PHE A 1 196 ? 23.133 18.351 60.800  1.00 10.81 ? 198  PHE A CG  1 
ATOM   1286 C  CD1 . PHE A 1 196 ? 24.456 18.761 60.689  1.00 10.86 ? 198  PHE A CD1 1 
ATOM   1287 C  CD2 . PHE A 1 196 ? 22.756 17.582 61.884  1.00 11.59 ? 198  PHE A CD2 1 
ATOM   1288 C  CE1 . PHE A 1 196 ? 25.407 18.361 61.614  1.00 11.30 ? 198  PHE A CE1 1 
ATOM   1289 C  CE2 . PHE A 1 196 ? 23.702 17.202 62.829  1.00 11.63 ? 198  PHE A CE2 1 
ATOM   1290 C  CZ  . PHE A 1 196 ? 25.023 17.581 62.683  1.00 11.48 ? 198  PHE A CZ  1 
ATOM   1291 N  N   . GLN A 1 197 ? 21.462 21.111 57.761  1.00 10.90 ? 199  GLN A N   1 
ATOM   1292 C  CA  . GLN A 1 197 ? 20.870 21.608 56.529  1.00 11.42 ? 199  GLN A CA  1 
ATOM   1293 C  C   . GLN A 1 197 ? 21.882 21.423 55.415  1.00 11.17 ? 199  GLN A C   1 
ATOM   1294 O  O   . GLN A 1 197 ? 23.001 21.927 55.507  1.00 11.10 ? 199  GLN A O   1 
ATOM   1295 C  CB  . GLN A 1 197 ? 20.487 23.081 56.668  1.00 12.45 ? 199  GLN A CB  1 
ATOM   1296 C  CG  . GLN A 1 197 ? 19.795 23.659 55.437  1.00 13.12 ? 199  GLN A CG  1 
ATOM   1297 C  CD  . GLN A 1 197 ? 19.454 25.110 55.658  1.00 14.24 ? 199  GLN A CD  1 
ATOM   1298 O  OE1 . GLN A 1 197 ? 18.320 25.452 55.984  1.00 14.92 ? 199  GLN A OE1 1 
ATOM   1299 N  NE2 . GLN A 1 197 ? 20.442 25.986 55.525  1.00 14.83 ? 199  GLN A NE2 1 
ATOM   1300 N  N   . ILE A 1 198 ? 21.475 20.667 54.389  1.00 10.84 ? 200  ILE A N   1 
ATOM   1301 C  CA  . ILE A 1 198 ? 22.288 20.466 53.202  1.00 10.87 ? 200  ILE A CA  1 
ATOM   1302 C  C   . ILE A 1 198 ? 21.637 21.273 52.078  1.00 10.82 ? 200  ILE A C   1 
ATOM   1303 O  O   . ILE A 1 198 ? 20.494 21.028 51.743  1.00 11.06 ? 200  ILE A O   1 
ATOM   1304 C  CB  . ILE A 1 198 ? 22.411 18.973 52.852  1.00 11.05 ? 200  ILE A CB  1 
ATOM   1305 C  CG1 . ILE A 1 198 ? 23.017 18.187 54.022  1.00 11.60 ? 200  ILE A CG1 1 
ATOM   1306 C  CG2 . ILE A 1 198 ? 23.198 18.764 51.567  1.00 11.18 ? 200  ILE A CG2 1 
ATOM   1307 C  CD1 . ILE A 1 198 ? 22.875 16.718 53.919  1.00 11.68 ? 200  ILE A CD1 1 
ATOM   1308 N  N   . THR A 1 199 ? 22.377 22.228 51.522  1.00 10.97 ? 201  THR A N   1 
ATOM   1309 C  CA  . THR A 1 199 ? 21.874 23.033 50.416  1.00 11.43 ? 201  THR A CA  1 
ATOM   1310 C  C   . THR A 1 199 ? 22.561 22.598 49.131  1.00 11.35 ? 201  THR A C   1 
ATOM   1311 O  O   . THR A 1 199 ? 23.786 22.688 49.025  1.00 11.18 ? 201  THR A O   1 
ATOM   1312 C  CB  . THR A 1 199 ? 22.091 24.522 50.702  1.00 12.36 ? 201  THR A CB  1 
ATOM   1313 O  OG1 . THR A 1 199 ? 21.356 24.825 51.894  1.00 12.35 ? 201  THR A OG1 1 
ATOM   1314 C  CG2 . THR A 1 199 ? 21.663 25.416 49.551  1.00 13.32 ? 201  THR A CG2 1 
ATOM   1315 N  N   . VAL A 1 200 ? 21.746 22.254 48.125  1.00 11.36 ? 202  VAL A N   1 
ATOM   1316 C  CA  . VAL A 1 200 ? 22.243 21.910 46.800  1.00 11.22 ? 202  VAL A CA  1 
ATOM   1317 C  C   . VAL A 1 200 ? 21.785 22.955 45.781  1.00 11.43 ? 202  VAL A C   1 
ATOM   1318 O  O   . VAL A 1 200 ? 20.601 23.240 45.667  1.00 11.12 ? 202  VAL A O   1 
ATOM   1319 C  CB  . VAL A 1 200 ? 21.795 20.486 46.421  1.00 11.40 ? 202  VAL A CB  1 
ATOM   1320 C  CG1 . VAL A 1 200 ? 22.205 20.095 45.014  1.00 11.62 ? 202  VAL A CG1 1 
ATOM   1321 C  CG2 . VAL A 1 200 ? 22.325 19.459 47.409  1.00 11.33 ? 202  VAL A CG2 1 
ATOM   1322 N  N   . THR A 1 201 ? 22.741 23.466 45.001  1.00 11.50 ? 203  THR A N   1 
ATOM   1323 C  CA  . THR A 1 201 ? 22.435 24.304 43.852  1.00 12.20 ? 203  THR A CA  1 
ATOM   1324 C  C   . THR A 1 201 ? 22.522 23.434 42.605  1.00 11.65 ? 203  THR A C   1 
ATOM   1325 O  O   . THR A 1 201 ? 23.308 22.481 42.563  1.00 11.43 ? 203  THR A O   1 
ATOM   1326 C  CB  . THR A 1 201 ? 23.369 25.529 43.769  1.00 12.93 ? 203  THR A CB  1 
ATOM   1327 O  OG1 . THR A 1 201 ? 24.715 25.078 43.569  1.00 13.02 ? 203  THR A OG1 1 
ATOM   1328 C  CG2 . THR A 1 201 ? 23.319 26.398 45.004  1.00 13.06 ? 203  THR A CG2 1 
ATOM   1329 N  N   . LEU A 1 202 ? 21.735 23.773 41.585  1.00 11.62 ? 204  LEU A N   1 
ATOM   1330 C  CA  . LEU A 1 202 ? 21.739 23.021 40.341  1.00 11.51 ? 204  LEU A CA  1 
ATOM   1331 C  C   . LEU A 1 202 ? 22.577 23.753 39.294  1.00 11.84 ? 204  LEU A C   1 
ATOM   1332 O  O   . LEU A 1 202 ? 22.784 24.960 39.391  1.00 12.15 ? 204  LEU A O   1 
ATOM   1333 C  CB  . LEU A 1 202 ? 20.288 22.826 39.885  1.00 11.78 ? 204  LEU A CB  1 
ATOM   1334 C  CG  . LEU A 1 202 ? 19.468 21.889 40.775  1.00 11.52 ? 204  LEU A CG  1 
ATOM   1335 C  CD1 . LEU A 1 202 ? 18.044 21.748 40.277  1.00 12.01 ? 204  LEU A CD1 1 
ATOM   1336 C  CD2 . LEU A 1 202 ? 20.110 20.517 40.858  1.00 11.04 ? 204  LEU A CD2 1 
ATOM   1337 N  N   . PRO A 1 203 ? 23.103 23.056 38.260  1.00 11.55 ? 205  PRO A N   1 
ATOM   1338 C  CA  . PRO A 1 203 ? 23.940 23.702 37.269  1.00 12.10 ? 205  PRO A CA  1 
ATOM   1339 C  C   . PRO A 1 203 ? 23.086 24.613 36.393  1.00 12.76 ? 205  PRO A C   1 
ATOM   1340 O  O   . PRO A 1 203 ? 21.887 24.403 36.222  1.00 12.46 ? 205  PRO A O   1 
ATOM   1341 C  CB  . PRO A 1 203 ? 24.558 22.527 36.480  1.00 12.03 ? 205  PRO A CB  1 
ATOM   1342 C  CG  . PRO A 1 203 ? 23.494 21.460 36.573  1.00 11.53 ? 205  PRO A CG  1 
ATOM   1343 C  CD  . PRO A 1 203 ? 22.944 21.624 37.973  1.00 11.26 ? 205  PRO A CD  1 
ATOM   1344 N  N   . SER A 1 204 ? 23.753 25.632 35.845  1.00 13.69 ? 206  SER A N   1 
ATOM   1345 C  CA  . SER A 1 204 ? 23.096 26.638 35.033  1.00 14.47 ? 206  SER A CA  1 
ATOM   1346 C  C   . SER A 1 204 ? 22.525 25.994 33.776  1.00 14.71 ? 206  SER A C   1 
ATOM   1347 O  O   . SER A 1 204 ? 21.617 26.571 33.183  1.00 15.80 ? 206  SER A O   1 
ATOM   1348 C  CB  . SER A 1 204 ? 24.048 27.757 34.729  1.00 15.32 ? 206  SER A CB  1 
ATOM   1349 O  OG  . SER A 1 204 ? 25.205 27.292 34.049  1.00 15.39 ? 206  SER A OG  1 
ATOM   1350 N  N   . ASN A 1 205 ? 23.083 24.850 33.342  1.00 14.17 ? 207  ASN A N   1 
ATOM   1351 C  CA  . ASN A 1 205 ? 22.654 24.169 32.137  1.00 14.53 ? 207  ASN A CA  1 
ATOM   1352 C  C   . ASN A 1 205 ? 21.748 22.975 32.443  1.00 14.03 ? 207  ASN A C   1 
ATOM   1353 O  O   . ASN A 1 205 ? 21.734 22.026 31.659  1.00 14.07 ? 207  ASN A O   1 
ATOM   1354 C  CB  . ASN A 1 205 ? 23.837 23.704 31.276  1.00 14.88 ? 207  ASN A CB  1 
ATOM   1355 C  CG  . ASN A 1 205 ? 24.747 22.666 31.918  1.00 14.12 ? 207  ASN A CG  1 
ATOM   1356 O  OD1 . ASN A 1 205 ? 24.697 22.434 33.123  1.00 13.54 ? 207  ASN A OD1 1 
ATOM   1357 N  ND2 . ASN A 1 205 ? 25.598 22.045 31.109  1.00 14.46 ? 207  ASN A ND2 1 
ATOM   1358 N  N   . TYR A 1 206 ? 21.049 23.004 33.591  1.00 13.87 ? 208  TYR A N   1 
ATOM   1359 C  CA  . TYR A 1 206 ? 20.123 21.968 34.023  1.00 13.70 ? 208  TYR A CA  1 
ATOM   1360 C  C   . TYR A 1 206 ? 19.073 21.702 32.943  1.00 14.44 ? 208  TYR A C   1 
ATOM   1361 O  O   . TYR A 1 206 ? 18.729 20.554 32.727  1.00 14.31 ? 208  TYR A O   1 
ATOM   1362 C  CB  . TYR A 1 206 ? 19.447 22.371 35.339  1.00 13.49 ? 208  TYR A CB  1 
ATOM   1363 C  CG  . TYR A 1 206 ? 18.422 21.380 35.866  1.00 13.37 ? 208  TYR A CG  1 
ATOM   1364 C  CD1 . TYR A 1 206 ? 18.813 20.196 36.471  1.00 12.74 ? 208  TYR A CD1 1 
ATOM   1365 C  CD2 . TYR A 1 206 ? 17.050 21.623 35.757  1.00 14.26 ? 208  TYR A CD2 1 
ATOM   1366 C  CE1 . TYR A 1 206 ? 17.880 19.290 36.968  1.00 12.69 ? 208  TYR A CE1 1 
ATOM   1367 C  CE2 . TYR A 1 206 ? 16.110 20.722 36.244  1.00 14.17 ? 208  TYR A CE2 1 
ATOM   1368 C  CZ  . TYR A 1 206 ? 16.528 19.545 36.840  1.00 13.46 ? 208  TYR A CZ  1 
ATOM   1369 O  OH  . TYR A 1 206 ? 15.583 18.675 37.319  1.00 14.51 ? 208  TYR A OH  1 
ATOM   1370 N  N   . GLY A 1 207 ? 18.574 22.756 32.277  1.00 15.95 ? 209  GLY A N   1 
ATOM   1371 C  CA  . GLY A 1 207 ? 17.571 22.641 31.215  1.00 16.82 ? 209  GLY A CA  1 
ATOM   1372 C  C   . GLY A 1 207 ? 17.964 21.759 30.023  1.00 17.66 ? 209  GLY A C   1 
ATOM   1373 O  O   . GLY A 1 207 ? 17.108 21.141 29.397  1.00 18.79 ? 209  GLY A O   1 
ATOM   1374 N  N   . ASP A 1 208 ? 19.257 21.712 29.688  1.00 17.90 ? 210  ASP A N   1 
ATOM   1375 C  CA  . ASP A 1 208 ? 19.784 20.872 28.616  1.00 18.24 ? 210  ASP A CA  1 
ATOM   1376 C  C   . ASP A 1 208 ? 19.686 19.373 28.926  1.00 17.38 ? 210  ASP A C   1 
ATOM   1377 O  O   . ASP A 1 208 ? 19.725 18.563 28.023  1.00 17.21 ? 210  ASP A O   1 
ATOM   1378 C  CB  . ASP A 1 208 ? 21.235 21.263 28.296  1.00 19.01 ? 210  ASP A CB  1 
ATOM   1379 C  CG  . ASP A 1 208 ? 21.405 22.672 27.745  1.00 20.45 ? 210  ASP A CG  1 
ATOM   1380 O  OD1 . ASP A 1 208 ? 20.377 23.259 27.338  1.00 22.20 ? 210  ASP A OD1 1 
ATOM   1381 O  OD2 . ASP A 1 208 ? 22.556 23.190 27.760  1.00 20.57 ? 210  ASP A OD2 1 
ATOM   1382 N  N   . PHE A 1 209 ? 19.608 18.969 30.192  1.00 16.02 ? 211  PHE A N   1 
ATOM   1383 C  CA  . PHE A 1 209 ? 19.484 17.555 30.520  1.00 16.23 ? 211  PHE A CA  1 
ATOM   1384 C  C   . PHE A 1 209 ? 18.055 17.079 30.253  1.00 17.31 ? 211  PHE A C   1 
ATOM   1385 O  O   . PHE A 1 209 ? 17.121 17.791 30.607  1.00 18.37 ? 211  PHE A O   1 
ATOM   1386 C  CB  . PHE A 1 209 ? 19.864 17.319 31.990  1.00 14.82 ? 211  PHE A CB  1 
ATOM   1387 C  CG  . PHE A 1 209 ? 21.322 17.522 32.314  1.00 14.27 ? 211  PHE A CG  1 
ATOM   1388 C  CD1 . PHE A 1 209 ? 21.841 18.791 32.512  1.00 13.99 ? 211  PHE A CD1 1 
ATOM   1389 C  CD2 . PHE A 1 209 ? 22.181 16.434 32.423  1.00 13.94 ? 211  PHE A CD2 1 
ATOM   1390 C  CE1 . PHE A 1 209 ? 23.182 18.968 32.826  1.00 13.90 ? 211  PHE A CE1 1 
ATOM   1391 C  CE2 . PHE A 1 209 ? 23.520 16.615 32.726  1.00 13.81 ? 211  PHE A CE2 1 
ATOM   1392 C  CZ  . PHE A 1 209 ? 24.020 17.884 32.921  1.00 13.77 ? 211  PHE A CZ  1 
ATOM   1393 N  N   . SER A 1 210 ? 17.902 15.883 29.670  1.00 18.23 ? 212  SER A N   1 
ATOM   1394 C  CA  . SER A 1 210 ? 16.614 15.222 29.469  1.00 19.41 ? 212  SER A CA  1 
ATOM   1395 C  C   . SER A 1 210 ? 16.152 14.533 30.750  1.00 19.01 ? 212  SER A C   1 
ATOM   1396 O  O   . SER A 1 210 ? 14.960 14.482 31.038  1.00 18.65 ? 212  SER A O   1 
ATOM   1397 C  CB  . SER A 1 210 ? 16.698 14.210 28.359  1.00 20.94 ? 212  SER A CB  1 
ATOM   1398 O  OG  . SER A 1 210 ? 17.096 14.842 27.161  1.00 23.77 ? 212  SER A OG  1 
ATOM   1399 N  N   . LYS A 1 211 ? 17.121 13.978 31.492  1.00 18.98 ? 213  LYS A N   1 
ATOM   1400 C  CA  . LYS A 1 211 ? 16.905 13.439 32.829  1.00 19.08 ? 213  LYS A CA  1 
ATOM   1401 C  C   . LYS A 1 211 ? 18.093 13.821 33.726  1.00 17.27 ? 213  LYS A C   1 
ATOM   1402 O  O   . LYS A 1 211 ? 19.182 14.100 33.220  1.00 16.61 ? 213  LYS A O   1 
ATOM   1403 C  CB  . LYS A 1 211 ? 16.694 11.931 32.732  1.00 21.71 ? 213  LYS A CB  1 
ATOM   1404 C  CG  . LYS A 1 211 ? 17.782 11.170 31.997  1.00 24.68 ? 213  LYS A CG  1 
ATOM   1405 C  CD  . LYS A 1 211 ? 17.516 9.682  31.959  1.00 28.11 ? 213  LYS A CD  1 
ATOM   1406 C  CE  . LYS A 1 211 ? 18.778 8.889  31.702  1.00 30.50 ? 213  LYS A CE  1 
ATOM   1407 N  NZ  . LYS A 1 211 ? 19.314 9.181  30.353  1.00 30.88 ? 213  LYS A NZ  1 
ATOM   1408 N  N   . TYR A 1 212 ? 17.895 13.792 35.057  1.00 15.27 ? 214  TYR A N   1 
ATOM   1409 C  CA  . TYR A 1 212 ? 18.917 14.256 35.976  1.00 13.73 ? 214  TYR A CA  1 
ATOM   1410 C  C   . TYR A 1 212 ? 18.952 13.369 37.225  1.00 13.53 ? 214  TYR A C   1 
ATOM   1411 O  O   . TYR A 1 212 ? 18.059 13.419 38.082  1.00 12.86 ? 214  TYR A O   1 
ATOM   1412 C  CB  . TYR A 1 212 ? 18.709 15.726 36.348  1.00 12.87 ? 214  TYR A CB  1 
ATOM   1413 C  CG  . TYR A 1 212 ? 19.987 16.404 36.824  1.00 12.17 ? 214  TYR A CG  1 
ATOM   1414 C  CD1 . TYR A 1 212 ? 20.939 16.865 35.913  1.00 12.16 ? 214  TYR A CD1 1 
ATOM   1415 C  CD2 . TYR A 1 212 ? 20.271 16.516 38.181  1.00 11.31 ? 214  TYR A CD2 1 
ATOM   1416 C  CE1 . TYR A 1 212 ? 22.098 17.502 36.342  1.00 11.80 ? 214  TYR A CE1 1 
ATOM   1417 C  CE2 . TYR A 1 212 ? 21.429 17.130 38.618  1.00 11.14 ? 214  TYR A CE2 1 
ATOM   1418 C  CZ  . TYR A 1 212 ? 22.343 17.631 37.705  1.00 11.18 ? 214  TYR A CZ  1 
ATOM   1419 O  OH  . TYR A 1 212 ? 23.493 18.185 38.170  1.00 10.76 ? 214  TYR A OH  1 
ATOM   1420 N  N   . HIS A 1 213 ? 20.007 12.555 37.305  1.00 13.81 ? 215  HIS A N   1 
ATOM   1421 C  CA  . HIS A 1 213 ? 20.254 11.730 38.478  1.00 13.98 ? 215  HIS A CA  1 
ATOM   1422 C  C   . HIS A 1 213 ? 20.666 12.651 39.626  1.00 12.67 ? 215  HIS A C   1 
ATOM   1423 O  O   . HIS A 1 213 ? 21.391 13.598 39.395  1.00 11.92 ? 215  HIS A O   1 
ATOM   1424 C  CB  . HIS A 1 213 ? 21.334 10.676 38.203  1.00 15.43 ? 215  HIS A CB  1 
ATOM   1425 C  CG  . HIS A 1 213 ? 21.560 9.789  39.387  1.00 17.13 ? 215  HIS A CG  1 
ATOM   1426 N  ND1 . HIS A 1 213 ? 20.652 8.823  39.763  1.00 19.02 ? 215  HIS A ND1 1 
ATOM   1427 C  CD2 . HIS A 1 213 ? 22.556 9.750  40.319  1.00 17.98 ? 215  HIS A CD2 1 
ATOM   1428 C  CE1 . HIS A 1 213 ? 21.093 8.219  40.876  1.00 19.51 ? 215  HIS A CE1 1 
ATOM   1429 N  NE2 . HIS A 1 213 ? 22.246 8.782  41.235  1.00 18.35 ? 215  HIS A NE2 1 
ATOM   1430 N  N   . PHE A 1 214 ? 20.192 12.367 40.843  1.00 12.54 ? 216  PHE A N   1 
ATOM   1431 C  CA  . PHE A 1 214 ? 20.394 13.240 41.977  1.00 12.12 ? 216  PHE A CA  1 
ATOM   1432 C  C   . PHE A 1 214 ? 20.399 12.391 43.240  1.00 12.36 ? 216  PHE A C   1 
ATOM   1433 O  O   . PHE A 1 214 ? 19.386 11.785 43.611  1.00 12.93 ? 216  PHE A O   1 
ATOM   1434 C  CB  . PHE A 1 214 ? 19.306 14.310 42.032  1.00 12.28 ? 216  PHE A CB  1 
ATOM   1435 C  CG  . PHE A 1 214 ? 19.464 15.328 43.134  1.00 12.19 ? 216  PHE A CG  1 
ATOM   1436 C  CD1 . PHE A 1 214 ? 19.073 15.044 44.431  1.00 12.13 ? 216  PHE A CD1 1 
ATOM   1437 C  CD2 . PHE A 1 214 ? 19.953 16.595 42.858  1.00 12.46 ? 216  PHE A CD2 1 
ATOM   1438 C  CE1 . PHE A 1 214 ? 19.214 15.973 45.445  1.00 11.99 ? 216  PHE A CE1 1 
ATOM   1439 C  CE2 . PHE A 1 214 ? 20.068 17.530 43.869  1.00 12.19 ? 216  PHE A CE2 1 
ATOM   1440 C  CZ  . PHE A 1 214 ? 19.709 17.218 45.163  1.00 12.02 ? 216  PHE A CZ  1 
ATOM   1441 N  N   . SER A 1 215 ? 21.566 12.317 43.866  1.00 12.16 ? 217  SER A N   1 
ATOM   1442 C  CA  . SER A 1 215 ? 21.712 11.485 45.052  1.00 12.21 ? 217  SER A CA  1 
ATOM   1443 C  C   . SER A 1 215 ? 22.672 12.157 46.024  1.00 11.53 ? 217  SER A C   1 
ATOM   1444 O  O   . SER A 1 215 ? 23.849 12.285 45.742  1.00 11.63 ? 217  SER A O   1 
ATOM   1445 C  CB  . SER A 1 215 ? 22.166 10.091 44.678  1.00 12.90 ? 217  SER A CB  1 
ATOM   1446 O  OG  . SER A 1 215 ? 22.299 9.300  45.843  1.00 13.40 ? 217  SER A OG  1 
ATOM   1447 N  N   . VAL A 1 216 ? 22.148 12.556 47.184  1.00 11.47 ? 218  VAL A N   1 
ATOM   1448 C  CA  . VAL A 1 216 ? 22.931 13.111 48.273  1.00 11.39 ? 218  VAL A CA  1 
ATOM   1449 C  C   . VAL A 1 216 ? 23.252 12.003 49.271  1.00 11.76 ? 218  VAL A C   1 
ATOM   1450 O  O   . VAL A 1 216 ? 22.344 11.298 49.694  1.00 11.47 ? 218  VAL A O   1 
ATOM   1451 C  CB  . VAL A 1 216 ? 22.147 14.242 48.960  1.00 11.25 ? 218  VAL A CB  1 
ATOM   1452 C  CG1 . VAL A 1 216 ? 22.780 14.677 50.277  1.00 11.14 ? 218  VAL A CG1 1 
ATOM   1453 C  CG2 . VAL A 1 216 ? 21.974 15.427 48.019  1.00 11.57 ? 218  VAL A CG2 1 
ATOM   1454 N  N   . LYS A 1 217 ? 24.542 11.864 49.607  1.00 12.07 ? 219  LYS A N   1 
ATOM   1455 C  CA  A LYS A 1 217 ? 25.006 10.919 50.609  0.50 12.21 ? 219  LYS A CA  1 
ATOM   1456 C  CA  B LYS A 1 217 ? 24.977 10.920 50.628  0.50 12.61 ? 219  LYS A CA  1 
ATOM   1457 C  C   . LYS A 1 217 ? 25.601 11.699 51.780  1.00 11.82 ? 219  LYS A C   1 
ATOM   1458 O  O   . LYS A 1 217 ? 26.437 12.570 51.566  1.00 11.23 ? 219  LYS A O   1 
ATOM   1459 C  CB  A LYS A 1 217 ? 26.032 9.980  49.961  0.50 13.01 ? 219  LYS A CB  1 
ATOM   1460 C  CB  B LYS A 1 217 ? 25.990 9.883  50.118  0.50 14.15 ? 219  LYS A CB  1 
ATOM   1461 C  CG  A LYS A 1 217 ? 26.521 8.831  50.835  0.50 13.86 ? 219  LYS A CG  1 
ATOM   1462 C  CG  B LYS A 1 217 ? 26.506 8.936  51.206  0.50 15.62 ? 219  LYS A CG  1 
ATOM   1463 C  CD  A LYS A 1 217 ? 27.425 7.855  50.094  0.50 14.66 ? 219  LYS A CD  1 
ATOM   1464 C  CD  B LYS A 1 217 ? 27.594 7.950  50.790  0.50 17.49 ? 219  LYS A CD  1 
ATOM   1465 C  CE  A LYS A 1 217 ? 26.772 7.248  48.877  0.50 14.95 ? 219  LYS A CE  1 
ATOM   1466 C  CE  B LYS A 1 217 ? 28.149 7.172  51.971  0.50 18.86 ? 219  LYS A CE  1 
ATOM   1467 N  NZ  A LYS A 1 217 ? 25.595 6.419  49.234  0.50 15.38 ? 219  LYS A NZ  1 
ATOM   1468 N  NZ  B LYS A 1 217 ? 29.344 6.365  51.621  0.50 20.14 ? 219  LYS A NZ  1 
ATOM   1469 N  N   . ASP A 1 218 ? 25.161 11.385 53.005  1.00 11.64 ? 220  ASP A N   1 
ATOM   1470 C  CA  . ASP A 1 218 ? 25.676 12.000 54.218  1.00 11.90 ? 220  ASP A CA  1 
ATOM   1471 C  C   . ASP A 1 218 ? 26.205 10.885 55.116  1.00 12.15 ? 220  ASP A C   1 
ATOM   1472 O  O   . ASP A 1 218 ? 25.514 9.893  55.335  1.00 12.50 ? 220  ASP A O   1 
ATOM   1473 C  CB  . ASP A 1 218 ? 24.601 12.860 54.881  1.00 12.32 ? 220  ASP A CB  1 
ATOM   1474 C  CG  . ASP A 1 218 ? 25.021 13.638 56.114  1.00 14.05 ? 220  ASP A CG  1 
ATOM   1475 O  OD1 . ASP A 1 218 ? 26.185 13.456 56.605  1.00 15.17 ? 220  ASP A OD1 1 
ATOM   1476 O  OD2 . ASP A 1 218 ? 24.199 14.491 56.556  1.00 15.85 ? 220  ASP A OD2 1 
ATOM   1477 N  N   . SER A 1 219 ? 27.453 11.037 55.590  1.00 12.01 ? 221  SER A N   1 
ATOM   1478 C  CA  . SER A 1 219 ? 28.084 10.035 56.442  1.00 12.87 ? 221  SER A CA  1 
ATOM   1479 C  C   . SER A 1 219 ? 27.355 9.936  57.775  1.00 13.46 ? 221  SER A C   1 
ATOM   1480 O  O   . SER A 1 219 ? 27.468 8.918  58.446  1.00 13.75 ? 221  SER A O   1 
ATOM   1481 C  CB  . SER A 1 219 ? 29.551 10.315 56.678  1.00 12.82 ? 221  SER A CB  1 
ATOM   1482 O  OG  . SER A 1 219 ? 29.753 11.553 57.372  1.00 11.87 ? 221  SER A OG  1 
ATOM   1483 N  N   . MET A 1 220 ? 26.678 11.028 58.166  1.00 13.98 ? 222  MET A N   1 
ATOM   1484 C  CA  . MET A 1 220 ? 26.148 11.242 59.509  1.00 15.39 ? 222  MET A CA  1 
ATOM   1485 C  C   . MET A 1 220 ? 27.302 11.311 60.507  1.00 16.01 ? 222  MET A C   1 
ATOM   1486 O  O   . MET A 1 220 ? 28.460 11.227 60.123  1.00 15.42 ? 222  MET A O   1 
ATOM   1487 C  CB  . MET A 1 220 ? 25.179 10.133 59.912  1.00 16.68 ? 222  MET A CB  1 
ATOM   1488 C  CG  . MET A 1 220 ? 24.101 9.896  58.881  1.00 16.73 ? 222  MET A CG  1 
ATOM   1489 S  SD  . MET A 1 220 ? 22.813 8.791  59.519  1.00 18.86 ? 222  MET A SD  1 
ATOM   1490 C  CE  . MET A 1 220 ? 23.276 7.254  58.722  1.00 19.92 ? 222  MET A CE  1 
ATOM   1491 N  N   . THR A 1 221 ? 26.973 11.474 61.789  1.00 17.77 ? 223  THR A N   1 
ATOM   1492 C  CA  . THR A 1 221 ? 27.957 11.803 62.804  1.00 19.27 ? 223  THR A CA  1 
ATOM   1493 C  C   . THR A 1 221 ? 28.011 10.638 63.776  1.00 19.73 ? 223  THR A C   1 
ATOM   1494 O  O   . THR A 1 221 ? 26.988 10.210 64.288  1.00 20.53 ? 223  THR A O   1 
ATOM   1495 C  CB  . THR A 1 221 ? 27.610 13.142 63.480  1.00 20.26 ? 223  THR A CB  1 
ATOM   1496 O  OG1 . THR A 1 221 ? 27.325 14.118 62.456  1.00 19.45 ? 223  THR A OG1 1 
ATOM   1497 C  CG2 . THR A 1 221 ? 28.711 13.613 64.402  1.00 19.49 ? 223  THR A CG2 1 
ATOM   1498 N  N   . SER A 1 222 ? 29.202 10.094 63.985  1.00 20.92 ? 224  SER A N   1 
ATOM   1499 C  CA  . SER A 1 222 ? 29.359 8.910  64.814  1.00 23.57 ? 224  SER A CA  1 
ATOM   1500 C  C   . SER A 1 222 ? 28.979 9.151  66.280  1.00 24.00 ? 224  SER A C   1 
ATOM   1501 O  O   . SER A 1 222 ? 28.426 8.276  66.960  1.00 25.95 ? 224  SER A O   1 
ATOM   1502 C  CB  . SER A 1 222 ? 30.761 8.439  64.691  1.00 26.05 ? 224  SER A CB  1 
ATOM   1503 O  OG  . SER A 1 222 ? 30.921 7.251  65.412  1.00 29.38 ? 224  SER A OG  1 
ATOM   1504 N  N   . GLY A 1 223 ? 29.265 10.338 66.802  1.00 21.55 ? 225  GLY A N   1 
ATOM   1505 C  CA  . GLY A 1 223 ? 28.913 10.600 68.187  1.00 20.56 ? 225  GLY A CA  1 
ATOM   1506 C  C   . GLY A 1 223 ? 27.536 11.244 68.333  1.00 18.78 ? 225  GLY A C   1 
ATOM   1507 O  O   . GLY A 1 223 ? 27.300 11.943 69.310  1.00 17.84 ? 225  GLY A O   1 
ATOM   1508 N  N   . MET A 1 224 ? 26.631 11.005 67.368  1.00 17.17 ? 226  MET A N   1 
ATOM   1509 C  CA  . MET A 1 224 ? 25.269 11.504 67.460  1.00 16.80 ? 226  MET A CA  1 
ATOM   1510 C  C   . MET A 1 224 ? 24.274 10.439 67.031  1.00 17.23 ? 226  MET A C   1 
ATOM   1511 O  O   . MET A 1 224 ? 24.618 9.525  66.290  1.00 17.81 ? 226  MET A O   1 
ATOM   1512 C  CB  . MET A 1 224 ? 25.102 12.723 66.540  1.00 16.02 ? 226  MET A CB  1 
ATOM   1513 C  CG  . MET A 1 224 ? 25.665 13.978 67.134  1.00 15.87 ? 226  MET A CG  1 
ATOM   1514 S  SD  . MET A 1 224 ? 25.494 15.330 65.948  1.00 15.96 ? 226  MET A SD  1 
ATOM   1515 C  CE  . MET A 1 224 ? 26.859 16.349 66.496  1.00 16.10 ? 226  MET A CE  1 
ATOM   1516 N  N   . ILE A 1 225 ? 23.028 10.623 67.452  1.00 17.43 ? 227  ILE A N   1 
ATOM   1517 C  CA  . ILE A 1 225 ? 21.907 9.827  66.996  1.00 18.58 ? 227  ILE A CA  1 
ATOM   1518 C  C   . ILE A 1 225 ? 21.068 10.677 66.049  1.00 18.30 ? 227  ILE A C   1 
ATOM   1519 O  O   . ILE A 1 225 ? 20.619 11.756 66.427  1.00 18.70 ? 227  ILE A O   1 
ATOM   1520 C  CB  . ILE A 1 225 ? 21.086 9.331  68.202  1.00 20.30 ? 227  ILE A CB  1 
ATOM   1521 C  CG1 . ILE A 1 225 ? 21.942 8.457  69.125  1.00 21.65 ? 227  ILE A CG1 1 
ATOM   1522 C  CG2 . ILE A 1 225 ? 19.843 8.579  67.745  1.00 21.21 ? 227  ILE A CG2 1 
ATOM   1523 C  CD1 . ILE A 1 225 ? 21.381 8.292  70.513  1.00 22.52 ? 227  ILE A CD1 1 
ATOM   1524 N  N   . ASN A 1 226 ? 20.822 10.161 64.846  1.00 18.09 ? 228  ASN A N   1 
ATOM   1525 C  CA  . ASN A 1 226 ? 19.949 10.836 63.898  1.00 18.72 ? 228  ASN A CA  1 
ATOM   1526 C  C   . ASN A 1 226 ? 18.490 10.678 64.339  1.00 19.64 ? 228  ASN A C   1 
ATOM   1527 O  O   . ASN A 1 226 ? 18.058 9.606  64.747  1.00 21.07 ? 228  ASN A O   1 
ATOM   1528 C  CB  . ASN A 1 226 ? 20.219 10.329 62.484  1.00 18.77 ? 228  ASN A CB  1 
ATOM   1529 C  CG  . ASN A 1 226 ? 19.510 11.180 61.455  1.00 19.40 ? 228  ASN A CG  1 
ATOM   1530 O  OD1 . ASN A 1 226 ? 18.284 11.126 61.363  1.00 19.80 ? 228  ASN A OD1 1 
ATOM   1531 N  ND2 . ASN A 1 226 ? 20.258 11.998 60.722  1.00 19.84 ? 228  ASN A ND2 1 
ATOM   1532 N  N   . ASN A 1 227 ? 17.719 11.767 64.297  1.00 19.06 ? 229  ASN A N   1 
ATOM   1533 C  CA  . ASN A 1 227 ? 16.348 11.746 64.785  1.00 20.15 ? 229  ASN A CA  1 
ATOM   1534 C  C   . ASN A 1 227 ? 15.385 11.221 63.726  1.00 21.24 ? 229  ASN A C   1 
ATOM   1535 O  O   . ASN A 1 227 ? 14.224 11.027 64.036  1.00 23.48 ? 229  ASN A O   1 
ATOM   1536 C  CB  . ASN A 1 227 ? 15.858 13.111 65.269  1.00 20.00 ? 229  ASN A CB  1 
ATOM   1537 C  CG  . ASN A 1 227 ? 16.533 13.542 66.556  1.00 20.15 ? 229  ASN A CG  1 
ATOM   1538 O  OD1 . ASN A 1 227 ? 16.696 12.730 67.465  1.00 20.96 ? 229  ASN A OD1 1 
ATOM   1539 N  ND2 . ASN A 1 227 ? 16.954 14.796 66.643  1.00 19.28 ? 229  ASN A ND2 1 
ATOM   1540 N  N   . GLY A 1 228 ? 15.856 10.969 62.506  1.00 20.74 ? 230  GLY A N   1 
ATOM   1541 C  CA  . GLY A 1 228 ? 15.017 10.403 61.462  1.00 22.70 ? 230  GLY A CA  1 
ATOM   1542 C  C   . GLY A 1 228 ? 13.860 11.328 61.073  1.00 23.84 ? 230  GLY A C   1 
ATOM   1543 O  O   . GLY A 1 228 ? 12.788 10.844 60.736  1.00 27.71 ? 230  GLY A O   1 
ATOM   1544 N  N   . ASP A 1 229 ? 14.078 12.649 61.100  1.00 21.82 ? 231  ASP A N   1 
ATOM   1545 C  CA  . ASP A 1 229 ? 13.039 13.625 60.807  1.00 21.96 ? 231  ASP A CA  1 
ATOM   1546 C  C   . ASP A 1 229 ? 13.408 14.354 59.515  1.00 20.28 ? 231  ASP A C   1 
ATOM   1547 O  O   . ASP A 1 229 ? 13.225 15.556 59.367  1.00 20.22 ? 231  ASP A O   1 
ATOM   1548 C  CB  . ASP A 1 229 ? 12.871 14.594 61.974  1.00 22.28 ? 231  ASP A CB  1 
ATOM   1549 C  CG  . ASP A 1 229 ? 14.141 15.348 62.354  1.00 21.33 ? 231  ASP A CG  1 
ATOM   1550 O  OD1 . ASP A 1 229 ? 15.237 15.012 61.847  1.00 18.98 ? 231  ASP A OD1 1 
ATOM   1551 O  OD2 . ASP A 1 229 ? 14.027 16.283 63.137  1.00 22.68 ? 231  ASP A OD2 1 
ATOM   1552 N  N   . ILE A 1 230 ? 13.955 13.604 58.577  1.00 20.03 ? 232  ILE A N   1 
ATOM   1553 C  CA  . ILE A 1 230 ? 14.514 14.195 57.381  1.00 19.32 ? 232  ILE A CA  1 
ATOM   1554 C  C   . ILE A 1 230 ? 13.399 14.681 56.448  1.00 18.76 ? 232  ILE A C   1 
ATOM   1555 O  O   . ILE A 1 230 ? 12.403 14.000 56.234  1.00 19.50 ? 232  ILE A O   1 
ATOM   1556 C  CB  . ILE A 1 230 ? 15.479 13.200 56.714  1.00 20.07 ? 232  ILE A CB  1 
ATOM   1557 C  CG1 . ILE A 1 230 ? 16.149 13.821 55.492  1.00 20.77 ? 232  ILE A CG1 1 
ATOM   1558 C  CG2 . ILE A 1 230 ? 14.777 11.906 56.353  1.00 21.52 ? 232  ILE A CG2 1 
ATOM   1559 C  CD1 . ILE A 1 230 ? 17.473 13.186 55.142  1.00 21.38 ? 232  ILE A CD1 1 
ATOM   1560 N  N   . GLN A 1 231 ? 13.586 15.893 55.911  1.00 17.49 ? 233  GLN A N   1 
ATOM   1561 C  CA  . GLN A 1 231 ? 12.672 16.490 54.951  1.00 17.53 ? 233  GLN A CA  1 
ATOM   1562 C  C   . GLN A 1 231 ? 13.494 17.106 53.828  1.00 15.63 ? 233  GLN A C   1 
ATOM   1563 O  O   . GLN A 1 231 ? 14.618 17.569 54.076  1.00 14.05 ? 233  GLN A O   1 
ATOM   1564 C  CB  . GLN A 1 231 ? 11.800 17.568 55.596  1.00 18.98 ? 233  GLN A CB  1 
ATOM   1565 C  CG  . GLN A 1 231 ? 10.942 17.073 56.748  1.00 20.62 ? 233  GLN A CG  1 
ATOM   1566 C  CD  . GLN A 1 231 ? 9.845  16.164 56.271  1.00 22.45 ? 233  GLN A CD  1 
ATOM   1567 O  OE1 . GLN A 1 231 ? 9.564  16.066 55.082  1.00 24.64 ? 233  GLN A OE1 1 
ATOM   1568 N  NE2 . GLN A 1 231 ? 9.208  15.476 57.195  1.00 23.94 ? 233  GLN A NE2 1 
ATOM   1569 N  N   . VAL A 1 232 ? 12.889 17.145 52.633  1.00 14.86 ? 234  VAL A N   1 
ATOM   1570 C  CA  . VAL A 1 232 ? 13.513 17.721 51.459  1.00 14.09 ? 234  VAL A CA  1 
ATOM   1571 C  C   . VAL A 1 232 ? 12.622 18.849 50.935  1.00 14.26 ? 234  VAL A C   1 
ATOM   1572 O  O   . VAL A 1 232 ? 11.395 18.713 50.903  1.00 14.73 ? 234  VAL A O   1 
ATOM   1573 C  CB  . VAL A 1 232 ? 13.762 16.648 50.381  1.00 13.87 ? 234  VAL A CB  1 
ATOM   1574 C  CG1 . VAL A 1 232 ? 14.705 17.164 49.310  1.00 13.46 ? 234  VAL A CG1 1 
ATOM   1575 C  CG2 . VAL A 1 232 ? 14.312 15.358 50.959  1.00 13.92 ? 234  VAL A CG2 1 
ATOM   1576 N  N   . TYR A 1 233 ? 13.255 19.953 50.514  1.00 13.68 ? 235  TYR A N   1 
ATOM   1577 C  CA  . TYR A 1 233 ? 12.512 21.145 50.131  1.00 14.41 ? 235  TYR A CA  1 
ATOM   1578 C  C   . TYR A 1 233 ? 12.977 21.666 48.785  1.00 13.89 ? 235  TYR A C   1 
ATOM   1579 O  O   . TYR A 1 233 ? 14.159 21.626 48.464  1.00 13.10 ? 235  TYR A O   1 
ATOM   1580 C  CB  . TYR A 1 233 ? 12.690 22.254 51.168  1.00 14.76 ? 235  TYR A CB  1 
ATOM   1581 C  CG  . TYR A 1 233 ? 12.141 21.889 52.534  1.00 15.59 ? 235  TYR A CG  1 
ATOM   1582 C  CD1 . TYR A 1 233 ? 10.782 21.961 52.811  1.00 16.95 ? 235  TYR A CD1 1 
ATOM   1583 C  CD2 . TYR A 1 233 ? 12.990 21.431 53.532  1.00 14.93 ? 235  TYR A CD2 1 
ATOM   1584 C  CE1 . TYR A 1 233 ? 10.288 21.612 54.055  1.00 17.48 ? 235  TYR A CE1 1 
ATOM   1585 C  CE2 . TYR A 1 233 ? 12.511 21.087 54.775  1.00 15.62 ? 235  TYR A CE2 1 
ATOM   1586 C  CZ  . TYR A 1 233 ? 11.157 21.156 55.028  1.00 16.92 ? 235  TYR A CZ  1 
ATOM   1587 O  OH  . TYR A 1 233 ? 10.751 20.772 56.266  1.00 17.77 ? 235  TYR A OH  1 
ATOM   1588 N  N   . LEU A 1 234 ? 12.021 22.184 48.019  1.00 14.49 ? 236  LEU A N   1 
ATOM   1589 C  CA  . LEU A 1 234 ? 12.351 22.970 46.846  1.00 14.31 ? 236  LEU A CA  1 
ATOM   1590 C  C   . LEU A 1 234 ? 12.322 24.450 47.232  1.00 15.02 ? 236  LEU A C   1 
ATOM   1591 O  O   . LEU A 1 234 ? 11.295 24.952 47.645  1.00 15.90 ? 236  LEU A O   1 
ATOM   1592 C  CB  . LEU A 1 234 ? 11.345 22.624 45.758  1.00 14.98 ? 236  LEU A CB  1 
ATOM   1593 C  CG  . LEU A 1 234 ? 11.291 23.578 44.576  1.00 15.52 ? 236  LEU A CG  1 
ATOM   1594 C  CD1 . LEU A 1 234 ? 12.649 23.693 43.917  1.00 14.64 ? 236  LEU A CD1 1 
ATOM   1595 C  CD2 . LEU A 1 234 ? 10.249 23.113 43.566  1.00 16.24 ? 236  LEU A CD2 1 
ATOM   1596 N  N   . GLN A 1 235 ? 13.468 25.128 47.107  1.00 14.80 ? 237  GLN A N   1 
ATOM   1597 C  CA  . GLN A 1 235 ? 13.614 26.513 47.522  1.00 15.71 ? 237  GLN A CA  1 
ATOM   1598 C  C   . GLN A 1 235 ? 13.915 27.373 46.304  1.00 16.24 ? 237  GLN A C   1 
ATOM   1599 O  O   . GLN A 1 235 ? 14.920 27.164 45.644  1.00 15.71 ? 237  GLN A O   1 
ATOM   1600 C  CB  . GLN A 1 235 ? 14.752 26.637 48.524  1.00 15.24 ? 237  GLN A CB  1 
ATOM   1601 C  CG  . GLN A 1 235 ? 14.962 28.048 49.056  1.00 16.18 ? 237  GLN A CG  1 
ATOM   1602 C  CD  . GLN A 1 235 ? 16.156 28.050 49.980  1.00 15.79 ? 237  GLN A CD  1 
ATOM   1603 O  OE1 . GLN A 1 235 ? 16.088 27.585 51.114  1.00 15.20 ? 237  GLN A OE1 1 
ATOM   1604 N  NE2 . GLN A 1 235 ? 17.265 28.593 49.506  1.00 16.06 ? 237  GLN A NE2 1 
ATOM   1605 N  N   . GLN A 1 236 ? 13.037 28.338 46.034  1.00 17.51 ? 238  GLN A N   1 
ATOM   1606 C  CA  . GLN A 1 236 ? 13.253 29.356 45.012  1.00 18.52 ? 238  GLN A CA  1 
ATOM   1607 C  C   . GLN A 1 236 ? 12.241 30.479 45.206  1.00 19.98 ? 238  GLN A C   1 
ATOM   1608 O  O   . GLN A 1 236 ? 11.154 30.243 45.724  1.00 20.37 ? 238  GLN A O   1 
ATOM   1609 C  CB  . GLN A 1 236 ? 13.084 28.737 43.629  1.00 18.84 ? 238  GLN A CB  1 
ATOM   1610 C  CG  . GLN A 1 236 ? 11.773 27.978 43.461  1.00 19.72 ? 238  GLN A CG  1 
ATOM   1611 C  CD  . GLN A 1 236 ? 11.786 27.101 42.228  1.00 19.75 ? 238  GLN A CD  1 
ATOM   1612 O  OE1 . GLN A 1 236 ? 12.687 27.177 41.401  1.00 20.01 ? 238  GLN A OE1 1 
ATOM   1613 N  NE2 . GLN A 1 236 ? 10.759 26.280 42.085  1.00 20.07 ? 238  GLN A NE2 1 
ATOM   1614 N  N   . GLY A 1 237 ? 12.596 31.708 44.815  1.00 21.08 ? 239  GLY A N   1 
ATOM   1615 C  CA  . GLY A 1 237 ? 11.686 32.840 44.928  1.00 23.02 ? 239  GLY A CA  1 
ATOM   1616 C  C   . GLY A 1 237 ? 11.356 33.208 46.377  1.00 23.73 ? 239  GLY A C   1 
ATOM   1617 O  O   . GLY A 1 237 ? 10.323 33.817 46.643  1.00 25.41 ? 239  GLY A O   1 
ATOM   1618 N  N   . GLY A 1 238 ? 12.242 32.855 47.312  1.00 22.61 ? 240  GLY A N   1 
ATOM   1619 C  CA  . GLY A 1 238 ? 12.024 33.138 48.716  1.00 23.56 ? 240  GLY A CA  1 
ATOM   1620 C  C   . GLY A 1 238 ? 10.967 32.242 49.368  1.00 23.83 ? 240  GLY A C   1 
ATOM   1621 O  O   . GLY A 1 238 ? 10.521 32.566 50.461  1.00 24.33 ? 240  GLY A O   1 
ATOM   1622 N  N   . SER A 1 239 ? 10.612 31.101 48.744  1.00 23.21 ? 241  SER A N   1 
ATOM   1623 C  CA  . SER A 1 239 ? 9.645  30.202 49.360  1.00 23.65 ? 241  SER A CA  1 
ATOM   1624 C  C   . SER A 1 239 ? 10.095 28.747 49.253  1.00 22.13 ? 241  SER A C   1 
ATOM   1625 O  O   . SER A 1 239 ? 10.996 28.428 48.480  1.00 20.64 ? 241  SER A O   1 
ATOM   1626 C  CB  . SER A 1 239 ? 8.296  30.402 48.773  1.00 25.08 ? 241  SER A CB  1 
ATOM   1627 O  OG  . SER A 1 239 ? 8.307  29.948 47.443  1.00 25.05 ? 241  SER A OG  1 
ATOM   1628 N  N   . GLU A 1 240 ? 9.456  27.892 50.065  1.00 22.47 ? 242  GLU A N   1 
ATOM   1629 C  CA  . GLU A 1 240 ? 9.801  26.489 50.167  1.00 21.32 ? 242  GLU A CA  1 
ATOM   1630 C  C   . GLU A 1 240 ? 8.550  25.624 50.070  1.00 21.35 ? 242  GLU A C   1 
ATOM   1631 O  O   . GLU A 1 240 ? 7.526  25.936 50.659  1.00 22.52 ? 242  GLU A O   1 
ATOM   1632 C  CB  . GLU A 1 240 ? 10.537 26.215 51.479  1.00 21.40 ? 242  GLU A CB  1 
ATOM   1633 C  CG  . GLU A 1 240 ? 11.984 26.679 51.428  1.00 21.25 ? 242  GLU A CG  1 
ATOM   1634 C  CD  . GLU A 1 240 ? 12.790 26.396 52.685  1.00 21.70 ? 242  GLU A CD  1 
ATOM   1635 O  OE1 . GLU A 1 240 ? 12.169 26.041 53.734  1.00 22.40 ? 242  GLU A OE1 1 
ATOM   1636 O  OE2 . GLU A 1 240 ? 14.046 26.522 52.608  1.00 21.10 ? 242  GLU A OE2 1 
ATOM   1637 N  N   . VAL A 1 241 ? 8.681  24.528 49.316  1.00 19.89 ? 243  VAL A N   1 
ATOM   1638 C  CA  . VAL A 1 241 ? 7.680  23.484 49.248  1.00 20.16 ? 243  VAL A CA  1 
ATOM   1639 C  C   . VAL A 1 241 ? 8.349  22.145 49.570  1.00 18.36 ? 243  VAL A C   1 
ATOM   1640 O  O   . VAL A 1 241 ? 9.447  21.859 49.081  1.00 16.78 ? 243  VAL A O   1 
ATOM   1641 C  CB  . VAL A 1 241 ? 7.056  23.482 47.845  1.00 21.07 ? 243  VAL A CB  1 
ATOM   1642 C  CG1 . VAL A 1 241 ? 5.964  22.436 47.755  1.00 22.14 ? 243  VAL A CG1 1 
ATOM   1643 C  CG2 . VAL A 1 241 ? 6.540  24.866 47.445  1.00 22.43 ? 243  VAL A CG2 1 
ATOM   1644 N  N   . ALA A 1 242 ? 7.686  21.334 50.398  1.00 18.61 ? 244  ALA A N   1 
ATOM   1645 C  CA  . ALA A 1 242 ? 8.185  20.012 50.759  1.00 17.63 ? 244  ALA A CA  1 
ATOM   1646 C  C   . ALA A 1 242 ? 8.046  19.077 49.560  1.00 17.48 ? 244  ALA A C   1 
ATOM   1647 O  O   . ALA A 1 242 ? 7.001  19.044 48.922  1.00 18.49 ? 244  ALA A O   1 
ATOM   1648 C  CB  . ALA A 1 242 ? 7.445  19.459 51.948  1.00 18.41 ? 244  ALA A CB  1 
ATOM   1649 N  N   . ILE A 1 243 ? 9.112  18.330 49.266  1.00 16.20 ? 245  ILE A N   1 
ATOM   1650 C  CA  . ILE A 1 243 ? 9.132  17.392 48.160  1.00 16.16 ? 245  ILE A CA  1 
ATOM   1651 C  C   . ILE A 1 243 ? 9.686  16.049 48.649  1.00 15.95 ? 245  ILE A C   1 
ATOM   1652 O  O   . ILE A 1 243 ? 10.166 15.262 47.839  1.00 15.15 ? 245  ILE A O   1 
ATOM   1653 C  CB  . ILE A 1 243 ? 9.984  17.961 47.014  1.00 15.28 ? 245  ILE A CB  1 
ATOM   1654 C  CG1 . ILE A 1 243 ? 11.396 18.315 47.490  1.00 14.20 ? 245  ILE A CG1 1 
ATOM   1655 C  CG2 . ILE A 1 243 ? 9.288  19.151 46.369  1.00 16.00 ? 245  ILE A CG2 1 
ATOM   1656 C  CD1 . ILE A 1 243 ? 12.346 18.749 46.398  1.00 13.42 ? 245  ILE A CD1 1 
ATOM   1657 N  N   . THR A 1 244 ? 9.596  15.789 49.959  1.00 16.54 ? 246  THR A N   1 
ATOM   1658 C  CA  . THR A 1 244 ? 10.247 14.655 50.599  1.00 16.94 ? 246  THR A CA  1 
ATOM   1659 C  C   . THR A 1 244 ? 9.782  13.317 50.032  1.00 18.00 ? 246  THR A C   1 
ATOM   1660 O  O   . THR A 1 244 ? 10.595 12.415 49.867  1.00 17.36 ? 246  THR A O   1 
ATOM   1661 C  CB  . THR A 1 244 ? 9.999  14.673 52.110  1.00 17.65 ? 246  THR A CB  1 
ATOM   1662 O  OG1 . THR A 1 244 ? 10.340 15.986 52.539  1.00 17.79 ? 246  THR A OG1 1 
ATOM   1663 C  CG2 . THR A 1 244 ? 10.832 13.674 52.883  1.00 17.40 ? 246  THR A CG2 1 
ATOM   1664 N  N   . ASP A 1 245 ? 8.487  13.191 49.742  1.00 20.47 ? 247  ASP A N   1 
ATOM   1665 C  CA  . ASP A 1 245 ? 7.919  11.926 49.298  1.00 22.20 ? 247  ASP A CA  1 
ATOM   1666 C  C   . ASP A 1 245 ? 8.435  11.523 47.915  1.00 21.09 ? 247  ASP A C   1 
ATOM   1667 O  O   . ASP A 1 245 ? 8.277  10.372 47.530  1.00 21.28 ? 247  ASP A O   1 
ATOM   1668 C  CB  . ASP A 1 245 ? 6.400  12.011 49.235  1.00 25.27 ? 247  ASP A CB  1 
ATOM   1669 C  CG  . ASP A 1 245 ? 5.735  12.326 50.557  1.00 28.39 ? 247  ASP A CG  1 
ATOM   1670 O  OD1 . ASP A 1 245 ? 6.449  12.386 51.588  1.00 29.65 ? 247  ASP A OD1 1 
ATOM   1671 O  OD2 . ASP A 1 245 ? 4.499  12.503 50.545  1.00 32.30 ? 247  ASP A OD2 1 
ATOM   1672 N  N   . SER A 1 246 ? 9.003  12.457 47.135  1.00 19.62 ? 248  SER A N   1 
ATOM   1673 C  CA  . SER A 1 246 ? 9.517  12.122 45.814  1.00 18.70 ? 248  SER A CA  1 
ATOM   1674 C  C   . SER A 1 246 ? 10.913 11.495 45.899  1.00 17.47 ? 248  SER A C   1 
ATOM   1675 O  O   . SER A 1 246 ? 11.454 11.039 44.897  1.00 17.86 ? 248  SER A O   1 
ATOM   1676 C  CB  . SER A 1 246 ? 9.536  13.331 44.910  1.00 18.60 ? 248  SER A CB  1 
ATOM   1677 O  OG  . SER A 1 246 ? 8.254  13.934 44.807  1.00 19.81 ? 248  SER A OG  1 
ATOM   1678 N  N   . PHE A 1 247 ? 11.509 11.431 47.090  1.00 16.58 ? 249  PHE A N   1 
ATOM   1679 C  CA  . PHE A 1 247 ? 12.876 10.958 47.244  1.00 15.65 ? 249  PHE A CA  1 
ATOM   1680 C  C   . PHE A 1 247 ? 12.889 9.637  47.996  1.00 16.44 ? 249  PHE A C   1 
ATOM   1681 O  O   . PHE A 1 247 ? 12.088 9.430  48.890  1.00 17.01 ? 249  PHE A O   1 
ATOM   1682 C  CB  . PHE A 1 247 ? 13.754 11.980 47.993  1.00 14.76 ? 249  PHE A CB  1 
ATOM   1683 C  CG  . PHE A 1 247 ? 14.029 13.235 47.202  1.00 14.11 ? 249  PHE A CG  1 
ATOM   1684 C  CD1 . PHE A 1 247 ? 13.028 14.170 46.993  1.00 14.51 ? 249  PHE A CD1 1 
ATOM   1685 C  CD2 . PHE A 1 247 ? 15.264 13.451 46.609  1.00 13.44 ? 249  PHE A CD2 1 
ATOM   1686 C  CE1 . PHE A 1 247 ? 13.261 15.292 46.219  1.00 14.10 ? 249  PHE A CE1 1 
ATOM   1687 C  CE2 . PHE A 1 247 ? 15.495 14.564 45.810  1.00 12.94 ? 249  PHE A CE2 1 
ATOM   1688 C  CZ  . PHE A 1 247 ? 14.495 15.489 45.627  1.00 13.24 ? 249  PHE A CZ  1 
ATOM   1689 N  N   . SER A 1 248 ? 13.826 8.771  47.604  1.00 16.71 ? 250  SER A N   1 
ATOM   1690 C  CA  . SER A 1 248 ? 14.161 7.557  48.332  1.00 17.65 ? 250  SER A CA  1 
ATOM   1691 C  C   . SER A 1 248 ? 15.193 7.898  49.408  1.00 16.80 ? 250  SER A C   1 
ATOM   1692 O  O   . SER A 1 248 ? 16.279 8.368  49.092  1.00 15.80 ? 250  SER A O   1 
ATOM   1693 C  CB  . SER A 1 248 ? 14.665 6.510  47.369  1.00 18.44 ? 250  SER A CB  1 
ATOM   1694 O  OG  . SER A 1 248 ? 15.230 5.411  48.072  1.00 20.00 ? 250  SER A OG  1 
ATOM   1695 N  N   . ILE A 1 249 ? 14.834 7.668  50.675  1.00 17.00 ? 251  ILE A N   1 
ATOM   1696 C  CA  . ILE A 1 249 ? 15.672 8.013  51.806  1.00 16.71 ? 251  ILE A CA  1 
ATOM   1697 C  C   . ILE A 1 249 ? 16.100 6.733  52.527  1.00 17.22 ? 251  ILE A C   1 
ATOM   1698 O  O   . ILE A 1 249 ? 15.258 6.053  53.095  1.00 18.32 ? 251  ILE A O   1 
ATOM   1699 C  CB  . ILE A 1 249 ? 14.899 8.994  52.711  1.00 17.15 ? 251  ILE A CB  1 
ATOM   1700 C  CG1 . ILE A 1 249 ? 14.563 10.274 51.934  1.00 16.95 ? 251  ILE A CG1 1 
ATOM   1701 C  CG2 . ILE A 1 249 ? 15.668 9.282  53.995  1.00 16.73 ? 251  ILE A CG2 1 
ATOM   1702 C  CD1 . ILE A 1 249 ? 13.654 11.242 52.652  1.00 17.50 ? 251  ILE A CD1 1 
ATOM   1703 N  N   . THR A 1 250 ? 17.392 6.376  52.439  1.00 16.69 ? 252  THR A N   1 
ATOM   1704 C  CA  . THR A 1 250 ? 17.888 5.083  52.907  1.00 17.58 ? 252  THR A CA  1 
ATOM   1705 C  C   . THR A 1 250 ? 19.030 5.271  53.897  1.00 17.22 ? 252  THR A C   1 
ATOM   1706 O  O   . THR A 1 250 ? 19.548 6.375  54.006  1.00 15.50 ? 252  THR A O   1 
ATOM   1707 C  CB  . THR A 1 250 ? 18.388 4.215  51.750  1.00 17.95 ? 252  THR A CB  1 
ATOM   1708 O  OG1 . THR A 1 250 ? 19.420 4.912  51.048  1.00 17.29 ? 252  THR A OG1 1 
ATOM   1709 C  CG2 . THR A 1 250 ? 17.279 3.856  50.792  1.00 18.72 ? 252  THR A CG2 1 
ATOM   1710 N  N   . THR A 1 251 ? 19.408 4.185  54.604  1.00 18.77 ? 253  THR A N   1 
ATOM   1711 C  CA  . THR A 1 251 ? 20.510 4.206  55.565  1.00 19.36 ? 253  THR A CA  1 
ATOM   1712 C  C   . THR A 1 251 ? 21.402 2.960  55.445  1.00 20.88 ? 253  THR A C   1 
ATOM   1713 O  O   . THR A 1 251 ? 22.079 2.588  56.410  1.00 21.97 ? 253  THR A O   1 
ATOM   1714 C  CB  . THR A 1 251 ? 19.994 4.376  57.008  1.00 19.89 ? 253  THR A CB  1 
ATOM   1715 O  OG1 . THR A 1 251 ? 19.144 3.263  57.279  1.00 21.13 ? 253  THR A OG1 1 
ATOM   1716 C  CG2 . THR A 1 251 ? 19.252 5.684  57.220  1.00 19.38 ? 253  THR A CG2 1 
ATOM   1717 N  N   . ASN A 1 252 ? 21.482 2.386  54.233  1.00 22.20 ? 254  ASN A N   1 
ATOM   1718 C  CA  . ASN A 1 252 ? 22.305 1.214  53.989  1.00 24.41 ? 254  ASN A CA  1 
ATOM   1719 C  C   . ASN A 1 252 ? 23.762 1.619  53.745  1.00 25.15 ? 254  ASN A C   1 
ATOM   1720 O  O   . ASN A 1 252 ? 24.688 0.873  54.065  1.00 27.57 ? 254  ASN A O   1 
ATOM   1721 C  CB  . ASN A 1 252 ? 21.766 0.363  52.835  1.00 25.78 ? 254  ASN A CB  1 
ATOM   1722 C  CG  . ASN A 1 252 ? 21.786 1.082  51.506  1.00 24.80 ? 254  ASN A CG  1 
ATOM   1723 O  OD1 . ASN A 1 252 ? 21.010 2.003  51.290  1.00 24.40 ? 254  ASN A OD1 1 
ATOM   1724 N  ND2 . ASN A 1 252 ? 22.645 0.655  50.597  1.00 25.67 ? 254  ASN A ND2 1 
ATOM   1725 N  N   . ASN A 1 253 ? 23.958 2.808  53.171  1.00 25.01 ? 255  ASN A N   1 
ATOM   1726 C  CA  . ASN A 1 253 ? 25.278 3.295  52.799  1.00 25.25 ? 255  ASN A CA  1 
ATOM   1727 C  C   . ASN A 1 253 ? 25.345 4.791  53.086  1.00 22.90 ? 255  ASN A C   1 
ATOM   1728 O  O   . ASN A 1 253 ? 25.128 5.611  52.191  1.00 22.06 ? 255  ASN A O   1 
ATOM   1729 C  CB  . ASN A 1 253 ? 25.564 2.997  51.319  1.00 26.55 ? 255  ASN A CB  1 
ATOM   1730 C  CG  . ASN A 1 253 ? 26.942 3.448  50.898  1.00 27.39 ? 255  ASN A CG  1 
ATOM   1731 O  OD1 . ASN A 1 253 ? 27.075 4.310  50.042  1.00 29.72 ? 255  ASN A OD1 1 
ATOM   1732 N  ND2 . ASN A 1 253 ? 27.971 2.861  51.477  1.00 28.89 ? 255  ASN A ND2 1 
ATOM   1733 N  N   . GLY A 1 254 ? 25.601 5.126  54.350  1.00 21.26 ? 256  GLY A N   1 
ATOM   1734 C  CA  . GLY A 1 254 ? 25.357 6.477  54.838  1.00 19.68 ? 256  GLY A CA  1 
ATOM   1735 C  C   . GLY A 1 254 ? 23.870 6.823  54.751  1.00 18.68 ? 256  GLY A C   1 
ATOM   1736 O  O   . GLY A 1 254 ? 23.052 5.978  54.397  1.00 20.70 ? 256  GLY A O   1 
ATOM   1737 N  N   . LEU A 1 255 ? 23.519 8.064  55.083  1.00 16.20 ? 257  LEU A N   1 
ATOM   1738 C  CA  . LEU A 1 255 ? 22.174 8.556  54.881  1.00 15.41 ? 257  LEU A CA  1 
ATOM   1739 C  C   . LEU A 1 255 ? 22.087 9.036  53.436  1.00 13.77 ? 257  LEU A C   1 
ATOM   1740 O  O   . LEU A 1 255 ? 22.746 10.000 53.088  1.00 12.30 ? 257  LEU A O   1 
ATOM   1741 C  CB  . LEU A 1 255 ? 21.911 9.695  55.864  1.00 15.47 ? 257  LEU A CB  1 
ATOM   1742 C  CG  . LEU A 1 255 ? 20.637 10.501 55.645  1.00 16.79 ? 257  LEU A CG  1 
ATOM   1743 C  CD1 . LEU A 1 255 ? 19.418 9.596  55.678  1.00 19.15 ? 257  LEU A CD1 1 
ATOM   1744 C  CD2 . LEU A 1 255 ? 20.509 11.570 56.711  1.00 17.34 ? 257  LEU A CD2 1 
ATOM   1745 N  N   . THR A 1 256 ? 21.331 8.331  52.594  1.00 13.98 ? 258  THR A N   1 
ATOM   1746 C  CA  . THR A 1 256 ? 21.267 8.688  51.182  1.00 13.48 ? 258  THR A CA  1 
ATOM   1747 C  C   . THR A 1 256 ? 19.867 9.178  50.833  1.00 13.55 ? 258  THR A C   1 
ATOM   1748 O  O   . THR A 1 256 ? 18.882 8.562  51.198  1.00 14.57 ? 258  THR A O   1 
ATOM   1749 C  CB  . THR A 1 256 ? 21.696 7.508  50.299  1.00 14.35 ? 258  THR A CB  1 
ATOM   1750 O  OG1 . THR A 1 256 ? 22.952 7.038  50.785  1.00 14.68 ? 258  THR A OG1 1 
ATOM   1751 C  CG2 . THR A 1 256 ? 21.867 7.889  48.849  1.00 14.09 ? 258  THR A CG2 1 
ATOM   1752 N  N   . VAL A 1 257 ? 19.790 10.299 50.102  1.00 12.84 ? 259  VAL A N   1 
ATOM   1753 C  CA  . VAL A 1 257 ? 18.534 10.892 49.685  1.00 13.23 ? 259  VAL A CA  1 
ATOM   1754 C  C   . VAL A 1 257 ? 18.582 11.000 48.159  1.00 13.12 ? 259  VAL A C   1 
ATOM   1755 O  O   . VAL A 1 257 ? 19.358 11.790 47.640  1.00 12.62 ? 259  VAL A O   1 
ATOM   1756 C  CB  . VAL A 1 257 ? 18.333 12.260 50.368  1.00 13.01 ? 259  VAL A CB  1 
ATOM   1757 C  CG1 . VAL A 1 257 ? 17.095 12.991 49.855  1.00 13.30 ? 259  VAL A CG1 1 
ATOM   1758 C  CG2 . VAL A 1 257 ? 18.316 12.119 51.886  1.00 13.38 ? 259  VAL A CG2 1 
ATOM   1759 N  N   . SER A 1 258 ? 17.764 10.211 47.455  1.00 14.17 ? 260  SER A N   1 
ATOM   1760 C  CA  . SER A 1 258 ? 17.925 10.004 46.022  1.00 14.76 ? 260  SER A CA  1 
ATOM   1761 C  C   . SER A 1 258 ? 16.610 10.191 45.282  1.00 14.51 ? 260  SER A C   1 
ATOM   1762 O  O   . SER A 1 258 ? 15.537 9.882  45.785  1.00 14.98 ? 260  SER A O   1 
ATOM   1763 C  CB  . SER A 1 258 ? 18.458 8.620  45.697  1.00 16.55 ? 260  SER A CB  1 
ATOM   1764 O  OG  . SER A 1 258 ? 19.746 8.424  46.263  1.00 19.10 ? 260  SER A OG  1 
ATOM   1765 N  N   . ILE A 1 259 ? 16.731 10.638 44.027  1.00 14.16 ? 261  ILE A N   1 
ATOM   1766 C  CA  . ILE A 1 259 ? 15.657 10.499 43.064  1.00 14.84 ? 261  ILE A CA  1 
ATOM   1767 C  C   . ILE A 1 259 ? 16.311 10.093 41.748  1.00 14.92 ? 261  ILE A C   1 
ATOM   1768 O  O   . ILE A 1 259 ? 17.358 10.632 41.374  1.00 14.82 ? 261  ILE A O   1 
ATOM   1769 C  CB  . ILE A 1 259 ? 14.837 11.807 42.972  1.00 14.74 ? 261  ILE A CB  1 
ATOM   1770 C  CG1 . ILE A 1 259 ? 13.604 11.657 42.078  1.00 15.44 ? 261  ILE A CG1 1 
ATOM   1771 C  CG2 . ILE A 1 259 ? 15.710 12.978 42.528  1.00 14.21 ? 261  ILE A CG2 1 
ATOM   1772 C  CD1 . ILE A 1 259 ? 12.618 12.786 42.194  1.00 15.68 ? 261  ILE A CD1 1 
ATOM   1773 N  N   . ALA A 1 260 ? 15.715 9.122  41.073  1.00 15.66 ? 262  ALA A N   1 
ATOM   1774 C  CA  . ALA A 1 260 ? 16.268 8.604  39.833  1.00 16.08 ? 262  ALA A CA  1 
ATOM   1775 C  C   . ALA A 1 260 ? 16.368 9.720  38.796  1.00 15.64 ? 262  ALA A C   1 
ATOM   1776 O  O   . ALA A 1 260 ? 17.372 9.806  38.095  1.00 15.45 ? 262  ALA A O   1 
ATOM   1777 C  CB  . ALA A 1 260 ? 15.414 7.460  39.338  1.00 17.32 ? 262  ALA A CB  1 
ATOM   1778 N  N   . ASP A 1 261 ? 15.330 10.572 38.727  1.00 15.50 ? 263  ASP A N   1 
ATOM   1779 C  CA  . ASP A 1 261 ? 15.245 11.603 37.714  1.00 15.37 ? 263  ASP A CA  1 
ATOM   1780 C  C   . ASP A 1 261 ? 14.554 12.826 38.310  1.00 15.07 ? 263  ASP A C   1 
ATOM   1781 O  O   . ASP A 1 261 ? 13.355 12.786 38.572  1.00 15.55 ? 263  ASP A O   1 
ATOM   1782 C  CB  . ASP A 1 261 ? 14.481 11.101 36.489  1.00 16.51 ? 263  ASP A CB  1 
ATOM   1783 C  CG  . ASP A 1 261 ? 14.455 12.110 35.354  1.00 16.84 ? 263  ASP A CG  1 
ATOM   1784 O  OD1 . ASP A 1 261 ? 15.190 13.140 35.456  1.00 15.91 ? 263  ASP A OD1 1 
ATOM   1785 O  OD2 . ASP A 1 261 ? 13.741 11.816 34.332  1.00 18.61 ? 263  ASP A OD2 1 
ATOM   1786 N  N   . LEU A 1 262 ? 15.348 13.892 38.545  1.00 14.21 ? 264  LEU A N   1 
ATOM   1787 C  CA  . LEU A 1 262 ? 14.878 15.122 39.164  1.00 13.67 ? 264  LEU A CA  1 
ATOM   1788 C  C   . LEU A 1 262 ? 13.970 15.896 38.203  1.00 14.49 ? 264  LEU A C   1 
ATOM   1789 O  O   . LEU A 1 262 ? 13.205 16.750 38.636  1.00 14.55 ? 264  LEU A O   1 
ATOM   1790 C  CB  . LEU A 1 262 ? 16.098 15.947 39.585  1.00 12.66 ? 264  LEU A CB  1 
ATOM   1791 C  CG  . LEU A 1 262 ? 15.822 17.168 40.455  1.00 12.40 ? 264  LEU A CG  1 
ATOM   1792 C  CD1 . LEU A 1 262 ? 15.186 16.777 41.775  1.00 12.49 ? 264  LEU A CD1 1 
ATOM   1793 C  CD2 . LEU A 1 262 ? 17.084 17.975 40.708  1.00 11.81 ? 264  LEU A CD2 1 
ATOM   1794 N  N   . LYS A 1 263 ? 14.002 15.540 36.915  1.00 15.01 ? 265  LYS A N   1 
ATOM   1795 C  CA  . LYS A 1 263 ? 13.157 16.175 35.916  1.00 16.11 ? 265  LYS A CA  1 
ATOM   1796 C  C   . LYS A 1 263 ? 11.690 15.802 36.106  1.00 16.77 ? 265  LYS A C   1 
ATOM   1797 O  O   . LYS A 1 263 ? 10.824 16.476 35.580  1.00 17.25 ? 265  LYS A O   1 
ATOM   1798 C  CB  . LYS A 1 263 ? 13.651 15.817 34.514  1.00 16.89 ? 265  LYS A CB  1 
ATOM   1799 C  CG  . LYS A 1 263 ? 15.006 16.425 34.166  1.00 16.89 ? 265  LYS A CG  1 
ATOM   1800 C  CD  . LYS A 1 263 ? 14.938 17.893 33.860  1.00 17.40 ? 265  LYS A CD  1 
ATOM   1801 C  CE  . LYS A 1 263 ? 16.282 18.475 33.503  1.00 17.60 ? 265  LYS A CE  1 
ATOM   1802 N  NZ  . LYS A 1 263 ? 16.145 19.765 32.780  1.00 18.54 ? 265  LYS A NZ  1 
ATOM   1803 N  N   . THR A 1 264 ? 11.401 14.756 36.876  1.00 16.72 ? 266  THR A N   1 
ATOM   1804 C  CA  . THR A 1 264 ? 10.029 14.372 37.158  1.00 17.87 ? 266  THR A CA  1 
ATOM   1805 C  C   . THR A 1 264 ? 9.389  15.360 38.139  1.00 18.38 ? 266  THR A C   1 
ATOM   1806 O  O   . THR A 1 264 ? 8.182  15.323 38.372  1.00 19.91 ? 266  THR A O   1 
ATOM   1807 C  CB  . THR A 1 264 ? 9.974  12.939 37.716  1.00 17.90 ? 266  THR A CB  1 
ATOM   1808 O  OG1 . THR A 1 264 ? 10.697 12.908 38.950  1.00 16.76 ? 266  THR A OG1 1 
ATOM   1809 C  CG2 . THR A 1 264 ? 10.545 11.920 36.755  1.00 17.99 ? 266  THR A CG2 1 
ATOM   1810 N  N   . LEU A 1 265 ? 10.203 16.223 38.762  1.00 17.79 ? 267  LEU A N   1 
ATOM   1811 C  CA  . LEU A 1 265 ? 9.692  17.355 39.526  1.00 17.93 ? 267  LEU A CA  1 
ATOM   1812 C  C   . LEU A 1 265 ? 9.692  18.578 38.611  1.00 17.70 ? 267  LEU A C   1 
ATOM   1813 O  O   . LEU A 1 265 ? 10.729 19.206 38.401  1.00 16.84 ? 267  LEU A O   1 
ATOM   1814 C  CB  . LEU A 1 265 ? 10.556 17.588 40.770  1.00 17.44 ? 267  LEU A CB  1 
ATOM   1815 C  CG  . LEU A 1 265 ? 10.719 16.365 41.672  1.00 17.55 ? 267  LEU A CG  1 
ATOM   1816 C  CD1 . LEU A 1 265 ? 11.315 16.738 43.014  1.00 17.30 ? 267  LEU A CD1 1 
ATOM   1817 C  CD2 . LEU A 1 265 ? 9.393  15.637 41.868  1.00 18.80 ? 267  LEU A CD2 1 
ATOM   1818 N  N   . PRO A 1 266 ? 8.541  18.945 38.020  1.00 18.50 ? 268  PRO A N   1 
ATOM   1819 C  CA  . PRO A 1 266 ? 8.538  19.954 36.948  1.00 18.74 ? 268  PRO A CA  1 
ATOM   1820 C  C   . PRO A 1 266 ? 8.871  21.396 37.357  1.00 18.65 ? 268  PRO A C   1 
ATOM   1821 O  O   . PRO A 1 266 ? 9.324  22.192 36.530  1.00 18.55 ? 268  PRO A O   1 
ATOM   1822 C  CB  . PRO A 1 266 ? 7.102  19.863 36.402  1.00 20.23 ? 268  PRO A CB  1 
ATOM   1823 C  CG  . PRO A 1 266 ? 6.280  19.344 37.578  1.00 20.89 ? 268  PRO A CG  1 
ATOM   1824 C  CD  . PRO A 1 266 ? 7.208  18.401 38.317  1.00 19.62 ? 268  PRO A CD  1 
ATOM   1825 N  N   . ASN A 1 267 ? 8.668  21.738 38.633  1.00 18.67 ? 269  ASN A N   1 
ATOM   1826 C  CA  . ASN A 1 267 ? 8.950  23.094 39.090  1.00 19.05 ? 269  ASN A CA  1 
ATOM   1827 C  C   . ASN A 1 267 ? 10.414 23.259 39.488  1.00 17.47 ? 269  ASN A C   1 
ATOM   1828 O  O   . ASN A 1 267 ? 10.800 24.330 39.905  1.00 17.67 ? 269  ASN A O   1 
ATOM   1829 C  CB  . ASN A 1 267 ? 8.037  23.527 40.237  1.00 20.17 ? 269  ASN A CB  1 
ATOM   1830 C  CG  . ASN A 1 267 ? 6.594  23.632 39.787  1.00 22.16 ? 269  ASN A CG  1 
ATOM   1831 O  OD1 . ASN A 1 267 ? 5.726  22.989 40.369  1.00 23.52 ? 269  ASN A OD1 1 
ATOM   1832 N  ND2 . ASN A 1 267 ? 6.322  24.406 38.745  1.00 22.72 ? 269  ASN A ND2 1 
ATOM   1833 N  N   . VAL A 1 268 ? 11.220 22.203 39.371  1.00 16.50 ? 270  VAL A N   1 
ATOM   1834 C  CA  . VAL A 1 268 ? 12.650 22.287 39.587  1.00 15.48 ? 270  VAL A CA  1 
ATOM   1835 C  C   . VAL A 1 268 ? 13.313 22.749 38.292  1.00 15.69 ? 270  VAL A C   1 
ATOM   1836 O  O   . VAL A 1 268 ? 13.046 22.189 37.243  1.00 15.60 ? 270  VAL A O   1 
ATOM   1837 C  CB  . VAL A 1 268 ? 13.215 20.945 40.086  1.00 14.78 ? 270  VAL A CB  1 
ATOM   1838 C  CG1 . VAL A 1 268 ? 14.732 20.972 40.133  1.00 13.91 ? 270  VAL A CG1 1 
ATOM   1839 C  CG2 . VAL A 1 268 ? 12.619 20.565 41.437  1.00 14.80 ? 270  VAL A CG2 1 
ATOM   1840 N  N   . ASN A 1 269 ? 14.200 23.751 38.401  1.00 15.72 ? 271  ASN A N   1 
ATOM   1841 C  CA  . ASN A 1 269 ? 14.904 24.345 37.275  1.00 16.54 ? 271  ASN A CA  1 
ATOM   1842 C  C   . ASN A 1 269 ? 16.299 24.786 37.727  1.00 15.95 ? 271  ASN A C   1 
ATOM   1843 O  O   . ASN A 1 269 ? 16.678 24.591 38.884  1.00 14.79 ? 271  ASN A O   1 
ATOM   1844 C  CB  . ASN A 1 269 ? 14.096 25.498 36.669  1.00 18.57 ? 271  ASN A CB  1 
ATOM   1845 C  CG  . ASN A 1 269 ? 13.804 26.575 37.689  1.00 20.05 ? 271  ASN A CG  1 
ATOM   1846 O  OD1 . ASN A 1 269 ? 14.694 27.310 38.127  1.00 20.35 ? 271  ASN A OD1 1 
ATOM   1847 N  ND2 . ASN A 1 269 ? 12.561 26.642 38.124  1.00 21.77 ? 271  ASN A ND2 1 
ATOM   1848 N  N   . GLU A 1 270 ? 17.079 25.321 36.778  1.00 16.53 ? 272  GLU A N   1 
ATOM   1849 C  CA  . GLU A 1 270 ? 18.480 25.682 36.970  1.00 17.12 ? 272  GLU A CA  1 
ATOM   1850 C  C   . GLU A 1 270 ? 18.669 26.610 38.159  1.00 17.20 ? 272  GLU A C   1 
ATOM   1851 O  O   . GLU A 1 270 ? 19.727 26.563 38.785  1.00 16.95 ? 272  GLU A O   1 
ATOM   1852 C  CB  . GLU A 1 270 ? 19.106 26.343 35.739  1.00 18.87 ? 272  GLU A CB  1 
ATOM   1853 C  CG  . GLU A 1 270 ? 18.313 27.517 35.147  1.00 20.99 ? 272  GLU A CG  1 
ATOM   1854 C  CD  . GLU A 1 270 ? 17.253 27.126 34.117  1.00 22.65 ? 272  GLU A CD  1 
ATOM   1855 O  OE1 . GLU A 1 270 ? 16.902 25.932 34.025  1.00 22.91 ? 272  GLU A OE1 1 
ATOM   1856 O  OE2 . GLU A 1 270 ? 16.808 28.021 33.363  1.00 27.27 ? 272  GLU A OE2 1 
ATOM   1857 N  N   . ASN A 1 271 ? 17.643 27.402 38.498  1.00 18.19 ? 273  ASN A N   1 
ATOM   1858 C  CA  . ASN A 1 271 ? 17.761 28.385 39.574  1.00 19.16 ? 273  ASN A CA  1 
ATOM   1859 C  C   . ASN A 1 271 ? 17.158 27.884 40.891  1.00 17.81 ? 273  ASN A C   1 
ATOM   1860 O  O   . ASN A 1 271 ? 17.145 28.622 41.886  1.00 17.37 ? 273  ASN A O   1 
ATOM   1861 C  CB  . ASN A 1 271 ? 17.154 29.713 39.119  1.00 22.18 ? 273  ASN A CB  1 
ATOM   1862 C  CG  . ASN A 1 271 ? 18.012 30.358 38.044  1.00 24.74 ? 273  ASN A CG  1 
ATOM   1863 O  OD1 . ASN A 1 271 ? 19.192 30.636 38.246  1.00 28.13 ? 273  ASN A OD1 1 
ATOM   1864 N  ND2 . ASN A 1 271 ? 17.420 30.591 36.879  1.00 26.22 ? 273  ASN A ND2 1 
ATOM   1865 N  N   . SER A 1 272 ? 16.721 26.626 40.911  1.00 16.56 ? 274  SER A N   1 
ATOM   1866 C  CA  . SER A 1 272 ? 16.150 26.007 42.100  1.00 16.50 ? 274  SER A CA  1 
ATOM   1867 C  C   . SER A 1 272 ? 17.270 25.603 43.045  1.00 15.83 ? 274  SER A C   1 
ATOM   1868 O  O   . SER A 1 272 ? 18.369 25.269 42.605  1.00 15.91 ? 274  SER A O   1 
ATOM   1869 C  CB  . SER A 1 272 ? 15.303 24.778 41.769  1.00 16.08 ? 274  SER A CB  1 
ATOM   1870 O  OG  . SER A 1 272 ? 14.226 25.100 40.890  1.00 16.81 ? 274  SER A OG  1 
ATOM   1871 N  N   . LYS A 1 273 ? 16.961 25.621 44.339  1.00 16.06 ? 275  LYS A N   1 
ATOM   1872 C  CA  . LYS A 1 273 ? 17.807 25.015 45.356  1.00 15.60 ? 275  LYS A CA  1 
ATOM   1873 C  C   . LYS A 1 273 ? 17.046 23.845 45.983  1.00 14.50 ? 275  LYS A C   1 
ATOM   1874 O  O   . LYS A 1 273 ? 15.864 23.948 46.295  1.00 14.76 ? 275  LYS A O   1 
ATOM   1875 C  CB  . LYS A 1 273 ? 18.224 26.047 46.399  1.00 17.22 ? 275  LYS A CB  1 
ATOM   1876 C  CG  . LYS A 1 273 ? 19.200 27.108 45.896  1.00 19.25 ? 275  LYS A CG  1 
ATOM   1877 C  CD  . LYS A 1 273 ? 19.578 28.066 46.980  1.00 21.56 ? 275  LYS A CD  1 
ATOM   1878 C  CE  . LYS A 1 273 ? 20.718 28.999 46.645  1.00 24.49 ? 275  LYS A CE  1 
ATOM   1879 N  NZ  . LYS A 1 273 ? 21.380 29.439 47.907  1.00 27.45 ? 275  LYS A NZ  1 
ATOM   1880 N  N   . ILE A 1 274 ? 17.749 22.724 46.155  1.00 13.45 ? 276  ILE A N   1 
ATOM   1881 C  CA  . ILE A 1 274 ? 17.218 21.599 46.901  1.00 13.06 ? 276  ILE A CA  1 
ATOM   1882 C  C   . ILE A 1 274 ? 17.848 21.613 48.286  1.00 12.45 ? 276  ILE A C   1 
ATOM   1883 O  O   . ILE A 1 274 ? 19.064 21.568 48.390  1.00 12.54 ? 276  ILE A O   1 
ATOM   1884 C  CB  . ILE A 1 274 ? 17.481 20.271 46.162  1.00 12.68 ? 276  ILE A CB  1 
ATOM   1885 C  CG1 . ILE A 1 274 ? 16.945 20.308 44.725  1.00 12.91 ? 276  ILE A CG1 1 
ATOM   1886 C  CG2 . ILE A 1 274 ? 16.903 19.105 46.937  1.00 12.81 ? 276  ILE A CG2 1 
ATOM   1887 C  CD1 . ILE A 1 274 ? 15.479 20.643 44.635  1.00 13.61 ? 276  ILE A CD1 1 
ATOM   1888 N  N   . VAL A 1 275 ? 17.009 21.652 49.322  1.00 12.26 ? 277  VAL A N   1 
ATOM   1889 C  CA  . VAL A 1 275 ? 17.465 21.781 50.695  1.00 12.05 ? 277  VAL A CA  1 
ATOM   1890 C  C   . VAL A 1 275 ? 16.948 20.597 51.500  1.00 11.85 ? 277  VAL A C   1 
ATOM   1891 O  O   . VAL A 1 275 ? 15.743 20.358 51.570  1.00 12.25 ? 277  VAL A O   1 
ATOM   1892 C  CB  . VAL A 1 275 ? 16.998 23.120 51.297  1.00 12.83 ? 277  VAL A CB  1 
ATOM   1893 C  CG1 . VAL A 1 275 ? 17.531 23.348 52.717  1.00 12.75 ? 277  VAL A CG1 1 
ATOM   1894 C  CG2 . VAL A 1 275 ? 17.378 24.274 50.377  1.00 13.04 ? 277  VAL A CG2 1 
ATOM   1895 N  N   . ILE A 1 276 ? 17.898 19.878 52.121  1.00 11.51 ? 278  ILE A N   1 
ATOM   1896 C  CA  . ILE A 1 276 ? 17.610 18.771 53.027  1.00 11.44 ? 278  ILE A CA  1 
ATOM   1897 C  C   . ILE A 1 276 ? 17.864 19.209 54.468  1.00 11.32 ? 278  ILE A C   1 
ATOM   1898 O  O   . ILE A 1 276 ? 18.938 19.692 54.774  1.00 11.03 ? 278  ILE A O   1 
ATOM   1899 C  CB  . ILE A 1 276 ? 18.487 17.564 52.666  1.00 11.00 ? 278  ILE A CB  1 
ATOM   1900 C  CG1 . ILE A 1 276 ? 18.226 17.120 51.226  1.00 11.23 ? 278  ILE A CG1 1 
ATOM   1901 C  CG2 . ILE A 1 276 ? 18.288 16.442 53.679  1.00 11.21 ? 278  ILE A CG2 1 
ATOM   1902 C  CD1 . ILE A 1 276 ? 19.308 16.242 50.651  1.00 11.14 ? 278  ILE A CD1 1 
ATOM   1903 N  N   . ARG A 1 277 ? 16.884 19.004 55.347  1.00 11.81 ? 279  ARG A N   1 
ATOM   1904 C  CA  . ARG A 1 277 ? 17.039 19.289 56.765  1.00 12.41 ? 279  ARG A CA  1 
ATOM   1905 C  C   . ARG A 1 277 ? 16.721 18.031 57.565  1.00 12.28 ? 279  ARG A C   1 
ATOM   1906 O  O   . ARG A 1 277 ? 15.840 17.257 57.198  1.00 12.40 ? 279  ARG A O   1 
ATOM   1907 C  CB  . ARG A 1 277 ? 16.119 20.428 57.216  1.00 13.35 ? 279  ARG A CB  1 
ATOM   1908 C  CG  . ARG A 1 277 ? 16.450 21.754 56.556  1.00 13.93 ? 279  ARG A CG  1 
ATOM   1909 C  CD  . ARG A 1 277 ? 15.740 22.944 57.188  1.00 15.33 ? 279  ARG A CD  1 
ATOM   1910 N  NE  . ARG A 1 277 ? 16.032 24.146 56.416  1.00 16.15 ? 279  ARG A NE  1 
ATOM   1911 C  CZ  . ARG A 1 277 ? 15.231 24.714 55.505  1.00 17.02 ? 279  ARG A CZ  1 
ATOM   1912 N  NH1 . ARG A 1 277 ? 14.007 24.271 55.322  1.00 18.02 ? 279  ARG A NH1 1 
ATOM   1913 N  NH2 . ARG A 1 277 ? 15.639 25.758 54.801  1.00 17.24 ? 279  ARG A NH2 1 
ATOM   1914 N  N   . TYR A 1 278 ? 17.478 17.848 58.648  1.00 12.01 ? 280  TYR A N   1 
ATOM   1915 C  CA  . TYR A 1 278 ? 17.201 16.824 59.633  1.00 12.48 ? 280  TYR A CA  1 
ATOM   1916 C  C   . TYR A 1 278 ? 17.841 17.266 60.938  1.00 12.34 ? 280  TYR A C   1 
ATOM   1917 O  O   . TYR A 1 278 ? 18.618 18.216 60.953  1.00 11.94 ? 280  TYR A O   1 
ATOM   1918 C  CB  . TYR A 1 278 ? 17.726 15.483 59.115  1.00 12.61 ? 280  TYR A CB  1 
ATOM   1919 C  CG  . TYR A 1 278 ? 19.236 15.369 59.034  1.00 12.21 ? 280  TYR A CG  1 
ATOM   1920 C  CD1 . TYR A 1 278 ? 19.991 15.103 60.162  1.00 12.80 ? 280  TYR A CD1 1 
ATOM   1921 C  CD2 . TYR A 1 278 ? 19.903 15.558 57.842  1.00 12.26 ? 280  TYR A CD2 1 
ATOM   1922 C  CE1 . TYR A 1 278 ? 21.370 15.010 60.093  1.00 12.74 ? 280  TYR A CE1 1 
ATOM   1923 C  CE2 . TYR A 1 278 ? 21.278 15.450 57.750  1.00 12.21 ? 280  TYR A CE2 1 
ATOM   1924 C  CZ  . TYR A 1 278 ? 22.016 15.165 58.883  1.00 12.68 ? 280  TYR A CZ  1 
ATOM   1925 O  OH  . TYR A 1 278 ? 23.383 15.080 58.809  1.00 13.24 ? 280  TYR A OH  1 
ATOM   1926 N  N   . THR A 1 279 ? 17.505 16.586 62.029  1.00 12.91 ? 281  THR A N   1 
ATOM   1927 C  CA  . THR A 1 279 ? 18.093 16.910 63.323  1.00 13.16 ? 281  THR A CA  1 
ATOM   1928 C  C   . THR A 1 279 ? 18.721 15.663 63.937  1.00 13.31 ? 281  THR A C   1 
ATOM   1929 O  O   . THR A 1 279 ? 18.374 14.544 63.590  1.00 13.80 ? 281  THR A O   1 
ATOM   1930 C  CB  . THR A 1 279 ? 17.068 17.496 64.293  1.00 13.98 ? 281  THR A CB  1 
ATOM   1931 O  OG1 . THR A 1 279 ? 16.170 16.456 64.657  1.00 15.05 ? 281  THR A OG1 1 
ATOM   1932 C  CG2 . THR A 1 279 ? 16.327 18.674 63.709  1.00 14.42 ? 281  THR A CG2 1 
ATOM   1933 N  N   . ALA A 1 280 ? 19.693 15.879 64.815  1.00 13.24 ? 282  ALA A N   1 
ATOM   1934 C  CA  . ALA A 1 280 ? 20.330 14.805 65.552  1.00 13.65 ? 282  ALA A CA  1 
ATOM   1935 C  C   . ALA A 1 280 ? 20.511 15.273 66.987  1.00 14.19 ? 282  ALA A C   1 
ATOM   1936 O  O   . ALA A 1 280 ? 20.252 16.427 67.307  1.00 14.02 ? 282  ALA A O   1 
ATOM   1937 C  CB  . ALA A 1 280 ? 21.649 14.449 64.904  1.00 12.83 ? 282  ALA A CB  1 
ATOM   1938 N  N   . ARG A 1 281 ? 20.943 14.361 67.843  1.00 15.38 ? 283  ARG A N   1 
ATOM   1939 C  CA  . ARG A 1 281 ? 21.273 14.704 69.216  1.00 16.76 ? 283  ARG A CA  1 
ATOM   1940 C  C   . ARG A 1 281 ? 22.556 13.995 69.626  1.00 16.29 ? 283  ARG A C   1 
ATOM   1941 O  O   . ARG A 1 281 ? 22.848 12.926 69.114  1.00 15.95 ? 283  ARG A O   1 
ATOM   1942 C  CB  . ARG A 1 281 ? 20.126 14.345 70.159  1.00 19.59 ? 283  ARG A CB  1 
