data_8WXD
# 
_entry.id   8WXD 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   8WXD         pdb_00008wxd 10.2210/pdb8wxd/pdb 
WWPDB D_1300042004 ?            ?                   
# 
_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       2025-05-07 
_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                        8WXD 
_pdbx_database_status.recvd_initial_deposition_date   2023-10-28 
_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        'Basal pilin PilB' 
_pdbx_database_related.db_id          8WGG 
_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 shaft pilin PilA 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 ?                   
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 'Surface protein, putative' 48837.707 2  ? ? ? ? 
2 non-polymer syn 'SODIUM ION'                22.990    6  ? ? ? ? 
3 non-polymer syn 'SULFATE ION'               96.063    2  ? ? ? ? 
4 non-polymer syn GLYCEROL                    92.094    1  ? ? ? ? 
5 non-polymer syn 'CADMIUM ION'               112.411   6  ? ? ? ? 
6 non-polymer syn 'CHLORIDE ION'              35.453    1  ? ? ? ? 
7 water       nat water                       18.015    34 ? ? ? ? 
# 
_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       
;MGSSHHHHHHSSGLVPRRGSHMSADTTYTIQLSGTSEGHYYEVYHIFSGTLDTSNTLTNIEWAPGVTEAGRTHFGNASDK
AASLSGKQNDSAEVKAFAQELNQYLSSAGVTTVQSQQGTTTISGLKPGYYLIKDSRGSLDNKKGHAYTSFMLQVAKDTTV
AVKADVPTLTKQVRANGSQNYTAATDYRIGQNILFQITATLPSNYADFTRYEFTIKDTIPAGMTYNNDAQVYLQEGGTEK
DISTFFPISYTGNVITITPGDLKYVQDVKVSSKIVIRYTARLNDDAVMGGLGNPNIARLTYSNDPNGFTSTTAETPDTKA
NVYTYQLKVNKVKENQQALAGAGFTLYKKVNNQYTEIKKFEADSNSTFDFKGLDSGDYKLVESTVPSGYNAMKDIEFTIS
GTIDSTGDLTNLTATSATASFETDVNTGIITLKVVNKQGALLPNTGGIGTT
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MGSSHHHHHHSSGLVPRRGSHMSADTTYTIQLSGTSEGHYYEVYHIFSGTLDTSNTLTNIEWAPGVTEAGRTHFGNASDK
AASLSGKQNDSAEVKAFAQELNQYLSSAGVTTVQSQQGTTTISGLKPGYYLIKDSRGSLDNKKGHAYTSFMLQVAKDTTV
AVKADVPTLTKQVRANGSQNYTAATDYRIGQNILFQITATLPSNYADFTRYEFTIKDTIPAGMTYNNDAQVYLQEGGTEK
DISTFFPISYTGNVITITPGDLKYVQDVKVSSKIVIRYTARLNDDAVMGGLGNPNIARLTYSNDPNGFTSTTAETPDTKA
NVYTYQLKVNKVKENQQALAGAGFTLYKKVNNQYTEIKKFEADSNSTFDFKGLDSGDYKLVESTVPSGYNAMKDIEFTIS
GTIDSTGDLTNLTATSATASFETDVNTGIITLKVVNKQGALLPNTGGIGTT
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'SODIUM ION'   NA  
3 'SULFATE ION'  SO4 
4 GLYCEROL       GOL 
5 'CADMIUM ION'  CD  
6 'CHLORIDE ION' CL  
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  TYR n 
1 29  THR n 
1 30  ILE n 
1 31  GLN n 
1 32  LEU n 
1 33  SER n 
1 34  GLY n 
1 35  THR n 
1 36  SER n 
1 37  GLU n 
1 38  GLY n 
1 39  HIS n 
1 40  TYR n 
1 41  TYR n 
1 42  GLU n 
1 43  VAL n 
1 44  TYR n 
1 45  HIS n 
1 46  ILE n 
1 47  PHE n 
1 48  SER n 
1 49  GLY n 
1 50  THR n 
1 51  LEU n 
1 52  ASP n 
1 53  THR n 
1 54  SER n 
1 55  ASN n 
1 56  THR n 
1 57  LEU n 
1 58  THR n 
1 59  ASN n 
1 60  ILE n 
1 61  GLU n 
1 62  TRP n 
1 63  ALA n 
1 64  PRO n 
1 65  GLY n 
1 66  VAL n 
1 67  THR n 
1 68  GLU n 
1 69  ALA n 
1 70  GLY n 
1 71  ARG n 
1 72  THR n 
1 73  HIS n 
1 74  PHE n 
1 75  GLY n 
1 76  ASN n 
1 77  ALA n 
1 78  SER n 
1 79  ASP n 
1 80  LYS n 
1 81  ALA n 
1 82  ALA n 
1 83  SER n 
1 84  LEU n 
1 85  SER n 
1 86  GLY n 
1 87  LYS n 
1 88  GLN n 
1 89  ASN n 
1 90  ASP n 
1 91  SER n 
1 92  ALA n 
1 93  GLU n 
1 94  VAL n 
1 95  LYS n 
1 96  ALA n 
1 97  PHE n 
1 98  ALA n 
1 99  GLN n 
1 100 GLU n 
1 101 LEU n 
1 102 ASN n 
1 103 GLN n 
1 104 TYR n 
1 105 LEU n 
1 106 SER n 
1 107 SER n 
1 108 ALA n 
1 109 GLY n 
1 110 VAL n 
1 111 THR n 
1 112 THR n 
1 113 VAL n 
1 114 GLN n 
1 115 SER n 
1 116 GLN n 
1 117 GLN n 
1 118 GLY n 
1 119 THR n 
1 120 THR n 
1 121 THR n 
1 122 ILE n 
1 123 SER n 
1 124 GLY n 
1 125 LEU n 
1 126 LYS n 
1 127 PRO n 
1 128 GLY n 
1 129 TYR n 
1 130 TYR n 
1 131 LEU n 
1 132 ILE n 
1 133 LYS n 
1 134 ASP n 
1 135 SER n 
1 136 ARG n 
1 137 GLY n 
1 138 SER n 
1 139 LEU n 
1 140 ASP n 
1 141 ASN n 
1 142 LYS n 
1 143 LYS n 
1 144 GLY n 
1 145 HIS n 
1 146 ALA n 
1 147 TYR n 
1 148 THR n 
1 149 SER n 
1 150 PHE n 
1 151 MET n 
1 152 LEU n 
1 153 GLN n 
1 154 VAL n 
1 155 ALA n 
1 156 LYS n 
1 157 ASP n 
1 158 THR n 
1 159 THR n 
1 160 VAL n 
1 161 ALA n 
1 162 VAL n 
1 163 LYS n 
1 164 ALA n 
1 165 ASP n 
1 166 VAL n 
1 167 PRO n 
1 168 THR n 
1 169 LEU n 
1 170 THR n 
1 171 LYS n 
1 172 GLN n 
1 173 VAL n 
1 174 ARG n 
1 175 ALA n 
1 176 ASN n 
1 177 GLY n 
1 178 SER n 
1 179 GLN n 
1 180 ASN n 
1 181 TYR n 
1 182 THR n 
1 183 ALA n 
1 184 ALA n 
1 185 THR n 
1 186 ASP n 
1 187 TYR n 
1 188 ARG n 
1 189 ILE n 
1 190 GLY n 
1 191 GLN n 
1 192 ASN n 
1 193 ILE n 
1 194 LEU n 
1 195 PHE n 
1 196 GLN n 
1 197 ILE n 
1 198 THR n 
1 199 ALA n 
1 200 THR n 
1 201 LEU n 
1 202 PRO n 
1 203 SER n 
1 204 ASN n 
1 205 TYR n 
1 206 ALA n 
1 207 ASP n 
1 208 PHE n 
1 209 THR n 
1 210 ARG n 
1 211 TYR n 
1 212 GLU n 
1 213 PHE n 
1 214 THR n 
1 215 ILE n 
1 216 LYS n 
1 217 ASP n 
1 218 THR n 
1 219 ILE n 
1 220 PRO n 
1 221 ALA n 
1 222 GLY n 
1 223 MET n 
1 224 THR n 
1 225 TYR n 
1 226 ASN n 
1 227 ASN n 
1 228 ASP n 
1 229 ALA n 
1 230 GLN n 
1 231 VAL n 
1 232 TYR n 
1 233 LEU n 
1 234 GLN n 
1 235 GLU n 
1 236 GLY n 
1 237 GLY n 
1 238 THR n 
1 239 GLU n 
1 240 LYS n 
1 241 ASP n 
1 242 ILE n 
1 243 SER n 
1 244 THR n 
1 245 PHE n 
1 246 PHE n 
1 247 PRO n 
1 248 ILE n 
1 249 SER n 
1 250 TYR n 
1 251 THR n 
1 252 GLY n 
1 253 ASN n 
1 254 VAL n 
1 255 ILE n 
1 256 THR n 
1 257 ILE n 
1 258 THR n 
1 259 PRO n 
1 260 GLY n 
1 261 ASP n 
1 262 LEU n 
1 263 LYS n 
1 264 TYR n 
1 265 VAL n 
1 266 GLN n 
1 267 ASP n 
1 268 VAL n 
1 269 LYS n 
1 270 VAL n 
1 271 SER 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 ASN n 
1 284 ASP n 
1 285 ASP n 
1 286 ALA n 
1 287 VAL n 
1 288 MET n 
1 289 GLY n 
1 290 GLY n 
1 291 LEU n 
1 292 GLY n 
1 293 ASN n 
1 294 PRO n 
1 295 ASN n 
1 296 ILE n 
1 297 ALA n 
1 298 ARG n 
1 299 LEU n 
1 300 THR n 
1 301 TYR n 
1 302 SER n 
1 303 ASN n 
1 304 ASP n 
1 305 PRO n 
1 306 ASN n 
1 307 GLY n 
1 308 PHE n 
1 309 THR n 
1 310 SER n 
1 311 THR n 
1 312 THR n 
1 313 ALA n 
1 314 GLU n 
1 315 THR n 
1 316 PRO n 
1 317 ASP n 
1 318 THR n 
1 319 LYS n 
1 320 ALA n 
1 321 ASN n 
1 322 VAL n 
1 323 TYR n 
1 324 THR n 
1 325 TYR n 
1 326 GLN n 
1 327 LEU n 
1 328 LYS n 
1 329 VAL n 
1 330 ASN n 
1 331 LYS n 
1 332 VAL n 
1 333 LYS n 
1 334 GLU n 
1 335 ASN n 
1 336 GLN n 
1 337 GLN n 
1 338 ALA n 
1 339 LEU 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 VAL n 
1 351 ASN n 
1 352 ASN n 
1 353 GLN n 
1 354 TYR n 
1 355 THR n 
1 356 GLU n 
1 357 ILE n 
1 358 LYS n 
1 359 LYS n 
1 360 PHE n 
1 361 GLU n 
1 362 ALA n 
1 363 ASP n 
1 364 SER n 
1 365 ASN n 
1 366 SER n 
1 367 THR n 
1 368 PHE n 
1 369 ASP n 
1 370 PHE n 
1 371 LYS n 
1 372 GLY n 
1 373 LEU n 
1 374 ASP n 
1 375 SER 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 VAL n 
1 386 PRO n 
1 387 SER n 
1 388 GLY n 
1 389 TYR n 
1 390 ASN n 
1 391 ALA 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 SER n 
1 401 GLY 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 ASP n 
1 409 LEU n 
1 410 THR n 
1 411 ASN n 
1 412 LEU n 
1 413 THR n 
1 414 ALA n 
1 415 THR n 
1 416 SER n 
1 417 ALA n 
1 418 THR n 
1 419 ALA n 
1 420 SER 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 THR n 
1 428 GLY n 
1 429 ILE n 
1 430 ILE n 
1 431 THR 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_1632 
_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 
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 
CD  non-polymer         . 'CADMIUM ION'   ?                               'Cd 2'           112.411 
CL  non-polymer         . 'CHLORIDE ION'  ?                               'Cl -1'          35.453  
GLN 'L-peptide linking' y GLUTAMINE       ?                               'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ?                               'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE         ?                               'C2 H5 N O2'     75.067  
GOL non-polymer         . GLYCEROL        'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3'       92.094  
HIS 'L-peptide linking' y HISTIDINE       ?                               'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER           ?                               'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE      ?                               'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE         ?                               'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE          ?                               'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE      ?                               'C5 H11 N O2 S'  149.211 
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 
SO4 non-polymer         . 'SULFATE ION'   ?                               'O4 S -2'        96.063  
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  ?   ?   ?   A . n 
A 1 27  THR 27  29  29  THR THR A . n 
A 1 28  TYR 28  30  30  TYR TYR A . n 
A 1 29  THR 29  31  31  THR THR A . n 
A 1 30  ILE 30  32  32  ILE ILE A . n 
A 1 31  GLN 31  33  33  GLN GLN A . n 
A 1 32  LEU 32  34  34  LEU LEU A . n 
A 1 33  SER 33  35  35  SER SER A . n 
A 1 34  GLY 34  36  36  GLY GLY A . n 
A 1 35  THR 35  37  37  THR THR A . n 
A 1 36  SER 36  38  38  SER SER A . n 
A 1 37  GLU 37  39  39  GLU GLU A . n 
A 1 38  GLY 38  40  40  GLY GLY A . n 
A 1 39  HIS 39  41  41  HIS HIS A . n 
A 1 40  TYR 40  42  42  TYR TYR A . n 
A 1 41  TYR 41  43  43  TYR TYR A . n 
A 1 42  GLU 42  44  44  GLU GLU A . n 
A 1 43  VAL 43  45  45  VAL VAL A . n 
A 1 44  TYR 44  46  46  TYR TYR A . n 
A 1 45  HIS 45  47  47  HIS HIS A . n 
A 1 46  ILE 46  48  48  ILE ILE A . n 
A 1 47  PHE 47  49  49  PHE PHE A . n 
A 1 48  SER 48  50  50  SER SER A . n 
A 1 49  GLY 49  51  51  GLY GLY A . n 
A 1 50  THR 50  52  52  THR THR A . n 
A 1 51  LEU 51  53  53  LEU LEU A . n 
A 1 52  ASP 52  54  54  ASP ASP A . n 
A 1 53  THR 53  55  55  THR THR A . n 
A 1 54  SER 54  56  56  SER SER A . n 
A 1 55  ASN 55  57  57  ASN ASN A . n 
A 1 56  THR 56  58  58  THR THR A . n 
A 1 57  LEU 57  59  59  LEU LEU A . n 
A 1 58  THR 58  60  60  THR THR A . n 
A 1 59  ASN 59  61  61  ASN ASN A . n 
A 1 60  ILE 60  62  62  ILE ILE A . n 
A 1 61  GLU 61  63  63  GLU GLU A . n 
A 1 62  TRP 62  64  64  TRP TRP A . n 
A 1 63  ALA 63  65  65  ALA ALA A . n 
A 1 64  PRO 64  66  66  PRO PRO A . n 
A 1 65  GLY 65  67  67  GLY GLY A . n 
A 1 66  VAL 66  68  68  VAL VAL A . n 
A 1 67  THR 67  69  69  THR THR A . n 
A 1 68  GLU 68  70  70  GLU GLU A . n 
A 1 69  ALA 69  71  71  ALA ALA A . n 
A 1 70  GLY 70  72  72  GLY GLY A . n 
A 1 71  ARG 71  73  73  ARG ARG A . n 
A 1 72  THR 72  74  74  THR THR A . n 
A 1 73  HIS 73  75  75  HIS HIS A . n 
A 1 74  PHE 74  76  76  PHE PHE A . n 
A 1 75  GLY 75  77  77  GLY GLY A . n 
A 1 76  ASN 76  78  78  ASN ASN A . n 
A 1 77  ALA 77  79  79  ALA ALA A . n 
A 1 78  SER 78  80  80  SER SER A . n 
A 1 79  ASP 79  81  81  ASP ASP A . n 
A 1 80  LYS 80  82  82  LYS LYS A . n 
A 1 81  ALA 81  83  83  ALA ALA A . n 
A 1 82  ALA 82  84  84  ALA ALA A . n 
A 1 83  SER 83  85  85  SER SER A . n 
A 1 84  LEU 84  86  86  LEU LEU A . n 
A 1 85  SER 85  87  87  SER SER A . n 
A 1 86  GLY 86  88  88  GLY GLY A . n 
A 1 87  LYS 87  89  89  LYS LYS A . n 
A 1 88  GLN 88  90  90  GLN GLN A . n 
A 1 89  ASN 89  91  91  ASN ASN A . n 
A 1 90  ASP 90  92  92  ASP ASP A . n 
A 1 91  SER 91  93  93  SER SER A . n 
A 1 92  ALA 92  94  94  ALA ALA A . n 
A 1 93  GLU 93  95  95  GLU GLU A . n 
A 1 94  VAL 94  96  96  VAL VAL A . n 
A 1 95  LYS 95  97  97  LYS LYS A . n 
A 1 96  ALA 96  98  98  ALA ALA A . n 
A 1 97  PHE 97  99  99  PHE PHE A . n 
A 1 98  ALA 98  100 100 ALA ALA A . n 
A 1 99  GLN 99  101 101 GLN GLN A . n 
A 1 100 GLU 100 102 102 GLU GLU A . n 
A 1 101 LEU 101 103 103 LEU LEU A . n 
A 1 102 ASN 102 104 104 ASN ASN A . n 
A 1 103 GLN 103 105 105 GLN GLN A . n 
A 1 104 TYR 104 106 106 TYR TYR A . n 
A 1 105 LEU 105 107 107 LEU LEU A . n 
A 1 106 SER 106 108 108 SER SER 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 GLY 109 111 111 GLY GLY A . n 
A 1 110 VAL 110 112 112 VAL VAL A . n 
A 1 111 THR 111 113 113 THR THR A . n 
A 1 112 THR 112 114 114 THR THR A . n 
A 1 113 VAL 113 115 115 VAL VAL A . n 
A 1 114 GLN 114 116 116 GLN GLN A . n 
A 1 115 SER 115 117 117 SER SER A . n 
A 1 116 GLN 116 118 118 GLN GLN A . n 
A 1 117 GLN 117 119 119 GLN GLN A . n 
A 1 118 GLY 118 120 120 GLY GLY A . n 
A 1 119 THR 119 121 121 THR THR 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 ILE 122 124 124 ILE ILE A . n 
A 1 123 SER 123 125 125 SER SER A . n 
A 1 124 GLY 124 126 126 GLY GLY A . n 
A 1 125 LEU 125 127 127 LEU LEU A . n 
A 1 126 LYS 126 128 128 LYS LYS A . n 
A 1 127 PRO 127 129 129 PRO PRO A . n 
A 1 128 GLY 128 130 130 GLY GLY A . n 
A 1 129 TYR 129 131 131 TYR TYR A . n 
A 1 130 TYR 130 132 132 TYR TYR A . n 
A 1 131 LEU 131 133 133 LEU LEU A . n 
A 1 132 ILE 132 134 134 ILE ILE A . n 
A 1 133 LYS 133 135 135 LYS LYS A . n 
A 1 134 ASP 134 136 136 ASP ASP A . n 
A 1 135 SER 135 137 137 SER SER A . n 
A 1 136 ARG 136 138 138 ARG ARG A . n 
A 1 137 GLY 137 139 139 GLY GLY A . n 
A 1 138 SER 138 140 140 SER SER A . n 
A 1 139 LEU 139 141 141 LEU LEU A . n 
A 1 140 ASP 140 142 142 ASP ASP A . n 
A 1 141 ASN 141 143 143 ASN ASN A . n 
A 1 142 LYS 142 144 144 LYS LYS A . n 
A 1 143 LYS 143 145 145 LYS LYS A . n 
A 1 144 GLY 144 146 146 GLY GLY A . n 
A 1 145 HIS 145 147 147 HIS HIS A . n 
A 1 146 ALA 146 148 148 ALA ALA A . n 
A 1 147 TYR 147 149 149 TYR TYR A . n 
A 1 148 THR 148 150 150 THR THR A . n 
A 1 149 SER 149 151 151 SER SER A . n 
A 1 150 PHE 150 152 152 PHE PHE A . n 
A 1 151 MET 151 153 153 MET MET A . n 
A 1 152 LEU 152 154 154 LEU LEU A . n 
A 1 153 GLN 153 155 155 GLN GLN A . n 
A 1 154 VAL 154 156 156 VAL VAL A . n 
A 1 155 ALA 155 157 157 ALA ALA A . n 
A 1 156 LYS 156 158 158 LYS LYS A . n 
A 1 157 ASP 157 159 159 ASP ASP A . n 
A 1 158 THR 158 160 160 THR THR A . n 
A 1 159 THR 159 161 161 THR THR A . n 
A 1 160 VAL 160 162 162 VAL VAL A . n 
A 1 161 ALA 161 163 163 ALA ALA A . n 
A 1 162 VAL 162 164 164 VAL VAL A . n 
A 1 163 LYS 163 165 165 LYS LYS A . n 
A 1 164 ALA 164 166 166 ALA ALA A . n 
A 1 165 ASP 165 167 167 ASP ASP A . n 
A 1 166 VAL 166 168 168 VAL VAL A . n 
A 1 167 PRO 167 169 169 PRO PRO A . n 
A 1 168 THR 168 170 170 THR THR A . n 
A 1 169 LEU 169 171 171 LEU LEU A . n 
A 1 170 THR 170 172 172 THR THR A . n 
A 1 171 LYS 171 173 173 LYS LYS A . n 
A 1 172 GLN 172 174 174 GLN GLN A . n 
A 1 173 VAL 173 175 175 VAL VAL A . n 
A 1 174 ARG 174 176 176 ARG ARG A . n 
A 1 175 ALA 175 177 177 ALA ALA A . n 
A 1 176 ASN 176 178 178 ASN ASN A . n 
A 1 177 GLY 177 179 179 GLY GLY A . n 
A 1 178 SER 178 180 180 SER SER A . n 
A 1 179 GLN 179 181 181 GLN GLN A . n 
A 1 180 ASN 180 182 182 ASN ASN A . n 
A 1 181 TYR 181 183 183 TYR TYR A . n 
A 1 182 THR 182 184 184 THR THR A . n 
A 1 183 ALA 183 185 185 ALA ALA A . n 
A 1 184 ALA 184 186 186 ALA ALA A . n 
A 1 185 THR 185 187 187 THR THR A . n 
A 1 186 ASP 186 188 188 ASP ASP A . n 
A 1 187 TYR 187 189 189 TYR TYR A . n 
A 1 188 ARG 188 190 190 ARG ARG A . n 
A 1 189 ILE 189 191 191 ILE ILE A . n 
A 1 190 GLY 190 192 192 GLY GLY A . n 
A 1 191 GLN 191 193 193 GLN GLN A . n 
A 1 192 ASN 192 194 194 ASN ASN A . n 
A 1 193 ILE 193 195 195 ILE ILE A . n 
A 1 194 LEU 194 196 196 LEU LEU A . n 
A 1 195 PHE 195 197 197 PHE PHE A . n 
A 1 196 GLN 196 198 198 GLN GLN A . n 
A 1 197 ILE 197 199 199 ILE ILE A . n 
A 1 198 THR 198 200 200 THR THR A . n 
A 1 199 ALA 199 201 201 ALA ALA A . n 
A 1 200 THR 200 202 202 THR THR A . n 
A 1 201 LEU 201 203 203 LEU LEU A . n 
A 1 202 PRO 202 204 204 PRO PRO A . n 
A 1 203 SER 203 205 205 SER SER A . n 
A 1 204 ASN 204 206 206 ASN ASN A . n 
A 1 205 TYR 205 207 207 TYR TYR A . n 
A 1 206 ALA 206 208 208 ALA ALA A . n 
A 1 207 ASP 207 209 209 ASP ASP A . n 
A 1 208 PHE 208 210 210 PHE PHE A . n 
A 1 209 THR 209 211 211 THR THR A . n 
A 1 210 ARG 210 212 212 ARG ARG A . n 
A 1 211 TYR 211 213 213 TYR TYR A . n 
A 1 212 GLU 212 214 214 GLU GLU A . n 
A 1 213 PHE 213 215 215 PHE PHE A . n 
A 1 214 THR 214 216 216 THR THR A . n 
A 1 215 ILE 215 217 217 ILE ILE A . n 
A 1 216 LYS 216 218 218 LYS LYS A . n 
A 1 217 ASP 217 219 219 ASP ASP A . n 
A 1 218 THR 218 220 220 THR THR A . n 
A 1 219 ILE 219 221 221 ILE ILE A . n 
A 1 220 PRO 220 222 222 PRO PRO A . n 
A 1 221 ALA 221 223 223 ALA ALA A . n 
A 1 222 GLY 222 224 224 GLY GLY A . n 
A 1 223 MET 223 225 225 MET MET A . n 
A 1 224 THR 224 226 226 THR THR A . n 
A 1 225 TYR 225 227 227 TYR TYR 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 ASP 228 230 230 ASP ASP A . n 
A 1 229 ALA 229 231 231 ALA ALA A . n 
A 1 230 GLN 230 232 232 GLN GLN A . n 
A 1 231 VAL 231 233 233 VAL VAL A . n 
A 1 232 TYR 232 234 234 TYR TYR A . n 
A 1 233 LEU 233 235 235 LEU LEU A . n 
A 1 234 GLN 234 236 236 GLN GLN A . n 
A 1 235 GLU 235 237 237 GLU GLU A . n 
A 1 236 GLY 236 238 238 GLY GLY A . n 
A 1 237 GLY 237 239 239 GLY GLY A . n 
A 1 238 THR 238 240 240 THR THR A . n 
A 1 239 GLU 239 241 241 GLU GLU A . n 
A 1 240 LYS 240 242 242 LYS LYS A . n 
A 1 241 ASP 241 243 243 ASP ASP A . n 
A 1 242 ILE 242 244 244 ILE ILE A . n 
A 1 243 SER 243 245 245 SER SER A . n 
A 1 244 THR 244 246 246 THR THR A . n 
A 1 245 PHE 245 247 247 PHE PHE A . n 
A 1 246 PHE 246 248 248 PHE PHE A . n 
A 1 247 PRO 247 249 249 PRO PRO A . n 
A 1 248 ILE 248 250 250 ILE ILE A . n 
A 1 249 SER 249 251 251 SER SER A . n 
A 1 250 TYR 250 252 252 TYR TYR A . n 
A 1 251 THR 251 253 253 THR THR A . n 
A 1 252 GLY 252 254 254 GLY GLY A . n 
A 1 253 ASN 253 255 255 ASN ASN A . n 
A 1 254 VAL 254 256 256 VAL VAL A . n 
A 1 255 ILE 255 257 257 ILE ILE A . n 
A 1 256 THR 256 258 258 THR THR A . n 
A 1 257 ILE 257 259 259 ILE ILE A . n 
A 1 258 THR 258 260 260 THR THR A . n 
A 1 259 PRO 259 261 261 PRO PRO A . n 
A 1 260 GLY 260 262 262 GLY GLY 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 TYR 264 266 266 TYR TYR A . n 
A 1 265 VAL 265 267 267 VAL VAL A . n 
A 1 266 GLN 266 268 268 GLN GLN A . n 
A 1 267 ASP 267 269 269 ASP ASP A . n 
A 1 268 VAL 268 270 270 VAL VAL A . n 
A 1 269 LYS 269 271 271 LYS LYS A . n 
A 1 270 VAL 270 272 272 VAL VAL A . n 
A 1 271 SER 271 273 273 SER SER 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 ASN 283 285 285 ASN ASN A . n 
A 1 284 ASP 284 286 286 ASP ASP A . n 
A 1 285 ASP 285 287 287 ASP ASP A . n 
A 1 286 ALA 286 288 288 ALA ALA A . n 
A 1 287 VAL 287 289 289 VAL VAL A . n 
A 1 288 MET 288 290 290 MET MET A . n 
A 1 289 GLY 289 291 291 GLY GLY A . n 
A 1 290 GLY 290 292 292 GLY GLY A . n 
A 1 291 LEU 291 293 293 LEU LEU 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 PRO 294 296 296 PRO PRO A . n 
A 1 295 ASN 295 297 297 ASN ASN A . n 
A 1 296 ILE 296 298 298 ILE ILE A . n 
A 1 297 ALA 297 299 299 ALA ALA A . n 
A 1 298 ARG 298 300 300 ARG ARG 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 ASP 304 306 306 ASP ASP 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 GLY 307 309 309 GLY GLY A . n 
A 1 308 PHE 308 310 310 PHE PHE A . n 
A 1 309 THR 309 311 311 THR THR 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 GLU 314 316 316 GLU GLU A . n 
A 1 315 THR 315 317 317 THR THR A . n 
A 1 316 PRO 316 318 318 PRO PRO A . n 
A 1 317 ASP 317 319 319 ASP ASP A . n 
A 1 318 THR 318 320 320 THR THR A . n 
A 1 319 LYS 319 321 321 LYS LYS A . n 
A 1 320 ALA 320 322 322 ALA ALA A . n 
A 1 321 ASN 321 323 323 ASN ASN 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 GLN 326 328 328 GLN GLN A . n 
A 1 327 LEU 327 329 329 LEU LEU A . n 
A 1 328 LYS 328 330 330 LYS LYS A . n 
A 1 329 VAL 329 331 331 VAL VAL A . n 
A 1 330 ASN 330 332 332 ASN ASN 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 LYS 333 335 335 LYS LYS A . n 
A 1 334 GLU 334 336 336 GLU GLU A . n 
A 1 335 ASN 335 337 337 ASN ASN A . n 
A 1 336 GLN 336 338 338 GLN GLN A . n 
A 1 337 GLN 337 339 339 GLN GLN A . n 
A 1 338 ALA 338 340 340 ALA ALA A . n 
A 1 339 LEU 339 341 341 LEU LEU 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 VAL 350 352 352 VAL VAL 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 THR 355 357 357 THR THR A . n 
A 1 356 GLU 356 358 358 GLU GLU A . n 
A 1 357 ILE 357 359 359 ILE ILE A . n 
A 1 358 LYS 358 360 360 LYS LYS A . n 
A 1 359 LYS 359 361 361 LYS LYS A . n 
A 1 360 PHE 360 362 362 PHE PHE 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 ASP 363 365 365 ASP ASP A . n 
A 1 364 SER 364 366 366 SER SER A . n 
A 1 365 ASN 365 367 367 ASN ASN 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 LYS 371 373 373 LYS LYS A . n 
A 1 372 GLY 372 374 374 GLY GLY A . n 
A 1 373 LEU 373 375 375 LEU LEU A . n 
A 1 374 ASP 374 376 376 ASP ASP A . n 
A 1 375 SER 375 377 377 SER SER 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 VAL 385 387 387 VAL VAL A . n 
A 1 386 PRO 386 388 388 PRO PRO A . n 
A 1 387 SER 387 389 389 SER SER 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 ALA 391 393 393 ALA ALA 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 SER 400 402 402 SER SER A . n 
A 1 401 GLY 401 403 403 GLY GLY 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 ASP 408 410 410 ASP ASP 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 ASN 411 413 413 ASN ASN A . n 
A 1 412 LEU 412 414 414 LEU LEU A . n 
A 1 413 THR 413 415 415 THR THR A . n 
A 1 414 ALA 414 416 416 ALA ALA 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 SER 420 422 422 SER SER 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 THR 427 429 429 THR THR A . n 
A 1 428 GLY 428 430 430 GLY GLY A . n 
A 1 429 ILE 429 431 431 ILE ILE A . n 
A 1 430 ILE 430 432 432 ILE ILE A . n 
A 1 431 THR 431 433 433 THR THR 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 444 446 446 ASN ASN A . n 
A 1 445 THR 445 447 447 THR THR 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 
B 1 1   MET 1   3   ?   ?   ?   B . n 
B 1 2   GLY 2   4   ?   ?   ?   B . n 
B 1 3   SER 3   5   ?   ?   ?   B . n 
B 1 4   SER 4   6   ?   ?   ?   B . n 
B 1 5   HIS 5   7   ?   ?   ?   B . n 
B 1 6   HIS 6   8   ?   ?   ?   B . n 
B 1 7   HIS 7   9   ?   ?   ?   B . n 
B 1 8   HIS 8   10  ?   ?   ?   B . n 
B 1 9   HIS 9   11  ?   ?   ?   B . n 
B 1 10  HIS 10  12  ?   ?   ?   B . n 
B 1 11  SER 11  13  ?   ?   ?   B . n 
B 1 12  SER 12  14  ?   ?   ?   B . n 
B 1 13  GLY 13  15  ?   ?   ?   B . n 
B 1 14  LEU 14  16  ?   ?   ?   B . n 
B 1 15  VAL 15  17  ?   ?   ?   B . n 
B 1 16  PRO 16  18  ?   ?   ?   B . n 
B 1 17  ARG 17  19  ?   ?   ?   B . n 
B 1 18  ARG 18  20  ?   ?   ?   B . n 
B 1 19  GLY 19  21  ?   ?   ?   B . n 
B 1 20  SER 20  22  ?   ?   ?   B . n 
B 1 21  HIS 21  23  ?   ?   ?   B . n 
B 1 22  MET 22  24  ?   ?   ?   B . n 
B 1 23  SER 23  25  ?   ?   ?   B . n 
B 1 24  ALA 24  26  ?   ?   ?   B . n 
B 1 25  ASP 25  27  ?   ?   ?   B . n 
B 1 26  THR 26  28  ?   ?   ?   B . n 
B 1 27  THR 27  29  29  THR THR B . n 
B 1 28  TYR 28  30  30  TYR TYR B . n 
B 1 29  THR 29  31  31  THR THR B . n 
B 1 30  ILE 30  32  32  ILE ILE B . n 
B 1 31  GLN 31  33  33  GLN GLN B . n 
B 1 32  LEU 32  34  34  LEU LEU B . n 
B 1 33  SER 33  35  35  SER SER B . n 
B 1 34  GLY 34  36  36  GLY GLY B . n 
B 1 35  THR 35  37  37  THR THR B . n 
B 1 36  SER 36  38  38  SER SER B . n 
B 1 37  GLU 37  39  39  GLU GLU B . n 
B 1 38  GLY 38  40  40  GLY GLY B . n 
B 1 39  HIS 39  41  41  HIS HIS B . n 
B 1 40  TYR 40  42  42  TYR TYR B . n 
B 1 41  TYR 41  43  43  TYR TYR B . n 
B 1 42  GLU 42  44  44  GLU GLU B . n 
B 1 43  VAL 43  45  45  VAL VAL B . n 
B 1 44  TYR 44  46  46  TYR TYR B . n 
B 1 45  HIS 45  47  47  HIS HIS B . n 
B 1 46  ILE 46  48  48  ILE ILE B . n 
B 1 47  PHE 47  49  49  PHE PHE B . n 
B 1 48  SER 48  50  50  SER SER B . n 
B 1 49  GLY 49  51  51  GLY GLY B . n 
B 1 50  THR 50  52  52  THR THR B . n 
B 1 51  LEU 51  53  53  LEU LEU B . n 
B 1 52  ASP 52  54  54  ASP ASP B . n 
B 1 53  THR 53  55  55  THR THR B . n 
B 1 54  SER 54  56  56  SER SER B . n 
B 1 55  ASN 55  57  57  ASN ASN B . n 
B 1 56  THR 56  58  58  THR THR B . n 
B 1 57  LEU 57  59  59  LEU LEU B . n 
B 1 58  THR 58  60  60  THR THR B . n 
B 1 59  ASN 59  61  61  ASN ASN B . n 
B 1 60  ILE 60  62  62  ILE ILE B . n 
B 1 61  GLU 61  63  63  GLU GLU B . n 
B 1 62  TRP 62  64  64  TRP TRP B . n 
B 1 63  ALA 63  65  65  ALA ALA B . n 
B 1 64  PRO 64  66  66  PRO PRO B . n 
B 1 65  GLY 65  67  67  GLY GLY B . n 
B 1 66  VAL 66  68  68  VAL VAL B . n 
B 1 67  THR 67  69  69  THR THR B . n 
B 1 68  GLU 68  70  70  GLU GLU B . n 
B 1 69  ALA 69  71  71  ALA ALA B . n 
B 1 70  GLY 70  72  72  GLY GLY B . n 
B 1 71  ARG 71  73  73  ARG ARG B . n 
B 1 72  THR 72  74  74  THR THR B . n 
B 1 73  HIS 73  75  75  HIS HIS B . n 
B 1 74  PHE 74  76  76  PHE PHE B . n 
B 1 75  GLY 75  77  77  GLY GLY B . n 
B 1 76  ASN 76  78  78  ASN ASN B . n 
B 1 77  ALA 77  79  79  ALA ALA B . n 
B 1 78  SER 78  80  80  SER SER B . n 
B 1 79  ASP 79  81  81  ASP ASP B . n 
B 1 80  LYS 80  82  82  LYS LYS B . n 
B 1 81  ALA 81  83  83  ALA ALA B . n 
B 1 82  ALA 82  84  84  ALA ALA B . n 
B 1 83  SER 83  85  85  SER SER B . n 
B 1 84  LEU 84  86  86  LEU LEU B . n 
B 1 85  SER 85  87  87  SER SER B . n 
B 1 86  GLY 86  88  88  GLY GLY B . n 
B 1 87  LYS 87  89  89  LYS LYS B . n 
B 1 88  GLN 88  90  90  GLN GLN B . n 
B 1 89  ASN 89  91  91  ASN ASN B . n 
B 1 90  ASP 90  92  92  ASP ASP B . n 
B 1 91  SER 91  93  93  SER SER B . n 
B 1 92  ALA 92  94  94  ALA ALA B . n 
B 1 93  GLU 93  95  95  GLU GLU B . n 
B 1 94  VAL 94  96  96  VAL VAL B . n 
B 1 95  LYS 95  97  97  LYS LYS B . n 
B 1 96  ALA 96  98  98  ALA ALA B . n 
B 1 97  PHE 97  99  99  PHE PHE B . n 
B 1 98  ALA 98  100 100 ALA ALA B . n 
B 1 99  GLN 99  101 101 GLN GLN B . n 
B 1 100 GLU 100 102 102 GLU GLU B . n 
B 1 101 LEU 101 103 103 LEU LEU B . n 
B 1 102 ASN 102 104 104 ASN ASN B . n 
B 1 103 GLN 103 105 105 GLN GLN B . n 
B 1 104 TYR 104 106 106 TYR TYR B . n 
B 1 105 LEU 105 107 107 LEU LEU B . n 
B 1 106 SER 106 108 108 SER SER B . n 
B 1 107 SER 107 109 109 SER SER B . n 
B 1 108 ALA 108 110 110 ALA ALA B . n 
B 1 109 GLY 109 111 111 GLY GLY B . n 
B 1 110 VAL 110 112 112 VAL VAL B . n 
B 1 111 THR 111 113 113 THR THR B . n 
B 1 112 THR 112 114 114 THR THR B . n 
B 1 113 VAL 113 115 115 VAL VAL B . n 
B 1 114 GLN 114 116 116 GLN GLN B . n 
B 1 115 SER 115 117 117 SER SER B . n 
B 1 116 GLN 116 118 118 GLN GLN B . n 
B 1 117 GLN 117 119 119 GLN GLN B . n 
B 1 118 GLY 118 120 120 GLY GLY B . n 
B 1 119 THR 119 121 121 THR THR B . n 
B 1 120 THR 120 122 122 THR THR B . n 
B 1 121 THR 121 123 123 THR THR B . n 
B 1 122 ILE 122 124 124 ILE ILE B . n 
B 1 123 SER 123 125 125 SER SER B . n 
B 1 124 GLY 124 126 126 GLY GLY B . n 
B 1 125 LEU 125 127 127 LEU LEU B . n 
B 1 126 LYS 126 128 128 LYS LYS B . n 
B 1 127 PRO 127 129 129 PRO PRO B . n 
B 1 128 GLY 128 130 130 GLY GLY B . n 
B 1 129 TYR 129 131 131 TYR TYR B . n 
B 1 130 TYR 130 132 132 TYR TYR B . n 
B 1 131 LEU 131 133 133 LEU LEU B . n 
B 1 132 ILE 132 134 134 ILE ILE B . n 
B 1 133 LYS 133 135 135 LYS LYS B . n 
B 1 134 ASP 134 136 136 ASP ASP B . n 
B 1 135 SER 135 137 137 SER SER B . n 
B 1 136 ARG 136 138 138 ARG ARG B . n 
B 1 137 GLY 137 139 139 GLY GLY B . n 
B 1 138 SER 138 140 140 SER SER B . n 
B 1 139 LEU 139 141 141 LEU LEU B . n 
B 1 140 ASP 140 142 142 ASP ASP B . n 
B 1 141 ASN 141 143 143 ASN ASN B . n 
B 1 142 LYS 142 144 144 LYS LYS B . n 
B 1 143 LYS 143 145 145 LYS LYS B . n 
B 1 144 GLY 144 146 146 GLY GLY B . n 
B 1 145 HIS 145 147 147 HIS HIS B . n 
B 1 146 ALA 146 148 148 ALA ALA B . n 
B 1 147 TYR 147 149 149 TYR TYR B . n 
B 1 148 THR 148 150 150 THR THR B . n 
B 1 149 SER 149 151 151 SER SER B . n 
B 1 150 PHE 150 152 152 PHE PHE B . n 
B 1 151 MET 151 153 153 MET MET B . n 
B 1 152 LEU 152 154 154 LEU LEU B . n 
B 1 153 GLN 153 155 155 GLN GLN B . n 
B 1 154 VAL 154 156 156 VAL VAL B . n 
B 1 155 ALA 155 157 157 ALA ALA B . n 
B 1 156 LYS 156 158 158 LYS LYS B . n 
B 1 157 ASP 157 159 159 ASP ASP B . n 
B 1 158 THR 158 160 160 THR THR B . n 
B 1 159 THR 159 161 161 THR THR B . n 
B 1 160 VAL 160 162 162 VAL VAL B . n 
B 1 161 ALA 161 163 163 ALA ALA B . n 
B 1 162 VAL 162 164 164 VAL VAL B . n 
B 1 163 LYS 163 165 165 LYS LYS B . n 
B 1 164 ALA 164 166 166 ALA ALA B . n 
B 1 165 ASP 165 167 167 ASP ASP B . n 
B 1 166 VAL 166 168 168 VAL VAL B . n 
B 1 167 PRO 167 169 169 PRO PRO B . n 
B 1 168 THR 168 170 170 THR THR B . n 
B 1 169 LEU 169 171 171 LEU LEU B . n 
B 1 170 THR 170 172 172 THR THR B . n 
B 1 171 LYS 171 173 173 LYS LYS B . n 
B 1 172 GLN 172 174 174 GLN GLN B . n 
B 1 173 VAL 173 175 175 VAL VAL B . n 
B 1 174 ARG 174 176 176 ARG ARG B . n 
B 1 175 ALA 175 177 177 ALA ALA B . n 
B 1 176 ASN 176 178 178 ASN ASN B . n 
B 1 177 GLY 177 179 179 GLY GLY B . n 
B 1 178 SER 178 180 180 SER SER B . n 
B 1 179 GLN 179 181 181 GLN GLN B . n 
B 1 180 ASN 180 182 182 ASN ASN B . n 
B 1 181 TYR 181 183 183 TYR TYR B . n 
B 1 182 THR 182 184 184 THR THR B . n 
B 1 183 ALA 183 185 185 ALA ALA B . n 
B 1 184 ALA 184 186 186 ALA ALA B . n 
B 1 185 THR 185 187 187 THR THR B . n 
B 1 186 ASP 186 188 188 ASP ASP B . n 
B 1 187 TYR 187 189 189 TYR TYR B . n 
B 1 188 ARG 188 190 190 ARG ARG B . n 
B 1 189 ILE 189 191 191 ILE ILE B . n 
B 1 190 GLY 190 192 192 GLY GLY B . n 
B 1 191 GLN 191 193 193 GLN GLN B . n 
B 1 192 ASN 192 194 194 ASN ASN B . n 
B 1 193 ILE 193 195 195 ILE ILE B . n 
B 1 194 LEU 194 196 196 LEU LEU B . n 
B 1 195 PHE 195 197 197 PHE PHE B . n 
B 1 196 GLN 196 198 198 GLN GLN B . n 
B 1 197 ILE 197 199 199 ILE ILE B . n 
B 1 198 THR 198 200 200 THR THR B . n 
B 1 199 ALA 199 201 201 ALA ALA B . n 
B 1 200 THR 200 202 202 THR THR B . n 
B 1 201 LEU 201 203 203 LEU LEU B . n 
B 1 202 PRO 202 204 204 PRO PRO B . n 
B 1 203 SER 203 205 205 SER SER B . n 
B 1 204 ASN 204 206 206 ASN ASN B . n 
B 1 205 TYR 205 207 207 TYR TYR B . n 
B 1 206 ALA 206 208 208 ALA ALA B . n 
B 1 207 ASP 207 209 209 ASP ASP B . n 
B 1 208 PHE 208 210 210 PHE PHE B . n 
B 1 209 THR 209 211 211 THR THR B . n 
B 1 210 ARG 210 212 212 ARG ARG B . n 
B 1 211 TYR 211 213 213 TYR TYR B . n 
B 1 212 GLU 212 214 214 GLU GLU B . n 
B 1 213 PHE 213 215 215 PHE PHE B . n 
B 1 214 THR 214 216 216 THR THR B . n 
B 1 215 ILE 215 217 217 ILE ILE B . n 
B 1 216 LYS 216 218 218 LYS LYS B . n 
B 1 217 ASP 217 219 219 ASP ASP B . n 
B 1 218 THR 218 220 220 THR THR B . n 
B 1 219 ILE 219 221 221 ILE ILE B . n 
B 1 220 PRO 220 222 222 PRO PRO B . n 
B 1 221 ALA 221 223 223 ALA ALA B . n 
B 1 222 GLY 222 224 224 GLY GLY B . n 
B 1 223 MET 223 225 225 MET MET B . n 
B 1 224 THR 224 226 226 THR THR B . n 
B 1 225 TYR 225 227 227 TYR TYR B . n 
B 1 226 ASN 226 228 228 ASN ASN B . n 
B 1 227 ASN 227 229 229 ASN ASN B . n 
B 1 228 ASP 228 230 230 ASP ASP B . n 
B 1 229 ALA 229 231 231 ALA ALA B . n 
B 1 230 GLN 230 232 232 GLN GLN B . n 
B 1 231 VAL 231 233 233 VAL VAL B . n 
B 1 232 TYR 232 234 234 TYR TYR B . n 
B 1 233 LEU 233 235 235 LEU LEU B . n 
B 1 234 GLN 234 236 236 GLN GLN B . n 
B 1 235 GLU 235 237 237 GLU GLU B . n 
B 1 236 GLY 236 238 238 GLY GLY B . n 
B 1 237 GLY 237 239 239 GLY GLY B . n 
B 1 238 THR 238 240 240 THR THR B . n 
B 1 239 GLU 239 241 241 GLU GLU B . n 
B 1 240 LYS 240 242 242 LYS LYS B . n 
B 1 241 ASP 241 243 243 ASP ASP B . n 
B 1 242 ILE 242 244 244 ILE ILE B . n 
B 1 243 SER 243 245 245 SER SER B . n 
B 1 244 THR 244 246 246 THR THR B . n 
B 1 245 PHE 245 247 247 PHE PHE B . n 
B 1 246 PHE 246 248 248 PHE PHE B . n 
B 1 247 PRO 247 249 249 PRO PRO B . n 
B 1 248 ILE 248 250 250 ILE ILE B . n 
B 1 249 SER 249 251 251 SER SER B . n 
B 1 250 TYR 250 252 252 TYR TYR B . n 
B 1 251 THR 251 253 253 THR THR B . n 
B 1 252 GLY 252 254 254 GLY GLY B . n 
B 1 253 ASN 253 255 255 ASN ASN B . n 
B 1 254 VAL 254 256 256 VAL VAL B . n 
B 1 255 ILE 255 257 257 ILE ILE B . n 
B 1 256 THR 256 258 258 THR THR B . n 
B 1 257 ILE 257 259 259 ILE ILE B . n 
B 1 258 THR 258 260 260 THR THR B . n 
B 1 259 PRO 259 261 261 PRO PRO B . n 
B 1 260 GLY 260 262 262 GLY GLY B . n 
B 1 261 ASP 261 263 263 ASP ASP B . n 
B 1 262 LEU 262 264 264 LEU LEU B . n 
B 1 263 LYS 263 265 265 LYS LYS B . n 
B 1 264 TYR 264 266 266 TYR TYR B . n 
B 1 265 VAL 265 267 267 VAL VAL B . n 
B 1 266 GLN 266 268 268 GLN GLN B . n 
B 1 267 ASP 267 269 269 ASP ASP B . n 
B 1 268 VAL 268 270 270 VAL VAL B . n 
B 1 269 LYS 269 271 271 LYS LYS B . n 
B 1 270 VAL 270 272 272 VAL VAL B . n 
B 1 271 SER 271 273 273 SER SER B . n 
B 1 272 SER 272 274 274 SER SER B . n 
B 1 273 LYS 273 275 275 LYS LYS B . n 
B 1 274 ILE 274 276 276 ILE ILE B . n 
B 1 275 VAL 275 277 277 VAL VAL B . n 
B 1 276 ILE 276 278 278 ILE ILE B . n 
B 1 277 ARG 277 279 279 ARG ARG B . n 
B 1 278 TYR 278 280 280 TYR TYR B . n 
B 1 279 THR 279 281 281 THR THR B . n 
B 1 280 ALA 280 282 282 ALA ALA B . n 
B 1 281 ARG 281 283 283 ARG ARG B . n 
B 1 282 LEU 282 284 284 LEU LEU B . n 
B 1 283 ASN 283 285 285 ASN ASN B . n 
B 1 284 ASP 284 286 286 ASP ASP B . n 
B 1 285 ASP 285 287 287 ASP ASP B . n 
B 1 286 ALA 286 288 288 ALA ALA B . n 
B 1 287 VAL 287 289 289 VAL VAL B . n 
B 1 288 MET 288 290 290 MET MET B . n 
B 1 289 GLY 289 291 291 GLY GLY B . n 
B 1 290 GLY 290 292 292 GLY GLY B . n 
B 1 291 LEU 291 293 293 LEU LEU B . n 
B 1 292 GLY 292 294 294 GLY GLY B . n 
B 1 293 ASN 293 295 295 ASN ASN B . n 
B 1 294 PRO 294 296 296 PRO PRO B . n 
B 1 295 ASN 295 297 297 ASN ASN B . n 
B 1 296 ILE 296 298 298 ILE ILE B . n 
B 1 297 ALA 297 299 299 ALA ALA B . n 
B 1 298 ARG 298 300 300 ARG ARG B . n 
B 1 299 LEU 299 301 301 LEU LEU B . n 
B 1 300 THR 300 302 302 THR THR B . n 
B 1 301 TYR 301 303 303 TYR TYR B . n 
B 1 302 SER 302 304 304 SER SER B . n 
B 1 303 ASN 303 305 305 ASN ASN B . n 
B 1 304 ASP 304 306 306 ASP ASP B . n 
B 1 305 PRO 305 307 307 PRO PRO B . n 
B 1 306 ASN 306 308 308 ASN ASN B . n 
B 1 307 GLY 307 309 309 GLY GLY B . n 
B 1 308 PHE 308 310 310 PHE PHE B . n 
B 1 309 THR 309 311 311 THR THR B . n 
B 1 310 SER 310 312 312 SER SER B . n 
B 1 311 THR 311 313 313 THR THR B . n 
B 1 312 THR 312 314 314 THR THR B . n 
B 1 313 ALA 313 315 315 ALA ALA B . n 
B 1 314 GLU 314 316 316 GLU GLU B . n 
B 1 315 THR 315 317 317 THR THR B . n 
B 1 316 PRO 316 318 318 PRO PRO B . n 
B 1 317 ASP 317 319 319 ASP ASP B . n 
B 1 318 THR 318 320 320 THR THR B . n 
B 1 319 LYS 319 321 321 LYS LYS B . n 
B 1 320 ALA 320 322 322 ALA ALA B . n 
B 1 321 ASN 321 323 323 ASN ASN B . n 
B 1 322 VAL 322 324 324 VAL VAL B . n 
B 1 323 TYR 323 325 325 TYR TYR B . n 
B 1 324 THR 324 326 326 THR THR B . n 
B 1 325 TYR 325 327 327 TYR TYR B . n 
B 1 326 GLN 326 328 328 GLN GLN B . n 
B 1 327 LEU 327 329 329 LEU LEU B . n 
B 1 328 LYS 328 330 330 LYS LYS B . n 
B 1 329 VAL 329 331 331 VAL VAL B . n 
B 1 330 ASN 330 332 332 ASN ASN B . n 
B 1 331 LYS 331 333 333 LYS LYS B . n 
B 1 332 VAL 332 334 334 VAL VAL B . n 
B 1 333 LYS 333 335 335 LYS LYS B . n 
B 1 334 GLU 334 336 336 GLU GLU B . n 
B 1 335 ASN 335 337 337 ASN ASN B . n 
B 1 336 GLN 336 338 338 GLN GLN B . n 
B 1 337 GLN 337 339 339 GLN GLN B . n 
B 1 338 ALA 338 340 340 ALA ALA B . n 
B 1 339 LEU 339 341 341 LEU LEU B . n 
B 1 340 ALA 340 342 342 ALA ALA B . n 
B 1 341 GLY 341 343 343 GLY GLY B . n 
B 1 342 ALA 342 344 344 ALA ALA B . n 
B 1 343 GLY 343 345 345 GLY GLY B . n 
B 1 344 PHE 344 346 346 PHE PHE B . n 
B 1 345 THR 345 347 347 THR THR B . n 
B 1 346 LEU 346 348 348 LEU LEU B . n 
B 1 347 TYR 347 349 349 TYR TYR B . n 
B 1 348 LYS 348 350 350 LYS LYS B . n 
B 1 349 LYS 349 351 351 LYS LYS B . n 
B 1 350 VAL 350 352 352 VAL VAL B . n 
B 1 351 ASN 351 353 353 ASN ASN B . n 
B 1 352 ASN 352 354 354 ASN ASN B . n 
B 1 353 GLN 353 355 355 GLN GLN B . n 
B 1 354 TYR 354 356 356 TYR TYR B . n 
B 1 355 THR 355 357 357 THR THR B . n 
B 1 356 GLU 356 358 358 GLU GLU B . n 
B 1 357 ILE 357 359 359 ILE ILE B . n 
B 1 358 LYS 358 360 360 LYS LYS B . n 
B 1 359 LYS 359 361 361 LYS LYS B . n 
B 1 360 PHE 360 362 362 PHE PHE B . n 
B 1 361 GLU 361 363 363 GLU GLU B . n 
B 1 362 ALA 362 364 364 ALA ALA B . n 
B 1 363 ASP 363 365 365 ASP ASP B . n 
B 1 364 SER 364 366 366 SER SER B . n 
B 1 365 ASN 365 367 367 ASN ASN B . n 
B 1 366 SER 366 368 368 SER SER B . n 
B 1 367 THR 367 369 369 THR THR B . n 
B 1 368 PHE 368 370 370 PHE PHE B . n 
B 1 369 ASP 369 371 371 ASP ASP B . n 
B 1 370 PHE 370 372 372 PHE PHE B . n 
B 1 371 LYS 371 373 373 LYS LYS B . n 
B 1 372 GLY 372 374 374 GLY GLY B . n 
B 1 373 LEU 373 375 375 LEU LEU B . n 
B 1 374 ASP 374 376 376 ASP ASP B . n 
B 1 375 SER 375 377 377 SER SER B . n 
B 1 376 GLY 376 378 378 GLY GLY B . n 
B 1 377 ASP 377 379 379 ASP ASP B . n 
B 1 378 TYR 378 380 380 TYR TYR B . n 
B 1 379 LYS 379 381 381 LYS LYS B . n 
B 1 380 LEU 380 382 382 LEU LEU B . n 
B 1 381 VAL 381 383 383 VAL VAL B . n 
B 1 382 GLU 382 384 384 GLU GLU B . n 
B 1 383 SER 383 385 385 SER SER B . n 
B 1 384 THR 384 386 386 THR THR B . n 
B 1 385 VAL 385 387 387 VAL VAL B . n 
B 1 386 PRO 386 388 388 PRO PRO B . n 
B 1 387 SER 387 389 389 SER SER B . n 
B 1 388 GLY 388 390 390 GLY GLY B . n 
B 1 389 TYR 389 391 391 TYR TYR B . n 
B 1 390 ASN 390 392 392 ASN ASN B . n 
B 1 391 ALA 391 393 393 ALA ALA B . n 
B 1 392 MET 392 394 394 MET MET B . n 
B 1 393 LYS 393 395 395 LYS LYS B . n 
B 1 394 ASP 394 396 396 ASP ASP B . n 
B 1 395 ILE 395 397 397 ILE ILE B . n 
B 1 396 GLU 396 398 398 GLU GLU B . n 
B 1 397 PHE 397 399 399 PHE PHE B . n 
B 1 398 THR 398 400 400 THR THR B . n 
B 1 399 ILE 399 401 401 ILE ILE B . n 
B 1 400 SER 400 402 402 SER SER B . n 
B 1 401 GLY 401 403 403 GLY GLY B . n 
B 1 402 THR 402 404 404 THR THR B . n 
B 1 403 ILE 403 405 405 ILE ILE B . n 
B 1 404 ASP 404 406 406 ASP ASP B . n 
B 1 405 SER 405 407 407 SER SER B . n 
B 1 406 THR 406 408 408 THR THR B . n 
B 1 407 GLY 407 409 409 GLY GLY B . n 
B 1 408 ASP 408 410 410 ASP ASP B . n 
B 1 409 LEU 409 411 411 LEU LEU B . n 
B 1 410 THR 410 412 412 THR THR B . n 
B 1 411 ASN 411 413 413 ASN ASN B . n 
B 1 412 LEU 412 414 414 LEU LEU B . n 
B 1 413 THR 413 415 415 THR THR B . n 
B 1 414 ALA 414 416 416 ALA ALA B . n 
B 1 415 THR 415 417 417 THR THR B . n 
B 1 416 SER 416 418 418 SER SER B . n 
B 1 417 ALA 417 419 419 ALA ALA B . n 
B 1 418 THR 418 420 420 THR THR B . n 
B 1 419 ALA 419 421 421 ALA ALA B . n 
B 1 420 SER 420 422 422 SER SER B . n 
B 1 421 PHE 421 423 423 PHE PHE B . n 
B 1 422 GLU 422 424 424 GLU GLU B . n 
B 1 423 THR 423 425 425 THR THR B . n 
B 1 424 ASP 424 426 426 ASP ASP B . n 
B 1 425 VAL 425 427 427 VAL VAL B . n 
B 1 426 ASN 426 428 428 ASN ASN B . n 
B 1 427 THR 427 429 429 THR THR B . n 
B 1 428 GLY 428 430 430 GLY GLY B . n 
B 1 429 ILE 429 431 431 ILE ILE B . n 
B 1 430 ILE 430 432 432 ILE ILE B . n 
B 1 431 THR 431 433 433 THR THR B . n 
B 1 432 LEU 432 434 434 LEU LEU B . n 
B 1 433 LYS 433 435 435 LYS LYS B . n 
B 1 434 VAL 434 436 436 VAL VAL B . n 
B 1 435 VAL 435 437 437 VAL VAL B . n 
B 1 436 ASN 436 438 438 ASN ASN B . n 
B 1 437 LYS 437 439 439 LYS LYS B . n 
B 1 438 GLN 438 440 440 GLN GLN B . n 
B 1 439 GLY 439 441 441 GLY GLY B . n 
B 1 440 ALA 440 442 442 ALA ALA B . n 
B 1 441 LEU 441 443 443 LEU LEU B . n 
B 1 442 LEU 442 444 444 LEU LEU B . n 
B 1 443 PRO 443 445 445 PRO PRO B . n 
B 1 444 ASN 444 446 446 ASN ASN B . n 
B 1 445 THR 445 447 447 THR THR B . n 
B 1 446 GLY 446 448 ?   ?   ?   B . n 
B 1 447 GLY 447 449 ?   ?   ?   B . n 
B 1 448 ILE 448 450 ?   ?   ?   B . n 
B 1 449 GLY 449 451 ?   ?   ?   B . n 
B 1 450 THR 450 452 ?   ?   ?   B . n 
B 1 451 THR 451 453 ?   ?   ?   B . 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 CD  ? ? CD  ? ? 'SUBJECT OF INVESTIGATION' ? 
2 GOL ? ? GOL ? ? 'SUBJECT OF INVESTIGATION' ? 
3 CL  ? ? CL  ? ? 'SUBJECT OF INVESTIGATION' ? 
4 NA  ? ? NA  ? ? 'SUBJECT OF INVESTIGATION' ? 
5 SO4 ? ? SO4 ? ? '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 
C 2 NA  1  501 2   NA  NA  A . 
D 2 NA  1  502 3   NA  NA  A . 
E 2 NA  1  503 4   NA  NA  A . 
F 2 NA  1  504 6   NA  NA  A . 
G 3 SO4 1  505 1   SO4 SO4 A . 
H 4 GOL 1  506 3   GOL GOL A . 
I 5 CD  1  507 1   CD  CD  A . 
J 5 CD  1  508 2   CD  CD  A . 
K 5 CD  1  509 3   CD  CD  A . 
L 6 CL  1  510 7   CL  CL  A . 
M 2 NA  1  501 1   NA  NA  B . 
N 2 NA  1  502 5   NA  NA  B . 
O 3 SO4 1  503 2   SO4 SO4 B . 
P 5 CD  1  504 4   CD  CD  B . 
Q 5 CD  1  505 5   CD  CD  B . 
R 5 CD  1  506 6   CD  CD  B . 
S 7 HOH 1  601 39  HOH HOH A . 
S 7 HOH 2  602 72  HOH HOH A . 
S 7 HOH 3  603 6   HOH HOH A . 
S 7 HOH 4  604 87  HOH HOH A . 
S 7 HOH 5  605 92  HOH HOH A . 
S 7 HOH 6  606 64  HOH HOH A . 
S 7 HOH 7  607 42  HOH HOH A . 
S 7 HOH 8  608 95  HOH HOH A . 
S 7 HOH 9  609 81  HOH HOH A . 
S 7 HOH 10 610 33  HOH HOH A . 
S 7 HOH 11 611 22  HOH HOH A . 
S 7 HOH 12 612 100 HOH HOH A . 
S 7 HOH 13 613 115 HOH HOH A . 
S 7 HOH 14 614 52  HOH HOH A . 
S 7 HOH 15 615 91  HOH HOH A . 
S 7 HOH 16 616 101 HOH HOH A . 
T 7 HOH 1  601 15  HOH HOH B . 
T 7 HOH 2  602 74  HOH HOH B . 
T 7 HOH 3  603 18  HOH HOH B . 
T 7 HOH 4  604 37  HOH HOH B . 
T 7 HOH 5  605 34  HOH HOH B . 
T 7 HOH 6  606 8   HOH HOH B . 
T 7 HOH 7  607 105 HOH HOH B . 
T 7 HOH 8  608 93  HOH HOH B . 
T 7 HOH 9  609 114 HOH HOH B . 
T 7 HOH 10 610 65  HOH HOH B . 
T 7 HOH 11 611 66  HOH HOH B . 
T 7 HOH 12 612 67  HOH HOH B . 
T 7 HOH 13 613 24  HOH HOH B . 
T 7 HOH 14 614 61  HOH HOH B . 
T 7 HOH 15 615 94  HOH HOH B . 
T 7 HOH 16 616 10  HOH HOH B . 
T 7 HOH 17 617 112 HOH HOH B . 
T 7 HOH 18 618 2   HOH HOH B . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1 1 Y 1 A ASN 297 ? ND2 ? A ASN 295 ND2 
2 1 Y 1 A ASN 438 ? ND2 ? A ASN 436 ND2 
3 1 Y 1 B ASN 297 ? ND2 ? B ASN 295 ND2 
4 1 Y 1 B ASN 438 ? ND2 ? B 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' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? 5.8.0258 1 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER  ? ? ? 7.0.0.78 2 
? 'model building' ? ? ? ? ? ? ? ? ? ? ? Coot    ? ? ? 0.8.9.2  3 
? refinement       ? ? ? ? ? ? ? ? ? ? ? REFMAC  ? ? ? 7.0.0.78 4 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .        5 
# 
_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                     8WXD 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     60.593 
_cell.length_a_esd                 ? 
_cell.length_b                     89.949 
_cell.length_b_esd                 ? 
_cell.length_c                     216.408 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_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                         8WXD 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                18 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 2 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                   8WXD 
_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             3.01 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          59.19 
_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              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    RT 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.1 M HEPES pH 7.5, 0.01 M Cadmium Sulphate, 1.0 M  Sodium acetate tri-hydrate.' 
_exptl_crystal_grow.pdbx_pH_range   7.5 
_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 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-04-08 
_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   0.8856 
_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 ID23-1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.8856 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   ID23-1 
_diffrn_source.pdbx_synchrotron_site       ESRF 
# 
_reflns.B_iso_Wilson_estimate                          29.2 
_reflns.entry_id                                       8WXD 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.995 
_reflns.d_resolution_low                               58.350 
_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                                     36257 
_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                           87.8 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                3.8 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          7.8 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                0.054 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.989 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.094 
_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                                    1.995 
_reflns_shell.d_res_low                                     2.159 
_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                             5501 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               0.379 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.592 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          90.5 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.543 
_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]                            -0.47 
_refine.aniso_B[1][2]                            -0.00 
_refine.aniso_B[1][3]                            0.00 
_refine.aniso_B[2][2]                            0.33 
_refine.aniso_B[2][3]                            -0.00 
_refine.aniso_B[3][3]                            0.14 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               32.359 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.930 
_refine.correlation_coeff_Fo_to_Fc_free          0.892 
_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                                 8WXD 
_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                            1.995 
_refine.ls_d_res_low                             58.35 
_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                     34403 
_refine.ls_number_reflns_R_free                  1854 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    87.8 
_refine.ls_percent_reflns_R_free                 5.1 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.21184 
_refine.ls_R_factor_R_free                       0.25936 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.20930 
_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               THROUGHOUT 
_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                       0.490 
_refine.pdbx_overall_ESU_R_Free                  0.300 
_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                             9.976 
_refine.overall_SU_ML                            0.139 
_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                       1.995 
_refine_hist.d_res_low                        58.35 
_refine_hist.number_atoms_solvent             34 
_refine_hist.number_atoms_total               6475 
_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        6412 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         29 
_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' ? 0.014  0.013  6581  ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.037  0.017  5852  ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 1.726  1.655  8939  ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 2.811  1.574  13658 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 8.088  5.000  844   ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 39.407 24.934 304   ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 14.564 15.000 1074  ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? 18.856 15.000 16    ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.070  0.200  932   ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.011  0.020  7434  ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.044  0.020  1286  ? 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' ? 1.783  2.989  3364  ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 1.783  2.988  3363  ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 3.096  4.479  4206  ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 3.096  4.479  4207  ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 1.914  3.150  3217  ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 1.914  3.151  3218  ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 3.211  4.647  4732  ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 6.415  55.390 26782 ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 6.415  55.395 26779 ? 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                       1.995 
_refine_ls_shell.d_res_low                        2.047 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             29 
_refine_ls_shell.number_reflns_R_work             502 
_refine_ls_shell.percent_reflns_obs               8.88 
_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                  0.263 
_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                  0.359 
# 
_struct.entry_id                     8WXD 
_struct.title                        'Crystal Structure of shaft pilin PilA 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        8WXD 
_struct_keywords.text            
;Shaft pilin, Backbone pilin, Isopeptide, Oral biofilm, Dental plaque, primary colonizer, sortase pili, Bacterial adhesion, Fimbrial subunit, STRUCTURAL PROTEIN
;
_struct_keywords.pdbx_keywords   'STRUCTURAL PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 2 ? 
E N N 2 ? 
F N N 2 ? 
G N N 3 ? 
H N N 4 ? 
I N N 5 ? 
J N N 5 ? 
K N N 5 ? 
L N N 6 ? 
M N N 2 ? 
N N N 2 ? 
O N N 3 ? 
P N N 5 ? 
Q N N 5 ? 
R N N 5 ? 
S N N 7 ? 
T N N 7 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    A3CPB5_STRSV 
_struct_ref.pdbx_db_accession          A3CPB5 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;SADTTYTIQLSGTSEGHYYEVYHIFSGTLDTSNTLTNIEWAPGVTEAGRTHFGNASDKAASLSGKQNDSAEVKAFAQELN
QYLSSAGVTTVQSQQGTTTISGLKPGYYLIKDSRGSLDNKKGHAYTSFMLQVAKDTTVAVKADVPTLTKQVRANGSQNYT
AATDYRIGQNILFQITATLPSNYADFTRYEFTIKDTIPAGMTYNNDAQVYLQEGGTEKDISTFFPISYTGNVITITPGDL
KYVQDVKVSSKIVIRYTARLNDDAVMGGLGNPNIARLTYSNDPNGFTSTTAETPDTKANVYTYQLKVNKVKENQQALAGA
GFTLYKKVNNQYTEIKKFEADSNSTFDFKGLDSGDYKLVESTVPSGYNAMKDIEFTISGTIDSTGDLTNLTATSATASFE
TDVNTGIITLKVVNKQGALLPNTGGIGTT
;
_struct_ref.pdbx_align_begin           25 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 8WXD A 23 ? 451 ? A3CPB5 25 ? 453 ? 25 453 
2 1 8WXD B 23 ? 451 ? A3CPB5 25 ? 453 ? 25 453 
# 
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 8WXD MET A 1  ? UNP A3CPB5 ? ? 'initiating methionine' 3  1  
1 8WXD GLY A 2  ? UNP A3CPB5 ? ? 'expression tag'        4  2  
1 8WXD SER A 3  ? UNP A3CPB5 ? ? 'expression tag'        5  3  
1 8WXD SER A 4  ? UNP A3CPB5 ? ? 'expression tag'        6  4  
1 8WXD HIS A 5  ? UNP A3CPB5 ? ? 'expression tag'        7  5  
1 8WXD HIS A 6  ? UNP A3CPB5 ? ? 'expression tag'        8  6  
1 8WXD HIS A 7  ? UNP A3CPB5 ? ? 'expression tag'        9  7  
1 8WXD HIS A 8  ? UNP A3CPB5 ? ? 'expression tag'        10 8  
1 8WXD HIS A 9  ? UNP A3CPB5 ? ? 'expression tag'        11 9  
1 8WXD HIS A 10 ? UNP A3CPB5 ? ? 'expression tag'        12 10 
1 8WXD SER A 11 ? UNP A3CPB5 ? ? 'expression tag'        13 11 
1 8WXD SER A 12 ? UNP A3CPB5 ? ? 'expression tag'        14 12 
1 8WXD GLY A 13 ? UNP A3CPB5 ? ? 'expression tag'        15 13 
1 8WXD LEU A 14 ? UNP A3CPB5 ? ? 'expression tag'        16 14 
1 8WXD VAL A 15 ? UNP A3CPB5 ? ? 'expression tag'        17 15 
1 8WXD PRO A 16 ? UNP A3CPB5 ? ? 'expression tag'        18 16 
1 8WXD ARG A 17 ? UNP A3CPB5 ? ? 'expression tag'        19 17 
1 8WXD ARG A 18 ? UNP A3CPB5 ? ? 'expression tag'        20 18 
1 8WXD GLY A 19 ? UNP A3CPB5 ? ? 'expression tag'        21 19 
1 8WXD SER A 20 ? UNP A3CPB5 ? ? 'expression tag'        22 20 
1 8WXD HIS A 21 ? UNP A3CPB5 ? ? 'expression tag'        23 21 
1 8WXD MET A 22 ? UNP A3CPB5 ? ? 'expression tag'        24 22 
2 8WXD MET B 1  ? UNP A3CPB5 ? ? 'initiating methionine' 3  23 
2 8WXD GLY B 2  ? UNP A3CPB5 ? ? 'expression tag'        4  24 
2 8WXD SER B 3  ? UNP A3CPB5 ? ? 'expression tag'        5  25 
2 8WXD SER B 4  ? UNP A3CPB5 ? ? 'expression tag'        6  26 
2 8WXD HIS B 5  ? UNP A3CPB5 ? ? 'expression tag'        7  27 
2 8WXD HIS B 6  ? UNP A3CPB5 ? ? 'expression tag'        8  28 
2 8WXD HIS B 7  ? UNP A3CPB5 ? ? 'expression tag'        9  29 
2 8WXD HIS B 8  ? UNP A3CPB5 ? ? 'expression tag'        10 30 
2 8WXD HIS B 9  ? UNP A3CPB5 ? ? 'expression tag'        11 31 
2 8WXD HIS B 10 ? UNP A3CPB5 ? ? 'expression tag'        12 32 
2 8WXD SER B 11 ? UNP A3CPB5 ? ? 'expression tag'        13 33 
2 8WXD SER B 12 ? UNP A3CPB5 ? ? 'expression tag'        14 34 
2 8WXD GLY B 13 ? UNP A3CPB5 ? ? 'expression tag'        15 35 
2 8WXD LEU B 14 ? UNP A3CPB5 ? ? 'expression tag'        16 36 
2 8WXD VAL B 15 ? UNP A3CPB5 ? ? 'expression tag'        17 37 
2 8WXD PRO B 16 ? UNP A3CPB5 ? ? 'expression tag'        18 38 
2 8WXD ARG B 17 ? UNP A3CPB5 ? ? 'expression tag'        19 39 
2 8WXD ARG B 18 ? UNP A3CPB5 ? ? 'expression tag'        20 40 
2 8WXD GLY B 19 ? UNP A3CPB5 ? ? 'expression tag'        21 41 
2 8WXD SER B 20 ? UNP A3CPB5 ? ? 'expression tag'        22 42 
2 8WXD HIS B 21 ? UNP A3CPB5 ? ? 'expression tag'        23 43 
2 8WXD MET B 22 ? UNP A3CPB5 ? ? 'expression tag'        24 44 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
_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,O,P,Q,R,S,T 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0 
_pdbx_struct_oper_list.matrix[1][2]         0.0 
_pdbx_struct_oper_list.matrix[1][3]         0.0 
_pdbx_struct_oper_list.vector[1]            0.0 
_pdbx_struct_oper_list.matrix[2][1]         0.0 
_pdbx_struct_oper_list.matrix[2][2]         1.0 
_pdbx_struct_oper_list.matrix[2][3]         0.0 
_pdbx_struct_oper_list.vector[2]            0.0 
_pdbx_struct_oper_list.matrix[3][1]         0.0 
_pdbx_struct_oper_list.matrix[3][2]         0.0 
_pdbx_struct_oper_list.matrix[3][3]         1.0 
_pdbx_struct_oper_list.vector[3]            0.0 
# 
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 THR A 67  ? GLY A 75  ? THR A 69  GLY A 77  1 ? 9  
HELX_P HELX_P2  AA2 ASN A 76  ? SER A 85  ? ASN A 78  SER A 87  1 ? 10 
HELX_P HELX_P3  AA3 SER A 91  ? ASN A 102 ? SER A 93  ASN A 104 1 ? 12 
HELX_P HELX_P4  AA4 GLN A 103 ? LEU A 105 ? GLN A 105 LEU A 107 5 ? 3  
HELX_P HELX_P5  AA5 SER A 106 ? ALA A 108 ? SER A 108 ALA A 110 5 ? 3  
HELX_P HELX_P6  AA6 ASN A 204 ? PHE A 208 ? ASN A 206 PHE A 210 5 ? 5  
HELX_P HELX_P7  AA7 SER A 243 ? PHE A 246 ? SER A 245 PHE A 248 5 ? 4  
HELX_P HELX_P8  AA8 ASP A 261 ? VAL A 265 ? ASP A 263 VAL A 267 5 ? 5  
HELX_P HELX_P9  AA9 THR B 67  ? GLY B 75  ? THR B 69  GLY B 77  1 ? 9  
HELX_P HELX_P10 AB1 ASN B 76  ? SER B 85  ? ASN B 78  SER B 87  1 ? 10 
HELX_P HELX_P11 AB2 SER B 91  ? ASN B 102 ? SER B 93  ASN B 104 1 ? 12 
HELX_P HELX_P12 AB3 GLN B 103 ? LEU B 105 ? GLN B 105 LEU B 107 5 ? 3  
HELX_P HELX_P13 AB4 SER B 106 ? ALA B 108 ? SER B 108 ALA B 110 5 ? 3  
HELX_P HELX_P14 AB5 ASN B 204 ? PHE B 208 ? ASN B 206 PHE B 210 5 ? 5  
HELX_P HELX_P15 AB6 SER B 243 ? PHE B 246 ? SER B 245 PHE B 248 5 ? 4  
HELX_P HELX_P16 AB7 ASP B 261 ? VAL B 265 ? ASP B 263 VAL B 267 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 SER 36  OG  ? ? ? 1_555 J CD  . CD ? ? A SER 38  A CD  508 1_555 ? ? ? ? ? ? ? 2.490 ? ? 
metalc2  metalc ? ? A HIS 39  NE2 ? ? ? 1_555 J CD  . CD ? ? A HIS 41  A CD  508 1_555 ? ? ? ? ? ? ? 2.530 ? ? 
metalc3  metalc ? ? A HIS 45  ND1 ? ? ? 1_555 K CD  . CD ? ? A HIS 47  A CD  509 1_555 ? ? ? ? ? ? ? 2.464 ? ? 
metalc4  metalc ? ? A HIS 73  NE2 ? ? ? 1_555 I CD  . CD ? ? A HIS 75  A CD  507 1_555 ? ? ? ? ? ? ? 2.450 ? ? 
metalc5  metalc ? ? A GLU 100 OE1 ? ? ? 1_555 F NA  . NA ? ? A GLU 102 A NA  504 1_555 ? ? ? ? ? ? ? 2.873 ? ? 
metalc6  metalc ? ? A GLU 100 OE1 ? ? ? 1_555 I CD  . CD ? ? A GLU 102 A CD  507 1_555 ? ? ? ? ? ? ? 2.593 ? ? 
metalc7  metalc ? ? A GLU 100 OE2 ? ? ? 1_555 I CD  . CD ? ? A GLU 102 A CD  507 1_555 ? ? ? ? ? ? ? 2.305 ? ? 
metalc8  metalc ? ? A HIS 145 ND1 ? ? ? 1_555 J CD  . CD ? ? A HIS 147 A CD  508 1_555 ? ? ? ? ? ? ? 2.462 ? ? 
metalc9  metalc ? ? A TYR 211 OH  ? ? ? 1_555 E NA  . NA ? ? A TYR 213 A NA  503 1_555 ? ? ? ? ? ? ? 3.049 ? ? 
metalc10 metalc ? ? A TYR 278 OH  ? ? ? 1_555 D NA  . NA ? ? A TYR 280 A NA  502 1_555 ? ? ? ? ? ? ? 2.751 ? ? 
metalc11 metalc ? ? A SER 302 O   ? ? ? 1_555 E NA  . NA ? ? A SER 304 A NA  503 1_555 ? ? ? ? ? ? ? 2.895 ? ? 
metalc12 metalc ? ? C NA  .   NA  ? ? ? 1_555 S HOH . O  ? ? A NA  501 A HOH 608 1_555 ? ? ? ? ? ? ? 2.223 ? ? 
metalc13 metalc ? ? E NA  .   NA  ? ? ? 1_555 S HOH . O  ? ? A NA  503 A HOH 606 1_555 ? ? ? ? ? ? ? 2.556 ? ? 
metalc14 metalc ? ? B SER 36  OG  ? ? ? 1_555 R CD  . CD ? ? B SER 38  B CD  506 1_555 ? ? ? ? ? ? ? 2.374 ? ? 
metalc15 metalc ? ? B HIS 39  NE2 ? ? ? 1_555 R CD  . CD ? ? B HIS 41  B CD  506 1_555 ? ? ? ? ? ? ? 2.449 ? ? 
metalc16 metalc ? ? B TYR 41  OH  ? ? ? 1_555 M NA  . NA ? ? B TYR 43  B NA  501 1_555 ? ? ? ? ? ? ? 2.761 ? ? 
metalc17 metalc ? ? B HIS 45  ND1 ? ? ? 1_555 P CD  . CD ? ? B HIS 47  B CD  504 1_555 ? ? ? ? ? ? ? 2.465 ? ? 
metalc18 metalc ? ? B HIS 73  ND1 ? ? ? 1_555 Q CD  . CD ? ? B HIS 75  B CD  505 1_555 ? ? ? ? ? ? ? 2.458 ? ? 
metalc19 metalc ? ? B ASP 134 OD2 ? ? ? 1_555 M NA  . NA ? ? B ASP 136 B NA  501 1_555 ? ? ? ? ? ? ? 2.399 ? ? 
metalc20 metalc ? ? B HIS 145 ND1 ? ? ? 1_555 R CD  . CD ? ? B HIS 147 B CD  506 1_555 ? ? ? ? ? ? ? 2.463 ? ? 
metalc21 metalc ? ? B ALA 146 O   ? ? ? 1_555 M NA  . NA ? ? B ALA 148 B NA  501 1_555 ? ? ? ? ? ? ? 2.763 ? ? 
metalc22 metalc ? ? B TYR 211 OH  ? ? ? 1_555 N NA  . NA ? ? B TYR 213 B NA  502 1_555 ? ? ? ? ? ? ? 2.909 ? ? 
metalc23 metalc ? ? B SER 302 O   ? ? ? 1_555 N NA  . NA ? ? B SER 304 B NA  502 1_555 ? ? ? ? ? ? ? 2.506 ? ? 
metalc24 metalc ? ? N NA  .   NA  ? ? ? 1_555 T HOH . O  ? ? B NA  502 B HOH 603 1_555 ? ? ? ? ? ? ? 2.877 ? ? 
metalc25 metalc ? ? R CD  .   CD  ? ? ? 1_555 T HOH . O  ? ? B CD  506 B HOH 617 1_555 ? ? ? ? ? ? ? 2.356 ? ? 
# 
_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  OG  ? A SER 36  ? A SER 38  ? 1_555 CD ? J CD . ? A CD 508 ? 1_555 NE2 ? A HIS 39  ? A HIS 41  ? 1_555 83.3  ? 
2  OG  ? A SER 36  ? A SER 38  ? 1_555 CD ? J CD . ? A CD 508 ? 1_555 ND1 ? A HIS 145 ? A HIS 147 ? 1_555 90.5  ? 
3  NE2 ? A HIS 39  ? A HIS 41  ? 1_555 CD ? J CD . ? A CD 508 ? 1_555 ND1 ? A HIS 145 ? A HIS 147 ? 1_555 83.6  ? 
4  NE2 ? A HIS 73  ? A HIS 75  ? 1_555 CD ? I CD . ? A CD 507 ? 1_555 OE1 ? A GLU 100 ? A GLU 102 ? 1_555 86.8  ? 
5  NE2 ? A HIS 73  ? A HIS 75  ? 1_555 CD ? I CD . ? A CD 507 ? 1_555 OE2 ? A GLU 100 ? A GLU 102 ? 1_555 64.7  ? 
6  OE1 ? A GLU 100 ? A GLU 102 ? 1_555 CD ? I CD . ? A CD 507 ? 1_555 OE2 ? A GLU 100 ? A GLU 102 ? 1_555 53.7  ? 
7  OH  ? A TYR 211 ? A TYR 213 ? 1_555 NA ? E NA . ? A NA 503 ? 1_555 O   ? A SER 302 ? A SER 304 ? 1_555 85.0  ? 
8  OH  ? A TYR 211 ? A TYR 213 ? 1_555 NA ? E NA . ? A NA 503 ? 1_555 O   ? S HOH .   ? A HOH 606 ? 1_555 135.9 ? 
9  O   ? A SER 302 ? A SER 304 ? 1_555 NA ? E NA . ? A NA 503 ? 1_555 O   ? S HOH .   ? A HOH 606 ? 1_555 122.1 ? 
10 OG  ? B SER 36  ? B SER 38  ? 1_555 CD ? R CD . ? B CD 506 ? 1_555 NE2 ? B HIS 39  ? B HIS 41  ? 1_555 82.8  ? 
11 OG  ? B SER 36  ? B SER 38  ? 1_555 CD ? R CD . ? B CD 506 ? 1_555 ND1 ? B HIS 145 ? B HIS 147 ? 1_555 97.1  ? 
12 NE2 ? B HIS 39  ? B HIS 41  ? 1_555 CD ? R CD . ? B CD 506 ? 1_555 ND1 ? B HIS 145 ? B HIS 147 ? 1_555 87.2  ? 
13 OG  ? B SER 36  ? B SER 38  ? 1_555 CD ? R CD . ? B CD 506 ? 1_555 O   ? T HOH .   ? B HOH 617 ? 1_555 134.7 ? 
14 NE2 ? B HIS 39  ? B HIS 41  ? 1_555 CD ? R CD . ? B CD 506 ? 1_555 O   ? T HOH .   ? B HOH 617 ? 1_555 103.0 ? 
15 ND1 ? B HIS 145 ? B HIS 147 ? 1_555 CD ? R CD . ? B CD 506 ? 1_555 O   ? T HOH .   ? B HOH 617 ? 1_555 127.8 ? 
16 OH  ? B TYR 41  ? B TYR 43  ? 1_555 NA ? M NA . ? B NA 501 ? 1_555 OD2 ? B ASP 134 ? B ASP 136 ? 1_555 107.7 ? 
17 OH  ? B TYR 41  ? B TYR 43  ? 1_555 NA ? M NA . ? B NA 501 ? 1_555 O   ? B ALA 146 ? B ALA 148 ? 1_555 142.3 ? 
18 OD2 ? B ASP 134 ? B ASP 136 ? 1_555 NA ? M NA . ? B NA 501 ? 1_555 O   ? B ALA 146 ? B ALA 148 ? 1_555 95.3  ? 
19 OH  ? B TYR 211 ? B TYR 213 ? 1_555 NA ? N NA . ? B NA 502 ? 1_555 O   ? B SER 302 ? B SER 304 ? 1_555 87.7  ? 
20 OH  ? B TYR 211 ? B TYR 213 ? 1_555 NA ? N NA . ? B NA 502 ? 1_555 O   ? T HOH .   ? B HOH 603 ? 1_555 123.6 ? 
21 O   ? B SER 302 ? B SER 304 ? 1_555 NA ? N NA . ? B NA 502 ? 1_555 O   ? T HOH .   ? B HOH 603 ? 1_555 127.4 ? 
# 
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 ? 
AB1 ? 3 ? 
AB2 ? 3 ? 
AB3 ? 4 ? 
AB4 ? 5 ? 
AB5 ? 6 ? 
AB6 ? 6 ? 
AB7 ? 4 ? 
AB8 ? 4 ? 
AB9 ? 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 
AB1 1 2 ? anti-parallel 
AB1 2 3 ? parallel      
AB2 1 2 ? anti-parallel 
AB2 2 3 ? anti-parallel 
AB3 1 2 ? anti-parallel 
AB3 2 3 ? anti-parallel 
AB3 3 4 ? anti-parallel 
AB4 1 2 ? anti-parallel 
AB4 2 3 ? anti-parallel 
AB4 3 4 ? anti-parallel 
AB4 4 5 ? anti-parallel 
AB5 1 2 ? anti-parallel 
AB5 2 3 ? anti-parallel 
AB5 3 4 ? anti-parallel 
AB5 4 5 ? anti-parallel 
AB5 5 6 ? anti-parallel 
AB6 1 2 ? parallel      
AB6 2 3 ? anti-parallel 
AB6 3 4 ? anti-parallel 
AB6 4 5 ? anti-parallel 
AB6 5 6 ? anti-parallel 
AB7 1 2 ? parallel      
AB7 2 3 ? anti-parallel 
AB7 3 4 ? anti-parallel 
AB8 1 2 ? anti-parallel 
AB8 2 3 ? parallel      
AB8 3 4 ? anti-parallel 
AB9 1 2 ? anti-parallel 
AB9 2 3 ? anti-parallel 
AB9 3 4 ? anti-parallel 
AB9 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 118 ? LEU A 125 ? GLY A 120 LEU A 127 
AA1 2 TYR A 28  ? THR A 35  ? TYR A 30  THR A 37  
AA1 3 THR A 158 ? ALA A 161 ? THR A 160 ALA A 163 
AA2 1 LEU A 57  ? TRP A 62  ? LEU A 59  TRP A 64  
AA2 2 TYR A 40  ? LEU A 51  ? TYR A 42  LEU A 53  
AA2 3 VAL A 110 ? GLN A 114 ? VAL A 112 GLN A 116 
AA3 1 LEU A 57  ? TRP A 62  ? LEU A 59  TRP A 64  
AA3 2 TYR A 40  ? LEU A 51  ? TYR A 42  LEU A 53  
AA3 3 GLY A 128 ? ASP A 134 ? GLY A 130 ASP A 136 
AA3 4 MET A 151 ? VAL A 154 ? MET A 153 VAL A 156 
AA4 1 TYR A 181 ? THR A 182 ? TYR A 183 THR A 184 
AA4 2 THR A 168 ? ARG A 174 ? THR A 170 ARG A 176 
AA4 3 ASN A 192 ? THR A 200 ? ASN A 194 THR A 202 
AA4 4 LYS A 273 ? LEU A 282 ? LYS A 275 LEU A 284 
AA4 5 MET A 223 ? TYR A 225 ? MET A 225 TYR A 227 
AA5 1 TYR A 181 ? THR A 182 ? TYR A 183 THR A 184 
AA5 2 THR A 168 ? ARG A 174 ? THR A 170 ARG A 176 
AA5 3 ASN A 192 ? THR A 200 ? ASN A 194 THR A 202 
AA5 4 LYS A 273 ? LEU A 282 ? LYS A 275 LEU A 284 
AA5 5 GLN A 230 ? GLN A 234 ? GLN A 232 GLN A 236 
AA5 6 GLU A 239 ? ASP A 241 ? GLU A 241 ASP A 243 
AA6 1 ALA A 184 ? ASP A 186 ? ALA A 186 ASP A 188 
AA6 2 THR A 318 ? TYR A 323 ? THR A 320 TYR A 325 
AA6 3 ASN A 293 ? SER A 302 ? ASN A 295 SER A 304 
AA6 4 PHE A 213 ? THR A 218 ? PHE A 215 THR A 220 
AA6 5 VAL A 254 ? ILE A 257 ? VAL A 256 ILE A 259 
AA6 6 ILE A 248 ? THR A 251 ? ILE A 250 THR A 253 
AA7 1 ALA A 184 ? ASP A 186 ? ALA A 186 ASP A 188 
AA7 2 THR A 318 ? TYR A 323 ? THR A 320 TYR A 325 
AA7 3 ASN A 293 ? SER A 302 ? ASN A 295 SER A 304 
AA7 4 THR A 312 ? GLU A 314 ? THR A 314 GLU A 316 
AA8 1 THR A 367 ? LEU A 373 ? THR A 369 LEU A 375 
AA8 2 TYR A 325 ? LYS A 333 ? TYR A 327 LYS A 335 
AA8 3 ILE A 429 ? ASN A 436 ? ILE A 431 ASN A 438 
AA8 4 GLU A 422 ? ASP A 424 ? GLU A 424 ASP A 426 
AA9 1 TYR A 354 ? PHE A 360 ? TYR A 356 PHE A 362 
AA9 2 GLY A 343 ? LYS A 349 ? GLY A 345 LYS A 351 
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 ? THR A 415 ? LEU A 411 THR A 417 
AB1 1 GLY B 118 ? LEU B 125 ? GLY B 120 LEU B 127 
AB1 2 TYR B 28  ? THR B 35  ? TYR B 30  THR B 37  
AB1 3 THR B 159 ? ALA B 161 ? THR B 161 ALA B 163 
AB2 1 LEU B 57  ? TRP B 62  ? LEU B 59  TRP B 64  
AB2 2 TYR B 40  ? LEU B 51  ? TYR B 42  LEU B 53  
AB2 3 VAL B 110 ? GLN B 114 ? VAL B 112 GLN B 116 
AB3 1 LEU B 57  ? TRP B 62  ? LEU B 59  TRP B 64  
AB3 2 TYR B 40  ? LEU B 51  ? TYR B 42  LEU B 53  
AB3 3 GLY B 128 ? ASP B 134 ? GLY B 130 ASP B 136 
AB3 4 MET B 151 ? VAL B 154 ? MET B 153 VAL B 156 
AB4 1 TYR B 181 ? THR B 182 ? TYR B 183 THR B 184 
AB4 2 THR B 168 ? ARG B 174 ? THR B 170 ARG B 176 
AB4 3 ASN B 192 ? THR B 200 ? ASN B 194 THR B 202 
AB4 4 LYS B 273 ? LEU B 282 ? LYS B 275 LEU B 284 
AB4 5 MET B 223 ? TYR B 225 ? MET B 225 TYR B 227 
AB5 1 TYR B 181 ? THR B 182 ? TYR B 183 THR B 184 
AB5 2 THR B 168 ? ARG B 174 ? THR B 170 ARG B 176 
AB5 3 ASN B 192 ? THR B 200 ? ASN B 194 THR B 202 
AB5 4 LYS B 273 ? LEU B 282 ? LYS B 275 LEU B 284 
AB5 5 GLN B 230 ? GLN B 234 ? GLN B 232 GLN B 236 
AB5 6 GLU B 239 ? ASP B 241 ? GLU B 241 ASP B 243 
AB6 1 ALA B 184 ? ASP B 186 ? ALA B 186 ASP B 188 
AB6 2 THR B 318 ? TYR B 323 ? THR B 320 TYR B 325 
AB6 3 ASN B 293 ? SER B 302 ? ASN B 295 SER B 304 
AB6 4 PHE B 213 ? THR B 218 ? PHE B 215 THR B 220 
AB6 5 VAL B 254 ? ILE B 257 ? VAL B 256 ILE B 259 
AB6 6 ILE B 248 ? THR B 251 ? ILE B 250 THR B 253 
AB7 1 ALA B 184 ? ASP B 186 ? ALA B 186 ASP B 188 
AB7 2 THR B 318 ? TYR B 323 ? THR B 320 TYR B 325 
AB7 3 ASN B 293 ? SER B 302 ? ASN B 295 SER B 304 
AB7 4 THR B 312 ? GLU B 314 ? THR B 314 GLU B 316 
AB8 1 THR B 367 ? LEU B 373 ? THR B 369 LEU B 375 
AB8 2 TYR B 325 ? LYS B 333 ? TYR B 327 LYS B 335 
AB8 3 ILE B 429 ? ASN B 436 ? ILE B 431 ASN B 438 
AB8 4 GLU B 422 ? ASP B 424 ? GLU B 424 ASP B 426 
AB9 1 TYR B 354 ? PHE B 360 ? TYR B 356 PHE B 362 
AB9 2 GLY B 343 ? LYS B 349 ? GLY B 345 LYS B 351 
AB9 3 GLY B 376 ? THR B 384 ? GLY B 378 THR B 386 
AB9 4 ILE B 395 ? ILE B 403 ? ILE B 397 ILE B 405 
AB9 5 LEU B 409 ? THR B 415 ? LEU B 411 THR B 417 
# 
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 LEU A 125 ? O LEU A 127 N TYR A 28  ? N TYR A 30  
AA1 2 3 N GLN A 31  ? N GLN A 33  O VAL A 160 ? O VAL A 162 
AA2 1 2 O THR A 58  ? O THR A 60  N THR A 50  ? N THR A 52  
AA2 2 3 N VAL A 43  ? N VAL A 45  O THR A 111 ? O THR A 113 
AA3 1 2 O THR A 58  ? O THR A 60  N THR A 50  ? N THR A 52  
AA3 2 3 N GLU A 42  ? N GLU A 44  O LYS A 133 ? O LYS A 135 
AA3 3 4 N TYR A 130 ? N TYR A 132 O GLN A 153 ? O GLN A 155 
AA4 1 2 O THR A 182 ? O THR A 184 N VAL A 173 ? N VAL A 175 
AA4 2 3 N ARG A 174 ? N ARG A 176 O LEU A 194 ? O LEU A 196 
AA4 3 4 N ALA A 199 ? N ALA A 201 O ILE A 274 ? O ILE A 276 
AA4 4 5 O ARG A 281 ? O ARG A 283 N THR A 224 ? N THR A 226 
AA5 1 2 O THR A 182 ? O THR A 184 N VAL A 173 ? N VAL A 175 
AA5 2 3 N ARG A 174 ? N ARG A 176 O LEU A 194 ? O LEU A 196 
AA5 3 4 N ALA A 199 ? N ALA A 201 O ILE A 274 ? O ILE A 276 
AA5 4 5 O LYS A 273 ? O LYS A 275 N GLN A 234 ? N GLN A 236 
AA5 5 6 N LEU A 233 ? N LEU A 235 O LYS A 240 ? O LYS A 242 
AA6 1 2 N THR A 185 ? N THR A 187 O TYR A 323 ? O TYR A 325 
AA6 2 3 O THR A 318 ? O THR A 320 N ALA A 297 ? N ALA A 299 
AA6 3 4 O ILE A 296 ? O ILE A 298 N THR A 218 ? N THR A 220 
AA6 4 5 N ASP A 217 ? N ASP A 219 O ILE A 255 ? O ILE A 257 
AA6 5 6 O THR A 256 ? O THR A 258 N SER A 249 ? N SER A 251 
AA7 1 2 N THR A 185 ? N THR A 187 O TYR A 323 ? O TYR A 325 
AA7 2 3 O THR A 318 ? O THR 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 LYS A 328 ? N LYS A 330 O ILE A 430 ? O ILE A 432 
AA8 3 4 O THR A 431 ? O THR A 433 N GLU A 422 ? N GLU A 424 
AA9 1 2 O THR A 355 ? O THR A 357 N LYS A 348 ? N LYS A 350 
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 398 ? N THR A 400 O THR A 415 ? O THR A 417 
AB1 1 2 O ILE B 122 ? O ILE B 124 N ILE B 30  ? N ILE B 32  
AB1 2 3 N GLN B 31  ? N GLN B 33  O VAL B 160 ? O VAL B 162 
AB2 1 2 O THR B 58  ? O THR B 60  N THR B 50  ? N THR B 52  
AB2 2 3 N VAL B 43  ? N VAL B 45  O THR B 111 ? O THR B 113 
AB3 1 2 O THR B 58  ? O THR B 60  N THR B 50  ? N THR B 52  
AB3 2 3 N GLU B 42  ? N GLU B 44  O LYS B 133 ? O LYS B 135 
AB3 3 4 N ILE B 132 ? N ILE B 134 O MET B 151 ? O MET B 153 
AB4 1 2 O THR B 182 ? O THR B 184 N VAL B 173 ? N VAL B 175 
AB4 2 3 N ARG B 174 ? N ARG B 176 O LEU B 194 ? O LEU B 196 
AB4 3 4 N ALA B 199 ? N ALA B 201 O ILE B 274 ? O ILE B 276 
AB4 4 5 O ARG B 281 ? O ARG B 283 N THR B 224 ? N THR B 226 
AB5 1 2 O THR B 182 ? O THR B 184 N VAL B 173 ? N VAL B 175 
AB5 2 3 N ARG B 174 ? N ARG B 176 O LEU B 194 ? O LEU B 196 
AB5 3 4 N ALA B 199 ? N ALA B 201 O ILE B 274 ? O ILE B 276 
AB5 4 5 O LYS B 273 ? O LYS B 275 N GLN B 234 ? N GLN B 236 
AB5 5 6 N LEU B 233 ? N LEU B 235 O LYS B 240 ? O LYS B 242 
AB6 1 2 N THR B 185 ? N THR B 187 O TYR B 323 ? O TYR B 325 
AB6 2 3 O THR B 318 ? O THR B 320 N ALA B 297 ? N ALA B 299 
AB6 3 4 O ILE B 296 ? O ILE B 298 N THR B 218 ? N THR B 220 
AB6 4 5 N ASP B 217 ? N ASP B 219 O ILE B 255 ? O ILE B 257 
AB6 5 6 O THR B 256 ? O THR B 258 N SER B 249 ? N SER B 251 
AB7 1 2 N THR B 185 ? N THR B 187 O TYR B 323 ? O TYR B 325 
AB7 2 3 O THR B 318 ? O THR B 320 N ALA B 297 ? N ALA B 299 
AB7 3 4 N TYR B 301 ? N TYR B 303 O ALA B 313 ? O ALA B 315 
AB8 1 2 O PHE B 370 ? O PHE B 372 N LEU B 327 ? N LEU B 329 
AB8 2 3 N ASN B 330 ? N ASN B 332 O VAL B 434 ? O VAL B 436 
AB8 3 4 O THR B 431 ? O THR B 433 N GLU B 422 ? N GLU B 424 
AB9 1 2 O THR B 355 ? O THR B 357 N LYS B 348 ? N LYS B 350 
AB9 2 3 N LYS B 349 ? N LYS B 351 O ASP B 377 ? O ASP B 379 
AB9 3 4 N TYR B 378 ? N TYR B 380 O PHE B 397 ? O PHE B 399 
AB9 4 5 N THR B 402 ? N THR B 404 O ASN B 411 ? O ASN B 413 
# 
_pdbx_entry_details.entry_id                   8WXD 
_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 173 ? ? CG A ASN 297 ? ? 1.33 
2 1 NZ B LYS 173 ? ? CG B ASN 297 ? ? 1.36 
3 1 NZ A LYS 333 ? ? CG A ASN 438 ? ? 1.37 
4 1 NZ B LYS 333 ? ? CG B ASN 438 ? ? 1.39 
# 
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 165 ? ? -91.63  54.53   
2  1 ASN A 178 ? ? -52.34  108.29  
3  1 GLN A 355 ? ? -151.14 87.55   
4  1 ASP A 365 ? A 166.48  -140.10 
5  1 ASP A 365 ? B -170.06 -148.71 
6  1 LYS B 128 ? ? -49.18  156.41  
7  1 ASN B 143 ? A 80.43   -9.10   
8  1 ASN B 178 ? ? -56.85  107.86  
9  1 SER B 180 ? ? -145.49 -10.67  
10 1 GLN B 181 ? ? 53.12   7.16    
11 1 ASN B 295 ? ? -116.64 78.30   
12 1 SER B 312 ? ? -141.44 37.56   
13 1 GLN B 355 ? ? -152.48 88.77   
14 1 ASP B 365 ? ? -170.86 -138.16 
15 1 ASP B 365 ? ? -167.23 -144.25 
# 
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 35.2053 116.6826 3.4499    0.0584 ? 0.0030  ? 0.0216 ? 0.0377 ? 0.0146  ? 0.0231 ? 0.0717 ? 0.1514 
? -0.2668 ? 0.5412 ? -0.0809 ? 2.1275 ? -0.0333 ? -0.0249 ? -0.0368 ? -0.0156 ? -0.0802 ? -0.0916 ? 0.2335  ? 0.0151  ? 0.1134 ? 
2 'X-RAY DIFFRACTION' ? refined 30.5599 126.8357 -31.4829  0.0305 ? 0.0076  ? 0.0110 ? 0.0634 ? -0.0162 ? 0.0147 ? 0.0433 ? 
-0.0255 ? -0.2295 ? 0.2889 ? 0.4664  ? 1.8136 ? 0.0037  ? 0.0240  ? -0.0186 ? -0.0002 ? -0.0836 ? 0.0240  ? -0.0919 ? -0.2030 ? 
0.0799 ? 
3 'X-RAY DIFFRACTION' ? refined 34.2450 112.6544 -67.8899  0.0432 ? -0.0232 ? 0.0039 ? 0.0449 ? -0.0150 ? 0.0199 ? 0.2222 ? 
-0.0068 ? -0.1469 ? 0.0351 ? 0.2730  ? 2.3478 ? -0.0370 ? 0.0061  ? 0.0528  ? 0.0183  ? -0.0273 ? 0.0120  ? 0.1882  ? -0.1616 ? 
0.0643 ? 
4 'X-RAY DIFFRACTION' ? refined 55.6268 113.7639 -118.4629 0.0472 ? -0.0184 ? 0.0384 ? 0.0373 ? -0.0343 ? 0.0549 ? 0.4985 ? 
-0.3912 ? -0.1472 ? 0.3196 ? -0.0239 ? 1.6552 ? -0.0852 ? 0.1349  ? -0.1376 ? 0.0667  ? -0.1062 ? 0.0963  ? 0.0817  ? -0.0229 ? 
0.1913 ? 
5 'X-RAY DIFFRACTION' ? refined 58.3541 126.7631 -84.4182  0.0213 ? -0.0018 ? 0.0202 ? 0.0293 ? 0.0090  ? 0.0281 ? 0.1802 ? 
-0.0335 ? -0.3070 ? 0.1599 ? -0.2621 ? 1.4707 ? 0.0021  ? -0.0257 ? 0.0012  ? -0.0107 ? -0.0245 ? -0.0435 ? -0.0478 ? 0.0859  ? 
0.0224 ? 
6 'X-RAY DIFFRACTION' ? refined 56.3004 114.7281 -47.1188  0.0483 ? 0.0412  ? 0.0069 ? 0.0668 ? 0.0065  ? 0.0105 ? 0.2223 ? 0.1359 
? -0.2192 ? 0.1061 ? -0.3292 ? 1.9118 ? 0.0058  ? -0.0405 ? 0.0316  ? -0.0161 ? -0.0402 ? 0.0108  ? 0.1907  ? 0.1807  ? 0.0344 ? 
# 
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 165 ? ? ? 
2 'X-RAY DIFFRACTION' 2 ? ? A 166 ? ? ? A 325 ? ? ? 
3 'X-RAY DIFFRACTION' 3 ? ? A 326 ? ? ? A 447 ? ? ? 
4 'X-RAY DIFFRACTION' 4 ? ? B 29  ? ? ? B 165 ? ? ? 
5 'X-RAY DIFFRACTION' 5 ? ? B 166 ? ? ? B 325 ? ? ? 
6 'X-RAY DIFFRACTION' 6 ? ? B 326 ? ? ? B 447 ? ? ? 
# 
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 THR 28  ? A THR 26  
27 1 Y 1 A GLY 448 ? A GLY 446 
28 1 Y 1 A GLY 449 ? A GLY 447 
29 1 Y 1 A ILE 450 ? A ILE 448 
30 1 Y 1 A GLY 451 ? A GLY 449 
31 1 Y 1 A THR 452 ? A THR 450 
32 1 Y 1 A THR 453 ? A THR 451 
33 1 Y 1 B MET 3   ? B MET 1   
34 1 Y 1 B GLY 4   ? B GLY 2   
35 1 Y 1 B SER 5   ? B SER 3   
36 1 Y 1 B SER 6   ? B SER 4   
37 1 Y 1 B HIS 7   ? B HIS 5   
38 1 Y 1 B HIS 8   ? B HIS 6   
39 1 Y 1 B HIS 9   ? B HIS 7   
40 1 Y 1 B HIS 10  ? B HIS 8   
41 1 Y 1 B HIS 11  ? B HIS 9   
42 1 Y 1 B HIS 12  ? B HIS 10  
43 1 Y 1 B SER 13  ? B SER 11  
44 1 Y 1 B SER 14  ? B SER 12  
45 1 Y 1 B GLY 15  ? B GLY 13  
46 1 Y 1 B LEU 16  ? B LEU 14  
47 1 Y 1 B VAL 17  ? B VAL 15  
48 1 Y 1 B PRO 18  ? B PRO 16  
49 1 Y 1 B ARG 19  ? B ARG 17  
50 1 Y 1 B ARG 20  ? B ARG 18  
51 1 Y 1 B GLY 21  ? B GLY 19  
52 1 Y 1 B SER 22  ? B SER 20  
53 1 Y 1 B HIS 23  ? B HIS 21  
54 1 Y 1 B MET 24  ? B MET 22  
55 1 Y 1 B SER 25  ? B SER 23  
56 1 Y 1 B ALA 26  ? B ALA 24  
57 1 Y 1 B ASP 27  ? B ASP 25  
58 1 Y 1 B THR 28  ? B THR 26  
59 1 Y 1 B GLY 448 ? B GLY 446 
60 1 Y 1 B GLY 449 ? B GLY 447 
61 1 Y 1 B ILE 450 ? B ILE 448 
62 1 Y 1 B GLY 451 ? B GLY 449 
63 1 Y 1 B THR 452 ? B THR 450 
64 1 Y 1 B THR 453 ? B 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 
ALA N    N  N N 1   
ALA CA   C  N S 2   
ALA C    C  N N 3   
ALA O    O  N N 4   
ALA CB   C  N N 5   
ALA OXT  O  N N 6   
ALA H    H  N N 7   
ALA H2   H  N N 8   
ALA HA   H  N N 9   
ALA HB1  H  N N 10  
ALA HB2  H  N N 11  
ALA HB3  H  N N 12  
ALA HXT  H  N N 13  
ARG N    N  N N 14  
ARG CA   C  N S 15  
ARG C    C  N N 16  
ARG O    O  N N 17  
ARG CB   C  N N 18  
ARG CG   C  N N 19  
ARG CD   C  N N 20  
ARG NE   N  N N 21  
ARG CZ   C  N N 22  
ARG NH1  N  N N 23  
ARG NH2  N  N N 24  
ARG OXT  O  N N 25  
ARG H    H  N N 26  
ARG H2   H  N N 27  
ARG HA   H  N N 28  
ARG HB2  H  N N 29  
ARG HB3  H  N N 30  
ARG HG2  H  N N 31  
ARG HG3  H  N N 32  
ARG HD2  H  N N 33  
ARG HD3  H  N N 34  
ARG HE   H  N N 35  
ARG HH11 H  N N 36  
ARG HH12 H  N N 37  
ARG HH21 H  N N 38  
ARG HH22 H  N N 39  
ARG HXT  H  N N 40  
ASN N    N  N N 41  
ASN CA   C  N S 42  
ASN C    C  N N 43  
ASN O    O  N N 44  
ASN CB   C  N N 45  
ASN CG   C  N N 46  
ASN OD1  O  N N 47  
ASN ND2  N  N N 48  
ASN OXT  O  N N 49  
ASN H    H  N N 50  
ASN H2   H  N N 51  
ASN HA   H  N N 52  
ASN HB2  H  N N 53  
ASN HB3  H  N N 54  
ASN HD21 H  N N 55  
ASN HD22 H  N N 56  
ASN HXT  H  N N 57  
ASP N    N  N N 58  
ASP CA   C  N S 59  
ASP C    C  N N 60  
ASP O    O  N N 61  
ASP CB   C  N N 62  
ASP CG   C  N N 63  
ASP OD1  O  N N 64  
ASP OD2  O  N N 65  
ASP OXT  O  N N 66  
ASP H    H  N N 67  
ASP H2   H  N N 68  
ASP HA   H  N N 69  
ASP HB2  H  N N 70  
ASP HB3  H  N N 71  
ASP HD2  H  N N 72  
ASP HXT  H  N N 73  
CD  CD   CD N N 74  
CL  CL   CL N N 75  
GLN N    N  N N 76  
GLN CA   C  N S 77  
GLN C    C  N N 78  
GLN O    O  N N 79  
GLN CB   C  N N 80  
GLN CG   C  N N 81  
GLN CD   C  N N 82  
GLN OE1  O  N N 83  
GLN NE2  N  N N 84  
GLN OXT  O  N N 85  
GLN H    H  N N 86  
GLN H2   H  N N 87  
GLN HA   H  N N 88  
GLN HB2  H  N N 89  
GLN HB3  H  N N 90  
GLN HG2  H  N N 91  
GLN HG3  H  N N 92  
GLN HE21 H  N N 93  
GLN HE22 H  N N 94  
GLN HXT  H  N N 95  
GLU N    N  N N 96  
GLU CA   C  N S 97  
GLU C    C  N N 98  
GLU O    O  N N 99  
GLU CB   C  N N 100 
GLU CG   C  N N 101 
GLU CD   C  N N 102 
GLU OE1  O  N N 103 
GLU OE2  O  N N 104 
GLU OXT  O  N N 105 
GLU H    H  N N 106 
GLU H2   H  N N 107 
GLU HA   H  N N 108 
GLU HB2  H  N N 109 
GLU HB3  H  N N 110 
GLU HG2  H  N N 111 
GLU HG3  H  N N 112 
GLU HE2  H  N N 113 
GLU HXT  H  N N 114 
GLY N    N  N N 115 
GLY CA   C  N N 116 
GLY C    C  N N 117 
GLY O    O  N N 118 
GLY OXT  O  N N 119 
GLY H    H  N N 120 
GLY H2   H  N N 121 
GLY HA2  H  N N 122 
GLY HA3  H  N N 123 
GLY HXT  H  N N 124 
GOL C1   C  N N 125 
GOL O1   O  N N 126 
GOL C2   C  N N 127 
GOL O2   O  N N 128 
GOL C3   C  N N 129 
GOL O3   O  N N 130 
GOL H11  H  N N 131 
GOL H12  H  N N 132 
GOL HO1  H  N N 133 
GOL H2   H  N N 134 
GOL HO2  H  N N 135 
GOL H31  H  N N 136 
GOL H32  H  N N 137 
GOL HO3  H  N N 138 
HIS N    N  N N 139 
HIS CA   C  N S 140 
HIS C    C  N N 141 
HIS O    O  N N 142 
HIS CB   C  N N 143 
HIS CG   C  Y N 144 
HIS ND1  N  Y N 145 
HIS CD2  C  Y N 146 
HIS CE1  C  Y N 147 
HIS NE2  N  Y N 148 
HIS OXT  O  N N 149 
HIS H    H  N N 150 
HIS H2   H  N N 151 
HIS HA   H  N N 152 
HIS HB2  H  N N 153 
HIS HB3  H  N N 154 
HIS HD1  H  N N 155 
HIS HD2  H  N N 156 
HIS HE1  H  N N 157 
HIS HE2  H  N N 158 
HIS HXT  H  N N 159 
HOH O    O  N N 160 
HOH H1   H  N N 161 
HOH H2   H  N N 162 
ILE N    N  N N 163 
ILE CA   C  N S 164 
ILE C    C  N N 165 
ILE O    O  N N 166 
ILE CB   C  N S 167 
ILE CG1  C  N N 168 
ILE CG2  C  N N 169 
ILE CD1  C  N N 170 
ILE OXT  O  N N 171 
ILE H    H  N N 172 
ILE H2   H  N N 173 
ILE HA   H  N N 174 
ILE HB   H  N N 175 
ILE HG12 H  N N 176 
ILE HG13 H  N N 177 
ILE HG21 H  N N 178 
ILE HG22 H  N N 179 
ILE HG23 H  N N 180 
ILE HD11 H  N N 181 
ILE HD12 H  N N 182 
ILE HD13 H  N N 183 
ILE HXT  H  N N 184 
LEU N    N  N N 185 
LEU CA   C  N S 186 
LEU C    C  N N 187 
LEU O    O  N N 188 
LEU CB   C  N N 189 
LEU CG   C  N N 190 
LEU CD1  C  N N 191 
LEU CD2  C  N N 192 
LEU OXT  O  N N 193 
LEU H    H  N N 194 
LEU H2   H  N N 195 
LEU HA   H  N N 196 
LEU HB2  H  N N 197 
LEU HB3  H  N N 198 
LEU HG   H  N N 199 
LEU HD11 H  N N 200 
LEU HD12 H  N N 201 
LEU HD13 H  N N 202 
LEU HD21 H  N N 203 
LEU HD22 H  N N 204 
LEU HD23 H  N N 205 
LEU HXT  H  N N 206 
LYS N    N  N N 207 
LYS CA   C  N S 208 
LYS C    C  N N 209 
LYS O    O  N N 210 
LYS CB   C  N N 211 
LYS CG   C  N N 212 
LYS CD   C  N N 213 
LYS CE   C  N N 214 
LYS NZ   N  N N 215 
LYS OXT  O  N N 216 
LYS H    H  N N 217 
LYS H2   H  N N 218 
LYS HA   H  N N 219 
LYS HB2  H  N N 220 
LYS HB3  H  N N 221 
LYS HG2  H  N N 222 
LYS HG3  H  N N 223 
LYS HD2  H  N N 224 
LYS HD3  H  N N 225 
LYS HE2  H  N N 226 
LYS HE3  H  N N 227 
LYS HZ1  H  N N 228 
LYS HZ2  H  N N 229 
LYS HZ3  H  N N 230 
LYS HXT  H  N N 231 
MET N    N  N N 232 
MET CA   C  N S 233 
MET C    C  N N 234 
MET O    O  N N 235 
MET CB   C  N N 236 
MET CG   C  N N 237 
MET SD   S  N N 238 
MET CE   C  N N 239 
MET OXT  O  N N 240 
MET H    H  N N 241 
MET H2   H  N N 242 
MET HA   H  N N 243 
MET HB2  H  N N 244 
MET HB3  H  N N 245 
MET HG2  H  N N 246 
MET HG3  H  N N 247 
MET HE1  H  N N 248 
MET HE2  H  N N 249 
MET HE3  H  N N 250 
MET HXT  H  N N 251 
NA  NA   NA N N 252 
PHE N    N  N N 253 
PHE CA   C  N S 254 
PHE C    C  N N 255 
PHE O    O  N N 256 
PHE CB   C  N N 257 
PHE CG   C  Y N 258 
PHE CD1  C  Y N 259 
PHE CD2  C  Y N 260 
PHE CE1  C  Y N 261 
PHE CE2  C  Y N 262 
PHE CZ   C  Y N 263 
PHE OXT  O  N N 264 
PHE H    H  N N 265 
PHE H2   H  N N 266 
PHE HA   H  N N 267 
PHE HB2  H  N N 268 
PHE HB3  H  N N 269 
PHE HD1  H  N N 270 
PHE HD2  H  N N 271 
PHE HE1  H  N N 272 
PHE HE2  H  N N 273 
PHE HZ   H  N N 274 
PHE HXT  H  N N 275 
PRO N    N  N N 276 
PRO CA   C  N S 277 
PRO C    C  N N 278 
PRO O    O  N N 279 
PRO CB   C  N N 280 
PRO CG   C  N N 281 
PRO CD   C  N N 282 
PRO OXT  O  N N 283 
PRO H    H  N N 284 
PRO HA   H  N N 285 
PRO HB2  H  N N 286 
PRO HB3  H  N N 287 
PRO HG2  H  N N 288 
PRO HG3  H  N N 289 
PRO HD2  H  N N 290 
PRO HD3  H  N N 291 
PRO HXT  H  N N 292 
SER N    N  N N 293 
SER CA   C  N S 294 
SER C    C  N N 295 
SER O    O  N N 296 
SER CB   C  N N 297 
SER OG   O  N N 298 
SER OXT  O  N N 299 
SER H    H  N N 300 
SER H2   H  N N 301 
SER HA   H  N N 302 
SER HB2  H  N N 303 
SER HB3  H  N N 304 
SER HG   H  N N 305 
SER HXT  H  N N 306 
SO4 S    S  N N 307 
SO4 O1   O  N N 308 
SO4 O2   O  N N 309 
SO4 O3   O  N N 310 
SO4 O4   O  N N 311 
THR N    N  N N 312 
THR CA   C  N S 313 
THR C    C  N N 314 
THR O    O  N N 315 
THR CB   C  N R 316 
THR OG1  O  N N 317 
THR CG2  C  N N 318 
THR OXT  O  N N 319 
THR H    H  N N 320 
THR H2   H  N N 321 
THR HA   H  N N 322 
THR HB   H  N N 323 
THR HG1  H  N N 324 
THR HG21 H  N N 325 
THR HG22 H  N N 326 
THR HG23 H  N N 327 
THR HXT  H  N N 328 
TRP N    N  N N 329 
TRP CA   C  N S 330 
TRP C    C  N N 331 
TRP O    O  N N 332 
TRP CB   C  N N 333 
TRP CG   C  Y N 334 
TRP CD1  C  Y N 335 
TRP CD2  C  Y N 336 
TRP NE1  N  Y N 337 
TRP CE2  C  Y N 338 
TRP CE3  C  Y N 339 
TRP CZ2  C  Y N 340 
TRP CZ3  C  Y N 341 
TRP CH2  C  Y N 342 
TRP OXT  O  N N 343 
TRP H    H  N N 344 
TRP H2   H  N N 345 
TRP HA   H  N N 346 
TRP HB2  H  N N 347 
TRP HB3  H  N N 348 
TRP HD1  H  N N 349 
TRP HE1  H  N N 350 
TRP HE3  H  N N 351 
TRP HZ2  H  N N 352 
TRP HZ3  H  N N 353 
TRP HH2  H  N N 354 
TRP HXT  H  N N 355 
TYR N    N  N N 356 
TYR CA   C  N S 357 
TYR C    C  N N 358 
TYR O    O  N N 359 
TYR CB   C  N N 360 
TYR CG   C  Y N 361 
TYR CD1  C  Y N 362 
TYR CD2  C  Y N 363 
TYR CE1  C  Y N 364 
TYR CE2  C  Y N 365 
TYR CZ   C  Y N 366 
TYR OH   O  N N 367 
TYR OXT  O  N N 368 
TYR H    H  N N 369 
TYR H2   H  N N 370 
TYR HA   H  N N 371 
TYR HB2  H  N N 372 
TYR HB3  H  N N 373 
TYR HD1  H  N N 374 
TYR HD2  H  N N 375 
TYR HE1  H  N N 376 
TYR HE2  H  N N 377 
TYR HH   H  N N 378 
TYR HXT  H  N N 379 
VAL N    N  N N 380 
VAL CA   C  N S 381 
VAL C    C  N N 382 
VAL O    O  N N 383 
VAL CB   C  N N 384 
VAL CG1  C  N N 385 
VAL CG2  C  N N 386 
VAL OXT  O  N N 387 
VAL H    H  N N 388 
VAL H2   H  N N 389 
VAL HA   H  N N 390 
VAL HB   H  N N 391 
VAL HG11 H  N N 392 
VAL HG12 H  N N 393 
VAL HG13 H  N N 394 
VAL HG21 H  N N 395 
VAL HG22 H  N N 396 
VAL HG23 H  N N 397 
VAL HXT  H  N N 398 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
GLN N   CA   sing N N 70  
GLN N   H    sing N N 71  
GLN N   H2   sing N N 72  
GLN CA  C    sing N N 73  
GLN CA  CB   sing N N 74  
GLN CA  HA   sing N N 75  
GLN C   O    doub N N 76  
GLN C   OXT  sing N N 77  
GLN CB  CG   sing N N 78  
GLN CB  HB2  sing N N 79  
GLN CB  HB3  sing N N 80  
GLN CG  CD   sing N N 81  
GLN CG  HG2  sing N N 82  
GLN CG  HG3  sing N N 83  
GLN CD  OE1  doub N N 84  
GLN CD  NE2  sing N N 85  
GLN NE2 HE21 sing N N 86  
GLN NE2 HE22 sing N N 87  
GLN OXT HXT  sing N N 88  
GLU N   CA   sing N N 89  
GLU N   H    sing N N 90  
GLU N   H2   sing N N 91  
GLU CA  C    sing N N 92  
GLU CA  CB   sing N N 93  
GLU CA  HA   sing N N 94  
GLU C   O    doub N N 95  
GLU C   OXT  sing N N 96  
GLU CB  CG   sing N N 97  
GLU CB  HB2  sing N N 98  
GLU CB  HB3  sing N N 99  
GLU CG  CD   sing N N 100 
GLU CG  HG2  sing N N 101 
GLU CG  HG3  sing N N 102 
GLU CD  OE1  doub N N 103 
GLU CD  OE2  sing N N 104 
GLU OE2 HE2  sing N N 105 
GLU OXT HXT  sing N N 106 
GLY N   CA   sing N N 107 
GLY N   H    sing N N 108 
GLY N   H2   sing N N 109 
GLY CA  C    sing N N 110 
GLY CA  HA2  sing N N 111 
GLY CA  HA3  sing N N 112 
GLY C   O    doub N N 113 
GLY C   OXT  sing N N 114 
GLY OXT HXT  sing N N 115 
GOL C1  O1   sing N N 116 
GOL C1  C2   sing N N 117 
GOL C1  H11  sing N N 118 
GOL C1  H12  sing N N 119 
GOL O1  HO1  sing N N 120 
GOL C2  O2   sing N N 121 
GOL C2  C3   sing N N 122 
GOL C2  H2   sing N N 123 
GOL O2  HO2  sing N N 124 
GOL C3  O3   sing N N 125 
GOL C3  H31  sing N N 126 
GOL C3  H32  sing N N 127 
GOL O3  HO3  sing N N 128 
HIS N   CA   sing N N 129 
HIS N   H    sing N N 130 
HIS N   H2   sing N N 131 
HIS CA  C    sing N N 132 
HIS CA  CB   sing N N 133 
HIS CA  HA   sing N N 134 
HIS C   O    doub N N 135 
HIS C   OXT  sing N N 136 
HIS CB  CG   sing N N 137 
HIS CB  HB2  sing N N 138 
HIS CB  HB3  sing N N 139 
HIS CG  ND1  sing Y N 140 
HIS CG  CD2  doub Y N 141 
HIS ND1 CE1  doub Y N 142 
HIS ND1 HD1  sing N N 143 
HIS CD2 NE2  sing Y N 144 
HIS CD2 HD2  sing N N 145 
HIS CE1 NE2  sing Y N 146 
HIS CE1 HE1  sing N N 147 
HIS NE2 HE2  sing N N 148 
HIS OXT HXT  sing N N 149 
HOH O   H1   sing N N 150 
HOH O   H2   sing N N 151 
ILE N   CA   sing N N 152 
ILE N   H    sing N N 153 
ILE N   H2   sing N N 154 
ILE CA  C    sing N N 155 
ILE CA  CB   sing N N 156 
ILE CA  HA   sing N N 157 
ILE C   O    doub N N 158 
ILE C   OXT  sing N N 159 
ILE CB  CG1  sing N N 160 
ILE CB  CG2  sing N N 161 
ILE CB  HB   sing N N 162 
ILE CG1 CD1  sing N N 163 
ILE CG1 HG12 sing N N 164 
ILE CG1 HG13 sing N N 165 
ILE CG2 HG21 sing N N 166 
ILE CG2 HG22 sing N N 167 
ILE CG2 HG23 sing N N 168 
ILE CD1 HD11 sing N N 169 
ILE CD1 HD12 sing N N 170 
ILE CD1 HD13 sing N N 171 
ILE OXT HXT  sing N N 172 
LEU N   CA   sing N N 173 
LEU N   H    sing N N 174 
LEU N   H2   sing N N 175 
LEU CA  C    sing N N 176 
LEU CA  CB   sing N N 177 
LEU CA  HA   sing N N 178 
LEU C   O    doub N N 179 
LEU C   OXT  sing N N 180 
LEU CB  CG   sing N N 181 
LEU CB  HB2  sing N N 182 
LEU CB  HB3  sing N N 183 
LEU CG  CD1  sing N N 184 
LEU CG  CD2  sing N N 185 
LEU CG  HG   sing N N 186 
LEU CD1 HD11 sing N N 187 
LEU CD1 HD12 sing N N 188 
LEU CD1 HD13 sing N N 189 
LEU CD2 HD21 sing N N 190 
LEU CD2 HD22 sing N N 191 
LEU CD2 HD23 sing N N 192 
LEU OXT HXT  sing N N 193 
LYS N   CA   sing N N 194 
LYS N   H    sing N N 195 
LYS N   H2   sing N N 196 
LYS CA  C    sing N N 197 
LYS CA  CB   sing N N 198 
LYS CA  HA   sing N N 199 
LYS C   O    doub N N 200 
LYS C   OXT  sing N N 201 
LYS CB  CG   sing N N 202 
LYS CB  HB2  sing N N 203 
LYS CB  HB3  sing N N 204 
LYS CG  CD   sing N N 205 
LYS CG  HG2  sing N N 206 
LYS CG  HG3  sing N N 207 
LYS CD  CE   sing N N 208 
LYS CD  HD2  sing N N 209 
LYS CD  HD3  sing N N 210 
LYS CE  NZ   sing N N 211 
LYS CE  HE2  sing N N 212 
LYS CE  HE3  sing N N 213 
LYS NZ  HZ1  sing N N 214 
LYS NZ  HZ2  sing N N 215 
LYS NZ  HZ3  sing N N 216 
LYS OXT HXT  sing N N 217 
MET N   CA   sing N N 218 
MET N   H    sing N N 219 
MET N   H2   sing N N 220 
MET CA  C    sing N N 221 
MET CA  CB   sing N N 222 
MET CA  HA   sing N N 223 
MET C   O    doub N N 224 
MET C   OXT  sing N N 225 
MET CB  CG   sing N N 226 
MET CB  HB2  sing N N 227 
MET CB  HB3  sing N N 228 
MET CG  SD   sing N N 229 
MET CG  HG2  sing N N 230 
MET CG  HG3  sing N N 231 
MET SD  CE   sing N N 232 
MET CE  HE1  sing N N 233 
MET CE  HE2  sing N N 234 
MET CE  HE3  sing N N 235 
MET OXT HXT  sing N N 236 
PHE N   CA   sing N N 237 
PHE N   H    sing N N 238 
PHE N   H2   sing N N 239 
PHE CA  C    sing N N 240 
PHE CA  CB   sing N N 241 
PHE CA  HA   sing N N 242 
PHE C   O    doub N N 243 
PHE C   OXT  sing N N 244 
PHE CB  CG   sing N N 245 
PHE CB  HB2  sing N N 246 
PHE CB  HB3  sing N N 247 
PHE CG  CD1  doub Y N 248 
PHE CG  CD2  sing Y N 249 
PHE CD1 CE1  sing Y N 250 
PHE CD1 HD1  sing N N 251 
PHE CD2 CE2  doub Y N 252 
PHE CD2 HD2  sing N N 253 
PHE CE1 CZ   doub Y N 254 
PHE CE1 HE1  sing N N 255 
PHE CE2 CZ   sing Y N 256 
PHE CE2 HE2  sing N N 257 
PHE CZ  HZ   sing N N 258 
PHE OXT HXT  sing N N 259 
PRO N   CA   sing N N 260 
PRO N   CD   sing N N 261 
PRO N   H    sing N N 262 
PRO CA  C    sing N N 263 
PRO CA  CB   sing N N 264 
PRO CA  HA   sing N N 265 
PRO C   O    doub N N 266 
PRO C   OXT  sing N N 267 
PRO CB  CG   sing N N 268 
PRO CB  HB2  sing N N 269 
PRO CB  HB3  sing N N 270 
PRO CG  CD   sing N N 271 
PRO CG  HG2  sing N N 272 
PRO CG  HG3  sing N N 273 
PRO CD  HD2  sing N N 274 
PRO CD  HD3  sing N N 275 
PRO OXT HXT  sing N N 276 
SER N   CA   sing N N 277 
SER N   H    sing N N 278 
SER N   H2   sing N N 279 
SER CA  C    sing N N 280 
SER CA  CB   sing N N 281 
SER CA  HA   sing N N 282 
SER C   O    doub N N 283 
SER C   OXT  sing N N 284 
SER CB  OG   sing N N 285 
SER CB  HB2  sing N N 286 
SER CB  HB3  sing N N 287 
SER OG  HG   sing N N 288 
SER OXT HXT  sing N N 289 
SO4 S   O1   doub N N 290 
SO4 S   O2   doub N N 291 
SO4 S   O3   sing N N 292 
SO4 S   O4   sing N N 293 
THR N   CA   sing N N 294 
THR N   H    sing N N 295 
THR N   H2   sing N N 296 
THR CA  C    sing N N 297 
THR CA  CB   sing N N 298 
THR CA  HA   sing N N 299 
THR C   O    doub N N 300 
THR C   OXT  sing N N 301 
THR CB  OG1  sing N N 302 
THR CB  CG2  sing N N 303 
THR CB  HB   sing N N 304 
THR OG1 HG1  sing N N 305 
THR CG2 HG21 sing N N 306 
THR CG2 HG22 sing N N 307 
THR CG2 HG23 sing N N 308 
THR OXT HXT  sing N N 309 
TRP N   CA   sing N N 310 
TRP N   H    sing N N 311 
TRP N   H2   sing N N 312 
TRP CA  C    sing N N 313 
TRP CA  CB   sing N N 314 
TRP CA  HA   sing N N 315 
TRP C   O    doub N N 316 
TRP C   OXT  sing N N 317 
TRP CB  CG   sing N N 318 
TRP CB  HB2  sing N N 319 
TRP CB  HB3  sing N N 320 
TRP CG  CD1  doub Y N 321 
TRP CG  CD2  sing Y N 322 
TRP CD1 NE1  sing Y N 323 
TRP CD1 HD1  sing N N 324 
TRP CD2 CE2  doub Y N 325 
TRP CD2 CE3  sing Y N 326 
TRP NE1 CE2  sing Y N 327 
TRP NE1 HE1  sing N N 328 
TRP CE2 CZ2  sing Y N 329 
TRP CE3 CZ3  doub Y N 330 
TRP CE3 HE3  sing N N 331 
TRP CZ2 CH2  doub Y N 332 
TRP CZ2 HZ2  sing N N 333 
TRP CZ3 CH2  sing Y N 334 
TRP CZ3 HZ3  sing N N 335 
TRP CH2 HH2  sing N N 336 
TRP OXT HXT  sing N N 337 
TYR N   CA   sing N N 338 
TYR N   H    sing N N 339 
TYR N   H2   sing N N 340 
TYR CA  C    sing N N 341 
TYR CA  CB   sing N N 342 
TYR CA  HA   sing N N 343 
TYR C   O    doub N N 344 
TYR C   OXT  sing N N 345 
TYR CB  CG   sing N N 346 
TYR CB  HB2  sing N N 347 
TYR CB  HB3  sing N N 348 
TYR CG  CD1  doub Y N 349 
TYR CG  CD2  sing Y N 350 
TYR CD1 CE1  sing Y N 351 
TYR CD1 HD1  sing N N 352 
TYR CD2 CE2  doub Y N 353 
TYR CD2 HD2  sing N N 354 
TYR CE1 CZ   doub Y N 355 
TYR CE1 HE1  sing N N 356 
TYR CE2 CZ   sing Y N 357 
TYR CE2 HE2  sing N N 358 
TYR CZ  OH   sing N N 359 
TYR OH  HH   sing N N 360 
TYR OXT HXT  sing N N 361 
VAL N   CA   sing N N 362 
VAL N   H    sing N N 363 
VAL N   H2   sing N N 364 
VAL CA  C    sing N N 365 
VAL CA  CB   sing N N 366 
VAL CA  HA   sing N N 367 
VAL C   O    doub N N 368 
VAL C   OXT  sing N N 369 
VAL CB  CG1  sing N N 370 
VAL CB  CG2  sing N N 371 
VAL CB  HB   sing N N 372 
VAL CG1 HG11 sing N N 373 
VAL CG1 HG12 sing N N 374 
VAL CG1 HG13 sing N N 375 
VAL CG2 HG21 sing N N 376 
VAL CG2 HG22 sing N N 377 
VAL CG2 HG23 sing N N 378 
VAL OXT HXT  sing N N 379 
# 
_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   8WGG 
_pdbx_initial_refinement_model.details          'PilB protein' 
# 
_atom_sites.entry_id                    8WXD 
_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]   0.016504 
_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]   0.011117 
_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]   0.004621 
_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  
CD 
CL 
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 27  ? 34.670 102.206 11.344   1.00 63.16  ? 29  THR A N   1 
ATOM   2    C  CA  . THR A 1 27  ? 35.142 102.857 10.049   1.00 62.85  ? 29  THR A CA  1 
ATOM   3    C  C   . THR A 1 27  ? 34.060 102.824 8.947    1.00 64.57  ? 29  THR A C   1 
ATOM   4    O  O   . THR A 1 27  ? 33.283 101.853 8.874    1.00 65.77  ? 29  THR A O   1 
ATOM   5    C  CB  . THR A 1 27  ? 36.423 102.228 9.471    1.00 63.75  ? 29  THR A CB  1 
ATOM   6    O  OG1 . THR A 1 27  ? 36.047 101.049 8.756    1.00 63.46  ? 29  THR A OG1 1 
ATOM   7    C  CG2 . THR A 1 27  ? 37.495 101.974 10.513   1.00 65.25  ? 29  THR A CG2 1 
ATOM   8    N  N   . TYR A 1 28  ? 34.038 103.836 8.076    1.00 61.94  ? 30  TYR A N   1 
ATOM   9    C  CA  . TYR A 1 28  ? 32.942 104.060 7.105    1.00 61.72  ? 30  TYR A CA  1 
ATOM   10   C  C   . TYR A 1 28  ? 33.510 104.156 5.693    1.00 60.24  ? 30  TYR A C   1 
ATOM   11   O  O   . TYR A 1 28  ? 34.720 104.320 5.541    1.00 57.71  ? 30  TYR A O   1 
ATOM   12   C  CB  . TYR A 1 28  ? 32.150 105.294 7.531    1.00 60.88  ? 30  TYR A CB  1 
ATOM   13   C  CG  . TYR A 1 28  ? 31.521 105.121 8.885    1.00 61.64  ? 30  TYR A CG  1 
ATOM   14   C  CD1 . TYR A 1 28  ? 30.423 104.288 9.050    1.00 63.38  ? 30  TYR A CD1 1 
ATOM   15   C  CD2 . TYR A 1 28  ? 32.053 105.745 9.999    1.00 61.72  ? 30  TYR A CD2 1 
ATOM   16   C  CE1 . TYR A 1 28  ? 29.843 104.101 10.292   1.00 64.83  ? 30  TYR A CE1 1 
ATOM   17   C  CE2 . TYR A 1 28  ? 31.485 105.566 11.247   1.00 64.66  ? 30  TYR A CE2 1 
ATOM   18   C  CZ  . TYR A 1 28  ? 30.378 104.743 11.396   1.00 65.19  ? 30  TYR A CZ  1 
ATOM   19   O  OH  . TYR A 1 28  ? 29.826 104.568 12.633   1.00 63.70  ? 30  TYR A OH  1 
ATOM   20   N  N   . THR A 1 29  ? 32.628 104.032 4.704    1.00 61.25  ? 31  THR A N   1 
ATOM   21   C  CA  . THR A 1 29  ? 32.966 104.115 3.263    1.00 63.00  ? 31  THR A CA  1 
ATOM   22   C  C   . THR A 1 29  ? 31.963 105.046 2.580    1.00 62.95  ? 31  THR A C   1 
ATOM   23   O  O   . THR A 1 29  ? 30.777 104.653 2.475    1.00 64.85  ? 31  THR A O   1 
ATOM   24   C  CB  . THR A 1 29  ? 33.002 102.729 2.609    1.00 62.97  ? 31  THR A CB  1 
ATOM   25   O  OG1 . THR A 1 29  ? 34.102 102.019 3.165    1.00 63.46  ? 31  THR A OG1 1 
ATOM   26   C  CG2 . THR A 1 29  ? 33.191 102.780 1.113    1.00 63.64  ? 31  THR A CG2 1 
ATOM   27   N  N   . ILE A 1 30  ? 32.424 106.220 2.131    1.00 60.15  ? 32  ILE A N   1 
ATOM   28   C  CA  . ILE A 1 30  ? 31.625 107.129 1.257    1.00 57.80  ? 32  ILE A CA  1 
ATOM   29   C  C   . ILE A 1 30  ? 31.807 106.686 -0.202   1.00 58.64  ? 32  ILE A C   1 
ATOM   30   O  O   . ILE A 1 30  ? 32.961 106.408 -0.618   1.00 61.10  ? 32  ILE A O   1 
ATOM   31   C  CB  . ILE A 1 30  ? 32.008 108.595 1.489    1.00 53.80  ? 32  ILE A CB  1 
ATOM   32   C  CG1 . ILE A 1 30  ? 31.546 109.050 2.873    1.00 52.87  ? 32  ILE A CG1 1 
ATOM   33   C  CG2 . ILE A 1 30  ? 31.457 109.476 0.379    1.00 51.57  ? 32  ILE A CG2 1 
ATOM   34   C  CD1 . ILE A 1 30  ? 32.319 110.234 3.411    1.00 52.85  ? 32  ILE A CD1 1 
ATOM   35   N  N   . GLN A 1 31  ? 30.700 106.568 -0.934   1.00 57.98  ? 33  GLN A N   1 
ATOM   36   C  CA  . GLN A 1 31  ? 30.728 106.329 -2.395   1.00 59.68  ? 33  GLN A CA  1 
ATOM   37   C  C   . GLN A 1 31  ? 30.392 107.641 -3.094   1.00 55.71  ? 33  GLN A C   1 
ATOM   38   O  O   . GLN A 1 31  ? 29.355 108.252 -2.810   1.00 57.43  ? 33  GLN A O   1 
ATOM   39   C  CB  . GLN A 1 31  ? 29.833 105.159 -2.790   1.00 64.68  ? 33  GLN A CB  1 
ATOM   40   C  CG  . GLN A 1 31  ? 30.619 103.856 -2.835   1.00 68.12  ? 33  GLN A CG  1 
ATOM   41   C  CD  . GLN A 1 31  ? 29.752 102.706 -2.412   1.00 72.87  ? 33  GLN A CD  1 
ATOM   42   O  OE1 . GLN A 1 31  ? 30.075 101.963 -1.495   1.00 78.95  ? 33  GLN A OE1 1 
ATOM   43   N  NE2 . GLN A 1 31  ? 28.610 102.586 -3.059   1.00 76.64  ? 33  GLN A NE2 1 
ATOM   44   N  N   . LEU A 1 32  ? 31.294 108.069 -3.959   1.00 51.57  ? 34  LEU A N   1 
ATOM   45   C  CA  . LEU A 1 32  ? 31.222 109.388 -4.614   1.00 47.38  ? 34  LEU A CA  1 
ATOM   46   C  C   . LEU A 1 32  ? 30.829 109.141 -6.066   1.00 44.65  ? 34  LEU A C   1 
ATOM   47   O  O   . LEU A 1 32  ? 31.682 108.741 -6.847   1.00 46.96  ? 34  LEU A O   1 
ATOM   48   C  CB  . LEU A 1 32  ? 32.587 110.056 -4.454   1.00 47.54  ? 34  LEU A CB  1 
ATOM   49   C  CG  . LEU A 1 32  ? 32.676 111.496 -4.933   1.00 46.91  ? 34  LEU A CG  1 
ATOM   50   C  CD1 . LEU A 1 32  ? 31.903 112.435 -4.012   1.00 45.68  ? 34  LEU A CD1 1 
ATOM   51   C  CD2 . LEU A 1 32  ? 34.139 111.887 -5.019   1.00 47.62  ? 34  LEU A CD2 1 
ATOM   52   N  N   . SER A 1 33  ? 29.558 109.350 -6.376   1.00 41.75  ? 35  SER A N   1 
ATOM   53   C  CA  . SER A 1 33  ? 28.942 109.045 -7.676   1.00 41.77  ? 35  SER A CA  1 
ATOM   54   C  C   . SER A 1 33  ? 29.101 110.231 -8.642   1.00 40.49  ? 35  SER A C   1 
ATOM   55   O  O   . SER A 1 33  ? 29.359 111.364 -8.182   1.00 38.70  ? 35  SER A O   1 
ATOM   56   C  CB  . SER A 1 33  ? 27.518 108.676 -7.475   1.00 43.16  ? 35  SER A CB  1 
ATOM   57   O  OG  . SER A 1 33  ? 26.753 109.809 -7.102   1.00 42.58  ? 35  SER A OG  1 
ATOM   58   N  N   . GLY A 1 34  ? 28.954 109.959 -9.944   1.00 39.67  ? 36  GLY A N   1 
ATOM   59   C  CA  . GLY A 1 34  ? 29.119 110.917 -11.045  1.00 37.92  ? 36  GLY A CA  1 
ATOM   60   C  C   . GLY A 1 34  ? 30.582 111.270 -11.292  1.00 37.54  ? 36  GLY A C   1 
ATOM   61   O  O   . GLY A 1 34  ? 30.825 112.369 -11.793  1.00 36.53  ? 36  GLY A O   1 
ATOM   62   N  N   . THR A 1 35  ? 31.558 110.415 -10.971  1.00 37.65  ? 37  THR A N   1 
ATOM   63   C  CA  . THR A 1 35  ? 32.994 110.741 -11.213  1.00 37.58  ? 37  THR A CA  1 
ATOM   64   C  C   . THR A 1 35  ? 33.446 110.221 -12.592  1.00 38.84  ? 37  THR A C   1 
ATOM   65   O  O   . THR A 1 35  ? 32.733 109.439 -13.241  1.00 38.96  ? 37  THR A O   1 
ATOM   66   C  CB  . THR A 1 35  ? 33.886 110.207 -10.090  1.00 39.17  ? 37  THR A CB  1 
ATOM   67   O  OG1 . THR A 1 35  ? 33.664 108.802 -9.976   1.00 42.37  ? 37  THR A OG1 1 
ATOM   68   C  CG2 . THR A 1 35  ? 33.574 110.835 -8.748   1.00 38.20  ? 37  THR A CG2 1 
ATOM   69   N  N   . SER A 1 36  ? 34.602 110.685 -13.029  1.00 38.07  ? 38  SER A N   1 
ATOM   70   C  CA  . SER A 1 36  ? 35.321 110.219 -14.234  1.00 39.56  ? 38  SER A CA  1 
ATOM   71   C  C   . SER A 1 36  ? 36.697 109.781 -13.744  1.00 41.14  ? 38  SER A C   1 
ATOM   72   O  O   . SER A 1 36  ? 37.002 110.014 -12.552  1.00 41.47  ? 38  SER A O   1 
ATOM   73   C  CB  . SER A 1 36  ? 35.391 111.314 -15.286  1.00 37.08  ? 38  SER A CB  1 
ATOM   74   O  OG  . SER A 1 36  ? 36.452 112.214 -15.021  1.00 34.60  ? 38  SER A OG  1 
ATOM   75   N  N   . GLU A 1 37  ? 37.496 109.159 -14.592  1.00 43.29  ? 39  GLU A N   1 
ATOM   76   C  CA  . GLU A 1 37  ? 38.923 108.976 -14.276  1.00 44.62  ? 39  GLU A CA  1 
ATOM   77   C  C   . GLU A 1 37  ? 39.541 110.351 -14.358  1.00 41.49  ? 39  GLU A C   1 
ATOM   78   O  O   . GLU A 1 37  ? 38.844 111.285 -14.820  1.00 39.66  ? 39  GLU A O   1 
ATOM   79   C  CB  . GLU A 1 37  ? 39.609 108.025 -15.239  1.00 49.44  ? 39  GLU A CB  1 
ATOM   80   C  CG  . GLU A 1 37  ? 39.075 106.621 -15.120  1.00 54.07  ? 39  GLU A CG  1 
ATOM   81   C  CD  . GLU A 1 37  ? 40.078 105.577 -15.567  1.00 58.52  ? 39  GLU A CD  1 
ATOM   82   O  OE1 . GLU A 1 37  ? 41.019 105.260 -14.770  1.00 59.73  ? 39  GLU A OE1 1 
ATOM   83   O  OE2 . GLU A 1 37  ? 39.930 105.102 -16.709  1.00 62.31  ? 39  GLU A OE2 1 
ATOM   84   N  N   . GLY A 1 38  ? 40.771 110.447 -13.882  1.00 41.46  ? 40  GLY A N   1 
ATOM   85   C  CA  . GLY A 1 38  ? 41.586 111.660 -14.018  1.00 42.06  ? 40  GLY A CA  1 
ATOM   86   C  C   . GLY A 1 38  ? 41.801 112.400 -12.716  1.00 43.17  ? 40  GLY A C   1 
ATOM   87   O  O   . GLY A 1 38  ? 42.811 113.133 -12.631  1.00 44.75  ? 40  GLY A O   1 
ATOM   88   N  N   . HIS A 1 39  ? 40.912 112.242 -11.728  1.00 41.84  ? 41  HIS A N   1 
ATOM   89   C  CA  . HIS A 1 39  ? 40.934 113.099 -10.520  1.00 40.07  ? 41  HIS A CA  1 
ATOM   90   C  C   . HIS A 1 39  ? 41.656 112.369 -9.396   1.00 41.43  ? 41  HIS A C   1 
ATOM   91   O  O   . HIS A 1 39  ? 41.672 111.119 -9.365   1.00 42.26  ? 41  HIS A O   1 
ATOM   92   C  CB  . HIS A 1 39  ? 39.523 113.555 -10.132  1.00 38.22  ? 41  HIS A CB  1 
ATOM   93   C  CG  . HIS A 1 39  ? 38.731 114.165 -11.246  1.00 36.34  ? 41  HIS A CG  1 
ATOM   94   N  ND1 . HIS A 1 39  ? 38.217 115.439 -11.167  1.00 33.18  ? 41  HIS A ND1 1 
ATOM   95   C  CD2 . HIS A 1 39  ? 38.340 113.667 -12.430  1.00 36.70  ? 41  HIS A CD2 1 
ATOM   96   C  CE1 . HIS A 1 39  ? 37.536 115.704 -12.242  1.00 33.96  ? 41  HIS A CE1 1 
ATOM   97   N  NE2 . HIS A 1 39  ? 37.639 114.650 -13.074  1.00 37.00  ? 41  HIS A NE2 1 
ATOM   98   N  N   . TYR A 1 40  ? 42.236 113.165 -8.507   1.00 42.74  ? 42  TYR A N   1 
ATOM   99   C  CA  . TYR A 1 40  ? 42.687 112.757 -7.156   1.00 43.33  ? 42  TYR A CA  1 
ATOM   100  C  C   . TYR A 1 40  ? 41.887 113.573 -6.145   1.00 39.52  ? 42  TYR A C   1 
ATOM   101  O  O   . TYR A 1 40  ? 42.147 114.776 -5.981   1.00 36.83  ? 42  TYR A O   1 
ATOM   102  C  CB  . TYR A 1 40  ? 44.193 112.957 -7.010   1.00 47.69  ? 42  TYR A CB  1 
ATOM   103  C  CG  . TYR A 1 40  ? 45.010 112.248 -8.057   1.00 51.58  ? 42  TYR A CG  1 
ATOM   104  C  CD1 . TYR A 1 40  ? 45.495 110.975 -7.831   1.00 54.78  ? 42  TYR A CD1 1 
ATOM   105  C  CD2 . TYR A 1 40  ? 45.302 112.861 -9.271   1.00 52.70  ? 42  TYR A CD2 1 
ATOM   106  C  CE1 . TYR A 1 40  ? 46.252 110.327 -8.795   1.00 59.26  ? 42  TYR A CE1 1 
ATOM   107  C  CE2 . TYR A 1 40  ? 46.047 112.226 -10.246  1.00 54.82  ? 42  TYR A CE2 1 
ATOM   108  C  CZ  . TYR A 1 40  ? 46.528 110.955 -10.001  1.00 58.38  ? 42  TYR A CZ  1 
ATOM   109  O  OH  . TYR A 1 40  ? 47.277 110.329 -10.948  1.00 62.09  ? 42  TYR A OH  1 
ATOM   110  N  N   . TYR A 1 41  ? 40.892 112.925 -5.543   1.00 36.66  ? 43  TYR A N   1 
ATOM   111  C  CA  . TYR A 1 41  ? 40.009 113.512 -4.518   1.00 34.30  ? 43  TYR A CA  1 
ATOM   112  C  C   . TYR A 1 41  ? 40.687 113.402 -3.160   1.00 34.33  ? 43  TYR A C   1 
ATOM   113  O  O   . TYR A 1 41  ? 41.122 112.340 -2.779   1.00 35.76  ? 43  TYR A O   1 
ATOM   114  C  CB  . TYR A 1 41  ? 38.663 112.819 -4.595   1.00 33.17  ? 43  TYR A CB  1 
ATOM   115  C  CG  . TYR A 1 41  ? 37.885 113.230 -5.813   1.00 31.76  ? 43  TYR A CG  1 
ATOM   116  C  CD1 . TYR A 1 41  ? 37.459 114.544 -5.939   1.00 30.14  ? 43  TYR A CD1 1 
ATOM   117  C  CD2 . TYR A 1 41  ? 37.564 112.336 -6.834   1.00 32.02  ? 43  TYR A CD2 1 
ATOM   118  C  CE1 . TYR A 1 41  ? 36.736 114.966 -7.045   1.00 29.08  ? 43  TYR A CE1 1 
ATOM   119  C  CE2 . TYR A 1 41  ? 36.828 112.745 -7.945   1.00 30.90  ? 43  TYR A CE2 1 
ATOM   120  C  CZ  . TYR A 1 41  ? 36.442 114.068 -8.053   1.00 29.17  ? 43  TYR A CZ  1 
ATOM   121  O  OH  . TYR A 1 41  ? 35.692 114.550 -9.064   1.00 27.83  ? 43  TYR A OH  1 
ATOM   122  N  N   . GLU A 1 42  ? 40.848 114.530 -2.496   1.00 34.49  ? 44  GLU A N   1 
ATOM   123  C  CA  . GLU A 1 42  ? 41.441 114.611 -1.141   1.00 36.14  ? 44  GLU A CA  1 
ATOM   124  C  C   . GLU A 1 42  ? 40.332 114.748 -0.106   1.00 33.44  ? 44  GLU A C   1 
ATOM   125  O  O   . GLU A 1 42  ? 39.451 115.592 -0.277   1.00 31.27  ? 44  GLU A O   1 
ATOM   126  C  CB  . GLU A 1 42  ? 42.404 115.787 -1.053   1.00 38.89  ? 44  GLU A CB  1 
ATOM   127  C  CG  . GLU A 1 42  ? 43.680 115.536 -1.825   1.00 42.27  ? 44  GLU A CG  1 
ATOM   128  C  CD  . GLU A 1 42  ? 44.707 116.653 -1.798   1.00 44.22  ? 44  GLU A CD  1 
ATOM   129  O  OE1 . GLU A 1 42  ? 44.333 117.804 -1.437   1.00 43.33  ? 44  GLU A OE1 1 
ATOM   130  O  OE2 . GLU A 1 42  ? 45.874 116.373 -2.193   1.00 48.17  ? 44  GLU A OE2 1 
ATOM   131  N  N   . VAL A 1 43  ? 40.393 113.910 0.923    1.00 34.07  ? 45  VAL A N   1 
ATOM   132  C  CA  . VAL A 1 43  ? 39.353 113.782 1.971    1.00 32.35  ? 45  VAL A CA  1 
ATOM   133  C  C   . VAL A 1 43  ? 39.993 114.134 3.305    1.00 31.72  ? 45  VAL A C   1 
ATOM   134  O  O   . VAL A 1 43  ? 40.895 113.415 3.741    1.00 33.03  ? 45  VAL A O   1 
ATOM   135  C  CB  . VAL A 1 43  ? 38.777 112.365 1.978    1.00 33.89  ? 45  VAL A CB  1 
ATOM   136  C  CG1 . VAL A 1 43  ? 37.607 112.289 2.937    1.00 33.19  ? 45  VAL A CG1 1 
ATOM   137  C  CG2 . VAL A 1 43  ? 38.382 111.924 0.576    1.00 33.90  ? 45  VAL A CG2 1 
ATOM   138  N  N   . TYR A 1 44  ? 39.599 115.264 3.858    1.00 28.91  ? 46  TYR A N   1 
ATOM   139  C  CA  . TYR A 1 44  ? 40.223 115.858 5.057    1.00 28.88  ? 46  TYR A CA  1 
ATOM   140  C  C   . TYR A 1 44  ? 39.333 115.573 6.276    1.00 26.89  ? 46  TYR A C   1 
ATOM   141  O  O   . TYR A 1 44  ? 38.138 115.922 6.294    1.00 25.91  ? 46  TYR A O   1 
ATOM   142  C  CB  . TYR A 1 44  ? 40.466 117.350 4.826    1.00 28.19  ? 46  TYR A CB  1 
ATOM   143  C  CG  . TYR A 1 44  ? 41.573 117.634 3.855    1.00 29.35  ? 46  TYR A CG  1 
ATOM   144  C  CD1 . TYR A 1 44  ? 41.318 117.637 2.498    1.00 28.33  ? 46  TYR A CD1 1 
ATOM   145  C  CD2 . TYR A 1 44  ? 42.867 117.914 4.288    1.00 30.58  ? 46  TYR A CD2 1 
ATOM   146  C  CE1 . TYR A 1 44  ? 42.325 117.910 1.591    1.00 29.86  ? 46  TYR A CE1 1 
ATOM   147  C  CE2 . TYR A 1 44  ? 43.888 118.182 3.384    1.00 31.43  ? 46  TYR A CE2 1 
ATOM   148  C  CZ  . TYR A 1 44  ? 43.608 118.178 2.031    1.00 31.01  ? 46  TYR A CZ  1 
ATOM   149  O  OH  . TYR A 1 44  ? 44.572 118.428 1.108    1.00 32.68  ? 46  TYR A OH  1 
ATOM   150  N  N   . HIS A 1 45  ? 39.894 114.908 7.265    1.00 26.77  ? 47  HIS A N   1 
ATOM   151  C  CA  . HIS A 1 45  ? 39.214 114.630 8.552    1.00 25.96  ? 47  HIS A CA  1 
ATOM   152  C  C   . HIS A 1 45  ? 39.120 115.955 9.335    1.00 24.90  ? 47  HIS A C   1 
ATOM   153  O  O   . HIS A 1 45  ? 40.163 116.427 9.813    1.00 25.29  ? 47  HIS A O   1 
ATOM   154  C  CB  . HIS A 1 45  ? 39.944 113.496 9.285    1.00 27.50  ? 47  HIS A CB  1 
ATOM   155  C  CG  . HIS A 1 45  ? 39.088 112.841 10.314   1.00 27.99  ? 47  HIS A CG  1 
ATOM   156  N  ND1 . HIS A 1 45  ? 39.569 111.871 11.169   1.00 30.39  ? 47  HIS A ND1 1 
ATOM   157  C  CD2 . HIS A 1 45  ? 37.776 112.999 10.628   1.00 27.12  ? 47  HIS A CD2 1 
ATOM   158  C  CE1 . HIS A 1 45  ? 38.585 111.488 11.988   1.00 29.61  ? 47  HIS A CE1 1 
ATOM   159  N  NE2 . HIS A 1 45  ? 37.478 112.150 11.673   1.00 27.75  ? 47  HIS A NE2 1 
ATOM   160  N  N   . ILE A 1 46  ? 37.930 116.557 9.420    1.00 23.11  ? 48  ILE A N   1 
ATOM   161  C  CA  . ILE A 1 46  ? 37.689 117.889 10.045   1.00 22.60  ? 48  ILE A CA  1 
ATOM   162  C  C   . ILE A 1 46  ? 37.283 117.704 11.517   1.00 22.89  ? 48  ILE A C   1 
ATOM   163  O  O   . ILE A 1 46  ? 37.827 118.396 12.378   1.00 24.06  ? 48  ILE A O   1 
ATOM   164  C  CB  . ILE A 1 46  ? 36.603 118.652 9.267    1.00 21.37  ? 48  ILE A CB  1 
ATOM   165  C  CG1 . ILE A 1 46  ? 36.935 118.794 7.774    1.00 21.75  ? 48  ILE A CG1 1 
ATOM   166  C  CG2 . ILE A 1 46  ? 36.318 119.999 9.913    1.00 20.89  ? 48  ILE A CG2 1 
ATOM   167  C  CD1 . ILE A 1 46  ? 38.324 119.323 7.447    1.00 22.05  ? 48  ILE A CD1 1 
ATOM   168  N  N   . PHE A 1 47  ? 36.260 116.891 11.783   1.00 23.06  ? 49  PHE A N   1 
ATOM   169  C  CA  . PHE A 1 47  ? 35.795 116.568 13.150   1.00 23.67  ? 49  PHE A CA  1 
ATOM   170  C  C   . PHE A 1 47  ? 35.918 115.060 13.307   1.00 26.12  ? 49  PHE A C   1 
ATOM   171  O  O   . PHE A 1 47  ? 35.487 114.334 12.415   1.00 25.57  ? 49  PHE A O   1 
ATOM   172  C  CB  . PHE A 1 47  ? 34.344 116.977 13.392   1.00 21.86  ? 49  PHE A CB  1 
ATOM   173  C  CG  . PHE A 1 47  ? 34.035 118.449 13.339   1.00 20.33  ? 49  PHE A CG  1 
ATOM   174  C  CD1 . PHE A 1 47  ? 34.878 119.385 13.901   1.00 20.61  ? 49  PHE A CD1 1 
ATOM   175  C  CD2 . PHE A 1 47  ? 32.842 118.900 12.818   1.00 19.07  ? 49  PHE A CD2 1 
ATOM   176  C  CE1 . PHE A 1 47  ? 34.544 120.738 13.910   1.00 19.94  ? 49  PHE A CE1 1 
ATOM   177  C  CE2 . PHE A 1 47  ? 32.527 120.250 12.809   1.00 18.54  ? 49  PHE A CE2 1 
ATOM   178  C  CZ  . PHE A 1 47  ? 33.382 121.173 13.331   1.00 18.75  ? 49  PHE A CZ  1 
ATOM   179  N  N   . SER A 1 48  ? 36.513 114.627 14.419   1.00 29.34  ? 50  SER A N   1 
ATOM   180  C  CA  . SER A 1 48  ? 36.336 113.275 15.007   1.00 31.24  ? 50  SER A CA  1 
ATOM   181  C  C   . SER A 1 48  ? 35.159 113.347 15.975   1.00 31.62  ? 50  SER A C   1 
ATOM   182  O  O   . SER A 1 48  ? 34.840 114.419 16.505   1.00 30.03  ? 50  SER A O   1 
ATOM   183  C  CB  . SER A 1 48  ? 37.573 112.788 15.707   1.00 32.51  ? 50  SER A CB  1 
ATOM   184  O  OG  . SER A 1 48  ? 38.035 113.763 16.629   1.00 32.19  ? 50  SER A OG  1 
ATOM   185  N  N   . GLY A 1 49  ? 34.489 112.228 16.137   1.00 34.57  ? 51  GLY A N   1 
ATOM   186  C  CA  . GLY A 1 49  ? 33.468 112.058 17.178   1.00 36.36  ? 51  GLY A CA  1 
ATOM   187  C  C   . GLY A 1 49  ? 32.853 110.691 17.046   1.00 39.28  ? 51  GLY A C   1 
ATOM   188  O  O   . GLY A 1 49  ? 33.333 109.903 16.230   1.00 41.61  ? 51  GLY A O   1 
ATOM   189  N  N   . THR A 1 50  ? 31.779 110.435 17.774   1.00 41.59  ? 52  THR A N   1 
ATOM   190  C  CA  . THR A 1 50  ? 31.062 109.145 17.730   1.00 44.06  ? 52  THR A CA  1 
ATOM   191  C  C   . THR A 1 50  ? 29.726 109.396 17.032   1.00 45.67  ? 52  THR A C   1 
ATOM   192  O  O   . THR A 1 50  ? 29.021 110.400 17.331   1.00 40.77  ? 52  THR A O   1 
ATOM   193  C  CB  . THR A 1 50  ? 31.028 108.521 19.128   1.00 45.22  ? 52  THR A CB  1 
ATOM   194  O  OG1 . THR A 1 50  ? 30.447 109.488 20.007   1.00 43.55  ? 52  THR A OG1 1 
ATOM   195  C  CG2 . THR A 1 50  ? 32.419 108.147 19.617   1.00 45.84  ? 52  THR A CG2 1 
ATOM   196  N  N   . LEU A 1 51  ? 29.465 108.541 16.057   1.00 50.39  ? 53  LEU A N   1 
ATOM   197  C  CA  . LEU A 1 51  ? 28.167 108.459 15.365   1.00 56.71  ? 53  LEU A CA  1 
ATOM   198  C  C   . LEU A 1 51  ? 27.353 107.389 16.080   1.00 63.72  ? 53  LEU A C   1 
ATOM   199  O  O   . LEU A 1 51  ? 27.862 106.269 16.209   1.00 70.62  ? 53  LEU A O   1 
ATOM   200  C  CB  . LEU A 1 51  ? 28.425 108.090 13.903   1.00 57.76  ? 53  LEU A CB  1 
ATOM   201  C  CG  . LEU A 1 51  ? 27.313 108.541 12.974   1.00 56.72  ? 53  LEU A CG  1 
ATOM   202  C  CD1 . LEU A 1 51  ? 27.564 109.983 12.566   1.00 54.88  ? 53  LEU A CD1 1 
ATOM   203  C  CD2 . LEU A 1 51  ? 27.180 107.602 11.784   1.00 58.48  ? 53  LEU A CD2 1 
ATOM   204  N  N   . ASP A 1 52  ? 26.165 107.707 16.582   1.00 69.65  ? 54  ASP A N   1 
ATOM   205  C  CA  . ASP A 1 52  ? 25.411 106.733 17.428   1.00 74.81  ? 54  ASP A CA  1 
ATOM   206  C  C   . ASP A 1 52  ? 24.472 105.944 16.504   1.00 77.88  ? 54  ASP A C   1 
ATOM   207  O  O   . ASP A 1 52  ? 24.587 106.116 15.261   1.00 75.13  ? 54  ASP A O   1 
ATOM   208  C  CB  . ASP A 1 52  ? 24.749 107.398 18.647   1.00 74.81  ? 54  ASP A CB  1 
ATOM   209  C  CG  . ASP A 1 52  ? 24.718 108.922 18.591   1.00 73.44  ? 54  ASP A CG  1 
ATOM   210  O  OD1 . ASP A 1 52  ? 24.063 109.451 17.648   1.00 68.71  ? 54  ASP A OD1 1 
ATOM   211  O  OD2 . ASP A 1 52  ? 25.362 109.572 19.480   1.00 67.60  ? 54  ASP A OD2 1 
ATOM   212  N  N   . THR A 1 53  ? 23.629 105.080 17.088   1.00 81.19  ? 55  THR A N   1 
ATOM   213  C  CA  . THR A 1 53  ? 22.457 104.432 16.430   1.00 83.75  ? 55  THR A CA  1 
ATOM   214  C  C   . THR A 1 53  ? 21.650 105.534 15.701   1.00 84.25  ? 55  THR A C   1 
ATOM   215  O  O   . THR A 1 53  ? 21.325 105.354 14.495   1.00 80.81  ? 55  THR A O   1 
ATOM   216  C  CB  . THR A 1 53  ? 21.691 103.564 17.453   1.00 84.31  ? 55  THR A CB  1 
ATOM   217  O  OG1 . THR A 1 53  ? 21.740 104.158 18.756   1.00 78.02  ? 55  THR A OG1 1 
ATOM   218  C  CG2 . THR A 1 53  ? 22.245 102.159 17.574   1.00 83.85  ? 55  THR A CG2 1 
ATOM   219  N  N   . SER A 1 54  ? 21.402 106.671 16.371   1.00 84.09  ? 56  SER A N   1 
ATOM   220  C  CA  . SER A 1 54  ? 20.855 107.913 15.757   1.00 79.71  ? 56  SER A CA  1 
ATOM   221  C  C   . SER A 1 54  ? 21.951 108.554 14.892   1.00 76.94  ? 56  SER A C   1 
ATOM   222  O  O   . SER A 1 54  ? 23.163 108.264 15.109   1.00 71.71  ? 56  SER A O   1 
ATOM   223  C  CB  . SER A 1 54  ? 20.313 108.872 16.804   1.00 78.39  ? 56  SER A CB  1 
ATOM   224  O  OG  . SER A 1 54  ? 21.356 109.475 17.555   1.00 73.92  ? 56  SER A OG  1 
ATOM   225  N  N   . ASN A 1 55  ? 21.570 109.403 13.941   1.00 75.30  ? 57  ASN A N   1 
ATOM   226  C  CA  . ASN A 1 55  ? 22.535 109.901 12.923   1.00 66.35  ? 57  ASN A CA  1 
ATOM   227  C  C   . ASN A 1 55  ? 23.222 111.178 13.437   1.00 57.33  ? 57  ASN A C   1 
ATOM   228  O  O   . ASN A 1 55  ? 23.619 111.993 12.620   1.00 52.84  ? 57  ASN A O   1 
ATOM   229  C  CB  . ASN A 1 55  ? 21.842 110.040 11.563   1.00 68.57  ? 57  ASN A CB  1 
ATOM   230  C  CG  . ASN A 1 55  ? 22.763 109.762 10.388   1.00 66.93  ? 57  ASN A CG  1 
ATOM   231  O  OD1 . ASN A 1 55  ? 22.311 109.657 9.254    1.00 67.86  ? 57  ASN A OD1 1 
ATOM   232  N  ND2 . ASN A 1 55  ? 24.054 109.641 10.632   1.00 63.00  ? 57  ASN A ND2 1 
ATOM   233  N  N   . THR A 1 56  ? 23.372 111.357 14.756   1.00 54.48  ? 58  THR A N   1 
ATOM   234  C  CA  . THR A 1 56  ? 24.040 112.566 15.334   1.00 47.97  ? 58  THR A CA  1 
ATOM   235  C  C   . THR A 1 56  ? 25.519 112.239 15.631   1.00 41.00  ? 58  THR A C   1 
ATOM   236  O  O   . THR A 1 56  ? 25.876 111.056 15.852   1.00 38.25  ? 58  THR A O   1 
ATOM   237  C  CB  . THR A 1 56  ? 23.278 113.186 16.528   1.00 49.06  ? 58  THR A CB  1 
ATOM   238  O  OG1 . THR A 1 56  ? 23.896 112.718 17.726   1.00 49.10  ? 58  THR A OG1 1 
ATOM   239  C  CG2 . THR A 1 56  ? 21.783 112.905 16.553   1.00 50.24  ? 58  THR A CG2 1 
ATOM   240  N  N   . LEU A 1 57  ? 26.360 113.265 15.538   1.00 35.77  ? 59  LEU A N   1 
ATOM   241  C  CA  . LEU A 1 57  ? 27.794 113.196 15.880   1.00 33.28  ? 59  LEU A CA  1 
ATOM   242  C  C   . LEU A 1 57  ? 27.961 113.811 17.257   1.00 32.40  ? 59  LEU A C   1 
ATOM   243  O  O   . LEU A 1 57  ? 27.502 114.962 17.456   1.00 28.74  ? 59  LEU A O   1 
ATOM   244  C  CB  . LEU A 1 57  ? 28.618 113.992 14.867   1.00 31.66  ? 59  LEU A CB  1 
ATOM   245  C  CG  . LEU A 1 57  ? 30.121 113.692 14.884   1.00 31.25  ? 59  LEU A CG  1 
ATOM   246  C  CD1 . LEU A 1 57  ? 30.411 112.263 14.427   1.00 31.79  ? 59  LEU A CD1 1 
ATOM   247  C  CD2 . LEU A 1 57  ? 30.883 114.693 14.027   1.00 30.03  ? 59  LEU A CD2 1 
ATOM   248  N  N   . THR A 1 58  ? 28.633 113.080 18.137   1.00 33.38  ? 60  THR A N   1 
ATOM   249  C  CA  . THR A 1 58  ? 28.876 113.529 19.524   1.00 34.29  ? 60  THR A CA  1 
ATOM   250  C  C   . THR A 1 58  ? 30.359 113.431 19.873   1.00 35.27  ? 60  THR A C   1 
ATOM   251  O  O   . THR A 1 58  ? 31.113 112.668 19.254   1.00 33.71  ? 60  THR A O   1 
ATOM   252  C  CB  . THR A 1 58  ? 28.046 112.720 20.528   1.00 34.79  ? 60  THR A CB  1 
ATOM   253  O  OG1 . THR A 1 58  ? 28.135 111.362 20.104   1.00 36.26  ? 60  THR A OG1 1 
ATOM   254  C  CG2 . THR A 1 58  ? 26.587 113.122 20.586   1.00 35.04  ? 60  THR A CG2 1 
ATOM   255  N  N   . ASN A 1 59  ? 30.731 114.161 20.919   1.00 37.35  ? 61  ASN A N   1 
ATOM   256  C  CA  . ASN A 1 59  ? 32.098 114.145 21.492   1.00 37.82  ? 61  ASN A CA  1 
ATOM   257  C  C   . ASN A 1 59  ? 33.016 114.622 20.368   1.00 36.30  ? 61  ASN A C   1 
ATOM   258  O  O   . ASN A 1 59  ? 33.962 113.886 20.024   1.00 36.83  ? 61  ASN A O   1 
ATOM   259  C  CB  . ASN A 1 59  ? 32.424 112.779 22.105   1.00 39.59  ? 61  ASN A CB  1 
ATOM   260  C  CG  . ASN A 1 59  ? 31.306 112.255 22.995   1.00 40.32  ? 61  ASN A CG  1 
ATOM   261  O  OD1 . ASN A 1 59  ? 30.985 111.078 22.907   1.00 43.44  ? 61  ASN A OD1 1 
ATOM   262  N  ND2 . ASN A 1 59  ? 30.691 113.090 23.827   1.00 36.88  ? 61  ASN A ND2 1 
ATOM   263  N  N   . ILE A 1 60  ? 32.712 115.825 19.856   1.00 33.89  ? 62  ILE A N   1 
ATOM   264  C  CA  . ILE A 1 60  ? 33.333 116.422 18.642   1.00 32.35  ? 62  ILE A CA  1 
ATOM   265  C  C   . ILE A 1 60  ? 34.613 117.146 19.045   1.00 32.89  ? 62  ILE A C   1 
ATOM   266  O  O   . ILE A 1 60  ? 34.579 117.986 19.975   1.00 33.70  ? 62  ILE A O   1 
ATOM   267  C  CB  . ILE A 1 60  ? 32.343 117.357 17.943   1.00 30.93  ? 62  ILE A CB  1 
ATOM   268  C  CG1 . ILE A 1 60  ? 31.166 116.554 17.387   1.00 30.24  ? 62  ILE A CG1 1 
ATOM   269  C  CG2 . ILE A 1 60  ? 33.054 118.178 16.883   1.00 29.82  ? 62  ILE A CG2 1 
ATOM   270  C  CD1 . ILE A 1 60  ? 29.930 117.382 17.148   1.00 30.12  ? 62  ILE A CD1 1 
ATOM   271  N  N   . GLU A 1 61  ? 35.708 116.741 18.417   1.00 32.73  ? 63  GLU A N   1 
ATOM   272  C  CA  . GLU A 1 61  ? 37.042 117.355 18.532   1.00 33.71  ? 63  GLU A CA  1 
ATOM   273  C  C   . GLU A 1 61  ? 37.533 117.643 17.103   1.00 31.95  ? 63  GLU A C   1 
ATOM   274  O  O   . GLU A 1 61  ? 37.026 117.041 16.136   1.00 29.07  ? 63  GLU A O   1 
ATOM   275  C  CB  . GLU A 1 61  ? 37.916 116.397 19.338   1.00 39.88  ? 63  GLU A CB  1 
ATOM   276  C  CG  . GLU A 1 61  ? 37.507 116.258 20.828   1.00 44.28  ? 63  GLU A CG  1 
ATOM   277  C  CD  . GLU A 1 61  ? 37.960 117.388 21.774   1.00 51.04  ? 63  GLU A CD  1 
ATOM   278  O  OE1 . GLU A 1 61  ? 38.778 118.235 21.328   1.00 56.13  ? 63  GLU A OE1 1 
ATOM   279  O  OE2 . GLU A 1 61  ? 37.545 117.427 22.995   1.00 55.71  ? 63  GLU A OE2 1 
ATOM   280  N  N   . TRP A 1 62  ? 38.472 118.570 16.969   1.00 30.42  ? 64  TRP A N   1 
ATOM   281  C  CA  . TRP A 1 62  ? 39.176 118.830 15.697   1.00 29.43  ? 64  TRP A CA  1 
ATOM   282  C  C   . TRP A 1 62  ? 40.018 117.605 15.404   1.00 31.31  ? 64  TRP A C   1 
ATOM   283  O  O   . TRP A 1 62  ? 40.630 117.087 16.347   1.00 30.35  ? 64  TRP A O   1 
ATOM   284  C  CB  . TRP A 1 62  ? 40.029 120.077 15.773   1.00 28.55  ? 64  TRP A CB  1 
ATOM   285  C  CG  . TRP A 1 62  ? 39.262 121.341 15.973   1.00 26.78  ? 64  TRP A CG  1 
ATOM   286  C  CD1 . TRP A 1 62  ? 39.252 122.135 17.093   1.00 26.49  ? 64  TRP A CD1 1 
ATOM   287  C  CD2 . TRP A 1 62  ? 38.459 122.003 14.982   1.00 24.89  ? 64  TRP A CD2 1 
ATOM   288  N  NE1 . TRP A 1 62  ? 38.467 123.238 16.872   1.00 26.03  ? 64  TRP A NE1 1 
ATOM   289  C  CE2 . TRP A 1 62  ? 37.970 123.181 15.588   1.00 24.79  ? 64  TRP A CE2 1 
ATOM   290  C  CE3 . TRP A 1 62  ? 38.093 121.700 13.662   1.00 23.57  ? 64  TRP A CE3 1 
ATOM   291  C  CZ2 . TRP A 1 62  ? 37.132 124.056 14.897   1.00 24.44  ? 64  TRP A CZ2 1 
ATOM   292  C  CZ3 . TRP A 1 62  ? 37.268 122.564 12.992   1.00 23.03  ? 64  TRP A CZ3 1 
ATOM   293  C  CH2 . TRP A 1 62  ? 36.791 123.726 13.600   1.00 23.46  ? 64  TRP A CH2 1 
ATOM   294  N  N   . ALA A 1 63  ? 39.960 117.129 14.161   1.00 32.71  ? 65  ALA A N   1 
ATOM   295  C  CA  . ALA A 1 63  ? 40.761 115.983 13.696   1.00 34.94  ? 65  ALA A CA  1 
ATOM   296  C  C   . ALA A 1 63  ? 42.015 116.530 13.026   1.00 37.10  ? 65  ALA A C   1 
ATOM   297  O  O   . ALA A 1 63  ? 42.195 117.741 12.896   1.00 36.51  ? 65  ALA A O   1 
ATOM   298  C  CB  . ALA A 1 63  ? 39.930 115.119 12.800   1.00 34.64  ? 65  ALA A CB  1 
ATOM   299  N  N   . PRO A 1 64  ? 42.949 115.659 12.610   1.00 40.18  ? 66  PRO A N   1 
ATOM   300  C  CA  . PRO A 1 64  ? 44.259 116.121 12.149   1.00 41.21  ? 66  PRO A CA  1 
ATOM   301  C  C   . PRO A 1 64  ? 44.209 116.895 10.812   1.00 40.00  ? 66  PRO A C   1 
ATOM   302  O  O   . PRO A 1 64  ? 45.188 117.520 10.444   1.00 40.15  ? 66  PRO A O   1 
ATOM   303  C  CB  . PRO A 1 64  ? 45.097 114.831 12.002   1.00 43.96  ? 66  PRO A CB  1 
ATOM   304  C  CG  . PRO A 1 64  ? 44.192 113.651 12.416   1.00 45.08  ? 66  PRO A CG  1 
ATOM   305  C  CD  . PRO A 1 64  ? 42.781 114.197 12.537   1.00 43.12  ? 66  PRO A CD  1 
ATOM   306  N  N   . GLY A 1 65  ? 43.082 116.842 10.100   1.00 36.66  ? 67  GLY A N   1 
ATOM   307  C  CA  . GLY A 1 65  ? 42.915 117.548 8.827    1.00 35.88  ? 67  GLY A CA  1 
ATOM   308  C  C   . GLY A 1 65  ? 42.809 119.042 9.020    1.00 33.89  ? 67  GLY A C   1 
ATOM   309  O  O   . GLY A 1 65  ? 42.797 119.745 8.004    1.00 32.86  ? 67  GLY A O   1 
ATOM   310  N  N   . VAL A 1 66  ? 42.700 119.543 10.243   1.00 31.21  ? 68  VAL A N   1 
ATOM   311  C  CA  . VAL A 1 66  ? 42.607 121.018 10.408   1.00 30.90  ? 68  VAL A CA  1 
ATOM   312  C  C   . VAL A 1 66  ? 43.827 121.513 11.165   1.00 34.08  ? 68  VAL A C   1 
ATOM   313  O  O   . VAL A 1 66  ? 44.182 120.857 12.165   1.00 35.78  ? 68  VAL A O   1 
ATOM   314  C  CB  . VAL A 1 66  ? 41.315 121.424 11.113   1.00 28.60  ? 68  VAL A CB  1 
ATOM   315  C  CG1 . VAL A 1 66  ? 41.210 122.932 11.243   1.00 28.10  ? 68  VAL A CG1 1 
ATOM   316  C  CG2 . VAL A 1 66  ? 40.110 120.831 10.423   1.00 27.19  ? 68  VAL A CG2 1 
ATOM   317  N  N   . THR A 1 67  ? 44.410 122.640 10.734   1.00 36.07  ? 69  THR A N   1 
ATOM   318  C  CA  . THR A 1 67  ? 45.635 123.220 11.345   1.00 38.62  ? 69  THR A CA  1 
ATOM   319  C  C   . THR A 1 67  ? 45.243 123.917 12.638   1.00 40.56  ? 69  THR A C   1 
ATOM   320  O  O   . THR A 1 67  ? 44.024 124.171 12.828   1.00 39.28  ? 69  THR A O   1 
ATOM   321  C  CB  . THR A 1 67  ? 46.360 124.203 10.428   1.00 38.09  ? 69  THR A CB  1 
ATOM   322  O  OG1 . THR A 1 67  ? 45.508 125.334 10.257   1.00 37.32  ? 69  THR A OG1 1 
ATOM   323  C  CG2 . THR A 1 67  ? 46.747 123.567 9.111    1.00 37.80  ? 69  THR A CG2 1 
ATOM   324  N  N   . GLU A 1 68  ? 46.242 124.195 13.482   1.00 44.93  ? 70  GLU A N   1 
ATOM   325  C  CA  . GLU A 1 68  ? 46.016 124.820 14.808   1.00 46.35  ? 70  GLU A CA  1 
ATOM   326  C  C   . GLU A 1 68  ? 45.506 126.252 14.592   1.00 43.50  ? 70  GLU A C   1 
ATOM   327  O  O   . GLU A 1 68  ? 44.727 126.756 15.442   1.00 42.07  ? 70  GLU A O   1 
ATOM   328  C  CB  . GLU A 1 68  ? 47.273 124.697 15.671   1.00 52.72  ? 70  GLU A CB  1 
ATOM   329  C  CG  . GLU A 1 68  ? 47.239 123.488 16.620   1.00 57.75  ? 70  GLU A CG  1 
ATOM   330  C  CD  . GLU A 1 68  ? 46.119 123.452 17.667   1.00 61.05  ? 70  GLU A CD  1 
ATOM   331  O  OE1 . GLU A 1 68  ? 45.585 124.529 18.019   1.00 65.40  ? 70  GLU A OE1 1 
ATOM   332  O  OE2 . GLU A 1 68  ? 45.775 122.346 18.153   1.00 64.14  ? 70  GLU A OE2 1 
ATOM   333  N  N   . ALA A 1 69  ? 45.865 126.864 13.467   1.00 40.70  ? 71  ALA A N   1 
ATOM   334  C  CA  . ALA A 1 69  ? 45.415 128.222 13.099   1.00 39.46  ? 71  ALA A CA  1 
ATOM   335  C  C   . ALA A 1 69  ? 43.901 128.196 12.842   1.00 36.93  ? 71  ALA A C   1 
ATOM   336  O  O   . ALA A 1 69  ? 43.158 129.093 13.311   1.00 34.69  ? 71  ALA A O   1 
ATOM   337  C  CB  . ALA A 1 69  ? 46.189 128.669 11.888   1.00 40.60  ? 71  ALA A CB  1 
ATOM   338  N  N   . GLY A 1 70  ? 43.458 127.188 12.093   1.00 36.03  ? 72  GLY A N   1 
ATOM   339  C  CA  . GLY A 1 70  ? 42.025 126.966 11.853   1.00 34.10  ? 72  GLY A CA  1 
ATOM   340  C  C   . GLY A 1 70  ? 41.304 126.724 13.167   1.00 32.33  ? 72  GLY A C   1 
ATOM   341  O  O   . GLY A 1 70  ? 40.276 127.386 13.408   1.00 30.51  ? 72  GLY A O   1 
ATOM   342  N  N   . ARG A 1 71  ? 41.809 125.779 13.962   1.00 33.36  ? 73  ARG A N   1 
ATOM   343  C  CA  . ARG A 1 71  ? 41.204 125.393 15.275   1.00 33.99  ? 73  ARG A CA  1 
ATOM   344  C  C   . ARG A 1 71  ? 41.013 126.642 16.118   1.00 34.90  ? 73  ARG A C   1 
ATOM   345  O  O   . ARG A 1 71  ? 39.939 126.777 16.705   1.00 35.98  ? 73  ARG A O   1 
ATOM   346  C  CB  . ARG A 1 71  ? 42.080 124.418 16.051   1.00 34.57  ? 73  ARG A CB  1 
ATOM   347  C  CG  . ARG A 1 71  ? 42.228 123.090 15.339   1.00 35.22  ? 73  ARG A CG  1 
ATOM   348  C  CD  . ARG A 1 71  ? 43.282 122.195 15.929   1.00 37.23  ? 73  ARG A CD  1 
ATOM   349  N  NE  . ARG A 1 71  ? 43.430 121.071 15.020   1.00 37.71  ? 73  ARG A NE  1 
ATOM   350  C  CZ  . ARG A 1 71  ? 43.758 119.837 15.378   1.00 38.86  ? 73  ARG A CZ  1 
ATOM   351  N  NH1 . ARG A 1 71  ? 43.980 119.533 16.643   1.00 39.57  ? 73  ARG A NH1 1 
ATOM   352  N  NH2 . ARG A 1 71  ? 43.837 118.890 14.466   1.00 39.67  ? 73  ARG A NH2 1 
ATOM   353  N  N   . THR A 1 72  ? 42.013 127.527 16.145   1.00 37.60  ? 74  THR A N   1 
ATOM   354  C  CA  . THR A 1 72  ? 41.953 128.794 16.927   1.00 39.18  ? 74  THR A CA  1 
ATOM   355  C  C   . THR A 1 72  ? 40.811 129.646 16.382   1.00 37.62  ? 74  THR A C   1 
ATOM   356  O  O   . THR A 1 72  ? 39.968 130.098 17.194   1.00 37.82  ? 74  THR A O   1 
ATOM   357  C  CB  . THR A 1 72  ? 43.234 129.626 16.821   1.00 41.26  ? 74  THR A CB  1 
ATOM   358  O  OG1 . THR A 1 72  ? 44.312 128.778 17.214   1.00 44.04  ? 74  THR A OG1 1 
ATOM   359  C  CG2 . THR A 1 72  ? 43.156 130.886 17.659   1.00 41.99  ? 74  THR A CG2 1 
ATOM   360  N  N   . HIS A 1 73  ? 40.814 129.830 15.061   1.00 35.32  ? 75  HIS A N   1 
ATOM   361  C  CA  . HIS A 1 73  ? 39.901 130.740 14.331   1.00 34.75  ? 75  HIS A CA  1 
ATOM   362  C  C   . HIS A 1 73  ? 38.456 130.285 14.560   1.00 31.52  ? 75  HIS A C   1 
ATOM   363  O  O   . HIS A 1 73  ? 37.604 131.134 14.864   1.00 30.58  ? 75  HIS A O   1 
ATOM   364  C  CB  . HIS A 1 73  ? 40.254 130.810 12.823   1.00 35.62  ? 75  HIS A CB  1 
ATOM   365  C  CG  . HIS A 1 73  ? 39.228 131.585 12.079   1.00 35.73  ? 75  HIS A CG  1 
ATOM   366  N  ND1 . HIS A 1 73  ? 39.187 132.956 12.154   1.00 37.49  ? 75  HIS A ND1 1 
ATOM   367  C  CD2 . HIS A 1 73  ? 38.115 131.197 11.417   1.00 36.81  ? 75  HIS A CD2 1 
ATOM   368  C  CE1 . HIS A 1 73  ? 38.128 133.397 11.500   1.00 38.67  ? 75  HIS A CE1 1 
ATOM   369  N  NE2 . HIS A 1 73  ? 37.457 132.332 11.007   1.00 39.90  ? 75  HIS A NE2 1 
ATOM   370  N  N   . PHE A 1 74  ? 38.188 128.988 14.399   1.00 29.35  ? 76  PHE A N   1 
ATOM   371  C  CA  . PHE A 1 74  ? 36.805 128.430 14.449   1.00 27.89  ? 76  PHE A CA  1 
ATOM   372  C  C   . PHE A 1 74  ? 36.360 128.202 15.899   1.00 27.43  ? 76  PHE A C   1 
ATOM   373  O  O   . PHE A 1 74  ? 35.141 128.080 16.131   1.00 26.19  ? 76  PHE A O   1 
ATOM   374  C  CB  . PHE A 1 74  ? 36.699 127.136 13.630   1.00 27.08  ? 76  PHE A CB  1 
ATOM   375  C  CG  . PHE A 1 74  ? 36.864 127.314 12.134   1.00 25.50  ? 76  PHE A CG  1 
ATOM   376  C  CD1 . PHE A 1 74  ? 36.032 128.174 11.424   1.00 25.27  ? 76  PHE A CD1 1 
ATOM   377  C  CD2 . PHE A 1 74  ? 37.836 126.621 11.431   1.00 25.38  ? 76  PHE A CD2 1 
ATOM   378  C  CE1 . PHE A 1 74  ? 36.180 128.347 10.047   1.00 25.35  ? 76  PHE A CE1 1 
ATOM   379  C  CE2 . PHE A 1 74  ? 37.947 126.765 10.045   1.00 25.26  ? 76  PHE A CE2 1 
ATOM   380  C  CZ  . PHE A 1 74  ? 37.127 127.632 9.351    1.00 24.18  ? 76  PHE A CZ  1 
ATOM   381  N  N   . GLY A 1 75  ? 37.311 128.129 16.828   1.00 27.34  ? 77  GLY A N   1 
ATOM   382  C  CA  . GLY A 1 75  ? 37.032 127.977 18.262   1.00 28.19  ? 77  GLY A CA  1 
ATOM   383  C  C   . GLY A 1 75  ? 36.749 126.533 18.601   1.00 27.80  ? 77  GLY A C   1 
ATOM   384  O  O   . GLY A 1 75  ? 37.190 125.615 17.859   1.00 28.05  ? 77  GLY A O   1 
ATOM   385  N  N   . ASN A 1 76  ? 36.087 126.345 19.736   1.00 28.75  ? 78  ASN A N   1 
ATOM   386  C  CA  . ASN A 1 76  ? 35.693 125.021 20.255   1.00 27.58  ? 78  ASN A CA  1 
ATOM   387  C  C   . ASN A 1 76  ? 35.021 124.236 19.126   1.00 26.08  ? 78  ASN A C   1 
ATOM   388  O  O   . ASN A 1 76  ? 34.055 124.796 18.531   1.00 26.17  ? 78  ASN A O   1 
ATOM   389  C  CB  . ASN A 1 76  ? 34.734 125.181 21.424   1.00 28.70  ? 78  ASN A CB  1 
ATOM   390  C  CG  . ASN A 1 76  ? 34.375 123.831 21.966   1.00 27.80  ? 78  ASN A CG  1 
ATOM   391  O  OD1 . ASN A 1 76  ? 33.318 123.294 21.695   1.00 27.88  ? 78  ASN A OD1 1 
ATOM   392  N  ND2 . ASN A 1 76  ? 35.335 123.231 22.604   1.00 30.17  ? 78  ASN A ND2 1 
ATOM   393  N  N   . ALA A 1 77  ? 35.489 123.003 18.890   1.00 24.63  ? 79  ALA A N   1 
ATOM   394  C  CA  . ALA A 1 77  ? 35.053 122.113 17.788   1.00 23.66  ? 79  ALA A CA  1 
ATOM   395  C  C   . ALA A 1 77  ? 33.595 121.749 17.986   1.00 22.46  ? 79  ALA A C   1 
ATOM   396  O  O   . ALA A 1 77  ? 32.848 121.837 17.047   1.00 20.28  ? 79  ALA A O   1 
ATOM   397  C  CB  . ALA A 1 77  ? 35.900 120.865 17.715   1.00 24.31  ? 79  ALA A CB  1 
ATOM   398  N  N   . SER A 1 78  ? 33.230 121.352 19.196   1.00 22.29  ? 80  SER A N   1 
ATOM   399  C  CA  . SER A 1 78  ? 31.868 120.869 19.499   1.00 22.72  ? 80  SER A CA  1 
ATOM   400  C  C   . SER A 1 78  ? 30.887 122.032 19.326   1.00 22.83  ? 80  SER A C   1 
ATOM   401  O  O   . SER A 1 78  ? 29.766 121.790 18.855   1.00 23.20  ? 80  SER A O   1 
ATOM   402  C  CB  . SER A 1 78  ? 31.804 120.276 20.899   1.00 24.33  ? 80  SER A CB  1 
ATOM   403  O  OG  . SER A 1 78  ? 30.663 119.423 21.035   1.00 24.54  ? 80  SER A OG  1 
ATOM   404  N  N   . ASP A 1 79  ? 31.259 123.246 19.728   1.00 24.29  ? 81  ASP A N   1 
ATOM   405  C  CA  . ASP A 1 79  ? 30.392 124.459 19.627   1.00 25.47  ? 81  ASP A CA  1 
ATOM   406  C  C   . ASP A 1 79  ? 30.277 124.888 18.152   1.00 24.26  ? 81  ASP A C   1 
ATOM   407  O  O   . ASP A 1 79  ? 29.208 125.408 17.770   1.00 23.08  ? 81  ASP A O   1 
ATOM   408  C  CB  . ASP A 1 79  ? 30.924 125.651 20.438   1.00 27.95  ? 81  ASP A CB  1 
ATOM   409  C  CG  . ASP A 1 79  ? 30.910 125.523 21.967   1.00 30.75  ? 81  ASP A CG  1 
ATOM   410  O  OD1 . ASP A 1 79  ? 30.128 124.678 22.514   1.00 31.34  ? 81  ASP A OD1 1 
ATOM   411  O  OD2 . ASP A 1 79  ? 31.693 126.280 22.612   1.00 33.34  ? 81  ASP A OD2 1 
ATOM   412  N  N   . LYS A 1 80  ? 31.344 124.728 17.359   1.00 23.21  ? 82  LYS A N   1 
ATOM   413  C  CA  . LYS A 1 80  ? 31.270 125.004 15.891   1.00 22.34  ? 82  LYS A CA  1 
ATOM   414  C  C   . LYS A 1 80  ? 30.279 124.042 15.222   1.00 22.44  ? 82  LYS A C   1 
ATOM   415  O  O   . LYS A 1 80  ? 29.361 124.516 14.459   1.00 22.78  ? 82  LYS A O   1 
ATOM   416  C  CB  . LYS A 1 80  ? 32.628 124.859 15.231   1.00 21.49  ? 82  LYS A CB  1 
ATOM   417  C  CG  . LYS A 1 80  ? 32.622 125.213 13.750   1.00 21.50  ? 82  LYS A CG  1 
ATOM   418  C  CD  . LYS A 1 80  ? 32.163 126.622 13.432   1.00 21.46  ? 82  LYS A CD  1 
ATOM   419  C  CE  . LYS A 1 80  ? 32.234 126.851 11.928   1.00 21.67  ? 82  LYS A CE  1 
ATOM   420  N  NZ  . LYS A 1 80  ? 32.063 128.274 11.527   1.00 22.08  ? 82  LYS A NZ  1 
ATOM   421  N  N   . ALA A 1 81  ? 30.439 122.741 15.494   1.00 22.58  ? 83  ALA A N   1 
ATOM   422  C  CA  . ALA A 1 81  ? 29.484 121.686 15.082   1.00 22.97  ? 83  ALA A CA  1 
ATOM   423  C  C   . ALA A 1 81  ? 28.059 122.099 15.465   1.00 23.92  ? 83  ALA A C   1 
ATOM   424  O  O   . ALA A 1 81  ? 27.175 122.013 14.588   1.00 25.12  ? 83  ALA A O   1 
ATOM   425  C  CB  . ALA A 1 81  ? 29.855 120.359 15.680   1.00 23.10  ? 83  ALA A CB  1 
ATOM   426  N  N   . ALA A 1 82  ? 27.848 122.576 16.692   1.00 24.31  ? 84  ALA A N   1 
ATOM   427  C  CA  . ALA A 1 82  ? 26.515 122.953 17.204   1.00 25.45  ? 84  ALA A CA  1 
ATOM   428  C  C   . ALA A 1 82  ? 25.907 124.088 16.362   1.00 25.95  ? 84  ALA A C   1 
ATOM   429  O  O   . ALA A 1 82  ? 24.730 123.996 16.024   1.00 26.49  ? 84  ALA A O   1 
ATOM   430  C  CB  . ALA A 1 82  ? 26.601 123.318 18.672   1.00 26.80  ? 84  ALA A CB  1 
ATOM   431  N  N   . SER A 1 83  ? 26.653 125.138 16.020   1.00 26.19  ? 85  SER A N   1 
ATOM   432  C  CA  . SER A 1 83  ? 26.126 126.250 15.175   1.00 27.19  ? 85  SER A CA  1 
ATOM   433  C  C   . SER A 1 83  ? 25.701 125.724 13.787   1.00 26.80  ? 85  SER A C   1 
ATOM   434  O  O   . SER A 1 83  ? 24.893 126.387 13.135   1.00 27.91  ? 85  SER A O   1 
ATOM   435  C  CB  . SER A 1 83  ? 27.134 127.356 15.057   1.00 27.16  ? 85  SER A CB  1 
ATOM   436  O  OG  . SER A 1 83  ? 28.215 126.919 14.235   1.00 26.32  ? 85  SER A OG  1 
ATOM   437  N  N   . LEU A 1 84  ? 26.228 124.582 13.325   1.00 27.41  ? 86  LEU A N   1 
ATOM   438  C  CA  . LEU A 1 84  ? 25.930 124.016 11.971   1.00 27.37  ? 86  LEU A CA  1 
ATOM   439  C  C   . LEU A 1 84  ? 24.806 122.982 12.047   1.00 28.81  ? 86  LEU A C   1 
ATOM   440  O  O   . LEU A 1 84  ? 24.325 122.540 10.981   1.00 31.00  ? 86  LEU A O   1 
ATOM   441  C  CB  . LEU A 1 84  ? 27.181 123.337 11.396   1.00 26.89  ? 86  LEU A CB  1 
ATOM   442  C  CG  . LEU A 1 84  ? 28.303 124.248 10.904   1.00 25.51  ? 86  LEU A CG  1 
ATOM   443  C  CD1 . LEU A 1 84  ? 29.520 123.432 10.545   1.00 25.00  ? 86  LEU A CD1 1 
ATOM   444  C  CD2 . LEU A 1 84  ? 27.850 125.050 9.718    1.00 25.58  ? 86  LEU A CD2 1 
ATOM   445  N  N   . SER A 1 85  ? 24.419 122.589 13.252   1.00 29.89  ? 87  SER A N   1 
ATOM   446  C  CA  . SER A 1 85  ? 23.447 121.506 13.520   1.00 30.48  ? 87  SER A CA  1 
ATOM   447  C  C   . SER A 1 85  ? 22.091 121.941 12.983   1.00 31.94  ? 87  SER A C   1 
ATOM   448  O  O   . SER A 1 85  ? 21.709 123.114 13.232   1.00 32.40  ? 87  SER A O   1 
ATOM   449  C  CB  . SER A 1 85  ? 23.363 121.196 14.977   1.00 30.84  ? 87  SER A CB  1 
ATOM   450  O  OG  . SER A 1 85  ? 22.782 119.934 15.117   1.00 31.44  ? 87  SER A OG  1 
ATOM   451  N  N   . GLY A 1 86  ? 21.417 121.031 12.277   1.00 32.98  ? 88  GLY A N   1 
ATOM   452  C  CA  . GLY A 1 86  ? 20.111 121.302 11.669   1.00 36.20  ? 88  GLY A CA  1 
ATOM   453  C  C   . GLY A 1 86  ? 20.175 122.177 10.414   1.00 38.27  ? 88  GLY A C   1 
ATOM   454  O  O   . GLY A 1 86  ? 19.145 122.283 9.776    1.00 41.21  ? 88  GLY A O   1 
ATOM   455  N  N   . LYS A 1 87  ? 21.285 122.838 10.057   1.00 39.46  ? 89  LYS A N   1 
ATOM   456  C  CA  . LYS A 1 87  ? 21.298 123.724 8.851    1.00 40.55  ? 89  LYS A CA  1 
ATOM   457  C  C   . LYS A 1 87  ? 21.081 122.859 7.602    1.00 40.91  ? 89  LYS A C   1 
ATOM   458  O  O   . LYS A 1 87  ? 21.382 121.648 7.650    1.00 38.03  ? 89  LYS A O   1 
ATOM   459  C  CB  . LYS A 1 87  ? 22.608 124.498 8.699    1.00 41.37  ? 89  LYS A CB  1 
ATOM   460  C  CG  . LYS A 1 87  ? 22.941 125.464 9.822    1.00 43.73  ? 89  LYS A CG  1 
ATOM   461  C  CD  . LYS A 1 87  ? 21.984 126.622 9.895    1.00 46.00  ? 89  LYS A CD  1 
ATOM   462  C  CE  . LYS A 1 87  ? 22.146 127.410 11.176   1.00 47.15  ? 89  LYS A CE  1 
ATOM   463  N  NZ  . LYS A 1 87  ? 20.830 127.700 11.800   1.00 49.92  ? 89  LYS A NZ  1 
ATOM   464  N  N   . GLN A 1 88  ? 20.588 123.465 6.515    1.00 42.65  ? 90  GLN A N   1 
ATOM   465  C  CA  . GLN A 1 88  ? 20.322 122.746 5.246    1.00 43.52  ? 90  GLN A CA  1 
ATOM   466  C  C   . GLN A 1 88  ? 21.654 122.281 4.631    1.00 41.02  ? 90  GLN A C   1 
ATOM   467  O  O   . GLN A 1 88  ? 22.701 122.926 4.838    1.00 36.22  ? 90  GLN A O   1 
ATOM   468  C  CB  . GLN A 1 88  ? 19.508 123.619 4.282    1.00 47.20  ? 90  GLN A CB  1 
ATOM   469  C  CG  . GLN A 1 88  ? 18.063 123.868 4.699    1.00 50.52  ? 90  GLN A CG  1 
ATOM   470  C  CD  . GLN A 1 88  ? 17.272 122.585 4.750    1.00 53.00  ? 90  GLN A CD  1 
ATOM   471  O  OE1 . GLN A 1 88  ? 17.584 121.632 4.037    1.00 56.74  ? 90  GLN A OE1 1 
ATOM   472  N  NE2 . GLN A 1 88  ? 16.263 122.542 5.609    1.00 52.99  ? 90  GLN A NE2 1 
ATOM   473  N  N   . ASN A 1 89  ? 21.576 121.177 3.893    1.00 41.32  ? 91  ASN A N   1 
ATOM   474  C  CA  . ASN A 1 89  ? 22.677 120.514 3.140    1.00 42.16  ? 91  ASN A CA  1 
ATOM   475  C  C   . ASN A 1 89  ? 23.314 121.496 2.133    1.00 40.59  ? 91  ASN A C   1 
ATOM   476  O  O   . ASN A 1 89  ? 24.559 121.503 1.985    1.00 37.77  ? 91  ASN A O   1 
ATOM   477  C  CB  . ASN A 1 89  ? 22.141 119.220 2.496    1.00 41.85  ? 91  ASN A CB  1 
ATOM   478  C  CG  . ASN A 1 89  ? 21.932 118.129 3.535    1.00 41.84  ? 91  ASN A CG  1 
ATOM   479  O  OD1 . ASN A 1 89  ? 22.537 118.153 4.606    1.00 39.50  ? 91  ASN A OD1 1 
ATOM   480  N  ND2 . ASN A 1 89  ? 21.093 117.158 3.243    1.00 41.06  ? 91  ASN A ND2 1 
ATOM   481  N  N   . ASP A 1 90  ? 22.506 122.355 1.529    1.00 41.33  ? 92  ASP A N   1 
ATOM   482  C  CA  . ASP A 1 90  ? 22.970 123.340 0.525    1.00 42.21  ? 92  ASP A CA  1 
ATOM   483  C  C   . ASP A 1 90  ? 22.983 124.733 1.170    1.00 39.39  ? 92  ASP A C   1 
ATOM   484  O  O   . ASP A 1 90  ? 22.921 125.724 0.459    1.00 39.81  ? 92  ASP A O   1 
ATOM   485  C  CB  . ASP A 1 90  ? 22.082 123.207 -0.718   1.00 43.90  ? 92  ASP A CB  1 
ATOM   486  C  CG  . ASP A 1 90  ? 20.589 123.445 -0.472   1.00 48.15  ? 92  ASP A CG  1 
ATOM   487  O  OD1 . ASP A 1 90  ? 20.200 123.723 0.702    1.00 51.48  ? 92  ASP A OD1 1 
ATOM   488  O  OD2 . ASP A 1 90  ? 19.802 123.361 -1.457   1.00 50.06  ? 92  ASP A OD2 1 
ATOM   489  N  N   . SER A 1 91  ? 22.985 124.839 2.485    1.00 38.35  ? 93  SER A N   1 
ATOM   490  C  CA  . SER A 1 91  ? 22.817 126.167 3.137    1.00 40.08  ? 93  SER A CA  1 
ATOM   491  C  C   . SER A 1 91  ? 24.089 127.003 2.925    1.00 39.56  ? 93  SER A C   1 
ATOM   492  O  O   . SER A 1 91  ? 25.159 126.393 2.713    1.00 38.15  ? 93  SER A O   1 
ATOM   493  C  CB  . SER A 1 91  ? 22.451 126.062 4.607    1.00 40.19  ? 93  SER A CB  1 
ATOM   494  O  OG  . SER A 1 91  ? 23.507 125.504 5.385    1.00 39.03  ? 93  SER A OG  1 
ATOM   495  N  N   . ALA A 1 92  ? 23.963 128.336 2.993    1.00 39.72  ? 94  ALA A N   1 
ATOM   496  C  CA  . ALA A 1 92  ? 25.073 129.318 2.980    1.00 37.65  ? 94  ALA A CA  1 
ATOM   497  C  C   . ALA A 1 92  ? 26.095 128.977 4.052    1.00 33.49  ? 94  ALA A C   1 
ATOM   498  O  O   . ALA A 1 92  ? 27.260 129.105 3.770    1.00 32.05  ? 94  ALA A O   1 
ATOM   499  C  CB  . ALA A 1 92  ? 24.564 130.719 3.204    1.00 39.27  ? 94  ALA A CB  1 
ATOM   500  N  N   . GLU A 1 93  ? 25.655 128.582 5.241    1.00 34.94  ? 95  GLU A N   1 
ATOM   501  C  CA  . GLU A 1 93  ? 26.546 128.360 6.415    1.00 33.42  ? 95  GLU A CA  1 
ATOM   502  C  C   . GLU A 1 93  ? 27.504 127.198 6.120    1.00 29.04  ? 95  GLU A C   1 
ATOM   503  O  O   . GLU A 1 93  ? 28.684 127.342 6.380    1.00 26.90  ? 95  GLU A O   1 
ATOM   504  C  CB  . GLU A 1 93  ? 25.730 128.131 7.691    1.00 38.37  ? 95  GLU A CB  1 
ATOM   505  C  CG  . GLU A 1 93  ? 24.923 129.349 8.157    1.00 43.11  ? 95  GLU A CG  1 
ATOM   506  C  CD  . GLU A 1 93  ? 23.507 129.488 7.583    1.00 51.32  ? 95  GLU A CD  1 
ATOM   507  O  OE1 . GLU A 1 93  ? 23.160 128.826 6.535    1.00 56.59  ? 95  GLU A OE1 1 
ATOM   508  O  OE2 . GLU A 1 93  ? 22.731 130.270 8.161    1.00 56.84  ? 95  GLU A OE2 1 
ATOM   509  N  N   . VAL A 1 94  ? 27.038 126.116 5.518    1.00 27.50  ? 96  VAL A N   1 
ATOM   510  C  CA  . VAL A 1 94  ? 27.883 124.921 5.219    1.00 26.97  ? 96  VAL A CA  1 
ATOM   511  C  C   . VAL A 1 94  ? 28.862 125.252 4.097    1.00 25.84  ? 96  VAL A C   1 
ATOM   512  O  O   . VAL A 1 94  ? 30.023 124.868 4.177    1.00 24.23  ? 96  VAL A O   1 
ATOM   513  C  CB  . VAL A 1 94  ? 27.019 123.714 4.826    1.00 29.15  ? 96  VAL A CB  1 
ATOM   514  C  CG1 . VAL A 1 94  ? 27.829 122.440 4.631    1.00 28.98  ? 96  VAL A CG1 1 
ATOM   515  C  CG2 . VAL A 1 94  ? 25.969 123.477 5.882    1.00 31.16  ? 96  VAL A CG2 1 
ATOM   516  N  N   . LYS A 1 95  ? 28.376 125.899 3.058    1.00 25.58  ? 97  LYS A N   1 
ATOM   517  C  CA  . LYS A 1 95  ? 29.215 126.424 1.962    1.00 25.93  ? 97  LYS A CA  1 
ATOM   518  C  C   . LYS A 1 95  ? 30.379 127.239 2.525    1.00 24.34  ? 97  LYS A C   1 
ATOM   519  O  O   . LYS A 1 95  ? 31.512 126.973 2.070    1.00 23.66  ? 97  LYS A O   1 
ATOM   520  C  CB  . LYS A 1 95  ? 28.406 127.350 1.049    1.00 28.82  ? 97  LYS A CB  1 
ATOM   521  C  CG  . LYS A 1 95  ? 27.932 126.739 -0.251   1.00 30.88  ? 97  LYS A CG  1 
ATOM   522  C  CD  . LYS A 1 95  ? 26.526 126.191 -0.235   1.00 33.80  ? 97  LYS A CD  1 
ATOM   523  C  CE  . LYS A 1 95  ? 25.980 126.022 -1.650   1.00 35.62  ? 97  LYS A CE  1 
ATOM   524  N  NZ  . LYS A 1 95  ? 25.080 124.843 -1.806   1.00 38.34  ? 97  LYS A NZ  1 
ATOM   525  N  N   . ALA A 1 96  ? 30.104 128.208 3.421    1.00 23.02  ? 98  ALA A N   1 
ATOM   526  C  CA  . ALA A 1 96  ? 31.082 129.206 3.921    1.00 22.32  ? 98  ALA A CA  1 
ATOM   527  C  C   . ALA A 1 96  ? 32.105 128.476 4.786    1.00 21.97  ? 98  ALA A C   1 
ATOM   528  O  O   . ALA A 1 96  ? 33.289 128.771 4.673    1.00 22.35  ? 98  ALA A O   1 
ATOM   529  C  CB  . ALA A 1 96  ? 30.393 130.319 4.686    1.00 22.83  ? 98  ALA A CB  1 
ATOM   530  N  N   . PHE A 1 97  ? 31.655 127.566 5.649    1.00 21.57  ? 99  PHE A N   1 
ATOM   531  C  CA  . PHE A 1 97  ? 32.551 126.669 6.424    1.00 21.10  ? 99  PHE A CA  1 
ATOM   532  C  C   . PHE A 1 97  ? 33.477 125.883 5.482    1.00 20.54  ? 99  PHE A C   1 
ATOM   533  O  O   . PHE A 1 97  ? 34.681 125.921 5.689    1.00 20.29  ? 99  PHE A O   1 
ATOM   534  C  CB  . PHE A 1 97  ? 31.733 125.732 7.312    1.00 20.92  ? 99  PHE A CB  1 
ATOM   535  C  CG  . PHE A 1 97  ? 32.542 124.951 8.314    1.00 21.17  ? 99  PHE A CG  1 
ATOM   536  C  CD1 . PHE A 1 97  ? 33.540 125.555 9.057    1.00 21.67  ? 99  PHE A CD1 1 
ATOM   537  C  CD2 . PHE A 1 97  ? 32.267 123.620 8.577    1.00 21.24  ? 99  PHE A CD2 1 
ATOM   538  C  CE1 . PHE A 1 97  ? 34.258 124.826 10.003   1.00 21.85  ? 99  PHE A CE1 1 
ATOM   539  C  CE2 . PHE A 1 97  ? 32.970 122.916 9.547    1.00 21.94  ? 99  PHE A CE2 1 
ATOM   540  C  CZ  . PHE A 1 97  ? 33.986 123.503 10.241   1.00 21.11  ? 99  PHE A CZ  1 
ATOM   541  N  N   . ALA A 1 98  ? 32.938 125.186 4.476    1.00 20.76  ? 100 ALA A N   1 
ATOM   542  C  CA  . ALA A 1 98  ? 33.736 124.407 3.492    1.00 21.06  ? 100 ALA A CA  1 
ATOM   543  C  C   . ALA A 1 98  ? 34.738 125.351 2.828    1.00 21.64  ? 100 ALA A C   1 
ATOM   544  O  O   . ALA A 1 98  ? 35.875 124.912 2.663    1.00 22.34  ? 100 ALA A O   1 
ATOM   545  C  CB  . ALA A 1 98  ? 32.874 123.736 2.433    1.00 21.01  ? 100 ALA A CB  1 
ATOM   546  N  N   . GLN A 1 99  ? 34.327 126.574 2.448    1.00 21.72  ? 101 GLN A N   1 
ATOM   547  C  CA  . GLN A 1 99  ? 35.235 127.548 1.801    1.00 22.70  ? 101 GLN A CA  1 
ATOM   548  C  C   . GLN A 1 99  ? 36.287 127.981 2.805    1.00 22.38  ? 101 GLN A C   1 
ATOM   549  O  O   . GLN A 1 99  ? 37.445 127.912 2.449    1.00 21.87  ? 101 GLN A O   1 
ATOM   550  C  CB  . GLN A 1 99  ? 34.530 128.761 1.205    1.00 24.48  ? 101 GLN A CB  1 
ATOM   551  C  CG  . GLN A 1 99  ? 33.736 128.439 -0.058   1.00 26.19  ? 101 GLN A CG  1 
ATOM   552  C  CD  . GLN A 1 99  ? 34.505 127.855 -1.231   1.00 27.86  ? 101 GLN A CD  1 
ATOM   553  O  OE1 . GLN A 1 99  ? 35.552 128.376 -1.641   1.00 29.68  ? 101 GLN A OE1 1 
ATOM   554  N  NE2 . GLN A 1 99  ? 33.987 126.762 -1.792   1.00 26.14  ? 101 GLN A NE2 1 
ATOM   555  N  N   . GLU A 1 100 ? 35.924 128.399 4.018    1.00 23.43  ? 102 GLU A N   1 
ATOM   556  C  CA  . GLU A 1 100 ? 36.913 129.011 4.931    1.00 24.45  ? 102 GLU A CA  1 
ATOM   557  C  C   . GLU A 1 100 ? 37.809 127.908 5.501    1.00 23.52  ? 102 GLU A C   1 
ATOM   558  O  O   . GLU A 1 100 ? 38.950 128.201 5.838    1.00 23.91  ? 102 GLU A O   1 
ATOM   559  C  CB  . GLU A 1 100 ? 36.256 129.858 6.013    1.00 27.19  ? 102 GLU A CB  1 
ATOM   560  C  CG  . GLU A 1 100 ? 37.271 130.705 6.786    1.00 30.28  ? 102 GLU A CG  1 
ATOM   561  C  CD  . GLU A 1 100 ? 36.688 131.470 7.943    1.00 33.85  ? 102 GLU A CD  1 
ATOM   562  O  OE1 . GLU A 1 100 ? 35.627 131.019 8.370    1.00 35.39  ? 102 GLU A OE1 1 
ATOM   563  O  OE2 . GLU A 1 100 ? 37.320 132.462 8.467    1.00 40.25  ? 102 GLU A OE2 1 
ATOM   564  N  N   . LEU A 1 101 ? 37.338 126.667 5.554    1.00 22.31  ? 103 LEU A N   1 
ATOM   565  C  CA  . LEU A 1 101 ? 38.164 125.515 5.990    1.00 22.49  ? 103 LEU A CA  1 
ATOM   566  C  C   . LEU A 1 101 ? 39.392 125.404 5.108    1.00 24.12  ? 103 LEU A C   1 
ATOM   567  O  O   . LEU A 1 101 ? 40.453 125.094 5.600    1.00 25.13  ? 103 LEU A O   1 
ATOM   568  C  CB  . LEU A 1 101 ? 37.348 124.223 5.905    1.00 21.84  ? 103 LEU A CB  1 
ATOM   569  C  CG  . LEU A 1 101 ? 36.650 123.788 7.202    1.00 20.91  ? 103 LEU A CG  1 
ATOM   570  C  CD1 . LEU A 1 101 ? 35.806 122.542 6.995    1.00 20.18  ? 103 LEU A CD1 1 
ATOM   571  C  CD2 . LEU A 1 101 ? 37.671 123.532 8.288    1.00 21.89  ? 103 LEU A CD2 1 
ATOM   572  N  N   . ASN A 1 102 ? 39.224 125.657 3.815    1.00 25.82  ? 104 ASN A N   1 
ATOM   573  C  CA  . ASN A 1 102 ? 40.210 125.281 2.781    1.00 27.45  ? 104 ASN A CA  1 
ATOM   574  C  C   . ASN A 1 102 ? 41.566 125.920 3.106    1.00 30.63  ? 104 ASN A C   1 
ATOM   575  O  O   . ASN A 1 102 ? 42.598 125.254 2.897    1.00 31.25  ? 104 ASN A O   1 
ATOM   576  C  CB  . ASN A 1 102 ? 39.719 125.677 1.396    1.00 26.27  ? 104 ASN A CB  1 
ATOM   577  C  CG  . ASN A 1 102 ? 40.668 125.166 0.356    1.00 26.77  ? 104 ASN A CG  1 
ATOM   578  O  OD1 . ASN A 1 102 ? 40.982 123.977 0.336    1.00 26.76  ? 104 ASN A OD1 1 
ATOM   579  N  ND2 . ASN A 1 102 ? 41.153 126.062 -0.475   1.00 27.02  ? 104 ASN A ND2 1 
ATOM   580  N  N   . GLN A 1 103 ? 41.585 127.148 3.629    1.00 33.15  ? 105 GLN A N   1 
ATOM   581  C  CA  . GLN A 1 103 ? 42.871 127.838 3.921    1.00 35.68  ? 105 GLN A CA  1 
ATOM   582  C  C   . GLN A 1 103 ? 43.517 127.215 5.174    1.00 34.01  ? 105 GLN A C   1 
ATOM   583  O  O   . GLN A 1 103 ? 44.667 127.513 5.454    1.00 34.99  ? 105 GLN A O   1 
ATOM   584  C  CB  . GLN A 1 103 ? 42.643 129.351 4.022    1.00 38.33  ? 105 GLN A CB  1 
ATOM   585  C  CG  . GLN A 1 103 ? 42.038 129.807 5.344    1.00 39.66  ? 105 GLN A CG  1 
ATOM   586  C  CD  . GLN A 1 103 ? 41.153 131.027 5.185    1.00 41.97  ? 105 GLN A CD  1 
ATOM   587  O  OE1 . GLN A 1 103 ? 40.404 131.154 4.217    1.00 46.02  ? 105 GLN A OE1 1 
ATOM   588  N  NE2 . GLN A 1 103 ? 41.207 131.937 6.148    1.00 43.02  ? 105 GLN A NE2 1 
ATOM   589  N  N   . TYR A 1 104 ? 42.848 126.316 5.878    1.00 31.69  ? 106 TYR A N   1 
ATOM   590  C  CA  . TYR A 1 104 ? 43.385 125.768 7.154    1.00 32.06  ? 106 TYR A CA  1 
ATOM   591  C  C   . TYR A 1 104 ? 43.567 124.257 7.049    1.00 31.45  ? 106 TYR A C   1 
ATOM   592  O  O   . TYR A 1 104 ? 43.717 123.628 8.051    1.00 31.36  ? 106 TYR A O   1 
ATOM   593  C  CB  . TYR A 1 104 ? 42.463 126.134 8.321    1.00 30.82  ? 106 TYR A CB  1 
ATOM   594  C  CG  . TYR A 1 104 ? 42.342 127.608 8.627    1.00 30.51  ? 106 TYR A CG  1 
ATOM   595  C  CD1 . TYR A 1 104 ? 43.444 128.347 9.016    1.00 31.49  ? 106 TYR A CD1 1 
ATOM   596  C  CD2 . TYR A 1 104 ? 41.118 128.248 8.603    1.00 29.06  ? 106 TYR A CD2 1 
ATOM   597  C  CE1 . TYR A 1 104 ? 43.341 129.686 9.345    1.00 31.65  ? 106 TYR A CE1 1 
ATOM   598  C  CE2 . TYR A 1 104 ? 41.005 129.597 8.887    1.00 29.63  ? 106 TYR A CE2 1 
ATOM   599  C  CZ  . TYR A 1 104 ? 42.122 130.314 9.264    1.00 30.92  ? 106 TYR A CZ  1 
ATOM   600  O  OH  . TYR A 1 104 ? 42.045 131.636 9.568    1.00 33.78  ? 106 TYR A OH  1 
ATOM   601  N  N   . LEU A 1 105 ? 43.556 123.679 5.856    1.00 32.47  ? 107 LEU A N   1 
ATOM   602  C  CA  . LEU A 1 105 ? 43.680 122.205 5.739    1.00 33.50  ? 107 LEU A CA  1 
ATOM   603  C  C   . LEU A 1 105 ? 45.118 121.796 6.030    1.00 37.11  ? 107 LEU A C   1 
ATOM   604  O  O   . LEU A 1 105 ? 46.007 122.607 5.837    1.00 39.53  ? 107 LEU A O   1 
ATOM   605  C  CB  . LEU A 1 105 ? 43.237 121.735 4.358    1.00 31.86  ? 107 LEU A CB  1 
ATOM   606  C  CG  . LEU A 1 105 ? 41.756 121.941 4.052    1.00 30.32  ? 107 LEU A CG  1 
ATOM   607  C  CD1 . LEU A 1 105 ? 41.421 121.421 2.660    1.00 29.81  ? 107 LEU A CD1 1 
ATOM   608  C  CD2 . LEU A 1 105 ? 40.870 121.268 5.083    1.00 29.77  ? 107 LEU A CD2 1 
ATOM   609  N  N   . SER A 1 106 ? 45.297 120.579 6.520    1.00 40.59  ? 108 SER A N   1 
ATOM   610  C  CA  . SER A 1 106 ? 46.598 119.923 6.782    1.00 44.84  ? 108 SER A CA  1 
ATOM   611  C  C   . SER A 1 106 ? 46.597 118.529 6.170    1.00 46.98  ? 108 SER A C   1 
ATOM   612  O  O   . SER A 1 106 ? 45.586 117.814 6.273    1.00 47.00  ? 108 SER A O   1 
ATOM   613  C  CB  . SER A 1 106 ? 46.853 119.829 8.258    1.00 48.16  ? 108 SER A CB  1 
ATOM   614  O  OG  . SER A 1 106 ? 47.728 118.739 8.536    1.00 51.83  ? 108 SER A OG  1 
ATOM   615  N  N   . SER A 1 107 ? 47.727 118.111 5.621    1.00 51.69  ? 109 SER A N   1 
ATOM   616  C  CA  . SER A 1 107 ? 47.902 116.740 5.069    1.00 55.19  ? 109 SER A CA  1 
ATOM   617  C  C   . SER A 1 107 ? 48.232 115.740 6.192    1.00 55.84  ? 109 SER A C   1 
ATOM   618  O  O   . SER A 1 107 ? 48.515 114.570 5.889    1.00 56.61  ? 109 SER A O   1 
ATOM   619  C  CB  . SER A 1 107 ? 48.941 116.769 4.012    1.00 58.90  ? 109 SER A CB  1 
ATOM   620  O  OG  . SER A 1 107 ? 49.903 117.753 4.359    1.00 64.29  ? 109 SER A OG  1 
ATOM   621  N  N   . ALA A 1 108 ? 48.156 116.173 7.451    1.00 54.78  ? 110 ALA A N   1 
ATOM   622  C  CA  . ALA A 1 108 ? 48.297 115.301 8.641    1.00 55.56  ? 110 ALA A CA  1 
ATOM   623  C  C   . ALA A 1 108 ? 47.072 114.373 8.757    1.00 53.96  ? 110 ALA A C   1 
ATOM   624  O  O   . ALA A 1 108 ? 47.194 113.232 9.266    1.00 53.15  ? 110 ALA A O   1 
ATOM   625  C  CB  . ALA A 1 108 ? 48.473 116.165 9.871    1.00 55.05  ? 110 ALA A CB  1 
ATOM   626  N  N   . GLY A 1 109 ? 45.906 114.861 8.326    1.00 53.06  ? 111 GLY A N   1 
ATOM   627  C  CA  . GLY A 1 109 ? 44.640 114.097 8.310    1.00 50.21  ? 111 GLY A CA  1 
ATOM   628  C  C   . GLY A 1 109 ? 44.039 114.060 6.915    1.00 46.69  ? 111 GLY A C   1 
ATOM   629  O  O   . GLY A 1 109 ? 42.856 114.395 6.812    1.00 42.77  ? 111 GLY A O   1 
ATOM   630  N  N   . VAL A 1 110 ? 44.822 113.704 5.877    1.00 45.72  ? 112 VAL A N   1 
ATOM   631  C  CA  . VAL A 1 110 ? 44.325 113.620 4.468    1.00 43.19  ? 112 VAL A CA  1 
ATOM   632  C  C   . VAL A 1 110 ? 44.382 112.173 3.984    1.00 43.57  ? 112 VAL A C   1 
ATOM   633  O  O   . VAL A 1 110 ? 45.407 111.514 4.200    1.00 43.19  ? 112 VAL A O   1 
ATOM   634  C  CB  . VAL A 1 110 ? 45.080 114.547 3.501    1.00 42.44  ? 112 VAL A CB  1 
ATOM   635  C  CG1 . VAL A 1 110 ? 46.489 114.052 3.190    1.00 43.73  ? 112 VAL A CG1 1 
ATOM   636  C  CG2 . VAL A 1 110 ? 44.265 114.754 2.236    1.00 39.53  ? 112 VAL A CG2 1 
ATOM   637  N  N   . THR A 1 111 ? 43.283 111.729 3.370    1.00 42.41  ? 113 THR A N   1 
ATOM   638  C  CA  . THR A 1 111 ? 43.169 110.499 2.541    1.00 43.11  ? 113 THR A CA  1 
ATOM   639  C  C   . THR A 1 111 ? 43.025 110.982 1.085    1.00 42.79  ? 113 THR A C   1 
ATOM   640  O  O   . THR A 1 111 ? 42.218 111.901 0.846    1.00 41.52  ? 113 THR A O   1 
ATOM   641  C  CB  . THR A 1 111 ? 42.012 109.624 3.058    1.00 42.13  ? 113 THR A CB  1 
ATOM   642  O  OG1 . THR A 1 111 ? 42.360 109.261 4.395    1.00 43.42  ? 113 THR A OG1 1 
ATOM   643  C  CG2 . THR A 1 111 ? 41.728 108.381 2.241    1.00 43.04  ? 113 THR A CG2 1 
ATOM   644  N  N   . THR A 1 112 ? 43.777 110.416 0.147    1.00 43.54  ? 114 THR A N   1 
ATOM   645  C  CA  . THR A 1 112 ? 43.737 110.821 -1.288   1.00 42.94  ? 114 THR A CA  1 
ATOM   646  C  C   . THR A 1 112 ? 43.374 109.606 -2.121   1.00 42.74  ? 114 THR A C   1 
ATOM   647  O  O   . THR A 1 112 ? 43.981 108.562 -1.947   1.00 43.61  ? 114 THR A O   1 
ATOM   648  C  CB  . THR A 1 112 ? 45.067 111.421 -1.749   1.00 44.49  ? 114 THR A CB  1 
ATOM   649  O  OG1 . THR A 1 112 ? 45.414 112.455 -0.833   1.00 46.11  ? 114 THR A OG1 1 
ATOM   650  C  CG2 . THR A 1 112 ? 45.017 111.999 -3.139   1.00 43.55  ? 114 THR A CG2 1 
ATOM   651  N  N   . VAL A 1 113 ? 42.418 109.753 -3.008   1.00 42.73  ? 115 VAL A N   1 
ATOM   652  C  CA  . VAL A 1 113 ? 41.878 108.592 -3.755   1.00 45.69  ? 115 VAL A CA  1 
ATOM   653  C  C   . VAL A 1 113 ? 41.825 108.953 -5.240   1.00 47.73  ? 115 VAL A C   1 
ATOM   654  O  O   . VAL A 1 113 ? 41.416 110.082 -5.542   1.00 45.91  ? 115 VAL A O   1 
ATOM   655  C  CB  . VAL A 1 113 ? 40.495 108.208 -3.221   1.00 45.08  ? 115 VAL A CB  1 
ATOM   656  C  CG1 . VAL A 1 113 ? 39.522 109.358 -3.370   1.00 43.47  ? 115 VAL A CG1 1 
ATOM   657  C  CG2 . VAL A 1 113 ? 39.959 106.978 -3.921   1.00 46.39  ? 115 VAL A CG2 1 
ATOM   658  N  N   . GLN A 1 114 ? 42.254 108.023 -6.106   1.00 52.34  ? 116 GLN A N   1 
ATOM   659  C  CA  . GLN A 1 114 ? 42.145 108.104 -7.579   1.00 52.29  ? 116 GLN A CA  1 
ATOM   660  C  C   . GLN A 1 114 ? 40.704 107.816 -7.982   1.00 51.44  ? 116 GLN A C   1 
ATOM   661  O  O   . GLN A 1 114 ? 40.171 106.795 -7.528   1.00 50.03  ? 116 GLN A O   1 
ATOM   662  C  CB  . GLN A 1 114 ? 43.035 107.061 -8.242   1.00 58.26  ? 116 GLN A CB  1 
ATOM   663  C  CG  . GLN A 1 114 ? 44.486 107.488 -8.390   1.00 61.19  ? 116 GLN A CG  1 
ATOM   664  C  CD  . GLN A 1 114 ? 45.129 106.696 -9.501   1.00 66.30  ? 116 GLN A CD  1 
ATOM   665  O  OE1 . GLN A 1 114 ? 45.014 105.472 -9.550   1.00 71.53  ? 116 GLN A OE1 1 
ATOM   666  N  NE2 . GLN A 1 114 ? 45.771 107.387 -10.431  1.00 63.32  ? 116 GLN A NE2 1 
ATOM   667  N  N   . SER A 1 115 ? 40.129 108.662 -8.839   1.00 50.90  ? 117 SER A N   1 
ATOM   668  C  CA  . SER A 1 115 ? 38.704 108.592 -9.241   1.00 52.42  ? 117 SER A CA  1 
ATOM   669  C  C   . SER A 1 115 ? 38.489 107.446 -10.234  1.00 55.15  ? 117 SER A C   1 
ATOM   670  O  O   . SER A 1 115 ? 39.281 107.309 -11.178  1.00 55.24  ? 117 SER A O   1 
ATOM   671  C  CB  . SER A 1 115 ? 38.236 109.895 -9.808   1.00 51.96  ? 117 SER A CB  1 
ATOM   672  O  OG  . SER A 1 115 ? 38.901 110.199 -11.024  1.00 51.93  ? 117 SER A OG  1 
ATOM   673  N  N   . GLN A 1 116 ? 37.444 106.653 -10.009  1.00 57.10  ? 118 GLN A N   1 
ATOM   674  C  CA  . GLN A 1 116 ? 37.010 105.573 -10.932  1.00 59.71  ? 118 GLN A CA  1 
ATOM   675  C  C   . GLN A 1 116 ? 36.016 106.168 -11.913  1.00 57.03  ? 118 GLN A C   1 
ATOM   676  O  O   . GLN A 1 116 ? 35.447 107.223 -11.609  1.00 53.45  ? 118 GLN A O   1 
ATOM   677  C  CB  . GLN A 1 116 ? 36.312 104.430 -10.190  1.00 63.68  ? 118 GLN A CB  1 
ATOM   678  C  CG  . GLN A 1 116 ? 37.089 103.881 -9.006   1.00 66.40  ? 118 GLN A CG  1 
ATOM   679  C  CD  . GLN A 1 116 ? 38.389 103.273 -9.461   1.00 69.49  ? 118 GLN A CD  1 
ATOM   680  O  OE1 . GLN A 1 116 ? 38.401 102.329 -10.243  1.00 71.90  ? 118 GLN A OE1 1 
ATOM   681  N  NE2 . GLN A 1 116 ? 39.496 103.815 -8.974   1.00 71.63  ? 118 GLN A NE2 1 
ATOM   682  N  N   . GLN A 1 117 ? 35.764 105.473 -13.015  1.00 58.95  ? 119 GLN A N   1 
ATOM   683  C  CA  . GLN A 1 117 ? 34.648 105.835 -13.922  1.00 59.57  ? 119 GLN A CA  1 
ATOM   684  C  C   . GLN A 1 117 ? 33.312 105.509 -13.236  1.00 57.78  ? 119 GLN A C   1 
ATOM   685  O  O   . GLN A 1 117 ? 33.055 104.340 -13.002  1.00 62.42  ? 119 GLN A O   1 
ATOM   686  C  CB  . GLN A 1 117 ? 34.818 105.133 -15.274  1.00 61.93  ? 119 GLN A CB  1 
ATOM   687  C  CG  . GLN A 1 117 ? 33.827 105.616 -16.319  1.00 62.07  ? 119 GLN A CG  1 
ATOM   688  C  CD  . GLN A 1 117 ? 33.708 107.126 -16.374  1.00 61.23  ? 119 GLN A CD  1 
ATOM   689  O  OE1 . GLN A 1 117 ? 34.685 107.861 -16.582  1.00 60.28  ? 119 GLN A OE1 1 
ATOM   690  N  NE2 . GLN A 1 117 ? 32.487 107.607 -16.186  1.00 58.34  ? 119 GLN A NE2 1 
ATOM   691  N  N   . GLY A 1 118 ? 32.492 106.512 -12.934  1.00 54.85  ? 120 GLY A N   1 
ATOM   692  C  CA  . GLY A 1 118 ? 31.111 106.329 -12.446  1.00 56.46  ? 120 GLY A CA  1 
ATOM   693  C  C   . GLY A 1 118 ? 30.972 106.604 -10.951  1.00 56.01  ? 120 GLY A C   1 
ATOM   694  O  O   . GLY A 1 118 ? 30.251 107.536 -10.596  1.00 54.58  ? 120 GLY A O   1 
ATOM   695  N  N   . THR A 1 119 ? 31.629 105.811 -10.100  1.00 57.29  ? 121 THR A N   1 