ATOM   1943 C  CG  . ARG A 1 281 ? 19.624 12.914 70.058  1.00 22.25 ? 283  ARG A CG  1 
ATOM   1944 C  CD  . ARG A 1 281 ? 18.515 12.696 71.072  1.00 25.50 ? 283  ARG A CD  1 
ATOM   1945 N  NE  . ARG A 1 281 ? 18.303 11.275 71.336  1.00 29.01 ? 283  ARG A NE  1 
ATOM   1946 C  CZ  . ARG A 1 281 ? 17.739 10.421 70.487  1.00 32.13 ? 283  ARG A CZ  1 
ATOM   1947 N  NH1 . ARG A 1 281 ? 17.288 10.839 69.319  1.00 33.01 ? 283  ARG A NH1 1 
ATOM   1948 N  NH2 . ARG A 1 281 ? 17.610 9.145  70.807  1.00 35.30 ? 283  ARG A NH2 1 
ATOM   1949 N  N   . LEU A 1 282 ? 23.342 14.637 70.500  1.00 15.94 ? 284  LEU A N   1 
ATOM   1950 C  CA  . LEU A 1 282 ? 24.621 14.105 70.931  1.00 15.88 ? 284  LEU A CA  1 
ATOM   1951 C  C   . LEU A 1 282 ? 24.381 12.861 71.793  1.00 16.75 ? 284  LEU A C   1 
ATOM   1952 O  O   . LEU A 1 282 ? 23.399 12.780 72.520  1.00 16.45 ? 284  LEU A O   1 
ATOM   1953 C  CB  . LEU A 1 282 ? 25.355 15.180 71.746  1.00 16.15 ? 284  LEU A CB  1 
ATOM   1954 C  CG  . LEU A 1 282 ? 25.965 16.345 70.972  1.00 15.58 ? 284  LEU A CG  1 
ATOM   1955 C  CD1 . LEU A 1 282 ? 26.418 17.447 71.928  1.00 16.09 ? 284  LEU A CD1 1 
ATOM   1956 C  CD2 . LEU A 1 282 ? 27.133 15.864 70.122  1.00 15.35 ? 284  LEU A CD2 1 
ATOM   1957 N  N   . LYS A 1 283 ? 25.258 11.863 71.632  1.00 17.52 ? 285  LYS A N   1 
ATOM   1958 C  CA  . LYS A 1 283 ? 25.327 10.738 72.541  1.00 19.10 ? 285  LYS A CA  1 
ATOM   1959 C  C   . LYS A 1 283 ? 26.158 11.154 73.742  1.00 19.63 ? 285  LYS A C   1 
ATOM   1960 O  O   . LYS A 1 283 ? 26.838 12.164 73.702  1.00 18.41 ? 285  LYS A O   1 
ATOM   1961 C  CB  . LYS A 1 283 ? 26.005 9.539  71.883  1.00 20.26 ? 285  LYS A CB  1 
ATOM   1962 C  CG  . LYS A 1 283 ? 25.320 9.026  70.633  1.00 20.98 ? 285  LYS A CG  1 
ATOM   1963 C  CD  . LYS A 1 283 ? 26.144 7.995  69.925  1.00 22.07 ? 285  LYS A CD  1 
ATOM   1964 C  CE  . LYS A 1 283 ? 25.342 7.216  68.921  1.00 23.46 ? 285  LYS A CE  1 
ATOM   1965 N  NZ  . LYS A 1 283 ? 26.235 6.306  68.172  1.00 25.15 ? 285  LYS A NZ  1 
ATOM   1966 N  N   . ASP A 1 284 ? 26.126 10.328 74.784  1.00 21.24 ? 286  ASP A N   1 
ATOM   1967 C  CA  . ASP A 1 284 ? 26.944 10.549 75.963  1.00 22.59 ? 286  ASP A CA  1 
ATOM   1968 C  C   . ASP A 1 284 ? 28.350 9.981  75.762  1.00 21.81 ? 286  ASP A C   1 
ATOM   1969 O  O   . ASP A 1 284 ? 29.103 9.903  76.728  1.00 24.10 ? 286  ASP A O   1 
ATOM   1970 C  CB  . ASP A 1 284 ? 26.276 9.923  77.189  1.00 24.78 ? 286  ASP A CB  1 
ATOM   1971 C  CG  . ASP A 1 284 ? 26.020 8.429  77.067  1.00 27.24 ? 286  ASP A CG  1 
ATOM   1972 O  OD1 . ASP A 1 284 ? 26.307 7.853  76.008  1.00 28.66 ? 286  ASP A OD1 1 
ATOM   1973 O  OD2 . ASP A 1 284 ? 25.563 7.835  78.051  1.00 31.88 ? 286  ASP A OD2 1 
ATOM   1974 N  N   . SER A 1 285 ? 28.659 9.528  74.545  1.00 20.11 ? 287  SER A N   1 
ATOM   1975 C  CA  . SER A 1 285 ? 29.983 9.100  74.149  1.00 19.30 ? 287  SER A CA  1 
ATOM   1976 C  C   . SER A 1 285 ? 30.494 9.973  72.990  1.00 17.55 ? 287  SER A C   1 
ATOM   1977 O  O   . SER A 1 285 ? 31.459 9.622  72.325  1.00 17.12 ? 287  SER A O   1 
ATOM   1978 C  CB  . SER A 1 285 ? 29.935 7.653  73.771  1.00 20.05 ? 287  SER A CB  1 
ATOM   1979 O  OG  . SER A 1 285 ? 29.131 7.489  72.613  1.00 19.96 ? 287  SER A OG  1 
ATOM   1980 N  N   . ALA A 1 286 ? 29.868 11.132 72.739  1.00 16.28 ? 288  ALA A N   1 
ATOM   1981 C  CA  . ALA A 1 286 ? 30.316 12.011 71.661  1.00 15.10 ? 288  ALA A CA  1 
ATOM   1982 C  C   . ALA A 1 286 ? 31.754 12.478 71.916  1.00 15.06 ? 288  ALA A C   1 
ATOM   1983 O  O   . ALA A 1 286 ? 32.201 12.554 73.068  1.00 15.60 ? 288  ALA A O   1 
ATOM   1984 C  CB  . ALA A 1 286 ? 29.377 13.188 71.557  1.00 14.59 ? 288  ALA A CB  1 
ATOM   1985 N  N   . THR A 1 287 ? 32.500 12.744 70.843  1.00 14.53 ? 289  THR A N   1 
ATOM   1986 C  CA  . THR A 1 287 ? 33.876 13.186 70.970  1.00 14.89 ? 289  THR A CA  1 
ATOM   1987 C  C   . THR A 1 287 ? 33.876 14.548 71.672  1.00 14.55 ? 289  THR A C   1 
ATOM   1988 O  O   . THR A 1 287 ? 33.108 15.436 71.298  1.00 13.77 ? 289  THR A O   1 
ATOM   1989 C  CB  . THR A 1 287 ? 34.556 13.274 69.599  1.00 14.94 ? 289  THR A CB  1 
ATOM   1990 O  OG1 . THR A 1 287 ? 34.506 12.006 68.947  1.00 15.18 ? 289  THR A OG1 1 
ATOM   1991 C  CG2 . THR A 1 287 ? 36.004 13.705 69.668  1.00 15.69 ? 289  THR A CG2 1 
ATOM   1992 N  N   . LEU A 1 288 ? 34.752 14.705 72.673  1.00 15.19 ? 290  LEU A N   1 
ATOM   1993 C  CA  . LEU A 1 288 ? 34.900 15.958 73.392  1.00 15.40 ? 290  LEU A CA  1 
ATOM   1994 C  C   . LEU A 1 288 ? 36.064 16.730 72.788  1.00 15.90 ? 290  LEU A C   1 
ATOM   1995 O  O   . LEU A 1 288 ? 37.002 16.131 72.268  1.00 16.88 ? 290  LEU A O   1 
ATOM   1996 C  CB  . LEU A 1 288 ? 35.203 15.682 74.862  1.00 16.19 ? 290  LEU A CB  1 
ATOM   1997 C  CG  . LEU A 1 288 ? 34.236 14.720 75.532  1.00 16.32 ? 290  LEU A CG  1 
ATOM   1998 C  CD1 . LEU A 1 288 ? 34.734 14.347 76.917  1.00 17.34 ? 290  LEU A CD1 1 
ATOM   1999 C  CD2 . LEU A 1 288 ? 32.849 15.332 75.575  1.00 15.75 ? 290  LEU A CD2 1 
ATOM   2000 N  N   . GLY A 1 289 ? 36.021 18.060 72.903  1.00 15.83 ? 291  GLY A N   1 
ATOM   2001 C  CA  . GLY A 1 289 ? 37.187 18.872 72.626  1.00 16.35 ? 291  GLY A CA  1 
ATOM   2002 C  C   . GLY A 1 289 ? 37.357 19.141 71.138  1.00 15.94 ? 291  GLY A C   1 
ATOM   2003 O  O   . GLY A 1 289 ? 36.370 19.219 70.389  1.00 14.83 ? 291  GLY A O   1 
ATOM   2004 N  N   . THR A 1 290 ? 38.624 19.292 70.744  1.00 16.71 ? 292  THR A N   1 
ATOM   2005 C  CA  . THR A 1 290 ? 38.965 19.964 69.503  1.00 16.81 ? 292  THR A CA  1 
ATOM   2006 C  C   . THR A 1 290 ? 38.793 19.054 68.294  1.00 16.31 ? 292  THR A C   1 
ATOM   2007 O  O   . THR A 1 290 ? 38.683 19.564 67.184  1.00 15.96 ? 292  THR A O   1 
ATOM   2008 C  CB  . THR A 1 290 ? 40.398 20.502 69.507  1.00 18.11 ? 292  THR A CB  1 
ATOM   2009 O  OG1 . THR A 1 290 ? 41.254 19.439 69.922  1.00 19.04 ? 292  THR A OG1 1 
ATOM   2010 C  CG2 . THR A 1 290 ? 40.578 21.702 70.400  1.00 18.79 ? 292  THR A CG2 1 
ATOM   2011 N  N   . THR A 1 291 ? 38.770 17.726 68.489  1.00 16.41 ? 293  THR A N   1 
ATOM   2012 C  CA  . THR A 1 291 ? 38.564 16.821 67.358  1.00 15.83 ? 293  THR A CA  1 
ATOM   2013 C  C   . THR A 1 291 ? 37.171 17.051 66.782  1.00 14.29 ? 293  THR A C   1 
ATOM   2014 O  O   . THR A 1 291 ? 36.995 17.104 65.582  1.00 13.49 ? 293  THR A O   1 
ATOM   2015 C  CB  . THR A 1 291 ? 38.787 15.352 67.752  1.00 16.69 ? 293  THR A CB  1 
ATOM   2016 O  OG1 . THR A 1 291 ? 40.183 15.192 68.024  1.00 18.09 ? 293  THR A OG1 1 
ATOM   2017 C  CG2 . THR A 1 291 ? 38.376 14.344 66.698  1.00 16.28 ? 293  THR A CG2 1 
ATOM   2018 N  N   . GLY A 1 292 ? 36.168 17.144 67.649  1.00 13.68 ? 294  GLY A N   1 
ATOM   2019 C  CA  . GLY A 1 292 ? 34.807 17.431 67.217  1.00 12.74 ? 294  GLY A CA  1 
ATOM   2020 C  C   . GLY A 1 292 ? 34.091 16.186 66.696  1.00 12.25 ? 294  GLY A C   1 
ATOM   2021 O  O   . GLY A 1 292 ? 34.641 15.096 66.700  1.00 12.55 ? 294  GLY A O   1 
ATOM   2022 N  N   . ASN A 1 293 ? 32.824 16.374 66.330  1.00 11.58 ? 295  ASN A N   1 
ATOM   2023 C  CA  . ASN A 1 293 ? 31.985 15.322 65.786  1.00 11.48 ? 295  ASN A CA  1 
ATOM   2024 C  C   . ASN A 1 293 ? 31.560 15.733 64.386  1.00 10.95 ? 295  ASN A C   1 
ATOM   2025 O  O   . ASN A 1 293 ? 30.670 16.568 64.256  1.00 10.17 ? 295  ASN A O   1 
ATOM   2026 C  CB  . ASN A 1 293 ? 30.785 15.070 66.691  1.00 11.58 ? 295  ASN A CB  1 
ATOM   2027 C  CG  . ASN A 1 293 ? 31.198 14.694 68.094  1.00 12.27 ? 295  ASN A CG  1 
ATOM   2028 O  OD1 . ASN A 1 293 ? 31.553 13.541 68.364  1.00 12.94 ? 295  ASN A OD1 1 
ATOM   2029 N  ND2 . ASN A 1 293 ? 31.131 15.652 69.010  1.00 12.49 ? 295  ASN A ND2 1 
ATOM   2030 N  N   . SER A 1 294 ? 32.212 15.161 63.361  1.00 11.31 ? 296  SER A N   1 
ATOM   2031 C  CA  . SER A 1 294 ? 32.067 15.649 62.004  1.00 11.01 ? 296  SER A CA  1 
ATOM   2032 C  C   . SER A 1 294 ? 31.243 14.679 61.151  1.00 10.88 ? 296  SER A C   1 
ATOM   2033 O  O   . SER A 1 294 ? 31.218 13.476 61.373  1.00 10.92 ? 296  SER A O   1 
ATOM   2034 C  CB  . SER A 1 294 ? 33.416 15.905 61.350  1.00 11.51 ? 296  SER A CB  1 
ATOM   2035 O  OG  . SER A 1 294 ? 34.117 16.914 62.045  1.00 12.22 ? 296  SER A OG  1 
ATOM   2036 N  N   . ASN A 1 295 ? 30.595 15.238 60.128  1.00 10.36 ? 297  ASN A N   1 
ATOM   2037 C  CA  . ASN A 1 295 ? 29.913 14.464 59.102  1.00 10.39 ? 297  ASN A CA  1 
ATOM   2038 C  C   . ASN A 1 295 ? 30.194 15.113 57.757  1.00 10.48 ? 297  ASN A C   1 
ATOM   2039 O  O   . ASN A 1 295 ? 30.436 16.325 57.695  1.00 10.55 ? 297  ASN A O   1 
ATOM   2040 C  CB  . ASN A 1 295 ? 28.412 14.398 59.354  1.00 10.20 ? 297  ASN A CB  1 
ATOM   2041 C  CG  . ASN A 1 295 ? 27.738 15.747 59.176  1.00 9.98  ? 297  ASN A CG  1 
ATOM   2042 O  OD1 . ASN A 1 295 ? 27.973 16.720 59.908  1.00 10.04 ? 297  ASN A OD1 1 
ATOM   2043 N  N   . THR A 1 296 ? 30.187 14.284 56.707  1.00 10.74 ? 298  THR A N   1 
ATOM   2044 C  CA  . THR A 1 296 ? 30.507 14.756 55.373  1.00 11.08 ? 298  THR A CA  1 
ATOM   2045 C  C   . THR A 1 296 ? 29.355 14.365 54.458  1.00 10.36 ? 298  THR A C   1 
ATOM   2046 O  O   . THR A 1 296 ? 28.756 13.299 54.593  1.00 10.30 ? 298  THR A O   1 
ATOM   2047 C  CB  . THR A 1 296 ? 31.860 14.227 54.866  1.00 12.31 ? 298  THR A CB  1 
ATOM   2048 O  OG1 . THR A 1 296 ? 31.808 12.812 54.987  1.00 13.68 ? 298  THR A OG1 1 
ATOM   2049 C  CG2 . THR A 1 296 ? 33.049 14.770 55.639  1.00 13.25 ? 298  THR A CG2 1 
ATOM   2050 N  N   . ALA A 1 297 ? 29.094 15.242 53.493  1.00 9.87  ? 299  ALA A N   1 
ATOM   2051 C  CA  . ALA A 1 297 ? 28.043 15.007 52.535  1.00 9.62  ? 299  ALA A CA  1 
ATOM   2052 C  C   . ALA A 1 297 ? 28.558 15.373 51.155  1.00 9.87  ? 299  ALA A C   1 
ATOM   2053 O  O   . ALA A 1 297 ? 29.357 16.293 51.018  1.00 9.84  ? 299  ALA A O   1 
ATOM   2054 C  CB  . ALA A 1 297 ? 26.834 15.812 52.916  1.00 9.16  ? 299  ALA A CB  1 
ATOM   2055 N  N   . SER A 1 298 ? 28.086 14.636 50.156  1.00 10.45 ? 300  SER A N   1 
ATOM   2056 C  CA  . SER A 1 298 ? 28.438 14.889 48.767  1.00 11.14 ? 300  SER A CA  1 
ATOM   2057 C  C   . SER A 1 298 ? 27.242 14.552 47.884  1.00 10.87 ? 300  SER A C   1 
ATOM   2058 O  O   . SER A 1 298 ? 26.384 13.765 48.273  1.00 10.84 ? 300  SER A O   1 
ATOM   2059 C  CB  . SER A 1 298 ? 29.644 14.068 48.351  1.00 12.40 ? 300  SER A CB  1 
ATOM   2060 O  OG  . SER A 1 298 ? 29.319 12.690 48.348  1.00 13.76 ? 300  SER A OG  1 
ATOM   2061 N  N   . LEU A 1 299 ? 27.230 15.121 46.671  1.00 10.88 ? 301  LEU A N   1 
ATOM   2062 C  CA  . LEU A 1 299 ? 26.155 14.896 45.726  1.00 10.70 ? 301  LEU A CA  1 
ATOM   2063 C  C   . LEU A 1 299 ? 26.674 14.090 44.545  1.00 11.01 ? 301  LEU A C   1 
ATOM   2064 O  O   . LEU A 1 299 ? 27.721 14.403 43.983  1.00 11.24 ? 301  LEU A O   1 
ATOM   2065 C  CB  . LEU A 1 299 ? 25.622 16.257 45.263  1.00 10.63 ? 301  LEU A CB  1 
ATOM   2066 C  CG  . LEU A 1 299 ? 24.658 16.215 44.075  1.00 10.97 ? 301  LEU A CG  1 
ATOM   2067 C  CD1 . LEU A 1 299 ? 23.311 15.619 44.461  1.00 10.75 ? 301  LEU A CD1 1 
ATOM   2068 C  CD2 . LEU A 1 299 ? 24.459 17.614 43.501  1.00 11.02 ? 301  LEU A CD2 1 
ATOM   2069 N  N   . THR A 1 300 ? 25.901 13.071 44.164  1.00 11.08 ? 302  THR A N   1 
ATOM   2070 C  CA  . THR A 1 300 ? 26.078 12.378 42.896  1.00 11.29 ? 302  THR A CA  1 
ATOM   2071 C  C   . THR A 1 300 ? 25.070 12.914 41.877  1.00 11.07 ? 302  THR A C   1 
ATOM   2072 O  O   . THR A 1 300 ? 23.875 12.944 42.137  1.00 10.79 ? 302  THR A O   1 
ATOM   2073 C  CB  . THR A 1 300 ? 25.987 10.862 43.109  1.00 12.01 ? 302  THR A CB  1 
ATOM   2074 O  OG1 . THR A 1 300 ? 27.041 10.525 44.018  1.00 12.06 ? 302  THR A OG1 1 
ATOM   2075 C  CG2 . THR A 1 300 ? 26.129 10.076 41.818  1.00 12.56 ? 302  THR A CG2 1 
ATOM   2076 N  N   . TYR A 1 301 ? 25.566 13.339 40.713  1.00 10.97 ? 303  TYR A N   1 
ATOM   2077 C  CA  . TYR A 1 301 ? 24.761 14.058 39.734  1.00 10.82 ? 303  TYR A CA  1 
ATOM   2078 C  C   . TYR A 1 301 ? 25.099 13.585 38.324  1.00 11.03 ? 303  TYR A C   1 
ATOM   2079 O  O   . TYR A 1 301 ? 26.216 13.146 38.054  1.00 11.24 ? 303  TYR A O   1 
ATOM   2080 C  CB  . TYR A 1 301 ? 24.989 15.576 39.866  1.00 10.58 ? 303  TYR A CB  1 
ATOM   2081 C  CG  . TYR A 1 301 ? 26.444 15.998 39.706  1.00 10.61 ? 303  TYR A CG  1 
ATOM   2082 C  CD1 . TYR A 1 301 ? 27.316 15.971 40.789  1.00 10.37 ? 303  TYR A CD1 1 
ATOM   2083 C  CD2 . TYR A 1 301 ? 26.944 16.401 38.472  1.00 10.84 ? 303  TYR A CD2 1 
ATOM   2084 C  CE1 . TYR A 1 301 ? 28.644 16.330 40.648  1.00 10.90 ? 303  TYR A CE1 1 
ATOM   2085 C  CE2 . TYR A 1 301 ? 28.275 16.746 38.316  1.00 11.38 ? 303  TYR A CE2 1 
ATOM   2086 C  CZ  . TYR A 1 301 ? 29.118 16.733 39.419  1.00 11.52 ? 303  TYR A CZ  1 
ATOM   2087 O  OH  . TYR A 1 301 ? 30.419 17.103 39.315  1.00 12.32 ? 303  TYR A OH  1 
ATOM   2088 N  N   . SER A 1 302 ? 24.116 13.699 37.418  1.00 11.00 ? 304  SER A N   1 
ATOM   2089 C  CA  . SER A 1 302 ? 24.342 13.516 35.996  1.00 11.31 ? 304  SER A CA  1 
ATOM   2090 C  C   . SER A 1 302 ? 25.323 14.572 35.518  1.00 11.25 ? 304  SER A C   1 
ATOM   2091 O  O   . SER A 1 302 ? 25.025 15.752 35.679  1.00 10.95 ? 304  SER A O   1 
ATOM   2092 C  CB  . SER A 1 302 ? 23.064 13.626 35.227  1.00 11.35 ? 304  SER A CB  1 
ATOM   2093 O  OG  . SER A 1 302 ? 22.178 12.581 35.536  1.00 11.57 ? 304  SER A OG  1 
ATOM   2094 N  N   . ASN A 1 303 ? 26.418 14.154 34.865  1.00 11.82 ? 305  ASN A N   1 
ATOM   2095 C  CA  . ASN A 1 303 ? 27.515 15.060 34.547  1.00 12.13 ? 305  ASN A CA  1 
ATOM   2096 C  C   . ASN A 1 303 ? 27.678 15.291 33.032  1.00 12.97 ? 305  ASN A C   1 
ATOM   2097 O  O   . ASN A 1 303 ? 28.679 15.890 32.611  1.00 13.30 ? 305  ASN A O   1 
ATOM   2098 C  CB  . ASN A 1 303 ? 28.828 14.552 35.144  1.00 12.39 ? 305  ASN A CB  1 
ATOM   2099 C  CG  . ASN A 1 303 ? 29.362 13.320 34.446  1.00 13.21 ? 305  ASN A CG  1 
ATOM   2100 O  OD1 . ASN A 1 303 ? 28.623 12.587 33.786  1.00 13.38 ? 305  ASN A OD1 1 
ATOM   2101 N  ND2 . ASN A 1 303 ? 30.659 13.094 34.577  1.00 13.91 ? 305  ASN A ND2 1 
ATOM   2102 N  N   . ASN A 1 304 ? 26.731 14.804 32.203  1.00 13.36 ? 306  ASN A N   1 
ATOM   2103 C  CA  . ASN A 1 304 ? 26.801 14.985 30.762  1.00 14.35 ? 306  ASN A CA  1 
ATOM   2104 C  C   . ASN A 1 304 ? 25.396 15.180 30.196  1.00 14.63 ? 306  ASN A C   1 
ATOM   2105 O  O   . ASN A 1 304 ? 24.602 14.248 30.134  1.00 14.73 ? 306  ASN A O   1 
ATOM   2106 C  CB  . ASN A 1 304 ? 27.501 13.817 30.066  1.00 15.31 ? 306  ASN A CB  1 
ATOM   2107 C  CG  . ASN A 1 304 ? 27.750 14.065 28.590  1.00 16.12 ? 306  ASN A CG  1 
ATOM   2108 O  OD1 . ASN A 1 304 ? 27.277 15.037 28.014  1.00 16.11 ? 306  ASN A OD1 1 
ATOM   2109 N  ND2 . ASN A 1 304 ? 28.453 13.165 27.932  1.00 17.02 ? 306  ASN A ND2 1 
ATOM   2110 N  N   . PRO A 1 305 ? 25.046 16.399 29.724  1.00 15.39 ? 307  PRO A N   1 
ATOM   2111 C  CA  . PRO A 1 305 ? 23.713 16.666 29.194  1.00 16.13 ? 307  PRO A CA  1 
ATOM   2112 C  C   . PRO A 1 305 ? 23.492 16.233 27.750  1.00 17.78 ? 307  PRO A C   1 
ATOM   2113 O  O   . PRO A 1 305 ? 22.373 16.313 27.259  1.00 18.42 ? 307  PRO A O   1 
ATOM   2114 C  CB  . PRO A 1 305 ? 23.640 18.196 29.294  1.00 16.00 ? 307  PRO A CB  1 
ATOM   2115 C  CG  . PRO A 1 305 ? 25.047 18.645 29.020  1.00 16.24 ? 307  PRO A CG  1 
ATOM   2116 C  CD  . PRO A 1 305 ? 25.918 17.582 29.658  1.00 15.86 ? 307  PRO A CD  1 
ATOM   2117 N  N   . ASN A 1 306 ? 24.542 15.745 27.077  1.00 19.18 ? 308  ASN A N   1 
ATOM   2118 C  CA  . ASN A 1 306 ? 24.474 15.426 25.666  1.00 20.66 ? 308  ASN A CA  1 
ATOM   2119 C  C   . ASN A 1 306 ? 24.107 13.957 25.436  1.00 22.81 ? 308  ASN A C   1 
ATOM   2120 O  O   . ASN A 1 306 ? 24.580 13.067 26.130  1.00 22.44 ? 308  ASN A O   1 
ATOM   2121 C  CB  . ASN A 1 306 ? 25.800 15.751 24.971  1.00 21.11 ? 308  ASN A CB  1 
ATOM   2122 C  CG  . ASN A 1 306 ? 26.289 17.151 25.301  1.00 20.75 ? 308  ASN A CG  1 
ATOM   2123 O  OD1 . ASN A 1 306 ? 25.622 18.134 24.969  1.00 20.49 ? 308  ASN A OD1 1 
ATOM   2124 N  ND2 . ASN A 1 306 ? 27.447 17.252 25.930  1.00 19.99 ? 308  ASN A ND2 1 
ATOM   2125 N  N   . ASN A 1 307 ? 23.284 13.719 24.410  1.00 25.79 ? 309  ASN A N   1 
ATOM   2126 C  CA  . ASN A 1 307 ? 22.970 12.385 23.900  1.00 29.27 ? 309  ASN A CA  1 
ATOM   2127 C  C   . ASN A 1 307 ? 22.318 11.526 24.988  1.00 30.30 ? 309  ASN A C   1 
ATOM   2128 O  O   . ASN A 1 307 ? 22.526 10.312 25.035  1.00 30.35 ? 309  ASN A O   1 
ATOM   2129 C  CB  . ASN A 1 307 ? 24.197 11.691 23.296  1.00 32.07 ? 309  ASN A CB  1 
ATOM   2130 C  CG  . ASN A 1 307 ? 24.755 12.422 22.090  1.00 36.90 ? 309  ASN A CG  1 
ATOM   2131 O  OD1 . ASN A 1 307 ? 24.558 11.998 20.956  1.00 39.70 ? 309  ASN A OD1 1 
ATOM   2132 N  ND2 . ASN A 1 307 ? 25.426 13.544 22.307  1.00 38.71 ? 309  ASN A ND2 1 
ATOM   2133 N  N   . ASN A 1 308 ? 21.524 12.175 25.855  1.00 31.83 ? 310  ASN A N   1 
ATOM   2134 C  CA  A ASN A 1 308 ? 20.758 11.511 26.902  0.50 32.78 ? 310  ASN A CA  1 
ATOM   2135 C  CA  B ASN A 1 308 ? 20.753 11.485 26.882  0.50 32.18 ? 310  ASN A CA  1 
ATOM   2136 C  C   . ASN A 1 308 ? 21.672 10.581 27.713  1.00 33.19 ? 310  ASN A C   1 
ATOM   2137 O  O   . ASN A 1 308 ? 21.287 9.476  28.109  1.00 33.27 ? 310  ASN A O   1 
ATOM   2138 C  CB  A ASN A 1 308 ? 19.528 10.819 26.299  0.50 34.50 ? 310  ASN A CB  1 
ATOM   2139 C  CB  B ASN A 1 308 ? 19.601 10.699 26.242  0.50 32.97 ? 310  ASN A CB  1 
ATOM   2140 C  CG  A ASN A 1 308 ? 18.617 11.768 25.541  0.50 35.06 ? 310  ASN A CG  1 
ATOM   2141 C  CG  B ASN A 1 308 ? 18.521 10.281 27.219  0.50 32.30 ? 310  ASN A CG  1 
ATOM   2142 O  OD1 A ASN A 1 308 ? 19.044 12.452 24.613  0.50 36.77 ? 310  ASN A OD1 1 
ATOM   2143 O  OD1 B ASN A 1 308 ? 18.480 10.757 28.351  0.50 30.61 ? 310  ASN A OD1 1 
ATOM   2144 N  ND2 A ASN A 1 308 ? 17.353 11.822 25.922  0.50 35.04 ? 310  ASN A ND2 1 
ATOM   2145 N  ND2 B ASN A 1 308 ? 17.639 9.395  26.783  0.50 33.17 ? 310  ASN A ND2 1 
ATOM   2146 N  N   . ALA A 1 309 ? 22.894 11.050 28.006  1.00 31.25 ? 311  ALA A N   1 
ATOM   2147 C  CA  . ALA A 1 309 ? 23.884 10.241 28.700  1.00 30.75 ? 311  ALA A CA  1 
ATOM   2148 C  C   . ALA A 1 309 ? 23.464 9.989  30.152  1.00 27.46 ? 311  ALA A C   1 
ATOM   2149 O  O   . ALA A 1 309 ? 22.693 10.752 30.739  1.00 26.45 ? 311  ALA A O   1 
ATOM   2150 C  CB  . ALA A 1 309 ? 25.242 10.905 28.610  1.00 30.43 ? 311  ALA A CB  1 
ATOM   2151 N  N   . SER A 1 310 ? 23.989 8.895  30.728  1.00 26.89 ? 312  SER A N   1 
ATOM   2152 C  CA  . SER A 1 310 ? 23.629 8.475  32.081  1.00 23.58 ? 312  SER A CA  1 
ATOM   2153 C  C   . SER A 1 310 ? 24.842 8.376  33.004  1.00 21.35 ? 312  SER A C   1 
ATOM   2154 O  O   . SER A 1 310 ? 24.695 7.855  34.108  1.00 20.19 ? 312  SER A O   1 
ATOM   2155 C  CB  . SER A 1 310 ? 22.924 7.147  32.051  1.00 24.67 ? 312  SER A CB  1 
ATOM   2156 O  OG  . SER A 1 310 ? 23.713 6.201  31.348  1.00 26.02 ? 312  SER A OG  1 
ATOM   2157 N  N   . THR A 1 311 ? 26.007 8.901  32.588  1.00 19.16 ? 313  THR A N   1 
ATOM   2158 C  CA  . THR A 1 311 ? 27.160 8.979  33.472  1.00 18.17 ? 313  THR A CA  1 
ATOM   2159 C  C   . THR A 1 311 ? 26.904 9.949  34.639  1.00 16.27 ? 313  THR A C   1 
ATOM   2160 O  O   . THR A 1 311 ? 26.108 10.882 34.536  1.00 15.32 ? 313  THR A O   1 
ATOM   2161 C  CB  . THR A 1 311 ? 28.425 9.329  32.693  1.00 18.36 ? 313  THR A CB  1 
ATOM   2162 O  OG1 . THR A 1 311 ? 28.183 10.589 32.053  1.00 17.74 ? 313  THR A OG1 1 
ATOM   2163 C  CG2 . THR A 1 311 ? 28.815 8.253  31.700  1.00 19.60 ? 313  THR A CG2 1 
ATOM   2164 N  N   . THR A 1 312 ? 27.604 9.743  35.755  1.00 15.61 ? 314  THR A N   1 
ATOM   2165 C  CA  . THR A 1 312 ? 27.484 10.629 36.903  1.00 14.88 ? 314  THR A CA  1 
ATOM   2166 C  C   . THR A 1 312 ? 28.868 11.053 37.380  1.00 14.81 ? 314  THR A C   1 
ATOM   2167 O  O   . THR A 1 312 ? 29.883 10.456 37.033  1.00 15.56 ? 314  THR A O   1 
ATOM   2168 C  CB  . THR A 1 312 ? 26.701 9.999  38.073  1.00 14.83 ? 314  THR A CB  1 
ATOM   2169 O  OG1 . THR A 1 312 ? 27.437 8.864  38.526  1.00 14.84 ? 314  THR A OG1 1 
ATOM   2170 C  CG2 . THR A 1 312 ? 25.286 9.604  37.687  1.00 15.01 ? 314  THR A CG2 1 
ATOM   2171 N  N   . ALA A 1 313 ? 28.876 12.126 38.155  1.00 14.29 ? 315  ALA A N   1 
ATOM   2172 C  CA  . ALA A 1 313 ? 30.041 12.522 38.920  1.00 14.74 ? 315  ALA A CA  1 
ATOM   2173 C  C   . ALA A 1 313 ? 29.626 12.808 40.357  1.00 14.37 ? 315  ALA A C   1 
ATOM   2174 O  O   . ALA A 1 313 ? 28.448 12.939 40.656  1.00 13.79 ? 315  ALA A O   1 
ATOM   2175 C  CB  . ALA A 1 313 ? 30.680 13.722 38.266  1.00 14.77 ? 315  ALA A CB  1 
ATOM   2176 N  N   . GLN A 1 314 ? 30.626 12.999 41.211  1.00 15.08 ? 316  GLN A N   1 
ATOM   2177 C  CA  . GLN A 1 314 ? 30.394 13.289 42.611  1.00 15.66 ? 316  GLN A CA  1 
ATOM   2178 C  C   . GLN A 1 314 ? 31.027 14.627 42.964  1.00 14.43 ? 316  GLN A C   1 
ATOM   2179 O  O   . GLN A 1 314 ? 32.141 14.883 42.525  1.00 14.58 ? 316  GLN A O   1 
ATOM   2180 C  CB  . GLN A 1 314 ? 30.996 12.139 43.417  1.00 17.44 ? 316  GLN A CB  1 
ATOM   2181 C  CG  . GLN A 1 314 ? 30.425 11.996 44.802  1.00 19.36 ? 316  GLN A CG  1 
ATOM   2182 C  CD  . GLN A 1 314 ? 31.135 10.865 45.509  1.00 21.73 ? 316  GLN A CD  1 
ATOM   2183 O  OE1 . GLN A 1 314 ? 31.539 10.989 46.665  1.00 24.15 ? 316  GLN A OE1 1 
ATOM   2184 N  NE2 . GLN A 1 314 ? 31.177 9.721  44.853  1.00 23.65 ? 316  GLN A NE2 1 
ATOM   2185 N  N   . THR A 1 315 ? 30.319 15.459 43.755  1.00 13.18 ? 317  THR A N   1 
ATOM   2186 C  CA  . THR A 1 315 ? 30.896 16.681 44.299  1.00 13.32 ? 317  THR A CA  1 
ATOM   2187 C  C   . THR A 1 315 ? 31.968 16.320 45.322  1.00 14.22 ? 317  THR A C   1 
ATOM   2188 O  O   . THR A 1 315 ? 31.965 15.216 45.857  1.00 14.12 ? 317  THR A O   1 
ATOM   2189 C  CB  . THR A 1 315 ? 29.849 17.584 44.982  1.00 12.15 ? 317  THR A CB  1 
ATOM   2190 O  OG1 . THR A 1 315 ? 29.219 16.869 46.040  1.00 11.74 ? 317  THR A OG1 1 
ATOM   2191 C  CG2 . THR A 1 315 ? 28.782 18.104 44.052  1.00 11.62 ? 317  THR A CG2 1 
ATOM   2192 N  N   . LEU A 1 316 ? 32.873 17.257 45.618  1.00 15.40 ? 318  LEU A N   1 
ATOM   2193 C  CA  . LEU A 1 316 ? 33.757 17.104 46.763  1.00 15.88 ? 318  LEU A CA  1 
ATOM   2194 C  C   . LEU A 1 316 ? 32.910 17.109 48.031  1.00 15.47 ? 318  LEU A C   1 
ATOM   2195 O  O   . LEU A 1 316 ? 31.826 17.677 48.044  1.00 15.17 ? 318  LEU A O   1 
ATOM   2196 C  CB  . LEU A 1 316 ? 34.768 18.254 46.802  1.00 16.83 ? 318  LEU A CB  1 
ATOM   2197 C  CG  . LEU A 1 316 ? 35.713 18.357 45.607  1.00 18.60 ? 318  LEU A CG  1 
ATOM   2198 C  CD1 . LEU A 1 316 ? 36.536 19.635 45.691  1.00 19.41 ? 318  LEU A CD1 1 
ATOM   2199 C  CD2 . LEU A 1 316 ? 36.610 17.124 45.527  1.00 19.61 ? 318  LEU A CD2 1 
ATOM   2200 N  N   . ASP A 1 317 ? 33.442 16.531 49.111  1.00 15.73 ? 319  ASP A N   1 
ATOM   2201 C  CA  . ASP A 1 317 ? 32.728 16.491 50.377  1.00 15.25 ? 319  ASP A CA  1 
ATOM   2202 C  C   . ASP A 1 317 ? 32.590 17.884 50.971  1.00 14.11 ? 319  ASP A C   1 
ATOM   2203 O  O   . ASP A 1 317 ? 33.484 18.715 50.854  1.00 14.64 ? 319  ASP A O   1 
ATOM   2204 C  CB  . ASP A 1 317 ? 33.472 15.623 51.387  1.00 17.09 ? 319  ASP A CB  1 
ATOM   2205 C  CG  . ASP A 1 317 ? 33.466 14.149 51.053  1.00 18.68 ? 319  ASP A CG  1 
ATOM   2206 O  OD1 . ASP A 1 317 ? 32.707 13.748 50.162  1.00 20.37 ? 319  ASP A OD1 1 
ATOM   2207 O  OD2 . ASP A 1 317 ? 34.204 13.410 51.720  1.00 20.94 ? 319  ASP A OD2 1 
ATOM   2208 N  N   . SER A 1 318 ? 31.453 18.110 51.626  1.00 12.57 ? 320  SER A N   1 
ATOM   2209 C  CA  . SER A 1 318 ? 31.235 19.256 52.488  1.00 11.87 ? 320  SER A CA  1 
ATOM   2210 C  C   . SER A 1 318 ? 31.108 18.764 53.929  1.00 11.85 ? 320  SER A C   1 
ATOM   2211 O  O   . SER A 1 318 ? 30.276 17.906 54.210  1.00 10.65 ? 320  SER A O   1 
ATOM   2212 C  CB  . SER A 1 318 ? 29.977 19.955 52.071  1.00 11.31 ? 320  SER A CB  1 
ATOM   2213 O  OG  . SER A 1 318 ? 29.762 21.125 52.828  1.00 10.82 ? 320  SER A OG  1 
ATOM   2214 N  N   . ARG A 1 319 ? 31.897 19.334 54.830  1.00 12.71 ? 321  ARG A N   1 
ATOM   2215 C  CA  . ARG A 1 319 ? 31.947 18.848 56.204  1.00 13.68 ? 321  ARG A CA  1 
ATOM   2216 C  C   . ARG A 1 319 ? 31.331 19.851 57.173  1.00 12.29 ? 321  ARG A C   1 
ATOM   2217 O  O   . ARG A 1 319 ? 31.552 21.054 57.069  1.00 12.62 ? 321  ARG A O   1 
ATOM   2218 C  CB  . ARG A 1 319 ? 33.401 18.557 56.577  1.00 16.63 ? 321  ARG A CB  1 
ATOM   2219 C  CG  . ARG A 1 319 ? 33.570 17.786 57.874  1.00 19.62 ? 321  ARG A CG  1 
ATOM   2220 C  CD  . ARG A 1 319 ? 35.021 17.427 58.111  1.00 23.85 ? 321  ARG A CD  1 
ATOM   2221 N  NE  . ARG A 1 319 ? 35.766 18.657 58.326  1.00 29.64 ? 321  ARG A NE  1 
ATOM   2222 C  CZ  . ARG A 1 319 ? 37.090 18.740 58.370  1.00 37.55 ? 321  ARG A CZ  1 
ATOM   2223 N  NH1 . ARG A 1 319 ? 37.813 17.647 58.223  1.00 42.87 ? 321  ARG A NH1 1 
ATOM   2224 N  NH2 . ARG A 1 319 ? 37.686 19.906 58.566  1.00 40.02 ? 321  ARG A NH2 1 
ATOM   2225 N  N   . ALA A 1 320 ? 30.601 19.335 58.171  1.00 11.39 ? 322  ALA A N   1 
ATOM   2226 C  CA  . ALA A 1 320 ? 30.142 20.128 59.302  1.00 10.80 ? 322  ALA A CA  1 
ATOM   2227 C  C   . ALA A 1 320 ? 30.630 19.450 60.576  1.00 10.75 ? 322  ALA A C   1 
ATOM   2228 O  O   . ALA A 1 320 ? 30.789 18.235 60.576  1.00 10.96 ? 322  ALA A O   1 
ATOM   2229 C  CB  . ALA A 1 320 ? 28.634 20.257 59.283  1.00 10.35 ? 322  ALA A CB  1 
ATOM   2230 N  N   . THR A 1 321 ? 30.860 20.240 61.633  1.00 10.88 ? 323  THR A N   1 
ATOM   2231 C  CA  . THR A 1 321 ? 31.431 19.740 62.869  1.00 10.99 ? 323  THR A CA  1 
ATOM   2232 C  C   . THR A 1 321 ? 30.639 20.288 64.057  1.00 10.93 ? 323  THR A C   1 
ATOM   2233 O  O   . THR A 1 321 ? 30.219 21.444 64.072  1.00 10.97 ? 323  THR A O   1 
ATOM   2234 C  CB  . THR A 1 321 ? 32.902 20.151 62.995  1.00 11.58 ? 323  THR A CB  1 
ATOM   2235 O  OG1 . THR A 1 321 ? 33.623 19.621 61.887  1.00 11.60 ? 323  THR A OG1 1 
ATOM   2236 C  CG2 . THR A 1 321 ? 33.548 19.649 64.267  1.00 12.07 ? 323  THR A CG2 1 
ATOM   2237 N  N   . VAL A 1 322 ? 30.464 19.448 65.081  1.00 10.89 ? 324  VAL A N   1 
ATOM   2238 C  CA  . VAL A 1 322 ? 29.869 19.872 66.329  1.00 11.15 ? 324  VAL A CA  1 
ATOM   2239 C  C   . VAL A 1 322 ? 30.826 19.527 67.467  1.00 11.51 ? 324  VAL A C   1 
ATOM   2240 O  O   . VAL A 1 322 ? 31.295 18.398 67.573  1.00 11.51 ? 324  VAL A O   1 
ATOM   2241 C  CB  . VAL A 1 322 ? 28.494 19.215 66.528  1.00 11.27 ? 324  VAL A CB  1 
ATOM   2242 C  CG1 . VAL A 1 322 ? 27.894 19.504 67.899  1.00 11.51 ? 324  VAL A CG1 1 
ATOM   2243 C  CG2 . VAL A 1 322 ? 27.538 19.629 65.417  1.00 11.31 ? 324  VAL A CG2 1 
ATOM   2244 N  N   . TYR A 1 323 ? 31.100 20.529 68.303  1.00 11.81 ? 325  TYR A N   1 
ATOM   2245 C  CA  . TYR A 1 323 ? 31.984 20.382 69.443  1.00 12.19 ? 325  TYR A CA  1 
ATOM   2246 C  C   . TYR A 1 323 ? 31.134 20.281 70.690  1.00 12.13 ? 325  TYR A C   1 
ATOM   2247 O  O   . TYR A 1 323 ? 30.021 20.787 70.740  1.00 11.71 ? 325  TYR A O   1 
ATOM   2248 C  CB  . TYR A 1 323 ? 32.947 21.567 69.520  1.00 12.63 ? 325  TYR A CB  1 
ATOM   2249 C  CG  . TYR A 1 323 ? 33.796 21.745 68.274  1.00 12.71 ? 325  TYR A CG  1 
ATOM   2250 C  CD1 . TYR A 1 323 ? 34.857 20.892 68.012  1.00 12.96 ? 325  TYR A CD1 1 
ATOM   2251 C  CD2 . TYR A 1 323 ? 33.529 22.759 67.347  1.00 12.69 ? 325  TYR A CD2 1 
ATOM   2252 C  CE1 . TYR A 1 323 ? 35.638 21.052 66.878  1.00 13.16 ? 325  TYR A CE1 1 
ATOM   2253 C  CE2 . TYR A 1 323 ? 34.305 22.930 66.210  1.00 12.84 ? 325  TYR A CE2 1 
ATOM   2254 C  CZ  . TYR A 1 323 ? 35.355 22.062 65.973  1.00 13.08 ? 325  TYR A CZ  1 
ATOM   2255 O  OH  . TYR A 1 323 ? 36.115 22.232 64.858  1.00 13.57 ? 325  TYR A OH  1 
ATOM   2256 N  N   . THR A 1 324 ? 31.674 19.591 71.691  1.00 12.59 ? 326  THR A N   1 
ATOM   2257 C  CA  . THR A 1 324 ? 31.043 19.553 72.989  1.00 12.96 ? 326  THR A CA  1 
ATOM   2258 C  C   . THR A 1 324 ? 32.124 19.295 74.032  1.00 13.78 ? 326  THR A C   1 
ATOM   2259 O  O   . THR A 1 324 ? 33.235 18.914 73.677  1.00 13.26 ? 326  THR A O   1 
ATOM   2260 C  CB  . THR A 1 324 ? 29.918 18.513 72.998  1.00 12.69 ? 326  THR A CB  1 
ATOM   2261 O  OG1 . THR A 1 324 ? 29.045 18.839 74.076  1.00 13.12 ? 326  THR A OG1 1 
ATOM   2262 C  CG2 . THR A 1 324 ? 30.441 17.102 73.147  1.00 12.89 ? 326  THR A CG2 1 
ATOM   2263 N  N   . TYR A 1 325 ? 31.781 19.580 75.294  1.00 11.87 ? 327  TYR A N   1 
ATOM   2264 C  CA  . TYR A 1 325 ? 32.698 19.427 76.407  1.00 12.22 ? 327  TYR A CA  1 
ATOM   2265 C  C   . TYR A 1 325 ? 32.087 18.531 77.478  1.00 12.01 ? 327  TYR A C   1 
ATOM   2266 O  O   . TYR A 1 325 ? 30.901 18.244 77.450  1.00 11.35 ? 327  TYR A O   1 
ATOM   2267 C  CB  . TYR A 1 325 ? 33.020 20.801 77.005  1.00 12.50 ? 327  TYR A CB  1 
ATOM   2268 C  CG  . TYR A 1 325 ? 33.369 21.816 75.934  1.00 14.03 ? 327  TYR A CG  1 
ATOM   2269 C  CD1 . TYR A 1 325 ? 34.469 21.627 75.114  1.00 15.44 ? 327  TYR A CD1 1 
ATOM   2270 C  CD2 . TYR A 1 325 ? 32.592 22.951 75.739  1.00 14.85 ? 327  TYR A CD2 1 
ATOM   2271 C  CE1 . TYR A 1 325 ? 34.788 22.537 74.123  1.00 16.77 ? 327  TYR A CE1 1 
ATOM   2272 C  CE2 . TYR A 1 325 ? 32.892 23.871 74.745  1.00 16.09 ? 327  TYR A CE2 1 
ATOM   2273 C  CZ  . TYR A 1 325 ? 33.998 23.659 73.940  1.00 17.35 ? 327  TYR A CZ  1 
ATOM   2274 O  OH  . TYR A 1 325 ? 34.322 24.548 72.966  1.00 19.28 ? 327  TYR A OH  1 
ATOM   2275 N  N   . ARG A 1 326 ? 32.930 18.134 78.446  1.00 12.52 ? 328  ARG A N   1 
ATOM   2276 C  CA  . ARG A 1 326 ? 32.485 17.487 79.665  1.00 12.69 ? 328  ARG A CA  1 
ATOM   2277 C  C   . ARG A 1 326 ? 32.842 18.379 80.850  1.00 11.87 ? 328  ARG A C   1 
ATOM   2278 O  O   . ARG A 1 326 ? 33.998 18.704 81.015  1.00 12.06 ? 328  ARG A O   1 
ATOM   2279 C  CB  . ARG A 1 326 ? 33.159 16.125 79.849  1.00 14.17 ? 328  ARG A CB  1 
ATOM   2280 C  CG  . ARG A 1 326 ? 32.750 15.414 81.132  1.00 15.59 ? 328  ARG A CG  1 
ATOM   2281 C  CD  . ARG A 1 326 ? 33.723 14.352 81.569  1.00 18.22 ? 328  ARG A CD  1 
ATOM   2282 N  NE  . ARG A 1 326 ? 34.962 14.937 82.046  1.00 20.41 ? 328  ARG A NE  1 
ATOM   2283 C  CZ  . ARG A 1 326 ? 36.067 14.232 82.313  1.00 24.90 ? 328  ARG A CZ  1 
ATOM   2284 N  NH1 . ARG A 1 326 ? 36.077 12.914 82.137  1.00 27.24 ? 328  ARG A NH1 1 
ATOM   2285 N  NH2 . ARG A 1 326 ? 37.150 14.854 82.757  1.00 25.52 ? 328  ARG A NH2 1 
ATOM   2286 N  N   . LEU A 1 327 ? 31.846 18.748 81.665  1.00 11.43 ? 329  LEU A N   1 
ATOM   2287 C  CA  . LEU A 1 327 ? 32.063 19.380 82.959  1.00 10.83 ? 329  LEU A CA  1 
ATOM   2288 C  C   . LEU A 1 327 ? 32.100 18.311 84.050  1.00 10.59 ? 329  LEU A C   1 
ATOM   2289 O  O   . LEU A 1 327 ? 31.129 17.585 84.254  1.00 10.40 ? 329  LEU A O   1 
ATOM   2290 C  CB  . LEU A 1 327 ? 30.955 20.408 83.235  1.00 11.00 ? 329  LEU A CB  1 
ATOM   2291 C  CG  . LEU A 1 327 ? 30.879 20.962 84.656  1.00 11.08 ? 329  LEU A CG  1 
ATOM   2292 C  CD1 . LEU A 1 327 ? 32.106 21.805 84.987  1.00 11.22 ? 329  LEU A CD1 1 
ATOM   2293 C  CD2 . LEU A 1 327 ? 29.600 21.777 84.827  1.00 11.43 ? 329  LEU A CD2 1 
ATOM   2294 N  N   . ARG A 1 328 ? 33.234 18.219 84.738  1.00 10.67 ? 330  ARG A N   1 
ATOM   2295 C  CA  . ARG A 1 328 ? 33.381 17.280 85.839  1.00 11.19 ? 330  ARG A CA  1 
ATOM   2296 C  C   . ARG A 1 328 ? 33.467 18.035 87.162  1.00 10.58 ? 330  ARG A C   1 
ATOM   2297 O  O   . ARG A 1 328 ? 34.238 18.981 87.262  1.00 10.18 ? 330  ARG A O   1 
ATOM   2298 C  CB  . ARG A 1 328 ? 34.639 16.431 85.644  1.00 12.17 ? 330  ARG A CB  1 
ATOM   2299 C  CG  . ARG A 1 328 ? 35.037 15.658 86.897  1.00 13.42 ? 330  ARG A CG  1 
ATOM   2300 C  CD  . ARG A 1 328 ? 36.046 14.575 86.582  1.00 14.75 ? 330  ARG A CD  1 
ATOM   2301 N  NE  . ARG A 1 328 ? 35.403 13.438 85.956  1.00 16.50 ? 330  ARG A NE  1 
ATOM   2302 C  CZ  . ARG A 1 328 ? 35.968 12.248 85.830  1.00 18.16 ? 330  ARG A CZ  1 
ATOM   2303 N  NH1 . ARG A 1 328 ? 37.188 12.048 86.294  1.00 20.09 ? 330  ARG A NH1 1 
ATOM   2304 N  NH2 . ARG A 1 328 ? 35.279 11.242 85.337  1.00 18.63 ? 330  ARG A NH2 1 
ATOM   2305 N  N   . LEU A 1 329 ? 32.712 17.584 88.174  1.00 10.32 ? 331  LEU A N   1 
ATOM   2306 C  CA  . LEU A 1 329 ? 32.886 18.085 89.532  1.00 10.49 ? 331  LEU A CA  1 
ATOM   2307 C  C   . LEU A 1 329 ? 33.510 16.969 90.367  1.00 10.34 ? 331  LEU A C   1 
ATOM   2308 O  O   . LEU A 1 329 ? 33.120 15.816 90.236  1.00 10.56 ? 331  LEU A O   1 
ATOM   2309 C  CB  . LEU A 1 329 ? 31.531 18.453 90.145  1.00 10.93 ? 331  LEU A CB  1 
ATOM   2310 C  CG  . LEU A 1 329 ? 30.567 19.223 89.255  1.00 11.66 ? 331  LEU A CG  1 
ATOM   2311 C  CD1 . LEU A 1 329 ? 29.296 19.566 90.010  1.00 12.16 ? 331  LEU A CD1 1 
ATOM   2312 C  CD2 . LEU A 1 329 ? 31.223 20.492 88.724  1.00 12.00 ? 331  LEU A CD2 1 
ATOM   2313 N  N   . THR A 1 330 ? 34.470 17.321 91.217  1.00 10.10 ? 332  THR A N   1 
ATOM   2314 C  CA  . THR A 1 330 ? 35.084 16.380 92.135  1.00 10.38 ? 332  THR A CA  1 
ATOM   2315 C  C   . THR A 1 330 ? 34.842 16.902 93.549  1.00 10.04 ? 332  THR A C   1 
ATOM   2316 O  O   . THR A 1 330 ? 35.333 17.973 93.901  1.00 9.78  ? 332  THR A O   1 
ATOM   2317 C  CB  . THR A 1 330 ? 36.582 16.240 91.846  1.00 11.30 ? 332  THR A CB  1 
ATOM   2318 O  OG1 . THR A 1 330 ? 36.720 15.684 90.536  1.00 11.38 ? 332  THR A OG1 1 
ATOM   2319 C  CG2 . THR A 1 330 ? 37.289 15.353 92.851  1.00 12.18 ? 332  THR A CG2 1 
ATOM   2320 N  N   . LYS A 1 331 ? 34.059 16.149 94.329  1.00 9.79  ? 333  LYS A N   1 
ATOM   2321 C  CA  . LYS A 1 331 ? 33.623 16.610 95.641  1.00 9.85  ? 333  LYS A CA  1 
ATOM   2322 C  C   . LYS A 1 331 ? 34.629 16.160 96.692  1.00 9.82  ? 333  LYS A C   1 
ATOM   2323 O  O   . LYS A 1 331 ? 34.884 14.957 96.820  1.00 9.77  ? 333  LYS A O   1 
ATOM   2324 C  CB  . LYS A 1 331 ? 32.233 16.074 96.001  1.00 10.16 ? 333  LYS A CB  1 
ATOM   2325 C  CG  . LYS A 1 331 ? 31.618 16.699 97.230  1.00 10.60 ? 333  LYS A CG  1 
ATOM   2326 C  CD  . LYS A 1 331 ? 31.212 18.145 97.079  1.00 11.06 ? 333  LYS A CD  1 
ATOM   2327 C  CE  . LYS A 1 331 ? 30.643 18.697 98.365  1.00 12.07 ? 333  LYS A CE  1 
ATOM   2328 N  NZ  . LYS A 1 331 ? 31.684 18.824 99.400  1.00 12.77 ? 333  LYS A NZ  1 
ATOM   2329 N  N   . VAL A 1 332 ? 35.235 17.137 97.373  1.00 9.83  ? 334  VAL A N   1 
ATOM   2330 C  CA  . VAL A 1 332 ? 36.281 16.843 98.335  1.00 10.43 ? 334  VAL A CA  1 
ATOM   2331 C  C   . VAL A 1 332 ? 35.949 17.579 99.632  1.00 10.52 ? 334  VAL A C   1 
ATOM   2332 O  O   . VAL A 1 332 ? 34.986 18.347 99.671  1.00 10.14 ? 334  VAL A O   1 
ATOM   2333 C  CB  . VAL A 1 332 ? 37.688 17.208 97.810  1.00 11.01 ? 334  VAL A CB  1 
ATOM   2334 C  CG1 . VAL A 1 332 ? 38.018 16.470 96.512  1.00 11.12 ? 334  VAL A CG1 1 
ATOM   2335 C  CG2 . VAL A 1 332 ? 37.878 18.701 97.638  1.00 11.25 ? 334  VAL A CG2 1 
ATOM   2336 N  N   . ASN A 1 333 ? 36.782 17.383 100.662 1.00 11.12 ? 335  ASN A N   1 
ATOM   2337 C  CA  . ASN A 1 333 ? 36.700 18.228 101.846 1.00 11.48 ? 335  ASN A CA  1 
ATOM   2338 C  C   . ASN A 1 333 ? 38.055 18.910 102.072 1.00 12.61 ? 335  ASN A C   1 
ATOM   2339 O  O   . ASN A 1 333 ? 38.961 18.759 101.264 1.00 12.61 ? 335  ASN A O   1 
ATOM   2340 C  CB  . ASN A 1 333 ? 36.160 17.449 103.040 1.00 11.61 ? 335  ASN A CB  1 
ATOM   2341 C  CG  . ASN A 1 333 ? 37.028 16.285 103.457 1.00 12.04 ? 335  ASN A CG  1 
ATOM   2342 O  OD1 . ASN A 1 333 ? 38.150 16.106 103.009 1.00 12.59 ? 335  ASN A OD1 1 
ATOM   2343 N  ND2 . ASN A 1 333 ? 36.482 15.452 104.311 1.00 12.51 ? 335  ASN A ND2 1 
ATOM   2344 N  N   . GLU A 1 334 ? 38.216 19.619 103.211 1.00 13.65 ? 336  GLU A N   1 
ATOM   2345 C  CA  . GLU A 1 334 ? 39.457 20.331 103.511 1.00 15.33 ? 336  GLU A CA  1 
ATOM   2346 C  C   . GLU A 1 334 ? 40.565 19.359 103.915 1.00 15.85 ? 336  GLU A C   1 
ATOM   2347 O  O   . GLU A 1 334 ? 41.743 19.706 103.874 1.00 17.13 ? 336  GLU A O   1 
ATOM   2348 C  CB  . GLU A 1 334 ? 39.236 21.365 104.624 1.00 16.66 ? 336  GLU A CB  1 
ATOM   2349 C  CG  . GLU A 1 334 ? 38.312 22.464 104.153 1.00 17.55 ? 336  GLU A CG  1 
ATOM   2350 C  CD  . GLU A 1 334 ? 38.142 23.635 105.103 1.00 19.63 ? 336  GLU A CD  1 
ATOM   2351 O  OE1 . GLU A 1 334 ? 37.643 23.438 106.232 1.00 20.66 ? 336  GLU A OE1 1 
ATOM   2352 O  OE2 . GLU A 1 334 ? 38.497 24.730 104.687 1.00 22.09 ? 336  GLU A OE2 1 
ATOM   2353 N  N   . ARG A 1 335 ? 40.182 18.139 104.292 1.00 15.16 ? 337  ARG A N   1 
ATOM   2354 C  CA  . ARG A 1 335 ? 41.155 17.100 104.585 1.00 16.33 ? 337  ARG A CA  1 
ATOM   2355 C  C   . ARG A 1 335 ? 41.623 16.430 103.290 1.00 16.38 ? 337  ARG A C   1 
ATOM   2356 O  O   . ARG A 1 335 ? 42.397 15.501 103.331 1.00 16.71 ? 337  ARG A O   1 
ATOM   2357 C  CB  . ARG A 1 335 ? 40.525 16.100 105.554 1.00 16.03 ? 337  ARG A CB  1 
ATOM   2358 C  CG  . ARG A 1 335 ? 40.250 16.660 106.951 1.00 16.49 ? 337  ARG A CG  1 
ATOM   2359 C  CD  . ARG A 1 335 ? 39.226 15.810 107.695 1.00 16.22 ? 337  ARG A CD  1 
ATOM   2360 N  NE  . ARG A 1 335 ? 39.716 14.433 107.856 1.00 16.87 ? 337  ARG A NE  1 
ATOM   2361 C  CZ  . ARG A 1 335 ? 40.650 14.082 108.719 1.00 18.23 ? 337  ARG A CZ  1 
ATOM   2362 N  NH1 . ARG A 1 335 ? 40.990 14.942 109.656 1.00 18.60 ? 337  ARG A NH1 1 
ATOM   2363 N  NH2 . ARG A 1 335 ? 41.209 12.879 108.656 1.00 19.21 ? 337  ARG A NH2 1 
ATOM   2364 N  N   . GLN A 1 336 ? 41.182 16.945 102.140 1.00 16.68 ? 338  GLN A N   1 
ATOM   2365 C  CA  . GLN A 1 336 ? 41.531 16.380 100.844 1.00 17.68 ? 338  GLN A CA  1 
ATOM   2366 C  C   . GLN A 1 336 ? 41.028 14.940 100.733 1.00 17.08 ? 338  GLN A C   1 
ATOM   2367 O  O   . GLN A 1 336 ? 41.624 14.112 100.043 1.00 17.70 ? 338  GLN A O   1 
ATOM   2368 C  CB  . GLN A 1 336 ? 43.040 16.440 100.601 1.00 20.43 ? 338  GLN A CB  1 
ATOM   2369 C  CG  . GLN A 1 336 ? 43.637 17.837 100.686 1.00 22.38 ? 338  GLN A CG  1 
ATOM   2370 C  CD  . GLN A 1 336 ? 44.872 17.930 99.828  1.00 25.25 ? 338  GLN A CD  1 
ATOM   2371 O  OE1 . GLN A 1 336 ? 46.000 17.814 100.298 1.00 28.31 ? 338  GLN A OE1 1 
ATOM   2372 N  NE2 . GLN A 1 336 ? 44.663 18.075 98.532  1.00 26.87 ? 338  GLN A NE2 1 
ATOM   2373 N  N   . GLU A 1 337 ? 39.888 14.667 101.363 1.00 16.14 ? 339  GLU A N   1 
ATOM   2374 C  CA  . GLU A 1 337 ? 39.234 13.381 101.230 1.00 16.21 ? 339  GLU A CA  1 
ATOM   2375 C  C   . GLU A 1 337 ? 38.123 13.501 100.192 1.00 15.38 ? 339  GLU A C   1 
ATOM   2376 O  O   . GLU A 1 337 ? 37.540 14.568 99.991  1.00 14.45 ? 339  GLU A O   1 
ATOM   2377 C  CB  . GLU A 1 337 ? 38.717 12.917 102.588 1.00 16.93 ? 339  GLU A CB  1 
ATOM   2378 C  CG  . GLU A 1 337 ? 39.830 12.675 103.601 1.00 18.29 ? 339  GLU A CG  1 
ATOM   2379 C  CD  . GLU A 1 337 ? 39.379 12.389 105.027 1.00 19.90 ? 339  GLU A CD  1 
ATOM   2380 O  OE1 . GLU A 1 337 ? 38.162 12.569 105.309 1.00 19.66 ? 339  GLU A OE1 1 
ATOM   2381 O  OE2 . GLU A 1 337 ? 40.257 11.998 105.894 1.00 20.81 ? 339  GLU A OE2 1 
ATOM   2382 N  N   . ARG A 1 338 ? 37.806 12.388 99.534  1.00 15.12 ? 340  ARG A N   1 
ATOM   2383 C  CA  . ARG A 1 338 ? 36.672 12.388 98.624  1.00 14.72 ? 340  ARG A CA  1 
ATOM   2384 C  C   . ARG A 1 338 ? 35.388 12.193 99.422  1.00 13.95 ? 340  ARG A C   1 
ATOM   2385 O  O   . ARG A 1 338 ? 35.375 11.445 100.400 1.00 14.03 ? 340  ARG A O   1 
ATOM   2386 C  CB  . ARG A 1 338 ? 36.872 11.333 97.544  1.00 15.89 ? 340  ARG A CB  1 
ATOM   2387 C  CG  . ARG A 1 338 ? 38.062 11.629 96.652  1.00 17.12 ? 340  ARG A CG  1 
ATOM   2388 C  CD  . ARG A 1 338 ? 38.352 10.435 95.788  1.00 19.48 ? 340  ARG A CD  1 
ATOM   2389 N  NE  . ARG A 1 338 ? 39.295 10.746 94.747  1.00 21.40 ? 340  ARG A NE  1 
ATOM   2390 C  CZ  . ARG A 1 338 ? 38.960 11.277 93.591  1.00 22.98 ? 340  ARG A CZ  1 
ATOM   2391 N  NH1 . ARG A 1 338 ? 37.698 11.587 93.342  1.00 23.31 ? 340  ARG A NH1 1 
ATOM   2392 N  NH2 . ARG A 1 338 ? 39.900 11.463 92.682  1.00 24.22 ? 340  ARG A NH2 1 
ATOM   2393 N  N   . VAL A 1 339 ? 34.343 12.944 99.049  1.00 12.71 ? 341  VAL A N   1 
ATOM   2394 C  CA  . VAL A 1 339 ? 33.095 12.998 99.793  1.00 12.54 ? 341  VAL A CA  1 
ATOM   2395 C  C   . VAL A 1 339 ? 31.958 12.556 98.882  1.00 12.38 ? 341  VAL A C   1 
ATOM   2396 O  O   . VAL A 1 339 ? 31.757 13.146 97.820  1.00 11.45 ? 341  VAL A O   1 
ATOM   2397 C  CB  . VAL A 1 339 ? 32.851 14.412 100.340 1.00 12.25 ? 341  VAL A CB  1 
ATOM   2398 C  CG1 . VAL A 1 339 ? 31.535 14.517 101.097 1.00 12.49 ? 341  VAL A CG1 1 
ATOM   2399 C  CG2 . VAL A 1 339 ? 34.011 14.860 101.221 1.00 12.37 ? 341  VAL A CG2 1 
ATOM   2400 N  N   . ALA A 1 340 ? 31.220 11.537 99.351  1.00 12.84 ? 342  ALA A N   1 
ATOM   2401 C  CA  . ALA A 1 340 ? 30.032 11.033 98.687  1.00 12.88 ? 342  ALA A CA  1 
ATOM   2402 C  C   . ALA A 1 340 ? 28.787 11.747 99.208  1.00 13.28 ? 342  ALA A C   1 
ATOM   2403 O  O   . ALA A 1 340 ? 28.802 12.346 100.281 1.00 13.70 ? 342  ALA A O   1 
ATOM   2404 C  CB  . ALA A 1 340 ? 29.944 9.540  98.902  1.00 13.72 ? 342  ALA A CB  1 
ATOM   2405 N  N   . GLY A 1 341 ? 27.698 11.649 98.452  1.00 13.59 ? 343  GLY A N   1 
ATOM   2406 C  CA  . GLY A 1 341 ? 26.386 12.056 98.925  1.00 14.33 ? 343  GLY A CA  1 
ATOM   2407 C  C   . GLY A 1 341 ? 25.989 13.477 98.552  1.00 13.94 ? 343  GLY A C   1 
ATOM   2408 O  O   . GLY A 1 341 ? 24.969 13.945 99.035  1.00 14.95 ? 343  GLY A O   1 
ATOM   2409 N  N   . ALA A 1 342 ? 26.805 14.155 97.729  1.00 13.00 ? 344  ALA A N   1 
ATOM   2410 C  CA  . ALA A 1 342 ? 26.440 15.436 97.170  1.00 13.23 ? 344  ALA A CA  1 
ATOM   2411 C  C   . ALA A 1 342 ? 25.557 15.205 95.953  1.00 13.54 ? 344  ALA A C   1 
ATOM   2412 O  O   . ALA A 1 342 ? 25.629 14.157 95.316  1.00 13.78 ? 344  ALA A O   1 
ATOM   2413 C  CB  . ALA A 1 342 ? 27.667 16.224 96.783  1.00 12.58 ? 344  ALA A CB  1 
ATOM   2414 N  N   . GLY A 1 343 ? 24.691 16.185 95.689  1.00 13.96 ? 345  GLY A N   1 
ATOM   2415 C  CA  . GLY A 1 343 ? 23.871 16.205 94.487  1.00 14.51 ? 345  GLY A CA  1 
ATOM   2416 C  C   . GLY A 1 343 ? 23.873 17.594 93.870  1.00 14.42 ? 345  GLY A C   1 
ATOM   2417 O  O   . GLY A 1 343 ? 23.817 18.582 94.594  1.00 14.52 ? 345  GLY A O   1 
ATOM   2418 N  N   . PHE A 1 344 ? 23.950 17.651 92.533  1.00 14.27 ? 346  PHE A N   1 
ATOM   2419 C  CA  . PHE A 1 344 ? 24.088 18.916 91.836  1.00 14.14 ? 346  PHE A CA  1 
ATOM   2420 C  C   . PHE A 1 344 ? 23.000 19.080 90.778  1.00 15.16 ? 346  PHE A C   1 
ATOM   2421 O  O   . PHE A 1 344 ? 22.629 18.121 90.097  1.00 15.74 ? 346  PHE A O   1 
ATOM   2422 C  CB  . PHE A 1 344 ? 25.484 19.007 91.239  1.00 13.26 ? 346  PHE A CB  1 
ATOM   2423 C  CG  . PHE A 1 344 ? 26.548 19.244 92.273  1.00 13.20 ? 346  PHE A CG  1 
ATOM   2424 C  CD1 . PHE A 1 344 ? 26.705 20.498 92.849  1.00 13.81 ? 346  PHE A CD1 1 
ATOM   2425 C  CD2 . PHE A 1 344 ? 27.367 18.210 92.701  1.00 12.82 ? 346  PHE A CD2 1 
ATOM   2426 C  CE1 . PHE A 1 344 ? 27.662 20.711 93.830  1.00 13.43 ? 346  PHE A CE1 1 
ATOM   2427 C  CE2 . PHE A 1 344 ? 28.319 18.429 93.681  1.00 12.45 ? 346  PHE A CE2 1 
ATOM   2428 C  CZ  . PHE A 1 344 ? 28.463 19.674 94.245  1.00 12.92 ? 346  PHE A CZ  1 
ATOM   2429 N  N   . THR A 1 345 ? 22.487 20.312 90.657  1.00 15.54 ? 347  THR A N   1 
ATOM   2430 C  CA  . THR A 1 345 ? 21.526 20.665 89.618  1.00 16.37 ? 347  THR A CA  1 
ATOM   2431 C  C   . THR A 1 345 ? 22.163 21.746 88.745  1.00 15.82 ? 347  THR A C   1 
ATOM   2432 O  O   . THR A 1 345 ? 22.546 22.784 89.245  1.00 15.57 ? 347  THR A O   1 
ATOM   2433 C  CB  . THR A 1 345 ? 20.173 21.105 90.212  1.00 17.88 ? 347  THR A CB  1 
ATOM   2434 O  OG1 . THR A 1 345 ? 19.648 20.079 91.060  1.00 18.43 ? 347  THR A OG1 1 
ATOM   2435 C  CG2 . THR A 1 345 ? 19.135 21.409 89.156  1.00 19.18 ? 347  THR A CG2 1 
ATOM   2436 N  N   . LEU A 1 346 ? 22.300 21.485 87.446  1.00 15.79 ? 348  LEU A N   1 
ATOM   2437 C  CA  . LEU A 1 346 ? 22.862 22.442 86.510  1.00 15.72 ? 348  LEU A CA  1 
ATOM   2438 C  C   . LEU A 1 346 ? 21.736 23.225 85.830  1.00 17.38 ? 348  LEU A C   1 
ATOM   2439 O  O   . LEU A 1 346 ? 20.789 22.645 85.307  1.00 17.78 ? 348  LEU A O   1 
ATOM   2440 C  CB  . LEU A 1 346 ? 23.714 21.707 85.469  1.00 15.27 ? 348  LEU A CB  1 
ATOM   2441 C  CG  . LEU A 1 346 ? 24.442 22.605 84.466  1.00 15.11 ? 348  LEU A CG  1 
ATOM   2442 C  CD1 . LEU A 1 346 ? 25.573 23.389 85.118  1.00 14.65 ? 348  LEU A CD1 1 
ATOM   2443 C  CD2 . LEU A 1 346 ? 24.966 21.788 83.301  1.00 15.05 ? 348  LEU A CD2 1 
ATOM   2444 N  N   . TYR A 1 347 ? 21.867 24.552 85.859  1.00 17.92 ? 349  TYR A N   1 
ATOM   2445 C  CA  . TYR A 1 347 ? 20.956 25.481 85.221  1.00 19.69 ? 349  TYR A CA  1 
ATOM   2446 C  C   . TYR A 1 347 ? 21.715 26.193 84.108  1.00 20.05 ? 349  TYR A C   1 
ATOM   2447 O  O   . TYR A 1 347 ? 22.910 26.438 84.223  1.00 18.76 ? 349  TYR A O   1 
ATOM   2448 C  CB  . TYR A 1 347 ? 20.443 26.502 86.246  1.00 21.00 ? 349  TYR A CB  1 
ATOM   2449 C  CG  . TYR A 1 347 ? 19.526 25.943 87.325  1.00 21.46 ? 349  TYR A CG  1 
ATOM   2450 C  CD1 . TYR A 1 347 ? 18.156 25.873 87.139  1.00 23.08 ? 349  TYR A CD1 1 
ATOM   2451 C  CD2 . TYR A 1 347 ? 20.041 25.447 88.512  1.00 20.63 ? 349  TYR A CD2 1 
ATOM   2452 C  CE1 . TYR A 1 347 ? 17.324 25.343 88.106  1.00 23.99 ? 349  TYR A CE1 1 
ATOM   2453 C  CE2 . TYR A 1 347 ? 19.219 24.921 89.493  1.00 21.35 ? 349  TYR A CE2 1 
ATOM   2454 C  CZ  . TYR A 1 347 ? 17.854 24.882 89.291  1.00 22.98 ? 349  TYR A CZ  1 
ATOM   2455 O  OH  . TYR A 1 347 ? 17.025 24.353 90.234  1.00 23.93 ? 349  TYR A OH  1 
ATOM   2456 N  N   . LYS A 1 348 ? 21.004 26.536 83.036  1.00 22.41 ? 350  LYS A N   1 
ATOM   2457 C  CA  . LYS A 1 348 ? 21.546 27.403 82.007  1.00 23.95 ? 350  LYS A CA  1 
ATOM   2458 C  C   . LYS A 1 348 ? 20.659 28.636 81.929  1.00 27.62 ? 350  LYS A C   1 
ATOM   2459 O  O   . LYS A 1 348 ? 19.448 28.547 82.122  1.00 28.93 ? 350  LYS A O   1 
ATOM   2460 C  CB  . LYS A 1 348 ? 21.616 26.681 80.656  1.00 23.65 ? 350  LYS A CB  1 
ATOM   2461 C  CG  . LYS A 1 348 ? 22.365 27.419 79.544  1.00 23.75 ? 350  LYS A CG  1 
ATOM   2462 C  CD  . LYS A 1 348 ? 22.417 26.634 78.238  1.00 23.38 ? 350  LYS A CD  1 
ATOM   2463 C  CE  . LYS A 1 348 ? 23.443 27.139 77.245  1.00 22.84 ? 350  LYS A CE  1 
ATOM   2464 N  NZ  . LYS A 1 348 ? 22.893 28.254 76.445  1.00 25.29 ? 350  LYS A NZ  1 
ATOM   2465 N  N   . LYS A 1 349 ? 21.284 29.775 81.632  1.00 30.86 ? 351  LYS A N   1 
ATOM   2466 C  CA  . LYS A 1 349 ? 20.577 31.042 81.635  1.00 37.10 ? 351  LYS A CA  1 
ATOM   2467 C  C   . LYS A 1 349 ? 19.909 31.254 80.283  1.00 38.52 ? 351  LYS A C   1 
ATOM   2468 O  O   . LYS A 1 349 ? 20.584 31.322 79.259  1.00 36.76 ? 351  LYS A O   1 
ATOM   2469 C  CB  . LYS A 1 349 ? 21.525 32.200 81.965  1.00 40.68 ? 351  LYS A CB  1 
ATOM   2470 C  CG  . LYS A 1 349 ? 20.817 33.433 82.510  1.00 45.04 ? 351  LYS A CG  1 
ATOM   2471 C  CD  . LYS A 1 349 ? 21.743 34.519 83.000  1.00 48.98 ? 351  LYS A CD  1 
ATOM   2472 C  CE  . LYS A 1 349 ? 22.513 35.196 81.888  1.00 51.74 ? 351  LYS A CE  1 
ATOM   2473 N  NZ  . LYS A 1 349 ? 23.297 36.338 82.416  1.00 54.81 ? 351  LYS A NZ  1 
ATOM   2474 N  N   . ILE A 1 350 ? 18.573 31.303 80.312  1.00 43.24 ? 352  ILE A N   1 
ATOM   2475 C  CA  . ILE A 1 350 ? 17.772 31.852 79.224  1.00 47.52 ? 352  ILE A CA  1 
ATOM   2476 C  C   . ILE A 1 350 ? 17.195 33.183 79.702  1.00 50.41 ? 352  ILE A C   1 
ATOM   2477 O  O   . ILE A 1 350 ? 16.340 33.196 80.590  1.00 51.85 ? 352  ILE A O   1 
ATOM   2478 C  CB  . ILE A 1 350 ? 16.663 30.864 78.802  1.00 48.19 ? 352  ILE A CB  1 
ATOM   2479 C  CG1 . ILE A 1 350 ? 17.235 29.651 78.050  1.00 45.85 ? 352  ILE A CG1 1 
ATOM   2480 C  CG2 . ILE A 1 350 ? 15.579 31.578 78.002  1.00 50.39 ? 352  ILE A CG2 1 
ATOM   2481 C  CD1 . ILE A 1 350 ? 17.764 28.550 78.937  1.00 43.46 ? 352  ILE A CD1 1 
ATOM   2482 N  N   . ASN A 1 351 ? 17.679 34.290 79.117  1.00 51.79 ? 353  ASN A N   1 
ATOM   2483 C  CA  . ASN A 1 351 ? 17.254 35.634 79.497  1.00 54.41 ? 353  ASN A CA  1 
ATOM   2484 C  C   . ASN A 1 351 ? 17.803 35.952 80.891  1.00 55.21 ? 353  ASN A C   1 
ATOM   2485 O  O   . ASN A 1 351 ? 19.011 35.859 81.110  1.00 51.73 ? 353  ASN A O   1 
ATOM   2486 C  CB  . ASN A 1 351 ? 15.732 35.804 79.384  1.00 56.04 ? 353  ASN A CB  1 
ATOM   2487 C  CG  . ASN A 1 351 ? 15.199 35.497 77.998  1.00 55.57 ? 353  ASN A CG  1 
ATOM   2488 O  OD1 . ASN A 1 351 ? 15.948 35.083 77.115  1.00 54.81 ? 353  ASN A OD1 1 
ATOM   2489 N  ND2 . ASN A 1 351 ? 13.905 35.693 77.797  1.00 55.86 ? 353  ASN A ND2 1 
ATOM   2490 N  N   . ASN A 1 352 ? 16.913 36.341 81.816  1.00 58.64 ? 354  ASN A N   1 
ATOM   2491 C  CA  . ASN A 1 352 ? 17.253 36.474 83.223  1.00 62.06 ? 354  ASN A CA  1 
ATOM   2492 C  C   . ASN A 1 352 ? 16.875 35.193 83.968  1.00 63.43 ? 354  ASN A C   1 
ATOM   2493 O  O   . ASN A 1 352 ? 17.112 35.087 85.171  1.00 62.98 ? 354  ASN A O   1 
ATOM   2494 C  CB  . ASN A 1 352 ? 16.580 37.699 83.849  1.00 65.91 ? 354  ASN A CB  1 
ATOM   2495 C  CG  . ASN A 1 352 ? 17.485 38.911 83.915  1.00 68.00 ? 354  ASN A CG  1 
ATOM   2496 O  OD1 . ASN A 1 352 ? 18.309 39.131 83.031  1.00 69.52 ? 354  ASN A OD1 1 
ATOM   2497 N  ND2 . ASN A 1 352 ? 17.361 39.691 84.975  1.00 70.52 ? 354  ASN A ND2 1 
ATOM   2498 N  N   . GLN A 1 353 ? 16.313 34.215 83.241  1.00 63.75 ? 355  GLN A N   1 
ATOM   2499 C  CA  . GLN A 1 353 ? 15.705 33.045 83.853  1.00 61.73 ? 355  GLN A CA  1 
ATOM   2500 C  C   . GLN A 1 353 ? 16.643 31.849 83.705  1.00 53.88 ? 355  GLN A C   1 
ATOM   2501 O  O   . GLN A 1 353 ? 16.934 31.407 82.593  1.00 53.41 ? 355  GLN A O   1 
ATOM   2502 C  CB  . GLN A 1 353 ? 14.344 32.790 83.198  1.00 66.07 ? 355  GLN A CB  1 
ATOM   2503 C  CG  . GLN A 1 353 ? 13.387 31.960 84.043  1.00 69.15 ? 355  GLN A CG  1 
ATOM   2504 C  CD  . GLN A 1 353 ? 11.944 32.295 83.732  1.00 75.46 ? 355  GLN A CD  1 
ATOM   2505 O  OE1 . GLN A 1 353 ? 11.182 31.479 83.215  1.00 76.49 ? 355  GLN A OE1 1 
ATOM   2506 N  NE2 . GLN A 1 353 ? 11.553 33.523 84.034  1.00 79.14 ? 355  GLN A NE2 1 
ATOM   2507 N  N   . TYR A 1 354 ? 17.100 31.322 84.844  1.00 47.37 ? 356  TYR A N   1 
ATOM   2508 C  CA  . TYR A 1 354 ? 17.863 30.086 84.868  1.00 39.99 ? 356  TYR A CA  1 
ATOM   2509 C  C   . TYR A 1 354 ? 16.891 28.922 84.713  1.00 38.56 ? 356  TYR A C   1 
ATOM   2510 O  O   . TYR A 1 354 ? 15.852 28.890 85.361  1.00 40.68 ? 356  TYR A O   1 
ATOM   2511 C  CB  . TYR A 1 354 ? 18.684 29.989 86.155  1.00 37.37 ? 356  TYR A CB  1 
ATOM   2512 C  CG  . TYR A 1 354 ? 19.949 30.831 86.128  1.00 35.43 ? 356  TYR A CG  1 
ATOM   2513 C  CD1 . TYR A 1 354 ? 21.034 30.467 85.346  1.00 32.80 ? 356  TYR A CD1 1 
ATOM   2514 C  CD2 . TYR A 1 354 ? 20.049 32.002 86.867  1.00 36.08 ? 356  TYR A CD2 1 
ATOM   2515 C  CE1 . TYR A 1 354 ? 22.189 31.225 85.311  1.00 32.03 ? 356  TYR A CE1 1 
ATOM   2516 C  CE2 . TYR A 1 354 ? 21.192 32.781 86.828  1.00 35.35 ? 356  TYR A CE2 1 
ATOM   2517 C  CZ  . TYR A 1 354 ? 22.268 32.383 86.059  1.00 33.61 ? 356  TYR A CZ  1 
ATOM   2518 O  OH  . TYR A 1 354 ? 23.401 33.134 86.027  1.00 33.26 ? 356  TYR A OH  1 
ATOM   2519 N  N   . SER A 1 355 ? 17.243 27.970 83.848  1.00 34.66 ? 357  SER A N   1 
ATOM   2520 C  CA  . SER A 1 355 ? 16.400 26.818 83.604  1.00 34.37 ? 357  SER A CA  1 
ATOM   2521 C  C   . SER A 1 355 ? 17.201 25.529 83.791  1.00 30.80 ? 357  SER A C   1 
ATOM   2522 O  O   . SER A 1 355 ? 18.284 25.389 83.233  1.00 27.44 ? 357  SER A O   1 
ATOM   2523 C  CB  . SER A 1 355 ? 15.817 26.911 82.231  1.00 36.00 ? 357  SER A CB  1 
ATOM   2524 O  OG  . SER A 1 355 ? 14.872 25.879 82.050  1.00 38.10 ? 357  SER A OG  1 
ATOM   2525 N  N   . GLU A 1 356 ? 16.661 24.590 84.582  1.00 30.35 ? 358  GLU A N   1 
ATOM   2526 C  CA  . GLU A 1 356 ? 17.343 23.333 84.856  1.00 28.70 ? 358  GLU A CA  1 
ATOM   2527 C  C   . GLU A 1 356 ? 17.523 22.551 83.552  1.00 27.47 ? 358  GLU A C   1 
ATOM   2528 O  O   . GLU A 1 356 ? 16.563 22.332 82.827  1.00 28.33 ? 358  GLU A O   1 
ATOM   2529 C  CB  . GLU A 1 356 ? 16.567 22.517 85.893  1.00 30.09 ? 358  GLU A CB  1 
ATOM   2530 C  CG  . GLU A 1 356 ? 17.101 21.106 86.140  1.00 29.12 ? 358  GLU A CG  1 
ATOM   2531 C  CD  . GLU A 1 356 ? 16.276 20.308 87.145  1.00 30.78 ? 358  GLU A CD  1 
ATOM   2532 O  OE1 . GLU A 1 356 ? 15.369 20.888 87.760  1.00 33.29 ? 358  GLU A OE1 1 
ATOM   2533 O  OE2 . GLU A 1 356 ? 16.524 19.103 87.309  1.00 29.54 ? 358  GLU A OE2 1 
ATOM   2534 N  N   . VAL A 1 357 ? 18.773 22.160 83.269  1.00 25.88 ? 359  VAL A N   1 
ATOM   2535 C  CA  . VAL A 1 357 ? 19.124 21.341 82.118  1.00 24.73 ? 359  VAL A CA  1 
ATOM   2536 C  C   . VAL A 1 357 ? 19.514 19.928 82.551  1.00 24.84 ? 359  VAL A C   1 
ATOM   2537 O  O   . VAL A 1 357 ? 19.122 18.979 81.881  1.00 26.67 ? 359  VAL A O   1 
ATOM   2538 C  CB  . VAL A 1 357 ? 20.208 21.995 81.238  1.00 23.27 ? 359  VAL A CB  1 
ATOM   2539 C  CG1 . VAL A 1 357 ? 19.667 23.222 80.518  1.00 24.65 ? 359  VAL A CG1 1 
ATOM   2540 C  CG2 . VAL A 1 357 ? 21.479 22.348 81.980  1.00 21.67 ? 359  VAL A CG2 1 
ATOM   2541 N  N   . ARG A 1 358 ? 20.272 19.767 83.642  1.00 23.85 ? 360  ARG A N   1 
ATOM   2542 C  CA  . ARG A 1 358 ? 20.642 18.439 84.116  1.00 24.89 ? 360  ARG A CA  1 
ATOM   2543 C  C   . ARG A 1 358 ? 20.651 18.423 85.640  1.00 23.68 ? 360  ARG A C   1 
ATOM   2544 O  O   . ARG A 1 358 ? 20.965 19.416 86.282  1.00 21.73 ? 360  ARG A O   1 
ATOM   2545 C  CB  . ARG A 1 358 ? 22.029 17.983 83.640  1.00 25.75 ? 360  ARG A CB  1 
ATOM   2546 C  CG  . ARG A 1 358 ? 22.251 17.969 82.130  1.00 29.15 ? 360  ARG A CG  1 
ATOM   2547 C  CD  . ARG A 1 358 ? 21.377 17.014 81.312  1.00 31.96 ? 360  ARG A CD  1 
ATOM   2548 N  NE  . ARG A 1 358 ? 21.862 15.642 81.257  1.00 34.79 ? 360  ARG A NE  1 
ATOM   2549 C  CZ  . ARG A 1 358 ? 21.423 14.707 80.406  1.00 36.60 ? 360  ARG A CZ  1 
ATOM   2550 N  NH1 . ARG A 1 358 ? 20.402 14.952 79.598  1.00 38.26 ? 360  ARG A NH1 1 
ATOM   2551 N  NH2 . ARG A 1 358 ? 22.013 13.521 80.364  1.00 36.13 ? 360  ARG A NH2 1 
ATOM   2552 N  N   . LYS A 1 359 ? 20.287 17.274 86.206  1.00 24.09 ? 361  LYS A N   1 
ATOM   2553 C  CA  . LYS A 1 359 ? 20.426 17.038 87.626  1.00 24.39 ? 361  LYS A CA  1 
ATOM   2554 C  C   . LYS A 1 359 ? 21.159 15.715 87.831  1.00 23.75 ? 361  LYS A C   1 
ATOM   2555 O  O   . LYS A 1 359 ? 20.884 14.744 87.135  1.00 24.33 ? 361  LYS A O   1 
ATOM   2556 C  CB  . LYS A 1 359 ? 19.058 16.996 88.314  1.00 26.74 ? 361  LYS A CB  1 
ATOM   2557 C  CG  . LYS A 1 359 ? 19.145 16.792 89.819  1.00 28.29 ? 361  LYS A CG  1 
ATOM   2558 C  CD  . LYS A 1 359 ? 17.856 16.464 90.535  1.00 31.88 ? 361  LYS A CD  1 
ATOM   2559 C  CE  . LYS A 1 359 ? 16.997 17.667 90.842  1.00 35.35 ? 361  LYS A CE  1 
ATOM   2560 N  NZ  . LYS A 1 359 ? 16.111 18.012 89.708  1.00 38.00 ? 361  LYS A NZ  1 
ATOM   2561 N  N   . ILE A 1 360 ? 22.092 15.688 88.788  1.00 21.96 ? 362  ILE A N   1 
ATOM   2562 C  CA  . ILE A 1 360 ? 22.683 14.440 89.243  1.00 21.42 ? 362  ILE A CA  1 
ATOM   2563 C  C   . ILE A 1 360 ? 22.345 14.243 90.713  1.00 21.36 ? 362  ILE A C   1 
ATOM   2564 O  O   . ILE A 1 360 ? 22.785 14.994 91.569  1.00 19.22 ? 362  ILE A O   1 
ATOM   2565 C  CB  . ILE A 1 360 ? 24.196 14.397 88.953  1.00 20.57 ? 362  ILE A CB  1 
ATOM   2566 C  CG1 . ILE A 1 360 ? 24.457 14.574 87.452  1.00 20.70 ? 362  ILE A CG1 1 
ATOM   2567 C  CG2 . ILE A 1 360 ? 24.814 13.110 89.513  1.00 20.57 ? 362  ILE A CG2 1 
ATOM   2568 C  CD1 . ILE A 1 360 ? 25.910 14.589 87.064  1.00 19.71 ? 362  ILE A CD1 1 
ATOM   2569 N  N   . GLU A 1 361 ? 21.514 13.235 90.984  1.00 23.30 ? 363  GLU A N   1 
ATOM   2570 C  CA  . GLU A 1 361 ? 21.044 12.963 92.331  1.00 24.58 ? 363  GLU A CA  1 
ATOM   2571 C  C   . GLU A 1 361 ? 22.203 12.443 93.175  1.00 21.46 ? 363  GLU A C   1 
ATOM   2572 O  O   . GLU A 1 361 ? 23.224 11.998 92.656  1.00 19.15 ? 363  GLU A O   1 
ATOM   2573 C  CB  . GLU A 1 361 ? 19.914 11.931 92.302  1.00 29.28 ? 363  GLU A CB  1 
ATOM   2574 C  CG  . GLU A 1 361 ? 18.668 12.418 91.580  1.00 34.23 ? 363  GLU A CG  1 
ATOM   2575 C  CD  . GLU A 1 361 ? 17.812 13.422 92.338  1.00 39.01 ? 363  GLU A CD  1 
ATOM   2576 O  OE1 . GLU A 1 361 ? 18.216 13.843 93.460  1.00 41.52 ? 363  GLU A OE1 1 
ATOM   2577 O  OE2 . GLU A 1 361 ? 16.732 13.784 91.808  1.00 44.50 ? 363  GLU A OE2 1 
ATOM   2578 N  N   . ALA A 1 362 ? 22.036 12.514 94.493  1.00 20.54 ? 364  ALA A N   1 
ATOM   2579 C  CA  . ALA A 1 362 ? 23.081 12.078 95.406  1.00 19.31 ? 364  ALA A CA  1 
ATOM   2580 C  C   . ALA A 1 362 ? 23.250 10.563 95.312  1.00 19.56 ? 364  ALA A C   1 
ATOM   2581 O  O   . ALA A 1 362 ? 22.272 9.834  95.173  1.00 21.24 ? 364  ALA A O   1 
ATOM   2582 C  CB  . ALA A 1 362 ? 22.758 12.521 96.812  1.00 19.09 ? 364  ALA A CB  1 
ATOM   2583 N  N   . SER A 1 363 ? 24.497 10.098 95.404  1.00 18.61 ? 365  SER A N   1 
ATOM   2584 C  CA  . SER A 1 363 ? 24.789 8.672  95.398  1.00 19.17 ? 365  SER A CA  1 
ATOM   2585 C  C   . SER A 1 363 ? 26.040 8.441  96.233  1.00 18.55 ? 365  SER A C   1 
ATOM   2586 O  O   . SER A 1 363 ? 26.451 9.316  96.983  1.00 18.17 ? 365  SER A O   1 
ATOM   2587 C  CB  . SER A 1 363 ? 24.929 8.131  93.991  1.00 19.06 ? 365  SER A CB  1 
ATOM   2588 O  OG  . SER A 1 363 ? 26.067 8.677  93.345  1.00 18.28 ? 365  SER A OG  1 
ATOM   2589 N  N   . SER A 1 364 ? 26.644 7.266  96.078  1.00 18.84 ? 366  SER A N   1 
ATOM   2590 C  CA  . SER A 1 364 ? 27.923 6.978  96.707  1.00 18.25 ? 366  SER A CA  1 
ATOM   2591 C  C   . SER A 1 364 ? 29.056 7.609  95.898  1.00 16.76 ? 366  SER A C   1 
ATOM   2592 O  O   . SER A 1 364 ? 30.201 7.537  96.320  1.00 16.96 ? 366  SER A O   1 
ATOM   2593 C  CB  . SER A 1 364 ? 28.110 5.496  96.845  1.00 19.30 ? 366  SER A CB  1 
ATOM   2594 O  OG  . SER A 1 364 ? 27.891 4.871  95.582  1.00 19.80 ? 366  SER A OG  1 
ATOM   2595 N  N   . SER A 1 365 ? 28.740 8.231  94.753  1.00 15.50 ? 367  SER A N   1 
ATOM   2596 C  CA  . SER A 1 365 ? 29.748 8.852  93.918  1.00 14.28 ? 367  SER A CA  1 
ATOM   2597 C  C   . SER A 1 365 ? 30.255 10.161 94.516  1.00 12.46 ? 367  SER A C   1 
ATOM   2598 O  O   . SER A 1 365 ? 29.493 10.937 95.089  1.00 11.79 ? 367  SER A O   1 
ATOM   2599 C  CB  . SER A 1 365 ? 29.223 9.100  92.558  1.00 14.60 ? 367  SER A CB  1 
ATOM   2600 O  OG  . SER A 1 365 ? 30.302 9.370  91.666  1.00 14.85 ? 367  SER A OG  1 
ATOM   2601 N  N   . SER A 1 366 ? 31.548 10.415 94.316  1.00 11.81 ? 368  SER A N   1 
ATOM   2602 C  CA  . SER A 1 366 ? 32.147 11.698 94.634  1.00 10.93 ? 368  SER A CA  1 
ATOM   2603 C  C   . SER A 1 366 ? 32.549 12.471 93.379  1.00 10.57 ? 368  SER A C   1 
ATOM   2604 O  O   . SER A 1 366 ? 33.194 13.526 93.486  1.00 10.07 ? 368  SER A O   1 
ATOM   2605 C  CB  . SER A 1 366 ? 33.338 11.498 95.497  1.00 11.18 ? 368  SER A CB  1 
ATOM   2606 O  OG  . SER A 1 366 ? 34.336 10.752 94.823  1.00 11.47 ? 368  SER A OG  1 
ATOM   2607 N  N   . THR A 1 367 ? 32.181 11.956 92.201  1.00 11.09 ? 369  THR A N   1 
ATOM   2608 C  CA  . THR A 1 367 ? 32.470 12.622 90.935  1.00 11.06 ? 369  THR A CA  1 
ATOM   2609 C  C   . THR A 1 367 ? 31.168 12.782 90.161  1.00 11.32 ? 369  THR A C   1 
ATOM   2610 O  O   . THR A 1 367 ? 30.296 11.915 90.227  1.00 12.26 ? 369  THR A O   1 
ATOM   2611 C  CB  . THR A 1 367 ? 33.490 11.840 90.098  1.00 12.20 ? 369  THR A CB  1 
ATOM   2612 O  OG1 . THR A 1 367 ? 34.669 11.704 90.889  1.00 12.72 ? 369  THR A OG1 1 
ATOM   2613 C  CG2 . THR A 1 367 ? 33.839 12.490 88.772  1.00 12.21 ? 369  THR A CG2 1 
ATOM   2614 N  N   . PHE A 1 368 ? 31.057 13.912 89.458  1.00 10.71 ? 370  PHE A N   1 
ATOM   2615 C  CA  . PHE A 1 368 ? 29.851 14.288 88.740  1.00 11.30 ? 370  PHE A CA  1 
ATOM   2616 C  C   . PHE A 1 368 ? 30.253 14.726 87.335  1.00 11.40 ? 370  PHE A C   1 
ATOM   2617 O  O   . PHE A 1 368 ? 30.888 15.753 87.178  1.00 11.34 ? 370  PHE A O   1 
ATOM   2618 C  CB  . PHE A 1 368 ? 29.104 15.417 89.458  1.00 10.98 ? 370  PHE A CB  1 
ATOM   2619 C  CG  . PHE A 1 368 ? 28.804 15.114 90.905  1.00 11.31 ? 370  PHE A CG  1 
ATOM   2620 C  CD1 . PHE A 1 368 ? 29.787 15.226 91.877  1.00 11.01 ? 370  PHE A CD1 1 
ATOM   2621 C  CD2 . PHE A 1 368 ? 27.539 14.684 91.285  1.00 12.05 ? 370  PHE A CD2 1 
ATOM   2622 C  CE1 . PHE A 1 368 ? 29.503 14.917 93.196  1.00 11.43 ? 370  PHE A CE1 1 
ATOM   2623 C  CE2 . PHE A 1 368 ? 27.261 14.373 92.605  1.00 12.39 ? 370  PHE A CE2 1 
ATOM   2624 C  CZ  . PHE A 1 368 ? 28.248 14.479 93.550  1.00 11.90 ? 370  PHE A CZ  1 
ATOM   2625 N  N   . ASP A 1 369 ? 29.816 13.957 86.344  1.00 12.62 ? 371  ASP A N   1 
ATOM   2626 C  CA  . ASP A 1 369 ? 30.115 14.238 84.943  1.00 14.01 ? 371  ASP A CA  1 
ATOM   2627 C  C   . ASP A 1 369 ? 28.860 14.745 84.245  1.00 13.44 ? 371  ASP A C   1 
ATOM   2628 O  O   . ASP A 1 369 ? 27.909 13.988 84.081  1.00 13.63 ? 371  ASP A O   1 
ATOM   2629 C  CB  . ASP A 1 369 ? 30.628 12.985 84.225  1.00 15.92 ? 371  ASP A CB  1 
ATOM   2630 C  CG  . ASP A 1 369 ? 32.030 12.607 84.672  1.00 18.02 ? 371  ASP A CG  1 
ATOM   2631 O  OD1 . ASP A 1 369 ? 32.646 13.433 85.306  1.00 19.76 ? 371  ASP A OD1 1 
ATOM   2632 O  OD2 . ASP A 1 369 ? 32.508 11.501 84.353  1.00 20.44 ? 371  ASP A OD2 1 
ATOM   2633 N  N   . PHE A 1 370 ? 28.902 16.019 83.854  1.00 12.73 ? 372  PHE A N   1 
ATOM   2634 C  CA  . PHE A 1 370 ? 27.918 16.619 82.972  1.00 13.33 ? 372  PHE A CA  1 
ATOM   2635 C  C   . PHE A 1 370 ? 28.452 16.522 81.558  1.00 13.09 ? 372  PHE A C   1 
ATOM   2636 O  O   . PHE A 1 370 ? 29.112 17.417 81.075  1.00 12.97 ? 372  PHE A O   1 
ATOM   2637 C  CB  . PHE A 1 370 ? 27.638 18.065 83.360  1.00 13.76 ? 372  PHE A CB  1 
ATOM   2638 C  CG  . PHE A 1 370 ? 26.934 18.196 84.679  1.00 14.24 ? 372  PHE A CG  1 
ATOM   2639 C  CD1 . PHE A 1 370 ? 25.565 17.998 84.776  1.00 15.41 ? 372  PHE A CD1 1 
ATOM   2640 C  CD2 . PHE A 1 370 ? 27.651 18.450 85.835  1.00 14.50 ? 372  PHE A CD2 1 
ATOM   2641 C  CE1 . PHE A 1 370 ? 24.920 18.104 86.005  1.00 16.09 ? 372  PHE A CE1 1 
ATOM   2642 C  CE2 . PHE A 1 370 ? 27.010 18.542 87.060  1.00 14.30 ? 372  PHE A CE2 1 
ATOM   2643 C  CZ  . PHE A 1 370 ? 25.641 18.411 87.139  1.00 15.33 ? 372  PHE A CZ  1 
ATOM   2644 N  N   . TYR A 1 371 ? 28.199 15.389 80.927  1.00 13.51 ? 373  TYR A N   1 
ATOM   2645 C  CA  . TYR A 1 371 ? 28.797 15.089 79.641  1.00 14.10 ? 373  TYR A CA  1 
ATOM   2646 C  C   . TYR A 1 371 ? 27.962 15.765 78.555  1.00 14.16 ? 373  TYR A C   1 
ATOM   2647 O  O   . TYR A 1 371 ? 26.790 15.465 78.392  1.00 14.83 ? 373  TYR A O   1 
ATOM   2648 C  CB  . TYR A 1 371 ? 28.913 13.571 79.526  1.00 14.97 ? 373  TYR A CB  1 
ATOM   2649 C  CG  . TYR A 1 371 ? 29.881 13.051 78.483  1.00 15.99 ? 373  TYR A CG  1 
ATOM   2650 C  CD1 . TYR A 1 371 ? 29.569 13.145 77.120  1.00 16.64 ? 373  TYR A CD1 1 
ATOM   2651 C  CD2 . TYR A 1 371 ? 31.076 12.435 78.841  1.00 16.10 ? 373  TYR A CD2 1 
ATOM   2652 C  CE1 . TYR A 1 371 ? 30.412 12.630 76.149  1.00 17.48 ? 373  TYR A CE1 1 
ATOM   2653 C  CE2 . TYR A 1 371 ? 31.923 11.915 77.872  1.00 17.14 ? 373  TYR A CE2 1 
ATOM   2654 C  CZ  . TYR A 1 371 ? 31.597 12.027 76.526  1.00 17.99 ? 373  TYR A CZ  1 
ATOM   2655 O  OH  . TYR A 1 371 ? 32.407 11.567 75.528  1.00 18.88 ? 373  TYR A OH  1 
ATOM   2656 N  N   . GLY A 1 372 ? 28.591 16.658 77.797  1.00 13.45 ? 374  GLY A N   1 
ATOM   2657 C  CA  . GLY A 1 372 ? 27.924 17.343 76.704  1.00 13.88 ? 374  GLY A CA  1 
ATOM   2658 C  C   . GLY A 1 372 ? 27.410 18.715 77.123  1.00 13.63 ? 374  GLY A C   1 
ATOM   2659 O  O   . GLY A 1 372 ? 26.215 18.931 77.297  1.00 14.11 ? 374  GLY A O   1 
ATOM   2660 N  N   . ILE A 1 373 ? 28.356 19.627 77.327  1.00 13.64 ? 375  ILE A N   1 
ATOM   2661 C  CA  . ILE A 1 373 ? 28.060 20.996 77.698  1.00 13.57 ? 375  ILE A CA  1 
ATOM   2662 C  C   . ILE A 1 373 ? 28.710 21.908 76.656  1.00 13.76 ? 375  ILE A C   1 
ATOM   2663 O  O   . ILE A 1 373 ? 29.702 21.544 76.022  1.00 13.37 ? 375  ILE A O   1 
ATOM   2664 C  CB  . ILE A 1 373 ? 28.520 21.289 79.140  1.00 13.17 ? 375  ILE A CB  1 
ATOM   2665 C  CG1 . ILE A 1 373 ? 27.974 22.632 79.628  1.00 13.39 ? 375  ILE A CG1 1 
ATOM   2666 C  CG2 . ILE A 1 373 ? 30.036 21.218 79.257  1.00 12.96 ? 375  ILE A CG2 1 
ATOM   2667 C  CD1 . ILE A 1 373 ? 28.084 22.850 81.161  1.00 13.22 ? 375  ILE A CD1 1 
ATOM   2668 N  N   . LYS A 1 374 ? 28.101 23.077 76.464  1.00 14.35 ? 376  LYS A N   1 
ATOM   2669 C  CA  . LYS A 1 374 ? 28.529 24.004 75.433  1.00 14.89 ? 376  LYS A CA  1 
ATOM   2670 C  C   . LYS A 1 374 ? 28.770 25.391 76.026  1.00 15.07 ? 376  LYS A C   1 
ATOM   2671 O  O   . LYS A 1 374 ? 28.619 25.620 77.224  1.00 14.45 ? 376  LYS A O   1 
ATOM   2672 C  CB  . LYS A 1 374 ? 27.473 24.048 74.335  1.00 15.69 ? 376  LYS A CB  1 
ATOM   2673 C  CG  . LYS A 1 374 ? 26.147 24.658 74.752  1.00 16.29 ? 376  LYS A CG  1 
ATOM   2674 C  CD  . LYS A 1 374 ? 25.161 24.695 73.620  1.00 17.30 ? 376  LYS A CD  1 
ATOM   2675 C  CE  . LYS A 1 374 ? 23.893 25.419 74.002  1.00 18.42 ? 376  LYS A CE  1 
ATOM   2676 N  NZ  . LYS A 1 374 ? 22.996 25.509 72.842  1.00 19.66 ? 376  LYS A NZ  1 
ATOM   2677 N  N   . ALA A 1 375 ? 29.138 26.340 75.158  1.00 15.80 ? 377  ALA A N   1 
ATOM   2678 C  CA  . ALA A 1 375 ? 29.289 27.720 75.568  1.00 16.25 ? 377  ALA A CA  1 
ATOM   2679 C  C   . ALA A 1 375 ? 27.932 28.261 75.993  1.00 16.68 ? 377  ALA A C   1 
ATOM   2680 O  O   . ALA A 1 375 ? 26.920 27.981 75.365  1.00 17.01 ? 377  ALA A O   1 
ATOM   2681 C  CB  . ALA A 1 375 ? 29.888 28.541 74.453  1.00 17.39 ? 377  ALA A CB  1 
ATOM   2682 N  N   . GLY A 1 376 ? 27.940 29.061 77.061  1.00 16.82 ? 378  GLY A N   1 
ATOM   2683 C  CA  . GLY A 1 376 ? 26.732 29.668 77.590  1.00 17.76 ? 378  GLY A CA  1 
ATOM   2684 C  C   . GLY A 1 376 ? 26.951 30.068 79.044  1.00 17.81 ? 378  GLY A C   1 
ATOM   2685 O  O   . GLY A 1 376 ? 28.051 29.887 79.568  1.00 16.80 ? 378  GLY A O   1 
ATOM   2686 N  N   . ASP A 1 377 ? 25.905 30.626 79.671  1.00 19.28 ? 379  ASP A N   1 
ATOM   2687 C  CA  . ASP A 1 377 ? 25.958 31.018 81.074  1.00 19.90 ? 379  ASP A CA  1 
ATOM   2688 C  C   . ASP A 1 377 ? 25.203 29.995 81.902  1.00 18.85 ? 379  ASP A C   1 
ATOM   2689 O  O   . ASP A 1 377 ? 24.098 29.599 81.540  1.00 19.24 ? 379  ASP A O   1 
ATOM   2690 C  CB  . ASP A 1 377 ? 25.353 32.398 81.309  1.00 22.66 ? 379  ASP A CB  1 
ATOM   2691 C  CG  . ASP A 1 377 ? 26.013 33.465 80.470  1.00 24.36 ? 379  ASP A CG  1 
ATOM   2692 O  OD1 . ASP A 1 377 ? 27.263 33.514 80.463  1.00 24.35 ? 379  ASP A OD1 1 
ATOM   2693 O  OD2 . ASP A 1 377 ? 25.273 34.291 79.909  1.00 26.89 ? 379  ASP A OD2 1 
ATOM   2694 N  N   . TYR A 1 378 ? 25.808 29.577 83.017  1.00 17.48 ? 380  TYR A N   1 
ATOM   2695 C  CA  . TYR A 1 378 ? 25.287 28.467 83.792  1.00 16.67 ? 380  TYR A CA  1 
ATOM   2696 C  C   . TYR A 1 378 ? 25.240 28.854 85.264  1.00 17.05 ? 380  TYR A C   1 
ATOM   2697 O  O   . TYR A 1 378 ? 25.889 29.802 85.684  1.00 17.13 ? 380  TYR A O   1 
ATOM   2698 C  CB  . TYR A 1 378 ? 26.198 27.260 83.569  1.00 15.00 ? 380  TYR A CB  1 
ATOM   2699 C  CG  . TYR A 1 378 ? 26.166 26.724 82.141  1.00 14.75 ? 380  TYR A CG  1 
ATOM   2700 C  CD1 . TYR A 1 378 ? 25.148 25.874 81.725  1.00 15.01 ? 380  TYR A CD1 1 
ATOM   2701 C  CD2 . TYR A 1 378 ? 27.138 27.064 81.218  1.00 14.64 ? 380  TYR A CD2 1 
ATOM   2702 C  CE1 . TYR A 1 378 ? 25.095 25.369 80.434  1.00 14.78 ? 380  TYR A CE1 1 
ATOM   2703 C  CE2 . TYR A 1 378 ? 27.096 26.572 79.922  1.00 14.61 ? 380  TYR A CE2 1 
ATOM   2704 C  CZ  . TYR A 1 378 ? 26.068 25.729 79.523  1.00 14.98 ? 380  TYR A CZ  1 
ATOM   2705 O  OH  . TYR A 1 378 ? 26.013 25.231 78.230  1.00 15.45 ? 380  TYR A OH  1 
ATOM   2706 N  N   . LYS A 1 379 ? 24.448 28.095 86.015  1.00 17.68 ? 381  LYS A N   1 
ATOM   2707 C  CA  . LYS A 1 379 ? 24.502 28.134 87.465  1.00 18.37 ? 381  LYS A CA  1 
ATOM   2708 C  C   . LYS A 1 379 ? 24.504 26.702 87.980  1.00 17.17 ? 381  LYS A C   1 
ATOM   2709 O  O   . LYS A 1 379 ? 23.668 25.894 87.582  1.00 17.01 ? 381  LYS A O   1 
ATOM   2710 C  CB  . LYS A 1 379 ? 23.314 28.896 88.053  1.00 20.87 ? 381  LYS A CB  1 
ATOM   2711 C  CG  . LYS A 1 379 ? 23.407 29.155 89.552  1.00 22.21 ? 381  LYS A CG  1 
ATOM   2712 C  CD  . LYS A 1 379 ? 22.476 30.223 90.045  1.00 25.44 ? 381  LYS A CD  1 
ATOM   2713 C  CE  . LYS A 1 379 ? 21.028 29.787 90.007  1.00 27.43 ? 381  LYS A CE  1 
ATOM   2714 N  NZ  . LYS A 1 379 ? 20.141 30.934 90.327  1.00 30.33 ? 381  LYS A NZ  1 
ATOM   2715 N  N   . LEU A 1 380 ? 25.414 26.430 88.910  1.00 16.06 ? 382  LEU A N   1 
ATOM   2716 C  CA  . LEU A 1 380 ? 25.518 25.129 89.539  1.00 15.60 ? 382  LEU A CA  1 
ATOM   2717 C  C   . LEU A 1 380 ? 25.011 25.229 90.980  1.00 15.63 ? 382  LEU A C   1 
ATOM   2718 O  O   . LEU A 1 380 ? 25.568 25.989 91.760  1.00 15.61 ? 382  LEU A O   1 
ATOM   2719 C  CB  . LEU A 1 380 ? 26.992 24.729 89.473  1.00 15.46 ? 382  LEU A CB  1 
ATOM   2720 C  CG  . LEU A 1 380 ? 27.329 23.362 90.055  1.00 16.50 ? 382  LEU A CG  1 
ATOM   2721 C  CD1 . LEU A 1 380 ? 26.822 22.228 89.156  1.00 15.78 ? 382  LEU A CD1 1 
ATOM   2722 C  CD2 . LEU A 1 380 ? 28.835 23.242 90.267  1.00 17.36 ? 382  LEU A CD2 1 
ATOM   2723 N  N   . VAL A 1 381 ? 23.980 24.454 91.283  1.00 15.64 ? 383  VAL A N   1 
ATOM   2724 C  CA  . VAL A 1 381 ? 23.341 24.401 92.627  1.00 16.44 ? 383  VAL A CA  1 
ATOM   2725 C  C   . VAL A 1 381 ? 23.642 23.054 93.301  1.00 15.59 ? 383  VAL A C   1 
ATOM   2726 O  O   . VAL A 1 381 ? 23.508 22.047 92.665  1.00 14.46 ? 383  VAL A O   1 
ATOM   2727 C  CB  . VAL A 1 381 ? 21.830 24.662 92.533  1.00 17.79 ? 383  VAL A CB  1 
ATOM   2728 C  CG1 . VAL A 1 381 ? 21.078 24.409 93.811  1.00 18.69 ? 383  VAL A CG1 1 
ATOM   2729 C  CG2 . VAL A 1 381 ? 21.490 26.027 91.981  1.00 19.08 ? 383  VAL A CG2 1 
ATOM   2730 N  N   . GLU A 1 382 ? 24.035 23.093 94.580  1.00 15.71 ? 384  GLU A N   1 
ATOM   2731 C  CA  . GLU A 1 382 ? 24.275 21.858 95.376  1.00 15.73 ? 384  GLU A CA  1 
ATOM   2732 C  C   . GLU A 1 382 ? 22.916 21.446 95.951  1.00 16.86 ? 384  GLU A C   1 
ATOM   2733 O  O   . GLU A 1 382 ? 22.621 21.814 97.105  1.00 17.55 ? 384  GLU A O   1 
ATOM   2734 C  CB  . GLU A 1 382 ? 25.293 22.123 96.486  1.00 15.70 ? 384  GLU A CB  1 
ATOM   2735 C  CG  . GLU A 1 382 ? 25.814 20.857 97.142  1.00 15.90 ? 384  GLU A CG  1 
ATOM   2736 C  CD  . GLU A 1 382 ? 26.864 21.086 98.215  1.00 15.90 ? 384  GLU A CD  1 
ATOM   2737 O  OE1 . GLU A 1 382 ? 26.766 22.104 98.928  1.00 17.04 ? 384  GLU A OE1 1 
ATOM   2738 O  OE2 . GLU A 1 382 ? 27.777 20.245 98.336  1.00 16.00 ? 384  GLU A OE2 1 
ATOM   2739 N  N   . SER A 1 383 ? 22.129 20.709 95.160  1.00 17.10 ? 385  SER A N   1 
ATOM   2740 C  CA  . SER A 1 383 ? 20.747 20.332 95.532  1.00 18.61 ? 385  SER A CA  1 
ATOM   2741 C  C   . SER A 1 383 ? 20.716 19.337 96.700  1.00 18.49 ? 385  SER A C   1 
ATOM   2742 O  O   . SER A 1 383 ? 19.751 19.248 97.338  1.00 19.35 ? 385  SER A O   1 
ATOM   2743 C  CB  . SER A 1 383 ? 19.990 19.853 94.339  1.00 19.69 ? 385  SER A CB  1 
ATOM   2744 O  OG  . SER A 1 383 ? 20.769 18.978 93.593  1.00 19.09 ? 385  SER A OG  1 
ATOM   2745 N  N   . THR A 1 384 ? 21.746 18.558 96.872  1.00 17.24 ? 386  THR A N   1 
ATOM   2746 C  CA  . THR A 1 384 ? 21.885 17.737 98.066  1.00 17.62 ? 386  THR A CA  1 
ATOM   2747 C  C   . THR A 1 384 ? 23.281 17.941 98.645  1.00 16.57 ? 386  THR A C   1 
ATOM   2748 O  O   . THR A 1 384 ? 24.273 17.828 97.923  1.00 15.05 ? 386  THR A O   1 
ATOM   2749 C  CB  . THR A 1 384 ? 21.668 16.240 97.795  1.00 17.91 ? 386  THR A CB  1 
ATOM   2750 O  OG1 . THR A 1 384 ? 20.384 16.065 97.202  1.00 19.66 ? 386  THR A OG1 1 
ATOM   2751 C  CG2 . THR A 1 384 ? 21.727 15.389 99.051  1.00 18.32 ? 386  THR A CG2 1 
ATOM   2752 N  N   . THR A 1 385 ? 23.343 18.269 99.936  1.00 16.91 ? 387  THR A N   1 
ATOM   2753 C  CA  . THR A 1 385 ? 24.604 18.522 100.608 1.00 16.83 ? 387  THR A CA  1 
ATOM   2754 C  C   . THR A 1 385 ? 24.992 17.274 101.386 1.00 16.95 ? 387  THR A C   1 
ATOM   2755 O  O   . THR A 1 385 ? 24.125 16.699 102.057 1.00 18.63 ? 387  THR A O   1 
ATOM   2756 C  CB  . THR A 1 385 ? 24.501 19.723 101.559 1.00 17.71 ? 387  THR A CB  1 
ATOM   2757 O  OG1 . THR A 1 385 ? 23.982 20.811 100.795 1.00 18.39 ? 387  THR A OG1 1 
ATOM   2758 C  CG2 . THR A 1 385 ? 25.834 20.097 102.167 1.00 17.20 ? 387  THR A CG2 1 
ATOM   2759 N  N   . PRO A 1 386 ? 26.269 16.815 101.326 1.00 15.64 ? 388  PRO A N   1 
ATOM   2760 C  CA  . PRO A 1 386 ? 26.698 15.665 102.111 1.00 15.80 ? 388  PRO A CA  1 
ATOM   2761 C  C   . PRO A 1 386 ? 26.494 15.958 103.587 1.00 16.76 ? 388  PRO A C   1 
ATOM   2762 O  O   . PRO A 1 386 ? 26.660 17.094 104.035 1.00 16.96 ? 388  PRO A O   1 
ATOM   2763 C  CB  . PRO A 1 386 ? 28.182 15.472 101.774 1.00 15.15 ? 388  PRO A CB  1 
ATOM   2764 C  CG  . PRO A 1 386 ? 28.350 16.180 100.423 1.00 14.38 ? 388  PRO A CG  1 
ATOM   2765 C  CD  . PRO A 1 386 ? 27.361 17.330 100.481 1.00 14.98 ? 388  PRO A CD  1 
ATOM   2766 N  N   . ALA A 1 387 ? 26.166 14.905 104.340 1.00 17.49 ? 389  ALA A N   1 
ATOM   2767 C  CA  . ALA A 1 387 ? 25.937 15.060 105.760 1.00 18.67 ? 389  ALA A CA  1 
ATOM   2768 C  C   . ALA A 1 387 ? 27.188 15.656 106.414 1.00 18.55 ? 389  ALA A C   1 
ATOM   2769 O  O   . ALA A 1 387 ? 28.300 15.192 106.140 1.00 19.42 ? 389  ALA A O   1 
ATOM   2770 C  CB  . ALA A 1 387 ? 25.568 13.716 106.370 1.00 19.07 ? 389  ALA A CB  1 
ATOM   2771 N  N   . GLY A 1 388 ? 26.980 16.656 107.283 1.00 17.95 ? 390  GLY A N   1 
ATOM   2772 C  CA  . GLY A 1 388 ? 28.005 17.204 108.158 1.00 17.68 ? 390  GLY A CA  1 
ATOM   2773 C  C   . GLY A 1 388 ? 28.873 18.276 107.505 1.00 16.82 ? 390  GLY A C   1 
ATOM   2774 O  O   . GLY A 1 388 ? 29.968 18.565 107.977 1.00 17.36 ? 390  GLY A O   1 
ATOM   2775 N  N   . TYR A 1 389 ? 28.385 18.898 106.434 1.00 15.67 ? 391  TYR A N   1 
ATOM   2776 C  CA  . TYR A 1 389 ? 29.131 19.951 105.774 1.00 14.99 ? 391  TYR A CA  1 
ATOM   2777 C  C   . TYR A 1 389 ? 28.194 21.100 105.430 1.00 15.50 ? 391  TYR A C   1 
ATOM   2778 O  O   . TYR A 1 389 ? 26.988 20.897 105.369 1.00 15.46 ? 391  TYR A O   1 
ATOM   2779 C  CB  . TYR A 1 389 ? 29.759 19.386 104.504 1.00 14.00 ? 391  TYR A CB  1 
ATOM   2780 C  CG  . TYR A 1 389 ? 30.849 18.356 104.721 1.00 13.33 ? 391  TYR A CG  1 
ATOM   2781 C  CD1 . TYR A 1 389 ? 32.096 18.697 105.209 1.00 13.51 ? 391  TYR A CD1 1 
ATOM   2782 C  CD2 . TYR A 1 389 ? 30.610 17.040 104.422 1.00 12.91 ? 391  TYR A CD2 1 
ATOM   2783 C  CE1 . TYR A 1 389 ? 33.091 17.744 105.363 1.00 13.52 ? 391  TYR A CE1 1 
ATOM   2784 C  CE2 . TYR A 1 389 ? 31.592 16.081 104.540 1.00 12.88 ? 391  TYR A CE2 1 
ATOM   2785 C  CZ  . TYR A 1 389 ? 32.825 16.432 105.034 1.00 13.31 ? 391  TYR A CZ  1 
ATOM   2786 O  OH  . TYR A 1 389 ? 33.724 15.415 105.129 1.00 13.90 ? 391  TYR A OH  1 
ATOM   2787 N  N   . ASN A 1 390 ? 28.784 22.294 105.247 1.00 15.90 ? 392  ASN A N   1 
ATOM   2788 C  CA  . ASN A 1 390 ? 28.083 23.470 104.778 1.00 16.68 ? 392  ASN A CA  1 
ATOM   2789 C  C   . ASN A 1 390 ? 27.647 23.242 103.328 1.00 16.19 ? 392  ASN A C   1 
ATOM   2790 O  O   . ASN A 1 390 ? 28.407 22.707 102.521 1.00 14.77 ? 392  ASN A O   1 
ATOM   2791 C  CB  . ASN A 1 390 ? 28.950 24.734 104.878 1.00 17.53 ? 392  ASN A CB  1 
ATOM   2792 C  CG  . ASN A 1 390 ? 29.378 25.077 106.299 1.00 18.86 ? 392  ASN A CG  1 
ATOM   2793 O  OD1 . ASN A 1 390 ? 30.565 25.245 106.586 1.00 20.37 ? 392  ASN A OD1 1 
ATOM   2794 N  ND2 . ASN A 1 390 ? 28.438 25.148 107.213 1.00 18.93 ? 392  ASN A ND2 1 
ATOM   2795 N  N   . THR A 1 391 ? 26.400 23.634 103.030 1.00 17.49 ? 393  THR A N   1 
ATOM   2796 C  CA  . THR A 1 391 ? 25.918 23.729 101.657 1.00 17.60 ? 393  THR A CA  1 
ATOM   2797 C  C   . THR A 1 391 ? 26.774 24.758 100.920 1.00 17.81 ? 393  THR A C   1 
ATOM   2798 O  O   . THR A 1 391 ? 26.949 25.867 101.383 1.00 18.88 ? 393  THR A O   1 
ATOM   2799 C  CB  . THR A 1 391 ? 24.421 24.075 101.615 1.00 18.40 ? 393  THR A CB  1 
ATOM   2800 O  OG1 . THR A 1 391 ? 23.702 23.078 102.334 1.00 18.27 ? 393  THR A OG1 1 
ATOM   2801 C  CG2 . THR A 1 391 ? 23.868 24.151 100.207 1.00 18.15 ? 393  THR A CG2 1 
ATOM   2802 N  N   . MET A 1 392 ? 27.286 24.382 99.747  1.00 17.86 ? 394  MET A N   1 
ATOM   2803 C  CA  . MET A 1 392 ? 28.022 25.281 98.871  1.00 18.47 ? 394  MET A CA  1 
ATOM   2804 C  C   . MET A 1 392 ? 27.111 26.420 98.385  1.00 19.63 ? 394  MET A C   1 
ATOM   2805 O  O   . MET A 1 392 ? 25.908 26.241 98.164  1.00 19.68 ? 394  MET A O   1 
ATOM   2806 C  CB  . MET A 1 392 ? 28.552 24.445 97.696  1.00 18.19 ? 394  MET A CB  1 
ATOM   2807 C  CG  . MET A 1 392 ? 29.008 25.219 96.517  1.00 18.86 ? 394  MET A CG  1 
ATOM   2808 S  SD  . MET A 1 392 ? 29.180 24.135 95.092  1.00 17.60 ? 394  MET A SD  1 
ATOM   2809 C  CE  . MET A 1 392 ? 27.696 24.554 94.166  1.00 18.17 ? 394  MET A CE  1 
ATOM   2810 N  N   . LYS A 1 393 ? 27.678 27.622 98.245  1.00 20.52 ? 395  LYS A N   1 
ATOM   2811 C  CA  . LYS A 1 393 ? 26.958 28.719 97.608  1.00 22.55 ? 395  LYS A CA  1 
ATOM   2812 C  C   . LYS A 1 393 ? 26.869 28.475 96.101  1.00 20.63 ? 395  LYS A C   1 
ATOM   2813 O  O   . LYS A 1 393 ? 27.818 27.964 95.505  1.00 19.09 ? 395  LYS A O   1 
ATOM   2814 C  CB  . LYS A 1 393 ? 27.658 30.057 97.839  1.00 25.38 ? 395  LYS A CB  1 
ATOM   2815 C  CG  . LYS A 1 393 ? 27.743 30.488 99.298  1.00 28.98 ? 395  LYS A CG  1 
ATOM   2816 C  CD  . LYS A 1 393 ? 28.180 31.920 99.449  1.00 32.56 ? 395  LYS A CD  1 
ATOM   2817 C  CE  . LYS A 1 393 ? 28.415 32.301 100.897 1.00 35.44 ? 395  LYS A CE  1 
ATOM   2818 N  NZ  . LYS A 1 393 ? 29.014 33.652 100.976 1.00 39.10 ? 395  LYS A NZ  1 
ATOM   2819 N  N   . ASP A 1 394 ? 25.757 28.900 95.497  1.00 20.75 ? 396  ASP A N   1 
ATOM   2820 C  CA  . ASP A 1 394 ? 25.534 28.718 94.063  1.00 19.76 ? 396  ASP A CA  1 
ATOM   2821 C  C   . ASP A 1 394 ? 26.695 29.328 93.280  1.00 18.66 ? 396  ASP A C   1 
ATOM   2822 O  O   . ASP A 1 394 ? 27.191 30.385 93.632  1.00 18.79 ? 396  ASP A O   1 
ATOM   2823 C  CB  . ASP A 1 394 ? 24.206 29.344 93.627  1.00 21.82 ? 396  ASP A CB  1 
ATOM   2824 C  CG  . ASP A 1 394 ? 22.983 28.713 94.273  1.00 23.20 ? 396  ASP A CG  1 
ATOM   2825 O  OD1 . ASP A 1 394 ? 23.164 27.756 95.055  1.00 22.66 ? 396  ASP A OD1 1 
ATOM   2826 O  OD2 . ASP A 1 394 ? 21.853 29.214 94.017  1.00 26.04 ? 396  ASP A OD2 1 
ATOM   2827 N  N   . ILE A 1 395 ? 27.130 28.631 92.223  1.00 17.50 ? 397  ILE A N   1 
ATOM   2828 C  CA  . ILE A 1 395 ? 28.212 29.106 91.365  1.00 17.19 ? 397  ILE A CA  1 
ATOM   2829 C  C   . ILE A 1 395 ? 27.650 29.455 89.993  1.00 17.68 ? 397  ILE A C   1 
ATOM   2830 O  O   . ILE A 1 395 ? 27.173 28.570 89.305  1.00 16.74 ? 397  ILE A O   1 
ATOM   2831 C  CB  . ILE A 1 395 ? 29.327 28.052 91.253  1.00 15.66 ? 397  ILE A CB  1 
ATOM   2832 C  CG1 . ILE A 1 395 ? 29.939 27.755 92.626  1.00 15.37 ? 397  ILE A CG1 1 
ATOM   2833 C  CG2 . ILE A 1 395 ? 30.386 28.488 90.255  1.00 15.68 ? 397  ILE A CG2 1 
ATOM   2834 C  CD1 . ILE A 1 395 ? 30.810 26.518 92.668  1.00 14.50 ? 397  ILE A CD1 1 
ATOM   2835 N  N   . GLU A 1 396 ? 27.747 30.737 89.615  1.00 19.07 ? 398  GLU A N   1 
ATOM   2836 C  CA  . GLU A 1 396 ? 27.442 31.190 88.265  1.00 19.83 ? 398  GLU A CA  1 
ATOM   2837 C  C   . GLU A 1 396 ? 28.740 31.212 87.480  1.00 18.78 ? 398  GLU A C   1 
ATOM   2838 O  O   . GLU A 1 396 ? 29.747 31.711 87.969  1.00 18.58 ? 398  GLU A O   1 
ATOM   2839 C  CB  . GLU A 1 396 ? 26.791 32.576 88.271  1.00 22.18 ? 398  GLU A CB  1 
ATOM   2840 C  CG  . GLU A 1 396 ? 25.541 32.634 89.143  1.00 24.09 ? 398  GLU A CG  1 
ATOM   2841 C  CD  . GLU A 1 396 ? 24.811 33.969 89.144  1.00 27.33 ? 398  GLU A CD  1 
ATOM   2842 O  OE1 . GLU A 1 396 ? 24.602 34.555 90.216  1.00 29.20 ? 398  GLU A OE1 1 
ATOM   2843 O  OE2 . GLU A 1 396 ? 24.441 34.408 88.065  1.00 29.27 ? 398  GLU A OE2 1 
ATOM   2844 N  N   . PHE A 1 397 ? 28.690 30.676 86.256  1.00 17.83 ? 399  PHE A N   1 
ATOM   2845 C  CA  . PHE A 1 397 ? 29.895 30.560 85.456  1.00 17.32 ? 399  PHE A CA  1 
ATOM   2846 C  C   . PHE A 1 397 ? 29.538 30.636 83.978  1.00 16.99 ? 399  PHE A C   1 
ATOM   2847 O  O   . PHE A 1 397 ? 28.407 30.398 83.577  1.00 16.73 ? 399  PHE A O   1 
ATOM   2848 C  CB  . PHE A 1 397 ? 30.697 29.284 85.753  1.00 15.75 ? 399  PHE A CB  1 
ATOM   2849 C  CG  . PHE A 1 397 ? 30.015 27.980 85.444  1.00 14.98 ? 399  PHE A CG  1 
ATOM   2850 C  CD1 . PHE A 1 397 ? 29.019 27.491 86.278  1.00 14.79 ? 399  PHE A CD1 1 
ATOM   2851 C  CD2 . PHE A 1 397 ? 30.394 27.224 84.337  1.00 14.30 ? 399  PHE A CD2 1 
ATOM   2852 C  CE1 . PHE A 1 397 ? 28.399 26.281 85.996  1.00 14.05 ? 399  PHE A CE1 1 
ATOM   2853 C  CE2 . PHE A 1 397 ? 29.772 26.018 84.054  1.00 13.62 ? 399  PHE A CE2 1 
ATOM   2854 C  CZ  . PHE A 1 397 ? 28.785 25.540 84.891  1.00 13.66 ? 399  PHE A CZ  1 
ATOM   2855 N  N   . THR A 1 398 ? 30.549 30.963 83.188  1.00 17.25 ? 400  THR A N   1 
ATOM   2856 C  CA  . THR A 1 398 ? 30.383 31.126 81.757  1.00 17.72 ? 400  THR A CA  1 
ATOM   2857 C  C   . THR A 1 398 ? 31.410 30.258 81.049  1.00 17.29 ? 400  THR A C   1 
ATOM   2858 O  O   . THR A 1 398 ? 32.586 30.307 81.377  1.00 17.26 ? 400  THR A O   1 
ATOM   2859 C  CB  . THR A 1 398 ? 30.535 32.604 81.378  1.00 19.52 ? 400  THR A CB  1 
ATOM   2860 O  OG1 . THR A 1 398 ? 29.477 33.343 81.996  1.00 20.01 ? 400  THR A OG1 1 
ATOM   2861 C  CG2 . THR A 1 398 ? 30.488 32.848 79.886  1.00 19.88 ? 400  THR A CG2 1 
ATOM   2862 N  N   . ILE A 1 399 ? 30.944 29.512 80.042  1.00 17.50 ? 401  ILE A N   1 
ATOM   2863 C  CA  . ILE A 1 399 ? 31.817 28.757 79.156  1.00 17.18 ? 401  ILE A CA  1 
ATOM   2864 C  C   . ILE A 1 399 ? 31.848 29.517 77.836  1.00 18.23 ? 401  ILE A C   1 
ATOM   2865 O  O   . ILE A 1 399 ? 30.808 29.927 77.358  1.00 18.67 ? 401  ILE A O   1 
ATOM   2866 C  CB  . ILE A 1 399 ? 31.307 27.309 78.982  1.00 15.92 ? 401  ILE A CB  1 
ATOM   2867 C  CG1 . ILE A 1 399 ? 31.274 26.544 80.311  1.00 15.24 ? 401  ILE A CG1 1 
ATOM   2868 C  CG2 . ILE A 1 399 ? 32.135 26.556 77.968  1.00 15.69 ? 401  ILE A CG2 1 
ATOM   2869 C  CD1 . ILE A 1 399 ? 30.544 25.226 80.225  1.00 14.47 ? 401  ILE A CD1 1 
ATOM   2870 N  N   . THR A 1 400 ? 33.044 29.748 77.306  1.00 19.53 ? 402  THR A N   1 
ATOM   2871 C  CA  . THR A 1 400 ? 33.197 30.337 75.986  1.00 21.78 ? 402  THR A CA  1 
ATOM   2872 C  C   . THR A 1 400 ? 33.835 29.321 75.031  1.00 21.58 ? 402  THR A C   1 
ATOM   2873 O  O   . THR A 1 400 ? 34.654 28.498 75.429  1.00 21.37 ? 402  THR A O   1 
ATOM   2874 C  CB  . THR A 1 400 ? 34.014 31.633 76.046  1.00 24.10 ? 402  THR A CB  1 
ATOM   2875 O  OG1 . THR A 1 400 ? 35.342 31.286 76.439  1.00 25.69 ? 402  THR A OG1 1 
ATOM   2876 C  CG2 . THR A 1 400 ? 33.442 32.644 77.020  1.00 24.97 ? 402  THR A CG2 1 
ATOM   2877 N  N   . SER A 1 401 ? 33.454 29.404 73.758  1.00 21.12 ? 403  SER A N   1 
ATOM   2878 C  CA  . SER A 1 401 ? 34.070 28.620 72.697  1.00 22.00 ? 403  SER A CA  1 
ATOM   2879 C  C   . SER A 1 401 ? 34.519 29.583 71.613  1.00 22.67 ? 403  SER A C   1 
ATOM   2880 O  O   . SER A 1 401 ? 33.713 30.406 71.214  1.00 23.53 ? 403  SER A O   1 
ATOM   2881 C  CB  . SER A 1 401 ? 33.103 27.609 72.107  1.00 21.10 ? 403  SER A CB  1 
ATOM   2882 O  OG  . SER A 1 401 ? 32.698 26.699 73.106  1.00 22.10 ? 403  SER A OG  1 
ATOM   2883 N  N   . THR A 1 402 ? 35.774 29.473 71.168  1.00 23.23 ? 404  THR A N   1 
ATOM   2884 C  CA  . THR A 1 402 ? 36.235 30.223 70.013  1.00 24.57 ? 404  THR A CA  1 
ATOM   2885 C  C   . THR A 1 402 ? 36.427 29.271 68.840  1.00 23.87 ? 404  THR A C   1 
ATOM   2886 O  O   . THR A 1 402 ? 37.273 28.377 68.875  1.00 22.95 ? 404  THR A O   1 
ATOM   2887 C  CB  . THR A 1 402 ? 37.542 30.972 70.290  1.00 26.20 ? 404  THR A CB  1 
ATOM   2888 O  OG1 . THR A 1 402 ? 37.389 31.545 71.579  1.00 26.61 ? 404  THR A OG1 1 
ATOM   2889 C  CG2 . THR A 1 402 ? 37.848 32.049 69.271  1.00 27.89 ? 404  THR A CG2 1 
ATOM   2890 N  N   . ILE A 1 403 ? 35.652 29.517 67.789  1.00 24.18 ? 405  ILE A N   1 
ATOM   2891 C  CA  . ILE A 1 403 ? 35.708 28.736 66.562  1.00 24.55 ? 405  ILE A CA  1 
ATOM   2892 C  C   . ILE A 1 403 ? 36.134 29.675 65.434  1.00 25.95 ? 405  ILE A C   1 
ATOM   2893 O  O   . ILE A 1 403 ? 35.446 30.653 65.185  1.00 26.88 ? 405  ILE A O   1 
ATOM   2894 C  CB  . ILE A 1 403 ? 34.335 28.071 66.321  1.00 23.40 ? 405  ILE A CB  1 
ATOM   2895 C  CG1 . ILE A 1 403 ? 34.005 27.082 67.441  1.00 22.05 ? 405  ILE A CG1 1 
ATOM   2896 C  CG2 . ILE A 1 403 ? 34.273 27.426 64.934  1.00 23.81 ? 405  ILE A CG2 1 
ATOM   2897 C  CD1 . ILE A 1 403 ? 32.592 26.542 67.420  1.00 21.42 ? 405  ILE A CD1 1 
ATOM   2898 N  N   . ASP A 1 404 ? 37.265 29.385 64.768  1.00 27.31 ? 406  ASP A N   1 
ATOM   2899 C  CA  . ASP A 1 404 ? 37.839 30.271 63.755  1.00 29.94 ? 406  ASP A CA  1 
ATOM   2900 C  C   . ASP A 1 404 ? 37.045 30.145 62.457  1.00 29.88 ? 406  ASP A C   1 
ATOM   2901 O  O   . ASP A 1 404 ? 36.070 29.392 62.407  1.00 28.83 ? 406  ASP A O   1 
ATOM   2902 C  CB  . ASP A 1 404 ? 39.337 30.006 63.527  1.00 31.84 ? 406  ASP A CB  1 
ATOM   2903 C  CG  . ASP A 1 404 ? 39.694 28.657 62.915  1.00 33.15 ? 406  ASP A CG  1 
ATOM   2904 O  OD1 . ASP A 1 404 ? 38.767 27.856 62.616  1.00 33.93 ? 406  ASP A OD1 1 
ATOM   2905 O  OD2 . ASP A 1 404 ? 40.911 28.391 62.780  1.00 34.72 ? 406  ASP A OD2 1 
ATOM   2906 N  N   . SER A 1 405 ? 37.469 30.890 61.424  1.00 31.53 ? 407  SER A N   1 
ATOM   2907 C  CA  . SER A 1 405 ? 36.764 30.930 60.149  1.00 32.02 ? 407  SER A CA  1 
ATOM   2908 C  C   . SER A 1 405 ? 36.725 29.567 59.447  1.00 31.83 ? 407  SER A C   1 
ATOM   2909 O  O   . SER A 1 405 ? 35.817 29.302 58.660  1.00 32.84 ? 407  SER A O   1 
ATOM   2910 C  CB  . SER A 1 405 ? 37.355 31.996 59.247  1.00 34.12 ? 407  SER A CB  1 
ATOM   2911 O  OG  . SER A 1 405 ? 38.692 31.694 58.864  1.00 35.12 ? 407  SER A OG  1 
ATOM   2912 N  N   . THR A 1 406 ? 37.738 28.724 59.669  1.00 31.09 ? 408  THR A N   1 
ATOM   2913 C  CA  . THR A 1 406 ? 37.810 27.399 59.067  1.00 31.05 ? 408  THR A CA  1 
ATOM   2914 C  C   . THR A 1 406 ? 36.902 26.398 59.788  1.00 29.21 ? 408  THR A C   1 
ATOM   2915 O  O   . THR A 1 406 ? 36.759 25.267 59.344  1.00 29.27 ? 408  THR A O   1 
ATOM   2916 C  CB  . THR A 1 406 ? 39.251 26.875 59.080  1.00 32.27 ? 408  THR A CB  1 
ATOM   2917 O  OG1 . THR A 1 406 ? 39.685 26.697 60.428  1.00 32.22 ? 408  THR A OG1 1 
ATOM   2918 C  CG2 . THR A 1 406 ? 40.210 27.810 58.380  1.00 34.50 ? 408  THR A CG2 1 
ATOM   2919 N  N   . GLY A 1 407 ? 36.315 26.799 60.915  1.00 27.89 ? 409  GLY A N   1 
ATOM   2920 C  CA  . GLY A 1 407 ? 35.458 25.926 61.706  1.00 26.22 ? 409  GLY A CA  1 
ATOM   2921 C  C   . GLY A 1 407 ? 36.221 25.122 62.760  1.00 25.17 ? 409  GLY A C   1 
ATOM   2922 O  O   . GLY A 1 407 ? 35.652 24.201 63.357  1.00 23.66 ? 409  GLY A O   1 
ATOM   2923 N  N   . ALA A 1 408 ? 37.498 25.473 62.987  1.00 25.99 ? 410  ALA A N   1 
ATOM   2924 C  CA  . ALA A 1 408 ? 38.313 24.783 63.977  1.00 26.08 ? 410  ALA A CA  1 
ATOM   2925 C  C   . ALA A 1 408 ? 38.082 25.393 65.353  1.00 25.01 ? 410  ALA A C   1 
ATOM   2926 O  O   . ALA A 1 408 ? 38.110 26.613 65.493  1.00 25.57 ? 410  ALA A O   1 
ATOM   2927 C  CB  . ALA A 1 408 ? 39.769 24.855 63.588  1.00 27.78 ? 410  ALA A CB  1 
ATOM   2928 N  N   . LEU A 1 409 ? 37.908 24.537 66.371  1.00 23.67 ? 411  LEU A N   1 
ATOM   2929 C  CA  . LEU A 1 409 ? 37.838 24.994 67.746  1.00 22.84 ? 411  LEU A CA  1 
ATOM   2930 C  C   . LEU A 1 409 ? 39.238 25.360 68.240  1.00 23.95 ? 411  LEU A C   1 
ATOM   2931 O  O   . LEU A 1 409 ? 40.115 24.502 68.334  1.00 24.36 ? 411  LEU A O   1 
ATOM   2932 C  CB  . LEU A 1 409 ? 37.197 23.896 68.595  1.00 21.31 ? 411  LEU A CB  1 
ATOM   2933 C  CG  . LEU A 1 409 ? 37.036 24.206 70.087  1.00 20.53 ? 411  LEU A CG  1 
ATOM   2934 C  CD1 . LEU A 1 409 ? 35.975 25.285 70.332  1.00 20.21 ? 411  LEU A CD1 1 
ATOM   2935 C  CD2 . LEU A 1 409 ? 36.702 22.938 70.864  1.00 19.34 ? 411  LEU A CD2 1 
ATOM   2936 N  N   . THR A 1 410 ? 39.438 26.652 68.543  1.00 24.54 ? 412  THR A N   1 
ATOM   2937 C  CA  . THR A 1 410 ? 40.762 27.183 68.841  1.00 26.29 ? 412  THR A CA  1 
ATOM   2938 C  C   . THR A 1 410 ? 40.954 27.338 70.346  1.00 26.73 ? 412  THR A C   1 
ATOM   2939 O  O   . THR A 1 410 ? 42.065 27.186 70.850  1.00 28.38 ? 412  THR A O   1 
ATOM   2940 C  CB  . THR A 1 410 ? 41.031 28.516 68.118  1.00 27.13 ? 412  THR A CB  1 
ATOM   2941 O  OG1 . THR A 1 410 ? 40.021 29.447 68.510  1.00 26.12 ? 412  THR A OG1 1 
ATOM   2942 C  CG2 . THR A 1 410 ? 41.059 28.349 66.617  1.00 27.89 ? 412  THR A CG2 1 
ATOM   2943 N  N   . ASP A 1 411 ? 39.880 27.665 71.065  1.00 25.69 ? 413  ASP A N   1 
ATOM   2944 C  CA  . ASP A 1 411 ? 40.006 27.937 72.485  1.00 25.87 ? 413  ASP A CA  1 
ATOM   2945 C  C   . ASP A 1 411 ? 38.678 27.649 73.171  1.00 23.87 ? 413  ASP A C   1 
ATOM   2946 O  O   . ASP A 1 411 ? 37.616 27.684 72.549  1.00 22.88 ? 413  ASP A O   1 
ATOM   2947 C  CB  . ASP A 1 411 ? 40.433 29.384 72.745  1.00 27.85 ? 413  ASP A CB  1 
ATOM   2948 C  CG  . ASP A 1 411 ? 41.037 29.597 74.120  1.00 29.53 ? 413  ASP A CG  1 
ATOM   2949 O  OD1 . ASP A 1 411 ? 41.198 28.599 74.861  1.00 28.42 ? 413  ASP A OD1 1 
ATOM   2950 O  OD2 . ASP A 1 411 ? 41.332 30.760 74.446  1.00 32.67 ? 413  ASP A OD2 1 
ATOM   2951 N  N   . MET A 1 412 ? 38.770 27.353 74.471  1.00 22.82 ? 414  MET A N   1 
ATOM   2952 C  CA  . MET A 1 412 ? 37.610 27.246 75.327  1.00 21.53 ? 414  MET A CA  1 
ATOM   2953 C  C   . MET A 1 412 ? 38.034 27.677 76.732  1.00 20.83 ? 414  MET A C   1 
ATOM   2954 O  O   . MET A 1 412 ? 39.113 27.311 77.177  1.00 21.55 ? 414  MET A O   1 
ATOM   2955 C  CB  . MET A 1 412 ? 37.086 25.804 75.315  1.00 20.51 ? 414  MET A CB  1 
ATOM   2956 C  CG  . MET A 1 412 ? 35.965 25.559 76.300  1.00 20.68 ? 414  MET A CG  1 
ATOM   2957 S  SD  . MET A 1 412 ? 36.512 25.138 77.984  1.00 21.24 ? 414  MET A SD  1 
ATOM   2958 C  CE  . MET A 1 412 ? 37.336 23.573 77.664  1.00 20.79 ? 414  MET A CE  1 
ATOM   2959 N  N   . THR A 1 413 ? 37.170 28.428 77.423  1.00 19.97 ? 415  THR A N   1 
ATOM   2960 C  CA  . THR A 1 413 ? 37.413 28.838 78.796  1.00 19.87 ? 415  THR A CA  1 
ATOM   2961 C  C   . THR A 1 413 ? 36.181 28.552 79.648  1.00 18.82 ? 415  THR A C   1 
ATOM   2962 O  O   . THR A 1 413 ? 35.069 28.424 79.137  1.00 19.09 ? 415  THR A O   1 
ATOM   2963 C  CB  . THR A 1 413 ? 37.768 30.329 78.897  1.00 21.30 ? 415  THR A CB  1 
ATOM   2964 O  OG1 . THR A 1 413 ? 36.584 31.100 78.700  1.00 21.60 ? 415  THR A OG1 1 
ATOM   2965 C  CG2 . THR A 1 413 ? 38.821 30.741 77.896  1.00 22.62 ? 415  THR A CG2 1 
ATOM   2966 N  N   . SER A 1 414 ? 36.405 28.464 80.960  1.00 18.58 ? 416  SER A N   1 
ATOM   2967 C  CA  . SER A 1 414 ? 35.339 28.347 81.935  1.00 17.91 ? 416  SER A CA  1 
ATOM   2968 C  C   . SER A 1 414 ? 35.729 29.190 83.148  1.00 18.22 ? 416  SER A C   1 
ATOM   2969 O  O   . SER A 1 414 ? 36.766 28.930 83.729  1.00 18.45 ? 416  SER A O   1 
ATOM   2970 C  CB  . SER A 1 414 ? 35.098 26.917 82.322  1.00 16.74 ? 416  SER A CB  1 
ATOM   2971 O  OG  . SER A 1 414 ? 33.955 26.788 83.165  1.00 16.78 ? 416  SER A OG  1 
ATOM   2972 N  N   . THR A 1 415 ? 34.907 30.192 83.475  1.00 18.99 ? 417  THR A N   1 
ATOM   2973 C  CA  . THR A 1 415 ? 35.247 31.178 84.489  1.00 20.89 ? 417  THR A CA  1 
ATOM   2974 C  C   . THR A 1 415 ? 34.022 31.552 85.327  1.00 20.90 ? 417  THR A C   1 
ATOM   2975 O  O   . THR A 1 415 ? 32.888 31.523 84.851  1.00 20.38 ? 417  THR A O   1 
ATOM   2976 C  CB  . THR A 1 415 ? 35.855 32.428 83.843  1.00 22.86 ? 417  THR A CB  1 
ATOM   2977 O  OG1 . THR A 1 415 ? 34.863 32.967 82.963  1.00 23.46 ? 417  THR A OG1 1 
ATOM   2978 C  CG2 . THR A 1 415 ? 37.131 32.148 83.072  1.00 23.64 ? 417  THR A CG2 1 
ATOM   2979 N  N   . SER A 1 416 ? 34.289 32.009 86.561  1.00 21.32 ? 418  SER A N   1 
ATOM   2980 C  CA  . SER A 1 416 ? 33.260 32.416 87.502  1.00 21.45 ? 418  SER A CA  1 
ATOM   2981 C  C   . SER A 1 416 ? 33.846 33.502 88.392  1.00 22.74 ? 418  SER A C   1 
ATOM   2982 O  O   . SER A 1 416 ? 35.073 33.583 88.538  1.00 22.63 ? 418  SER A O   1 
ATOM   2983 C  CB  . SER A 1 416 ? 32.781 31.246 88.337  1.00 20.22 ? 418  SER A CB  1 
ATOM   2984 O  OG  . SER A 1 416 ? 31.906 31.675 89.383  1.00 20.77 ? 418  SER A OG  1 
ATOM   2985 N  N   . ALA A 1 417 ? 32.961 34.305 88.989  1.00 23.82 ? 419  ALA A N   1 
ATOM   2986 C  CA  . ALA A 1 417 ? 33.402 35.321 89.937  1.00 26.23 ? 419  ALA A CA  1 
ATOM   2987 C  C   . ALA A 1 417 ? 33.705 34.685 91.295  1.00 26.26 ? 419  ALA A C   1 
ATOM   2988 O  O   . ALA A 1 417 ? 34.340 35.314 92.134  1.00 28.09 ? 419  ALA A O   1 
ATOM   2989 C  CB  . ALA A 1 417 ? 32.370 36.417 90.069  1.00 27.70 ? 419  ALA A CB  1 
ATOM   2990 N  N   . THR A 1 418 ? 33.262 33.440 91.519  1.00 24.92 ? 420  THR A N   1 
ATOM   2991 C  CA  . THR A 1 418 ? 33.344 32.844 92.841  1.00 24.91 ? 420  THR A CA  1 
ATOM   2992 C  C   . THR A 1 418 ? 33.967 31.447 92.824  1.00 23.51 ? 420  THR A C   1 
ATOM   2993 O  O   . THR A 1 418 ? 33.852 30.735 93.820  1.00 22.76 ? 420  THR A O   1 
ATOM   2994 C  CB  . THR A 1 418 ? 31.949 32.793 93.483  1.00 25.11 ? 420  THR A CB  1 
ATOM   2995 O  OG1 . THR A 1 418 ? 31.132 31.925 92.692  1.00 23.08 ? 420  THR A OG1 1 
ATOM   2996 C  CG2 . THR A 1 418 ? 31.310 34.160 93.630  1.00 27.39 ? 420  THR A CG2 1 
ATOM   2997 N  N   . ALA A 1 419 ? 34.642 31.063 91.726  1.00 23.13 ? 421  ALA A N   1 
ATOM   2998 C  CA  . ALA A 1 419 ? 35.196 29.725 91.579  1.00 21.76 ? 421  ALA A CA  1 
ATOM   2999 C  C   . ALA A 1 419 ? 36.253 29.685 90.478  1.00 21.98 ? 421  ALA A C   1 
ATOM   3000 O  O   . ALA A 1 419 ? 36.304 30.568 89.622  1.00 23.38 ? 421  ALA A O   1 
ATOM   3001 C  CB  . ALA A 1 419 ? 34.097 28.725 91.301  1.00 20.51 ? 421  ALA A CB  1 
ATOM   3002 N  N   . THR A 1 420 ? 37.104 28.657 90.540  1.00 20.77 ? 422  THR A N   1 
ATOM   3003 C  CA  . THR A 1 420 ? 38.159 28.446 89.564  1.00 21.46 ? 422  THR A CA  1 
ATOM   3004 C  C   . THR A 1 420 ? 37.980 27.069 88.927  1.00 20.07 ? 422  THR A C   1 
ATOM   3005 O  O   . THR A 1 420 ? 37.843 26.065 89.625  1.00 18.95 ? 422  THR A O   1 
ATOM   3006 C  CB  . THR A 1 420 ? 39.552 28.528 90.197  1.00 23.23 ? 422  THR A CB  1 
ATOM   3007 O  OG1 . THR A 1 420 ? 39.592 29.750 90.928  1.00 25.47 ? 422  THR A OG1 1 
ATOM   3008 C  CG2 . THR A 1 420 ? 40.682 28.494 89.191  1.00 23.67 ? 422  THR A CG2 1 
ATOM   3009 N  N   . PHE A 1 421 ? 37.988 27.061 87.589  1.00 19.47 ? 423  PHE A N   1 
ATOM   3010 C  CA  . PHE A 1 421 ? 37.927 25.846 86.804  1.00 17.94 ? 423  PHE A CA  1 
ATOM   3011 C  C   . PHE A 1 421 ? 39.294 25.578 86.205  1.00 19.62 ? 423  PHE A C   1 
ATOM   3012 O  O   . PHE A 1 421 ? 40.052 26.501 85.965  1.00 21.57 ? 423  PHE A O   1 
ATOM   3013 C  CB  . PHE A 1 421 ? 36.899 25.977 85.683  1.00 16.79 ? 423  PHE A CB  1 
ATOM   3014 C  CG  . PHE A 1 421 ? 35.483 26.184 86.144  1.00 15.27 ? 423  PHE A CG  1 
ATOM   3015 C  CD1 . PHE A 1 421 ? 35.033 27.447 86.482  1.00 15.41 ? 423  PHE A CD1 1 
ATOM   3016 C  CD2 . PHE A 1 421 ? 34.589 25.124 86.184  1.00 14.05 ? 423  PHE A CD2 1 
ATOM   3017 C  CE1 . PHE A 1 421 ? 33.724 27.638 86.898  1.00 15.21 ? 423  PHE A CE1 1 
ATOM   3018 C  CE2 . PHE A 1 421 ? 33.283 25.317 86.612  1.00 13.79 ? 423  PHE A CE2 1 
ATOM   3019 C  CZ  . PHE A 1 421 ? 32.856 26.574 86.975  1.00 14.43 ? 423  PHE A CZ  1 
ATOM   3020 N  N   . GLU A 1 422 ? 39.586 24.305 85.973  1.00 19.78 ? 424  GLU A N   1 
ATOM   3021 C  CA  . GLU A 1 422 ? 40.700 23.902 85.141  1.00 21.49 ? 424  GLU A CA  1 
ATOM   3022 C  C   . GLU A 1 422 ? 40.133 23.338 83.839  1.00 19.78 ? 424  GLU A C   1 
ATOM   3023 O  O   . GLU A 1 422 ? 39.205 22.545 83.878  1.00 17.99 ? 424  GLU A O   1 
ATOM   3024 C  CB  . GLU A 1 422 ? 41.499 22.823 85.860  1.00 24.25 ? 424  GLU A CB  1 
ATOM   3025 C  CG  . GLU A 1 422 ? 42.083 23.278 87.175  1.00 28.65 ? 424  GLU A CG  1 
ATOM   3026 C  CD  . GLU A 1 422 ? 43.077 22.255 87.706  1.00 33.82 ? 424  GLU A CD  1 
ATOM   3027 O  OE1 . GLU A 1 422 ? 42.701 21.066 87.758  1.00 37.88 ? 424  GLU A OE1 1 
ATOM   3028 O  OE2 . GLU A 1 422 ? 44.229 22.633 88.034  1.00 41.02 ? 424  GLU A OE2 1 
ATOM   3029 N  N   . THR A 1 423 ? 40.710 23.732 82.703  1.00 20.54 ? 425  THR A N   1 
ATOM   3030 C  CA  . THR A 1 423 ? 40.192 23.348 81.402  1.00 20.80 ? 425  THR A CA  1 
ATOM   3031 C  C   . THR A 1 423 ? 41.296 22.704 80.573  1.00 22.95 ? 425  THR A C   1 
ATOM   3032 O  O   . THR A 1 423 ? 42.453 23.070 80.687  1.00 24.52 ? 425  THR A O   1 
ATOM   3033 C  CB  . THR A 1 423 ? 39.583 24.537 80.644  1.00 20.30 ? 425  THR A CB  1 
ATOM   3034 O  OG1 . THR A 1 423 ? 40.510 25.613 80.637  1.00 21.69 ? 425  THR A OG1 1 
ATOM   3035 C  CG2 . THR A 1 423 ? 38.301 25.051 81.250  1.00 19.33 ? 425  THR A CG2 1 
ATOM   3036 N  N   . ASP A 1 424 ? 40.896 21.750 79.722  1.00 23.55 ? 426  ASP A N   1 
ATOM   3037 C  CA  . ASP A 1 424 ? 41.735 21.160 78.695  1.00 24.56 ? 426  ASP A CA  1 
ATOM   3038 C  C   . ASP A 1 424 ? 40.947 21.239 77.393  1.00 24.24 ? 426  ASP A C   1 
ATOM   3039 O  O   . ASP A 1 424 ? 40.011 20.471 77.172  1.00 22.69 ? 426  ASP A O   1 
ATOM   3040 C  CB  . ASP A 1 424 ? 42.107 19.733 79.090  1.00 25.33 ? 426  ASP A CB  1 
ATOM   3041 C  CG  . ASP A 1 424 ? 43.096 19.017 78.182  1.00 28.59 ? 426  ASP A CG  1 
ATOM   3042 O  OD1 . ASP A 1 424 ? 43.472 19.572 77.130  1.00 29.44 ? 426  ASP A OD1 1 
ATOM   3043 O  OD2 . ASP A 1 424 ? 43.486 17.877 78.557  1.00 30.73 ? 426  ASP A OD2 1 
ATOM   3044 N  N   . VAL A 1 425 ? 41.334 22.189 76.542  1.00 25.79 ? 427  VAL A N   1 
ATOM   3045 C  CA  . VAL A 1 425 ? 40.600 22.481 75.321  1.00 25.98 ? 427  VAL A CA  1 
ATOM   3046 C  C   . VAL A 1 425 ? 40.654 21.298 74.353  1.00 24.98 ? 427  VAL A C   1 
ATOM   3047 O  O   . VAL A 1 425 ? 39.649 20.980 73.726  1.00 24.88 ? 427  VAL A O   1 
ATOM   3048 C  CB  . VAL A 1 425 ? 41.133 23.763 74.660  1.00 28.12 ? 427  VAL A CB  1 
ATOM   3049 C  CG1 . VAL A 1 425 ? 40.389 24.076 73.378  1.00 27.95 ? 427  VAL A CG1 1 
ATOM   3050 C  CG2 . VAL A 1 425 ? 41.077 24.933 75.631  1.00 29.33 ? 427  VAL A CG2 1 
ATOM   3051 N  N   . ASN A 1 426 ? 41.824 20.666 74.223  1.00 25.78 ? 428  ASN A N   1 
ATOM   3052 C  CA  . ASN A 1 426 ? 42.020 19.555 73.307  1.00 26.90 ? 428  ASN A CA  1 
ATOM   3053 C  C   . ASN A 1 426 ? 41.132 18.382 73.702  1.00 25.09 ? 428  ASN A C   1 
ATOM   3054 O  O   . ASN A 1 426 ? 40.478 17.806 72.851  1.00 24.47 ? 428  ASN A O   1 
ATOM   3055 C  CB  . ASN A 1 426 ? 43.478 19.104 73.252  1.00 30.05 ? 428  ASN A CB  1 
ATOM   3056 C  CG  . ASN A 1 426 ? 44.379 20.107 72.565  1.00 34.64 ? 428  ASN A CG  1 
ATOM   3057 O  OD1 . ASN A 1 426 ? 43.982 21.238 72.289  1.00 35.37 ? 428  ASN A OD1 1 
ATOM   3058 N  ND2 . ASN A 1 426 ? 45.593 19.688 72.248  1.00 38.10 ? 428  ASN A ND2 1 
ATOM   3059 N  N   . ARG A 1 427 ? 41.108 18.023 74.986  1.00 24.11 ? 429  ARG A N   1 
ATOM   3060 C  CA  . ARG A 1 427 ? 40.314 16.892 75.439  1.00 24.15 ? 429  ARG A CA  1 
ATOM   3061 C  C   . ARG A 1 427 ? 38.868 17.303 75.719  1.00 20.97 ? 429  ARG A C   1 
ATOM   3062 O  O   . ARG A 1 427 ? 38.011 16.442 75.919  1.00 20.36 ? 429  ARG A O   1 
ATOM   3063 C  CB  . ARG A 1 427 ? 40.953 16.294 76.693  1.00 26.97 ? 429  ARG A CB  1 
ATOM   3064 C  CG  . ARG A 1 427 ? 42.314 15.674 76.428  1.00 32.61 ? 429  ARG A CG  1 
ATOM   3065 C  CD  . ARG A 1 427 ? 42.693 14.693 77.527  1.00 37.87 ? 429  ARG A CD  1 
ATOM   3066 N  NE  . ARG A 1 427 ? 44.011 14.124 77.280  1.00 44.56 ? 429  ARG A NE  1 
ATOM   3067 C  CZ  . ARG A 1 427 ? 45.157 14.790 77.399  1.00 49.05 ? 429  ARG A CZ  1 
ATOM   3068 N  NH1 . ARG A 1 427 ? 45.174 16.000 77.931  1.00 48.99 ? 429  ARG A NH1 1 
ATOM   3069 N  NH2 . ARG A 1 427 ? 46.293 14.229 77.019  1.00 52.80 ? 429  ARG A NH2 1 
ATOM   3070 N  N   . GLY A 1 428 ? 38.617 18.614 75.795  1.00 19.45 ? 430  GLY A N   1 
ATOM   3071 C  CA  . GLY A 1 428 ? 37.290 19.145 76.038  1.00 17.98 ? 430  GLY A CA  1 
ATOM   3072 C  C   . GLY A 1 428 ? 36.842 18.913 77.476  1.00 16.98 ? 430  GLY A C   1 
ATOM   3073 O  O   . GLY A 1 428 ? 35.671 18.616 77.701  1.00 15.70 ? 430  GLY A O   1 
ATOM   3074 N  N   . TYR A 1 429 ? 37.770 19.065 78.437  1.00 17.11 ? 431  TYR A N   1 
ATOM   3075 C  CA  . TYR A 1 429 ? 37.472 18.892 79.851  1.00 16.42 ? 431  TYR A CA  1 
ATOM   3076 C  C   . TYR A 1 429 ? 37.335 20.244 80.541  1.00 15.44 ? 431  TYR A C   1 
ATOM   3077 O  O   . TYR A 1 429 ? 38.105 21.163 80.300  1.00 16.46 ? 431  TYR A O   1 
ATOM   3078 C  CB  . TYR A 1 429 ? 38.595 18.152 80.582  1.00 17.79 ? 431  TYR A CB  1 
ATOM   3079 C  CG  . TYR A 1 429 ? 38.821 16.710 80.177  1.00 19.46 ? 431  TYR A CG  1 
ATOM   3080 C  CD1 . TYR A 1 429 ? 37.856 16.003 79.459  1.00 19.36 ? 431  TYR A CD1 1 
ATOM   3081 C  CD2 . TYR A 1 429 ? 40.011 16.065 80.493  1.00 21.21 ? 431  TYR A CD2 1 
ATOM   3082 C  CE1 . TYR A 1 429 ? 38.055 14.681 79.105  1.00 20.71 ? 431  TYR A CE1 1 
ATOM   3083 C  CE2 . TYR A 1 429 ? 40.224 14.744 80.135  1.00 22.57 ? 431  TYR A CE2 1 
ATOM   3084 C  CZ  . TYR A 1 429 ? 39.246 14.062 79.430  1.00 21.99 ? 431  TYR A CZ  1 
ATOM   3085 O  OH  . TYR A 1 429 ? 39.410 12.768 79.083  1.00 23.79 ? 431  TYR A OH  1 
ATOM   3086 N  N   . ILE A 1 430 ? 36.319 20.361 81.379  1.00 13.84 ? 432  ILE A N   1 
ATOM   3087 C  CA  . ILE A 1 430 ? 36.177 21.454 82.321  1.00 13.85 ? 432  ILE A CA  1 
ATOM   3088 C  C   . ILE A 1 430 ? 36.041 20.807 83.695  1.00 13.40 ? 432  ILE A C   1 
ATOM   3089 O  O   . ILE A 1 430 ? 35.104 20.021 83.916  1.00 12.39 ? 432  ILE A O   1 
ATOM   3090 C  CB  . ILE A 1 430 ? 34.925 22.288 81.993  1.00 13.61 ? 432  ILE A CB  1 
ATOM   3091 C  CG1 . ILE A 1 430 ? 34.952 22.837 80.567  1.00 14.52 ? 432  ILE A CG1 1 
ATOM   3092 C  CG2 . ILE A 1 430 ? 34.707 23.379 83.028  1.00 13.79 ? 432  ILE A CG2 1 
ATOM   3093 C  CD1 . ILE A 1 430 ? 33.588 23.304 80.085  1.00 14.53 ? 432  ILE A CD1 1 
ATOM   3094 N  N   . ASN A 1 431 ? 36.974 21.141 84.600  1.00 14.07 ? 433  ASN A N   1 
ATOM   3095 C  CA  . ASN A 1 431 ? 37.055 20.469 85.892  1.00 14.45 ? 433  ASN A CA  1 
ATOM   3096 C  C   . ASN A 1 431 ? 36.897 21.492 87.009  1.00 13.59 ? 433  ASN A C   1 
ATOM   3097 O  O   . ASN A 1 431 ? 37.521 22.544 86.954  1.00 13.67 ? 433  ASN A O   1 
ATOM   3098 C  CB  . ASN A 1 431 ? 38.360 19.691 86.048  1.00 16.75 ? 433  ASN A CB  1 
ATOM   3099 C  CG  . ASN A 1 431 ? 38.555 18.635 84.978  1.00 20.31 ? 433  ASN A CG  1 
ATOM   3100 O  OD1 . ASN A 1 431 ? 37.711 17.771 84.766  1.00 21.06 ? 433  ASN A OD1 1 
ATOM   3101 N  ND2 . ASN A 1 431 ? 39.668 18.704 84.265  1.00 24.22 ? 433  ASN A ND2 1 
ATOM   3102 N  N   . LEU A 1 432 ? 36.024 21.181 87.979  1.00 12.67 ? 434  LEU A N   1 
ATOM   3103 C  CA  . LEU A 1 432 ? 35.822 21.994 89.170  1.00 12.66 ? 434  LEU A CA  1 
ATOM   3104 C  C   . LEU A 1 432 ? 35.938 21.092 90.394  1.00 12.27 ? 434  LEU A C   1 
ATOM   3105 O  O   . LEU A 1 432 ? 35.313 20.040 90.467  1.00 11.29 ? 434  LEU A O   1 
ATOM   3106 C  CB  . LEU A 1 432 ? 34.440 22.664 89.133  1.00 12.33 ? 434  LEU A CB  1 
ATOM   3107 C  CG  . LEU A 1 432 ? 34.043 23.443 90.381  1.00 13.12 ? 434  LEU A CG  1 
ATOM   3108 C  CD1 . LEU A 1 432 ? 34.886 24.700 90.533  1.00 14.25 ? 434  LEU A CD1 1 
ATOM   3109 C  CD2 . LEU A 1 432 ? 32.565 23.809 90.367  1.00 13.35 ? 434  LEU A CD2 1 
ATOM   3110 N  N   . LYS A 1 433 ? 36.753 21.518 91.355  1.00 12.83 ? 435  LYS A N   1 
ATOM   3111 C  CA  A LYS A 1 433 ? 36.861 20.850 92.640  0.50 12.93 ? 435  LYS A CA  1 
ATOM   3112 C  CA  B LYS A 1 433 ? 36.823 20.821 92.626  0.50 13.07 ? 435  LYS A CA  1 
ATOM   3113 C  C   . LYS A 1 433 ? 35.972 21.583 93.643  1.00 13.00 ? 435  LYS A C   1 
ATOM   3114 O  O   . LYS A 1 433 ? 36.220 22.756 93.914  1.00 13.86 ? 435  LYS A O   1 
ATOM   3115 C  CB  A LYS A 1 433 ? 38.328 20.863 93.077  0.50 14.22 ? 435  LYS A CB  1 
ATOM   3116 C  CB  B LYS A 1 433 ? 38.285 20.634 93.034  0.50 14.56 ? 435  LYS A CB  1 
ATOM   3117 C  CG  A LYS A 1 433 ? 38.621 20.256 94.448  0.50 14.54 ? 435  LYS A CG  1 
ATOM   3118 C  CG  B LYS A 1 433 ? 38.500 19.793 94.290  0.50 15.09 ? 435  LYS A CG  1 
ATOM   3119 C  CD  A LYS A 1 433 ? 40.108 20.214 94.780  0.50 16.02 ? 435  LYS A CD  1 
ATOM   3120 C  CD  B LYS A 1 433 ? 39.940 19.320 94.474  0.50 16.65 ? 435  LYS A CD  1 
ATOM   3121 C  CE  A LYS A 1 433 ? 40.607 21.453 95.490  0.50 17.12 ? 435  LYS A CE  1 
ATOM   3122 C  CE  B LYS A 1 433 ? 40.319 18.177 93.559  0.50 17.31 ? 435  LYS A CE  1 
ATOM   3123 N  NZ  A LYS A 1 433 ? 42.070 21.616 95.331  0.50 18.87 ? 435  LYS A NZ  1 
ATOM   3124 N  NZ  B LYS A 1 433 ? 41.734 17.786 93.755  0.50 18.90 ? 435  LYS A NZ  1 
ATOM   3125 N  N   . VAL A 1 434 ? 34.935 20.902 94.171  1.00 11.95 ? 436  VAL A N   1 
ATOM   3126 C  CA  . VAL A 1 434 ? 34.033 21.481 95.152  1.00 12.35 ? 436  VAL A CA  1 
ATOM   3127 C  C   . VAL A 1 434 ? 34.518 21.071 96.536  1.00 12.11 ? 436  VAL A C   1 
ATOM   3128 O  O   . VAL A 1 434 ? 34.495 19.885 96.858  1.00 11.41 ? 436  VAL A O   1 
ATOM   3129 C  CB  . VAL A 1 434 ? 32.599 20.988 94.925  1.00 12.64 ? 436  VAL A CB  1 
ATOM   3130 C  CG1 . VAL A 1 434 ? 31.619 21.590 95.915  1.00 13.63 ? 436  VAL A CG1 1 
ATOM   3131 C  CG2 . VAL A 1 434 ? 32.149 21.252 93.505  1.00 12.99 ? 436  VAL A CG2 1 
ATOM   3132 N  N   . VAL A 1 435 ? 34.974 22.049 97.315  1.00 12.97 ? 437  VAL A N   1 
ATOM   3133 C  CA  . VAL A 1 435 ? 35.569 21.798 98.622  1.00 13.58 ? 437  VAL A CA  1 
ATOM   3134 C  C   . VAL A 1 435 ? 34.500 21.932 99.712  1.00 13.84 ? 437  VAL A C   1 
ATOM   3135 O  O   . VAL A 1 435 ? 33.975 23.001 99.954  1.00 14.27 ? 437  VAL A O   1 
ATOM   3136 C  CB  . VAL A 1 435 ? 36.751 22.750 98.893  1.00 14.64 ? 437  VAL A CB  1 
ATOM   3137 C  CG1 . VAL A 1 435 ? 37.413 22.450 100.236 1.00 15.13 ? 437  VAL A CG1 1 
ATOM   3138 C  CG2 . VAL A 1 435 ? 37.735 22.731 97.728  1.00 14.67 ? 437  VAL A CG2 1 
ATOM   3139 N  N   . ASN A 1 436 ? 34.174 20.818 100.358 1.00 13.95 ? 438  ASN A N   1 
ATOM   3140 C  CA  . ASN A 1 436 ? 33.197 20.779 101.429 1.00 14.59 ? 438  ASN A CA  1 
ATOM   3141 C  C   . ASN A 1 436 ? 33.885 21.164 102.739 1.00 15.09 ? 438  ASN A C   1 
ATOM   3142 O  O   . ASN A 1 436 ? 34.977 20.690 103.011 1.00 14.75 ? 438  ASN A O   1 
ATOM   3143 C  CB  . ASN A 1 436 ? 32.579 19.393 101.589 1.00 14.03 ? 438  ASN A CB  1 
ATOM   3144 C  CG  . ASN A 1 436 ? 31.416 19.158 100.666 1.00 13.85 ? 438  ASN A CG  1 
ATOM   3145 O  OD1 . ASN A 1 436 ? 30.282 19.295 101.078 1.00 15.58 ? 438  ASN A OD1 1 
ATOM   3146 N  N   . LYS A 1 437 ? 33.245 22.022 103.533 1.00 16.43 ? 439  LYS A N   1 
ATOM   3147 C  CA  . LYS A 1 437 ? 33.791 22.444 104.815 1.00 18.21 ? 439  LYS A CA  1 
ATOM   3148 C  C   . LYS A 1 437 ? 32.793 22.165 105.934 1.00 17.74 ? 439  LYS A C   1 
ATOM   3149 O  O   . LYS A 1 437 ? 31.589 22.309 105.768 1.00 17.75 ? 439  LYS A O   1 
ATOM   3150 C  CB  . LYS A 1 437 ? 34.106 23.938 104.814 1.00 21.66 ? 439  LYS A CB  1 
ATOM   3151 C  CG  . LYS A 1 437 ? 34.974 24.427 103.654 1.00 23.89 ? 439  LYS A CG  1 
ATOM   3152 C  CD  . LYS A 1 437 ? 35.564 25.816 103.932 1.00 28.53 ? 439  LYS A CD  1 
ATOM   3153 C  CE  . LYS A 1 437 ? 36.510 26.320 102.860 1.00 31.52 ? 439  LYS A CE  1 
ATOM   3154 N  NZ  . LYS A 1 437 ? 35.784 26.788 101.657 1.00 33.67 ? 439  LYS A NZ  1 
ATOM   3155 N  N   . GLN A 1 438 ? 33.325 21.718 107.071 1.00 17.40 ? 440  GLN A N   1 
ATOM   3156 C  CA  . GLN A 1 438 ? 32.510 21.417 108.231 1.00 17.96 ? 440  GLN A CA  1 
ATOM   3157 C  C   . GLN A 1 438 ? 32.063 22.716 108.911 1.00 18.25 ? 440  GLN A C   1 
ATOM   3158 O  O   . GLN A 1 438 ? 32.630 23.782 108.704 1.00 18.08 ? 440  GLN A O   1 
ATOM   3159 C  CB  . GLN A 1 438 ? 33.288 20.493 109.169 1.00 18.95 ? 440  GLN A CB  1 
ATOM   3160 C  CG  . GLN A 1 438 ? 33.643 19.149 108.524 1.00 18.70 ? 440  GLN A CG  1 
ATOM   3161 C  CD  . GLN A 1 438 ? 34.532 18.316 109.419 1.00 20.19 ? 440  GLN A CD  1 
ATOM   3162 O  OE1 . GLN A 1 438 ? 35.640 17.918 109.063 1.00 22.50 ? 440  GLN A OE1 1 
ATOM   3163 N  NE2 . GLN A 1 438 ? 34.026 18.000 110.586 1.00 19.92 ? 440  GLN A NE2 1 
ATOM   3164 N  N   . GLY A 1 439 ? 31.017 22.606 109.728 1.00 18.50 ? 441  GLY A N   1 
ATOM   3165 C  CA  . GLY A 1 439 ? 30.504 23.736 110.470 1.00 19.41 ? 441  GLY A CA  1 
ATOM   3166 C  C   . GLY A 1 439 ? 31.360 24.015 111.707 1.00 20.10 ? 441  GLY A C   1 
ATOM   3167 O  O   . GLY A 1 439 ? 32.424 23.438 111.891 1.00 19.35 ? 441  GLY A O   1 
ATOM   3168 N  N   . ALA A 1 440 ? 30.835 24.865 112.584 1.00 21.37 ? 442  ALA A N   1 
ATOM   3169 C  CA  . ALA A 1 440 ? 31.560 25.307 113.764 1.00 22.51 ? 442  ALA A CA  1 
ATOM   3170 C  C   . ALA A 1 440 ? 31.036 24.587 114.999 1.00 23.10 ? 442  ALA A C   1 
ATOM   3171 O  O   . ALA A 1 440 ? 29.831 24.486 115.210 1.00 22.77 ? 442  ALA A O   1 
ATOM   3172 C  CB  . ALA A 1 440 ? 31.433 26.805 113.912 1.00 24.14 ? 442  ALA A CB  1 
ATOM   3173 N  N   . LEU A 1 441 ? 31.980 24.080 115.796 1.00 23.77 ? 443  LEU A N   1 
ATOM   3174 C  CA  . LEU A 1 441 ? 31.695 23.591 117.125 1.00 25.51 ? 443  LEU A CA  1 
ATOM   3175 C  C   . LEU A 1 441 ? 31.987 24.743 118.082 1.00 27.39 ? 443  LEU A C   1 
ATOM   3176 O  O   . LEU A 1 441 ? 33.141 25.108 118.258 1.00 27.47 ? 443  LEU A O   1 
ATOM   3177 C  CB  . LEU A 1 441 ? 32.584 22.372 117.404 1.00 25.56 ? 443  LEU A CB  1 
ATOM   3178 C  CG  . LEU A 1 441 ? 32.325 21.655 118.727 1.00 27.23 ? 443  LEU A CG  1 
ATOM   3179 C  CD1 . LEU A 1 441 ? 31.043 20.816 118.654 1.00 27.06 ? 443  LEU A CD1 1 
ATOM   3180 C  CD2 . LEU A 1 441 ? 33.524 20.793 119.104 1.00 27.45 ? 443  LEU A CD2 1 
ATOM   3181 N  N   . LEU A 1 442 ? 30.939 25.324 118.668 1.00 28.97 ? 444  LEU A N   1 
ATOM   3182 C  CA  . LEU A 1 442 ? 31.081 26.446 119.581 1.00 31.93 ? 444  LEU A CA  1 
ATOM   3183 C  C   . LEU A 1 442 ? 30.742 25.983 120.996 1.00 33.68 ? 444  LEU A C   1 
ATOM   3184 O  O   . LEU A 1 442 ? 29.602 26.100 121.403 1.00 34.59 ? 444  LEU A O   1 
ATOM   3185 C  CB  . LEU A 1 442 ? 30.134 27.553 119.112 1.00 32.79 ? 444  LEU A CB  1 
ATOM   3186 C  CG  . LEU A 1 442 ? 30.416 28.099 117.714 1.00 32.26 ? 444  LEU A CG  1 
ATOM   3187 C  CD1 . LEU A 1 442 ? 29.288 28.989 117.221 1.00 33.00 ? 444  LEU A CD1 1 
ATOM   3188 C  CD2 . LEU A 1 442 ? 31.724 28.861 117.701 1.00 33.34 ? 444  LEU A CD2 1 
ATOM   3189 N  N   . PRO A 1 443 ? 31.660 25.360 121.769 1.00 35.74 ? 445  PRO A N   1 
ATOM   3190 C  CA  . PRO A 1 443 ? 31.362 24.980 123.153 1.00 38.07 ? 445  PRO A CA  1 
ATOM   3191 C  C   . PRO A 1 443 ? 31.324 26.208 124.067 1.00 40.73 ? 445  PRO A C   1 
ATOM   3192 O  O   . PRO A 1 443 ? 30.402 26.235 124.833 1.00 44.12 ? 445  PRO A O   1 
ATOM   3193 C  CB  . PRO A 1 443 ? 32.495 24.018 123.560 1.00 37.38 ? 445  PRO A CB  1 
ATOM   3194 C  CG  . PRO A 1 443 ? 33.208 23.695 122.261 1.00 35.14 ? 445  PRO A CG  1 
ATOM   3195 C  CD  . PRO A 1 443 ? 33.002 24.906 121.371 1.00 35.24 ? 445  PRO A CD  1 
HETATM 3196 C  C   . FMT B 2 .   ? 38.446 22.759 7.550   1.00 32.86 ? 801  FMT A C   1 
HETATM 3197 O  O1  . FMT B 2 .   ? 37.269 22.460 7.463   1.00 28.66 ? 801  FMT A O1  1 
HETATM 3198 O  O2  . FMT B 2 .   ? 39.455 21.888 7.823   1.00 36.77 ? 801  FMT A O2  1 
HETATM 3199 C  C   . FMT C 2 .   ? 33.034 23.112 42.055  1.00 28.27 ? 802  FMT A C   1 
HETATM 3200 O  O1  . FMT C 2 .   ? 31.855 23.266 42.316  1.00 26.12 ? 802  FMT A O1  1 
HETATM 3201 O  O2  . FMT C 2 .   ? 33.535 22.155 41.200  1.00 26.37 ? 802  FMT A O2  1 
HETATM 3202 C  C   . ACY D 3 .   ? 34.103 40.226 23.561  1.00 37.48 ? 803  ACY A C   1 
HETATM 3203 O  O   . ACY D 3 .   ? 33.427 39.355 23.023  1.00 35.21 ? 803  ACY A O   1 
HETATM 3204 O  OXT . ACY D 3 .   ? 33.626 41.113 24.264  1.00 44.05 ? 803  ACY A OXT 1 
HETATM 3205 C  CH3 . ACY D 3 .   ? 35.606 40.208 23.352  1.00 38.91 ? 803  ACY A CH3 1 
HETATM 3206 C  C1  . EDO E 4 .   ? 30.217 12.040 51.747  1.00 26.91 ? 804  EDO A C1  1 
HETATM 3207 O  O1  . EDO E 4 .   ? 30.751 11.580 50.533  1.00 23.46 ? 804  EDO A O1  1 
HETATM 3208 C  C2  . EDO E 4 .   ? 30.176 10.989 52.789  1.00 27.76 ? 804  EDO A C2  1 
HETATM 3209 O  O2  . EDO E 4 .   ? 29.539 9.843  52.309  1.00 34.03 ? 804  EDO A O2  1 
HETATM 3210 C  C   . ACY F 3 .   ? 38.956 37.539 22.247  1.00 42.98 ? 805  ACY A C   1 
HETATM 3211 O  O   . ACY F 3 .   ? 38.877 37.449 20.993  1.00 43.30 ? 805  ACY A O   1 
HETATM 3212 O  OXT . ACY F 3 .   ? 38.010 37.921 22.982  1.00 35.54 ? 805  ACY A OXT 1 
HETATM 3213 C  CH3 . ACY F 3 .   ? 40.311 37.212 22.902  1.00 43.53 ? 805  ACY A CH3 1 
HETATM 3214 C  C1  . EDO G 4 .   ? 20.039 35.410 62.851  1.00 38.94 ? 806  EDO A C1  1 
HETATM 3215 O  O1  . EDO G 4 .   ? 21.267 35.999 62.457  1.00 43.58 ? 806  EDO A O1  1 
HETATM 3216 C  C2  . EDO G 4 .   ? 19.854 35.452 64.312  1.00 37.26 ? 806  EDO A C2  1 
HETATM 3217 O  O2  . EDO G 4 .   ? 18.818 34.638 64.812  1.00 35.48 ? 806  EDO A O2  1 
HETATM 3218 C  C1  . EDO H 4 .   ? 7.045  19.733 41.708  1.00 29.68 ? 807  EDO A C1  1 
HETATM 3219 O  O1  . EDO H 4 .   ? 8.248  20.190 41.178  1.00 23.54 ? 807  EDO A O1  1 
HETATM 3220 C  C2  . EDO H 4 .   ? 6.995  19.990 43.161  1.00 30.41 ? 807  EDO A C2  1 
HETATM 3221 O  O2  . EDO H 4 .   ? 7.158  21.364 43.424  1.00 32.88 ? 807  EDO A O2  1 
HETATM 3222 C  C1  . EDO I 4 .   ? 33.438 25.230 96.224  1.00 28.55 ? 808  EDO A C1  1 
HETATM 3223 O  O1  . EDO I 4 .   ? 34.697 24.679 96.585  1.00 26.79 ? 808  EDO A O1  1 
HETATM 3224 C  C2  . EDO I 4 .   ? 33.585 26.344 95.266  1.00 31.34 ? 808  EDO A C2  1 
HETATM 3225 O  O2  . EDO I 4 .   ? 34.407 26.019 94.155  1.00 30.11 ? 808  EDO A O2  1 
HETATM 3226 C  C   . FMT J 2 .   ? 17.442 -0.324 51.083  1.00 33.78 ? 809  FMT A C   1 
HETATM 3227 O  O1  . FMT J 2 .   ? 16.256 -0.180 50.830  1.00 29.55 ? 809  FMT A O1  1 
HETATM 3228 O  O2  . FMT J 2 .   ? 18.150 0.434  51.988  1.00 27.78 ? 809  FMT A O2  1 
HETATM 3229 C  C   . ACT K 5 .   ? 12.418 7.433  43.198  1.00 37.03 ? 810  ACT A C   1 
HETATM 3230 O  O   . ACT K 5 .   ? 13.122 7.683  42.190  1.00 32.76 ? 810  ACT A O   1 
HETATM 3231 O  OXT . ACT K 5 .   ? 12.470 8.086  44.272  1.00 36.85 ? 810  ACT A OXT 1 
HETATM 3232 C  CH3 . ACT K 5 .   ? 11.439 6.258  43.116  1.00 37.17 ? 810  ACT A CH3 1 
HETATM 3233 C  C   . FMT L 2 .   ? 29.511 25.488 40.142  1.00 35.84 ? 811  FMT A C   1 
HETATM 3234 O  O1  . FMT L 2 .   ? 28.448 26.079 40.173  1.00 35.79 ? 811  FMT A O1  1 
HETATM 3235 O  O2  . FMT L 2 .   ? 30.582 25.787 40.926  1.00 37.61 ? 811  FMT A O2  1 
HETATM 3236 NA NA  . NA  M 6 .   ? 34.754 23.263 31.634  1.00 28.11 ? 812  NA  A NA  1 
HETATM 3237 O  O   . HOH N 7 .   ? 35.727 17.052 82.559  1.00 17.51 ? 901  HOH A O   1 
HETATM 3238 O  O   . HOH N 7 .   ? 28.843 21.042 100.510 1.00 20.91 ? 902  HOH A O   1 
HETATM 3239 O  O   . HOH N 7 .   ? 30.065 23.081 55.822  1.00 10.41 ? 903  HOH A O   1 
HETATM 3240 O  O   . HOH N 7 .   ? 13.514 12.836 32.189  1.00 20.64 ? 904  HOH A O   1 
HETATM 3241 O  O   . HOH N 7 .   ? 20.252 26.177 41.458  1.00 13.58 ? 905  HOH A O   1 
HETATM 3242 O  O   . HOH N 7 .   ? 34.909 39.585 5.655   1.00 49.16 ? 906  HOH A O   1 
HETATM 3243 O  O   . HOH N 7 .   ? 21.351 13.757 73.382  1.00 15.46 ? 907  HOH A O   1 
HETATM 3244 O  O   . HOH N 7 .   ? 22.201 4.928  52.367  1.00 16.21 ? 908  HOH A O   1 
HETATM 3245 O  O   . HOH N 7 .   ? 21.983 20.910 99.396  1.00 22.33 ? 909  HOH A O   1 
HETATM 3246 O  O   . HOH N 7 .   ? 21.017 12.608 32.591  1.00 24.76 ? 910  HOH A O   1 
HETATM 3247 O  O   . HOH N 7 .   ? 16.822 29.193 44.262  1.00 25.82 ? 911  HOH A O   1 
HETATM 3248 O  O   . HOH N 7 .   ? 43.999 29.194 26.990  1.00 21.85 ? 912  HOH A O   1 
HETATM 3249 O  O   . HOH N 7 .   ? 17.446 20.464 92.192  1.00 30.26 ? 913  HOH A O   1 
HETATM 3250 O  O   . HOH N 7 .   ? 9.993  25.118 54.578  1.00 33.02 ? 914  HOH A O   1 
HETATM 3251 O  O   . HOH N 7 .   ? 44.551 26.893 34.750  1.00 21.10 ? 915  HOH A O   1 
HETATM 3252 O  O   . HOH N 7 .   ? 29.802 28.434 69.978  1.00 20.67 ? 916  HOH A O   1 
HETATM 3253 O  O   . HOH N 7 .   ? 26.749 -0.109 53.006  1.00 28.84 ? 917  HOH A O   1 
HETATM 3254 O  O   . HOH N 7 .   ? 22.577 2.068  58.827  1.00 14.70 ? 918  HOH A O   1 
HETATM 3255 O  O   . HOH N 7 .   ? 26.033 20.379 34.260  1.00 5.97  ? 919  HOH A O   1 
HETATM 3256 O  O   . HOH N 7 .   ? 27.996 11.647 102.570 1.00 20.57 ? 920  HOH A O   1 
HETATM 3257 O  O   . HOH N 7 .   ? 23.666 12.956 100.962 1.00 16.10 ? 921  HOH A O   1 