ATOM   696  C  CA  . THR A 1 119 ? 31.538 105.905 -8.623   1.00 56.58  ? 121 THR A CA  1 
ATOM   697  C  C   . THR A 1 119 ? 32.902 105.620 -7.992   1.00 56.02  ? 121 THR A C   1 
ATOM   698  O  O   . THR A 1 119 ? 33.489 104.575 -8.273   1.00 57.00  ? 121 THR A O   1 
ATOM   699  C  CB  . THR A 1 119 ? 30.438 105.005 -8.052   1.00 59.09  ? 121 THR A CB  1 
ATOM   700  O  OG1 . THR A 1 119 ? 29.194 105.589 -8.438   1.00 59.57  ? 121 THR A OG1 1 
ATOM   701  C  CG2 . THR A 1 119 ? 30.480 104.904 -6.543   1.00 59.57  ? 121 THR A CG2 1 
ATOM   702  N  N   . THR A 1 120 ? 33.353 106.544 -7.146   1.00 54.16  ? 122 THR A N   1 
ATOM   703  C  CA  . THR A 1 120 ? 34.657 106.489 -6.448   1.00 54.41  ? 122 THR A CA  1 
ATOM   704  C  C   . THR A 1 120 ? 34.390 106.068 -4.999   1.00 53.01  ? 122 THR A C   1 
ATOM   705  O  O   . THR A 1 120 ? 33.727 106.808 -4.272   1.00 52.64  ? 122 THR A O   1 
ATOM   706  C  CB  . THR A 1 120 ? 35.397 107.826 -6.593   1.00 52.52  ? 122 THR A CB  1 
ATOM   707  O  OG1 . THR A 1 120 ? 35.349 108.212 -7.970   1.00 53.33  ? 122 THR A OG1 1 
ATOM   708  C  CG2 . THR A 1 120 ? 36.836 107.766 -6.132   1.00 51.98  ? 122 THR A CG2 1 
ATOM   709  N  N   . THR A 1 121 ? 34.913 104.919 -4.597   1.00 53.62  ? 123 THR A N   1 
ATOM   710  C  CA  . THR A 1 121 ? 34.749 104.367 -3.235   1.00 54.84  ? 123 THR A CA  1 
ATOM   711  C  C   . THR A 1 121 ? 35.856 104.907 -2.335   1.00 53.92  ? 123 THR A C   1 
ATOM   712  O  O   . THR A 1 121 ? 37.008 104.838 -2.728   1.00 54.56  ? 123 THR A O   1 
ATOM   713  C  CB  . THR A 1 121 ? 34.701 102.840 -3.306   1.00 58.42  ? 123 THR A CB  1 
ATOM   714  O  OG1 . THR A 1 121 ? 33.562 102.540 -4.111   1.00 58.41  ? 123 THR A OG1 1 
ATOM   715  C  CG2 . THR A 1 121 ? 34.528 102.174 -1.956   1.00 61.73  ? 123 THR A CG2 1 
ATOM   716  N  N   . ILE A 1 122 ? 35.506 105.417 -1.159   1.00 54.27  ? 124 ILE A N   1 
ATOM   717  C  CA  . ILE A 1 122 ? 36.487 106.007 -0.201   1.00 54.45  ? 124 ILE A CA  1 
ATOM   718  C  C   . ILE A 1 122 ? 36.360 105.272 1.136    1.00 56.70  ? 124 ILE A C   1 
ATOM   719  O  O   . ILE A 1 122 ? 35.471 105.630 1.924    1.00 56.38  ? 124 ILE A O   1 
ATOM   720  C  CB  . ILE A 1 122 ? 36.297 107.532 -0.061   1.00 51.10  ? 124 ILE A CB  1 
ATOM   721  C  CG1 . ILE A 1 122 ? 36.345 108.242 -1.422   1.00 49.05  ? 124 ILE A CG1 1 
ATOM   722  C  CG2 . ILE A 1 122 ? 37.323 108.083 0.923    1.00 50.78  ? 124 ILE A CG2 1 
ATOM   723  C  CD1 . ILE A 1 122 ? 35.760 109.650 -1.444   1.00 46.06  ? 124 ILE A CD1 1 
ATOM   724  N  N   . SER A 1 123 ? 37.237 104.290 1.367    1.00 61.55  ? 125 SER A N   1 
ATOM   725  C  CA  . SER A 1 123 ? 37.171 103.297 2.480    1.00 62.70  ? 125 SER A CA  1 
ATOM   726  C  C   . SER A 1 123 ? 37.954 103.766 3.701    1.00 61.09  ? 125 SER A C   1 
ATOM   727  O  O   . SER A 1 123 ? 38.749 104.716 3.584    1.00 60.94  ? 125 SER A O   1 
ATOM   728  C  CB  . SER A 1 123 ? 37.682 101.950 2.050    1.00 65.21  ? 125 SER A CB  1 
ATOM   729  O  OG  . SER A 1 123 ? 36.783 101.380 1.116    1.00 69.70  ? 125 SER A OG  1 
ATOM   730  N  N   . GLY A 1 124 ? 37.735 103.064 4.816    1.00 60.02  ? 126 GLY A N   1 
ATOM   731  C  CA  . GLY A 1 124 ? 38.526 103.151 6.052    1.00 59.04  ? 126 GLY A CA  1 
ATOM   732  C  C   . GLY A 1 124 ? 38.351 104.497 6.719    1.00 55.82  ? 126 GLY A C   1 
ATOM   733  O  O   . GLY A 1 124 ? 39.268 104.902 7.425    1.00 57.60  ? 126 GLY A O   1 
ATOM   734  N  N   . LEU A 1 125 ? 37.224 105.180 6.512    1.00 52.60  ? 127 LEU A N   1 
ATOM   735  C  CA  . LEU A 1 125 ? 36.980 106.503 7.147    1.00 50.20  ? 127 LEU A CA  1 
ATOM   736  C  C   . LEU A 1 125 ? 36.623 106.309 8.626    1.00 50.22  ? 127 LEU A C   1 
ATOM   737  O  O   . LEU A 1 125 ? 35.532 105.799 8.906    1.00 47.93  ? 127 LEU A O   1 
ATOM   738  C  CB  . LEU A 1 125 ? 35.839 107.237 6.437    1.00 48.11  ? 127 LEU A CB  1 
ATOM   739  C  CG  . LEU A 1 125 ? 36.195 107.822 5.076    1.00 49.41  ? 127 LEU A CG  1 
ATOM   740  C  CD1 . LEU A 1 125 ? 35.086 108.739 4.586    1.00 48.43  ? 127 LEU A CD1 1 
ATOM   741  C  CD2 . LEU A 1 125 ? 37.527 108.564 5.131    1.00 48.70  ? 127 LEU A CD2 1 
ATOM   742  N  N   . LYS A 1 126 ? 37.502 106.749 9.524    1.00 51.17  ? 128 LYS A N   1 
ATOM   743  C  CA  . LYS A 1 126 ? 37.204 106.991 10.956   1.00 52.23  ? 128 LYS A CA  1 
ATOM   744  C  C   . LYS A 1 126 ? 35.964 107.880 11.070   1.00 50.79  ? 128 LYS A C   1 
ATOM   745  O  O   . LYS A 1 126 ? 35.727 108.770 10.251   1.00 49.75  ? 128 LYS A O   1 
ATOM   746  C  CB  . LYS A 1 126 ? 38.396 107.671 11.628   1.00 55.01  ? 128 LYS A CB  1 
ATOM   747  C  CG  . LYS A 1 126 ? 39.758 107.205 11.112   1.00 61.36  ? 128 LYS A CG  1 
ATOM   748  C  CD  . LYS A 1 126 ? 40.948 107.375 12.054   1.00 66.80  ? 128 LYS A CD  1 
ATOM   749  C  CE  . LYS A 1 126 ? 41.905 106.187 11.966   1.00 72.20  ? 128 LYS A CE  1 
ATOM   750  N  NZ  . LYS A 1 126 ? 42.933 106.187 13.037   1.00 76.52  ? 128 LYS A NZ  1 
ATOM   751  N  N   . PRO A 1 127 ? 35.142 107.725 12.126   1.00 47.59  ? 129 PRO A N   1 
ATOM   752  C  CA  . PRO A 1 127 ? 33.869 108.442 12.178   1.00 43.90  ? 129 PRO A CA  1 
ATOM   753  C  C   . PRO A 1 127 ? 34.131 109.952 12.280   1.00 38.60  ? 129 PRO A C   1 
ATOM   754  O  O   . PRO A 1 127 ? 35.174 110.336 12.754   1.00 36.28  ? 129 PRO A O   1 
ATOM   755  C  CB  . PRO A 1 127 ? 33.201 107.893 13.447   1.00 45.48  ? 129 PRO A CB  1 
ATOM   756  C  CG  . PRO A 1 127 ? 34.003 106.648 13.789   1.00 47.86  ? 129 PRO A CG  1 
ATOM   757  C  CD  . PRO A 1 127 ? 35.414 106.931 13.326   1.00 47.98  ? 129 PRO A CD  1 
ATOM   758  N  N   . GLY A 1 128 ? 33.183 110.774 11.843   1.00 34.87  ? 130 GLY A N   1 
ATOM   759  C  CA  . GLY A 1 128 ? 33.341 112.236 11.930   1.00 31.69  ? 130 GLY A CA  1 
ATOM   760  C  C   . GLY A 1 128 ? 32.879 112.968 10.677   1.00 29.85  ? 130 GLY A C   1 
ATOM   761  O  O   . GLY A 1 128 ? 31.971 112.469 9.960    1.00 29.51  ? 130 GLY A O   1 
ATOM   762  N  N   . TYR A 1 129 ? 33.476 114.134 10.444   1.00 27.47  ? 131 TYR A N   1 
ATOM   763  C  CA  . TYR A 1 129 ? 33.092 115.096 9.384    1.00 26.51  ? 131 TYR A CA  1 
ATOM   764  C  C   . TYR A 1 129 ? 34.305 115.257 8.455    1.00 27.39  ? 131 TYR A C   1 
ATOM   765  O  O   . TYR A 1 129 ? 35.426 115.489 8.957    1.00 31.42  ? 131 TYR A O   1 
ATOM   766  C  CB  . TYR A 1 129 ? 32.670 116.407 10.054   1.00 24.21  ? 131 TYR A CB  1 
ATOM   767  C  CG  . TYR A 1 129 ? 31.715 117.322 9.314    1.00 22.93  ? 131 TYR A CG  1 
ATOM   768  C  CD1 . TYR A 1 129 ? 30.615 116.849 8.591    1.00 22.32  ? 131 TYR A CD1 1 
ATOM   769  C  CD2 . TYR A 1 129 ? 31.876 118.701 9.394    1.00 21.57  ? 131 TYR A CD2 1 
ATOM   770  C  CE1 . TYR A 1 129 ? 29.713 117.713 7.990    1.00 20.94  ? 131 TYR A CE1 1 
ATOM   771  C  CE2 . TYR A 1 129 ? 30.997 119.577 8.781    1.00 20.48  ? 131 TYR A CE2 1 
ATOM   772  C  CZ  . TYR A 1 129 ? 29.908 119.082 8.088    1.00 20.40  ? 131 TYR A CZ  1 
ATOM   773  O  OH  . TYR A 1 129 ? 29.029 119.978 7.557    1.00 19.36  ? 131 TYR A OH  1 
ATOM   774  N  N   . TYR A 1 130 ? 34.107 115.158 7.145    1.00 26.35  ? 132 TYR A N   1 
ATOM   775  C  CA  . TYR A 1 130 ? 35.196 115.195 6.143    1.00 25.05  ? 132 TYR A CA  1 
ATOM   776  C  C   . TYR A 1 130 ? 34.909 116.325 5.159    1.00 22.85  ? 132 TYR A C   1 
ATOM   777  O  O   . TYR A 1 130 ? 33.716 116.574 4.815    1.00 20.86  ? 132 TYR A O   1 
ATOM   778  C  CB  . TYR A 1 130 ? 35.338 113.834 5.465    1.00 26.08  ? 132 TYR A CB  1 
ATOM   779  C  CG  . TYR A 1 130 ? 35.910 112.787 6.376    1.00 28.16  ? 132 TYR A CG  1 
ATOM   780  C  CD1 . TYR A 1 130 ? 35.104 112.137 7.295    1.00 28.75  ? 132 TYR A CD1 1 
ATOM   781  C  CD2 . TYR A 1 130 ? 37.264 112.505 6.379    1.00 29.09  ? 132 TYR A CD2 1 
ATOM   782  C  CE1 . TYR A 1 130 ? 35.620 111.188 8.153    1.00 30.52  ? 132 TYR A CE1 1 
ATOM   783  C  CE2 . TYR A 1 130 ? 37.801 111.574 7.251    1.00 30.86  ? 132 TYR A CE2 1 
ATOM   784  C  CZ  . TYR A 1 130 ? 36.975 110.896 8.132    1.00 31.59  ? 132 TYR A CZ  1 
ATOM   785  O  OH  . TYR A 1 130 ? 37.493 109.954 8.988    1.00 33.00  ? 132 TYR A OH  1 
ATOM   786  N  N   . LEU A 1 131 ? 35.978 117.015 4.758    1.00 21.38  ? 133 LEU A N   1 
ATOM   787  C  CA  . LEU A 1 131 ? 35.946 117.877 3.564    1.00 20.98  ? 133 LEU A CA  1 
ATOM   788  C  C   . LEU A 1 131 ? 36.588 117.127 2.391    1.00 21.32  ? 133 LEU A C   1 
ATOM   789  O  O   . LEU A 1 131 ? 37.691 116.643 2.548    1.00 20.28  ? 133 LEU A O   1 
ATOM   790  C  CB  . LEU A 1 131 ? 36.649 119.192 3.865    1.00 20.70  ? 133 LEU A CB  1 
ATOM   791  C  CG  . LEU A 1 131 ? 36.492 120.225 2.756    1.00 20.54  ? 133 LEU A CG  1 
ATOM   792  C  CD1 . LEU A 1 131 ? 36.778 121.622 3.287    1.00 20.42  ? 133 LEU A CD1 1 
ATOM   793  C  CD2 . LEU A 1 131 ? 37.369 119.881 1.534    1.00 20.80  ? 133 LEU A CD2 1 
ATOM   794  N  N   . ILE A 1 132 ? 35.831 116.974 1.288    1.00 22.57  ? 134 ILE A N   1 
ATOM   795  C  CA  . ILE A 1 132 ? 36.263 116.349 0.007    1.00 23.24  ? 134 ILE A CA  1 
ATOM   796  C  C   . ILE A 1 132 ? 36.454 117.456 -1.030   1.00 23.13  ? 134 ILE A C   1 
ATOM   797  O  O   . ILE A 1 132 ? 35.491 118.235 -1.275   1.00 22.31  ? 134 ILE A O   1 
ATOM   798  C  CB  . ILE A 1 132 ? 35.233 115.335 -0.508   1.00 23.87  ? 134 ILE A CB  1 
ATOM   799  C  CG1 . ILE A 1 132 ? 34.946 114.263 0.540    1.00 24.21  ? 134 ILE A CG1 1 
ATOM   800  C  CG2 . ILE A 1 132 ? 35.700 114.763 -1.862   1.00 23.76  ? 134 ILE A CG2 1 
ATOM   801  C  CD1 . ILE A 1 132 ? 33.802 113.342 0.161    1.00 25.32  ? 134 ILE A CD1 1 
ATOM   802  N  N   . LYS A 1 133 ? 37.624 117.475 -1.647   1.00 23.63  ? 135 LYS A N   1 
ATOM   803  C  CA  . LYS A 1 133 ? 37.933 118.377 -2.778   1.00 23.34  ? 135 LYS A CA  1 
ATOM   804  C  C   . LYS A 1 133 ? 38.840 117.638 -3.758   1.00 24.64  ? 135 LYS A C   1 
ATOM   805  O  O   . LYS A 1 133 ? 39.581 116.741 -3.320   1.00 24.17  ? 135 LYS A O   1 
ATOM   806  C  CB  . LYS A 1 133 ? 38.678 119.628 -2.317   1.00 23.15  ? 135 LYS A CB  1 
ATOM   807  C  CG  . LYS A 1 133 ? 39.959 119.322 -1.580   1.00 24.55  ? 135 LYS A CG  1 
ATOM   808  C  CD  . LYS A 1 133 ? 40.575 120.542 -0.979   1.00 25.44  ? 135 LYS A CD  1 
ATOM   809  C  CE  . LYS A 1 133 ? 41.511 121.232 -1.940   1.00 26.49  ? 135 LYS A CE  1 
ATOM   810  N  NZ  . LYS A 1 133 ? 42.287 122.302 -1.273   1.00 27.41  ? 135 LYS A NZ  1 
ATOM   811  N  N   . ASP A 1 134 ? 38.791 118.048 -5.036   1.00 24.47  ? 136 ASP A N   1 
ATOM   812  C  CA  . ASP A 1 134 ? 39.892 117.824 -5.990   1.00 26.10  ? 136 ASP A CA  1 
ATOM   813  C  C   . ASP A 1 134 ? 41.163 118.352 -5.336   1.00 26.65  ? 136 ASP A C   1 
ATOM   814  O  O   . ASP A 1 134 ? 41.166 119.484 -4.822   1.00 24.95  ? 136 ASP A O   1 
ATOM   815  C  CB  . ASP A 1 134 ? 39.608 118.475 -7.350   1.00 26.28  ? 136 ASP A CB  1 
ATOM   816  C  CG  . ASP A 1 134 ? 38.701 117.630 -8.222   1.00 27.28  ? 136 ASP A CG  1 
ATOM   817  O  OD1 . ASP A 1 134 ? 39.230 116.661 -8.814   1.00 28.26  ? 136 ASP A OD1 1 
ATOM   818  O  OD2 . ASP A 1 134 ? 37.468 117.949 -8.306   1.00 28.80  ? 136 ASP A OD2 1 
ATOM   819  N  N   . SER A 1 135 ? 42.227 117.573 -5.447   1.00 28.65  ? 137 SER A N   1 
ATOM   820  C  CA  . SER A 1 135 ? 43.608 118.019 -5.178   1.00 30.15  ? 137 SER A CA  1 
ATOM   821  C  C   . SER A 1 135 ? 43.961 119.270 -6.006   1.00 30.61  ? 137 SER A C   1 
ATOM   822  O  O   . SER A 1 135 ? 43.680 119.341 -7.237   1.00 28.47  ? 137 SER A O   1 
ATOM   823  C  CB  . SER A 1 135 ? 44.516 116.885 -5.429   1.00 32.25  ? 137 SER A CB  1 
ATOM   824  O  OG  . SER A 1 135 ? 45.829 117.328 -5.288   1.00 35.40  ? 137 SER A OG  1 
ATOM   825  N  N   . ARG A 1 136 ? 44.547 120.249 -5.330   1.00 32.47  ? 138 ARG A N   1 
ATOM   826  C  CA  . ARG A 1 136 ? 44.969 121.564 -5.877   1.00 35.91  ? 138 ARG A CA  1 
ATOM   827  C  C   . ARG A 1 136 ? 45.788 121.396 -7.175   1.00 37.13  ? 138 ARG A C   1 
ATOM   828  O  O   . ARG A 1 136 ? 46.749 120.619 -7.194   1.00 38.59  ? 138 ARG A O   1 
ATOM   829  C  CB  . ARG A 1 136 ? 45.768 122.225 -4.765   1.00 39.54  ? 138 ARG A CB  1 
ATOM   830  C  CG  . ARG A 1 136 ? 46.198 123.647 -5.037   1.00 44.42  ? 138 ARG A CG  1 
ATOM   831  C  CD  . ARG A 1 136 ? 46.682 124.272 -3.733   1.00 50.02  ? 138 ARG A CD  1 
ATOM   832  N  NE  . ARG A 1 136 ? 47.403 125.479 -4.097   1.00 56.63  ? 138 ARG A NE  1 
ATOM   833  C  CZ  . ARG A 1 136 ? 46.841 126.585 -4.610   1.00 60.93  ? 138 ARG A CZ  1 
ATOM   834  N  NH1 . ARG A 1 136 ? 45.522 126.668 -4.761   1.00 59.64  ? 138 ARG A NH1 1 
ATOM   835  N  NH2 . ARG A 1 136 ? 47.611 127.616 -4.951   1.00 61.74  ? 138 ARG A NH2 1 
ATOM   836  N  N   . GLY A 1 137 ? 45.409 122.072 -8.250   1.00 37.53  ? 139 GLY A N   1 
ATOM   837  C  CA  . GLY A 1 137 ? 46.150 122.060 -9.538   1.00 38.75  ? 139 GLY A CA  1 
ATOM   838  C  C   . GLY A 1 137 ? 46.097 120.733 -10.287  1.00 38.66  ? 139 GLY A C   1 
ATOM   839  O  O   . GLY A 1 137 ? 46.666 120.655 -11.389  1.00 39.43  ? 139 GLY A O   1 
ATOM   840  N  N   . SER A 1 138 ? 45.402 119.748 -9.736   1.00 37.76  ? 140 SER A N   1 
ATOM   841  C  CA  . SER A 1 138 ? 45.353 118.327 -10.152  1.00 38.86  ? 140 SER A CA  1 
ATOM   842  C  C   . SER A 1 138 ? 44.863 118.188 -11.597  1.00 38.87  ? 140 SER A C   1 
ATOM   843  O  O   . SER A 1 138 ? 45.031 117.127 -12.165  1.00 38.61  ? 140 SER A O   1 
ATOM   844  C  CB  . SER A 1 138 ? 44.414 117.619 -9.194   1.00 39.24  ? 140 SER A CB  1 
ATOM   845  O  OG  . SER A 1 138 ? 44.330 116.240 -9.472   1.00 42.23  ? 140 SER A OG  1 
ATOM   846  N  N   . LEU A 1 139 ? 44.174 119.188 -12.135  1.00 39.18  ? 141 LEU A N   1 
ATOM   847  C  CA  . LEU A 1 139 ? 43.449 119.054 -13.423  1.00 41.71  ? 141 LEU A CA  1 
ATOM   848  C  C   . LEU A 1 139 ? 43.993 120.057 -14.453  1.00 44.31  ? 141 LEU A C   1 
ATOM   849  O  O   . LEU A 1 139 ? 43.364 120.185 -15.473  1.00 46.19  ? 141 LEU A O   1 
ATOM   850  C  CB  . LEU A 1 139 ? 41.948 119.281 -13.177  1.00 39.14  ? 141 LEU A CB  1 
ATOM   851  C  CG  . LEU A 1 139 ? 41.215 118.260 -12.303  1.00 37.48  ? 141 LEU A CG  1 
ATOM   852  C  CD1 . LEU A 1 139 ? 39.735 118.631 -12.243  1.00 36.12  ? 141 LEU A CD1 1 
ATOM   853  C  CD2 . LEU A 1 139 ? 41.419 116.819 -12.783  1.00 36.97  ? 141 LEU A CD2 1 
ATOM   854  N  N   . ASP A 1 140 ? 45.131 120.708 -14.228  1.00 49.86  ? 142 ASP A N   1 
ATOM   855  C  CA  . ASP A 1 140 ? 45.552 121.900 -15.014  1.00 55.87  ? 142 ASP A CA  1 
ATOM   856  C  C   . ASP A 1 140 ? 46.008 121.531 -16.424  1.00 58.47  ? 142 ASP A C   1 
ATOM   857  O  O   . ASP A 1 140 ? 45.743 122.340 -17.344  1.00 62.58  ? 142 ASP A O   1 
ATOM   858  C  CB  . ASP A 1 140 ? 46.626 122.701 -14.290  1.00 61.00  ? 142 ASP A CB  1 
ATOM   859  C  CG  . ASP A 1 140 ? 46.030 123.471 -13.125  1.00 64.46  ? 142 ASP A CG  1 
ATOM   860  O  OD1 . ASP A 1 140 ? 44.775 123.397 -12.935  1.00 63.17  ? 142 ASP A OD1 1 
ATOM   861  O  OD2 . ASP A 1 140 ? 46.811 124.137 -12.414  1.00 69.54  ? 142 ASP A OD2 1 
ATOM   862  N  N   . ASN A 1 141 ? 46.636 120.380 -16.634  1.00 59.76  ? 143 ASN A N   1 
ATOM   863  C  CA  . ASN A 1 141 ? 47.050 120.025 -18.019  1.00 64.74  ? 143 ASN A CA  1 
ATOM   864  C  C   . ASN A 1 141 ? 45.933 119.250 -18.738  1.00 60.75  ? 143 ASN A C   1 
ATOM   865  O  O   . ASN A 1 141 ? 46.028 119.121 -19.964  1.00 63.88  ? 143 ASN A O   1 
ATOM   866  C  CB  . ASN A 1 141 ? 48.423 119.343 -18.055  1.00 70.87  ? 143 ASN A CB  1 
ATOM   867  C  CG  . ASN A 1 141 ? 49.539 120.353 -18.269  1.00 77.62  ? 143 ASN A CG  1 
ATOM   868  O  OD1 . ASN A 1 141 ? 49.860 120.719 -19.411  1.00 77.32  ? 143 ASN A OD1 1 
ATOM   869  N  ND2 . ASN A 1 141 ? 50.144 120.811 -17.179  1.00 82.55  ? 143 ASN A ND2 1 
ATOM   870  N  N   . LYS A 1 142 ? 44.880 118.819 -18.043  1.00 54.41  ? 144 LYS A N   1 
ATOM   871  C  CA  . LYS A 1 142 ? 43.887 117.866 -18.608  1.00 49.95  ? 144 LYS A CA  1 
ATOM   872  C  C   . LYS A 1 142 ? 42.688 118.632 -19.166  1.00 45.32  ? 144 LYS A C   1 
ATOM   873  O  O   . LYS A 1 142 ? 42.292 119.649 -18.574  1.00 44.45  ? 144 LYS A O   1 
ATOM   874  C  CB  . LYS A 1 142 ? 43.444 116.882 -17.526  1.00 50.06  ? 144 LYS A CB  1 
ATOM   875  C  CG  . LYS A 1 142 ? 44.588 116.167 -16.843  1.00 51.55  ? 144 LYS A CG  1 
ATOM   876  C  CD  . LYS A 1 142 ? 44.210 115.479 -15.547  1.00 53.44  ? 144 LYS A CD  1 
ATOM   877  C  CE  . LYS A 1 142 ? 45.440 114.991 -14.803  1.00 55.19  ? 144 LYS A CE  1 
ATOM   878  N  NZ  . LYS A 1 142 ? 45.170 113.780 -13.992  1.00 55.86  ? 144 LYS A NZ  1 
ATOM   879  N  N   . LYS A 1 143 ? 42.107 118.119 -20.242  1.00 40.80  ? 145 LYS A N   1 
ATOM   880  C  CA  . LYS A 1 143 ? 40.947 118.740 -20.924  1.00 38.26  ? 145 LYS A CA  1 
ATOM   881  C  C   . LYS A 1 143 ? 39.685 117.997 -20.511  1.00 34.77  ? 145 LYS A C   1 
ATOM   882  O  O   . LYS A 1 143 ? 39.807 116.804 -20.214  1.00 34.49  ? 145 LYS A O   1 
ATOM   883  C  CB  . LYS A 1 143 ? 41.097 118.650 -22.444  1.00 39.22  ? 145 LYS A CB  1 
ATOM   884  C  CG  . LYS A 1 143 ? 42.224 119.486 -23.037  1.00 40.50  ? 145 LYS A CG  1 
ATOM   885  C  CD  . LYS A 1 143 ? 42.265 119.383 -24.541  1.00 41.99  ? 145 LYS A CD  1 
ATOM   886  C  CE  . LYS A 1 143 ? 42.976 120.544 -25.188  1.00 44.01  ? 145 LYS A CE  1 
ATOM   887  N  NZ  . LYS A 1 143 ? 42.471 120.742 -26.577  1.00 46.22  ? 145 LYS A NZ  1 
ATOM   888  N  N   . GLY A 1 144 ? 38.545 118.696 -20.494  1.00 32.07  ? 146 GLY A N   1 
ATOM   889  C  CA  . GLY A 1 144 ? 37.203 118.121 -20.267  1.00 31.61  ? 146 GLY A CA  1 
ATOM   890  C  C   . GLY A 1 144 ? 36.892 117.803 -18.794  1.00 30.71  ? 146 GLY A C   1 
ATOM   891  O  O   . GLY A 1 144 ? 35.949 117.023 -18.556  1.00 28.90  ? 146 GLY A O   1 
ATOM   892  N  N   . HIS A 1 145 ? 37.616 118.394 -17.836  1.00 30.09  ? 147 HIS A N   1 
ATOM   893  C  CA  . HIS A 1 145 ? 37.416 118.115 -16.391  1.00 30.13  ? 147 HIS A CA  1 
ATOM   894  C  C   . HIS A 1 145 ? 37.035 119.387 -15.672  1.00 28.19  ? 147 HIS A C   1 
ATOM   895  O  O   . HIS A 1 145 ? 37.249 120.452 -16.217  1.00 27.63  ? 147 HIS A O   1 
ATOM   896  C  CB  . HIS A 1 145 ? 38.648 117.452 -15.775  1.00 32.22  ? 147 HIS A CB  1 
ATOM   897  C  CG  . HIS A 1 145 ? 38.925 116.106 -16.357  1.00 35.99  ? 147 HIS A CG  1 
ATOM   898  N  ND1 . HIS A 1 145 ? 37.989 115.081 -16.356  1.00 39.05  ? 147 HIS A ND1 1 
ATOM   899  C  CD2 . HIS A 1 145 ? 40.005 115.625 -17.002  1.00 36.78  ? 147 HIS A CD2 1 
ATOM   900  C  CE1 . HIS A 1 145 ? 38.489 114.041 -16.983  1.00 39.26  ? 147 HIS A CE1 1 
ATOM   901  N  NE2 . HIS A 1 145 ? 39.726 114.344 -17.352  1.00 38.48  ? 147 HIS A NE2 1 
ATOM   902  N  N   . ALA A 1 146 ? 36.506 119.239 -14.458  1.00 26.73  ? 148 ALA A N   1 
ATOM   903  C  CA  . ALA A 1 146 ? 36.181 120.391 -13.606  1.00 25.72  ? 148 ALA A CA  1 
ATOM   904  C  C   . ALA A 1 146 ? 36.382 120.012 -12.150  1.00 24.88  ? 148 ALA A C   1 
ATOM   905  O  O   . ALA A 1 146 ? 36.117 118.829 -11.830  1.00 24.39  ? 148 ALA A O   1 
ATOM   906  C  CB  . ALA A 1 146 ? 34.761 120.830 -13.851  1.00 26.07  ? 148 ALA A CB  1 
ATOM   907  N  N   . TYR A 1 147 ? 36.854 120.981 -11.356  1.00 24.28  ? 149 TYR A N   1 
ATOM   908  C  CA  . TYR A 1 147 ? 37.036 120.883 -9.875   1.00 23.54  ? 149 TYR A CA  1 
ATOM   909  C  C   . TYR A 1 147 ? 35.666 120.869 -9.204   1.00 22.22  ? 149 TYR A C   1 
ATOM   910  O  O   . TYR A 1 147 ? 34.761 121.625 -9.608   1.00 21.96  ? 149 TYR A O   1 
ATOM   911  C  CB  . TYR A 1 147 ? 37.874 122.031 -9.303   1.00 23.42  ? 149 TYR A CB  1 
ATOM   912  C  CG  . TYR A 1 147 ? 39.314 122.027 -9.748   1.00 24.65  ? 149 TYR A CG  1 
ATOM   913  C  CD1 . TYR A 1 147 ? 40.265 121.275 -9.082   1.00 25.59  ? 149 TYR A CD1 1 
ATOM   914  C  CD2 . TYR A 1 147 ? 39.734 122.775 -10.851  1.00 25.25  ? 149 TYR A CD2 1 
ATOM   915  C  CE1 . TYR A 1 147 ? 41.582 121.241 -9.522   1.00 27.65  ? 149 TYR A CE1 1 
ATOM   916  C  CE2 . TYR A 1 147 ? 41.056 122.783 -11.277  1.00 25.67  ? 149 TYR A CE2 1 
ATOM   917  C  CZ  . TYR A 1 147 ? 41.982 121.985 -10.633  1.00 26.63  ? 149 TYR A CZ  1 
ATOM   918  O  OH  . TYR A 1 147 ? 43.300 122.013 -10.991  1.00 27.52  ? 149 TYR A OH  1 
ATOM   919  N  N   . THR A 1 148 ? 35.515 120.003 -8.206   1.00 21.93  ? 150 THR A N   1 
ATOM   920  C  CA  . THR A 1 148 ? 34.256 119.894 -7.437   1.00 20.86  ? 150 THR A CA  1 
ATOM   921  C  C   . THR A 1 148 ? 34.201 121.037 -6.428   1.00 20.21  ? 150 THR A C   1 
ATOM   922  O  O   . THR A 1 148 ? 35.241 121.480 -5.948   1.00 19.61  ? 150 THR A O   1 
ATOM   923  C  CB  . THR A 1 148 ? 34.132 118.565 -6.710   1.00 21.19  ? 150 THR A CB  1 
ATOM   924  O  OG1 . THR A 1 148 ? 32.890 118.577 -5.999   1.00 21.15  ? 150 THR A OG1 1 
ATOM   925  C  CG2 . THR A 1 148 ? 35.268 118.361 -5.737   1.00 21.10  ? 150 THR A CG2 1 
ATOM   926  N  N   . SER A 1 149 ? 33.011 121.558 -6.187   1.00 20.70  ? 151 SER A N   1 
ATOM   927  C  CA  . SER A 1 149 ? 32.705 122.309 -4.945   1.00 20.46  ? 151 SER A CA  1 
ATOM   928  C  C   . SER A 1 149 ? 33.255 121.487 -3.776   1.00 20.57  ? 151 SER A C   1 
ATOM   929  O  O   . SER A 1 149 ? 33.104 120.244 -3.753   1.00 19.96  ? 151 SER A O   1 
ATOM   930  C  CB  . SER A 1 149 ? 31.229 122.573 -4.776   1.00 20.68  ? 151 SER A CB  1 
ATOM   931  O  OG  . SER A 1 149 ? 30.730 123.496 -5.742   1.00 21.20  ? 151 SER A OG  1 
ATOM   932  N  N   . PHE A 1 150 ? 33.891 122.170 -2.837   1.00 20.70  ? 152 PHE A N   1 
ATOM   933  C  CA  . PHE A 1 150 ? 34.230 121.582 -1.536   1.00 20.87  ? 152 PHE A CA  1 
ATOM   934  C  C   . PHE A 1 150 ? 32.936 120.970 -0.995   1.00 20.56  ? 152 PHE A C   1 
ATOM   935  O  O   . PHE A 1 150 ? 31.857 121.658 -0.941   1.00 19.19  ? 152 PHE A O   1 
ATOM   936  C  CB  . PHE A 1 150 ? 34.890 122.621 -0.633   1.00 21.44  ? 152 PHE A CB  1 
ATOM   937  C  CG  . PHE A 1 150 ? 36.105 123.310 -1.207   1.00 22.94  ? 152 PHE A CG  1 
ATOM   938  C  CD1 . PHE A 1 150 ? 36.994 122.639 -2.050   1.00 24.94  ? 152 PHE A CD1 1 
ATOM   939  C  CD2 . PHE A 1 150 ? 36.370 124.636 -0.900   1.00 23.36  ? 152 PHE A CD2 1 
ATOM   940  C  CE1 . PHE A 1 150 ? 38.100 123.284 -2.592   1.00 25.07  ? 152 PHE A CE1 1 
ATOM   941  C  CE2 . PHE A 1 150 ? 37.485 125.274 -1.419   1.00 24.37  ? 152 PHE A CE2 1 
ATOM   942  C  CZ  . PHE A 1 150 ? 38.351 124.598 -2.261   1.00 24.85  ? 152 PHE A CZ  1 
ATOM   943  N  N   . MET A 1 151 ? 33.043 119.676 -0.675   1.00 20.62  ? 153 MET A N   1 
ATOM   944  C  CA  . MET A 1 151 ? 31.951 118.893 -0.067   1.00 21.07  ? 153 MET A CA  1 
ATOM   945  C  C   . MET A 1 151 ? 32.266 118.601 1.390    1.00 20.50  ? 153 MET A C   1 
ATOM   946  O  O   . MET A 1 151 ? 33.265 117.907 1.681    1.00 20.00  ? 153 MET A O   1 
ATOM   947  C  CB  . MET A 1 151 ? 31.730 117.587 -0.811   1.00 22.51  ? 153 MET A CB  1 
ATOM   948  C  CG  . MET A 1 151 ? 31.457 117.844 -2.257   1.00 23.84  ? 153 MET A CG  1 
ATOM   949  S  SD  . MET A 1 151 ? 31.535 116.335 -3.186   0.89 26.06  ? 153 MET A SD  1 
ATOM   950  C  CE  . MET A 1 151 ? 30.093 115.541 -2.489   1.00 28.01  ? 153 MET A CE  1 
ATOM   951  N  N   . LEU A 1 152 ? 31.385 119.050 2.264    1.00 20.10  ? 154 LEU A N   1 
ATOM   952  C  CA  . LEU A 1 152 ? 31.407 118.585 3.673    1.00 20.88  ? 154 LEU A CA  1 
ATOM   953  C  C   . LEU A 1 152 ? 30.488 117.360 3.794    1.00 22.50  ? 154 LEU A C   1 
ATOM   954  O  O   . LEU A 1 152 ? 29.365 117.385 3.321    1.00 22.13  ? 154 LEU A O   1 
ATOM   955  C  CB  . LEU A 1 152 ? 31.021 119.748 4.576    1.00 19.13  ? 154 LEU A CB  1 
ATOM   956  C  CG  . LEU A 1 152 ? 32.125 120.757 4.772    1.00 18.13  ? 154 LEU A CG  1 
ATOM   957  C  CD1 . LEU A 1 152 ? 31.569 121.955 5.481    1.00 18.21  ? 154 LEU A CD1 1 
ATOM   958  C  CD2 . LEU A 1 152 ? 33.231 120.158 5.607    1.00 18.11  ? 154 LEU A CD2 1 
ATOM   959  N  N   . GLN A 1 153 ? 30.993 116.304 4.403    1.00 24.91  ? 155 GLN A N   1 
ATOM   960  C  CA  . GLN A 1 153 ? 30.282 115.021 4.489    1.00 27.75  ? 155 GLN A CA  1 
ATOM   961  C  C   . GLN A 1 153 ? 30.542 114.418 5.861    1.00 29.44  ? 155 GLN A C   1 
ATOM   962  O  O   . GLN A 1 153 ? 31.700 114.394 6.268    1.00 30.50  ? 155 GLN A O   1 
ATOM   963  C  CB  . GLN A 1 153 ? 30.783 114.067 3.416    1.00 29.68  ? 155 GLN A CB  1 
ATOM   964  C  CG  . GLN A 1 153 ? 29.919 112.814 3.266    1.00 31.73  ? 155 GLN A CG  1 
ATOM   965  C  CD  . GLN A 1 153 ? 28.458 113.100 3.012    1.00 31.69  ? 155 GLN A CD  1 
ATOM   966  O  OE1 . GLN A 1 153 ? 28.118 113.840 2.060    1.00 31.29  ? 155 GLN A OE1 1 
ATOM   967  N  NE2 . GLN A 1 153 ? 27.621 112.507 3.869    1.00 31.04  ? 155 GLN A NE2 1 
ATOM   968  N  N   . VAL A 1 154 ? 29.494 113.932 6.512    1.00 31.84  ? 156 VAL A N   1 
ATOM   969  C  CA  . VAL A 1 154 ? 29.576 113.011 7.670    1.00 33.42  ? 156 VAL A CA  1 
ATOM   970  C  C   . VAL A 1 154 ? 29.951 111.628 7.126    1.00 35.96  ? 156 VAL A C   1 
ATOM   971  O  O   . VAL A 1 154 ? 29.372 111.177 6.119    1.00 36.53  ? 156 VAL A O   1 
ATOM   972  C  CB  . VAL A 1 154 ? 28.250 113.026 8.445    1.00 34.69  ? 156 VAL A CB  1 
ATOM   973  C  CG1 . VAL A 1 154 ? 28.312 112.078 9.613    1.00 37.13  ? 156 VAL A CG1 1 
ATOM   974  C  CG2 . VAL A 1 154 ? 27.905 114.407 8.977    1.00 33.90  ? 156 VAL A CG2 1 
ATOM   975  N  N   . ALA A 1 155 ? 30.948 111.000 7.718    1.00 38.86  ? 157 ALA A N   1 
ATOM   976  C  CA  . ALA A 1 155 ? 31.303 109.605 7.412    1.00 43.28  ? 157 ALA A CA  1 
ATOM   977  C  C   . ALA A 1 155 ? 30.124 108.694 7.789    1.00 47.69  ? 157 ALA A C   1 
ATOM   978  O  O   . ALA A 1 155 ? 29.917 108.435 8.993    1.00 43.88  ? 157 ALA A O   1 
ATOM   979  C  CB  . ALA A 1 155 ? 32.543 109.239 8.177    1.00 45.19  ? 157 ALA A CB  1 
ATOM   980  N  N   . LYS A 1 156 ? 29.376 108.230 6.785    1.00 51.20  ? 158 LYS A N   1 
ATOM   981  C  CA  . LYS A 1 156 ? 28.470 107.048 6.887    1.00 56.29  ? 158 LYS A CA  1 
ATOM   982  C  C   . LYS A 1 156 ? 28.807 106.069 5.752    1.00 59.43  ? 158 LYS A C   1 
ATOM   983  O  O   . LYS A 1 156 ? 29.681 106.380 4.898    1.00 62.19  ? 158 LYS A O   1 
ATOM   984  C  CB  . LYS A 1 156 ? 26.983 107.413 6.793    1.00 56.92  ? 158 LYS A CB  1 
ATOM   985  C  CG  . LYS A 1 156 ? 26.564 108.720 7.445    1.00 57.15  ? 158 LYS A CG  1 
ATOM   986  C  CD  . LYS A 1 156 ? 25.390 109.391 6.741    1.00 58.57  ? 158 LYS A CD  1 
ATOM   987  C  CE  . LYS A 1 156 ? 25.290 110.877 7.029    1.00 58.47  ? 158 LYS A CE  1 
ATOM   988  N  NZ  . LYS A 1 156 ? 24.077 111.482 6.433    1.00 59.05  ? 158 LYS A NZ  1 
ATOM   989  N  N   . ASP A 1 157 ? 28.124 104.925 5.723    1.00 61.26  ? 159 ASP A N   1 
ATOM   990  C  CA  . ASP A 1 157 ? 28.168 103.995 4.571    1.00 62.10  ? 159 ASP A CA  1 
ATOM   991  C  C   . ASP A 1 157 ? 27.121 104.512 3.575    1.00 60.76  ? 159 ASP A C   1 
ATOM   992  O  O   . ASP A 1 157 ? 26.007 103.980 3.557    1.00 64.45  ? 159 ASP A O   1 
ATOM   993  C  CB  . ASP A 1 157 ? 28.048 102.542 5.052    1.00 66.18  ? 159 ASP A CB  1 
ATOM   994  C  CG  . ASP A 1 157 ? 29.386 101.891 5.395    1.00 69.15  ? 159 ASP A CG  1 
ATOM   995  O  OD1 . ASP A 1 157 ? 30.363 102.635 5.617    1.00 70.05  ? 159 ASP A OD1 1 
ATOM   996  O  OD2 . ASP A 1 157 ? 29.454 100.641 5.430    1.00 72.17  ? 159 ASP A OD2 1 
ATOM   997  N  N   . THR A 1 158 ? 27.463 105.547 2.802    1.00 55.52  ? 160 THR A N   1 
ATOM   998  C  CA  . THR A 1 158 ? 26.490 106.384 2.051    1.00 53.69  ? 160 THR A CA  1 
ATOM   999  C  C   . THR A 1 158 ? 27.032 106.689 0.652    1.00 52.14  ? 160 THR A C   1 
ATOM   1000 O  O   . THR A 1 158 ? 28.255 106.588 0.455    1.00 51.21  ? 160 THR A O   1 
ATOM   1001 C  CB  . THR A 1 158 ? 26.171 107.689 2.798    1.00 52.14  ? 160 THR A CB  1 
ATOM   1002 O  OG1 . THR A 1 158 ? 25.052 108.294 2.159    1.00 52.18  ? 160 THR A OG1 1 
ATOM   1003 C  CG2 . THR A 1 158 ? 27.299 108.703 2.813    1.00 51.58  ? 160 THR A CG2 1 
ATOM   1004 N  N   . THR A 1 159 ? 26.152 107.097 -0.260   1.00 51.45  ? 161 THR A N   1 
ATOM   1005 C  CA  . THR A 1 159 ? 26.506 107.526 -1.643   1.00 50.41  ? 161 THR A CA  1 
ATOM   1006 C  C   . THR A 1 159 ? 26.166 109.003 -1.813   1.00 46.79  ? 161 THR A C   1 
ATOM   1007 O  O   . THR A 1 159 ? 25.020 109.375 -1.593   1.00 47.81  ? 161 THR A O   1 
ATOM   1008 C  CB  . THR A 1 159 ? 25.810 106.680 -2.712   1.00 52.14  ? 161 THR A CB  1 
ATOM   1009 O  OG1 . THR A 1 159 ? 26.434 105.397 -2.607   1.00 54.98  ? 161 THR A OG1 1 
ATOM   1010 C  CG2 . THR A 1 159 ? 25.951 107.264 -4.105   1.00 52.81  ? 161 THR A CG2 1 
ATOM   1011 N  N   . VAL A 1 160 ? 27.140 109.820 -2.182   1.00 43.05  ? 162 VAL A N   1 
ATOM   1012 C  CA  . VAL A 1 160 ? 26.877 111.255 -2.484   1.00 40.54  ? 162 VAL A CA  1 
ATOM   1013 C  C   . VAL A 1 160 ? 27.419 111.600 -3.875   1.00 37.80  ? 162 VAL A C   1 
ATOM   1014 O  O   . VAL A 1 160 ? 28.545 111.166 -4.225   1.00 36.81  ? 162 VAL A O   1 
ATOM   1015 C  CB  . VAL A 1 160 ? 27.465 112.148 -1.386   1.00 40.89  ? 162 VAL A CB  1 
ATOM   1016 C  CG1 . VAL A 1 160 ? 28.950 111.881 -1.160   1.00 39.14  ? 162 VAL A CG1 1 
ATOM   1017 C  CG2 . VAL A 1 160 ? 27.152 113.614 -1.676   1.00 41.07  ? 162 VAL A CG2 1 
ATOM   1018 N  N   . ALA A 1 161 ? 26.649 112.344 -4.653   1.00 35.08  ? 163 ALA A N   1 
ATOM   1019 C  CA  . ALA A 1 161 ? 27.093 112.727 -6.013   1.00 34.28  ? 163 ALA A CA  1 
ATOM   1020 C  C   . ALA A 1 161 ? 28.166 113.798 -5.890   1.00 31.96  ? 163 ALA A C   1 
ATOM   1021 O  O   . ALA A 1 161 ? 27.917 114.804 -5.202   1.00 29.73  ? 163 ALA A O   1 
ATOM   1022 C  CB  . ALA A 1 161 ? 25.952 113.223 -6.848   1.00 34.41  ? 163 ALA A CB  1 
ATOM   1023 N  N   . VAL A 1 162 ? 29.276 113.636 -6.600   1.00 31.58  ? 164 VAL A N   1 
ATOM   1024 C  CA  . VAL A 1 162 ? 30.322 114.688 -6.598   1.00 31.09  ? 164 VAL A CA  1 
ATOM   1025 C  C   . VAL A 1 162 ? 29.702 116.012 -7.093   1.00 29.94  ? 164 VAL A C   1 
ATOM   1026 O  O   . VAL A 1 162 ? 28.859 115.958 -7.975   1.00 30.44  ? 164 VAL A O   1 
ATOM   1027 C  CB  . VAL A 1 162 ? 31.524 114.238 -7.432   1.00 31.68  ? 164 VAL A CB  1 
ATOM   1028 C  CG1 . VAL A 1 162 ? 31.207 114.276 -8.919   1.00 32.37  ? 164 VAL A CG1 1 
ATOM   1029 C  CG2 . VAL A 1 162 ? 32.746 115.084 -7.121   1.00 31.45  ? 164 VAL A CG2 1 
ATOM   1030 N  N   . LYS A 1 163 ? 30.099 117.162 -6.542   1.00 29.59  ? 165 LYS A N   1 
ATOM   1031 C  CA  . LYS A 1 163 ? 29.549 118.480 -6.933   1.00 30.77  ? 165 LYS A CA  1 
ATOM   1032 C  C   . LYS A 1 163 ? 30.407 119.078 -8.044   1.00 29.77  ? 165 LYS A C   1 
ATOM   1033 O  O   . LYS A 1 163 ? 30.868 120.211 -7.899   1.00 28.20  ? 165 LYS A O   1 
ATOM   1034 C  CB  . LYS A 1 163 ? 29.480 119.407 -5.725   1.00 32.25  ? 165 LYS A CB  1 
ATOM   1035 C  CG  . LYS A 1 163 ? 28.537 118.916 -4.645   1.00 35.64  ? 165 LYS A CG  1 
ATOM   1036 C  CD  . LYS A 1 163 ? 27.074 118.870 -5.080   1.00 39.16  ? 165 LYS A CD  1 
ATOM   1037 C  CE  . LYS A 1 163 ? 26.426 120.236 -5.135   1.00 40.72  ? 165 LYS A CE  1 
ATOM   1038 N  NZ  . LYS A 1 163 ? 26.060 120.704 -3.780   1.00 43.31  ? 165 LYS A NZ  1 
ATOM   1039 N  N   . ALA A 1 164 ? 30.593 118.331 -9.123   1.00 34.43  ? 166 ALA A N   1 
ATOM   1040 C  CA  . ALA A 1 164 ? 31.401 118.748 -10.297  1.00 35.22  ? 166 ALA A CA  1 
ATOM   1041 C  C   . ALA A 1 164 ? 30.643 118.387 -11.569  1.00 34.16  ? 166 ALA A C   1 
ATOM   1042 O  O   . ALA A 1 164 ? 30.130 117.277 -11.647  1.00 34.83  ? 166 ALA A O   1 
ATOM   1043 C  CB  . ALA A 1 164 ? 32.749 118.075 -10.282  1.00 35.18  ? 166 ALA A CB  1 
ATOM   1044 N  N   . ASP A 1 165 ? 30.537 119.306 -12.516  1.00 32.97  ? 167 ASP A N   1 
ATOM   1045 C  CA  . ASP A 1 165 ? 30.146 118.930 -13.896  1.00 32.39  ? 167 ASP A CA  1 
ATOM   1046 C  C   . ASP A 1 165 ? 31.039 119.711 -14.857  1.00 29.80  ? 167 ASP A C   1 
ATOM   1047 O  O   . ASP A 1 165 ? 31.804 120.593 -14.391  1.00 27.43  ? 167 ASP A O   1 
ATOM   1048 C  CB  . ASP A 1 165 ? 28.649 119.145 -14.173  1.00 33.64  ? 167 ASP A CB  1 
ATOM   1049 C  CG  . ASP A 1 165 ? 28.119 118.337 -15.345  1.00 34.28  ? 167 ASP A CG  1 
ATOM   1050 O  OD1 . ASP A 1 165 ? 28.876 117.443 -15.772  1.00 35.20  ? 167 ASP A OD1 1 
ATOM   1051 O  OD2 . ASP A 1 165 ? 26.964 118.611 -15.830  1.00 34.31  ? 167 ASP A OD2 1 
ATOM   1052 N  N   . VAL A 1 166 ? 30.951 119.363 -16.137  1.00 28.31  ? 168 VAL A N   1 
ATOM   1053 C  CA  . VAL A 1 166 ? 31.697 120.045 -17.226  1.00 26.63  ? 168 VAL A CA  1 
ATOM   1054 C  C   . VAL A 1 166 ? 30.683 120.420 -18.281  1.00 26.82  ? 168 VAL A C   1 
ATOM   1055 O  O   . VAL A 1 166 ? 29.676 119.741 -18.452  1.00 28.62  ? 168 VAL A O   1 
ATOM   1056 C  CB  . VAL A 1 166 ? 32.812 119.150 -17.768  1.00 26.15  ? 168 VAL A CB  1 
ATOM   1057 C  CG1 . VAL A 1 166 ? 33.863 118.920 -16.694  1.00 26.91  ? 168 VAL A CG1 1 
ATOM   1058 C  CG2 . VAL A 1 166 ? 32.270 117.826 -18.267  1.00 26.62  ? 168 VAL A CG2 1 
ATOM   1059 N  N   . PRO A 1 167 ? 30.894 121.536 -18.995  1.00 26.48  ? 169 PRO A N   1 
ATOM   1060 C  CA  . PRO A 1 167 ? 30.145 121.815 -20.207  1.00 27.36  ? 169 PRO A CA  1 
ATOM   1061 C  C   . PRO A 1 167 ? 30.600 120.833 -21.298  1.00 26.71  ? 169 PRO A C   1 
ATOM   1062 O  O   . PRO A 1 167 ? 31.628 120.177 -21.164  1.00 26.16  ? 169 PRO A O   1 
ATOM   1063 C  CB  . PRO A 1 167 ? 30.517 123.264 -20.536  1.00 26.56  ? 169 PRO A CB  1 
ATOM   1064 C  CG  . PRO A 1 167 ? 31.923 123.381 -20.002  1.00 25.43  ? 169 PRO A CG  1 
ATOM   1065 C  CD  . PRO A 1 167 ? 31.907 122.556 -18.734  1.00 26.63  ? 169 PRO A CD  1 
ATOM   1066 N  N   . THR A 1 168 ? 29.784 120.714 -22.341  1.00 27.31  ? 170 THR A N   1 
ATOM   1067 C  CA  . THR A 1 168 ? 30.194 120.025 -23.593  1.00 26.26  ? 170 THR A CA  1 
ATOM   1068 C  C   . THR A 1 168 ? 30.133 121.000 -24.771  1.00 24.59  ? 170 THR A C   1 
ATOM   1069 O  O   . THR A 1 168 ? 29.380 122.009 -24.744  1.00 23.78  ? 170 THR A O   1 
ATOM   1070 C  CB  . THR A 1 168 ? 29.379 118.751 -23.810  1.00 27.66  ? 170 THR A CB  1 
ATOM   1071 O  OG1 . THR A 1 168 ? 28.065 119.198 -24.138  1.00 28.56  ? 170 THR A OG1 1 
ATOM   1072 C  CG2 . THR A 1 168 ? 29.368 117.847 -22.599  1.00 28.97  ? 170 THR A CG2 1 
ATOM   1073 N  N   . LEU A 1 169 ? 30.942 120.697 -25.775  1.00 23.34  ? 171 LEU A N   1 
ATOM   1074 C  CA  . LEU A 1 169 ? 30.888 121.391 -27.071  1.00 22.30  ? 171 LEU A CA  1 
ATOM   1075 C  C   . LEU A 1 169 ? 30.812 120.345 -28.188  1.00 22.66  ? 171 LEU A C   1 
ATOM   1076 O  O   . LEU A 1 169 ? 31.645 119.434 -28.210  1.00 23.26  ? 171 LEU A O   1 
ATOM   1077 C  CB  . LEU A 1 169 ? 32.083 122.317 -27.215  1.00 20.96  ? 171 LEU A CB  1 
ATOM   1078 C  CG  . LEU A 1 169 ? 31.879 123.334 -28.320  1.00 20.28  ? 171 LEU A CG  1 
ATOM   1079 C  CD1 . LEU A 1 169 ? 30.973 124.436 -27.858  1.00 20.29  ? 171 LEU A CD1 1 
ATOM   1080 C  CD2 . LEU A 1 169 ? 33.189 123.906 -28.820  1.00 20.30  ? 171 LEU A CD2 1 
ATOM   1081 N  N   . THR A 1 170 ? 29.761 120.427 -29.000  1.00 23.21  ? 172 THR A N   1 
ATOM   1082 C  CA  . THR A 1 170 ? 29.523 119.576 -30.197  1.00 24.00  ? 172 THR A CA  1 
ATOM   1083 C  C   . THR A 1 170 ? 29.482 120.469 -31.434  1.00 23.53  ? 172 THR A C   1 
ATOM   1084 O  O   . THR A 1 170 ? 28.827 121.531 -31.430  1.00 22.59  ? 172 THR A O   1 
ATOM   1085 C  CB  . THR A 1 170 ? 28.255 118.736 -30.031  1.00 25.19  ? 172 THR A CB  1 
ATOM   1086 O  OG1 . THR A 1 170 ? 28.474 118.053 -28.798  1.00 26.86  ? 172 THR A OG1 1 
ATOM   1087 C  CG2 . THR A 1 170 ? 28.005 117.752 -31.149  1.00 25.79  ? 172 THR A CG2 1 
ATOM   1088 N  N   . LYS A 1 171 ? 30.189 120.038 -32.466  1.00 23.77  ? 173 LYS A N   1 
ATOM   1089 C  CA  . LYS A 1 171 ? 30.182 120.719 -33.774  1.00 23.65  ? 173 LYS A CA  1 
ATOM   1090 C  C   . LYS A 1 171 ? 29.675 119.730 -34.802  1.00 24.86  ? 173 LYS A C   1 
ATOM   1091 O  O   . LYS A 1 171 ? 30.090 118.539 -34.775  1.00 24.81  ? 173 LYS A O   1 
ATOM   1092 C  CB  . LYS A 1 171 ? 31.572 121.172 -34.192  1.00 22.37  ? 173 LYS A CB  1 
ATOM   1093 C  CG  . LYS A 1 171 ? 31.569 121.928 -35.504  1.00 21.31  ? 173 LYS A CG  1 
ATOM   1094 C  CD  . LYS A 1 171 ? 32.947 122.316 -35.990  1.00 20.37  ? 173 LYS A CD  1 
ATOM   1095 C  CE  . LYS A 1 171 ? 32.872 123.163 -37.244  1.00 20.50  ? 173 LYS A CE  1 
ATOM   1096 N  NZ  . LYS A 1 171 ? 34.215 123.563 -37.696  1.00 18.71  ? 173 LYS A NZ  1 
ATOM   1097 N  N   . GLN A 1 172 ? 28.803 120.221 -35.667  1.00 26.87  ? 174 GLN A N   1 
ATOM   1098 C  CA  . GLN A 1 172 ? 28.345 119.445 -36.830  1.00 28.75  ? 174 GLN A CA  1 
ATOM   1099 C  C   . GLN A 1 172 ? 28.104 120.341 -38.031  1.00 28.31  ? 174 GLN A C   1 
ATOM   1100 O  O   . GLN A 1 172 ? 28.030 121.593 -37.903  1.00 26.99  ? 174 GLN A O   1 
ATOM   1101 C  CB  . GLN A 1 172 ? 27.055 118.752 -36.441  1.00 32.16  ? 174 GLN A CB  1 
ATOM   1102 C  CG  . GLN A 1 172 ? 27.263 117.659 -35.412  1.00 33.71  ? 174 GLN A CG  1 
ATOM   1103 C  CD  . GLN A 1 172 ? 25.944 116.975 -35.199  1.00 35.19  ? 174 GLN A CD  1 
ATOM   1104 O  OE1 . GLN A 1 172 ? 24.989 117.620 -34.772  1.00 34.40  ? 174 GLN A OE1 1 
ATOM   1105 N  NE2 . GLN A 1 172 ? 25.891 115.707 -35.584  1.00 35.24  ? 174 GLN A NE2 1 
ATOM   1106 N  N   . VAL A 1 173 ? 27.950 119.671 -39.157  1.00 29.15  ? 175 VAL A N   1 
ATOM   1107 C  CA  . VAL A 1 173 ? 27.766 120.324 -40.467  1.00 30.88  ? 175 VAL A CA  1 
ATOM   1108 C  C   . VAL A 1 173 ? 26.410 119.872 -40.997  1.00 33.61  ? 175 VAL A C   1 
ATOM   1109 O  O   . VAL A 1 173 ? 26.075 118.682 -40.835  1.00 34.10  ? 175 VAL A O   1 
ATOM   1110 C  CB  . VAL A 1 173 ? 28.936 119.967 -41.394  1.00 28.91  ? 175 VAL A CB  1 
ATOM   1111 C  CG1 . VAL A 1 173 ? 29.035 118.471 -41.628  1.00 28.82  ? 175 VAL A CG1 1 
ATOM   1112 C  CG2 . VAL A 1 173 ? 28.832 120.733 -42.683  1.00 28.75  ? 175 VAL A CG2 1 
ATOM   1113 N  N   . ARG A 1 174 ? 25.642 120.787 -41.574  1.00 37.15  ? 176 ARG A N   1 
ATOM   1114 C  CA  . ARG A 1 174 ? 24.365 120.383 -42.206  1.00 41.59  ? 176 ARG A CA  1 
ATOM   1115 C  C   . ARG A 1 174 ? 24.672 119.587 -43.475  1.00 42.52  ? 176 ARG A C   1 
ATOM   1116 O  O   . ARG A 1 174 ? 25.438 120.074 -44.331  1.00 40.05  ? 176 ARG A O   1 
ATOM   1117 C  CB  . ARG A 1 174 ? 23.446 121.557 -42.522  1.00 45.28  ? 176 ARG A CB  1 
ATOM   1118 C  CG  . ARG A 1 174 ? 21.983 121.138 -42.450  1.00 50.17  ? 176 ARG A CG  1 
ATOM   1119 C  CD  . ARG A 1 174 ? 21.021 122.256 -42.757  1.00 53.95  ? 176 ARG A CD  1 
ATOM   1120 N  NE  . ARG A 1 174 ? 21.165 122.613 -44.140  1.00 55.28  ? 176 ARG A NE  1 
ATOM   1121 C  CZ  . ARG A 1 174 ? 20.551 123.630 -44.730  1.00 61.99  ? 176 ARG A CZ  1 
ATOM   1122 N  NH1 . ARG A 1 174 ? 19.753 124.429 -44.036  1.00 62.99  ? 176 ARG A NH1 1 
ATOM   1123 N  NH2 . ARG A 1 174 ? 20.755 123.850 -46.024  1.00 63.23  ? 176 ARG A NH2 1 
ATOM   1124 N  N   . ALA A 1 175 ? 24.069 118.406 -43.573  1.00 44.21  ? 177 ALA A N   1 
ATOM   1125 C  CA  . ALA A 1 175 ? 24.346 117.424 -44.626  1.00 45.22  ? 177 ALA A CA  1 
ATOM   1126 C  C   . ALA A 1 175 ? 23.832 117.964 -45.968  1.00 48.39  ? 177 ALA A C   1 
ATOM   1127 O  O   . ALA A 1 175 ? 22.967 118.863 -45.996  1.00 45.41  ? 177 ALA A O   1 
ATOM   1128 C  CB  . ALA A 1 175 ? 23.743 116.097 -44.252  1.00 45.63  ? 177 ALA A CB  1 
ATOM   1129 N  N   . ASN A 1 176 ? 24.423 117.439 -47.040  1.00 53.91  ? 178 ASN A N   1 
ATOM   1130 C  CA  . ASN A 1 176 ? 24.050 117.691 -48.461  1.00 61.99  ? 178 ASN A CA  1 
ATOM   1131 C  C   . ASN A 1 176 ? 22.533 117.421 -48.614  1.00 65.14  ? 178 ASN A C   1 
ATOM   1132 O  O   . ASN A 1 176 ? 22.109 116.232 -48.510  1.00 62.18  ? 178 ASN A O   1 
ATOM   1133 C  CB  . ASN A 1 176 ? 24.970 116.859 -49.386  1.00 63.11  ? 178 ASN A CB  1 
ATOM   1134 C  CG  . ASN A 1 176 ? 25.244 117.435 -50.766  1.00 64.20  ? 178 ASN A CG  1 
ATOM   1135 O  OD1 . ASN A 1 176 ? 24.601 118.401 -51.198  1.00 69.13  ? 178 ASN A OD1 1 
ATOM   1136 N  ND2 . ASN A 1 176 ? 26.184 116.816 -51.480  1.00 56.21  ? 178 ASN A ND2 1 
ATOM   1137 N  N   . GLY A 1 177 ? 21.728 118.480 -48.789  1.00 67.71  ? 179 GLY A N   1 
ATOM   1138 C  CA  . GLY A 1 177 ? 20.303 118.383 -49.186  1.00 73.07  ? 179 GLY A CA  1 
ATOM   1139 C  C   . GLY A 1 177 ? 19.503 117.417 -48.320  1.00 77.09  ? 179 GLY A C   1 
ATOM   1140 O  O   . GLY A 1 177 ? 18.515 116.843 -48.798  1.00 80.59  ? 179 GLY A O   1 
ATOM   1141 N  N   . SER A 1 178 ? 19.900 117.257 -47.063  1.00 80.03  ? 180 SER A N   1 
ATOM   1142 C  CA  . SER A 1 178 ? 19.267 116.359 -46.060  1.00 78.68  ? 180 SER A CA  1 
ATOM   1143 C  C   . SER A 1 178 ? 18.654 117.224 -44.944  1.00 74.52  ? 180 SER A C   1 
ATOM   1144 O  O   . SER A 1 178 ? 17.696 116.770 -44.327  1.00 78.16  ? 180 SER A O   1 
ATOM   1145 C  CB  . SER A 1 178 ? 20.304 115.340 -45.580  1.00 76.73  ? 180 SER A CB  1 
ATOM   1146 O  OG  . SER A 1 178 ? 19.883 114.601 -44.442  1.00 73.46  ? 180 SER A OG  1 
ATOM   1147 N  N   . GLN A 1 179 ? 19.183 118.433 -44.715  1.00 71.82  ? 181 GLN A N   1 
ATOM   1148 C  CA  . GLN A 1 179 ? 18.666 119.493 -43.788  1.00 73.73  ? 181 GLN A CA  1 
ATOM   1149 C  C   . GLN A 1 179 ? 18.909 119.098 -42.322  1.00 69.86  ? 181 GLN A C   1 
ATOM   1150 O  O   . GLN A 1 179 ? 18.568 119.907 -41.441  1.00 72.94  ? 181 GLN A O   1 
ATOM   1151 C  CB  . GLN A 1 179 ? 17.187 119.851 -44.030  1.00 76.89  ? 181 GLN A CB  1 
ATOM   1152 C  CG  . GLN A 1 179 ? 16.966 120.735 -45.252  1.00 77.64  ? 181 GLN A CG  1 
ATOM   1153 C  CD  . GLN A 1 179 ? 17.416 120.071 -46.540  1.00 79.57  ? 181 GLN A CD  1 
ATOM   1154 O  OE1 . GLN A 1 179 ? 18.369 120.501 -47.197  1.00 78.31  ? 181 GLN A OE1 1 
ATOM   1155 N  NE2 . GLN A 1 179 ? 16.728 119.008 -46.930  1.00 77.47  ? 181 GLN A NE2 1 
ATOM   1156 N  N   . ASN A 1 180 ? 19.513 117.940 -42.048  1.00 63.11  ? 182 ASN A N   1 
ATOM   1157 C  CA  . ASN A 1 180 ? 19.921 117.588 -40.665  1.00 59.93  ? 182 ASN A CA  1 
ATOM   1158 C  C   . ASN A 1 180 ? 21.454 117.631 -40.555  1.00 51.34  ? 182 ASN A C   1 
ATOM   1159 O  O   . ASN A 1 180 ? 22.168 117.662 -41.584  1.00 50.39  ? 182 ASN A O   1 
ATOM   1160 C  CB  . ASN A 1 180 ? 19.255 116.295 -40.182  1.00 63.54  ? 182 ASN A CB  1 
ATOM   1161 C  CG  . ASN A 1 180 ? 19.571 115.093 -41.039  1.00 64.33  ? 182 ASN A CG  1 
ATOM   1162 O  OD1 . ASN A 1 180 ? 20.354 115.184 -41.981  1.00 66.00  ? 182 ASN A OD1 1 
ATOM   1163 N  ND2 . ASN A 1 180 ? 18.964 113.966 -40.709  1.00 65.47  ? 182 ASN A ND2 1 
ATOM   1164 N  N   . TYR A 1 181 ? 21.940 117.670 -39.323  1.00 45.03  ? 183 TYR A N   1 
ATOM   1165 C  CA  . TYR A 1 181 ? 23.360 117.895 -38.986  1.00 39.46  ? 183 TYR A CA  1 
ATOM   1166 C  C   . TYR A 1 181 ? 24.038 116.560 -38.763  1.00 37.40  ? 183 TYR A C   1 
ATOM   1167 O  O   . TYR A 1 181 ? 23.396 115.613 -38.337  1.00 39.50  ? 183 TYR A O   1 
ATOM   1168 C  CB  . TYR A 1 181 ? 23.465 118.811 -37.783  1.00 37.86  ? 183 TYR A CB  1 
ATOM   1169 C  CG  . TYR A 1 181 ? 23.104 120.213 -38.169  1.00 38.50  ? 183 TYR A CG  1 
ATOM   1170 C  CD1 . TYR A 1 181 ? 21.792 120.642 -38.229  1.00 39.78  ? 183 TYR A CD1 1 
ATOM   1171 C  CD2 . TYR A 1 181 ? 24.087 121.099 -38.548  1.00 37.74  ? 183 TYR A CD2 1 
ATOM   1172 C  CE1 . TYR A 1 181 ? 21.477 121.942 -38.588  1.00 41.10  ? 183 TYR A CE1 1 
ATOM   1173 C  CE2 . TYR A 1 181 ? 23.795 122.396 -38.930  1.00 38.83  ? 183 TYR A CE2 1 
ATOM   1174 C  CZ  . TYR A 1 181 ? 22.488 122.828 -38.929  1.00 41.97  ? 183 TYR A CZ  1 
ATOM   1175 O  OH  . TYR A 1 181 ? 22.290 124.132 -39.291  1.00 44.83  ? 183 TYR A OH  1 
ATOM   1176 N  N   . THR A 1 182 ? 25.323 116.510 -39.070  1.00 34.31  ? 184 THR A N   1 
ATOM   1177 C  CA  . THR A 1 182 ? 26.114 115.266 -39.060  1.00 33.04  ? 184 THR A CA  1 
ATOM   1178 C  C   . THR A 1 182 ? 27.593 115.625 -38.886  1.00 29.77  ? 184 THR A C   1 
ATOM   1179 O  O   . THR A 1 182 ? 27.933 116.819 -38.985  1.00 28.14  ? 184 THR A O   1 
ATOM   1180 C  CB  . THR A 1 182 ? 25.808 114.518 -40.359  1.00 34.84  ? 184 THR A CB  1 
ATOM   1181 O  OG1 . THR A 1 182 ? 26.410 113.232 -40.302  1.00 36.89  ? 184 THR A OG1 1 
ATOM   1182 C  CG2 . THR A 1 182 ? 26.317 115.251 -41.575  1.00 34.24  ? 184 THR A CG2 1 
ATOM   1183 N  N   . ALA A 1 183 ? 28.428 114.626 -38.619  1.00 27.98  ? 185 ALA A N   1 
ATOM   1184 C  CA  . ALA A 1 183 ? 29.858 114.823 -38.366  1.00 26.39  ? 185 ALA A CA  1 
ATOM   1185 C  C   . ALA A 1 183 ? 30.540 115.120 -39.694  1.00 25.80  ? 185 ALA A C   1 
ATOM   1186 O  O   . ALA A 1 183 ? 31.547 115.793 -39.683  1.00 25.75  ? 185 ALA A O   1 
ATOM   1187 C  CB  . ALA A 1 183 ? 30.438 113.618 -37.679  1.00 26.86  ? 185 ALA A CB  1 
ATOM   1188 N  N   . ALA A 1 184 ? 30.029 114.651 -40.819  1.00 26.57  ? 186 ALA A N   1 
ATOM   1189 C  CA  . ALA A 1 184 ? 30.714 114.904 -42.108  1.00 26.45  ? 186 ALA A CA  1 
ATOM   1190 C  C   . ALA A 1 184 ? 29.804 114.680 -43.308  1.00 26.85  ? 186 ALA A C   1 
ATOM   1191 O  O   . ALA A 1 184 ? 28.897 113.885 -43.213  1.00 28.89  ? 186 ALA A O   1 
ATOM   1192 C  CB  . ALA A 1 184 ? 31.953 114.041 -42.202  1.00 26.61  ? 186 ALA A CB  1 
ATOM   1193 N  N   . THR A 1 185 ? 30.074 115.383 -44.399  1.00 25.57  ? 187 THR A N   1 
ATOM   1194 C  CA  . THR A 1 185 ? 29.273 115.327 -45.634  1.00 26.51  ? 187 THR A CA  1 
ATOM   1195 C  C   . THR A 1 185 ? 30.152 115.700 -46.831  1.00 25.67  ? 187 THR A C   1 
ATOM   1196 O  O   . THR A 1 185 ? 31.381 115.873 -46.657  1.00 24.31  ? 187 THR A O   1 
ATOM   1197 C  CB  . THR A 1 185 ? 28.052 116.224 -45.429  1.00 27.83  ? 187 THR A CB  1 
ATOM   1198 O  OG1 . THR A 1 185 ? 27.062 115.874 -46.397  1.00 28.63  ? 187 THR A OG1 1 
ATOM   1199 C  CG2 . THR A 1 185 ? 28.392 117.688 -45.514  1.00 27.40  ? 187 THR A CG2 1 
ATOM   1200 N  N   . ASP A 1 186 ? 29.578 115.780 -48.029  1.00 26.32  ? 188 ASP A N   1 
ATOM   1201 C  CA  . ASP A 1 186 ? 30.339 116.244 -49.205  1.00 25.54  ? 188 ASP A CA  1 
ATOM   1202 C  C   . ASP A 1 186 ? 29.595 117.406 -49.839  1.00 26.60  ? 188 ASP A C   1 
ATOM   1203 O  O   . ASP A 1 186 ? 28.344 117.456 -49.802  1.00 29.40  ? 188 ASP A O   1 
ATOM   1204 C  CB  . ASP A 1 186 ? 30.710 115.117 -50.155  1.00 25.48  ? 188 ASP A CB  1 
ATOM   1205 C  CG  . ASP A 1 186 ? 29.605 114.219 -50.692  1.00 26.41  ? 188 ASP A CG  1 
ATOM   1206 O  OD1 . ASP A 1 186 ? 28.478 114.726 -51.083  1.00 27.12  ? 188 ASP A OD1 1 
ATOM   1207 O  OD2 . ASP A 1 186 ? 29.909 113.008 -50.766  1.00 25.96  ? 188 ASP A OD2 1 
ATOM   1208 N  N   . TYR A 1 187 ? 30.365 118.347 -50.343  1.00 26.02  ? 189 TYR A N   1 
ATOM   1209 C  CA  . TYR A 1 187 ? 29.831 119.529 -51.051  1.00 28.58  ? 189 TYR A CA  1 
ATOM   1210 C  C   . TYR A 1 187 ? 30.700 119.765 -52.280  1.00 27.75  ? 189 TYR A C   1 
ATOM   1211 O  O   . TYR A 1 187 ? 31.773 119.141 -52.386  1.00 27.16  ? 189 TYR A O   1 
ATOM   1212 C  CB  . TYR A 1 187 ? 29.770 120.761 -50.147  1.00 28.14  ? 189 TYR A CB  1 
ATOM   1213 C  CG  . TYR A 1 187 ? 28.554 120.840 -49.265  1.00 29.44  ? 189 TYR A CG  1 
ATOM   1214 C  CD1 . TYR A 1 187 ? 28.580 120.295 -47.994  1.00 29.98  ? 189 TYR A CD1 1 
ATOM   1215 C  CD2 . TYR A 1 187 ? 27.414 121.531 -49.644  1.00 30.96  ? 189 TYR A CD2 1 
ATOM   1216 C  CE1 . TYR A 1 187 ? 27.489 120.373 -47.148  1.00 30.40  ? 189 TYR A CE1 1 
ATOM   1217 C  CE2 . TYR A 1 187 ? 26.310 121.616 -48.809  1.00 31.79  ? 189 TYR A CE2 1 
ATOM   1218 C  CZ  . TYR A 1 187 ? 26.353 121.042 -47.553  1.00 31.71  ? 189 TYR A CZ  1 
ATOM   1219 O  OH  . TYR A 1 187 ? 25.312 121.096 -46.675  1.00 33.56  ? 189 TYR A OH  1 
ATOM   1220 N  N   . ARG A 1 188 ? 30.232 120.642 -53.156  1.00 28.98  ? 190 ARG A N   1 
ATOM   1221 C  CA  . ARG A 1 188 ? 31.014 121.168 -54.299  1.00 28.52  ? 190 ARG A CA  1 
ATOM   1222 C  C   . ARG A 1 188 ? 31.672 122.471 -53.865  1.00 27.14  ? 190 ARG A C   1 
ATOM   1223 O  O   . ARG A 1 188 ? 31.129 123.188 -52.989  1.00 26.66  ? 190 ARG A O   1 
ATOM   1224 C  CB  . ARG A 1 188 ? 30.141 121.390 -55.540  1.00 30.27  ? 190 ARG A CB  1 
ATOM   1225 C  CG  . ARG A 1 188 ? 29.476 120.109 -56.020  1.00 32.34  ? 190 ARG A CG  1 
ATOM   1226 C  CD  . ARG A 1 188 ? 28.932 120.164 -57.442  1.00 34.30  ? 190 ARG A CD  1 
ATOM   1227 N  NE  . ARG A 1 188 ? 27.845 121.126 -57.539  1.00 36.83  ? 190 ARG A NE  1 
ATOM   1228 C  CZ  . ARG A 1 188 ? 27.947 122.367 -58.018  1.00 37.77  ? 190 ARG A CZ  1 
ATOM   1229 N  NH1 . ARG A 1 188 ? 29.091 122.839 -58.486  1.00 36.67  ? 190 ARG A NH1 1 
ATOM   1230 N  NH2 . ARG A 1 188 ? 26.880 123.141 -58.047  1.00 40.12  ? 190 ARG A NH2 1 
ATOM   1231 N  N   . ILE A 1 189 ? 32.813 122.740 -54.470  1.00 26.62  ? 191 ILE A N   1 
ATOM   1232 C  CA  . ILE A 1 189 ? 33.556 124.013 -54.293  1.00 27.25  ? 191 ILE A CA  1 
ATOM   1233 C  C   . ILE A 1 189 ? 32.601 125.146 -54.678  1.00 29.51  ? 191 ILE A C   1 
ATOM   1234 O  O   . ILE A 1 189 ? 31.919 124.994 -55.686  1.00 28.65  ? 191 ILE A O   1 
ATOM   1235 C  CB  . ILE A 1 189 ? 34.873 124.037 -55.104  1.00 25.46  ? 191 ILE A CB  1 
ATOM   1236 C  CG1 . ILE A 1 189 ? 35.898 123.044 -54.534  1.00 24.41  ? 191 ILE A CG1 1 
ATOM   1237 C  CG2 . ILE A 1 189 ? 35.410 125.461 -55.162  1.00 25.36  ? 191 ILE A CG2 1 
ATOM   1238 C  CD1 . ILE A 1 189 ? 37.150 122.876 -55.370  1.00 24.20  ? 191 ILE A CD1 1 
ATOM   1239 N  N   . GLY A 1 190 ? 32.549 126.199 -53.851  1.00 31.30  ? 192 GLY A N   1 
ATOM   1240 C  CA  . GLY A 1 190 ? 31.765 127.417 -54.101  1.00 33.02  ? 192 GLY A CA  1 
ATOM   1241 C  C   . GLY A 1 190 ? 30.409 127.352 -53.431  1.00 35.70  ? 192 GLY A C   1 
ATOM   1242 O  O   . GLY A 1 190 ? 29.818 128.416 -53.333  1.00 40.83  ? 192 GLY A O   1 
ATOM   1243 N  N   . GLN A 1 191 ? 29.923 126.176 -52.997  1.00 35.10  ? 193 GLN A N   1 
ATOM   1244 C  CA  . GLN A 1 191 ? 28.604 126.032 -52.329  1.00 36.87  ? 193 GLN A CA  1 
ATOM   1245 C  C   . GLN A 1 191 ? 28.741 126.429 -50.840  1.00 36.06  ? 193 GLN A C   1 
ATOM   1246 O  O   . GLN A 1 191 ? 29.722 126.001 -50.174  1.00 34.29  ? 193 GLN A O   1 
ATOM   1247 C  CB  . GLN A 1 191 ? 28.079 124.606 -52.474  1.00 39.94  ? 193 GLN A CB  1 
ATOM   1248 C  CG  . GLN A 1 191 ? 27.459 124.283 -53.835  1.00 44.65  ? 193 GLN A CG  1 
ATOM   1249 C  CD  . GLN A 1 191 ? 26.964 122.845 -53.906  1.00 48.38  ? 193 GLN A CD  1 
ATOM   1250 O  OE1 . GLN A 1 191 ? 27.265 121.989 -53.059  1.00 48.84  ? 193 GLN A OE1 1 
ATOM   1251 N  NE2 . GLN A 1 191 ? 26.188 122.545 -54.942  1.00 53.38  ? 193 GLN A NE2 1 
ATOM   1252 N  N   . ASN A 1 192 ? 27.794 127.228 -50.340  1.00 36.16  ? 194 ASN A N   1 
ATOM   1253 C  CA  . ASN A 1 192 ? 27.737 127.711 -48.932  1.00 35.64  ? 194 ASN A CA  1 
ATOM   1254 C  C   . ASN A 1 192 ? 27.249 126.575 -48.017  1.00 34.14  ? 194 ASN A C   1 
ATOM   1255 O  O   . ASN A 1 192 ? 26.282 125.902 -48.328  1.00 35.45  ? 194 ASN A O   1 
ATOM   1256 C  CB  . ASN A 1 192 ? 26.876 128.965 -48.795  1.00 36.54  ? 194 ASN A CB  1 
ATOM   1257 C  CG  . ASN A 1 192 ? 27.546 130.194 -49.367  1.00 37.25  ? 194 ASN A CG  1 
ATOM   1258 O  OD1 . ASN A 1 192 ? 28.764 130.374 -49.289  1.00 36.55  ? 194 ASN A OD1 1 
ATOM   1259 N  ND2 . ASN A 1 192 ? 26.748 131.053 -49.971  1.00 39.75  ? 194 ASN A ND2 1 
ATOM   1260 N  N   . ILE A 1 193 ? 27.949 126.330 -46.931  1.00 32.60  ? 195 ILE A N   1 
ATOM   1261 C  CA  . ILE A 1 193 ? 27.715 125.133 -46.084  1.00 32.02  ? 195 ILE A CA  1 
ATOM   1262 C  C   . ILE A 1 193 ? 27.397 125.624 -44.670  1.00 30.93  ? 195 ILE A C   1 
ATOM   1263 O  O   . ILE A 1 193 ? 28.119 126.504 -44.172  1.00 28.58  ? 195 ILE A O   1 
ATOM   1264 C  CB  . ILE A 1 193 ? 28.923 124.190 -46.104  1.00 30.81  ? 195 ILE A CB  1 
ATOM   1265 C  CG1 . ILE A 1 193 ? 29.319 123.814 -47.537  1.00 31.89  ? 195 ILE A CG1 1 
ATOM   1266 C  CG2 . ILE A 1 193 ? 28.623 122.987 -45.217  1.00 30.79  ? 195 ILE A CG2 1 
ATOM   1267 C  CD1 . ILE A 1 193 ? 30.692 123.163 -47.651  1.00 31.51  ? 195 ILE A CD1 1 
ATOM   1268 N  N   . LEU A 1 194 ? 26.322 125.106 -44.104  1.00 32.26  ? 196 LEU A N   1 
ATOM   1269 C  CA  . LEU A 1 194 ? 25.813 125.548 -42.787  1.00 34.93  ? 196 LEU A CA  1 
ATOM   1270 C  C   . LEU A 1 194 ? 26.434 124.684 -41.709  1.00 31.54  ? 196 LEU A C   1 
ATOM   1271 O  O   . LEU A 1 194 ? 26.326 123.449 -41.778  1.00 29.90  ? 196 LEU A O   1 
ATOM   1272 C  CB  . LEU A 1 194 ? 24.297 125.403 -42.803  1.00 40.28  ? 196 LEU A CB  1 
ATOM   1273 C  CG  . LEU A 1 194 ? 23.557 126.118 -41.684  1.00 44.86  ? 196 LEU A CG  1 
ATOM   1274 C  CD1 . LEU A 1 194 ? 23.690 127.637 -41.784  1.00 47.45  ? 196 LEU A CD1 1 
ATOM   1275 C  CD2 . LEU A 1 194 ? 22.097 125.698 -41.721  1.00 47.38  ? 196 LEU A CD2 1 
ATOM   1276 N  N   . PHE A 1 195 ? 27.041 125.344 -40.731  1.00 31.11  ? 197 PHE A N   1 
ATOM   1277 C  CA  . PHE A 1 195 ? 27.704 124.697 -39.575  1.00 28.41  ? 197 PHE A CA  1 
ATOM   1278 C  C   . PHE A 1 195 ? 26.975 125.089 -38.282  1.00 29.22  ? 197 PHE A C   1 
ATOM   1279 O  O   . PHE A 1 195 ? 26.320 126.169 -38.155  1.00 28.25  ? 197 PHE A O   1 
ATOM   1280 C  CB  . PHE A 1 195 ? 29.181 125.081 -39.547  1.00 26.27  ? 197 PHE A CB  1 
ATOM   1281 C  CG  . PHE A 1 195 ? 29.995 124.413 -40.620  1.00 24.44  ? 197 PHE A CG  1 
ATOM   1282 C  CD1 . PHE A 1 195 ? 30.540 123.164 -40.406  1.00 23.25  ? 197 PHE A CD1 1 
ATOM   1283 C  CD2 . PHE A 1 195 ? 30.177 125.019 -41.840  1.00 24.25  ? 197 PHE A CD2 1 
ATOM   1284 C  CE1 . PHE A 1 195 ? 31.273 122.531 -41.381  1.00 23.27  ? 197 PHE A CE1 1 
ATOM   1285 C  CE2 . PHE A 1 195 ? 30.934 124.403 -42.817  1.00 23.52  ? 197 PHE A CE2 1 
ATOM   1286 C  CZ  . PHE A 1 195 ? 31.469 123.152 -42.594  1.00 23.28  ? 197 PHE A CZ  1 
ATOM   1287 N  N   . GLN A 1 196 ? 27.093 124.203 -37.307  1.00 29.59  ? 198 GLN A N   1 
ATOM   1288 C  CA  . GLN A 1 196 ? 26.428 124.421 -36.008  1.00 30.69  ? 198 GLN A CA  1 
ATOM   1289 C  C   . GLN A 1 196 ? 27.296 123.904 -34.867  1.00 29.26  ? 198 GLN A C   1 
ATOM   1290 O  O   . GLN A 1 196 ? 27.759 122.762 -34.934  1.00 28.16  ? 198 GLN A O   1 
ATOM   1291 C  CB  . GLN A 1 196 ? 25.087 123.739 -36.052  1.00 32.88  ? 198 GLN A CB  1 
ATOM   1292 C  CG  . GLN A 1 196 ? 24.246 124.065 -34.847  1.00 36.41  ? 198 GLN A CG  1 
ATOM   1293 C  CD  . GLN A 1 196 ? 22.955 123.315 -34.974  1.00 38.50  ? 198 GLN A CD  1 
ATOM   1294 O  OE1 . GLN A 1 196 ? 21.913 123.929 -35.239  1.00 41.09  ? 198 GLN A OE1 1 
ATOM   1295 N  NE2 . GLN A 1 196 ? 23.076 121.993 -34.885  1.00 37.66  ? 198 GLN A NE2 1 
ATOM   1296 N  N   . ILE A 1 197 ? 27.519 124.770 -33.884  1.00 29.03  ? 199 ILE A N   1 
ATOM   1297 C  CA  . ILE A 1 197 ? 28.237 124.437 -32.633  1.00 29.27  ? 199 ILE A CA  1 
ATOM   1298 C  C   . ILE A 1 197 ? 27.248 124.587 -31.474  1.00 29.48  ? 199 ILE A C   1 
ATOM   1299 O  O   . ILE A 1 197 ? 26.634 125.642 -31.355  1.00 29.12  ? 199 ILE A O   1 
ATOM   1300 C  CB  . ILE A 1 197 ? 29.485 125.306 -32.478  1.00 29.12  ? 199 ILE A CB  1 
ATOM   1301 C  CG1 . ILE A 1 197 ? 30.475 125.072 -33.621  1.00 28.77  ? 199 ILE A CG1 1 
ATOM   1302 C  CG2 . ILE A 1 197 ? 30.135 125.029 -31.148  1.00 30.49  ? 199 ILE A CG2 1 
ATOM   1303 C  CD1 . ILE A 1 197 ? 31.578 126.125 -33.691  1.00 28.21  ? 199 ILE A CD1 1 
ATOM   1304 N  N   . THR A 1 198 ? 27.081 123.520 -30.700  1.00 29.24  ? 200 THR A N   1 
ATOM   1305 C  CA  . THR A 1 198 ? 26.149 123.424 -29.555  1.00 30.86  ? 200 THR A CA  1 
ATOM   1306 C  C   . THR A 1 198 ? 26.951 123.315 -28.251  1.00 30.32  ? 200 THR A C   1 
ATOM   1307 O  O   . THR A 1 198 ? 27.662 122.300 -28.055  1.00 30.28  ? 200 THR A O   1 
ATOM   1308 C  CB  . THR A 1 198 ? 25.222 122.235 -29.807  1.00 32.14  ? 200 THR A CB  1 
ATOM   1309 O  OG1 . THR A 1 198 ? 24.416 122.712 -30.887  1.00 33.61  ? 200 THR A OG1 1 
ATOM   1310 C  CG2 . THR A 1 198 ? 24.413 121.798 -28.605  1.00 33.51  ? 200 THR A CG2 1 
ATOM   1311 N  N   . ALA A 1 199 ? 26.835 124.300 -27.367  1.00 30.32  ? 201 ALA A N   1 
ATOM   1312 C  CA  . ALA A 1 199 ? 27.431 124.236 -26.005  1.00 29.13  ? 201 ALA A CA  1 
ATOM   1313 C  C   . ALA A 1 199 ? 26.330 123.892 -25.012  1.00 29.98  ? 201 ALA A C   1 
ATOM   1314 O  O   . ALA A 1 199 ? 25.307 124.566 -25.029  1.00 31.51  ? 201 ALA A O   1 
ATOM   1315 C  CB  . ALA A 1 199 ? 28.090 125.531 -25.654  1.00 27.75  ? 201 ALA A CB  1 
ATOM   1316 N  N   . THR A 1 200 ? 26.499 122.840 -24.226  1.00 30.40  ? 202 THR A N   1 
ATOM   1317 C  CA  . THR A 1 200 ? 25.707 122.621 -22.983  1.00 31.42  ? 202 THR A CA  1 
ATOM   1318 C  C   . THR A 1 200 ? 26.478 123.246 -21.807  1.00 30.89  ? 202 THR A C   1 
ATOM   1319 O  O   . THR A 1 200 ? 27.729 123.330 -21.867  1.00 30.68  ? 202 THR A O   1 
ATOM   1320 C  CB  . THR A 1 200 ? 25.416 121.129 -22.773  1.00 32.05  ? 202 THR A CB  1 
ATOM   1321 O  OG1 . THR A 1 200 ? 26.663 120.520 -22.419  1.00 31.99  ? 202 THR A OG1 1 
ATOM   1322 C  CG2 . THR A 1 200 ? 24.841 120.449 -24.002  1.00 33.49  ? 202 THR A CG2 1 
ATOM   1323 N  N   . LEU A 1 201 ? 25.779 123.623 -20.742  1.00 31.24  ? 203 LEU A N   1 
ATOM   1324 C  CA  . LEU A 1 201 ? 26.405 124.223 -19.535  1.00 30.54  ? 203 LEU A CA  1 
ATOM   1325 C  C   . LEU A 1 201 ? 26.472 123.159 -18.446  1.00 29.99  ? 203 LEU A C   1 
ATOM   1326 O  O   . LEU A 1 201 ? 25.778 122.167 -18.495  1.00 31.56  ? 203 LEU A O   1 
ATOM   1327 C  CB  . LEU A 1 201 ? 25.611 125.470 -19.143  1.00 31.48  ? 203 LEU A CB  1 
ATOM   1328 C  CG  . LEU A 1 201 ? 25.608 126.567 -20.206  1.00 32.47  ? 203 LEU A CG  1 
ATOM   1329 C  CD1 . LEU A 1 201 ? 24.790 127.764 -19.793  1.00 33.36  ? 203 LEU A CD1 1 
ATOM   1330 C  CD2 . LEU A 1 201 ? 27.021 127.008 -20.493  1.00 32.60  ? 203 LEU A CD2 1 
ATOM   1331 N  N   . PRO A 1 202 ? 27.383 123.266 -17.475  1.00 28.85  ? 204 PRO A N   1 
ATOM   1332 C  CA  . PRO A 1 202 ? 27.502 122.244 -16.438  1.00 29.51  ? 204 PRO A CA  1 
ATOM   1333 C  C   . PRO A 1 202 ? 26.329 122.325 -15.445  1.00 30.83  ? 204 PRO A C   1 
ATOM   1334 O  O   . PRO A 1 202 ? 25.792 123.435 -15.274  1.00 30.18  ? 204 PRO A O   1 
ATOM   1335 C  CB  . PRO A 1 202 ? 28.815 122.657 -15.768  1.00 29.08  ? 204 PRO A CB  1 
ATOM   1336 C  CG  . PRO A 1 202 ? 28.798 124.162 -15.887  1.00 28.52  ? 204 PRO A CG  1 
ATOM   1337 C  CD  . PRO A 1 202 ? 28.287 124.403 -17.286  1.00 28.38  ? 204 PRO A CD  1 
ATOM   1338 N  N   . SER A 1 203 ? 25.950 121.188 -14.824  1.00 31.86  ? 205 SER A N   1 
ATOM   1339 C  CA  . SER A 1 203 ? 24.791 121.086 -13.873  1.00 33.21  ? 205 SER A CA  1 
ATOM   1340 C  C   . SER A 1 203 ? 24.953 122.093 -12.723  1.00 31.87  ? 205 SER A C   1 
ATOM   1341 O  O   . SER A 1 203 ? 23.916 122.531 -12.235  1.00 33.42  ? 205 SER A O   1 
ATOM   1342 C  CB  . SER A 1 203 ? 24.567 119.687 -13.345  1.00 33.36  ? 205 SER A CB  1 
ATOM   1343 O  OG  . SER A 1 203 ? 25.718 119.232 -12.654  1.00 32.86  ? 205 SER A OG  1 
ATOM   1344 N  N   . ASN A 1 204 ? 26.187 122.506 -12.369  1.00 29.74  ? 206 ASN A N   1 
ATOM   1345 C  CA  . ASN A 1 204 ? 26.445 123.498 -11.279  1.00 28.09  ? 206 ASN A CA  1 
ATOM   1346 C  C   . ASN A 1 204 ? 26.729 124.889 -11.853  1.00 27.35  ? 206 ASN A C   1 
ATOM   1347 O  O   . ASN A 1 204 ? 27.439 125.629 -11.209  1.00 27.06  ? 206 ASN A O   1 
ATOM   1348 C  CB  . ASN A 1 204 ? 27.565 123.038 -10.338  1.00 26.39  ? 206 ASN A CB  1 
ATOM   1349 C  CG  . ASN A 1 204 ? 28.877 122.738 -11.025  1.00 25.30  ? 206 ASN A CG  1 
ATOM   1350 O  OD1 . ASN A 1 204 ? 28.939 122.700 -12.266  1.00 24.28  ? 206 ASN A OD1 1 
ATOM   1351 N  ND2 . ASN A 1 204 ? 29.920 122.491 -10.242  1.00 23.47  ? 206 ASN A ND2 1 
ATOM   1352 N  N   . TYR A 1 205 ? 26.163 125.248 -13.000  1.00 28.15  ? 207 TYR A N   1 
ATOM   1353 C  CA  . TYR A 1 205 ? 26.371 126.600 -13.583  1.00 28.72  ? 207 TYR A CA  1 
ATOM   1354 C  C   . TYR A 1 205 ? 26.087 127.698 -12.539  1.00 30.15  ? 207 TYR A C   1 
ATOM   1355 O  O   . TYR A 1 205 ? 26.852 128.687 -12.449  1.00 30.23  ? 207 TYR A O   1 
ATOM   1356 C  CB  . TYR A 1 205 ? 25.521 126.783 -14.826  1.00 29.02  ? 207 TYR A CB  1 
ATOM   1357 C  CG  . TYR A 1 205 ? 25.664 128.120 -15.501  1.00 29.10  ? 207 TYR A CG  1 
ATOM   1358 C  CD1 . TYR A 1 205 ? 26.789 128.459 -16.234  1.00 28.53  ? 207 TYR A CD1 1 
ATOM   1359 C  CD2 . TYR A 1 205 ? 24.614 129.010 -15.494  1.00 29.41  ? 207 TYR A CD2 1 
ATOM   1360 C  CE1 . TYR A 1 205 ? 26.899 129.692 -16.866  1.00 28.78  ? 207 TYR A CE1 1 
ATOM   1361 C  CE2 . TYR A 1 205 ? 24.700 130.235 -16.128  1.00 30.53  ? 207 TYR A CE2 1 
ATOM   1362 C  CZ  . TYR A 1 205 ? 25.843 130.590 -16.824  1.00 30.36  ? 207 TYR A CZ  1 
ATOM   1363 O  OH  . TYR A 1 205 ? 25.864 131.827 -17.433  1.00 31.59  ? 207 TYR A OH  1 
ATOM   1364 N  N   . ALA A 1 206 ? 25.031 127.551 -11.741  1.00 31.71  ? 208 ALA A N   1 
ATOM   1365 C  CA  . ALA A 1 206 ? 24.596 128.607 -10.794  1.00 32.31  ? 208 ALA A CA  1 
ATOM   1366 C  C   . ALA A 1 206 ? 25.610 128.721 -9.636   1.00 31.75  ? 208 ALA A C   1 
ATOM   1367 O  O   . ALA A 1 206 ? 25.611 129.775 -8.979   1.00 32.89  ? 208 ALA A O   1 
ATOM   1368 C  CB  . ALA A 1 206 ? 23.182 128.344 -10.322  1.00 32.99  ? 208 ALA A CB  1 
ATOM   1369 N  N   . ASP A 1 207 ? 26.477 127.727 -9.417   1.00 31.36  ? 209 ASP A N   1 
ATOM   1370 C  CA  . ASP A 1 207 ? 27.500 127.761 -8.334   1.00 32.53  ? 209 ASP A CA  1 
ATOM   1371 C  C   . ASP A 1 207 ? 28.657 128.708 -8.700   1.00 30.70  ? 209 ASP A C   1 
ATOM   1372 O  O   . ASP A 1 207 ? 29.497 128.967 -7.851   1.00 30.47  ? 209 ASP A O   1 
ATOM   1373 C  CB  . ASP A 1 207 ? 28.047 126.364 -8.014   1.00 34.75  ? 209 ASP A CB  1 
ATOM   1374 C  CG  . ASP A 1 207 ? 27.068 125.421 -7.309   1.00 38.07  ? 209 ASP A CG  1 
ATOM   1375 O  OD1 . ASP A 1 207 ? 26.012 125.889 -6.832   1.00 36.79  ? 209 ASP A OD1 1 
ATOM   1376 O  OD2 . ASP A 1 207 ? 27.387 124.200 -7.230   1.00 42.09  ? 209 ASP A OD2 1 
ATOM   1377 N  N   . PHE A 1 208 ? 28.749 129.171 -9.945   1.00 29.46  ? 210 PHE A N   1 
ATOM   1378 C  CA  . PHE A 1 208 ? 29.797 130.128 -10.411  1.00 27.17  ? 210 PHE A CA  1 
ATOM   1379 C  C   . PHE A 1 208 ? 29.272 131.555 -10.194  1.00 28.14  ? 210 PHE A C   1 
ATOM   1380 O  O   . PHE A 1 208 ? 28.089 131.840 -10.416  1.00 27.88  ? 210 PHE A O   1 
ATOM   1381 C  CB  . PHE A 1 208 ? 30.178 129.865 -11.887  1.00 24.89  ? 210 PHE A CB  1 
ATOM   1382 C  CG  . PHE A 1 208 ? 30.933 128.576 -12.088  1.00 22.20  ? 210 PHE A CG  1 
ATOM   1383 C  CD1 . PHE A 1 208 ? 30.284 127.356 -12.023  1.00 22.08  ? 210 PHE A CD1 1 
ATOM   1384 C  CD2 . PHE A 1 208 ? 32.296 128.580 -12.226  1.00 20.24  ? 210 PHE A CD2 1 
ATOM   1385 C  CE1 . PHE A 1 208 ? 30.983 126.167 -12.121  1.00 21.27  ? 210 PHE A CE1 1 
ATOM   1386 C  CE2 . PHE A 1 208 ? 32.988 127.389 -12.336  1.00 20.25  ? 210 PHE A CE2 1 
ATOM   1387 C  CZ  . PHE A 1 208 ? 32.329 126.185 -12.306  1.00 20.63  ? 210 PHE A CZ  1 
ATOM   1388 N  N   . THR A 1 209 ? 30.165 132.440 -9.798   1.00 29.06  ? 211 THR A N   1 
ATOM   1389 C  CA  . THR A 1 209 ? 29.920 133.895 -9.729   1.00 30.36  ? 211 THR A CA  1 
ATOM   1390 C  C   . THR A 1 209 ? 30.131 134.520 -11.117  1.00 29.78  ? 211 THR A C   1 
ATOM   1391 O  O   . THR A 1 209 ? 29.454 135.487 -11.471  1.00 29.73  ? 211 THR A O   1 
ATOM   1392 C  CB  . THR A 1 209 ? 30.848 134.460 -8.653   1.00 31.96  ? 211 THR A CB  1 
ATOM   1393 O  OG1 . THR A 1 209 ? 30.220 135.686 -8.314   1.00 39.87  ? 211 THR A OG1 1 
ATOM   1394 C  CG2 . THR A 1 209 ? 32.289 134.727 -9.041   1.00 31.00  ? 211 THR A CG2 1 
ATOM   1395 N  N   . ARG A 1 210 ? 31.141 134.015 -11.818  1.00 29.80  ? 212 ARG A N   1 
ATOM   1396 C  CA  . ARG A 1 210 ? 31.587 134.400 -13.197  1.00 28.98  ? 212 ARG A CA  1 
ATOM   1397 C  C   . ARG A 1 210 ? 31.859 133.115 -13.982  1.00 26.32  ? 212 ARG A C   1 
ATOM   1398 O  O   . ARG A 1 210 ? 32.305 132.135 -13.396  1.00 24.14  ? 212 ARG A O   1 
ATOM   1399 C  CB  . ARG A 1 210 ? 32.806 135.312 -13.027  1.00 30.34  ? 212 ARG A CB  1 
ATOM   1400 C  CG  . ARG A 1 210 ? 33.877 135.242 -14.107  1.00 31.01  ? 212 ARG A CG  1 
ATOM   1401 C  CD  . ARG A 1 210 ? 34.951 136.218 -13.651  1.00 32.08  ? 212 ARG A CD  1 
ATOM   1402 N  NE  . ARG A 1 210 ? 36.100 136.431 -14.509  1.00 32.32  ? 212 ARG A NE  1 
ATOM   1403 C  CZ  . ARG A 1 210 ? 37.052 135.531 -14.741  1.00 33.18  ? 212 ARG A CZ  1 
ATOM   1404 N  NH1 . ARG A 1 210 ? 36.986 134.333 -14.190  1.00 33.43  ? 212 ARG A NH1 1 
ATOM   1405 N  NH2 . ARG A 1 210 ? 38.075 135.835 -15.517  1.00 33.08  ? 212 ARG A NH2 1 
ATOM   1406 N  N   . TYR A 1 211 ? 31.632 133.114 -15.292  1.00 25.75  ? 213 TYR A N   1 
ATOM   1407 C  CA  . TYR A 1 211 ? 31.810 131.894 -16.109  1.00 24.14  ? 213 TYR A CA  1 
ATOM   1408 C  C   . TYR A 1 211 ? 32.440 132.295 -17.427  1.00 25.46  ? 213 TYR A C   1 
ATOM   1409 O  O   . TYR A 1 211 ? 31.737 132.780 -18.281  1.00 25.07  ? 213 TYR A O   1 
ATOM   1410 C  CB  . TYR A 1 211 ? 30.488 131.164 -16.293  1.00 22.75  ? 213 TYR A CB  1 
ATOM   1411 C  CG  . TYR A 1 211 ? 30.670 129.723 -16.656  1.00 21.37  ? 213 TYR A CG  1 
ATOM   1412 C  CD1 . TYR A 1 211 ? 30.904 128.754 -15.700  1.00 20.80  ? 213 TYR A CD1 1 
ATOM   1413 C  CD2 . TYR A 1 211 ? 30.596 129.327 -17.975  1.00 21.16  ? 213 TYR A CD2 1 
ATOM   1414 C  CE1 . TYR A 1 211 ? 31.073 127.423 -16.050  1.00 20.38  ? 213 TYR A CE1 1 
ATOM   1415 C  CE2 . TYR A 1 211 ? 30.712 127.998 -18.339  1.00 20.44  ? 213 TYR A CE2 1 
ATOM   1416 C  CZ  . TYR A 1 211 ? 30.997 127.049 -17.384  1.00 20.27  ? 213 TYR A CZ  1 
ATOM   1417 O  OH  . TYR A 1 211 ? 31.157 125.769 -17.820  1.00 19.35  ? 213 TYR A OH  1 
ATOM   1418 N  N   . GLU A 1 212 ? 33.762 132.172 -17.513  1.00 27.25  ? 214 GLU A N   1 
ATOM   1419 C  CA  . GLU A 1 212 ? 34.500 132.425 -18.758  1.00 28.69  ? 214 GLU A CA  1 
ATOM   1420 C  C   . GLU A 1 212 ? 34.024 131.379 -19.738  1.00 27.61  ? 214 GLU A C   1 
ATOM   1421 O  O   . GLU A 1 212 ? 33.862 130.201 -19.333  1.00 28.30  ? 214 GLU A O   1 
ATOM   1422 C  CB  . GLU A 1 212 ? 36.007 132.308 -18.593  1.00 31.48  ? 214 GLU A CB  1 
ATOM   1423 C  CG  . GLU A 1 212 ? 36.544 133.269 -17.556  1.00 34.76  ? 214 GLU A CG  1 
ATOM   1424 C  CD  . GLU A 1 212 ? 38.027 133.504 -17.741  1.00 38.27  ? 214 GLU A CD  1 
ATOM   1425 O  OE1 . GLU A 1 212 ? 38.399 133.909 -18.872  1.00 42.11  ? 214 GLU A OE1 1 
ATOM   1426 O  OE2 . GLU A 1 212 ? 38.810 133.255 -16.775  1.00 40.49  ? 214 GLU A OE2 1 
ATOM   1427 N  N   . PHE A 1 213 ? 33.764 131.842 -20.947  1.00 25.97  ? 215 PHE A N   1 
ATOM   1428 C  CA  . PHE A 1 213 ? 33.181 131.048 -22.040  1.00 25.22  ? 215 PHE A CA  1 
ATOM   1429 C  C   . PHE A 1 213 ? 33.768 131.569 -23.351  1.00 24.75  ? 215 PHE A C   1 
ATOM   1430 O  O   . PHE A 1 213 ? 33.464 132.731 -23.739  1.00 25.55  ? 215 PHE A O   1 
ATOM   1431 C  CB  . PHE A 1 213 ? 31.668 131.191 -21.947  1.00 25.75  ? 215 PHE A CB  1 
ATOM   1432 C  CG  . PHE A 1 213 ? 30.888 130.339 -22.905  1.00 25.63  ? 215 PHE A CG  1 
ATOM   1433 C  CD1 . PHE A 1 213 ? 30.636 130.782 -24.199  1.00 25.27  ? 215 PHE A CD1 1 
ATOM   1434 C  CD2 . PHE A 1 213 ? 30.406 129.100 -22.506  1.00 25.28  ? 215 PHE A CD2 1 
ATOM   1435 C  CE1 . PHE A 1 213 ? 29.873 130.016 -25.064  1.00 25.43  ? 215 PHE A CE1 1 
ATOM   1436 C  CE2 . PHE A 1 213 ? 29.650 128.328 -23.384  1.00 25.41  ? 215 PHE A CE2 1 
ATOM   1437 C  CZ  . PHE A 1 213 ? 29.398 128.786 -24.662  1.00 25.38  ? 215 PHE A CZ  1 
ATOM   1438 N  N   . THR A 1 214 ? 34.615 130.761 -23.989  1.00 22.76  ? 216 THR A N   1 
ATOM   1439 C  CA  . THR A 1 214 ? 35.248 131.139 -25.261  1.00 22.17  ? 216 THR A CA  1 
ATOM   1440 C  C   . THR A 1 214 ? 35.289 129.931 -26.175  1.00 21.77  ? 216 THR A C   1 
ATOM   1441 O  O   . THR A 1 214 ? 35.942 128.940 -25.839  1.00 21.61  ? 216 THR A O   1 
ATOM   1442 C  CB  . THR A 1 214 ? 36.660 131.669 -25.033  1.00 21.71  ? 216 THR A CB  1 
ATOM   1443 O  OG1 . THR A 1 214 ? 36.564 132.763 -24.122  1.00 20.86  ? 216 THR A OG1 1 
ATOM   1444 C  CG2 . THR A 1 214 ? 37.305 132.086 -26.332  1.00 21.41  ? 216 THR A CG2 1 
ATOM   1445 N  N   . ILE A 1 215 ? 34.576 130.003 -27.277  1.00 22.13  ? 217 ILE A N   1 
ATOM   1446 C  CA  . ILE A 1 215 ? 34.669 128.962 -28.326  1.00 22.51  ? 217 ILE A CA  1 
ATOM   1447 C  C   . ILE A 1 215 ? 35.676 129.459 -29.342  1.00 22.87  ? 217 ILE A C   1 
ATOM   1448 O  O   . ILE A 1 215 ? 35.527 130.606 -29.801  1.00 23.12  ? 217 ILE A O   1 
ATOM   1449 C  CB  . ILE A 1 215 ? 33.304 128.722 -28.947  1.00 23.54  ? 217 ILE A CB  1 
ATOM   1450 C  CG1 . ILE A 1 215 ? 32.338 128.152 -27.907  1.00 24.45  ? 217 ILE A CG1 1 
ATOM   1451 C  CG2 . ILE A 1 215 ? 33.420 127.854 -30.205  1.00 24.42  ? 217 ILE A CG2 1 
ATOM   1452 C  CD1 . ILE A 1 215 ? 30.872 128.352 -28.259  1.00 25.00  ? 217 ILE A CD1 1 
ATOM   1453 N  N   . LYS A 1 216 ? 36.676 128.632 -29.625  1.00 23.42  ? 218 LYS A N   1 
ATOM   1454 C  CA  . LYS A 1 216 ? 37.597 128.810 -30.766  1.00 23.11  ? 218 LYS A CA  1 
ATOM   1455 C  C   . LYS A 1 216 ? 37.320 127.732 -31.789  1.00 22.03  ? 218 LYS A C   1 
ATOM   1456 O  O   . LYS A 1 216 ? 37.321 126.549 -31.408  1.00 20.94  ? 218 LYS A O   1 
ATOM   1457 C  CB  . LYS A 1 216 ? 39.014 128.689 -30.245  1.00 25.46  ? 218 LYS A CB  1 
ATOM   1458 C  CG  . LYS A 1 216 ? 39.558 130.013 -29.767  1.00 28.57  ? 218 LYS A CG  1 
ATOM   1459 C  CD  . LYS A 1 216 ? 40.901 129.890 -29.106  1.00 32.26  ? 218 LYS A CD  1 
ATOM   1460 C  CE  . LYS A 1 216 ? 41.201 131.112 -28.265  1.00 36.36  ? 218 LYS A CE  1 
ATOM   1461 N  NZ  . LYS A 1 216 ? 40.788 132.344 -28.998  1.00 40.12  ? 218 LYS A NZ  1 
ATOM   1462 N  N   . ASP A 1 217 ? 37.088 128.174 -33.029  1.00 21.18  ? 219 ASP A N   1 
ATOM   1463 C  CA  . ASP A 1 217 ? 36.767 127.347 -34.221  1.00 20.17  ? 219 ASP A CA  1 
ATOM   1464 C  C   . ASP A 1 217 ? 37.823 127.580 -35.309  1.00 19.21  ? 219 ASP A C   1 
ATOM   1465 O  O   . ASP A 1 217 ? 37.932 128.667 -35.797  1.00 18.54  ? 219 ASP A O   1 
ATOM   1466 C  CB  . ASP A 1 217 ? 35.339 127.629 -34.678  1.00 20.90  ? 219 ASP A CB  1 
ATOM   1467 C  CG  . ASP A 1 217 ? 34.776 126.718 -35.756  1.00 21.37  ? 219 ASP A CG  1 
ATOM   1468 O  OD1 . ASP A 1 217 ? 35.341 125.707 -36.036  1.00 22.42  ? 219 ASP A OD1 1 
ATOM   1469 O  OD2 . ASP A 1 217 ? 33.753 127.043 -36.266  1.00 20.65  ? 219 ASP A OD2 1 
ATOM   1470 N  N   . THR A 1 218 ? 38.588 126.551 -35.620  1.00 18.23  ? 220 THR A N   1 
ATOM   1471 C  CA  . THR A 1 218 ? 39.650 126.624 -36.639  1.00 18.13  ? 220 THR A CA  1 
ATOM   1472 C  C   . THR A 1 218 ? 39.129 126.165 -38.000  1.00 18.23  ? 220 THR A C   1 
ATOM   1473 O  O   . THR A 1 218 ? 38.780 125.032 -38.127  1.00 17.75  ? 220 THR A O   1 
ATOM   1474 C  CB  . THR A 1 218 ? 40.872 125.821 -36.225  1.00 17.95  ? 220 THR A CB  1 
ATOM   1475 O  OG1 . THR A 1 218 ? 41.239 126.489 -35.028  1.00 18.07  ? 220 THR A OG1 1 
ATOM   1476 C  CG2 . THR A 1 218 ? 41.982 125.918 -37.239  1.00 17.92  ? 220 THR A CG2 1 
ATOM   1477 N  N   . ILE A 1 219 ? 39.153 127.075 -38.961  1.00 18.54  ? 221 ILE A N   1 
ATOM   1478 C  CA  . ILE A 1 219 ? 38.682 126.835 -40.345  1.00 19.23  ? 221 ILE A CA  1 
ATOM   1479 C  C   . ILE A 1 219 ? 39.882 126.372 -41.135  1.00 17.95  ? 221 ILE A C   1 
ATOM   1480 O  O   . ILE A 1 219 ? 40.952 126.950 -41.009  1.00 17.46  ? 221 ILE A O   1 
ATOM   1481 C  CB  . ILE A 1 219 ? 38.031 128.099 -40.946  1.00 21.29  ? 221 ILE A CB  1 
ATOM   1482 C  CG1 . ILE A 1 219 ? 36.976 128.676 -39.995  1.00 22.31  ? 221 ILE A CG1 1 
ATOM   1483 C  CG2 . ILE A 1 219 ? 37.418 127.798 -42.307  1.00 21.55  ? 221 ILE A CG2 1 
ATOM   1484 C  CD1 . ILE A 1 219 ? 35.863 127.688 -39.719  1.00 22.14  ? 221 ILE A CD1 1 
ATOM   1485 N  N   . PRO A 1 220 ? 39.743 125.275 -41.898  1.00 17.19  ? 222 PRO A N   1 
ATOM   1486 C  CA  . PRO A 1 220 ? 40.853 124.778 -42.713  1.00 17.98  ? 222 PRO A CA  1 
ATOM   1487 C  C   . PRO A 1 220 ? 41.183 125.710 -43.891  1.00 18.56  ? 222 PRO A C   1 
ATOM   1488 O  O   . PRO A 1 220 ? 40.350 126.524 -44.245  1.00 18.67  ? 222 PRO A O   1 
ATOM   1489 C  CB  . PRO A 1 220 ? 40.359 123.424 -43.263  1.00 17.90  ? 222 PRO A CB  1 
ATOM   1490 C  CG  . PRO A 1 220 ? 38.837 123.553 -43.214  1.00 17.72  ? 222 PRO A CG  1 
ATOM   1491 C  CD  . PRO A 1 220 ? 38.540 124.447 -42.008  1.00 16.84  ? 222 PRO A CD  1 
ATOM   1492 N  N   . ALA A 1 221 ? 42.394 125.590 -44.437  1.00 18.96  ? 223 ALA A N   1 
ATOM   1493 C  CA  . ALA A 1 221 ? 42.870 126.383 -45.598  1.00 20.49  ? 223 ALA A CA  1 
ATOM   1494 C  C   . ALA A 1 221 ? 41.883 126.245 -46.746  1.00 20.56  ? 223 ALA A C   1 
ATOM   1495 O  O   . ALA A 1 221 ? 41.605 127.241 -47.412  1.00 20.56  ? 223 ALA A O   1 
ATOM   1496 C  CB  . ALA A 1 221 ? 44.225 125.899 -46.031  1.00 20.64  ? 223 ALA A CB  1 
ATOM   1497 N  N   . GLY A 1 222 ? 41.335 125.041 -46.923  1.00 21.49  ? 224 GLY A N   1 
ATOM   1498 C  CA  . GLY A 1 222 ? 40.509 124.728 -48.102  1.00 22.23  ? 224 GLY A CA  1 
ATOM   1499 C  C   . GLY A 1 222 ? 39.072 125.172 -47.927  1.00 23.56  ? 224 GLY A C   1 
ATOM   1500 O  O   . GLY A 1 222 ? 38.224 124.718 -48.736  1.00 23.54  ? 224 GLY A O   1 
ATOM   1501 N  N   . MET A 1 223 ? 38.782 125.972 -46.900  1.00 24.06  ? 225 MET A N   1 
ATOM   1502 C  CA  . MET A 1 223 ? 37.408 126.465 -46.630  1.00 25.36  ? 225 MET A CA  1 
ATOM   1503 C  C   . MET A 1 223 ? 37.454 127.980 -46.356  1.00 25.33  ? 225 MET A C   1 
ATOM   1504 O  O   . MET A 1 223 ? 38.500 128.497 -45.903  1.00 22.87  ? 225 MET A O   1 
ATOM   1505 C  CB  . MET A 1 223 ? 36.793 125.705 -45.459  1.00 26.04  ? 225 MET A CB  1 
ATOM   1506 C  CG  . MET A 1 223 ? 35.297 125.718 -45.478  1.00 28.92  ? 225 MET A CG  1 
ATOM   1507 S  SD  . MET A 1 223 ? 34.402 124.131 -45.583  1.00 31.19  ? 225 MET A SD  1 
ATOM   1508 C  CE  . MET A 1 223 ? 35.795 123.017 -45.488  1.00 30.74  ? 225 MET A CE  1 
ATOM   1509 N  N   . THR A 1 224 ? 36.392 128.697 -46.730  1.00 26.39  ? 226 THR A N   1 
ATOM   1510 C  CA  . THR A 1 224 ? 36.324 130.177 -46.617  1.00 27.29  ? 226 THR A CA  1 
ATOM   1511 C  C   . THR A 1 224 ? 35.112 130.529 -45.774  1.00 27.29  ? 226 THR A C   1 
ATOM   1512 O  O   . THR A 1 224 ? 34.027 130.077 -46.133  1.00 26.93  ? 226 THR A O   1 
ATOM   1513 C  CB  . THR A 1 224 ? 36.293 130.876 -47.977  1.00 28.77  ? 226 THR A CB  1 
ATOM   1514 O  OG1 . THR A 1 224 ? 37.481 130.547 -48.696  1.00 28.20  ? 226 THR A OG1 1 
ATOM   1515 C  CG2 . THR A 1 224 ? 36.199 132.378 -47.845  1.00 30.11  ? 226 THR A CG2 1 
ATOM   1516 N  N   . TYR A 1 225 ? 35.348 131.201 -44.634  1.00 28.33  ? 227 TYR A N   1 
ATOM   1517 C  CA  . TYR A 1 225 ? 34.309 131.621 -43.663  1.00 27.83  ? 227 TYR A CA  1 
ATOM   1518 C  C   . TYR A 1 225 ? 33.590 132.841 -44.237  1.00 29.47  ? 227 TYR A C   1 
ATOM   1519 O  O   . TYR A 1 225 ? 34.240 133.738 -44.792  1.00 28.38  ? 227 TYR A O   1 
ATOM   1520 C  CB  . TYR A 1 225 ? 34.952 131.897 -42.307  1.00 28.43  ? 227 TYR A CB  1 
ATOM   1521 C  CG  . TYR A 1 225 ? 34.094 132.562 -41.258  1.00 28.77  ? 227 TYR A CG  1 
ATOM   1522 C  CD1 . TYR A 1 225 ? 32.957 131.958 -40.746  1.00 28.74  ? 227 TYR A CD1 1 
ATOM   1523 C  CD2 . TYR A 1 225 ? 34.491 133.778 -40.715  1.00 30.57  ? 227 TYR A CD2 1 
ATOM   1524 C  CE1 . TYR A 1 225 ? 32.217 132.562 -39.737  1.00 30.37  ? 227 TYR A CE1 1 
ATOM   1525 C  CE2 . TYR A 1 225 ? 33.781 134.382 -39.683  1.00 31.55  ? 227 TYR A CE2 1 
ATOM   1526 C  CZ  . TYR A 1 225 ? 32.632 133.780 -39.196  1.00 31.33  ? 227 TYR A CZ  1 
ATOM   1527 O  OH  . TYR A 1 225 ? 31.903 134.466 -38.253  1.00 31.41  ? 227 TYR A OH  1 
ATOM   1528 N  N   . ASN A 1 226 ? 32.270 132.868 -44.077  1.00 30.81  ? 228 ASN A N   1 
ATOM   1529 C  CA  . ASN A 1 226 ? 31.389 133.899 -44.669  1.00 32.92  ? 228 ASN A CA  1 
ATOM   1530 C  C   . ASN A 1 226 ? 31.167 135.052 -43.675  1.00 36.18  ? 228 ASN A C   1 
ATOM   1531 O  O   . ASN A 1 226 ? 30.288 135.876 -43.954  1.00 37.69  ? 228 ASN A O   1 
ATOM   1532 C  CB  . ASN A 1 226 ? 30.124 133.209 -45.179  1.00 32.90  ? 228 ASN A CB  1 
ATOM   1533 C  CG  . ASN A 1 226 ? 30.400 132.389 -46.431  1.00 32.97  ? 228 ASN A CG  1 
ATOM   1534 O  OD1 . ASN A 1 226 ? 31.244 132.757 -47.242  1.00 32.09  ? 228 ASN A OD1 1 
ATOM   1535 N  ND2 . ASN A 1 226 ? 29.752 131.244 -46.577  1.00 32.87  ? 228 ASN A ND2 1 
ATOM   1536 N  N   . ASN A 1 227 ? 31.903 135.111 -42.549  1.00 37.27  ? 229 ASN A N   1 
ATOM   1537 C  CA  . ASN A 1 227 ? 31.800 136.195 -41.529  1.00 39.40  ? 229 ASN A CA  1 
ATOM   1538 C  C   . ASN A 1 227 ? 30.336 136.370 -41.128  1.00 38.36  ? 229 ASN A C   1 
ATOM   1539 O  O   . ASN A 1 227 ? 29.893 137.514 -41.027  1.00 39.16  ? 229 ASN A O   1 
ATOM   1540 C  CB  . ASN A 1 227 ? 32.396 137.508 -42.045  1.00 42.93  ? 229 ASN A CB  1 
ATOM   1541 C  CG  . ASN A 1 227 ? 33.889 137.400 -42.238  1.00 44.56  ? 229 ASN A CG  1 
ATOM   1542 O  OD1 . ASN A 1 227 ? 34.671 137.809 -41.379  1.00 50.41  ? 229 ASN A OD1 1 
ATOM   1543 N  ND2 . ASN A 1 227 ? 34.295 136.771 -43.319  1.00 44.98  ? 229 ASN A ND2 1 
ATOM   1544 N  N   . ASP A 1 228 ? 29.612 135.280 -40.910  1.00 36.69  ? 230 ASP A N   1 
ATOM   1545 C  CA  . ASP A 1 228 ? 28.163 135.365 -40.621  1.00 38.32  ? 230 ASP A CA  1 
ATOM   1546 C  C   . ASP A 1 228 ? 27.799 134.552 -39.372  1.00 38.02  ? 230 ASP A C   1 
ATOM   1547 O  O   . ASP A 1 228 ? 26.606 134.198 -39.203  1.00 40.92  ? 230 ASP A O   1 
ATOM   1548 C  CB  . ASP A 1 228 ? 27.387 134.909 -41.856  1.00 39.75  ? 230 ASP A CB  1 
ATOM   1549 C  CG  . ASP A 1 228 ? 27.635 133.458 -42.240  1.00 38.50  ? 230 ASP A CG  1 
ATOM   1550 O  OD1 . ASP A 1 228 ? 28.598 132.827 -41.695  1.00 35.81  ? 230 ASP A OD1 1 
ATOM   1551 O  OD2 . ASP A 1 228 ? 26.871 132.980 -43.083  1.00 39.12  ? 230 ASP A OD2 1 
ATOM   1552 N  N   . ALA A 1 229 ? 28.742 134.262 -38.491  1.00 36.91  ? 231 ALA A N   1 
ATOM   1553 C  CA  . ALA A 1 229 ? 28.406 133.538 -37.247  1.00 36.39  ? 231 ALA A CA  1 
ATOM   1554 C  C   . ALA A 1 229 ? 27.369 134.343 -36.473  1.00 37.60  ? 231 ALA A C   1 
ATOM   1555 O  O   . ALA A 1 229 ? 27.505 135.577 -36.393  1.00 37.34  ? 231 ALA A O   1 
ATOM   1556 C  CB  . ALA A 1 229 ? 29.623 133.248 -36.418  1.00 35.26  ? 231 ALA A CB  1 
ATOM   1557 N  N   . GLN A 1 230 ? 26.372 133.638 -35.940  1.00 39.16  ? 232 GLN A N   1 
ATOM   1558 C  CA  . GLN A 1 230 ? 25.364 134.187 -34.999  1.00 41.34  ? 232 GLN A CA  1 
ATOM   1559 C  C   . GLN A 1 230 ? 25.177 133.250 -33.794  1.00 38.82  ? 232 GLN A C   1 
ATOM   1560 O  O   . GLN A 1 230 ? 25.354 132.036 -33.927  1.00 35.62  ? 232 GLN A O   1 
ATOM   1561 C  CB  . GLN A 1 230 ? 24.096 134.432 -35.808  1.00 44.46  ? 232 GLN A CB  1 
ATOM   1562 C  CG  . GLN A 1 230 ? 24.271 135.589 -36.785  1.00 46.61  ? 232 GLN A CG  1 
ATOM   1563 C  CD  . GLN A 1 230 ? 22.969 135.979 -37.429  1.00 50.16  ? 232 GLN A CD  1 
ATOM   1564 O  OE1 . GLN A 1 230 ? 21.906 135.517 -37.025  1.00 53.68  ? 232 GLN A OE1 1 
ATOM   1565 N  NE2 . GLN A 1 230 ? 23.046 136.854 -38.419  1.00 51.30  ? 232 GLN A NE2 1 
ATOM   1566 N  N   . VAL A 1 231 ? 24.849 133.814 -32.637  1.00 39.81  ? 233 VAL A N   1 
ATOM   1567 C  CA  . VAL A 1 231 ? 24.798 133.051 -31.354  1.00 40.63  ? 233 VAL A CA  1 
ATOM   1568 C  C   . VAL A 1 231 ? 23.347 133.021 -30.889  1.00 43.18  ? 233 VAL A C   1 
ATOM   1569 O  O   . VAL A 1 231 ? 22.689 134.086 -30.877  1.00 44.51  ? 233 VAL A O   1 
ATOM   1570 C  CB  . VAL A 1 231 ? 25.752 133.617 -30.287  1.00 39.20  ? 233 VAL A CB  1 
ATOM   1571 C  CG1 . VAL A 1 231 ? 25.922 132.654 -29.113  1.00 38.01  ? 233 VAL A CG1 1 
ATOM   1572 C  CG2 . VAL A 1 231 ? 27.104 133.958 -30.901  1.00 38.88  ? 233 VAL A CG2 1 
ATOM   1573 N  N   . TYR A 1 232 ? 22.859 131.826 -30.583  1.00 43.65  ? 234 TYR A N   1 
ATOM   1574 C  CA  . TYR A 1 232 ? 21.432 131.602 -30.272  1.00 46.56  ? 234 TYR A CA  1 
ATOM   1575 C  C   . TYR A 1 232 ? 21.305 130.919 -28.915  1.00 45.68  ? 234 TYR A C   1 
ATOM   1576 O  O   . TYR A 1 232 ? 21.990 129.944 -28.670  1.00 42.96  ? 234 TYR A O   1 
ATOM   1577 C  CB  . TYR A 1 232 ? 20.766 130.760 -31.352  1.00 47.82  ? 234 TYR A CB  1 
ATOM   1578 C  CG  . TYR A 1 232 ? 20.644 131.434 -32.699  1.00 51.46  ? 234 TYR A CG  1 
ATOM   1579 C  CD1 . TYR A 1 232 ? 19.809 132.525 -32.900  1.00 53.22  ? 234 TYR A CD1 1 
ATOM   1580 C  CD2 . TYR A 1 232 ? 21.347 130.949 -33.791  1.00 51.93  ? 234 TYR A CD2 1 
ATOM   1581 C  CE1 . TYR A 1 232 ? 19.695 133.125 -34.142  1.00 55.56  ? 234 TYR A CE1 1 
ATOM   1582 C  CE2 . TYR A 1 232 ? 21.238 131.526 -35.043  1.00 52.68  ? 234 TYR A CE2 1 
ATOM   1583 C  CZ  . TYR A 1 232 ? 20.411 132.620 -35.217  1.00 55.87  ? 234 TYR A CZ  1 
ATOM   1584 O  OH  . TYR A 1 232 ? 20.306 133.176 -36.459  1.00 58.95  ? 234 TYR A OH  1 
ATOM   1585 N  N   . LEU A 1 233 ? 20.372 131.378 -28.102  1.00 48.62  ? 235 LEU A N   1 
ATOM   1586 C  CA  . LEU A 1 233 ? 20.017 130.664 -26.857  1.00 51.89  ? 235 LEU A CA  1 
ATOM   1587 C  C   . LEU A 1 233 ? 18.885 129.675 -27.154  1.00 53.70  ? 235 LEU A C   1 
ATOM   1588 O  O   . LEU A 1 233 ? 17.920 130.099 -27.780  1.00 55.07  ? 235 LEU A O   1 
ATOM   1589 C  CB  . LEU A 1 233 ? 19.629 131.717 -25.826  1.00 53.46  ? 235 LEU A CB  1 
ATOM   1590 C  CG  . LEU A 1 233 ? 19.075 131.172 -24.515  1.00 55.30  ? 235 LEU A CG  1 
ATOM   1591 C  CD1 . LEU A 1 233 ? 20.043 130.220 -23.846  1.00 53.41  ? 235 LEU A CD1 1 
ATOM   1592 C  CD2 . LEU A 1 233 ? 18.746 132.323 -23.584  1.00 58.64  ? 235 LEU A CD2 1 
ATOM   1593 N  N   . GLN A 1 234 ? 19.031 128.410 -26.752  1.00 56.13  ? 236 GLN A N   1 
ATOM   1594 C  CA  . GLN A 1 234 ? 17.995 127.352 -26.906  1.00 61.66  ? 236 GLN A CA  1 
ATOM   1595 C  C   . GLN A 1 234 ? 17.477 126.949 -25.530  1.00 67.84  ? 236 GLN A C   1 
ATOM   1596 O  O   . GLN A 1 234 ? 18.262 126.426 -24.751  1.00 69.09  ? 236 GLN A O   1 
ATOM   1597 C  CB  . GLN A 1 234 ? 18.530 126.110 -27.616  1.00 60.22  ? 236 GLN A CB  1 
ATOM   1598 C  CG  . GLN A 1 234 ? 18.302 126.148 -29.115  1.00 61.01  ? 236 GLN A CG  1 
ATOM   1599 C  CD  . GLN A 1 234 ? 18.687 124.872 -29.828  1.00 61.54  ? 236 GLN A CD  1 
ATOM   1600 O  OE1 . GLN A 1 234 ? 19.025 123.859 -29.210  1.00 61.72  ? 236 GLN A OE1 1 
ATOM   1601 N  NE2 . GLN A 1 234 ? 18.644 124.919 -31.155  1.00 58.11  ? 236 GLN A NE2 1 
ATOM   1602 N  N   . GLU A 1 235 ? 16.197 127.202 -25.259  1.00 79.69  ? 237 GLU A N   1 
ATOM   1603 C  CA  . GLU A 1 235 ? 15.492 126.801 -24.006  1.00 88.32  ? 237 GLU A CA  1 
ATOM   1604 C  C   . GLU A 1 235 ? 14.403 125.779 -24.384  1.00 96.40  ? 237 GLU A C   1 
ATOM   1605 O  O   . GLU A 1 235 ? 13.264 126.197 -24.734  1.00 97.49  ? 237 GLU A O   1 
ATOM   1606 C  CB  . GLU A 1 235 ? 14.968 128.041 -23.265  1.00 87.94  ? 237 GLU A CB  1 
ATOM   1607 C  CG  . GLU A 1 235 ? 16.016 128.727 -22.403  1.00 83.66  ? 237 GLU A CG  1 
ATOM   1608 C  CD  . GLU A 1 235 ? 16.251 128.084 -21.043  1.00 83.44  ? 237 GLU A CD  1 
ATOM   1609 O  OE1 . GLU A 1 235 ? 16.316 126.835 -20.963  1.00 81.70  ? 237 GLU A OE1 1 
ATOM   1610 O  OE2 . GLU A 1 235 ? 16.369 128.834 -20.056  1.00 84.00  ? 237 GLU A OE2 1 
ATOM   1611 N  N   . GLY A 1 236 ? 14.761 124.488 -24.364  1.00 98.54  ? 238 GLY A N   1 
ATOM   1612 C  CA  . GLY A 1 236 ? 14.021 123.408 -25.044  1.00 100.53 ? 238 GLY A CA  1 
ATOM   1613 C  C   . GLY A 1 236 ? 14.127 123.536 -26.562  1.00 101.52 ? 238 GLY A C   1 
ATOM   1614 O  O   . GLY A 1 236 ? 15.258 123.393 -27.112  1.00 101.83 ? 238 GLY A O   1 
ATOM   1615 N  N   . GLY A 1 237 ? 12.994 123.800 -27.222  1.00 100.19 ? 239 GLY A N   1 
ATOM   1616 C  CA  . GLY A 1 237 ? 12.883 123.911 -28.691  1.00 95.09  ? 239 GLY A CA  1 
ATOM   1617 C  C   . GLY A 1 237 ? 12.414 125.297 -29.093  1.00 94.56  ? 239 GLY A C   1 
ATOM   1618 O  O   . GLY A 1 237 ? 11.480 125.402 -29.888  1.00 90.48  ? 239 GLY A O   1 
ATOM   1619 N  N   . THR A 1 238 ? 13.018 126.336 -28.518  1.00 93.05  ? 240 THR A N   1 
ATOM   1620 C  CA  . THR A 1 238 ? 12.747 127.753 -28.861  1.00 89.02  ? 240 THR A CA  1 
ATOM   1621 C  C   . THR A 1 238 ? 14.083 128.506 -28.830  1.00 82.63  ? 240 THR A C   1 
ATOM   1622 O  O   . THR A 1 238 ? 14.785 128.384 -27.833  1.00 81.61  ? 240 THR A O   1 
ATOM   1623 C  CB  . THR A 1 238 ? 11.643 128.307 -27.952  1.00 88.86  ? 240 THR A CB  1 
ATOM   1624 O  OG1 . THR A 1 238 ? 11.467 129.675 -28.305  1.00 92.21  ? 240 THR A OG1 1 
ATOM   1625 C  CG2 . THR A 1 238 ? 11.940 128.227 -26.471  1.00 86.16  ? 240 THR A CG2 1 
ATOM   1626 N  N   . GLU A 1 239 ? 14.424 129.218 -29.907  1.00 77.60  ? 241 GLU A N   1 
ATOM   1627 C  CA  . GLU A 1 239 ? 15.732 129.894 -30.098  1.00 70.16  ? 241 GLU A CA  1 
ATOM   1628 C  C   . GLU A 1 239 ? 15.595 131.406 -29.997  1.00 66.78  ? 241 GLU A C   1 
ATOM   1629 O  O   . GLU A 1 239 ? 14.650 131.944 -30.526  1.00 68.42  ? 241 GLU A O   1 
ATOM   1630 C  CB  . GLU A 1 239 ? 16.268 129.622 -31.493  1.00 69.02  ? 241 GLU A CB  1 
ATOM   1631 C  CG  . GLU A 1 239 ? 16.860 128.244 -31.638  1.00 70.80  ? 241 GLU A CG  1 
ATOM   1632 C  CD  . GLU A 1 239 ? 17.971 128.177 -32.667  1.00 72.30  ? 241 GLU A CD  1 
ATOM   1633 O  OE1 . GLU A 1 239 ? 18.025 129.085 -33.540  1.00 73.58  ? 241 GLU A OE1 1 
ATOM   1634 O  OE2 . GLU A 1 239 ? 18.785 127.224 -32.589  1.00 72.93  ? 241 GLU A OE2 1 
ATOM   1635 N  N   . LYS A 1 240 ? 16.595 132.075 -29.462  1.00 64.15  ? 242 LYS A N   1 
ATOM   1636 C  CA  . LYS A 1 240 ? 16.568 133.545 -29.293  1.00 65.71  ? 242 LYS A CA  1 
ATOM   1637 C  C   . LYS A 1 240 ? 17.942 134.096 -29.676  1.00 61.88  ? 242 LYS A C   1 
ATOM   1638 O  O   . LYS A 1 240 ? 18.974 133.573 -29.146  1.00 57.00  ? 242 LYS A O   1 
ATOM   1639 C  CB  . LYS A 1 240 ? 16.185 133.846 -27.844  1.00 67.87  ? 242 LYS A CB  1 
ATOM   1640 C  CG  . LYS A 1 240 ? 16.110 135.313 -27.464  1.00 72.00  ? 242 LYS A CG  1 
ATOM   1641 C  CD  . LYS A 1 240 ? 15.705 135.477 -26.015  1.00 76.37  ? 242 LYS A CD  1 
ATOM   1642 C  CE  . LYS A 1 240 ? 15.081 136.823 -25.688  1.00 81.70  ? 242 LYS A CE  1 
ATOM   1643 N  NZ  . LYS A 1 240 ? 16.080 137.913 -25.741  1.00 83.45  ? 242 LYS A NZ  1 
ATOM   1644 N  N   . ASP A 1 241 ? 17.962 135.090 -30.567  1.00 59.88  ? 243 ASP A N   1 
ATOM   1645 C  CA  . ASP A 1 241 ? 19.231 135.665 -31.081  1.00 58.38  ? 243 ASP A CA  1 
ATOM   1646 C  C   . ASP A 1 241 ? 19.900 136.423 -29.932  1.00 56.17  ? 243 ASP A C   1 
ATOM   1647 O  O   . ASP A 1 241 ? 19.387 137.475 -29.578  1.00 57.16  ? 243 ASP A O   1 
ATOM   1648 C  CB  . ASP A 1 241 ? 19.025 136.518 -32.341  1.00 59.85  ? 243 ASP A CB  1 
ATOM   1649 C  CG  . ASP A 1 241 ? 20.314 136.810 -33.102  1.00 59.43  ? 243 ASP A CG  1 
ATOM   1650 O  OD1 . ASP A 1 241 ? 21.400 136.556 -32.542  1.00 58.32  ? 243 ASP A OD1 1 
ATOM   1651 O  OD2 . ASP A 1 241 ? 20.238 137.257 -34.268  1.00 60.22  ? 243 ASP A OD2 1 
ATOM   1652 N  N   . ILE A 1 242 ? 20.999 135.888 -29.385  1.00 53.11  ? 244 ILE A N   1 
ATOM   1653 C  CA  . ILE A 1 242 ? 21.810 136.541 -28.312  1.00 52.01  ? 244 ILE A CA  1 
ATOM   1654 C  C   . ILE A 1 242 ? 23.141 137.031 -28.893  1.00 49.66  ? 244 ILE A C   1 
ATOM   1655 O  O   . ILE A 1 242 ? 24.026 137.363 -28.088  1.00 45.73  ? 244 ILE A O   1 
ATOM   1656 C  CB  . ILE A 1 242 ? 22.003 135.603 -27.094  1.00 50.87  ? 244 ILE A CB  1 
ATOM   1657 C  CG1 . ILE A 1 242 ? 22.887 134.395 -27.407  1.00 49.29  ? 244 ILE A CG1 1 
ATOM   1658 C  CG2 . ILE A 1 242 ? 20.662 135.154 -26.549  1.00 51.33  ? 244 ILE A CG2 1 
ATOM   1659 C  CD1 . ILE A 1 242 ? 23.183 133.519 -26.213  1.00 47.95  ? 244 ILE A CD1 1 
ATOM   1660 N  N   . SER A 1 243 ? 23.267 137.073 -30.228  1.00 50.48  ? 245 SER A N   1 
ATOM   1661 C  CA  . SER A 1 243 ? 24.488 137.482 -30.971  1.00 49.77  ? 245 SER A CA  1 
ATOM   1662 C  C   . SER A 1 243 ? 25.067 138.755 -30.364  1.00 50.53  ? 245 SER A C   1 
ATOM   1663 O  O   . SER A 1 243 ? 26.287 138.835 -30.167  1.00 50.24  ? 245 SER A O   1 
ATOM   1664 C  CB  . SER A 1 243 ? 24.218 137.710 -32.441  1.00 49.82  ? 245 SER A CB  1 
ATOM   1665 O  OG  . SER A 1 243 ? 24.107 136.481 -33.124  1.00 50.35  ? 245 SER A OG  1 
ATOM   1666 N  N   . THR A 1 244 ? 24.205 139.725 -30.108  1.00 53.83  ? 246 THR A N   1 
ATOM   1667 C  CA  . THR A 1 244 ? 24.591 141.066 -29.619  1.00 55.75  ? 246 THR A CA  1 
ATOM   1668 C  C   . THR A 1 244 ? 25.558 140.953 -28.426  1.00 51.99  ? 246 THR A C   1 
ATOM   1669 O  O   . THR A 1 244 ? 26.358 141.848 -28.278  1.00 49.88  ? 246 THR A O   1 
ATOM   1670 C  CB  . THR A 1 244 ? 23.324 141.882 -29.348  1.00 60.34  ? 246 THR A CB  1 
ATOM   1671 O  OG1 . THR A 1 244 ? 23.812 143.186 -29.052  1.00 65.22  ? 246 THR A OG1 1 
ATOM   1672 C  CG2 . THR A 1 244 ? 22.448 141.352 -28.232  1.00 58.54  ? 246 THR A CG2 1 
ATOM   1673 N  N   . PHE A 1 245 ? 25.518 139.882 -27.632  1.00 51.98  ? 247 PHE A N   1 
ATOM   1674 C  CA  . PHE A 1 245 ? 26.352 139.710 -26.403  1.00 53.40  ? 247 PHE A CA  1 
ATOM   1675 C  C   . PHE A 1 245 ? 27.734 139.140 -26.711  1.00 49.24  ? 247 PHE A C   1 
ATOM   1676 O  O   . PHE A 1 245 ? 28.646 139.250 -25.852  1.00 46.75  ? 247 PHE A O   1 
ATOM   1677 C  CB  . PHE A 1 245 ? 25.698 138.756 -25.402  1.00 55.90  ? 247 PHE A CB  1 
ATOM   1678 C  CG  . PHE A 1 245 ? 24.622 139.422 -24.587  1.00 63.22  ? 247 PHE A CG  1 
ATOM   1679 C  CD1 . PHE A 1 245 ? 24.965 140.218 -23.495  1.00 65.88  ? 247 PHE A CD1 1 
ATOM   1680 C  CD2 . PHE A 1 245 ? 23.277 139.283 -24.919  1.00 65.33  ? 247 PHE A CD2 1 
ATOM   1681 C  CE1 . PHE A 1 245 ? 23.987 140.863 -22.750  1.00 66.60  ? 247 PHE A CE1 1 
ATOM   1682 C  CE2 . PHE A 1 245 ? 22.300 139.927 -24.172  1.00 68.33  ? 247 PHE A CE2 1 
ATOM   1683 C  CZ  . PHE A 1 245 ? 22.657 140.714 -23.089  1.00 69.01  ? 247 PHE A CZ  1 
ATOM   1684 N  N   . PHE A 1 246 ? 27.874 138.504 -27.873  1.00 46.01  ? 248 PHE A N   1 
ATOM   1685 C  CA  . PHE A 1 246 ? 29.100 137.770 -28.269  1.00 42.29  ? 248 PHE A CA  1 
ATOM   1686 C  C   . PHE A 1 246 ? 29.777 138.513 -29.411  1.00 42.59  ? 248 PHE A C   1 
ATOM   1687 O  O   . PHE A 1 246 ? 29.510 138.211 -30.558  1.00 41.69  ? 248 PHE A O   1 
ATOM   1688 C  CB  . PHE A 1 246 ? 28.755 136.352 -28.711  1.00 39.11  ? 248 PHE A CB  1 
ATOM   1689 C  CG  . PHE A 1 246 ? 28.127 135.521 -27.637  1.00 37.64  ? 248 PHE A CG  1 
ATOM   1690 C  CD1 . PHE A 1 246 ? 26.845 135.784 -27.214  1.00 39.15  ? 248 PHE A CD1 1 
ATOM   1691 C  CD2 . PHE A 1 246 ? 28.814 134.479 -27.051  1.00 36.70  ? 248 PHE A CD2 1 
ATOM   1692 C  CE1 . PHE A 1 246 ? 26.253 135.008 -26.231  1.00 39.15  ? 248 PHE A CE1 1 
ATOM   1693 C  CE2 . PHE A 1 246 ? 28.229 133.697 -26.066  1.00 36.38  ? 248 PHE A CE2 1 
ATOM   1694 C  CZ  . PHE A 1 246 ? 26.942 133.958 -25.665  1.00 37.54  ? 248 PHE A CZ  1 
ATOM   1695 N  N   . PRO A 1 247 ? 30.682 139.480 -29.158  1.00 43.17  ? 249 PRO A N   1 
ATOM   1696 C  CA  . PRO A 1 247 ? 31.532 139.982 -30.234  1.00 44.15  ? 249 PRO A CA  1 
ATOM   1697 C  C   . PRO A 1 247 ? 32.411 138.815 -30.731  1.00 43.30  ? 249 PRO A C   1 
ATOM   1698 O  O   . PRO A 1 247 ? 32.936 137.996 -29.941  1.00 43.91  ? 249 PRO A O   1 
ATOM   1699 C  CB  . PRO A 1 247 ? 32.306 141.137 -29.588  1.00 44.94  ? 249 PRO A CB  1 
ATOM   1700 C  CG  . PRO A 1 247 ? 32.316 140.769 -28.113  1.00 44.37  ? 249 PRO A CG  1 
ATOM   1701 C  CD  . PRO A 1 247 ? 31.000 140.064 -27.847  1.00 43.47  ? 249 PRO A CD  1 
ATOM   1702 N  N   . ILE A 1 248 ? 32.502 138.708 -32.046  1.00 42.33  ? 250 ILE A N   1 
ATOM   1703 C  CA  . ILE A 1 248 ? 33.156 137.570 -32.744  1.00 41.11  ? 250 ILE A CA  1 
ATOM   1704 C  C   . ILE A 1 248 ? 34.334 138.127 -33.521  1.00 39.81  ? 250 ILE A C   1 
ATOM   1705 O  O   . ILE A 1 248 ? 34.174 139.179 -34.092  1.00 42.71  ? 250 ILE A O   1 
ATOM   1706 C  CB  . ILE A 1 248 ? 32.137 136.862 -33.651  1.00 40.83  ? 250 ILE A CB  1 
ATOM   1707 C  CG1 . ILE A 1 248 ? 31.176 136.060 -32.774  1.00 40.28  ? 250 ILE A CG1 1 
ATOM   1708 C  CG2 . ILE A 1 248 ? 32.837 136.008 -34.698  1.00 40.23  ? 250 ILE A CG2 1 
ATOM   1709 C  CD1 . ILE A 1 248 ? 30.089 135.341 -33.514  1.00 40.20  ? 250 ILE A CD1 1 
ATOM   1710 N  N   . SER A 1 249 ? 35.480 137.469 -33.492  1.00 38.15  ? 251 SER A N   1 
ATOM   1711 C  CA  . SER A 1 249 ? 36.637 137.842 -34.336  1.00 38.25  ? 251 SER A CA  1 
ATOM   1712 C  C   . SER A 1 249 ? 37.086 136.638 -35.181  1.00 36.74  ? 251 SER A C   1 
ATOM   1713 O  O   . SER A 1 249 ? 36.821 135.473 -34.834  1.00 35.94  ? 251 SER A O   1 
ATOM   1714 C  CB  . SER A 1 249 ? 37.757 138.414 -33.532  1.00 38.45  ? 251 SER A CB  1 
ATOM   1715 O  OG  . SER A 1 249 ? 38.203 137.463 -32.603  1.00 40.18  ? 251 SER A OG  1 
ATOM   1716 N  N   . TYR A 1 250 ? 37.708 136.943 -36.306  1.00 35.27  ? 252 TYR A N   1 
ATOM   1717 C  CA  . TYR A 1 250 ? 38.290 135.963 -37.242  1.00 34.39  ? 252 TYR A CA  1 
ATOM   1718 C  C   . TYR A 1 250 ? 39.645 136.494 -37.692  1.00 34.84  ? 252 TYR A C   1 
ATOM   1719 O  O   . TYR A 1 250 ? 39.710 137.544 -38.308  1.00 36.25  ? 252 TYR A O   1 
ATOM   1720 C  CB  . TYR A 1 250 ? 37.362 135.767 -38.424  1.00 33.87  ? 252 TYR A CB  1 
ATOM   1721 C  CG  . TYR A 1 250 ? 37.747 134.640 -39.333  1.00 32.84  ? 252 TYR A CG  1 
ATOM   1722 C  CD1 . TYR A 1 250 ? 37.687 133.328 -38.898  1.00 30.93  ? 252 TYR A CD1 1 
ATOM   1723 C  CD2 . TYR A 1 250 ? 38.115 134.888 -40.646  1.00 33.59  ? 252 TYR A CD2 1 
ATOM   1724 C  CE1 . TYR A 1 250 ? 38.003 132.281 -39.749  1.00 31.09  ? 252 TYR A CE1 1 
ATOM   1725 C  CE2 . TYR A 1 250 ? 38.446 133.860 -41.509  1.00 32.86  ? 252 TYR A CE2 1 
ATOM   1726 C  CZ  . TYR A 1 250 ? 38.376 132.556 -41.062  1.00 32.71  ? 252 TYR A CZ  1 
ATOM   1727 O  OH  . TYR A 1 250 ? 38.670 131.555 -41.937  1.00 32.16  ? 252 TYR A OH  1 
ATOM   1728 N  N   . THR A 1 251 ? 40.695 135.821 -37.258  1.00 34.40  ? 253 THR A N   1 
ATOM   1729 C  CA  . THR A 1 251 ? 42.107 136.082 -37.591  1.00 34.88  ? 253 THR A CA  1 
ATOM   1730 C  C   . THR A 1 251 ? 42.735 134.692 -37.646  1.00 33.47  ? 253 THR A C   1 
ATOM   1731 O  O   . THR A 1 251 ? 42.388 133.842 -36.815  1.00 31.78  ? 253 THR A O   1 
ATOM   1732 C  CB  . THR A 1 251 ? 42.754 137.008 -36.548  1.00 37.82  ? 253 THR A CB  1 
ATOM   1733 O  OG1 . THR A 1 251 ? 42.999 136.295 -35.334  1.00 36.30  ? 253 THR A OG1 1 
ATOM   1734 C  CG2 . THR A 1 251 ? 41.896 138.194 -36.142  1.00 39.26  ? 253 THR A CG2 1 
ATOM   1735 N  N   . GLY A 1 252 ? 43.554 134.410 -38.642  1.00 33.27  ? 254 GLY A N   1 
ATOM   1736 C  CA  . GLY A 1 252 ? 44.370 133.182 -38.626  1.00 30.90  ? 254 GLY A CA  1 
ATOM   1737 C  C   . GLY A 1 252 ? 43.503 131.979 -38.894  1.00 28.15  ? 254 GLY A C   1 
ATOM   1738 O  O   . GLY A 1 252 ? 43.902 130.871 -38.462  1.00 29.68  ? 254 GLY A O   1 
ATOM   1739 N  N   . ASN A 1 253 ? 42.338 132.196 -39.511  1.00 25.02  ? 255 ASN A N   1 
ATOM   1740 C  CA  . ASN A 1 253 ? 41.392 131.098 -39.813  1.00 23.46  ? 255 ASN A CA  1 
ATOM   1741 C  C   . ASN A 1 253 ? 40.799 130.573 -38.497  1.00 22.28  ? 255 ASN A C   1 
ATOM   1742 O  O   . ASN A 1 253 ? 40.338 129.409 -38.449  1.00 20.36  ? 255 ASN A O   1 
ATOM   1743 C  CB  . ASN A 1 253 ? 42.085 129.987 -40.611  1.00 22.89  ? 255 ASN A CB  1 
ATOM   1744 C  CG  . ASN A 1 253 ? 41.911 130.209 -42.090  1.00 23.28  ? 255 ASN A CG  1 
ATOM   1745 O  OD1 . ASN A 1 253 ? 42.346 131.242 -42.583  1.00 24.21  ? 255 ASN A OD1 1 
ATOM   1746 N  ND2 . ASN A 1 253 ? 41.219 129.303 -42.767  1.00 22.52  ? 255 ASN A ND2 1 
ATOM   1747 N  N   . VAL A 1 254 ? 40.767 131.408 -37.467  1.00 22.31  ? 256 VAL A N   1 
ATOM   1748 C  CA  . VAL A 1 254 ? 40.195 130.987 -36.167  1.00 21.80  ? 256 VAL A CA  1 
ATOM   1749 C  C   . VAL A 1 254 ? 39.040 131.922 -35.857  1.00 22.26  ? 256 VAL A C   1 
ATOM   1750 O  O   . VAL A 1 254 ? 39.263 133.126 -35.804  1.00 23.08  ? 256 VAL A O   1 
ATOM   1751 C  CB  . VAL A 1 254 ? 41.264 130.969 -35.071  1.00 21.78  ? 256 VAL A CB  1 
ATOM   1752 C  CG1 . VAL A 1 254 ? 40.627 130.729 -33.725  1.00 21.66  ? 256 VAL A CG1 1 
ATOM   1753 C  CG2 . VAL A 1 254 ? 42.347 129.948 -35.365  1.00 21.50  ? 256 VAL A CG2 1 
ATOM   1754 N  N   . ILE A 1 255 ? 37.838 131.378 -35.748  1.00 22.03  ? 257 ILE A N   1 
ATOM   1755 C  CA  . ILE A 1 255 ? 36.699 132.144 -35.188  1.00 23.22  ? 257 ILE A CA  1 
ATOM   1756 C  C   . ILE A 1 255 ? 36.797 132.086 -33.646  1.00 23.47  ? 257 ILE A C   1 
ATOM   1757 O  O   . ILE A 1 255 ? 36.788 130.978 -33.082  1.00 22.47  ? 257 ILE A O   1 
ATOM   1758 C  CB  . ILE A 1 255 ? 35.352 131.588 -35.654  1.00 23.27  ? 257 ILE A CB  1 
ATOM   1759 C  CG1 . ILE A 1 255 ? 35.312 131.284 -37.147  1.00 23.44  ? 257 ILE A CG1 1 
ATOM   1760 C  CG2 . ILE A 1 255 ? 34.229 132.533 -35.230  1.00 24.20  ? 257 ILE A CG2 1 
ATOM   1761 C  CD1 . ILE A 1 255 ? 34.090 130.510 -37.569  1.00 23.62  ? 257 ILE A CD1 1 
ATOM   1762 N  N   . THR A 1 256 ? 36.802 133.238 -32.990  1.00 24.32  ? 258 THR A N   1 
ATOM   1763 C  CA  . THR A 1 256 ? 36.731 133.349 -31.516  1.00 25.34  ? 258 THR A CA  1 
ATOM   1764 C  C   . THR A 1 256 ? 35.352 133.890 -31.154  1.00 26.85  ? 258 THR A C   1 
ATOM   1765 O  O   . THR A 1 256 ? 34.978 134.968 -31.657  1.00 29.09  ? 258 THR A O   1 
ATOM   1766 C  CB  . THR A 1 256 ? 37.864 134.218 -30.979  1.00 25.70  ? 258 THR A CB  1 
ATOM   1767 O  OG1 . THR A 1 256 ? 39.066 133.549 -31.350  1.00 25.21  ? 258 THR A OG1 1 
ATOM   1768 C  CG2 . THR A 1 256 ? 37.812 134.376 -29.472  1.00 25.96  ? 258 THR A CG2 1 
ATOM   1769 N  N   . ILE A 1 257 ? 34.587 133.156 -30.359  1.00 27.24  ? 259 ILE A N   1 
ATOM   1770 C  CA  . ILE A 1 257 ? 33.255 133.646 -29.900  1.00 27.87  ? 259 ILE A CA  1 
ATOM   1771 C  C   . ILE A 1 257 ? 33.304 133.650 -28.386  1.00 27.95  ? 259 ILE A C   1 
ATOM   1772 O  O   . ILE A 1 257 ? 33.456 132.556 -27.834  1.00 26.57  ? 259 ILE A O   1 
ATOM   1773 C  CB  . ILE A 1 257 ? 32.087 132.784 -30.415  1.00 28.11  ? 259 ILE A CB  1 
ATOM   1774 C  CG1 . ILE A 1 257 ? 32.131 132.516 -31.934  1.00 28.26  ? 259 ILE A CG1 1 
ATOM   1775 C  CG2 . ILE A 1 257 ? 30.779 133.437 -30.021  1.00 29.30  ? 259 ILE A CG2 1 
ATOM   1776 C  CD1 . ILE A 1 257 ? 32.628 131.126 -32.292  1.00 26.87  ? 259 ILE A CD1 1 
ATOM   1777 N  N   . THR A 1 258 ? 33.148 134.819 -27.771  1.00 29.48  ? 260 THR A N   1 
ATOM   1778 C  CA  . THR A 1 258 ? 33.146 134.954 -26.299  1.00 30.88  ? 260 THR A CA  1 
ATOM   1779 C  C   . THR A 1 258 ? 32.350 136.176 -25.871  1.00 32.53  ? 260 THR A C   1 
ATOM   1780 O  O   . THR A 1 258 ? 32.530 137.253 -26.440  1.00 33.46  ? 260 THR A O   1 
ATOM   1781 C  CB  . THR A 1 258 ? 34.576 135.011 -25.731  1.00 30.52  ? 260 THR A CB  1 
ATOM   1782 O  OG1 . THR A 1 258 ? 34.477 135.122 -24.304  1.00 29.56  ? 260 THR A OG1 1 
ATOM   1783 C  CG2 . THR A 1 258 ? 35.394 136.136 -26.327  1.00 30.94  ? 260 THR A CG2 1 
ATOM   1784 N  N   . PRO A 1 259 ? 31.504 136.027 -24.816  1.00 32.85  ? 261 PRO A N   1 
ATOM   1785 C  CA  . PRO A 1 259 ? 30.859 137.166 -24.163  1.00 33.88  ? 261 PRO A CA  1 
ATOM   1786 C  C   . PRO A 1 259 ? 31.681 137.773 -23.020  1.00 34.09  ? 261 PRO A C   1 
ATOM   1787 O  O   . PRO A 1 259 ? 31.180 138.654 -22.345  1.00 35.45  ? 261 PRO A O   1 
ATOM   1788 C  CB  . PRO A 1 259 ? 29.582 136.519 -23.624  1.00 34.30  ? 261 PRO A CB  1 
ATOM   1789 C  CG  . PRO A 1 259 ? 29.994 135.105 -23.261  1.00 33.67  ? 261 PRO A CG  1 
ATOM   1790 C  CD  . PRO A 1 259 ? 31.098 134.741 -24.230  1.00 32.09  ? 261 PRO A CD  1 
ATOM   1791 N  N   . GLY A 1 260 ? 32.912 137.282 -22.843  1.00 32.73  ? 262 GLY A N   1 
ATOM   1792 C  CA  . GLY A 1 260 ? 33.791 137.578 -21.701  1.00 31.64  ? 262 GLY A CA  1 
ATOM   1793 C  C   . GLY A 1 260 ? 33.348 136.792 -20.476  1.00 30.23  ? 262 GLY A C   1 
ATOM   1794 O  O   . GLY A 1 260 ? 34.076 135.897 -20.012  1.00 28.25  ? 262 GLY A O   1 
ATOM   1795 N  N   . ASP A 1 261 ? 32.131 137.058 -20.035  1.00 28.89  ? 263 ASP A N   1 
ATOM   1796 C  CA  . ASP A 1 261 ? 31.490 136.310 -18.947  1.00 28.03  ? 263 ASP A CA  1 
ATOM   1797 C  C   . ASP A 1 261 ? 30.093 135.904 -19.404  1.00 26.90  ? 263 ASP A C   1 
ATOM   1798 O  O   . ASP A 1 261 ? 29.271 136.789 -19.721  1.00 27.84  ? 263 ASP A O   1 
ATOM   1799 C  CB  . ASP A 1 261 ? 31.486 137.222 -17.722  1.00 28.87  ? 263 ASP A CB  1 
ATOM   1800 C  CG  . ASP A 1 261 ? 31.016 136.563 -16.431  1.00 29.93  ? 263 ASP A CG  1 
ATOM   1801 O  OD1 . ASP A 1 261 ? 30.547 135.365 -16.460  1.00 28.69  ? 263 ASP A OD1 1 
ATOM   1802 O  OD2 . ASP A 1 261 ? 31.170 137.254 -15.386  1.00 31.43  ? 263 ASP A OD2 1 
ATOM   1803 N  N   . LEU A 1 262 ? 29.788 134.622 -19.371  1.00 25.50  ? 264 LEU A N   1 
ATOM   1804 C  CA  . LEU A 1 262 ? 28.451 134.150 -19.795  1.00 26.72  ? 264 LEU A CA  1 
ATOM   1805 C  C   . LEU A 1 262 ? 27.387 134.666 -18.828  1.00 28.63  ? 264 LEU A C   1 
ATOM   1806 O  O   . LEU A 1 262 ? 26.226 134.790 -19.242  1.00 29.25  ? 264 LEU A O   1 
ATOM   1807 C  CB  . LEU A 1 262 ? 28.458 132.622 -19.868  1.00 26.24  ? 264 LEU A CB  1 
ATOM   1808 C  CG  . LEU A 1 262 ? 27.230 131.985 -20.525  1.00 26.88  ? 264 LEU A CG  1 
ATOM   1809 C  CD1 . LEU A 1 262 ? 26.983 132.520 -21.929  1.00 27.33  ? 264 LEU A CD1 1 
ATOM   1810 C  CD2 . LEU A 1 262 ? 27.375 130.476 -20.560  1.00 26.41  ? 264 LEU A CD2 1 
ATOM   1811 N  N   . LYS A 1 263 ? 27.745 134.973 -17.578  1.00 29.69  ? 265 LYS A N   1 
ATOM   1812 C  CA  . LYS A 1 263 ? 26.744 135.501 -16.620  1.00 31.85  ? 265 LYS A CA  1 
ATOM   1813 C  C   . LYS A 1 263 ? 26.231 136.869 -17.110  1.00 34.13  ? 265 LYS A C   1 
ATOM   1814 O  O   . LYS A 1 263 ? 25.191 137.347 -16.610  1.00 37.85  ? 265 LYS A O   1 
ATOM   1815 C  CB  . LYS A 1 263 ? 27.334 135.636 -15.213  1.00 31.97  ? 265 LYS A CB  1 
ATOM   1816 C  CG  . LYS A 1 263 ? 27.857 134.359 -14.588  1.00 31.50  ? 265 LYS A CG  1 
ATOM   1817 C  CD  . LYS A 1 263 ? 26.792 133.305 -14.364  1.00 32.35  ? 265 LYS A CD  1 
ATOM   1818 C  CE  . LYS A 1 263 ? 27.325 132.106 -13.605  1.00 32.16  ? 265 LYS A CE  1 
ATOM   1819 N  NZ  . LYS A 1 263 ? 26.255 131.264 -13.020  1.00 33.79  ? 265 LYS A NZ  1 
ATOM   1820 N  N   . TYR A 1 264 ? 26.924 137.529 -18.025  1.00 34.38  ? 266 TYR A N   1 
ATOM   1821 C  CA  . TYR A 1 264 ? 26.417 138.789 -18.625  1.00 35.98  ? 266 TYR A CA  1 
ATOM   1822 C  C   . TYR A 1 264 ? 25.145 138.514 -19.436  1.00 39.14  ? 266 TYR A C   1 
ATOM   1823 O  O   . TYR A 1 264 ? 24.398 139.469 -19.714  1.00 40.17  ? 266 TYR A O   1 
ATOM   1824 C  CB  . TYR A 1 264 ? 27.497 139.463 -19.471  1.00 34.27  ? 266 TYR A CB  1 
ATOM   1825 C  CG  . TYR A 1 264 ? 28.659 139.999 -18.677  1.00 32.52  ? 266 TYR A CG  1 
ATOM   1826 C  CD1 . TYR A 1 264 ? 28.650 140.046 -17.286  1.00 31.96  ? 266 TYR A CD1 1 
ATOM   1827 C  CD2 . TYR A 1 264 ? 29.780 140.471 -19.332  1.00 32.01  ? 266 TYR A CD2 1 
ATOM   1828 C  CE1 . TYR A 1 264 ? 29.737 140.540 -16.581  1.00 31.26  ? 266 TYR A CE1 1 
ATOM   1829 C  CE2 . TYR A 1 264 ? 30.857 141.002 -18.644  1.00 32.54  ? 266 TYR A CE2 1 
ATOM   1830 C  CZ  . TYR A 1 264 ? 30.831 141.045 -17.256  1.00 30.81  ? 266 TYR A CZ  1 
ATOM   1831 O  OH  . TYR A 1 264 ? 31.904 141.556 -16.601  1.00 29.65  ? 266 TYR A OH  1 
ATOM   1832 N  N   . VAL A 1 265 ? 24.914 137.262 -19.843  1.00 41.11  ? 267 VAL A N   1 
ATOM   1833 C  CA  . VAL A 1 265 ? 23.708 136.895 -20.632  1.00 44.49  ? 267 VAL A CA  1 
ATOM   1834 C  C   . VAL A 1 265 ? 22.739 136.287 -19.630  1.00 46.54  ? 267 VAL A C   1 
ATOM   1835 O  O   . VAL A 1 265 ? 22.880 135.104 -19.307  1.00 45.59  ? 267 VAL A O   1 
ATOM   1836 C  CB  . VAL A 1 265 ? 24.009 135.991 -21.852  1.00 44.78  ? 267 VAL A CB  1 
ATOM   1837 C  CG1 . VAL A 1 265 ? 22.835 135.973 -22.828  1.00 47.04  ? 267 VAL A CG1 1 
ATOM   1838 C  CG2 . VAL A 1 265 ? 25.265 136.417 -22.598  1.00 42.61  ? 267 VAL A CG2 1 
ATOM   1839 N  N   . GLN A 1 266 ? 21.843 137.124 -19.105  1.00 52.25  ? 268 GLN A N   1 
ATOM   1840 C  CA  . GLN A 1 266 ? 21.089 136.850 -17.849  1.00 54.76  ? 268 GLN A CA  1 
ATOM   1841 C  C   . GLN A 1 266 ? 20.005 135.822 -18.171  1.00 56.53  ? 268 GLN A C   1 
ATOM   1842 O  O   . GLN A 1 266 ? 19.662 135.052 -17.264  1.00 57.15  ? 268 GLN A O   1 
ATOM   1843 C  CB  . GLN A 1 266 ? 20.596 138.164 -17.230  1.00 57.90  ? 268 GLN A CB  1 
ATOM   1844 C  CG  . GLN A 1 266 ? 21.743 139.149 -16.973  1.00 60.55  ? 268 GLN A CG  1 
ATOM   1845 C  CD  . GLN A 1 266 ? 21.477 140.390 -16.141  1.00 64.23  ? 268 GLN A CD  1 
ATOM   1846 O  OE1 . GLN A 1 266 ? 20.430 141.029 -16.238  1.00 68.74  ? 268 GLN A OE1 1 
ATOM   1847 N  NE2 . GLN A 1 266 ? 22.466 140.785 -15.343  1.00 62.71  ? 268 GLN A NE2 1 
ATOM   1848 N  N   . ASP A 1 267 ? 19.568 135.772 -19.435  1.00 58.50  ? 269 ASP A N   1 
ATOM   1849 C  CA  . ASP A 1 267 ? 18.575 134.799 -19.968  1.00 62.03  ? 269 ASP A CA  1 
ATOM   1850 C  C   . ASP A 1 267 ? 19.125 133.361 -19.885  1.00 60.04  ? 269 ASP A C   1 
ATOM   1851 O  O   . ASP A 1 267 ? 18.326 132.425 -19.906  1.00 59.33  ? 269 ASP A O   1 
ATOM   1852 C  CB  . ASP A 1 267 ? 18.160 135.181 -21.398  1.00 65.03  ? 269 ASP A CB  1 
ATOM   1853 C  CG  . ASP A 1 267 ? 17.104 136.293 -21.512  1.00 71.12  ? 269 ASP A CG  1 
ATOM   1854 O  OD1 . ASP A 1 267 ? 16.901 137.064 -20.523  1.00 70.03  ? 269 ASP A OD1 1 
ATOM   1855 O  OD2 . ASP A 1 267 ? 16.481 136.398 -22.616  1.00 75.96  ? 269 ASP A OD2 1 
ATOM   1856 N  N   . VAL A 1 268 ? 20.444 133.177 -19.798  1.00 59.17  ? 270 VAL A N   1 
ATOM   1857 C  CA  . VAL A 1 268 ? 21.096 131.836 -19.894  1.00 56.63  ? 270 VAL A CA  1 
ATOM   1858 C  C   . VAL A 1 268 ? 20.939 131.096 -18.566  1.00 56.04  ? 270 VAL A C   1 
ATOM   1859 O  O   . VAL A 1 268 ? 21.486 131.567 -17.588  1.00 54.45  ? 270 VAL A O   1 
ATOM   1860 C  CB  . VAL A 1 268 ? 22.590 131.946 -20.240  1.00 52.96  ? 270 VAL A CB  1 
ATOM   1861 C  CG1 . VAL A 1 268 ? 23.258 130.583 -20.171  1.00 50.70  ? 270 VAL A CG1 1 
ATOM   1862 C  CG2 . VAL A 1 268 ? 22.815 132.604 -21.589  1.00 53.29  ? 270 VAL A CG2 1 
ATOM   1863 N  N   . LYS A 1 269 ? 20.270 129.948 -18.568  1.00 58.14  ? 271 LYS A N   1 
ATOM   1864 C  CA  . LYS A 1 269 ? 20.082 129.088 -17.375  1.00 58.16  ? 271 LYS A CA  1 
ATOM   1865 C  C   . LYS A 1 269 ? 20.935 127.844 -17.552  1.00 52.91  ? 271 LYS A C   1 
ATOM   1866 O  O   . LYS A 1 269 ? 21.482 127.660 -18.628  1.00 49.47  ? 271 LYS A O   1 
ATOM   1867 C  CB  . LYS A 1 269 ? 18.611 128.699 -17.225  1.00 66.28  ? 271 LYS A CB  1 
ATOM   1868 C  CG  . LYS A 1 269 ? 17.758 129.701 -16.454  1.00 73.07  ? 271 LYS A CG  1 
ATOM   1869 C  CD  . LYS A 1 269 ? 17.578 131.042 -17.148  1.00 77.24  ? 271 LYS A CD  1 
ATOM   1870 C  CE  . LYS A 1 269 ? 16.714 131.996 -16.349  1.00 81.47  ? 271 LYS A CE  1 
ATOM   1871 N  NZ  . LYS A 1 269 ? 16.060 132.990 -17.232  1.00 85.32  ? 271 LYS A NZ  1 
ATOM   1872 N  N   . VAL A 1 270 ? 21.016 127.036 -16.510  1.00 49.01  ? 272 VAL A N   1 
ATOM   1873 C  CA  . VAL A 1 270 ? 21.769 125.752 -16.490  1.00 49.30  ? 272 VAL A CA  1 
ATOM   1874 C  C   . VAL A 1 270 ? 21.243 124.848 -17.605  1.00 49.38  ? 272 VAL A C   1 
ATOM   1875 O  O   . VAL A 1 270 ? 21.990 124.038 -18.101  1.00 48.48  ? 272 VAL A O   1 
ATOM   1876 C  CB  . VAL A 1 270 ? 21.629 125.065 -15.116  1.00 51.86  ? 272 VAL A CB  1 
ATOM   1877 C  CG1 . VAL A 1 270 ? 20.182 124.691 -14.803  1.00 54.54  ? 272 VAL A CG1 1 
ATOM   1878 C  CG2 . VAL A 1 270 ? 22.514 123.837 -15.004  1.00 51.49  ? 272 VAL A CG2 1 
ATOM   1879 N  N   . SER A 1 271 ? 19.956 124.923 -17.908  1.00 51.10  ? 273 SER A N   1 
ATOM   1880 C  CA  . SER A 1 271 ? 19.276 123.986 -18.834  1.00 50.94  ? 273 SER A CA  1 
ATOM   1881 C  C   . SER A 1 271 ? 19.398 124.516 -20.257  1.00 47.66  ? 273 SER A C   1 
ATOM   1882 O  O   . SER A 1 271 ? 18.942 123.821 -21.142  1.00 47.57  ? 273 SER A O   1 
ATOM   1883 C  CB  . SER A 1 271 ? 17.815 123.786 -18.448  1.00 53.46  ? 273 SER A CB  1 
ATOM   1884 O  OG  . SER A 1 271 ? 17.069 124.992 -18.590  1.00 53.76  ? 273 SER A OG  1 
ATOM   1885 N  N   . SER A 1 272 ? 19.957 125.710 -20.451  1.00 46.13  ? 274 SER A N   1 
ATOM   1886 C  CA  . SER A 1 272 ? 20.119 126.352 -21.786  1.00 46.65  ? 274 SER A CA  1 
ATOM   1887 C  C   . SER A 1 272 ? 21.180 125.626 -22.624  1.00 45.29  ? 274 SER A C   1 
ATOM   1888 O  O   . SER A 1 272 ? 22.148 125.070 -22.034  1.00 44.93  ? 274 SER A O   1 
ATOM   1889 C  CB  . SER A 1 272 ? 20.489 127.790 -21.644  1.00 46.23  ? 274 SER A CB  1 
ATOM   1890 O  OG  . SER A 1 272 ? 19.529 128.470 -20.866  1.00 48.40  ? 274 SER A OG  1 
ATOM   1891 N  N   . LYS A 1 273 ? 20.996 125.620 -23.944  1.00 45.86  ? 275 LYS A N   1 
ATOM   1892 C  CA  . LYS A 1 273 ? 22.070 125.328 -24.931  1.00 44.82  ? 275 LYS A CA  1 
ATOM   1893 C  C   . LYS A 1 273 ? 22.485 126.623 -25.636  1.00 43.05  ? 275 LYS A C   1 
ATOM   1894 O  O   . LYS A 1 273 ? 21.590 127.328 -26.126  1.00 47.51  ? 275 LYS A O   1 
ATOM   1895 C  CB  . LYS A 1 273 ? 21.565 124.324 -25.953  1.00 46.33  ? 275 LYS A CB  1 
ATOM   1896 C  CG  . LYS A 1 273 ? 21.389 122.922 -25.403  1.00 49.14  ? 275 LYS A CG  1 
ATOM   1897 C  CD  . LYS A 1 273 ? 21.021 121.957 -26.522  1.00 51.69  ? 275 LYS A CD  1 
ATOM   1898 C  CE  . LYS A 1 273 ? 21.374 120.514 -26.242  1.00 53.02  ? 275 LYS A CE  1 
ATOM   1899 N  NZ  . LYS A 1 273 ? 20.704 120.066 -25.005  1.00 56.48  ? 275 LYS A NZ  1 
ATOM   1900 N  N   . ILE A 1 274 ? 23.779 126.934 -25.684  1.00 38.88  ? 276 ILE A N   1 
ATOM   1901 C  CA  . ILE A 1 274 ? 24.326 127.998 -26.581  1.00 37.90  ? 276 ILE A CA  1 
ATOM   1902 C  C   . ILE A 1 274 ? 24.657 127.384 -27.961  1.00 35.84  ? 276 ILE A C   1 
ATOM   1903 O  O   . ILE A 1 274 ? 25.401 126.357 -28.038  1.00 32.34  ? 276 ILE A O   1 
ATOM   1904 C  CB  . ILE A 1 274 ? 25.557 128.659 -25.938  1.00 37.64  ? 276 ILE A CB  1 
ATOM   1905 C  CG1 . ILE A 1 274 ? 25.308 129.073 -24.482  1.00 37.60  ? 276 ILE A CG1 1 
ATOM   1906 C  CG2 . ILE A 1 274 ? 26.057 129.816 -26.800  1.00 37.42  ? 276 ILE A CG2 1 
ATOM   1907 C  CD1 . ILE A 1 274 ? 24.083 129.923 -24.291  1.00 39.16  ? 276 ILE A CD1 1 
ATOM   1908 N  N   . VAL A 1 275 ? 24.138 127.990 -29.031  1.00 35.96  ? 277 VAL A N   1 
ATOM   1909 C  CA  . VAL A 1 275 ? 24.277 127.455 -30.410  1.00 35.43  ? 277 VAL A CA  1 
ATOM   1910 C  C   . VAL A 1 275 ? 24.874 128.518 -31.325  1.00 34.90  ? 277 VAL A C   1 
ATOM   1911 O  O   . VAL A 1 275 ? 24.208 129.546 -31.542  1.00 35.67  ? 277 VAL A O   1 
ATOM   1912 C  CB  . VAL A 1 275 ? 22.929 126.964 -30.953  1.00 36.80  ? 277 VAL A CB  1 
ATOM   1913 C  CG1 . VAL A 1 275 ? 23.086 126.345 -32.325  1.00 36.41  ? 277 VAL A CG1 1 
ATOM   1914 C  CG2 . VAL A 1 275 ? 22.309 125.978 -29.980  1.00 38.37  ? 277 VAL A CG2 1 
ATOM   1915 N  N   . ILE A 1 276 ? 26.034 128.218 -31.906  1.00 33.81  ? 278 ILE A N   1 
ATOM   1916 C  CA  . ILE A 1 276 ? 26.668 129.061 -32.959  1.00 34.39  ? 278 ILE A CA  1 
ATOM   1917 C  C   . ILE A 1 276 ? 26.366 128.467 -34.341  1.00 34.06  ? 278 ILE A C   1 
ATOM   1918 O  O   . ILE A 1 276 ? 26.590 127.275 -34.579  1.00 31.61  ? 278 ILE A O   1 
ATOM   1919 C  CB  . ILE A 1 276 ? 28.181 129.240 -32.740  1.00 34.19  ? 278 ILE A CB  1 
ATOM   1920 C  CG1 . ILE A 1 276 ? 28.493 129.999 -31.452  1.00 34.19  ? 278 ILE A CG1 1 
ATOM   1921 C  CG2 . ILE A 1 276 ? 28.787 129.935 -33.943  1.00 34.67  ? 278 ILE A CG2 1 
ATOM   1922 C  CD1 . ILE A 1 276 ? 28.399 129.160 -30.227  1.00 34.95  ? 278 ILE A CD1 1 
ATOM   1923 N  N   . ARG A 1 277 ? 25.891 129.323 -35.229  1.00 35.16  ? 279 ARG A N   1 
ATOM   1924 C  CA  . ARG A 1 277 ? 25.657 128.966 -36.633  1.00 36.41  ? 279 ARG A CA  1 
ATOM   1925 C  C   . ARG A 1 277 ? 26.372 129.967 -37.508  1.00 34.06  ? 279 ARG A C   1 
ATOM   1926 O  O   . ARG A 1 277 ? 26.358 131.160 -37.179  1.00 33.92  ? 279 ARG A O   1 
ATOM   1927 C  CB  . ARG A 1 277 ? 24.166 128.934 -36.933  1.00 41.29  ? 279 ARG A CB  1 
ATOM   1928 C  CG  . ARG A 1 277 ? 23.530 127.687 -36.359  1.00 44.17  ? 279 ARG A CG  1 
ATOM   1929 C  CD  . ARG A 1 277 ? 22.223 127.370 -37.039  1.00 48.53  ? 279 ARG A CD  1 
ATOM   1930 N  NE  . ARG A 1 277 ? 21.513 126.489 -36.117  1.00 50.39  ? 279 ARG A NE  1 
ATOM   1931 C  CZ  . ARG A 1 277 ? 20.534 126.863 -35.296  1.00 51.88  ? 279 ARG A CZ  1 
ATOM   1932 N  NH1 . ARG A 1 277 ? 20.118 128.124 -35.260  1.00 52.44  ? 279 ARG A NH1 1 
ATOM   1933 N  NH2 . ARG A 1 277 ? 19.989 125.956 -34.502  1.00 53.17  ? 279 ARG A NH2 1 
ATOM   1934 N  N   . TYR A 1 278 ? 27.015 129.441 -38.533  1.00 31.36  ? 280 TYR A N   1 
ATOM   1935 C  CA  . TYR A 1 278 ? 27.706 130.233 -39.571  1.00 31.16  ? 280 TYR A CA  1 
ATOM   1936 C  C   . TYR A 1 278 ? 27.721 129.383 -40.842  1.00 30.20  ? 280 TYR A C   1 
ATOM   1937 O  O   . TYR A 1 278 ? 27.372 128.169 -40.804  1.00 28.91  ? 280 TYR A O   1 
ATOM   1938 C  CB  . TYR A 1 278 ? 29.106 130.661 -39.113  1.00 29.60  ? 280 TYR A CB  1 
ATOM   1939 C  CG  . TYR A 1 278 ? 30.059 129.514 -38.924  1.00 27.79  ? 280 TYR A CG  1 
ATOM   1940 C  CD1 . TYR A 1 278 ? 30.057 128.796 -37.756  1.00 26.64  ? 280 TYR A CD1 1 
ATOM   1941 C  CD2 . TYR A 1 278 ? 30.930 129.117 -39.925  1.00 26.72  ? 280 TYR A CD2 1 
ATOM   1942 C  CE1 . TYR A 1 278 ? 30.911 127.722 -37.576  1.00 25.55  ? 280 TYR A CE1 1 
ATOM   1943 C  CE2 . TYR A 1 278 ? 31.811 128.065 -39.747  1.00 25.23  ? 280 TYR A CE2 1 
ATOM   1944 C  CZ  . TYR A 1 278 ? 31.791 127.350 -38.565  1.00 24.42  ? 280 TYR A CZ  1 
ATOM   1945 O  OH  . TYR A 1 278 ? 32.609 126.279 -38.342  1.00 22.71  ? 280 TYR A OH  1 
ATOM   1946 N  N   . THR A 1 279 ? 28.093 130.010 -41.940  1.00 29.61  ? 281 THR A N   1 
ATOM   1947 C  CA  . THR A 1 279 ? 28.382 129.254 -43.178  1.00 30.09  ? 281 THR A CA  1 
ATOM   1948 C  C   . THR A 1 279 ? 29.847 129.433 -43.548  1.00 29.44  ? 281 THR A C   1 
ATOM   1949 O  O   . THR A 1 279 ? 30.489 130.480 -43.173  1.00 28.36  ? 281 THR A O   1 
ATOM   1950 C  CB  . THR A 1 279 ? 27.448 129.635 -44.329  1.00 31.55  ? 281 THR A CB  1 
ATOM   1951 O  OG1 . THR A 1 279 ? 27.772 130.987 -44.637  1.00 33.16  ? 281 THR A OG1 1 
ATOM   1952 C  CG2 . THR A 1 279 ? 25.979 129.484 -43.987  1.00 32.42  ? 281 THR A CG2 1 
ATOM   1953 N  N   . ALA A 1 280 ? 30.349 128.442 -44.283  1.00 29.51  ? 282 ALA A N   1 
ATOM   1954 C  CA  . ALA A 1 280 ? 31.652 128.513 -44.975  1.00 28.70  ? 282 ALA A CA  1 
ATOM   1955 C  C   . ALA A 1 280 ? 31.510 127.806 -46.328  1.00 29.16  ? 282 ALA A C   1 
ATOM   1956 O  O   . ALA A 1 280 ? 30.592 126.958 -46.501  1.00 30.08  ? 282 ALA A O   1 
ATOM   1957 C  CB  . ALA A 1 280 ? 32.714 127.880 -44.118  1.00 27.03  ? 282 ALA A CB  1 
ATOM   1958 N  N   . ARG A 1 281 ? 32.417 128.064 -47.244  1.00 28.05  ? 283 ARG A N   1 
ATOM   1959 C  CA  . ARG A 1 281 ? 32.358 127.316 -48.518  1.00 29.18  ? 283 ARG A CA  1 
ATOM   1960 C  C   . ARG A 1 281 ? 33.744 126.797 -48.839  1.00 25.72  ? 283 ARG A C   1 
ATOM   1961 O  O   . ARG A 1 281 ? 34.728 127.520 -48.569  1.00 23.62  ? 283 ARG A O   1 
ATOM   1962 C  CB  . ARG A 1 281 ? 31.766 128.188 -49.623  1.00 32.29  ? 283 ARG A CB  1 
ATOM   1963 C  CG  . ARG A 1 281 ? 32.458 129.528 -49.751  1.00 35.76  ? 283 ARG A CG  1 
ATOM   1964 C  CD  . ARG A 1 281 ? 31.720 130.415 -50.736  1.00 42.51  ? 283 ARG A CD  1 
ATOM   1965 N  NE  . ARG A 1 281 ? 32.721 131.327 -51.256  1.00 46.66  ? 283 ARG A NE  1 
ATOM   1966 C  CZ  . ARG A 1 281 ? 33.219 132.368 -50.590  1.00 51.31  ? 283 ARG A CZ  1 
ATOM   1967 N  NH1 . ARG A 1 281 ? 32.776 132.674 -49.381  1.00 53.52  ? 283 ARG A NH1 1 
ATOM   1968 N  NH2 . ARG A 1 281 ? 34.181 133.094 -51.137  1.00 53.72  ? 283 ARG A NH2 1 
ATOM   1969 N  N   . LEU A 1 282 ? 33.785 125.586 -49.395  1.00 24.62  ? 284 LEU A N   1 
ATOM   1970 C  CA  . LEU A 1 282 ? 35.018 125.051 -50.010  1.00 23.08  ? 284 LEU A CA  1 
ATOM   1971 C  C   . LEU A 1 282 ? 35.569 126.074 -51.016  1.00 23.20  ? 284 LEU A C   1 
ATOM   1972 O  O   . LEU A 1 282 ? 34.801 126.737 -51.725  1.00 26.08  ? 284 LEU A O   1 
ATOM   1973 C  CB  . LEU A 1 282 ? 34.705 123.709 -50.654  1.00 22.54  ? 284 LEU A CB  1 
ATOM   1974 C  CG  . LEU A 1 282 ? 34.532 122.535 -49.705  1.00 22.21  ? 284 LEU A CG  1 
ATOM   1975 C  CD1 . LEU A 1 282 ? 33.939 121.361 -50.441  1.00 23.28  ? 284 LEU A CD1 1 
ATOM   1976 C  CD2 . LEU A 1 282 ? 35.849 122.111 -49.089  1.00 22.01  ? 284 LEU A CD2 1 
ATOM   1977 N  N   . ASN A 1 283 ? 36.879 126.213 -51.076  1.00 22.34  ? 285 ASN A N   1 
ATOM   1978 C  CA  . ASN A 1 283 ? 37.546 127.086 -52.057  1.00 22.79  ? 285 ASN A CA  1 
ATOM   1979 C  C   . ASN A 1 283 ? 38.501 126.237 -52.905  1.00 23.54  ? 285 ASN A C   1 
ATOM   1980 O  O   . ASN A 1 283 ? 38.530 125.026 -52.738  1.00 22.72  ? 285 ASN A O   1 
ATOM   1981 C  CB  . ASN A 1 283 ? 38.240 128.216 -51.322  1.00 22.42  ? 285 ASN A CB  1 
ATOM   1982 C  CG  . ASN A 1 283 ? 39.252 127.698 -50.322  1.00 21.45  ? 285 ASN A CG  1 
ATOM   1983 O  OD1 . ASN A 1 283 ? 40.121 126.889 -50.667  1.00 20.57  ? 285 ASN A OD1 1 
ATOM   1984 N  ND2 . ASN A 1 283 ? 39.206 128.234 -49.115  1.00 20.32  ? 285 ASN A ND2 1 
ATOM   1985 N  N   . ASP A 1 284 ? 39.242 126.870 -53.810  1.00 25.99  ? 286 ASP A N   1 
ATOM   1986 C  CA  . ASP A 1 284 ? 40.152 126.207 -54.778  1.00 26.69  ? 286 ASP A CA  1 
ATOM   1987 C  C   . ASP A 1 284 ? 41.226 125.385 -54.056  1.00 26.09  ? 286 ASP A C   1 
ATOM   1988 O  O   . ASP A 1 284 ? 41.686 124.348 -54.617  1.00 25.44  ? 286 ASP A O   1 
ATOM   1989 C  CB  . ASP A 1 284 ? 40.765 127.270 -55.677  1.00 30.27  ? 286 ASP A CB  1 
ATOM   1990 C  CG  . ASP A 1 284 ? 39.741 127.853 -56.641  1.00 34.63  ? 286 ASP A CG  1 
ATOM   1991 O  OD1 . ASP A 1 284 ? 38.656 127.200 -56.853  1.00 35.37  ? 286 ASP A OD1 1 
ATOM   1992 O  OD2 . ASP A 1 284 ? 40.025 128.952 -57.187  1.00 41.73  ? 286 ASP A OD2 1 
ATOM   1993 N  N   . ASP A 1 285 ? 41.612 125.768 -52.841  1.00 25.10  ? 287 ASP A N   1 
ATOM   1994 C  CA  . ASP A 1 285 ? 42.629 125.014 -52.045  1.00 24.70  ? 287 ASP A CA  1 
ATOM   1995 C  C   . ASP A 1 285 ? 42.053 123.771 -51.332  1.00 21.03  ? 287 ASP A C   1 
ATOM   1996 O  O   . ASP A 1 285 ? 42.756 123.196 -50.554  1.00 19.62  ? 287 ASP A O   1 
ATOM   1997 C  CB  . ASP A 1 285 ? 43.277 125.945 -51.029  1.00 27.25  ? 287 ASP A CB  1 
ATOM   1998 C  CG  . ASP A 1 285 ? 43.968 127.131 -51.679  1.00 30.65  ? 287 ASP A CG  1 
ATOM   1999 O  OD1 . ASP A 1 285 ? 44.471 127.029 -52.808  1.00 32.64  ? 287 ASP A OD1 1 
ATOM   2000 O  OD2 . ASP A 1 285 ? 43.995 128.153 -51.040  1.00 37.34  ? 287 ASP A OD2 1 
ATOM   2001 N  N   . ALA A 1 286 ? 40.834 123.357 -51.630  1.00 18.76  ? 288 ALA A N   1 
ATOM   2002 C  CA  . ALA A 1 286 ? 40.140 122.237 -50.977  1.00 17.88  ? 288 ALA A CA  1 
ATOM   2003 C  C   . ALA A 1 286 ? 40.931 120.953 -51.152  1.00 16.88  ? 288 ALA A C   1 
ATOM   2004 O  O   . ALA A 1 286 ? 41.486 120.757 -52.167  1.00 16.76  ? 288 ALA A O   1 
ATOM   2005 C  CB  . ALA A 1 286 ? 38.749 122.094 -51.545  1.00 18.20  ? 288 ALA A CB  1 
ATOM   2006 N  N   . VAL A 1 287 ? 41.012 120.136 -50.120  1.00 16.47  ? 289 VAL A N   1 
ATOM   2007 C  CA  . VAL A 1 287 ? 41.562 118.758 -50.181  1.00 16.13  ? 289 VAL A CA  1 
ATOM   2008 C  C   . VAL A 1 287 ? 40.539 117.861 -50.856  1.00 16.19  ? 289 VAL A C   1 
ATOM   2009 O  O   . VAL A 1 287 ? 39.355 117.932 -50.518  1.00 16.88  ? 289 VAL A O   1 
ATOM   2010 C  CB  . VAL A 1 287 ? 41.827 118.240 -48.769  1.00 16.18  ? 289 VAL A CB  1 
ATOM   2011 C  CG1 . VAL A 1 287 ? 42.056 116.737 -48.761  1.00 16.16  ? 289 VAL A CG1 1 
ATOM   2012 C  CG2 . VAL A 1 287 ? 42.956 119.019 -48.104  1.00 16.65  ? 289 VAL A CG2 1 
ATOM   2013 N  N   . MET A 1 288 ? 41.002 116.967 -51.705  1.00 16.94  ? 290 MET A N   1 
ATOM   2014 C  CA  . MET A 1 288 ? 40.132 116.047 -52.467  1.00 17.38  ? 290 MET A CA  1 
ATOM   2015 C  C   . MET A 1 288 ? 40.156 114.698 -51.760  1.00 17.21  ? 290 MET A C   1 
ATOM   2016 O  O   . MET A 1 288 ? 41.229 114.154 -51.563  1.00 17.20  ? 290 MET A O   1 
ATOM   2017 C  CB  . MET A 1 288 ? 40.625 115.887 -53.913  1.00 18.74  ? 290 MET A CB  1 
ATOM   2018 C  CG  . MET A 1 288 ? 40.759 117.218 -54.673  1.00 19.18  ? 290 MET A CG  1 
ATOM   2019 S  SD  . MET A 1 288 ? 39.159 117.997 -55.006  1.00 20.87  ? 290 MET A SD  1 
ATOM   2020 C  CE  . MET A 1 288 ? 39.702 119.446 -55.898  1.00 21.62  ? 290 MET A CE  1 
ATOM   2021 N  N   . GLY A 1 289 ? 38.996 114.122 -51.471  1.00 17.05  ? 291 GLY A N   1 
ATOM   2022 C  CA  . GLY A 1 289 ? 38.952 112.812 -50.810  1.00 17.62  ? 291 GLY A CA  1 
ATOM   2023 C  C   . GLY A 1 289 ? 39.758 112.855 -49.524  1.00 17.38  ? 291 GLY A C   1 
ATOM   2024 O  O   . GLY A 1 289 ? 39.833 113.942 -48.900  1.00 16.74  ? 291 GLY A O   1 
ATOM   2025 N  N   . GLY A 1 290 ? 40.347 111.711 -49.175  1.00 18.06  ? 292 GLY A N   1 
ATOM   2026 C  CA  . GLY A 1 290 ? 41.361 111.553 -48.125  1.00 18.80  ? 292 GLY A CA  1 
ATOM   2027 C  C   . GLY A 1 290 ? 40.817 111.944 -46.767  1.00 18.72  ? 292 GLY A C   1 
ATOM   2028 O  O   . GLY A 1 290 ? 39.690 111.529 -46.434  1.00 19.56  ? 292 GLY A O   1 
ATOM   2029 N  N   . LEU A 1 291 ? 41.553 112.792 -46.051  1.00 18.26  ? 293 LEU A N   1 
ATOM   2030 C  CA  . LEU A 1 291 ? 41.220 113.277 -44.691  1.00 18.00  ? 293 LEU A CA  1 
ATOM   2031 C  C   . LEU A 1 291 ? 40.271 114.484 -44.777  1.00 17.28  ? 293 LEU A C   1 
ATOM   2032 O  O   . LEU A 1 291 ? 39.958 115.086 -43.736  1.00 15.91  ? 293 LEU A O   1 
ATOM   2033 C  CB  . LEU A 1 291 ? 42.537 113.687 -44.040  1.00 18.21  ? 293 LEU A CB  1 
ATOM   2034 C  CG  . LEU A 1 291 ? 43.542 112.554 -43.839  1.00 19.58  ? 293 LEU A CG  1 
ATOM   2035 C  CD1 . LEU A 1 291 ? 44.699 113.036 -42.988  1.00 19.78  ? 293 LEU A CD1 1 
ATOM   2036 C  CD2 . LEU A 1 291 ? 42.893 111.342 -43.185  1.00 20.73  ? 293 LEU A CD2 1 
ATOM   2037 N  N   . GLY A 1 292 ? 39.941 114.952 -45.983  1.00 16.68  ? 294 GLY A N   1 
ATOM   2038 C  CA  . GLY A 1 292 ? 38.935 116.020 -46.136  1.00 16.53  ? 294 GLY A CA  1 
ATOM   2039 C  C   . GLY A 1 292 ? 39.374 117.374 -45.614  1.00 16.12  ? 294 GLY A C   1 
ATOM   2040 O  O   . GLY A 1 292 ? 40.532 117.596 -45.496  1.00 16.74  ? 294 GLY A O   1 
ATOM   2041 N  N   . ASN A 1 293 ? 38.436 118.250 -45.292  1.00 16.41  ? 295 ASN A N   1 
ATOM   2042 C  CA  . ASN A 1 293 ? 38.690 119.664 -44.917  1.00 16.34  ? 295 ASN A CA  1 
ATOM   2043 C  C   . ASN A 1 293 ? 38.057 119.882 -43.561  1.00 16.58  ? 295 ASN A C   1 
ATOM   2044 O  O   . ASN A 1 293 ? 36.908 120.290 -43.469  1.00 17.17  ? 295 ASN A O   1 
ATOM   2045 C  CB  . ASN A 1 293 ? 38.123 120.597 -45.993  1.00 16.50  ? 295 ASN A CB  1 
ATOM   2046 C  CG  . ASN A 1 293 ? 38.649 120.308 -47.381  1.00 16.11  ? 295 ASN A CG  1 
ATOM   2047 O  OD1 . ASN A 1 293 ? 39.607 120.911 -47.861  1.00 15.96  ? 295 ASN A OD1 1 
ATOM   2048 N  ND2 . ASN A 1 293 ? 38.028 119.360 -48.034  1.00 16.57  ? 295 ASN A ND2 1 
ATOM   2049 N  N   . PRO A 1 294 ? 38.705 119.475 -42.445  1.00 16.37  ? 296 PRO A N   1 
ATOM   2050 C  CA  . PRO A 1 294 ? 38.049 119.544 -41.150  1.00 16.19  ? 296 PRO A CA  1 
ATOM   2051 C  C   . PRO A 1 294 ? 38.169 120.920 -40.496  1.00 15.99  ? 296 PRO A C   1 
ATOM   2052 O  O   . PRO A 1 294 ? 39.147 121.606 -40.609  1.00 15.75  ? 296 PRO A O   1 
ATOM   2053 C  CB  . PRO A 1 294 ? 38.805 118.516 -40.310  1.00 16.28  ? 296 PRO A CB  1 
ATOM   2054 C  CG  . PRO A 1 294 ? 40.224 118.625 -40.843  1.00 16.68  ? 296 PRO A CG  1 
ATOM   2055 C  CD  . PRO A 1 294 ? 40.051 118.888 -42.344  1.00 16.52  ? 296 PRO A CD  1 
ATOM   2056 N  N   . ASN A 1 295 ? 37.123 121.277 -39.778  1.00 16.61  ? 297 ASN A N   1 
ATOM   2057 C  CA  . ASN A 1 295 ? 37.167 122.374 -38.789  1.00 16.56  ? 297 ASN A CA  1 
ATOM   2058 C  C   . ASN A 1 295 ? 37.118 121.765 -37.381  1.00 16.80  ? 297 ASN A C   1 
ATOM   2059 O  O   . ASN A 1 295 ? 36.413 120.773 -37.128  1.00 17.10  ? 297 ASN A O   1 
ATOM   2060 C  CB  . ASN A 1 295 ? 36.066 123.390 -39.044  1.00 16.83  ? 297 ASN A CB  1 
ATOM   2061 C  CG  . ASN A 1 295 ? 34.689 122.828 -38.701  1.00 17.55  ? 297 ASN A CG  1 
ATOM   2062 O  OD1 . ASN A 1 295 ? 34.168 121.974 -39.429  1.00 16.62  ? 297 ASN A OD1 1 
ATOM   2063 N  N   . ILE A 1 296 ? 37.842 122.398 -36.480  1.00 16.87  ? 298 ILE A N   1 
ATOM   2064 C  CA  . ILE A 1 296 ? 38.011 121.903 -35.097  1.00 16.96  ? 298 ILE A CA  1 
ATOM   2065 C  C   . ILE A 1 296 ? 37.664 123.048 -34.155  1.00 17.54  ? 298 ILE A C   1 
ATOM   2066 O  O   . ILE A 1 296 ? 38.179 124.146 -34.321  1.00 17.04  ? 298 ILE A O   1 
ATOM   2067 C  CB  . ILE A 1 296 ? 39.426 121.333 -34.902  1.00 16.79  ? 298 ILE A CB  1 
ATOM   2068 C  CG1 . ILE A 1 296 ? 39.723 120.250 -35.940  1.00 16.73  ? 298 ILE A CG1 1 
ATOM   2069 C  CG2 . ILE A 1 296 ? 39.579 120.791 -33.517  1.00 17.22  ? 298 ILE A CG2 1 
ATOM   2070 C  CD1 . ILE A 1 296 ? 41.156 119.809 -35.989  1.00 17.00  ? 298 ILE A CD1 1 
ATOM   2071 N  N   . ALA A 1 297 ? 36.775 122.766 -33.212  1.00 18.34  ? 299 ALA A N   1 
ATOM   2072 C  CA  . ALA A 1 297 ? 36.300 123.725 -32.205  1.00 19.31  ? 299 ALA A CA  1 
ATOM   2073 C  C   . ALA A 1 297 ? 36.564 123.144 -30.819  1.00 20.44  ? 299 ALA A C   1 
ATOM   2074 O  O   . ALA A 1 297 ? 36.504 121.902 -30.673  1.00 19.25  ? 299 ALA A O   1 
ATOM   2075 C  CB  . ALA A 1 297 ? 34.851 123.968 -32.449  1.00 19.87  ? 299 ALA A CB  1 
ATOM   2076 N  N   . ARG A 1 298 ? 36.924 123.992 -29.854  1.00 22.91  ? 300 ARG A N   1 
ATOM   2077 C  CA  . ARG A 1 298 ? 36.972 123.599 -28.410  1.00 24.99  ? 300 ARG A CA  1 
ATOM   2078 C  C   . ARG A 1 298 ? 36.422 124.788 -27.613  1.00 23.84  ? 300 ARG A C   1 
ATOM   2079 O  O   . ARG A 1 298 ? 36.427 125.933 -28.163  1.00 22.37  ? 300 ARG A O   1 
ATOM   2080 C  CB  . ARG A 1 298 ? 38.382 123.161 -28.007  1.00 28.74  ? 300 ARG A CB  1 
ATOM   2081 C  CG  . ARG A 1 298 ? 39.408 124.176 -28.452  1.00 34.60  ? 300 ARG A CG  1 
ATOM   2082 C  CD  . ARG A 1 298 ? 40.713 124.266 -27.691  1.00 41.92  ? 300 ARG A CD  1 
ATOM   2083 N  NE  . ARG A 1 298 ? 41.608 125.336 -28.179  1.00 48.64  ? 300 ARG A NE  1 
ATOM   2084 C  CZ  . ARG A 1 298 ? 41.770 125.739 -29.465  1.00 52.96  ? 300 ARG A CZ  1 
ATOM   2085 N  NH1 . ARG A 1 298 ? 42.613 126.730 -29.734  1.00 55.12  ? 300 ARG A NH1 1 
ATOM   2086 N  NH2 . ARG A 1 298 ? 41.120 125.170 -30.478  1.00 52.64  ? 300 ARG A NH2 1 
ATOM   2087 N  N   . LEU A 1 299 ? 35.886 124.532 -26.406  1.00 22.96  ? 301 LEU A N   1 
ATOM   2088 C  CA  . LEU A 1 299 ? 35.343 125.593 -25.511  1.00 20.95  ? 301 LEU A CA  1 
ATOM   2089 C  C   . LEU A 1 299 ? 36.304 125.762 -24.338  1.00 19.84  ? 301 LEU A C   1 
ATOM   2090 O  O   . LEU A 1 299 ? 36.663 124.768 -23.714  1.00 19.16  ? 301 LEU A O   1 
ATOM   2091 C  CB  . LEU A 1 299 ? 33.928 125.204 -25.078  1.00 21.12  ? 301 LEU A CB  1 
ATOM   2092 C  CG  . LEU A 1 299 ? 33.387 125.936 -23.855  1.00 21.92  ? 301 LEU A CG  1 
ATOM   2093 C  CD1 . LEU A 1 299 ? 32.926 127.345 -24.208  1.00 22.07  ? 301 LEU A CD1 1 
ATOM   2094 C  CD2 . LEU A 1 299 ? 32.248 125.159 -23.201  1.00 22.08  ? 301 LEU A CD2 1 
ATOM   2095 N  N   . THR A 1 300 ? 36.728 126.988 -24.074  1.00 19.01  ? 302 THR A N   1 
ATOM   2096 C  CA  . THR A 1 300 ? 37.397 127.338 -22.812  1.00 19.06  ? 302 THR A CA  1 
ATOM   2097 C  C   . THR A 1 300 ? 36.369 127.798 -21.777  1.00 18.79  ? 302 THR A C   1 
ATOM   2098 O  O   . THR A 1 300 ? 35.581 128.692 -22.074  1.00 18.59  ? 302 THR A O   1 
ATOM   2099 C  CB  . THR A 1 300 ? 38.503 128.350 -23.006  1.00 19.44  ? 302 THR A CB  1 
ATOM   2100 O  OG1 . THR A 1 300 ? 39.316 127.655 -23.930  1.00 20.41  ? 302 THR A OG1 1 
ATOM   2101 C  CG2 . THR A 1 300 ? 39.294 128.590 -21.742  1.00 19.97  ? 302 THR A CG2 1 
ATOM   2102 N  N   . TYR A 1 301 ? 36.372 127.159 -20.614  1.00 18.51  ? 303 TYR A N   1 
ATOM   2103 C  CA  . TYR A 1 301 ? 35.335 127.368 -19.569  1.00 18.71  ? 303 TYR A CA  1 
ATOM   2104 C  C   . TYR A 1 301 ? 35.946 127.422 -18.175  1.00 18.34  ? 303 TYR A C   1 
ATOM   2105 O  O   . TYR A 1 301 ? 36.922 126.693 -17.926  1.00 17.75  ? 303 TYR A O   1 
ATOM   2106 C  CB  . TYR A 1 301 ? 34.335 126.223 -19.638  1.00 18.61  ? 303 TYR A CB  1 
ATOM   2107 C  CG  . TYR A 1 301 ? 34.926 124.845 -19.431  1.00 18.29  ? 303 TYR A CG  1 
ATOM   2108 C  CD1 . TYR A 1 301 ? 34.990 124.295 -18.156  1.00 17.82  ? 303 TYR A CD1 1 
ATOM   2109 C  CD2 . TYR A 1 301 ? 35.355 124.072 -20.504  1.00 17.25  ? 303 TYR A CD2 1 
ATOM   2110 C  CE1 . TYR A 1 301 ? 35.465 123.015 -17.944  1.00 18.05  ? 303 TYR A CE1 1 
ATOM   2111 C  CE2 . TYR A 1 301 ? 35.833 122.788 -20.306  1.00 17.85  ? 303 TYR A CE2 1 
ATOM   2112 C  CZ  . TYR A 1 301 ? 35.883 122.259 -19.020  1.00 18.40  ? 303 TYR A CZ  1 
ATOM   2113 O  OH  . TYR A 1 301 ? 36.406 121.021 -18.815  1.00 19.25  ? 303 TYR A OH  1 
ATOM   2114 N  N   . SER A 1 302 ? 35.370 128.253 -17.299  1.00 18.72  ? 304 SER A N   1 
ATOM   2115 C  CA  . SER A 1 302 ? 35.665 128.264 -15.837  1.00 19.42  ? 304 SER A CA  1 
ATOM   2116 C  C   . SER A 1 302 ? 35.469 126.849 -15.269  1.00 19.15  ? 304 SER A C   1 
ATOM   2117 O  O   . SER A 1 302 ? 34.363 126.263 -15.453  1.00 18.52  ? 304 SER A O   1 
ATOM   2118 C  CB  . SER A 1 302 ? 34.833 129.288 -15.136  1.00 19.70  ? 304 SER A CB  1 
ATOM   2119 O  OG  . SER A 1 302 ? 35.213 130.581 -15.555  1.00 20.68  ? 304 SER A OG  1 
ATOM   2120 N  N   . ASN A 1 303 ? 36.518 126.276 -14.672  1.00 19.46  ? 305 ASN A N   1 
ATOM   2121 C  CA  . ASN A 1 303 ? 36.477 124.848 -14.235  1.00 20.98  ? 305 ASN A CA  1 
ATOM   2122 C  C   . ASN A 1 303 ? 36.503 124.731 -12.701  1.00 21.32  ? 305 ASN A C   1 
ATOM   2123 O  O   . ASN A 1 303 ? 36.713 123.603 -12.217  1.00 21.08  ? 305 ASN A O   1 
ATOM   2124 C  CB  . ASN A 1 303 ? 37.627 124.019 -14.810  1.00 21.90  ? 305 ASN A CB  1 
ATOM   2125 C  CG  . ASN A 1 303 ? 38.975 124.557 -14.403  1.00 23.49  ? 305 ASN A CG  1 
ATOM   2126 O  OD1 . ASN A 1 303 ? 39.081 125.709 -13.982  1.00 24.92  ? 305 ASN A OD1 1 
ATOM   2127 N  ND2 . ASN A 1 303 ? 40.019 123.754 -14.550  1.00 25.30  ? 305 ASN A ND2 1 
ATOM   2128 N  N   . ASP A 1 304 ? 36.342 125.825 -11.953  1.00 21.77  ? 306 ASP A N   1 
ATOM   2129 C  CA  . ASP A 1 304 ? 36.396 125.726 -10.453  1.00 23.02  ? 306 ASP A CA  1 
ATOM   2130 C  C   . ASP A 1 304 ? 35.352 126.628 -9.809   1.00 23.25  ? 306 ASP A C   1 
ATOM   2131 O  O   . ASP A 1 304 ? 35.524 127.841 -9.707   1.00 23.31  ? 306 ASP A O   1 
ATOM   2132 C  CB  . ASP A 1 304 ? 37.785 126.054 -9.915   1.00 23.42  ? 306 ASP A CB  1 
ATOM   2133 C  CG  . ASP A 1 304 ? 37.938 125.780 -8.433   1.00 24.77  ? 306 ASP A CG  1 
ATOM   2134 O  OD1 . ASP A 1 304 ? 36.948 125.366 -7.806   1.00 25.66  ? 306 ASP A OD1 1 
ATOM   2135 O  OD2 . ASP A 1 304 ? 39.039 125.943 -7.941   1.00 25.00  ? 306 ASP A OD2 1 
ATOM   2136 N  N   . PRO A 1 305 ? 34.264 126.065 -9.266   1.00 25.06  ? 307 PRO A N   1 
ATOM   2137 C  CA  . PRO A 1 305 ? 33.232 126.887 -8.626   1.00 25.96  ? 307 PRO A CA  1 
ATOM   2138 C  C   . PRO A 1 305 ? 33.576 127.479 -7.244   1.00 26.58  ? 307 PRO A C   1 
ATOM   2139 O  O   . PRO A 1 305 ? 32.779 128.263 -6.747   1.00 26.20  ? 307 PRO A O   1 
ATOM   2140 C  CB  . PRO A 1 305 ? 32.069 125.891 -8.525   1.00 26.05  ? 307 PRO A CB  1 
ATOM   2141 C  CG  . PRO A 1 305 ? 32.761 124.563 -8.290   1.00 26.39  ? 307 PRO A CG  1 
ATOM   2142 C  CD  . PRO A 1 305 ? 33.995 124.625 -9.166   1.00 25.98  ? 307 PRO A CD  1 
ATOM   2143 N  N   . ASN A 1 306 ? 34.756 127.177 -6.696   1.00 28.90  ? 308 ASN A N   1 
ATOM   2144 C  CA  . ASN A 1 306 ? 35.121 127.454 -5.283   1.00 31.81  ? 308 ASN A CA  1 
ATOM   2145 C  C   . ASN A 1 306 ? 35.711 128.853 -5.165   1.00 37.24  ? 308 ASN A C   1 
ATOM   2146 O  O   . ASN A 1 306 ? 36.938 128.993 -5.432   1.00 43.02  ? 308 ASN A O   1 
ATOM   2147 C  CB  . ASN A 1 306 ? 36.130 126.444 -4.755   1.00 30.49  ? 308 ASN A CB  1 
ATOM   2148 C  CG  . ASN A 1 306 ? 35.520 125.072 -4.687   1.00 30.14  ? 308 ASN A CG  1 
ATOM   2149 O  OD1 . ASN A 1 306 ? 34.619 124.877 -3.873   1.00 28.38  ? 308 ASN A OD1 1 
ATOM   2150 N  ND2 . ASN A 1 306 ? 35.953 124.166 -5.568   1.00 29.02  ? 308 ASN A ND2 1 
ATOM   2151 N  N   . GLY A 1 307 ? 34.877 129.833 -4.794   1.00 40.93  ? 309 GLY A N   1 
ATOM   2152 C  CA  . GLY A 1 307 ? 35.288 131.201 -4.407   1.00 43.64  ? 309 GLY A CA  1 
ATOM   2153 C  C   . GLY A 1 307 ? 35.844 132.021 -5.576   1.00 45.92  ? 309 GLY A C   1 
ATOM   2154 O  O   . GLY A 1 307 ? 35.479 131.740 -6.747   1.00 48.74  ? 309 GLY A O   1 
ATOM   2155 N  N   . PHE A 1 308 ? 36.697 133.005 -5.269   1.00 46.33  ? 310 PHE A N   1 
ATOM   2156 C  CA  . PHE A 1 308 ? 37.336 133.919 -6.247   1.00 48.08  ? 310 PHE A CA  1 
ATOM   2157 C  C   . PHE A 1 308 ? 38.484 133.161 -6.913   1.00 49.81  ? 310 PHE A C   1 
ATOM   2158 O  O   . PHE A 1 308 ? 39.572 133.032 -6.333   1.00 50.80  ? 310 PHE A O   1 
ATOM   2159 C  CB  . PHE A 1 308 ? 37.830 135.216 -5.594   1.00 48.89  ? 310 PHE A CB  1 
ATOM   2160 C  CG  . PHE A 1 308 ? 36.786 136.052 -4.893   1.00 49.70  ? 310 PHE A CG  1 
ATOM   2161 C  CD1 . PHE A 1 308 ? 35.461 136.070 -5.335   1.00 49.43  ? 310 PHE A CD1 1 
ATOM   2162 C  CD2 . PHE A 1 308 ? 37.143 136.856 -3.813   1.00 47.14  ? 310 PHE A CD2 1 
ATOM   2163 C  CE1 . PHE A 1 308 ? 34.513 136.860 -4.693   1.00 49.27  ? 310 PHE A CE1 1 
ATOM   2164 C  CE2 . PHE A 1 308 ? 36.195 137.654 -3.192   1.00 47.38  ? 310 PHE A CE2 1 
ATOM   2165 C  CZ  . PHE A 1 308 ? 34.883 137.646 -3.620   1.00 48.60  ? 310 PHE A CZ  1 
ATOM   2166 N  N   . THR A 1 309 ? 38.237 132.650 -8.117   1.00 51.90  ? 311 THR A N   1 
ATOM   2167 C  CA  . THR A 1 309 ? 39.240 131.885 -8.898   1.00 50.69  ? 311 THR A CA  1 
ATOM   2168 C  C   . THR A 1 309 ? 39.092 132.320 -10.345  1.00 48.41  ? 311 THR A C   1 
ATOM   2169 O  O   . THR A 1 309 ? 37.974 132.684 -10.742  1.00 50.79  ? 311 THR A O   1 
ATOM   2170 C  CB  . THR A 1 309 ? 39.096 130.364 -8.688   1.00 53.65  ? 311 THR A CB  1 
ATOM   2171 O  OG1 . THR A 1 309 ? 39.902 129.713 -9.672   1.00 54.66  ? 311 THR A OG1 1 
ATOM   2172 C  CG2 . THR A 1 309 ? 37.674 129.840 -8.781   1.00 53.15  ? 311 THR A CG2 1 
ATOM   2173 N  N   . SER A 1 310 ? 40.172 132.311 -11.108  1.00 44.07  ? 312 SER A N   1 
ATOM   2174 C  CA  . SER A 1 310 ? 40.068 132.506 -12.570  1.00 41.85  ? 312 SER A CA  1 
ATOM   2175 C  C   . SER A 1 310 ? 40.787 131.382 -13.327  1.00 37.26  ? 312 SER A C   1 
ATOM   2176 O  O   . SER A 1 310 ? 41.381 131.713 -14.328  1.00 38.72  ? 312 SER A O   1 
ATOM   2177 C  CB  . SER A 1 310 ? 40.440 133.939 -13.036  1.00 43.04  ? 312 SER A CB  1 
ATOM   2178 O  OG  . SER A 1 310 ? 41.688 134.425 -12.580  1.00 42.61  ? 312 SER A OG  1 
ATOM   2179 N  N   . THR A 1 311 ? 40.632 130.110 -12.933  1.00 32.74  ? 313 THR A N   1 
ATOM   2180 C  CA  . THR A 1 311 ? 41.176 128.950 -13.692  1.00 30.63  ? 313 THR A CA  1 
ATOM   2181 C  C   . THR A 1 311 ? 40.174 128.515 -14.759  1.00 27.93  ? 313 THR A C   1 
ATOM   2182 O  O   . THR A 1 311 ? 38.960 128.689 -14.557  1.00 26.08  ? 313 THR A O   1 
ATOM   2183 C  CB  . THR A 1 311 ? 41.530 127.708 -12.853  1.00 30.98  ? 313 THR A CB  1 
ATOM   2184 O  OG1 . THR A 1 311 ? 40.387 127.149 -12.216  1.00 30.29  ? 313 THR A OG1 1 
ATOM   2185 C  CG2 . THR A 1 311 ? 42.542 127.970 -11.765  1.00 32.03  ? 313 THR A CG2 1 
ATOM   2186 N  N   . THR A 1 312 ? 40.699 127.911 -15.823  1.00 26.65  ? 314 THR A N   1 
ATOM   2187 C  CA  . THR A 1 312 ? 39.912 127.359 -16.945  1.00 26.85  ? 314 THR A CA  1 
ATOM   2188 C  C   . THR A 1 312 ? 40.442 125.999 -17.426  1.00 26.10  ? 314 THR A C   1 
ATOM   2189 O  O   . THR A 1 312 ? 41.594 125.626 -17.174  1.00 26.59  ? 314 THR A O   1 
ATOM   2190 C  CB  . THR A 1 312 ? 39.867 128.340 -18.119  1.00 25.97  ? 314 THR A CB  1 
ATOM   2191 O  OG1 . THR A 1 312 ? 41.214 128.613 -18.462  1.00 26.86  ? 314 THR A OG1 1 
ATOM   2192 C  CG2 . THR A 1 312 ? 39.162 129.630 -17.771  1.00 26.59  ? 314 THR A CG2 1 
ATOM   2193 N  N   . ALA A 1 313 ? 39.549 125.258 -18.057  1.00 24.34  ? 315 ALA A N   1 
ATOM   2194 C  CA  . ALA A 1 313 ? 39.869 124.056 -18.825  1.00 24.10  ? 315 ALA A CA  1 
ATOM   2195 C  C   . ALA A 1 313 ? 39.350 124.268 -20.246  1.00 23.28  ? 315 ALA A C   1 
ATOM   2196 O  O   . ALA A 1 313 ? 38.526 125.164 -20.483  1.00 21.44  ? 315 ALA A O   1 
ATOM   2197 C  CB  . ALA A 1 313 ? 39.276 122.858 -18.152  1.00 23.74  ? 315 ALA A CB  1 
ATOM   2198 N  N   . GLU A 1 314 ? 39.833 123.458 -21.164  1.00 24.51  ? 316 GLU A N   1 
ATOM   2199 C  CA  . GLU A 1 314 ? 39.305 123.451 -22.542  1.00 25.66  ? 316 GLU A CA  1 
ATOM   2200 C  C   . GLU A 1 314 ? 38.589 122.114 -22.666  1.00 23.97  ? 316 GLU A C   1 
ATOM   2201 O  O   . GLU A 1 314 ? 39.082 121.144 -22.062  1.00 24.07  ? 316 GLU A O   1 
ATOM   2202 C  CB  . GLU A 1 314 ? 40.407 123.615 -23.602  1.00 28.35  ? 316 GLU A CB  1 
ATOM   2203 C  CG  . GLU A 1 314 ? 41.323 124.829 -23.439  1.00 31.02  ? 316 GLU A CG  1 
ATOM   2204 C  CD  . GLU A 1 314 ? 42.591 124.755 -24.322  1.00 35.52  ? 316 GLU A CD  1 
ATOM   2205 O  OE1 . GLU A 1 314 ? 43.590 124.067 -23.947  1.00 38.41  ? 316 GLU A OE1 1 
ATOM   2206 O  OE2 . GLU A 1 314 ? 42.614 125.364 -25.408  1.00 38.76  ? 316 GLU A OE2 1 
ATOM   2207 N  N   . THR A 1 315 ? 37.474 122.076 -23.378  1.00 21.98  ? 317 THR A N   1 
ATOM   2208 C  CA  . THR A 1 315 ? 36.797 120.816 -23.754  1.00 21.94  ? 317 THR A CA  1 
ATOM   2209 C  C   . THR A 1 315 ? 37.700 120.057 -24.713  1.00 23.86  ? 317 THR A C   1 
ATOM   2210 O  O   . THR A 1 315 ? 38.587 120.653 -25.337  1.00 23.70  ? 317 THR A O   1 
ATOM   2211 C  CB  . THR A 1 315 ? 35.471 121.065 -24.467  1.00 20.73  ? 317 THR A CB  1 
ATOM   2212 O  OG1 . THR A 1 315 ? 35.822 121.799 -25.649  1.00 19.62  ? 317 THR A OG1 1 
ATOM   2213 C  CG2 . THR A 1 315 ? 34.477 121.825 -23.626  1.00 19.95  ? 317 THR A CG2 1 
ATOM   2214 N  N   . PRO A 1 316 ? 37.488 118.729 -24.883  1.00 25.72  ? 318 PRO A N   1 
ATOM   2215 C  CA  . PRO A 1 316 ? 38.144 117.982 -25.952  1.00 26.36  ? 318 PRO A CA  1 
ATOM   2216 C  C   . PRO A 1 316 ? 37.777 118.653 -27.285  1.00 25.86  ? 318 PRO A C   1 
ATOM   2217 O  O   . PRO A 1 316 ? 36.753 119.247 -27.377  1.00 26.16  ? 318 PRO A O   1 
ATOM   2218 C  CB  . PRO A 1 316 ? 37.577 116.567 -25.802  1.00 26.66  ? 318 PRO A CB  1 
ATOM   2219 C  CG  . PRO A 1 316 ? 37.225 116.493 -24.355  1.00 27.66  ? 318 PRO A CG  1 
ATOM   2220 C  CD  . PRO A 1 316 ? 36.655 117.860 -24.039  1.00 26.70  ? 318 PRO A CD  1 
ATOM   2221 N  N   . ASP A 1 317 ? 38.676 118.651 -28.258  1.00 28.11  ? 319 ASP A N   1 
ATOM   2222 C  CA  . ASP A 1 317 ? 38.389 119.094 -29.653  1.00 26.57  ? 319 ASP A CA  1 
ATOM   2223 C  C   . ASP A 1 317 ? 37.084 118.426 -30.108  1.00 25.47  ? 319 ASP A C   1 
ATOM   2224 O  O   . ASP A 1 317 ? 36.875 117.222 -29.798  1.00 26.36  ? 319 ASP A O   1 
ATOM   2225 C  CB  . ASP A 1 317 ? 39.571 118.735 -30.552  1.00 28.32  ? 319 ASP A CB  1 
ATOM   2226 C  CG  . ASP A 1 317 ? 40.810 119.594 -30.316  1.00 31.00  ? 319 ASP A CG  1 
ATOM   2227 O  OD1 . ASP A 1 317 ? 40.656 120.754 -29.828  1.00 33.57  ? 319 ASP A OD1 1 
ATOM   2228 O  OD2 . ASP A 1 317 ? 41.931 119.108 -30.607  1.00 32.86  ? 319 ASP A OD2 1 
ATOM   2229 N  N   . THR A 1 318 ? 36.200 119.184 -30.746  1.00 23.45  ? 320 THR A N   1 
ATOM   2230 C  CA  . THR A 1 318 ? 35.085 118.654 -31.564  1.00 22.75  ? 320 THR A CA  1 
ATOM   2231 C  C   . THR A 1 318 ? 35.318 119.074 -33.032  1.00 22.59  ? 320 THR A C   1 
ATOM   2232 O  O   . THR A 1 318 ? 35.634 120.244 -33.319  1.00 21.15  ? 320 THR A O   1 
ATOM   2233 C  CB  . THR A 1 318 ? 33.748 119.112 -30.986  1.00 22.91  ? 320 THR A CB  1 
ATOM   2234 O  OG1 . THR A 1 318 ? 32.649 118.584 -31.720  1.00 21.57  ? 320 THR A OG1 1 
ATOM   2235 C  CG2 . THR A 1 318 ? 33.596 120.617 -31.010  1.00 23.26  ? 320 THR A CG2 1 
ATOM   2236 N  N   . LYS A 1 319 ? 35.073 118.152 -33.948  1.00 23.30  ? 321 LYS A N   1 
ATOM   2237 C  CA  . LYS A 1 319 ? 35.465 118.232 -35.380  1.00 23.40  ? 321 LYS A CA  1 
ATOM   2238 C  C   . LYS A 1 319 ? 34.221 118.015 -36.261  1.00 23.34  ? 321 LYS A C   1 
ATOM   2239 O  O   . LYS A 1 319 ? 33.427 117.131 -35.958  1.00 23.83  ? 321 LYS A O   1 
ATOM   2240 C  CB  . LYS A 1 319 ? 36.581 117.199 -35.535  1.00 24.74  ? 321 LYS A CB  1 
ATOM   2241 C  CG  . LYS A 1 319 ? 37.220 117.071 -36.900  1.00 27.35  ? 321 LYS A CG  1 
ATOM   2242 C  CD  . LYS A 1 319 ? 38.240 115.893 -36.972  1.00 29.45  ? 321 LYS A CD  1 
ATOM   2243 C  CE  . LYS A 1 319 ? 39.084 115.890 -38.243  1.00 30.83  ? 321 LYS A CE  1 
ATOM   2244 N  NZ  . LYS A 1 319 ? 39.483 114.532 -38.728  1.00 32.13  ? 321 LYS A NZ  1 
ATOM   2245 N  N   . ALA A 1 320 ? 34.036 118.810 -37.319  1.00 22.43  ? 322 ALA A N   1 
ATOM   2246 C  CA  . ALA A 1 320 ? 33.206 118.450 -38.499  1.00 21.88  ? 322 ALA A CA  1 
ATOM   2247 C  C   . ALA A 1 320 ? 34.092 118.337 -39.743  1.00 20.89  ? 322 ALA A C   1 
ATOM   2248 O  O   . ALA A 1 320 ? 35.246 118.777 -39.720  1.00 19.94  ? 322 ALA A O   1 
ATOM   2249 C  CB  . ALA A 1 320 ? 32.125 119.457 -38.728  1.00 21.57  ? 322 ALA A CB  1 
ATOM   2250 N  N   . ASN A 1 321 ? 33.532 117.820 -40.817  1.00 21.47  ? 323 ASN A N   1 
ATOM   2251 C  CA  . ASN A 1 321 ? 34.315 117.504 -42.024  1.00 21.52  ? 323 ASN A CA  1 
ATOM   2252 C  C   . ASN A 1 321 ? 33.431 117.650 -43.263  1.00 22.49  ? 323 ASN A C   1 
ATOM   2253 O  O   . ASN A 1 321 ? 32.254 117.266 -43.251  1.00 24.17  ? 323 ASN A O   1 
ATOM   2254 C  CB  . ASN A 1 321 ? 35.024 116.147 -41.922  1.00 21.83  ? 323 ASN A CB  1 
ATOM   2255 C  CG  . ASN A 1 321 ? 36.364 116.170 -42.643  1.00 22.35  ? 323 ASN A CG  1 
ATOM   2256 O  OD1 . ASN A 1 321 ? 36.639 117.051 -43.488  1.00 22.98  ? 323 ASN A OD1 1 
ATOM   2257 N  ND2 . ASN A 1 321 ? 37.176 115.168 -42.389  1.00 21.12  ? 323 ASN A ND2 1 
ATOM   2258 N  N   . VAL A 1 322 ? 34.006 118.230 -44.295  1.00 21.08  ? 324 VAL A N   1 
ATOM   2259 C  CA  . VAL A 1 322 ? 33.410 118.298 -45.644  1.00 21.08  ? 324 VAL A CA  1 
ATOM   2260 C  C   . VAL A 1 322 ? 34.428 117.736 -46.627  1.00 20.33  ? 324 VAL A C   1 
ATOM   2261 O  O   . VAL A 1 322 ? 35.534 118.251 -46.696  1.00 19.27  ? 324 VAL A O   1 
ATOM   2262 C  CB  . VAL A 1 322 ? 33.058 119.745 -45.982  1.00 21.62  ? 324 VAL A CB  1 
ATOM   2263 C  CG1 . VAL A 1 322 ? 32.349 119.825 -47.327  1.00 22.00  ? 324 VAL A CG1 1 
ATOM   2264 C  CG2 . VAL A 1 322 ? 32.235 120.348 -44.872  1.00 22.14  ? 324 VAL A CG2 1 
ATOM   2265 N  N   . TYR A 1 323 ? 34.062 116.688 -47.337  1.00 20.56  ? 325 TYR A N   1 
ATOM   2266 C  CA  . TYR A 1 323 ? 34.891 116.075 -48.400  1.00 19.86  ? 325 TYR A CA  1 
ATOM   2267 C  C   . TYR A 1 323 ? 34.421 116.606 -49.743  1.00 19.37  ? 325 TYR A C   1 
ATOM   2268 O  O   . TYR A 1 323 ? 33.294 117.061 -49.867  1.00 19.20  ? 325 TYR A O   1 
ATOM   2269 C  CB  . TYR A 1 323 ? 34.745 114.563 -48.386  1.00 20.62  ? 325 TYR A CB  1 
ATOM   2270 C  CG  . TYR A 1 323 ? 35.138 113.960 -47.072  1.00 21.59  ? 325 TYR A CG  1 
ATOM   2271 C  CD1 . TYR A 1 323 ? 36.455 113.630 -46.822  1.00 22.07  ? 325 TYR A CD1 1 
ATOM   2272 C  CD2 . TYR A 1 323 ? 34.205 113.722 -46.072  1.00 22.33  ? 325 TYR A CD2 1 
ATOM   2273 C  CE1 . TYR A 1 323 ? 36.839 113.082 -45.600  1.00 22.66  ? 325 TYR A CE1 1 
ATOM   2274 C  CE2 . TYR A 1 323 ? 34.567 113.146 -44.869  1.00 22.83  ? 325 TYR A CE2 1 
ATOM   2275 C  CZ  . TYR A 1 323 ? 35.889 112.817 -44.637  1.00 22.65  ? 325 TYR A CZ  1 
ATOM   2276 O  OH  . TYR A 1 323 ? 36.289 112.286 -43.451  1.00 22.61  ? 325 TYR A OH  1 
ATOM   2277 N  N   . THR A 1 324 ? 35.300 116.571 -50.730  1.00 20.06  ? 326 THR A N   1 
ATOM   2278 C  CA  . THR A 1 324 ? 34.939 116.832 -52.150  1.00 19.50  ? 326 THR A CA  1 
ATOM   2279 C  C   . THR A 1 324 ? 35.829 115.947 -53.014  1.00 19.64  ? 326 THR A C   1 
ATOM   2280 O  O   . THR A 1 324 ? 36.857 115.493 -52.485  1.00 19.72  ? 326 THR A O   1 
ATOM   2281 C  CB  . THR A 1 324 ? 35.015 118.339 -52.407  1.00 19.24  ? 326 THR A CB  1 
ATOM   2282 O  OG1 . THR A 1 324 ? 34.330 118.639 -53.612  1.00 19.76  ? 326 THR A OG1 1 
ATOM   2283 C  CG2 . THR A 1 324 ? 36.429 118.857 -52.440  1.00 19.11  ? 326 THR A CG2 1 
ATOM   2284 N  N   . TYR A 1 325 ? 35.465 115.731 -54.282  1.00 19.56  ? 327 TYR A N   1 
ATOM   2285 C  CA  . TYR A 1 325 ? 36.133 114.755 -55.179  1.00 20.08  ? 327 TYR A CA  1 
ATOM   2286 C  C   . TYR A 1 325 ? 36.518 115.492 -56.459  1.00 19.61  ? 327 TYR A C   1 
ATOM   2287 O  O   . TYR A 1 325 ? 36.072 116.649 -56.747  1.00 19.11  ? 327 TYR A O   1 
ATOM   2288 C  CB  . TYR A 1 325 ? 35.264 113.509 -55.414  1.00 21.08  ? 327 TYR A CB  1 
ATOM   2289 C  CG  . TYR A 1 325 ? 34.466 113.115 -54.195  1.00 22.66  ? 327 TYR A CG  1 
ATOM   2290 C  CD1 . TYR A 1 325 ? 35.104 112.696 -53.038  1.00 22.69  ? 327 TYR A CD1 1 
ATOM   2291 C  CD2 . TYR A 1 325 ? 33.083 113.252 -54.148  1.00 23.38  ? 327 TYR A CD2 1 
ATOM   2292 C  CE1 . TYR A 1 325 ? 34.403 112.380 -51.888  1.00 23.73  ? 327 TYR A CE1 1 
ATOM   2293 C  CE2 . TYR A 1 325 ? 32.365 112.931 -53.005  1.00 23.81  ? 327 TYR A CE2 1 
ATOM   2294 C  CZ  . TYR A 1 325 ? 33.027 112.526 -51.853  1.00 23.95  ? 327 TYR A CZ  1 
ATOM   2295 O  OH  . TYR A 1 325 ? 32.337 112.241 -50.703  1.00 23.02  ? 327 TYR A OH  1 
ATOM   2296 N  N   . GLN A 1 326 ? 37.340 114.816 -57.243  1.00 19.65  ? 328 GLN A N   1 
ATOM   2297 C  CA  . GLN A 1 326 ? 37.839 115.352 -58.523  1.00 18.98  ? 328 GLN A CA  1 
ATOM   2298 C  C   . GLN A 1 326 ? 37.591 114.333 -59.643  1.00 18.29  ? 328 GLN A C   1 
ATOM   2299 O  O   . GLN A 1 326 ? 38.059 113.192 -59.522  1.00 18.37  ? 328 GLN A O   1 
ATOM   2300 C  CB  . GLN A 1 326 ? 39.313 115.675 -58.323  1.00 19.21  ? 328 GLN A CB  1 
ATOM   2301 C  CG  . GLN A 1 326 ? 39.963 116.147 -59.613  1.00 19.65  ? 328 GLN A CG  1 
ATOM   2302 C  CD  . GLN A 1 326 ? 41.388 116.538 -59.339  1.00 20.51  ? 328 GLN A CD  1 
ATOM   2303 O  OE1 . GLN A 1 326 ? 41.832 116.605 -58.188  1.00 22.14  ? 328 GLN A OE1 1 
ATOM   2304 N  NE2 . GLN A 1 326 ? 42.129 116.743 -60.408  1.00 20.33  ? 328 GLN A NE2 1 
ATOM   2305 N  N   . LEU A 1 327 ? 36.882 114.719 -60.696  1.00 17.79  ? 329 LEU A N   1 
ATOM   2306 C  CA  . LEU A 1 327 ? 36.836 113.903 -61.944  1.00 17.39  ? 329 LEU A CA  1 
ATOM   2307 C  C   . LEU A 1 327 ? 37.992 114.303 -62.873  1.00 17.20  ? 329 LEU A C   1 
ATOM   2308 O  O   . LEU A 1 327 ? 38.155 115.484 -63.191  1.00 16.71  ? 329 LEU A O   1 
ATOM   2309 C  CB  . LEU A 1 327 ? 35.484 114.095 -62.606  1.00 17.69  ? 329 LEU A CB  1 
ATOM   2310 C  CG  . LEU A 1 327 ? 35.315 113.529 -64.019  1.00 17.73  ? 329 LEU A CG  1 
ATOM   2311 C  CD1 . LEU A 1 327 ? 35.251 112.001 -64.052  1.00 18.01  ? 329 LEU A CD1 1 
ATOM   2312 C  CD2 . LEU A 1 327 ? 34.066 114.100 -64.658  1.00 18.17  ? 329 LEU A CD2 1 
ATOM   2313 N  N   . LYS A 1 328 ? 38.809 113.330 -63.259  1.00 17.41  ? 330 LYS A N   1 
ATOM   2314 C  CA  . LYS A 1 328 ? 39.890 113.480 -64.247  1.00 16.67  ? 330 LYS A CA  1 
ATOM   2315 C  C   . LYS A 1 328 ? 39.498 112.734 -65.516  1.00 16.78  ? 330 LYS A C   1 
ATOM   2316 O  O   . LYS A 1 328 ? 39.445 111.520 -65.456  1.00 17.35  ? 330 LYS A O   1 
ATOM   2317 C  CB  . LYS A 1 328 ? 41.197 112.910 -63.706  1.00 16.99  ? 330 LYS A CB  1 
ATOM   2318 C  CG  . LYS A 1 328 ? 42.383 113.116 -64.635  1.00 16.82  ? 330 LYS A CG  1 
ATOM   2319 C  CD  . LYS A 1 328 ? 43.589 112.368 -64.238  1.00 17.38  ? 330 LYS A CD  1 
ATOM   2320 C  CE  . LYS A 1 328 ? 44.207 112.955 -62.999  1.00 17.41  ? 330 LYS A CE  1 
ATOM   2321 N  NZ  . LYS A 1 328 ? 44.533 114.389 -63.199  1.00 17.15  ? 330 LYS A NZ  1 
ATOM   2322 N  N   . VAL A 1 329 ? 39.259 113.459 -66.603  1.00 16.38  ? 331 VAL A N   1 
ATOM   2323 C  CA  . VAL A 1 329 ? 38.925 112.891 -67.942  1.00 16.58  ? 331 VAL A CA  1 
ATOM   2324 C  C   . VAL A 1 329 ? 40.173 112.945 -68.831  1.00 17.09  ? 331 VAL A C   1 
ATOM   2325 O  O   . VAL A 1 329 ? 40.702 114.045 -69.087  1.00 16.82  ? 331 VAL A O   1 
ATOM   2326 C  CB  . VAL A 1 329 ? 37.749 113.630 -68.595  1.00 16.28  ? 331 VAL A CB  1 
ATOM   2327 C  CG1 . VAL A 1 329 ? 37.376 113.015 -69.951  1.00 16.13  ? 331 VAL A CG1 1 
ATOM   2328 C  CG2 . VAL A 1 329 ? 36.555 113.690 -67.652  1.00 16.44  ? 331 VAL A CG2 1 
ATOM   2329 N  N   . ASN A 1 330 ? 40.639 111.783 -69.270  1.00 17.60  ? 332 ASN A N   1 
ATOM   2330 C  CA  . ASN A 1 330 ? 41.763 111.675 -70.218  1.00 18.23  ? 332 ASN A CA  1 
ATOM   2331 C  C   . ASN A 1 330 ? 41.190 111.458 -71.633  1.00 18.48  ? 332 ASN A C   1 
ATOM   2332 O  O   . ASN A 1 330 ? 40.443 110.493 -71.854  1.00 18.67  ? 332 ASN A O   1 
ATOM   2333 C  CB  . ASN A 1 330 ? 42.706 110.559 -69.824  1.00 19.07  ? 332 ASN A CB  1 
ATOM   2334 C  CG  . ASN A 1 330 ? 43.488 110.883 -68.581  1.00 19.80  ? 332 ASN A CG  1 
ATOM   2335 O  OD1 . ASN A 1 330 ? 44.066 111.954 -68.459  1.00 19.80  ? 332 ASN A OD1 1 
ATOM   2336 N  ND2 . ASN A 1 330 ? 43.486 109.961 -67.635  1.00 21.23  ? 332 ASN A ND2 1 
ATOM   2337 N  N   . LYS A 1 331 ? 41.478 112.371 -72.542  1.00 18.57  ? 333 LYS A N   1 
ATOM   2338 C  CA  . LYS A 1 331 ? 41.051 112.258 -73.964  1.00 19.96  ? 333 LYS A CA  1 
ATOM   2339 C  C   . LYS A 1 331 ? 42.140 111.543 -74.763  1.00 20.07  ? 333 LYS A C   1 
ATOM   2340 O  O   . LYS A 1 331 ? 43.226 112.099 -74.845  1.00 19.00  ? 333 LYS A O   1 
ATOM   2341 C  CB  . LYS A 1 331 ? 40.800 113.648 -74.545  1.00 20.54  ? 333 LYS A CB  1 
ATOM   2342 C  CG  . LYS A 1 331 ? 39.797 113.674 -75.690  1.00 22.10  ? 333 LYS A CG  1 
ATOM   2343 C  CD  . LYS A 1 331 ? 39.473 112.301 -76.260  1.00 23.23  ? 333 LYS A CD  1 
ATOM   2344 C  CE  . LYS A 1 331 ? 38.159 112.267 -76.997  1.00 24.32  ? 333 LYS A CE  1 
ATOM   2345 N  NZ  . LYS A 1 331 ? 38.010 111.000 -77.745  1.00 25.09  ? 333 LYS A NZ  1 
ATOM   2346 N  N   . VAL A 1 332 ? 41.857 110.357 -75.300  1.00 21.30  ? 334 VAL A N   1 
ATOM   2347 C  CA  . VAL A 1 332 ? 42.854 109.557 -76.061  1.00 23.18  ? 334 VAL A CA  1 
ATOM   2348 C  C   . VAL A 1 332 ? 42.208 109.016 -77.338  1.00 25.11  ? 334 VAL A C   1 
ATOM   2349 O  O   . VAL A 1 332 ? 40.997 109.217 -77.573  1.00 23.75  ? 334 VAL A O   1 
ATOM   2350 C  CB  . VAL A 1 332 ? 43.475 108.420 -75.237  1.00 24.13  ? 334 VAL A CB  1 
ATOM   2351 C  CG1 . VAL A 1 332 ? 44.194 108.950 -74.015  1.00 25.51  ? 334 VAL A CG1 1 
ATOM   2352 C  CG2 . VAL A 1 332 ? 42.438 107.402 -74.821  1.00 24.75  ? 334 VAL A CG2 1 
ATOM   2353 N  N   . LYS A 1 333 ? 43.043 108.403 -78.162  1.00 28.44  ? 335 LYS A N   1 
ATOM   2354 C  CA  . LYS A 1 333 ? 42.616 107.683 -79.388  1.00 32.72  ? 335 LYS A CA  1 
ATOM   2355 C  C   . LYS A 1 333 ? 42.979 106.205 -79.189  1.00 37.96  ? 335 LYS A C   1 
ATOM   2356 O  O   . LYS A 1 333 ? 43.533 105.873 -78.089  1.00 40.13  ? 335 LYS A O   1 
ATOM   2357 C  CB  . LYS A 1 333 ? 43.214 108.350 -80.630  1.00 31.93  ? 335 LYS A CB  1 
ATOM   2358 C  CG  . LYS A 1 333 ? 44.708 108.586 -80.576  1.00 32.22  ? 335 LYS A CG  1 
ATOM   2359 C  CD  . LYS A 1 333 ? 45.114 109.678 -81.512  1.00 32.65  ? 335 LYS A CD  1 
ATOM   2360 C  CE  . LYS A 1 333 ? 46.554 110.059 -81.257  1.00 34.54  ? 335 LYS A CE  1 
ATOM   2361 N  NZ  . LYS A 1 333 ? 47.038 111.032 -82.265  1.00 36.18  ? 335 LYS A NZ  1 
ATOM   2362 N  N   . GLU A 1 334 ? 42.648 105.342 -80.161  1.00 40.86  ? 336 GLU A N   1 
ATOM   2363 C  CA  . GLU A 1 334 ? 42.527 103.882 -79.912  1.00 43.20  ? 336 GLU A CA  1 
ATOM   2364 C  C   . GLU A 1 334 ? 43.902 103.342 -79.517  1.00 42.64  ? 336 GLU A C   1 
ATOM   2365 O  O   . GLU A 1 334 ? 43.947 102.399 -78.704  1.00 44.47  ? 336 GLU A O   1 
ATOM   2366 C  CB  . GLU A 1 334 ? 41.851 103.209 -81.103  1.00 47.19  ? 336 GLU A CB  1 
ATOM   2367 C  CG  . GLU A 1 334 ? 40.401 103.640 -81.255  1.00 50.13  ? 336 GLU A CG  1 
ATOM   2368 C  CD  . GLU A 1 334 ? 39.692 103.245 -82.548  1.00 54.97  ? 336 GLU A CD  1 
ATOM   2369 O  OE1 . GLU A 1 334 ? 40.077 103.737 -83.656  1.00 57.70  ? 336 GLU A OE1 1 
ATOM   2370 O  OE2 . GLU A 1 334 ? 38.727 102.469 -82.452  1.00 57.86  ? 336 GLU A OE2 1 
ATOM   2371 N  N   . ASN A 1 335 ? 44.980 103.992 -79.955  1.00 41.46  ? 337 ASN A N   1 
ATOM   2372 C  CA  . ASN A 1 335 ? 46.360 103.577 -79.590  1.00 43.56  ? 337 ASN A CA  1 
ATOM   2373 C  C   . ASN A 1 335 ? 46.756 104.133 -78.208  1.00 43.73  ? 337 ASN A C   1 
ATOM   2374 O  O   . ASN A 1 335 ? 47.973 104.077 -77.887  1.00 44.39  ? 337 ASN A O   1 
ATOM   2375 C  CB  . ASN A 1 335 ? 47.354 103.976 -80.681  1.00 44.08  ? 337 ASN A CB  1 
ATOM   2376 C  CG  . ASN A 1 335 ? 47.509 105.469 -80.851  1.00 43.31  ? 337 ASN A CG  1 
ATOM   2377 O  OD1 . ASN A 1 335 ? 47.528 106.218 -79.881  1.00 43.82  ? 337 ASN A OD1 1 
ATOM   2378 N  ND2 . ASN A 1 335 ? 47.628 105.916 -82.084  1.00 41.18  ? 337 ASN A ND2 1 
ATOM   2379 N  N   . GLN A 1 336 ? 45.809 104.741 -77.478  1.00 41.63  ? 338 GLN A N   1 
ATOM   2380 C  CA  . GLN A 1 336 ? 45.974 105.219 -76.072  1.00 42.73  ? 338 GLN A CA  1 
ATOM   2381 C  C   . GLN A 1 336 ? 46.908 106.434 -75.987  1.00 39.71  ? 338 GLN A C   1 
ATOM   2382 O  O   . GLN A 1 336 ? 47.185 106.829 -74.872  1.00 38.21  ? 338 GLN A O   1 
ATOM   2383 C  CB  . GLN A 1 336 ? 46.522 104.115 -75.153  1.00 45.01  ? 338 GLN A CB  1 
ATOM   2384 C  CG  . GLN A 1 336 ? 45.690 102.843 -75.187  1.00 46.29  ? 338 GLN A CG  1 
ATOM   2385 C  CD  . GLN A 1 336 ? 44.301 103.137 -74.692  1.00 46.24  ? 338 GLN A CD  1 
ATOM   2386 O  OE1 . GLN A 1 336 ? 44.091 103.383 -73.510  1.00 50.24  ? 338 GLN A OE1 1 
ATOM   2387 N  NE2 . GLN A 1 336 ? 43.337 103.147 -75.591  1.00 44.85  ? 338 GLN A NE2 1 
ATOM   2388 N  N   . GLN A 1 337 ? 47.364 107.009 -77.104  1.00 37.96  ? 339 GLN A N   1 
ATOM   2389 C  CA  . GLN A 1 337 ? 48.104 108.304 -77.095  1.00 36.98  ? 339 GLN A CA  1 
ATOM   2390 C  C   . GLN A 1 337 ? 47.065 109.425 -76.915  1.00 31.58  ? 339 GLN A C   1 
ATOM   2391 O  O   . GLN A 1 337 ? 45.871 109.245 -77.228  1.00 29.20  ? 339 GLN A O   1 
ATOM   2392 C  CB  . GLN A 1 337 ? 49.023 108.495 -78.325  1.00 40.86  ? 339 GLN A CB  1 
ATOM   2393 C  CG  . GLN A 1 337 ? 50.384 107.768 -78.258  1.00 45.92  ? 339 GLN A CG  1 