HETATM 3258 O  O   . HOH N 7 .   ? 29.417 32.736 91.009  1.00 15.74 ? 922  HOH A O   1 
HETATM 3259 O  O   . HOH N 7 .   ? 41.631 36.543 15.719  1.00 17.11 ? 923  HOH A O   1 
HETATM 3260 O  O   . HOH N 7 .   ? 36.333 21.476 107.174 1.00 12.75 ? 924  HOH A O   1 
HETATM 3261 O  O   . HOH N 7 .   ? 26.912 27.715 72.829  1.00 16.63 ? 925  HOH A O   1 
HETATM 3262 O  O   . HOH N 7 .   ? 29.324 13.133 105.034 1.00 22.23 ? 926  HOH A O   1 
HETATM 3263 O  O   . HOH N 7 .   ? 37.142 31.038 4.544   1.00 23.10 ? 927  HOH A O   1 
HETATM 3264 O  O   . HOH N 7 .   ? 33.125 21.325 30.628  1.00 16.47 ? 928  HOH A O   1 
HETATM 3265 O  O   . HOH N 7 .   ? 44.145 21.990 32.222  1.00 18.76 ? 929  HOH A O   1 
HETATM 3266 O  O   . HOH N 7 .   ? 13.938 29.019 40.132  1.00 27.86 ? 930  HOH A O   1 
HETATM 3267 O  O   . HOH N 7 .   ? 27.273 12.284 2.923   1.00 32.64 ? 931  HOH A O   1 
HETATM 3268 O  O   . HOH N 7 .   ? 25.888 11.094 92.459  1.00 20.94 ? 932  HOH A O   1 
HETATM 3269 O  O   . HOH N 7 .   ? 38.314 13.970 75.242  1.00 23.81 ? 933  HOH A O   1 
HETATM 3270 O  O   . HOH N 7 .   ? 31.440 27.355 33.891  1.00 28.20 ? 934  HOH A O   1 
HETATM 3271 O  O   . HOH N 7 .   ? 26.707 11.808 95.162  1.00 16.67 ? 935  HOH A O   1 
HETATM 3272 O  O   . HOH N 7 .   ? 32.330 14.154 25.328  1.00 14.89 ? 936  HOH A O   1 
HETATM 3273 O  O   . HOH N 7 .   ? 35.794 13.260 21.790  1.00 17.39 ? 937  HOH A O   1 
HETATM 3274 O  O   . HOH N 7 .   ? 33.885 27.861 2.276   1.00 19.78 ? 938  HOH A O   1 
HETATM 3275 O  O   . HOH N 7 .   ? 32.373 11.211 37.164  1.00 27.43 ? 939  HOH A O   1 
HETATM 3276 O  O   . HOH N 7 .   ? 10.153 10.259 42.778  1.00 21.44 ? 940  HOH A O   1 
HETATM 3277 O  O   . HOH N 7 .   ? 30.410 37.658 23.526  1.00 37.19 ? 941  HOH A O   1 
HETATM 3278 O  O   . HOH N 7 .   ? 30.489 11.817 16.040  1.00 19.02 ? 942  HOH A O   1 
HETATM 3279 O  O   . HOH N 7 .   ? 13.109 19.481 37.037  1.00 14.99 ? 943  HOH A O   1 
HETATM 3280 O  O   . HOH N 7 .   ? 31.523 22.894 52.041  1.00 26.61 ? 944  HOH A O   1 
HETATM 3281 O  O   . HOH N 7 .   ? 26.271 42.267 6.721   1.00 29.06 ? 945  HOH A O   1 
HETATM 3282 O  O   . HOH N 7 .   ? 21.955 27.788 38.161  1.00 25.24 ? 946  HOH A O   1 
HETATM 3283 O  O   . HOH N 7 .   ? 17.851 21.850 60.066  1.00 13.32 ? 947  HOH A O   1 
HETATM 3284 O  O   . HOH N 7 .   ? 30.354 37.406 4.768   1.00 15.33 ? 948  HOH A O   1 
HETATM 3285 O  O   . HOH N 7 .   ? 7.912  28.946 51.907  1.00 27.98 ? 949  HOH A O   1 
HETATM 3286 O  O   . HOH N 7 .   ? 23.690 7.598  43.083  1.00 22.10 ? 950  HOH A O   1 
HETATM 3287 O  O   . HOH N 7 .   ? 39.208 16.466 70.875  1.00 17.82 ? 951  HOH A O   1 
HETATM 3288 O  O   . HOH N 7 .   ? 32.989 13.246 47.591  1.00 15.24 ? 952  HOH A O   1 
HETATM 3289 O  O   . HOH N 7 .   ? 33.065 13.899 35.978  1.00 17.58 ? 953  HOH A O   1 
HETATM 3290 O  O   . HOH N 7 .   ? 29.858 13.732 20.397  1.00 26.76 ? 954  HOH A O   1 
HETATM 3291 O  O   . HOH N 7 .   ? 37.136 31.543 87.319  1.00 19.17 ? 955  HOH A O   1 
HETATM 3292 O  O   . HOH N 7 .   ? 38.019 13.129 41.130  1.00 23.08 ? 956  HOH A O   1 
HETATM 3293 O  O   . HOH N 7 .   ? 36.669 28.964 6.340   1.00 15.35 ? 957  HOH A O   1 
HETATM 3294 O  O   . HOH N 7 .   ? 30.043 7.899  70.170  1.00 36.95 ? 958  HOH A O   1 
HETATM 3295 O  O   . HOH N 7 .   ? 34.578 33.093 11.290  1.00 11.80 ? 959  HOH A O   1 
HETATM 3296 O  O   . HOH N 7 .   ? 39.229 21.893 66.061  1.00 17.86 ? 960  HOH A O   1 
HETATM 3297 O  O   . HOH N 7 .   ? 35.099 21.034 43.012  1.00 21.87 ? 961  HOH A O   1 
HETATM 3298 O  O   . HOH N 7 .   ? 38.981 28.516 81.563  1.00 22.91 ? 962  HOH A O   1 
HETATM 3299 O  O   . HOH N 7 .   ? 37.482 17.582 29.113  1.00 14.46 ? 963  HOH A O   1 
HETATM 3300 O  O   . HOH N 7 .   ? 29.730 21.473 46.082  1.00 10.02 ? 964  HOH A O   1 
HETATM 3301 O  O   . HOH N 7 .   ? 44.100 28.026 10.663  1.00 31.18 ? 965  HOH A O   1 
HETATM 3302 O  O   . HOH N 7 .   ? 19.289 25.569 32.369  1.00 19.02 ? 966  HOH A O   1 
HETATM 3303 O  O   . HOH N 7 .   ? 22.865 24.607 54.096  1.00 16.15 ? 967  HOH A O   1 
HETATM 3304 O  O   . HOH N 7 .   ? 28.478 16.704 62.527  1.00 14.98 ? 968  HOH A O   1 
HETATM 3305 O  O   . HOH N 7 .   ? 39.488 23.889 39.372  1.00 37.61 ? 969  HOH A O   1 
HETATM 3306 O  O   . HOH N 7 .   ? 24.829 9.058  46.665  1.00 30.52 ? 970  HOH A O   1 
HETATM 3307 O  O   . HOH N 7 .   ? 27.114 34.043 11.014  1.00 23.49 ? 971  HOH A O   1 
HETATM 3308 O  O   . HOH N 7 .   ? 38.042 24.669 93.506  1.00 27.63 ? 972  HOH A O   1 
HETATM 3309 O  O   . HOH N 7 .   ? 22.551 17.001 71.485  1.00 14.32 ? 973  HOH A O   1 
HETATM 3310 O  O   . HOH N 7 .   ? 24.747 14.036 60.868  1.00 19.32 ? 974  HOH A O   1 
HETATM 3311 O  O   . HOH N 7 .   ? 10.480 9.787  51.006  1.00 26.18 ? 975  HOH A O   1 
HETATM 3312 O  O   . HOH N 7 .   ? 27.717 20.764 32.143  1.00 9.72  ? 976  HOH A O   1 
HETATM 3313 O  O   . HOH N 7 .   ? 34.001 17.959 70.495  1.00 8.09  ? 977  HOH A O   1 
HETATM 3314 O  O   . HOH N 7 .   ? 17.058 27.524 57.138  1.00 34.11 ? 978  HOH A O   1 
HETATM 3315 O  O   . HOH N 7 .   ? 31.292 11.856 65.900  1.00 23.22 ? 979  HOH A O   1 
HETATM 3316 O  O   . HOH N 7 .   ? 39.031 22.776 14.026  1.00 13.48 ? 980  HOH A O   1 
HETATM 3317 O  O   . HOH N 7 .   ? 44.285 19.970 17.835  1.00 31.91 ? 981  HOH A O   1 
HETATM 3318 O  O   . HOH N 7 .   ? 28.831 28.844 67.399  1.00 22.28 ? 982  HOH A O   1 
HETATM 3319 O  O   . HOH N 7 .   ? 35.640 15.461 63.741  1.00 18.29 ? 983  HOH A O   1 
HETATM 3320 O  O   . HOH N 7 .   ? 37.450 23.859 5.157   1.00 32.44 ? 984  HOH A O   1 
HETATM 3321 O  O   . HOH N 7 .   ? 19.497 1.176  58.962  1.00 35.45 ? 985  HOH A O   1 
HETATM 3322 O  O   . HOH N 7 .   ? 27.359 28.844 34.568  1.00 27.28 ? 986  HOH A O   1 
HETATM 3323 O  O   . HOH N 7 .   ? 30.424 21.138 43.181  1.00 8.17  ? 987  HOH A O   1 
HETATM 3324 O  O   . HOH N 7 .   ? 12.463 27.913 55.667  1.00 23.07 ? 988  HOH A O   1 
HETATM 3325 O  O   . HOH N 7 .   ? 29.845 22.026 1.057   1.00 21.11 ? 989  HOH A O   1 
HETATM 3326 O  O   . HOH N 7 .   ? 17.172 23.225 9.387   1.00 28.20 ? 990  HOH A O   1 
HETATM 3327 O  O   . HOH N 7 .   ? 38.693 23.619 90.435  1.00 10.42 ? 991  HOH A O   1 
HETATM 3328 O  O   . HOH N 7 .   ? 29.870 19.888 110.344 1.00 15.39 ? 992  HOH A O   1 
HETATM 3329 O  O   . HOH N 7 .   ? 20.196 16.374 94.101  1.00 31.25 ? 993  HOH A O   1 
HETATM 3330 O  O   . HOH N 7 .   ? 38.108 29.586 85.997  1.00 19.60 ? 994  HOH A O   1 
HETATM 3331 O  O   . HOH N 7 .   ? 19.739 29.248 50.421  1.00 15.43 ? 995  HOH A O   1 
HETATM 3332 O  O   . HOH N 7 .   ? 30.485 28.215 95.968  1.00 21.26 ? 996  HOH A O   1 
HETATM 3333 O  O   . HOH N 7 .   ? 32.739 12.900 104.817 1.00 20.73 ? 997  HOH A O   1 
HETATM 3334 O  O   . HOH N 7 .   ? 36.875 9.547  47.073  1.00 33.07 ? 998  HOH A O   1 
HETATM 3335 O  O   . HOH N 7 .   ? 26.749 10.972 46.689  1.00 18.54 ? 999  HOH A O   1 
HETATM 3336 O  O   . HOH N 7 .   ? 32.812 39.583 16.044  1.00 31.72 ? 1000 HOH A O   1 
HETATM 3337 O  O   . HOH N 7 .   ? 15.128 1.432  48.939  1.00 15.70 ? 1001 HOH A O   1 
HETATM 3338 O  O   . HOH N 7 .   ? 18.847 -1.909 53.204  1.00 15.51 ? 1002 HOH A O   1 
HETATM 3339 O  O   . HOH N 7 .   ? 20.461 27.397 52.114  1.00 17.56 ? 1003 HOH A O   1 
HETATM 3340 O  O   . HOH N 7 .   ? 16.532 15.980 69.683  1.00 23.61 ? 1004 HOH A O   1 
HETATM 3341 O  O   . HOH N 7 .   ? 28.495 28.109 -0.912  1.00 25.78 ? 1005 HOH A O   1 
HETATM 3342 O  O   . HOH N 7 .   ? 29.876 32.247 76.251  1.00 18.73 ? 1006 HOH A O   1 
HETATM 3343 O  O   . HOH N 7 .   ? 36.014 13.047 94.927  1.00 27.29 ? 1007 HOH A O   1 
HETATM 3344 O  O   . HOH N 7 .   ? 24.646 25.576 95.814  1.00 17.79 ? 1008 HOH A O   1 
HETATM 3345 O  O   . HOH N 7 .   ? 24.860 18.836 105.155 1.00 26.24 ? 1009 HOH A O   1 
HETATM 3346 O  O   . HOH N 7 .   ? 27.249 24.800 0.415   1.00 18.71 ? 1010 HOH A O   1 
HETATM 3347 O  O   . HOH N 7 .   ? 25.573 24.516 47.919  1.00 14.11 ? 1011 HOH A O   1 
HETATM 3348 O  O   . HOH N 7 .   ? 35.892 15.392 6.961   1.00 24.76 ? 1012 HOH A O   1 
HETATM 3349 O  O   . HOH N 7 .   ? 19.734 13.749 95.746  1.00 27.86 ? 1013 HOH A O   1 
HETATM 3350 O  O   . HOH N 7 .   ? 32.085 9.565  29.287  1.00 24.03 ? 1014 HOH A O   1 
HETATM 3351 O  O   . HOH N 7 .   ? 12.789 9.822  39.462  1.00 18.56 ? 1015 HOH A O   1 
HETATM 3352 O  O   . HOH N 7 .   ? 25.378 18.545 36.198  1.00 9.16  ? 1016 HOH A O   1 
HETATM 3353 O  O   . HOH N 7 .   ? 35.209 23.589 3.659   1.00 20.84 ? 1017 HOH A O   1 
HETATM 3354 O  O   . HOH N 7 .   ? 37.072 12.946 90.321  1.00 21.52 ? 1018 HOH A O   1 
HETATM 3355 O  O   . HOH N 7 .   ? 24.922 12.388 32.542  1.00 11.22 ? 1019 HOH A O   1 
HETATM 3356 O  O   . HOH N 7 .   ? 25.900 17.564 79.960  1.00 34.92 ? 1020 HOH A O   1 
HETATM 3357 O  O   . HOH N 7 .   ? 24.383 17.022 108.174 1.00 31.37 ? 1021 HOH A O   1 
HETATM 3358 O  O   . HOH N 7 .   ? 17.850 29.404 90.008  1.00 29.60 ? 1022 HOH A O   1 
HETATM 3359 O  O   . HOH N 7 .   ? 13.700 3.658  49.589  1.00 21.23 ? 1023 HOH A O   1 
HETATM 3360 O  O   . HOH N 7 .   ? 18.339 6.524  48.789  1.00 14.27 ? 1024 HOH A O   1 
HETATM 3361 O  O   . HOH N 7 .   ? 29.888 30.519 94.747  1.00 24.55 ? 1025 HOH A O   1 
HETATM 3362 O  O   . HOH N 7 .   ? 29.404 13.460 96.365  1.00 14.01 ? 1026 HOH A O   1 
HETATM 3363 O  O   . HOH N 7 .   ? 23.349 30.952 78.616  1.00 24.35 ? 1027 HOH A O   1 
HETATM 3364 O  O   . HOH N 7 .   ? 34.162 13.213 63.760  1.00 14.11 ? 1028 HOH A O   1 
HETATM 3365 O  O   . HOH N 7 .   ? 24.431 10.682 63.277  1.00 17.55 ? 1029 HOH A O   1 
HETATM 3366 O  O   . HOH N 7 .   ? 31.889 10.323 101.774 1.00 22.32 ? 1030 HOH A O   1 
HETATM 3367 O  O   . HOH N 7 .   ? 31.525 10.581 33.277  1.00 20.47 ? 1031 HOH A O   1 
HETATM 3368 O  O   . HOH N 7 .   ? 27.469 6.277  57.526  1.00 17.43 ? 1032 HOH A O   1 
HETATM 3369 O  O   . HOH N 7 .   ? 34.589 33.988 18.719  1.00 14.36 ? 1033 HOH A O   1 
HETATM 3370 O  O   . HOH N 7 .   ? 25.374 25.093 40.833  1.00 14.99 ? 1034 HOH A O   1 
HETATM 3371 O  O   . HOH N 7 .   ? 27.562 11.236 90.195  1.00 17.35 ? 1035 HOH A O   1 
HETATM 3372 O  O   . HOH N 7 .   ? 25.894 7.408  29.273  1.00 20.07 ? 1036 HOH A O   1 
HETATM 3373 O  O   . HOH N 7 .   ? 20.834 11.336 89.011  1.00 29.01 ? 1037 HOH A O   1 
HETATM 3374 O  O   . HOH N 7 .   ? 30.896 17.838 26.027  1.00 7.33  ? 1038 HOH A O   1 
HETATM 3375 O  O   . HOH N 7 .   ? 35.750 8.651  100.231 1.00 29.66 ? 1039 HOH A O   1 
HETATM 3376 O  O   . HOH N 7 .   ? 15.232 31.938 43.808  1.00 29.86 ? 1040 HOH A O   1 
HETATM 3377 O  O   . HOH N 7 .   ? 21.781 7.577  64.176  1.00 24.35 ? 1041 HOH A O   1 
HETATM 3378 O  O   . HOH N 7 .   ? 29.848 10.792 29.756  1.00 21.26 ? 1042 HOH A O   1 
HETATM 3379 O  O   . HOH N 7 .   ? 37.688 34.087 5.097   1.00 29.38 ? 1043 HOH A O   1 
HETATM 3380 O  O   . HOH N 7 .   ? 35.774 14.919 48.785  1.00 22.06 ? 1044 HOH A O   1 
HETATM 3381 O  O   . HOH N 7 .   ? 20.446 14.801 25.426  1.00 35.21 ? 1045 HOH A O   1 
HETATM 3382 O  O   . HOH N 7 .   ? 37.172 30.630 74.277  1.00 21.10 ? 1046 HOH A O   1 
HETATM 3383 O  O   . HOH N 7 .   ? 36.853 27.078 92.913  1.00 16.22 ? 1047 HOH A O   1 
HETATM 3384 O  O   . HOH N 7 .   ? 20.967 25.095 75.410  1.00 27.69 ? 1048 HOH A O   1 
HETATM 3385 O  O   . HOH N 7 .   ? 25.450 12.407 103.137 1.00 14.76 ? 1049 HOH A O   1 
HETATM 3386 O  O   . HOH N 7 .   ? 33.056 11.821 40.255  1.00 14.91 ? 1050 HOH A O   1 
HETATM 3387 O  O   . HOH N 7 .   ? 40.282 17.677 110.138 1.00 29.22 ? 1051 HOH A O   1 
HETATM 3388 O  O   . HOH N 7 .   ? 27.273 21.762 0.675   1.00 22.51 ? 1052 HOH A O   1 
HETATM 3389 O  O   . HOH N 7 .   ? 21.020 18.364 101.624 1.00 18.70 ? 1053 HOH A O   1 
HETATM 3390 O  O   . HOH N 7 .   ? 37.668 10.888 12.402  1.00 34.44 ? 1054 HOH A O   1 
HETATM 3391 O  O   . HOH N 7 .   ? 29.137 27.404 56.261  1.00 17.13 ? 1055 HOH A O   1 
HETATM 3392 O  O   . HOH N 7 .   ? 13.272 16.700 30.336  1.00 28.35 ? 1056 HOH A O   1 
HETATM 3393 O  O   . HOH N 7 .   ? 41.215 27.250 83.445  1.00 33.60 ? 1057 HOH A O   1 
HETATM 3394 O  O   . HOH N 7 .   ? 33.407 21.031 34.764  1.00 18.99 ? 1058 HOH A O   1 
HETATM 3395 O  O   . HOH N 7 .   ? 32.322 11.157 27.111  1.00 20.45 ? 1059 HOH A O   1 
HETATM 3396 O  O   . HOH N 7 .   ? 39.678 13.494 86.115  1.00 32.79 ? 1060 HOH A O   1 
HETATM 3397 O  O   . HOH N 7 .   ? 17.387 20.906 97.318  1.00 35.15 ? 1061 HOH A O   1 
HETATM 3398 O  O   . HOH N 7 .   ? 17.595 4.572  46.642  1.00 18.37 ? 1062 HOH A O   1 
HETATM 3399 O  O   . HOH N 7 .   ? 23.259 19.681 25.584  1.00 17.48 ? 1063 HOH A O   1 
HETATM 3400 O  O   . HOH N 7 .   ? 36.435 18.959 4.247   1.00 26.81 ? 1064 HOH A O   1 
HETATM 3401 O  O   . HOH N 7 .   ? 19.826 21.067 0.946   1.00 42.01 ? 1065 HOH A O   1 
HETATM 3402 O  O   . HOH N 7 .   ? 27.052 29.090 30.410  1.00 17.24 ? 1066 HOH A O   1 
HETATM 3403 O  O   . HOH N 7 .   ? 29.880 34.460 88.877  1.00 20.03 ? 1067 HOH A O   1 
HETATM 3404 O  O   . HOH N 7 .   ? 39.490 13.768 70.453  1.00 38.97 ? 1068 HOH A O   1 
HETATM 3405 O  O   . HOH N 7 .   ? 33.826 21.298 53.915  1.00 14.97 ? 1069 HOH A O   1 
HETATM 3406 O  O   . HOH N 7 .   ? 33.874 24.786 33.765  1.00 20.44 ? 1070 HOH A O   1 
HETATM 3407 O  O   . HOH N 7 .   ? 26.601 30.449 68.074  1.00 19.44 ? 1071 HOH A O   1 
HETATM 3408 O  O   . HOH N 7 .   ? 36.558 12.586 73.557  1.00 13.24 ? 1072 HOH A O   1 
HETATM 3409 O  O   . HOH N 7 .   ? 28.315 39.033 4.358   1.00 15.32 ? 1073 HOH A O   1 
HETATM 3410 O  O   . HOH N 7 .   ? 21.801 13.353 29.733  1.00 22.68 ? 1074 HOH A O   1 
HETATM 3411 O  O   . HOH N 7 .   ? 43.088 17.137 17.075  1.00 25.40 ? 1075 HOH A O   1 
HETATM 3412 O  O   . HOH N 7 .   ? 12.107 6.809  51.317  1.00 24.08 ? 1076 HOH A O   1 
HETATM 3413 O  O   . HOH N 7 .   ? 23.825 30.476 97.054  1.00 24.39 ? 1077 HOH A O   1 
HETATM 3414 O  O   . HOH N 7 .   ? 29.759 9.227  40.293  1.00 17.38 ? 1078 HOH A O   1 
HETATM 3415 O  O   . HOH N 7 .   ? 21.225 24.366 97.539  1.00 16.60 ? 1079 HOH A O   1 
HETATM 3416 O  O   . HOH N 7 .   ? 9.650  26.918 46.189  1.00 29.10 ? 1080 HOH A O   1 
HETATM 3417 O  O   . HOH N 7 .   ? 28.302 33.958 26.734  1.00 21.47 ? 1081 HOH A O   1 
HETATM 3418 O  O   . HOH N 7 .   ? 32.714 19.613 43.825  1.00 11.44 ? 1082 HOH A O   1 
HETATM 3419 O  O   . HOH N 7 .   ? 11.795 9.582  34.464  1.00 23.07 ? 1083 HOH A O   1 
HETATM 3420 O  O   . HOH N 7 .   ? 20.290 25.966 26.123  1.00 31.48 ? 1084 HOH A O   1 
HETATM 3421 O  O   . HOH N 7 .   ? 33.574 31.584 68.260  1.00 32.84 ? 1085 HOH A O   1 
HETATM 3422 O  O   . HOH N 7 .   ? 46.401 23.087 24.373  1.00 26.56 ? 1086 HOH A O   1 
HETATM 3423 O  O   . HOH N 7 .   ? 18.171 35.404 7.853   1.00 39.72 ? 1087 HOH A O   1 
HETATM 3424 O  O   . HOH N 7 .   ? 22.923 12.183 62.027  1.00 22.96 ? 1088 HOH A O   1 
HETATM 3425 O  O   . HOH N 7 .   ? 44.300 26.437 16.377  1.00 29.89 ? 1089 HOH A O   1 
HETATM 3426 O  O   . HOH N 7 .   ? 23.794 8.488  74.536  1.00 19.74 ? 1090 HOH A O   1 
HETATM 3427 O  O   . HOH N 7 .   ? 40.685 15.642 30.678  1.00 24.60 ? 1091 HOH A O   1 
HETATM 3428 O  O   . HOH N 7 .   ? 31.293 31.437 73.406  1.00 21.18 ? 1092 HOH A O   1 
HETATM 3429 O  O   . HOH N 7 .   ? 25.195 27.082 31.066  1.00 17.40 ? 1093 HOH A O   1 
HETATM 3430 O  O   . HOH N 7 .   ? 30.585 28.025 98.896  1.00 18.10 ? 1094 HOH A O   1 
HETATM 3431 O  O   . HOH N 7 .   ? 29.540 7.444  35.473  1.00 16.33 ? 1095 HOH A O   1 
HETATM 3432 O  O   . HOH N 7 .   ? 28.003 32.205 17.415  1.00 16.39 ? 1096 HOH A O   1 
HETATM 3433 O  O   . HOH N 7 .   ? 28.204 11.502 87.080  1.00 15.43 ? 1097 HOH A O   1 
HETATM 3434 O  O   . HOH N 7 .   ? 40.929 25.769 12.287  1.00 17.83 ? 1098 HOH A O   1 
HETATM 3435 O  O   . HOH N 7 .   ? 36.709 35.748 6.902   1.00 5.94  ? 1099 HOH A O   1 
HETATM 3436 O  O   . HOH N 7 .   ? 37.234 33.681 90.720  1.00 44.71 ? 1100 HOH A O   1 
HETATM 3437 O  O   . HOH N 7 .   ? 21.584 29.796 40.004  1.00 33.47 ? 1101 HOH A O   1 
HETATM 3438 O  O   . HOH N 7 .   ? 6.507  15.369 50.783  1.00 30.51 ? 1102 HOH A O   1 
HETATM 3439 O  O   . HOH N 7 .   ? 33.079 11.833 57.634  1.00 28.86 ? 1103 HOH A O   1 
HETATM 3440 O  O   . HOH N 7 .   ? 17.091 17.969 84.478  1.00 31.43 ? 1104 HOH A O   1 
HETATM 3441 O  O   . HOH N 7 .   ? 25.187 35.613 77.089  1.00 37.63 ? 1105 HOH A O   1 
HETATM 3442 O  O   . HOH N 7 .   ? 33.689 26.778 55.950  1.00 40.91 ? 1106 HOH A O   1 
HETATM 3443 O  O   . HOH N 7 .   ? 6.498  8.456  49.282  1.00 33.86 ? 1107 HOH A O   1 
HETATM 3444 O  O   . HOH N 7 .   ? 17.462 22.514 71.418  1.00 29.22 ? 1108 HOH A O   1 
HETATM 3445 O  O   . HOH N 7 .   ? 29.876 15.343 25.168  1.00 20.93 ? 1109 HOH A O   1 
HETATM 3446 O  O   . HOH N 7 .   ? 39.199 18.719 36.630  1.00 26.81 ? 1110 HOH A O   1 
HETATM 3447 O  O   . HOH N 7 .   ? 22.144 11.825 86.562  1.00 24.58 ? 1111 HOH A O   1 
HETATM 3448 O  O   . HOH N 7 .   ? 36.117 12.453 6.917   1.00 30.66 ? 1112 HOH A O   1 
HETATM 3449 O  O   . HOH N 7 .   ? 31.903 8.712  35.115  1.00 28.98 ? 1113 HOH A O   1 
HETATM 3450 O  O   . HOH N 7 .   ? 33.995 36.932 -0.716  1.00 24.35 ? 1114 HOH A O   1 
HETATM 3451 O  O   . HOH N 7 .   ? 15.857 4.246  57.401  1.00 33.04 ? 1115 HOH A O   1 
HETATM 3452 O  O   . HOH N 7 .   ? 27.566 34.148 92.174  1.00 30.88 ? 1116 HOH A O   1 
HETATM 3453 O  O   . HOH N 7 .   ? 40.513 25.011 95.382  1.00 37.51 ? 1117 HOH A O   1 
HETATM 3454 O  O   . HOH N 7 .   ? 32.687 38.610 3.705   1.00 44.47 ? 1118 HOH A O   1 
HETATM 3455 O  O   . HOH N 7 .   ? 9.978  24.425 57.068  1.00 29.32 ? 1119 HOH A O   1 
HETATM 3456 O  O   . HOH N 7 .   ? 37.240 21.325 110.017 1.00 30.68 ? 1120 HOH A O   1 
HETATM 3457 O  O   . HOH N 7 .   ? 24.682 27.373 48.949  1.00 42.30 ? 1121 HOH A O   1 
HETATM 3458 O  O   . HOH N 7 .   ? 12.640 8.380  36.727  1.00 21.72 ? 1122 HOH A O   1 
HETATM 3459 O  O   . HOH N 7 .   ? 34.308 13.677 58.768  1.00 31.50 ? 1123 HOH A O   1 
HETATM 3460 O  O   . HOH N 7 .   ? 39.225 19.767 108.321 1.00 19.25 ? 1124 HOH A O   1 
HETATM 3461 O  O   . HOH N 7 .   ? 21.145 28.941 42.811  1.00 30.56 ? 1125 HOH A O   1 
HETATM 3462 O  O   . HOH N 7 .   ? 18.760 23.234 96.658  1.00 32.67 ? 1126 HOH A O   1 
HETATM 3463 O  O   . HOH N 7 .   ? 14.637 23.855 7.923   1.00 33.21 ? 1127 HOH A O   1 
HETATM 3464 O  O   . HOH N 7 .   ? 15.570 21.118 61.167  1.00 25.63 ? 1128 HOH A O   1 
HETATM 3465 O  O   . HOH N 7 .   ? 42.568 14.402 29.109  1.00 34.29 ? 1129 HOH A O   1 
HETATM 3466 O  O   . HOH N 7 .   ? 38.809 26.923 5.588   1.00 23.54 ? 1130 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 
8    N N   . THR A 27  ? 0.2556 0.2921 0.1584 -0.0642 0.0575  0.0295  29  THR A N   
9    C CA  . THR A 27  ? 0.2537 0.2720 0.1582 -0.0680 0.0479  0.0277  29  THR A CA  
10   C C   . THR A 27  ? 0.2233 0.2568 0.1493 -0.0550 0.0417  0.0208  29  THR A C   
11   O O   . THR A 27  ? 0.2128 0.2504 0.1420 -0.0397 0.0408  0.0167  29  THR A O   
12   C CB  . THR A 27  ? 0.2720 0.2478 0.1513 -0.0633 0.0424  0.0290  29  THR A CB  
13   O OG1 . THR A 27  ? 0.3065 0.2628 0.1610 -0.0714 0.0476  0.0357  29  THR A OG1 
14   C CG2 . THR A 27  ? 0.2811 0.2343 0.1550 -0.0688 0.0363  0.0283  29  THR A CG2 
15   N N   . THR A 28  ? 0.2107 0.2489 0.1476 -0.0626 0.0368  0.0197  30  THR A N   
16   C CA  . THR A 28  ? 0.1850 0.2341 0.1390 -0.0521 0.0306  0.0143  30  THR A CA  
17   C C   . THR A 28  ? 0.1895 0.2128 0.1341 -0.0563 0.0238  0.0132  30  THR A C   
18   O O   . THR A 28  ? 0.2095 0.2095 0.1357 -0.0684 0.0242  0.0162  30  THR A O   
19   C CB  . THR A 28  ? 0.1717 0.2603 0.1504 -0.0544 0.0321  0.0145  30  THR A CB  
20   O OG1 . THR A 28  ? 0.1753 0.2721 0.1562 -0.0749 0.0310  0.0188  30  THR A OG1 
21   C CG2 . THR A 28  ? 0.1743 0.2885 0.1605 -0.0463 0.0413  0.0155  30  THR A CG2 
22   N N   . TYR A 29  ? 0.1760 0.2004 0.1298 -0.0457 0.0184  0.0090  31  TYR A N   
23   C CA  . TYR A 29  ? 0.1871 0.1872 0.1304 -0.0453 0.0137  0.0075  31  TYR A CA  
24   C C   . TYR A 29  ? 0.1753 0.1901 0.1328 -0.0448 0.0088  0.0044  31  TYR A C   
25   O O   . TYR A 29  ? 0.1548 0.1973 0.1312 -0.0412 0.0081  0.0035  31  TYR A O   
26   C CB  . TYR A 29  ? 0.1882 0.1715 0.1242 -0.0304 0.0128  0.0072  31  TYR A CB  
27   C CG  . TYR A 29  ? 0.2083 0.1713 0.1251 -0.0307 0.0160  0.0114  31  TYR A CG  
28   C CD1 . TYR A 29  ? 0.2363 0.1677 0.1302 -0.0356 0.0169  0.0139  31  TYR A CD1 
29   C CD2 . TYR A 29  ? 0.2094 0.1808 0.1264 -0.0264 0.0181  0.0128  31  TYR A CD2 
30   C CE1 . TYR A 29  ? 0.2623 0.1718 0.1357 -0.0352 0.0195  0.0188  31  TYR A CE1 
31   C CE2 . TYR A 29  ? 0.2310 0.1833 0.1281 -0.0272 0.0204  0.0175  31  TYR A CE2 
32   C CZ  . TYR A 29  ? 0.2586 0.1804 0.1347 -0.0313 0.0210  0.0210  31  TYR A CZ  
33   O OH  . TYR A 29  ? 0.2871 0.1874 0.1413 -0.0306 0.0228  0.0265  31  TYR A OH  
34   N N   . THR A 30  ? 0.1919 0.1846 0.1364 -0.0473 0.0059  0.0030  32  THR A N   
35   C CA  . THR A 30  ? 0.1922 0.1918 0.1428 -0.0485 0.0008  0.0005  32  THR A CA  
36   C C   . THR A 30  ? 0.1923 0.1763 0.1376 -0.0350 0.0005  -0.0014 32  THR A C   
37   O O   . THR A 30  ? 0.2071 0.1666 0.1362 -0.0296 0.0036  -0.0007 32  THR A O   
38   C CB  . THR A 30  ? 0.2188 0.2062 0.1547 -0.0670 -0.0023 0.0007  32  THR A CB  
39   O OG1 . THR A 30  ? 0.2196 0.2318 0.1667 -0.0812 -0.0021 0.0041  32  THR A OG1 
40   C CG2 . THR A 30  ? 0.2220 0.2117 0.1581 -0.0693 -0.0087 -0.0018 32  THR A CG2 
41   N N   . ILE A 31  ? 0.1793 0.1785 0.1379 -0.0291 -0.0027 -0.0028 33  ILE A N   
42   C CA  . ILE A 31  ? 0.1838 0.1712 0.1366 -0.0208 -0.0027 -0.0038 33  ILE A CA  
43   C C   . ILE A 31  ? 0.1954 0.1825 0.1433 -0.0280 -0.0072 -0.0055 33  ILE A C   
44   O O   . ILE A 31  ? 0.1896 0.1983 0.1514 -0.0316 -0.0120 -0.0052 33  ILE A O   
45   C CB  . ILE A 31  ? 0.1673 0.1685 0.1353 -0.0095 -0.0031 -0.0028 33  ILE A CB  
46   C CG1 . ILE A 31  ? 0.1631 0.1641 0.1331 -0.0038 -0.0008 -0.0010 33  ILE A CG1 
47   C CG2 . ILE A 31  ? 0.1669 0.1618 0.1312 -0.0035 -0.0025 -0.0024 33  ILE A CG2 
48   C CD1 . ILE A 31  ? 0.1550 0.1687 0.1374 0.0022  -0.0034 -0.0004 33  ILE A CD1 
49   N N   . GLN A 32  ? 0.2221 0.1834 0.1480 -0.0289 -0.0057 -0.0072 34  GLN A N   
50   C CA  . GLN A 32  ? 0.2439 0.1996 0.1590 -0.0352 -0.0103 -0.0092 34  GLN A CA  
51   C C   . GLN A 32  ? 0.2341 0.1838 0.1452 -0.0227 -0.0066 -0.0093 34  GLN A C   
52   O O   . GLN A 32  ? 0.2370 0.1697 0.1366 -0.0131 0.0006  -0.0091 34  GLN A O   
53   C CB  . GLN A 32  ? 0.2948 0.2206 0.1807 -0.0483 -0.0115 -0.0117 34  GLN A CB  
54   C CG  . GLN A 32  ? 0.3414 0.2592 0.2117 -0.0568 -0.0179 -0.0142 34  GLN A CG  
55   C CD  . GLN A 32  ? 0.4136 0.2983 0.2506 -0.0735 -0.0213 -0.0172 34  GLN A CD  
56   O OE1 . GLN A 32  ? 0.4938 0.3414 0.2979 -0.0704 -0.0181 -0.0210 34  GLN A OE1 
57   N NE2 . GLN A 32  ? 0.4360 0.3332 0.2795 -0.0920 -0.0276 -0.0153 34  GLN A NE2 
58   N N   . LEU A 33  ? 0.2215 0.1867 0.1421 -0.0224 -0.0112 -0.0085 35  LEU A N   
59   C CA  . LEU A 33  ? 0.2236 0.1860 0.1409 -0.0131 -0.0075 -0.0072 35  LEU A CA  
60   C C   . LEU A 33  ? 0.2380 0.1821 0.1303 -0.0181 -0.0093 -0.0096 35  LEU A C   
61   O O   . LEU A 33  ? 0.2394 0.1900 0.1308 -0.0278 -0.0183 -0.0102 35  LEU A O   
62   C CB  . LEU A 33  ? 0.2119 0.1976 0.1512 -0.0100 -0.0116 -0.0041 35  LEU A CB  
63   C CG  . LEU A 33  ? 0.2020 0.2011 0.1605 -0.0048 -0.0100 -0.0023 35  LEU A CG  
64   C CD1 . LEU A 33  ? 0.1987 0.2130 0.1719 -0.0033 -0.0156 -0.0007 35  LEU A CD1 
65   C CD2 . LEU A 33  ? 0.2086 0.2045 0.1673 0.0029  -0.0031 0.0001  35  LEU A CD2 
66   N N   . THR A 34  ? 0.2568 0.1795 0.1282 -0.0104 -0.0008 -0.0107 36  THR A N   
67   C CA  . THR A 34  ? 0.2917 0.1914 0.1326 -0.0138 -0.0011 -0.0137 36  THR A CA  
68   C C   . THR A 34  ? 0.2793 0.1884 0.1227 -0.0059 0.0028  -0.0102 36  THR A C   
69   O O   . THR A 34  ? 0.2491 0.1775 0.1144 0.0023  0.0079  -0.0055 36  THR A O   
70   C CB  . THR A 34  ? 0.3433 0.2059 0.1509 -0.0087 0.0075  -0.0178 36  THR A CB  
71   O OG1 . THR A 34  ? 0.3436 0.2116 0.1598 0.0091  0.0199  -0.0143 36  THR A OG1 
72   C CG2 . THR A 34  ? 0.3653 0.2121 0.1645 -0.0190 0.0034  -0.0205 36  THR A CG2 
73   N N   . GLY A 35  ? 0.2959 0.1906 0.1149 -0.0107 -0.0001 -0.0120 37  GLY A N   
74   C CA  . GLY A 35  ? 0.2999 0.2005 0.1161 -0.0058 0.0030  -0.0080 37  GLY A CA  
75   C C   . GLY A 35  ? 0.2717 0.1987 0.1138 -0.0095 -0.0064 -0.0029 37  GLY A C   
76   O O   . GLY A 35  ? 0.2629 0.1988 0.1114 -0.0048 -0.0024 0.0023  37  GLY A O   
77   N N   . THR A 36  ? 0.2570 0.1960 0.1134 -0.0173 -0.0181 -0.0038 38  THR A N   
78   C CA  . THR A 36  ? 0.2365 0.1978 0.1155 -0.0172 -0.0265 0.0006  38  THR A CA  
79   C C   . THR A 36  ? 0.2579 0.2168 0.1220 -0.0221 -0.0367 0.0025  38  THR A C   
80   O O   . THR A 36  ? 0.2791 0.2215 0.1172 -0.0291 -0.0398 -0.0007 38  THR A O   
81   C CB  . THR A 36  ? 0.2168 0.1962 0.1192 -0.0198 -0.0323 -0.0002 38  THR A CB  
82   O OG1 . THR A 36  ? 0.2308 0.2067 0.1229 -0.0308 -0.0389 -0.0036 38  THR A OG1 
83   C CG2 . THR A 36  ? 0.2021 0.1840 0.1182 -0.0148 -0.0237 -0.0011 38  THR A CG2 
84   N N   . SER A 37  ? 0.2556 0.2276 0.1331 -0.0180 -0.0424 0.0079  39  SER A N   
85   C CA  . SER A 37  ? 0.2788 0.2503 0.1439 -0.0198 -0.0530 0.0117  39  SER A CA  
86   C C   . SER A 37  ? 0.2590 0.2542 0.1471 -0.0172 -0.0645 0.0147  39  SER A C   
87   O O   . SER A 37  ? 0.2374 0.2437 0.1477 -0.0107 -0.0613 0.0152  39  SER A O   
88   C CB  . SER A 37  ? 0.3017 0.2624 0.1558 -0.0148 -0.0482 0.0172  39  SER A CB  
89   O OG  . SER A 37  ? 0.3324 0.2777 0.1693 -0.0147 -0.0350 0.0155  39  SER A OG  
90   N N   . SER A 38  ? 0.2702 0.2733 0.1514 -0.0214 -0.0776 0.0171  40  SER A N   
91   C CA  . SER A 38  ? 0.2587 0.2884 0.1615 -0.0152 -0.0885 0.0220  40  SER A CA  
92   C C   . SER A 38  ? 0.2518 0.2751 0.1578 -0.0013 -0.0870 0.0277  40  SER A C   
93   O O   . SER A 38  ? 0.2655 0.2662 0.1522 -0.0008 -0.0825 0.0298  40  SER A O   
94   C CB  . SER A 38  ? 0.2788 0.3202 0.1725 -0.0227 -0.1040 0.0250  40  SER A CB  
95   O OG  . SER A 38  ? 0.3144 0.3346 0.1798 -0.0221 -0.1075 0.0283  40  SER A OG  
96   N N   . GLY A 39  ? 0.2361 0.2778 0.1637 0.0098  -0.0907 0.0306  41  GLY A N   
97   C CA  . GLY A 39  ? 0.2431 0.2728 0.1674 0.0235  -0.0918 0.0363  41  GLY A CA  
98   C C   . GLY A 39  ? 0.2345 0.2488 0.1635 0.0272  -0.0804 0.0337  41  GLY A C   
99   O O   . GLY A 39  ? 0.2459 0.2398 0.1649 0.0339  -0.0797 0.0376  41  GLY A O   
100  N N   . HIS A 40  ? 0.2143 0.2366 0.1562 0.0215  -0.0725 0.0274  42  HIS A N   
101  C CA  . HIS A 40  ? 0.2054 0.2168 0.1525 0.0236  -0.0637 0.0249  42  HIS A CA  
102  C C   . HIS A 40  ? 0.1905 0.2201 0.1575 0.0308  -0.0627 0.0218  42  HIS A C   
103  O O   . HIS A 40  ? 0.1789 0.2329 0.1584 0.0296  -0.0659 0.0210  42  HIS A O   
104  C CB  . HIS A 40  ? 0.2017 0.2062 0.1450 0.0129  -0.0543 0.0212  42  HIS A CB  
105  C CG  . HIS A 40  ? 0.2192 0.2072 0.1435 0.0076  -0.0514 0.0245  42  HIS A CG  
106  N ND1 . HIS A 40  ? 0.2194 0.1964 0.1406 0.0045  -0.0436 0.0265  42  HIS A ND1 
107  C CD2 . HIS A 40  ? 0.2389 0.2212 0.1458 0.0041  -0.0548 0.0267  42  HIS A CD2 
108  C CE1 . HIS A 40  ? 0.2389 0.2062 0.1429 0.0001  -0.0407 0.0302  42  HIS A CE1 
109  N NE2 . HIS A 40  ? 0.2536 0.2212 0.1464 0.0004  -0.0474 0.0299  42  HIS A NE2 
110  N N   . VAL A 41  ? 0.1918 0.2087 0.1594 0.0366  -0.0581 0.0206  43  VAL A N   
111  C CA  . VAL A 41  ? 0.1930 0.2222 0.1748 0.0429  -0.0545 0.0168  43  VAL A CA  
112  C C   . VAL A 41  ? 0.1872 0.2045 0.1676 0.0352  -0.0471 0.0129  43  VAL A C   
113  O O   . VAL A 41  ? 0.2007 0.1960 0.1701 0.0346  -0.0464 0.0138  43  VAL A O   
114  C CB  . VAL A 41  ? 0.2102 0.2334 0.1899 0.0605  -0.0568 0.0186  43  VAL A CB  
115  C CG1 . VAL A 41  ? 0.2036 0.2355 0.1932 0.0674  -0.0505 0.0140  43  VAL A CG1 
116  C CG2 . VAL A 41  ? 0.2226 0.2637 0.2069 0.0710  -0.0649 0.0242  43  VAL A CG2 
117  N N   . TYR A 42  ? 0.1797 0.2111 0.1697 0.0282  -0.0428 0.0094  44  TYR A N   
118  C CA  . TYR A 42  ? 0.1822 0.2060 0.1720 0.0224  -0.0367 0.0067  44  TYR A CA  
119  C C   . TYR A 42  ? 0.1787 0.2045 0.1736 0.0288  -0.0342 0.0036  44  TYR A C   
120  O O   . TYR A 42  ? 0.1720 0.2145 0.1758 0.0346  -0.0337 0.0026  44  TYR A O   
121  C CB  . TYR A 42  ? 0.1794 0.2108 0.1717 0.0134  -0.0329 0.0049  44  TYR A CB  
122  C CG  . TYR A 42  ? 0.1994 0.2250 0.1812 0.0080  -0.0339 0.0068  44  TYR A CG  
123  C CD1 . TYR A 42  ? 0.2217 0.2344 0.1941 0.0069  -0.0326 0.0101  44  TYR A CD1 
124  C CD2 . TYR A 42  ? 0.2129 0.2448 0.1916 0.0024  -0.0360 0.0055  44  TYR A CD2 
125  C CE1 . TYR A 42  ? 0.2286 0.2354 0.1884 0.0030  -0.0318 0.0118  44  TYR A CE1 
126  C CE2 . TYR A 42  ? 0.2281 0.2501 0.1914 -0.0023 -0.0367 0.0063  44  TYR A CE2 
127  C CZ  . TYR A 42  ? 0.2380 0.2475 0.1915 -0.0007 -0.0338 0.0093  44  TYR A CZ  
128  O OH  . TYR A 42  ? 0.2717 0.2707 0.2070 -0.0043 -0.0329 0.0100  44  TYR A OH  
129  N N   . GLU A 43  ? 0.1869 0.1977 0.1757 0.0266  -0.0325 0.0026  45  GLU A N   
130  C CA  . GLU A 43  ? 0.1924 0.1992 0.1796 0.0314  -0.0303 -0.0009 45  GLU A CA  
131  C C   . GLU A 43  ? 0.1785 0.1883 0.1687 0.0232  -0.0270 -0.0022 45  GLU A C   
132  O O   . GLU A 43  ? 0.1710 0.1762 0.1598 0.0157  -0.0276 0.0001  45  GLU A O   
133  C CB  . GLU A 43  ? 0.2216 0.2021 0.1926 0.0355  -0.0339 -0.0009 45  GLU A CB  
134  C CG  . GLU A 43  ? 0.2437 0.2163 0.2083 0.0456  -0.0377 0.0015  45  GLU A CG  
135  C CD  . GLU A 43  ? 0.2788 0.2178 0.2213 0.0524  -0.0407 0.0008  45  GLU A CD  
136  O OE1 . GLU A 43  ? 0.2917 0.2098 0.2220 0.0412  -0.0431 0.0011  45  GLU A OE1 
137  O OE2 . GLU A 43  ? 0.3044 0.2384 0.2412 0.0689  -0.0409 0.0005  45  GLU A OE2 
138  N N   . LEU A 44  ? 0.1645 0.1839 0.1588 0.0258  -0.0231 -0.0050 46  LEU A N   
139  C CA  . LEU A 44  ? 0.1556 0.1759 0.1500 0.0204  -0.0204 -0.0057 46  LEU A CA  
140  C C   . LEU A 44  ? 0.1567 0.1662 0.1410 0.0245  -0.0203 -0.0088 46  LEU A C   
141  O O   . LEU A 44  ? 0.1580 0.1706 0.1405 0.0329  -0.0171 -0.0113 46  LEU A O   
142  C CB  . LEU A 44  ? 0.1525 0.1879 0.1543 0.0178  -0.0159 -0.0058 46  LEU A CB  
143  C CG  . LEU A 44  ? 0.1627 0.2022 0.1676 0.0119  -0.0162 -0.0039 46  LEU A CG  
144  C CD1 . LEU A 44  ? 0.1680 0.2159 0.1768 0.0138  -0.0194 -0.0031 46  LEU A CD1 
145  C CD2 . LEU A 44  ? 0.1648 0.2076 0.1690 0.0062  -0.0122 -0.0040 46  LEU A CD2 
146  N N   . TYR A 45  ? 0.1545 0.1526 0.1314 0.0187  -0.0240 -0.0082 47  TYR A N   
147  C CA  . TYR A 45  ? 0.1679 0.1510 0.1297 0.0200  -0.0258 -0.0115 47  TYR A CA  
148  C C   . TYR A 45  ? 0.1604 0.1507 0.1228 0.0160  -0.0245 -0.0109 47  TYR A C   
149  O O   . TYR A 45  ? 0.1489 0.1469 0.1188 0.0097  -0.0267 -0.0068 47  TYR A O   
150  C CB  . TYR A 45  ? 0.1885 0.1505 0.1372 0.0138  -0.0337 -0.0109 47  TYR A CB  
151  C CG  . TYR A 45  ? 0.2009 0.1474 0.1419 0.0191  -0.0353 -0.0113 47  TYR A CG  
152  C CD1 . TYR A 45  ? 0.1877 0.1418 0.1390 0.0167  -0.0359 -0.0069 47  TYR A CD1 
153  C CD2 . TYR A 45  ? 0.2320 0.1541 0.1523 0.0286  -0.0354 -0.0160 47  TYR A CD2 
154  C CE1 . TYR A 45  ? 0.2052 0.1436 0.1472 0.0226  -0.0380 -0.0062 47  TYR A CE1 
155  C CE2 . TYR A 45  ? 0.2448 0.1493 0.1552 0.0364  -0.0370 -0.0156 47  TYR A CE2 
156  C CZ  . TYR A 45  ? 0.2331 0.1466 0.1552 0.0330  -0.0388 -0.0103 47  TYR A CZ  
157  O OH  . TYR A 45  ? 0.2521 0.1460 0.1616 0.0421  -0.0409 -0.0093 47  TYR A OH  
158  N N   . HIS A 46  ? 0.1699 0.1570 0.1226 0.0211  -0.0204 -0.0143 48  HIS A N   
159  C CA  . HIS A 46  ? 0.1654 0.1563 0.1146 0.0182  -0.0190 -0.0132 48  HIS A CA  
160  C C   . HIS A 46  ? 0.1750 0.1527 0.1111 0.0119  -0.0279 -0.0128 48  HIS A C   
161  O O   . HIS A 46  ? 0.2002 0.1588 0.1163 0.0130  -0.0307 -0.0171 48  HIS A O   
162  C CB  . HIS A 46  ? 0.1722 0.1657 0.1144 0.0250  -0.0105 -0.0162 48  HIS A CB  
163  C CG  . HIS A 46  ? 0.1666 0.1658 0.1068 0.0215  -0.0070 -0.0135 48  HIS A CG  
164  N ND1 . HIS A 46  ? 0.1828 0.1811 0.1107 0.0251  0.0000  -0.0152 48  HIS A ND1 
165  C CD2 . HIS A 46  ? 0.1561 0.1591 0.1015 0.0159  -0.0092 -0.0089 48  HIS A CD2 
166  C CE1 . HIS A 46  ? 0.1786 0.1791 0.1043 0.0199  0.0013  -0.0112 48  HIS A CE1 
167  N NE2 . HIS A 46  ? 0.1652 0.1673 0.1009 0.0154  -0.0044 -0.0074 48  HIS A NE2 
168  N N   . ILE A 47  ? 0.1622 0.1501 0.1082 0.0054  -0.0327 -0.0072 49  ILE A N   
169  C CA  . ILE A 47  ? 0.1738 0.1574 0.1125 -0.0027 -0.0431 -0.0047 49  ILE A CA  
170  C C   . ILE A 47  ? 0.1864 0.1682 0.1130 -0.0020 -0.0445 -0.0041 49  ILE A C   
171  O O   . ILE A 47  ? 0.2128 0.1787 0.1186 -0.0059 -0.0509 -0.0071 49  ILE A O   
172  C CB  . ILE A 47  ? 0.1611 0.1637 0.1196 -0.0082 -0.0469 0.0027  49  ILE A CB  
173  C CG1 . ILE A 47  ? 0.1519 0.1551 0.1196 -0.0088 -0.0444 0.0027  49  ILE A CG1 
174  C CG2 . ILE A 47  ? 0.1748 0.1811 0.1302 -0.0188 -0.0589 0.0072  49  ILE A CG2 
175  C CD1 . ILE A 47  ? 0.1715 0.1519 0.1232 -0.0125 -0.0488 -0.0015 49  ILE A CD1 
176  N N   . PHE A 48  ? 0.1733 0.1678 0.1092 0.0021  -0.0392 -0.0001 50  PHE A N   
177  C CA  . PHE A 48  ? 0.1868 0.1781 0.1097 0.0034  -0.0400 0.0017  50  PHE A CA  
178  C C   . PHE A 48  ? 0.1910 0.1795 0.1096 0.0089  -0.0282 -0.0001 50  PHE A C   
179  O O   . PHE A 48  ? 0.1723 0.1683 0.1041 0.0108  -0.0215 0.0010  50  PHE A O   
180  C CB  . PHE A 48  ? 0.1789 0.1851 0.1128 0.0040  -0.0449 0.0104  50  PHE A CB  
181  C CG  . PHE A 48  ? 0.1797 0.1990 0.1226 -0.0024 -0.0569 0.0156  50  PHE A CG  
182  C CD1 . PHE A 48  ? 0.2009 0.2112 0.1289 -0.0118 -0.0678 0.0135  50  PHE A CD1 
183  C CD2 . PHE A 48  ? 0.1664 0.2078 0.1311 0.0004  -0.0572 0.0233  50  PHE A CD2 
184  C CE1 . PHE A 48  ? 0.2068 0.2329 0.1442 -0.0216 -0.0802 0.0197  50  PHE A CE1 
185  C CE2 . PHE A 48  ? 0.1693 0.2308 0.1462 -0.0064 -0.0677 0.0301  50  PHE A CE2 
186  C CZ  . PHE A 48  ? 0.1882 0.2437 0.1528 -0.0191 -0.0800 0.0287  50  PHE A CZ  
187  N N   . SER A 49  ? 0.2196 0.1970 0.1174 0.0100  -0.0259 -0.0025 51  SER A N   
188  C CA  . SER A 49  ? 0.2283 0.2059 0.1211 0.0123  -0.0154 -0.0014 51  SER A CA  
189  C C   . SER A 49  ? 0.2446 0.2193 0.1296 0.0117  -0.0189 0.0056  51  SER A C   
190  O O   . SER A 49  ? 0.2508 0.2249 0.1318 0.0109  -0.0297 0.0089  51  SER A O   
191  C CB  . SER A 49  ? 0.2492 0.2185 0.1235 0.0152  -0.0084 -0.0068 51  SER A CB  
192  O OG  . SER A 49  ? 0.2735 0.2273 0.1234 0.0142  -0.0158 -0.0080 51  SER A OG  
193  N N   . GLY A 50  ? 0.2509 0.2234 0.1327 0.0116  -0.0103 0.0088  52  GLY A N   
194  C CA  . GLY A 50  ? 0.2717 0.2353 0.1406 0.0127  -0.0124 0.0161  52  GLY A CA  
195  C C   . GLY A 50  ? 0.2812 0.2384 0.1476 0.0100  -0.0025 0.0194  52  GLY A C   
196  O O   . GLY A 50  ? 0.2800 0.2437 0.1544 0.0054  0.0057  0.0161  52  GLY A O   
197  N N   . ASP A 51  ? 0.3019 0.2456 0.1556 0.0125  -0.0044 0.0268  53  ASP A N   
198  C CA  . ASP A 51  ? 0.3165 0.2455 0.1611 0.0083  0.0034  0.0308  53  ASP A CA  
199  C C   . ASP A 51  ? 0.3062 0.2273 0.1564 0.0153  0.0001  0.0345  53  ASP A C   
200  O O   . ASP A 51  ? 0.3114 0.2325 0.1607 0.0255  -0.0075 0.0394  53  ASP A O   
201  C CB  . ASP A 51  ? 0.3546 0.2651 0.1710 0.0064  0.0056  0.0370  53  ASP A CB  
202  C CG  . ASP A 51  ? 0.3774 0.2944 0.1836 0.0019  0.0102  0.0336  53  ASP A CG  
203  O OD1 . ASP A 51  ? 0.3782 0.3087 0.1946 -0.0040 0.0191  0.0288  53  ASP A OD1 
204  O OD2 . ASP A 51  ? 0.4117 0.3207 0.1985 0.0056  0.0047  0.0363  53  ASP A OD2 
205  N N   . LEU A 52  ? 0.3026 0.2173 0.1567 0.0101  0.0061  0.0327  54  LEU A N   
206  C CA  . LEU A 52  ? 0.3091 0.2115 0.1635 0.0177  0.0052  0.0350  54  LEU A CA  
207  C C   . LEU A 52  ? 0.3442 0.2116 0.1702 0.0164  0.0092  0.0407  54  LEU A C   
208  O O   . LEU A 52  ? 0.3570 0.2131 0.1714 0.0019  0.0151  0.0402  54  LEU A O   
209  C CB  . LEU A 52  ? 0.2883 0.2001 0.1591 0.0124  0.0079  0.0287  54  LEU A CB  
210  C CG  . LEU A 52  ? 0.2971 0.2006 0.1699 0.0225  0.0075  0.0294  54  LEU A CG  
211  C CD1 . LEU A 52  ? 0.2809 0.2100 0.1752 0.0334  0.0017  0.0300  54  LEU A CD1 
212  C CD2 . LEU A 52  ? 0.2941 0.1935 0.1695 0.0131  0.0113  0.0239  54  LEU A CD2 
213  N N   . ASP A 53  ? 0.3644 0.2153 0.1792 0.0317  0.0062  0.0468  55  ASP A N   
214  C CA  . ASP A 53  ? 0.4119 0.2213 0.1941 0.0337  0.0096  0.0528  55  ASP A CA  
215  C C   . ASP A 53  ? 0.4199 0.2069 0.1949 0.0363  0.0138  0.0500  55  ASP A C   
216  O O   . ASP A 53  ? 0.3931 0.1999 0.1893 0.0348  0.0142  0.0436  55  ASP A O   
217  C CB  . ASP A 53  ? 0.4419 0.2425 0.2108 0.0513  0.0039  0.0622  55  ASP A CB  
218  C CG  . ASP A 53  ? 0.4388 0.2512 0.2212 0.0740  -0.0001 0.0657  55  ASP A CG  
219  O OD1 . ASP A 53  ? 0.4227 0.2542 0.2272 0.0756  0.0013  0.0602  55  ASP A OD1 
220  O OD2 . ASP A 53  ? 0.4627 0.2667 0.2328 0.0905  -0.0048 0.0750  55  ASP A OD2 
221  N N   . ALA A 54  ? 0.4665 0.2080 0.2073 0.0407  0.0166  0.0548  56  ALA A N   
222  C CA  . ALA A 54  ? 0.4923 0.1995 0.2140 0.0418  0.0211  0.0517  56  ALA A CA  
223  C C   . ALA A 54  ? 0.4871 0.2031 0.2201 0.0669  0.0212  0.0516  56  ALA A C   
224  O O   . ALA A 54  ? 0.4965 0.1930 0.2195 0.0688  0.0254  0.0469  56  ALA A O   
225  C CB  . ALA A 54  ? 0.5496 0.1991 0.2254 0.0387  0.0239  0.0571  56  ALA A CB  
226  N N   . ASN A 55  ? 0.4719 0.2187 0.2253 0.0850  0.0166  0.0574  57  ASN A N   
227  C CA  . ASN A 55  ? 0.4633 0.2307 0.2344 0.1083  0.0170  0.0593  57  ASN A CA  
228  C C   . ASN A 55  ? 0.4029 0.2231 0.2156 0.1020  0.0137  0.0547  57  ASN A C   
229  O O   . ASN A 55  ? 0.3946 0.2435 0.2286 0.1178  0.0129  0.0580  57  ASN A O   
230  C CB  . ASN A 55  ? 0.4847 0.2560 0.2527 0.1324  0.0129  0.0708  57  ASN A CB  
231  C CG  . ASN A 55  ? 0.5522 0.2652 0.2747 0.1424  0.0166  0.0763  57  ASN A CG  
232  O OD1 . ASN A 55  ? 0.5844 0.2845 0.2910 0.1428  0.0120  0.0835  57  ASN A OD1 
233  N ND2 . ASN A 55  ? 0.5933 0.2668 0.2908 0.1507  0.0247  0.0730  57  ASN A ND2 
234  N N   . ASN A 56  ? 0.3783 0.2109 0.2014 0.0792  0.0122  0.0479  58  ASN A N   
235  C CA  . ASN A 56  ? 0.3311 0.2055 0.1875 0.0715  0.0088  0.0431  58  ASN A CA  
236  C C   . ASN A 56  ? 0.3189 0.2281 0.1966 0.0789  0.0007  0.0485  58  ASN A C   
237  O O   . ASN A 56  ? 0.2892 0.2303 0.1925 0.0800  -0.0020 0.0477  58  ASN A O   
238  C CB  . ASN A 56  ? 0.3223 0.2038 0.1895 0.0755  0.0131  0.0387  58  ASN A CB  
239  C CG  . ASN A 56  ? 0.3468 0.1911 0.1888 0.0673  0.0191  0.0332  58  ASN A CG  
240  O OD1 . ASN A 56  ? 0.3909 0.2136 0.2176 0.0796  0.0246  0.0331  58  ASN A OD1 
241  N ND2 . ASN A 56  ? 0.3370 0.1744 0.1736 0.0466  0.0183  0.0290  58  ASN A ND2 
242  N N   . VAL A 57  ? 0.3336 0.2350 0.1982 0.0811  -0.0036 0.0543  59  VAL A N   
243  C CA  . VAL A 57  ? 0.3229 0.2539 0.2021 0.0838  -0.0137 0.0593  59  VAL A CA  
244  C C   . VAL A 57  ? 0.3100 0.2457 0.1885 0.0655  -0.0164 0.0533  59  VAL A C   
245  O O   . VAL A 57  ? 0.3309 0.2433 0.1899 0.0561  -0.0111 0.0508  59  VAL A O   
246  C CB  . VAL A 57  ? 0.3509 0.2709 0.2138 0.0994  -0.0180 0.0701  59  VAL A CB  
247  C CG1 . VAL A 57  ? 0.3430 0.2939 0.2185 0.0990  -0.0309 0.0754  59  VAL A CG1 
248  C CG2 . VAL A 57  ? 0.3715 0.2858 0.2335 0.1223  -0.0135 0.0763  59  VAL A CG2 
249  N N   . LEU A 58  ? 0.2863 0.2511 0.1838 0.0606  -0.0241 0.0516  60  LEU A N   
250  C CA  . LEU A 58  ? 0.2801 0.2475 0.1750 0.0464  -0.0257 0.0449  60  LEU A CA  
251  C C   . LEU A 58  ? 0.2840 0.2541 0.1670 0.0459  -0.0354 0.0491  60  LEU A C   
252  O O   . LEU A 58  ? 0.2664 0.2569 0.1604 0.0498  -0.0461 0.0541  60  LEU A O   
253  C CB  . LEU A 58  ? 0.2702 0.2588 0.1876 0.0401  -0.0275 0.0388  60  LEU A CB  
254  C CG  . LEU A 58  ? 0.2753 0.2601 0.1899 0.0287  -0.0237 0.0298  60  LEU A CG  
255  C CD1 . LEU A 58  ? 0.2777 0.2506 0.1900 0.0254  -0.0131 0.0262  60  LEU A CD1 
256  C CD2 . LEU A 58  ? 0.2659 0.2673 0.1969 0.0241  -0.0288 0.0255  60  LEU A CD2 
257  N N   . THR A 59  ? 0.2960 0.2473 0.1561 0.0396  -0.0316 0.0472  61  THR A N   
258  C CA  . THR A 59  ? 0.3140 0.2621 0.1555 0.0382  -0.0397 0.0503  61  THR A CA  
259  C C   . THR A 59  ? 0.3128 0.2597 0.1464 0.0272  -0.0374 0.0412  61  THR A C   
260  O O   . THR A 59  ? 0.2942 0.2406 0.1345 0.0220  -0.0275 0.0342  61  THR A O   
261  C CB  . THR A 59  ? 0.3456 0.2683 0.1598 0.0428  -0.0365 0.0579  61  THR A CB  
262  O OG1 . THR A 59  ? 0.3522 0.2567 0.1582 0.0360  -0.0228 0.0544  61  THR A OG1 
263  C CG2 . THR A 59  ? 0.3567 0.2780 0.1720 0.0583  -0.0418 0.0685  61  THR A CG2 
264  N N   . ASN A 60  ? 0.3357 0.2813 0.1529 0.0248  -0.0471 0.0420  62  ASN A N   
265  C CA  . ASN A 60  ? 0.3557 0.2921 0.1540 0.0176  -0.0444 0.0341  62  ASN A CA  
266  C C   . ASN A 60  ? 0.3361 0.2821 0.1512 0.0134  -0.0436 0.0248  62  ASN A C   
267  O O   . ASN A 60  ? 0.3328 0.2738 0.1445 0.0117  -0.0325 0.0176  62  ASN A O   
268  C CB  . ASN A 60  ? 0.3777 0.2980 0.1571 0.0159  -0.0297 0.0335  62  ASN A CB  
269  C CG  . ASN A 60  ? 0.4072 0.3124 0.1655 0.0194  -0.0313 0.0438  62  ASN A CG  
270  O OD1 . ASN A 60  ? 0.4350 0.3293 0.1898 0.0192  -0.0215 0.0478  62  ASN A OD1 
271  N ND2 . ASN A 60  ? 0.4133 0.3161 0.1558 0.0219  -0.0447 0.0485  62  ASN A ND2 
272  N N   . ILE A 61  ? 0.3348 0.2957 0.1671 0.0121  -0.0557 0.0263  63  ILE A N   
273  C CA  . ILE A 61  ? 0.3082 0.2783 0.1599 0.0083  -0.0559 0.0203  63  ILE A CA  
274  C C   . ILE A 61  ? 0.3276 0.2841 0.1593 0.0014  -0.0614 0.0124  63  ILE A C   
275  O O   . ILE A 61  ? 0.3464 0.2967 0.1592 -0.0033 -0.0735 0.0140  63  ILE A O   
276  C CB  . ILE A 61  ? 0.2930 0.2862 0.1714 0.0089  -0.0649 0.0271  63  ILE A CB  
277  C CG1 . ILE A 61  ? 0.2797 0.2799 0.1750 0.0181  -0.0557 0.0322  63  ILE A CG1 
278  C CG2 . ILE A 61  ? 0.2796 0.2801 0.1716 0.0013  -0.0689 0.0224  63  ILE A CG2 
279  C CD1 . ILE A 61  ? 0.2725 0.2965 0.1903 0.0235  -0.0625 0.0410  63  ILE A CD1 
280  N N   . GLU A 62  ? 0.3213 0.2718 0.1558 0.0016  -0.0530 0.0041  64  GLU A N   
281  C CA  . GLU A 62  ? 0.3419 0.2744 0.1569 -0.0026 -0.0572 -0.0041 64  GLU A CA  
282  C C   . GLU A 62  ? 0.3087 0.2467 0.1443 -0.0038 -0.0562 -0.0071 64  GLU A C   
283  O O   . GLU A 62  ? 0.2708 0.2264 0.1330 -0.0005 -0.0502 -0.0038 64  GLU A O   
284  C CB  . GLU A 62  ? 0.3822 0.2958 0.1712 0.0037  -0.0447 -0.0114 64  GLU A CB  
285  C CG  . GLU A 62  ? 0.4268 0.3335 0.1930 0.0054  -0.0418 -0.0082 64  GLU A CG  
286  C CD  . GLU A 62  ? 0.4800 0.3716 0.2172 -0.0011 -0.0571 -0.0072 64  GLU A CD  
287  O OE1 . GLU A 62  ? 0.5054 0.3912 0.2390 -0.0093 -0.0714 -0.0094 64  GLU A OE1 
288  O OE2 . GLU A 62  ? 0.5348 0.4199 0.2515 0.0003  -0.0556 -0.0036 64  GLU A OE2 
289  N N   . TRP A 63  ? 0.3210 0.2392 0.1393 -0.0084 -0.0620 -0.0136 65  TRP A N   
290  C CA  . TRP A 63  ? 0.3077 0.2238 0.1380 -0.0087 -0.0603 -0.0168 65  TRP A CA  
291  C C   . TRP A 63  ? 0.3024 0.2176 0.1364 0.0041  -0.0441 -0.0217 65  TRP A C   
292  O O   . TRP A 63  ? 0.3186 0.2202 0.1312 0.0118  -0.0359 -0.0270 65  TRP A O   
293  C CB  . TRP A 63  ? 0.3379 0.2250 0.1414 -0.0178 -0.0716 -0.0221 65  TRP A CB  
294  C CG  . TRP A 63  ? 0.3358 0.2318 0.1437 -0.0346 -0.0892 -0.0156 65  TRP A CG  
295  C CD1 . TRP A 63  ? 0.3656 0.2488 0.1484 -0.0461 -0.1035 -0.0153 65  TRP A CD1 
296  C CD2 . TRP A 63  ? 0.3063 0.2301 0.1471 -0.0425 -0.0945 -0.0073 65  TRP A CD2 
297  N NE1 . TRP A 63  ? 0.3593 0.2648 0.1606 -0.0614 -0.1182 -0.0066 65  TRP A NE1 
298  C CE2 . TRP A 63  ? 0.3196 0.2513 0.1573 -0.0586 -0.1118 -0.0014 65  TRP A CE2 
299  C CE3 . TRP A 63  ? 0.2707 0.2146 0.1422 -0.0375 -0.0862 -0.0040 65  TRP A CE3 
300  C CZ2 . TRP A 63  ? 0.3001 0.2636 0.1677 -0.0688 -0.1193 0.0084  65  TRP A CZ2 
301  C CZ3 . TRP A 63  ? 0.2542 0.2238 0.1505 -0.0470 -0.0930 0.0046  65  TRP A CZ3 
302  C CH2 . TRP A 63  ? 0.2705 0.2521 0.1668 -0.0620 -0.1086 0.0112  65  TRP A CH2 
303  N N   . GLY A 64  ? 0.2745 0.2070 0.1360 0.0065  -0.0394 -0.0193 66  GLY A N   
304  C CA  . GLY A 64  ? 0.2714 0.2075 0.1394 0.0171  -0.0269 -0.0229 66  GLY A CA  
305  C C   . GLY A 64  ? 0.2905 0.2038 0.1427 0.0221  -0.0277 -0.0292 66  GLY A C   
306  O O   . GLY A 64  ? 0.3148 0.2072 0.1513 0.0142  -0.0385 -0.0307 66  GLY A O   
307  N N   . ALA A 65  ? 0.2928 0.2102 0.1480 0.0350  -0.0166 -0.0322 67  ALA A N   
308  C CA  . ALA A 65  ? 0.3224 0.2163 0.1601 0.0452  -0.0151 -0.0379 67  ALA A CA  
309  C C   . ALA A 65  ? 0.3187 0.2078 0.1669 0.0404  -0.0229 -0.0357 67  ALA A C   
310  O O   . ALA A 65  ? 0.3469 0.2086 0.1760 0.0464  -0.0249 -0.0396 67  ALA A O   
311  C CB  . ALA A 65  ? 0.3233 0.2331 0.1675 0.0622  -0.0004 -0.0393 67  ALA A CB  
312  N N   . GLY A 66  ? 0.2841 0.1971 0.1597 0.0305  -0.0266 -0.0294 68  GLY A N   
313  C CA  . GLY A 66  ? 0.2826 0.1942 0.1685 0.0250  -0.0326 -0.0262 68  GLY A CA  
314  C C   . GLY A 66  ? 0.3090 0.1957 0.1768 0.0116  -0.0447 -0.0260 68  GLY A C   
315  O O   . GLY A 66  ? 0.3294 0.2045 0.1957 0.0076  -0.0492 -0.0242 68  GLY A O   
316  N N   . VAL A 67  ? 0.3177 0.1962 0.1705 0.0031  -0.0509 -0.0269 69  VAL A N   
317  C CA  . VAL A 67  ? 0.3507 0.2067 0.1845 -0.0129 -0.0644 -0.0263 69  VAL A CA  
318  C C   . VAL A 67  ? 0.4093 0.2198 0.1999 -0.0080 -0.0658 -0.0352 69  VAL A C   
319  O O   . VAL A 67  ? 0.4259 0.2297 0.2002 0.0009  -0.0604 -0.0403 69  VAL A O   
320  C CB  . VAL A 67  ? 0.3383 0.2153 0.1817 -0.0265 -0.0729 -0.0206 69  VAL A CB  
321  C CG1 . VAL A 67  ? 0.3641 0.2272 0.1942 -0.0473 -0.0886 -0.0177 69  VAL A CG1 
322  C CG2 . VAL A 67  ? 0.2912 0.2097 0.1728 -0.0249 -0.0680 -0.0129 69  VAL A CG2 
323  N N   . ALA A 68  ? 0.4460 0.2221 0.2148 -0.0134 -0.0722 -0.0370 70  ALA A N   
324  C CA  . ALA A 68  ? 0.5205 0.2434 0.2412 -0.0083 -0.0741 -0.0460 70  ALA A CA  
325  C C   . ALA A 68  ? 0.5573 0.2648 0.2513 -0.0213 -0.0835 -0.0491 70  ALA A C   
326  O O   . ALA A 68  ? 0.5491 0.2731 0.2542 -0.0428 -0.0962 -0.0429 70  ALA A O   
327  C CB  . ALA A 68  ? 0.5452 0.2305 0.2454 -0.0169 -0.0820 -0.0455 70  ALA A CB  
328  N N   . ILE A 69  ? 0.6147 0.2912 0.2724 -0.0074 -0.0774 -0.0583 71  ILE A N   
329  C CA  . ILE A 69  ? 0.6626 0.3241 0.2913 -0.0167 -0.0848 -0.0619 71  ILE A CA  
330  C C   . ILE A 69  ? 0.6990 0.3283 0.2996 -0.0442 -0.1056 -0.0614 71  ILE A C   
331  O O   . ILE A 69  ? 0.7088 0.3503 0.3082 -0.0619 -0.1180 -0.0580 71  ILE A O   
332  C CB  . ILE A 69  ? 0.7186 0.3472 0.3075 0.0053  -0.0721 -0.0725 71  ILE A CB  
333  C CG1 . ILE A 69  ? 0.6921 0.3613 0.3135 0.0289  -0.0520 -0.0709 71  ILE A CG1 
334  C CG2 . ILE A 69  ? 0.7497 0.3566 0.3012 -0.0051 -0.0806 -0.0768 71  ILE A CG2 
335  C CD1 . ILE A 69  ? 0.7303 0.3732 0.3229 0.0561  -0.0358 -0.0793 71  ILE A CD1 
336  N N   . GLY A 70  ? 0.7351 0.3235 0.3123 -0.0484 -0.1099 -0.0640 72  GLY A N   
337  C CA  . GLY A 70  ? 0.7847 0.3389 0.3329 -0.0778 -0.1298 -0.0629 72  GLY A CA  
338  C C   . GLY A 70  ? 0.7535 0.3594 0.3459 -0.1039 -0.1425 -0.0497 72  GLY A C   
339  O O   . GLY A 70  ? 0.7654 0.3635 0.3424 -0.1312 -0.1608 -0.0468 72  GLY A O   
340  N N   . ASP A 71  ? 0.6989 0.3585 0.3454 -0.0954 -0.1329 -0.0414 73  ASP A N   
341  C CA  . ASP A 71  ? 0.6881 0.3958 0.3766 -0.1158 -0.1415 -0.0285 73  ASP A CA  
342  C C   . ASP A 71  ? 0.6500 0.4101 0.3708 -0.1156 -0.1427 -0.0223 73  ASP A C   
343  O O   . ASP A 71  ? 0.6410 0.4439 0.3954 -0.1307 -0.1503 -0.0111 73  ASP A O   
344  C CB  . ASP A 71  ? 0.6740 0.4067 0.3984 -0.1071 -0.1307 -0.0227 73  ASP A CB  
345  C CG  . ASP A 71  ? 0.7380 0.4229 0.4338 -0.1123 -0.1330 -0.0249 73  ASP A CG  
346  O OD1 . ASP A 71  ? 0.7984 0.4596 0.4723 -0.1393 -0.1482 -0.0219 73  ASP A OD1 
347  O OD2 . ASP A 71  ? 0.7362 0.4060 0.4289 -0.0898 -0.1204 -0.0292 73  ASP A OD2 
348  N N   . ARG A 72  ? 0.6330 0.3896 0.3426 -0.0977 -0.1346 -0.0288 74  ARG A N   
349  C CA  . ARG A 72  ? 0.5868 0.3872 0.3232 -0.0934 -0.1335 -0.0230 74  ARG A CA  
350  C C   . ARG A 72  ? 0.6137 0.4234 0.3429 -0.1168 -0.1538 -0.0171 74  ARG A C   
351  O O   . ARG A 72  ? 0.5708 0.4289 0.3362 -0.1215 -0.1584 -0.0061 74  ARG A O   
352  C CB  . ARG A 72  ? 0.5793 0.3671 0.2979 -0.0719 -0.1205 -0.0311 74  ARG A CB  
353  C CG  . ARG A 72  ? 0.5321 0.3309 0.2715 -0.0491 -0.1005 -0.0334 74  ARG A CG  
354  C CD  . ARG A 72  ? 0.5391 0.3270 0.2597 -0.0303 -0.0873 -0.0405 74  ARG A CD  
355  N NE  . ARG A 72  ? 0.5130 0.3129 0.2532 -0.0113 -0.0701 -0.0421 74  ARG A NE  
356  C CZ  . ARG A 72  ? 0.5154 0.3166 0.2495 0.0059  -0.0554 -0.0462 74  ARG A CZ  
357  N NH1 . ARG A 72  ? 0.5476 0.3347 0.2532 0.0073  -0.0547 -0.0498 74  ARG A NH1 
358  N NH2 . ARG A 72  ? 0.4946 0.3122 0.2497 0.0207  -0.0418 -0.0462 74  ARG A NH2 
359  N N   . ALA A 73  ? 0.6900 0.4519 0.3703 -0.1308 -0.1663 -0.0242 75  ALA A N   
360  C CA  . ALA A 73  ? 0.7258 0.4919 0.3920 -0.1548 -0.1880 -0.0194 75  ALA A CA  
361  C C   . ALA A 73  ? 0.7015 0.5093 0.4040 -0.1792 -0.2016 -0.0056 75  ALA A C   
362  O O   . ALA A 73  ? 0.7004 0.5406 0.4148 -0.1954 -0.2178 0.0035  75  ALA A O   
363  C CB  . ALA A 73  ? 0.8035 0.5013 0.4039 -0.1656 -0.1978 -0.0312 75  ALA A CB  
364  N N   . LYS A 74  ? 0.6897 0.5005 0.4113 -0.1813 -0.1950 -0.0029 76  LYS A N   
365  C CA  . LYS A 74  ? 0.6765 0.5290 0.4329 -0.2041 -0.2052 0.0110  76  LYS A CA  
366  C C   . LYS A 74  ? 0.6100 0.5340 0.4246 -0.1908 -0.1972 0.0229  76  LYS A C   
367  O O   . LYS A 74  ? 0.6150 0.5867 0.4621 -0.2071 -0.2067 0.0365  76  LYS A O   
368  C CB  . LYS A 74  ? 0.6862 0.5122 0.4367 -0.2114 -0.2004 0.0100  76  LYS A CB  
369  C CG  . LYS A 74  ? 0.6344 0.4961 0.4290 -0.1936 -0.1823 0.0154  76  LYS A CG  
370  C CD  . LYS A 74  ? 0.6561 0.4807 0.4351 -0.1966 -0.1769 0.0127  76  LYS A CD  
371  C CE  . LYS A 74  ? 0.6187 0.4812 0.4400 -0.1824 -0.1611 0.0193  76  LYS A CE  
372  N NZ  . LYS A 74  ? 0.6364 0.4587 0.4389 -0.1788 -0.1542 0.0156  76  LYS A NZ  
373  N N   . PHE A 75  ? 0.5413 0.4726 0.3675 -0.1614 -0.1800 0.0186  77  PHE A N   
374  C CA  . PHE A 75  ? 0.4679 0.4555 0.3386 -0.1469 -0.1729 0.0284  77  PHE A CA  
375  C C   . PHE A 75  ? 0.4690 0.4698 0.3337 -0.1430 -0.1814 0.0309  77  PHE A C   
376  O O   . PHE A 75  ? 0.4363 0.4857 0.3351 -0.1372 -0.1825 0.0424  77  PHE A O   
377  C CB  . PHE A 75  ? 0.4261 0.4132 0.3111 -0.1200 -0.1507 0.0235  77  PHE A CB  
378  C CG  . PHE A 75  ? 0.4019 0.3840 0.2980 -0.1204 -0.1416 0.0232  77  PHE A CG  
379  C CD1 . PHE A 75  ? 0.3803 0.4022 0.3107 -0.1289 -0.1420 0.0347  77  PHE A CD1 
380  C CD2 . PHE A 75  ? 0.4118 0.3505 0.2828 -0.1116 -0.1328 0.0121  77  PHE A CD2 
381  C CE1 . PHE A 75  ? 0.3739 0.3886 0.3105 -0.1301 -0.1340 0.0349  77  PHE A CE1 
382  C CE2 . PHE A 75  ? 0.4045 0.3373 0.2834 -0.1115 -0.1259 0.0127  77  PHE A CE2 
383  C CZ  . PHE A 75  ? 0.3904 0.3594 0.3005 -0.1217 -0.1268 0.0239  77  PHE A CZ  
384  N N   . GLY A 76  ? 0.4903 0.4460 0.3097 -0.1438 -0.1861 0.0203  78  GLY A N   
385  C CA  . GLY A 76  ? 0.5017 0.4614 0.3064 -0.1409 -0.1945 0.0217  78  GLY A CA  
386  C C   . GLY A 76  ? 0.4797 0.4341 0.2834 -0.1134 -0.1761 0.0169  78  GLY A C   
387  O O   . GLY A 76  ? 0.4681 0.4046 0.2713 -0.0990 -0.1584 0.0091  78  GLY A O   
388  N N   . ASP A 77  ? 0.4787 0.4518 0.2836 -0.1074 -0.1812 0.0230  79  ASP A N   
389  C CA  . ASP A 77  ? 0.4688 0.4389 0.2718 -0.0848 -0.1657 0.0211  79  ASP A CA  
390  C C   . ASP A 77  ? 0.4050 0.4020 0.2485 -0.0691 -0.1487 0.0253  79  ASP A C   
391  O O   . ASP A 77  ? 0.3738 0.4096 0.2528 -0.0705 -0.1522 0.0358  79  ASP A O   
392  C CB  . ASP A 77  ? 0.5036 0.4897 0.3003 -0.0833 -0.1774 0.0297  79  ASP A CB  
393  C CG  . ASP A 77  ? 0.5323 0.5102 0.3211 -0.0627 -0.1623 0.0288  79  ASP A CG  
394  O OD1 . ASP A 77  ? 0.5719 0.5137 0.3298 -0.0574 -0.1511 0.0180  79  ASP A OD1 
395  O OD2 . ASP A 77  ? 0.5361 0.5432 0.3484 -0.0518 -0.1614 0.0396  79  ASP A OD2 
396  N N   . ALA A 78  ? 0.3800 0.3568 0.2164 -0.0542 -0.1301 0.0172  80  ALA A N   
397  C CA  . ALA A 78  ? 0.3330 0.3272 0.2004 -0.0414 -0.1144 0.0191  80  ALA A CA  
398  C C   . ALA A 78  ? 0.3126 0.3362 0.2018 -0.0307 -0.1132 0.0301  80  ALA A C   
399  O O   . ALA A 78  ? 0.2866 0.3366 0.2064 -0.0256 -0.1092 0.0367  80  ALA A O   
400  C CB  . ALA A 78  ? 0.3248 0.2940 0.1782 -0.0304 -0.0974 0.0092  80  ALA A CB  
401  N N   . SER A 79  ? 0.3229 0.3379 0.1920 -0.0258 -0.1157 0.0320  81  SER A N   
402  C CA  . SER A 79  ? 0.3158 0.3499 0.1974 -0.0136 -0.1149 0.0425  81  SER A CA  
403  C C   . SER A 79  ? 0.3065 0.3805 0.2169 -0.0154 -0.1275 0.0550  81  SER A C   
404  O O   . SER A 79  ? 0.2904 0.3859 0.2248 -0.0021 -0.1211 0.0628  81  SER A O   
405  C CB  . SER A 79  ? 0.3426 0.3574 0.1923 -0.0111 -0.1183 0.0429  81  SER A CB  
406  O OG  . SER A 79  ? 0.3452 0.3676 0.2016 0.0034  -0.1128 0.0516  81  SER A OG  
407  N N   . GLU A 80  ? 0.3235 0.4075 0.2303 -0.0320 -0.1454 0.0572  82  GLU A N   
408  C CA  . GLU A 80  ? 0.3258 0.4552 0.2623 -0.0364 -0.1589 0.0708  82  GLU A CA  
409  C C   . GLU A 80  ? 0.2893 0.4417 0.2582 -0.0399 -0.1523 0.0723  82  GLU A C   
410  O O   . GLU A 80  ? 0.2698 0.4644 0.2715 -0.0335 -0.1532 0.0843  82  GLU A O   
411  C CB  . GLU A 80  ? 0.3776 0.5103 0.2977 -0.0576 -0.1821 0.0730  82  GLU A CB  
412  C CG  . GLU A 80  ? 0.4259 0.5553 0.3237 -0.0531 -0.1936 0.0783  82  GLU A CG  
413  C CD  . GLU A 80  ? 0.4943 0.6156 0.3656 -0.0771 -0.2168 0.0774  82  GLU A CD  
414  O OE1 . GLU A 80  ? 0.5293 0.6461 0.4001 -0.0975 -0.2232 0.0726  82  GLU A OE1 
415  O OE2 . GLU A 80  ? 0.5481 0.6645 0.3960 -0.0764 -0.2291 0.0814  82  GLU A OE2 
416  N N   . LYS A 81  ? 0.2817 0.4065 0.2400 -0.0486 -0.1451 0.0608  83  LYS A N   
417  C CA  . LYS A 81  ? 0.2569 0.3975 0.2412 -0.0508 -0.1370 0.0618  83  LYS A CA  
418  C C   . LYS A 81  ? 0.2244 0.3753 0.2279 -0.0286 -0.1194 0.0643  83  LYS A C   
419  O O   . LYS A 81  ? 0.2066 0.3891 0.2390 -0.0242 -0.1148 0.0720  83  LYS A O   
420  C CB  . LYS A 81  ? 0.2712 0.3742 0.2352 -0.0615 -0.1329 0.0491  83  LYS A CB  
421  C CG  . LYS A 81  ? 0.2599 0.3751 0.2455 -0.0672 -0.1269 0.0507  83  LYS A CG  
422  C CD  . LYS A 81  ? 0.2693 0.4205 0.2751 -0.0860 -0.1409 0.0621  83  LYS A CD  
423  C CE  . LYS A 81  ? 0.2565 0.4201 0.2820 -0.0923 -0.1339 0.0649  83  LYS A CE  
424  N NZ  . LYS A 81  ? 0.2552 0.4704 0.3117 -0.1047 -0.1427 0.0801  83  LYS A NZ  
425  N N   . ALA A 82  ? 0.2227 0.3444 0.2072 -0.0160 -0.1088 0.0572  84  ALA A N   
426  C CA  . ALA A 82  ? 0.2099 0.3319 0.2038 0.0027  -0.0936 0.0586  84  ALA A CA  
427  C C   . ALA A 82  ? 0.2070 0.3595 0.2178 0.0165  -0.0966 0.0720  84  ALA A C   
428  O O   . ALA A 82  ? 0.1937 0.3622 0.2233 0.0293  -0.0870 0.0768  84  ALA A O   
429  C CB  . ALA A 82  ? 0.2217 0.3081 0.1895 0.0086  -0.0848 0.0503  84  ALA A CB  
430  N N   . ALA A 83  ? 0.2247 0.3843 0.2265 0.0150  -0.1102 0.0780  85  ALA A N   
431  C CA  . ALA A 83  ? 0.2299 0.4189 0.2459 0.0305  -0.1149 0.0920  85  ALA A CA  
432  C C   . ALA A 83  ? 0.2152 0.4547 0.2686 0.0298  -0.1184 0.1028  85  ALA A C   
433  O O   . ALA A 83  ? 0.2116 0.4763 0.2836 0.0499  -0.1126 0.1130  85  ALA A O   
434  C CB  . ALA A 83  ? 0.2525 0.4399 0.2498 0.0261  -0.1313 0.0965  85  ALA A CB  
435  N N   . SER A 84  ? 0.2114 0.4644 0.2733 0.0069  -0.1276 0.1012  86  SER A N   
436  C CA  . SER A 84  ? 0.2007 0.5043 0.2982 0.0009  -0.1316 0.1123  86  SER A CA  
437  C C   . SER A 84  ? 0.1809 0.4908 0.2961 0.0145  -0.1117 0.1118  86  SER A C   
438  O O   . SER A 84  ? 0.1755 0.5312 0.3218 0.0206  -0.1090 0.1234  86  SER A O   
439  C CB  . SER A 84  ? 0.2102 0.5152 0.3044 -0.0302 -0.1458 0.1095  86  SER A CB  
440  O OG  . SER A 84  ? 0.2015 0.4662 0.2787 -0.0389 -0.1362 0.0956  86  SER A OG  
441  N N   . LEU A 85  ? 0.1749 0.4405 0.2699 0.0183  -0.0981 0.0985  87  LEU A N   
442  C CA  . LEU A 85  ? 0.1607 0.4243 0.2653 0.0288  -0.0805 0.0961  87  LEU A CA  
443  C C   . LEU A 85  ? 0.1642 0.4147 0.2619 0.0559  -0.0676 0.0972  87  LEU A C   
444  O O   . LEU A 85  ? 0.1560 0.4049 0.2589 0.0672  -0.0532 0.0962  87  LEU A O   
445  C CB  . LEU A 85  ? 0.1569 0.3808 0.2427 0.0165  -0.0749 0.0818  87  LEU A CB  
446  C CG  . LEU A 85  ? 0.1615 0.3891 0.2495 -0.0084 -0.0847 0.0799  87  LEU A CG  
447  C CD1 . LEU A 85  ? 0.1618 0.3483 0.2295 -0.0148 -0.0782 0.0664  87  LEU A CD1 
448  C CD2 . LEU A 85  ? 0.1555 0.4269 0.2736 -0.0139 -0.0839 0.0909  87  LEU A CD2 
449  N N   . SER A 86  ? 0.1785 0.4152 0.2602 0.0653  -0.0728 0.0991  88  SER A N   
450  C CA  . SER A 86  ? 0.1950 0.4057 0.2604 0.0882  -0.0616 0.0990  88  SER A CA  
451  C C   . SER A 86  ? 0.2034 0.4447 0.2891 0.1118  -0.0533 0.1104  88  SER A C   
452  O O   . SER A 86  ? 0.2068 0.4929 0.3154 0.1179  -0.0616 0.1235  88  SER A O   
453  C CB  . SER A 86  ? 0.2161 0.4072 0.2590 0.0910  -0.0707 0.1006  88  SER A CB  
454  O OG  . SER A 86  ? 0.2359 0.3942 0.2574 0.1104  -0.0604 0.1006  88  SER A OG  
455  N N   . GLY A 87  ? 0.2196 0.4373 0.2957 0.1255  -0.0367 0.1056  89  GLY A N   
456  C CA  . GLY A 87  ? 0.2489 0.4864 0.3365 0.1520  -0.0255 0.1147  89  GLY A CA  
457  C C   . GLY A 87  ? 0.2581 0.5316 0.3723 0.1486  -0.0177 0.1172  89  GLY A C   
458  O O   . GLY A 87  ? 0.2819 0.5708 0.4040 0.1713  -0.0052 0.1236  89  GLY A O   
459  N N   . LYS A 88  ? 0.2649 0.5490 0.3899 0.1215  -0.0241 0.1123  90  LYS A N   
460  C CA  . LYS A 88  ? 0.2792 0.5985 0.4286 0.1150  -0.0181 0.1164  90  LYS A CA  
461  C C   . LYS A 88  ? 0.3034 0.5863 0.4344 0.1159  -0.0031 0.1051  90  LYS A C   
462  O O   . LYS A 88  ? 0.2935 0.5286 0.3973 0.1109  -0.0024 0.0930  90  LYS A O   
463  C CB  . LYS A 88  ? 0.2664 0.6105 0.4322 0.0844  -0.0332 0.1179  90  LYS A CB  
464  C CG  . LYS A 88  ? 0.2814 0.6697 0.4681 0.0798  -0.0498 0.1308  90  LYS A CG  
465  C CD  . LYS A 88  ? 0.2857 0.6987 0.4869 0.0479  -0.0644 0.1334  90  LYS A CD  
466  C CE  . LYS A 88  ? 0.3055 0.7576 0.5224 0.0397  -0.0840 0.1453  90  LYS A CE  
467  N NZ  . LYS A 88  ? 0.3113 0.8163 0.5566 0.0651  -0.0802 0.1618  90  LYS A NZ  
468  N N   . GLN A 89  ? 0.3508 0.6604 0.4974 0.1218  0.0085  0.1102  91  GLN A N   
469  C CA  . GLN A 89  ? 0.3948 0.6741 0.5234 0.1243  0.0228  0.1011  91  GLN A CA  
470  C C   . GLN A 89  ? 0.3872 0.6432 0.5070 0.0965  0.0153  0.0907  91  GLN A C   
471  O O   . GLN A 89  ? 0.3580 0.6330 0.4920 0.0760  0.0024  0.0933  91  GLN A O   