ATOM   2394 C  CD  . GLN A 1 337 ? 51.380 108.292 -77.226  1.00 50.18  ? 339 GLN A CD  1 
ATOM   2395 O  OE1 . GLN A 1 337 ? 51.115 109.263 -76.507  1.00 52.70  ? 339 GLN A OE1 1 
ATOM   2396 N  NE2 . GLN A 1 337 ? 52.550 107.660 -77.127  1.00 50.45  ? 339 GLN A NE2 1 
ATOM   2397 N  N   . ALA A 1 338 ? 47.514 110.545 -76.377  1.00 29.18  ? 340 ALA A N   1 
ATOM   2398 C  CA  . ALA A 1 338 ? 46.666 111.703 -76.062  1.00 26.61  ? 340 ALA A CA  1 
ATOM   2399 C  C   . ALA A 1 338 ? 46.058 112.213 -77.367  1.00 24.61  ? 340 ALA A C   1 
ATOM   2400 O  O   . ALA A 1 338 ? 46.768 112.171 -78.348  1.00 26.02  ? 340 ALA A O   1 
ATOM   2401 C  CB  . ALA A 1 338 ? 47.507 112.758 -75.400  1.00 26.81  ? 340 ALA A CB  1 
ATOM   2402 N  N   . LEU A 1 339 ? 44.815 112.706 -77.346  1.00 21.82  ? 341 LEU A N   1 
ATOM   2403 C  CA  . LEU A 1 339 ? 44.185 113.422 -78.479  1.00 20.44  ? 341 LEU A CA  1 
ATOM   2404 C  C   . LEU A 1 339 ? 43.915 114.847 -78.036  1.00 19.21  ? 341 LEU A C   1 
ATOM   2405 O  O   . LEU A 1 339 ? 43.128 115.021 -77.113  1.00 19.87  ? 341 LEU A O   1 
ATOM   2406 C  CB  . LEU A 1 339 ? 42.874 112.733 -78.881  1.00 20.05  ? 341 LEU A CB  1 
ATOM   2407 C  CG  . LEU A 1 339 ? 42.103 113.351 -80.047  1.00 19.83  ? 341 LEU A CG  1 
ATOM   2408 C  CD1 . LEU A 1 339 ? 42.974 113.530 -81.282  1.00 20.41  ? 341 LEU A CD1 1 
ATOM   2409 C  CD2 . LEU A 1 339 ? 40.932 112.475 -80.445  1.00 19.86  ? 341 LEU A CD2 1 
ATOM   2410 N  N   . ALA A 1 340 ? 44.546 115.822 -78.673  1.00 18.51  ? 342 ALA A N   1 
ATOM   2411 C  CA  . ALA A 1 340 ? 44.256 117.266 -78.474  1.00 18.22  ? 342 ALA A CA  1 
ATOM   2412 C  C   . ALA A 1 340 ? 42.916 117.634 -79.083  1.00 17.09  ? 342 ALA A C   1 
ATOM   2413 O  O   . ALA A 1 340 ? 42.449 116.882 -79.972  1.00 16.38  ? 342 ALA A O   1 
ATOM   2414 C  CB  . ALA A 1 340 ? 45.322 118.140 -79.073  1.00 19.13  ? 342 ALA A CB  1 
ATOM   2415 N  N   . GLY A 1 341 ? 42.354 118.748 -78.621  1.00 16.70  ? 343 GLY A N   1 
ATOM   2416 C  CA  . GLY A 1 341 ? 41.311 119.482 -79.352  1.00 17.61  ? 343 GLY A CA  1 
ATOM   2417 C  C   . GLY A 1 341 ? 39.922 119.117 -78.898  1.00 17.61  ? 343 GLY A C   1 
ATOM   2418 O  O   . GLY A 1 341 ? 38.972 119.483 -79.598  1.00 18.69  ? 343 GLY A O   1 
ATOM   2419 N  N   . ALA A 1 342 ? 39.785 118.320 -77.856  1.00 17.22  ? 344 ALA A N   1 
ATOM   2420 C  CA  . ALA A 1 342 ? 38.477 117.991 -77.247  1.00 17.86  ? 344 ALA A CA  1 
ATOM   2421 C  C   . ALA A 1 342 ? 38.112 119.071 -76.212  1.00 18.87  ? 344 ALA A C   1 
ATOM   2422 O  O   . ALA A 1 342 ? 39.015 119.742 -75.630  1.00 19.80  ? 344 ALA A O   1 
ATOM   2423 C  CB  . ALA A 1 342 ? 38.502 116.627 -76.597  1.00 17.53  ? 344 ALA A CB  1 
ATOM   2424 N  N   . GLY A 1 343 ? 36.821 119.265 -76.004  1.00 19.13  ? 345 GLY A N   1 
ATOM   2425 C  CA  . GLY A 1 343 ? 36.284 120.068 -74.899  1.00 19.77  ? 345 GLY A CA  1 
ATOM   2426 C  C   . GLY A 1 343 ? 35.158 119.314 -74.245  1.00 19.70  ? 345 GLY A C   1 
ATOM   2427 O  O   . GLY A 1 343 ? 34.483 118.534 -74.953  1.00 20.41  ? 345 GLY A O   1 
ATOM   2428 N  N   . PHE A 1 344 ? 34.936 119.540 -72.957  1.00 19.70  ? 346 PHE A N   1 
ATOM   2429 C  CA  . PHE A 1 344 ? 33.950 118.782 -72.156  1.00 19.20  ? 346 PHE A CA  1 
ATOM   2430 C  C   . PHE A 1 344 ? 33.170 119.749 -71.277  1.00 20.69  ? 346 PHE A C   1 
ATOM   2431 O  O   . PHE A 1 344 ? 33.746 120.707 -70.740  1.00 20.73  ? 346 PHE A O   1 
ATOM   2432 C  CB  . PHE A 1 344 ? 34.625 117.728 -71.289  1.00 17.56  ? 346 PHE A CB  1 
ATOM   2433 C  CG  . PHE A 1 344 ? 35.166 116.555 -72.042  1.00 16.77  ? 346 PHE A CG  1 
ATOM   2434 C  CD1 . PHE A 1 344 ? 34.339 115.514 -72.388  1.00 17.30  ? 346 PHE A CD1 1 
ATOM   2435 C  CD2 . PHE A 1 344 ? 36.492 116.493 -72.426  1.00 16.40  ? 346 PHE A CD2 1 
ATOM   2436 C  CE1 . PHE A 1 344 ? 34.826 114.430 -73.110  1.00 17.40  ? 346 PHE A CE1 1 
ATOM   2437 C  CE2 . PHE A 1 344 ? 36.978 115.411 -73.145  1.00 16.61  ? 346 PHE A CE2 1 
ATOM   2438 C  CZ  . PHE A 1 344 ? 36.141 114.381 -73.503  1.00 16.69  ? 346 PHE A CZ  1 
ATOM   2439 N  N   . THR A 1 345 ? 31.869 119.465 -71.149  1.00 22.13  ? 347 THR A N   1 
ATOM   2440 C  CA  . THR A 1 345 ? 30.931 120.151 -70.237  1.00 23.09  ? 347 THR A CA  1 
ATOM   2441 C  C   . THR A 1 345 ? 30.393 119.102 -69.266  1.00 22.80  ? 347 THR A C   1 
ATOM   2442 O  O   . THR A 1 345 ? 30.120 117.980 -69.677  1.00 22.17  ? 347 THR A O   1 
ATOM   2443 C  CB  . THR A 1 345 ? 29.878 120.929 -71.028  1.00 24.32  ? 347 THR A CB  1 
ATOM   2444 O  OG1 . THR A 1 345 ? 30.571 121.838 -71.891  1.00 24.33  ? 347 THR A OG1 1 
ATOM   2445 C  CG2 . THR A 1 345 ? 28.965 121.700 -70.104  1.00 25.61  ? 347 THR A CG2 1 
ATOM   2446 N  N   . LEU A 1 346 ? 30.400 119.450 -67.988  1.00 23.90  ? 348 LEU A N   1 
ATOM   2447 C  CA  . LEU A 1 346 ? 29.886 118.588 -66.907  1.00 24.49  ? 348 LEU A CA  1 
ATOM   2448 C  C   . LEU A 1 346 ? 28.677 119.270 -66.318  1.00 26.34  ? 348 LEU A C   1 
ATOM   2449 O  O   . LEU A 1 346 ? 28.720 120.465 -66.035  1.00 27.07  ? 348 LEU A O   1 
ATOM   2450 C  CB  . LEU A 1 346 ? 30.940 118.383 -65.836  1.00 23.74  ? 348 LEU A CB  1 
ATOM   2451 C  CG  . LEU A 1 346 ? 30.539 117.454 -64.694  1.00 23.55  ? 348 LEU A CG  1 
ATOM   2452 C  CD1 . LEU A 1 346 ? 30.427 116.009 -65.143  1.00 23.34  ? 348 LEU A CD1 1 
ATOM   2453 C  CD2 . LEU A 1 346 ? 31.549 117.566 -63.581  1.00 22.92  ? 348 LEU A CD2 1 
ATOM   2454 N  N   . TYR A 1 347 ? 27.631 118.493 -66.162  1.00 28.63  ? 349 TYR A N   1 
ATOM   2455 C  CA  . TYR A 1 347 ? 26.343 118.965 -65.622  1.00 31.22  ? 349 TYR A CA  1 
ATOM   2456 C  C   . TYR A 1 347 ? 26.091 118.160 -64.367  1.00 32.09  ? 349 TYR A C   1 
ATOM   2457 O  O   . TYR A 1 347 ? 26.454 116.956 -64.337  1.00 30.73  ? 349 TYR A O   1 
ATOM   2458 C  CB  . TYR A 1 347 ? 25.206 118.745 -66.629  1.00 32.73  ? 349 TYR A CB  1 
ATOM   2459 C  CG  . TYR A 1 347 ? 25.309 119.482 -67.943  1.00 32.75  ? 349 TYR A CG  1 
ATOM   2460 C  CD1 . TYR A 1 347 ? 25.933 118.911 -69.041  1.00 31.94  ? 349 TYR A CD1 1 
ATOM   2461 C  CD2 . TYR A 1 347 ? 24.725 120.726 -68.106  1.00 34.05  ? 349 TYR A CD2 1 
ATOM   2462 C  CE1 . TYR A 1 347 ? 25.995 119.565 -70.262  1.00 32.25  ? 349 TYR A CE1 1 
ATOM   2463 C  CE2 . TYR A 1 347 ? 24.775 121.393 -69.320  1.00 34.34  ? 349 TYR A CE2 1 
ATOM   2464 C  CZ  . TYR A 1 347 ? 25.403 120.805 -70.396  1.00 33.37  ? 349 TYR A CZ  1 
ATOM   2465 O  OH  . TYR A 1 347 ? 25.441 121.490 -71.561  1.00 34.15  ? 349 TYR A OH  1 
ATOM   2466 N  N   . LYS A 1 348 ? 25.455 118.793 -63.385  1.00 35.40  ? 350 LYS A N   1 
ATOM   2467 C  CA  . LYS A 1 348 ? 24.938 118.057 -62.213  1.00 37.19  ? 350 LYS A CA  1 
ATOM   2468 C  C   . LYS A 1 348 ? 23.417 118.097 -62.260  1.00 41.92  ? 350 LYS A C   1 
ATOM   2469 O  O   . LYS A 1 348 ? 22.869 119.164 -62.610  1.00 43.25  ? 350 LYS A O   1 
ATOM   2470 C  CB  . LYS A 1 348 ? 25.483 118.619 -60.901  1.00 36.90  ? 350 LYS A CB  1 
ATOM   2471 C  CG  . LYS A 1 348 ? 25.201 117.710 -59.715  1.00 36.43  ? 350 LYS A CG  1 
ATOM   2472 C  CD  . LYS A 1 348 ? 25.635 118.219 -58.386  1.00 35.64  ? 350 LYS A CD  1 
ATOM   2473 C  CE  . LYS A 1 348 ? 25.291 117.240 -57.287  1.00 35.99  ? 350 LYS A CE  1 
ATOM   2474 N  NZ  . LYS A 1 348 ? 25.376 117.912 -55.972  1.00 37.29  ? 350 LYS A NZ  1 
ATOM   2475 N  N   . LYS A 1 349 ? 22.773 116.972 -61.931  1.00 47.22  ? 351 LYS A N   1 
ATOM   2476 C  CA  . LYS A 1 349 ? 21.303 116.926 -61.700  1.00 54.15  ? 351 LYS A CA  1 
ATOM   2477 C  C   . LYS A 1 349 ? 21.028 117.575 -60.334  1.00 55.52  ? 351 LYS A C   1 
ATOM   2478 O  O   . LYS A 1 349 ? 21.436 117.004 -59.288  1.00 48.96  ? 351 LYS A O   1 
ATOM   2479 C  CB  . LYS A 1 349 ? 20.785 115.490 -61.802  1.00 58.58  ? 351 LYS A CB  1 
ATOM   2480 C  CG  . LYS A 1 349 ? 19.266 115.373 -61.752  1.00 65.16  ? 351 LYS A CG  1 
ATOM   2481 C  CD  . LYS A 1 349 ? 18.720 113.940 -61.770  1.00 67.71  ? 351 LYS A CD  1 
ATOM   2482 C  CE  . LYS A 1 349 ? 18.745 113.295 -63.142  1.00 67.86  ? 351 LYS A CE  1 
ATOM   2483 N  NZ  . LYS A 1 349 ? 18.859 111.820 -63.020  1.00 68.62  ? 351 LYS A NZ  1 
ATOM   2484 N  N   . VAL A 1 350 ? 20.435 118.768 -60.348  1.00 61.29  ? 352 VAL A N   1 
ATOM   2485 C  CA  . VAL A 1 350 ? 20.183 119.565 -59.111  1.00 66.76  ? 352 VAL A CA  1 
ATOM   2486 C  C   . VAL A 1 350 ? 18.741 119.297 -58.645  1.00 71.99  ? 352 VAL A C   1 
ATOM   2487 O  O   . VAL A 1 350 ? 18.557 118.908 -57.473  1.00 75.10  ? 352 VAL A O   1 
ATOM   2488 C  CB  . VAL A 1 350 ? 20.480 121.061 -59.340  1.00 65.28  ? 352 VAL A CB  1 
ATOM   2489 C  CG1 . VAL A 1 350 ? 20.077 121.938 -58.167  1.00 66.14  ? 352 VAL A CG1 1 
ATOM   2490 C  CG2 . VAL A 1 350 ? 21.941 121.266 -59.658  1.00 62.03  ? 352 VAL A CG2 1 
ATOM   2491 N  N   . ASN A 1 351 ? 17.757 119.465 -59.527  1.00 75.95  ? 353 ASN A N   1 
ATOM   2492 C  CA  . ASN A 1 351 ? 16.326 119.306 -59.173  1.00 79.95  ? 353 ASN A CA  1 
ATOM   2493 C  C   . ASN A 1 351 ? 15.648 118.558 -60.311  1.00 80.10  ? 353 ASN A C   1 
ATOM   2494 O  O   . ASN A 1 351 ? 14.745 119.111 -60.905  1.00 81.51  ? 353 ASN A O   1 
ATOM   2495 C  CB  . ASN A 1 351 ? 15.685 120.668 -58.904  1.00 84.13  ? 353 ASN A CB  1 
ATOM   2496 C  CG  . ASN A 1 351 ? 16.345 121.414 -57.761  1.00 85.80  ? 353 ASN A CG  1 
ATOM   2497 O  OD1 . ASN A 1 351 ? 16.845 122.522 -57.947  1.00 87.67  ? 353 ASN A OD1 1 
ATOM   2498 N  ND2 . ASN A 1 351 ? 16.369 120.816 -56.579  1.00 82.73  ? 353 ASN A ND2 1 
ATOM   2499 N  N   . ASN A 1 352 ? 16.107 117.347 -60.610  1.00 81.69  ? 354 ASN A N   1 
ATOM   2500 C  CA  . ASN A 1 352 ? 15.779 116.645 -61.881  1.00 84.74  ? 354 ASN A CA  1 
ATOM   2501 C  C   . ASN A 1 352 ? 16.000 117.610 -63.062  1.00 83.32  ? 354 ASN A C   1 
ATOM   2502 O  O   . ASN A 1 352 ? 15.168 117.646 -63.987  1.00 82.07  ? 354 ASN A O   1 
ATOM   2503 C  CB  . ASN A 1 352 ? 14.376 116.050 -61.792  1.00 88.85  ? 354 ASN A CB  1 
ATOM   2504 C  CG  . ASN A 1 352 ? 14.352 114.859 -60.861  1.00 91.53  ? 354 ASN A CG  1 
ATOM   2505 O  OD1 . ASN A 1 352 ? 14.192 113.731 -61.322  1.00 95.47  ? 354 ASN A OD1 1 
ATOM   2506 N  ND2 . ASN A 1 352 ? 14.559 115.090 -59.570  1.00 91.72  ? 354 ASN A ND2 1 
ATOM   2507 N  N   . GLN A 1 353 ? 17.104 118.360 -63.015  1.00 82.32  ? 355 GLN A N   1 
ATOM   2508 C  CA  . GLN A 1 353 ? 17.415 119.491 -63.927  1.00 81.38  ? 355 GLN A CA  1 
ATOM   2509 C  C   . GLN A 1 353 ? 18.938 119.628 -64.073  1.00 73.45  ? 355 GLN A C   1 
ATOM   2510 O  O   . GLN A 1 353 ? 19.555 120.384 -63.282  1.00 77.02  ? 355 GLN A O   1 
ATOM   2511 C  CB  . GLN A 1 353 ? 16.809 120.787 -63.384  1.00 86.45  ? 355 GLN A CB  1 
ATOM   2512 C  CG  . GLN A 1 353 ? 16.960 121.965 -64.342  1.00 87.73  ? 355 GLN A CG  1 
ATOM   2513 C  CD  . GLN A 1 353 ? 16.011 121.830 -65.507  1.00 89.25  ? 355 GLN A CD  1 
ATOM   2514 O  OE1 . GLN A 1 353 ? 16.415 121.639 -66.655  1.00 88.30  ? 355 GLN A OE1 1 
ATOM   2515 N  NE2 . GLN A 1 353 ? 14.727 121.892 -65.202  1.00 87.89  ? 355 GLN A NE2 1 
ATOM   2516 N  N   . TYR A 1 354 ? 19.518 118.898 -65.029  1.00 63.54  ? 356 TYR A N   1 
ATOM   2517 C  CA  . TYR A 1 354 ? 20.955 118.952 -65.399  1.00 53.72  ? 356 TYR A CA  1 
ATOM   2518 C  C   . TYR A 1 354 ? 21.390 120.403 -65.596  1.00 50.62  ? 356 TYR A C   1 
ATOM   2519 O  O   . TYR A 1 354 ? 20.948 121.036 -66.561  1.00 51.29  ? 356 TYR A O   1 
ATOM   2520 C  CB  . TYR A 1 354 ? 21.185 118.148 -66.668  1.00 49.83  ? 356 TYR A CB  1 
ATOM   2521 C  CG  . TYR A 1 354 ? 21.309 116.678 -66.419  1.00 48.22  ? 356 TYR A CG  1 
ATOM   2522 C  CD1 . TYR A 1 354 ? 22.182 116.201 -65.465  1.00 46.54  ? 356 TYR A CD1 1 
ATOM   2523 C  CD2 . TYR A 1 354 ? 20.589 115.767 -67.160  1.00 48.31  ? 356 TYR A CD2 1 
ATOM   2524 C  CE1 . TYR A 1 354 ? 22.345 114.848 -65.253  1.00 47.56  ? 356 TYR A CE1 1 
ATOM   2525 C  CE2 . TYR A 1 354 ? 20.743 114.408 -66.973  1.00 48.37  ? 356 TYR A CE2 1 
ATOM   2526 C  CZ  . TYR A 1 354 ? 21.630 113.951 -66.019  1.00 49.55  ? 356 TYR A CZ  1 
ATOM   2527 O  OH  . TYR A 1 354 ? 21.795 112.620 -65.783  1.00 53.90  ? 356 TYR A OH  1 
ATOM   2528 N  N   . THR A 1 355 ? 22.217 120.902 -64.687  1.00 47.60  ? 357 THR A N   1 
ATOM   2529 C  CA  . THR A 1 355 ? 22.735 122.288 -64.703  1.00 47.47  ? 357 THR A CA  1 
ATOM   2530 C  C   . THR A 1 355 ? 24.259 122.240 -64.907  1.00 44.88  ? 357 THR A C   1 
ATOM   2531 O  O   . THR A 1 355 ? 24.956 121.379 -64.308  1.00 41.31  ? 357 THR A O   1 
ATOM   2532 C  CB  . THR A 1 355 ? 22.322 123.054 -63.438  1.00 48.29  ? 357 THR A CB  1 
ATOM   2533 O  OG1 . THR A 1 355 ? 22.624 124.430 -63.630  1.00 50.04  ? 357 THR A OG1 1 
ATOM   2534 C  CG2 . THR A 1 355 ? 23.063 122.662 -62.184  1.00 47.56  ? 357 THR A CG2 1 
ATOM   2535 N  N   . GLU A 1 356 ? 24.752 123.141 -65.750  1.00 45.03  ? 358 GLU A N   1 
ATOM   2536 C  CA  . GLU A 1 356 ? 26.175 123.250 -66.157  1.00 42.49  ? 358 GLU A CA  1 
ATOM   2537 C  C   . GLU A 1 356 ? 26.974 123.749 -64.957  1.00 39.69  ? 358 GLU A C   1 
ATOM   2538 O  O   . GLU A 1 356 ? 26.655 124.824 -64.425  1.00 38.00  ? 358 GLU A O   1 
ATOM   2539 C  CB  . GLU A 1 356 ? 26.292 124.186 -67.362  1.00 43.56  ? 358 GLU A CB  1 
ATOM   2540 C  CG  . GLU A 1 356 ? 27.710 124.396 -67.851  1.00 43.51  ? 358 GLU A CG  1 
ATOM   2541 C  CD  . GLU A 1 356 ? 27.843 125.266 -69.098  1.00 45.36  ? 358 GLU A CD  1 
ATOM   2542 O  OE1 . GLU A 1 356 ? 27.039 125.081 -70.067  1.00 45.86  ? 358 GLU A OE1 1 
ATOM   2543 O  OE2 . GLU A 1 356 ? 28.756 126.134 -69.099  1.00 45.32  ? 358 GLU A OE2 1 
ATOM   2544 N  N   . ILE A 1 357 ? 27.996 122.991 -64.572  1.00 37.03  ? 359 ILE A N   1 
ATOM   2545 C  CA  . ILE A 1 357 ? 28.876 123.377 -63.442  1.00 34.84  ? 359 ILE A CA  1 
ATOM   2546 C  C   . ILE A 1 357 ? 30.276 123.700 -63.948  1.00 34.26  ? 359 ILE A C   1 
ATOM   2547 O  O   . ILE A 1 357 ? 30.940 124.474 -63.296  1.00 34.13  ? 359 ILE A O   1 
ATOM   2548 C  CB  . ILE A 1 357 ? 28.864 122.302 -62.352  1.00 33.31  ? 359 ILE A CB  1 
ATOM   2549 C  CG1 . ILE A 1 357 ? 29.514 120.991 -62.782  1.00 30.94  ? 359 ILE A CG1 1 
ATOM   2550 C  CG2 . ILE A 1 357 ? 27.428 122.115 -61.861  1.00 35.16  ? 359 ILE A CG2 1 
ATOM   2551 C  CD1 . ILE A 1 357 ? 29.379 119.893 -61.742  1.00 30.67  ? 359 ILE A CD1 1 
ATOM   2552 N  N   . LYS A 1 358 ? 30.695 123.188 -65.099  1.00 34.69  ? 360 LYS A N   1 
ATOM   2553 C  CA  . LYS A 1 358 ? 32.087 123.401 -65.572  1.00 33.02  ? 360 LYS A CA  1 
ATOM   2554 C  C   . LYS A 1 358 ? 32.185 123.086 -67.056  1.00 31.00  ? 360 LYS A C   1 
ATOM   2555 O  O   . LYS A 1 358 ? 31.747 122.022 -67.475  1.00 27.60  ? 360 LYS A O   1 
ATOM   2556 C  CB  . LYS A 1 358 ? 33.027 122.484 -64.788  1.00 33.25  ? 360 LYS A CB  1 
ATOM   2557 C  CG  . LYS A 1 358 ? 34.514 122.670 -65.036  1.00 33.90  ? 360 LYS A CG  1 
ATOM   2558 C  CD  . LYS A 1 358 ? 35.022 123.968 -64.534  1.00 36.53  ? 360 LYS A CD  1 
ATOM   2559 C  CE  . LYS A 1 358 ? 36.421 124.268 -65.010  1.00 38.41  ? 360 LYS A CE  1 
ATOM   2560 N  NZ  . LYS A 1 358 ? 36.861 125.568 -64.451  1.00 41.87  ? 360 LYS A NZ  1 
ATOM   2561 N  N   . LYS A 1 359 ? 32.848 123.960 -67.782  1.00 32.02  ? 361 LYS A N   1 
ATOM   2562 C  CA  . LYS A 1 359 ? 33.104 123.774 -69.225  1.00 33.06  ? 361 LYS A CA  1 
ATOM   2563 C  C   . LYS A 1 359 ? 34.581 124.032 -69.493  1.00 31.38  ? 361 LYS A C   1 
ATOM   2564 O  O   . LYS A 1 359 ? 35.112 124.986 -68.924  1.00 32.74  ? 361 LYS A O   1 
ATOM   2565 C  CB  . LYS A 1 359 ? 32.265 124.756 -70.031  1.00 37.54  ? 361 LYS A CB  1 
ATOM   2566 C  CG  . LYS A 1 359 ? 32.517 124.718 -71.530  1.00 40.11  ? 361 LYS A CG  1 
ATOM   2567 C  CD  . LYS A 1 359 ? 31.551 125.541 -72.326  1.00 45.07  ? 361 LYS A CD  1 
ATOM   2568 C  CE  . LYS A 1 359 ? 31.308 126.917 -71.728  1.00 48.65  ? 361 LYS A CE  1 
ATOM   2569 N  NZ  . LYS A 1 359 ? 30.562 127.801 -72.668  1.00 52.76  ? 361 LYS A NZ  1 
ATOM   2570 N  N   . PHE A 1 360 ? 35.215 123.165 -70.276  1.00 28.89  ? 362 PHE A N   1 
ATOM   2571 C  CA  . PHE A 1 360 ? 36.567 123.357 -70.842  1.00 27.96  ? 362 PHE A CA  1 
ATOM   2572 C  C   . PHE A 1 360 ? 36.439 123.506 -72.362  1.00 28.21  ? 362 PHE A C   1 
ATOM   2573 O  O   . PHE A 1 360 ? 35.848 122.656 -73.006  1.00 27.83  ? 362 PHE A O   1 
ATOM   2574 C  CB  . PHE A 1 360 ? 37.472 122.175 -70.505  1.00 25.91  ? 362 PHE A CB  1 
ATOM   2575 C  CG  . PHE A 1 360 ? 37.816 122.018 -69.054  1.00 25.10  ? 362 PHE A CG  1 
ATOM   2576 C  CD1 . PHE A 1 360 ? 38.781 122.805 -68.469  1.00 25.18  ? 362 PHE A CD1 1 
ATOM   2577 C  CD2 . PHE A 1 360 ? 37.172 121.071 -68.266  1.00 24.62  ? 362 PHE A CD2 1 
ATOM   2578 C  CE1 . PHE A 1 360 ? 39.071 122.678 -67.116  1.00 25.59  ? 362 PHE A CE1 1 
ATOM   2579 C  CE2 . PHE A 1 360 ? 37.522 120.890 -66.942  1.00 23.92  ? 362 PHE A CE2 1 
ATOM   2580 C  CZ  . PHE A 1 360 ? 38.452 121.717 -66.359  1.00 24.06  ? 362 PHE A CZ  1 
ATOM   2581 N  N   . GLU A 1 361 ? 37.121 124.546 -72.856  1.00 30.08  ? 363 GLU A N   1 
ATOM   2582 C  CA  . GLU A 1 361 ? 37.262 124.855 -74.299  1.00 31.02  ? 363 GLU A CA  1 
ATOM   2583 C  C   . GLU A 1 361 ? 38.369 123.949 -74.853  1.00 28.54  ? 363 GLU A C   1 
ATOM   2584 O  O   . GLU A 1 361 ? 39.165 123.401 -74.058  1.00 28.44  ? 363 GLU A O   1 
ATOM   2585 C  CB  . GLU A 1 361 ? 37.602 126.333 -74.499  1.00 35.16  ? 363 GLU A CB  1 
ATOM   2586 C  CG  . GLU A 1 361 ? 36.677 127.038 -75.474  1.00 39.84  ? 363 GLU A CG  1 
ATOM   2587 C  CD  . GLU A 1 361 ? 35.220 127.083 -75.045  1.00 42.60  ? 363 GLU A CD  1 
ATOM   2588 O  OE1 . GLU A 1 361 ? 34.964 127.362 -73.857  1.00 43.08  ? 363 GLU A OE1 1 
ATOM   2589 O  OE2 . GLU A 1 361 ? 34.346 126.838 -75.899  1.00 44.47  ? 363 GLU A OE2 1 
ATOM   2590 N  N   . ALA A 1 362 ? 38.446 123.841 -76.175  1.00 29.18  ? 364 ALA A N   1 
ATOM   2591 C  CA  . ALA A 1 362 ? 39.405 122.927 -76.837  1.00 28.10  ? 364 ALA A CA  1 
ATOM   2592 C  C   . ALA A 1 362 ? 40.678 123.697 -77.228  1.00 29.19  ? 364 ALA A C   1 
ATOM   2593 O  O   . ALA A 1 362 ? 40.566 124.883 -77.465  1.00 30.63  ? 364 ALA A O   1 
ATOM   2594 C  CB  . ALA A 1 362 ? 38.689 122.344 -78.008  1.00 28.78  ? 364 ALA A CB  1 
ATOM   2595 N  N   A ASP A 1 363 ? 41.832 123.019 -77.411  0.50 28.55  ? 365 ASP A N   1 
ATOM   2596 N  N   B ASP A 1 363 ? 41.817 123.000 -77.136  0.50 29.82  ? 365 ASP A N   1 
ATOM   2597 C  CA  A ASP A 1 363 ? 43.247 123.518 -77.578  0.50 28.80  ? 365 ASP A CA  1 
ATOM   2598 C  CA  B ASP A 1 363 ? 43.233 123.483 -77.177  0.50 30.40  ? 365 ASP A CA  1 
ATOM   2599 C  C   A ASP A 1 363 ? 44.146 122.252 -77.396  0.50 27.42  ? 365 ASP A C   1 
ATOM   2600 C  C   B ASP A 1 363 ? 44.118 122.224 -77.280  0.50 28.22  ? 365 ASP A C   1 
ATOM   2601 O  O   A ASP A 1 363 ? 43.696 121.190 -77.862  0.50 25.85  ? 365 ASP A O   1 
ATOM   2602 O  O   B ASP A 1 363 ? 43.667 121.198 -77.833  0.50 26.62  ? 365 ASP A O   1 
ATOM   2603 C  CB  A ASP A 1 363 ? 43.619 124.689 -76.623  0.50 30.87  ? 365 ASP A CB  1 
ATOM   2604 C  CB  B ASP A 1 363 ? 43.636 124.421 -75.991  0.50 32.57  ? 365 ASP A CB  1 
ATOM   2605 C  CG  A ASP A 1 363 ? 43.570 126.159 -77.084  0.50 31.77  ? 365 ASP A CG  1 
ATOM   2606 C  CG  B ASP A 1 363 ? 43.399 123.992 -74.525  0.50 32.49  ? 365 ASP A CG  1 
ATOM   2607 O  OD1 A ASP A 1 363 ? 44.594 126.643 -77.609  0.50 31.81  ? 365 ASP A OD1 1 
ATOM   2608 O  OD1 B ASP A 1 363 ? 44.381 123.994 -73.694  0.50 28.73  ? 365 ASP A OD1 1 
ATOM   2609 O  OD2 A ASP A 1 363 ? 42.576 126.867 -76.747  0.50 31.82  ? 365 ASP A OD2 1 
ATOM   2610 O  OD2 B ASP A 1 363 ? 42.205 123.762 -74.176  0.50 33.52  ? 365 ASP A OD2 1 
ATOM   2611 N  N   . SER A 1 364 ? 45.320 122.265 -76.723  1.00 27.18  ? 366 SER A N   1 
ATOM   2612 C  CA  . SER A 1 364 ? 46.306 121.147 -76.861  1.00 26.36  ? 366 SER A CA  1 
ATOM   2613 C  C   . SER A 1 364 ? 46.154 120.141 -75.724  1.00 26.09  ? 366 SER A C   1 
ATOM   2614 O  O   . SER A 1 364 ? 46.754 118.991 -75.818  1.00 24.20  ? 366 SER A O   1 
ATOM   2615 C  CB  . SER A 1 364 ? 47.741 121.611 -76.962  1.00 26.68  ? 366 SER A CB  1 
ATOM   2616 O  OG  . SER A 1 364 ? 48.107 122.472 -75.915  1.00 25.38  ? 366 SER A OG  1 
ATOM   2617 N  N   . ASN A 1 365 ? 45.355 120.543 -74.733  1.00 25.51  ? 367 ASN A N   1 
ATOM   2618 C  CA  . ASN A 1 365 ? 45.151 119.750 -73.505  1.00 26.61  ? 367 ASN A CA  1 
ATOM   2619 C  C   . ASN A 1 365 ? 44.297 118.520 -73.813  1.00 22.90  ? 367 ASN A C   1 
ATOM   2620 O  O   . ASN A 1 365 ? 43.446 118.593 -74.670  1.00 23.48  ? 367 ASN A O   1 
ATOM   2621 C  CB  . ASN A 1 365 ? 44.656 120.597 -72.329  1.00 28.10  ? 367 ASN A CB  1 
ATOM   2622 C  CG  . ASN A 1 365 ? 45.181 120.036 -71.011  1.00 31.51  ? 367 ASN A CG  1 
ATOM   2623 O  OD1 . ASN A 1 365 ? 46.434 119.964 -70.747  1.00 31.55  ? 367 ASN A OD1 1 
ATOM   2624 N  ND2 . ASN A 1 365 ? 44.203 119.601 -70.206  1.00 30.05  ? 367 ASN A ND2 1 
ATOM   2625 N  N   . SER A 1 366 ? 44.660 117.411 -73.191  1.00 21.00  ? 368 SER A N   1 
ATOM   2626 C  CA  . SER A 1 366 ? 44.001 116.094 -73.290  1.00 19.72  ? 368 SER A CA  1 
ATOM   2627 C  C   . SER A 1 366 ? 43.501 115.616 -71.902  1.00 19.22  ? 368 SER A C   1 
ATOM   2628 O  O   . SER A 1 366 ? 42.802 114.577 -71.829  1.00 18.62  ? 368 SER A O   1 
ATOM   2629 C  CB  . SER A 1 366 ? 44.963 115.146 -73.925  1.00 20.00  ? 368 SER A CB  1 
ATOM   2630 O  OG  . SER A 1 366 ? 44.984 115.368 -75.326  1.00 19.85  ? 368 SER A OG  1 
ATOM   2631 N  N   . THR A 1 367 ? 43.794 116.355 -70.828  1.00 18.15  ? 369 THR A N   1 
ATOM   2632 C  CA  . THR A 1 367 ? 43.370 115.983 -69.460  1.00 17.53  ? 369 THR A CA  1 
ATOM   2633 C  C   . THR A 1 367 ? 42.420 117.044 -68.911  1.00 17.35  ? 369 THR A C   1 
ATOM   2634 O  O   . THR A 1 367 ? 42.803 118.213 -68.908  1.00 18.21  ? 369 THR A O   1 
ATOM   2635 C  CB  . THR A 1 367 ? 44.581 115.817 -68.552  1.00 17.60  ? 369 THR A CB  1 
ATOM   2636 O  OG1 . THR A 1 367 ? 45.400 114.805 -69.128  1.00 17.52  ? 369 THR A OG1 1 
ATOM   2637 C  CG2 . THR A 1 367 ? 44.198 115.437 -67.146  1.00 17.26  ? 369 THR A CG2 1 
ATOM   2638 N  N   . PHE A 1 368 ? 41.219 116.648 -68.501  1.00 16.78  ? 370 PHE A N   1 
ATOM   2639 C  CA  . PHE A 1 368 ? 40.203 117.588 -67.988  1.00 17.10  ? 370 PHE A CA  1 
ATOM   2640 C  C   . PHE A 1 368 ? 39.997 117.267 -66.502  1.00 17.51  ? 370 PHE A C   1 
ATOM   2641 O  O   . PHE A 1 368 ? 39.433 116.215 -66.166  1.00 17.62  ? 370 PHE A O   1 
ATOM   2642 C  CB  . PHE A 1 368 ? 38.978 117.526 -68.901  1.00 16.90  ? 370 PHE A CB  1 
ATOM   2643 C  CG  . PHE A 1 368 ? 39.303 117.789 -70.343  1.00 17.04  ? 370 PHE A CG  1 
ATOM   2644 C  CD1 . PHE A 1 368 ? 39.792 116.769 -71.148  1.00 16.96  ? 370 PHE A CD1 1 
ATOM   2645 C  CD2 . PHE A 1 368 ? 39.192 119.065 -70.886  1.00 17.49  ? 370 PHE A CD2 1 
ATOM   2646 C  CE1 . PHE A 1 368 ? 40.187 117.029 -72.454  1.00 17.64  ? 370 PHE A CE1 1 
ATOM   2647 C  CE2 . PHE A 1 368 ? 39.527 119.309 -72.208  1.00 17.97  ? 370 PHE A CE2 1 
ATOM   2648 C  CZ  . PHE A 1 368 ? 40.029 118.291 -72.997  1.00 17.76  ? 370 PHE A CZ  1 
ATOM   2649 N  N   . ASP A 1 369 ? 40.443 118.151 -65.615  1.00 17.92  ? 371 ASP A N   1 
ATOM   2650 C  CA  . ASP A 1 369 ? 40.375 117.921 -64.137  1.00 18.25  ? 371 ASP A CA  1 
ATOM   2651 C  C   . ASP A 1 369 ? 39.166 118.689 -63.613  1.00 17.79  ? 371 ASP A C   1 
ATOM   2652 O  O   . ASP A 1 369 ? 39.233 119.892 -63.603  1.00 18.66  ? 371 ASP A O   1 
ATOM   2653 C  CB  . ASP A 1 369 ? 41.672 118.346 -63.433  1.00 18.97  ? 371 ASP A CB  1 
ATOM   2654 C  CG  . ASP A 1 369 ? 42.851 117.383 -63.659  1.00 20.47  ? 371 ASP A CG  1 
ATOM   2655 O  OD1 . ASP A 1 369 ? 42.704 116.155 -63.326  1.00 20.44  ? 371 ASP A OD1 1 
ATOM   2656 O  OD2 . ASP A 1 369 ? 43.937 117.835 -64.185  1.00 22.55  ? 371 ASP A OD2 1 
ATOM   2657 N  N   . PHE A 1 370 ? 38.059 118.025 -63.319  1.00 16.98  ? 372 PHE A N   1 
ATOM   2658 C  CA  . PHE A 1 370 ? 36.862 118.669 -62.751  1.00 17.37  ? 372 PHE A CA  1 
ATOM   2659 C  C   . PHE A 1 370 ? 37.008 118.608 -61.234  1.00 17.88  ? 372 PHE A C   1 
ATOM   2660 O  O   . PHE A 1 370 ? 36.774 117.568 -60.659  1.00 17.46  ? 372 PHE A O   1 
ATOM   2661 C  CB  . PHE A 1 370 ? 35.607 117.992 -63.264  1.00 17.22  ? 372 PHE A CB  1 
ATOM   2662 C  CG  . PHE A 1 370 ? 35.387 118.151 -64.752  1.00 16.99  ? 372 PHE A CG  1 
ATOM   2663 C  CD1 . PHE A 1 370 ? 35.892 117.238 -65.645  1.00 16.53  ? 372 PHE A CD1 1 
ATOM   2664 C  CD2 . PHE A 1 370 ? 34.667 119.213 -65.249  1.00 17.38  ? 372 PHE A CD2 1 
ATOM   2665 C  CE1 . PHE A 1 370 ? 35.676 117.388 -67.008  1.00 16.96  ? 372 PHE A CE1 1 
ATOM   2666 C  CE2 . PHE A 1 370 ? 34.412 119.338 -66.603  1.00 17.48  ? 372 PHE A CE2 1 
ATOM   2667 C  CZ  . PHE A 1 370 ? 34.941 118.440 -67.491  1.00 17.20  ? 372 PHE A CZ  1 
ATOM   2668 N  N   . LYS A 1 371 ? 37.460 119.701 -60.640  1.00 18.98  ? 373 LYS A N   1 
ATOM   2669 C  CA  . LYS A 1 371 ? 37.761 119.749 -59.194  1.00 20.66  ? 373 LYS A CA  1 
ATOM   2670 C  C   . LYS A 1 371 ? 36.497 120.116 -58.446  1.00 19.83  ? 373 LYS A C   1 
ATOM   2671 O  O   . LYS A 1 371 ? 35.857 121.023 -58.850  1.00 19.16  ? 373 LYS A O   1 
ATOM   2672 C  CB  . LYS A 1 371 ? 38.920 120.710 -58.926  1.00 23.26  ? 373 LYS A CB  1 
ATOM   2673 C  CG  . LYS A 1 371 ? 40.256 120.125 -59.359  1.00 26.40  ? 373 LYS A CG  1 
ATOM   2674 C  CD  . LYS A 1 371 ? 41.487 120.820 -58.805  1.00 30.99  ? 373 LYS A CD  1 
ATOM   2675 C  CE  . LYS A 1 371 ? 42.757 120.493 -59.570  1.00 34.89  ? 373 LYS A CE  1 
ATOM   2676 N  NZ  . LYS A 1 371 ? 43.960 121.153 -58.999  1.00 37.95  ? 373 LYS A NZ  1 
ATOM   2677 N  N   . GLY A 1 372 ? 36.207 119.456 -57.330  1.00 19.99  ? 374 GLY A N   1 
ATOM   2678 C  CA  . GLY A 1 372 ? 35.236 119.988 -56.352  1.00 20.33  ? 374 GLY A CA  1 
ATOM   2679 C  C   . GLY A 1 372 ? 33.865 119.455 -56.617  1.00 20.40  ? 374 GLY A C   1 
ATOM   2680 O  O   . GLY A 1 372 ? 32.900 120.233 -56.574  1.00 20.26  ? 374 GLY A O   1 
ATOM   2681 N  N   . LEU A 1 373 ? 33.795 118.158 -56.882  1.00 20.48  ? 375 LEU A N   1 
ATOM   2682 C  CA  . LEU A 1 373 ? 32.495 117.488 -57.070  1.00 21.57  ? 375 LEU A CA  1 
ATOM   2683 C  C   . LEU A 1 373 ? 32.109 116.758 -55.786  1.00 22.55  ? 375 LEU A C   1 
ATOM   2684 O  O   . LEU A 1 373 ? 33.015 116.280 -55.040  1.00 22.41  ? 375 LEU A O   1 
ATOM   2685 C  CB  . LEU A 1 373 ? 32.601 116.486 -58.212  1.00 20.86  ? 375 LEU A CB  1 
ATOM   2686 C  CG  . LEU A 1 373 ? 33.193 116.999 -59.516  1.00 20.30  ? 375 LEU A CG  1 
ATOM   2687 C  CD1 . LEU A 1 373 ? 32.984 115.965 -60.571  1.00 19.55  ? 375 LEU A CD1 1 
ATOM   2688 C  CD2 . LEU A 1 373 ? 32.576 118.320 -59.924  1.00 21.16  ? 375 LEU A CD2 1 
ATOM   2689 N  N   . ASP A 1 374 ? 30.806 116.634 -55.579  1.00 24.58  ? 376 ASP A N   1 
ATOM   2690 C  CA  . ASP A 1 374 ? 30.230 115.861 -54.461  1.00 26.96  ? 376 ASP A CA  1 
ATOM   2691 C  C   . ASP A 1 374 ? 29.441 114.662 -55.004  1.00 27.58  ? 376 ASP A C   1 
ATOM   2692 O  O   . ASP A 1 374 ? 29.352 114.454 -56.245  1.00 27.77  ? 376 ASP A O   1 
ATOM   2693 C  CB  . ASP A 1 374 ? 29.448 116.798 -53.535  1.00 28.35  ? 376 ASP A CB  1 
ATOM   2694 C  CG  . ASP A 1 374 ? 28.214 117.403 -54.152  1.00 30.70  ? 376 ASP A CG  1 
ATOM   2695 O  OD1 . ASP A 1 374 ? 28.043 117.248 -55.358  1.00 31.07  ? 376 ASP A OD1 1 
ATOM   2696 O  OD2 . ASP A 1 374 ? 27.414 118.016 -53.391  1.00 35.48  ? 376 ASP A OD2 1 
ATOM   2697 N  N   . SER A 1 375 ? 28.874 113.898 -54.078  1.00 29.03  ? 377 SER A N   1 
ATOM   2698 C  CA  . SER A 1 375 ? 27.969 112.781 -54.397  1.00 29.67  ? 377 SER A CA  1 
ATOM   2699 C  C   . SER A 1 375 ? 26.813 113.358 -55.194  1.00 32.15  ? 377 SER A C   1 
ATOM   2700 O  O   . SER A 1 375 ? 26.397 114.480 -54.895  1.00 34.17  ? 377 SER A O   1 
ATOM   2701 C  CB  . SER A 1 375 ? 27.533 112.086 -53.173  1.00 29.18  ? 377 SER A CB  1 
ATOM   2702 O  OG  . SER A 1 375 ? 28.670 111.588 -52.495  1.00 27.13  ? 377 SER A OG  1 
ATOM   2703 N  N   . GLY A 1 376 ? 26.372 112.636 -56.208  1.00 32.76  ? 378 GLY A N   1 
ATOM   2704 C  CA  . GLY A 1 376 ? 25.224 113.059 -57.023  1.00 34.96  ? 378 GLY A CA  1 
ATOM   2705 C  C   . GLY A 1 376 ? 25.256 112.448 -58.410  1.00 35.35  ? 378 GLY A C   1 
ATOM   2706 O  O   . GLY A 1 376 ? 26.160 111.637 -58.701  1.00 33.18  ? 378 GLY A O   1 
ATOM   2707 N  N   . ASP A 1 377 ? 24.307 112.892 -59.238  1.00 37.38  ? 379 ASP A N   1 
ATOM   2708 C  CA  . ASP A 1 377 ? 24.096 112.439 -60.625  1.00 37.27  ? 379 ASP A CA  1 
ATOM   2709 C  C   . ASP A 1 377 ? 24.617 113.512 -61.557  1.00 35.39  ? 379 ASP A C   1 
ATOM   2710 O  O   . ASP A 1 377 ? 24.160 114.680 -61.451  1.00 34.99  ? 379 ASP A O   1 
ATOM   2711 C  CB  . ASP A 1 377 ? 22.617 112.192 -60.901  1.00 40.99  ? 379 ASP A CB  1 
ATOM   2712 C  CG  . ASP A 1 377 ? 22.077 111.050 -60.066  1.00 43.57  ? 379 ASP A CG  1 
ATOM   2713 O  OD1 . ASP A 1 377 ? 22.917 110.230 -59.574  1.00 41.44  ? 379 ASP A OD1 1 
ATOM   2714 O  OD2 . ASP A 1 377 ? 20.835 111.001 -59.908  1.00 47.61  ? 379 ASP A OD2 1 
ATOM   2715 N  N   . TYR A 1 378 ? 25.502 113.090 -62.453  1.00 32.85  ? 380 TYR A N   1 
ATOM   2716 C  CA  . TYR A 1 378 ? 26.220 113.985 -63.384  1.00 31.33  ? 380 TYR A CA  1 
ATOM   2717 C  C   . TYR A 1 378 ? 26.037 113.499 -64.819  1.00 31.66  ? 380 TYR A C   1 
ATOM   2718 O  O   . TYR A 1 378 ? 25.836 112.276 -65.075  1.00 31.60  ? 380 TYR A O   1 
ATOM   2719 C  CB  . TYR A 1 378 ? 27.703 114.022 -63.038  1.00 29.49  ? 380 TYR A CB  1 
ATOM   2720 C  CG  . TYR A 1 378 ? 28.001 114.679 -61.719  1.00 29.39  ? 380 TYR A CG  1 
ATOM   2721 C  CD1 . TYR A 1 378 ? 28.210 116.048 -61.649  1.00 29.19  ? 380 TYR A CD1 1 
ATOM   2722 C  CD2 . TYR A 1 378 ? 28.070 113.940 -60.550  1.00 29.02  ? 380 TYR A CD2 1 
ATOM   2723 C  CE1 . TYR A 1 378 ? 28.495 116.674 -60.451  1.00 28.51  ? 380 TYR A CE1 1 
ATOM   2724 C  CE2 . TYR A 1 378 ? 28.334 114.551 -59.335  1.00 28.47  ? 380 TYR A CE2 1 
ATOM   2725 C  CZ  . TYR A 1 378 ? 28.550 115.920 -59.295  1.00 28.29  ? 380 TYR A CZ  1 
ATOM   2726 O  OH  . TYR A 1 378 ? 28.849 116.547 -58.123  1.00 29.12  ? 380 TYR A OH  1 
ATOM   2727 N  N   . LYS A 1 379 ? 26.173 114.444 -65.743  1.00 31.87  ? 381 LYS A N   1 
ATOM   2728 C  CA  . LYS A 1 379 ? 26.261 114.133 -67.187  1.00 31.27  ? 381 LYS A CA  1 
ATOM   2729 C  C   . LYS A 1 379 ? 27.497 114.812 -67.760  1.00 28.34  ? 381 LYS A C   1 
ATOM   2730 O  O   . LYS A 1 379 ? 27.587 116.033 -67.653  1.00 27.35  ? 381 LYS A O   1 
ATOM   2731 C  CB  . LYS A 1 379 ? 24.999 114.590 -67.911  1.00 34.65  ? 381 LYS A CB  1 
ATOM   2732 C  CG  . LYS A 1 379 ? 24.945 114.202 -69.380  1.00 36.22  ? 381 LYS A CG  1 
ATOM   2733 C  CD  . LYS A 1 379 ? 23.663 114.607 -70.128  1.00 39.39  ? 381 LYS A CD  1 
ATOM   2734 C  CE  . LYS A 1 379 ? 23.322 116.087 -70.030  1.00 40.46  ? 381 LYS A CE  1 
ATOM   2735 N  NZ  . LYS A 1 379 ? 22.087 116.426 -70.786  1.00 42.53  ? 381 LYS A NZ  1 
ATOM   2736 N  N   . LEU A 1 380 ? 28.386 114.023 -68.362  1.00 26.13  ? 382 LEU A N   1 
ATOM   2737 C  CA  . LEU A 1 380 ? 29.575 114.512 -69.094  1.00 24.60  ? 382 LEU A CA  1 
ATOM   2738 C  C   . LEU A 1 380 ? 29.236 114.550 -70.589  1.00 24.25  ? 382 LEU A C   1 
ATOM   2739 O  O   . LEU A 1 380 ? 28.912 113.498 -71.157  1.00 23.28  ? 382 LEU A O   1 
ATOM   2740 C  CB  . LEU A 1 380 ? 30.784 113.599 -68.834  1.00 23.68  ? 382 LEU A CB  1 
ATOM   2741 C  CG  . LEU A 1 380 ? 32.115 114.075 -69.435  1.00 22.46  ? 382 LEU A CG  1 
ATOM   2742 C  CD1 . LEU A 1 380 ? 32.561 115.360 -68.763  1.00 21.95  ? 382 LEU A CD1 1 
ATOM   2743 C  CD2 . LEU A 1 380 ? 33.211 113.023 -69.336  1.00 21.55  ? 382 LEU A CD2 1 
ATOM   2744 N  N   . VAL A 1 381 ? 29.304 115.741 -71.174  1.00 24.33  ? 383 VAL A N   1 
ATOM   2745 C  CA  . VAL A 1 381 ? 29.019 115.979 -72.616  1.00 25.43  ? 383 VAL A CA  1 
ATOM   2746 C  C   . VAL A 1 381 ? 30.314 116.409 -73.273  1.00 25.07  ? 383 VAL A C   1 
ATOM   2747 O  O   . VAL A 1 381 ? 30.961 117.315 -72.687  1.00 26.27  ? 383 VAL A O   1 
ATOM   2748 C  CB  . VAL A 1 381 ? 27.959 117.069 -72.786  1.00 26.49  ? 383 VAL A CB  1 
ATOM   2749 C  CG1 . VAL A 1 381 ? 27.831 117.492 -74.245  1.00 26.84  ? 383 VAL A CG1 1 
ATOM   2750 C  CG2 . VAL A 1 381 ? 26.636 116.608 -72.203  1.00 27.64  ? 383 VAL A CG2 1 
ATOM   2751 N  N   . GLU A 1 382 ? 30.695 115.776 -74.390  1.00 25.35  ? 384 GLU A N   1 
ATOM   2752 C  CA  . GLU A 1 382 ? 31.890 116.184 -75.182  1.00 23.89  ? 384 GLU A CA  1 
ATOM   2753 C  C   . GLU A 1 382 ? 31.430 117.347 -76.072  1.00 23.49  ? 384 GLU A C   1 
ATOM   2754 O  O   . GLU A 1 382 ? 31.120 117.159 -77.211  1.00 21.88  ? 384 GLU A O   1 
ATOM   2755 C  CB  . GLU A 1 382 ? 32.512 114.985 -75.900  1.00 25.19  ? 384 GLU A CB  1 
ATOM   2756 C  CG  . GLU A 1 382 ? 33.806 115.331 -76.629  1.00 26.32  ? 384 GLU A CG  1 
ATOM   2757 C  CD  . GLU A 1 382 ? 34.263 114.363 -77.710  1.00 27.85  ? 384 GLU A CD  1 
ATOM   2758 O  OE1 . GLU A 1 382 ? 33.411 113.878 -78.454  1.00 30.42  ? 384 GLU A OE1 1 
ATOM   2759 O  OE2 . GLU A 1 382 ? 35.475 114.119 -77.840  1.00 29.21  ? 384 GLU A OE2 1 
ATOM   2760 N  N   . SER A 1 383 ? 31.413 118.544 -75.519  1.00 23.87  ? 385 SER A N   1 
ATOM   2761 C  CA  . SER A 1 383 ? 30.866 119.759 -76.160  1.00 25.00  ? 385 SER A CA  1 
ATOM   2762 C  C   . SER A 1 383 ? 31.785 120.227 -77.299  1.00 25.46  ? 385 SER A C   1 
ATOM   2763 O  O   . SER A 1 383 ? 31.379 121.132 -78.056  1.00 26.74  ? 385 SER A O   1 
ATOM   2764 C  CB  . SER A 1 383 ? 30.669 120.818 -75.128  1.00 25.54  ? 385 SER A CB  1 
ATOM   2765 O  OG  . SER A 1 383 ? 31.738 120.772 -74.203  1.00 24.30  ? 385 SER A OG  1 
ATOM   2766 N  N   . THR A 1 384 ? 32.976 119.667 -77.454  1.00 24.75  ? 386 THR A N   1 
ATOM   2767 C  CA  . THR A 1 384 ? 33.798 119.936 -78.651  1.00 25.83  ? 386 THR A CA  1 
ATOM   2768 C  C   . THR A 1 384 ? 34.481 118.658 -79.094  1.00 24.45  ? 386 THR A C   1 
ATOM   2769 O  O   . THR A 1 384 ? 35.159 118.010 -78.281  1.00 21.46  ? 386 THR A O   1 
ATOM   2770 C  CB  . THR A 1 384 ? 34.862 121.020 -78.459  1.00 27.53  ? 386 THR A CB  1 
ATOM   2771 O  OG1 . THR A 1 384 ? 34.235 122.182 -77.910  1.00 31.04  ? 386 THR A OG1 1 
ATOM   2772 C  CG2 . THR A 1 384 ? 35.564 121.332 -79.769  1.00 27.92  ? 386 THR A CG2 1 
ATOM   2773 N  N   . VAL A 1 385 ? 34.303 118.321 -80.361  1.00 23.35  ? 387 VAL A N   1 
ATOM   2774 C  CA  . VAL A 1 385 ? 34.787 117.015 -80.870  1.00 23.17  ? 387 VAL A CA  1 
ATOM   2775 C  C   . VAL A 1 385 ? 36.039 117.263 -81.708  1.00 22.24  ? 387 VAL A C   1 
ATOM   2776 O  O   . VAL A 1 385 ? 36.059 118.122 -82.575  1.00 22.44  ? 387 VAL A O   1 
ATOM   2777 C  CB  . VAL A 1 385 ? 33.678 116.290 -81.654  1.00 24.50  ? 387 VAL A CB  1 
ATOM   2778 C  CG1 . VAL A 1 385 ? 34.155 114.915 -82.119  1.00 25.12  ? 387 VAL A CG1 1 
ATOM   2779 C  CG2 . VAL A 1 385 ? 32.405 116.167 -80.841  1.00 24.36  ? 387 VAL A CG2 1 
ATOM   2780 N  N   . PRO A 1 386 ? 37.153 116.549 -81.459  1.00 20.93  ? 388 PRO A N   1 
ATOM   2781 C  CA  . PRO A 1 386 ? 38.337 116.697 -82.301  1.00 20.15  ? 388 PRO A CA  1 
ATOM   2782 C  C   . PRO A 1 386 ? 38.008 116.359 -83.759  1.00 20.11  ? 388 PRO A C   1 
ATOM   2783 O  O   . PRO A 1 386 ? 37.331 115.420 -84.028  1.00 19.67  ? 388 PRO A O   1 
ATOM   2784 C  CB  . PRO A 1 386 ? 39.356 115.734 -81.699  1.00 19.65  ? 388 PRO A CB  1 
ATOM   2785 C  CG  . PRO A 1 386 ? 38.848 115.530 -80.288  1.00 19.69  ? 388 PRO A CG  1 
ATOM   2786 C  CD  . PRO A 1 386 ? 37.342 115.597 -80.360  1.00 19.88  ? 388 PRO A CD  1 
ATOM   2787 N  N   . SER A 1 387 ? 38.512 117.181 -84.650  1.00 20.43  ? 389 SER A N   1 
ATOM   2788 C  CA  . SER A 1 387 ? 38.315 117.067 -86.112  1.00 21.53  ? 389 SER A CA  1 
ATOM   2789 C  C   . SER A 1 387 ? 38.674 115.628 -86.561  1.00 21.23  ? 389 SER A C   1 
ATOM   2790 O  O   . SER A 1 387 ? 39.743 115.104 -86.178  1.00 21.97  ? 389 SER A O   1 
ATOM   2791 C  CB  . SER A 1 387 ? 39.130 118.148 -86.739  1.00 22.29  ? 389 SER A CB  1 
ATOM   2792 O  OG  . SER A 1 387 ? 39.241 117.954 -88.129  1.00 25.04  ? 389 SER A OG  1 
ATOM   2793 N  N   . GLY A 1 388 ? 37.749 114.932 -87.222  1.00 21.33  ? 390 GLY A N   1 
ATOM   2794 C  CA  . GLY A 1 388 ? 37.984 113.595 -87.809  1.00 21.00  ? 390 GLY A CA  1 
ATOM   2795 C  C   . GLY A 1 388 ? 37.711 112.457 -86.848  1.00 20.51  ? 390 GLY A C   1 
ATOM   2796 O  O   . GLY A 1 388 ? 38.014 111.322 -87.173  1.00 20.86  ? 390 GLY A O   1 
ATOM   2797 N  N   . TYR A 1 389 ? 37.148 112.756 -85.686  1.00 20.37  ? 391 TYR A N   1 
ATOM   2798 C  CA  . TYR A 1 389 ? 36.750 111.755 -84.681  1.00 19.77  ? 391 TYR A CA  1 
ATOM   2799 C  C   . TYR A 1 389 ? 35.246 111.872 -84.507  1.00 20.31  ? 391 TYR A C   1 
ATOM   2800 O  O   . TYR A 1 389 ? 34.677 112.947 -84.669  1.00 19.46  ? 391 TYR A O   1 
ATOM   2801 C  CB  . TYR A 1 389 ? 37.559 111.963 -83.393  1.00 19.54  ? 391 TYR A CB  1 
ATOM   2802 C  CG  . TYR A 1 389 ? 39.013 111.669 -83.597  1.00 19.08  ? 391 TYR A CG  1 
ATOM   2803 C  CD1 . TYR A 1 389 ? 39.884 112.623 -84.077  1.00 18.98  ? 391 TYR A CD1 1 
ATOM   2804 C  CD2 . TYR A 1 389 ? 39.494 110.401 -83.372  1.00 20.03  ? 391 TYR A CD2 1 
ATOM   2805 C  CE1 . TYR A 1 389 ? 41.212 112.324 -84.341  1.00 19.72  ? 391 TYR A CE1 1 
ATOM   2806 C  CE2 . TYR A 1 389 ? 40.824 110.091 -83.585  1.00 20.92  ? 391 TYR A CE2 1 
ATOM   2807 C  CZ  . TYR A 1 389 ? 41.685 111.046 -84.095  1.00 20.74  ? 391 TYR A CZ  1 
ATOM   2808 O  OH  . TYR A 1 389 ? 42.991 110.680 -84.286  1.00 22.09  ? 391 TYR A OH  1 
ATOM   2809 N  N   . ASN A 1 390 ? 34.643 110.748 -84.162  1.00 22.18  ? 392 ASN A N   1 
ATOM   2810 C  CA  . ASN A 1 390 ? 33.211 110.632 -83.808  1.00 23.79  ? 392 ASN A CA  1 
ATOM   2811 C  C   . ASN A 1 390 ? 33.011 111.230 -82.429  1.00 24.61  ? 392 ASN A C   1 
ATOM   2812 O  O   . ASN A 1 390 ? 33.827 110.968 -81.542  1.00 24.06  ? 392 ASN A O   1 
ATOM   2813 C  CB  . ASN A 1 390 ? 32.749 109.173 -83.838  1.00 25.20  ? 392 ASN A CB  1 
ATOM   2814 C  CG  . ASN A 1 390 ? 32.875 108.594 -85.235  1.00 26.20  ? 392 ASN A CG  1 
ATOM   2815 O  OD1 . ASN A 1 390 ? 33.586 107.611 -85.436  1.00 27.93  ? 392 ASN A OD1 1 
ATOM   2816 N  ND2 . ASN A 1 390 ? 32.298 109.274 -86.209  1.00 24.73  ? 392 ASN A ND2 1 
ATOM   2817 N  N   . ALA A 1 391 ? 31.955 112.016 -82.279  1.00 26.05  ? 393 ALA A N   1 
ATOM   2818 C  CA  . ALA A 1 391 ? 31.459 112.460 -80.961  1.00 26.49  ? 393 ALA A CA  1 
ATOM   2819 C  C   . ALA A 1 391 ? 31.300 111.239 -80.015  1.00 27.16  ? 393 ALA A C   1 
ATOM   2820 O  O   . ALA A 1 391 ? 30.690 110.215 -80.401  1.00 27.45  ? 393 ALA A O   1 
ATOM   2821 C  CB  . ALA A 1 391 ? 30.183 113.255 -81.138  1.00 27.15  ? 393 ALA A CB  1 
ATOM   2822 N  N   . MET A 1 392 ? 31.928 111.313 -78.839  1.00 26.98  ? 394 MET A N   1 
ATOM   2823 C  CA  . MET A 1 392 ? 31.556 110.546 -77.629  1.00 28.46  ? 394 MET A CA  1 
ATOM   2824 C  C   . MET A 1 392 ? 30.049 110.690 -77.445  1.00 30.44  ? 394 MET A C   1 
ATOM   2825 O  O   . MET A 1 392 ? 29.555 111.828 -77.621  1.00 30.89  ? 394 MET A O   1 
ATOM   2826 C  CB  . MET A 1 392 ? 32.233 111.186 -76.416  1.00 28.37  ? 394 MET A CB  1 
ATOM   2827 C  CG  . MET A 1 392 ? 31.912 110.492 -75.101  1.00 28.94  ? 394 MET A CG  1 
ATOM   2828 S  SD  . MET A 1 392 ? 32.652 111.315 -73.671  0.89 28.78  ? 394 MET A SD  1 
ATOM   2829 C  CE  . MET A 1 392 ? 31.384 112.534 -73.295  1.00 27.22  ? 394 MET A CE  1 
ATOM   2830 N  N   . LYS A 1 393 ? 29.359 109.622 -77.081  1.00 33.38  ? 395 LYS A N   1 
ATOM   2831 C  CA  . LYS A 1 393 ? 27.937 109.782 -76.706  1.00 36.95  ? 395 LYS A CA  1 
ATOM   2832 C  C   . LYS A 1 393 ? 27.947 110.243 -75.244  1.00 35.07  ? 395 LYS A C   1 
ATOM   2833 O  O   . LYS A 1 393 ? 28.772 109.754 -74.513  1.00 34.60  ? 395 LYS A O   1 
ATOM   2834 C  CB  . LYS A 1 393 ? 27.223 108.434 -76.768  1.00 41.64  ? 395 LYS A CB  1 
ATOM   2835 C  CG  . LYS A 1 393 ? 26.451 108.129 -78.038  1.00 46.60  ? 395 LYS A CG  1 
ATOM   2836 C  CD  . LYS A 1 393 ? 26.422 106.657 -78.348  1.00 52.14  ? 395 LYS A CD  1 
ATOM   2837 C  CE  . LYS A 1 393 ? 25.320 106.246 -79.303  1.00 56.05  ? 395 LYS A CE  1 
ATOM   2838 N  NZ  . LYS A 1 393 ? 24.823 104.877 -79.029  1.00 60.42  ? 395 LYS A NZ  1 
ATOM   2839 N  N   . ASP A 1 394 ? 27.028 111.110 -74.838  1.00 34.83  ? 396 ASP A N   1 
ATOM   2840 C  CA  . ASP A 1 394 ? 26.904 111.629 -73.446  1.00 36.65  ? 396 ASP A CA  1 
ATOM   2841 C  C   . ASP A 1 394 ? 26.942 110.522 -72.386  1.00 36.44  ? 396 ASP A C   1 
ATOM   2842 O  O   . ASP A 1 394 ? 26.361 109.469 -72.589  1.00 36.28  ? 396 ASP A O   1 
ATOM   2843 C  CB  . ASP A 1 394 ? 25.620 112.424 -73.274  1.00 38.05  ? 396 ASP A CB  1 
ATOM   2844 C  CG  . ASP A 1 394 ? 25.594 113.634 -74.161  1.00 39.43  ? 396 ASP A CG  1 
ATOM   2845 O  OD1 . ASP A 1 394 ? 26.584 113.871 -74.798  1.00 39.56  ? 396 ASP A OD1 1 
ATOM   2846 O  OD2 . ASP A 1 394 ? 24.584 114.303 -74.203  1.00 42.98  ? 396 ASP A OD2 1 
ATOM   2847 N  N   . ILE A 1 395 ? 27.569 110.818 -71.249  1.00 36.39  ? 397 ILE A N   1 
ATOM   2848 C  CA  . ILE A 1 395 ? 27.722 109.853 -70.130  1.00 36.84  ? 397 ILE A CA  1 
ATOM   2849 C  C   . ILE A 1 395 ? 26.981 110.423 -68.925  1.00 38.42  ? 397 ILE A C   1 
ATOM   2850 O  O   . ILE A 1 395 ? 27.443 111.418 -68.344  1.00 41.11  ? 397 ILE A O   1 
ATOM   2851 C  CB  . ILE A 1 395 ? 29.197 109.592 -69.804  1.00 34.84  ? 397 ILE A CB  1 
ATOM   2852 C  CG1 . ILE A 1 395 ? 29.956 109.092 -71.025  1.00 34.83  ? 397 ILE A CG1 1 
ATOM   2853 C  CG2 . ILE A 1 395 ? 29.307 108.617 -68.644  1.00 36.51  ? 397 ILE A CG2 1 
ATOM   2854 C  CD1 . ILE A 1 395 ? 31.454 109.163 -70.891  1.00 33.47  ? 397 ILE A CD1 1 
ATOM   2855 N  N   . GLU A 1 396 ? 25.885 109.787 -68.549  1.00 38.91  ? 398 GLU A N   1 
ATOM   2856 C  CA  . GLU A 1 396 ? 25.205 110.030 -67.261  1.00 38.73  ? 398 GLU A CA  1 
ATOM   2857 C  C   . GLU A 1 396 ? 25.898 109.145 -66.238  1.00 36.83  ? 398 GLU A C   1 
ATOM   2858 O  O   . GLU A 1 396 ? 26.067 107.935 -66.519  1.00 37.66  ? 398 GLU A O   1 
ATOM   2859 C  CB  . GLU A 1 396 ? 23.735 109.671 -67.436  1.00 42.78  ? 398 GLU A CB  1 
ATOM   2860 C  CG  . GLU A 1 396 ? 22.990 110.651 -68.326  1.00 44.40  ? 398 GLU A CG  1 
ATOM   2861 C  CD  . GLU A 1 396 ? 21.513 110.360 -68.419  1.00 49.04  ? 398 GLU A CD  1 
ATOM   2862 O  OE1 . GLU A 1 396 ? 21.125 109.557 -69.285  1.00 56.15  ? 398 GLU A OE1 1 
ATOM   2863 O  OE2 . GLU A 1 396 ? 20.760 110.888 -67.593  1.00 52.25  ? 398 GLU A OE2 1 
ATOM   2864 N  N   . PHE A 1 397 ? 26.325 109.689 -65.106  1.00 34.05  ? 399 PHE A N   1 
ATOM   2865 C  CA  . PHE A 1 397 ? 27.068 108.862 -64.118  1.00 33.54  ? 399 PHE A CA  1 
ATOM   2866 C  C   . PHE A 1 397 ? 26.729 109.317 -62.701  1.00 32.64  ? 399 PHE A C   1 
ATOM   2867 O  O   . PHE A 1 397 ? 26.185 110.436 -62.479  1.00 31.04  ? 399 PHE A O   1 
ATOM   2868 C  CB  . PHE A 1 397 ? 28.575 108.838 -64.426  1.00 32.00  ? 399 PHE A CB  1 
ATOM   2869 C  CG  . PHE A 1 397 ? 29.310 110.148 -64.258  1.00 30.30  ? 399 PHE A CG  1 
ATOM   2870 C  CD1 . PHE A 1 397 ? 29.201 111.141 -65.215  1.00 29.64  ? 399 PHE A CD1 1 
ATOM   2871 C  CD2 . PHE A 1 397 ? 30.093 110.400 -63.139  1.00 29.86  ? 399 PHE A CD2 1 
ATOM   2872 C  CE1 . PHE A 1 397 ? 29.849 112.354 -65.064  1.00 28.30  ? 399 PHE A CE1 1 
ATOM   2873 C  CE2 . PHE A 1 397 ? 30.735 111.615 -62.986  1.00 28.61  ? 399 PHE A CE2 1 
ATOM   2874 C  CZ  . PHE A 1 397 ? 30.606 112.593 -63.947  1.00 27.83  ? 399 PHE A CZ  1 
ATOM   2875 N  N   . THR A 1 398 ? 27.003 108.433 -61.756  1.00 33.91  ? 400 THR A N   1 
ATOM   2876 C  CA  . THR A 1 398 ? 26.735 108.720 -60.317  1.00 35.71  ? 400 THR A CA  1 
ATOM   2877 C  C   . THR A 1 398 ? 28.016 108.609 -59.486  1.00 35.52  ? 400 THR A C   1 
ATOM   2878 O  O   . THR A 1 398 ? 28.675 107.565 -59.533  1.00 36.22  ? 400 THR A O   1 
ATOM   2879 C  CB  . THR A 1 398 ? 25.567 107.901 -59.760  1.00 37.73  ? 400 THR A CB  1 
ATOM   2880 O  OG1 . THR A 1 398 ? 24.419 108.488 -60.370  1.00 38.81  ? 400 THR A OG1 1 
ATOM   2881 C  CG2 . THR A 1 398 ? 25.415 107.984 -58.249  1.00 37.87  ? 400 THR A CG2 1 
ATOM   2882 N  N   . ILE A 1 399 ? 28.321 109.689 -58.766  1.00 35.24  ? 401 ILE A N   1 
ATOM   2883 C  CA  . ILE A 1 399 ? 29.393 109.774 -57.736  1.00 34.85  ? 401 ILE A CA  1 
ATOM   2884 C  C   . ILE A 1 399 ? 28.746 109.557 -56.360  1.00 35.16  ? 401 ILE A C   1 
ATOM   2885 O  O   . ILE A 1 399 ? 27.746 110.241 -55.998  1.00 32.63  ? 401 ILE A O   1 
ATOM   2886 C  CB  . ILE A 1 399 ? 30.100 111.136 -57.754  1.00 33.90  ? 401 ILE A CB  1 
ATOM   2887 C  CG1 . ILE A 1 399 ? 30.715 111.468 -59.099  1.00 33.57  ? 401 ILE A CG1 1 
ATOM   2888 C  CG2 . ILE A 1 399 ? 31.120 111.194 -56.640  1.00 33.47  ? 401 ILE A CG2 1 
ATOM   2889 C  CD1 . ILE A 1 399 ? 31.314 112.826 -59.119  1.00 33.05  ? 401 ILE A CD1 1 
ATOM   2890 N  N   . SER A 1 400 ? 29.334 108.644 -55.605  1.00 36.07  ? 402 SER A N   1 
ATOM   2891 C  CA  . SER A 1 400 ? 28.849 108.281 -54.264  1.00 38.24  ? 402 SER A CA  1 
ATOM   2892 C  C   . SER A 1 400 ? 30.033 108.150 -53.299  1.00 36.32  ? 402 SER A C   1 
ATOM   2893 O  O   . SER A 1 400 ? 30.783 107.151 -53.382  1.00 36.00  ? 402 SER A O   1 
ATOM   2894 C  CB  . SER A 1 400 ? 28.014 107.060 -54.378  1.00 41.32  ? 402 SER A CB  1 
ATOM   2895 O  OG  . SER A 1 400 ? 27.104 107.019 -53.305  1.00 45.92  ? 402 SER A OG  1 
ATOM   2896 N  N   . GLY A 1 401 ? 30.201 109.155 -52.435  1.00 34.63  ? 403 GLY A N   1 
ATOM   2897 C  CA  . GLY A 1 401 ? 31.153 109.101 -51.321  1.00 33.72  ? 403 GLY A CA  1 
ATOM   2898 C  C   . GLY A 1 401 ? 30.484 108.448 -50.133  1.00 35.27  ? 403 GLY A C   1 
ATOM   2899 O  O   . GLY A 1 401 ? 29.437 108.958 -49.748  1.00 36.04  ? 403 GLY A O   1 
ATOM   2900 N  N   . THR A 1 402 ? 31.030 107.353 -49.597  1.00 35.96  ? 404 THR A N   1 
ATOM   2901 C  CA  . THR A 1 402 ? 30.571 106.726 -48.329  1.00 37.41  ? 404 THR A CA  1 
ATOM   2902 C  C   . THR A 1 402 ? 31.258 107.441 -47.148  1.00 37.37  ? 404 THR A C   1 
ATOM   2903 O  O   . THR A 1 402 ? 32.486 107.297 -46.975  1.00 36.36  ? 404 THR A O   1 
ATOM   2904 C  CB  . THR A 1 402 ? 30.816 105.209 -48.326  1.00 38.74  ? 404 THR A CB  1 
ATOM   2905 O  OG1 . THR A 1 402 ? 30.091 104.643 -49.407  1.00 38.32  ? 404 THR A OG1 1 
ATOM   2906 C  CG2 . THR A 1 402 ? 30.348 104.502 -47.071  1.00 40.21  ? 404 THR A CG2 1 
ATOM   2907 N  N   . ILE A 1 403 ? 30.481 108.177 -46.361  1.00 38.63  ? 405 ILE A N   1 
ATOM   2908 C  CA  . ILE A 1 403 ? 30.927 108.849 -45.103  1.00 39.51  ? 405 ILE A CA  1 
ATOM   2909 C  C   . ILE A 1 403 ? 30.176 108.229 -43.911  1.00 42.15  ? 405 ILE A C   1 
ATOM   2910 O  O   . ILE A 1 403 ? 28.970 108.532 -43.749  1.00 41.69  ? 405 ILE A O   1 
ATOM   2911 C  CB  . ILE A 1 403 ? 30.664 110.360 -45.249  1.00 38.95  ? 405 ILE A CB  1 
ATOM   2912 C  CG1 . ILE A 1 403 ? 31.425 110.926 -46.460  1.00 37.34  ? 405 ILE A CG1 1 
ATOM   2913 C  CG2 . ILE A 1 403 ? 30.920 111.106 -43.927  1.00 38.65  ? 405 ILE A CG2 1 
ATOM   2914 C  CD1 . ILE A 1 403 ? 30.991 112.330 -46.863  1.00 36.49  ? 405 ILE A CD1 1 
ATOM   2915 N  N   . ASP A 1 404 ? 30.867 107.433 -43.089  1.00 43.40  ? 406 ASP A N   1 
ATOM   2916 C  CA  . ASP A 1 404 ? 30.274 106.741 -41.915  1.00 45.76  ? 406 ASP A CA  1 
ATOM   2917 C  C   . ASP A 1 404 ? 29.979 107.732 -40.768  1.00 47.96  ? 406 ASP A C   1 
ATOM   2918 O  O   . ASP A 1 404 ? 30.143 108.977 -40.933  1.00 46.04  ? 406 ASP A O   1 
ATOM   2919 C  CB  . ASP A 1 404 ? 31.132 105.551 -41.476  1.00 46.61  ? 406 ASP A CB  1 
ATOM   2920 C  CG  . ASP A 1 404 ? 32.453 105.918 -40.828  1.00 45.74  ? 406 ASP A CG  1 
ATOM   2921 O  OD1 . ASP A 1 404 ? 32.595 107.089 -40.403  1.00 45.09  ? 406 ASP A OD1 1 
ATOM   2922 O  OD2 . ASP A 1 404 ? 33.346 105.034 -40.797  1.00 46.24  ? 406 ASP A OD2 1 
ATOM   2923 N  N   . SER A 1 405 ? 29.458 107.200 -39.652  1.00 50.93  ? 407 SER A N   1 
ATOM   2924 C  CA  . SER A 1 405 ? 28.905 107.980 -38.508  1.00 50.80  ? 407 SER A CA  1 
ATOM   2925 C  C   . SER A 1 405 ? 30.012 108.812 -37.831  1.00 48.21  ? 407 SER A C   1 
ATOM   2926 O  O   . SER A 1 405 ? 29.723 109.995 -37.535  1.00 46.87  ? 407 SER A O   1 
ATOM   2927 C  CB  . SER A 1 405 ? 28.196 107.062 -37.550  1.00 53.58  ? 407 SER A CB  1 
ATOM   2928 O  OG  . SER A 1 405 ? 29.019 105.946 -37.243  1.00 55.02  ? 407 SER A OG  1 
ATOM   2929 N  N   . THR A 1 406 ? 31.217 108.238 -37.651  1.00 46.83  ? 408 THR A N   1 
ATOM   2930 C  CA  . THR A 1 406 ? 32.475 108.938 -37.238  1.00 46.98  ? 408 THR A CA  1 
ATOM   2931 C  C   . THR A 1 406 ? 32.724 110.176 -38.101  1.00 47.57  ? 408 THR A C   1 
ATOM   2932 O  O   . THR A 1 406 ? 33.101 111.210 -37.543  1.00 47.81  ? 408 THR A O   1 
ATOM   2933 C  CB  . THR A 1 406 ? 33.732 108.093 -37.458  1.00 47.47  ? 408 THR A CB  1 
ATOM   2934 O  OG1 . THR A 1 406 ? 33.398 106.844 -36.879  1.00 50.93  ? 408 THR A OG1 1 
ATOM   2935 C  CG2 . THR A 1 406 ? 34.997 108.646 -36.843  1.00 45.44  ? 408 THR A CG2 1 
ATOM   2936 N  N   . GLY A 1 407 ? 32.559 110.060 -39.418  1.00 46.12  ? 409 GLY A N   1 
ATOM   2937 C  CA  . GLY A 1 407 ? 32.892 111.139 -40.364  1.00 45.63  ? 409 GLY A CA  1 
ATOM   2938 C  C   . GLY A 1 407 ? 34.095 110.802 -41.237  1.00 43.72  ? 409 GLY A C   1 
ATOM   2939 O  O   . GLY A 1 407 ? 34.647 111.764 -41.777  1.00 42.14  ? 409 GLY A O   1 
ATOM   2940 N  N   . ASP A 1 408 ? 34.452 109.507 -41.372  1.00 43.37  ? 410 ASP A N   1 
ATOM   2941 C  CA  . ASP A 1 408 ? 35.527 108.963 -42.252  1.00 43.50  ? 410 ASP A CA  1 
ATOM   2942 C  C   . ASP A 1 408 ? 34.981 108.776 -43.673  1.00 39.57  ? 410 ASP A C   1 
ATOM   2943 O  O   . ASP A 1 408 ? 33.895 108.167 -43.864  1.00 38.00  ? 410 ASP A O   1 
ATOM   2944 C  CB  . ASP A 1 408 ? 36.131 107.651 -41.740  1.00 48.09  ? 410 ASP A CB  1 
ATOM   2945 C  CG  . ASP A 1 408 ? 36.615 107.742 -40.296  1.00 55.38  ? 410 ASP A CG  1 
ATOM   2946 O  OD1 . ASP A 1 408 ? 36.994 108.888 -39.857  1.00 56.55  ? 410 ASP A OD1 1 
ATOM   2947 O  OD2 . ASP A 1 408 ? 36.573 106.686 -39.589  1.00 62.68  ? 410 ASP A OD2 1 
ATOM   2948 N  N   . LEU A 1 409 ? 35.690 109.322 -44.653  1.00 35.71  ? 411 LEU A N   1 
ATOM   2949 C  CA  . LEU A 1 409 ? 35.404 108.954 -46.056  1.00 32.93  ? 411 LEU A CA  1 
ATOM   2950 C  C   . LEU A 1 409 ? 36.044 107.585 -46.264  1.00 32.60  ? 411 LEU A C   1 
ATOM   2951 O  O   . LEU A 1 409 ? 37.269 107.510 -46.261  1.00 31.20  ? 411 LEU A O   1 
ATOM   2952 C  CB  . LEU A 1 409 ? 35.954 110.023 -46.987  1.00 31.85  ? 411 LEU A CB  1 
ATOM   2953 C  CG  . LEU A 1 409 ? 35.783 109.680 -48.465  1.00 31.90  ? 411 LEU A CG  1 
ATOM   2954 C  CD1 . LEU A 1 409 ? 34.394 110.032 -48.966  1.00 31.03  ? 411 LEU A CD1 1 
ATOM   2955 C  CD2 . LEU A 1 409 ? 36.855 110.367 -49.280  1.00 32.14  ? 411 LEU A CD2 1 
ATOM   2956 N  N   . THR A 1 410 ? 35.234 106.538 -46.357  1.00 34.12  ? 412 THR A N   1 
ATOM   2957 C  CA  . THR A 1 410 ? 35.692 105.118 -46.387  1.00 37.17  ? 412 THR A CA  1 
ATOM   2958 C  C   . THR A 1 410 ? 35.674 104.562 -47.815  1.00 38.86  ? 412 THR A C   1 
ATOM   2959 O  O   . THR A 1 410 ? 36.415 103.614 -48.104  1.00 40.99  ? 412 THR A O   1 
ATOM   2960 C  CB  . THR A 1 410 ? 34.798 104.273 -45.479  1.00 37.89  ? 412 THR A CB  1 
ATOM   2961 O  OG1 . THR A 1 410 ? 33.435 104.478 -45.857  1.00 37.52  ? 412 THR A OG1 1 
ATOM   2962 C  CG2 . THR A 1 410 ? 35.012 104.635 -44.029  1.00 38.29  ? 412 THR A CG2 1 
ATOM   2963 N  N   . ASN A 1 411 ? 34.828 105.125 -48.674  1.00 39.95  ? 413 ASN A N   1 
ATOM   2964 C  CA  . ASN A 1 411 ? 34.595 104.605 -50.045  1.00 39.79  ? 413 ASN A CA  1 
ATOM   2965 C  C   . ASN A 1 411 ? 34.240 105.764 -50.961  1.00 35.91  ? 413 ASN A C   1 
ATOM   2966 O  O   . ASN A 1 411 ? 33.628 106.731 -50.489  1.00 33.83  ? 413 ASN A O   1 
ATOM   2967 C  CB  . ASN A 1 411 ? 33.469 103.560 -50.084  1.00 43.74  ? 413 ASN A CB  1 
ATOM   2968 C  CG  . ASN A 1 411 ? 33.875 102.288 -50.803  1.00 45.84  ? 413 ASN A CG  1 
ATOM   2969 O  OD1 . ASN A 1 411 ? 34.352 101.349 -50.162  1.00 47.30  ? 413 ASN A OD1 1 
ATOM   2970 N  ND2 . ASN A 1 411 ? 33.756 102.265 -52.121  1.00 44.12  ? 413 ASN A ND2 1 
ATOM   2971 N  N   . LEU A 1 412 ? 34.614 105.638 -52.229  1.00 34.21  ? 414 LEU A N   1 
ATOM   2972 C  CA  . LEU A 1 412 ? 34.223 106.588 -53.282  1.00 32.53  ? 414 LEU A CA  1 
ATOM   2973 C  C   . LEU A 1 412 ? 34.052 105.802 -54.573  1.00 34.03  ? 414 LEU A C   1 
ATOM   2974 O  O   . LEU A 1 412 ? 35.028 105.161 -55.022  1.00 35.13  ? 414 LEU A O   1 
ATOM   2975 C  CB  . LEU A 1 412 ? 35.301 107.656 -53.420  1.00 30.57  ? 414 LEU A CB  1 
ATOM   2976 C  CG  . LEU A 1 412 ? 35.169 108.586 -54.623  1.00 28.44  ? 414 LEU A CG  1 
ATOM   2977 C  CD1 . LEU A 1 412 ? 33.961 109.492 -54.507  1.00 28.13  ? 414 LEU A CD1 1 
ATOM   2978 C  CD2 . LEU A 1 412 ? 36.416 109.418 -54.768  1.00 27.58  ? 414 LEU A CD2 1 
ATOM   2979 N  N   . THR A 1 413 ? 32.864 105.890 -55.168  1.00 34.01  ? 415 THR A N   1 
ATOM   2980 C  CA  . THR A 1 413 ? 32.503 105.109 -56.365  1.00 34.50  ? 415 THR A CA  1 
ATOM   2981 C  C   . THR A 1 413 ? 31.922 106.040 -57.431  1.00 34.32  ? 415 THR A C   1 
ATOM   2982 O  O   . THR A 1 413 ? 31.356 107.104 -57.098  1.00 32.45  ? 415 THR A O   1 
ATOM   2983 C  CB  . THR A 1 413 ? 31.538 103.991 -55.996  1.00 36.44  ? 415 THR A CB  1 
ATOM   2984 O  OG1 . THR A 1 413 ? 30.311 104.674 -55.734  1.00 37.35  ? 415 THR A OG1 1 
ATOM   2985 C  CG2 . THR A 1 413 ? 32.031 103.181 -54.817  1.00 37.54  ? 415 THR A CG2 1 
ATOM   2986 N  N   . ALA A 1 414 ? 32.143 105.671 -58.686  1.00 34.06  ? 416 ALA A N   1 
ATOM   2987 C  CA  . ALA A 1 414 ? 31.505 106.319 -59.848  1.00 34.89  ? 416 ALA A CA  1 
ATOM   2988 C  C   . ALA A 1 414 ? 31.022 105.196 -60.776  1.00 35.92  ? 416 ALA A C   1 
ATOM   2989 O  O   . ALA A 1 414 ? 31.802 104.261 -61.091  1.00 35.27  ? 416 ALA A O   1 
ATOM   2990 C  CB  . ALA A 1 414 ? 32.464 107.282 -60.513  1.00 33.75  ? 416 ALA A CB  1 
ATOM   2991 N  N   . THR A 1 415 ? 29.753 105.245 -61.145  1.00 36.57  ? 417 THR A N   1 
ATOM   2992 C  CA  . THR A 1 415 ? 29.105 104.190 -61.955  1.00 38.35  ? 417 THR A CA  1 
ATOM   2993 C  C   . THR A 1 415 ? 28.328 104.859 -63.080  1.00 38.60  ? 417 THR A C   1 
ATOM   2994 O  O   . THR A 1 415 ? 27.841 106.013 -62.894  1.00 36.81  ? 417 THR A O   1 
ATOM   2995 C  CB  . THR A 1 415 ? 28.212 103.319 -61.075  1.00 40.69  ? 417 THR A CB  1 
ATOM   2996 O  OG1 . THR A 1 415 ? 27.229 104.233 -60.586  1.00 41.86  ? 417 THR A OG1 1 
ATOM   2997 C  CG2 . THR A 1 415 ? 28.962 102.658 -59.932  1.00 40.81  ? 417 THR A CG2 1 
ATOM   2998 N  N   . SER A 1 416 ? 28.245 104.156 -64.205  1.00 39.04  ? 418 SER A N   1 
ATOM   2999 C  CA  . SER A 1 416 ? 27.472 104.561 -65.401  1.00 41.59  ? 418 SER A CA  1 
ATOM   3000 C  C   . SER A 1 416 ? 27.115 103.293 -66.177  1.00 44.95  ? 418 SER A C   1 
ATOM   3001 O  O   . SER A 1 416 ? 27.956 102.342 -66.193  1.00 46.00  ? 418 SER A O   1 
ATOM   3002 C  CB  . SER A 1 416 ? 28.283 105.500 -66.249  1.00 39.41  ? 418 SER A CB  1 
ATOM   3003 O  OG  . SER A 1 416 ? 27.595 105.912 -67.404  1.00 38.51  ? 418 SER A OG  1 
ATOM   3004 N  N   . ALA A 1 417 ? 25.916 103.268 -66.761  1.00 46.88  ? 419 ALA A N   1 
ATOM   3005 C  CA  . ALA A 1 417 ? 25.494 102.239 -67.731  1.00 50.11  ? 419 ALA A CA  1 
ATOM   3006 C  C   . ALA A 1 417 ? 26.440 102.275 -68.937  1.00 50.82  ? 419 ALA A C   1 
ATOM   3007 O  O   . ALA A 1 417 ? 26.786 101.197 -69.421  1.00 53.91  ? 419 ALA A O   1 
ATOM   3008 C  CB  . ALA A 1 417 ? 24.066 102.486 -68.129  1.00 51.94  ? 419 ALA A CB  1 
ATOM   3009 N  N   . THR A 1 418 ? 26.902 103.464 -69.331  1.00 50.67  ? 420 THR A N   1 
ATOM   3010 C  CA  . THR A 1 418 ? 27.615 103.752 -70.606  1.00 48.79  ? 420 THR A CA  1 
ATOM   3011 C  C   . THR A 1 418 ? 29.137 103.666 -70.465  1.00 46.14  ? 420 THR A C   1 
ATOM   3012 O  O   . THR A 1 418 ? 29.768 103.671 -71.489  1.00 47.27  ? 420 THR A O   1 
ATOM   3013 C  CB  . THR A 1 418 ? 27.388 105.204 -71.060  1.00 50.31  ? 420 THR A CB  1 
ATOM   3014 O  OG1 . THR A 1 418 ? 26.212 105.684 -70.410  1.00 56.56  ? 420 THR A OG1 1 
ATOM   3015 C  CG2 . THR A 1 418 ? 27.289 105.388 -72.560  1.00 51.71  ? 420 THR A CG2 1 
ATOM   3016 N  N   . ALA A 1 419 ? 29.728 103.684 -69.269  1.00 44.65  ? 421 ALA A N   1 
ATOM   3017 C  CA  . ALA A 1 419 ? 31.175 103.981 -69.099  1.00 41.18  ? 421 ALA A CA  1 
ATOM   3018 C  C   . ALA A 1 419 ? 31.730 103.315 -67.832  1.00 39.89  ? 421 ALA A C   1 
ATOM   3019 O  O   . ALA A 1 419 ? 30.945 102.802 -67.010  1.00 41.90  ? 421 ALA A O   1 
ATOM   3020 C  CB  . ALA A 1 419 ? 31.363 105.480 -69.093  1.00 38.94  ? 421 ALA A CB  1 
ATOM   3021 N  N   . SER A 1 420 ? 33.049 103.280 -67.699  1.00 38.42  ? 422 SER A N   1 
ATOM   3022 C  CA  . SER A 1 420 ? 33.762 102.725 -66.519  1.00 39.84  ? 422 SER A CA  1 
ATOM   3023 C  C   . SER A 1 420 ? 34.702 103.784 -65.966  1.00 38.07  ? 422 SER A C   1 
ATOM   3024 O  O   . SER A 1 420 ? 35.427 104.413 -66.764  1.00 36.63  ? 422 SER A O   1 
ATOM   3025 C  CB  . SER A 1 420 ? 34.564 101.502 -66.835  1.00 42.25  ? 422 SER A CB  1 
ATOM   3026 O  OG  . SER A 1 420 ? 33.860 100.652 -67.718  1.00 46.98  ? 422 SER A OG  1 
ATOM   3027 N  N   . PHE A 1 421 ? 34.738 103.923 -64.645  1.00 37.59  ? 423 PHE A N   1 
ATOM   3028 C  CA  . PHE A 1 421 ? 35.629 104.881 -63.959  1.00 36.11  ? 423 PHE A CA  1 
ATOM   3029 C  C   . PHE A 1 421 ? 36.632 104.116 -63.111  1.00 38.03  ? 423 PHE A C   1 
ATOM   3030 O  O   . PHE A 1 421 ? 36.336 102.986 -62.742  1.00 40.05  ? 423 PHE A O   1 
ATOM   3031 C  CB  . PHE A 1 421 ? 34.808 105.849 -63.115  1.00 34.80  ? 423 PHE A CB  1 
ATOM   3032 C  CG  . PHE A 1 421 ? 33.820 106.662 -63.908  1.00 32.90  ? 423 PHE A CG  1 
ATOM   3033 C  CD1 . PHE A 1 421 ? 32.606 106.134 -64.261  1.00 34.07  ? 423 PHE A CD1 1 
ATOM   3034 C  CD2 . PHE A 1 421 ? 34.094 107.966 -64.253  1.00 31.80  ? 423 PHE A CD2 1 
ATOM   3035 C  CE1 . PHE A 1 421 ? 31.704 106.885 -64.992  1.00 35.85  ? 423 PHE A CE1 1 
ATOM   3036 C  CE2 . PHE A 1 421 ? 33.201 108.713 -64.997  1.00 32.10  ? 423 PHE A CE2 1 
ATOM   3037 C  CZ  . PHE A 1 421 ? 32.007 108.173 -65.364  1.00 34.13  ? 423 PHE A CZ  1 
ATOM   3038 N  N   . GLU A 1 422 ? 37.795 104.725 -62.875  1.00 38.33  ? 424 GLU A N   1 
ATOM   3039 C  CA  . GLU A 1 422 ? 38.704 104.413 -61.754  1.00 38.59  ? 424 GLU A CA  1 
ATOM   3040 C  C   . GLU A 1 422 ? 38.378 105.403 -60.633  1.00 35.39  ? 424 GLU A C   1 
ATOM   3041 O  O   . GLU A 1 422 ? 38.025 106.557 -60.914  1.00 32.44  ? 424 GLU A O   1 
ATOM   3042 C  CB  . GLU A 1 422 ? 40.153 104.606 -62.158  1.00 43.26  ? 424 GLU A CB  1 
ATOM   3043 C  CG  . GLU A 1 422 ? 40.584 103.785 -63.361  1.00 49.97  ? 424 GLU A CG  1 
ATOM   3044 C  CD  . GLU A 1 422 ? 41.009 102.385 -62.959  1.00 55.92  ? 424 GLU A CD  1 
ATOM   3045 O  OE1 . GLU A 1 422 ? 40.809 102.069 -61.782  1.00 62.43  ? 424 GLU A OE1 1 
ATOM   3046 O  OE2 . GLU A 1 422 ? 41.525 101.625 -63.806  1.00 60.17  ? 424 GLU A OE2 1 
ATOM   3047 N  N   . THR A 1 423 ? 38.490 104.969 -59.389  1.00 34.21  ? 425 THR A N   1 
ATOM   3048 C  CA  . THR A 1 423 ? 38.434 105.877 -58.221  1.00 32.29  ? 425 THR A CA  1 
ATOM   3049 C  C   . THR A 1 423 ? 39.503 105.485 -57.214  1.00 31.37  ? 425 THR A C   1 
ATOM   3050 O  O   . THR A 1 423 ? 39.865 104.298 -57.150  1.00 31.57  ? 425 THR A O   1 
ATOM   3051 C  CB  . THR A 1 423 ? 37.079 105.860 -57.520  1.00 32.18  ? 425 THR A CB  1 
ATOM   3052 O  OG1 . THR A 1 423 ? 37.082 104.594 -56.857  1.00 33.04  ? 425 THR A OG1 1 
ATOM   3053 C  CG2 . THR A 1 423 ? 35.922 106.075 -58.472  1.00 31.13  ? 425 THR A CG2 1 
ATOM   3054 N  N   . ASP A 1 424 ? 40.011 106.507 -56.536  1.00 30.31  ? 426 ASP A N   1 
ATOM   3055 C  CA  . ASP A 1 424 ? 40.874 106.394 -55.344  1.00 31.18  ? 426 ASP A CA  1 
ATOM   3056 C  C   . ASP A 1 424 ? 40.307 107.287 -54.239  1.00 29.22  ? 426 ASP A C   1 
ATOM   3057 O  O   . ASP A 1 424 ? 40.263 108.503 -54.396  1.00 27.45  ? 426 ASP A O   1 
ATOM   3058 C  CB  . ASP A 1 424 ? 42.306 106.738 -55.703  1.00 32.14  ? 426 ASP A CB  1 
ATOM   3059 C  CG  . ASP A 1 424 ? 43.211 106.506 -54.519  1.00 33.96  ? 426 ASP A CG  1 
ATOM   3060 O  OD1 . ASP A 1 424 ? 42.692 106.387 -53.399  1.00 34.95  ? 426 ASP A OD1 1 
ATOM   3061 O  OD2 . ASP A 1 424 ? 44.411 106.412 -54.727  1.00 37.32  ? 426 ASP A OD2 1 
ATOM   3062 N  N   . VAL A 1 425 ? 39.891 106.675 -53.141  1.00 30.52  ? 427 VAL A N   1 
ATOM   3063 C  CA  . VAL A 1 425 ? 39.275 107.399 -51.999  1.00 29.44  ? 427 VAL A CA  1 
ATOM   3064 C  C   . VAL A 1 425 ? 40.322 108.322 -51.363  1.00 28.71  ? 427 VAL A C   1 
ATOM   3065 O  O   . VAL A 1 425 ? 39.958 109.459 -50.992  1.00 27.02  ? 427 VAL A O   1 
ATOM   3066 C  CB  . VAL A 1 425 ? 38.640 106.424 -51.002  1.00 31.17  ? 427 VAL A CB  1 
ATOM   3067 C  CG1 . VAL A 1 425 ? 39.632 105.403 -50.473  1.00 33.22  ? 427 VAL A CG1 1 
ATOM   3068 C  CG2 . VAL A 1 425 ? 38.015 107.190 -49.859  1.00 31.44  ? 427 VAL A CG2 1 
ATOM   3069 N  N   . ASN A 1 426 ? 41.584 107.891 -51.305  1.00 29.89  ? 428 ASN A N   1 
ATOM   3070 C  CA  . ASN A 1 426 ? 42.705 108.676 -50.707  1.00 30.83  ? 428 ASN A CA  1 
ATOM   3071 C  C   . ASN A 1 426 ? 42.965 110.009 -51.431  1.00 28.52  ? 428 ASN A C   1 
ATOM   3072 O  O   . ASN A 1 426 ? 43.202 111.027 -50.771  1.00 29.23  ? 428 ASN A O   1 
ATOM   3073 C  CB  . ASN A 1 426 ? 43.982 107.846 -50.712  1.00 34.80  ? 428 ASN A CB  1 
ATOM   3074 C  CG  . ASN A 1 426 ? 43.805 106.512 -50.001  1.00 39.71  ? 428 ASN A CG  1 
ATOM   3075 O  OD1 . ASN A 1 426 ? 42.771 106.257 -49.374  1.00 41.44  ? 428 ASN A OD1 1 
ATOM   3076 N  ND2 . ASN A 1 426 ? 44.814 105.650 -50.081  1.00 43.50  ? 428 ASN A ND2 1 
ATOM   3077 N  N   . THR A 1 427 ? 42.939 110.023 -52.764  1.00 27.03  ? 429 THR A N   1 
ATOM   3078 C  CA  . THR A 1 427 ? 43.249 111.225 -53.550  1.00 24.70  ? 429 THR A CA  1 
ATOM   3079 C  C   . THR A 1 427 ? 41.948 111.945 -53.867  1.00 22.74  ? 429 THR A C   1 
ATOM   3080 O  O   . THR A 1 427 ? 42.040 113.130 -54.335  1.00 21.97  ? 429 THR A O   1 
ATOM   3081 C  CB  . THR A 1 427 ? 44.053 110.832 -54.787  1.00 24.60  ? 429 THR A CB  1 
ATOM   3082 O  OG1 . THR A 1 427 ? 43.287 109.906 -55.551  1.00 24.26  ? 429 THR A OG1 1 
ATOM   3083 C  CG2 . THR A 1 427 ? 45.353 110.192 -54.394  1.00 25.30  ? 429 THR A CG2 1 
ATOM   3084 N  N   . GLY A 1 428 ? 40.821 111.257 -53.664  1.00 21.85  ? 430 GLY A N   1 
ATOM   3085 C  CA  . GLY A 1 428 ? 39.481 111.732 -54.082  1.00 21.28  ? 430 GLY A CA  1 
ATOM   3086 C  C   . GLY A 1 428 ? 39.338 111.820 -55.608  1.00 20.95  ? 430 GLY A C   1 
ATOM   3087 O  O   . GLY A 1 428 ? 38.432 112.529 -56.074  1.00 19.24  ? 430 GLY A O   1 
ATOM   3088 N  N   . ILE A 1 429 ? 40.210 111.153 -56.368  1.00 22.11  ? 431 ILE A N   1 
ATOM   3089 C  CA  . ILE A 1 429 ? 40.237 111.285 -57.861  1.00 22.79  ? 431 ILE A CA  1 
ATOM   3090 C  C   . ILE A 1 429 ? 39.467 110.137 -58.516  1.00 23.11  ? 431 ILE A C   1 
ATOM   3091 O  O   . ILE A 1 429 ? 39.741 108.994 -58.209  1.00 23.71  ? 431 ILE A O   1 
ATOM   3092 C  CB  . ILE A 1 429 ? 41.667 111.397 -58.409  1.00 23.13  ? 431 ILE A CB  1 
ATOM   3093 C  CG1 . ILE A 1 429 ? 42.356 112.698 -57.999  1.00 22.81  ? 431 ILE A CG1 1 
ATOM   3094 C  CG2 . ILE A 1 429 ? 41.653 111.249 -59.909  1.00 23.68  ? 431 ILE A CG2 1 
ATOM   3095 C  CD1 . ILE A 1 429 ? 43.836 112.581 -58.109  1.00 23.63  ? 431 ILE A CD1 1 
ATOM   3096 N  N   . ILE A 1 430 ? 38.501 110.505 -59.346  1.00 22.93  ? 432 ILE A N   1 
ATOM   3097 C  CA  . ILE A 1 430 ? 37.724 109.628 -60.260  1.00 23.90  ? 432 ILE A CA  1 
ATOM   3098 C  C   . ILE A 1 430 ? 38.255 109.821 -61.675  1.00 23.32  ? 432 ILE A C   1 
ATOM   3099 O  O   . ILE A 1 430 ? 38.173 110.957 -62.153  1.00 20.98  ? 432 ILE A O   1 
ATOM   3100 C  CB  . ILE A 1 430 ? 36.262 110.055 -60.227  1.00 24.40  ? 432 ILE A CB  1 
ATOM   3101 C  CG1 . ILE A 1 430 ? 35.714 110.021 -58.805  1.00 25.83  ? 432 ILE A CG1 1 
ATOM   3102 C  CG2 . ILE A 1 430 ? 35.450 109.226 -61.196  1.00 24.82  ? 432 ILE A CG2 1 
ATOM   3103 C  CD1 . ILE A 1 430 ? 34.533 110.977 -58.618  1.00 26.24  ? 432 ILE A CD1 1 
ATOM   3104 N  N   . THR A 1 431 ? 38.790 108.767 -62.287  1.00 24.76  ? 433 THR A N   1 
ATOM   3105 C  CA  . THR A 1 431 ? 39.359 108.820 -63.652  1.00 24.65  ? 433 THR A CA  1 
ATOM   3106 C  C   . THR A 1 431 ? 38.366 108.263 -64.684  1.00 25.04  ? 433 THR A C   1 
ATOM   3107 O  O   . THR A 1 431 ? 37.887 107.131 -64.547  1.00 26.41  ? 433 THR A O   1 
ATOM   3108 C  CB  . THR A 1 431 ? 40.659 108.025 -63.789  1.00 25.74  ? 433 THR A CB  1 
ATOM   3109 O  OG1 . THR A 1 431 ? 41.593 108.507 -62.846  1.00 25.53  ? 433 THR A OG1 1 
ATOM   3110 C  CG2 . THR A 1 431 ? 41.285 108.173 -65.168  1.00 27.25  ? 433 THR A CG2 1 
ATOM   3111 N  N   . LEU A 1 432 ? 38.145 109.004 -65.757  1.00 24.07  ? 434 LEU A N   1 
ATOM   3112 C  CA  . LEU A 1 432 ? 37.472 108.494 -66.968  1.00 24.09  ? 434 LEU A CA  1 
ATOM   3113 C  C   . LEU A 1 432 ? 38.433 108.661 -68.137  1.00 24.34  ? 434 LEU A C   1 
ATOM   3114 O  O   . LEU A 1 432 ? 38.863 109.795 -68.433  1.00 22.14  ? 434 LEU A O   1 
ATOM   3115 C  CB  . LEU A 1 432 ? 36.172 109.264 -67.164  1.00 23.32  ? 434 LEU A CB  1 
ATOM   3116 C  CG  . LEU A 1 432 ? 35.397 108.925 -68.437  1.00 23.29  ? 434 LEU A CG  1 
ATOM   3117 C  CD1 . LEU A 1 432 ? 34.914 107.483 -68.394  1.00 24.24  ? 434 LEU A CD1 1 
ATOM   3118 C  CD2 . LEU A 1 432 ? 34.228 109.879 -68.603  1.00 22.78  ? 434 LEU A CD2 1 
ATOM   3119 N  N   . LYS A 1 433 ? 38.771 107.547 -68.763  1.00 27.65  ? 435 LYS A N   1 
ATOM   3120 C  CA  . LYS A 1 433 ? 39.514 107.526 -70.052  1.00 28.71  ? 435 LYS A CA  1 
ATOM   3121 C  C   . LYS A 1 433 ? 38.532 107.488 -71.229  1.00 28.62  ? 435 LYS A C   1 
ATOM   3122 O  O   . LYS A 1 433 ? 37.756 106.566 -71.287  1.00 29.51  ? 435 LYS A O   1 
ATOM   3123 C  CB  . LYS A 1 433 ? 40.428 106.315 -70.075  1.00 31.41  ? 435 LYS A CB  1 
ATOM   3124 C  CG  . LYS A 1 433 ? 41.316 106.262 -71.294  1.00 34.16  ? 435 LYS A CG  1 
ATOM   3125 C  CD  . LYS A 1 433 ? 42.298 105.128 -71.238  1.00 38.58  ? 435 LYS A CD  1 
ATOM   3126 C  CE  . LYS A 1 433 ? 41.595 103.790 -71.345  1.00 43.92  ? 435 LYS A CE  1 
ATOM   3127 N  NZ  . LYS A 1 433 ? 42.564 102.677 -71.514  1.00 49.27  ? 435 LYS A NZ  1 
ATOM   3128 N  N   . VAL A 1 434 ? 38.565 108.475 -72.117  1.00 26.66  ? 436 VAL A N   1 
ATOM   3129 C  CA  . VAL A 1 434 ? 37.600 108.602 -73.242  1.00 27.24  ? 436 VAL A CA  1 
ATOM   3130 C  C   . VAL A 1 434 ? 38.370 108.299 -74.507  1.00 27.48  ? 436 VAL A C   1 
ATOM   3131 O  O   . VAL A 1 434 ? 39.288 109.092 -74.836  1.00 26.03  ? 436 VAL A O   1 
ATOM   3132 C  CB  . VAL A 1 434 ? 36.968 109.997 -73.388  1.00 26.57  ? 436 VAL A CB  1 
ATOM   3133 C  CG1 . VAL A 1 434 ? 36.139 110.061 -74.662  1.00 26.71  ? 436 VAL A CG1 1 
ATOM   3134 C  CG2 . VAL A 1 434 ? 36.160 110.384 -72.155  1.00 26.65  ? 436 VAL A CG2 1 
ATOM   3135 N  N   . VAL A 1 435 ? 38.020 107.189 -75.146  1.00 28.68  ? 437 VAL A N   1 
ATOM   3136 C  CA  . VAL A 1 435 ? 38.741 106.698 -76.342  1.00 29.15  ? 437 VAL A CA  1 
ATOM   3137 C  C   . VAL A 1 435 ? 38.009 107.220 -77.575  1.00 29.13  ? 437 VAL A C   1 
ATOM   3138 O  O   . VAL A 1 435 ? 36.836 106.889 -77.739  1.00 31.18  ? 437 VAL A O   1 
ATOM   3139 C  CB  . VAL A 1 435 ? 38.905 105.173 -76.328  1.00 30.64  ? 437 VAL A CB  1 
ATOM   3140 C  CG1 . VAL A 1 435 ? 39.631 104.719 -77.591  1.00 31.78  ? 437 VAL A CG1 1 
ATOM   3141 C  CG2 . VAL A 1 435 ? 39.648 104.714 -75.076  1.00 30.86  ? 437 VAL A CG2 1 
ATOM   3142 N  N   . ASN A 1 436 ? 38.666 108.073 -78.357  1.00 27.64  ? 438 ASN A N   1 
ATOM   3143 C  CA  . ASN A 1 436 ? 38.094 108.649 -79.601  1.00 27.92  ? 438 ASN A CA  1 
ATOM   3144 C  C   . ASN A 1 436 ? 38.357 107.690 -80.771  1.00 27.35  ? 438 ASN A C   1 
ATOM   3145 O  O   . ASN A 1 436 ? 39.483 107.223 -80.939  1.00 25.75  ? 438 ASN A O   1 
ATOM   3146 C  CB  . ASN A 1 436 ? 38.597 110.070 -79.862  1.00 28.30  ? 438 ASN A CB  1 
ATOM   3147 C  CG  . ASN A 1 436 ? 37.805 111.116 -79.090  1.00 29.44  ? 438 ASN A CG  1 
ATOM   3148 O  OD1 . ASN A 1 436 ? 36.961 111.839 -79.657  1.00 35.39  ? 438 ASN A OD1 1 
ATOM   3149 N  N   . LYS A 1 437 ? 37.307 107.380 -81.510  1.00 29.15  ? 439 LYS A N   1 
ATOM   3150 C  CA  . LYS A 1 437 ? 37.347 106.626 -82.793  1.00 30.63  ? 439 LYS A CA  1 
ATOM   3151 C  C   . LYS A 1 437 ? 37.316 107.604 -83.963  1.00 28.17  ? 439 LYS A C   1 
ATOM   3152 O  O   . LYS A 1 437 ? 36.440 108.473 -83.963  1.00 24.83  ? 439 LYS A O   1 
ATOM   3153 C  CB  . LYS A 1 437 ? 36.157 105.669 -82.841  1.00 35.19  ? 439 LYS A CB  1 
ATOM   3154 C  CG  . LYS A 1 437 ? 36.284 104.466 -81.904  1.00 39.97  ? 439 LYS A CG  1 
ATOM   3155 C  CD  . LYS A 1 437 ? 35.771 104.674 -80.482  1.00 44.02  ? 439 LYS A CD  1 
ATOM   3156 C  CE  . LYS A 1 437 ? 36.239 103.581 -79.527  1.00 46.12  ? 439 LYS A CE  1 
ATOM   3157 N  NZ  . LYS A 1 437 ? 35.862 103.890 -78.127  1.00 47.04  ? 439 LYS A NZ  1 
ATOM   3158 N  N   . GLN A 1 438 ? 38.220 107.406 -84.938  1.00 28.67  ? 440 GLN A N   1 
ATOM   3159 C  CA  . GLN A 1 438 ? 38.284 108.153 -86.219  1.00 28.64  ? 440 GLN A CA  1 
ATOM   3160 C  C   . GLN A 1 438 ? 36.999 107.997 -87.025  1.00 28.63  ? 440 GLN A C   1 
ATOM   3161 O  O   . GLN A 1 438 ? 36.357 106.935 -86.982  1.00 29.35  ? 440 GLN A O   1 
ATOM   3162 C  CB  . GLN A 1 438 ? 39.393 107.644 -87.133  1.00 30.31  ? 440 GLN A CB  1 
ATOM   3163 C  CG  . GLN A 1 438 ? 40.782 108.025 -86.646  1.00 31.31  ? 440 GLN A CG  1 
ATOM   3164 C  CD  . GLN A 1 438 ? 41.826 107.681 -87.670  1.00 32.90  ? 440 GLN A CD  1 
ATOM   3165 O  OE1 . GLN A 1 438 ? 41.611 107.886 -88.855  1.00 34.97  ? 440 GLN A OE1 1 
ATOM   3166 N  NE2 . GLN A 1 438 ? 42.958 107.158 -87.231  1.00 33.91  ? 440 GLN A NE2 1 
ATOM   3167 N  N   . GLY A 1 439 ? 36.632 109.042 -87.754  1.00 27.48  ? 441 GLY A N   1 
ATOM   3168 C  CA  . GLY A 1 439 ? 35.545 108.943 -88.739  1.00 28.30  ? 441 GLY A CA  1 
ATOM   3169 C  C   . GLY A 1 439 ? 35.938 108.033 -89.902  1.00 28.13  ? 441 GLY A C   1 
ATOM   3170 O  O   . GLY A 1 439 ? 37.038 107.424 -89.856  1.00 26.35  ? 441 GLY A O   1 
ATOM   3171 N  N   . ALA A 1 440 ? 35.050 107.918 -90.892  1.00 28.04  ? 442 ALA A N   1 
ATOM   3172 C  CA  . ALA A 1 440 ? 35.267 107.090 -92.093  1.00 28.72  ? 442 ALA A CA  1 
ATOM   3173 C  C   . ALA A 1 440 ? 35.801 107.997 -93.209  1.00 27.38  ? 442 ALA A C   1 
ATOM   3174 O  O   . ALA A 1 440 ? 35.279 109.128 -93.417  1.00 24.58  ? 442 ALA A O   1 
ATOM   3175 C  CB  . ALA A 1 440 ? 34.010 106.351 -92.468  1.00 30.10  ? 442 ALA A CB  1 
ATOM   3176 N  N   . LEU A 1 441 ? 36.889 107.548 -93.826  1.00 28.33  ? 443 LEU A N   1 
ATOM   3177 C  CA  . LEU A 1 441 ? 37.410 108.172 -95.053  1.00 29.75  ? 443 LEU A CA  1 
ATOM   3178 C  C   . LEU A 1 441 ? 36.866 107.350 -96.233  1.00 29.43  ? 443 LEU A C   1 
ATOM   3179 O  O   . LEU A 1 441 ? 37.443 106.272 -96.546  1.00 26.42  ? 443 LEU A O   1 
ATOM   3180 C  CB  . LEU A 1 441 ? 38.934 108.228 -95.021  1.00 32.39  ? 443 LEU A CB  1 
ATOM   3181 C  CG  . LEU A 1 441 ? 39.493 109.238 -96.025  1.00 34.39  ? 443 LEU A CG  1 
ATOM   3182 C  CD1 . LEU A 1 441 ? 39.803 110.569 -95.317  1.00 34.83  ? 443 LEU A CD1 1 
ATOM   3183 C  CD2 . LEU A 1 441 ? 40.694 108.679 -96.827  1.00 34.84  ? 443 LEU A CD2 1 
ATOM   3184 N  N   . LEU A 1 442 ? 35.724 107.803 -96.755  1.00 29.19  ? 444 LEU A N   1 
ATOM   3185 C  CA  . LEU A 1 442 ? 34.874 106.966 -97.620  1.00 31.55  ? 444 LEU A CA  1 
ATOM   3186 C  C   . LEU A 1 442 ? 35.411 107.018 -99.042  1.00 32.65  ? 444 LEU A C   1 
ATOM   3187 O  O   . LEU A 1 442 ? 35.746 108.084 -99.563  1.00 34.54  ? 444 LEU A O   1 
ATOM   3188 C  CB  . LEU A 1 442 ? 33.423 107.436 -97.548  1.00 31.60  ? 444 LEU A CB  1 
ATOM   3189 C  CG  . LEU A 1 442 ? 32.651 106.905 -96.341  1.00 32.96  ? 444 LEU A CG  1 
ATOM   3190 C  CD1 . LEU A 1 442 ? 31.219 107.408 -96.362  1.00 33.59  ? 444 LEU A CD1 1 
ATOM   3191 C  CD2 . LEU A 1 442 ? 32.702 105.380 -96.261  1.00 33.27  ? 444 LEU A CD2 1 
ATOM   3192 N  N   . PRO A 1 443 ? 35.469 105.858 -99.717  1.00 33.37  ? 445 PRO A N   1 
ATOM   3193 C  CA  . PRO A 1 443 ? 35.824 105.813 -101.141 1.00 33.14  ? 445 PRO A CA  1 
ATOM   3194 C  C   . PRO A 1 443 ? 34.778 106.412 -102.088 1.00 32.76  ? 445 PRO A C   1 
ATOM   3195 O  O   . PRO A 1 443 ? 33.619 106.331 -101.830 1.00 31.82  ? 445 PRO A O   1 
ATOM   3196 C  CB  . PRO A 1 443 ? 35.914 104.314 -101.427 1.00 34.64  ? 445 PRO A CB  1 
ATOM   3197 C  CG  . PRO A 1 443 ? 34.996 103.675 -100.374 1.00 36.11  ? 445 PRO A CG  1 
ATOM   3198 C  CD  . PRO A 1 443 ? 35.125 104.549 -99.151  1.00 34.11  ? 445 PRO A CD  1 
ATOM   3199 N  N   . ASN A 1 444 ? 35.254 106.946 -103.204 1.00 33.78  ? 446 ASN A N   1 
ATOM   3200 C  CA  . ASN A 1 444 ? 34.411 107.592 -104.241 1.00 35.26  ? 446 ASN A CA  1 
ATOM   3201 C  C   . ASN A 1 444 ? 34.579 106.826 -105.556 1.00 35.43  ? 446 ASN A C   1 
ATOM   3202 O  O   . ASN A 1 444 ? 35.707 106.759 -106.046 1.00 33.54  ? 446 ASN A O   1 
ATOM   3203 C  CB  . ASN A 1 444 ? 34.750 109.078 -104.405 1.00 35.11  ? 446 ASN A CB  1 
ATOM   3204 C  CG  . ASN A 1 444 ? 34.612 109.847 -103.108 1.00 33.35  ? 446 ASN A CG  1 
ATOM   3205 O  OD1 . ASN A 1 444 ? 35.551 110.490 -102.665 1.00 34.42  ? 446 ASN A OD1 1 
ATOM   3206 N  ND2 . ASN A 1 444 ? 33.469 109.752 -102.475 1.00 32.04  ? 446 ASN A ND2 1 
ATOM   3207 N  N   . THR A 1 445 ? 33.490 106.262 -106.077 1.00 36.71  ? 447 THR A N   1 
ATOM   3208 C  CA  . THR A 1 445 ? 33.492 105.534 -107.359 1.00 37.61  ? 447 THR A CA  1 
ATOM   3209 C  C   . THR A 1 445 ? 34.079 106.476 -108.418 1.00 37.64  ? 447 THR A C   1 
ATOM   3210 O  O   . THR A 1 445 ? 34.820 106.006 -109.234 1.00 40.11  ? 447 THR A O   1 
ATOM   3211 C  CB  . THR A 1 445 ? 32.088 105.015 -107.685 1.00 38.07  ? 447 THR A CB  1 
ATOM   3212 O  OG1 . THR A 1 445 ? 31.659 103.950 -106.824 1.00 35.49  ? 447 THR A OG1 1 
ATOM   3213 C  CG2 . THR A 1 445 ? 32.028 104.530 -109.122 1.00 39.70  ? 447 THR A CG2 1 
ATOM   3214 N  N   . THR B 1 27  ? 57.472 98.620  -125.139 1.00 79.22  ? 29  THR B N   1 
ATOM   3215 C  CA  . THR B 1 27  ? 57.008 99.569  -124.044 1.00 77.53  ? 29  THR B CA  1 
ATOM   3216 C  C   . THR B 1 27  ? 58.074 99.697  -122.934 1.00 75.82  ? 29  THR B C   1 
ATOM   3217 O  O   . THR B 1 27  ? 58.934 98.805  -122.810 1.00 79.12  ? 29  THR B O   1 
ATOM   3218 C  CB  . THR B 1 27  ? 55.641 99.177  -123.445 1.00 77.96  ? 29  THR B CB  1 
ATOM   3219 O  OG1 . THR B 1 27  ? 55.787 97.897  -122.831 1.00 78.75  ? 29  THR B OG1 1 
ATOM   3220 C  CG2 . THR B 1 27  ? 54.495 99.198  -124.443 1.00 76.97  ? 29  THR B CG2 1 
ATOM   3221 N  N   . TYR B 1 28  ? 58.025 100.777 -122.149 1.00 70.77  ? 30  TYR B N   1 
ATOM   3222 C  CA  . TYR B 1 28  ? 59.123 101.197 -121.242 1.00 67.16  ? 30  TYR B CA  1 
ATOM   3223 C  C   . TYR B 1 28  ? 58.585 101.483 -119.838 1.00 68.18  ? 30  TYR B C   1 
ATOM   3224 O  O   . TYR B 1 28  ? 57.349 101.674 -119.646 1.00 66.50  ? 30  TYR B O   1 
ATOM   3225 C  CB  . TYR B 1 28  ? 59.811 102.424 -121.833 1.00 65.22  ? 30  TYR B CB  1 
ATOM   3226 C  CG  . TYR B 1 28  ? 60.332 102.216 -123.230 1.00 64.46  ? 30  TYR B CG  1 
ATOM   3227 C  CD1 . TYR B 1 28  ? 61.486 101.485 -123.455 1.00 64.87  ? 30  TYR B CD1 1 
ATOM   3228 C  CD2 . TYR B 1 28  ? 59.674 102.743 -124.327 1.00 63.33  ? 30  TYR B CD2 1 
ATOM   3229 C  CE1 . TYR B 1 28  ? 61.980 101.287 -124.732 1.00 64.73  ? 30  TYR B CE1 1 
ATOM   3230 C  CE2 . TYR B 1 28  ? 60.151 102.549 -125.609 1.00 63.62  ? 30  TYR B CE2 1 
ATOM   3231 C  CZ  . TYR B 1 28  ? 61.301 101.813 -125.812 1.00 64.27  ? 30  TYR B CZ  1 
ATOM   3232 O  OH  . TYR B 1 28  ? 61.762 101.639 -127.077 1.00 63.47  ? 30  TYR B OH  1 
ATOM   3233 N  N   . THR B 1 29  ? 59.498 101.516 -118.870 1.00 66.92  ? 31  THR B N   1 
ATOM   3234 C  CA  . THR B 1 29  ? 59.150 101.585 -117.431 1.00 67.12  ? 31  THR B CA  1 
ATOM   3235 C  C   . THR B 1 29  ? 60.023 102.616 -116.720 1.00 65.23  ? 31  THR B C   1 
ATOM   3236 O  O   . THR B 1 29  ? 61.221 102.330 -116.473 1.00 62.13  ? 31  THR B O   1 
ATOM   3237 C  CB  . THR B 1 29  ? 59.248 100.214 -116.757 1.00 68.79  ? 31  THR B CB  1 
ATOM   3238 O  OG1 . THR B 1 29  ? 58.276 99.388  -117.387 1.00 70.17  ? 31  THR B OG1 1 
ATOM   3239 C  CG2 . THR B 1 29  ? 58.980 100.267 -115.269 1.00 67.96  ? 31  THR B CG2 1 
ATOM   3240 N  N   . ILE B 1 30  ? 59.393 103.734 -116.349 1.00 63.51  ? 32  ILE B N   1 
ATOM   3241 C  CA  . ILE B 1 30  ? 59.994 104.799 -115.502 1.00 58.82  ? 32  ILE B CA  1 
ATOM   3242 C  C   . ILE B 1 30  ? 59.840 104.391 -114.034 1.00 56.20  ? 32  ILE B C   1 
ATOM   3243 O  O   . ILE B 1 30  ? 58.725 104.036 -113.588 1.00 52.77  ? 32  ILE B O   1 
ATOM   3244 C  CB  . ILE B 1 30  ? 59.384 106.179 -115.805 1.00 56.92  ? 32  ILE B CB  1 
ATOM   3245 C  CG1 . ILE B 1 30  ? 59.642 106.588 -117.262 1.00 56.20  ? 32  ILE B CG1 1 
ATOM   3246 C  CG2 . ILE B 1 30  ? 59.918 107.192 -114.805 1.00 55.14  ? 32  ILE B CG2 1 
ATOM   3247 C  CD1 . ILE B 1 30  ? 58.769 107.722 -117.766 1.00 54.44  ? 32  ILE B CD1 1 
ATOM   3248 N  N   . GLN B 1 31  ? 60.967 104.397 -113.336 1.00 54.98  ? 33  GLN B N   1 
ATOM   3249 C  CA  . GLN B 1 31  ? 61.032 104.252 -111.866 1.00 55.06  ? 33  GLN B CA  1 
ATOM   3250 C  C   . GLN B 1 31  ? 61.145 105.666 -111.304 1.00 49.49  ? 33  GLN B C   1 
ATOM   3251 O  O   . GLN B 1 31  ? 62.110 106.392 -111.674 1.00 47.32  ? 33  GLN B O   1 
ATOM   3252 C  CB  . GLN B 1 31  ? 62.231 103.396 -111.439 1.00 59.52  ? 33  GLN B CB  1 
ATOM   3253 C  CG  . GLN B 1 31  ? 62.450 102.116 -112.247 1.00 60.81  ? 33  GLN B CG  1 
ATOM   3254 C  CD  . GLN B 1 31  ? 61.476 101.041 -111.838 1.00 64.15  ? 33  GLN B CD  1 
ATOM   3255 O  OE1 . GLN B 1 31  ? 61.001 101.004 -110.700 1.00 63.66  ? 33  GLN B OE1 1 
ATOM   3256 N  NE2 . GLN B 1 31  ? 61.153 100.168 -112.777 1.00 65.02  ? 33  GLN B NE2 1 
ATOM   3257 N  N   . LEU B 1 32  ? 60.184 106.057 -110.481 1.00 45.78  ? 34  LEU B N   1 
ATOM   3258 C  CA  . LEU B 1 32  ? 60.124 107.422 -109.915 1.00 44.04  ? 34  LEU B CA  1 
ATOM   3259 C  C   . LEU B 1 32  ? 60.563 107.364 -108.456 1.00 42.30  ? 34  LEU B C   1 
ATOM   3260 O  O   . LEU B 1 32  ? 59.742 106.995 -107.609 1.00 44.01  ? 34  LEU B O   1 
ATOM   3261 C  CB  . LEU B 1 32  ? 58.692 107.915 -110.062 1.00 45.20  ? 34  LEU B CB  1 
ATOM   3262 C  CG  . LEU B 1 32  ? 58.460 109.381 -109.755 1.00 45.28  ? 34  LEU B CG  1 
ATOM   3263 C  CD1 . LEU B 1 32  ? 59.305 110.270 -110.662 1.00 46.53  ? 34  LEU B CD1 1 
ATOM   3264 C  CD2 . LEU B 1 32  ? 56.980 109.674 -109.934 1.00 46.68  ? 34  LEU B CD2 1 
ATOM   3265 N  N   . SER B 1 33  ? 61.821 107.680 -108.187 1.00 39.12  ? 35  SER B N   1 
ATOM   3266 C  CA  . SER B 1 33  ? 62.432 107.429 -106.864 1.00 39.59  ? 35  SER B CA  1 
ATOM   3267 C  C   . SER B 1 33  ? 62.159 108.611 -105.936 1.00 38.04  ? 35  SER B C   1 
ATOM   3268 O  O   . SER B 1 33  ? 61.872 109.727 -106.439 1.00 36.59  ? 35  SER B O   1 
ATOM   3269 C  CB  . SER B 1 33  ? 63.906 107.130 -106.969 1.00 39.78  ? 35  SER B CB  1 
ATOM   3270 O  OG  . SER B 1 33  ? 64.625 108.242 -107.470 1.00 38.78  ? 35  SER B OG  1 
ATOM   3271 N  N   . GLY B 1 34  ? 62.275 108.352 -104.628 1.00 38.75  ? 36  GLY B N   1 
ATOM   3272 C  CA  . GLY B 1 34  ? 62.102 109.331 -103.541 1.00 37.30  ? 36  GLY B CA  1 
ATOM   3273 C  C   . GLY B 1 34  ? 60.637 109.697 -103.349 1.00 37.27  ? 36  GLY B C   1 
ATOM   3274 O  O   . GLY B 1 34  ? 60.376 110.818 -102.853 1.00 36.45  ? 36  GLY B O   1 
ATOM   3275 N  N   . THR B 1 35  ? 59.707 108.823 -103.757 1.00 36.95  ? 37  THR B N   1 
ATOM   3276 C  CA  . THR B 1 35  ? 58.257 109.036 -103.526 1.00 37.53  ? 37  THR B CA  1 
ATOM   3277 C  C   . THR B 1 35  ? 57.873 108.554 -102.113 1.00 39.72  ? 37  THR B C   1 
ATOM   3278 O  O   . THR B 1 35  ? 58.666 107.823 -101.446 1.00 41.53  ? 37  THR B O   1 
ATOM   3279 C  CB  . THR B 1 35  ? 57.400 108.352 -104.592 1.00 36.91  ? 37  THR B CB  1 
ATOM   3280 O  OG1 . THR B 1 35  ? 57.689 106.952 -104.566 1.00 37.65  ? 37  THR B OG1 1 
ATOM   3281 C  CG2 . THR B 1 35  ? 57.665 108.923 -105.968 1.00 36.66  ? 37  THR B CG2 1 
ATOM   3282 N  N   . SER B 1 36  ? 56.681 108.955 -101.683 1.00 39.46  ? 38  SER B N   1 
ATOM   3283 C  CA  . SER B 1 36  ? 56.001 108.464 -100.468 1.00 40.23  ? 38  SER B CA  1 
ATOM   3284 C  C   . SER B 1 36  ? 54.670 107.867 -100.926 1.00 41.59  ? 38  SER B C   1 
ATOM   3285 O  O   . SER B 1 36  ? 54.342 108.006 -102.110 1.00 36.64  ? 38  SER B O   1 
ATOM   3286 C  CB  . SER B 1 36  ? 55.832 109.583 -99.453  1.00 38.66  ? 38  SER B CB  1 
ATOM   3287 O  OG  . SER B 1 36  ? 54.762 110.463 -99.786  1.00 37.71  ? 38  SER B OG  1 
ATOM   3288 N  N   . GLU B 1 37  ? 53.934 107.233 -100.005 1.00 44.80  ? 39  GLU B N   1 
ATOM   3289 C  CA  . GLU B 1 37  ? 52.524 106.830 -100.255 1.00 46.56  ? 39  GLU B CA  1 
ATOM   3290 C  C   . GLU B 1 37  ? 51.727 108.125 -100.240 1.00 42.41  ? 39  GLU B C   1 
ATOM   3291 O  O   . GLU B 1 37  ? 52.299 109.137 -99.771  1.00 39.97  ? 39  GLU B O   1 
ATOM   3292 C  CB  . GLU B 1 37  ? 51.989 105.830 -99.225  1.00 51.78  ? 39  GLU B CB  1 
ATOM   3293 C  CG  . GLU B 1 37  ? 52.684 104.472 -99.235  1.00 55.99  ? 39  GLU B CG  1 
ATOM   3294 C  CD  . GLU B 1 37  ? 51.819 103.307 -98.756  1.00 60.33  ? 39  GLU B CD  1 
ATOM   3295 O  OE1 . GLU B 1 37  ? 50.913 102.909 -99.525  1.00 62.60  ? 39  GLU B OE1 1 
ATOM   3296 O  OE2 . GLU B 1 37  ? 52.040 102.799 -97.624  1.00 61.55  ? 39  GLU B OE2 1 
ATOM   3297 N  N   . GLY B 1 38  ? 50.514 108.097 -100.783 1.00 41.19  ? 40  GLY B N   1 
ATOM   3298 C  CA  . GLY B 1 38  ? 49.562 109.223 -100.690 1.00 41.64  ? 40  GLY B CA  1 
ATOM   3299 C  C   . GLY B 1 38  ? 49.235 109.867 -102.029 1.00 41.36  ? 40  GLY B C   1 
ATOM   3300 O  O   . GLY B 1 38  ? 48.162 110.477 -102.139 1.00 42.50  ? 40  GLY B O   1 
ATOM   3301 N  N   . HIS B 1 39  ? 50.089 109.705 -103.040 1.00 40.46  ? 41  HIS B N   1 
ATOM   3302 C  CA  . HIS B 1 39  ? 50.020 110.488 -104.293 1.00 38.28  ? 41  HIS B CA  1 
ATOM   3303 C  C   . HIS B 1 39  ? 49.393 109.638 -105.391 1.00 38.76  ? 41  HIS B C   1 
ATOM   3304 O  O   . HIS B 1 39  ? 49.620 108.438 -105.442 1.00 39.63  ? 41  HIS B O   1 
ATOM   3305 C  CB  . HIS B 1 39  ? 51.412 110.991 -104.685 1.00 36.52  ? 41  HIS B CB  1 
ATOM   3306 C  CG  . HIS B 1 39  ? 52.137 111.714 -103.605 1.00 34.77  ? 41  HIS B CG  1 
ATOM   3307 N  ND1 . HIS B 1 39  ? 52.532 113.016 -103.748 1.00 32.73  ? 41  HIS B ND1 1 
ATOM   3308 C  CD2 . HIS B 1 39  ? 52.533 111.308 -102.382 1.00 37.54  ? 41  HIS B CD2 1 
ATOM   3309 C  CE1 . HIS B 1 39  ? 53.148 113.392 -102.651 1.00 35.69  ? 41  HIS B CE1 1 
ATOM   3310 N  NE2 . HIS B 1 39  ? 53.112 112.367 -101.740 1.00 37.24  ? 41  HIS B NE2 1 
ATOM   3311 N  N   . TYR B 1 40  ? 48.640 110.285 -106.254 1.00 38.56  ? 42  TYR B N   1 
ATOM   3312 C  CA  . TYR B 1 40  ? 48.256 109.745 -107.571 1.00 39.93  ? 42  TYR B CA  1 
ATOM   3313 C  C   . TYR B 1 40  ? 49.015 110.523 -108.638 1.00 37.14  ? 42  TYR B C   1 
ATOM   3314 O  O   . TYR B 1 40  ? 48.601 111.656 -108.909 1.00 38.14  ? 42  TYR B O   1 
ATOM   3315 C  CB  . TYR B 1 40  ? 46.744 109.815 -107.685 1.00 43.26  ? 42  TYR B CB  1 
ATOM   3316 C  CG  . TYR B 1 40  ? 46.088 108.835 -106.755 1.00 48.00  ? 42  TYR B CG  1 
ATOM   3317 C  CD1 . TYR B 1 40  ? 45.980 107.497 -107.117 1.00 50.55  ? 42  TYR B CD1 1 
ATOM   3318 C  CD2 . TYR B 1 40  ? 45.647 109.220 -105.494 1.00 49.38  ? 42  TYR B CD2 1 
ATOM   3319 C  CE1 . TYR B 1 40  ? 45.417 106.562 -106.268 1.00 52.93  ? 42  TYR B CE1 1 
ATOM   3320 C  CE2 . TYR B 1 40  ? 45.070 108.299 -104.635 1.00 51.93  ? 42  TYR B CE2 1 
ATOM   3321 C  CZ  . TYR B 1 40  ? 44.956 106.975 -105.032 1.00 54.94  ? 42  TYR B CZ  1 
ATOM   3322 O  OH  . TYR B 1 40  ? 44.364 106.054 -104.234 1.00 58.89  ? 42  TYR B OH  1 
ATOM   3323 N  N   . TYR B 1 41  ? 50.072 109.918 -109.200 1.00 34.70  ? 43  TYR B N   1 
ATOM   3324 C  CA  . TYR B 1 41  ? 50.953 110.520 -110.221 1.00 31.54  ? 43  TYR B CA  1 
ATOM   3325 C  C   . TYR B 1 41  ? 50.380 110.257 -111.591 1.00 32.50  ? 43  TYR B C   1 
ATOM   3326 O  O   . TYR B 1 41  ? 50.137 109.099 -111.922 1.00 34.09  ? 43  TYR B O   1 
ATOM   3327 C  CB  . TYR B 1 41  ? 52.363 109.963 -110.123 1.00 29.78  ? 43  TYR B CB  1 
ATOM   3328 C  CG  . TYR B 1 41  ? 53.143 110.539 -108.966 1.00 28.69  ? 43  TYR B CG  1 
ATOM   3329 C  CD1 . TYR B 1 41  ? 53.460 111.893 -108.940 1.00 26.60  ? 43  TYR B CD1 1 
ATOM   3330 C  CD2 . TYR B 1 41  ? 53.549 109.744 -107.896 1.00 27.46  ? 43  TYR B CD2 1 
ATOM   3331 C  CE1 . TYR B 1 41  ? 54.175 112.431 -107.885 1.00 26.46  ? 43  TYR B CE1 1 
ATOM   3332 C  CE2 . TYR B 1 41  ? 54.299 110.266 -106.862 1.00 26.89  ? 43  TYR B CE2 1 
ATOM   3333 C  CZ  . TYR B 1 41  ? 54.575 111.622 -106.828 1.00 25.81  ? 43  TYR B CZ  1 
ATOM   3334 O  OH  . TYR B 1 41  ? 55.317 112.165 -105.828 1.00 24.32  ? 43  TYR B OH  1 
ATOM   3335 N  N   . GLU B 1 42  ? 50.228 111.318 -112.370 1.00 31.81  ? 44  GLU B N   1 
ATOM   3336 C  CA  . GLU B 1 42  ? 49.632 111.261 -113.709 1.00 32.43  ? 44  GLU B CA  1 
ATOM   3337 C  C   . GLU B 1 42  ? 50.730 111.402 -114.757 1.00 32.08  ? 44  GLU B C   1 
ATOM   3338 O  O   . GLU B 1 42  ? 51.577 112.309 -114.610 1.00 30.28  ? 44  GLU B O   1 
ATOM   3339 C  CB  . GLU B 1 42  ? 48.609 112.372 -113.855 1.00 33.47  ? 44  GLU B CB  1 
ATOM   3340 C  CG  . GLU B 1 42  ? 47.345 112.074 -113.111 1.00 35.73  ? 44  GLU B CG  1 
ATOM   3341 C  CD  . GLU B 1 42  ? 46.295 113.151 -113.256 1.00 37.16  ? 44  GLU B CD  1 
ATOM   3342 O  OE1 . GLU B 1 42  ? 46.641 114.237 -113.731 1.00 35.99  ? 44  GLU B OE1 1 
ATOM   3343 O  OE2 . GLU B 1 42  ? 45.148 112.901 -112.845 1.00 41.39  ? 44  GLU B OE2 1 
ATOM   3344 N  N   . VAL B 1 43  ? 50.661 110.577 -115.810 1.00 32.70  ? 45  VAL B N   1 
ATOM   3345 C  CA  . VAL B 1 43  ? 51.680 110.541 -116.899 1.00 31.93  ? 45  VAL B CA  1 
ATOM   3346 C  C   . VAL B 1 43  ? 51.027 110.843 -118.233 1.00 31.22  ? 45  VAL B C   1 
ATOM   3347 O  O   . VAL B 1 43  ? 50.212 110.066 -118.695 1.00 32.72  ? 45  VAL B O   1 
ATOM   3348 C  CB  . VAL B 1 43  ? 52.412 109.209 -116.932 1.00 32.68  ? 45  VAL B CB  1 
ATOM   3349 C  CG1 . VAL B 1 43  ? 53.627 109.337 -117.793 1.00 32.16  ? 45  VAL B CG1 1 
ATOM   3350 C  CG2 . VAL B 1 43  ? 52.792 108.786 -115.527 1.00 33.41  ? 45  VAL B CG2 1 
ATOM   3351 N  N   . TYR B 1 44  ? 51.344 111.999 -118.774 1.00 29.99  ? 46  TYR B N   1 
ATOM   3352 C  CA  . TYR B 1 44  ? 50.712 112.506 -120.006 1.00 31.11  ? 46  TYR B CA  1 
ATOM   3353 C  C   . TYR B 1 44  ? 51.647 112.229 -121.180 1.00 30.69  ? 46  TYR B C   1 
ATOM   3354 O  O   . TYR B 1 44  ? 52.801 112.653 -121.132 1.00 30.00  ? 46  TYR B O   1 
ATOM   3355 C  CB  . TYR B 1 44  ? 50.357 113.977 -119.833 1.00 30.53  ? 46  TYR B CB  1 
ATOM   3356 C  CG  . TYR B 1 44  ? 49.232 114.183 -118.856 1.00 31.66  ? 46  TYR B CG  1 
ATOM   3357 C  CD1 . TYR B 1 44  ? 47.908 114.150 -119.272 1.00 32.83  ? 46  TYR B CD1 1 
ATOM   3358 C  CD2 . TYR B 1 44  ? 49.491 114.379 -117.510 1.00 31.62  ? 46  TYR B CD2 1 
ATOM   3359 C  CE1 . TYR B 1 44  ? 46.869 114.368 -118.388 1.00 33.55  ? 46  TYR B CE1 1 
ATOM   3360 C  CE2 . TYR B 1 44  ? 48.461 114.604 -116.612 1.00 32.27  ? 46  TYR B CE2 1 
ATOM   3361 C  CZ  . TYR B 1 44  ? 47.149 114.606 -117.053 1.00 33.12  ? 46  TYR B CZ  1 
ATOM   3362 O  OH  . TYR B 1 44  ? 46.137 114.803 -116.157 1.00 34.13  ? 46  TYR B OH  1 
ATOM   3363 N  N   . HIS B 1 45  ? 51.146 111.542 -122.198 1.00 31.53  ? 47  HIS B N   1 
ATOM   3364 C  CA  . HIS B 1 45  ? 51.890 111.264 -123.450 1.00 31.97  ? 47  HIS B CA  1 
ATOM   3365 C  C   . HIS B 1 45  ? 51.857 112.530 -124.286 1.00 30.08  ? 47  HIS B C   1 
ATOM   3366 O  O   . HIS B 1 45  ? 50.766 112.871 -124.751 1.00 30.21  ? 47  HIS B O   1 
ATOM   3367 C  CB  . HIS B 1 45  ? 51.267 110.087 -124.194 1.00 35.51  ? 47  HIS B CB  1 
ATOM   3368 C  CG  . HIS B 1 45  ? 52.189 109.444 -125.160 1.00 37.33  ? 47  HIS B CG  1 
ATOM   3369 N  ND1 . HIS B 1 45  ? 51.771 108.406 -125.966 1.00 40.46  ? 47  HIS B ND1 1 
ATOM   3370 C  CD2 . HIS B 1 45  ? 53.484 109.692 -125.459 1.00 37.69  ? 47  HIS B CD2 1 
ATOM   3371 C  CE1 . HIS B 1 45  ? 52.779 108.040 -126.738 1.00 41.38  ? 47  HIS B CE1 1 
ATOM   3372 N  NE2 . HIS B 1 45  ? 53.846 108.811 -126.437 1.00 40.12  ? 47  HIS B NE2 1 
ATOM   3373 N  N   . ILE B 1 46  ? 52.998 113.201 -124.410 1.00 27.90  ? 48  ILE B N   1 
ATOM   3374 C  CA  . ILE B 1 46  ? 53.128 114.514 -125.097 1.00 26.89  ? 48  ILE B CA  1 
ATOM   3375 C  C   . ILE B 1 46  ? 53.559 114.247 -126.544 1.00 27.78  ? 48  ILE B C   1 
ATOM   3376 O  O   . ILE B 1 46  ? 52.926 114.764 -127.457 1.00 28.04  ? 48  ILE B O   1 
ATOM   3377 C  CB  . ILE B 1 46  ? 54.128 115.423 -124.358 1.00 25.06  ? 48  ILE B CB  1 
ATOM   3378 C  CG1 . ILE B 1 46  ? 53.820 115.590 -122.858 1.00 24.34  ? 48  ILE B CG1 1 
ATOM   3379 C  CG2 . ILE B 1 46  ? 54.227 116.754 -125.086 1.00 25.25  ? 48  ILE B CG2 1 
ATOM   3380 C  CD1 . ILE B 1 46  ? 52.407 115.974 -122.507 1.00 24.20  ? 48  ILE B CD1 1 
ATOM   3381 N  N   . PHE B 1 47  ? 54.641 113.501 -126.753 1.00 28.08  ? 49  PHE B N   1 
ATOM   3382 C  CA  . PHE B 1 47  ? 55.106 113.124 -128.109 1.00 28.69  ? 49  PHE B CA  1 
ATOM   3383 C  C   . PHE B 1 47  ? 55.112 111.599 -128.240 1.00 31.59  ? 49  PHE B C   1 
ATOM   3384 O  O   . PHE B 1 47  ? 55.605 110.905 -127.320 1.00 32.00  ? 49  PHE B O   1 
ATOM   3385 C  CB  . PHE B 1 47  ? 56.514 113.637 -128.361 1.00 26.67  ? 49  PHE B CB  1 
ATOM   3386 C  CG  . PHE B 1 47  ? 56.714 115.126 -128.369 1.00 24.97  ? 49  PHE B CG  1 
ATOM   3387 C  CD1 . PHE B 1 47  ? 55.765 115.984 -128.876 1.00 24.95  ? 49  PHE B CD1 1 
ATOM   3388 C  CD2 . PHE B 1 47  ? 57.923 115.667 -127.947 1.00 23.52  ? 49  PHE B CD2 1 
ATOM   3389 C  CE1 . PHE B 1 47  ? 56.008 117.356 -128.905 1.00 24.34  ? 49  PHE B CE1 1 
ATOM   3390 C  CE2 . PHE B 1 47  ? 58.172 117.027 -128.019 1.00 22.66  ? 49  PHE B CE2 1 
ATOM   3391 C  CZ  . PHE B 1 47  ? 57.212 117.874 -128.499 1.00 22.77  ? 49  PHE B CZ  1 
ATOM   3392 N  N   . SER B 1 48  ? 54.578 111.090 -129.357 1.00 34.73  ? 50  SER B N   1 
ATOM   3393 C  CA  . SER B 1 48  ? 54.794 109.707 -129.860 1.00 37.57  ? 50  SER B CA  1 
ATOM   3394 C  C   . SER B 1 48  ? 56.003 109.743 -130.797 1.00 39.89  ? 50  SER B C   1 
ATOM   3395 O  O   . SER B 1 48  ? 56.319 110.808 -131.384 1.00 40.71  ? 50  SER B O   1 
ATOM   3396 C  CB  . SER B 1 48  ? 53.586 109.134 -130.572 1.00 38.17  ? 50  SER B CB  1 
ATOM   3397 O  OG  . SER B 1 48  ? 53.215 109.963 -131.669 1.00 36.22  ? 50  SER B OG  1 
ATOM   3398 N  N   . GLY B 1 49  ? 56.682 108.613 -130.913 1.00 43.03  ? 51  GLY B N   1 
ATOM   3399 C  CA  . GLY B 1 49  ? 57.842 108.485 -131.805 1.00 44.36  ? 51  GLY B CA  1 
ATOM   3400 C  C   . GLY B 1 49  ? 58.420 107.088 -131.763 1.00 46.74  ? 51  GLY B C   1 
ATOM   3401 O  O   . GLY B 1 49  ? 57.895 106.229 -131.028 1.00 46.92  ? 51  GLY B O   1 
ATOM   3402 N  N   . THR B 1 50  ? 59.461 106.862 -132.562 1.00 49.01  ? 52  THR B N   1 
ATOM   3403 C  CA  . THR B 1 50  ? 60.238 105.602 -132.567 1.00 49.88  ? 52  THR B CA  1 
ATOM   3404 C  C   . THR B 1 50  ? 61.580 105.930 -131.916 1.00 50.72  ? 52  THR B C   1 
ATOM   3405 O  O   . THR B 1 50  ? 62.181 106.984 -132.186 1.00 47.39  ? 52  THR B O   1 
ATOM   3406 C  CB  . THR B 1 50  ? 60.236 104.976 -133.967 1.00 49.19  ? 52  THR B CB  1 
ATOM   3407 O  OG1 . THR B 1 50  ? 60.779 106.000 -134.809 1.00 47.20  ? 52  THR B OG1 1 
ATOM   3408 C  CG2 . THR B 1 50  ? 58.853 104.506 -134.388 1.00 48.31  ? 52  THR B CG2 1 
ATOM   3409 N  N   . LEU B 1 51  ? 61.947 105.099 -130.961 1.00 57.15  ? 53  LEU B N   1 
ATOM   3410 C  CA  . LEU B 1 51  ? 63.220 105.206 -130.224 1.00 62.27  ? 53  LEU B CA  1 
ATOM   3411 C  C   . LEU B 1 51  ? 64.155 104.180 -130.865 1.00 71.59  ? 53  LEU B C   1 
ATOM   3412 O  O   . LEU B 1 51  ? 63.847 102.968 -130.810 1.00 77.47  ? 53  LEU B O   1 
ATOM   3413 C  CB  . LEU B 1 51  ? 62.944 104.941 -128.743 1.00 60.43  ? 53  LEU B CB  1 
ATOM   3414 C  CG  . LEU B 1 51  ? 63.991 105.500 -127.793 1.00 58.87  ? 53  LEU B CG  1 
ATOM   3415 C  CD1 . LEU B 1 51  ? 63.949 107.022 -127.784 1.00 56.78  ? 53  LEU B CD1 1 
ATOM   3416 C  CD2 . LEU B 1 51  ? 63.775 104.932 -126.405 1.00 58.32  ? 53  LEU B CD2 1 
ATOM   3417 N  N   . ASP B 1 52  ? 65.192 104.653 -131.549 1.00 76.71  ? 54  ASP B N   1 
ATOM   3418 C  CA  . ASP B 1 52  ? 65.954 103.819 -132.516 1.00 80.53  ? 54  ASP B CA  1 
ATOM   3419 C  C   . ASP B 1 52  ? 67.136 103.226 -131.762 1.00 82.81  ? 54  ASP B C   1 
ATOM   3420 O  O   . ASP B 1 52  ? 67.279 103.530 -130.525 1.00 81.28  ? 54  ASP B O   1 
ATOM   3421 C  CB  . ASP B 1 52  ? 66.394 104.630 -133.739 1.00 82.67  ? 54  ASP B CB  1 
ATOM   3422 C  CG  . ASP B 1 52  ? 66.582 106.082 -133.361 1.00 82.45  ? 54  ASP B CG  1 
ATOM   3423 O  OD1 . ASP B 1 52  ? 67.479 106.352 -132.532 1.00 76.85  ? 54  ASP B OD1 1 
ATOM   3424 O  OD2 . ASP B 1 52  ? 65.751 106.908 -133.801 1.00 83.14  ? 54  ASP B OD2 1 
ATOM   3425 N  N   . THR B 1 53  ? 67.947 102.450 -132.491 1.00 83.69  ? 55  THR B N   1 
ATOM   3426 C  CA  . THR B 1 53  ? 69.231 101.857 -132.017 1.00 81.96  ? 55  THR B CA  1 
ATOM   3427 C  C   . THR B 1 53  ? 70.104 103.012 -131.465 1.00 79.74  ? 55  THR B C   1 
ATOM   3428 O  O   . THR B 1 53  ? 70.909 102.736 -130.562 1.00 76.30  ? 55  THR B O   1 
ATOM   3429 C  CB  . THR B 1 53  ? 69.849 100.941 -133.100 1.00 81.33  ? 55  THR B CB  1 
ATOM   3430 O  OG1 . THR B 1 53  ? 70.500 101.706 -134.108 1.00 79.10  ? 55  THR B OG1 1 
ATOM   3431 C  CG2 . THR B 1 53  ? 68.855 100.049 -133.819 1.00 80.39  ? 55  THR B CG2 1 
ATOM   3432 N  N   . SER B 1 54  ? 69.880 104.263 -131.926 1.00 77.44  ? 56  SER B N   1 
ATOM   3433 C  CA  . SER B 1 54  ? 70.619 105.505 -131.546 1.00 72.66  ? 56  SER B CA  1 
ATOM   3434 C  C   . SER B 1 54  ? 70.131 106.129 -130.230 1.00 66.98  ? 56  SER B C   1 
ATOM   3435 O  O   . SER B 1 54  ? 70.905 106.934 -129.693 1.00 66.70  ? 56  SER B O   1 
ATOM   3436 C  CB  . SER B 1 54  ? 70.583 106.546 -132.653 1.00 70.28  ? 56  SER B CB  1 
ATOM   3437 O  OG  . SER B 1 54  ? 71.511 106.224 -133.688 1.00 70.82  ? 56  SER B OG  1 
ATOM   3438 N  N   . ASN B 1 55  ? 68.899 105.874 -129.772 1.00 64.68  ? 57  ASN B N   1 
ATOM   3439 C  CA  . ASN B 1 55  ? 68.331 106.489 -128.524 1.00 65.62  ? 57  ASN B CA  1 
ATOM   3440 C  C   . ASN B 1 55  ? 67.942 107.967 -128.748 1.00 63.07  ? 57  ASN B C   1 
ATOM   3441 O  O   . ASN B 1 55  ? 67.650 108.690 -127.741 1.00 59.72  ? 57  ASN B O   1 
ATOM   3442 C  CB  . ASN B 1 55  ? 69.282 106.383 -127.320 1.00 65.76  ? 57  ASN B CB  1 
ATOM   3443 C  CG  . ASN B 1 55  ? 68.949 107.320 -126.174 1.00 65.44  ? 57  ASN B CG  1 
ATOM   3444 O  OD1 . ASN B 1 55  ? 69.679 108.288 -125.923 1.00 65.77  ? 57  ASN B OD1 1 
ATOM   3445 N  ND2 . ASN B 1 55  ? 67.858 107.034 -125.476 1.00 60.82  ? 57  ASN B ND2 1 
ATOM   3446 N  N   . THR B 1 56  ? 67.908 108.426 -130.006 1.00 59.20  ? 58  THR B N   1 
ATOM   3447 C  CA  . THR B 1 56  ? 67.233 109.697 -130.344 1.00 53.34  ? 58  THR B CA  1 
ATOM   3448 C  C   . THR B 1 56  ? 65.774 109.307 -130.559 1.00 48.36  ? 58  THR B C   1 
ATOM   3449 O  O   . THR B 1 56  ? 65.487 108.098 -130.765 1.00 46.53  ? 58  THR B O   1 
ATOM   3450 C  CB  . THR B 1 56  ? 67.925 110.428 -131.508 1.00 55.85  ? 58  THR B CB  1 
ATOM   3451 O  OG1 . THR B 1 56  ? 67.512 109.816 -132.730 1.00 58.37  ? 58  THR B OG1 1 
ATOM   3452 C  CG2 . THR B 1 56  ? 69.443 110.434 -131.445 1.00 56.16  ? 58  THR B CG2 1 
ATOM   3453 N  N   . LEU B 1 57  ? 64.873 110.270 -130.481 1.00 44.13  ? 59  LEU B N   1 
ATOM   3454 C  CA  . LEU B 1 57  ? 63.447 110.018 -130.794 1.00 41.98  ? 59  LEU B CA  1 
ATOM   3455 C  C   . LEU B 1 57  ? 63.119 110.560 -132.178 1.00 38.92  ? 59  LEU B C   1 
ATOM   3456 O  O   . LEU B 1 57  ? 63.342 111.756 -132.416 1.00 35.00  ? 59  LEU B O   1 
ATOM   3457 C  CB  . LEU B 1 57  ? 62.569 110.715 -129.764 1.00 40.51  ? 59  LEU B CB  1 
ATOM   3458 C  CG  . LEU B 1 57  ? 61.111 110.288 -129.798 1.00 41.78  ? 59  LEU B CG  1 
ATOM   3459 C  CD1 . LEU B 1 57  ? 60.976 108.880 -129.240 1.00 43.16  ? 59  LEU B CD1 1 
ATOM   3460 C  CD2 . LEU B 1 57  ? 60.258 111.272 -129.007 1.00 42.49  ? 59  LEU B CD2 1 
ATOM   3461 N  N   . THR B 1 58  ? 62.495 109.737 -133.005 1.00 40.52  ? 60  THR B N   1 
ATOM   3462 C  CA  . THR B 1 58  ? 62.273 110.070 -134.439 1.00 42.87  ? 60  THR B CA  1 
ATOM   3463 C  C   . THR B 1 58  ? 60.793 109.920 -134.776 1.00 45.25  ? 60  THR B C   1 
ATOM   3464 O  O   . THR B 1 58  ? 60.103 109.147 -134.067 1.00 45.50  ? 60  THR B O   1 
ATOM   3465 C  CB  . THR B 1 58  ? 63.142 109.203 -135.363 1.00 43.35  ? 60  THR B CB  1 
ATOM   3466 O  OG1 . THR B 1 58  ? 63.113 107.825 -134.982 1.00 42.62  ? 60  THR B OG1 1 
ATOM   3467 C  CG2 . THR B 1 58  ? 64.580 109.656 -135.359 1.00 43.89  ? 60  THR B CG2 1 
ATOM   3468 N  N   . ASN B 1 59  ? 60.347 110.593 -135.844 1.00 47.14  ? 61  ASN B N   1 
ATOM   3469 C  CA  . ASN B 1 59  ? 58.965 110.453 -136.373 1.00 49.20  ? 61  ASN B CA  1 
ATOM   3470 C  C   . ASN B 1 59  ? 58.047 110.935 -135.240 1.00 46.74  ? 61  ASN B C   1 
ATOM   3471 O  O   . ASN B 1 59  ? 57.157 110.180 -134.794 1.00 45.75  ? 61  ASN B O   1 
ATOM   3472 C  CB  . ASN B 1 59  ? 58.750 109.039 -136.938 1.00 51.37  ? 61  ASN B CB  1 
ATOM   3473 C  CG  . ASN B 1 59  ? 59.909 108.602 -137.837 1.00 54.14  ? 61  ASN B CG  1 
ATOM   3474 O  OD1 . ASN B 1 59  ? 60.516 109.410 -138.559 1.00 51.97  ? 61  ASN B OD1 1 
ATOM   3475 N  ND2 . ASN B 1 59  ? 60.275 107.326 -137.778 1.00 55.04  ? 61  ASN B ND2 1 
ATOM   3476 N  N   . ILE B 1 60  ? 58.309 112.170 -134.804 1.00 44.33  ? 62  ILE B N   1 
ATOM   3477 C  CA  . ILE B 1 60  ? 57.655 112.798 -133.623 1.00 44.01  ? 62  ILE B CA  1 
ATOM   3478 C  C   . ILE B 1 60  ? 56.328 113.439 -134.047 1.00 44.40  ? 62  ILE B C   1 
ATOM   3479 O  O   . ILE B 1 60  ? 56.278 114.267 -135.023 1.00 39.79  ? 62  ILE B O   1 
ATOM   3480 C  CB  . ILE B 1 60  ? 58.584 113.799 -132.925 1.00 42.05  ? 62  ILE B CB  1 
ATOM   3481 C  CG1 . ILE B 1 60  ? 59.767 113.088 -132.269 1.00 40.72  ? 62  ILE B CG1 1 
ATOM   3482 C  CG2 . ILE B 1 60  ? 57.804 114.630 -131.920 1.00 42.27  ? 62  ILE B CG2 1 
ATOM   3483 C  CD1 . ILE B 1 60  ? 60.857 114.029 -131.824 1.00 39.83  ? 62  ILE B CD1 1 
ATOM   3484 N  N   . GLU B 1 61  ? 55.285 113.022 -133.334 1.00 44.38  ? 63  GLU B N   1 
ATOM   3485 C  CA  . GLU B 1 61  ? 53.941 113.621 -133.407 1.00 46.10  ? 63  GLU B CA  1 
ATOM   3486 C  C   . GLU B 1 61  ? 53.461 113.913 -131.988 1.00 42.57  ? 63  GLU B C   1 
ATOM   3487 O  O   . GLU B 1 61  ? 53.976 113.299 -131.045 1.00 38.83  ? 63  GLU B O   1 
ATOM   3488 C  CB  . GLU B 1 61  ? 53.012 112.665 -134.138 1.00 52.79  ? 63  GLU B CB  1 
ATOM   3489 C  CG  . GLU B 1 61  ? 53.543 112.260 -135.504 1.00 57.19  ? 63  GLU B CG  1 
ATOM   3490 C  CD  . GLU B 1 61  ? 52.476 111.725 -136.431 1.00 66.26  ? 63  GLU B CD  1 
ATOM   3491 O  OE1 . GLU B 1 61  ? 51.411 111.275 -135.909 1.00 72.40  ? 63  GLU B OE1 1 
ATOM   3492 O  OE2 . GLU B 1 61  ? 52.703 111.759 -137.672 1.00 74.65  ? 63  GLU B OE2 1 
ATOM   3493 N  N   . TRP B 1 62  ? 52.533 114.864 -131.873 1.00 39.50  ? 64  TRP B N   1 
ATOM   3494 C  CA  . TRP B 1 62  ? 51.711 115.106 -130.673 1.00 36.78  ? 64  TRP B CA  1 
ATOM   3495 C  C   . TRP B 1 62  ? 50.929 113.841 -130.341 1.00 38.55  ? 64  TRP B C   1 
ATOM   3496 O  O   . TRP B 1 62  ? 50.323 113.246 -131.254 1.00 38.97  ? 64  TRP B O   1 
ATOM   3497 C  CB  . TRP B 1 62  ? 50.751 116.244 -130.927 1.00 35.65  ? 64  TRP B CB  1 
ATOM   3498 C  CG  . TRP B 1 62  ? 51.417 117.552 -131.124 1.00 33.07  ? 64  TRP B CG  1 
ATOM   3499 C  CD1 . TRP B 1 62  ? 51.348 118.323 -132.240 1.00 32.89  ? 64  TRP B CD1 1 
ATOM   3500 C  CD2 . TRP B 1 62  ? 52.150 118.296 -130.142 1.00 30.92  ? 64  TRP B CD2 1 
ATOM   3501 N  NE1 . TRP B 1 62  ? 52.057 119.477 -132.053 1.00 32.64  ? 64  TRP B NE1 1 
ATOM   3502 C  CE2 . TRP B 1 62  ? 52.550 119.493 -130.769 1.00 30.95  ? 64  TRP B CE2 1 
ATOM   3503 C  CE3 . TRP B 1 62  ? 52.496 118.075 -128.803 1.00 29.88  ? 64  TRP B CE3 1 
ATOM   3504 C  CZ2 . TRP B 1 62  ? 53.275 120.471 -130.103 1.00 29.66  ? 64  TRP B CZ2 1 
ATOM   3505 C  CZ3 . TRP B 1 62  ? 53.242 119.029 -128.163 1.00 28.64  ? 64  TRP B CZ3 1 
ATOM   3506 C  CH2 . TRP B 1 62  ? 53.641 120.200 -128.810 1.00 28.57  ? 64  TRP B CH2 1 
ATOM   3507 N  N   . ALA B 1 63  ? 50.935 113.462 -129.074 1.00 38.65  ? 65  ALA B N   1 
ATOM   3508 C  CA  . ALA B 1 63  ? 50.258 112.264 -128.553 1.00 41.01  ? 65  ALA B CA  1 
ATOM   3509 C  C   . ALA B 1 63  ? 48.977 112.687 -127.840 1.00 42.45  ? 65  ALA B C   1 
ATOM   3510 O  O   . ALA B 1 63  ? 48.740 113.877 -127.612 1.00 39.95  ? 65  ALA B O   1 
ATOM   3511 C  CB  . ALA B 1 63  ? 51.207 111.534 -127.650 1.00 41.13  ? 65  ALA B CB  1 
ATOM   3512 N  N   . PRO B 1 64  ? 48.102 111.716 -127.498 1.00 44.59  ? 66  PRO B N   1 
ATOM   3513 C  CA  . PRO B 1 64  ? 46.742 112.039 -127.076 1.00 45.78  ? 66  PRO B CA  1 
ATOM   3514 C  C   . PRO B 1 64  ? 46.687 112.892 -125.798 1.00 45.04  ? 66  PRO B C   1 
ATOM   3515 O  O   . PRO B 1 64  ? 45.669 113.456 -125.503 1.00 45.82  ? 66  PRO B O   1 
ATOM   3516 C  CB  . PRO B 1 64  ? 46.140 110.634 -126.879 1.00 48.38  ? 66  PRO B CB  1 
ATOM   3517 C  CG  . PRO B 1 64  ? 46.977 109.728 -127.764 1.00 47.49  ? 66  PRO B CG  1 
ATOM   3518 C  CD  . PRO B 1 64  ? 48.363 110.265 -127.552 1.00 45.74  ? 66  PRO B CD  1 
ATOM   3519 N  N   . GLY B 1 65  ? 47.795 112.956 -125.062 1.00 43.22  ? 67  GLY B N   1 
ATOM   3520 C  CA  . GLY B 1 65  ? 47.889 113.714 -123.809 1.00 41.16  ? 67  GLY B CA  1 
ATOM   3521 C  C   . GLY B 1 65  ? 47.942 115.208 -124.050 1.00 39.07  ? 67  GLY B C   1 
ATOM   3522 O  O   . GLY B 1 65  ? 47.973 115.919 -123.078 1.00 39.76  ? 67  GLY B O   1 
ATOM   3523 N  N   . VAL B 1 66  ? 47.961 115.689 -125.285 1.00 36.43  ? 68  VAL B N   1 
ATOM   3524 C  CA  . VAL B 1 66  ? 47.874 117.148 -125.534 1.00 35.57  ? 68  VAL B CA  1 
ATOM   3525 C  C   . VAL B 1 66  ? 46.618 117.417 -126.340 1.00 37.05  ? 68  VAL B C   1 
ATOM   3526 O  O   . VAL B 1 66  ? 46.358 116.669 -127.268 1.00 40.29  ? 68  VAL B O   1 
ATOM   3527 C  CB  . VAL B 1 66  ? 49.115 117.672 -126.265 1.00 34.20  ? 68  VAL B CB  1 
ATOM   3528 C  CG1 . VAL B 1 66  ? 49.069 119.184 -126.393 1.00 33.47  ? 68  VAL B CG1 1 
ATOM   3529 C  CG2 . VAL B 1 66  ? 50.379 117.216 -125.558 1.00 33.50  ? 68  VAL B CG2 1 
ATOM   3530 N  N   . THR B 1 67  ? 45.935 118.513 -126.044 1.00 38.18  ? 69  THR B N   1 
ATOM   3531 C  CA  . THR B 1 67  ? 44.688 118.927 -126.727 1.00 40.95  ? 69  THR B CA  1 
ATOM   3532 C  C   . THR B 1 67  ? 45.041 119.530 -128.073 1.00 41.32  ? 69  THR B C   1 
ATOM   3533 O  O   . THR B 1 67  ? 46.211 119.890 -128.277 1.00 40.01  ? 69  THR B O   1 
ATOM   3534 C  CB  . THR B 1 67  ? 43.878 119.960 -125.933 1.00 42.22  ? 69  THR B CB  1 
ATOM   3535 O  OG1 . THR B 1 67  ? 44.650 121.160 -125.815 1.00 42.49  ? 69  THR B OG1 1 
ATOM   3536 C  CG2 . THR B 1 67  ? 43.466 119.457 -124.566 1.00 42.73  ? 69  THR B CG2 1 
ATOM   3537 N  N   . GLU B 1 68  ? 44.025 119.669 -128.922 1.00 44.68  ? 70  GLU B N   1 
ATOM   3538 C  CA  . GLU B 1 68  ? 44.141 120.283 -130.266 1.00 46.81  ? 70  GLU B CA  1 
ATOM   3539 C  C   . GLU B 1 68  ? 44.564 121.750 -130.118 1.00 45.12  ? 70  GLU B C   1 
ATOM   3540 O  O   . GLU B 1 68  ? 45.320 122.242 -130.959 1.00 47.38  ? 70  GLU B O   1 
ATOM   3541 C  CB  . GLU B 1 68  ? 42.820 120.126 -131.028 1.00 50.79  ? 70  GLU B CB  1 
ATOM   3542 C  CG  . GLU B 1 68  ? 42.954 120.374 -132.519 1.00 54.97  ? 70  GLU B CG  1 
ATOM   3543 C  CD  . GLU B 1 68  ? 43.755 119.353 -133.340 1.00 58.89  ? 70  GLU B CD  1 
ATOM   3544 O  OE1 . GLU B 1 68  ? 44.594 118.603 -132.781 1.00 59.12  ? 70  GLU B OE1 1 
ATOM   3545 O  OE2 . GLU B 1 68  ? 43.527 119.284 -134.575 1.00 65.34  ? 70  GLU B OE2 1 
ATOM   3546 N  N   . ALA B 1 69  ? 44.054 122.427 -129.102 1.00 43.60  ? 71  ALA B N   1 
ATOM   3547 C  CA  . ALA B 1 69  ? 44.357 123.833 -128.785 1.00 42.43  ? 71  ALA B CA  1 
ATOM   3548 C  C   . ALA B 1 69  ? 45.855 123.952 -128.537 1.00 40.30  ? 71  ALA B C   1 
ATOM   3549 O  O   . ALA B 1 69  ? 46.439 124.904 -129.045 1.00 40.07  ? 71  ALA B O   1 
ATOM   3550 C  CB  . ALA B 1 69  ? 43.556 124.274 -127.579 1.00 42.38  ? 71  ALA B CB  1 
ATOM   3551 N  N   . GLY B 1 70  ? 46.404 123.055 -127.710 1.00 40.37  ? 72  GLY B N   1 
ATOM   3552 C  CA  . GLY B 1 70  ? 47.842 122.984 -127.379 1.00 38.46  ? 72  GLY B CA  1 
ATOM   3553 C  C   . GLY B 1 70  ? 48.659 122.694 -128.631 1.00 37.75  ? 72  GLY B C   1 
ATOM   3554 O  O   . GLY B 1 70  ? 49.641 123.398 -128.887 1.00 36.57  ? 72  GLY B O   1 
ATOM   3555 N  N   . ARG B 1 71  ? 48.269 121.688 -129.400 1.00 38.56  ? 73  ARG B N   1 
ATOM   3556 C  CA  . ARG B 1 71  ? 48.962 121.365 -130.678 1.00 39.72  ? 73  ARG B CA  1 
ATOM   3557 C  C   . ARG B 1 71  ? 49.043 122.617 -131.537 1.00 40.35  ? 73  ARG B C   1 
ATOM   3558 O  O   . ARG B 1 71  ? 50.151 122.906 -132.017 1.00 40.20  ? 73  ARG B O   1 
ATOM   3559 C  CB  . ARG B 1 71  ? 48.242 120.267 -131.439 1.00 40.57  ? 73  ARG B CB  1 
ATOM   3560 C  CG  . ARG B 1 71  ? 48.244 118.975 -130.661 1.00 41.18  ? 73  ARG B CG  1 
ATOM   3561 C  CD  . ARG B 1 71  ? 47.343 117.964 -131.284 1.00 43.19  ? 73  ARG B CD  1 
ATOM   3562 N  NE  . ARG B 1 71  ? 47.228 116.891 -130.315 1.00 44.27  ? 73  ARG B NE  1 
ATOM   3563 C  CZ  . ARG B 1 71  ? 47.050 115.626 -130.636 1.00 45.40  ? 73  ARG B CZ  1 
ATOM   3564 N  NH1 . ARG B 1 71  ? 46.968 115.294 -131.916 1.00 46.64  ? 73  ARG B NH1 1 
ATOM   3565 N  NH2 . ARG B 1 71  ? 46.940 114.708 -129.688 1.00 45.03  ? 73  ARG B NH2 1 
ATOM   3566 N  N   . THR B 1 72  ? 47.922 123.330 -131.678 1.00 42.50  ? 74  THR B N   1 
ATOM   3567 C  CA  . THR B 1 72  ? 47.807 124.553 -132.512 1.00 43.87  ? 74  THR B CA  1 
ATOM   3568 C  C   . THR B 1 72  ? 48.701 125.637 -131.904 1.00 42.43  ? 74  THR B C   1 
ATOM   3569 O  O   . THR B 1 72  ? 49.472 126.282 -132.641 1.00 41.51  ? 74  THR B O   1 
ATOM   3570 C  CB  . THR B 1 72  ? 46.355 125.031 -132.641 1.00 47.01  ? 74  THR B CB  1 
ATOM   3571 O  OG1 . THR B 1 72  ? 45.542 123.992 -133.192 1.00 48.84  ? 74  THR B OG1 1 
ATOM   3572 C  CG2 . THR B 1 72  ? 46.249 126.230 -133.555 1.00 48.71  ? 74  THR B CG2 1 
ATOM   3573 N  N   . HIS B 1 73  ? 48.637 125.801 -130.587 1.00 39.31  ? 75  HIS B N   1 
ATOM   3574 C  CA  . HIS B 1 73  ? 49.469 126.788 -129.863 1.00 37.96  ? 75  HIS B CA  1 
ATOM   3575 C  C   . HIS B 1 73  ? 50.958 126.522 -130.094 1.00 35.13  ? 75  HIS B C   1 
ATOM   3576 O  O   . HIS B 1 73  ? 51.654 127.454 -130.404 1.00 36.01  ? 75  HIS B O   1 
ATOM   3577 C  CB  . HIS B 1 73  ? 49.146 126.754 -128.374 1.00 37.77  ? 75  HIS B CB  1 
ATOM   3578 C  CG  . HIS B 1 73  ? 50.069 127.621 -127.619 1.00 38.16  ? 75  HIS B CG  1 
ATOM   3579 N  ND1 . HIS B 1 73  ? 50.011 128.988 -127.734 1.00 41.81  ? 75  HIS B ND1 1 
ATOM   3580 C  CD2 . HIS B 1 73  ? 51.085 127.332 -126.784 1.00 37.54  ? 75  HIS B CD2 1 
ATOM   3581 C  CE1 . HIS B 1 73  ? 50.951 129.512 -126.960 1.00 40.39  ? 75  HIS B CE1 1 
ATOM   3582 N  NE2 . HIS B 1 73  ? 51.631 128.511 -126.371 1.00 38.19  ? 75  HIS B NE2 1 
ATOM   3583 N  N   . PHE B 1 74  ? 51.439 125.306 -129.872 1.00 33.06  ? 76  PHE B N   1 
ATOM   3584 C  CA  . PHE B 1 74  ? 52.886 124.988 -129.887 1.00 32.41  ? 76  PHE B CA  1 
ATOM   3585 C  C   . PHE B 1 74  ? 53.392 124.790 -131.329 1.00 32.63  ? 76  PHE B C   1 
ATOM   3586 O  O   . PHE B 1 74  ? 54.604 124.849 -131.521 1.00 32.60  ? 76  PHE B O   1 
ATOM   3587 C  CB  . PHE B 1 74  ? 53.187 123.759 -129.012 1.00 31.47  ? 76  PHE B CB  1 
ATOM   3588 C  CG  . PHE B 1 74  ? 53.095 123.986 -127.524 1.00 30.97  ? 76  PHE B CG  1 
ATOM   3589 C  CD1 . PHE B 1 74  ? 53.936 124.886 -126.888 1.00 30.13  ? 76  PHE B CD1 1 
ATOM   3590 C  CD2 . PHE B 1 74  ? 52.179 123.278 -126.746 1.00 30.66  ? 76  PHE B CD2 1 
ATOM   3591 C  CE1 . PHE B 1 74  ? 53.816 125.123 -125.524 1.00 29.82  ? 76  PHE B CE1 1 
ATOM   3592 C  CE2 . PHE B 1 74  ? 52.081 123.501 -125.379 1.00 30.41  ? 76  PHE B CE2 1 
ATOM   3593 C  CZ  . PHE B 1 74  ? 52.894 124.429 -124.770 1.00 29.26  ? 76  PHE B CZ  1 
ATOM   3594 N  N   . GLY B 1 75  ? 52.528 124.546 -132.324 1.00 33.50  ? 77  GLY B N   1 
ATOM   3595 C  CA  . GLY B 1 75  ? 52.969 124.275 -133.711 1.00 33.50  ? 77  GLY B CA  1 
ATOM   3596 C  C   . GLY B 1 75  ? 53.522 122.859 -133.866 1.00 33.29  ? 77  GLY B C   1 
ATOM   3597 O  O   . GLY B 1 75  ? 53.202 121.971 -133.050 1.00 34.04  ? 77  GLY B O   1 
ATOM   3598 N  N   . ASN B 1 76  ? 54.340 122.624 -134.879 1.00 33.74  ? 78  ASN B N   1 
ATOM   3599 C  CA  . ASN B 1 76  ? 54.706 121.258 -135.326 1.00 33.44  ? 78  ASN B CA  1 
ATOM   3600 C  C   . ASN B 1 76  ? 55.468 120.554 -134.203 1.00 31.03  ? 78  ASN B C   1 
ATOM   3601 O  O   . ASN B 1 76  ? 56.381 121.178 -133.614 1.00 30.82  ? 78  ASN B O   1 
ATOM   3602 C  CB  . ASN B 1 76  ? 55.524 121.288 -136.620 1.00 35.17  ? 78  ASN B CB  1 
ATOM   3603 C  CG  . ASN B 1 76  ? 56.027 119.918 -137.035 1.00 36.30  ? 78  ASN B CG  1 
ATOM   3604 O  OD1 . ASN B 1 76  ? 57.154 119.509 -136.705 1.00 35.00  ? 78  ASN B OD1 1 
ATOM   3605 N  ND2 . ASN B 1 76  ? 55.202 119.212 -137.795 1.00 38.38  ? 78  ASN B ND2 1 
ATOM   3606 N  N   . ALA B 1 77  ? 55.116 119.292 -133.955 1.00 29.71  ? 79  ALA B N   1 
ATOM   3607 C  CA  . ALA B 1 77  ? 55.585 118.455 -132.824 1.00 28.53  ? 79  ALA B CA  1 
ATOM   3608 C  C   . ALA B 1 77  ? 57.061 118.176 -132.998 1.00 27.78  ? 79  ALA B C   1 
ATOM   3609 O  O   . ALA B 1 77  ? 57.812 118.371 -132.073 1.00 26.25  ? 79  ALA B O   1 
ATOM   3610 C  CB  . ALA B 1 77  ? 54.825 117.162 -132.799 1.00 29.14  ? 79  ALA B CB  1 
ATOM   3611 N  N   . SER B 1 78  ? 57.454 117.764 -134.203 1.00 27.85  ? 80  SER B N   1 
ATOM   3612 C  CA  . SER B 1 78  ? 58.843 117.346 -134.515 1.00 27.71  ? 80  SER B CA  1 
ATOM   3613 C  C   . SER B 1 78  ? 59.756 118.570 -134.438 1.00 27.81  ? 80  SER B C   1 
ATOM   3614 O  O   . SER B 1 78  ? 60.911 118.389 -134.009 1.00 28.27  ? 80  SER B O   1 
ATOM   3615 C  CB  . SER B 1 78  ? 58.939 116.640 -135.887 1.00 29.12  ? 80  SER B CB  1 
ATOM   3616 O  OG  . SER B 1 78  ? 60.093 115.798 -135.940 1.00 28.37  ? 80  SER B OG  1 
ATOM   3617 N  N   . ASP B 1 79  ? 59.261 119.740 -134.861 1.00 29.13  ? 81  ASP B N   1 
ATOM   3618 C  CA  . ASP B 1 79  ? 59.992 121.038 -134.829 1.00 30.67  ? 81  ASP B CA  1 
ATOM   3619 C  C   . ASP B 1 79  ? 60.180 121.446 -133.362 1.00 29.80  ? 81  ASP B C   1 
ATOM   3620 O  O   . ASP B 1 79  ? 61.237 121.996 -133.003 1.00 29.78  ? 81  ASP B O   1 
ATOM   3621 C  CB  . ASP B 1 79  ? 59.238 122.180 -135.520 1.00 32.57  ? 81  ASP B CB  1 
ATOM   3622 C  CG  . ASP B 1 79  ? 59.137 122.142 -137.040 1.00 36.02  ? 81  ASP B CG  1 
ATOM   3623 O  OD1 . ASP B 1 79  ? 59.892 121.375 -137.677 1.00 38.97  ? 81  ASP B OD1 1 
ATOM   3624 O  OD2 . ASP B 1 79  ? 58.313 122.903 -137.598 1.00 37.83  ? 81  ASP B OD2 1 
ATOM   3625 N  N   . LYS B 1 80  ? 59.193 121.189 -132.514 1.00 30.23  ? 82  LYS B N   1 
ATOM   3626 C  CA  . LYS B 1 80  ? 59.314 121.563 -131.075 1.00 28.59  ? 82  LYS B CA  1 
ATOM   3627 C  C   . LYS B 1 80  ? 60.381 120.678 -130.425 1.00 29.00  ? 82  LYS B C   1 
ATOM   3628 O  O   . LYS B 1 80  ? 61.263 121.231 -129.723 1.00 29.73  ? 82  LYS B O   1 
ATOM   3629 C  CB  . LYS B 1 80  ? 57.982 121.461 -130.340 1.00 28.15  ? 82  LYS B CB  1 
ATOM   3630 C  CG  . LYS B 1 80  ? 58.046 121.872 -128.871 1.00 27.35  ? 82  LYS B CG  1 
ATOM   3631 C  CD  . LYS B 1 80  ? 58.476 123.281 -128.686 1.00 27.68  ? 82  LYS B CD  1 
ATOM   3632 C  CE  . LYS B 1 80  ? 58.230 123.729 -127.266 1.00 28.68  ? 82  LYS B CE  1 
ATOM   3633 N  NZ  . LYS B 1 80  ? 58.578 125.149 -127.019 1.00 29.66  ? 82  LYS B NZ  1 
ATOM   3634 N  N   . ALA B 1 81  ? 60.300 119.361 -130.634 1.00 29.26  ? 83  ALA B N   1 
ATOM   3635 C  CA  . ALA B 1 81  ? 61.335 118.384 -130.207 1.00 29.43  ? 83  ALA B CA  1 
ATOM   3636 C  C   . ALA B 1 81  ? 62.708 118.819 -130.726 1.00 30.69  ? 83  ALA B C   1 
ATOM   3637 O  O   . ALA B 1 81  ? 63.681 118.750 -129.970 1.00 31.75  ? 83  ALA B O   1 
ATOM   3638 C  CB  . ALA B 1 81  ? 61.019 117.002 -130.710 1.00 30.26  ? 83  ALA B CB  1 
ATOM   3639 N  N   . ALA B 1 82  ? 62.798 119.268 -131.974 1.00 32.27  ? 84  ALA B N   1 
ATOM   3640 C  CA  . ALA B 1 82  ? 64.093 119.670 -132.568 1.00 33.80  ? 84  ALA B CA  1 
ATOM   3641 C  C   . ALA B 1 82  ? 64.698 120.814 -131.742 1.00 34.05  ? 84  ALA B C   1 
ATOM   3642 O  O   . ALA B 1 82  ? 65.911 120.704 -131.447 1.00 35.25  ? 84  ALA B O   1 
ATOM   3643 C  CB  . ALA B 1 82  ? 63.962 120.036 -134.035 1.00 33.68  ? 84  ALA B CB  1 
ATOM   3644 N  N   . SER B 1 83  ? 63.923 121.859 -131.398 1.00 34.43  ? 85  SER B N   1 
ATOM   3645 C  CA  . SER B 1 83  ? 64.412 123.045 -130.626 1.00 36.12  ? 85  SER B CA  1 
ATOM   3646 C  C   . SER B 1 83  ? 64.858 122.635 -129.209 1.00 34.20  ? 85  SER B C   1 
ATOM   3647 O  O   . SER B 1 83  ? 65.538 123.429 -128.524 1.00 34.52  ? 85  SER B O   1 
ATOM   3648 C  CB  . SER B 1 83  ? 63.357 124.127 -130.566 1.00 37.30  ? 85  SER B CB  1 
ATOM   3649 O  OG  . SER B 1 83  ? 62.313 123.756 -129.665 1.00 37.71  ? 85  SER B OG  1 
ATOM   3650 N  N   . LEU B 1 84  ? 64.457 121.451 -128.755 1.00 33.22  ? 86  LEU B N   1 
ATOM   3651 C  CA  . LEU B 1 84  ? 64.750 120.969 -127.368 1.00 33.19  ? 86  LEU B CA  1 
ATOM   3652 C  C   . LEU B 1 84  ? 65.900 119.971 -127.409 1.00 34.28  ? 86  LEU B C   1 
ATOM   3653 O  O   . LEU B 1 84  ? 66.418 119.615 -126.350 1.00 35.69  ? 86  LEU B O   1 
ATOM   3654 C  CB  . LEU B 1 84  ? 63.505 120.311 -126.756 1.00 30.98  ? 86  LEU B CB  1 
ATOM   3655 C  CG  . LEU B 1 84  ? 62.343 121.253 -126.416 1.00 30.31  ? 86  LEU B CG  1 
ATOM   3656 C  CD1 . LEU B 1 84  ? 61.130 120.463 -125.938 1.00 29.92  ? 86  LEU B CD1 1 
ATOM   3657 C  CD2 . LEU B 1 84  ? 62.729 122.295 -125.374 1.00 30.24  ? 86  LEU B CD2 1 
ATOM   3658 N  N   . SER B 1 85  ? 66.297 119.535 -128.595 1.00 35.89  ? 87  SER B N   1 
ATOM   3659 C  CA  . SER B 1 85  ? 67.259 118.422 -128.738 1.00 36.80  ? 87  SER B CA  1 
ATOM   3660 C  C   . SER B 1 85  ? 68.622 118.862 -128.213 1.00 37.36  ? 87  SER B C   1 
ATOM   3661 O  O   . SER B 1 85  ? 69.047 119.978 -128.541 1.00 37.95  ? 87  SER B O   1 
ATOM   3662 C  CB  . SER B 1 85  ? 67.355 117.953 -130.143 1.00 37.95  ? 87  SER B CB  1 
ATOM   3663 O  OG  . SER B 1 85  ? 68.098 116.749 -130.162 1.00 40.28  ? 87  SER B OG  1 
ATOM   3664 N  N   . GLY B 1 86  ? 69.248 118.005 -127.404 1.00 38.85  ? 88  GLY B N   1 
ATOM   3665 C  CA  . GLY B 1 86  ? 70.550 118.226 -126.744 1.00 40.14  ? 88  GLY B CA  1 
ATOM   3666 C  C   . GLY B 1 86  ? 70.562 119.377 -125.745 1.00 41.71  ? 88  GLY B C   1 
ATOM   3667 O  O   . GLY B 1 86  ? 71.653 119.665 -125.277 1.00 41.76  ? 88  GLY B O   1 
ATOM   3668 N  N   . LYS B 1 87  ? 69.425 120.023 -125.423 1.00 43.58  ? 89  LYS B N   1 
ATOM   3669 C  CA  . LYS B 1 87  ? 69.337 121.012 -124.309 1.00 44.11  ? 89  LYS B CA  1 
ATOM   3670 C  C   . LYS B 1 87  ? 69.514 120.264 -122.997 1.00 44.55  ? 89  LYS B C   1 
ATOM   3671 O  O   . LYS B 1 87  ? 69.211 119.059 -122.957 1.00 42.99  ? 89  LYS B O   1 
ATOM   3672 C  CB  . LYS B 1 87  ? 68.000 121.753 -124.267 1.00 44.84  ? 89  LYS B CB  1 
ATOM   3673 C  CG  . LYS B 1 87  ? 67.725 122.622 -125.488 1.00 46.82  ? 89  LYS B CG  1 
ATOM   3674 C  CD  . LYS B 1 87  ? 68.591 123.845 -125.553 1.00 48.98  ? 89  LYS B CD  1 
ATOM   3675 C  CE  . LYS B 1 87  ? 68.302 124.679 -126.776 1.00 52.85  ? 89  LYS B CE  1 
ATOM   3676 N  NZ  . LYS B 1 87  ? 69.367 125.680 -126.999 1.00 55.88  ? 89  LYS B NZ  1 
ATOM   3677 N  N   . GLN B 1 88  ? 70.008 120.965 -121.980 1.00 45.71  ? 90  GLN B N   1 
ATOM   3678 C  CA  . GLN B 1 88  ? 70.281 120.390 -120.638 1.00 47.09  ? 90  GLN B CA  1 
ATOM   3679 C  C   . GLN B 1 88  ? 68.987 119.922 -119.978 1.00 42.17  ? 90  GLN B C   1 
ATOM   3680 O  O   . GLN B 1 88  ? 67.893 120.430 -120.279 1.00 39.48  ? 90  GLN B O   1 
ATOM   3681 C  CB  . GLN B 1 88  ? 71.009 121.421 -119.782 1.00 52.11  ? 90  GLN B CB  1 
ATOM   3682 C  CG  . GLN B 1 88  ? 72.392 121.755 -120.337 1.00 57.69  ? 90  GLN B CG  1 
ATOM   3683 C  CD  . GLN B 1 88  ? 73.401 120.678 -120.019 1.00 61.51  ? 90  GLN B CD  1 
ATOM   3684 O  OE1 . GLN B 1 88  ? 73.050 119.598 -119.523 1.00 64.37  ? 90  GLN B OE1 1 
ATOM   3685 N  NE2 . GLN B 1 88  ? 74.668 120.990 -120.254 1.00 63.54  ? 90  GLN B NE2 1 
ATOM   3686 N  N   . ASN B 1 89  ? 69.131 118.997 -119.054 1.00 43.25  ? 91  ASN B N   1 
ATOM   3687 C  CA  . ASN B 1 89  ? 67.985 118.375 -118.342 1.00 43.11  ? 91  ASN B CA  1 
ATOM   3688 C  C   . ASN B 1 89  ? 67.232 119.409 -117.475 1.00 41.76  ? 91  ASN B C   1 
ATOM   3689 O  O   . ASN B 1 89  ? 65.976 119.336 -117.370 1.00 41.58  ? 91  ASN B O   1 
ATOM   3690 C  CB  . ASN B 1 89  ? 68.467 117.113 -117.623 1.00 43.65  ? 91  ASN B CB  1 
ATOM   3691 C  CG  . ASN B 1 89  ? 68.732 115.959 -118.579 1.00 44.79  ? 91  ASN B CG  1 
ATOM   3692 O  OD1 . ASN B 1 89  ? 68.202 115.894 -119.694 1.00 46.59  ? 91  ASN B OD1 1 
ATOM   3693 N  ND2 . ASN B 1 89  ? 69.541 115.014 -118.152 1.00 46.23  ? 91  ASN B ND2 1 
ATOM   3694 N  N   . ASP B 1 90  ? 67.929 120.389 -116.930 1.00 41.26  ? 92  ASP B N   1 
ATOM   3695 C  CA  . ASP B 1 90  ? 67.302 121.418 -116.059 1.00 41.97  ? 92  ASP B CA  1 
ATOM   3696 C  C   . ASP B 1 90  ? 67.229 122.715 -116.878 1.00 39.59  ? 92  ASP B C   1 
ATOM   3697 O  O   . ASP B 1 90  ? 67.163 123.812 -116.271 1.00 40.07  ? 92  ASP B O   1 
ATOM   3698 C  CB  . ASP B 1 90  ? 68.102 121.564 -114.750 1.00 44.55  ? 92  ASP B CB  1 
ATOM   3699 C  CG  . ASP B 1 90  ? 69.573 121.985 -114.948 1.00 49.13  ? 92  ASP B CG  1 
ATOM   3700 O  OD1 . ASP B 1 90  ? 70.072 121.997 -116.121 1.00 51.31  ? 92  ASP B OD1 1 
ATOM   3701 O  OD2 . ASP B 1 90  ? 70.231 122.309 -113.942 1.00 52.95  ? 92  ASP B OD2 1 
ATOM   3702 N  N   . SER B 1 91  ? 67.324 122.629 -118.205 1.00 36.22  ? 93  SER B N   1 
ATOM   3703 C  CA  . SER B 1 91  ? 67.467 123.839 -119.038 1.00 35.18  ? 93  SER B CA  1 
ATOM   3704 C  C   . SER B 1 91  ? 66.194 124.667 -118.854 1.00 34.10  ? 93  SER B C   1 
ATOM   3705 O  O   . SER B 1 91  ? 65.168 124.094 -118.472 1.00 33.27  ? 93  SER B O   1 
ATOM   3706 C  CB  . SER B 1 91  ? 67.759 123.515 -120.490 1.00 35.97  ? 93  SER B CB  1 
ATOM   3707 O  OG  . SER B 1 91  ? 66.705 122.780 -121.099 1.00 34.63  ? 93  SER B OG  1 
ATOM   3708 N  N   . ALA B 1 92  ? 66.256 125.973 -119.097 1.00 34.45  ? 94  ALA B N   1 
ATOM   3709 C  CA  . ALA B 1 92  ? 65.096 126.883 -119.009 1.00 33.74  ? 94  ALA B CA  1 
ATOM   3710 C  C   . ALA B 1 92  ? 64.074 126.468 -120.066 1.00 32.01  ? 94  ALA B C   1 
ATOM   3711 O  O   . ALA B 1 92  ? 62.864 126.581 -119.770 1.00 31.36  ? 94  ALA B O   1 
ATOM   3712 C  CB  . ALA B 1 92  ? 65.525 128.310 -119.193 1.00 35.27  ? 94  ALA B CB  1 
ATOM   3713 N  N   . GLU B 1 93  ? 64.550 125.972 -121.215 1.00 31.75  ? 95  GLU B N   1 
ATOM   3714 C  CA  . GLU B 1 93  ? 63.699 125.573 -122.357 1.00 30.77  ? 95  GLU B CA  1 
ATOM   3715 C  C   . GLU B 1 93  ? 62.787 124.427 -121.918 1.00 29.02  ? 95  GLU B C   1 
ATOM   3716 O  O   . GLU B 1 93  ? 61.525 124.494 -122.146 1.00 26.92  ? 95  GLU B O   1 
ATOM   3717 C  CB  . GLU B 1 93  ? 64.533 125.149 -123.569 1.00 33.13  ? 95  GLU B CB  1 
ATOM   3718 C  CG  . GLU B 1 93  ? 65.343 126.267 -124.225 1.00 36.55  ? 95  GLU B CG  1 
ATOM   3719 C  CD  . GLU B 1 93  ? 66.706 126.614 -123.597 1.00 40.20  ? 95  GLU B CD  1 
ATOM   3720 O  OE1 . GLU B 1 93  ? 67.105 125.996 -122.555 1.00 39.69  ? 95  GLU B OE1 1 
ATOM   3721 O  OE2 . GLU B 1 93  ? 67.392 127.525 -124.142 1.00 43.83  ? 95  GLU B OE2 1 
ATOM   3722 N  N   . VAL B 1 94  ? 63.356 123.391 -121.316 1.00 29.27  ? 96  VAL B N   1 
ATOM   3723 C  CA  . VAL B 1 94  ? 62.517 122.233 -120.887 1.00 29.40  ? 96  VAL B CA  1 
ATOM   3724 C  C   . VAL B 1 94  ? 61.537 122.651 -119.787 1.00 28.43  ? 96  VAL B C   1 
ATOM   3725 O  O   . VAL B 1 94  ? 60.395 122.111 -119.785 1.00 28.32  ? 96  VAL B O   1 
ATOM   3726 C  CB  . VAL B 1 94  ? 63.342 121.018 -120.459 1.00 29.86  ? 96  VAL B CB  1 
ATOM   3727 C  CG1 . VAL B 1 94  ? 64.137 121.290 -119.207 1.00 32.79  ? 96  VAL B CG1 1 
ATOM   3728 C  CG2 . VAL B 1 94  ? 62.461 119.811 -120.255 1.00 28.80  ? 96  VAL B CG2 1 
ATOM   3729 N  N   . LYS B 1 95  ? 61.929 123.555 -118.880 1.00 29.14  ? 97  LYS B N   1 
ATOM   3730 C  CA  . LYS B 1 95  ? 61.057 123.979 -117.759 1.00 28.07  ? 97  LYS B CA  1 
ATOM   3731 C  C   . LYS B 1 95  ? 59.911 124.800 -118.302 1.00 26.67  ? 97  LYS B C   1 
ATOM   3732 O  O   . LYS B 1 95  ? 58.801 124.604 -117.812 1.00 26.84  ? 97  LYS B O   1 
ATOM   3733 C  CB  . LYS B 1 95  ? 61.779 124.838 -116.727 1.00 31.50  ? 97  LYS B CB  1 
ATOM   3734 C  CG  . LYS B 1 95  ? 62.907 124.113 -116.040 1.00 32.80  ? 97  LYS B CG  1 
ATOM   3735 C  CD  . LYS B 1 95  ? 63.463 124.871 -114.928 1.00 35.98  ? 97  LYS B CD  1 
ATOM   3736 C  CE  . LYS B 1 95  ? 64.168 123.920 -113.998 1.00 38.10  ? 97  LYS B CE  1 
ATOM   3737 N  NZ  . LYS B 1 95  ? 64.972 124.709 -113.044 1.00 41.73  ? 97  LYS B NZ  1 
ATOM   3738 N  N   . ALA B 1 96  ? 60.160 125.661 -119.285 1.00 25.38  ? 98  ALA B N   1 
ATOM   3739 C  CA  . ALA B 1 96  ? 59.095 126.517 -119.839 1.00 24.51  ? 98  ALA B CA  1 
ATOM   3740 C  C   . ALA B 1 96  ? 58.074 125.617 -120.534 1.00 23.90  ? 98  ALA B C   1 
ATOM   3741 O  O   . ALA B 1 96  ? 56.849 125.795 -120.321 1.00 23.77  ? 98  ALA B O   1 
ATOM   3742 C  CB  . ALA B 1 96  ? 59.675 127.499 -120.790 1.00 25.21  ? 98  ALA B CB  1 
ATOM   3743 N  N   . PHE B 1 97  ? 58.556 124.665 -121.334 1.00 22.49  ? 99  PHE B N   1 
ATOM   3744 C  CA  . PHE B 1 97  ? 57.672 123.697 -122.038 1.00 22.02  ? 99  PHE B CA  1 
ATOM   3745 C  C   . PHE B 1 97  ? 56.805 122.970 -121.003 1.00 20.62  ? 99  PHE B C   1 
ATOM   3746 O  O   . PHE B 1 97  ? 55.581 122.967 -121.169 1.00 21.03  ? 99  PHE B O   1 
ATOM   3747 C  CB  . PHE B 1 97  ? 58.471 122.785 -122.982 1.00 21.55  ? 99  PHE B CB  1 
ATOM   3748 C  CG  . PHE B 1 97  ? 57.638 121.947 -123.929 1.00 21.69  ? 99  PHE B CG  1 
ATOM   3749 C  CD1 . PHE B 1 97  ? 56.592 122.483 -124.664 1.00 21.57  ? 99  PHE B CD1 1 
ATOM   3750 C  CD2 . PHE B 1 97  ? 57.919 120.605 -124.112 1.00 21.46  ? 99  PHE B CD2 1 
ATOM   3751 C  CE1 . PHE B 1 97  ? 55.833 121.694 -125.506 1.00 21.74  ? 99  PHE B CE1 1 
ATOM   3752 C  CE2 . PHE B 1 97  ? 57.158 119.825 -124.964 1.00 21.98  ? 99  PHE B CE2 1 
ATOM   3753 C  CZ  . PHE B 1 97  ? 56.122 120.370 -125.670 1.00 21.74  ? 99  PHE B CZ  1 
ATOM   3754 N  N   . ALA B 1 98  ? 57.392 122.354 -119.989 1.00 19.96  ? 100 ALA B N   1 
ATOM   3755 C  CA  . ALA B 1 98  ? 56.608 121.608 -118.973 1.00 20.20  ? 100 ALA B CA  1 
ATOM   3756 C  C   . ALA B 1 98  ? 55.525 122.504 -118.341 1.00 20.49  ? 100 ALA B C   1 
ATOM   3757 O  O   . ALA B 1 98  ? 54.384 122.041 -118.202 1.00 20.90  ? 100 ALA B O   1 
ATOM   3758 C  CB  . ALA B 1 98  ? 57.506 121.012 -117.919 1.00 19.96  ? 100 ALA B CB  1 
ATOM   3759 N  N   . GLN B 1 99  ? 55.852 123.744 -117.967 1.00 21.08  ? 101 GLN B N   1 
ATOM   3760 C  CA  . GLN B 1 99  ? 54.907 124.683 -117.305 1.00 21.66  ? 101 GLN B CA  1 
ATOM   3761 C  C   . GLN B 1 99  ? 53.825 125.073 -118.290 1.00 22.07  ? 101 GLN B C   1 
ATOM   3762 O  O   . GLN B 1 99  ? 52.663 124.976 -117.916 1.00 22.17  ? 101 GLN B O   1 
ATOM   3763 C  CB  . GLN B 1 99  ? 55.590 125.943 -116.788 1.00 22.73  ? 101 GLN B CB  1 
ATOM   3764 C  CG  . GLN B 1 99  ? 56.333 125.744 -115.460 1.00 23.85  ? 101 GLN B CG  1 
ATOM   3765 C  CD  . GLN B 1 99  ? 55.470 125.164 -114.346 1.00 24.34  ? 101 GLN B CD  1 
ATOM   3766 O  OE1 . GLN B 1 99  ? 54.403 125.694 -113.991 1.00 24.81  ? 101 GLN B OE1 1 
ATOM   3767 N  NE2 . GLN B 1 99  ? 55.902 124.024 -113.819 1.00 23.53  ? 101 GLN B NE2 1 
ATOM   3768 N  N   . GLU B 1 100 ? 54.192 125.413 -119.524 1.00 23.03  ? 102 GLU B N   1 
ATOM   3769 C  CA  . GLU B 1 100 ? 53.253 125.949 -120.542 1.00 24.17  ? 102 GLU B CA  1 
ATOM   3770 C  C   . GLU B 1 100 ? 52.372 124.819 -121.075 1.00 24.13  ? 102 GLU B C   1 
ATOM   3771 O  O   . GLU B 1 100 ? 51.279 125.108 -121.545 1.00 24.66  ? 102 GLU B O   1 
ATOM   3772 C  CB  . GLU B 1 100 ? 54.038 126.660 -121.644 1.00 25.27  ? 102 GLU B CB  1 
ATOM   3773 C  CG  . GLU B 1 100 ? 54.485 128.053 -121.236 1.00 26.65  ? 102 GLU B CG  1 
ATOM   3774 C  CD  . GLU B 1 100 ? 53.307 128.954 -120.857 1.00 28.94  ? 102 GLU B CD  1 
ATOM   3775 O  OE1 . GLU B 1 100 ? 52.462 129.246 -121.748 1.00 32.29  ? 102 GLU B OE1 1 
ATOM   3776 O  OE2 . GLU B 1 100 ? 53.180 129.337 -119.672 1.00 29.91  ? 102 GLU B OE2 1 
ATOM   3777 N  N   . LEU B 1 101 ? 52.835 123.576 -120.998 1.00 23.70  ? 103 LEU B N   1 
ATOM   3778 C  CA  . LEU B 1 101 ? 52.054 122.395 -121.443 1.00 24.46  ? 103 LEU B CA  1 
ATOM   3779 C  C   . LEU B 1 101 ? 50.813 122.243 -120.595 1.00 25.81  ? 103 LEU B C   1 
ATOM   3780 O  O   . LEU B 1 101 ? 49.778 121.936 -121.168 1.00 27.10  ? 103 LEU B O   1 
ATOM   3781 C  CB  . LEU B 1 101 ? 52.873 121.106 -121.334 1.00 23.86  ? 103 LEU B CB  1 
ATOM   3782 C  CG  . LEU B 1 101 ? 53.581 120.625 -122.600 1.00 23.45  ? 103 LEU B CG  1 
ATOM   3783 C  CD1 . LEU B 1 101 ? 54.536 119.488 -122.260 1.00 22.72  ? 103 LEU B CD1 1 
ATOM   3784 C  CD2 . LEU B 1 101 ? 52.573 120.213 -123.693 1.00 24.28  ? 103 LEU B CD2 1 
ATOM   3785 N  N   . ASN B 1 102 ? 50.958 122.442 -119.278 1.00 28.05  ? 104 ASN B N   1 
ATOM   3786 C  CA  . ASN B 1 102 ? 49.991 122.006 -118.234 1.00 28.63  ? 104 ASN B CA  1 
ATOM   3787 C  C   . ASN B 1 102 ? 48.589 122.470 -118.599 1.00 30.66  ? 104 ASN B C   1 
ATOM   3788 O  O   . ASN B 1 102 ? 47.658 121.688 -118.381 1.00 31.49  ? 104 ASN B O   1 
ATOM   3789 C  CB  . ASN B 1 102 ? 50.324 122.524 -116.836 1.00 28.16  ? 104 ASN B CB  1 
ATOM   3790 C  CG  . ASN B 1 102 ? 49.369 121.981 -115.794 1.00 27.76  ? 104 ASN B CG  1 
ATOM   3791 O  OD1 . ASN B 1 102 ? 49.105 120.778 -115.743 1.00 27.11  ? 104 ASN B OD1 1 
ATOM   3792 N  ND2 . ASN B 1 102 ? 48.850 122.863 -114.966 1.00 26.88  ? 104 ASN B ND2 1 
ATOM   3793 N  N   . GLN B 1 103 ? 48.459 123.682 -119.131 1.00 31.59  ? 105 GLN B N   1 
ATOM   3794 C  CA  . GLN B 1 103 ? 47.144 124.243 -119.490 1.00 33.61  ? 105 GLN B CA  1 
ATOM   3795 C  C   . GLN B 1 103 ? 46.555 123.536 -120.711 1.00 32.74  ? 105 GLN B C   1 
ATOM   3796 O  O   . GLN B 1 103 ? 45.428 123.806 -121.010 1.00 33.21  ? 105 GLN B O   1 
ATOM   3797 C  CB  . GLN B 1 103 ? 47.269 125.744 -119.713 1.00 36.84  ? 105 GLN B CB  1 
ATOM   3798 C  CG  . GLN B 1 103 ? 48.033 126.131 -120.968 1.00 38.27  ? 105 GLN B CG  1 
ATOM   3799 C  CD  . GLN B 1 103 ? 48.655 127.502 -120.812 1.00 40.75  ? 105 GLN B CD  1 
ATOM   3800 O  OE1 . GLN B 1 103 ? 48.072 128.384 -120.195 1.00 44.70  ? 105 GLN B OE1 1 
ATOM   3801 N  NE2 . GLN B 1 103 ? 49.867 127.685 -121.318 1.00 40.63  ? 105 GLN B NE2 1 
ATOM   3802 N  N   . TYR B 1 104 ? 47.264 122.662 -121.411 1.00 32.07  ? 106 TYR B N   1 
ATOM   3803 C  CA  . TYR B 1 104 ? 46.719 122.024 -122.635 1.00 32.37  ? 106 TYR B CA  1 
ATOM   3804 C  C   . TYR B 1 104 ? 46.636 120.513 -122.492 1.00 32.13  ? 106 TYR B C   1 
ATOM   3805 O  O   . TYR B 1 104 ? 46.479 119.841 -123.497 1.00 32.09  ? 106 TYR B O   1 
ATOM   3806 C  CB  . TYR B 1 104 ? 47.581 122.362 -123.850 1.00 31.96  ? 106 TYR B CB  1 
ATOM   3807 C  CG  . TYR B 1 104 ? 47.588 123.826 -124.187 1.00 32.26  ? 106 TYR B CG  1 
ATOM   3808 C  CD1 . TYR B 1 104 ? 46.460 124.431 -124.710 1.00 33.57  ? 106 TYR B CD1 1 
ATOM   3809 C  CD2 . TYR B 1 104 ? 48.724 124.599 -124.011 1.00 31.67  ? 106 TYR B CD2 1 
ATOM   3810 C  CE1 . TYR B 1 104 ? 46.471 125.772 -125.059 1.00 34.52  ? 106 TYR B CE1 1 
ATOM   3811 C  CE2 . TYR B 1 104 ? 48.743 125.949 -124.323 1.00 32.68  ? 106 TYR B CE2 1 
ATOM   3812 C  CZ  . TYR B 1 104 ? 47.608 126.541 -124.842 1.00 34.36  ? 106 TYR B CZ  1 
ATOM   3813 O  OH  . TYR B 1 104 ? 47.655 127.867 -125.166 1.00 35.30  ? 106 TYR B OH  1 
ATOM   3814 N  N   . LEU B 1 105 ? 46.765 119.992 -121.294 1.00 32.80  ? 107 LEU B N   1 
ATOM   3815 C  CA  . LEU B 1 105 ? 46.795 118.525 -121.107 1.00 35.22  ? 107 LEU B CA  1 
ATOM   3816 C  C   . LEU B 1 105 ? 45.374 117.962 -121.307 1.00 40.18  ? 107 LEU B C   1 
ATOM   3817 O  O   . LEU B 1 105 ? 44.374 118.684 -121.038 1.00 43.08  ? 107 LEU B O   1 
ATOM   3818 C  CB  . LEU B 1 105 ? 47.330 118.184 -119.707 1.00 33.83  ? 107 LEU B CB  1 
ATOM   3819 C  CG  . LEU B 1 105 ? 48.783 118.541 -119.411 1.00 31.58  ? 107 LEU B CG  1 
ATOM   3820 C  CD1 . LEU B 1 105 ? 49.143 118.044 -118.039 1.00 30.75  ? 107 LEU B CD1 1 
ATOM   3821 C  CD2 . LEU B 1 105 ? 49.723 117.950 -120.436 1.00 31.33  ? 107 LEU B CD2 1 
ATOM   3822 N  N   . SER B 1 106 ? 45.293 116.691 -121.699 1.00 42.32  ? 108 SER B N   1 
ATOM   3823 C  CA  . SER B 1 106 ? 44.044 115.934 -121.917 1.00 45.20  ? 108 SER B CA  1 
ATOM   3824 C  C   . SER B 1 106 ? 44.124 114.598 -121.189 1.00 48.48  ? 108 SER B C   1 
ATOM   3825 O  O   . SER B 1 106 ? 45.218 114.026 -121.170 1.00 49.81  ? 108 SER B O   1 
ATOM   3826 C  CB  . SER B 1 106 ? 43.851 115.736 -123.372 1.00 47.09  ? 108 SER B CB  1 
ATOM   3827 O  OG  . SER B 1 106 ? 43.085 114.574 -123.587 1.00 48.84  ? 108 SER B OG  1 
ATOM   3828 N  N   . SER B 1 107 ? 42.993 114.092 -120.684 1.00 53.91  ? 109 SER B N   1 
ATOM   3829 C  CA  . SER B 1 107 ? 42.845 112.728 -120.096 1.00 56.37  ? 109 SER B CA  1 
ATOM   3830 C  C   . SER B 1 107 ? 42.617 111.661 -121.182 1.00 58.60  ? 109 SER B C   1 
ATOM   3831 O  O   . SER B 1 107 ? 42.381 110.473 -120.823 1.00 56.24  ? 109 SER B O   1 
ATOM   3832 C  CB  . SER B 1 107 ? 41.769 112.733 -119.079 1.00 58.53  ? 109 SER B CB  1 
ATOM   3833 O  OG  . SER B 1 107 ? 42.216 113.508 -117.977 1.00 57.86  ? 109 SER B OG  1 
ATOM   3834 N  N   . ALA B 1 108 ? 42.739 112.066 -122.458 1.00 59.90  ? 110 ALA B N   1 
ATOM   3835 C  CA  . ALA B 1 108 ? 42.669 111.173 -123.639 1.00 64.20  ? 110 ALA B CA  1 
ATOM   3836 C  C   . ALA B 1 108 ? 43.944 110.334 -123.694 1.00 67.39  ? 110 ALA B C   1 
ATOM   3837 O  O   . ALA B 1 108 ? 43.844 109.184 -124.172 1.00 74.87  ? 110 ALA B O   1 
ATOM   3838 C  CB  . ALA B 1 108 ? 42.460 111.935 -124.929 1.00 62.35  ? 110 ALA B CB  1 
ATOM   3839 N  N   . GLY B 1 109 ? 45.079 110.900 -123.245 1.00 66.07  ? 111 GLY B N   1 
ATOM   3840 C  CA  . GLY B 1 109 ? 46.398 110.235 -123.173 1.00 61.38  ? 111 GLY B CA  1 
ATOM   3841 C  C   . GLY B 1 109 ? 47.032 110.384 -121.797 1.00 57.81  ? 111 GLY B C   1 
ATOM   3842 O  O   . GLY B 1 109 ? 48.201 110.778 -121.751 1.00 50.02  ? 111 GLY B O   1 
ATOM   3843 N  N   . VAL B 1 110 ? 46.288 110.045 -120.727 1.00 60.00  ? 112 VAL B N   1 
ATOM   3844 C  CA  . VAL B 1 110 ? 46.755 110.025 -119.298 1.00 58.78  ? 112 VAL B CA  1 
ATOM   3845 C  C   . VAL B 1 110 ? 46.797 108.588 -118.770 1.00 57.68  ? 112 VAL B C   1 
ATOM   3846 O  O   . VAL B 1 110 ? 45.764 107.896 -118.901 1.00 59.35  ? 112 VAL B O   1 
ATOM   3847 C  CB  . VAL B 1 110 ? 45.870 110.870 -118.361 1.00 58.76  ? 112 VAL B CB  1 
ATOM   3848 C  CG1 . VAL B 1 110 ? 44.500 110.233 -118.117 1.00 60.34  ? 112 VAL B CG1 1 
ATOM   3849 C  CG2 . VAL B 1 110 ? 46.581 111.144 -117.043 1.00 57.44  ? 112 VAL B CG2 1 
ATOM   3850 N  N   . THR B 1 111 ? 47.931 108.198 -118.176 1.00 52.78  ? 113 THR B N   1 
ATOM   3851 C  CA  . THR B 1 111 ? 48.063 107.049 -117.246 1.00 51.85  ? 113 THR B CA  1 
ATOM   3852 C  C   . THR B 1 111 ? 48.192 107.596 -115.821 1.00 49.94  ? 113 THR B C   1 
ATOM   3853 O  O   . THR B 1 111 ? 48.931 108.585 -115.647 1.00 47.59  ? 113 THR B O   1 
ATOM   3854 C  CB  . THR B 1 111 ? 49.274 106.178 -117.589 1.00 50.61  ? 113 THR B CB  1 
ATOM   3855 O  OG1 . THR B 1 111 ? 49.157 105.928 -118.982 1.00 51.34  ? 113 THR B OG1 1 
ATOM   3856 C  CG2 . THR B 1 111 ? 49.326 104.889 -116.796 1.00 51.46  ? 113 THR B CG2 1 
ATOM   3857 N  N   . THR B 1 112 ? 47.552 106.954 -114.842 1.00 49.41  ? 114 THR B N   1 
ATOM   3858 C  CA  . THR B 1 112 ? 47.597 107.385 -113.424 1.00 47.07  ? 114 THR B CA  1 
ATOM   3859 C  C   . THR B 1 112 ? 48.117 106.250 -112.565 1.00 47.70  ? 114 THR B C   1 
ATOM   3860 O  O   . THR B 1 112 ? 47.644 105.132 -112.727 1.00 49.86  ? 114 THR B O   1 
ATOM   3861 C  CB  . THR B 1 112 ? 46.234 107.859 -112.945 1.00 46.21  ? 114 THR B CB  1 
ATOM   3862 O  OG1 . THR B 1 112 ? 45.836 108.918 -113.806 1.00 45.29  ? 114 THR B OG1 1 
ATOM   3863 C  CG2 . THR B 1 112 ? 46.273 108.377 -111.533 1.00 46.06  ? 114 THR B CG2 1 
ATOM   3864 N  N   . VAL B 1 113 ? 49.050 106.557 -111.677 1.00 47.08  ? 115 VAL B N   1 
ATOM   3865 C  CA  . VAL B 1 113 ? 49.726 105.536 -110.840 1.00 48.28  ? 115 VAL B CA  1 
ATOM   3866 C  C   . VAL B 1 113 ? 49.647 105.947 -109.374 1.00 49.59  ? 115 VAL B C   1 
ATOM   3867 O  O   . VAL B 1 113 ? 49.827 107.119 -109.071 1.00 48.48  ? 115 VAL B O   1 
ATOM   3868 C  CB  . VAL B 1 113 ? 51.169 105.363 -111.330 1.00 47.58  ? 115 VAL B CB  1 
ATOM   3869 C  CG1 . VAL B 1 113 ? 52.076 104.788 -110.266 1.00 48.59  ? 115 VAL B CG1 1 
ATOM   3870 C  CG2 . VAL B 1 113 ? 51.209 104.534 -112.596 1.00 48.74  ? 115 VAL B CG2 1 
ATOM   3871 N  N   . GLN B 1 114 ? 49.443 104.972 -108.499 1.00 53.51  ? 116 GLN B N   1 
ATOM   3872 C  CA  . GLN B 1 114 ? 49.429 105.145 -107.030 1.00 55.61  ? 116 GLN B CA  1 
ATOM   3873 C  C   . GLN B 1 114 ? 50.868 105.059 -106.521 1.00 53.75  ? 116 GLN B C   1 
ATOM   3874 O  O   . GLN B 1 114 ? 51.549 104.088 -106.846 1.00 53.13  ? 116 GLN B O   1 
ATOM   3875 C  CB  . GLN B 1 114 ? 48.554 104.042 -106.448 1.00 61.25  ? 116 GLN B CB  1 
ATOM   3876 C  CG  . GLN B 1 114 ? 47.937 104.337 -105.101 1.00 64.07  ? 116 GLN B CG  1 
ATOM   3877 C  CD  . GLN B 1 114 ? 46.882 103.286 -104.824 1.00 71.32  ? 116 GLN B CD  1 
ATOM   3878 O  OE1 . GLN B 1 114 ? 45.846 103.236 -105.485 1.00 76.52  ? 116 GLN B OE1 1 
ATOM   3879 N  NE2 . GLN B 1 114 ? 47.141 102.405 -103.868 1.00 71.93  ? 116 GLN B NE2 1 
ATOM   3880 N  N   . SER B 1 115 ? 51.297 106.018 -105.715 1.00 52.71  ? 117 SER B N   1 
ATOM   3881 C  CA  . SER B 1 115 ? 52.706 106.140 -105.269 1.00 53.92  ? 117 SER B CA  1 
ATOM   3882 C  C   . SER B 1 115 ? 53.055 105.096 -104.205 1.00 56.07  ? 117 SER B C   1 
ATOM   3883 O  O   . SER B 1 115 ? 52.340 104.971 -103.236 1.00 60.72  ? 117 SER B O   1 
ATOM   3884 C  CB  . SER B 1 115 ? 53.007 107.523 -104.773 1.00 52.82  ? 117 SER B CB  1 
ATOM   3885 O  OG  . SER B 1 115 ? 52.303 107.820 -103.575 1.00 51.34  ? 117 SER B OG  1 
ATOM   3886 N  N   . GLN B 1 116 ? 54.168 104.404 -104.392 1.00 59.19  ? 118 GLN B N   1 
ATOM   3887 C  CA  . GLN B 1 116 ? 54.752 103.462 -103.409 1.00 62.06  ? 118 GLN B CA  1 
ATOM   3888 C  C   . GLN B 1 116 ? 55.744 104.231 -102.533 1.00 60.85  ? 118 GLN B C   1 
ATOM   3889 O  O   . GLN B 1 116 ? 56.278 105.289 -102.952 1.00 56.53  ? 118 GLN B O   1 
ATOM   3890 C  CB  . GLN B 1 116 ? 55.421 102.270 -104.111 1.00 64.72  ? 118 GLN B CB  1 
ATOM   3891 C  CG  . GLN B 1 116 ? 54.521 101.053 -104.297 1.00 67.08  ? 118 GLN B CG  1 
ATOM   3892 C  CD  . GLN B 1 116 ? 53.215 101.398 -104.970 1.00 67.71  ? 118 GLN B CD  1 
ATOM   3893 O  OE1 . GLN B 1 116 ? 52.143 101.324 -104.376 1.00 70.23  ? 118 GLN B OE1 1 
ATOM   3894 N  NE2 . GLN B 1 116 ? 53.291 101.784 -106.229 1.00 68.27  ? 118 GLN B NE2 1 
ATOM   3895 N  N   . GLN B 1 117 ? 55.982 103.695 -101.345 1.00 62.05  ? 119 GLN B N   1 
ATOM   3896 C  CA  . GLN B 1 117 ? 56.997 104.235 -100.420 1.00 62.31  ? 119 GLN B CA  1 
ATOM   3897 C  C   . GLN B 1 117 ? 58.384 103.898 -100.974 1.00 61.40  ? 119 GLN B C   1 
ATOM   3898 O  O   . GLN B 1 117 ? 58.741 102.710 -100.961 1.00 64.72  ? 119 GLN B O   1 
ATOM   3899 C  CB  . GLN B 1 117 ? 56.792 103.655 -99.024  1.00 64.64  ? 119 GLN B CB  1 
ATOM   3900 C  CG  . GLN B 1 117 ? 57.739 104.257 -98.002  1.00 64.89  ? 119 GLN B CG  1 
ATOM   3901 C  CD  . GLN B 1 117 ? 57.624 105.763 -97.978  1.00 63.76  ? 119 GLN B CD  1 
ATOM   3902 O  OE1 . GLN B 1 117 ? 56.530 106.318 -97.824  1.00 65.66  ? 119 GLN B OE1 1 
ATOM   3903 N  NE2 . GLN B 1 117 ? 58.760 106.432 -98.106  1.00 59.70  ? 119 GLN B NE2 1 
ATOM   3904 N  N   . GLY B 1 118 ? 59.126 104.904 -101.440 1.00 57.94  ? 120 GLY B N   1 
ATOM   3905 C  CA  . GLY B 1 118 ? 60.499 104.741 -101.960 1.00 56.33  ? 120 GLY B CA  1 
ATOM   3906 C  C   . GLY B 1 118 ? 60.573 104.953 -103.462 1.00 54.80  ? 120 GLY B C   1 
ATOM   3907 O  O   . GLY B 1 118 ? 61.162 105.962 -103.878 1.00 52.40  ? 120 GLY B O   1 
ATOM   3908 N  N   . THR B 1 119 ? 60.008 104.032 -104.253 1.00 54.63  ? 121 THR B N   1 
ATOM   3909 C  CA  . THR B 1 119 ? 60.071 104.078 -105.730 1.00 53.38  ? 121 THR B CA  1 
ATOM   3910 C  C   . THR B 1 119 ? 58.750 103.644 -106.362 1.00 54.08  ? 121 THR B C   1 
ATOM   3911 O  O   . THR B 1 119 ? 58.293 102.538 -106.106 1.00 54.98  ? 121 THR B O   1 
ATOM   3912 C  CB  . THR B 1 119 ? 61.237 103.250 -106.268 1.00 53.76  ? 121 THR B CB  1 
ATOM   3913 O  OG1 . THR B 1 119 ? 62.419 103.853 -105.744 1.00 53.23  ? 121 THR B OG1 1 
ATOM   3914 C  CG2 . THR B 1 119 ? 61.286 103.238 -107.780 1.00 52.78  ? 121 THR B CG2 1 
ATOM   3915 N  N   . THR B 1 120 ? 58.225 104.487 -107.245 1.00 54.62  ? 122 THR B N   1 
ATOM   3916 C  CA  . THR B 1 120 ? 56.922 104.295 -107.918 1.00 54.30  ? 122 THR B CA  1 
ATOM   3917 C  C   . THR B 1 120 ? 57.156 103.870 -109.371 1.00 55.32  ? 122 THR B C   1 
ATOM   3918 O  O   . THR B 1 120 ? 57.730 104.636 -110.164 1.00 54.39  ? 122 THR B O   1 
ATOM   3919 C  CB  . THR B 1 120 ? 56.083 105.568 -107.828 1.00 52.22  ? 122 THR B CB  1 
ATOM   3920 O  OG1 . THR B 1 120 ? 56.137 106.071 -106.492 1.00 49.84  ? 122 THR B OG1 1 
ATOM   3921 C  CG2 . THR B 1 120 ? 54.658 105.304 -108.259 1.00 53.42  ? 122 THR B CG2 1 
ATOM   3922 N  N   . THR B 1 121 ? 56.707 102.680 -109.721 1.00 57.39  ? 123 THR B N   1 
ATOM   3923 C  CA  . THR B 1 121 ? 57.028 102.077 -111.031 1.00 58.78  ? 123 THR B CA  1 
ATOM   3924 C  C   . THR B 1 121 ? 55.877 102.377 -111.983 1.00 57.71  ? 123 THR B C   1 
ATOM   3925 O  O   . THR B 1 121 ? 54.736 102.125 -111.622 1.00 57.72  ? 123 THR B O   1 
ATOM   3926 C  CB  . THR B 1 121 ? 57.354 100.592 -110.861 1.00 62.55  ? 123 THR B CB  1 
ATOM   3927 O  OG1 . THR B 1 121 ? 58.324 100.488 -109.816 1.00 64.31  ? 123 THR B OG1 1 
ATOM   3928 C  CG2 . THR B 1 121 ? 57.896 99.966  -112.124 1.00 62.93  ? 123 THR B CG2 1 
ATOM   3929 N  N   . ILE B 1 122 ? 56.192 102.894 -113.164 1.00 58.08  ? 124 ILE B N   1 
ATOM   3930 C  CA  . ILE B 1 122 ? 55.192 103.217 -114.222 1.00 57.91  ? 124 ILE B CA  1 
ATOM   3931 C  C   . ILE B 1 122 ? 55.528 102.361 -115.451 1.00 58.10  ? 124 ILE B C   1 
ATOM   3932 O  O   . ILE B 1 122 ? 56.435 102.728 -116.192 1.00 57.23  ? 124 ILE B O   1 
ATOM   3933 C  CB  . ILE B 1 122 ? 55.183 104.733 -114.522 1.00 56.08  ? 124 ILE B CB  1 
ATOM   3934 C  CG1 . ILE B 1 122 ? 55.158 105.598 -113.248 1.00 54.76  ? 124 ILE B CG1 1 
ATOM   3935 C  CG2 . ILE B 1 122 ? 54.026 105.051 -115.450 1.00 56.35  ? 124 ILE B CG2 1 
ATOM   3936 C  CD1 . ILE B 1 122 ? 55.607 107.051 -113.433 1.00 51.11  ? 124 ILE B CD1 1 
ATOM   3937 N  N   . SER B 1 123 ? 54.830 101.240 -115.627 1.00 60.25  ? 125 SER B N   1 
ATOM   3938 C  CA  . SER B 1 123 ? 55.058 100.243 -116.707 1.00 61.69  ? 125 SER B CA  1 
ATOM   3939 C  C   . SER B 1 123 ? 54.232 100.611 -117.939 1.00 62.27  ? 125 SER B C   1 
ATOM   3940 O  O   . SER B 1 123 ? 53.383 101.512 -117.835 1.00 64.28  ? 125 SER B O   1 
ATOM   3941 C  CB  . SER B 1 123 ? 54.719 98.849  -116.237 1.00 62.91  ? 125 SER B CB  1 
ATOM   3942 O  OG  . SER B 1 123 ? 55.702 98.376  -115.339 1.00 61.60  ? 125 SER B OG  1 
ATOM   3943 N  N   . GLY B 1 124 ? 54.467 99.928  -119.061 1.00 61.89  ? 126 GLY B N   1 
ATOM   3944 C  CA  . GLY B 1 124 ? 53.542 99.913  -120.206 1.00 60.70  ? 126 GLY B CA  1 
ATOM   3945 C  C   . GLY B 1 124 ? 53.543 101.217 -120.974 1.00 58.55  ? 126 GLY B C   1 
ATOM   3946 O  O   . GLY B 1 124 ? 52.583 101.453 -121.691 1.00 59.68  ? 126 GLY B O   1 
ATOM   3947 N  N   . LEU B 1 125 ? 54.585 102.034 -120.869 1.00 56.52  ? 127 LEU B N   1 
ATOM   3948 C  CA  . LEU B 1 125 ? 54.642 103.321 -121.608 1.00 55.87  ? 127 LEU B CA  1 
ATOM   3949 C  C   . LEU B 1 125 ? 55.081 103.062 -123.050 1.00 57.36  ? 127 LEU B C   1 
ATOM   3950 O  O   . LEU B 1 125 ? 56.273 102.687 -123.239 1.00 57.44  ? 127 LEU B O   1 
ATOM   3951 C  CB  . LEU B 1 125 ? 55.656 104.249 -120.936 1.00 54.60  ? 127 LEU B CB  1 
ATOM   3952 C  CG  . LEU B 1 125 ? 55.267 104.812 -119.572 1.00 53.11  ? 127 LEU B CG  1 
ATOM   3953 C  CD1 . LEU B 1 125 ? 56.295 105.857 -119.159 1.00 51.91  ? 127 LEU B CD1 1 
ATOM   3954 C  CD2 . LEU B 1 125 ? 53.855 105.385 -119.583 1.00 51.21  ? 127 LEU B CD2 1 
ATOM   3955 N  N   . LYS B 1 126 ? 54.195 103.300 -124.020 1.00 58.16  ? 128 LYS B N   1 
ATOM   3956 C  CA  . LYS B 1 126 ? 54.567 103.422 -125.458 1.00 59.31  ? 128 LYS B CA  1 
ATOM   3957 C  C   . LYS B 1 126 ? 55.745 104.389 -125.582 1.00 54.87  ? 128 LYS B C   1 
ATOM   3958 O  O   . LYS B 1 126 ? 55.951 105.252 -124.735 1.00 53.47  ? 128 LYS B O   1 
ATOM   3959 C  CB  . LYS B 1 126 ? 53.409 103.966 -126.302 1.00 62.55  ? 128 LYS B CB  1 
ATOM   3960 C  CG  . LYS B 1 126 ? 52.092 103.192 -126.251 1.00 68.60  ? 128 LYS B CG  1 
ATOM   3961 C  CD  . LYS B 1 126 ? 51.066 103.724 -127.257 1.00 72.48  ? 128 LYS B CD  1 
ATOM   3962 C  CE  . LYS B 1 126 ? 49.621 103.430 -126.899 1.00 77.12  ? 128 LYS B CE  1 
ATOM   3963 N  NZ  . LYS B 1 126 ? 49.274 102.018 -127.160 1.00 82.99  ? 128 LYS B NZ  1 
ATOM   3964 N  N   . PRO B 1 127 ? 56.563 104.320 -126.651 1.00 53.66  ? 129 PRO B N   1 
ATOM   3965 C  CA  . PRO B 1 127 ? 57.700 105.234 -126.787 1.00 49.30  ? 129 PRO B CA  1 
ATOM   3966 C  C   . PRO B 1 127 ? 57.256 106.694 -126.957 1.00 44.72  ? 129 PRO B C   1 
ATOM   3967 O  O   . PRO B 1 127 ? 56.156 106.956 -127.403 1.00 44.52  ? 129 PRO B O   1 
ATOM   3968 C  CB  . PRO B 1 127 ? 58.438 104.758 -128.043 1.00 49.61  ? 129 PRO B CB  1 
ATOM   3969 C  CG  . PRO B 1 127 ? 57.879 103.373 -128.308 1.00 53.24  ? 129 PRO B CG  1 
ATOM   3970 C  CD  . PRO B 1 127 ? 56.462 103.365 -127.768 1.00 54.48  ? 129 PRO B CD  1 
ATOM   3971 N  N   . GLY B 1 128 ? 58.132 107.615 -126.569 1.00 40.05  ? 130 GLY B N   1 
ATOM   3972 C  CA  . GLY B 1 128 ? 57.893 109.058 -126.719 1.00 36.50  ? 130 GLY B CA  1 
ATOM   3973 C  C   . GLY B 1 128 ? 58.216 109.833 -125.453 1.00 33.24  ? 130 GLY B C   1 
ATOM   3974 O  O   . GLY B 1 128 ? 59.020 109.373 -124.681 1.00 32.56  ? 130 GLY B O   1 
ATOM   3975 N  N   . TYR B 1 129 ? 57.581 110.985 -125.285 1.00 30.91  ? 131 TYR B N   1 
ATOM   3976 C  CA  . TYR B 1 129 ? 57.890 112.022 -124.274 1.00 29.36  ? 131 TYR B CA  1 
ATOM   3977 C  C   . TYR B 1 129 ? 56.653 112.184 -123.390 1.00 29.71  ? 131 TYR B C   1 
ATOM   3978 O  O   . TYR B 1 129 ? 55.543 112.372 -123.904 1.00 31.87  ? 131 TYR B O   1 
ATOM   3979 C  CB  . TYR B 1 129 ? 58.242 113.306 -125.019 1.00 27.70  ? 131 TYR B CB  1 
ATOM   3980 C  CG  . TYR B 1 129 ? 59.118 114.323 -124.339 1.00 25.82  ? 131 TYR B CG  1 
ATOM   3981 C  CD1 . TYR B 1 129 ? 60.233 113.944 -123.630 1.00 26.07  ? 131 TYR B CD1 1 
ATOM   3982 C  CD2 . TYR B 1 129 ? 58.897 115.678 -124.510 1.00 25.22  ? 131 TYR B CD2 1 
ATOM   3983 C  CE1 . TYR B 1 129 ? 61.040 114.879 -123.002 1.00 25.44  ? 131 TYR B CE1 1 
ATOM   3984 C  CE2 . TYR B 1 129 ? 59.723 116.630 -123.947 1.00 24.35  ? 131 TYR B CE2 1 
ATOM   3985 C  CZ  . TYR B 1 129 ? 60.794 116.221 -123.183 1.00 24.75  ? 131 TYR B CZ  1 
ATOM   3986 O  OH  . TYR B 1 129 ? 61.664 117.093 -122.625 1.00 24.32  ? 131 TYR B OH  1 
ATOM   3987 N  N   . TYR B 1 130 ? 56.833 112.094 -122.080 1.00 29.87  ? 132 TYR B N   1 
ATOM   3988 C  CA  . TYR B 1 130 ? 55.740 112.129 -121.080 1.00 28.72  ? 132 TYR B CA  1 
ATOM   3989 C  C   . TYR B 1 130 ? 55.954 113.311 -120.129 1.00 25.97  ? 132 TYR B C   1 
ATOM   3990 O  O   . TYR B 1 130 ? 57.115 113.600 -119.723 1.00 24.60  ? 132 TYR B O   1 
ATOM   3991 C  CB  . TYR B 1 130 ? 55.702 110.787 -120.353 1.00 30.34  ? 132 TYR B CB  1 
ATOM   3992 C  CG  . TYR B 1 130 ? 55.241 109.654 -121.228 1.00 32.54  ? 132 TYR B CG  1 
ATOM   3993 C  CD1 . TYR B 1 130 ? 56.126 108.949 -122.023 1.00 34.04  ? 132 TYR B CD1 1 
ATOM   3994 C  CD2 . TYR B 1 130 ? 53.901 109.312 -121.289 1.00 34.18  ? 132 TYR B CD2 1 
ATOM   3995 C  CE1 . TYR B 1 130 ? 55.691 107.909 -122.832 1.00 35.80  ? 132 TYR B CE1 1 
ATOM   3996 C  CE2 . TYR B 1 130 ? 53.449 108.282 -122.094 1.00 35.69  ? 132 TYR B CE2 1 
ATOM   3997 C  CZ  . TYR B 1 130 ? 54.346 107.586 -122.870 1.00 36.66  ? 132 TYR B CZ  1 
ATOM   3998 O  OH  . TYR B 1 130 ? 53.874 106.582 -123.652 1.00 40.29  ? 132 TYR B OH  1 
ATOM   3999 N  N   . LEU B 1 131 ? 54.857 113.981 -119.784 1.00 24.62  ? 133 LEU B N   1 
ATOM   4000 C  CA  . LEU B 1 131 ? 54.797 114.907 -118.628 1.00 24.27  ? 133 LEU B CA  1 
ATOM   4001 C  C   . LEU B 1 131 ? 54.230 114.162 -117.412 1.00 23.91  ? 133 LEU B C   1 
ATOM   4002 O  O   . LEU B 1 131 ? 53.136 113.662 -117.465 1.00 23.72  ? 133 LEU B O   1 
ATOM   4003 C  CB  . LEU B 1 131 ? 53.977 116.147 -118.984 1.00 24.05  ? 133 LEU B CB  1 
ATOM   4004 C  CG  . LEU B 1 131 ? 54.081 117.268 -117.947 1.00 23.79  ? 133 LEU B CG  1 
ATOM   4005 C  CD1 . LEU B 1 131 ? 53.772 118.605 -118.564 1.00 23.84  ? 133 LEU B CD1 1 
ATOM   4006 C  CD2 . LEU B 1 131 ? 53.154 117.009 -116.753 1.00 24.51  ? 133 LEU B CD2 1 
ATOM   4007 N  N   . ILE B 1 132 ? 54.991 114.113 -116.336 1.00 24.78  ? 134 ILE B N   1 
ATOM   4008 C  CA  . ILE B 1 132 ? 54.541 113.573 -115.031 1.00 25.42  ? 134 ILE B CA  1 
ATOM   4009 C  C   . ILE B 1 132 ? 54.215 114.721 -114.068 1.00 24.53  ? 134 ILE B C   1 
ATOM   4010 O  O   . ILE B 1 132 ? 55.045 115.658 -113.897 1.00 23.27  ? 134 ILE B O   1 
ATOM   4011 C  CB  . ILE B 1 132 ? 55.634 112.691 -114.435 1.00 26.67  ? 134 ILE B CB  1 
ATOM   4012 C  CG1 . ILE B 1 132 ? 56.043 111.556 -115.368 1.00 28.06  ? 134 ILE B CG1 1 
ATOM   4013 C  CG2 . ILE B 1 132 ? 55.192 112.205 -113.076 1.00 26.61  ? 134 ILE B CG2 1 
ATOM   4014 C  CD1 . ILE B 1 132 ? 57.148 110.708 -114.780 1.00 29.30  ? 134 ILE B CD1 1 
ATOM   4015 N  N   . LYS B 1 133 ? 53.048 114.632 -113.453 1.00 24.46  ? 135 LYS B N   1 
ATOM   4016 C  CA  . LYS B 1 133 ? 52.632 115.551 -112.368 1.00 24.00  ? 135 LYS B CA  1 
ATOM   4017 C  C   . LYS B 1 133 ? 51.795 114.800 -111.332 1.00 24.87  ? 135 LYS B C   1 
ATOM   4018 O  O   . LYS B 1 133 ? 51.215 113.755 -111.660 1.00 25.57  ? 135 LYS B O   1 
ATOM   4019 C  CB  . LYS B 1 133 ? 51.794 116.677 -112.955 1.00 23.77  ? 135 LYS B CB  1 
ATOM   4020 C  CG  . LYS B 1 133 ? 50.578 116.183 -113.690 1.00 24.83  ? 135 LYS B CG  1 
ATOM   4021 C  CD  . LYS B 1 133 ? 49.859 117.290 -114.350 1.00 25.80  ? 135 LYS B CD  1 
ATOM   4022 C  CE  . LYS B 1 133 ? 48.977 118.042 -113.394 1.00 26.81  ? 135 LYS B CE  1 
ATOM   4023 N  NZ  . LYS B 1 133 ? 48.136 119.045 -114.087 1.00 27.48  ? 135 LYS B NZ  1 
ATOM   4024 N  N   . ASP B 1 134 ? 51.705 115.353 -110.124 1.00 24.50  ? 136 ASP B N   1 
ATOM   4025 C  CA  . ASP B 1 134 ? 50.635 114.974 -109.186 1.00 25.97  ? 136 ASP B CA  1 
ATOM   4026 C  C   . ASP B 1 134 ? 49.320 115.414 -109.827 1.00 26.42  ? 136 ASP B C   1 
ATOM   4027 O  O   . ASP B 1 134 ? 49.240 116.552 -110.336 1.00 25.03  ? 136 ASP B O   1 
ATOM   4028 C  CB  . ASP B 1 134 ? 50.825 115.618 -107.816 1.00 25.05  ? 136 ASP B CB  1 
ATOM   4029 C  CG  . ASP B 1 134 ? 51.906 115.012 -106.956 1.00 26.02  ? 136 ASP B CG  1 
ATOM   4030 O  OD1 . ASP B 1 134 ? 51.568 114.173 -106.121 1.00 28.62  ? 136 ASP B OD1 1 
ATOM   4031 O  OD2 . ASP B 1 134 ? 53.054 115.461 -107.024 1.00 25.75  ? 136 ASP B OD2 1 
ATOM   4032 N  N   . SER B 1 135 ? 48.332 114.538 -109.765 1.00 28.55  ? 137 SER B N   1 
ATOM   4033 C  CA  . SER B 1 135 ? 46.924 114.820 -110.097 1.00 31.57  ? 137 SER B CA  1 
ATOM   4034 C  C   . SER B 1 135 ? 46.407 116.024 -109.312 1.00 33.51  ? 137 SER B C   1 
ATOM   4035 O  O   . SER B 1 135 ? 46.617 116.055 -108.075 1.00 35.97  ? 137 SER B O   1 
ATOM   4036 C  CB  . SER B 1 135 ? 46.107 113.626 -109.815 1.00 33.21  ? 137 SER B CB  1 
ATOM   4037 O  OG  . SER B 1 135 ? 44.776 113.965 -110.067 1.00 35.19  ? 137 SER B OG  1 
ATOM   4038 N  N   . ARG B 1 136 ? 45.742 116.967 -109.972 1.00 35.64  ? 138 ARG B N   1 
ATOM   4039 C  CA  . ARG B 1 136 ? 45.494 118.301 -109.370 1.00 39.17  ? 138 ARG B CA  1 
ATOM   4040 C  C   . ARG B 1 136 ? 44.507 118.120 -108.224 1.00 40.09  ? 138 ARG B C   1 
ATOM   4041 O  O   . ARG B 1 136 ? 43.603 117.285 -108.337 1.00 41.72  ? 138 ARG B O   1 
ATOM   4042 C  CB  . ARG B 1 136 ? 45.000 119.344 -110.371 1.00 41.70  ? 138 ARG B CB  1 
ATOM   4043 C  CG  . ARG B 1 136 ? 43.579 119.140 -110.864 1.00 46.94  ? 138 ARG B CG  1 
ATOM   4044 C  CD  . ARG B 1 136 ? 43.285 120.113 -111.988 1.00 52.07  ? 138 ARG B CD  1 
ATOM   4045 N  NE  . ARG B 1 136 ? 43.741 121.455 -111.619 1.00 56.11  ? 138 ARG B NE  1 
ATOM   4046 C  CZ  . ARG B 1 136 ? 43.098 122.306 -110.798 1.00 59.88  ? 138 ARG B CZ  1 
ATOM   4047 N  NH1 . ARG B 1 136 ? 41.931 121.977 -110.263 1.00 63.21  ? 138 ARG B NH1 1 
ATOM   4048 N  NH2 . ARG B 1 136 ? 43.616 123.500 -110.536 1.00 58.61  ? 138 ARG B NH2 1 
ATOM   4049 N  N   . GLY B 1 137 ? 44.740 118.831 -107.131 1.00 40.09  ? 139 GLY B N   1 
ATOM   4050 C  CA  . GLY B 1 137 ? 43.894 118.753 -105.928 1.00 39.92  ? 139 GLY B CA  1 
ATOM   4051 C  C   . GLY B 1 137 ? 44.111 117.479 -105.137 1.00 39.47  ? 139 GLY B C   1 
ATOM   4052 O  O   . GLY B 1 137 ? 43.572 117.394 -104.036 1.00 38.45  ? 139 GLY B O   1 
ATOM   4053 N  N   . SER B 1 138 ? 44.874 116.512 -105.642 1.00 38.99  ? 140 SER B N   1 
ATOM   4054 C  CA  . SER B 1 138 ? 44.904 115.147 -105.058 1.00 40.12  ? 140 SER B CA  1 
ATOM   4055 C  C   . SER B 1 138 ? 45.562 115.172 -103.669 1.00 40.58  ? 140 SER B C   1 
ATOM   4056 O  O   . SER B 1 138 ? 45.477 114.148 -102.984 1.00 42.21  ? 140 SER B O   1 
ATOM   4057 C  CB  . SER B 1 138 ? 45.542 114.121 -105.983 1.00 40.13  ? 140 SER B CB  1 
ATOM   4058 O  OG  . SER B 1 138 ? 46.946 114.313 -106.135 1.00 38.79  ? 140 SER B OG  1 
ATOM   4059 N  N   . LEU B 1 139 ? 46.189 116.272 -103.247 1.00 39.64  ? 141 LEU B N   1 
ATOM   4060 C  CA  . LEU B 1 139 ? 46.874 116.347 -101.926 1.00 40.08  ? 141 LEU B CA  1 
ATOM   4061 C  C   . LEU B 1 139 ? 46.211 117.392 -101.018 1.00 41.03  ? 141 LEU B C   1 
ATOM   4062 O  O   . LEU B 1 139 ? 46.790 117.747 -99.989  1.00 41.93  ? 141 LEU B O   1 
ATOM   4063 C  CB  . LEU B 1 139 ? 48.343 116.688 -102.166 1.00 38.06  ? 141 LEU B CB  1 
ATOM   4064 C  CG  . LEU B 1 139 ? 49.159 115.683 -102.978 1.00 37.76  ? 141 LEU B CG  1 
ATOM   4065 C  CD1 . LEU B 1 139 ? 50.620 116.150 -103.052 1.00 36.75  ? 141 LEU B CD1 1 
ATOM   4066 C  CD2 . LEU B 1 139 ? 49.077 114.260 -102.414 1.00 38.74  ? 141 LEU B CD2 1 
ATOM   4067 N  N   . ASP B 1 140 ? 45.028 117.869 -101.357 1.00 44.09  ? 142 ASP B N   1 
ATOM   4068 C  CA  . ASP B 1 140 ? 44.378 118.933 -100.560 1.00 48.42  ? 142 ASP B CA  1 
ATOM   4069 C  C   . ASP B 1 140 ? 43.820 118.277 -99.292  1.00 50.56  ? 142 ASP B C   1 
ATOM   4070 O  O   . ASP B 1 140 ? 43.286 117.151 -99.347  1.00 51.53  ? 142 ASP B O   1 
ATOM   4071 C  CB  . ASP B 1 140 ? 43.356 119.709 -101.391 1.00 51.14  ? 142 ASP B CB  1 
ATOM   4072 C  CG  . ASP B 1 140 ? 43.945 120.449 -102.606 1.00 55.11  ? 142 ASP B CG  1 
ATOM   4073 O  OD1 . ASP B 1 140 ? 45.235 120.537 -102.783 1.00 49.97  ? 142 ASP B OD1 1 
ATOM   4074 O  OD2 . ASP B 1 140 ? 43.111 120.955 -103.404 1.00 60.19  ? 142 ASP B OD2 1 
ATOM   4075 N  N   A ASN B 1 141 ? 44.006 118.935 -98.151  0.50 49.97  ? 143 ASN B N   1 
ATOM   4076 N  N   B ASN B 1 141 ? 43.975 118.947 -98.153  0.50 50.25  ? 143 ASN B N   1 
ATOM   4077 C  CA  A ASN B 1 141 ? 43.469 118.470 -96.847  0.50 51.61  ? 143 ASN B CA  1 
ATOM   4078 C  CA  B ASN B 1 141 ? 43.473 118.426 -96.858  0.50 52.08  ? 143 ASN B CA  1 
ATOM   4079 C  C   A ASN B 1 141 ? 44.382 117.374 -96.263  0.50 50.39  ? 143 ASN B C   1 
ATOM   4080 C  C   B ASN B 1 141 ? 44.126 117.055 -96.578  0.50 50.62  ? 143 ASN B C   1 
ATOM   4081 O  O   A ASN B 1 141 ? 44.218 117.073 -95.054  0.50 51.11  ? 143 ASN B O   1 
ATOM   4082 O  O   B ASN B 1 141 ? 43.468 116.165 -96.001  0.50 52.67  ? 143 ASN B O   1 
ATOM   4083 C  CB  A ASN B 1 141 ? 42.002 118.015 -96.977  0.50 53.85  ? 143 ASN B CB  1 
ATOM   4084 C  CB  B ASN B 1 141 ? 41.939 118.391 -96.879  0.50 54.64  ? 143 ASN B CB  1 
ATOM   4085 C  CG  A ASN B 1 141 ? 41.139 118.463 -95.816  0.50 54.33  ? 143 ASN B CG  1 
ATOM   4086 C  CG  B ASN B 1 141 ? 41.342 119.529 -97.684  0.50 54.38  ? 143 ASN B CG  1 
ATOM   4087 O  OD1 A ASN B 1 141 ? 41.373 119.532 -95.265  0.50 53.81  ? 143 ASN B OD1 1 
ATOM   4088 O  OD1 B ASN B 1 141 ? 40.600 119.294 -98.637  0.50 54.18  ? 143 ASN B OD1 1 
ATOM   4089 N  ND2 A ASN B 1 141 ? 40.143 117.672 -95.451  0.50 54.55  ? 143 ASN B ND2 1 
ATOM   4090 N  ND2 B ASN B 1 141 ? 41.682 120.759 -97.326  0.50 53.21  ? 143 ASN B ND2 1 
ATOM   4091 N  N   . LYS B 1 142 ? 45.365 116.862 -97.018  1.00 47.22  ? 144 LYS B N   1 
ATOM   4092 C  CA  . LYS B 1 142 ? 46.248 115.771 -96.528  1.00 44.54  ? 144 LYS B CA  1 
ATOM   4093 C  C   . LYS B 1 142 ? 47.545 116.403 -96.040  1.00 39.87  ? 144 LYS B C   1 
ATOM   4094 O  O   . LYS B 1 142 ? 47.922 117.445 -96.523  1.00 40.75  ? 144 LYS B O   1 
ATOM   4095 C  CB  . LYS B 1 142 ? 46.539 114.750 -97.626  1.00 45.69  ? 144 LYS B CB  1 
ATOM   4096 C  CG  . LYS B 1 142 ? 45.324 114.243 -98.388  1.00 47.83  ? 144 LYS B CG  1 
ATOM   4097 C  CD  . LYS B 1 142 ? 45.699 113.158 -99.341  1.00 49.96  ? 144 LYS B CD  1 
ATOM   4098 C  CE  . LYS B 1 142 ? 46.547 112.087 -98.686  1.00 50.64  ? 144 LYS B CE  1 
ATOM   4099 N  NZ  . LYS B 1 142 ? 46.534 110.836 -99.483  1.00 51.82  ? 144 LYS B NZ  1 
ATOM   4100 N  N   . LYS B 1 143 ? 48.230 115.807 -95.098  1.00 36.37  ? 145 LYS B N   1 
ATOM   4101 C  CA  . LYS B 1 143 ? 49.271 116.572 -94.388  1.00 34.41  ? 145 LYS B CA  1 
ATOM   4102 C  C   . LYS B 1 143 ? 50.614 115.990 -94.744  1.00 31.74  ? 145 LYS B C   1 
ATOM   4103 O  O   . LYS B 1 143 ? 50.683 114.787 -94.930  1.00 31.57  ? 145 LYS B O   1 
ATOM   4104 C  CB  . LYS B 1 143 ? 49.101 116.518 -92.869  1.00 35.27  ? 145 LYS B CB  1 
ATOM   4105 C  CG  . LYS B 1 143 ? 47.894 117.278 -92.352  1.00 36.68  ? 145 LYS B CG  1 
ATOM   4106 C  CD  . LYS B 1 143 ? 47.992 117.495 -90.882  1.00 37.57  ? 145 LYS B CD  1 
ATOM   4107 C  CE  . LYS B 1 143 ? 46.815 118.239 -90.302  1.00 39.16  ? 145 LYS B CE  1 
ATOM   4108 N  NZ  . LYS B 1 143 ? 47.156 118.782 -88.960  1.00 40.63  ? 145 LYS B NZ  1 
ATOM   4109 N  N   . GLY B 1 144 ? 51.626 116.848 -94.773  1.00 30.00  ? 146 GLY B N   1 
ATOM   4110 C  CA  . GLY B 1 144 ? 53.041 116.471 -94.921  1.00 29.00  ? 146 GLY B CA  1 
ATOM   4111 C  C   . GLY B 1 144 ? 53.434 116.134 -96.350  1.00 28.06  ? 146 GLY B C   1 
ATOM   4112 O  O   . GLY B 1 144 ? 54.529 115.558 -96.492  1.00 26.85  ? 146 GLY B O   1 
ATOM   4113 N  N   . HIS B 1 145 ? 52.614 116.486 -97.356  1.00 27.02  ? 147 HIS B N   1 
ATOM   4114 C  CA  . HIS B 1 145 ? 52.870 116.110 -98.774  1.00 26.81  ? 147 HIS B CA  1 
ATOM   4115 C  C   . HIS B 1 145 ? 53.112 117.345 -99.624  1.00 24.69  ? 147 HIS B C   1 
ATOM   4116 O  O   . HIS B 1 145 ? 52.763 118.434 -99.174  1.00 24.28  ? 147 HIS B O   1 
ATOM   4117 C  CB  . HIS B 1 145 ? 51.721 115.270 -99.320  1.00 28.48  ? 147 HIS B CB  1 
ATOM   4118 C  CG  . HIS B 1 145 ? 51.539 113.962 -98.615  1.00 30.26  ? 147 HIS B CG  1 
ATOM   4119 N  ND1 . HIS B 1 145 ? 52.572 113.030 -98.462  1.00 31.09  ? 147 HIS B ND1 1 
ATOM   4120 C  CD2 . HIS B 1 145 ? 50.442 113.397 -98.068  1.00 31.50  ? 147 HIS B CD2 1 
ATOM   4121 C  CE1 . HIS B 1 145 ? 52.120 111.960 -97.833  1.00 31.77  ? 147 HIS B CE1 1 
ATOM   4122 N  NE2 . HIS B 1 145 ? 50.809 112.163 -97.587  1.00 32.89  ? 147 HIS B NE2 1 
ATOM   4123 N  N   . ALA B 1 146 ? 53.693 117.160 -100.812 1.00 23.52  ? 148 ALA B N   1 
ATOM   4124 C  CA  . ALA B 1 146 ? 53.879 118.278 -101.748 1.00 22.33  ? 148 ALA B CA  1 
ATOM   4125 C  C   . ALA B 1 146 ? 53.690 117.826 -103.189 1.00 22.52  ? 148 ALA B C   1 
ATOM   4126 O  O   . ALA B 1 146 ? 53.946 116.638 -103.497 1.00 22.59  ? 148 ALA B O   1 
ATOM   4127 C  CB  . ALA B 1 146 ? 55.228 118.888 -101.544 1.00 21.90  ? 148 ALA B CB  1 
ATOM   4128 N  N   . TYR B 1 147 ? 53.263 118.763 -104.038 1.00 22.06  ? 149 TYR B N   1 
ATOM   4129 C  CA  . TYR B 1 147 ? 53.178 118.559 -105.510 1.00 22.17  ? 149 TYR B CA  1 
ATOM   4130 C  C   . TYR B 1 147 ? 54.591 118.605 -106.116 1.00 21.06  ? 149 TYR B C   1 
ATOM   4131 O  O   . TYR B 1 147 ? 55.495 119.386 -105.687 1.00 20.30  ? 149 TYR B O   1 
ATOM   4132 C  CB  . TYR B 1 147 ? 52.205 119.556 -106.143 1.00 22.82  ? 149 TYR B CB  1 
ATOM   4133 C  CG  . TYR B 1 147 ? 50.770 119.404 -105.683 1.00 24.36  ? 149 TYR B CG  1 
ATOM   4134 C  CD1 . TYR B 1 147 ? 49.899 118.541 -106.329 1.00 24.87  ? 149 TYR B CD1 1 
ATOM   4135 C  CD2 . TYR B 1 147 ? 50.269 120.129 -104.601 1.00 24.98  ? 149 TYR B CD2 1 
ATOM   4136 C  CE1 . TYR B 1 147 ? 48.586 118.393 -105.913 1.00 26.12  ? 149 TYR B CE1 1 
ATOM   4137 C  CE2 . TYR B 1 147 ? 48.955 120.004 -104.178 1.00 25.30  ? 149 TYR B CE2 1 
ATOM   4138 C  CZ  . TYR B 1 147 ? 48.119 119.135 -104.838 1.00 26.32  ? 149 TYR B CZ  1 
ATOM   4139 O  OH  . TYR B 1 147 ? 46.821 119.034 -104.469 1.00 28.82  ? 149 TYR B OH  1 
ATOM   4140 N  N   . THR B 1 148 ? 54.798 117.731 -107.098 1.00 21.25  ? 150 THR B N   1 
ATOM   4141 C  CA  . THR B 1 148 ? 56.056 117.665 -107.880 1.00 20.28  ? 150 THR B CA  1 
ATOM   4142 C  C   . THR B 1 148 ? 56.011 118.764 -108.915 1.00 19.28  ? 150 THR B C   1 
ATOM   4143 O  O   . THR B 1 148 ? 54.933 119.075 -109.400 1.00 18.96  ? 150 THR B O   1 
ATOM   4144 C  CB  . THR B 1 148 ? 56.334 116.309 -108.532 1.00 20.46  ? 150 THR B CB  1 
ATOM   4145 O  OG1 . THR B 1 148 ? 57.612 116.446 -109.157 1.00 20.07  ? 150 THR B OG1 1 
ATOM   4146 C  CG2 . THR B 1 148 ? 55.301 115.907 -109.551 1.00 21.04  ? 150 THR B CG2 1 
ATOM   4147 N  N   . SER B 1 149 ? 57.154 119.377 -109.142 1.00 19.31  ? 151 SER B N   1 
ATOM   4148 C  CA  . SER B 1 149 ? 57.422 120.165 -110.355 1.00 19.50  ? 151 SER B CA  1 
ATOM   4149 C  C   . SER B 1 149 ? 57.088 119.254 -111.535 1.00 19.43  ? 151 SER B C   1 
ATOM   4150 O  O   . SER B 1 149 ? 57.388 118.043 -111.472 1.00 18.65  ? 151 SER B O   1 
ATOM   4151 C  CB  . SER B 1 149 ? 58.850 120.639 -110.421 1.00 19.82  ? 151 SER B CB  1 
ATOM   4152 O  OG  . SER B 1 149 ? 59.068 121.775 -109.603 1.00 19.85  ? 151 SER B OG  1 
ATOM   4153 N  N   . PHE B 1 150 ? 56.408 119.798 -112.532 1.00 20.12  ? 152 PHE B N   1 
ATOM   4154 C  CA  . PHE B 1 150 ? 56.048 119.046 -113.756 1.00 21.03  ? 152 PHE B CA  1 
ATOM   4155 C  C   . PHE B 1 150 ? 57.349 118.512 -114.345 1.00 20.76  ? 152 PHE B C   1 
ATOM   4156 O  O   . PHE B 1 150 ? 58.368 119.252 -114.408 1.00 20.32  ? 152 PHE B O   1 
ATOM   4157 C  CB  . PHE B 1 150 ? 55.237 119.896 -114.734 1.00 21.89  ? 152 PHE B CB  1 
ATOM   4158 C  CG  . PHE B 1 150 ? 53.978 120.501 -114.160 1.00 22.86  ? 152 PHE B CG  1 
ATOM   4159 C  CD1 . PHE B 1 150 ? 53.224 119.836 -113.193 1.00 23.63  ? 152 PHE B CD1 1 
ATOM   4160 C  CD2 . PHE B 1 150 ? 53.600 121.775 -114.549 1.00 23.29  ? 152 PHE B CD2 1 
ATOM   4161 C  CE1 . PHE B 1 150 ? 52.086 120.430 -112.648 1.00 24.78  ? 152 PHE B CE1 1 
ATOM   4162 C  CE2 . PHE B 1 150 ? 52.466 122.363 -114.023 1.00 24.68  ? 152 PHE B CE2 1 
ATOM   4163 C  CZ  . PHE B 1 150 ? 51.701 121.693 -113.070 1.00 25.36  ? 152 PHE B CZ  1 
ATOM   4164 N  N   . MET B 1 151 ? 57.345 117.215 -114.616 1.00 20.75  ? 153 MET B N   1 
ATOM   4165 C  CA  . MET B 1 151 ? 58.562 116.517 -115.064 1.00 21.51  ? 153 MET B CA  1 
ATOM   4166 C  C   . MET B 1 151 ? 58.371 116.063 -116.502 1.00 21.63  ? 153 MET B C   1 
ATOM   4167 O  O   . MET B 1 151 ? 57.424 115.270 -116.742 1.00 22.10  ? 153 MET B O   1 
ATOM   4168 C  CB  . MET B 1 151 ? 58.826 115.309 -114.175 1.00 22.12  ? 153 MET B CB  1 
ATOM   4169 C  CG  . MET B 1 151 ? 59.423 115.708 -112.860 1.00 22.20  ? 153 MET B CG  1 
ATOM   4170 S  SD  . MET B 1 151 ? 59.607 114.321 -111.722 1.00 23.42  ? 153 MET B SD  1 
ATOM   4171 C  CE  . MET B 1 151 ? 57.934 113.693 -111.812 1.00 23.48  ? 153 MET B CE  1 
ATOM   4172 N  N   . LEU B 1 152 ? 59.232 116.511 -117.414 1.00 21.64  ? 154 LEU B N   1 
ATOM   4173 C  CA  . LEU B 1 152 ? 59.258 115.946 -118.795 1.00 22.41  ? 154 LEU B CA  1 
ATOM   4174 C  C   . LEU B 1 152 ? 60.272 114.805 -118.821 1.00 24.18  ? 154 LEU B C   1 
ATOM   4175 O  O   . LEU B 1 152 ? 61.404 114.972 -118.329 1.00 24.52  ? 154 LEU B O   1 
ATOM   4176 C  CB  . LEU B 1 152 ? 59.594 117.071 -119.752 1.00 21.51  ? 154 LEU B CB  1 
ATOM   4177 C  CG  . LEU B 1 152 ? 58.412 117.957 -120.096 1.00 21.30  ? 154 LEU B CG  1 
ATOM   4178 C  CD1 . LEU B 1 152 ? 58.873 119.147 -120.917 1.00 21.60  ? 154 LEU B CD1 1 
ATOM   4179 C  CD2 . LEU B 1 152 ? 57.377 117.170 -120.880 1.00 21.49  ? 154 LEU B CD2 1 
ATOM   4180 N  N   . GLN B 1 153 ? 59.850 113.631 -119.243 1.00 26.41  ? 155 GLN B N   1 
ATOM   4181 C  CA  . GLN B 1 153 ? 60.749 112.452 -119.273 1.00 28.97  ? 155 GLN B CA  1 
ATOM   4182 C  C   . GLN B 1 153 ? 60.520 111.738 -120.605 1.00 29.45  ? 155 GLN B C   1 
ATOM   4183 O  O   . GLN B 1 153 ? 59.355 111.604 -120.985 1.00 29.68  ? 155 GLN B O   1 
ATOM   4184 C  CB  . GLN B 1 153 ? 60.477 111.596 -118.027 1.00 30.78  ? 155 GLN B CB  1 
ATOM   4185 C  CG  . GLN B 1 153 ? 61.355 110.346 -117.895 1.00 33.56  ? 155 GLN B CG  1 
ATOM   4186 C  CD  . GLN B 1 153 ? 62.842 110.635 -117.815 1.00 35.11  ? 155 GLN B CD  1 
ATOM   4187 O  OE1 . GLN B 1 153 ? 63.306 111.298 -116.885 1.00 35.76  ? 155 GLN B OE1 1 
ATOM   4188 N  NE2 . GLN B 1 153 ? 63.615 110.146 -118.785 1.00 35.21  ? 155 GLN B NE2 1 
ATOM   4189 N  N   . VAL B 1 154 ? 61.587 111.340 -121.296 1.00 30.88  ? 156 VAL B N   1 
ATOM   4190 C  CA  . VAL B 1 154 ? 61.525 110.368 -122.425 1.00 32.90  ? 156 VAL B CA  1 
ATOM   4191 C  C   . VAL B 1 154 ? 61.303 108.993 -121.804 1.00 35.49  ? 156 VAL B C   1 
ATOM   4192 O  O   . VAL B 1 154 ? 61.986 108.677 -120.839 1.00 36.49  ? 156 VAL B O   1 
ATOM   4193 C  CB  . VAL B 1 154 ? 62.801 110.344 -123.301 1.00 33.48  ? 156 VAL B CB  1 
ATOM   4194 C  CG1 . VAL B 1 154 ? 62.638 109.385 -124.468 1.00 33.82  ? 156 VAL B CG1 1 
ATOM   4195 C  CG2 . VAL B 1 154 ? 63.231 111.717 -123.812 1.00 32.57  ? 156 VAL B CG2 1 
ATOM   4196 N  N   . ALA B 1 155 ? 60.467 108.182 -122.419 1.00 40.84  ? 157 ALA B N   1 
ATOM   4197 C  CA  . ALA B 1 155 ? 60.251 106.801 -121.978 1.00 45.58  ? 157 ALA B CA  1 
ATOM   4198 C  C   . ALA B 1 155 ? 61.431 105.874 -122.312 1.00 48.88  ? 157 ALA B C   1 
ATOM   4199 O  O   . ALA B 1 155 ? 61.569 105.464 -123.447 1.00 49.46  ? 157 ALA B O   1 
ATOM   4200 C  CB  . ALA B 1 155 ? 58.977 106.292 -122.576 1.00 47.06  ? 157 ALA B CB  1 
ATOM   4201 N  N   . LYS B 1 156 ? 62.323 105.689 -121.350 1.00 51.90  ? 158 LYS B N   1 
ATOM   4202 C  CA  . LYS B 1 156 ? 63.312 104.591 -121.333 1.00 55.08  ? 158 LYS B CA  1 
ATOM   4203 C  C   . LYS B 1 156 ? 63.005 103.737 -120.109 1.00 57.48  ? 158 LYS B C   1 
ATOM   4204 O  O   . LYS B 1 156 ? 62.122 104.126 -119.301 1.00 61.91  ? 158 LYS B O   1 
ATOM   4205 C  CB  . LYS B 1 156 ? 64.753 105.079 -121.189 1.00 56.35  ? 158 LYS B CB  1 
ATOM   4206 C  CG  . LYS B 1 156 ? 65.034 106.542 -121.514 1.00 58.19  ? 158 LYS B CG  1 
ATOM   4207 C  CD  . LYS B 1 156 ? 66.539 106.861 -121.438 1.00 61.84  ? 158 LYS B CD  1 
ATOM   4208 C  CE  . LYS B 1 156 ? 66.917 108.183 -120.782 1.00 61.55  ? 158 LYS B CE  1 
ATOM   4209 N  NZ  . LYS B 1 156 ? 66.516 109.350 -121.611 1.00 62.66  ? 158 LYS B NZ  1 
ATOM   4210 N  N   . ASP B 1 157 ? 63.721 102.631 -119.959 1.00 59.15  ? 159 ASP B N   1 
ATOM   4211 C  CA  . ASP B 1 157 ? 63.739 101.864 -118.692 1.00 61.20  ? 159 ASP B CA  1 
ATOM   4212 C  C   . ASP B 1 157 ? 64.744 102.591 -117.784 1.00 60.46  ? 159 ASP B C   1 
ATOM   4213 O  O   . ASP B 1 157 ? 65.875 102.130 -117.634 1.00 60.87  ? 159 ASP B O   1 
ATOM   4214 C  CB  . ASP B 1 157 ? 63.960 100.370 -118.968 1.00 64.10  ? 159 ASP B CB  1 
ATOM   4215 C  CG  . ASP B 1 157 ? 62.760 99.663  -119.593 1.00 66.23  ? 159 ASP B CG  1 
ATOM   4216 O  OD1 . ASP B 1 157 ? 61.761 100.333 -119.871 1.00 65.65  ? 159 ASP B OD1 1 
ATOM   4217 O  OD2 . ASP B 1 157 ? 62.816 98.436  -119.767 1.00 68.89  ? 159 ASP B OD2 1 
ATOM   4218 N  N   . THR B 1 158 ? 64.327 103.713 -117.200 1.00 59.54  ? 160 THR B N   1 
ATOM   4219 C  CA  . THR B 1 158 ? 65.196 104.658 -116.450 1.00 58.08  ? 160 THR B CA  1 
ATOM   4220 C  C   . THR B 1 158 ? 64.649 104.884 -115.024 1.00 57.25  ? 160 THR B C   1 
ATOM   4221 O  O   . THR B 1 158 ? 63.461 104.614 -114.769 1.00 59.63  ? 160 THR B O   1 
ATOM   4222 C  CB  . THR B 1 158 ? 65.337 105.943 -117.279 1.00 57.42  ? 160 THR B CB  1 
ATOM   4223 O  OG1 . THR B 1 158 ? 66.413 106.705 -116.753 1.00 58.37  ? 160 THR B OG1 1 
ATOM   4224 C  CG2 . THR B 1 158 ? 64.105 106.823 -117.281 1.00 56.76  ? 160 THR B CG2 1 
ATOM   4225 N  N   . THR B 1 159 ? 65.493 105.388 -114.123 1.00 53.55  ? 161 THR B N   1 
ATOM   4226 C  CA  . THR B 1 159 ? 65.109 105.843 -112.757 1.00 50.44  ? 161 THR B CA  1 
ATOM   4227 C  C   . THR B 1 159 ? 65.378 107.346 -112.624 1.00 45.20  ? 161 THR B C   1 
ATOM   4228 O  O   . THR B 1 159 ? 66.518 107.761 -112.762 1.00 41.80  ? 161 THR B O   1 
ATOM   4229 C  CB  . THR B 1 159 ? 65.842 105.071 -111.647 1.00 51.12  ? 161 THR B CB  1 
ATOM   4230 O  OG1 . THR B 1 159 ? 65.405 103.716 -111.741 1.00 52.25  ? 161 THR B OG1 1 
ATOM   4231 C  CG2 . THR B 1 159 ? 65.581 105.603 -110.253 1.00 51.00  ? 161 THR B CG2 1 
ATOM   4232 N  N   . VAL B 1 160 ? 64.356 108.127 -112.307 1.00 42.25  ? 162 VAL B N   1 
ATOM   4233 C  CA  . VAL B 1 160 ? 64.526 109.582 -112.071 1.00 39.28  ? 162 VAL B CA  1 
ATOM   4234 C  C   . VAL B 1 160 ? 63.883 109.936 -110.729 1.00 36.59  ? 162 VAL B C   1 
ATOM   4235 O  O   . VAL B 1 160 ? 62.804 109.400 -110.400 1.00 34.55  ? 162 VAL B O   1 
ATOM   4236 C  CB  . VAL B 1 160 ? 63.944 110.372 -113.256 1.00 38.98  ? 162 VAL B CB  1 
ATOM   4237 C  CG1 . VAL B 1 160 ? 62.490 109.979 -113.550 1.00 38.30  ? 162 VAL B CG1 1 
ATOM   4238 C  CG2 . VAL B 1 160 ? 64.108 111.881 -113.061 1.00 38.36  ? 162 VAL B CG2 1 
ATOM   4239 N  N   . ALA B 1 161 ? 64.495 110.858 -109.998 1.00 35.58  ? 163 ALA B N   1 
ATOM   4240 C  CA  . ALA B 1 161 ? 63.975 111.310 -108.682 1.00 35.61  ? 163 ALA B CA  1 
ATOM   4241 C  C   . ALA B 1 161 ? 62.790 112.263 -108.880 1.00 34.00  ? 163 ALA B C   1 
ATOM   4242 O  O   . ALA B 1 161 ? 62.897 113.208 -109.676 1.00 32.52  ? 163 ALA B O   1 
ATOM   4243 C  CB  . ALA B 1 161 ? 65.060 111.955 -107.869 1.00 35.79  ? 163 ALA B CB  1 
ATOM   4244 N  N   . VAL B 1 162 ? 61.713 112.063 -108.127 1.00 32.42  ? 164 VAL B N   1 
ATOM   4245 C  CA  . VAL B 1 162 ? 60.524 112.945 -108.246 1.00 30.74  ? 164 VAL B CA  1 
ATOM   4246 C  C   . VAL B 1 162 ? 60.904 114.341 -107.741 1.00 29.70  ? 164 VAL B C   1 
ATOM   4247 O  O   . VAL B 1 162 ? 61.519 114.387 -106.711 1.00 30.69  ? 164 VAL B O   1 
ATOM   4248 C  CB  . VAL B 1 162 ? 59.358 112.380 -107.438 1.00 29.69  ? 164 VAL B CB  1 
ATOM   4249 C  CG1 . VAL B 1 162 ? 59.636 112.500 -105.939 1.00 29.29  ? 164 VAL B CG1 1 
ATOM   4250 C  CG2 . VAL B 1 162 ? 58.076 113.084 -107.859 1.00 29.04  ? 164 VAL B CG2 1 
ATOM   4251 N  N   . LYS B 1 163 ? 60.470 115.418 -108.402 1.00 29.50  ? 165 LYS B N   1 
ATOM   4252 C  CA  . LYS B 1 163 ? 60.901 116.802 -108.118 1.00 30.30  ? 165 LYS B CA  1 
ATOM   4253 C  C   . LYS B 1 163 ? 59.953 117.404 -107.068 1.00 31.49  ? 165 LYS B C   1 
ATOM   4254 O  O   . LYS B 1 163 ? 59.304 118.451 -107.251 1.00 30.59  ? 165 LYS B O   1 
ATOM   4255 C  CB  . LYS B 1 163 ? 61.015 117.546 -109.430 1.00 32.53  ? 165 LYS B CB  1 
ATOM   4256 C  CG  . LYS B 1 163 ? 62.367 117.359 -110.081 1.00 35.70  ? 165 LYS B CG  1 
ATOM   4257 C  CD  . LYS B 1 163 ? 62.619 118.372 -111.155 1.00 40.25  ? 165 LYS B CD  1 
ATOM   4258 C  CE  . LYS B 1 163 ? 62.832 119.777 -110.623 1.00 43.34  ? 165 LYS B CE  1 
ATOM   4259 N  NZ  . LYS B 1 163 ? 63.753 120.518 -111.516 1.00 45.58  ? 165 LYS B NZ  1 
ATOM   4260 N  N   . ALA B 1 164 ? 59.888 116.745 -105.932 1.00 33.91  ? 166 ALA B N   1 
ATOM   4261 C  CA  . ALA B 1 164 ? 58.935 117.096 -104.868 1.00 34.39  ? 166 ALA B CA  1 
ATOM   4262 C  C   . ALA B 1 164 ? 59.657 116.971 -103.538 1.00 33.85  ? 166 ALA B C   1 
ATOM   4263 O  O   . ALA B 1 164 ? 60.321 115.947 -103.345 1.00 37.22  ? 166 ALA B O   1 
ATOM   4264 C  CB  . ALA B 1 164 ? 57.752 116.174 -104.971 1.00 35.01  ? 166 ALA B CB  1 
ATOM   4265 N  N   . ASP B 1 165 ? 59.575 117.967 -102.665 1.00 32.19  ? 167 ASP B N   1 
ATOM   4266 C  CA  . ASP B 1 165 ? 59.999 117.760 -101.265 1.00 31.25  ? 167 ASP B CA  1 
ATOM   4267 C  C   . ASP B 1 165 ? 59.029 118.505 -100.364 1.00 28.25  ? 167 ASP B C   1 
ATOM   4268 O  O   . ASP B 1 165 ? 58.197 119.281 -100.836 1.00 27.11  ? 167 ASP B O   1 
ATOM   4269 C  CB  . ASP B 1 165 ? 61.443 118.206 -101.034 1.00 33.29  ? 167 ASP B CB  1 
ATOM   4270 C  CG  . ASP B 1 165 ? 62.137 117.578 -99.823  1.00 35.10  ? 167 ASP B CG  1 
ATOM   4271 O  OD1 . ASP B 1 165 ? 61.587 116.564 -99.288  1.00 37.73  ? 167 ASP B OD1 1 
ATOM   4272 O  OD2 . ASP B 1 165 ? 63.239 118.090 -99.424  1.00 34.86  ? 167 ASP B OD2 1 
ATOM   4273 N  N   . VAL B 1 166 ? 59.146 118.260 -99.086  1.00 27.42  ? 168 VAL B N   1 
ATOM   4274 C  CA  . VAL B 1 166 ? 58.280 118.920 -98.070  1.00 25.36  ? 168 VAL B CA  1 
ATOM   4275 C  C   . VAL B 1 166 ? 59.207 119.477 -97.020  1.00 23.73  ? 168 VAL B C   1 
ATOM   4276 O  O   . VAL B 1 166 ? 60.249 118.878 -96.748  1.00 24.13  ? 168 VAL B O   1 
ATOM   4277 C  CB  . VAL B 1 166 ? 57.269 117.956 -97.455  1.00 25.06  ? 168 VAL B CB  1 
ATOM   4278 C  CG1 . VAL B 1 166 ? 56.318 117.478 -98.515  1.00 25.54  ? 168 VAL B CG1 1 
ATOM   4279 C  CG2 . VAL B 1 166 ? 57.956 116.788 -96.769  1.00 26.01  ? 168 VAL B CG2 1 
ATOM   4280 N  N   . PRO B 1 167 ? 58.864 120.648 -96.453  1.00 22.29  ? 169 PRO B N   1 
ATOM   4281 C  CA  . PRO B 1 167 ? 59.550 121.143 -95.264  1.00 22.45  ? 169 PRO B CA  1 
ATOM   4282 C  C   . PRO B 1 167 ? 59.250 120.189 -94.101  1.00 21.15  ? 169 PRO B C   1 
ATOM   4283 O  O   . PRO B 1 167 ? 58.359 119.398 -94.229  1.00 20.81  ? 169 PRO B O   1 
ATOM   4284 C  CB  . PRO B 1 167 ? 58.962 122.545 -95.075  1.00 21.65  ? 169 PRO B CB  1 
ATOM   4285 C  CG  . PRO B 1 167 ? 57.574 122.404 -95.641  1.00 21.05  ? 169 PRO B CG  1 
ATOM   4286 C  CD  . PRO B 1 167 ? 57.764 121.523 -96.858  1.00 21.76  ? 169 PRO B CD  1 
ATOM   4287 N  N   . THR B 1 168 ? 60.028 120.262 -93.034  1.00 20.88  ? 170 THR B N   1 
ATOM   4288 C  CA  . THR B 1 168 ? 59.722 119.503 -91.788  1.00 21.13  ? 170 THR B CA  1 
ATOM   4289 C  C   . THR B 1 168 ? 59.701 120.450 -90.595  1.00 20.16  ? 170 THR B C   1 
ATOM   4290 O  O   . THR B 1 168 ? 60.365 121.529 -90.634  1.00 19.56  ? 170 THR B O   1 
ATOM   4291 C  CB  . THR B 1 168 ? 60.705 118.355 -91.519  1.00 22.24  ? 170 THR B CB  1 
ATOM   4292 O  OG1 . THR B 1 168 ? 61.963 118.957 -91.200  1.00 22.72  ? 170 THR B OG1 1 
ATOM   4293 C  CG2 . THR B 1 168 ? 60.830 117.385 -92.683  1.00 23.60  ? 170 THR B CG2 1 
ATOM   4294 N  N   . LEU B 1 169 ? 58.942 120.061 -89.571  1.00 19.52  ? 171 LEU B N   1 
ATOM   4295 C  CA  . LEU B 1 169 ? 58.848 120.861 -88.331  1.00 18.32  ? 171 LEU B CA  1 
ATOM   4296 C  C   . LEU B 1 169 ? 59.078 119.932 -87.132  1.00 18.49  ? 171 LEU B C   1 
ATOM   4297 O  O   . LEU B 1 169 ? 58.490 118.847 -87.058  1.00 17.39  ? 171 LEU B O   1 
ATOM   4298 C  CB  . LEU B 1 169 ? 57.523 121.615 -88.294  1.00 17.35  ? 171 LEU B CB  1 
ATOM   4299 C  CG  . LEU B 1 169 ? 57.497 122.812 -87.336  1.00 17.25  ? 171 LEU B CG  1 
ATOM   4300 C  CD1 . LEU B 1 169 ? 58.216 123.997 -87.924  1.00 17.04  ? 171 LEU B CD1 1 
ATOM   4301 C  CD2 . LEU B 1 169 ? 56.084 123.242 -86.991  1.00 16.99  ? 171 LEU B CD2 1 
ATOM   4302 N  N   . THR B 1 170 ? 60.038 120.315 -86.313  1.00 19.21  ? 172 THR B N   1 
ATOM   4303 C  CA  . THR B 1 170 ? 60.425 119.592 -85.082  1.00 20.77  ? 172 THR B CA  1 
ATOM   4304 C  C   . THR B 1 170 ? 60.253 120.553 -83.908  1.00 20.50  ? 172 THR B C   1 
ATOM   4305 O  O   . THR B 1 170 ? 60.769 121.716 -83.964  1.00 22.18  ? 172 THR B O   1 
ATOM   4306 C  CB  . THR B 1 170 ? 61.831 119.012 -85.215  1.00 22.52  ? 172 THR B CB  1 
ATOM   4307 O  OG1 . THR B 1 170 ? 61.740 118.083 -86.299  1.00 25.73  ? 172 THR B OG1 1 
ATOM   4308 C  CG2 . THR B 1 170 ? 62.338 118.318 -83.976  1.00 24.16  ? 172 THR B CG2 1 
ATOM   4309 N  N   . LYS B 1 171 ? 59.532 120.110 -82.893  1.00 19.11  ? 173 LYS B N   1 
ATOM   4310 C  CA  . LYS B 1 171 ? 59.445 120.882 -81.644  1.00 18.82  ? 173 LYS B CA  1 
ATOM   4311 C  C   . LYS B 1 171 ? 60.114 120.091 -80.525  1.00 19.57  ? 173 LYS B C   1 
ATOM   4312 O  O   . LYS B 1 171 ? 59.855 118.857 -80.386  1.00 18.77  ? 173 LYS B O   1 
ATOM   4313 C  CB  . LYS B 1 171 ? 58.004 121.203 -81.265  1.00 17.83  ? 173 LYS B CB  1 
ATOM   4314 C  CG  . LYS B 1 171 ? 57.918 121.994 -79.979  1.00 17.28  ? 173 LYS B CG  1 
ATOM   4315 C  CD  . LYS B 1 171 ? 56.524 122.341 -79.568  1.00 16.88  ? 173 LYS B CD  1 
ATOM   4316 C  CE  . LYS B 1 171 ? 56.509 123.399 -78.486  1.00 16.87  ? 173 LYS B CE  1 
ATOM   4317 N  NZ  . LYS B 1 171 ? 55.143 123.583 -77.934  1.00 16.44  ? 173 LYS B NZ  1 
ATOM   4318 N  N   . GLN B 1 172 ? 60.944 120.796 -79.757  1.00 21.20  ? 174 GLN B N   1 
ATOM   4319 C  CA  . GLN B 1 172 ? 61.582 120.220 -78.554  1.00 22.80  ? 174 GLN B CA  1 
ATOM   4320 C  C   . GLN B 1 172 ? 61.647 121.193 -77.373  1.00 22.75  ? 174 GLN B C   1 
ATOM   4321 O  O   . GLN B 1 172 ? 61.509 122.429 -77.537  1.00 21.50  ? 174 GLN B O   1 
ATOM   4322 C  CB  . GLN B 1 172 ? 62.963 119.724 -78.931  1.00 25.04  ? 174 GLN B CB  1 
ATOM   4323 C  CG  . GLN B 1 172 ? 62.932 118.496 -79.838  1.00 26.50  ? 174 GLN B CG  1 
ATOM   4324 C  CD  . GLN B 1 172 ? 64.333 117.972 -80.013  1.00 28.20  ? 174 GLN B CD  1 
ATOM   4325 O  OE1 . GLN B 1 172 ? 65.219 118.706 -80.481  1.00 28.20  ? 174 GLN B OE1 1 
ATOM   4326 N  NE2 . GLN B 1 172 ? 64.536 116.738 -79.557  1.00 29.25  ? 174 GLN B NE2 1 
ATOM   4327 N  N   . VAL B 1 173 ? 61.834 120.602 -76.198  1.00 23.38  ? 175 VAL B N   1 
ATOM   4328 C  CA  . VAL B 1 173 ? 61.900 121.362 -74.932  1.00 24.01  ? 175 VAL B CA  1 
ATOM   4329 C  C   . VAL B 1 173 ? 63.293 121.119 -74.415  1.00 26.24  ? 175 VAL B C   1 
ATOM   4330 O  O   . VAL B 1 173 ? 63.761 119.978 -74.498  1.00 25.40  ? 175 VAL B O   1 
ATOM   4331 C  CB  . VAL B 1 173 ? 60.804 120.943 -73.928  1.00 23.67  ? 175 VAL B CB  1 
ATOM   4332 C  CG1 . VAL B 1 173 ? 60.846 119.462 -73.565  1.00 24.06  ? 175 VAL B CG1 1 
ATOM   4333 C  CG2 . VAL B 1 173 ? 60.846 121.788 -72.666  1.00 23.45  ? 175 VAL B CG2 1 
ATOM   4334 N  N   . ARG B 1 174 ? 63.908 122.163 -73.894  1.00 30.20  ? 176 ARG B N   1 
ATOM   4335 C  CA  . ARG B 1 174 ? 65.233 122.005 -73.274  1.00 35.06  ? 176 ARG B CA  1 
ATOM   4336 C  C   . ARG B 1 174 ? 65.074 121.287 -71.940  1.00 37.62  ? 176 ARG B C   1 
ATOM   4337 O  O   . ARG B 1 174 ? 64.272 121.747 -71.109  1.00 36.19  ? 176 ARG B O   1 
ATOM   4338 C  CB  . ARG B 1 174 ? 65.941 123.336 -73.094  1.00 38.04  ? 176 ARG B CB  1 
ATOM   4339 C  CG  . ARG B 1 174 ? 67.438 123.148 -73.253  1.00 41.43  ? 176 ARG B CG  1 
ATOM   4340 C  CD  . ARG B 1 174 ? 68.195 124.439 -73.121  1.00 44.51  ? 176 ARG B CD  1 
ATOM   4341 N  NE  . ARG B 1 174 ? 68.132 124.871 -71.744  1.00 46.81  ? 176 ARG B NE  1 
ATOM   4342 C  CZ  . ARG B 1 174 ? 68.598 126.028 -71.321  1.00 49.53  ? 176 ARG B CZ  1 
ATOM   4343 N  NH1 . ARG B 1 174 ? 69.177 126.863 -72.176  1.00 51.42  ? 176 ARG B NH1 1 
ATOM   4344 N  NH2 . ARG B 1 174 ? 68.487 126.334 -70.044  1.00 50.02  ? 176 ARG B NH2 1 
ATOM   4345 N  N   . ALA B 1 175 ? 65.803 120.179 -71.772  1.00 40.53  ? 177 ALA B N   1 
ATOM   4346 C  CA  . ALA B 1 175 ? 65.654 119.254 -70.628  1.00 41.91  ? 177 ALA B CA  1 
ATOM   4347 C  C   . ALA B 1 175 ? 66.043 119.985 -69.347  1.00 44.52  ? 177 ALA B C   1 
ATOM   4348 O  O   . ALA B 1 175 ? 66.788 120.999 -69.382  1.00 42.97  ? 177 ALA B O   1 
ATOM   4349 C  CB  . ALA B 1 175 ? 66.462 117.994 -70.818  1.00 42.46  ? 177 ALA B CB  1 
ATOM   4350 N  N   . ASN B 1 176 ? 65.531 119.474 -68.245  1.00 47.62  ? 178 ASN B N   1 
ATOM   4351 C  CA  . ASN B 1 176 ? 65.884 119.977 -66.897  1.00 57.91  ? 178 ASN B CA  1 
ATOM   4352 C  C   . ASN B 1 176 ? 67.425 119.878 -66.729  1.00 63.57  ? 178 ASN B C   1 
ATOM   4353 O  O   . ASN B 1 176 ? 67.946 118.719 -66.593  1.00 64.65  ? 178 ASN B O   1 
ATOM   4354 C  CB  . ASN B 1 176 ? 65.021 119.257 -65.842  1.00 58.24  ? 178 ASN B CB  1 
ATOM   4355 C  CG  . ASN B 1 176 ? 64.919 119.983 -64.516  1.00 58.80  ? 178 ASN B CG  1 
ATOM   4356 O  OD1 . ASN B 1 176 ? 65.620 120.970 -64.255  1.00 59.91  ? 178 ASN B OD1 1 
ATOM   4357 N  ND2 . ASN B 1 176 ? 64.035 119.485 -63.669  1.00 55.57  ? 178 ASN B ND2 1 
ATOM   4358 N  N   . GLY B 1 177 ? 68.119 121.038 -66.747  1.00 64.70  ? 179 GLY B N   1 
ATOM   4359 C  CA  . GLY B 1 177 ? 69.551 121.207 -66.412  1.00 66.56  ? 179 GLY B CA  1 
ATOM   4360 C  C   . GLY B 1 177 ? 70.442 120.242 -67.173  1.00 69.07  ? 179 GLY B C   1 
ATOM   4361 O  O   . GLY B 1 177 ? 71.164 119.492 -66.544  1.00 72.27  ? 179 GLY B O   1 
ATOM   4362 N  N   . SER B 1 178 ? 70.381 120.255 -68.496  1.00 69.53  ? 180 SER B N   1 
ATOM   4363 C  CA  . SER B 1 178 ? 71.050 119.279 -69.394  1.00 70.73  ? 180 SER B CA  1 
ATOM   4364 C  C   . SER B 1 178 ? 71.487 120.005 -70.662  1.00 72.21  ? 180 SER B C   1 
ATOM   4365 O  O   . SER B 1 178 ? 72.196 119.402 -71.468  1.00 80.56  ? 180 SER B O   1 
ATOM   4366 C  CB  . SER B 1 178 ? 70.090 118.145 -69.701  1.00 71.82  ? 180 SER B CB  1 
ATOM   4367 O  OG  . SER B 1 178 ? 70.648 117.153 -70.542  1.00 69.47  ? 180 SER B OG  1 
ATOM   4368 N  N   . GLN B 1 179 ? 71.026 121.248 -70.847  1.00 72.37  ? 181 GLN B N   1 
ATOM   4369 C  CA  . GLN B 1 179 ? 71.235 122.086 -72.065  1.00 72.44  ? 181 GLN B CA  1 
ATOM   4370 C  C   . GLN B 1 179 ? 70.798 121.317 -73.315  1.00 65.70  ? 181 GLN B C   1 
ATOM   4371 O  O   . GLN B 1 179 ? 71.025 121.855 -74.401  1.00 64.31  ? 181 GLN B O   1 
ATOM   4372 C  CB  . GLN B 1 179 ? 72.705 122.520 -72.194  1.00 79.05  ? 181 GLN B CB  1 
ATOM   4373 C  CG  . GLN B 1 179 ? 73.033 123.814 -71.458  1.00 83.81  ? 181 GLN B CG  1 
ATOM   4374 C  CD  . GLN B 1 179 ? 72.516 123.813 -70.038  1.00 87.00  ? 181 GLN B CD  1 
ATOM   4375 O  OE1 . GLN B 1 179 ? 71.434 124.324 -69.752  1.00 88.53  ? 181 GLN B OE1 1 
ATOM   4376 N  NE2 . GLN B 1 179 ? 73.275 123.210 -69.132  1.00 91.11  ? 181 GLN B NE2 1 
ATOM   4377 N  N   . ASN B 1 180 ? 70.183 120.136 -73.163  1.00 61.12  ? 182 ASN B N   1 
ATOM   4378 C  CA  . ASN B 1 180 ? 69.836 119.243 -74.298  1.00 57.53  ? 182 ASN B CA  1 
ATOM   4379 C  C   . ASN B 1 180 ? 68.360 119.383 -74.621  1.00 50.06  ? 182 ASN B C   1 
ATOM   4380 O  O   . ASN B 1 180 ? 67.566 119.495 -73.703  1.00 51.66  ? 182 ASN B O   1 
ATOM   4381 C  CB  . ASN B 1 180 ? 70.199 117.784 -74.039  1.00 61.26  ? 182 ASN B CB  1 
ATOM   4382 C  CG  . ASN B 1 180 ? 71.617 117.491 -74.490  1.00 68.04  ? 182 ASN B CG  1 
ATOM   4383 O  OD1 . ASN B 1 180 ? 72.433 118.409 -74.622  1.00 73.39  ? 182 ASN B OD1 1 
ATOM   4384 N  ND2 . ASN B 1 180 ? 71.915 116.224 -74.751  1.00 70.18  ? 182 ASN B ND2 1 
ATOM   4385 N  N   . TYR B 1 181 ? 68.023 119.387 -75.897  1.00 43.22  ? 183 TYR B N   1 
ATOM   4386 C  CA  . TYR B 1 181 ? 66.621 119.402 -76.346  1.00 38.19  ? 183 TYR B CA  1 
ATOM   4387 C  C   . TYR B 1 181 ? 66.131 117.961 -76.467  1.00 37.16  ? 183 TYR B C   1 
ATOM   4388 O  O   . TYR B 1 181 ? 66.930 117.063 -76.804  1.00 38.50  ? 183 TYR B O   1 
ATOM   4389 C  CB  . TYR B 1 181 ? 66.499 120.222 -77.610  1.00 35.96  ? 183 TYR B CB  1 
ATOM   4390 C  CG  . TYR B 1 181 ? 66.643 121.678 -77.312  1.00 35.77  ? 183 TYR B CG  1 
ATOM   4391 C  CD1 . TYR B 1 181 ? 65.610 122.387 -76.769  1.00 34.76  ? 183 TYR B CD1 1 
ATOM   4392 C  CD2 . TYR B 1 181 ? 67.817 122.345 -77.567  1.00 37.89  ? 183 TYR B CD2 1 
ATOM   4393 C  CE1 . TYR B 1 181 ? 65.726 123.741 -76.523  1.00 35.70  ? 183 TYR B CE1 1 
ATOM   4394 C  CE2 . TYR B 1 181 ? 67.957 123.699 -77.331  1.00 38.19  ? 183 TYR B CE2 1 
ATOM   4395 C  CZ  . TYR B 1 181 ? 66.903 124.399 -76.795  1.00 36.88  ? 183 TYR B CZ  1 
ATOM   4396 O  OH  . TYR B 1 181 ? 67.023 125.728 -76.551  1.00 38.80  ? 183 TYR B OH  1 
ATOM   4397 N  N   . THR B 1 182 ? 64.849 117.758 -76.133  1.00 33.47  ? 184 THR B N   1 
ATOM   4398 C  CA  . THR B 1 182 ? 64.213 116.432 -75.998  1.00 30.81  ? 184 THR B CA  1 
ATOM   4399 C  C   . THR B 1 182 ? 62.731 116.593 -76.330  1.00 26.96  ? 184 THR B C   1 
ATOM   4400 O  O   . THR B 1 182 ? 62.247 117.759 -76.374  1.00 25.32  ? 184 THR B O   1 
ATOM   4401 C  CB  . THR B 1 182 ? 64.515 115.888 -74.587  1.00 32.46  ? 184 THR B CB  1 
ATOM   4402 O  OG1 . THR B 1 182 ? 63.881 114.615 -74.437  1.00 34.08  ? 184 THR B OG1 1 
ATOM   4403 C  CG2 . THR B 1 182 ? 64.016 116.789 -73.478  1.00 31.61  ? 184 THR B CG2 1 
ATOM   4404 N  N   . ALA B 1 183 ? 62.037 115.471 -76.508  1.00 25.28  ? 185 ALA B N   1 
ATOM   4405 C  CA  . ALA B 1 183 ? 60.576 115.431 -76.736  1.00 24.05  ? 185 ALA B CA  1 
ATOM   4406 C  C   . ALA B 1 183 ? 59.837 115.866 -75.468  1.00 24.39  ? 185 ALA B C   1 
ATOM   4407 O  O   . ALA B 1 183 ? 58.701 116.401 -75.606  1.00 23.92  ? 185 ALA B O   1 
ATOM   4408 C  CB  . ALA B 1 183 ? 60.136 114.053 -77.164  1.00 23.91  ? 185 ALA B CB  1 
ATOM   4409 N  N   . ALA B 1 184 ? 60.391 115.594 -74.273  1.00 25.80  ? 186 ALA B N   1 
ATOM   4410 C  CA  . ALA B 1 184 ? 59.675 115.798 -72.982  1.00 25.33  ? 186 ALA B CA  1 
ATOM   4411 C  C   . ALA B 1 184 ? 60.603 115.760 -71.764  1.00 26.59  ? 186 ALA B C   1 
ATOM   4412 O  O   . ALA B 1 184 ? 61.642 115.064 -71.747  1.00 28.03  ? 186 ALA B O   1 
ATOM   4413 C  CB  . ALA B 1 184 ? 58.571 114.783 -72.850  1.00 25.36  ? 186 ALA B CB  1 
ATOM   4414 N  N   . THR B 1 185 ? 60.225 116.494 -70.729  1.00 26.94  ? 187 THR B N   1 
ATOM   4415 C  CA  . THR B 1 185 ? 61.001 116.552 -69.472  1.00 27.17  ? 187 THR B CA  1 
ATOM   4416 C  C   . THR B 1 185 ? 60.060 116.911 -68.310  1.00 25.38  ? 187 THR B C   1 
ATOM   4417 O  O   . THR B 1 185 ? 58.854 116.964 -68.502  1.00 23.93  ? 187 THR B O   1 
ATOM   4418 C  CB  . THR B 1 185 ? 62.142 117.537 -69.718  1.00 28.83  ? 187 THR B CB  1 
ATOM   4419 O  OG1 . THR B 1 185 ? 63.134 117.402 -68.701  1.00 31.02  ? 187 THR B OG1 1 
ATOM   4420 C  CG2 . THR B 1 185 ? 61.649 118.967 -69.738  1.00 29.00  ? 187 THR B CG2 1 
ATOM   4421 N  N   . ASP B 1 186 ? 60.575 117.112 -67.102  1.00 26.11  ? 188 ASP B N   1 
ATOM   4422 C  CA  . ASP B 1 186 ? 59.744 117.548 -65.949  1.00 24.28  ? 188 ASP B CA  1 
ATOM   4423 C  C   . ASP B 1 186 ? 60.351 118.830 -65.428  1.00 24.43  ? 188 ASP B C   1 
ATOM   4424 O  O   . ASP B 1 186 ? 61.586 119.009 -65.476  1.00 26.53  ? 188 ASP B O   1 
ATOM   4425 C  CB  . ASP B 1 186 ? 59.506 116.437 -64.942  1.00 24.41  ? 188 ASP B CB  1 
ATOM   4426 C  CG  . ASP B 1 186 ? 60.745 115.749 -64.400  1.00 25.78  ? 188 ASP B CG  1 
ATOM   4427 O  OD1 . ASP B 1 186 ? 61.775 116.458 -64.166  1.00 26.84  ? 188 ASP B OD1 1 
ATOM   4428 O  OD2 . ASP B 1 186 ? 60.668 114.510 -64.184  1.00 25.70  ? 188 ASP B OD2 1 
ATOM   4429 N  N   . TYR B 1 187 ? 59.491 119.735 -65.030  1.00 24.45  ? 189 TYR B N   1 
ATOM   4430 C  CA  . TYR B 1 187 ? 59.910 120.978 -64.365  1.00 26.77  ? 189 TYR B CA  1 
ATOM   4431 C  C   . TYR B 1 187 ? 59.003 121.199 -63.162  1.00 27.13  ? 189 TYR B C   1 
ATOM   4432 O  O   . TYR B 1 187 ? 58.051 120.426 -62.940  1.00 27.35  ? 189 TYR B O   1 
ATOM   4433 C  CB  . TYR B 1 187 ? 59.887 122.171 -65.308  1.00 27.72  ? 189 TYR B CB  1 
ATOM   4434 C  CG  . TYR B 1 187 ? 61.065 122.330 -66.234  1.00 29.87  ? 189 TYR B CG  1 
ATOM   4435 C  CD1 . TYR B 1 187 ? 61.091 121.720 -67.483  1.00 29.33  ? 189 TYR B CD1 1 
ATOM   4436 C  CD2 . TYR B 1 187 ? 62.099 123.208 -65.923  1.00 31.45  ? 189 TYR B CD2 1 
ATOM   4437 C  CE1 . TYR B 1 187 ? 62.144 121.916 -68.364  1.00 30.17  ? 189 TYR B CE1 1 
ATOM   4438 C  CE2 . TYR B 1 187 ? 63.154 123.424 -66.804  1.00 32.00  ? 189 TYR B CE2 1 
ATOM   4439 C  CZ  . TYR B 1 187 ? 63.181 122.775 -68.026  1.00 31.38  ? 189 TYR B CZ  1 
ATOM   4440 O  OH  . TYR B 1 187 ? 64.232 122.990 -68.877  1.00 32.12  ? 189 TYR B OH  1 
ATOM   4441 N  N   . ARG B 1 188 ? 59.330 122.225 -62.389  1.00 27.97  ? 190 ARG B N   1 
ATOM   4442 C  CA  . ARG B 1 188 ? 58.478 122.703 -61.279  1.00 27.79  ? 190 ARG B CA  1 
ATOM   4443 C  C   . ARG B 1 188 ? 57.640 123.875 -61.785  1.00 26.30  ? 190 ARG B C   1 
ATOM   4444 O  O   . ARG B 1 188 ? 58.038 124.546 -62.774  1.00 24.93  ? 190 ARG B O   1 
ATOM   4445 C  CB  . ARG B 1 188 ? 59.329 123.092 -60.060  1.00 30.19  ? 190 ARG B CB  1 
ATOM   4446 C  CG  . ARG B 1 188 ? 60.143 121.944 -59.480  1.00 31.32  ? 190 ARG B CG  1 
ATOM   4447 C  CD  . ARG B 1 188 ? 60.676 122.260 -58.112  1.00 32.73  ? 190 ARG B CD  1 
ATOM   4448 N  NE  . ARG B 1 188 ? 61.507 123.453 -58.112  1.00 34.95  ? 190 ARG B NE  1 
ATOM   4449 C  CZ  . ARG B 1 188 ? 61.149 124.644 -57.622  1.00 35.83  ? 190 ARG B CZ  1 
ATOM   4450 N  NH1 . ARG B 1 188 ? 59.948 124.839 -57.110  1.00 35.10  ? 190 ARG B NH1 1 
ATOM   4451 N  NH2 . ARG B 1 188 ? 61.987 125.664 -57.656  1.00 37.31  ? 190 ARG B NH2 1 
ATOM   4452 N  N   . ILE B 1 189 ? 56.506 124.090 -61.127  1.00 24.95  ? 191 ILE B N   1 
ATOM   4453 C  CA  . ILE B 1 189 ? 55.600 125.224 -61.425  1.00 25.09  ? 191 ILE B CA  1 
ATOM   4454 C  C   . ILE B 1 189 ? 56.368 126.517 -61.174  1.00 26.06  ? 191 ILE B C   1 
ATOM   4455 O  O   . ILE B 1 189 ? 57.152 126.545 -60.261  1.00 26.32  ? 191 ILE B O   1 
ATOM   4456 C  CB  . ILE B 1 189 ? 54.296 125.082 -60.629  1.00 25.09  ? 191 ILE B CB  1 
ATOM   4457 C  CG1 . ILE B 1 189 ? 53.490 123.921 -61.210  1.00 24.88  ? 191 ILE B CG1 1 
ATOM   4458 C  CG2 . ILE B 1 189 ? 53.512 126.380 -60.626  1.00 25.16  ? 191 ILE B CG2 1 
ATOM   4459 C  CD1 . ILE B 1 189 ? 52.219 123.607 -60.486  1.00 24.69  ? 191 ILE B CD1 1 
ATOM   4460 N  N   . GLY B 1 190 ? 56.223 127.487 -62.068  1.00 27.57  ? 192 GLY B N   1 
ATOM   4461 C  CA  . GLY B 1 190 ? 56.838 128.820 -61.956  1.00 29.98  ? 192 GLY B CA  1 
ATOM   4462 C  C   . GLY B 1 190 ? 58.226 128.895 -62.566  1.00 32.77  ? 192 GLY B C   1 
ATOM   4463 O  O   . GLY B 1 190 ? 58.707 130.026 -62.732  1.00 34.77  ? 192 GLY B O   1 
ATOM   4464 N  N   . GLN B 1 191 ? 58.878 127.758 -62.842  1.00 34.42  ? 193 GLN B N   1 
ATOM   4465 C  CA  . GLN B 1 191 ? 60.192 127.717 -63.536  1.00 36.11  ? 193 GLN B CA  1 
ATOM   4466 C  C   . GLN B 1 191 ? 59.974 128.013 -65.022  1.00 34.47  ? 193 GLN B C   1 
ATOM   4467 O  O   . GLN B 1 191 ? 59.026 127.395 -65.632  1.00 32.62  ? 193 GLN B O   1 
ATOM   4468 C  CB  . GLN B 1 191 ? 60.866 126.357 -63.361  1.00 39.94  ? 193 GLN B CB  1 
ATOM   4469 C  CG  . GLN B 1 191 ? 61.517 126.168 -61.991  1.00 44.57  ? 193 GLN B CG  1 
ATOM   4470 C  CD  . GLN B 1 191 ? 62.247 124.841 -61.829  1.00 49.36  ? 193 GLN B CD  1 
ATOM   4471 O  OE1 . GLN B 1 191 ? 62.070 123.867 -62.583  1.00 49.03  ? 193 GLN B OE1 1 
ATOM   4472 N  NE2 . GLN B 1 191 ? 63.070 124.768 -60.789  1.00 56.63  ? 193 GLN B NE2 1 
ATOM   4473 N  N   . ASN B 1 192 ? 60.786 128.933 -65.566  1.00 33.85  ? 194 ASN B N   1 
ATOM   4474 C  CA  . ASN B 1 192 ? 60.821 129.295 -67.019  1.00 33.25  ? 194 ASN B CA  1 
ATOM   4475 C  C   . ASN B 1 192 ? 61.512 128.170 -67.792  1.00 30.35  ? 194 ASN B C   1 
ATOM   4476 O  O   . ASN B 1 192 ? 62.505 127.628 -67.314  1.00 29.60  ? 194 ASN B O   1 
ATOM   4477 C  CB  . ASN B 1 192 ? 61.443 130.667 -67.304  1.00 34.92  ? 194 ASN B CB  1 
ATOM   4478 C  CG  . ASN B 1 192 ? 60.594 131.816 -66.785  1.00 37.09  ? 194 ASN B CG  1 
ATOM   4479 O  OD1 . ASN B 1 192 ? 59.384 131.834 -66.970  1.00 37.65  ? 194 ASN B OD1 1 
ATOM   4480 N  ND2 . ASN B 1 192 ? 61.201 132.783 -66.117  1.00 39.72  ? 194 ASN B ND2 1 
ATOM   4481 N  N   . ILE B 1 193 ? 60.909 127.765 -68.900  1.00 28.35  ? 195 ILE B N   1 
ATOM   4482 C  CA  . ILE B 1 193 ? 61.343 126.569 -69.674  1.00 27.93  ? 195 ILE B CA  1 
ATOM   4483 C  C   . ILE B 1 193 ? 61.636 127.051 -71.096  1.00 28.53  ? 195 ILE B C   1 
ATOM   4484 O  O   . ILE B 1 193 ? 60.890 127.891 -71.623  1.00 27.45  ? 195 ILE B O   1 
ATOM   4485 C  CB  . ILE B 1 193 ? 60.288 125.439 -69.624  1.00 26.90  ? 195 ILE B CB  1 
ATOM   4486 C  CG1 . ILE B 1 193 ? 59.918 125.074 -68.173  1.00 26.51  ? 195 ILE B CG1 1 
ATOM   4487 C  CG2 . ILE B 1 193 ? 60.749 124.220 -70.413  1.00 26.17  ? 195 ILE B CG2 1 
ATOM   4488 C  CD1 . ILE B 1 193 ? 58.544 124.486 -68.039  1.00 25.42  ? 195 ILE B CD1 1 
ATOM   4489 N  N   . LEU B 1 194 ? 62.693 126.543 -71.702  1.00 29.31  ? 196 LEU B N   1 
ATOM   4490 C  CA  . LEU B 1 194 ? 63.086 127.000 -73.044  1.00 30.06  ? 196 LEU B CA  1 
ATOM   4491 C  C   . LEU B 1 194 ? 62.581 125.991 -74.064  1.00 27.76  ? 196 LEU B C   1 
ATOM   4492 O  O   . LEU B 1 194 ? 62.873 124.788 -73.930  1.00 26.99  ? 196 LEU B O   1 
ATOM   4493 C  CB  . LEU B 1 194 ? 64.599 127.196 -73.125  1.00 33.64  ? 196 LEU B CB  1 
ATOM   4494 C  CG  . LEU B 1 194 ? 65.029 128.102 -74.279  1.00 36.87  ? 196 LEU B CG  1 
ATOM   4495 C  CD1 . LEU B 1 194 ? 65.237 129.539 -73.786  1.00 37.71  ? 196 LEU B CD1 1 
ATOM   4496 C  CD2 . LEU B 1 194 ? 66.277 127.551 -74.952  1.00 38.52  ? 196 LEU B CD2 1 
ATOM   4497 N  N   . PHE B 1 195 ? 61.854 126.507 -75.053  1.00 25.86  ? 197 PHE B N   1 
ATOM   4498 C  CA  . PHE B 1 195 ? 61.329 125.704 -76.176  1.00 24.25  ? 197 PHE B CA  1 
ATOM   4499 C  C   . PHE B 1 195 ? 61.976 126.141 -77.487  1.00 23.96  ? 197 PHE B C   1 
ATOM   4500 O  O   . PHE B 1 195 ? 62.421 127.306 -77.634  1.00 22.99  ? 197 PHE B O   1 
ATOM   4501 C  CB  . PHE B 1 195 ? 59.821 125.817 -76.229  1.00 22.35  ? 197 PHE B CB  1 
ATOM   4502 C  CG  . PHE B 1 195 ? 59.147 125.122 -75.081  1.00 20.97  ? 197 PHE B CG  1 
ATOM   4503 C  CD1 . PHE B 1 195 ? 58.770 123.793 -75.188  1.00 19.99  ? 197 PHE B CD1 1 
ATOM   4504 C  CD2 . PHE B 1 195 ? 58.830 125.820 -73.927  1.00 20.54  ? 197 PHE B CD2 1 
ATOM   4505 C  CE1 . PHE B 1 195 ? 58.116 123.164 -74.141  1.00 19.63  ? 197 PHE B CE1 1 
ATOM   4506 C  CE2 . PHE B 1 195 ? 58.173 125.187 -72.881  1.00 20.03  ? 197 PHE B CE2 1 
ATOM   4507 C  CZ  . PHE B 1 195 ? 57.820 123.860 -72.990  1.00 19.45  ? 197 PHE B CZ  1 
ATOM   4508 N  N   . GLN B 1 196 ? 62.048 125.180 -78.399  1.00 24.49  ? 198 GLN B N   1 
ATOM   4509 C  CA  . GLN B 1 196 ? 62.729 125.353 -79.709  1.00 26.34  ? 198 GLN B CA  1 
ATOM   4510 C  C   . GLN B 1 196 ? 61.904 124.655 -80.791  1.00 23.82  ? 198 GLN B C   1 
ATOM   4511 O  O   . GLN B 1 196 ? 61.565 123.475 -80.595  1.00 23.20  ? 198 GLN B O   1 
ATOM   4512 C  CB  . GLN B 1 196 ? 64.157 124.818 -79.614  1.00 29.30  ? 198 GLN B CB  1 
ATOM   4513 C  CG  . GLN B 1 196 ? 65.016 125.147 -80.826  1.00 32.78  ? 198 GLN B CG  1 
ATOM   4514 C  CD  . GLN B 1 196 ? 66.455 124.681 -80.718  1.00 35.94  ? 198 GLN B CD  1 
ATOM   4515 O  OE1 . GLN B 1 196 ? 67.381 125.489 -80.708  1.00 38.68  ? 198 GLN B OE1 1 
ATOM   4516 N  NE2 . GLN B 1 196 ? 66.655 123.370 -80.632  1.00 36.41  ? 198 GLN B NE2 1 
ATOM   4517 N  N   . ILE B 1 197 ? 61.549 125.384 -81.845  1.00 21.89  ? 199 ILE B N   1 
ATOM   4518 C  CA  . ILE B 1 197 ? 60.906 124.789 -83.043  1.00 21.15  ? 199 ILE B CA  1 
ATOM   4519 C  C   . ILE B 1 197 ? 61.845 124.997 -84.231  1.00 21.78  ? 199 ILE B C   1 
ATOM   4520 O  O   . ILE B 1 197 ? 62.284 126.120 -84.488  1.00 21.25  ? 199 ILE B O   1 
ATOM   4521 C  CB  . ILE B 1 197 ? 59.521 125.386 -83.305  1.00 20.14  ? 199 ILE B CB  1 
ATOM   4522 C  CG1 . ILE B 1 197 ? 58.543 125.080 -82.175  1.00 19.43  ? 199 ILE B CG1 1 
ATOM   4523 C  CG2 . ILE B 1 197 ? 58.980 124.897 -84.633  1.00 20.45  ? 199 ILE B CG2 1 
ATOM   4524 C  CD1 . ILE B 1 197 ? 57.401 126.062 -82.091  1.00 18.80  ? 199 ILE B CD1 1 
ATOM   4525 N  N   . THR B 1 198 ? 62.143 123.916 -84.925  1.00 22.64  ? 200 THR B N   1 
ATOM   4526 C  CA  . THR B 1 198 ? 63.084 123.916 -86.063  1.00 23.71  ? 200 THR B CA  1 
ATOM   4527 C  C   . THR B 1 198 ? 62.364 123.519 -87.344  1.00 23.15  ? 200 THR B C   1 
ATOM   4528 O  O   . THR B 1 198 ? 61.810 122.394 -87.398  1.00 22.52  ? 200 THR B O   1 
ATOM   4529 C  CB  . THR B 1 198 ? 64.218 122.926 -85.821  1.00 25.22  ? 200 THR B CB  1 
ATOM   4530 O  OG1 . THR B 1 198 ? 64.830 123.311 -84.593  1.00 24.83  ? 200 THR B OG1 1 
ATOM   4531 C  CG2 . THR B 1 198 ? 65.205 122.928 -86.965  1.00 25.64  ? 200 THR B CG2 1 
ATOM   4532 N  N   . ALA B 1 199 ? 62.362 124.420 -88.324  1.00 23.09  ? 201 ALA B N   1 
ATOM   4533 C  CA  . ALA B 1 199 ? 61.792 124.180 -89.667  1.00 22.77  ? 201 ALA B CA  1 
ATOM   4534 C  C   . ALA B 1 199 ? 62.955 123.960 -90.616  1.00 23.58  ? 201 ALA B C   1 
ATOM   4535 O  O   . ALA B 1 199 ? 63.905 124.797 -90.623  1.00 24.54  ? 201 ALA B O   1 
ATOM   4536 C  CB  . ALA B 1 199 ? 60.927 125.335 -90.110  1.00 22.12  ? 201 ALA B CB  1 
ATOM   4537 N  N   . THR B 1 200 ? 62.905 122.872 -91.364  1.00 23.59  ? 202 THR B N   1 
ATOM   4538 C  CA  . THR B 1 200 ? 63.786 122.684 -92.526  1.00 24.20  ? 202 THR B CA  1 
ATOM   4539 C  C   . THR B 1 200 ? 62.994 123.093 -93.765  1.00 24.39  ? 202 THR B C   1 
ATOM   4540 O  O   . THR B 1 200 ? 61.750 123.057 -93.719  1.00 24.27  ? 202 THR B O   1 
ATOM   4541 C  CB  . THR B 1 200 ? 64.242 121.237 -92.663  1.00 24.80  ? 202 THR B CB  1 
ATOM   4542 O  OG1 . THR B 1 200 ? 63.085 120.482 -93.006  1.00 24.88  ? 202 THR B OG1 1 
ATOM   4543 C  CG2 . THR B 1 200 ? 64.892 120.688 -91.422  1.00 26.00  ? 202 THR B CG2 1 
ATOM   4544 N  N   . LEU B 1 201 ? 63.683 123.439 -94.842  1.00 25.40  ? 203 LEU B N   1 
ATOM   4545 C  CA  . LEU B 1 201 ? 63.021 123.896 -96.086  1.00 25.38  ? 203 LEU B CA  1 
ATOM   4546 C  C   . LEU B 1 201 ? 63.109 122.768 -97.093  1.00 25.12  ? 203 LEU B C   1 
ATOM   4547 O  O   . LEU B 1 201 ? 63.964 121.914 -96.986  1.00 26.22  ? 203 LEU B O   1 
ATOM   4548 C  CB  . LEU B 1 201 ? 63.693 125.181 -96.566  1.00 26.53  ? 203 LEU B CB  1 
ATOM   4549 C  CG  . LEU B 1 201 ? 63.487 126.394 -95.654  1.00 28.26  ? 203 LEU B CG  1 
ATOM   4550 C  CD1 . LEU B 1 201 ? 64.203 127.623 -96.184  1.00 29.43  ? 203 LEU B CD1 1 
ATOM   4551 C  CD2 . LEU B 1 201 ? 62.006 126.711 -95.489  1.00 28.90  ? 203 LEU B CD2 1 
ATOM   4552 N  N   . PRO B 1 202 ? 62.203 122.708 -98.075  1.00 24.18  ? 204 PRO B N   1 
ATOM   4553 C  CA  . PRO B 1 202 ? 62.238 121.641 -99.070  1.00 24.73  ? 204 PRO B CA  1 
ATOM   4554 C  C   . PRO B 1 202 ? 63.392 121.847 -100.077 1.00 25.15  ? 204 PRO B C   1 
ATOM   4555 O  O   . PRO B 1 202 ? 63.853 122.970 -100.284 1.00 24.43  ? 204 PRO B O   1 
ATOM   4556 C  CB  . PRO B 1 202 ? 60.861 121.830 -99.725  1.00 24.58  ? 204 PRO B CB  1 
ATOM   4557 C  CG  . PRO B 1 202 ? 60.632 123.320 -99.680  1.00 23.72  ? 204 PRO B CG  1 
ATOM   4558 C  CD  . PRO B 1 202 ? 61.141 123.701 -98.312  1.00 23.74  ? 204 PRO B CD  1 
ATOM   4559 N  N   . SER B 1 203 ? 63.887 120.764 -100.667 1.00 25.46  ? 205 SER B N   1 
ATOM   4560 C  CA  . SER B 1 203 ? 65.067 120.803 -101.563 1.00 25.40  ? 205 SER B CA  1 
ATOM   4561 C  C   . SER B 1 203 ? 64.740 121.631 -102.802 1.00 25.48  ? 205 SER B C   1 
ATOM   4562 O  O   . SER B 1 203 ? 65.667 122.138 -103.384 1.00 27.06  ? 205 SER B O   1 
ATOM   4563 C  CB  . SER B 1 203 ? 65.497 119.439 -101.912 1.00 26.03  ? 205 SER B CB  1 
ATOM   4564 O  OG  . SER B 1 203 ? 64.431 118.734 -102.518 1.00 25.57  ? 205 SER B OG  1 
ATOM   4565 N  N   . ASN B 1 204 ? 63.470 121.829 -103.157 1.00 24.86  ? 206 ASN B N   1 
ATOM   4566 C  CA  . ASN B 1 204 ? 63.079 122.660 -104.329 1.00 25.15  ? 206 ASN B CA  1 
ATOM   4567 C  C   . ASN B 1 204 ? 62.667 124.068 -103.882 1.00 24.43  ? 206 ASN B C   1 
ATOM   4568 O  O   . ASN B 1 204 ? 61.934 124.725 -104.624 1.00 22.83  ? 206 ASN B O   1 
ATOM   4569 C  CB  . ASN B 1 204 ? 61.983 122.010 -105.201 1.00 25.02  ? 206 ASN B CB  1 
ATOM   4570 C  CG  . ASN B 1 204 ? 60.782 121.516 -104.429 1.00 24.87  ? 206 ASN B CG  1 
ATOM   4571 O  OD1 . ASN B 1 204 ? 60.761 121.645 -103.194 1.00 26.43  ? 206 ASN B OD1 1 
ATOM   4572 N  ND2 . ASN B 1 204 ? 59.787 120.973 -105.114 1.00 23.92  ? 206 ASN B ND2 1 
ATOM   4573 N  N   . TYR B 1 205 ? 63.156 124.537 -102.742 1.00 24.69  ? 207 TYR B N   1 
ATOM   4574 C  CA  . TYR B 1 205 ? 62.735 125.846 -102.194 1.00 25.45  ? 207 TYR B CA  1 
ATOM   4575 C  C   . TYR B 1 205 ? 62.870 126.900 -103.300 1.00 25.28  ? 207 TYR B C   1 
ATOM   4576 O  O   . TYR B 1 205 ? 61.995 127.736 -103.414 1.00 23.91  ? 207 TYR B O   1 
ATOM   4577 C  CB  . TYR B 1 205 ? 63.504 126.193 -100.924 1.00 25.98  ? 207 TYR B CB  1 
ATOM   4578 C  CG  . TYR B 1 205 ? 63.204 127.556 -100.364 1.00 27.15  ? 207 TYR B CG  1 
ATOM   4579 C  CD1 . TYR B 1 205 ? 62.019 127.818 -99.699  1.00 27.29  ? 207 TYR B CD1 1 
ATOM   4580 C  CD2 . TYR B 1 205 ? 64.133 128.577 -100.448 1.00 27.97  ? 207 TYR B CD2 1 
ATOM   4581 C  CE1 . TYR B 1 205 ? 61.727 129.086 -99.213  1.00 28.18  ? 207 TYR B CE1 1 
ATOM   4582 C  CE2 . TYR B 1 205 ? 63.865 129.847 -99.954  1.00 29.11  ? 207 TYR B CE2 1 
ATOM   4583 C  CZ  . TYR B 1 205 ? 62.653 130.113 -99.335  1.00 30.04  ? 207 TYR B CZ  1 
ATOM   4584 O  OH  . TYR B 1 205 ? 62.420 131.380 -98.844  1.00 31.91  ? 207 TYR B OH  1 
ATOM   4585 N  N   . ALA B 1 206 ? 63.915 126.830 -104.116 1.00 27.86  ? 208 ALA B N   1 
ATOM   4586 C  CA  . ALA B 1 206 ? 64.258 127.853 -105.147 1.00 28.78  ? 208 ALA B CA  1 
ATOM   4587 C  C   . ALA B 1 206 ? 63.242 127.862 -106.284 1.00 29.36  ? 208 ALA B C   1 
ATOM   4588 O  O   . ALA B 1 206 ? 63.148 128.890 -106.965 1.00 30.71  ? 208 ALA B O   1 
ATOM   4589 C  CB  . ALA B 1 206 ? 65.638 127.626 -105.684 1.00 28.99  ? 208 ALA B CB  1 
ATOM   4590 N  N   . ASP B 1 207 ? 62.529 126.755 -106.494 1.00 30.26  ? 209 ASP B N   1 
ATOM   4591 C  CA  . ASP B 1 207 ? 61.546 126.610 -107.598 1.00 30.54  ? 209 ASP B CA  1 
ATOM   4592 C  C   . ASP B 1 207 ? 60.254 127.355 -107.235 1.00 28.44  ? 209 ASP B C   1 
ATOM   4593 O  O   . ASP B 1 207 ? 59.420 127.520 -108.111 1.00 28.56  ? 209 ASP B O   1 
ATOM   4594 C  CB  . ASP B 1 207 ? 61.239 125.137 -107.886 1.00 33.32  ? 209 ASP B CB  1 
ATOM   4595 C  CG  . ASP B 1 207 ? 62.406 124.289 -108.377 1.00 35.87  ? 209 ASP B CG  1 
ATOM   4596 O  OD1 . ASP B 1 207 ? 63.414 124.881 -108.791 1.00 37.75  ? 209 ASP B OD1 1 
ATOM   4597 O  OD2 . ASP B 1 207 ? 62.292 123.026 -108.346 1.00 37.94  ? 209 ASP B OD2 1 
ATOM   4598 N  N   . PHE B 1 208 ? 60.059 127.781 -105.986 1.00 26.31  ? 210 PHE B N   1 
ATOM   4599 C  CA  . PHE B 1 208 ? 58.882 128.599 -105.588 1.00 24.50  ? 210 PHE B CA  1 
ATOM   4600 C  C   . PHE B 1 208 ? 59.200 130.068 -105.817 1.00 25.37  ? 210 PHE B C   1 
ATOM   4601 O  O   . PHE B 1 208 ? 60.316 130.467 -105.547 1.00 26.08  ? 210 PHE B O   1 
ATOM   4602 C  CB  . PHE B 1 208 ? 58.544 128.408 -104.116 1.00 22.68  ? 210 PHE B CB  1 
ATOM   4603 C  CG  . PHE B 1 208 ? 57.984 127.055 -103.818 1.00 21.26  ? 210 PHE B CG  1 
ATOM   4604 C  CD1 . PHE B 1 208 ? 58.812 125.965 -103.710 1.00 21.05  ? 210 PHE B CD1 1 
ATOM   4605 C  CD2 . PHE B 1 208 ? 56.641 126.880 -103.620 1.00 20.70  ? 210 PHE B CD2 1 
ATOM   4606 C  CE1 . PHE B 1 208 ? 58.304 124.717 -103.397 1.00 20.58  ? 210 PHE B CE1 1 
ATOM   4607 C  CE2 . PHE B 1 208 ? 56.131 125.622 -103.361 1.00 20.62  ? 210 PHE B CE2 1 
ATOM   4608 C  CZ  . PHE B 1 208 ? 56.966 124.542 -103.252 1.00 20.39  ? 210 PHE B CZ  1 
ATOM   4609 N  N   . THR B 1 209 ? 58.246 130.855 -106.285 1.00 27.05  ? 211 THR B N   1 
ATOM   4610 C  CA  . THR B 1 209 ? 58.458 132.319 -106.407 1.00 29.26  ? 211 THR B CA  1 
ATOM   4611 C  C   . THR B 1 209 ? 57.929 132.989 -105.144 1.00 29.66  ? 211 THR B C   1 
ATOM   4612 O  O   . THR B 1 209 ? 58.481 134.019 -104.765 1.00 31.12  ? 211 THR B O   1 
ATOM   4613 C  CB  . THR B 1 209 ? 57.822 132.904 -107.673 1.00 30.14  ? 211 THR B CB  1 
ATOM   4614 O  OG1 . THR B 1 209 ? 56.552 132.262 -107.793 1.00 29.74  ? 211 THR B OG1 1 
ATOM   4615 C  CG2 . THR B 1 209 ? 58.690 132.694 -108.907 1.00 31.06  ? 211 THR B CG2 1 
ATOM   4616 N  N   . ARG B 1 210 ? 56.890 132.438 -104.528 1.00 30.02  ? 212 ARG B N   1 
ATOM   4617 C  CA  . ARG B 1 210 ? 56.411 132.933 -103.205 1.00 30.94  ? 212 ARG B CA  1 
ATOM   4618 C  C   . ARG B 1 210 ? 56.309 131.722 -102.284 1.00 27.86  ? 212 ARG B C   1 
ATOM   4619 O  O   . ARG B 1 210 ? 55.938 130.641 -102.782 1.00 28.05  ? 212 ARG B O   1 
ATOM   4620 C  CB  . ARG B 1 210 ? 55.116 133.720 -103.448 1.00 35.78  ? 212 ARG B CB  1 
ATOM   4621 C  CG  . ARG B 1 210 ? 54.089 133.724 -102.319 1.00 41.18  ? 212 ARG B CG  1 
ATOM   4622 C  CD  . ARG B 1 210 ? 52.980 132.695 -102.547 1.00 44.40  ? 212 ARG B CD  1 
ATOM   4623 N  NE  . ARG B 1 210 ? 51.733 133.058 -101.872 1.00 47.06  ? 212 ARG B NE  1 
ATOM   4624 C  CZ  . ARG B 1 210 ? 50.743 133.762 -102.415 1.00 49.67  ? 212 ARG B CZ  1 
ATOM   4625 N  NH1 . ARG B 1 210 ? 50.818 134.222 -103.654 1.00 52.85  ? 212 ARG B NH1 1 
ATOM   4626 N  NH2 . ARG B 1 210 ? 49.670 134.017 -101.702 1.00 51.26  ? 212 ARG B NH2 1 
ATOM   4627 N  N   . TYR B 1 211 ? 56.632 131.878 -100.993 1.00 25.81  ? 213 TYR B N   1 
ATOM   4628 C  CA  . TYR B 1 211 ? 56.668 130.742 -100.040 1.00 22.64  ? 213 TYR B CA  1 
ATOM   4629 C  C   . TYR B 1 211 ? 55.920 131.140 -98.784  1.00 22.43  ? 213 TYR B C   1 
ATOM   4630 O  O   . TYR B 1 211 ? 56.518 131.789 -97.899  1.00 21.26  ? 213 TYR B O   1 
ATOM   4631 C  CB  . TYR B 1 211 ? 58.091 130.252 -99.744  1.00 20.92  ? 213 TYR B CB  1 
ATOM   4632 C  CG  . TYR B 1 211 ? 58.109 128.825 -99.264  1.00 19.19  ? 213 TYR B CG  1 
ATOM   4633 C  CD1 . TYR B 1 211 ? 58.000 127.786 -100.163 1.00 18.41  ? 213 TYR B CD1 1 
ATOM   4634 C  CD2 . TYR B 1 211 ? 58.150 128.508 -97.914  1.00 18.15  ? 213 TYR B CD2 1 
ATOM   4635 C  CE1 . TYR B 1 211 ? 57.970 126.470 -99.743  1.00 18.11  ? 213 TYR B CE1 1 
ATOM   4636 C  CE2 . TYR B 1 211 ? 58.121 127.194 -97.481  1.00 17.52  ? 213 TYR B CE2 1 
ATOM   4637 C  CZ  . TYR B 1 211 ? 57.996 126.168 -98.393  1.00 17.54  ? 213 TYR B CZ  1 
ATOM   4638 O  OH  . TYR B 1 211 ? 57.947 124.863 -98.004  1.00 17.07  ? 213 TYR B OH  1 
ATOM   4639 N  N   . GLU B 1 212 ? 54.649 130.741 -98.720  1.00 23.52  ? 214 GLU B N   1 
ATOM   4640 C  CA  . GLU B 1 212 ? 53.808 130.921 -97.509  1.00 24.13  ? 214 GLU B CA  1 
ATOM   4641 C  C   . GLU B 1 212 ? 54.388 130.017 -96.428  1.00 22.17  ? 214 GLU B C   1 
ATOM   4642 O  O   . GLU B 1 212 ? 54.609 128.833 -96.680  1.00 20.87  ? 214 GLU B O   1 
ATOM   4643 C  CB  . GLU B 1 212 ? 52.326 130.636 -97.763  1.00 27.10  ? 214 GLU B CB  1 
ATOM   4644 C  CG  . GLU B 1 212 ? 51.672 131.642 -98.688  1.00 30.78  ? 214 GLU B CG  1 
ATOM   4645 C  CD  . GLU B 1 212 ? 50.182 131.411 -98.937  1.00 35.04  ? 214 GLU B CD  1 
ATOM   4646 O  OE1 . GLU B 1 212 ? 49.813 130.583 -99.792  1.00 38.38  ? 214 GLU B OE1 1 
ATOM   4647 O  OE2 . GLU B 1 212 ? 49.372 132.044 -98.241  1.00 43.10  ? 214 GLU B OE2 1 
ATOM   4648 N  N   . PHE B 1 213 ? 54.626 130.605 -95.257  1.00 21.30  ? 215 PHE B N   1 
ATOM   4649 C  CA  . PHE B 1 213 ? 55.282 129.982 -94.091  1.00 19.85  ? 215 PHE B CA  1 
ATOM   4650 C  C   . PHE B 1 213 ? 54.576 130.444 -92.820  1.00 19.31  ? 215 PHE B C   1 
ATOM   4651 O  O   . PHE B 1 213 ? 54.699 131.628 -92.472  1.00 19.09  ? 215 PHE B O   1 
ATOM   4652 C  CB  . PHE B 1 213 ? 56.730 130.449 -94.063  1.00 19.75  ? 215 PHE B CB  1 
ATOM   4653 C  CG  . PHE B 1 213 ? 57.621 129.719 -93.105  1.00 19.53  ? 215 PHE B CG  1 
ATOM   4654 C  CD1 . PHE B 1 213 ? 58.276 128.545 -93.490  1.00 19.04  ? 215 PHE B CD1 1 
ATOM   4655 C  CD2 . PHE B 1 213 ? 57.788 130.211 -91.805  1.00 19.57  ? 215 PHE B CD2 1 
ATOM   4656 C  CE1 . PHE B 1 213 ? 59.123 127.898 -92.594  1.00 18.61  ? 215 PHE B CE1 1 
ATOM   4657 C  CE2 . PHE B 1 213 ? 58.648 129.573 -90.937  1.00 19.08  ? 215 PHE B CE2 1 
ATOM   4658 C  CZ  . PHE B 1 213 ? 59.304 128.422 -91.334  1.00 19.12  ? 215 PHE B CZ  1 
ATOM   4659 N  N   . THR B 1 214 ? 53.856 129.550 -92.162  1.00 18.71  ? 216 THR B N   1 
ATOM   4660 C  CA  . THR B 1 214 ? 53.118 129.904 -90.927  1.00 18.98  ? 216 THR B CA  1 
ATOM   4661 C  C   . THR B 1 214 ? 53.276 128.778 -89.916  1.00 18.82  ? 216 THR B C   1 
ATOM   4662 O  O   . THR B 1 214 ? 52.819 127.646 -90.198  1.00 18.15  ? 216 THR B O   1 
ATOM   4663 C  CB  . THR B 1 214 ? 51.660 130.231 -91.222  1.00 19.24  ? 216 THR B CB  1 
ATOM   4664 O  OG1 . THR B 1 214 ? 51.755 131.294 -92.165  1.00 19.78  ? 216 THR B OG1 1 
ATOM   4665 C  CG2 . THR B 1 214 ? 50.874 130.652 -90.001  1.00 19.72  ? 216 THR B CG2 1 
ATOM   4666 N  N   . ILE B 1 215 ? 53.928 129.088 -88.796  1.00 18.30  ? 217 ILE B N   1 
ATOM   4667 C  CA  . ILE B 1 215 ? 54.007 128.141 -87.659  1.00 18.36  ? 217 ILE B CA  1 
ATOM   4668 C  C   . ILE B 1 215 ? 52.950 128.575 -86.663  1.00 19.35  ? 217 ILE B C   1 
ATOM   4669 O  O   . ILE B 1 215 ? 52.957 129.760 -86.274  1.00 19.56  ? 217 ILE B O   1 
ATOM   4670 C  CB  . ILE B 1 215 ? 55.414 128.123 -87.074  1.00 18.01  ? 217 ILE B CB  1 
ATOM   4671 C  CG1 . ILE B 1 215 ? 56.388 127.555 -88.104  1.00 18.52  ? 217 ILE B CG1 1 
ATOM   4672 C  CG2 . ILE B 1 215 ? 55.434 127.323 -85.814  1.00 18.32  ? 217 ILE B CG2 1 
ATOM   4673 C  CD1 . ILE B 1 215 ? 57.848 127.675 -87.748  1.00 18.71  ? 217 ILE B CD1 1 
ATOM   4674 N  N   . LYS B 1 216 ? 52.034 127.665 -86.333  1.00 20.32  ? 218 LYS B N   1 
ATOM   4675 C  CA  . LYS B 1 216 ? 51.102 127.828 -85.192  1.00 20.47  ? 218 LYS B CA  1 
ATOM   4676 C  C   . LYS B 1 216 ? 51.493 126.875 -84.088  1.00 18.88  ? 218 LYS B C   1 
ATOM   4677 O  O   . LYS B 1 216 ? 51.607 125.693 -84.366  1.00 18.85  ? 218 LYS B O   1 
ATOM   4678 C  CB  . LYS B 1 216 ? 49.693 127.505 -85.645  1.00 23.24  ? 218 LYS B CB  1 
ATOM   4679 C  CG  . LYS B 1 216 ? 49.079 128.645 -86.413  1.00 25.70  ? 218 LYS B CG  1 
ATOM   4680 C  CD  . LYS B 1 216 ? 47.672 128.347 -86.844  1.00 28.95  ? 218 LYS B CD  1 
ATOM   4681 C  CE  . LYS B 1 216 ? 47.049 129.559 -87.513  1.00 31.99  ? 218 LYS B CE  1 
ATOM   4682 N  NZ  . LYS B 1 216 ? 47.047 130.680 -86.528  1.00 33.48  ? 218 LYS B NZ  1 
ATOM   4683 N  N   . ASP B 1 217 ? 51.651 127.390 -82.879  1.00 17.31  ? 219 ASP B N   1 
ATOM   4684 C  CA  . ASP B 1 217 ? 52.072 126.595 -81.706  1.00 16.62  ? 219 ASP B CA  1 
ATOM   4685 C  C   . ASP B 1 217 ? 51.035 126.761 -80.602  1.00 16.13  ? 219 ASP B C   1 
ATOM   4686 O  O   . ASP B 1 217 ? 50.843 127.882 -80.076  1.00 15.72  ? 219 ASP B O   1 
ATOM   4687 C  CB  . ASP B 1 217 ? 53.447 127.060 -81.230  1.00 16.60  ? 219 ASP B CB  1 
ATOM   4688 C  CG  . ASP B 1 217 ? 54.025 126.283 -80.069  1.00 16.34  ? 219 ASP B CG  1 
ATOM   4689 O  OD1 . ASP B 1 217 ? 53.526 125.184 -79.767  1.00 16.43  ? 219 ASP B OD1 1 
ATOM   4690 O  OD2 . ASP B 1 217 ? 54.986 126.776 -79.486  1.00 16.36  ? 219 ASP B OD2 1 
ATOM   4691 N  N   . THR B 1 218 ? 50.389 125.672 -80.243  1.00 16.06  ? 220 THR B N   1 
ATOM   4692 C  CA  . THR B 1 218 ? 49.308 125.722 -79.233  1.00 16.26  ? 220 THR B CA  1 
ATOM   4693 C  C   . THR B 1 218 ? 49.881 125.403 -77.863  1.00 16.29  ? 220 THR B C   1 
ATOM   4694 O  O   . THR B 1 218 ? 50.340 124.266 -77.704  1.00 16.30  ? 220 THR B O   1 
ATOM   4695 C  CB  . THR B 1 218 ? 48.162 124.784 -79.589  1.00 16.12  ? 220 THR B CB  1 
ATOM   4696 O  OG1 . THR B 1 218 ? 47.788 125.283 -80.858  1.00 16.04  ? 220 THR B OG1 1 
ATOM   4697 C  CG2 . THR B 1 218 ? 47.012 124.864 -78.615  1.00 16.58  ? 220 THR B CG2 1 
ATOM   4698 N  N   . ILE B 1 219 ? 49.789 126.374 -76.944  1.00 16.21  ? 221 ILE B N   1 
ATOM   4699 C  CA  . ILE B 1 219 ? 50.215 126.265 -75.539  1.00 16.90  ? 221 ILE B CA  1 
ATOM   4700 C  C   . ILE B 1 219 ? 49.069 125.637 -74.747  1.00 16.34  ? 221 ILE B C   1 
ATOM   4701 O  O   . ILE B 1 219 ? 47.907 126.004 -74.917  1.00 16.94  ? 221 ILE B O   1 
ATOM   4702 C  CB  . ILE B 1 219 ? 50.581 127.656 -74.992  1.00 18.08  ? 221 ILE B CB  1 
ATOM   4703 C  CG1 . ILE B 1 219 ? 51.508 128.425 -75.937  1.00 18.49  ? 221 ILE B CG1 1 
ATOM   4704 C  CG2 . ILE B 1 219 ? 51.167 127.528 -73.589  1.00 18.19  ? 221 ILE B CG2 1 
ATOM   4705 C  CD1 . ILE B 1 219 ? 52.734 127.678 -76.327  1.00 18.96  ? 221 ILE B CD1 1 
ATOM   4706 N  N   . PRO B 1 220 ? 49.328 124.627 -73.904  1.00 15.46  ? 222 PRO B N   1 
ATOM   4707 C  CA  . PRO B 1 220 ? 48.264 124.068 -73.072  1.00 15.79  ? 222 PRO B CA  1 
ATOM   4708 C  C   . PRO B 1 220 ? 47.845 125.019 -71.932  1.00 16.29  ? 222 PRO B C   1 
ATOM   4709 O  O   . PRO B 1 220 ? 48.599 125.896 -71.589  1.00 15.83  ? 222 PRO B O   1 
ATOM   4710 C  CB  . PRO B 1 220 ? 48.935 122.822 -72.510  1.00 15.83  ? 222 PRO B CB  1 
ATOM   4711 C  CG  . PRO B 1 220 ? 50.395 123.226 -72.356  1.00 15.42  ? 222 PRO B CG  1 
ATOM   4712 C  CD  . PRO B 1 220 ? 50.646 124.019 -73.634  1.00 15.41  ? 222 PRO B CD  1 
ATOM   4713 N  N   . ALA B 1 221 ? 46.624 124.877 -71.421  1.00 16.98  ? 223 ALA B N   1 
ATOM   4714 C  CA  . ALA B 1 221 ? 46.101 125.695 -70.301  1.00 18.20  ? 223 ALA B CA  1 
ATOM   4715 C  C   . ALA B 1 221 ? 47.070 125.652 -69.123  1.00 18.02  ? 223 ALA B C   1 
ATOM   4716 O  O   . ALA B 1 221 ? 47.170 126.680 -68.420  1.00 18.40  ? 223 ALA B O   1 
ATOM   4717 C  CB  . ALA B 1 221 ? 44.749 125.206 -69.864  1.00 18.58  ? 223 ALA B CB  1 
ATOM   4718 N  N   . GLY B 1 222 ? 47.805 124.549 -68.953  1.00 18.31  ? 224 GLY B N   1 
ATOM   4719 C  CA  . GLY B 1 222 ? 48.719 124.384 -67.802  1.00 19.01  ? 224 GLY B CA  1 
ATOM   4720 C  C   . GLY B 1 222 ? 49.964 125.241 -67.910  1.00 19.95  ? 224 GLY B C   1 
ATOM   4721 O  O   . GLY B 1 222 ? 50.848 125.124 -67.026  1.00 19.27  ? 224 GLY B O   1 
ATOM   4722 N  N   . MET B 1 223 ? 50.112 126.025 -68.980  1.00 20.56  ? 225 MET B N   1 
ATOM   4723 C  CA  . MET B 1 223 ? 51.403 126.715 -69.218  1.00 22.92  ? 225 MET B CA  1 
ATOM   4724 C  C   . MET B 1 223 ? 51.150 128.156 -69.648  1.00 23.00  ? 225 MET B C   1 
ATOM   4725 O  O   . MET B 1 223 ? 50.138 128.418 -70.251  1.00 23.49  ? 225 MET B O   1 
ATOM   4726 C  CB  . MET B 1 223 ? 52.256 125.963 -70.250  1.00 23.68  ? 225 MET B CB  1 
ATOM   4727 C  CG  . MET B 1 223 ? 53.729 126.043 -69.942  1.00 26.79  ? 225 MET B CG  1 
ATOM   4728 S  SD  . MET B 1 223 ? 54.793 124.599 -70.259  0.98 31.11  ? 225 MET B SD  1 
ATOM   4729 C  CE  . MET B 1 223 ? 53.580 123.293 -70.095  1.00 30.89  ? 225 MET B CE  1 
ATOM   4730 N  N   . THR B 1 224 ? 52.063 129.047 -69.308  1.00 23.74  ? 226 THR B N   1 
ATOM   4731 C  CA  . THR B 1 224 ? 51.962 130.488 -69.607  1.00 24.66  ? 226 THR B CA  1 
ATOM   4732 C  C   . THR B 1 224 ? 53.164 130.858 -70.463  1.00 24.91  ? 226 THR B C   1 
ATOM   4733 O  O   . THR B 1 224 ? 54.314 130.700 -70.021  1.00 26.58  ? 226 THR B O   1 
ATOM   4734 C  CB  . THR B 1 224 ? 51.915 131.351 -68.333  1.00 26.83  ? 226 THR B CB  1 
ATOM   4735 O  OG1 . THR B 1 224 ? 50.879 130.907 -67.464  1.00 25.62  ? 226 THR B OG1 1 
ATOM   4736 C  CG2 . THR B 1 224 ? 51.649 132.808 -68.637  1.00 27.92  ? 226 THR B CG2 1 
ATOM   4737 N  N   . TYR B 1 225 ? 52.900 131.344 -71.662  1.00 25.41  ? 227 TYR B N   1 
ATOM   4738 C  CA  . TYR B 1 225 ? 53.914 131.850 -72.606  1.00 24.06  ? 227 TYR B CA  1 
ATOM   4739 C  C   . TYR B 1 225 ? 54.405 133.229 -72.125  1.00 25.67  ? 227 TYR B C   1 
ATOM   4740 O  O   . TYR B 1 225 ? 53.634 134.049 -71.578  1.00 25.41  ? 227 TYR B O   1 
ATOM   4741 C  CB  . TYR B 1 225 ? 53.273 131.808 -73.982  1.00 23.72  ? 227 TYR B CB  1 
ATOM   4742 C  CG  . TYR B 1 225 ? 54.038 132.529 -75.056  1.00 23.14  ? 227 TYR B CG  1 
ATOM   4743 C  CD1 . TYR B 1 225 ? 55.276 132.119 -75.483  1.00 22.64  ? 227 TYR B CD1 1 
ATOM   4744 C  CD2 . TYR B 1 225 ? 53.471 133.614 -75.691  1.00 24.04  ? 227 TYR B CD2 1 
ATOM   4745 C  CE1 . TYR B 1 225 ? 55.930 132.776 -76.522  1.00 22.80  ? 227 TYR B CE1 1 
ATOM   4746 C  CE2 . TYR B 1 225 ? 54.137 134.307 -76.686  1.00 23.85  ? 227 TYR B CE2 1 
ATOM   4747 C  CZ  . TYR B 1 225 ? 55.375 133.896 -77.103  1.00 23.20  ? 227 TYR B CZ  1 
ATOM   4748 O  OH  . TYR B 1 225 ? 55.959 134.644 -78.089  1.00 24.56  ? 227 TYR B OH  1 
ATOM   4749 N  N   . ASN B 1 226 ? 55.688 133.502 -72.343  1.00 26.35  ? 228 ASN B N   1 
ATOM   4750 C  CA  . ASN B 1 226 ? 56.378 134.698 -71.804  1.00 28.10  ? 228 ASN B CA  1 
ATOM   4751 C  C   . ASN B 1 226 ? 56.468 135.802 -72.864  1.00 29.80  ? 228 ASN B C   1 
ATOM   4752 O  O   . ASN B 1 226 ? 57.190 136.808 -72.615  1.00 30.66  ? 228 ASN B O   1 
ATOM   4753 C  CB  . ASN B 1 226 ? 57.733 134.276 -71.234  1.00 28.56  ? 228 ASN B CB  1 
ATOM   4754 C  CG  . ASN B 1 226 ? 57.585 133.491 -69.941  1.00 27.28  ? 228 ASN B CG  1 
ATOM   4755 O  OD1 . ASN B 1 226 ? 56.726 133.791 -69.144  1.00 27.39  ? 228 ASN B OD1 1 
ATOM   4756 N  ND2 . ASN B 1 226 ? 58.391 132.467 -69.745  1.00 26.96  ? 228 ASN B ND2 1 
ATOM   4757 N  N   . ASN B 1 227 ? 55.772 135.639 -73.994  1.00 30.19  ? 229 ASN B N   1 
ATOM   4758 C  CA  . ASN B 1 227 ? 55.669 136.665 -75.065  1.00 32.25  ? 229 ASN B CA  1 
ATOM   4759 C  C   . ASN B 1 227 ? 57.085 137.041 -75.522  1.00 33.04  ? 229 ASN B C   1 
ATOM   4760 O  O   . ASN B 1 227 ? 57.384 138.251 -75.679  1.00 36.22  ? 229 ASN B O   1 
ATOM   4761 C  CB  . ASN B 1 227 ? 54.824 137.837 -74.563  1.00 33.91  ? 229 ASN B CB  1 
ATOM   4762 C  CG  . ASN B 1 227 ? 53.377 137.426 -74.450  1.00 34.21  ? 229 ASN B CG  1 
ATOM   4763 O  OD1 . ASN B 1 227 ? 52.642 137.472 -75.438  1.00 37.71  ? 229 ASN B OD1 1 
ATOM   4764 N  ND2 . ASN B 1 227 ? 52.993 136.919 -73.294  1.00 34.79  ? 229 ASN B ND2 1 
ATOM   4765 N  N   . ASP B 1 228 ? 57.944 136.048 -75.723  1.00 31.42  ? 230 ASP B N   1 
ATOM   4766 C  CA  . ASP B 1 228 ? 59.375 136.318 -75.984  1.00 32.25  ? 230 ASP B CA  1 
ATOM   4767 C  C   . ASP B 1 228 ? 59.882 135.452 -77.145  1.00 32.44  ? 230 ASP B C   1 
ATOM   4768 O  O   . ASP B 1 228 ? 61.082 135.248 -77.243  1.00 33.22  ? 230 ASP B O   1 
ATOM   4769 C  CB  . ASP B 1 228 ? 60.154 136.134 -74.683  1.00 31.53  ? 230 ASP B CB  1 
ATOM   4770 C  CG  . ASP B 1 228 ? 60.163 134.699 -74.227  1.00 29.49  ? 230 ASP B CG  1 
ATOM   4771 O  OD1 . ASP B 1 228 ? 59.364 133.891 -74.778  1.00 28.67  ? 230 ASP B OD1 1 
ATOM   4772 O  OD2 . ASP B 1 228 ? 60.986 134.400 -73.392  1.00 28.22  ? 230 ASP B OD2 1 
ATOM   4773 N  N   . ALA B 1 229 ? 59.022 135.010 -78.055  1.00 32.83  ? 231 ALA B N   1 
ATOM   4774 C  CA  . ALA B 1 229 ? 59.473 134.219 -79.224  1.00 32.63  ? 231 ALA B CA  1 
ATOM   4775 C  C   . ALA B 1 229 ? 60.446 135.035 -80.100  1.00 33.18  ? 231 ALA B C   1 
ATOM   4776 O  O   . ALA B 1 229 ? 60.193 136.216 -80.375  1.00 31.76  ? 231 ALA B O   1 
ATOM   4777 C  CB  . ALA B 1 229 ? 58.280 133.733 -80.013  1.00 32.09  ? 231 ALA B CB  1 
ATOM   4778 N  N   . GLN B 1 230 ? 61.541 134.411 -80.532  1.00 34.88  ? 232 GLN B N   1 
ATOM   4779 C  CA  . GLN B 1 230 ? 62.476 135.003 -81.522  1.00 36.31  ? 232 GLN B CA  1 
ATOM   4780 C  C   . GLN B 1 230 ? 62.769 133.989 -82.622  1.00 32.73  ? 232 GLN B C   1 
ATOM   4781 O  O   . GLN B 1 230 ? 62.754 132.782 -82.377  1.00 30.38  ? 232 GLN B O   1 
ATOM   4782 C  CB  . GLN B 1 230 ? 63.749 135.464 -80.823  1.00 40.71  ? 232 GLN B CB  1 
ATOM   4783 C  CG  . GLN B 1 230 ? 63.520 136.661 -79.911  1.00 45.45  ? 232 GLN B CG  1 
ATOM   4784 C  CD  . GLN B 1 230 ? 64.771 137.030 -79.151  1.00 50.69  ? 232 GLN B CD  1 
ATOM   4785 O  OE1 . GLN B 1 230 ? 65.402 136.179 -78.509  1.00 53.14  ? 232 GLN B OE1 1 
ATOM   4786 N  NE2 . GLN B 1 230 ? 65.133 138.304 -79.226  1.00 52.76  ? 232 GLN B NE2 1 
ATOM   4787 N  N   . VAL B 1 231 ? 63.003 134.499 -83.811  1.00 32.06  ? 233 VAL B N   1 
ATOM   4788 C  CA  . VAL B 1 231 ? 63.180 133.666 -85.022  1.00 30.88  ? 233 VAL B CA  1 
ATOM   4789 C  C   . VAL B 1 231 ? 64.612 133.848 -85.504  1.00 31.51  ? 233 VAL B C   1 
ATOM   4790 O  O   . VAL B 1 231 ? 65.062 134.989 -85.615  1.00 30.98  ? 233 VAL B O   1 
ATOM   4791 C  CB  . VAL B 1 231 ? 62.132 134.053 -86.071  1.00 30.72  ? 233 VAL B CB  1 
ATOM   4792 C  CG1 . VAL B 1 231 ? 62.075 133.048 -87.220  1.00 29.90  ? 233 VAL B CG1 1 
ATOM   4793 C  CG2 . VAL B 1 231 ? 60.771 134.206 -85.402  1.00 29.61  ? 233 VAL B CG2 1 
ATOM   4794 N  N   . TYR B 1 232 ? 65.284 132.734 -85.762  1.00 32.27  ? 234 TYR B N   1 
ATOM   4795 C  CA  . TYR B 1 232 ? 66.713 132.691 -86.115  1.00 34.78  ? 234 TYR B CA  1 
ATOM   4796 C  C   . TYR B 1 232 ? 66.876 131.947 -87.429  1.00 35.48  ? 234 TYR B C   1 
ATOM   4797 O  O   . TYR B 1 232 ? 66.289 130.874 -87.600  1.00 33.82  ? 234 TYR B O   1 
ATOM   4798 C  CB  . TYR B 1 232 ? 67.509 132.004 -85.016  1.00 37.52  ? 234 TYR B CB  1 
ATOM   4799 C  CG  . TYR B 1 232 ? 67.516 132.751 -83.699  1.00 39.89  ? 234 TYR B CG  1 
ATOM   4800 C  CD1 . TYR B 1 232 ? 68.232 133.930 -83.552  1.00 41.49  ? 234 TYR B CD1 1 
ATOM   4801 C  CD2 . TYR B 1 232 ? 66.786 132.298 -82.606  1.00 39.88  ? 234 TYR B CD2 1 
ATOM   4802 C  CE1 . TYR B 1 232 ? 68.227 134.634 -82.355  1.00 43.11  ? 234 TYR B CE1 1 
ATOM   4803 C  CE2 . TYR B 1 232 ? 66.786 132.978 -81.399  1.00 41.24  ? 234 TYR B CE2 1 
ATOM   4804 C  CZ  . TYR B 1 232 ? 67.507 134.154 -81.275  1.00 43.24  ? 234 TYR B CZ  1 
ATOM   4805 O  OH  . TYR B 1 232 ? 67.493 134.849 -80.098  1.00 47.09  ? 234 TYR B OH  1 
ATOM   4806 N  N   . LEU B 1 233 ? 67.670 132.510 -88.329  1.00 37.83  ? 235 LEU B N   1 
ATOM   4807 C  CA  . LEU B 1 233 ? 68.139 131.784 -89.533  1.00 39.77  ? 235 LEU B CA  1 
ATOM   4808 C  C   . LEU B 1 233 ? 69.403 131.009 -89.148  1.00 41.96  ? 235 LEU B C   1 
ATOM   4809 O  O   . LEU B 1 233 ? 70.345 131.640 -88.636  1.00 45.53  ? 235 LEU B O   1 
ATOM   4810 C  CB  . LEU B 1 233 ? 68.373 132.793 -90.660  1.00 40.91  ? 235 LEU B CB  1 
ATOM   4811 C  CG  . LEU B 1 233 ? 69.148 132.263 -91.860  1.00 42.64  ? 235 LEU B CG  1 
ATOM   4812 C  CD1 . LEU B 1 233 ? 68.455 131.055 -92.466  1.00 42.52  ? 235 LEU B CD1 1 
ATOM   4813 C  CD2 . LEU B 1 233 ? 69.354 133.361 -92.904  1.00 44.67  ? 235 LEU B CD2 1 
ATOM   4814 N  N   . GLN B 1 234 ? 69.417 129.692 -89.348  1.00 43.22  ? 236 GLN B N   1 
ATOM   4815 C  CA  . GLN B 1 234 ? 70.547 128.817 -88.945  1.00 48.04  ? 236 GLN B CA  1 
ATOM   4816 C  C   . GLN B 1 234 ? 71.194 128.233 -90.208  1.00 53.87  ? 236 GLN B C   1 
ATOM   4817 O  O   . GLN B 1 234 ? 70.538 127.474 -90.924  1.00 53.88  ? 236 GLN B O   1 
ATOM   4818 C  CB  . GLN B 1 234 ? 70.016 127.781 -87.962  1.00 47.60  ? 236 GLN B CB  1 
ATOM   4819 C  CG  . GLN B 1 234 ? 71.080 126.930 -87.277  1.00 49.19  ? 236 GLN B CG  1 
ATOM   4820 C  CD  . GLN B 1 234 ? 70.476 125.938 -86.303  1.00 48.24  ? 236 GLN B CD  1 
ATOM   4821 O  OE1 . GLN B 1 234 ? 69.671 126.305 -85.464  1.00 48.40  ? 236 GLN B OE1 1 
ATOM   4822 N  NE2 . GLN B 1 234 ? 70.788 124.653 -86.433  1.00 48.17  ? 236 GLN B NE2 1 
ATOM   4823 N  N   . GLU B 1 235 ? 72.434 128.622 -90.496  1.00 62.22  ? 237 GLU B N   1 
ATOM   4824 C  CA  . GLU B 1 235 ? 73.151 128.212 -91.729  1.00 68.73  ? 237 GLU B CA  1 
ATOM   4825 C  C   . GLU B 1 235 ? 74.449 127.481 -91.347  1.00 73.51  ? 237 GLU B C   1 
ATOM   4826 O  O   . GLU B 1 235 ? 75.480 128.162 -91.146  1.00 75.47  ? 237 GLU B O   1 
ATOM   4827 C  CB  . GLU B 1 235 ? 73.379 129.427 -92.632  1.00 70.43  ? 237 GLU B CB  1 
ATOM   4828 C  CG  . GLU B 1 235 ? 73.894 129.054 -94.011  1.00 74.57  ? 237 GLU B CG  1 
ATOM   4829 C  CD  . GLU B 1 235 ? 73.214 127.826 -94.607  1.00 77.45  ? 237 GLU B CD  1 
ATOM   4830 O  OE1 . GLU B 1 235 ? 73.613 126.691 -94.257  1.00 80.00  ? 237 GLU B OE1 1 
ATOM   4831 O  OE2 . GLU B 1 235 ? 72.269 127.997 -95.407  1.00 78.24  ? 237 GLU B OE2 1 
ATOM   4832 N  N   . GLY B 1 236 ? 74.396 126.142 -91.265  1.00 73.83  ? 238 GLY B N   1 
ATOM   4833 C  CA  . GLY B 1 236 ? 75.565 125.266 -91.040  1.00 75.73  ? 238 GLY B CA  1 
ATOM   4834 C  C   . GLY B 1 236 ? 75.923 125.144 -89.563  1.00 79.94  ? 238 GLY B C   1 
ATOM   4835 O  O   . GLY B 1 236 ? 75.839 124.018 -89.021  1.00 81.57  ? 238 GLY B O   1 
ATOM   4836 N  N   . GLY B 1 237 ? 76.347 126.245 -88.933  1.00 79.67  ? 239 GLY B N   1 
ATOM   4837 C  CA  . GLY B 1 237 ? 76.568 126.330 -87.479  1.00 77.43  ? 239 GLY B CA  1 
ATOM   4838 C  C   . GLY B 1 237 ? 76.440 127.709 -86.876  1.00 78.36  ? 239 GLY B C   1 
ATOM   4839 O  O   . GLY B 1 237 ? 77.003 127.943 -85.804  1.00 81.92  ? 239 GLY B O   1 
ATOM   4840 N  N   . THR B 1 238 ? 75.745 128.614 -87.558  1.00 75.04  ? 240 THR B N   1 
ATOM   4841 C  CA  . THR B 1 238 ? 75.733 130.069 -87.267  1.00 72.35  ? 240 THR B CA  1 
ATOM   4842 C  C   . THR B 1 238 ? 74.293 130.570 -87.319  1.00 66.22  ? 240 THR B C   1 
ATOM   4843 O  O   . THR B 1 238 ? 73.629 130.340 -88.319  1.00 65.16  ? 240 THR B O   1 
ATOM   4844 C  CB  . THR B 1 238 ? 76.609 130.836 -88.260  1.00 74.90  ? 240 THR B CB  1 
ATOM   4845 O  OG1 . THR B 1 238 ? 76.073 130.587 -89.554  1.00 75.27  ? 240 THR B OG1 1 
ATOM   4846 C  CG2 . THR B 1 238 ? 78.057 130.406 -88.265  1.00 78.68  ? 240 THR B CG2 1 
ATOM   4847 N  N   . GLU B 1 239 ? 73.834 131.236 -86.272  1.00 61.04  ? 241 GLU B N   1 
ATOM   4848 C  CA  . GLU B 1 239 ? 72.458 131.771 -86.208  1.00 57.97  ? 241 GLU B CA  1 
ATOM   4849 C  C   . GLU B 1 239 ? 72.427 133.271 -86.493  1.00 55.97  ? 241 GLU B C   1 
ATOM   4850 O  O   . GLU B 1 239 ? 73.321 134.000 -86.101  1.00 57.10  ? 241 GLU B O   1 
ATOM   4851 C  CB  . GLU B 1 239 ? 71.871 131.526 -84.828  1.00 57.66  ? 241 GLU B CB  1 
ATOM   4852 C  CG  . GLU B 1 239 ? 71.456 130.101 -84.617  1.00 58.00  ? 241 GLU B CG  1 
ATOM   4853 C  CD  . GLU B 1 239 ? 70.651 129.986 -83.348  1.00 60.21  ? 241 GLU B CD  1 
ATOM   4854 O  OE1 . GLU B 1 239 ? 70.492 131.003 -82.660  1.00 65.34  ? 241 GLU B OE1 1 
ATOM   4855 O  OE2 . GLU B 1 239 ? 70.180 128.905 -83.049  1.00 59.85  ? 241 GLU B OE2 1 
ATOM   4856 N  N   . LYS B 1 240 ? 71.343 133.732 -87.069  1.00 54.27  ? 242 LYS B N   1 
ATOM   4857 C  CA  . LYS B 1 240 ? 71.149 135.169 -87.311  1.00 55.61  ? 242 LYS B CA  1 
ATOM   4858 C  C   . LYS B 1 240 ? 69.697 135.518 -86.972  1.00 51.06  ? 242 LYS B C   1 
ATOM   4859 O  O   . LYS B 1 240 ? 68.756 134.864 -87.456  1.00 47.61  ? 242 LYS B O   1 
ATOM   4860 C  CB  . LYS B 1 240 ? 71.552 135.444 -88.760  1.00 59.59  ? 242 LYS B CB  1 
ATOM   4861 C  CG  . LYS B 1 240 ? 71.919 136.893 -89.055  1.00 64.60  ? 242 LYS B CG  1 
ATOM   4862 C  CD  . LYS B 1 240 ? 72.529 137.122 -90.441  1.00 66.91  ? 242 LYS B CD  1 
ATOM   4863 C  CE  . LYS B 1 240 ? 71.654 136.635 -91.586  1.00 68.28  ? 242 LYS B CE  1 
ATOM   4864 N  NZ  . LYS B 1 240 ? 70.381 137.396 -91.718  1.00 68.30  ? 242 LYS B NZ  1 
ATOM   4865 N  N   . ASP B 1 241 ? 69.522 136.531 -86.152  1.00 49.07  ? 243 ASP B N   1 
ATOM   4866 C  CA  . ASP B 1 241 ? 68.187 136.914 -85.658  1.00 48.22  ? 243 ASP B CA  1 
ATOM   4867 C  C   . ASP B 1 241 ? 67.438 137.527 -86.829  1.00 45.65  ? 243 ASP B C   1 
ATOM   4868 O  O   . ASP B 1 241 ? 67.847 138.588 -87.264  1.00 48.26  ? 243 ASP B O   1 
ATOM   4869 C  CB  . ASP B 1 241 ? 68.292 137.849 -84.454  1.00 50.57  ? 243 ASP B CB  1 
ATOM   4870 C  CG  . ASP B 1 241 ? 66.961 138.135 -83.795  1.00 50.35  ? 243 ASP B CG  1 
ATOM   4871 O  OD1 . ASP B 1 241 ? 65.964 137.609 -84.261  1.00 49.81  ? 243 ASP B OD1 1 
ATOM   4872 O  OD2 . ASP B 1 241 ? 66.939 138.872 -82.817  1.00 54.79  ? 243 ASP B OD2 1 
ATOM   4873 N  N   . ILE B 1 242 ? 66.377 136.869 -87.296  1.00 42.32  ? 244 ILE B N   1 
ATOM   4874 C  CA  . ILE B 1 242 ? 65.529 137.364 -88.415  1.00 39.32  ? 244 ILE B CA  1 
ATOM   4875 C  C   . ILE B 1 242 ? 64.162 137.784 -87.873  1.00 37.43  ? 244 ILE B C   1 
ATOM   4876 O  O   . ILE B 1 242 ? 63.254 138.052 -88.702  1.00 35.85  ? 244 ILE B O   1 
ATOM   4877 C  CB  . ILE B 1 242 ? 65.436 136.303 -89.526  1.00 38.12  ? 244 ILE B CB  1 
ATOM   4878 C  CG1 . ILE B 1 242 ? 64.770 135.002 -89.079  1.00 35.86  ? 244 ILE B CG1 1 
ATOM   4879 C  CG2 . ILE B 1 242 ? 66.818 136.047 -90.087  1.00 39.54  ? 244 ILE B CG2 1 
ATOM   4880 C  CD1 . ILE B 1 242 ? 64.577 133.995 -90.192  1.00 34.29  ? 244 ILE B CD1 1 
ATOM   4881 N  N   . SER B 1 243 ? 64.019 137.845 -86.545  1.00 36.34  ? 245 SER B N   1 
ATOM   4882 C  CA  . SER B 1 243 ? 62.744 138.134 -85.833  1.00 34.77  ? 245 SER B CA  1 
ATOM   4883 C  C   . SER B 1 243 ? 61.980 139.281 -86.495  1.00 35.83  ? 245 SER B C   1 
ATOM   4884 O  O   . SER B 1 243 ? 60.743 139.164 -86.620  1.00 33.94  ? 245 SER B O   1 
ATOM   4885 C  CB  . SER B 1 243 ? 62.964 138.425 -84.386  1.00 34.65  ? 245 SER B CB  1 
ATOM   4886 O  OG  . SER B 1 243 ? 63.272 137.241 -83.675  1.00 33.99  ? 245 SER B OG  1 
ATOM   4887 N  N   . THR B 1 244 ? 62.670 140.322 -86.964  1.00 39.30  ? 246 THR B N   1 
ATOM   4888 C  CA  . THR B 1 244 ? 62.014 141.567 -87.448  1.00 41.18  ? 246 THR B CA  1 
ATOM   4889 C  C   . THR B 1 244 ? 61.124 141.257 -88.659  1.00 39.28  ? 246 THR B C   1 
ATOM   4890 O  O   . THR B 1 244 ? 60.187 142.037 -88.924  1.00 38.16  ? 246 THR B O   1 
ATOM   4891 C  CB  . THR B 1 244 ? 63.048 142.670 -87.699  1.00 45.99  ? 246 THR B CB  1 
ATOM   4892 O  OG1 . THR B 1 244 ? 62.278 143.807 -88.095  1.00 49.42  ? 246 THR B OG1 1 
ATOM   4893 C  CG2 . THR B 1 244 ? 64.084 142.323 -88.747  1.00 47.54  ? 246 THR B CG2 1 
ATOM   4894 N  N   . PHE B 1 245 ? 61.362 140.140 -89.354  1.00 37.15  ? 247 PHE B N   1 
ATOM   4895 C  CA  . PHE B 1 245 ? 60.501 139.691 -90.487  1.00 35.69  ? 247 PHE B CA  1 
ATOM   4896 C  C   . PHE B 1 245 ? 59.218 138.992 -90.019  1.00 33.13  ? 247 PHE B C   1 
ATOM   4897 O  O   . PHE B 1 245 ? 58.289 138.887 -90.822  1.00 32.16  ? 247 PHE B O   1 
ATOM   4898 C  CB  . PHE B 1 245 ? 61.260 138.747 -91.419  1.00 34.79  ? 247 PHE B CB  1 
ATOM   4899 C  CG  . PHE B 1 245 ? 62.280 139.428 -92.288  1.00 35.66  ? 247 PHE B CG  1 
ATOM   4900 C  CD1 . PHE B 1 245 ? 61.884 140.088 -93.433  1.00 36.36  ? 247 PHE B CD1 1 
ATOM   4901 C  CD2 . PHE B 1 245 ? 63.628 139.392 -91.971  1.00 36.57  ? 247 PHE B CD2 1 
ATOM   4902 C  CE1 . PHE B 1 245 ? 62.823 140.675 -94.260  1.00 37.28  ? 247 PHE B CE1 1 
ATOM   4903 C  CE2 . PHE B 1 245 ? 64.567 139.986 -92.791  1.00 37.32  ? 247 PHE B CE2 1 
ATOM   4904 C  CZ  . PHE B 1 245 ? 64.159 140.620 -93.937  1.00 38.37  ? 247 PHE B CZ  1 
ATOM   4905 N  N   . PHE B 1 246 ? 59.187 138.477 -88.791  1.00 32.28  ? 248 PHE B N   1 
ATOM   4906 C  CA  . PHE B 1 246 ? 58.106 137.604 -88.269  1.00 29.68  ? 248 PHE B CA  1 
ATOM   4907 C  C   . PHE B 1 246 ? 57.350 138.344 -87.172  1.00 31.13  ? 248 PHE B C   1 
ATOM   4908 O  O   . PHE B 1 246 ? 57.707 138.248 -86.006  1.00 32.47  ? 248 PHE B O   1 
ATOM   4909 C  CB  . PHE B 1 246 ? 58.693 136.290 -87.753  1.00 27.47  ? 248 PHE B CB  1 
ATOM   4910 C  CG  . PHE B 1 246 ? 59.452 135.485 -88.775  1.00 26.23  ? 248 PHE B CG  1 
ATOM   4911 C  CD1 . PHE B 1 246 ? 60.715 135.864 -89.174  1.00 26.16  ? 248 PHE B CD1 1 
ATOM   4912 C  CD2 . PHE B 1 246 ? 58.896 134.347 -89.341  1.00 24.96  ? 248 PHE B CD2 1 
ATOM   4913 C  CE1 . PHE B 1 246 ? 61.412 135.100 -90.096  1.00 26.47  ? 248 PHE B CE1 1 
ATOM   4914 C  CE2 . PHE B 1 246 ? 59.588 133.596 -90.274  1.00 24.11  ? 248 PHE B CE2 1 
ATOM   4915 C  CZ  . PHE B 1 246 ? 60.853 133.966 -90.638  1.00 24.89  ? 248 PHE B CZ  1 
ATOM   4916 N  N   . PRO B 1 247 ? 56.291 139.125 -87.474  1.00 31.57  ? 249 PRO B N   1 
ATOM   4917 C  CA  . PRO B 1 247 ? 55.420 139.607 -86.404  1.00 32.44  ? 249 PRO B CA  1 
ATOM   4918 C  C   . PRO B 1 247 ? 54.689 138.362 -85.853  1.00 32.53  ? 249 PRO B C   1 
ATOM   4919 O  O   . PRO B 1 247 ? 54.321 137.409 -86.599  1.00 34.50  ? 249 PRO B O   1 
ATOM   4920 C  CB  . PRO B 1 247 ? 54.553 140.662 -87.089  1.00 32.43  ? 249 PRO B CB  1 
ATOM   4921 C  CG  . PRO B 1 247 ? 54.520 140.204 -88.529  1.00 31.36  ? 249 PRO B CG  1 
ATOM   4922 C  CD  . PRO B 1 247 ? 55.855 139.543 -88.810  1.00 30.70  ? 249 PRO B CD  1 
ATOM   4923 N  N   . ILE B 1 248 ? 54.632 138.281 -84.542  1.00 30.92  ? 250 ILE B N   1 
ATOM   4924 C  CA  . ILE B 1 248 ? 54.191 137.081 -83.790  1.00 29.53  ? 250 ILE B CA  1 
ATOM   4925 C  C   . ILE B 1 248 ? 52.975 137.522 -82.994  1.00 29.33  ? 250 ILE B C   1 
ATOM   4926 O  O   . ILE B 1 248 ? 52.998 138.615 -82.439  1.00 30.34  ? 250 ILE B O   1 
ATOM   4927 C  CB  . ILE B 1 248 ? 55.357 136.564 -82.927  1.00 29.92  ? 250 ILE B CB  1 
ATOM   4928 C  CG1 . ILE B 1 248 ? 56.392 135.889 -83.836  1.00 29.39  ? 250 ILE B CG1 1 
ATOM   4929 C  CG2 . ILE B 1 248 ? 54.881 135.649 -81.813  1.00 29.78  ? 250 ILE B CG2 1 
ATOM   4930 C  CD1 . ILE B 1 248 ? 57.703 135.624 -83.169  1.00 29.39  ? 250 ILE B CD1 1 
ATOM   4931 N  N   . SER B 1 249 ? 51.895 136.770 -83.076  1.00 28.85  ? 251 SER B N   1 
ATOM   4932 C  CA  . SER B 1 249 ? 50.676 137.013 -82.282  1.00 29.05  ? 251 SER B CA  1 
ATOM   4933 C  C   . SER B 1 249 ? 50.414 135.799 -81.382  1.00 27.88  ? 251 SER B C   1 
ATOM   4934 O  O   . SER B 1 249 ? 50.864 134.679 -81.662  1.00 26.87  ? 251 SER B O   1 
ATOM   4935 C  CB  . SER B 1 249 ? 49.518 137.367 -83.148  1.00 29.88  ? 251 SER B CB  1 
ATOM   4936 O  OG  . SER B 1 249 ? 49.253 136.313 -84.040  1.00 30.72  ? 251 SER B OG  1 
ATOM   4937 N  N   . TYR B 1 250 ? 49.798 136.086 -80.254  1.00 27.48  ? 252 TYR B N   1 
ATOM   4938 C  CA  . TYR B 1 250 ? 49.362 135.123 -79.226  1.00 26.93  ? 252 TYR B CA  1 
ATOM   4939 C  C   . TYR B 1 250 ? 47.899 135.421 -78.902  1.00 27.95  ? 252 TYR B C   1 
ATOM   4940 O  O   . TYR B 1 250 ? 47.617 136.481 -78.373  1.00 28.26  ? 252 TYR B O   1 
ATOM   4941 C  CB  . TYR B 1 250 ? 50.278 135.273 -78.023  1.00 25.67  ? 252 TYR B CB  1 
ATOM   4942 C  CG  . TYR B 1 250 ? 50.111 134.182 -77.019  1.00 24.62  ? 252 TYR B CG  1 
ATOM   4943 C  CD1 . TYR B 1 250 ? 50.236 132.870 -77.412  1.00 23.66  ? 252 TYR B CD1 1 
ATOM   4944 C  CD2 . TYR B 1 250 ? 49.791 134.455 -75.698  1.00 24.87  ? 252 TYR B CD2 1 
ATOM   4945 C  CE1 . TYR B 1 250 ? 50.065 131.846 -76.508  1.00 23.73  ? 252 TYR B CE1 1 
ATOM   4946 C  CE2 . TYR B 1 250 ? 49.613 133.444 -74.774  1.00 23.89  ? 252 TYR B CE2 1 
ATOM   4947 C  CZ  . TYR B 1 250 ? 49.776 132.141 -75.186  1.00 23.43  ? 252 TYR B CZ  1 
ATOM   4948 O  OH  . TYR B 1 250 ? 49.646 131.099 -74.352  1.00 23.10  ? 252 TYR B OH  1 
ATOM   4949 N  N   . THR B 1 251 ? 46.991 134.565 -79.340  1.00 28.81  ? 253 THR B N   1 
ATOM   4950 C  CA  . THR B 1 251 ? 45.551 134.644 -79.024  1.00 30.63  ? 253 THR B CA  1 
ATOM   4951 C  C   . THR B 1 251 ? 45.045 133.218 -78.892  1.00 29.93  ? 253 THR B C   1 
ATOM   4952 O  O   . THR B 1 251 ? 45.424 132.397 -79.747  1.00 31.45  ? 253 THR B O   1 
ATOM   4953 C  CB  . THR B 1 251 ? 44.722 135.291 -80.132  1.00 35.02  ? 253 THR B CB  1 
ATOM   4954 O  OG1 . THR B 1 251 ? 45.428 136.409 -80.666  1.00 38.70  ? 253 THR B OG1 1 
ATOM   4955 C  CG2 . THR B 1 251 ? 43.354 135.688 -79.611  1.00 37.11  ? 253 THR B CG2 1 
ATOM   4956 N  N   . GLY B 1 252 ? 44.236 132.933 -77.877  1.00 29.76  ? 254 GLY B N   1 
ATOM   4957 C  CA  . GLY B 1 252 ? 43.621 131.609 -77.690  1.00 27.53  ? 254 GLY B CA  1 
ATOM   4958 C  C   . GLY B 1 252 ? 44.669 130.587 -77.342  1.00 25.07  ? 254 GLY B C   1 
ATOM   4959 O  O   . GLY B 1 252 ? 44.482 129.381 -77.696  1.00 24.45  ? 254 GLY B O   1 
ATOM   4960 N  N   . ASN B 1 253 ? 45.735 131.041 -76.684  1.00 22.50  ? 255 ASN B N   1 
ATOM   4961 C  CA  . ASN B 1 253 ? 46.873 130.136 -76.365  1.00 21.33  ? 255 ASN B CA  1 
ATOM   4962 C  C   . ASN B 1 253 ? 47.525 129.624 -77.665  1.00 18.94  ? 255 ASN B C   1 
ATOM   4963 O  O   . ASN B 1 253 ? 48.112 128.534 -77.653  1.00 17.35  ? 255 ASN B O   1 
ATOM   4964 C  CB  . ASN B 1 253 ? 46.438 128.945 -75.479  1.00 20.53  ? 255 ASN B CB  1 
ATOM   4965 C  CG  . ASN B 1 253 ? 46.528 129.273 -74.016  1.00 21.07  ? 255 ASN B CG  1 
ATOM   4966 O  OD1 . ASN B 1 253 ? 45.892 130.242 -73.619  1.00 22.31  ? 255 ASN B OD1 1 
ATOM   4967 N  ND2 . ASN B 1 253 ? 47.297 128.508 -73.242  1.00 18.87  ? 255 ASN B ND2 1 
ATOM   4968 N  N   . VAL B 1 254 ? 47.446 130.377 -78.752  1.00 19.12  ? 256 VAL B N   1 
ATOM   4969 C  CA  . VAL B 1 254 ? 48.047 129.953 -80.053  1.00 18.27  ? 256 VAL B CA  1 
ATOM   4970 C  C   . VAL B 1 254 ? 49.116 130.961 -80.437  1.00 17.91  ? 256 VAL B C   1 
ATOM   4971 O  O   . VAL B 1 254 ? 48.801 132.119 -80.522  1.00 18.51  ? 256 VAL B O   1 
ATOM   4972 C  CB  . VAL B 1 254 ? 46.973 129.832 -81.134  1.00 18.51  ? 256 VAL B CB  1 
ATOM   4973 C  CG1 . VAL B 1 254 ? 47.589 129.715 -82.509  1.00 18.71  ? 256 VAL B CG1 1 
ATOM   4974 C  CG2 . VAL B 1 254 ? 46.092 128.641 -80.844  1.00 18.83  ? 256 VAL B CG2 1 
ATOM   4975 N  N   . ILE B 1 255 ? 50.362 130.547 -80.553  1.00 17.45  ? 257 ILE B N   1 
ATOM   4976 C  CA  . ILE B 1 255 ? 51.418 131.443 -81.092  1.00 18.50  ? 257 ILE B CA  1 
ATOM   4977 C  C   . ILE B 1 255 ? 51.354 131.289 -82.609  1.00 19.05  ? 257 ILE B C   1 
ATOM   4978 O  O   . ILE B 1 255 ? 51.515 130.144 -83.083  1.00 18.52  ? 257 ILE B O   1 
ATOM   4979 C  CB  . ILE B 1 255 ? 52.815 131.079 -80.567  1.00 18.47  ? 257 ILE B CB  1 
ATOM   4980 C  CG1 . ILE B 1 255 ? 52.868 131.025 -79.038  1.00 18.63  ? 257 ILE B CG1 1 
ATOM   4981 C  CG2 . ILE B 1 255 ? 53.868 132.030 -81.141  1.00 18.59  ? 257 ILE B CG2 1 
ATOM   4982 C  CD1 . ILE B 1 255 ? 54.153 130.380 -78.514  1.00 19.19  ? 257 ILE B CD1 1 
ATOM   4983 N  N   . THR B 1 256 ? 51.106 132.366 -83.338  1.00 20.64  ? 258 THR B N   1 
ATOM   4984 C  CA  . THR B 1 256 ? 51.265 132.384 -84.821  1.00 21.60  ? 258 THR B CA  1 
ATOM   4985 C  C   . THR B 1 256 ? 52.561 133.105 -85.172  1.00 23.00  ? 258 THR B C   1 
ATOM   4986 O  O   . THR B 1 256 ? 52.694 134.241 -84.735  1.00 24.10  ? 258 THR B O   1 
ATOM   4987 C  CB  . THR B 1 256 ? 50.055 133.012 -85.506  1.00 22.07  ? 258 THR B CB  1 
ATOM   4988 O  OG1 . THR B 1 256 ? 48.967 132.172 -85.130  1.00 21.46  ? 258 THR B OG1 1 
ATOM   4989 C  CG2 . THR B 1 256 ? 50.153 133.031 -87.020  1.00 22.10  ? 258 THR B CG2 1 
ATOM   4990 N  N   . ILE B 1 257 ? 53.469 132.450 -85.907  1.00 23.59  ? 259 ILE B N   1 
ATOM   4991 C  CA  . ILE B 1 257 ? 54.733 133.047 -86.439  1.00 24.22  ? 259 ILE B CA  1 
ATOM   4992 C  C   . ILE B 1 257 ? 54.664 132.931 -87.959  1.00 23.98  ? 259 ILE B C   1 
ATOM   4993 O  O   . ILE B 1 257 ? 54.512 131.785 -88.459  1.00 22.15  ? 259 ILE B O   1 
ATOM   4994 C  CB  . ILE B 1 257 ? 55.968 132.324 -85.868  1.00 24.95  ? 259 ILE B CB  1 
ATOM   4995 C  CG1 . ILE B 1 257 ? 55.942 132.246 -84.333  1.00 26.10  ? 259 ILE B CG1 1 
ATOM   4996 C  CG2 . ILE B 1 257 ? 57.262 132.964 -86.336  1.00 26.07  ? 259 ILE B CG2 1 
ATOM   4997 C  CD1 . ILE B 1 257 ? 55.660 130.857 -83.813  1.00 25.21  ? 259 ILE B CD1 1 
ATOM   4998 N  N   . THR B 1 258 ? 54.683 134.068 -88.664  1.00 25.29  ? 260 THR B N   1 
ATOM   4999 C  CA  . THR B 1 258 ? 54.606 134.115 -90.154  1.00 25.29  ? 260 THR B CA  1 
ATOM   5000 C  C   . THR B 1 258 ? 55.161 135.437 -90.657  1.00 26.07  ? 260 THR B C   1 
ATOM   5001 O  O   . THR B 1 258 ? 54.817 136.507 -90.151  1.00 26.59  ? 260 THR B O   1 
ATOM   5002 C  CB  . THR B 1 258 ? 53.195 133.849 -90.701  1.00 24.63  ? 260 THR B CB  1 
ATOM   5003 O  OG1 . THR B 1 258 ? 53.303 133.910 -92.121  1.00 24.85  ? 260 THR B OG1 1 
ATOM   5004 C  CG2 . THR B 1 258 ? 52.159 134.837 -90.226  1.00 24.93  ? 260 THR B CG2 1 
ATOM   5005 N  N   . PRO B 1 259 ? 56.045 135.365 -91.671  1.00 26.04  ? 261 PRO B N   1 
ATOM   5006 C  CA  . PRO B 1 259 ? 56.544 136.549 -92.358  1.00 27.70  ? 261 PRO B CA  1 
ATOM   5007 C  C   . PRO B 1 259 ? 55.690 136.916 -93.572  1.00 28.40  ? 261 PRO B C   1 
ATOM   5008 O  O   . PRO B 1 259 ? 56.126 137.828 -94.282  1.00 31.12  ? 261 PRO B O   1 
ATOM   5009 C  CB  . PRO B 1 259 ? 57.913 136.116 -92.862  1.00 27.02  ? 261 PRO B CB  1 
ATOM   5010 C  CG  . PRO B 1 259 ? 57.685 134.651 -93.187  1.00 26.58  ? 261 PRO B CG  1 
ATOM   5011 C  CD  . PRO B 1 259 ? 56.616 134.138 -92.232  1.00 25.59  ? 261 PRO B CD  1 
ATOM   5012 N  N   . GLY B 1 260 ? 54.548 136.224 -93.765  1.00 27.79  ? 262 GLY B N   1 
ATOM   5013 C  CA  . GLY B 1 260 ? 53.677 136.322 -94.953  1.00 27.96  ? 262 GLY B CA  1 
ATOM   5014 C  C   . GLY B 1 260 ? 54.305 135.580 -96.128  1.00 28.24  ? 262 GLY B C   1 
ATOM   5015 O  O   . GLY B 1 260 ? 53.749 134.548 -96.585  1.00 28.42  ? 262 GLY B O   1 
ATOM   5016 N  N   . ASP B 1 261 ? 55.473 136.041 -96.567  1.00 27.13  ? 263 ASP B N   1 
ATOM   5017 C  CA  . ASP B 1 261 ? 56.266 135.330 -97.580  1.00 26.53  ? 263 ASP B CA  1 
ATOM   5018 C  C   . ASP B 1 261 ? 57.679 135.117 -97.042  1.00 25.28  ? 263 ASP B C   1 
ATOM   5019 O  O   . ASP B 1 261 ? 58.329 136.111 -96.730  1.00 25.78  ? 263 ASP B O   1 
ATOM   5020 C  CB  . ASP B 1 261 ? 56.199 136.138 -98.872  1.00 27.71  ? 263 ASP B CB  1 
ATOM   5021 C  CG  . ASP B 1 261 ? 56.877 135.472 -100.043 1.00 28.74  ? 263 ASP B CG  1 
ATOM   5022 O  OD1 . ASP B 1 261 ? 57.337 134.304 -99.913  1.00 28.34  ? 263 ASP B OD1 1 
ATOM   5023 O  OD2 . ASP B 1 261 ? 56.920 136.133 -101.095 1.00 31.46  ? 263 ASP B OD2 1 
ATOM   5024 N  N   . LEU B 1 262 ? 58.145 133.868 -96.962  1.00 24.07  ? 264 LEU B N   1 
ATOM   5025 C  CA  . LEU B 1 262 ? 59.500 133.572 -96.443  1.00 24.22  ? 264 LEU B CA  1 
ATOM   5026 C  C   . LEU B 1 262 ? 60.519 134.086 -97.458  1.00 26.28  ? 264 LEU B C   1 
ATOM   5027 O  O   . LEU B 1 262 ? 61.639 134.378 -97.045  1.00 28.70  ? 264 LEU B O   1 
ATOM   5028 C  CB  . LEU B 1 262 ? 59.662 132.070 -96.190  1.00 23.27  ? 264 LEU B CB  1 
ATOM   5029 C  CG  . LEU B 1 262 ? 60.997 131.638 -95.564  1.00 23.55  ? 264 LEU B CG  1 
ATOM   5030 C  CD1 . LEU B 1 262 ? 61.161 132.214 -94.158  1.00 23.75  ? 264 LEU B CD1 1 
ATOM   5031 C  CD2 . LEU B 1 262 ? 61.114 130.127 -95.499  1.00 22.97  ? 264 LEU B CD2 1 
ATOM   5032 N  N   . LYS B 1 263 ? 60.160 134.236 -98.739  1.00 26.64  ? 265 LYS B N   1 
ATOM   5033 C  CA  . LYS B 1 263 ? 61.105 134.810 -99.734  1.00 28.09  ? 265 LYS B CA  1 
ATOM   5034 C  C   . LYS B 1 263 ? 61.447 136.262 -99.367  1.00 29.50  ? 265 LYS B C   1 
ATOM   5035 O  O   . LYS B 1 263 ? 62.406 136.781 -99.951  1.00 31.07  ? 265 LYS B O   1 
ATOM   5036 C  CB  . LYS B 1 263 ? 60.541 134.791 -101.158 1.00 28.01  ? 265 LYS B CB  1 
ATOM   5037 C  CG  . LYS B 1 263 ? 60.228 133.409 -101.713 1.00 27.83  ? 265 LYS B CG  1 
ATOM   5038 C  CD  . LYS B 1 263 ? 61.441 132.545 -101.959 1.00 27.99  ? 265 LYS B CD  1 
ATOM   5039 C  CE  . LYS B 1 263 ? 61.072 131.245 -102.638 1.00 28.12  ? 265 LYS B CE  1 
ATOM   5040 N  NZ  . LYS B 1 263 ? 62.278 130.510 -103.093 1.00 29.13  ? 265 LYS B NZ  1 
ATOM   5041 N  N   . TYR B 1 264 ? 60.721 136.919 -98.457  1.00 29.01  ? 266 TYR B N   1 
ATOM   5042 C  CA  . TYR B 1 264 ? 61.136 138.261 -97.996  1.00 30.05  ? 266 TYR B CA  1 
ATOM   5043 C  C   . TYR B 1 264 ? 62.522 138.153 -97.363  1.00 32.00  ? 266 TYR B C   1 
ATOM   5044 O  O   . TYR B 1 264 ? 63.280 139.118 -97.433  1.00 33.86  ? 266 TYR B O   1 
ATOM   5045 C  CB  . TYR B 1 264 ? 60.190 138.855 -96.961  1.00 29.86  ? 266 TYR B CB  1 
ATOM   5046 C  CG  . TYR B 1 264 ? 58.863 139.345 -97.459  1.00 29.17  ? 266 TYR B CG  1 
ATOM   5047 C  CD1 . TYR B 1 264 ? 58.759 140.111 -98.603  1.00 29.23  ? 266 TYR B CD1 1 
ATOM   5048 C  CD2 . TYR B 1 264 ? 57.717 139.119 -96.711  1.00 29.26  ? 266 TYR B CD2 1 
ATOM   5049 C  CE1 . TYR B 1 264 ? 57.539 140.571 -99.057  1.00 28.77  ? 266 TYR B CE1 1 
ATOM   5050 C  CE2 . TYR B 1 264 ? 56.486 139.584 -97.142  1.00 29.03  ? 266 TYR B CE2 1 
ATOM   5051 C  CZ  . TYR B 1 264 ? 56.405 140.295 -98.326  1.00 28.38  ? 266 TYR B CZ  1 
ATOM   5052 O  OH  . TYR B 1 264 ? 55.209 140.777 -98.725  1.00 28.23  ? 266 TYR B OH  1 
ATOM   5053 N  N   . VAL B 1 265 ? 62.826 137.025 -96.734  1.00 32.98  ? 267 VAL B N   1 
ATOM   5054 C  CA  . VAL B 1 265 ? 64.154 136.766 -96.110  1.00 35.94  ? 267 VAL B CA  1 
ATOM   5055 C  C   . VAL B 1 265 ? 65.081 136.185 -97.196  1.00 39.71  ? 267 VAL B C   1 
ATOM   5056 O  O   . VAL B 1 265 ? 65.044 134.948 -97.453  1.00 38.12  ? 267 VAL B O   1 
ATOM   5057 C  CB  . VAL B 1 265 ? 64.034 135.849 -94.877  1.00 34.86  ? 267 VAL B CB  1 
ATOM   5058 C  CG1 . VAL B 1 265 ? 65.335 135.816 -94.105  1.00 35.55  ? 267 VAL B CG1 1 
ATOM   5059 C  CG2 . VAL B 1 265 ? 62.888 136.256 -93.952  1.00 33.35  ? 267 VAL B CG2 1 
ATOM   5060 N  N   . GLN B 1 266 ? 65.891 137.054 -97.805  1.00 45.24  ? 268 GLN B N   1 
ATOM   5061 C  CA  . GLN B 1 266 ? 66.677 136.758 -99.034  1.00 51.42  ? 268 GLN B CA  1 
ATOM   5062 C  C   . GLN B 1 266 ? 67.878 135.881 -98.658  1.00 52.52  ? 268 GLN B C   1 
ATOM   5063 O  O   . GLN B 1 266 ? 68.286 135.058 -99.491  1.00 52.63  ? 268 GLN B O   1 
ATOM   5064 C  CB  . GLN B 1 266 ? 67.092 138.056 -99.745  1.00 55.35  ? 268 GLN B CB  1 
ATOM   5065 C  CG  . GLN B 1 266 ? 65.907 138.905 -100.214 1.00 56.25  ? 268 GLN B CG  1 
ATOM   5066 C  CD  . GLN B 1 266 ? 66.312 140.197 -100.891 1.00 59.72  ? 268 GLN B CD  1 
ATOM   5067 O  OE1 . GLN B 1 266 ? 67.272 140.252 -101.658 1.00 65.18  ? 268 GLN B OE1 1 
ATOM   5068 N  NE2 . GLN B 1 266 ? 65.558 141.256 -100.648 1.00 59.29  ? 268 GLN B NE2 1 
ATOM   5069 N  N   . ASP B 1 267 ? 68.370 135.990 -97.428  1.00 53.64  ? 269 ASP B N   1 
ATOM   5070 C  CA  . ASP B 1 267 ? 69.539 135.203 -96.957  1.00 57.37  ? 269 ASP B CA  1 
ATOM   5071 C  C   . ASP B 1 267 ? 69.224 133.690 -96.924  1.00 53.96  ? 269 ASP B C   1 
ATOM   5072 O  O   . ASP B 1 267 ? 70.159 132.880 -96.777  1.00 51.64  ? 269 ASP B O   1 
ATOM   5073 C  CB  . ASP B 1 267 ? 70.003 135.771 -95.614  1.00 63.24  ? 269 ASP B CB  1 
ATOM   5074 C  CG  . ASP B 1 267 ? 70.902 137.008 -95.719  1.00 70.56  ? 269 ASP B CG  1 
ATOM   5075 O  OD1 . ASP B 1 267 ? 71.225 137.434 -96.864  1.00 73.90  ? 269 ASP B OD1 1 
ATOM   5076 O  OD2 . ASP B 1 267 ? 71.298 137.543 -94.647  1.00 74.24  ? 269 ASP B OD2 1 
ATOM   5077 N  N   . VAL B 1 268 ? 67.958 133.300 -97.049  1.00 51.44  ? 270 VAL B N   1 
ATOM   5078 C  CA  . VAL B 1 268 ? 67.507 131.903 -96.796  1.00 48.03  ? 270 VAL B CA  1 
ATOM   5079 C  C   . VAL B 1 268 ? 67.919 131.048 -97.982  1.00 46.35  ? 270 VAL B C   1 
ATOM   5080 O  O   . VAL B 1 268 ? 67.455 131.305 -99.075  1.00 47.16  ? 270 VAL B O   1 
ATOM   5081 C  CB  . VAL B 1 268 ? 65.991 131.833 -96.547  1.00 45.71  ? 270 VAL B CB  1 
ATOM   5082 C  CG1 . VAL B 1 268 ? 65.460 130.415 -96.622  1.00 43.61  ? 270 VAL B CG1 1 
ATOM   5083 C  CG2 . VAL B 1 268 ? 65.651 132.451 -95.204  1.00 47.99  ? 270 VAL B CG2 1 
ATOM   5084 N  N   . LYS B 1 269 ? 68.753 130.051 -97.749  1.00 47.26  ? 271 LYS B N   1 
ATOM   5085 C  CA  . LYS B 1 269 ? 69.054 129.013 -98.759  1.00 46.88  ? 271 LYS B CA  1 
ATOM   5086 C  C   . LYS B 1 269 ? 68.247 127.755 -98.429  1.00 43.36  ? 271 LYS B C   1 
ATOM   5087 O  O   . LYS B 1 269 ? 67.662 127.665 -97.362  1.00 44.14  ? 271 LYS B O   1 
ATOM   5088 C  CB  . LYS B 1 269 ? 70.550 128.684 -98.768  1.00 52.11  ? 271 LYS B CB  1 
ATOM   5089 C  CG  . LYS B 1 269 ? 71.547 129.830 -98.577  1.00 57.45  ? 271 LYS B CG  1 
ATOM   5090 C  CD  . LYS B 1 269 ? 72.989 129.414 -98.997  1.00 63.88  ? 271 LYS B CD  1 
ATOM   5091 C  CE  . LYS B 1 269 ? 74.115 129.779 -98.036  1.00 69.11  ? 271 LYS B CE  1 
ATOM   5092 N  NZ  . LYS B 1 269 ? 74.324 131.247 -97.901  1.00 71.03  ? 271 LYS B NZ  1 
ATOM   5093 N  N   . VAL B 1 270 ? 68.256 126.799 -99.334  1.00 41.28  ? 272 VAL B N   1 
ATOM   5094 C  CA  . VAL B 1 270 ? 67.619 125.462 -99.187  1.00 40.38  ? 272 VAL B CA  1 
ATOM   5095 C  C   . VAL B 1 270 ? 68.196 124.710 -97.964  1.00 40.60  ? 272 VAL B C   1 
ATOM   5096 O  O   . VAL B 1 270 ? 67.525 123.863 -97.369  1.00 37.43  ? 272 VAL B O   1 
ATOM   5097 C  CB  . VAL B 1 270 ? 67.806 124.696 -100.513 1.00 40.34  ? 272 VAL B CB  1 
ATOM   5098 C  CG1 . VAL B 1 270 ? 69.260 124.673 -100.968 1.00 40.69  ? 272 VAL B CG1 1 
ATOM   5099 C  CG2 . VAL B 1 270 ? 67.248 123.294 -100.418 1.00 41.64  ? 272 VAL B CG2 1 
ATOM   5100 N  N   . SER B 1 271 ? 69.439 124.972 -97.596  1.00 42.54  ? 273 SER B N   1 
ATOM   5101 C  CA  . SER B 1 271 ? 70.125 124.267 -96.479  1.00 42.79  ? 273 SER B CA  1 
ATOM   5102 C  C   . SER B 1 271 ? 69.888 125.012 -95.162  1.00 40.95  ? 273 SER B C   1 
ATOM   5103 O  O   . SER B 1 271 ? 70.431 124.571 -94.152  1.00 39.62  ? 273 SER B O   1 
ATOM   5104 C  CB  . SER B 1 271 ? 71.602 124.167 -96.756  1.00 45.20  ? 273 SER B CB  1 
ATOM   5105 O  OG  . SER B 1 271 ? 72.200 125.461 -96.765  1.00 46.03  ? 273 SER B OG  1 
ATOM   5106 N  N   . SER B 1 272 ? 69.134 126.116 -95.184  1.00 39.20  ? 274 SER B N   1 
ATOM   5107 C  CA  . SER B 1 272 ? 68.849 126.945 -93.991  1.00 37.83  ? 274 SER B CA  1 
ATOM   5108 C  C   . SER B 1 272 ? 67.849 126.228 -93.101  1.00 36.09  ? 274 SER B C   1 
ATOM   5109 O  O   . SER B 1 272 ? 66.923 125.567 -93.651  1.00 34.94  ? 274 SER B O   1 
ATOM   5110 C  CB  . SER B 1 272 ? 68.302 128.268 -94.366  1.00 38.12  ? 274 SER B CB  1 
ATOM   5111 O  OG  . SER B 1 272 ? 69.234 128.947 -95.168  1.00 43.00  ? 274 SER B OG  1 
ATOM   5112 N  N   . LYS B 1 273 ? 68.003 126.422 -91.793  1.00 34.71  ? 275 LYS B N   1 
ATOM   5113 C  CA  . LYS B 1 273 ? 66.946 126.115 -90.787  1.00 33.93  ? 275 LYS B CA  1 
ATOM   5114 C  C   . LYS B 1 273 ? 66.306 127.414 -90.271  1.00 30.43  ? 275 LYS B C   1 
ATOM   5115 O  O   . LYS B 1 273 ? 67.033 128.399 -90.102  1.00 29.69  ? 275 LYS B O   1 
ATOM   5116 C  CB  . LYS B 1 273 ? 67.520 125.158 -89.744  1.00 33.88  ? 275 LYS B CB  1 
ATOM   5117 C  CG  . LYS B 1 273 ? 67.701 123.772 -90.334  1.00 35.72  ? 275 LYS B CG  1 
ATOM   5118 C  CD  . LYS B 1 273 ? 68.217 122.733 -89.408  1.00 38.81  ? 275 LYS B CD  1 
ATOM   5119 C  CE  . LYS B 1 273 ? 68.589 121.497 -90.196  1.00 41.60  ? 275 LYS B CE  1 
ATOM   5120 N  NZ  . LYS B 1 273 ? 69.603 120.702 -89.468  1.00 44.38  ? 275 LYS B NZ  1 
ATOM   5121 N  N   . ILE B 1 274 ? 64.974 127.424 -90.144  1.00 27.09  ? 276 ILE B N   1 
ATOM   5122 C  CA  . ILE B 1 274 ? 64.245 128.488 -89.398  1.00 26.21  ? 276 ILE B CA  1 
ATOM   5123 C  C   . ILE B 1 274 ? 64.020 127.958 -87.983  1.00 25.46  ? 276 ILE B C   1 
ATOM   5124 O  O   . ILE B 1 274 ? 63.391 126.894 -87.845  1.00 24.34  ? 276 ILE B O   1 
ATOM   5125 C  CB  . ILE B 1 274 ? 62.927 128.905 -90.071  1.00 25.18  ? 276 ILE B CB  1 
ATOM   5126 C  CG1 . ILE B 1 274 ? 63.087 129.091 -91.586  1.00 25.70  ? 276 ILE B CG1 1 
ATOM   5127 C  CG2 . ILE B 1 274 ? 62.381 130.166 -89.401  1.00 25.07  ? 276 ILE B CG2 1 
ATOM   5128 C  CD1 . ILE B 1 274 ? 63.982 130.246 -91.937  1.00 26.71  ? 276 ILE B CD1 1 
ATOM   5129 N  N   . VAL B 1 275 ? 64.556 128.645 -86.979  1.00 25.51  ? 277 VAL B N   1 
ATOM   5130 C  CA  . VAL B 1 275 ? 64.467 128.168 -85.587  1.00 25.78  ? 277 VAL B CA  1 
ATOM   5131 C  C   . VAL B 1 275 ? 63.790 129.234 -84.725  1.00 25.86  ? 277 VAL B C   1 
ATOM   5132 O  O   . VAL B 1 275 ? 64.208 130.385 -84.744  1.00 25.90  ? 277 VAL B O   1 
ATOM   5133 C  CB  . VAL B 1 275 ? 65.840 127.763 -85.060  1.00 27.12  ? 277 VAL B CB  1 
ATOM   5134 C  CG1 . VAL B 1 275 ? 65.712 127.240 -83.649  1.00 27.41  ? 277 VAL B CG1 1 
ATOM   5135 C  CG2 . VAL B 1 275 ? 66.507 126.745 -85.962  1.00 26.94  ? 277 VAL B CG2 1 
ATOM   5136 N  N   . ILE B 1 276 ? 62.725 128.826 -84.039  1.00 25.91  ? 278 ILE B N   1 
ATOM   5137 C  CA  . ILE B 1 276 ? 61.918 129.687 -83.141  1.00 26.17  ? 278 ILE B CA  1 
ATOM   5138 C  C   . ILE B 1 276 ? 62.329 129.296 -81.744  1.00 25.95  ? 278 ILE B C   1 
ATOM   5139 O  O   . ILE B 1 276 ? 62.349 128.095 -81.454  1.00 26.47  ? 278 ILE B O   1 
ATOM   5140 C  CB  . ILE B 1 276 ? 60.401 129.492 -83.341  1.00 26.49  ? 278 ILE B CB  1 
ATOM   5141 C  CG1 . ILE B 1 276 ? 59.932 129.955 -84.720  1.00 26.56  ? 278 ILE B CG1 1 
ATOM   5142 C  CG2 . ILE B 1 276 ? 59.591 130.167 -82.248  1.00 26.41  ? 278 ILE B CG2 1 
ATOM   5143 C  CD1 . ILE B 1 276 ? 60.221 128.971 -85.794  1.00 26.62  ? 278 ILE B CD1 1 
ATOM   5144 N  N   . ARG B 1 277 ? 62.614 130.281 -80.920  1.00 26.32  ? 279 ARG B N   1 
ATOM   5145 C  CA  . ARG B 1 277 ? 62.802 130.013 -79.479  1.00 27.40  ? 279 ARG B CA  1 
ATOM   5146 C  C   . ARG B 1 277 ? 61.951 130.967 -78.657  1.00 25.82  ? 279 ARG B C   1 
ATOM   5147 O  O   . ARG B 1 277 ? 61.756 132.142 -79.051  1.00 24.87  ? 279 ARG B O   1 
ATOM   5148 C  CB  . ARG B 1 277 ? 64.262 130.113 -79.082  1.00 30.71  ? 279 ARG B CB  1 
ATOM   5149 C  CG  . ARG B 1 277 ? 65.061 128.906 -79.533  1.00 32.82  ? 279 ARG B CG  1 
ATOM   5150 C  CD  . ARG B 1 277 ? 66.458 128.915 -78.964  1.00 35.88  ? 279 ARG B CD  1 
ATOM   5151 N  NE  . ARG B 1 277 ? 67.270 128.101 -79.846  1.00 37.57  ? 279 ARG B NE  1 
ATOM   5152 C  CZ  . ARG B 1 277 ? 68.191 128.581 -80.682  1.00 39.44  ? 279 ARG B CZ  1 
ATOM   5153 N  NH1 . ARG B 1 277 ? 68.446 129.884 -80.727  1.00 40.09  ? 279 ARG B NH1 1 
ATOM   5154 N  NH2 . ARG B 1 277 ? 68.887 127.740 -81.433  1.00 39.68  ? 279 ARG B NH2 1 
ATOM   5155 N  N   . TYR B 1 278 ? 61.406 130.420 -77.588  1.00 23.83  ? 280 TYR B N   1 
ATOM   5156 C  CA  . TYR B 1 278 ? 60.603 131.190 -76.627  1.00 23.34  ? 280 TYR B CA  1 
ATOM   5157 C  C   . TYR B 1 278 ? 60.707 130.456 -75.300  1.00 23.01  ? 280 TYR B C   1 
ATOM   5158 O  O   . TYR B 1 278 ? 61.226 129.308 -75.202  1.00 21.90  ? 280 TYR B O   1 
ATOM   5159 C  CB  . TYR B 1 278 ? 59.161 131.329 -77.110  1.00 22.23  ? 280 TYR B CB  1 
ATOM   5160 C  CG  . TYR B 1 278 ? 58.390 130.038 -77.173  1.00 20.66  ? 280 TYR B CG  1 
ATOM   5161 C  CD1 . TYR B 1 278 ? 58.434 129.278 -78.311  1.00 20.39  ? 280 TYR B CD1 1 
ATOM   5162 C  CD2 . TYR B 1 278 ? 57.616 129.576 -76.122  1.00 19.73  ? 280 TYR B CD2 1 
ATOM   5163 C  CE1 . TYR B 1 278 ? 57.743 128.075 -78.392  1.00 19.85  ? 280 TYR B CE1 1 
ATOM   5164 C  CE2 . TYR B 1 278 ? 56.910 128.389 -76.183  1.00 19.00  ? 280 TYR B CE2 1 
ATOM   5165 C  CZ  . TYR B 1 278 ? 56.986 127.618 -77.328  1.00 18.96  ? 280 TYR B CZ  1 
ATOM   5166 O  OH  . TYR B 1 278 ? 56.324 126.429 -77.485  1.00 17.55  ? 280 TYR B OH  1 
ATOM   5167 N  N   . THR B 1 279 ? 60.195 131.109 -74.292  1.00 23.31  ? 281 THR B N   1 
ATOM   5168 C  CA  . THR B 1 279 ? 60.053 130.462 -72.983  1.00 24.04  ? 281 THR B CA  1 
ATOM   5169 C  C   . THR B 1 279 ? 58.583 130.440 -72.598  1.00 24.40  ? 281 THR B C   1 
ATOM   5170 O  O   . THR B 1 279 ? 57.817 131.317 -73.016  1.00 23.98  ? 281 THR B O   1 
ATOM   5171 C  CB  . THR B 1 279 ? 60.923 131.136 -71.928  1.00 25.34  ? 281 THR B CB  1 
ATOM   5172 O  OG1 . THR B 1 279 ? 60.436 132.468 -71.767  1.00 26.32  ? 281 THR B OG1 1 
ATOM   5173 C  CG2 . THR B 1 279 ? 62.386 131.110 -72.298  1.00 26.06  ? 281 THR B CG2 1 
ATOM   5174 N  N   . ALA B 1 280 ? 58.240 129.473 -71.758  1.00 25.17  ? 282 ALA B N   1 
ATOM   5175 C  CA  . ALA B 1 280 ? 56.919 129.345 -71.125  1.00 24.44  ? 282 ALA B CA  1 
ATOM   5176 C  C   . ALA B 1 280 ? 57.198 128.816 -69.726  1.00 25.32  ? 282 ALA B C   1 
ATOM   5177 O  O   . ALA B 1 280 ? 58.358 128.414 -69.458  1.00 26.29  ? 282 ALA B O   1 
ATOM   5178 C  CB  . ALA B 1 280 ? 56.046 128.441 -71.964  1.00 23.16  ? 282 ALA B CB  1 
ATOM   5179 N  N   . ARG B 1 281 ? 56.221 128.871 -68.847  1.00 25.80  ? 283 ARG B N   1 
ATOM   5180 C  CA  . ARG B 1 281 ? 56.379 128.308 -67.476  1.00 26.74  ? 283 ARG B CA  1 
ATOM   5181 C  C   . ARG B 1 281 ? 55.092 127.619 -67.075  1.00 23.90  ? 283 ARG B C   1 
ATOM   5182 O  O   . ARG B 1 281 ? 54.008 128.154 -67.377  1.00 24.11  ? 283 ARG B O   1 
ATOM   5183 C  CB  . ARG B 1 281 ? 56.771 129.390 -66.477  1.00 30.38  ? 283 ARG B CB  1 
ATOM   5184 C  CG  . ARG B 1 281 ? 55.801 130.552 -66.412  1.00 33.81  ? 283 ARG B CG  1 
ATOM   5185 C  CD  . ARG B 1 281 ? 56.325 131.735 -65.611  1.00 37.70  ? 283 ARG B CD  1 
ATOM   5186 N  NE  . ARG B 1 281 ? 55.370 132.788 -65.872  1.00 39.73  ? 283 ARG B NE  1 
ATOM   5187 C  CZ  . ARG B 1 281 ? 54.215 132.908 -65.242  1.00 41.89  ? 283 ARG B CZ  1 
ATOM   5188 N  NH1 . ARG B 1 281 ? 53.903 132.084 -64.245  1.00 42.51  ? 283 ARG B NH1 1 
ATOM   5189 N  NH2 . ARG B 1 281 ? 53.396 133.882 -65.601  1.00 43.62  ? 283 ARG B NH2 1 
ATOM   5190 N  N   . LEU B 1 282 ? 55.207 126.445 -66.479  1.00 23.13  ? 284 LEU B N   1 
ATOM   5191 C  CA  . LEU B 1 282 ? 54.053 125.797 -65.798  1.00 22.53  ? 284 LEU B CA  1 
ATOM   5192 C  C   . LEU B 1 282 ? 53.374 126.779 -64.828  1.00 21.82  ? 284 LEU B C   1 
ATOM   5193 O  O   . LEU B 1 282 ? 54.088 127.523 -64.105  1.00 22.87  ? 284 LEU B O   1 
ATOM   5194 C  CB  . LEU B 1 282 ? 54.558 124.560 -65.064  1.00 22.28  ? 284 LEU B CB  1 
ATOM   5195 C  CG  . LEU B 1 282 ? 54.825 123.343 -65.933  1.00 22.34  ? 284 LEU B CG  1 
ATOM   5196 C  CD1 . LEU B 1 282 ? 55.533 122.264 -65.135  1.00 22.82  ? 284 LEU B CD1 1 
ATOM   5197 C  CD2 . LEU B 1 282 ? 53.543 122.794 -66.527  1.00 21.94  ? 284 LEU B CD2 1 
ATOM   5198 N  N   . ASN B 1 283 ? 52.047 126.775 -64.804  1.00 21.03  ? 285 ASN B N   1 
ATOM   5199 C  CA  . ASN B 1 283 ? 51.224 127.586 -63.863  1.00 21.64  ? 285 ASN B CA  1 
ATOM   5200 C  C   . ASN B 1 283 ? 50.369 126.660 -62.976  1.00 22.36  ? 285 ASN B C   1 
ATOM   5201 O  O   . ASN B 1 283 ? 50.511 125.406 -63.049  1.00 21.57  ? 285 ASN B O   1 
ATOM   5202 C  CB  . ASN B 1 283 ? 50.352 128.567 -64.640  1.00 21.29  ? 285 ASN B CB  1 
ATOM   5203 C  CG  . ASN B 1 283 ? 49.436 127.855 -65.619  1.00 20.10  ? 285 ASN B CG  1 
ATOM   5204 O  OD1 . ASN B 1 283 ? 48.709 126.934 -65.239  1.00 19.30  ? 285 ASN B OD1 1 
ATOM   5205 N  ND2 . ASN B 1 283 ? 49.474 128.271 -66.874  1.00 18.76  ? 285 ASN B ND2 1 
ATOM   5206 N  N   . ASP B 1 284 ? 49.499 127.228 -62.139  1.00 24.62  ? 286 ASP B N   1 
ATOM   5207 C  CA  . ASP B 1 284 ? 48.781 126.456 -61.078  1.00 25.23  ? 286 ASP B CA  1 
ATOM   5208 C  C   . ASP B 1 284 ? 47.821 125.458 -61.730  1.00 24.62  ? 286 ASP B C   1 
ATOM   5209 O  O   . ASP B 1 284 ? 47.570 124.391 -61.148  1.00 24.52  ? 286 ASP B O   1 
ATOM   5210 C  CB  . ASP B 1 284 ? 48.101 127.409 -60.108  1.00 27.47  ? 286 ASP B CB  1 
ATOM   5211 C  CG  . ASP B 1 284 ? 49.115 128.243 -59.328  1.00 30.40  ? 286 ASP B CG  1 
ATOM   5212 O  OD1 . ASP B 1 284 ? 50.254 127.702 -59.075  1.00 30.72  ? 286 ASP B OD1 1 
ATOM   5213 O  OD2 . ASP B 1 284 ? 48.780 129.456 -58.980  1.00 32.93  ? 286 ASP B OD2 1 
ATOM   5214 N  N   . ASP B 1 285 ? 47.394 125.736 -62.955  1.00 23.57  ? 287 ASP B N   1 
ATOM   5215 C  CA  . ASP B 1 285 ? 46.476 124.861 -63.722  1.00 23.56  ? 287 ASP B CA  1 
ATOM   5216 C  C   . ASP B 1 285 ? 47.232 123.692 -64.387  1.00 21.04  ? 287 ASP B C   1 
ATOM   5217 O  O   . ASP B 1 285 ? 46.600 122.900 -65.105  1.00 19.78  ? 287 ASP B O   1 
ATOM   5218 C  CB  . ASP B 1 285 ? 45.719 125.686 -64.758  1.00 25.92  ? 287 ASP B CB  1 
ATOM   5219 C  CG  . ASP B 1 285 ? 44.945 126.852 -64.165  1.00 28.82  ? 287 ASP B CG  1 
ATOM   5220 O  OD1 . ASP B 1 285 ? 44.320 126.673 -63.118  1.00 31.67  ? 287 ASP B OD1 1 
ATOM   5221 O  OD2 . ASP B 1 285 ? 44.946 127.931 -64.778  1.00 34.06  ? 287 ASP B OD2 1 
ATOM   5222 N  N   . ALA B 1 286 ? 48.519 123.524 -64.121  1.00 18.98  ? 288 ALA B N   1 
ATOM   5223 C  CA  . ALA B 1 286 ? 49.294 122.443 -64.738  1.00 18.41  ? 288 ALA B CA  1 
ATOM   5224 C  C   . ALA B 1 286 ? 48.635 121.098 -64.447  1.00 17.68  ? 288 ALA B C   1 
ATOM   5225 O  O   . ALA B 1 286 ? 48.130 120.890 -63.376  1.00 18.23  ? 288 ALA B O   1 
ATOM   5226 C  CB  . ALA B 1 286 ? 50.718 122.488 -64.237  1.00 18.80  ? 288 ALA B CB  1 
ATOM   5227 N  N   . VAL B 1 287 ? 48.742 120.175 -65.372  1.00 17.05  ? 289 VAL B N   1 
ATOM   5228 C  CA  . VAL B 1 287 ? 48.374 118.748 -65.182  1.00 17.17  ? 289 VAL B CA  1 
ATOM   5229 C  C   . VAL B 1 287 ? 49.519 118.051 -64.449  1.00 17.39  ? 289 VAL B C   1 
ATOM   5230 O  O   . VAL B 1 287 ? 50.717 118.230 -64.817  1.00 17.23  ? 289 VAL B O   1 
ATOM   5231 C  CB  . VAL B 1 287 ? 48.073 118.103 -66.549  1.00 17.30  ? 289 VAL B CB  1 
ATOM   5232 C  CG1 . VAL B 1 287 ? 47.964 116.584 -66.496  1.00 17.59  ? 289 VAL B CG1 1 
ATOM   5233 C  CG2 . VAL B 1 287 ? 46.830 118.722 -67.196  1.00 17.63  ? 289 VAL B CG2 1 
ATOM   5234 N  N   . MET B 1 288 ? 49.146 117.222 -63.487  1.00 17.90  ? 290 MET B N   1 
ATOM   5235 C  CA  . MET B 1 288 ? 50.086 116.405 -62.689  1.00 18.63  ? 290 MET B CA  1 
ATOM   5236 C  C   . MET B 1 288 ? 50.215 115.015 -63.318  1.00 18.10  ? 290 MET B C   1 
ATOM   5237 O  O   . MET B 1 288 ? 49.215 114.313 -63.460  1.00 18.56  ? 290 MET B O   1 
ATOM   5238 C  CB  . MET B 1 288 ? 49.652 116.277 -61.209  1.00 19.37  ? 290 MET B CB  1 
ATOM   5239 C  CG  . MET B 1 288 ? 49.212 117.593 -60.567  1.00 19.54  ? 290 MET B CG  1 
ATOM   5240 S  SD  . MET B 1 288 ? 50.634 118.588 -60.155  1.00 21.68  ? 290 MET B SD  1 
ATOM   5241 C  CE  . MET B 1 288 ? 50.350 120.101 -61.067  1.00 22.19  ? 290 MET B CE  1 
ATOM   5242 N  N   . GLY B 1 289 ? 51.447 114.605 -63.581  1.00 17.87  ? 291 GLY B N   1 
ATOM   5243 C  CA  . GLY B 1 289 ? 51.723 113.283 -64.154  1.00 18.59  ? 291 GLY B CA  1 
ATOM   5244 C  C   . GLY B 1 289 ? 50.953 113.124 -65.463  1.00 18.63  ? 291 GLY B C   1 
ATOM   5245 O  O   . GLY B 1 289 ? 50.887 114.158 -66.218  1.00 16.83  ? 291 GLY B O   1 
ATOM   5246 N  N   . GLY B 1 290 ? 50.425 111.900 -65.680  1.00 19.06  ? 292 GLY B N   1 
ATOM   5247 C  CA  . GLY B 1 290 ? 49.470 111.543 -66.733  1.00 19.47  ? 292 GLY B CA  1 
ATOM   5248 C  C   . GLY B 1 290 ? 49.952 111.974 -68.110  1.00 19.49  ? 292 GLY B C   1 
ATOM   5249 O  O   . GLY B 1 290 ? 51.143 111.745 -68.434  1.00 20.34  ? 292 GLY B O   1 
ATOM   5250 N  N   . LEU B 1 291 ? 49.092 112.630 -68.878  1.00 18.59  ? 293 LEU B N   1 
ATOM   5251 C  CA  . LEU B 1 291 ? 49.364 113.006 -70.296  1.00 18.75  ? 293 LEU B CA  1 
ATOM   5252 C  C   . LEU B 1 291 ? 50.168 114.309 -70.315  1.00 17.64  ? 293 LEU B C   1 
ATOM   5253 O  O   . LEU B 1 291 ? 50.469 114.803 -71.391  1.00 18.01  ? 293 LEU B O   1 
ATOM   5254 C  CB  . LEU B 1 291 ? 48.011 113.123 -71.004  1.00 18.71  ? 293 LEU B CB  1 
ATOM   5255 C  CG  . LEU B 1 291 ? 47.163 111.843 -70.992  1.00 20.08  ? 293 LEU B CG  1 
ATOM   5256 C  CD1 . LEU B 1 291 ? 45.931 111.992 -71.875  1.00 20.74  ? 293 LEU B CD1 1 
ATOM   5257 C  CD2 . LEU B 1 291 ? 47.970 110.664 -71.494  1.00 21.13  ? 293 LEU B CD2 1 
ATOM   5258 N  N   . GLY B 1 292 ? 50.472 114.855 -69.144  1.00 16.75  ? 294 GLY B N   1 
ATOM   5259 C  CA  . GLY B 1 292 ? 51.316 116.054 -69.019  1.00 15.89  ? 294 GLY B CA  1 
ATOM   5260 C  C   . GLY B 1 292 ? 50.710 117.304 -69.650  1.00 14.66  ? 294 GLY B C   1 
ATOM   5261 O  O   . GLY B 1 292 ? 49.478 117.386 -69.806  1.00 13.82  ? 294 GLY B O   1 
ATOM   5262 N  N   . ASN B 1 293 ? 51.583 118.263 -69.953  1.00 14.35  ? 295 ASN B N   1 
ATOM   5263 C  CA  . ASN B 1 293 ? 51.193 119.600 -70.445  1.00 14.62  ? 295 ASN B CA  1 
ATOM   5264 C  C   . ASN B 1 293 ? 51.742 119.775 -71.854  1.00 14.90  ? 295 ASN B C   1 
ATOM   5265 O  O   . ASN B 1 293 ? 52.813 120.348 -72.060  1.00 15.88  ? 295 ASN B O   1 
ATOM   5266 C  CB  . ASN B 1 293 ? 51.675 120.650 -69.461  1.00 14.44  ? 295 ASN B CB  1 
ATOM   5267 C  CG  . ASN B 1 293 ? 51.180 120.402 -68.039  1.00 14.82  ? 295 ASN B CG  1 
ATOM   5268 O  OD1 . ASN B 1 293 ? 50.118 120.892 -67.672  1.00 15.44  ? 295 ASN B OD1 1 
ATOM   5269 N  ND2 . ASN B 1 293 ? 51.891 119.606 -67.266  1.00 13.75  ? 295 ASN B ND2 1 
ATOM   5270 N  N   . PRO B 1 294 ? 51.123 119.201 -72.900  1.00 15.17  ? 296 PRO B N   1 
ATOM   5271 C  CA  . PRO B 1 294 ? 51.764 119.231 -74.212  1.00 15.41  ? 296 PRO B CA  1 
ATOM   5272 C  C   . PRO B 1 294 ? 51.525 120.530 -74.979  1.00 15.09  ? 296 PRO B C   1 
ATOM   5273 O  O   . PRO B 1 294 ? 50.499 121.065 -74.837  1.00 15.80  ? 296 PRO B O   1 
ATOM   5274 C  CB  . PRO B 1 294 ? 51.156 118.050 -74.969  1.00 15.59  ? 296 PRO B CB  1 
ATOM   5275 C  CG  . PRO B 1 294 ? 49.840 117.793 -74.286  1.00 15.87  ? 296 PRO B CG  1 
ATOM   5276 C  CD  . PRO B 1 294 ? 49.906 118.388 -72.888  1.00 15.47  ? 296 PRO B CD  1 
ATOM   5277 N  N   . ASN B 1 295 ? 52.526 121.014 -75.713  1.00 14.79  ? 297 ASN B N   1 
ATOM   5278 C  CA  . ASN B 1 295 ? 52.361 122.080 -76.735  1.00 14.03  ? 297 ASN B CA  1 
ATOM   5279 C  C   . ASN B 1 295 ? 52.578 121.435 -78.108  1.00 14.13  ? 297 ASN B C   1 
ATOM   5280 O  O   . ASN B 1 295 ? 53.495 120.598 -78.259  1.00 14.35  ? 297 ASN B O   1 
ATOM   5281 C  CB  . ASN B 1 295 ? 53.270 123.275 -76.501  1.00 13.88  ? 297 ASN B CB  1 
ATOM   5282 C  CG  . ASN B 1 295 ? 54.727 122.976 -76.792  1.00 14.60  ? 297 ASN B CG  1 
ATOM   5283 O  OD1 . ASN B 1 295 ? 55.346 122.193 -76.080  1.00 14.06  ? 297 ASN B OD1 1 
ATOM   5284 N  N   . ILE B 1 296 ? 51.709 121.783 -79.049  1.00 13.72  ? 298 ILE B N   1 
ATOM   5285 C  CA  . ILE B 1 296 ? 51.578 121.118 -80.360  1.00 13.90  ? 298 ILE B CA  1 
ATOM   5286 C  C   . ILE B 1 296 ? 51.769 122.181 -81.423  1.00 13.97  ? 298 ILE B C   1 
ATOM   5287 O  O   . ILE B 1 296 ? 51.029 123.165 -81.368  1.00 14.13  ? 298 ILE B O   1 
ATOM   5288 C  CB  . ILE B 1 296 ? 50.223 120.422 -80.491  1.00 13.81  ? 298 ILE B CB  1 
ATOM   5289 C  CG1 . ILE B 1 296 ? 50.041 119.414 -79.370  1.00 14.09  ? 298 ILE B CG1 1 
ATOM   5290 C  CG2 . ILE B 1 296 ? 50.146 119.751 -81.841  1.00 14.22  ? 298 ILE B CG2 1 
ATOM   5291 C  CD1 . ILE B 1 296 ? 48.687 118.810 -79.330  1.00 14.53  ? 298 ILE B CD1 1 
ATOM   5292 N  N   . ALA B 1 297 ? 52.737 121.994 -82.305  1.00 14.32  ? 299 ALA B N   1 
ATOM   5293 C  CA  . ALA B 1 297 ? 53.041 122.936 -83.408  1.00 14.87  ? 299 ALA B CA  1 
ATOM   5294 C  C   . ALA B 1 297 ? 52.794 122.283 -84.776  1.00 16.23  ? 299 ALA B C   1 
ATOM   5295 O  O   . ALA B 1 297 ? 52.953 121.060 -84.923  1.00 15.28  ? 299 ALA B O   1 
ATOM   5296 C  CB  . ALA B 1 297 ? 54.458 123.390 -83.257  1.00 14.69  ? 299 ALA B CB  1 
ATOM   5297 N  N   . ARG B 1 298 ? 52.381 123.085 -85.745  1.00 18.43  ? 300 ARG B N   1 
ATOM   5298 C  CA  . ARG B 1 298 ? 52.374 122.657 -87.156  1.00 21.69  ? 300 ARG B CA  1 
ATOM   5299 C  C   . ARG B 1 298 ? 52.791 123.844 -88.034  1.00 20.50  ? 300 ARG B C   1 
ATOM   5300 O  O   . ARG B 1 298 ? 52.670 124.992 -87.570  1.00 19.39  ? 300 ARG B O   1 
ATOM   5301 C  CB  . ARG B 1 298 ? 51.036 122.020 -87.526  1.00 26.05  ? 300 ARG B CB  1 
ATOM   5302 C  CG  . ARG B 1 298 ? 49.901 123.018 -87.589  1.00 32.22  ? 300 ARG B CG  1 
ATOM   5303 C  CD  . ARG B 1 298 ? 48.533 122.363 -87.737  1.00 40.19  ? 300 ARG B CD  1 
ATOM   5304 N  NE  . ARG B 1 298 ? 47.439 123.351 -87.799  1.00 48.07  ? 300 ARG B NE  1 
ATOM   5305 C  CZ  . ARG B 1 298 ? 46.966 124.086 -86.770  1.00 53.69  ? 300 ARG B CZ  1 
ATOM   5306 N  NH1 . ARG B 1 298 ? 47.474 123.974 -85.545  1.00 52.92  ? 300 ARG B NH1 1 
ATOM   5307 N  NH2 . ARG B 1 298 ? 45.965 124.929 -86.983  1.00 54.82  ? 300 ARG B NH2 1 
ATOM   5308 N  N   . LEU B 1 299 ? 53.303 123.523 -89.237  1.00 20.02  ? 301 LEU B N   1 
ATOM   5309 C  CA  . LEU B 1 299 ? 53.755 124.464 -90.294  1.00 19.11  ? 301 LEU B CA  1 
ATOM   5310 C  C   . LEU B 1 299 ? 52.800 124.338 -91.464  1.00 18.69  ? 301 LEU B C   1 
ATOM   5311 O  O   . LEU B 1 299 ? 52.516 123.236 -91.907  1.00 18.30  ? 301 LEU B O   1 
ATOM   5312 C  CB  . LEU B 1 299 ? 55.192 124.139 -90.705  1.00 19.02  ? 301 LEU B CB  1 
ATOM   5313 C  CG  . LEU B 1 299 ? 55.756 124.852 -91.934  1.00 18.95  ? 301 LEU B CG  1 
ATOM   5314 C  CD1 . LEU B 1 299 ? 56.071 126.327 -91.680  1.00 18.94  ? 301 LEU B CD1 1 
ATOM   5315 C  CD2 . LEU B 1 299 ? 57.033 124.155 -92.329  1.00 18.90  ? 301 LEU B CD2 1 
ATOM   5316 N  N   . THR B 1 300 ? 52.251 125.465 -91.858  1.00 18.61  ? 302 THR B N   1 
ATOM   5317 C  CA  . THR B 1 300 ? 51.496 125.641 -93.106  1.00 18.66  ? 302 THR B CA  1 
ATOM   5318 C  C   . THR B 1 300 ? 52.476 126.202 -94.129  1.00 18.20  ? 302 THR B C   1 
ATOM   5319 O  O   . THR B 1 300 ? 53.075 127.285 -93.857  1.00 18.15  ? 302 THR B O   1 
ATOM   5320 C  CB  . THR B 1 300 ? 50.299 126.569 -92.916  1.00 19.47  ? 302 THR B CB  1 
ATOM   5321 O  OG1 . THR B 1 300 ? 49.464 125.823 -92.030  1.00 19.65  ? 302 THR B OG1 1 
ATOM   5322 C  CG2 . THR B 1 300 ? 49.620 126.923 -94.224  1.00 19.69  ? 302 THR B CG2 1 
ATOM   5323 N  N   . TYR B 1 301 ? 52.626 125.503 -95.252  1.00 17.57  ? 303 TYR B N   1 
ATOM   5324 C  CA  . TYR B 1 301 ? 53.665 125.799 -96.258  1.00 17.20  ? 303 TYR B CA  1 
ATOM   5325 C  C   . TYR B 1 301 ? 53.073 125.714 -97.671  1.00 17.33  ? 303 TYR B C   1 
ATOM   5326 O  O   . TYR B 1 301 ? 52.208 124.893 -97.960  1.00 16.99  ? 303 TYR B O   1 
ATOM   5327 C  CB  . TYR B 1 301 ? 54.827 124.826 -96.028  1.00 17.01  ? 303 TYR B CB  1 
ATOM   5328 C  CG  . TYR B 1 301 ? 54.461 123.370 -96.196  1.00 17.14  ? 303 TYR B CG  1 
ATOM   5329 C  CD1 . TYR B 1 301 ? 54.016 122.619 -95.129  1.00 16.89  ? 303 TYR B CD1 1 
ATOM   5330 C  CD2 . TYR B 1 301 ? 54.512 122.748 -97.435  1.00 17.36  ? 303 TYR B CD2 1 
ATOM   5331 C  CE1 . TYR B 1 301 ? 53.671 121.284 -95.259  1.00 17.31  ? 303 TYR B CE1 1 
ATOM   5332 C  CE2 . TYR B 1 301 ? 54.191 121.405 -97.580  1.00 18.05  ? 303 TYR B CE2 1 
ATOM   5333 C  CZ  . TYR B 1 301 ? 53.778 120.666 -96.482  1.00 17.98  ? 303 TYR B CZ  1 
ATOM   5334 O  OH  . TYR B 1 301 ? 53.411 119.361 -96.596  1.00 19.00  ? 303 TYR B OH  1 
ATOM   5335 N  N   . SER B 1 302 ? 53.565 126.564 -98.551  1.00 17.50  ? 304 SER B N   1 
ATOM   5336 C  CA  . SER B 1 302 ? 53.339 126.489 -100.015 1.00 17.98  ? 304 SER B CA  1 
ATOM   5337 C  C   . SER B 1 302 ? 53.767 125.106 -100.499 1.00 18.32  ? 304 SER B C   1 
ATOM   5338 O  O   . SER B 1 302 ? 54.936 124.724 -100.255 1.00 18.00  ? 304 SER B O   1 
ATOM   5339 C  CB  . SER B 1 302 ? 54.071 127.608 -100.637 1.00 17.72  ? 304 SER B CB  1 
ATOM   5340 O  OG  . SER B 1 302 ? 53.261 128.774 -100.531 1.00 18.06  ? 304 SER B OG  1 
ATOM   5341 N  N   . ASN B 1 303 ? 52.843 124.322 -101.055 1.00 19.05  ? 305 ASN B N   1 
ATOM   5342 C  CA  . ASN B 1 303 ? 53.154 122.901 -101.392 1.00 20.29  ? 305 ASN B CA  1 
ATOM   5343 C  C   . ASN B 1 303 ? 53.226 122.680 -102.921 1.00 21.80  ? 305 ASN B C   1 
ATOM   5344 O  O   . ASN B 1 303 ? 53.384 121.475 -103.301 1.00 22.16  ? 305 ASN B O   1 
ATOM   5345 C  CB  . ASN B 1 303 ? 52.165 121.930 -100.739 1.00 20.11  ? 305 ASN B CB  1 
ATOM   5346 C  CG  . ASN B 1 303 ? 50.754 122.184 -101.196 1.00 21.33  ? 305 ASN B CG  1 
ATOM   5347 O  OD1 . ASN B 1 303 ? 50.409 123.255 -101.701 1.00 21.51  ? 305 ASN B OD1 1 
ATOM   5348 N  ND2 . ASN B 1 303 ? 49.905 121.198 -101.015 1.00 23.47  ? 305 ASN B ND2 1 
ATOM   5349 N  N   . ASP B 1 304 ? 53.063 123.729 -103.774 1.00 22.52  ? 306 ASP B N   1 
ATOM   5350 C  CA  . ASP B 1 304 ? 53.048 123.540 -105.263 1.00 23.38  ? 306 ASP B CA  1 
ATOM   5351 C  C   . ASP B 1 304 ? 54.026 124.487 -105.974 1.00 23.34  ? 306 ASP B C   1 
ATOM   5352 O  O   . ASP B 1 304 ? 53.725 125.656 -106.234 1.00 22.44  ? 306 ASP B O   1 
ATOM   5353 C  CB  . ASP B 1 304 ? 51.632 123.574 -105.845 1.00 23.90  ? 306 ASP B CB  1 
ATOM   5354 C  CG  . ASP B 1 304 ? 51.620 123.137 -107.317 1.00 25.04  ? 306 ASP B CG  1 
ATOM   5355 O  OD1 . ASP B 1 304 ? 52.693 122.867 -107.869 1.00 23.40  ? 306 ASP B OD1 1 
ATOM   5356 O  OD2 . ASP B 1 304 ? 50.529 123.050 -107.889 1.00 27.31  ? 306 ASP B OD2 1 
ATOM   5357 N  N   . PRO B 1 305 ? 55.208 123.977 -106.398 1.00 23.93  ? 307 PRO B N   1 
ATOM   5358 C  CA  . PRO B 1 305 ? 56.219 124.814 -107.023 1.00 25.51  ? 307 PRO B CA  1 
ATOM   5359 C  C   . PRO B 1 305 ? 55.897 125.230 -108.470 1.00 26.36  ? 307 PRO B C   1 
ATOM   5360 O  O   . PRO B 1 305 ? 56.636 126.044 -108.996 1.00 27.44  ? 307 PRO B O   1 
ATOM   5361 C  CB  . PRO B 1 305 ? 57.473 123.936 -106.964 1.00 25.40  ? 307 PRO B CB  1 
ATOM   5362 C  CG  . PRO B 1 305 ? 56.943 122.560 -107.074 1.00 25.31  ? 307 PRO B CG  1 
ATOM   5363 C  CD  . PRO B 1 305 ? 55.621 122.574 -106.349 1.00 24.60  ? 307 PRO B CD  1 
ATOM   5364 N  N   . ASN B 1 306 ? 54.766 124.788 -109.017 1.00 27.69  ? 308 ASN B N   1 
ATOM   5365 C  CA  . ASN B 1 306 ? 54.395 125.001 -110.436 1.00 30.28  ? 308 ASN B CA  1 
ATOM   5366 C  C   . ASN B 1 306 ? 53.631 126.306 -110.620 1.00 35.96  ? 308 ASN B C   1 
ATOM   5367 O  O   . ASN B 1 306 ? 52.409 126.306 -110.403 1.00 39.70  ? 308 ASN B O   1 
ATOM   5368 C  CB  . ASN B 1 306 ? 53.578 123.834 -110.959 1.00 28.64  ? 308 ASN B CB  1 
ATOM   5369 C  CG  . ASN B 1 306 ? 54.407 122.577 -110.871 1.00 27.93  ? 308 ASN B CG  1 
ATOM   5370 O  OD1 . ASN B 1 306 ? 55.369 122.441 -111.623 1.00 25.47  ? 308 ASN B OD1 1 
ATOM   5371 N  ND2 . ASN B 1 306 ? 54.092 121.704 -109.915 1.00 26.17  ? 308 ASN B ND2 1 
ATOM   5372 N  N   . GLY B 1 307 ? 54.330 127.354 -111.069 1.00 41.85  ? 309 GLY B N   1 
ATOM   5373 C  CA  . GLY B 1 307 ? 53.731 128.601 -111.573 1.00 46.52  ? 309 GLY B CA  1 
ATOM   5374 C  C   . GLY B 1 307 ? 53.176 129.443 -110.447 1.00 52.41  ? 309 GLY B C   1 
ATOM   5375 O  O   . GLY B 1 307 ? 53.686 129.313 -109.328 1.00 56.79  ? 309 GLY B O   1 
ATOM   5376 N  N   . PHE B 1 308 ? 52.116 130.196 -110.740 1.00 60.27  ? 310 PHE B N   1 
ATOM   5377 C  CA  . PHE B 1 308 ? 51.549 131.336 -109.968 1.00 63.49  ? 310 PHE B CA  1 
ATOM   5378 C  C   . PHE B 1 308 ? 50.552 130.815 -108.920 1.00 61.63  ? 310 PHE B C   1 
ATOM   5379 O  O   . PHE B 1 308 ? 49.419 131.254 -108.931 1.00 65.82  ? 310 PHE B O   1 
ATOM   5380 C  CB  . PHE B 1 308 ? 50.863 132.291 -110.963 1.00 71.30  ? 310 PHE B CB  1 
ATOM   5381 C  CG  . PHE B 1 308 ? 49.928 131.644 -111.978 1.00 76.39  ? 310 PHE B CG  1 
ATOM   5382 C  CD1 . PHE B 1 308 ? 50.419 131.113 -113.174 1.00 78.10  ? 310 PHE B CD1 1 
ATOM   5383 C  CD2 . PHE B 1 308 ? 48.545 131.580 -111.770 1.00 78.53  ? 310 PHE B CD2 1 
ATOM   5384 C  CE1 . PHE B 1 308 ? 49.568 130.518 -114.104 1.00 77.75  ? 310 PHE B CE1 1 
ATOM   5385 C  CE2 . PHE B 1 308 ? 47.696 130.982 -112.700 1.00 78.33  ? 310 PHE B CE2 1 
ATOM   5386 C  CZ  . PHE B 1 308 ? 48.208 130.448 -113.863 1.00 77.17  ? 310 PHE B CZ  1 
ATOM   5387 N  N   . THR B 1 309 ? 50.925 129.882 -108.051 1.00 61.75  ? 311 THR B N   1 
ATOM   5388 C  CA  . THR B 1 309 ? 49.956 129.087 -107.246 1.00 61.37  ? 311 THR B CA  1 
ATOM   5389 C  C   . THR B 1 309 ? 50.103 129.402 -105.759 1.00 56.82  ? 311 THR B C   1 
ATOM   5390 O  O   . THR B 1 309 ? 51.186 129.833 -105.343 1.00 57.78  ? 311 THR B O   1 
ATOM   5391 C  CB  . THR B 1 309 ? 50.092 127.582 -107.517 1.00 65.48  ? 311 THR B CB  1 
ATOM   5392 O  OG1 . THR B 1 309 ? 49.265 126.839 -106.604 1.00 67.21  ? 311 THR B OG1 1 
ATOM   5393 C  CG2 . THR B 1 309 ? 51.520 127.094 -107.406 1.00 65.51  ? 311 THR B CG2 1 
ATOM   5394 N  N   . SER B 1 310 ? 49.024 129.186 -105.010 1.00 54.56  ? 312 SER B N   1 
ATOM   5395 C  CA  . SER B 1 310 ? 48.896 129.514 -103.567 1.00 52.50  ? 312 SER B CA  1 
ATOM   5396 C  C   . SER B 1 310 ? 48.107 128.410 -102.843 1.00 45.38  ? 312 SER B C   1 
ATOM   5397 O  O   . SER B 1 310 ? 47.315 128.745 -101.933 1.00 43.66  ? 312 SER B O   1 
ATOM   5398 C  CB  . SER B 1 310 ? 48.295 130.901 -103.381 1.00 53.99  ? 312 SER B CB  1 
ATOM   5399 O  OG  . SER B 1 310 ? 46.934 130.939 -103.760 1.00 54.05  ? 312 SER B OG  1 
ATOM   5400 N  N   . THR B 1 311 ? 48.314 127.139 -103.226 1.00 38.64  ? 313 THR B N   1 
ATOM   5401 C  CA  . THR B 1 311 ? 47.886 125.995 -102.377 1.00 33.56  ? 313 THR B CA  1 
ATOM   5402 C  C   . THR B 1 311 ? 48.886 125.850 -101.226 1.00 29.66  ? 313 THR B C   1 
ATOM   5403 O  O   . THR B 1 311 ? 50.089 126.208 -101.356 1.00 28.72  ? 313 THR B O   1 
ATOM   5404 C  CB  . THR B 1 311 ? 47.711 124.648 -103.100 1.00 33.05  ? 313 THR B CB  1 
ATOM   5405 O  OG1 . THR B 1 311 ? 48.951 124.254 -103.664 1.00 31.55  ? 313 THR B OG1 1 
ATOM   5406 C  CG2 . THR B 1 311 ? 46.632 124.653 -104.154 1.00 33.59  ? 313 THR B CG2 1 
ATOM   5407 N  N   . THR B 1 312 ? 48.388 125.375 -100.089 1.00 26.20  ? 314 THR B N   1 
ATOM   5408 C  CA  . THR B 1 312 ? 49.235 125.095 -98.916  1.00 23.40  ? 314 THR B CA  1 
ATOM   5409 C  C   . THR B 1 312 ? 48.884 123.722 -98.361  1.00 22.18  ? 314 THR B C   1 
ATOM   5410 O  O   . THR B 1 312 ? 47.789 123.233 -98.621  1.00 22.55  ? 314 THR B O   1 
ATOM   5411 C  CB  . THR B 1 312 ? 49.137 126.248 -97.921  1.00 21.85  ? 314 THR B CB  1 
ATOM   5412 O  OG1 . THR B 1 312 ? 47.753 126.350 -97.666  1.00 22.07  ? 314 THR B OG1 1 
ATOM   5413 C  CG2 . THR B 1 312 ? 49.627 127.574 -98.452  1.00 21.46  ? 314 THR B CG2 1 
ATOM   5414 N  N   . ALA B 1 313 ? 49.833 123.125 -97.672  1.00 20.29  ? 315 ALA B N   1 
ATOM   5415 C  CA  . ALA B 1 313 ? 49.592 121.972 -96.803  1.00 20.93  ? 315 ALA B CA  1 
ATOM   5416 C  C   . ALA B 1 313 ? 50.074 122.316 -95.372  1.00 21.07  ? 315 ALA B C   1 
ATOM   5417 O  O   . ALA B 1 313 ? 50.802 123.324 -95.141  1.00 19.42  ? 315 ALA B O   1 
ATOM   5418 C  CB  . ALA B 1 313 ? 50.252 120.744 -97.371  1.00 20.70  ? 315 ALA B CB  1 
ATOM   5419 N  N   . GLU B 1 314 ? 49.686 121.495 -94.415  1.00 22.22  ? 316 GLU B N   1 
ATOM   5420 C  CA  . GLU B 1 314 ? 50.234 121.589 -93.048  1.00 22.58  ? 316 GLU B CA  1 
ATOM   5421 C  C   . GLU B 1 314 ? 51.194 120.422 -92.850  1.00 20.53  ? 316 GLU B C   1 
ATOM   5422 O  O   . GLU B 1 314 ? 50.899 119.327 -93.370  1.00 19.83  ? 316 GLU B O   1 
ATOM   5423 C  CB  . GLU B 1 314 ? 49.092 121.574 -92.047  1.00 26.13  ? 316 GLU B CB  1 
ATOM   5424 C  CG  . GLU B 1 314 ? 48.085 122.674 -92.282  1.00 29.57  ? 316 GLU B CG  1 
ATOM   5425 C  CD  . GLU B 1 314 ? 46.981 122.629 -91.238  1.00 34.55  ? 316 GLU B CD  1 
ATOM   5426 O  OE1 . GLU B 1 314 ? 46.852 121.599 -90.530  1.00 38.04  ? 316 GLU B OE1 1 
ATOM   5427 O  OE2 . GLU B 1 314 ? 46.224 123.618 -91.142  1.00 41.66  ? 316 GLU B OE2 1 
ATOM   5428 N  N   . THR B 1 315 ? 52.271 120.626 -92.088  1.00 18.32  ? 317 THR B N   1 
ATOM   5429 C  CA  . THR B 1 315 ? 53.087 119.495 -91.572  1.00 18.06  ? 317 THR B CA  1 
ATOM   5430 C  C   . THR B 1 315 ? 52.255 118.680 -90.599  1.00 18.83  ? 317 THR B C   1 
ATOM   5431 O  O   . THR B 1 315 ? 51.317 119.191 -90.030  1.00 19.10  ? 317 THR B O   1 
ATOM   5432 C  CB  . THR B 1 315 ? 54.341 119.951 -90.854  1.00 16.69  ? 317 THR B CB  1 
ATOM   5433 O  OG1 . THR B 1 315 ? 53.868 120.716 -89.749  1.00 15.15  ? 317 THR B OG1 1 
ATOM   5434 C  CG2 . THR B 1 315 ? 55.248 120.743 -91.767  1.00 16.28  ? 317 THR B CG2 1 
ATOM   5435 N  N   . PRO B 1 316 ? 52.547 117.380 -90.422  1.00 20.40  ? 318 PRO B N   1 
ATOM   5436 C  CA  . PRO B 1 316 ? 52.004 116.609 -89.309  1.00 20.91  ? 318 PRO B CA  1 
ATOM   5437 C  C   . PRO B 1 316 ? 52.371 117.352 -88.021  1.00 20.04  ? 318 PRO B C   1 
ATOM   5438 O  O   . PRO B 1 316 ? 53.212 118.149 -88.036  1.00 19.28  ? 318 PRO B O   1 
ATOM   5439 C  CB  . PRO B 1 316 ? 52.710 115.253 -89.339  1.00 21.66  ? 318 PRO B CB  1 
ATOM   5440 C  CG  . PRO B 1 316 ? 53.357 115.189 -90.702  1.00 22.72  ? 318 PRO B CG  1 
ATOM   5441 C  CD  . PRO B 1 316 ? 53.522 116.616 -91.215  1.00 21.40  ? 318 PRO B CD  1 
ATOM   5442 N  N   . ASP B 1 317 ? 51.689 117.074 -86.932  1.00 21.79  ? 319 ASP B N   1 
ATOM   5443 C  CA  . ASP B 1 317 ? 51.857 117.813 -85.667  1.00 21.44  ? 319 ASP B CA  1 
ATOM   5444 C  C   . ASP B 1 317 ? 53.236 117.476 -85.126  1.00 20.86  ? 319 ASP B C   1 
ATOM   5445 O  O   . ASP B 1 317 ? 53.665 116.374 -85.295  1.00 20.96  ? 319 ASP B O   1 
ATOM   5446 C  CB  . ASP B 1 317 ? 50.781 117.443 -84.664  1.00 23.34  ? 319 ASP B CB  1 
ATOM   5447 C  CG  . ASP B 1 317 ? 49.419 118.026 -84.963  1.00 25.65  ? 319 ASP B CG  1 
ATOM   5448 O  OD1 . ASP B 1 317 ? 49.356 119.124 -85.583  1.00 27.51  ? 319 ASP B OD1 1 
ATOM   5449 O  OD2 . ASP B 1 317 ? 48.417 117.364 -84.578  1.00 28.82  ? 319 ASP B OD2 1 
ATOM   5450 N  N   . THR B 1 318 ? 53.898 118.430 -84.510  1.00 19.72  ? 320 THR B N   1 
ATOM   5451 C  CA  . THR B 1 318 ? 55.086 118.167 -83.687  1.00 20.06  ? 320 THR B CA  1 
ATOM   5452 C  C   . THR B 1 318 ? 54.785 118.643 -82.260  1.00 19.74  ? 320 THR B C   1 
ATOM   5453 O  O   . THR B 1 318 ? 54.181 119.703 -82.080  1.00 19.04  ? 320 THR B O   1 
ATOM   5454 C  CB  . THR B 1 318 ? 56.321 118.789 -84.342  1.00 19.90  ? 320 THR B CB  1 
ATOM   5455 O  OG1 . THR B 1 318 ? 57.467 118.433 -83.569  1.00 20.08  ? 320 THR B OG1 1 
ATOM   5456 C  CG2 . THR B 1 318 ? 56.216 120.292 -84.454  1.00 19.52  ? 320 THR B CG2 1 
ATOM   5457 N  N   . LYS B 1 319 ? 55.188 117.855 -81.281  1.00 20.62  ? 321 LYS B N   1 
ATOM   5458 C  CA  . LYS B 1 319 ? 54.668 117.911 -79.889  1.00 21.11  ? 321 LYS B CA  1 
ATOM   5459 C  C   . LYS B 1 319 ? 55.828 117.864 -78.921  1.00 21.18  ? 321 LYS B C   1 
ATOM   5460 O  O   . LYS B 1 319 ? 56.646 116.942 -79.066  1.00 21.33  ? 321 LYS B O   1 
ATOM   5461 C  CB  . LYS B 1 319 ? 53.811 116.677 -79.650  1.00 22.49  ? 321 LYS B CB  1 
ATOM   5462 C  CG  . LYS B 1 319 ? 53.062 116.665 -78.357  1.00 24.02  ? 321 LYS B CG  1 
ATOM   5463 C  CD  . LYS B 1 319 ? 52.331 115.331 -78.081  1.00 26.59  ? 321 LYS B CD  1 
ATOM   5464 C  CE  . LYS B 1 319 ? 51.933 115.245 -76.599  1.00 27.21  ? 321 LYS B CE  1 
ATOM   5465 N  NZ  . LYS B 1 319 ? 51.114 114.067 -76.194  1.00 28.14  ? 321 LYS B NZ  1 
ATOM   5466 N  N   . ALA B 1 320 ? 55.881 118.802 -77.971  1.00 20.58  ? 322 ALA B N   1 
ATOM   5467 C  CA  . ALA B 1 320 ? 56.771 118.721 -76.791  1.00 20.41  ? 322 ALA B CA  1 
ATOM   5468 C  C   . ALA B 1 320 ? 55.901 118.641 -75.550  1.00 19.09  ? 322 ALA B C   1 
ATOM   5469 O  O   . ALA B 1 320 ? 54.690 118.944 -75.613  1.00 17.10  ? 322 ALA B O   1 
ATOM   5470 C  CB  . ALA B 1 320 ? 57.716 119.889 -76.702  1.00 20.83  ? 322 ALA B CB  1 
ATOM   5471 N  N   . ASN B 1 321 ? 56.505 118.173 -74.470  1.00 19.99  ? 323 ASN B N   1 
ATOM   5472 C  CA  . ASN B 1 321 ? 55.745 117.809 -73.250  1.00 19.39  ? 323 ASN B CA  1 
ATOM   5473 C  C   . ASN B 1 321 ? 56.559 118.146 -72.009  1.00 19.75  ? 323 ASN B C   1 
ATOM   5474 O  O   . ASN B 1 321 ? 57.745 117.893 -71.995  1.00 21.64  ? 323 ASN B O   1 
ATOM   5475 C  CB  . ASN B 1 321 ? 55.219 116.370 -73.302  1.00 19.64  ? 323 ASN B CB  1 
ATOM   5476 C  CG  . ASN B 1 321 ? 53.888 116.260 -72.576  1.00 20.07  ? 323 ASN B CG  1 
ATOM   5477 O  OD1 . ASN B 1 321 ? 53.498 117.170 -71.837  1.00 19.47  ? 323 ASN B OD1 1 
ATOM   5478 N  ND2 . ASN B 1 321 ? 53.179 115.157 -72.755  1.00 20.40  ? 323 ASN B ND2 1 
ATOM   5479 N  N   . VAL B 1 322 ? 55.900 118.688 -71.002  1.00 18.39  ? 324 VAL B N   1 
ATOM   5480 C  CA  . VAL B 1 322 ? 56.512 119.018 -69.696  1.00 18.83  ? 324 VAL B CA  1 
ATOM   5481 C  C   . VAL B 1 322 ? 55.623 118.425 -68.631  1.00 18.40  ? 324 VAL B C   1 
ATOM   5482 O  O   . VAL B 1 322 ? 54.440 118.809 -68.575  1.00 17.87  ? 324 VAL B O   1 
ATOM   5483 C  CB  . VAL B 1 322 ? 56.614 120.529 -69.504  1.00 18.88  ? 324 VAL B CB  1 
ATOM   5484 C  CG1 . VAL B 1 322 ? 57.194 120.858 -68.148  1.00 19.36  ? 324 VAL B CG1 1 
ATOM   5485 C  CG2 . VAL B 1 322 ? 57.401 121.159 -70.636  1.00 19.11  ? 324 VAL B CG2 1 
ATOM   5486 N  N   . TYR B 1 323 ? 56.148 117.471 -67.880  1.00 19.07  ? 325 TYR B N   1 
ATOM   5487 C  CA  . TYR B 1 323 ? 55.412 116.814 -66.764  1.00 18.80  ? 325 TYR B CA  1 
ATOM   5488 C  C   . TYR B 1 323 ? 55.739 117.565 -65.470  1.00 18.58  ? 325 TYR B C   1 
ATOM   5489 O  O   . TYR B 1 323 ? 56.726 118.296 -65.430  1.00 18.05  ? 325 TYR B O   1 
ATOM   5490 C  CB  . TYR B 1 323 ? 55.726 115.321 -66.678  1.00 19.62  ? 325 TYR B CB  1 
ATOM   5491 C  CG  . TYR B 1 323 ? 55.387 114.586 -67.939  1.00 20.57  ? 325 TYR B CG  1 
ATOM   5492 C  CD1 . TYR B 1 323 ? 56.280 114.527 -68.991  1.00 21.16  ? 325 TYR B CD1 1 
ATOM   5493 C  CD2 . TYR B 1 323 ? 54.155 113.980 -68.094  1.00 21.35  ? 325 TYR B CD2 1 
ATOM   5494 C  CE1 . TYR B 1 323 ? 55.964 113.864 -70.168  1.00 22.23  ? 325 TYR B CE1 1 
ATOM   5495 C  CE2 . TYR B 1 323 ? 53.814 113.310 -69.258  1.00 22.33  ? 325 TYR B CE2 1 
ATOM   5496 C  CZ  . TYR B 1 323 ? 54.718 113.268 -70.308  1.00 22.75  ? 325 TYR B CZ  1 
ATOM   5497 O  OH  . TYR B 1 323 ? 54.376 112.608 -71.454  1.00 23.82  ? 325 TYR B OH  1 
ATOM   5498 N  N   . THR B 1 324 ? 54.884 117.415 -64.461  1.00 18.79  ? 326 THR B N   1 
ATOM   5499 C  CA  . THR B 1 324 ? 55.167 117.867 -63.075  1.00 18.74  ? 326 THR B CA  1 
ATOM   5500 C  C   . THR B 1 324 ? 54.347 116.978 -62.161  1.00 18.66  ? 326 THR B C   1 
ATOM   5501 O  O   . THR B 1 324 ? 53.391 116.375 -62.657  1.00 17.81  ? 326 THR B O   1 
ATOM   5502 C  CB  . THR B 1 324 ? 54.904 119.366 -62.936  1.00 18.36  ? 326 THR B CB  1 
ATOM   5503 O  OG1 . THR B 1 324 ? 55.517 119.858 -61.763  1.00 18.03  ? 326 THR B OG1 1 
ATOM   5504 C  CG2 . THR B 1 324 ? 53.440 119.715 -62.861  1.00 18.43  ? 326 THR B CG2 1 
ATOM   5505 N  N   . TYR B 1 325 ? 54.785 116.856 -60.909  1.00 19.57  ? 327 TYR B N   1 
ATOM   5506 C  CA  . TYR B 1 325 ? 54.232 115.886 -59.931  1.00 20.37  ? 327 TYR B CA  1 
ATOM   5507 C  C   . TYR B 1 325 ? 53.747 116.656 -58.701  1.00 19.96  ? 327 TYR B C   1 
ATOM   5508 O  O   . TYR B 1 325 ? 54.097 117.824 -58.471  1.00 19.48  ? 327 TYR B O   1 
ATOM   5509 C  CB  . TYR B 1 325 ? 55.269 114.801 -59.623  1.00 21.22  ? 327 TYR B CB  1 
ATOM   5510 C  CG  . TYR B 1 325 ? 56.090 114.384 -60.817  1.00 21.77  ? 327 TYR B CG  1 
ATOM   5511 C  CD1 . TYR B 1 325 ? 55.503 113.778 -61.907  1.00 22.51  ? 327 TYR B CD1 1 
ATOM   5512 C  CD2 . TYR B 1 325 ? 57.447 114.633 -60.892  1.00 22.34  ? 327 TYR B CD2 1 
ATOM   5513 C  CE1 . TYR B 1 325 ? 56.233 113.426 -63.026  1.00 22.86  ? 327 TYR B CE1 1 
ATOM   5514 C  CE2 . TYR B 1 325 ? 58.195 114.270 -61.999  1.00 23.13  ? 327 TYR B CE2 1 
ATOM   5515 C  CZ  . TYR B 1 325 ? 57.591 113.672 -63.087  1.00 23.05  ? 327 TYR B CZ  1 
ATOM   5516 O  OH  . TYR B 1 325 ? 58.302 113.336 -64.223  1.00 24.01  ? 327 TYR B OH  1 
ATOM   5517 N  N   . GLN B 1 326 ? 52.938 115.976 -57.913  1.00 20.43  ? 328 GLN B N   1 
ATOM   5518 C  CA  . GLN B 1 326 ? 52.414 116.484 -56.617  1.00 20.21  ? 328 GLN B CA  1 
ATOM   5519 C  C   . GLN B 1 326 ? 52.823 115.553 -55.472  1.00 19.56  ? 328 GLN B C   1 
ATOM   5520 O  O   . GLN B 1 326 ? 52.651 114.329 -55.597  1.00 19.52  ? 328 GLN B O   1 
ATOM   5521 C  CB  . GLN B 1 326 ? 50.903 116.559 -56.756  1.00 21.01  ? 328 GLN B CB  1 
ATOM   5522 C  CG  . GLN B 1 326 ? 50.191 117.053 -55.515  1.00 22.05  ? 328 GLN B CG  1 
ATOM   5523 C  CD  . GLN B 1 326 ? 48.722 117.115 -55.827  1.00 22.56  ? 328 GLN B CD  1 
ATOM   5524 O  OE1 . GLN B 1 326 ? 48.330 116.917 -56.951  1.00 23.95  ? 328 GLN B OE1 1 
ATOM   5525 N  NE2 . GLN B 1 326 ? 47.909 117.376 -54.827  1.00 24.35  ? 328 GLN B NE2 1 
ATOM   5526 N  N   . LEU B 1 327 ? 53.341 116.110 -54.390  1.00 19.04  ? 329 LEU B N   1 
ATOM   5527 C  CA  . LEU B 1 327 ? 53.539 115.351 -53.122  1.00 19.12  ? 329 LEU B CA  1 
ATOM   5528 C  C   . LEU B 1 327 ? 52.343 115.629 -52.214  1.00 19.13  ? 329 LEU B C   1 
ATOM   5529 O  O   . LEU B 1 327 ? 52.073 116.797 -51.887  1.00 18.93  ? 329 LEU B O   1 
ATOM   5530 C  CB  . LEU B 1 327 ? 54.853 115.752 -52.462  1.00 18.96  ? 329 LEU B CB  1 
ATOM   5531 C  CG  . LEU B 1 327 ? 55.066 115.244 -51.036  1.00 19.63  ? 329 LEU B CG  1 
ATOM   5532 C  CD1 . LEU B 1 327 ? 55.357 113.751 -51.030  1.00 20.15  ? 329 LEU B CD1 1 
ATOM   5533 C  CD2 . LEU B 1 327 ? 56.171 116.041 -50.357  1.00 19.31  ? 329 LEU B CD2 1 
ATOM   5534 N  N   . LYS B 1 328 ? 51.643 114.573 -51.833  1.00 19.62  ? 330 LYS B N   1 
ATOM   5535 C  CA  . LYS B 1 328 ? 50.580 114.648 -50.813  1.00 20.11  ? 330 LYS B CA  1 
ATOM   5536 C  C   . LYS B 1 328 ? 51.120 114.087 -49.502  1.00 20.61  ? 330 LYS B C   1 
ATOM   5537 O  O   . LYS B 1 328 ? 51.359 112.880 -49.463  1.00 21.91  ? 330 LYS B O   1 
ATOM   5538 C  CB  . LYS B 1 328 ? 49.374 113.830 -51.256  1.00 20.40  ? 330 LYS B CB  1 
ATOM   5539 C  CG  . LYS B 1 328 ? 48.190 113.961 -50.329  1.00 20.25  ? 330 LYS B CG  1 
ATOM   5540 C  CD  . LYS B 1 328 ? 47.059 113.099 -50.767  1.00 20.95  ? 330 LYS B CD  1 
ATOM   5541 C  CE  . LYS B 1 328 ? 46.408 113.514 -52.065  1.00 20.46  ? 330 LYS B CE  1 
ATOM   5542 N  NZ  . LYS B 1 328 ? 45.758 114.830 -51.953  1.00 19.92  ? 330 LYS B NZ  1 
ATOM   5543 N  N   . VAL B 1 329 ? 51.292 114.926 -48.480  1.00 20.13  ? 331 VAL B N   1 
ATOM   5544 C  CA  . VAL B 1 329 ? 51.665 114.490 -47.114  1.00 20.18  ? 331 VAL B CA  1 
ATOM   5545 C  C   . VAL B 1 329 ? 50.401 114.456 -46.260  1.00 20.36  ? 331 VAL B C   1 
ATOM   5546 O  O   . VAL B 1 329 ? 49.751 115.491 -46.145  1.00 19.28  ? 331 VAL B O   1 
ATOM   5547 C  CB  . VAL B 1 329 ? 52.733 115.419 -46.512  1.00 20.28  ? 331 VAL B CB  1 
ATOM   5548 C  CG1 . VAL B 1 329 ? 53.069 115.041 -45.077  1.00 20.51  ? 331 VAL B CG1 1 
ATOM   5549 C  CG2 . VAL B 1 329 ? 53.991 115.446 -47.361  1.00 20.35  ? 331 VAL B CG2 1 
ATOM   5550 N  N   . ASN B 1 330 ? 50.110 113.304 -45.659  1.00 21.33  ? 332 ASN B N   1 
ATOM   5551 C  CA  . ASN B 1 330 ? 49.008 113.094 -44.697  1.00 21.73  ? 332 ASN B CA  1 
ATOM   5552 C  C   . ASN B 1 330 ? 49.571 113.024 -43.274  1.00 22.52  ? 332 ASN B C   1 
ATOM   5553 O  O   . ASN B 1 330 ? 50.435 112.161 -42.987  1.00 22.70  ? 332 ASN B O   1 
ATOM   5554 C  CB  . ASN B 1 330 ? 48.272 111.793 -44.947  1.00 22.85  ? 332 ASN B CB  1 
ATOM   5555 C  CG  . ASN B 1 330 ? 47.550 111.746 -46.263  1.00 23.17  ? 332 ASN B CG  1 
ATOM   5556 O  OD1 . ASN B 1 330 ? 47.681 110.763 -46.974  1.00 24.70  ? 332 ASN B OD1 1 
ATOM   5557 N  ND2 . ASN B 1 330 ? 46.810 112.786 -46.588  1.00 23.11  ? 332 ASN B ND2 1 
ATOM   5558 N  N   . LYS B 1 331 ? 49.118 113.905 -42.393  1.00 22.82  ? 333 LYS B N   1 
ATOM   5559 C  CA  . LYS B 1 331 ? 49.540 113.934 -40.964  1.00 22.56  ? 333 LYS B CA  1 
ATOM   5560 C  C   . LYS B 1 331 ? 48.540 113.168 -40.123  1.00 23.09  ? 333 LYS B C   1 
ATOM   5561 O  O   . LYS B 1 331 ? 47.403 113.609 -40.039  1.00 22.78  ? 333 LYS B O   1 
ATOM   5562 C  CB  . LYS B 1 331 ? 49.603 115.350 -40.414  1.00 22.49  ? 333 LYS B CB  1 
ATOM   5563 C  CG  . LYS B 1 331 ? 50.315 115.403 -39.069  1.00 23.46  ? 333 LYS B CG  1 
ATOM   5564 C  CD  . LYS B 1 331 ? 51.474 114.430 -38.974  1.00 23.99  ? 333 LYS B CD  1 
ATOM   5565 C  CE  . LYS B 1 331 ? 52.289 114.657 -37.722  1.00 25.75  ? 333 LYS B CE  1 
ATOM   5566 N  NZ  . LYS B 1 331 ? 52.955 113.416 -37.256  1.00 26.34  ? 333 LYS B NZ  1 
ATOM   5567 N  N   . VAL B 1 332 ? 48.949 112.059 -39.584  1.00 24.86  ? 334 VAL B N   1 
ATOM   5568 C  CA  . VAL B 1 332 ? 48.019 111.246 -38.743  1.00 27.12  ? 334 VAL B CA  1 
ATOM   5569 C  C   . VAL B 1 332 ? 48.713 110.867 -37.435  1.00 29.06  ? 334 VAL B C   1 
ATOM   5570 O  O   . VAL B 1 332 ? 49.914 111.169 -37.278  1.00 28.20  ? 334 VAL B O   1 
ATOM   5571 C  CB  . VAL B 1 332 ? 47.549 110.004 -39.516  1.00 28.22  ? 334 VAL B CB  1 
ATOM   5572 C  CG1 . VAL B 1 332 ? 46.800 110.411 -40.780  1.00 27.77  ? 334 VAL B CG1 1 
ATOM   5573 C  CG2 . VAL B 1 332 ? 48.730 109.089 -39.843  1.00 28.94  ? 334 VAL B CG2 1 
ATOM   5574 N  N   . LYS B 1 333 ? 47.969 110.200 -36.558  1.00 32.09  ? 335 LYS B N   1 
ATOM   5575 C  CA  . LYS B 1 333 ? 48.486 109.565 -35.321  1.00 35.13  ? 335 LYS B CA  1 
ATOM   5576 C  C   . LYS B 1 333 ? 48.285 108.053 -35.453  1.00 39.09  ? 335 LYS B C   1 
ATOM   5577 O  O   . LYS B 1 333 ? 47.833 107.601 -36.544  1.00 40.40  ? 335 LYS B O   1 
ATOM   5578 C  CB  . LYS B 1 333 ? 47.829 110.228 -34.107  1.00 35.14  ? 335 LYS B CB  1 
ATOM   5579 C  CG  . LYS B 1 333 ? 46.312 110.321 -34.117  1.00 34.33  ? 335 LYS B CG  1 
ATOM   5580 C  CD  . LYS B 1 333 ? 45.782 111.356 -33.186  1.00 34.04  ? 335 LYS B CD  1 
ATOM   5581 C  CE  . LYS B 1 333 ? 44.380 111.710 -33.601  1.00 36.50  ? 335 LYS B CE  1 
ATOM   5582 N  NZ  . LYS B 1 333 ? 43.593 112.350 -32.527  1.00 38.83  ? 335 LYS B NZ  1 
ATOM   5583 N  N   . GLU B 1 334 ? 48.657 107.281 -34.431  1.00 41.89  ? 336 GLU B N   1 
ATOM   5584 C  CA  . GLU B 1 334 ? 48.891 105.817 -34.585  1.00 44.93  ? 336 GLU B CA  1 
ATOM   5585 C  C   . GLU B 1 334 ? 47.570 105.110 -34.845  1.00 42.99  ? 336 GLU B C   1 
ATOM   5586 O  O   . GLU B 1 334 ? 47.619 104.041 -35.417  1.00 44.44  ? 336 GLU B O   1 
ATOM   5587 C  CB  . GLU B 1 334 ? 49.655 105.248 -33.394  1.00 48.95  ? 336 GLU B CB  1 
ATOM   5588 C  CG  . GLU B 1 334 ? 51.046 105.847 -33.312  1.00 52.50  ? 336 GLU B CG  1 
ATOM   5589 C  CD  . GLU B 1 334 ? 51.980 105.323 -32.233  1.00 56.96  ? 336 GLU B CD  1 
ATOM   5590 O  OE1 . GLU B 1 334 ? 51.642 104.276 -31.608  1.00 62.68  ? 336 GLU B OE1 1 
ATOM   5591 O  OE2 . GLU B 1 334 ? 53.061 105.962 -32.030  1.00 58.43  ? 336 GLU B OE2 1 
ATOM   5592 N  N   . ASN B 1 335 ? 46.437 105.732 -34.553  1.00 41.63  ? 337 ASN B N   1 
ATOM   5593 C  CA  . ASN B 1 335 ? 45.123 105.142 -34.924  1.00 43.68  ? 337 ASN B CA  1 
ATOM   5594 C  C   . ASN B 1 335 ? 44.755 105.553 -36.356  1.00 46.08  ? 337 ASN B C   1 
ATOM   5595 O  O   . ASN B 1 335 ? 43.582 105.338 -36.758  1.00 49.11  ? 337 ASN B O   1 
ATOM   5596 C  CB  . ASN B 1 335 ? 44.032 105.516 -33.917  1.00 43.19  ? 337 ASN B CB  1 
ATOM   5597 C  CG  . ASN B 1 335 ? 43.818 107.010 -33.826  1.00 41.50  ? 337 ASN B CG  1 
ATOM   5598 O  OD1 . ASN B 1 335 ? 44.068 107.714 -34.779  1.00 41.09  ? 337 ASN B OD1 1 
ATOM   5599 N  ND2 . ASN B 1 335 ? 43.376 107.527 -32.695  1.00 40.55  ? 337 ASN B ND2 1 
ATOM   5600 N  N   . GLN B 1 336 ? 45.676 106.182 -37.094  1.00 44.14  ? 338 GLN B N   1 
ATOM   5601 C  CA  . GLN B 1 336 ? 45.484 106.512 -38.525  1.00 43.91  ? 338 GLN B CA  1 
ATOM   5602 C  C   . GLN B 1 336 ? 44.440 107.612 -38.719  1.00 41.10  ? 338 GLN B C   1 
ATOM   5603 O  O   . GLN B 1 336 ? 44.182 107.958 -39.838  1.00 40.09  ? 338 GLN B O   1 
ATOM   5604 C  CB  . GLN B 1 336 ? 45.051 105.265 -39.311  1.00 46.78  ? 338 GLN B CB  1 
ATOM   5605 C  CG  . GLN B 1 336 ? 46.052 104.127 -39.209  1.00 48.58  ? 338 GLN B CG  1 
ATOM   5606 C  CD  . GLN B 1 336 ? 47.415 104.594 -39.659  1.00 48.89  ? 338 GLN B CD  1 
ATOM   5607 O  OE1 . GLN B 1 336 ? 47.618 104.949 -40.813  1.00 50.92  ? 338 GLN B OE1 1 
ATOM   5608 N  NE2 . GLN B 1 336 ? 48.370 104.618 -38.749  1.00 48.62  ? 338 GLN B NE2 1 
ATOM   5609 N  N   . GLN B 1 337 ? 43.838 108.169 -37.683  1.00 39.88  ? 339 GLN B N   1 
ATOM   5610 C  CA  . GLN B 1 337 ? 42.945 109.325 -37.926  1.00 37.94  ? 339 GLN B CA  1 
ATOM   5611 C  C   . GLN B 1 337 ? 43.828 110.576 -37.933  1.00 33.86  ? 339 GLN B C   1 
ATOM   5612 O  O   . GLN B 1 337 ? 44.981 110.537 -37.433  1.00 33.05  ? 339 GLN B O   1 
ATOM   5613 C  CB  . GLN B 1 337 ? 41.765 109.316 -36.953  1.00 40.75  ? 339 GLN B CB  1 
ATOM   5614 C  CG  . GLN B 1 337 ? 42.056 110.016 -35.632  1.00 41.45  ? 339 GLN B CG  1 
ATOM   5615 C  CD  . GLN B 1 337 ? 40.951 109.850 -34.618  1.00 45.20  ? 339 GLN B CD  1 
ATOM   5616 O  OE1 . GLN B 1 337 ? 41.067 110.305 -33.462  1.00 45.88  ? 339 GLN B OE1 1 
ATOM   5617 N  NE2 . GLN B 1 337 ? 39.872 109.208 -35.062  1.00 45.62  ? 339 GLN B NE2 1 
ATOM   5618 N  N   . ALA B 1 338 ? 43.309 111.627 -38.539  1.00 31.77  ? 340 ALA B N   1 
ATOM   5619 C  CA  . ALA B 1 338 ? 44.027 112.872 -38.874  1.00 29.78  ? 340 ALA B CA  1 
ATOM   5620 C  C   . ALA B 1 338 ? 44.639 113.452 -37.611  1.00 27.47  ? 340 ALA B C   1 
ATOM   5621 O  O   . ALA B 1 338 ? 44.045 113.297 -36.564  1.00 29.70  ? 340 ALA B O   1 
ATOM   5622 C  CB  . ALA B 1 338 ? 43.070 113.857 -39.495  1.00 30.27  ? 340 ALA B CB  1 
ATOM   5623 N  N   . LEU B 1 339 ? 45.772 114.126 -37.716  1.00 24.40  ? 341 LEU B N   1 
ATOM   5624 C  CA  . LEU B 1 339 ? 46.282 114.956 -36.611  1.00 22.79  ? 341 LEU B CA  1 
ATOM   5625 C  C   . LEU B 1 339 ? 46.437 116.383 -37.117  1.00 21.38  ? 341 LEU B C   1 
ATOM   5626 O  O   . LEU B 1 339 ? 47.206 116.606 -38.029  1.00 21.83  ? 341 LEU B O   1 
ATOM   5627 C  CB  . LEU B 1 339 ? 47.608 114.388 -36.122  1.00 22.43  ? 341 LEU B CB  1 
ATOM   5628 C  CG  . LEU B 1 339 ? 48.244 115.174 -34.973  1.00 22.54  ? 341 LEU B CG  1 
ATOM   5629 C  CD1 . LEU B 1 339 ? 47.312 115.326 -33.775  1.00 22.51  ? 341 LEU B CD1 1 
ATOM   5630 C  CD2 . LEU B 1 339 ? 49.545 114.503 -34.552  1.00 22.92  ? 341 LEU B CD2 1 
ATOM   5631 N  N   . ALA B 1 340 ? 45.737 117.324 -36.533  1.00 20.68  ? 342 ALA B N   1 
ATOM   5632 C  CA  . ALA B 1 340 ? 45.836 118.746 -36.894  1.00 20.50  ? 342 ALA B CA  1 
ATOM   5633 C  C   . ALA B 1 340 ? 47.052 119.333 -36.228  1.00 19.94  ? 342 ALA B C   1 
ATOM   5634 O  O   . ALA B 1 340 ? 47.586 118.703 -35.365  1.00 19.16  ? 342 ALA B O   1 
ATOM   5635 C  CB  . ALA B 1 340 ? 44.591 119.481 -36.471  1.00 21.43  ? 342 ALA B CB  1 
ATOM   5636 N  N   . GLY B 1 341 ? 47.486 120.491 -36.673  1.00 20.42  ? 343 GLY B N   1 
ATOM   5637 C  CA  . GLY B 1 341 ? 48.495 121.268 -35.935  1.00 21.11  ? 343 GLY B CA  1 
ATOM   5638 C  C   . GLY B 1 341 ? 49.916 121.047 -36.435  1.00 21.42  ? 343 GLY B C   1 
ATOM   5639 O  O   . GLY B 1 341 ? 50.817 121.677 -35.905  1.00 22.26  ? 343 GLY B O   1 
ATOM   5640 N  N   . ALA B 1 342 ? 50.126 120.228 -37.459  1.00 21.42  ? 344 ALA B N   1 
ATOM   5641 C  CA  . ALA B 1 342 ? 51.453 120.066 -38.079  1.00 21.30  ? 344 ALA B CA  1 
ATOM   5642 C  C   . ALA B 1 342 ? 51.635 121.123 -39.174  1.00 21.97  ? 344 ALA B C   1 
ATOM   5643 O  O   . ALA B 1 342 ? 50.643 121.582 -39.827  1.00 21.12  ? 344 ALA B O   1 
ATOM   5644 C  CB  . ALA B 1 342 ? 51.610 118.665 -38.600  1.00 21.30  ? 344 ALA B CB  1 
ATOM   5645 N  N   . GLY B 1 343 ? 52.887 121.527 -39.348  1.00 22.95  ? 345 GLY B N   1 
ATOM   5646 C  CA  . GLY B 1 343 ? 53.344 122.350 -40.481  1.00 23.18  ? 345 GLY B CA  1 
ATOM   5647 C  C   . GLY B 1 343 ? 54.512 121.672 -41.148  1.00 23.26  ? 345 GLY B C   1 
ATOM   5648 O  O   . GLY B 1 343 ? 55.241 120.981 -40.442  1.00 23.27  ? 345 GLY B O   1 
ATOM   5649 N  N   . PHE B 1 344 ? 54.652 121.804 -42.470  1.00 23.34  ? 346 PHE B N   1 
ATOM   5650 C  CA  . PHE B 1 344 ? 55.767 121.181 -43.208  1.00 23.66  ? 346 PHE B CA  1 
ATOM   5651 C  C   . PHE B 1 344 ? 56.427 122.209 -44.117  1.00 25.19  ? 346 PHE B C   1 
ATOM   5652 O  O   . PHE B 1 344 ? 55.741 123.056 -44.733  1.00 26.87  ? 346 PHE B O   1 
ATOM   5653 C  CB  . PHE B 1 344 ? 55.271 120.004 -44.033  1.00 23.43  ? 346 PHE B CB  1 
ATOM   5654 C  CG  . PHE B 1 344 ? 54.927 118.812 -43.198  1.00 23.46  ? 346 PHE B CG  1 
ATOM   5655 C  CD1 . PHE B 1 344 ? 53.722 118.733 -42.536  1.00 23.83  ? 346 PHE B CD1 1 
ATOM   5656 C  CD2 . PHE B 1 344 ? 55.834 117.784 -43.052  1.00 24.18  ? 346 PHE B CD2 1 
ATOM   5657 C  CE1 . PHE B 1 344 ? 53.441 117.638 -41.728  1.00 24.83  ? 346 PHE B CE1 1 
ATOM   5658 C  CE2 . PHE B 1 344 ? 55.533 116.677 -42.280  1.00 24.40  ? 346 PHE B CE2 1 
ATOM   5659 C  CZ  . PHE B 1 344 ? 54.345 116.609 -41.603  1.00 24.54  ? 346 PHE B CZ  1 
ATOM   5660 N  N   . THR B 1 345 ? 57.749 122.113 -44.206  1.00 25.49  ? 347 THR B N   1 
ATOM   5661 C  CA  . THR B 1 345 ? 58.560 122.827 -45.191  1.00 25.21  ? 347 THR B CA  1 
ATOM   5662 C  C   . THR B 1 345 ? 59.195 121.778 -46.095  1.00 24.39  ? 347 THR B C   1 
ATOM   5663 O  O   . THR B 1 345 ? 59.641 120.749 -45.612  1.00 24.20  ? 347 THR B O   1 
ATOM   5664 C  CB  . THR B 1 345 ? 59.529 123.776 -44.496  1.00 26.37  ? 347 THR B CB  1 
ATOM   5665 O  OG1 . THR B 1 345 ? 58.830 124.550 -43.518  1.00 26.61  ? 347 THR B OG1 1 
ATOM   5666 C  CG2 . THR B 1 345 ? 60.193 124.689 -45.505  1.00 27.73  ? 347 THR B CG2 1 
ATOM   5667 N  N   . LEU B 1 346 ? 59.174 122.033 -47.380  1.00 24.01  ? 348 LEU B N   1 
ATOM   5668 C  CA  . LEU B 1 346 ? 59.820 121.165 -48.398  1.00 24.84  ? 348 LEU B CA  1 
ATOM   5669 C  C   . LEU B 1 346 ? 60.987 121.929 -49.008  1.00 26.28  ? 348 LEU B C   1 
ATOM   5670 O  O   . LEU B 1 346 ? 60.800 123.119 -49.322  1.00 26.63  ? 348 LEU B O   1 
ATOM   5671 C  CB  . LEU B 1 346 ? 58.818 120.777 -49.478  1.00 23.65  ? 348 LEU B CB  1 
ATOM   5672 C  CG  . LEU B 1 346 ? 59.357 119.870 -50.583  1.00 23.49  ? 348 LEU B CG  1 
ATOM   5673 C  CD1 . LEU B 1 346 ? 59.602 118.458 -50.085  1.00 23.32  ? 348 LEU B CD1 1 
ATOM   5674 C  CD2 . LEU B 1 346 ? 58.402 119.834 -51.766  1.00 23.31  ? 348 LEU B CD2 1 
ATOM   5675 N  N   . TYR B 1 347 ? 62.143 121.269 -49.106  1.00 28.05  ? 349 TYR B N   1 
ATOM   5676 C  CA  . TYR B 1 347 ? 63.392 121.812 -49.688  1.00 29.92  ? 349 TYR B CA  1 
ATOM   5677 C  C   . TYR B 1 347 ? 63.749 120.953 -50.889  1.00 30.70  ? 349 TYR B C   1 
ATOM   5678 O  O   . TYR B 1 347 ? 63.582 119.736 -50.858  1.00 29.60  ? 349 TYR B O   1 
ATOM   5679 C  CB  . TYR B 1 347 ? 64.537 121.825 -48.674  1.00 31.13  ? 349 TYR B CB  1 
ATOM   5680 C  CG  . TYR B 1 347 ? 64.300 122.661 -47.441  1.00 30.98  ? 349 TYR B CG  1 
ATOM   5681 C  CD1 . TYR B 1 347 ? 63.673 122.132 -46.337  1.00 30.50  ? 349 TYR B CD1 1 
ATOM   5682 C  CD2 . TYR B 1 347 ? 64.671 123.992 -47.388  1.00 31.46  ? 349 TYR B CD2 1 
ATOM   5683 C  CE1 . TYR B 1 347 ? 63.408 122.905 -45.219  1.00 30.70  ? 349 TYR B CE1 1 
ATOM   5684 C  CE2 . TYR B 1 347 ? 64.434 124.772 -46.276  1.00 31.23  ? 349 TYR B CE2 1 
ATOM   5685 C  CZ  . TYR B 1 347 ? 63.804 124.225 -45.188  1.00 31.24  ? 349 TYR B CZ  1 
ATOM   5686 O  OH  . TYR B 1 347 ? 63.598 124.985 -44.081  1.00 31.87  ? 349 TYR B OH  1 
ATOM   5687 N  N   . LYS B 1 348 ? 64.232 121.598 -51.928  1.00 33.48  ? 350 LYS B N   1 
ATOM   5688 C  CA  . LYS B 1 348 ? 64.835 120.879 -53.075  1.00 37.77  ? 350 LYS B CA  1 
ATOM   5689 C  C   . LYS B 1 348 ? 66.345 121.120 -53.077  1.00 41.08  ? 350 LYS B C   1 
ATOM   5690 O  O   . LYS B 1 348 ? 66.762 122.264 -52.822  1.00 40.68  ? 350 LYS B O   1 
ATOM   5691 C  CB  . LYS B 1 348 ? 64.229 121.344 -54.406  1.00 37.11  ? 350 LYS B CB  1 
ATOM   5692 C  CG  . LYS B 1 348 ? 64.628 120.465 -55.586  1.00 38.24  ? 350 LYS B CG  1 
ATOM   5693 C  CD  . LYS B 1 348 ? 64.117 120.901 -56.947  1.00 37.48  ? 350 LYS B CD  1 
ATOM   5694 C  CE  . LYS B 1 348 ? 64.540 119.930 -58.032  1.00 37.95  ? 350 LYS B CE  1 
ATOM   5695 N  NZ  . LYS B 1 348 ? 64.193 120.443 -59.379  1.00 37.90  ? 350 LYS B NZ  1 
ATOM   5696 N  N   . LYS B 1 349 ? 67.124 120.088 -53.399  1.00 45.91  ? 351 LYS B N   1 
ATOM   5697 C  CA  . LYS B 1 349 ? 68.581 120.220 -53.659  1.00 50.19  ? 351 LYS B CA  1 
ATOM   5698 C  C   . LYS B 1 349 ? 68.778 120.925 -55.009  1.00 50.15  ? 351 LYS B C   1 
ATOM   5699 O  O   . LYS B 1 349 ? 68.509 120.308 -56.060  1.00 44.91  ? 351 LYS B O   1 
ATOM   5700 C  CB  . LYS B 1 349 ? 69.228 118.841 -53.592  1.00 54.10  ? 351 LYS B CB  1 
ATOM   5701 C  CG  . LYS B 1 349 ? 70.745 118.863 -53.582  1.00 60.62  ? 351 LYS B CG  1 
ATOM   5702 C  CD  . LYS B 1 349 ? 71.354 117.488 -53.829  1.00 63.71  ? 351 LYS B CD  1 
ATOM   5703 C  CE  . LYS B 1 349 ? 71.139 116.519 -52.674  1.00 64.71  ? 351 LYS B CE  1 
ATOM   5704 N  NZ  . LYS B 1 349 ? 71.982 116.845 -51.496  1.00 65.91  ? 351 LYS B NZ  1 
ATOM   5705 N  N   . VAL B 1 350 ? 69.140 122.205 -54.963  1.00 53.74  ? 352 VAL B N   1 
ATOM   5706 C  CA  . VAL B 1 350 ? 69.592 122.985 -56.147  1.00 58.09  ? 352 VAL B CA  1 
ATOM   5707 C  C   . VAL B 1 350 ? 71.106 123.177 -56.030  1.00 64.49  ? 352 VAL B C   1 
ATOM   5708 O  O   . VAL B 1 350 ? 71.534 123.998 -55.190  1.00 70.03  ? 352 VAL B O   1 
ATOM   5709 C  CB  . VAL B 1 350 ? 68.838 124.316 -56.275  1.00 57.17  ? 352 VAL B CB  1 
ATOM   5710 C  CG1 . VAL B 1 350 ? 69.415 125.177 -57.394  1.00 59.03  ? 352 VAL B CG1 1 
ATOM   5711 C  CG2 . VAL B 1 350 ? 67.368 124.053 -56.523  1.00 55.28  ? 352 VAL B CG2 1 
ATOM   5712 N  N   . ASN B 1 351 ? 71.873 122.417 -56.829  1.00 67.43  ? 353 ASN B N   1 
ATOM   5713 C  CA  A ASN B 1 351 ? 73.367 122.420 -56.850  0.50 68.83  ? 353 ASN B CA  1 
ATOM   5714 C  CA  B ASN B 1 351 ? 73.361 122.459 -56.849  0.50 67.30  ? 353 ASN B CA  1 
ATOM   5715 C  C   . ASN B 1 351 ? 73.876 122.192 -55.419  1.00 69.93  ? 353 ASN B C   1 
ATOM   5716 O  O   . ASN B 1 351 ? 74.554 123.079 -54.863  1.00 70.72  ? 353 ASN B O   1 
ATOM   5717 C  CB  A ASN B 1 351 ? 73.957 123.658 -57.549  0.50 68.35  ? 353 ASN B CB  1 
ATOM   5718 C  CB  B ASN B 1 351 ? 73.833 123.779 -57.482  0.50 65.05  ? 353 ASN B CB  1 
ATOM   5719 C  CG  A ASN B 1 351 ? 73.518 124.993 -56.982  0.50 67.00  ? 353 ASN B CG  1 
ATOM   5720 C  CG  B ASN B 1 351 ? 73.000 124.209 -58.677  0.50 60.09  ? 353 ASN B CG  1 
ATOM   5721 O  OD1 A ASN B 1 351 ? 74.026 125.450 -55.953  0.50 64.15  ? 353 ASN B OD1 1 
ATOM   5722 O  OD1 B ASN B 1 351 ? 72.682 123.407 -59.545  0.50 56.77  ? 353 ASN B OD1 1 
ATOM   5723 N  ND2 A ASN B 1 351 ? 72.588 125.636 -57.670  0.50 64.33  ? 353 ASN B ND2 1 
ATOM   5724 N  ND2 B ASN B 1 351 ? 72.636 125.476 -58.735  0.50 58.04  ? 353 ASN B ND2 1 
ATOM   5725 N  N   . ASN B 1 352 ? 73.540 121.026 -54.850  1.00 71.70  ? 354 ASN B N   1 
ATOM   5726 C  CA  . ASN B 1 352 ? 73.933 120.593 -53.476  1.00 76.22  ? 354 ASN B CA  1 
ATOM   5727 C  C   . ASN B 1 352 ? 73.717 121.729 -52.469  1.00 77.56  ? 354 ASN B C   1 
ATOM   5728 O  O   . ASN B 1 352 ? 74.635 122.024 -51.685  1.00 80.35  ? 354 ASN B O   1 
ATOM   5729 C  CB  . ASN B 1 352 ? 75.395 120.146 -53.399  1.00 79.43  ? 354 ASN B CB  1 
ATOM   5730 C  CG  . ASN B 1 352 ? 75.584 118.760 -53.964  1.00 79.56  ? 354 ASN B CG  1 
ATOM   5731 O  OD1 . ASN B 1 352 ? 75.662 117.794 -53.201  1.00 77.77  ? 354 ASN B OD1 1 
ATOM   5732 N  ND2 . ASN B 1 352 ? 75.601 118.668 -55.287  1.00 76.97  ? 354 ASN B ND2 1 
ATOM   5733 N  N   . GLN B 1 353 ? 72.547 122.354 -52.500  1.00 76.80  ? 355 GLN B N   1 
ATOM   5734 C  CA  . GLN B 1 353 ? 72.190 123.462 -51.580  1.00 74.50  ? 355 GLN B CA  1 
ATOM   5735 C  C   . GLN B 1 353 ? 70.661 123.416 -51.448  1.00 67.79  ? 355 GLN B C   1 
ATOM   5736 O  O   . GLN B 1 353 ? 69.951 124.081 -52.230  1.00 69.30  ? 355 GLN B O   1 
ATOM   5737 C  CB  . GLN B 1 353 ? 72.827 124.759 -52.101  1.00 77.82  ? 355 GLN B CB  1 
ATOM   5738 C  CG  . GLN B 1 353 ? 72.411 126.023 -51.357  1.00 80.18  ? 355 GLN B CG  1 
ATOM   5739 C  CD  . GLN B 1 353 ? 72.906 126.085 -49.932  1.00 82.90  ? 355 GLN B CD  1 
ATOM   5740 O  OE1 . GLN B 1 353 ? 74.082 126.317 -49.668  1.00 86.80  ? 355 GLN B OE1 1 
ATOM   5741 N  NE2 . GLN B 1 353 ? 71.999 125.901 -48.990  1.00 81.25  ? 355 GLN B NE2 1 
ATOM   5742 N  N   . TYR B 1 354 ? 70.180 122.638 -50.482  1.00 60.96  ? 356 TYR B N   1 
ATOM   5743 C  CA  . TYR B 1 354 ? 68.737 122.522 -50.167  1.00 54.81  ? 356 TYR B CA  1 
ATOM   5744 C  C   . TYR B 1 354 ? 68.111 123.907 -50.091  1.00 53.98  ? 356 TYR B C   1 
ATOM   5745 O  O   . TYR B 1 354 ? 68.455 124.662 -49.206  1.00 54.41  ? 356 TYR B O   1 
ATOM   5746 C  CB  . TYR B 1 354 ? 68.544 121.837 -48.820  1.00 51.57  ? 356 TYR B CB  1 
ATOM   5747 C  CG  . TYR B 1 354 ? 68.590 120.341 -48.918  1.00 50.75  ? 356 TYR B CG  1 
ATOM   5748 C  CD1 . TYR B 1 354 ? 67.892 119.685 -49.900  1.00 48.96  ? 356 TYR B CD1 1 
ATOM   5749 C  CD2 . TYR B 1 354 ? 69.346 119.587 -48.052  1.00 52.30  ? 356 TYR B CD2 1 
ATOM   5750 C  CE1 . TYR B 1 354 ? 67.938 118.313 -50.016  1.00 50.09  ? 356 TYR B CE1 1 
ATOM   5751 C  CE2 . TYR B 1 354 ? 69.402 118.212 -48.154  1.00 52.83  ? 356 TYR B CE2 1 
ATOM   5752 C  CZ  . TYR B 1 354 ? 68.695 117.569 -49.143  1.00 51.92  ? 356 TYR B CZ  1 
ATOM   5753 O  OH  . TYR B 1 354 ? 68.728 116.217 -49.260  1.00 52.45  ? 356 TYR B OH  1 
ATOM   5754 N  N   . THR B 1 355 ? 67.230 124.209 -51.036  1.00 52.51  ? 357 THR B N   1 
ATOM   5755 C  CA  . THR B 1 355 ? 66.501 125.489 -51.085  1.00 50.93  ? 357 THR B CA  1 
ATOM   5756 C  C   . THR B 1 355 ? 65.018 125.239 -50.775  1.00 47.20  ? 357 THR B C   1 
ATOM   5757 O  O   . THR B 1 355 ? 64.473 124.231 -51.248  1.00 46.02  ? 357 THR B O   1 
ATOM   5758 C  CB  . THR B 1 355 ? 66.770 126.136 -52.439  1.00 53.12  ? 357 THR B CB  1 
ATOM   5759 O  OG1 . THR B 1 355 ? 66.520 127.507 -52.165  1.00 59.20  ? 357 THR B OG1 1 
ATOM   5760 C  CG2 . THR B 1 355 ? 65.889 125.627 -53.558  1.00 52.86  ? 357 THR B CG2 1 
ATOM   5761 N  N   . GLU B 1 356 ? 64.404 126.130 -49.994  1.00 46.71  ? 358 GLU B N   1 
ATOM   5762 C  CA  . GLU B 1 356 ? 62.982 126.074 -49.551  1.00 44.14  ? 358 GLU B CA  1 
ATOM   5763 C  C   . GLU B 1 356 ? 62.120 126.374 -50.774  1.00 41.59  ? 358 GLU B C   1 
ATOM   5764 O  O   . GLU B 1 356 ? 62.397 127.386 -51.419  1.00 42.96  ? 358 GLU B O   1 
ATOM   5765 C  CB  . GLU B 1 356 ? 62.721 127.111 -48.456  1.00 45.20  ? 358 GLU B CB  1 
ATOM   5766 C  CG  . GLU B 1 356 ? 61.278 127.192 -47.973  1.00 46.17  ? 358 GLU B CG  1 
ATOM   5767 C  CD  . GLU B 1 356 ? 61.051 128.145 -46.802  1.00 47.85  ? 358 GLU B CD  1 
ATOM   5768 O  OE1 . GLU B 1 356 ? 61.760 128.019 -45.805  1.00 54.18  ? 358 GLU B OE1 1 
ATOM   5769 O  OE2 . GLU B 1 356 ? 60.189 129.030 -46.892  1.00 48.26  ? 358 GLU B OE2 1 
ATOM   5770 N  N   . ILE B 1 357 ? 61.123 125.548 -51.084  1.00 37.44  ? 359 ILE B N   1 
ATOM   5771 C  CA  . ILE B 1 357 ? 60.226 125.789 -52.258  1.00 35.50  ? 359 ILE B CA  1 
ATOM   5772 C  C   . ILE B 1 357 ? 58.763 125.986 -51.799  1.00 34.23  ? 359 ILE B C   1 
ATOM   5773 O  O   . ILE B 1 357 ? 57.991 126.655 -52.472  1.00 32.49  ? 359 ILE B O   1 
ATOM   5774 C  CB  . ILE B 1 357 ? 60.422 124.666 -53.292  1.00 34.07  ? 359 ILE B CB  1 
ATOM   5775 C  CG1 . ILE B 1 357 ? 60.038 123.285 -52.771  1.00 33.01  ? 359 ILE B CG1 1 
ATOM   5776 C  CG2 . ILE B 1 357 ? 61.855 124.664 -53.788  1.00 36.03  ? 359 ILE B CG2 1 
ATOM   5777 C  CD1 . ILE B 1 357 ? 60.250 122.171 -53.780  1.00 32.42  ? 359 ILE B CD1 1 
ATOM   5778 N  N   . LYS B 1 358 ? 58.382 125.447 -50.656  1.00 34.16  ? 360 LYS B N   1 
ATOM   5779 C  CA  . LYS B 1 358 ? 56.994 125.551 -50.168  1.00 34.08  ? 360 LYS B CA  1 
ATOM   5780 C  C   . LYS B 1 358 ? 56.941 125.312 -48.659  1.00 33.79  ? 360 LYS B C   1 
ATOM   5781 O  O   . LYS B 1 358 ? 57.490 124.333 -48.178  1.00 33.33  ? 360 LYS B O   1 
ATOM   5782 C  CB  . LYS B 1 358 ? 56.128 124.528 -50.884  1.00 33.75  ? 360 LYS B CB  1 
ATOM   5783 C  CG  . LYS B 1 358 ? 54.649 124.653 -50.578  1.00 34.57  ? 360 LYS B CG  1 
ATOM   5784 C  CD  . LYS B 1 358 ? 54.119 126.053 -50.773  1.00 36.24  ? 360 LYS B CD  1 
ATOM   5785 C  CE  . LYS B 1 358 ? 52.632 126.146 -50.530  1.00 39.21  ? 360 LYS B CE  1 
ATOM   5786 N  NZ  . LYS B 1 358 ? 52.053 127.243 -51.345  1.00 42.48  ? 360 LYS B NZ  1 
ATOM   5787 N  N   . LYS B 1 359 ? 56.263 126.192 -47.952  1.00 34.96  ? 361 LYS B N   1 
ATOM   5788 C  CA  . LYS B 1 359 ? 55.993 126.021 -46.508  1.00 35.99  ? 361 LYS B CA  1 