472  C CB  . GLN A 89  ? 0.4379 0.7551 0.5855 0.1330  0.0363  0.1098  91  GLN A CB  
473  C CG  . GLN A 89  ? 0.4824 0.8443 0.6513 0.1597  0.0434  0.1245  91  GLN A CG  
474  C CD  . GLN A 89  ? 0.5465 0.8691 0.6868 0.1902  0.0535  0.1207  91  GLN A CD  
475  O OE1 . GLN A 89  ? 0.5755 0.8487 0.6834 0.1958  0.0640  0.1095  91  GLN A OE1 
476  N NE2 . GLN A 89  ? 0.5690 0.9099 0.7180 0.2089  0.0488  0.1303  91  GLN A NE2 
477  N N   . ASN A 90  ? 0.4241 0.6383 0.5189 0.0965  0.0229  0.0794  92  ASN A N   
478  C CA  . ASN A 90  ? 0.4395 0.6316 0.5252 0.0747  0.0171  0.0701  92  ASN A CA  
479  C C   . ASN A 90  ? 0.4325 0.6531 0.5358 0.0615  0.0180  0.0756  92  ASN A C   
480  O O   . ASN A 90  ? 0.4242 0.6373 0.5266 0.0416  0.0094  0.0720  92  ASN A O   
481  C CB  . ASN A 90  ? 0.4580 0.6044 0.5147 0.0785  0.0241  0.0586  92  ASN A CB  
482  C CG  . ASN A 90  ? 0.4331 0.5575 0.4808 0.0596  0.0166  0.0495  92  ASN A CG  
483  O OD1 . ASN A 90  ? 0.4118 0.5296 0.4549 0.0529  0.0198  0.0463  92  ASN A OD1 
484  N ND2 . ASN A 90  ? 0.4433 0.5571 0.4875 0.0522  0.0071  0.0458  92  ASN A ND2 
485  N N   . ASP A 91  ? 0.4390 0.6909 0.5564 0.0736  0.0292  0.0850  93  ASP A N   
486  C CA  . ASP A 91  ? 0.4537 0.7345 0.5867 0.0613  0.0327  0.0920  93  ASP A CA  
487  C C   . ASP A 91  ? 0.4177 0.7562 0.5848 0.0573  0.0280  0.1073  93  ASP A C   
488  O O   . ASP A 91  ? 0.3963 0.7703 0.5811 0.0518  0.0345  0.1170  93  ASP A O   
489  C CB  . ASP A 91  ? 0.5068 0.7803 0.6275 0.0758  0.0509  0.0912  93  ASP A CB  
490  C CG  . ASP A 91  ? 0.5554 0.8385 0.6750 0.1060  0.0648  0.0956  93  ASP A CG  
491  O OD1 . ASP A 91  ? 0.5673 0.8648 0.6979 0.1168  0.0595  0.1004  93  ASP A OD1 
492  O OD2 . ASP A 91  ? 0.5354 0.8089 0.6401 0.1201  0.0808  0.0944  93  ASP A OD2 
493  N N   . SER A 92  ? 0.3736 0.7240 0.5500 0.0591  0.0164  0.1104  94  SER A N   
494  C CA  . SER A 92  ? 0.3423 0.7494 0.5513 0.0518  0.0078  0.1253  94  SER A CA  
495  C C   . SER A 92  ? 0.3265 0.7363 0.5397 0.0174  -0.0071 0.1257  94  SER A C   
496  O O   . SER A 92  ? 0.3035 0.6677 0.4928 0.0043  -0.0125 0.1136  94  SER A O   
497  C CB  . SER A 92  ? 0.3432 0.7593 0.5567 0.0655  -0.0009 0.1288  94  SER A CB  
498  O OG  . SER A 92  ? 0.3157 0.6870 0.5052 0.0557  -0.0132 0.1171  94  SER A OG  
499  N N   . SER A 93  ? 0.3459 0.8091 0.5886 0.0030  -0.0146 0.1401  95  SER A N   
500  C CA  . SER A 93  ? 0.3586 0.8237 0.6028 -0.0317 -0.0278 0.1422  95  SER A CA  
501  C C   . SER A 93  ? 0.3592 0.7851 0.5814 -0.0474 -0.0469 0.1322  95  SER A C   
502  O O   . SER A 93  ? 0.3743 0.7649 0.5766 -0.0687 -0.0539 0.1250  95  SER A O   
503  C CB  . SER A 93  ? 0.3654 0.8998 0.6466 -0.0458 -0.0320 0.1613  95  SER A CB  
504  O OG  . SER A 93  ? 0.3760 0.9456 0.6757 -0.0412 -0.0447 0.1694  95  SER A OG  
505  N N   . GLU A 94  ? 0.3500 0.7801 0.5730 -0.0354 -0.0548 0.1322  96  GLU A N   
506  C CA  . GLU A 94  ? 0.3385 0.7360 0.5401 -0.0490 -0.0724 0.1240  96  GLU A CA  
507  C C   . GLU A 94  ? 0.2921 0.6255 0.4593 -0.0441 -0.0672 0.1064  96  GLU A C   
508  O O   . GLU A 94  ? 0.2896 0.5877 0.4343 -0.0605 -0.0779 0.0979  96  GLU A O   
509  C CB  . GLU A 94  ? 0.3649 0.7803 0.5726 -0.0349 -0.0805 0.1287  96  GLU A CB  
510  C CG  . GLU A 94  ? 0.3861 0.8713 0.6306 -0.0368 -0.0877 0.1475  96  GLU A CG  
511  C CD  . GLU A 94  ? 0.4048 0.9341 0.6770 -0.0087 -0.0699 0.1586  96  GLU A CD  
512  O OE1 . GLU A 94  ? 0.4023 0.9039 0.6622 0.0110  -0.0511 0.1509  96  GLU A OE1 
513  O OE2 . GLU A 94  ? 0.4153 1.0073 0.7206 -0.0060 -0.0750 0.1752  96  GLU A OE2 
514  N N   . VAL A 95  ? 0.2603 0.5794 0.4225 -0.0211 -0.0507 0.1015  97  VAL A N   
515  C CA  . VAL A 95  ? 0.2460 0.5124 0.3799 -0.0161 -0.0456 0.0865  97  VAL A CA  
516  C C   . VAL A 95  ? 0.2582 0.5052 0.3832 -0.0305 -0.0429 0.0822  97  VAL A C   
517  O O   . VAL A 95  ? 0.2468 0.4549 0.3497 -0.0374 -0.0471 0.0717  97  VAL A O   
518  C CB  . VAL A 95  ? 0.2274 0.4825 0.3556 0.0100  -0.0311 0.0831  97  VAL A CB  
519  C CG1 . VAL A 95  ? 0.2203 0.4270 0.3221 0.0117  -0.0272 0.0690  97  VAL A CG1 
520  C CG2 . VAL A 95  ? 0.2331 0.5022 0.3661 0.0255  -0.0342 0.0884  97  VAL A CG2 
521  N N   . LYS A 96  ? 0.2704 0.5454 0.4119 -0.0334 -0.0351 0.0909  98  LYS A N   
522  C CA  . LYS A 96  ? 0.2931 0.5506 0.4249 -0.0479 -0.0331 0.0890  98  LYS A CA  
523  C C   . LYS A 96  ? 0.2773 0.5200 0.3992 -0.0737 -0.0496 0.0884  98  LYS A C   
524  O O   . LYS A 96  ? 0.2912 0.4943 0.3906 -0.0814 -0.0519 0.0804  98  LYS A O   
525  C CB  . LYS A 96  ? 0.3274 0.6207 0.4779 -0.0483 -0.0216 0.1004  98  LYS A CB  
526  C CG  . LYS A 96  ? 0.3519 0.6473 0.5020 -0.0228 -0.0034 0.0989  98  LYS A CG  
527  C CD  . LYS A 96  ? 0.3761 0.6839 0.5287 -0.0238 0.0100  0.1048  98  LYS A CD  
528  C CE  . LYS A 96  ? 0.4140 0.7632 0.5882 -0.0449 0.0076  0.1194  98  LYS A CE  
529  N NZ  . LYS A 96  ? 0.4172 0.8237 0.6242 -0.0416 0.0059  0.1325  98  LYS A NZ  
530  N N   . ALA A 97  ? 0.2563 0.5292 0.3927 -0.0858 -0.0614 0.0969  99  ALA A N   
531  C CA  . ALA A 97  ? 0.2626 0.5198 0.3858 -0.1128 -0.0787 0.0968  99  ALA A CA  
532  C C   . ALA A 97  ? 0.2745 0.4790 0.3655 -0.1093 -0.0852 0.0819  99  ALA A C   
533  O O   . ALA A 97  ? 0.3010 0.4661 0.3666 -0.1236 -0.0919 0.0757  99  ALA A O   
534  C CB  . ALA A 97  ? 0.2584 0.5625 0.4043 -0.1253 -0.0909 0.1093  99  ALA A CB  
535  N N   . PHE A 98  ? 0.2334 0.4366 0.3239 -0.0893 -0.0822 0.0768  100 PHE A N   
536  C CA  . PHE A 98  ? 0.2285 0.3892 0.2912 -0.0844 -0.0863 0.0641  100 PHE A CA  
537  C C   . PHE A 98  ? 0.2221 0.3445 0.2667 -0.0772 -0.0771 0.0538  100 PHE A C   
538  O O   . PHE A 98  ? 0.2314 0.3156 0.2502 -0.0810 -0.0820 0.0448  100 PHE A O   
539  C CB  . PHE A 98  ? 0.2132 0.3845 0.2807 -0.0658 -0.0839 0.0634  100 PHE A CB  
540  C CG  . PHE A 98  ? 0.2199 0.3545 0.2604 -0.0616 -0.0876 0.0524  100 PHE A CG  
541  C CD1 . PHE A 98  ? 0.2416 0.3507 0.2586 -0.0775 -0.1004 0.0477  100 PHE A CD1 
542  C CD2 . PHE A 98  ? 0.2120 0.3363 0.2480 -0.0423 -0.0779 0.0471  100 PHE A CD2 
543  C CE1 . PHE A 98  ? 0.2568 0.3332 0.2474 -0.0716 -0.1016 0.0377  100 PHE A CE1 
544  C CE2 . PHE A 98  ? 0.2204 0.3151 0.2326 -0.0390 -0.0796 0.0382  100 PHE A CE2 
545  C CZ  . PHE A 98  ? 0.2415 0.3136 0.2315 -0.0524 -0.0906 0.0335  100 PHE A CZ  
546  N N   . ALA A 99  ? 0.2018 0.3349 0.2584 -0.0657 -0.0640 0.0555  101 ALA A N   
547  C CA  . ALA A 99  ? 0.2053 0.3079 0.2470 -0.0590 -0.0565 0.0474  101 ALA A CA  
548  C C   . ALA A 99  ? 0.2308 0.3084 0.2563 -0.0755 -0.0629 0.0468  101 ALA A C   
549  O O   . ALA A 99  ? 0.2236 0.2654 0.2274 -0.0724 -0.0641 0.0383  101 ALA A O   
550  C CB  . ALA A 99  ? 0.1894 0.3088 0.2443 -0.0466 -0.0432 0.0504  101 ALA A CB  
551  N N   . GLN A 100 ? 0.2599 0.3566 0.2952 -0.0927 -0.0669 0.0569  102 GLN A N   
552  C CA  . GLN A 100 ? 0.3100 0.3811 0.3280 -0.1104 -0.0724 0.0585  102 GLN A CA  
553  C C   . GLN A 100 ? 0.3403 0.3763 0.3317 -0.1233 -0.0865 0.0529  102 GLN A C   
554  O O   . GLN A 100 ? 0.3714 0.3651 0.3355 -0.1285 -0.0899 0.0482  102 GLN A O   
555  C CB  . GLN A 100 ? 0.3253 0.4312 0.3625 -0.1276 -0.0717 0.0726  102 GLN A CB  
556  C CG  . GLN A 100 ? 0.3154 0.4492 0.3717 -0.1139 -0.0557 0.0777  102 GLN A CG  
557  C CD  . GLN A 100 ? 0.3171 0.4178 0.3545 -0.1059 -0.0486 0.0720  102 GLN A CD  
558  O OE1 . GLN A 100 ? 0.3284 0.4018 0.3473 -0.1195 -0.0530 0.0735  102 GLN A OE1 
559  N NE2 . GLN A 100 ? 0.2923 0.3924 0.3316 -0.0843 -0.0387 0.0658  102 GLN A NE2 
560  N N   . GLU A 101 ? 0.3424 0.3926 0.3381 -0.1274 -0.0949 0.0533  103 GLU A N   
561  C CA  . GLU A 101 ? 0.3862 0.3998 0.3515 -0.1391 -0.1084 0.0469  103 GLU A CA  
562  C C   . GLU A 101 ? 0.3624 0.3374 0.3037 -0.1191 -0.1035 0.0331  103 GLU A C   
563  O O   . GLU A 101 ? 0.3882 0.3169 0.2955 -0.1231 -0.1092 0.0257  103 GLU A O   
564  C CB  . GLU A 101 ? 0.4207 0.4642 0.3973 -0.1498 -0.1197 0.0524  103 GLU A CB  
565  C CG  . GLU A 101 ? 0.4762 0.5492 0.4675 -0.1773 -0.1297 0.0659  103 GLU A CG  
566  C CD  . GLU A 101 ? 0.5126 0.6433 0.5362 -0.1794 -0.1350 0.0765  103 GLU A CD  
567  O OE1 . GLU A 101 ? 0.5437 0.6701 0.5579 -0.1757 -0.1435 0.0724  103 GLU A OE1 
568  O OE2 . GLU A 101 ? 0.5415 0.7220 0.5990 -0.1824 -0.1297 0.0894  103 GLU A OE2 
569  N N   . LEU A 102 ? 0.3103 0.3042 0.2679 -0.0977 -0.0927 0.0302  104 LEU A N   
570  C CA  . LEU A 102 ? 0.3053 0.2725 0.2464 -0.0792 -0.0862 0.0192  104 LEU A CA  
571  C C   . LEU A 102 ? 0.3166 0.2546 0.2436 -0.0732 -0.0812 0.0151  104 LEU A C   
572  O O   . LEU A 102 ? 0.3253 0.2312 0.2292 -0.0632 -0.0800 0.0065  104 LEU A O   
573  C CB  . LEU A 102 ? 0.2649 0.2603 0.2280 -0.0617 -0.0757 0.0192  104 LEU A CB  
574  C CG  . LEU A 102 ? 0.2566 0.2699 0.2253 -0.0600 -0.0794 0.0207  104 LEU A CG  
575  C CD1 . LEU A 102 ? 0.2236 0.2607 0.2121 -0.0441 -0.0685 0.0225  104 LEU A CD1 
576  C CD2 . LEU A 102 ? 0.2767 0.2595 0.2170 -0.0578 -0.0836 0.0119  104 LEU A CD2 
577  N N   . SER A 103 ? 0.3178 0.2688 0.2585 -0.0775 -0.0775 0.0219  105 SER A N   
578  C CA  . SER A 103 ? 0.3304 0.2570 0.2589 -0.0709 -0.0733 0.0198  105 SER A CA  
579  C C   . SER A 103 ? 0.3786 0.2569 0.2717 -0.0790 -0.0818 0.0163  105 SER A C   
580  O O   . SER A 103 ? 0.3905 0.2404 0.2667 -0.0676 -0.0790 0.0124  105 SER A O   
581  C CB  . SER A 103 ? 0.3222 0.2703 0.2679 -0.0762 -0.0685 0.0286  105 SER A CB  
582  O OG  . SER A 103 ? 0.3387 0.2862 0.2809 -0.0988 -0.0760 0.0368  105 SER A OG  
583  N N   . ASN A 104 ? 0.4122 0.2799 0.2921 -0.0983 -0.0929 0.0179  106 ASN A N   
584  C CA  . ASN A 104 ? 0.4672 0.2814 0.3064 -0.1088 -0.1025 0.0140  106 ASN A CA  
585  C C   . ASN A 104 ? 0.4770 0.2658 0.2914 -0.1016 -0.1061 0.0038  106 ASN A C   
586  O O   . ASN A 104 ? 0.5206 0.2641 0.2973 -0.1129 -0.1157 0.0000  106 ASN A O   
587  C CB  . ASN A 104 ? 0.5086 0.3228 0.3436 -0.1405 -0.1143 0.0233  106 ASN A CB  
588  C CG  . ASN A 104 ? 0.5073 0.3470 0.3645 -0.1487 -0.1093 0.0344  106 ASN A CG  
589  O OD1 . ASN A 104 ? 0.5010 0.3892 0.3900 -0.1600 -0.1087 0.0441  106 ASN A OD1 
590  N ND2 . ASN A 104 ? 0.5263 0.3355 0.3670 -0.1404 -0.1047 0.0336  106 ASN A ND2 
591  N N   . SER A 105 ? 0.4325 0.2467 0.2642 -0.0833 -0.0980 -0.0005 107 SER A N   
592  C CA  . SER A 105 ? 0.4361 0.2334 0.2470 -0.0762 -0.0996 -0.0091 107 SER A CA  
593  C C   . SER A 105 ? 0.4028 0.2063 0.2199 -0.0489 -0.0859 -0.0157 107 SER A C   
594  O O   . SER A 105 ? 0.3942 0.2027 0.2075 -0.0413 -0.0833 -0.0203 107 SER A O   
595  C CB  . SER A 105 ? 0.4258 0.2557 0.2528 -0.0892 -0.1067 -0.0046 107 SER A CB  
596  O OG  . SER A 105 ? 0.4622 0.2938 0.2872 -0.1164 -0.1201 0.0029  107 SER A OG  
597  N N   . LEU A 106 ? 0.3873 0.1929 0.2140 -0.0355 -0.0778 -0.0150 108 LEU A N   
598  C CA  . LEU A 106 ? 0.3618 0.1873 0.2042 -0.0136 -0.0657 -0.0183 108 LEU A CA  
599  C C   . LEU A 106 ? 0.4023 0.1940 0.2152 0.0044  -0.0612 -0.0268 108 LEU A C   
600  O O   . LEU A 106 ? 0.4447 0.1922 0.2243 0.0032  -0.0664 -0.0298 108 LEU A O   
601  C CB  . LEU A 106 ? 0.3341 0.1805 0.2003 -0.0085 -0.0606 -0.0130 108 LEU A CB  
602  C CG  . LEU A 106 ? 0.3043 0.1861 0.1995 -0.0215 -0.0614 -0.0049 108 LEU A CG  
603  C CD1 . LEU A 106 ? 0.2855 0.1811 0.1964 -0.0153 -0.0560 -0.0010 108 LEU A CD1 
604  C CD2 . LEU A 106 ? 0.2780 0.1903 0.1917 -0.0202 -0.0581 -0.0049 108 LEU A CD2 
605  N N   . SER A 107 ? 0.3901 0.2029 0.2149 0.0215  -0.0507 -0.0300 109 SER A N   
606  C CA  . SER A 107 ? 0.4271 0.2193 0.2310 0.0432  -0.0429 -0.0366 109 SER A CA  
607  C C   . SER A 107 ? 0.3970 0.2259 0.2301 0.0600  -0.0322 -0.0343 109 SER A C   
608  O O   . SER A 107 ? 0.3535 0.2208 0.2165 0.0546  -0.0292 -0.0306 109 SER A O   
609  C CB  . SER A 107 ? 0.4573 0.2372 0.2395 0.0451  -0.0408 -0.0429 109 SER A CB  
610  O OG  . SER A 107 ? 0.4864 0.2523 0.2503 0.0687  -0.0301 -0.0489 109 SER A OG  
611  N N   . ALA A 108 ? 0.4150 0.2305 0.2373 0.0805  -0.0270 -0.0363 110 ALA A N   
612  C CA  . ALA A 108 ? 0.3886 0.2414 0.2380 0.0968  -0.0183 -0.0333 110 ALA A CA  
613  C C   . ALA A 108 ? 0.3662 0.2473 0.2261 0.1043  -0.0075 -0.0355 110 ALA A C   
614  O O   . ALA A 108 ? 0.3258 0.2472 0.2139 0.1104  -0.0010 -0.0318 110 ALA A O   
615  C CB  . ALA A 108 ? 0.4248 0.2557 0.2580 0.1189  -0.0163 -0.0338 110 ALA A CB  
616  N N   . ALA A 109 ? 0.3909 0.2495 0.2254 0.1025  -0.0060 -0.0412 111 ALA A N   
617  C CA  . ALA A 109 ? 0.3869 0.2677 0.2258 0.1074  0.0043  -0.0429 111 ALA A CA  
618  C C   . ALA A 109 ? 0.3356 0.2596 0.2095 0.0932  0.0051  -0.0371 111 ALA A C   
619  O O   . ALA A 109 ? 0.3260 0.2812 0.2157 0.0991  0.0152  -0.0353 111 ALA A O   
620  C CB  . ALA A 109 ? 0.4273 0.2723 0.2296 0.1024  0.0021  -0.0493 111 ALA A CB  
621  N N   . GLY A 110 ? 0.3149 0.2390 0.1981 0.0745  -0.0047 -0.0340 112 GLY A N   
622  C CA  . GLY A 110 ? 0.2758 0.2316 0.1853 0.0624  -0.0041 -0.0290 112 GLY A CA  
623  C C   . GLY A 110 ? 0.2495 0.2224 0.1826 0.0573  -0.0080 -0.0240 112 GLY A C   
624  O O   . GLY A 110 ? 0.2241 0.2067 0.1692 0.0448  -0.0116 -0.0206 112 GLY A O   
625  N N   . ARG A 111 ? 0.2597 0.2345 0.1965 0.0687  -0.0071 -0.0235 113 ARG A N   
626  C CA  . ARG A 111 ? 0.2523 0.2385 0.2056 0.0648  -0.0118 -0.0190 113 ARG A CA  
627  C C   . ARG A 111 ? 0.2320 0.2547 0.2089 0.0683  -0.0068 -0.0157 113 ARG A C   
628  O O   . ARG A 111 ? 0.2400 0.2784 0.2208 0.0805  0.0000  -0.0160 113 ARG A O   
629  C CB  . ARG A 111 ? 0.2824 0.2435 0.2212 0.0736  -0.0167 -0.0191 113 ARG A CB  
630  C CG  . ARG A 111 ? 0.2782 0.2481 0.2296 0.0701  -0.0218 -0.0139 113 ARG A CG  
631  C CD  . ARG A 111 ? 0.3072 0.2496 0.2410 0.0808  -0.0261 -0.0131 113 ARG A CD  
632  N NE  . ARG A 111 ? 0.3301 0.2766 0.2610 0.1031  -0.0208 -0.0144 113 ARG A NE  
633  C CZ  . ARG A 111 ? 0.3729 0.2862 0.2791 0.1188  -0.0217 -0.0159 113 ARG A CZ  
634  N NH1 . ARG A 111 ? 0.3963 0.2685 0.2783 0.1111  -0.0291 -0.0158 113 ARG A NH1 
635  N NH2 . ARG A 111 ? 0.3877 0.3076 0.2915 0.1423  -0.0146 -0.0171 113 ARG A NH2 
636  N N   . THR A 112 ? 0.2158 0.2526 0.2073 0.0566  -0.0103 -0.0121 114 THR A N   
637  C CA  . THR A 112 ? 0.2028 0.2703 0.2136 0.0557  -0.0092 -0.0085 114 THR A CA  
638  C C   . THR A 112 ? 0.2029 0.2667 0.2158 0.0533  -0.0168 -0.0056 114 THR A C   
639  O O   . THR A 112 ? 0.1972 0.2466 0.2047 0.0434  -0.0203 -0.0053 114 THR A O   
640  C CB  . THR A 112 ? 0.1944 0.2767 0.2136 0.0417  -0.0063 -0.0074 114 THR A CB  
641  O OG1 . THR A 112 ? 0.1923 0.2731 0.2053 0.0429  0.0003  -0.0095 114 THR A OG1 
642  C CG2 . THR A 112 ? 0.1877 0.3004 0.2240 0.0365  -0.0065 -0.0036 114 THR A CG2 
643  N N   . ARG A 113 ? 0.2144 0.2930 0.2348 0.0637  -0.0189 -0.0028 115 ARG A N   
644  C CA  . ARG A 113 ? 0.2299 0.3056 0.2501 0.0624  -0.0266 0.0007  115 ARG A CA  
645  C C   . ARG A 113 ? 0.2088 0.3154 0.2453 0.0535  -0.0293 0.0040  115 ARG A C   
646  O O   . ARG A 113 ? 0.1990 0.3358 0.2507 0.0563  -0.0265 0.0058  115 ARG A O   
647  C CB  . ARG A 113 ? 0.2684 0.3348 0.2813 0.0809  -0.0294 0.0026  115 ARG A CB  
648  C CG  . ARG A 113 ? 0.3163 0.3446 0.3064 0.0876  -0.0279 -0.0011 115 ARG A CG  
649  C CD  . ARG A 113 ? 0.3706 0.3821 0.3477 0.1078  -0.0301 0.0005  115 ARG A CD  
650  N NE  . ARG A 113 ? 0.4063 0.4120 0.3808 0.1062  -0.0383 0.0059  115 ARG A NE  
651  C CZ  . ARG A 113 ? 0.4780 0.4457 0.4291 0.1096  -0.0430 0.0075  115 ARG A CZ  
652  N NH1 . ARG A 113 ? 0.5311 0.4610 0.4582 0.1132  -0.0413 0.0034  115 ARG A NH1 
653  N NH2 . ARG A 113 ? 0.4724 0.4376 0.4209 0.1083  -0.0500 0.0134  115 ARG A NH2 
654  N N   . VAL A 114 ? 0.2013 0.3001 0.2330 0.0421  -0.0346 0.0052  116 VAL A N   
655  C CA  . VAL A 114 ? 0.2013 0.3202 0.2406 0.0304  -0.0389 0.0075  116 VAL A CA  
656  C C   . VAL A 114 ? 0.2042 0.3146 0.2348 0.0301  -0.0473 0.0105  116 VAL A C   
657  O O   . VAL A 114 ? 0.1855 0.2695 0.2015 0.0289  -0.0470 0.0097  116 VAL A O   
658  C CB  . VAL A 114 ? 0.2077 0.3171 0.2415 0.0149  -0.0348 0.0044  116 VAL A CB  
659  C CG1 . VAL A 114 ? 0.2296 0.3444 0.2601 0.0004  -0.0400 0.0054  116 VAL A CG1 
660  C CG2 . VAL A 114 ? 0.2141 0.3339 0.2553 0.0144  -0.0274 0.0028  116 VAL A CG2 
661  N N   . ARG A 115 ? 0.2223 0.3577 0.2621 0.0308  -0.0549 0.0150  117 ARG A N   
662  C CA  . ARG A 115 ? 0.2566 0.3840 0.2850 0.0283  -0.0640 0.0182  117 ARG A CA  
663  C C   . ARG A 115 ? 0.2356 0.3513 0.2515 0.0095  -0.0644 0.0152  117 ARG A C   
664  O O   . ARG A 115 ? 0.2380 0.3648 0.2592 -0.0022 -0.0628 0.0132  117 ARG A O   
665  C CB  . ARG A 115 ? 0.3094 0.4683 0.3506 0.0357  -0.0738 0.0249  117 ARG A CB  
666  C CG  . ARG A 115 ? 0.3575 0.5568 0.4188 0.0250  -0.0769 0.0269  117 ARG A CG  
667  C CD  . ARG A 115 ? 0.4202 0.6546 0.4942 0.0289  -0.0897 0.0351  117 ARG A CD  
668  N NE  . ARG A 115 ? 0.4889 0.7093 0.5440 0.0179  -0.1012 0.0366  117 ARG A NE  
669  C CZ  . ARG A 115 ? 0.5215 0.7336 0.5633 -0.0050 -0.1055 0.0335  117 ARG A CZ  
670  N NH1 . ARG A 115 ? 0.5358 0.7531 0.5824 -0.0208 -0.1002 0.0297  117 ARG A NH1 
671  N NH2 . ARG A 115 ? 0.5258 0.7203 0.5453 -0.0120 -0.1149 0.0344  117 ARG A NH2 
672  N N   . SER A 116 ? 0.2305 0.3209 0.2267 0.0070  -0.0657 0.0152  118 SER A N   
673  C CA  . SER A 116 ? 0.2244 0.2976 0.2033 -0.0067 -0.0639 0.0118  118 SER A CA  
674  C C   . SER A 116 ? 0.2450 0.3294 0.2175 -0.0184 -0.0745 0.0131  118 SER A C   
675  O O   . SER A 116 ? 0.2432 0.3465 0.2221 -0.0147 -0.0847 0.0183  118 SER A O   
676  C CB  . SER A 116 ? 0.2289 0.2749 0.1893 -0.0039 -0.0599 0.0122  118 SER A CB  
677  O OG  . SER A 116 ? 0.2218 0.2654 0.1732 0.0005  -0.0680 0.0172  118 SER A OG  
678  N N   . GLU A 117 ? 0.2663 0.3360 0.2232 -0.0325 -0.0726 0.0087  119 GLU A N   
679  C CA  . GLU A 117 ? 0.2998 0.3648 0.2375 -0.0466 -0.0825 0.0085  119 GLU A CA  
680  C C   . GLU A 117 ? 0.3154 0.3433 0.2210 -0.0471 -0.0773 0.0051  119 GLU A C   
681  O O   . GLU A 117 ? 0.3030 0.3144 0.2058 -0.0389 -0.0653 0.0031  119 GLU A O   
682  C CB  . GLU A 117 ? 0.3375 0.4065 0.2741 -0.0640 -0.0843 0.0056  119 GLU A CB  
683  C CG  . GLU A 117 ? 0.3449 0.4551 0.3139 -0.0655 -0.0874 0.0098  119 GLU A CG  
684  C CD  . GLU A 117 ? 0.3820 0.4948 0.3457 -0.0881 -0.0909 0.0084  119 GLU A CD  
685  O OE1 . GLU A 117 ? 0.4354 0.5371 0.3772 -0.1043 -0.1013 0.0076  119 GLU A OE1 
686  O OE2 . GLU A 117 ? 0.3900 0.5105 0.3665 -0.0906 -0.0833 0.0080  119 GLU A OE2 
687  N N   . GLN A 118 ? 0.3381 0.3553 0.2193 -0.0567 -0.0865 0.0049  120 GLN A N   
688  C CA  . GLN A 118 ? 0.3728 0.3534 0.2181 -0.0580 -0.0805 0.0011  120 GLN A CA  
689  C C   . GLN A 118 ? 0.3853 0.3403 0.2119 -0.0663 -0.0728 -0.0060 120 GLN A C   
690  O O   . GLN A 118 ? 0.4027 0.3604 0.2269 -0.0812 -0.0802 -0.0080 120 GLN A O   
691  C CB  . GLN A 118 ? 0.4070 0.3812 0.2269 -0.0664 -0.0939 0.0028  120 GLN A CB  
692  C CG  . GLN A 118 ? 0.4439 0.3809 0.2246 -0.0640 -0.0862 -0.0001 120 GLN A CG  
693  C CD  . GLN A 118 ? 0.4383 0.3759 0.2263 -0.0485 -0.0769 0.0048  120 GLN A CD  
694  O OE1 . GLN A 118 ? 0.4175 0.3735 0.2217 -0.0423 -0.0840 0.0116  120 GLN A OE1 
695  N NE2 . GLN A 118 ? 0.4621 0.3789 0.2371 -0.0418 -0.0606 0.0022  120 GLN A NE2 
696  N N   . GLY A 119 ? 0.3831 0.3146 0.1972 -0.0561 -0.0578 -0.0087 121 GLY A N   
697  C CA  . GLY A 119 ? 0.4049 0.3058 0.1956 -0.0590 -0.0490 -0.0150 121 GLY A CA  
698  C C   . GLY A 119 ? 0.3659 0.2772 0.1818 -0.0531 -0.0407 -0.0149 121 GLY A C   
699  O O   . GLY A 119 ? 0.3606 0.2626 0.1765 -0.0406 -0.0279 -0.0152 121 GLY A O   
700  N N   . THR A 120 ? 0.3554 0.2890 0.1932 -0.0624 -0.0484 -0.0136 122 THR A N   
701  C CA  . THR A 120 ? 0.3376 0.2778 0.1936 -0.0600 -0.0418 -0.0137 122 THR A CA  
702  C C   . THR A 120 ? 0.2914 0.2717 0.1844 -0.0598 -0.0473 -0.0091 122 THR A C   
703  O O   . THR A 120 ? 0.3020 0.3035 0.2035 -0.0697 -0.0582 -0.0068 122 THR A O   
704  C CB  . THR A 120 ? 0.3793 0.2937 0.2115 -0.0743 -0.0426 -0.0177 122 THR A CB  
705  O OG1 . THR A 120 ? 0.4371 0.3097 0.2328 -0.0683 -0.0343 -0.0223 122 THR A OG1 
706  C CG2 . THR A 120 ? 0.3654 0.2865 0.2138 -0.0745 -0.0374 -0.0167 122 THR A CG2 
707  N N   . THR A 121 ? 0.2524 0.2439 0.1665 -0.0475 -0.0396 -0.0076 123 THR A N   
708  C CA  . THR A 121 ? 0.2168 0.2405 0.1608 -0.0444 -0.0423 -0.0043 123 THR A CA  
709  C C   . THR A 121 ? 0.2076 0.2309 0.1586 -0.0453 -0.0353 -0.0053 123 THR A C   
710  O O   . THR A 121 ? 0.2149 0.2212 0.1598 -0.0379 -0.0272 -0.0066 123 THR A O   
711  C CB  . THR A 121 ? 0.1963 0.2293 0.1536 -0.0298 -0.0412 -0.0015 123 THR A CB  
712  O OG1 . THR A 121 ? 0.2016 0.2317 0.1484 -0.0297 -0.0477 0.0002  123 THR A OG1 
713  C CG2 . THR A 121 ? 0.1738 0.2337 0.1560 -0.0234 -0.0428 0.0009  123 THR A CG2 
714  N N   . THR A 122 ? 0.2024 0.2475 0.1671 -0.0540 -0.0384 -0.0035 124 THR A N   
715  C CA  . THR A 122 ? 0.1990 0.2419 0.1659 -0.0577 -0.0321 -0.0037 124 THR A CA  
716  C C   . THR A 122 ? 0.1813 0.2546 0.1745 -0.0492 -0.0295 -0.0010 124 THR A C   
717  O O   . THR A 122 ? 0.1798 0.2831 0.1904 -0.0490 -0.0344 0.0020  124 THR A O   
718  C CB  . THR A 122 ? 0.2176 0.2571 0.1734 -0.0787 -0.0363 -0.0032 124 THR A CB  
719  O OG1 . THR A 122 ? 0.2433 0.2507 0.1695 -0.0859 -0.0399 -0.0066 124 THR A OG1 
720  C CG2 . THR A 122 ? 0.2228 0.2506 0.1729 -0.0843 -0.0292 -0.0029 124 THR A CG2 
721  N N   . ILE A 123 ? 0.1738 0.2386 0.1678 -0.0411 -0.0217 -0.0018 125 ILE A N   
722  C CA  . ILE A 123 ? 0.1587 0.2445 0.1700 -0.0328 -0.0179 -0.0004 125 ILE A CA  
723  C C   . ILE A 123 ? 0.1665 0.2476 0.1726 -0.0405 -0.0119 0.0002  125 ILE A C   
724  O O   . ILE A 123 ? 0.1657 0.2215 0.1573 -0.0390 -0.0081 -0.0010 125 ILE A O   
725  C CB  . ILE A 123 ? 0.1569 0.2336 0.1693 -0.0173 -0.0157 -0.0020 125 ILE A CB  
726  C CG1 . ILE A 123 ? 0.1630 0.2360 0.1743 -0.0117 -0.0210 -0.0019 125 ILE A CG1 
727  C CG2 . ILE A 123 ? 0.1555 0.2478 0.1791 -0.0081 -0.0120 -0.0017 125 ILE A CG2 
728  C CD1 . ILE A 123 ? 0.1685 0.2182 0.1645 -0.0136 -0.0205 -0.0030 125 ILE A CD1 
729  N N   . SER A 124 ? 0.1693 0.2769 0.1876 -0.0485 -0.0108 0.0034  126 SER A N   
730  C CA  . SER A 124 ? 0.1879 0.2929 0.2006 -0.0578 -0.0046 0.0054  126 SER A CA  
731  C C   . SER A 124 ? 0.1720 0.2997 0.1985 -0.0470 0.0025  0.0068  126 SER A C   
732  O O   . SER A 124 ? 0.1637 0.3115 0.2048 -0.0337 0.0021  0.0064  126 SER A O   
733  C CB  . SER A 124 ? 0.2126 0.3273 0.2237 -0.0798 -0.0078 0.0090  126 SER A CB  
734  O OG  . SER A 124 ? 0.2244 0.3808 0.2591 -0.0815 -0.0121 0.0124  126 SER A OG  
735  N N   . GLY A 125 ? 0.1762 0.2962 0.1937 -0.0519 0.0094  0.0084  127 GLY A N   
736  C CA  . GLY A 125 ? 0.1707 0.3106 0.1961 -0.0438 0.0178  0.0099  127 GLY A CA  
737  C C   . GLY A 125 ? 0.1677 0.2905 0.1858 -0.0253 0.0193  0.0054  127 GLY A C   
738  O O   . GLY A 125 ? 0.1745 0.3113 0.1975 -0.0138 0.0249  0.0048  127 GLY A O   
739  N N   . LEU A 126 ? 0.1689 0.2616 0.1739 -0.0230 0.0146  0.0028  128 LEU A N   
740  C CA  . LEU A 126 ? 0.1697 0.2467 0.1675 -0.0101 0.0138  -0.0003 128 LEU A CA  
741  C C   . LEU A 126 ? 0.1791 0.2448 0.1626 -0.0107 0.0188  0.0009  128 LEU A C   
742  O O   . LEU A 126 ? 0.1816 0.2364 0.1551 -0.0205 0.0205  0.0040  128 LEU A O   
743  C CB  . LEU A 126 ? 0.1691 0.2260 0.1616 -0.0089 0.0075  -0.0015 128 LEU A CB  
744  C CG  . LEU A 126 ? 0.1582 0.2219 0.1603 -0.0075 0.0023  -0.0026 128 LEU A CG  
745  C CD1 . LEU A 126 ? 0.1547 0.1999 0.1495 -0.0081 -0.0011 -0.0028 128 LEU A CD1 
746  C CD2 . LEU A 126 ? 0.1650 0.2364 0.1737 0.0041  0.0011  -0.0046 128 LEU A CD2 
747  N N   . LYS A 127 ? 0.1855 0.2501 0.1642 -0.0002 0.0207  -0.0015 129 LYS A N   
748  C CA  . LYS A 127 ? 0.1953 0.2449 0.1563 0.0005  0.0230  -0.0008 129 LYS A CA  
749  C C   . LYS A 127 ? 0.1829 0.2113 0.1356 -0.0010 0.0162  0.0006  129 LYS A C   
750  O O   . LYS A 127 ? 0.1595 0.1851 0.1193 0.0016  0.0102  -0.0006 129 LYS A O   
751  C CB  . LYS A 127 ? 0.2218 0.2680 0.1742 0.0118  0.0241  -0.0050 129 LYS A CB  
752  C CG  . LYS A 127 ? 0.2506 0.3176 0.2090 0.0186  0.0332  -0.0061 129 LYS A CG  
753  C CD  . LYS A 127 ? 0.2887 0.3431 0.2303 0.0317  0.0350  -0.0113 129 LYS A CD  
754  C CE  . LYS A 127 ? 0.3152 0.3901 0.2631 0.0440  0.0450  -0.0126 129 LYS A CE  
755  N NZ  . LYS A 127 ? 0.3656 0.4175 0.2918 0.0585  0.0449  -0.0192 129 LYS A NZ  
756  N N   . PRO A 128 ? 0.1867 0.2009 0.1239 -0.0042 0.0174  0.0043  130 PRO A N   
757  C CA  . PRO A 128 ? 0.1889 0.1864 0.1195 -0.0022 0.0116  0.0070  130 PRO A CA  
758  C C   . PRO A 128 ? 0.1787 0.1759 0.1117 0.0054  0.0039  0.0053  130 PRO A C   
759  O O   . PRO A 128 ? 0.1846 0.1831 0.1122 0.0081  0.0027  0.0025  130 PRO A O   
760  C CB  . PRO A 128 ? 0.2140 0.1963 0.1248 -0.0049 0.0144  0.0120  130 PRO A CB  
761  C CG  . PRO A 128 ? 0.2238 0.2162 0.1324 -0.0127 0.0234  0.0123  130 PRO A CG  
762  C CD  . PRO A 128 ? 0.2073 0.2214 0.1317 -0.0081 0.0249  0.0069  130 PRO A CD  
763  N N   . GLY A 129 ? 0.1671 0.1617 0.1058 0.0083  -0.0010 0.0075  131 GLY A N   
764  C CA  . GLY A 129 ? 0.1645 0.1625 0.1068 0.0124  -0.0090 0.0084  131 GLY A CA  
765  C C   . GLY A 129 ? 0.1494 0.1556 0.1071 0.0137  -0.0116 0.0084  131 GLY A C   
766  O O   . GLY A 129 ? 0.1474 0.1519 0.1089 0.0137  -0.0075 0.0087  131 GLY A O   
767  N N   . TYR A 130 ? 0.1442 0.1569 0.1074 0.0132  -0.0185 0.0081  132 TYR A N   
768  C CA  . TYR A 130 ? 0.1322 0.1544 0.1089 0.0130  -0.0214 0.0101  132 TYR A CA  
769  C C   . TYR A 130 ? 0.1281 0.1490 0.1075 0.0096  -0.0219 0.0051  132 TYR A C   
770  O O   . TYR A 130 ? 0.1375 0.1510 0.1078 0.0082  -0.0244 0.0012  132 TYR A O   
771  C CB  . TYR A 130 ? 0.1395 0.1710 0.1191 0.0119  -0.0301 0.0152  132 TYR A CB  
772  C CG  . TYR A 130 ? 0.1324 0.1816 0.1282 0.0129  -0.0321 0.0216  132 TYR A CG  
773  C CD1 . TYR A 130 ? 0.1294 0.1827 0.1315 0.0209  -0.0248 0.0246  132 TYR A CD1 
774  C CD2 . TYR A 130 ? 0.1362 0.1982 0.1388 0.0056  -0.0413 0.0252  132 TYR A CD2 
775  C CE1 . TYR A 130 ? 0.1235 0.1964 0.1404 0.0242  -0.0246 0.0312  132 TYR A CE1 
776  C CE2 . TYR A 130 ? 0.1296 0.2149 0.1498 0.0059  -0.0424 0.0329  132 TYR A CE2 
777  C CZ  . TYR A 130 ? 0.1260 0.2186 0.1543 0.0167  -0.0331 0.0362  132 TYR A CZ  
778  O OH  . TYR A 130 ? 0.1286 0.2479 0.1748 0.0180  -0.0328 0.0444  132 TYR A OH  
779  N N   . TYR A 131 ? 0.1144 0.1395 0.1029 0.0097  -0.0196 0.0054  133 TYR A N   
780  C CA  . TYR A 131 ? 0.1144 0.1370 0.1044 0.0081  -0.0202 0.0019  133 TYR A CA  
781  C C   . TYR A 131 ? 0.1101 0.1374 0.1074 0.0050  -0.0233 0.0054  133 TYR A C   
782  O O   . TYR A 131 ? 0.1079 0.1440 0.1122 0.0062  -0.0210 0.0097  133 TYR A O   
783  C CB  . TYR A 131 ? 0.1094 0.1330 0.1012 0.0096  -0.0145 -0.0004 133 TYR A CB  
784  C CG  . TYR A 131 ? 0.1144 0.1377 0.1009 0.0106  -0.0110 -0.0033 133 TYR A CG  
785  C CD1 . TYR A 131 ? 0.1192 0.1406 0.1004 0.0093  -0.0073 -0.0018 133 TYR A CD1 
786  C CD2 . TYR A 131 ? 0.1185 0.1434 0.1044 0.0139  -0.0104 -0.0067 133 TYR A CD2 
787  C CE1 . TYR A 131 ? 0.1271 0.1506 0.1034 0.0087  -0.0029 -0.0032 133 TYR A CE1 
788  C CE2 . TYR A 131 ? 0.1237 0.1539 0.1068 0.0160  -0.0051 -0.0083 133 TYR A CE2 
789  C CZ  . TYR A 131 ? 0.1256 0.1563 0.1044 0.0120  -0.0011 -0.0064 133 TYR A CZ  
790  O OH  . TYR A 131 ? 0.1356 0.1737 0.1115 0.0127  0.0052  -0.0070 133 TYR A OH  
791  N N   . LEU A 132 ? 0.1216 0.1410 0.1147 0.0020  -0.0276 0.0036  134 LEU A N   
792  C CA  . LEU A 132 ? 0.1265 0.1472 0.1236 -0.0027 -0.0298 0.0071  134 LEU A CA  
793  C C   . LEU A 132 ? 0.1282 0.1444 0.1244 0.0010  -0.0267 0.0049  134 LEU A C   
794  O O   . LEU A 132 ? 0.1397 0.1478 0.1299 0.0056  -0.0269 0.0007  134 LEU A O   
795  C CB  . LEU A 132 ? 0.1463 0.1554 0.1344 -0.0107 -0.0379 0.0076  134 LEU A CB  
796  C CG  . LEU A 132 ? 0.1537 0.1600 0.1422 -0.0185 -0.0406 0.0121  134 LEU A CG  
797  C CD1 . LEU A 132 ? 0.1752 0.1767 0.1579 -0.0321 -0.0497 0.0156  134 LEU A CD1 
798  C CD2 . LEU A 132 ? 0.1649 0.1517 0.1422 -0.0139 -0.0403 0.0086  134 LEU A CD2 
799  N N   . ILE A 133 ? 0.1208 0.1435 0.1221 0.0001  -0.0237 0.0084  135 ILE A N   
800  C CA  . ILE A 133 ? 0.1220 0.1413 0.1207 0.0025  -0.0222 0.0072  135 ILE A CA  
801  C C   . ILE A 133 ? 0.1332 0.1471 0.1285 -0.0019 -0.0246 0.0115  135 ILE A C   
802  O O   . ILE A 133 ? 0.1356 0.1570 0.1349 -0.0071 -0.0231 0.0167  135 ILE A O   
803  C CB  . ILE A 133 ? 0.1183 0.1434 0.1184 0.0047  -0.0166 0.0069  135 ILE A CB  
804  C CG1 . ILE A 133 ? 0.1184 0.1451 0.1189 0.0067  -0.0143 0.0041  135 ILE A CG1 
805  C CG2 . ILE A 133 ? 0.1196 0.1416 0.1149 0.0051  -0.0173 0.0056  135 ILE A CG2 
806  C CD1 . ILE A 133 ? 0.1231 0.1472 0.1188 0.0075  -0.0093 0.0037  135 ILE A CD1 
807  N N   . LYS A 134 ? 0.1427 0.1447 0.1301 0.0004  -0.0281 0.0102  136 LYS A N   
808  C CA  . LYS A 134 ? 0.1615 0.1531 0.1411 -0.0037 -0.0306 0.0148  136 LYS A CA  
809  C C   . LYS A 134 ? 0.1663 0.1513 0.1393 0.0032  -0.0328 0.0137  136 LYS A C   
810  O O   . LYS A 134 ? 0.1533 0.1439 0.1301 0.0107  -0.0332 0.0096  136 LYS A O   
811  C CB  . LYS A 134 ? 0.1856 0.1596 0.1554 -0.0094 -0.0364 0.0160  136 LYS A CB  
812  C CG  . LYS A 134 ? 0.2096 0.1675 0.1698 -0.0008 -0.0398 0.0102  136 LYS A CG  
813  C CD  . LYS A 134 ? 0.2535 0.1850 0.1962 -0.0064 -0.0458 0.0099  136 LYS A CD  
814  C CE  . LYS A 134 ? 0.2915 0.2008 0.2190 -0.0126 -0.0498 0.0151  136 LYS A CE  
815  N NZ  . LYS A 134 ? 0.3469 0.2191 0.2489 -0.0139 -0.0561 0.0127  136 LYS A NZ  
816  N N   . ASP A 135 ? 0.1799 0.1554 0.1436 0.0003  -0.0345 0.0185  137 ASP A N   
817  C CA  . ASP A 135 ? 0.2001 0.1659 0.1546 0.0077  -0.0391 0.0193  137 ASP A CA  
818  C C   . ASP A 135 ? 0.2229 0.1667 0.1663 0.0133  -0.0441 0.0186  137 ASP A C   
819  O O   . ASP A 135 ? 0.2387 0.1656 0.1732 0.0058  -0.0456 0.0201  137 ASP A O   
820  C CB  . ASP A 135 ? 0.2151 0.1751 0.1593 0.0026  -0.0389 0.0254  137 ASP A CB  
821  C CG  . ASP A 135 ? 0.2135 0.1882 0.1604 0.0021  -0.0351 0.0245  137 ASP A CG  
822  O OD1 . ASP A 135 ? 0.2208 0.2009 0.1678 0.0078  -0.0392 0.0223  137 ASP A OD1 
823  O OD2 . ASP A 135 ? 0.2150 0.1962 0.1631 -0.0037 -0.0282 0.0262  137 ASP A OD2 
824  N N   . SER A 136 ? 0.2280 0.1718 0.1704 0.0268  -0.0470 0.0168  138 SER A N   
825  C CA  . SER A 136 ? 0.2555 0.1748 0.1831 0.0373  -0.0505 0.0159  138 SER A CA  
826  C C   . SER A 136 ? 0.2849 0.1712 0.1897 0.0321  -0.0550 0.0216  138 SER A C   
827  O O   . SER A 136 ? 0.2848 0.1715 0.1858 0.0284  -0.0565 0.0273  138 SER A O   
828  C CB  . SER A 136 ? 0.2604 0.1929 0.1942 0.0549  -0.0517 0.0151  138 SER A CB  
829  O OG  . SER A 136 ? 0.2996 0.2065 0.2166 0.0698  -0.0536 0.0143  138 SER A OG  
830  N N   . ASN A 137 ? 0.3113 0.1657 0.1970 0.0305  -0.0573 0.0204  139 ASN A N   
831  C CA  . ASN A 137 ? 0.3558 0.1737 0.2162 0.0206  -0.0620 0.0263  139 ASN A CA  
832  C C   . ASN A 137 ? 0.3785 0.1788 0.2234 0.0331  -0.0659 0.0316  139 ASN A C   
833  O O   . ASN A 137 ? 0.3983 0.1928 0.2386 0.0540  -0.0674 0.0294  139 ASN A O   
834  C CB  . ASN A 137 ? 0.3939 0.1731 0.2299 0.0174  -0.0654 0.0229  139 ASN A CB  
835  C CG  . ASN A 137 ? 0.3811 0.1744 0.2282 0.0010  -0.0643 0.0197  139 ASN A CG  
836  O OD1 . ASN A 137 ? 0.3561 0.1844 0.2272 -0.0093 -0.0607 0.0220  139 ASN A OD1 
837  N ND2 . ASN A 137 ? 0.4141 0.1786 0.2412 -0.0007 -0.0677 0.0148  139 ASN A ND2 
838  N N   . GLY A 138 ? 0.3895 0.1828 0.2260 0.0211  -0.0673 0.0395  140 GLY A N   
839  C CA  . GLY A 138 ? 0.4222 0.1929 0.2384 0.0305  -0.0723 0.0463  140 GLY A CA  
840  C C   . GLY A 138 ? 0.4019 0.2046 0.2343 0.0446  -0.0731 0.0471  140 GLY A C   
841  O O   . GLY A 138 ? 0.4338 0.2228 0.2513 0.0550  -0.0786 0.0531  140 GLY A O   
842  N N   . SER A 139 ? 0.3547 0.1985 0.2154 0.0434  -0.0688 0.0418  141 SER A N   
843  C CA  . SER A 139 ? 0.3381 0.2130 0.2143 0.0540  -0.0710 0.0416  141 SER A CA  
844  C C   . SER A 139 ? 0.3440 0.2246 0.2142 0.0448  -0.0726 0.0474  141 SER A C   
845  O O   . SER A 139 ? 0.3458 0.2421 0.2189 0.0528  -0.0781 0.0496  141 SER A O   
846  C CB  . SER A 139 ? 0.2948 0.2049 0.1981 0.0534  -0.0660 0.0341  141 SER A CB  
847  O OG  . SER A 139 ? 0.2687 0.1887 0.1796 0.0362  -0.0599 0.0321  141 SER A OG  
848  N N   . LEU A 140 ? 0.3589 0.2274 0.2193 0.0281  -0.0679 0.0506  142 LEU A N   
849  C CA  . LEU A 140 ? 0.3672 0.2398 0.2188 0.0191  -0.0665 0.0557  142 LEU A CA  
850  C C   . LEU A 140 ? 0.4093 0.2482 0.2327 0.0127  -0.0683 0.0653  142 LEU A C   
851  O O   . LEU A 140 ? 0.4094 0.2484 0.2225 0.0020  -0.0641 0.0705  142 LEU A O   
852  C CB  . LEU A 140 ? 0.3384 0.2317 0.2039 0.0058  -0.0564 0.0523  142 LEU A CB  
853  C CG  . LEU A 140 ? 0.3089 0.2299 0.1980 0.0095  -0.0539 0.0435  142 LEU A CG  
854  C CD1 . LEU A 140 ? 0.2901 0.2251 0.1890 -0.0009 -0.0437 0.0414  142 LEU A CD1 
855  C CD2 . LEU A 140 ? 0.3028 0.2395 0.1942 0.0163  -0.0595 0.0416  142 LEU A CD2 
856  N N   . ASP A 141 ? 0.4407 0.2476 0.2481 0.0191  -0.0737 0.0680  143 ASP A N   
857  C CA  . ASP A 141 ? 0.4894 0.2585 0.2667 0.0100  -0.0753 0.0775  143 ASP A CA  
858  C C   . ASP A 141 ? 0.5144 0.2777 0.2739 0.0168  -0.0807 0.0850  143 ASP A C   
859  O O   . ASP A 141 ? 0.5228 0.2910 0.2834 0.0357  -0.0888 0.0844  143 ASP A O   
860  C CB  . ASP A 141 ? 0.5298 0.2573 0.2875 0.0150  -0.0802 0.0779  143 ASP A CB  
861  C CG  . ASP A 141 ? 0.5285 0.2554 0.2956 0.0011  -0.0758 0.0725  143 ASP A CG  
862  O OD1 . ASP A 141 ? 0.4919 0.2532 0.2830 -0.0116 -0.0686 0.0699  143 ASP A OD1 
863  O OD2 . ASP A 141 ? 0.5770 0.2673 0.3252 0.0037  -0.0798 0.0711  143 ASP A OD2 
864  N N   . ASN A 142 ? 0.5349 0.2911 0.2788 0.0010  -0.0760 0.0926  144 ASN A N   
865  C CA  . ASN A 142 ? 0.5639 0.3093 0.2841 0.0041  -0.0806 0.1009  144 ASN A CA  
866  C C   . ASN A 142 ? 0.5258 0.3051 0.2601 0.0134  -0.0838 0.0959  144 ASN A C   
867  O O   . ASN A 142 ? 0.5407 0.3141 0.2587 0.0229  -0.0930 0.1011  144 ASN A O   
868  C CB  . ASN A 142 ? 0.6289 0.3323 0.3202 0.0171  -0.0915 0.1085  144 ASN A CB  
869  C CG  . ASN A 142 ? 0.6828 0.3442 0.3529 0.0046  -0.0895 0.1134  144 ASN A CG  
870  O OD1 . ASN A 142 ? 0.7220 0.3560 0.3840 0.0154  -0.0947 0.1112  144 ASN A OD1 
871  N ND2 . ASN A 142 ? 0.7047 0.3610 0.3647 -0.0188 -0.0815 0.1202  144 ASN A ND2 
872  N N   . VAL A 143 ? 0.4703 0.2830 0.2317 0.0094  -0.0769 0.0866  145 VAL A N   
873  C CA  . VAL A 143 ? 0.4451 0.2852 0.2150 0.0125  -0.0790 0.0817  145 VAL A CA  
874  C C   . VAL A 143 ? 0.4295 0.2756 0.1913 -0.0017 -0.0672 0.0818  145 VAL A C   
875  O O   . VAL A 143 ? 0.4033 0.2590 0.1788 -0.0103 -0.0556 0.0788  145 VAL A O   
876  C CB  . VAL A 143 ? 0.4176 0.2867 0.2190 0.0195  -0.0802 0.0715  145 VAL A CB  
877  C CG1 . VAL A 143 ? 0.4154 0.3088 0.2215 0.0197  -0.0847 0.0673  145 VAL A CG1 
878  C CG2 . VAL A 143 ? 0.4247 0.2890 0.2340 0.0355  -0.0883 0.0717  145 VAL A CG2 
879  N N   . LYS A 144 ? 0.4376 0.2783 0.1757 -0.0025 -0.0706 0.0857  146 LYS A N   
880  C CA  . LYS A 144 ? 0.4392 0.2797 0.1611 -0.0132 -0.0584 0.0869  146 LYS A CA  
881  C C   . LYS A 144 ? 0.4037 0.2676 0.1419 -0.0143 -0.0511 0.0760  146 LYS A C   
882  O O   . LYS A 144 ? 0.3863 0.2636 0.1376 -0.0088 -0.0596 0.0690  146 LYS A O   
883  C CB  . LYS A 144 ? 0.4749 0.2989 0.1616 -0.0128 -0.0652 0.0935  146 LYS A CB  
884  C CG  . LYS A 144 ? 0.5125 0.3068 0.1746 -0.0134 -0.0696 0.1063  146 LYS A CG  
885  C CD  . LYS A 144 ? 0.5515 0.3301 0.1762 -0.0139 -0.0751 0.1131  146 LYS A CD  
886  C CE  . LYS A 144 ? 0.5950 0.3400 0.1917 -0.0144 -0.0796 0.1269  146 LYS A CE  
887  N NZ  . LYS A 144 ? 0.6400 0.3687 0.1964 -0.0177 -0.0814 0.1344  146 LYS A NZ  
888  N N   . GLY A 145 ? 0.3979 0.2670 0.1355 -0.0213 -0.0347 0.0757  147 GLY A N   
889  C CA  . GLY A 145 ? 0.3809 0.2645 0.1252 -0.0207 -0.0257 0.0665  147 GLY A CA  
890  C C   . GLY A 145 ? 0.3473 0.2490 0.1251 -0.0173 -0.0264 0.0585  147 GLY A C   
891  O O   . GLY A 145 ? 0.3383 0.2474 0.1194 -0.0154 -0.0247 0.0502  147 GLY A O   
892  N N   . GLN A 146 ? 0.3327 0.2376 0.1306 -0.0174 -0.0291 0.0611  148 GLN A N   
893  C CA  . GLN A 146 ? 0.3134 0.2339 0.1402 -0.0145 -0.0292 0.0542  148 GLN A CA  
894  C C   . GLN A 146 ? 0.2907 0.2162 0.1319 -0.0204 -0.0210 0.0583  148 GLN A C   
895  O O   . GLN A 146 ? 0.3008 0.2169 0.1310 -0.0276 -0.0176 0.0670  148 GLN A O   
896  C CB  . GLN A 146 ? 0.3262 0.2467 0.1630 -0.0072 -0.0433 0.0519  148 GLN A CB  
897  C CG  . GLN A 146 ? 0.3531 0.2771 0.1813 -0.0032 -0.0538 0.0492  148 GLN A CG  
898  C CD  . GLN A 146 ? 0.3637 0.2979 0.1928 -0.0064 -0.0501 0.0412  148 GLN A CD  
899  O OE1 . GLN A 146 ? 0.3709 0.3168 0.2188 -0.0064 -0.0455 0.0351  148 GLN A OE1 
900  N NE2 . GLN A 146 ? 0.4110 0.3364 0.2149 -0.0098 -0.0526 0.0411  148 GLN A NE2 
901  N N   . ALA A 147 ? 0.2594 0.2004 0.1241 -0.0188 -0.0183 0.0526  149 ALA A N   
902  C CA  . ALA A 147 ? 0.2460 0.1958 0.1267 -0.0253 -0.0130 0.0559  149 ALA A CA  
903  C C   . ALA A 147 ? 0.2160 0.1745 0.1176 -0.0211 -0.0172 0.0488  149 ALA A C   
904  O O   . ALA A 147 ? 0.1999 0.1647 0.1070 -0.0141 -0.0189 0.0414  149 ALA A O   
905  C CB  . ALA A 147 ? 0.2444 0.2116 0.1287 -0.0285 0.0014  0.0592  149 ALA A CB  
906  N N   . TYR A 148 ? 0.2113 0.1680 0.1215 -0.0273 -0.0194 0.0515  150 TYR A N   
907  C CA  . TYR A 148 ? 0.1907 0.1547 0.1178 -0.0246 -0.0224 0.0455  150 TYR A CA  
908  C C   . TYR A 148 ? 0.1687 0.1571 0.1123 -0.0242 -0.0135 0.0438  150 TYR A C   
909  O O   . TYR A 148 ? 0.1695 0.1711 0.1164 -0.0294 -0.0053 0.0498  150 TYR A O   
910  C CB  . TYR A 148 ? 0.2024 0.1521 0.1271 -0.0329 -0.0282 0.0488  150 TYR A CB  
911  C CG  . TYR A 148 ? 0.2276 0.1470 0.1333 -0.0282 -0.0374 0.0491  150 TYR A CG  
912  C CD1 . TYR A 148 ? 0.2549 0.1545 0.1402 -0.0330 -0.0390 0.0568  150 TYR A CD1 
913  C CD2 . TYR A 148 ? 0.2253 0.1357 0.1319 -0.0174 -0.0434 0.0424  150 TYR A CD2 
914  C CE1 . TYR A 148 ? 0.2824 0.1515 0.1479 -0.0262 -0.0475 0.0581  150 TYR A CE1 
915  C CE2 . TYR A 148 ? 0.2530 0.1362 0.1416 -0.0091 -0.0507 0.0433  150 TYR A CE2 
916  C CZ  . TYR A 148 ? 0.2820 0.1435 0.1498 -0.0128 -0.0532 0.0512  150 TYR A CZ  
917  O OH  . TYR A 148 ? 0.3147 0.1468 0.1625 -0.0022 -0.0606 0.0529  150 TYR A OH  
918  N N   . THR A 149 ? 0.1519 0.1469 0.1055 -0.0171 -0.0146 0.0364  151 THR A N   
919  C CA  . THR A 149 ? 0.1430 0.1562 0.1093 -0.0144 -0.0071 0.0349  151 THR A CA  
920  C C   . THR A 149 ? 0.1385 0.1653 0.1188 -0.0216 -0.0068 0.0400  151 THR A C   
921  O O   . THR A 149 ? 0.1445 0.1617 0.1244 -0.0278 -0.0148 0.0403  151 THR A O   
922  C CB  . THR A 149 ? 0.1315 0.1447 0.1020 -0.0071 -0.0091 0.0268  151 THR A CB  
923  O OG1 . THR A 149 ? 0.1242 0.1495 0.1015 -0.0030 -0.0012 0.0264  151 THR A OG1 
924  C CG2 . THR A 149 ? 0.1272 0.1367 0.1042 -0.0072 -0.0167 0.0235  151 THR A CG2 
925  N N   . SER A 150 ? 0.1359 0.1843 0.1269 -0.0199 0.0020  0.0441  152 SER A N   
926  C CA  . SER A 150 ? 0.1317 0.2007 0.1407 -0.0244 0.0009  0.0483  152 SER A CA  
927  C C   . SER A 150 ? 0.1249 0.1866 0.1368 -0.0203 -0.0060 0.0408  152 SER A C   
928  O O   . SER A 150 ? 0.1209 0.1760 0.1287 -0.0106 -0.0038 0.0343  152 SER A O   
929  C CB  . SER A 150 ? 0.1278 0.2246 0.1493 -0.0178 0.0121  0.0540  152 SER A CB  
930  O OG  . SER A 150 ? 0.1351 0.2416 0.1538 -0.0213 0.0206  0.0616  152 SER A OG  
931  N N   . ILE A 151 ? 0.1300 0.1903 0.1457 -0.0293 -0.0146 0.0419  153 ILE A N   
932  C CA  . ILE A 151 ? 0.1316 0.1837 0.1468 -0.0257 -0.0204 0.0351  153 ILE A CA  
933  C C   . ILE A 151 ? 0.1143 0.1853 0.1411 -0.0168 -0.0151 0.0353  153 ILE A C   
934  O O   . ILE A 151 ? 0.1108 0.2056 0.1505 -0.0176 -0.0116 0.0426  153 ILE A O   
935  C CB  . ILE A 151 ? 0.1542 0.1978 0.1657 -0.0380 -0.0306 0.0365  153 ILE A CB  
936  C CG1 . ILE A 151 ? 0.1729 0.1863 0.1655 -0.0420 -0.0357 0.0343  153 ILE A CG1 
937  C CG2 . ILE A 151 ? 0.1514 0.1931 0.1632 -0.0347 -0.0352 0.0312  153 ILE A CG2 
938  C CD1 . ILE A 151 ? 0.1994 0.1960 0.1810 -0.0557 -0.0453 0.0359  153 ILE A CD1 
939  N N   . MET A 152 ? 0.1046 0.1649 0.1260 -0.0082 -0.0144 0.0280  154 MET A N   
940  C CA  . MET A 152 ? 0.1039 0.1719 0.1291 0.0010  -0.0093 0.0274  154 MET A CA  
941  C C   . MET A 152 ? 0.0994 0.1642 0.1246 0.0009  -0.0152 0.0244  154 MET A C   
942  O O   . MET A 152 ? 0.0983 0.1492 0.1161 -0.0022 -0.0203 0.0193  154 MET A O   
943  C CB  . MET A 152 ? 0.1101 0.1641 0.1241 0.0080  -0.0037 0.0220  154 MET A CB  
944  C CG  . MET A 152 ? 0.1252 0.1779 0.1332 0.0091  0.0021  0.0239  154 MET A CG  
945  S SD  . MET A 152 ? 0.1490 0.1807 0.1389 0.0117  0.0038  0.0166  154 MET A SD  
946  C CE  . MET A 152 ? 0.1621 0.1885 0.1454 0.0215  0.0113  0.0154  154 MET A CE  
947  N N   . LEU A 153 ? 0.0995 0.1771 0.1314 0.0062  -0.0140 0.0281  155 LEU A N   
948  C CA  . LEU A 153 ? 0.1067 0.1789 0.1345 0.0082  -0.0179 0.0255  155 LEU A CA  
949  C C   . LEU A 153 ? 0.1183 0.1828 0.1395 0.0189  -0.0107 0.0240  155 LEU A C   
950  O O   . LEU A 153 ? 0.1179 0.1905 0.1425 0.0274  -0.0047 0.0286  155 LEU A O   
951  C CB  . LEU A 153 ? 0.1096 0.2006 0.1472 0.0043  -0.0249 0.0322  155 LEU A CB  
952  C CG  . LEU A 153 ? 0.1178 0.2088 0.1555 -0.0101 -0.0342 0.0331  155 LEU A CG  
953  C CD1 . LEU A 153 ? 0.1245 0.2400 0.1741 -0.0169 -0.0422 0.0416  155 LEU A CD1 
954  C CD2 . LEU A 153 ? 0.1242 0.1892 0.1446 -0.0132 -0.0388 0.0246  155 LEU A CD2 
955  N N   . GLN A 154 ? 0.1315 0.1794 0.1418 0.0183  -0.0108 0.0180  156 GLN A N   
956  C CA  . GLN A 154 ? 0.1522 0.1862 0.1514 0.0241  -0.0048 0.0162  156 GLN A CA  
957  C C   . GLN A 154 ? 0.1509 0.1759 0.1420 0.0225  -0.0066 0.0141  156 GLN A C   
958  O O   . GLN A 154 ? 0.1400 0.1647 0.1307 0.0168  -0.0100 0.0105  156 GLN A O   
959  C CB  . GLN A 154 ? 0.1772 0.2000 0.1693 0.0209  -0.0014 0.0113  156 GLN A CB  
960  C CG  . GLN A 154 ? 0.2100 0.2371 0.2043 0.0227  0.0017  0.0131  156 GLN A CG  
961  C CD  . GLN A 154 ? 0.2538 0.2798 0.2437 0.0335  0.0089  0.0172  156 GLN A CD  
962  O OE1 . GLN A 154 ? 0.2627 0.2707 0.2380 0.0386  0.0126  0.0157  156 GLN A OE1 
963  N NE2 . GLN A 154 ? 0.2572 0.3023 0.2589 0.0373  0.0110  0.0231  156 GLN A NE2 
964  N N   . VAL A 155 ? 0.1575 0.1726 0.1389 0.0288  -0.0033 0.0166  157 VAL A N   
965  C CA  . VAL A 155 ? 0.1646 0.1666 0.1336 0.0263  -0.0030 0.0154  157 VAL A CA  
966  C C   . VAL A 155 ? 0.1734 0.1616 0.1332 0.0194  0.0012  0.0108  157 VAL A C   
967  O O   . VAL A 155 ? 0.1823 0.1597 0.1352 0.0210  0.0048  0.0101  157 VAL A O   
968  C CB  . VAL A 155 ? 0.1785 0.1718 0.1378 0.0357  -0.0019 0.0212  157 VAL A CB  
969  C CG1 . VAL A 155 ? 0.1964 0.1715 0.1384 0.0318  -0.0006 0.0208  157 VAL A CG1 
970  C CG2 . VAL A 155 ? 0.1737 0.1873 0.1450 0.0411  -0.0083 0.0271  157 VAL A CG2 
971  N N   . ALA A 156 ? 0.1727 0.1631 0.1319 0.0116  0.0008  0.0078  158 ALA A N   
972  C CA  . ALA A 156 ? 0.1874 0.1717 0.1409 0.0026  0.0037  0.0052  158 ALA A CA  
973  C C   . ALA A 156 ? 0.2060 0.1677 0.1398 0.0000  0.0073  0.0077  158 ALA A C   
974  O O   . ALA A 156 ? 0.2111 0.1701 0.1385 -0.0016 0.0083  0.0100  158 ALA A O   
975  C CB  . ALA A 156 ? 0.1777 0.1781 0.1403 -0.0026 0.0033  0.0027  158 ALA A CB  
976  N N   . LYS A 157 ? 0.2194 0.1607 0.1392 -0.0003 0.0093  0.0075  159 LYS A N   
977  C CA  . LYS A 157 ? 0.2535 0.1642 0.1484 -0.0008 0.0124  0.0103  159 LYS A CA  
978  C C   . LYS A 157 ? 0.2666 0.1521 0.1415 -0.0118 0.0138  0.0077  159 LYS A C   
979  O O   . LYS A 157 ? 0.2973 0.1484 0.1460 -0.0078 0.0165  0.0089  159 LYS A O   
980  C CB  . LYS A 157 ? 0.2714 0.1724 0.1605 0.0170  0.0136  0.0144  159 LYS A CB  
981  C CG  . LYS A 157 ? 0.2751 0.1811 0.1705 0.0278  0.0150  0.0135  159 LYS A CG  
982  C CD  . LYS A 157 ? 0.3186 0.2123 0.2040 0.0465  0.0184  0.0189  159 LYS A CD  
983  C CE  . LYS A 157 ? 0.3298 0.2326 0.2221 0.0593  0.0223  0.0194  159 LYS A CE  
984  N NZ  . LYS A 157 ? 0.3170 0.2598 0.2398 0.0629  0.0182  0.0231  159 LYS A NZ  
985  N N   . ASP A 158 ? 0.2527 0.1541 0.1378 -0.0253 0.0111  0.0044  160 ASP A N   
986  C CA  . ASP A 158 ? 0.2810 0.1632 0.1481 -0.0409 0.0096  0.0021  160 ASP A CA  
987  C C   . ASP A 158 ? 0.3098 0.1623 0.1555 -0.0322 0.0110  -0.0005 160 ASP A C   
988  O O   . ASP A 158 ? 0.3530 0.1655 0.1663 -0.0370 0.0124  -0.0013 160 ASP A O   
989  C CB  . ASP A 158 ? 0.3068 0.1673 0.1534 -0.0558 0.0110  0.0053  160 ASP A CB  
990  C CG  . ASP A 158 ? 0.2875 0.1795 0.1538 -0.0645 0.0118  0.0085  160 ASP A CG  
991  O OD1 . ASP A 158 ? 0.2542 0.1836 0.1486 -0.0613 0.0103  0.0071  160 ASP A OD1 
992  O OD2 . ASP A 158 ? 0.3060 0.1826 0.1568 -0.0732 0.0146  0.0126  160 ASP A OD2 
993  N N   . THR A 159 ? 0.2957 0.1647 0.1564 -0.0183 0.0116  -0.0017 161 THR A N   
994  C CA  . THR A 159 ? 0.3259 0.1718 0.1677 -0.0082 0.0150  -0.0039 161 THR A CA  
995  C C   . THR A 159 ? 0.3104 0.1791 0.1679 -0.0093 0.0121  -0.0065 161 THR A C   
996  O O   . THR A 159 ? 0.2762 0.1780 0.1605 -0.0131 0.0079  -0.0058 161 THR A O   
997  C CB  . THR A 159 ? 0.3427 0.1824 0.1824 0.0142  0.0214  -0.0001 161 THR A CB  
998  O OG1 . THR A 159 ? 0.3245 0.2044 0.1979 0.0209  0.0196  0.0029  161 THR A OG1 
999  C CG2 . THR A 159 ? 0.3784 0.1890 0.1967 0.0184  0.0240  0.0032  161 THR A CG2 
1000 N N   . THR A 160 ? 0.3452 0.1915 0.1809 -0.0052 0.0149  -0.0094 162 THR A N   
1001 C CA  . THR A 160 ? 0.3522 0.2135 0.1956 -0.0047 0.0132  -0.0112 162 THR A CA  
1002 C C   . THR A 160 ? 0.3575 0.2312 0.2117 0.0149  0.0206  -0.0079 162 THR A C   
1003 O O   . THR A 160 ? 0.4083 0.2643 0.2485 0.0295  0.0285  -0.0063 162 THR A O   
1004 C CB  . THR A 160 ? 0.4082 0.2361 0.2169 -0.0137 0.0117  -0.0163 162 THR A CB  
1005 O OG1 . THR A 160 ? 0.4586 0.2518 0.2387 0.0020  0.0214  -0.0172 162 THR A OG1 
1006 C CG2 . THR A 160 ? 0.4242 0.2369 0.2183 -0.0360 0.0040  -0.0184 162 THR A CG2 
1007 N N   . ILE A 161 ? 0.3138 0.2180 0.1921 0.0153  0.0183  -0.0061 163 ILE A N   
1008 C CA  . ILE A 161 ? 0.3012 0.2207 0.1902 0.0293  0.0248  -0.0020 163 ILE A CA  
1009 C C   . ILE A 161 ? 0.2787 0.2058 0.1677 0.0250  0.0233  -0.0028 163 ILE A C   
1010 O O   . ILE A 161 ? 0.2753 0.2053 0.1659 0.0125  0.0150  -0.0053 163 ILE A O   
1011 C CB  . ILE A 161 ? 0.2864 0.2363 0.2057 0.0327  0.0226  0.0031  163 ILE A CB  
1012 C CG1 . ILE A 161 ? 0.2708 0.2400 0.2084 0.0211  0.0139  0.0023  163 ILE A CG1 
1013 C CG2 . ILE A 161 ? 0.3154 0.2565 0.2318 0.0358  0.0227  0.0042  163 ILE A CG2 
1014 C CD1 . ILE A 161 ? 0.2706 0.2607 0.2298 0.0218  0.0105  0.0056  163 ILE A CD1 
1015 N N   . ALA A 162 ? 0.2697 0.2003 0.1555 0.0361  0.0319  0.0001  164 ALA A N   
1016 C CA  . ALA A 162 ? 0.2602 0.1980 0.1448 0.0326  0.0317  0.0009  164 ALA A CA  
1017 C C   . ALA A 162 ? 0.2176 0.1868 0.1329 0.0278  0.0262  0.0060  164 ALA A C   
1018 O O   . ALA A 162 ? 0.1958 0.1848 0.1310 0.0328  0.0284  0.0111  164 ALA A O   
1019 C CB  . ALA A 162 ? 0.2872 0.2166 0.1545 0.0461  0.0448  0.0027  164 ALA A CB  
1020 N N   . ILE A 163 ? 0.2090 0.1810 0.1259 0.0178  0.0179  0.0050  165 ILE A N   
1021 C CA  . ILE A 163 ? 0.1851 0.1772 0.1223 0.0142  0.0133  0.0098  165 ILE A CA  
1022 C C   . ILE A 163 ? 0.1869 0.1902 0.1270 0.0190  0.0221  0.0163  165 ILE A C   
1023 O O   . ILE A 163 ? 0.1950 0.1886 0.1167 0.0230  0.0296  0.0165  165 ILE A O   
1024 C CB  . ILE A 163 ? 0.1895 0.1787 0.1234 0.0062  0.0035  0.0082  165 ILE A CB  
1025 C CG1 . ILE A 163 ? 0.1843 0.1861 0.1350 0.0037  -0.0019 0.0122  165 ILE A CG1 
1026 C CG2 . ILE A 163 ? 0.2073 0.1835 0.1187 0.0050  0.0051  0.0081  165 ILE A CG2 
1027 C CD1 . ILE A 163 ? 0.1863 0.1889 0.1414 0.0008  -0.0119 0.0098  165 ILE A CD1 
1028 N N   . LYS A 164 ? 0.1714 0.1955 0.1331 0.0176  0.0213  0.0221  166 LYS A N   
1029 C CA  . LYS A 164 ? 0.1888 0.2313 0.1585 0.0186  0.0288  0.0304  166 LYS A CA  
1030 C C   . LYS A 164 ? 0.1780 0.2173 0.1427 0.0088  0.0247  0.0336  166 LYS A C   
1031 O O   . LYS A 164 ? 0.1712 0.2205 0.1479 0.0002  0.0199  0.0389  166 LYS A O   
1032 C CB  . LYS A 164 ? 0.1990 0.2665 0.1930 0.0180  0.0277  0.0363  166 LYS A CB  
1033 C CG  . LYS A 164 ? 0.2416 0.3197 0.2406 0.0317  0.0360  0.0381  166 LYS A CG  
1034 C CD  . LYS A 164 ? 0.2722 0.3767 0.2953 0.0306  0.0319  0.0443  166 LYS A CD  
1035 C CE  . LYS A 164 ? 0.3040 0.4384 0.3454 0.0211  0.0320  0.0545  166 LYS A CE  
1036 N NZ  . LYS A 164 ? 0.3422 0.4898 0.3812 0.0282  0.0459  0.0605  166 LYS A NZ  
1037 N N   . SER A 165 ? 0.3189 0.2496 0.1257 -0.0912 -0.0629 0.0631  167 SER A N   
1038 C CA  . SER A 165 ? 0.2915 0.2417 0.1162 -0.0820 -0.0568 0.0558  167 SER A CA  
1039 C C   . SER A 165 ? 0.2824 0.2225 0.1152 -0.0834 -0.0584 0.0558  167 SER A C   
1040 O O   . SER A 165 ? 0.2909 0.2230 0.1146 -0.0961 -0.0605 0.0617  167 SER A O   
1041 C CB  . SER A 165 ? 0.2904 0.2741 0.1150 -0.0861 -0.0489 0.0555  167 SER A CB  
1042 O OG  . SER A 165 ? 0.2700 0.2712 0.1091 -0.0742 -0.0437 0.0480  167 SER A OG  
1043 N N   . ASP A 166 ? 0.2646 0.2042 0.1123 -0.0713 -0.0574 0.0492  168 ASP A N   
1044 C CA  . ASP A 166 ? 0.2622 0.1951 0.1183 -0.0711 -0.0581 0.0481  168 ASP A CA  
1045 C C   . ASP A 166 ? 0.2420 0.1849 0.1134 -0.0589 -0.0544 0.0408  168 ASP A C   
1046 O O   . ASP A 166 ? 0.2333 0.1800 0.1065 -0.0505 -0.0532 0.0367  168 ASP A O   
1047 C CB  . ASP A 166 ? 0.2766 0.1799 0.1270 -0.0707 -0.0659 0.0502  168 ASP A CB  
1048 C CG  . ASP A 166 ? 0.2820 0.1743 0.1349 -0.0730 -0.0676 0.0502  168 ASP A CG  
1049 O OD1 . ASP A 166 ? 0.2810 0.1883 0.1376 -0.0795 -0.0632 0.0505  168 ASP A OD1 
1050 O OD2 . ASP A 166 ? 0.2935 0.1641 0.1441 -0.0675 -0.0734 0.0494  168 ASP A OD2 
1051 N N   . VAL A 167 ? 0.2330 0.1773 0.1128 -0.0588 -0.0531 0.0394  169 VAL A N   
1052 C CA  . VAL A 167 ? 0.2204 0.1697 0.1123 -0.0485 -0.0505 0.0336  169 VAL A CA  
1053 C C   . VAL A 167 ? 0.2168 0.1498 0.1146 -0.0466 -0.0540 0.0324  169 VAL A C   
1054 O O   . VAL A 167 ? 0.2270 0.1486 0.1200 -0.0529 -0.0571 0.0355  169 VAL A O   
1055 C CB  . VAL A 167 ? 0.2166 0.1893 0.1133 -0.0484 -0.0450 0.0324  169 VAL A CB  
1056 C CG1 . VAL A 167 ? 0.2189 0.2122 0.1105 -0.0466 -0.0411 0.0319  169 VAL A CG1 
1057 C CG2 . VAL A 167 ? 0.2246 0.2008 0.1205 -0.0598 -0.0454 0.0365  169 VAL A CG2 
1058 N N   . PRO A 168 ? 0.2069 0.1370 0.1130 -0.0380 -0.0538 0.0277  170 PRO A N   
1059 C CA  . PRO A 168 ? 0.2027 0.1242 0.1156 -0.0359 -0.0555 0.0260  170 PRO A CA  
1060 C C   . PRO A 168 ? 0.1984 0.1278 0.1149 -0.0388 -0.0524 0.0261  170 PRO A C   
1061 O O   . PRO A 168 ? 0.1950 0.1397 0.1120 -0.0392 -0.0486 0.0261  170 PRO A O   
1062 C CB  . PRO A 168 ? 0.1926 0.1145 0.1120 -0.0288 -0.0550 0.0216  170 PRO A CB  
1063 C CG  . PRO A 168 ? 0.1920 0.1224 0.1075 -0.0264 -0.0518 0.0203  170 PRO A CG  
1064 C CD  . PRO A 168 ? 0.2038 0.1383 0.1110 -0.0310 -0.0521 0.0238  170 PRO A CD  
1065 N N   . THR A 169 ? 0.2016 0.1222 0.1207 -0.0391 -0.0542 0.0253  171 THR A N   
1066 C CA  . THR A 169 ? 0.2027 0.1296 0.1249 -0.0419 -0.0520 0.0250  171 THR A CA  
1067 C C   . THR A 169 ? 0.1940 0.1187 0.1245 -0.0354 -0.0513 0.0210  171 THR A C   
1068 O O   . THR A 169 ? 0.1924 0.1091 0.1250 -0.0310 -0.0535 0.0191  171 THR A O   
1069 C CB  . THR A 169 ? 0.2179 0.1349 0.1315 -0.0510 -0.0550 0.0281  171 THR A CB  
1070 O OG1 . THR A 169 ? 0.2291 0.1267 0.1401 -0.0469 -0.0593 0.0263  171 THR A OG1 
1071 C CG2 . THR A 169 ? 0.2323 0.1485 0.1346 -0.0603 -0.0565 0.0331  171 THR A CG2 
1072 N N   . LEU A 170 ? 0.1869 0.1214 0.1217 -0.0350 -0.0482 0.0199  172 LEU A N   
1073 C CA  . LEU A 170 ? 0.1832 0.1156 0.1237 -0.0309 -0.0474 0.0169  172 LEU A CA  
1074 C C   . LEU A 170 ? 0.1858 0.1209 0.1262 -0.0346 -0.0468 0.0169  172 LEU A C   
1075 O O   . LEU A 170 ? 0.1904 0.1370 0.1299 -0.0382 -0.0454 0.0187  172 LEU A O   
1076 C CB  . LEU A 170 ? 0.1797 0.1175 0.1228 -0.0256 -0.0450 0.0153  172 LEU A CB  
1077 C CG  . LEU A 170 ? 0.1758 0.1114 0.1227 -0.0233 -0.0441 0.0131  172 LEU A CG  
1078 C CD1 . LEU A 170 ? 0.1774 0.1096 0.1222 -0.0204 -0.0438 0.0120  172 LEU A CD1 
1079 C CD2 . LEU A 170 ? 0.1761 0.1178 0.1236 -0.0235 -0.0423 0.0132  172 LEU A CD2 
1080 N N   . THR A 171 ? 0.1927 0.1197 0.1340 -0.0333 -0.0481 0.0146  173 THR A N   
1081 C CA  . THR A 171 ? 0.1916 0.1189 0.1314 -0.0366 -0.0479 0.0138  173 THR A CA  
1082 C C   . THR A 171 ? 0.1866 0.1157 0.1317 -0.0314 -0.0461 0.0106  173 THR A C   
1083 O O   . THR A 171 ? 0.1932 0.1170 0.1399 -0.0273 -0.0469 0.0081  173 THR A O   
1084 C CB  . THR A 171 ? 0.2053 0.1167 0.1357 -0.0409 -0.0521 0.0138  173 THR A CB  
1085 O OG1 . THR A 171 ? 0.2195 0.1258 0.1428 -0.0464 -0.0544 0.0175  173 THR A OG1 
1086 C CG2 . THR A 171 ? 0.2054 0.1167 0.1314 -0.0470 -0.0525 0.0134  173 THR A CG2 
1087 N N   . LYS A 172 ? 0.1788 0.1171 0.1259 -0.0317 -0.0437 0.0107  174 LYS A N   
1088 C CA  . LYS A 172 ? 0.1689 0.1085 0.1184 -0.0289 -0.0420 0.0084  174 LYS A CA  
1089 C C   . LYS A 172 ? 0.1751 0.1119 0.1209 -0.0318 -0.0430 0.0067  174 LYS A C   
1090 O O   . LYS A 172 ? 0.1807 0.1206 0.1232 -0.0370 -0.0441 0.0082  174 LYS A O   
1091 C CB  . LYS A 172 ? 0.1620 0.1091 0.1121 -0.0268 -0.0399 0.0099  174 LYS A CB  
1092 C CG  . LYS A 172 ? 0.1596 0.1066 0.1096 -0.0256 -0.0384 0.0087  174 LYS A CG  
1093 C CD  . LYS A 172 ? 0.1594 0.1083 0.1059 -0.0231 -0.0376 0.0106  174 LYS A CD  
1094 C CE  . LYS A 172 ? 0.1590 0.1052 0.1031 -0.0242 -0.0363 0.0101  174 LYS A CE  
1095 N NZ  . LYS A 172 ? 0.1656 0.1089 0.1023 -0.0213 -0.0368 0.0126  174 LYS A NZ  
1096 N N   . GLN A 173 ? 0.1765 0.1089 0.1223 -0.0287 -0.0428 0.0031  175 GLN A N   
1097 C CA  . GLN A 173 ? 0.1834 0.1103 0.1232 -0.0301 -0.0441 0.0002  175 GLN A CA  
1098 C C   . GLN A 173 ? 0.1772 0.1103 0.1195 -0.0263 -0.0412 -0.0028 175 GLN A C   
1099 O O   . GLN A 173 ? 0.1693 0.1094 0.1173 -0.0235 -0.0388 -0.0028 175 GLN A O   
1100 C CB  . GLN A 173 ? 0.2001 0.1106 0.1321 -0.0286 -0.0481 -0.0021 175 GLN A CB  
1101 C CG  . GLN A 173 ? 0.2114 0.1133 0.1373 -0.0351 -0.0514 0.0015  175 GLN A CG  
1102 C CD  . GLN A 173 ? 0.2296 0.1099 0.1442 -0.0329 -0.0564 -0.0001 175 GLN A CD  
1103 O OE1 . GLN A 173 ? 0.2253 0.1025 0.1420 -0.0242 -0.0572 -0.0023 175 GLN A OE1 
1104 N NE2 . GLN A 173 ? 0.2551 0.1197 0.1558 -0.0410 -0.0606 0.0007  175 GLN A NE2 
1105 N N   . VAL A 174 ? 0.1810 0.1117 0.1175 -0.0277 -0.0416 -0.0053 176 VAL A N   
1106 C CA  . VAL A 174 ? 0.1838 0.1206 0.1202 -0.0247 -0.0389 -0.0087 176 VAL A CA  
1107 C C   . VAL A 174 ? 0.1986 0.1244 0.1265 -0.0207 -0.0411 -0.0147 176 VAL A C   
1108 O O   . VAL A 174 ? 0.2103 0.1215 0.1289 -0.0241 -0.0452 -0.0152 176 VAL A O   
1109 C CB  . VAL A 174 ? 0.1824 0.1269 0.1177 -0.0289 -0.0374 -0.0062 176 VAL A CB  
1110 C CG1 . VAL A 174 ? 0.1895 0.1296 0.1178 -0.0343 -0.0406 -0.0061 176 VAL A CG1 
1111 C CG2 . VAL A 174 ? 0.1879 0.1397 0.1222 -0.0271 -0.0342 -0.0087 176 VAL A CG2 
1112 N N   . LYS A 175 ? 0.2029 0.1355 0.1322 -0.0137 -0.0387 -0.0194 177 LYS A N   
1113 C CA  . LYS A 175 ? 0.2246 0.1473 0.1441 -0.0065 -0.0407 -0.0265 177 LYS A CA  
1114 C C   . LYS A 175 ? 0.2352 0.1510 0.1443 -0.0114 -0.0417 -0.0282 177 LYS A C   
1115 O O   . LYS A 175 ? 0.2239 0.1529 0.1362 -0.0153 -0.0382 -0.0266 177 LYS A O   
1116 C CB  . LYS A 175 ? 0.2293 0.1690 0.1541 0.0025  -0.0369 -0.0315 177 LYS A CB  
1117 C CG  . LYS A 175 ? 0.2562 0.1862 0.1707 0.0151  -0.0395 -0.0401 177 LYS A CG  
1118 C CD  . LYS A 175 ? 0.2632 0.2176 0.1831 0.0242  -0.0347 -0.0458 177 LYS A CD  
1119 C CE  . LYS A 175 ? 0.2720 0.2362 0.1880 0.0207  -0.0306 -0.0479 177 LYS A CE  
1120 N NZ  . LYS A 175 ? 0.2982 0.2416 0.1966 0.0265  -0.0341 -0.0548 177 LYS A NZ  
1121 N N   . ALA A 176 ? 0.2548 0.1480 0.1494 -0.0118 -0.0470 -0.0312 178 ALA A N   
1122 C CA  . ALA A 176 ? 0.2799 0.1640 0.1617 -0.0172 -0.0491 -0.0338 178 ALA A CA  
1123 C C   . ALA A 176 ? 0.2820 0.1775 0.1628 -0.0100 -0.0450 -0.0397 178 ALA A C   
1124 O O   . ALA A 176 ? 0.2777 0.1792 0.1607 0.0014  -0.0429 -0.0447 178 ALA A O   
1125 C CB  . ALA A 176 ? 0.3128 0.1661 0.1752 -0.0183 -0.0563 -0.0371 178 ALA A CB  
1126 N N   . SER A 177 ? 0.2931 0.1948 0.1708 -0.0169 -0.0440 -0.0389 179 SER A N   
1127 C CA  . SER A 177 ? 0.3052 0.2179 0.1796 -0.0123 -0.0401 -0.0439 179 SER A CA  
1128 C C   . SER A 177 ? 0.3396 0.2368 0.1990 -0.0011 -0.0423 -0.0540 179 SER A C   
1129 O O   . SER A 177 ? 0.3463 0.2580 0.2075 0.0087  -0.0379 -0.0594 179 SER A O   
1130 C CB  . SER A 177 ? 0.3060 0.2228 0.1760 -0.0220 -0.0406 -0.0413 179 SER A CB  
1131 O OG  . SER A 177 ? 0.3263 0.2535 0.1918 -0.0181 -0.0368 -0.0458 179 SER A OG  
1132 N N   . ASN A 178 ? 0.3790 0.2466 0.2217 -0.0027 -0.0494 -0.0567 180 ASN A N   
1133 C CA  . ASN A 178 ? 0.4273 0.2721 0.2486 0.0071  -0.0533 -0.0668 180 ASN A CA  
1134 C C   . ASN A 178 ? 0.4506 0.2737 0.2640 0.0190  -0.0579 -0.0705 180 ASN A C   
1135 O O   . ASN A 178 ? 0.4847 0.2789 0.2753 0.0270  -0.0636 -0.0784 180 ASN A O   
1136 C CB  . ASN A 178 ? 0.4574 0.2800 0.2595 -0.0049 -0.0591 -0.0677 180 ASN A CB  
1137 C CG  . ASN A 178 ? 0.4571 0.3030 0.2667 -0.0145 -0.0550 -0.0643 180 ASN A CG  
1138 O OD1 . ASN A 178 ? 0.4661 0.3160 0.2791 -0.0289 -0.0570 -0.0574 180 ASN A OD1 
1139 N ND2 . ASN A 178 ? 0.4515 0.3158 0.2640 -0.0059 -0.0492 -0.0689 180 ASN A ND2 
1140 N N   . SER A 179 ? 0.4352 0.2707 0.2652 0.0212  -0.0561 -0.0653 181 SER A N   
1141 C CA  . SER A 179 ? 0.4672 0.2840 0.2902 0.0331  -0.0609 -0.0681 181 SER A CA  
1142 C C   . SER A 179 ? 0.4335 0.2766 0.2798 0.0363  -0.0566 -0.0630 181 SER A C   
1143 O O   . SER A 179 ? 0.3955 0.2668 0.2606 0.0283  -0.0503 -0.0574 181 SER A O   
1144 C CB  . SER A 179 ? 0.5017 0.2799 0.3054 0.0234  -0.0698 -0.0650 181 SER A CB  
1145 O OG  . SER A 179 ? 0.5020 0.2899 0.3179 0.0052  -0.0687 -0.0547 181 SER A OG  
1146 N N   . GLU A 180 ? 0.4640 0.2949 0.3063 0.0477  -0.0608 -0.0648 182 GLU A N   
1147 C CA  . GLU A 180 ? 0.4496 0.3055 0.3120 0.0525  -0.0576 -0.0614 182 GLU A CA  
1148 C C   . GLU A 180 ? 0.4259 0.2742 0.2942 0.0397  -0.0599 -0.0518 182 GLU A C   
1149 O O   . GLU A 180 ? 0.3806 0.2487 0.2655 0.0400  -0.0572 -0.0478 182 GLU A O   
1150 C CB  . GLU A 180 ? 0.4962 0.3483 0.3522 0.0742  -0.0611 -0.0691 182 GLU A CB  
1151 C CG  . GLU A 180 ? 0.5347 0.4055 0.3891 0.0895  -0.0574 -0.0792 182 GLU A CG  
1152 C CD  . GLU A 180 ? 0.5434 0.4624 0.4214 0.0860  -0.0476 -0.0779 182 GLU A CD  
1153 O OE1 . GLU A 180 ? 0.5336 0.4706 0.4296 0.0741  -0.0444 -0.0696 182 GLU A OE1 
1154 O OE2 . GLU A 180 ? 0.6020 0.5392 0.4784 0.0944  -0.0433 -0.0852 182 GLU A OE2 
1155 N N   . ASN A 181 ? 0.4284 0.2498 0.2827 0.0275  -0.0647 -0.0481 183 ASN A N   
1156 C CA  . ASN A 181 ? 0.4336 0.2491 0.2916 0.0165  -0.0669 -0.0397 183 ASN A CA  
1157 C C   . ASN A 181 ? 0.3731 0.2139 0.2489 0.0029  -0.0609 -0.0327 183 ASN A C   
1158 O O   . ASN A 181 ? 0.3582 0.2118 0.2376 -0.0014 -0.0571 -0.0334 183 ASN A O   
1159 C CB  . ASN A 181 ? 0.5235 0.3008 0.3575 0.0083  -0.0751 -0.0380 183 ASN A CB  
1160 C CG  . ASN A 181 ? 0.5685 0.3357 0.3904 -0.0036 -0.0763 -0.0389 183 ASN A CG  
1161 O OD1 . ASN A 181 ? 0.6383 0.4004 0.4511 0.0039  -0.0763 -0.0463 183 ASN A OD1 
1162 N ND2 . ASN A 181 ? 0.5744 0.3407 0.3955 -0.0220 -0.0774 -0.0317 183 ASN A ND2 
1163 N N   . TYR A 182 ? 0.3256 0.1720 0.2105 -0.0025 -0.0607 -0.0262 184 TYR A N   
1164 C CA  . TYR A 182 ? 0.2855 0.1537 0.1857 -0.0119 -0.0559 -0.0199 184 TYR A CA  
1165 C C   . TYR A 182 ? 0.2852 0.1446 0.1782 -0.0259 -0.0586 -0.0147 184 TYR A C   
1166 O O   . TYR A 182 ? 0.3133 0.1532 0.1948 -0.0299 -0.0637 -0.0128 184 TYR A O   
1167 C CB  . TYR A 182 ? 0.2653 0.1460 0.1782 -0.0075 -0.0541 -0.0174 184 TYR A CB  
1168 C CG  . TYR A 182 ? 0.2471 0.1491 0.1717 0.0006  -0.0495 -0.0208 184 TYR A CG  
1169 C CD1 . TYR A 182 ? 0.2232 0.1450 0.1585 -0.0045 -0.0441 -0.0182 184 TYR A CD1 
1170 C CD2 . TYR A 182 ? 0.2562 0.1588 0.1790 0.0134  -0.0508 -0.0269 184 TYR A CD2 
1171 C CE1 . TYR A 182 ? 0.2153 0.1565 0.1588 -0.0004 -0.0401 -0.0206 184 TYR A CE1 
1172 C CE2 . TYR A 182 ? 0.2443 0.1718 0.1779 0.0192  -0.0463 -0.0300 184 TYR A CE2 
1173 C CZ  . TYR A 182 ? 0.2258 0.1724 0.1695 0.0106  -0.0408 -0.0265 184 TYR A CZ  
1174 O OH  . TYR A 182 ? 0.2255 0.1969 0.1782 0.0128  -0.0364 -0.0285 184 TYR A OH  
1175 N N   . ILE A 183 ? 0.2589 0.1344 0.1583 -0.0333 -0.0554 -0.0122 185 ILE A N   
1176 C CA  . ILE A 183 ? 0.2539 0.1298 0.1485 -0.0465 -0.0575 -0.0078 185 ILE A CA  
1177 C C   . ILE A 183 ? 0.2198 0.1216 0.1292 -0.0485 -0.0530 -0.0034 185 ILE A C   
1178 O O   . ILE A 183 ? 0.2069 0.1199 0.1266 -0.0412 -0.0490 -0.0036 185 ILE A O   
1179 C CB  . ILE A 183 ? 0.2722 0.1368 0.1528 -0.0524 -0.0606 -0.0112 185 ILE A CB  
1180 C CG1 . ILE A 183 ? 0.2614 0.1374 0.1466 -0.0459 -0.0568 -0.0154 185 ILE A CG1 
1181 C CG2 . ILE A 183 ? 0.3048 0.1364 0.1650 -0.0516 -0.0670 -0.0149 185 ILE A CG2 
1182 C CD1 . ILE A 183 ? 0.2795 0.1457 0.1502 -0.0522 -0.0600 -0.0190 185 ILE A CD1 
1183 N N   . SER A 184 ? 0.2122 0.1238 0.1209 -0.0586 -0.0540 0.0005  186 SER A N   
1184 C CA  A SER A 184 ? 0.1905 0.1258 0.1111 -0.0576 -0.0505 0.0042  186 SER A CA  
1185 C CA  B SER A 184 ? 0.1910 0.1265 0.1114 -0.0579 -0.0506 0.0043  186 SER A CA  
1186 C C   . SER A 184 ? 0.1841 0.1310 0.1076 -0.0549 -0.0485 0.0030  186 SER A C   
1187 O O   . SER A 184 ? 0.1741 0.1336 0.1053 -0.0492 -0.0457 0.0049  186 SER A O   
1188 C CB  A SER A 184 ? 0.1916 0.1387 0.1115 -0.0674 -0.0521 0.0086  186 SER A CB  
1189 C CB  B SER A 184 ? 0.1931 0.1405 0.1123 -0.0683 -0.0523 0.0085  186 SER A CB  
1190 O OG  A SER A 184 ? 0.1916 0.1307 0.1099 -0.0687 -0.0529 0.0107  186 SER A OG  
1191 O OG  B SER A 184 ? 0.2041 0.1506 0.1142 -0.0789 -0.0557 0.0080  186 SER A OG  
1192 N N   . ALA A 185 ? 0.1915 0.1316 0.1064 -0.0589 -0.0506 0.0000  187 ALA A N   
1193 C CA  . ALA A 185 ? 0.1882 0.1399 0.1041 -0.0577 -0.0494 -0.0007 187 ALA A CA  
1194 C C   . ALA A 185 ? 0.2012 0.1392 0.1070 -0.0576 -0.0505 -0.0062 187 ALA A C   
1195 O O   . ALA A 185 ? 0.2187 0.1390 0.1129 -0.0625 -0.0543 -0.0091 187 ALA A O   
1196 C CB  . ALA A 185 ? 0.1877 0.1578 0.1044 -0.0653 -0.0515 0.0027  187 ALA A CB  
1197 N N   . THR A 186 ? 0.1954 0.1405 0.1029 -0.0524 -0.0477 -0.0076 188 THR A N   
1198 C CA  . THR A 186 ? 0.2075 0.1437 0.1051 -0.0516 -0.0481 -0.0132 188 THR A CA  
1199 C C   . THR A 186 ? 0.2037 0.1543 0.1030 -0.0500 -0.0457 -0.0120 188 THR A C   
1200 O O   . THR A 186 ? 0.1889 0.1530 0.0954 -0.0492 -0.0448 -0.0067 188 THR A O   
1201 C CB  . THR A 186 ? 0.2134 0.1367 0.1089 -0.0433 -0.0465 -0.0184 188 THR A CB  
1202 O OG1 . THR A 186 ? 0.2308 0.1438 0.1138 -0.0414 -0.0476 -0.0251 188 THR A OG1 
1203 C CG2 . THR A 186 ? 0.2005 0.1355 0.1070 -0.0360 -0.0413 -0.0170 188 THR A CG2 
1204 N N   . ASP A 187 ? 0.2158 0.1618 0.1066 -0.0485 -0.0450 -0.0170 189 ASP A N   
1205 C CA  . ASP A 187 ? 0.2160 0.1738 0.1062 -0.0471 -0.0426 -0.0157 189 ASP A CA  
1206 C C   . ASP A 187 ? 0.2155 0.1734 0.1058 -0.0404 -0.0376 -0.0192 189 ASP A C   
1207 O O   . ASP A 187 ? 0.2299 0.1788 0.1171 -0.0361 -0.0371 -0.0251 189 ASP A O   
1208 C CB  . ASP A 187 ? 0.2318 0.1903 0.1113 -0.0532 -0.0462 -0.0178 189 ASP A CB  
1209 C CG  . ASP A 187 ? 0.2591 0.2007 0.1247 -0.0545 -0.0485 -0.0257 189 ASP A CG  
1210 O OD1 . ASP A 187 ? 0.2787 0.2060 0.1422 -0.0501 -0.0483 -0.0297 189 ASP A OD1 
1211 O OD2 . ASP A 187 ? 0.2740 0.2157 0.1292 -0.0594 -0.0511 -0.0280 189 ASP A OD2 
1212 N N   . TYR A 188 ? 0.2063 0.1748 0.0985 -0.0396 -0.0343 -0.0155 190 TYR A N   
1213 C CA  . TYR A 188 ? 0.2020 0.1763 0.0945 -0.0362 -0.0291 -0.0176 190 TYR A CA  
1214 C C   . TYR A 188 ? 0.2046 0.1868 0.0897 -0.0391 -0.0273 -0.0151 190 TYR A C   
1215 O O   . TYR A 188 ? 0.2001 0.1827 0.0817 -0.0420 -0.0304 -0.0106 190 TYR A O   
1216 C CB  . TYR A 188 ? 0.1914 0.1685 0.0939 -0.0346 -0.0266 -0.0142 190 TYR A CB  
1217 C CG  . TYR A 188 ? 0.1904 0.1635 0.0984 -0.0295 -0.0265 -0.0190 190 TYR A CG  
1218 C CD1 . TYR A 188 ? 0.2010 0.1787 0.1069 -0.0238 -0.0238 -0.0260 190 TYR A CD1 
1219 C CD2 . TYR A 188 ? 0.1857 0.1514 0.0997 -0.0292 -0.0292 -0.0167 190 TYR A CD2 
1220 C CE1 . TYR A 188 ? 0.2043 0.1782 0.1136 -0.0166 -0.0246 -0.0306 190 TYR A CE1 
1221 C CE2 . TYR A 188 ? 0.1883 0.1484 0.1051 -0.0240 -0.0299 -0.0207 190 TYR A CE2 
1222 C CZ  . TYR A 188 ? 0.1991 0.1629 0.1135 -0.0171 -0.0280 -0.0276 190 TYR A CZ  
1223 O OH  . TYR A 188 ? 0.2067 0.1649 0.1222 -0.0093 -0.0295 -0.0319 190 TYR A OH  
1224 N N   . ALA A 189 ? 0.2091 0.1992 0.0912 -0.0379 -0.0225 -0.0182 191 ALA A N   
1225 C CA  . ALA A 189 ? 0.2182 0.2160 0.0914 -0.0417 -0.0203 -0.0157 191 ALA A CA  
1226 C C   . ALA A 189 ? 0.2177 0.2223 0.0932 -0.0455 -0.0163 -0.0099 191 ALA A C   
1227 O O   . ALA A 189 ? 0.2109 0.2167 0.0955 -0.0445 -0.0150 -0.0095 191 ALA A O   
1228 C CB  . ALA A 189 ? 0.2304 0.2334 0.0953 -0.0392 -0.0179 -0.0240 191 ALA A CB  
1229 N N   . ILE A 190 ? 0.2306 0.2383 0.0956 -0.0509 -0.0151 -0.0051 192 ILE A N   
1230 C CA  . ILE A 190 ? 0.2379 0.2480 0.0994 -0.0579 -0.0124 0.0015  192 ILE A CA  
1231 C C   . ILE A 190 ? 0.2357 0.2641 0.1026 -0.0598 -0.0060 -0.0027 192 ILE A C   
1232 O O   . ILE A 190 ? 0.2344 0.2661 0.1030 -0.0662 -0.0041 0.0018  192 ILE A O   
1233 C CB  . ILE A 190 ? 0.2570 0.2632 0.1019 -0.0637 -0.0136 0.0078  192 ILE A CB  
1234 C CG1 . ILE A 190 ? 0.2709 0.2688 0.1065 -0.0722 -0.0135 0.0170  192 ILE A CG1 
1235 C CG2 . ILE A 190 ? 0.2670 0.2873 0.1043 -0.0654 -0.0095 0.0029  192 ILE A CG2 
1236 C CD1 . ILE A 190 ? 0.2712 0.2498 0.1072 -0.0689 -0.0192 0.0226  192 ILE A CD1 
1237 N N   . TRP A 191 ? 0.2367 0.2777 0.1050 -0.0541 -0.0030 -0.0117 193 TRP A N   
1238 C CA  . TRP A 191 ? 0.2400 0.3041 0.1137 -0.0530 0.0031  -0.0170 193 TRP A CA  
1239 C C   . TRP A 191 ? 0.2333 0.2989 0.1213 -0.0450 0.0024  -0.0217 193 TRP A C   
1240 O O   . TRP A 191 ? 0.2375 0.3246 0.1320 -0.0425 0.0068  -0.0260 193 TRP A O   
1241 C CB  . TRP A 191 ? 0.2526 0.3301 0.1186 -0.0480 0.0066  -0.0253 193 TRP A CB  
1242 C CG  . TRP A 191 ? 0.2590 0.3206 0.1220 -0.0380 0.0022  -0.0327 193 TRP A CG  
1243 C CD1 . TRP A 191 ? 0.2603 0.3164 0.1286 -0.0269 0.0004  -0.0410 193 TRP A CD1 
1244 C CD2 . TRP A 191 ? 0.2725 0.3190 0.1242 -0.0398 -0.0021 -0.0318 193 TRP A CD2 
1245 N NE1 . TRP A 191 ? 0.2705 0.3072 0.1300 -0.0233 -0.0047 -0.0452 193 TRP A NE1 
1246 C CE2 . TRP A 191 ? 0.2774 0.3102 0.1278 -0.0315 -0.0062 -0.0399 193 TRP A CE2 
1247 C CE3 . TRP A 191 ? 0.2843 0.3273 0.1253 -0.0478 -0.0037 -0.0250 193 TRP A CE3 
1248 C CZ2 . TRP A 191 ? 0.2914 0.3098 0.1315 -0.0328 -0.0115 -0.0412 193 TRP A CZ2 
1249 C CZ3 . TRP A 191 ? 0.2922 0.3233 0.1246 -0.0470 -0.0088 -0.0265 193 TRP A CZ3 
1250 C CH2 . TRP A 191 ? 0.2941 0.3142 0.1265 -0.0405 -0.0126 -0.0346 193 TRP A CH2 
1251 N N   . ASP A 192 ? 0.2268 0.2721 0.1193 -0.0409 -0.0030 -0.0207 194 ASP A N   
1252 C CA  . ASP A 192 ? 0.2186 0.2616 0.1220 -0.0330 -0.0046 -0.0250 194 ASP A CA  
1253 C C   . ASP A 192 ? 0.2075 0.2512 0.1195 -0.0385 -0.0049 -0.0185 194 ASP A C   
1254 O O   . ASP A 192 ? 0.2079 0.2434 0.1155 -0.0471 -0.0060 -0.0105 194 ASP A O   
1255 C CB  . ASP A 192 ? 0.2160 0.2369 0.1179 -0.0277 -0.0106 -0.0271 194 ASP A CB  
1256 C CG  . ASP A 192 ? 0.2318 0.2473 0.1236 -0.0219 -0.0117 -0.0350 194 ASP A CG  
1257 O OD1 . ASP A 192 ? 0.2434 0.2699 0.1333 -0.0143 -0.0087 -0.0427 194 ASP A OD1 
1258 O OD2 . ASP A 192 ? 0.2382 0.2395 0.1233 -0.0248 -0.0160 -0.0336 194 ASP A OD2 
1259 N N   . THR A 193 ? 0.2016 0.2543 0.1237 -0.0326 -0.0043 -0.0226 195 THR A N   
1260 C CA  . THR A 193 ? 0.1932 0.2425 0.1237 -0.0353 -0.0062 -0.0183 195 THR A CA  
1261 C C   . THR A 193 ? 0.1869 0.2145 0.1196 -0.0289 -0.0116 -0.0189 195 THR A C   
1262 O O   . THR A 193 ? 0.1953 0.2175 0.1271 -0.0199 -0.0134 -0.0253 195 THR A O   
1263 C CB  . THR A 193 ? 0.1917 0.2660 0.1318 -0.0327 -0.0030 -0.0221 195 THR A CB  
1264 O OG1 . THR A 193 ? 0.2005 0.2971 0.1372 -0.0416 0.0022  -0.0206 195 THR A OG1 
1265 C CG2 . THR A 193 ? 0.1858 0.2583 0.1337 -0.0371 -0.0051 -0.0177 195 THR A CG2 
1266 N N   . VAL A 194 ? 0.1788 0.1927 0.1118 -0.0340 -0.0144 -0.0122 196 VAL A N   
1267 C CA  . VAL A 194 ? 0.1752 0.1721 0.1098 -0.0302 -0.0191 -0.0116 196 VAL A CA  
1268 C C   . VAL A 194 ? 0.1686 0.1658 0.1118 -0.0280 -0.0203 -0.0115 196 VAL A C   
1269 O O   . VAL A 194 ? 0.1629 0.1587 0.1077 -0.0331 -0.0205 -0.0065 196 VAL A O   
1270 C CB  . VAL A 194 ? 0.1746 0.1598 0.1038 -0.0348 -0.0214 -0.0052 196 VAL A CB  
1271 C CG1 . VAL A 194 ? 0.1718 0.1458 0.1029 -0.0319 -0.0256 -0.0048 196 VAL A CG1 
1272 C CG2 . VAL A 194 ? 0.1829 0.1696 0.1030 -0.0373 -0.0206 -0.0046 196 VAL A CG2 
1273 N N   . PRO A 195 ? 0.1713 0.1680 0.1180 -0.0198 -0.0218 -0.0170 197 PRO A N   
1274 C CA  . PRO A 195 ? 0.1653 0.1617 0.1191 -0.0171 -0.0238 -0.0166 197 PRO A CA  
1275 C C   . PRO A 195 ? 0.1616 0.1401 0.1144 -0.0183 -0.0278 -0.0129 197 PRO A C   
1276 O O   . PRO A 195 ? 0.1621 0.1280 0.1094 -0.0170 -0.0304 -0.0139 197 PRO A O   
1277 C CB  . PRO A 195 ? 0.1735 0.1737 0.1278 -0.0058 -0.0248 -0.0241 197 PRO A CB  
1278 C CG  . PRO A 195 ? 0.1831 0.1879 0.1306 -0.0033 -0.0223 -0.0289 197 PRO A CG  
1279 C CD  . PRO A 195 ? 0.1804 0.1745 0.1218 -0.0121 -0.0225 -0.0240 197 PRO A CD  
1280 N N   . PHE A 196 ? 0.1547 0.1334 0.1119 -0.0215 -0.0283 -0.0089 198 PHE A N   
1281 C CA  . PHE A 196 ? 0.1575 0.1234 0.1141 -0.0221 -0.0314 -0.0057 198 PHE A CA  
1282 C C   . PHE A 196 ? 0.1582 0.1244 0.1197 -0.0183 -0.0336 -0.0068 198 PHE A C   
1283 O O   . PHE A 196 ? 0.1504 0.1293 0.1170 -0.0170 -0.0324 -0.0087 198 PHE A O   
1284 C CB  . PHE A 196 ? 0.1607 0.1237 0.1151 -0.0275 -0.0310 -0.0003 198 PHE A CB  
1285 C CG  . PHE A 196 ? 0.1675 0.1277 0.1156 -0.0295 -0.0304 0.0017  198 PHE A CG  
1286 C CD1 . PHE A 196 ? 0.1705 0.1258 0.1164 -0.0284 -0.0325 0.0027  198 PHE A CD1 
1287 C CD2 . PHE A 196 ? 0.1772 0.1418 0.1210 -0.0331 -0.0281 0.0028  198 PHE A CD2 
1288 C CE1 . PHE A 196 ? 0.1774 0.1335 0.1182 -0.0293 -0.0327 0.0046  198 PHE A CE1 
1289 C CE2 . PHE A 196 ? 0.1812 0.1427 0.1180 -0.0340 -0.0284 0.0050  198 PHE A CE2 
1290 C CZ  . PHE A 196 ? 0.1807 0.1387 0.1167 -0.0313 -0.0308 0.0057  198 PHE A CZ  
1291 N N   . GLN A 197 ? 0.1668 0.1211 0.1263 -0.0174 -0.0367 -0.0054 199 GLN A N   
1292 C CA  . GLN A 197 ? 0.1735 0.1249 0.1352 -0.0136 -0.0396 -0.0059 199 GLN A CA  
1293 C C   . GLN A 197 ? 0.1744 0.1163 0.1336 -0.0170 -0.0415 -0.0017 199 GLN A C   
1294 O O   . GLN A 197 ? 0.1778 0.1119 0.1318 -0.0194 -0.0426 -0.0004 199 GLN A O   
1295 C CB  . GLN A 197 ? 0.1906 0.1346 0.1477 -0.0060 -0.0426 -0.0105 199 GLN A CB  
1296 C CG  . GLN A 197 ? 0.2003 0.1401 0.1578 -0.0002 -0.0466 -0.0110 199 GLN A CG  
1297 C CD  . GLN A 197 ? 0.2217 0.1488 0.1703 0.0091  -0.0506 -0.0157 199 GLN A CD  
1298 O OE1 . GLN A 197 ? 0.2260 0.1634 0.1772 0.0190  -0.0508 -0.0208 199 GLN A OE1 
1299 N NE2 . GLN A 197 ? 0.2406 0.1455 0.1771 0.0062  -0.0541 -0.0144 199 GLN A NE2 
1300 N N   . ILE A 198 ? 0.1683 0.1128 0.1306 -0.0180 -0.0419 0.0002  200 ILE A N   
1301 C CA  . ILE A 198 ? 0.1718 0.1096 0.1314 -0.0200 -0.0434 0.0035  200 ILE A CA  
1302 C C   . ILE A 198 ? 0.1727 0.1062 0.1321 -0.0167 -0.0470 0.0029  200 ILE A C   
1303 O O   . ILE A 198 ? 0.1720 0.1124 0.1359 -0.0144 -0.0477 0.0015  200 ILE A O   
1304 C CB  . ILE A 198 ? 0.1734 0.1134 0.1329 -0.0228 -0.0419 0.0057  200 ILE A CB  
1305 C CG1 . ILE A 198 ? 0.1808 0.1221 0.1377 -0.0245 -0.0394 0.0066  200 ILE A CG1 
1306 C CG2 . ILE A 198 ? 0.1779 0.1131 0.1339 -0.0228 -0.0432 0.0081  200 ILE A CG2 
1307 C CD1 . ILE A 198 ? 0.1843 0.1224 0.1368 -0.0266 -0.0389 0.0083  200 ILE A CD1 
1308 N N   . THR A 199 ? 0.1802 0.1030 0.1332 -0.0175 -0.0496 0.0044  201 THR A N   
1309 C CA  . THR A 199 ? 0.1901 0.1047 0.1393 -0.0145 -0.0539 0.0049  201 THR A CA  
1310 C C   . THR A 199 ? 0.1904 0.1037 0.1371 -0.0189 -0.0542 0.0088  201 THR A C   
1311 O O   . THR A 199 ? 0.1901 0.1019 0.1325 -0.0242 -0.0533 0.0115  201 THR A O   
1312 C CB  . THR A 199 ? 0.2106 0.1091 0.1497 -0.0130 -0.0577 0.0039  201 THR A CB  
1313 O OG1 . THR A 199 ? 0.2088 0.1103 0.1499 -0.0068 -0.0570 -0.0009 201 THR A OG1 
1314 C CG2 . THR A 199 ? 0.2301 0.1150 0.1610 -0.0097 -0.0633 0.0051  201 THR A CG2 
1315 N N   . VAL A 200 ? 0.1892 0.1046 0.1378 -0.0165 -0.0560 0.0090  202 VAL A N   
1316 C CA  . VAL A 200 ? 0.1893 0.1030 0.1339 -0.0195 -0.0567 0.0121  202 VAL A CA  
1317 C C   . VAL A 200 ? 0.1976 0.1011 0.1354 -0.0174 -0.0619 0.0135  202 VAL A C   
1318 O O   . VAL A 200 ? 0.1927 0.0969 0.1329 -0.0113 -0.0651 0.0114  202 VAL A O   
1319 C CB  . VAL A 200 ? 0.1874 0.1093 0.1364 -0.0197 -0.0550 0.0113  202 VAL A CB  
1320 C CG1 . VAL A 200 ? 0.1927 0.1125 0.1361 -0.0212 -0.0558 0.0134  202 VAL A CG1 
1321 C CG2 . VAL A 200 ? 0.1842 0.1106 0.1353 -0.0213 -0.0509 0.0106  202 VAL A CG2 
1322 N N   . THR A 201 ? 0.2040 0.1000 0.1327 -0.0227 -0.0630 0.0174  203 THR A N   
1323 C CA  . THR A 201 ? 0.2202 0.1043 0.1391 -0.0223 -0.0682 0.0200  203 THR A CA  
1324 C C   . THR A 201 ? 0.2106 0.1023 0.1298 -0.0241 -0.0672 0.0216  203 THR A C   
1325 O O   . THR A 201 ? 0.2033 0.1053 0.1255 -0.0272 -0.0626 0.0217  203 THR A O   
1326 C CB  . THR A 201 ? 0.2393 0.1077 0.1441 -0.0293 -0.0707 0.0239  203 THR A CB  
1327 O OG1 . THR A 201 ? 0.2370 0.1162 0.1414 -0.0385 -0.0663 0.0267  203 THR A OG1 
1328 C CG2 . THR A 201 ? 0.2459 0.1030 0.1471 -0.0278 -0.0724 0.0216  203 THR A CG2 
1329 N N   . LEU A 202 ? 0.2136 0.0996 0.1281 -0.0210 -0.0720 0.0227  204 LEU A N   
1330 C CA  . LEU A 202 ? 0.2110 0.1026 0.1237 -0.0227 -0.0718 0.0239  204 LEU A CA  
1331 C C   . LEU A 202 ? 0.2226 0.1056 0.1214 -0.0289 -0.0735 0.0291  204 LEU A C   
1332 O O   . LEU A 202 ? 0.2348 0.1032 0.1237 -0.0314 -0.0770 0.0321  204 LEU A O   
1333 C CB  . LEU A 202 ? 0.2121 0.1066 0.1288 -0.0164 -0.0763 0.0217  204 LEU A CB  
1334 C CG  . LEU A 202 ? 0.2000 0.1078 0.1297 -0.0138 -0.0740 0.0171  204 LEU A CG  
1335 C CD1 . LEU A 202 ? 0.2020 0.1181 0.1361 -0.0094 -0.0787 0.0152  204 LEU A CD1 
1336 C CD2 . LEU A 202 ? 0.1914 0.1050 0.1230 -0.0185 -0.0688 0.0160  204 LEU A CD2 
1337 N N   . PRO A 203 ? 0.2175 0.1082 0.1129 -0.0322 -0.0712 0.0303  205 PRO A N   
1338 C CA  . PRO A 203 ? 0.2303 0.1171 0.1123 -0.0396 -0.0719 0.0356  205 PRO A CA  
1339 C C   . PRO A 203 ? 0.2477 0.1183 0.1186 -0.0381 -0.0794 0.0387  205 PRO A C   
1340 O O   . PRO A 203 ? 0.2427 0.1122 0.1182 -0.0302 -0.0833 0.0361  205 PRO A O   
1341 C CB  . PRO A 203 ? 0.2241 0.1264 0.1065 -0.0402 -0.0671 0.0342  205 PRO A CB  
1342 C CG  . PRO A 203 ? 0.2142 0.1185 0.1051 -0.0326 -0.0678 0.0291  205 PRO A CG  
1343 C CD  . PRO A 203 ? 0.2081 0.1102 0.1094 -0.0294 -0.0681 0.0267  205 PRO A CD  
1344 N N   . SER A 204 ? 0.2687 0.1276 0.1238 -0.0465 -0.0818 0.0447  206 SER A N   
1345 C CA  . SER A 204 ? 0.2906 0.1289 0.1302 -0.0455 -0.0900 0.0489  206 SER A CA  
1346 C C   . SER A 204 ? 0.2916 0.1370 0.1302 -0.0421 -0.0915 0.0487  206 SER A C   
1347 O O   . SER A 204 ? 0.3127 0.1446 0.1429 -0.0367 -0.0991 0.0504  206 SER A O   
1348 C CB  . SER A 204 ? 0.3131 0.1358 0.1329 -0.0583 -0.0920 0.0561  206 SER A CB  
1349 O OG  . SER A 204 ? 0.3088 0.1497 0.1262 -0.0693 -0.0859 0.0590  206 SER A OG  
1350 N N   . ASN A 205 ? 0.2762 0.1410 0.1209 -0.0445 -0.0851 0.0466  207 ASN A N   
1351 C CA  . ASN A 205 ? 0.2798 0.1506 0.1213 -0.0423 -0.0863 0.0458  207 ASN A CA  
1352 C C   . ASN A 205 ? 0.2652 0.1463 0.1212 -0.0342 -0.0856 0.0388  207 ASN A C   
1353 O O   . ASN A 205 ? 0.2637 0.1527 0.1182 -0.0339 -0.0841 0.0364  207 ASN A O   
1354 C CB  . ASN A 205 ? 0.2826 0.1663 0.1164 -0.0497 -0.0805 0.0475  207 ASN A CB  
1355 C CG  . ASN A 205 ? 0.2631 0.1656 0.1077 -0.0489 -0.0721 0.0429  207 ASN A CG  
1356 O OD1 . ASN A 205 ? 0.2513 0.1552 0.1077 -0.0456 -0.0702 0.0397  207 ASN A OD1 
1357 N ND2 . ASN A 205 ? 0.2643 0.1816 0.1032 -0.0509 -0.0673 0.0423  207 ASN A ND2 
1358 N N   . TYR A 206 ? 0.2593 0.1400 0.1275 -0.0288 -0.0866 0.0356  208 TYR A N   
1359 C CA  . TYR A 206 ? 0.2496 0.1402 0.1307 -0.0238 -0.0863 0.0299  208 TYR A CA  
1360 C C   . TYR A 206 ? 0.2594 0.1519 0.1372 -0.0214 -0.0922 0.0292  208 TYR A C   
1361 O O   . TYR A 206 ? 0.2540 0.1543 0.1353 -0.0223 -0.0911 0.0254  208 TYR A O   
1362 C CB  . TYR A 206 ? 0.2431 0.1340 0.1354 -0.0188 -0.0873 0.0276  208 TYR A CB  
1363 C CG  . TYR A 206 ? 0.2330 0.1368 0.1381 -0.0161 -0.0871 0.0225  208 TYR A CG  
1364 C CD1 . TYR A 206 ? 0.2211 0.1310 0.1318 -0.0195 -0.0815 0.0194  208 TYR A CD1 
1365 C CD2 . TYR A 206 ? 0.2403 0.1509 0.1506 -0.0107 -0.0931 0.0210  208 TYR A CD2 
1366 C CE1 . TYR A 206 ? 0.2144 0.1338 0.1337 -0.0200 -0.0817 0.0156  208 TYR A CE1 
1367 C CE2 . TYR A 206 ? 0.2301 0.1562 0.1518 -0.0112 -0.0928 0.0169  208 TYR A CE2 
1368 C CZ  . TYR A 206 ? 0.2190 0.1480 0.1442 -0.0173 -0.0871 0.0145  208 TYR A CZ  
1369 O OH  . TYR A 206 ? 0.2252 0.1674 0.1587 -0.0206 -0.0874 0.0113  208 TYR A OH  
1370 N N   . GLY A 207 ? 0.2844 0.1679 0.1535 -0.0187 -0.0992 0.0331  209 GLY A N   
1371 C CA  . GLY A 207 ? 0.2958 0.1822 0.1610 -0.0158 -0.1059 0.0331  209 GLY A CA  
1372 C C   . GLY A 207 ? 0.3083 0.1979 0.1647 -0.0213 -0.1043 0.0327  209 GLY A C   
1373 O O   . GLY A 207 ? 0.3201 0.2167 0.1771 -0.0205 -0.1082 0.0302  209 GLY A O   
1374 N N   . ASP A 208 ? 0.3155 0.2018 0.1627 -0.0269 -0.0987 0.0350  210 ASP A N   
1375 C CA  . ASP A 208 ? 0.3216 0.2121 0.1591 -0.0305 -0.0960 0.0337  210 ASP A CA  
1376 C C   . ASP A 208 ? 0.3062 0.2039 0.1502 -0.0296 -0.0923 0.0266  210 ASP A C   
1377 O O   . ASP A 208 ? 0.3068 0.2053 0.1418 -0.0305 -0.0923 0.0239  210 ASP A O   
1378 C CB  . ASP A 208 ? 0.3348 0.2254 0.1620 -0.0361 -0.0903 0.0377  210 ASP A CB  
1379 C CG  . ASP A 208 ? 0.3612 0.2404 0.1750 -0.0405 -0.0947 0.0458  210 ASP A CG  
1380 O OD1 . ASP A 208 ? 0.3880 0.2576 0.1976 -0.0369 -0.1030 0.0479  210 ASP A OD1 
1381 O OD2 . ASP A 208 ? 0.3649 0.2449 0.1715 -0.0478 -0.0904 0.0500  210 ASP A OD2 
1382 N N   . PHE A 209 ? 0.2838 0.1841 0.1406 -0.0281 -0.0892 0.0236  211 PHE A N   
1383 C CA  . PHE A 209 ? 0.2851 0.1870 0.1443 -0.0282 -0.0868 0.0176  211 PHE A CA  
1384 C C   . PHE A 209 ? 0.2973 0.2013 0.1590 -0.0298 -0.0934 0.0150  211 PHE A C   
1385 O O   . PHE A 209 ? 0.3057 0.2155 0.1768 -0.0284 -0.0978 0.0167  211 PHE A O   
1386 C CB  . PHE A 209 ? 0.2631 0.1664 0.1333 -0.0271 -0.0819 0.0160  211 PHE A CB  
1387 C CG  . PHE A 209 ? 0.2564 0.1614 0.1245 -0.0262 -0.0753 0.0175  211 PHE A CG  
1388 C CD1 . PHE A 209 ? 0.2520 0.1581 0.1214 -0.0278 -0.0747 0.0226  211 PHE A CD1 
1389 C CD2 . PHE A 209 ? 0.2536 0.1591 0.1168 -0.0236 -0.0704 0.0135  211 PHE A CD2 
1390 C CE1 . PHE A 209 ? 0.2493 0.1613 0.1174 -0.0292 -0.0688 0.0240  211 PHE A CE1 
1391 C CE2 . PHE A 209 ? 0.2496 0.1627 0.1124 -0.0219 -0.0646 0.0146  211 PHE A CE2 
1392 C CZ  . PHE A 209 ? 0.2461 0.1646 0.1123 -0.0259 -0.0636 0.0200  211 PHE A CZ  
1393 N N   . SER A 210 ? 0.3133 0.2133 0.1658 -0.0325 -0.0942 0.0107  212 SER A N   
1394 C CA  . SER A 210 ? 0.3270 0.2299 0.1803 -0.0373 -0.1004 0.0078  212 SER A CA  
1395 C C   . SER A 210 ? 0.3180 0.2229 0.1812 -0.0410 -0.0989 0.0052  212 SER A C   
1396 O O   . SER A 210 ? 0.3069 0.2229 0.1787 -0.0453 -0.1034 0.0048  212 SER A O   
1397 C CB  . SER A 210 ? 0.3555 0.2491 0.1911 -0.0403 -0.1023 0.0040  212 SER A CB  
1398 O OG  . SER A 210 ? 0.3945 0.2882 0.2203 -0.0377 -0.1035 0.0066  212 SER A OG  
1399 N N   . LYS A 211 ? 0.3215 0.2173 0.1823 -0.0392 -0.0928 0.0037  213 LYS A N   
1400 C CA  . LYS A 211 ? 0.3202 0.2157 0.1888 -0.0422 -0.0905 0.0023  213 LYS A CA  
1401 C C   . LYS A 211 ? 0.2963 0.1901 0.1698 -0.0360 -0.0837 0.0038  213 LYS A C   
1402 O O   . LYS A 211 ? 0.2909 0.1822 0.1580 -0.0309 -0.0804 0.0046  213 LYS A O   
1403 C CB  . LYS A 211 ? 0.3634 0.2439 0.2175 -0.0486 -0.0924 -0.0019 213 LYS A CB  
1404 C CG  . LYS A 211 ? 0.4135 0.2760 0.2479 -0.0434 -0.0903 -0.0052 213 LYS A CG  
1405 C CD  . LYS A 211 ? 0.4705 0.3114 0.2861 -0.0492 -0.0935 -0.0099 213 LYS A CD  
1406 C CE  . LYS A 211 ? 0.5135 0.3350 0.3102 -0.0395 -0.0903 -0.0140 213 LYS A CE  
1407 N NZ  . LYS A 211 ? 0.5205 0.3447 0.3081 -0.0331 -0.0899 -0.0154 213 LYS A NZ  
1408 N N   . TYR A 212 ? 0.2662 0.1637 0.1503 -0.0373 -0.0815 0.0040  214 TYR A N   
1409 C CA  . TYR A 212 ? 0.2446 0.1427 0.1344 -0.0322 -0.0759 0.0055  214 TYR A CA  
1410 C C   . TYR A 212 ? 0.2435 0.1362 0.1342 -0.0344 -0.0735 0.0038  214 TYR A C   
1411 O O   . TYR A 212 ? 0.2295 0.1295 0.1296 -0.0390 -0.0744 0.0041  214 TYR A O   
1412 C CB  . TYR A 212 ? 0.2259 0.1349 0.1283 -0.0297 -0.0761 0.0090  214 TYR A CB  
1413 C CG  . TYR A 212 ? 0.2168 0.1251 0.1204 -0.0259 -0.0713 0.0112  214 TYR A CG  
1414 C CD1 . TYR A 212 ? 0.2196 0.1269 0.1153 -0.0244 -0.0700 0.0133  214 TYR A CD1 
1415 C CD2 . TYR A 212 ? 0.2024 0.1129 0.1141 -0.0251 -0.0679 0.0111  214 TYR A CD2 
1416 C CE1 . TYR A 212 ? 0.2137 0.1240 0.1104 -0.0236 -0.0659 0.0157  214 TYR A CE1 
1417 C CE2 . TYR A 212 ? 0.1997 0.1113 0.1122 -0.0232 -0.0641 0.0131  214 TYR A CE2 
1418 C CZ  . TYR A 212 ? 0.2024 0.1147 0.1077 -0.0231 -0.0632 0.0155  214 TYR A CZ  
1419 O OH  . TYR A 212 ? 0.1953 0.1120 0.1013 -0.0235 -0.0595 0.0175  214 TYR A OH  
1420 N N   . HIS A 213 ? 0.2548 0.1355 0.1343 -0.0303 -0.0705 0.0020  215 HIS A N   
1421 C CA  . HIS A 213 ? 0.2607 0.1326 0.1376 -0.0307 -0.0685 0.0010  215 HIS A CA  
1422 C C   . HIS A 213 ? 0.2351 0.1192 0.1269 -0.0281 -0.0646 0.0036  215 HIS A C   
1423 O O   . HIS A 213 ? 0.2211 0.1137 0.1179 -0.0237 -0.0623 0.0053  215 HIS A O   
1424 C CB  . HIS A 213 ? 0.2905 0.1460 0.1497 -0.0234 -0.0673 -0.0020 215 HIS A CB  
1425 C CG  . HIS A 213 ? 0.3184 0.1608 0.1714 -0.0229 -0.0665 -0.0027 215 HIS A CG  
1426 N ND1 . HIS A 213 ? 0.3510 0.1774 0.1941 -0.0321 -0.0704 -0.0033 215 HIS A ND1 
1427 C CD2 . HIS A 213 ? 0.3282 0.1717 0.1829 -0.0156 -0.0629 -0.0021 215 HIS A CD2 
1428 C CE1 . HIS A 213 ? 0.3629 0.1781 0.2002 -0.0301 -0.0692 -0.0029 215 HIS A CE1 
1429 N NE2 . HIS A 213 ? 0.3418 0.1681 0.1870 -0.0192 -0.0647 -0.0024 215 HIS A NE2 
1430 N N   . PHE A 214 ? 0.2319 0.1160 0.1285 -0.0323 -0.0640 0.0039  216 PHE A N   
1431 C CA  . PHE A 214 ? 0.2184 0.1136 0.1282 -0.0307 -0.0608 0.0058  216 PHE A CA  
1432 C C   . PHE A 214 ? 0.2248 0.1131 0.1315 -0.0333 -0.0594 0.0056  216 PHE A C   
1433 O O   . PHE A 214 ? 0.2332 0.1197 0.1382 -0.0416 -0.0614 0.0054  216 PHE A O   
1434 C CB  . PHE A 214 ? 0.2111 0.1210 0.1342 -0.0333 -0.0627 0.0068  216 PHE A CB  
1435 C CG  . PHE A 214 ? 0.2033 0.1222 0.1376 -0.0305 -0.0601 0.0078  216 PHE A CG  
1436 C CD1 . PHE A 214 ? 0.1996 0.1226 0.1386 -0.0334 -0.0582 0.0074  216 PHE A CD1 
1437 C CD2 . PHE A 214 ? 0.2047 0.1263 0.1424 -0.0260 -0.0600 0.0094  216 PHE A CD2 
1438 C CE1 . PHE A 214 ? 0.1925 0.1228 0.1400 -0.0303 -0.0560 0.0076  216 PHE A CE1 
1439 C CE2 . PHE A 214 ? 0.1975 0.1233 0.1422 -0.0238 -0.0585 0.0098  216 PHE A CE2 
1440 C CZ  . PHE A 214 ? 0.1920 0.1226 0.1419 -0.0253 -0.0564 0.0085  216 PHE A CZ  
1441 N N   . SER A 215 ? 0.2240 0.1094 0.1287 -0.0271 -0.0563 0.0059  217 SER A N   
1442 C CA  . SER A 215 ? 0.2296 0.1059 0.1285 -0.0283 -0.0554 0.0062  217 SER A CA  
1443 C C   . SER A 215 ? 0.2151 0.1008 0.1221 -0.0228 -0.0518 0.0074  217 SER A C   
1444 O O   . SER A 215 ? 0.2163 0.1043 0.1212 -0.0152 -0.0502 0.0072  217 SER A O   
1445 C CB  . SER A 215 ? 0.2527 0.1064 0.1310 -0.0252 -0.0577 0.0045  217 SER A CB  
1446 O OG  . SER A 215 ? 0.2659 0.1074 0.1358 -0.0263 -0.0578 0.0054  217 SER A OG  
1447 N N   . VAL A 216 ? 0.2090 0.1020 0.1247 -0.0272 -0.0505 0.0085  218 VAL A N   
1448 C CA  . VAL A 216 ? 0.2036 0.1038 0.1252 -0.0238 -0.0476 0.0094  218 VAL A CA  
1449 C C   . VAL A 216 ? 0.2158 0.1042 0.1268 -0.0234 -0.0476 0.0101  218 VAL A C   
1450 O O   . VAL A 216 ? 0.2165 0.0972 0.1219 -0.0308 -0.0488 0.0106  218 VAL A O   
1451 C CB  . VAL A 216 ? 0.1930 0.1066 0.1279 -0.0274 -0.0466 0.0095  218 VAL A CB  
1452 C CG1 . VAL A 216 ? 0.1887 0.1071 0.1272 -0.0258 -0.0441 0.0100  218 VAL A CG1 
1453 C CG2 . VAL A 216 ? 0.1923 0.1130 0.1341 -0.0258 -0.0477 0.0092  218 VAL A CG2 
1454 N N   . LYS A 217 ? 0.2209 0.1092 0.1283 -0.0153 -0.0465 0.0103  219 LYS A N   
1455 C CA  A LYS A 217 ? 0.2302 0.1071 0.1265 -0.0124 -0.0471 0.0112  219 LYS A CA  
1456 C CA  B LYS A 217 ? 0.2353 0.1121 0.1317 -0.0127 -0.0471 0.0112  219 LYS A CA  
1457 C C   . LYS A 217 ? 0.2173 0.1085 0.1233 -0.0112 -0.0446 0.0123  219 LYS A C   
1458 O O   . LYS A 217 ? 0.2020 0.1080 0.1166 -0.0074 -0.0431 0.0119  219 LYS A O   
1459 C CB  A LYS A 217 ? 0.2492 0.1143 0.1307 -0.0011 -0.0490 0.0097  219 LYS A CB  
1460 C CB  B LYS A 217 ? 0.2646 0.1278 0.1450 -0.0015 -0.0492 0.0099  219 LYS A CB  
1461 C CG  A LYS A 217 ? 0.2717 0.1185 0.1362 0.0047  -0.0514 0.0105  219 LYS A CG  
1462 C CG  B LYS A 217 ? 0.2926 0.1416 0.1591 0.0035  -0.0509 0.0112  219 LYS A CG  
1463 C CD  A LYS A 217 ? 0.2923 0.1252 0.1394 0.0189  -0.0541 0.0079  219 LYS A CD  
1464 C CD  B LYS A 217 ? 0.3263 0.1624 0.1755 0.0188  -0.0536 0.0092  219 LYS A CD  
1465 C CE  A LYS A 217 ? 0.3061 0.1209 0.1411 0.0166  -0.0568 0.0056  219 LYS A CE  
1466 C CE  B LYS A 217 ? 0.3525 0.1757 0.1883 0.0255  -0.0560 0.0108  219 LYS A CE  
1467 N NZ  A LYS A 217 ? 0.3251 0.1136 0.1456 0.0043  -0.0603 0.0073  219 LYS A NZ  
1468 N NZ  B LYS A 217 ? 0.3762 0.1921 0.1967 0.0446  -0.0588 0.0082  219 LYS A NZ  
1469 N N   . ASP A 218 ? 0.2174 0.1042 0.1206 -0.0159 -0.0444 0.0138  220 ASP A N   
1470 C CA  . ASP A 218 ? 0.2147 0.1128 0.1243 -0.0152 -0.0425 0.0145  220 ASP A CA  
1471 C C   . ASP A 218 ? 0.2274 0.1119 0.1222 -0.0113 -0.0443 0.0164  220 ASP A C   
1472 O O   . ASP A 218 ? 0.2424 0.1087 0.1238 -0.0161 -0.0463 0.0179  220 ASP A O   
1473 C CB  . ASP A 218 ? 0.2132 0.1214 0.1335 -0.0236 -0.0404 0.0142  220 ASP A CB  
1474 C CG  . ASP A 218 ? 0.2296 0.1485 0.1556 -0.0235 -0.0386 0.0141  220 ASP A CG  
1475 O OD1 . ASP A 218 ? 0.2448 0.1646 0.1669 -0.0181 -0.0391 0.0150  220 ASP A OD1 
1476 O OD2 . ASP A 218 ? 0.2467 0.1746 0.1809 -0.0278 -0.0369 0.0125  220 ASP A OD2 
1477 N N   . SER A 219 ? 0.2226 0.1156 0.1180 -0.0028 -0.0444 0.0166  221 SER A N   
1478 C CA  . SER A 219 ? 0.2425 0.1234 0.1229 0.0036  -0.0470 0.0184  221 SER A CA  
1479 C C   . SER A 219 ? 0.2528 0.1285 0.1299 -0.0053 -0.0464 0.0208  221 SER A C   
1480 O O   . SER A 219 ? 0.2683 0.1259 0.1281 -0.0035 -0.0493 0.0233  221 SER A O   
1481 C CB  . SER A 219 ? 0.2349 0.1327 0.1191 0.0146  -0.0473 0.0179  221 SER A CB  
1482 O OG  . SER A 219 ? 0.2109 0.1300 0.1101 0.0088  -0.0447 0.0178  221 SER A OG  
1483 N N   . MET A 220 ? 0.2492 0.1408 0.1411 -0.0140 -0.0430 0.0199  222 MET A N   
1484 C CA  . MET A 220 ? 0.2657 0.1611 0.1579 -0.0213 -0.0413 0.0212  222 MET A CA  
1485 C C   . MET A 220 ? 0.2726 0.1734 0.1621 -0.0148 -0.0423 0.0222  222 MET A C   
1486 O O   . MET A 220 ? 0.2640 0.1687 0.1530 -0.0050 -0.0442 0.0218  222 MET A O   
1487 C CB  . MET A 220 ? 0.2930 0.1704 0.1700 -0.0298 -0.0424 0.0242  222 MET A CB  
1488 C CG  . MET A 220 ? 0.2950 0.1676 0.1728 -0.0369 -0.0425 0.0234  222 MET A CG  
1489 S SD  . MET A 220 ? 0.3326 0.1904 0.1937 -0.0529 -0.0434 0.0274  222 MET A SD  
1490 C CE  . MET A 220 ? 0.3673 0.1877 0.2018 -0.0490 -0.0499 0.0296  222 MET A CE  
1491 N N   . THR A 221 ? 0.2945 0.1984 0.1822 -0.0204 -0.0410 0.0233  223 THR A N   
1492 C CA  . THR A 221 ? 0.3104 0.2236 0.1979 -0.0160 -0.0417 0.0237  223 THR A CA  
1493 C C   . THR A 221 ? 0.3281 0.2247 0.1966 -0.0156 -0.0445 0.0279  223 THR A C   
1494 O O   . THR A 221 ? 0.3440 0.2313 0.2047 -0.0251 -0.0433 0.0300  223 THR A O   
1495 C CB  . THR A 221 ? 0.3132 0.2433 0.2131 -0.0221 -0.0384 0.0208  223 THR A CB  
1496 O OG1 . THR A 221 ? 0.2959 0.2339 0.2089 -0.0231 -0.0368 0.0175  223 THR A OG1 
1497 C CG2 . THR A 221 ? 0.2997 0.2408 0.2000 -0.0188 -0.0397 0.0206  223 THR A CG2 
1498 N N   . SER A 222 ? 0.3472 0.2406 0.2070 -0.0046 -0.0485 0.0295  224 SER A N   
1499 C CA  . SER A 222 ? 0.3951 0.2676 0.2327 -0.0017 -0.0526 0.0339  224 SER A CA  
1500 C C   . SER A 222 ? 0.4003 0.2768 0.2345 -0.0104 -0.0511 0.0360  224 SER A C   
1501 O O   . SER A 222 ? 0.4379 0.2947 0.2534 -0.0164 -0.0527 0.0404  224 SER A O   
1502 C CB  . SER A 222 ? 0.4283 0.3017 0.2595 0.0149  -0.0575 0.0341  224 SER A CB  
1503 O OG  . SER A 222 ? 0.4872 0.3355 0.2936 0.0198  -0.0628 0.0385  224 SER A OG  
1504 N N   . GLY A 223 ? 0.3561 0.2567 0.2058 -0.0122 -0.0483 0.0330  225 GLY A N   
1505 C CA  . GLY A 223 ? 0.3435 0.2486 0.1890 -0.0197 -0.0466 0.0342  225 GLY A CA  
1506 C C   . GLY A 223 ? 0.3158 0.2281 0.1695 -0.0322 -0.0408 0.0318  225 GLY A C   
1507 O O   . GLY A 223 ? 0.2987 0.2234 0.1555 -0.0368 -0.0381 0.0299  225 GLY A O   
1508 N N   . MET A 224 ? 0.2964 0.2027 0.1531 -0.0367 -0.0391 0.0314  226 MET A N   
1509 C CA  . MET A 224 ? 0.2858 0.2024 0.1501 -0.0471 -0.0340 0.0291  226 MET A CA  
1510 C C   . MET A 224 ? 0.2996 0.2019 0.1532 -0.0561 -0.0343 0.0328  226 MET A C   
1511 O O   . MET A 224 ? 0.3171 0.1992 0.1601 -0.0529 -0.0384 0.0355  226 MET A O   
1512 C CB  . MET A 224 ? 0.2643 0.1958 0.1485 -0.0440 -0.0317 0.0232  226 MET A CB  
1513 C CG  . MET A 224 ? 0.2547 0.2006 0.1476 -0.0405 -0.0308 0.0190  226 MET A CG  
1514 S SD  . MET A 224 ? 0.2472 0.2019 0.1573 -0.0374 -0.0297 0.0133  226 MET A SD  
1515 C CE  . MET A 224 ? 0.2462 0.2075 0.1581 -0.0337 -0.0320 0.0110  226 MET A CE  
1516 N N   . ILE A 225 ? 0.2970 0.2117 0.1534 -0.0674 -0.0299 0.0322  227 ILE A N   
1517 C CA  . ILE A 225 ? 0.3158 0.2246 0.1654 -0.0794 -0.0295 0.0350  227 ILE A CA  
1518 C C   . ILE A 225 ? 0.2989 0.2277 0.1687 -0.0796 -0.0263 0.0296  227 ILE A C   
1519 O O   . ILE A 225 ? 0.2913 0.2438 0.1753 -0.0778 -0.0221 0.0247  227 ILE A O   
1520 C CB  . ILE A 225 ? 0.3403 0.2535 0.1772 -0.0937 -0.0269 0.0390  227 ILE A CB  
1521 C CG1 . ILE A 225 ? 0.3730 0.2625 0.1868 -0.0930 -0.0312 0.0451  227 ILE A CG1 
1522 C CG2 . ILE A 225 ? 0.3543 0.2665 0.1848 -0.1098 -0.0263 0.0420  227 ILE A CG2 
1523 C CD1 . ILE A 225 ? 0.3848 0.2829 0.1877 -0.1049 -0.0281 0.0483  227 ILE A CD1 
1524 N N   . ASN A 226 ? 0.3002 0.2180 0.1690 -0.0811 -0.0289 0.0304  228 ASN A N   
1525 C CA  . ASN A 226 ? 0.2966 0.2323 0.1824 -0.0818 -0.0268 0.0261  228 ASN A CA  
1526 C C   . ASN A 226 ? 0.3011 0.2569 0.1881 -0.0962 -0.0232 0.0267  228 ASN A C   
1527 O O   . ASN A 226 ? 0.3280 0.2739 0.1985 -0.1099 -0.0241 0.0321  228 ASN A O   
1528 C CB  . ASN A 226 ? 0.3040 0.2220 0.1871 -0.0788 -0.0309 0.0267  228 ASN A CB  
1529 C CG  . ASN A 226 ? 0.2998 0.2360 0.2011 -0.0768 -0.0295 0.0221  228 ASN A CG  
1530 O OD1 . ASN A 226 ? 0.2983 0.2502 0.2038 -0.0864 -0.0278 0.0217  228 ASN A OD1 
1531 N ND2 . ASN A 226 ? 0.3019 0.2383 0.2133 -0.0648 -0.0304 0.0189  228 ASN A ND2 
1532 N N   . ASN A 227 ? 0.2778 0.2630 0.1831 -0.0930 -0.0192 0.0210  229 ASN A N   
1533 C CA  . ASN A 227 ? 0.2809 0.2943 0.1902 -0.1044 -0.0151 0.0204  229 ASN A CA  
1534 C C   . ASN A 227 ? 0.2918 0.3113 0.2036 -0.1143 -0.0167 0.0216  229 ASN A C   
1535 O O   . ASN A 227 ? 0.3109 0.3561 0.2250 -0.1265 -0.0138 0.0220  229 ASN A O   
1536 C CB  . ASN A 227 ? 0.2632 0.3076 0.1891 -0.0946 -0.0105 0.0130  229 ASN A CB  
1537 C CG  . ASN A 227 ? 0.2673 0.3102 0.1881 -0.0895 -0.0083 0.0118  229 ASN A CG  
1538 O OD1 . ASN A 227 ? 0.2848 0.3203 0.1910 -0.0992 -0.0077 0.0170  229 ASN A OD1 
1539 N ND2 . ASN A 227 ? 0.2518 0.2988 0.1818 -0.0750 -0.0079 0.0054  229 ASN A ND2 
1540 N N   . GLY A 228 ? 0.2930 0.2914 0.2035 -0.1099 -0.0213 0.0221  230 GLY A N   
1541 C CA  . GLY A 228 ? 0.3171 0.3178 0.2274 -0.1199 -0.0238 0.0233  230 GLY A CA  
1542 C C   . GLY A 228 ? 0.3115 0.3511 0.2429 -0.1176 -0.0211 0.0179  230 GLY A C   
1543 O O   . GLY A 228 ? 0.3547 0.4112 0.2867 -0.1311 -0.0214 0.0192  230 GLY A O   
1544 N N   . ASP A 229 ? 0.2765 0.3292 0.2231 -0.1005 -0.0192 0.0119  231 ASP A N   
1545 C CA  . ASP A 229 ? 0.2608 0.3482 0.2252 -0.0938 -0.0175 0.0060  231 ASP A CA  
1546 C C   . ASP A 229 ? 0.2404 0.3171 0.2129 -0.0803 -0.0214 0.0030  231 ASP A C   
1547 O O   . ASP A 229 ? 0.2317 0.3211 0.2153 -0.0661 -0.0212 -0.0024 231 ASP A O   
1548 C CB  . ASP A 229 ? 0.2555 0.3645 0.2265 -0.0845 -0.0127 0.0010  231 ASP A CB  
1549 C CG  . ASP A 229 ? 0.2522 0.3378 0.2202 -0.0709 -0.0133 -0.0009 231 ASP A CG  
1550 O OD1 . ASP A 229 ? 0.2351 0.2902 0.1958 -0.0697 -0.0167 0.0023  231 ASP A OD1 
1551 O OD2 . ASP A 229 ? 0.2634 0.3626 0.2357 -0.0614 -0.0105 -0.0062 231 ASP A OD2 
1552 N N   . ILE A 230 ? 0.2487 0.2993 0.2127 -0.0846 -0.0255 0.0068  232 ILE A N   
1553 C CA  . ILE A 230 ? 0.2428 0.2797 0.2113 -0.0732 -0.0290 0.0050  232 ILE A CA  
1554 C C   . ILE A 230 ? 0.2240 0.2840 0.2046 -0.0709 -0.0308 0.0019  232 ILE A C   
1555 O O   . ILE A 230 ? 0.2276 0.3043 0.2089 -0.0831 -0.0313 0.0033  232 ILE A O   
1556 C CB  . ILE A 230 ? 0.2681 0.2719 0.2225 -0.0771 -0.0324 0.0093  232 ILE A CB  
1557 C CG1 . ILE A 230 ? 0.2796 0.2714 0.2379 -0.0658 -0.0354 0.0077  232 ILE A CG1 
1558 C CG2 . ILE A 230 ? 0.2914 0.2909 0.2353 -0.0934 -0.0346 0.0130  232 ILE A CG2 
1559 C CD1 . ILE A 230 ? 0.3012 0.2639 0.2471 -0.0633 -0.0373 0.0104  232 ILE A CD1 
1560 N N   . GLN A 231 ? 0.2049 0.2656 0.1937 -0.0557 -0.0324 -0.0020 233 GLN A N   
1561 C CA  . GLN A 231 ? 0.1960 0.2748 0.1949 -0.0497 -0.0353 -0.0049 233 GLN A CA  
1562 C C   . GLN A 231 ? 0.1806 0.2357 0.1773 -0.0398 -0.0393 -0.0049 233 GLN A C   
1563 O O   . GLN A 231 ? 0.1692 0.2036 0.1609 -0.0339 -0.0389 -0.0046 233 GLN A O   
1564 C CB  . GLN A 231 ? 0.2010 0.3094 0.2106 -0.0383 -0.0334 -0.0108 233 GLN A CB  
1565 C CG  . GLN A 231 ? 0.2107 0.3493 0.2233 -0.0476 -0.0286 -0.0114 233 GLN A CG  
1566 C CD  . GLN A 231 ? 0.2244 0.3877 0.2408 -0.0625 -0.0295 -0.0091 233 GLN A CD  
1567 O OE1 . GLN A 231 ? 0.2517 0.4139 0.2706 -0.0629 -0.0340 -0.0085 233 GLN A OE1 
1568 N NE2 . GLN A 231 ? 0.2358 0.4221 0.2515 -0.0764 -0.0254 -0.0076 233 GLN A NE2 
1569 N N   . VAL A 232 ? 0.1675 0.2290 0.1681 -0.0391 -0.0433 -0.0051 234 VAL A N   
1570 C CA  . VAL A 232 ? 0.1651 0.2071 0.1628 -0.0311 -0.0474 -0.0047 234 VAL A CA  
1571 C C   . VAL A 232 ? 0.1591 0.2179 0.1649 -0.0187 -0.0509 -0.0085 234 VAL A C   
1572 O O   . VAL A 232 ? 0.1525 0.2404 0.1667 -0.0199 -0.0516 -0.0104 234 VAL A O   
1573 C CB  . VAL A 232 ? 0.1695 0.1974 0.1600 -0.0409 -0.0499 -0.0011 234 VAL A CB  
1574 C CG1 . VAL A 232 ? 0.1732 0.1793 0.1586 -0.0337 -0.0527 0.0000  234 VAL A CG1 
1575 C CG2 . VAL A 232 ? 0.1782 0.1921 0.1585 -0.0527 -0.0474 0.0020  234 VAL A CG2 
1576 N N   . TYR A 233 ? 0.1592 0.1995 0.1610 -0.0070 -0.0536 -0.0092 235 TYR A N   
1577 C CA  . TYR A 233 ? 0.1644 0.2135 0.1694 0.0075  -0.0579 -0.0129 235 TYR A CA  
1578 C C   . TYR A 233 ? 0.1674 0.1950 0.1652 0.0117  -0.0634 -0.0105 235 TYR A C   
1579 O O   . TYR A 233 ? 0.1685 0.1712 0.1578 0.0074  -0.0630 -0.0071 235 TYR A O   
1580 C CB  . TYR A 233 ? 0.1714 0.2158 0.1736 0.0194  -0.0569 -0.0171 235 TYR A CB  
1581 C CG  . TYR A 233 ? 0.1715 0.2403 0.1804 0.0172  -0.0514 -0.0202 235 TYR A CG  
1582 C CD1 . TYR A 233 ? 0.1733 0.2783 0.1924 0.0228  -0.0510 -0.0246 235 TYR A CD1 
1583 C CD2 . TYR A 233 ? 0.1681 0.2264 0.1727 0.0090  -0.0465 -0.0186 235 TYR A CD2 
1584 C CE1 . TYR A 233 ? 0.1698 0.3000 0.1942 0.0193  -0.0454 -0.0271 235 TYR A CE1 
1585 C CE2 . TYR A 233 ? 0.1682 0.2479 0.1771 0.0059  -0.0415 -0.0209 235 TYR A CE2 
1586 C CZ  . TYR A 233 ? 0.1694 0.2853 0.1880 0.0101  -0.0406 -0.0250 235 TYR A CZ  
1587 O OH  . TYR A 233 ? 0.1717 0.3099 0.1933 0.0052  -0.0350 -0.0267 235 TYR A OH  
1588 N N   . LEU A 234 ? 0.1697 0.2098 0.1707 0.0206  -0.0686 -0.0123 236 LEU A N   
1589 C CA  . LEU A 234 ? 0.1776 0.1965 0.1696 0.0275  -0.0747 -0.0103 236 LEU A CA  
1590 C C   . LEU A 234 ? 0.1935 0.1993 0.1778 0.0439  -0.0783 -0.0135 236 LEU A C   
1591 O O   . LEU A 234 ? 0.1963 0.2219 0.1859 0.0566  -0.0802 -0.0185 236 LEU A O   
1592 C CB  . LEU A 234 ? 0.1780 0.2158 0.1754 0.0276  -0.0794 -0.0099 236 LEU A CB  
1593 C CG  . LEU A 234 ? 0.1929 0.2152 0.1813 0.0381  -0.0870 -0.0086 236 LEU A CG  
1594 C CD1 . LEU A 234 ? 0.1977 0.1858 0.1726 0.0315  -0.0870 -0.0036 236 LEU A CD1 
1595 C CD2 . LEU A 234 ? 0.1923 0.2376 0.1872 0.0372  -0.0916 -0.0085 236 LEU A CD2 
1596 N N   . GLN A 235 ? 0.2063 0.1790 0.1769 0.0433  -0.0796 -0.0109 237 GLN A N   
1597 C CA  . GLN A 235 ? 0.2292 0.1805 0.1870 0.0560  -0.0836 -0.0135 237 GLN A CA  
1598 C C   . GLN A 235 ? 0.2503 0.1740 0.1925 0.0599  -0.0912 -0.0098 237 GLN A C   
1599 O O   . GLN A 235 ? 0.2515 0.1583 0.1870 0.0480  -0.0906 -0.0042 237 GLN A O   
1600 C CB  . GLN A 235 ? 0.2309 0.1651 0.1827 0.0489  -0.0791 -0.0131 237 GLN A CB  
1601 C CG  . GLN A 235 ? 0.2571 0.1650 0.1923 0.0598  -0.0837 -0.0162 237 GLN A CG  
1602 C CD  . GLN A 235 ? 0.2588 0.1525 0.1886 0.0494  -0.0794 -0.0152 237 GLN A CD  
1603 O OE1 . GLN A 235 ? 0.2432 0.1528 0.1814 0.0480  -0.0738 -0.0184 237 GLN A OE1 
1604 N NE2 . GLN A 235 ? 0.2767 0.1418 0.1917 0.0413  -0.0822 -0.0105 237 GLN A NE2 
1605 N N   . GLN A 236 ? 0.2699 0.1901 0.2053 0.0771  -0.0985 -0.0129 238 GLN A N   
1606 C CA  . GLN A 236 ? 0.3001 0.1882 0.2154 0.0829  -0.1073 -0.0094 238 GLN A CA  
1607 C C   . GLN A 236 ? 0.3232 0.2064 0.2294 0.1065  -0.1152 -0.0152 238 GLN A C   
1608 O O   . GLN A 236 ? 0.3121 0.2287 0.2328 0.1182  -0.1139 -0.0213 238 GLN A O   
1609 C CB  . GLN A 236 ? 0.2998 0.1966 0.2192 0.0763  -0.1093 -0.0045 238 GLN A CB  
1610 C CG  . GLN A 236 ? 0.2909 0.2286 0.2296 0.0818  -0.1091 -0.0080 238 GLN A CG  
1611 C CD  . GLN A 236 ? 0.2868 0.2333 0.2300 0.0704  -0.1094 -0.0033 238 GLN A CD  
1612 O OE1 . GLN A 236 ? 0.3023 0.2246 0.2334 0.0617  -0.1105 0.0022  238 GLN A OE1 
1613 N NE2 . GLN A 236 ? 0.2737 0.2559 0.2331 0.0700  -0.1088 -0.0057 238 GLN A NE2 
1614 N N   . GLY A 237 ? 0.3597 0.2011 0.2399 0.1138  -0.1236 -0.0133 239 GLY A N   
1615 C CA  . GLY A 237 ? 0.3930 0.2224 0.2591 0.1390  -0.1327 -0.0189 239 GLY A CA  
1616 C C   . GLY A 237 ? 0.3995 0.2353 0.2667 0.1517  -0.1300 -0.0278 239 GLY A C   
1617 O O   . GLY A 237 ? 0.4190 0.2632 0.2831 0.1757  -0.1352 -0.0349 239 GLY A O   
1618 N N   . GLY A 238 ? 0.3852 0.2178 0.2559 0.1368  -0.1222 -0.0276 240 GLY A N   
1619 C CA  . GLY A 238 ? 0.3951 0.2338 0.2662 0.1464  -0.1189 -0.0357 240 GLY A CA  
1620 C C   . GLY A 238 ? 0.3705 0.2653 0.2697 0.1524  -0.1116 -0.0416 240 GLY A C   
1621 O O   . GLY A 238 ? 0.3732 0.2786 0.2726 0.1652  -0.1097 -0.0495 240 GLY A O   
1622 N N   . SER A 239 ? 0.3435 0.2735 0.2646 0.1413  -0.1075 -0.0377 241 SER A N   
1623 C CA  . SER A 239 ? 0.3231 0.3062 0.2690 0.1423  -0.1007 -0.0422 241 SER A CA  
1624 C C   . SER A 239 ? 0.2916 0.2942 0.2547 0.1171  -0.0925 -0.0362 241 SER A C   
1625 O O   . SER A 239 ? 0.2821 0.2622 0.2399 0.1025  -0.0929 -0.0292 241 SER A O   
1626 C CB  . SER A 239 ? 0.3288 0.3419 0.2822 0.1605  -0.1063 -0.0460 241 SER A CB  
1627 O OG  . SER A 239 ? 0.3275 0.3402 0.2838 0.1513  -0.1098 -0.0393 241 SER A OG  
1628 N N   . GLU A 240 ? 0.2762 0.3199 0.2575 0.1126  -0.0854 -0.0393 242 GLU A N   
1629 C CA  . GLU A 240 ? 0.2520 0.3116 0.2461 0.0898  -0.0781 -0.0345 242 GLU A CA  
1630 C C   . GLU A 240 ? 0.2298 0.3386 0.2426 0.0867  -0.0761 -0.0360 242 GLU A C   
1631 O O   . GLU A 240 ? 0.2311 0.3726 0.2516 0.0997  -0.0757 -0.0423 242 GLU A O   
1632 C CB  . GLU A 240 ? 0.2555 0.3091 0.2485 0.0812  -0.0708 -0.0352 242 GLU A CB  
1633 C CG  . GLU A 240 ? 0.2739 0.2827 0.2507 0.0754  -0.0720 -0.0314 242 GLU A CG  
1634 C CD  . GLU A 240 ? 0.2819 0.2850 0.2573 0.0665  -0.0656 -0.0317 242 GLU A CD  
1635 O OE1 . GLU A 240 ? 0.2788 0.3094 0.2629 0.0679  -0.0605 -0.0359 242 GLU A OE1 
1636 O OE2 . GLU A 240 ? 0.2877 0.2610 0.2528 0.0577  -0.0657 -0.0276 242 GLU A OE2 
1637 N N   . VAL A 241 ? 0.2078 0.3215 0.2263 0.0688  -0.0750 -0.0302 243 VAL A N   
1638 C CA  . VAL A 241 ? 0.1920 0.3480 0.2257 0.0583  -0.0728 -0.0301 243 VAL A CA  
1639 C C   . VAL A 241 ? 0.1713 0.3207 0.2054 0.0343  -0.0665 -0.0250 243 VAL A C   
1640 O O   . VAL A 241 ? 0.1658 0.2812 0.1905 0.0261  -0.0667 -0.0202 243 VAL A O   
1641 C CB  . VAL A 241 ? 0.1999 0.3646 0.2359 0.0609  -0.0800 -0.0285 243 VAL A CB  
1642 C CG1 . VAL A 241 ? 0.1932 0.4037 0.2440 0.0483  -0.0785 -0.0285 243 VAL A CG1 
1643 C CG2 . VAL A 241 ? 0.2196 0.3818 0.2505 0.0867  -0.0877 -0.0328 243 VAL A CG2 
1644 N N   . ALA A 242 ? 0.1603 0.3427 0.2038 0.0237  -0.0613 -0.0259 244 ALA A N   
1645 C CA  . ALA A 242 ? 0.1512 0.3265 0.1922 0.0014  -0.0565 -0.0210 244 ALA A CA  
1646 C C   . ALA A 242 ? 0.1507 0.3230 0.1902 -0.0125 -0.0601 -0.0166 244 ALA A C   
1647 O O   . ALA A 242 ? 0.1513 0.3523 0.1987 -0.0120 -0.0639 -0.0179 244 ALA A O   
1648 C CB  . ALA A 242 ? 0.1469 0.3572 0.1954 -0.0072 -0.0507 -0.0227 244 ALA A CB  
1649 N N   . ILE A 243 ? 0.1496 0.2879 0.1781 -0.0239 -0.0592 -0.0119 245 ILE A N   
1650 C CA  . ILE A 243 ? 0.1540 0.2827 0.1770 -0.0367 -0.0626 -0.0083 245 ILE A CA  
1651 C C   . ILE A 243 ? 0.1603 0.2722 0.1733 -0.0550 -0.0591 -0.0045 245 ILE A C   
1652 O O   . ILE A 243 ? 0.1614 0.2504 0.1638 -0.0635 -0.0615 -0.0017 245 ILE A O   
1653 C CB  . ILE A 243 ? 0.1557 0.2538 0.1709 -0.0275 -0.0668 -0.0070 245 ILE A CB  
1654 C CG1 . ILE A 243 ? 0.1556 0.2215 0.1624 -0.0229 -0.0635 -0.0057 245 ILE A CG1 
1655 C CG2 . ILE A 243 ? 0.1581 0.2701 0.1794 -0.0110 -0.0721 -0.0098 245 ILE A CG2 
1656 C CD1 . ILE A 243 ? 0.1580 0.1958 0.1558 -0.0178 -0.0667 -0.0035 245 ILE A CD1 
1657 N N   . THR A 244 ? 0.1639 0.2861 0.1783 -0.0603 -0.0540 -0.0047 246 THR A N   
1658 C CA  . THR A 244 ? 0.1801 0.2812 0.1820 -0.0748 -0.0510 -0.0009 246 THR A CA  
1659 C C   . THR A 244 ? 0.1979 0.2957 0.1903 -0.0945 -0.0540 0.0023  246 THR A C   
1660 O O   . THR A 244 ? 0.2063 0.2707 0.1826 -0.1019 -0.0548 0.0053  246 THR A O   
1661 C CB  . THR A 244 ? 0.1822 0.3008 0.1875 -0.0776 -0.0454 -0.0016 246 THR A CB  
1662 O OG1 . THR A 244 ? 0.1809 0.3015 0.1934 -0.0587 -0.0437 -0.0055 246 THR A OG1 
1663 C CG2 . THR A 244 ? 0.1928 0.2849 0.1832 -0.0890 -0.0428 0.0025  246 THR A CG2 
1664 N N   . ASP A 245 ? 0.2148 0.3471 0.2157 -0.1027 -0.0561 0.0013  247 ASP A N   
1665 C CA  . ASP A 245 ? 0.2405 0.3720 0.2308 -0.1249 -0.0594 0.0044  247 ASP A CA  
1666 C C   . ASP A 245 ? 0.2408 0.3410 0.2193 -0.1251 -0.0650 0.0052  247 ASP A C   
1667 O O   . ASP A 245 ? 0.2535 0.3383 0.2166 -0.1428 -0.0683 0.0077  247 ASP A O   
1668 C CB  . ASP A 245 ? 0.2578 0.4402 0.2620 -0.1334 -0.0607 0.0028  247 ASP A CB  
1669 C CG  . ASP A 245 ? 0.2806 0.5015 0.2964 -0.1346 -0.0549 0.0015  247 ASP A CG  
1670 O OD1 . ASP A 245 ? 0.3037 0.5082 0.3147 -0.1311 -0.0499 0.0022  247 ASP A OD1 
1671 O OD2 . ASP A 245 ? 0.3094 0.5789 0.3389 -0.1389 -0.0555 -0.0004 247 ASP A OD2 
1672 N N   . SER A 246 ? 0.2238 0.3142 0.2075 -0.1064 -0.0665 0.0031  248 SER A N   
1673 C CA  . SER A 246 ? 0.2249 0.2882 0.1972 -0.1057 -0.0712 0.0037  248 SER A CA  
1674 C C   . SER A 246 ? 0.2297 0.2495 0.1843 -0.1046 -0.0696 0.0055  248 SER A C   
1675 O O   . SER A 246 ? 0.2472 0.2421 0.1891 -0.1044 -0.0728 0.0057  248 SER A O   
1676 C CB  . SER A 246 ? 0.2178 0.2885 0.2003 -0.0882 -0.0738 0.0015  248 SER A CB  
1677 O OG  . SER A 246 ? 0.2143 0.3258 0.2125 -0.0857 -0.0762 -0.0006 248 SER A OG  
1678 N N   . PHE A 247 ? 0.2218 0.2336 0.1746 -0.1032 -0.0648 0.0066  249 PHE A N   
1679 C CA  . PHE A 247 ? 0.2269 0.2025 0.1650 -0.0987 -0.0633 0.0080  249 PHE A CA  
1680 C C   . PHE A 247 ? 0.2488 0.2064 0.1692 -0.1138 -0.0634 0.0108  249 PHE A C   
1681 O O   . PHE A 247 ? 0.2487 0.2249 0.1724 -0.1252 -0.0617 0.0121  249 PHE A O   
1682 C CB  . PHE A 247 ? 0.2123 0.1887 0.1596 -0.0836 -0.0587 0.0073  249 PHE A CB  
1683 C CG  . PHE A 247 ? 0.1988 0.1808 0.1564 -0.0691 -0.0596 0.0053  249 PHE A CG  
1684 C CD1 . PHE A 247 ? 0.1900 0.1992 0.1619 -0.0646 -0.0610 0.0033  249 PHE A CD1 
1685 C CD2 . PHE A 247 ? 0.1996 0.1601 0.1507 -0.0602 -0.0596 0.0057  249 PHE A CD2 
1686 C CE1 . PHE A 247 ? 0.1833 0.1920 0.1601 -0.0518 -0.0631 0.0022  249 PHE A CE1 
1687 C CE2 . PHE A 247 ? 0.1903 0.1537 0.1475 -0.0499 -0.0610 0.0049  249 PHE A CE2 
1688 C CZ  . PHE A 247 ? 0.1832 0.1678 0.1520 -0.0458 -0.0630 0.0034  249 PHE A CZ  
1689 N N   . SER A 248 ? 0.2714 0.1921 0.1714 -0.1128 -0.0655 0.0115  250 SER A N   
1690 C CA  . SER A 248 ? 0.3000 0.1927 0.1779 -0.1223 -0.0664 0.0143  250 SER A CA  
1691 C C   . SER A 248 ? 0.2904 0.1773 0.1707 -0.1108 -0.0618 0.0152  250 SER A C   
1692 O O   . SER A 248 ? 0.2797 0.1581 0.1625 -0.0950 -0.0606 0.0136  250 SER A O   
1693 C CB  . SER A 248 ? 0.3307 0.1860 0.1838 -0.1233 -0.0718 0.0137  250 SER A CB  
1694 O OG  . SER A 248 ? 0.3701 0.1911 0.1984 -0.1272 -0.0733 0.0161  250 SER A OG  
1695 N N   . ILE A 249 ? 0.2909 0.1848 0.1701 -0.1198 -0.0594 0.0178  251 ILE A N   
1696 C CA  . ILE A 249 ? 0.2869 0.1789 0.1688 -0.1107 -0.0553 0.0187  251 ILE A CA  
1697 C C   . ILE A 249 ? 0.3131 0.1723 0.1686 -0.1183 -0.0575 0.0225  251 ILE A C   
1698 O O   . ILE A 249 ? 0.3303 0.1897 0.1758 -0.1362 -0.0585 0.0258  251 ILE A O   
1699 C CB  . ILE A 249 ? 0.2728 0.2027 0.1758 -0.1122 -0.0504 0.0179  251 ILE A CB  
1700 C CG1 . ILE A 249 ? 0.2545 0.2100 0.1793 -0.1014 -0.0496 0.0139  251 ILE A CG1 
1701 C CG2 . ILE A 249 ? 0.2681 0.1959 0.1716 -0.1054 -0.0464 0.0189  251 ILE A CG2 
1702 C CD1 . ILE A 249 ? 0.2428 0.2356 0.1865 -0.1004 -0.0460 0.0118  251 ILE A CD1 
1703 N N   . THR A 250 ? 0.3201 0.1511 0.1626 -0.1050 -0.0590 0.0223  252 THR A N   
1704 C CA  . THR A 250 ? 0.3542 0.1469 0.1669 -0.1084 -0.0630 0.0254  252 THR A CA  
1705 C C   . THR A 250 ? 0.3513 0.1393 0.1636 -0.0949 -0.0607 0.0264  252 THR A C   
1706 O O   . THR A 250 ? 0.3144 0.1261 0.1484 -0.0829 -0.0564 0.0241  252 THR A O   
1707 C CB  . THR A 250 ? 0.3776 0.1359 0.1684 -0.1028 -0.0689 0.0235  252 THR A CB  
1708 O OG1 . THR A 250 ? 0.3627 0.1283 0.1658 -0.0825 -0.0670 0.0195  252 THR A OG1 
1709 C CG2 . THR A 250 ? 0.3890 0.1469 0.1752 -0.1182 -0.0725 0.0228  252 THR A CG2 
1710 N N   . THR A 251 ? 0.3907 0.1464 0.1761 -0.0975 -0.0643 0.0300  253 THR A N   
1711 C CA  . THR A 251 ? 0.4016 0.1506 0.1831 -0.0846 -0.0634 0.0313  253 THR A CA  
1712 C C   . THR A 251 ? 0.4468 0.1509 0.1953 -0.0751 -0.0702 0.0323  253 THR A C   
1713 O O   . THR A 251 ? 0.4695 0.1599 0.2054 -0.0689 -0.0716 0.0350  253 THR A O   
1714 C CB  . THR A 251 ? 0.4026 0.1657 0.1873 -0.0963 -0.0602 0.0354  253 THR A CB  
1715 O OG1 . THR A 251 ? 0.4346 0.1742 0.1941 -0.1161 -0.0642 0.0401  253 THR A OG1 
1716 C CG2 . THR A 251 ? 0.3707 0.1786 0.1870 -0.1003 -0.0535 0.0331  253 THR A CG2 
1717 N N   . ASN A 252 ? 0.4755 0.1577 0.2103 -0.0712 -0.0747 0.0293  254 ASN A N   
1718 C CA  . ASN A 252 ? 0.5295 0.1672 0.2307 -0.0591 -0.0817 0.0288  254 ASN A CA  
1719 C C   . ASN A 252 ? 0.5324 0.1802 0.2428 -0.0323 -0.0802 0.0247  254 ASN A C   
1720 O O   . ASN A 252 ? 0.5792 0.2009 0.2673 -0.0172 -0.0848 0.0247  254 ASN A O   
1721 C CB  . ASN A 252 ? 0.5645 0.1717 0.2430 -0.0662 -0.0877 0.0268  254 ASN A CB  
1722 C CG  . ASN A 252 ? 0.5373 0.1680 0.2368 -0.0592 -0.0848 0.0212  254 ASN A CG  
1723 O OD1 . ASN A 252 ? 0.5115 0.1774 0.2382 -0.0695 -0.0801 0.0210  254 ASN A OD1 
1724 N ND2 . ASN A 252 ? 0.5595 0.1708 0.2450 -0.0411 -0.0881 0.0164  254 ASN A ND2 
1725 N N   . ASN A 253 ? 0.5073 0.1937 0.2493 -0.0266 -0.0743 0.0213  255 ASN A N   
1726 C CA  . ASN A 253 ? 0.5011 0.2039 0.2541 -0.0048 -0.0723 0.0176  255 ASN A CA  
1727 C C   . ASN A 253 ? 0.4449 0.1921 0.2330 -0.0066 -0.0652 0.0175  255 ASN A C   
1728 O O   . ASN A 253 ? 0.4212 0.1894 0.2275 -0.0079 -0.0621 0.0151  255 ASN A O   
1729 C CB  . ASN A 253 ? 0.5233 0.2168 0.2686 0.0048  -0.0744 0.0125  255 ASN A CB  
1730 C CG  . ASN A 253 ? 0.5235 0.2379 0.2791 0.0264  -0.0720 0.0087  255 ASN A CG  
1731 O OD1 . ASN A 253 ? 0.5374 0.2785 0.3129 0.0279  -0.0680 0.0062  255 ASN A OD1 
1732 N ND2 . ASN A 253 ? 0.5509 0.2545 0.2922 0.0428  -0.0748 0.0084  255 ASN A ND2 
1733 N N   . GLY A 254 ? 0.4183 0.1764 0.2129 -0.0073 -0.0632 0.0204  256 GLY A N   
1734 C CA  . GLY A 254 ? 0.3772 0.1703 0.2000 -0.0133 -0.0574 0.0206  256 GLY A CA  
1735 C C   . GLY A 254 ? 0.3590 0.1599 0.1907 -0.0312 -0.0555 0.0215  256 GLY A C   
1736 O O   . GLY A 254 ? 0.3964 0.1774 0.2128 -0.0411 -0.0586 0.0225  256 GLY A O   
1737 N N   . LEU A 255 ? 0.3101 0.1403 0.1652 -0.0351 -0.0508 0.0207  257 LEU A N   
1738 C CA  . LEU A 255 ? 0.2914 0.1359 0.1581 -0.0478 -0.0489 0.0204  257 LEU A CA  
1739 C C   . LEU A 255 ? 0.2654 0.1165 0.1411 -0.0441 -0.0492 0.0173  257 LEU A C   
1740 O O   . LEU A 255 ? 0.2375 0.1031 0.1265 -0.0356 -0.0473 0.0155  257 LEU A O   
1741 C CB  . LEU A 255 ? 0.2775 0.1478 0.1623 -0.0498 -0.0444 0.0200  257 LEU A CB  
1742 C CG  . LEU A 255 ? 0.2816 0.1739 0.1822 -0.0576 -0.0421 0.0182  257 LEU A CG  
1743 C CD1 . LEU A 255 ? 0.3161 0.2041 0.2073 -0.0725 -0.0435 0.0202  257 LEU A CD1 
1744 C CD2 . LEU A 255 ? 0.2771 0.1904 0.1911 -0.0564 -0.0381 0.0169  257 LEU A CD2 
1745 N N   . THR A 256 ? 0.2755 0.1141 0.1414 -0.0514 -0.0523 0.0172  258 THR A N   
1746 C CA  . THR A 256 ? 0.2658 0.1086 0.1375 -0.0478 -0.0533 0.0145  258 THR A CA  
1747 C C   . THR A 256 ? 0.2568 0.1173 0.1406 -0.0591 -0.0530 0.0140  258 THR A C   
1748 O O   . THR A 256 ? 0.2726 0.1309 0.1499 -0.0722 -0.0543 0.0157  258 THR A O   
1749 C CB  . THR A 256 ? 0.2939 0.1080 0.1431 -0.0439 -0.0578 0.0134  258 THR A CB  
1750 O OG1 . THR A 256 ? 0.3062 0.1071 0.1442 -0.0314 -0.0583 0.0136  258 THR A OG1 
1751 C CG2 . THR A 256 ? 0.2874 0.1065 0.1413 -0.0380 -0.0583 0.0104  258 THR A CG2 
1752 N N   . VAL A 257 ? 0.2362 0.1150 0.1364 -0.0539 -0.0517 0.0120  259 VAL A N   
1753 C CA  . VAL A 257 ? 0.2306 0.1287 0.1432 -0.0605 -0.0521 0.0111  259 VAL A CA  
1754 C C   . VAL A 257 ? 0.2309 0.1253 0.1423 -0.0570 -0.0549 0.0095  259 VAL A C   
1755 O O   . VAL A 257 ? 0.2215 0.1190 0.1387 -0.0473 -0.0539 0.0087  259 VAL A O   
1756 C CB  . VAL A 257 ? 0.2137 0.1355 0.1448 -0.0560 -0.0487 0.0101  259 VAL A CB  
1757 C CG1 . VAL A 257 ? 0.2060 0.1492 0.1498 -0.0582 -0.0498 0.0083  259 VAL A CG1 
1758 C CG2 . VAL A 257 ? 0.2172 0.1429 0.1480 -0.0594 -0.0458 0.0113  259 VAL A CG2 
1759 N N   . SER A 258 ? 0.2493 0.1371 0.1518 -0.0662 -0.0587 0.0093  260 SER A N   
1760 C CA  . SER A 258 ? 0.2625 0.1405 0.1578 -0.0633 -0.0619 0.0076  260 SER A CA  
1761 C C   . SER A 258 ? 0.2520 0.1453 0.1537 -0.0720 -0.0651 0.0070  260 SER A C   
1762 O O   . SER A 258 ? 0.2536 0.1580 0.1575 -0.0841 -0.0660 0.0079  260 SER A O   
1763 C CB  . SER A 258 ? 0.3038 0.1504 0.1744 -0.0643 -0.0650 0.0072  260 SER A CB  
1764 O OG  . SER A 258 ? 0.3423 0.1769 0.2065 -0.0533 -0.0627 0.0073  260 SER A OG  
1765 N N   . ILE A 259 ? 0.2467 0.1413 0.1500 -0.0664 -0.0670 0.0056  261 ILE A N   
1766 C CA  . ILE A 259 ? 0.2527 0.1551 0.1558 -0.0742 -0.0716 0.0047  261 ILE A CA  
1767 C C   . ILE A 259 ? 0.2650 0.1481 0.1537 -0.0694 -0.0742 0.0031  261 ILE A C   
1768 O O   . ILE A 259 ? 0.2645 0.1441 0.1542 -0.0577 -0.0718 0.0028  261 ILE A O   
1769 C CB  . ILE A 259 ? 0.2345 0.1671 0.1584 -0.0707 -0.0717 0.0047  261 ILE A CB  
1770 C CG1 . ILE A 259 ? 0.2381 0.1848 0.1635 -0.0789 -0.0770 0.0039  261 ILE A CG1 
1771 C CG2 . ILE A 259 ? 0.2257 0.1583 0.1558 -0.0567 -0.0700 0.0048  261 ILE A CG2 
1772 C CD1 . ILE A 259 ? 0.2240 0.2030 0.1687 -0.0748 -0.0778 0.0034  261 ILE A CD1 
1773 N N   . ALA A 260 ? 0.2833 0.1543 0.1573 -0.0794 -0.0791 0.0019  262 ALA A N   
1774 C CA  . ALA A 260 ? 0.3011 0.1518 0.1581 -0.0751 -0.0819 -0.0004 262 ALA A CA  
1775 C C   . ALA A 260 ? 0.2863 0.1532 0.1547 -0.0667 -0.0818 -0.0006 262 ALA A C   
1776 O O   . ALA A 260 ? 0.2895 0.1467 0.1505 -0.0568 -0.0804 -0.0018 262 ALA A O   
1777 C CB  . ALA A 260 ? 0.3279 0.1634 0.1666 -0.0897 -0.0881 -0.0018 262 ALA A CB  
1778 N N   . ASP A 261 ? 0.2705 0.1628 0.1557 -0.0702 -0.0835 0.0006  263 ASP A N   
1779 C CA  . ASP A 261 ? 0.2621 0.1668 0.1549 -0.0633 -0.0851 0.0010  263 ASP A CA  
1780 C C   . ASP A 261 ? 0.2428 0.1733 0.1563 -0.0601 -0.0846 0.0027  263 ASP A C   
1781 O O   . ASP A 261 ? 0.2399 0.1892 0.1617 -0.0671 -0.0873 0.0024  263 ASP A O   
1782 C CB  . ASP A 261 ? 0.2802 0.1835 0.1633 -0.0706 -0.0914 -0.0005 263 ASP A CB  
1783 C CG  . ASP A 261 ? 0.2798 0.1928 0.1673 -0.0631 -0.0938 0.0003  263 ASP A CG  
1784 O OD1 . ASP A 261 ? 0.2647 0.1804 0.1592 -0.0529 -0.0903 0.0023  263 ASP A OD1 
1785 O OD2 . ASP A 261 ? 0.3035 0.2188 0.1845 -0.0687 -0.0995 -0.0008 263 ASP A OD2 
1786 N N   . LEU A 262 ? 0.2293 0.1607 0.1496 -0.0494 -0.0812 0.0042  264 LEU A N   
1787 C CA  . LEU A 262 ? 0.2115 0.1604 0.1471 -0.0435 -0.0809 0.0052  264 LEU A CA  
1788 C C   . LEU A 262 ? 0.2161 0.1782 0.1560 -0.0402 -0.0867 0.0055  264 LEU A C   
1789 O O   . LEU A 262 ? 0.2074 0.1866 0.1588 -0.0349 -0.0883 0.0053  264 LEU A O   
1790 C CB  . LEU A 262 ? 0.2017 0.1415 0.1378 -0.0353 -0.0766 0.0068  264 LEU A CB  
1791 C CG  . LEU A 262 ? 0.1911 0.1413 0.1387 -0.0288 -0.0759 0.0072  264 LEU A CG  
1792 C CD1 . LEU A 262 ? 0.1852 0.1478 0.1414 -0.0324 -0.0735 0.0055  264 LEU A CD1 
1793 C CD2 . LEU A 262 ? 0.1885 0.1269 0.1330 -0.0237 -0.0728 0.0091  264 LEU A CD2 
1794 N N   . LYS A 263 ? 0.2287 0.1833 0.1582 -0.0424 -0.0903 0.0056  265 LYS A N   
1795 C CA  . LYS A 263 ? 0.2381 0.2042 0.1695 -0.0394 -0.0968 0.0061  265 LYS A CA  
1796 C C   . LYS A 263 ? 0.2352 0.2260 0.1759 -0.0458 -0.1010 0.0043  265 LYS A C   
1797 O O   . LYS A 263 ? 0.2337 0.2415 0.1803 -0.0408 -0.1065 0.0044  265 LYS A O   
1798 C CB  . LYS A 263 ? 0.2579 0.2095 0.1742 -0.0410 -0.0992 0.0066  265 LYS A CB  
1799 C CG  . LYS A 263 ? 0.2660 0.2014 0.1744 -0.0345 -0.0955 0.0090  265 LYS A CG  
1800 C CD  . LYS A 263 ? 0.2708 0.2084 0.1817 -0.0263 -0.0985 0.0124  265 LYS A CD  
1801 C CE  . LYS A 263 ? 0.2814 0.2044 0.1828 -0.0239 -0.0950 0.0155  265 LYS A CE  
1802 N NZ  . LYS A 263 ? 0.2963 0.2154 0.1925 -0.0188 -0.1001 0.0196  265 LYS A NZ  
1803 N N   . THR A 264 ? 0.2332 0.2273 0.1745 -0.0569 -0.0987 0.0028  266 THR A N   
1804 C CA  . THR A 264 ? 0.2355 0.2574 0.1858 -0.0660 -0.1020 0.0015  266 THR A CA  
1805 C C   . THR A 264 ? 0.2269 0.2758 0.1953 -0.0571 -0.1006 0.0010  266 THR A C   
1806 O O   . THR A 264 ? 0.2320 0.3129 0.2114 -0.0611 -0.1033 -0.0003 266 THR A O   
1807 C CB  . THR A 264 ? 0.2419 0.2550 0.1831 -0.0830 -0.1002 0.0009  266 THR A CB  
1808 O OG1 . THR A 264 ? 0.2301 0.2334 0.1730 -0.0806 -0.0936 0.0015  266 THR A OG1 
1809 C CG2 . THR A 264 ? 0.2599 0.2435 0.1798 -0.0901 -0.1025 0.0003  266 THR A CG2 
1810 N N   . LEU A 265 ? 0.2225 0.2600 0.1934 -0.0452 -0.0963 0.0016  267 LEU A N   
1811 C CA  . LEU A 265 ? 0.2133 0.2704 0.1974 -0.0328 -0.0960 0.0004  267 LEU A CA  
1812 C C   . LEU A 265 ? 0.2129 0.2650 0.1946 -0.0181 -0.1015 0.0013  267 LEU A C   
1813 O O   . LEU A 265 ? 0.2134 0.2397 0.1864 -0.0118 -0.1003 0.0033  267 LEU A O   
1814 C CB  . LEU A 265 ? 0.2111 0.2555 0.1960 -0.0296 -0.0892 0.0004  267 LEU A CB  
1815 C CG  . LEU A 265 ? 0.2136 0.2564 0.1968 -0.0437 -0.0841 0.0004  267 LEU A CG  
1816 C CD1 . LEU A 265 ? 0.2107 0.2491 0.1974 -0.0391 -0.0782 0.0001  267 LEU A CD1 
1817 C CD2 . LEU A 265 ? 0.2170 0.2899 0.2072 -0.0557 -0.0860 -0.0007 267 LEU A CD2 
1818 N N   . PRO A 266 ? 0.2127 0.2893 0.2007 -0.0129 -0.1082 0.0001  268 PRO A N   
1819 C CA  . PRO A 266 ? 0.2211 0.2883 0.2023 -0.0003 -0.1149 0.0018  268 PRO A CA  
1820 C C   . PRO A 266 ? 0.2253 0.2791 0.2040 0.0172  -0.1158 0.0021  268 PRO A C   
1821 O O   . PRO A 266 ? 0.2356 0.2672 0.2020 0.0246  -0.1202 0.0050  268 PRO A O   
1822 C CB  . PRO A 266 ? 0.2253 0.3278 0.2154 0.0008  -0.1220 0.0000  268 PRO A CB  
1823 C CG  . PRO A 266 ? 0.2172 0.3536 0.2228 -0.0050 -0.1182 -0.0034 268 PRO A CG  
1824 C CD  . PRO A 266 ? 0.2096 0.3253 0.2103 -0.0196 -0.1100 -0.0024 268 PRO A CD  
1825 N N   . ASN A 267 ? 0.2189 0.2837 0.2066 0.0232  -0.1120 -0.0008 269 ASN A N   
1826 C CA  . ASN A 267 ? 0.2308 0.2796 0.2131 0.0398  -0.1136 -0.0014 269 ASN A CA  
1827 C C   . ASN A 267 ? 0.2259 0.2402 0.1975 0.0347  -0.1081 0.0013  269 ASN A C   
1828 O O   . ASN A 267 ? 0.2371 0.2330 0.2012 0.0449  -0.1092 0.0012  269 ASN A O   
1829 C CB  . ASN A 267 ? 0.2318 0.3081 0.2264 0.0514  -0.1128 -0.0067 269 ASN A CB  
1830 C CG  . ASN A 267 ? 0.2410 0.3551 0.2457 0.0604  -0.1195 -0.0096 269 ASN A CG  
1831 O OD1 . ASN A 267 ? 0.2403 0.3930 0.2602 0.0553  -0.1168 -0.0128 269 ASN A OD1 
1832 N ND2 . ASN A 267 ? 0.2540 0.3593 0.2498 0.0728  -0.1283 -0.0082 269 ASN A ND2 
1833 N N   . VAL A 268 ? 0.2171 0.2229 0.1869 0.0193  -0.1026 0.0034  270 VAL A N   