ATOM   5789 C  C   . LYS B 1 359 ? 54.487 126.127 -46.276  1.00 33.51  ? 361 LYS B C   1 
ATOM   5790 O  O   . LYS B 1 359 ? 53.859 127.031 -46.827  1.00 31.73  ? 361 LYS B O   1 
ATOM   5791 C  CB  . LYS B 1 359 ? 56.769 127.068 -45.711  1.00 40.40  ? 361 LYS B CB  1 
ATOM   5792 C  CG  . LYS B 1 359 ? 56.504 127.076 -44.212  1.00 44.83  ? 361 LYS B CG  1 
ATOM   5793 C  CD  . LYS B 1 359 ? 57.610 127.700 -43.346  1.00 50.11  ? 361 LYS B CD  1 
ATOM   5794 C  CE  . LYS B 1 359 ? 58.225 128.958 -43.950  1.00 54.14  ? 361 LYS B CE  1 
ATOM   5795 N  NZ  . LYS B 1 359 ? 57.213 130.015 -44.223  1.00 54.42  ? 361 LYS B NZ  1 
ATOM   5796 N  N   . PHE B 1 360 ? 53.950 125.215 -45.470  1.00 31.37  ? 362 PHE B N   1 
ATOM   5797 C  CA  . PHE B 1 360 ? 52.601 125.318 -44.865  1.00 30.67  ? 362 PHE B CA  1 
ATOM   5798 C  C   . PHE B 1 360 ? 52.753 125.628 -43.361  1.00 30.53  ? 362 PHE B C   1 
ATOM   5799 O  O   . PHE B 1 360 ? 53.368 124.819 -42.660  1.00 27.61  ? 362 PHE B O   1 
ATOM   5800 C  CB  . PHE B 1 360 ? 51.824 124.022 -45.103  1.00 29.56  ? 362 PHE B CB  1 
ATOM   5801 C  CG  . PHE B 1 360 ? 51.481 123.732 -46.536  1.00 29.73  ? 362 PHE B CG  1 
ATOM   5802 C  CD1 . PHE B 1 360 ? 50.434 124.389 -47.154  1.00 30.58  ? 362 PHE B CD1 1 
ATOM   5803 C  CD2 . PHE B 1 360 ? 52.167 122.766 -47.249  1.00 29.60  ? 362 PHE B CD2 1 
ATOM   5804 C  CE1 . PHE B 1 360 ? 50.103 124.104 -48.469  1.00 31.41  ? 362 PHE B CE1 1 
ATOM   5805 C  CE2 . PHE B 1 360 ? 51.835 122.474 -48.562  1.00 29.95  ? 362 PHE B CE2 1 
ATOM   5806 C  CZ  . PHE B 1 360 ? 50.803 123.148 -49.175  1.00 31.07  ? 362 PHE B CZ  1 
ATOM   5807 N  N   . GLU B 1 361 ? 52.231 126.764 -42.904  1.00 31.81  ? 363 GLU B N   1 
ATOM   5808 C  CA  . GLU B 1 361 ? 52.035 127.086 -41.466  1.00 33.11  ? 363 GLU B CA  1 
ATOM   5809 C  C   . GLU B 1 361 ? 50.943 126.150 -40.913  1.00 30.88  ? 363 GLU B C   1 
ATOM   5810 O  O   . GLU B 1 361 ? 50.204 125.566 -41.708  1.00 30.10  ? 363 GLU B O   1 
ATOM   5811 C  CB  . GLU B 1 361 ? 51.752 128.591 -41.344  1.00 38.01  ? 363 GLU B CB  1 
ATOM   5812 C  CG  . GLU B 1 361 ? 52.514 129.306 -40.202  1.00 44.43  ? 363 GLU B CG  1 
ATOM   5813 C  CD  . GLU B 1 361 ? 54.001 129.620 -40.428  1.00 48.10  ? 363 GLU B CD  1 
ATOM   5814 O  OE1 . GLU B 1 361 ? 54.338 130.059 -41.549  1.00 50.59  ? 363 GLU B OE1 1 
ATOM   5815 O  OE2 . GLU B 1 361 ? 54.834 129.423 -39.482  1.00 50.68  ? 363 GLU B OE2 1 
ATOM   5816 N  N   . ALA B 1 362 ? 50.877 126.036 -39.585  1.00 31.07  ? 364 ALA B N   1 
ATOM   5817 C  CA  . ALA B 1 362 ? 50.010 125.076 -38.867  1.00 30.23  ? 364 ALA B CA  1 
ATOM   5818 C  C   . ALA B 1 362 ? 48.603 125.580 -38.544  1.00 30.68  ? 364 ALA B C   1 
ATOM   5819 O  O   . ALA B 1 362 ? 48.454 126.733 -38.300  1.00 30.39  ? 364 ALA B O   1 
ATOM   5820 C  CB  . ALA B 1 362 ? 50.736 124.572 -37.661  1.00 30.65  ? 364 ALA B CB  1 
ATOM   5821 N  N   . ASP B 1 363 ? 47.645 124.662 -38.547  1.00 31.73  ? 365 ASP B N   1 
ATOM   5822 C  CA  A ASP B 1 363 ? 46.159 124.788 -38.302  0.50 30.85  ? 365 ASP B CA  1 
ATOM   5823 C  CA  B ASP B 1 363 ? 46.167 124.769 -38.433  0.50 30.83  ? 365 ASP B CA  1 
ATOM   5824 C  C   . ASP B 1 363 ? 45.337 123.436 -38.165  1.00 29.64  ? 365 ASP B C   1 
ATOM   5825 O  O   . ASP B 1 363 ? 45.773 122.295 -37.743  1.00 30.96  ? 365 ASP B O   1 
ATOM   5826 C  CB  A ASP B 1 363 ? 45.478 125.675 -39.350  0.50 31.91  ? 365 ASP B CB  1 
ATOM   5827 C  CB  B ASP B 1 363 ? 45.549 125.533 -39.613  0.50 31.83  ? 365 ASP B CB  1 
ATOM   5828 C  CG  A ASP B 1 363 ? 45.343 127.153 -39.004  0.50 32.37  ? 365 ASP B CG  1 
ATOM   5829 C  CG  B ASP B 1 363 ? 45.894 125.001 -41.006  0.50 31.45  ? 365 ASP B CG  1 
ATOM   5830 O  OD1 A ASP B 1 363 ? 44.513 127.487 -38.140  0.50 30.62  ? 365 ASP B OD1 1 
ATOM   5831 O  OD1 B ASP B 1 363 ? 45.022 125.056 -41.901  0.50 29.45  ? 365 ASP B OD1 1 
ATOM   5832 O  OD2 A ASP B 1 363 ? 46.037 127.975 -39.647  0.50 30.11  ? 365 ASP B OD2 1 
ATOM   5833 O  OD2 B ASP B 1 363 ? 47.049 124.535 -41.194  0.50 28.77  ? 365 ASP B OD2 1 
ATOM   5834 N  N   . SER B 1 364 ? 44.160 123.408 -38.778  1.00 27.04  ? 366 SER B N   1 
ATOM   5835 C  CA  . SER B 1 364 ? 43.320 122.176 -38.679  1.00 25.83  ? 366 SER B CA  1 
ATOM   5836 C  C   . SER B 1 364 ? 43.610 121.187 -39.803  1.00 24.26  ? 366 SER B C   1 
ATOM   5837 O  O   . SER B 1 364 ? 43.261 120.030 -39.687  1.00 22.70  ? 366 SER B O   1 
ATOM   5838 C  CB  . SER B 1 364 ? 41.846 122.425 -38.532  1.00 26.73  ? 366 SER B CB  1 
ATOM   5839 O  OG  . SER B 1 364 ? 41.299 123.155 -39.596  1.00 27.19  ? 366 SER B OG  1 
ATOM   5840 N  N   . ASN B 1 365 ? 44.258 121.665 -40.843  1.00 23.67  ? 367 ASN B N   1 
ATOM   5841 C  CA  . ASN B 1 365 ? 44.589 120.848 -42.022  1.00 23.31  ? 367 ASN B CA  1 
ATOM   5842 C  C   . ASN B 1 365 ? 45.541 119.723 -41.637  1.00 21.56  ? 367 ASN B C   1 
ATOM   5843 O  O   . ASN B 1 365 ? 46.491 119.972 -40.847  1.00 21.36  ? 367 ASN B O   1 
ATOM   5844 C  CB  . ASN B 1 365 ? 45.193 121.706 -43.134  1.00 23.92  ? 367 ASN B CB  1 
ATOM   5845 C  CG  . ASN B 1 365 ? 44.904 121.072 -44.469  1.00 25.59  ? 367 ASN B CG  1 
ATOM   5846 O  OD1 . ASN B 1 365 ? 43.723 120.916 -44.849  1.00 28.40  ? 367 ASN B OD1 1 
ATOM   5847 N  ND2 . ASN B 1 365 ? 45.970 120.643 -45.132  1.00 24.70  ? 367 ASN B ND2 1 
ATOM   5848 N  N   . SER B 1 366 ? 45.274 118.534 -42.155  1.00 20.61  ? 368 SER B N   1 
ATOM   5849 C  CA  . SER B 1 366 ? 46.126 117.335 -41.977  1.00 20.24  ? 368 SER B CA  1 
ATOM   5850 C  C   . SER B 1 366 ? 46.698 116.824 -43.312  1.00 20.03  ? 368 SER B C   1 
ATOM   5851 O  O   . SER B 1 366 ? 47.540 115.910 -43.288  1.00 19.86  ? 368 SER B O   1 
ATOM   5852 C  CB  . SER B 1 366 ? 45.330 116.308 -41.250  1.00 20.59  ? 368 SER B CB  1 
ATOM   5853 O  OG  . SER B 1 366 ? 45.264 116.666 -39.872  1.00 21.19  ? 368 SER B OG  1 
ATOM   5854 N  N   . THR B 1 367 ? 46.288 117.397 -44.438  1.00 19.71  ? 369 THR B N   1 
ATOM   5855 C  CA  . THR B 1 367 ? 46.790 117.025 -45.776  1.00 19.71  ? 369 THR B CA  1 
ATOM   5856 C  C   . THR B 1 367 ? 47.583 118.185 -46.385  1.00 19.72  ? 369 THR B C   1 
ATOM   5857 O  O   . THR B 1 367 ? 47.037 119.263 -46.538  1.00 20.01  ? 369 THR B O   1 
ATOM   5858 C  CB  . THR B 1 367 ? 45.628 116.599 -46.662  1.00 20.23  ? 369 THR B CB  1 
ATOM   5859 O  OG1 . THR B 1 367 ? 45.083 115.447 -46.038  1.00 20.64  ? 369 THR B OG1 1 
ATOM   5860 C  CG2 . THR B 1 367 ? 46.055 116.245 -48.069  1.00 20.49  ? 369 THR B CG2 1 
ATOM   5861 N  N   . PHE B 1 368 ? 48.843 117.964 -46.728  1.00 19.40  ? 370 PHE B N   1 
ATOM   5862 C  CA  . PHE B 1 368 ? 49.695 119.006 -47.337  1.00 19.53  ? 370 PHE B CA  1 
ATOM   5863 C  C   . PHE B 1 368 ? 50.005 118.606 -48.785  1.00 19.82  ? 370 PHE B C   1 
ATOM   5864 O  O   . PHE B 1 368 ? 50.660 117.596 -49.016  1.00 19.21  ? 370 PHE B O   1 
ATOM   5865 C  CB  . PHE B 1 368 ? 50.926 119.221 -46.469  1.00 19.34  ? 370 PHE B CB  1 
ATOM   5866 C  CG  . PHE B 1 368 ? 50.573 119.458 -45.018  1.00 19.38  ? 370 PHE B CG  1 
ATOM   5867 C  CD1 . PHE B 1 368 ? 50.264 118.391 -44.181  1.00 19.18  ? 370 PHE B CD1 1 
ATOM   5868 C  CD2 . PHE B 1 368 ? 50.429 120.757 -44.538  1.00 19.38  ? 370 PHE B CD2 1 
ATOM   5869 C  CE1 . PHE B 1 368 ? 49.898 118.626 -42.857  1.00 19.91  ? 370 PHE B CE1 1 
ATOM   5870 C  CE2 . PHE B 1 368 ? 50.056 120.986 -43.225  1.00 19.70  ? 370 PHE B CE2 1 
ATOM   5871 C  CZ  . PHE B 1 368 ? 49.785 119.919 -42.393  1.00 19.67  ? 370 PHE B CZ  1 
ATOM   5872 N  N   . ASP B 1 369 ? 49.507 119.392 -49.738  1.00 20.99  ? 371 ASP B N   1 
ATOM   5873 C  CA  . ASP B 1 369 ? 49.570 119.078 -51.200  1.00 21.72  ? 371 ASP B CA  1 
ATOM   5874 C  C   . ASP B 1 369 ? 50.615 119.998 -51.820  1.00 21.30  ? 371 ASP B C   1 
ATOM   5875 O  O   . ASP B 1 369 ? 50.309 121.178 -51.956  1.00 22.61  ? 371 ASP B O   1 
ATOM   5876 C  CB  . ASP B 1 369 ? 48.216 119.209 -51.911  1.00 22.40  ? 371 ASP B CB  1 
ATOM   5877 C  CG  . ASP B 1 369 ? 47.248 118.057 -51.639  1.00 23.46  ? 371 ASP B CG  1 
ATOM   5878 O  OD1 . ASP B 1 369 ? 47.611 116.860 -51.854  1.00 23.85  ? 371 ASP B OD1 1 
ATOM   5879 O  OD2 . ASP B 1 369 ? 46.124 118.355 -51.218  1.00 25.49  ? 371 ASP B OD2 1 
ATOM   5880 N  N   . PHE B 1 370 ? 51.826 119.487 -52.039  1.00 20.21  ? 372 PHE B N   1 
ATOM   5881 C  CA  . PHE B 1 370 ? 52.933 120.216 -52.685  1.00 19.94  ? 372 PHE B CA  1 
ATOM   5882 C  C   . PHE B 1 370 ? 52.783 119.976 -54.192  1.00 20.42  ? 372 PHE B C   1 
ATOM   5883 O  O   . PHE B 1 370 ? 53.191 118.897 -54.675  1.00 20.34  ? 372 PHE B O   1 
ATOM   5884 C  CB  . PHE B 1 370 ? 54.256 119.726 -52.133  1.00 19.42  ? 372 PHE B CB  1 
ATOM   5885 C  CG  . PHE B 1 370 ? 54.454 120.004 -50.662  1.00 19.49  ? 372 PHE B CG  1 
ATOM   5886 C  CD1 . PHE B 1 370 ? 54.036 119.085 -49.711  1.00 19.22  ? 372 PHE B CD1 1 
ATOM   5887 C  CD2 . PHE B 1 370 ? 55.077 121.166 -50.243  1.00 19.07  ? 372 PHE B CD2 1 
ATOM   5888 C  CE1 . PHE B 1 370 ? 54.223 119.321 -48.366  1.00 19.57  ? 372 PHE B CE1 1 
ATOM   5889 C  CE2 . PHE B 1 370 ? 55.254 121.408 -48.897  1.00 19.53  ? 372 PHE B CE2 1 
ATOM   5890 C  CZ  . PHE B 1 370 ? 54.823 120.492 -47.965  1.00 19.54  ? 372 PHE B CZ  1 
ATOM   5891 N  N   . LYS B 1 371 ? 52.110 120.895 -54.876  1.00 20.69  ? 373 LYS B N   1 
ATOM   5892 C  CA  . LYS B 1 371 ? 51.872 120.783 -56.332  1.00 21.98  ? 373 LYS B CA  1 
ATOM   5893 C  C   . LYS B 1 371 ? 53.100 121.286 -57.081  1.00 20.85  ? 373 LYS B C   1 
ATOM   5894 O  O   . LYS B 1 371 ? 53.561 122.393 -56.809  1.00 20.31  ? 373 LYS B O   1 
ATOM   5895 C  CB  . LYS B 1 371 ? 50.615 121.568 -56.692  1.00 24.26  ? 373 LYS B CB  1 
ATOM   5896 C  CG  . LYS B 1 371 ? 49.322 120.971 -56.135  1.00 27.54  ? 373 LYS B CG  1 
ATOM   5897 C  CD  . LYS B 1 371 ? 48.104 121.480 -56.883  1.00 31.89  ? 373 LYS B CD  1 
ATOM   5898 C  CE  . LYS B 1 371 ? 46.777 120.897 -56.432  1.00 35.92  ? 373 LYS B CE  1 
ATOM   5899 N  NZ  . LYS B 1 371 ? 46.378 121.360 -55.067  1.00 40.04  ? 373 LYS B NZ  1 
ATOM   5900 N  N   . GLY B 1 372 ? 53.587 120.536 -58.052  1.00 20.95  ? 374 GLY B N   1 
ATOM   5901 C  CA  . GLY B 1 372 ? 54.437 121.132 -59.101  1.00 20.59  ? 374 GLY B CA  1 
ATOM   5902 C  C   . GLY B 1 372 ? 55.892 120.829 -58.866  1.00 20.77  ? 374 GLY B C   1 
ATOM   5903 O  O   . GLY B 1 372 ? 56.713 121.766 -58.926  1.00 19.56  ? 374 GLY B O   1 
ATOM   5904 N  N   . LEU B 1 373 ? 56.167 119.564 -58.552  1.00 21.85  ? 375 LEU B N   1 
ATOM   5905 C  CA  . LEU B 1 373 ? 57.527 119.048 -58.272  1.00 22.96  ? 375 LEU B CA  1 
ATOM   5906 C  C   . LEU B 1 373 ? 58.013 118.284 -59.485  1.00 24.05  ? 375 LEU B C   1 
ATOM   5907 O  O   . LEU B 1 373 ? 57.192 117.621 -60.139  1.00 23.44  ? 375 LEU B O   1 
ATOM   5908 C  CB  . LEU B 1 373 ? 57.499 118.112 -57.066  1.00 22.79  ? 375 LEU B CB  1 
ATOM   5909 C  CG  . LEU B 1 373 ? 56.872 118.699 -55.812  1.00 22.76  ? 375 LEU B CG  1 
ATOM   5910 C  CD1 . LEU B 1 373 ? 57.097 117.730 -54.687  1.00 23.29  ? 375 LEU B CD1 1 
ATOM   5911 C  CD2 . LEU B 1 373 ? 57.435 120.087 -55.488  1.00 22.98  ? 375 LEU B CD2 1 
ATOM   5912 N  N   . ASP B 1 374 ? 59.319 118.329 -59.701  1.00 26.07  ? 376 ASP B N   1 
ATOM   5913 C  CA  . ASP B 1 374 ? 59.974 117.582 -60.800  1.00 28.47  ? 376 ASP B CA  1 
ATOM   5914 C  C   . ASP B 1 374 ? 60.901 116.515 -60.208  1.00 29.54  ? 376 ASP B C   1 
ATOM   5915 O  O   . ASP B 1 374 ? 60.969 116.377 -58.957  1.00 29.24  ? 376 ASP B O   1 
ATOM   5916 C  CB  . ASP B 1 374 ? 60.690 118.542 -61.767  1.00 29.84  ? 376 ASP B CB  1 
ATOM   5917 C  CG  . ASP B 1 374 ? 61.805 119.416 -61.187  1.00 31.16  ? 376 ASP B CG  1 
ATOM   5918 O  OD1 . ASP B 1 374 ? 62.056 119.312 -59.988  1.00 31.69  ? 376 ASP B OD1 1 
ATOM   5919 O  OD2 . ASP B 1 374 ? 62.413 120.256 -61.963  1.00 34.04  ? 376 ASP B OD2 1 
ATOM   5920 N  N   . SER B 1 375 ? 61.632 115.825 -61.083  1.00 30.75  ? 377 SER B N   1 
ATOM   5921 C  CA  . SER B 1 375 ? 62.689 114.868 -60.690  1.00 31.60  ? 377 SER B CA  1 
ATOM   5922 C  C   . SER B 1 375 ? 63.795 115.652 -59.970  1.00 32.97  ? 377 SER B C   1 
ATOM   5923 O  O   . SER B 1 375 ? 64.149 116.761 -60.373  1.00 34.46  ? 377 SER B O   1 
ATOM   5924 C  CB  . SER B 1 375 ? 63.169 114.093 -61.874  1.00 32.14  ? 377 SER B CB  1 
ATOM   5925 O  OG  . SER B 1 375 ? 62.094 113.363 -62.467  1.00 31.33  ? 377 SER B OG  1 
ATOM   5926 N  N   . GLY B 1 376 ? 64.287 115.121 -58.872  1.00 33.04  ? 378 GLY B N   1 
ATOM   5927 C  CA  . GLY B 1 376 ? 65.274 115.821 -58.044  1.00 34.26  ? 378 GLY B CA  1 
ATOM   5928 C  C   . GLY B 1 376 ? 65.284 115.265 -56.630  1.00 34.51  ? 378 GLY B C   1 
ATOM   5929 O  O   . GLY B 1 376 ? 64.549 114.289 -56.317  1.00 32.01  ? 378 GLY B O   1 
ATOM   5930 N  N   . ASP B 1 377 ? 66.094 115.885 -55.782  1.00 38.27  ? 379 ASP B N   1 
ATOM   5931 C  CA  . ASP B 1 377 ? 66.318 115.431 -54.391  1.00 38.68  ? 379 ASP B CA  1 
ATOM   5932 C  C   . ASP B 1 377 ? 65.703 116.470 -53.477  1.00 37.20  ? 379 ASP B C   1 
ATOM   5933 O  O   . ASP B 1 377 ? 65.979 117.676 -53.638  1.00 37.10  ? 379 ASP B O   1 
ATOM   5934 C  CB  . ASP B 1 377 ? 67.805 115.233 -54.086  1.00 43.23  ? 379 ASP B CB  1 
ATOM   5935 C  CG  . ASP B 1 377 ? 68.447 114.096 -54.869  1.00 45.62  ? 379 ASP B CG  1 
ATOM   5936 O  OD1 . ASP B 1 377 ? 67.748 113.107 -55.162  1.00 45.14  ? 379 ASP B OD1 1 
ATOM   5937 O  OD2 . ASP B 1 377 ? 69.632 114.228 -55.214  1.00 50.63  ? 379 ASP B OD2 1 
ATOM   5938 N  N   . TYR B 1 378 ? 64.905 115.976 -52.547  1.00 35.26  ? 380 TYR B N   1 
ATOM   5939 C  CA  . TYR B 1 378 ? 64.026 116.801 -51.709  1.00 33.65  ? 380 TYR B CA  1 
ATOM   5940 C  C   . TYR B 1 378 ? 64.304 116.443 -50.265  1.00 34.24  ? 380 TYR B C   1 
ATOM   5941 O  O   . TYR B 1 378 ? 64.706 115.301 -49.982  1.00 34.53  ? 380 TYR B O   1 
ATOM   5942 C  CB  . TYR B 1 378 ? 62.566 116.569 -52.093  1.00 32.05  ? 380 TYR B CB  1 
ATOM   5943 C  CG  . TYR B 1 378 ? 62.203 117.115 -53.449  1.00 30.79  ? 380 TYR B CG  1 
ATOM   5944 C  CD1 . TYR B 1 378 ? 61.912 118.462 -53.631  1.00 30.81  ? 380 TYR B CD1 1 
ATOM   5945 C  CD2 . TYR B 1 378 ? 62.166 116.296 -54.561  1.00 31.07  ? 380 TYR B CD2 1 
ATOM   5946 C  CE1 . TYR B 1 378 ? 61.551 118.971 -54.869  1.00 29.32  ? 380 TYR B CE1 1 
ATOM   5947 C  CE2 . TYR B 1 378 ? 61.847 116.793 -55.819  1.00 29.74  ? 380 TYR B CE2 1 
ATOM   5948 C  CZ  . TYR B 1 378 ? 61.552 118.134 -55.967  1.00 29.33  ? 380 TYR B CZ  1 
ATOM   5949 O  OH  . TYR B 1 378 ? 61.213 118.635 -57.176  1.00 28.59  ? 380 TYR B OH  1 
ATOM   5950 N  N   . LYS B 1 379 ? 64.060 117.415 -49.401  1.00 34.85  ? 381 LYS B N   1 
ATOM   5951 C  CA  . LYS B 1 379 ? 64.011 117.222 -47.931  1.00 35.12  ? 381 LYS B CA  1 
ATOM   5952 C  C   . LYS B 1 379 ? 62.701 117.788 -47.393  1.00 31.82  ? 381 LYS B C   1 
ATOM   5953 O  O   . LYS B 1 379 ? 62.450 118.987 -47.551  1.00 29.91  ? 381 LYS B O   1 
ATOM   5954 C  CB  . LYS B 1 379 ? 65.194 117.918 -47.263  1.00 39.11  ? 381 LYS B CB  1 
ATOM   5955 C  CG  . LYS B 1 379 ? 65.396 117.543 -45.793  1.00 40.93  ? 381 LYS B CG  1 
ATOM   5956 C  CD  . LYS B 1 379 ? 66.653 118.140 -45.140  1.00 44.02  ? 381 LYS B CD  1 
ATOM   5957 C  CE  . LYS B 1 379 ? 66.705 119.664 -45.195  1.00 44.73  ? 381 LYS B CE  1 
ATOM   5958 N  NZ  . LYS B 1 379 ? 67.891 120.242 -44.504  1.00 46.53  ? 381 LYS B NZ  1 
ATOM   5959 N  N   . LEU B 1 380 ? 61.933 116.947 -46.722  1.00 30.03  ? 382 LEU B N   1 
ATOM   5960 C  CA  . LEU B 1 380 ? 60.708 117.369 -45.999  1.00 28.28  ? 382 LEU B CA  1 
ATOM   5961 C  C   . LEU B 1 380 ? 61.000 117.560 -44.495  1.00 29.10  ? 382 LEU B C   1 
ATOM   5962 O  O   . LEU B 1 380 ? 61.539 116.643 -43.844  1.00 30.08  ? 382 LEU B O   1 
ATOM   5963 C  CB  . LEU B 1 380 ? 59.672 116.284 -46.245  1.00 27.08  ? 382 LEU B CB  1 
ATOM   5964 C  CG  . LEU B 1 380 ? 58.307 116.579 -45.654  1.00 26.00  ? 382 LEU B CG  1 
ATOM   5965 C  CD1 . LEU B 1 380 ? 57.701 117.805 -46.334  1.00 24.84  ? 382 LEU B CD1 1 
ATOM   5966 C  CD2 . LEU B 1 380 ? 57.421 115.335 -45.746  1.00 25.81  ? 382 LEU B CD2 1 
ATOM   5967 N  N   . VAL B 1 381 ? 60.669 118.732 -43.967  1.00 28.28  ? 383 VAL B N   1 
ATOM   5968 C  CA  . VAL B 1 381 ? 60.956 119.107 -42.561  1.00 29.19  ? 383 VAL B CA  1 
ATOM   5969 C  C   . VAL B 1 381 ? 59.630 119.424 -41.895  1.00 28.63  ? 383 VAL B C   1 
ATOM   5970 O  O   . VAL B 1 381 ? 58.898 120.306 -42.432  1.00 27.67  ? 383 VAL B O   1 
ATOM   5971 C  CB  . VAL B 1 381 ? 61.887 120.323 -42.468  1.00 30.27  ? 383 VAL B CB  1 
ATOM   5972 C  CG1 . VAL B 1 381 ? 62.053 120.759 -41.013  1.00 31.27  ? 383 VAL B CG1 1 
ATOM   5973 C  CG2 . VAL B 1 381 ? 63.222 120.031 -43.125  1.00 32.17  ? 383 VAL B CG2 1 
ATOM   5974 N  N   . GLU B 1 382 ? 59.350 118.797 -40.748  1.00 29.18  ? 384 GLU B N   1 
ATOM   5975 C  CA  . GLU B 1 382 ? 58.091 119.084 -40.026  1.00 27.75  ? 384 GLU B CA  1 
ATOM   5976 C  C   . GLU B 1 382 ? 58.361 120.365 -39.256  1.00 26.90  ? 384 GLU B C   1 
ATOM   5977 O  O   . GLU B 1 382 ? 58.687 120.290 -38.127  1.00 26.60  ? 384 GLU B O   1 
ATOM   5978 C  CB  . GLU B 1 382 ? 57.626 117.854 -39.260  1.00 29.10  ? 384 GLU B CB  1 
ATOM   5979 C  CG  . GLU B 1 382 ? 56.334 118.099 -38.510  1.00 31.08  ? 384 GLU B CG  1 
ATOM   5980 C  CD  . GLU B 1 382 ? 56.005 117.114 -37.397  1.00 32.98  ? 384 GLU B CD  1 
ATOM   5981 O  OE1 . GLU B 1 382 ? 56.880 116.793 -36.619  1.00 39.41  ? 384 GLU B OE1 1 
ATOM   5982 O  OE2 . GLU B 1 382 ? 54.857 116.695 -37.270  1.00 37.03  ? 384 GLU B OE2 1 
ATOM   5983 N  N   . SER B 1 383 ? 58.243 121.513 -39.899  1.00 27.04  ? 385 SER B N   1 
ATOM   5984 C  CA  . SER B 1 383 ? 58.652 122.827 -39.343  1.00 28.87  ? 385 SER B CA  1 
ATOM   5985 C  C   . SER B 1 383 ? 57.749 123.262 -38.187  1.00 30.20  ? 385 SER B C   1 
ATOM   5986 O  O   . SER B 1 383 ? 58.055 124.279 -37.556  1.00 32.29  ? 385 SER B O   1 
ATOM   5987 C  CB  . SER B 1 383 ? 58.665 123.861 -40.416  1.00 29.75  ? 385 SER B CB  1 
ATOM   5988 O  OG  . SER B 1 383 ? 57.511 123.746 -41.237  1.00 29.10  ? 385 SER B OG  1 
ATOM   5989 N  N   . THR B 1 384 ? 56.642 122.561 -37.937  1.00 29.99  ? 386 THR B N   1 
ATOM   5990 C  CA  . THR B 1 384 ? 55.803 122.771 -36.743  1.00 29.19  ? 386 THR B CA  1 
ATOM   5991 C  C   . THR B 1 384 ? 55.315 121.415 -36.249  1.00 28.48  ? 386 THR B C   1 
ATOM   5992 O  O   . THR B 1 384 ? 54.799 120.640 -37.040  1.00 26.00  ? 386 THR B O   1 
ATOM   5993 C  CB  . THR B 1 384 ? 54.641 123.733 -36.987  1.00 29.48  ? 386 THR B CB  1 
ATOM   5994 O  OG1 . THR B 1 384 ? 55.124 124.898 -37.657  1.00 30.17  ? 386 THR B OG1 1 
ATOM   5995 C  CG2 . THR B 1 384 ? 53.963 124.103 -35.683  1.00 29.31  ? 386 THR B CG2 1 
ATOM   5996 N  N   . VAL B 1 385 ? 55.506 121.170 -34.957  1.00 28.94  ? 387 VAL B N   1 
ATOM   5997 C  CA  . VAL B 1 385 ? 55.172 119.871 -34.309  1.00 28.95  ? 387 VAL B CA  1 
ATOM   5998 C  C   . VAL B 1 385 ? 53.867 120.080 -33.557  1.00 26.99  ? 387 VAL B C   1 
ATOM   5999 O  O   . VAL B 1 385 ? 53.708 121.030 -32.793  1.00 27.31  ? 387 VAL B O   1 
ATOM   6000 C  CB  . VAL B 1 385 ? 56.329 119.342 -33.431  1.00 30.22  ? 387 VAL B CB  1 
ATOM   6001 C  CG1 . VAL B 1 385 ? 56.040 117.956 -32.866  1.00 30.35  ? 387 VAL B CG1 1 
ATOM   6002 C  CG2 . VAL B 1 385 ? 57.626 119.299 -34.230  1.00 30.74  ? 387 VAL B CG2 1 
ATOM   6003 N  N   . PRO B 1 386 ? 52.858 119.227 -33.788  1.00 25.67  ? 388 PRO B N   1 
ATOM   6004 C  CA  . PRO B 1 386 ? 51.657 119.277 -32.960  1.00 26.73  ? 388 PRO B CA  1 
ATOM   6005 C  C   . PRO B 1 386 ? 52.062 119.076 -31.484  1.00 27.79  ? 388 PRO B C   1 
ATOM   6006 O  O   . PRO B 1 386 ? 52.876 118.197 -31.177  1.00 28.10  ? 388 PRO B O   1 
ATOM   6007 C  CB  . PRO B 1 386 ? 50.777 118.130 -33.467  1.00 25.45  ? 388 PRO B CB  1 
ATOM   6008 C  CG  . PRO B 1 386 ? 51.358 117.819 -34.817  1.00 25.57  ? 388 PRO B CG  1 
ATOM   6009 C  CD  . PRO B 1 386 ? 52.833 118.132 -34.748  1.00 25.37  ? 388 PRO B CD  1 
ATOM   6010 N  N   . SER B 1 387 ? 51.522 119.913 -30.614  1.00 28.41  ? 389 SER B N   1 
ATOM   6011 C  CA  . SER B 1 387 ? 51.630 119.793 -29.147  1.00 28.73  ? 389 SER B CA  1 
ATOM   6012 C  C   . SER B 1 387 ? 51.303 118.353 -28.697  1.00 28.53  ? 389 SER B C   1 
ATOM   6013 O  O   . SER B 1 387 ? 50.265 117.840 -29.078  1.00 28.43  ? 389 SER B O   1 
ATOM   6014 C  CB  . SER B 1 387 ? 50.699 120.786 -28.555  1.00 30.29  ? 389 SER B CB  1 
ATOM   6015 O  OG  . SER B 1 387 ? 50.857 120.812 -27.143  1.00 33.51  ? 389 SER B OG  1 
ATOM   6016 N  N   . GLY B 1 388 ? 52.155 117.717 -27.885  1.00 29.43  ? 390 GLY B N   1 
ATOM   6017 C  CA  . GLY B 1 388 ? 51.916 116.362 -27.334  1.00 28.16  ? 390 GLY B CA  1 
ATOM   6018 C  C   . GLY B 1 388 ? 52.546 115.262 -28.174  1.00 27.14  ? 390 GLY B C   1 
ATOM   6019 O  O   . GLY B 1 388 ? 52.460 114.103 -27.791  1.00 26.75  ? 390 GLY B O   1 
ATOM   6020 N  N   . TYR B 1 389 ? 53.191 115.609 -29.286  1.00 26.41  ? 391 TYR B N   1 
ATOM   6021 C  CA  . TYR B 1 389 ? 53.730 114.638 -30.263  1.00 25.31  ? 391 TYR B CA  1 
ATOM   6022 C  C   . TYR B 1 389 ? 55.222 114.886 -30.435  1.00 25.03  ? 391 TYR B C   1 
ATOM   6023 O  O   . TYR B 1 389 ? 55.689 116.056 -30.343  1.00 24.25  ? 391 TYR B O   1 
ATOM   6024 C  CB  . TYR B 1 389 ? 52.924 114.747 -31.570  1.00 25.77  ? 391 TYR B CB  1 
ATOM   6025 C  CG  . TYR B 1 389 ? 51.534 114.221 -31.392  1.00 25.80  ? 391 TYR B CG  1 
ATOM   6026 C  CD1 . TYR B 1 389 ? 51.283 112.867 -31.488  1.00 26.32  ? 391 TYR B CD1 1 
ATOM   6027 C  CD2 . TYR B 1 389 ? 50.508 115.056 -31.001  1.00 26.31  ? 391 TYR B CD2 1 
ATOM   6028 C  CE1 . TYR B 1 389 ? 50.016 112.350 -31.292  1.00 26.97  ? 391 TYR B CE1 1 
ATOM   6029 C  CE2 . TYR B 1 389 ? 49.226 114.562 -30.810  1.00 27.34  ? 391 TYR B CE2 1 
ATOM   6030 C  CZ  . TYR B 1 389 ? 48.984 113.201 -30.947  1.00 27.96  ? 391 TYR B CZ  1 
ATOM   6031 O  OH  . TYR B 1 389 ? 47.746 112.676 -30.708  1.00 30.09  ? 391 TYR B OH  1 
ATOM   6032 N  N   . ASN B 1 390 ? 55.947 113.807 -30.734  1.00 26.07  ? 392 ASN B N   1 
ATOM   6033 C  CA  . ASN B 1 390 ? 57.388 113.846 -31.107  1.00 28.08  ? 392 ASN B CA  1 
ATOM   6034 C  C   . ASN B 1 390 ? 57.531 114.449 -32.509  1.00 29.01  ? 392 ASN B C   1 
ATOM   6035 O  O   . ASN B 1 390 ? 56.676 114.161 -33.394  1.00 29.14  ? 392 ASN B O   1 
ATOM   6036 C  CB  . ASN B 1 390 ? 58.003 112.452 -30.975  1.00 29.75  ? 392 ASN B CB  1 
ATOM   6037 C  CG  . ASN B 1 390 ? 58.032 111.998 -29.522  1.00 32.24  ? 392 ASN B CG  1 
ATOM   6038 O  OD1 . ASN B 1 390 ? 57.537 110.909 -29.182  1.00 34.24  ? 392 ASN B OD1 1 
ATOM   6039 N  ND2 . ASN B 1 390 ? 58.508 112.878 -28.651  1.00 30.99  ? 392 ASN B ND2 1 
ATOM   6040 N  N   . ALA B 1 391 ? 58.570 115.256 -32.708  1.00 30.44  ? 393 ALA B N   1 
ATOM   6041 C  CA  . ALA B 1 391 ? 59.018 115.710 -34.045  1.00 31.05  ? 393 ALA B CA  1 
ATOM   6042 C  C   . ALA B 1 391 ? 59.298 114.465 -34.914  1.00 32.56  ? 393 ALA B C   1 
ATOM   6043 O  O   . ALA B 1 391 ? 59.898 113.493 -34.448  1.00 34.75  ? 393 ALA B O   1 
ATOM   6044 C  CB  . ALA B 1 391 ? 60.227 116.618 -33.950  1.00 30.89  ? 393 ALA B CB  1 
ATOM   6045 N  N   . MET B 1 392 ? 58.746 114.431 -36.121  1.00 31.99  ? 394 MET B N   1 
ATOM   6046 C  CA  . MET B 1 392 ? 59.198 113.556 -37.229  1.00 31.43  ? 394 MET B CA  1 
ATOM   6047 C  C   . MET B 1 392 ? 60.680 113.885 -37.507  1.00 31.09  ? 394 MET B C   1 
ATOM   6048 O  O   . MET B 1 392 ? 61.040 115.049 -37.391  1.00 29.82  ? 394 MET B O   1 
ATOM   6049 C  CB  . MET B 1 392 ? 58.309 113.879 -38.436  1.00 30.76  ? 394 MET B CB  1 
ATOM   6050 C  CG  . MET B 1 392 ? 58.765 113.297 -39.722  1.00 31.33  ? 394 MET B CG  1 
ATOM   6051 S  SD  . MET B 1 392 ? 57.938 114.063 -41.157  0.89 29.60  ? 394 MET B SD  1 
ATOM   6052 C  CE  . MET B 1 392 ? 59.206 115.233 -41.678  1.00 28.07  ? 394 MET B CE  1 
ATOM   6053 N  N   . LYS B 1 393 ? 61.530 112.898 -37.793  1.00 32.37  ? 395 LYS B N   1 
ATOM   6054 C  CA  . LYS B 1 393 ? 62.890 113.140 -38.361  1.00 34.29  ? 395 LYS B CA  1 
ATOM   6055 C  C   . LYS B 1 393 ? 62.737 113.609 -39.831  1.00 34.01  ? 395 LYS B C   1 
ATOM   6056 O  O   . LYS B 1 393 ? 61.912 113.022 -40.557  1.00 31.58  ? 395 LYS B O   1 
ATOM   6057 C  CB  . LYS B 1 393 ? 63.764 111.876 -38.342  1.00 36.79  ? 395 LYS B CB  1 
ATOM   6058 C  CG  . LYS B 1 393 ? 64.028 111.222 -36.988  1.00 40.33  ? 395 LYS B CG  1 
ATOM   6059 C  CD  . LYS B 1 393 ? 64.910 112.042 -36.040  1.00 41.90  ? 395 LYS B CD  1 
ATOM   6060 C  CE  . LYS B 1 393 ? 64.986 111.469 -34.630  1.00 43.59  ? 395 LYS B CE  1 
ATOM   6061 N  NZ  . LYS B 1 393 ? 65.186 112.547 -33.637  1.00 44.44  ? 395 LYS B NZ  1 
ATOM   6062 N  N   . ASP B 1 394 ? 63.571 114.570 -40.250  1.00 34.14  ? 396 ASP B N   1 
ATOM   6063 C  CA  . ASP B 1 394 ? 63.691 115.076 -41.644  1.00 35.45  ? 396 ASP B CA  1 
ATOM   6064 C  C   . ASP B 1 394 ? 63.722 113.872 -42.594  1.00 35.47  ? 396 ASP B C   1 
ATOM   6065 O  O   . ASP B 1 394 ? 64.244 112.801 -42.218  1.00 36.47  ? 396 ASP B O   1 
ATOM   6066 C  CB  . ASP B 1 394 ? 64.860 116.068 -41.781  1.00 36.45  ? 396 ASP B CB  1 
ATOM   6067 C  CG  . ASP B 1 394 ? 64.638 117.329 -40.933  1.00 36.81  ? 396 ASP B CG  1 
ATOM   6068 O  OD1 . ASP B 1 394 ? 63.650 117.357 -40.202  1.00 36.35  ? 396 ASP B OD1 1 
ATOM   6069 O  OD2 . ASP B 1 394 ? 65.406 118.308 -41.047  1.00 38.62  ? 396 ASP B OD2 1 
ATOM   6070 N  N   . ILE B 1 395 ? 63.069 114.012 -43.746  1.00 34.57  ? 397 ILE B N   1 
ATOM   6071 C  CA  . ILE B 1 395 ? 63.060 112.966 -44.804  1.00 35.37  ? 397 ILE B CA  1 
ATOM   6072 C  C   . ILE B 1 395 ? 63.737 113.530 -46.050  1.00 35.60  ? 397 ILE B C   1 
ATOM   6073 O  O   . ILE B 1 395 ? 63.200 114.467 -46.610  1.00 36.77  ? 397 ILE B O   1 
ATOM   6074 C  CB  . ILE B 1 395 ? 61.641 112.447 -45.077  1.00 33.41  ? 397 ILE B CB  1 
ATOM   6075 C  CG1 . ILE B 1 395 ? 61.033 111.846 -43.811  1.00 32.27  ? 397 ILE B CG1 1 
ATOM   6076 C  CG2 . ILE B 1 395 ? 61.682 111.459 -46.228  1.00 33.29  ? 397 ILE B CG2 1 
ATOM   6077 C  CD1 . ILE B 1 395 ? 59.552 111.690 -43.856  1.00 30.74  ? 397 ILE B CD1 1 
ATOM   6078 N  N   . GLU B 1 396 ? 64.943 113.049 -46.356  1.00 37.80  ? 398 GLU B N   1 
ATOM   6079 C  CA  . GLU B 1 396 ? 65.653 113.272 -47.638  1.00 38.96  ? 398 GLU B CA  1 
ATOM   6080 C  C   . GLU B 1 396 ? 65.067 112.206 -48.559  1.00 37.80  ? 398 GLU B C   1 
ATOM   6081 O  O   . GLU B 1 396 ? 65.054 111.028 -48.144  1.00 37.73  ? 398 GLU B O   1 
ATOM   6082 C  CB  . GLU B 1 396 ? 67.185 113.153 -47.512  1.00 42.91  ? 398 GLU B CB  1 
ATOM   6083 C  CG  . GLU B 1 396 ? 67.866 114.289 -46.736  1.00 45.67  ? 398 GLU B CG  1 
ATOM   6084 C  CD  . GLU B 1 396 ? 69.360 114.152 -46.370  1.00 50.25  ? 398 GLU B CD  1 
ATOM   6085 O  OE1 . GLU B 1 396 ? 69.698 113.399 -45.411  1.00 53.77  ? 398 GLU B OE1 1 
ATOM   6086 O  OE2 . GLU B 1 396 ? 70.211 114.844 -46.993  1.00 52.91  ? 398 GLU B OE2 1 
ATOM   6087 N  N   . PHE B 1 397 ? 64.525 112.609 -49.714  1.00 35.64  ? 399 PHE B N   1 
ATOM   6088 C  CA  . PHE B 1 397 ? 63.908 111.663 -50.673  1.00 34.98  ? 399 PHE B CA  1 
ATOM   6089 C  C   . PHE B 1 397 ? 64.186 112.134 -52.080  1.00 34.96  ? 399 PHE B C   1 
ATOM   6090 O  O   . PHE B 1 397 ? 64.551 113.305 -52.294  1.00 34.25  ? 399 PHE B O   1 
ATOM   6091 C  CB  . PHE B 1 397 ? 62.411 111.477 -50.434  1.00 34.05  ? 399 PHE B CB  1 
ATOM   6092 C  CG  . PHE B 1 397 ? 61.531 112.689 -50.652  1.00 32.58  ? 399 PHE B CG  1 
ATOM   6093 C  CD1 . PHE B 1 397 ? 61.571 113.776 -49.783  1.00 31.58  ? 399 PHE B CD1 1 
ATOM   6094 C  CD2 . PHE B 1 397 ? 60.626 112.724 -51.701  1.00 31.48  ? 399 PHE B CD2 1 
ATOM   6095 C  CE1 . PHE B 1 397 ? 60.740 114.868 -49.956  1.00 29.90  ? 399 PHE B CE1 1 
ATOM   6096 C  CE2 . PHE B 1 397 ? 59.814 113.833 -51.876  1.00 30.41  ? 399 PHE B CE2 1 
ATOM   6097 C  CZ  . PHE B 1 397 ? 59.875 114.902 -51.010  1.00 29.39  ? 399 PHE B CZ  1 
ATOM   6098 N  N   . THR B 1 398 ? 64.027 111.206 -53.012  1.00 36.58  ? 400 THR B N   1 
ATOM   6099 C  CA  . THR B 1 398 ? 64.291 111.458 -54.448  1.00 36.98  ? 400 THR B CA  1 
ATOM   6100 C  C   . THR B 1 398 ? 63.054 111.131 -55.282  1.00 35.87  ? 400 THR B C   1 
ATOM   6101 O  O   . THR B 1 398 ? 62.512 110.006 -55.139  1.00 36.12  ? 400 THR B O   1 
ATOM   6102 C  CB  . THR B 1 398 ? 65.524 110.678 -54.914  1.00 39.89  ? 400 THR B CB  1 
ATOM   6103 O  OG1 . THR B 1 398 ? 66.672 111.287 -54.315  1.00 41.59  ? 400 THR B OG1 1 
ATOM   6104 C  CG2 . THR B 1 398 ? 65.666 110.664 -56.420  1.00 39.55  ? 400 THR B CG2 1 
ATOM   6105 N  N   . ILE B 1 399 ? 62.659 112.081 -56.141  1.00 34.73  ? 401 ILE B N   1 
ATOM   6106 C  CA  . ILE B 1 399 ? 61.564 111.920 -57.139  1.00 32.60  ? 401 ILE B CA  1 
ATOM   6107 C  C   . ILE B 1 399 ? 62.220 111.685 -58.491  1.00 33.05  ? 401 ILE B C   1 
ATOM   6108 O  O   . ILE B 1 399 ? 63.107 112.455 -58.918  1.00 30.24  ? 401 ILE B O   1 
ATOM   6109 C  CB  . ILE B 1 399 ? 60.638 113.138 -57.194  1.00 31.91  ? 401 ILE B CB  1 
ATOM   6110 C  CG1 . ILE B 1 399 ? 59.914 113.386 -55.868  1.00 32.08  ? 401 ILE B CG1 1 
ATOM   6111 C  CG2 . ILE B 1 399 ? 59.673 112.982 -58.360  1.00 31.59  ? 401 ILE B CG2 1 
ATOM   6112 C  CD1 . ILE B 1 399 ? 59.122 114.686 -55.827  1.00 31.49  ? 401 ILE B CD1 1 
ATOM   6113 N  N   . SER B 1 400 ? 61.787 110.618 -59.124  1.00 33.97  ? 402 SER B N   1 
ATOM   6114 C  CA  . SER B 1 400 ? 62.320 110.214 -60.423  1.00 35.71  ? 402 SER B CA  1 
ATOM   6115 C  C   . SER B 1 400 ? 61.147 109.882 -61.346  1.00 35.40  ? 402 SER B C   1 
ATOM   6116 O  O   . SER B 1 400 ? 60.485 108.854 -61.147  1.00 36.62  ? 402 SER B O   1 
ATOM   6117 C  CB  . SER B 1 400 ? 63.307 109.104 -60.247  1.00 37.93  ? 402 SER B CB  1 
ATOM   6118 O  OG  . SER B 1 400 ? 63.928 108.796 -61.496  1.00 41.01  ? 402 SER B OG  1 
ATOM   6119 N  N   . GLY B 1 401 ? 60.880 110.774 -62.294  1.00 34.18  ? 403 GLY B N   1 
ATOM   6120 C  CA  . GLY B 1 401 ? 59.958 110.497 -63.405  1.00 34.76  ? 403 GLY B CA  1 
ATOM   6121 C  C   . GLY B 1 401 ? 60.715 109.841 -64.531  1.00 36.26  ? 403 GLY B C   1 
ATOM   6122 O  O   . GLY B 1 401 ? 61.750 110.369 -64.920  1.00 36.72  ? 403 GLY B O   1 
ATOM   6123 N  N   . THR B 1 402 ? 60.241 108.707 -65.024  1.00 38.38  ? 404 THR B N   1 
ATOM   6124 C  CA  . THR B 1 402 ? 60.779 108.065 -66.244  1.00 39.00  ? 404 THR B CA  1 
ATOM   6125 C  C   . THR B 1 402 ? 60.072 108.669 -67.465  1.00 39.38  ? 404 THR B C   1 
ATOM   6126 O  O   . THR B 1 402 ? 58.853 108.454 -67.639  1.00 38.04  ? 404 THR B O   1 
ATOM   6127 C  CB  . THR B 1 402 ? 60.611 106.545 -66.170  1.00 40.53  ? 404 THR B CB  1 
ATOM   6128 O  OG1 . THR B 1 402 ? 61.267 106.110 -64.990  1.00 41.34  ? 404 THR B OG1 1 
ATOM   6129 C  CG2 . THR B 1 402 ? 61.177 105.809 -67.366  1.00 42.18  ? 404 THR B CG2 1 
ATOM   6130 N  N   . ILE B 1 403 ? 60.827 109.346 -68.324  1.00 39.98  ? 405 ILE B N   1 
ATOM   6131 C  CA  . ILE B 1 403 ? 60.287 109.980 -69.561  1.00 40.70  ? 405 ILE B CA  1 
ATOM   6132 C  C   . ILE B 1 403 ? 61.076 109.425 -70.748  1.00 42.99  ? 405 ILE B C   1 
ATOM   6133 O  O   . ILE B 1 403 ? 62.206 109.869 -70.967  1.00 41.55  ? 405 ILE B O   1 
ATOM   6134 C  CB  . ILE B 1 403 ? 60.357 111.525 -69.485  1.00 39.07  ? 405 ILE B CB  1 
ATOM   6135 C  CG1 . ILE B 1 403 ? 59.665 112.063 -68.229  1.00 37.94  ? 405 ILE B CG1 1 
ATOM   6136 C  CG2 . ILE B 1 403 ? 59.823 112.155 -70.770  1.00 38.40  ? 405 ILE B CG2 1 
ATOM   6137 C  CD1 . ILE B 1 403 ? 59.919 113.522 -67.975  1.00 36.63  ? 405 ILE B CD1 1 
ATOM   6138 N  N   . ASP B 1 404 ? 60.484 108.504 -71.500  1.00 46.87  ? 406 ASP B N   1 
ATOM   6139 C  CA  . ASP B 1 404 ? 61.140 107.837 -72.654  1.00 50.54  ? 406 ASP B CA  1 
ATOM   6140 C  C   . ASP B 1 404 ? 61.265 108.821 -73.853  1.00 50.84  ? 406 ASP B C   1 
ATOM   6141 O  O   . ASP B 1 404 ? 60.879 110.014 -73.763  1.00 46.46  ? 406 ASP B O   1 
ATOM   6142 C  CB  . ASP B 1 404 ? 60.445 106.492 -72.917  1.00 53.15  ? 406 ASP B CB  1 
ATOM   6143 C  CG  . ASP B 1 404 ? 59.092 106.541 -73.609  1.00 54.10  ? 406 ASP B CG  1 
ATOM   6144 O  OD1 . ASP B 1 404 ? 58.656 107.633 -74.072  1.00 52.04  ? 406 ASP B OD1 1 
ATOM   6145 O  OD2 . ASP B 1 404 ? 58.467 105.473 -73.673  1.00 58.32  ? 406 ASP B OD2 1 
ATOM   6146 N  N   . SER B 1 405 ? 61.867 108.368 -74.950  1.00 54.50  ? 407 SER B N   1 
ATOM   6147 C  CA  . SER B 1 405 ? 62.225 109.237 -76.104  1.00 54.61  ? 407 SER B CA  1 
ATOM   6148 C  C   . SER B 1 405 ? 60.945 109.688 -76.823  1.00 53.12  ? 407 SER B C   1 
ATOM   6149 O  O   . SER B 1 405 ? 60.964 110.845 -77.295  1.00 49.89  ? 407 SER B O   1 
ATOM   6150 C  CB  . SER B 1 405 ? 63.183 108.542 -77.022  1.00 58.10  ? 407 SER B CB  1 
ATOM   6151 O  OG  . SER B 1 405 ? 62.640 107.296 -77.433  1.00 62.15  ? 407 SER B OG  1 
ATOM   6152 N  N   . THR B 1 406 ? 59.906 108.823 -76.876  1.00 53.24  ? 408 THR B N   1 
ATOM   6153 C  CA  . THR B 1 406 ? 58.504 109.159 -77.273  1.00 53.48  ? 408 THR B CA  1 
ATOM   6154 C  C   . THR B 1 406 ? 58.064 110.454 -76.573  1.00 51.46  ? 408 THR B C   1 
ATOM   6155 O  O   . THR B 1 406 ? 57.395 111.268 -77.209  1.00 51.33  ? 408 THR B O   1 
ATOM   6156 C  CB  . THR B 1 406 ? 57.470 108.089 -76.868  1.00 55.59  ? 408 THR B CB  1 
ATOM   6157 O  OG1 . THR B 1 406 ? 57.983 106.801 -77.187  1.00 57.53  ? 408 THR B OG1 1 
ATOM   6158 C  CG2 . THR B 1 406 ? 56.120 108.279 -77.533  1.00 55.15  ? 408 THR B CG2 1 
ATOM   6159 N  N   . GLY B 1 407 ? 58.391 110.595 -75.285  1.00 50.33  ? 409 GLY B N   1 
ATOM   6160 C  CA  . GLY B 1 407 ? 57.944 111.685 -74.394  1.00 46.50  ? 409 GLY B CA  1 
ATOM   6161 C  C   . GLY B 1 407 ? 56.779 111.250 -73.511  1.00 43.82  ? 409 GLY B C   1 
ATOM   6162 O  O   . GLY B 1 407 ? 56.122 112.150 -72.990  1.00 40.50  ? 409 GLY B O   1 
ATOM   6163 N  N   . ASP B 1 408 ? 56.512 109.936 -73.388  1.00 44.63  ? 410 ASP B N   1 
ATOM   6164 C  CA  . ASP B 1 408 ? 55.551 109.350 -72.413  1.00 46.25  ? 410 ASP B CA  1 
ATOM   6165 C  C   . ASP B 1 408 ? 56.172 109.406 -71.013  1.00 43.07  ? 410 ASP B C   1 
ATOM   6166 O  O   . ASP B 1 408 ? 57.353 109.001 -70.834  1.00 43.55  ? 410 ASP B O   1 
ATOM   6167 C  CB  . ASP B 1 408 ? 55.170 107.905 -72.732  1.00 50.39  ? 410 ASP B CB  1 
ATOM   6168 C  CG  . ASP B 1 408 ? 54.463 107.750 -74.071  1.00 58.30  ? 410 ASP B CG  1 
ATOM   6169 O  OD1 . ASP B 1 408 ? 53.970 108.792 -74.636  1.00 58.16  ? 410 ASP B OD1 1 
ATOM   6170 O  OD2 . ASP B 1 408 ? 54.422 106.592 -74.560  1.00 67.32  ? 410 ASP B OD2 1 
ATOM   6171 N  N   . LEU B 1 409 ? 55.421 109.890 -70.037  1.00 39.01  ? 411 LEU B N   1 
ATOM   6172 C  CA  . LEU B 1 409 ? 55.768 109.606 -68.631  1.00 36.85  ? 411 LEU B CA  1 
ATOM   6173 C  C   . LEU B 1 409 ? 55.338 108.169 -68.360  1.00 36.75  ? 411 LEU B C   1 
ATOM   6174 O  O   . LEU B 1 409 ? 54.155 107.908 -68.425  1.00 35.93  ? 411 LEU B O   1 
ATOM   6175 C  CB  . LEU B 1 409 ? 55.030 110.603 -67.745  1.00 36.09  ? 411 LEU B CB  1 
ATOM   6176 C  CG  . LEU B 1 409 ? 55.265 110.452 -66.244  1.00 34.17  ? 411 LEU B CG  1 
ATOM   6177 C  CD1 . LEU B 1 409 ? 56.587 111.045 -65.808  1.00 33.66  ? 411 LEU B CD1 1 
ATOM   6178 C  CD2 . LEU B 1 409 ? 54.140 111.123 -65.502  1.00 34.07  ? 411 LEU B CD2 1 
ATOM   6179 N  N   . THR B 1 410 ? 56.276 107.259 -68.152  1.00 38.43  ? 412 THR B N   1 
ATOM   6180 C  CA  . THR B 1 410 ? 56.001 105.792 -68.078  1.00 41.44  ? 412 THR B CA  1 
ATOM   6181 C  C   . THR B 1 410 ? 56.074 105.317 -66.623  1.00 42.04  ? 412 THR B C   1 
ATOM   6182 O  O   . THR B 1 410 ? 55.558 104.240 -66.336  1.00 42.82  ? 412 THR B O   1 
ATOM   6183 C  CB  . THR B 1 410 ? 57.011 104.990 -68.906  1.00 42.90  ? 412 THR B CB  1 
ATOM   6184 O  OG1 . THR B 1 410 ? 58.301 105.278 -68.350  1.00 43.83  ? 412 THR B OG1 1 
ATOM   6185 C  CG2 . THR B 1 410 ? 56.982 105.352 -70.373  1.00 42.11  ? 412 THR B CG2 1 
ATOM   6186 N  N   . ASN B 1 411 ? 56.749 106.069 -65.760  1.00 42.63  ? 413 ASN B N   1 
ATOM   6187 C  CA  . ASN B 1 411 ? 57.068 105.639 -64.375  1.00 43.91  ? 413 ASN B CA  1 
ATOM   6188 C  C   . ASN B 1 411 ? 57.266 106.863 -63.480  1.00 40.59  ? 413 ASN B C   1 
ATOM   6189 O  O   . ASN B 1 411 ? 57.767 107.916 -63.954  1.00 39.16  ? 413 ASN B O   1 
ATOM   6190 C  CB  . ASN B 1 411 ? 58.307 104.743 -64.345  1.00 48.31  ? 413 ASN B CB  1 
ATOM   6191 C  CG  . ASN B 1 411 ? 58.099 103.536 -63.460  1.00 53.61  ? 413 ASN B CG  1 
ATOM   6192 O  OD1 . ASN B 1 411 ? 57.544 102.533 -63.918  1.00 61.85  ? 413 ASN B OD1 1 
ATOM   6193 N  ND2 . ASN B 1 411 ? 58.539 103.617 -62.214  1.00 51.82  ? 413 ASN B ND2 1 
ATOM   6194 N  N   . LEU B 1 412 ? 56.877 106.719 -62.219  1.00 38.63  ? 414 LEU B N   1 
ATOM   6195 C  CA  . LEU B 1 412 ? 57.091 107.749 -61.184  1.00 36.06  ? 414 LEU B CA  1 
ATOM   6196 C  C   . LEU B 1 412 ? 57.417 107.039 -59.874  1.00 36.09  ? 414 LEU B C   1 
ATOM   6197 O  O   . LEU B 1 412 ? 56.624 106.188 -59.423  1.00 34.35  ? 414 LEU B O   1 
ATOM   6198 C  CB  . LEU B 1 412 ? 55.849 108.625 -61.035  1.00 33.97  ? 414 LEU B CB  1 
ATOM   6199 C  CG  . LEU B 1 412 ? 55.958 109.748 -60.001  1.00 31.70  ? 414 LEU B CG  1 
ATOM   6200 C  CD1 . LEU B 1 412 ? 57.037 110.772 -60.332  1.00 30.90  ? 414 LEU B CD1 1 
ATOM   6201 C  CD2 . LEU B 1 412 ? 54.627 110.454 -59.883  1.00 30.75  ? 414 LEU B CD2 1 
ATOM   6202 N  N   . THR B 1 413 ? 58.577 107.363 -59.322  1.00 36.76  ? 415 THR B N   1 
ATOM   6203 C  CA  . THR B 1 413 ? 59.069 106.757 -58.060  1.00 38.62  ? 415 THR B CA  1 
ATOM   6204 C  C   . THR B 1 413 ? 59.552 107.844 -57.111  1.00 36.79  ? 415 THR B C   1 
ATOM   6205 O  O   . THR B 1 413 ? 60.151 108.874 -57.548  1.00 34.21  ? 415 THR B O   1 
ATOM   6206 C  CB  . THR B 1 413 ? 60.212 105.770 -58.305  1.00 41.18  ? 415 THR B CB  1 
ATOM   6207 O  OG1 . THR B 1 413 ? 61.310 106.620 -58.648  1.00 41.35  ? 415 THR B OG1 1 
ATOM   6208 C  CG2 . THR B 1 413 ? 59.880 104.740 -59.367  1.00 42.04  ? 415 THR B CG2 1 
ATOM   6209 N  N   . ALA B 1 414 ? 59.308 107.589 -55.838  1.00 37.44  ? 416 ALA B N   1 
ATOM   6210 C  CA  . ALA B 1 414 ? 59.843 108.397 -54.730  1.00 37.47  ? 416 ALA B CA  1 
ATOM   6211 C  C   . ALA B 1 414 ? 60.523 107.433 -53.772  1.00 38.76  ? 416 ALA B C   1 
ATOM   6212 O  O   . ALA B 1 414 ? 59.900 106.427 -53.393  1.00 39.89  ? 416 ALA B O   1 
ATOM   6213 C  CB  . ALA B 1 414 ? 58.721 109.155 -54.087  1.00 36.05  ? 416 ALA B CB  1 
ATOM   6214 N  N   . THR B 1 415 ? 61.778 107.676 -53.432  1.00 39.29  ? 417 THR B N   1 
ATOM   6215 C  CA  . THR B 1 415 ? 62.505 106.766 -52.519  1.00 39.77  ? 417 THR B CA  1 
ATOM   6216 C  C   . THR B 1 415 ? 63.142 107.609 -51.426  1.00 38.09  ? 417 THR B C   1 
ATOM   6217 O  O   . THR B 1 415 ? 63.480 108.795 -51.660  1.00 34.54  ? 417 THR B O   1 
ATOM   6218 C  CB  . THR B 1 415 ? 63.474 105.849 -53.275  1.00 42.86  ? 417 THR B CB  1 
ATOM   6219 O  OG1 . THR B 1 415 ? 64.331 106.730 -54.002  1.00 44.84  ? 417 THR B OG1 1 
ATOM   6220 C  CG2 . THR B 1 415 ? 62.790 104.872 -54.219  1.00 43.21  ? 417 THR B CG2 1 
ATOM   6221 N  N   . SER B 1 416 ? 63.210 107.007 -50.249  1.00 38.17  ? 418 SER B N   1 
ATOM   6222 C  CA  . SER B 1 416 ? 63.956 107.543 -49.086  1.00 39.65  ? 418 SER B CA  1 
ATOM   6223 C  C   . SER B 1 416 ? 64.544 106.364 -48.327  1.00 41.24  ? 418 SER B C   1 
ATOM   6224 O  O   . SER B 1 416 ? 63.847 105.333 -48.278  1.00 42.50  ? 418 SER B O   1 
ATOM   6225 C  CB  . SER B 1 416 ? 63.073 108.349 -48.211  1.00 37.92  ? 418 SER B CB  1 
ATOM   6226 O  OG  . SER B 1 416 ? 63.828 108.928 -47.166  1.00 39.06  ? 418 SER B OG  1 
ATOM   6227 N  N   . ALA B 1 417 ? 65.772 106.505 -47.816  1.00 43.27  ? 419 ALA B N   1 
ATOM   6228 C  CA  . ALA B 1 417 ? 66.345 105.647 -46.743  1.00 47.12  ? 419 ALA B CA  1 
ATOM   6229 C  C   . ALA B 1 417 ? 65.346 105.557 -45.577  1.00 47.53  ? 419 ALA B C   1 
ATOM   6230 O  O   . ALA B 1 417 ? 65.063 104.432 -45.142  1.00 49.21  ? 419 ALA B O   1 
ATOM   6231 C  CB  . ALA B 1 417 ? 67.684 106.194 -46.284  1.00 47.49  ? 419 ALA B CB  1 
ATOM   6232 N  N   . THR B 1 418 ? 64.758 106.694 -45.195  1.00 47.88  ? 420 THR B N   1 
ATOM   6233 C  CA  . THR B 1 418 ? 64.095 106.950 -43.886  1.00 48.16  ? 420 THR B CA  1 
ATOM   6234 C  C   . THR B 1 418 ? 62.566 106.828 -43.960  1.00 45.90  ? 420 THR B C   1 
ATOM   6235 O  O   . THR B 1 418 ? 61.937 107.149 -42.969  1.00 45.15  ? 420 THR B O   1 
ATOM   6236 C  CB  . THR B 1 418 ? 64.392 108.380 -43.394  1.00 49.47  ? 420 THR B CB  1 
ATOM   6237 O  OG1 . THR B 1 418 ? 64.039 109.341 -44.403  1.00 51.06  ? 420 THR B OG1 1 
ATOM   6238 C  CG2 . THR B 1 418 ? 65.845 108.582 -43.033  1.00 52.06  ? 420 THR B CG2 1 
ATOM   6239 N  N   . ALA B 1 419 ? 61.950 106.531 -45.099  1.00 46.29  ? 421 ALA B N   1 
ATOM   6240 C  CA  . ALA B 1 419 ? 60.481 106.718 -45.282  1.00 43.79  ? 421 ALA B CA  1 
ATOM   6241 C  C   . ALA B 1 419 ? 59.965 105.931 -46.483  1.00 44.22  ? 421 ALA B C   1 
ATOM   6242 O  O   . ALA B 1 419 ? 60.791 105.367 -47.245  1.00 46.33  ? 421 ALA B O   1 
ATOM   6243 C  CB  . ALA B 1 419 ? 60.148 108.184 -45.452  1.00 41.77  ? 421 ALA B CB  1 
ATOM   6244 N  N   . SER B 1 420 ? 58.650 105.949 -46.668  1.00 41.70  ? 422 SER B N   1 
ATOM   6245 C  CA  . SER B 1 420 ? 57.964 105.104 -47.659  1.00 41.71  ? 422 SER B CA  1 
ATOM   6246 C  C   . SER B 1 420 ? 56.832 105.888 -48.348  1.00 39.65  ? 422 SER B C   1 
ATOM   6247 O  O   . SER B 1 420 ? 55.999 106.446 -47.669  1.00 40.60  ? 422 SER B O   1 
ATOM   6248 C  CB  . SER B 1 420 ? 57.497 103.878 -46.981  1.00 42.53  ? 422 SER B CB  1 
ATOM   6249 O  OG  . SER B 1 420 ? 56.944 103.030 -47.956  1.00 45.74  ? 422 SER B OG  1 
ATOM   6250 N  N   . PHE B 1 421 ? 56.795 105.919 -49.672  1.00 39.07  ? 423 PHE B N   1 
ATOM   6251 C  CA  . PHE B 1 421 ? 55.821 106.710 -50.476  1.00 35.90  ? 423 PHE B CA  1 
ATOM   6252 C  C   . PHE B 1 421 ? 54.966 105.799 -51.328  1.00 36.70  ? 423 PHE B C   1 
ATOM   6253 O  O   . PHE B 1 421 ? 55.454 104.801 -51.735  1.00 39.54  ? 423 PHE B O   1 
ATOM   6254 C  CB  . PHE B 1 421 ? 56.520 107.653 -51.444  1.00 32.73  ? 423 PHE B CB  1 
ATOM   6255 C  CG  . PHE B 1 421 ? 57.429 108.624 -50.761  1.00 30.81  ? 423 PHE B CG  1 
ATOM   6256 C  CD1 . PHE B 1 421 ? 58.703 108.260 -50.415  1.00 31.88  ? 423 PHE B CD1 1 
ATOM   6257 C  CD2 . PHE B 1 421 ? 56.995 109.890 -50.455  1.00 29.59  ? 423 PHE B CD2 1 
ATOM   6258 C  CE1 . PHE B 1 421 ? 59.530 109.161 -49.768  1.00 32.61  ? 423 PHE B CE1 1 
ATOM   6259 C  CE2 . PHE B 1 421 ? 57.811 110.790 -49.793  1.00 29.56  ? 423 PHE B CE2 1 
ATOM   6260 C  CZ  . PHE B 1 421 ? 59.084 110.427 -49.466  1.00 31.20  ? 423 PHE B CZ  1 
ATOM   6261 N  N   . GLU B 1 422 ? 53.736 106.186 -51.585  1.00 37.81  ? 424 GLU B N   1 
ATOM   6262 C  CA  . GLU B 1 422 ? 52.938 105.676 -52.715  1.00 39.90  ? 424 GLU B CA  1 
ATOM   6263 C  C   . GLU B 1 422 ? 53.149 106.639 -53.885  1.00 37.31  ? 424 GLU B C   1 
ATOM   6264 O  O   . GLU B 1 422 ? 53.410 107.828 -53.663  1.00 34.67  ? 424 GLU B O   1 
ATOM   6265 C  CB  . GLU B 1 422 ? 51.463 105.553 -52.322  1.00 43.99  ? 424 GLU B CB  1 
ATOM   6266 C  CG  . GLU B 1 422 ? 51.157 104.377 -51.404  1.00 50.61  ? 424 GLU B CG  1 
ATOM   6267 C  CD  . GLU B 1 422 ? 51.486 102.984 -51.958  1.00 57.58  ? 424 GLU B CD  1 
ATOM   6268 O  OE1 . GLU B 1 422 ? 51.739 102.863 -53.193  1.00 63.19  ? 424 GLU B OE1 1 
ATOM   6269 O  OE2 . GLU B 1 422 ? 51.508 101.998 -51.158  1.00 60.63  ? 424 GLU B OE2 1 
ATOM   6270 N  N   . THR B 1 423 ? 53.065 106.131 -55.104  1.00 38.00  ? 425 THR B N   1 
ATOM   6271 C  CA  . THR B 1 423 ? 53.092 106.954 -56.331  1.00 35.84  ? 425 THR B CA  1 
ATOM   6272 C  C   . THR B 1 423 ? 52.092 106.393 -57.327  1.00 37.47  ? 425 THR B C   1 
ATOM   6273 O  O   . THR B 1 423 ? 51.956 105.169 -57.412  1.00 40.35  ? 425 THR B O   1 
ATOM   6274 C  CB  . THR B 1 423 ? 54.489 106.978 -56.945  1.00 36.20  ? 425 THR B CB  1 
ATOM   6275 O  OG1 . THR B 1 423 ? 54.800 105.629 -57.248  1.00 36.52  ? 425 THR B OG1 1 
ATOM   6276 C  CG2 . THR B 1 423 ? 55.550 107.503 -56.011  1.00 36.75  ? 425 THR B CG2 1 
ATOM   6277 N  N   . ASP B 1 424 ? 51.435 107.275 -58.066  1.00 37.05  ? 426 ASP B N   1 
ATOM   6278 C  CA  . ASP B 1 424 ? 50.558 106.909 -59.206  1.00 37.67  ? 426 ASP B CA  1 
ATOM   6279 C  C   . ASP B 1 424 ? 50.924 107.815 -60.375  1.00 34.34  ? 426 ASP B C   1 
ATOM   6280 O  O   . ASP B 1 424 ? 50.750 109.031 -60.286  1.00 32.98  ? 426 ASP B O   1 
ATOM   6281 C  CB  . ASP B 1 424 ? 49.072 107.041 -58.883  1.00 39.43  ? 426 ASP B CB  1 
ATOM   6282 C  CG  . ASP B 1 424 ? 48.173 106.661 -60.049  1.00 42.80  ? 426 ASP B CG  1 
ATOM   6283 O  OD1 . ASP B 1 424 ? 48.667 106.573 -61.204  1.00 46.11  ? 426 ASP B OD1 1 
ATOM   6284 O  OD2 . ASP B 1 424 ? 46.985 106.445 -59.810  1.00 48.30  ? 426 ASP B OD2 1 
ATOM   6285 N  N   . VAL B 1 425 ? 51.444 107.227 -61.432  1.00 34.92  ? 427 VAL B N   1 
ATOM   6286 C  CA  . VAL B 1 425 ? 52.027 107.987 -62.580  1.00 31.92  ? 427 VAL B CA  1 
ATOM   6287 C  C   . VAL B 1 425 ? 50.886 108.757 -63.259  1.00 30.94  ? 427 VAL B C   1 
ATOM   6288 O  O   . VAL B 1 425 ? 51.091 109.912 -63.712  1.00 30.18  ? 427 VAL B O   1 
ATOM   6289 C  CB  . VAL B 1 425 ? 52.820 107.063 -63.518  1.00 32.41  ? 427 VAL B CB  1 
ATOM   6290 C  CG1 . VAL B 1 425 ? 51.997 105.926 -64.096  1.00 34.07  ? 427 VAL B CG1 1 
ATOM   6291 C  CG2 . VAL B 1 425 ? 53.446 107.862 -64.626  1.00 31.52  ? 427 VAL B CG2 1 
ATOM   6292 N  N   . ASN B 1 426 ? 49.697 108.170 -63.296  1.00 30.80  ? 428 ASN B N   1 
ATOM   6293 C  CA  . ASN B 1 426 ? 48.543 108.758 -64.015  1.00 29.39  ? 428 ASN B CA  1 
ATOM   6294 C  C   . ASN B 1 426 ? 48.017 110.005 -63.318  1.00 28.38  ? 428 ASN B C   1 
ATOM   6295 O  O   . ASN B 1 426 ? 47.553 110.865 -64.017  1.00 29.47  ? 428 ASN B O   1 
ATOM   6296 C  CB  . ASN B 1 426 ? 47.461 107.717 -64.133  1.00 31.30  ? 428 ASN B CB  1 
ATOM   6297 C  CG  . ASN B 1 426 ? 48.017 106.528 -64.884  1.00 34.14  ? 428 ASN B CG  1 
ATOM   6298 O  OD1 . ASN B 1 426 ? 48.022 105.424 -64.359  1.00 36.69  ? 428 ASN B OD1 1 
ATOM   6299 N  ND2 . ASN B 1 426 ? 48.539 106.749 -66.084  1.00 33.77  ? 428 ASN B ND2 1 
ATOM   6300 N  N   . THR B 1 427 ? 48.057 110.098 -61.982  1.00 26.28  ? 429 THR B N   1 
ATOM   6301 C  CA  . THR B 1 427 ? 47.643 111.324 -61.279  1.00 24.62  ? 429 THR B CA  1 
ATOM   6302 C  C   . THR B 1 427 ? 48.880 112.192 -61.033  1.00 23.07  ? 429 THR B C   1 
ATOM   6303 O  O   . THR B 1 427 ? 48.723 113.358 -60.699  1.00 22.01  ? 429 THR B O   1 
ATOM   6304 C  CB  . THR B 1 427 ? 46.868 110.961 -60.007  1.00 25.11  ? 429 THR B CB  1 
ATOM   6305 O  OG1 . THR B 1 427 ? 47.705 110.130 -59.218  1.00 25.01  ? 429 THR B OG1 1 
ATOM   6306 C  CG2 . THR B 1 427 ? 45.597 110.189 -60.269  1.00 26.40  ? 429 THR B CG2 1 
ATOM   6307 N  N   . GLY B 1 428 ? 50.081 111.638 -61.115  1.00 22.83  ? 430 GLY B N   1 
ATOM   6308 C  CA  . GLY B 1 428 ? 51.318 112.367 -60.741  1.00 21.95  ? 430 GLY B CA  1 
ATOM   6309 C  C   . GLY B 1 428 ? 51.435 112.611 -59.236  1.00 21.97  ? 430 GLY B C   1 
ATOM   6310 O  O   . GLY B 1 428 ? 52.241 113.474 -58.803  1.00 20.32  ? 430 GLY B O   1 
ATOM   6311 N  N   . ILE B 1 429 ? 50.641 111.904 -58.446  1.00 22.08  ? 431 ILE B N   1 
ATOM   6312 C  CA  . ILE B 1 429 ? 50.615 112.098 -56.966  1.00 22.29  ? 431 ILE B CA  1 
ATOM   6313 C  C   . ILE B 1 429 ? 51.563 111.113 -56.326  1.00 22.71  ? 431 ILE B C   1 
ATOM   6314 O  O   . ILE B 1 429 ? 51.485 109.928 -56.619  1.00 24.08  ? 431 ILE B O   1 
ATOM   6315 C  CB  . ILE B 1 429 ? 49.206 111.965 -56.409  1.00 21.92  ? 431 ILE B CB  1 
ATOM   6316 C  CG1 . ILE B 1 429 ? 48.310 112.972 -57.125  1.00 21.34  ? 431 ILE B CG1 1 
ATOM   6317 C  CG2 . ILE B 1 429 ? 49.251 112.147 -54.893  1.00 22.11  ? 431 ILE B CG2 1 
ATOM   6318 C  CD1 . ILE B 1 429 ? 46.902 112.834 -56.769  1.00 21.85  ? 431 ILE B CD1 1 
ATOM   6319 N  N   . ILE B 1 430 ? 52.480 111.658 -55.558  1.00 23.01  ? 432 ILE B N   1 
ATOM   6320 C  CA  . ILE B 1 430 ? 53.313 110.917 -54.560  1.00 24.15  ? 432 ILE B CA  1 
ATOM   6321 C  C   . ILE B 1 430 ? 52.686 111.098 -53.177  1.00 23.81  ? 432 ILE B C   1 
ATOM   6322 O  O   . ILE B 1 430 ? 52.624 112.246 -52.743  1.00 23.91  ? 432 ILE B O   1 
ATOM   6323 C  CB  . ILE B 1 430 ? 54.735 111.482 -54.647  1.00 24.02  ? 432 ILE B CB  1 
ATOM   6324 C  CG1 . ILE B 1 430 ? 55.284 111.325 -56.061  1.00 23.82  ? 432 ILE B CG1 1 
ATOM   6325 C  CG2 . ILE B 1 430 ? 55.641 110.867 -53.625  1.00 25.15  ? 432 ILE B CG2 1 
ATOM   6326 C  CD1 . ILE B 1 430 ? 56.307 112.354 -56.382  1.00 23.40  ? 432 ILE B CD1 1 
ATOM   6327 N  N   . THR B 1 431 ? 52.216 110.025 -52.531  1.00 24.64  ? 433 THR B N   1 
ATOM   6328 C  CA  . THR B 1 431 ? 51.628 110.102 -51.171  1.00 24.45  ? 433 THR B CA  1 
ATOM   6329 C  C   . THR B 1 431 ? 52.640 109.706 -50.104  1.00 24.52  ? 433 THR B C   1 
ATOM   6330 O  O   . THR B 1 431 ? 53.251 108.692 -50.247  1.00 24.91  ? 433 THR B O   1 
ATOM   6331 C  CB  . THR B 1 431 ? 50.380 109.244 -50.965  1.00 25.49  ? 433 THR B CB  1 
ATOM   6332 O  OG1 . THR B 1 431 ? 49.343 109.593 -51.882  1.00 26.37  ? 433 THR B OG1 1 
ATOM   6333 C  CG2 . THR B 1 431 ? 49.779 109.484 -49.600  1.00 25.74  ? 433 THR B CG2 1 
ATOM   6334 N  N   . LEU B 1 432 ? 52.765 110.517 -49.059  1.00 24.25  ? 434 LEU B N   1 
ATOM   6335 C  CA  . LEU B 1 432 ? 53.517 110.213 -47.828  1.00 25.30  ? 434 LEU B CA  1 
ATOM   6336 C  C   . LEU B 1 432 ? 52.583 110.358 -46.627  1.00 25.96  ? 434 LEU B C   1 
ATOM   6337 O  O   . LEU B 1 432 ? 52.082 111.465 -46.392  1.00 23.38  ? 434 LEU B O   1 
ATOM   6338 C  CB  . LEU B 1 432 ? 54.692 111.172 -47.673  1.00 24.82  ? 434 LEU B CB  1 
ATOM   6339 C  CG  . LEU B 1 432 ? 55.506 110.925 -46.402  1.00 25.56  ? 434 LEU B CG  1 
ATOM   6340 C  CD1 . LEU B 1 432 ? 56.014 109.493 -46.403  1.00 26.35  ? 434 LEU B CD1 1 
ATOM   6341 C  CD2 . LEU B 1 432 ? 56.655 111.929 -46.259  1.00 25.34  ? 434 LEU B CD2 1 
ATOM   6342 N  N   . LYS B 1 433 ? 52.386 109.264 -45.895  1.00 29.10  ? 435 LYS B N   1 
ATOM   6343 C  CA  . LYS B 1 433 ? 51.593 109.242 -44.652  1.00 30.99  ? 435 LYS B CA  1 
ATOM   6344 C  C   . LYS B 1 433 ? 52.548 109.356 -43.476  1.00 30.04  ? 435 LYS B C   1 
ATOM   6345 O  O   . LYS B 1 433 ? 53.350 108.475 -43.342  1.00 31.92  ? 435 LYS B O   1 
ATOM   6346 C  CB  . LYS B 1 433 ? 50.829 107.939 -44.503  1.00 34.18  ? 435 LYS B CB  1 
ATOM   6347 C  CG  . LYS B 1 433 ? 50.115 107.837 -43.174  1.00 36.63  ? 435 LYS B CG  1 
ATOM   6348 C  CD  . LYS B 1 433 ? 49.302 106.589 -43.076  1.00 40.15  ? 435 LYS B CD  1 
ATOM   6349 C  CE  . LYS B 1 433 ? 50.219 105.404 -42.893  1.00 43.88  ? 435 LYS B CE  1 
ATOM   6350 N  NZ  . LYS B 1 433 ? 49.457 104.187 -42.530  1.00 47.39  ? 435 LYS B NZ  1 
ATOM   6351 N  N   . VAL B 1 434 ? 52.488 110.435 -42.714  1.00 28.09  ? 436 VAL B N   1 
ATOM   6352 C  CA  . VAL B 1 434 ? 53.410 110.684 -41.575  1.00 27.74  ? 436 VAL B CA  1 
ATOM   6353 C  C   . VAL B 1 434 ? 52.667 110.324 -40.284  1.00 28.43  ? 436 VAL B C   1 
ATOM   6354 O  O   . VAL B 1 434 ? 51.625 110.974 -39.961  1.00 26.47  ? 436 VAL B O   1 
ATOM   6355 C  CB  . VAL B 1 434 ? 53.883 112.142 -41.550  1.00 26.71  ? 436 VAL B CB  1 
ATOM   6356 C  CG1 . VAL B 1 434 ? 54.637 112.428 -40.269  1.00 27.59  ? 436 VAL B CG1 1 
ATOM   6357 C  CG2 . VAL B 1 434 ? 54.693 112.500 -42.783  1.00 26.15  ? 436 VAL B CG2 1 
ATOM   6358 N  N   . VAL B 1 435 ? 53.135 109.287 -39.594  1.00 29.87  ? 437 VAL B N   1 
ATOM   6359 C  CA  . VAL B 1 435 ? 52.452 108.779 -38.375  1.00 30.30  ? 437 VAL B CA  1 
ATOM   6360 C  C   . VAL B 1 435 ? 53.078 109.464 -37.150  1.00 29.85  ? 437 VAL B C   1 
ATOM   6361 O  O   . VAL B 1 435 ? 54.281 109.378 -36.967  1.00 29.38  ? 437 VAL B O   1 
ATOM   6362 C  CB  . VAL B 1 435 ? 52.486 107.245 -38.316  1.00 31.35  ? 437 VAL B CB  1 
ATOM   6363 C  CG1 . VAL B 1 435 ? 51.707 106.765 -37.105  1.00 32.08  ? 437 VAL B CG1 1 
ATOM   6364 C  CG2 . VAL B 1 435 ? 51.939 106.632 -39.597  1.00 31.28  ? 437 VAL B CG2 1 
ATOM   6365 N  N   . ASN B 1 436 ? 52.302 110.247 -36.415  1.00 29.78  ? 438 ASN B N   1 
ATOM   6366 C  CA  . ASN B 1 436 ? 52.821 110.998 -35.241  1.00 31.23  ? 438 ASN B CA  1 
ATOM   6367 C  C   . ASN B 1 436 ? 52.709 110.103 -33.991  1.00 33.04  ? 438 ASN B C   1 
ATOM   6368 O  O   . ASN B 1 436 ? 51.650 109.499 -33.756  1.00 34.52  ? 438 ASN B O   1 
ATOM   6369 C  CB  . ASN B 1 436 ? 52.183 112.391 -35.101  1.00 30.00  ? 438 ASN B CB  1 
ATOM   6370 C  CG  . ASN B 1 436 ? 52.941 113.471 -35.863  1.00 30.66  ? 438 ASN B CG  1 
ATOM   6371 O  OD1 . ASN B 1 436 ? 53.705 114.299 -35.315  1.00 32.82  ? 438 ASN B OD1 1 
ATOM   6372 N  N   . LYS B 1 437 ? 53.806 109.987 -33.256  1.00 36.38  ? 439 LYS B N   1 
ATOM   6373 C  CA  . LYS B 1 437 ? 53.896 109.350 -31.911  1.00 37.36  ? 439 LYS B CA  1 
ATOM   6374 C  C   . LYS B 1 437 ? 53.708 110.401 -30.821  1.00 34.43  ? 439 LYS B C   1 
ATOM   6375 O  O   . LYS B 1 437 ? 54.426 111.432 -30.848  1.00 30.96  ? 439 LYS B O   1 
ATOM   6376 C  CB  . LYS B 1 437 ? 55.290 108.750 -31.694  1.00 42.25  ? 439 LYS B CB  1 
ATOM   6377 C  CG  . LYS B 1 437 ? 55.852 107.899 -32.833  1.00 46.82  ? 439 LYS B CG  1 
ATOM   6378 C  CD  . LYS B 1 437 ? 57.066 107.079 -32.408  1.00 50.85  ? 439 LYS B CD  1 
ATOM   6379 C  CE  . LYS B 1 437 ? 57.610 106.171 -33.494  1.00 53.21  ? 439 LYS B CE  1 
ATOM   6380 N  NZ  . LYS B 1 437 ? 58.935 105.616 -33.107  1.00 54.73  ? 439 LYS B NZ  1 
ATOM   6381 N  N   . GLN B 1 438 ? 52.837 110.100 -29.860  1.00 33.99  ? 440 GLN B N   1 
ATOM   6382 C  CA  . GLN B 1 438 ? 52.661 110.894 -28.621  1.00 33.84  ? 440 GLN B CA  1 
ATOM   6383 C  C   . GLN B 1 438 ? 53.960 110.942 -27.826  1.00 32.80  ? 440 GLN B C   1 
ATOM   6384 O  O   . GLN B 1 438 ? 54.649 109.908 -27.774  1.00 32.46  ? 440 GLN B O   1 
ATOM   6385 C  CB  . GLN B 1 438 ? 51.642 110.232 -27.712  1.00 36.26  ? 440 GLN B CB  1 
ATOM   6386 C  CG  . GLN B 1 438 ? 50.259 110.233 -28.342  1.00 38.40  ? 440 GLN B CG  1 
ATOM   6387 C  CD  . GLN B 1 438 ? 49.232 109.766 -27.345  1.00 39.72  ? 440 GLN B CD  1 
ATOM   6388 O  OE1 . GLN B 1 438 ? 49.318 110.099 -26.173  1.00 40.99  ? 440 GLN B OE1 1 
ATOM   6389 N  NE2 . GLN B 1 438 ? 48.260 108.988 -27.796  1.00 41.10  ? 440 GLN B NE2 1 
ATOM   6390 N  N   . GLY B 1 439 ? 54.273 112.104 -27.254  1.00 31.56  ? 441 GLY B N   1 
ATOM   6391 C  CA  . GLY B 1 439 ? 55.245 112.247 -26.148  1.00 31.98  ? 441 GLY B CA  1 
ATOM   6392 C  C   . GLY B 1 439 ? 54.885 111.367 -24.951  1.00 32.21  ? 441 GLY B C   1 
ATOM   6393 O  O   . GLY B 1 439 ? 53.748 110.869 -24.882  1.00 30.67  ? 441 GLY B O   1 
ATOM   6394 N  N   . ALA B 1 440 ? 55.813 111.219 -24.007  1.00 33.18  ? 442 ALA B N   1 
ATOM   6395 C  CA  . ALA B 1 440 ? 55.684 110.309 -22.855  1.00 33.36  ? 442 ALA B CA  1 
ATOM   6396 C  C   . ALA B 1 440 ? 55.056 111.082 -21.690  1.00 33.68  ? 442 ALA B C   1 
ATOM   6397 O  O   . ALA B 1 440 ? 55.429 112.264 -21.488  1.00 32.68  ? 442 ALA B O   1 
ATOM   6398 C  CB  . ALA B 1 440 ? 57.036 109.736 -22.550  1.00 33.97  ? 442 ALA B CB  1 
ATOM   6399 N  N   . LEU B 1 441 ? 54.044 110.499 -21.049  1.00 33.76  ? 443 LEU B N   1 
ATOM   6400 C  CA  . LEU B 1 441 ? 53.482 111.020 -19.778  1.00 36.80  ? 443 LEU B CA  1 
ATOM   6401 C  C   . LEU B 1 441 ? 54.106 110.199 -18.652  1.00 35.44  ? 443 LEU B C   1 
ATOM   6402 O  O   . LEU B 1 441 ? 53.635 109.096 -18.385  1.00 33.23  ? 443 LEU B O   1 
ATOM   6403 C  CB  . LEU B 1 441 ? 51.954 110.928 -19.768  1.00 39.34  ? 443 LEU B CB  1 
ATOM   6404 C  CG  . LEU B 1 441 ? 51.249 112.175 -20.306  1.00 41.63  ? 443 LEU B CG  1 
ATOM   6405 C  CD1 . LEU B 1 441 ? 49.739 111.953 -20.426  1.00 41.70  ? 443 LEU B CD1 1 
ATOM   6406 C  CD2 . LEU B 1 441 ? 51.578 113.406 -19.446  1.00 42.19  ? 443 LEU B CD2 1 
ATOM   6407 N  N   . LEU B 1 442 ? 55.228 110.662 -18.142  1.00 35.64  ? 444 LEU B N   1 
ATOM   6408 C  CA  . LEU B 1 442 ? 56.091 109.791 -17.312  1.00 38.50  ? 444 LEU B CA  1 
ATOM   6409 C  C   . LEU B 1 442 ? 55.560 109.707 -15.883  1.00 38.75  ? 444 LEU B C   1 
ATOM   6410 O  O   . LEU B 1 442 ? 55.094 110.689 -15.309  1.00 38.11  ? 444 LEU B O   1 
ATOM   6411 C  CB  . LEU B 1 442 ? 57.525 110.312 -17.374  1.00 38.66  ? 444 LEU B CB  1 
ATOM   6412 C  CG  . LEU B 1 442 ? 58.242 110.019 -18.683  1.00 38.30  ? 444 LEU B CG  1 
ATOM   6413 C  CD1 . LEU B 1 442 ? 59.623 110.683 -18.699  1.00 38.23  ? 444 LEU B CD1 1 
ATOM   6414 C  CD2 . LEU B 1 442 ? 58.289 108.507 -18.923  1.00 38.82  ? 444 LEU B CD2 1 
ATOM   6415 N  N   . PRO B 1 443 ? 55.594 108.497 -15.287  1.00 40.93  ? 445 PRO B N   1 
ATOM   6416 C  CA  . PRO B 1 443 ? 55.227 108.327 -13.888  1.00 42.20  ? 445 PRO B CA  1 
ATOM   6417 C  C   . PRO B 1 443 ? 56.298 108.927 -12.967  1.00 43.32  ? 445 PRO B C   1 
ATOM   6418 O  O   . PRO B 1 443 ? 57.459 108.954 -13.316  1.00 42.35  ? 445 PRO B O   1 
ATOM   6419 C  CB  . PRO B 1 443 ? 55.135 106.801 -13.720  1.00 43.33  ? 445 PRO B CB  1 
ATOM   6420 C  CG  . PRO B 1 443 ? 56.093 106.239 -14.767  1.00 44.13  ? 445 PRO B CG  1 
ATOM   6421 C  CD  . PRO B 1 443 ? 56.031 107.231 -15.913  1.00 42.18  ? 445 PRO B CD  1 
ATOM   6422 N  N   . ASN B 1 444 ? 55.861 109.369 -11.796  1.00 45.63  ? 446 ASN B N   1 
ATOM   6423 C  CA  . ASN B 1 444 ? 56.730 109.959 -10.750  1.00 48.07  ? 446 ASN B CA  1 
ATOM   6424 C  C   . ASN B 1 444 ? 56.639 109.066 -9.517   1.00 49.42  ? 446 ASN B C   1 
ATOM   6425 O  O   . ASN B 1 444 ? 55.526 108.901 -9.030   1.00 49.78  ? 446 ASN B O   1 
ATOM   6426 C  CB  . ASN B 1 444 ? 56.306 111.401 -10.434  1.00 49.11  ? 446 ASN B CB  1 
ATOM   6427 C  CG  . ASN B 1 444 ? 56.133 112.284 -11.662  1.00 48.80  ? 446 ASN B CG  1 
ATOM   6428 O  OD1 . ASN B 1 444 ? 57.101 112.626 -12.336  1.00 49.01  ? 446 ASN B OD1 1 
ATOM   6429 N  ND2 . ASN B 1 444 ? 54.904 112.671 -11.960  1.00 47.51  ? 446 ASN B ND2 1 
ATOM   6430 N  N   . THR B 1 445 ? 57.755 108.536 -9.016   1.00 50.62  ? 447 THR B N   1 
ATOM   6431 C  CA  . THR B 1 445 ? 57.767 107.668 -7.812   1.00 50.28  ? 447 THR B CA  1 
ATOM   6432 C  C   . THR B 1 445 ? 57.156 108.473 -6.645   1.00 50.12  ? 447 THR B C   1 
ATOM   6433 O  O   . THR B 1 445 ? 56.382 107.943 -5.860   1.00 47.84  ? 447 THR B O   1 
ATOM   6434 C  CB  . THR B 1 445 ? 59.166 107.100 -7.512   1.00 51.08  ? 447 THR B CB  1 
ATOM   6435 O  OG1 . THR B 1 445 ? 59.680 106.143 -8.447   1.00 49.29  ? 447 THR B OG1 1 
ATOM   6436 C  CG2 . THR B 1 445 ? 59.166 106.383 -6.183   1.00 53.53  ? 447 THR B CG2 1 
HETATM 6437 NA NA  . NA  C 2 .   ? 34.943 123.829 -42.272  0.74 24.18  1 501 NA  A NA  1 
HETATM 6438 NA NA  . NA  D 2 .   ? 33.433 125.242 -40.753  0.75 25.71  1 502 NA  A NA  1 
HETATM 6439 NA NA  . NA  E 2 .   ? 32.369 124.165 -15.528  0.96 24.18  1 503 NA  A NA  1 
HETATM 6440 NA NA  . NA  F 2 .   ? 33.778 131.710 10.457   1.00 23.88  1 504 NA  A NA  1 
HETATM 6441 S  S   . SO4 G 3 .   ? 31.091 125.981 25.552   0.04 28.92  ? 505 SO4 A S   1 
HETATM 6442 O  O1  . SO4 G 3 .   ? 29.739 125.887 25.064   0.74 29.29  ? 505 SO4 A O1  1 
HETATM 6443 O  O2  . SO4 G 3 .   ? 31.901 124.954 24.943   0.74 27.45  ? 505 SO4 A O2  1 
HETATM 6444 O  O3  . SO4 G 3 .   ? 31.087 125.816 26.975   0.74 29.43  ? 505 SO4 A O3  1 
HETATM 6445 O  O4  . SO4 G 3 .   ? 31.636 127.273 25.233   0.74 29.29  ? 505 SO4 A O4  1 
HETATM 6446 C  C1  . GOL H 4 .   ? 42.700 124.440 -3.992   1.00 53.81  ? 506 GOL A C1  1 
HETATM 6447 O  O1  . GOL H 4 .   ? 42.523 125.564 -3.136   1.00 47.57  ? 506 GOL A O1  1 
HETATM 6448 C  C2  . GOL H 4 .   ? 41.397 123.990 -4.624   1.00 57.87  ? 506 GOL A C2  1 
HETATM 6449 O  O2  . GOL H 4 .   ? 40.801 125.075 -5.341   1.00 62.35  ? 506 GOL A O2  1 
HETATM 6450 C  C3  . GOL H 4 .   ? 41.561 122.800 -5.550   1.00 56.75  ? 506 GOL A C3  1 
HETATM 6451 O  O3  . GOL H 4 .   ? 40.302 122.293 -5.990   1.00 56.26  ? 506 GOL A O3  1 
HETATM 6452 CD CD  . CD  I 5 .   ? 35.555 133.218 9.743    0.85 25.43  ? 507 CD  A CD  1 
HETATM 6453 CD CD  . CD  J 5 .   ? 35.985 114.660 -14.989  1.00 31.42  ? 508 CD  A CD  1 
HETATM 6454 CD CD  . CD  K 5 .   ? 41.813 110.913 10.826   0.38 38.98  ? 509 CD  A CD  1 
HETATM 6455 CL CL  . CL  L 6 .   ? 34.518 116.293 -14.461  1.00 32.45  ? 510 CL  A CL  1 
HETATM 6456 NA NA  . NA  M 2 .   ? 54.739 114.836 -105.435 0.78 23.80  1 501 NA  B NA  1 
HETATM 6457 NA NA  . NA  N 2 .   ? 56.718 123.004 -99.874  1.00 24.10  1 502 NA  B NA  1 
HETATM 6458 S  S   . SO4 O 3 .   ? 53.806 115.129 -139.292 0.05 37.17  ? 503 SO4 B S   1 
HETATM 6459 O  O1  . SO4 O 3 .   ? 55.055 115.828 -139.080 1.00 37.45  ? 503 SO4 B O1  1 
HETATM 6460 O  O2  . SO4 O 3 .   ? 53.626 114.892 -140.694 1.00 38.23  ? 503 SO4 B O2  1 
HETATM 6461 O  O3  . SO4 O 3 .   ? 52.710 115.903 -138.796 1.00 36.52  ? 503 SO4 B O3  1 
HETATM 6462 O  O4  . SO4 O 3 .   ? 53.813 113.883 -138.593 1.00 37.35  ? 503 SO4 B O4  1 
HETATM 6463 CD CD  . CD  P 5 .   ? 50.323 106.696 -124.938 0.46 42.59  ? 504 CD  B CD  1 
HETATM 6464 CD CD  . CD  Q 5 .   ? 48.997 130.837 -128.997 0.78 39.63  ? 505 CD  B CD  1 
HETATM 6465 CD CD  . CD  R 5 .   ? 54.597 112.830 -99.849  1.00 31.11  ? 506 CD  B CD  1 
HETATM 6466 O  O   . HOH S 7 .   ? 33.814 115.112 -38.663  1.00 20.47  ? 601 HOH A O   1 
HETATM 6467 O  O   . HOH S 7 .   ? 37.779 120.963 -5.539   1.00 15.39  ? 602 HOH A O   1 
HETATM 6468 O  O   . HOH S 7 .   ? 41.778 115.853 -9.000   1.00 23.63  ? 603 HOH A O   1 
HETATM 6469 O  O   . HOH S 7 .   ? 35.329 120.284 21.036   1.00 18.31  ? 604 HOH A O   1 
HETATM 6470 O  O   . HOH S 7 .   ? 46.435 112.964 -67.502  1.00 15.99  ? 605 HOH A O   1 
HETATM 6471 O  O   . HOH S 7 .   ? 31.490 123.052 -13.401  1.00 19.42  ? 606 HOH A O   1 
HETATM 6472 O  O   . HOH S 7 .   ? 40.844 129.830 -45.757  1.00 16.57  ? 607 HOH A O   1 
HETATM 6473 O  O   . HOH S 7 .   ? 34.748 121.621 -42.102  1.00 11.15  ? 608 HOH A O   1 
HETATM 6474 O  O   . HOH S 7 .   ? 33.711 122.488 -75.193  1.00 29.77  ? 609 HOH A O   1 
HETATM 6475 O  O   . HOH S 7 .   ? 48.045 121.816 -69.432  1.00 20.93  ? 610 HOH A O   1 
HETATM 6476 O  O   . HOH S 7 .   ? 46.178 116.668 -62.974  1.00 13.68  ? 611 HOH A O   1 
HETATM 6477 O  O   . HOH S 7 .   ? 38.319 110.301 -44.050  1.00 18.66  ? 612 HOH A O   1 
HETATM 6478 O  O   . HOH S 7 .   ? 35.483 133.725 -9.468   1.00 20.26  ? 613 HOH A O   1 
HETATM 6479 O  O   . HOH S 7 .   ? 33.017 137.379 -38.188  1.00 22.91  ? 614 HOH A O   1 
HETATM 6480 O  O   . HOH S 7 .   ? 40.645 103.555 -53.329  1.00 23.73  ? 615 HOH A O   1 
HETATM 6481 O  O   . HOH S 7 .   ? 35.598 109.267 -109.080 1.00 28.74  ? 616 HOH A O   1 
HETATM 6482 O  O   . HOH T 7 .   ? 49.010 113.040 -106.035 1.00 34.50  ? 601 HOH B O   1 
HETATM 6483 O  O   . HOH T 7 .   ? 48.176 121.843 -39.752  1.00 13.07  ? 602 HOH B O   1 
HETATM 6484 O  O   . HOH T 7 .   ? 58.192 121.546 -101.868 1.00 15.28  ? 603 HOH B O   1 
HETATM 6485 O  O   . HOH T 7 .   ? 62.918 120.273 -88.410  1.00 20.84  ? 604 HOH B O   1 
HETATM 6486 O  O   . HOH T 7 .   ? 48.203 118.717 -39.187  1.00 12.34  ? 605 HOH B O   1 
HETATM 6487 O  O   . HOH T 7 .   ? 55.677 125.557 -75.110  1.00 17.66  ? 606 HOH B O   1 
HETATM 6488 O  O   . HOH T 7 .   ? 60.850 106.633 -125.669 1.00 38.02  ? 607 HOH B O   1 
HETATM 6489 O  O   . HOH T 7 .   ? 49.842 114.166 -73.899  1.00 22.29  ? 608 HOH B O   1 
HETATM 6490 O  O   . HOH T 7 .   ? 62.003 113.344 -115.846 1.00 26.87  ? 609 HOH B O   1 
HETATM 6491 O  O   . HOH T 7 .   ? 53.443 106.964 -46.848  1.00 22.97  ? 610 HOH B O   1 
HETATM 6492 O  O   . HOH T 7 .   ? 46.988 117.024 -70.864  1.00 11.58  ? 611 HOH B O   1 
HETATM 6493 O  O   . HOH T 7 .   ? 53.744 128.473 -124.610 1.00 26.37  ? 612 HOH B O   1 
HETATM 6494 O  O   . HOH T 7 .   ? 55.228 121.610 -73.393  1.00 17.64  ? 613 HOH B O   1 
HETATM 6495 O  O   . HOH T 7 .   ? 50.125 126.135 -118.493 1.00 27.26  ? 614 HOH B O   1 
HETATM 6496 O  O   . HOH T 7 .   ? 48.848 119.454 -110.041 1.00 25.58  ? 615 HOH B O   1 
HETATM 6497 O  O   . HOH T 7 .   ? 66.254 124.938 -104.104 1.00 18.28  ? 616 HOH B O   1 
HETATM 6498 O  O   . HOH T 7 .   ? 55.967 114.565 -100.665 1.00 13.11  ? 617 HOH B O   1 
HETATM 6499 O  O   . HOH T 7 .   ? 54.056 123.987 -73.365  1.00 15.65  ? 618 HOH B O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . THR A 27  ? 0.9785 0.7111 0.7099 -0.0003 0.0581  0.0258  29  THR A N   
2    C CA  . THR A 27  ? 0.9623 0.7126 0.7131 0.0058  0.0577  0.0265  29  THR A CA  
3    C C   . THR A 27  ? 0.9863 0.7346 0.7325 -0.0078 0.0607  0.0204  29  THR A C   
4    O O   . THR A 27  ? 1.0189 0.7419 0.7380 -0.0183 0.0655  0.0171  29  THR A O   
5    C CB  . THR A 27  ? 0.9813 0.7177 0.7232 0.0234  0.0614  0.0326  29  THR A CB  
6    O OG1 . THR A 27  ? 0.9993 0.7019 0.7099 0.0200  0.0689  0.0307  29  THR A OG1 
7    C CG2 . THR A 27  ? 1.0014 0.7359 0.7417 0.0380  0.0595  0.0391  29  THR A CG2 
8    N N   . TYR A 28  ? 0.9366 0.7100 0.7068 -0.0078 0.0579  0.0191  30  TYR A N   
9    C CA  . TYR A 28  ? 0.9314 0.7109 0.7027 -0.0210 0.0589  0.0132  30  TYR A CA  
10   C C   . TYR A 28  ? 0.9112 0.6909 0.6865 -0.0140 0.0611  0.0145  30  TYR A C   
11   O O   . TYR A 28  ? 0.8754 0.6582 0.6591 0.0006  0.0610  0.0197  30  TYR A O   
12   C CB  . TYR A 28  ? 0.9023 0.7129 0.6980 -0.0289 0.0529  0.0097  30  TYR A CB  
13   C CG  . TYR A 28  ? 0.9147 0.7233 0.7040 -0.0367 0.0517  0.0080  30  TYR A CG  
14   C CD1 . TYR A 28  ? 0.9490 0.7425 0.7167 -0.0513 0.0553  0.0034  30  TYR A CD1 
15   C CD2 . TYR A 28  ? 0.9070 0.7277 0.7101 -0.0302 0.0472  0.0110  30  TYR A CD2 
16   C CE1 . TYR A 28  ? 0.9703 0.7616 0.7312 -0.0590 0.0546  0.0017  30  TYR A CE1 
17   C CE2 . TYR A 28  ? 0.9477 0.7652 0.7438 -0.0374 0.0463  0.0094  30  TYR A CE2 
18   C CZ  . TYR A 28  ? 0.9663 0.7691 0.7415 -0.0516 0.0502  0.0048  30  TYR A CZ  
19   O OH  . TYR A 28  ? 0.9509 0.7506 0.7186 -0.0590 0.0497  0.0031  30  TYR A OH  
20   N N   . THR A 29  ? 0.9271 0.7043 0.6958 -0.0249 0.0632  0.0099  31  THR A N   
21   C CA  . THR A 29  ? 0.9490 0.7252 0.7193 -0.0210 0.0656  0.0102  31  THR A CA  
22   C C   . THR A 29  ? 0.9348 0.7352 0.7216 -0.0317 0.0619  0.0052  31  THR A C   
23   O O   . THR A 29  ? 0.9644 0.7608 0.7387 -0.0466 0.0630  0.0003  31  THR A O   
24   C CB  . THR A 29  ? 0.9719 0.7117 0.7086 -0.0225 0.0733  0.0101  31  THR A CB  
25   O OG1 . THR A 29  ? 0.9889 0.7090 0.7131 -0.0082 0.0765  0.0157  31  THR A OG1 
26   C CG2 . THR A 29  ? 0.9815 0.7188 0.7176 -0.0207 0.0761  0.0097  31  THR A CG2 
27   N N   . ILE A 30  ? 0.8828 0.7073 0.6952 -0.0246 0.0579  0.0066  32  ILE A N   
28   C CA  . ILE A 30  ? 0.8415 0.6867 0.6679 -0.0315 0.0548  0.0027  32  ILE A CA  
29   C C   . ILE A 30  ? 0.8602 0.6921 0.6756 -0.0310 0.0590  0.0024  32  ILE A C   
30   O O   . ILE A 30  ? 0.8961 0.7166 0.7087 -0.0194 0.0622  0.0066  32  ILE A O   
31   C CB  . ILE A 30  ? 0.7721 0.6450 0.6269 -0.0246 0.0489  0.0041  32  ILE A CB  
32   C CG1 . ILE A 30  ? 0.7534 0.6387 0.6165 -0.0279 0.0449  0.0032  32  ILE A CG1 
33   C CG2 . ILE A 30  ? 0.7346 0.6237 0.6008 -0.0278 0.0466  0.0013  32  ILE A CG2 
34   C CD1 . ILE A 30  ? 0.7399 0.6435 0.6246 -0.0190 0.0402  0.0063  32  ILE A CD1 
35   N N   . GLN A 31  ? 0.8537 0.6871 0.6619 -0.0435 0.0592  -0.0022 33  GLN A N   
36   C CA  . GLN A 31  ? 0.8813 0.7055 0.6807 -0.0448 0.0622  -0.0031 33  GLN A CA  
37   C C   . GLN A 31  ? 0.8141 0.6660 0.6364 -0.0445 0.0569  -0.0047 33  GLN A C   
38   O O   . GLN A 31  ? 0.8257 0.6982 0.6579 -0.0524 0.0525  -0.0081 33  GLN A O   
39   C CB  . GLN A 31  ? 0.9613 0.7640 0.7322 -0.0592 0.0666  -0.0068 33  GLN A CB  
40   C CG  . GLN A 31  ? 1.0265 0.7920 0.7695 -0.0543 0.0741  -0.0040 33  GLN A CG  
41   C CD  . GLN A 31  ? 1.1038 0.8469 0.8178 -0.0691 0.0777  -0.0072 33  GLN A CD  
42   O OE1 . GLN A 31  ? 1.1925 0.9158 0.8911 -0.0665 0.0806  -0.0053 33  GLN A OE1 
43   N NE2 . GLN A 31  ? 1.1527 0.9003 0.8587 -0.0855 0.0772  -0.0122 33  GLN A NE2 
44   N N   . LEU A 32  ? 0.7592 0.6113 0.5889 -0.0348 0.0577  -0.0020 34  LEU A N   
45   C CA  . LEU A 32  ? 0.6914 0.5666 0.5419 -0.0320 0.0530  -0.0026 34  LEU A CA  
46   C C   . LEU A 32  ? 0.6629 0.5308 0.5027 -0.0374 0.0551  -0.0048 34  LEU A C   
47   O O   . LEU A 32  ? 0.7001 0.5521 0.5318 -0.0313 0.0596  -0.0025 34  LEU A O   
48   C CB  . LEU A 32  ? 0.6866 0.5672 0.5523 -0.0183 0.0526  0.0021  34  LEU A CB  
49   C CG  . LEU A 32  ? 0.6650 0.5667 0.5506 -0.0148 0.0479  0.0020  34  LEU A CG  
50   C CD1 . LEU A 32  ? 0.6380 0.5602 0.5374 -0.0180 0.0420  0.0001  34  LEU A CD1 
51   C CD2 . LEU A 32  ? 0.6704 0.5731 0.5656 -0.0032 0.0492  0.0068  34  LEU A CD2 
52   N N   . SER A 33  ? 0.6222 0.5023 0.4614 -0.0485 0.0520  -0.0091 35  SER A N   
53   C CA  . SER A 33  ? 0.6283 0.5033 0.4554 -0.0566 0.0532  -0.0119 35  SER A CA  
54   C C   . SER A 33  ? 0.6016 0.4923 0.4443 -0.0506 0.0496  -0.0115 35  SER A C   
55   O O   . SER A 33  ? 0.5662 0.4751 0.4291 -0.0429 0.0453  -0.0101 35  SER A O   
56   C CB  . SER A 33  ? 0.6456 0.5292 0.4647 -0.0717 0.0513  -0.0164 35  SER A CB  
57   O OG  . SER A 33  ? 0.6212 0.5357 0.4608 -0.0718 0.0447  -0.0181 35  SER A OG  
58   N N   . GLY A 34  ? 0.5980 0.4797 0.4294 -0.0545 0.0514  -0.0127 36  GLY A N   
59   C CA  . GLY A 34  ? 0.5695 0.4607 0.4105 -0.0497 0.0490  -0.0124 36  GLY A CA  
60   C C   . GLY A 34  ? 0.5652 0.4480 0.4130 -0.0367 0.0519  -0.0082 36  GLY A C   
61   O O   . GLY A 34  ? 0.5439 0.4389 0.4049 -0.0311 0.0488  -0.0074 36  GLY A O   
62   N N   . THR A 35  ? 0.5760 0.4394 0.4149 -0.0314 0.0578  -0.0053 37  THR A N   
63   C CA  . THR A 35  ? 0.5739 0.4334 0.4205 -0.0187 0.0608  -0.0010 37  THR A CA  
64   C C   . THR A 35  ? 0.6011 0.4417 0.4328 -0.0176 0.0665  -0.0006 37  THR A C   
65   O O   . THR A 35  ? 0.6138 0.4399 0.4263 -0.0267 0.0687  -0.0033 37  THR A O   
66   C CB  . THR A 35  ? 0.5960 0.4489 0.4433 -0.0111 0.0637  0.0025  37  THR A CB  
67   O OG1 . THR A 35  ? 0.6523 0.4812 0.4761 -0.0154 0.0690  0.0019  37  THR A OG1 
68   C CG2 . THR A 35  ? 0.5723 0.4438 0.4350 -0.0114 0.0581  0.0024  37  THR A CG2 
69   N N   . SER A 36  ? 0.5882 0.4298 0.4283 -0.0074 0.0688  0.0026  38  SER A N   
70   C CA  . SER A 36  ? 0.6171 0.4410 0.4449 -0.0034 0.0754  0.0039  38  SER A CA  
71   C C   . SER A 36  ? 0.6386 0.4563 0.4682 0.0090  0.0809  0.0087  38  SER A C   
72   O O   . SER A 36  ? 0.6344 0.4643 0.4766 0.0132  0.0782  0.0107  38  SER A O   
73   C CB  . SER A 36  ? 0.5788 0.4136 0.4163 -0.0030 0.0729  0.0032  38  SER A CB  
74   O OG  . SER A 36  ? 0.5365 0.3854 0.3924 0.0061  0.0722  0.0065  38  SER A OG  
75   N N   . GLU A 37  ? 0.6757 0.4760 0.4928 0.0152  0.0884  0.0107  39  GLU A N   
76   C CA  . GLU A 37  ? 0.6902 0.4916 0.5134 0.0293  0.0933  0.0158  39  GLU A CA  
77   C C   . GLU A 37  ? 0.6336 0.4611 0.4816 0.0328  0.0893  0.0172  39  GLU A C   
78   O O   . GLU A 37  ? 0.6047 0.4423 0.4598 0.0252  0.0839  0.0142  39  GLU A O   
79   C CB  . GLU A 37  ? 0.7659 0.5432 0.5693 0.0360  0.1028  0.0175  39  GLU A CB  
80   C CG  . GLU A 37  ? 0.8443 0.5913 0.6188 0.0325  0.1077  0.0162  39  GLU A CG  
81   C CD  . GLU A 37  ? 0.9152 0.6379 0.6704 0.0449  0.1181  0.0198  39  GLU A CD  
82   O OE1 . GLU A 37  ? 0.9279 0.6537 0.6878 0.0580  0.1208  0.0243  39  GLU A OE1 
83   O OE2 . GLU A 37  ? 0.9769 0.6782 0.7124 0.0419  0.1234  0.0181  39  GLU A OE2 
84   N N   . GLY A 38  ? 0.6261 0.4638 0.4854 0.0437  0.0916  0.0217  40  GLY A N   
85   C CA  . GLY A 38  ? 0.6189 0.4799 0.4992 0.0469  0.0893  0.0237  40  GLY A CA  
86   C C   . GLY A 38  ? 0.6193 0.5024 0.5186 0.0475  0.0831  0.0253  40  GLY A C   
87   O O   . GLY A 38  ? 0.6281 0.5293 0.5426 0.0520  0.0829  0.0282  40  GLY A O   
88   N N   . HIS A 39  ? 0.6030 0.4856 0.5012 0.0423  0.0783  0.0235  41  HIS A N   
89   C CA  . HIS A 39  ? 0.5680 0.4709 0.4834 0.0409  0.0717  0.0242  41  HIS A CA  
90   C C   . HIS A 39  ? 0.5844 0.4888 0.5009 0.0489  0.0733  0.0283  41  HIS A C   
91   O O   . HIS A 39  ? 0.6064 0.4922 0.5068 0.0533  0.0784  0.0292  41  HIS A O   
92   C CB  . HIS A 39  ? 0.5440 0.4486 0.4593 0.0308  0.0652  0.0197  41  HIS A CB  
93   C CG  . HIS A 39  ? 0.5219 0.4245 0.4340 0.0241  0.0634  0.0160  41  HIS A CG  
94   N ND1 . HIS A 39  ? 0.4739 0.3902 0.3964 0.0197  0.0572  0.0140  41  HIS A ND1 
95   C CD2 . HIS A 39  ? 0.5361 0.4240 0.4343 0.0214  0.0669  0.0140  41  HIS A CD2 
96   C CE1 . HIS A 39  ? 0.4877 0.3990 0.4037 0.0154  0.0566  0.0111  41  HIS A CE1 
97   N NE2 . HIS A 39  ? 0.5365 0.4310 0.4381 0.0158  0.0625  0.0110  41  HIS A NE2 
98   N N   . TYR A 40  ? 0.5884 0.5136 0.5219 0.0504  0.0690  0.0306  42  TYR A N   
99   C CA  . TYR A 40  ? 0.5925 0.5239 0.5300 0.0556  0.0676  0.0340  42  TYR A CA  
100  C C   . TYR A 40  ? 0.5380 0.4795 0.4840 0.0473  0.0599  0.0315  42  TYR A C   
101  O O   . TYR A 40  ? 0.4936 0.4522 0.4535 0.0441  0.0556  0.0317  42  TYR A O   
102  C CB  . TYR A 40  ? 0.6375 0.5868 0.5874 0.0650  0.0695  0.0394  42  TYR A CB  
103  C CG  . TYR A 40  ? 0.6918 0.6336 0.6343 0.0742  0.0776  0.0418  42  TYR A CG  
104  C CD1 . TYR A 40  ? 0.7404 0.6698 0.6709 0.0855  0.0832  0.0452  42  TYR A CD1 
105  C CD2 . TYR A 40  ? 0.7036 0.6492 0.6495 0.0723  0.0800  0.0409  42  TYR A CD2 
106  C CE1 . TYR A 40  ? 0.8025 0.7241 0.7249 0.0953  0.0913  0.0476  42  TYR A CE1 
107  C CE2 . TYR A 40  ? 0.7351 0.6737 0.6738 0.0809  0.0879  0.0430  42  TYR A CE2 
108  C CZ  . TYR A 40  ? 0.7879 0.7148 0.7151 0.0928  0.0937  0.0464  42  TYR A CZ  
109  O OH  . TYR A 40  ? 0.8403 0.7596 0.7592 0.1026  0.1022  0.0487  42  TYR A OH  
110  N N   . TYR A 41  ? 0.5094 0.4385 0.4450 0.0431  0.0588  0.0291  43  TYR A N   
111  C CA  . TYR A 41  ? 0.4751 0.4117 0.4162 0.0358  0.0524  0.0266  43  TYR A CA  
112  C C   . TYR A 41  ? 0.4704 0.4157 0.4180 0.0404  0.0503  0.0304  43  TYR A C   
113  O O   . TYR A 41  ? 0.4947 0.4304 0.4336 0.0469  0.0537  0.0331  43  TYR A O   
114  C CB  . TYR A 41  ? 0.4708 0.3918 0.3973 0.0285  0.0528  0.0222  43  TYR A CB  
115  C CG  . TYR A 41  ? 0.4549 0.3734 0.3782 0.0225  0.0527  0.0183  43  TYR A CG  
116  C CD1 . TYR A 41  ? 0.4256 0.3587 0.3606 0.0184  0.0475  0.0162  43  TYR A CD1 
117  C CD2 . TYR A 41  ? 0.4695 0.3702 0.3767 0.0209  0.0576  0.0167  43  TYR A CD2 
118  C CE1 . TYR A 41  ? 0.4138 0.3454 0.3456 0.0138  0.0469  0.0129  43  TYR A CE1 
119  C CE2 . TYR A 41  ? 0.4566 0.3564 0.3609 0.0149  0.0568  0.0132  43  TYR A CE2 
120  C CZ  . TYR A 41  ? 0.4249 0.3411 0.3423 0.0120  0.0513  0.0115  43  TYR A CZ  
121  O OH  . TYR A 41  ? 0.4085 0.3254 0.3234 0.0072  0.0498  0.0084  43  TYR A OH  
122  N N   . GLU A 42  ? 0.4620 0.4248 0.4237 0.0374  0.0449  0.0307  44  GLU A N   
123  C CA  . GLU A 42  ? 0.4769 0.4504 0.4458 0.0400  0.0417  0.0341  44  GLU A CA  
124  C C   . GLU A 42  ? 0.4444 0.4151 0.4107 0.0330  0.0374  0.0309  44  GLU A C   
125  O O   . GLU A 42  ? 0.4152 0.3887 0.3841 0.0260  0.0345  0.0270  44  GLU A O   
126  C CB  . GLU A 42  ? 0.4998 0.4939 0.4839 0.0400  0.0388  0.0366  44  GLU A CB  
127  C CG  . GLU A 42  ? 0.5390 0.5400 0.5270 0.0478  0.0432  0.0407  44  GLU A CG  
128  C CD  . GLU A 42  ? 0.5515 0.5746 0.5539 0.0461  0.0408  0.0433  44  GLU A CD  
129  O OE1 . GLU A 42  ? 0.5366 0.5657 0.5438 0.0377  0.0359  0.0411  44  GLU A OE1 
130  O OE2 . GLU A 42  ? 0.5965 0.6301 0.6037 0.0532  0.0444  0.0474  44  GLU A OE2 
131  N N   . VAL A 43  ? 0.4563 0.4212 0.4167 0.0357  0.0376  0.0328  45  VAL A N   
132  C CA  . VAL A 43  ? 0.4380 0.3979 0.3933 0.0294  0.0347  0.0299  45  VAL A CA  
133  C C   . VAL A 43  ? 0.4235 0.3948 0.3867 0.0312  0.0306  0.0333  45  VAL A C   
134  O O   . VAL A 43  ? 0.4412 0.4116 0.4022 0.0389  0.0320  0.0378  45  VAL A O   
135  C CB  . VAL A 43  ? 0.4707 0.4093 0.4075 0.0294  0.0390  0.0288  45  VAL A CB  
136  C CG1 . VAL A 43  ? 0.4648 0.3997 0.3964 0.0210  0.0364  0.0252  45  VAL A CG1 
137  C CG2 . VAL A 43  ? 0.4780 0.4046 0.4054 0.0281  0.0435  0.0263  45  VAL A CG2 
138  N N   . TYR A 44  ? 0.3815 0.3636 0.3532 0.0250  0.0257  0.0314  46  TYR A N   
139  C CA  . TYR A 44  ? 0.3744 0.3687 0.3541 0.0248  0.0212  0.0343  46  TYR A CA  
140  C C   . TYR A 44  ? 0.3536 0.3411 0.3267 0.0203  0.0191  0.0322  46  TYR A C   
141  O O   . TYR A 44  ? 0.3432 0.3273 0.3136 0.0138  0.0184  0.0275  46  TYR A O   
142  C CB  . TYR A 44  ? 0.3575 0.3654 0.3479 0.0205  0.0179  0.0337  46  TYR A CB  
143  C CG  . TYR A 44  ? 0.3670 0.3840 0.3642 0.0243  0.0197  0.0366  46  TYR A CG  
144  C CD1 . TYR A 44  ? 0.3565 0.3680 0.3517 0.0248  0.0231  0.0344  46  TYR A CD1 
145  C CD2 . TYR A 44  ? 0.3745 0.4070 0.3803 0.0268  0.0180  0.0414  46  TYR A CD2 
146  C CE1 . TYR A 44  ? 0.3712 0.3909 0.3722 0.0279  0.0253  0.0369  46  TYR A CE1 
147  C CE2 . TYR A 44  ? 0.3795 0.4227 0.3920 0.0296  0.0201  0.0440  46  TYR A CE2 
148  C CZ  . TYR A 44  ? 0.3774 0.4135 0.3873 0.0302  0.0240  0.0416  46  TYR A CZ  
149  O OH  . TYR A 44  ? 0.3934 0.4392 0.4090 0.0326  0.0266  0.0439  46  TYR A OH  
150  N N   . HIS A 45  ? 0.3537 0.3397 0.3236 0.0243  0.0185  0.0358  47  HIS A N   
151  C CA  . HIS A 45  ? 0.3478 0.3275 0.3110 0.0202  0.0164  0.0345  47  HIS A CA  
152  C C   . HIS A 45  ? 0.3271 0.3194 0.2995 0.0143  0.0112  0.0337  47  HIS A C   
153  O O   . HIS A 45  ? 0.3256 0.3297 0.3054 0.0163  0.0081  0.0377  47  HIS A O   
154  C CB  . HIS A 45  ? 0.3724 0.3449 0.3275 0.0274  0.0175  0.0392  47  HIS A CB  
155  C CG  . HIS A 45  ? 0.3873 0.3461 0.3299 0.0232  0.0174  0.0372  47  HIS A CG  
156  N ND1 . HIS A 45  ? 0.4243 0.3737 0.3567 0.0288  0.0178  0.0409  47  HIS A ND1 
157  C CD2 . HIS A 45  ? 0.3798 0.3330 0.3176 0.0140  0.0173  0.0319  47  HIS A CD2 
158  C CE1 . HIS A 45  ? 0.4221 0.3593 0.3434 0.0220  0.0179  0.0378  47  HIS A CE1 
159  N NE2 . HIS A 45  ? 0.3963 0.3367 0.3213 0.0128  0.0177  0.0322  47  HIS A NE2 
160  N N   . ILE A 46  ? 0.3055 0.2960 0.2767 0.0075  0.0104  0.0287  48  ILE A N   
161  C CA  . ILE A 46  ? 0.2944 0.2932 0.2711 0.0024  0.0063  0.0272  48  ILE A CA  
162  C C   . ILE A 46  ? 0.3009 0.2962 0.2724 -0.0008 0.0043  0.0269  48  ILE A C   
163  O O   . ILE A 46  ? 0.3126 0.3140 0.2873 -0.0024 0.0006  0.0290  48  ILE A O   
164  C CB  . ILE A 46  ? 0.2785 0.2774 0.2558 -0.0010 0.0070  0.0221  48  ILE A CB  
165  C CG1 . ILE A 46  ? 0.2816 0.2822 0.2625 0.0018  0.0092  0.0222  48  ILE A CG1 
166  C CG2 . ILE A 46  ? 0.2700 0.2739 0.2496 -0.0048 0.0036  0.0207  48  ILE A CG2 
167  C CD1 . ILE A 46  ? 0.2801 0.2892 0.2684 0.0045  0.0080  0.0265  48  ILE A CD1 
168  N N   . PHE A 47  ? 0.3093 0.2948 0.2720 -0.0032 0.0066  0.0238  49  PHE A N   
169  C CA  . PHE A 47  ? 0.3211 0.3012 0.2768 -0.0068 0.0055  0.0232  49  PHE A CA  
170  C C   . PHE A 47  ? 0.3603 0.3273 0.3048 -0.0043 0.0085  0.0248  49  PHE A C   
171  O O   . PHE A 47  ? 0.3577 0.3171 0.2964 -0.0041 0.0124  0.0230  49  PHE A O   
172  C CB  . PHE A 47  ? 0.2992 0.2792 0.2522 -0.0131 0.0062  0.0175  49  PHE A CB  
173  C CG  . PHE A 47  ? 0.2744 0.2636 0.2343 -0.0146 0.0039  0.0155  49  PHE A CG  
174  C CD1 . PHE A 47  ? 0.2751 0.2688 0.2391 -0.0142 0.0003  0.0183  49  PHE A CD1 
175  C CD2 . PHE A 47  ? 0.2572 0.2498 0.2175 -0.0166 0.0054  0.0107  49  PHE A CD2 
176  C CE1 . PHE A 47  ? 0.2647 0.2622 0.2307 -0.0158 -0.0011 0.0163  49  PHE A CE1 
177  C CE2 . PHE A 47  ? 0.2474 0.2457 0.2111 -0.0164 0.0037  0.0091  49  PHE A CE2 
178  C CZ  . PHE A 47  ? 0.2493 0.2481 0.2147 -0.0160 0.0006  0.0118  49  PHE A CZ  
179  N N   . SER A 48  ? 0.4038 0.3671 0.3436 -0.0024 0.0066  0.0284  50  SER A N   
180  C CA  . SER A 48  ? 0.4386 0.3853 0.3630 -0.0017 0.0092  0.0291  50  SER A CA  
181  C C   . SER A 48  ? 0.4471 0.3893 0.3648 -0.0104 0.0091  0.0248  50  SER A C   
182  O O   . SER A 48  ? 0.4212 0.3734 0.3464 -0.0144 0.0062  0.0231  50  SER A O   
183  C CB  . SER A 48  ? 0.4559 0.4014 0.3779 0.0058  0.0070  0.0354  50  SER A CB  
184  O OG  . SER A 48  ? 0.4446 0.4029 0.3754 0.0040  0.0017  0.0373  50  SER A OG  
185  N N   . GLY A 49  ? 0.4948 0.4211 0.3972 -0.0137 0.0129  0.0228  51  GLY A N   
186  C CA  . GLY A 49  ? 0.5225 0.4430 0.4158 -0.0222 0.0135  0.0193  51  GLY A CA  
187  C C   . GLY A 49  ? 0.5723 0.4735 0.4464 -0.0263 0.0186  0.0173  51  GLY A C   
188  O O   . GLY A 49  ? 0.6077 0.4983 0.4748 -0.0214 0.0213  0.0193  51  GLY A O   
189  N N   . THR A 50  ? 0.6064 0.5027 0.4712 -0.0358 0.0203  0.0132  52  THR A N   
190  C CA  . THR A 50  ? 0.6512 0.5279 0.4948 -0.0429 0.0255  0.0105  52  THR A CA  
191  C C   . THR A 50  ? 0.6668 0.5545 0.5138 -0.0530 0.0280  0.0042  52  THR A C   
192  O O   . THR A 50  ? 0.5942 0.5006 0.4541 -0.0567 0.0261  0.0011  52  THR A O   
193  C CB  . THR A 50  ? 0.6764 0.5378 0.5040 -0.0460 0.0257  0.0115  52  THR A CB  
194  O OG1 . THR A 50  ? 0.6466 0.5232 0.4846 -0.0512 0.0231  0.0090  52  THR A OG1 
195  C CG2 . THR A 50  ? 0.6891 0.5402 0.5123 -0.0344 0.0232  0.0185  52  THR A CG2 
196  N N   . LEU A 51  ? 0.7340 0.6107 0.5697 -0.0560 0.0321  0.0027  53  LEU A N   
197  C CA  . LEU A 51  ? 0.8119 0.6965 0.6460 -0.0672 0.0350  -0.0031 53  LEU A CA  
198  C C   . LEU A 51  ? 0.9137 0.7818 0.7252 -0.0795 0.0392  -0.0061 53  LEU A C   
199  O O   . LEU A 51  ? 1.0172 0.8585 0.8075 -0.0785 0.0421  -0.0037 53  LEU A O   
200  C CB  . LEU A 51  ? 0.8276 0.7073 0.6597 -0.0646 0.0371  -0.0027 53  LEU A CB  
201  C CG  . LEU A 51  ? 0.8054 0.7037 0.6459 -0.0724 0.0376  -0.0078 53  LEU A CG  
202  C CD1 . LEU A 51  ? 0.7659 0.6880 0.6313 -0.0641 0.0331  -0.0070 53  LEU A CD1 
203  C CD2 . LEU A 51  ? 0.8373 0.7213 0.6630 -0.0767 0.0417  -0.0089 53  LEU A CD2 
204  N N   . ASP A 52  ? 0.9832 0.8657 0.7974 -0.0902 0.0397  -0.0110 54  ASP A N   
205  C CA  . ASP A 52  ? 1.0609 0.9283 0.8530 -0.1031 0.0438  -0.0139 54  ASP A CA  
206  C C   . ASP A 52  ? 1.1053 0.9696 0.8841 -0.1162 0.0484  -0.0185 54  ASP A C   
207  O O   . ASP A 52  ? 1.0658 0.9366 0.8519 -0.1130 0.0480  -0.0184 54  ASP A O   
208  C CB  . ASP A 52  ? 1.0533 0.9360 0.8531 -0.1077 0.0425  -0.0163 54  ASP A CB  
209  C CG  . ASP A 52  ? 1.0172 0.9286 0.8443 -0.0999 0.0380  -0.0163 54  ASP A CG  
210  O OD1 . ASP A 52  ? 0.9466 0.8782 0.7859 -0.1013 0.0379  -0.0192 54  ASP A OD1 
211  O OD2 . ASP A 52  ? 0.9407 0.8528 0.7750 -0.0923 0.0346  -0.0133 54  ASP A OD2 
212  N N   . THR A 53  ? 1.1579 1.0110 0.9159 -0.1311 0.0527  -0.0221 55  THR A N   
213  C CA  . THR A 53  ? 1.1936 1.0496 0.9390 -0.1482 0.0570  -0.0276 55  THR A CA  
214  C C   . THR A 53  ? 1.1778 1.0733 0.9499 -0.1489 0.0543  -0.0308 55  THR A C   
215  O O   . THR A 53  ? 1.1326 1.0334 0.9042 -0.1531 0.0552  -0.0326 55  THR A O   
216  C CB  . THR A 53  ? 1.2131 1.0552 0.9349 -0.1643 0.0614  -0.0309 55  THR A CB  
217  O OG1 . THR A 53  ? 1.1277 0.9778 0.8587 -0.1605 0.0592  -0.0301 55  THR A OG1 
218  C CG2 . THR A 53  ? 1.2337 1.0318 0.9204 -0.1675 0.0658  -0.0288 55  THR A CG2 
219  N N   . SER A 54  ? 1.1601 1.0809 0.9538 -0.1435 0.0509  -0.0312 56  SER A N   
220  C CA  . SER A 54  ? 1.0842 1.0404 0.9040 -0.1386 0.0477  -0.0330 56  SER A CA  
221  C C   . SER A 54  ? 1.0451 0.9996 0.8785 -0.1227 0.0439  -0.0286 56  SER A C   
222  O O   . SER A 54  ? 0.9885 0.9200 0.8159 -0.1138 0.0431  -0.0239 56  SER A O   
223  C CB  . SER A 54  ? 1.0553 1.0335 0.8894 -0.1367 0.0462  -0.0345 56  SER A CB  
224  O OG  . SER A 54  ? 0.9997 0.9684 0.8404 -0.1238 0.0429  -0.0301 56  SER A OG  
225  N N   . ASN A 55  ? 1.0105 0.9890 0.8613 -0.1188 0.0416  -0.0299 57  ASN A N   
226  C CA  . ASN A 55  ? 0.8947 0.8705 0.7557 -0.1062 0.0388  -0.0263 57  ASN A CA  
227  C C   . ASN A 55  ? 0.7715 0.7561 0.6504 -0.0924 0.0344  -0.0231 57  ASN A C   
228  O O   . ASN A 55  ? 0.7074 0.7009 0.5994 -0.0834 0.0317  -0.0216 57  ASN A O   
229  C CB  . ASN A 55  ? 0.9155 0.9078 0.7817 -0.1098 0.0387  -0.0290 57  ASN A CB  
230  C CG  . ASN A 55  ? 0.9009 0.8778 0.7641 -0.1035 0.0386  -0.0260 57  ASN A CG  
231  O OD1 . ASN A 55  ? 0.9103 0.8945 0.7733 -0.1075 0.0390  -0.0279 57  ASN A OD1 
232  N ND2 . ASN A 55  ? 0.8587 0.8155 0.7195 -0.0936 0.0380  -0.0212 57  ASN A ND2 
233  N N   . THR A 56  ? 0.7370 0.7179 0.6148 -0.0915 0.0339  -0.0222 58  THR A N   
234  C CA  . THR A 56  ? 0.6478 0.6349 0.5398 -0.0801 0.0299  -0.0193 58  THR A CA  
235  C C   . THR A 56  ? 0.5684 0.5339 0.4556 -0.0726 0.0283  -0.0137 58  THR A C   
236  O O   . THR A 56  ? 0.5460 0.4906 0.4167 -0.0762 0.0307  -0.0124 58  THR A O   
237  C CB  . THR A 56  ? 0.6562 0.6559 0.5519 -0.0827 0.0299  -0.0218 58  THR A CB  
238  O OG1 . THR A 56  ? 0.6663 0.6476 0.5517 -0.0835 0.0300  -0.0193 58  THR A OG1 
239  C CG2 . THR A 56  ? 0.6662 0.6830 0.5594 -0.0938 0.0332  -0.0273 58  THR A CG2 
240  N N   . LEU A 57  ? 0.4960 0.4668 0.3963 -0.0623 0.0245  -0.0105 59  LEU A N   
241  C CA  . LEU A 57  ? 0.4692 0.4265 0.3687 -0.0545 0.0221  -0.0049 59  LEU A CA  
242  C C   . LEU A 57  ? 0.4569 0.4156 0.3584 -0.0536 0.0197  -0.0038 59  LEU A C   
243  O O   . LEU A 57  ? 0.4025 0.3756 0.3139 -0.0523 0.0180  -0.0057 59  LEU A O   
244  C CB  . LEU A 57  ? 0.4421 0.4062 0.3545 -0.0455 0.0195  -0.0022 59  LEU A CB  
245  C CG  . LEU A 57  ? 0.4409 0.3938 0.3524 -0.0379 0.0179  0.0035  59  LEU A CG  
246  C CD1 . LEU A 57  ? 0.4585 0.3936 0.3556 -0.0383 0.0215  0.0048  59  LEU A CD1 
247  C CD2 . LEU A 57  ? 0.4175 0.3804 0.3428 -0.0306 0.0152  0.0058  59  LEU A CD2 
248  N N   . THR A 58  ? 0.4781 0.4210 0.3689 -0.0534 0.0194  -0.0007 60  THR A N   
249  C CA  . THR A 58  ? 0.4904 0.4319 0.3804 -0.0533 0.0169  0.0007  60  THR A CA  
250  C C   . THR A 58  ? 0.5057 0.4386 0.3955 -0.0456 0.0134  0.0070  60  THR A C   
251  O O   . THR A 58  ? 0.4903 0.4144 0.3761 -0.0409 0.0141  0.0101  60  THR A O   
252  C CB  . THR A 58  ? 0.5047 0.4369 0.3799 -0.0624 0.0201  -0.0020 60  THR A CB  
253  O OG1 . THR A 58  ? 0.5339 0.4493 0.3942 -0.0650 0.0233  -0.0015 60  THR A OG1 
254  C CG2 . THR A 58  ? 0.5020 0.4489 0.3801 -0.0700 0.0227  -0.0080 60  THR A CG2 
255  N N   . ASN A 59  ? 0.5301 0.4659 0.4228 -0.0447 0.0100  0.0087  61  ASN A N   
256  C CA  . ASN A 59  ? 0.5377 0.4689 0.4303 -0.0387 0.0058  0.0148  61  ASN A CA  
257  C C   . ASN A 59  ? 0.5112 0.4516 0.4162 -0.0315 0.0039  0.0178  61  ASN A C   
258  O O   . ASN A 59  ? 0.5206 0.4554 0.4232 -0.0255 0.0037  0.0221  61  ASN A O   
259  C CB  . ASN A 59  ? 0.5716 0.4846 0.4478 -0.0384 0.0071  0.0174  61  ASN A CB  
260  C CG  . ASN A 59  ? 0.5887 0.4919 0.4511 -0.0475 0.0103  0.0132  61  ASN A CG  
261  O OD1 . ASN A 59  ? 0.6384 0.5264 0.4858 -0.0505 0.0141  0.0124  61  ASN A OD1 
262  N ND2 . ASN A 59  ? 0.5417 0.4522 0.4073 -0.0525 0.0094  0.0105  61  ASN A ND2 
263  N N   . ILE A 60  ? 0.4726 0.4259 0.3891 -0.0319 0.0029  0.0155  62  ILE A N   
264  C CA  . ILE A 60  ? 0.4462 0.4086 0.3740 -0.0269 0.0019  0.0170  62  ILE A CA  
265  C C   . ILE A 60  ? 0.4491 0.4173 0.3831 -0.0236 -0.0027 0.0219  62  ILE A C   
266  O O   . ILE A 60  ? 0.4588 0.4291 0.3924 -0.0269 -0.0054 0.0217  62  ILE A O   
267  C CB  . ILE A 60  ? 0.4231 0.3946 0.3573 -0.0288 0.0032  0.0122  62  ILE A CB  
268  C CG1 . ILE A 60  ? 0.4166 0.3862 0.3458 -0.0325 0.0077  0.0078  62  ILE A CG1 
269  C CG2 . ILE A 60  ? 0.4031 0.3824 0.3474 -0.0242 0.0016  0.0139  62  ILE A CG2 
270  C CD1 . ILE A 60  ? 0.4102 0.3905 0.3435 -0.0351 0.0089  0.0027  62  ILE A CD1 
271  N N   . GLU A 61  ? 0.4450 0.4155 0.3829 -0.0177 -0.0035 0.0262  63  GLU A N   
272  C CA  . GLU A 61  ? 0.4515 0.4319 0.3971 -0.0148 -0.0078 0.0312  63  GLU A CA  
273  C C   . GLU A 61  ? 0.4236 0.4120 0.3784 -0.0108 -0.0066 0.0319  63  GLU A C   
274  O O   . GLU A 61  ? 0.3890 0.3727 0.3425 -0.0088 -0.0027 0.0297  63  GLU A O   
275  C CB  . GLU A 61  ? 0.5328 0.5095 0.4727 -0.0106 -0.0096 0.0364  63  GLU A CB  
276  C CG  . GLU A 61  ? 0.5945 0.5631 0.5246 -0.0153 -0.0113 0.0359  63  GLU A CG  
277  C CD  . GLU A 61  ? 0.6765 0.6530 0.6095 -0.0199 -0.0164 0.0374  63  GLU A CD  
278  O OE1 . GLU A 61  ? 0.7336 0.7227 0.6761 -0.0196 -0.0191 0.0397  63  GLU A OE1 
279  O OE2 . GLU A 61  ? 0.7408 0.7103 0.6654 -0.0246 -0.0177 0.0365  63  GLU A OE2 
280  N N   . TRP A 62  ? 0.3976 0.3974 0.3606 -0.0108 -0.0099 0.0347  64  TRP A N   
281  C CA  . TRP A 62  ? 0.3793 0.3879 0.3510 -0.0071 -0.0090 0.0363  64  TRP A CA  
282  C C   . TRP A 62  ? 0.4029 0.4120 0.3746 0.0008  -0.0075 0.0408  64  TRP A C   
283  O O   . TRP A 62  ? 0.3915 0.4014 0.3602 0.0032  -0.0099 0.0447  64  TRP A O   
284  C CB  . TRP A 62  ? 0.3620 0.3824 0.3401 -0.0107 -0.0128 0.0384  64  TRP A CB  
285  C CG  . TRP A 62  ? 0.3419 0.3586 0.3170 -0.0173 -0.0136 0.0343  64  TRP A CG  
286  C CD1 . TRP A 62  ? 0.3403 0.3555 0.3105 -0.0233 -0.0168 0.0342  64  TRP A CD1 
287  C CD2 . TRP A 62  ? 0.3190 0.3322 0.2944 -0.0178 -0.0110 0.0299  64  TRP A CD2 
288  N NE1 . TRP A 62  ? 0.3377 0.3472 0.3040 -0.0267 -0.0159 0.0300  64  TRP A NE1 
289  C CE2 . TRP A 62  ? 0.3210 0.3300 0.2907 -0.0230 -0.0125 0.0275  64  TRP A CE2 
290  C CE3 . TRP A 62  ? 0.3015 0.3140 0.2799 -0.0139 -0.0075 0.0280  64  TRP A CE3 
291  C CZ2 . TRP A 62  ? 0.3189 0.3233 0.2861 -0.0230 -0.0107 0.0234  64  TRP A CZ2 
292  C CZ3 . TRP A 62  ? 0.2962 0.3057 0.2732 -0.0150 -0.0062 0.0239  64  TRP A CZ3 
293  C CH2 . TRP A 62  ? 0.3047 0.3104 0.2762 -0.0188 -0.0078 0.0217  64  TRP A CH2 
294  N N   . ALA A 63  ? 0.4209 0.4276 0.3940 0.0052  -0.0035 0.0400  65  ALA A N   
295  C CA  . ALA A 63  ? 0.4502 0.4555 0.4216 0.0143  -0.0010 0.0441  65  ALA A CA  
296  C C   . ALA A 63  ? 0.4679 0.4906 0.4512 0.0179  -0.0022 0.0481  65  ALA A C   
297  O O   . ALA A 63  ? 0.4543 0.4876 0.4452 0.0121  -0.0048 0.0472  65  ALA A O   
298  C CB  . ALA A 63  ? 0.4541 0.4446 0.4174 0.0158  0.0043  0.0408  65  ALA A CB  
299  N N   . PRO A 64  ? 0.5054 0.5316 0.4894 0.0276  -0.0001 0.0527  66  PRO A N   
300  C CA  . PRO A 64  ? 0.5076 0.5545 0.5036 0.0312  -0.0014 0.0572  66  PRO A CA  
301  C C   . PRO A 64  ? 0.4884 0.5400 0.4915 0.0281  0.0008  0.0545  66  PRO A C   
302  O O   . PRO A 64  ? 0.4809 0.5504 0.4939 0.0278  -0.0003 0.0573  66  PRO A O   
303  C CB  . PRO A 64  ? 0.5436 0.5904 0.5363 0.0445  0.0014  0.0625  66  PRO A CB  
304  C CG  . PRO A 64  ? 0.5720 0.5933 0.5476 0.0472  0.0043  0.0606  66  PRO A CG  
305  C CD  . PRO A 64  ? 0.5524 0.5619 0.5240 0.0356  0.0040  0.0537  66  PRO A CD  
306  N N   . GLY A 65  ? 0.4530 0.4894 0.4503 0.0254  0.0040  0.0492  67  GLY A N   
307  C CA  . GLY A 65  ? 0.4410 0.4794 0.4429 0.0227  0.0061  0.0465  67  GLY A CA  
308  C C   . GLY A 65  ? 0.4116 0.4576 0.4184 0.0136  0.0023  0.0445  67  GLY A C   
309  O O   . GLY A 65  ? 0.3969 0.4448 0.4068 0.0114  0.0036  0.0427  67  GLY A O   
310  N N   . VAL A 66  ? 0.3773 0.4253 0.3829 0.0084  -0.0019 0.0446  68  VAL A N   
311  C CA  . VAL A 66  ? 0.3718 0.4234 0.3785 -0.0003 -0.0049 0.0426  68  VAL A CA  
312  C C   . VAL A 66  ? 0.4052 0.4728 0.4169 -0.0038 -0.0091 0.0473  68  VAL A C   
313  O O   . VAL A 66  ? 0.4256 0.4969 0.4370 -0.0012 -0.0112 0.0505  68  VAL A O   
314  C CB  . VAL A 66  ? 0.3495 0.3885 0.3484 -0.0051 -0.0060 0.0380  68  VAL A CB  
315  C CG1 . VAL A 66  ? 0.3440 0.3830 0.3407 -0.0127 -0.0084 0.0361  68  VAL A CG1 
316  C CG2 . VAL A 66  ? 0.3371 0.3642 0.3316 -0.0024 -0.0022 0.0337  68  VAL A CG2 
317  N N   . THR A 67  ? 0.4266 0.5026 0.4413 -0.0101 -0.0103 0.0476  69  THR A N   
318  C CA  . THR A 67  ? 0.4513 0.5452 0.4705 -0.0159 -0.0143 0.0519  69  THR A CA  
319  C C   . THR A 67  ? 0.4807 0.5682 0.4920 -0.0241 -0.0185 0.0507  69  THR A C   
320  O O   . THR A 67  ? 0.4732 0.5429 0.4763 -0.0252 -0.0176 0.0460  69  THR A O   
321  C CB  . THR A 67  ? 0.4404 0.5437 0.4629 -0.0220 -0.0136 0.0522  69  THR A CB  
322  O OG1 . THR A 67  ? 0.4394 0.5264 0.4520 -0.0292 -0.0135 0.0473  69  THR A OG1 
323  C CG2 . THR A 67  ? 0.4324 0.5415 0.4620 -0.0141 -0.0090 0.0532  69  THR A CG2 
324  N N   . GLU A 68  ? 0.5302 0.6330 0.5440 -0.0294 -0.0228 0.0548  70  GLU A N   
325  C CA  . GLU A 68  ? 0.5528 0.6500 0.5580 -0.0378 -0.0272 0.0543  70  GLU A CA  
326  C C   . GLU A 68  ? 0.5248 0.6083 0.5195 -0.0477 -0.0268 0.0500  70  GLU A C   
327  O O   . GLU A 68  ? 0.5155 0.5838 0.4992 -0.0520 -0.0281 0.0472  70  GLU A O   
328  C CB  . GLU A 68  ? 0.6247 0.7434 0.6350 -0.0410 -0.0321 0.0601  70  GLU A CB  
329  C CG  . GLU A 68  ? 0.6875 0.8076 0.6989 -0.0327 -0.0338 0.0630  70  GLU A CG  
330  C CD  . GLU A 68  ? 0.7401 0.8394 0.7399 -0.0347 -0.0347 0.0596  70  GLU A CD  
331  O OE1 . GLU A 68  ? 0.8021 0.8899 0.7928 -0.0442 -0.0356 0.0561  70  GLU A OE1 
332  O OE2 . GLU A 68  ? 0.7816 0.8752 0.7800 -0.0267 -0.0341 0.0605  70  GLU A OE2 
333  N N   . ALA A 69  ? 0.4878 0.5743 0.4842 -0.0502 -0.0247 0.0493  71  ALA A N   
334  C CA  . ALA A 69  ? 0.4816 0.5523 0.4654 -0.0584 -0.0237 0.0454  71  ALA A CA  
335  C C   . ALA A 69  ? 0.4589 0.5082 0.4358 -0.0520 -0.0206 0.0401  71  ALA A C   
336  O O   . ALA A 69  ? 0.4407 0.4732 0.4041 -0.0562 -0.0209 0.0369  71  ALA A O   
337  C CB  . ALA A 69  ? 0.4917 0.5714 0.4795 -0.0613 -0.0217 0.0463  71  ALA A CB  
338  N N   . GLY A 70  ? 0.4444 0.4949 0.4296 -0.0419 -0.0176 0.0394  72  GLY A N   
339  C CA  . GLY A 70  ? 0.4265 0.4616 0.4072 -0.0359 -0.0149 0.0348  72  GLY A CA  
340  C C   . GLY A 70  ? 0.4083 0.4364 0.3836 -0.0361 -0.0165 0.0336  72  GLY A C   
341  O O   . GLY A 70  ? 0.3930 0.4074 0.3587 -0.0369 -0.0157 0.0297  72  GLY A O   
342  N N   . ARG A 71  ? 0.4165 0.4536 0.3973 -0.0345 -0.0184 0.0370  73  ARG A N   
343  C CA  . ARG A 71  ? 0.4283 0.4591 0.4039 -0.0349 -0.0200 0.0363  73  ARG A CA  
344  C C   . ARG A 71  ? 0.4467 0.4685 0.4107 -0.0432 -0.0222 0.0348  73  ARG A C   
345  O O   . ARG A 71  ? 0.4669 0.4767 0.4232 -0.0426 -0.0212 0.0314  73  ARG A O   
346  C CB  . ARG A 71  ? 0.4300 0.4722 0.4111 -0.0331 -0.0227 0.0413  73  ARG A CB  
347  C CG  . ARG A 71  ? 0.4341 0.4810 0.4229 -0.0237 -0.0199 0.0429  73  ARG A CG  
348  C CD  . ARG A 71  ? 0.4538 0.5132 0.4475 -0.0198 -0.0223 0.0486  73  ARG A CD  
349  N NE  . ARG A 71  ? 0.4578 0.5187 0.4564 -0.0101 -0.0185 0.0499  73  ARG A NE  
350  C CZ  . ARG A 71  ? 0.4721 0.5338 0.4703 -0.0023 -0.0181 0.0533  73  ARG A CZ  
351  N NH1 . ARG A 71  ? 0.4822 0.5447 0.4764 -0.0029 -0.0217 0.0559  73  ARG A NH1 
352  N NH2 . ARG A 71  ? 0.4827 0.5421 0.4824 0.0063  -0.0139 0.0540  73  ARG A NH2 
353  N N   . THR A 72  ? 0.4799 0.5071 0.4415 -0.0510 -0.0247 0.0372  74  THR A N   
354  C CA  . THR A 72  ? 0.5086 0.5244 0.4554 -0.0605 -0.0266 0.0359  74  THR A CA  
355  C C   . THR A 72  ? 0.4987 0.4959 0.4347 -0.0583 -0.0230 0.0308  74  THR A C   
356  O O   . THR A 72  ? 0.5098 0.4929 0.4342 -0.0590 -0.0226 0.0280  74  THR A O   
357  C CB  . THR A 72  ? 0.5329 0.5573 0.4775 -0.0709 -0.0293 0.0390  74  THR A CB  
358  O OG1 . THR A 72  ? 0.5568 0.6029 0.5136 -0.0710 -0.0326 0.0442  74  THR A OG1 
359  C CG2 . THR A 72  ? 0.5535 0.5625 0.4792 -0.0816 -0.0310 0.0376  74  THR A CG2 
360  N N   . HIS A 73  ? 0.4682 0.4661 0.4077 -0.0550 -0.0205 0.0297  75  HIS A N   
361  C CA  . HIS A 73  ? 0.4699 0.4516 0.3987 -0.0523 -0.0174 0.0255  75  HIS A CA  
362  C C   . HIS A 73  ? 0.4312 0.4065 0.3597 -0.0439 -0.0151 0.0218  75  HIS A C   
363  O O   . HIS A 73  ? 0.4286 0.3892 0.3438 -0.0428 -0.0137 0.0187  75  HIS A O   
364  C CB  . HIS A 73  ? 0.4776 0.4637 0.4121 -0.0499 -0.0154 0.0257  75  HIS A CB  
365  C CG  . HIS A 73  ? 0.4877 0.4580 0.4117 -0.0451 -0.0124 0.0216  75  HIS A CG  
366  N ND1 . HIS A 73  ? 0.5221 0.4748 0.4273 -0.0500 -0.0121 0.0202  75  HIS A ND1 
367  C CD2 . HIS A 73  ? 0.5010 0.4693 0.4283 -0.0357 -0.0099 0.0186  75  HIS A CD2 
368  C CE1 . HIS A 73  ? 0.5435 0.4843 0.4413 -0.0422 -0.0094 0.0168  75  HIS A CE1 
369  N NE2 . HIS A 73  ? 0.5505 0.5025 0.4629 -0.0335 -0.0082 0.0157  75  HIS A NE2 
370  N N   . PHE A 74  ? 0.3960 0.3817 0.3375 -0.0380 -0.0143 0.0222  76  PHE A N   
371  C CA  . PHE A 74  ? 0.3781 0.3610 0.3205 -0.0312 -0.0118 0.0185  76  PHE A CA  
372  C C   . PHE A 74  ? 0.3751 0.3544 0.3126 -0.0332 -0.0127 0.0180  76  PHE A C   
373  O O   . PHE A 74  ? 0.3615 0.3371 0.2962 -0.0292 -0.0104 0.0144  76  PHE A O   
374  C CB  . PHE A 74  ? 0.3603 0.3530 0.3153 -0.0258 -0.0101 0.0188  76  PHE A CB  
375  C CG  . PHE A 74  ? 0.3384 0.3330 0.2972 -0.0228 -0.0084 0.0184  76  PHE A CG  
376  C CD1 . PHE A 74  ? 0.3403 0.3273 0.2924 -0.0198 -0.0067 0.0151  76  PHE A CD1 
377  C CD2 . PHE A 74  ? 0.3308 0.3346 0.2989 -0.0222 -0.0083 0.0216  76  PHE A CD2 
378  C CE1 . PHE A 74  ? 0.3403 0.3280 0.2947 -0.0172 -0.0052 0.0148  76  PHE A CE1 
379  C CE2 . PHE A 74  ? 0.3280 0.3327 0.2989 -0.0196 -0.0063 0.0210  76  PHE A CE2 
380  C CZ  . PHE A 74  ? 0.3195 0.3158 0.2834 -0.0176 -0.0050 0.0176  76  PHE A CZ  
381  N N   . GLY A 75  ? 0.3734 0.3554 0.3101 -0.0393 -0.0160 0.0214  77  GLY A N   
382  C CA  . GLY A 75  ? 0.3877 0.3652 0.3182 -0.0423 -0.0173 0.0214  77  GLY A CA  
383  C C   . GLY A 75  ? 0.3779 0.3619 0.3164 -0.0388 -0.0168 0.0219  77  GLY A C   
384  O O   . GLY A 75  ? 0.3746 0.3676 0.3233 -0.0352 -0.0164 0.0238  77  GLY A O   
385  N N   . ASN A 76  ? 0.3940 0.3722 0.3262 -0.0401 -0.0166 0.0204  78  ASN A N   
386  C CA  . ASN A 76  ? 0.3774 0.3578 0.3127 -0.0381 -0.0158 0.0204  78  ASN A CA  
387  C C   . ASN A 76  ? 0.3546 0.3391 0.2972 -0.0325 -0.0122 0.0182  78  ASN A C   
388  O O   . ASN A 76  ? 0.3566 0.3396 0.2979 -0.0300 -0.0095 0.0142  78  ASN A O   
389  C CB  . ASN A 76  ? 0.3976 0.3696 0.3233 -0.0403 -0.0146 0.0175  78  ASN A CB  
390  C CG  . ASN A 76  ? 0.3855 0.3581 0.3123 -0.0397 -0.0135 0.0175  78  ASN A CG  
391  O OD1 . ASN A 76  ? 0.3863 0.3591 0.3138 -0.0375 -0.0099 0.0139  78  ASN A OD1 
392  N ND2 . ASN A 76  ? 0.4152 0.3889 0.3421 -0.0415 -0.0169 0.0218  78  ASN A ND2 
393  N N   . ALA A 77  ? 0.3329 0.3216 0.2810 -0.0303 -0.0122 0.0206  79  ALA A N   
394  C CA  . ALA A 77  ? 0.3182 0.3092 0.2713 -0.0259 -0.0088 0.0192  79  ALA A CA  
395  C C   . ALA A 77  ? 0.3056 0.2933 0.2545 -0.0266 -0.0055 0.0143  79  ALA A C   
396  O O   . ALA A 77  ? 0.2761 0.2667 0.2275 -0.0246 -0.0030 0.0112  79  ALA A O   
397  C CB  . ALA A 77  ? 0.3251 0.3176 0.2809 -0.0232 -0.0092 0.0232  79  ALA A CB  
398  N N   . SER A 78  ? 0.3072 0.2900 0.2496 -0.0298 -0.0055 0.0138  80  SER A N   
399  C CA  . SER A 78  ? 0.3146 0.2960 0.2525 -0.0317 -0.0019 0.0093  80  SER A CA  
400  C C   . SER A 78  ? 0.3148 0.3000 0.2526 -0.0308 -0.0005 0.0052  80  SER A C   
401  O O   . SER A 78  ? 0.3173 0.3079 0.2561 -0.0303 0.0026  0.0013  80  SER A O   
402  C CB  . SER A 78  ? 0.3401 0.3144 0.2698 -0.0358 -0.0023 0.0099  80  SER A CB  
403  O OG  . SER A 78  ? 0.3447 0.3177 0.2698 -0.0387 0.0015  0.0061  80  SER A OG  
404  N N   . ASP A 79  ? 0.3352 0.3174 0.2702 -0.0306 -0.0026 0.0061  81  ASP A N   
405  C CA  . ASP A 79  ? 0.3512 0.3337 0.2827 -0.0279 -0.0010 0.0026  81  ASP A CA  
406  C C   . ASP A 79  ? 0.3322 0.3200 0.2694 -0.0230 -0.0002 0.0017  81  ASP A C   
407  O O   . ASP A 79  ? 0.3161 0.3081 0.2524 -0.0190 0.0021  -0.0017 81  ASP A O   
408  C CB  . ASP A 79  ? 0.3885 0.3618 0.3114 -0.0296 -0.0031 0.0040  81  ASP A CB  
409  C CG  . ASP A 79  ? 0.4290 0.3955 0.3438 -0.0345 -0.0038 0.0044  81  ASP A CG  
410  O OD1 . ASP A 79  ? 0.4359 0.4047 0.3502 -0.0358 -0.0015 0.0023  81  ASP A OD1 
411  O OD2 . ASP A 79  ? 0.4668 0.4253 0.3744 -0.0378 -0.0066 0.0068  81  ASP A OD2 
412  N N   . LYS A 80  ? 0.3170 0.3052 0.2595 -0.0227 -0.0022 0.0050  82  LYS A N   
413  C CA  . LYS A 80  ? 0.3028 0.2954 0.2504 -0.0185 -0.0013 0.0042  82  LYS A CA  
414  C C   . LYS A 80  ? 0.3000 0.3004 0.2522 -0.0171 0.0014  0.0013  82  LYS A C   
415  O O   . LYS A 80  ? 0.3022 0.3081 0.2552 -0.0131 0.0030  -0.0017 82  LYS A O   
416  C CB  . LYS A 80  ? 0.2904 0.2830 0.2429 -0.0190 -0.0034 0.0083  82  LYS A CB  
417  C CG  . LYS A 80  ? 0.2883 0.2837 0.2447 -0.0152 -0.0025 0.0076  82  LYS A CG  
418  C CD  . LYS A 80  ? 0.2916 0.2823 0.2414 -0.0124 -0.0022 0.0055  82  LYS A CD  
419  C CE  . LYS A 80  ? 0.2926 0.2852 0.2456 -0.0088 -0.0015 0.0052  82  LYS A CE  
420  N NZ  . LYS A 80  ? 0.3033 0.2880 0.2474 -0.0058 -0.0015 0.0041  82  LYS A NZ  
421  N N   . ALA A 81  ? 0.3013 0.3017 0.2548 -0.0203 0.0020  0.0023  83  ALA A N   
422  C CA  . ALA A 81  ? 0.3043 0.3097 0.2585 -0.0218 0.0050  -0.0006 83  ALA A CA  
423  C C   . ALA A 81  ? 0.3145 0.3275 0.2667 -0.0220 0.0070  -0.0051 83  ALA A C   
424  O O   . ALA A 81  ? 0.3256 0.3480 0.2806 -0.0208 0.0087  -0.0080 83  ALA A O   
425  C CB  . ALA A 81  ? 0.3092 0.3084 0.2598 -0.0259 0.0056  0.0011  83  ALA A CB  
426  N N   . ALA A 82  ? 0.3221 0.3321 0.2694 -0.0232 0.0068  -0.0056 84  ALA A N   
427  C CA  . ALA A 82  ? 0.3346 0.3526 0.2795 -0.0227 0.0094  -0.0097 84  ALA A CA  
428  C C   . ALA A 82  ? 0.3379 0.3633 0.2848 -0.0152 0.0098  -0.0116 84  ALA A C   
429  O O   . ALA A 82  ? 0.3393 0.3784 0.2886 -0.0137 0.0121  -0.0150 84  ALA A O   
430  C CB  . ALA A 82  ? 0.3567 0.3671 0.2945 -0.0249 0.0091  -0.0093 84  ALA A CB  
431  N N   . SER A 83  ? 0.3442 0.3615 0.2892 -0.0107 0.0077  -0.0094 85  SER A N   
432  C CA  . SER A 83  ? 0.3561 0.3768 0.3000 -0.0026 0.0081  -0.0109 85  SER A CA  
433  C C   . SER A 83  ? 0.3448 0.3770 0.2962 -0.0009 0.0085  -0.0121 85  SER A C   
434  O O   . SER A 83  ? 0.3563 0.3965 0.3076 0.0058  0.0093  -0.0141 85  SER A O   
435  C CB  . SER A 83  ? 0.3627 0.3689 0.3002 -0.0003 0.0060  -0.0082 85  SER A CB  
436  O OG  . SER A 83  ? 0.3511 0.3548 0.2940 -0.0030 0.0040  -0.0053 85  SER A OG  
437  N N   . LEU A 84  ? 0.3509 0.3833 0.3073 -0.0064 0.0081  -0.0108 86  LEU A N   
438  C CA  . LEU A 84  ? 0.3457 0.3865 0.3075 -0.0060 0.0086  -0.0117 86  LEU A CA  
439  C C   . LEU A 84  ? 0.3591 0.4130 0.3226 -0.0111 0.0109  -0.0150 86  LEU A C   
440  O O   . LEU A 84  ? 0.3827 0.4456 0.3493 -0.0118 0.0114  -0.0164 86  LEU A O   
441  C CB  . LEU A 84  ? 0.3421 0.3737 0.3059 -0.0089 0.0075  -0.0084 86  LEU A CB  
442  C CG  . LEU A 84  ? 0.3276 0.3502 0.2911 -0.0052 0.0054  -0.0053 86  LEU A CG  
443  C CD1 . LEU A 84  ? 0.3223 0.3389 0.2887 -0.0080 0.0049  -0.0019 86  LEU A CD1 
444  C CD2 . LEU A 84  ? 0.3273 0.3537 0.2910 0.0006  0.0053  -0.0067 86  LEU A CD2 
445  N N   . SER A 85  ? 0.3734 0.4280 0.3340 -0.0157 0.0123  -0.0161 87  SER A N   
446  C CA  . SER A 85  ? 0.3777 0.4427 0.3377 -0.0233 0.0149  -0.0192 87  SER A CA  
447  C C   . SER A 85  ? 0.3876 0.4741 0.3516 -0.0200 0.0161  -0.0228 87  SER A C   
448  O O   . SER A 85  ? 0.3917 0.4831 0.3560 -0.0116 0.0159  -0.0234 87  SER A O   
449  C CB  . SER A 85  ? 0.3855 0.4455 0.3404 -0.0281 0.0162  -0.0195 87  SER A CB  
450  O OG  . SER A 85  ? 0.3929 0.4569 0.3448 -0.0376 0.0187  -0.0216 87  SER A OG  
451  N N   . GLY A 86  ? 0.3965 0.4945 0.3620 -0.0263 0.0174  -0.0250 88  GLY A N   
452  C CA  . GLY A 86  ? 0.4275 0.5502 0.3977 -0.0243 0.0181  -0.0283 88  GLY A CA  
453  C C   . GLY A 86  ? 0.4509 0.5779 0.4251 -0.0146 0.0157  -0.0274 88  GLY A C   
454  O O   . GLY A 86  ? 0.4797 0.6280 0.4578 -0.0129 0.0159  -0.0297 88  GLY A O   
455  N N   . LYS A 87  ? 0.4723 0.5816 0.4452 -0.0082 0.0137  -0.0242 89  LYS A N   
456  C CA  . LYS A 87  ? 0.4846 0.5965 0.4593 0.0009  0.0117  -0.0235 89  LYS A CA  
457  C C   . LYS A 87  ? 0.4860 0.6053 0.4631 -0.0044 0.0113  -0.0243 89  LYS A C   
458  O O   . LYS A 87  ? 0.4521 0.5654 0.4274 -0.0146 0.0126  -0.0243 89  LYS A O   
459  C CB  . LYS A 87  ? 0.5034 0.5937 0.4747 0.0061  0.0099  -0.0199 89  LYS A CB  
460  C CG  . LYS A 87  ? 0.5385 0.6181 0.5047 0.0108  0.0099  -0.0188 89  LYS A CG  
461  C CD  . LYS A 87  ? 0.5652 0.6540 0.5285 0.0214  0.0105  -0.0205 89  LYS A CD  
462  C CE  . LYS A 87  ? 0.5859 0.6636 0.5417 0.0244  0.0114  -0.0200 89  LYS A CE  
463  N NZ  . LYS A 87  ? 0.6155 0.7100 0.5710 0.0296  0.0139  -0.0229 89  LYS A NZ  
464  N N   . GLN A 88  ? 0.5036 0.6338 0.4828 0.0024  0.0098  -0.0249 90  GLN A N   
465  C CA  . GLN A 88  ? 0.5117 0.6495 0.4922 -0.0025 0.0092  -0.0258 90  GLN A CA  
466  C C   . GLN A 88  ? 0.4887 0.6037 0.4662 -0.0056 0.0090  -0.0230 90  GLN A C   
467  O O   . GLN A 88  ? 0.4339 0.5320 0.4100 -0.0004 0.0083  -0.0202 90  GLN A O   
468  C CB  . GLN A 88  ? 0.5520 0.7067 0.5347 0.0069  0.0072  -0.0266 90  GLN A CB  
469  C CG  . GLN A 88  ? 0.5832 0.7665 0.5698 0.0098  0.0076  -0.0295 90  GLN A CG  
470  C CD  . GLN A 88  ? 0.6079 0.8091 0.5967 -0.0041 0.0091  -0.0324 90  GLN A CD  
471  O OE1 . GLN A 88  ? 0.6582 0.8528 0.6445 -0.0140 0.0091  -0.0324 90  GLN A OE1 
472  N NE2 . GLN A 88  ? 0.5996 0.8220 0.5916 -0.0057 0.0108  -0.0348 90  GLN A NE2 
473  N N   . ASN A 89  ? 0.4928 0.6084 0.4685 -0.0143 0.0098  -0.0238 91  ASN A N   
474  C CA  . ASN A 89  ? 0.5112 0.6075 0.4831 -0.0176 0.0105  -0.0215 91  ASN A CA  
475  C C   . ASN A 89  ? 0.4932 0.5828 0.4663 -0.0084 0.0085  -0.0194 91  ASN A C   
476  O O   . ASN A 89  ? 0.4637 0.5356 0.4355 -0.0070 0.0089  -0.0165 91  ASN A O   
477  C CB  . ASN A 89  ? 0.5076 0.6078 0.4746 -0.0287 0.0122  -0.0236 91  ASN A CB  
478  C CG  . ASN A 89  ? 0.5104 0.6072 0.4721 -0.0390 0.0149  -0.0249 91  ASN A CG  
479  O OD1 . ASN A 89  ? 0.4844 0.5706 0.4458 -0.0376 0.0156  -0.0233 91  ASN A OD1 
480  N ND2 . ASN A 89  ? 0.4997 0.6045 0.4557 -0.0501 0.0165  -0.0278 91  ASN A ND2 
481  N N   . ASP A 90  ? 0.4972 0.6009 0.4722 -0.0018 0.0065  -0.0207 92  ASP A N   
482  C CA  . ASP A 90  ? 0.5111 0.6079 0.4848 0.0069  0.0046  -0.0190 92  ASP A CA  
483  C C   . ASP A 90  ? 0.4763 0.5710 0.4491 0.0173  0.0035  -0.0182 92  ASP A C   
484  O O   . ASP A 90  ? 0.4833 0.5764 0.4529 0.0259  0.0019  -0.0176 92  ASP A O   
485  C CB  . ASP A 90  ? 0.5277 0.6391 0.5011 0.0068  0.0032  -0.0209 92  ASP A CB  
486  C CG  . ASP A 90  ? 0.5714 0.7097 0.5481 0.0090  0.0020  -0.0236 92  ASP A CG  
487  O OD1 . ASP A 90  ? 0.6106 0.7558 0.5896 0.0109  0.0028  -0.0244 92  ASP A OD1 
488  O OD2 . ASP A 90  ? 0.5903 0.7443 0.5673 0.0088  0.0003  -0.0250 92  ASP A OD2 
489  N N   . SER A 91  ? 0.4632 0.5570 0.4367 0.0167  0.0044  -0.0183 93  SER A N   
490  C CA  . SER A 91  ? 0.4871 0.5786 0.4571 0.0266  0.0038  -0.0179 93  SER A CA  
491  C C   . SER A 91  ? 0.4900 0.5590 0.4541 0.0300  0.0032  -0.0149 93  SER A C   
492  O O   . SER A 91  ? 0.4752 0.5331 0.4409 0.0237  0.0036  -0.0130 93  SER A O   
493  C CB  . SER A 91  ? 0.4867 0.5826 0.4577 0.0245  0.0052  -0.0189 93  SER A CB  
494  O OG  . SER A 91  ? 0.4770 0.5579 0.4478 0.0173  0.0061  -0.0171 93  SER A OG  
495  N N   . ALA A 92  ? 0.4967 0.5593 0.4532 0.0397  0.0025  -0.0145 94  ALA A N   
496  C CA  . ALA A 92  ? 0.4808 0.5211 0.4286 0.0421  0.0022  -0.0121 94  ALA A CA  
497  C C   . ALA A 92  ? 0.4310 0.4611 0.3802 0.0342  0.0029  -0.0103 94  ALA A C   
498  O O   . ALA A 92  ? 0.4178 0.4348 0.3652 0.0308  0.0026  -0.0080 94  ALA A O   
499  C CB  . ALA A 92  ? 0.5073 0.5413 0.4434 0.0531  0.0022  -0.0124 94  ALA A CB  
500  N N   . GLU A 93  ? 0.4461 0.4829 0.3982 0.0317  0.0037  -0.0114 95  GLU A N   
501  C CA  . GLU A 93  ? 0.4302 0.4574 0.3821 0.0251  0.0039  -0.0096 95  GLU A CA  
502  C C   . GLU A 93  ? 0.3728 0.3985 0.3320 0.0170  0.0039  -0.0077 95  GLU A C   
503  O O   . GLU A 93  ? 0.3497 0.3646 0.3076 0.0138  0.0033  -0.0050 95  GLU A O   
504  C CB  . GLU A 93  ? 0.4899 0.5252 0.4425 0.0244  0.0051  -0.0115 95  GLU A CB  
505  C CG  . GLU A 93  ? 0.5533 0.5876 0.4970 0.0336  0.0058  -0.0129 95  GLU A CG  
506  C CD  . GLU A 93  ? 0.6504 0.7032 0.5961 0.0417  0.0064  -0.0156 95  GLU A CD  
507  O OE1 . GLU A 93  ? 0.7105 0.7760 0.6634 0.0404  0.0057  -0.0164 95  GLU A OE1 
508  O OE2 . GLU A 93  ? 0.7215 0.7769 0.6610 0.0498  0.0076  -0.0168 95  GLU A OE2 
509  N N   . VAL A 94  ? 0.3479 0.3839 0.3131 0.0141  0.0047  -0.0090 96  VAL A N   
510  C CA  . VAL A 94  ? 0.3409 0.3735 0.3104 0.0076  0.0054  -0.0072 96  VAL A CA  
511  C C   . VAL A 94  ? 0.3296 0.3537 0.2985 0.0092  0.0051  -0.0050 96  VAL A C   
512  O O   . VAL A 94  ? 0.3109 0.3281 0.2816 0.0062  0.0054  -0.0021 96  VAL A O   
513  C CB  . VAL A 94  ? 0.3641 0.4071 0.3362 0.0034  0.0068  -0.0095 96  VAL A CB  
514  C CG1 . VAL A 94  ? 0.3641 0.3999 0.3369 -0.0023 0.0084  -0.0077 96  VAL A CG1 
515  C CG2 . VAL A 94  ? 0.3861 0.4394 0.3584 0.0012  0.0075  -0.0121 96  VAL A CG2 
516  N N   . LYS A 95  ? 0.3264 0.3524 0.2928 0.0141  0.0046  -0.0062 97  LYS A N   
517  C CA  . LYS A 95  ? 0.3347 0.3517 0.2985 0.0159  0.0044  -0.0044 97  LYS A CA  
518  C C   . LYS A 95  ? 0.3197 0.3251 0.2800 0.0150  0.0038  -0.0017 97  LYS A C   
519  O O   . LYS A 95  ? 0.3118 0.3125 0.2744 0.0119  0.0044  0.0007  97  LYS A O   
520  C CB  . LYS A 95  ? 0.3727 0.3912 0.3309 0.0229  0.0034  -0.0061 97  LYS A CB  
521  C CG  . LYS A 95  ? 0.3959 0.4211 0.3561 0.0229  0.0036  -0.0073 97  LYS A CG  
522  C CD  . LYS A 95  ? 0.4263 0.4685 0.3894 0.0231  0.0032  -0.0103 97  LYS A CD  
523  C CE  . LYS A 95  ? 0.4477 0.4959 0.4096 0.0245  0.0025  -0.0115 97  LYS A CE  
524  N NZ  . LYS A 95  ? 0.4759 0.5390 0.4417 0.0183  0.0030  -0.0138 97  LYS A NZ  
525  N N   . ALA A 96  ? 0.3064 0.3077 0.2604 0.0173  0.0029  -0.0021 98  ALA A N   
526  C CA  . ALA A 96  ? 0.3042 0.2928 0.2510 0.0155  0.0022  0.0000  98  ALA A CA  
527  C C   . ALA A 96  ? 0.2971 0.2872 0.2504 0.0086  0.0020  0.0025  98  ALA A C   
528  O O   . ALA A 96  ? 0.3039 0.2888 0.2564 0.0048  0.0016  0.0052  98  ALA A O   
529  C CB  . ALA A 96  ? 0.3164 0.2985 0.2523 0.0200  0.0018  -0.0014 98  ALA A CB  
530  N N   . PHE A 97  ? 0.2878 0.2852 0.2465 0.0069  0.0022  0.0018  99  PHE A N   
531  C CA  . PHE A 97  ? 0.2792 0.2786 0.2438 0.0017  0.0019  0.0045  99  PHE A CA  
532  C C   . PHE A 97  ? 0.2694 0.2706 0.2402 0.0005  0.0030  0.0069  99  PHE A C   
533  O O   . PHE A 97  ? 0.2659 0.2663 0.2387 -0.0021 0.0024  0.0101  99  PHE A O   
534  C CB  . PHE A 97  ? 0.2741 0.2794 0.2413 0.0005  0.0025  0.0029  99  PHE A CB  
535  C CG  . PHE A 97  ? 0.2764 0.2813 0.2465 -0.0037 0.0020  0.0056  99  PHE A CG  
536  C CD1 . PHE A 97  ? 0.2847 0.2857 0.2530 -0.0063 0.0000  0.0085  99  PHE A CD1 
537  C CD2 . PHE A 97  ? 0.2753 0.2833 0.2481 -0.0054 0.0033  0.0053  99  PHE A CD2 
538  C CE1 . PHE A 97  ? 0.2856 0.2879 0.2564 -0.0094 -0.0009 0.0113  99  PHE A CE1 
539  C CE2 . PHE A 97  ? 0.2847 0.2909 0.2581 -0.0081 0.0027  0.0080  99  PHE A CE2 
540  C CZ  . PHE A 97  ? 0.2747 0.2791 0.2480 -0.0095 0.0004  0.0112  99  PHE A CZ  
541  N N   . ALA A 98  ? 0.2704 0.2747 0.2435 0.0025  0.0046  0.0053  100 ALA A N   
542  C CA  . ALA A 98  ? 0.2729 0.2771 0.2500 0.0023  0.0065  0.0073  100 ALA A CA  
543  C C   . ALA A 98  ? 0.2819 0.2824 0.2578 0.0023  0.0061  0.0093  100 ALA A C   
544  O O   . ALA A 98  ? 0.2888 0.2909 0.2690 0.0011  0.0071  0.0125  100 ALA A O   
545  C CB  . ALA A 98  ? 0.2718 0.2778 0.2484 0.0036  0.0082  0.0047  100 ALA A CB  
546  N N   . GLN A 99  ? 0.2867 0.2823 0.2559 0.0040  0.0051  0.0077  101 GLN A N   
547  C CA  . GLN A 99  ? 0.3026 0.2921 0.2676 0.0027  0.0051  0.0093  101 GLN A CA  
548  C C   . GLN A 99  ? 0.2988 0.2880 0.2635 -0.0023 0.0038  0.0121  101 GLN A C   
549  O O   . GLN A 99  ? 0.2901 0.2822 0.2584 -0.0053 0.0045  0.0149  101 GLN A O   
550  C CB  . GLN A 99  ? 0.3317 0.3125 0.2859 0.0061  0.0046  0.0070  101 GLN A CB  
551  C CG  . GLN A 99  ? 0.3529 0.3351 0.3070 0.0106  0.0056  0.0049  101 GLN A CG  
552  C CD  . GLN A 99  ? 0.3726 0.3553 0.3307 0.0093  0.0076  0.0063  101 GLN A CD  
553  O OE1 . GLN A 99  ? 0.3979 0.3758 0.3538 0.0066  0.0084  0.0083  101 GLN A OE1 
554  N NE2 . GLN A 99  ? 0.3473 0.3355 0.3103 0.0105  0.0088  0.0052  101 GLN A NE2 
555  N N   . GLU A 100 ? 0.3141 0.3011 0.2748 -0.0036 0.0020  0.0115  102 GLU A N   
556  C CA  . GLU A 100 ? 0.3286 0.3140 0.2863 -0.0097 0.0003  0.0140  102 GLU A CA  
557  C C   . GLU A 100 ? 0.3093 0.3061 0.2781 -0.0121 0.0000  0.0174  102 GLU A C   
558  O O   . GLU A 100 ? 0.3125 0.3134 0.2825 -0.0173 -0.0011 0.0204  102 GLU A O   
559  C CB  . GLU A 100 ? 0.3696 0.3465 0.3169 -0.0103 -0.0010 0.0124  102 GLU A CB  
560  C CG  . GLU A 100 ? 0.4128 0.3847 0.3529 -0.0182 -0.0027 0.0147  102 GLU A CG  
561  C CD  . GLU A 100 ? 0.4654 0.4269 0.3936 -0.0191 -0.0038 0.0132  102 GLU A CD  
562  O OE1 . GLU A 100 ? 0.4835 0.4471 0.4140 -0.0138 -0.0033 0.0110  102 GLU A OE1 
563  O OE2 . GLU A 100 ? 0.5537 0.5056 0.4699 -0.0260 -0.0049 0.0143  102 GLU A OE2 
564  N N   . LEU A 101 ? 0.2898 0.2920 0.2656 -0.0084 0.0010  0.0169  103 LEU A N   
565  C CA  . LEU A 101 ? 0.2866 0.2973 0.2707 -0.0085 0.0012  0.0203  103 LEU A CA  
566  C C   . LEU A 101 ? 0.3033 0.3203 0.2928 -0.0086 0.0025  0.0235  103 LEU A C   
567  O O   . LEU A 101 ? 0.3112 0.3371 0.3061 -0.0101 0.0016  0.0273  103 LEU A O   
568  C CB  . LEU A 101 ? 0.2776 0.2881 0.2640 -0.0046 0.0031  0.0188  103 LEU A CB  
569  C CG  . LEU A 101 ? 0.2669 0.2763 0.2512 -0.0056 0.0019  0.0177  103 LEU A CG  
570  C CD1 . LEU A 101 ? 0.2583 0.2661 0.2421 -0.0035 0.0043  0.0157  103 LEU A CD1 
571  C CD2 . LEU A 101 ? 0.2770 0.2907 0.2637 -0.0076 0.0000  0.0217  103 LEU A CD2 
572  N N   . ASN A 102 ? 0.3265 0.3398 0.3145 -0.0069 0.0046  0.0220  104 ASN A N   
573  C CA  . ASN A 102 ? 0.3435 0.3625 0.3369 -0.0056 0.0072  0.0244  104 ASN A CA  
574  C C   . ASN A 102 ? 0.3797 0.4078 0.3759 -0.0109 0.0059  0.0280  104 ASN A C   
575  O O   . ASN A 102 ? 0.3811 0.4207 0.3853 -0.0092 0.0074  0.0316  104 ASN A O   
576  C CB  . ASN A 102 ? 0.3325 0.3441 0.3214 -0.0040 0.0093  0.0218  104 ASN A CB  
577  C CG  . ASN A 102 ? 0.3355 0.3522 0.3294 -0.0023 0.0125  0.0241  104 ASN A CG  
578  O OD1 . ASN A 102 ? 0.3319 0.3532 0.3313 0.0017  0.0146  0.0260  104 ASN A OD1 
579  N ND2 . ASN A 102 ? 0.3402 0.3552 0.3310 -0.0052 0.0134  0.0242  104 ASN A ND2 
580  N N   . GLN A 103 ? 0.4157 0.4393 0.4046 -0.0173 0.0034  0.0273  105 GLN A N   
581  C CA  . GLN A 103 ? 0.4444 0.4770 0.4340 -0.0249 0.0020  0.0305  105 GLN A CA  
582  C C   . GLN A 103 ? 0.4165 0.4623 0.4134 -0.0259 -0.0005 0.0341  105 GLN A C   
583  O O   . GLN A 103 ? 0.4233 0.4821 0.4238 -0.0317 -0.0018 0.0374  105 GLN A O   
584  C CB  . GLN A 103 ? 0.4872 0.5066 0.4624 -0.0322 0.0006  0.0283  105 GLN A CB  
585  C CG  . GLN A 103 ? 0.5093 0.5208 0.4767 -0.0347 -0.0023 0.0271  105 GLN A CG  
586  C CD  . GLN A 103 ? 0.5509 0.5423 0.5014 -0.0356 -0.0022 0.0234  105 GLN A CD  
587  O OE1 . GLN A 103 ? 0.6062 0.5891 0.5530 -0.0300 -0.0002 0.0209  105 GLN A OE1 
588  N NE2 . GLN A 103 ? 0.5710 0.5537 0.5096 -0.0421 -0.0042 0.0233  105 GLN A NE2 
589  N N   . TYR A 104 ? 0.3869 0.4309 0.3861 -0.0206 -0.0011 0.0336  106 TYR A N   
590  C CA  . TYR A 104 ? 0.3867 0.4407 0.3905 -0.0213 -0.0039 0.0369  106 TYR A CA  
591  C C   . TYR A 104 ? 0.3743 0.4346 0.3859 -0.0124 -0.0018 0.0392  106 TYR A C   
592  O O   . TYR A 104 ? 0.3713 0.4356 0.3846 -0.0107 -0.0037 0.0414  106 TYR A O   
593  C CB  . TYR A 104 ? 0.3773 0.4206 0.3730 -0.0240 -0.0065 0.0345  106 TYR A CB  
594  C CG  . TYR A 104 ? 0.3801 0.4145 0.3647 -0.0322 -0.0084 0.0327  106 TYR A CG  
595  C CD1 . TYR A 104 ? 0.3903 0.4325 0.3733 -0.0411 -0.0107 0.0355  106 TYR A CD1 
596  C CD2 . TYR A 104 ? 0.3705 0.3886 0.3447 -0.0312 -0.0077 0.0283  106 TYR A CD2 
597  C CE1 . TYR A 104 ? 0.4010 0.4312 0.3699 -0.0496 -0.0121 0.0338  106 TYR A CE1 
598  C CE2 . TYR A 104 ? 0.3862 0.3926 0.3469 -0.0375 -0.0088 0.0267  106 TYR A CE2 
599  C CZ  . TYR A 104 ? 0.4024 0.4130 0.3593 -0.0472 -0.0109 0.0294  106 TYR A CZ  
600  O OH  . TYR A 104 ? 0.4491 0.4448 0.3892 -0.0545 -0.0116 0.0279  106 TYR A OH  
601  N N   . LEU A 105 ? 0.3867 0.4459 0.4011 -0.0067 0.0021  0.0388  107 LEU A N   
602  C CA  . LEU A 105 ? 0.3981 0.4586 0.4159 0.0021  0.0048  0.0409  107 LEU A CA  
603  C C   . LEU A 105 ? 0.4349 0.5140 0.4611 0.0051  0.0043  0.0467  107 LEU A C   
604  O O   . LEU A 105 ? 0.4596 0.5518 0.4905 0.0000  0.0032  0.0486  107 LEU A O   
605  C CB  . LEU A 105 ? 0.3808 0.4328 0.3968 0.0067  0.0094  0.0386  107 LEU A CB  
606  C CG  . LEU A 105 ? 0.3689 0.4056 0.3773 0.0051  0.0098  0.0332  107 LEU A CG  
607  C CD1 . LEU A 105 ? 0.3654 0.3953 0.3718 0.0090  0.0141  0.0314  107 LEU A CD1 
608  C CD2 . LEU A 105 ? 0.3656 0.3955 0.3697 0.0057  0.0086  0.0317  107 LEU A CD2 
609  N N   . SER A 106 ? 0.4784 0.5583 0.5052 0.0129  0.0051  0.0495  108 SER A N   
610  C CA  . SER A 106 ? 0.5238 0.6216 0.5580 0.0196  0.0052  0.0555  108 SER A CA  
611  C C   . SER A 106 ? 0.5546 0.6444 0.5857 0.0315  0.0105  0.0568  108 SER A C   
612  O O   . SER A 106 ? 0.5646 0.6350 0.5861 0.0337  0.0121  0.0540  108 SER A O   
613  C CB  . SER A 106 ? 0.5636 0.6680 0.5980 0.0183  0.0003  0.0583  108 SER A CB  
614  O OG  . SER A 106 ? 0.6055 0.7204 0.6432 0.0290  0.0013  0.0638  108 SER A OG  
615  N N   . SER A 107 ? 0.6073 0.7117 0.6450 0.0391  0.0132  0.0613  109 SER A N   
616  C CA  . SER A 107 ? 0.6560 0.7522 0.6886 0.0523  0.0189  0.0634  109 SER A CA  
617  C C   . SER A 107 ? 0.6654 0.7620 0.6942 0.0610  0.0175  0.0677  109 SER A C   
618  O O   . SER A 107 ? 0.6797 0.7688 0.7021 0.0733  0.0222  0.0703  109 SER A O   
619  C CB  . SER A 107 ? 0.6952 0.8067 0.7357 0.0575  0.0229  0.0662  109 SER A CB  
620  O OG  . SER A 107 ? 0.7506 0.8888 0.8033 0.0512  0.0189  0.0690  109 SER A OG  
621  N N   . ALA A 108 ? 0.6495 0.7518 0.6798 0.0550  0.0115  0.0683  110 ALA A N   
622  C CA  . ALA A 108 ? 0.6622 0.7619 0.6868 0.0618  0.0094  0.0718  110 ALA A CA  
623  C C   . ALA A 108 ? 0.6577 0.7265 0.6657 0.0635  0.0124  0.0680  110 ALA A C   
624  O O   . ALA A 108 ? 0.6542 0.7128 0.6522 0.0731  0.0139  0.0709  110 ALA A O   
625  C CB  . ALA A 108 ? 0.6495 0.7626 0.6794 0.0526  0.0022  0.0727  110 ALA A CB  
626  N N   . GLY A 109 ? 0.6524 0.7070 0.6566 0.0540  0.0131  0.0617  111 GLY A N   
627  C CA  . GLY A 109 ? 0.6301 0.6582 0.6193 0.0527  0.0160  0.0573  111 GLY A CA  
628  C C   . GLY A 109 ? 0.5902 0.6075 0.5762 0.0513  0.0208  0.0532  111 GLY A C   
629  O O   . GLY A 109 ? 0.5455 0.5524 0.5272 0.0428  0.0204  0.0478  111 GLY A O   
630  N N   . VAL A 110 ? 0.5760 0.5970 0.5640 0.0593  0.0252  0.0558  112 VAL A N   
631  C CA  . VAL A 110 ? 0.5491 0.5590 0.5329 0.0582  0.0300  0.0522  112 VAL A CA  
632  C C   . VAL A 110 ? 0.5655 0.5559 0.5339 0.0680  0.0365  0.0536  112 VAL A C   
633  O O   . VAL A 110 ? 0.5594 0.5545 0.5270 0.0796  0.0384  0.0591  112 VAL A O   
634  C CB  . VAL A 110 ? 0.5294 0.5568 0.5261 0.0574  0.0304  0.0531  112 VAL A CB  
635  C CG1 . VAL A 110 ? 0.5395 0.5804 0.5414 0.0691  0.0336  0.0591  112 VAL A CG1 
636  C CG2 . VAL A 110 ? 0.4981 0.5134 0.4903 0.0527  0.0335  0.0481  112 VAL A CG2 
637  N N   . THR A 111 ? 0.5622 0.5315 0.5177 0.0632  0.0397  0.0488  113 THR A N   
638  C CA  . THR A 111 ? 0.5845 0.5311 0.5224 0.0694  0.0468  0.0487  113 THR A CA  
639  C C   . THR A 111 ? 0.5789 0.5266 0.5204 0.0663  0.0495  0.0460  113 THR A C   
640  O O   . THR A 111 ? 0.5588 0.5116 0.5068 0.0558  0.0461  0.0415  113 THR A O   
641  C CB  . THR A 111 ? 0.5868 0.5087 0.5052 0.0639  0.0479  0.0453  113 THR A CB  
642  O OG1 . THR A 111 ? 0.6037 0.5263 0.5198 0.0681  0.0453  0.0486  113 THR A OG1 
643  C CG2 . THR A 111 ? 0.6150 0.5092 0.5110 0.0671  0.0552  0.0443  113 THR A CG2 
644  N N   . THR A 112 ? 0.5914 0.5345 0.5283 0.0756  0.0553  0.0486  114 THR A N   
645  C CA  . THR A 112 ? 0.5830 0.5261 0.5222 0.0733  0.0584  0.0463  114 THR A CA  
646  C C   . THR A 112 ? 0.5972 0.5123 0.5143 0.0766  0.0656  0.0451  114 THR A C   
647  O O   . THR A 112 ? 0.6161 0.5194 0.5212 0.0877  0.0703  0.0489  114 THR A O   
648  C CB  . THR A 112 ? 0.5898 0.5556 0.5447 0.0802  0.0593  0.0505  114 THR A CB  
649  O OG1 . THR A 112 ? 0.5967 0.5862 0.5687 0.0759  0.0526  0.0518  114 THR A OG1 
650  C CG2 . THR A 112 ? 0.5766 0.5434 0.5345 0.0765  0.0617  0.0480  114 THR A CG2 
651  N N   . VAL A 113 ? 0.6028 0.5071 0.5134 0.0675  0.0664  0.0400  115 VAL A N   
652  C CA  . VAL A 113 ? 0.6581 0.5331 0.5445 0.0672  0.0729  0.0380  115 VAL A CA  
653  C C   . VAL A 113 ? 0.6843 0.5580 0.5711 0.0647  0.0757  0.0359  115 VAL A C   
654  O O   . VAL A 113 ? 0.6513 0.5405 0.5522 0.0568  0.0710  0.0331  115 VAL A O   
655  C CB  . VAL A 113 ? 0.6597 0.5199 0.5331 0.0555  0.0707  0.0333  115 VAL A CB  
656  C CG1 . VAL A 113 ? 0.6297 0.5053 0.5164 0.0431  0.0647  0.0286  115 VAL A CG1 
657  C CG2 . VAL A 113 ? 0.6959 0.5248 0.5416 0.0534  0.0773  0.0313  115 VAL A CG2 
658  N N   . GLN A 114 ? 0.7546 0.6090 0.6249 0.0721  0.0834  0.0373  116 GLN A N   
659  C CA  . GLN A 114 ? 0.7586 0.6050 0.6231 0.0697  0.0875  0.0351  116 GLN A CA  
660  C C   . GLN A 114 ? 0.7589 0.5874 0.6078 0.0560  0.0866  0.0293  116 GLN A C   
661  O O   . GLN A 114 ? 0.7550 0.5619 0.5838 0.0536  0.0889  0.0283  116 GLN A O   
662  C CB  . GLN A 114 ? 0.8456 0.6738 0.6939 0.0826  0.0967  0.0387  116 GLN A CB  
663  C CG  . GLN A 114 ? 0.8697 0.7200 0.7352 0.0956  0.0986  0.0440  116 GLN A CG  
664  C CD  . GLN A 114 ? 0.9456 0.7783 0.7952 0.1058  0.1082  0.0459  116 GLN A CD  
665  O OE1 . GLN A 114 ? 1.0300 0.8335 0.8542 0.1113  0.1144  0.0465  116 GLN A OE1 
666  N NE2 . GLN A 114 ? 0.8985 0.7465 0.7608 0.1077  0.1100  0.0466  116 GLN A NE2 
667  N N   . SER A 115 ? 0.7469 0.5837 0.6031 0.0473  0.0838  0.0257  117 SER A N   
668  C CA  . SER A 115 ? 0.7729 0.6003 0.6183 0.0334  0.0816  0.0201  117 SER A CA  
669  C C   . SER A 115 ? 0.8265 0.6242 0.6448 0.0319  0.0889  0.0188  117 SER A C   
670  O O   . SER A 115 ? 0.8310 0.6221 0.6456 0.0393  0.0943  0.0208  117 SER A O   
671  C CB  . SER A 115 ? 0.7552 0.6020 0.6169 0.0269  0.0760  0.0173  117 SER A CB  
672  O OG  . SER A 115 ? 0.7546 0.6008 0.6176 0.0312  0.0794  0.0184  117 SER A OG  
673  N N   . GLN A 116 ? 0.8633 0.6436 0.6624 0.0217  0.0893  0.0155  118 GLN A N   
674  C CA  . GLN A 116 ? 0.9165 0.6663 0.6859 0.0162  0.0956  0.0133  118 GLN A CA  
675  C C   . GLN A 116 ? 0.8793 0.6366 0.6507 0.0035  0.0919  0.0086  118 GLN A C   
676  O O   . GLN A 116 ? 0.8186 0.6016 0.6107 -0.0016 0.0844  0.0068  118 GLN A O   
677  C CB  . GLN A 116 ? 0.9825 0.7094 0.7276 0.0089  0.0977  0.0117  118 GLN A CB  
678  C CG  . GLN A 116 ? 1.0198 0.7403 0.7626 0.0203  0.0999  0.0160  118 GLN A CG  
679  C CD  . GLN A 116 ? 1.0677 0.7721 0.8005 0.0370  0.1078  0.0209  118 GLN A CD  
680  O OE1 . GLN A 116 ? 1.1175 0.7916 0.8227 0.0372  0.1152  0.0205  118 GLN A OE1 
681  N NE2 . GLN A 116 ? 1.0806 0.8057 0.8350 0.0510  0.1065  0.0257  118 GLN A NE2 
682  N N   . GLN A 117 ? 0.9189 0.6532 0.6676 -0.0014 0.0971  0.0068  119 GLN A N   
683  C CA  . GLN A 117 ? 0.9261 0.6652 0.6719 -0.0155 0.0934  0.0021  119 GLN A CA  
684  C C   . GLN A 117 ? 0.9053 0.6464 0.6435 -0.0305 0.0893  -0.0018 119 GLN A C   
685  O O   . GLN A 117 ? 0.9812 0.6968 0.6936 -0.0360 0.0941  -0.0026 119 GLN A O   
686  C CB  . GLN A 117 ? 0.9730 0.6855 0.6945 -0.0169 0.1004  0.0015  119 GLN A CB  
687  C CG  . GLN A 117 ? 0.9725 0.6926 0.6931 -0.0298 0.0963  -0.0026 119 GLN A CG  
688  C CD  . GLN A 117 ? 0.9403 0.6944 0.6915 -0.0278 0.0882  -0.0028 119 GLN A CD  
689  O OE1 . GLN A 117 ? 0.9195 0.6836 0.6871 -0.0164 0.0886  0.0001  119 GLN A OE1 
690  N NE2 . GLN A 117 ? 0.8954 0.6677 0.6534 -0.0391 0.0809  -0.0064 119 GLN A NE2 
691  N N   . GLY A 118 ? 0.8517 0.6218 0.6104 -0.0368 0.0811  -0.0042 120 GLY A N   
692  C CA  . GLY A 118 ? 0.8711 0.6491 0.6249 -0.0520 0.0769  -0.0085 120 GLY A CA  
693  C C   . GLY A 118 ? 0.8555 0.6489 0.6236 -0.0502 0.0731  -0.0079 120 GLY A C   
694  O O   . GLY A 118 ? 0.8220 0.6427 0.6090 -0.0538 0.0662  -0.0098 120 GLY A O   
695  N N   . THR A 119 ? 0.8809 0.6566 0.6391 -0.0444 0.0775  -0.0052 121 THR A N   
696  C CA  . THR A 119 ? 0.8654 0.6512 0.6332 -0.0431 0.0746  -0.0045 121 THR A CA  
697  C C   . THR A 119 ? 0.8614 0.6366 0.6306 -0.0275 0.0783  0.0008  121 THR A C   
698  O O   . THR A 119 ? 0.8907 0.6373 0.6375 -0.0230 0.0854  0.0027  121 THR A O   
699  C CB  . THR A 119 ? 0.9073 0.6824 0.6551 -0.0583 0.0754  -0.0081 121 THR A CB  
700  O OG1 . THR A 119 ? 0.9033 0.7008 0.6591 -0.0710 0.0700  -0.0126 121 THR A OG1 
701  C CG2 . THR A 119 ? 0.9106 0.6894 0.6633 -0.0563 0.0739  -0.0069 121 THR A CG2 
702  N N   . THR A 120 ? 0.8218 0.6199 0.6158 -0.0197 0.0735  0.0030  122 THR A N   
703  C CA  . THR A 120 ? 0.8232 0.6199 0.6241 -0.0048 0.0754  0.0084  122 THR A CA  
704  C C   . THR A 120 ? 0.8075 0.6018 0.6046 -0.0069 0.0739  0.0087  122 THR A C   
705  O O   . THR A 120 ? 0.7909 0.6058 0.6032 -0.0127 0.0680  0.0067  122 THR A O   
706  C CB  . THR A 120 ? 0.7811 0.6041 0.6101 0.0036  0.0712  0.0107  122 THR A CB  
707  O OG1 . THR A 120 ? 0.7908 0.6148 0.6205 0.0021  0.0721  0.0093  122 THR A OG1 
708  C CG2 . THR A 120 ? 0.7715 0.5957 0.6076 0.0185  0.0735  0.0165  122 THR A CG2 
709  N N   . THR A 121 ? 0.8307 0.5994 0.6070 -0.0014 0.0796  0.0113  123 THR A N   
710  C CA  . THR A 121 ? 0.8515 0.6126 0.6196 -0.0025 0.0791  0.0120  123 THR A CA  
711  C C   . THR A 121 ? 0.8278 0.6049 0.6156 0.0115  0.0763  0.0172  123 THR A C   
712  O O   . THR A 121 ? 0.8357 0.6110 0.6262 0.0249  0.0794  0.0216  123 THR A O   
713  C CB  . THR A 121 ? 0.9219 0.6440 0.6536 -0.0041 0.0868  0.0121  123 THR A CB  
714  O OG1 . THR A 121 ? 0.9298 0.6429 0.6464 -0.0204 0.0879  0.0067  123 THR A OG1 
715  C CG2 . THR A 121 ? 0.9724 0.6819 0.6910 -0.0056 0.0870  0.0128  123 THR A CG2 
716  N N   . ILE A 122 ? 0.8227 0.6158 0.6233 0.0080  0.0709  0.0166  124 ILE A N   
717  C CA  . ILE A 122 ? 0.8129 0.6233 0.6324 0.0192  0.0672  0.0213  124 ILE A CA  
718  C C   . ILE A 122 ? 0.8500 0.6476 0.6565 0.0188  0.0673  0.0224  124 ILE A C   
719  O O   . ILE A 122 ? 0.8413 0.6481 0.6527 0.0087  0.0632  0.0192  124 ILE A O   
720  C CB  . ILE A 122 ? 0.7500 0.5929 0.5985 0.0161  0.0600  0.0200  124 ILE A CB  
721  C CG1 . ILE A 122 ? 0.7176 0.5701 0.5758 0.0158  0.0601  0.0186  124 ILE A CG1 
722  C CG2 . ILE A 122 ? 0.7351 0.5939 0.6001 0.0258  0.0565  0.0247  124 ILE A CG2 
723  C CD1 . ILE A 122 ? 0.6642 0.5421 0.5435 0.0098  0.0537  0.0158  124 ILE A CD1 
724  N N   . SER A 123 ? 0.9239 0.7009 0.7137 0.0304  0.0721  0.0269  125 SER A N   
725  C CA  . SER A 123 ? 0.9528 0.7079 0.7214 0.0313  0.0740  0.0283  125 SER A CA  
726  C C   . SER A 123 ? 0.9210 0.6938 0.7061 0.0406  0.0691  0.0328  125 SER A C   
727  O O   . SER A 123 ? 0.9019 0.7012 0.7122 0.0481  0.0655  0.0357  125 SER A O   
728  C CB  . SER A 123 ? 1.0065 0.7265 0.7443 0.0401  0.0822  0.0310  125 SER A CB  
729  O OG  . SER A 123 ? 1.0775 0.7763 0.7942 0.0279  0.0868  0.0261  125 SER A OG  
730  N N   . GLY A 124 ? 0.9183 0.6751 0.6871 0.0394  0.0694  0.0335  126 GLY A N   
731  C CA  . GLY A 124 ? 0.9008 0.6659 0.6765 0.0494  0.0659  0.0385  126 GLY A CA  
732  C C   . GLY A 124 ? 0.8389 0.6375 0.6442 0.0437  0.0579  0.0373  126 GLY A C   
733  O O   . GLY A 124 ? 0.8517 0.6662 0.6706 0.0531  0.0541  0.0421  126 GLY A O   
734  N N   . LEU A 125 ? 0.7917 0.6009 0.6057 0.0291  0.0553  0.0314  127 LEU A N   
735  C CA  . LEU A 125 ? 0.7431 0.5814 0.5825 0.0238  0.0482  0.0301  127 LEU A CA  
736  C C   . LEU A 125 ? 0.7468 0.5812 0.5801 0.0197  0.0456  0.0300  127 LEU A C   
737  O O   . LEU A 125 ? 0.7274 0.5481 0.5456 0.0084  0.0475  0.0256  127 LEU A O   
738  C CB  . LEU A 125 ? 0.7100 0.5597 0.5582 0.0113  0.0469  0.0240  127 LEU A CB  
739  C CG  . LEU A 125 ? 0.7190 0.5792 0.5790 0.0147  0.0476  0.0240  127 LEU A CG  
740  C CD1 . LEU A 125 ? 0.6978 0.5733 0.5689 0.0037  0.0447  0.0185  127 LEU A CD1 
741  C CD2 . LEU A 125 ? 0.6977 0.5761 0.5765 0.0263  0.0448  0.0292  127 LEU A CD2 
742  N N   . LYS A 126 ? 0.7504 0.5980 0.5957 0.0276  0.0414  0.0345  128 LYS A N   
743  C CA  . LYS A 126 ? 0.7621 0.6138 0.6087 0.0230  0.0372  0.0343  128 LYS A CA  
744  C C   . LYS A 126 ? 0.7361 0.6009 0.5928 0.0091  0.0345  0.0282  128 LYS A C   
745  O O   . LYS A 126 ? 0.7124 0.5933 0.5844 0.0064  0.0332  0.0258  128 LYS A O   
746  C CB  . LYS A 126 ? 0.7850 0.6564 0.6486 0.0326  0.0320  0.0399  128 LYS A CB  
747  C CG  . LYS A 126 ? 0.8655 0.7368 0.7289 0.0480  0.0341  0.0462  128 LYS A CG  
748  C CD  . LYS A 126 ? 0.9270 0.8123 0.7987 0.0583  0.0297  0.0528  128 LYS A CD  
749  C CE  . LYS A 126 ? 1.0056 0.8759 0.8617 0.0742  0.0338  0.0587  128 LYS A CE  
750  N NZ  . LYS A 126 ? 1.0546 0.9372 0.9153 0.0841  0.0293  0.0651  128 LYS A NZ  
751  N N   . PRO A 127 ? 0.6999 0.5594 0.5488 0.0005  0.0336  0.0255  129 PRO A N   
752  C CA  . PRO A 127 ? 0.6467 0.5183 0.5030 -0.0119 0.0322  0.0194  129 PRO A CA  
753  C C   . PRO A 127 ? 0.5624 0.4604 0.4435 -0.0100 0.0267  0.0199  129 PRO A C   
754  O O   . PRO A 127 ? 0.5279 0.4330 0.4174 -0.0023 0.0235  0.0245  129 PRO A O   
755  C CB  . PRO A 127 ? 0.6753 0.5354 0.5172 -0.0193 0.0326  0.0177  129 PRO A CB  
756  C CG  . PRO A 127 ? 0.7207 0.5557 0.5418 -0.0117 0.0355  0.0223  129 PRO A CG  
757  C CD  . PRO A 127 ? 0.7154 0.5588 0.5485 0.0029  0.0338  0.0282  129 PRO A CD  
758  N N   . GLY A 128 ? 0.5075 0.4190 0.3982 -0.0170 0.0258  0.0151  130 GLY A N   
759  C CA  . GLY A 128 ? 0.4537 0.3862 0.3640 -0.0155 0.0211  0.0152  130 GLY A CA  
760  C C   . GLY A 128 ? 0.4235 0.3672 0.3433 -0.0167 0.0213  0.0122  130 GLY A C   
761  O O   . GLY A 128 ? 0.4229 0.3625 0.3356 -0.0224 0.0244  0.0085  130 GLY A O   
762  N N   . TYR A 129 ? 0.3840 0.3411 0.3183 -0.0124 0.0180  0.0139  131 TYR A N   
763  C CA  . TYR A 129 ? 0.3650 0.3333 0.3088 -0.0127 0.0173  0.0114  131 TYR A CA  
764  C C   . TYR A 129 ? 0.3738 0.3433 0.3235 -0.0056 0.0175  0.0152  131 TYR A C   
765  O O   . TYR A 129 ? 0.4221 0.3949 0.3768 -0.0009 0.0155  0.0196  131 TYR A O   
766  C CB  . TYR A 129 ? 0.3291 0.3094 0.2813 -0.0145 0.0137  0.0098  131 TYR A CB  
767  C CG  . TYR A 129 ? 0.3079 0.2980 0.2651 -0.0160 0.0132  0.0057  131 TYR A CG  
768  C CD1 . TYR A 129 ? 0.3011 0.2926 0.2542 -0.0201 0.0156  0.0018  131 TYR A CD1 
769  C CD2 . TYR A 129 ? 0.2856 0.2836 0.2502 -0.0136 0.0103  0.0059  131 TYR A CD2 
770  C CE1 . TYR A 129 ? 0.2782 0.2810 0.2361 -0.0203 0.0147  -0.0014 131 TYR A CE1 
771  C CE2 . TYR A 129 ? 0.2683 0.2741 0.2357 -0.0133 0.0099  0.0026  131 TYR A CE2 
772  C CZ  . TYR A 129 ? 0.2669 0.2763 0.2317 -0.0160 0.0119  -0.0009 131 TYR A CZ  
773  O OH  . TYR A 129 ? 0.2496 0.2687 0.2173 -0.0144 0.0110  -0.0038 131 TYR A OH  
774  N N   . TYR A 130 ? 0.3611 0.3296 0.3105 -0.0052 0.0198  0.0137  132 TYR A N   
775  C CA  . TYR A 130 ? 0.3431 0.3118 0.2966 0.0011  0.0210  0.0170  132 TYR A CA  
776  C C   . TYR A 130 ? 0.3094 0.2876 0.2711 0.0003  0.0197  0.0148  132 TYR A C   
777  O O   . TYR A 130 ? 0.2841 0.2644 0.2440 -0.0042 0.0196  0.0104  132 TYR A O   
778  C CB  . TYR A 130 ? 0.3654 0.3189 0.3066 0.0031  0.0260  0.0177  132 TYR A CB  
779  C CG  . TYR A 130 ? 0.3986 0.3408 0.3304 0.0067  0.0275  0.0211  132 TYR A CG  
780  C CD1 . TYR A 130 ? 0.4128 0.3457 0.3335 0.0011  0.0279  0.0190  132 TYR A CD1 
781  C CD2 . TYR A 130 ? 0.4096 0.3519 0.3436 0.0161  0.0282  0.0266  132 TYR A CD2 
782  C CE1 . TYR A 130 ? 0.4431 0.3634 0.3529 0.0048  0.0292  0.0222  132 TYR A CE1 
783  C CE2 . TYR A 130 ? 0.4385 0.3708 0.3630 0.0211  0.0292  0.0301  132 TYR A CE2 
784  C CZ  . TYR A 130 ? 0.4564 0.3759 0.3677 0.0155  0.0297  0.0280  132 TYR A CZ  
785  O OH  . TYR A 130 ? 0.4824 0.3895 0.3820 0.0208  0.0308  0.0316  132 TYR A OH  
786  N N   . LEU A 131 ? 0.2859 0.2704 0.2558 0.0047  0.0187  0.0179  133 LEU A N   
787  C CA  . LEU A 131 ? 0.2778 0.2668 0.2522 0.0050  0.0186  0.0166  133 LEU A CA  
788  C C   . LEU A 131 ? 0.2852 0.2680 0.2567 0.0090  0.0227  0.0183  133 LEU A C   
789  O O   . LEU A 131 ? 0.2717 0.2542 0.2444 0.0139  0.0241  0.0225  133 LEU A O   
790  C CB  . LEU A 131 ? 0.2684 0.2668 0.2511 0.0054  0.0152  0.0184  133 LEU A CB  
791  C CG  . LEU A 131 ? 0.2649 0.2656 0.2497 0.0051  0.0149  0.0166  133 LEU A CG  
792  C CD1 . LEU A 131 ? 0.2606 0.2665 0.2485 0.0033  0.0114  0.0171  133 LEU A CD1 
793  C CD2 . LEU A 131 ? 0.2683 0.2675 0.2542 0.0085  0.0181  0.0188  133 LEU A CD2 
794  N N   . ILE A 132 ? 0.3042 0.2824 0.2709 0.0070  0.0246  0.0151  134 ILE A N   
795  C CA  . ILE A 132 ? 0.3168 0.2873 0.2788 0.0099  0.0289  0.0160  134 ILE A CA  
796  C C   . ILE A 132 ? 0.3113 0.2882 0.2794 0.0104  0.0278  0.0154  134 ILE A C   
797  O O   . ILE A 132 ? 0.2992 0.2801 0.2680 0.0069  0.0253  0.0119  134 ILE A O   
798  C CB  . ILE A 132 ? 0.3328 0.2918 0.2822 0.0056  0.0317  0.0126  134 ILE A CB  
799  C CG1 . ILE A 132 ? 0.3431 0.2932 0.2833 0.0036  0.0330  0.0127  134 ILE A CG1 
800  C CG2 . ILE A 132 ? 0.3368 0.2860 0.2797 0.0084  0.0363  0.0134  134 ILE A CG2 
801  C CD1 . ILE A 132 ? 0.3655 0.3049 0.2916 -0.0036 0.0355  0.0088  134 ILE A CD1 
802  N N   . LYS A 133 ? 0.3162 0.2938 0.2875 0.0150  0.0302  0.0187  135 LYS A N   
803  C CA  . LYS A 133 ? 0.3103 0.2912 0.2851 0.0152  0.0303  0.0183  135 LYS A CA  
804  C C   . LYS A 133 ? 0.3295 0.3049 0.3015 0.0200  0.0356  0.0208  135 LYS A C   
805  O O   . LYS A 133 ? 0.3245 0.2980 0.2955 0.0248  0.0383  0.0241  135 LYS A O   
806  C CB  . LYS A 133 ? 0.3012 0.2932 0.2850 0.0148  0.0271  0.0203  135 LYS A CB  
807  C CG  . LYS A 133 ? 0.3144 0.3139 0.3044 0.0182  0.0277  0.0250  135 LYS A CG  
808  C CD  . LYS A 133 ? 0.3197 0.3302 0.3167 0.0151  0.0240  0.0265  135 LYS A CD  
809  C CE  . LYS A 133 ? 0.3300 0.3459 0.3305 0.0148  0.0257  0.0281  135 LYS A CE  
810  N NZ  . LYS A 133 ? 0.3362 0.3630 0.3420 0.0104  0.0225  0.0301  135 LYS A NZ  
811  N N   . ASP A 134 ? 0.3289 0.3017 0.2990 0.0194  0.0371  0.0194  136 ASP A N   
812  C CA  . ASP A 134 ? 0.3498 0.3214 0.3203 0.0239  0.0418  0.0222  136 ASP A CA  
813  C C   . ASP A 134 ? 0.3483 0.3342 0.3298 0.0265  0.0409  0.0263  136 ASP A C   
814  O O   . ASP A 134 ? 0.3218 0.3166 0.3095 0.0224  0.0365  0.0260  136 ASP A O   
815  C CB  . ASP A 134 ? 0.3543 0.3223 0.3217 0.0216  0.0424  0.0198  136 ASP A CB  
816  C CG  . ASP A 134 ? 0.3757 0.3298 0.3309 0.0200  0.0449  0.0169  136 ASP A CG  
817  O OD1 . ASP A 134 ? 0.3934 0.3382 0.3419 0.0238  0.0504  0.0184  136 ASP A OD1 
818  O OD2 . ASP A 134 ? 0.3965 0.3495 0.3482 0.0151  0.0415  0.0131  136 ASP A OD2 
819  N N   . SER A 135 ? 0.3725 0.3605 0.3553 0.0331  0.0452  0.0302  137 SER A N   
820  C CA  . SER A 135 ? 0.3821 0.3873 0.3759 0.0360  0.0455  0.0346  137 SER A CA  
821  C C   . SER A 135 ? 0.3843 0.3962 0.3824 0.0309  0.0449  0.0337  137 SER A C   
822  O O   . SER A 135 ? 0.3623 0.3649 0.3544 0.0302  0.0478  0.0316  137 SER A O   
823  C CB  . SER A 135 ? 0.4094 0.4142 0.4016 0.0455  0.0513  0.0385  137 SER A CB  
824  O OG  . SER A 135 ? 0.4388 0.4637 0.4425 0.0480  0.0517  0.0427  137 SER A OG  
825  N N   . ARG A 136 ? 0.4002 0.4266 0.4066 0.0267  0.0413  0.0353  138 ARG A N   
826  C CA  . ARG A 136 ? 0.4411 0.4735 0.4497 0.0202  0.0403  0.0347  138 ARG A CA  
827  C C   . ARG A 136 ? 0.4558 0.4902 0.4647 0.0229  0.0461  0.0361  138 ARG A C   
828  O O   . ARG A 136 ? 0.4691 0.5136 0.4833 0.0295  0.0501  0.0399  138 ARG A O   
829  C CB  . ARG A 136 ? 0.4787 0.5279 0.4955 0.0161  0.0366  0.0376  138 ARG A CB  
830  C CG  . ARG A 136 ? 0.5390 0.5932 0.5555 0.0071  0.0350  0.0370  138 ARG A CG  
831  C CD  . ARG A 136 ? 0.6041 0.6710 0.6254 0.0013  0.0303  0.0390  138 ARG A CD  
832  N NE  . ARG A 136 ? 0.6862 0.7593 0.7061 -0.0078 0.0302  0.0393  138 ARG A NE  
833  C CZ  . ARG A 136 ? 0.7493 0.8075 0.7582 -0.0144 0.0292  0.0358  138 ARG A CZ  
834  N NH1 . ARG A 136 ? 0.7421 0.7815 0.7423 -0.0119 0.0277  0.0320  138 ARG A NH1 
835  N NH2 . ARG A 136 ? 0.7591 0.8218 0.7647 -0.0235 0.0297  0.0363  138 ARG A NH2 
836  N N   . GLY A 137 ? 0.4662 0.4910 0.4685 0.0188  0.0470  0.0332  139 GLY A N   
837  C CA  . GLY A 137 ? 0.4818 0.5074 0.4831 0.0201  0.0526  0.0340  139 GLY A CA  
838  C C   . GLY A 137 ? 0.4853 0.5015 0.4819 0.0285  0.0584  0.0345  139 GLY A C   
839  O O   . GLY A 137 ? 0.4960 0.5114 0.4907 0.0301  0.0637  0.0350  139 GLY A O   
840  N N   . SER A 138 ? 0.4781 0.4856 0.4709 0.0328  0.0578  0.0340  140 SER A N   
841  C CA  . SER A 138 ? 0.4984 0.4943 0.4837 0.0409  0.0634  0.0347  140 SER A CA  
842  C C   . SER A 138 ? 0.5077 0.4871 0.4818 0.0398  0.0671  0.0318  140 SER A C   
843  O O   . SER A 138 ? 0.5106 0.4795 0.4767 0.0460  0.0729  0.0327  140 SER A O   
844  C CB  . SER A 138 ? 0.5078 0.4948 0.4883 0.0415  0.0604  0.0335  140 SER A CB  
845  O OG  . SER A 138 ? 0.5539 0.5266 0.5238 0.0482  0.0656  0.0341  140 SER A OG  
846  N N   . LEU A 139 ? 0.5142 0.4891 0.4853 0.0325  0.0637  0.0284  141 LEU A N   
847  C CA  . LEU A 139 ? 0.5558 0.5139 0.5148 0.0307  0.0657  0.0251  141 LEU A CA  
848  C C   . LEU A 139 ? 0.5879 0.5482 0.5471 0.0274  0.0673  0.0249  141 LEU A C   
849  O O   . LEU A 139 ? 0.6194 0.5668 0.5687 0.0250  0.0677  0.0221  141 LEU A O   
850  C CB  . LEU A 139 ? 0.5279 0.4778 0.4811 0.0256  0.0599  0.0210  141 LEU A CB  
851  C CG  . LEU A 139 ? 0.5096 0.4547 0.4595 0.0267  0.0588  0.0204  141 LEU A CG  
852  C CD1 . LEU A 139 ? 0.4954 0.4363 0.4405 0.0209  0.0533  0.0161  141 LEU A CD1 
853  C CD2 . LEU A 139 ? 0.5111 0.4428 0.4506 0.0315  0.0653  0.0214  141 LEU A CD2 
854  N N   . ASP A 140 ? 0.6499 0.6258 0.6187 0.0267  0.0682  0.0277  142 ASP A N   
855  C CA  . ASP A 140 ? 0.7258 0.7036 0.6934 0.0207  0.0685  0.0270  142 ASP A CA  
856  C C   . ASP A 140 ? 0.7635 0.7336 0.7244 0.0230  0.0754  0.0270  142 ASP A C   
857  O O   . ASP A 140 ? 0.8212 0.7822 0.7743 0.0178  0.0750  0.0247  142 ASP A O   
858  C CB  . ASP A 140 ? 0.7805 0.7781 0.7591 0.0171  0.0673  0.0298  142 ASP A CB  
859  C CG  . ASP A 140 ? 0.8228 0.8228 0.8035 0.0122  0.0599  0.0287  142 ASP A CG  
860  O OD1 . ASP A 140 ? 0.8126 0.8002 0.7871 0.0124  0.0560  0.0257  142 ASP A OD1 
861  O OD2 . ASP A 140 ? 0.8797 0.8945 0.8677 0.0078  0.0583  0.0308  142 ASP A OD2 
862  N N   . ASN A 141 ? 0.7790 0.7505 0.7409 0.0307  0.0818  0.0295  143 ASN A N   
863  C CA  . ASN A 141 ? 0.8478 0.8101 0.8016 0.0331  0.0891  0.0295  143 ASN A CA  
864  C C   . ASN A 141 ? 0.8104 0.7488 0.7488 0.0341  0.0898  0.0263  143 ASN A C   
865  O O   . ASN A 141 ? 0.8570 0.7840 0.7858 0.0341  0.0946  0.0254  143 ASN A O   
866  C CB  . ASN A 141 ? 0.9183 0.8949 0.8795 0.0413  0.0966  0.0339  143 ASN A CB  
867  C CG  . ASN A 141 ? 0.9940 0.9903 0.9646 0.0365  0.0982  0.0357  143 ASN A CG  
868  O OD1 . ASN A 141 ? 0.9938 0.9853 0.9587 0.0337  0.1026  0.0347  143 ASN A OD1 
869  N ND2 . ASN A 141 ? 1.0447 1.0631 1.0286 0.0346  0.0948  0.0382  143 ASN A ND2 
870  N N   . LYS A 142 ? 0.7335 0.6650 0.6688 0.0336  0.0851  0.0246  144 LYS A N   
871  C CA  . LYS A 142 ? 0.6889 0.5997 0.6091 0.0339  0.0864  0.0220  144 LYS A CA  
872  C C   . LYS A 142 ? 0.6354 0.5378 0.5484 0.0262  0.0806  0.0179  144 LYS A C   
873  O O   . LYS A 142 ? 0.6192 0.5305 0.5389 0.0223  0.0740  0.0169  144 LYS A O   
874  C CB  . LYS A 142 ? 0.6912 0.5999 0.6108 0.0369  0.0851  0.0225  144 LYS A CB  
875  C CG  . LYS A 142 ? 0.7048 0.6226 0.6312 0.0460  0.0899  0.0270  144 LYS A CG  
876  C CD  . LYS A 142 ? 0.7280 0.6464 0.6557 0.0483  0.0871  0.0278  144 LYS A CD  
877  C CE  . LYS A 142 ? 0.7429 0.6745 0.6794 0.0580  0.0907  0.0329  144 LYS A CE  
878  N NZ  . LYS A 142 ? 0.7578 0.6786 0.6860 0.0635  0.0920  0.0340  144 LYS A NZ  
879  N N   . LYS A 143 ? 0.5888 0.4742 0.4872 0.0246  0.0829  0.0156  145 LYS A N   
880  C CA  . LYS A 143 ? 0.5619 0.4398 0.4519 0.0183  0.0776  0.0119  145 LYS A CA  
881  C C   . LYS A 143 ? 0.5217 0.3940 0.4052 0.0154  0.0739  0.0095  145 LYS A C   
882  O O   . LYS A 143 ? 0.5221 0.3874 0.4007 0.0178  0.0781  0.0104  145 LYS A O   
883  C CB  . LYS A 143 ? 0.5831 0.4467 0.4602 0.0172  0.0823  0.0110  145 LYS A CB  
884  C CG  . LYS A 143 ? 0.5964 0.4647 0.4777 0.0181  0.0860  0.0127  145 LYS A CG  
885  C CD  . LYS A 143 ? 0.6253 0.4778 0.4922 0.0165  0.0905  0.0115  145 LYS A CD  
886  C CE  . LYS A 143 ? 0.6493 0.5050 0.5177 0.0143  0.0916  0.0120  145 LYS A CE  
887  N NZ  . LYS A 143 ? 0.6882 0.5270 0.5406 0.0107  0.0921  0.0096  145 LYS A NZ  
888  N N   . GLY A 144 ? 0.4867 0.3623 0.3694 0.0108  0.0667  0.0067  146 GLY A N   
889  C CA  . GLY A 144 ? 0.4839 0.3571 0.3599 0.0063  0.0626  0.0039  146 GLY A CA  
890  C C   . GLY A 144 ? 0.4662 0.3494 0.3510 0.0067  0.0598  0.0042  146 GLY A C   
891  O O   . GLY A 144 ? 0.4467 0.3267 0.3246 0.0025  0.0584  0.0022  146 GLY A O   
892  N N   . HIS A 145 ? 0.4500 0.3449 0.3483 0.0105  0.0588  0.0066  147 HIS A N   
893  C CA  . HIS A 145 ? 0.4448 0.3486 0.3512 0.0111  0.0562  0.0072  147 HIS A CA  
894  C C   . HIS A 145 ? 0.4125 0.3297 0.3289 0.0104  0.0495  0.0065  147 HIS A C   
895  O O   . HIS A 145 ? 0.4046 0.3231 0.3219 0.0106  0.0481  0.0065  147 HIS A O   
896  C CB  . HIS A 145 ? 0.4692 0.3738 0.3808 0.0166  0.0614  0.0109  147 HIS A CB  
897  C CG  . HIS A 145 ? 0.5266 0.4152 0.4254 0.0187  0.0684  0.0116  147 HIS A CG  
898  N ND1 . HIS A 145 ? 0.5739 0.4502 0.4595 0.0146  0.0689  0.0093  147 HIS A ND1 
899  C CD2 . HIS A 145 ? 0.5402 0.4218 0.4353 0.0242  0.0756  0.0141  147 HIS A CD2 
900  C CE1 . HIS A 145 ? 0.5864 0.4462 0.4590 0.0174  0.0762  0.0104  147 HIS A CE1 
901  N NE2 . HIS A 145 ? 0.5733 0.4365 0.4522 0.0243  0.0805  0.0135  147 HIS A NE2 
902  N N   . ALA A 146 ? 0.3896 0.3145 0.3115 0.0096  0.0462  0.0061  148 ALA A N   
903  C CA  . ALA A 146 ? 0.3701 0.3065 0.3004 0.0097  0.0404  0.0057  148 ALA A CA  
904  C C   . ALA A 146 ? 0.3545 0.2980 0.2927 0.0106  0.0397  0.0071  148 ALA A C   
905  O O   . ALA A 146 ? 0.3510 0.2902 0.2852 0.0096  0.0418  0.0069  148 ALA A O   
906  C CB  . ALA A 146 ? 0.3751 0.3144 0.3010 0.0073  0.0353  0.0023  148 ALA A CB  
907  N N   . TYR A 147 ? 0.3414 0.2932 0.2879 0.0118  0.0371  0.0085  149 TYR A N   
908  C CA  . TYR A 147 ? 0.3267 0.2865 0.2811 0.0122  0.0353  0.0099  149 TYR A CA  
909  C C   . TYR A 147 ? 0.3092 0.2725 0.2623 0.0099  0.0311  0.0069  149 TYR A C   
910  O O   . TYR A 147 ? 0.3064 0.2713 0.2565 0.0092  0.0277  0.0044  149 TYR A O   
911  C CB  . TYR A 147 ? 0.3204 0.2873 0.2819 0.0125  0.0334  0.0120  149 TYR A CB  
912  C CG  . TYR A 147 ? 0.3344 0.3029 0.2993 0.0139  0.0375  0.0153  149 TYR A CG  
913  C CD1 . TYR A 147 ? 0.3421 0.3167 0.3134 0.0166  0.0401  0.0187  149 TYR A CD1 
914  C CD2 . TYR A 147 ? 0.3444 0.3092 0.3057 0.0129  0.0390  0.0152  149 TYR A CD2 
915  C CE1 . TYR A 147 ? 0.3651 0.3448 0.3406 0.0186  0.0442  0.0219  149 TYR A CE1 
916  C CE2 . TYR A 147 ? 0.3472 0.3159 0.3121 0.0136  0.0433  0.0182  149 TYR A CE2 
917  C CZ  . TYR A 147 ? 0.3538 0.3313 0.3265 0.0167  0.0460  0.0216  149 TYR A CZ  
918  O OH  . TYR A 147 ? 0.3608 0.3464 0.3385 0.0179  0.0502  0.0248  149 TYR A OH  
919  N N   . THR A 148 ? 0.3045 0.2693 0.2591 0.0092  0.0314  0.0073  150 THR A N   
920  C CA  . THR A 148 ? 0.2896 0.2595 0.2435 0.0063  0.0281  0.0045  150 THR A CA  
921  C C   . THR A 148 ? 0.2762 0.2545 0.2368 0.0074  0.0239  0.0047  150 THR A C   
922  O O   . THR A 148 ? 0.2665 0.2462 0.2323 0.0091  0.0241  0.0075  150 THR A O   
923  C CB  . THR A 148 ? 0.2961 0.2622 0.2468 0.0043  0.0303  0.0047  150 THR A CB  
924  O OG1 . THR A 148 ? 0.2933 0.2663 0.2437 0.0004  0.0271  0.0018  150 THR A OG1 
925  C CG2 . THR A 148 ? 0.2927 0.2595 0.2492 0.0076  0.0316  0.0085  150 THR A CG2 
926  N N   . SER A 149 ? 0.2808 0.2651 0.2405 0.0066  0.0204  0.0019  151 SER A N   
927  C CA  . SER A 149 ? 0.2740 0.2651 0.2379 0.0074  0.0172  0.0016  151 SER A CA  
928  C C   . SER A 149 ? 0.2741 0.2653 0.2418 0.0058  0.0184  0.0035  151 SER A C   
929  O O   . SER A 149 ? 0.2685 0.2565 0.2332 0.0036  0.0209  0.0033  151 SER A O   
930  C CB  . SER A 149 ? 0.2747 0.2740 0.2369 0.0072  0.0143  -0.0017 151 SER A CB  
931  O OG  . SER A 149 ? 0.2823 0.2823 0.2406 0.0104  0.0124  -0.0031 151 SER A OG  
932  N N   . PHE A 150 ? 0.2737 0.2671 0.2457 0.0068  0.0169  0.0055  152 PHE A N   
933  C CA  . PHE A 150 ? 0.2742 0.2694 0.2494 0.0056  0.0168  0.0071  152 PHE A CA  
934  C C   . PHE A 150 ? 0.2702 0.2681 0.2426 0.0029  0.0162  0.0040  152 PHE A C   
935  O O   . PHE A 150 ? 0.2512 0.2550 0.2227 0.0030  0.0139  0.0011  152 PHE A O   
936  C CB  . PHE A 150 ? 0.2793 0.2772 0.2581 0.0059  0.0144  0.0091  152 PHE A CB  
937  C CG  . PHE A 150 ? 0.2980 0.2949 0.2785 0.0065  0.0150  0.0118  152 PHE A CG  
938  C CD1 . PHE A 150 ? 0.3232 0.3189 0.3054 0.0078  0.0183  0.0140  152 PHE A CD1 
939  C CD2 . PHE A 150 ? 0.3039 0.3005 0.2829 0.0053  0.0126  0.0121  152 PHE A CD2 
940  C CE1 . PHE A 150 ? 0.3236 0.3208 0.3078 0.0076  0.0192  0.0163  152 PHE A CE1 
941  C CE2 . PHE A 150 ? 0.3168 0.3128 0.2960 0.0039  0.0134  0.0144  152 PHE A CE2 
942  C CZ  . PHE A 150 ? 0.3211 0.3189 0.3040 0.0049  0.0166  0.0165  152 PHE A CZ  
943  N N   . MET A 151 ? 0.2734 0.2669 0.2430 0.0010  0.0187  0.0047  153 MET A N   
944  C CA  . MET A 151 ? 0.2802 0.2749 0.2454 -0.0034 0.0189  0.0019  153 MET A CA  
945  C C   . MET A 151 ? 0.2727 0.2669 0.2391 -0.0041 0.0184  0.0035  153 MET A C   
946  O O   . MET A 151 ? 0.2689 0.2563 0.2343 -0.0022 0.0202  0.0069  153 MET A O   
947  C CB  . MET A 151 ? 0.3043 0.2903 0.2607 -0.0067 0.0226  0.0010  153 MET A CB  
948  C CG  . MET A 151 ? 0.3217 0.3078 0.2761 -0.0065 0.0231  -0.0003 153 MET A CG  
949  S SD  . MET A 151 ? 0.3590 0.3303 0.3006 -0.0100 0.0281  -0.0005 153 MET A SD  
950  C CE  . MET A 151 ? 0.3852 0.3597 0.3192 -0.0193 0.0278  -0.0045 153 MET A CE  
951  N N   . LEU A 152 ? 0.2648 0.2662 0.2325 -0.0062 0.0161  0.0013  154 LEU A N   
952  C CA  . LEU A 152 ? 0.2755 0.2755 0.2420 -0.0084 0.0159  0.0020  154 LEU A CA  
953  C C   . LEU A 152 ? 0.3000 0.2966 0.2581 -0.0145 0.0184  -0.0006 154 LEU A C   
954  O O   . LEU A 152 ? 0.2935 0.2971 0.2499 -0.0181 0.0184  -0.0042 154 LEU A O   
955  C CB  . LEU A 152 ? 0.2494 0.2571 0.2201 -0.0076 0.0128  0.0010  154 LEU A CB  
956  C CG  . LEU A 152 ? 0.2355 0.2425 0.2108 -0.0039 0.0107  0.0042  154 LEU A CG  
957  C CD1 . LEU A 152 ? 0.2349 0.2463 0.2106 -0.0032 0.0082  0.0026  154 LEU A CD1 
958  C CD2 . LEU A 152 ? 0.2365 0.2391 0.2125 -0.0039 0.0109  0.0081  154 LEU A CD2 
959  N N   . GLN A 153 ? 0.3362 0.3222 0.2879 -0.0157 0.0205  0.0013  155 GLN A N   
960  C CA  . GLN A 153 ? 0.3790 0.3566 0.3185 -0.0225 0.0236  -0.0008 155 GLN A CA  
961  C C   . GLN A 153 ? 0.4047 0.3749 0.3390 -0.0237 0.0240  0.0006  155 GLN A C   
962  O O   . GLN A 153 ? 0.4192 0.3841 0.3555 -0.0177 0.0235  0.0049  155 GLN A O   
963  C CB  . GLN A 153 ? 0.4111 0.3749 0.3415 -0.0217 0.0273  0.0003  155 GLN A CB  
964  C CG  . GLN A 153 ? 0.4460 0.3992 0.3604 -0.0306 0.0309  -0.0026 155 GLN A CG  
965  C CD  . GLN A 153 ? 0.4403 0.4078 0.3557 -0.0390 0.0296  -0.0076 155 GLN A CD  
966  O OE1 . GLN A 153 ? 0.4290 0.4079 0.3516 -0.0376 0.0278  -0.0089 155 GLN A OE1 
967  N NE2 . GLN A 153 ? 0.4347 0.4020 0.3424 -0.0474 0.0306  -0.0101 155 GLN A NE2 
968  N N   . VAL A 154 ? 0.4372 0.4079 0.3645 -0.0315 0.0249  -0.0025 156 VAL A N   
969  C CA  . VAL A 154 ? 0.4649 0.4234 0.3814 -0.0347 0.0264  -0.0017 156 VAL A CA  
970  C C   . VAL A 154 ? 0.5095 0.4472 0.4095 -0.0359 0.0309  -0.0005 156 VAL A C   
971  O O   . VAL A 154 ? 0.5201 0.4548 0.4130 -0.0410 0.0333  -0.0031 156 VAL A O   
972  C CB  . VAL A 154 ? 0.4789 0.4462 0.3930 -0.0437 0.0264  -0.0061 156 VAL A CB  
973  C CG1 . VAL A 154 ? 0.5189 0.4718 0.4200 -0.0478 0.0282  -0.0054 156 VAL A CG1 
974  C CG2 . VAL A 154 ? 0.4580 0.4436 0.3863 -0.0407 0.0226  -0.0071 156 VAL A CG2 
975  N N   . ALA A 155 ? 0.5533 0.4766 0.4465 -0.0304 0.0320  0.0036  157 ALA A N   
976  C CA  . ALA A 155 ? 0.6239 0.5231 0.4971 -0.0302 0.0369  0.0051  157 ALA A CA  
977  C C   . ALA A 155 ? 0.6895 0.5779 0.5446 -0.0429 0.0399  0.0008  157 ALA A C   
978  O O   . ALA A 155 ? 0.6444 0.5287 0.4938 -0.0461 0.0395  0.0007  157 ALA A O   
979  C CB  . ALA A 155 ? 0.6525 0.5415 0.5228 -0.0204 0.0368  0.0106  157 ALA A CB  
980  N N   . LYS A 156 ? 0.7384 0.6228 0.5841 -0.0508 0.0428  -0.0026 158 LYS A N   
981  C CA  . LYS A 156 ? 0.8163 0.6838 0.6383 -0.0640 0.0471  -0.0062 158 LYS A CA  
982  C C   . LYS A 156 ? 0.8702 0.7144 0.6731 -0.0640 0.0521  -0.0055 158 LYS A C   
983  O O   . LYS A 156 ? 0.9025 0.7471 0.7133 -0.0535 0.0520  -0.0025 158 LYS A O   
984  C CB  . LYS A 156 ? 0.8161 0.7038 0.6427 -0.0774 0.0459  -0.0120 158 LYS A CB  
985  C CG  . LYS A 156 ? 0.8017 0.7182 0.6515 -0.0752 0.0409  -0.0131 158 LYS A CG  
986  C CD  . LYS A 156 ? 0.8076 0.7493 0.6681 -0.0818 0.0390  -0.0176 158 LYS A CD  
987  C CE  . LYS A 156 ? 0.7902 0.7573 0.6740 -0.0741 0.0342  -0.0174 158 LYS A CE  
988  N NZ  . LYS A 156 ? 0.7863 0.7784 0.6788 -0.0792 0.0326  -0.0216 158 LYS A NZ  
989  N N   . ASP A 157 ? 0.9089 0.7327 0.6859 -0.0762 0.0567  -0.0084 159 ASP A N   
990  C CA  . ASP A 157 ? 0.9344 0.7351 0.6897 -0.0797 0.0618  -0.0089 159 ASP A CA  
991  C C   . ASP A 157 ? 0.9072 0.7295 0.6716 -0.0904 0.0600  -0.0137 159 ASP A C   
992  O O   . ASP A 157 ? 0.9590 0.7803 0.7093 -0.1067 0.0617  -0.0182 159 ASP A O   
993  C CB  . ASP A 157 ? 1.0097 0.7747 0.7299 -0.0873 0.0678  -0.0093 159 ASP A CB  
994  C CG  . ASP A 157 ? 1.0609 0.7985 0.7679 -0.0717 0.0709  -0.0034 159 ASP A CG  
995  O OD1 . ASP A 157 ? 1.0604 0.8121 0.7891 -0.0563 0.0674  0.0010  159 ASP A OD1 
996  O OD2 . ASP A 157 ? 1.1220 0.8241 0.7960 -0.0749 0.0769  -0.0030 159 ASP A OD2 
997  N N   . THR A 158 ? 0.8266 0.6691 0.6136 -0.0816 0.0564  -0.0125 160 THR A N   
998  C CA  . THR A 158 ? 0.7891 0.6593 0.5912 -0.0883 0.0528  -0.0164 160 THR A CA  
999  C C   . THR A 158 ? 0.7684 0.6377 0.5750 -0.0814 0.0530  -0.0149 160 THR A C   
1000 O O   . THR A 158 ? 0.7614 0.6164 0.5676 -0.0690 0.0548  -0.0105 160 THR A O   
1001 C CB  . THR A 158 ? 0.7503 0.6517 0.5789 -0.0841 0.0470  -0.0168 160 THR A CB  
1002 O OG1 . THR A 158 ? 0.7394 0.6657 0.5776 -0.0915 0.0443  -0.0208 160 THR A OG1 
1003 C CG2 . THR A 158 ? 0.7340 0.6429 0.5826 -0.0679 0.0439  -0.0124 160 THR A CG2 
1004 N N   . THR A 159 ? 0.7521 0.6385 0.5640 -0.0888 0.0510  -0.0184 161 THR A N   
1005 C CA  . THR A 159 ? 0.7364 0.6251 0.5537 -0.0835 0.0504  -0.0176 161 THR A CA  
1006 C C   . THR A 159 ? 0.6710 0.5920 0.5147 -0.0781 0.0442  -0.0182 161 THR A C   
1007 O O   . THR A 159 ? 0.6745 0.6173 0.5245 -0.0860 0.0413  -0.0217 161 THR A O   
1008 C CB  . THR A 159 ? 0.7690 0.6464 0.5656 -0.0966 0.0535  -0.0208 161 THR A CB  
1009 O OG1 . THR A 159 ? 0.8257 0.6671 0.5959 -0.0974 0.0600  -0.0191 161 THR A OG1 
1010 C CG2 . THR A 159 ? 0.7726 0.6572 0.5765 -0.0926 0.0520  -0.0206 161 THR A CG2 
1011 N N   . VAL A 160 ? 0.6180 0.5418 0.4758 -0.0649 0.0427  -0.0148 162 VAL A N   
1012 C CA  . VAL A 160 ? 0.5705 0.5201 0.4495 -0.0593 0.0373  -0.0153 162 VAL A CA  
1013 C C   . VAL A 160 ? 0.5367 0.4824 0.4171 -0.0539 0.0376  -0.0140 162 VAL A C   
1014 O O   . VAL A 160 ? 0.5324 0.4592 0.4068 -0.0475 0.0412  -0.0108 162 VAL A O   
1015 C CB  . VAL A 160 ? 0.5666 0.5252 0.4616 -0.0498 0.0344  -0.0127 162 VAL A CB  
1016 C CG1 . VAL A 160 ? 0.5506 0.4919 0.4445 -0.0403 0.0369  -0.0080 162 VAL A CG1 
1017 C CG2 . VAL A 160 ? 0.5557 0.5365 0.4682 -0.0442 0.0295  -0.0133 162 VAL A CG2 
1018 N N   . ALA A 161 ? 0.4940 0.4574 0.3814 -0.0556 0.0341  -0.0163 163 ALA A N   
1019 C CA  . ALA A 161 ? 0.4849 0.4446 0.3728 -0.0510 0.0341  -0.0153 163 ALA A CA  
1020 C C   . ALA A 161 ? 0.4497 0.4121 0.3523 -0.0382 0.0325  -0.0118 163 ALA A C   
1021 O O   . ALA A 161 ? 0.4116 0.3904 0.3275 -0.0342 0.0285  -0.0119 163 ALA A O   
1022 C CB  . ALA A 161 ? 0.4797 0.4577 0.3699 -0.0561 0.0304  -0.0186 163 ALA A CB  
1023 N N   . VAL A 162 ? 0.4510 0.3985 0.3504 -0.0324 0.0357  -0.0090 164 VAL A N   
1024 C CA  . VAL A 162 ? 0.4389 0.3906 0.3517 -0.0219 0.0343  -0.0058 164 VAL A CA  
1025 C C   . VAL A 162 ? 0.4155 0.3840 0.3379 -0.0200 0.0293  -0.0074 164 VAL A C   
1026 O O   . VAL A 162 ? 0.4223 0.3947 0.3395 -0.0247 0.0283  -0.0100 164 VAL A O   
1027 C CB  . VAL A 162 ? 0.4538 0.3890 0.3608 -0.0168 0.0391  -0.0028 164 VAL A CB  
1028 C CG1 . VAL A 162 ? 0.4661 0.3974 0.3662 -0.0194 0.0398  -0.0045 164 VAL A CG1 
1029 C CG2 . VAL A 162 ? 0.4451 0.3848 0.3650 -0.0076 0.0385  0.0008  164 VAL A CG2 
1030 N N   . LYS A 163 ? 0.4042 0.3815 0.3385 -0.0135 0.0263  -0.0059 165 LYS A N   
1031 C CA  . LYS A 163 ? 0.4128 0.4027 0.3534 -0.0102 0.0220  -0.0071 165 LYS A CA  
1032 C C   . LYS A 163 ? 0.4027 0.3853 0.3430 -0.0054 0.0229  -0.0053 165 LYS A C   
1033 O O   . LYS A 163 ? 0.3798 0.3652 0.3261 -0.0002 0.0209  -0.0039 165 LYS A O   
1034 C CB  . LYS A 163 ? 0.4254 0.4250 0.3750 -0.0065 0.0188  -0.0067 165 LYS A CB  
1035 C CG  . LYS A 163 ? 0.4653 0.4737 0.4152 -0.0113 0.0180  -0.0088 165 LYS A CG  
1036 C CD  . LYS A 163 ? 0.5060 0.5282 0.4535 -0.0157 0.0159  -0.0125 165 LYS A CD  
1037 C CE  . LYS A 163 ? 0.5191 0.5556 0.4725 -0.0091 0.0117  -0.0135 165 LYS A CE  
1038 N NZ  . LYS A 163 ? 0.5470 0.5925 0.5060 -0.0072 0.0103  -0.0139 165 LYS A NZ  
1039 N N   . ALA A 164 ? 0.5059 0.4160 0.3860 -0.0391 0.0380  -0.0098 166 ALA A N   
1040 C CA  . ALA A 164 ? 0.5090 0.4288 0.4003 -0.0329 0.0339  -0.0077 166 ALA A CA  
1041 C C   . ALA A 164 ? 0.4920 0.4182 0.3877 -0.0373 0.0365  -0.0107 166 ALA A C   
1042 O O   . ALA A 164 ? 0.5081 0.4233 0.3919 -0.0429 0.0411  -0.0126 166 ALA A O   
1043 C CB  . ALA A 164 ? 0.5151 0.4234 0.3979 -0.0255 0.0314  -0.0039 166 ALA A CB  
1044 N N   . ASP A 165 ? 0.4665 0.4091 0.3771 -0.0353 0.0340  -0.0113 167 ASP A N   