1834 C CA  . VAL A 268 ? 0.2165 0.1948 0.1768 0.0144  -0.0979 0.0061  270 VAL A CA  
1835 C C   . VAL A 268 ? 0.2314 0.1877 0.1769 0.0142  -0.1018 0.0105  270 VAL A C   
1836 O O   . VAL A 268 ? 0.2297 0.1903 0.1727 0.0097  -0.1045 0.0116  270 VAL A O   
1837 C CB  . VAL A 268 ? 0.2059 0.1860 0.1695 0.0009  -0.0908 0.0059  270 VAL A CB  
1838 C CG1 . VAL A 268 ? 0.2060 0.1624 0.1600 -0.0030 -0.0864 0.0087  270 VAL A CG1 
1839 C CG2 . VAL A 268 ? 0.1956 0.1954 0.1713 -0.0002 -0.0868 0.0025  270 VAL A CG2 
1840 N N   . ASN A 269 ? 0.2435 0.1761 0.1777 0.0175  -0.1020 0.0132  271 ASN A N   
1841 C CA  . ASN A 269 ? 0.2664 0.1774 0.1844 0.0158  -0.1054 0.0183  271 ASN A CA  
1842 C C   . ASN A 269 ? 0.2686 0.1597 0.1776 0.0098  -0.1010 0.0211  271 ASN A C   
1843 O O   . ASN A 269 ? 0.2505 0.1447 0.1665 0.0081  -0.0957 0.0189  271 ASN A O   
1844 C CB  . ASN A 269 ? 0.2977 0.2009 0.2067 0.0282  -0.1150 0.0194  271 ASN A CB  
1845 C CG  . ASN A 269 ? 0.3199 0.2147 0.2270 0.0402  -0.1174 0.0170  271 ASN A CG  
1846 O OD1 . ASN A 269 ? 0.3355 0.2065 0.2310 0.0383  -0.1165 0.0190  271 ASN A OD1 
1847 N ND2 . ASN A 269 ? 0.3309 0.2472 0.2491 0.0522  -0.1204 0.0121  271 ASN A ND2 
1848 N N   . GLU A 270 ? 0.2872 0.1603 0.1804 0.0052  -0.1032 0.0264  272 GLU A N   
1849 C CA  . GLU A 270 ? 0.3025 0.1614 0.1862 -0.0037 -0.0992 0.0300  272 GLU A CA  
1850 C C   . GLU A 270 ? 0.3088 0.1549 0.1898 -0.0005 -0.0997 0.0291  272 GLU A C   
1851 O O   . GLU A 270 ? 0.3065 0.1504 0.1871 -0.0085 -0.0945 0.0299  272 GLU A O   
1852 C CB  . GLU A 270 ? 0.3367 0.1788 0.2012 -0.0097 -0.1028 0.0365  272 GLU A CB  
1853 C CG  . GLU A 270 ? 0.3750 0.1978 0.2247 -0.0013 -0.1130 0.0392  272 GLU A CG  
1854 C CD  . GLU A 270 ? 0.3917 0.2250 0.2437 0.0051  -0.1181 0.0386  272 GLU A CD  
1855 O OE1 . GLU A 270 ? 0.3824 0.2386 0.2492 0.0037  -0.1142 0.0348  272 GLU A OE1 
1856 O OE2 . GLU A 270 ? 0.4610 0.2777 0.2974 0.0108  -0.1267 0.0421  272 GLU A OE2 
1857 N N   . ASN A 271 ? 0.3241 0.1637 0.2032 0.0119  -0.1059 0.0266  273 ASN A N   
1858 C CA  . ASN A 271 ? 0.3442 0.1672 0.2165 0.0168  -0.1076 0.0249  273 ASN A CA  
1859 C C   . ASN A 271 ? 0.3143 0.1575 0.2046 0.0234  -0.1032 0.0181  273 ASN A C   
1860 O O   . ASN A 271 ? 0.3138 0.1461 0.1997 0.0291  -0.1042 0.0153  273 ASN A O   
1861 C CB  . ASN A 271 ? 0.3976 0.1946 0.2505 0.0280  -0.1181 0.0264  273 ASN A CB  
1862 C CG  . ASN A 271 ? 0.4463 0.2171 0.2764 0.0174  -0.1221 0.0343  273 ASN A CG  
1863 O OD1 . ASN A 271 ? 0.4950 0.2585 0.3151 0.0210  -0.1284 0.0376  273 ASN A OD1 
1864 N ND2 . ASN A 271 ? 0.4722 0.2305 0.2934 0.0032  -0.1185 0.0378  273 ASN A ND2 
1865 N N   . SER A 272 ? 0.2833 0.1541 0.1916 0.0212  -0.0984 0.0157  274 SER A N   
1866 C CA  . SER A 272 ? 0.2700 0.1623 0.1945 0.0243  -0.0937 0.0102  274 SER A CA  
1867 C C   . SER A 272 ? 0.2614 0.1514 0.1883 0.0149  -0.0865 0.0105  274 SER A C   
1868 O O   . SER A 272 ? 0.2663 0.1497 0.1883 0.0048  -0.0837 0.0143  274 SER A O   
1869 C CB  . SER A 272 ? 0.2507 0.1703 0.1899 0.0222  -0.0919 0.0083  274 SER A CB  
1870 O OG  . SER A 272 ? 0.2576 0.1844 0.1963 0.0307  -0.0988 0.0079  274 SER A OG  
1871 N N   . LYS A 273 ? 0.2592 0.1575 0.1934 0.0190  -0.0837 0.0061  275 LYS A N   
1872 C CA  . LYS A 273 ? 0.2505 0.1526 0.1896 0.0110  -0.0769 0.0057  275 LYS A CA  
1873 C C   . LYS A 273 ? 0.2230 0.1504 0.1773 0.0101  -0.0725 0.0026  275 LYS A C   
1874 O O   . LYS A 273 ? 0.2188 0.1617 0.1802 0.0176  -0.0740 -0.0011 275 LYS A O   
1875 C CB  . LYS A 273 ? 0.2786 0.1657 0.2098 0.0142  -0.0775 0.0039  275 LYS A CB  
1876 C CG  . LYS A 273 ? 0.3196 0.1790 0.2325 0.0098  -0.0816 0.0081  275 LYS A CG  
1877 C CD  . LYS A 273 ? 0.3579 0.2005 0.2608 0.0114  -0.0828 0.0058  275 LYS A CD  
1878 C CE  . LYS A 273 ? 0.4104 0.2260 0.2940 0.0017  -0.0863 0.0106  275 LYS A CE  
1879 N NZ  . LYS A 273 ? 0.4524 0.2596 0.3307 -0.0022 -0.0848 0.0084  275 LYS A NZ  
1880 N N   . ILE A 274 ? 0.2072 0.1389 0.1649 0.0005  -0.0674 0.0042  276 ILE A N   
1881 C CA  . ILE A 274 ? 0.1931 0.1423 0.1605 -0.0032 -0.0633 0.0022  276 ILE A CA  
1882 C C   . ILE A 274 ? 0.1858 0.1334 0.1537 -0.0047 -0.0590 0.0011  276 ILE A C   
1883 O O   . ILE A 274 ? 0.1924 0.1289 0.1550 -0.0088 -0.0571 0.0034  276 ILE A O   
1884 C CB  . ILE A 274 ? 0.1882 0.1384 0.1548 -0.0115 -0.0619 0.0044  276 ILE A CB  
1885 C CG1 . ILE A 274 ? 0.1919 0.1423 0.1562 -0.0106 -0.0666 0.0055  276 ILE A CG1 
1886 C CG2 . ILE A 274 ? 0.1838 0.1470 0.1560 -0.0175 -0.0588 0.0031  276 ILE A CG2 
1887 C CD1 . ILE A 274 ? 0.1927 0.1601 0.1642 -0.0052 -0.0704 0.0029  276 ILE A CD1 
1888 N N   . VAL A 275 ? 0.1765 0.1383 0.1509 -0.0014 -0.0574 -0.0023 277 VAL A N   
1889 C CA  . VAL A 275 ? 0.1741 0.1354 0.1482 -0.0019 -0.0537 -0.0039 277 VAL A CA  
1890 C C   . VAL A 275 ? 0.1637 0.1421 0.1442 -0.0083 -0.0494 -0.0044 277 VAL A C   
1891 O O   . VAL A 275 ? 0.1599 0.1580 0.1475 -0.0077 -0.0494 -0.0065 277 VAL A O   
1892 C CB  . VAL A 275 ? 0.1854 0.1449 0.1572 0.0089  -0.0559 -0.0083 277 VAL A CB  
1893 C CG1 . VAL A 275 ? 0.1861 0.1429 0.1554 0.0084  -0.0525 -0.0104 277 VAL A CG1 
1894 C CG2 . VAL A 275 ? 0.1987 0.1366 0.1599 0.0141  -0.0617 -0.0071 277 VAL A CG2 
1895 N N   . ILE A 276 ? 0.1630 0.1342 0.1400 -0.0148 -0.0461 -0.0021 278 ILE A N   
1896 C CA  . ILE A 276 ? 0.1585 0.1392 0.1368 -0.0220 -0.0425 -0.0016 278 ILE A CA  
1897 C C   . ILE A 276 ? 0.1562 0.1397 0.1340 -0.0200 -0.0395 -0.0036 278 ILE A C   
1898 O O   . ILE A 276 ? 0.1584 0.1292 0.1314 -0.0182 -0.0395 -0.0031 278 ILE A O   
1899 C CB  . ILE A 276 ? 0.1597 0.1272 0.1308 -0.0289 -0.0421 0.0023  278 ILE A CB  
1900 C CG1 . ILE A 276 ? 0.1645 0.1281 0.1340 -0.0306 -0.0451 0.0035  278 ILE A CG1 
1901 C CG2 . ILE A 276 ? 0.1626 0.1331 0.1302 -0.0366 -0.0393 0.0036  278 ILE A CG2 
1902 C CD1 . ILE A 276 ? 0.1719 0.1192 0.1321 -0.0326 -0.0454 0.0061  278 ILE A CD1 
1903 N N   . ARG A 277 ? 0.1548 0.1569 0.1371 -0.0215 -0.0369 -0.0058 279 ARG A N   
1904 C CA  . ARG A 277 ? 0.1614 0.1679 0.1422 -0.0204 -0.0337 -0.0079 279 ARG A CA  
1905 C C   . ARG A 277 ? 0.1572 0.1731 0.1362 -0.0313 -0.0302 -0.0053 279 ARG A C   
1906 O O   . ARG A 277 ? 0.1540 0.1818 0.1354 -0.0386 -0.0301 -0.0039 279 ARG A O   
1907 C CB  . ARG A 277 ? 0.1668 0.1884 0.1521 -0.0100 -0.0336 -0.0141 279 ARG A CB  
1908 C CG  . ARG A 277 ? 0.1806 0.1862 0.1624 0.0009  -0.0382 -0.0165 279 ARG A CG  
1909 C CD  . ARG A 277 ? 0.1962 0.2091 0.1772 0.0141  -0.0389 -0.0235 279 ARG A CD  
1910 N NE  . ARG A 277 ? 0.2164 0.2074 0.1896 0.0235  -0.0448 -0.0249 279 ARG A NE  
1911 C CZ  . ARG A 277 ? 0.2261 0.2198 0.2006 0.0332  -0.0492 -0.0268 279 ARG A CZ  
1912 N NH1 . ARG A 277 ? 0.2255 0.2481 0.2110 0.0360  -0.0482 -0.0286 279 ARG A NH1 
1913 N NH2 . ARG A 277 ? 0.2411 0.2091 0.2046 0.0397  -0.0551 -0.0267 279 ARG A NH2 
1914 N N   . TYR A 278 ? 0.1581 0.1671 0.1310 -0.0334 -0.0280 -0.0042 280 TYR A N   
1915 C CA  . TYR A 278 ? 0.1634 0.1791 0.1315 -0.0432 -0.0249 -0.0016 280 TYR A CA  
1916 C C   . TYR A 278 ? 0.1637 0.1773 0.1275 -0.0403 -0.0226 -0.0030 280 TYR A C   
1917 O O   . TYR A 278 ? 0.1621 0.1660 0.1256 -0.0324 -0.0241 -0.0054 280 TYR A O   
1918 C CB  . TYR A 278 ? 0.1741 0.1718 0.1329 -0.0518 -0.0268 0.0041  280 TYR A CB  
1919 C CG  . TYR A 278 ? 0.1788 0.1546 0.1305 -0.0474 -0.0286 0.0063  280 TYR A CG  
1920 C CD1 . TYR A 278 ? 0.1907 0.1605 0.1349 -0.0481 -0.0274 0.0079  280 TYR A CD1 
1921 C CD2 . TYR A 278 ? 0.1829 0.1475 0.1355 -0.0424 -0.0314 0.0066  280 TYR A CD2 
1922 C CE1 . TYR A 278 ? 0.1965 0.1520 0.1355 -0.0433 -0.0293 0.0097  280 TYR A CE1 
1923 C CE2 . TYR A 278 ? 0.1884 0.1396 0.1356 -0.0383 -0.0327 0.0083  280 TYR A CE2 
1924 C CZ  . TYR A 278 ? 0.1977 0.1454 0.1386 -0.0385 -0.0318 0.0098  280 TYR A CZ  
1925 O OH  . TYR A 278 ? 0.2088 0.1487 0.1456 -0.0336 -0.0333 0.0112  280 TYR A OH  
1926 N N   . THR A 279 ? 0.1697 0.1920 0.1286 -0.0481 -0.0194 -0.0014 281 THR A N   
1927 C CA  . THR A 279 ? 0.1752 0.1960 0.1285 -0.0462 -0.0174 -0.0025 281 THR A CA  
1928 C C   . THR A 279 ? 0.1857 0.1934 0.1266 -0.0554 -0.0175 0.0038  281 THR A C   
1929 O O   . THR A 279 ? 0.1954 0.1982 0.1306 -0.0647 -0.0183 0.0084  281 THR A O   
1930 C CB  . THR A 279 ? 0.1759 0.2219 0.1331 -0.0443 -0.0133 -0.0076 281 THR A CB  
1931 O OG1 . THR A 279 ? 0.1849 0.2467 0.1400 -0.0569 -0.0104 -0.0041 281 THR A OG1 
1932 C CG2 . THR A 279 ? 0.1740 0.2326 0.1411 -0.0327 -0.0140 -0.0144 281 THR A CG2 
1933 N N   . ALA A 280 ? 0.1896 0.1890 0.1243 -0.0524 -0.0177 0.0040  282 ALA A N   
1934 C CA  . ALA A 280 ? 0.2034 0.1904 0.1246 -0.0586 -0.0184 0.0097  282 ALA A CA  
1935 C C   . ALA A 280 ? 0.2089 0.2039 0.1260 -0.0579 -0.0160 0.0077  282 ALA A C   
1936 O O   . ALA A 280 ? 0.2006 0.2076 0.1245 -0.0518 -0.0141 0.0015  282 ALA A O   
1937 C CB  . ALA A 280 ? 0.2013 0.1678 0.1181 -0.0535 -0.0228 0.0127  282 ALA A CB  
1938 N N   . ARG A 281 ? 0.2315 0.2175 0.1351 -0.0635 -0.0165 0.0129  283 ARG A N   
1939 C CA  . ARG A 281 ? 0.2493 0.2406 0.1467 -0.0631 -0.0149 0.0118  283 ARG A CA  
1940 C C   . ARG A 281 ? 0.2538 0.2265 0.1386 -0.0619 -0.0192 0.0171  283 ARG A C   
1941 O O   . ARG A 281 ? 0.2578 0.2138 0.1341 -0.0638 -0.0224 0.0226  283 ARG A O   
1942 C CB  . ARG A 281 ? 0.2813 0.2892 0.1735 -0.0730 -0.0101 0.0125  283 ARG A CB  
1943 C CG  . ARG A 281 ? 0.3219 0.3212 0.2020 -0.0863 -0.0107 0.0202  283 ARG A CG  
1944 C CD  . ARG A 281 ? 0.3576 0.3785 0.2327 -0.0980 -0.0054 0.0210  283 ARG A CD  
1945 N NE  . ARG A 281 ? 0.4134 0.4194 0.2692 -0.1134 -0.0070 0.0300  283 ARG A NE  
1946 C CZ  . ARG A 281 ? 0.4571 0.4548 0.3087 -0.1236 -0.0089 0.0342  283 ARG A CZ  
1947 N NH1 . ARG A 281 ? 0.4599 0.4668 0.3274 -0.1195 -0.0090 0.0301  283 ARG A NH1 
1948 N NH2 . ARG A 281 ? 0.5112 0.4894 0.3404 -0.1386 -0.0115 0.0427  283 ARG A NH2 
1949 N N   . LEU A 282 ? 0.2490 0.2243 0.1320 -0.0573 -0.0198 0.0148  284 LEU A N   
1950 C CA  . LEU A 282 ? 0.2559 0.2188 0.1286 -0.0542 -0.0243 0.0191  284 LEU A CA  
1951 C C   . LEU A 282 ? 0.2762 0.2295 0.1305 -0.0616 -0.0248 0.0259  284 LEU A C   
1952 O O   . LEU A 282 ? 0.2707 0.2334 0.1207 -0.0702 -0.0206 0.0261  284 LEU A O   
1953 C CB  . LEU A 282 ? 0.2558 0.2272 0.1305 -0.0500 -0.0249 0.0146  284 LEU A CB  
1954 C CG  . LEU A 282 ? 0.2435 0.2179 0.1304 -0.0441 -0.0266 0.0095  284 LEU A CG  
1955 C CD1 . LEU A 282 ? 0.2484 0.2292 0.1334 -0.0434 -0.0270 0.0044  284 LEU A CD1 
1956 C CD2 . LEU A 282 ? 0.2427 0.2098 0.1308 -0.0394 -0.0313 0.0132  284 LEU A CD2 
1957 N N   . LYS A 283 ? 0.2964 0.2306 0.1386 -0.0581 -0.0302 0.0317  285 LYS A N   
1958 C CA  . LYS A 283 ? 0.3288 0.2478 0.1489 -0.0630 -0.0327 0.0387  285 LYS A CA  
1959 C C   . LYS A 283 ? 0.3347 0.2607 0.1502 -0.0590 -0.0341 0.0382  285 LYS A C   
1960 O O   . LYS A 283 ? 0.3107 0.2498 0.1390 -0.0522 -0.0344 0.0330  285 LYS A O   
1961 C CB  . LYS A 283 ? 0.3570 0.2496 0.1630 -0.0572 -0.0393 0.0442  285 LYS A CB  
1962 C CG  . LYS A 283 ? 0.3694 0.2509 0.1767 -0.0608 -0.0392 0.0447  285 LYS A CG  
1963 C CD  . LYS A 283 ? 0.3968 0.2516 0.1898 -0.0513 -0.0461 0.0482  285 LYS A CD  
1964 C CE  . LYS A 283 ? 0.4230 0.2597 0.2086 -0.0582 -0.0469 0.0500  285 LYS A CE  
1965 N NZ  . LYS A 283 ? 0.4580 0.2681 0.2291 -0.0455 -0.0539 0.0517  285 LYS A NZ  
1966 N N   . ASP A 284 ? 0.3655 0.2807 0.1605 -0.0643 -0.0358 0.0442  286 ASP A N   
1967 C CA  . ASP A 284 ? 0.3837 0.3034 0.1709 -0.0606 -0.0383 0.0448  286 ASP A CA  
1968 C C   . ASP A 284 ? 0.3806 0.2874 0.1605 -0.0477 -0.0464 0.0482  286 ASP A C   
1969 O O   . ASP A 284 ? 0.4126 0.3204 0.1825 -0.0439 -0.0501 0.0503  286 ASP A O   
1970 C CB  . ASP A 284 ? 0.4200 0.3347 0.1868 -0.0722 -0.0367 0.0502  286 ASP A CB  
1971 C CG  . ASP A 284 ? 0.4689 0.3541 0.2117 -0.0781 -0.0408 0.0595  286 ASP A CG  
1972 O OD1 . ASP A 284 ? 0.4932 0.3608 0.2350 -0.0721 -0.0448 0.0610  286 ASP A OD1 
1973 O OD2 . ASP A 284 ? 0.5369 0.4148 0.2595 -0.0889 -0.0404 0.0653  286 ASP A OD2 
1974 N N   . SER A 285 ? 0.3616 0.2573 0.1449 -0.0404 -0.0493 0.0487  287 SER A N   
1975 C CA  . SER A 285 ? 0.3545 0.2442 0.1346 -0.0254 -0.0563 0.0501  287 SER A CA  
1976 C C   . SER A 285 ? 0.3185 0.2260 0.1223 -0.0186 -0.0550 0.0440  287 SER A C   
1977 O O   . SER A 285 ? 0.3132 0.2196 0.1176 -0.0062 -0.0596 0.0443  287 SER A O   
1978 C CB  . SER A 285 ? 0.3823 0.2397 0.1397 -0.0217 -0.0615 0.0564  287 SER A CB  
1979 O OG  . SER A 285 ? 0.3819 0.2311 0.1451 -0.0266 -0.0587 0.0550  287 SER A OG  
1980 N N   . ALA A 286 ? 0.2907 0.2149 0.1128 -0.0260 -0.0490 0.0383  288 ALA A N   
1981 C CA  . ALA A 286 ? 0.2645 0.2028 0.1061 -0.0216 -0.0481 0.0332  288 ALA A CA  
1982 C C   . ALA A 286 ? 0.2569 0.2118 0.1032 -0.0140 -0.0524 0.0320  288 ALA A C   
1983 O O   . ALA A 286 ? 0.2643 0.2249 0.1034 -0.0144 -0.0545 0.0330  288 ALA A O   
1984 C CB  . ALA A 286 ? 0.2499 0.1992 0.1051 -0.0302 -0.0422 0.0276  288 ALA A CB  
1985 N N   . THR A 287 ? 0.2432 0.2079 0.1009 -0.0076 -0.0538 0.0301  289 THR A N   
1986 C CA  . THR A 287 ? 0.2386 0.2248 0.1023 -0.0020 -0.0577 0.0291  289 THR A CA  
1987 C C   . THR A 287 ? 0.2270 0.2275 0.0981 -0.0124 -0.0559 0.0249  289 THR A C   
1988 O O   . THR A 287 ? 0.2152 0.2137 0.0941 -0.0201 -0.0517 0.0210  289 THR A O   
1989 C CB  . THR A 287 ? 0.2318 0.2290 0.1068 0.0044  -0.0584 0.0277  289 THR A CB  
1990 O OG1 . THR A 287 ? 0.2436 0.2241 0.1090 0.0151  -0.0603 0.0306  289 THR A OG1 
1991 C CG2 . THR A 287 ? 0.2294 0.2551 0.1115 0.0088  -0.0622 0.0270  289 THR A CG2 
1992 N N   . LEU A 288 ? 0.2323 0.2458 0.0989 -0.0116 -0.0598 0.0255  290 LEU A N   
1993 C CA  . LEU A 288 ? 0.2300 0.2551 0.1000 -0.0214 -0.0595 0.0212  290 LEU A CA  
1994 C C   . LEU A 288 ? 0.2250 0.2726 0.1062 -0.0230 -0.0624 0.0194  290 LEU A C   
1995 O O   . LEU A 288 ? 0.2317 0.2932 0.1163 -0.0142 -0.0657 0.0220  290 LEU A O   
1996 C CB  . LEU A 288 ? 0.2434 0.2708 0.1007 -0.0214 -0.0626 0.0230  290 LEU A CB  
1997 C CG  . LEU A 288 ? 0.2567 0.2638 0.0994 -0.0204 -0.0606 0.0267  290 LEU A CG  
1998 C CD1 . LEU A 288 ? 0.2734 0.2835 0.1018 -0.0191 -0.0648 0.0296  290 LEU A CD1 
1999 C CD2 . LEU A 288 ? 0.2519 0.2495 0.0967 -0.0296 -0.0537 0.0227  290 LEU A CD2 
2000 N N   . GLY A 289 ? 0.2217 0.2730 0.1066 -0.0343 -0.0617 0.0147  291 GLY A N   
2001 C CA  . GLY A 289 ? 0.2187 0.2921 0.1102 -0.0405 -0.0655 0.0136  291 GLY A CA  
2002 C C   . GLY A 289 ? 0.2083 0.2865 0.1108 -0.0413 -0.0640 0.0136  291 GLY A C   
2003 O O   . GLY A 289 ? 0.1995 0.2595 0.1043 -0.0411 -0.0598 0.0125  291 GLY A O   
2004 N N   . THR A 290 ? 0.2067 0.3125 0.1157 -0.0428 -0.0676 0.0149  292 THR A N   
2005 C CA  . THR A 290 ? 0.2019 0.3169 0.1196 -0.0497 -0.0667 0.0145  292 THR A CA  
2006 C C   . THR A 290 ? 0.1937 0.3079 0.1179 -0.0376 -0.0639 0.0166  292 THR A C   
2007 O O   . THR A 290 ? 0.1877 0.3011 0.1174 -0.0428 -0.0619 0.0161  292 THR A O   
2008 C CB  . THR A 290 ? 0.2052 0.3552 0.1275 -0.0583 -0.0713 0.0153  292 THR A CB  
2009 O OG1 . THR A 290 ? 0.2081 0.3827 0.1323 -0.0448 -0.0743 0.0179  292 THR A OG1 
2010 C CG2 . THR A 290 ? 0.2173 0.3649 0.1317 -0.0753 -0.0746 0.0126  292 THR A CG2 
2011 N N   . THR A 291 ? 0.1970 0.3087 0.1179 -0.0219 -0.0643 0.0189  293 THR A N   
2012 C CA  . THR A 291 ? 0.1906 0.2966 0.1140 -0.0101 -0.0622 0.0203  293 THR A CA  
2013 C C   . THR A 291 ? 0.1811 0.2577 0.1040 -0.0148 -0.0576 0.0189  293 THR A C   
2014 O O   . THR A 291 ? 0.1697 0.2447 0.0980 -0.0142 -0.0554 0.0186  293 THR A O   
2015 C CB  . THR A 291 ? 0.2058 0.3078 0.1205 0.0076  -0.0649 0.0229  293 THR A CB  
2016 O OG1 . THR A 291 ? 0.2112 0.3471 0.1288 0.0144  -0.0696 0.0237  293 THR A OG1 
2017 C CG2 . THR A 291 ? 0.2068 0.2930 0.1186 0.0197  -0.0634 0.0237  293 THR A CG2 
2018 N N   . GLY A 292 ? 0.1827 0.2382 0.0986 -0.0187 -0.0561 0.0180  294 GLY A N   
2019 C CA  . GLY A 292 ? 0.1783 0.2112 0.0945 -0.0229 -0.0519 0.0161  294 GLY A CA  
2020 C C   . GLY A 292 ? 0.1787 0.1954 0.0911 -0.0140 -0.0503 0.0183  294 GLY A C   
2021 O O   . GLY A 292 ? 0.1839 0.2019 0.0908 -0.0036 -0.0527 0.0211  294 GLY A O   
2022 N N   . ASN A 293 ? 0.1755 0.1757 0.0887 -0.0181 -0.0467 0.0169  295 ASN A N   
2023 C CA  . ASN A 293 ? 0.1812 0.1648 0.0900 -0.0136 -0.0453 0.0187  295 ASN A CA  
2024 C C   . ASN A 293 ? 0.1723 0.1539 0.0896 -0.0151 -0.0433 0.0170  295 ASN A C   
2025 O O   . ASN A 293 ? 0.1625 0.1397 0.0842 -0.0215 -0.0409 0.0144  295 ASN A O   
2026 C CB  . ASN A 293 ? 0.1892 0.1597 0.0910 -0.0184 -0.0429 0.0189  295 ASN A CB  
2027 C CG  . ASN A 293 ? 0.2008 0.1727 0.0925 -0.0178 -0.0449 0.0209  295 ASN A CG  
2028 O OD1 . ASN A 293 ? 0.2157 0.1796 0.0962 -0.0114 -0.0478 0.0249  295 ASN A OD1 
2029 N ND2 . ASN A 293 ? 0.2006 0.1800 0.0936 -0.0238 -0.0439 0.0180  295 ASN A ND2 
2030 N N   . SER A 294 ? 0.1753 0.1605 0.0937 -0.0080 -0.0447 0.0183  296 SER A N   
2031 C CA  . SER A 294 ? 0.1683 0.1554 0.0944 -0.0096 -0.0433 0.0170  296 SER A CA  
2032 C C   . SER A 294 ? 0.1739 0.1440 0.0955 -0.0056 -0.0425 0.0177  296 SER A C   
2033 O O   . SER A 294 ? 0.1818 0.1402 0.0928 0.0007  -0.0441 0.0196  296 SER A O   
2034 C CB  . SER A 294 ? 0.1660 0.1741 0.0972 -0.0065 -0.0448 0.0172  296 SER A CB  
2035 O OG  . SER A 294 ? 0.1686 0.1924 0.1034 -0.0138 -0.0459 0.0167  296 SER A OG  
2036 N N   . ASN A 295 ? 0.1661 0.1334 0.0940 -0.0097 -0.0408 0.0162  297 ASN A N   
2037 C CA  . ASN A 295 ? 0.1719 0.1262 0.0965 -0.0071 -0.0406 0.0164  297 ASN A CA  
2038 C C   . ASN A 295 ? 0.1680 0.1301 0.0999 -0.0074 -0.0401 0.0154  297 ASN A C   
2039 O O   . ASN A 295 ? 0.1633 0.1353 0.1021 -0.0132 -0.0396 0.0146  297 ASN A O   
2040 C CB  . ASN A 295 ? 0.1739 0.1159 0.0976 -0.0137 -0.0389 0.0160  297 ASN A CB  
2041 C CG  . ASN A 295 ? 0.1658 0.1138 0.0995 -0.0198 -0.0372 0.0134  297 ASN A CG  
2042 O OD1 . ASN A 295 ? 0.1632 0.1181 0.1000 -0.0225 -0.0369 0.0120  297 ASN A OD1 
2043 N N   . THR A 296 ? 0.1750 0.1305 0.1024 -0.0017 -0.0406 0.0155  298 THR A N   
2044 C CA  . THR A 296 ? 0.1750 0.1385 0.1073 -0.0014 -0.0401 0.0147  298 THR A CA  
2045 C C   . THR A 296 ? 0.1720 0.1197 0.1017 -0.0029 -0.0400 0.0141  298 THR A C   
2046 O O   . THR A 296 ? 0.1796 0.1114 0.1003 -0.0010 -0.0411 0.0143  298 THR A O   
2047 C CB  . THR A 296 ? 0.1867 0.1645 0.1165 0.0083  -0.0408 0.0147  298 THR A CB  
2048 O OG1 . THR A 296 ? 0.2134 0.1757 0.1306 0.0184  -0.0427 0.0145  298 THR A OG1 
2049 C CG2 . THR A 296 ? 0.1894 0.1899 0.1239 0.0080  -0.0411 0.0154  298 THR A CG2 
2050 N N   . ALA A 297 ? 0.1624 0.1142 0.0983 -0.0073 -0.0394 0.0136  299 ALA A N   
2051 C CA  . ALA A 297 ? 0.1635 0.1040 0.0980 -0.0090 -0.0398 0.0129  299 ALA A CA  
2052 C C   . ALA A 297 ? 0.1639 0.1114 0.0994 -0.0077 -0.0398 0.0129  299 ALA A C   
2053 O O   . ALA A 297 ? 0.1576 0.1186 0.0976 -0.0103 -0.0392 0.0138  299 ALA A O   
2054 C CB  . ALA A 297 ? 0.1566 0.0942 0.0971 -0.0159 -0.0396 0.0123  299 ALA A CB  
2055 N N   . SER A 298 ? 0.1764 0.1144 0.1063 -0.0051 -0.0407 0.0120  300 SER A N   
2056 C CA  . SER A 298 ? 0.1835 0.1270 0.1126 -0.0039 -0.0405 0.0118  300 SER A CA  
2057 C C   . SER A 298 ? 0.1858 0.1157 0.1115 -0.0061 -0.0422 0.0109  300 SER A C   
2058 O O   . SER A 298 ? 0.1912 0.1080 0.1125 -0.0073 -0.0435 0.0102  300 SER A O   
2059 C CB  . SER A 298 ? 0.1992 0.1505 0.1215 0.0060  -0.0399 0.0107  300 SER A CB  
2060 O OG  . SER A 298 ? 0.2265 0.1595 0.1367 0.0131  -0.0418 0.0088  300 SER A OG  
2061 N N   . LEU A 299 ? 0.1843 0.1182 0.1108 -0.0078 -0.0425 0.0112  301 LEU A N   
2062 C CA  . LEU A 299 ? 0.1864 0.1103 0.1099 -0.0100 -0.0447 0.0104  301 LEU A CA  
2063 C C   . LEU A 299 ? 0.1945 0.1160 0.1078 -0.0042 -0.0449 0.0087  301 LEU A C   
2064 O O   . LEU A 299 ? 0.1933 0.1276 0.1060 -0.0011 -0.0430 0.0091  301 LEU A O   
2065 C CB  . LEU A 299 ? 0.1819 0.1098 0.1121 -0.0157 -0.0457 0.0121  301 LEU A CB  
2066 C CG  . LEU A 299 ? 0.1891 0.1110 0.1166 -0.0173 -0.0485 0.0117  301 LEU A CG  
2067 C CD1 . LEU A 299 ? 0.1880 0.1033 0.1169 -0.0198 -0.0505 0.0102  301 LEU A CD1 
2068 C CD2 . LEU A 299 ? 0.1879 0.1124 0.1182 -0.0206 -0.0502 0.0140  301 LEU A CD2 
2069 N N   . THR A 300 ? 0.2036 0.1093 0.1078 -0.0037 -0.0473 0.0067  302 THR A N   
2070 C CA  . THR A 300 ? 0.2124 0.1116 0.1048 0.0009  -0.0485 0.0044  302 THR A CA  
2071 C C   . THR A 300 ? 0.2092 0.1075 0.1039 -0.0058 -0.0507 0.0050  302 THR A C   
2072 O O   . THR A 300 ? 0.2063 0.0991 0.1045 -0.0126 -0.0531 0.0054  302 THR A O   
2073 C CB  . THR A 300 ? 0.2340 0.1121 0.1102 0.0059  -0.0508 0.0015  302 THR A CB  
2074 O OG1 . THR A 300 ? 0.2341 0.1155 0.1083 0.0143  -0.0491 0.0013  302 THR A OG1 
2075 C CG2 . THR A 300 ? 0.2499 0.1170 0.1102 0.0117  -0.0527 -0.0020 302 THR A CG2 
2076 N N   . TYR A 301 ? 0.2060 0.1122 0.0983 -0.0040 -0.0501 0.0051  303 TYR A N   
2077 C CA  . TYR A 301 ? 0.2032 0.1103 0.0975 -0.0097 -0.0525 0.0066  303 TYR A CA  
2078 C C   . TYR A 301 ? 0.2105 0.1159 0.0925 -0.0060 -0.0530 0.0045  303 TYR A C   
2079 O O   . TYR A 301 ? 0.2135 0.1246 0.0887 0.0013  -0.0501 0.0026  303 TYR A O   
2080 C CB  . TYR A 301 ? 0.1928 0.1118 0.0971 -0.0140 -0.0515 0.0107  303 TYR A CB  
2081 C CG  . TYR A 301 ? 0.1888 0.1220 0.0921 -0.0122 -0.0478 0.0122  303 TYR A CG  
2082 C CD1 . TYR A 301 ? 0.1815 0.1231 0.0894 -0.0101 -0.0449 0.0123  303 TYR A CD1 
2083 C CD2 . TYR A 301 ? 0.1912 0.1320 0.0884 -0.0134 -0.0472 0.0137  303 TYR A CD2 
2084 C CE1 . TYR A 301 ? 0.1821 0.1420 0.0900 -0.0096 -0.0416 0.0137  303 TYR A CE1 
2085 C CE2 . TYR A 301 ? 0.1923 0.1512 0.0887 -0.0136 -0.0434 0.0152  303 TYR A CE2 
2086 C CZ  . TYR A 301 ? 0.1884 0.1582 0.0909 -0.0119 -0.0407 0.0152  303 TYR A CZ  
2087 O OH  . TYR A 301 ? 0.1907 0.1834 0.0937 -0.0134 -0.0372 0.0169  303 TYR A OH  
2088 N N   . SER A 302 ? 0.2129 0.1127 0.0921 -0.0106 -0.0567 0.0046  304 SER A N   
2089 C CA  . SER A 302 ? 0.2206 0.1203 0.0886 -0.0085 -0.0575 0.0032  304 SER A CA  
2090 C C   . SER A 302 ? 0.2135 0.1298 0.0841 -0.0087 -0.0541 0.0067  304 SER A C   
2091 O O   . SER A 302 ? 0.2054 0.1260 0.0843 -0.0148 -0.0552 0.0111  304 SER A O   
2092 C CB  . SER A 302 ? 0.2239 0.1171 0.0901 -0.0145 -0.0627 0.0035  304 SER A CB  
2093 O OG  . SER A 302 ? 0.2329 0.1125 0.0942 -0.0172 -0.0661 0.0004  304 SER A OG  
2094 N N   . ASN A 303 ? 0.2207 0.1458 0.0824 -0.0024 -0.0507 0.0045  305 ASN A N   
2095 C CA  . ASN A 303 ? 0.2169 0.1628 0.0809 -0.0044 -0.0467 0.0081  305 ASN A CA  
2096 C C   . ASN A 303 ? 0.2292 0.1811 0.0825 -0.0061 -0.0467 0.0088  305 ASN A C   
2097 O O   . ASN A 303 ? 0.2272 0.1988 0.0792 -0.0086 -0.0429 0.0116  305 ASN A O   
2098 C CB  . ASN A 303 ? 0.2149 0.1763 0.0796 0.0037  -0.0418 0.0057  305 ASN A CB  
2099 C CG  . ASN A 303 ? 0.2298 0.1915 0.0805 0.0165  -0.0404 -0.0007 305 ASN A CG  
2100 O OD1 . ASN A 303 ? 0.2420 0.1849 0.0814 0.0190  -0.0438 -0.0043 305 ASN A OD1 
2101 N ND2 . ASN A 303 ? 0.2314 0.2153 0.0817 0.0250  -0.0358 -0.0025 305 ASN A ND2 
2102 N N   . ASN A 304 ? 0.2419 0.1788 0.0865 -0.0058 -0.0509 0.0064  306 ASN A N   
2103 C CA  . ASN A 304 ? 0.2569 0.1981 0.0900 -0.0073 -0.0513 0.0069  306 ASN A CA  
2104 C C   . ASN A 304 ? 0.2666 0.1919 0.0974 -0.0129 -0.0581 0.0082  306 ASN A C   
2105 O O   . ASN A 304 ? 0.2742 0.1851 0.1002 -0.0106 -0.0617 0.0036  306 ASN A O   
2106 C CB  . ASN A 304 ? 0.2729 0.2172 0.0916 0.0035  -0.0485 0.0000  306 ASN A CB  
2107 C CG  . ASN A 304 ? 0.2842 0.2377 0.0905 0.0020  -0.0478 0.0005  306 ASN A CG  
2108 O OD1 . ASN A 304 ? 0.2839 0.2375 0.0907 -0.0078 -0.0504 0.0064  306 ASN A OD1 
2109 N ND2 . ASN A 304 ? 0.2980 0.2576 0.0908 0.0127  -0.0447 -0.0058 306 ASN A ND2 
2110 N N   . PRO A 305 ? 0.2751 0.2023 0.1074 -0.0206 -0.0608 0.0145  307 PRO A N   
2111 C CA  . PRO A 305 ? 0.2888 0.2043 0.1196 -0.0241 -0.0680 0.0158  307 PRO A CA  
2112 C C   . PRO A 305 ? 0.3155 0.2288 0.1311 -0.0238 -0.0704 0.0138  307 PRO A C   
2113 O O   . PRO A 305 ? 0.3269 0.2323 0.1406 -0.0262 -0.0769 0.0143  307 PRO A O   
2114 C CB  . PRO A 305 ? 0.2855 0.2019 0.1203 -0.0303 -0.0701 0.0235  307 PRO A CB  
2115 C CG  . PRO A 305 ? 0.2861 0.2156 0.1152 -0.0336 -0.0642 0.0267  307 PRO A CG  
2116 C CD  . PRO A 305 ? 0.2765 0.2161 0.1096 -0.0268 -0.0579 0.0209  307 PRO A CD  
2117 N N   . ASN A 306 ? 0.3341 0.2561 0.1385 -0.0200 -0.0654 0.0111  308 ASN A N   
2118 C CA  . ASN A 306 ? 0.3585 0.2799 0.1464 -0.0195 -0.0669 0.0092  308 ASN A CA  
2119 C C   . ASN A 306 ? 0.3935 0.3019 0.1710 -0.0128 -0.0688 0.0004  308 ASN A C   
2120 O O   . ASN A 306 ? 0.3900 0.2949 0.1674 -0.0056 -0.0657 -0.0048 308 ASN A O   
2121 C CB  . ASN A 306 ? 0.3607 0.3013 0.1400 -0.0192 -0.0604 0.0109  308 ASN A CB  
2122 C CG  . ASN A 306 ? 0.3503 0.3012 0.1368 -0.0283 -0.0587 0.0199  308 ASN A CG  
2123 O OD1 . ASN A 306 ? 0.3504 0.2926 0.1353 -0.0359 -0.0641 0.0264  308 ASN A OD1 
2124 N ND2 . ASN A 306 ? 0.3329 0.3013 0.1253 -0.0277 -0.0520 0.0204  308 ASN A ND2 
2125 N N   . ASN A 307 ? 0.4381 0.3376 0.2043 -0.0155 -0.0745 -0.0010 309 ASN A N   
2126 C CA  . ASN A 307 ? 0.4926 0.3770 0.2425 -0.0112 -0.0772 -0.0094 309 ASN A CA  
2127 C C   . ASN A 307 ? 0.5092 0.3774 0.2644 -0.0115 -0.0801 -0.0131 309 ASN A C   
2128 O O   . ASN A 307 ? 0.5197 0.3725 0.2607 -0.0056 -0.0802 -0.0204 309 ASN A O   
2129 C CB  . ASN A 307 ? 0.5318 0.4213 0.2653 -0.0007 -0.0712 -0.0155 309 ASN A CB  
2130 C CG  . ASN A 307 ? 0.5899 0.4968 0.3152 -0.0024 -0.0684 -0.0122 309 ASN A CG  
2131 O OD1 . ASN A 307 ? 0.6330 0.5347 0.3405 -0.0012 -0.0708 -0.0160 309 ASN A OD1 
2132 N ND2 . ASN A 307 ? 0.6027 0.5292 0.3387 -0.0067 -0.0638 -0.0046 309 ASN A ND2 
2133 N N   . ASN A 308 ? 0.5216 0.3924 0.2951 -0.0182 -0.0828 -0.0081 310 ASN A N   
2134 C CA  A ASN A 308 ? 0.5353 0.3949 0.3152 -0.0215 -0.0857 -0.0102 310 ASN A CA  
2135 C CA  B ASN A 308 ? 0.5280 0.3872 0.3074 -0.0215 -0.0858 -0.0103 310 ASN A CA  
2136 C C   . ASN A 308 ? 0.5453 0.3956 0.3198 -0.0136 -0.0809 -0.0148 310 ASN A C   
2137 O O   . ASN A 308 ? 0.5560 0.3870 0.3208 -0.0145 -0.0839 -0.0194 310 ASN A O   
2138 C CB  A ASN A 308 ? 0.5644 0.4120 0.3342 -0.0290 -0.0938 -0.0133 310 ASN A CB  
2139 C CB  B ASN A 308 ? 0.5464 0.3922 0.3139 -0.0284 -0.0936 -0.0140 310 ASN A CB  
2140 C CG  A ASN A 308 ? 0.5655 0.4250 0.3415 -0.0349 -0.0993 -0.0086 310 ASN A CG  
2141 C CG  B ASN A 308 ? 0.5367 0.3773 0.3130 -0.0369 -0.0979 -0.0141 310 ASN A CG  
2142 O OD1 A ASN A 308 ? 0.5864 0.4531 0.3574 -0.0325 -0.0984 -0.0060 310 ASN A OD1 
2143 O OD1 B ASN A 308 ? 0.5067 0.3556 0.3004 -0.0373 -0.0952 -0.0107 310 ASN A OD1 
2144 N ND2 A ASN A 308 ? 0.5607 0.4239 0.3468 -0.0426 -0.1052 -0.0074 310 ASN A ND2 
2145 N ND2 B ASN A 308 ? 0.5564 0.3842 0.3197 -0.0448 -0.1045 -0.0178 310 ASN A ND2 
2146 N N   . ALA A 309 ? 0.5144 0.3785 0.2944 -0.0063 -0.0739 -0.0132 311 ALA A N   
2147 C CA  . ALA A 309 ? 0.5114 0.3709 0.2861 0.0039  -0.0695 -0.0175 311 ALA A CA  
2148 C C   . ALA A 309 ? 0.4689 0.3198 0.2545 0.0009  -0.0704 -0.0164 311 ALA A C   
2149 O O   . ALA A 309 ? 0.4485 0.3059 0.2507 -0.0078 -0.0720 -0.0113 311 ALA A O   
2150 C CB  . ALA A 309 ? 0.4976 0.3810 0.2774 0.0106  -0.0621 -0.0155 311 ALA A CB  
2151 N N   . SER A 310 ? 0.4705 0.3063 0.2447 0.0093  -0.0696 -0.0213 312 SER A N   
2152 C CA  . SER A 310 ? 0.4307 0.2548 0.2103 0.0063  -0.0708 -0.0204 312 SER A CA  
2153 C C   . SER A 310 ? 0.3988 0.2301 0.1822 0.0175  -0.0655 -0.0208 312 SER A C   
2154 O O   . SER A 310 ? 0.3883 0.2069 0.1717 0.0171  -0.0666 -0.0207 312 SER A O   
2155 C CB  . SER A 310 ? 0.4621 0.2544 0.2206 0.0032  -0.0770 -0.0252 312 SER A CB  
2156 O OG  . SER A 310 ? 0.4928 0.2690 0.2266 0.0163  -0.0772 -0.0321 312 SER A OG  
2157 N N   . THR A 311 ? 0.3624 0.2162 0.1493 0.0263  -0.0600 -0.0207 313 THR A N   
2158 C CA  . THR A 311 ? 0.3426 0.2111 0.1367 0.0356  -0.0550 -0.0204 313 THR A CA  
2159 C C   . THR A 311 ? 0.3071 0.1872 0.1237 0.0260  -0.0536 -0.0138 313 THR A C   
2160 O O   . THR A 311 ? 0.2895 0.1747 0.1179 0.0144  -0.0550 -0.0092 313 THR A O   
2161 C CB  . THR A 311 ? 0.3364 0.2318 0.1292 0.0450  -0.0495 -0.0217 313 THR A CB  
2162 O OG1 . THR A 311 ? 0.3187 0.2321 0.1230 0.0330  -0.0481 -0.0159 313 THR A OG1 
2163 C CG2 . THR A 311 ? 0.3638 0.2483 0.1326 0.0586  -0.0503 -0.0298 313 THR A CG2 
2164 N N   . THR A 312 ? 0.2959 0.1800 0.1170 0.0323  -0.0513 -0.0137 314 THR A N   
2165 C CA  . THR A 312 ? 0.2766 0.1716 0.1169 0.0245  -0.0498 -0.0084 314 THR A CA  
2166 C C   . THR A 312 ? 0.2647 0.1849 0.1128 0.0313  -0.0447 -0.0073 314 THR A C   
2167 O O   . THR A 312 ? 0.2744 0.2034 0.1133 0.0442  -0.0426 -0.0113 314 THR A O   
2168 C CB  . THR A 312 ? 0.2832 0.1574 0.1229 0.0210  -0.0530 -0.0082 314 THR A CB  
2169 O OG1 . THR A 312 ? 0.2920 0.1541 0.1175 0.0336  -0.0533 -0.0122 314 THR A OG1 
2170 C CG2 . THR A 312 ? 0.2942 0.1484 0.1275 0.0113  -0.0581 -0.0088 314 THR A CG2 
2171 N N   . ALA A 313 ? 0.2484 0.1816 0.1130 0.0226  -0.0432 -0.0022 315 ALA A N   
2172 C CA  . ALA A 313 ? 0.2438 0.1993 0.1168 0.0258  -0.0394 -0.0007 315 ALA A CA  
2173 C C   . ALA A 313 ? 0.2378 0.1868 0.1211 0.0204  -0.0404 0.0018  315 ALA A C   
2174 O O   . ALA A 313 ? 0.2351 0.1676 0.1211 0.0129  -0.0433 0.0030  315 ALA A O   
2175 C CB  . ALA A 313 ? 0.2335 0.2144 0.1134 0.0184  -0.0363 0.0031  315 ALA A CB  
2176 N N   . GLN A 314 ? 0.2389 0.2053 0.1286 0.0237  -0.0380 0.0027  316 GLN A N   
2177 C CA  . GLN A 314 ? 0.2446 0.2073 0.1429 0.0193  -0.0386 0.0049  316 GLN A CA  
2178 C C   . GLN A 314 ? 0.2178 0.2025 0.1280 0.0103  -0.0364 0.0090  316 GLN A C   
2179 O O   . GLN A 314 ? 0.2115 0.2202 0.1223 0.0119  -0.0337 0.0094  316 GLN A O   
2180 C CB  . GLN A 314 ? 0.2709 0.2294 0.1621 0.0320  -0.0390 0.0019  316 GLN A CB  
2181 C CG  . GLN A 314 ? 0.2988 0.2434 0.1931 0.0284  -0.0407 0.0034  316 GLN A CG  
2182 C CD  . GLN A 314 ? 0.3341 0.2734 0.2181 0.0419  -0.0419 0.0010  316 GLN A CD  
2183 O OE1 . GLN A 314 ? 0.3743 0.3006 0.2426 0.0536  -0.0437 -0.0026 316 GLN A OE1 
2184 N NE2 . GLN A 314 ? 0.3524 0.3023 0.2437 0.0416  -0.0412 0.0030  316 GLN A NE2 
2185 N N   . THR A 315 ? 0.2020 0.1787 0.1199 0.0007  -0.0377 0.0117  317 THR A N   
2186 C CA  . THR A 315 ? 0.1966 0.1876 0.1220 -0.0081 -0.0367 0.0151  317 THR A CA  
2187 C C   . THR A 315 ? 0.2015 0.2086 0.1300 -0.0030 -0.0351 0.0144  317 THR A C   
2188 O O   . THR A 315 ? 0.2037 0.2040 0.1287 0.0072  -0.0356 0.0117  317 THR A O   
2189 C CB  . THR A 315 ? 0.1852 0.1608 0.1154 -0.0166 -0.0391 0.0169  317 THR A CB  
2190 O OG1 . THR A 315 ? 0.1833 0.1475 0.1151 -0.0123 -0.0398 0.0148  317 THR A OG1 
2191 C CG2 . THR A 315 ? 0.1838 0.1459 0.1116 -0.0208 -0.0416 0.0178  317 THR A CG2 
2192 N N   . LEU A 316 ? 0.2080 0.2354 0.1415 -0.0108 -0.0340 0.0172  318 LEU A N   
2193 C CA  . LEU A 316 ? 0.2074 0.2506 0.1451 -0.0081 -0.0334 0.0169  318 LEU A CA  
2194 C C   . LEU A 316 ? 0.2084 0.2311 0.1482 -0.0094 -0.0354 0.0166  318 LEU A C   
2195 O O   . LEU A 316 ? 0.2108 0.2145 0.1510 -0.0158 -0.0368 0.0172  318 LEU A O   
2196 C CB  . LEU A 316 ? 0.2100 0.2779 0.1515 -0.0206 -0.0325 0.0204  318 LEU A CB  
2197 C CG  . LEU A 316 ? 0.2238 0.3192 0.1637 -0.0222 -0.0299 0.0214  318 LEU A CG  
2198 C CD1 . LEU A 316 ? 0.2266 0.3424 0.1681 -0.0402 -0.0298 0.0261  318 LEU A CD1 
2199 C CD2 . LEU A 316 ? 0.2287 0.3474 0.1687 -0.0049 -0.0277 0.0175  318 LEU A CD2 
2200 N N   . ASP A 317 ? 0.2090 0.2384 0.1499 -0.0029 -0.0355 0.0156  319 ASP A N   
2201 C CA  . ASP A 317 ? 0.2081 0.2211 0.1499 -0.0044 -0.0369 0.0154  319 ASP A CA  
2202 C C   . ASP A 317 ? 0.1921 0.2052 0.1385 -0.0174 -0.0376 0.0172  319 ASP A C   
2203 O O   . ASP A 317 ? 0.1924 0.2230 0.1407 -0.0251 -0.0375 0.0191  319 ASP A O   
2204 C CB  . ASP A 317 ? 0.2294 0.2505 0.1695 0.0051  -0.0374 0.0145  319 ASP A CB  
2205 C CG  . ASP A 317 ? 0.2561 0.2669 0.1865 0.0199  -0.0382 0.0122  319 ASP A CG  
2206 O OD1 . ASP A 317 ? 0.2847 0.2790 0.2099 0.0210  -0.0384 0.0110  319 ASP A OD1 
2207 O OD2 . ASP A 317 ? 0.2840 0.3013 0.2103 0.0303  -0.0394 0.0114  319 ASP A OD2 
2208 N N   . SER A 318 ? 0.1791 0.1726 0.1257 -0.0200 -0.0386 0.0165  320 SER A N   
2209 C CA  . SER A 318 ? 0.1712 0.1603 0.1192 -0.0287 -0.0398 0.0168  320 SER A CA  
2210 C C   . SER A 318 ? 0.1716 0.1584 0.1199 -0.0254 -0.0397 0.0156  320 SER A C   
2211 O O   . SER A 318 ? 0.1607 0.1362 0.1076 -0.0201 -0.0392 0.0145  320 SER A O   
2212 C CB  . SER A 318 ? 0.1706 0.1414 0.1175 -0.0321 -0.0410 0.0162  320 SER A CB  
2213 O OG  . SER A 318 ? 0.1675 0.1308 0.1127 -0.0385 -0.0427 0.0157  320 SER A OG  
2214 N N   . ARG A 319 ? 0.1790 0.1761 0.1278 -0.0301 -0.0404 0.0160  321 ARG A N   
2215 C CA  . ARG A 319 ? 0.1914 0.1888 0.1394 -0.0268 -0.0405 0.0152  321 ARG A CA  
2216 C C   . ARG A 319 ? 0.1777 0.1647 0.1244 -0.0336 -0.0414 0.0136  321 ARG A C   
2217 O O   . ARG A 319 ? 0.1831 0.1686 0.1278 -0.0421 -0.0430 0.0135  321 ARG A O   
2218 C CB  . ARG A 319 ? 0.2207 0.2413 0.1697 -0.0247 -0.0412 0.0164  321 ARG A CB  
2219 C CG  . ARG A 319 ? 0.2592 0.2805 0.2056 -0.0186 -0.0419 0.0161  321 ARG A CG  
2220 C CD  . ARG A 319 ? 0.3037 0.3511 0.2513 -0.0138 -0.0432 0.0171  321 ARG A CD  
2221 N NE  . ARG A 319 ? 0.3702 0.4345 0.3213 -0.0263 -0.0443 0.0177  321 ARG A NE  
2222 C CZ  . ARG A 319 ? 0.4592 0.5538 0.4135 -0.0273 -0.0455 0.0188  321 ARG A CZ  
2223 N NH1 . ARG A 319 ? 0.5205 0.6326 0.4757 -0.0132 -0.0457 0.0188  321 ARG A NH1 
2224 N NH2 . ARG A 319 ? 0.4859 0.5933 0.4412 -0.0423 -0.0470 0.0197  321 ARG A NH2 
2225 N N   . ALA A 320 ? 0.1694 0.1484 0.1148 -0.0302 -0.0405 0.0122  322 ALA A N   
2226 C CA  . ALA A 320 ? 0.1648 0.1376 0.1077 -0.0343 -0.0409 0.0099  322 ALA A CA  
2227 C C   . ALA A 320 ? 0.1627 0.1424 0.1032 -0.0320 -0.0409 0.0104  322 ALA A C   
2228 O O   . ALA A 320 ? 0.1651 0.1467 0.1045 -0.0256 -0.0404 0.0123  322 ALA A O   
2229 C CB  . ALA A 320 ? 0.1632 0.1231 0.1066 -0.0325 -0.0396 0.0074  322 ALA A CB  
2230 N N   . THR A 321 ? 0.1650 0.1458 0.1023 -0.0369 -0.0420 0.0086  323 THR A N   
2231 C CA  . THR A 321 ? 0.1649 0.1535 0.0989 -0.0356 -0.0426 0.0093  323 THR A CA  
2232 C C   . THR A 321 ? 0.1686 0.1486 0.0978 -0.0381 -0.0419 0.0059  323 THR A C   
2233 O O   . THR A 321 ? 0.1727 0.1443 0.0996 -0.0423 -0.0425 0.0025  323 THR A O   
2234 C CB  . THR A 321 ? 0.1664 0.1726 0.1009 -0.0399 -0.0455 0.0106  323 THR A CB  
2235 O OG1 . THR A 321 ? 0.1610 0.1796 0.1001 -0.0362 -0.0456 0.0131  323 THR A OG1 
2236 C CG2 . THR A 321 ? 0.1704 0.1867 0.1013 -0.0378 -0.0470 0.0114  323 THR A CG2 
2237 N N   . VAL A 322 ? 0.1690 0.1500 0.0944 -0.0351 -0.0409 0.0068  324 VAL A N   
2238 C CA  . VAL A 322 ? 0.1755 0.1528 0.0953 -0.0373 -0.0399 0.0037  324 VAL A CA  
2239 C C   . VAL A 322 ? 0.1789 0.1650 0.0931 -0.0378 -0.0420 0.0054  324 VAL A C   
2240 O O   . VAL A 322 ? 0.1781 0.1685 0.0907 -0.0331 -0.0429 0.0095  324 VAL A O   
2241 C CB  . VAL A 322 ? 0.1792 0.1505 0.0984 -0.0348 -0.0361 0.0034  324 VAL A CB  
2242 C CG1 . VAL A 322 ? 0.1841 0.1561 0.0970 -0.0365 -0.0342 0.0002  324 VAL A CG1 
2243 C CG2 . VAL A 322 ? 0.1795 0.1454 0.1049 -0.0338 -0.0347 0.0013  324 VAL A CG2 
2244 N N   . TYR A 323 ? 0.1840 0.1711 0.0934 -0.0430 -0.0436 0.0019  325 TYR A N   
2245 C CA  . TYR A 323 ? 0.1876 0.1842 0.0911 -0.0447 -0.0463 0.0029  325 TYR A CA  
2246 C C   . TYR A 323 ? 0.1914 0.1823 0.0869 -0.0443 -0.0439 0.0006  325 TYR A C   
2247 O O   . TYR A 323 ? 0.1893 0.1716 0.0838 -0.0443 -0.0408 -0.0035 325 TYR A O   
2248 C CB  . TYR A 323 ? 0.1920 0.1942 0.0935 -0.0530 -0.0503 0.0007  325 TYR A CB  
2249 C CG  . TYR A 323 ? 0.1873 0.1990 0.0963 -0.0557 -0.0523 0.0032  325 TYR A CG  
2250 C CD1 . TYR A 323 ? 0.1821 0.2138 0.0963 -0.0517 -0.0539 0.0076  325 TYR A CD1 
2251 C CD2 . TYR A 323 ? 0.1906 0.1916 0.0998 -0.0614 -0.0526 0.0013  325 TYR A CD2 
2252 C CE1 . TYR A 323 ? 0.1780 0.2230 0.0990 -0.0541 -0.0550 0.0096  325 TYR A CE1 
2253 C CE2 . TYR A 323 ? 0.1873 0.1984 0.1020 -0.0655 -0.0540 0.0041  325 TYR A CE2 
2254 C CZ  . TYR A 323 ? 0.1800 0.2152 0.1015 -0.0620 -0.0547 0.0081  325 TYR A CZ  
2255 O OH  . TYR A 323 ? 0.1796 0.2291 0.1066 -0.0659 -0.0555 0.0105  325 TYR A OH  
2256 N N   . THR A 324 ? 0.1972 0.1948 0.0864 -0.0433 -0.0455 0.0034  326 THR A N   
2257 C CA  . THR A 324 ? 0.2059 0.2007 0.0857 -0.0445 -0.0435 0.0015  326 THR A CA  
2258 C C   . THR A 324 ? 0.2156 0.2199 0.0879 -0.0453 -0.0478 0.0038  326 THR A C   
2259 O O   . THR A 324 ? 0.2045 0.2190 0.0803 -0.0430 -0.0518 0.0074  326 THR A O   
2260 C CB  . THR A 324 ? 0.2051 0.1938 0.0833 -0.0418 -0.0392 0.0043  326 THR A CB  
2261 O OG1 . THR A 324 ? 0.2131 0.2016 0.0839 -0.0444 -0.0357 0.0007  326 THR A OG1 
2262 C CG2 . THR A 324 ? 0.2099 0.1976 0.0823 -0.0380 -0.0414 0.0116  326 THR A CG2 
2263 N N   . TYR A 325 ? 0.2121 0.1413 0.0973 -0.0324 -0.0319 -0.0093 327 TYR A N   
2264 C CA  . TYR A 325 ? 0.2073 0.1522 0.1045 -0.0259 -0.0246 -0.0110 327 TYR A CA  
2265 C C   . TYR A 325 ? 0.2022 0.1479 0.1061 -0.0217 -0.0250 -0.0135 327 TYR A C   
2266 O O   . TYR A 325 ? 0.1964 0.1353 0.0994 -0.0258 -0.0317 -0.0133 327 TYR A O   
2267 C CB  . TYR A 325 ? 0.2020 0.1589 0.1139 -0.0291 -0.0271 -0.0096 327 TYR A CB  
2268 C CG  . TYR A 325 ? 0.2269 0.1774 0.1286 -0.0370 -0.0293 -0.0060 327 TYR A CG  
2269 C CD1 . TYR A 325 ? 0.2465 0.2027 0.1373 -0.0392 -0.0220 -0.0040 327 TYR A CD1 
2270 C CD2 . TYR A 325 ? 0.2417 0.1802 0.1423 -0.0411 -0.0384 -0.0041 327 TYR A CD2 
2271 C CE1 . TYR A 325 ? 0.2689 0.2195 0.1486 -0.0486 -0.0239 0.0000  327 TYR A CE1 
2272 C CE2 . TYR A 325 ? 0.2657 0.1931 0.1525 -0.0492 -0.0412 -0.0002 327 TYR A CE2 
2273 C CZ  . TYR A 325 ? 0.2829 0.2166 0.1595 -0.0547 -0.0340 0.0019  327 TYR A CZ  
2274 O OH  . TYR A 325 ? 0.3157 0.2393 0.1772 -0.0647 -0.0363 0.0064  327 TYR A OH  
2275 N N   . ARG A 326 ? 0.2024 0.1600 0.1133 -0.0144 -0.0182 -0.0149 328 ARG A N   
2276 C CA  . ARG A 326 ? 0.2010 0.1614 0.1197 -0.0108 -0.0184 -0.0167 328 ARG A CA  
2277 C C   . ARG A 326 ? 0.1770 0.1574 0.1163 -0.0093 -0.0184 -0.0169 328 ARG A C   
2278 O O   . ARG A 326 ? 0.1738 0.1675 0.1166 -0.0072 -0.0136 -0.0161 328 ARG A O   
2279 C CB  . ARG A 326 ? 0.2278 0.1795 0.1309 -0.0016 -0.0108 -0.0179 328 ARG A CB  
2280 C CG  . ARG A 326 ? 0.2444 0.1959 0.1520 0.0010  -0.0111 -0.0190 328 ARG A CG  
2281 C CD  . ARG A 326 ? 0.2837 0.2303 0.1783 0.0141  -0.0031 -0.0195 328 ARG A CD  
2282 N NE  . ARG A 326 ? 0.2966 0.2718 0.2071 0.0219  0.0021  -0.0182 328 ARG A NE  
2283 C CZ  . ARG A 326 ? 0.3535 0.3357 0.2566 0.0367  0.0099  -0.0171 328 ARG A CZ  
2284 N NH1 . ARG A 326 ? 0.4015 0.3562 0.2772 0.0474  0.0137  -0.0180 328 ARG A NH1 
2285 N NH2 . ARG A 326 ? 0.3442 0.3604 0.2648 0.0406  0.0133  -0.0145 328 ARG A NH2 
2286 N N   . LEU A 327 ? 0.1664 0.1502 0.1175 -0.0108 -0.0236 -0.0177 329 LEU A N   
2287 C CA  . LEU A 327 ? 0.1497 0.1468 0.1150 -0.0083 -0.0234 -0.0191 329 LEU A CA  
2288 C C   . LEU A 327 ? 0.1440 0.1462 0.1119 -0.0033 -0.0195 -0.0203 329 LEU A C   
2289 O O   . LEU A 327 ? 0.1441 0.1411 0.1098 -0.0045 -0.0214 -0.0202 329 LEU A O   
2290 C CB  . LEU A 327 ? 0.1494 0.1461 0.1223 -0.0091 -0.0301 -0.0193 329 LEU A CB  
2291 C CG  . LEU A 327 ? 0.1443 0.1494 0.1270 -0.0051 -0.0300 -0.0216 329 LEU A CG  
2292 C CD1 . LEU A 327 ? 0.1466 0.1523 0.1271 -0.0081 -0.0287 -0.0222 329 LEU A CD1 
2293 C CD2 . LEU A 327 ? 0.1478 0.1519 0.1343 -0.0008 -0.0354 -0.0216 329 LEU A CD2 
2294 N N   . ARG A 328 ? 0.1402 0.1537 0.1113 0.0010  -0.0148 -0.0204 330 ARG A N   
2295 C CA  . ARG A 328 ? 0.1451 0.1627 0.1170 0.0071  -0.0115 -0.0210 330 ARG A CA  
2296 C C   . ARG A 328 ? 0.1283 0.1600 0.1136 0.0068  -0.0129 -0.0223 330 ARG A C   
2297 O O   . ARG A 328 ? 0.1185 0.1599 0.1083 0.0037  -0.0136 -0.0221 330 ARG A O   
2298 C CB  . ARG A 328 ? 0.1595 0.1807 0.1222 0.0160  -0.0047 -0.0194 330 ARG A CB  
2299 C CG  . ARG A 328 ? 0.1728 0.2005 0.1363 0.0242  -0.0017 -0.0190 330 ARG A CG  
2300 C CD  . ARG A 328 ? 0.1956 0.2209 0.1439 0.0380  0.0049  -0.0169 330 ARG A CD  
2301 N NE  . ARG A 328 ? 0.2369 0.2289 0.1607 0.0405  0.0057  -0.0178 330 ARG A NE  
2302 C CZ  . ARG A 328 ? 0.2713 0.2465 0.1719 0.0547  0.0111  -0.0169 330 ARG A CZ  
2303 N NH1 . ARG A 328 ? 0.2878 0.2839 0.1914 0.0701  0.0166  -0.0143 330 ARG A NH1 
2304 N NH2 . ARG A 328 ? 0.2996 0.2363 0.1716 0.0535  0.0102  -0.0180 330 ARG A NH2 
2305 N N   . LEU A 329 ? 0.1240 0.1556 0.1123 0.0084  -0.0134 -0.0234 331 LEU A N   
2306 C CA  . LEU A 329 ? 0.1195 0.1626 0.1162 0.0097  -0.0136 -0.0250 331 LEU A CA  
2307 C C   . LEU A 329 ? 0.1173 0.1650 0.1106 0.0157  -0.0096 -0.0237 331 LEU A C   
2308 O O   . LEU A 329 ? 0.1273 0.1632 0.1107 0.0179  -0.0079 -0.0225 331 LEU A O   
2309 C CB  . LEU A 329 ? 0.1234 0.1662 0.1255 0.0089  -0.0163 -0.0267 331 LEU A CB  
2310 C CG  . LEU A 329 ? 0.1339 0.1716 0.1373 0.0069  -0.0205 -0.0266 331 LEU A CG  
2311 C CD1 . LEU A 329 ? 0.1353 0.1812 0.1453 0.0103  -0.0218 -0.0274 331 LEU A CD1 
2312 C CD2 . LEU A 329 ? 0.1414 0.1727 0.1418 0.0050  -0.0230 -0.0276 331 LEU A CD2 
2313 N N   . THR A 330 ? 0.1076 0.1702 0.1058 0.0174  -0.0089 -0.0235 332 THR A N   
2314 C CA  . THR A 330 ? 0.1098 0.1793 0.1051 0.0249  -0.0060 -0.0216 332 THR A CA  
2315 C C   . THR A 330 ? 0.1010 0.1781 0.1021 0.0223  -0.0081 -0.0236 332 THR A C   
2316 O O   . THR A 330 ? 0.0929 0.1797 0.0987 0.0171  -0.0109 -0.0248 332 THR A O   
2317 C CB  . THR A 330 ? 0.1153 0.2030 0.1110 0.0306  -0.0033 -0.0179 332 THR A CB  
2318 O OG1 . THR A 330 ? 0.1227 0.2004 0.1092 0.0353  0.0000  -0.0166 332 THR A OG1 
2319 C CG2 . THR A 330 ? 0.1239 0.2222 0.1166 0.0411  -0.0009 -0.0150 332 THR A CG2 
2320 N N   . LYS A 331 ? 0.1015 0.1715 0.0987 0.0244  -0.0070 -0.0238 333 LYS A N   
2321 C CA  . LYS A 331 ? 0.0993 0.1750 0.1000 0.0226  -0.0081 -0.0260 333 LYS A CA  
2322 C C   . LYS A 331 ? 0.0961 0.1826 0.0942 0.0271  -0.0074 -0.0239 333 LYS A C   
2323 O O   . LYS A 331 ? 0.0997 0.1816 0.0896 0.0338  -0.0051 -0.0204 333 LYS A O   
2324 C CB  . LYS A 331 ? 0.1062 0.1751 0.1047 0.0209  -0.0070 -0.0262 333 LYS A CB  
2325 C CG  . LYS A 331 ? 0.1081 0.1847 0.1099 0.0206  -0.0069 -0.0289 333 LYS A CG  
2326 C CD  . LYS A 331 ? 0.1123 0.1894 0.1185 0.0205  -0.0089 -0.0332 333 LYS A CD  
2327 C CE  . LYS A 331 ? 0.1244 0.2059 0.1284 0.0236  -0.0076 -0.0364 333 LYS A CE  
2328 N NZ  . LYS A 331 ? 0.1349 0.2176 0.1327 0.0228  -0.0085 -0.0375 333 LYS A NZ  
2329 N N   . VAL A 332 ? 0.0910 0.1894 0.0928 0.0233  -0.0103 -0.0255 334 VAL A N   
2330 C CA  . VAL A 332 ? 0.0938 0.2080 0.0944 0.0260  -0.0112 -0.0226 334 VAL A CA  
2331 C C   . VAL A 332 ? 0.0960 0.2099 0.0936 0.0208  -0.0137 -0.0264 334 VAL A C   
2332 O O   . VAL A 332 ? 0.0960 0.1974 0.0918 0.0175  -0.0139 -0.0312 334 VAL A O   
2333 C CB  . VAL A 332 ? 0.0922 0.2280 0.0980 0.0242  -0.0131 -0.0189 334 VAL A CB  
2334 C CG1 . VAL A 332 ? 0.0934 0.2293 0.0995 0.0321  -0.0091 -0.0155 334 VAL A CG1 
2335 C CG2 . VAL A 332 ? 0.0944 0.2315 0.1013 0.0103  -0.0179 -0.0217 334 VAL A CG2 
2336 N N   . ASN A 333 ? 0.0997 0.2277 0.0948 0.0214  -0.0157 -0.0239 335 ASN A N   
2337 C CA  . ASN A 333 ? 0.1070 0.2338 0.0952 0.0148  -0.0190 -0.0277 335 ASN A CA  
2338 C C   . ASN A 333 ? 0.1152 0.2610 0.1029 0.0055  -0.0253 -0.0252 335 ASN A C   
2339 O O   . ASN A 333 ? 0.1063 0.2705 0.1022 0.0050  -0.0260 -0.0202 335 ASN A O   
2340 C CB  . ASN A 333 ? 0.1118 0.2354 0.0937 0.0203  -0.0165 -0.0275 335 ASN A CB  
2341 C CG  . ASN A 333 ? 0.1130 0.2502 0.0939 0.0278  -0.0166 -0.0206 335 ASN A CG  
2342 O OD1 . ASN A 333 ? 0.1123 0.2675 0.0985 0.0305  -0.0185 -0.0158 335 ASN A OD1 
2343 N ND2 . ASN A 333 ? 0.1243 0.2538 0.0971 0.0325  -0.0140 -0.0193 335 ASN A ND2 
2344 N N   . GLU A 334 ? 0.1327 0.2765 0.1093 -0.0026 -0.0298 -0.0280 336 GLU A N   
2345 C CA  . GLU A 334 ? 0.1492 0.3112 0.1219 -0.0165 -0.0376 -0.0251 336 GLU A CA  
2346 C C   . GLU A 334 ? 0.1407 0.3387 0.1229 -0.0108 -0.0389 -0.0163 336 GLU A C   
2347 O O   . GLU A 334 ? 0.1458 0.3730 0.1318 -0.0208 -0.0447 -0.0107 336 GLU A O   
2348 C CB  . GLU A 334 ? 0.1797 0.3220 0.1312 -0.0276 -0.0427 -0.0313 336 GLU A CB  
2349 C CG  . GLU A 334 ? 0.2073 0.3138 0.1454 -0.0307 -0.0421 -0.0392 336 GLU A CG  
2350 C CD  . GLU A 334 ? 0.2530 0.3309 0.1619 -0.0405 -0.0472 -0.0461 336 GLU A CD  
2351 O OE1 . GLU A 334 ? 0.2719 0.3423 0.1708 -0.0340 -0.0450 -0.0497 336 GLU A OE1 
2352 O OE2 . GLU A 334 ? 0.2954 0.3554 0.1882 -0.0547 -0.0532 -0.0479 336 GLU A OE2 
2353 N N   . ARG A 335 ? 0.1317 0.3283 0.1159 0.0051  -0.0338 -0.0143 337 ARG A N   
2354 C CA  . ARG A 335 ? 0.1350 0.3605 0.1248 0.0163  -0.0342 -0.0055 337 ARG A CA  
2355 C C   . ARG A 335 ? 0.1277 0.3662 0.1284 0.0281  -0.0296 -0.0003 337 ARG A C   
2356 O O   . ARG A 335 ? 0.1238 0.3839 0.1272 0.0427  -0.0284 0.0071  337 ARG A O   
2357 C CB  . ARG A 335 ? 0.1395 0.3497 0.1197 0.0278  -0.0311 -0.0054 337 ARG A CB  
2358 C CG  . ARG A 335 ? 0.1518 0.3550 0.1195 0.0182  -0.0352 -0.0093 337 ARG A CG  
2359 C CD  . ARG A 335 ? 0.1592 0.3402 0.1166 0.0268  -0.0299 -0.0108 337 ARG A CD  
2360 N NE  . ARG A 335 ? 0.1656 0.3542 0.1209 0.0419  -0.0287 -0.0025 337 ARG A NE  
2361 C CZ  . ARG A 335 ? 0.1771 0.3869 0.1285 0.0461  -0.0337 0.0039  337 ARG A CZ  
2362 N NH1 . ARG A 335 ? 0.1793 0.4008 0.1265 0.0334  -0.0401 0.0020  337 ARG A NH1 
2363 N NH2 . ARG A 335 ? 0.1885 0.4047 0.1366 0.0637  -0.0326 0.0121  337 ARG A NH2 
2364 N N   . GLN A 336 ? 0.1347 0.3596 0.1393 0.0229  -0.0271 -0.0041 338 GLN A N   
2365 C CA  . GLN A 336 ? 0.1425 0.3751 0.1541 0.0334  -0.0222 -0.0003 338 GLN A CA  
2366 C C   . GLN A 336 ? 0.1444 0.3566 0.1477 0.0530  -0.0160 0.0009  338 GLN A C   
2367 O O   . GLN A 336 ? 0.1496 0.3706 0.1521 0.0684  -0.0120 0.0060  338 GLN A O   
2368 C CB  . GLN A 336 ? 0.1580 0.4378 0.1801 0.0344  -0.0245 0.0083  338 GLN A CB  
2369 C CG  . GLN A 336 ? 0.1746 0.4748 0.2007 0.0100  -0.0321 0.0087  338 GLN A CG  
2370 C CD  . GLN A 336 ? 0.1916 0.5373 0.2305 0.0088  -0.0318 0.0174  338 GLN A CD  
2371 O OE1 . GLN A 336 ? 0.2121 0.6044 0.2588 0.0087  -0.0354 0.0261  338 GLN A OE1 
2372 N NE2 . GLN A 336 ? 0.2144 0.5506 0.2558 0.0091  -0.0270 0.0160  338 GLN A NE2 
2373 N N   . GLU A 337 ? 0.1455 0.3281 0.1394 0.0518  -0.0149 -0.0037 339 GLU A N   
2374 C CA  . GLU A 337 ? 0.1597 0.3155 0.1405 0.0640  -0.0101 -0.0026 339 GLU A CA  
2375 C C   . GLU A 337 ? 0.1580 0.2882 0.1380 0.0582  -0.0072 -0.0076 339 GLU A C   
2376 O O   . GLU A 337 ? 0.1440 0.2728 0.1322 0.0459  -0.0088 -0.0127 339 GLU A O   
2377 C CB  . GLU A 337 ? 0.1762 0.3206 0.1462 0.0640  -0.0110 -0.0026 339 GLU A CB  
2378 C CG  . GLU A 337 ? 0.1856 0.3548 0.1542 0.0713  -0.0147 0.0032  339 GLU A CG  
2379 C CD  . GLU A 337 ? 0.2130 0.3728 0.1702 0.0691  -0.0163 0.0032  339 GLU A CD  
2380 O OE1 . GLU A 337 ? 0.2186 0.3569 0.1715 0.0598  -0.0142 -0.0021 339 GLU A OE1 
2381 O OE2 . GLU A 337 ? 0.2200 0.3977 0.1729 0.0770  -0.0197 0.0092  339 GLU A OE2 
2382 N N   . ARG A 338 ? 0.1668 0.2741 0.1335 0.0673  -0.0034 -0.0057 340 ARG A N   
2383 C CA  . ARG A 338 ? 0.1705 0.2543 0.1343 0.0597  -0.0018 -0.0094 340 ARG A CA  
2384 C C   . ARG A 338 ? 0.1678 0.2362 0.1260 0.0509  -0.0020 -0.0114 340 ARG A C   
2385 O O   . ARG A 338 ? 0.1750 0.2366 0.1212 0.0543  -0.0018 -0.0086 340 ARG A O   
2386 C CB  . ARG A 338 ? 0.1978 0.2607 0.1450 0.0704  0.0015  -0.0068 340 ARG A CB  
2387 C CG  . ARG A 338 ? 0.2039 0.2879 0.1586 0.0795  0.0032  -0.0048 340 ARG A CG  
2388 C CD  . ARG A 338 ? 0.2495 0.3095 0.1811 0.0953  0.0076  -0.0022 340 ARG A CD  
2389 N NE  . ARG A 338 ? 0.2647 0.3453 0.2032 0.1034  0.0107  -0.0006 340 ARG A NE  
2390 C CZ  . ARG A 338 ? 0.2846 0.3607 0.2276 0.0949  0.0113  -0.0036 340 ARG A CZ  
2391 N NH1 . ARG A 338 ? 0.2962 0.3503 0.2392 0.0789  0.0085  -0.0081 340 ARG A NH1 
2392 N NH2 . ARG A 338 ? 0.2922 0.3887 0.2390 0.1033  0.0150  -0.0012 340 ARG A NH2 
2393 N N   . VAL A 339 ? 0.1495 0.2165 0.1168 0.0400  -0.0025 -0.0156 341 VAL A N   
2394 C CA  . VAL A 339 ? 0.1484 0.2125 0.1153 0.0319  -0.0020 -0.0171 341 VAL A CA  
2395 C C   . VAL A 339 ? 0.1526 0.2027 0.1151 0.0245  -0.0015 -0.0164 341 VAL A C   
2396 O O   . VAL A 339 ? 0.1375 0.1890 0.1084 0.0223  -0.0025 -0.0185 341 VAL A O   
2397 C CB  . VAL A 339 ? 0.1347 0.2152 0.1152 0.0281  -0.0033 -0.0221 341 VAL A CB  
2398 C CG1 . VAL A 339 ? 0.1370 0.2200 0.1175 0.0233  -0.0012 -0.0234 341 VAL A CG1 
2399 C CG2 . VAL A 339 ? 0.1318 0.2249 0.1130 0.0312  -0.0055 -0.0223 341 VAL A CG2 
2400 N N   . ALA A 340 ? 0.1675 0.2047 0.1154 0.0188  -0.0006 -0.0129 342 ALA A N   
2401 C CA  . ALA A 340 ? 0.1736 0.2007 0.1150 0.0068  -0.0012 -0.0108 342 ALA A CA  
2402 C C   . ALA A 340 ? 0.1651 0.2171 0.1223 -0.0012 -0.0004 -0.0116 342 ALA A C   
2403 O O   . ALA A 340 ? 0.1624 0.2306 0.1276 0.0026  0.0014  -0.0137 342 ALA A O   
2404 C CB  . ALA A 340 ? 0.2038 0.2014 0.1158 0.0024  -0.0014 -0.0054 342 ALA A CB  
2405 N N   . GLY A 341 ? 0.1670 0.2228 0.1264 -0.0120 -0.0019 -0.0095 343 GLY A N   
2406 C CA  . GLY A 341 ? 0.1626 0.2468 0.1348 -0.0192 -0.0006 -0.0079 343 GLY A CA  
2407 C C   . GLY A 341 ? 0.1425 0.2501 0.1368 -0.0111 -0.0005 -0.0121 343 GLY A C   
2408 O O   . GLY A 341 ? 0.1426 0.2774 0.1478 -0.0113 0.0017  -0.0111 343 GLY A O   
2409 N N   . ALA A 342 ? 0.1330 0.2297 0.1312 -0.0031 -0.0025 -0.0164 344 ALA A N   
2410 C CA  . ALA A 342 ? 0.1269 0.2362 0.1393 0.0036  -0.0037 -0.0197 344 ALA A CA  
2411 C C   . ALA A 342 ? 0.1282 0.2423 0.1437 -0.0044 -0.0071 -0.0158 344 ALA A C   
2412 O O   . ALA A 342 ? 0.1407 0.2388 0.1440 -0.0149 -0.0093 -0.0123 344 ALA A O   
2413 C CB  . ALA A 342 ? 0.1237 0.2186 0.1357 0.0114  -0.0051 -0.0245 344 ALA A CB  
2414 N N   . GLY A 343 ? 0.1221 0.2572 0.1510 0.0012  -0.0078 -0.0161 345 GLY A N   
2415 C CA  . GLY A 343 ? 0.1242 0.2686 0.1582 -0.0045 -0.0122 -0.0122 345 GLY A CA  
2416 C C   . GLY A 343 ? 0.1203 0.2656 0.1620 0.0089  -0.0141 -0.0157 345 GLY A C   
2417 O O   . GLY A 343 ? 0.1184 0.2697 0.1635 0.0225  -0.0113 -0.0195 345 GLY A O   
2418 N N   . PHE A 344 ? 0.1226 0.2571 0.1623 0.0049  -0.0190 -0.0145 346 PHE A N   
2419 C CA  . PHE A 344 ? 0.1226 0.2502 0.1644 0.0160  -0.0216 -0.0173 346 PHE A CA  
2420 C C   . PHE A 344 ? 0.1274 0.2723 0.1760 0.0143  -0.0268 -0.0120 346 PHE A C   
2421 O O   . PHE A 344 ? 0.1343 0.2828 0.1807 -0.0004 -0.0302 -0.0072 346 PHE A O   
2422 C CB  . PHE A 344 ? 0.1252 0.2221 0.1565 0.0139  -0.0224 -0.0211 346 PHE A CB  
2423 C CG  . PHE A 344 ? 0.1294 0.2158 0.1562 0.0183  -0.0187 -0.0258 346 PHE A CG  
2424 C CD1 . PHE A 344 ? 0.1394 0.2213 0.1641 0.0284  -0.0183 -0.0300 346 PHE A CD1 
2425 C CD2 . PHE A 344 ? 0.1289 0.2082 0.1500 0.0126  -0.0161 -0.0255 346 PHE A CD2 
2426 C CE1 . PHE A 344 ? 0.1394 0.2127 0.1580 0.0293  -0.0162 -0.0339 346 PHE A CE1 
2427 C CE2 . PHE A 344 ? 0.1266 0.2018 0.1447 0.0162  -0.0137 -0.0287 346 PHE A CE2 
2428 C CZ  . PHE A 344 ? 0.1333 0.2068 0.1508 0.0229  -0.0141 -0.0328 346 PHE A CZ  
2429 N N   . THR A 345 ? 0.1278 0.2812 0.1813 0.0299  -0.0280 -0.0126 347 THR A N   
2430 C CA  . THR A 345 ? 0.1304 0.3012 0.1901 0.0323  -0.0337 -0.0072 347 THR A CA  
2431 C C   . THR A 345 ? 0.1372 0.2775 0.1863 0.0409  -0.0373 -0.0106 347 THR A C   
2432 O O   . THR A 345 ? 0.1422 0.2656 0.1835 0.0549  -0.0353 -0.0154 347 THR A O   
2433 C CB  . THR A 345 ? 0.1307 0.3442 0.2042 0.0461  -0.0321 -0.0027 347 THR A CB  
2434 O OG1 . THR A 345 ? 0.1251 0.3678 0.2071 0.0346  -0.0284 0.0011  347 THR A OG1 
2435 C CG2 . THR A 345 ? 0.1358 0.3752 0.2178 0.0493  -0.0388 0.0046  347 THR A CG2 
2436 N N   . LEU A 346 ? 0.1417 0.2715 0.1864 0.0307  -0.0428 -0.0078 348 LEU A N   
2437 C CA  . LEU A 346 ? 0.1540 0.2560 0.1872 0.0359  -0.0466 -0.0097 348 LEU A CA  
2438 C C   . LEU A 346 ? 0.1683 0.2867 0.2052 0.0480  -0.0525 -0.0044 348 LEU A C   
2439 O O   . LEU A 346 ? 0.1604 0.3078 0.2074 0.0416  -0.0567 0.0022  348 LEU A O   
2440 C CB  . LEU A 346 ? 0.1583 0.2394 0.1823 0.0194  -0.0484 -0.0097 348 LEU A CB  
2441 C CG  . LEU A 346 ? 0.1701 0.2230 0.1808 0.0209  -0.0515 -0.0110 348 LEU A CG  
2442 C CD1 . LEU A 346 ? 0.1749 0.2050 0.1766 0.0251  -0.0478 -0.0166 348 LEU A CD1 
2443 C CD2 . LEU A 346 ? 0.1762 0.2169 0.1784 0.0064  -0.0531 -0.0095 348 LEU A CD2 
2444 N N   . TYR A 347 ? 0.1858 0.2837 0.2114 0.0652  -0.0533 -0.0070 349 TYR A N   
2445 C CA  . TYR A 347 ? 0.2068 0.3113 0.2299 0.0820  -0.0589 -0.0023 349 TYR A CA  
2446 C C   . TYR A 347 ? 0.2316 0.2954 0.2348 0.0786  -0.0641 -0.0032 349 TYR A C   
2447 O O   . TYR A 347 ? 0.2313 0.2610 0.2204 0.0708  -0.0619 -0.0086 349 TYR A O   
2448 C CB  . TYR A 347 ? 0.2245 0.3307 0.2425 0.1083  -0.0552 -0.0046 349 TYR A CB  
2449 C CG  . TYR A 347 ? 0.2081 0.3612 0.2458 0.1150  -0.0495 -0.0025 349 TYR A CG  
2450 C CD1 . TYR A 347 ? 0.2064 0.4093 0.2612 0.1260  -0.0515 0.0060  349 TYR A CD1 
2451 C CD2 . TYR A 347 ? 0.1974 0.3492 0.2371 0.1087  -0.0422 -0.0078 349 TYR A CD2 
2452 C CE1 . TYR A 347 ? 0.1956 0.4469 0.2689 0.1297  -0.0458 0.0092  349 TYR A CE1 
2453 C CE2 . TYR A 347 ? 0.1869 0.3814 0.2429 0.1129  -0.0366 -0.0052 349 TYR A CE2 
2454 C CZ  . TYR A 347 ? 0.1850 0.4301 0.2578 0.1231  -0.0381 0.0033  349 TYR A CZ  
2455 O OH  . TYR A 347 ? 0.1754 0.4687 0.2650 0.1252  -0.0322 0.0072  349 TYR A OH  
2456 N N   . LYS A 348 ? 0.2597 0.3303 0.2615 0.0839  -0.0714 0.0030  350 LYS A N   
2457 C CA  . LYS A 348 ? 0.2995 0.3311 0.2793 0.0841  -0.0769 0.0033  350 LYS A CA  
2458 C C   . LYS A 348 ? 0.3510 0.3784 0.3198 0.1114  -0.0813 0.0067  350 LYS A C   
2459 O O   . LYS A 348 ? 0.3485 0.4172 0.3333 0.1264  -0.0824 0.0122  350 LYS A O   
2460 C CB  . LYS A 348 ? 0.2937 0.3294 0.2754 0.0654  -0.0823 0.0078  350 LYS A CB  
2461 C CG  . LYS A 348 ? 0.3164 0.3115 0.2745 0.0606  -0.0867 0.0081  350 LYS A CG  
2462 C CD  . LYS A 348 ? 0.3102 0.3098 0.2682 0.0427  -0.0912 0.0122  350 LYS A CD  
2463 C CE  . LYS A 348 ? 0.3238 0.2848 0.2590 0.0330  -0.0926 0.0115  350 LYS A CE  
2464 N NZ  . LYS A 348 ? 0.3657 0.3105 0.2847 0.0453  -0.1012 0.0170  350 LYS A NZ  
2465 N N   . LYS A 349 ? 0.4186 0.3961 0.3578 0.1174  -0.0839 0.0043  351 LYS A N   
2466 C CA  . LYS A 349 ? 0.5105 0.4699 0.4293 0.1463  -0.0878 0.0066  351 LYS A CA  
2467 C C   . LYS A 349 ? 0.5265 0.4935 0.4434 0.1510  -0.0971 0.0154  351 LYS A C   
2468 O O   . LYS A 349 ? 0.5180 0.4572 0.4212 0.1340  -0.1017 0.0166  351 LYS A O   
2469 C CB  . LYS A 349 ? 0.5903 0.4848 0.4704 0.1488  -0.0876 0.0003  351 LYS A CB  
2470 C CG  . LYS A 349 ? 0.6627 0.5322 0.5161 0.1832  -0.0885 -0.0001 351 LYS A CG  
2471 C CD  . LYS A 349 ? 0.7507 0.5504 0.5596 0.1824  -0.0886 -0.0070 351 LYS A CD  
2472 C CE  . LYS A 349 ? 0.8133 0.5617 0.5907 0.1667  -0.0964 -0.0046 351 LYS A CE  
2473 N NZ  . LYS A 349 ? 0.8921 0.5701 0.6204 0.1650  -0.0979 -0.0102 351 LYS A NZ  
2474 N N   . ILE A 350 ? 0.5668 0.5771 0.4989 0.1735  -0.0996 0.0223  352 ILE A N   
2475 C CA  . ILE A 350 ? 0.6216 0.6375 0.5465 0.1884  -0.1093 0.0316  352 ILE A CA  
2476 C C   . ILE A 350 ? 0.6740 0.6673 0.5738 0.2281  -0.1095 0.0321  352 ILE A C   
2477 O O   . ILE A 350 ? 0.6746 0.7064 0.5889 0.2518  -0.1045 0.0332  352 ILE A O   
2478 C CB  . ILE A 350 ? 0.5939 0.6824 0.5545 0.1833  -0.1133 0.0410  352 ILE A CB  
2479 C CG1 . ILE A 350 ? 0.5581 0.6532 0.5305 0.1451  -0.1153 0.0408  352 ILE A CG1 
2480 C CG2 . ILE A 350 ? 0.6169 0.7244 0.5732 0.2088  -0.1228 0.0518  352 ILE A CG2 
2481 C CD1 . ILE A 350 ? 0.5178 0.6260 0.5073 0.1242  -0.1064 0.0342  352 ILE A CD1 
2482 N N   . ASN A 351 ? 0.7267 0.6554 0.5856 0.2354  -0.1150 0.0316  353 ASN A N   
2483 C CA  . ASN A 351 ? 0.7852 0.6744 0.6076 0.2735  -0.1160 0.0314  353 ASN A CA  
2484 C C   . ASN A 351 ? 0.8113 0.6689 0.6173 0.2785  -0.1066 0.0206  353 ASN A C   
2485 O O   . ASN A 351 ? 0.7844 0.6032 0.5779 0.2505  -0.1044 0.0131  353 ASN A O   
2486 C CB  . ASN A 351 ? 0.7821 0.7264 0.6207 0.3104  -0.1189 0.0415  353 ASN A CB  
2487 C CG  . ASN A 351 ? 0.7606 0.7368 0.6137 0.3033  -0.1297 0.0529  353 ASN A CG  
2488 O OD1 . ASN A 351 ? 0.7579 0.7150 0.6095 0.2703  -0.1342 0.0526  353 ASN A OD1 
2489 N ND2 . ASN A 351 ? 0.7427 0.7703 0.6095 0.3345  -0.1339 0.0634  353 ASN A ND2 
2490 N N   . ASN A 352 ? 0.8488 0.7254 0.6537 0.3147  -0.1014 0.0202  354 ASN A N   
2491 C CA  . ASN A 352 ? 0.9014 0.7606 0.6959 0.3204  -0.0917 0.0103  354 ASN A CA  
2492 C C   . ASN A 352 ? 0.8757 0.8125 0.7219 0.3093  -0.0835 0.0103  354 ASN A C   
2493 O O   . ASN A 352 ? 0.8711 0.8055 0.7162 0.3110  -0.0749 0.0027  354 ASN A O   
2494 C CB  . ASN A 352 ? 0.9749 0.7999 0.7294 0.3679  -0.0896 0.0088  354 ASN A CB  
2495 C CG  . ASN A 352 ? 1.0577 0.7791 0.7467 0.3683  -0.0933 0.0016  354 ASN A CG  
2496 O OD1 . ASN A 352 ? 1.0980 0.7753 0.7678 0.3419  -0.1011 0.0025  354 ASN A OD1 
2497 N ND2 . ASN A 352 ? 1.1157 0.7965 0.7671 0.3960  -0.0877 -0.0054 354 ASN A ND2 
2498 N N   . GLN A 353 ? 0.8443 0.8460 0.7318 0.2954  -0.0869 0.0190  355 GLN A N   
2499 C CA  . GLN A 353 ? 0.7781 0.8564 0.7109 0.2871  -0.0808 0.0217  355 GLN A CA  
2500 C C   . GLN A 353 ? 0.6709 0.7527 0.6234 0.2424  -0.0800 0.0181  355 GLN A C   
2501 O O   . GLN A 353 ? 0.6636 0.7439 0.6217 0.2197  -0.0870 0.0219  355 GLN A O   
2502 C CB  . GLN A 353 ? 0.8000 0.9492 0.7608 0.3021  -0.0860 0.0350  355 GLN A CB  
2503 C CG  . GLN A 353 ? 0.7986 1.0303 0.7985 0.3061  -0.0790 0.0398  355 GLN A CG  
2504 C CD  . GLN A 353 ? 0.8519 1.1477 0.8673 0.3389  -0.0823 0.0527  355 GLN A CD  
2505 O OE1 . GLN A 353 ? 0.8303 1.1960 0.8798 0.3245  -0.0874 0.0636  355 GLN A OE1 
2506 N NE2 . GLN A 353 ? 0.9161 1.1875 0.9031 0.3839  -0.0799 0.0521  355 GLN A NE2 
2507 N N   . TYR A 354 ? 0.5843 0.6702 0.5451 0.2320  -0.0713 0.0109  356 TYR A N   
2508 C CA  . TYR A 354 ? 0.4808 0.5772 0.4613 0.1952  -0.0693 0.0083  356 TYR A CA  
2509 C C   . TYR A 354 ? 0.4263 0.5947 0.4440 0.1850  -0.0700 0.0169  356 TYR A C   
2510 O O   . TYR A 354 ? 0.4314 0.6487 0.4654 0.2033  -0.0662 0.0214  356 TYR A O   
2511 C CB  . TYR A 354 ? 0.4577 0.5316 0.4306 0.1894  -0.0607 -0.0014 356 TYR A CB  
2512 C CG  . TYR A 354 ? 0.4686 0.4715 0.4060 0.1831  -0.0622 -0.0092 356 TYR A CG  
2513 C CD1 . TYR A 354 ? 0.4443 0.4232 0.3785 0.1546  -0.0658 -0.0102 356 TYR A CD1 
2514 C CD2 . TYR A 354 ? 0.5023 0.4621 0.4062 0.2051  -0.0602 -0.0149 356 TYR A CD2 