1045 C CA  . ASP A 165 ? 0.4558 0.4043 0.3706 -0.0372 0.0353  -0.0132 167 ASP A CA  
1046 C C   . ASP A 165 ? 0.4162 0.3736 0.3422 -0.0302 0.0306  -0.0106 167 ASP A C   
1047 O O   . ASP A 165 ? 0.3839 0.3439 0.3142 -0.0255 0.0270  -0.0081 167 ASP A O   
1048 C CB  . ASP A 165 ? 0.4655 0.4268 0.3856 -0.0441 0.0386  -0.0187 167 ASP A CB  
1049 C CG  . ASP A 165 ? 0.4732 0.4367 0.3923 -0.0486 0.0415  -0.0216 167 ASP A CG  
1050 O OD1 . ASP A 165 ? 0.4918 0.4424 0.4030 -0.0471 0.0419  -0.0191 167 ASP A OD1 
1051 O OD2 . ASP A 165 ? 0.4663 0.4450 0.3923 -0.0530 0.0433  -0.0265 167 ASP A OD2 
1052 N N   . VAL A 166 ? 0.3950 0.3562 0.3243 -0.0305 0.0311  -0.0115 168 VAL A N   
1053 C CA  . VAL A 166 ? 0.3676 0.3372 0.3069 -0.0250 0.0274  -0.0096 168 VAL A CA  
1054 C C   . VAL A 166 ? 0.3632 0.3452 0.3105 -0.0274 0.0283  -0.0130 168 VAL A C   
1055 O O   . VAL A 166 ? 0.3867 0.3698 0.3309 -0.0332 0.0319  -0.0166 168 VAL A O   
1056 C CB  . VAL A 166 ? 0.3664 0.3270 0.3002 -0.0213 0.0267  -0.0068 168 VAL A CB  
1057 C CG1 . VAL A 166 ? 0.3816 0.3329 0.3080 -0.0169 0.0249  -0.0038 168 VAL A CG1 
1058 C CG2 . VAL A 166 ? 0.3783 0.3300 0.3029 -0.0257 0.0309  -0.0086 168 VAL A CG2 
1059 N N   . PRO A 167 ? 0.3525 0.3443 0.3092 -0.0233 0.0251  -0.0124 169 PRO A N   
1060 C CA  . PRO A 167 ? 0.3579 0.3604 0.3210 -0.0235 0.0252  -0.0151 169 PRO A CA  
1061 C C   . PRO A 167 ? 0.3517 0.3501 0.3131 -0.0239 0.0261  -0.0144 169 PRO A C   
1062 O O   . PRO A 167 ? 0.3497 0.3380 0.3060 -0.0222 0.0258  -0.0113 169 PRO A O   
1063 C CB  . PRO A 167 ? 0.3437 0.3520 0.3132 -0.0181 0.0215  -0.0137 169 PRO A CB  
1064 C CG  . PRO A 167 ? 0.3328 0.3331 0.3000 -0.0156 0.0194  -0.0095 169 PRO A CG  
1065 C CD  . PRO A 167 ? 0.3531 0.3452 0.3132 -0.0184 0.0213  -0.0092 169 PRO A CD  
1066 N N   . THR A 168 ? 0.3552 0.3621 0.3203 -0.0258 0.0272  -0.0175 170 THR A N   
1067 C CA  . THR A 168 ? 0.3425 0.3474 0.3076 -0.0255 0.0275  -0.0169 170 THR A CA  
1068 C C   . THR A 168 ? 0.3151 0.3305 0.2887 -0.0213 0.0248  -0.0173 170 THR A C   
1069 O O   . THR A 168 ? 0.3000 0.3253 0.2782 -0.0195 0.0235  -0.0194 170 THR A O   
1070 C CB  . THR A 168 ? 0.3633 0.3654 0.3219 -0.0326 0.0321  -0.0203 170 THR A CB  
1071 O OG1 . THR A 168 ? 0.3676 0.3852 0.3321 -0.0354 0.0330  -0.0254 170 THR A OG1 
1072 C CG2 . THR A 168 ? 0.3883 0.3771 0.3353 -0.0370 0.0353  -0.0202 170 THR A CG2 
1073 N N   . LEU A 169 ? 0.3000 0.3122 0.2744 -0.0191 0.0239  -0.0152 171 LEU A N   
1074 C CA  . LEU A 169 ? 0.2822 0.3022 0.2626 -0.0159 0.0219  -0.0156 171 LEU A CA  
1075 C C   . LEU A 169 ? 0.2875 0.3066 0.2667 -0.0182 0.0237  -0.0167 171 LEU A C   
1076 O O   . LEU A 169 ? 0.2999 0.3093 0.2744 -0.0186 0.0247  -0.0144 171 LEU A O   
1077 C CB  . LEU A 169 ? 0.2656 0.2826 0.2479 -0.0111 0.0188  -0.0119 171 LEU A CB  
1078 C CG  . LEU A 169 ? 0.2537 0.2767 0.2398 -0.0077 0.0168  -0.0126 171 LEU A CG  
1079 C CD1 . LEU A 169 ? 0.2520 0.2803 0.2384 -0.0056 0.0158  -0.0146 171 LEU A CD1 
1080 C CD2 . LEU A 169 ? 0.2554 0.2741 0.2417 -0.0052 0.0149  -0.0094 171 LEU A CD2 
1081 N N   . THR A 170 ? 0.2899 0.3194 0.2724 -0.0195 0.0244  -0.0205 172 THR A N   
1082 C CA  . THR A 170 ? 0.2996 0.3305 0.2816 -0.0221 0.0261  -0.0222 172 THR A CA  
1083 C C   . THR A 170 ? 0.2890 0.3280 0.2769 -0.0170 0.0232  -0.0225 172 THR A C   
1084 O O   . THR A 170 ? 0.2730 0.3211 0.2642 -0.0135 0.0213  -0.0243 172 THR A O   
1085 C CB  . THR A 170 ? 0.3136 0.3503 0.2928 -0.0295 0.0299  -0.0275 172 THR A CB  
1086 O OG1 . THR A 170 ? 0.3411 0.3665 0.3127 -0.0334 0.0324  -0.0264 172 THR A OG1 
1087 C CG2 . THR A 170 ? 0.3219 0.3588 0.2989 -0.0337 0.0323  -0.0296 172 THR A CG2 
1088 N N   . LYS A 171 ? 0.2936 0.3281 0.2812 -0.0161 0.0231  -0.0206 173 LYS A N   
1089 C CA  . LYS A 171 ? 0.2890 0.3292 0.2805 -0.0120 0.0209  -0.0209 173 LYS A CA  
1090 C C   . LYS A 171 ? 0.3034 0.3469 0.2943 -0.0157 0.0230  -0.0236 173 LYS A C   
1091 O O   . LYS A 171 ? 0.3071 0.3419 0.2934 -0.0197 0.0256  -0.0227 173 LYS A O   
1092 C CB  . LYS A 171 ? 0.2753 0.3077 0.2669 -0.0082 0.0189  -0.0164 173 LYS A CB  
1093 C CG  . LYS A 171 ? 0.2600 0.2959 0.2535 -0.0043 0.0170  -0.0166 173 LYS A CG  
1094 C CD  . LYS A 171 ? 0.2507 0.2795 0.2436 -0.0022 0.0157  -0.0129 173 LYS A CD  
1095 C CE  . LYS A 171 ? 0.2521 0.2823 0.2446 0.0012  0.0142  -0.0133 173 LYS A CE  
1096 N NZ  . LYS A 171 ? 0.2319 0.2557 0.2232 0.0018  0.0136  -0.0102 173 LYS A NZ  
1097 N N   . GLN A 172 ? 0.3237 0.3789 0.3181 -0.0138 0.0218  -0.0269 174 GLN A N   
1098 C CA  . GLN A 172 ? 0.3459 0.4059 0.3403 -0.0167 0.0233  -0.0297 174 GLN A CA  
1099 C C   . GLN A 172 ? 0.3367 0.4044 0.3343 -0.0106 0.0203  -0.0306 174 GLN A C   
1100 O O   . GLN A 172 ? 0.3190 0.3891 0.3174 -0.0041 0.0173  -0.0300 174 GLN A O   
1101 C CB  . GLN A 172 ? 0.3858 0.4562 0.3796 -0.0236 0.0263  -0.0355 174 GLN A CB  
1102 C CG  . GLN A 172 ? 0.4113 0.4706 0.3985 -0.0309 0.0302  -0.0349 174 GLN A CG  
1103 C CD  . GLN A 172 ? 0.4271 0.4972 0.4125 -0.0394 0.0339  -0.0414 174 GLN A CD  
1104 O OE1 . GLN A 172 ? 0.4107 0.4959 0.4004 -0.0389 0.0332  -0.0455 174 GLN A OE1 
1105 N NE2 . GLN A 172 ? 0.4325 0.4955 0.4109 -0.0471 0.0380  -0.0429 174 GLN A NE2 
1106 N N   . VAL A 173 ? 0.3465 0.4166 0.3441 -0.0127 0.0213  -0.0322 175 VAL A N   
1107 C CA  . VAL A 173 ? 0.3659 0.4419 0.3651 -0.0072 0.0187  -0.0331 175 VAL A CA  
1108 C C   . VAL A 173 ? 0.3943 0.4871 0.3954 -0.0102 0.0197  -0.0396 175 VAL A C   
1109 O O   . VAL A 173 ? 0.4006 0.4945 0.4004 -0.0187 0.0234  -0.0421 175 VAL A O   
1110 C CB  . VAL A 173 ? 0.3455 0.4098 0.3431 -0.0069 0.0188  -0.0290 175 VAL A CB  
1111 C CG1 . VAL A 173 ? 0.3464 0.4065 0.3418 -0.0141 0.0225  -0.0297 175 VAL A CG1 
1112 C CG2 . VAL A 173 ? 0.3422 0.4100 0.3400 -0.0010 0.0162  -0.0295 175 VAL A CG2 
1113 N N   . ARG A 174 ? 0.4344 0.5397 0.4372 -0.0034 0.0167  -0.0427 176 ARG A N   
1114 C CA  . ARG A 174 ? 0.4833 0.6082 0.4886 -0.0055 0.0172  -0.0497 176 ARG A CA  
1115 C C   . ARG A 174 ? 0.4964 0.6182 0.5008 -0.0088 0.0184  -0.0495 176 ARG A C   
1116 O O   . ARG A 174 ? 0.4689 0.5811 0.4716 -0.0031 0.0162  -0.0455 176 ARG A O   
1117 C CB  . ARG A 174 ? 0.5246 0.6649 0.5308 0.0044  0.0132  -0.0534 176 ARG A CB  
1118 C CG  . ARG A 174 ? 0.5768 0.7424 0.5869 0.0008  0.0143  -0.0620 176 ARG A CG  
1119 C CD  . ARG A 174 ? 0.6186 0.8020 0.6292 0.0123  0.0101  -0.0664 176 ARG A CD  
1120 N NE  . ARG A 174 ? 0.6367 0.8189 0.6447 0.0194  0.0072  -0.0657 176 ARG A NE  
1121 C CZ  . ARG A 174 ? 0.7193 0.9115 0.7245 0.0319  0.0029  -0.0684 176 ARG A CZ  
1122 N NH1 . ARG A 174 ? 0.7280 0.9327 0.7327 0.0395  0.0008  -0.0719 176 ARG A NH1 
1123 N NH2 . ARG A 174 ? 0.7373 0.9259 0.7389 0.0375  0.0007  -0.0675 176 ARG A NH2 
1124 N N   . ALA A 175 ? 0.5154 0.6443 0.5198 -0.0185 0.0221  -0.0539 177 ALA A N   
1125 C CA  . ALA A 175 ? 0.5306 0.6546 0.5326 -0.0237 0.0243  -0.0539 177 ALA A CA  
1126 C C   . ALA A 175 ? 0.5657 0.7027 0.5702 -0.0174 0.0210  -0.0568 177 ALA A C   
1127 O O   . ALA A 175 ? 0.5215 0.6750 0.5287 -0.0106 0.0179  -0.0606 177 ALA A O   
1128 C CB  . ALA A 175 ? 0.5358 0.6629 0.5347 -0.0364 0.0296  -0.0584 177 ALA A CB  
1129 N N   . ASN A 176 ? 0.6393 0.7675 0.6415 -0.0187 0.0217  -0.0547 178 ASN A N   
1130 C CA  . ASN A 176 ? 0.7382 0.8758 0.7413 -0.0143 0.0193  -0.0571 178 ASN A CA  
1131 C C   . ASN A 176 ? 0.7683 0.9322 0.7744 -0.0179 0.0198  -0.0662 178 ASN A C   
1132 O O   . ASN A 176 ? 0.7299 0.8978 0.7347 -0.0299 0.0244  -0.0701 178 ASN A O   
1133 C CB  . ASN A 176 ? 0.7586 0.8810 0.7583 -0.0181 0.0214  -0.0535 178 ASN A CB  
1134 C CG  . ASN A 176 ? 0.7729 0.8944 0.7720 -0.0106 0.0182  -0.0522 178 ASN A CG  
1135 O OD1 . ASN A 176 ? 0.8310 0.9644 0.8311 -0.0023 0.0144  -0.0547 178 ASN A OD1 
1136 N ND2 . ASN A 176 ? 0.6774 0.7844 0.6738 -0.0131 0.0199  -0.0484 178 ASN A ND2 
1137 N N   . GLY A 177 ? 0.7941 0.9753 0.8029 -0.0083 0.0156  -0.0698 179 GLY A N   
1138 C CA  . GLY A 177 ? 0.8511 1.0615 0.8633 -0.0090 0.0149  -0.0791 179 GLY A CA  
1139 C C   . GLY A 177 ? 0.8969 1.1207 0.9112 -0.0223 0.0198  -0.0853 179 GLY A C   
1140 O O   . GLY A 177 ? 0.9333 1.1788 0.9496 -0.0287 0.0213  -0.0932 179 GLY A O   
1141 N N   . SER A 178 ? 0.9386 1.1502 0.9517 -0.0268 0.0223  -0.0821 180 SER A N   
1142 C CA  . SER A 178 ? 0.9193 1.1382 0.9318 -0.0402 0.0275  -0.0871 180 SER A CA  
1143 C C   . SER A 178 ? 0.8609 1.0930 0.8773 -0.0349 0.0256  -0.0896 180 SER A C   
1144 O O   . SER A 178 ? 0.9006 1.1505 0.9184 -0.0436 0.0288  -0.0968 180 SER A O   
1145 C CB  . SER A 178 ? 0.9065 1.0971 0.9118 -0.0495 0.0323  -0.0812 180 SER A CB  
1146 O OG  . SER A 178 ? 0.8662 1.0568 0.8680 -0.0611 0.0374  -0.0844 180 SER A OG  
1147 N N   . GLN A 179 ? 0.8295 1.0529 0.8464 -0.0216 0.0209  -0.0841 181 GLN A N   
1148 C CA  . GLN A 179 ? 0.8493 1.0833 0.8687 -0.0131 0.0181  -0.0857 181 GLN A CA  
1149 C C   . GLN A 179 ? 0.8041 1.0279 0.8223 -0.0214 0.0219  -0.0838 181 GLN A C   
1150 O O   . GLN A 179 ? 0.8404 1.0706 0.8602 -0.0155 0.0200  -0.0845 181 GLN A O   
1151 C CB  . GLN A 179 ? 0.8761 1.1449 0.9002 -0.0092 0.0162  -0.0957 181 GLN A CB  
1152 C CG  . GLN A 179 ? 0.8828 1.1604 0.9065 0.0051  0.0105  -0.0965 181 GLN A CG  
1153 C CD  . GLN A 179 ? 0.9104 1.1804 0.9324 0.0012  0.0112  -0.0950 181 GLN A CD  
1154 O OE1 . GLN A 179 ? 0.9028 1.1519 0.9206 0.0081  0.0089  -0.0880 181 GLN A OE1 
1155 N NE2 . GLN A 179 ? 0.8772 1.1642 0.9019 -0.0104 0.0147  -0.1019 181 GLN A NE2 
1156 N N   . ASN A 180 ? 0.7257 0.9325 0.7398 -0.0335 0.0268  -0.0811 182 ASN A N   
1157 C CA  . ASN A 180 ? 0.6913 0.8836 0.7020 -0.0398 0.0300  -0.0782 182 ASN A CA  
1158 C C   . ASN A 180 ? 0.5938 0.7564 0.6005 -0.0363 0.0293  -0.0683 182 ASN A C   
1159 O O   . ASN A 180 ? 0.5852 0.7383 0.5910 -0.0322 0.0275  -0.0645 182 ASN A O   
1160 C CB  . ASN A 180 ? 0.7366 0.9340 0.7434 -0.0560 0.0366  -0.0841 182 ASN A CB  
1161 C CG  . ASN A 180 ? 0.7523 0.9389 0.7530 -0.0653 0.0404  -0.0840 182 ASN A CG  
1162 O OD1 . ASN A 180 ? 0.7773 0.9526 0.7777 -0.0594 0.0380  -0.0791 182 ASN A OD1 
1163 N ND2 . ASN A 180 ? 0.7679 0.9570 0.7625 -0.0802 0.0466  -0.0895 182 ASN A ND2 
1164 N N   . TYR A 181 ? 0.5189 0.6687 0.5231 -0.0377 0.0304  -0.0646 183 TYR A N   
1165 C CA  . TYR A 181 ? 0.4574 0.5831 0.4586 -0.0332 0.0291  -0.0560 183 TYR A CA  
1166 C C   . TYR A 181 ? 0.4401 0.5473 0.4337 -0.0423 0.0337  -0.0535 183 TYR A C   
1167 O O   . TYR A 181 ? 0.4674 0.5767 0.4564 -0.0526 0.0383  -0.0578 183 TYR A O   
1168 C CB  . TYR A 181 ? 0.4374 0.5613 0.4398 -0.0281 0.0272  -0.0539 183 TYR A CB  
1169 C CG  . TYR A 181 ? 0.4403 0.5754 0.4468 -0.0166 0.0223  -0.0547 183 TYR A CG  
1170 C CD1 . TYR A 181 ? 0.4475 0.6060 0.4577 -0.0141 0.0212  -0.0616 183 TYR A CD1 
1171 C CD2 . TYR A 181 ? 0.4354 0.5575 0.4407 -0.0080 0.0188  -0.0487 183 TYR A CD2 
1172 C CE1 . TYR A 181 ? 0.4614 0.6277 0.4725 -0.0017 0.0165  -0.0622 183 TYR A CE1 
1173 C CE2 . TYR A 181 ? 0.4474 0.5753 0.4527 0.0027  0.0146  -0.0491 183 TYR A CE2 
1174 C CZ  . TYR A 181 ? 0.4793 0.6283 0.4868 0.0067  0.0133  -0.0556 183 TYR A CZ  
1175 O OH  . TYR A 181 ? 0.5160 0.6668 0.5205 0.0189  0.0091  -0.0554 183 TYR A OH  
1176 N N   . THR A 182 ? 0.4076 0.4968 0.3989 -0.0382 0.0325  -0.0469 184 THR A N   
1177 C CA  . THR A 182 ? 0.4008 0.4709 0.3835 -0.0440 0.0361  -0.0439 184 THR A CA  
1178 C C   . THR A 182 ? 0.3650 0.4190 0.3471 -0.0367 0.0337  -0.0365 184 THR A C   
1179 O O   . THR A 182 ? 0.3408 0.3989 0.3291 -0.0288 0.0295  -0.0342 184 THR A O   
1180 C CB  . THR A 182 ? 0.4232 0.4964 0.4040 -0.0482 0.0379  -0.0468 184 THR A CB  
1181 O OG1 . THR A 182 ? 0.4592 0.5131 0.4291 -0.0542 0.0421  -0.0448 184 THR A OG1 
1182 C CG2 . THR A 182 ? 0.4128 0.4887 0.3994 -0.0397 0.0338  -0.0442 184 THR A CG2 
1183 N N   . ALA A 183 ? 0.3510 0.3873 0.3247 -0.0392 0.0363  -0.0334 185 ALA A N   
1184 C CA  . ALA A 183 ? 0.3355 0.3587 0.3082 -0.0327 0.0342  -0.0272 185 ALA A CA  
1185 C C   . ALA A 183 ? 0.3265 0.3504 0.3032 -0.0276 0.0319  -0.0250 185 ALA A C   
1186 O O   . ALA A 183 ? 0.3258 0.3467 0.3057 -0.0215 0.0292  -0.0211 185 ALA A O   
1187 C CB  . ALA A 183 ? 0.3513 0.3566 0.3123 -0.0358 0.0377  -0.0252 185 ALA A CB  
1188 N N   . ALA A 184 ? 0.3350 0.3631 0.3113 -0.0306 0.0332  -0.0278 186 ALA A N   
1189 C CA  . ALA A 184 ? 0.3327 0.3603 0.3120 -0.0259 0.0312  -0.0257 186 ALA A CA  
1190 C C   . ALA A 184 ? 0.3341 0.3714 0.3147 -0.0290 0.0319  -0.0299 186 ALA A C   
1191 O O   . ALA A 184 ? 0.3601 0.4005 0.3368 -0.0364 0.0351  -0.0342 186 ALA A O   
1192 C CB  . ALA A 184 ? 0.3421 0.3540 0.3149 -0.0246 0.0326  -0.0217 186 ALA A CB  
1193 N N   . THR A 185 ? 0.3147 0.3565 0.3001 -0.0237 0.0290  -0.0289 187 THR A N   
1194 C CA  . THR A 185 ? 0.3225 0.3747 0.3097 -0.0249 0.0288  -0.0328 187 THR A CA  
1195 C C   . THR A 185 ? 0.3130 0.3606 0.3014 -0.0195 0.0267  -0.0296 187 THR A C   
1196 O O   . THR A 185 ? 0.2996 0.3367 0.2874 -0.0160 0.0261  -0.0249 187 THR A O   
1197 C CB  . THR A 185 ? 0.3318 0.4016 0.3240 -0.0233 0.0266  -0.0372 187 THR A CB  
1198 O OG1 . THR A 185 ? 0.3373 0.4200 0.3303 -0.0263 0.0272  -0.0425 187 THR A OG1 
1199 C CG2 . THR A 185 ? 0.3245 0.3961 0.3204 -0.0140 0.0222  -0.0347 187 THR A CG2 
1200 N N   . ASP A 186 ? 0.3182 0.3740 0.3079 -0.0191 0.0259  -0.0324 188 ASP A N   
1201 C CA  . ASP A 186 ? 0.3094 0.3609 0.2997 -0.0140 0.0240  -0.0296 188 ASP A CA  
1202 C C   . ASP A 186 ? 0.3182 0.3812 0.3112 -0.0083 0.0204  -0.0320 188 ASP A C   
1203 O O   . ASP A 186 ? 0.3482 0.4256 0.3429 -0.0093 0.0199  -0.0371 188 ASP A O   
1204 C CB  . ASP A 186 ? 0.3123 0.3570 0.2988 -0.0177 0.0266  -0.0294 188 ASP A CB  
1205 C CG  . ASP A 186 ? 0.3222 0.3746 0.3066 -0.0244 0.0290  -0.0347 188 ASP A CG  
1206 O OD1 . ASP A 186 ? 0.3247 0.3932 0.3125 -0.0238 0.0272  -0.0393 188 ASP A OD1 
1207 O OD2 . ASP A 186 ? 0.3221 0.3642 0.3001 -0.0299 0.0327  -0.0343 188 ASP A OD2 
1208 N N   . TYR A 187 ? 0.3131 0.3698 0.3054 -0.0022 0.0180  -0.0286 189 TYR A N   
1209 C CA  . TYR A 187 ? 0.3441 0.4065 0.3351 0.0047  0.0146  -0.0301 189 TYR A CA  
1210 C C   . TYR A 187 ? 0.3377 0.3909 0.3256 0.0072  0.0141  -0.0273 189 TYR A C   
1211 O O   . TYR A 187 ? 0.3333 0.3772 0.3213 0.0039  0.0162  -0.0242 189 TYR A O   
1212 C CB  . TYR A 187 ? 0.3392 0.4008 0.3291 0.0099  0.0123  -0.0290 189 TYR A CB  
1213 C CG  . TYR A 187 ? 0.3503 0.4254 0.3428 0.0100  0.0117  -0.0332 189 TYR A CG  
1214 C CD1 . TYR A 187 ? 0.3563 0.4313 0.3514 0.0048  0.0138  -0.0330 189 TYR A CD1 
1215 C CD2 . TYR A 187 ? 0.3656 0.4534 0.3570 0.0162  0.0089  -0.0375 189 TYR A CD2 
1216 C CE1 . TYR A 187 ? 0.3566 0.4442 0.3540 0.0041  0.0137  -0.0371 189 TYR A CE1 
1217 C CE2 . TYR A 187 ? 0.3703 0.4729 0.3646 0.0165  0.0085  -0.0419 189 TYR A CE2 
1218 C CZ  . TYR A 187 ? 0.3682 0.4706 0.3657 0.0099  0.0110  -0.0417 189 TYR A CZ  
1219 O OH  . TYR A 187 ? 0.3861 0.5028 0.3862 0.0092  0.0111  -0.0462 189 TYR A OH  
1220 N N   . ARG A 188 ? 0.3536 0.4095 0.3380 0.0133  0.0114  -0.0287 190 ARG A N   
1221 C CA  . ARG A 188 ? 0.3529 0.3984 0.3320 0.0164  0.0107  -0.0261 190 ARG A CA  
1222 C C   . ARG A 188 ? 0.3411 0.3756 0.3144 0.0206  0.0094  -0.0230 190 ARG A C   
1223 O O   . ARG A 188 ? 0.3345 0.3717 0.3065 0.0240  0.0079  -0.0239 190 ARG A O   
1224 C CB  . ARG A 188 ? 0.3741 0.4263 0.3498 0.0211  0.0086  -0.0294 190 ARG A CB  
1225 C CG  . ARG A 188 ? 0.3947 0.4584 0.3753 0.0157  0.0102  -0.0331 190 ARG A CG  
1226 C CD  . ARG A 188 ? 0.4190 0.4879 0.3964 0.0192  0.0085  -0.0358 190 ARG A CD  
1227 N NE  . ARG A 188 ? 0.4486 0.5281 0.4227 0.0277  0.0047  -0.0394 190 ARG A NE  
1228 C CZ  . ARG A 188 ? 0.4662 0.5374 0.4314 0.0369  0.0018  -0.0380 190 ARG A CZ  
1229 N NH1 . ARG A 188 ? 0.4606 0.5131 0.4193 0.0374  0.0026  -0.0332 190 ARG A NH1 
1230 N NH2 . ARG A 188 ? 0.4939 0.5754 0.4550 0.0458  -0.0017 -0.0417 190 ARG A NH2 
1231 N N   . ILE A 189 ? 0.3398 0.3624 0.3092 0.0197  0.0105  -0.0198 191 ILE A N   
1232 C CA  . ILE A 189 ? 0.3546 0.3646 0.3159 0.0220  0.0100  -0.0172 191 ILE A CA  
1233 C C   . ILE A 189 ? 0.3872 0.3953 0.3386 0.0302  0.0071  -0.0191 191 ILE A C   
1234 O O   . ILE A 189 ? 0.3755 0.3880 0.3248 0.0338  0.0057  -0.0213 191 ILE A O   
1235 C CB  . ILE A 189 ? 0.3365 0.3361 0.2945 0.0186  0.0121  -0.0146 191 ILE A CB  
1236 C CG1 . ILE A 189 ? 0.3195 0.3215 0.2862 0.0124  0.0146  -0.0128 191 ILE A CG1 
1237 C CG2 . ILE A 189 ? 0.3439 0.3296 0.2900 0.0204  0.0119  -0.0130 191 ILE A CG2 
1238 C CD1 . ILE A 189 ? 0.3193 0.3155 0.2847 0.0092  0.0167  -0.0111 191 ILE A CD1 
1239 N N   . GLY A 190 ? 0.4142 0.4159 0.3591 0.0334  0.0061  -0.0183 192 GLY A N   
1240 C CA  . GLY A 190 ? 0.4422 0.4382 0.3742 0.0428  0.0033  -0.0197 192 GLY A CA  
1241 C C   . GLY A 190 ? 0.4695 0.4810 0.4058 0.0481  0.0009  -0.0234 192 GLY A C   
1242 O O   . GLY A 190 ? 0.5396 0.5464 0.4650 0.0567  -0.0014 -0.0244 192 GLY A O   
1243 N N   . GLN A 191 ? 0.4515 0.4801 0.4017 0.0433  0.0016  -0.0256 193 GLN A N   
1244 C CA  . GLN A 191 ? 0.4664 0.5126 0.4216 0.0467  -0.0001 -0.0300 193 GLN A CA  
1245 C C   . GLN A 191 ? 0.4565 0.5005 0.4131 0.0455  0.0003  -0.0287 193 GLN A C   
1246 O O   . GLN A 191 ? 0.4346 0.4721 0.3959 0.0379  0.0029  -0.0254 193 GLN A O   
1247 C CB  . GLN A 191 ? 0.4956 0.5589 0.4628 0.0401  0.0013  -0.0332 193 GLN A CB  
1248 C CG  . GLN A 191 ? 0.5528 0.6245 0.5189 0.0429  0.0000  -0.0365 193 GLN A CG  
1249 C CD  . GLN A 191 ? 0.5916 0.6787 0.5679 0.0345  0.0022  -0.0400 193 GLN A CD  
1250 O OE1 . GLN A 191 ? 0.5951 0.6826 0.5778 0.0261  0.0052  -0.0392 193 GLN A OE1 
1251 N NE2 . GLN A 191 ? 0.6508 0.7500 0.6272 0.0365  0.0010  -0.0442 193 GLN A NE2 
1252 N N   . ASN A 192 ? 0.4574 0.5070 0.4094 0.0534  -0.0021 -0.0313 194 ASN A N   
1253 C CA  . ASN A 192 ? 0.4512 0.4994 0.4033 0.0535  -0.0020 -0.0306 194 ASN A CA  
1254 C C   . ASN A 192 ? 0.4219 0.4872 0.3878 0.0462  -0.0003 -0.0332 194 ASN A C   
1255 O O   . ASN A 192 ? 0.4306 0.5136 0.4025 0.0459  -0.0006 -0.0378 194 ASN A O   
1256 C CB  . ASN A 192 ? 0.4667 0.5142 0.4074 0.0657  -0.0052 -0.0328 194 ASN A CB  
1257 C CG  . ASN A 192 ? 0.4896 0.5132 0.4125 0.0715  -0.0059 -0.0293 194 ASN A CG  
1258 O OD1 . ASN A 192 ? 0.4874 0.4941 0.4069 0.0650  -0.0035 -0.0250 194 ASN A OD1 
1259 N ND2 . ASN A 192 ? 0.5260 0.5480 0.4362 0.0838  -0.0090 -0.0317 194 ASN A ND2 
1260 N N   . ILE A 193 ? 0.4031 0.4625 0.3729 0.0398  0.0017  -0.0303 195 ILE A N   
1261 C CA  . ILE A 193 ? 0.3885 0.4588 0.3690 0.0315  0.0041  -0.0318 195 ILE A CA  
1262 C C   . ILE A 193 ? 0.3741 0.4462 0.3548 0.0325  0.0039  -0.0322 195 ILE A C   
1263 O O   . ILE A 193 ? 0.3508 0.4093 0.3257 0.0345  0.0034  -0.0286 195 ILE A O   
1264 C CB  . ILE A 193 ? 0.3751 0.4361 0.3594 0.0230  0.0070  -0.0280 195 ILE A CB  
1265 C CG1 . ILE A 193 ? 0.3902 0.4480 0.3733 0.0226  0.0073  -0.0274 195 ILE A CG1 
1266 C CG2 . ILE A 193 ? 0.3698 0.4386 0.3612 0.0154  0.0096  -0.0297 195 ILE A CG2 
1267 C CD1 . ILE A 193 ? 0.3886 0.4353 0.3733 0.0168  0.0097  -0.0233 195 ILE A CD1 
1268 N N   . LEU A 194 ? 0.3833 0.4722 0.3699 0.0307  0.0043  -0.0368 196 LEU A N   
1269 C CA  . LEU A 194 ? 0.4154 0.5090 0.4025 0.0320  0.0040  -0.0381 196 LEU A CA  
1270 C C   . LEU A 194 ? 0.3726 0.4612 0.3646 0.0225  0.0072  -0.0358 196 LEU A C   
1271 O O   . LEU A 194 ? 0.3484 0.4423 0.3453 0.0147  0.0098  -0.0373 196 LEU A O   
1272 C CB  . LEU A 194 ? 0.4743 0.5910 0.4649 0.0347  0.0031  -0.0452 196 LEU A CB  
1273 C CG  . LEU A 194 ? 0.5300 0.6544 0.5198 0.0394  0.0020  -0.0477 196 LEU A CG  
1274 C CD1 . LEU A 194 ? 0.5704 0.6832 0.5492 0.0516  -0.0013 -0.0455 196 LEU A CD1 
1275 C CD2 . LEU A 194 ? 0.5512 0.7025 0.5465 0.0397  0.0019  -0.0557 196 LEU A CD2 
1276 N N   . PHE A 195 ? 0.3716 0.4495 0.3608 0.0234  0.0070  -0.0324 197 PHE A N   
1277 C CA  . PHE A 195 ? 0.3384 0.4102 0.3306 0.0161  0.0094  -0.0298 197 PHE A CA  
1278 C C   . PHE A 195 ? 0.3464 0.4247 0.3391 0.0170  0.0093  -0.0319 197 PHE A C   
1279 O O   . PHE A 195 ? 0.3340 0.4161 0.3230 0.0246  0.0069  -0.0337 197 PHE A O   
1280 C CB  . PHE A 195 ? 0.3180 0.3730 0.3069 0.0156  0.0094  -0.0241 197 PHE A CB  
1281 C CG  . PHE A 195 ? 0.2962 0.3461 0.2860 0.0129  0.0103  -0.0222 197 PHE A CG  
1282 C CD1 . PHE A 195 ? 0.2807 0.3288 0.2740 0.0065  0.0128  -0.0211 197 PHE A CD1 
1283 C CD2 . PHE A 195 ? 0.2965 0.3426 0.2821 0.0172  0.0088  -0.0217 197 PHE A CD2 
1284 C CE1 . PHE A 195 ? 0.2822 0.3259 0.2758 0.0047  0.0137  -0.0195 197 PHE A CE1 
1285 C CE2 . PHE A 195 ? 0.2884 0.3303 0.2749 0.0146  0.0099  -0.0200 197 PHE A CE2 
1286 C CZ  . PHE A 195 ? 0.2840 0.3253 0.2750 0.0085  0.0122  -0.0190 197 PHE A CZ  
1287 N N   . GLN A 196 ? 0.3500 0.4282 0.3461 0.0097  0.0119  -0.0317 198 GLN A N   
1288 C CA  . GLN A 196 ? 0.3617 0.4458 0.3584 0.0091  0.0123  -0.0338 198 GLN A CA  
1289 C C   . GLN A 196 ? 0.3475 0.4203 0.3439 0.0032  0.0143  -0.0302 198 GLN A C   
1290 O O   . GLN A 196 ? 0.3348 0.4031 0.3319 -0.0029 0.0167  -0.0291 198 GLN A O   
1291 C CB  . GLN A 196 ? 0.3820 0.4846 0.3826 0.0057  0.0139  -0.0403 198 GLN A CB  
1292 C CG  . GLN A 196 ? 0.4234 0.5352 0.4247 0.0058  0.0143  -0.0436 198 GLN A CG  
1293 C CD  . GLN A 196 ? 0.4416 0.5739 0.4469 0.0008  0.0164  -0.0509 198 GLN A CD  
1294 O OE1 . GLN A 196 ? 0.4682 0.6180 0.4750 0.0069  0.0144  -0.0560 198 GLN A OE1 
1295 N NE2 . GLN A 196 ? 0.4319 0.5615 0.4375 -0.0098 0.0203  -0.0515 198 GLN A NE2 
1296 N N   . ILE A 197 ? 0.3470 0.4148 0.3412 0.0060  0.0132  -0.0283 199 ILE A N   
1297 C CA  . ILE A 197 ? 0.3532 0.4120 0.3467 0.0016  0.0146  -0.0253 199 ILE A CA  
1298 C C   . ILE A 197 ? 0.3531 0.4199 0.3470 0.0008  0.0153  -0.0286 199 ILE A C   
1299 O O   . ILE A 197 ? 0.3472 0.4192 0.3398 0.0068  0.0134  -0.0303 199 ILE A O   
1300 C CB  . ILE A 197 ? 0.3566 0.4027 0.3468 0.0045  0.0128  -0.0205 199 ILE A CB  
1301 C CG1 . ILE A 197 ? 0.3544 0.3943 0.3444 0.0044  0.0126  -0.0179 199 ILE A CG1 
1302 C CG2 . ILE A 197 ? 0.3764 0.4159 0.3660 0.0009  0.0138  -0.0180 199 ILE A CG2 
1303 C CD1 . ILE A 197 ? 0.3521 0.3819 0.3379 0.0068  0.0111  -0.0143 199 ILE A CD1 
1304 N N   . THR A 198 ? 0.3498 0.4168 0.3442 -0.0063 0.0183  -0.0296 200 THR A N   
1305 C CA  . THR A 198 ? 0.3679 0.4423 0.3624 -0.0093 0.0200  -0.0332 200 THR A CA  
1306 C C   . THR A 198 ? 0.3663 0.4281 0.3576 -0.0118 0.0207  -0.0293 200 THR A C   
1307 O O   . THR A 198 ? 0.3701 0.4218 0.3586 -0.0165 0.0227  -0.0270 200 THR A O   
1308 C CB  . THR A 198 ? 0.3804 0.4648 0.3758 -0.0169 0.0235  -0.0383 200 THR A CB  
1309 O OG1 . THR A 198 ? 0.3929 0.4922 0.3919 -0.0124 0.0218  -0.0422 200 THR A OG1 
1310 C CG2 . THR A 198 ? 0.3963 0.4862 0.3904 -0.0233 0.0266  -0.0420 200 THR A CG2 
1311 N N   . ALA A 199 ? 0.3665 0.4282 0.3570 -0.0082 0.0192  -0.0288 201 ALA A N   
1312 C CA  . ALA A 199 ? 0.3557 0.4075 0.3432 -0.0106 0.0199  -0.0260 201 ALA A CA  
1313 C C   . ALA A 199 ? 0.3640 0.4237 0.3511 -0.0150 0.0225  -0.0303 201 ALA A C   
1314 O O   . ALA A 199 ? 0.3784 0.4508 0.3678 -0.0118 0.0218  -0.0342 201 ALA A O   
1315 C CB  . ALA A 199 ? 0.3410 0.3864 0.3268 -0.0049 0.0170  -0.0227 201 ALA A CB  
1316 N N   . THR A 200 ? 0.3731 0.4255 0.3563 -0.0218 0.0255  -0.0299 202 THR A N   
1317 C CA  . THR A 200 ? 0.3858 0.4414 0.3666 -0.0265 0.0281  -0.0329 202 THR A CA  
1318 C C   . THR A 200 ? 0.3835 0.4284 0.3616 -0.0238 0.0265  -0.0287 202 THR A C   
1319 O O   . THR A 200 ? 0.3851 0.4187 0.3618 -0.0211 0.0245  -0.0237 202 THR A O   
1320 C CB  . THR A 200 ? 0.3972 0.4481 0.3721 -0.0361 0.0329  -0.0352 202 THR A CB  
1321 O OG1 . THR A 200 ? 0.4048 0.4370 0.3734 -0.0363 0.0329  -0.0298 202 THR A OG1 
1322 C CG2 . THR A 200 ? 0.4121 0.4716 0.3887 -0.0397 0.0347  -0.0389 202 THR A CG2 
1323 N N   . LEU A 201 ? 0.3867 0.4362 0.3641 -0.0249 0.0274  -0.0311 203 LEU A N   
1324 C CA  . LEU A 201 ? 0.3819 0.4220 0.3563 -0.0229 0.0260  -0.0276 203 LEU A CA  
1325 C C   . LEU A 201 ? 0.3803 0.4111 0.3480 -0.0299 0.0294  -0.0275 203 LEU A C   
1326 O O   . LEU A 201 ? 0.4004 0.4334 0.3652 -0.0366 0.0332  -0.0310 203 LEU A O   
1327 C CB  . LEU A 201 ? 0.3897 0.4396 0.3665 -0.0181 0.0245  -0.0300 203 LEU A CB  
1328 C CG  . LEU A 201 ? 0.3998 0.4546 0.3793 -0.0100 0.0211  -0.0298 203 LEU A CG  
1329 C CD1 . LEU A 201 ? 0.4087 0.4712 0.3877 -0.0039 0.0197  -0.0324 203 LEU A CD1 
1330 C CD2 . LEU A 201 ? 0.4066 0.4479 0.3842 -0.0072 0.0186  -0.0240 203 LEU A CD2 
1331 N N   . PRO A 202 ? 0.3714 0.3900 0.3348 -0.0288 0.0283  -0.0233 204 PRO A N   
1332 C CA  . PRO A 202 ? 0.3863 0.3937 0.3410 -0.0343 0.0314  -0.0229 204 PRO A CA  
1333 C C   . PRO A 202 ? 0.4016 0.4150 0.3546 -0.0391 0.0343  -0.0273 204 PRO A C   
1334 O O   . PRO A 202 ? 0.3879 0.4121 0.3466 -0.0355 0.0325  -0.0289 204 PRO A O   
1335 C CB  . PRO A 202 ? 0.3852 0.3819 0.3377 -0.0297 0.0282  -0.0176 204 PRO A CB  
1336 C CG  . PRO A 202 ? 0.3732 0.3780 0.3325 -0.0244 0.0249  -0.0172 204 PRO A CG  
1337 C CD  . PRO A 202 ? 0.3658 0.3810 0.3312 -0.0226 0.0244  -0.0194 204 PRO A CD  
1338 N N   . SER A 203 ? 0.4202 0.4260 0.3641 -0.0469 0.0388  -0.0292 205 SER A N   
1339 C CA  . SER A 203 ? 0.4365 0.4480 0.3773 -0.0536 0.0427  -0.0342 205 SER A CA  
1340 C C   . SER A 203 ? 0.4193 0.4302 0.3614 -0.0494 0.0404  -0.0323 205 SER A C   
1341 O O   . SER A 203 ? 0.4341 0.4569 0.3787 -0.0515 0.0419  -0.0368 205 SER A O   
1342 C CB  . SER A 203 ? 0.4473 0.4455 0.3746 -0.0632 0.0482  -0.0358 205 SER A CB  
1343 O OG  . SER A 203 ? 0.4514 0.4284 0.3686 -0.0607 0.0473  -0.0303 205 SER A OG  
1344 N N   . ASN A 204 ? 0.3964 0.3960 0.3373 -0.0435 0.0367  -0.0265 206 ASN A N   
1345 C CA  . ASN A 204 ? 0.3760 0.3738 0.3172 -0.0399 0.0344  -0.0245 206 ASN A CA  
1346 C C   . ASN A 204 ? 0.3613 0.3671 0.3109 -0.0321 0.0299  -0.0230 206 ASN A C   
1347 O O   . ASN A 204 ? 0.3597 0.3598 0.3083 -0.0287 0.0274  -0.0198 206 ASN A O   
1348 C CB  . ASN A 204 ? 0.3631 0.3437 0.2956 -0.0394 0.0336  -0.0199 206 ASN A CB  
1349 C CG  . ASN A 204 ? 0.3518 0.3252 0.2840 -0.0349 0.0308  -0.0155 206 ASN A CG  
1350 O OD1 . ASN A 204 ? 0.3352 0.3144 0.2729 -0.0334 0.0300  -0.0158 206 ASN A OD1 
1351 N ND2 . ASN A 204 ? 0.3348 0.2965 0.2604 -0.0326 0.0292  -0.0118 206 ASN A ND2 
1352 N N   . TYR A 205 ? 0.3651 0.3830 0.3213 -0.0298 0.0293  -0.0255 207 TYR A N   
1353 C CA  . TYR A 205 ? 0.3692 0.3917 0.3301 -0.0221 0.0255  -0.0243 207 TYR A CA  
1354 C C   . TYR A 205 ? 0.3879 0.4106 0.3470 -0.0192 0.0245  -0.0245 207 TYR A C   
1355 O O   . TYR A 205 ? 0.3915 0.4077 0.3492 -0.0147 0.0216  -0.0211 207 TYR A O   
1356 C CB  . TYR A 205 ? 0.3667 0.4029 0.3330 -0.0197 0.0254  -0.0281 207 TYR A CB  
1357 C CG  . TYR A 205 ? 0.3664 0.4048 0.3343 -0.0114 0.0218  -0.0270 207 TYR A CG  
1358 C CD1 . TYR A 205 ? 0.3623 0.3920 0.3297 -0.0085 0.0193  -0.0227 207 TYR A CD1 
1359 C CD2 . TYR A 205 ? 0.3665 0.4157 0.3351 -0.0063 0.0213  -0.0308 207 TYR A CD2 
1360 C CE1 . TYR A 205 ? 0.3661 0.3949 0.3321 -0.0017 0.0167  -0.0219 207 TYR A CE1 
1361 C CE2 . TYR A 205 ? 0.3818 0.4297 0.3484 0.0020  0.0183  -0.0299 207 TYR A CE2 
1362 C CZ  . TYR A 205 ? 0.3841 0.4206 0.3486 0.0039  0.0162  -0.0253 207 TYR A CZ  
1363 O OH  . TYR A 205 ? 0.4026 0.4354 0.3622 0.0116  0.0138  -0.0248 207 TYR A OH  
1364 N N   . ALA A 206 ? 0.4056 0.4352 0.3638 -0.0223 0.0272  -0.0286 208 ALA A N   
1365 C CA  . ALA A 206 ? 0.4133 0.4446 0.3698 -0.0189 0.0265  -0.0295 208 ALA A CA  
1366 C C   . ALA A 206 ? 0.4130 0.4292 0.3640 -0.0204 0.0257  -0.0249 208 ALA A C   
1367 O O   . ALA A 206 ? 0.4289 0.4429 0.3775 -0.0167 0.0242  -0.0242 208 ALA A O   
1368 C CB  . ALA A 206 ? 0.4168 0.4621 0.3745 -0.0222 0.0298  -0.0358 208 ALA A CB  
1369 N N   . ASP A 207 ? 0.4124 0.4184 0.3604 -0.0246 0.0263  -0.0219 209 ASP A N   
1370 C CA  . ASP A 207 ? 0.4333 0.4265 0.3759 -0.0252 0.0251  -0.0178 209 ASP A CA  
1371 C C   . ASP A 207 ? 0.4114 0.4001 0.3549 -0.0205 0.0212  -0.0138 209 ASP A C   
1372 O O   . ASP A 207 ? 0.4123 0.3934 0.3520 -0.0206 0.0198  -0.0110 209 ASP A O   
1373 C CB  . ASP A 207 ? 0.4665 0.4500 0.4036 -0.0297 0.0268  -0.0162 209 ASP A CB  
1374 C CG  . ASP A 207 ? 0.5107 0.4932 0.4424 -0.0364 0.0314  -0.0198 209 ASP A CG  
1375 O OD1 . ASP A 207 ? 0.4913 0.4821 0.4244 -0.0379 0.0332  -0.0235 209 ASP A OD1 
1376 O OD2 . ASP A 207 ? 0.5673 0.5398 0.4918 -0.0400 0.0335  -0.0190 209 ASP A OD2 
1377 N N   . PHE A 208 ? 0.3928 0.3861 0.3404 -0.0171 0.0196  -0.0138 210 PHE A N   
1378 C CA  . PHE A 208 ? 0.3655 0.3543 0.3125 -0.0138 0.0166  -0.0108 210 PHE A CA  
1379 C C   . PHE A 208 ? 0.3788 0.3675 0.3227 -0.0100 0.0159  -0.0118 210 PHE A C   
1380 O O   . PHE A 208 ? 0.3729 0.3687 0.3177 -0.0072 0.0168  -0.0152 210 PHE A O   
1381 C CB  . PHE A 208 ? 0.3343 0.3260 0.2853 -0.0124 0.0158  -0.0102 210 PHE A CB  
1382 C CG  . PHE A 208 ? 0.3006 0.2901 0.2528 -0.0151 0.0161  -0.0086 210 PHE A CG  
1383 C CD1 . PHE A 208 ? 0.2987 0.2894 0.2506 -0.0181 0.0188  -0.0105 210 PHE A CD1 
1384 C CD2 . PHE A 208 ? 0.2772 0.2626 0.2289 -0.0147 0.0141  -0.0055 210 PHE A CD2 
1385 C CE1 . PHE A 208 ? 0.2910 0.2763 0.2407 -0.0197 0.0193  -0.0088 210 PHE A CE1 
1386 C CE2 . PHE A 208 ? 0.2783 0.2615 0.2296 -0.0155 0.0142  -0.0042 210 PHE A CE2 
1387 C CZ  . PHE A 208 ? 0.2841 0.2658 0.2336 -0.0175 0.0168  -0.0056 210 PHE A CZ  
1388 N N   . THR A 209 ? 0.3947 0.3753 0.3339 -0.0097 0.0142  -0.0093 211 THR A N   
1389 C CA  . THR A 209 ? 0.4150 0.3907 0.3477 -0.0060 0.0135  -0.0096 211 THR A CA  
1390 C C   . THR A 209 ? 0.4087 0.3828 0.3398 -0.0026 0.0124  -0.0093 211 THR A C   
1391 O O   . THR A 209 ? 0.4107 0.3825 0.3361 0.0027  0.0123  -0.0108 211 THR A O   
1392 C CB  . THR A 209 ? 0.4401 0.4069 0.3671 -0.0090 0.0128  -0.0072 211 THR A CB  
1393 O OG1 . THR A 209 ? 0.5446 0.5061 0.4638 -0.0053 0.0130  -0.0083 211 THR A OG1 
1394 C CG2 . THR A 209 ? 0.4301 0.3921 0.3554 -0.0118 0.0113  -0.0046 211 THR A CG2 
1395 N N   . ARG A 210 ? 0.4079 0.3818 0.3424 -0.0053 0.0117  -0.0074 212 ARG A N   
1396 C CA  . ARG A 210 ? 0.3985 0.3706 0.3320 -0.0037 0.0109  -0.0067 212 ARG A CA  
1397 C C   . ARG A 210 ? 0.3594 0.3390 0.3016 -0.0054 0.0110  -0.0065 212 ARG A C   
1398 O O   . ARG A 210 ? 0.3297 0.3116 0.2758 -0.0087 0.0112  -0.0056 212 ARG A O   
1399 C CB  . ARG A 210 ? 0.4214 0.3837 0.3476 -0.0069 0.0102  -0.0046 212 ARG A CB  
1400 C CG  . ARG A 210 ? 0.4295 0.3915 0.3568 -0.0094 0.0097  -0.0034 212 ARG A CG  
1401 C CD  . ARG A 210 ? 0.4488 0.4024 0.3677 -0.0142 0.0097  -0.0023 212 ARG A CD  
1402 N NE  . ARG A 210 ? 0.4526 0.4053 0.3700 -0.0182 0.0097  -0.0017 212 ARG A NE  
1403 C CZ  . ARG A 210 ? 0.4575 0.4197 0.3833 -0.0212 0.0090  -0.0012 212 ARG A CZ  
1404 N NH1 . ARG A 210 ? 0.4549 0.4256 0.3895 -0.0200 0.0082  -0.0008 212 ARG A NH1 
1405 N NH2 . ARG A 210 ? 0.4568 0.4193 0.3808 -0.0252 0.0093  -0.0013 212 ARG A NH2 
1406 N N   . TYR A 211 ? 0.3507 0.3330 0.2947 -0.0028 0.0107  -0.0073 213 TYR A N   
1407 C CA  . TYR A 211 ? 0.3256 0.3144 0.2770 -0.0042 0.0110  -0.0073 213 TYR A CA  
1408 C C   . TYR A 211 ? 0.3434 0.3300 0.2938 -0.0032 0.0102  -0.0063 213 TYR A C   
1409 O O   . TYR A 211 ? 0.3389 0.3260 0.2873 0.0008  0.0100  -0.0078 213 TYR A O   
1410 C CB  . TYR A 211 ? 0.3035 0.3014 0.2594 -0.0028 0.0124  -0.0104 213 TYR A CB  
1411 C CG  . TYR A 211 ? 0.2828 0.2847 0.2442 -0.0061 0.0134  -0.0104 213 TYR A CG  
1412 C CD1 . TYR A 211 ? 0.2763 0.2762 0.2376 -0.0099 0.0146  -0.0097 213 TYR A CD1 
1413 C CD2 . TYR A 211 ? 0.2777 0.2837 0.2425 -0.0051 0.0134  -0.0110 213 TYR A CD2 
1414 C CE1 . TYR A 211 ? 0.2703 0.2707 0.2333 -0.0124 0.0159  -0.0096 213 TYR A CE1 
1415 C CE2 . TYR A 211 ? 0.2668 0.2749 0.2349 -0.0080 0.0147  -0.0112 213 TYR A CE2 
1416 C CZ  . TYR A 211 ? 0.2665 0.2708 0.2329 -0.0116 0.0160  -0.0103 213 TYR A CZ  
1417 O OH  . TYR A 211 ? 0.2550 0.2583 0.2217 -0.0139 0.0174  -0.0103 213 TYR A OH  
1418 N N   . GLU A 212 ? 0.3668 0.3510 0.3176 -0.0066 0.0096  -0.0042 214 GLU A N   
1419 C CA  . GLU A 212 ? 0.3857 0.3685 0.3359 -0.0070 0.0092  -0.0035 214 GLU A CA  
1420 C C   . GLU A 212 ? 0.3674 0.3571 0.3244 -0.0053 0.0095  -0.0043 214 GLU A C   
1421 O O   . GLU A 212 ? 0.3729 0.3674 0.3350 -0.0064 0.0101  -0.0045 214 GLU A O   
1422 C CB  . GLU A 212 ? 0.4206 0.4039 0.3715 -0.0115 0.0087  -0.0019 214 GLU A CB  
1423 C CG  . GLU A 212 ? 0.4661 0.4439 0.4104 -0.0146 0.0086  -0.0014 214 GLU A CG  
1424 C CD  . GLU A 212 ? 0.5103 0.4900 0.4537 -0.0195 0.0083  -0.0010 214 GLU A CD  
1425 O OE1 . GLU A 212 ? 0.5604 0.5382 0.5015 -0.0207 0.0088  -0.0013 214 GLU A OE1 
1426 O OE2 . GLU A 212 ? 0.5364 0.5204 0.4814 -0.0222 0.0076  -0.0007 214 GLU A OE2 
1427 N N   . PHE A 213 ? 0.3476 0.3362 0.3027 -0.0027 0.0093  -0.0050 215 PHE A N   
1428 C CA  . PHE A 213 ? 0.3342 0.3292 0.2946 -0.0007 0.0096  -0.0063 215 PHE A CA  
1429 C C   . PHE A 213 ? 0.3305 0.3217 0.2880 0.0000  0.0092  -0.0056 215 PHE A C   
1430 O O   . PHE A 213 ? 0.3459 0.3299 0.2949 0.0030  0.0089  -0.0060 215 PHE A O   
1431 C CB  . PHE A 213 ? 0.3393 0.3391 0.2996 0.0033  0.0099  -0.0092 215 PHE A CB  
1432 C CG  . PHE A 213 ? 0.3329 0.3418 0.2988 0.0046  0.0104  -0.0114 215 PHE A CG  
1433 C CD1 . PHE A 213 ? 0.3289 0.3382 0.2929 0.0086  0.0096  -0.0123 215 PHE A CD1 
1434 C CD2 . PHE A 213 ? 0.3242 0.3402 0.2958 0.0013  0.0119  -0.0129 215 PHE A CD2 
1435 C CE1 . PHE A 213 ? 0.3260 0.3450 0.2952 0.0096  0.0100  -0.0148 215 PHE A CE1 
1436 C CE2 . PHE A 213 ? 0.3217 0.3462 0.2975 0.0013  0.0128  -0.0156 215 PHE A CE2 
1437 C CZ  . PHE A 213 ? 0.3206 0.3477 0.2960 0.0055  0.0117  -0.0165 215 PHE A CZ  
1438 N N   . THR A 214 ? 0.3026 0.2969 0.2650 -0.0025 0.0093  -0.0045 216 THR A N   
1439 C CA  . THR A 214 ? 0.2970 0.2883 0.2571 -0.0027 0.0092  -0.0040 216 THR A CA  
1440 C C   . THR A 214 ? 0.2872 0.2853 0.2547 -0.0025 0.0095  -0.0042 216 THR A C   
1441 O O   . THR A 214 ? 0.2821 0.2842 0.2546 -0.0047 0.0097  -0.0034 216 THR A O   
1442 C CB  . THR A 214 ? 0.2934 0.2811 0.2502 -0.0074 0.0093  -0.0027 216 THR A CB  
1443 O OG1 . THR A 214 ? 0.2878 0.2681 0.2366 -0.0082 0.0094  -0.0027 216 THR A OG1 
1444 C CG2 . THR A 214 ? 0.2919 0.2762 0.2452 -0.0087 0.0098  -0.0026 216 THR A CG2 
1445 N N   . ILE A 215 ? 0.2915 0.2905 0.2586 0.0005  0.0094  -0.0055 217 ILE A N   
1446 C CA  . ILE A 215 ? 0.2927 0.2968 0.2655 0.0003  0.0098  -0.0057 217 ILE A CA  
1447 C C   . ILE A 215 ? 0.2997 0.2995 0.2694 -0.0007 0.0097  -0.0046 217 ILE A C   
1448 O O   . ILE A 215 ? 0.3080 0.3007 0.2698 0.0008  0.0095  -0.0048 217 ILE A O   
1449 C CB  . ILE A 215 ? 0.3036 0.3129 0.2778 0.0038  0.0098  -0.0082 217 ILE A CB  
1450 C CG1 . ILE A 215 ? 0.3121 0.3273 0.2893 0.0033  0.0105  -0.0101 217 ILE A CG1 
1451 C CG2 . ILE A 215 ? 0.3121 0.3251 0.2904 0.0035  0.0103  -0.0085 217 ILE A CG2 
1452 C CD1 . ILE A 215 ? 0.3165 0.3392 0.2938 0.0071  0.0104  -0.0137 217 ILE A CD1 
1453 N N   . LYS A 216 ? 0.3040 0.3073 0.2785 -0.0033 0.0101  -0.0035 218 LYS A N   
1454 C CA  . LYS A 216 ? 0.3007 0.3030 0.2741 -0.0048 0.0104  -0.0031 218 LYS A CA  
1455 C C   . LYS A 216 ? 0.2838 0.2906 0.2624 -0.0032 0.0107  -0.0035 218 LYS A C   
1456 O O   . LYS A 216 ? 0.2670 0.2781 0.2505 -0.0032 0.0111  -0.0033 218 LYS A O   
1457 C CB  . LYS A 216 ? 0.3288 0.3343 0.3039 -0.0086 0.0105  -0.0022 218 LYS A CB  
1458 C CG  . LYS A 216 ? 0.3725 0.3726 0.3403 -0.0121 0.0108  -0.0023 218 LYS A CG  
1459 C CD  . LYS A 216 ? 0.4162 0.4230 0.3864 -0.0162 0.0108  -0.0023 218 LYS A CD  
1460 C CE  . LYS A 216 ? 0.4724 0.4739 0.4350 -0.0203 0.0113  -0.0027 218 LYS A CE  
1461 N NZ  . LYS A 216 ? 0.5281 0.5167 0.4795 -0.0215 0.0125  -0.0030 218 LYS A NZ  
1462 N N   . ASP A 217 ? 0.2750 0.2789 0.2506 -0.0018 0.0108  -0.0040 219 ASP A N   
1463 C CA  . ASP A 217 ? 0.2599 0.2672 0.2391 -0.0003 0.0111  -0.0046 219 ASP A CA  
1464 C C   . ASP A 217 ? 0.2491 0.2543 0.2266 -0.0022 0.0116  -0.0040 219 ASP A C   
1465 O O   . ASP A 217 ? 0.2452 0.2436 0.2154 -0.0024 0.0117  -0.0040 219 ASP A O   
1466 C CB  . ASP A 217 ? 0.2697 0.2774 0.2469 0.0035  0.0105  -0.0066 219 ASP A CB  
1467 C CG  . ASP A 217 ? 0.2726 0.2856 0.2538 0.0047  0.0108  -0.0079 219 ASP A CG  
1468 O OD1 . ASP A 217 ? 0.2838 0.2989 0.2691 0.0025  0.0117  -0.0072 219 ASP A OD1 
1469 O OD2 . ASP A 217 ? 0.2635 0.2784 0.2427 0.0082  0.0101  -0.0098 219 ASP A OD2 
1470 N N   . THR A 218 ? 0.2331 0.2434 0.2161 -0.0034 0.0122  -0.0034 220 THR A N   
1471 C CA  . THR A 218 ? 0.2317 0.2425 0.2143 -0.0053 0.0129  -0.0032 220 THR A CA  
1472 C C   . THR A 218 ? 0.2330 0.2433 0.2162 -0.0033 0.0132  -0.0037 220 THR A C   
1473 O O   . THR A 218 ? 0.2242 0.2381 0.2119 -0.0019 0.0134  -0.0039 220 THR A O   
1474 C CB  . THR A 218 ? 0.2255 0.2434 0.2129 -0.0066 0.0132  -0.0027 220 THR A CB  
1475 O OG1 . THR A 218 ? 0.2275 0.2458 0.2132 -0.0086 0.0128  -0.0026 220 THR A OG1 
1476 C CG2 . THR A 218 ? 0.2240 0.2451 0.2116 -0.0088 0.0141  -0.0032 220 THR A CG2 
1477 N N   . ILE A 219 ? 0.2409 0.2453 0.2179 -0.0036 0.0135  -0.0041 221 ILE A N   
1478 C CA  . ILE A 219 ? 0.2503 0.2535 0.2265 -0.0015 0.0136  -0.0046 221 ILE A CA  
1479 C C   . ILE A 219 ? 0.2324 0.2383 0.2110 -0.0042 0.0148  -0.0043 221 ILE A C   
1480 O O   . ILE A 219 ? 0.2272 0.2327 0.2034 -0.0081 0.0157  -0.0042 221 ILE A O   
1481 C CB  . ILE A 219 ? 0.2831 0.2767 0.2489 0.0007  0.0131  -0.0052 221 ILE A CB  
1482 C CG1 . ILE A 219 ? 0.2976 0.2895 0.2603 0.0041  0.0118  -0.0059 221 ILE A CG1 
1483 C CG2 . ILE A 219 ? 0.2868 0.2802 0.2518 0.0039  0.0128  -0.0061 221 ILE A CG2 
1484 C CD1 . ILE A 219 ? 0.2897 0.2910 0.2603 0.0069  0.0110  -0.0072 221 ILE A CD1 
1485 N N   . PRO A 220 ? 0.2199 0.2297 0.2033 -0.0027 0.0151  -0.0044 222 PRO A N   
1486 C CA  . PRO A 220 ? 0.2282 0.2412 0.2138 -0.0044 0.0163  -0.0043 222 PRO A CA  
1487 C C   . PRO A 220 ? 0.2397 0.2468 0.2187 -0.0064 0.0172  -0.0047 222 PRO A C   
1488 O O   . PRO A 220 ? 0.2459 0.2453 0.2181 -0.0048 0.0166  -0.0050 222 PRO A O   
1489 C CB  . PRO A 220 ? 0.2248 0.2404 0.2147 -0.0019 0.0165  -0.0044 222 PRO A CB  
1490 C CG  . PRO A 220 ? 0.2237 0.2372 0.2122 0.0001  0.0156  -0.0053 222 PRO A CG  
1491 C CD  . PRO A 220 ? 0.2139 0.2257 0.2001 0.0000  0.0146  -0.0052 222 PRO A CD  
1492 N N   . ALA A 221 ? 0.2431 0.2539 0.2231 -0.0095 0.0186  -0.0050 223 ALA A N   
1493 C CA  . ALA A 221 ? 0.2669 0.2719 0.2398 -0.0127 0.0201  -0.0057 223 ALA A CA  
1494 C C   . ALA A 221 ? 0.2708 0.2696 0.2407 -0.0091 0.0196  -0.0056 223 ALA A C   
1495 O O   . ALA A 221 ? 0.2776 0.2660 0.2374 -0.0094 0.0200  -0.0058 223 ALA A O   
1496 C CB  . ALA A 221 ? 0.2643 0.2783 0.2415 -0.0159 0.0218  -0.0065 223 ALA A CB  
1497 N N   . GLY A 222 ? 0.2784 0.2826 0.2555 -0.0055 0.0188  -0.0054 224 GLY A N   
1498 C CA  . GLY A 222 ? 0.2892 0.2905 0.2647 -0.0027 0.0184  -0.0058 224 GLY A CA  
1499 C C   . GLY A 222 ? 0.3083 0.3063 0.2803 0.0012  0.0166  -0.0065 224 GLY A C   
1500 O O   . GLY A 222 ? 0.3075 0.3067 0.2800 0.0040  0.0159  -0.0074 224 GLY A O   
1501 N N   . MET A 223 ? 0.3166 0.3119 0.2854 0.0016  0.0158  -0.0063 225 MET A N   
1502 C CA  . MET A 223 ? 0.3348 0.3286 0.2999 0.0064  0.0138  -0.0074 225 MET A CA  
1503 C C   . MET A 223 ? 0.3422 0.3246 0.2953 0.0072  0.0136  -0.0071 225 MET A C   
1504 O O   . MET A 223 ? 0.3135 0.2916 0.2636 0.0024  0.0150  -0.0061 225 MET A O   
1505 C CB  . MET A 223 ? 0.3380 0.3403 0.3111 0.0067  0.0132  -0.0079 225 MET A CB  
1506 C CG  . MET A 223 ? 0.3730 0.3797 0.3459 0.0112  0.0116  -0.0101 225 MET A CG  
1507 S SD  . MET A 223 ? 0.3949 0.4134 0.3767 0.0102  0.0121  -0.0123 225 MET A SD  
1508 C CE  . MET A 223 ? 0.3881 0.4051 0.3747 0.0054  0.0144  -0.0100 225 MET A CE  
1509 N N   . THR A 224 ? 0.3602 0.3373 0.3049 0.0132  0.0119  -0.0082 226 THR A N   
1510 C CA  . THR A 224 ? 0.3818 0.3441 0.3108 0.0155  0.0118  -0.0079 226 THR A CA  
1511 C C   . THR A 224 ? 0.3813 0.3464 0.3090 0.0218  0.0095  -0.0092 226 THR A C   
1512 O O   . THR A 224 ? 0.3724 0.3466 0.3042 0.0273  0.0077  -0.0111 226 THR A O   
1513 C CB  . THR A 224 ? 0.4095 0.3590 0.3247 0.0183  0.0120  -0.0081 226 THR A CB  
1514 O OG1 . THR A 224 ? 0.4021 0.3501 0.3190 0.0115  0.0144  -0.0073 226 THR A OG1 
1515 C CG2 . THR A 224 ? 0.4393 0.3699 0.3346 0.0211  0.0122  -0.0078 226 THR A CG2 
1516 N N   . TYR A 225 ? 0.3975 0.3574 0.3213 0.0202  0.0099  -0.0084 227 TYR A N   
1517 C CA  . TYR A 225 ? 0.3910 0.3531 0.3130 0.0259  0.0081  -0.0095 227 TYR A CA  
1518 C C   . TYR A 225 ? 0.4223 0.3708 0.3262 0.0345  0.0067  -0.0104 227 TYR A C   
1519 O O   . TYR A 225 ? 0.4197 0.3503 0.3082 0.0332  0.0082  -0.0092 227 TYR A O   
1520 C CB  . TYR A 225 ? 0.3990 0.3590 0.3222 0.0206  0.0092  -0.0082 227 TYR A CB  
1521 C CG  . TYR A 225 ? 0.4053 0.3638 0.3238 0.0256  0.0079  -0.0090 227 TYR A CG  
1522 C CD1 . TYR A 225 ? 0.3970 0.3698 0.3249 0.0300  0.0062  -0.0110 227 TYR A CD1 
1523 C CD2 . TYR A 225 ? 0.4382 0.3808 0.3423 0.0248  0.0088  -0.0080 227 TYR A CD2 
1524 C CE1 . TYR A 225 ? 0.4191 0.3916 0.3430 0.0344  0.0051  -0.0120 227 TYR A CE1 
1525 C CE2 . TYR A 225 ? 0.4529 0.3935 0.3523 0.0293  0.0077  -0.0086 227 TYR A CE2 
1526 C CZ  . TYR A 225 ? 0.4415 0.3976 0.3512 0.0346  0.0057  -0.0106 227 TYR A CZ  
1527 O OH  . TYR A 225 ? 0.4452 0.3991 0.3489 0.0398  0.0047  -0.0115 227 TYR A OH  
1528 N N   . ASN A 226 ? 0.4363 0.3932 0.3409 0.0431  0.0041  -0.0128 228 ASN A N   
1529 C CA  . ASN A 226 ? 0.4720 0.4190 0.3596 0.0544  0.0020  -0.0143 228 ASN A CA  
1530 C C   . ASN A 226 ? 0.5220 0.4565 0.3960 0.0586  0.0018  -0.0139 228 ASN A C   
1531 O O   . ASN A 226 ? 0.5482 0.4760 0.4078 0.0699  -0.0003 -0.0156 228 ASN A O   
1532 C CB  . ASN A 226 ? 0.4622 0.4287 0.3588 0.0616  -0.0006 -0.0179 228 ASN A CB  
1533 C CG  . ASN A 226 ? 0.4594 0.4309 0.3622 0.0586  -0.0001 -0.0180 228 ASN A CG  
1534 O OD1 . ASN A 226 ? 0.4565 0.4128 0.3499 0.0561  0.0012  -0.0159 228 ASN A OD1 
1535 N ND2 . ASN A 226 ? 0.4461 0.4384 0.3643 0.0576  -0.0009 -0.0206 228 ASN A ND2 
1536 N N   . ASN A 227 ? 0.5354 0.4673 0.4130 0.0507  0.0037  -0.0121 229 ASN A N   
1537 C CA  . ASN A 227 ? 0.5712 0.4900 0.4356 0.0532  0.0039  -0.0116 229 ASN A CA  
1538 C C   . ASN A 227 ? 0.5548 0.4836 0.4189 0.0650  0.0008  -0.0146 229 ASN A C   
1539 O O   . ASN A 227 ? 0.5764 0.4900 0.4213 0.0737  0.0000  -0.0149 229 ASN A O   
1540 C CB  . ASN A 227 ? 0.6341 0.5243 0.4728 0.0537  0.0057  -0.0101 229 ASN A CB  
1541 C CG  . ASN A 227 ? 0.6570 0.5398 0.4964 0.0403  0.0092  -0.0080 229 ASN A CG  
1542 O OD1 . ASN A 227 ? 0.7346 0.6102 0.5706 0.0325  0.0115  -0.0068 229 ASN A OD1 
1543 N ND2 . ASN A 227 ? 0.6587 0.5461 0.5041 0.0373  0.0098  -0.0078 229 ASN A ND2 
1544 N N   . ASP A 228 ? 0.5191 0.4724 0.4024 0.0653  -0.0005 -0.0169 230 ASP A N   
1545 C CA  . ASP A 228 ? 0.5345 0.5021 0.4191 0.0760  -0.0033 -0.0209 230 ASP A CA  
1546 C C   . ASP A 228 ? 0.5186 0.5052 0.4207 0.0709  -0.0029 -0.0223 230 ASP A C   
1547 O O   . ASP A 228 ? 0.5465 0.5524 0.4557 0.0766  -0.0046 -0.0265 230 ASP A O   
1548 C CB  . ASP A 228 ? 0.5474 0.5277 0.4350 0.0826  -0.0054 -0.0240 230 ASP A CB  
1549 C CG  . ASP A 228 ? 0.5193 0.5166 0.4266 0.0731  -0.0042 -0.0244 230 ASP A CG  
1550 O OD1 . ASP A 228 ? 0.4826 0.4785 0.3995 0.0619  -0.0017 -0.0216 230 ASP A OD1 
1551 O OD2 . ASP A 228 ? 0.5210 0.5322 0.4328 0.0775  -0.0058 -0.0276 230 ASP A OD2 
1552 N N   . ALA A 229 ? 0.5039 0.4863 0.4121 0.0607  -0.0006 -0.0194 231 ALA A N   
1553 C CA  . ALA A 229 ? 0.4876 0.4850 0.4097 0.0562  0.0000  -0.0206 231 ALA A CA  
1554 C C   . ALA A 229 ? 0.5045 0.5042 0.4196 0.0652  -0.0016 -0.0231 231 ALA A C   
1555 O O   . ALA A 229 ? 0.5130 0.4946 0.4108 0.0710  -0.0021 -0.0218 231 ALA A O   
1556 C CB  . ALA A 229 ? 0.4740 0.4646 0.4009 0.0457  0.0022  -0.0170 231 ALA A CB  
1557 N N   . GLN A 230 ? 0.5132 0.5342 0.4404 0.0658  -0.0021 -0.0269 232 GLN A N   
1558 C CA  . GLN A 230 ? 0.5394 0.5677 0.4637 0.0729  -0.0033 -0.0300 232 GLN A CA  
1559 C C   . GLN A 230 ? 0.4976 0.5404 0.4367 0.0644  -0.0015 -0.0311 232 GLN A C   
1560 O O   . GLN A 230 ? 0.4496 0.5024 0.4013 0.0557  0.0000  -0.0315 232 GLN A O   
1561 C CB  . GLN A 230 ? 0.5752 0.6175 0.4962 0.0850  -0.0061 -0.0351 232 GLN A CB  
1562 C CG  . GLN A 230 ? 0.6157 0.6383 0.5169 0.0953  -0.0079 -0.0335 232 GLN A CG  
1563 C CD  . GLN A 230 ? 0.6580 0.6941 0.5535 0.1100  -0.0112 -0.0389 232 GLN A CD  
1564 O OE1 . GLN A 230 ? 0.6906 0.7520 0.5969 0.1126  -0.0121 -0.0441 232 GLN A OE1 
1565 N NE2 . GLN A 230 ? 0.6841 0.7034 0.5615 0.1199  -0.0130 -0.0379 232 GLN A NE2 
1566 N N   . VAL A 231 ? 0.5118 0.5534 0.4474 0.0667  -0.0015 -0.0317 233 VAL A N   
1567 C CA  . VAL A 231 ? 0.5154 0.5661 0.4621 0.0582  0.0004  -0.0321 233 VAL A CA  
1568 C C   . VAL A 231 ? 0.5395 0.6111 0.4900 0.0639  -0.0003 -0.0382 233 VAL A C   
1569 O O   . VAL A 231 ? 0.5601 0.6306 0.5002 0.0755  -0.0024 -0.0402 233 VAL A O   
1570 C CB  . VAL A 231 ? 0.5051 0.5381 0.4461 0.0541  0.0014  -0.0277 233 VAL A CB  
1571 C CG1 . VAL A 231 ? 0.4839 0.5241 0.4362 0.0444  0.0036  -0.0274 233 VAL A CG1 
1572 C CG2 . VAL A 231 ? 0.5098 0.5233 0.4438 0.0505  0.0019  -0.0228 233 VAL A CG2 
1573 N N   . TYR A 232 ? 0.5350 0.6249 0.4987 0.0562  0.0015  -0.0415 234 TYR A N   
1574 C CA  . TYR A 232 ? 0.5617 0.6764 0.5310 0.0593  0.0014  -0.0486 234 TYR A CA  
1575 C C   . TYR A 232 ? 0.5462 0.6666 0.5227 0.0498  0.0043  -0.0495 234 TYR A C   
1576 O O   . TYR A 232 ? 0.5118 0.6268 0.4937 0.0388  0.0069  -0.0469 234 TYR A O   
1577 C CB  . TYR A 232 ? 0.5686 0.7026 0.5455 0.0580  0.0014  -0.0533 234 TYR A CB  
1578 C CG  . TYR A 232 ? 0.6178 0.7498 0.5873 0.0689  -0.0017 -0.0537 234 TYR A CG  
1579 C CD1 . TYR A 232 ? 0.6413 0.7789 0.6017 0.0837  -0.0049 -0.0570 234 TYR A CD1 
1580 C CD2 . TYR A 232 ? 0.6261 0.7504 0.5966 0.0651  -0.0014 -0.0509 234 TYR A CD2 
1581 C CE1 . TYR A 232 ? 0.6751 0.8091 0.6267 0.0944  -0.0078 -0.0573 234 TYR A CE1 
1582 C CE2 . TYR A 232 ? 0.6390 0.7606 0.6020 0.0747  -0.0042 -0.0512 234 TYR A CE2 
1583 C CZ  . TYR A 232 ? 0.6812 0.8070 0.6342 0.0894  -0.0074 -0.0544 234 TYR A CZ  
1584 O OH  . TYR A 232 ? 0.7249 0.8464 0.6685 0.0996  -0.0102 -0.0547 234 TYR A OH  
1585 N N   . LEU A 233 ? 0.5797 0.7120 0.5555 0.0545  0.0040  -0.0536 235 LEU A N   
1586 C CA  . LEU A 233 ? 0.6158 0.7572 0.5985 0.0453  0.0072  -0.0559 235 LEU A CA  
1587 C C   . LEU A 233 ? 0.6266 0.7953 0.6185 0.0402  0.0091  -0.0636 235 LEU A C   
1588 O O   . LEU A 233 ? 0.6377 0.8249 0.6298 0.0492  0.0070  -0.0692 235 LEU A O   
1589 C CB  . LEU A 233 ? 0.6384 0.7780 0.6147 0.0528  0.0061  -0.0565 235 LEU A CB  
1590 C CG  . LEU A 233 ? 0.6560 0.8068 0.6381 0.0451  0.0091  -0.0598 235 LEU A CG  
1591 C CD1 . LEU A 233 ? 0.6357 0.7724 0.6209 0.0317  0.0122  -0.0552 235 LEU A CD1 
1592 C CD2 . LEU A 233 ? 0.7019 0.8493 0.6766 0.0539  0.0077  -0.0601 235 LEU A CD2 
1593 N N   . GLN A 234 ? 0.6547 0.8252 0.6527 0.0264  0.0131  -0.0641 236 GLN A N   
1594 C CA  . GLN A 234 ? 0.7143 0.9088 0.7194 0.0180  0.0162  -0.0718 236 GLN A CA  
1595 C C   . GLN A 234 ? 0.7898 0.9913 0.7966 0.0099  0.0198  -0.0751 236 GLN A C   
1596 O O   . GLN A 234 ? 0.8124 0.9958 0.8170 0.0016  0.0223  -0.0703 236 GLN A O   
1597 C CB  . GLN A 234 ? 0.6973 0.8858 0.7048 0.0073  0.0189  -0.0703 236 GLN A CB  
1598 C CG  . GLN A 234 ? 0.7037 0.9015 0.7129 0.0126  0.0166  -0.0723 236 GLN A CG  
1599 C CD  . GLN A 234 ? 0.7110 0.9048 0.7222 0.0017  0.0195  -0.0717 236 GLN A CD  
1600 O OE1 . GLN A 234 ? 0.7165 0.9014 0.7269 -0.0100 0.0236  -0.0705 236 GLN A OE1 
1601 N NE2 . GLN A 234 ? 0.6656 0.8644 0.6778 0.0062  0.0174  -0.0725 236 GLN A NE2 
1602 N N   . GLU A 235 ? 0.9301 1.1575 0.9401 0.0128  0.0201  -0.0832 237 GLU A N   
1603 C CA  . GLU A 235 ? 1.0349 1.2739 1.0468 0.0044  0.0240  -0.0881 237 GLU A CA  
1604 C C   . GLU A 235 ? 1.1261 1.3926 1.1440 -0.0058 0.0279  -0.0976 237 GLU A C   
1605 O O   . GLU A 235 ? 1.1287 1.4246 1.1509 0.0007  0.0264  -0.1058 237 GLU A O   
1606 C CB  . GLU A 235 ? 1.0284 1.2744 1.0382 0.0163  0.0213  -0.0898 237 GLU A CB  
1607 C CG  . GLU A 235 ? 0.9860 1.2035 0.9890 0.0196  0.0200  -0.0812 237 GLU A CG  
1608 C CD  . GLU A 235 ? 0.9864 1.1949 0.9888 0.0076  0.0242  -0.0799 237 GLU A CD  
1609 O OE1 . GLU A 235 ? 0.9640 1.1720 0.9683 -0.0060 0.0285  -0.0810 237 GLU A OE1 
1610 O OE2 . GLU A 235 ? 0.9975 1.1981 0.9960 0.0120  0.0233  -0.0777 237 GLU A OE2 
1611 N N   . GLY A 236 ? 1.1567 1.4138 1.1736 -0.0211 0.0326  -0.0968 238 GLY A N   
1612 C CA  . GLY A 236 ? 1.1745 1.4506 1.1945 -0.0323 0.0365  -0.1043 238 GLY A CA  
1613 C C   . GLY A 236 ? 1.1845 1.4657 1.2071 -0.0253 0.0330  -0.1041 238 GLY A C   
1614 O O   . GLY A 236 ? 1.1977 1.4542 1.2171 -0.0241 0.0316  -0.0960 238 GLY A O   
1615 N N   . GLY A 237 ? 1.1550 1.4684 1.1833 -0.0205 0.0316  -0.1129 239 GLY A N   
1616 C CA  . GLY A 237 ? 1.0862 1.4095 1.1171 -0.0135 0.0283  -0.1144 239 GLY A CA  
1617 C C   . GLY A 237 ? 1.0744 1.4119 1.1063 0.0063  0.0219  -0.1161 239 GLY A C   
1618 O O   . GLY A 237 ? 1.0118 1.3780 1.0479 0.0114  0.0201  -0.1240 239 GLY A O   
1619 N N   . THR A 238 ? 1.0636 1.3814 1.0903 0.0174  0.0186  -0.1093 240 THR A N   
1620 C CA  . THR A 238 ? 1.0123 1.3347 1.0351 0.0377  0.0126  -0.1093 240 THR A CA  
1621 C C   . THR A 238 ? 0.9468 1.2319 0.9609 0.0446  0.0098  -0.0979 240 THR A C   
1622 O O   . THR A 238 ? 0.9411 1.2065 0.9532 0.0378  0.0120  -0.0926 240 THR A O   
1623 C CB  . THR A 238 ? 1.0015 1.3485 1.0261 0.0434  0.0124  -0.1168 240 THR A CB  
1624 O OG1 . THR A 238 ? 1.0464 1.3931 1.0641 0.0642  0.0065  -0.1160 240 THR A OG1 
1625 C CG2 . THR A 238 ? 0.9723 1.3060 0.9955 0.0355  0.0157  -0.1138 240 THR A CG2 
1626 N N   . GLU A 239 ? 0.8878 1.1641 0.8963 0.0569  0.0055  -0.0948 241 GLU A N   
1627 C CA  . GLU A 239 ? 0.8082 1.0497 0.8076 0.0619  0.0034  -0.0847 241 GLU A CA  
1628 C C   . GLU A 239 ? 0.7718 1.0056 0.7599 0.0797  -0.0008 -0.0834 241 GLU A C   
1629 O O   . GLU A 239 ? 0.7868 1.0398 0.7728 0.0921  -0.0039 -0.0893 241 GLU A O   
1630 C CB  . GLU A 239 ? 0.7967 1.0304 0.7952 0.0624  0.0020  -0.0820 241 GLU A CB  
1631 C CG  . GLU A 239 ? 0.8188 1.0472 0.8241 0.0457  0.0061  -0.0800 241 GLU A CG  
1632 C CD  . GLU A 239 ? 0.8462 1.0530 0.8478 0.0459  0.0050  -0.0733 241 GLU A CD  
1633 O OE1 . GLU A 239 ? 0.8661 1.0683 0.8610 0.0584  0.0011  -0.0721 241 GLU A OE1 
1634 O OE2 . GLU A 239 ? 0.8574 1.0515 0.8617 0.0339  0.0081  -0.0694 241 GLU A OE2 
1635 N N   . LYS A 240 ? 0.7510 0.9556 0.7305 0.0811  -0.0012 -0.0756 242 LYS A N   
1636 C CA  . LYS A 240 ? 0.7799 0.9714 0.7451 0.0970  -0.0046 -0.0737 242 LYS A CA  
1637 C C   . LYS A 240 ? 0.7468 0.9034 0.7011 0.0972  -0.0054 -0.0647 242 LYS A C   
1638 O O   . LYS A 240 ? 0.6889 0.8297 0.6469 0.0847  -0.0027 -0.0592 242 LYS A O   
1639 C CB  . LYS A 240 ? 0.8061 1.0012 0.7714 0.0965  -0.0033 -0.0753 242 LYS A CB  
1640 C CG  . LYS A 240 ? 0.8684 1.0492 0.8180 0.1118  -0.0062 -0.0736 242 LYS A CG  
1641 C CD  . LYS A 240 ? 0.9213 1.1077 0.8726 0.1100  -0.0045 -0.0755 242 LYS A CD  
1642 C CE  . LYS A 240 ? 0.9942 1.1786 0.9312 0.1278  -0.0074 -0.0775 242 LYS A CE  
1643 N NZ  . LYS A 240 ? 1.0350 1.1822 0.9535 0.1339  -0.0088 -0.0697 242 LYS A NZ  
1644 N N   . ASP A 241 ? 0.7297 0.8751 0.6702 0.1109  -0.0087 -0.0636 243 ASP A N   
1645 C CA  . ASP A 241 ? 0.7257 0.8384 0.6539 0.1108  -0.0090 -0.0559 243 ASP A CA  
1646 C C   . ASP A 241 ? 0.7084 0.7985 0.6273 0.1094  -0.0079 -0.0511 243 ASP A C   
1647 O O   . ASP A 241 ? 0.7268 0.8120 0.6327 0.1215  -0.0096 -0.0525 243 ASP A O   
1648 C CB  . ASP A 241 ? 0.7519 0.8568 0.6653 0.1254  -0.0124 -0.0563 243 ASP A CB  
1649 C CG  . ASP A 241 ? 0.7597 0.8351 0.6631 0.1218  -0.0119 -0.0494 243 ASP A CG  
1650 O OD1 . ASP A 241 ? 0.7499 0.8098 0.6562 0.1096  -0.0092 -0.0442 243 ASP A OD1 
1651 O OD2 . ASP A 241 ? 0.7754 0.8443 0.6682 0.1309  -0.0140 -0.0496 243 ASP A OD2 
1652 N N   . ILE A 242 ? 0.6720 0.7493 0.5967 0.0954  -0.0051 -0.0460 244 ILE A N   
1653 C CA  . ILE A 242 ? 0.6680 0.7234 0.5845 0.0920  -0.0039 -0.0411 244 ILE A CA  
1654 C C   . ILE A 242 ? 0.6511 0.6789 0.5566 0.0889  -0.0035 -0.0349 244 ILE A C   
1655 O O   . ILE A 242 ? 0.6084 0.6195 0.5094 0.0826  -0.0019 -0.0308 244 ILE A O   
1656 C CB  . ILE A 242 ? 0.6461 0.7100 0.5766 0.0792  -0.0011 -0.0408 244 ILE A CB  
1657 C CG1 . ILE A 242 ? 0.6223 0.6859 0.5644 0.0660  0.0008  -0.0380 244 ILE A CG1 
1658 C CG2 . ILE A 242 ? 0.6397 0.7308 0.5796 0.0813  -0.0009 -0.0476 244 ILE A CG2 
1659 C CD1 . ILE A 242 ? 0.6008 0.6680 0.5528 0.0545  0.0035  -0.0371 244 ILE A CD1 
1660 N N   . SER A 243 ? 0.6641 0.6884 0.5653 0.0927  -0.0047 -0.0347 245 SER A N   
1661 C CA  . SER A 243 ? 0.6666 0.6667 0.5574 0.0891  -0.0040 -0.0296 245 SER A CA  
1662 C C   . SER A 243 ? 0.6916 0.6652 0.5631 0.0913  -0.0033 -0.0263 245 SER A C   
1663 O O   . SER A 243 ? 0.6940 0.6517 0.5630 0.0814  -0.0012 -0.0220 245 SER A O   
1664 C CB  . SER A 243 ? 0.6705 0.6689 0.5536 0.0974  -0.0058 -0.0308 245 SER A CB  
1665 O OG  . SER A 243 ? 0.6651 0.6825 0.5652 0.0916  -0.0057 -0.0325 245 SER A OG  
1666 N N   . THR A 244 ? 0.7394 0.7090 0.5967 0.1041  -0.0050 -0.0286 246 THR A N   
1667 C CA  . THR A 244 ? 0.7808 0.7223 0.6149 0.1082  -0.0043 -0.0260 246 THR A CA  
1668 C C   . THR A 244 ? 0.7342 0.6678 0.5731 0.0948  -0.0016 -0.0226 246 THR A C   
1669 O O   . THR A 244 ? 0.7219 0.6299 0.5434 0.0923  0.0000  -0.0194 246 THR A O   
1670 C CB  . THR A 244 ? 0.8421 0.7866 0.6638 0.1250  -0.0067 -0.0299 246 THR A CB  
1671 O OG1 . THR A 244 ? 0.9234 0.8356 0.7190 0.1285  -0.0056 -0.0269 246 THR A OG1 
1672 C CG2 . THR A 244 ? 0.8055 0.7754 0.6432 0.1251  -0.0070 -0.0337 246 THR A CG2 
1673 N N   . PHE A 245 ? 0.7202 0.6742 0.5806 0.0862  -0.0009 -0.0233 247 PHE A N   
1674 C CA  . PHE A 245 ? 0.7380 0.6871 0.6037 0.0747  0.0012  -0.0205 247 PHE A CA  
1675 C C   . PHE A 245 ? 0.6851 0.6284 0.5574 0.0618  0.0029  -0.0169 247 PHE A C   
1676 O O   . PHE A 245 ? 0.6565 0.5912 0.5283 0.0530  0.0046  -0.0143 247 PHE A O   
1677 C CB  . PHE A 245 ? 0.7558 0.7281 0.6400 0.0714  0.0013  -0.0231 247 PHE A CB  
1678 C CG  . PHE A 245 ? 0.8494 0.8256 0.7270 0.0809  0.0004  -0.0262 247 PHE A CG  
1679 C CD1 . PHE A 245 ? 0.8918 0.8524 0.7588 0.0798  0.0014  -0.0242 247 PHE A CD1 
1680 C CD2 . PHE A 245 ? 0.8682 0.8643 0.7496 0.0913  -0.0013 -0.0315 247 PHE A CD2 
1681 C CE1 . PHE A 245 ? 0.9023 0.8657 0.7622 0.0893  0.0007  -0.0270 247 PHE A CE1 
1682 C CE2 . PHE A 245 ? 0.9067 0.9078 0.7817 0.1009  -0.0022 -0.0348 247 PHE A CE2 
1683 C CZ  . PHE A 245 ? 0.9246 0.9086 0.7887 0.1002  -0.0011 -0.0324 247 PHE A CZ  
1684 N N   . PHE A 246 ? 0.6397 0.5896 0.5186 0.0608  0.0025  -0.0170 248 PHE A N   
1685 C CA  . PHE A 246 ? 0.5899 0.5391 0.4777 0.0495  0.0040  -0.0143 248 PHE A CA  
1686 C C   . PHE A 246 ? 0.6050 0.5355 0.4776 0.0502  0.0044  -0.0126 248 PHE A C   
1687 O O   . PHE A 246 ? 0.5916 0.5265 0.4657 0.0539  0.0035  -0.0135 248 PHE A O   
1688 C CB  . PHE A 246 ? 0.5361 0.5069 0.4430 0.0469  0.0035  -0.0160 248 PHE A CB  
1689 C CG  . PHE A 246 ? 0.5074 0.4951 0.4277 0.0445  0.0038  -0.0179 248 PHE A CG  
1690 C CD1 . PHE A 246 ? 0.5234 0.5210 0.4429 0.0523  0.0028  -0.0216 248 PHE A CD1 
1691 C CD2 . PHE A 246 ? 0.4894 0.4829 0.4220 0.0347  0.0052  -0.0164 248 PHE A CD2 
1692 C CE1 . PHE A 246 ? 0.5144 0.5275 0.4455 0.0489  0.0036  -0.0238 248 PHE A CE1 
1693 C CE2 . PHE A 246 ? 0.4777 0.4842 0.4202 0.0320  0.0059  -0.0182 248 PHE A CE2 
1694 C CZ  . PHE A 246 ? 0.4893 0.5057 0.4313 0.0383  0.0053  -0.0220 248 PHE A CZ  
1695 N N   . PRO A 247 ? 0.6246 0.5338 0.4816 0.0458  0.0062  -0.0102 249 PRO A N   
1696 C CA  . PRO A 247 ? 0.6469 0.5394 0.4911 0.0426  0.0076  -0.0087 249 PRO A CA  
1697 C C   . PRO A 247 ? 0.6256 0.5316 0.4878 0.0332  0.0083  -0.0078 249 PRO A C   
1698 O O   . PRO A 247 ? 0.6241 0.5426 0.5017 0.0256  0.0088  -0.0071 249 PRO A O   
1699 C CB  . PRO A 247 ? 0.6708 0.5404 0.4961 0.0373  0.0101  -0.0071 249 PRO A CB  
1700 C CG  . PRO A 247 ? 0.6559 0.5366 0.4931 0.0331  0.0100  -0.0070 249 PRO A CG  
1701 C CD  . PRO A 247 ? 0.6333 0.5339 0.4843 0.0419  0.0074  -0.0092 249 PRO A CD  
1702 N N   . ILE A 248 ? 0.6151 0.5187 0.4745 0.0349  0.0082  -0.0079 250 ILE A N   
1703 C CA  . ILE A 248 ? 0.5900 0.5067 0.4654 0.0284  0.0085  -0.0073 250 ILE A CA  
1704 C C   . ILE A 248 ? 0.5825 0.4836 0.4462 0.0216  0.0109  -0.0059 250 ILE A C   
1705 O O   . ILE A 248 ? 0.6325 0.5144 0.4759 0.0258  0.0115  -0.0060 250 ILE A O   
1706 C CB  . ILE A 248 ? 0.5791 0.5092 0.4629 0.0362  0.0064  -0.0093 250 ILE A CB  
1707 C CG1 . ILE A 248 ? 0.5607 0.5102 0.4594 0.0388  0.0050  -0.0112 250 ILE A CG1 
1708 C CG2 . ILE A 248 ? 0.5664 0.5025 0.4593 0.0309  0.0071  -0.0086 250 ILE A CG2 
1709 C CD1 . ILE A 248 ? 0.5514 0.5171 0.4588 0.0451  0.0033  -0.0141 250 ILE A CD1 
1710 N N   . SER A 249 ? 0.5554 0.4640 0.4299 0.0116  0.0123  -0.0050 251 SER A N   
1711 C CA  . SER A 249 ? 0.5630 0.4614 0.4289 0.0040  0.0149  -0.0045 251 SER A CA  
1712 C C   . SER A 249 ? 0.5332 0.4472 0.4155 0.0013  0.0146  -0.0045 251 SER A C   
1713 O O   . SER A 249 ? 0.5110 0.4430 0.4114 0.0025  0.0130  -0.0045 251 SER A O   
1714 C CB  . SER A 249 ? 0.5697 0.4615 0.4296 -0.0062 0.0174  -0.0042 251 SER A CB  
1715 O OG  . SER A 249 ? 0.5790 0.4897 0.4578 -0.0105 0.0166  -0.0040 251 SER A OG  
1716 N N   . TYR A 250 ? 0.5204 0.4255 0.3942 -0.0019 0.0163  -0.0045 252 TYR A N   
1717 C CA  . TYR A 250 ? 0.5012 0.4181 0.3872 -0.0050 0.0166  -0.0045 252 TYR A CA  
1718 C C   . TYR A 250 ? 0.5125 0.4214 0.3897 -0.0153 0.0199  -0.0048 252 TYR A C   
1719 O O   . TYR A 250 ? 0.5436 0.4328 0.4009 -0.0162 0.0219  -0.0051 252 TYR A O   
1720 C CB  . TYR A 250 ? 0.4957 0.4111 0.3798 0.0033  0.0150  -0.0049 252 TYR A CB  
1721 C CG  . TYR A 250 ? 0.4739 0.4022 0.3716 0.0014  0.0150  -0.0049 252 TYR A CG  
1722 C CD1 . TYR A 250 ? 0.4370 0.3842 0.3540 0.0011  0.0138  -0.0049 252 TYR A CD1 
1723 C CD2 . TYR A 250 ? 0.4890 0.4089 0.3783 0.0003  0.0163  -0.0050 252 TYR A CD2 
1724 C CE1 . TYR A 250 ? 0.4321 0.3893 0.3596 0.0000  0.0139  -0.0049 252 TYR A CE1 
1725 C CE2 . TYR A 250 ? 0.4720 0.4032 0.3732 -0.0010 0.0163  -0.0051 252 TYR A CE2 
1726 C CZ  . TYR A 250 ? 0.4576 0.4074 0.3778 -0.0008 0.0150  -0.0051 252 TYR A CZ  
1727 O OH  . TYR A 250 ? 0.4444 0.4033 0.3742 -0.0016 0.0152  -0.0051 252 TYR A OH  
1728 N N   . THR A 251 ? 0.4976 0.4213 0.3878 -0.0227 0.0207  -0.0052 253 THR A N   
1729 C CA  . THR A 251 ? 0.5048 0.4289 0.3915 -0.0336 0.0239  -0.0064 253 THR A CA  
1730 C C   . THR A 251 ? 0.4722 0.4194 0.3800 -0.0345 0.0228  -0.0066 253 THR A C   
1731 O O   . THR A 251 ? 0.4422 0.4017 0.3633 -0.0303 0.0205  -0.0059 253 THR A O   
1732 C CB  . THR A 251 ? 0.5473 0.4651 0.4243 -0.0417 0.0260  -0.0074 253 THR A CB  
1733 O OG1 . THR A 251 ? 0.5170 0.4524 0.4097 -0.0421 0.0243  -0.0073 253 THR A OG1 
1734 C CG2 . THR A 251 ? 0.5795 0.4751 0.4371 -0.0380 0.0263  -0.0067 253 THR A CG2 
1735 N N   . GLY A 252 ? 0.4676 0.4193 0.3771 -0.0389 0.0245  -0.0077 254 GLY A N   
1736 C CA  . GLY A 252 ? 0.4245 0.3977 0.3516 -0.0400 0.0239  -0.0083 254 GLY A CA  
1737 C C   . GLY A 252 ? 0.3833 0.3636 0.3225 -0.0309 0.0211  -0.0067 254 GLY A C   
1738 O O   . GLY A 252 ? 0.3930 0.3888 0.3457 -0.0295 0.0199  -0.0066 254 GLY A O   
1739 N N   . ASN A 253 ? 0.3492 0.3186 0.2826 -0.0248 0.0201  -0.0057 255 ASN A N   
1740 C CA  . ASN A 253 ? 0.3238 0.3000 0.2674 -0.0173 0.0179  -0.0049 255 ASN A CA  
1741 C C   . ASN A 253 ? 0.3038 0.2870 0.2555 -0.0140 0.0160  -0.0043 255 ASN A C   
1742 O O   . ASN A 253 ? 0.2732 0.2652 0.2351 -0.0103 0.0148  -0.0040 255 ASN A O   
1743 C CB  . ASN A 253 ? 0.3094 0.2968 0.2631 -0.0181 0.0183  -0.0051 255 ASN A CB  
1744 C CG  . ASN A 253 ? 0.3191 0.2990 0.2664 -0.0173 0.0192  -0.0054 255 ASN A CG  
1745 O OD1 . ASN A 253 ? 0.3386 0.3076 0.2736 -0.0217 0.0211  -0.0060 255 ASN A OD1 
1746 N ND2 . ASN A 253 ? 0.3060 0.2899 0.2596 -0.0122 0.0179  -0.0050 255 ASN A ND2 
1747 N N   . VAL A 254 ? 0.3081 0.2859 0.2537 -0.0157 0.0161  -0.0043 256 VAL A N   
1748 C CA  . VAL A 254 ? 0.2976 0.2810 0.2496 -0.0130 0.0145  -0.0038 256 VAL A CA  
1749 C C   . VAL A 254 ? 0.3103 0.2828 0.2527 -0.0087 0.0137  -0.0039 256 VAL A C   
1750 O O   . VAL A 254 ? 0.3291 0.2892 0.2584 -0.0110 0.0149  -0.0040 256 VAL A O   
1751 C CB  . VAL A 254 ? 0.2940 0.2840 0.2494 -0.0182 0.0149  -0.0039 256 VAL A CB  
1752 C CG1 . VAL A 254 ? 0.2905 0.2829 0.2496 -0.0155 0.0135  -0.0034 256 VAL A CG1 
1753 C CG2 . VAL A 254 ? 0.2830 0.2860 0.2480 -0.0201 0.0152  -0.0043 256 VAL A CG2 
1754 N N   . ILE A 255 ? 0.3042 0.2811 0.2517 -0.0026 0.0122  -0.0042 257 ILE A N   
1755 C CA  . ILE A 255 ? 0.3236 0.2944 0.2639 0.0024  0.0111  -0.0048 257 ILE A CA  
1756 C C   . ILE A 255 ? 0.3244 0.2988 0.2685 0.0003  0.0109  -0.0044 257 ILE A C   
1757 O O   . ILE A 255 ? 0.3044 0.2896 0.2598 -0.0004 0.0106  -0.0043 257 ILE A O   
1758 C CB  . ILE A 255 ? 0.3205 0.2981 0.2653 0.0091  0.0096  -0.0063 257 ILE A CB  
1759 C CG1 . ILE A 255 ? 0.3227 0.3005 0.2674 0.0108  0.0096  -0.0067 257 ILE A CG1 
1760 C CG2 . ILE A 255 ? 0.3371 0.3092 0.2729 0.0157  0.0084  -0.0075 257 ILE A CG2 
1761 C CD1 . ILE A 255 ? 0.3192 0.3076 0.2706 0.0158  0.0084  -0.0087 257 ILE A CD1 
1762 N N   . THR A 256 ? 0.3422 0.3062 0.2754 -0.0001 0.0113  -0.0043 258 THR A N   
1763 C CA  . THR A 256 ? 0.3540 0.3197 0.2889 -0.0013 0.0110  -0.0040 258 THR A CA  
1764 C C   . THR A 256 ? 0.3763 0.3383 0.3056 0.0057  0.0098  -0.0051 258 THR A C   
1765 O O   . THR A 256 ? 0.4136 0.3629 0.3288 0.0097  0.0099  -0.0054 258 THR A O   
1766 C CB  . THR A 256 ? 0.3639 0.3218 0.2906 -0.0082 0.0125  -0.0035 258 THR A CB  
1767 O OG1 . THR A 256 ? 0.3523 0.3187 0.2866 -0.0139 0.0132  -0.0033 258 THR A OG1 
1768 C CG2 . THR A 256 ? 0.3664 0.3257 0.2941 -0.0095 0.0121  -0.0032 258 THR A CG2 
1769 N N   . ILE A 257 ? 0.3746 0.3471 0.3131 0.0079  0.0090  -0.0058 259 ILE A N   
1770 C CA  . ILE A 257 ? 0.3840 0.3564 0.3183 0.0147  0.0079  -0.0076 259 ILE A CA  
1771 C C   . ILE A 257 ? 0.3838 0.3578 0.3205 0.0120  0.0082  -0.0072 259 ILE A C   
1772 O O   . ILE A 257 ? 0.3593 0.3432 0.3071 0.0086  0.0084  -0.0070 259 ILE A O   
1773 C CB  . ILE A 257 ? 0.3797 0.3655 0.3226 0.0193  0.0070  -0.0100 259 ILE A CB  
1774 C CG1 . ILE A 257 ? 0.3813 0.3679 0.3244 0.0210  0.0068  -0.0103 259 ILE A CG1 
1775 C CG2 . ILE A 257 ? 0.3960 0.3834 0.3335 0.0269  0.0059  -0.0125 259 ILE A CG2 
1776 C CD1 . ILE A 257 ? 0.3564 0.3524 0.3118 0.0158  0.0076  -0.0099 259 ILE A CD1 
1777 N N   . THR A 258 ? 0.4107 0.3737 0.3356 0.0140  0.0082  -0.0071 260 THR A N   
1778 C CA  . THR A 258 ? 0.4281 0.3914 0.3538 0.0118  0.0084  -0.0067 260 THR A CA  
1779 C C   . THR A 258 ? 0.4568 0.4099 0.3691 0.0180  0.0080  -0.0077 260 THR A C   
1780 O O   . THR A 258 ? 0.4787 0.4166 0.3759 0.0202  0.0084  -0.0073 260 THR A O   
1781 C CB  . THR A 258 ? 0.4248 0.3843 0.3504 0.0034  0.0094  -0.0048 260 THR A CB  
1782 O OG1 . THR A 258 ? 0.4123 0.3724 0.3384 0.0020  0.0094  -0.0046 260 THR A OG1 
1783 C CG2 . THR A 258 ? 0.4397 0.3844 0.3513 0.0004  0.0106  -0.0041 260 THR A CG2 
1784 N N   . PRO A 259 ? 0.4573 0.4173 0.3734 0.0206  0.0076  -0.0090 261 PRO A N   
1785 C CA  . PRO A 259 ? 0.4778 0.4282 0.3812 0.0263  0.0074  -0.0098 261 PRO A CA  
1786 C C   . PRO A 259 ? 0.4863 0.4259 0.3831 0.0203  0.0085  -0.0079 261 PRO A C   
1787 O O   . PRO A 259 ? 0.5097 0.4410 0.3960 0.0244  0.0085  -0.0085 261 PRO A O   
1788 C CB  . PRO A 259 ? 0.4744 0.4412 0.3876 0.0308  0.0066  -0.0127 261 PRO A CB  
1789 C CG  . PRO A 259 ? 0.4568 0.4363 0.3860 0.0229  0.0074  -0.0122 261 PRO A CG  
1790 C CD  . PRO A 259 ? 0.4372 0.4134 0.3685 0.0183  0.0076  -0.0100 261 PRO A CD  
1791 N N   . GLY A 260 ? 0.4664 0.4076 0.3695 0.0112  0.0093  -0.0061 262 GLY A N   
1792 C CA  . GLY A 260 ? 0.4549 0.3914 0.3556 0.0042  0.0101  -0.0048 262 GLY A CA  
1793 C C   . GLY A 260 ? 0.4296 0.3775 0.3412 0.0039  0.0096  -0.0052 262 GLY A C   
1794 O O   . GLY A 260 ? 0.3985 0.3547 0.3201 -0.0015 0.0096  -0.0042 262 GLY A O   
1795 N N   . ASP A 261 ? 0.4130 0.3620 0.3223 0.0103  0.0092  -0.0068 263 ASP A N   
1796 C CA  . ASP A 261 ? 0.3955 0.3555 0.3141 0.0102  0.0091  -0.0078 263 ASP A CA  
1797 C C   . ASP A 261 ? 0.3758 0.3469 0.2993 0.0170  0.0087  -0.0109 263 ASP A C   
1798 O O   . ASP A 261 ? 0.3919 0.3592 0.3064 0.0248  0.0081  -0.0126 263 ASP A O   
1799 C CB  . ASP A 261 ? 0.4123 0.3629 0.3217 0.0099  0.0095  -0.0074 263 ASP A CB  
1800 C CG  . ASP A 261 ? 0.4201 0.3795 0.3372 0.0084  0.0098  -0.0082 263 ASP A CG  
1801 O OD1 . ASP A 261 ? 0.3962 0.3687 0.3249 0.0077  0.0100  -0.0094 263 ASP A OD1 
1802 O OD2 . ASP A 261 ? 0.4441 0.3957 0.3541 0.0071  0.0101  -0.0076 263 ASP A OD2 
1803 N N   . LEU A 262 ? 0.3494 0.3340 0.2854 0.0145  0.0091  -0.0120 264 LEU A N   
1804 C CA  . LEU A 262 ? 0.3585 0.3567 0.2999 0.0192  0.0091  -0.0158 264 LEU A CA  
1805 C C   . LEU A 262 ? 0.3825 0.3845 0.3207 0.0235  0.0093  -0.0185 264 LEU A C   
1806 O O   . LEU A 262 ? 0.3868 0.3991 0.3254 0.0299  0.0089  -0.0223 264 LEU A O   
1807 C CB  . LEU A 262 ? 0.3448 0.3539 0.2979 0.0133  0.0103  -0.0164 264 LEU A CB  
1808 C CG  . LEU A 262 ? 0.3459 0.3702 0.3050 0.0157  0.0108  -0.0207 264 LEU A CG  
1809 C CD1 . LEU A 262 ? 0.3524 0.3775 0.3084 0.0222  0.0093  -0.0217 264 LEU A CD1 
1810 C CD2 . LEU A 262 ? 0.3351 0.3656 0.3024 0.0085  0.0127  -0.0210 264 LEU A CD2 
1811 N N   . LYS A 263 ? 0.3992 0.3944 0.3342 0.0204  0.0098  -0.0169 265 LYS A N   
1812 C CA  . LYS A 263 ? 0.4267 0.4252 0.3582 0.0247  0.0101  -0.0196 265 LYS A CA  
1813 C C   . LYS A 263 ? 0.4624 0.4534 0.3810 0.0348  0.0088  -0.0206 265 LYS A C   
1814 O O   . LYS A 263 ? 0.5087 0.5052 0.4239 0.0414  0.0087  -0.0238 265 LYS A O   
1815 C CB  . LYS A 263 ? 0.4316 0.4221 0.3607 0.0194  0.0109  -0.0173 265 LYS A CB  
1816 C CG  . LYS A 263 ? 0.4211 0.4162 0.3595 0.0109  0.0121  -0.0161 265 LYS A CG  
1817 C CD  . LYS A 263 ? 0.4242 0.4341 0.3706 0.0093  0.0137  -0.0199 265 LYS A CD  
1818 C CE  . LYS A 263 ? 0.4205 0.4298 0.3715 0.0013  0.0153  -0.0184 265 LYS A CE  
1819 N NZ  . LYS A 263 ? 0.4364 0.4562 0.3912 -0.0017 0.0178  -0.0223 265 LYS A NZ  
1820 N N   . TYR A 264 ? 0.4729 0.4506 0.3827 0.0367  0.0080  -0.0183 266 TYR A N   
1821 C CA  . TYR A 264 ? 0.5017 0.4693 0.3961 0.0473  0.0068  -0.0193 266 TYR A CA  
1822 C C   . TYR A 264 ? 0.5344 0.5190 0.4334 0.0562  0.0056  -0.0239 266 TYR A C   
1823 O O   . TYR A 264 ? 0.5529 0.5336 0.4396 0.0677  0.0043  -0.0259 266 TYR A O   
1824 C CB  . TYR A 264 ? 0.4903 0.4386 0.3730 0.0456  0.0069  -0.0160 266 TYR A CB  
1825 C CG  . TYR A 264 ? 0.4762 0.4082 0.3512 0.0376  0.0082  -0.0127 266 TYR A CG  
1826 C CD1 . TYR A 264 ? 0.4686 0.4008 0.3448 0.0343  0.0088  -0.0124 266 TYR A CD1 
1827 C CD2 . TYR A 264 ? 0.4778 0.3947 0.3438 0.0327  0.0089  -0.0101 266 TYR A CD2 
1828 C CE1 . TYR A 264 ? 0.4666 0.3852 0.3357 0.0267  0.0099  -0.0098 266 TYR A CE1 
1829 C CE2 . TYR A 264 ? 0.4914 0.3951 0.3498 0.0245  0.0103  -0.0079 266 TYR A CE2 
1830 C CZ  . TYR A 264 ? 0.4686 0.3734 0.3286 0.0217  0.0107  -0.0078 266 TYR A CZ  
1831 O OH  . TYR A 264 ? 0.4601 0.3536 0.3128 0.0132  0.0121  -0.0060 266 TYR A OH  
1832 N N   . VAL A 265 ? 0.5482 0.5507 0.4628 0.0516  0.0060  -0.0256 267 VAL A N   
1833 C CA  . VAL A 265 ? 0.5827 0.6047 0.5030 0.0585  0.0050  -0.0306 267 VAL A CA  
1834 C C   . VAL A 265 ? 0.5991 0.6400 0.5289 0.0565  0.0063  -0.0349 267 VAL A C   
1835 O O   . VAL A 265 ? 0.5801 0.6300 0.5218 0.0465  0.0082  -0.0352 267 VAL A O   
1836 C CB  . VAL A 265 ? 0.5812 0.6098 0.5101 0.0546  0.0050  -0.0304 267 VAL A CB  
1837 C CG1 . VAL A 265 ? 0.6038 0.6492 0.5342 0.0637  0.0034  -0.0356 267 VAL A CG1 
1838 C CG2 . VAL A 265 ? 0.5630 0.5718 0.4841 0.0525  0.0046  -0.0255 267 VAL A CG2 
1839 N N   . GLN A 266 ? 0.6726 0.7171 0.5953 0.0656  0.0055  -0.0380 268 GLN A N   
1840 C CA  . GLN A 266 ? 0.6982 0.7557 0.6265 0.0634  0.0071  -0.0414 268 GLN A CA  
1841 C C   . GLN A 266 ? 0.7068 0.7926 0.6484 0.0615  0.0081  -0.0478 268 GLN A C   
1842 O O   . GLN A 266 ? 0.7083 0.8050 0.6580 0.0534  0.0106  -0.0501 268 GLN A O   
1843 C CB  . GLN A 266 ? 0.7450 0.7951 0.6597 0.0744  0.0060  -0.0424 268 GLN A CB  
1844 C CG  . GLN A 266 ? 0.7935 0.8136 0.6933 0.0742  0.0056  -0.0362 268 GLN A CG  
1845 C CD  . GLN A 266 ? 0.8497 0.8568 0.7339 0.0823  0.0053  -0.0361 268 GLN A CD  
1846 O OE1 . GLN A 266 ? 0.9067 0.9211 0.7839 0.0950  0.0039  -0.0403 268 GLN A OE1 
1847 N NE2 . GLN A 266 ? 0.8394 0.8264 0.7167 0.0755  0.0064  -0.0315 268 GLN A NE2 
1848 N N   . ASP A 267 ? 0.7279 0.8239 0.6707 0.0676  0.0065  -0.0505 269 ASP A N   
1849 C CA  . ASP A 267 ? 0.7594 0.8832 0.7142 0.0652  0.0074  -0.0571 269 ASP A CA  
1850 C C   . ASP A 267 ? 0.7301 0.8551 0.6958 0.0495  0.0105  -0.0556 269 ASP A C   
1851 O O   . ASP A 267 ? 0.7111 0.8571 0.6858 0.0435  0.0127  -0.0612 269 ASP A O   
1852 C CB  . ASP A 267 ? 0.7960 0.9269 0.7478 0.0760  0.0045  -0.0595 269 ASP A CB  
1853 C CG  . ASP A 267 ? 0.8729 1.0137 0.8156 0.0929  0.0017  -0.0643 269 ASP A CG  
1854 O OD1 . ASP A 267 ? 0.8635 0.9985 0.7988 0.0980  0.0016  -0.0643 269 ASP A OD1 
1855 O OD2 . ASP A 267 ? 0.9298 1.0841 0.8721 0.1018  -0.0004 -0.0683 269 ASP A OD2 
1856 N N   . VAL A 268 ? 0.7271 0.8302 0.6906 0.0430  0.0109  -0.0486 270 VAL A N   
1857 C CA  . VAL A 268 ? 0.6931 0.7941 0.6642 0.0304  0.0133  -0.0466 270 VAL A CA  
1858 C C   . VAL A 268 ? 0.6836 0.7872 0.6582 0.0208  0.0166  -0.0476 270 VAL A C   
1859 O O   . VAL A 268 ? 0.6696 0.7598 0.6394 0.0204  0.0165  -0.0441 270 VAL A O   
1860 C CB  . VAL A 268 ? 0.6554 0.7340 0.6227 0.0281  0.0123  -0.0393 270 VAL A CB  
1861 C CG1 . VAL A 268 ? 0.6257 0.7015 0.5991 0.0167  0.0147  -0.0373 270 VAL A CG1 
1862 C CG2 . VAL A 268 ? 0.6626 0.7366 0.6253 0.0359  0.0096  -0.0381 270 VAL A CG2 
1863 N N   . LYS A 269 ? 0.7030 0.8216 0.6842 0.0127  0.0197  -0.0523 271 LYS A N   
1864 C CA  . LYS A 269 ? 0.7026 0.8221 0.6850 0.0022  0.0235  -0.0537 271 LYS A CA  
1865 C C   . LYS A 269 ? 0.6399 0.7476 0.6227 -0.0077 0.0258  -0.0502 271 LYS A C   
1866 O O   . LYS A 269 ? 0.5973 0.7007 0.5812 -0.0063 0.0243  -0.0479 271 LYS A O   
1867 C CB  . LYS A 269 ? 0.7953 0.9405 0.7824 -0.0005 0.0262  -0.0625 271 LYS A CB  
1868 C CG  . LYS A 269 ? 0.8781 1.0345 0.8638 0.0070  0.0253  -0.0663 271 LYS A CG  
1869 C CD  . LYS A 269 ? 0.9312 1.0898 0.9136 0.0226  0.0207  -0.0662 271 LYS A CD  
1870 C CE  . LYS A 269 ? 0.9823 1.1512 0.9617 0.0310  0.0199  -0.0702 271 LYS A CE  
1871 N NZ  . LYS A 269 ? 1.0284 1.2085 1.0048 0.0463  0.0161  -0.0735 271 LYS A NZ  
1872 N N   . VAL A 270 ? 0.5932 0.6950 0.5737 -0.0168 0.0292  -0.0501 272 VAL A N   
1873 C CA  . VAL A 270 ? 0.6023 0.6907 0.5800 -0.0260 0.0318  -0.0472 272 VAL A CA  
1874 C C   . VAL A 270 ? 0.5987 0.6979 0.5794 -0.0308 0.0338  -0.0513 272 VAL A C   
1875 O O   . VAL A 270 ? 0.5919 0.6796 0.5703 -0.0344 0.0345  -0.0481 272 VAL A O   
1876 C CB  . VAL A 270 ? 0.6387 0.7205 0.6110 -0.0346 0.0356  -0.0479 272 VAL A CB  
1877 C CG1 . VAL A 270 ? 0.6657 0.7669 0.6396 -0.0409 0.0397  -0.0562 272 VAL A CG1 
1878 C CG2 . VAL A 270 ? 0.6422 0.7060 0.6081 -0.0418 0.0379  -0.0442 272 VAL A CG2 
1879 N N   . SER A 271 ? 0.6115 0.7332 0.5967 -0.0312 0.0351  -0.0587 273 SER A N   
1880 C CA  . SER A 271 ? 0.6041 0.7393 0.5918 -0.0379 0.0379  -0.0641 273 SER A CA  
1881 C C   . SER A 271 ? 0.5588 0.7004 0.5513 -0.0291 0.0339  -0.0635 273 SER A C   
1882 O O   . SER A 271 ? 0.5535 0.7056 0.5483 -0.0335 0.0356  -0.0674 273 SER A O   
1883 C CB  . SER A 271 ? 0.6271 0.7866 0.6174 -0.0435 0.0415  -0.0735 273 SER A CB  
1884 O OG  . SER A 271 ? 0.6226 0.8015 0.6185 -0.0324 0.0380  -0.0771 273 SER A OG  
1885 N N   . SER A 272 ? 0.5417 0.6766 0.5343 -0.0175 0.0292  -0.0590 274 SER A N   
1886 C CA  . SER A 272 ? 0.5466 0.6845 0.5414 -0.0082 0.0253  -0.0579 274 SER A CA  
1887 C C   . SER A 272 ? 0.5346 0.6577 0.5285 -0.0118 0.0253  -0.0530 274 SER A C   
1888 O O   . SER A 272 ? 0.5371 0.6423 0.5274 -0.0171 0.0266  -0.0480 274 SER A O   
1889 C CB  . SER A 272 ? 0.5450 0.6751 0.5364 0.0034  0.0211  -0.0543 274 SER A CB  
1890 O OG  . SER A 272 ? 0.5683 0.7111 0.5594 0.0079  0.0209  -0.0588 274 SER A OG  
1891 N N   . LYS A 273 ? 0.5382 0.6692 0.5349 -0.0084 0.0238  -0.0546 275 LYS A N   
1892 C CA  . LYS A 273 ? 0.5300 0.6472 0.5258 -0.0080 0.0226  -0.0494 275 LYS A CA  
1893 C C   . LYS A 273 ? 0.5096 0.6220 0.5038 0.0035  0.0180  -0.0463 275 LYS A C   
1894 O O   . LYS A 273 ? 0.5611 0.6877 0.5560 0.0112  0.0161  -0.0505 275 LYS A O   
1895 C CB  . LYS A 273 ? 0.5444 0.6725 0.5433 -0.0136 0.0247  -0.0535 275 LYS A CB  
1896 C CG  . LYS A 273 ? 0.5814 0.7074 0.5780 -0.0266 0.0299  -0.0556 275 LYS A CG  
1897 C CD  . LYS A 273 ? 0.6108 0.7445 0.6086 -0.0324 0.0321  -0.0592 275 LYS A CD  
1898 C CE  . LYS A 273 ? 0.6343 0.7546 0.6256 -0.0444 0.0370  -0.0585 275 LYS A CE  
1899 N NZ  . LYS A 273 ? 0.6786 0.8014 0.6659 -0.0529 0.0412  -0.0623 275 LYS A NZ  
1900 N N   . ILE A 274 ? 0.4644 0.5577 0.4551 0.0049  0.0166  -0.0397 276 ILE A N   
1901 C CA  . ILE A 274 ? 0.4558 0.5413 0.4428 0.0137  0.0131  -0.0367 276 ILE A CA  
1902 C C   . ILE A 274 ? 0.4288 0.5146 0.4181 0.0124  0.0130  -0.0362 276 ILE A C   
1903 O O   . ILE A 274 ? 0.3862 0.4651 0.3773 0.0052  0.0149  -0.0337 276 ILE A O   
1904 C CB  . ILE A 274 ? 0.4605 0.5270 0.4423 0.0142  0.0121  -0.0307 276 ILE A CB  
1905 C CG1 . ILE A 274 ? 0.4612 0.5264 0.4408 0.0138  0.0127  -0.0309 276 ILE A CG1 
1906 C CG2 . ILE A 274 ? 0.4631 0.5201 0.4384 0.0218  0.0094  -0.0282 276 ILE A CG2 
1907 C CD1 . ILE A 274 ? 0.4778 0.5545 0.4555 0.0212  0.0116  -0.0355 276 ILE A CD1 
1908 N N   . VAL A 275 ? 0.4284 0.5212 0.4166 0.0199  0.0108  -0.0384 277 VAL A N   
1909 C CA  . VAL A 275 ? 0.4202 0.5154 0.4105 0.0193  0.0106  -0.0387 277 VAL A CA  
1910 C C   . VAL A 275 ? 0.4195 0.5034 0.4032 0.0275  0.0076  -0.0355 277 VAL A C   
1911 O O   . VAL A 275 ? 0.4298 0.5172 0.4081 0.0370  0.0053  -0.0377 277 VAL A O   
1912 C CB  . VAL A 275 ? 0.4285 0.5461 0.4236 0.0194  0.0112  -0.0458 277 VAL A CB  
1913 C CG1 . VAL A 275 ? 0.4221 0.5419 0.4193 0.0179  0.0112  -0.0462 277 VAL A CG1 
1914 C CG2 . VAL A 275 ? 0.4435 0.5713 0.4430 0.0099  0.0148  -0.0496 277 VAL A CG2 
1915 N N   . ILE A 276 ? 0.4100 0.4812 0.3931 0.0241  0.0080  -0.0311 278 ILE A N   
1916 C CA  . ILE A 276 ? 0.4234 0.4833 0.3996 0.0298  0.0060  -0.0283 278 ILE A CA  
1917 C C   . ILE A 276 ? 0.4156 0.4833 0.3949 0.0303  0.0057  -0.0304 278 ILE A C   
1918 O O   . ILE A 276 ? 0.3812 0.4526 0.3670 0.0231  0.0077  -0.0305 278 ILE A O   
1919 C CB  . ILE A 276 ? 0.4278 0.4703 0.4010 0.0256  0.0065  -0.0227 278 ILE A CB  
1920 C CG1 . ILE A 276 ? 0.4320 0.4662 0.4006 0.0256  0.0065  -0.0208 278 ILE A CG1 
1921 C CG2 . ILE A 276 ? 0.4398 0.4717 0.4058 0.0294  0.0053  -0.0207 278 ILE A CG2 
1922 C CD1 . ILE A 276 ? 0.4377 0.4773 0.4128 0.0195  0.0082  -0.0212 278 ILE A CD1 
1923 N N   . ARG A 277 ? 0.4315 0.4999 0.4045 0.0392  0.0033  -0.0319 279 ARG A N   
1924 C CA  . ARG A 277 ? 0.4450 0.5192 0.4190 0.0411  0.0026  -0.0336 279 ARG A CA  
1925 C C   . ARG A 277 ? 0.4245 0.4817 0.3875 0.0470  0.0010  -0.0302 279 ARG A C   
1926 O O   . ARG A 277 ? 0.4298 0.4766 0.3821 0.0537  -0.0003 -0.0293 279 ARG A O   
1927 C CB  . ARG A 277 ? 0.4989 0.5944 0.4754 0.0469  0.0013  -0.0402 279 ARG A CB  
1928 C CG  . ARG A 277 ? 0.5260 0.6387 0.5133 0.0379  0.0039  -0.0442 279 ARG A CG  
1929 C CD  . ARG A 277 ? 0.5720 0.7084 0.5634 0.0408  0.0032  -0.0514 279 ARG A CD  
1930 N NE  . ARG A 277 ? 0.5880 0.7397 0.5867 0.0322  0.0062  -0.0558 279 ARG A NE  
1931 C CZ  . ARG A 277 ? 0.6015 0.7682 0.6014 0.0352  0.0059  -0.0605 279 ARG A CZ  
1932 N NH1 . ARG A 277 ? 0.6101 0.7783 0.6038 0.0481  0.0024  -0.0614 279 ARG A NH1 
1933 N NH2 . ARG A 277 ? 0.6117 0.7906 0.6176 0.0253  0.0093  -0.0644 279 ARG A NH2 
1934 N N   . TYR A 278 ? 0.3912 0.4444 0.3559 0.0435  0.0016  -0.0285 280 TYR A N   
1935 C CA  . TYR A 278 ? 0.3973 0.4349 0.3515 0.0475  0.0006  -0.0258 280 TYR A CA  
1936 C C   . TYR A 278 ? 0.3814 0.4252 0.3407 0.0455  0.0009  -0.0267 280 TYR A C   
1937 O O   . TYR A 278 ? 0.3567 0.4144 0.3270 0.0397  0.0022  -0.0289 280 TYR A O   
1938 C CB  . TYR A 278 ? 0.3854 0.4045 0.3347 0.0422  0.0021  -0.0208 280 TYR A CB  
1939 C CG  . TYR A 278 ? 0.3583 0.3792 0.3181 0.0323  0.0044  -0.0186 280 TYR A CG  
1940 C CD1 . TYR A 278 ? 0.3390 0.3663 0.3069 0.0270  0.0056  -0.0186 280 TYR A CD1 
1941 C CD2 . TYR A 278 ? 0.3462 0.3621 0.3067 0.0289  0.0053  -0.0167 280 TYR A CD2 
1942 C CE1 . TYR A 278 ? 0.3227 0.3502 0.2978 0.0196  0.0075  -0.0167 280 TYR A CE1 
1943 C CE2 . TYR A 278 ? 0.3240 0.3415 0.2928 0.0214  0.0072  -0.0148 280 TYR A CE2 
1944 C CZ  . TYR A 278 ? 0.3097 0.3327 0.2853 0.0172  0.0082  -0.0148 280 TYR A CZ  
1945 O OH  . TYR A 278 ? 0.2859 0.3094 0.2675 0.0115  0.0099  -0.0132 280 TYR A OH  
1946 N N   . THR A 279 ? 0.3808 0.4134 0.3306 0.0498  0.0000  -0.0253 281 THR A N   
1947 C CA  . THR A 279 ? 0.3848 0.4197 0.3385 0.0470  0.0005  -0.0253 281 THR A CA  
1948 C C   . THR A 279 ? 0.3839 0.4014 0.3332 0.0418  0.0021  -0.0206 281 THR A C   
1949 O O   . THR A 279 ? 0.3789 0.3807 0.3177 0.0427  0.0023  -0.0180 281 THR A O   
1950 C CB  . THR A 279 ? 0.4034 0.4440 0.3510 0.0563  -0.0020 -0.0286 281 THR A CB  
1951 O OG1 . THR A 279 ? 0.4358 0.4574 0.3666 0.0635  -0.0032 -0.0265 281 THR A OG1 
1952 C CG2 . THR A 279 ? 0.4059 0.4677 0.3582 0.0617  -0.0038 -0.0343 281 THR A CG2 
1953 N N   . ALA A 280 ? 0.3814 0.4020 0.3377 0.0364  0.0035  -0.0199 282 ALA A N   
1954 C CA  . ALA A 280 ? 0.3766 0.3845 0.3294 0.0322  0.0050  -0.0166 282 ALA A CA  
1955 C C   . ALA A 280 ? 0.3798 0.3926 0.3354 0.0323  0.0050  -0.0177 282 ALA A C   
1956 O O   . ALA A 280 ? 0.3841 0.4113 0.3473 0.0326  0.0045  -0.0208 282 ALA A O   
1957 C CB  . ALA A 280 ? 0.3532 0.3603 0.3135 0.0241  0.0072  -0.0141 282 ALA A CB  
1958 N N   . ARG A 281 ? 0.3713 0.3730 0.3212 0.0308  0.0059  -0.0156 283 ARG A N   
1959 C CA  . ARG A 281 ? 0.3832 0.3892 0.3361 0.0303  0.0061  -0.0165 283 ARG A CA  
1960 C C   . ARG A 281 ? 0.3402 0.3405 0.2963 0.0232  0.0086  -0.0137 283 ARG A C   
1961 O O   . ARG A 281 ? 0.3192 0.3087 0.2694 0.0207  0.0097  -0.0115 283 ARG A O   
1962 C CB  . ARG A 281 ? 0.4286 0.4287 0.3696 0.0383  0.0040  -0.0178 283 ARG A CB  
1963 C CG  . ARG A 281 ? 0.4845 0.4645 0.4096 0.0401  0.0044  -0.0155 283 ARG A CG  
1964 C CD  . ARG A 281 ? 0.5775 0.5498 0.4878 0.0499  0.0021  -0.0170 283 ARG A CD  
1965 N NE  . ARG A 281 ? 0.6425 0.5930 0.5374 0.0479  0.0039  -0.0144 283 ARG A NE  
1966 C CZ  . ARG A 281 ? 0.7107 0.6453 0.5933 0.0469  0.0051  -0.0127 283 ARG A CZ  
1967 N NH1 . ARG A 281 ? 0.7372 0.6751 0.6211 0.0489  0.0042  -0.0131 283 ARG A NH1 
1968 N NH2 . ARG A 281 ? 0.7525 0.6677 0.6207 0.0428  0.0076  -0.0108 283 ARG A NH2 
1969 N N   . LEU A 282 ? 0.3210 0.3290 0.2852 0.0202  0.0096  -0.0143 284 LEU A N   
1970 C CA  . LEU A 282 ? 0.3022 0.3059 0.2685 0.0153  0.0117  -0.0122 284 LEU A CA  
1971 C C   . LEU A 282 ? 0.3115 0.3030 0.2667 0.0167  0.0118  -0.0112 284 LEU A C   
1972 O O   . LEU A 282 ? 0.3521 0.3398 0.2990 0.0223  0.0101  -0.0125 284 LEU A O   
1973 C CB  . LEU A 282 ? 0.2903 0.3022 0.2636 0.0135  0.0125  -0.0136 284 LEU A CB  
1974 C CG  . LEU A 282 ? 0.2809 0.3003 0.2624 0.0099  0.0137  -0.0140 284 LEU A CG  
1975 C CD1 . LEU A 282 ? 0.2914 0.3170 0.2761 0.0083  0.0146  -0.0161 284 LEU A CD1 
1976 C CD2 . LEU A 282 ? 0.2788 0.2944 0.2630 0.0063  0.0154  -0.0113 284 LEU A CD2 
1977 N N   . ASN A 283 ? 0.3030 0.2886 0.2571 0.0117  0.0139  -0.0093 285 ASN A N   
1978 C CA  . ASN A 283 ? 0.3166 0.2899 0.2593 0.0108  0.0150  -0.0087 285 ASN A CA  
1979 C C   . ASN A 283 ? 0.3232 0.2996 0.2714 0.0064  0.0170  -0.0082 285 ASN A C   
1980 O O   . ASN A 283 ? 0.3059 0.2924 0.2649 0.0054  0.0173  -0.0083 285 ASN A O   
1981 C CB  . ASN A 283 ? 0.3181 0.2815 0.2522 0.0078  0.0161  -0.0077 285 ASN A CB  
1982 C CG  . ASN A 283 ? 0.2999 0.2712 0.2438 0.0018  0.0176  -0.0069 285 ASN A CG  
1983 O OD1 . ASN A 283 ? 0.2841 0.2620 0.2353 -0.0017 0.0191  -0.0067 285 ASN A OD1 
1984 N ND2 . ASN A 283 ? 0.2862 0.2566 0.2290 0.0013  0.0172  -0.0066 285 ASN A ND2 
1985 N N   . ASP A 284 ? 0.3605 0.3272 0.2996 0.0040  0.0187  -0.0078 286 ASP A N   
1986 C CA  . ASP A 284 ? 0.3674 0.3365 0.3100 0.0002  0.0208  -0.0077 286 ASP A CA  
1987 C C   . ASP A 284 ? 0.3525 0.3323 0.3063 -0.0042 0.0223  -0.0073 286 ASP A C   
1988 O O   . ASP A 284 ? 0.3398 0.3262 0.3004 -0.0049 0.0233  -0.0074 286 ASP A O   
1989 C CB  . ASP A 284 ? 0.4220 0.3774 0.3504 -0.0026 0.0227  -0.0077 286 ASP A CB  
1990 C CG  . ASP A 284 ? 0.4849 0.4293 0.4013 0.0035  0.0210  -0.0082 286 ASP A CG  
1991 O OD1 . ASP A 284 ? 0.4898 0.4418 0.4121 0.0093  0.0184  -0.0089 286 ASP A OD1 
1992 O OD2 . ASP A 284 ? 0.5856 0.5140 0.4857 0.0023  0.0224  -0.0081 286 ASP A OD2 
1993 N N   . ASP A 285 ? 0.3389 0.3207 0.2940 -0.0064 0.0225  -0.0070 287 ASP A N   
1994 C CA  . ASP A 285 ? 0.3267 0.3199 0.2918 -0.0093 0.0235  -0.0069 287 ASP A CA  
1995 C C   . ASP A 285 ? 0.2742 0.2756 0.2490 -0.0056 0.0220  -0.0064 287 ASP A C   
1996 O O   . ASP A 285 ? 0.2519 0.2606 0.2327 -0.0063 0.0224  -0.0062 287 ASP A O   
1997 C CB  . ASP A 285 ? 0.3604 0.3527 0.3221 -0.0135 0.0242  -0.0071 287 ASP A CB  
1998 C CG  . ASP A 285 ? 0.4106 0.3934 0.3605 -0.0191 0.0266  -0.0080 287 ASP A CG  
1999 O OD1 . ASP A 285 ? 0.4370 0.4185 0.3845 -0.0213 0.0283  -0.0086 287 ASP A OD1 
2000 O OD2 . ASP A 285 ? 0.5004 0.4761 0.4423 -0.0218 0.0270  -0.0081 287 ASP A OD2 
2001 N N   . ALA A 286 ? 0.2458 0.2459 0.2210 -0.0019 0.0206  -0.0066 288 ALA A N   
2002 C CA  . ALA A 286 ? 0.2306 0.2364 0.2123 0.0001  0.0199  -0.0068 288 ALA A CA  
2003 C C   . ALA A 286 ? 0.2147 0.2250 0.2014 -0.0002 0.0214  -0.0064 288 ALA A C   
2004 O O   . ALA A 286 ? 0.2137 0.2234 0.1996 -0.0008 0.0225  -0.0064 288 ALA A O   
2005 C CB  . ALA A 286 ? 0.2352 0.2405 0.2155 0.0027  0.0186  -0.0081 288 ALA A CB  
2006 N N   . VAL A 287 ? 0.2073 0.2208 0.1977 0.0004  0.0214  -0.0059 289 VAL A N   
2007 C CA  . VAL A 287 ? 0.2018 0.2169 0.1940 0.0018  0.0228  -0.0056 289 VAL A CA  
2008 C C   . VAL A 287 ? 0.2042 0.2160 0.1948 0.0020  0.0234  -0.0064 289 VAL A C   
2009 O O   . VAL A 287 ? 0.2132 0.2247 0.2034 0.0013  0.0227  -0.0074 289 VAL A O   
2010 C CB  . VAL A 287 ? 0.2014 0.2183 0.1949 0.0031  0.0226  -0.0049 289 VAL A CB  
2011 C CG1 . VAL A 287 ? 0.2026 0.2169 0.1942 0.0057  0.0239  -0.0046 289 VAL A CG1 
2012 C CG2 . VAL A 287 ? 0.2048 0.2272 0.2003 0.0026  0.0220  -0.0046 289 VAL A CG2 
2013 N N   . MET A 288 ? 0.2145 0.2248 0.2041 0.0028  0.0248  -0.0063 290 MET A N   
2014 C CA  . MET A 288 ? 0.2222 0.2288 0.2091 0.0020  0.0259  -0.0074 290 MET A CA  
2015 C C   . MET A 288 ? 0.2227 0.2248 0.2061 0.0027  0.0276  -0.0071 290 MET A C   
2016 O O   . MET A 288 ? 0.2235 0.2244 0.2056 0.0057  0.0283  -0.0059 290 MET A O   
2017 C CB  . MET A 288 ? 0.2401 0.2456 0.2260 0.0023  0.0268  -0.0075 290 MET A CB  
2018 C CG  . MET A 288 ? 0.2450 0.2521 0.2314 0.0016  0.0257  -0.0076 290 MET A CG  
2019 S SD  . MET A 288 ? 0.2672 0.2741 0.2517 0.0013  0.0237  -0.0093 290 MET A SD  
2020 C CE  . MET A 288 ? 0.2791 0.2826 0.2596 0.0015  0.0230  -0.0089 290 MET A CE  
2021 N N   . GLY A 289 ? 0.2226 0.2218 0.2031 0.0000  0.0284  -0.0085 291 GLY A N   
2022 C CA  . GLY A 289 ? 0.2348 0.2259 0.2084 -0.0002 0.0307  -0.0084 291 GLY A CA  
2023 C C   . GLY A 289 ? 0.2322 0.2225 0.2055 0.0031  0.0300  -0.0067 291 GLY A C   
2024 O O   . GLY A 289 ? 0.2198 0.2170 0.1991 0.0033  0.0279  -0.0063 291 GLY A O   
2025 N N   . GLY A 290 ? 0.2463 0.2280 0.2118 0.0061  0.0318  -0.0057 292 GLY A N   
2026 C CA  . GLY A 290 ? 0.2565 0.2375 0.2201 0.0114  0.0310  -0.0041 292 GLY A CA  
2027 C C   . GLY A 290 ? 0.2551 0.2366 0.2195 0.0096  0.0302  -0.0041 292 GLY A C   
2028 O O   . GLY A 290 ? 0.2693 0.2448 0.2289 0.0050  0.0318  -0.0054 292 GLY A O   
2029 N N   . LEU A 291 ? 0.2445 0.2343 0.2149 0.0122  0.0279  -0.0032 293 LEU A N   
2030 C CA  . LEU A 291 ? 0.2403 0.2315 0.2120 0.0112  0.0268  -0.0030 293 LEU A CA  
2031 C C   . LEU A 291 ? 0.2265 0.2244 0.2054 0.0063  0.0255  -0.0041 293 LEU A C   
2032 O O   . LEU A 291 ? 0.2077 0.2079 0.1886 0.0052  0.0244  -0.0040 293 LEU A O   
2033 C CB  . LEU A 291 ? 0.2396 0.2380 0.2143 0.0162  0.0249  -0.0019 293 LEU A CB  
2034 C CG  . LEU A 291 ? 0.2610 0.2547 0.2280 0.0234  0.0255  -0.0011 293 LEU A CG  
2035 C CD1 . LEU A 291 ? 0.2588 0.2629 0.2296 0.0281  0.0232  -0.0009 293 LEU A CD1 
2036 C CD2 . LEU A 291 ? 0.2854 0.2628 0.2394 0.0241  0.0276  -0.0007 293 LEU A CD2 
2037 N N   . GLY A 292 ? 0.2166 0.2179 0.1990 0.0043  0.0254  -0.0050 294 GLY A N   
2038 C CA  . GLY A 292 ? 0.2116 0.2179 0.1983 0.0013  0.0241  -0.0063 294 GLY A CA  
2039 C C   . GLY A 292 ? 0.2032 0.2148 0.1941 0.0020  0.0220  -0.0055 294 GLY A C   
2040 O O   . GLY A 292 ? 0.2100 0.2238 0.2022 0.0037  0.0216  -0.0044 294 GLY A O   
2041 N N   . ASN A 293 ? 0.2058 0.2196 0.1980 0.0006  0.0208  -0.0065 295 ASN A N   
2042 C CA  . ASN A 293 ? 0.2037 0.2198 0.1973 0.0009  0.0191  -0.0060 295 ASN A CA  
2043 C C   . ASN A 293 ? 0.2065 0.2232 0.2002 0.0005  0.0184  -0.0063 295 ASN A C   
2044 O O   . ASN A 293 ? 0.2135 0.2318 0.2070 0.0002  0.0178  -0.0079 295 ASN A O   
2045 C CB  . ASN A 293 ? 0.2061 0.2221 0.1984 0.0012  0.0182  -0.0070 295 ASN A CB  
2046 C CG  . ASN A 293 ? 0.2018 0.2167 0.1935 0.0013  0.0190  -0.0069 295 ASN A CG  
2047 O OD1 . ASN A 293 ? 0.2006 0.2145 0.1913 0.0008  0.0191  -0.0061 295 ASN A OD1 
2048 N ND2 . ASN A 293 ? 0.2076 0.2225 0.1992 0.0010  0.0199  -0.0080 295 ASN A ND2 
2049 N N   . PRO A 294 ? 0.2040 0.2200 0.1977 0.0008  0.0187  -0.0051 296 PRO A N   
2050 C CA  . PRO A 294 ? 0.2020 0.2177 0.1952 0.0001  0.0184  -0.0055 296 PRO A CA  
2051 C C   . PRO A 294 ? 0.1986 0.2161 0.1927 0.0001  0.0167  -0.0051 296 PRO A C   
2052 O O   . PRO A 294 ? 0.1952 0.2136 0.1896 0.0001  0.0162  -0.0041 296 PRO A O   
2053 C CB  . PRO A 294 ? 0.2049 0.2175 0.1958 0.0013  0.0193  -0.0042 296 PRO A CB  
2054 C CG  . PRO A 294 ? 0.2085 0.2240 0.2010 0.0035  0.0188  -0.0031 296 PRO A CG  
2055 C CD  . PRO A 294 ? 0.2059 0.2221 0.1995 0.0026  0.0191  -0.0038 296 PRO A CD  
2056 N N   . ASN A 295 ? 0.2064 0.2245 0.2001 -0.0002 0.0163  -0.0062 297 ASN A N   
2057 C CA  . ASN A 295 ? 0.2061 0.2241 0.1991 -0.0001 0.0150  -0.0057 297 ASN A CA  
2058 C C   . ASN A 295 ? 0.2092 0.2268 0.2023 -0.0008 0.0155  -0.0053 297 ASN A C   
2059 O O   . ASN A 295 ? 0.2135 0.2303 0.2057 -0.0019 0.0168  -0.0064 297 ASN A O   
2060 C CB  . ASN A 295 ? 0.2099 0.2285 0.2010 0.0012  0.0140  -0.0073 297 ASN A CB  
2061 C CG  . ASN A 295 ? 0.2171 0.2402 0.2094 0.0010  0.0144  -0.0098 297 ASN A CG  
2062 O OD1 . ASN A 295 ? 0.2041 0.2299 0.1974 0.0000  0.0155  -0.0114 297 ASN A OD1 
2063 N N   . ILE A 296 ? 0.2103 0.2277 0.2031 -0.0008 0.0146  -0.0041 298 ILE A N   
2064 C CA  . ILE A 296 ? 0.2120 0.2284 0.2040 -0.0010 0.0147  -0.0034 298 ILE A CA  
2065 C C   . ILE A 296 ? 0.2195 0.2360 0.2108 -0.0016 0.0136  -0.0036 298 ILE A C   
2066 O O   . ILE A 296 ? 0.2134 0.2299 0.2039 -0.0020 0.0128  -0.0032 298 ILE A O   
2067 C CB  . ILE A 296 ? 0.2094 0.2269 0.2015 0.0004  0.0146  -0.0020 298 ILE A CB  
2068 C CG1 . ILE A 296 ? 0.2092 0.2255 0.2007 0.0019  0.0157  -0.0020 298 ILE A CG1 
2069 C CG2 . ILE A 296 ? 0.2164 0.2318 0.2060 0.0014  0.0145  -0.0013 298 ILE A CG2 
2070 C CD1 . ILE A 296 ? 0.2115 0.2311 0.2032 0.0048  0.0153  -0.0011 298 ILE A CD1 
2071 N N   . ALA A 297 ? 0.2301 0.2459 0.2206 -0.0021 0.0141  -0.0044 299 ALA A N   
2072 C CA  . ALA A 297 ? 0.2428 0.2585 0.2322 -0.0024 0.0133  -0.0047 299 ALA A CA  
2073 C C   . ALA A 297 ? 0.2581 0.2720 0.2463 -0.0031 0.0136  -0.0039 299 ALA A C   
2074 O O   . ALA A 297 ? 0.2444 0.2558 0.2310 -0.0034 0.0150  -0.0039 299 ALA A O   
2075 C CB  . ALA A 297 ? 0.2491 0.2673 0.2385 -0.0019 0.0135  -0.0072 299 ALA A CB  
2076 N N   . ARG A 298 ? 0.2899 0.3032 0.2771 -0.0033 0.0125  -0.0031 300 ARG A N   
2077 C CA  . ARG A 298 ? 0.3176 0.3290 0.3029 -0.0038 0.0127  -0.0026 300 ARG A CA  
2078 C C   . ARG A 298 ? 0.3034 0.3146 0.2876 -0.0044 0.0119  -0.0031 300 ARG A C   
2079 O O   . ARG A 298 ? 0.2851 0.2961 0.2686 -0.0040 0.0112  -0.0033 300 ARG A O   
2080 C CB  . ARG A 298 ? 0.3650 0.3770 0.3498 -0.0025 0.0119  -0.0009 300 ARG A CB  
2081 C CG  . ARG A 298 ? 0.4372 0.4535 0.4239 -0.0031 0.0106  -0.0006 300 ARG A CG  
2082 C CD  . ARG A 298 ? 0.5284 0.5492 0.5151 -0.0028 0.0094  0.0000  300 ARG A CD  
2083 N NE  . ARG A 298 ? 0.6115 0.6372 0.5991 -0.0057 0.0090  -0.0006 300 ARG A NE  
2084 C CZ  . ARG A 298 ? 0.6659 0.6921 0.6541 -0.0071 0.0096  -0.0011 300 ARG A CZ  
2085 N NH1 . ARG A 298 ? 0.6926 0.7219 0.6796 -0.0110 0.0098  -0.0019 300 ARG A NH1 
2086 N NH2 . ARG A 298 ? 0.6623 0.6859 0.6516 -0.0054 0.0104  -0.0010 300 ARG A NH2 
2087 N N   . LEU A 299 ? 0.2934 0.3030 0.2759 -0.0052 0.0125  -0.0035 301 LEU A N   
2088 C CA  . LEU A 299 ? 0.2687 0.2777 0.2495 -0.0054 0.0119  -0.0040 301 LEU A CA  
2089 C C   . LEU A 299 ? 0.2558 0.2628 0.2349 -0.0061 0.0110  -0.0023 301 LEU A C   
2090 O O   . LEU A 299 ? 0.2481 0.2536 0.2261 -0.0060 0.0114  -0.0016 301 LEU A O   
2091 C CB  . LEU A 299 ? 0.2703 0.2810 0.2509 -0.0061 0.0134  -0.0064 301 LEU A CB  
2092 C CG  . LEU A 299 ? 0.2813 0.2914 0.2598 -0.0063 0.0132  -0.0070 301 LEU A CG  
2093 C CD1 . LEU A 299 ? 0.2835 0.2944 0.2606 -0.0035 0.0119  -0.0079 301 LEU A CD1 
2094 C CD2 . LEU A 299 ? 0.2828 0.2951 0.2608 -0.0086 0.0153  -0.0094 301 LEU A CD2 
2095 N N   . THR A 300 ? 0.2462 0.2523 0.2235 -0.0067 0.0100  -0.0019 302 THR A N   
2096 C CA  . THR A 300 ? 0.2478 0.2530 0.2230 -0.0079 0.0092  -0.0010 302 THR A CA  
2097 C C   . THR A 300 ? 0.2463 0.2485 0.2189 -0.0080 0.0096  -0.0017 302 THR A C   
2098 O O   . THR A 300 ? 0.2450 0.2455 0.2155 -0.0071 0.0097  -0.0028 302 THR A O   
2099 C CB  . THR A 300 ? 0.2530 0.2590 0.2266 -0.0101 0.0083  -0.0006 302 THR A CB  
2100 O OG1 . THR A 300 ? 0.2626 0.2732 0.2396 -0.0096 0.0082  -0.0003 302 THR A OG1 
2101 C CG2 . THR A 300 ? 0.2598 0.2672 0.2318 -0.0118 0.0075  -0.0001 302 THR A CG2 
2102 N N   . TYR A 301 ? 0.2434 0.2446 0.2151 -0.0085 0.0098  -0.0013 303 TYR A N   
2103 C CA  . TYR A 301 ? 0.2474 0.2464 0.2168 -0.0089 0.0105  -0.0023 303 TYR A CA  
2104 C C   . TYR A 301 ? 0.2445 0.2411 0.2110 -0.0099 0.0098  -0.0012 303 TYR A C   
2105 O O   . TYR A 301 ? 0.2370 0.2341 0.2033 -0.0094 0.0091  0.0000  303 TYR A O   
2106 C CB  . TYR A 301 ? 0.2458 0.2454 0.2158 -0.0094 0.0125  -0.0039 303 TYR A CB  
2107 C CG  . TYR A 301 ? 0.2434 0.2398 0.2115 -0.0097 0.0132  -0.0028 303 TYR A CG  
2108 C CD1 . TYR A 301 ? 0.2409 0.2321 0.2040 -0.0104 0.0138  -0.0022 303 TYR A CD1 
2109 C CD2 . TYR A 301 ? 0.2296 0.2265 0.1990 -0.0087 0.0135  -0.0024 303 TYR A CD2 
2110 C CE1 . TYR A 301 ? 0.2475 0.2327 0.2055 -0.0095 0.0146  -0.0013 303 TYR A CE1 
2111 C CE2 . TYR A 301 ? 0.2405 0.2321 0.2054 -0.0079 0.0143  -0.0015 303 TYR A CE2 
2112 C CZ  . TYR A 301 ? 0.2518 0.2369 0.2102 -0.0080 0.0149  -0.0009 303 TYR A CZ  
2113 O OH  . TYR A 301 ? 0.2677 0.2449 0.2187 -0.0059 0.0156  0.0001  303 TYR A OH  
2114 N N   . SER A 302 ? 0.2509 0.2453 0.2148 -0.0106 0.0099  -0.0018 304 SER A N   
2115 C CA  . SER A 302 ? 0.2618 0.2535 0.2224 -0.0116 0.0096  -0.0010 304 SER A CA  
2116 C C   . SER A 302 ? 0.2597 0.2491 0.2189 -0.0116 0.0107  -0.0009 304 SER A C   
2117 O O   . SER A 302 ? 0.2519 0.2408 0.2110 -0.0124 0.0128  -0.0026 304 SER A O   
2118 C CB  . SER A 302 ? 0.2672 0.2563 0.2249 -0.0120 0.0100  -0.0020 304 SER A CB  
2119 O OG  . SER A 302 ? 0.2810 0.2683 0.2362 -0.0121 0.0091  -0.0018 304 SER A OG  
2120 N N   . ASN A 303 ? 0.2647 0.2528 0.2215 -0.0106 0.0095  0.0005  305 ASN A N   
2121 C CA  . ASN A 303 ? 0.2875 0.2700 0.2394 -0.0094 0.0107  0.0009  305 ASN A CA  
2122 C C   . ASN A 303 ? 0.2958 0.2728 0.2415 -0.0097 0.0106  0.0015  305 ASN A C   
2123 O O   . ASN A 303 ? 0.2974 0.2673 0.2360 -0.0079 0.0113  0.0022  305 ASN A O   
2124 C CB  . ASN A 303 ? 0.2991 0.2827 0.2504 -0.0059 0.0094  0.0022  305 ASN A CB  
2125 C CG  . ASN A 303 ? 0.3167 0.3066 0.2692 -0.0039 0.0064  0.0031  305 ASN A CG  
2126 O OD1 . ASN A 303 ? 0.3330 0.3263 0.2875 -0.0064 0.0055  0.0028  305 ASN A OD1 
2127 N ND2 . ASN A 303 ? 0.3395 0.3315 0.2900 0.0004  0.0050  0.0038  305 ASN A ND2 
2128 N N   . ASP A 304 ? 0.3007 0.2792 0.2472 -0.0113 0.0099  0.0012  306 ASP A N   
2129 C CA  . ASP A 304 ? 0.3203 0.2935 0.2607 -0.0116 0.0098  0.0018  306 ASP A CA  
2130 C C   . ASP A 304 ? 0.3234 0.2958 0.2639 -0.0145 0.0110  0.0005  306 ASP A C   
2131 O O   . ASP A 304 ? 0.3225 0.2979 0.2650 -0.0152 0.0098  0.0005  306 ASP A O   
2132 C CB  . ASP A 304 ? 0.3243 0.3013 0.2641 -0.0095 0.0067  0.0031  306 ASP A CB  
2133 C CG  . ASP A 304 ? 0.3457 0.3171 0.2783 -0.0087 0.0062  0.0037  306 ASP A CG  
2134 O OD1 . ASP A 304 ? 0.3612 0.3246 0.2889 -0.0104 0.0086  0.0032  306 ASP A OD1 
2135 O OD2 . ASP A 304 ? 0.3474 0.3233 0.2792 -0.0066 0.0036  0.0043  306 ASP A OD2 
2136 N N   . PRO A 305 ? 0.3492 0.3168 0.2859 -0.0166 0.0138  -0.0008 307 PRO A N   
2137 C CA  . PRO A 305 ? 0.3603 0.3288 0.2972 -0.0187 0.0151  -0.0026 307 PRO A CA  
2138 C C   . PRO A 305 ? 0.3707 0.3355 0.3034 -0.0190 0.0140  -0.0016 307 PRO A C   
2139 O O   . PRO A 305 ? 0.3657 0.3313 0.2983 -0.0202 0.0149  -0.0030 307 PRO A O   
2140 C CB  . PRO A 305 ? 0.3632 0.3294 0.2971 -0.0218 0.0188  -0.0049 307 PRO A CB  
2141 C CG  . PRO A 305 ? 0.3730 0.3301 0.2995 -0.0214 0.0192  -0.0033 307 PRO A CG  
2142 C CD  . PRO A 305 ? 0.3653 0.3257 0.2958 -0.0173 0.0161  -0.0011 307 PRO A CD  
2143 N N   . ASN A 306 ? 0.4021 0.3642 0.3315 -0.0174 0.0118  0.0004  308 ASN A N   
2144 C CA  . ASN A 306 ? 0.4421 0.4002 0.3661 -0.0177 0.0109  0.0013  308 ASN A CA  
2145 C C   . ASN A 306 ? 0.5084 0.4711 0.4351 -0.0183 0.0087  0.0016  308 ASN A C   
2146 O O   . ASN A 306 ? 0.5796 0.5471 0.5078 -0.0173 0.0062  0.0026  308 ASN A O   
2147 C CB  . ASN A 306 ? 0.4288 0.3828 0.3468 -0.0147 0.0093  0.0029  308 ASN A CB  
2148 C CG  . ASN A 306 ? 0.4299 0.3744 0.3407 -0.0148 0.0121  0.0026  308 ASN A CG  
2149 O OD1 . ASN A 306 ? 0.4117 0.3495 0.3170 -0.0178 0.0148  0.0016  308 ASN A OD1 
2150 N ND2 . ASN A 306 ? 0.4164 0.3599 0.3263 -0.0121 0.0120  0.0032  308 ASN A ND2 
2151 N N   . GLY A 307 ? 0.5557 0.5172 0.4820 -0.0201 0.0098  0.0005  309 GLY A N   
2152 C CA  . GLY A 307 ? 0.5906 0.5520 0.5153 -0.0215 0.0085  0.0007  309 GLY A CA  
2153 C C   . GLY A 307 ? 0.6173 0.5823 0.5448 -0.0218 0.0076  0.0007  309 GLY A C   
2154 O O   . GLY A 307 ? 0.6509 0.6185 0.5824 -0.0203 0.0082  0.0002  309 GLY A O   
2155 N N   . PHE A 308 ? 0.6237 0.5884 0.5480 -0.0243 0.0063  0.0010  310 PHE A N   
2156 C CA  . PHE A 308 ? 0.6456 0.6115 0.5694 -0.0263 0.0060  0.0007  310 PHE A CA  
2157 C C   . PHE A 308 ? 0.6628 0.6377 0.5919 -0.0263 0.0044  0.0010  310 PHE A C   
2158 O O   . PHE A 308 ? 0.6735 0.6541 0.6023 -0.0278 0.0027  0.0010  310 PHE A O   
2159 C CB  . PHE A 308 ? 0.6600 0.6212 0.5763 -0.0306 0.0060  0.0003  310 PHE A CB  
2160 C CG  . PHE A 308 ? 0.6757 0.6272 0.5852 -0.0300 0.0074  0.0000  310 PHE A CG  
2161 C CD1 . PHE A 308 ? 0.6733 0.6216 0.5831 -0.0257 0.0088  -0.0005 310 PHE A CD1 
2162 C CD2 . PHE A 308 ? 0.6473 0.5939 0.5496 -0.0335 0.0074  0.0000  310 PHE A CD2 
2163 C CE1 . PHE A 308 ? 0.6758 0.6168 0.5791 -0.0240 0.0101  -0.0013 310 PHE A CE1 
2164 C CE2 . PHE A 308 ? 0.6560 0.5930 0.5510 -0.0323 0.0088  -0.0004 310 PHE A CE2 
2165 C CZ  . PHE A 308 ? 0.6721 0.6067 0.5678 -0.0271 0.0101  -0.0010 310 PHE A CZ  
2166 N N   . THR A 309 ? 0.6870 0.6642 0.6207 -0.0241 0.0049  0.0010  311 THR A N   
2167 C CA  . THR A 309 ? 0.6671 0.6528 0.6058 -0.0231 0.0036  0.0012  311 THR A CA  
2168 C C   . THR A 309 ? 0.6376 0.6232 0.5782 -0.0237 0.0045  0.0007  311 THR A C   
2169 O O   . THR A 309 ? 0.6702 0.6498 0.6094 -0.0224 0.0059  0.0005  311 THR A O   
2170 C CB  . THR A 309 ? 0.7036 0.6904 0.6445 -0.0188 0.0032  0.0020  311 THR A CB  
2171 O OG1 . THR A 309 ? 0.7126 0.7063 0.6576 -0.0169 0.0022  0.0020  311 THR A OG1 
2172 C CG2 . THR A 309 ? 0.6994 0.6798 0.6402 -0.0173 0.0054  0.0019  311 THR A CG2 
2173 N N   . SER A 310 ? 0.5795 0.5723 0.5226 -0.0252 0.0037  0.0003  312 SER A N   
2174 C CA  . SER A 310 ? 0.5508 0.5435 0.4957 -0.0253 0.0046  0.0000  312 SER A CA  
2175 C C   . SER A 310 ? 0.4874 0.4893 0.4388 -0.0228 0.0036  0.0001  312 SER A C   
2176 O O   . SER A 310 ? 0.5043 0.5099 0.4569 -0.0249 0.0038  -0.0005 312 SER A O   
2177 C CB  . SER A 310 ? 0.5696 0.5576 0.5079 -0.0305 0.0057  -0.0009 312 SER A CB  
2178 O OG  . SER A 310 ? 0.5629 0.5570 0.4991 -0.0361 0.0052  -0.0021 312 SER A OG  
2179 N N   . THR A 311 ? 0.4288 0.4322 0.3827 -0.0184 0.0029  0.0009  313 THR A N   
2180 C CA  . THR A 311 ? 0.3987 0.4081 0.3567 -0.0147 0.0022  0.0012  313 THR A CA  
2181 C C   . THR A 311 ? 0.3655 0.3700 0.3255 -0.0132 0.0038  0.0015  313 THR A C   
2182 O O   . THR A 311 ? 0.3449 0.3427 0.3033 -0.0134 0.0053  0.0014  313 THR A O   
2183 C CB  . THR A 311 ? 0.4035 0.4137 0.3597 -0.0099 0.0009  0.0019  313 THR A CB  
2184 O OG1 . THR A 311 ? 0.3995 0.3994 0.3519 -0.0087 0.0023  0.0027  313 THR A OG1 
2185 C CG2 . THR A 311 ? 0.4152 0.4321 0.3695 -0.0101 -0.0011 0.0014  313 THR A CG2 
2186 N N   . THR A 312 ? 0.3465 0.3559 0.3100 -0.0114 0.0036  0.0014  314 THR A N   
2187 C CA  . THR A 312 ? 0.3493 0.3557 0.3149 -0.0099 0.0050  0.0015  314 THR A CA  
2188 C C   . THR A 312 ? 0.3387 0.3475 0.3053 -0.0059 0.0047  0.0020  314 THR A C   
2189 O O   . THR A 312 ? 0.3429 0.3579 0.3094 -0.0035 0.0030  0.0020  314 THR A O   
2190 C CB  . THR A 312 ? 0.3373 0.3447 0.3046 -0.0124 0.0056  0.0008  314 THR A CB  
2191 O OG1 . THR A 312 ? 0.3456 0.3607 0.3143 -0.0140 0.0046  0.0003  314 THR A OG1 
2192 C CG2 . THR A 312 ? 0.3484 0.3499 0.3117 -0.0149 0.0063  0.0003  314 THR A CG2 
2193 N N   . ALA A 313 ? 0.3182 0.3219 0.2847 -0.0049 0.0064  0.0020  315 ALA A N   
2194 C CA  . ALA A 313 ? 0.3153 0.3188 0.2815 -0.0017 0.0067  0.0023  315 ALA A CA  
2195 C C   . ALA A 313 ? 0.3031 0.3078 0.2734 -0.0032 0.0079  0.0016  315 ALA A C   
2196 O O   . ALA A 313 ? 0.2794 0.2836 0.2515 -0.0058 0.0085  0.0009  315 ALA A O   
2197 C CB  . ALA A 313 ? 0.3162 0.3102 0.2755 0.0000  0.0082  0.0027  315 ALA A CB  
2198 N N   . GLU A 314 ? 0.3179 0.3240 0.2891 -0.0008 0.0080  0.0019  316 GLU A N   
2199 C CA  . GLU A 314 ? 0.3313 0.3379 0.3057 -0.0018 0.0091  0.0012  316 GLU A CA  
2200 C C   . GLU A 314 ? 0.3137 0.3130 0.2838 -0.0009 0.0112  0.0011  316 GLU A C   
2201 O O   . GLU A 314 ? 0.3186 0.3131 0.2828 0.0020  0.0112  0.0019  316 GLU A O   
2202 C CB  . GLU A 314 ? 0.3618 0.3755 0.3400 -0.0008 0.0081  0.0013  316 GLU A CB  
2203 C CG  . GLU A 314 ? 0.3924 0.4132 0.3728 -0.0031 0.0067  0.0008  316 GLU A CG  
2204 C CD  . GLU A 314 ? 0.4454 0.4753 0.4288 -0.0024 0.0060  0.0003  316 GLU A CD  
2205 O OE1 . GLU A 314 ? 0.4799 0.5162 0.4632 0.0011  0.0047  0.0002  316 GLU A OE1 
2206 O OE2 . GLU A 314 ? 0.4854 0.5165 0.4708 -0.0050 0.0067  -0.0002 316 GLU A OE2 
2207 N N   . THR A 315 ? 0.2884 0.2867 0.2600 -0.0033 0.0129  -0.0002 317 THR A N   
2208 C CA  . THR A 315 ? 0.2915 0.2836 0.2585 -0.0042 0.0155  -0.0010 317 THR A CA  
2209 C C   . THR A 315 ? 0.3162 0.3076 0.2825 -0.0010 0.0152  0.0000  317 THR A C   
2210 O O   . THR A 315 ? 0.3101 0.3086 0.2817 0.0008  0.0133  0.0005  317 THR A O   
2211 C CB  . THR A 315 ? 0.2740 0.2693 0.2443 -0.0076 0.0171  -0.0034 317 THR A CB  
2212 O OG1 . THR A 315 ? 0.2558 0.2574 0.2321 -0.0062 0.0156  -0.0032 317 THR A OG1 
2213 C CG2 . THR A 315 ? 0.2630 0.2607 0.2341 -0.0099 0.0175  -0.0050 317 THR A CG2 
2214 N N   . PRO A 316 ? 0.3454 0.3279 0.3040 -0.0006 0.0175  -0.0001 318 PRO A N   
2215 C CA  . PRO A 316 ? 0.3544 0.3355 0.3116 0.0023  0.0177  0.0004  318 PRO A CA  
2216 C C   . PRO A 316 ? 0.3423 0.3317 0.3083 0.0000  0.0175  -0.0006 318 PRO A C   
2217 O O   . PRO A 316 ? 0.3439 0.3366 0.3134 -0.0035 0.0181  -0.0022 318 PRO A O   
2218 C CB  . PRO A 316 ? 0.3670 0.3339 0.3119 0.0011  0.0211  0.0000  318 PRO A CB  
2219 C CG  . PRO A 316 ? 0.3841 0.3443 0.3224 -0.0002 0.0218  0.0000  318 PRO A CG  
2220 C CD  . PRO A 316 ? 0.3646 0.3361 0.3135 -0.0035 0.0204  -0.0010 318 PRO A CD  
2221 N N   . ASP A 317 ? 0.3683 0.3620 0.3375 0.0030  0.0163  0.0000  319 ASP A N   
2222 C CA  . ASP A 317 ? 0.3450 0.3441 0.3203 0.0013  0.0164  -0.0008 319 ASP A CA  
2223 C C   . ASP A 317 ? 0.3335 0.3283 0.3060 -0.0023 0.0192  -0.0027 319 ASP A C   
2224 O O   . ASP A 317 ? 0.3508 0.3360 0.3146 -0.0029 0.0215  -0.0029 319 ASP A O   
2225 C CB  . ASP A 317 ? 0.3659 0.3677 0.3422 0.0050  0.0157  0.0000  319 ASP A CB  
2226 C CG  . ASP A 317 ? 0.3954 0.4061 0.3762 0.0070  0.0132  0.0007  319 ASP A CG  
2227 O OD1 . ASP A 317 ? 0.4256 0.4402 0.4097 0.0043  0.0122  0.0004  319 ASP A OD1 
2228 O OD2 . ASP A 317 ? 0.4180 0.4322 0.3983 0.0110  0.0125  0.0011  319 ASP A OD2 
2229 N N   . THR A 318 ? 0.3039 0.3049 0.2818 -0.0048 0.0191  -0.0045 320 THR A N   
2230 C CA  . THR A 318 ? 0.2951 0.2967 0.2724 -0.0081 0.0212  -0.0070 320 THR A CA  
2231 C C   . THR A 318 ? 0.2898 0.2965 0.2720 -0.0066 0.0201  -0.0070 320 THR A C   
2232 O O   . THR A 318 ? 0.2684 0.2801 0.2552 -0.0047 0.0180  -0.0064 320 THR A O   
2233 C CB  . THR A 318 ? 0.2951 0.3015 0.2736 -0.0115 0.0220  -0.0098 320 THR A CB  
2234 O OG1 . THR A 318 ? 0.2771 0.2871 0.2553 -0.0153 0.0241  -0.0131 320 THR A OG1 
2235 C CG2 . THR A 318 ? 0.2950 0.3090 0.2795 -0.0091 0.0193  -0.0099 320 THR A CG2 
2236 N N   . LYS A 319 ? 0.3002 0.3046 0.2801 -0.0080 0.0220  -0.0080 321 LYS A N   
2237 C CA  . LYS A 319 ? 0.2996 0.3066 0.2825 -0.0064 0.0214  -0.0078 321 LYS A CA  
2238 C C   . LYS A 319 ? 0.2972 0.3086 0.2810 -0.0096 0.0227  -0.0110 321 LYS A C   
2239 O O   . LYS A 319 ? 0.3057 0.3147 0.2850 -0.0139 0.0254  -0.0132 321 LYS A O   
2240 C CB  . LYS A 319 ? 0.3207 0.3203 0.2988 -0.0040 0.0222  -0.0057 321 LYS A CB  
2241 C CG  . LYS A 319 ? 0.3526 0.3537 0.3327 -0.0021 0.0219  -0.0051 321 LYS A CG  
2242 C CD  . LYS A 319 ? 0.3839 0.3774 0.3576 0.0013  0.0229  -0.0035 321 LYS A CD  
2243 C CE  . LYS A 319 ? 0.3993 0.3960 0.3759 0.0039  0.0223  -0.0029 321 LYS A CE  
2244 N NZ  . LYS A 319 ? 0.4214 0.4092 0.3899 0.0063  0.0243  -0.0025 321 LYS A NZ  
2245 N N   . ALA A 320 ? 0.2820 0.2998 0.2704 -0.0080 0.0211  -0.0117 322 ALA A N   
2246 C CA  . ALA A 320 ? 0.2733 0.2956 0.2623 -0.0097 0.0221  -0.0144 322 ALA A CA  
2247 C C   . ALA A 320 ? 0.2614 0.2811 0.2510 -0.0075 0.0216  -0.0127 322 ALA A C   
2248 O O   . ALA A 320 ? 0.2500 0.2670 0.2405 -0.0046 0.0203  -0.0099 322 ALA A O   
2249 C CB  . ALA A 320 ? 0.2648 0.2972 0.2574 -0.0085 0.0205  -0.0173 322 ALA A CB  
2250 N N   . ASN A 321 ? 0.2682 0.2901 0.2574 -0.0092 0.0227  -0.0147 323 ASN A N   
2251 C CA  . ASN A 321 ? 0.2700 0.2887 0.2588 -0.0077 0.0228  -0.0133 323 ASN A CA  
2252 C C   . ASN A 321 ? 0.2795 0.3048 0.2700 -0.0083 0.0225  -0.0161 323 ASN A C   
2253 O O   . ASN A 321 ? 0.2991 0.3302 0.2891 -0.0117 0.0237  -0.0197 323 ASN A O   
2254 C CB  . ASN A 321 ? 0.2790 0.2881 0.2621 -0.0087 0.0252  -0.0119 323 ASN A CB  
2255 C CG  . ASN A 321 ? 0.2862 0.2926 0.2701 -0.0048 0.0244  -0.0092 323 ASN A CG  
2256 O OD1 . ASN A 321 ? 0.2912 0.3023 0.2794 -0.0031 0.0227  -0.0089 323 ASN A OD1 
2257 N ND2 . ASN A 321 ? 0.2750 0.2736 0.2535 -0.0033 0.0258  -0.0076 323 ASN A ND2 
2258 N N   . VAL A 322 ? 0.2612 0.2864 0.2531 -0.0052 0.0210  -0.0148 324 VAL A N   
2259 C CA  . VAL A 322 ? 0.2596 0.2893 0.2520 -0.0048 0.0206  -0.0169 324 VAL A CA  
2260 C C   . VAL A 322 ? 0.2526 0.2762 0.2437 -0.0045 0.0216  -0.0148 324 VAL A C   
2261 O O   . VAL A 322 ? 0.2402 0.2601 0.2317 -0.0021 0.0207  -0.0121 324 VAL A O   
2262 C CB  . VAL A 322 ? 0.2647 0.2987 0.2579 -0.0003 0.0177  -0.0174 324 VAL A CB  
2263 C CG1 . VAL A 322 ? 0.2680 0.3072 0.2606 0.0010  0.0169  -0.0199 324 VAL A CG1 
2264 C CG2 . VAL A 322 ? 0.2693 0.3086 0.2633 0.0004  0.0167  -0.0190 324 VAL A CG2 
2265 N N   . TYR A 323 ? 0.2564 0.2792 0.2453 -0.0073 0.0236  -0.0165 325 TYR A N   
2266 C CA  . TYR A 323 ? 0.2501 0.2673 0.2371 -0.0068 0.0247  -0.0150 325 TYR A CA  
2267 C C   . TYR A 323 ? 0.2417 0.2639 0.2300 -0.0057 0.0234  -0.0166 325 TYR A C   
2268 O O   . TYR A 323 ? 0.2365 0.2667 0.2260 -0.0057 0.0222  -0.0196 325 TYR A O   
2269 C CB  . TYR A 323 ? 0.2638 0.2745 0.2450 -0.0108 0.0280  -0.0159 325 TYR A CB  
2270 C CG  . TYR A 323 ? 0.2799 0.2834 0.2570 -0.0113 0.0295  -0.0145 325 TYR A CG  
2271 C CD1 . TYR A 323 ? 0.2891 0.2854 0.2638 -0.0074 0.0296  -0.0113 325 TYR A CD1 
2272 C CD2 . TYR A 323 ? 0.2897 0.2942 0.2646 -0.0153 0.0307  -0.0166 325 TYR A CD2 
2273 C CE1 . TYR A 323 ? 0.3007 0.2900 0.2703 -0.0066 0.0306  -0.0100 325 TYR A CE1 
2274 C CE2 . TYR A 323 ? 0.3006 0.2966 0.2700 -0.0156 0.0322  -0.0152 325 TYR A CE2 
2275 C CZ  . TYR A 323 ? 0.3021 0.2898 0.2683 -0.0108 0.0319  -0.0118 325 TYR A CZ  
2276 O OH  . TYR A 323 ? 0.3066 0.2858 0.2663 -0.0096 0.0329  -0.0104 325 TYR A OH  
2277 N N   . THR A 324 ? 0.2465 0.2728 0.2429 -0.0096 0.0009  -0.0335 326 THR A N   
2278 C CA  . THR A 324 ? 0.2389 0.2647 0.2374 -0.0100 0.0003  -0.0325 326 THR A CA  
2279 C C   . THR A 324 ? 0.2448 0.2635 0.2378 -0.0096 0.0012  -0.0296 326 THR A C   
2280 O O   . THR A 324 ? 0.2479 0.2639 0.2371 -0.0074 0.0017  -0.0286 326 THR A O   
2281 C CB  . THR A 324 ? 0.2324 0.2607 0.2379 -0.0075 -0.0016 -0.0336 326 THR A CB  
2282 O OG1 . THR A 324 ? 0.2384 0.2672 0.2452 -0.0072 -0.0022 -0.0331 326 THR A OG1 
2283 C CG2 . THR A 324 ? 0.2313 0.2568 0.2380 -0.0065 -0.0022 -0.0326 326 THR A CG2 
2284 N N   . TYR A 325 ? 0.2447 0.2615 0.2370 -0.0109 0.0013  -0.0283 327 TYR A N   
2285 C CA  . TYR A 325 ? 0.2561 0.2653 0.2414 -0.0106 0.0024  -0.0257 327 TYR A CA  
2286 C C   . TYR A 325 ? 0.2476 0.2586 0.2388 -0.0094 0.0011  -0.0245 327 TYR A C   
2287 O O   . TYR A 325 ? 0.2374 0.2529 0.2356 -0.0092 -0.0004 -0.0255 327 TYR A O   
2288 C CB  . TYR A 325 ? 0.2742 0.2772 0.2493 -0.0150 0.0046  -0.0256 327 TYR A CB  
2289 C CG  . TYR A 325 ? 0.2955 0.2992 0.2661 -0.0185 0.0058  -0.0276 327 TYR A CG  
2290 C CD1 . TYR A 325 ? 0.2994 0.2982 0.2643 -0.0162 0.0065  -0.0274 327 TYR A CD1 
2291 C CD2 . TYR A 325 ? 0.3012 0.3131 0.2738 -0.0237 0.0062  -0.0300 327 TYR A CD2 
2292 C CE1 . TYR A 325 ? 0.3138 0.3133 0.2744 -0.0197 0.0076  -0.0292 327 TYR A CE1 
2293 C CE2 . TYR A 325 ? 0.3071 0.3219 0.2757 -0.0277 0.0073  -0.0321 327 TYR A CE2 
2294 C CZ  . TYR A 325 ? 0.3131 0.3208 0.2759 -0.0259 0.0081  -0.0316 327 TYR A CZ  
2295 O OH  . TYR A 325 ? 0.3018 0.3121 0.2604 -0.0300 0.0092  -0.0336 327 TYR A OH  
2296 N N   . GLN A 326 ? 0.2513 0.2574 0.2378 -0.0079 0.0016  -0.0223 328 GLN A N   
2297 C CA  . GLN A 326 ? 0.2409 0.2484 0.2316 -0.0072 0.0006  -0.0208 328 GLN A CA  
2298 C C   . GLN A 326 ? 0.2364 0.2379 0.2204 -0.0082 0.0018  -0.0192 328 GLN A C   
2299 O O   . GLN A 326 ? 0.2430 0.2375 0.2173 -0.0065 0.0033  -0.0181 328 GLN A O   
2300 C CB  . GLN A 326 ? 0.2422 0.2532 0.2343 -0.0044 0.0000  -0.0202 328 GLN A CB  
2301 C CG  . GLN A 326 ? 0.2462 0.2591 0.2412 -0.0046 -0.0007 -0.0187 328 GLN A CG  
2302 C CD  . GLN A 326 ? 0.2540 0.2745 0.2505 -0.0034 -0.0011 -0.0188 328 GLN A CD  
2303 O OE1 . GLN A 326 ? 0.2732 0.2981 0.2697 -0.0023 -0.0011 -0.0202 328 GLN A OE1 
2304 N NE2 . GLN A 326 ? 0.2503 0.2741 0.2478 -0.0038 -0.0015 -0.0176 328 GLN A NE2 
2305 N N   . LEU A 327 ? 0.2283 0.2317 0.2159 -0.0103 0.0013  -0.0190 329 LEU A N   
2306 C CA  . LEU A 327 ? 0.2266 0.2252 0.2089 -0.0114 0.0022  -0.0174 329 LEU A CA  
2307 C C   . LEU A 327 ? 0.2228 0.2225 0.2081 -0.0085 0.0012  -0.0154 329 LEU A C   
2308 O O   . LEU A 327 ? 0.2125 0.2170 0.2053 -0.0084 -0.0003 -0.0154 329 LEU A O   
2309 C CB  . LEU A 327 ? 0.2282 0.2309 0.2128 -0.0151 0.0022  -0.0184 329 LEU A CB  
2310 C CG  . LEU A 327 ? 0.2308 0.2310 0.2119 -0.0169 0.0028  -0.0171 329 LEU A CG  
2311 C CD1 . LEU A 327 ? 0.2424 0.2320 0.2098 -0.0201 0.0054  -0.0168 329 LEU A CD1 
2312 C CD2 . LEU A 327 ? 0.2315 0.2409 0.2177 -0.0191 0.0021  -0.0183 329 LEU A CD2 
2313 N N   . LYS A 328 ? 0.2297 0.2243 0.2074 -0.0060 0.0022  -0.0139 330 LYS A N   
2314 C CA  . LYS A 328 ? 0.2188 0.2164 0.1981 -0.0034 0.0016  -0.0123 330 LYS A CA  
2315 C C   . LYS A 328 ? 0.2240 0.2157 0.1979 -0.0045 0.0024  -0.0110 330 LYS A C   
2316 O O   . LYS A 328 ? 0.2381 0.2204 0.2004 -0.0034 0.0042  -0.0108 330 LYS A O   
2317 C CB  . LYS A 328 ? 0.2242 0.2231 0.1980 0.0022  0.0019  -0.0119 330 LYS A CB  
2318 C CG  . LYS A 328 ? 0.2189 0.2254 0.1947 0.0048  0.0012  -0.0107 330 LYS A CG  
2319 C CD  . LYS A 328 ? 0.2272 0.2373 0.1958 0.0121  0.0016  -0.0105 330 LYS A CD  
2320 C CE  . LYS A 328 ? 0.2228 0.2430 0.1957 0.0131  0.0009  -0.0120 330 LYS A CE  
2321 N NZ  . LYS A 328 ? 0.2119 0.2434 0.1962 0.0072  -0.0003 -0.0128 330 LYS A NZ  
2322 N N   . VAL A 329 ? 0.2152 0.2112 0.1958 -0.0066 0.0014  -0.0103 331 VAL A N   
2323 C CA  . VAL A 329 ? 0.2202 0.2127 0.1971 -0.0079 0.0020  -0.0092 331 VAL A CA  
2324 C C   . VAL A 329 ? 0.2254 0.2209 0.2029 -0.0047 0.0015  -0.0075 331 VAL A C   
2325 O O   . VAL A 329 ? 0.2168 0.2198 0.2022 -0.0052 0.0000  -0.0071 331 VAL A O   
2326 C CB  . VAL A 329 ? 0.2128 0.2095 0.1961 -0.0116 0.0012  -0.0097 331 VAL A CB  
2327 C CG1 . VAL A 329 ? 0.2129 0.2075 0.1925 -0.0135 0.0020  -0.0088 331 VAL A CG1 
2328 C CG2 . VAL A 329 ? 0.2141 0.2126 0.1978 -0.0143 0.0016  -0.0119 331 VAL A CG2 
2329 N N   . ASN A 330 ? 0.2371 0.2264 0.2048 -0.0016 0.0027  -0.0067 332 ASN A N   
2330 C CA  . ASN A 330 ? 0.2439 0.2376 0.2110 0.0020  0.0023  -0.0053 332 ASN A CA  
2331 C C   . ASN A 330 ? 0.2484 0.2390 0.2147 -0.0007 0.0026  -0.0044 332 ASN A C   
2332 O O   . ASN A 330 ? 0.2574 0.2375 0.2144 -0.0024 0.0042  -0.0047 332 ASN A O   
2333 C CB  . ASN A 330 ? 0.2600 0.2493 0.2152 0.0095  0.0034  -0.0052 332 ASN A CB  
2334 C CG  . ASN A 330 ? 0.2659 0.2629 0.2233 0.0131  0.0027  -0.0061 332 ASN A CG  
2335 O OD1 . ASN A 330 ? 0.2579 0.2683 0.2257 0.0114  0.0014  -0.0065 332 ASN A OD1 
2336 N ND2 . ASN A 330 ? 0.2909 0.2786 0.2369 0.0176  0.0040  -0.0066 332 ASN A ND2 
2337 N N   . LYS A 331 ? 0.2440 0.2428 0.2187 -0.0023 0.0013  -0.0034 333 LYS A N   
2338 C CA  . LYS A 331 ? 0.2620 0.2597 0.2367 -0.0045 0.0013  -0.0023 333 LYS A CA  
2339 C C   . LYS A 331 ? 0.2650 0.2635 0.2340 0.0000  0.0018  -0.0013 333 LYS A C   
2340 O O   . LYS A 331 ? 0.2466 0.2552 0.2200 0.0018  0.0008  -0.0008 333 LYS A O   
2341 C CB  . LYS A 331 ? 0.2636 0.2681 0.2484 -0.0078 -0.0002 -0.0015 333 LYS A CB  
2342 C CG  . LYS A 331 ? 0.2835 0.2868 0.2692 -0.0105 -0.0002 -0.0009 333 LYS A CG  
2343 C CD  . LYS A 331 ? 0.3029 0.2999 0.2797 -0.0107 0.0014  -0.0012 333 LYS A CD  
2344 C CE  . LYS A 331 ? 0.3162 0.3141 0.2936 -0.0148 0.0017  -0.0017 333 LYS A CE  
2345 N NZ  . LYS A 331 ? 0.3315 0.3226 0.2990 -0.0163 0.0035  -0.0019 333 LYS A NZ  
2346 N N   . VAL A 332 ? 0.2875 0.2761 0.2458 0.0012  0.0033  -0.0012 334 VAL A N   
2347 C CA  . VAL A 332 ? 0.3143 0.3019 0.2645 0.0072  0.0038  -0.0005 334 VAL A CA  
2348 C C   . VAL A 332 ? 0.3425 0.3234 0.2880 0.0042  0.0047  0.0000  334 VAL A C   
2349 O O   . VAL A 332 ? 0.3251 0.3035 0.2735 -0.0024 0.0050  -0.0004 334 VAL A O   
2350 C CB  . VAL A 332 ? 0.3342 0.3126 0.2698 0.0149  0.0051  -0.0011 334 VAL A CB  
2351 C CG1 . VAL A 332 ? 0.3468 0.3347 0.2875 0.0183  0.0041  -0.0017 334 VAL A CG1 
2352 C CG2 . VAL A 332 ? 0.3533 0.3121 0.2750 0.0122  0.0073  -0.0020 334 VAL A CG2 
2353 N N   . LYS A 333 ? 0.3870 0.3675 0.3259 0.0094  0.0050  0.0005  335 LYS A N   
2354 C CA  . LYS A 333 ? 0.4464 0.4189 0.3778 0.0078  0.0061  0.0008  335 LYS A CA  
2355 C C   . LYS A 333 ? 0.5255 0.4806 0.4359 0.0144  0.0082  0.0001  335 LYS A C   
2356 O O   . LYS A 333 ? 0.5566 0.5078 0.4602 0.0207  0.0085  -0.0002 335 LYS A O   
2357 C CB  . LYS A 333 ? 0.4287 0.4148 0.3696 0.0079  0.0047  0.0022  335 LYS A CB  
2358 C CG  . LYS A 333 ? 0.4272 0.4263 0.3705 0.0149  0.0036  0.0026  335 LYS A CG  
2359 C CD  . LYS A 333 ? 0.4233 0.4380 0.3793 0.0112  0.0020  0.0038  335 LYS A CD  
2360 C CE  . LYS A 333 ? 0.4406 0.4719 0.3998 0.0156  0.0011  0.0036  335 LYS A CE  
2361 N NZ  . LYS A 333 ? 0.4535 0.4990 0.4220 0.0107  0.0000  0.0047  335 LYS A NZ  
2362 N N   . GLU A 334 ? 0.5701 0.5133 0.4688 0.0133  0.0098  0.0000  336 GLU A N   
2363 C CA  . GLU A 334 ? 0.6163 0.5348 0.4900 0.0164  0.0125  -0.0009 336 GLU A CA  
2364 C C   . GLU A 334 ? 0.6136 0.5299 0.4764 0.0307  0.0122  -0.0006 336 GLU A C   
2365 O O   . GLU A 334 ? 0.6500 0.5467 0.4930 0.0356  0.0140  -0.0012 336 GLU A O   
2366 C CB  . GLU A 334 ? 0.6739 0.5812 0.5379 0.0107  0.0142  -0.0014 336 GLU A CB  
2367 C CG  . GLU A 334 ? 0.7071 0.6181 0.5796 -0.0028 0.0147  -0.0024 336 GLU A CG  
2368 C CD  . GLU A 334 ? 0.7709 0.6785 0.6389 -0.0100 0.0160  -0.0030 336 GLU A CD  
2369 O OE1 . GLU A 334 ? 0.7977 0.7181 0.6764 -0.0080 0.0144  -0.0018 336 GLU A OE1 
2370 O OE2 . GLU A 334 ? 0.8172 0.7102 0.6709 -0.0186 0.0187  -0.0049 336 GLU A OE2 
2371 N N   . ASN A 335 ? 0.5875 0.5249 0.4626 0.0369  0.0100  0.0001  337 ASN A N   
2372 C CA  . ASN A 335 ? 0.6152 0.5577 0.4819 0.0514  0.0095  0.0000  337 ASN A CA  
2373 C C   . ASN A 335 ? 0.6114 0.5645 0.4855 0.0539  0.0084  -0.0002 337 ASN A C   
2374 O O   . ASN A 335 ? 0.6160 0.5823 0.4883 0.0651  0.0074  -0.0006 337 ASN A O   
2375 C CB  . ASN A 335 ? 0.6118 0.5752 0.4875 0.0560  0.0078  0.0005  337 ASN A CB  
2376 C CG  . ASN A 335 ? 0.5852 0.5744 0.4859 0.0479  0.0057  0.0011  337 ASN A CG  
2377 O OD1 . ASN A 335 ? 0.5854 0.5834 0.4960 0.0450  0.0048  0.0009  337 ASN A OD1 
2378 N ND2 . ASN A 335 ? 0.5517 0.5517 0.4610 0.0441  0.0049  0.0018  337 ASN A ND2 
2379 N N   . GLN A 336 ? 0.5822 0.5337 0.4658 0.0438  0.0084  -0.0003 338 GLN A N   
2380 C CA  . GLN A 336 ? 0.5921 0.5499 0.4813 0.0447  0.0077  -0.0009 338 GLN A CA  
2381 C C   . GLN A 336 ? 0.5380 0.5242 0.4462 0.0451  0.0053  -0.0009 338 GLN A C   
2382 O O   . GLN A 336 ? 0.5152 0.5086 0.4277 0.0463  0.0047  -0.0015 338 GLN A O   
2383 C CB  . GLN A 336 ? 0.6328 0.5763 0.5009 0.0567  0.0089  -0.0013 338 GLN A CB  
2384 C CG  . GLN A 336 ? 0.6678 0.5790 0.5118 0.0557  0.0118  -0.0015 338 GLN A CG  
2385 C CD  . GLN A 336 ? 0.6683 0.5713 0.5173 0.0418  0.0128  -0.0019 338 GLN A CD  
2386 O OE1 . GLN A 336 ? 0.7179 0.6213 0.5694 0.0404  0.0127  -0.0024 338 GLN A OE1 
2387 N NE2 . GLN A 336 ? 0.6514 0.5497 0.5027 0.0314  0.0136  -0.0021 338 GLN A NE2 
2388 N N   . GLN A 337 ? 0.5075 0.5089 0.4258 0.0431  0.0042  -0.0003 339 GLN A N   
2389 C CA  . GLN A 337 ? 0.4809 0.5076 0.4164 0.0394  0.0023  -0.0004 339 GLN A CA  
2390 C C   . GLN A 337 ? 0.4086 0.4337 0.3573 0.0271  0.0018  0.0000  339 GLN A C   
2391 O O   . GLN A 337 ? 0.3838 0.3944 0.3310 0.0218  0.0026  0.0004  339 GLN A O   
2392 C CB  . GLN A 337 ? 0.5232 0.5666 0.4624 0.0412  0.0015  -0.0001 339 GLN A CB  
2393 C CG  . GLN A 337 ? 0.5862 0.6424 0.5159 0.0547  0.0014  -0.0013 339 GLN A CG  
2394 C CD  . GLN A 337 ? 0.6311 0.7092 0.5662 0.0577  0.0004  -0.0029 339 GLN A CD  
2395 O OE1 . GLN A 337 ? 0.6577 0.7407 0.6038 0.0488  0.0000  -0.0031 339 GLN A OE1 
2396 N NE2 . GLN A 337 ? 0.6325 0.7252 0.5592 0.0707  0.0002  -0.0042 339 GLN A NE2 
2397 N N   . ALA A 338 ? 0.3695 0.4095 0.3295 0.0230  0.0006  -0.0005 340 ALA A N   
2398 C CA  . ALA A 338 ? 0.3341 0.3722 0.3044 0.0133  0.0000  -0.0002 340 ALA A CA  
2399 C C   . ALA A 338 ? 0.3081 0.3437 0.2832 0.0071  -0.0002 0.0012  340 ALA A C   
2400 O O   . ALA A 338 ? 0.3231 0.3672 0.2983 0.0082  -0.0005 0.0018  340 ALA A O   
2401 C CB  . ALA A 338 ? 0.3289 0.3828 0.3069 0.0102  -0.0008 -0.0012 340 ALA A CB  
2402 N N   . LEU A 339 ? 0.2745 0.3009 0.2534 0.0015  -0.0004 0.0015  341 LEU A N   
2403 C CA  . LEU A 339 ? 0.2557 0.2813 0.2396 -0.0037 -0.0010 0.0029  341 LEU A CA  
2404 C C   . LEU A 339 ? 0.2373 0.2643 0.2281 -0.0090 -0.0020 0.0030  341 LEU A C   
2405 O O   . LEU A 339 ? 0.2473 0.2686 0.2388 -0.0095 -0.0021 0.0021  341 LEU A O   
2406 C CB  . LEU A 339 ? 0.2557 0.2701 0.2358 -0.0045 -0.0002 0.0030  341 LEU A CB  
2407 C CG  . LEU A 339 ? 0.2515 0.2660 0.2359 -0.0086 -0.0008 0.0042  341 LEU A CG  
2408 C CD1 . LEU A 339 ? 0.2561 0.2775 0.2416 -0.0085 -0.0012 0.0058  341 LEU A CD1 
2409 C CD2 . LEU A 339 ? 0.2559 0.2632 0.2354 -0.0097 0.0002  0.0036  341 LEU A CD2 
2410 N N   . ALA A 340 ? 0.2254 0.2587 0.2191 -0.0130 -0.0028 0.0040  342 ALA A N   
2411 C CA  . ALA A 340 ? 0.2221 0.2519 0.2183 -0.0184 -0.0036 0.0044  342 ALA A CA  
2412 C C   . ALA A 340 ? 0.2108 0.2311 0.2072 -0.0187 -0.0041 0.0055  342 ALA A C   
2413 O O   . ALA A 340 ? 0.2022 0.2220 0.1980 -0.0168 -0.0038 0.0062  342 ALA A O   
2414 C CB  . ALA A 340 ? 0.2313 0.2681 0.2272 -0.0239 -0.0038 0.0051  342 ALA A CB  
2415 N N   . GLY A 341 ? 0.2082 0.2217 0.2044 -0.0205 -0.0048 0.0054  343 GLY A N   
2416 C CA  . GLY A 341 ? 0.2227 0.2288 0.2174 -0.0201 -0.0056 0.0067  343 GLY A CA  
2417 C C   . GLY A 341 ? 0.2229 0.2271 0.2189 -0.0161 -0.0058 0.0055  343 GLY A C   
2418 O O   . GLY A 341 ? 0.2376 0.2397 0.2327 -0.0141 -0.0065 0.0063  343 GLY A O   
2419 N N   . ALA A 342 ? 0.2166 0.2231 0.2143 -0.0149 -0.0052 0.0036  344 ALA A N   
2420 C CA  . ALA A 342 ? 0.2246 0.2310 0.2230 -0.0128 -0.0051 0.0019  344 ALA A CA  
2421 C C   . ALA A 342 ? 0.2386 0.2412 0.2370 -0.0116 -0.0060 0.0009  344 ALA A C   
2422 O O   . ALA A 342 ? 0.2518 0.2511 0.2492 -0.0134 -0.0061 0.0009  344 ALA A O   
2423 C CB  . ALA A 342 ? 0.2201 0.2283 0.2175 -0.0129 -0.0037 0.0004  344 ALA A CB  
2424 N N   . GLY A 343 ? 0.2413 0.2453 0.2399 -0.0088 -0.0065 -0.0002 345 GLY A N   
2425 C CA  . GLY A 343 ? 0.2505 0.2520 0.2486 -0.0063 -0.0073 -0.0019 345 GLY A CA  
2426 C C   . GLY A 343 ? 0.2462 0.2556 0.2465 -0.0053 -0.0068 -0.0043 345 GLY A C   
2427 O O   . GLY A 343 ? 0.2528 0.2689 0.2535 -0.0061 -0.0062 -0.0046 345 GLY A O   
2428 N N   . PHE A 344 ? 0.2461 0.2553 0.2470 -0.0044 -0.0069 -0.0063 346 PHE A N   
2429 C CA  . PHE A 344 ? 0.2366 0.2539 0.2388 -0.0049 -0.0061 -0.0090 346 PHE A CA  
2430 C C   . PHE A 344 ? 0.2549 0.2740 0.2571 -0.0004 -0.0073 -0.0109 346 PHE A C   
2431 O O   . PHE A 344 ? 0.2589 0.2693 0.2595 0.0014  -0.0081 -0.0105 346 PHE A O   
2432 C CB  . PHE A 344 ? 0.2167 0.2318 0.2184 -0.0088 -0.0045 -0.0096 346 PHE A CB  
2433 C CG  . PHE A 344 ? 0.2082 0.2215 0.2072 -0.0119 -0.0030 -0.0083 346 PHE A CG  
2434 C CD1 . PHE A 344 ? 0.2147 0.2317 0.2106 -0.0151 -0.0016 -0.0095 346 PHE A CD1 
2435 C CD2 . PHE A 344 ? 0.2054 0.2139 0.2037 -0.0119 -0.0030 -0.0063 346 PHE A CD2 
2436 C CE1 . PHE A 344 ? 0.2193 0.2316 0.2101 -0.0176 -0.0002 -0.0084 346 PHE A CE1 
2437 C CE2 . PHE A 344 ? 0.2099 0.2165 0.2045 -0.0131 -0.0017 -0.0054 346 PHE A CE2 
2438 C CZ  . PHE A 344 ? 0.2124 0.2192 0.2026 -0.0157 -0.0003 -0.0063 346 PHE A CZ  
2439 N N   . THR A 345 ? 0.2688 0.2999 0.2720 0.0009  -0.0073 -0.0132 347 THR A N   
2440 C CA  . THR A 345 ? 0.2789 0.3163 0.2821 0.0058  -0.0083 -0.0159 347 THR A CA  
2441 C C   . THR A 345 ? 0.2714 0.3184 0.2765 0.0007  -0.0067 -0.0187 347 THR A C   
2442 O O   . THR A 345 ? 0.2617 0.3143 0.2661 -0.0052 -0.0051 -0.0191 347 THR A O   
2443 C CB  . THR A 345 ? 0.2923 0.3378 0.2937 0.0134  -0.0100 -0.0164 347 THR A CB  
2444 O OG1 . THR A 345 ? 0.2985 0.3302 0.2957 0.0170  -0.0111 -0.0133 347 THR A OG1 
2445 C CG2 . THR A 345 ? 0.3069 0.3591 0.3070 0.0206  -0.0112 -0.0192 347 THR A CG2 
2446 N N   . LEU A 346 ? 0.2855 0.3311 0.2911 0.0020  -0.0070 -0.0203 348 LEU A N   
2447 C CA  . LEU A 346 ? 0.2902 0.3437 0.2963 -0.0027 -0.0055 -0.0230 348 LEU A CA  
2448 C C   . LEU A 346 ? 0.3087 0.3760 0.3160 0.0026  -0.0067 -0.0262 348 LEU A C   
2449 O O   . LEU A 346 ? 0.3198 0.3823 0.3263 0.0103  -0.0085 -0.0262 348 LEU A O   
2450 C CB  . LEU A 346 ? 0.2847 0.3269 0.2903 -0.0050 -0.0047 -0.0223 348 LEU A CB  
2451 C CG  . LEU A 346 ? 0.2812 0.3281 0.2854 -0.0102 -0.0030 -0.0246 348 LEU A CG  
2452 C CD1 . LEU A 346 ? 0.2804 0.3268 0.2795 -0.0179 -0.0007 -0.0244 348 LEU A CD1 
2453 C CD2 . LEU A 346 ? 0.2765 0.3136 0.2807 -0.0098 -0.0029 -0.0241 348 LEU A CD2 
2454 N N   . TYR A 347 ? 0.3323 0.4159 0.3396 -0.0019 -0.0055 -0.0290 349 TYR A N   
2455 C CA  . TYR A 347 ? 0.3581 0.4612 0.3668 0.0025  -0.0064 -0.0329 349 TYR A CA  
2456 C C   . TYR A 347 ? 0.3676 0.4757 0.3758 -0.0049 -0.0046 -0.0354 349 TYR A C   
2457 O O   . TYR A 347 ? 0.3535 0.4554 0.3583 -0.0150 -0.0021 -0.0347 349 TYR A O   
2458 C CB  . TYR A 347 ? 0.3703 0.4942 0.3791 0.0026  -0.0065 -0.0347 349 TYR A CB  
2459 C CG  . TYR A 347 ? 0.3717 0.4925 0.3800 0.0104  -0.0083 -0.0323 349 TYR A CG  
2460 C CD1 . TYR A 347 ? 0.3646 0.4765 0.3721 0.0052  -0.0074 -0.0294 349 TYR A CD1 
2461 C CD2 . TYR A 347 ? 0.3866 0.5134 0.3935 0.0234  -0.0108 -0.0331 349 TYR A CD2 
2462 C CE1 . TYR A 347 ? 0.3697 0.4792 0.3762 0.0119  -0.0089 -0.0272 349 TYR A CE1 
2463 C CE2 . TYR A 347 ? 0.3926 0.5152 0.3968 0.0309  -0.0124 -0.0308 349 TYR A CE2 
2464 C CZ  . TYR A 347 ? 0.3828 0.4975 0.3874 0.0246  -0.0114 -0.0278 349 TYR A CZ  
2465 O OH  . TYR A 347 ? 0.3952 0.5056 0.3966 0.0320  -0.0129 -0.0255 349 TYR A OH  
2466 N N   . LYS A 348 ? 0.4056 0.5240 0.4154 0.0001  -0.0056 -0.0383 350 LYS A N   
2467 C CA  . LYS A 348 ? 0.4252 0.5534 0.4342 -0.0072 -0.0038 -0.0414 350 LYS A CA  
2468 C C   . LYS A 348 ? 0.4749 0.6328 0.4849 -0.0066 -0.0040 -0.0459 350 LYS A C   
2469 O O   . LYS A 348 ? 0.4877 0.6560 0.4996 0.0051  -0.0065 -0.0469 350 LYS A O   
2470 C CB  . LYS A 348 ? 0.4246 0.5427 0.4347 -0.0034 -0.0045 -0.0415 350 LYS A CB  
2471 C CG  . LYS A 348 ? 0.4175 0.5408 0.4256 -0.0124 -0.0023 -0.0438 350 LYS A CG  
2472 C CD  . LYS A 348 ? 0.4095 0.5258 0.4189 -0.0088 -0.0030 -0.0443 350 LYS A CD  
2473 C CE  . LYS A 348 ? 0.4132 0.5348 0.4194 -0.0183 -0.0006 -0.0465 350 LYS A CE  
2474 N NZ  . LYS A 348 ? 0.4287 0.5504 0.4374 -0.0134 -0.0017 -0.0480 350 LYS A NZ  
2475 N N   . LYS A 349 ? 0.5387 0.7094 0.5457 -0.0190 -0.0014 -0.0486 351 LYS A N   
2476 C CA  . LYS A 349 ? 0.6152 0.8189 0.6231 -0.0208 -0.0012 -0.0540 351 LYS A CA  
2477 C C   . LYS A 349 ? 0.6296 0.8399 0.6399 -0.0147 -0.0023 -0.0564 351 LYS A C   
2478 O O   . LYS A 349 ? 0.5508 0.7505 0.5587 -0.0223 -0.0005 -0.0563 351 LYS A O   
2479 C CB  . LYS A 349 ? 0.6706 0.8832 0.6719 -0.0385 0.0024  -0.0561 351 LYS A CB  
2480 C CG  . LYS A 349 ? 0.7410 0.9918 0.7427 -0.0428 0.0030  -0.0620 351 LYS A CG  
2481 C CD  . LYS A 349 ? 0.7738 1.0325 0.7662 -0.0634 0.0072  -0.0647 351 LYS A CD  
2482 C CE  . LYS A 349 ? 0.7781 1.0341 0.7661 -0.0705 0.0086  -0.0636 351 LYS A CE  
2483 N NZ  . LYS A 349 ? 0.7970 1.0387 0.7712 -0.0904 0.0132  -0.0639 351 LYS A NZ  
2484 N N   . VAL A 350 ? 0.6968 0.9214 0.7104 -0.0002 -0.0052 -0.0583 352 VAL A N   
2485 C CA  . VAL A 350 ? 0.7638 0.9935 0.7790 0.0082  -0.0067 -0.0607 352 VAL A CA  
2486 C C   . VAL A 350 ? 0.8172 1.0848 0.8332 0.0053  -0.0061 -0.0668 352 VAL A C   
2487 O O   . VAL A 350 ? 0.8549 1.1278 0.8706 -0.0014 -0.0047 -0.0691 352 VAL A O   
2488 C CB  . VAL A 350 ? 0.7493 0.9672 0.7639 0.0266  -0.0101 -0.0591 352 VAL A CB  
2489 C CG1 . VAL A 350 ? 0.7580 0.9824 0.7723 0.0368  -0.0117 -0.0622 352 VAL A CG1 
2490 C CG2 . VAL A 350 ? 0.7202 0.9028 0.7335 0.0264  -0.0102 -0.0537 352 VAL A CG2 
2491 N N   . ASN A 351 ? 0.8580 1.1528 0.8747 0.0097  -0.0070 -0.0694 353 ASN A N   
2492 C CA  . ASN A 351 ? 0.8942 1.2313 0.9119 0.0080  -0.0067 -0.0759 353 ASN A CA  
2493 C C   . ASN A 351 ? 0.8890 1.2486 0.9058 -0.0014 -0.0051 -0.0776 353 ASN A C   
2494 O O   . ASN A 351 ? 0.8967 1.2852 0.9149 0.0089  -0.0070 -0.0806 353 ASN A O   
2495 C CB  . ASN A 351 ? 0.9414 1.2949 0.9601 0.0294  -0.0103 -0.0786 353 ASN A CB  
2496 C CG  . ASN A 351 ? 0.9704 1.3007 0.9886 0.0377  -0.0116 -0.0772 353 ASN A CG  
2497 O OD1 . ASN A 351 ? 1.0019 1.3116 1.0173 0.0534  -0.0141 -0.0747 353 ASN A OD1 
2498 N ND2 . ASN A 351 ? 0.9307 1.2627 0.9499 0.0266  -0.0096 -0.0790 353 ASN A ND2 
2499 N N   . ASN A 352 ? 0.9152 1.2603 0.9283 -0.0198 -0.0018 -0.0757 354 ASN A N   
2500 C CA  . ASN A 352 ? 0.9511 1.3067 0.9618 -0.0290 -0.0002 -0.0760 354 ASN A CA  
2501 C C   . ASN A 352 ? 0.9335 1.2845 0.9474 -0.0120 -0.0035 -0.0731 354 ASN A C   
2502 O O   . ASN A 352 ? 0.9083 1.2870 0.9229 -0.0100 -0.0040 -0.0757 354 ASN A O   
2503 C CB  . ASN A 352 ? 0.9890 1.3887 0.9982 -0.0405 0.0016  -0.0829 354 ASN A CB  
2504 C CG  . ASN A 352 ? 1.0269 1.4218 1.0289 -0.0619 0.0058  -0.0847 354 ASN A CG  
2505 O OD1 . ASN A 352 ? 1.0794 1.4744 1.0735 -0.0806 0.0094  -0.0856 354 ASN A OD1 
2506 N ND2 . ASN A 352 ? 1.0316 1.4188 1.0344 -0.0596 0.0056  -0.0849 354 ASN A ND2 
2507 N N   . GLN A 353 ? 0.9320 1.2491 0.9467 -0.0007 -0.0055 -0.0680 355 GLN A N   
2508 C CA  . GLN A 353 ? 0.9232 1.2300 0.9385 0.0170  -0.0088 -0.0649 355 GLN A CA  
2509 C C   . GLN A 353 ? 0.8377 1.1011 0.8518 0.0171  -0.0088 -0.0586 355 GLN A C   
2510 O O   . GLN A 353 ? 0.8894 1.1335 0.9032 0.0251  -0.0102 -0.0570 355 GLN A O   
2511 C CB  . GLN A 353 ? 0.9831 1.3032 0.9984 0.0365  -0.0120 -0.0674 355 GLN A CB  
2512 C CG  . GLN A 353 ? 1.0039 1.3137 1.0157 0.0554  -0.0152 -0.0646 355 GLN A CG  
2513 C CD  . GLN A 353 ? 1.0128 1.3533 1.0247 0.0582  -0.0157 -0.0669 355 GLN A CD  
2514 O OE1 . GLN A 353 ? 1.0046 1.3345 1.0158 0.0560  -0.0155 -0.0636 355 GLN A OE1 
2515 N NE2 . GLN A 353 ? 0.9816 1.3632 0.9946 0.0627  -0.0163 -0.0728 355 GLN A NE2 
2516 N N   . TYR A 354 ? 0.7169 0.9672 0.7300 0.0080  -0.0073 -0.0555 356 TYR A N   
2517 C CA  . TYR A 354 ? 0.6050 0.8190 0.6171 0.0077  -0.0073 -0.0497 356 TYR A CA  
2518 C C   . TYR A 354 ? 0.5710 0.7701 0.5822 0.0248  -0.0105 -0.0472 356 TYR A C   
2519 O O   . TYR A 354 ? 0.5772 0.7845 0.5869 0.0347  -0.0123 -0.0470 356 TYR A O   
2520 C CB  . TYR A 354 ? 0.5573 0.7679 0.5680 -0.0006 -0.0058 -0.0477 356 TYR A CB  
2521 C CG  . TYR A 354 ? 0.5392 0.7466 0.5463 -0.0186 -0.0021 -0.0485 356 TYR A CG  
2522 C CD1 . TYR A 354 ? 0.5261 0.7114 0.5307 -0.0245 -0.0007 -0.0468 356 TYR A CD1 
2523 C CD2 . TYR A 354 ? 0.5356 0.7601 0.5396 -0.0296 0.0000  -0.0508 356 TYR A CD2 
2524 C CE1 . TYR A 354 ? 0.5440 0.7214 0.5416 -0.0398 0.0027  -0.0471 356 TYR A CE1 
2525 C CE2 . TYR A 354 ? 0.5417 0.7577 0.5383 -0.0465 0.0036  -0.0514 356 TYR A CE2 
2526 C CZ  . TYR A 354 ? 0.5663 0.7572 0.5589 -0.0510 0.0049  -0.0493 356 TYR A CZ  
2527 O OH  . TYR A 354 ? 0.6291 0.8078 0.6109 -0.0662 0.0087  -0.0496 356 TYR A OH  
2528 N N   . THR A 355 ? 0.5402 0.7176 0.5506 0.0277  -0.0110 -0.0455 357 THR A N   
2529 C CA  . THR A 355 ? 0.5464 0.7044 0.5528 0.0416  -0.0135 -0.0433 357 THR A CA  
2530 C C   . THR A 355 ? 0.5243 0.6510 0.5298 0.0362  -0.0128 -0.0385 357 THR A C   
2531 O O   . THR A 355 ? 0.4809 0.5995 0.4889 0.0253  -0.0108 -0.0377 357 THR A O   
2532 C CB  . THR A 355 ? 0.5560 0.7179 0.5608 0.0499  -0.0147 -0.0463 357 THR A CB  
2533 O OG1 . THR A 355 ? 0.5868 0.7302 0.5840 0.0641  -0.0170 -0.0446 357 THR A OG1 
2534 C CG2 . THR A 355 ? 0.5502 0.6994 0.5573 0.0415  -0.0132 -0.0461 357 THR A CG2 
2535 N N   . GLU A 356 ? 0.5333 0.6436 0.5338 0.0440  -0.0143 -0.0355 358 GLU A N   
2536 C CA  . GLU A 356 ? 0.5106 0.5942 0.5093 0.0396  -0.0138 -0.0311 358 GLU A CA  
2537 C C   . GLU A 356 ? 0.4813 0.5482 0.4784 0.0392  -0.0138 -0.0310 358 GLU A C   
2538 O O   . GLU A 356 ? 0.4634 0.5255 0.4546 0.0488  -0.0153 -0.0324 358 GLU A O   
2539 C CB  . GLU A 356 ? 0.5302 0.6029 0.5221 0.0482  -0.0154 -0.0285 358 GLU A CB  
2540 C CG  . GLU A 356 ? 0.5388 0.5865 0.5279 0.0433  -0.0149 -0.0243 358 GLU A CG  
2541 C CD  . GLU A 356 ? 0.5690 0.6045 0.5498 0.0502  -0.0162 -0.0215 358 GLU A CD  
2542 O OE1 . GLU A 356 ? 0.5705 0.6202 0.5517 0.0544  -0.0168 -0.0216 358 GLU A OE1 
2543 O OE2 . GLU A 356 ? 0.5790 0.5909 0.5519 0.0508  -0.0164 -0.0193 358 GLU A OE2 
2544 N N   . ILE A 357 ? 0.4494 0.5075 0.4501 0.0289  -0.0121 -0.0295 359 ILE A N   
2545 C CA  . ILE A 357 ? 0.4266 0.4706 0.4263 0.0272  -0.0119 -0.0295 359 ILE A CA  
2546 C C   . ILE A 357 ? 0.4269 0.4510 0.4238 0.0237  -0.0116 -0.0260 359 ILE A C   
2547 O O   . ILE A 357 ? 0.4310 0.4418 0.4238 0.0243  -0.0119 -0.0260 359 ILE A O   
2548 C CB  . ILE A 357 ? 0.4025 0.4554 0.4075 0.0196  -0.0102 -0.0312 359 ILE A CB  
2549 C CG1 . ILE A 357 ? 0.3721 0.4237 0.3795 0.0100  -0.0082 -0.0292 359 ILE A CG1 
2550 C CG2 . ILE A 357 ? 0.4183 0.4926 0.4249 0.0223  -0.0104 -0.0351 359 ILE A CG2 
2551 C CD1 . ILE A 357 ? 0.3662 0.4240 0.3751 0.0030  -0.0064 -0.0309 359 ILE A CD1 
2552 N N   . LYS A 358 ? 0.4324 0.4551 0.4304 0.0199  -0.0111 -0.0234 360 LYS A N   
2553 C CA  . LYS A 358 ? 0.4172 0.4244 0.4129 0.0155  -0.0106 -0.0204 360 LYS A CA  
2554 C C   . LYS A 358 ? 0.3915 0.3992 0.3872 0.0144  -0.0106 -0.0178 360 LYS A C   
2555 O O   . LYS A 358 ? 0.3431 0.3624 0.3432 0.0115  -0.0097 -0.0180 360 LYS A O   
2556 C CB  . LYS A 358 ? 0.4184 0.4262 0.4187 0.0079  -0.0091 -0.0203 360 LYS A CB  
2557 C CG  . LYS A 358 ? 0.4307 0.4278 0.4294 0.0033  -0.0086 -0.0181 360 LYS A CG  
2558 C CD  . LYS A 358 ? 0.4700 0.4549 0.4628 0.0041  -0.0093 -0.0186 360 LYS A CD  
2559 C CE  . LYS A 358 ? 0.4975 0.4743 0.4875 -0.0018 -0.0087 -0.0167 360 LYS A CE  
2560 N NZ  . LYS A 358 ? 0.5487 0.5120 0.5302 -0.0029 -0.0089 -0.0176 360 LYS A NZ  
2561 N N   . LYS A 359 ? 0.4109 0.4049 0.4006 0.0153  -0.0112 -0.0156 361 LYS A N   
2562 C CA  . LYS A 359 ? 0.4248 0.4174 0.4138 0.0140  -0.0111 -0.0129 361 LYS A CA  
2563 C C   . LYS A 359 ? 0.4084 0.3889 0.3949 0.0077  -0.0105 -0.0106 361 LYS A C   
2564 O O   . LYS A 359 ? 0.4317 0.4001 0.4119 0.0071  -0.0106 -0.0109 361 LYS A O   
2565 C CB  . LYS A 359 ? 0.4854 0.4740 0.4669 0.0227  -0.0127 -0.0123 361 LYS A CB  
2566 C CG  . LYS A 359 ? 0.5194 0.5053 0.4990 0.0219  -0.0128 -0.0094 361 LYS A CG  
2567 C CD  . LYS A 359 ? 0.5854 0.5698 0.5571 0.0319  -0.0144 -0.0090 361 LYS A CD  
2568 C CE  . LYS A 359 ? 0.6401 0.6088 0.5994 0.0401  -0.0155 -0.0097 361 LYS A CE  
2569 N NZ  . LYS A 359 ? 0.6981 0.6606 0.6459 0.0512  -0.0171 -0.0086 361 LYS A NZ  
2570 N N   . PHE A 360 ? 0.3740 0.3590 0.3646 0.0029  -0.0096 -0.0089 362 PHE A N   
2571 C CA  . PHE A 360 ? 0.3653 0.3433 0.3536 -0.0027 -0.0090 -0.0067 362 PHE A CA  
2572 C C   . PHE A 360 ? 0.3701 0.3459 0.3556 -0.0017 -0.0094 -0.0043 362 PHE A C   
2573 O O   . PHE A 360 ? 0.3607 0.3459 0.3506 -0.0003 -0.0093 -0.0040 362 PHE A O   
2574 C CB  . PHE A 360 ? 0.3345 0.3209 0.3289 -0.0077 -0.0077 -0.0069 362 PHE A CB  
2575 C CG  . PHE A 360 ? 0.3229 0.3113 0.3193 -0.0090 -0.0072 -0.0089 362 PHE A CG  
2576 C CD1 . PHE A 360 ? 0.3267 0.3099 0.3200 -0.0126 -0.0071 -0.0094 362 PHE A CD1 
2577 C CD2 . PHE A 360 ? 0.3131 0.3088 0.3134 -0.0074 -0.0067 -0.0106 362 PHE A CD2 
2578 C CE1 . PHE A 360 ? 0.3302 0.3164 0.3254 -0.0135 -0.0067 -0.0115 362 PHE A CE1 
2579 C CE2 . PHE A 360 ? 0.3033 0.3006 0.3049 -0.0084 -0.0062 -0.0123 362 PHE A CE2 
2580 C CZ  . PHE A 360 ? 0.3071 0.3003 0.3068 -0.0108 -0.0063 -0.0128 362 PHE A CZ  
2581 N N   . GLU A 361 ? 0.4008 0.3638 0.3781 -0.0039 -0.0096 -0.0027 363 GLU A N   
2582 C CA  . GLU A 361 ? 0.4159 0.3739 0.3885 -0.0042 -0.0098 0.0000  363 GLU A CA  
2583 C C   . GLU A 361 ? 0.3797 0.3463 0.3583 -0.0110 -0.0087 0.0011  363 GLU A C   
2584 O O   . GLU A 361 ? 0.3748 0.3477 0.3580 -0.0150 -0.0079 0.0000  363 GLU A O   
2585 C CB  . GLU A 361 ? 0.4798 0.4178 0.4381 -0.0052 -0.0101 0.0011  363 GLU A CB  
2586 C CG  . GLU A 361 ? 0.5453 0.4741 0.4944 0.0025  -0.0113 0.0028  363 GLU A CG  
2587 C CD  . GLU A 361 ? 0.5782 0.5122 0.5280 0.0135  -0.0126 0.0010  363 GLU A CD  
2588 O OE1 . GLU A 361 ? 0.5852 0.5173 0.5342 0.0157  -0.0127 -0.0013 363 GLU A OE1 
2589 O OE2 . GLU A 361 ? 0.5988 0.5408 0.5501 0.0199  -0.0135 0.0017  363 GLU A OE2 
2590 N N   . ALA A 362 ? 0.3880 0.3551 0.3656 -0.0114 -0.0088 0.0033  364 ALA A N   
2591 C CA  . ALA A 362 ? 0.3695 0.3459 0.3522 -0.0162 -0.0079 0.0043  364 ALA A CA  
2592 C C   . ALA A 362 ? 0.3872 0.3580 0.3638 -0.0234 -0.0074 0.0055  364 ALA A C   
2593 O O   . ALA A 362 ? 0.4135 0.3700 0.3800 -0.0244 -0.0077 0.0065  364 ALA A O   
2594 C CB  . ALA A 362 ? 0.3756 0.3570 0.3606 -0.0128 -0.0082 0.0056  364 ALA A CB  
2595 N N   A ASP A 363 ? 0.3740 0.3558 0.3548 -0.0282 -0.0065 0.0055  365 ASP A N   
2596 N N   B ASP A 363 ? 0.3899 0.3719 0.3712 -0.0280 -0.0064 0.0051  365 ASP A N   
2597 C CA  A ASP A 363 ? 0.3777 0.3618 0.3546 -0.0368 -0.0056 0.0057  365 ASP A CA  
2598 C CA  B ASP A 363 ? 0.3975 0.3822 0.3752 -0.0365 -0.0056 0.0050  365 ASP A CA  
2599 C C   A ASP A 363 ? 0.3513 0.3541 0.3364 -0.0367 -0.0049 0.0046  365 ASP A C   
2600 C C   B ASP A 363 ? 0.3614 0.3642 0.3467 -0.0364 -0.0049 0.0044  365 ASP A C   
2601 O O   A ASP A 363 ? 0.3281 0.3360 0.3180 -0.0312 -0.0051 0.0051  365 ASP A O   
2602 O O   B ASP A 363 ? 0.3380 0.3455 0.3278 -0.0311 -0.0051 0.0051  365 ASP A O   
2603 C CB  A ASP A 363 ? 0.4099 0.3840 0.3788 -0.0425 -0.0052 0.0042  365 ASP A CB  
2604 C CB  B ASP A 363 ? 0.4290 0.4071 0.4012 -0.0414 -0.0051 0.0031  365 ASP A CB  
2605 C CG  A ASP A 363 ? 0.4330 0.3869 0.3871 -0.0474 -0.0050 0.0055  365 ASP A CG  
2606 C CG  B ASP A 363 ? 0.4246 0.4074 0.4022 -0.0380 -0.0052 0.0006  365 ASP A CG  
2607 O OD1 A ASP A 363 ? 0.4357 0.3896 0.3834 -0.0569 -0.0040 0.0060  365 ASP A OD1 
2608 O OD1 B ASP A 363 ? 0.3739 0.3651 0.3524 -0.0429 -0.0045 -0.0013 365 ASP A OD1 
2609 O OD2 A ASP A 363 ? 0.4414 0.3791 0.3885 -0.0422 -0.0058 0.0056  365 ASP A OD2 
2610 O OD2 B ASP A 363 ? 0.4384 0.4167 0.4183 -0.0309 -0.0060 0.0003  365 ASP A OD2 
2611 N N   . SER A 364 ? 0.3446 0.3577 0.3302 -0.0414 -0.0042 0.0029  366 SER A N   
2612 C CA  . SER A 364 ? 0.3264 0.3582 0.3170 -0.0398 -0.0037 0.0022  366 SER A CA  
2613 C C   . SER A 364 ? 0.3197 0.3569 0.3146 -0.0330 -0.0037 0.0004  366 SER A C   
2614 O O   . SER A 364 ? 0.2911 0.3402 0.2879 -0.0281 -0.0033 0.0000  366 SER A O   
2615 C CB  . SER A 364 ? 0.3267 0.3719 0.3150 -0.0479 -0.0030 0.0011  366 SER A CB  
2616 O OG  . SER A 364 ? 0.3118 0.3557 0.2968 -0.0542 -0.0025 -0.0008 366 SER A OG  
2617 N N   . ASN A 365 ? 0.3157 0.3430 0.3104 -0.0320 -0.0040 -0.0004 367 ASN A N   
2618 C CA  . ASN A 365 ? 0.3278 0.3581 0.3252 -0.0268 -0.0038 -0.0021 367 ASN A CA  
2619 C C   . ASN A 365 ? 0.2814 0.3085 0.2799 -0.0201 -0.0037 -0.0013 367 ASN A C   
2620 O O   . ASN A 365 ? 0.2912 0.3115 0.2895 -0.0197 -0.0040 0.0000  367 ASN A O   
2621 C CB  . ASN A 365 ? 0.3495 0.3720 0.3461 -0.0286 -0.0041 -0.0036 367 ASN A CB  
2622 C CG  . ASN A 365 ? 0.3890 0.4204 0.3876 -0.0264 -0.0037 -0.0057 367 ASN A CG  
2623 O OD1 . ASN A 365 ? 0.3848 0.4301 0.3835 -0.0286 -0.0032 -0.0069 367 ASN A OD1 
2624 N ND2 . ASN A 365 ? 0.3722 0.3973 0.3720 -0.0219 -0.0038 -0.0063 367 ASN A ND2 
2625 N N   . SER A 366 ? 0.2558 0.2884 0.2537 -0.0152 -0.0031 -0.0023 368 SER A N   
2626 C CA  . SER A 366 ? 0.2422 0.2696 0.2373 -0.0098 -0.0024 -0.0020 368 SER A CA  
2627 C C   . SER A 366 ? 0.2379 0.2609 0.2314 -0.0072 -0.0020 -0.0036 368 SER A C   
2628 O O   . SER A 366 ? 0.2343 0.2500 0.2231 -0.0045 -0.0011 -0.0036 368 SER A O   
2629 C CB  . SER A 366 ? 0.2447 0.2790 0.2362 -0.0056 -0.0019 -0.0015 368 SER A CB  
2630 O OG  . SER A 366 ? 0.2422 0.2773 0.2346 -0.0079 -0.0022 0.0000  368 SER A OG  
2631 N N   . THR A 367 ? 0.2224 0.2486 0.2184 -0.0089 -0.0024 -0.0049 369 THR A N   
2632 C CA  . THR A 367 ? 0.2160 0.2391 0.2108 -0.0067 -0.0020 -0.0064 369 THR A CA  
2633 C C   . THR A 367 ? 0.2142 0.2321 0.2127 -0.0102 -0.0027 -0.0073 369 THR A C   
2634 O O   . THR A 367 ? 0.2239 0.2434 0.2245 -0.0140 -0.0034 -0.0075 369 THR A O   
2635 C CB  . THR A 367 ? 0.2139 0.2470 0.2078 -0.0042 -0.0018 -0.0076 369 THR A CB  
2636 O OG1 . THR A 367 ? 0.2128 0.2509 0.2017 0.0011  -0.0013 -0.0069 369 THR A OG1 
2637 C CG2 . THR A 367 ? 0.2113 0.2409 0.2033 -0.0017 -0.0014 -0.0090 369 THR A CG2 
2638 N N   . PHE A 368 ? 0.2094 0.2211 0.2071 -0.0092 -0.0024 -0.0079 370 PHE A N   
2639 C CA  . PHE A 368 ? 0.2136 0.2220 0.2140 -0.0107 -0.0031 -0.0090 370 PHE A CA  
2640 C C   . PHE A 368 ? 0.2188 0.2275 0.2187 -0.0096 -0.0027 -0.0109 370 PHE A C   
2641 O O   . PHE A 368 ? 0.2221 0.2286 0.2186 -0.0085 -0.0016 -0.0113 370 PHE A O   
2642 C CB  . PHE A 368 ? 0.2120 0.2177 0.2124 -0.0107 -0.0033 -0.0084 370 PHE A CB  
2643 C CG  . PHE A 368 ? 0.2137 0.2193 0.2142 -0.0115 -0.0038 -0.0064 370 PHE A CG  
2644 C CD1 . PHE A 368 ? 0.2131 0.2200 0.2113 -0.0111 -0.0029 -0.0052 370 PHE A CD1 
2645 C CD2 . PHE A 368 ? 0.2203 0.2229 0.2213 -0.0123 -0.0049 -0.0057 370 PHE A CD2 
2646 C CE1 . PHE A 368 ? 0.2213 0.2291 0.2198 -0.0120 -0.0033 -0.0034 370 PHE A CE1 
2647 C CE2 . PHE A 368 ? 0.2269 0.2288 0.2270 -0.0134 -0.0052 -0.0037 370 PHE A CE2 
2648 C CZ  . PHE A 368 ? 0.2230 0.2287 0.2228 -0.0135 -0.0044 -0.0026 370 PHE A CZ  
2649 N N   . ASP A 369 ? 0.2229 0.2333 0.2248 -0.0106 -0.0033 -0.0121 371 ASP A N   
2650 C CA  . ASP A 369 ? 0.2266 0.2384 0.2284 -0.0095 -0.0029 -0.0140 371 ASP A CA  
2651 C C   . ASP A 369 ? 0.2213 0.2297 0.2248 -0.0098 -0.0036 -0.0155 371 ASP A C   
2652 O O   . ASP A 369 ? 0.2329 0.2388 0.2371 -0.0110 -0.0045 -0.0159 371 ASP A O   
2653 C CB  . ASP A 369 ? 0.2333 0.2514 0.2358 -0.0105 -0.0030 -0.0148 371 ASP A CB  
2654 C CG  . ASP A 369 ? 0.2509 0.2761 0.2507 -0.0077 -0.0023 -0.0140 371 ASP A CG  
2655 O OD1 . ASP A 369 ? 0.2529 0.2757 0.2480 -0.0033 -0.0014 -0.0137 371 ASP A OD1 
2656 O OD2 . ASP A 369 ? 0.2742 0.3073 0.2750 -0.0098 -0.0026 -0.0137 371 ASP A OD2 
2657 N N   . PHE A 370 ? 0.2113 0.2195 0.2141 -0.0089 -0.0030 -0.0163 372 PHE A N   
2658 C CA  . PHE A 370 ? 0.2154 0.2244 0.2199 -0.0082 -0.0037 -0.0182 372 PHE A CA  
2659 C C   . PHE A 370 ? 0.2213 0.2318 0.2260 -0.0080 -0.0034 -0.0201 372 PHE A C   
2660 O O   . PHE A 370 ? 0.2165 0.2279 0.2187 -0.0086 -0.0022 -0.0205 372 PHE A O   
2661 C CB  . PHE A 370 ? 0.2129 0.2249 0.2164 -0.0086 -0.0032 -0.0186 372 PHE A CB  
2662 C CG  . PHE A 370 ? 0.2100 0.2218 0.2137 -0.0083 -0.0037 -0.0170 372 PHE A CG  
2663 C CD1 . PHE A 370 ? 0.2056 0.2154 0.2068 -0.0100 -0.0027 -0.0151 372 PHE A CD1 
2664 C CD2 . PHE A 370 ? 0.2142 0.2271 0.2191 -0.0054 -0.0051 -0.0173 372 PHE A CD2 
2665 C CE1 . PHE A 370 ? 0.2108 0.2211 0.2124 -0.0099 -0.0031 -0.0137 372 PHE A CE1 
2666 C CE2 . PHE A 370 ? 0.2155 0.2287 0.2200 -0.0047 -0.0056 -0.0158 372 PHE A CE2 
2667 C CZ  . PHE A 370 ? 0.2125 0.2248 0.2161 -0.0074 -0.0046 -0.0139 372 PHE A CZ  
2668 N N   . LYS A 371 ? 0.2352 0.2444 0.2412 -0.0079 -0.0043 -0.0211 373 LYS A N   
2669 C CA  . LYS A 371 ? 0.2558 0.2670 0.2622 -0.0080 -0.0040 -0.0229 373 LYS A CA  
2670 C C   . LYS A 371 ? 0.2444 0.2569 0.2518 -0.0063 -0.0045 -0.0252 373 LYS A C   
2671 O O   . LYS A 371 ? 0.2369 0.2471 0.2440 -0.0043 -0.0055 -0.0258 373 LYS A O   
2672 C CB  . LYS A 371 ? 0.2891 0.2993 0.2954 -0.0100 -0.0045 -0.0233 373 LYS A CB  
2673 C CG  . LYS A 371 ? 0.3274 0.3423 0.3333 -0.0114 -0.0038 -0.0218 373 LYS A CG  
2674 C CD  . LYS A 371 ? 0.3841 0.4036 0.3897 -0.0147 -0.0039 -0.0230 373 LYS A CD  
2675 C CE  . LYS A 371 ? 0.4310 0.4582 0.4362 -0.0163 -0.0035 -0.0217 373 LYS A CE  
2676 N NZ  . LYS A 371 ? 0.4671 0.5029 0.4719 -0.0208 -0.0033 -0.0235 373 LYS A NZ  
2677 N N   . GLY A 372 ? 0.2454 0.2615 0.2526 -0.0065 -0.0037 -0.0266 374 GLY A N   
2678 C CA  . GLY A 372 ? 0.2481 0.2675 0.2566 -0.0050 -0.0042 -0.0293 374 GLY A CA  
2679 C C   . GLY A 372 ? 0.2470 0.2726 0.2553 -0.0050 -0.0039 -0.0303 374 GLY A C   
2680 O O   . GLY A 372 ? 0.2434 0.2733 0.2529 -0.0018 -0.0049 -0.0322 374 GLY A O   
2681 N N   . LEU A 373 ? 0.2489 0.2750 0.2542 -0.0083 -0.0023 -0.0292 375 LEU A N   
2682 C CA  . LEU A 373 ? 0.2609 0.2942 0.2644 -0.0110 -0.0013 -0.0306 375 LEU A CA  
2683 C C   . LEU A 373 ? 0.2735 0.3095 0.2737 -0.0143 0.0000  -0.0324 375 LEU A C   
2684 O O   . LEU A 373 ? 0.2751 0.3041 0.2721 -0.0146 0.0008  -0.0314 375 LEU A O   
2685 C CB  . LEU A 373 ? 0.2547 0.2841 0.2538 -0.0144 0.0000  -0.0285 375 LEU A CB  
2686 C CG  . LEU A 373 ? 0.2481 0.2737 0.2495 -0.0119 -0.0012 -0.0262 375 LEU A CG  
2687 C CD1 . LEU A 373 ? 0.2406 0.2646 0.2374 -0.0154 0.0001  -0.0249 375 LEU A CD1 
2688 C CD2 . LEU A 373 ? 0.2558 0.2863 0.2618 -0.0075 -0.0032 -0.0272 375 LEU A CD2 
2689 N N   . ASP A 374 ? 0.2956 0.3425 0.2957 -0.0167 0.0004  -0.0349 376 ASP A N   
2690 C CA  . ASP A 374 ? 0.3260 0.3768 0.3214 -0.0218 0.0021  -0.0369 376 ASP A CA  
2691 C C   . ASP A 374 ? 0.3358 0.3887 0.3232 -0.0301 0.0045  -0.0374 376 ASP A C   
2692 O O   . ASP A 374 ? 0.3388 0.3909 0.3254 -0.0313 0.0046  -0.0362 376 ASP A O   
2693 C CB  . ASP A 374 ? 0.3375 0.4009 0.3386 -0.0185 0.0008  -0.0403 376 ASP A CB  
2694 C CG  . ASP A 374 ? 0.3607 0.4401 0.3656 -0.0162 -0.0003 -0.0427 376 ASP A CG  
2695 O OD1 . ASP A 374 ? 0.3653 0.4455 0.3697 -0.0168 -0.0003 -0.0416 376 ASP A OD1 
2696 O OD2 . ASP A 374 ? 0.4161 0.5081 0.4239 -0.0131 -0.0012 -0.0459 376 ASP A OD2 
2697 N N   . SER A 375 ? 0.3558 0.4108 0.3364 -0.0367 0.0065  -0.0392 377 SER A N   
2698 C CA  . SER A 375 ? 0.3663 0.4240 0.3368 -0.0473 0.0093  -0.0406 377 SER A CA  
2699 C C   . SER A 375 ? 0.3883 0.4672 0.3660 -0.0476 0.0082  -0.0432 377 SER A C   
2700 O O   . SER A 375 ? 0.4058 0.4989 0.3935 -0.0405 0.0058  -0.0451 377 SER A O   
2701 C CB  . SER A 375 ? 0.3630 0.4205 0.3249 -0.0544 0.0115  -0.0424 377 SER A CB  
2702 O OG  . SER A 375 ? 0.3462 0.3838 0.3007 -0.0520 0.0122  -0.0397 377 SER A OG  
2703 N N   . GLY A 376 ? 0.3977 0.4777 0.3693 -0.0545 0.0098  -0.0432 378 GLY A N   
2704 C CA  . GLY A 376 ? 0.4161 0.5189 0.3932 -0.0553 0.0090  -0.0460 378 GLY A CA  
2705 C C   . GLY A 376 ? 0.4243 0.5223 0.3965 -0.0598 0.0101  -0.0446 378 GLY A C   
2706 O O   . GLY A 376 ? 0.4073 0.4828 0.3706 -0.0625 0.0117  -0.0414 378 GLY A O   
2707 N N   . ASP A 377 ? 0.4409 0.5604 0.4188 -0.0590 0.0091  -0.0468 379 ASP A N   
2708 C CA  . ASP A 377 ? 0.4400 0.5611 0.4147 -0.0634 0.0100  -0.0463 379 ASP A CA  
2709 C C   . ASP A 377 ? 0.4133 0.5331 0.3982 -0.0506 0.0067  -0.0436 379 ASP A C   
2710 O O   . ASP A 377 ? 0.4001 0.5351 0.3940 -0.0407 0.0040  -0.0451 379 ASP A O   
2711 C CB  . ASP A 377 ? 0.4780 0.6278 0.4514 -0.0718 0.0112  -0.0511 379 ASP A CB  
2712 C CG  . ASP A 377 ? 0.5149 0.6650 0.4754 -0.0875 0.0150  -0.0539 379 ASP A CG  
2713 O OD1 . ASP A 377 ? 0.5009 0.6233 0.4502 -0.0922 0.0171  -0.0513 379 ASP A OD1 
2714 O OD2 . ASP A 377 ? 0.5566 0.7348 0.5172 -0.0945 0.0159  -0.0587 379 ASP A OD2 
2715 N N   . TYR A 378 ? 0.3883 0.4899 0.3696 -0.0510 0.0072  -0.0401 380 TYR A N   
2716 C CA  . TYR A 378 ? 0.3687 0.4643 0.3574 -0.0406 0.0046  -0.0370 380 TYR A CA  
2717 C C   . TYR A 378 ? 0.3732 0.4706 0.3590 -0.0444 0.0053  -0.0362 380 TYR A C   
2718 O O   . TYR A 378 ? 0.3773 0.4702 0.3529 -0.0555 0.0083  -0.0369 380 TYR A O   
2719 C CB  . TYR A 378 ? 0.3533 0.4257 0.3412 -0.0364 0.0042  -0.0333 380 TYR A CB  
2720 C CG  . TYR A 378 ? 0.3513 0.4221 0.3431 -0.0315 0.0031  -0.0338 380 TYR A CG  
2721 C CD1 . TYR A 378 ? 0.3454 0.4183 0.3451 -0.0217 0.0003  -0.0334 380 TYR A CD1 
2722 C CD2 . TYR A 378 ? 0.3504 0.4158 0.3361 -0.0369 0.0050  -0.0348 380 TYR A CD2 
2723 C CE1 . TYR A 378 ? 0.3367 0.4073 0.3390 -0.0177 -0.0006 -0.0342 380 TYR A CE1 
2724 C CE2 . TYR A 378 ? 0.3423 0.4073 0.3319 -0.0325 0.0039  -0.0355 380 TYR A CE2 
2725 C CZ  . TYR A 378 ? 0.3361 0.4042 0.3344 -0.0230 0.0011  -0.0353 380 TYR A CZ  
2726 O OH  . TYR A 378 ? 0.3462 0.4127 0.3474 -0.0191 0.0002  -0.0361 380 TYR A OH  
2727 N N   . LYS A 379 ? 0.3723 0.4732 0.3652 -0.0355 0.0028  -0.0346 381 LYS A N   
2728 C CA  . LYS A 379 ? 0.3657 0.4653 0.3571 -0.0371 0.0031  -0.0330 381 LYS A CA  
2729 C C   . LYS A 379 ? 0.3329 0.4160 0.3279 -0.0289 0.0012  -0.0288 381 LYS A C   
2730 O O   . LYS A 379 ? 0.3178 0.4026 0.3186 -0.0195 -0.0012 -0.0282 381 LYS A O   
2731 C CB  . LYS A 379 ? 0.3987 0.5238 0.3939 -0.0352 0.0021  -0.0358 381 LYS A CB  
2732 C CG  . LYS A 379 ? 0.4186 0.5454 0.4120 -0.0380 0.0025  -0.0347 381 LYS A CG  
2733 C CD  . LYS A 379 ? 0.4481 0.6033 0.4449 -0.0358 0.0015  -0.0377 381 LYS A CD  
2734 C CE  . LYS A 379 ? 0.4559 0.6216 0.4596 -0.0206 -0.0019 -0.0378 381 LYS A CE  
2735 N NZ  . LYS A 379 ? 0.4717 0.6666 0.4773 -0.0167 -0.0030 -0.0409 381 LYS A NZ  
2736 N N   . LEU A 380 ? 0.3118 0.3793 0.3017 -0.0326 0.0026  -0.0262 382 LEU A N   
2737 C CA  . LEU A 380 ? 0.2958 0.3505 0.2884 -0.0267 0.0012  -0.0224 382 LEU A CA  
2738 C C   . LEU A 380 ? 0.2890 0.3499 0.2824 -0.0265 0.0008  -0.0216 382 LEU A C   
2739 O O   . LEU A 380 ? 0.2785 0.3402 0.2658 -0.0340 0.0029  -0.0224 382 LEU A O   
2740 C CB  . LEU A 380 ? 0.2924 0.3288 0.2784 -0.0293 0.0028  -0.0203 382 LEU A CB  
2741 C CG  . LEU A 380 ? 0.2793 0.3056 0.2682 -0.0238 0.0015  -0.0168 382 LEU A CG  
2742 C CD1 . LEU A 380 ? 0.2706 0.2970 0.2662 -0.0177 -0.0005 -0.0164 382 LEU A CD1 
2743 C CD2 . LEU A 380 ? 0.2752 0.2873 0.2562 -0.0253 0.0032  -0.0152 382 LEU A CD2 
2744 N N   . VAL A 381 ? 0.2871 0.3508 0.2862 -0.0185 -0.0016 -0.0202 383 VAL A N   
2745 C CA  . VAL A 381 ? 0.2988 0.3684 0.2989 -0.0165 -0.0024 -0.0190 383 VAL A CA  
2746 C C   . VAL A 381 ? 0.2991 0.3535 0.2998 -0.0131 -0.0033 -0.0151 383 VAL A C   
2747 O O   . VAL A 381 ? 0.3165 0.3626 0.3188 -0.0083 -0.0047 -0.0140 383 VAL A O   
2748 C CB  . VAL A 381 ? 0.3059 0.3911 0.3093 -0.0087 -0.0046 -0.0206 383 VAL A CB  
2749 C CG1 . VAL A 381 ? 0.3091 0.3977 0.3128 -0.0046 -0.0058 -0.0188 383 VAL A CG1 
2750 C CG2 . VAL A 381 ? 0.3137 0.4193 0.3169 -0.0127 -0.0036 -0.0251 383 VAL A CG2 
2751 N N   . GLU A 382 ? 0.3046 0.3555 0.3031 -0.0162 -0.0025 -0.0135 384 GLU A N   
2752 C CA  . GLU A 382 ? 0.2896 0.3293 0.2887 -0.0135 -0.0033 -0.0100 384 GLU A CA  
2753 C C   . GLU A 382 ? 0.2822 0.3270 0.2834 -0.0073 -0.0054 -0.0089 384 GLU A C   
2754 O O   . GLU A 382 ? 0.2601 0.3100 0.2610 -0.0077 -0.0054 -0.0082 384 GLU A O   
2755 C CB  . GLU A 382 ? 0.3095 0.3432 0.3043 -0.0186 -0.0015 -0.0089 384 GLU A CB  
2756 C CG  . GLU A 382 ? 0.3264 0.3514 0.3220 -0.0161 -0.0022 -0.0057 384 GLU A CG  
2757 C CD  . GLU A 382 ? 0.3482 0.3700 0.3398 -0.0190 -0.0009 -0.0045 384 GLU A CD  
2758 O OE1 . GLU A 382 ? 0.3793 0.4072 0.3691 -0.0219 -0.0002 -0.0055 384 GLU A OE1 
2759 O OE2 . GLU A 382 ? 0.3683 0.3829 0.3583 -0.0181 -0.0007 -0.0028 384 GLU A OE2 
2760 N N   . SER A 383 ? 0.2879 0.3295 0.2896 -0.0013 -0.0071 -0.0087 385 SER A N   
2761 C CA  . SER A 383 ? 0.3022 0.3454 0.3022 0.0066  -0.0092 -0.0079 385 SER A CA  
2762 C C   . SER A 383 ? 0.3126 0.3445 0.3101 0.0071  -0.0097 -0.0043 385 SER A C   
2763 O O   . SER A 383 ? 0.3304 0.3613 0.3241 0.0134  -0.0112 -0.0030 385 SER A O   
2764 C CB  . SER A 383 ? 0.3113 0.3499 0.3092 0.0126  -0.0105 -0.0089 385 SER A CB  
2765 O OG  . SER A 383 ? 0.2992 0.3263 0.2976 0.0086  -0.0097 -0.0084 385 SER A OG  
2766 N N   . THR A 384 ? 0.3059 0.3301 0.3042 0.0013  -0.0086 -0.0026 386 THR A N   
2767 C CA  . THR A 384 ? 0.3225 0.3400 0.3189 0.0005  -0.0088 0.0004  386 THR A CA  
2768 C C   . THR A 384 ? 0.3037 0.3231 0.3021 -0.0053 -0.0072 0.0008  386 THR A C   
2769 O O   . THR A 384 ? 0.2664 0.2832 0.2655 -0.0084 -0.0061 0.0001  386 THR A O   
2770 C CB  . THR A 384 ? 0.3500 0.3535 0.3424 0.0006  -0.0094 0.0023  386 THR A CB  
2771 O OG1 . THR A 384 ? 0.3980 0.3958 0.3855 0.0065  -0.0107 0.0017  386 THR A OG1 
2772 C CG2 . THR A 384 ? 0.3577 0.3560 0.3471 -0.0009 -0.0096 0.0053  386 THR A CG2 
2773 N N   . VAL A 385 ? 0.2885 0.3118 0.2866 -0.0059 -0.0071 0.0020  387 VAL A N   
2774 C CA  . VAL A 385 ? 0.2860 0.3105 0.2839 -0.0106 -0.0054 0.0020  387 VAL A CA  
2775 C C   . VAL A 385 ? 0.2762 0.2950 0.2734 -0.0113 -0.0056 0.0048  387 VAL A C   
2776 O O   . VAL A 385 ? 0.2796 0.2970 0.2760 -0.0095 -0.0067 0.0068  387 VAL A O   
2777 C CB  . VAL A 385 ? 0.2996 0.3341 0.2970 -0.0123 -0.0047 0.0006  387 VAL A CB  
2778 C CG1 . VAL A 385 ? 0.3095 0.3414 0.3035 -0.0174 -0.0027 0.0004  387 VAL A CG1 
2779 C CG2 . VAL A 385 ? 0.2945 0.3385 0.2925 -0.0125 -0.0045 -0.0025 387 VAL A CG2 
2780 N N   . PRO A 386 ? 0.2609 0.2767 0.2574 -0.0135 -0.0045 0.0050  388 PRO A N   
2781 C CA  . PRO A 386 ? 0.2516 0.2662 0.2475 -0.0144 -0.0046 0.0072  388 PRO A CA  
2782 C C   . PRO A 386 ? 0.2503 0.2682 0.2456 -0.0148 -0.0046 0.0083  388 PRO A C   
2783 O O   . PRO A 386 ? 0.2443 0.2648 0.2382 -0.0156 -0.0036 0.0070  388 PRO A O   
2784 C CB  . PRO A 386 ? 0.2460 0.2602 0.2404 -0.0148 -0.0034 0.0064  388 PRO A CB  
2785 C CG  . PRO A 386 ? 0.2472 0.2594 0.2415 -0.0143 -0.0030 0.0043  388 PRO A CG  
2786 C CD  . PRO A 386 ? 0.2488 0.2629 0.2436 -0.0145 -0.0032 0.0031  388 PRO A CD  
2787 N N   . SER A 387 ? 0.2547 0.2717 0.2498 -0.0150 -0.0055 0.0107  389 SER A N   
2788 C CA  . SER A 387 ? 0.2678 0.2878 0.2622 -0.0151 -0.0056 0.0122  389 SER A CA  
2789 C C   . SER A 387 ? 0.2634 0.2865 0.2567 -0.0164 -0.0041 0.0113  389 SER A C   
2790 O O   . SER A 387 ? 0.2734 0.2957 0.2655 -0.0166 -0.0034 0.0110  389 SER A O   
2791 C CB  . SER A 387 ? 0.2792 0.2957 0.2719 -0.0163 -0.0065 0.0148  389 SER A CB  
2792 O OG  . SER A 387 ? 0.3131 0.3329 0.3052 -0.0169 -0.0065 0.0164  389 SER A OG  
2793 N N   . GLY A 388 ? 0.2639 0.2902 0.2561 -0.0171 -0.0035 0.0104  390 GLY A N   
2794 C CA  . GLY A 388 ? 0.2613 0.2873 0.2493 -0.0186 -0.0019 0.0095  390 GLY A CA  
2795 C C   . GLY A 388 ? 0.2585 0.2793 0.2411 -0.0199 -0.0001 0.0069  390 GLY A C   
2796 O O   . GLY A 388 ? 0.2669 0.2829 0.2424 -0.0206 0.0014  0.0061  390 GLY A O   
2797 N N   . TYR A 389 ? 0.2564 0.2767 0.2405 -0.0201 -0.0003 0.0056  391 TYR A N   
2798 C CA  . TYR A 389 ? 0.2528 0.2675 0.2307 -0.0223 0.0014  0.0030  391 TYR A CA  
2799 C C   . TYR A 389 ? 0.2569 0.2787 0.2360 -0.0257 0.0016  0.0009  391 TYR A C   
2800 O O   . TYR A 389 ? 0.2411 0.2712 0.2269 -0.0236 -0.0001 0.0015  391 TYR A O   
2801 C CB  . TYR A 389 ? 0.2512 0.2613 0.2296 -0.0194 0.0012  0.0031  391 TYR A CB  
2802 C CG  . TYR A 389 ? 0.2472 0.2544 0.2232 -0.0160 0.0012  0.0044  391 TYR A CG  
2803 C CD1 . TYR A 389 ? 0.2420 0.2551 0.2240 -0.0144 -0.0002 0.0064  391 TYR A CD1 
2804 C CD2 . TYR A 389 ? 0.2655 0.2643 0.2312 -0.0142 0.0030  0.0035  391 TYR A CD2 
2805 C CE1 . TYR A 389 ? 0.2514 0.2663 0.2313 -0.0115 -0.0001 0.0072  391 TYR A CE1 
2806 C CE2 . TYR A 389 ? 0.2778 0.2767 0.2404 -0.0092 0.0029  0.0044  391 TYR A CE2 
2807 C CZ  . TYR A 389 ? 0.2693 0.2785 0.2401 -0.0081 0.0013  0.0061  391 TYR A CZ  
2808 O OH  . TYR A 389 ? 0.2861 0.2993 0.2538 -0.0032 0.0013  0.0064  391 TYR A OH  
2809 N N   . ASN A 390 ? 0.2846 0.3026 0.2554 -0.0308 0.0038  -0.0015 392 ASN A N   
2810 C CA  . ASN A 390 ? 0.3022 0.3291 0.2725 -0.0360 0.0046  -0.0045 392 ASN A CA  
2811 C C   . ASN A 390 ? 0.3106 0.3391 0.2850 -0.0339 0.0037  -0.0053 392 ASN A C   
2812 O O   . ASN A 390 ? 0.3084 0.3260 0.2797 -0.0322 0.0042  -0.0048 392 ASN A O   
2813 C CB  . ASN A 390 ? 0.3270 0.3466 0.2839 -0.0443 0.0078  -0.0072 392 ASN A CB  
2814 C CG  . ASN A 390 ? 0.3418 0.3598 0.2938 -0.0466 0.0087  -0.0068 392 ASN A CG  
2815 O OD1 . ASN A 390 ? 0.3725 0.3752 0.3132 -0.0472 0.0104  -0.0065 392 ASN A OD1 
2816 N ND2 . ASN A 390 ? 0.3154 0.3487 0.2755 -0.0460 0.0072  -0.0064 392 ASN A ND2 
2817 N N   . ALA A 391 ? 0.3222 0.3646 0.3028 -0.0332 0.0025  -0.0066 393 ALA A N   
2818 C CA  . ALA A 391 ? 0.3256 0.3718 0.3088 -0.0322 0.0020  -0.0083 393 ALA A CA  
2819 C C   . ALA A 391 ? 0.3397 0.3783 0.3136 -0.0393 0.0048  -0.0107 393 ALA A C   
2820 O O   . ALA A 391 ? 0.3461 0.3853 0.3115 -0.0474 0.0072  -0.0129 393 ALA A O   
2821 C CB  . ALA A 391 ? 0.3260 0.3909 0.3146 -0.0301 0.0006  -0.0100 393 ALA A CB  
2822 N N   . MET A 392 ? 0.3407 0.3701 0.3142 -0.0369 0.0047  -0.0103 394 MET A N   
2823 C CA  . MET A 392 ? 0.3636 0.3881 0.3295 -0.0422 0.0068  -0.0128 394 MET A CA  
2824 C C   . MET A 392 ? 0.3820 0.4244 0.3499 -0.0473 0.0071  -0.0162 394 MET A C   
2825 O O   . MET A 392 ? 0.3794 0.4365 0.3575 -0.0417 0.0046  -0.0162 394 MET A O   
2826 C CB  . MET A 392 ? 0.3625 0.3823 0.3331 -0.0364 0.0055  -0.0118 394 MET A CB  
2827 C CG  . MET A 392 ? 0.3740 0.3884 0.3371 -0.0409 0.0073  -0.0140 394 MET A CG  
2828 S SD  . MET A 392 ? 0.3708 0.3821 0.3403 -0.0342 0.0057  -0.0131 394 MET A SD  
2829 C CE  . MET A 392 ? 0.3410 0.3717 0.3212 -0.0327 0.0037  -0.0153 394 MET A CE  
2830 N N   . LYS A 393 ? 0.4232 0.4644 0.3804 -0.0572 0.0100  -0.0192 395 LYS A N   
2831 C CA  . LYS A 393 ? 0.4607 0.5229 0.4200 -0.0628 0.0103  -0.0231 395 LYS A CA  
2832 C C   . LYS A 393 ? 0.4358 0.4979 0.3986 -0.0596 0.0096  -0.0237 395 LYS A C   
2833 O O   . LYS A 393 ? 0.4381 0.4816 0.3946 -0.0595 0.0106  -0.0224 395 LYS A O   
2834 C CB  . LYS A 393 ? 0.5259 0.5859 0.4702 -0.0771 0.0142  -0.0265 395 LYS A CB  
2835 C CG  . LYS A 393 ? 0.5847 0.6587 0.5271 -0.0837 0.0151  -0.0284 395 LYS A CG  
2836 C CD  . LYS A 393 ? 0.6669 0.7242 0.5898 -0.0969 0.0193  -0.0300 395 LYS A CD  
2837 C CE  . LYS A 393 ? 0.7115 0.7875 0.6306 -0.1079 0.0210  -0.0337 395 LYS A CE  
2838 N NZ  . LYS A 393 ? 0.7779 0.8423 0.6754 -0.1252 0.0258  -0.0373 395 LYS A NZ  
2839 N N   . ASP A 394 ? 0.4229 0.5057 0.3944 -0.0566 0.0079  -0.0259 396 ASP A N   
2840 C CA  . ASP A 394 ? 0.4440 0.5292 0.4192 -0.0533 0.0071  -0.0269 396 ASP A CA  
2841 C C   . ASP A 394 ? 0.4491 0.5224 0.4128 -0.0627 0.0102  -0.0285 396 ASP A C   