2515 C CE1 . TYR A 354 ? 0.4641 0.3858 0.3671 0.1455  -0.0675 -0.0156 356 TYR A CE1 
2516 C CE2 . TYR A 354 ? 0.5269 0.4213 0.3948 0.1946  -0.0630 -0.0209 356 TYR A CE2 
2517 C CZ  . TYR A 354 ? 0.5094 0.3886 0.3790 0.1633  -0.0667 -0.0207 356 TYR A CZ  
2518 O OH  . TYR A 354 ? 0.5351 0.3576 0.3709 0.1497  -0.0697 -0.0250 356 TYR A OH  
2519 N N   . SER A 355 ? 0.3717 0.5455 0.3998 0.1549  -0.0748 0.0194  357 SER A N   
2520 C CA  . SER A 355 ? 0.3389 0.5718 0.3951 0.1387  -0.0773 0.0277  357 SER A CA  
2521 C C   . SER A 355 ? 0.2946 0.5196 0.3560 0.1058  -0.0742 0.0235  357 SER A C   
2522 O O   . SER A 355 ? 0.2714 0.4530 0.3180 0.0904  -0.0753 0.0185  357 SER A O   
2523 C CB  . SER A 355 ? 0.3545 0.6013 0.4120 0.1365  -0.0882 0.0367  357 SER A CB  
2524 O OG  . SER A 355 ? 0.3525 0.6601 0.4348 0.1204  -0.0919 0.0458  357 SER A OG  
2525 N N   . GLU A 356 ? 0.2682 0.5359 0.3488 0.0961  -0.0701 0.0262  358 GLU A N   
2526 C CA  . GLU A 356 ? 0.2505 0.5081 0.3319 0.0679  -0.0671 0.0228  358 GLU A CA  
2527 C C   . GLU A 356 ? 0.2403 0.4873 0.3158 0.0430  -0.0752 0.0263  358 GLU A C   
2528 O O   . GLU A 356 ? 0.2372 0.5183 0.3210 0.0372  -0.0829 0.0353  358 GLU A O   
2529 C CB  . GLU A 356 ? 0.2458 0.5518 0.3455 0.0616  -0.0624 0.0270  358 GLU A CB  
2530 C CG  . GLU A 356 ? 0.2382 0.5335 0.3346 0.0319  -0.0607 0.0253  358 GLU A CG  
2531 C CD  . GLU A 356 ? 0.2387 0.5808 0.3499 0.0229  -0.0568 0.0308  358 GLU A CD  
2532 O OE1 . GLU A 356 ? 0.2508 0.6369 0.3772 0.0417  -0.0536 0.0350  358 GLU A OE1 
2533 O OE2 . GLU A 356 ? 0.2276 0.5619 0.3328 -0.0023 -0.0567 0.0314  358 GLU A OE2 
2534 N N   . VAL A 357 ? 0.2411 0.4417 0.3004 0.0295  -0.0732 0.0193  359 VAL A N   
2535 C CA  . VAL A 357 ? 0.2365 0.4186 0.2842 0.0072  -0.0786 0.0207  359 VAL A CA  
2536 C C   . VAL A 357 ? 0.2419 0.4170 0.2846 -0.0142 -0.0749 0.0187  359 VAL A C   
2537 O O   . VAL A 357 ? 0.2659 0.4453 0.3018 -0.0345 -0.0806 0.0233  359 VAL A O   
2538 C CB  . VAL A 357 ? 0.2396 0.3755 0.2688 0.0102  -0.0794 0.0157  359 VAL A CB  
2539 C CG1 . VAL A 357 ? 0.2568 0.3953 0.2843 0.0269  -0.0859 0.0199  359 VAL A CG1 
2540 C CG2 . VAL A 357 ? 0.2327 0.3363 0.2543 0.0161  -0.0710 0.0070  359 VAL A CG2 
2541 N N   . ARG A 358 ? 0.2342 0.3955 0.2765 -0.0103 -0.0663 0.0123  360 ARG A N   
2542 C CA  . ARG A 358 ? 0.2533 0.4047 0.2876 -0.0276 -0.0629 0.0110  360 ARG A CA  
2543 C C   . ARG A 358 ? 0.2297 0.3956 0.2745 -0.0199 -0.0553 0.0086  360 ARG A C   
2544 O O   . ARG A 358 ? 0.2036 0.3678 0.2542 -0.0014 -0.0509 0.0042  360 ARG A O   
2545 C CB  . ARG A 358 ? 0.2862 0.3919 0.3002 -0.0329 -0.0598 0.0048  360 ARG A CB  
2546 C CG  . ARG A 358 ? 0.3414 0.4258 0.3402 -0.0399 -0.0655 0.0058  360 ARG A CG  
2547 C CD  . ARG A 358 ? 0.3785 0.4689 0.3668 -0.0602 -0.0735 0.0120  360 ARG A CD  
2548 N NE  . ARG A 358 ? 0.4324 0.4929 0.3964 -0.0758 -0.0717 0.0101  360 ARG A NE  
2549 C CZ  . ARG A 358 ? 0.4673 0.5141 0.4092 -0.0959 -0.0785 0.0136  360 ARG A CZ  
2550 N NH1 . ARG A 358 ? 0.4794 0.5490 0.4254 -0.1054 -0.0884 0.0204  360 ARG A NH1 
2551 N NH2 . ARG A 358 ? 0.4840 0.4923 0.3962 -0.1060 -0.0759 0.0107  360 ARG A NH2 
2552 N N   . LYS A 359 ? 0.2318 0.4086 0.2747 -0.0356 -0.0543 0.0117  361 LYS A N   
2553 C CA  . LYS A 359 ? 0.2313 0.4160 0.2793 -0.0318 -0.0470 0.0094  361 LYS A CA  
2554 C C   . LYS A 359 ? 0.2404 0.3936 0.2683 -0.0478 -0.0450 0.0077  361 LYS A C   
2555 O O   . LYS A 359 ? 0.2565 0.3987 0.2689 -0.0670 -0.0502 0.0117  361 LYS A O   
2556 C CB  . LYS A 359 ? 0.2379 0.4747 0.3035 -0.0336 -0.0471 0.0169  361 LYS A CB  
2557 C CG  . LYS A 359 ? 0.2527 0.4993 0.3225 -0.0293 -0.0390 0.0149  361 LYS A CG  
2558 C CD  . LYS A 359 ? 0.2757 0.5754 0.3600 -0.0360 -0.0380 0.0234  361 LYS A CD  
2559 C CE  . LYS A 359 ? 0.2981 0.6418 0.4033 -0.0119 -0.0355 0.0255  361 LYS A CE  
2560 N NZ  . LYS A 359 ? 0.3186 0.6915 0.4336 -0.0122 -0.0436 0.0330  361 LYS A NZ  
2561 N N   . ILE A 360 ? 0.2244 0.3606 0.2492 -0.0392 -0.0381 0.0020  362 ILE A N   
2562 C CA  . ILE A 360 ? 0.2324 0.3431 0.2382 -0.0499 -0.0355 0.0014  362 ILE A CA  
2563 C C   . ILE A 360 ? 0.2224 0.3534 0.2358 -0.0490 -0.0306 0.0026  362 ILE A C   
2564 O O   . ILE A 360 ? 0.1900 0.3267 0.2135 -0.0335 -0.0255 -0.0018 362 ILE A O   
2565 C CB  . ILE A 360 ? 0.2388 0.3117 0.2309 -0.0411 -0.0322 -0.0049 362 ILE A CB  
2566 C CG1 . ILE A 360 ? 0.2492 0.3045 0.2325 -0.0429 -0.0364 -0.0054 362 ILE A CG1 
2567 C CG2 . ILE A 360 ? 0.2549 0.3012 0.2252 -0.0469 -0.0291 -0.0050 362 ILE A CG2 
2568 C CD1 . ILE A 360 ? 0.2501 0.2769 0.2218 -0.0338 -0.0324 -0.0104 362 ILE A CD1 
2569 N N   . GLU A 361 ? 0.2459 0.3875 0.2517 -0.0680 -0.0327 0.0092  363 GLU A N   
2570 C CA  . GLU A 361 ? 0.2525 0.4172 0.2640 -0.0706 -0.0282 0.0120  363 GLU A CA  
2571 C C   . GLU A 361 ? 0.2296 0.3604 0.2254 -0.0652 -0.0231 0.0072  363 GLU A C   
2572 O O   . GLU A 361 ? 0.2196 0.3110 0.1970 -0.0632 -0.0236 0.0036  363 GLU A O   
2573 C CB  . GLU A 361 ? 0.3091 0.4913 0.3121 -0.0975 -0.0329 0.0217  363 GLU A CB  
2574 C CG  . GLU A 361 ? 0.3502 0.5781 0.3720 -0.1037 -0.0386 0.0287  363 GLU A CG  
2575 C CD  . GLU A 361 ? 0.3811 0.6671 0.4337 -0.0880 -0.0339 0.0312  363 GLU A CD  
2576 O OE1 . GLU A 361 ? 0.4106 0.6979 0.4690 -0.0715 -0.0258 0.0262  363 GLU A OE1 
2577 O OE2 . GLU A 361 ? 0.4303 0.7610 0.4995 -0.0909 -0.0384 0.0384  363 GLU A OE2 
2578 N N   . ALA A 362 ? 0.2094 0.3587 0.2122 -0.0611 -0.0178 0.0075  364 ALA A N   
2579 C CA  . ALA A 362 ? 0.2071 0.3298 0.1965 -0.0550 -0.0135 0.0038  364 ALA A CA  
2580 C C   . ALA A 362 ? 0.2325 0.3201 0.1905 -0.0723 -0.0160 0.0081  364 ALA A C   
2581 O O   . ALA A 362 ? 0.2546 0.3492 0.2031 -0.0935 -0.0197 0.0152  364 ALA A O   
2582 C CB  . ALA A 362 ? 0.1909 0.3416 0.1927 -0.0478 -0.0077 0.0035  364 ALA A CB  
2583 N N   . SER A 363 ? 0.2392 0.2890 0.1788 -0.0631 -0.0144 0.0043  365 SER A N   
2584 C CA  . SER A 363 ? 0.2727 0.2801 0.1756 -0.0739 -0.0162 0.0078  365 SER A CA  
2585 C C   . SER A 363 ? 0.2748 0.2618 0.1681 -0.0568 -0.0119 0.0046  365 SER A C   
2586 O O   . SER A 363 ? 0.2546 0.2656 0.1701 -0.0432 -0.0082 0.0010  365 SER A O   
2587 C CB  . SER A 363 ? 0.2899 0.2637 0.1705 -0.0803 -0.0209 0.0078  365 SER A CB  
2588 O OG  . SER A 363 ? 0.2818 0.2446 0.1678 -0.0602 -0.0187 0.0015  365 SER A OG  
2589 N N   . SER A 364 ? 0.3059 0.2470 0.1629 -0.0571 -0.0128 0.0063  366 SER A N   
2590 C CA  . SER A 364 ? 0.3083 0.2307 0.1544 -0.0377 -0.0093 0.0044  366 SER A CA  
2591 C C   . SER A 364 ? 0.2851 0.2089 0.1427 -0.0180 -0.0075 -0.0009 366 SER A C   
2592 O O   . SER A 364 ? 0.2900 0.2095 0.1447 -0.0003 -0.0047 -0.0020 366 SER A O   
2593 C CB  . SER A 364 ? 0.3542 0.2254 0.1536 -0.0421 -0.0108 0.0088  366 SER A CB  
2594 O OG  . SER A 364 ? 0.3817 0.2171 0.1535 -0.0508 -0.0144 0.0092  366 SER A OG  
2595 N N   . SER A 365 ? 0.2616 0.1949 0.1322 -0.0217 -0.0093 -0.0032 367 SER A N   
2596 C CA  . SER A 365 ? 0.2420 0.1783 0.1224 -0.0063 -0.0076 -0.0073 367 SER A CA  
2597 C C   . SER A 365 ? 0.1952 0.1689 0.1090 0.0035  -0.0055 -0.0107 367 SER A C   
2598 O O   . SER A 365 ? 0.1714 0.1709 0.1055 -0.0025 -0.0062 -0.0115 367 SER A O   
2599 C CB  . SER A 365 ? 0.2472 0.1794 0.1278 -0.0147 -0.0106 -0.0082 367 SER A CB  
2600 O OG  . SER A 365 ? 0.2529 0.1787 0.1324 -0.0003 -0.0082 -0.0112 367 SER A OG  
2601 N N   . SER A 366 ? 0.1854 0.1614 0.1019 0.0186  -0.0031 -0.0124 368 SER A N   
2602 C CA  . SER A 366 ? 0.1552 0.1618 0.0980 0.0242  -0.0026 -0.0154 368 SER A CA  
2603 C C   . SER A 366 ? 0.1459 0.1580 0.0977 0.0257  -0.0031 -0.0174 368 SER A C   
2604 O O   . SER A 366 ? 0.1272 0.1598 0.0953 0.0284  -0.0033 -0.0192 368 SER A O   
2605 C CB  . SER A 366 ? 0.1565 0.1706 0.0977 0.0365  -0.0006 -0.0141 368 SER A CB  
2606 O OG  . SER A 366 ? 0.1698 0.1707 0.0951 0.0493  0.0018  -0.0120 368 SER A OG  
2607 N N   . THR A 367 ? 0.1638 0.1557 0.1016 0.0221  -0.0037 -0.0168 369 THR A N   
2608 C CA  . THR A 367 ? 0.1607 0.1554 0.1039 0.0224  -0.0041 -0.0183 369 THR A CA  
2609 C C   . THR A 367 ? 0.1662 0.1544 0.1094 0.0094  -0.0084 -0.0184 369 THR A C   
2610 O O   . THR A 367 ? 0.1880 0.1609 0.1168 0.0006  -0.0104 -0.0163 369 THR A O   
2611 C CB  . THR A 367 ? 0.1874 0.1653 0.1107 0.0337  -0.0002 -0.0172 369 THR A CB  
2612 O OG1 . THR A 367 ? 0.1882 0.1805 0.1144 0.0472  0.0033  -0.0157 369 THR A OG1 
2613 C CG2 . THR A 367 ? 0.1849 0.1668 0.1120 0.0335  0.0001  -0.0182 369 THR A CG2 
2614 N N   . PHE A 368 ? 0.1494 0.1501 0.1072 0.0073  -0.0106 -0.0199 370 PHE A N   
2615 C CA  . PHE A 368 ? 0.1550 0.1571 0.1169 -0.0025 -0.0154 -0.0192 370 PHE A CA  
2616 C C   . PHE A 368 ? 0.1601 0.1548 0.1181 -0.0022 -0.0164 -0.0198 370 PHE A C   
2617 O O   . PHE A 368 ? 0.1523 0.1575 0.1211 0.0018  -0.0158 -0.0211 370 PHE A O   
2618 C CB  . PHE A 368 ? 0.1360 0.1617 0.1192 -0.0030 -0.0175 -0.0201 370 PHE A CB  
2619 C CG  . PHE A 368 ? 0.1354 0.1714 0.1228 -0.0022 -0.0154 -0.0199 370 PHE A CG  
2620 C CD1 . PHE A 368 ? 0.1300 0.1690 0.1192 0.0051  -0.0121 -0.0218 370 PHE A CD1 
2621 C CD2 . PHE A 368 ? 0.1412 0.1866 0.1300 -0.0103 -0.0171 -0.0169 370 PHE A CD2 
2622 C CE1 . PHE A 368 ? 0.1322 0.1791 0.1229 0.0055  -0.0103 -0.0214 370 PHE A CE1 
2623 C CE2 . PHE A 368 ? 0.1413 0.1969 0.1323 -0.0105 -0.0145 -0.0161 370 PHE A CE2 
2624 C CZ  . PHE A 368 ? 0.1357 0.1895 0.1266 -0.0020 -0.0110 -0.0187 370 PHE A CZ  
2625 N N   . ASP A 369 ? 0.1883 0.1632 0.1279 -0.0087 -0.0185 -0.0184 371 ASP A N   
2626 C CA  . ASP A 369 ? 0.2119 0.1769 0.1434 -0.0092 -0.0193 -0.0186 371 ASP A CA  
2627 C C   . ASP A 369 ? 0.2009 0.1716 0.1382 -0.0200 -0.0267 -0.0167 371 ASP A C   
2628 O O   . ASP A 369 ? 0.2094 0.1726 0.1358 -0.0309 -0.0309 -0.0143 371 ASP A O   
2629 C CB  . ASP A 369 ? 0.2568 0.1908 0.1570 -0.0068 -0.0162 -0.0187 371 ASP A CB  
2630 C CG  . ASP A 369 ? 0.2855 0.2188 0.1803 0.0090  -0.0083 -0.0196 371 ASP A CG  
2631 O OD1 . ASP A 369 ? 0.2916 0.2508 0.2083 0.0143  -0.0064 -0.0199 371 ASP A OD1 
2632 O OD2 . ASP A 369 ? 0.3345 0.2411 0.2009 0.0165  -0.0045 -0.0197 371 ASP A OD2 
2633 N N   . PHE A 370 ? 0.1826 0.1663 0.1346 -0.0174 -0.0287 -0.0171 372 PHE A N   
2634 C CA  . PHE A 370 ? 0.1876 0.1758 0.1429 -0.0236 -0.0357 -0.0147 372 PHE A CA  
2635 C C   . PHE A 370 ? 0.1967 0.1659 0.1346 -0.0259 -0.0358 -0.0147 372 PHE A C   
2636 O O   . PHE A 370 ? 0.1940 0.1639 0.1349 -0.0218 -0.0347 -0.0153 372 PHE A O   
2637 C CB  . PHE A 370 ? 0.1809 0.1866 0.1552 -0.0172 -0.0379 -0.0149 372 PHE A CB  
2638 C CG  . PHE A 370 ? 0.1756 0.2008 0.1646 -0.0136 -0.0375 -0.0149 372 PHE A CG  
2639 C CD1 . PHE A 370 ? 0.1819 0.2254 0.1780 -0.0179 -0.0420 -0.0111 372 PHE A CD1 
2640 C CD2 . PHE A 370 ? 0.1758 0.2043 0.1707 -0.0068 -0.0325 -0.0182 372 PHE A CD2 
2641 C CE1 . PHE A 370 ? 0.1787 0.2443 0.1881 -0.0137 -0.0402 -0.0106 372 PHE A CE1 
2642 C CE2 . PHE A 370 ? 0.1641 0.2093 0.1697 -0.0031 -0.0314 -0.0184 372 PHE A CE2 
2643 C CZ  . PHE A 370 ? 0.1683 0.2324 0.1815 -0.0055 -0.0347 -0.0148 372 PHE A CZ  
2644 N N   . TYR A 371 ? 0.2161 0.1654 0.1318 -0.0334 -0.0371 -0.0139 373 TYR A N   
2645 C CA  . TYR A 371 ? 0.2386 0.1652 0.1316 -0.0338 -0.0356 -0.0146 373 TYR A CA  
2646 C C   . TYR A 371 ? 0.2381 0.1679 0.1319 -0.0422 -0.0439 -0.0117 373 TYR A C   
2647 O O   . TYR A 371 ? 0.2459 0.1794 0.1380 -0.0533 -0.0516 -0.0086 373 TYR A O   
2648 C CB  . TYR A 371 ? 0.2702 0.1664 0.1319 -0.0367 -0.0333 -0.0157 373 TYR A CB  
2649 C CG  . TYR A 371 ? 0.3020 0.1709 0.1347 -0.0299 -0.0275 -0.0179 373 TYR A CG  
2650 C CD1 . TYR A 371 ? 0.3208 0.1750 0.1363 -0.0377 -0.0318 -0.0172 373 TYR A CD1 
2651 C CD2 . TYR A 371 ? 0.3106 0.1698 0.1313 -0.0144 -0.0177 -0.0202 373 TYR A CD2 
2652 C CE1 . TYR A 371 ? 0.3502 0.1782 0.1356 -0.0305 -0.0257 -0.0195 373 TYR A CE1 
2653 C CE2 . TYR A 371 ? 0.3410 0.1772 0.1329 -0.0050 -0.0113 -0.0219 373 TYR A CE2 
2654 C CZ  . TYR A 371 ? 0.3632 0.1832 0.1371 -0.0130 -0.0148 -0.0219 373 TYR A CZ  
2655 O OH  . TYR A 371 ? 0.3919 0.1898 0.1357 -0.0029 -0.0077 -0.0237 373 TYR A OH  
2656 N N   . GLY A 372 ? 0.2286 0.1583 0.1237 -0.0380 -0.0426 -0.0119 374 GLY A N   
2657 C CA  . GLY A 372 ? 0.2350 0.1645 0.1278 -0.0442 -0.0505 -0.0088 374 GLY A CA  
2658 C C   . GLY A 372 ? 0.2170 0.1675 0.1332 -0.0395 -0.0551 -0.0066 374 GLY A C   
2659 O O   . GLY A 372 ? 0.2143 0.1804 0.1412 -0.0415 -0.0624 -0.0033 374 GLY A O   
2660 N N   . ILE A 373 ? 0.2150 0.1660 0.1369 -0.0328 -0.0507 -0.0081 375 ILE A N   
2661 C CA  . ILE A 373 ? 0.2073 0.1663 0.1418 -0.0273 -0.0546 -0.0069 375 ILE A CA  
2662 C C   . ILE A 373 ? 0.2185 0.1633 0.1407 -0.0297 -0.0556 -0.0052 375 ILE A C   
2663 O O   . ILE A 373 ? 0.2203 0.1570 0.1306 -0.0337 -0.0501 -0.0058 375 ILE A O   
2664 C CB  . ILE A 373 ? 0.1944 0.1632 0.1426 -0.0206 -0.0496 -0.0100 375 ILE A CB  
2665 C CG1 . ILE A 373 ? 0.1942 0.1651 0.1493 -0.0132 -0.0544 -0.0093 375 ILE A CG1 
2666 C CG2 . ILE A 373 ? 0.1947 0.1595 0.1380 -0.0216 -0.0419 -0.0122 375 ILE A CG2 
2667 C CD1 . ILE A 373 ? 0.1852 0.1654 0.1517 -0.0064 -0.0507 -0.0127 375 ILE A CD1 
2668 N N   . LYS A 374 ? 0.2268 0.1685 0.1497 -0.0261 -0.0627 -0.0024 376 LYS A N   
2669 C CA  . LYS A 374 ? 0.2447 0.1689 0.1521 -0.0298 -0.0655 0.0003  376 LYS A CA  
2670 C C   . LYS A 374 ? 0.2513 0.1648 0.1566 -0.0251 -0.0674 0.0003  376 LYS A C   
2671 O O   . LYS A 374 ? 0.2379 0.1577 0.1535 -0.0180 -0.0661 -0.0023 376 LYS A O   
2672 C CB  . LYS A 374 ? 0.2584 0.1794 0.1583 -0.0309 -0.0745 0.0049  376 LYS A CB  
2673 C CG  . LYS A 374 ? 0.2586 0.1910 0.1691 -0.0200 -0.0826 0.0079  376 LYS A CG  
2674 C CD  . LYS A 374 ? 0.2729 0.2078 0.1766 -0.0214 -0.0923 0.0139  376 LYS A CD  
2675 C CE  . LYS A 374 ? 0.2778 0.2296 0.1924 -0.0066 -0.1001 0.0183  376 LYS A CE  
2676 N NZ  . LYS A 374 ? 0.2938 0.2514 0.2017 -0.0079 -0.1105 0.0254  376 LYS A NZ  
2677 N N   . ALA A 375 ? 0.2733 0.1663 0.1605 -0.0300 -0.0709 0.0036  377 ALA A N   
2678 C CA  . ALA A 375 ? 0.2902 0.1619 0.1653 -0.0275 -0.0747 0.0043  377 ALA A CA  
2679 C C   . ALA A 375 ? 0.2952 0.1650 0.1734 -0.0104 -0.0817 0.0051  377 ALA A C   
2680 O O   . ALA A 375 ? 0.2947 0.1745 0.1771 -0.0046 -0.0870 0.0086  377 ALA A O   
2681 C CB  . ALA A 375 ? 0.3208 0.1682 0.1717 -0.0382 -0.0777 0.0088  377 ALA A CB  
2682 N N   . GLY A 376 ? 0.3024 0.1603 0.1764 -0.0023 -0.0818 0.0024  378 GLY A N   
2683 C CA  . GLY A 376 ? 0.3148 0.1708 0.1890 0.0181  -0.0868 0.0029  378 GLY A CA  
2684 C C   . GLY A 376 ? 0.3176 0.1675 0.1913 0.0251  -0.0829 -0.0025 378 GLY A C   
2685 O O   . GLY A 376 ? 0.3056 0.1533 0.1792 0.0117  -0.0778 -0.0059 378 GLY A O   
2686 N N   . ASP A 377 ? 0.3372 0.1860 0.2092 0.0470  -0.0854 -0.0028 379 ASP A N   
2687 C CA  . ASP A 377 ? 0.3488 0.1902 0.2170 0.0565  -0.0817 -0.0084 379 ASP A CA  
2688 C C   . ASP A 377 ? 0.3098 0.1966 0.2097 0.0650  -0.0765 -0.0098 379 ASP A C   
2689 O O   . ASP A 377 ? 0.2996 0.2157 0.2154 0.0752  -0.0787 -0.0054 379 ASP A O   
2690 C CB  . ASP A 377 ? 0.4063 0.2104 0.2443 0.0781  -0.0867 -0.0083 379 ASP A CB  
2691 C CG  . ASP A 377 ? 0.4576 0.2100 0.2579 0.0686  -0.0932 -0.0059 379 ASP A CG  
2692 O OD1 . ASP A 377 ? 0.4662 0.2024 0.2563 0.0445  -0.0918 -0.0075 379 ASP A OD1 
2693 O OD2 . ASP A 377 ? 0.5046 0.2333 0.2837 0.0860  -0.0997 -0.0019 379 ASP A OD2 
2694 N N   . TYR A 378 ? 0.2874 0.1813 0.1951 0.0590  -0.0701 -0.0151 380 TYR A N   
2695 C CA  . TYR A 378 ? 0.2543 0.1891 0.1899 0.0616  -0.0647 -0.0161 380 TYR A CA  
2696 C C   . TYR A 378 ? 0.2618 0.1926 0.1933 0.0728  -0.0603 -0.0215 380 TYR A C   
2697 O O   . TYR A 378 ? 0.2833 0.1778 0.1898 0.0729  -0.0612 -0.0253 380 TYR A O   
2698 C CB  . TYR A 378 ? 0.2238 0.1729 0.1730 0.0408  -0.0607 -0.0166 380 TYR A CB  
2699 C CG  . TYR A 378 ? 0.2184 0.1720 0.1697 0.0306  -0.0640 -0.0119 380 TYR A CG  
2700 C CD1 . TYR A 378 ? 0.2074 0.1889 0.1740 0.0316  -0.0659 -0.0079 380 TYR A CD1 
2701 C CD2 . TYR A 378 ? 0.2298 0.1605 0.1657 0.0185  -0.0655 -0.0109 380 TYR A CD2 
2702 C CE1 . TYR A 378 ? 0.2050 0.1871 0.1691 0.0213  -0.0696 -0.0040 380 TYR A CE1 
2703 C CE2 . TYR A 378 ? 0.2289 0.1622 0.1638 0.0102  -0.0679 -0.0070 380 TYR A CE2 
2704 C CZ  . TYR A 378 ? 0.2217 0.1782 0.1693 0.0120  -0.0703 -0.0040 380 TYR A CZ  
2705 O OH  . TYR A 378 ? 0.2298 0.1851 0.1720 0.0025  -0.0735 -0.0004 380 TYR A OH  
2706 N N   . LYS A 379 ? 0.2501 0.2178 0.2036 0.0804  -0.0559 -0.0213 381 LYS A N   
2707 C CA  . LYS A 379 ? 0.2579 0.2287 0.2112 0.0873  -0.0502 -0.0265 381 LYS A CA  
2708 C C   . LYS A 379 ? 0.2219 0.2294 0.2009 0.0760  -0.0450 -0.0259 381 LYS A C   
2709 O O   . LYS A 379 ? 0.2028 0.2429 0.2005 0.0747  -0.0455 -0.0209 381 LYS A O   
2710 C CB  . LYS A 379 ? 0.2896 0.2660 0.2371 0.1148  -0.0493 -0.0265 381 LYS A CB  
2711 C CG  . LYS A 379 ? 0.3115 0.2819 0.2504 0.1241  -0.0432 -0.0327 381 LYS A CG  
2712 C CD  . LYS A 379 ? 0.3623 0.3218 0.2824 0.1547  -0.0421 -0.0341 381 LYS A CD  
2713 C CE  . LYS A 379 ? 0.3605 0.3749 0.3066 0.1725  -0.0395 -0.0276 381 LYS A CE  
2714 N NZ  . LYS A 379 ? 0.4080 0.4113 0.3328 0.2077  -0.0383 -0.0280 381 LYS A NZ  
2715 N N   . LEU A 380 ? 0.2109 0.2115 0.1877 0.0677  -0.0409 -0.0305 382 LEU A N   
2716 C CA  . LEU A 380 ? 0.1900 0.2175 0.1850 0.0586  -0.0360 -0.0302 382 LEU A CA  
2717 C C   . LEU A 380 ? 0.1857 0.2255 0.1824 0.0703  -0.0309 -0.0332 382 LEU A C   
2718 O O   . LEU A 380 ? 0.1988 0.2154 0.1788 0.0744  -0.0299 -0.0384 382 LEU A O   
2719 C CB  . LEU A 380 ? 0.1944 0.2078 0.1850 0.0422  -0.0352 -0.0321 382 LEU A CB  
2720 C CG  . LEU A 380 ? 0.1969 0.2297 0.2003 0.0338  -0.0305 -0.0317 382 LEU A CG  
2721 C CD1 . LEU A 380 ? 0.1795 0.2272 0.1927 0.0268  -0.0313 -0.0269 382 LEU A CD1 
2722 C CD2 . LEU A 380 ? 0.2135 0.2352 0.2106 0.0239  -0.0293 -0.0336 382 LEU A CD2 
2723 N N   . VAL A 381 ? 0.1679 0.2441 0.1822 0.0742  -0.0281 -0.0294 383 VAL A N   
2724 C CA  . VAL A 381 ? 0.1704 0.2658 0.1884 0.0846  -0.0221 -0.0310 383 VAL A CA  
2725 C C   . VAL A 381 ? 0.1506 0.2620 0.1795 0.0689  -0.0184 -0.0300 383 VAL A C   
2726 O O   . VAL A 381 ? 0.1281 0.2537 0.1674 0.0556  -0.0201 -0.0251 383 VAL A O   
2727 C CB  . VAL A 381 ? 0.1717 0.3029 0.2012 0.1009  -0.0211 -0.0258 383 VAL A CB  
2728 C CG1 . VAL A 381 ? 0.1715 0.3312 0.2071 0.1108  -0.0136 -0.0262 383 VAL A CG1 
2729 C CG2 . VAL A 381 ? 0.1991 0.3117 0.2140 0.1214  -0.0247 -0.0263 383 VAL A CG2 
2730 N N   . GLU A 382 ? 0.1562 0.2619 0.1786 0.0707  -0.0139 -0.0345 384 GLU A N   
2731 C CA  . GLU A 382 ? 0.1485 0.2704 0.1786 0.0597  -0.0101 -0.0329 384 GLU A CA  
2732 C C   . GLU A 382 ? 0.1461 0.3063 0.1881 0.0655  -0.0056 -0.0285 384 GLU A C   
2733 O O   . GLU A 382 ? 0.1535 0.3217 0.1915 0.0780  -0.0005 -0.0313 384 GLU A O   
2734 C CB  . GLU A 382 ? 0.1587 0.2610 0.1765 0.0585  -0.0080 -0.0386 384 GLU A CB  
2735 C CG  . GLU A 382 ? 0.1558 0.2697 0.1786 0.0475  -0.0049 -0.0362 384 GLU A CG  
2736 C CD  . GLU A 382 ? 0.1644 0.2633 0.1761 0.0460  -0.0039 -0.0406 384 GLU A CD  
2737 O OE1 . GLU A 382 ? 0.1849 0.2761 0.1862 0.0552  -0.0026 -0.0453 384 GLU A OE1 
2738 O OE2 . GLU A 382 ? 0.1672 0.2618 0.1786 0.0365  -0.0047 -0.0390 384 GLU A OE2 
2739 N N   . SER A 383 ? 0.1365 0.3216 0.1914 0.0553  -0.0078 -0.0213 385 SER A N   
2740 C CA  . SER A 383 ? 0.1360 0.3662 0.2046 0.0576  -0.0050 -0.0147 385 SER A CA  
2741 C C   . SER A 383 ? 0.1288 0.3749 0.1986 0.0461  0.0000  -0.0123 385 SER A C   
2742 O O   . SER A 383 ? 0.1239 0.4085 0.2027 0.0502  0.0045  -0.0080 385 SER A O   
2743 C CB  . SER A 383 ? 0.1400 0.3892 0.2186 0.0473  -0.0112 -0.0072 385 SER A CB  
2744 O OG  . SER A 383 ? 0.1411 0.3704 0.2136 0.0250  -0.0150 -0.0056 385 SER A OG  
2745 N N   . THR A 384 ? 0.1257 0.3438 0.1855 0.0326  -0.0006 -0.0145 386 THR A N   
2746 C CA  . THR A 384 ? 0.1308 0.3530 0.1857 0.0250  0.0039  -0.0137 386 THR A CA  
2747 C C   . THR A 384 ? 0.1334 0.3208 0.1753 0.0289  0.0046  -0.0209 386 THR A C   
2748 O O   . THR A 384 ? 0.1250 0.2855 0.1612 0.0247  0.0005  -0.0229 386 THR A O   
2749 C CB  . THR A 384 ? 0.1348 0.3594 0.1862 0.0019  0.0014  -0.0063 386 THR A CB  
2750 O OG1 . THR A 384 ? 0.1412 0.4014 0.2043 -0.0057 -0.0007 0.0014  386 THR A OG1 
2751 C CG2 . THR A 384 ? 0.1420 0.3689 0.1850 -0.0062 0.0059  -0.0043 386 THR A CG2 
2752 N N   . THR A 385 ? 0.1381 0.3294 0.1751 0.0370  0.0098  -0.0242 387 THR A N   
2753 C CA  . THR A 385 ? 0.1504 0.3142 0.1748 0.0395  0.0096  -0.0303 387 THR A CA  
2754 C C   . THR A 385 ? 0.1544 0.3167 0.1727 0.0279  0.0111  -0.0269 387 THR A C   
2755 O O   . THR A 385 ? 0.1678 0.3521 0.1879 0.0235  0.0152  -0.0224 387 THR A O   
2756 C CB  . THR A 385 ? 0.1651 0.3268 0.1811 0.0554  0.0133  -0.0368 387 THR A CB  
2757 O OG1 . THR A 385 ? 0.1735 0.3340 0.1911 0.0680  0.0119  -0.0388 387 THR A OG1 
2758 C CG2 . THR A 385 ? 0.1729 0.3063 0.1740 0.0546  0.0110  -0.0426 387 THR A CG2 
2759 N N   . PRO A 386 ? 0.1485 0.2871 0.1585 0.0233  0.0079  -0.0279 388 PRO A N   
2760 C CA  . PRO A 386 ? 0.1557 0.2887 0.1559 0.0161  0.0090  -0.0244 388 PRO A CA  
2761 C C   . PRO A 386 ? 0.1662 0.3094 0.1613 0.0207  0.0134  -0.0264 388 PRO A C   
2762 O O   . PRO A 386 ? 0.1696 0.3117 0.1631 0.0306  0.0143  -0.0326 388 PRO A O   
2763 C CB  . PRO A 386 ? 0.1568 0.2680 0.1506 0.0171  0.0051  -0.0258 388 PRO A CB  
2764 C CG  . PRO A 386 ? 0.1463 0.2522 0.1478 0.0191  0.0018  -0.0280 388 PRO A CG  
2765 C CD  . PRO A 386 ? 0.1472 0.2660 0.1560 0.0254  0.0034  -0.0313 388 PRO A CD  
2766 N N   . ALA A 387 ? 0.1759 0.3244 0.1639 0.0126  0.0160  -0.0211 389 ALA A N   
2767 C CA  . ALA A 387 ? 0.1896 0.3486 0.1709 0.0158  0.0207  -0.0222 389 ALA A CA  
2768 C C   . ALA A 387 ? 0.1969 0.3387 0.1691 0.0231  0.0183  -0.0281 389 ALA A C   
2769 O O   . ALA A 387 ? 0.2148 0.3403 0.1827 0.0209  0.0135  -0.0270 389 ALA A O   
2770 C CB  . ALA A 387 ? 0.1973 0.3588 0.1684 0.0029  0.0225  -0.0144 389 ALA A CB  
2771 N N   . GLY A 388 ? 0.1893 0.3362 0.1565 0.0319  0.0215  -0.0339 390 GLY A N   
2772 C CA  . GLY A 388 ? 0.1951 0.3275 0.1488 0.0351  0.0189  -0.0389 390 GLY A CA  
2773 C C   . GLY A 388 ? 0.1902 0.3058 0.1428 0.0381  0.0130  -0.0447 390 GLY A C   
2774 O O   . GLY A 388 ? 0.2041 0.3087 0.1467 0.0355  0.0082  -0.0469 390 GLY A O   
2775 N N   . TYR A 389 ? 0.1731 0.2878 0.1344 0.0421  0.0128  -0.0464 391 TYR A N   
2776 C CA  . TYR A 389 ? 0.1721 0.2684 0.1291 0.0429  0.0071  -0.0512 391 TYR A CA  
2777 C C   . TYR A 389 ? 0.1816 0.2724 0.1346 0.0543  0.0095  -0.0560 391 TYR A C   
2778 O O   . TYR A 389 ? 0.1718 0.2817 0.1337 0.0614  0.0153  -0.0538 391 TYR A O   
2779 C CB  . TYR A 389 ? 0.1554 0.2511 0.1251 0.0360  0.0028  -0.0467 391 TYR A CB  
2780 C CG  . TYR A 389 ? 0.1460 0.2442 0.1162 0.0295  0.0001  -0.0419 391 TYR A CG  
2781 C CD1 . TYR A 389 ? 0.1522 0.2465 0.1146 0.0260  -0.0048 -0.0430 391 TYR A CD1 
2782 C CD2 . TYR A 389 ? 0.1371 0.2407 0.1127 0.0272  0.0020  -0.0357 391 TYR A CD2 
2783 C CE1 . TYR A 389 ? 0.1494 0.2510 0.1132 0.0239  -0.0071 -0.0374 391 TYR A CE1 
2784 C CE2 . TYR A 389 ? 0.1386 0.2402 0.1106 0.0257  -0.0001 -0.0311 391 TYR A CE2 
2785 C CZ  . TYR A 389 ? 0.1448 0.2483 0.1125 0.0259  -0.0043 -0.0317 391 TYR A CZ  
2786 O OH  . TYR A 389 ? 0.1525 0.2583 0.1172 0.0283  -0.0059 -0.0259 391 TYR A OH  
2787 N N   . ASN A 390 ? 0.2005 0.2656 0.1378 0.0556  0.0048  -0.0618 392 ASN A N   
2788 C CA  . ASN A 390 ? 0.2188 0.2687 0.1461 0.0680  0.0055  -0.0663 392 ASN A CA  
2789 C C   . ASN A 390 ? 0.2026 0.2628 0.1497 0.0681  0.0043  -0.0617 392 ASN A C   
2790 O O   . ASN A 390 ? 0.1805 0.2417 0.1387 0.0562  -0.0001 -0.0580 392 ASN A O   
2791 C CB  . ASN A 390 ? 0.2519 0.2632 0.1508 0.0648  -0.0010 -0.0728 392 ASN A CB  
2792 C CG  . ASN A 390 ? 0.2823 0.2785 0.1557 0.0632  -0.0012 -0.0779 392 ASN A CG  
2793 O OD1 . ASN A 390 ? 0.3095 0.2928 0.1713 0.0480  -0.0084 -0.0786 392 ASN A OD1 
2794 N ND2 . ASN A 390 ? 0.2843 0.2858 0.1489 0.0778  0.0065  -0.0809 392 ASN A ND2 
2795 N N   . THR A 391 ? 0.2143 0.2848 0.1651 0.0830  0.0086  -0.0616 393 THR A N   
2796 C CA  . THR A 391 ? 0.2095 0.2855 0.1736 0.0851  0.0062  -0.0580 393 THR A CA  
2797 C C   . THR A 391 ? 0.2299 0.2692 0.1773 0.0821  -0.0010 -0.0617 393 THR A C   
2798 O O   . THR A 391 ? 0.2625 0.2715 0.1833 0.0894  -0.0023 -0.0678 393 THR A O   
2799 C CB  . THR A 391 ? 0.2102 0.3088 0.1798 0.1041  0.0118  -0.0564 393 THR A CB  
2800 O OG1 . THR A 391 ? 0.1912 0.3274 0.1756 0.1020  0.0182  -0.0517 393 THR A OG1 
2801 C CG2 . THR A 391 ? 0.1992 0.3073 0.1828 0.1061  0.0083  -0.0517 393 THR A CG2 
2802 N N   . MET A 392 ? 0.2262 0.2661 0.1860 0.0705  -0.0057 -0.0577 394 MET A N   
2803 C CA  . MET A 392 ? 0.2483 0.2586 0.1946 0.0653  -0.0123 -0.0594 394 MET A CA  
2804 C C   . MET A 392 ? 0.2737 0.2661 0.2060 0.0823  -0.0129 -0.0615 394 MET A C   
2805 O O   . MET A 392 ? 0.2624 0.2778 0.2075 0.0962  -0.0091 -0.0587 394 MET A O   
2806 C CB  . MET A 392 ? 0.2344 0.2569 0.1996 0.0522  -0.0150 -0.0537 394 MET A CB  
2807 C CG  . MET A 392 ? 0.2529 0.2539 0.2096 0.0474  -0.0207 -0.0533 394 MET A CG  
2808 S SD  . MET A 392 ? 0.2234 0.2431 0.2021 0.0380  -0.0214 -0.0467 394 MET A SD  
2809 C CE  . MET A 392 ? 0.2282 0.2511 0.2111 0.0511  -0.0222 -0.0447 394 MET A CE  
2810 N N   . LYS A 393 ? 0.3086 0.2594 0.2116 0.0814  -0.0182 -0.0657 395 LYS A N   
2811 C CA  . LYS A 393 ? 0.3489 0.2744 0.2333 0.0978  -0.0202 -0.0670 395 LYS A CA  
2812 C C   . LYS A 393 ? 0.3155 0.2508 0.2173 0.0923  -0.0239 -0.0609 395 LYS A C   
2813 O O   . LYS A 393 ? 0.2911 0.2306 0.2034 0.0724  -0.0272 -0.0581 395 LYS A O   
2814 C CB  . LYS A 393 ? 0.4182 0.2872 0.2588 0.0947  -0.0260 -0.0728 395 LYS A CB  
2815 C CG  . LYS A 393 ? 0.4796 0.3282 0.2931 0.1004  -0.0235 -0.0798 395 LYS A CG  
2816 C CD  . LYS A 393 ? 0.5641 0.3478 0.3251 0.0998  -0.0299 -0.0857 395 LYS A CD  
2817 C CE  . LYS A 393 ? 0.6193 0.3785 0.3488 0.1010  -0.0285 -0.0931 395 LYS A CE  
2818 N NZ  . LYS A 393 ? 0.7081 0.3969 0.3804 0.0931  -0.0370 -0.0984 395 LYS A NZ  
2819 N N   . ASP A 394 ? 0.3158 0.2545 0.2181 0.1113  -0.0235 -0.0588 396 ASP A N   
2820 C CA  . ASP A 394 ? 0.2955 0.2433 0.2120 0.1075  -0.0276 -0.0529 396 ASP A CA  
2821 C C   . ASP A 394 ? 0.3007 0.2104 0.1977 0.0904  -0.0348 -0.0534 396 ASP A C   
2822 O O   . ASP A 394 ? 0.3280 0.1947 0.1912 0.0901  -0.0381 -0.0578 396 ASP A O   
2823 C CB  . ASP A 394 ? 0.3209 0.2738 0.2342 0.1332  -0.0275 -0.0504 396 ASP A CB  
2824 C CG  . ASP A 394 ? 0.3142 0.3165 0.2508 0.1487  -0.0203 -0.0476 396 ASP A CG  
2825 O OD1 . ASP A 394 ? 0.2932 0.3210 0.2464 0.1376  -0.0156 -0.0479 396 ASP A OD1 
2826 O OD2 . ASP A 394 ? 0.3456 0.3616 0.2819 0.1723  -0.0194 -0.0446 396 ASP A OD2 
2827 N N   . ILE A 395 ? 0.2745 0.1999 0.1904 0.0749  -0.0370 -0.0484 397 ILE A N   
2828 C CA  . ILE A 395 ? 0.2843 0.1830 0.1856 0.0574  -0.0428 -0.0473 397 ILE A CA  
2829 C C   . ILE A 395 ? 0.2935 0.1851 0.1932 0.0626  -0.0470 -0.0428 397 ILE A C   
2830 O O   . ILE A 395 ? 0.2630 0.1855 0.1873 0.0622  -0.0458 -0.0384 397 ILE A O   
2831 C CB  . ILE A 395 ? 0.2508 0.1726 0.1712 0.0367  -0.0412 -0.0451 397 ILE A CB  
2832 C CG1 . ILE A 395 ? 0.2450 0.1736 0.1652 0.0318  -0.0382 -0.0487 397 ILE A CG1 
2833 C CG2 . ILE A 395 ? 0.2608 0.1651 0.1697 0.0191  -0.0460 -0.0423 397 ILE A CG2 
2834 C CD1 . ILE A 395 ? 0.2168 0.1754 0.1587 0.0189  -0.0353 -0.0458 397 ILE A CD1 
2835 N N   . GLU A 396 ? 0.3368 0.1842 0.2034 0.0659  -0.0526 -0.0437 398 GLU A N   
2836 C CA  . GLU A 396 ? 0.3536 0.1870 0.2126 0.0679  -0.0579 -0.0389 398 GLU A CA  
2837 C C   . GLU A 396 ? 0.3467 0.1676 0.1992 0.0414  -0.0613 -0.0365 398 GLU A C   
2838 O O   . GLU A 396 ? 0.3586 0.1563 0.1910 0.0262  -0.0630 -0.0388 398 GLU A O   
2839 C CB  . GLU A 396 ? 0.4109 0.1991 0.2327 0.0882  -0.0622 -0.0404 398 GLU A CB  
2840 C CG  . GLU A 396 ? 0.4283 0.2323 0.2546 0.1181  -0.0574 -0.0427 398 GLU A CG  
2841 C CD  . GLU A 396 ? 0.4972 0.2569 0.2842 0.1454  -0.0606 -0.0439 398 GLU A CD  
2842 O OE1 . GLU A 396 ? 0.5368 0.2730 0.2994 0.1614  -0.0577 -0.0498 398 GLU A OE1 
2843 O OE2 . GLU A 396 ? 0.5287 0.2759 0.3073 0.1521  -0.0660 -0.0389 398 GLU A OE2 
2844 N N   . PHE A 397 ? 0.3237 0.1619 0.1918 0.0353  -0.0623 -0.0312 399 PHE A N   
2845 C CA  . PHE A 397 ? 0.3191 0.1544 0.1844 0.0119  -0.0636 -0.0282 399 PHE A CA  
2846 C C   . PHE A 397 ? 0.3169 0.1481 0.1805 0.0117  -0.0673 -0.0228 399 PHE A C   
2847 O O   . PHE A 397 ? 0.3058 0.1494 0.1801 0.0272  -0.0683 -0.0209 399 PHE A O   
2848 C CB  . PHE A 397 ? 0.2771 0.1512 0.1699 -0.0002 -0.0574 -0.0281 399 PHE A CB  
2849 C CG  . PHE A 397 ? 0.2460 0.1554 0.1676 0.0069  -0.0532 -0.0266 399 PHE A CG  
2850 C CD1 . PHE A 397 ? 0.2327 0.1603 0.1687 0.0213  -0.0504 -0.0287 399 PHE A CD1 
2851 C CD2 . PHE A 397 ? 0.2298 0.1528 0.1606 -0.0022 -0.0519 -0.0228 399 PHE A CD2 
2852 C CE1 . PHE A 397 ? 0.2061 0.1634 0.1641 0.0232  -0.0477 -0.0264 399 PHE A CE1 
2853 C CE2 . PHE A 397 ? 0.2066 0.1541 0.1564 0.0019  -0.0491 -0.0216 399 PHE A CE2 
2854 C CZ  . PHE A 397 ? 0.1974 0.1614 0.1602 0.0128  -0.0475 -0.0231 399 PHE A CZ  
2855 N N   . THR A 398 ? 0.3294 0.1466 0.1794 -0.0076 -0.0696 -0.0196 400 THR A N   
2856 C CA  . THR A 398 ? 0.3405 0.1492 0.1836 -0.0109 -0.0733 -0.0143 400 THR A CA  
2857 C C   . THR A 398 ? 0.3213 0.1563 0.1790 -0.0292 -0.0687 -0.0114 400 THR A C   
2858 O O   . THR A 398 ? 0.3204 0.1601 0.1751 -0.0456 -0.0664 -0.0112 400 THR A O   
2859 C CB  . THR A 398 ? 0.3942 0.1510 0.1962 -0.0150 -0.0810 -0.0123 400 THR A CB  
2860 O OG1 . THR A 398 ? 0.4143 0.1457 0.2003 0.0084  -0.0844 -0.0151 400 THR A OG1 
2861 C CG2 . THR A 398 ? 0.4065 0.1515 0.1974 -0.0208 -0.0853 -0.0061 400 THR A CG2 
2862 N N   . ILE A 399 ? 0.3141 0.1659 0.1848 -0.0260 -0.0679 -0.0086 401 ILE A N   
2863 C CA  . ILE A 399 ? 0.3017 0.1718 0.1791 -0.0396 -0.0633 -0.0057 401 ILE A CA  
2864 C C   . ILE A 399 ? 0.3305 0.1764 0.1857 -0.0470 -0.0687 -0.0005 401 ILE A C   
2865 O O   . ILE A 399 ? 0.3440 0.1739 0.1913 -0.0361 -0.0748 0.0009  401 ILE A O   
2866 C CB  . ILE A 399 ? 0.2684 0.1676 0.1689 -0.0321 -0.0587 -0.0068 401 ILE A CB  
2867 C CG1 . ILE A 399 ? 0.2465 0.1667 0.1659 -0.0257 -0.0537 -0.0112 401 ILE A CG1 
2868 C CG2 . ILE A 399 ? 0.2614 0.1725 0.1618 -0.0420 -0.0536 -0.0043 401 ILE A CG2 
2869 C CD1 . ILE A 399 ? 0.2249 0.1648 0.1601 -0.0192 -0.0511 -0.0118 401 ILE A CD1 
2870 N N   . THR A 400 ? 0.3507 0.1962 0.1951 -0.0654 -0.0664 0.0028  402 THR A N   
2871 C CA  . THR A 400 ? 0.3928 0.2187 0.2159 -0.0752 -0.0703 0.0084  402 THR A CA  
2872 C C   . THR A 400 ? 0.3775 0.2315 0.2109 -0.0820 -0.0628 0.0108  402 THR A C   
2873 O O   . THR A 400 ? 0.3592 0.2438 0.2088 -0.0847 -0.0545 0.0094  402 THR A O   
2874 C CB  . THR A 400 ? 0.4417 0.2383 0.2354 -0.0935 -0.0747 0.0119  402 THR A CB  
2875 O OG1 . THR A 400 ? 0.4487 0.2751 0.2522 -0.1101 -0.0680 0.0130  402 THR A OG1 
2876 C CG2 . THR A 400 ? 0.4711 0.2312 0.2463 -0.0855 -0.0818 0.0088  402 THR A CG2 
2877 N N   . SER A 401 ? 0.3800 0.2216 0.2008 -0.0830 -0.0659 0.0145  403 SER A N   
2878 C CA  . SER A 401 ? 0.3848 0.2447 0.2061 -0.0896 -0.0590 0.0169  403 SER A CA  
2879 C C   . SER A 401 ? 0.4093 0.2482 0.2038 -0.1051 -0.0626 0.0237  403 SER A C   
2880 O O   . SER A 401 ? 0.4368 0.2436 0.2136 -0.1024 -0.0721 0.0260  403 SER A O   
2881 C CB  . SER A 401 ? 0.3693 0.2340 0.1982 -0.0774 -0.0595 0.0149  403 SER A CB  
2882 O OG  . SER A 401 ? 0.3688 0.2513 0.2194 -0.0661 -0.0564 0.0095  403 SER A OG  
2883 N N   . THR A 402 ? 0.4110 0.2696 0.2018 -0.1201 -0.0549 0.0275  404 THR A N   
2884 C CA  . THR A 402 ? 0.4416 0.2851 0.2066 -0.1367 -0.0567 0.0348  404 THR A CA  
2885 C C   . THR A 402 ? 0.4267 0.2883 0.1919 -0.1340 -0.0490 0.0358  404 THR A C   
2886 O O   . THR A 402 ? 0.3988 0.2958 0.1772 -0.1324 -0.0375 0.0349  404 THR A O   
2887 C CB  . THR A 402 ? 0.4619 0.3158 0.2176 -0.1600 -0.0543 0.0404  404 THR A CB  
2888 O OG1 . THR A 402 ? 0.4710 0.3113 0.2287 -0.1599 -0.0600 0.0372  404 THR A OG1 
2889 C CG2 . THR A 402 ? 0.5035 0.3303 0.2258 -0.1806 -0.0596 0.0488  404 THR A CG2 
2890 N N   . ILE A 403 ? 0.4454 0.2806 0.1925 -0.1325 -0.0557 0.0382  405 ILE A N   
2891 C CA  . ILE A 403 ? 0.4502 0.2928 0.1895 -0.1310 -0.0502 0.0391  405 ILE A CA  
2892 C C   . ILE A 403 ? 0.4835 0.3085 0.1937 -0.1487 -0.0528 0.0474  405 ILE A C   
2893 O O   . ILE A 403 ? 0.5133 0.3027 0.2052 -0.1517 -0.0646 0.0509  405 ILE A O   
2894 C CB  . ILE A 403 ? 0.4388 0.2682 0.1818 -0.1152 -0.0569 0.0348  405 ILE A CB  
2895 C CG1 . ILE A 403 ? 0.4068 0.2549 0.1761 -0.1011 -0.0534 0.0275  405 ILE A CG1 
2896 C CG2 . ILE A 403 ? 0.4509 0.2770 0.1766 -0.1164 -0.0541 0.0361  405 ILE A CG2 
2897 C CD1 . ILE A 403 ? 0.4000 0.2391 0.1746 -0.0895 -0.0616 0.0245  405 ILE A CD1 
2898 N N   . ASP A 404 ? 0.4943 0.3445 0.1986 -0.1592 -0.0415 0.0512  406 ASP A N   
2899 C CA  . ASP A 404 ? 0.5404 0.3798 0.2171 -0.1798 -0.0423 0.0603  406 ASP A CA  
2900 C C   . ASP A 404 ? 0.5556 0.3688 0.2108 -0.1756 -0.0473 0.0616  406 ASP A C   
2901 O O   . ASP A 404 ? 0.5422 0.3479 0.2050 -0.1585 -0.0508 0.0556  406 ASP A O   
2902 C CB  . ASP A 404 ? 0.5484 0.4329 0.2283 -0.1923 -0.0276 0.0651  406 ASP A CB  
2903 C CG  . ASP A 404 ? 0.5528 0.4675 0.2390 -0.1771 -0.0134 0.0616  406 ASP A CG  
2904 O OD1 . ASP A 404 ? 0.5691 0.4655 0.2543 -0.1597 -0.0157 0.0549  406 ASP A OD1 
2905 O OD2 . ASP A 404 ? 0.5569 0.5146 0.2477 -0.1824 -0.0001 0.0657  406 ASP A OD2 
2906 N N   . SER A 405 ? 0.5902 0.3903 0.2171 -0.1934 -0.0483 0.0700  407 SER A N   
2907 C CA  . SER A 405 ? 0.6140 0.3866 0.2160 -0.1922 -0.0544 0.0726  407 SER A CA  
2908 C C   . SER A 405 ? 0.6043 0.3957 0.2092 -0.1796 -0.0448 0.0674  407 SER A C   
2909 O O   . SER A 405 ? 0.6293 0.3982 0.2202 -0.1732 -0.0520 0.0664  407 SER A O   
2910 C CB  . SER A 405 ? 0.6570 0.4128 0.2263 -0.2157 -0.0564 0.0834  407 SER A CB  
2911 O OG  . SER A 405 ? 0.6566 0.4522 0.2255 -0.2289 -0.0408 0.0874  407 SER A OG  
2912 N N   . THR A 406 ? 0.5772 0.4082 0.1958 -0.1761 -0.0287 0.0646  408 THR A N   
2913 C CA  . THR A 406 ? 0.5740 0.4170 0.1887 -0.1619 -0.0181 0.0589  408 THR A CA  
2914 C C   . THR A 406 ? 0.5470 0.3835 0.1791 -0.1426 -0.0217 0.0492  408 THR A C   
2915 O O   . THR A 406 ? 0.5515 0.3861 0.1745 -0.1311 -0.0158 0.0437  408 THR A O   
2916 C CB  . THR A 406 ? 0.5723 0.4609 0.1928 -0.1611 0.0010  0.0602  408 THR A CB  
2917 O OG1 . THR A 406 ? 0.5520 0.4686 0.2033 -0.1552 0.0048  0.0575  408 THR A OG1 
2918 C CG2 . THR A 406 ? 0.6010 0.5044 0.2053 -0.1832 0.0057  0.0712  408 THR A CG2 
2919 N N   . GLY A 407 ? 0.5247 0.3563 0.1785 -0.1399 -0.0311 0.0473  409 GLY A N   
2920 C CA  . GLY A 407 ? 0.4982 0.3278 0.1702 -0.1243 -0.0347 0.0393  409 GLY A CA  
2921 C C   . GLY A 407 ? 0.4672 0.3273 0.1618 -0.1143 -0.0226 0.0342  409 GLY A C   
2922 O O   . GLY A 407 ? 0.4449 0.3035 0.1504 -0.1017 -0.0232 0.0276  409 GLY A O   
2923 N N   . ALA A 408 ? 0.4659 0.3551 0.1664 -0.1209 -0.0123 0.0382  410 ALA A N   
2924 C CA  . ALA A 408 ? 0.4485 0.3717 0.1706 -0.1107 -0.0011 0.0350  410 ALA A CA  
2925 C C   . ALA A 408 ? 0.4258 0.3523 0.1719 -0.1134 -0.0088 0.0342  410 ALA A C   
2926 O O   . ALA A 408 ? 0.4369 0.3544 0.1803 -0.1288 -0.0165 0.0394  410 ALA A O   
2927 C CB  . ALA A 408 ? 0.4583 0.4195 0.1774 -0.1163 0.0129  0.0410  410 ALA A CB  
2928 N N   . LEU A 409 ? 0.3992 0.3356 0.1645 -0.0987 -0.0062 0.0278  411 LEU A N   
2929 C CA  . LEU A 409 ? 0.3787 0.3226 0.1662 -0.0998 -0.0110 0.0266  411 LEU A CA  
2930 C C   . LEU A 409 ? 0.3766 0.3588 0.1744 -0.1086 -0.0028 0.0316  411 LEU A C   
2931 O O   . LEU A 409 ? 0.3683 0.3837 0.1734 -0.0987 0.0095  0.0314  411 LEU A O   
2932 C CB  . LEU A 409 ? 0.3552 0.2976 0.1570 -0.0825 -0.0107 0.0190  411 LEU A CB  
2933 C CG  . LEU A 409 ? 0.3351 0.2852 0.1595 -0.0809 -0.0149 0.0167  411 LEU A CG  
2934 C CD1 . LEU A 409 ? 0.3407 0.2633 0.1639 -0.0869 -0.0288 0.0173  411 LEU A CD1 
2935 C CD2 . LEU A 409 ? 0.3145 0.2694 0.1506 -0.0645 -0.0112 0.0104  411 LEU A CD2 
2936 N N   . THR A 410 ? 0.3866 0.3634 0.1821 -0.1275 -0.0102 0.0368  412 THR A N   
2937 C CA  . THR A 410 ? 0.3953 0.4081 0.1955 -0.1438 -0.0048 0.0438  412 THR A CA  
2938 C C   . THR A 410 ? 0.3897 0.4158 0.2099 -0.1441 -0.0077 0.0416  412 THR A C   
2939 O O   . THR A 410 ? 0.3915 0.4617 0.2250 -0.1489 -0.0005 0.0455  412 THR A O   
2940 C CB  . THR A 410 ? 0.4193 0.4154 0.1959 -0.1701 -0.0111 0.0524  412 THR A CB  
2941 O OG1 . THR A 410 ? 0.4264 0.3740 0.1919 -0.1743 -0.0258 0.0503  412 THR A OG1 
2942 C CG2 . THR A 410 ? 0.4375 0.4281 0.1939 -0.1715 -0.0065 0.0559  412 THR A CG2 
2943 N N   . ASP A 411 ? 0.3878 0.3788 0.2095 -0.1389 -0.0183 0.0360  413 ASP A N   
2944 C CA  . ASP A 411 ? 0.3832 0.3808 0.2189 -0.1405 -0.0218 0.0337  413 ASP A CA  
2945 C C   . ASP A 411 ? 0.3648 0.3340 0.2079 -0.1228 -0.0283 0.0255  413 ASP A C   
2946 O O   . ASP A 411 ? 0.3655 0.3048 0.1990 -0.1156 -0.0338 0.0235  413 ASP A O   
2947 C CB  . ASP A 411 ? 0.4191 0.4014 0.2376 -0.1665 -0.0303 0.0395  413 ASP A CB  
2948 C CG  . ASP A 411 ? 0.4298 0.4317 0.2604 -0.1738 -0.0316 0.0392  413 ASP A CG  
2949 O OD1 . ASP A 411 ? 0.3974 0.4300 0.2525 -0.1576 -0.0250 0.0351  413 ASP A OD1 
2950 O OD2 . ASP A 411 ? 0.4823 0.4649 0.2940 -0.1962 -0.0397 0.0431  413 ASP A OD2 
2951 N N   . MET A 412 ? 0.3410 0.3244 0.2016 -0.1164 -0.0276 0.0216  414 MET A N   
2952 C CA  . MET A 412 ? 0.3296 0.2911 0.1974 -0.1027 -0.0336 0.0149  414 MET A CA  
2953 C C   . MET A 412 ? 0.3154 0.2849 0.1908 -0.1079 -0.0356 0.0136  414 MET A C   
2954 O O   . MET A 412 ? 0.3089 0.3142 0.1957 -0.1127 -0.0295 0.0160  414 MET A O   
2955 C CB  . MET A 412 ? 0.3082 0.2807 0.1903 -0.0831 -0.0277 0.0100  414 MET A CB  
2956 C CG  . MET A 412 ? 0.3109 0.2710 0.2037 -0.0706 -0.0325 0.0042  414 MET A CG  
2957 S SD  . MET A 412 ? 0.3033 0.2881 0.2156 -0.0659 -0.0286 0.0010  414 MET A SD  
2958 C CE  . MET A 412 ? 0.2848 0.3001 0.2050 -0.0553 -0.0164 0.0013  414 MET A CE  
2959 N N   . THR A 413 ? 0.3177 0.2553 0.1856 -0.1053 -0.0442 0.0101  415 THR A N   
2960 C CA  . THR A 413 ? 0.3155 0.2535 0.1860 -0.1088 -0.0469 0.0076  415 THR A CA  
2961 C C   . THR A 413 ? 0.3038 0.2277 0.1832 -0.0890 -0.0493 0.0006  415 THR A C   
2962 O O   . THR A 413 ? 0.3130 0.2207 0.1914 -0.0765 -0.0518 -0.0009 415 THR A O   
2963 C CB  . THR A 413 ? 0.3538 0.2602 0.1952 -0.1293 -0.0554 0.0109  415 THR A CB  
2964 O OG1 . THR A 413 ? 0.3800 0.2390 0.2014 -0.1201 -0.0633 0.0084  415 THR A OG1 
2965 C CG2 . THR A 413 ? 0.3711 0.2885 0.1998 -0.1521 -0.0542 0.0193  415 THR A CG2 
2966 N N   . SER A 414 ? 0.2947 0.2285 0.1827 -0.0874 -0.0486 -0.0026 416 SER A N   
2967 C CA  . SER A 414 ? 0.2880 0.2103 0.1821 -0.0710 -0.0505 -0.0086 416 SER A CA  
2968 C C   . SER A 414 ? 0.3004 0.2095 0.1821 -0.0790 -0.0545 -0.0107 416 SER A C   
2969 O O   . SER A 414 ? 0.2924 0.2269 0.1817 -0.0895 -0.0518 -0.0093 416 SER A O   
2970 C CB  . SER A 414 ? 0.2548 0.2068 0.1743 -0.0573 -0.0436 -0.0112 416 SER A CB  
2971 O OG  . SER A 414 ? 0.2559 0.2000 0.1815 -0.0427 -0.0452 -0.0160 416 SER A OG  
2972 N N   . THR A 415 ? 0.3307 0.1998 0.1908 -0.0732 -0.0611 -0.0137 417 THR A N   
2973 C CA  . THR A 415 ? 0.3715 0.2142 0.2078 -0.0823 -0.0662 -0.0161 417 THR A CA  
2974 C C   . THR A 415 ? 0.3835 0.1994 0.2109 -0.0607 -0.0682 -0.0225 417 THR A C   
2975 O O   . THR A 415 ? 0.3788 0.1863 0.2089 -0.0420 -0.0686 -0.0231 417 THR A O   
2976 C CB  . THR A 415 ? 0.4205 0.2272 0.2208 -0.1040 -0.0736 -0.0115 417 THR A CB  
2977 O OG1 . THR A 415 ? 0.4451 0.2173 0.2288 -0.0916 -0.0775 -0.0110 417 THR A OG1 
2978 C CG2 . THR A 415 ? 0.4168 0.2560 0.2251 -0.1271 -0.0710 -0.0040 417 THR A CG2 
2979 N N   . SER A 416 ? 0.3984 0.2002 0.2114 -0.0641 -0.0701 -0.0265 418 SER A N   
2980 C CA  . SER A 416 ? 0.4124 0.1892 0.2130 -0.0433 -0.0708 -0.0329 418 SER A CA  
2981 C C   . SER A 416 ? 0.4556 0.1914 0.2169 -0.0568 -0.0768 -0.0359 418 SER A C   
2982 O O   . SER A 416 ? 0.4528 0.1976 0.2094 -0.0833 -0.0792 -0.0329 418 SER A O   
2983 C CB  . SER A 416 ? 0.3718 0.1895 0.2069 -0.0280 -0.0634 -0.0362 418 SER A CB  
2984 O OG  . SER A 416 ? 0.3897 0.1876 0.2117 -0.0093 -0.0630 -0.0421 418 SER A OG  
2985 N N   . ALA A 417 ? 0.4934 0.1862 0.2255 -0.0382 -0.0791 -0.0414 419 ALA A N   
2986 C CA  . ALA A 417 ? 0.5546 0.1997 0.2422 -0.0489 -0.0849 -0.0457 419 ALA A CA  
2987 C C   . ALA A 417 ? 0.5396 0.2138 0.2441 -0.0498 -0.0808 -0.0500 419 ALA A C   
2988 O O   . ALA A 417 ? 0.5829 0.2287 0.2556 -0.0658 -0.0858 -0.0527 419 ALA A O   
2989 C CB  . ALA A 417 ? 0.6083 0.1917 0.2523 -0.0252 -0.0883 -0.0503 419 ALA A CB  
2990 N N   . THR A 418 ? 0.4892 0.2172 0.2401 -0.0347 -0.0723 -0.0503 420 THR A N   
2991 C CA  . THR A 418 ? 0.4770 0.2283 0.2412 -0.0310 -0.0681 -0.0545 420 THR A CA  
2992 C C   . THR A 418 ? 0.4233 0.2366 0.2334 -0.0389 -0.0627 -0.0502 420 THR A C   
2993 O O   . THR A 418 ? 0.4002 0.2378 0.2268 -0.0316 -0.0581 -0.0528 420 THR A O   
2994 C CB  . THR A 418 ? 0.4808 0.2270 0.2461 0.0010  -0.0626 -0.0601 420 THR A CB  
2995 O OG1 . THR A 418 ? 0.4304 0.2139 0.2326 0.0161  -0.0573 -0.0565 420 THR A OG1 
2996 C CG2 . THR A 418 ? 0.5473 0.2303 0.2630 0.0154  -0.0668 -0.0648 420 THR A CG2 
2997 N N   . ALA A 419 ? 0.4053 0.2413 0.2320 -0.0525 -0.0630 -0.0437 421 ALA A N   
2998 C CA  . ALA A 419 ? 0.3573 0.2470 0.2224 -0.0551 -0.0572 -0.0395 421 ALA A CA  
2999 C C   . ALA A 419 ? 0.3528 0.2592 0.2228 -0.0744 -0.0586 -0.0323 421 ALA A C   
3000 O O   . ALA A 419 ? 0.3872 0.2653 0.2356 -0.0837 -0.0634 -0.0302 421 ALA A O   
3001 C CB  . ALA A 419 ? 0.3256 0.2357 0.2177 -0.0331 -0.0505 -0.0404 421 ALA A CB  
3002 N N   . THR A 420 ? 0.3135 0.2659 0.2096 -0.0789 -0.0541 -0.0283 422 THR A N   
3003 C CA  . THR A 420 ? 0.3104 0.2899 0.2151 -0.0936 -0.0532 -0.0208 422 THR A CA  
3004 C C   . THR A 420 ? 0.2724 0.2841 0.2060 -0.0776 -0.0447 -0.0190 422 THR A C   
3005 O O   . THR A 420 ? 0.2456 0.2779 0.1965 -0.0648 -0.0400 -0.0207 422 THR A O   
3006 C CB  . THR A 420 ? 0.3227 0.3320 0.2279 -0.1138 -0.0557 -0.0160 422 THR A CB  
3007 O OG1 . THR A 420 ? 0.3745 0.3460 0.2472 -0.1292 -0.0645 -0.0188 422 THR A OG1 
3008 C CG2 . THR A 420 ? 0.3154 0.3569 0.2271 -0.1304 -0.0547 -0.0070 422 THR A CG2 
3009 N N   . PHE A 421 ? 0.2650 0.2759 0.1987 -0.0794 -0.0433 -0.0156 423 PHE A N   
3010 C CA  . PHE A 421 ? 0.2316 0.2658 0.1842 -0.0670 -0.0359 -0.0137 423 PHE A CA  
3011 C C   . PHE A 421 ? 0.2390 0.3087 0.1977 -0.0774 -0.0322 -0.0065 423 PHE A C   
3012 O O   . PHE A 421 ? 0.2670 0.3383 0.2140 -0.0973 -0.0363 -0.0021 423 PHE A O   
3013 C CB  . PHE A 421 ? 0.2275 0.2365 0.1739 -0.0602 -0.0367 -0.0148 423 PHE A CB  
3014 C CG  . PHE A 421 ? 0.2179 0.2012 0.1611 -0.0471 -0.0396 -0.0202 423 PHE A CG  
3015 C CD1 . PHE A 421 ? 0.2374 0.1878 0.1602 -0.0498 -0.0461 -0.0227 423 PHE A CD1 
3016 C CD2 . PHE A 421 ? 0.1948 0.1865 0.1525 -0.0322 -0.0358 -0.0223 423 PHE A CD2 
3017 C CE1 . PHE A 421 ? 0.2415 0.1743 0.1620 -0.0339 -0.0475 -0.0269 423 PHE A CE1 
3018 C CE2 . PHE A 421 ? 0.1963 0.1739 0.1536 -0.0208 -0.0380 -0.0258 423 PHE A CE2 
3019 C CZ  . PHE A 421 ? 0.2188 0.1701 0.1592 -0.0198 -0.0433 -0.0280 423 PHE A CZ  
3020 N N   . GLU A 422 ? 0.2265 0.3238 0.2010 -0.0636 -0.0243 -0.0049 424 GLU A N   
3021 C CA  . GLU A 422 ? 0.2350 0.3664 0.2148 -0.0661 -0.0184 0.0017  424 GLU A CA  
3022 C C   . GLU A 422 ? 0.2195 0.3366 0.1954 -0.0557 -0.0138 0.0009  424 GLU A C   
3023 O O   . GLU A 422 ? 0.2021 0.3017 0.1795 -0.0408 -0.0122 -0.0037 424 GLU A O   
3024 C CB  . GLU A 422 ? 0.2520 0.4223 0.2470 -0.0536 -0.0123 0.0042  424 GLU A CB  
3025 C CG  . GLU A 422 ? 0.3004 0.4886 0.2995 -0.0640 -0.0174 0.0056  424 GLU A CG  
3026 C CD  . GLU A 422 ? 0.3453 0.5800 0.3594 -0.0514 -0.0115 0.0106  424 GLU A CD  
3027 O OE1 . GLU A 422 ? 0.3972 0.6272 0.4149 -0.0288 -0.0055 0.0081  424 GLU A OE1 
3028 O OE2 . GLU A 422 ? 0.4209 0.6965 0.4409 -0.0643 -0.0134 0.0179  424 GLU A OE2 
3029 N N   . THR A 423 ? 0.2285 0.3539 0.1977 -0.0655 -0.0121 0.0059  425 THR A N   
3030 C CA  . THR A 423 ? 0.2402 0.3488 0.2013 -0.0585 -0.0088 0.0052  425 THR A CA  
3031 C C   . THR A 423 ? 0.2551 0.3986 0.2180 -0.0538 0.0008  0.0109  425 THR A C   
3032 O O   . THR A 423 ? 0.2608 0.4416 0.2292 -0.0642 0.0028  0.0175  425 THR A O   
3033 C CB  . THR A 423 ? 0.2501 0.3256 0.1953 -0.0729 -0.0163 0.0054  425 THR A CB  
3034 O OG1 . THR A 423 ? 0.2662 0.3533 0.2043 -0.0947 -0.0197 0.0112  425 THR A OG1 
3035 C CG2 . THR A 423 ? 0.2516 0.2905 0.1923 -0.0700 -0.0244 -0.0003 425 THR A CG2 
3036 N N   . ASP A 424 ? 0.2692 0.4004 0.2251 -0.0383 0.0066  0.0086  426 ASP A N   
3037 C CA  . ASP A 424 ? 0.2763 0.4301 0.2265 -0.0305 0.0166  0.0129  426 ASP A CA  
3038 C C   . ASP A 424 ? 0.2897 0.4090 0.2222 -0.0326 0.0153  0.0108  426 ASP A C   
3039 O O   . ASP A 424 ? 0.2831 0.3720 0.2068 -0.0214 0.0147  0.0053  426 ASP A O   
3040 C CB  . ASP A 424 ? 0.2806 0.4486 0.2330 -0.0055 0.0255  0.0116  426 ASP A CB  
3041 C CG  . ASP A 424 ? 0.3156 0.5105 0.2600 0.0093  0.0379  0.0160  426 ASP A CG  
3042 O OD1 . ASP A 424 ? 0.3253 0.5301 0.2632 -0.0008 0.0404  0.0201  426 ASP A OD1 
3043 O OD2 . ASP A 424 ? 0.3402 0.5448 0.2824 0.0328  0.0453  0.0154  426 ASP A OD2 
3044 N N   . VAL A 425 ? 0.3099 0.4345 0.2354 -0.0494 0.0140  0.0159  427 VAL A N   
3045 C CA  . VAL A 425 ? 0.3292 0.4210 0.2369 -0.0545 0.0109  0.0149  427 VAL A CA  
3046 C C   . VAL A 425 ? 0.3221 0.4103 0.2164 -0.0374 0.0203  0.0133  427 VAL A C   
3047 O O   . VAL A 425 ? 0.3375 0.3899 0.2178 -0.0342 0.0166  0.0091  427 VAL A O   
3048 C CB  . VAL A 425 ? 0.3568 0.4548 0.2566 -0.0775 0.0078  0.0219  427 VAL A CB  
3049 C CG1 . VAL A 425 ? 0.3728 0.4366 0.2526 -0.0821 0.0041  0.0216  427 VAL A CG1 
3050 C CG2 . VAL A 425 ? 0.3729 0.4643 0.2771 -0.0950 -0.0022 0.0229  427 VAL A CG2 
3051 N N   . ASN A 426 ? 0.3194 0.4447 0.2154 -0.0261 0.0322  0.0169  428 ASN A N   
3052 C CA  . ASN A 426 ? 0.3418 0.4615 0.2188 -0.0069 0.0427  0.0153  428 ASN A CA  
3053 C C   . ASN A 426 ? 0.3343 0.4175 0.2014 0.0102  0.0414  0.0075  428 ASN A C   
3054 O O   . ASN A 426 ? 0.3461 0.3938 0.1898 0.0150  0.0414  0.0036  428 ASN A O   
3055 C CB  . ASN A 426 ? 0.3628 0.5345 0.2444 0.0067  0.0565  0.0213  428 ASN A CB  
3056 C CG  . ASN A 426 ? 0.4069 0.6168 0.2923 -0.0116 0.0595  0.0304  428 ASN A CG  
3057 O OD1 . ASN A 426 ? 0.4215 0.6162 0.3059 -0.0365 0.0501  0.0323  428 ASN A OD1 
3058 N ND2 . ASN A 426 ? 0.4337 0.6931 0.3208 0.0011  0.0729  0.0367  428 ASN A ND2 
3059 N N   . ARG A 427 ? 0.3144 0.4050 0.1965 0.0173  0.0398  0.0057  429 ARG A N   
3060 C CA  . ARG A 427 ? 0.3301 0.3867 0.2008 0.0310  0.0385  -0.0006 429 ARG A CA  
3061 C C   . ARG A 427 ? 0.2996 0.3232 0.1737 0.0165  0.0255  -0.0046 429 ARG A C   
3062 O O   . ARG A 427 ? 0.3060 0.2991 0.1682 0.0218  0.0227  -0.0090 429 ARG A O   
3063 C CB  . ARG A 427 ? 0.3537 0.4339 0.2371 0.0458  0.0428  0.0001  429 ARG A CB  
3064 C CG  . ARG A 427 ? 0.4155 0.5301 0.2934 0.0667  0.0563  0.0046  429 ARG A CG  
3065 C CD  . ARG A 427 ? 0.4791 0.6009 0.3585 0.0882  0.0602  0.0042  429 ARG A CD  
3066 N NE  . ARG A 427 ? 0.5528 0.7126 0.4274 0.1123  0.0735  0.0095  429 ARG A NE  
3067 C CZ  . ARG A 427 ? 0.5808 0.8038 0.4789 0.1092  0.0778  0.0178  429 ARG A CZ  
3068 N NH1 . ARG A 427 ? 0.5626 0.8111 0.4876 0.0821  0.0690  0.0211  429 ARG A NH1 
3069 N NH2 . ARG A 427 ? 0.6176 0.8787 0.5099 0.1335  0.0910  0.0233  429 ARG A NH2 
3070 N N   . GLY A 428 ? 0.2731 0.3039 0.1619 -0.0014 0.0177  -0.0024 430 GLY A N   
3071 C CA  . GLY A 428 ? 0.2614 0.2672 0.1544 -0.0118 0.0061  -0.0051 430 GLY A CA  
3072 C C   . GLY A 428 ? 0.2429 0.2508 0.1513 -0.0081 0.0027  -0.0079 430 GLY A C   
3073 O O   . GLY A 428 ? 0.2342 0.2211 0.1410 -0.0088 -0.0033 -0.0109 430 GLY A O   
3074 N N   . TYR A 429 ? 0.2303 0.2665 0.1533 -0.0054 0.0064  -0.0061 431 TYR A N   
3075 C CA  . TYR A 429 ? 0.2157 0.2558 0.1522 -0.0021 0.0037  -0.0084 431 TYR A CA  
3076 C C   . TYR A 429 ? 0.1970 0.2431 0.1465 -0.0153 -0.0035 -0.0078 431 TYR A C   
3077 O O   . TYR A 429 ? 0.2046 0.2652 0.1554 -0.0259 -0.0039 -0.0040 431 TYR A O   
3078 C CB  . TYR A 429 ? 0.2224 0.2892 0.1642 0.0105  0.0116  -0.0066 431 TYR A CB  
3079 C CG  . TYR A 429 ? 0.2533 0.3092 0.1769 0.0289  0.0196  -0.0076 431 TYR A CG  
3080 C CD1 . TYR A 429 ? 0.2716 0.2894 0.1743 0.0304  0.0179  -0.0112 431 TYR A CD1 
3081 C CD2 . TYR A 429 ? 0.2664 0.3490 0.1904 0.0450  0.0284  -0.0044 431 TYR A CD2 
3082 C CE1 . TYR A 429 ? 0.3038 0.3016 0.1813 0.0466  0.0246  -0.0126 431 TYR A CE1 
3083 C CE2 . TYR A 429 ? 0.2972 0.3626 0.1978 0.0656  0.0360  -0.0056 431 TYR A CE2 
3084 C CZ  . TYR A 429 ? 0.3139 0.3327 0.1887 0.0657  0.0341  -0.0101 431 TYR A CZ  
3085 O OH  . TYR A 429 ? 0.3562 0.3477 0.2000 0.0846  0.0406  -0.0119 431 TYR A OH  
3086 N N   . ILE A 430 ? 0.1792 0.2119 0.1346 -0.0151 -0.0093 -0.0113 432 ILE A N   
3087 C CA  . ILE A 430 ? 0.1762 0.2103 0.1396 -0.0226 -0.0150 -0.0120 432 ILE A CA  
3088 C C   . ILE A 430 ? 0.1646 0.2067 0.1377 -0.0147 -0.0137 -0.0146 432 ILE A C   
3089 O O   . ILE A 430 ? 0.1556 0.1865 0.1285 -0.0078 -0.0139 -0.0171 432 ILE A O   
3090 C CB  . ILE A 430 ? 0.1831 0.1924 0.1416 -0.0263 -0.0229 -0.0136 432 ILE A CB  
3091 C CG1 . ILE A 430 ? 0.2027 0.2002 0.1487 -0.0334 -0.0250 -0.0107 432 ILE A CG1 
3092 C CG2 . ILE A 430 ? 0.1867 0.1901 0.1471 -0.0299 -0.0282 -0.0154 432 ILE A CG2 
3093 C CD1 . ILE A 430 ? 0.2119 0.1872 0.1527 -0.0321 -0.0324 -0.0114 432 ILE A CD1 
3094 N N   . ASN A 431 ? 0.1641 0.2264 0.1441 -0.0177 -0.0129 -0.0133 433 ASN A N   
3095 C CA  . ASN A 431 ? 0.1628 0.2356 0.1506 -0.0100 -0.0111 -0.0148 433 ASN A CA  
3096 C C   . ASN A 431 ? 0.1517 0.2222 0.1423 -0.0176 -0.0168 -0.0169 433 ASN A C   
3097 O O   . ASN A 431 ? 0.1530 0.2267 0.1395 -0.0301 -0.0202 -0.0150 433 ASN A O   
3098 C CB  . ASN A 431 ? 0.1810 0.2827 0.1725 -0.0029 -0.0045 -0.0108 433 ASN A CB  
3099 C CG  . ASN A 431 ? 0.2303 0.3289 0.2125 0.0085  0.0021  -0.0094 433 ASN A CG  
3100 O OD1 . ASN A 431 ? 0.2507 0.3255 0.2238 0.0159  0.0029  -0.0122 433 ASN A OD1 
3101 N ND2 . ASN A 431 ? 0.2720 0.3944 0.2536 0.0090  0.0070  -0.0047 433 ASN A ND2 
3102 N N   . LEU A 432 ? 0.1418 0.2040 0.1355 -0.0112 -0.0178 -0.0206 434 LEU A N   
3103 C CA  . LEU A 432 ? 0.1433 0.2012 0.1364 -0.0148 -0.0219 -0.0234 434 LEU A CA  
3104 C C   . LEU A 432 ? 0.1316 0.2028 0.1315 -0.0073 -0.0189 -0.0241 434 LEU A C   
3105 O O   . LEU A 432 ? 0.1193 0.1879 0.1216 0.0014  -0.0158 -0.0246 434 LEU A O   
3106 C CB  . LEU A 432 ? 0.1487 0.1828 0.1367 -0.0121 -0.0257 -0.0271 434 LEU A CB  
3107 C CG  . LEU A 432 ? 0.1636 0.1883 0.1464 -0.0112 -0.0286 -0.0311 434 LEU A CG  
3108 C CD1 . LEU A 432 ? 0.1865 0.2002 0.1545 -0.0239 -0.0335 -0.0311 434 LEU A CD1 
3109 C CD2 . LEU A 432 ? 0.1723 0.1819 0.1528 -0.0017 -0.0301 -0.0339 434 LEU A CD2 
3110 N N   . LYS A 433 ? 0.1345 0.2183 0.1344 -0.0129 -0.0208 -0.0236 435 LYS A N   
3111 C CA  A LYS A 433 ? 0.1308 0.2255 0.1348 -0.0068 -0.0193 -0.0241 435 LYS A CA  
3112 C CA  B LYS A 433 ? 0.1327 0.2269 0.1368 -0.0064 -0.0192 -0.0242 435 LYS A CA  
3113 C C   . LYS A 433 ? 0.1396 0.2169 0.1374 -0.0079 -0.0225 -0.0294 435 LYS A C   
3114 O O   . LYS A 433 ? 0.1570 0.2246 0.1447 -0.0175 -0.0274 -0.0312 435 LYS A O   
3115 C CB  A LYS A 433 ? 0.1364 0.2599 0.1438 -0.0122 -0.0200 -0.0194 435 LYS A CB  
3116 C CB  B LYS A 433 ? 0.1402 0.2643 0.1485 -0.0096 -0.0190 -0.0192 435 LYS A CB  
3117 C CG  A LYS A 433 ? 0.1350 0.2722 0.1451 -0.0066 -0.0197 -0.0189 435 LYS A CG  
3118 C CG  B LYS A 433 ? 0.1416 0.2785 0.1531 -0.0013 -0.0175 -0.0185 435 LYS A CG  
3119 C CD  A LYS A 433 ? 0.1398 0.3135 0.1553 -0.0110 -0.0209 -0.0125 435 LYS A CD  
3120 C CD  B LYS A 433 ? 0.1471 0.3204 0.1650 0.0010  -0.0164 -0.0117 435 LYS A CD  
3121 C CE  A LYS A 433 ? 0.1547 0.3322 0.1633 -0.0300 -0.0286 -0.0128 435 LYS A CE  
3122 C CE  B LYS A 433 ? 0.1517 0.3342 0.1716 0.0162  -0.0096 -0.0076 435 LYS A CE  
3123 N NZ  A LYS A 433 ? 0.1609 0.3799 0.1760 -0.0402 -0.0308 -0.0046 435 LYS A NZ  
3124 N NZ  B LYS A 433 ? 0.1558 0.3797 0.1825 0.0223  -0.0079 0.0000  435 LYS A NZ  
3125 N N   . VAL A 434 ? 0.1270 0.1991 0.1277 0.0014  -0.0198 -0.0316 436 VAL A N   
3126 C CA  . VAL A 434 ? 0.1376 0.1985 0.1330 0.0040  -0.0209 -0.0362 436 VAL A CA  
3127 C C   . VAL A 434 ? 0.1311 0.2032 0.1258 0.0046  -0.0202 -0.0363 436 VAL A C   
3128 O O   . VAL A 434 ? 0.1169 0.1993 0.1173 0.0103  -0.0166 -0.0338 436 VAL A O   
3129 C CB  . VAL A 434 ? 0.1410 0.1978 0.1412 0.0120  -0.0182 -0.0369 436 VAL A CB  
3130 C CG1 . VAL A 434 ? 0.1569 0.2084 0.1525 0.0179  -0.0178 -0.0410 436 VAL A CG1 
3131 C CG2 . VAL A 434 ? 0.1478 0.1965 0.1491 0.0113  -0.0197 -0.0357 436 VAL A CG2 
3132 N N   . VAL A 435 ? 0.1475 0.2140 0.1313 -0.0020 -0.0242 -0.0389 437 VAL A N   
3133 C CA  . VAL A 435 ? 0.1525 0.2301 0.1332 -0.0037 -0.0250 -0.0387 437 VAL A CA  
3134 C C   . VAL A 435 ? 0.1623 0.2281 0.1355 0.0034  -0.0228 -0.0437 437 VAL A C   
3135 O O   . VAL A 435 ? 0.1794 0.2245 0.1382 0.0037  -0.0245 -0.0488 437 VAL A O   
3136 C CB  . VAL A 435 ? 0.1689 0.2486 0.1388 -0.0187 -0.0317 -0.0379 437 VAL A CB  
3137 C CG1 . VAL A 435 ? 0.1710 0.2659 0.1379 -0.0215 -0.0338 -0.0368 437 VAL A CG1 
3138 C CG2 . VAL A 435 ? 0.1609 0.2574 0.1389 -0.0265 -0.0330 -0.0321 437 VAL A CG2 
3139 N N   . ASN A 436 ? 0.1574 0.2351 0.1375 0.0102  -0.0186 -0.0418 438 ASN A N   
3140 C CA  . ASN A 436 ? 0.1687 0.2424 0.1432 0.0165  -0.0153 -0.0451 438 ASN A CA  
3141 C C   . ASN A 436 ? 0.1797 0.2527 0.1409 0.0120  -0.0182 -0.0472 438 ASN A C   
3142 O O   . ASN A 436 ? 0.1697 0.2570 0.1335 0.0069  -0.0211 -0.0431 438 ASN A O   
3143 C CB  . ASN A 436 ? 0.1547 0.2398 0.1383 0.0218  -0.0102 -0.0412 438 ASN A CB  
3144 C CG  . ASN A 436 ? 0.1501 0.2342 0.1416 0.0250  -0.0073 -0.0403 438 ASN A CG  
3145 O OD1 . ASN A 436 ? 0.1710 0.2584 0.1626 0.0294  -0.0040 -0.0418 438 ASN A OD1 
3146 N N   . LYS A 437 ? 0.2072 0.2643 0.1525 0.0151  -0.0176 -0.0532 439 LYS A N   
3147 C CA  . LYS A 437 ? 0.2378 0.2891 0.1650 0.0100  -0.0208 -0.0561 439 LYS A CA  
3148 C C   . LYS A 437 ? 0.2338 0.2853 0.1547 0.0201  -0.0145 -0.0589 439 LYS A C   
3149 O O   . LYS A 437 ? 0.2344 0.2830 0.1570 0.0308  -0.0087 -0.0612 439 LYS A O   
3150 C CB  . LYS A 437 ? 0.2993 0.3218 0.2016 0.0026  -0.0268 -0.0617 439 LYS A CB  
3151 C CG  . LYS A 437 ? 0.3275 0.3477 0.2323 -0.0097 -0.0330 -0.0587 439 LYS A CG  
3152 C CD  . LYS A 437 ? 0.4072 0.3968 0.2799 -0.0240 -0.0412 -0.0629 439 LYS A CD  
3153 C CE  . LYS A 437 ? 0.4448 0.4349 0.3177 -0.0408 -0.0479 -0.0586 439 LYS A CE  
3154 N NZ  . LYS A 437 ? 0.4785 0.4491 0.3516 -0.0338 -0.0458 -0.0600 439 LYS A NZ  
3155 N N   . GLN A 438 ? 0.2291 0.2884 0.1435 0.0164  -0.0156 -0.0577 440 GLN A N   
3156 C CA  . GLN A 438 ? 0.2383 0.2993 0.1445 0.0240  -0.0096 -0.0597 440 GLN A CA  
3157 C C   . GLN A 438 ? 0.2599 0.2950 0.1384 0.0285  -0.0091 -0.0685 440 GLN A C   
3158 O O   . GLN A 438 ? 0.2715 0.2832 0.1320 0.0219  -0.0155 -0.0727 440 GLN A O   
3159 C CB  . GLN A 438 ? 0.2461 0.3218 0.1521 0.0188  -0.0118 -0.0547 440 GLN A CB  
3160 C CG  . GLN A 438 ? 0.2298 0.3241 0.1563 0.0191  -0.0114 -0.0462 440 GLN A CG  
3161 C CD  . GLN A 438 ? 0.2461 0.3522 0.1687 0.0168  -0.0146 -0.0406 440 GLN A CD  
3162 O OE1 . GLN A 438 ? 0.2688 0.3873 0.1985 0.0145  -0.0197 -0.0352 440 GLN A OE1 
3163 N NE2 . GLN A 438 ? 0.2468 0.3517 0.1580 0.0190  -0.0113 -0.0412 440 GLN A NE2 
3164 N N   . GLY A 439 ? 0.2641 0.3023 0.1362 0.0398  -0.0010 -0.0710 441 GLY A N   
3165 C CA  . GLY A 439 ? 0.2943 0.3070 0.1361 0.0490  0.0014  -0.0797 441 GLY A CA  
3166 C C   . GLY A 439 ? 0.3171 0.3146 0.1317 0.0395  -0.0038 -0.0829 441 GLY A C   
3167 O O   . GLY A 439 ? 0.3012 0.3109 0.1230 0.0254  -0.0106 -0.0778 441 GLY A O   
3168 N N   . ALA A 440 ? 0.3523 0.3249 0.1345 0.0491  -0.0001 -0.0910 442 ALA A N   
3169 C CA  . ALA A 440 ? 0.3852 0.3361 0.1338 0.0396  -0.0057 -0.0954 442 ALA A CA  
3170 C C   . ALA A 440 ? 0.3875 0.3563 0.1336 0.0466  0.0021  -0.0947 442 ALA A C   
3171 O O   . ALA A 440 ? 0.3791 0.3581 0.1278 0.0642  0.0138  -0.0961 442 ALA A O   
3172 C CB  . ALA A 440 ? 0.4377 0.3379 0.1416 0.0443  -0.0081 -0.1058 442 ALA A CB  
3173 N N   . LEU A 441 ? 0.3950 0.3713 0.1365 0.0320  -0.0045 -0.0912 443 LEU A N   
3174 C CA  . LEU A 441 ? 0.4189 0.4030 0.1473 0.0352  0.0005  -0.0913 443 LEU A CA  
3175 C C   . LEU A 441 ? 0.4725 0.4160 0.1519 0.0325  -0.0035 -0.1011 443 LEU A C   
3176 O O   . LEU A 441 ? 0.4836 0.4130 0.1472 0.0139  -0.0163 -0.1012 443 LEU A O   
3177 C CB  . LEU A 441 ? 0.4033 0.4159 0.1517 0.0223  -0.0054 -0.0812 443 LEU A CB  
3178 C CG  . LEU A 441 ? 0.4244 0.4480 0.1621 0.0241  -0.0006 -0.0789 443 LEU A CG  
3179 C CD1 . LEU A 441 ? 0.4081 0.4549 0.1651 0.0364  0.0128  -0.0749 443 LEU A CD1 
3180 C CD2 . LEU A 441 ? 0.4192 0.4596 0.1642 0.0107  -0.0107 -0.0702 443 LEU A CD2 
3181 N N   . LEU A 442 ? 0.5073 0.4326 0.1608 0.0509  0.0070  -0.1091 444 LEU A N   
3182 C CA  . LEU A 442 ? 0.5787 0.4569 0.1775 0.0517  0.0045  -0.1198 444 LEU A CA  
3183 C C   . LEU A 442 ? 0.6035 0.4907 0.1854 0.0566  0.0115  -0.1207 444 LEU A C   
3184 O O   . LEU A 442 ? 0.6172 0.5070 0.1898 0.0783  0.0255  -0.1246 444 LEU A O   
3185 C CB  . LEU A 442 ? 0.6083 0.4533 0.1840 0.0740  0.0121  -0.1287 444 LEU A CB  
3186 C CG  . LEU A 442 ? 0.6026 0.4333 0.1897 0.0696  0.0051  -0.1280 444 LEU A CG  
3187 C CD1 . LEU A 442 ? 0.6257 0.4321 0.1961 0.0974  0.0145  -0.1348 444 LEU A CD1 
3188 C CD2 . LEU A 442 ? 0.6400 0.4311 0.1955 0.0437  -0.0115 -0.1307 444 LEU A CD2 
3189 N N   . PRO A 443 ? 0.6263 0.5250 0.2066 0.0380  0.0029  -0.1156 445 PRO A N   
3190 C CA  . PRO A 443 ? 0.6614 0.5645 0.2206 0.0417  0.0090  -0.1166 445 PRO A CA  
3191 C C   . PRO A 443 ? 0.7334 0.5837 0.2303 0.0455  0.0084  -0.1295 445 PRO A C   
3192 O O   . PRO A 443 ? 0.7827 0.6320 0.2615 0.0634  0.0217  -0.1339 445 PRO A O   
3193 C CB  . PRO A 443 ? 0.6391 0.5671 0.2138 0.0204  -0.0026 -0.1066 445 PRO A CB  
3194 C CG  . PRO A 443 ? 0.5915 0.5385 0.2050 0.0102  -0.0114 -0.0991 445 PRO A CG  
3195 C CD  . PRO A 443 ? 0.6079 0.5222 0.2086 0.0144  -0.0121 -0.1074 445 PRO A CD  
# 