2842 O O   . ASP A 394 ? 0.4507 0.5242 0.4033 -0.0743 0.0131  -0.0309 396 ASP A O   
2843 C CB  . ASP A 394 ? 0.4502 0.5629 0.4327 -0.0506 0.0056  -0.0302 396 ASP A CB  
2844 C CG  . ASP A 394 ? 0.4619 0.5831 0.4531 -0.0389 0.0024  -0.0284 396 ASP A CG  
2845 O OD1 . ASP A 394 ? 0.4684 0.5742 0.4606 -0.0345 0.0015  -0.0247 396 ASP A OD1 
2846 O OD2 . ASP A 394 ? 0.4980 0.6413 0.4937 -0.0343 0.0009  -0.0308 396 ASP A OD2 
2847 N N   . ILE A 395 ? 0.4512 0.5145 0.4166 -0.0580 0.0095  -0.0274 397 ILE A N   
2848 C CA  . ILE A 395 ? 0.4655 0.5149 0.4192 -0.0650 0.0121  -0.0284 397 ILE A CA  
2849 C C   . ILE A 395 ? 0.4787 0.5429 0.4380 -0.0645 0.0114  -0.0311 397 ILE A C   
2850 O O   . ILE A 395 ? 0.5093 0.5740 0.4783 -0.0548 0.0089  -0.0298 397 ILE A O   
2851 C CB  . ILE A 395 ? 0.4496 0.4749 0.3991 -0.0592 0.0121  -0.0248 397 ILE A CB  
2852 C CG1 . ILE A 395 ? 0.4554 0.4682 0.3997 -0.0581 0.0126  -0.0223 397 ILE A CG1 
2853 C CG2 . ILE A 395 ? 0.4803 0.4907 0.4159 -0.0650 0.0148  -0.0257 397 ILE A CG2 
2854 C CD1 . ILE A 395 ? 0.4434 0.4404 0.3877 -0.0494 0.0115  -0.0188 397 ILE A CD1 
2855 N N   . GLU A 396 ? 0.4835 0.5590 0.4358 -0.0756 0.0138  -0.0350 398 GLU A N   
2856 C CA  . GLU A 396 ? 0.4764 0.5642 0.4307 -0.0775 0.0139  -0.0380 398 GLU A CA  
2857 C C   . GLU A 396 ? 0.4648 0.5282 0.4063 -0.0820 0.0162  -0.0368 398 GLU A C   
2858 O O   . GLU A 396 ? 0.4867 0.5324 0.4116 -0.0913 0.0194  -0.0366 398 GLU A O   
2859 C CB  . GLU A 396 ? 0.5204 0.6334 0.4714 -0.0888 0.0156  -0.0430 398 GLU A CB  
2860 C CG  . GLU A 396 ? 0.5275 0.6682 0.4913 -0.0816 0.0129  -0.0443 398 GLU A CG  
2861 C CD  . GLU A 396 ? 0.5765 0.7484 0.5382 -0.0919 0.0145  -0.0499 398 GLU A CD  
2862 O OE1 . GLU A 396 ? 0.6682 0.8435 0.6217 -0.1029 0.0168  -0.0514 398 GLU A OE1 
2863 O OE2 . GLU A 396 ? 0.6082 0.8015 0.5754 -0.0897 0.0135  -0.0531 398 GLU A OE2 
2864 N N   . PHE A 397 ? 0.4288 0.4890 0.3757 -0.0753 0.0148  -0.0361 399 PHE A N   
2865 C CA  . PHE A 397 ? 0.4345 0.4711 0.3687 -0.0778 0.0169  -0.0348 399 PHE A CA  
2866 C C   . PHE A 397 ? 0.4186 0.4640 0.3574 -0.0767 0.0163  -0.0366 399 PHE A C   
2867 O O   . PHE A 397 ? 0.3865 0.4532 0.3397 -0.0708 0.0137  -0.0383 399 PHE A O   
2868 C CB  . PHE A 397 ? 0.4225 0.4375 0.3559 -0.0684 0.0158  -0.0303 399 PHE A CB  
2869 C CG  . PHE A 397 ? 0.3936 0.4142 0.3435 -0.0557 0.0121  -0.0284 399 PHE A CG  
2870 C CD1 . PHE A 397 ? 0.3768 0.4099 0.3392 -0.0499 0.0096  -0.0278 399 PHE A CD1 
2871 C CD2 . PHE A 397 ? 0.3902 0.4029 0.3415 -0.0501 0.0114  -0.0273 399 PHE A CD2 
2872 C CE1 . PHE A 397 ? 0.3553 0.3904 0.3294 -0.0399 0.0066  -0.0262 399 PHE A CE1 
2873 C CE2 . PHE A 397 ? 0.3683 0.3858 0.3329 -0.0405 0.0084  -0.0260 399 PHE A CE2 
2874 C CZ  . PHE A 397 ? 0.3515 0.3790 0.3266 -0.0359 0.0061  -0.0254 399 PHE A CZ  
2875 N N   . THR A 398 ? 0.4451 0.4733 0.3698 -0.0821 0.0188  -0.0365 400 THR A N   
2876 C CA  . THR A 398 ? 0.4652 0.4994 0.3922 -0.0820 0.0186  -0.0382 400 THR A CA  
2877 C C   . THR A 398 ? 0.4711 0.4840 0.3945 -0.0743 0.0182  -0.0350 400 THR A C   
2878 O O   . THR A 398 ? 0.4934 0.4825 0.4002 -0.0765 0.0205  -0.0329 400 THR A O   
2879 C CB  . THR A 398 ? 0.4926 0.5339 0.4070 -0.0972 0.0220  -0.0421 400 THR A CB  
2880 O OG1 . THR A 398 ? 0.4926 0.5640 0.4177 -0.0998 0.0210  -0.0456 400 THR A OG1 
2881 C CG2 . THR A 398 ? 0.4942 0.5372 0.4075 -0.0980 0.0224  -0.0435 400 THR A CG2 
2882 N N   . ILE A 399 ? 0.4597 0.4818 0.3974 -0.0651 0.0154  -0.0349 401 ILE A N   
2883 C CA  . ILE A 399 ? 0.4593 0.4684 0.3963 -0.0580 0.0147  -0.0328 401 ILE A CA  
2884 C C   . ILE A 399 ? 0.4633 0.4766 0.3957 -0.0636 0.0161  -0.0354 401 ILE A C   
2885 O O   . ILE A 399 ? 0.4210 0.4558 0.3629 -0.0653 0.0151  -0.0386 401 ILE A O   
2886 C CB  . ILE A 399 ? 0.4391 0.4557 0.3933 -0.0464 0.0111  -0.0316 401 ILE A CB  
2887 C CG1 . ILE A 399 ? 0.4340 0.4482 0.3932 -0.0415 0.0097  -0.0292 401 ILE A CG1 
2888 C CG2 . ILE A 399 ? 0.4371 0.4441 0.3903 -0.0408 0.0107  -0.0303 401 ILE A CG2 
2889 C CD1 . ILE A 399 ? 0.4207 0.4410 0.3939 -0.0325 0.0066  -0.0284 401 ILE A CD1 
2890 N N   . SER A 400 ? 0.4865 0.4799 0.4038 -0.0651 0.0182  -0.0340 402 SER A N   
2891 C CA  . SER A 400 ? 0.5168 0.5099 0.4263 -0.0708 0.0199  -0.0359 402 SER A CA  
2892 C C   . SER A 400 ? 0.4991 0.4764 0.4042 -0.0625 0.0195  -0.0333 402 SER A C   
2893 O O   . SER A 400 ? 0.5087 0.4626 0.3964 -0.0614 0.0214  -0.0308 402 SER A O   
2894 C CB  . SER A 400 ? 0.5653 0.5496 0.4547 -0.0853 0.0239  -0.0374 402 SER A CB  
2895 O OG  . SER A 400 ? 0.6207 0.6162 0.5079 -0.0933 0.0252  -0.0406 402 SER A OG  
2896 N N   . GLY A 401 ? 0.4685 0.4588 0.3883 -0.0561 0.0171  -0.0342 403 GLY A N   
2897 C CA  . GLY A 401 ? 0.4611 0.4419 0.3779 -0.0494 0.0167  -0.0327 403 GLY A CA  
2898 C C   . GLY A 401 ? 0.4860 0.4633 0.3905 -0.0572 0.0192  -0.0344 403 GLY A C   
2899 O O   . GLY A 401 ? 0.4868 0.4825 0.3997 -0.0626 0.0189  -0.0377 403 GLY A O   
2900 N N   . THR A 402 ? 0.5092 0.4636 0.3932 -0.0576 0.0216  -0.0324 404 THR A N   
2901 C CA  . THR A 402 ? 0.5347 0.4821 0.4046 -0.0642 0.0240  -0.0336 404 THR A CA  
2902 C C   . THR A 402 ? 0.5281 0.4827 0.4088 -0.0547 0.0218  -0.0334 404 THR A C   
2903 O O   . THR A 402 ? 0.5203 0.4636 0.3975 -0.0444 0.0210  -0.0306 404 THR A O   
2904 C CB  . THR A 402 ? 0.5723 0.4881 0.4113 -0.0686 0.0278  -0.0314 404 THR A CB  
2905 O OG1 . THR A 402 ? 0.5717 0.4829 0.4013 -0.0791 0.0300  -0.0322 404 THR A OG1 
2906 C CG2 . THR A 402 ? 0.6006 0.5056 0.4214 -0.0764 0.0307  -0.0322 404 THR A CG2 
2907 N N   . ILE A 403 ? 0.5335 0.5076 0.4266 -0.0580 0.0208  -0.0365 405 ILE A N   
2908 C CA  . ILE A 403 ? 0.5390 0.5210 0.4413 -0.0513 0.0191  -0.0371 405 ILE A CA  
2909 C C   . ILE A 403 ? 0.5774 0.5568 0.4670 -0.0600 0.0216  -0.0388 405 ILE A C   
2910 O O   . ILE A 403 ? 0.5638 0.5607 0.4592 -0.0685 0.0220  -0.0423 405 ILE A O   
2911 C CB  . ILE A 403 ? 0.5155 0.5218 0.4425 -0.0468 0.0157  -0.0395 405 ILE A CB  
2912 C CG1 . ILE A 403 ? 0.4919 0.4981 0.4287 -0.0395 0.0136  -0.0376 405 ILE A CG1 
2913 C CG2 . ILE A 403 ? 0.5056 0.5212 0.4417 -0.0418 0.0141  -0.0410 405 ILE A CG2 
2914 C CD1 . ILE A 403 ? 0.4682 0.4937 0.4243 -0.0364 0.0107  -0.0399 405 ILE A CD1 
2915 N N   . ASP A 404 ? 0.6054 0.5654 0.4781 -0.0573 0.0232  -0.0365 406 ASP A N   
2916 C CA  . ASP A 404 ? 0.6428 0.5959 0.4997 -0.0656 0.0259  -0.0376 406 ASP A CA  
2917 C C   . ASP A 404 ? 0.6574 0.6328 0.5317 -0.0636 0.0239  -0.0404 406 ASP A C   
2918 O O   . ASP A 404 ? 0.6189 0.6141 0.5164 -0.0565 0.0205  -0.0419 406 ASP A O   
2919 C CB  . ASP A 404 ? 0.6729 0.5950 0.5031 -0.0617 0.0283  -0.0339 406 ASP A CB  
2920 C CG  . ASP A 404 ? 0.6600 0.5815 0.4961 -0.0464 0.0259  -0.0318 406 ASP A CG  
2921 O OD1 . ASP A 404 ? 0.6363 0.5808 0.4958 -0.0415 0.0229  -0.0337 406 ASP A OD1 
2922 O OD2 . ASP A 404 ? 0.6809 0.5790 0.4968 -0.0392 0.0271  -0.0285 406 ASP A OD2 
2923 N N   . SER A 405 ? 0.7005 0.6722 0.5622 -0.0708 0.0262  -0.0416 407 SER A N   
2924 C CA  . SER A 405 ? 0.6873 0.6805 0.5623 -0.0719 0.0250  -0.0449 407 SER A CA  
2925 C C   . SER A 405 ? 0.6483 0.6462 0.5370 -0.0580 0.0219  -0.0439 407 SER A C   
2926 O O   . SER A 405 ? 0.6170 0.6373 0.5262 -0.0548 0.0193  -0.0469 407 SER A O   
2927 C CB  . SER A 405 ? 0.7319 0.7168 0.5869 -0.0836 0.0285  -0.0459 407 SER A CB  
2928 O OG  . SER A 405 ? 0.7690 0.7224 0.5989 -0.0813 0.0309  -0.0418 407 SER A OG  
2929 N N   . THR A 406 ? 0.6412 0.6196 0.5182 -0.0497 0.0222  -0.0402 408 THR A N   
2930 C CA  . THR A 406 ? 0.6376 0.6209 0.5263 -0.0364 0.0194  -0.0391 408 THR A CA  
2931 C C   . THR A 406 ? 0.6318 0.6319 0.5435 -0.0314 0.0162  -0.0404 408 THR A C   
2932 O O   . THR A 406 ? 0.6249 0.6393 0.5521 -0.0260 0.0138  -0.0420 408 THR A O   
2933 C CB  . THR A 406 ? 0.6562 0.6185 0.5288 -0.0274 0.0200  -0.0350 408 THR A CB  
2934 O OG1 . THR A 406 ? 0.7160 0.6568 0.5622 -0.0327 0.0235  -0.0335 408 THR A OG1 
2935 C CG2 . THR A 406 ? 0.6250 0.5950 0.5064 -0.0151 0.0177  -0.0343 408 THR A CG2 
2936 N N   . GLY A 407 ? 0.6144 0.6112 0.5265 -0.0333 0.0163  -0.0395 409 GLY A N   
2937 C CA  . GLY A 407 ? 0.5982 0.6068 0.5287 -0.0283 0.0135  -0.0400 409 GLY A CA  
2938 C C   . GLY A 407 ? 0.5792 0.5764 0.5053 -0.0212 0.0131  -0.0366 409 GLY A C   
2939 O O   . GLY A 407 ? 0.5511 0.5580 0.4918 -0.0163 0.0107  -0.0369 409 GLY A O   
2940 N N   . ASP A 408 ? 0.5885 0.5654 0.4939 -0.0207 0.0154  -0.0337 410 ASP A N   
2941 C CA  . ASP A 408 ? 0.5970 0.5615 0.4941 -0.0133 0.0154  -0.0305 410 ASP A CA  
2942 C C   . ASP A 408 ? 0.5487 0.5092 0.4453 -0.0186 0.0160  -0.0301 410 ASP A C   
2943 O O   . ASP A 408 ? 0.5345 0.4882 0.4211 -0.0287 0.0183  -0.0309 410 ASP A O   
2944 C CB  . ASP A 408 ? 0.6710 0.6133 0.5429 -0.0085 0.0176  -0.0277 410 ASP A CB  
2945 C CG  . ASP A 408 ? 0.7625 0.7085 0.6329 -0.0031 0.0172  -0.0280 410 ASP A CG  
2946 O OD1 . ASP A 408 ? 0.7636 0.7306 0.6544 0.0001  0.0147  -0.0299 410 ASP A OD1 
2947 O OD2 . ASP A 408 ? 0.8688 0.7960 0.7165 -0.0029 0.0197  -0.0265 410 ASP A OD2 
2948 N N   . LEU A 409 ? 0.4943 0.4606 0.4017 -0.0130 0.0140  -0.0292 411 LEU A N   
2949 C CA  . LEU A 409 ? 0.4627 0.4221 0.3664 -0.0163 0.0147  -0.0281 411 LEU A CA  
2950 C C   . LEU A 409 ? 0.4744 0.4101 0.3540 -0.0122 0.0170  -0.0250 411 LEU A C   
2951 O O   . LEU A 409 ? 0.4578 0.3919 0.3355 -0.0015 0.0159  -0.0232 411 LEU A O   
2952 C CB  . LEU A 409 ? 0.4382 0.4113 0.3604 -0.0118 0.0120  -0.0281 411 LEU A CB  
2953 C CG  . LEU A 409 ? 0.4419 0.4089 0.3612 -0.0141 0.0125  -0.0268 411 LEU A CG  
2954 C CD1 . LEU A 409 ? 0.4259 0.4010 0.3519 -0.0234 0.0127  -0.0290 411 LEU A CD1 
2955 C CD2 . LEU A 409 ? 0.4388 0.4131 0.3691 -0.0069 0.0103  -0.0257 411 LEU A CD2 
2956 N N   . THR A 410 ? 0.5061 0.4241 0.3660 -0.0205 0.0201  -0.0248 412 THR A N   
2957 C CA  . THR A 410 ? 0.5644 0.4532 0.3946 -0.0174 0.0229  -0.0220 412 THR A CA  
2958 C C   . THR A 410 ? 0.5928 0.4693 0.4142 -0.0191 0.0239  -0.0207 412 THR A C   
2959 O O   . THR A 410 ? 0.6341 0.4887 0.4343 -0.0117 0.0252  -0.0181 412 THR A O   
2960 C CB  . THR A 410 ? 0.5856 0.4586 0.3951 -0.0274 0.0262  -0.0227 412 THR A CB  
2961 O OG1 . THR A 410 ? 0.5758 0.4583 0.3915 -0.0423 0.0273  -0.0255 412 THR A OG1 
2962 C CG2 . THR A 410 ? 0.5866 0.4677 0.4006 -0.0235 0.0253  -0.0234 412 THR A CG2 
2963 N N   . ASN A 411 ? 0.5972 0.4875 0.4332 -0.0279 0.0234  -0.0226 413 ASN A N   
2964 C CA  . ASN A 411 ? 0.6011 0.4813 0.4292 -0.0320 0.0246  -0.0218 413 ASN A CA  
2965 C C   . ASN A 411 ? 0.5349 0.4399 0.3896 -0.0339 0.0220  -0.0234 413 ASN A C   
2966 O O   . ASN A 411 ? 0.4955 0.4213 0.3684 -0.0372 0.0204  -0.0258 413 ASN A O   
2967 C CB  . ASN A 411 ? 0.6647 0.5270 0.4699 -0.0466 0.0287  -0.0229 413 ASN A CB  
2968 C CG  . ASN A 411 ? 0.7113 0.5423 0.4879 -0.0454 0.0314  -0.0205 413 ASN A CG  
2969 O OD1 . ASN A 411 ? 0.7470 0.5521 0.4978 -0.0410 0.0335  -0.0187 413 ASN A OD1 
2970 N ND2 . ASN A 411 ? 0.6881 0.5201 0.4678 -0.0478 0.0314  -0.0205 413 ASN A ND2 
2971 N N   . LEU A 412 ? 0.5145 0.4159 0.3692 -0.0313 0.0216  -0.0220 414 LEU A N   
2972 C CA  . LEU A 412 ? 0.4800 0.4006 0.3554 -0.0336 0.0195  -0.0231 414 LEU A CA  
2973 C C   . LEU A 412 ? 0.5074 0.4150 0.3705 -0.0376 0.0213  -0.0221 414 LEU A C   
2974 O O   . LEU A 412 ? 0.5307 0.4224 0.3816 -0.0298 0.0217  -0.0196 414 LEU A O   
2975 C CB  . LEU A 412 ? 0.4440 0.3789 0.3385 -0.0226 0.0161  -0.0221 414 LEU A CB  
2976 C CG  . LEU A 412 ? 0.4063 0.3557 0.3183 -0.0228 0.0139  -0.0224 414 LEU A CG  
2977 C CD1 . LEU A 412 ? 0.3918 0.3587 0.3180 -0.0294 0.0130  -0.0252 414 LEU A CD1 
2978 C CD2 . LEU A 412 ? 0.3884 0.3466 0.3129 -0.0133 0.0113  -0.0211 414 LEU A CD2 
2979 N N   . THR A 413 ? 0.5031 0.4193 0.3697 -0.0486 0.0221  -0.0243 415 THR A N   
2980 C CA  . THR A 413 ? 0.5173 0.4223 0.3712 -0.0551 0.0242  -0.0240 415 THR A CA  
2981 C C   . THR A 413 ? 0.5006 0.4282 0.3750 -0.0573 0.0221  -0.0254 415 THR A C   
2982 O O   . THR A 413 ? 0.4632 0.4134 0.3565 -0.0576 0.0200  -0.0274 415 THR A O   
2983 C CB  . THR A 413 ? 0.5548 0.4444 0.3851 -0.0690 0.0284  -0.0258 415 THR A CB  
2984 O OG1 . THR A 413 ? 0.5532 0.4679 0.3980 -0.0783 0.0279  -0.0293 415 THR A OG1 
2985 C CG2 . THR A 413 ? 0.5835 0.4502 0.3926 -0.0664 0.0304  -0.0244 415 THR A CG2 
2986 N N   . ALA A 414 ? 0.5011 0.4217 0.3710 -0.0572 0.0226  -0.0241 416 ALA A N   
2987 C CA  . ALA A 414 ? 0.5009 0.4395 0.3852 -0.0605 0.0212  -0.0253 416 ALA A CA  
2988 C C   . ALA A 414 ? 0.5249 0.4494 0.3904 -0.0702 0.0244  -0.0257 416 ALA A C   
2989 O O   . ALA A 414 ? 0.5309 0.4310 0.3781 -0.0671 0.0261  -0.0235 416 ALA A O   
2990 C CB  . ALA A 414 ? 0.4778 0.4250 0.3795 -0.0489 0.0178  -0.0231 416 ALA A CB  
2991 N N   . THR A 415 ? 0.5274 0.4668 0.3953 -0.0816 0.0255  -0.0288 417 THR A N   
2992 C CA  . THR A 415 ? 0.5598 0.4884 0.4089 -0.0942 0.0290  -0.0302 417 THR A CA  
2993 C C   . THR A 415 ? 0.5491 0.5030 0.4144 -0.0974 0.0275  -0.0320 417 THR A C   
2994 O O   . THR A 415 ? 0.5104 0.4912 0.3970 -0.0936 0.0246  -0.0335 417 THR A O   
2995 C CB  . THR A 415 ? 0.5986 0.5193 0.4280 -0.1089 0.0329  -0.0330 417 THR A CB  
2996 O OG1 . THR A 415 ? 0.5966 0.5491 0.4448 -0.1124 0.0313  -0.0362 417 THR A OG1 
2997 C CG2 . THR A 415 ? 0.6149 0.5091 0.4265 -0.1049 0.0344  -0.0310 417 THR A CG2 
2998 N N   . SER A 416 ? 0.5618 0.5060 0.4156 -0.1031 0.0294  -0.0319 418 SER A N   
2999 C CA  . SER A 416 ? 0.5831 0.5492 0.4478 -0.1075 0.0286  -0.0338 418 SER A CA  
3000 C C   . SER A 416 ? 0.6392 0.5883 0.4803 -0.1207 0.0327  -0.0350 418 SER A C   
3001 O O   . SER A 416 ? 0.6703 0.5868 0.4906 -0.1191 0.0348  -0.0326 418 SER A O   
3002 C CB  . SER A 416 ? 0.5469 0.5200 0.4303 -0.0934 0.0247  -0.0308 418 SER A CB  
3003 O OG  . SER A 416 ? 0.5257 0.5186 0.4188 -0.0961 0.0238  -0.0322 418 SER A OG  
3004 N N   . ALA A 417 ? 0.6561 0.6263 0.4988 -0.1330 0.0339  -0.0388 419 ALA A N   
3005 C CA  . ALA A 417 ? 0.7071 0.6664 0.5304 -0.1465 0.0376  -0.0405 419 ALA A CA  
3006 C C   . ALA A 417 ? 0.7190 0.6666 0.5453 -0.1360 0.0359  -0.0370 419 ALA A C   
3007 O O   . ALA A 417 ? 0.7751 0.6949 0.5783 -0.1412 0.0390  -0.0363 419 ALA A O   
3008 C CB  . ALA A 417 ? 0.7165 0.7098 0.5470 -0.1592 0.0383  -0.0455 419 ALA A CB  
3009 N N   . THR A 418 ? 0.7027 0.6681 0.5544 -0.1214 0.0314  -0.0347 420 THR A N   
3010 C CA  . THR A 418 ? 0.6768 0.6405 0.5364 -0.1123 0.0294  -0.0319 420 THR A CA  
3011 C C   . THR A 418 ? 0.6520 0.5920 0.5088 -0.0985 0.0281  -0.0275 420 THR A C   
3012 O O   . THR A 418 ? 0.6674 0.6026 0.5260 -0.0926 0.0272  -0.0254 420 THR A O   
3013 C CB  . THR A 418 ? 0.6764 0.6709 0.5639 -0.1030 0.0250  -0.0316 420 THR A CB  
3014 O OG1 . THR A 418 ? 0.7446 0.7645 0.6399 -0.1087 0.0248  -0.0353 420 THR A OG1 
3015 C CG2 . THR A 418 ? 0.6891 0.6930 0.5825 -0.1022 0.0241  -0.0312 420 THR A CG2 
3016 N N   . ALA A 419 ? 0.6376 0.5668 0.4919 -0.0925 0.0278  -0.0262 421 ALA A N   
3017 C CA  . ALA A 419 ? 0.5958 0.5140 0.4548 -0.0771 0.0255  -0.0223 421 ALA A CA  
3018 C C   . ALA A 419 ? 0.5921 0.4886 0.4348 -0.0745 0.0271  -0.0215 421 ALA A C   
3019 O O   . ALA A 419 ? 0.6233 0.5148 0.4538 -0.0847 0.0296  -0.0238 421 ALA A O   
3020 C CB  . ALA A 419 ? 0.5501 0.4929 0.4366 -0.0679 0.0212  -0.0214 421 ALA A CB  
3021 N N   . SER A 420 ? 0.5781 0.4626 0.4191 -0.0614 0.0257  -0.0185 422 SER A N   
3022 C CA  . SER A 420 ? 0.6073 0.4728 0.4336 -0.0554 0.0267  -0.0173 422 SER A CA  
3023 C C   . SER A 420 ? 0.5731 0.4536 0.4198 -0.0426 0.0230  -0.0156 422 SER A C   
3024 O O   . SER A 420 ? 0.5467 0.4377 0.4072 -0.0348 0.0205  -0.0140 422 SER A O   
3025 C CB  . SER A 420 ? 0.6569 0.4919 0.4564 -0.0503 0.0290  -0.0156 422 SER A CB  
3026 O OG  . SER A 420 ? 0.7270 0.5486 0.5091 -0.0614 0.0321  -0.0170 422 SER A OG  
3027 N N   . PHE A 421 ? 0.5670 0.4475 0.4137 -0.0411 0.0229  -0.0160 423 PHE A N   
3028 C CA  . PHE A 421 ? 0.5380 0.4320 0.4018 -0.0303 0.0198  -0.0148 423 PHE A CA  
3029 C C   . PHE A 421 ? 0.5742 0.4498 0.4208 -0.0212 0.0207  -0.0132 423 PHE A C   
3030 O O   . PHE A 421 ? 0.6157 0.4682 0.4378 -0.0250 0.0239  -0.0135 423 PHE A O   
3031 C CB  . PHE A 421 ? 0.5095 0.4225 0.3900 -0.0352 0.0185  -0.0168 423 PHE A CB  
3032 C CG  . PHE A 421 ? 0.4736 0.4062 0.3701 -0.0416 0.0173  -0.0184 423 PHE A CG  
3033 C CD1 . PHE A 421 ? 0.4909 0.4238 0.3796 -0.0533 0.0196  -0.0207 423 PHE A CD1 
3034 C CD2 . PHE A 421 ? 0.4465 0.3973 0.3642 -0.0360 0.0140  -0.0179 423 PHE A CD2 
3035 C CE1 . PHE A 421 ? 0.5018 0.4553 0.4049 -0.0576 0.0183  -0.0223 423 PHE A CE1 
3036 C CE2 . PHE A 421 ? 0.4407 0.4080 0.3708 -0.0399 0.0129  -0.0192 423 PHE A CE2 
3037 C CZ  . PHE A 421 ? 0.4677 0.4377 0.3912 -0.0498 0.0148  -0.0214 423 PHE A CZ  
3038 N N   . GLU A 422 ? 0.5709 0.4567 0.4286 -0.0095 0.0182  -0.0118 424 GLU A N   
3039 C CA  . GLU A 422 ? 0.5794 0.4584 0.4283 0.0001  0.0181  -0.0110 424 GLU A CA  
3040 C C   . GLU A 422 ? 0.5275 0.4236 0.3935 -0.0024 0.0165  -0.0123 424 GLU A C   
3041 O O   . GLU A 422 ? 0.4762 0.3923 0.3639 -0.0061 0.0145  -0.0133 424 GLU A O   
3042 C CB  . GLU A 422 ? 0.6347 0.5212 0.4877 0.0134  0.0161  -0.0093 424 GLU A CB  
3043 C CG  . GLU A 422 ? 0.7287 0.6021 0.5676 0.0178  0.0171  -0.0081 424 GLU A CG  
3044 C CD  . GLU A 422 ? 0.8240 0.6691 0.6315 0.0256  0.0196  -0.0071 424 GLU A CD  
3045 O OE1 . GLU A 422 ? 0.9130 0.7485 0.7104 0.0255  0.0207  -0.0073 424 GLU A OE1 
3046 O OE2 . GLU A 422 ? 0.8875 0.7192 0.6795 0.0322  0.0204  -0.0060 424 GLU A OE2 
3047 N N   . THR A 423 ? 0.5191 0.4063 0.3741 0.0000  0.0176  -0.0125 425 THR A N   
3048 C CA  . THR A 423 ? 0.4845 0.3876 0.3547 -0.0001 0.0159  -0.0137 425 THR A CA  
3049 C C   . THR A 423 ? 0.4779 0.3756 0.3382 0.0109  0.0158  -0.0127 425 THR A C   
3050 O O   . THR A 423 ? 0.4959 0.3716 0.3318 0.0163  0.0179  -0.0113 425 THR A O   
3051 C CB  . THR A 423 ? 0.4839 0.3859 0.3528 -0.0116 0.0174  -0.0158 425 THR A CB  
3052 O OG1 . THR A 423 ? 0.5117 0.3893 0.3542 -0.0115 0.0204  -0.0151 425 THR A OG1 
3053 C CG2 . THR A 423 ? 0.4664 0.3747 0.3417 -0.0224 0.0179  -0.0172 425 THR A CG2 
3054 N N   . ASP A 424 ? 0.4519 0.3694 0.3300 0.0145  0.0135  -0.0134 426 ASP A N   
3055 C CA  . ASP A 424 ? 0.4639 0.3832 0.3373 0.0234  0.0130  -0.0132 426 ASP A CA  
3056 C C   . ASP A 424 ? 0.4301 0.3623 0.3178 0.0177  0.0121  -0.0152 426 ASP A C   
3057 O O   . ASP A 424 ? 0.3944 0.3454 0.3029 0.0146  0.0100  -0.0164 426 ASP A O   
3058 C CB  . ASP A 424 ? 0.4692 0.4029 0.3492 0.0344  0.0110  -0.0125 426 ASP A CB  
3059 C CG  . ASP A 424 ? 0.4934 0.4304 0.3666 0.0446  0.0107  -0.0125 426 ASP A CG  
3060 O OD1 . ASP A 424 ? 0.5092 0.4405 0.3781 0.0418  0.0115  -0.0131 426 ASP A OD1 
3061 O OD2 . ASP A 424 ? 0.5333 0.4797 0.4049 0.0553  0.0096  -0.0119 426 ASP A OD2 
3062 N N   . VAL A 425 ? 0.4548 0.3753 0.3295 0.0164  0.0138  -0.0155 427 VAL A N   
3063 C CA  . VAL A 425 ? 0.4337 0.3650 0.3196 0.0110  0.0132  -0.0175 427 VAL A CA  
3064 C C   . VAL A 425 ? 0.4133 0.3638 0.3137 0.0183  0.0108  -0.0181 427 VAL A C   
3065 O O   . VAL A 425 ? 0.3807 0.3467 0.2989 0.0135  0.0092  -0.0201 427 VAL A O   
3066 C CB  . VAL A 425 ? 0.4683 0.3814 0.3344 0.0075  0.0159  -0.0175 427 VAL A CB  
3067 C CG1 . VAL A 425 ? 0.5071 0.4038 0.3513 0.0190  0.0170  -0.0154 427 VAL A CG1 
3068 C CG2 . VAL A 425 ? 0.4632 0.3895 0.3417 0.0023  0.0152  -0.0198 427 VAL A CG2 
3069 N N   . ASN A 426 ? 0.4308 0.3814 0.3234 0.0295  0.0104  -0.0168 428 ASN A N   
3070 C CA  . ASN A 426 ? 0.4317 0.4033 0.3363 0.0361  0.0083  -0.0178 428 ASN A CA  
3071 C C   . ASN A 426 ? 0.3885 0.3801 0.3149 0.0317  0.0061  -0.0191 428 ASN A C   
3072 O O   . ASN A 426 ? 0.3879 0.3951 0.3275 0.0295  0.0048  -0.0210 428 ASN A O   
3073 C CB  . ASN A 426 ? 0.4873 0.4572 0.3775 0.0498  0.0084  -0.0162 428 ASN A CB  
3074 C CG  . ASN A 426 ? 0.5662 0.5120 0.4304 0.0557  0.0106  -0.0147 428 ASN A CG  
3075 O OD1 . ASN A 426 ? 0.5945 0.5270 0.4527 0.0480  0.0122  -0.0149 428 ASN A OD1 
3076 N ND2 . ASN A 426 ? 0.6219 0.5618 0.4689 0.0696  0.0109  -0.0131 428 ASN A ND2 
3077 N N   . THR A 427 ? 0.3695 0.3593 0.2979 0.0300  0.0060  -0.0181 429 THR A N   
3078 C CA  . THR A 427 ? 0.3290 0.3347 0.2746 0.0260  0.0042  -0.0189 429 THR A CA  
3079 C C   . THR A 427 ? 0.3019 0.3049 0.2570 0.0162  0.0040  -0.0198 429 THR A C   
3080 O O   . THR A 427 ? 0.2842 0.2979 0.2527 0.0122  0.0025  -0.0208 429 THR A O   
3081 C CB  . THR A 427 ? 0.3285 0.3355 0.2704 0.0310  0.0040  -0.0173 429 THR A CB  
3082 O OG1 . THR A 427 ? 0.3342 0.3225 0.2648 0.0297  0.0056  -0.0157 429 THR A OG1 
3083 C CG2 . THR A 427 ? 0.3384 0.3519 0.2709 0.0425  0.0040  -0.0169 429 THR A CG2 
3084 N N   . GLY A 428 ? 0.2980 0.2874 0.2448 0.0125  0.0056  -0.0197 430 GLY A N   
3085 C CA  . GLY A 428 ? 0.2888 0.2774 0.2423 0.0041  0.0056  -0.0207 430 GLY A CA  
3086 C C   . GLY A 428 ? 0.2841 0.2717 0.2403 0.0022  0.0053  -0.0196 430 GLY A C   
3087 O O   . GLY A 428 ? 0.2581 0.2500 0.2229 -0.0029 0.0046  -0.0206 430 GLY A O   
3088 N N   . ILE A 429 ? 0.3026 0.2857 0.2514 0.0072  0.0057  -0.0177 431 ILE A N   
3089 C CA  . ILE A 429 ? 0.3100 0.2936 0.2621 0.0060  0.0053  -0.0165 431 ILE A CA  
3090 C C   . ILE A 429 ? 0.3237 0.2919 0.2623 0.0031  0.0073  -0.0157 431 ILE A C   
3091 O O   . ILE A 429 ? 0.3413 0.2959 0.2634 0.0067  0.0090  -0.0148 431 ILE A O   
3092 C CB  . ILE A 429 ? 0.3114 0.3026 0.2649 0.0125  0.0043  -0.0154 431 ILE A CB  
3093 C CG1 . ILE A 429 ? 0.2972 0.3049 0.2643 0.0118  0.0024  -0.0167 431 ILE A CG1 
3094 C CG2 . ILE A 429 ? 0.3191 0.3079 0.2725 0.0115  0.0043  -0.0140 431 ILE A CG2 
3095 C CD1 . ILE A 429 ? 0.3046 0.3229 0.2702 0.0183  0.0019  -0.0164 431 ILE A CD1 
3096 N N   . ILE A 430 ? 0.3186 0.2890 0.2633 -0.0032 0.0072  -0.0161 432 ILE A N   
3097 C CA  . ILE A 430 ? 0.3379 0.2976 0.2725 -0.0081 0.0090  -0.0157 432 ILE A CA  
3098 C C   . ILE A 430 ? 0.3282 0.2907 0.2670 -0.0058 0.0081  -0.0142 432 ILE A C   
3099 O O   . ILE A 430 ? 0.2896 0.2644 0.2430 -0.0069 0.0062  -0.0145 432 ILE A O   
3100 C CB  . ILE A 430 ? 0.3399 0.3062 0.2807 -0.0165 0.0092  -0.0178 432 ILE A CB  
3101 C CG1 . ILE A 430 ? 0.3586 0.3255 0.2973 -0.0191 0.0098  -0.0196 432 ILE A CG1 
3102 C CG2 . ILE A 430 ? 0.3510 0.3098 0.2821 -0.0230 0.0111  -0.0179 432 ILE A CG2 
3103 C CD1 . ILE A 430 ? 0.3546 0.3364 0.3058 -0.0239 0.0088  -0.0221 432 ILE A CD1 
3104 N N   . THR A 431 ? 0.3551 0.3053 0.2801 -0.0024 0.0094  -0.0127 433 THR A N   
3105 C CA  . THR A 431 ? 0.3522 0.3048 0.2796 0.0001  0.0087  -0.0113 433 THR A CA  
3106 C C   . THR A 431 ? 0.3618 0.3065 0.2829 -0.0067 0.0102  -0.0114 433 THR A C   
3107 O O   . THR A 431 ? 0.3904 0.3188 0.2941 -0.0099 0.0128  -0.0117 433 THR A O   
3108 C CB  . THR A 431 ? 0.3721 0.3180 0.2877 0.0098  0.0091  -0.0098 433 THR A CB  
3109 O OG1 . THR A 431 ? 0.3642 0.3205 0.2852 0.0159  0.0078  -0.0100 433 THR A OG1 
3110 C CG2 . THR A 431 ? 0.3881 0.3396 0.3077 0.0124  0.0082  -0.0086 433 THR A CG2 
3111 N N   . LEU A 432 ? 0.3420 0.2970 0.2752 -0.0090 0.0089  -0.0111 434 LEU A N   
3112 C CA  . LEU A 432 ? 0.3457 0.2959 0.2737 -0.0141 0.0100  -0.0111 434 LEU A CA  
3113 C C   . LEU A 432 ? 0.3467 0.3000 0.2781 -0.0089 0.0089  -0.0092 434 LEU A C   
3114 O O   . LEU A 432 ? 0.3093 0.2761 0.2555 -0.0070 0.0066  -0.0086 434 LEU A O   
3115 C CB  . LEU A 432 ? 0.3282 0.2904 0.2673 -0.0213 0.0094  -0.0127 434 LEU A CB  
3116 C CG  . LEU A 432 ? 0.3286 0.2911 0.2651 -0.0270 0.0102  -0.0130 434 LEU A CG  
3117 C CD1 . LEU A 432 ? 0.3528 0.2988 0.2691 -0.0333 0.0136  -0.0140 434 LEU A CD1 
3118 C CD2 . LEU A 432 ? 0.3125 0.2915 0.2616 -0.0313 0.0090  -0.0147 434 LEU A CD2 
3119 N N   . LYS A 433 ? 0.3981 0.3379 0.3144 -0.0068 0.0105  -0.0084 435 LYS A N   
3120 C CA  . LYS A 433 ? 0.4102 0.3525 0.3279 -0.0028 0.0098  -0.0069 435 LYS A CA  
3121 C C   . LYS A 433 ? 0.4085 0.3512 0.3276 -0.0103 0.0104  -0.0072 435 LYS A C   
3122 O O   . LYS A 433 ? 0.4285 0.3586 0.3340 -0.0160 0.0128  -0.0083 435 LYS A O   
3123 C CB  . LYS A 433 ? 0.4559 0.3829 0.3545 0.0051  0.0113  -0.0060 435 LYS A CB  
3124 C CG  . LYS A 433 ? 0.4889 0.4203 0.3884 0.0108  0.0105  -0.0047 435 LYS A CG  
3125 C CD  . LYS A 433 ? 0.5559 0.4739 0.4359 0.0214  0.0116  -0.0041 435 LYS A CD  
3126 C CE  . LYS A 433 ? 0.6407 0.5316 0.4963 0.0185  0.0148  -0.0045 435 LYS A CE  
3127 N NZ  . LYS A 433 ? 0.7213 0.5960 0.5547 0.0306  0.0159  -0.0037 435 LYS A NZ  
3128 N N   . VAL A 434 ? 0.3741 0.3307 0.3080 -0.0108 0.0084  -0.0065 436 VAL A N   
3129 C CA  . VAL A 434 ? 0.3790 0.3396 0.3163 -0.0171 0.0086  -0.0068 436 VAL A CA  
3130 C C   . VAL A 434 ? 0.3835 0.3424 0.3182 -0.0136 0.0085  -0.0052 436 VAL A C   
3131 O O   . VAL A 434 ? 0.3586 0.3272 0.3032 -0.0089 0.0065  -0.0037 436 VAL A O   
3132 C CB  . VAL A 434 ? 0.3594 0.3361 0.3137 -0.0193 0.0064  -0.0070 436 VAL A CB  
3133 C CG1 . VAL A 434 ? 0.3587 0.3406 0.3152 -0.0236 0.0064  -0.0072 436 VAL A CG1 
3134 C CG2 . VAL A 434 ? 0.3581 0.3385 0.3157 -0.0219 0.0063  -0.0089 436 VAL A CG2 
3135 N N   . VAL A 435 ? 0.4075 0.3541 0.3280 -0.0166 0.0106  -0.0057 437 VAL A N   
3136 C CA  . VAL A 435 ? 0.4167 0.3592 0.3315 -0.0127 0.0109  -0.0044 437 VAL A CA  
3137 C C   . VAL A 435 ? 0.4098 0.3627 0.3341 -0.0183 0.0102  -0.0043 437 VAL A C   
3138 O O   . VAL A 435 ? 0.4376 0.3889 0.3579 -0.0263 0.0116  -0.0060 437 VAL A O   
3139 C CB  . VAL A 435 ? 0.4511 0.3711 0.3418 -0.0114 0.0137  -0.0049 437 VAL A CB  
3140 C CG1 . VAL A 435 ? 0.4685 0.3852 0.3536 -0.0065 0.0138  -0.0038 437 VAL A CG1 
3141 C CG2 . VAL A 435 ? 0.4607 0.3706 0.3411 -0.0040 0.0142  -0.0048 437 VAL A CG2 
3142 N N   . ASN A 436 ? 0.3831 0.3477 0.3194 -0.0146 0.0080  -0.0025 438 ASN A N   
3143 C CA  . ASN A 436 ? 0.3804 0.3548 0.3253 -0.0183 0.0071  -0.0020 438 ASN A CA  
3144 C C   . ASN A 436 ? 0.3793 0.3460 0.3137 -0.0181 0.0085  -0.0017 438 ASN A C   
3145 O O   . ASN A 436 ? 0.3628 0.3243 0.2910 -0.0116 0.0086  -0.0007 438 ASN A O   
3146 C CB  . ASN A 436 ? 0.3757 0.3635 0.3359 -0.0155 0.0044  -0.0002 438 ASN A CB  
3147 C CG  . ASN A 436 ? 0.3846 0.3795 0.3541 -0.0176 0.0032  -0.0009 438 ASN A CG  
3148 O OD1 . ASN A 436 ? 0.4553 0.4578 0.4313 -0.0197 0.0022  -0.0009 438 ASN A OD1 
3149 N N   . LYS A 437 ? 0.4030 0.3699 0.3347 -0.0250 0.0096  -0.0028 439 LYS A N   
3150 C CA  . LYS A 437 ? 0.4262 0.3879 0.3495 -0.0265 0.0108  -0.0028 439 LYS A CA  
3151 C C   . LYS A 437 ? 0.3852 0.3624 0.3227 -0.0261 0.0087  -0.0012 439 LYS A C   
3152 O O   . LYS A 437 ? 0.3353 0.3246 0.2833 -0.0293 0.0075  -0.0015 439 LYS A O   
3153 C CB  . LYS A 437 ? 0.4913 0.4444 0.4014 -0.0361 0.0137  -0.0055 439 LYS A CB  
3154 C CG  . LYS A 437 ? 0.5659 0.4970 0.4554 -0.0371 0.0165  -0.0069 439 LYS A CG  
3155 C CD  . LYS A 437 ? 0.6168 0.5483 0.5074 -0.0398 0.0167  -0.0081 439 LYS A CD  
3156 C CE  . LYS A 437 ? 0.6582 0.5662 0.5280 -0.0376 0.0191  -0.0086 439 LYS A CE  
3157 N NZ  . LYS A 437 ? 0.6680 0.5781 0.5409 -0.0393 0.0190  -0.0094 439 LYS A NZ  
3158 N N   . GLN A 438 ? 0.3923 0.3686 0.3281 -0.0219 0.0084  0.0002  440 GLN A N   
3159 C CA  . GLN A 438 ? 0.3846 0.3730 0.3305 -0.0218 0.0067  0.0019  440 GLN A CA  
3160 C C   . GLN A 438 ? 0.3832 0.3759 0.3286 -0.0289 0.0075  0.0006  440 GLN A C   
3161 O O   . GLN A 438 ? 0.3995 0.3832 0.3325 -0.0344 0.0100  -0.0017 440 GLN A O   
3162 C CB  . GLN A 438 ? 0.4085 0.3939 0.3492 -0.0170 0.0069  0.0031  440 GLN A CB  
3163 C CG  . GLN A 438 ? 0.4188 0.4079 0.3629 -0.0096 0.0056  0.0044  440 GLN A CG  
3164 C CD  . GLN A 438 ? 0.4391 0.4308 0.3800 -0.0047 0.0055  0.0054  440 GLN A CD  
3165 O OE1 . GLN A 438 ? 0.4624 0.4595 0.4069 -0.0072 0.0051  0.0062  440 GLN A OE1 
3166 N NE2 . GLN A 438 ? 0.4550 0.4445 0.3889 0.0029  0.0057  0.0052  440 GLN A NE2 
3167 N N   . GLY A 439 ? 0.3601 0.3664 0.3173 -0.0290 0.0056  0.0019  441 GLY A N   
3168 C CA  . GLY A 439 ? 0.3678 0.3821 0.3253 -0.0342 0.0060  0.0008  441 GLY A CA  
3169 C C   . GLY A 439 ? 0.3703 0.3789 0.3194 -0.0354 0.0074  0.0008  441 GLY A C   
3170 O O   . GLY A 439 ? 0.3539 0.3513 0.2957 -0.0312 0.0081  0.0015  441 GLY A O   
3171 N N   . ALA A 440 ? 0.3665 0.3832 0.3156 -0.0403 0.0078  -0.0001 442 ALA A N   
3172 C CA  . ALA A 440 ? 0.3793 0.3915 0.3203 -0.0424 0.0092  -0.0004 442 ALA A CA  
3173 C C   . ALA A 440 ? 0.3552 0.3780 0.3069 -0.0375 0.0069  0.0026  442 ALA A C   
3174 O O   . ALA A 440 ? 0.3116 0.3477 0.2745 -0.0363 0.0048  0.0038  442 ALA A O   
3175 C CB  . ALA A 440 ? 0.3986 0.4135 0.3316 -0.0521 0.0115  -0.0039 442 ALA A CB  
3176 N N   . LEU A 441 ? 0.3711 0.3870 0.3182 -0.0338 0.0071  0.0038  443 LEU A N   
3177 C CA  . LEU A 441 ? 0.3836 0.4086 0.3380 -0.0309 0.0055  0.0064  443 LEU A CA  
3178 C C   . LEU A 441 ? 0.3818 0.4070 0.3291 -0.0356 0.0071  0.0048  443 LEU A C   
3179 O O   . LEU A 441 ? 0.3517 0.3650 0.2869 -0.0350 0.0089  0.0037  443 LEU A O   
3180 C CB  . LEU A 441 ? 0.4183 0.4398 0.3726 -0.0244 0.0048  0.0083  443 LEU A CB  
3181 C CG  . LEU A 441 ? 0.4365 0.4694 0.4004 -0.0224 0.0028  0.0113  443 LEU A CG  
3182 C CD1 . LEU A 441 ? 0.4375 0.4752 0.4107 -0.0208 0.0008  0.0133  443 LEU A CD1 
3183 C CD2 . LEU A 441 ? 0.4440 0.4764 0.4033 -0.0187 0.0031  0.0119  443 LEU A CD2 
3184 N N   . LEU A 442 ? 0.3728 0.4106 0.3256 -0.0398 0.0066  0.0042  444 LEU A N   
3185 C CA  . LEU A 442 ? 0.4044 0.4445 0.3497 -0.0469 0.0085  0.0015  444 LEU A CA  
3186 C C   . LEU A 442 ? 0.4165 0.4606 0.3634 -0.0447 0.0079  0.0034  444 LEU A C   
3187 O O   . LEU A 442 ? 0.4336 0.4874 0.3912 -0.0399 0.0054  0.0065  444 LEU A O   
3188 C CB  . LEU A 442 ? 0.3978 0.4542 0.3486 -0.0517 0.0082  -0.0002 444 LEU A CB  
3189 C CG  . LEU A 442 ? 0.4184 0.4711 0.3627 -0.0578 0.0100  -0.0036 444 LEU A CG  
3190 C CD1 . LEU A 442 ? 0.4171 0.4913 0.3676 -0.0619 0.0095  -0.0058 444 LEU A CD1 
3191 C CD2 . LEU A 442 ? 0.4345 0.4692 0.3602 -0.0655 0.0137  -0.0068 444 LEU A CD2 
3192 N N   . PRO A 443 ? 0.4325 0.4680 0.3670 -0.0486 0.0102  0.0013  445 PRO A N   
3193 C CA  . PRO A 443 ? 0.4276 0.4682 0.3630 -0.0474 0.0098  0.0024  445 PRO A CA  
3194 C C   . PRO A 443 ? 0.4137 0.4734 0.3573 -0.0511 0.0088  0.0024  445 PRO A C   
3195 O O   . PRO A 443 ? 0.3994 0.4670 0.3423 -0.0571 0.0096  -0.0001 445 PRO A O   
3196 C CB  . PRO A 443 ? 0.4584 0.4823 0.3751 -0.0518 0.0131  -0.0006 445 PRO A CB  
3197 C CG  . PRO A 443 ? 0.4833 0.4987 0.3899 -0.0596 0.0154  -0.0042 445 PRO A CG  
3198 C CD  . PRO A 443 ? 0.4532 0.4722 0.3704 -0.0549 0.0135  -0.0024 445 PRO A CD  
3199 N N   . ASN A 444 ? 0.4220 0.4895 0.3719 -0.0472 0.0072  0.0052  446 ASN A N   
3200 C CA  . ASN A 444 ? 0.4323 0.5178 0.3894 -0.0484 0.0059  0.0058  446 ASN A CA  
3201 C C   . ASN A 444 ? 0.4365 0.5221 0.3874 -0.0514 0.0072  0.0049  446 ASN A C   
3202 O O   . ASN A 444 ? 0.4150 0.4943 0.3651 -0.0470 0.0068  0.0070  446 ASN A O   
3203 C CB  . ASN A 444 ? 0.4238 0.5173 0.3926 -0.0411 0.0028  0.0103  446 ASN A CB  
3204 C CG  . ASN A 444 ? 0.4006 0.4922 0.3741 -0.0380 0.0016  0.0111  446 ASN A CG  
3205 O OD1 . ASN A 444 ? 0.4153 0.5003 0.3920 -0.0335 0.0003  0.0139  446 ASN A OD1 
3206 N ND2 . ASN A 444 ? 0.3820 0.4801 0.3551 -0.0411 0.0021  0.0083  446 ASN A ND2 
3207 N N   . THR A 445 ? 0.4515 0.5455 0.3977 -0.0591 0.0089  0.0015  447 THR A N   
3208 C CA  . THR A 445 ? 0.4648 0.5599 0.4043 -0.0631 0.0103  0.0000  447 THR A CA  
3209 C C   . THR A 445 ? 0.4583 0.5634 0.4083 -0.0560 0.0076  0.0044  447 THR A C   
3210 O O   . THR A 445 ? 0.4929 0.5925 0.4386 -0.0550 0.0082  0.0049  447 THR A O   
3211 C CB  . THR A 445 ? 0.4681 0.5757 0.4027 -0.0735 0.0122  -0.0044 447 THR A CB  
3212 O OG1 . THR A 445 ? 0.4443 0.5389 0.3649 -0.0825 0.0155  -0.0088 447 THR A OG1 
3213 C CG2 . THR A 445 ? 0.4882 0.6013 0.4187 -0.0771 0.0131  -0.0054 447 THR A CG2 
3214 N N   . THR B 27  ? 1.0593 0.9378 1.0130 -0.0043 0.0977  -0.0890 29  THR B N   
3215 C CA  . THR B 27  ? 1.0314 0.9185 0.9955 -0.0099 0.0963  -0.0842 29  THR B CA  
3216 C C   . THR B 27  ? 1.0138 0.8958 0.9710 -0.0018 0.0985  -0.0721 29  THR B C   
3217 O O   . THR B 27  ? 1.0652 0.9322 1.0088 0.0063  0.1034  -0.0686 29  THR B O   
3218 C CB  . THR B 27  ? 1.0387 0.9153 1.0079 -0.0225 0.1012  -0.0915 29  THR B CB  
3219 O OG1 . THR B 27  ? 1.0624 0.9110 1.0185 -0.0224 0.1105  -0.0916 29  THR B OG1 
3220 C CG2 . THR B 27  ? 1.0198 0.9064 0.9982 -0.0316 0.0982  -0.1036 29  THR B CG2 
3221 N N   . TYR B 28  ? 0.9431 0.8374 0.9084 -0.0035 0.0949  -0.0660 30  TYR B N   
3222 C CA  . TYR B 28  ? 0.8981 0.7948 0.8589 0.0042  0.0944  -0.0545 30  TYR B CA  
3223 C C   . TYR B 28  ? 0.9121 0.8024 0.8757 -0.0007 0.0972  -0.0515 30  TYR B C   
3224 O O   . TYR B 28  ? 0.8883 0.7784 0.8600 -0.0102 0.0979  -0.0576 30  TYR B O   
3225 C CB  . TYR B 28  ? 0.8633 0.7843 0.8304 0.0079  0.0854  -0.0492 30  TYR B CB  
3226 C CG  . TYR B 28  ? 0.8516 0.7810 0.8163 0.0132  0.0826  -0.0516 30  TYR B CG  
3227 C CD1 . TYR B 28  ? 0.8622 0.7870 0.8156 0.0236  0.0852  -0.0471 30  TYR B CD1 
3228 C CD2 . TYR B 28  ? 0.8302 0.7728 0.8033 0.0090  0.0773  -0.0582 30  TYR B CD2 
3229 C CE1 . TYR B 28  ? 0.8586 0.7916 0.8091 0.0294  0.0827  -0.0490 30  TYR B CE1 
3230 C CE2 . TYR B 28  ? 0.8321 0.7826 0.8025 0.0145  0.0748  -0.0603 30  TYR B CE2 
3231 C CZ  . TYR B 28  ? 0.8458 0.7912 0.8050 0.0246  0.0775  -0.0557 30  TYR B CZ  
3232 O OH  . TYR B 28  ? 0.8338 0.7877 0.7900 0.0307  0.0750  -0.0576 30  TYR B OH  
3233 N N   . THR B 29  ? 0.8997 0.7864 0.8564 0.0061  0.0989  -0.0423 31  THR B N   
3234 C CA  . THR B 29  ? 0.9055 0.7829 0.8615 0.0037  0.1028  -0.0387 31  THR B CA  
3235 C C   . THR B 29  ? 0.8768 0.7676 0.8338 0.0087  0.0974  -0.0292 31  THR B C   
3236 O O   . THR B 29  ? 0.8406 0.7311 0.7888 0.0179  0.0983  -0.0222 31  THR B O   
3237 C CB  . THR B 29  ? 0.9396 0.7913 0.8825 0.0068  0.1131  -0.0382 31  THR B CB  
3238 O OG1 . THR B 29  ? 0.9612 0.8005 0.9044 -0.0007 0.1175  -0.0480 31  THR B OG1 
3239 C CG2 . THR B 29  ? 0.9328 0.7753 0.8739 0.0057  0.1175  -0.0336 31  THR B CG2 
3240 N N   . ILE B 30  ? 0.8484 0.7498 0.8149 0.0027  0.0924  -0.0292 32  ILE B N   
3241 C CA  . ILE B 30  ? 0.7853 0.6967 0.7527 0.0050  0.0873  -0.0212 32  ILE B CA  
3242 C C   . ILE B 30  ? 0.7589 0.6558 0.7204 0.0062  0.0934  -0.0179 32  ILE B C   
3243 O O   . ILE B 30  ? 0.7183 0.6044 0.6820 0.0004  0.0985  -0.0226 32  ILE B O   
3244 C CB  . ILE B 30  ? 0.7527 0.6793 0.7304 -0.0009 0.0792  -0.0230 32  ILE B CB  
3245 C CG1 . ILE B 30  ? 0.7375 0.6783 0.7195 -0.0008 0.0734  -0.0253 32  ILE B CG1 
3246 C CG2 . ILE B 30  ? 0.7288 0.6610 0.7053 0.0005  0.0747  -0.0155 32  ILE B CG2 
3247 C CD1 . ILE B 30  ? 0.7084 0.6608 0.6993 -0.0067 0.0670  -0.0292 32  ILE B CD1 
3248 N N   . GLN B 31  ? 0.7456 0.6434 0.6998 0.0139  0.0933  -0.0098 33  GLN B N   
3249 C CA  . GLN B 31  ? 0.7520 0.6399 0.7001 0.0167  0.0974  -0.0050 33  GLN B CA  
3250 C C   . GLN B 31  ? 0.6750 0.5768 0.6284 0.0146  0.0893  -0.0012 33  GLN B C   
3251 O O   . GLN B 31  ? 0.6421 0.5593 0.5964 0.0169  0.0822  0.0030  33  GLN B O   
3252 C CB  . GLN B 31  ? 0.8147 0.6963 0.7504 0.0276  0.1019  0.0013  33  GLN B CB  
3253 C CG  . GLN B 31  ? 0.8375 0.7072 0.7656 0.0320  0.1082  -0.0015 33  GLN B CG  
3254 C CD  . GLN B 31  ? 0.8897 0.7350 0.8127 0.0287  0.1181  -0.0062 33  GLN B CD  
3255 O OE1 . GLN B 31  ? 0.8872 0.7230 0.8083 0.0272  0.1222  -0.0044 33  GLN B OE1 
3256 N NE2 . GLN B 31  ? 0.9051 0.7399 0.8254 0.0269  0.1220  -0.0124 33  GLN B NE2 
3257 N N   . LEU B 32  ? 0.6288 0.5253 0.5851 0.0099  0.0903  -0.0029 34  LEU B N   
3258 C CA  . LEU B 32  ? 0.6024 0.5088 0.5621 0.0076  0.0828  -0.0003 34  LEU B CA  
3259 C C   . LEU B 32  ? 0.5850 0.4850 0.5369 0.0128  0.0852  0.0056  34  LEU B C   
3260 O O   . LEU B 32  ? 0.6112 0.4993 0.5615 0.0118  0.0911  0.0043  34  LEU B O   
3261 C CB  . LEU B 32  ? 0.6145 0.5207 0.5822 0.0000  0.0821  -0.0067 34  LEU B CB  
3262 C CG  . LEU B 32  ? 0.6114 0.5268 0.5821 -0.0024 0.0739  -0.0055 34  LEU B CG  
3263 C CD1 . LEU B 32  ? 0.6221 0.5514 0.5945 -0.0026 0.0651  -0.0033 34  LEU B CD1 
3264 C CD2 . LEU B 32  ? 0.6269 0.5422 0.6045 -0.0082 0.0746  -0.0122 34  LEU B CD2 
3265 N N   . SER B 33  ? 0.5434 0.4520 0.4906 0.0182  0.0809  0.0120  35  SER B N   
3266 C CA  . SER B 33  ? 0.5541 0.4577 0.4924 0.0250  0.0836  0.0179  35  SER B CA  
3267 C C   . SER B 33  ? 0.5331 0.4401 0.4722 0.0222  0.0778  0.0193  35  SER B C   
3268 O O   . SER B 33  ? 0.5097 0.4255 0.4550 0.0161  0.0701  0.0172  35  SER B O   
3269 C CB  . SER B 33  ? 0.5553 0.4683 0.4877 0.0327  0.0822  0.0238  35  SER B CB  
3270 O OG  . SER B 33  ? 0.5349 0.4666 0.4720 0.0296  0.0723  0.0260  35  SER B OG  
3271 N N   . GLY B 34  ? 0.5471 0.4464 0.4787 0.0275  0.0815  0.0229  36  GLY B N   
3272 C CA  . GLY B 34  ? 0.5291 0.4294 0.4586 0.0269  0.0768  0.0247  36  GLY B CA  
3273 C C   . GLY B 34  ? 0.5297 0.4223 0.4637 0.0213  0.0783  0.0197  36  GLY B C   
3274 O O   . GLY B 34  ? 0.5184 0.4141 0.4523 0.0191  0.0720  0.0198  36  GLY B O   
3275 N N   . THR B 35  ? 0.5275 0.4111 0.4651 0.0188  0.0862  0.0154  37  THR B N   
3276 C CA  . THR B 35  ? 0.5350 0.4134 0.4775 0.0137  0.0888  0.0106  37  THR B CA  
3277 C C   . THR B 35  ? 0.5691 0.4354 0.5047 0.0180  0.0962  0.0134  37  THR B C   
3278 O O   . THR B 35  ? 0.5971 0.4569 0.5240 0.0251  0.1008  0.0183  37  THR B O   
3279 C CB  . THR B 35  ? 0.5253 0.4016 0.4754 0.0078  0.0936  0.0043  37  THR B CB  
3280 O OG1 . THR B 35  ? 0.5403 0.4048 0.4853 0.0109  0.1028  0.0053  37  THR B OG1 
3281 C CG2 . THR B 35  ? 0.5158 0.4046 0.4725 0.0041  0.0861  0.0014  37  THR B CG2 
3282 N N   . SER B 36  ? 0.5652 0.4297 0.5042 0.0146  0.0974  0.0104  38  SER B N   
3283 C CA  . SER B 36  ? 0.5801 0.4337 0.5145 0.0172  0.1057  0.0120  38  SER B CA  
3284 C C   . SER B 36  ? 0.5958 0.4462 0.5382 0.0100  0.1128  0.0063  38  SER B C   
3285 O O   . SER B 36  ? 0.5278 0.3856 0.4786 0.0040  0.1098  0.0011  38  SER B O   
3286 C CB  . SER B 36  ? 0.5605 0.4172 0.4911 0.0203  0.1001  0.0141  38  SER B CB  
3287 O OG  . SER B 36  ? 0.5439 0.4073 0.4814 0.0152  0.0960  0.0094  38  SER B OG  
3288 N N   . GLU B 37  ? 0.6407 0.4811 0.5803 0.0105  0.1220  0.0073  39  GLU B N   
3289 C CA  . GLU B 37  ? 0.6602 0.5004 0.6082 0.0025  0.1285  0.0019  39  GLU B CA  
3290 C C   . GLU B 37  ? 0.6011 0.4549 0.5551 0.0007  0.1211  -0.0009 39  GLU B C   
3291 O O   . GLU B 37  ? 0.5707 0.4282 0.5195 0.0064  0.1131  0.0023  39  GLU B O   
3292 C CB  . GLU B 37  ? 0.7328 0.5589 0.6756 0.0031  0.1408  0.0045  39  GLU B CB  
3293 C CG  . GLU B 37  ? 0.7944 0.6036 0.7290 0.0053  0.1494  0.0073  39  GLU B CG  
3294 C CD  . GLU B 37  ? 0.8551 0.6494 0.7877 0.0008  0.1628  0.0071  39  GLU B CD  
3295 O OE1 . GLU B 37  ? 0.8802 0.6762 0.8218 -0.0095 0.1661  0.0008  39  GLU B OE1 
3296 O OE2 . GLU B 37  ? 0.8785 0.6597 0.8004 0.0072  0.1700  0.0131  39  GLU B OE2 
3297 N N   . GLY B 38  ? 0.5800 0.4410 0.5439 -0.0065 0.1233  -0.0069 40  GLY B N   
3298 C CA  . GLY B 38  ? 0.5798 0.4536 0.5487 -0.0071 0.1180  -0.0097 40  GLY B CA  
3299 C C   . GLY B 38  ? 0.5687 0.4564 0.5464 -0.0117 0.1105  -0.0158 40  GLY B C   
3300 O O   . GLY B 38  ? 0.5775 0.4764 0.5610 -0.0136 0.1088  -0.0196 40  GLY B O   
3301 N N   . HIS B 39  ? 0.5569 0.4447 0.5355 -0.0130 0.1066  -0.0167 41  HIS B N   
3302 C CA  . HIS B 39  ? 0.5230 0.4235 0.5077 -0.0155 0.0981  -0.0212 41  HIS B CA  
3303 C C   . HIS B 39  ? 0.5243 0.4295 0.5186 -0.0232 0.1024  -0.0280 41  HIS B C   
3304 O O   . HIS B 39  ? 0.5389 0.4341 0.5325 -0.0260 0.1098  -0.0281 41  HIS B O   
3305 C CB  . HIS B 39  ? 0.5030 0.4024 0.4821 -0.0116 0.0902  -0.0173 41  HIS B CB  
3306 C CG  . HIS B 39  ? 0.4858 0.3802 0.4550 -0.0051 0.0860  -0.0110 41  HIS B CG  
3307 N ND1 . HIS B 39  ? 0.4595 0.3588 0.4252 -0.0029 0.0760  -0.0097 41  HIS B ND1 
3308 C CD2 . HIS B 39  ? 0.5268 0.4112 0.4883 -0.0005 0.0905  -0.0059 41  HIS B CD2 
3309 C CE1 . HIS B 39  ? 0.5022 0.3952 0.4586 0.0020  0.0741  -0.0045 41  HIS B CE1 
3310 N NE2 . HIS B 39  ? 0.5255 0.4101 0.4794 0.0042  0.0830  -0.0020 41  HIS B NE2 
3311 N N   . TYR B 40  ? 0.5145 0.4340 0.5164 -0.0261 0.0975  -0.0336 42  TYR B N   
3312 C CA  . TYR B 40  ? 0.5264 0.4535 0.5371 -0.0327 0.0981  -0.0406 42  TYR B CA  
3313 C C   . TYR B 40  ? 0.4891 0.4228 0.4992 -0.0300 0.0886  -0.0407 42  TYR B C   
3314 O O   . TYR B 40  ? 0.4978 0.4422 0.5092 -0.0279 0.0817  -0.0420 42  TYR B O   
3315 C CB  . TYR B 40  ? 0.5611 0.5015 0.5811 -0.0377 0.1006  -0.0470 42  TYR B CB  
3316 C CG  . TYR B 40  ? 0.6231 0.5564 0.6443 -0.0421 0.1114  -0.0467 42  TYR B CG  
3317 C CD1 . TYR B 40  ? 0.6570 0.5825 0.6811 -0.0499 0.1193  -0.0501 42  TYR B CD1 
3318 C CD2 . TYR B 40  ? 0.6421 0.5742 0.6597 -0.0383 0.1139  -0.0426 42  TYR B CD2 
3319 C CE1 . TYR B 40  ? 0.6901 0.6067 0.7140 -0.0547 0.1298  -0.0493 42  TYR B CE1 
3320 C CE2 . TYR B 40  ? 0.6765 0.6018 0.6947 -0.0424 0.1243  -0.0417 42  TYR B CE2 
3321 C CZ  . TYR B 40  ? 0.7162 0.6335 0.7376 -0.0510 0.1324  -0.0449 42  TYR B CZ  
3322 O OH  . TYR B 40  ? 0.7689 0.6781 0.7903 -0.0562 0.1432  -0.0440 42  TYR B OH  
3323 N N   . TYR B 41  ? 0.4612 0.3883 0.4686 -0.0297 0.0887  -0.0391 43  TYR B N   
3324 C CA  . TYR B 41  ? 0.4196 0.3526 0.4260 -0.0273 0.0805  -0.0383 43  TYR B CA  
3325 C C   . TYR B 41  ? 0.4256 0.3689 0.4402 -0.0320 0.0797  -0.0460 43  TYR B C   
3326 O O   . TYR B 41  ? 0.4462 0.3852 0.4639 -0.0366 0.0861  -0.0501 43  TYR B O   
3327 C CB  . TYR B 41  ? 0.4030 0.3262 0.4023 -0.0239 0.0814  -0.0326 43  TYR B CB  
3328 C CG  . TYR B 41  ? 0.3939 0.3112 0.3847 -0.0184 0.0791  -0.0248 43  TYR B CG  
3329 C CD1 . TYR B 41  ? 0.3663 0.2898 0.3544 -0.0159 0.0701  -0.0221 43  TYR B CD1 
3330 C CD2 . TYR B 41  ? 0.3847 0.2894 0.3691 -0.0156 0.0857  -0.0204 43  TYR B CD2 
3331 C CE1 . TYR B 41  ? 0.3690 0.2872 0.3489 -0.0117 0.0674  -0.0157 43  TYR B CE1 
3332 C CE2 . TYR B 41  ? 0.3814 0.2823 0.3578 -0.0102 0.0831  -0.0138 43  TYR B CE2 
3333 C CZ  . TYR B 41  ? 0.3660 0.2739 0.3406 -0.0087 0.0738  -0.0117 43  TYR B CZ  
3334 O OH  . TYR B 41  ? 0.3510 0.2554 0.3175 -0.0043 0.0705  -0.0058 43  TYR B OH  
3335 N N   . GLU B 42  ? 0.4119 0.3675 0.4289 -0.0305 0.0718  -0.0476 44  GLU B N   
3336 C CA  . GLU B 42  ? 0.4131 0.3812 0.4376 -0.0337 0.0697  -0.0551 44  GLU B CA  
3337 C C   . GLU B 42  ? 0.4090 0.3788 0.4310 -0.0313 0.0646  -0.0532 44  GLU B C   
3338 O O   . GLU B 42  ? 0.3885 0.3573 0.4046 -0.0269 0.0588  -0.0469 44  GLU B O   
3339 C CB  . GLU B 42  ? 0.4207 0.4023 0.4485 -0.0324 0.0649  -0.0582 44  GLU B CB  
3340 C CG  . GLU B 42  ? 0.4466 0.4317 0.4793 -0.0357 0.0705  -0.0619 44  GLU B CG  
3341 C CD  . GLU B 42  ? 0.4588 0.4589 0.4941 -0.0329 0.0660  -0.0650 44  GLU B CD  
3342 O OE1 . GLU B 42  ? 0.4444 0.4478 0.4750 -0.0276 0.0583  -0.0630 44  GLU B OE1 
3343 O OE2 . GLU B 42  ? 0.5077 0.5158 0.5488 -0.0358 0.0704  -0.0691 44  GLU B OE2 
3344 N N   . VAL B 43  ? 0.4143 0.3873 0.4407 -0.0343 0.0666  -0.0589 45  VAL B N   
3345 C CA  . VAL B 43  ? 0.4044 0.3798 0.4288 -0.0316 0.0627  -0.0576 45  VAL B CA  
3346 C C   . VAL B 43  ? 0.3885 0.3787 0.4191 -0.0328 0.0586  -0.0647 45  VAL B C   
3347 O O   . VAL B 43  ? 0.4044 0.3980 0.4408 -0.0375 0.0623  -0.0726 45  VAL B O   
3348 C CB  . VAL B 43  ? 0.4190 0.3826 0.4399 -0.0320 0.0687  -0.0570 45  VAL B CB  
3349 C CG1 . VAL B 43  ? 0.4127 0.3792 0.4298 -0.0274 0.0644  -0.0532 45  VAL B CG1 
3350 C CG2 . VAL B 43  ? 0.4351 0.3842 0.4500 -0.0308 0.0741  -0.0510 45  VAL B CG2 
3351 N N   . TYR B 44  ? 0.3707 0.3692 0.3994 -0.0288 0.0512  -0.0619 46  TYR B N   
3352 C CA  . TYR B 44  ? 0.3784 0.3920 0.4117 -0.0282 0.0466  -0.0678 46  TYR B CA  
3353 C C   . TYR B 44  ? 0.3727 0.3889 0.4045 -0.0261 0.0443  -0.0672 46  TYR B C   
3354 O O   . TYR B 44  ? 0.3671 0.3795 0.3930 -0.0227 0.0414  -0.0594 46  TYR B O   
3355 C CB  . TYR B 44  ? 0.3700 0.3893 0.4004 -0.0245 0.0404  -0.0650 46  TYR B CB  
3356 C CG  . TYR B 44  ? 0.3835 0.4035 0.4160 -0.0257 0.0429  -0.0673 46  TYR B CG  
3357 C CD1 . TYR B 44  ? 0.3913 0.4250 0.4311 -0.0273 0.0435  -0.0755 46  TYR B CD1 
3358 C CD2 . TYR B 44  ? 0.3884 0.3968 0.4159 -0.0251 0.0446  -0.0614 46  TYR B CD2 
3359 C CE1 . TYR B 44  ? 0.3987 0.4355 0.4406 -0.0279 0.0458  -0.0773 46  TYR B CE1 
3360 C CE2 . TYR B 44  ? 0.3958 0.4055 0.4246 -0.0254 0.0469  -0.0631 46  TYR B CE2 
3361 C CZ  . TYR B 44  ? 0.3993 0.4236 0.4354 -0.0267 0.0476  -0.0708 46  TYR B CZ  
3362 O OH  . TYR B 44  ? 0.4105 0.4381 0.4482 -0.0266 0.0502  -0.0722 46  TYR B OH  
3363 N N   . HIS B 45  ? 0.3792 0.4027 0.4161 -0.0281 0.0455  -0.0753 47  HIS B N   
3364 C CA  . HIS B 45  ? 0.3837 0.4115 0.4192 -0.0252 0.0433  -0.0760 47  HIS B CA  
3365 C C   . HIS B 45  ? 0.3557 0.3965 0.3906 -0.0208 0.0359  -0.0746 47  HIS B C   
3366 O O   . HIS B 45  ? 0.3520 0.4041 0.3916 -0.0212 0.0341  -0.0812 47  HIS B O   
3367 C CB  . HIS B 45  ? 0.4263 0.4563 0.4666 -0.0292 0.0470  -0.0861 47  HIS B CB  
3368 C CG  . HIS B 45  ? 0.4511 0.4795 0.4877 -0.0261 0.0469  -0.0861 47  HIS B CG  
3369 N ND1 . HIS B 45  ? 0.4899 0.5187 0.5286 -0.0289 0.0496  -0.0953 47  HIS B ND1 
3370 C CD2 . HIS B 45  ? 0.4581 0.4851 0.4887 -0.0204 0.0445  -0.0783 47  HIS B CD2 
3371 C CE1 . HIS B 45  ? 0.5039 0.5310 0.5373 -0.0240 0.0488  -0.0931 47  HIS B CE1 
3372 N NE2 . HIS B 45  ? 0.4895 0.5165 0.5184 -0.0186 0.0458  -0.0824 47  HIS B NE2 
3373 N N   . ILE B 46  ? 0.3307 0.3698 0.3596 -0.0169 0.0322  -0.0659 48  ILE B N   
3374 C CA  . ILE B 46  ? 0.3160 0.3638 0.3418 -0.0128 0.0255  -0.0625 48  ILE B CA  
3375 C C   . ILE B 46  ? 0.3240 0.3812 0.3503 -0.0098 0.0237  -0.0646 48  ILE B C   
3376 O O   . ILE B 46  ? 0.3230 0.3914 0.3508 -0.0072 0.0203  -0.0689 48  ILE B O   
3377 C CB  . ILE B 46  ? 0.2978 0.3379 0.3164 -0.0118 0.0226  -0.0518 48  ILE B CB  
3378 C CG1 . ILE B 46  ? 0.2926 0.3222 0.3097 -0.0143 0.0246  -0.0495 48  ILE B CG1 
3379 C CG2 . ILE B 46  ? 0.2996 0.3460 0.3137 -0.0085 0.0163  -0.0483 48  ILE B CG2 
3380 C CD1 . ILE B 46  ? 0.2890 0.3214 0.3087 -0.0147 0.0247  -0.0553 48  ILE B CD1 
3381 N N   . PHE B 47  ? 0.3297 0.3832 0.3540 -0.0089 0.0257  -0.0612 49  PHE B N   
3382 C CA  . PHE B 47  ? 0.3347 0.3967 0.3587 -0.0052 0.0246  -0.0632 49  PHE B CA  
3383 C C   . PHE B 47  ? 0.3728 0.4291 0.3982 -0.0065 0.0301  -0.0694 49  PHE B C   
3384 O O   . PHE B 47  ? 0.3828 0.4269 0.4059 -0.0081 0.0346  -0.0663 49  PHE B O   
3385 C CB  . PHE B 47  ? 0.3103 0.3740 0.3288 -0.0017 0.0220  -0.0529 49  PHE B CB  
3386 C CG  . PHE B 47  ? 0.2888 0.3560 0.3037 -0.0010 0.0165  -0.0459 49  PHE B CG  
3387 C CD1 . PHE B 47  ? 0.2865 0.3598 0.3017 0.0003  0.0130  -0.0497 49  PHE B CD1 
3388 C CD2 . PHE B 47  ? 0.2730 0.3375 0.2831 -0.0013 0.0149  -0.0355 49  PHE B CD2 
3389 C CE1 . PHE B 47  ? 0.2806 0.3539 0.2901 0.0014  0.0084  -0.0428 49  PHE B CE1 
3390 C CE2 . PHE B 47  ? 0.2632 0.3291 0.2687 -0.0016 0.0100  -0.0290 49  PHE B CE2 
3391 C CZ  . PHE B 47  ? 0.2641 0.3327 0.2684 0.0000  0.0069  -0.0326 49  PHE B CZ  
3392 N N   . SER B 48  ? 0.4091 0.4732 0.4372 -0.0055 0.0298  -0.0781 50  SER B N   
3393 C CA  . SER B 48  ? 0.4473 0.5061 0.4740 -0.0053 0.0340  -0.0838 50  SER B CA  
3394 C C   . SER B 48  ? 0.4765 0.5408 0.4980 0.0017  0.0318  -0.0783 50  SER B C   
3395 O O   . SER B 48  ? 0.4834 0.5591 0.5043 0.0054  0.0268  -0.0733 50  SER B O   
3396 C CB  . SER B 48  ? 0.4513 0.5158 0.4830 -0.0086 0.0345  -0.0967 50  SER B CB  
3397 O OG  . SER B 48  ? 0.4202 0.5017 0.4541 -0.0047 0.0288  -0.0992 50  SER B OG  
3398 N N   . GLY B 49  ? 0.5208 0.5766 0.5375 0.0040  0.0359  -0.0787 51  GLY B N   
3399 C CA  . GLY B 49  ? 0.5374 0.5991 0.5486 0.0117  0.0346  -0.0739 51  GLY B CA  
3400 C C   . GLY B 49  ? 0.5741 0.6231 0.5785 0.0145  0.0401  -0.0756 51  GLY B C   
3401 O O   . GLY B 49  ? 0.5817 0.6156 0.5854 0.0098  0.0451  -0.0806 51  GLY B O   
3402 N N   . THR B 50  ? 0.6029 0.6575 0.6016 0.0225  0.0395  -0.0715 52  THR B N   
3403 C CA  . THR B 50  ? 0.6208 0.6637 0.6104 0.0281  0.0445  -0.0713 52  THR B CA  
3404 C C   . THR B 50  ? 0.6318 0.6776 0.6176 0.0328  0.0449  -0.0582 52  THR B C   
3405 O O   . THR B 50  ? 0.5835 0.6450 0.5721 0.0346  0.0404  -0.0503 52  THR B O   
3406 C CB  . THR B 50  ? 0.6122 0.6592 0.5974 0.0338  0.0438  -0.0785 52  THR B CB  
3407 O OG1 . THR B 50  ? 0.5796 0.6466 0.5671 0.0388  0.0384  -0.0723 52  THR B OG1 
3408 C CG2 . THR B 50  ? 0.6014 0.6437 0.5902 0.0274  0.0440  -0.0924 52  THR B CG2 
3409 N N   . LEU B 51  ? 0.7203 0.7508 0.7003 0.0337  0.0503  -0.0562 53  LEU B N   
3410 C CA  . LEU B 51  ? 0.7859 0.8186 0.7615 0.0387  0.0515  -0.0446 53  LEU B CA  
3411 C C   . LEU B 51  ? 0.9079 0.9388 0.8731 0.0494  0.0546  -0.0436 53  LEU B C   
3412 O O   . LEU B 51  ? 0.9912 1.0035 0.9487 0.0512  0.0600  -0.0503 53  LEU B O   
3413 C CB  . LEU B 51  ? 0.7679 0.7849 0.7430 0.0339  0.0556  -0.0433 53  LEU B CB  
3414 C CG  . LEU B 51  ? 0.7464 0.7695 0.7206 0.0360  0.0548  -0.0315 53  LEU B CG  
3415 C CD1 . LEU B 51  ? 0.7120 0.7508 0.6946 0.0306  0.0480  -0.0266 53  LEU B CD1 
3416 C CD2 . LEU B 51  ? 0.7466 0.7517 0.7173 0.0337  0.0601  -0.0311 53  LEU B CD2 
3417 N N   . ASP B 52  ? 0.9670 1.0162 0.9312 0.0563  0.0515  -0.0361 54  ASP B N   
3418 C CA  . ASP B 52  ? 1.0175 1.0696 0.9724 0.0676  0.0533  -0.0364 54  ASP B CA  
3419 C C   . ASP B 52  ? 1.0503 1.0995 0.9964 0.0757  0.0575  -0.0279 54  ASP B C   
3420 O O   . ASP B 52  ? 1.0313 1.0770 0.9798 0.0715  0.0584  -0.0225 54  ASP B O   
3421 C CB  . ASP B 52  ? 1.0356 1.1110 0.9942 0.0712  0.0480  -0.0329 54  ASP B CB  
3422 C CG  . ASP B 52  ? 1.0245 1.1154 0.9926 0.0645  0.0431  -0.0245 54  ASP B CG  
3423 O OD1 . ASP B 52  ? 0.9520 1.0480 0.9197 0.0651  0.0436  -0.0150 54  ASP B OD1 
3424 O OD2 . ASP B 52  ? 1.0293 1.1251 1.0045 0.0583  0.0390  -0.0283 54  ASP B OD2 
3425 N N   . THR B 53  ? 1.0640 1.1156 1.0000 0.0876  0.0597  -0.0268 55  THR B N   
3426 C CA  . THR B 53  ? 1.0448 1.0985 0.9708 0.0989  0.0634  -0.0182 55  THR B CA  
3427 C C   . THR B 53  ? 1.0060 1.0831 0.9404 0.0964  0.0595  -0.0059 55  THR B C   
3428 O O   . THR B 53  ? 0.9640 1.0415 0.8935 0.1012  0.0622  0.0010  55  THR B O   
3429 C CB  . THR B 53  ? 1.0405 1.0951 0.9542 0.1127  0.0657  -0.0198 55  THR B CB  
3430 O OG1 . THR B 53  ? 1.0015 1.0835 0.9202 0.1165  0.0609  -0.0143 55  THR B OG1 
3431 C CG2 . THR B 53  ? 1.0378 1.0713 0.9450 0.1122  0.0677  -0.0331 55  THR B CG2 
3432 N N   . SER B 54  ? 0.9674 1.0615 0.9132 0.0886  0.0534  -0.0040 56  SER B N   
3433 C CA  . SER B 54  ? 0.8970 1.0128 0.8510 0.0839  0.0489  0.0068  56  SER B CA  
3434 C C   . SER B 54  ? 0.8259 0.9331 0.7859 0.0731  0.0478  0.0079  56  SER B C   
3435 O O   . SER B 54  ? 0.8161 0.9381 0.7799 0.0702  0.0450  0.0171  56  SER B O   
3436 C CB  . SER B 54  ? 0.8582 0.9926 0.8193 0.0806  0.0435  0.0084  56  SER B CB  
3437 O OG  . SER B 54  ? 0.8611 1.0121 0.8174 0.0914  0.0439  0.0124  56  SER B OG  
3438 N N   . ASN B 55  ? 0.8033 0.8896 0.7646 0.0666  0.0495  -0.0008 57  ASN B N   
3439 C CA  . ASN B 55  ? 0.8162 0.8939 0.7829 0.0568  0.0485  -0.0002 57  ASN B CA  
3440 C C   . ASN B 55  ? 0.7769 0.8662 0.7532 0.0474  0.0419  0.0016  57  ASN B C   
3441 O O   . ASN B 55  ? 0.7345 0.8198 0.7147 0.0398  0.0401  0.0038  57  ASN B O   
3442 C CB  . ASN B 55  ? 0.8186 0.8982 0.7818 0.0595  0.0503  0.0082  57  ASN B CB  
3443 C CG  . ASN B 55  ? 0.8133 0.8906 0.7825 0.0497  0.0475  0.0109  57  ASN B CG  
3444 O OD1 . ASN B 55  ? 0.8109 0.9041 0.7837 0.0465  0.0431  0.0190  57  ASN B OD1 
3445 N ND2 . ASN B 55  ? 0.7612 0.8186 0.7307 0.0448  0.0501  0.0043  57  ASN B ND2 
3446 N N   . THR B 56  ? 0.7229 0.8245 0.7017 0.0484  0.0386  0.0007  58  THR B N   
3447 C CA  . THR B 56  ? 0.6446 0.7517 0.6304 0.0403  0.0332  0.0000  58  THR B CA  
3448 C C   . THR B 56  ? 0.5857 0.6783 0.5734 0.0374  0.0344  -0.0119 58  THR B C   
3449 O O   . THR B 56  ? 0.5675 0.6494 0.5509 0.0419  0.0389  -0.0189 58  THR B O   
3450 C CB  . THR B 56  ? 0.6691 0.7966 0.6561 0.0428  0.0294  0.0057  58  THR B CB  
3451 O OG1 . THR B 56  ? 0.7014 0.8296 0.6865 0.0488  0.0304  -0.0013 58  THR B OG1 
3452 C CG2 . THR B 56  ? 0.6683 0.8125 0.6530 0.0474  0.0296  0.0166  58  THR B CG2 
3453 N N   . LEU B 57  ? 0.5307 0.6223 0.5238 0.0302  0.0308  -0.0144 59  LEU B N   
3454 C CA  . LEU B 57  ? 0.5054 0.5882 0.5014 0.0273  0.0313  -0.0259 59  LEU B CA  
3455 C C   . LEU B 57  ? 0.4618 0.5569 0.4597 0.0293  0.0274  -0.0288 59  LEU B C   
3456 O O   . LEU B 57  ? 0.4083 0.5133 0.4078 0.0274  0.0230  -0.0227 59  LEU B O   
3457 C CB  . LEU B 57  ? 0.4881 0.5626 0.4882 0.0193  0.0301  -0.0271 59  LEU B CB  
3458 C CG  . LEU B 57  ? 0.5060 0.5716 0.5095 0.0158  0.0317  -0.0387 59  LEU B CG  
3459 C CD1 . LEU B 57  ? 0.5296 0.5802 0.5300 0.0163  0.0381  -0.0436 59  LEU B CD1 
3460 C CD2 . LEU B 57  ? 0.5148 0.5773 0.5223 0.0093  0.0292  -0.0389 59  LEU B CD2 
3461 N N   . THR B 58  ? 0.4832 0.5760 0.4804 0.0323  0.0290  -0.0384 60  THR B N   
3462 C CA  . THR B 58  ? 0.5084 0.6141 0.5061 0.0364  0.0257  -0.0417 60  THR B CA  
3463 C C   . THR B 58  ? 0.5386 0.6405 0.5402 0.0329  0.0250  -0.0541 60  THR B C   
3464 O O   . THR B 58  ? 0.5458 0.6343 0.5485 0.0286  0.0285  -0.0609 60  THR B O   
3465 C CB  . THR B 58  ? 0.5147 0.6258 0.5064 0.0455  0.0275  -0.0412 60  THR B CB  
3466 O OG1 . THR B 58  ? 0.5120 0.6083 0.4990 0.0474  0.0328  -0.0468 60  THR B OG1 
3467 C CG2 . THR B 58  ? 0.5184 0.6415 0.5077 0.0495  0.0268  -0.0283 60  THR B CG2 
3468 N N   . ASN B 59  ? 0.5579 0.6720 0.5612 0.0351  0.0209  -0.0567 61  ASN B N   
3469 C CA  . ASN B 59  ? 0.5823 0.6977 0.5894 0.0332  0.0196  -0.0690 61  ASN B CA  
3470 C C   . ASN B 59  ? 0.5519 0.6600 0.5640 0.0252  0.0197  -0.0707 61  ASN B C   
3471 O O   . ASN B 59  ? 0.5411 0.6409 0.5562 0.0204  0.0225  -0.0796 61  ASN B O   
3472 C CB  . ASN B 59  ? 0.6123 0.7224 0.6168 0.0355  0.0228  -0.0792 61  ASN B CB  
3473 C CG  . ASN B 59  ? 0.6479 0.7636 0.6455 0.0447  0.0232  -0.0749 61  ASN B CG  
3474 O OD1 . ASN B 59  ? 0.6161 0.7457 0.6126 0.0498  0.0200  -0.0678 61  ASN B OD1 
3475 N ND2 . ASN B 59  ? 0.6650 0.7695 0.6568 0.0473  0.0275  -0.0784 61  ASN B ND2 
3476 N N   . ILE B 60  ? 0.5203 0.6314 0.5326 0.0239  0.0167  -0.0618 62  ILE B N   
3477 C CA  . ILE B 60  ? 0.5178 0.6214 0.5329 0.0176  0.0164  -0.0609 62  ILE B CA  
3478 C C   . ILE B 60  ? 0.5192 0.6299 0.5377 0.0171  0.0133  -0.0683 62  ILE B C   
3479 O O   . ILE B 60  ? 0.4578 0.5796 0.4743 0.0218  0.0093  -0.0669 62  ILE B O   
3480 C CB  . ILE B 60  ? 0.4947 0.5963 0.5065 0.0163  0.0146  -0.0483 62  ILE B CB  
3481 C CG1 . ILE B 60  ? 0.4806 0.5762 0.4900 0.0164  0.0180  -0.0419 62  ILE B CG1 
3482 C CG2 . ILE B 60  ? 0.4993 0.5943 0.5125 0.0113  0.0132  -0.0480 62  ILE B CG2 
3483 C CD1 . ILE B 60  ? 0.4696 0.5676 0.4759 0.0153  0.0157  -0.0296 62  ILE B CD1 
3484 N N   . GLU B 61  ? 0.5193 0.6245 0.5424 0.0120  0.0155  -0.0758 63  GLU B N   
3485 C CA  . GLU B 61  ? 0.5374 0.6495 0.5644 0.0108  0.0131  -0.0826 63  GLU B CA  
3486 C C   . GLU B 61  ? 0.4953 0.5978 0.5241 0.0054  0.0148  -0.0808 63  GLU B C   
3487 O O   . GLU B 61  ? 0.4522 0.5425 0.4805 0.0017  0.0186  -0.0775 63  GLU B O   
3488 C CB  . GLU B 61  ? 0.6182 0.7373 0.6501 0.0099  0.0143  -0.0957 63  GLU B CB  
3489 C CG  . GLU B 61  ? 0.6722 0.7994 0.7012 0.0159  0.0129  -0.0978 63  GLU B CG  
3490 C CD  . GLU B 61  ? 0.7819 0.9203 0.8151 0.0160  0.0119  -0.1111 63  GLU B CD  
3491 O OE1 . GLU B 61  ? 0.8581 0.9957 0.8972 0.0095  0.0138  -0.1196 63  GLU B OE1 
3492 O OE2 . GLU B 61  ? 0.8857 1.0345 0.9161 0.0225  0.0092  -0.1130 63  GLU B OE2 
3493 N N   . TRP B 62  ? 0.4543 0.5624 0.4839 0.0060  0.0119  -0.0824 64  TRP B N   
3494 C CA  . TRP B 62  ? 0.4209 0.5235 0.4529 0.0018  0.0133  -0.0836 64  TRP B CA  
3495 C C   . TRP B 62  ? 0.4412 0.5427 0.4805 -0.0040 0.0181  -0.0933 64  TRP B C   
3496 O O   . TRP B 62  ? 0.4417 0.5536 0.4853 -0.0041 0.0181  -0.1028 64  TRP B O   
3497 C CB  . TRP B 62  ? 0.4038 0.5159 0.4347 0.0058  0.0092  -0.0855 64  TRP B CB  
3498 C CG  . TRP B 62  ? 0.3750 0.4844 0.3969 0.0107  0.0049  -0.0758 64  TRP B CG  
3499 C CD1 . TRP B 62  ? 0.3711 0.4899 0.3886 0.0172  0.0010  -0.0753 64  TRP B CD1 
3500 C CD2 . TRP B 62  ? 0.3545 0.4502 0.3699 0.0090  0.0042  -0.0657 64  TRP B CD2 
3501 N NE1 . TRP B 62  ? 0.3737 0.4842 0.3819 0.0192  -0.0017 -0.0650 64  TRP B NE1 
3502 C CE2 . TRP B 62  ? 0.3575 0.4540 0.3644 0.0138  0.0000  -0.0593 64  TRP B CE2 
3503 C CE3 . TRP B 62  ? 0.3457 0.4284 0.3610 0.0040  0.0069  -0.0616 64  TRP B CE3 
3504 C CZ2 . TRP B 62  ? 0.3480 0.4322 0.3465 0.0126  -0.0020 -0.0493 64  TRP B CZ2 
3505 C CZ3 . TRP B 62  ? 0.3361 0.4083 0.3435 0.0035  0.0045  -0.0519 64  TRP B CZ3 
3506 C CH2 . TRP B 62  ? 0.3378 0.4105 0.3370 0.0072  0.0001  -0.0460 64  TRP B CH2 
3507 N N   . ALA B 63  ? 0.4463 0.5356 0.4865 -0.0090 0.0222  -0.0912 65  ALA B N   
3508 C CA  . ALA B 63  ? 0.4757 0.5605 0.5217 -0.0159 0.0278  -0.0988 65  ALA B CA  
3509 C C   . ALA B 63  ? 0.4905 0.5808 0.5413 -0.0188 0.0282  -0.1028 65  ALA B C   
3510 O O   . ALA B 63  ? 0.4583 0.5528 0.5065 -0.0148 0.0244  -0.0987 65  ALA B O   
3511 C CB  . ALA B 63  ? 0.4844 0.5517 0.5267 -0.0183 0.0325  -0.0928 65  ALA B CB  
3512 N N   . PRO B 64  ? 0.5152 0.6059 0.5728 -0.0259 0.0330  -0.1111 66  PRO B N   
3513 C CA  . PRO B 64  ? 0.5244 0.6264 0.5883 -0.0286 0.0333  -0.1166 66  PRO B CA  
3514 C C   . PRO B 64  ? 0.5185 0.6136 0.5791 -0.0270 0.0334  -0.1089 66  PRO B C   
3515 O O   . PRO B 64  ? 0.5238 0.6295 0.5874 -0.0263 0.0324  -0.1117 66  PRO B O   
3516 C CB  . PRO B 64  ? 0.5562 0.6553 0.6266 -0.0383 0.0396  -0.1253 66  PRO B CB  
3517 C CG  . PRO B 64  ? 0.5484 0.6403 0.6156 -0.0384 0.0404  -0.1273 66  PRO B CG  
3518 C CD  . PRO B 64  ? 0.5330 0.6134 0.5915 -0.0316 0.0385  -0.1155 66  PRO B CD  
3519 N N   . GLY B 65  ? 0.5034 0.5815 0.5573 -0.0260 0.0345  -0.0995 67  GLY B N   
3520 C CA  . GLY B 65  ? 0.4817 0.5510 0.5311 -0.0245 0.0345  -0.0920 67  GLY B CA  
3521 C C   . GLY B 65  ? 0.4557 0.5298 0.4988 -0.0173 0.0278  -0.0872 67  GLY B C   
3522 O O   . GLY B 65  ? 0.4686 0.5352 0.5068 -0.0156 0.0271  -0.0816 67  GLY B O   
3523 N N   . VAL B 66  ? 0.4189 0.5039 0.4611 -0.0128 0.0232  -0.0891 68  VAL B N   
3524 C CA  . VAL B 66  ? 0.4095 0.4978 0.4442 -0.0056 0.0173  -0.0848 68  VAL B CA  
3525 C C   . VAL B 66  ? 0.4203 0.5279 0.4592 -0.0020 0.0153  -0.0934 68  VAL B C   
3526 O O   . VAL B 66  ? 0.4555 0.5743 0.5009 -0.0038 0.0160  -0.1007 68  VAL B O   
3527 C CB  . VAL B 66  ? 0.3962 0.4796 0.4235 -0.0021 0.0135  -0.0776 68  VAL B CB  
3528 C CG1 . VAL B 66  ? 0.3906 0.4728 0.4081 0.0043  0.0081  -0.0724 68  VAL B CG1 
3529 C CG2 . VAL B 66  ? 0.3932 0.4617 0.4179 -0.0058 0.0158  -0.0701 68  VAL B CG2 
3530 N N   . THR B 67  ? 0.4352 0.5463 0.4690 0.0036  0.0124  -0.0922 69  THR B N   
3531 C CA  . THR B 67  ? 0.4628 0.5939 0.4992 0.0090  0.0101  -0.0996 69  THR B CA  
3532 C C   . THR B 67  ? 0.4672 0.6046 0.4981 0.0159  0.0053  -0.0989 69  THR B C   
3533 O O   . THR B 67  ? 0.4575 0.5819 0.4809 0.0168  0.0035  -0.0910 69  THR B O   
3534 C CB  . THR B 67  ? 0.4807 0.6123 0.5110 0.0149  0.0087  -0.0978 69  THR B CB  
3535 O OG1 . THR B 67  ? 0.4941 0.6100 0.5100 0.0208  0.0047  -0.0883 69  THR B OG1 
3536 C CG2 . THR B 67  ? 0.4873 0.6138 0.5224 0.0091  0.0136  -0.0981 69  THR B CG2 
3537 N N   . GLU B 68  ? 0.5018 0.6597 0.5361 0.0207  0.0033  -0.1068 70  GLU B N   
3538 C CA  . GLU B 68  ? 0.5277 0.6946 0.5563 0.0290  -0.0011 -0.1071 70  GLU B CA  
3539 C C   . GLU B 68  ? 0.5159 0.6695 0.5288 0.0373  -0.0048 -0.0973 70  GLU B C   
3540 O O   . GLU B 68  ? 0.5483 0.6978 0.5538 0.0413  -0.0076 -0.0924 70  GLU B O   
3541 C CB  . GLU B 68  ? 0.5668 0.7603 0.6025 0.0328  -0.0022 -0.1181 70  GLU B CB  
3542 C CG  . GLU B 68  ? 0.6170 0.8221 0.6495 0.0400  -0.0061 -0.1205 70  GLU B CG  
3543 C CD  . GLU B 68  ? 0.6649 0.8697 0.7028 0.0346  -0.0052 -0.1229 70  GLU B CD  
3544 O OE1 . GLU B 68  ? 0.6720 0.8615 0.7126 0.0264  -0.0019 -0.1196 70  GLU B OE1 
3545 O OE2 . GLU B 68  ? 0.7411 0.9615 0.7799 0.0396  -0.0078 -0.1285 70  GLU B OE2 
3546 N N   . ALA B 69  ? 0.5006 0.6478 0.5080 0.0397  -0.0047 -0.0947 71  ALA B N   
3547 C CA  . ALA B 69  ? 0.4967 0.6279 0.4874 0.0471  -0.0080 -0.0859 71  ALA B CA  
3548 C C   . ALA B 69  ? 0.4789 0.5885 0.4637 0.0416  -0.0083 -0.0762 71  ALA B C   
3549 O O   . ALA B 69  ? 0.4832 0.5835 0.4556 0.0464  -0.0116 -0.0696 71  ALA B O   
3550 C CB  . ALA B 69  ? 0.4984 0.6259 0.4857 0.0493  -0.0070 -0.0859 71  ALA B CB  
3551 N N   . GLY B 70  ? 0.4798 0.5818 0.4722 0.0322  -0.0048 -0.0751 72  GLY B N   
3552 C CA  . GLY B 70  ? 0.4624 0.5473 0.4514 0.0263  -0.0046 -0.0665 72  GLY B CA  
3553 C C   . GLY B 70  ? 0.4511 0.5414 0.4415 0.0262  -0.0057 -0.0654 72  GLY B C   
3554 O O   . GLY B 70  ? 0.4427 0.5228 0.4239 0.0268  -0.0082 -0.0570 72  GLY B O   
3555 N N   . ARG B 71  ? 0.4525 0.5587 0.4538 0.0252  -0.0039 -0.0735 73  ARG B N   
3556 C CA  . ARG B 71  ? 0.4644 0.5776 0.4669 0.0265  -0.0050 -0.0733 73  ARG B CA  
3557 C C   . ARG B 71  ? 0.4762 0.5899 0.4669 0.0349  -0.0093 -0.0688 73  ARG B C   
3558 O O   . ARG B 71  ? 0.4782 0.5857 0.4635 0.0346  -0.0105 -0.0613 73  ARG B O   
3559 C CB  . ARG B 71  ? 0.4654 0.5965 0.4793 0.0258  -0.0032 -0.0845 73  ARG B CB  
3560 C CG  . ARG B 71  ? 0.4710 0.5987 0.4948 0.0169  0.0016  -0.0886 73  ARG B CG  
3561 C CD  . ARG B 71  ? 0.4876 0.6316 0.5217 0.0149  0.0033  -0.1006 73  ARG B CD  
3562 N NE  . ARG B 71  ? 0.5011 0.6381 0.5426 0.0061  0.0084  -0.1035 73  ARG B NE  
3563 C CZ  . ARG B 71  ? 0.5115 0.6527 0.5608 0.0005  0.0117  -0.1114 73  ARG B CZ  
3564 N NH1 . ARG B 71  ? 0.5225 0.6758 0.5736 0.0031  0.0097  -0.1176 73  ARG B NH1 
3565 N NH2 . ARG B 71  ? 0.5081 0.6403 0.5623 -0.0073 0.0169  -0.1132 73  ARG B NH2 
3566 N N   . THR B 72  ? 0.5024 0.6233 0.4889 0.0422  -0.0112 -0.0727 74  THR B N   
3567 C CA  . THR B 72  ? 0.5241 0.6451 0.4976 0.0520  -0.0150 -0.0690 74  THR B CA  
3568 C C   . THR B 72  ? 0.5184 0.6162 0.4776 0.0509  -0.0165 -0.0574 74  THR B C   
3569 O O   . THR B 72  ? 0.5116 0.6037 0.4617 0.0531  -0.0184 -0.0505 74  THR B O   
3570 C CB  . THR B 72  ? 0.5602 0.6941 0.5316 0.0609  -0.0163 -0.0760 74  THR B CB  
3571 O OG1 . THR B 72  ? 0.5711 0.7280 0.5565 0.0602  -0.0150 -0.0874 74  THR B OG1 
3572 C CG2 . THR B 72  ? 0.5870 0.7202 0.5435 0.0722  -0.0197 -0.0723 74  THR B CG2 
3573 N N   . HIS B 73  ? 0.4838 0.5685 0.4412 0.0468  -0.0157 -0.0551 75  HIS B N   
3574 C CA  . HIS B 73  ? 0.4789 0.5405 0.4228 0.0443  -0.0174 -0.0449 75  HIS B CA  
3575 C C   . HIS B 73  ? 0.4446 0.5001 0.3898 0.0367  -0.0172 -0.0375 75  HIS B C   
3576 O O   . HIS B 73  ? 0.4636 0.5079 0.3968 0.0372  -0.0194 -0.0296 75  HIS B O   
3577 C CB  . HIS B 73  ? 0.4798 0.5311 0.4239 0.0406  -0.0161 -0.0452 75  HIS B CB  
3578 C CG  . HIS B 73  ? 0.4967 0.5250 0.4281 0.0367  -0.0181 -0.0356 75  HIS B CG  
3579 N ND1 . HIS B 73  ? 0.5538 0.5676 0.4670 0.0424  -0.0213 -0.0306 75  HIS B ND1 
3580 C CD2 . HIS B 73  ? 0.4918 0.5092 0.4250 0.0277  -0.0173 -0.0303 75  HIS B CD2 
3581 C CE1 . HIS B 73  ? 0.5453 0.5393 0.4498 0.0358  -0.0227 -0.0228 75  HIS B CE1 
3582 N NE2 . HIS B 73  ? 0.5120 0.5094 0.4293 0.0269  -0.0204 -0.0226 75  HIS B NE2 
3583 N N   . PHE B 74  ? 0.4119 0.4736 0.3702 0.0299  -0.0142 -0.0396 76  PHE B N   
3584 C CA  . PHE B 74  ? 0.4049 0.4617 0.3647 0.0229  -0.0137 -0.0323 76  PHE B CA  
3585 C C   . PHE B 74  ? 0.4031 0.4719 0.3645 0.0258  -0.0141 -0.0316 76  PHE B C   
3586 O O   . PHE B 74  ? 0.4044 0.4701 0.3639 0.0218  -0.0143 -0.0239 76  PHE B O   
3587 C CB  . PHE B 74  ? 0.3890 0.4464 0.3602 0.0161  -0.0100 -0.0347 76  PHE B CB  
3588 C CG  . PHE B 74  ? 0.3882 0.4318 0.3566 0.0122  -0.0095 -0.0326 76  PHE B CG  
3589 C CD1 . PHE B 74  ? 0.3862 0.4143 0.3442 0.0088  -0.0120 -0.0237 76  PHE B CD1 
3590 C CD2 . PHE B 74  ? 0.3809 0.4270 0.3568 0.0116  -0.0065 -0.0395 76  PHE B CD2 
3591 C CE1 . PHE B 74  ? 0.3877 0.4030 0.3421 0.0060  -0.0119 -0.0223 76  PHE B CE1 
3592 C CE2 . PHE B 74  ? 0.3830 0.4168 0.3557 0.0089  -0.0059 -0.0374 76  PHE B CE2 
3593 C CZ  . PHE B 74  ? 0.3773 0.3955 0.3389 0.0066  -0.0088 -0.0290 76  PHE B CZ  
3594 N N   . GLY B 75  ? 0.4081 0.4917 0.3729 0.0327  -0.0142 -0.0391 77  GLY B N   
3595 C CA  . GLY B 75  ? 0.4034 0.4994 0.3698 0.0363  -0.0145 -0.0391 77  GLY B CA  
3596 C C   . GLY B 75  ? 0.3939 0.4985 0.3724 0.0318  -0.0115 -0.0425 77  GLY B C   
3597 O O   . GLY B 75  ? 0.4009 0.5046 0.3878 0.0273  -0.0089 -0.0477 77  GLY B O   
3598 N N   . ASN B 76  ? 0.3970 0.5090 0.3757 0.0335  -0.0116 -0.0394 78  ASN B N   
3599 C CA  . ASN B 76  ? 0.3868 0.5086 0.3750 0.0324  -0.0089 -0.0442 78  ASN B CA  
3600 C C   . ASN B 76  ? 0.3579 0.4704 0.3505 0.0247  -0.0061 -0.0409 78  ASN B C   
3601 O O   . ASN B 76  ? 0.3601 0.4631 0.3474 0.0208  -0.0068 -0.0311 78  ASN B O   
3602 C CB  . ASN B 76  ? 0.4066 0.5376 0.3920 0.0369  -0.0097 -0.0401 78  ASN B CB  
3603 C CG  . ASN B 76  ? 0.4157 0.5546 0.4087 0.0365  -0.0069 -0.0442 78  ASN B CG  
3604 O OD1 . ASN B 76  ? 0.4002 0.5356 0.3938 0.0329  -0.0051 -0.0378 78  ASN B OD1 
3605 N ND2 . ASN B 76  ? 0.4369 0.5868 0.4346 0.0406  -0.0068 -0.0550 78  ASN B ND2 
3606 N N   . ALA B 77  ? 0.3375 0.4526 0.3387 0.0226  -0.0029 -0.0489 79  ALA B N   
3607 C CA  . ALA B 77  ? 0.3242 0.4301 0.3295 0.0164  0.0005  -0.0478 79  ALA B CA  
3608 C C   . ALA B 77  ? 0.3154 0.4211 0.3187 0.0157  0.0014  -0.0394 79  ALA B C   
3609 O O   . ALA B 77  ? 0.2994 0.3968 0.3008 0.0116  0.0019  -0.0321 79  ALA B O   
3610 C CB  . ALA B 77  ? 0.3283 0.4371 0.3415 0.0150  0.0040  -0.0587 79  ALA B CB  
3611 N N   . SER B 78  ? 0.3127 0.4290 0.3163 0.0204  0.0014  -0.0405 80  SER B N   
3612 C CA  . SER B 78  ? 0.3102 0.4300 0.3125 0.0213  0.0027  -0.0332 80  SER B CA  
3613 C C   . SER B 78  ? 0.3137 0.4328 0.3099 0.0196  0.0000  -0.0211 80  SER B C   
3614 O O   . SER B 78  ? 0.3199 0.4386 0.3156 0.0170  0.0011  -0.0135 80  SER B O   
3615 C CB  . SER B 78  ? 0.3238 0.4556 0.3269 0.0279  0.0032  -0.0380 80  SER B CB  
3616 O OG  . SER B 78  ? 0.3138 0.4473 0.3166 0.0292  0.0059  -0.0338 80  SER B OG  
3617 N N   . ASP B 79  ? 0.3322 0.4512 0.3233 0.0211  -0.0033 -0.0196 81  ASP B N   
3618 C CA  . ASP B 79  ? 0.3554 0.4709 0.3388 0.0185  -0.0060 -0.0085 81  ASP B CA  
3619 C C   . ASP B 79  ? 0.3496 0.4512 0.3313 0.0111  -0.0064 -0.0043 81  ASP B C   
3620 O O   . ASP B 79  ? 0.3514 0.4505 0.3294 0.0061  -0.0074 0.0053  81  ASP B O   
3621 C CB  . ASP B 79  ? 0.3822 0.4968 0.3584 0.0226  -0.0090 -0.0088 81  ASP B CB  
3622 C CG  . ASP B 79  ? 0.4218 0.5499 0.3968 0.0305  -0.0095 -0.0108 81  ASP B CG  
3623 O OD1 . ASP B 79  ? 0.4545 0.5930 0.4330 0.0325  -0.0078 -0.0097 81  ASP B OD1 
3624 O OD2 . ASP B 79  ? 0.4466 0.5747 0.4160 0.0356  -0.0116 -0.0131 81  ASP B OD2 
3625 N N   . LYS B 80  ? 0.3568 0.4505 0.3411 0.0100  -0.0056 -0.0113 82  LYS B N   
3626 C CA  . LYS B 80  ? 0.3412 0.4215 0.3233 0.0038  -0.0060 -0.0078 82  LYS B CA  
3627 C C   . LYS B 80  ? 0.3445 0.4260 0.3311 0.0001  -0.0033 -0.0040 82  LYS B C   
3628 O O   . LYS B 80  ? 0.3567 0.4332 0.3395 -0.0050 -0.0047 0.0041  82  LYS B O   
3629 C CB  . LYS B 80  ? 0.3374 0.4106 0.3214 0.0044  -0.0053 -0.0160 82  LYS B CB  
3630 C CG  . LYS B 80  ? 0.3331 0.3923 0.3138 -0.0008 -0.0057 -0.0126 82  LYS B CG  
3631 C CD  . LYS B 80  ? 0.3439 0.3938 0.3138 -0.0033 -0.0097 -0.0045 82  LYS B CD  
3632 C CE  . LYS B 80  ? 0.3629 0.3981 0.3285 -0.0071 -0.0106 -0.0035 82  LYS B CE  
3633 N NZ  . LYS B 80  ? 0.3837 0.4064 0.3367 -0.0101 -0.0147 0.0036  82  LYS B NZ  
3634 N N   . ALA B 81  ? 0.3437 0.4309 0.3370 0.0029  0.0003  -0.0099 83  ALA B N   
3635 C CA  . ALA B 81  ? 0.3441 0.4335 0.3403 0.0019  0.0034  -0.0067 83  ALA B CA  
3636 C C   . ALA B 81  ? 0.3579 0.4568 0.3512 0.0015  0.0018  0.0034  83  ALA B C   
3637 O O   . ALA B 81  ? 0.3716 0.4704 0.3643 -0.0018 0.0022  0.0100  83  ALA B O   
3638 C CB  . ALA B 81  ? 0.3517 0.4452 0.3528 0.0064  0.0073  -0.0147 83  ALA B CB  
3639 N N   . ALA B 82  ? 0.3755 0.4837 0.3668 0.0049  0.0001  0.0048  84  ALA B N   
3640 C CA  . ALA B 82  ? 0.3918 0.5112 0.3809 0.0043  -0.0009 0.0148  84  ALA B CA  
3641 C C   . ALA B 82  ? 0.3987 0.5118 0.3830 -0.0038 -0.0038 0.0237  84  ALA B C   
3642 O O   . ALA B 82  ? 0.4112 0.5319 0.3962 -0.0070 -0.0035 0.0314  84  ALA B O   
3643 C CB  . ALA B 82  ? 0.3878 0.5170 0.3747 0.0096  -0.0021 0.0147  84  ALA B CB  
3644 N N   . SER B 83  ? 0.4096 0.5099 0.3886 -0.0069 -0.0067 0.0229  85  SER B N   
3645 C CA  . SER B 83  ? 0.4364 0.5272 0.4086 -0.0153 -0.0099 0.0307  85  SER B CA  
3646 C C   . SER B 83  ? 0.4129 0.4987 0.3876 -0.0202 -0.0093 0.0319  85  SER B C   
3647 O O   . SER B 83  ? 0.4201 0.5011 0.3901 -0.0278 -0.0119 0.0388  85  SER B O   
3648 C CB  . SER B 83  ? 0.4588 0.5349 0.4232 -0.0153 -0.0127 0.0281  85  SER B CB  
3649 O OG  . SER B 83  ? 0.4668 0.5329 0.4331 -0.0138 -0.0118 0.0202  85  SER B OG  
3650 N N   . LEU B 84  ? 0.3986 0.4843 0.3793 -0.0163 -0.0058 0.0252  86  LEU B N   
3651 C CA  . LEU B 84  ? 0.3996 0.4794 0.3820 -0.0194 -0.0045 0.0257  86  LEU B CA  
3652 C C   . LEU B 84  ? 0.4074 0.5007 0.3942 -0.0174 -0.0017 0.0294  86  LEU B C   
3653 O O   . LEU B 84  ? 0.4257 0.5173 0.4130 -0.0194 -0.0008 0.0317  86  LEU B O   
3654 C CB  . LEU B 84  ? 0.3742 0.4435 0.3593 -0.0163 -0.0019 0.0162  86  LEU B CB  
3655 C CG  . LEU B 84  ? 0.3716 0.4277 0.3520 -0.0176 -0.0045 0.0125  86  LEU B CG  
3656 C CD1 . LEU B 84  ? 0.3672 0.4174 0.3519 -0.0144 -0.0012 0.0031  86  LEU B CD1 
3657 C CD2 . LEU B 84  ? 0.3768 0.4221 0.3500 -0.0241 -0.0080 0.0184  86  LEU B CD2 
3658 N N   . SER B 85  ? 0.4225 0.5293 0.4116 -0.0125 -0.0004 0.0301  87  SER B N   
3659 C CA  . SER B 85  ? 0.4288 0.5483 0.4211 -0.0078 0.0029  0.0324  87  SER B CA  
3660 C C   . SER B 85  ? 0.4328 0.5623 0.4241 -0.0131 0.0011  0.0426  87  SER B C   
3661 O O   . SER B 85  ? 0.4398 0.5735 0.4286 -0.0191 -0.0024 0.0489  87  SER B O   
3662 C CB  . SER B 85  ? 0.4389 0.5702 0.4326 -0.0010 0.0044  0.0309  87  SER B CB  
3663 O OG  . SER B 85  ? 0.4650 0.6048 0.4603 0.0050  0.0082  0.0315  87  SER B OG  
3664 N N   . GLY B 86  ? 0.4501 0.5829 0.4428 -0.0109 0.0037  0.0439  88  GLY B N   
3665 C CA  . GLY B 86  ? 0.4626 0.6072 0.4551 -0.0151 0.0023  0.0527  88  GLY B CA  
3666 C C   . GLY B 86  ? 0.4864 0.6222 0.4760 -0.0254 -0.0020 0.0559  88  GLY B C   
3667 O O   . GLY B 86  ? 0.4832 0.6306 0.4727 -0.0302 -0.0039 0.0631  88  GLY B O   
3668 N N   . LYS B 87  ? 0.5174 0.6343 0.5040 -0.0287 -0.0039 0.0509  89  LYS B N   
3669 C CA  . LYS B 87  ? 0.5298 0.6343 0.5116 -0.0373 -0.0079 0.0527  89  LYS B CA  
3670 C C   . LYS B 87  ? 0.5362 0.6375 0.5189 -0.0355 -0.0059 0.0515  89  LYS B C   
3671 O O   . LYS B 87  ? 0.5156 0.6165 0.5014 -0.0275 -0.0010 0.0468  89  LYS B O   
3672 C CB  . LYS B 87  ? 0.5470 0.6320 0.5245 -0.0386 -0.0096 0.0470  89  LYS B CB  
3673 C CG  . LYS B 87  ? 0.5730 0.6584 0.5474 -0.0397 -0.0118 0.0483  89  LYS B CG  
3674 C CD  . LYS B 87  ? 0.6015 0.6890 0.5703 -0.0492 -0.0162 0.0568  89  LYS B CD  
3675 C CE  . LYS B 87  ? 0.6524 0.7386 0.6168 -0.0495 -0.0176 0.0585  89  LYS B CE  
3676 N NZ  . LYS B 87  ? 0.6904 0.7822 0.6504 -0.0593 -0.0207 0.0680  89  LYS B NZ  
3677 N N   . GLN B 88  ? 0.5529 0.6515 0.5321 -0.0429 -0.0095 0.0555  90  GLN B N   
3678 C CA  . GLN B 88  ? 0.5713 0.6677 0.5502 -0.0415 -0.0082 0.0553  90  GLN B CA  
3679 C C   . GLN B 88  ? 0.5157 0.5927 0.4936 -0.0369 -0.0052 0.0473  90  GLN B C   
3680 O O   . GLN B 88  ? 0.4867 0.5506 0.4627 -0.0376 -0.0061 0.0426  90  GLN B O   
3681 C CB  . GLN B 88  ? 0.6360 0.7332 0.6106 -0.0514 -0.0137 0.0607  90  GLN B CB  
3682 C CG  . GLN B 88  ? 0.6984 0.8183 0.6752 -0.0568 -0.0161 0.0690  90  GLN B CG  
3683 C CD  . GLN B 88  ? 0.7387 0.8783 0.7199 -0.0506 -0.0130 0.0722  90  GLN B CD  
3684 O OE1 . GLN B 88  ? 0.7763 0.9110 0.7583 -0.0414 -0.0085 0.0681  90  GLN B OE1 
3685 N NE2 . GLN B 88  ? 0.7563 0.9182 0.7396 -0.0558 -0.0154 0.0797  90  GLN B NE2 
3686 N N   . ASN B 89  ? 0.5296 0.6056 0.5081 -0.0321 -0.0017 0.0462  91  ASN B N   
3687 C CA  . ASN B 89  ? 0.5337 0.5927 0.5116 -0.0277 0.0022  0.0392  91  ASN B CA  
3688 C C   . ASN B 89  ? 0.5237 0.5665 0.4964 -0.0331 -0.0015 0.0374  91  ASN B C   
3689 O O   . ASN B 89  ? 0.5259 0.5553 0.4985 -0.0310 0.0003  0.0310  91  ASN B O   
3690 C CB  . ASN B 89  ? 0.5394 0.6013 0.5177 -0.0208 0.0074  0.0398  91  ASN B CB  
3691 C CG  . ASN B 89  ? 0.5498 0.6206 0.5313 -0.0132 0.0124  0.0387  91  ASN B CG  
3692 O OD1 . ASN B 89  ? 0.5717 0.6427 0.5559 -0.0122 0.0131  0.0352  91  ASN B OD1 
3693 N ND2 . ASN B 89  ? 0.5661 0.6438 0.5464 -0.0069 0.0161  0.0416  91  ASN B ND2 
3694 N N   . ASP B 90  ? 0.5184 0.5626 0.4865 -0.0401 -0.0070 0.0424  92  ASP B N   
3695 C CA  . ASP B 90  ? 0.5353 0.5628 0.4964 -0.0449 -0.0110 0.0409  92  ASP B CA  
3696 C C   . ASP B 90  ? 0.5076 0.5319 0.4644 -0.0516 -0.0163 0.0427  92  ASP B C   
3697 O O   . ASP B 90  ? 0.5205 0.5330 0.4689 -0.0577 -0.0212 0.0439  92  ASP B O   
3698 C CB  . ASP B 90  ? 0.5689 0.5975 0.5260 -0.0478 -0.0135 0.0445  92  ASP B CB  
3699 C CG  . ASP B 90  ? 0.6210 0.6673 0.5784 -0.0544 -0.0176 0.0519  92  ASP B CG  
3700 O OD1 . ASP B 90  ? 0.6427 0.7024 0.6043 -0.0557 -0.0176 0.0549  92  ASP B OD1 
3701 O OD2 . ASP B 90  ? 0.6699 0.7181 0.6236 -0.0584 -0.0209 0.0547  92  ASP B OD2 
3702 N N   . SER B 91  ? 0.4604 0.4943 0.4212 -0.0506 -0.0154 0.0435  93  SER B N   
3703 C CA  . SER B 91  ? 0.4494 0.4818 0.4053 -0.0570 -0.0199 0.0468  93  SER B CA  
3704 C C   . SER B 91  ? 0.4451 0.4567 0.3935 -0.0566 -0.0218 0.0420  93  SER B C   
3705 O O   . SER B 91  ? 0.4365 0.4406 0.3868 -0.0503 -0.0185 0.0357  93  SER B O   
3706 C CB  . SER B 91  ? 0.4526 0.4997 0.4141 -0.0545 -0.0180 0.0484  93  SER B CB  
3707 O OG  . SER B 91  ? 0.4351 0.4796 0.4009 -0.0462 -0.0138 0.0415  93  SER B OG  
3708 N N   . ALA B 92  ? 0.4558 0.4581 0.3949 -0.0630 -0.0266 0.0450  94  ALA B N   
3709 C CA  . ALA B 92  ? 0.4569 0.4388 0.3862 -0.0616 -0.0287 0.0412  94  ALA B CA  
3710 C C   . ALA B 92  ? 0.4325 0.4172 0.3665 -0.0534 -0.0252 0.0360  94  ALA B C   
3711 O O   . ALA B 92  ? 0.4291 0.4023 0.3599 -0.0481 -0.0245 0.0301  94  ALA B O   
3712 C CB  . ALA B 92  ? 0.4839 0.4551 0.4011 -0.0701 -0.0341 0.0462  94  ALA B CB  
3713 N N   . GLU B 93  ? 0.4214 0.4223 0.3627 -0.0520 -0.0232 0.0378  95  GLU B N   
3714 C CA  . GLU B 93  ? 0.4057 0.4117 0.3514 -0.0446 -0.0204 0.0329  95  GLU B CA  
3715 C C   . GLU B 93  ? 0.3809 0.3875 0.3342 -0.0378 -0.0159 0.0251  95  GLU B C   
3716 O O   . GLU B 93  ? 0.3564 0.3572 0.3091 -0.0326 -0.0149 0.0187  95  GLU B O   
3717 C CB  . GLU B 93  ? 0.4274 0.4517 0.3794 -0.0443 -0.0191 0.0367  95  GLU B CB  
3718 C CG  . GLU B 93  ? 0.4729 0.4981 0.4178 -0.0510 -0.0228 0.0445  95  GLU B CG  
3719 C CD  . GLU B 93  ? 0.5179 0.5479 0.4613 -0.0608 -0.0254 0.0524  95  GLU B CD  
3720 O OE1 . GLU B 93  ? 0.5091 0.5422 0.4566 -0.0618 -0.0246 0.0521  95  GLU B OE1 
3721 O OE2 . GLU B 93  ? 0.5653 0.5965 0.5032 -0.0677 -0.0281 0.0591  95  GLU B OE2 
3722 N N   . VAL B 94  ? 0.3794 0.3931 0.3395 -0.0375 -0.0128 0.0255  96  VAL B N   
3723 C CA  . VAL B 94  ? 0.3792 0.3919 0.3458 -0.0319 -0.0077 0.0184  96  VAL B CA  
3724 C C   . VAL B 94  ? 0.3736 0.3711 0.3353 -0.0315 -0.0083 0.0147  96  VAL B C   
3725 O O   . VAL B 94  ? 0.3716 0.3670 0.3372 -0.0270 -0.0049 0.0077  96  VAL B O   
3726 C CB  . VAL B 94  ? 0.3801 0.4014 0.3528 -0.0307 -0.0038 0.0199  96  VAL B CB  
3727 C CG1 . VAL B 94  ? 0.4199 0.4374 0.3884 -0.0348 -0.0057 0.0250  96  VAL B CG1 
3728 C CG2 . VAL B 94  ? 0.3656 0.3845 0.3441 -0.0254 0.0020  0.0126  96  VAL B CG2 
3729 N N   . LYS B 95  ? 0.3888 0.3763 0.3420 -0.0361 -0.0123 0.0189  97  LYS B N   
3730 C CA  . LYS B 95  ? 0.3822 0.3547 0.3293 -0.0350 -0.0130 0.0157  97  LYS B CA  
3731 C C   . LYS B 95  ? 0.3689 0.3339 0.3104 -0.0318 -0.0147 0.0119  97  LYS B C   
3732 O O   . LYS B 95  ? 0.3726 0.3325 0.3146 -0.0273 -0.0125 0.0064  97  LYS B O   
3733 C CB  . LYS B 95  ? 0.4321 0.3948 0.3697 -0.0407 -0.0176 0.0208  97  LYS B CB  
3734 C CG  . LYS B 95  ? 0.4444 0.4155 0.3863 -0.0432 -0.0164 0.0247  97  LYS B CG  
3735 C CD  . LYS B 95  ? 0.4907 0.4527 0.4236 -0.0483 -0.0209 0.0282  97  LYS B CD  
3736 C CE  . LYS B 95  ? 0.5135 0.4830 0.4511 -0.0474 -0.0182 0.0298  97  LYS B CE  
3737 N NZ  . LYS B 95  ? 0.5638 0.5285 0.4931 -0.0537 -0.0236 0.0339  97  LYS B NZ  
3738 N N   . ALA B 96  ? 0.3543 0.3193 0.2905 -0.0334 -0.0182 0.0149  98  ALA B N   
3739 C CA  . ALA B 96  ? 0.3482 0.3057 0.2771 -0.0290 -0.0200 0.0117  98  ALA B CA  
3740 C C   . ALA B 96  ? 0.3333 0.3022 0.2724 -0.0223 -0.0156 0.0043  98  ALA B C   
3741 O O   . ALA B 96  ? 0.3338 0.2984 0.2709 -0.0171 -0.0149 -0.0010 98  ALA B O   
3742 C CB  . ALA B 96  ? 0.3603 0.3159 0.2814 -0.0321 -0.0237 0.0170  98  ALA B CB  
3743 N N   . PHE B 97  ? 0.3071 0.2908 0.2566 -0.0224 -0.0128 0.0040  99  PHE B N   
3744 C CA  . PHE B 97  ? 0.2940 0.2889 0.2535 -0.0172 -0.0087 -0.0035 99  PHE B CA  
3745 C C   . PHE B 97  ? 0.2758 0.2676 0.2401 -0.0156 -0.0049 -0.0091 99  PHE B C   
3746 O O   . PHE B 97  ? 0.2799 0.2734 0.2458 -0.0115 -0.0037 -0.0156 99  PHE B O   
3747 C CB  . PHE B 97  ? 0.2805 0.2895 0.2484 -0.0176 -0.0065 -0.0025 99  PHE B CB  
3748 C CG  . PHE B 97  ? 0.2760 0.2959 0.2522 -0.0128 -0.0033 -0.0103 99  PHE B CG  
3749 C CD1 . PHE B 97  ? 0.2742 0.2966 0.2485 -0.0084 -0.0048 -0.0151 99  PHE B CD1 
3750 C CD2 . PHE B 97  ? 0.2674 0.2952 0.2524 -0.0125 0.0010  -0.0131 99  PHE B CD2 
3751 C CE1 . PHE B 97  ? 0.2699 0.3038 0.2520 -0.0047 -0.0023 -0.0229 99  PHE B CE1 
3752 C CE2 . PHE B 97  ? 0.2689 0.3055 0.2607 -0.0091 0.0036  -0.0209 99  PHE B CE2 
3753 C CZ  . PHE B 97  ? 0.2647 0.3054 0.2557 -0.0056 0.0017  -0.0259 99  PHE B CZ  
3754 N N   . ALA B 98  ? 0.2678 0.2563 0.2343 -0.0186 -0.0026 -0.0069 100 ALA B N   
3755 C CA  . ALA B 98  ? 0.2706 0.2554 0.2412 -0.0172 0.0017  -0.0116 100 ALA B CA  
3756 C C   . ALA B 98  ? 0.2797 0.2554 0.2432 -0.0146 -0.0001 -0.0141 100 ALA B C   
3757 O O   . ALA B 98  ? 0.2821 0.2612 0.2507 -0.0118 0.0032  -0.0204 100 ALA B O   
3758 C CB  . ALA B 98  ? 0.2688 0.2497 0.2398 -0.0199 0.0037  -0.0075 100 ALA B CB  
3759 N N   . GLN B 99  ? 0.2948 0.2595 0.2464 -0.0155 -0.0053 -0.0093 101 GLN B N   
3760 C CA  . GLN B 99  ? 0.3090 0.2627 0.2510 -0.0118 -0.0075 -0.0110 101 GLN B CA  
3761 C C   . GLN B 99  ? 0.3123 0.2720 0.2539 -0.0062 -0.0081 -0.0159 101 GLN B C   
3762 O O   . GLN B 99  ? 0.3126 0.2741 0.2557 -0.0017 -0.0060 -0.0211 101 GLN B O   
3763 C CB  . GLN B 99  ? 0.3327 0.2709 0.2599 -0.0144 -0.0133 -0.0048 101 GLN B CB  
3764 C CG  . GLN B 99  ? 0.3501 0.2808 0.2752 -0.0184 -0.0133 -0.0013 101 GLN B CG  
3765 C CD  . GLN B 99  ? 0.3560 0.2845 0.2839 -0.0147 -0.0092 -0.0053 101 GLN B CD  
3766 O OE1 . GLN B 99  ? 0.3661 0.2886 0.2880 -0.0095 -0.0096 -0.0086 101 GLN B OE1 
3767 N NE2 . GLN B 99  ? 0.3410 0.2751 0.2778 -0.0165 -0.0047 -0.0051 101 GLN B NE2 
3768 N N   . GLU B 100 ? 0.3230 0.2880 0.2638 -0.0062 -0.0104 -0.0144 102 GLU B N   
3769 C CA  . GLU B 100 ? 0.3366 0.3070 0.2746 0.0000  -0.0117 -0.0183 102 GLU B CA  
3770 C C   . GLU B 100 ? 0.3255 0.3134 0.2778 0.0025  -0.0072 -0.0264 102 GLU B C   
3771 O O   . GLU B 100 ? 0.3302 0.3247 0.2818 0.0085  -0.0075 -0.0315 102 GLU B O   
3772 C CB  . GLU B 100 ? 0.3529 0.3225 0.2845 -0.0009 -0.0153 -0.0132 102 GLU B CB  
3773 C CG  . GLU B 100 ? 0.3826 0.3329 0.2968 -0.0023 -0.0202 -0.0068 102 GLU B CG  
3774 C CD  . GLU B 100 ? 0.4191 0.3589 0.3213 0.0053  -0.0218 -0.0098 102 GLU B CD  
3775 O OE1 . GLU B 100 ? 0.4600 0.4064 0.3603 0.0127  -0.0220 -0.0134 102 GLU B OE1 
3776 O OE2 . GLU B 100 ? 0.4384 0.3648 0.3330 0.0050  -0.0228 -0.0090 102 GLU B OE2 
3777 N N   . LEU B 101 ? 0.3139 0.3088 0.2778 -0.0018 -0.0032 -0.0275 103 LEU B N   
3778 C CA  . LEU B 101 ? 0.3143 0.3236 0.2913 -0.0012 0.0014  -0.0355 103 LEU B CA  
3779 C C   . LEU B 101 ? 0.3304 0.3404 0.3097 0.0008  0.0041  -0.0409 103 LEU B C   
3780 O O   . LEU B 101 ? 0.3403 0.3632 0.3260 0.0034  0.0056  -0.0480 103 LEU B O   
3781 C CB  . LEU B 101 ? 0.3030 0.3146 0.2887 -0.0062 0.0056  -0.0350 103 LEU B CB  
3782 C CG  . LEU B 101 ? 0.2933 0.3143 0.2834 -0.0066 0.0054  -0.0347 103 LEU B CG  
3783 C CD1 . LEU B 101 ? 0.2829 0.3025 0.2779 -0.0104 0.0093  -0.0325 103 LEU B CD1 
3784 C CD2 . LEU B 101 ? 0.2969 0.3318 0.2938 -0.0036 0.0064  -0.0433 103 LEU B CD2 
3785 N N   . ASN B 102 ? 0.3644 0.3623 0.3388 -0.0004 0.0046  -0.0374 104 ASN B N   
3786 C CA  . ASN B 102 ? 0.3705 0.3687 0.3486 0.0001  0.0088  -0.0414 104 ASN B CA  
3787 C C   . ASN B 102 ? 0.3927 0.4012 0.3710 0.0060  0.0081  -0.0475 104 ASN B C   
3788 O O   . ASN B 102 ? 0.3965 0.4153 0.3843 0.0052  0.0127  -0.0535 104 ASN B O   
3789 C CB  . ASN B 102 ? 0.3728 0.3554 0.3416 0.0001  0.0079  -0.0361 104 ASN B CB  
3790 C CG  . ASN B 102 ? 0.3657 0.3498 0.3390 0.0009  0.0128  -0.0398 104 ASN B CG  
3791 O OD1 . ASN B 102 ? 0.3513 0.3427 0.3358 -0.0026 0.0186  -0.0435 104 ASN B OD1 
3792 N ND2 . ASN B 102 ? 0.3604 0.3368 0.3240 0.0056  0.0108  -0.0386 104 ASN B ND2 
3793 N N   . GLN B 103 ? 0.4090 0.4147 0.3764 0.0118  0.0029  -0.0457 105 GLN B N   
3794 C CA  . GLN B 103 ? 0.4318 0.4478 0.3972 0.0194  0.0019  -0.0510 105 GLN B CA  
3795 C C   . GLN B 103 ? 0.4099 0.4467 0.3873 0.0195  0.0035  -0.0583 105 GLN B C   
3796 O O   . GLN B 103 ? 0.4113 0.4608 0.3895 0.0254  0.0032  -0.0636 105 GLN B O   
3797 C CB  . GLN B 103 ? 0.4827 0.4866 0.4305 0.0262  -0.0039 -0.0464 105 GLN B CB  
3798 C CG  . GLN B 103 ? 0.5021 0.5056 0.4462 0.0260  -0.0073 -0.0435 105 GLN B CG  
3799 C CD  . GLN B 103 ? 0.5466 0.5297 0.4718 0.0283  -0.0123 -0.0362 105 GLN B CD  
3800 O OE1 . GLN B 103 ? 0.6043 0.5771 0.5169 0.0344  -0.0141 -0.0356 105 GLN B OE1 
3801 N NE2 . GLN B 103 ? 0.5485 0.5246 0.4707 0.0231  -0.0145 -0.0303 105 GLN B NE2 
3802 N N   . TYR B 104 ? 0.3970 0.4384 0.3830 0.0139  0.0050  -0.0589 106 TYR B N   
3803 C CA  . TYR B 104 ? 0.3910 0.4516 0.3872 0.0142  0.0059  -0.0664 106 TYR B CA  
3804 C C   . TYR B 104 ? 0.3811 0.4483 0.3914 0.0064  0.0116  -0.0716 106 TYR B C   
3805 O O   . TYR B 104 ? 0.3737 0.4535 0.3919 0.0049  0.0124  -0.0773 106 TYR B O   
3806 C CB  . TYR B 104 ? 0.3871 0.4477 0.3793 0.0156  0.0022  -0.0633 106 TYR B CB  
3807 C CG  . TYR B 104 ? 0.3981 0.4519 0.3755 0.0232  -0.0029 -0.0587 106 TYR B CG  
3808 C CD1 . TYR B 104 ? 0.4120 0.4771 0.3862 0.0316  -0.0047 -0.0635 106 TYR B CD1 
3809 C CD2 . TYR B 104 ? 0.4002 0.4366 0.3662 0.0219  -0.0059 -0.0497 106 TYR B CD2 
3810 C CE1 . TYR B 104 ? 0.4321 0.4888 0.3906 0.0395  -0.0092 -0.0590 106 TYR B CE1 
3811 C CE2 . TYR B 104 ? 0.4212 0.4484 0.3719 0.0281  -0.0104 -0.0453 106 TYR B CE2 
3812 C CZ  . TYR B 104 ? 0.4411 0.4770 0.3872 0.0374  -0.0118 -0.0498 106 TYR B CZ  
3813 O OH  . TYR B 104 ? 0.4626 0.4869 0.3915 0.0442  -0.0158 -0.0451 106 TYR B OH  
3814 N N   . LEU B 105 ? 0.3920 0.4499 0.4042 0.0019  0.0156  -0.0697 107 LEU B N   
3815 C CA  . LEU B 105 ? 0.4183 0.4783 0.4416 -0.0056 0.0217  -0.0737 107 LEU B CA  
3816 C C   . LEU B 105 ? 0.4716 0.5493 0.5054 -0.0072 0.0249  -0.0834 107 LEU B C   
3817 O O   . LEU B 105 ? 0.5062 0.5923 0.5383 -0.0024 0.0235  -0.0854 107 LEU B O   
3818 C CB  . LEU B 105 ? 0.4068 0.4509 0.4276 -0.0091 0.0253  -0.0682 107 LEU B CB  
3819 C CG  . LEU B 105 ? 0.3862 0.4150 0.3985 -0.0091 0.0228  -0.0591 107 LEU B CG  
3820 C CD1 . LEU B 105 ? 0.3802 0.3965 0.3914 -0.0120 0.0270  -0.0552 107 LEU B CD1 
3821 C CD2 . LEU B 105 ? 0.3815 0.4123 0.3965 -0.0111 0.0225  -0.0586 107 LEU B CD2 
3822 N N   . SER B 106 ? 0.4938 0.5766 0.5374 -0.0140 0.0292  -0.0892 108 SER B N   
3823 C CA  . SER B 106 ? 0.5209 0.6205 0.5757 -0.0185 0.0329  -0.0991 108 SER B CA  
3824 C C   . SER B 106 ? 0.5635 0.6540 0.6242 -0.0278 0.0404  -0.1006 108 SER B C   
3825 O O   . SER B 106 ? 0.5863 0.6621 0.6440 -0.0300 0.0420  -0.0965 108 SER B O   
3826 C CB  . SER B 106 ? 0.5385 0.6528 0.5977 -0.0179 0.0301  -0.1059 108 SER B CB  
3827 O OG  . SER B 106 ? 0.5535 0.6783 0.6239 -0.0260 0.0347  -0.1152 108 SER B OG  
3828 N N   . SER B 107 ? 0.6265 0.7266 0.6953 -0.0329 0.0451  -0.1063 109 SER B N   
3829 C CA  . SER B 107 ? 0.6580 0.7507 0.7329 -0.0429 0.0532  -0.1092 109 SER B CA  
3830 C C   . SER B 107 ? 0.6811 0.7814 0.7636 -0.0501 0.0549  -0.1184 109 SER B C   
3831 O O   . SER B 107 ? 0.6519 0.7459 0.7390 -0.0595 0.0618  -0.1221 109 SER B O   
3832 C CB  . SER B 107 ? 0.6815 0.7812 0.7609 -0.0455 0.0574  -0.1105 109 SER B CB  
3833 O OG  . SER B 107 ? 0.6803 0.7671 0.7507 -0.0393 0.0566  -0.1014 109 SER B OG  
3834 N N   . ALA B 108 ? 0.6940 0.8054 0.7763 -0.0457 0.0489  -0.1217 110 ALA B N   
3835 C CA  . ALA B 108 ? 0.7445 0.8626 0.8320 -0.0507 0.0491  -0.1304 110 ALA B CA  
3836 C C   . ALA B 108 ? 0.7942 0.8903 0.8758 -0.0526 0.0518  -0.1264 110 ALA B C   
3837 O O   . ALA B 108 ? 0.8887 0.9823 0.9737 -0.0598 0.0554  -0.1333 110 ALA B O   
3838 C CB  . ALA B 108 ? 0.7149 0.8513 0.8026 -0.0437 0.0419  -0.1342 110 ALA B CB  
3839 N N   . GLY B 109 ? 0.7854 0.8670 0.8580 -0.0462 0.0500  -0.1159 111 GLY B N   
3840 C CA  . GLY B 109 ? 0.7347 0.7969 0.8005 -0.0460 0.0523  -0.1104 111 GLY B CA  
3841 C C   . GLY B 109 ? 0.6971 0.7425 0.7569 -0.0447 0.0552  -0.1008 111 GLY B C   
3842 O O   . GLY B 109 ? 0.6038 0.6405 0.6562 -0.0394 0.0525  -0.0928 111 GLY B O   
3843 N N   . VAL B 110 ? 0.7248 0.7668 0.7877 -0.0497 0.0606  -0.1017 112 VAL B N   
3844 C CA  . VAL B 110 ? 0.7167 0.7425 0.7740 -0.0490 0.0646  -0.0934 112 VAL B CA  
3845 C C   . VAL B 110 ? 0.7078 0.7185 0.7650 -0.0560 0.0735  -0.0951 112 VAL B C   
3846 O O   . VAL B 110 ? 0.7247 0.7411 0.7891 -0.0638 0.0778  -0.1032 112 VAL B O   
3847 C CB  . VAL B 110 ? 0.7135 0.7462 0.7725 -0.0476 0.0641  -0.0919 112 VAL B CB  
3848 C CG1 . VAL B 110 ? 0.7274 0.7697 0.7956 -0.0554 0.0697  -0.0998 112 VAL B CG1 
3849 C CG2 . VAL B 110 ? 0.7049 0.7217 0.7559 -0.0442 0.0657  -0.0824 112 VAL B CG2 
3850 N N   . THR B 111 ? 0.6546 0.6471 0.7034 -0.0531 0.0761  -0.0876 113 THR B N   
3851 C CA  . THR B 111 ? 0.6503 0.6243 0.6955 -0.0572 0.0851  -0.0860 113 THR B CA  
3852 C C   . THR B 111 ? 0.6296 0.5971 0.6707 -0.0537 0.0864  -0.0779 113 THR B C   
3853 O O   . THR B 111 ? 0.6009 0.5699 0.6373 -0.0467 0.0803  -0.0713 113 THR B O   
3854 C CB  . THR B 111 ? 0.6425 0.6009 0.6795 -0.0546 0.0873  -0.0832 113 THR B CB  
3855 O OG1 . THR B 111 ? 0.6476 0.6147 0.6880 -0.0562 0.0844  -0.0906 113 THR B OG1 
3856 C CG2 . THR B 111 ? 0.6619 0.5998 0.6935 -0.0586 0.0972  -0.0826 113 THR B CG2 
3857 N N   . THR B 112 ? 0.6252 0.5848 0.6671 -0.0587 0.0941  -0.0783 114 THR B N   
3858 C CA  . THR B 112 ? 0.5992 0.5523 0.6367 -0.0552 0.0961  -0.0710 114 THR B CA  
3859 C C   . THR B 112 ? 0.6167 0.5485 0.6469 -0.0562 0.1049  -0.0669 114 THR B C   
3860 O O   . THR B 112 ? 0.6459 0.5705 0.6779 -0.0635 0.1121  -0.0719 114 THR B O   
3861 C CB  . THR B 112 ? 0.5814 0.5478 0.6264 -0.0586 0.0971  -0.0744 114 THR B CB  
3862 O OG1 . THR B 112 ? 0.5619 0.5472 0.6117 -0.0559 0.0887  -0.0779 114 THR B OG1 
3863 C CG2 . THR B 112 ? 0.5833 0.5436 0.6229 -0.0539 0.0985  -0.0671 114 THR B CG2 
3864 N N   . VAL B 113 ? 0.6151 0.5371 0.6366 -0.0489 0.1043  -0.0582 115 VAL B N   
3865 C CA  . VAL B 113 ? 0.6403 0.5415 0.6525 -0.0472 0.1122  -0.0530 115 VAL B CA  
3866 C C   . VAL B 113 ? 0.6598 0.5564 0.6678 -0.0434 0.1144  -0.0465 115 VAL B C   
3867 O O   . VAL B 113 ? 0.6431 0.5484 0.6506 -0.0384 0.1073  -0.0430 115 VAL B O   
3868 C CB  . VAL B 113 ? 0.6362 0.5310 0.6406 -0.0405 0.1092  -0.0487 115 VAL B CB  
3869 C CG1 . VAL B 113 ? 0.6584 0.5360 0.6515 -0.0345 0.1145  -0.0409 115 VAL B CG1 
3870 C CG2 . VAL B 113 ? 0.6508 0.5441 0.6567 -0.0443 0.1103  -0.0552 115 VAL B CG2 
3871 N N   . GLN B 114 ? 0.7160 0.5974 0.7195 -0.0455 0.1242  -0.0447 116 GLN B N   
3872 C CA  . GLN B 114 ? 0.7469 0.6211 0.7446 -0.0412 0.1279  -0.0380 116 GLN B CA  
3873 C C   . GLN B 114 ? 0.7312 0.5937 0.7171 -0.0318 0.1269  -0.0300 116 GLN B C   
3874 O O   . GLN B 114 ? 0.7296 0.5796 0.7094 -0.0307 0.1312  -0.0293 116 GLN B O   
3875 C CB  . GLN B 114 ? 0.8220 0.6850 0.8201 -0.0483 0.1396  -0.0399 116 GLN B CB  
3876 C CG  . GLN B 114 ? 0.8581 0.7209 0.8551 -0.0468 0.1437  -0.0358 116 GLN B CG  
3877 C CD  . GLN B 114 ? 0.9511 0.8071 0.9515 -0.0567 0.1549  -0.0393 116 GLN B CD  
3878 O OE1 . GLN B 114 ? 1.0091 0.8778 1.0204 -0.0660 0.1552  -0.0468 116 GLN B OE1 
3879 N NE2 . GLN B 114 ? 0.9688 0.8048 0.9594 -0.0552 0.1644  -0.0339 116 GLN B NE2 
3880 N N   . SER B 115 ? 0.7181 0.5845 0.7001 -0.0249 0.1217  -0.0242 117 SER B N   
3881 C CA  . SER B 115 ? 0.7388 0.5992 0.7106 -0.0160 0.1188  -0.0168 117 SER B CA  
3882 C C   . SER B 115 ? 0.7754 0.6176 0.7370 -0.0119 0.1286  -0.0116 117 SER B C   
3883 O O   . SER B 115 ? 0.8364 0.6735 0.7970 -0.0126 0.1342  -0.0104 117 SER B O   
3884 C CB  . SER B 115 ? 0.7220 0.5922 0.6927 -0.0114 0.1098  -0.0132 117 SER B CB  
3885 O OG  . SER B 115 ? 0.7047 0.5724 0.6735 -0.0101 0.1127  -0.0113 117 SER B OG  
3886 N N   . GLN B 116 ? 0.8207 0.6540 0.7740 -0.0065 0.1303  -0.0083 118 GLN B N   
3887 C CA  . GLN B 116 ? 0.8671 0.6829 0.8078 0.0002  0.1388  -0.0022 118 GLN B CA  
3888 C C   . GLN B 116 ? 0.8522 0.6733 0.7862 0.0097  0.1329  0.0049  118 GLN B C   
3889 O O   . GLN B 116 ? 0.7912 0.6274 0.7290 0.0107  0.1225  0.0053  118 GLN B O   
3890 C CB  . GLN B 116 ? 0.9072 0.7106 0.8410 0.0022  0.1440  -0.0027 118 GLN B CB  
3891 C CG  . GLN B 116 ? 0.9432 0.7296 0.8760 -0.0051 0.1549  -0.0074 118 GLN B CG  
3892 C CD  . GLN B 116 ? 0.9428 0.7399 0.8898 -0.0172 0.1532  -0.0156 118 GLN B CD  
3893 O OE1 . GLN B 116 ? 0.9739 0.7693 0.9250 -0.0234 0.1584  -0.0172 118 GLN B OE1 
3894 N NE2 . GLN B 116 ? 0.9430 0.7529 0.8977 -0.0204 0.1459  -0.0208 118 GLN B NE2 
3895 N N   . GLN B 117 ? 0.8751 0.6837 0.7988 0.0162  0.1398  0.0105  119 GLN B N   
3896 C CA  . GLN B 117 ? 0.8797 0.6922 0.7953 0.0260  0.1353  0.0174  119 GLN B CA  
3897 C C   . GLN B 117 ? 0.8693 0.6843 0.7790 0.0327  0.1325  0.0204  119 GLN B C   
3898 O O   . GLN B 117 ? 0.9192 0.7199 0.8200 0.0373  0.1409  0.0223  119 GLN B O   
3899 C CB  . GLN B 117 ? 0.9173 0.7156 0.8230 0.0317  0.1443  0.0222  119 GLN B CB  
3900 C CG  . GLN B 117 ? 0.9215 0.7250 0.8189 0.0417  0.1393  0.0286  119 GLN B CG  
3901 C CD  . GLN B 117 ? 0.8993 0.7195 0.8038 0.0389  0.1275  0.0271  119 GLN B CD  
3902 O OE1 . GLN B 117 ? 0.9204 0.7429 0.8312 0.0333  0.1269  0.0237  119 GLN B OE1 
3903 N NE2 . GLN B 117 ? 0.8446 0.6764 0.7471 0.0429  0.1184  0.0297  119 GLN B NE2 
3904 N N   . GLY B 118 ? 0.8185 0.6507 0.7323 0.0333  0.1215  0.0211  120 GLY B N   
3905 C CA  . GLY B 118 ? 0.7971 0.6366 0.7064 0.0396  0.1178  0.0245  120 GLY B CA  
3906 C C   . GLY B 118 ? 0.7715 0.6211 0.6895 0.0338  0.1126  0.0199  120 GLY B C   
3907 O O   . GLY B 118 ? 0.7341 0.6002 0.6566 0.0327  0.1028  0.0208  120 GLY B O   
3908 N N   . THR B 119 ? 0.7721 0.6115 0.6917 0.0301  0.1190  0.0152  121 THR B N   
3909 C CA  . THR B 119 ? 0.7513 0.5990 0.6779 0.0255  0.1150  0.0105  121 THR B CA  
3910 C C   . THR B 119 ? 0.7603 0.6004 0.6940 0.0162  0.1196  0.0026  121 THR B C   
3911 O O   . THR B 119 ? 0.7794 0.6018 0.7076 0.0157  0.1293  0.0012  121 THR B O   
3912 C CB  . THR B 119 ? 0.7593 0.6054 0.6777 0.0336  0.1170  0.0135  121 THR B CB  
3913 O OG1 . THR B 119 ? 0.7496 0.6087 0.6641 0.0409  0.1111  0.0203  121 THR B OG1 
3914 C CG2 . THR B 119 ? 0.7422 0.5962 0.6669 0.0298  0.1134  0.0086  121 THR B CG2 
3915 N N   . THR B 120 ? 0.7589 0.6125 0.7037 0.0091  0.1125  -0.0023 122 THR B N   
3916 C CA  . THR B 120 ? 0.7524 0.6047 0.7060 -0.0003 0.1149  -0.0104 122 THR B CA  
3917 C C   . THR B 120 ? 0.7634 0.6190 0.7195 -0.0020 0.1134  -0.0151 122 THR B C   
3918 O O   . THR B 120 ? 0.7452 0.6159 0.7052 -0.0008 0.1051  -0.0146 122 THR B O   
3919 C CB  . THR B 120 ? 0.7183 0.5840 0.6815 -0.0056 0.1082  -0.0129 122 THR B CB  
3920 O OG1 . THR B 120 ? 0.6904 0.5539 0.6491 -0.0019 0.1080  -0.0076 122 THR B OG1 
3921 C CG2 . THR B 120 ? 0.7308 0.5962 0.7024 -0.0146 0.1118  -0.0208 122 THR B CG2 
3922 N N   . THR B 121 ? 0.7953 0.6365 0.7486 -0.0050 0.1215  -0.0197 123 THR B N   
3923 C CA  . THR B 121 ? 0.8133 0.6540 0.7658 -0.0050 0.1211  -0.0240 123 THR B CA  
3924 C C   . THR B 121 ? 0.7926 0.6427 0.7572 -0.0151 0.1183  -0.0331 123 THR B C   
3925 O O   . THR B 121 ? 0.7931 0.6379 0.7620 -0.0228 0.1231  -0.0375 123 THR B O   
3926 C CB  . THR B 121 ? 0.8732 0.6907 0.8126 -0.0011 0.1312  -0.0234 123 THR B CB  
3927 O OG1 . THR B 121 ? 0.9008 0.7127 0.8297 0.0089  0.1333  -0.0145 123 THR B OG1 
3928 C CG2 . THR B 121 ? 0.8799 0.6957 0.8155 0.0014  0.1307  -0.0268 123 THR B CG2 
3929 N N   . ILE B 122 ? 0.7907 0.6554 0.7604 -0.0148 0.1109  -0.0356 124 ILE B N   
3930 C CA  . ILE B 122 ? 0.7812 0.6573 0.7619 -0.0228 0.1073  -0.0444 124 ILE B CA  
3931 C C   . ILE B 122 ? 0.7860 0.6580 0.7634 -0.0220 0.1085  -0.0492 124 ILE B C   
3932 O O   . ILE B 122 ? 0.7721 0.6539 0.7482 -0.0162 0.1028  -0.0466 124 ILE B O   
3933 C CB  . ILE B 122 ? 0.7482 0.6455 0.7371 -0.0225 0.0971  -0.0430 124 ILE B CB  
3934 C CG1 . ILE B 122 ? 0.7310 0.6299 0.7195 -0.0209 0.0953  -0.0368 124 ILE B CG1 
3935 C CG2 . ILE B 122 ? 0.7442 0.6530 0.7436 -0.0299 0.0942  -0.0519 124 ILE B CG2 
3936 C CD1 . ILE B 122 ? 0.6786 0.5934 0.6699 -0.0184 0.0852  -0.0330 124 ILE B CD1 
3937 N N   . SER B 123 ? 0.8189 0.6760 0.7940 -0.0279 0.1159  -0.0559 125 SER B N   
3938 C CA  . SER B 123 ? 0.8421 0.6902 0.8115 -0.0276 0.1182  -0.0615 125 SER B CA  
3939 C C   . SER B 123 ? 0.8404 0.7043 0.8209 -0.0346 0.1128  -0.0709 125 SER B C   
3940 O O   . SER B 123 ? 0.8569 0.7364 0.8488 -0.0401 0.1087  -0.0731 125 SER B O   
3941 C CB  . SER B 123 ? 0.8696 0.6912 0.8292 -0.0311 0.1291  -0.0641 125 SER B CB  
3942 O OG  . SER B 123 ? 0.8626 0.6687 0.8089 -0.0216 0.1341  -0.0553 125 SER B OG  
3943 N N   . GLY B 124 ? 0.8383 0.6983 0.8147 -0.0337 0.1128  -0.0764 126 GLY B N   
3944 C CA  . GLY B 124 ? 0.8170 0.6872 0.8018 -0.0415 0.1098  -0.0873 126 GLY B CA  
3945 C C   . GLY B 124 ? 0.7775 0.6744 0.7726 -0.0393 0.0997  -0.0872 126 GLY B C   
3946 O O   . GLY B 124 ? 0.7846 0.6940 0.7889 -0.0459 0.0967  -0.0957 126 GLY B O   
3947 N N   . LEU B 125 ? 0.7494 0.6552 0.7426 -0.0304 0.0946  -0.0782 127 LEU B N   
3948 C CA  . LEU B 125 ? 0.7307 0.6599 0.7321 -0.0282 0.0852  -0.0774 127 LEU B CA  
3949 C C   . LEU B 125 ? 0.7482 0.6836 0.7476 -0.0243 0.0819  -0.0813 127 LEU B C   
3950 O O   . LEU B 125 ? 0.7540 0.6842 0.7443 -0.0161 0.0825  -0.0758 127 LEU B O   
3951 C CB  . LEU B 125 ? 0.7136 0.6483 0.7126 -0.0213 0.0813  -0.0660 127 LEU B CB  
3952 C CG  . LEU B 125 ? 0.6947 0.6271 0.6960 -0.0239 0.0824  -0.0616 127 LEU B CG  
3953 C CD1 . LEU B 125 ? 0.6775 0.6181 0.6766 -0.0178 0.0767  -0.0516 127 LEU B CD1 
3954 C CD2 . LEU B 125 ? 0.6641 0.6059 0.6755 -0.0315 0.0807  -0.0682 127 LEU B CD2 
3955 N N   . LYS B 126 ? 0.7516 0.6995 0.7588 -0.0290 0.0782  -0.0901 128 LYS B N   
3956 C CA  . LYS B 126 ? 0.7622 0.7219 0.7692 -0.0244 0.0731  -0.0933 128 LYS B CA  
3957 C C   . LYS B 126 ? 0.7029 0.6738 0.7080 -0.0157 0.0675  -0.0828 128 LYS B C   
3958 O O   . LYS B 126 ? 0.6833 0.6578 0.6903 -0.0152 0.0656  -0.0754 128 LYS B O   
3959 C CB  . LYS B 126 ? 0.7940 0.7711 0.8113 -0.0297 0.0683  -0.1024 128 LYS B CB  
3960 C CG  . LYS B 126 ? 0.8708 0.8430 0.8927 -0.0402 0.0726  -0.1136 128 LYS B CG  
3961 C CD  . LYS B 126 ? 0.9096 0.9029 0.9413 -0.0437 0.0671  -0.1228 128 LYS B CD  
3962 C CE  . LYS B 126 ? 0.9645 0.9609 1.0047 -0.0550 0.0700  -0.1319 128 LYS B CE  
3963 N NZ  . LYS B 126 ? 1.0451 1.0264 1.0816 -0.0625 0.0759  -0.1410 128 LYS B NZ  
3964 N N   . PRO B 127 ? 0.6868 0.6642 0.6877 -0.0087 0.0646  -0.0817 129 PRO B N   
3965 C CA  . PRO B 127 ? 0.6280 0.6175 0.6276 -0.0016 0.0597  -0.0715 129 PRO B CA  
3966 C C   . PRO B 127 ? 0.5616 0.5680 0.5694 -0.0039 0.0528  -0.0698 129 PRO B C   
3967 O O   . PRO B 127 ? 0.5548 0.5678 0.5690 -0.0084 0.0508  -0.0775 129 PRO B O   
3968 C CB  . PRO B 127 ? 0.6322 0.6263 0.6263 0.0055  0.0586  -0.0726 129 PRO B CB  
3969 C CG  . PRO B 127 ? 0.6852 0.6631 0.6744 0.0032  0.0643  -0.0825 129 PRO B CG  
3970 C CD  . PRO B 127 ? 0.6998 0.6735 0.6967 -0.0074 0.0660  -0.0902 129 PRO B CD  
3971 N N   . GLY B 128 ? 0.5008 0.5136 0.5074 -0.0007 0.0493  -0.0596 130 GLY B N   
3972 C CA  . GLY B 128 ? 0.4497 0.4757 0.4612 -0.0020 0.0428  -0.0566 130 GLY B CA  
3973 C C   . GLY B 128 ? 0.4100 0.4323 0.4206 -0.0038 0.0418  -0.0484 130 GLY B C   
3974 O O   . GLY B 128 ? 0.4054 0.4200 0.4114 -0.0019 0.0449  -0.0428 130 GLY B O   
3975 N N   . TYR B 129 ? 0.3775 0.4053 0.3915 -0.0066 0.0374  -0.0481 131 TYR B N   
3976 C CA  . TYR B 129 ? 0.3592 0.3850 0.3713 -0.0080 0.0346  -0.0403 131 TYR B CA  
3977 C C   . TYR B 129 ? 0.3647 0.3843 0.3799 -0.0123 0.0361  -0.0450 131 TYR B C   
3978 O O   . TYR B 129 ? 0.3886 0.4137 0.4083 -0.0139 0.0351  -0.0523 131 TYR B O   
3979 C CB  . TYR B 129 ? 0.3348 0.3718 0.3459 -0.0066 0.0278  -0.0358 131 TYR B CB  
3980 C CG  . TYR B 129 ? 0.3126 0.3490 0.3194 -0.0075 0.0241  -0.0260 131 TYR B CG  
3981 C CD1 . TYR B 129 ? 0.3179 0.3512 0.3214 -0.0068 0.0258  -0.0193 131 TYR B CD1 
3982 C CD2 . TYR B 129 ? 0.3046 0.3441 0.3095 -0.0088 0.0185  -0.0234 131 TYR B CD2 
3983 C CE1 . TYR B 129 ? 0.3108 0.3449 0.3106 -0.0087 0.0220  -0.0108 131 TYR B CE1 
3984 C CE2 . TYR B 129 ? 0.2958 0.3336 0.2957 -0.0108 0.0148  -0.0148 131 TYR B CE2 
3985 C CZ  . TYR B 129 ? 0.3021 0.3380 0.3001 -0.0113 0.0164  -0.0087 131 TYR B CZ  
3986 O OH  . TYR B 129 ? 0.2982 0.3340 0.2917 -0.0141 0.0127  -0.0006 131 TYR B OH  
3987 N N   . TYR B 130 ? 0.3709 0.3804 0.3836 -0.0136 0.0387  -0.0409 132 TYR B N   
3988 C CA  . TYR B 130 ? 0.3578 0.3605 0.3726 -0.0171 0.0413  -0.0444 132 TYR B CA  
3989 C C   . TYR B 130 ? 0.3251 0.3255 0.3361 -0.0170 0.0373  -0.0377 132 TYR B C   
3990 O O   . TYR B 130 ? 0.3101 0.3085 0.3160 -0.0155 0.0354  -0.0297 132 TYR B O   
3991 C CB  . TYR B 130 ? 0.3827 0.3733 0.3968 -0.0184 0.0492  -0.0463 132 TYR B CB  
3992 C CG  . TYR B 130 ? 0.4097 0.3998 0.4267 -0.0199 0.0532  -0.0545 132 TYR B CG  
3993 C CD1 . TYR B 130 ? 0.4299 0.4197 0.4434 -0.0162 0.0542  -0.0539 132 TYR B CD1 
3994 C CD2 . TYR B 130 ? 0.4282 0.4192 0.4512 -0.0250 0.0559  -0.0633 132 TYR B CD2 
3995 C CE1 . TYR B 130 ? 0.4526 0.4402 0.4673 -0.0176 0.0577  -0.0621 132 TYR B CE1 
3996 C CE2 . TYR B 130 ? 0.4468 0.4370 0.4721 -0.0277 0.0593  -0.0717 132 TYR B CE2 
3997 C CZ  . TYR B 130 ? 0.4616 0.4490 0.4823 -0.0239 0.0601  -0.0712 132 TYR B CZ  
3998 O OH  . TYR B 130 ? 0.5080 0.4929 0.5297 -0.0266 0.0632  -0.0800 132 TYR B OH  
3999 N N   . LEU B 131 ? 0.3071 0.3082 0.3198 -0.0185 0.0359  -0.0410 133 LEU B N   
4000 C CA  . LEU B 131 ? 0.3064 0.3013 0.3144 -0.0185 0.0336  -0.0362 133 LEU B CA  
4001 C C   . LEU B 131 ? 0.3044 0.2903 0.3135 -0.0201 0.0399  -0.0379 133 LEU B C   
4002 O O   . LEU B 131 ? 0.2997 0.2874 0.3142 -0.0222 0.0436  -0.0447 133 LEU B O   
4003 C CB  . LEU B 131 ? 0.3020 0.3026 0.3092 -0.0174 0.0282  -0.0382 133 LEU B CB  
4004 C CG  . LEU B 131 ? 0.3039 0.2965 0.3033 -0.0166 0.0245  -0.0327 133 LEU B CG  
4005 C CD1 . LEU B 131 ? 0.3049 0.3010 0.2996 -0.0144 0.0181  -0.0323 133 LEU B CD1 
4006 C CD2 . LEU B 131 ? 0.3147 0.3015 0.3150 -0.0170 0.0287  -0.0353 133 LEU B CD2 
4007 N N   . ILE B 132 ? 0.3203 0.2972 0.3240 -0.0192 0.0410  -0.0316 134 ILE B N   
4008 C CA  . ILE B 132 ? 0.3319 0.2992 0.3347 -0.0198 0.0467  -0.0316 134 ILE B CA  
4009 C C   . ILE B 132 ? 0.3233 0.2874 0.3213 -0.0187 0.0429  -0.0286 134 ILE B C   
4010 O O   . ILE B 132 ? 0.3098 0.2728 0.3015 -0.0174 0.0369  -0.0228 134 ILE B O   
4011 C CB  . ILE B 132 ? 0.3519 0.3110 0.3503 -0.0181 0.0508  -0.0264 134 ILE B CB  
4012 C CG1 . ILE B 132 ? 0.3684 0.3285 0.3691 -0.0178 0.0546  -0.0290 134 ILE B CG1 
4013 C CG2 . ILE B 132 ? 0.3554 0.3039 0.3517 -0.0180 0.0567  -0.0258 134 ILE B CG2 
4014 C CD1 . ILE B 132 ? 0.3888 0.3410 0.3835 -0.0143 0.0587  -0.0235 134 ILE B CD1 
4015 N N   . LYS B 133 ? 0.3221 0.2847 0.3225 -0.0194 0.0463  -0.0326 135 LYS B N   
4016 C CA  . LYS B 133 ? 0.3197 0.2776 0.3145 -0.0173 0.0441  -0.0302 135 LYS B CA  
4017 C C   . LYS B 133 ? 0.3315 0.2846 0.3286 -0.0180 0.0516  -0.0322 135 LYS B C   
4018 O O   . LYS B 133 ? 0.3372 0.2927 0.3414 -0.0214 0.0578  -0.0372 135 LYS B O   
4019 C CB  . LYS B 133 ? 0.3143 0.2797 0.3090 -0.0159 0.0386  -0.0334 135 LYS B CB  
4020 C CG  . LYS B 133 ? 0.3210 0.2973 0.3250 -0.0177 0.0418  -0.0415 135 LYS B CG  
4021 C CD  . LYS B 133 ? 0.3308 0.3158 0.3336 -0.0148 0.0362  -0.0443 135 LYS B CD  
4022 C CE  . LYS B 133 ? 0.3458 0.3289 0.3440 -0.0112 0.0356  -0.0442 135 LYS B CE  
4023 N NZ  . LYS B 133 ? 0.3517 0.3441 0.3481 -0.0070 0.0309  -0.0477 135 LYS B NZ  
4024 N N   . ASP B 134 ? 0.3313 0.2775 0.3218 -0.0152 0.0510  -0.0286 136 ASP B N   
4025 C CA  . ASP B 134 ? 0.3498 0.2943 0.3423 -0.0152 0.0571  -0.0308 136 ASP B CA  
4026 C C   . ASP B 134 ? 0.3495 0.3063 0.3480 -0.0159 0.0560  -0.0373 136 ASP B C   
4027 O O   . ASP B 134 ? 0.3316 0.2928 0.3266 -0.0131 0.0488  -0.0375 136 ASP B O   
4028 C CB  . ASP B 134 ? 0.3443 0.2798 0.3273 -0.0108 0.0557  -0.0256 136 ASP B CB  
4029 C CG  . ASP B 134 ? 0.3619 0.2870 0.3395 -0.0095 0.0585  -0.0198 136 ASP B CG  
4030 O OD1 . ASP B 134 ? 0.3965 0.3162 0.3746 -0.0093 0.0661  -0.0194 136 ASP B OD1 
4031 O OD2 . ASP B 134 ? 0.3613 0.2839 0.3332 -0.0083 0.0530  -0.0154 136 ASP B OD2 
4032 N N   . SER B 135 ? 0.3720 0.3339 0.3786 -0.0195 0.0631  -0.0423 137 SER B N   
4033 C CA  . SER B 135 ? 0.4033 0.3793 0.4166 -0.0202 0.0635  -0.0486 137 SER B CA  
4034 C C   . SER B 135 ? 0.4301 0.4067 0.4362 -0.0137 0.0596  -0.0464 137 SER B C   
4035 O O   . SER B 135 ? 0.4669 0.4331 0.4665 -0.0111 0.0618  -0.0417 137 SER B O   
4036 C CB  . SER B 135 ? 0.4203 0.3992 0.4420 -0.0262 0.0727  -0.0527 137 SER B CB  
4037 O OG  . SER B 135 ? 0.4378 0.4331 0.4661 -0.0267 0.0728  -0.0584 137 SER B OG  
4038 N N   . ARG B 136 ? 0.4535 0.4411 0.4594 -0.0103 0.0542  -0.0497 138 ARG B N   
4039 C CA  . ARG B 136 ? 0.5031 0.4873 0.4979 -0.0024 0.0488  -0.0469 138 ARG B CA  
4040 C C   . ARG B 136 ? 0.5134 0.5004 0.5091 -0.0004 0.0544  -0.0473 138 ARG B C   
4041 O O   . ARG B 136 ? 0.5263 0.5256 0.5331 -0.0049 0.0608  -0.0521 138 ARG B O   
4042 C CB  . ARG B 136 ? 0.5325 0.5266 0.5251 0.0020  0.0422  -0.0500 138 ARG B CB  
4043 C CG  . ARG B 136 ? 0.5888 0.6034 0.5911 0.0022  0.0450  -0.0573 138 ARG B CG  
4044 C CD  . ARG B 136 ? 0.6519 0.6754 0.6509 0.0074  0.0382  -0.0600 138 ARG B CD  
4045 N NE  . ARG B 136 ? 0.7133 0.7226 0.6958 0.0151  0.0315  -0.0546 138 ARG B NE  
4046 C CZ  . ARG B 136 ? 0.7652 0.7718 0.7379 0.0231  0.0301  -0.0534 138 ARG B CZ  
4047 N NH1 . ARG B 136 ? 0.8009 0.8209 0.7797 0.0249  0.0351  -0.0568 138 ARG B NH1 
4048 N NH2 . ARG B 136 ? 0.7600 0.7504 0.7162 0.0292  0.0238  -0.0488 138 ARG B NH2 
4049 N N   . GLY B 137 ? 0.5212 0.4967 0.5053 0.0054  0.0523  -0.0423 139 GLY B N   
4050 C CA  . GLY B 137 ? 0.5190 0.4958 0.5017 0.0088  0.0574  -0.0417 139 GLY B CA  
4051 C C   . GLY B 137 ? 0.5134 0.4847 0.5014 0.0034  0.0661  -0.0397 139 GLY B C   
4052 O O   . GLY B 137 ? 0.5016 0.4719 0.4872 0.0064  0.0707  -0.0379 139 GLY B O   
4053 N N   . SER B 138 ? 0.5068 0.4738 0.5005 -0.0033 0.0689  -0.0396 140 SER B N   
4054 C CA  . SER B 138 ? 0.5210 0.4830 0.5201 -0.0088 0.0786  -0.0387 140 SER B CA  
4055 C C   . SER B 138 ? 0.5356 0.4820 0.5241 -0.0041 0.0803  -0.0318 140 SER B C   
4056 O O   . SER B 138 ? 0.5573 0.4985 0.5480 -0.0069 0.0889  -0.0302 140 SER B O   
4057 C CB  . SER B 138 ? 0.5197 0.4795 0.5253 -0.0160 0.0810  -0.0406 140 SER B CB  
4058 O OG  . SER B 138 ? 0.5090 0.4574 0.5074 -0.0140 0.0761  -0.0360 140 SER B OG  
4059 N N   . LEU B 139 ? 0.5301 0.4688 0.5069 0.0024  0.0726  -0.0278 141 LEU B N   
4060 C CA  . LEU B 139 ? 0.5440 0.4687 0.5101 0.0072  0.0733  -0.0216 141 LEU B CA  
4061 C C   . LEU B 139 ? 0.5592 0.4835 0.5162 0.0151  0.0704  -0.0206 141 LEU B C   
4062 O O   . LEU B 139 ? 0.5780 0.4909 0.5240 0.0201  0.0685  -0.0160 141 LEU B O   
4063 C CB  . LEU B 139 ? 0.5239 0.4391 0.4829 0.0075  0.0665  -0.0178 141 LEU B CB  
4064 C CG  . LEU B 139 ? 0.5181 0.4328 0.4838 0.0017  0.0691  -0.0179 141 LEU B CG  
4065 C CD1 . LEU B 139 ? 0.5101 0.4179 0.4681 0.0030  0.0620  -0.0133 141 LEU B CD1 
4066 C CD2 . LEU B 139 ? 0.5308 0.4407 0.5003 -0.0006 0.0798  -0.0168 141 LEU B CD2 
4067 N N   . ASP B 140 ? 0.5926 0.5293 0.5532 0.0169  0.0699  -0.0249 142 ASP B N   
4068 C CA  . ASP B 140 ? 0.6510 0.5872 0.6012 0.0259  0.0667  -0.0241 142 ASP B CA  
4069 C C   . ASP B 140 ? 0.6781 0.6141 0.6287 0.0280  0.0755  -0.0217 142 ASP B C   
4070 O O   . ASP B 140 ? 0.6837 0.6277 0.6461 0.0218  0.0845  -0.0232 142 ASP B O   
4071 C CB  . ASP B 140 ? 0.6800 0.6305 0.6326 0.0287  0.0630  -0.0291 142 ASP B CB  
4072 C CG  . ASP B 140 ? 0.7317 0.6805 0.6817 0.0278  0.0543  -0.0306 142 ASP B CG  
4073 O OD1 . ASP B 140 ? 0.6724 0.6084 0.6174 0.0250  0.0498  -0.0274 142 ASP B OD1 
4074 O OD2 . ASP B 140 ? 0.7910 0.7524 0.7436 0.0300  0.0519  -0.0350 142 ASP B OD2 
4075 N N   A ASN B 141 ? 0.6786 0.6042 0.6157 0.0361  0.0731  -0.0178 143 ASN B N   
4076 N N   B ASN B 141 ? 0.6820 0.6080 0.6192 0.0362  0.0731  -0.0179 143 ASN B N   
4077 C CA  A ASN B 141 ? 0.7002 0.6252 0.6353 0.0401  0.0809  -0.0149 143 ASN B CA  
4078 C CA  B ASN B 141 ? 0.7060 0.6311 0.6415 0.0398  0.0812  -0.0149 143 ASN B CA  
4079 C C   A ASN B 141 ? 0.6884 0.6021 0.6240 0.0363  0.0869  -0.0105 143 ASN B C   
4080 C C   B ASN B 141 ? 0.6878 0.6062 0.6292 0.0333  0.0893  -0.0120 143 ASN B C   
4081 O O   A ASN B 141 ? 0.7008 0.6096 0.6312 0.0409  0.0925  -0.0068 143 ASN B O   
4082 O O   B ASN B 141 ? 0.7105 0.6329 0.6576 0.0314  0.0992  -0.0111 143 ASN B O   
4083 C CB  A ASN B 141 ? 0.7183 0.6623 0.6651 0.0383  0.0886  -0.0185 143 ASN B CB  
4084 C CB  B ASN B 141 ? 0.7297 0.6732 0.6729 0.0412  0.0865  -0.0184 143 ASN B CB  
4085 C CG  A ASN B 141 ? 0.7257 0.6732 0.6652 0.0476  0.0913  -0.0165 143 ASN B CG  
4086 C CG  B ASN B 141 ? 0.7241 0.6771 0.6649 0.0457  0.0787  -0.0226 143 ASN B CG  
4087 O OD1 A ASN B 141 ? 0.7272 0.6654 0.6517 0.0571  0.0844  -0.0148 143 ASN B OD1 
4088 O OD1 B ASN B 141 ? 0.7119 0.6818 0.6647 0.0411  0.0803  -0.0275 143 ASN B OD1 
4089 N ND2 A ASN B 141 ? 0.7210 0.6814 0.6702 0.0448  0.1012  -0.0170 143 ASN B ND2 
4090 N ND2 B ASN B 141 ? 0.7185 0.6601 0.6430 0.0547  0.0703  -0.0210 143 ASN B ND2 
4091 N N   . LYS B 142 ? 0.6484 0.5573 0.5882 0.0298  0.0855  -0.0105 144 LYS B N   
4092 C CA  . LYS B 142 ? 0.6181 0.5166 0.5575 0.0274  0.0915  -0.0063 144 LYS B CA  
4093 C C   . LYS B 142 ? 0.5674 0.4535 0.4940 0.0323  0.0837  -0.0022 144 LYS B C   
4094 O O   . LYS B 142 ? 0.5805 0.4658 0.5020 0.0333  0.0740  -0.0034 144 LYS B O   
4095 C CB  . LYS B 142 ? 0.6279 0.5290 0.5787 0.0181  0.0952  -0.0087 144 LYS B CB  
4096 C CG  . LYS B 142 ? 0.6459 0.5610 0.6103 0.0113  0.1008  -0.0143 144 LYS B CG  
4097 C CD  . LYS B 142 ? 0.6702 0.5846 0.6434 0.0026  0.1047  -0.0165 144 LYS B CD  
4098 C CE  . LYS B 142 ? 0.6854 0.5847 0.6540 0.0025  0.1116  -0.0115 144 LYS B CE  
4099 N NZ  . LYS B 142 ? 0.6980 0.5959 0.6750 -0.0061 0.1185  -0.0144 144 LYS B NZ  
4100 N N   . LYS B 143 ? 0.5282 0.4047 0.4488 0.0351  0.0877  0.0025  145 LYS B N   
4101 C CA  . LYS B 143 ? 0.5110 0.3781 0.4180 0.0410  0.0799  0.0061  145 LYS B CA  
4102 C C   . LYS B 143 ? 0.4784 0.3414 0.3859 0.0378  0.0788  0.0086  145 LYS B C   
4103 O O   . LYS B 143 ? 0.4743 0.3368 0.3883 0.0347  0.0872  0.0095  145 LYS B O   
4104 C CB  . LYS B 143 ? 0.5275 0.3879 0.4245 0.0492  0.0839  0.0100  145 LYS B CB  
4105 C CG  . LYS B 143 ? 0.5453 0.4096 0.4387 0.0547  0.0837  0.0082  145 LYS B CG  
4106 C CD  . LYS B 143 ? 0.5636 0.4198 0.4439 0.0640  0.0846  0.0121  145 LYS B CD  
4107 C CE  . LYS B 143 ? 0.5842 0.4442 0.4593 0.0711  0.0846  0.0108  145 LYS B CE  
4108 N NZ  . LYS B 143 ? 0.6116 0.4616 0.4704 0.0811  0.0816  0.0140  145 LYS B NZ  
4109 N N   . GLY B 144 ? 0.4602 0.3199 0.3597 0.0390  0.0689  0.0099  146 GLY B N   
4110 C CA  . GLY B 144 ? 0.4487 0.3064 0.3465 0.0375  0.0665  0.0130  146 GLY B CA  
4111 C C   . GLY B 144 ? 0.4313 0.2954 0.3391 0.0302  0.0653  0.0110  146 GLY B C   
4112 O O   . GLY B 144 ? 0.4161 0.2802 0.3238 0.0296  0.0656  0.0139  146 GLY B O   
4113 N N   . HIS B 145 ? 0.4136 0.2839 0.3291 0.0258  0.0639  0.0063  147 HIS B N   
4114 C CA  . HIS B 145 ? 0.4053 0.2824 0.3307 0.0192  0.0633  0.0039  147 HIS B CA  
4115 C C   . HIS B 145 ? 0.3778 0.2585 0.3016 0.0167  0.0528  0.0021  147 HIS B C   
4116 O O   . HIS B 145 ? 0.3766 0.2537 0.2923 0.0198  0.0472  0.0016  147 HIS B O   
4117 C CB  . HIS B 145 ? 0.4210 0.3032 0.3575 0.0155  0.0717  -0.0001 147 HIS B CB  
4118 C CG  . HIS B 145 ? 0.4450 0.3218 0.3828 0.0164  0.0829  0.0017  147 HIS B CG  
4119 N ND1 . HIS B 145 ? 0.4583 0.3290 0.3937 0.0173  0.0867  0.0055  147 HIS B ND1 
4120 C CD2 . HIS B 145 ? 0.4597 0.3362 0.4007 0.0163  0.0916  0.0006  147 HIS B CD2 
4121 C CE1 . HIS B 145 ? 0.4690 0.3334 0.4047 0.0181  0.0973  0.0068  147 HIS B CE1 
4122 N NE2 . HIS B 145 ? 0.4806 0.3487 0.4202 0.0167  0.1005  0.0038  147 HIS B NE2 
4123 N N   . ALA B 146 ? 0.3590 0.2453 0.2891 0.0117  0.0506  0.0012  148 ALA B N   
4124 C CA  . ALA B 146 ? 0.3433 0.2329 0.2721 0.0089  0.0415  -0.0002 148 ALA B CA  
4125 C C   . ALA B 146 ? 0.3391 0.2376 0.2789 0.0041  0.0429  -0.0036 148 ALA B C   
4126 O O   . ALA B 146 ? 0.3368 0.2378 0.2835 0.0023  0.0493  -0.0036 148 ALA B O   
4127 C CB  . ALA B 146 ? 0.3415 0.2281 0.2623 0.0082  0.0340  0.0040  148 ALA B CB  
4128 N N   . TYR B 147 ? 0.3319 0.2342 0.2719 0.0027  0.0371  -0.0065 149 TYR B N   
4129 C CA  . TYR B 147 ? 0.3273 0.2387 0.2762 -0.0013 0.0366  -0.0097 149 TYR B CA  
4130 C C   . TYR B 147 ? 0.3131 0.2260 0.2610 -0.0043 0.0321  -0.0059 149 TYR B C   
4131 O O   . TYR B 147 ? 0.3079 0.2160 0.2471 -0.0043 0.0258  -0.0017 149 TYR B O   
4132 C CB  . TYR B 147 ? 0.3346 0.2497 0.2826 -0.0002 0.0323  -0.0137 149 TYR B CB  
4133 C CG  . TYR B 147 ? 0.3521 0.2704 0.3029 0.0027  0.0373  -0.0177 149 TYR B CG  
4134 C CD1 . TYR B 147 ? 0.3510 0.2799 0.3138 0.0002  0.0434  -0.0227 149 TYR B CD1 
4135 C CD2 . TYR B 147 ? 0.3653 0.2769 0.3067 0.0081  0.0359  -0.0166 149 TYR B CD2 
4136 C CE1 . TYR B 147 ? 0.3638 0.2984 0.3302 0.0021  0.0481  -0.0263 149 TYR B CE1 
4137 C CE2 . TYR B 147 ? 0.3667 0.2835 0.3109 0.0114  0.0407  -0.0199 149 TYR B CE2 
4138 C CZ  . TYR B 147 ? 0.3711 0.3005 0.3284 0.0080  0.0468  -0.0246 149 TYR B CZ  
4139 O OH  . TYR B 147 ? 0.3988 0.3362 0.3598 0.0104  0.0514  -0.0279 149 TYR B OH  
4140 N N   . THR B 148 ? 0.3102 0.2303 0.2670 -0.0070 0.0355  -0.0075 150 THR B N   
4141 C CA  . THR B 148 ? 0.2960 0.2208 0.2536 -0.0094 0.0321  -0.0043 150 THR B CA  
4142 C C   . THR B 148 ? 0.2823 0.2113 0.2388 -0.0115 0.0248  -0.0054 150 THR B C   
4143 O O   . THR B 148 ? 0.2766 0.2079 0.2357 -0.0109 0.0249  -0.0100 150 THR B O   
4144 C CB  . THR B 148 ? 0.2941 0.2237 0.2596 -0.0102 0.0385  -0.0055 150 THR B CB  
4145 O OG1 . THR B 148 ? 0.2876 0.2227 0.2521 -0.0114 0.0342  -0.0015 150 THR B OG1 
4146 C CG2 . THR B 148 ? 0.2967 0.2320 0.2708 -0.0122 0.0415  -0.0121 150 THR B CG2 
4147 N N   . SER B 149 ? 0.2839 0.2137 0.2357 -0.0137 0.0188  -0.0008 151 SER B N   
4148 C CA  . SER B 149 ? 0.2846 0.2196 0.2364 -0.0165 0.0131  -0.0005 151 SER B CA  
4149 C C   . SER B 149 ? 0.2770 0.2218 0.2393 -0.0167 0.0175  -0.0045 151 SER B C   
4150 O O   . SER B 149 ? 0.2644 0.2118 0.2321 -0.0160 0.0234  -0.0046 151 SER B O   
4151 C CB  . SER B 149 ? 0.2896 0.2266 0.2369 -0.0200 0.0077  0.0055  151 SER B CB  
4152 O OG  . SER B 149 ? 0.2968 0.2242 0.2331 -0.0214 0.0018  0.0081  151 SER B OG  
4153 N N   . PHE B 150 ? 0.2839 0.2326 0.2478 -0.0168 0.0151  -0.0080 152 PHE B N   
4154 C CA  . PHE B 150 ? 0.2889 0.2477 0.2621 -0.0169 0.0183  -0.0125 152 PHE B CA  
4155 C C   . PHE B 150 ? 0.2828 0.2475 0.2582 -0.0185 0.0182  -0.0084 152 PHE B C   
4156 O O   . PHE B 150 ? 0.2789 0.2442 0.2490 -0.0204 0.0129  -0.0027 152 PHE B O   
4157 C CB  . PHE B 150 ? 0.2986 0.2617 0.2715 -0.0159 0.0145  -0.0161 152 PHE B CB  
4158 C CG  . PHE B 150 ? 0.3134 0.2722 0.2829 -0.0130 0.0143  -0.0197 152 PHE B CG  
4159 C CD1 . PHE B 150 ? 0.3229 0.2794 0.2955 -0.0119 0.0198  -0.0225 152 PHE B CD1 
4160 C CD2 . PHE B 150 ? 0.3222 0.2787 0.2840 -0.0108 0.0086  -0.0196 152 PHE B CD2 
4161 C CE1 . PHE B 150 ? 0.3393 0.2937 0.3084 -0.0085 0.0196  -0.0253 152 PHE B CE1 
4162 C CE2 . PHE B 150 ? 0.3425 0.2955 0.2997 -0.0065 0.0083  -0.0226 152 PHE B CE2 
4163 C CZ  . PHE B 150 ? 0.3497 0.3028 0.3110 -0.0053 0.0137  -0.0255 152 PHE B CZ  
4164 N N   . MET B 151 ? 0.2794 0.2476 0.2615 -0.0177 0.0244  -0.0110 153 MET B N   
4165 C CA  . MET B 151 ? 0.2866 0.2603 0.2700 -0.0174 0.0255  -0.0073 153 MET B CA  
4166 C C   . MET B 151 ? 0.2833 0.2657 0.2726 -0.0172 0.0264  -0.0115 153 MET B C   
4167 O O   . MET B 151 ? 0.2878 0.2696 0.2823 -0.0169 0.0313  -0.0181 153 MET B O   
4168 C CB  . MET B 151 ? 0.2963 0.2643 0.2797 -0.0154 0.0323  -0.0065 153 MET B CB  
4169 C CG  . MET B 151 ? 0.3015 0.2635 0.2782 -0.0148 0.0307  -0.0010 153 MET B CG  
4170 S SD  . MET B 151 ? 0.3203 0.2741 0.2954 -0.0109 0.0392  0.0000  153 MET B SD  
4171 C CE  . MET B 151 ? 0.3211 0.2689 0.3019 -0.0122 0.0457  -0.0082 153 MET B CE  
4172 N N   . LEU B 152 ? 0.2809 0.2717 0.2695 -0.0175 0.0222  -0.0078 154 LEU B N   
4173 C CA  . LEU B 152 ? 0.2859 0.2859 0.2794 -0.0161 0.0233  -0.0111 154 LEU B CA  
4174 C C   . LEU B 152 ? 0.3075 0.3097 0.3013 -0.0135 0.0275  -0.0084 154 LEU B C   
4175 O O   . LEU B 152 ? 0.3125 0.3167 0.3025 -0.0132 0.0259  -0.0013 154 LEU B O   
4176 C CB  . LEU B 152 ? 0.2726 0.2802 0.2643 -0.0170 0.0170  -0.0082 154 LEU B CB  
4177 C CG  . LEU B 152 ? 0.2706 0.2768 0.2617 -0.0173 0.0140  -0.0128 154 LEU B CG  
4178 C CD1 . LEU B 152 ? 0.2745 0.2852 0.2611 -0.0181 0.0079  -0.0084 154 LEU B CD1 
4179 C CD2 . LEU B 152 ? 0.2690 0.2803 0.2670 -0.0155 0.0176  -0.0215 154 LEU B CD2 
4180 N N   . GLN B 153 ? 0.3351 0.3358 0.3323 -0.0117 0.0330  -0.0140 155 GLN B N   
4181 C CA  . GLN B 153 ? 0.3685 0.3685 0.3637 -0.0078 0.0377  -0.0119 155 GLN B CA  
4182 C C   . GLN B 153 ? 0.3719 0.3767 0.3701 -0.0059 0.0395  -0.0176 155 GLN B C   
4183 O O   . GLN B 153 ? 0.3742 0.3770 0.3765 -0.0083 0.0407  -0.0253 155 GLN B O   
4184 C CB  . GLN B 153 ? 0.3967 0.3834 0.3894 -0.0071 0.0440  -0.0126 155 GLN B CB  
4185 C CG  . GLN B 153 ? 0.4347 0.4175 0.4229 -0.0017 0.0497  -0.0102 155 GLN B CG  
4186 C CD  . GLN B 153 ? 0.4522 0.4449 0.4365 0.0019  0.0465  -0.0015 155 GLN B CD  
4187 O OE1 . GLN B 153 ? 0.4609 0.4547 0.4428 0.0009  0.0436  0.0039  155 GLN B OE1 
4188 N NE2 . GLN B 153 ? 0.4511 0.4521 0.4344 0.0062  0.0468  -0.0002 155 GLN B NE2 
4189 N N   . VAL B 154 ? 0.3883 0.4005 0.3843 -0.0017 0.0395  -0.0140 156 VAL B N   
4190 C CA  . VAL B 154 ? 0.4131 0.4270 0.4097 0.0016  0.0425  -0.0193 156 VAL B CA  
4191 C C   . VAL B 154 ? 0.4521 0.4511 0.4452 0.0034  0.0503  -0.0228 156 VAL B C   
4192 O O   . VAL B 154 ? 0.4682 0.4616 0.4564 0.0061  0.0529  -0.0172 156 VAL B O   
4193 C CB  . VAL B 154 ? 0.4170 0.4437 0.4111 0.0069  0.0404  -0.0136 156 VAL B CB  
4194 C CG1 . VAL B 154 ? 0.4214 0.4486 0.4149 0.0109  0.0432  -0.0199 156 VAL B CG1 
4195 C CG2 . VAL B 154 ? 0.4002 0.4409 0.3963 0.0046  0.0333  -0.0082 156 VAL B CG2 
4196 N N   . ALA B 155 ? 0.5213 0.5144 0.5159 0.0024  0.0538  -0.0315 157 ALA B N   
4197 C CA  . ALA B 155 ? 0.5885 0.5650 0.5782 0.0034  0.0617  -0.0353 157 ALA B CA  
4198 C C   . ALA B 155 ? 0.6339 0.6080 0.6150 0.0118  0.0648  -0.0316 157 ALA B C   
4199 O O   . ALA B 155 ? 0.6404 0.6183 0.6203 0.0148  0.0645  -0.0352 157 ALA B O   
4200 C CB  . ALA B 155 ? 0.6073 0.5792 0.6013 -0.0016 0.0639  -0.0462 157 ALA B CB  
4201 N N   . LYS B 156 ? 0.6755 0.6457 0.6505 0.0163  0.0671  -0.0239 158 LYS B N   
4202 C CA  . LYS B 156 ? 0.7215 0.6850 0.6861 0.0254  0.0721  -0.0207 158 LYS B CA  
4203 C C   . LYS B 156 ? 0.7610 0.7038 0.7190 0.0257  0.0796  -0.0209 158 LYS B C   
4204 O O   . LYS B 156 ? 0.8173 0.7546 0.7802 0.0186  0.0800  -0.0227 158 LYS B O   
4205 C CB  . LYS B 156 ? 0.7333 0.7124 0.6952 0.0321  0.0686  -0.0104 158 LYS B CB  
4206 C CG  . LYS B 156 ? 0.7471 0.7466 0.7172 0.0278  0.0601  -0.0060 158 LYS B CG  
4207 C CD  . LYS B 156 ? 0.7887 0.8047 0.7559 0.0338  0.0573  0.0039  158 LYS B CD  
4208 C CE  . LYS B 156 ? 0.7796 0.8075 0.7514 0.0283  0.0511  0.0104  158 LYS B CE  
4209 N NZ  . LYS B 156 ? 0.7878 0.8260 0.7669 0.0216  0.0446  0.0092  158 LYS B NZ  
4210 N N   . ASP B 157 ? 0.7897 0.7215 0.7362 0.0343  0.0855  -0.0186 159 ASP B N   
4211 C CA  . ASP B 157 ? 0.8249 0.7378 0.7626 0.0371  0.0928  -0.0161 159 ASP B CA  
4212 C C   . ASP B 157 ? 0.8114 0.7373 0.7486 0.0416  0.0894  -0.0060 159 ASP B C   
4213 O O   . ASP B 157 ? 0.8186 0.7473 0.7469 0.0518  0.0912  0.0000  159 ASP B O   
4214 C CB  . ASP B 157 ? 0.8729 0.7659 0.7967 0.0443  0.1009  -0.0188 159 ASP B CB  
4215 C CG  . ASP B 157 ? 0.9051 0.7818 0.8295 0.0368  0.1047  -0.0297 159 ASP B CG  
4216 O OD1 . ASP B 157 ? 0.8913 0.7753 0.8279 0.0265  0.1009  -0.0353 159 ASP B OD1 
4217 O OD2 . ASP B 157 ? 0.9497 0.8061 0.8617 0.0411  0.1116  -0.0328 159 ASP B OD2 
4218 N N   . THR B 158 ? 0.7939 0.7281 0.7400 0.0343  0.0844  -0.0047 160 THR B N   
4219 C CA  . THR B 158 ? 0.7701 0.7190 0.7175 0.0360  0.0792  0.0038  160 THR B CA  
4220 C C   . THR B 158 ? 0.7632 0.7017 0.7102 0.0326  0.0812  0.0049  160 THR B C   
4221 O O   . THR B 158 ? 0.7973 0.7217 0.7465 0.0268  0.0850  -0.0009 160 THR B O   
4222 C CB  . THR B 158 ? 0.7515 0.7212 0.7086 0.0307  0.0700  0.0046  160 THR B CB  
4223 O OG1 . THR B 158 ? 0.7587 0.7436 0.7155 0.0327  0.0651  0.0130  160 THR B OG1 
4224 C CG2 . THR B 158 ? 0.7408 0.7091 0.7068 0.0206  0.0665  -0.0006 160 THR B CG2 
4225 N N   . THR B 159 ? 0.7144 0.6613 0.6589 0.0360  0.0784  0.0124  161 THR B N   
4226 C CA  . THR B 159 ? 0.6771 0.6179 0.6213 0.0332  0.0786  0.0143  161 THR B CA  
4227 C C   . THR B 159 ? 0.6028 0.5605 0.5538 0.0277  0.0690  0.0176  161 THR B C   
4228 O O   . THR B 159 ? 0.5547 0.5284 0.5048 0.0306  0.0643  0.0233  161 THR B O   
4229 C CB  . THR B 159 ? 0.6918 0.6252 0.6250 0.0426  0.0841  0.0200  161 THR B CB  
4230 O OG1 . THR B 159 ? 0.7155 0.6285 0.6412 0.0465  0.0936  0.0164  161 THR B OG1 
4231 C CG2 . THR B 159 ? 0.6920 0.6215 0.6243 0.0409  0.0835  0.0226  161 THR B CG2 
4232 N N   . VAL B 160 ? 0.5651 0.5186 0.5214 0.0200  0.0664  0.0141  162 VAL B N   
4233 C CA  . VAL B 160 ? 0.5224 0.4874 0.4826 0.0147  0.0576  0.0168  162 VAL B CA  
4234 C C   . VAL B 160 ? 0.4925 0.4471 0.4505 0.0129  0.0584  0.0168  162 VAL B C   
4235 O O   . VAL B 160 ? 0.4711 0.4120 0.4295 0.0118  0.0642  0.0122  162 VAL B O   
4236 C CB  . VAL B 160 ? 0.5137 0.4856 0.4815 0.0081  0.0524  0.0126  162 VAL B CB  
4237 C CG1 . VAL B 160 ? 0.5076 0.4680 0.4795 0.0046  0.0566  0.0044  162 VAL B CG1 
4238 C CG2 . VAL B 160 ? 0.5025 0.4828 0.4721 0.0026  0.0436  0.0155  162 VAL B CG2 
4239 N N   . ALA B 161 ? 0.4781 0.4397 0.4339 0.0121  0.0524  0.0217  163 ALA B N   
4240 C CA  . ALA B 161 ? 0.4825 0.4352 0.4350 0.0111  0.0522  0.0220  163 ALA B CA  
4241 C C   . ALA B 161 ? 0.4619 0.4107 0.4191 0.0042  0.0485  0.0171  163 ALA B C   
4242 O O   . ALA B 161 ? 0.4391 0.3966 0.3997 -0.0004 0.0417  0.0168  163 ALA B O   
4243 C CB  . ALA B 161 ? 0.4835 0.4450 0.4312 0.0126  0.0467  0.0282  163 ALA B CB  
4244 N N   . VAL B 162 ? 0.4462 0.3829 0.4027 0.0041  0.0530  0.0139  164 VAL B N   
4245 C CA  . VAL B 162 ? 0.4245 0.3586 0.3847 -0.0009 0.0499  0.0093  164 VAL B CA  
4246 C C   . VAL B 162 ? 0.4117 0.3490 0.3677 -0.0030 0.0411  0.0125  164 VAL B C   
4247 O O   . VAL B 162 ? 0.4269 0.3623 0.3768 -0.0002 0.0406  0.0166  164 VAL B O   
4248 C CB  . VAL B 162 ? 0.4152 0.3374 0.3752 -0.0001 0.0571  0.0059  164 VAL B CB  
4249 C CG1 . VAL B 162 ? 0.4149 0.3307 0.3672 0.0038  0.0579  0.0103  164 VAL B CG1 
4250 C CG2 . VAL B 162 ? 0.4050 0.3280 0.3703 -0.0046 0.0549  0.0003  164 VAL B CG2 
4251 N N   . LYS B 163 ? 0.4075 0.3478 0.3654 -0.0075 0.0349  0.0103  165 LYS B N   
4252 C CA  . LYS B 163 ? 0.4191 0.3606 0.3715 -0.0105 0.0261  0.0132  165 LYS B CA  
4253 C C   . LYS B 163 ? 0.4395 0.3700 0.3867 -0.0095 0.0256  0.0113  165 LYS B C   
4254 O O   . LYS B 163 ? 0.4300 0.3572 0.3748 -0.0117 0.0208  0.0091  165 LYS B O   
4255 C CB  . LYS B 163 ? 0.4438 0.3926 0.3992 -0.0149 0.0206  0.0125  165 LYS B CB  
4256 C CG  . LYS B 163 ? 0.4796 0.4404 0.4365 -0.0159 0.0185  0.0171  165 LYS B CG  
4257 C CD  . LYS B 163 ? 0.5349 0.5021 0.4924 -0.0209 0.0119  0.0180  165 LYS B CD  
4258 C CE  . LYS B 163 ? 0.5784 0.5404 0.5279 -0.0255 0.0043  0.0206  165 LYS B CE  
4259 N NZ  . LYS B 163 ? 0.6037 0.5750 0.5528 -0.0310 -0.0014 0.0246  165 LYS B NZ  
4260 N N   . ALA B 164 ? 0.4823 0.4027 0.4032 0.0159  0.0504  0.0053  166 ALA B N   
4261 C CA  . ALA B 164 ? 0.4842 0.4112 0.4113 0.0109  0.0470  0.0040  166 ALA B CA  
4262 C C   . ALA B 164 ? 0.4748 0.4043 0.4069 0.0145  0.0477  0.0061  166 ALA B C   
4263 O O   . ALA B 164 ? 0.5234 0.4432 0.4474 0.0185  0.0511  0.0073  166 ALA B O   
4264 C CB  . ALA B 164 ? 0.4987 0.4165 0.4149 0.0041  0.0466  0.0010  166 ALA B CB  
4265 N N   . ASP B 165 ? 0.4459 0.3873 0.3897 0.0137  0.0449  0.0068  167 ASP B N   
4266 C CA  . ASP B 165 ? 0.4319 0.3757 0.3796 0.0156  0.0450  0.0083  167 ASP B CA  
4267 C C   . ASP B 165 ? 0.3888 0.3405 0.3438 0.0110  0.0413  0.0070  167 ASP B C   
4268 O O   . ASP B 165 ? 0.3718 0.3284 0.3297 0.0076  0.0390  0.0057  167 ASP B O   
4269 C CB  . ASP B 165 ? 0.4531 0.4044 0.4074 0.0215  0.0464  0.0116  167 ASP B CB  
4270 C CG  . ASP B 165 ? 0.4758 0.4275 0.4303 0.0253  0.0479  0.0137  167 ASP B CG  
4271 O OD1 . ASP B 165 ? 0.5149 0.4569 0.4616 0.0243  0.0488  0.0126  167 ASP B OD1 
4272 O OD2 . ASP B 165 ? 0.4669 0.4289 0.4287 0.0290  0.0482  0.0167  167 ASP B OD2 
4273 N N   . VAL B 166 ? 0.3770 0.3301 0.3345 0.0115  0.0411  0.0077  168 VAL B N   
4274 C CA  . VAL B 166 ? 0.3464 0.3066 0.3105 0.0078  0.0379  0.0068  168 VAL B CA  
4275 C C   . VAL B 166 ? 0.3206 0.2882 0.2926 0.0109  0.0375  0.0089  168 VAL B C   
4276 O O   . VAL B 166 ? 0.3267 0.2927 0.2972 0.0151  0.0398  0.0109  168 VAL B O   
4277 C CB  . VAL B 166 ? 0.3468 0.3008 0.3046 0.0039  0.0376  0.0051  168 VAL B CB  
4278 C CG1 . VAL B 166 ? 0.3574 0.3058 0.3071 -0.0006 0.0376  0.0029  168 VAL B CG1 
4279 C CG2 . VAL B 166 ? 0.3637 0.3091 0.3154 0.0070  0.0405  0.0062  168 VAL B CG2 
4280 N N   . PRO B 167 ? 0.2972 0.2730 0.2767 0.0089  0.0349  0.0087  169 PRO B N   
4281 C CA  . PRO B 167 ? 0.2949 0.2772 0.2808 0.0101  0.0341  0.0102  169 PRO B CA  
4282 C C   . PRO B 167 ? 0.2803 0.2594 0.2638 0.0101  0.0343  0.0101  169 PRO B C   
4283 O O   . PRO B 167 ? 0.2800 0.2526 0.2577 0.0080  0.0346  0.0085  169 PRO B O   
4284 C CB  . PRO B 167 ? 0.2812 0.2691 0.2722 0.0075  0.0316  0.0095  169 PRO B CB  
4285 C CG  . PRO B 167 ? 0.2757 0.2608 0.2630 0.0050  0.0307  0.0075  169 PRO B CG  
4286 C CD  . PRO B 167 ? 0.2888 0.2678 0.2700 0.0058  0.0327  0.0072  169 PRO B CD  
4287 N N   . THR B 168 ? 0.2739 0.2580 0.2614 0.0120  0.0343  0.0118  170 THR B N   
4288 C CA  . THR B 168 ? 0.2782 0.2603 0.2642 0.0121  0.0343  0.0118  170 THR B CA  
4289 C C   . THR B 168 ? 0.2608 0.2510 0.2539 0.0105  0.0318  0.0119  170 THR B C   
4290 O O   . THR B 168 ? 0.2492 0.2463 0.2475 0.0102  0.0308  0.0128  170 THR B O   
4291 C CB  . THR B 168 ? 0.2949 0.2735 0.2765 0.0172  0.0374  0.0140  170 THR B CB  
4292 O OG1 . THR B 168 ? 0.2953 0.2844 0.2833 0.0201  0.0374  0.0166  170 THR B OG1 
4293 C CG2 . THR B 168 ? 0.3186 0.2868 0.2910 0.0194  0.0405  0.0140  170 THR B CG2 
4294 N N   . LEU B 169 ? 0.2536 0.2422 0.2459 0.0091  0.0309  0.0111  171 LEU B N   
4295 C CA  . LEU B 169 ? 0.2345 0.2294 0.2320 0.0078  0.0287  0.0112  171 LEU B CA  
4296 C C   . LEU B 169 ? 0.2372 0.2314 0.2336 0.0097  0.0294  0.0122  171 LEU B C   
4297 O O   . LEU B 169 ? 0.2277 0.2146 0.2184 0.0097  0.0307  0.0117  171 LEU B O   
4298 C CB  . LEU B 169 ? 0.2219 0.2170 0.2202 0.0044  0.0265  0.0092  171 LEU B CB  
4299 C CG  . LEU B 169 ? 0.2175 0.2178 0.2201 0.0034  0.0246  0.0092  171 LEU B CG  
4300 C CD1 . LEU B 169 ? 0.2132 0.2162 0.2179 0.0030  0.0243  0.0096  171 LEU B CD1 
4301 C CD2 . LEU B 169 ? 0.2144 0.2147 0.2163 0.0017  0.0231  0.0079  171 LEU B CD2 
4302 N N   . THR B 170 ? 0.2425 0.2441 0.2432 0.0113  0.0290  0.0139  172 THR B N   
4303 C CA  . THR B 170 ? 0.2619 0.2651 0.2622 0.0138  0.0296  0.0154  172 THR B CA  
4304 C C   . THR B 170 ? 0.2546 0.2644 0.2599 0.0111  0.0269  0.0149  172 THR B C   
4305 O O   . THR B 170 ? 0.2725 0.2885 0.2818 0.0091  0.0254  0.0149  172 THR B O   
4306 C CB  . THR B 170 ? 0.2827 0.2901 0.2826 0.0189  0.0320  0.0185  172 THR B CB  
4307 O OG1 . THR B 170 ? 0.3289 0.3268 0.3219 0.0214  0.0348  0.0185  172 THR B OG1 
4308 C CG2 . THR B 170 ? 0.3025 0.3132 0.3020 0.0225  0.0329  0.0206  172 THR B CG2 
4309 N N   . LYS B 171 ? 0.2382 0.2456 0.2423 0.0107  0.0264  0.0143  173 LYS B N   
4310 C CA  . LYS B 171 ? 0.2315 0.2444 0.2391 0.0090  0.0241  0.0140  173 LYS B CA  
4311 C C   . LYS B 171 ? 0.2398 0.2561 0.2474 0.0121  0.0249  0.0160  173 LYS B C   
4312 O O   . LYS B 171 ? 0.2332 0.2434 0.2364 0.0148  0.0270  0.0167  173 LYS B O   
4313 C CB  . LYS B 171 ? 0.2205 0.2296 0.2272 0.0062  0.0226  0.0119  173 LYS B CB  
4314 C CG  . LYS B 171 ? 0.2114 0.2247 0.2205 0.0050  0.0207  0.0117  173 LYS B CG  
4315 C CD  . LYS B 171 ? 0.2075 0.2182 0.2155 0.0034  0.0195  0.0101  173 LYS B CD  
4316 C CE  . LYS B 171 ? 0.2060 0.2195 0.2151 0.0023  0.0178  0.0098  173 LYS B CE  
4317 N NZ  . LYS B 171 ? 0.2017 0.2134 0.2093 0.0020  0.0171  0.0089  173 LYS B NZ  
4318 N N   . GLN B 172 ? 0.2561 0.2817 0.2677 0.0115  0.0235  0.0171  174 GLN B N   
4319 C CA  . GLN B 172 ? 0.2741 0.3056 0.2864 0.0144  0.0238  0.0192  174 GLN B CA  
4320 C C   . GLN B 172 ? 0.2703 0.3084 0.2857 0.0110  0.0210  0.0185  174 GLN B C   
4321 O O   . GLN B 172 ? 0.2539 0.2925 0.2704 0.0065  0.0192  0.0169  174 GLN B O   
4322 C CB  . GLN B 172 ? 0.2997 0.3387 0.3127 0.0187  0.0257  0.0224  174 GLN B CB  
4323 C CG  . GLN B 172 ? 0.3230 0.3532 0.3304 0.0236  0.0292  0.0234  174 GLN B CG  
4324 C CD  . GLN B 172 ? 0.3417 0.3805 0.3491 0.0295  0.0316  0.0274  174 GLN B CD  
4325 O OE1 . GLN B 172 ? 0.3368 0.3861 0.3486 0.0284  0.0308  0.0285  174 GLN B OE1 
4326 N NE2 . GLN B 172 ? 0.3580 0.3931 0.3601 0.0359  0.0346  0.0297  174 GLN B NE2 
4327 N N   . VAL B 173 ? 0.2772 0.3187 0.2925 0.0134  0.0211  0.0199  175 VAL B N   
4328 C CA  . VAL B 173 ? 0.2826 0.3299 0.2997 0.0105  0.0187  0.0194  175 VAL B CA  
4329 C C   . VAL B 173 ? 0.3055 0.3661 0.3251 0.0127  0.0189  0.0225  175 VAL B C   
4330 O O   . VAL B 173 ? 0.2948 0.3568 0.3131 0.0186  0.0214  0.0252  175 VAL B O   
4331 C CB  . VAL B 173 ? 0.2810 0.3222 0.2961 0.0111  0.0184  0.0183  175 VAL B CB  
4332 C CG1 . VAL B 173 ? 0.2876 0.3264 0.3000 0.0166  0.0209  0.0204  175 VAL B CG1 
4333 C CG2 . VAL B 173 ? 0.2763 0.3224 0.2923 0.0081  0.0159  0.0176  175 VAL B CG2 
4334 N N   . ARG B 174 ? 0.3521 0.4215 0.3738 0.0079  0.0165  0.0223  176 ARG B N   
4335 C CA  . ARG B 174 ? 0.4074 0.4928 0.4318 0.0091  0.0162  0.0255  176 ARG B CA  
4336 C C   . ARG B 174 ? 0.4393 0.5269 0.4629 0.0127  0.0162  0.0266  176 ARG B C   
4337 O O   . ARG B 174 ? 0.4236 0.5056 0.4458 0.0096  0.0145  0.0242  176 ARG B O   
4338 C CB  . ARG B 174 ? 0.4417 0.5362 0.4675 0.0014  0.0136  0.0248  176 ARG B CB  
4339 C CG  . ARG B 174 ? 0.4773 0.5901 0.5066 0.0024  0.0140  0.0287  176 ARG B CG  
4340 C CD  . ARG B 174 ? 0.5129 0.6355 0.5428 -0.0066 0.0114  0.0280  176 ARG B CD  
4341 N NE  . ARG B 174 ? 0.5413 0.6672 0.5697 -0.0107 0.0091  0.0270  176 ARG B NE  
4342 C CZ  . ARG B 174 ? 0.5747 0.7058 0.6011 -0.0200 0.0066  0.0257  176 ARG B CZ  
4343 N NH1 . ARG B 174 ? 0.5979 0.7317 0.6238 -0.0263 0.0063  0.0254  176 ARG B NH1 
4344 N NH2 . ARG B 174 ? 0.5812 0.7140 0.6053 -0.0233 0.0046  0.0246  176 ARG B NH2 
4345 N N   . ALA B 175 ? 0.4737 0.5685 0.4975 0.0198  0.0185  0.0304  177 ALA B N   
4346 C CA  . ALA B 175 ? 0.4917 0.5869 0.5136 0.0250  0.0195  0.0321  177 ALA B CA  
4347 C C   . ALA B 175 ? 0.5201 0.6270 0.5443 0.0208  0.0164  0.0320  177 ALA B C   
4348 O O   . ALA B 175 ? 0.4959 0.6139 0.5228 0.0148  0.0141  0.0319  177 ALA B O   
4349 C CB  . ALA B 175 ? 0.4976 0.5977 0.5177 0.0343  0.0232  0.0366  177 ALA B CB  
4350 N N   . ASN B 176 ? 0.5611 0.6648 0.5834 0.0234  0.0165  0.0321  178 ASN B N   
4351 C CA  . ASN B 176 ? 0.6873 0.8019 0.7109 0.0205  0.0138  0.0323  178 ASN B CA  
4352 C C   . ASN B 176 ? 0.7508 0.8870 0.7775 0.0224  0.0137  0.0366  178 ASN B C   
4353 O O   . ASN B 176 ? 0.7627 0.9047 0.7888 0.0315  0.0166  0.0408  178 ASN B O   
4354 C CB  . ASN B 176 ? 0.6952 0.8016 0.7158 0.0243  0.0146  0.0321  178 ASN B CB  
4355 C CG  . ASN B 176 ? 0.7006 0.8121 0.7213 0.0197  0.0115  0.0307  178 ASN B CG  
4356 O OD1 . ASN B 176 ? 0.7105 0.8328 0.7327 0.0136  0.0088  0.0302  178 ASN B OD1 
4357 N ND2 . ASN B 176 ? 0.6633 0.7665 0.6815 0.0223  0.0121  0.0300  178 ASN B ND2 
4358 N N   . GLY B 177 ? 0.7604 0.9082 0.7896 0.0143  0.0108  0.0358  179 GLY B N   
4359 C CA  . GLY B 177 ? 0.7749 0.9467 0.8074 0.0132  0.0096  0.0395  179 GLY B CA  
4360 C C   . GLY B 177 ? 0.8025 0.9848 0.8370 0.0220  0.0129  0.0445  179 GLY B C   
4361 O O   . GLY B 177 ? 0.8379 1.0346 0.8732 0.0289  0.0141  0.0490  179 GLY B O   
4362 N N   . SER B 178 ? 0.8107 0.9857 0.8454 0.0225  0.0146  0.0440  180 SER B N   
4363 C CA  . SER B 178 ? 0.8242 1.0040 0.8590 0.0319  0.0185  0.0484  180 SER B CA  
4364 C C   . SER B 178 ? 0.8411 1.0239 0.8783 0.0269  0.0181  0.0478  180 SER B C   
4365 O O   . SER B 178 ? 0.9445 1.1341 0.9822 0.0336  0.0210  0.0516  180 SER B O   
4366 C CB  . SER B 178 ? 0.8469 1.0056 0.8763 0.0400  0.0221  0.0478  180 SER B CB  
4367 O OG  . SER B 178 ? 0.8177 0.9770 0.8446 0.0496  0.0265  0.0518  180 SER B OG  
4368 N N   . GLN B 179 ? 0.8453 1.0214 0.8829 0.0160  0.0150  0.0433  181 GLN B N   
4369 C CA  . GLN B 179 ? 0.8463 1.0209 0.8850 0.0099  0.0145  0.0418  181 GLN B CA  
4370 C C   . GLN B 179 ? 0.7661 0.9270 0.8030 0.0170  0.0181  0.0420  181 GLN B C   
4371 O O   . GLN B 179 ? 0.7484 0.9087 0.7862 0.0136  0.0182  0.0414  181 GLN B O   
4372 C CB  . GLN B 179 ? 0.9202 1.1201 0.9631 0.0065  0.0136  0.0456  181 GLN B CB  
4373 C CG  . GLN B 179 ? 0.9775 1.1863 1.0204 -0.0061 0.0095  0.0435  181 GLN B CG  
4374 C CD  . GLN B 179 ? 1.0196 1.2255 1.0604 -0.0073 0.0076  0.0418  181 GLN B CD  
4375 O OE1 . GLN B 179 ? 1.0466 1.2335 1.0834 -0.0113 0.0065  0.0371  181 GLN B OE1 
4376 N NE2 . GLN B 179 ? 1.0645 1.2895 1.1076 -0.0030 0.0075  0.0459  181 GLN B NE2 
4377 N N   . ASN B 180 ? 0.7130 0.8625 0.7465 0.0257  0.0208  0.0427  182 ASN B N   
4378 C CA  . ASN B 180 ? 0.6732 0.8094 0.7031 0.0327  0.0246  0.0432  182 ASN B CA  
4379 C C   . ASN B 180 ? 0.5873 0.7010 0.6138 0.0293  0.0242  0.0382  182 ASN B C   
4380 O O   . ASN B 180 ? 0.6100 0.7173 0.6355 0.0269  0.0226  0.0359  182 ASN B O   
4381 C CB  . ASN B 180 ? 0.7215 0.8585 0.7474 0.0445  0.0287  0.0475  182 ASN B CB  
4382 C CG  . ASN B 180 ? 0.8003 0.9564 0.8283 0.0505  0.0308  0.0531  182 ASN B CG  
4383 O OD1 . ASN B 180 ? 0.8603 1.0340 0.8940 0.0447  0.0283  0.0540  182 ASN B OD1 
4384 N ND2 . ASN B 180 ? 0.8305 0.9831 0.8528 0.0622  0.0355  0.0569  182 ASN B ND2 
4385 N N   . TYR B 181 ? 0.5045 0.6081 0.5294 0.0292  0.0255  0.0368  183 TYR B N   
4386 C CA  . TYR B 181 ? 0.4484 0.5325 0.4699 0.0267  0.0255  0.0326  183 TYR B CA  
4387 C C   . TYR B 181 ? 0.4417 0.5133 0.4568 0.0341  0.0291  0.0336  183 TYR B C   
4388 O O   . TYR B 181 ? 0.4585 0.5333 0.4709 0.0415  0.0324  0.0372  183 TYR B O   
4389 C CB  . TYR B 181 ? 0.4210 0.5014 0.4436 0.0221  0.0248  0.0306  183 TYR B CB  
4390 C CG  . TYR B 181 ? 0.4154 0.5021 0.4414 0.0136  0.0214  0.0287  183 TYR B CG  
4391 C CD1 . TYR B 181 ? 0.4060 0.4839 0.4307 0.0086  0.0192  0.0252  183 TYR B CD1 
4392 C CD2 . TYR B 181 ? 0.4363 0.5375 0.4657 0.0105  0.0206  0.0306  183 TYR B CD2 
4393 C CE1 . TYR B 181 ? 0.4168 0.4974 0.4421 0.0010  0.0167  0.0234  183 TYR B CE1 
4394 C CE2 . TYR B 181 ? 0.4387 0.5433 0.4690 0.0017  0.0178  0.0287  183 TYR B CE2 
4395 C CZ  . TYR B 181 ? 0.4268 0.5198 0.4544 -0.0028 0.0160  0.0249  183 TYR B CZ  
4396 O OH  . TYR B 181 ? 0.4516 0.5450 0.4776 -0.0111 0.0137  0.0230  183 TYR B OH  
4397 N N   . THR B 182 ? 0.4005 0.4586 0.4125 0.0319  0.0287  0.0306  184 THR B N   
4398 C CA  . THR B 182 ? 0.3737 0.4184 0.3783 0.0369  0.0318  0.0309  184 THR B CA  
4399 C C   . THR B 182 ? 0.3303 0.3611 0.3327 0.0314  0.0308  0.0268  184 THR B C   
4400 O O   . THR B 182 ? 0.3072 0.3405 0.3142 0.0253  0.0276  0.0242  184 THR B O   
4401 C CB  . THR B 182 ? 0.3930 0.4432 0.3970 0.0409  0.0323  0.0333  184 THR B CB  
4402 O OG1 . THR B 182 ? 0.4213 0.4568 0.4167 0.0451  0.0356  0.0336  184 THR B OG1 
4403 C CG2 . THR B 182 ? 0.3790 0.4342 0.3877 0.0351  0.0284  0.0311  184 THR B CG2 
4404 N N   . ALA B 183 ? 0.3162 0.3332 0.3109 0.0336  0.0336  0.0265  185 ALA B N   
4405 C CA  . ALA B 183 ? 0.3054 0.3109 0.2972 0.0284  0.0328  0.0231  185 ALA B CA  
4406 C C   . ALA B 183 ? 0.3078 0.3162 0.3027 0.0252  0.0303  0.0218  185 ALA B C   
4407 O O   . ALA B 183 ? 0.3025 0.3077 0.2986 0.0200  0.0283  0.0191  185 ALA B O   
4408 C CB  . ALA B 183 ? 0.3123 0.3026 0.2936 0.0306  0.0367  0.0233  185 ALA B CB  
4409 N N   . ALA B 184 ? 0.3234 0.3376 0.3191 0.0287  0.0304  0.0239  186 ALA B N   
4410 C CA  . ALA B 184 ? 0.3166 0.3320 0.3138 0.0265  0.0286  0.0230  186 ALA B CA  
4411 C C   . ALA B 184 ? 0.3283 0.3541 0.3278 0.0303  0.0282  0.0256  186 ALA B C   
4412 O O   . ALA B 184 ? 0.3460 0.3755 0.3434 0.0364  0.0307  0.0288  186 ALA B O   
4413 C CB  . ALA B 184 ? 0.3236 0.3261 0.3137 0.0258  0.0306  0.0221  186 ALA B CB  
4414 N N   . THR B 185 ? 0.3297 0.3607 0.3329 0.0272  0.0253  0.0244  187 THR B N   
4415 C CA  . THR B 185 ? 0.3284 0.3700 0.3337 0.0298  0.0245  0.0265  187 THR B CA  
4416 C C   . THR B 185 ? 0.3061 0.3461 0.3119 0.0268  0.0224  0.0247  187 THR B C   
4417 O O   . THR B 185 ? 0.2912 0.3224 0.2954 0.0237  0.0222  0.0224  187 THR B O   
4418 C CB  . THR B 185 ? 0.3432 0.3983 0.3539 0.0281  0.0224  0.0272  187 THR B CB  
4419 O OG1 . THR B 185 ? 0.3660 0.4340 0.3785 0.0312  0.0221  0.0301  187 THR B OG1 
4420 C CG2 . THR B 185 ? 0.3440 0.3999 0.3579 0.0208  0.0189  0.0239  187 THR B CG2 
4421 N N   . ASP B 186 ? 0.3117 0.3608 0.3194 0.0279  0.0211  0.0260  188 ASP B N   
4422 C CA  . ASP B 186 ? 0.2888 0.3368 0.2967 0.0253  0.0191  0.0243  188 ASP B CA  
4423 C C   . ASP B 186 ? 0.2860 0.3444 0.2976 0.0214  0.0158  0.0235  188 ASP B C   
4424 O O   . ASP B 186 ? 0.3081 0.3777 0.3219 0.0220  0.0153  0.0253  188 ASP B O   
4425 C CB  . ASP B 186 ? 0.2927 0.3377 0.2969 0.0298  0.0211  0.0262  188 ASP B CB  
4426 C CG  . ASP B 186 ? 0.3073 0.3612 0.3110 0.0360  0.0227  0.0300  188 ASP B CG  
4427 O OD1 . ASP B 186 ? 0.3147 0.3825 0.3226 0.0353  0.0206  0.0310  188 ASP B OD1 
4428 O OD2 . ASP B 186 ? 0.3103 0.3575 0.3085 0.0415  0.0261  0.0322  188 ASP B OD2 
4429 N N   . TYR B 187 ? 0.2877 0.3422 0.2989 0.0171  0.0137  0.0208  189 TYR B N   
4430 C CA  . TYR B 187 ? 0.3147 0.3755 0.3266 0.0127  0.0108  0.0195  189 TYR B CA  
4431 C C   . TYR B 187 ? 0.3214 0.3783 0.3309 0.0122  0.0098  0.0183  189 TYR B C   
4432 O O   . TYR B 187 ? 0.3268 0.3772 0.3351 0.0150  0.0114  0.0185  189 TYR B O   
4433 C CB  . TYR B 187 ? 0.3278 0.3858 0.3395 0.0076  0.0096  0.0173  189 TYR B CB  
4434 C CG  . TYR B 187 ? 0.3518 0.4171 0.3659 0.0064  0.0097  0.0185  189 TYR B CG  
4435 C CD1 . TYR B 187 ? 0.3456 0.4078 0.3609 0.0089  0.0117  0.0192  189 TYR B CD1 
4436 C CD2 . TYR B 187 ? 0.3685 0.4434 0.3830 0.0018  0.0076  0.0185  189 TYR B CD2 
4437 C CE1 . TYR B 187 ? 0.3531 0.4223 0.3706 0.0081  0.0119  0.0205  189 TYR B CE1 
4438 C CE2 . TYR B 187 ? 0.3720 0.4549 0.3889 0.0000  0.0077  0.0198  189 TYR B CE2 
4439 C CZ  . TYR B 187 ? 0.3644 0.4447 0.3831 0.0036  0.0099  0.0208  189 TYR B CZ  
4440 O OH  . TYR B 187 ? 0.3702 0.4590 0.3912 0.0023  0.0100  0.0223  189 TYR B OH  
4441 N N   . ARG B 188 ? 0.3312 0.3919 0.3393 0.0085  0.0075  0.0171  190 ARG B N   
4442 C CA  . ARG B 188 ? 0.3316 0.3877 0.3363 0.0076  0.0065  0.0156  190 ARG B CA  
4443 C C   . ARG B 188 ? 0.3172 0.3637 0.3184 0.0043  0.0059  0.0128  190 ARG B C   
4444 O O   . ARG B 188 ? 0.3002 0.3457 0.3012 0.0012  0.0057  0.0119  190 ARG B O   
4445 C CB  . ARG B 188 ? 0.3595 0.4244 0.3630 0.0056  0.0045  0.0160  190 ARG B CB  
4446 C CG  . ARG B 188 ? 0.3693 0.4449 0.3758 0.0102  0.0052  0.0193  190 ARG B CG  
4447 C CD  . ARG B 188 ? 0.3849 0.4688 0.3897 0.0087  0.0032  0.0197  190 ARG B CD  
4448 N NE  . ARG B 188 ? 0.4117 0.5014 0.4147 0.0015  0.0007  0.0182  190 ARG B NE  
4449 C CZ  . ARG B 188 ? 0.4270 0.5100 0.4242 -0.0041 -0.0010 0.0152  190 ARG B CZ  
4450 N NH1 . ARG B 188 ? 0.4230 0.4944 0.4163 -0.0025 -0.0005 0.0135  190 ARG B NH1 
4451 N NH2 . ARG B 188 ? 0.4453 0.5328 0.4394 -0.0115 -0.0030 0.0140  190 ARG B NH2 
4452 N N   . ILE B 189 ? 0.3032 0.3433 0.3013 0.0054  0.0061  0.0119  191 ILE B N   
4453 C CA  . ILE B 189 ? 0.3096 0.3406 0.3028 0.0039  0.0061  0.0097  191 ILE B CA  
4454 C C   . ILE B 189 ? 0.3243 0.3538 0.3120 -0.0010 0.0045  0.0080  191 ILE B C   
4455 O O   . ILE B 189 ? 0.3260 0.3611 0.3128 -0.0030 0.0031  0.0083  191 ILE B O   
4456 C CB  . ILE B 189 ? 0.3118 0.3387 0.3028 0.0072  0.0068  0.0098  191 ILE B CB  
4457 C CG1 . ILE B 189 ? 0.3075 0.3349 0.3028 0.0102  0.0085  0.0112  191 ILE B CG1 
4458 C CG2 . ILE B 189 ? 0.3179 0.3362 0.3019 0.0067  0.0069  0.0081  191 ILE B CG2 
4459 C CD1 . ILE B 189 ? 0.3060 0.3319 0.3001 0.0128  0.0093  0.0117  191 ILE B CD1 
4460 N N   . GLY B 190 ? 0.3471 0.3694 0.3310 -0.0034 0.0049  0.0066  192 GLY B N   
4461 C CA  . GLY B 190 ? 0.3819 0.3990 0.3579 -0.0091 0.0039  0.0046  192 GLY B CA  
4462 C C   . GLY B 190 ? 0.4137 0.4386 0.3926 -0.0141 0.0029  0.0050  192 GLY B C   
4463 O O   . GLY B 190 ? 0.4432 0.4627 0.4150 -0.0200 0.0024  0.0033  192 GLY B O   
4464 N N   . GLN B 191 ? 0.4279 0.4645 0.4155 -0.0121 0.0028  0.0072  193 GLN B N   
4465 C CA  . GLN B 191 ? 0.4447 0.4910 0.4360 -0.0157 0.0022  0.0083  193 GLN B CA  
4466 C C   . GLN B 191 ? 0.4258 0.4661 0.4177 -0.0158 0.0035  0.0077  193 GLN B C   
4467 O O   . GLN B 191 ? 0.4031 0.4386 0.3977 -0.0107 0.0051  0.0081  193 GLN B O   
4468 C CB  . GLN B 191 ? 0.4861 0.5459 0.4853 -0.0115 0.0024  0.0113  193 GLN B CB  
4469 C CG  . GLN B 191 ? 0.5415 0.6114 0.5404 -0.0124 0.0008  0.0124  193 GLN B CG  
4470 C CD  . GLN B 191 ? 0.5955 0.6789 0.6011 -0.0070 0.0015  0.0160  193 GLN B CD  
4471 O OE1 . GLN B 191 ? 0.5903 0.6728 0.5997 -0.0015 0.0036  0.0176  193 GLN B OE1 
4472 N NE2 . GLN B 191 ? 0.6834 0.7790 0.6892 -0.0083 0.0000  0.0174  193 GLN B NE2 
4473 N N   . ASN B 192 ? 0.4189 0.4593 0.4076 -0.0220 0.0029  0.0069  194 ASN B N   
4474 C CA  . ASN B 192 ? 0.4127 0.4488 0.4018 -0.0230 0.0041  0.0066  194 ASN B CA  
4475 C C   . ASN B 192 ? 0.3690 0.4167 0.3672 -0.0198 0.0047  0.0092  194 ASN B C   
4476 O O   . ASN B 192 ? 0.3538 0.4147 0.3559 -0.0201 0.0038  0.0112  194 ASN B O   
4477 C CB  . ASN B 192 ? 0.4381 0.4691 0.4195 -0.0310 0.0036  0.0048  194 ASN B CB  
4478 C CG  . ASN B 192 ? 0.4749 0.4896 0.4446 -0.0328 0.0040  0.0022  194 ASN B CG  
4479 O OD1 . ASN B 192 ? 0.4859 0.4909 0.4537 -0.0273 0.0055  0.0018  194 ASN B OD1 
4480 N ND2 . ASN B 192 ? 0.5123 0.5237 0.4731 -0.0404 0.0030  0.0007  194 ASN B ND2 
4481 N N   . ILE B 193 ? 0.3446 0.3872 0.3452 -0.0159 0.0063  0.0093  195 ILE B N   
4482 C CA  . ILE B 193 ? 0.3345 0.3846 0.3420 -0.0116 0.0075  0.0117  195 ILE B CA  
4483 C C   . ILE B 193 ? 0.3429 0.3907 0.3505 -0.0136 0.0083  0.0114  195 ILE B C   
4484 O O   . ILE B 193 ? 0.3341 0.3712 0.3374 -0.0151 0.0087  0.0094  195 ILE B O   
4485 C CB  . ILE B 193 ? 0.3224 0.3679 0.3317 -0.0053 0.0089  0.0122  195 ILE B CB  
4486 C CG1 . ILE B 193 ? 0.3172 0.3640 0.3258 -0.0037 0.0082  0.0124  195 ILE B CG1 
4487 C CG2 . ILE B 193 ? 0.3102 0.3603 0.3238 -0.0011 0.0107  0.0144  195 ILE B CG2 
4488 C CD1 . ILE B 193 ? 0.3063 0.3454 0.3141 0.0000  0.0093  0.0119  195 ILE B CD1 
4489 N N   . LEU B 194 ? 0.3479 0.4057 0.3599 -0.0130 0.0088  0.0136  196 LEU B N   
4490 C CA  . LEU B 194 ? 0.3576 0.4144 0.3699 -0.0151 0.0096  0.0135  196 LEU B CA  
4491 C C   . LEU B 194 ? 0.3288 0.3818 0.3438 -0.0091 0.0116  0.0143  196 LEU B C   
4492 O O   . LEU B 194 ? 0.3163 0.3747 0.3343 -0.0042 0.0127  0.0165  196 LEU B O   
4493 C CB  . LEU B 194 ? 0.3975 0.4685 0.4122 -0.0189 0.0089  0.0155  196 LEU B CB  
4494 C CG  . LEU B 194 ? 0.4396 0.5086 0.4527 -0.0237 0.0093  0.0149  196 LEU B CG  
4495 C CD1 . LEU B 194 ? 0.4538 0.5189 0.4600 -0.0326 0.0077  0.0128  196 LEU B CD1 
4496 C CD2 . LEU B 194 ? 0.4537 0.5375 0.4722 -0.0225 0.0100  0.0182  196 LEU B CD2 
4497 N N   . PHE B 195 ? 0.3087 0.3521 0.3215 -0.0098 0.0123  0.0126  197 PHE B N   
4498 C CA  . PHE B 195 ? 0.2893 0.3284 0.3035 -0.0055 0.0141  0.0130  197 PHE B CA  
4499 C C   . PHE B 195 ? 0.2852 0.3253 0.2999 -0.0072 0.0148  0.0133  197 PHE B C   
4500 O O   . PHE B 195 ? 0.2736 0.3137 0.2862 -0.0122 0.0140  0.0126  197 PHE B O   
4501 C CB  . PHE B 195 ? 0.2696 0.2985 0.2809 -0.0043 0.0142  0.0110  197 PHE B CB  
4502 C CG  . PHE B 195 ? 0.2523 0.2808 0.2637 -0.0020 0.0140  0.0111  197 PHE B CG  
4503 C CD1 . PHE B 195 ? 0.2397 0.2674 0.2522 0.0016  0.0153  0.0121  197 PHE B CD1 
4504 C CD2 . PHE B 195 ? 0.2480 0.2753 0.2569 -0.0038 0.0126  0.0101  197 PHE B CD2 
4505 C CE1 . PHE B 195 ? 0.2357 0.2625 0.2476 0.0033  0.0152  0.0122  197 PHE B CE1 
4506 C CE2 . PHE B 195 ? 0.2417 0.2687 0.2506 -0.0015 0.0124  0.0103  197 PHE B CE2 
4507 C CZ  . PHE B 195 ? 0.2337 0.2609 0.2444 0.0018  0.0137  0.0114  197 PHE B CZ  
4508 N N   . GLN B 196 ? 0.2911 0.3314 0.3077 -0.0032 0.0166  0.0145  198 GLN B N   
4509 C CA  . GLN B 196 ? 0.3137 0.3559 0.3312 -0.0035 0.0176  0.0154  198 GLN B CA  
4510 C C   . GLN B 196 ? 0.2848 0.3190 0.3012 -0.0001 0.0193  0.0148  198 GLN B C   
4511 O O   . GLN B 196 ? 0.2778 0.3100 0.2936 0.0037  0.0204  0.0154  198 GLN B O   
4512 C CB  . GLN B 196 ? 0.3457 0.4008 0.3666 -0.0020 0.0183  0.0185  198 GLN B CB  
4513 C CG  . GLN B 196 ? 0.3879 0.4473 0.4100 -0.0030 0.0192  0.0197  198 GLN B CG  
4514 C CD  . GLN B 196 ? 0.4216 0.4965 0.4472 -0.0011 0.0200  0.0234  198 GLN B CD  
4515 O OE1 . GLN B 196 ? 0.4525 0.5373 0.4797 -0.0061 0.0190  0.0244  198 GLN B OE1 
4516 N NE2 . GLN B 196 ? 0.4267 0.5038 0.4527 0.0060  0.0220  0.0257  198 GLN B NE2 
4517 N N   . ILE B 197 ? 0.2626 0.2916 0.2774 -0.0019 0.0195  0.0135  199 ILE B N   
4518 C CA  . ILE B 197 ? 0.2556 0.2786 0.2691 0.0006  0.0209  0.0130  199 ILE B CA  
4519 C C   . ILE B 197 ? 0.2624 0.2883 0.2768 0.0005  0.0221  0.0142  199 ILE B C   
4520 O O   . ILE B 197 ? 0.2551 0.2826 0.2695 -0.0029 0.0214  0.0140  199 ILE B O   
4521 C CB  . ILE B 197 ? 0.2463 0.2618 0.2570 -0.0004 0.0203  0.0109  199 ILE B CB  
4522 C CG1 . ILE B 197 ? 0.2381 0.2519 0.2481 0.0000  0.0194  0.0101  199 ILE B CG1 
4523 C CG2 . ILE B 197 ? 0.2521 0.2633 0.2614 0.0010  0.0215  0.0105  199 ILE B CG2 
4524 C CD1 . ILE B 197 ? 0.2325 0.2419 0.2398 -0.0009 0.0186  0.0086  199 ILE B CD1 
4525 N N   . THR B 198 ? 0.2735 0.2992 0.2876 0.0043  0.0240  0.0155  200 THR B N   
4526 C CA  . THR B 198 ? 0.2856 0.3147 0.3004 0.0055  0.0255  0.0170  200 THR B CA  
4527 C C   . THR B 198 ? 0.2824 0.3030 0.2940 0.0070  0.0268  0.0159  200 THR B C   
4528 O O   . THR B 198 ? 0.2775 0.2922 0.2858 0.0096  0.0280  0.0156  200 THR B O   
4529 C CB  . THR B 198 ? 0.3019 0.3385 0.3178 0.0099  0.0272  0.0202  200 THR B CB  
4530 O OG1 . THR B 198 ? 0.2927 0.3389 0.3118 0.0080  0.0257  0.0213  200 THR B OG1 
4531 C CG2 . THR B 198 ? 0.3054 0.3468 0.3220 0.0117  0.0290  0.0222  200 THR B CG2 
4532 N N   . ALA B 199 ? 0.2821 0.3016 0.2936 0.0049  0.0266  0.0152  201 ALA B N   
4533 C CA  . ALA B 199 ? 0.2812 0.2941 0.2898 0.0060  0.0278  0.0143  201 ALA B CA  
4534 C C   . ALA B 199 ? 0.2900 0.3067 0.2991 0.0082  0.0297  0.0164  201 ALA B C   
4535 O O   . ALA B 199 ? 0.2987 0.3227 0.3108 0.0062  0.0294  0.0177  201 ALA B O   
4536 C CB  . ALA B 199 ? 0.2745 0.2836 0.2820 0.0031  0.0266  0.0124  201 ALA B CB  
4537 N N   . THR B 200 ? 0.2929 0.3048 0.2985 0.0118  0.0318  0.0167  202 THR B N   
4538 C CA  . THR B 200 ? 0.3004 0.3138 0.3050 0.0145  0.0339  0.0185  202 THR B CA  
4539 C C   . THR B 200 ? 0.3059 0.3127 0.3080 0.0129  0.0338  0.0165  202 THR B C   
4540 O O   . THR B 200 ? 0.3072 0.3079 0.3070 0.0110  0.0326  0.0141  202 THR B O   
4541 C CB  . THR B 200 ? 0.3105 0.3209 0.3107 0.0202  0.0368  0.0203  202 THR B CB  
4542 O OG1 . THR B 200 ? 0.3177 0.3161 0.3115 0.0198  0.0373  0.0179  202 THR B OG1 
4543 C CG2 . THR B 200 ? 0.3233 0.3397 0.3249 0.0230  0.0373  0.0225  202 THR B CG2 
4544 N N   . LEU B 201 ? 0.3179 0.3267 0.3202 0.0137  0.0350  0.0176  203 LEU B N   
4545 C CA  . LEU B 201 ? 0.3203 0.3237 0.3202 0.0125  0.0351  0.0160  203 LEU B CA  
4546 C C   . LEU B 201 ? 0.3208 0.3183 0.3152 0.0162  0.0375  0.0163  203 LEU B C   
4547 O O   . LEU B 201 ? 0.3349 0.3335 0.3278 0.0203  0.0397  0.0184  203 LEU B O   
4548 C CB  . LEU B 201 ? 0.3321 0.3407 0.3351 0.0103  0.0348  0.0170  203 LEU B CB  
4549 C CG  . LEU B 201 ? 0.3525 0.3633 0.3579 0.0060  0.0327  0.0162  203 LEU B CG  
4550 C CD1 . LEU B 201 ? 0.3660 0.3798 0.3723 0.0030  0.0330  0.0171  203 LEU B CD1 
4551 C CD2 . LEU B 201 ? 0.3637 0.3677 0.3666 0.0048  0.0312  0.0137  203 LEU B CD2 
4552 N N   . PRO B 202 ? 0.3126 0.3033 0.3028 0.0152  0.0375  0.0144  204 PRO B N   
4553 C CA  . PRO B 202 ? 0.3244 0.3077 0.3076 0.0180  0.0399  0.0143  204 PRO B CA  
4554 C C   . PRO B 202 ? 0.3284 0.3149 0.3121 0.0212  0.0420  0.0166  204 PRO B C   
4555 O O   . PRO B 202 ? 0.3153 0.3087 0.3042 0.0198  0.0412  0.0175  204 PRO B O   
4556 C CB  . PRO B 202 ? 0.3252 0.3036 0.3052 0.0145  0.0384  0.0115  204 PRO B CB  
4557 C CG  . PRO B 202 ? 0.3101 0.2949 0.2961 0.0122  0.0363  0.0113  204 PRO B CG  
4558 C CD  . PRO B 202 ? 0.3068 0.2971 0.2980 0.0117  0.0353  0.0124  204 PRO B CD  
4559 N N   . SER B 203 ? 0.3363 0.3172 0.3135 0.0257  0.0451  0.0177  205 SER B N   
4560 C CA  . SER B 203 ? 0.3344 0.3190 0.3116 0.0300  0.0476  0.0204  205 SER B CA  
4561 C C   . SER B 203 ? 0.3355 0.3194 0.3130 0.0277  0.0470  0.0192  205 SER B C   
4562 O O   . SER B 203 ? 0.3525 0.3427 0.3328 0.0294  0.0481  0.0215  205 SER B O   
4563 C CB  . SER B 203 ? 0.3482 0.3245 0.3162 0.0358  0.0513  0.0217  205 SER B CB  
4564 O OG  . SER B 203 ? 0.3501 0.3126 0.3088 0.0339  0.0517  0.0186  205 SER B OG  
4565 N N   . ASN B 204 ? 0.3304 0.3085 0.3054 0.0238  0.0451  0.0161  206 ASN B N   
4566 C CA  . ASN B 204 ? 0.3342 0.3122 0.3092 0.0222  0.0445  0.0152  206 ASN B CA  
4567 C C   . ASN B 204 ? 0.3209 0.3049 0.3024 0.0185  0.0419  0.0147  206 ASN B C   
4568 O O   . ASN B 204 ? 0.3014 0.2841 0.2818 0.0169  0.0410  0.0134  206 ASN B O   
4569 C CB  . ASN B 204 ? 0.3382 0.3071 0.3051 0.0208  0.0445  0.0125  206 ASN B CB  
4570 C CG  . ASN B 204 ? 0.3383 0.3038 0.3028 0.0171  0.0426  0.0101  206 ASN B CG  
4571 O OD1 . ASN B 204 ? 0.3553 0.3244 0.3243 0.0162  0.0413  0.0104  206 ASN B OD1 
4572 N ND2 . ASN B 204 ? 0.3306 0.2901 0.2880 0.0145  0.0422  0.0078  206 ASN B ND2 
4573 N N   . TYR B 205 ? 0.3204 0.3104 0.3074 0.0174  0.0409  0.0158  207 TYR B N   
4574 C CA  . TYR B 205 ? 0.3276 0.3207 0.3185 0.0138  0.0388  0.0151  207 TYR B CA  
4575 C C   . TYR B 205 ? 0.3256 0.3187 0.3161 0.0133  0.0394  0.0156  207 TYR B C   
4576 O O   . TYR B 205 ? 0.3094 0.3003 0.2988 0.0118  0.0383  0.0144  207 TYR B O   
4577 C CB  . TYR B 205 ? 0.3306 0.3301 0.3264 0.0123  0.0382  0.0165  207 TYR B CB  
4578 C CG  . TYR B 205 ? 0.3445 0.3449 0.3421 0.0085  0.0365  0.0159  207 TYR B CG  
4579 C CD1 . TYR B 205 ? 0.3478 0.3447 0.3443 0.0072  0.0348  0.0140  207 TYR B CD1 
4580 C CD2 . TYR B 205 ? 0.3530 0.3573 0.3524 0.0061  0.0370  0.0174  207 TYR B CD2 
4581 C CE1 . TYR B 205 ? 0.3597 0.3553 0.3558 0.0046  0.0339  0.0136  207 TYR B CE1 
4582 C CE2 . TYR B 205 ? 0.3685 0.3706 0.3669 0.0023  0.0361  0.0168  207 TYR B CE2 
4583 C CZ  . TYR B 205 ? 0.3827 0.3796 0.3789 0.0020  0.0346  0.0148  207 TYR B CZ  
4584 O OH  . TYR B 205 ? 0.4086 0.4016 0.4020 -0.0008 0.0343  0.0143  207 TYR B OH  
4585 N N   . ALA B 206 ? 0.3574 0.3529 0.3481 0.0152  0.0414  0.0175  208 ALA B N   
4586 C CA  . ALA B 206 ? 0.3690 0.3650 0.3593 0.0146  0.0424  0.0184  208 ALA B CA  
4587 C C   . ALA B 206 ? 0.3799 0.3699 0.3656 0.0158  0.0424  0.0167  208 ALA B C   
4588 O O   . ALA B 206 ? 0.3977 0.3867 0.3823 0.0151  0.0428  0.0170  208 ALA B O   
4589 C CB  . ALA B 206 ? 0.3693 0.3708 0.3611 0.0165  0.0447  0.0212  208 ALA B CB  
4590 N N   . ASP B 207 ? 0.3938 0.3799 0.3759 0.0172  0.0422  0.0152  209 ASP B N   
4591 C CA  . ASP B 207 ? 0.4004 0.3823 0.3775 0.0177  0.0420  0.0136  209 ASP B CA  
4592 C C   . ASP B 207 ? 0.3736 0.3560 0.3507 0.0158  0.0398  0.0121  209 ASP B C   
4593 O O   . ASP B 207 ? 0.3765 0.3581 0.3502 0.0161  0.0395  0.0113  209 ASP B O   
4594 C CB  . ASP B 207 ? 0.4392 0.4160 0.4107 0.0186  0.0426  0.0122  209 ASP B CB  
4595 C CG  . ASP B 207 ? 0.4732 0.4476 0.4421 0.0221  0.0455  0.0139  209 ASP B CG  
4596 O OD1 . ASP B 207 ? 0.4946 0.4731 0.4664 0.0239  0.0469  0.0161  209 ASP B OD1 
4597 O OD2 . ASP B 207 ? 0.5035 0.4715 0.4663 0.0231  0.0465  0.0130  209 ASP B OD2 
4598 N N   . PHE B 208 ? 0.3450 0.3293 0.3253 0.0141  0.0385  0.0120  210 PHE B N   
4599 C CA  . PHE B 208 ? 0.3220 0.3071 0.3018 0.0134  0.0369  0.0112  210 PHE B CA  
4600 C C   . PHE B 208 ? 0.3334 0.3173 0.3129 0.0139  0.0378  0.0125  210 PHE B C   
4601 O O   . PHE B 208 ? 0.3417 0.3256 0.3233 0.0127  0.0388  0.0137  210 PHE B O   
4602 C CB  . PHE B 208 ? 0.2976 0.2841 0.2799 0.0118  0.0353  0.0106  210 PHE B CB  
4603 C CG  . PHE B 208 ? 0.2800 0.2664 0.2611 0.0108  0.0344  0.0092  210 PHE B CG  
4604 C CD1 . PHE B 208 ? 0.2783 0.2624 0.2591 0.0111  0.0355  0.0094  210 PHE B CD1 
4605 C CD2 . PHE B 208 ? 0.2728 0.2612 0.2522 0.0097  0.0328  0.0080  210 PHE B CD2 
4606 C CE1 . PHE B 208 ? 0.2742 0.2556 0.2518 0.0100  0.0352  0.0081  210 PHE B CE1 
4607 C CE2 . PHE B 208 ? 0.2730 0.2604 0.2501 0.0076  0.0322  0.0066  210 PHE B CE2 
4608 C CZ  . PHE B 208 ? 0.2721 0.2547 0.2477 0.0076  0.0335  0.0065  210 PHE B CZ  
4609 N N   . THR B 209 ? 0.3561 0.3393 0.3323 0.0155  0.0377  0.0124  211 THR B N   
4610 C CA  . THR B 209 ? 0.3862 0.3656 0.3598 0.0162  0.0391  0.0137  211 THR B CA  
4611 C C   . THR B 209 ? 0.3921 0.3697 0.3649 0.0157  0.0383  0.0135  211 THR B C   
4612 O O   . THR B 209 ? 0.4132 0.3856 0.3835 0.0144  0.0395  0.0143  211 THR B O   
4613 C CB  . THR B 209 ? 0.3992 0.3775 0.3682 0.0195  0.0402  0.0143  211 THR B CB  
4614 O OG1 . THR B 209 ? 0.3926 0.3760 0.3610 0.0209  0.0385  0.0133  211 THR B OG1 
4615 C CG2 . THR B 209 ? 0.4112 0.3888 0.3800 0.0198  0.0417  0.0150  211 THR B CG2 
4616 N N   . ARG B 210 ? 0.3952 0.3765 0.3688 0.0163  0.0365  0.0126  212 ARG B N   
4617 C CA  . ARG B 210 ? 0.4074 0.3876 0.3805 0.0161  0.0358  0.0124  212 ARG B CA  
4618 C C   . ARG B 210 ? 0.3653 0.3499 0.3432 0.0138  0.0338  0.0112  212 ARG B C   
4619 O O   . ARG B 210 ? 0.3660 0.3546 0.3451 0.0136  0.0330  0.0104  212 ARG B O   
4620 C CB  . ARG B 210 ? 0.4704 0.4508 0.4384 0.0205  0.0362  0.0132  212 ARG B CB  
4621 C CG  . ARG B 210 ? 0.5377 0.5211 0.5056 0.0217  0.0349  0.0130  212 ARG B CG  
4622 C CD  . ARG B 210 ? 0.5743 0.5679 0.5447 0.0220  0.0330  0.0125  212 ARG B CD  
4623 N NE  . ARG B 210 ? 0.6071 0.6055 0.5755 0.0251  0.0325  0.0133  212 ARG B NE  
4624 C CZ  . ARG B 210 ? 0.6403 0.6427 0.6043 0.0303  0.0334  0.0151  212 ARG B CZ  
4625 N NH1 . ARG B 210 ? 0.6819 0.6832 0.6426 0.0329  0.0348  0.0160  212 ARG B NH1 
4626 N NH2 . ARG B 210 ? 0.6589 0.6669 0.6215 0.0335  0.0330  0.0162  212 ARG B NH2 
4627 N N   . TYR B 211 ? 0.3392 0.3226 0.3187 0.0120  0.0332  0.0110  213 TYR B N   
4628 C CA  . TYR B 211 ? 0.2965 0.2835 0.2803 0.0100  0.0317  0.0101  213 TYR B CA  
4629 C C   . TYR B 211 ? 0.2939 0.2810 0.2771 0.0102  0.0306  0.0099  213 TYR B C   
4630 O O   . TYR B 211 ? 0.2804 0.2641 0.2632 0.0087  0.0308  0.0101  213 TYR B O   
4631 C CB  . TYR B 211 ? 0.2733 0.2606 0.2607 0.0077  0.0321  0.0105  213 TYR B CB  
4632 C CG  . TYR B 211 ? 0.2497 0.2397 0.2397 0.0072  0.0312  0.0098  213 TYR B CG  
4633 C CD1 . TYR B 211 ? 0.2402 0.2302 0.2291 0.0079  0.0317  0.0094  213 TYR B CD1 
4634 C CD2 . TYR B 211 ? 0.2353 0.2267 0.2276 0.0059  0.0302  0.0096  213 TYR B CD2 
4635 C CE1 . TYR B 211 ? 0.2365 0.2262 0.2253 0.0074  0.0315  0.0088  213 TYR B CE1 
4636 C CE2 . TYR B 211 ? 0.2266 0.2190 0.2200 0.0058  0.0298  0.0092  213 TYR B CE2 
4637 C CZ  . TYR B 211 ? 0.2281 0.2190 0.2192 0.0065  0.0306  0.0087  213 TYR B CZ  
4638 O OH  . TYR B 211 ? 0.2231 0.2123 0.2129 0.0063  0.0308  0.0082  213 TYR B OH  
4639 N N   . GLU B 212 ? 0.3065 0.2979 0.2892 0.0117  0.0296  0.0095  214 GLU B N   
4640 C CA  . GLU B 212 ? 0.3136 0.3068 0.2961 0.0123  0.0285  0.0095  214 GLU B CA  
4641 C C   . GLU B 212 ? 0.2872 0.2810 0.2738 0.0092  0.0275  0.0086  214 GLU B C   
4642 O O   . GLU B 212 ? 0.2695 0.2652 0.2583 0.0075  0.0271  0.0080  214 GLU B O   
4643 C CB  . GLU B 212 ? 0.3493 0.3497 0.3307 0.0142  0.0277  0.0097  214 GLU B CB  
4644 C CG  . GLU B 212 ? 0.3971 0.3983 0.3738 0.0186  0.0289  0.0111  214 GLU B CG  
4645 C CD  . GLU B 212 ? 0.4478 0.4596 0.4237 0.0207  0.0280  0.0119  214 GLU B CD  
4646 O OE1 . GLU B 212 ? 0.4878 0.5058 0.4647 0.0187  0.0270  0.0113  214 GLU B OE1 
4647 O OE2 . GLU B 212 ? 0.5497 0.5641 0.5235 0.0242  0.0282  0.0131  214 GLU B OE2 
4648 N N   . PHE B 213 ? 0.2772 0.2684 0.2636 0.0088  0.0273  0.0087  215 PHE B N   
4649 C CA  . PHE B 213 ? 0.2575 0.2493 0.2474 0.0063  0.0264  0.0083  215 PHE B CA  
4650 C C   . PHE B 213 ? 0.2512 0.2427 0.2397 0.0070  0.0257  0.0082  215 PHE B C   
4651 O O   . PHE B 213 ? 0.2514 0.2377 0.2359 0.0076  0.0265  0.0085  215 PHE B O   
4652 C CB  . PHE B 213 ? 0.2569 0.2460 0.2475 0.0041  0.0272  0.0088  215 PHE B CB  
4653 C CG  . PHE B 213 ? 0.2518 0.2437 0.2464 0.0020  0.0265  0.0088  215 PHE B CG  
4654 C CD1 . PHE B 213 ? 0.2435 0.2386 0.2413 0.0021  0.0268  0.0092  215 PHE B CD1 
4655 C CD2 . PHE B 213 ? 0.2526 0.2438 0.2469 0.0003  0.0258  0.0087  215 PHE B CD2 
4656 C CE1 . PHE B 213 ? 0.2358 0.2343 0.2367 0.0012  0.0266  0.0098  215 PHE B CE1 
4657 C CE2 . PHE B 213 ? 0.2439 0.2391 0.2419 -0.0013 0.0251  0.0090  215 PHE B CE2 
4658 C CZ  . PHE B 213 ? 0.2418 0.2412 0.2433 -0.0005 0.0256  0.0098  215 PHE B CZ  
4659 N N   . THR B 214 ? 0.2414 0.2373 0.2322 0.0068  0.0245  0.0078  216 THR B N   
4660 C CA  . THR B 214 ? 0.2449 0.2414 0.2345 0.0078  0.0238  0.0079  216 THR B CA  
4661 C C   . THR B 214 ? 0.2407 0.2400 0.2342 0.0056  0.0226  0.0074  216 THR B C   
4662 O O   . THR B 214 ? 0.2304 0.2334 0.2255 0.0046  0.0222  0.0070  216 THR B O   
4663 C CB  . THR B 214 ? 0.2477 0.2485 0.2347 0.0111  0.0238  0.0087  216 THR B CB  
4664 O OG1 . THR B 214 ? 0.2574 0.2541 0.2401 0.0136  0.0254  0.0094  216 THR B OG1 
4665 C CG2 . THR B 214 ? 0.2540 0.2558 0.2393 0.0132  0.0235  0.0092  216 THR B CG2 
4666 N N   . ILE B 215 ? 0.2347 0.2318 0.2287 0.0046  0.0223  0.0073  217 ILE B N   
4667 C CA  . ILE B 215 ? 0.2336 0.2332 0.2307 0.0033  0.0213  0.0070  217 ILE B CA  
4668 C C   . ILE B 215 ? 0.2464 0.2469 0.2416 0.0048  0.0207  0.0071  217 ILE B C   
4669 O O   . ILE B 215 ? 0.2518 0.2481 0.2432 0.0060  0.0212  0.0073  217 ILE B O   
4670 C CB  . ILE B 215 ? 0.2289 0.2276 0.2279 0.0013  0.0213  0.0072  217 ILE B CB  
4671 C CG1 . ILE B 215 ? 0.2344 0.2338 0.2353 0.0008  0.0222  0.0076  217 ILE B CG1 
4672 C CG2 . ILE B 215 ? 0.2312 0.2324 0.2325 0.0009  0.0204  0.0072  217 ILE B CG2 
4673 C CD1 . ILE B 215 ? 0.2354 0.2368 0.2384 -0.0007 0.0223  0.0084  217 ILE B CD1 
4674 N N   . LYS B 216 ? 0.2567 0.2619 0.2533 0.0047  0.0201  0.0071  218 LYS B N   
4675 C CA  . LYS B 216 ? 0.2580 0.2658 0.2539 0.0060  0.0195  0.0075  218 LYS B CA  
4676 C C   . LYS B 216 ? 0.2368 0.2451 0.2354 0.0041  0.0188  0.0072  218 LYS B C   
4677 O O   . LYS B 216 ? 0.2354 0.2449 0.2357 0.0021  0.0188  0.0069  218 LYS B O   
4678 C CB  . LYS B 216 ? 0.2908 0.3056 0.2863 0.0069  0.0193  0.0081  218 LYS B CB  
4679 C CG  . LYS B 216 ? 0.3229 0.3385 0.3148 0.0107  0.0201  0.0091  218 LYS B CG  
4680 C CD  . LYS B 216 ? 0.3608 0.3865 0.3525 0.0117  0.0198  0.0102  218 LYS B CD  
4681 C CE  . LYS B 216 ? 0.4002 0.4275 0.3876 0.0171  0.0210  0.0118  218 LYS B CE  
4682 N NZ  . LYS B 216 ? 0.4227 0.4438 0.4056 0.0214  0.0221  0.0126  218 LYS B NZ  
4683 N N   . ASP B 217 ? 0.2177 0.2244 0.2156 0.0047  0.0184  0.0072  219 ASP B N   
4684 C CA  . ASP B 217 ? 0.2078 0.2153 0.2081 0.0034  0.0177  0.0071  219 ASP B CA  
4685 C C   . ASP B 217 ? 0.2013 0.2111 0.2003 0.0048  0.0173  0.0075  219 ASP B C   
4686 O O   . ASP B 217 ? 0.1981 0.2052 0.1938 0.0068  0.0174  0.0076  219 ASP B O   
4687 C CB  . ASP B 217 ? 0.2085 0.2131 0.2091 0.0022  0.0176  0.0069  219 ASP B CB  
4688 C CG  . ASP B 217 ? 0.2037 0.2103 0.2066 0.0014  0.0170  0.0072  219 ASP B CG  
4689 O OD1 . ASP B 217 ? 0.2037 0.2123 0.2080 0.0016  0.0171  0.0074  219 ASP B OD1 
4690 O OD2 . ASP B 217 ? 0.2041 0.2104 0.2070 0.0002  0.0166  0.0072  219 ASP B OD2 
4691 N N   . THR B 218 ? 0.1986 0.2123 0.1993 0.0038  0.0170  0.0077  220 THR B N   
4692 C CA  . THR B 218 ? 0.2000 0.2177 0.2001 0.0051  0.0166  0.0084  220 THR B CA  
4693 C C   . THR B 218 ? 0.2007 0.2165 0.2016 0.0047  0.0161  0.0082  220 THR B C   
4694 O O   . THR B 218 ? 0.2002 0.2158 0.2031 0.0028  0.0162  0.0081  220 THR B O   
4695 C CB  . THR B 218 ? 0.1958 0.2200 0.1966 0.0034  0.0165  0.0089  220 THR B CB  
4696 O OG1 . THR B 218 ? 0.1944 0.2207 0.1941 0.0041  0.0168  0.0090  220 THR B OG1 
4697 C CG2 . THR B 218 ? 0.1997 0.2299 0.2000 0.0047  0.0162  0.0100  220 THR B CG2 
4698 N N   . ILE B 219 ? 0.2010 0.2152 0.1996 0.0068  0.0159  0.0083  221 ILE B N   
4699 C CA  . ILE B 219 ? 0.2101 0.2231 0.2088 0.0067  0.0153  0.0082  221 ILE B CA  
4700 C C   . ILE B 219 ? 0.2011 0.2191 0.2004 0.0075  0.0153  0.0091  221 ILE B C   
4701 O O   . ILE B 219 ? 0.2080 0.2298 0.2058 0.0095  0.0156  0.0100  221 ILE B O   
4702 C CB  . ILE B 219 ? 0.2285 0.2359 0.2224 0.0080  0.0153  0.0078  221 ILE B CB  
4703 C CG1 . ILE B 219 ? 0.2359 0.2385 0.2280 0.0066  0.0157  0.0071  221 ILE B CG1 
4704 C CG2 . ILE B 219 ? 0.2302 0.2369 0.2241 0.0070  0.0145  0.0075  221 ILE B CG2 
4705 C CD1 . ILE B 219 ? 0.2397 0.2441 0.2363 0.0036  0.0153  0.0069  221 ILE B CD1 
4706 N N   . PRO B 220 ? 0.1890 0.2079 0.1903 0.0061  0.0150  0.0092  222 PRO B N   
4707 C CA  . PRO B 220 ? 0.1916 0.2150 0.1931 0.0065  0.0150  0.0101  222 PRO B CA  
4708 C C   . PRO B 220 ? 0.1988 0.2221 0.1977 0.0096  0.0148  0.0105  222 PRO B C   
4709 O O   . PRO B 220 ? 0.1956 0.2138 0.1921 0.0105  0.0145  0.0098  222 PRO B O   
4710 C CB  . PRO B 220 ? 0.1922 0.2139 0.1952 0.0045  0.0152  0.0101  222 PRO B CB  
4711 C CG  . PRO B 220 ? 0.1881 0.2061 0.1916 0.0050  0.0148  0.0096  222 PRO B CG  
4712 C CD  . PRO B 220 ? 0.1887 0.2050 0.1918 0.0048  0.0149  0.0089  222 PRO B CD  
4713 N N   . ALA B 221 ? 0.2059 0.2349 0.2043 0.0110  0.0150  0.0118  223 ALA B N   
4714 C CA  . ALA B 221 ? 0.2224 0.2515 0.2175 0.0148  0.0152  0.0125  223 ALA B CA  
4715 C C   . ALA B 221 ? 0.2220 0.2459 0.2166 0.0142  0.0145  0.0116  223 ALA B C   
4716 O O   . ALA B 221 ? 0.2300 0.2493 0.2198 0.0168  0.0146  0.0113  223 ALA B O   
4717 C CB  . ALA B 221 ? 0.2239 0.2620 0.2199 0.0157  0.0155  0.0143  223 ALA B CB  
4718 N N   . GLY B 222 ? 0.2246 0.2485 0.2226 0.0113  0.0141  0.0113  224 GLY B N   
4719 C CA  . GLY B 222 ? 0.2343 0.2556 0.2322 0.0110  0.0135  0.0109  224 GLY B CA  
4720 C C   . GLY B 222 ? 0.2483 0.2650 0.2446 0.0102  0.0128  0.0097  224 GLY B C   
4721 O O   . GLY B 222 ? 0.2397 0.2561 0.2361 0.0094  0.0121  0.0095  224 GLY B O   
4722 N N   . MET B 223 ? 0.2575 0.2713 0.2522 0.0099  0.0130  0.0090  225 MET B N   
4723 C CA  . MET B 223 ? 0.2892 0.2992 0.2825 0.0077  0.0125  0.0079  225 MET B CA  
4724 C C   . MET B 223 ? 0.2945 0.2980 0.2813 0.0085  0.0131  0.0072  225 MET B C   
4725 O O   . MET B 223 ? 0.3012 0.3046 0.2866 0.0112  0.0141  0.0078  225 MET B O   
4726 C CB  . MET B 223 ? 0.2964 0.3088 0.2943 0.0057  0.0125  0.0081  225 MET B CB  
4727 C CG  . MET B 223 ? 0.3351 0.3487 0.3339 0.0033  0.0117  0.0079  225 MET B CG  
4728 S SD  . MET B 223 ? 0.3860 0.4053 0.3904 0.0033  0.0121  0.0092  225 MET B SD  
4729 C CE  . MET B 223 ? 0.3831 0.4021 0.3884 0.0054  0.0133  0.0100  225 MET B CE  
4730 N N   . THR B 224 ? 0.3072 0.3053 0.2894 0.0061  0.0126  0.0061  226 THR B N   
4731 C CA  . THR B 224 ? 0.3251 0.3136 0.2983 0.0063  0.0136  0.0052  226 THR B CA  
4732 C C   . THR B 224 ? 0.3289 0.3153 0.3020 0.0018  0.0134  0.0043  226 THR B C   
4733 O O   . THR B 224 ? 0.3485 0.3379 0.3234 -0.0024 0.0121  0.0039  226 THR B O   
4734 C CB  . THR B 224 ? 0.3579 0.3390 0.3222 0.0064  0.0137  0.0044  226 THR B CB  
4735 O OG1 . THR B 224 ? 0.3412 0.3256 0.3064 0.0106  0.0140  0.0054  226 THR B OG1 
4736 C CG2 . THR B 224 ? 0.3801 0.3483 0.3324 0.0076  0.0156  0.0037  226 THR B CG2 
4737 N N   . TYR B 225 ? 0.3371 0.3199 0.3084 0.0028  0.0146  0.0044  227 TYR B N   
4738 C CA  . TYR B 225 ? 0.3213 0.3013 0.2915 -0.0011 0.0147  0.0037  227 TYR B CA  
4739 C C   . TYR B 225 ? 0.3493 0.3178 0.3080 -0.0045 0.0153  0.0024  227 TYR B C   
4740 O O   . TYR B 225 ? 0.3523 0.3113 0.3015 -0.0015 0.0166  0.0021  227 TYR B O   
4741 C CB  . TYR B 225 ? 0.3164 0.2966 0.2883 0.0019  0.0160  0.0045  227 TYR B CB  
4742 C CG  . TYR B 225 ? 0.3117 0.2868 0.2805 -0.0009 0.0167  0.0039  227 TYR B CG  
4743 C CD1 . TYR B 225 ? 0.3019 0.2822 0.2760 -0.0055 0.0157  0.0038  227 TYR B CD1 
4744 C CD2 . TYR B 225 ? 0.3291 0.2948 0.2894 0.0015  0.0187  0.0039  227 TYR B CD2 
4745 C CE1 . TYR B 225 ? 0.3061 0.2825 0.2776 -0.0082 0.0166  0.0036  227 TYR B CE1 
4746 C CE2 . TYR B 225 ? 0.3297 0.2898 0.2864 -0.0011 0.0197  0.0035  227 TYR B CE2 
4747 C CZ  . TYR B 225 ? 0.3177 0.2833 0.2802 -0.0065 0.0185  0.0032  227 TYR B CZ  
4748 O OH  . TYR B 225 ? 0.3382 0.2981 0.2965 -0.0091 0.0197  0.0030  227 TYR B OH  
4749 N N   . ASN B 226 ? 0.3580 0.3269 0.3164 -0.0108 0.0145  0.0016  228 ASN B N   
4750 C CA  . ASN B 226 ? 0.3872 0.3460 0.3342 -0.0166 0.0147  0.0001  228 ASN B CA  
4751 C C   . ASN B 226 ? 0.4156 0.3627 0.3537 -0.0181 0.0168  -0.0004 228 ASN B C   
4752 O O   . ASN B 226 ? 0.4333 0.3708 0.3608 -0.0247 0.0172  -0.0018 228 ASN B O   
4753 C CB  . ASN B 226 ? 0.3879 0.3569 0.3400 -0.0234 0.0124  0.0000  228 ASN B CB  
4754 C CG  . ASN B 226 ? 0.3678 0.3444 0.3243 -0.0217 0.0108  0.0003  228 ASN B CG  
4755 O OD1 . ASN B 226 ? 0.3735 0.3431 0.3241 -0.0186 0.0114  -0.0001 228 ASN B OD1 
4756 N ND2 . ASN B 226 ? 0.3557 0.3465 0.3221 -0.0229 0.0091  0.0015  228 ASN B ND2 
4757 N N   . ASN B 227 ? 0.4195 0.3668 0.3607 -0.0129 0.0182  0.0005  229 ASN B N   
4758 C CA  . ASN B 227 ? 0.4523 0.3880 0.3847 -0.0126 0.0206  0.0004  229 ASN B CA  
4759 C C   . ASN B 227 ? 0.4628 0.3984 0.3942 -0.0213 0.0201  -0.0003 229 ASN B C   
4760 O O   . ASN B 227 ? 0.5122 0.4334 0.4303 -0.0252 0.0219  -0.0014 229 ASN B O   
4761 C CB  . ASN B 227 ? 0.4843 0.4031 0.4009 -0.0089 0.0233  0.0000  229 ASN B CB  
4762 C CG  . ASN B 227 ? 0.4860 0.4085 0.4052 0.0005  0.0241  0.0015  229 ASN B CG  
4763 O OD1 . ASN B 227 ? 0.5297 0.4530 0.4498 0.0060  0.0256  0.0029  229 ASN B OD1 
4764 N ND2 . ASN B 227 ? 0.4908 0.4182 0.4128 0.0021  0.0229  0.0016  229 ASN B ND2 
4765 N N   . ASP B 228 ? 0.4330 0.3837 0.3768 -0.0242 0.0179  0.0003  230 ASP B N   
4766 C CA  . ASP B 228 ? 0.4422 0.3968 0.3862 -0.0327 0.0171  0.0000  230 ASP B CA  
4767 C C   . ASP B 228 ? 0.4365 0.4034 0.3923 -0.0317 0.0167  0.0015  230 ASP B C   
4768 O O   . ASP B 228 ? 0.4418 0.4183 0.4020 -0.0372 0.0155  0.0021  230 ASP B O   
4769 C CB  . ASP B 228 ? 0.4305 0.3921 0.3752 -0.0384 0.0149  -0.0004 230 ASP B CB  
4770 C CG  . ASP B 228 ? 0.3949 0.3725 0.3531 -0.0343 0.0130  0.0010  230 ASP B CG  
4771 O OD1 . ASP B 228 ? 0.3811 0.3617 0.3462 -0.0273 0.0135  0.0019  230 ASP B OD1 
4772 O OD2 . ASP B 228 ? 0.3747 0.3616 0.3357 -0.0385 0.0111  0.0012  230 ASP B OD2 
4773 N N   . ALA B 229 ? 0.4402 0.4069 0.4000 -0.0250 0.0177  0.0023  231 ALA B N   
4774 C CA  . ALA B 229 ? 0.4314 0.4076 0.4006 -0.0238 0.0176  0.0036  231 ALA B CA  
4775 C C   . ALA B 229 ? 0.4406 0.4140 0.4059 -0.0296 0.0185  0.0036  231 ALA B C   
4776 O O   . ALA B 229 ? 0.4309 0.3907 0.3852 -0.0312 0.0203  0.0026  231 ALA B O   
4777 C CB  . ALA B 229 ? 0.4239 0.3991 0.3960 -0.0166 0.0186  0.0041  231 ALA B CB  
4778 N N   . GLN B 230 ? 0.4554 0.4412 0.4286 -0.0322 0.0177  0.0049  232 GLN B N   
4779 C CA  . GLN B 230 ? 0.4740 0.4600 0.4454 -0.0372 0.0186  0.0053  232 GLN B CA  
4780 C C   . GLN B 230 ? 0.4219 0.4182 0.4032 -0.0332 0.0189  0.0071  232 GLN B C   
4781 O O   . GLN B 230 ? 0.3862 0.3921 0.3757 -0.0291 0.0180  0.0081  232 GLN B O   
4782 C CB  . GLN B 230 ? 0.5284 0.5205 0.4976 -0.0464 0.0174  0.0054  232 GLN B CB  
4783 C CG  . GLN B 230 ? 0.5975 0.5756 0.5535 -0.0518 0.0177  0.0033  232 GLN B CG  
4784 C CD  . GLN B 230 ? 0.6621 0.6480 0.6158 -0.0620 0.0161  0.0033  232 GLN B CD  
4785 O OE1 . GLN B 230 ? 0.6845 0.6871 0.6472 -0.0624 0.0140  0.0047  232 GLN B OE1 
4786 N NE2 . GLN B 230 ? 0.6967 0.6705 0.6375 -0.0703 0.0173  0.0019  232 GLN B NE2 
4787 N N   . VAL B 231 ? 0.4155 0.4080 0.3945 -0.0343 0.0204  0.0074  233 VAL B N   
4788 C CA  . VAL B 231 ? 0.3958 0.3952 0.3822 -0.0302 0.0210  0.0088  233 VAL B CA  
4789 C C   . VAL B 231 ? 0.4000 0.4086 0.3887 -0.0357 0.0212  0.0104  233 VAL B C   
4790 O O   . VAL B 231 ? 0.3975 0.4004 0.3789 -0.0423 0.0218  0.0099  233 VAL B O   
4791 C CB  . VAL B 231 ? 0.3988 0.3873 0.3811 -0.0258 0.0227  0.0081  233 VAL B CB  
4792 C CG1 . VAL B 231 ? 0.3840 0.3786 0.3733 -0.0209 0.0233  0.0093  233 VAL B CG1 
4793 C CG2 . VAL B 231 ? 0.3889 0.3691 0.3670 -0.0217 0.0226  0.0068  233 VAL B CG2 
4794 N N   . TYR B 232 ? 0.4021 0.4244 0.3996 -0.0329 0.0209  0.0125  234 TYR B N   
4795 C CA  . TYR B 232 ? 0.4281 0.4637 0.4295 -0.0370 0.0210  0.0148  234 TYR B CA  
4796 C C   . TYR B 232 ? 0.4342 0.4735 0.4403 -0.0315 0.0226  0.0165  234 TYR B C   
4797 O O   . TYR B 232 ? 0.4120 0.4510 0.4217 -0.0244 0.0229  0.0166  234 TYR B O   
4798 C CB  . TYR B 232 ? 0.4560 0.5067 0.4627 -0.0378 0.0195  0.0166  234 TYR B CB  
4799 C CG  . TYR B 232 ? 0.4884 0.5370 0.4901 -0.0442 0.0178  0.0150  234 TYR B CG  
4800 C CD1 . TYR B 232 ? 0.5109 0.5590 0.5063 -0.0541 0.0175  0.0146  234 TYR B CD1 
4801 C CD2 . TYR B 232 ? 0.4891 0.5349 0.4910 -0.0410 0.0167  0.0140  234 TYR B CD2 
4802 C CE1 . TYR B 232 ? 0.5349 0.5792 0.5239 -0.0607 0.0161  0.0129  234 TYR B CE1 
4803 C CE2 . TYR B 232 ? 0.5091 0.5522 0.5056 -0.0467 0.0152  0.0125  234 TYR B CE2 
4804 C CZ  . TYR B 232 ? 0.5370 0.5789 0.5267 -0.0566 0.0149  0.0119  234 TYR B CZ  
4805 O OH  . TYR B 232 ? 0.5897 0.6272 0.5722 -0.0629 0.0136  0.0102  234 TYR B OH  
4806 N N   . LEU B 233 ? 0.4632 0.5055 0.4685 -0.0352 0.0236  0.0176  235 LEU B N   
4807 C CA  . LEU B 233 ? 0.4839 0.5329 0.4941 -0.0304 0.0252  0.0198  235 LEU B CA  
4808 C C   . LEU B 233 ? 0.5030 0.5713 0.5199 -0.0299 0.0250  0.0232  235 LEU B C   
4809 O O   . LEU B 233 ? 0.5449 0.6231 0.5617 -0.0372 0.0241  0.0244  235 LEU B O   
4810 C CB  . LEU B 233 ? 0.5017 0.5450 0.5076 -0.0344 0.0266  0.0197  235 LEU B CB  
4811 C CG  . LEU B 233 ? 0.5192 0.5714 0.5295 -0.0314 0.0283  0.0223  235 LEU B CG  
4812 C CD1 . LEU B 233 ? 0.5177 0.5668 0.5309 -0.0220 0.0292  0.0223  235 LEU B CD1 
4813 C CD2 . LEU B 233 ? 0.5487 0.5945 0.5540 -0.0360 0.0297  0.0221  235 LEU B CD2 
4814 N N   . GLN B 234 ? 0.5158 0.5891 0.5372 -0.0217 0.0259  0.0249  236 GLN B N   
4815 C CA  . GLN B 234 ? 0.5689 0.6603 0.5958 -0.0187 0.0263  0.0287  236 GLN B CA  
4816 C C   . GLN B 234 ? 0.6401 0.7374 0.6692 -0.0134 0.0288  0.0316  236 GLN B C   
4817 O O   . GLN B 234 ? 0.6439 0.7315 0.6716 -0.0067 0.0304  0.0309  236 GLN B O   
4818 C CB  . GLN B 234 ? 0.5635 0.6537 0.5915 -0.0129 0.0259  0.0285  236 GLN B CB  
4819 C CG  . GLN B 234 ? 0.5761 0.6842 0.6085 -0.0092 0.0263  0.0325  236 GLN B CG  
4820 C CD  . GLN B 234 ? 0.5654 0.6698 0.5975 -0.0036 0.0261  0.0321  236 GLN B CD  
4821 O OE1 . GLN B 234 ? 0.5707 0.6671 0.6010 -0.0068 0.0242  0.0293  236 GLN B OE1 
4822 N NE2 . GLN B 234 ? 0.5630 0.6713 0.5958 0.0052  0.0284  0.0350  236 GLN B NE2 
4823 N N   . GLU B 235 ? 0.7398 0.8525 0.7716 -0.0170 0.0293  0.0347  237 GLU B N   
4824 C CA  . GLU B 235 ? 0.8193 0.9390 0.8529 -0.0123 0.0318  0.0378  237 GLU B CA  
4825 C C   . GLU B 235 ? 0.8706 1.0130 0.9093 -0.0084 0.0328  0.0430  237 GLU B C   
4826 O O   . GLU B 235 ? 0.8889 1.0482 0.9303 -0.0152 0.0319  0.0454  237 GLU B O   
4827 C CB  . GLU B 235 ? 0.8424 0.9594 0.8739 -0.0198 0.0320  0.0370  237 GLU B CB  
4828 C CG  . GLU B 235 ? 0.8934 1.0140 0.9260 -0.0148 0.0347  0.0395  237 GLU B CG  
4829 C CD  . GLU B 235 ? 0.9337 1.0440 0.9649 -0.0040 0.0366  0.0392  237 GLU B CD  
4830 O OE1 . GLU B 235 ? 0.9629 1.0810 0.9958 0.0035  0.0379  0.0419  237 GLU B OE1 
4831 O OE2 . GLU B 235 ? 0.9503 1.0444 0.9777 -0.0031 0.0370  0.0362  237 GLU B OE2 
4832 N N   . GLY B 236 ? 0.8745 1.0172 0.9134 0.0022  0.0347  0.0449  238 GLY B N   
4833 C CA  . GLY B 236 ? 0.8907 1.0535 0.9330 0.0092  0.0366  0.0506  238 GLY B CA  
4834 C C   . GLY B 236 ? 0.9387 1.1146 0.9838 0.0077  0.0348  0.0520  238 GLY B C   
4835 O O   . GLY B 236 ? 0.9597 1.1356 1.0038 0.0167  0.0362  0.0536  238 GLY B O   
4836 N N   . GLY B 237 ? 0.9310 1.1175 0.9784 -0.0033 0.0318  0.0515  239 GLY B N   
4837 C CA  . GLY B 237 ? 0.8984 1.0958 0.9477 -0.0070 0.0294  0.0519  239 GLY B CA  
4838 C C   . GLY B 237 ? 0.9111 1.1069 0.9590 -0.0210 0.0260  0.0485  239 GLY B C   
4839 O O   . GLY B 237 ? 0.9506 1.1615 1.0004 -0.0261 0.0239  0.0498  239 GLY B O   
4840 N N   . THR B 238 ? 0.8766 1.0544 0.9202 -0.0270 0.0256  0.0445  240 THR B N   
4841 C CA  . THR B 238 ? 0.8452 1.0189 0.8847 -0.0407 0.0233  0.0415  240 THR B CA  
4842 C C   . THR B 238 ? 0.7789 0.9251 0.8119 -0.0418 0.0229  0.0361  240 THR B C   
4843 O O   . THR B 238 ? 0.7703 0.9032 0.8020 -0.0363 0.0246  0.0349  240 THR B O   
4844 C CB  . THR B 238 ? 0.8746 1.0571 0.9141 -0.0474 0.0242  0.0434  240 THR B CB  
4845 O OG1 . THR B 238 ? 0.8842 1.0528 0.9226 -0.0409 0.0266  0.0426  240 THR B OG1 
4846 C CG2 . THR B 238 ? 0.9103 1.1226 0.9564 -0.0465 0.0248  0.0494  240 THR B CG2 
4847 N N   . GLU B 239 ? 0.7171 0.8561 0.7458 -0.0485 0.0207  0.0331  241 GLU B N   
4848 C CA  . GLU B 239 ? 0.6888 0.8031 0.7108 -0.0490 0.0204  0.0283  241 GLU B CA  
4849 C C   . GLU B 239 ? 0.6698 0.7730 0.6835 -0.0597 0.0203  0.0259  241 GLU B C   
4850 O O   . GLU B 239 ? 0.6816 0.7945 0.6931 -0.0697 0.0193  0.0267  241 GLU B O   
4851 C CB  . GLU B 239 ? 0.6862 0.7972 0.7072 -0.0482 0.0186  0.0266  241 GLU B CB  
4852 C CG  . GLU B 239 ? 0.6881 0.8012 0.7144 -0.0369 0.0193  0.0279  241 GLU B CG  
4853 C CD  . GLU B 239 ? 0.7191 0.8250 0.7433 -0.0365 0.0176  0.0256  241 GLU B CD  
4854 O OE1 . GLU B 239 ? 0.7878 0.8881 0.8066 -0.0445 0.0160  0.0233  241 GLU B OE1 
4855 O OE2 . GLU B 239 ? 0.7141 0.8189 0.7409 -0.0284 0.0182  0.0261  241 GLU B OE2 
4856 N N   . LYS B 240 ? 0.6573 0.7396 0.6651 -0.0578 0.0213  0.0229  242 LYS B N   
4857 C CA  . LYS B 240 ? 0.6826 0.7500 0.6800 -0.0666 0.0218  0.0205  242 LYS B CA  
4858 C C   . LYS B 240 ? 0.6346 0.6803 0.6249 -0.0632 0.0220  0.0169  242 LYS B C   
4859 O O   . LYS B 240 ? 0.5923 0.6312 0.5852 -0.0540 0.0227  0.0164  242 LYS B O   
4860 C CB  . LYS B 240 ? 0.7331 0.8004 0.7305 -0.0668 0.0239  0.0218  242 LYS B CB  
4861 C CG  . LYS B 240 ? 0.8031 0.8613 0.7902 -0.0781 0.0248  0.0207  242 LYS B CG  
4862 C CD  . LYS B 240 ? 0.8308 0.8925 0.8188 -0.0791 0.0268  0.0227  242 LYS B CD  
4863 C CE  . LYS B 240 ? 0.8509 0.9026 0.8409 -0.0684 0.0286  0.0223  242 LYS B CE  
4864 N NZ  . LYS B 240 ? 0.8625 0.8900 0.8426 -0.0669 0.0296  0.0189  242 LYS B NZ  
4865 N N   . ASP B 241 ? 0.6162 0.6514 0.5967 -0.0707 0.0214  0.0147  243 ASP B N   
4866 C CA  . ASP B 241 ? 0.6144 0.6303 0.5874 -0.0672 0.0217  0.0117  243 ASP B CA  
4867 C C   . ASP B 241 ? 0.5895 0.5889 0.5561 -0.0640 0.0242  0.0107  243 ASP B C   
4868 O O   . ASP B 241 ? 0.6283 0.6195 0.5859 -0.0710 0.0257  0.0103  243 ASP B O   
4869 C CB  . ASP B 241 ? 0.6501 0.6586 0.6128 -0.0760 0.0208  0.0097  243 ASP B CB  
4870 C CG  . ASP B 241 ? 0.6557 0.6465 0.6109 -0.0712 0.0212  0.0072  243 ASP B CG  
4871 O OD1 . ASP B 241 ? 0.6491 0.6353 0.6079 -0.0617 0.0219  0.0071  243 ASP B OD1 
4872 O OD2 . ASP B 241 ? 0.7179 0.7003 0.6635 -0.0773 0.0208  0.0055  243 ASP B OD2 
4873 N N   . ILE B 242 ? 0.5475 0.5425 0.5179 -0.0540 0.0248  0.0105  244 ILE B N   
4874 C CA  . ILE B 242 ? 0.5160 0.4969 0.4808 -0.0495 0.0270  0.0098  244 ILE B CA  
4875 C C   . ILE B 242 ? 0.4997 0.4654 0.4568 -0.0449 0.0276  0.0079  244 ILE B C   
4876 O O   . ILE B 242 ? 0.4842 0.4402 0.4376 -0.0392 0.0293  0.0076  244 ILE B O   
4877 C CB  . ILE B 242 ? 0.4946 0.4843 0.4693 -0.0422 0.0273  0.0113  244 ILE B CB  
4878 C CG1 . ILE B 242 ? 0.4611 0.4574 0.4440 -0.0348 0.0259  0.0114  244 ILE B CG1 
4879 C CG2 . ILE B 242 ? 0.5059 0.5097 0.4864 -0.0463 0.0274  0.0136  244 ILE B CG2 
4880 C CD1 . ILE B 242 ? 0.4373 0.4386 0.4269 -0.0282 0.0266  0.0125  244 ILE B CD1 
4881 N N   . SER B 243 ? 0.4870 0.4517 0.4417 -0.0470 0.0262  0.0068  245 SER B N   
4882 C CA  . SER B 243 ? 0.4735 0.4260 0.4216 -0.0422 0.0266  0.0053  245 SER B CA  
4883 C C   . SER B 243 ? 0.4974 0.4312 0.4325 -0.0399 0.0296  0.0047  245 SER B C   
4884 O O   . SER B 243 ? 0.4756 0.4043 0.4096 -0.0316 0.0304  0.0046  245 SER B O   
4885 C CB  . SER B 243 ? 0.4740 0.4250 0.4175 -0.0473 0.0253  0.0042  245 SER B CB  
4886 O OG  . SER B 243 ? 0.4562 0.4236 0.4116 -0.0460 0.0227  0.0049  245 SER B OG  
4887 N N   . THR B 244 ? 0.5477 0.4722 0.4731 -0.0466 0.0315  0.0045  246 THR B N   
4888 C CA  . THR B 244 ? 0.5839 0.4873 0.4934 -0.0447 0.0350  0.0040  246 THR B CA  
4889 C C   . THR B 244 ? 0.5584 0.4622 0.4718 -0.0350 0.0364  0.0052  246 THR B C   
4890 O O   . THR B 244 ? 0.5529 0.4418 0.4550 -0.0294 0.0392  0.0052  246 THR B O   
4891 C CB  . THR B 244 ? 0.6520 0.5454 0.5497 -0.0553 0.0369  0.0035  246 THR B CB  
4892 O OG1 . THR B 244 ? 0.7086 0.5794 0.5895 -0.0517 0.0408  0.0032  246 THR B OG1 
4893 C CG2 . THR B 244 ? 0.6644 0.5706 0.5711 -0.0594 0.0364  0.0050  246 THR B CG2 
4894 N N   . PHE B 245 ? 0.5211 0.4413 0.4491 -0.0325 0.0346  0.0063  247 PHE B N   
4895 C CA  . PHE B 245 ? 0.5003 0.4229 0.4329 -0.0238 0.0354  0.0073  247 PHE B CA  
4896 C C   . PHE B 245 ? 0.4650 0.3917 0.4021 -0.0159 0.0343  0.0072  247 PHE B C   
4897 O O   . PHE B 245 ? 0.4528 0.3791 0.3900 -0.0089 0.0353  0.0079  247 PHE B O   
4898 C CB  . PHE B 245 ? 0.4799 0.4171 0.4247 -0.0246 0.0343  0.0083  247 PHE B CB  
4899 C CG  . PHE B 245 ? 0.4932 0.4274 0.4341 -0.0303 0.0359  0.0090  247 PHE B CG  
4900 C CD1 . PHE B 245 ? 0.5075 0.4322 0.4417 -0.0270 0.0386  0.0096  247 PHE B CD1 
4901 C CD2 . PHE B 245 ? 0.5010 0.4433 0.4449 -0.0388 0.0349  0.0094  247 PHE B CD2 
4902 C CE1 . PHE B 245 ? 0.5212 0.4434 0.4518 -0.0324 0.0402  0.0103  247 PHE B CE1 
4903 C CE2 . PHE B 245 ? 0.5120 0.4533 0.4527 -0.0445 0.0364  0.0103  247 PHE B CE2 
4904 C CZ  . PHE B 245 ? 0.5310 0.4616 0.4650 -0.0414 0.0391  0.0107  247 PHE B CZ  
4905 N N   . PHE B 246 ? 0.4512 0.3830 0.3921 -0.0171 0.0322  0.0065  248 PHE B N   
4906 C CA  . PHE B 246 ? 0.4139 0.3525 0.3610 -0.0109 0.0308  0.0065  248 PHE B CA  
4907 C C   . PHE B 246 ? 0.4391 0.3673 0.3763 -0.0090 0.0316  0.0059  248 PHE B C   
4908 O O   . PHE B 246 ? 0.4557 0.3848 0.3931 -0.0127 0.0302  0.0050  248 PHE B O   
4909 C CB  . PHE B 246 ? 0.3770 0.3302 0.3365 -0.0131 0.0280  0.0065  248 PHE B CB  
4910 C CG  . PHE B 246 ? 0.3551 0.3181 0.3233 -0.0139 0.0275  0.0074  248 PHE B CG  
4911 C CD1 . PHE B 246 ? 0.3540 0.3182 0.3218 -0.0196 0.0280  0.0078  248 PHE B CD1 
4912 C CD2 . PHE B 246 ? 0.3339 0.3046 0.3097 -0.0092 0.0269  0.0078  248 PHE B CD2 
4913 C CE1 . PHE B 246 ? 0.3522 0.3258 0.3276 -0.0195 0.0279  0.0090  248 PHE B CE1 
4914 C CE2 . PHE B 246 ? 0.3187 0.2966 0.3007 -0.0094 0.0269  0.0086  248 PHE B CE2 
4915 C CZ  . PHE B 246 ? 0.3279 0.3075 0.3100 -0.0140 0.0274  0.0093  248 PHE B CZ  
4916 N N   . PRO B 247 ? 0.4512 0.3692 0.3788 -0.0026 0.0341  0.0065  249 PRO B N   
4917 C CA  . PRO B 247 ? 0.4675 0.3779 0.3869 0.0011  0.0350  0.0064  249 PRO B CA  
4918 C C   . PRO B 247 ? 0.4598 0.3850 0.3911 0.0047  0.0323  0.0067  249 PRO B C   
4919 O O   . PRO B 247 ? 0.4774 0.4146 0.4188 0.0073  0.0311  0.0074  249 PRO B O   
4920 C CB  . PRO B 247 ? 0.4759 0.3737 0.3826 0.0081  0.0387  0.0077  249 PRO B CB  
4921 C CG  . PRO B 247 ? 0.4570 0.3633 0.3712 0.0102  0.0386  0.0087  249 PRO B CG  
4922 C CD  . PRO B 247 ? 0.4426 0.3569 0.3666 0.0020  0.0363  0.0077  249 PRO B CD  
4923 N N   . ILE B 248 ? 0.4399 0.3645 0.3702 0.0033  0.0313  0.0059  250 ILE B N   
4924 C CA  . ILE B 248 ? 0.4144 0.3521 0.3555 0.0047  0.0287  0.0060  250 ILE B CA  
4925 C C   . ILE B 248 ? 0.4158 0.3488 0.3497 0.0109  0.0299  0.0067  250 ILE B C   
4926 O O   . ILE B 248 ? 0.4375 0.3564 0.3586 0.0110  0.0319  0.0063  250 ILE B O   
4927 C CB  . ILE B 248 ? 0.4159 0.3583 0.3624 -0.0025 0.0264  0.0048  250 ILE B CB  
4928 C CG1 . ILE B 248 ? 0.4033 0.3543 0.3588 -0.0065 0.0253  0.0050  250 ILE B CG1 
4929 C CG2 . ILE B 248 ? 0.4092 0.3600 0.3622 -0.0010 0.0244  0.0048  250 ILE B CG2 
4930 C CD1 . ILE B 248 ? 0.4005 0.3564 0.3595 -0.0135 0.0237  0.0044  250 ILE B CD1 
4931 N N   . SER B 249 ? 0.4040 0.3477 0.3444 0.0163  0.0292  0.0079  251 SER B N   
4932 C CA  . SER B 249 ? 0.4082 0.3516 0.3438 0.0227  0.0301  0.0091  251 SER B CA  
4933 C C   . SER B 249 ? 0.3858 0.3416 0.3317 0.0214  0.0274  0.0088  251 SER B C   
4934 O O   . SER B 249 ? 0.3662 0.3318 0.3228 0.0175  0.0252  0.0083  251 SER B O   
4935 C CB  . SER B 249 ? 0.4191 0.3649 0.3512 0.0306  0.0322  0.0113  251 SER B CB  
4936 O OG  . SER B 249 ? 0.4211 0.3814 0.3645 0.0301  0.0304  0.0118  251 SER B OG  
4937 N N   . TYR B 250 ? 0.3832 0.3364 0.3242 0.0245  0.0279  0.0092  252 TYR B N   
4938 C CA  . TYR B 250 ? 0.3705 0.3336 0.3187 0.0243  0.0259  0.0093  252 TYR B CA  
4939 C C   . TYR B 250 ? 0.3839 0.3503 0.3277 0.0323  0.0275  0.0116  252 TYR B C   
4940 O O   . TYR B 250 ? 0.3953 0.3507 0.3275 0.0365  0.0298  0.0121  252 TYR B O   
4941 C CB  . TYR B 250 ? 0.3577 0.3141 0.3034 0.0194  0.0250  0.0076  252 TYR B CB  
4942 C CG  . TYR B 250 ? 0.3384 0.3046 0.2924 0.0181  0.0228  0.0075  252 TYR B CG  
4943 C CD1 . TYR B 250 ? 0.3184 0.2964 0.2839 0.0157  0.0209  0.0076  252 TYR B CD1 
4944 C CD2 . TYR B 250 ? 0.3443 0.3071 0.2935 0.0197  0.0230  0.0074  252 TYR B CD2 
4945 C CE1 . TYR B 250 ? 0.3147 0.3004 0.2865 0.0147  0.0194  0.0076  252 TYR B CE1 
4946 C CE2 . TYR B 250 ? 0.3264 0.2981 0.2829 0.0187  0.0211  0.0075  252 TYR B CE2 
4947 C CZ  . TYR B 250 ? 0.3132 0.2960 0.2809 0.0162  0.0194  0.0076  252 TYR B CZ  
4948 O OH  . TYR B 250 ? 0.3044 0.2947 0.2784 0.0151  0.0179  0.0078  252 TYR B OH  
4949 N N   . THR B 251 ? 0.3873 0.3683 0.3390 0.0344  0.0266  0.0131  253 THR B N   
4950 C CA  . THR B 251 ? 0.4081 0.3975 0.3580 0.0415  0.0277  0.0157  253 THR B CA  
4951 C C   . THR B 251 ? 0.3899 0.3957 0.3514 0.0383  0.0252  0.0160  253 THR B C   
4952 O O   . THR B 251 ? 0.4050 0.4161 0.3737 0.0335  0.0237  0.0151  253 THR B O   
4953 C CB  . THR B 251 ? 0.4642 0.4566 0.4095 0.0482  0.0299  0.0182  253 THR B CB  
4954 O OG1 . THR B 251 ? 0.5195 0.4958 0.4549 0.0492  0.0321  0.0175  253 THR B OG1 
4955 C CG2 . THR B 251 ? 0.4901 0.4893 0.4304 0.0570  0.0317  0.0215  253 THR B CG2 
4956 N N   . GLY B 252 ? 0.3853 0.3978 0.3476 0.0407  0.0250  0.0173  254 GLY B N   
4957 C CA  . GLY B 252 ? 0.3489 0.3765 0.3205 0.0373  0.0230  0.0178  254 GLY B CA  
4958 C C   . GLY B 252 ? 0.3166 0.3414 0.2946 0.0297  0.0209  0.0153  254 GLY B C   
4959 O O   . GLY B 252 ? 0.3033 0.3371 0.2883 0.0252  0.0194  0.0151  254 GLY B O   
4960 N N   . ASN B 253 ? 0.2890 0.3019 0.2639 0.0281  0.0208  0.0135  255 ASN B N   
4961 C CA  . ASN B 253 ? 0.2729 0.2838 0.2535 0.0218  0.0191  0.0115  255 ASN B CA  
4962 C C   . ASN B 253 ? 0.2409 0.2527 0.2258 0.0181  0.0186  0.0106  255 ASN B C   
4963 O O   . ASN B 253 ? 0.2183 0.2323 0.2086 0.0139  0.0175  0.0098  255 ASN B O   
4964 C CB  . ASN B 253 ? 0.2583 0.2772 0.2443 0.0198  0.0179  0.0118  255 ASN B CB  
4965 C CG  . ASN B 253 ? 0.2674 0.2824 0.2504 0.0212  0.0178  0.0117  255 ASN B CG  
4966 O OD1 . ASN B 253 ? 0.2863 0.2986 0.2628 0.0261  0.0192  0.0128  255 ASN B OD1 
4967 N ND2 . ASN B 253 ? 0.2387 0.2528 0.2252 0.0175  0.0166  0.0107  255 ASN B ND2 
4968 N N   . VAL B 254 ? 0.2452 0.2545 0.2267 0.0202  0.0197  0.0110  256 VAL B N   
4969 C CA  . VAL B 254 ? 0.2330 0.2429 0.2180 0.0171  0.0194  0.0103  256 VAL B CA  
4970 C C   . VAL B 254 ? 0.2335 0.2328 0.2140 0.0166  0.0203  0.0093  256 VAL B C   
4971 O O   . VAL B 254 ? 0.2456 0.2388 0.2187 0.0204  0.0219  0.0100  256 VAL B O   
4972 C CB  . VAL B 254 ? 0.2332 0.2514 0.2187 0.0193  0.0198  0.0116  256 VAL B CB  
4973 C CG1 . VAL B 254 ? 0.2358 0.2523 0.2227 0.0172  0.0199  0.0109  256 VAL B CG1 
4974 C CG2 . VAL B 254 ? 0.2319 0.2612 0.2222 0.0172  0.0187  0.0123  256 VAL B CG2 
4975 N N   . ILE B 255 ? 0.2274 0.2242 0.2112 0.0121  0.0195  0.0081  257 ILE B N   
4976 C CA  . ILE B 255 ? 0.2447 0.2333 0.2247 0.0104  0.0203  0.0074  257 ILE B CA  
4977 C C   . ILE B 255 ? 0.2503 0.2412 0.2321 0.0108  0.0208  0.0077  257 ILE B C   
4978 O O   . ILE B 255 ? 0.2396 0.2366 0.2276 0.0088  0.0200  0.0076  257 ILE B O   
4979 C CB  . ILE B 255 ? 0.2435 0.2315 0.2267 0.0055  0.0192  0.0064  257 ILE B CB  
4980 C CG1 . ILE B 255 ? 0.2459 0.2335 0.2283 0.0048  0.0183  0.0061  257 ILE B CG1 
4981 C CG2 . ILE B 255 ? 0.2487 0.2298 0.2277 0.0027  0.0200  0.0059  257 ILE B CG2 
4982 C CD1 . ILE B 255 ? 0.2502 0.2413 0.2373 0.0006  0.0170  0.0057  257 ILE B CD1 
4983 N N   . THR B 256 ? 0.2744 0.2598 0.2499 0.0135  0.0225  0.0082  258 THR B N   
4984 C CA  . THR B 256 ? 0.2860 0.2721 0.2623 0.0136  0.0232  0.0085  258 THR B CA  
4985 C C   . THR B 256 ? 0.3076 0.2853 0.2809 0.0104  0.0239  0.0077  258 THR B C   
4986 O O   . THR B 256 ? 0.3275 0.2957 0.2925 0.0108  0.0252  0.0076  258 THR B O   
4987 C CB  . THR B 256 ? 0.2931 0.2806 0.2647 0.0193  0.0246  0.0100  258 THR B CB  
4988 O OG1 . THR B 256 ? 0.2804 0.2785 0.2562 0.0208  0.0235  0.0108  258 THR B OG1 
4989 C CG2 . THR B 256 ? 0.2928 0.2816 0.2651 0.0197  0.0253  0.0104  258 THR B CG2 
4990 N N   . ILE B 257 ? 0.3122 0.2931 0.2909 0.0070  0.0233  0.0073  259 ILE B N   
4991 C CA  . ILE B 257 ? 0.3225 0.2982 0.2994 0.0035  0.0241  0.0070  259 ILE B CA  
4992 C C   . ILE B 257 ? 0.3186 0.2958 0.2966 0.0049  0.0249  0.0075  259 ILE B C   
4993 O O   . ILE B 257 ? 0.2910 0.2755 0.2751 0.0051  0.0241  0.0076  259 ILE B O   
4994 C CB  . ILE B 257 ? 0.3283 0.3087 0.3110 -0.0010 0.0227  0.0067  259 ILE B CB  
4995 C CG1 . ILE B 257 ? 0.3428 0.3236 0.3252 -0.0021 0.0216  0.0062  259 ILE B CG1 
4996 C CG2 . ILE B 257 ? 0.3440 0.3215 0.3249 -0.0053 0.0234  0.0067  259 ILE B CG2 
4997 C CD1 . ILE B 257 ? 0.3264 0.3153 0.3159 -0.0011 0.0202  0.0064  259 ILE B CD1 
4998 N N   . THR B 258 ? 0.3401 0.3097 0.3111 0.0061  0.0268  0.0079  260 THR B N   
4999 C CA  . THR B 258 ? 0.3398 0.3101 0.3109 0.0078  0.0278  0.0085  260 THR B CA  
5000 C C   . THR B 258 ? 0.3561 0.3156 0.3188 0.0069  0.0300  0.0088  260 THR B C   
5001 O O   . THR B 258 ? 0.3690 0.3188 0.3224 0.0085  0.0316  0.0089  260 THR B O   
5002 C CB  . THR B 258 ? 0.3296 0.3052 0.3008 0.0131  0.0279  0.0094  260 THR B CB  
5003 O OG1 . THR B 258 ? 0.3323 0.3085 0.3033 0.0140  0.0288  0.0098  260 THR B OG1 
5004 C CG2 . THR B 258 ? 0.3377 0.3087 0.3009 0.0181  0.0294  0.0103  260 THR B CG2 
5005 N N   . PRO B 259 ? 0.3548 0.3149 0.3196 0.0044  0.0305  0.0089  261 PRO B N   
5006 C CA  . PRO B 259 ? 0.3817 0.3320 0.3384 0.0033  0.0328  0.0093  261 PRO B CA  
5007 C C   . PRO B 259 ? 0.3926 0.3409 0.3454 0.0091  0.0346  0.0104  261 PRO B C   
5008 O O   . PRO B 259 ? 0.4321 0.3719 0.3781 0.0085  0.0368  0.0109  261 PRO B O   
5009 C CB  . PRO B 259 ? 0.3696 0.3246 0.3321 -0.0019 0.0323  0.0093  261 PRO B CB  
5010 C CG  . PRO B 259 ? 0.3569 0.3236 0.3294 0.0001  0.0305  0.0093  261 PRO B CG  
5011 C CD  . PRO B 259 ? 0.3428 0.3125 0.3169 0.0028  0.0292  0.0089  261 PRO B CD  
5012 N N   . GLY B 260 ? 0.3808 0.3374 0.3376 0.0139  0.0336  0.0108  262 GLY B N   
5013 C CA  . GLY B 260 ? 0.3825 0.3420 0.3376 0.0192  0.0346  0.0120  262 GLY B CA  
5014 C C   . GLY B 260 ? 0.3822 0.3471 0.3434 0.0170  0.0340  0.0118  262 GLY B C   
5015 O O   . GLY B 260 ? 0.3793 0.3539 0.3463 0.0179  0.0325  0.0116  262 GLY B O   
5016 N N   . ASP B 261 ? 0.3706 0.3296 0.3302 0.0135  0.0352  0.0117  263 ASP B N   
5017 C CA  . ASP B 261 ? 0.3595 0.3235 0.3249 0.0113  0.0348  0.0116  263 ASP B CA  
5018 C C   . ASP B 261 ? 0.3423 0.3067 0.3114 0.0053  0.0343  0.0112  263 ASP B C   
5019 O O   . ASP B 261 ? 0.3530 0.3099 0.3166 0.0022  0.0355  0.0113  263 ASP B O   
5020 C CB  . ASP B 261 ? 0.3780 0.3370 0.3376 0.0139  0.0371  0.0127  263 ASP B CB  
5021 C CG  . ASP B 261 ? 0.3879 0.3517 0.3524 0.0127  0.0370  0.0128  263 ASP B CG  
5022 O OD1 . ASP B 261 ? 0.3780 0.3488 0.3497 0.0104  0.0354  0.0121  263 ASP B OD1 
5023 O OD2 . ASP B 261 ? 0.4253 0.3849 0.3852 0.0146  0.0389  0.0137  263 ASP B OD2 
5024 N N   . LEU B 262 ? 0.3216 0.2943 0.2985 0.0039  0.0327  0.0109  264 LEU B N   
5025 C CA  . LEU B 262 ? 0.3210 0.2970 0.3020 -0.0006 0.0323  0.0111  264 LEU B CA  
5026 C C   . LEU B 262 ? 0.3479 0.3227 0.3277 -0.0027 0.0340  0.0121  264 LEU B C   
5027 O O   . LEU B 262 ? 0.3778 0.3543 0.3583 -0.0074 0.0341  0.0127  264 LEU B O   
5028 C CB  . LEU B 262 ? 0.3039 0.2881 0.2921 0.0000  0.0309  0.0110  264 LEU B CB  
5029 C CG  . LEU B 262 ? 0.3039 0.2940 0.2966 -0.0032 0.0306  0.0118  264 LEU B CG  
5030 C CD1 . LEU B 262 ? 0.3072 0.2963 0.2987 -0.0065 0.0296  0.0114  264 LEU B CD1 
5031 C CD2 . LEU B 262 ? 0.2930 0.2890 0.2905 -0.0010 0.0301  0.0121  264 LEU B CD2 
5032 N N   . LYS B 263 ? 0.3539 0.3266 0.3315 0.0002  0.0352  0.0125  265 LYS B N   
5033 C CA  . LYS B 263 ? 0.3734 0.3444 0.3492 -0.0017 0.0370  0.0137  265 LYS B CA  
5034 C C   . LYS B 263 ? 0.3970 0.3587 0.3649 -0.0056 0.0385  0.0138  265 LYS B C   
5035 O O   . LYS B 263 ? 0.4178 0.3785 0.3840 -0.0091 0.0399  0.0148  265 LYS B O   
5036 C CB  . LYS B 263 ? 0.3736 0.3431 0.3475 0.0025  0.0382  0.0140  265 LYS B CB  
5037 C CG  . LYS B 263 ? 0.3671 0.3436 0.3464 0.0054  0.0372  0.0136  265 LYS B CG  
5038 C CD  . LYS B 263 ? 0.3654 0.3480 0.3499 0.0040  0.0374  0.0145  265 LYS B CD  
5039 C CE  . LYS B 263 ? 0.3654 0.3511 0.3518 0.0071  0.0371  0.0140  265 LYS B CE  
5040 N NZ  . LYS B 263 ? 0.3758 0.3658 0.3652 0.0073  0.0382  0.0153  265 LYS B NZ  
5041 N N   . TYR B 264 ? 0.3953 0.3496 0.3573 -0.0052 0.0384  0.0130  266 TYR B N   
5042 C CA  . TYR B 264 ? 0.4154 0.3586 0.3677 -0.0099 0.0401  0.0129  266 TYR B CA  
5043 C C   . TYR B 264 ? 0.4369 0.3861 0.3929 -0.0178 0.0392  0.0131  266 TYR B C   
5044 O O   . TYR B 264 ? 0.4648 0.4076 0.4139 -0.0238 0.0407  0.0135  266 TYR B O   
5045 C CB  . TYR B 264 ? 0.4184 0.3527 0.3633 -0.0079 0.0403  0.0121  266 TYR B CB  
5046 C CG  . TYR B 264 ? 0.4144 0.3415 0.3524 -0.0003 0.0420  0.0125  266 TYR B CG  
5047 C CD1 . TYR B 264 ? 0.4200 0.3396 0.3510 0.0021  0.0447  0.0136  266 TYR B CD1 
5048 C CD2 . TYR B 264 ? 0.4151 0.3434 0.3530 0.0045  0.0411  0.0122  266 TYR B CD2 
5049 C CE1 . TYR B 264 ? 0.4179 0.3326 0.3423 0.0101  0.0464  0.0145  266 TYR B CE1 
5050 C CE2 . TYR B 264 ? 0.4157 0.3399 0.3473 0.0121  0.0427  0.0132  266 TYR B CE2 
5051 C CZ  . TYR B 264 ? 0.4118 0.3297 0.3368 0.0151  0.0454  0.0144  266 TYR B CZ  
5052 O OH  . TYR B 264 ? 0.4130 0.3282 0.3314 0.0234  0.0472  0.0159  266 TYR B OH  
5053 N N   . VAL B 265 ? 0.4420 0.4032 0.4076 -0.0180 0.0369  0.0131  267 VAL B N   
5054 C CA  . VAL B 265 ? 0.4747 0.4457 0.4452 -0.0244 0.0358  0.0138  267 VAL B CA  
5055 C C   . VAL B 265 ? 0.5170 0.4979 0.4938 -0.0242 0.0364  0.0157  267 VAL B C   
5056 O O   . VAL B 265 ? 0.4913 0.4810 0.4759 -0.0194 0.0356  0.0162  267 VAL B O   
5057 C CB  . VAL B 265 ? 0.4563 0.4351 0.4331 -0.0237 0.0334  0.0133  267 VAL B CB  
5058 C CG1 . VAL B 265 ? 0.4607 0.4492 0.4406 -0.0304 0.0324  0.0143  267 VAL B CG1 
5059 C CG2 . VAL B 265 ? 0.4421 0.4115 0.4133 -0.0218 0.0329  0.0116  267 VAL B CG2 
5060 N N   . GLN B 266 ? 0.5892 0.5678 0.5617 -0.0293 0.0381  0.0167  268 GLN B N   
5061 C CA  . GLN B 266 ? 0.6638 0.6496 0.6402 -0.0287 0.0394  0.0186  268 GLN B CA  
5062 C C   . GLN B 266 ? 0.6689 0.6721 0.6544 -0.0307 0.0383  0.0206  268 GLN B C   
5063 O O   . GLN B 266 ? 0.6657 0.6772 0.6568 -0.0265 0.0389  0.0223  268 GLN B O   
5064 C CB  . GLN B 266 ? 0.7194 0.6964 0.6872 -0.0338 0.0417  0.0191  268 GLN B CB  
5065 C CG  . GLN B 266 ? 0.7398 0.6995 0.6976 -0.0300 0.0435  0.0178  268 GLN B CG  
5066 C CD  . GLN B 266 ? 0.7910 0.7395 0.7384 -0.0349 0.0464  0.0183  268 GLN B CD  
5067 O OE1 . GLN B 266 ? 0.8575 0.8121 0.8069 -0.0383 0.0474  0.0200  268 GLN B OE1 
5068 N NE2 . GLN B 266 ? 0.7955 0.7268 0.7304 -0.0348 0.0481  0.0172  268 GLN B NE2 
5069 N N   . ASP B 267 ? 0.6809 0.6897 0.6673 -0.0360 0.0368  0.0206  269 ASP B N   
5070 C CA  . ASP B 267 ? 0.7192 0.7465 0.7138 -0.0375 0.0358  0.0230  269 ASP B CA  
5071 C C   . ASP B 267 ? 0.6714 0.7053 0.6734 -0.0286 0.0352  0.0236  269 ASP B C   
5072 O O   . ASP B 267 ? 0.6349 0.6838 0.6433 -0.0271 0.0352  0.0262  269 ASP B O   
5073 C CB  . ASP B 267 ? 0.7931 0.8237 0.7856 -0.0457 0.0342  0.0226  269 ASP B CB  
5074 C CG  . ASP B 267 ? 0.8880 0.9185 0.8743 -0.0565 0.0351  0.0232  269 ASP B CG  
5075 O OD1 . ASP B 267 ? 0.9318 0.9601 0.9159 -0.0575 0.0371  0.0243  269 ASP B OD1 
5076 O OD2 . ASP B 267 ? 0.9351 0.9675 0.9181 -0.0646 0.0338  0.0227  269 ASP B OD2 
5077 N N   . VAL B 268 ? 0.6434 0.6669 0.6439 -0.0228 0.0350  0.0214  270 VAL B N   
5078 C CA  . VAL B 268 ? 0.5976 0.6244 0.6027 -0.0159 0.0343  0.0214  270 VAL B CA  
5079 C C   . VAL B 268 ? 0.5739 0.6052 0.5817 -0.0106 0.0361  0.0231  270 VAL B C   
5080 O O   . VAL B 268 ? 0.5876 0.6116 0.5924 -0.0088 0.0372  0.0225  270 VAL B O   
5081 C CB  . VAL B 268 ? 0.5732 0.5883 0.5751 -0.0128 0.0334  0.0186  270 VAL B CB  
5082 C CG1 . VAL B 268 ? 0.5452 0.5614 0.5500 -0.0065 0.0333  0.0183  270 VAL B CG1 
5083 C CG2 . VAL B 268 ? 0.6040 0.6158 0.6035 -0.0168 0.0319  0.0172  270 VAL B CG2 
5084 N N   . LYS B 269 ? 0.5802 0.6228 0.5926 -0.0075 0.0365  0.0255  271 LYS B N   
5085 C CA  . LYS B 269 ? 0.5744 0.6192 0.5876 -0.0009 0.0386  0.0272  271 LYS B CA  
5086 C C   . LYS B 269 ? 0.5320 0.5711 0.5442 0.0048  0.0385  0.0260  271 LYS B C   
5087 O O   . LYS B 269 ? 0.5425 0.5793 0.5550 0.0037  0.0368  0.0245  271 LYS B O   
5088 C CB  . LYS B 269 ? 0.6337 0.6948 0.6512 0.0000  0.0399  0.0314  271 LYS B CB  
5089 C CG  . LYS B 269 ? 0.6973 0.7688 0.7167 -0.0079 0.0395  0.0331  271 LYS B CG  
5090 C CD  . LYS B 269 ? 0.7713 0.8606 0.7949 -0.0058 0.0414  0.0378  271 LYS B CD  
5091 C CE  . LYS B 269 ? 0.8301 0.9378 0.8579 -0.0116 0.0403  0.0406  271 LYS B CE  
5092 N NZ  . LYS B 269 ? 0.8553 0.9623 0.8808 -0.0230 0.0391  0.0395  271 LYS B NZ  
5093 N N   . VAL B 270 ? 0.5072 0.5437 0.5175 0.0107  0.0405  0.0267  272 VAL B N   
5094 C CA  . VAL B 270 ? 0.4991 0.5287 0.5062 0.0159  0.0412  0.0258  272 VAL B CA  
5095 C C   . VAL B 270 ? 0.4987 0.5357 0.5081 0.0182  0.0412  0.0277  272 VAL B C   
5096 O O   . VAL B 270 ? 0.4615 0.4921 0.4683 0.0204  0.0410  0.0264  272 VAL B O   
5097 C CB  . VAL B 270 ? 0.5015 0.5268 0.5044 0.0212  0.0439  0.0267  272 VAL B CB  
5098 C CG1 . VAL B 270 ? 0.5013 0.5382 0.5066 0.0240  0.0462  0.0308  272 VAL B CG1 
5099 C CG2 . VAL B 270 ? 0.5229 0.5392 0.5201 0.0259  0.0452  0.0258  272 VAL B CG2 
5100 N N   . SER B 271 ? 0.5170 0.5681 0.5308 0.0178  0.0416  0.0310  273 SER B N   
5101 C CA  . SER B 271 ? 0.5162 0.5772 0.5323 0.0208  0.0419  0.0336  273 SER B CA  
5102 C C   . SER B 271 ? 0.4906 0.5552 0.5100 0.0145  0.0388  0.0322  273 SER B C   
5103 O O   . SER B 271 ? 0.4698 0.5437 0.4916 0.0161  0.0387  0.0342  273 SER B O   
5104 C CB  . SER B 271 ? 0.5402 0.6175 0.5595 0.0237  0.0439  0.0384  273 SER B CB  
5105 O OG  . SER B 271 ? 0.5459 0.6334 0.5696 0.0160  0.0423  0.0390  273 SER B OG  
5106 N N   . SER B 272 ? 0.4710 0.5285 0.4898 0.0080  0.0368  0.0290  274 SER B N   
5107 C CA  . SER B 272 ? 0.4529 0.5113 0.4730 0.0018  0.0341  0.0274  274 SER B CA  
5108 C C   . SER B 272 ? 0.4339 0.4848 0.4525 0.0042  0.0331  0.0254  274 SER B C   
5109 O O   . SER B 272 ? 0.4240 0.4642 0.4392 0.0078  0.0339  0.0237  274 SER B O   
5110 C CB  . SER B 272 ? 0.4601 0.5106 0.4777 -0.0041 0.0330  0.0250  274 SER B CB  
5111 O OG  . SER B 272 ? 0.5196 0.5764 0.5378 -0.0071 0.0341  0.0268  274 SER B OG  
5112 N N   . LYS B 273 ? 0.4138 0.4702 0.4345 0.0015  0.0314  0.0255  275 LYS B N   
5113 C CA  . LYS B 273 ? 0.4069 0.4559 0.4262 0.0018  0.0299  0.0232  275 LYS B CA  
5114 C C   . LYS B 273 ? 0.3650 0.4086 0.3826 -0.0046 0.0278  0.0206  275 LYS B C   
5115 O O   . LYS B 273 ? 0.3537 0.4028 0.3717 -0.0101 0.0271  0.0212  275 LYS B O   
5116 C CB  . LYS B 273 ? 0.4027 0.4602 0.4241 0.0053  0.0302  0.0254  275 LYS B CB  
5117 C CG  . LYS B 273 ? 0.4273 0.4830 0.4467 0.0132  0.0330  0.0273  275 LYS B CG  
5118 C CD  . LYS B 273 ? 0.4643 0.5263 0.4840 0.0184  0.0341  0.0299  275 LYS B CD  
5119 C CE  . LYS B 273 ? 0.5020 0.5610 0.5174 0.0265  0.0378  0.0322  275 LYS B CE  
5120 N NZ  . LYS B 273 ? 0.5332 0.6035 0.5493 0.0326  0.0396  0.0364  275 LYS B NZ  
5121 N N   . ILE B 274 ? 0.3272 0.3599 0.3420 -0.0039 0.0271  0.0179  276 ILE B N   
5122 C CA  . ILE B 274 ? 0.3190 0.3457 0.3310 -0.0081 0.0254  0.0157  276 ILE B CA  
5123 C C   . ILE B 274 ? 0.3081 0.3374 0.3215 -0.0075 0.0241  0.0155  276 ILE B C   
5124 O O   . ILE B 274 ? 0.2947 0.3215 0.3084 -0.0033 0.0244  0.0153  276 ILE B O   
5125 C CB  . ILE B 274 ? 0.3110 0.3266 0.3190 -0.0071 0.0256  0.0136  276 ILE B CB  
5126 C CG1 . ILE B 274 ? 0.3187 0.3322 0.3256 -0.0060 0.0271  0.0140  276 ILE B CG1 
5127 C CG2 . ILE B 274 ? 0.3132 0.3225 0.3168 -0.0106 0.0246  0.0120  276 ILE B CG2 
5128 C CD1 . ILE B 274 ? 0.3314 0.3463 0.3369 -0.0106 0.0276  0.0147  276 ILE B CD1 
5129 N N   . VAL B 275 ? 0.3073 0.3410 0.3207 -0.0120 0.0228  0.0157  277 VAL B N   
5130 C CA  . VAL B 275 ? 0.3090 0.3464 0.3239 -0.0116 0.0216  0.0157  277 VAL B CA  
5131 C C   . VAL B 275 ? 0.3139 0.3440 0.3243 -0.0157 0.0201  0.0135  277 VAL B C   
5132 O O   . VAL B 275 ? 0.3162 0.3447 0.3231 -0.0212 0.0199  0.0130  277 VAL B O   
5133 C CB  . VAL B 275 ? 0.3199 0.3717 0.3388 -0.0121 0.0214  0.0185  277 VAL B CB  
5134 C CG1 . VAL B 275 ? 0.3219 0.3773 0.3420 -0.0110 0.0202  0.0187  277 VAL B CG1 
5135 C CG2 . VAL B 275 ? 0.3146 0.3726 0.3364 -0.0067 0.0235  0.0211  277 VAL B CG2 
5136 N N   . ILE B 276 ? 0.3165 0.3415 0.3261 -0.0129 0.0195  0.0122  278 ILE B N   
5137 C CA  . ILE B 276 ? 0.3239 0.3415 0.3287 -0.0151 0.0185  0.0103  278 ILE B CA  
5138 C C   . ILE B 276 ? 0.3183 0.3426 0.3251 -0.0161 0.0172  0.0109  278 ILE B C   
5139 O O   . ILE B 276 ? 0.3216 0.3512 0.3326 -0.0121 0.0173  0.0120  278 ILE B O   
5140 C CB  . ILE B 276 ? 0.3313 0.3408 0.3341 -0.0110 0.0189  0.0090  278 ILE B CB  
5141 C CG1 . ILE B 276 ? 0.3350 0.3387 0.3353 -0.0099 0.0201  0.0086  278 ILE B CG1 
5142 C CG2 . ILE B 276 ? 0.3338 0.3375 0.3320 -0.0117 0.0181  0.0077  278 ILE B CG2 
5143 C CD1 . ILE B 276 ? 0.3331 0.3407 0.3374 -0.0073 0.0210  0.0096  278 ILE B CD1 
5144 N N   . ARG B 277 ? 0.3248 0.3476 0.3274 -0.0212 0.0162  0.0100  279 ARG B N   
5145 C CA  . ARG B 277 ? 0.3365 0.3645 0.3400 -0.0221 0.0147  0.0102  279 ARG B CA  
5146 C C   . ARG B 277 ? 0.3225 0.3397 0.3186 -0.0241 0.0142  0.0080  279 ARG B C   
5147 O O   . ARG B 277 ? 0.3162 0.3235 0.3050 -0.0272 0.0149  0.0067  279 ARG B O   
5148 C CB  . ARG B 277 ? 0.3733 0.4141 0.3792 -0.0270 0.0138  0.0118  279 ARG B CB  
5149 C CG  . ARG B 277 ? 0.3934 0.4468 0.4066 -0.0226 0.0145  0.0148  279 ARG B CG  
5150 C CD  . ARG B 277 ? 0.4259 0.4955 0.4420 -0.0264 0.0135  0.0171  279 ARG B CD  
5151 N NE  . ARG B 277 ? 0.4420 0.5219 0.4633 -0.0223 0.0150  0.0201  279 ARG B NE  
5152 C CZ  . ARG B 277 ? 0.4631 0.5501 0.4853 -0.0259 0.0155  0.0215  279 ARG B CZ  
5153 N NH1 . ARG B 277 ? 0.4737 0.5580 0.4915 -0.0346 0.0146  0.0199  279 ARG B NH1 
5154 N NH2 . ARG B 277 ? 0.4615 0.5580 0.4882 -0.0207 0.0172  0.0245  279 ARG B NH2 
5155 N N   . TYR B 278 ? 0.2966 0.3148 0.2939 -0.0215 0.0133  0.0078  280 TYR B N   
5156 C CA  . TYR B 278 ? 0.2958 0.3048 0.2861 -0.0224 0.0129  0.0061  280 TYR B CA  
5157 C C   . TYR B 278 ? 0.2882 0.3042 0.2817 -0.0214 0.0116  0.0066  280 TYR B C   
5158 O O   . TYR B 278 ? 0.2682 0.2948 0.2688 -0.0190 0.0113  0.0084  280 TYR B O   
5159 C CB  . TYR B 278 ? 0.2860 0.2852 0.2733 -0.0174 0.0142  0.0053  280 TYR B CB  
5160 C CG  . TYR B 278 ? 0.2624 0.2661 0.2561 -0.0118 0.0142  0.0061  280 TYR B CG  
5161 C CD1 . TYR B 278 ? 0.2565 0.2633 0.2549 -0.0096 0.0150  0.0069  280 TYR B CD1 
5162 C CD2 . TYR B 278 ? 0.2505 0.2544 0.2445 -0.0093 0.0137  0.0060  280 TYR B CD2 
5163 C CE1 . TYR B 278 ? 0.2475 0.2568 0.2498 -0.0057 0.0153  0.0075  280 TYR B CE1 
5164 C CE2 . TYR B 278 ? 0.2386 0.2459 0.2373 -0.0054 0.0139  0.0067  280 TYR B CE2 
5165 C CZ  . TYR B 278 ? 0.2361 0.2457 0.2385 -0.0040 0.0148  0.0074  280 TYR B CZ  
5166 O OH  . TYR B 278 ? 0.2168 0.2279 0.2219 -0.0013 0.0153  0.0079  280 TYR B OH  
5167 N N   . THR B 279 ? 0.2964 0.3057 0.2836 -0.0227 0.0110  0.0052  281 THR B N   
5168 C CA  . THR B 279 ? 0.3032 0.3175 0.2926 -0.0210 0.0099  0.0056  281 THR B CA  
5169 C C   . THR B 279 ? 0.3114 0.3174 0.2980 -0.0162 0.0105  0.0048  281 THR B C   
5170 O O   . THR B 279 ? 0.3118 0.3073 0.2919 -0.0154 0.0117  0.0037  281 THR B O   
5171 C CB  . THR B 279 ? 0.3202 0.3372 0.3052 -0.0274 0.0084  0.0050  281 THR B CB  
5172 O OG1 . THR B 279 ? 0.3412 0.3438 0.3150 -0.0305 0.0090  0.0029  281 THR B OG1 
5173 C CG2 . THR B 279 ? 0.3243 0.3530 0.3128 -0.0325 0.0076  0.0064  281 THR B CG2 
5174 N N   . ALA B 280 ? 0.3180 0.3292 0.3088 -0.0129 0.0100  0.0056  282 ALA B N   
5175 C CA  . ALA B 280 ? 0.3112 0.3175 0.2999 -0.0088 0.0104  0.0052  282 ALA B CA  
5176 C C   . ALA B 280 ? 0.3200 0.3318 0.3102 -0.0089 0.0092  0.0057  282 ALA B C   
5177 O O   . ALA B 280 ? 0.3282 0.3487 0.3220 -0.0112 0.0082  0.0066  282 ALA B O   
5178 C CB  . ALA B 280 ? 0.2929 0.3005 0.2864 -0.0045 0.0114  0.0060  282 ALA B CB  
5179 N N   . ARG B 281 ? 0.3282 0.3362 0.3156 -0.0063 0.0092  0.0053  283 ARG B N   
5180 C CA  . ARG B 281 ? 0.3380 0.3511 0.3267 -0.0058 0.0082  0.0058  283 ARG B CA  
5181 C C   . ARG B 281 ? 0.3019 0.3141 0.2920 -0.0009 0.0090  0.0064  283 ARG B C   
5182 O O   . ARG B 281 ? 0.3078 0.3139 0.2943 0.0011  0.0099  0.0060  283 ARG B O   
5183 C CB  . ARG B 281 ? 0.3880 0.3969 0.3690 -0.0097 0.0072  0.0044  283 ARG B CB  
5184 C CG  . ARG B 281 ? 0.4390 0.4350 0.4103 -0.0088 0.0083  0.0030  283 ARG B CG  
5185 C CD  . ARG B 281 ? 0.4943 0.4827 0.4551 -0.0138 0.0078  0.0012  283 ARG B CD  
5186 N NE  . ARG B 281 ? 0.5282 0.5025 0.4788 -0.0114 0.0098  0.0003  283 ARG B NE  
5187 C CZ  . ARG B 281 ? 0.5586 0.5277 0.5051 -0.0060 0.0109  0.0005  283 ARG B CZ  
5188 N NH1 . ARG B 281 ? 0.5624 0.5387 0.5138 -0.0035 0.0099  0.0014  283 ARG B NH1 
5189 N NH2 . ARG B 281 ? 0.5879 0.5447 0.5246 -0.0027 0.0132  0.0002  283 ARG B NH2 
5190 N N   . LEU B 282 ? 0.2884 0.3071 0.2834 0.0008  0.0088  0.0078  284 LEU B N   
5191 C CA  . LEU B 282 ? 0.2807 0.2990 0.2761 0.0043  0.0094  0.0084  284 LEU B CA  
5192 C C   . LEU B 282 ? 0.2756 0.2888 0.2646 0.0049  0.0091  0.0075  284 LEU B C   
5193 O O   . LEU B 282 ? 0.2908 0.3024 0.2756 0.0023  0.0080  0.0065  284 LEU B O   
5194 C CB  . LEU B 282 ? 0.2741 0.2987 0.2735 0.0055  0.0093  0.0099  284 LEU B CB  
5195 C CG  . LEU B 282 ? 0.2727 0.2997 0.2764 0.0068  0.0106  0.0113  284 LEU B CG  
5196 C CD1 . LEU B 282 ? 0.2765 0.3085 0.2820 0.0088  0.0110  0.0131  284 LEU B CD1 
5197 C CD2 . LEU B 282 ? 0.2688 0.2923 0.2725 0.0080  0.0120  0.0113  284 LEU B CD2 
5198 N N   . ASN B 283 ? 0.2667 0.2778 0.2544 0.0081  0.0101  0.0078  285 ASN B N   
5199 C CA  . ASN B 283 ? 0.2781 0.2845 0.2593 0.0104  0.0104  0.0075  285 ASN B CA  
5200 C C   . ASN B 283 ? 0.2847 0.2960 0.2687 0.0132  0.0107  0.0089  285 ASN B C   
5201 O O   . ASN B 283 ? 0.2709 0.2877 0.2609 0.0128  0.0107  0.0100  285 ASN B O   
5202 C CB  . ASN B 283 ? 0.2774 0.2779 0.2533 0.0127  0.0118  0.0073  285 ASN B CB  
5203 C CG  . ASN B 283 ? 0.2587 0.2647 0.2400 0.0146  0.0127  0.0086  285 ASN B CG  
5204 O OD1 . ASN B 283 ? 0.2453 0.2574 0.2305 0.0160  0.0128  0.0099  285 ASN B OD1 
5205 N ND2 . ASN B 283 ? 0.2426 0.2466 0.2235 0.0142  0.0132  0.0084  285 ASN B ND2 
5206 N N   . ASP B 284 ? 0.3159 0.3245 0.2947 0.0162  0.0113  0.0092  286 ASP B N   
5207 C CA  . ASP B 284 ? 0.3215 0.3347 0.3021 0.0185  0.0115  0.0105  286 ASP B CA  
5208 C C   . ASP B 284 ? 0.3099 0.3295 0.2960 0.0193  0.0124  0.0121  286 ASP B C   
5209 O O   . ASP B 284 ? 0.3060 0.3300 0.2954 0.0191  0.0126  0.0132  286 ASP B O   
5210 C CB  . ASP B 284 ? 0.3541 0.3626 0.3269 0.0219  0.0121  0.0105  286 ASP B CB  
5211 C CG  . ASP B 284 ? 0.3957 0.3973 0.3619 0.0196  0.0111  0.0087  286 ASP B CG  
5212 O OD1 . ASP B 284 ? 0.3973 0.4025 0.3674 0.0158  0.0095  0.0081  286 ASP B OD1 
5213 O OD2 . ASP B 284 ? 0.4342 0.4267 0.3903 0.0215  0.0120  0.0079  286 ASP B OD2 
5214 N N   . ASP B 285 ? 0.2963 0.3162 0.2830 0.0193  0.0131  0.0122  287 ASP B N   
5215 C CA  . ASP B 285 ? 0.2925 0.3190 0.2835 0.0188  0.0138  0.0135  287 ASP B CA  
5216 C C   . ASP B 285 ? 0.2588 0.2859 0.2545 0.0150  0.0136  0.0132  287 ASP B C   
5217 O O   . ASP B 285 ? 0.2408 0.2716 0.2389 0.0133  0.0143  0.0139  287 ASP B O   
5218 C CB  . ASP B 285 ? 0.3228 0.3501 0.3117 0.0208  0.0146  0.0139  287 ASP B CB  
5219 C CG  . ASP B 285 ? 0.3623 0.3877 0.3447 0.0260  0.0156  0.0147  287 ASP B CG  
5220 O OD1 . ASP B 285 ? 0.3977 0.4263 0.3792 0.0282  0.0159  0.0159  287 ASP B OD1 
5221 O OD2 . ASP B 285 ? 0.4321 0.4523 0.4094 0.0283  0.0163  0.0143  287 ASP B OD2 
5222 N N   . ALA B 286 ? 0.2334 0.2575 0.2299 0.0138  0.0129  0.0124  288 ALA B N   
5223 C CA  . ALA B 286 ? 0.2252 0.2493 0.2248 0.0116  0.0132  0.0125  288 ALA B CA  
5224 C C   . ALA B 286 ? 0.2150 0.2409 0.2156 0.0109  0.0144  0.0137  288 ALA B C   
5225 O O   . ALA B 286 ? 0.2218 0.2493 0.2214 0.0120  0.0145  0.0145  288 ALA B O   
5226 C CB  . ALA B 286 ? 0.2303 0.2537 0.2303 0.0114  0.0124  0.0121  288 ALA B CB  
5227 N N   . VAL B 287 ? 0.2073 0.2318 0.2085 0.0089  0.0154  0.0139  289 VAL B N   
5228 C CA  . VAL B 287 ? 0.2098 0.2326 0.2096 0.0072  0.0171  0.0149  289 VAL B CA  
5229 C C   . VAL B 287 ? 0.2140 0.2337 0.2130 0.0092  0.0178  0.0156  289 VAL B C   
5230 O O   . VAL B 287 ? 0.2118 0.2307 0.2118 0.0105  0.0175  0.0154  289 VAL B O   
5231 C CB  . VAL B 287 ? 0.2127 0.2331 0.2113 0.0039  0.0182  0.0146  289 VAL B CB  
5232 C CG1 . VAL B 287 ? 0.2196 0.2345 0.2141 0.0016  0.0204  0.0153  289 VAL B CG1 
5233 C CG2 . VAL B 287 ? 0.2147 0.2409 0.2142 0.0021  0.0175  0.0144  289 VAL B CG2 
5234 N N   . MET B 288 ? 0.2215 0.2402 0.2184 0.0096  0.0189  0.0168  290 MET B N   
5235 C CA  . MET B 288 ? 0.2322 0.2482 0.2274 0.0123  0.0200  0.0181  290 MET B CA  
5236 C C   . MET B 288 ? 0.2297 0.2379 0.2200 0.0113  0.0230  0.0189  290 MET B C   
5237 O O   . MET B 288 ? 0.2379 0.2425 0.2247 0.0079  0.0244  0.0190  290 MET B O   
5238 C CB  . MET B 288 ? 0.2412 0.2592 0.2355 0.0138  0.0200  0.0190  290 MET B CB  
5239 C CG  . MET B 288 ? 0.2406 0.2643 0.2373 0.0145  0.0176  0.0182  290 MET B CG  
5240 S SD  . MET B 288 ? 0.2662 0.2927 0.2647 0.0168  0.0156  0.0175  290 MET B SD  
5241 C CE  . MET B 288 ? 0.2723 0.2992 0.2716 0.0151  0.0139  0.0155  290 MET B CE  
5242 N N   . GLY B 289 ? 0.2280 0.2335 0.2172 0.0144  0.0241  0.0197  291 GLY B N   
5243 C CA  . GLY B 289 ? 0.2426 0.2384 0.2251 0.0149  0.0275  0.0207  291 GLY B CA  
5244 C C   . GLY B 289 ? 0.2455 0.2366 0.2257 0.0098  0.0280  0.0192  291 GLY B C   
5245 O O   . GLY B 289 ? 0.2190 0.2158 0.2045 0.0083  0.0257  0.0178  291 GLY B O   
5246 N N   . GLY B 290 ? 0.2570 0.2379 0.2290 0.0070  0.0311  0.0196  292 GLY B N   
5247 C CA  . GLY B 290 ? 0.2651 0.2415 0.2331 0.0005  0.0317  0.0182  292 GLY B CA  
5248 C C   . GLY B 290 ? 0.2647 0.2411 0.2345 0.0003  0.0311  0.0171  292 GLY B C   
5249 O O   . GLY B 290 ? 0.2774 0.2498 0.2457 0.0050  0.0325  0.0179  292 GLY B O   
5250 N N   . LEU B 291 ? 0.2503 0.2325 0.2235 -0.0042 0.0291  0.0156  293 LEU B N   
5251 C CA  . LEU B 291 ? 0.2520 0.2339 0.2263 -0.0053 0.0286  0.0144  293 LEU B CA  
5252 C C   . LEU B 291 ? 0.2323 0.2227 0.2150 -0.0008 0.0261  0.0142  293 LEU B C   
5253 O O   . LEU B 291 ? 0.2361 0.2275 0.2206 -0.0011 0.0255  0.0134  293 LEU B O   
5254 C CB  . LEU B 291 ? 0.2504 0.2362 0.2241 -0.0121 0.0276  0.0132  293 LEU B CB  
5255 C CG  . LEU B 291 ? 0.2735 0.2513 0.2379 -0.0185 0.0300  0.0132  293 LEU B CG  
5256 C CD1 . LEU B 291 ? 0.2799 0.2641 0.2440 -0.0259 0.0288  0.0121  293 LEU B CD1 
5257 C CD2 . LEU B 291 ? 0.2957 0.2573 0.2497 -0.0180 0.0337  0.0132  293 LEU B CD2 
5258 N N   . GLY B 292 ? 0.2178 0.2138 0.2047 0.0024  0.0248  0.0150  294 GLY B N   
5259 C CA  . GLY B 292 ? 0.2027 0.2054 0.1957 0.0056  0.0226  0.0148  294 GLY B CA  
5260 C C   . GLY B 292 ? 0.1839 0.1922 0.1809 0.0037  0.0204  0.0134  294 GLY B C   
5261 O O   . GLY B 292 ? 0.1726 0.1831 0.1691 0.0009  0.0200  0.0130  294 GLY B O   
5262 N N   . ASN B 293 ? 0.1779 0.1890 0.1782 0.0055  0.0191  0.0130  295 ASN B N   
5263 C CA  . ASN B 293 ? 0.1793 0.1940 0.1820 0.0047  0.0174  0.0119  295 ASN B CA  
5264 C C   . ASN B 293 ? 0.1833 0.1963 0.1864 0.0040  0.0177  0.0113  295 ASN B C   
5265 O O   . ASN B 293 ? 0.1948 0.2087 0.1995 0.0051  0.0172  0.0113  295 ASN B O   
5266 C CB  . ASN B 293 ? 0.1754 0.1932 0.1797 0.0064  0.0158  0.0117  295 ASN B CB  
5267 C CG  . ASN B 293 ? 0.1801 0.1993 0.1836 0.0075  0.0156  0.0124  295 ASN B CG  
5268 O OD1 . ASN B 293 ? 0.1875 0.2085 0.1904 0.0074  0.0151  0.0122  295 ASN B OD1 
5269 N ND2 . ASN B 293 ? 0.1668 0.1856 0.1700 0.0089  0.0162  0.0134  295 ASN B ND2 
5270 N N   . PRO B 294 ? 0.1882 0.1987 0.1893 0.0018  0.0187  0.0109  296 PRO B N   
5271 C CA  . PRO B 294 ? 0.1921 0.2003 0.1930 0.0016  0.0193  0.0105  296 PRO B CA  
5272 C C   . PRO B 294 ? 0.1863 0.1976 0.1893 0.0013  0.0179  0.0096  296 PRO B C   
5273 O O   . PRO B 294 ? 0.1942 0.2087 0.1974 0.0008  0.0171  0.0094  296 PRO B O   
5274 C CB  . PRO B 294 ? 0.1975 0.2007 0.1939 -0.0011 0.0210  0.0103  296 PRO B CB  
5275 C CG  . PRO B 294 ? 0.2006 0.2064 0.1958 -0.0037 0.0206  0.0103  296 PRO B CG  
5276 C CD  . PRO B 294 ? 0.1931 0.2031 0.1914 -0.0011 0.0194  0.0110  296 PRO B CD  
5277 N N   . ASN B 295 ? 0.1823 0.1929 0.1866 0.0021  0.0179  0.0095  297 ASN B N   
5278 C CA  . ASN B 295 ? 0.1722 0.1836 0.1770 0.0017  0.0173  0.0087  297 ASN B CA  
5279 C C   . ASN B 295 ? 0.1748 0.1835 0.1785 0.0007  0.0185  0.0085  297 ASN B C   
5280 O O   . ASN B 295 ? 0.1788 0.1846 0.1816 0.0015  0.0198  0.0091  297 ASN B O   
5281 C CB  . ASN B 295 ? 0.1698 0.1818 0.1757 0.0024  0.0164  0.0086  297 ASN B CB  
5282 C CG  . ASN B 295 ? 0.1783 0.1907 0.1857 0.0026  0.0169  0.0092  297 ASN B CG  
5283 O OD1 . ASN B 295 ? 0.1708 0.1846 0.1788 0.0037  0.0174  0.0102  297 ASN B OD1 
5284 N N   . ILE B 296 ? 0.1696 0.1793 0.1724 -0.0004 0.0183  0.0079  298 ILE B N   
5285 C CA  . ILE B 296 ? 0.1734 0.1806 0.1740 -0.0022 0.0193  0.0075  298 ILE B CA  
5286 C C   . ILE B 296 ? 0.1736 0.1819 0.1752 -0.0014 0.0189  0.0072  298 ILE B C   
5287 O O   . ILE B 296 ? 0.1743 0.1861 0.1764 -0.0006 0.0181  0.0072  298 ILE B O   
5288 C CB  . ILE B 296 ? 0.1725 0.1814 0.1705 -0.0054 0.0194  0.0072  298 ILE B CB  
5289 C CG1 . ILE B 296 ? 0.1775 0.1843 0.1736 -0.0065 0.0200  0.0076  298 ILE B CG1 
5290 C CG2 . ILE B 296 ? 0.1801 0.1856 0.1746 -0.0079 0.0204  0.0066  298 ILE B CG2 
5291 C CD1 . ILE B 296 ? 0.1829 0.1926 0.1764 -0.0106 0.0199  0.0075  298 ILE B CD1 
5292 N N   . ALA B 297 ? 0.1791 0.1843 0.1805 -0.0010 0.0199  0.0072  299 ALA B N   
5293 C CA  . ALA B 297 ? 0.1858 0.1912 0.1878 -0.0004 0.0198  0.0069  299 ALA B CA  
5294 C C   . ALA B 297 ? 0.2046 0.2079 0.2040 -0.0017 0.0208  0.0065  299 ALA B C   
5295 O O   . ALA B 297 ? 0.1948 0.1941 0.1914 -0.0028 0.0220  0.0064  299 ALA B O   
5296 C CB  . ALA B 297 ? 0.1831 0.1880 0.1870 0.0007  0.0200  0.0075  299 ALA B CB  
5297 N N   . ARG B 298 ? 0.2319 0.2371 0.2312 -0.0016 0.0204  0.0062  300 ARG B N   
5298 C CA  . ARG B 298 ? 0.2746 0.2779 0.2715 -0.0026 0.0213  0.0058  300 ARG B CA  
5299 C C   . ARG B 298 ? 0.2590 0.2628 0.2570 -0.0008 0.0213  0.0060  300 ARG B C   
5300 O O   . ARG B 298 ? 0.2439 0.2495 0.2430 0.0006  0.0207  0.0063  300 ARG B O   
5301 C CB  . ARG B 298 ? 0.3299 0.3358 0.3239 -0.0058 0.0209  0.0052  300 ARG B CB  
5302 C CG  . ARG B 298 ? 0.4051 0.4189 0.4002 -0.0050 0.0197  0.0056  300 ARG B CG  
5303 C CD  . ARG B 298 ? 0.5046 0.5247 0.4976 -0.0087 0.0190  0.0055  300 ARG B CD  
5304 N NE  . ARG B 298 ? 0.6007 0.6307 0.5949 -0.0066 0.0181  0.0067  300 ARG B NE  
5305 C CZ  . ARG B 298 ? 0.6699 0.7042 0.6658 -0.0035 0.0176  0.0078  300 ARG B CZ  
5306 N NH1 . ARG B 298 ? 0.6611 0.6911 0.6583 -0.0028 0.0176  0.0077  300 ARG B NH1 
5307 N NH2 . ARG B 298 ? 0.6813 0.7244 0.6769 -0.0006 0.0173  0.0093  300 ARG B NH2 
5308 N N   . LEU B 299 ? 0.2543 0.2554 0.2508 -0.0010 0.0224  0.0058  301 LEU B N   
5309 C CA  . LEU B 299 ? 0.2427 0.2436 0.2395 0.0003  0.0228  0.0060  301 LEU B CA  
5310 C C   . LEU B 299 ? 0.2378 0.2403 0.2319 -0.0005 0.0227  0.0055  301 LEU B C   
5311 O O   . LEU B 299 ? 0.2343 0.2352 0.2255 -0.0028 0.0231  0.0048  301 LEU B O   
5312 C CB  . LEU B 299 ? 0.2425 0.2401 0.2399 0.0012  0.0241  0.0066  301 LEU B CB  
5313 C CG  . LEU B 299 ? 0.2420 0.2389 0.2391 0.0021  0.0249  0.0070  301 LEU B CG  
5314 C CD1 . LEU B 299 ? 0.2410 0.2389 0.2395 0.0025  0.0245  0.0074  301 LEU B CD1 
5315 C CD2 . LEU B 299 ? 0.2419 0.2370 0.2392 0.0031  0.0265  0.0078  301 LEU B CD2 
5316 N N   . THR B 300 ? 0.2358 0.2414 0.2298 0.0011  0.0223  0.0060  302 THR B N   
5317 C CA  . THR B 300 ? 0.2361 0.2450 0.2279 0.0012  0.0224  0.0059  302 THR B CA  
5318 C C   . THR B 300 ? 0.2317 0.2364 0.2231 0.0028  0.0236  0.0062  302 THR B C   
5319 O O   . THR B 300 ? 0.2317 0.2340 0.2238 0.0047  0.0240  0.0069  302 THR B O   
5320 C CB  . THR B 300 ? 0.2444 0.2598 0.2356 0.0035  0.0217  0.0069  302 THR B CB  
5321 O OG1 . THR B 300 ? 0.2449 0.2650 0.2367 0.0013  0.0207  0.0067  302 THR B OG1 
5322 C CG2 . THR B 300 ? 0.2463 0.2664 0.2352 0.0046  0.0219  0.0074  302 THR B CG2 
5323 N N   . TYR B 301 ? 0.2249 0.2282 0.2142 0.0015  0.0242  0.0056  303 TYR B N   
5324 C CA  . TYR B 301 ? 0.2217 0.2211 0.2107 0.0029  0.0255  0.0060  303 TYR B CA  
5325 C C   . TYR B 301 ? 0.2238 0.2248 0.2097 0.0027  0.0257  0.0056  303 TYR B C   
5326 O O   . TYR B 301 ? 0.2196 0.2231 0.2028 0.0000  0.0250  0.0048  303 TYR B O   
5327 C CB  . TYR B 301 ? 0.2206 0.2153 0.2100 0.0023  0.0266  0.0059  303 TYR B CB  
5328 C CG  . TYR B 301 ? 0.2246 0.2163 0.2100 0.0000  0.0270  0.0049  303 TYR B CG  
5329 C CD1 . TYR B 301 ? 0.2218 0.2131 0.2066 -0.0017 0.0264  0.0044  303 TYR B CD1 
5330 C CD2 . TYR B 301 ? 0.2302 0.2183 0.2110 -0.0006 0.0281  0.0043  303 TYR B CD2 
5331 C CE1 . TYR B 301 ? 0.2306 0.2171 0.2098 -0.0045 0.0271  0.0034  303 TYR B CE1 
5332 C CE2 . TYR B 301 ? 0.2427 0.2254 0.2174 -0.0034 0.0288  0.0031  303 TYR B CE2 
5333 C CZ  . TYR B 301 ? 0.2427 0.2241 0.2162 -0.0055 0.0284  0.0027  303 TYR B CZ  
5334 O OH  . TYR B 301 ? 0.2606 0.2348 0.2262 -0.0090 0.0295  0.0015  303 TYR B OH  
5335 N N   . SER B 302 ? 0.2265 0.2262 0.2121 0.0049  0.0267  0.0063  304 SER B N   
5336 C CA  . SER B 302 ? 0.2333 0.2336 0.2159 0.0052  0.0272  0.0062  304 SER B CA  
5337 C C   . SER B 302 ? 0.2401 0.2360 0.2199 0.0027  0.0279  0.0050  304 SER B C   
5338 O O   . SER B 302 ? 0.2374 0.2283 0.2182 0.0035  0.0291  0.0054  304 SER B O   
5339 C CB  . SER B 302 ? 0.2309 0.2287 0.2137 0.0080  0.0285  0.0073  304 SER B CB  
5340 O OG  . SER B 302 ? 0.2344 0.2353 0.2163 0.0105  0.0283  0.0082  304 SER B OG  
5341 N N   . ASN B 303 ? 0.2501 0.2478 0.2258 -0.0001 0.0272  0.0039  305 ASN B N   
5342 C CA  . ASN B 303 ? 0.2700 0.2605 0.2403 -0.0030 0.0283  0.0026  305 ASN B CA  
5343 C C   . ASN B 303 ? 0.2916 0.2796 0.2568 -0.0033 0.0292  0.0020  305 ASN B C   
5344 O O   . ASN B 303 ? 0.3010 0.2813 0.2593 -0.0059 0.0304  0.0007  305 ASN B O   
5345 C CB  . ASN B 303 ? 0.2685 0.2599 0.2355 -0.0079 0.0272  0.0013  305 ASN B CB  
5346 C CG  . ASN B 303 ? 0.2810 0.2824 0.2468 -0.0109 0.0253  0.0010  305 ASN B CG  
5347 O OD1 . ASN B 303 ? 0.2799 0.2886 0.2485 -0.0079 0.0247  0.0021  305 ASN B OD1 
5348 N ND2 . ASN B 303 ? 0.3095 0.3116 0.2705 -0.0168 0.0245  -0.0002 305 ASN B ND2 
5349 N N   . ASP B 304 ? 0.2985 0.2916 0.2654 -0.0009 0.0289  0.0029  306 ASP B N   
5350 C CA  . ASP B 304 ? 0.3115 0.3031 0.2735 -0.0012 0.0297  0.0023  306 ASP B CA  
5351 C C   . ASP B 304 ? 0.3107 0.3007 0.2752 0.0034  0.0312  0.0038  306 ASP B C   
5352 O O   . ASP B 304 ? 0.2967 0.2919 0.2638 0.0060  0.0308  0.0050  306 ASP B O   
5353 C CB  . ASP B 304 ? 0.3160 0.3165 0.2752 -0.0043 0.0278  0.0017  306 ASP B CB  
5354 C CG  . ASP B 304 ? 0.3335 0.3315 0.2863 -0.0058 0.0285  0.0008  306 ASP B CG  
5355 O OD1 . ASP B 304 ? 0.3165 0.3055 0.2671 -0.0038 0.0305  0.0007  306 ASP B OD1 
5356 O OD2 . ASP B 304 ? 0.3607 0.3667 0.3103 -0.0090 0.0270  0.0002  306 ASP B OD2 
5357 N N   . PRO B 305 ? 0.3214 0.3037 0.2841 0.0049  0.0333  0.0040  307 PRO B N   
5358 C CA  . PRO B 305 ? 0.3408 0.3224 0.3060 0.0087  0.0348  0.0056  307 PRO B CA  
5359 C C   . PRO B 305 ? 0.3521 0.3351 0.3141 0.0097  0.0352  0.0056  307 PRO B C   
5360 O O   . PRO B 305 ? 0.3653 0.3480 0.3292 0.0126  0.0365  0.0071  307 PRO B O   
5361 C CB  . PRO B 305 ? 0.3421 0.3170 0.3058 0.0101  0.0370  0.0061  307 PRO B CB  
5362 C CG  . PRO B 305 ? 0.3455 0.3144 0.3017 0.0072  0.0372  0.0042  307 PRO B CG  
5363 C CD  . PRO B 305 ? 0.3346 0.3085 0.2915 0.0033  0.0347  0.0029  307 PRO B CD  
5364 N N   . ASN B 306 ? 0.3696 0.3554 0.3270 0.0069  0.0339  0.0042  308 ASN B N   
5365 C CA  . ASN B 306 ? 0.4030 0.3908 0.3564 0.0074  0.0340  0.0041  308 ASN B CA  
5366 C C   . ASN B 306 ? 0.4711 0.4677 0.4274 0.0099  0.0330  0.0055  308 ASN B C   
5367 O O   . ASN B 306 ? 0.5159 0.5207 0.4717 0.0080  0.0311  0.0052  308 ASN B O   
5368 C CB  . ASN B 306 ? 0.3851 0.3720 0.3309 0.0023  0.0332  0.0019  308 ASN B CB  
5369 C CG  . ASN B 306 ? 0.3820 0.3568 0.3222 0.0010  0.0351  0.0007  308 ASN B CG  
5370 O OD1 . ASN B 306 ? 0.3539 0.3221 0.2916 0.0040  0.0373  0.0013  308 ASN B OD1 
5371 N ND2 . ASN B 306 ? 0.3615 0.3332 0.2996 -0.0026 0.0346  -0.0004 308 ASN B ND2 
5372 N N   . GLY B 307 ? 0.5455 0.5406 0.5039 0.0142  0.0346  0.0072  309 GLY B N   
5373 C CA  . GLY B 307 ? 0.6029 0.6035 0.5612 0.0178  0.0346  0.0089  309 GLY B CA  
5374 C C   . GLY B 307 ? 0.6752 0.6795 0.6365 0.0194  0.0339  0.0100  309 GLY B C   
5375 O O   . GLY B 307 ? 0.7308 0.7315 0.6953 0.0181  0.0338  0.0097  309 GLY B O   
5376 N N   . PHE B 308 ? 0.7728 0.7845 0.7323 0.0224  0.0335  0.0113  310 PHE B N   
5377 C CA  . PHE B 308 ? 0.8127 0.8268 0.7725 0.0264  0.0338  0.0131  310 PHE B CA  
5378 C C   . PHE B 308 ? 0.7859 0.8079 0.7477 0.0242  0.0316  0.0126  310 PHE B C   
5379 O O   . PHE B 308 ? 0.8363 0.8679 0.7966 0.0271  0.0310  0.0141  310 PHE B O   
5380 C CB  . PHE B 308 ? 0.9114 0.9304 0.8670 0.0320  0.0349  0.0153  310 PHE B CB  
5381 C CG  . PHE B 308 ? 0.9729 1.0032 0.9264 0.0308  0.0333  0.0150  310 PHE B CG  
5382 C CD1 . PHE B 308 ? 0.9959 1.0238 0.9475 0.0289  0.0336  0.0139  310 PHE B CD1 
5383 C CD2 . PHE B 308 ? 0.9954 1.0397 0.9485 0.0315  0.0316  0.0159  310 PHE B CD2 
5384 C CE1 . PHE B 308 ? 0.9892 1.0271 0.9379 0.0270  0.0321  0.0134  310 PHE B CE1 
5385 C CE2 . PHE B 308 ? 0.9896 1.0460 0.9406 0.0292  0.0299  0.0157  310 PHE B CE2 
5386 C CZ  . PHE B 308 ? 0.9770 1.0295 0.9254 0.0266  0.0301  0.0142  310 PHE B CZ  
5387 N N   . THR B 309 ? 0.7875 0.8064 0.7521 0.0196  0.0306  0.0108  311 THR B N   
5388 C CA  . THR B 309 ? 0.7798 0.8064 0.7456 0.0159  0.0284  0.0099  311 THR B CA  
5389 C C   . THR B 309 ? 0.7220 0.7458 0.6910 0.0166  0.0283  0.0102  311 THR B C   
5390 O O   . THR B 309 ? 0.7367 0.7513 0.7072 0.0176  0.0296  0.0103  311 THR B O   
5391 C CB  . THR B 309 ? 0.8328 0.8576 0.7971 0.0095  0.0274  0.0075  311 THR B CB  
5392 O OG1 . THR B 309 ? 0.8527 0.8832 0.8177 0.0053  0.0255  0.0066  311 THR B OG1 
5393 C CG2 . THR B 309 ? 0.8372 0.8496 0.8022 0.0086  0.0288  0.0065  311 THR B CG2 
5394 N N   . SER B 310 ? 0.6902 0.7229 0.6600 0.0156  0.0267  0.0105  312 SER B N   
5395 C CA  . SER B 310 ? 0.6635 0.6954 0.6357 0.0166  0.0264  0.0110  312 SER B CA  
5396 C C   . SER B 310 ? 0.5704 0.6096 0.5441 0.0115  0.0244  0.0099  312 SER B C   
5397 O O   . SER B 310 ? 0.5460 0.5918 0.5209 0.0132  0.0237  0.0111  312 SER B O   
5398 C CB  . SER B 310 ? 0.6820 0.7169 0.6521 0.0235  0.0276  0.0136  312 SER B CB  
5399 O OG  . SER B 310 ? 0.6785 0.7278 0.6472 0.0255  0.0267  0.0152  312 SER B OG  
5400 N N   . THR B 311 ? 0.4861 0.5232 0.4588 0.0055  0.0236  0.0078  313 THR B N   
5401 C CA  . THR B 311 ? 0.4211 0.4599 0.3939 -0.0002 0.0222  0.0064  313 THR B CA  
5402 C C   . THR B 311 ? 0.3742 0.4028 0.3499 0.0001  0.0230  0.0059  313 THR B C   
5403 O O   . THR B 311 ? 0.3649 0.3845 0.3416 0.0025  0.0244  0.0059  313 THR B O   
5404 C CB  . THR B 311 ? 0.4166 0.4542 0.3846 -0.0072 0.0216  0.0043  313 THR B CB  
5405 O OG1 . THR B 311 ? 0.4026 0.4273 0.3686 -0.0070 0.0233  0.0032  313 THR B OG1 
5406 C CG2 . THR B 311 ? 0.4204 0.4703 0.3854 -0.0092 0.0204  0.0047  313 THR B CG2 
5407 N N   . THR B 312 ? 0.3290 0.3604 0.3060 -0.0023 0.0219  0.0056  314 THR B N   
5408 C CA  . THR B 312 ? 0.2954 0.3186 0.2749 -0.0024 0.0224  0.0051  314 THR B CA  
5409 C C   . THR B 312 ? 0.2811 0.3032 0.2584 -0.0083 0.0218  0.0037  314 THR B C   
5410 O O   . THR B 312 ? 0.2841 0.3140 0.2588 -0.0124 0.0206  0.0033  314 THR B O   
5411 C CB  . THR B 312 ? 0.2740 0.2993 0.2568 0.0020  0.0224  0.0066  314 THR B CB  
5412 O OG1 . THR B 312 ? 0.2730 0.3099 0.2556 0.0018  0.0211  0.0076  314 THR B OG1 
5413 C CG2 . THR B 312 ? 0.2701 0.2925 0.2526 0.0072  0.0237  0.0079  314 THR B CG2 
5414 N N   . ALA B 313 ? 0.2601 0.2729 0.2377 -0.0087 0.0227  0.0030  315 ALA B N   
5415 C CA  . ALA B 313 ? 0.2699 0.2798 0.2453 -0.0130 0.0225  0.0021  315 ALA B CA  
5416 C C   . ALA B 313 ? 0.2706 0.2791 0.2507 -0.0102 0.0225  0.0029  315 ALA B C   
5417 O O   . ALA B 313 ? 0.2486 0.2563 0.2327 -0.0057 0.0228  0.0038  315 ALA B O   
5418 C CB  . ALA B 313 ? 0.2729 0.2716 0.2417 -0.0158 0.0242  0.0006  315 ALA B CB  
5419 N N   . GLU B 314 ? 0.2858 0.2935 0.2647 -0.0133 0.0222  0.0024  316 GLU B N   
5420 C CA  . GLU B 314 ? 0.2900 0.2953 0.2725 -0.0111 0.0223  0.0030  316 GLU B CA  
5421 C C   . GLU B 314 ? 0.2689 0.2634 0.2476 -0.0118 0.0241  0.0024  316 GLU B C   
5422 O O   . GLU B 314 ? 0.2640 0.2532 0.2359 -0.0158 0.0250  0.0013  316 GLU B O   
5423 C CB  . GLU B 314 ? 0.3321 0.3449 0.3159 -0.0130 0.0209  0.0033  316 GLU B CB  
5424 C CG  . GLU B 314 ? 0.3709 0.3951 0.3572 -0.0111 0.0196  0.0045  316 GLU B CG  
5425 C CD  . GLU B 314 ? 0.4308 0.4635 0.4183 -0.0123 0.0185  0.0053  316 GLU B CD  
5426 O OE1 . GLU B 314 ? 0.4764 0.5064 0.4622 -0.0164 0.0185  0.0046  316 GLU B OE1 
5427 O OE2 . GLU B 314 ? 0.5171 0.5591 0.5066 -0.0089 0.0178  0.0068  316 GLU B OE2 
5428 N N   . THR B 315 ? 0.2408 0.2323 0.2229 -0.0082 0.0248  0.0033  317 THR B N   
5429 C CA  . THR B 315 ? 0.2414 0.2245 0.2200 -0.0077 0.0267  0.0035  317 THR B CA  
5430 C C   . THR B 315 ? 0.2524 0.2345 0.2282 -0.0111 0.0264  0.0030  317 THR B C   
5431 O O   . THR B 315 ? 0.2523 0.2420 0.2314 -0.0126 0.0245  0.0030  317 THR B O   
5432 C CB  . THR B 315 ? 0.2223 0.2060 0.2058 -0.0032 0.0272  0.0049  317 THR B CB  
5433 O OG1 . THR B 315 ? 0.1989 0.1889 0.1874 -0.0033 0.0253  0.0052  317 THR B OG1 
5434 C CG2 . THR B 315 ? 0.2157 0.2008 0.2018 -0.0005 0.0276  0.0057  317 THR B CG2 
5435 N N   . PRO B 316 ? 0.2781 0.2502 0.2466 -0.0122 0.0286  0.0027  318 PRO B N   
5436 C CA  . PRO B 316 ? 0.2864 0.2560 0.2520 -0.0147 0.0288  0.0026  318 PRO B CA  
5437 C C   . PRO B 316 ? 0.2705 0.2467 0.2443 -0.0110 0.0275  0.0039  318 PRO B C   
5438 O O   . PRO B 316 ? 0.2579 0.2374 0.2370 -0.0070 0.0272  0.0048  318 PRO B O   
5439 C CB  . PRO B 316 ? 0.3039 0.2592 0.2596 -0.0139 0.0322  0.0027  318 PRO B CB  
5440 C CG  . PRO B 316 ? 0.3204 0.2704 0.2723 -0.0122 0.0337  0.0025  318 PRO B CG  
5441 C CD  . PRO B 316 ? 0.2965 0.2581 0.2584 -0.0099 0.0314  0.0029  318 PRO B CD  
5442 N N   . ASP B 317 ? 0.2919 0.2700 0.2658 -0.0130 0.0268  0.0039  319 ASP B N   
5443 C CA  . ASP B 317 ? 0.2829 0.2676 0.2639 -0.0101 0.0254  0.0049  319 ASP B CA  
5444 C C   . ASP B 317 ? 0.2771 0.2571 0.2583 -0.0054 0.0271  0.0062  319 ASP B C   
5445 O O   . ASP B 317 ? 0.2835 0.2546 0.2580 -0.0049 0.0295  0.0065  319 ASP B O   
5446 C CB  . ASP B 317 ? 0.3064 0.2938 0.2866 -0.0133 0.0246  0.0048  319 ASP B CB  
5447 C CG  . ASP B 317 ? 0.3318 0.3286 0.3138 -0.0168 0.0226  0.0044  319 ASP B CG  
5448 O OD1 . ASP B 317 ? 0.3520 0.3550 0.3381 -0.0147 0.0214  0.0045  319 ASP B OD1 
5449 O OD2 . ASP B 317 ? 0.3725 0.3710 0.3513 -0.0214 0.0225  0.0041  319 ASP B OD2 
5450 N N   . THR B 318 ? 0.2583 0.2445 0.2463 -0.0023 0.0259  0.0071  320 THR B N   
5451 C CA  . THR B 318 ? 0.2624 0.2481 0.2516 0.0016  0.0269  0.0087  320 THR B CA  
5452 C C   . THR B 318 ? 0.2551 0.2463 0.2484 0.0016  0.0251  0.0090  320 THR B C   
5453 O O   . THR B 318 ? 0.2431 0.2397 0.2403 0.0003  0.0231  0.0083  320 THR B O   
5454 C CB  . THR B 318 ? 0.2583 0.2471 0.2507 0.0045  0.0272  0.0097  320 THR B CB  
5455 O OG1 . THR B 318 ? 0.2596 0.2502 0.2530 0.0084  0.0283  0.0117  320 THR B OG1 
5456 C CG2 . THR B 318 ? 0.2493 0.2449 0.2474 0.0034  0.0249  0.0092  320 THR B CG2 
5457 N N   . LYS B 319 ? 0.2676 0.2566 0.2591 0.0035  0.0263  0.0101  321 LYS B N   
5458 C CA  . LYS B 319 ? 0.2722 0.2641 0.2655 0.0030  0.0251  0.0103  321 LYS B CA  
5459 C C   . LYS B 319 ? 0.2713 0.2664 0.2668 0.0069  0.0255  0.0120  321 LYS B C   
5460 O O   . LYS B 319 ? 0.2758 0.2669 0.2676 0.0102  0.0279  0.0135  321 LYS B O   
5461 C CB  . LYS B 319 ? 0.2943 0.2790 0.2809 0.0008  0.0267  0.0099  321 LYS B CB  
5462 C CG  . LYS B 319 ? 0.3124 0.2999 0.3002 -0.0003 0.0256  0.0100  321 LYS B CG  
5463 C CD  . LYS B 319 ? 0.3502 0.3297 0.3303 -0.0032 0.0276  0.0099  321 LYS B CD  
5464 C CE  . LYS B 319 ? 0.3566 0.3389 0.3381 -0.0029 0.0270  0.0106  321 LYS B CE  
5465 N NZ  . LYS B 319 ? 0.3733 0.3485 0.3474 -0.0065 0.0288  0.0105  321 LYS B NZ  
5466 N N   . ALA B 320 ? 0.2598 0.2618 0.2603 0.0068  0.0233  0.0120  322 ALA B N   
5467 C CA  . ALA B 320 ? 0.2556 0.2620 0.2579 0.0096  0.0232  0.0136  322 ALA B CA  
5468 C C   . ALA B 320 ? 0.2388 0.2454 0.2409 0.0086  0.0222  0.0132  322 ALA B C   
5469 O O   . ALA B 320 ? 0.2142 0.2195 0.2159 0.0058  0.0213  0.0118  322 ALA B O   
5470 C CB  . ALA B 320 ? 0.2567 0.2710 0.2637 0.0094  0.0215  0.0140  322 ALA B CB  
5471 N N   . ASN B 321 ? 0.2495 0.2583 0.2515 0.0113  0.0227  0.0148  323 ASN B N   
5472 C CA  . ASN B 321 ? 0.2427 0.2505 0.2435 0.0110  0.0224  0.0148  323 ASN B CA  
5473 C C   . ASN B 321 ? 0.2439 0.2588 0.2476 0.0132  0.0213  0.0160  323 ASN B C   
5474 O O   . ASN B 321 ? 0.2663 0.2852 0.2706 0.0162  0.0222  0.0179  323 ASN B O   
5475 C CB  . ASN B 321 ? 0.2510 0.2498 0.2453 0.0114  0.0252  0.0153  323 ASN B CB  
5476 C CG  . ASN B 321 ? 0.2572 0.2548 0.2504 0.0084  0.0245  0.0144  323 ASN B CG  
5477 O OD1 . ASN B 321 ? 0.2463 0.2499 0.2436 0.0076  0.0222  0.0138  323 ASN B OD1 
5478 N ND2 . ASN B 321 ? 0.2661 0.2557 0.2530 0.0064  0.0266  0.0143  323 ASN B ND2 
5479 N N   . VAL B 322 ? 0.2256 0.2425 0.2305 0.0118  0.0196  0.0152  324 VAL B N   
5480 C CA  . VAL B 322 ? 0.2285 0.2518 0.2352 0.0131  0.0183  0.0161  324 VAL B CA  
5481 C C   . VAL B 322 ? 0.2246 0.2451 0.2292 0.0137  0.0187  0.0163  324 VAL B C   
5482 O O   . VAL B 322 ? 0.2188 0.2371 0.2230 0.0113  0.0180  0.0149  324 VAL B O   
5483 C CB  . VAL B 322 ? 0.2269 0.2544 0.2360 0.0102  0.0157  0.0146  324 VAL B CB  
5484 C CG1 . VAL B 322 ? 0.2307 0.2643 0.2404 0.0105  0.0143  0.0153  324 VAL B CG1 
5485 C CG2 . VAL B 322 ? 0.2286 0.2580 0.2392 0.0087  0.0154  0.0144  324 VAL B CG2 
5486 N N   . TYR B 323 ? 0.2336 0.2545 0.2364 0.0171  0.0203  0.0183  325 TYR B N   
5487 C CA  . TYR B 323 ? 0.2319 0.2500 0.2321 0.0179  0.0210  0.0188  325 TYR B CA  
5488 C C   . TYR B 323 ? 0.2258 0.2514 0.2287 0.0184  0.0187  0.0190  325 TYR B C   
5489 O O   . TYR B 323 ? 0.2158 0.2484 0.2214 0.0184  0.0172  0.0191  325 TYR B O   
5490 C CB  . TYR B 323 ? 0.2462 0.2581 0.2409 0.0217  0.0244  0.0210  325 TYR B CB  
5491 C CG  . TYR B 323 ? 0.2630 0.2655 0.2530 0.0205  0.0268  0.0205  325 TYR B CG  
5492 C CD1 . TYR B 323 ? 0.2705 0.2729 0.2603 0.0223  0.0279  0.0211  325 TYR B CD1 
5493 C CD2 . TYR B 323 ? 0.2771 0.2715 0.2625 0.0169  0.0280  0.0195  325 TYR B CD2 
5494 C CE1 . TYR B 323 ? 0.2891 0.2819 0.2736 0.0210  0.0301  0.0205  325 TYR B CE1 
5495 C CE2 . TYR B 323 ? 0.2942 0.2797 0.2742 0.0146  0.0301  0.0188  325 TYR B CE2 
5496 C CZ  . TYR B 323 ? 0.3004 0.2843 0.2797 0.0168  0.0311  0.0192  325 TYR B CZ  
5497 O OH  . TYR B 323 ? 0.3192 0.2935 0.2922 0.0144  0.0332  0.0184  325 TYR B OH  
5498 N N   . THR B 324 ? 0.2434 0.2569 0.2135 0.0322  0.0000  0.0169  326 THR B N   
5499 C CA  . THR B 324 ? 0.2398 0.2571 0.2149 0.0333  0.0003  0.0160  326 THR B CA  
5500 C C   . THR B 324 ? 0.2434 0.2529 0.2127 0.0321  0.0007  0.0148  326 THR B C   
5501 O O   . THR B 324 ? 0.2363 0.2399 0.2002 0.0286  0.0004  0.0148  326 THR B O   
5502 C CB  . THR B 324 ? 0.2290 0.2536 0.2150 0.0306  -0.0004 0.0166  326 THR B CB  
5503 O OG1 . THR B 324 ? 0.2226 0.2507 0.2116 0.0314  0.0000  0.0157  326 THR B OG1 
5504 C CG2 . THR B 324 ? 0.2290 0.2524 0.2185 0.0272  -0.0010 0.0168  326 THR B CG2 
5505 N N   . TYR B 325 ? 0.2546 0.2647 0.2239 0.0343  0.0015  0.0138  327 TYR B N   
5506 C CA  . TYR B 325 ? 0.2699 0.2719 0.2320 0.0338  0.0021  0.0127  327 TYR B CA  
5507 C C   . TYR B 325 ? 0.2602 0.2674 0.2306 0.0316  0.0018  0.0118  327 TYR B C   
5508 O O   . TYR B 325 ? 0.2486 0.2636 0.2279 0.0316  0.0016  0.0120  327 TYR B O   
5509 C CB  . TYR B 325 ? 0.2862 0.2822 0.2375 0.0398  0.0037  0.0126  327 TYR B CB  
5510 C CG  . TYR B 325 ? 0.2961 0.2900 0.2409 0.0440  0.0045  0.0137  327 TYR B CG  
5511 C CD1 . TYR B 325 ? 0.3114 0.2958 0.2478 0.0417  0.0045  0.0138  327 TYR B CD1 
5512 C CD2 . TYR B 325 ? 0.2995 0.3026 0.2464 0.0500  0.0052  0.0150  327 TYR B CD2 
5513 C CE1 . TYR B 325 ? 0.3189 0.3009 0.2488 0.0457  0.0054  0.0147  327 TYR B CE1 
5514 C CE2 . TYR B 325 ? 0.3116 0.3143 0.2527 0.0545  0.0061  0.0162  327 TYR B CE2 
5515 C CZ  . TYR B 325 ? 0.3172 0.3086 0.2497 0.0527  0.0063  0.0159  327 TYR B CZ  
5516 O OH  . TYR B 325 ? 0.3318 0.3222 0.2580 0.0572  0.0074  0.0170  327 TYR B OH  
5517 N N   . GLN B 326 ? 0.2695 0.2712 0.2354 0.0295  0.0020  0.0109  328 GLN B N   
5518 C CA  . GLN B 326 ? 0.2635 0.2690 0.2353 0.0279  0.0021  0.0100  328 GLN B CA  
5519 C C   . GLN B 326 ? 0.2594 0.2594 0.2240 0.0299  0.0030  0.0090  328 GLN B C   
5520 O O   . GLN B 326 ? 0.2662 0.2560 0.2191 0.0299  0.0034  0.0089  328 GLN B O   
5521 C CB  . GLN B 326 ? 0.2726 0.2791 0.2462 0.0230  0.0014  0.0103  328 GLN B CB  
5522 C CG  . GLN B 326 ? 0.2826 0.2934 0.2617 0.0217  0.0017  0.0096  328 GLN B CG  
5523 C CD  . GLN B 326 ? 0.2870 0.3023 0.2678 0.0175  0.0011  0.0108  328 GLN B CD  
5524 O OE1 . GLN B 326 ? 0.3051 0.3209 0.2840 0.0153  0.0003  0.0122  328 GLN B OE1 
5525 N NE2 . GLN B 326 ? 0.3070 0.3268 0.2912 0.0164  0.0015  0.0105  328 GLN B NE2 
5526 N N   . LEU B 327 ? 0.2493 0.2548 0.2192 0.0314  0.0034  0.0083  329 LEU B N   
5527 C CA  . LEU B 327 ? 0.2533 0.2552 0.2178 0.0329  0.0041  0.0075  329 LEU B CA  
5528 C C   . LEU B 327 ? 0.2519 0.2546 0.2202 0.0285  0.0039  0.0064  329 LEU B C   
5529 O O   . LEU B 327 ? 0.2440 0.2537 0.2215 0.0271  0.0038  0.0060  329 LEU B O   
5530 C CB  . LEU B 327 ? 0.2477 0.2572 0.2152 0.0366  0.0046  0.0078  329 LEU B CB  
5531 C CG  . LEU B 327 ? 0.2575 0.2663 0.2218 0.0379  0.0053  0.0071  329 LEU B CG  
5532 C CD1 . LEU B 327 ? 0.2719 0.2705 0.2229 0.0424  0.0063  0.0080  329 LEU B CD1 
5533 C CD2 . LEU B 327 ? 0.2477 0.2680 0.2179 0.0390  0.0055  0.0074  329 LEU B CD2 
5534 N N   . LYS B 328 ? 0.2635 0.2585 0.2233 0.0263  0.0040  0.0061  330 LYS B N   
5535 C CA  . LYS B 328 ? 0.2683 0.2652 0.2304 0.0223  0.0038  0.0052  330 LYS B CA  
5536 C C   . LYS B 328 ? 0.2771 0.2710 0.2348 0.0243  0.0046  0.0043  330 LYS B C   
5537 O O   . LYS B 328 ? 0.3011 0.2847 0.2467 0.0254  0.0050  0.0046  330 LYS B O   
5538 C CB  . LYS B 328 ? 0.2760 0.2679 0.2309 0.0167  0.0032  0.0057  330 LYS B CB  
5539 C CG  . LYS B 328 ? 0.2714 0.2686 0.2293 0.0123  0.0030  0.0053  330 LYS B CG  
5540 C CD  . LYS B 328 ? 0.2840 0.2782 0.2335 0.0053  0.0022  0.0061  330 LYS B CD  
5541 C CE  . LYS B 328 ? 0.2745 0.2751 0.2276 0.0026  0.0013  0.0078  330 LYS B CE  
5542 N NZ  . LYS B 328 ? 0.2579 0.2736 0.2252 0.0041  0.0013  0.0087  330 LYS B NZ  
5543 N N   . VAL B 329 ? 0.2659 0.2671 0.2316 0.0247  0.0049  0.0034  331 VAL B N   
5544 C CA  . VAL B 329 ? 0.2679 0.2681 0.2305 0.0258  0.0055  0.0026  331 VAL B CA  
5545 C C   . VAL B 329 ? 0.2696 0.2705 0.2334 0.0212  0.0055  0.0017  331 VAL B C   
5546 O O   . VAL B 329 ? 0.2507 0.2586 0.2231 0.0196  0.0056  0.0012  331 VAL B O   
5547 C CB  . VAL B 329 ? 0.2641 0.2727 0.2336 0.0282  0.0060  0.0023  331 VAL B CB  
5548 C CG1 . VAL B 329 ? 0.2676 0.2770 0.2346 0.0288  0.0065  0.0017  331 VAL B CG1 
5549 C CG2 . VAL B 329 ? 0.2645 0.2757 0.2330 0.0323  0.0059  0.0037  331 VAL B CG2 
5550 N N   . ASN B 330 ? 0.2876 0.2809 0.2417 0.0196  0.0055  0.0016  332 ASN B N   
5551 C CA  . ASN B 330 ? 0.2924 0.2870 0.2460 0.0149  0.0054  0.0008  332 ASN B CA  
5552 C C   . ASN B 330 ? 0.3022 0.2976 0.2557 0.0167  0.0061  0.0000  332 ASN B C   
5553 O O   . ASN B 330 ? 0.3097 0.2980 0.2545 0.0200  0.0065  0.0005  332 ASN B O   
5554 C CB  . ASN B 330 ? 0.3145 0.2988 0.2550 0.0101  0.0050  0.0015  332 ASN B CB  
5555 C CG  . ASN B 330 ? 0.3190 0.3032 0.2580 0.0064  0.0041  0.0025  332 ASN B CG  
5556 O OD1 . ASN B 330 ? 0.3466 0.3187 0.2729 0.0051  0.0041  0.0031  332 ASN B OD1 
5557 N ND2 . ASN B 330 ? 0.3102 0.3068 0.2609 0.0050  0.0038  0.0028  332 ASN B ND2 
5558 N N   . LYS B 331 ? 0.3004 0.3042 0.2624 0.0153  0.0065  -0.0012 333 LYS B N   
5559 C CA  . LYS B 331 ? 0.2963 0.3021 0.2588 0.0160  0.0071  -0.0023 333 LYS B CA  
5560 C C   . LYS B 331 ? 0.3055 0.3089 0.2628 0.0117  0.0070  -0.0026 333 LYS B C   
5561 O O   . LYS B 331 ? 0.2980 0.3073 0.2599 0.0083  0.0070  -0.0030 333 LYS B O   
5562 C CB  . LYS B 331 ? 0.2891 0.3035 0.2617 0.0163  0.0080  -0.0037 333 LYS B CB  
5563 C CG  . LYS B 331 ? 0.3008 0.3173 0.2730 0.0167  0.0085  -0.0047 333 LYS B CG  
5564 C CD  . LYS B 331 ? 0.3110 0.3243 0.2762 0.0200  0.0082  -0.0033 333 LYS B CD  
5565 C CE  . LYS B 331 ? 0.3311 0.3500 0.2972 0.0204  0.0087  -0.0037 333 LYS B CE  
5566 N NZ  . LYS B 331 ? 0.3427 0.3580 0.3000 0.0238  0.0086  -0.0020 333 LYS B NZ  
5567 N N   . VAL B 332 ? 0.3341 0.3293 0.2812 0.0121  0.0070  -0.0021 334 VAL B N   
5568 C CA  . VAL B 332 ? 0.3662 0.3578 0.3063 0.0070  0.0068  -0.0023 334 VAL B CA  
5569 C C   . VAL B 332 ? 0.3925 0.3824 0.3292 0.0092  0.0073  -0.0026 334 VAL B C   
5570 O O   . VAL B 332 ? 0.3799 0.3723 0.3192 0.0146  0.0078  -0.0023 334 VAL B O   
5571 C CB  . VAL B 332 ? 0.3890 0.3679 0.3150 0.0034  0.0062  -0.0011 334 VAL B CB  
5572 C CG1 . VAL B 332 ? 0.3807 0.3637 0.3106 0.0003  0.0055  -0.0006 334 VAL B CG1 
5573 C CG2 . VAL B 332 ? 0.4068 0.3720 0.3206 0.0091  0.0068  0.0000  334 VAL B CG2 
5574 N N   . LYS B 333 ? 0.4338 0.4208 0.3644 0.0046  0.0072  -0.0029 335 LYS B N   
5575 C CA  . LYS B 333 ? 0.4757 0.4588 0.4000 0.0060  0.0076  -0.0028 335 LYS B CA  
5576 C C   . LYS B 333 ? 0.5378 0.5038 0.4437 0.0039  0.0075  -0.0013 335 LYS B C   
5577 O O   . LYS B 333 ? 0.5595 0.5174 0.4582 0.0011  0.0071  -0.0007 335 LYS B O   
5578 C CB  . LYS B 333 ? 0.4695 0.4634 0.4023 0.0024  0.0078  -0.0044 335 LYS B CB  
5579 C CG  . LYS B 333 ? 0.4569 0.4557 0.3916 -0.0044 0.0074  -0.0050 335 LYS B CG  
5580 C CD  . LYS B 333 ? 0.4452 0.4570 0.3909 -0.0052 0.0082  -0.0066 335 LYS B CD  
5581 C CE  . LYS B 333 ? 0.4720 0.4926 0.4221 -0.0094 0.0080  -0.0064 335 LYS B CE  
5582 N NZ  . LYS B 333 ? 0.4955 0.5274 0.4521 -0.0108 0.0091  -0.0075 335 LYS B NZ  
5583 N N   . GLU B 334 ? 0.5785 0.5378 0.4753 0.0052  0.0080  -0.0007 336 GLU B N   
5584 C CA  . GLU B 334 ? 0.6309 0.5694 0.5065 0.0063  0.0086  0.0010  336 GLU B CA  
5585 C C   . GLU B 334 ? 0.6133 0.5422 0.4778 -0.0039 0.0078  0.0007  336 GLU B C   
5586 O O   . GLU B 334 ? 0.6443 0.5538 0.4901 -0.0045 0.0084  0.0019  336 GLU B O   
5587 C CB  . GLU B 334 ? 0.6854 0.6200 0.5542 0.0112  0.0095  0.0022  336 GLU B CB  
5588 C CG  . GLU B 334 ? 0.7238 0.6692 0.6017 0.0209  0.0102  0.0032  336 GLU B CG  
5589 C CD  . GLU B 334 ? 0.7825 0.7272 0.6543 0.0274  0.0112  0.0052  336 GLU B CD  
5590 O OE1 . GLU B 334 ? 0.8647 0.7953 0.7215 0.0259  0.0117  0.0061  336 GLU B OE1 
5591 O OE2 . GLU B 334 ? 0.7931 0.7521 0.6746 0.0336  0.0115  0.0062  336 GLU B OE2 
5592 N N   . ASN B 335 ? 0.5881 0.5306 0.4629 -0.0116 0.0067  -0.0005 337 ASN B N   
5593 C CA  . ASN B 335 ? 0.6187 0.5567 0.4841 -0.0226 0.0057  -0.0003 337 ASN B CA  
5594 C C   . ASN B 335 ? 0.6464 0.5882 0.5161 -0.0244 0.0051  -0.0001 337 ASN B C   
5595 O O   . ASN B 335 ? 0.6850 0.6299 0.5510 -0.0341 0.0040  0.0002  337 ASN B O   
5596 C CB  . ASN B 335 ? 0.6048 0.5579 0.4781 -0.0298 0.0050  -0.0011 337 ASN B CB  
5597 C CG  . ASN B 335 ? 0.5686 0.5440 0.4643 -0.0266 0.0051  -0.0023 337 ASN B CG  
5598 O OD1 . ASN B 335 ? 0.5590 0.5391 0.4631 -0.0226 0.0052  -0.0023 337 ASN B OD1 
5599 N ND2 . ASN B 335 ? 0.5495 0.5374 0.4539 -0.0279 0.0054  -0.0033 337 ASN B ND2 
5600 N N   . GLN B 336 ? 0.6182 0.5624 0.4962 -0.0159 0.0057  -0.0001 338 GLN B N   
5601 C CA  . GLN B 336 ? 0.6139 0.5597 0.4947 -0.0166 0.0052  0.0002  338 GLN B CA  
5602 C C   . GLN B 336 ? 0.5658 0.5324 0.4632 -0.0207 0.0043  -0.0001 338 GLN B C   
5603 O O   . GLN B 336 ? 0.5506 0.5208 0.4514 -0.0215 0.0038  0.0004  338 GLN B O   
5604 C CB  . GLN B 336 ? 0.6636 0.5904 0.5230 -0.0234 0.0049  0.0011  338 GLN B CB  
5605 C CG  . GLN B 336 ? 0.7011 0.6040 0.5407 -0.0180 0.0065  0.0018  338 GLN B CG  
5606 C CD  . GLN B 336 ? 0.7021 0.6063 0.5488 -0.0054 0.0076  0.0022  338 GLN B CD  
5607 O OE1 . GLN B 336 ? 0.7262 0.6320 0.5766 -0.0034 0.0075  0.0024  338 GLN B OE1 
5608 N NE2 . GLN B 336 ? 0.6977 0.6031 0.5466 0.0026  0.0087  0.0026  338 GLN B NE2 
5609 N N   . GLN B 337 ? 0.5427 0.5229 0.4496 -0.0225 0.0043  -0.0008 339 GLN B N   
5610 C CA  . GLN B 337 ? 0.5063 0.5062 0.4287 -0.0235 0.0041  -0.0008 339 GLN B CA  
5611 C C   . GLN B 337 ? 0.4478 0.4541 0.3844 -0.0142 0.0052  -0.0018 339 GLN B C   
5612 O O   . GLN B 337 ? 0.4401 0.4397 0.3758 -0.0088 0.0058  -0.0027 339 GLN B O   
5613 C CB  . GLN B 337 ? 0.5373 0.5491 0.4616 -0.0299 0.0039  -0.0006 339 GLN B CB  
5614 C CG  . GLN B 337 ? 0.5407 0.5596 0.4743 -0.0251 0.0051  -0.0023 339 GLN B CG  
5615 C CD  . GLN B 337 ? 0.5848 0.6142 0.5183 -0.0313 0.0051  -0.0021 339 GLN B CD  
5616 O OE1 . GLN B 337 ? 0.5898 0.6244 0.5290 -0.0286 0.0061  -0.0034 339 GLN B OE1 
5617 N NE2 . GLN B 337 ? 0.5910 0.6245 0.5175 -0.0403 0.0038  -0.0003 339 GLN B NE2 
5618 N N   . ALA B 338 ? 0.4134 0.4321 0.3614 -0.0127 0.0054  -0.0015 340 ALA B N   
5619 C CA  . ALA B 338 ? 0.3832 0.4059 0.3423 -0.0053 0.0064  -0.0022 340 ALA B CA  
5620 C C   . ALA B 338 ? 0.3518 0.3761 0.3156 -0.0017 0.0077  -0.0041 340 ALA B C   
5621 O O   . ALA B 338 ? 0.3787 0.4073 0.3421 -0.0044 0.0080  -0.0047 340 ALA B O   
5622 C CB  . ALA B 338 ? 0.3819 0.4177 0.3504 -0.0048 0.0069  -0.0012 340 ALA B CB  
5623 N N   . LEU B 339 ? 0.3123 0.3344 0.2802 0.0034  0.0083  -0.0049 341 LEU B N   
5624 C CA  . LEU B 339 ? 0.2891 0.3145 0.2621 0.0058  0.0096  -0.0068 341 LEU B CA  
5625 C C   . LEU B 339 ? 0.2674 0.2966 0.2482 0.0092  0.0108  -0.0073 341 LEU B C   
5626 O O   . LEU B 339 ? 0.2739 0.3001 0.2554 0.0113  0.0104  -0.0068 341 LEU B O   
5627 C CB  . LEU B 339 ? 0.2882 0.3076 0.2562 0.0075  0.0093  -0.0069 341 LEU B CB  
5628 C CG  . LEU B 339 ? 0.2870 0.3105 0.2590 0.0086  0.0104  -0.0086 341 LEU B CG  
5629 C CD1 . LEU B 339 ? 0.2848 0.3125 0.2580 0.0058  0.0113  -0.0100 341 LEU B CD1 
5630 C CD2 . LEU B 339 ? 0.2945 0.3151 0.2613 0.0105  0.0099  -0.0079 341 LEU B CD2 
5631 N N   . ALA B 340 ? 0.2551 0.2898 0.2406 0.0100  0.0125  -0.0084 342 ALA B N   
5632 C CA  . ALA B 340 ? 0.2512 0.2862 0.2413 0.0135  0.0143  -0.0090 342 ALA B CA  
5633 C C   . ALA B 340 ? 0.2459 0.2765 0.2349 0.0137  0.0150  -0.0109 342 ALA B C   
5634 O O   . ALA B 340 ? 0.2371 0.2672 0.2234 0.0117  0.0144  -0.0116 342 ALA B O   
5635 C CB  . ALA B 340 ? 0.2599 0.3012 0.2529 0.0154  0.0164  -0.0091 342 ALA B CB  
5636 N N   . GLY B 341 ? 0.2527 0.2801 0.2429 0.0155  0.0162  -0.0115 343 GLY B N   
5637 C CA  . GLY B 341 ? 0.2636 0.2872 0.2512 0.0139  0.0173  -0.0135 343 GLY B CA  
5638 C C   . GLY B 341 ? 0.2679 0.2912 0.2544 0.0125  0.0156  -0.0127 343 GLY B C   
5639 O O   . GLY B 341 ? 0.2798 0.3022 0.2638 0.0099  0.0162  -0.0140 343 GLY B O   
5640 N N   . ALA B 342 ? 0.2673 0.2918 0.2547 0.0138  0.0137  -0.0107 344 ALA B N   
5641 C CA  . ALA B 342 ? 0.2656 0.2915 0.2521 0.0137  0.0124  -0.0095 344 ALA B CA  
5642 C C   . ALA B 342 ? 0.2744 0.2978 0.2624 0.0141  0.0128  -0.0092 344 ALA B C   
5643 O O   . ALA B 342 ? 0.2639 0.2845 0.2539 0.0160  0.0136  -0.0090 344 ALA B O   
5644 C CB  . ALA B 342 ? 0.2661 0.2924 0.2506 0.0158  0.0107  -0.0075 344 ALA B CB  
5645 N N   . GLY B 343 ? 0.2866 0.3121 0.2732 0.0122  0.0124  -0.0090 345 GLY B N   
5646 C CA  . GLY B 343 ? 0.2900 0.3138 0.2768 0.0118  0.0123  -0.0082 345 GLY B CA  
5647 C C   . GLY B 343 ? 0.2886 0.3192 0.2756 0.0125  0.0105  -0.0061 345 GLY B C   
5648 O O   . GLY B 343 ? 0.2872 0.3240 0.2727 0.0124  0.0099  -0.0055 345 GLY B O   
5649 N N   . PHE B 344 ? 0.2895 0.3195 0.2778 0.0140  0.0098  -0.0047 346 PHE B N   
5650 C CA  . PHE B 344 ? 0.2913 0.3283 0.2793 0.0157  0.0084  -0.0024 346 PHE B CA  
5651 C C   . PHE B 344 ? 0.3101 0.3485 0.2983 0.0131  0.0082  -0.0018 346 PHE B C   
5652 O O   . PHE B 344 ? 0.3336 0.3646 0.3225 0.0123  0.0089  -0.0025 346 PHE B O   
5653 C CB  . PHE B 344 ? 0.2893 0.3237 0.2772 0.0206  0.0077  -0.0010 346 PHE B CB  
5654 C CG  . PHE B 344 ? 0.2912 0.3240 0.2760 0.0226  0.0076  -0.0010 346 PHE B CG  
5655 C CD1 . PHE B 344 ? 0.2973 0.3254 0.2826 0.0213  0.0082  -0.0026 346 PHE B CD1 
5656 C CD2 . PHE B 344 ? 0.3005 0.3370 0.2811 0.0262  0.0073  0.0006  346 PHE B CD2 
5657 C CE1 . PHE B 344 ? 0.3119 0.3380 0.2932 0.0222  0.0081  -0.0025 346 PHE B CE1 
5658 C CE2 . PHE B 344 ? 0.3061 0.3389 0.2819 0.0282  0.0075  0.0008  346 PHE B CE2 
5659 C CZ  . PHE B 344 ? 0.3096 0.3370 0.2858 0.0255  0.0078  -0.0009 346 PHE B CZ  
5660 N N   . THR B 345 ? 0.3109 0.3595 0.2980 0.0119  0.0074  -0.0002 347 THR B N   
5661 C CA  . THR B 345 ? 0.3059 0.3588 0.2928 0.0092  0.0068  0.0010  347 THR B CA  
5662 C C   . THR B 345 ? 0.2927 0.3534 0.2806 0.0150  0.0058  0.0038  347 THR B C   
5663 O O   . THR B 345 ? 0.2886 0.3556 0.2752 0.0191  0.0057  0.0051  347 THR B O   
5664 C CB  . THR B 345 ? 0.3196 0.3790 0.3031 0.0015  0.0069  0.0006  347 THR B CB  
5665 O OG1 . THR B 345 ? 0.3271 0.3763 0.3076 -0.0025 0.0084  -0.0021 347 THR B OG1 
5666 C CG2 . THR B 345 ? 0.3367 0.3981 0.3185 -0.0029 0.0064  0.0017  347 THR B CG2 
5667 N N   . LEU B 346 ? 0.2880 0.3469 0.2771 0.0158  0.0053  0.0047  348 LEU B N   
5668 C CA  . LEU B 346 ? 0.2965 0.3617 0.2853 0.0213  0.0047  0.0073  348 LEU B CA  
5669 C C   . LEU B 346 ? 0.3108 0.3874 0.2999 0.0175  0.0040  0.0090  348 LEU B C   
5670 O O   . LEU B 346 ? 0.3169 0.3887 0.3061 0.0114  0.0039  0.0079  348 LEU B O   
5671 C CB  . LEU B 346 ? 0.2847 0.3394 0.2743 0.0247  0.0046  0.0071  348 LEU B CB  
5672 C CG  . LEU B 346 ? 0.2823 0.3401 0.2699 0.0304  0.0043  0.0093  348 LEU B CG  
5673 C CD1 . LEU B 346 ? 0.2819 0.3397 0.2642 0.0369  0.0049  0.0103  348 LEU B CD1 
5674 C CD2 . LEU B 346 ? 0.2830 0.3312 0.2713 0.0311  0.0040  0.0090  348 LEU B CD2 
5675 N N   . TYR B 347 ? 0.3288 0.4200 0.3168 0.0211  0.0037  0.0118  349 TYR B N   
5676 C CA  . TYR B 347 ? 0.3473 0.4542 0.3354 0.0179  0.0029  0.0142  349 TYR B CA  
5677 C C   . TYR B 347 ? 0.3559 0.4667 0.3437 0.0261  0.0030  0.0167  349 TYR B C   
5678 O O   . TYR B 347 ? 0.3440 0.4513 0.3293 0.0347  0.0038  0.0174  349 TYR B O   
5679 C CB  . TYR B 347 ? 0.3568 0.4822 0.3436 0.0153  0.0028  0.0161  349 TYR B CB  
5680 C CG  . TYR B 347 ? 0.3565 0.4785 0.3419 0.0064  0.0029  0.0137  349 TYR B CG  
5681 C CD1 . TYR B 347 ? 0.3528 0.4681 0.3379 0.0089  0.0036  0.0120  349 TYR B CD1 
5682 C CD2 . TYR B 347 ? 0.3629 0.4864 0.3458 -0.0047 0.0024  0.0128  349 TYR B CD2 
5683 C CE1 . TYR B 347 ? 0.3574 0.4682 0.3406 0.0011  0.0039  0.0095  349 TYR B CE1 
5684 C CE2 . TYR B 347 ? 0.3633 0.4807 0.3425 -0.0129 0.0029  0.0103  349 TYR B CE2 
5685 C CZ  . TYR B 347 ? 0.3651 0.4767 0.3450 -0.0096 0.0037  0.0087  349 TYR B CZ  
5686 O OH  . TYR B 347 ? 0.3765 0.4821 0.3520 -0.0176 0.0044  0.0062  349 TYR B OH  
5687 N N   . LYS B 348 ? 0.3888 0.5052 0.3777 0.0230  0.0023  0.0179  350 LYS B N   
5688 C CA  . LYS B 348 ? 0.4411 0.5648 0.4291 0.0304  0.0024  0.0206  350 LYS B CA  
5689 C C   . LYS B 348 ? 0.4747 0.6232 0.4627 0.0288  0.0020  0.0242  350 LYS B C   
5690 O O   . LYS B 348 ? 0.4669 0.6228 0.4557 0.0183  0.0010  0.0240  350 LYS B O   
5691 C CB  . LYS B 348 ? 0.4357 0.5488 0.4252 0.0287  0.0019  0.0198  350 LYS B CB  
5692 C CG  . LYS B 348 ? 0.4495 0.5661 0.4371 0.0370  0.0024  0.0220  350 LYS B CG  
5693 C CD  . LYS B 348 ? 0.4422 0.5505 0.4312 0.0352  0.0018  0.0215  350 LYS B CD  
5694 C CE  . LYS B 348 ? 0.4484 0.5593 0.4339 0.0438  0.0025  0.0236  350 LYS B CE  
5695 N NZ  . LYS B 348 ? 0.4489 0.5548 0.4362 0.0411  0.0018  0.0234  350 LYS B NZ  
5696 N N   . LYS B 349 ? 0.5325 0.6932 0.5184 0.0389  0.0029  0.0275  351 LYS B N   
5697 C CA  . LYS B 349 ? 0.5777 0.7656 0.5637 0.0393  0.0027  0.0319  351 LYS B CA  
5698 C C   . LYS B 349 ? 0.5758 0.7659 0.5636 0.0349  0.0017  0.0323  351 LYS B C   
5699 O O   . LYS B 349 ? 0.5126 0.6945 0.4990 0.0426  0.0025  0.0326  351 LYS B O   
5700 C CB  . LYS B 349 ? 0.6253 0.8231 0.6071 0.0538  0.0046  0.0355  351 LYS B CB  
5701 C CG  . LYS B 349 ? 0.6969 0.9272 0.6790 0.0560  0.0047  0.0407  351 LYS B CG  
5702 C CD  . LYS B 349 ? 0.7354 0.9734 0.7117 0.0732  0.0072  0.0448  351 LYS B CD  
5703 C CE  . LYS B 349 ? 0.7518 0.9833 0.7234 0.0815  0.0088  0.0451  351 LYS B CE  
5704 N NZ  . LYS B 349 ? 0.7576 1.0145 0.7320 0.0775  0.0081  0.0480  351 LYS B NZ  
5705 N N   . VAL B 350 ? 0.6182 0.8159 0.6075 0.0221  0.0001  0.0321  352 VAL B N   
5706 C CA  . VAL B 350 ? 0.6709 0.8754 0.6609 0.0163  -0.0008 0.0333  352 VAL B CA  
5707 C C   . VAL B 350 ? 0.7412 0.9782 0.7309 0.0130  -0.0015 0.0379  352 VAL B C   
5708 O O   . VAL B 350 ? 0.8086 1.0550 0.7969 0.0014  -0.0025 0.0380  352 VAL B O   
5709 C CB  . VAL B 350 ? 0.6654 0.8520 0.6548 0.0038  -0.0019 0.0299  352 VAL B CB  
5710 C CG1 . VAL B 350 ? 0.6866 0.8810 0.6753 -0.0034 -0.0031 0.0316  352 VAL B CG1 
5711 C CG2 . VAL B 350 ? 0.6501 0.8095 0.6406 0.0086  -0.0012 0.0264  352 VAL B CG2 
5712 N N   . ASN B 351 ? 0.7727 1.0264 0.7627 0.0230  -0.0006 0.0417  353 ASN B N   
5713 C CA  A ASN B 351 ? 0.7785 1.0681 0.7685 0.0227  -0.0009 0.0472  353 ASN B CA  
5714 C CA  B ASN B 351 ? 0.7592 1.0486 0.7492 0.0223  -0.0010 0.0471  353 ASN B CA  
5715 C C   . ASN B 351 ? 0.7873 1.0928 0.7767 0.0222  -0.0007 0.0490  353 ASN B C   
5716 O O   . ASN B 351 ? 0.7915 1.1151 0.7805 0.0090  -0.0023 0.0503  353 ASN B O   
5717 C CB  A ASN B 351 ? 0.7684 1.0702 0.7584 0.0084  -0.0029 0.0483  353 ASN B CB  
5718 C CB  B ASN B 351 ? 0.7276 1.0262 0.7176 0.0069  -0.0031 0.0476  353 ASN B CB  
5719 C CG  A ASN B 351 ? 0.7565 1.0449 0.7442 -0.0091 -0.0046 0.0448  353 ASN B CG  
5720 C CG  B ASN B 351 ? 0.6725 0.9476 0.6627 0.0050  -0.0035 0.0446  353 ASN B CG  
5721 O OD1 A ASN B 351 ? 0.7169 1.0181 0.7024 -0.0184 -0.0054 0.0455  353 ASN B OD1 
5722 O OD1 B ASN B 351 ? 0.6328 0.9002 0.6239 0.0166  -0.0023 0.0447  353 ASN B OD1 
5723 N ND2 A ASN B 351 ? 0.7317 0.9940 0.7185 -0.0137 -0.0050 0.0411  353 ASN B ND2 
5724 N ND2 B ASN B 351 ? 0.6514 0.9142 0.6396 -0.0095 -0.0050 0.0421  353 ASN B ND2 
5725 N N   . ASN B 352 ? 0.8126 1.1106 0.8008 0.0357  0.0011  0.0490  354 ASN B N   
5726 C CA  . ASN B 352 ? 0.8657 1.1769 0.8531 0.0382  0.0016  0.0509  354 ASN B CA  
5727 C C   . ASN B 352 ? 0.8834 1.1921 0.8714 0.0209  -0.0002 0.0480  354 ASN B C   
5728 O O   . ASN B 352 ? 0.9102 1.2449 0.8979 0.0146  -0.0010 0.0512  354 ASN B O   
5729 C CB  . ASN B 352 ? 0.8935 1.2436 0.8807 0.0450  0.0023  0.0579  354 ASN B CB  
5730 C CG  . ASN B 352 ? 0.8964 1.2465 0.8800 0.0659  0.0053  0.0609  354 ASN B CG  
5731 O OD1 . ASN B 352 ? 0.8745 1.2257 0.8547 0.0777  0.0073  0.0628  354 ASN B OD1 
5732 N ND2 . ASN B 352 ? 0.8651 1.2112 0.8480 0.0704  0.0059  0.0612  354 ASN B ND2 
5733 N N   . GLN B 353 ? 0.8838 1.1624 0.8716 0.0136  -0.0008 0.0425  355 GLN B N   
5734 C CA  . GLN B 353 ? 0.8582 1.1280 0.8443 -0.0018 -0.0020 0.0391  355 GLN B CA  
5735 C C   . GLN B 353 ? 0.7849 1.0194 0.7711 0.0003  -0.0012 0.0337  355 GLN B C   
5736 O O   . GLN B 353 ? 0.8104 1.0260 0.7963 -0.0040 -0.0016 0.0309  355 GLN B O   
5737 C CB  . GLN B 353 ? 0.8977 1.1778 0.8812 -0.0174 -0.0037 0.0399  355 GLN B CB  
5738 C CG  . GLN B 353 ? 0.9344 1.1994 0.9124 -0.0341 -0.0045 0.0360  355 GLN B CG  
5739 C CD  . GLN B 353 ? 0.9650 1.2442 0.9405 -0.0404 -0.0047 0.0369  355 GLN B CD  
5740 O OE1 . GLN B 353 ? 1.0051 1.3140 0.9788 -0.0479 -0.0058 0.0409  355 GLN B OE1 
5741 N NE2 . GLN B 353 ? 0.9508 1.2103 0.9260 -0.0382 -0.0038 0.0332  355 GLN B NE2 
5742 N N   . TYR B 354 ? 0.7007 0.9281 0.6871 0.0071  -0.0002 0.0326  356 TYR B N   
5743 C CA  . TYR B 354 ? 0.6328 0.8304 0.6193 0.0089  0.0004  0.0279  356 TYR B CA  
5744 C C   . TYR B 354 ? 0.6282 0.8098 0.6128 -0.0042 -0.0001 0.0241  356 TYR B C   
5745 O O   . TYR B 354 ? 0.6330 0.8197 0.6145 -0.0146 -0.0006 0.0235  356 TYR B O   
5746 C CB  . TYR B 354 ? 0.5921 0.7894 0.5778 0.0129  0.0012  0.0275  356 TYR B CB  
5747 C CG  . TYR B 354 ? 0.5815 0.7802 0.5665 0.0283  0.0026  0.0298  356 TYR B CG  
5748 C CD1 . TYR B 354 ? 0.5647 0.7466 0.5489 0.0367  0.0034  0.0288  356 TYR B CD1 
5749 C CD2 . TYR B 354 ? 0.5959 0.8119 0.5793 0.0345  0.0033  0.0331  356 TYR B CD2 
5750 C CE1 . TYR B 354 ? 0.5811 0.7605 0.5612 0.0503  0.0051  0.0307  356 TYR B CE1 
5751 C CE2 . TYR B 354 ? 0.6044 0.8186 0.5843 0.0495  0.0051  0.0354  356 TYR B CE2 
5752 C CZ  . TYR B 354 ? 0.6002 0.7946 0.5776 0.0572  0.0061  0.0341  356 TYR B CZ  
5753 O OH  . TYR B 354 ? 0.6112 0.7997 0.5818 0.0714  0.0082  0.0361  356 TYR B OH  
5754 N N   . THR B 355 ? 0.6158 0.7781 0.6012 -0.0034 0.0000  0.0219  357 THR B N   
5755 C CA  . THR B 355 ? 0.6030 0.7466 0.5854 -0.0133 -0.0001 0.0186  357 THR B CA  
5756 C C   . THR B 355 ? 0.5631 0.6832 0.5468 -0.0081 0.0010  0.0151  357 THR B C   
5757 O O   . THR B 355 ? 0.5486 0.6641 0.5357 0.0017  0.0013  0.0154  357 THR B O   
5758 C CB  . THR B 355 ? 0.6309 0.7748 0.6126 -0.0167 -0.0008 0.0197  357 THR B CB  
5759 O OG1 . THR B 355 ? 0.7144 0.8452 0.6897 -0.0287 -0.0007 0.0175  357 THR B OG1 
5760 C CG2 . THR B 355 ? 0.6307 0.7613 0.6162 -0.0078 -0.0005 0.0192  357 THR B CG2 
5761 N N   . GLU B 356 ? 0.5628 0.6690 0.5427 -0.0151 0.0017  0.0122  358 GLU B N   
5762 C CA  . GLU B 356 ? 0.5368 0.6228 0.5174 -0.0113 0.0029  0.0091  358 GLU B CA  
5763 C C   . GLU B 356 ? 0.5085 0.5810 0.4905 -0.0083 0.0031  0.0087  358 GLU B C   
5764 O O   . GLU B 356 ? 0.5282 0.5974 0.5066 -0.0144 0.0030  0.0090  358 GLU B O   
5765 C CB  . GLU B 356 ? 0.5558 0.6315 0.5299 -0.0198 0.0040  0.0064  358 GLU B CB  
5766 C CG  . GLU B 356 ? 0.5743 0.6311 0.5487 -0.0159 0.0057  0.0035  358 GLU B CG  
5767 C CD  . GLU B 356 ? 0.6017 0.6479 0.5683 -0.0231 0.0073  0.0007  358 GLU B CD  
5768 O OE1 . GLU B 356 ? 0.6793 0.7353 0.6437 -0.0278 0.0070  0.0007  358 GLU B OE1 
5769 O OE2 . GLU B 356 ? 0.6147 0.6426 0.5764 -0.0238 0.0090  -0.0010 358 GLU B OE2 
5770 N N   . ILE B 357 ? 0.4569 0.5221 0.4433 0.0000  0.0034  0.0082  359 ILE B N   
5771 C CA  . ILE B 357 ? 0.4355 0.4897 0.4236 0.0028  0.0035  0.0082  359 ILE B CA  
5772 C C   . ILE B 357 ? 0.4242 0.4635 0.4127 0.0052  0.0049  0.0061  359 ILE B C   
5773 O O   . ILE B 357 ? 0.4055 0.4350 0.3937 0.0056  0.0055  0.0060  359 ILE B O   
5774 C CB  . ILE B 357 ? 0.4139 0.4750 0.4055 0.0096  0.0026  0.0102  359 ILE B CB  
5775 C CG1 . ILE B 357 ? 0.4000 0.4615 0.3928 0.0165  0.0029  0.0100  359 ILE B CG1 
5776 C CG2 . ILE B 357 ? 0.4336 0.5106 0.4245 0.0078  0.0017  0.0127  359 ILE B CG2 
5777 C CD1 . ILE B 357 ? 0.3914 0.4561 0.3842 0.0231  0.0025  0.0118  359 ILE B CD1 
5778 N N   . LYS B 358 ? 0.4233 0.4621 0.4123 0.0068  0.0055  0.0047  360 LYS B N   
5779 C CA  . LYS B 358 ? 0.4258 0.4535 0.4154 0.0094  0.0068  0.0031  360 LYS B CA  
5780 C C   . LYS B 358 ? 0.4224 0.4507 0.4106 0.0082  0.0076  0.0013  360 LYS B C   
5781 O O   . LYS B 358 ? 0.4133 0.4503 0.4026 0.0097  0.0068  0.0018  360 LYS B O   
5782 C CB  . LYS B 358 ? 0.4203 0.4477 0.4142 0.0154  0.0062  0.0040  360 LYS B CB  
5783 C CG  . LYS B 358 ? 0.4329 0.4525 0.4280 0.0178  0.0074  0.0031  360 LYS B CG  
5784 C CD  . LYS B 358 ? 0.4577 0.4686 0.4506 0.0169  0.0089  0.0029  360 LYS B CD  
5785 C CE  . LYS B 358 ? 0.4963 0.5028 0.4907 0.0209  0.0103  0.0028  360 LYS B CE  
5786 N NZ  . LYS B 358 ? 0.5404 0.5401 0.5334 0.0228  0.0116  0.0041  360 LYS B NZ  
5787 N N   . LYS B 359 ? 0.4417 0.4601 0.4266 0.0063  0.0093  -0.0005 361 LYS B N   
5788 C CA  . LYS B 359 ? 0.4555 0.4729 0.4390 0.0055  0.0104  -0.0024 361 LYS B CA  
5789 C C   . LYS B 359 ? 0.4265 0.4353 0.4113 0.0100  0.0120  -0.0034 361 LYS B C   
5790 O O   . LYS B 359 ? 0.4075 0.4076 0.3903 0.0113  0.0133  -0.0032 361 LYS B O   
5791 C CB  . LYS B 359 ? 0.5147 0.5293 0.4908 -0.0020 0.0113  -0.0039 361 LYS B CB  
5792 C CG  . LYS B 359 ? 0.5725 0.5847 0.5459 -0.0037 0.0127  -0.0061 361 LYS B CG  
5793 C CD  . LYS B 359 ? 0.6408 0.6558 0.6071 -0.0126 0.0128  -0.0071 361 LYS B CD  
5794 C CE  . LYS B 359 ? 0.6969 0.7050 0.6549 -0.0198 0.0133  -0.0070 361 LYS B CE  
5795 N NZ  . LYS B 359 ? 0.7093 0.6973 0.6608 -0.0180 0.0159  -0.0084 361 LYS B NZ  
5796 N N   . PHE B 360 ? 0.3974 0.4095 0.3849 0.0124  0.0119  -0.0040 362 PHE B N   
5797 C CA  . PHE B 360 ? 0.3900 0.3971 0.3780 0.0154  0.0136  -0.0050 362 PHE B CA  
5798 C C   . PHE B 360 ? 0.3904 0.3952 0.3744 0.0124  0.0150  -0.0073 362 PHE B C   
5799 O O   . PHE B 360 ? 0.3508 0.3625 0.3355 0.0107  0.0139  -0.0076 362 PHE B O   
5800 C CB  . PHE B 360 ? 0.3725 0.3852 0.3653 0.0190  0.0123  -0.0038 362 PHE B CB  
5801 C CG  . PHE B 360 ? 0.3731 0.3873 0.3689 0.0214  0.0112  -0.0017 362 PHE B CG  
5802 C CD1 . PHE B 360 ? 0.3843 0.3959 0.3815 0.0241  0.0122  -0.0006 362 PHE B CD1 
5803 C CD2 . PHE B 360 ? 0.3699 0.3883 0.3662 0.0215  0.0092  -0.0004 362 PHE B CD2 
5804 C CE1 . PHE B 360 ? 0.3931 0.4072 0.3929 0.0258  0.0110  0.0014  362 PHE B CE1 
5805 C CE2 . PHE B 360 ? 0.3736 0.3925 0.3715 0.0231  0.0082  0.0013  362 PHE B CE2 
5806 C CZ  . PHE B 360 ? 0.3876 0.4049 0.3877 0.0247  0.0090  0.0022  362 PHE B CZ  
5807 N N   . GLU B 361 ? 0.4117 0.4065 0.3904 0.0123  0.0177  -0.0088 363 GLU B N   
5808 C CA  . GLU B 361 ? 0.4310 0.4216 0.4052 0.0105  0.0197  -0.0112 363 GLU B CA  
5809 C C   . GLU B 361 ? 0.3989 0.3955 0.3786 0.0149  0.0196  -0.0111 363 GLU B C   
5810 O O   . GLU B 361 ? 0.3858 0.3868 0.3709 0.0189  0.0187  -0.0092 363 GLU B O   
5811 C CB  . GLU B 361 ? 0.5014 0.4767 0.4659 0.0102  0.0230  -0.0126 363 GLU B CB  
5812 C CG  . GLU B 361 ? 0.5885 0.5564 0.5430 0.0030  0.0245  -0.0153 363 GLU B CG  
5813 C CD  . GLU B 361 ? 0.6359 0.6058 0.5857 -0.0058 0.0229  -0.0152 363 GLU B CD  
5814 O OE1 . GLU B 361 ? 0.6688 0.6359 0.6173 -0.0065 0.0223  -0.0138 363 GLU B OE1 
5815 O OE2 . GLU B 361 ? 0.6674 0.6432 0.6148 -0.0124 0.0221  -0.0164 363 GLU B OE2 
5816 N N   . ALA B 362 ? 0.4021 0.3988 0.3796 0.0131  0.0206  -0.0131 364 ALA B N   
5817 C CA  . ALA B 362 ? 0.3879 0.3910 0.3696 0.0155  0.0203  -0.0131 364 ALA B CA  
5818 C C   . ALA B 362 ? 0.3947 0.3949 0.3760 0.0204  0.0231  -0.0134 364 ALA B C   
5819 O O   . ALA B 362 ? 0.3963 0.3869 0.3714 0.0216  0.0260  -0.0146 364 ALA B O   
5820 C CB  . ALA B 362 ? 0.3925 0.3992 0.3726 0.0112  0.0196  -0.0146 364 ALA B CB  
5821 N N   . ASP B 363 ? 0.4033 0.4121 0.3900 0.0229  0.0222  -0.0121 365 ASP B N   
5822 C CA  A ASP B 363 ? 0.3902 0.4032 0.3786 0.0278  0.0242  -0.0112 365 ASP B CA  
5823 C CA  B ASP B 363 ? 0.3899 0.4030 0.3786 0.0279  0.0240  -0.0110 365 ASP B CA  
5824 C C   . ASP B 363 ? 0.3693 0.3942 0.3627 0.0269  0.0221  -0.0097 365 ASP B C   
5825 O O   . ASP B 363 ? 0.3849 0.4128 0.3786 0.0226  0.0198  -0.0101 365 ASP B O   
5826 C CB  A ASP B 363 ? 0.4043 0.4151 0.3928 0.0336  0.0259  -0.0092 365 ASP B CB  
5827 C CB  B ASP B 363 ? 0.4027 0.4144 0.3921 0.0332  0.0252  -0.0087 365 ASP B CB  
5828 C CG  A ASP B 363 ? 0.4169 0.4154 0.3976 0.0377  0.0301  -0.0104 365 ASP B CG  
5829 C CG  B ASP B 363 ? 0.3954 0.4106 0.3889 0.0321  0.0223  -0.0065 365 ASP B CG  
5830 O OD1 A ASP B 363 ? 0.3955 0.3942 0.3737 0.0416  0.0329  -0.0109 365 ASP B OD1 
5831 O OD1 B ASP B 363 ? 0.3672 0.3879 0.3639 0.0358  0.0224  -0.0039 365 ASP B OD1 
5832 O OD2 A ASP B 363 ? 0.3935 0.3813 0.3692 0.0371  0.0307  -0.0105 365 ASP B OD2 
5833 O OD2 B ASP B 363 ? 0.3622 0.3755 0.3553 0.0276  0.0201  -0.0073 365 ASP B OD2 
5834 N N   . SER B 364 ? 0.3327 0.3653 0.3294 0.0304  0.0225  -0.0073 366 SER B N   
5835 C CA  . SER B 364 ? 0.3126 0.3566 0.3122 0.0278  0.0206  -0.0057 366 SER B CA  
5836 C C   . SER B 364 ? 0.2918 0.3373 0.2923 0.0243  0.0174  -0.0040 366 SER B C   
5837 O O   . SER B 364 ? 0.2710 0.3210 0.2704 0.0201  0.0155  -0.0033 366 SER B O   
5838 C CB  . SER B 364 ? 0.3193 0.3749 0.3214 0.0316  0.0224  -0.0037 366 SER B CB  
5839 O OG  . SER B 364 ? 0.3234 0.3822 0.3275 0.0369  0.0235  -0.0010 366 SER B OG  
5840 N N   . ASN B 365 ? 0.2861 0.3263 0.2870 0.0258  0.0170  -0.0035 367 ASN B N   
5841 C CA  . ASN B 365 ? 0.2815 0.3218 0.2824 0.0233  0.0143  -0.0019 367 ASN B CA  
5842 C C   . ASN B 365 ? 0.2623 0.2976 0.2592 0.0193  0.0124  -0.0031 367 ASN B C   
5843 O O   . ASN B 365 ? 0.2618 0.2924 0.2573 0.0192  0.0130  -0.0051 367 ASN B O   
5844 C CB  . ASN B 365 ? 0.2905 0.3258 0.2925 0.0260  0.0146  -0.0012 367 ASN B CB  
5845 C CG  . ASN B 365 ? 0.3099 0.3491 0.3130 0.0248  0.0126  0.0011  367 ASN B CG  
5846 O OD1 . ASN B 365 ? 0.3418 0.3901 0.3469 0.0249  0.0125  0.0034  367 ASN B OD1 
5847 N ND2 . ASN B 365 ? 0.3013 0.3348 0.3024 0.0232  0.0110  0.0008  367 ASN B ND2 
5848 N N   . SER B 366 ? 0.2508 0.2871 0.2449 0.0161  0.0105  -0.0018 368 SER B N   
5849 C CA  . SER B 366 ? 0.2506 0.2801 0.2382 0.0136  0.0090  -0.0023 368 SER B CA  
5850 C C   . SER B 366 ? 0.2506 0.2753 0.2352 0.0137  0.0076  -0.0010 368 SER B C   
5851 O O   . SER B 366 ? 0.2528 0.2706 0.2309 0.0136  0.0069  -0.0011 368 SER B O   
5852 C CB  . SER B 366 ? 0.2562 0.2870 0.2391 0.0094  0.0084  -0.0022 368 SER B CB  
5853 O OG  . SER B 366 ? 0.2623 0.2956 0.2470 0.0098  0.0097  -0.0038 368 SER B OG  
5854 N N   . THR B 367 ? 0.2441 0.2721 0.2324 0.0147  0.0075  0.0003  369 THR B N   
5855 C CA  . THR B 367 ? 0.2464 0.2702 0.2321 0.0148  0.0063  0.0015  369 THR B CA  
5856 C C   . THR B 367 ? 0.2447 0.2687 0.2357 0.0186  0.0069  0.0014  369 THR B C   
5857 O O   . THR B 367 ? 0.2452 0.2735 0.2415 0.0203  0.0079  0.0019  369 THR B O   
5858 C CB  . THR B 367 ? 0.2520 0.2801 0.2363 0.0114  0.0054  0.0035  369 THR B CB  
5859 O OG1 . THR B 367 ? 0.2604 0.2864 0.2373 0.0064  0.0048  0.0033  369 THR B OG1 
5860 C CG2 . THR B 367 ? 0.2580 0.2816 0.2390 0.0111  0.0043  0.0046  369 THR B CG2 
5861 N N   . PHE B 368 ? 0.2430 0.2624 0.2314 0.0200  0.0065  0.0012  370 PHE B N   
5862 C CA  . PHE B 368 ? 0.2432 0.2633 0.2355 0.0222  0.0068  0.0013  370 PHE B CA  
5863 C C   . PHE B 368 ? 0.2480 0.2665 0.2385 0.0227  0.0056  0.0029  370 PHE B C   
5864 O O   . PHE B 368 ? 0.2435 0.2582 0.2281 0.0234  0.0050  0.0032  370 PHE B O   
5865 C CB  . PHE B 368 ? 0.2411 0.2610 0.2325 0.0227  0.0072  0.0001  370 PHE B CB  
5866 C CG  . PHE B 368 ? 0.2412 0.2619 0.2331 0.0216  0.0083  -0.0015 370 PHE B CG  
5867 C CD1 . PHE B 368 ? 0.2402 0.2600 0.2284 0.0207  0.0080  -0.0019 370 PHE B CD1 
5868 C CD2 . PHE B 368 ? 0.2403 0.2611 0.2349 0.0213  0.0098  -0.0027 370 PHE B CD2 
5869 C CE1 . PHE B 368 ? 0.2487 0.2700 0.2376 0.0195  0.0090  -0.0034 370 PHE B CE1 
5870 C CE2 . PHE B 368 ? 0.2444 0.2652 0.2386 0.0204  0.0110  -0.0043 370 PHE B CE2 
5871 C CZ  . PHE B 368 ? 0.2442 0.2664 0.2365 0.0195  0.0105  -0.0046 370 PHE B CZ  
5872 N N   . ASP B 369 ? 0.2606 0.2815 0.2552 0.0231  0.0056  0.0040  371 ASP B N   
5873 C CA  . ASP B 369 ? 0.2706 0.2908 0.2639 0.0230  0.0046  0.0057  371 ASP B CA  
5874 C C   . ASP B 369 ? 0.2641 0.2846 0.2602 0.0248  0.0047  0.0059  371 ASP B C   
5875 O O   . ASP B 369 ? 0.2790 0.3008 0.2792 0.0254  0.0054  0.0062  371 ASP B O   
5876 C CB  . ASP B 369 ? 0.2769 0.3015 0.2725 0.0216  0.0042  0.0074  371 ASP B CB  
5877 C CG  . ASP B 369 ? 0.2918 0.3170 0.2825 0.0177  0.0036  0.0077  371 ASP B CG  
5878 O OD1 . ASP B 369 ? 0.3018 0.3200 0.2841 0.0157  0.0028  0.0074  371 ASP B OD1 
5879 O OD2 . ASP B 369 ? 0.3140 0.3462 0.3079 0.0167  0.0040  0.0085  371 ASP B OD2 
5880 N N   . PHE B 370 ? 0.2519 0.2712 0.2446 0.0259  0.0042  0.0059  372 PHE B N   
5881 C CA  . PHE B 370 ? 0.2472 0.2688 0.2416 0.0267  0.0041  0.0065  372 PHE B CA  
5882 C C   . PHE B 370 ? 0.2537 0.2747 0.2475 0.0272  0.0032  0.0081  372 PHE B C   
5883 O O   . PHE B 370 ? 0.2551 0.2739 0.2435 0.0286  0.0028  0.0085  372 PHE B O   
5884 C CB  . PHE B 370 ? 0.2408 0.2650 0.2320 0.0281  0.0041  0.0062  372 PHE B CB  
5885 C CG  . PHE B 370 ? 0.2409 0.2667 0.2326 0.0269  0.0048  0.0048  372 PHE B CG  
5886 C CD1 . PHE B 370 ? 0.2393 0.2627 0.2280 0.0275  0.0051  0.0040  372 PHE B CD1 
5887 C CD2 . PHE B 370 ? 0.2338 0.2629 0.2277 0.0244  0.0053  0.0042  372 PHE B CD2 
5888 C CE1 . PHE B 370 ? 0.2430 0.2683 0.2320 0.0263  0.0058  0.0027  372 PHE B CE1 
5889 C CE2 . PHE B 370 ? 0.2394 0.2697 0.2328 0.0225  0.0060  0.0028  372 PHE B CE2 
5890 C CZ  . PHE B 370 ? 0.2405 0.2696 0.2321 0.0238  0.0062  0.0021  372 PHE B CZ  
5891 N N   . LYS B 371 ? 0.2553 0.2773 0.2534 0.0264  0.0032  0.0090  373 LYS B N   
5892 C CA  . LYS B 371 ? 0.2715 0.2940 0.2696 0.0264  0.0023  0.0107  373 LYS B CA  
5893 C C   . LYS B 371 ? 0.2564 0.2806 0.2549 0.0270  0.0020  0.0113  373 LYS B C   
5894 O O   . LYS B 371 ? 0.2486 0.2737 0.2494 0.0262  0.0025  0.0111  373 LYS B O   
5895 C CB  . LYS B 371 ? 0.2982 0.3227 0.3006 0.0260  0.0026  0.0120  373 LYS B CB  
5896 C CG  . LYS B 371 ? 0.3393 0.3658 0.3412 0.0249  0.0027  0.0121  373 LYS B CG  
5897 C CD  . LYS B 371 ? 0.3911 0.4235 0.3967 0.0250  0.0026  0.0146  373 LYS B CD  
5898 C CE  . LYS B 371 ? 0.4404 0.4787 0.4457 0.0230  0.0025  0.0154  373 LYS B CE  
5899 N NZ  . LYS B 371 ? 0.4914 0.5309 0.4988 0.0248  0.0040  0.0143  373 LYS B NZ  
5900 N N   . GLY B 372 ? 0.2588 0.2829 0.2540 0.0280  0.0013  0.0121  374 GLY B N   
5901 C CA  . GLY B 372 ? 0.2528 0.2802 0.2494 0.0282  0.0009  0.0133  374 GLY B CA  
5902 C C   . GLY B 372 ? 0.2544 0.2861 0.2484 0.0300  0.0011  0.0133  374 GLY B C   
5903 O O   . GLY B 372 ? 0.2365 0.2734 0.2330 0.0283  0.0009  0.0137  374 GLY B O   
5904 N N   . LEU B 373 ? 0.2707 0.3004 0.2589 0.0331  0.0015  0.0130  375 LEU B N   
5905 C CA  . LEU B 373 ? 0.2841 0.3193 0.2687 0.0369  0.0021  0.0136  375 LEU B CA  
5906 C C   . LEU B 373 ? 0.3000 0.3344 0.2791 0.0407  0.0023  0.0149  375 LEU B C   
5907 O O   . LEU B 373 ? 0.2969 0.3222 0.2715 0.0405  0.0023  0.0147  375 LEU B O   
5908 C CB  . LEU B 373 ? 0.2847 0.3166 0.2645 0.0394  0.0029  0.0127  375 LEU B CB  
5909 C CG  . LEU B 373 ? 0.2831 0.3144 0.2671 0.0358  0.0029  0.0112  375 LEU B CG  
5910 C CD1 . LEU B 373 ? 0.2921 0.3216 0.2709 0.0387  0.0037  0.0107  375 LEU B CD1 
5911 C CD2 . LEU B 373 ? 0.2813 0.3203 0.2714 0.0322  0.0026  0.0111  375 LEU B CD2 
5912 N N   . ASP B 374 ? 0.3226 0.3667 0.3012 0.0438  0.0026  0.0164  376 ASP B N   
5913 C CA  . ASP B 374 ? 0.3549 0.3995 0.3273 0.0491  0.0033  0.0179  376 ASP B CA  
5914 C C   . ASP B 374 ? 0.3703 0.4171 0.3348 0.0570  0.0051  0.0190  376 ASP B C   
5915 O O   . ASP B 374 ? 0.3660 0.4142 0.3307 0.0575  0.0055  0.0186  376 ASP B O   
5916 C CB  . ASP B 374 ? 0.3666 0.4223 0.3445 0.0470  0.0024  0.0194  376 ASP B CB  
5917 C CG  . ASP B 374 ? 0.3765 0.4479 0.3594 0.0449  0.0020  0.0206  376 ASP B CG  
5918 O OD1 . ASP B 374 ? 0.3820 0.4568 0.3649 0.0453  0.0024  0.0203  376 ASP B OD1 
5919 O OD2 . ASP B 374 ? 0.4087 0.4894 0.3951 0.0417  0.0012  0.0219  376 ASP B OD2 
5920 N N   . SER B 375 ? 0.3876 0.4354 0.3451 0.0636  0.0064  0.0207  377 SER B N   
5921 C CA  . SER B 375 ? 0.3999 0.4519 0.3488 0.0735  0.0086  0.0227  377 SER B CA  
5922 C C   . SER B 375 ? 0.4071 0.4813 0.3643 0.0730  0.0080  0.0246  377 SER B C   
5923 O O   . SER B 375 ? 0.4189 0.5055 0.3847 0.0671  0.0064  0.0251  377 SER B O   
5924 C CB  . SER B 375 ? 0.4113 0.4594 0.3505 0.0809  0.0104  0.0241  377 SER B CB  
5925 O OG  . SER B 375 ? 0.4113 0.4377 0.3411 0.0794  0.0109  0.0222  377 SER B OG  
5926 N N   . GLY B 376 ? 0.4076 0.4862 0.3613 0.0780  0.0092  0.0256  378 GLY B N   
5927 C CA  . GLY B 376 ? 0.4134 0.5140 0.3743 0.0763  0.0085  0.0275  378 GLY B CA  
5928 C C   . GLY B 376 ? 0.4178 0.5175 0.3756 0.0793  0.0094  0.0276  378 GLY B C   
5929 O O   . GLY B 376 ? 0.3953 0.4763 0.3446 0.0833  0.0106  0.0262  378 GLY B O   
5930 N N   . ASP B 377 ? 0.4570 0.5764 0.4207 0.0765  0.0086  0.0292  379 ASP B N   
5931 C CA  . ASP B 377 ? 0.4615 0.5849 0.4230 0.0794  0.0094  0.0299  379 ASP B CA  
5932 C C   . ASP B 377 ? 0.4405 0.5628 0.4100 0.0675  0.0074  0.0270  379 ASP B C   
5933 O O   . ASP B 377 ? 0.4334 0.5662 0.4098 0.0585  0.0058  0.0267  379 ASP B O   
5934 C CB  . ASP B 377 ? 0.5107 0.6601 0.4714 0.0863  0.0104  0.0347  379 ASP B CB  
5935 C CG  . ASP B 377 ? 0.5442 0.6941 0.4948 0.1008  0.0131  0.0380  379 ASP B CG  
5936 O OD1 . ASP B 377 ? 0.5494 0.6756 0.4899 0.1073  0.0149  0.0366  379 ASP B OD1 
5937 O OD2 . ASP B 377 ? 0.5992 0.7730 0.5512 0.1053  0.0136  0.0421  379 ASP B OD2 
5938 N N   . TYR B 378 ? 0.4213 0.5301 0.3880 0.0678  0.0078  0.0250  380 TYR B N   
5939 C CA  . TYR B 378 ? 0.4013 0.5035 0.3737 0.0580  0.0065  0.0216  380 TYR B CA  
5940 C C   . TYR B 378 ? 0.4074 0.5153 0.3783 0.0593  0.0070  0.0222  380 TYR B C   
5941 O O   . TYR B 378 ? 0.4133 0.5214 0.3770 0.0689  0.0086  0.0244  380 TYR B O   
5942 C CB  . TYR B 378 ? 0.3889 0.4689 0.3599 0.0561  0.0064  0.0185  380 TYR B CB  
5943 C CG  . TYR B 378 ? 0.3735 0.4491 0.3472 0.0532  0.0056  0.0179  380 TYR B CG  
5944 C CD1 . TYR B 378 ? 0.3706 0.4482 0.3515 0.0446  0.0043  0.0166  380 TYR B CD1 
5945 C CD2 . TYR B 378 ? 0.3815 0.4499 0.3491 0.0592  0.0065  0.0189  380 TYR B CD2 
5946 C CE1 . TYR B 378 ? 0.3523 0.4258 0.3355 0.0422  0.0036  0.0164  380 TYR B CE1 
5947 C CE2 . TYR B 378 ? 0.3647 0.4301 0.3349 0.0563  0.0057  0.0185  380 TYR B CE2 
5948 C CZ  . TYR B 378 ? 0.3556 0.4244 0.3342 0.0479  0.0042  0.0174  380 TYR B CZ  
5949 O OH  . TYR B 378 ? 0.3465 0.4122 0.3274 0.0454  0.0034  0.0174  380 TYR B OH  
5950 N N   . LYS B 379 ? 0.4123 0.5231 0.3887 0.0501  0.0059  0.0202  381 LYS B N   
5951 C CA  . LYS B 379 ? 0.4153 0.5281 0.3910 0.0491  0.0062  0.0197  381 LYS B CA  
5952 C C   . LYS B 379 ? 0.3778 0.4749 0.3562 0.0418  0.0057  0.0155  381 LYS B C   
5953 O O   . LYS B 379 ? 0.3524 0.4487 0.3351 0.0336  0.0049  0.0137  381 LYS B O   
5954 C CB  . LYS B 379 ? 0.4572 0.5928 0.4357 0.0444  0.0056  0.0218  381 LYS B CB  
5955 C CG  . LYS B 379 ? 0.4787 0.6205 0.4557 0.0450  0.0059  0.0224  381 LYS B CG  
5956 C CD  . LYS B 379 ? 0.5086 0.6762 0.4875 0.0400  0.0053  0.0252  381 LYS B CD  
5957 C CE  . LYS B 379 ? 0.5155 0.6861 0.4979 0.0259  0.0039  0.0230  381 LYS B CE  
5958 N NZ  . LYS B 379 ? 0.5299 0.7254 0.5123 0.0187  0.0031  0.0257  381 LYS B NZ  
5959 N N   . LEU B 380 ? 0.3603 0.4456 0.3350 0.0450  0.0064  0.0144  382 LEU B N   
5960 C CA  . LEU B 380 ? 0.3413 0.4148 0.3183 0.0390  0.0062  0.0109  382 LEU B CA  
5961 C C   . LEU B 380 ? 0.3491 0.4299 0.3267 0.0359  0.0063  0.0104  382 LEU B C   
5962 O O   . LEU B 380 ? 0.3611 0.4471 0.3345 0.0415  0.0069  0.0125  382 LEU B O   
5963 C CB  . LEU B 380 ? 0.3332 0.3905 0.3051 0.0432  0.0068  0.0101  382 LEU B CB  
5964 C CG  . LEU B 380 ? 0.3224 0.3691 0.2964 0.0380  0.0066  0.0070  382 LEU B CG  
5965 C CD1 . LEU B 380 ? 0.3062 0.3509 0.2865 0.0326  0.0061  0.0054  382 LEU B CD1 
5966 C CD2 . LEU B 380 ? 0.3269 0.3599 0.2937 0.0411  0.0070  0.0068  382 LEU B CD2 
5967 N N   . VAL B 381 ? 0.3375 0.4179 0.3189 0.0277  0.0060  0.0080  383 VAL B N   
5968 C CA  . VAL B 381 ? 0.3468 0.4339 0.3283 0.0229  0.0062  0.0072  383 VAL B CA  
5969 C C   . VAL B 381 ? 0.3441 0.4172 0.3263 0.0196  0.0068  0.0037  383 VAL B C   
5970 O O   . VAL B 381 ? 0.3342 0.3985 0.3184 0.0161  0.0070  0.0017  383 VAL B O   
5971 C CB  . VAL B 381 ? 0.3562 0.4553 0.3386 0.0149  0.0057  0.0075  383 VAL B CB  
5972 C CG1 . VAL B 381 ? 0.3677 0.4714 0.3488 0.0086  0.0059  0.0063  383 VAL B CG1 
5973 C CG2 . VAL B 381 ? 0.3744 0.4913 0.3566 0.0180  0.0051  0.0116  383 VAL B CG2 
5974 N N   . GLU B 382 ? 0.3520 0.4241 0.3324 0.0207  0.0072  0.0032  384 GLU B N   
5975 C CA  . GLU B 382 ? 0.3374 0.3983 0.3185 0.0177  0.0078  0.0000  384 GLU B CA  
5976 C C   . GLU B 382 ? 0.3255 0.3896 0.3070 0.0100  0.0083  -0.0018 384 GLU B C   
5977 O O   . GLU B 382 ? 0.3204 0.3898 0.3004 0.0077  0.0085  -0.0021 384 GLU B O   
5978 C CB  . GLU B 382 ? 0.3567 0.4139 0.3348 0.0217  0.0080  0.0003  384 GLU B CB  
5979 C CG  . GLU B 382 ? 0.3844 0.4328 0.3634 0.0186  0.0087  -0.0025 384 GLU B CG  
5980 C CD  . GLU B 382 ? 0.4101 0.4569 0.3858 0.0200  0.0089  -0.0025 384 GLU B CD  
5981 O OE1 . GLU B 382 ? 0.4896 0.5444 0.4633 0.0208  0.0088  -0.0012 384 GLU B OE1 
5982 O OE2 . GLU B 382 ? 0.4645 0.5031 0.4393 0.0200  0.0091  -0.0037 384 GLU B OE2 
5983 N N   . SER B 383 ? 0.3286 0.3881 0.3105 0.0059  0.0087  -0.0030 385 SER B N   
5984 C CA  . SER B 383 ? 0.3528 0.4124 0.3316 -0.0024 0.0094  -0.0046 385 SER B CA  
5985 C C   . SER B 383 ? 0.3736 0.4238 0.3501 -0.0049 0.0110  -0.0078 385 SER B C   
5986 O O   . SER B 383 ? 0.4024 0.4504 0.3739 -0.0121 0.0120  -0.0095 385 SER B O   
5987 C CB  . SER B 383 ? 0.3663 0.4199 0.3439 -0.0052 0.0096  -0.0049 385 SER B CB  
5988 O OG  . SER B 383 ? 0.3607 0.4035 0.3412 0.0000  0.0101  -0.0054 385 SER B OG  
5989 N N   . THR B 384 ? 0.3720 0.4163 0.3510 0.0000  0.0114  -0.0085 386 THR B N   
5990 C CA  . THR B 384 ? 0.3644 0.4027 0.3418 -0.0013 0.0130  -0.0111 386 THR B CA  
5991 C C   . THR B 384 ? 0.3538 0.3948 0.3335 0.0032  0.0123  -0.0103 386 THR B C   
5992 O O   . THR B 384 ? 0.3223 0.3612 0.3042 0.0079  0.0115  -0.0090 386 THR B O   
5993 C CB  . THR B 384 ? 0.3727 0.3982 0.3491 -0.0008 0.0150  -0.0132 386 THR B CB  
5994 O OG1 . THR B 384 ? 0.3844 0.4049 0.3569 -0.0044 0.0156  -0.0134 386 THR B OG1 
5995 C CG2 . THR B 384 ? 0.3733 0.3937 0.3466 -0.0024 0.0170  -0.0158 386 THR B CG2 
5996 N N   . VAL B 385 ? 0.3589 0.4038 0.3368 0.0010  0.0125  -0.0111 387 VAL B N   
5997 C CA  . VAL B 385 ? 0.3583 0.4053 0.3364 0.0045  0.0119  -0.0102 387 VAL B CA  
5998 C C   . VAL B 385 ? 0.3357 0.3756 0.3140 0.0037  0.0133  -0.0127 387 VAL B C   
5999 O O   . VAL B 385 ? 0.3411 0.3786 0.3176 -0.0001 0.0149  -0.0151 387 VAL B O   
6000 C CB  . VAL B 385 ? 0.3714 0.4294 0.3473 0.0036  0.0111  -0.0085 387 VAL B CB  
6001 C CG1 . VAL B 385 ? 0.3736 0.4316 0.3478 0.0080  0.0106  -0.0071 387 VAL B CG1 
6002 C CG2 . VAL B 385 ? 0.3746 0.4426 0.3506 0.0047  0.0100  -0.0056 387 VAL B CG2 
6003 N N   . PRO B 386 ? 0.3198 0.3562 0.2991 0.0070  0.0130  -0.0122 388 PRO B N   
6004 C CA  . PRO B 386 ? 0.3342 0.3676 0.3138 0.0062  0.0142  -0.0140 388 PRO B CA  
6005 C C   . PRO B 386 ? 0.3471 0.3843 0.3242 0.0035  0.0145  -0.0150 388 PRO B C   
6006 O O   . PRO B 386 ? 0.3502 0.3921 0.3254 0.0042  0.0132  -0.0132 388 PRO B O   
6007 C CB  . PRO B 386 ? 0.3185 0.3501 0.2981 0.0087  0.0132  -0.0125 388 PRO B CB  
6008 C CG  . PRO B 386 ? 0.3205 0.3510 0.3000 0.0112  0.0119  -0.0105 388 PRO B CG  
6009 C CD  . PRO B 386 ? 0.3165 0.3518 0.2954 0.0109  0.0116  -0.0098 388 PRO B CD  
6010 N N   . SER B 387 ? 0.3559 0.3910 0.3324 0.0010  0.0164  -0.0176 389 SER B N   
6011 C CA  . SER B 387 ? 0.3598 0.3979 0.3339 -0.0020 0.0169  -0.0189 389 SER B CA  
6012 C C   . SER B 387 ? 0.3565 0.3973 0.3302 -0.0004 0.0155  -0.0173 389 SER B C   
6013 O O   . SER B 387 ? 0.3558 0.3939 0.3305 0.0014  0.0153  -0.0169 389 SER B O   
6014 C CB  . SER B 387 ? 0.3816 0.4145 0.3546 -0.0030 0.0196  -0.0218 389 SER B CB  
6015 O OG  . SER B 387 ? 0.4227 0.4578 0.3927 -0.0066 0.0204  -0.0234 389 SER B OG  
6016 N N   . GLY B 388 ? 0.3670 0.4130 0.3382 -0.0014 0.0146  -0.0162 390 GLY B N   
6017 C CA  . GLY B 388 ? 0.3517 0.3980 0.3201 0.0000  0.0135  -0.0146 390 GLY B CA  
6018 C C   . GLY B 388 ? 0.3402 0.3853 0.3055 0.0045  0.0120  -0.0113 390 GLY B C   
6019 O O   . GLY B 388 ? 0.3379 0.3803 0.2979 0.0062  0.0114  -0.0096 390 GLY B O   
6020 N N   . TYR B 389 ? 0.3301 0.3760 0.2971 0.0066  0.0116  -0.0102 391 TYR B N   
6021 C CA  . TYR B 389 ? 0.3183 0.3617 0.2815 0.0119  0.0106  -0.0071 391 TYR B CA  
6022 C C   . TYR B 389 ? 0.3113 0.3646 0.2749 0.0138  0.0103  -0.0050 391 TYR B C   
6023 O O   . TYR B 389 ? 0.2979 0.3578 0.2656 0.0098  0.0106  -0.0063 391 TYR B O   
6024 C CB  . TYR B 389 ? 0.3260 0.3622 0.2908 0.0126  0.0105  -0.0075 391 TYR B CB  
6025 C CG  . TYR B 389 ? 0.3292 0.3587 0.2920 0.0106  0.0106  -0.0084 391 TYR B CG  
6026 C CD1 . TYR B 389 ? 0.3411 0.3632 0.2957 0.0120  0.0099  -0.0067 391 TYR B CD1 
6027 C CD2 . TYR B 389 ? 0.3335 0.3647 0.3012 0.0072  0.0115  -0.0109 391 TYR B CD2 
6028 C CE1 . TYR B 389 ? 0.3520 0.3691 0.3035 0.0084  0.0098  -0.0073 391 TYR B CE1 
6029 C CE2 . TYR B 389 ? 0.3480 0.3767 0.3142 0.0051  0.0115  -0.0112 391 TYR B CE2 
6030 C CZ  . TYR B 389 ? 0.3605 0.3829 0.3188 0.0048  0.0104  -0.0094 391 TYR B CZ  
6031 O OH  . TYR B 389 ? 0.3889 0.4099 0.3444 0.0009  0.0102  -0.0096 391 TYR B OH  
6032 N N   . ASN B 390 ? 0.3261 0.3800 0.2843 0.0200  0.0099  -0.0015 392 ASN B N   
6033 C CA  . ASN B 390 ? 0.3477 0.4133 0.3058 0.0238  0.0096  0.0015  392 ASN B CA  
6034 C C   . ASN B 390 ? 0.3584 0.4234 0.3202 0.0242  0.0094  0.0014  392 ASN B C   
6035 O O   . ASN B 390 ? 0.3645 0.4175 0.3252 0.0255  0.0094  0.0005  392 ASN B O   
6036 C CB  . ASN B 390 ? 0.3718 0.4368 0.3215 0.0322  0.0098  0.0055  392 ASN B CB  
6037 C CG  . ASN B 390 ? 0.4034 0.4715 0.3499 0.0315  0.0100  0.0061  392 ASN B CG  
6038 O OD1 . ASN B 390 ? 0.4352 0.4921 0.3737 0.0347  0.0104  0.0069  392 ASN B OD1 
6039 N ND2 . ASN B 390 ? 0.3812 0.4631 0.3331 0.0259  0.0098  0.0052  392 ASN B ND2 
6040 N N   . ALA B 391 ? 0.3712 0.4490 0.3364 0.0224  0.0091  0.0023  393 ALA B N   
6041 C CA  . ALA B 391 ? 0.3773 0.4573 0.3449 0.0235  0.0087  0.0032  393 ALA B CA  
6042 C C   . ALA B 391 ? 0.3997 0.4755 0.3617 0.0330  0.0089  0.0065  393 ALA B C   
6043 O O   . ALA B 391 ? 0.4281 0.5076 0.3844 0.0392  0.0093  0.0095  393 ALA B O   
6044 C CB  . ALA B 391 ? 0.3688 0.4657 0.3390 0.0193  0.0083  0.0045  393 ALA B CB  
6045 N N   . MET B 392 ? 0.3959 0.4616 0.3580 0.0343  0.0088  0.0057  394 MET B N   
6046 C CA  . MET B 392 ? 0.3917 0.4540 0.3483 0.0423  0.0091  0.0086  394 MET B CA  
6047 C C   . MET B 392 ? 0.3806 0.4614 0.3392 0.0453  0.0090  0.0119  394 MET B C   
6048 O O   . MET B 392 ? 0.3587 0.4504 0.3239 0.0384  0.0083  0.0109  394 MET B O   
6049 C CB  . MET B 392 ? 0.3863 0.4374 0.3449 0.0401  0.0088  0.0066  394 MET B CB  
6050 C CG  . MET B 392 ? 0.3961 0.4441 0.3502 0.0466  0.0091  0.0089  394 MET B CG  
6051 S SD  . MET B 392 ? 0.3748 0.4156 0.3341 0.0423  0.0084  0.0068  394 MET B SD  
6052 C CE  . MET B 392 ? 0.3472 0.4055 0.3137 0.0410  0.0079  0.0081  394 MET B CE  
6053 N N   . LYS B 393 ? 0.3977 0.4825 0.3495 0.0550  0.0099  0.0159  395 LYS B N   
6054 C CA  . LYS B 393 ? 0.4151 0.5190 0.3687 0.0591  0.0099  0.0197  395 LYS B CA  
6055 C C   . LYS B 393 ? 0.4121 0.5114 0.3685 0.0581  0.0095  0.0187  395 LYS B C   
6056 O O   . LYS B 393 ? 0.3890 0.4699 0.3407 0.0607  0.0100  0.0174  395 LYS B O   
6057 C CB  . LYS B 393 ? 0.4485 0.5567 0.3926 0.0722  0.0115  0.0247  395 LYS B CB  
6058 C CG  . LYS B 393 ? 0.4934 0.6062 0.4328 0.0758  0.0122  0.0268  395 LYS B CG  
6059 C CD  . LYS B 393 ? 0.5020 0.6409 0.4489 0.0702  0.0112  0.0284  395 LYS B CD  
6060 C CE  . LYS B 393 ? 0.5237 0.6659 0.4667 0.0721  0.0116  0.0299  395 LYS B CE  
6061 N NZ  . LYS B 393 ? 0.5263 0.6846 0.4775 0.0605  0.0101  0.0283  395 LYS B NZ  
6062 N N   . ASP B 394 ? 0.4060 0.5223 0.3686 0.0541  0.0087  0.0197  396 ASP B N   
6063 C CA  . ASP B 394 ? 0.4218 0.5379 0.3871 0.0533  0.0083  0.0196  396 ASP B CA  
6064 C C   . ASP B 394 ? 0.4280 0.5342 0.3853 0.0646  0.0096  0.0218  396 ASP B C   
6065 O O   . ASP B 394 ? 0.4427 0.5507 0.3922 0.0743  0.0111  0.0250  396 ASP B O   
6066 C CB  . ASP B 394 ? 0.4251 0.5644 0.3955 0.0482  0.0074  0.0217  396 ASP B CB  
6067 C CG  . ASP B 394 ? 0.4270 0.5692 0.4021 0.0352  0.0063  0.0186  396 ASP B CG  
6068 O OD1 . ASP B 394 ? 0.4259 0.5542 0.4010 0.0322  0.0065  0.0153  396 ASP B OD1 
6069 O OD2 . ASP B 394 ? 0.4442 0.6012 0.4220 0.0277  0.0054  0.0194  396 ASP B OD2 
6070 N N   . ILE B 395 ? 0.4207 0.5142 0.3784 0.0634  0.0094  0.0199  397 ILE B N   
6071 C CA  . ILE B 395 ? 0.4377 0.5196 0.3864 0.0727  0.0108  0.0215  397 ILE B CA  
6072 C C   . ILE B 395 ? 0.4359 0.5282 0.3885 0.0732  0.0104  0.0229  397 ILE B C   
6073 O O   . ILE B 395 ? 0.4493 0.5388 0.4088 0.0652  0.0091  0.0204  397 ILE B O   
6074 C CB  . ILE B 395 ? 0.4228 0.4800 0.3665 0.0706  0.0109  0.0183  397 ILE B CB  
6075 C CG1 . ILE B 395 ? 0.4129 0.4612 0.3519 0.0698  0.0112  0.0173  397 ILE B CG1 
6076 C CG2 . ILE B 395 ? 0.4292 0.4736 0.3620 0.0785  0.0123  0.0197  397 ILE B CG2 
6077 C CD1 . ILE B 395 ? 0.4003 0.4301 0.3376 0.0638  0.0107  0.0138  397 ILE B CD1 
6078 N N   . GLU B 396 ? 0.4603 0.5667 0.4090 0.0824  0.0116  0.0273  398 GLU B N   
6079 C CA  . GLU B 396 ? 0.4716 0.5873 0.4213 0.0856  0.0118  0.0293  398 GLU B CA  
6080 C C   . GLU B 396 ? 0.4681 0.5611 0.4069 0.0932  0.0135  0.0288  398 GLU B C   
6081 O O   . GLU B 396 ? 0.4749 0.5567 0.4018 0.1022  0.0155  0.0302  398 GLU B O   
6082 C CB  . GLU B 396 ? 0.5127 0.6555 0.4622 0.0930  0.0126  0.0347  398 GLU B CB  
6083 C CG  . GLU B 396 ? 0.5360 0.7038 0.4953 0.0832  0.0107  0.0355  398 GLU B CG  
6084 C CD  . GLU B 396 ? 0.5835 0.7827 0.5428 0.0892  0.0114  0.0415  398 GLU B CD  
6085 O OE1 . GLU B 396 ? 0.6279 0.8326 0.5824 0.0966  0.0126  0.0442  398 GLU B OE1 
6086 O OE2 . GLU B 396 ? 0.6086 0.8288 0.5726 0.0858  0.0105  0.0437  398 GLU B OE2 
6087 N N   . PHE B 397 ? 0.4429 0.5272 0.3841 0.0889  0.0127  0.0267  399 PHE B N   
6088 C CA  . PHE B 397 ? 0.4456 0.5076 0.3755 0.0940  0.0141  0.0260  399 PHE B CA  
6089 C C   . PHE B 397 ? 0.4428 0.5093 0.3759 0.0935  0.0137  0.0264  399 PHE B C   
6090 O O   . PHE B 397 ? 0.4243 0.5075 0.3692 0.0867  0.0119  0.0264  399 PHE B O   
6091 C CB  . PHE B 397 ? 0.4419 0.4819 0.3696 0.0868  0.0133  0.0220  399 PHE B CB  
6092 C CG  . PHE B 397 ? 0.4189 0.4599 0.3591 0.0748  0.0109  0.0188  399 PHE B CG  
6093 C CD1 . PHE B 397 ? 0.3982 0.4520 0.3497 0.0677  0.0094  0.0178  399 PHE B CD1 
6094 C CD2 . PHE B 397 ? 0.4095 0.4378 0.3487 0.0710  0.0103  0.0170  399 PHE B CD2 
6095 C CE1 . PHE B 397 ? 0.3746 0.4266 0.3349 0.0583  0.0078  0.0151  399 PHE B CE1 
6096 C CE2 . PHE B 397 ? 0.3919 0.4217 0.3418 0.0617  0.0084  0.0147  399 PHE B CE2 
6097 C CZ  . PHE B 397 ? 0.3719 0.4127 0.3319 0.0560  0.0074  0.0138  399 PHE B CZ  
6098 N N   . THR B 398 ? 0.4726 0.5233 0.3937 0.1002  0.0155  0.0267  400 THR B N   
6099 C CA  . THR B 398 ? 0.4768 0.5297 0.3986 0.1012  0.0155  0.0273  400 THR B CA  
6100 C C   . THR B 398 ? 0.4725 0.5017 0.3884 0.0964  0.0153  0.0242  400 THR B C   
6101 O O   . THR B 398 ? 0.4876 0.4956 0.3889 0.1000  0.0170  0.0235  400 THR B O   
6102 C CB  . THR B 398 ? 0.5144 0.5749 0.4264 0.1152  0.0184  0.0315  400 THR B CB  
6103 O OG1 . THR B 398 ? 0.5231 0.6126 0.4443 0.1167  0.0179  0.0347  400 THR B OG1 
6104 C CG2 . THR B 398 ? 0.5121 0.5696 0.4210 0.1173  0.0190  0.0318  400 THR B CG2 
6105 N N   . ILE B 399 ? 0.4535 0.4866 0.3793 0.0884  0.0132  0.0227  401 ILE B N   
6106 C CA  . ILE B 399 ? 0.4336 0.4493 0.3556 0.0834  0.0127  0.0205  401 ILE B CA  
6107 C C   . ILE B 399 ? 0.4407 0.4575 0.3573 0.0891  0.0139  0.0221  401 ILE B C   
6108 O O   . ILE B 399 ? 0.3958 0.4316 0.3214 0.0899  0.0132  0.0239  401 ILE B O   
6109 C CB  . ILE B 399 ? 0.4190 0.4384 0.3549 0.0718  0.0099  0.0182  401 ILE B CB  
6110 C CG1 . ILE B 399 ? 0.4201 0.4379 0.3607 0.0664  0.0090  0.0164  401 ILE B CG1 
6111 C CG2 . ILE B 399 ? 0.4205 0.4268 0.3528 0.0675  0.0094  0.0169  401 ILE B CG2 
6112 C CD1 . ILE B 399 ? 0.4066 0.4294 0.3602 0.0570  0.0068  0.0147  401 ILE B CD1 
6113 N N   . SER B 400 ? 0.4645 0.4607 0.3655 0.0924  0.0157  0.0215  402 SER B N   
6114 C CA  . SER B 400 ? 0.4904 0.4833 0.3829 0.0986  0.0174  0.0228  402 SER B CA  
6115 C C   . SER B 400 ? 0.4956 0.4685 0.3806 0.0915  0.0169  0.0204  402 SER B C   
6116 O O   . SER B 400 ? 0.5238 0.4746 0.3929 0.0913  0.0184  0.0191  402 SER B O   
6117 C CB  . SER B 400 ? 0.5252 0.5138 0.4019 0.1128  0.0212  0.0255  402 SER B CB  
6118 O OG  . SER B 400 ? 0.5672 0.5549 0.4361 0.1198  0.0232  0.0270  402 SER B OG  
6119 N N   . GLY B 401 ? 0.4739 0.4550 0.3698 0.0850  0.0148  0.0199  403 GLY B N   
6120 C CA  . GLY B 401 ? 0.4884 0.4547 0.3774 0.0791  0.0144  0.0184  403 GLY B CA  
6121 C C   . GLY B 401 ? 0.5137 0.4740 0.3897 0.0872  0.0170  0.0197  403 GLY B C   
6122 O O   . GLY B 401 ? 0.5112 0.4889 0.3948 0.0925  0.0172  0.0217  403 GLY B O   
6123 N N   . THR B 402 ? 0.5554 0.4916 0.4112 0.0880  0.0191  0.0186  404 THR B N   
6124 C CA  . THR B 402 ? 0.5715 0.4979 0.4124 0.0947  0.0218  0.0193  404 THR B CA  
6125 C C   . THR B 402 ? 0.5734 0.5018 0.4210 0.0847  0.0194  0.0182  404 THR B C   
6126 O O   . THR B 402 ? 0.5623 0.4777 0.4052 0.0744  0.0181  0.0163  404 THR B O   
6127 C CB  . THR B 402 ? 0.6105 0.5066 0.4229 0.0999  0.0256  0.0186  404 THR B CB  
6128 O OG1 . THR B 402 ? 0.6218 0.5186 0.4301 0.1095  0.0277  0.0200  404 THR B OG1 
6129 C CG2 . THR B 402 ? 0.6421 0.5247 0.4358 0.1079  0.0292  0.0192  404 THR B CG2 
6130 N N   . ILE B 403 ? 0.5723 0.5170 0.4295 0.0877  0.0190  0.0198  405 ILE B N   
6131 C CA  . ILE B 403 ? 0.5779 0.5263 0.4420 0.0794  0.0168  0.0193  405 ILE B CA  
6132 C C   . ILE B 403 ? 0.6130 0.5562 0.4642 0.0872  0.0196  0.0202  405 ILE B C   
6133 O O   . ILE B 403 ? 0.5863 0.5473 0.4449 0.0947  0.0202  0.0224  405 ILE B O   
6134 C CB  . ILE B 403 ? 0.5406 0.5141 0.4297 0.0738  0.0132  0.0202  405 ILE B CB  
6135 C CG1 . ILE B 403 ? 0.5212 0.4990 0.4213 0.0678  0.0111  0.0193  405 ILE B CG1 
6136 C CG2 . ILE B 403 ? 0.5291 0.5058 0.4241 0.0663  0.0112  0.0201  405 ILE B CG2 
6137 C CD1 . ILE B 403 ? 0.4906 0.4899 0.4113 0.0641  0.0085  0.0202  405 ILE B CD1 
6138 N N   . ASP B 404 ? 0.6763 0.5963 0.5080 0.0848  0.0213  0.0187  406 ASP B N   
6139 C CA  . ASP B 404 ? 0.7316 0.6416 0.5468 0.0925  0.0246  0.0192  406 ASP B CA  
6140 C C   . ASP B 404 ? 0.7246 0.6523 0.5546 0.0879  0.0222  0.0200  406 ASP B C   
6141 O O   . ASP B 404 ? 0.6557 0.6021 0.5075 0.0796  0.0182  0.0204  406 ASP B O   
6142 C CB  . ASP B 404 ? 0.7856 0.6617 0.5721 0.0904  0.0274  0.0170  406 ASP B CB  
6143 C CG  . ASP B 404 ? 0.8016 0.6680 0.5858 0.0746  0.0248  0.0150  406 ASP B CG  
6144 O OD1 . ASP B 404 ? 0.7622 0.6480 0.5671 0.0662  0.0210  0.0154  406 ASP B OD1 
6145 O OD2 . ASP B 404 ? 0.8722 0.7112 0.6325 0.0706  0.0268  0.0132  406 ASP B OD2 
6146 N N   . SER B 405 ? 0.7770 0.6991 0.5947 0.0943  0.0249  0.0206  407 SER B N   
6147 C CA  . SER B 405 ? 0.7682 0.7081 0.5985 0.0921  0.0232  0.0218  407 SER B CA  
6148 C C   . SER B 405 ? 0.7488 0.6850 0.5844 0.0772  0.0197  0.0203  407 SER B C   
6149 O O   . SER B 405 ? 0.6948 0.6511 0.5496 0.0722  0.0166  0.0215  407 SER B O   
6150 C CB  . SER B 405 ? 0.8197 0.7538 0.6339 0.1035  0.0273  0.0228  407 SER B CB  
6151 O OG  . SER B 405 ? 0.8908 0.7929 0.6777 0.1036  0.0306  0.0206  407 SER B OG  
6152 N N   . THR B 406 ? 0.7639 0.6762 0.5826 0.0703  0.0204  0.0181  408 THR B N   
6153 C CA  . THR B 406 ? 0.7661 0.6763 0.5894 0.0551  0.0169  0.0170  408 THR B CA  
6154 C C   . THR B 406 ? 0.7242 0.6569 0.5740 0.0493  0.0128  0.0181  408 THR B C   
6155 O O   . THR B 406 ? 0.7149 0.6584 0.5769 0.0408  0.0097  0.0188  408 THR B O   
6156 C CB  . THR B 406 ? 0.8078 0.6930 0.6111 0.0479  0.0179  0.0149  408 THR B CB  
6157 O OG1 . THR B 406 ? 0.8503 0.7099 0.6253 0.0553  0.0226  0.0137  408 THR B OG1 
6158 C CG2 . THR B 406 ? 0.8021 0.6865 0.6065 0.0326  0.0149  0.0144  408 THR B CG2 
6159 N N   . GLY B 407 ? 0.7058 0.6439 0.5624 0.0540  0.0129  0.0183  409 GLY B N   
6160 C CA  . GLY B 407 ? 0.6448 0.5995 0.5224 0.0491  0.0097  0.0189  409 GLY B CA  
6161 C C   . GLY B 407 ? 0.6159 0.5598 0.4891 0.0421  0.0089  0.0174  409 GLY B C   
6162 O O   . GLY B 407 ? 0.5644 0.5207 0.4537 0.0365  0.0062  0.0179  409 GLY B O   
6163 N N   . ASP B 408 ? 0.6412 0.5624 0.4921 0.0421  0.0114  0.0159  410 ASP B N   
6164 C CA  . ASP B 408 ? 0.6681 0.5775 0.5114 0.0360  0.0111  0.0145  410 ASP B CA  
6165 C C   . ASP B 408 ? 0.6245 0.5383 0.4735 0.0438  0.0119  0.0146  410 ASP B C   
6166 O O   . ASP B 408 ? 0.6338 0.5449 0.4760 0.0553  0.0147  0.0152  410 ASP B O   
6167 C CB  . ASP B 408 ? 0.7397 0.6208 0.5541 0.0332  0.0137  0.0129  410 ASP B CB  
6168 C CG  . ASP B 408 ? 0.8444 0.7199 0.6508 0.0235  0.0129  0.0126  410 ASP B CG  
6169 O OD1 . ASP B 408 ? 0.8297 0.7250 0.6549 0.0174  0.0096  0.0140  410 ASP B OD1 
6170 O OD2 . ASP B 408 ? 0.9757 0.8264 0.7558 0.0223  0.0157  0.0112  410 ASP B OD2 
6171 N N   . LEU B 409 ? 0.5668 0.4882 0.4273 0.0381  0.0097  0.0144  411 LEU B N   
6172 C CA  . LEU B 409 ? 0.5404 0.4597 0.4001 0.0435  0.0108  0.0141  411 LEU B CA  
6173 C C   . LEU B 409 ? 0.5562 0.4493 0.3907 0.0419  0.0132  0.0126  411 LEU B C   
6174 O O   . LEU B 409 ? 0.5498 0.4360 0.3791 0.0309  0.0118  0.0117  411 LEU B O   
6175 C CB  . LEU B 409 ? 0.5190 0.4539 0.3981 0.0374  0.0079  0.0142  411 LEU B CB  
6176 C CG  . LEU B 409 ? 0.4942 0.4292 0.3749 0.0413  0.0086  0.0137  411 LEU B CG  
6177 C CD1 . LEU B 409 ? 0.4796 0.4285 0.3706 0.0507  0.0093  0.0149  411 LEU B CD1 
6178 C CD2 . LEU B 409 ? 0.4858 0.4295 0.3791 0.0331  0.0061  0.0134  411 LEU B CD2 
6179 N N   . THR B 410 ? 0.5877 0.4666 0.4056 0.0525  0.0168  0.0126  412 THR B N   
6180 C CA  . THR B 410 ? 0.6460 0.4942 0.4341 0.0522  0.0199  0.0113  412 THR B CA  
6181 C C   . THR B 410 ? 0.6574 0.4990 0.4408 0.0560  0.0209  0.0111  412 THR B C   
6182 O O   . THR B 410 ? 0.6831 0.5000 0.4438 0.0524  0.0227  0.0099  412 THR B O   
6183 C CB  . THR B 410 ? 0.6765 0.5090 0.4445 0.0634  0.0241  0.0117  412 THR B CB  
6184 O OG1 . THR B 410 ? 0.6805 0.5272 0.4576 0.0778  0.0256  0.0137  412 THR B OG1 
6185 C CG2 . THR B 410 ? 0.6642 0.5011 0.4344 0.0599  0.0234  0.0118  412 THR B CG2 
6186 N N   . ASN B 411 ? 0.6517 0.5139 0.4542 0.0628  0.0201  0.0124  413 ASN B N   
6187 C CA  . ASN B 411 ? 0.6704 0.5288 0.4691 0.0687  0.0215  0.0127  413 ASN B CA  
6188 C C   . ASN B 411 ? 0.6100 0.4961 0.4360 0.0686  0.0187  0.0135  413 ASN B C   
6189 O O   . ASN B 411 ? 0.5789 0.4860 0.4230 0.0699  0.0171  0.0145  413 ASN B O   
6190 C CB  . ASN B 411 ? 0.7361 0.5825 0.5168 0.0844  0.0260  0.0142  413 ASN B CB  
6191 C CG  . ASN B 411 ? 0.8195 0.6404 0.5770 0.0869  0.0287  0.0137  413 ASN B CG  
6192 O OD1 . ASN B 411 ? 0.9418 0.7342 0.6740 0.0827  0.0307  0.0123  413 ASN B OD1 
6193 N ND2 . ASN B 411 ? 0.7915 0.6213 0.5558 0.0929  0.0289  0.0149  413 ASN B ND2 
6194 N N   . LEU B 412 ? 0.5853 0.4699 0.4124 0.0664  0.0182  0.0129  414 LEU B N   
6195 C CA  . LEU B 412 ? 0.5379 0.4450 0.3870 0.0666  0.0161  0.0135  414 LEU B CA  
6196 C C   . LEU B 412 ? 0.5437 0.4434 0.3840 0.0724  0.0179  0.0138  414 LEU B C   
6197 O O   . LEU B 412 ? 0.5328 0.4136 0.3585 0.0677  0.0185  0.0126  414 LEU B O   
6198 C CB  . LEU B 412 ? 0.5031 0.4198 0.3676 0.0541  0.0126  0.0122  414 LEU B CB  
6199 C CG  . LEU B 412 ? 0.4607 0.3977 0.3460 0.0534  0.0108  0.0123  414 LEU B CG  
6200 C CD1 . LEU B 412 ? 0.4393 0.3956 0.3391 0.0586  0.0103  0.0138  414 LEU B CD1 
6201 C CD2 . LEU B 412 ? 0.4429 0.3860 0.3393 0.0425  0.0082  0.0113  414 LEU B CD2 
6202 N N   . THR B 413 ? 0.5445 0.4593 0.3926 0.0821  0.0188  0.0157  415 THR B N   
6203 C CA  . THR B 413 ? 0.5715 0.4830 0.4127 0.0893  0.0206  0.0168  415 THR B CA  
6204 C C   . THR B 413 ? 0.5325 0.4699 0.3952 0.0892  0.0186  0.0176  415 THR B C   
6205 O O   . THR B 413 ? 0.4877 0.4458 0.3660 0.0893  0.0172  0.0185  415 THR B O   
6206 C CB  . THR B 413 ? 0.6131 0.5153 0.4360 0.1043  0.0247  0.0193  415 THR B CB  
6207 O OG1 . THR B 413 ? 0.6016 0.5296 0.4398 0.1103  0.0243  0.0215  415 THR B OG1 
6208 C CG2 . THR B 413 ? 0.6411 0.5158 0.4402 0.1052  0.0272  0.0185  415 THR B CG2 
6209 N N   . ALA B 414 ? 0.5419 0.4770 0.4035 0.0884  0.0186  0.0172  416 ALA B N   
6210 C CA  . ALA B 414 ? 0.5298 0.4863 0.4074 0.0891  0.0173  0.0181  416 ALA B CA  
6211 C C   . ALA B 414 ? 0.5523 0.5032 0.4171 0.0992  0.0200  0.0201  416 ALA B C   
6212 O O   . ALA B 414 ? 0.5793 0.5083 0.4279 0.0988  0.0213  0.0193  416 ALA B O   
6213 C CB  . ALA B 414 ? 0.5066 0.4665 0.3966 0.0773  0.0146  0.0155  416 ALA B CB  
6214 N N   . THR B 415 ? 0.5508 0.5209 0.4210 0.1080  0.0209  0.0232  417 THR B N   
6215 C CA  . THR B 415 ? 0.5618 0.5292 0.4199 0.1192  0.0236  0.0260  417 THR B CA  
6216 C C   . THR B 415 ? 0.5261 0.5202 0.4007 0.1183  0.0220  0.0274  417 THR B C   
6217 O O   . THR B 415 ? 0.4681 0.4840 0.3600 0.1128  0.0197  0.0273  417 THR B O   
6218 C CB  . THR B 415 ? 0.6086 0.5697 0.4499 0.1342  0.0275  0.0293  417 THR B CB  
6219 O OG1 . THR B 415 ? 0.6209 0.6068 0.4760 0.1359  0.0266  0.0311  417 THR B OG1 
6220 C CG2 . THR B 415 ? 0.6307 0.5600 0.4509 0.1346  0.0295  0.0276  417 THR B CG2 
6221 N N   . SER B 416 ? 0.5306 0.5209 0.3986 0.1222  0.0231  0.0284  418 SER B N   
6222 C CA  . SER B 416 ? 0.5375 0.5520 0.4169 0.1233  0.0222  0.0305  418 SER B CA  
6223 C C   . SER B 416 ? 0.5652 0.5732 0.4285 0.1363  0.0254  0.0341  418 SER B C   
6224 O O   . SER B 416 ? 0.5964 0.5762 0.4422 0.1382  0.0272  0.0329  418 SER B O   
6225 C CB  . SER B 416 ? 0.5104 0.5277 0.4026 0.1100  0.0193  0.0271  418 SER B CB  
6226 O OG  . SER B 416 ? 0.5136 0.5542 0.4160 0.1099  0.0185  0.0289  418 SER B OG  
6227 N N   . ALA B 417 ? 0.5810 0.6140 0.4488 0.1447  0.0262  0.0385  419 ALA B N   
6228 C CA  . ALA B 417 ? 0.6329 0.6670 0.4901 0.1558  0.0286  0.0423  419 ALA B CA  
6229 C C   . ALA B 417 ? 0.6424 0.6635 0.4999 0.1467  0.0271  0.0391  419 ALA B C   
6230 O O   . ALA B 417 ? 0.6772 0.6759 0.5166 0.1532  0.0295  0.0398  419 ALA B O   
6231 C CB  . ALA B 417 ? 0.6217 0.6927 0.4900 0.1613  0.0284  0.0472  419 ALA B CB  
6232 N N   . THR B 418 ? 0.6373 0.6690 0.5128 0.1319  0.0235  0.0355  420 THR B N   
6233 C CA  . THR B 418 ? 0.6390 0.6703 0.5203 0.1230  0.0218  0.0332  420 THR B CA  
6234 C C   . THR B 418 ? 0.6198 0.6260 0.4980 0.1124  0.0206  0.0282  420 THR B C   
6235 O O   . THR B 418 ? 0.6080 0.6149 0.4923 0.1044  0.0190  0.0260  420 THR B O   
6236 C CB  . THR B 418 ? 0.6397 0.6983 0.5416 0.1130  0.0189  0.0322  420 THR B CB  
6237 O OG1 . THR B 418 ? 0.6556 0.7164 0.5677 0.1045  0.0170  0.0295  420 THR B OG1 
6238 C CG2 . THR B 418 ? 0.6613 0.7491 0.5674 0.1202  0.0194  0.0373  420 THR B CG2 
6239 N N   . ALA B 419 ? 0.6332 0.6212 0.5042 0.1109  0.0210  0.0263  421 ALA B N   
6240 C CA  . ALA B 419 ? 0.6063 0.5784 0.4789 0.0984  0.0191  0.0218  421 ALA B CA  
6241 C C   . ALA B 419 ? 0.6247 0.5733 0.4820 0.0994  0.0205  0.0210  421 ALA B C   
6242 O O   . ALA B 419 ? 0.6563 0.6010 0.5029 0.1101  0.0229  0.0237  421 ALA B O   
6243 C CB  . ALA B 419 ? 0.5680 0.5574 0.4615 0.0878  0.0162  0.0193  421 ALA B CB  
6244 N N   . SER B 420 ? 0.5976 0.5327 0.4540 0.0884  0.0190  0.0177  422 SER B N   
6245 C CA  . SER B 420 ? 0.6117 0.5221 0.4509 0.0865  0.0200  0.0166  422 SER B CA  
6246 C C   . SER B 420 ? 0.5809 0.4940 0.4315 0.0737  0.0173  0.0136  422 SER B C   
6247 O O   . SER B 420 ? 0.5872 0.5068 0.4485 0.0649  0.0153  0.0117  422 SER B O   
6248 C CB  . SER B 420 ? 0.6369 0.5237 0.4554 0.0868  0.0217  0.0167  422 SER B CB  
6249 O OG  . SER B 420 ? 0.6924 0.5540 0.4913 0.0846  0.0230  0.0158  422 SER B OG  
6250 N N   . PHE B 421 ? 0.5759 0.4844 0.4239 0.0735  0.0175  0.0134  423 PHE B N   
6251 C CA  . PHE B 421 ? 0.5304 0.4439 0.3895 0.0628  0.0150  0.0113  423 PHE B CA  
6252 C C   . PHE B 421 ? 0.5541 0.4449 0.3951 0.0574  0.0156  0.0104  423 PHE B C   
6253 O O   . PHE B 421 ? 0.6025 0.4756 0.4241 0.0641  0.0182  0.0114  423 PHE B O   
6254 C CB  . PHE B 421 ? 0.4805 0.4101 0.3529 0.0658  0.0144  0.0121  423 PHE B CB  
6255 C CG  . PHE B 421 ? 0.4430 0.3954 0.3319 0.0694  0.0137  0.0131  423 PHE B CG  
6256 C CD1 . PHE B 421 ? 0.4562 0.4144 0.3407 0.0801  0.0156  0.0158  423 PHE B CD1 
6257 C CD2 . PHE B 421 ? 0.4165 0.3841 0.3236 0.0620  0.0114  0.0117  423 PHE B CD2 
6258 C CE1 . PHE B 421 ? 0.4530 0.4338 0.3520 0.0816  0.0148  0.0169  423 PHE B CE1 
6259 C CE2 . PHE B 421 ? 0.4056 0.3921 0.3254 0.0636  0.0109  0.0124  423 PHE B CE2 
6260 C CZ  . PHE B 421 ? 0.4252 0.4191 0.3412 0.0725  0.0124  0.0150  423 PHE B CZ  
6261 N N   . GLU B 422 ? 0.5656 0.4582 0.4125 0.0458  0.0134  0.0087  424 GLU B N   
6262 C CA  . GLU B 422 ? 0.6010 0.4794 0.4356 0.0386  0.0133  0.0080  424 GLU B CA  
6263 C C   . GLU B 422 ? 0.5587 0.4513 0.4075 0.0390  0.0121  0.0082  424 GLU B C   
6264 O O   . GLU B 422 ? 0.5113 0.4249 0.3810 0.0402  0.0107  0.0084  424 GLU B O   
6265 C CB  . GLU B 422 ? 0.6540 0.5301 0.4872 0.0254  0.0114  0.0067  424 GLU B CB  
6266 C CG  . GLU B 422 ? 0.7511 0.6075 0.5643 0.0231  0.0127  0.0064  424 GLU B CG  
6267 C CD  . GLU B 422 ? 0.8594 0.6856 0.6425 0.0260  0.0156  0.0068  424 GLU B CD  
6268 O OE1 . GLU B 422 ? 0.9350 0.7545 0.7115 0.0276  0.0164  0.0070  424 GLU B OE1 
6269 O OE2 . GLU B 422 ? 0.9105 0.7180 0.6749 0.0270  0.0173  0.0070  424 GLU B OE2 
6270 N N   . THR B 423 ? 0.5757 0.4558 0.4120 0.0378  0.0129  0.0083  425 THR B N   
6271 C CA  . THR B 423 ? 0.5406 0.4324 0.3886 0.0365  0.0116  0.0086  425 THR B CA  
6272 C C   . THR B 423 ? 0.5701 0.4486 0.4049 0.0268  0.0111  0.0079  425 THR B C   
6273 O O   . THR B 423 ? 0.6224 0.4774 0.4333 0.0254  0.0130  0.0075  425 THR B O   
6274 C CB  . THR B 423 ? 0.5449 0.4385 0.3918 0.0483  0.0135  0.0099  425 THR B CB  
6275 O OG1 . THR B 423 ? 0.5659 0.4346 0.3868 0.0530  0.0165  0.0102  425 THR B OG1 
6276 C CG2 . THR B 423 ? 0.5428 0.4517 0.4015 0.0571  0.0139  0.0111  425 THR B CG2 
6277 N N   . ASP B 424 ? 0.5551 0.4482 0.4041 0.0203  0.0088  0.0080  426 ASP B N   
6278 C CA  . ASP B 424 ? 0.5689 0.4544 0.4080 0.0109  0.0081  0.0079  426 ASP B CA  
6279 C C   . ASP B 424 ? 0.5178 0.4166 0.3701 0.0134  0.0072  0.0088  426 ASP B C   
6280 O O   . ASP B 424 ? 0.4866 0.4061 0.3603 0.0132  0.0054  0.0094  426 ASP B O   
6281 C CB  . ASP B 424 ? 0.5875 0.4802 0.4302 -0.0018 0.0058  0.0079  426 ASP B CB  
6282 C CG  . ASP B 424 ? 0.6354 0.5231 0.4677 -0.0127 0.0048  0.0082  426 ASP B CG  
6283 O OD1 . ASP B 424 ? 0.6810 0.5628 0.5079 -0.0101 0.0056  0.0084  426 ASP B OD1 
6284 O OD2 . ASP B 424 ? 0.7051 0.5956 0.5342 -0.0240 0.0033  0.0085  426 ASP B OD2 
6285 N N   . VAL B 425 ? 0.5341 0.4198 0.3725 0.0162  0.0088  0.0088  427 VAL B N   
6286 C CA  . VAL B 425 ? 0.4890 0.3857 0.3380 0.0203  0.0084  0.0097  427 VAL B CA  
6287 C C   . VAL B 425 ? 0.4679 0.3785 0.3289 0.0100  0.0055  0.0104  427 VAL B C   
6288 O O   . VAL B 425 ? 0.4463 0.3747 0.3256 0.0122  0.0042  0.0114  427 VAL B O   
6289 C CB  . VAL B 425 ? 0.5082 0.3862 0.3370 0.0260  0.0112  0.0096  427 VAL B CB  
6290 C CG1 . VAL B 425 ? 0.5451 0.4000 0.3494 0.0168  0.0120  0.0086  427 VAL B CG1 
6291 C CG2 . VAL B 425 ? 0.4887 0.3797 0.3292 0.0301  0.0107  0.0106  427 VAL B CG2 
6292 N N   . ASN B 426 ? 0.4719 0.3758 0.3225 -0.0010 0.0047  0.0101  428 ASN B N   
6293 C CA  . ASN B 426 ? 0.4463 0.3644 0.3059 -0.0109 0.0021  0.0114  428 ASN B CA  
6294 C C   . ASN B 426 ? 0.4177 0.3594 0.3009 -0.0107 0.0002  0.0125  428 ASN B C   
6295 O O   . ASN B 426 ? 0.4223 0.3793 0.3180 -0.0129 -0.0013 0.0142  428 ASN B O   
6296 C CB  . ASN B 426 ? 0.4809 0.3867 0.3213 -0.0236 0.0018  0.0111  428 ASN B CB  
6297 C CG  . ASN B 426 ? 0.5346 0.4136 0.3489 -0.0234 0.0042  0.0098  428 ASN B CG  
6298 O OD1 . ASN B 426 ? 0.5812 0.4385 0.3741 -0.0254 0.0060  0.0085  428 ASN B OD1 
6299 N ND2 . ASN B 426 ? 0.5297 0.4088 0.3443 -0.0201 0.0046  0.0102  428 ASN B ND2 
6300 N N   . THR B 427 ? 0.3888 0.3327 0.2769 -0.0080 0.0005  0.0118  429 THR B N   
6301 C CA  . THR B 427 ? 0.3541 0.3182 0.2631 -0.0065 -0.0006 0.0127  429 THR B CA  
6302 C C   . THR B 427 ? 0.3287 0.2980 0.2497 0.0039  0.0001  0.0124  429 THR B C   
6303 O O   . THR B 427 ? 0.3051 0.2888 0.2422 0.0058  -0.0006 0.0131  429 THR B O   
6304 C CB  . THR B 427 ? 0.3609 0.3253 0.2676 -0.0110 -0.0008 0.0122  429 THR B CB  
6305 O OG1 . THR B 427 ? 0.3688 0.3173 0.2641 -0.0064 0.0008  0.0105  429 THR B OG1 
6306 C CG2 . THR B 427 ? 0.3817 0.3443 0.2769 -0.0231 -0.0019 0.0130  429 THR B CG2 
6307 N N   . GLY B 428 ? 0.3323 0.2902 0.2447 0.0104  0.0017  0.0115  430 GLY B N   
6308 C CA  . GLY B 428 ? 0.3155 0.2804 0.2381 0.0194  0.0024  0.0114  430 GLY B CA  
6309 C C   . GLY B 428 ? 0.3124 0.2814 0.2409 0.0216  0.0027  0.0107  430 GLY B C   
6310 O O   . GLY B 428 ? 0.2847 0.2632 0.2241 0.0266  0.0028  0.0107  430 GLY B O   
6311 N N   . ILE B 429 ? 0.3185 0.2809 0.2396 0.0171  0.0027  0.0099  431 ILE B N   
6312 C CA  . ILE B 429 ? 0.3181 0.2843 0.2444 0.0183  0.0029  0.0091  431 ILE B CA  
6313 C C   . ILE B 429 ? 0.3316 0.2856 0.2455 0.0240  0.0047  0.0085  431 ILE B C   
6314 O O   . ILE B 429 ? 0.3602 0.2980 0.2566 0.0230  0.0057  0.0084  431 ILE B O   
6315 C CB  . ILE B 429 ? 0.3126 0.2812 0.2389 0.0103  0.0019  0.0090  431 ILE B CB  
6316 C CG1 . ILE B 429 ? 0.2964 0.2792 0.2349 0.0066  0.0005  0.0104  431 ILE B CG1 
6317 C CG2 . ILE B 429 ? 0.3122 0.2843 0.2434 0.0121  0.0023  0.0080  431 ILE B CG2 
6318 C CD1 . ILE B 429 ? 0.3009 0.2896 0.2394 -0.0009 -0.0003 0.0110  431 ILE B CD1 
6319 N N   . ILE B 430 ? 0.3299 0.2919 0.2521 0.0301  0.0052  0.0085  432 ILE B N   
6320 C CA  . ILE B 430 ? 0.3492 0.3049 0.2632 0.0361  0.0068  0.0085  432 ILE B CA  
6321 C C   . ILE B 430 ? 0.3421 0.3015 0.2610 0.0325  0.0062  0.0075  432 ILE B C   
6322 O O   . ILE B 430 ? 0.3338 0.3069 0.2676 0.0316  0.0054  0.0072  432 ILE B O   
6323 C CB  . ILE B 430 ? 0.3418 0.3080 0.2627 0.0440  0.0074  0.0096  432 ILE B CB  
6324 C CG1 . ILE B 430 ? 0.3417 0.3053 0.2579 0.0473  0.0079  0.0106  432 ILE B CG1 
6325 C CG2 . ILE B 430 ? 0.3588 0.3233 0.2734 0.0510  0.0090  0.0102  432 ILE B CG2 
6326 C CD1 . ILE B 430 ? 0.3269 0.3067 0.2553 0.0510  0.0076  0.0117  432 ILE B CD1 
6327 N N   . THR B 431 ? 0.3613 0.3078 0.2670 0.0304  0.0069  0.0070  433 THR B N   
6328 C CA  . THR B 431 ? 0.3565 0.3064 0.2659 0.0270  0.0065  0.0061  433 THR B CA  
6329 C C   . THR B 431 ? 0.3593 0.3074 0.2649 0.0340  0.0079  0.0064  433 THR B C   
6330 O O   . THR B 431 ? 0.3736 0.3086 0.2643 0.0392  0.0095  0.0073  433 THR B O   
6331 C CB  . THR B 431 ? 0.3770 0.3164 0.2750 0.0186  0.0061  0.0056  433 THR B CB  
6332 O OG1 . THR B 431 ? 0.3853 0.3295 0.2870 0.0112  0.0047  0.0058  433 THR B OG1 
6333 C CG2 . THR B 431 ? 0.3758 0.3220 0.2800 0.0153  0.0056  0.0048  433 THR B CG2 
6334 N N   . LEU B 432 ? 0.3475 0.3082 0.2655 0.0341  0.0074  0.0059  434 LEU B N   
6335 C CA  . LEU B 432 ? 0.3611 0.3229 0.2770 0.0389  0.0083  0.0062  434 LEU B CA  
6336 C C   . LEU B 432 ? 0.3675 0.3316 0.2872 0.0330  0.0077  0.0048  434 LEU B C   
6337 O O   . LEU B 432 ? 0.3264 0.3023 0.2596 0.0292  0.0067  0.0037  434 LEU B O   
6338 C CB  . LEU B 432 ? 0.3459 0.3234 0.2735 0.0438  0.0084  0.0069  434 LEU B CB  
6339 C CG  . LEU B 432 ? 0.3543 0.3363 0.2805 0.0483  0.0092  0.0077  434 LEU B CG  
6340 C CD1 . LEU B 432 ? 0.3748 0.3429 0.2834 0.0555  0.0110  0.0095  434 LEU B CD1 
6341 C CD2 . LEU B 432 ? 0.3418 0.3417 0.2791 0.0511  0.0090  0.0086  434 LEU B CD2 
6342 N N   . LYS B 433 ? 0.4156 0.3677 0.3222 0.0327  0.0084  0.0049  435 LYS B N   
6343 C CA  . LYS B 433 ? 0.4384 0.3923 0.3467 0.0275  0.0079  0.0038  435 LYS B CA  
6344 C C   . LYS B 433 ? 0.4232 0.3834 0.3346 0.0330  0.0087  0.0042  435 LYS B C   
6345 O O   . LYS B 433 ? 0.4537 0.4056 0.3535 0.0393  0.0100  0.0057  435 LYS B O   
6346 C CB  . LYS B 433 ? 0.4905 0.4270 0.3810 0.0229  0.0083  0.0038  435 LYS B CB  
6347 C CG  . LYS B 433 ? 0.5204 0.4592 0.4119 0.0179  0.0078  0.0029  435 LYS B CG  
6348 C CD  . LYS B 433 ? 0.5770 0.4985 0.4497 0.0114  0.0080  0.0030  435 LYS B CD  
6349 C CE  . LYS B 433 ? 0.6370 0.5395 0.4906 0.0183  0.0099  0.0043  435 LYS B CE  
6350 N NZ  . LYS B 433 ? 0.6948 0.5779 0.5277 0.0114  0.0102  0.0043  435 LYS B NZ  
6351 N N   . VAL B 434 ? 0.3889 0.3635 0.3145 0.0310  0.0081  0.0030  436 VAL B N   
6352 C CA  . VAL B 434 ? 0.3805 0.3636 0.3099 0.0348  0.0086  0.0034  436 VAL B CA  
6353 C C   . VAL B 434 ? 0.3909 0.3715 0.3178 0.0307  0.0085  0.0023  436 VAL B C   
6354 O O   . VAL B 434 ? 0.3619 0.3473 0.2964 0.0244  0.0079  0.0005  436 VAL B O   
6355 C CB  . VAL B 434 ? 0.3573 0.3560 0.3015 0.0341  0.0081  0.0026  436 VAL B CB  
6356 C CG1 . VAL B 434 ? 0.3642 0.3723 0.3117 0.0353  0.0085  0.0027  436 VAL B CG1 
6357 C CG2 . VAL B 434 ? 0.3482 0.3506 0.2947 0.0378  0.0081  0.0039  436 VAL B CG2 
6358 N N   . VAL B 435 ? 0.4155 0.3883 0.3309 0.0344  0.0094  0.0036  437 VAL B N   
6359 C CA  . VAL B 435 ? 0.4239 0.3925 0.3346 0.0304  0.0094  0.0029  437 VAL B CA  
6360 C C   . VAL B 435 ? 0.4105 0.3930 0.3306 0.0317  0.0094  0.0026  437 VAL B C   
6361 O O   . VAL B 435 ? 0.4031 0.3908 0.3223 0.0382  0.0101  0.0045  437 VAL B O   
6362 C CB  . VAL B 435 ? 0.4503 0.3997 0.3408 0.0329  0.0104  0.0045  437 VAL B CB  
6363 C CG1 . VAL B 435 ? 0.4627 0.4078 0.3482 0.0274  0.0102  0.0037  437 VAL B CG1 
6364 C CG2 . VAL B 435 ? 0.4581 0.3928 0.3376 0.0305  0.0104  0.0046  437 VAL B CG2 
6365 N N   . ASN B 436 ? 0.4038 0.3940 0.3334 0.0257  0.0089  0.0004  438 ASN B N   
6366 C CA  . ASN B 436 ? 0.4153 0.4179 0.3530 0.0255  0.0091  -0.0003 438 ASN B CA  
6367 C C   . ASN B 436 ? 0.4425 0.4406 0.3722 0.0252  0.0094  0.0001  438 ASN B C   
6368 O O   . ASN B 436 ? 0.4661 0.4556 0.3898 0.0207  0.0092  -0.0005 438 ASN B O   
6369 C CB  . ASN B 436 ? 0.3926 0.4042 0.3428 0.0204  0.0089  -0.0029 438 ASN B CB  
6370 C CG  . ASN B 436 ? 0.3959 0.4150 0.3538 0.0219  0.0089  -0.0029 438 ASN B CG  
6371 O OD1 . ASN B 436 ? 0.4185 0.4468 0.3815 0.0213  0.0092  -0.0034 438 ASN B OD1 
6372 N N   . LYS B 437 ? 0.4830 0.4875 0.4117 0.0296  0.0098  0.0017  439 LYS B N   
6373 C CA  . LYS B 437 ? 0.4975 0.5013 0.4205 0.0299  0.0101  0.0025  439 LYS B CA  
6374 C C   . LYS B 437 ? 0.4525 0.4690 0.3864 0.0245  0.0099  0.0001  439 LYS B C   
6375 O O   . LYS B 437 ? 0.4016 0.4303 0.3443 0.0243  0.0099  -0.0002 439 LYS B O   
6376 C CB  . LYS B 437 ? 0.5603 0.5677 0.4771 0.0386  0.0109  0.0061  439 LYS B CB  
6377 C CG  . LYS B 437 ? 0.6251 0.6225 0.5312 0.0466  0.0118  0.0090  439 LYS B CG  
6378 C CD  . LYS B 437 ? 0.6786 0.6781 0.5754 0.0568  0.0131  0.0133  439 LYS B CD  
6379 C CE  . LYS B 437 ? 0.7168 0.7042 0.6004 0.0664  0.0146  0.0162  439 LYS B CE  
6380 N NZ  . LYS B 437 ? 0.7357 0.7310 0.6128 0.0781  0.0162  0.0211  439 LYS B NZ  
6381 N N   . GLN B 438 ? 0.4489 0.4620 0.3806 0.0200  0.0099  -0.0011 440 GLN B N   
6382 C CA  . GLN B 438 ? 0.4411 0.4642 0.3802 0.0154  0.0100  -0.0033 440 GLN B CA  
6383 C C   . GLN B 438 ? 0.4245 0.4579 0.3637 0.0186  0.0102  -0.0014 440 GLN B C   
6384 O O   . GLN B 438 ? 0.4243 0.4543 0.3546 0.0246  0.0103  0.0018  440 GLN B O   
6385 C CB  . GLN B 438 ? 0.4755 0.4927 0.4093 0.0113  0.0100  -0.0041 440 GLN B CB  
6386 C CG  . GLN B 438 ? 0.5045 0.5158 0.4386 0.0067  0.0097  -0.0056 440 GLN B CG  
6387 C CD  . GLN B 438 ? 0.5230 0.5326 0.4536 0.0013  0.0096  -0.0065 440 GLN B CD  
6388 O OE1 . GLN B 438 ? 0.5357 0.5521 0.4695 -0.0001 0.0100  -0.0076 440 GLN B OE1 
6389 N NE2 . GLN B 438 ? 0.5459 0.5468 0.4689 -0.0023 0.0091  -0.0060 440 GLN B NE2 
6390 N N   . GLY B 439 ? 0.4021 0.4470 0.3497 0.0148  0.0104  -0.0033 441 GLY B N   
6391 C CA  . GLY B 439 ? 0.4033 0.4602 0.3513 0.0146  0.0104  -0.0021 441 GLY B CA  
6392 C C   . GLY B 439 ? 0.4093 0.4631 0.3513 0.0142  0.0105  -0.0015 441 GLY B C   
6393 O O   . GLY B 439 ? 0.3945 0.4374 0.3331 0.0122  0.0105  -0.0029 441 GLY B O   
6394 N N   . ALA B 440 ? 0.4185 0.4829 0.3592 0.0154  0.0105  0.0005  442 ALA B N   
6395 C CA  . ALA B 440 ? 0.4237 0.4860 0.3576 0.0162  0.0105  0.0019  442 ALA B CA  
6396 C C   . ALA B 440 ? 0.4244 0.4914 0.3635 0.0080  0.0107  -0.0017 442 ALA B C   
6397 O O   . ALA B 440 ? 0.4061 0.4832 0.3521 0.0034  0.0109  -0.0037 442 ALA B O   
6398 C CB  . ALA B 440 ? 0.4294 0.5021 0.3590 0.0231  0.0105  0.0067  442 ALA B CB  
6399 N N   . LEU B 441 ? 0.4297 0.4882 0.3648 0.0056  0.0108  -0.0029 443 LEU B N   
6400 C CA  . LEU B 441 ? 0.4655 0.5287 0.4038 -0.0009 0.0112  -0.0058 443 LEU B CA  
6401 C C   . LEU B 441 ? 0.4488 0.5166 0.3811 0.0008  0.0109  -0.0028 443 LEU B C   
6402 O O   . LEU B 441 ? 0.4268 0.4849 0.3508 0.0025  0.0107  -0.0013 443 LEU B O   
6403 C CB  . LEU B 441 ? 0.5008 0.5547 0.4390 -0.0049 0.0115  -0.0086 443 LEU B CB  
6404 C CG  . LEU B 441 ? 0.5269 0.5817 0.4731 -0.0082 0.0124  -0.0123 443 LEU B CG  
6405 C CD1 . LEU B 441 ? 0.5299 0.5786 0.4758 -0.0109 0.0127  -0.0139 443 LEU B CD1 
6406 C CD2 . LEU B 441 ? 0.5294 0.5929 0.4805 -0.0123 0.0136  -0.0150 443 LEU B CD2 
6407 N N   . LEU B 442 ? 0.4456 0.5277 0.3805 0.0008  0.0108  -0.0014 444 LEU B N   
6408 C CA  . LEU B 442 ? 0.4815 0.5707 0.4104 0.0051  0.0105  0.0029  444 LEU B CA  
6409 C C   . LEU B 442 ? 0.4845 0.5752 0.4122 -0.0002 0.0106  0.0013  444 LEU B C   
6410 O O   . LEU B 442 ? 0.4732 0.5679 0.4067 -0.0079 0.0110  -0.0028 444 LEU B O   
6411 C CB  . LEU B 442 ? 0.4762 0.5839 0.4086 0.0069  0.0102  0.0057  444 LEU B CB  
6412 C CG  . LEU B 442 ? 0.4720 0.5798 0.4031 0.0149  0.0102  0.0090  444 LEU B CG  
6413 C CD1 . LEU B 442 ? 0.4624 0.5923 0.3979 0.0147  0.0098  0.0117  444 LEU B CD1 
6414 C CD2 . LEU B 442 ? 0.4864 0.5823 0.4061 0.0251  0.0106  0.0133  444 LEU B CD2 
6415 N N   . PRO B 443 ? 0.5168 0.6026 0.4355 0.0039  0.0104  0.0046  445 PRO B N   
6416 C CA  . PRO B 443 ? 0.5326 0.6212 0.4495 -0.0008 0.0104  0.0038  445 PRO B CA  
6417 C C   . PRO B 443 ? 0.5386 0.6474 0.4597 -0.0030 0.0102  0.0051  445 PRO B C   
6418 O O   . PRO B 443 ? 0.5224 0.6428 0.4440 0.0018  0.0100  0.0088  445 PRO B O   
6419 C CB  . PRO B 443 ? 0.5555 0.6314 0.4593 0.0055  0.0103  0.0080  445 PRO B CB  
6420 C CG  . PRO B 443 ? 0.5681 0.6420 0.4667 0.0159  0.0106  0.0125  445 PRO B CG  
6421 C CD  . PRO B 443 ? 0.5395 0.6156 0.4475 0.0138  0.0105  0.0096  445 PRO B CD  
6422 N N   . ASN B 444 ? 0.5657 0.6790 0.4890 -0.0105 0.0104  0.0022  446 ASN B N   
6423 C CA  . ASN B 444 ? 0.5894 0.7213 0.5154 -0.0150 0.0102  0.0029  446 ASN B CA  
6424 C C   . ASN B 444 ? 0.6081 0.7412 0.5281 -0.0145 0.0099  0.0052  446 ASN B C   
6425 O O   . ASN B 444 ? 0.6168 0.7394 0.5352 -0.0185 0.0103  0.0021  446 ASN B O   
6426 C CB  . ASN B 444 ? 0.5997 0.7343 0.5319 -0.0253 0.0111  -0.0030 446 ASN B CB  
6427 C CG  . ASN B 444 ? 0.5961 0.7250 0.5330 -0.0260 0.0116  -0.0059 446 ASN B CG  
6428 O OD1 . ASN B 444 ? 0.5954 0.7327 0.5340 -0.0244 0.0112  -0.0038 446 ASN B OD1 
6429 N ND2 . ASN B 444 ? 0.5835 0.6993 0.5222 -0.0283 0.0127  -0.0103 446 ASN B ND2 
6430 N N   . THR B 445 ? 0.6199 0.7667 0.5364 -0.0097 0.0094  0.0108  447 THR B N   
6431 C CA  . THR B 445 ? 0.6172 0.7659 0.5271 -0.0084 0.0092  0.0138  447 THR B CA  
6432 C C   . THR B 445 ? 0.6122 0.7655 0.5265 -0.0200 0.0094  0.0087  447 THR B C   
6433 O O   . THR B 445 ? 0.5874 0.7328 0.4975 -0.0220 0.0094  0.0077  447 THR B O   
6434 C CB  . THR B 445 ? 0.6228 0.7890 0.5290 -0.0004 0.0088  0.0212  447 THR B CB  
6435 O OG1 . THR B 445 ? 0.6046 0.7644 0.5037 0.0125  0.0092  0.0266  447 THR B OG1 
6436 C CG2 . THR B 445 ? 0.6547 0.8243 0.5548 -0.0002 0.0086  0.0239  447 THR B CG2 
# 
